data_9C0U
# 
_entry.id   9C0U 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9C0U         pdb_00009c0u 10.2210/pdb9c0u/pdb 
WWPDB D_1000284514 ?            ?                   
# 
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 2025-05-07 ? 
2 'Structure model' 1 1 2025-05-14 ? 
3 'Structure model' 1 2 2025-05-28 ? 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Derived calculations' 
2 3 'Structure model' 'Database references'  
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' pdbx_struct_assembly     
2 2 'Structure model' pdbx_struct_assembly_gen 
3 2 'Structure model' pdbx_struct_oper_list    
4 3 'Structure model' citation                 
5 3 'Structure model' citation_author          
# 
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' '_pdbx_struct_assembly.oligomeric_count'   
2  2 'Structure model' '_pdbx_struct_assembly.oligomeric_details' 
3  3 'Structure model' '_citation.country'                        
4  3 'Structure model' '_citation.journal_abbrev'                 
5  3 'Structure model' '_citation.journal_id_ASTM'                
6  3 'Structure model' '_citation.journal_id_CSD'                 
7  3 'Structure model' '_citation.journal_id_ISSN'                
8  3 'Structure model' '_citation.journal_volume'                 
9  3 'Structure model' '_citation.page_first'                     
10 3 'Structure model' '_citation.page_last'                      
11 3 'Structure model' '_citation.pdbx_database_id_DOI'           
12 3 'Structure model' '_citation.pdbx_database_id_PubMed'        
13 3 'Structure model' '_citation.title'                          
14 3 'Structure model' '_citation.year'                           
# 
_database_PDB_caveat.id     1 
_database_PDB_caveat.text   'NAG S 2 HAS WRONG CHIRALITY AT ATOM C1' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9C0U 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              wilson@scripps.edu 
_pdbx_contact_author.name_first         YEN 
_pdbx_contact_author.name_last          NGUYEN 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6469-2419 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Nguyen, T.K.Y.' 1 0000-0001-6424-4168 
'Zhu, X.'        2 0000-0002-6021-3740 
'Wilson, I.A.'   3 0000-0002-6469-2419 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Proc.Natl.Acad.Sci.USA 
_citation.journal_id_ASTM           PNASA6 
_citation.journal_id_CSD            0040 
_citation.journal_id_ISSN           1091-6490 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            122 
_citation.language                  ? 
_citation.page_first                e2416628122 
_citation.page_last                 e2416628122 
_citation.title                     
'Structural characterization of influenza group 1 chimeric hemagglutinins as broad vaccine immunogens.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1073/pnas.2416628122 
_citation.pdbx_database_id_PubMed   39937865 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Nguyen, Y.T.K.'  1  0000-0001-6424-4168 
primary 'Zhu, X.'         2  0000-0002-6021-3740 
primary 'Han, J.'         3  0000-0002-3402-2609 
primary 'Rodriguez, A.J.' 4  0009-0009-6510-7558 
primary 'Sun, W.'         5  0000-0002-2435-5047 
primary 'Yu, W.'          6  0000-0002-4025-2646 
primary 'Palese, P.'      7  0000-0002-0337-5823 
primary 'Krammer, F.'     8  0000-0003-4121-776X 
primary 'Ward, A.B.'      9  0000-0001-7153-3769 
primary 'Wilson, I.A.'    10 0000-0002-6469-2419 
# 
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 Hemagglutinin 56980.824 2 ? ? ? ? 
2 polymer     man 'Antibody 31.b.09 Fab heavy chain' 23915.730 1 ? ? ? ? 
3 polymer     man 'Antibody 31.b.09 Fab light chain' 24070.746 1 ? ? ? ? 
4 branched    man 
'beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 586.542   1 ? 
? ? ? 
5 branched    man '2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 424.401   1 ? ? ? ? 
6 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   1 ? ? ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;GDTLCIGYHANNSTDTVDTVLEKNVTVTHSVNLLEDKHNGKLCDLDGVKPLILRDCSVAGWLLGNPMCDEFINVPEWSYI
VEKANPVNDLCYPGDFNDYEELKHLLSRINHFEKIQIIPKSSWSSHEASLGVSSACPYQGKSSFFRNVVWLIKKNSTYPT
IKRSYNNTNQEDLLVLWGIHHPNDAAEQTKLYQNPTTYISVGTSTLNQRLVPRIATRSKVNGQSGRMEFFWTILKPNDAI
NFESNGNFIAPEYAYKIVKKGDSTIMKSELEYGNCNTTCQTPKGAINTSLPFQNIHPITIGKCPKYVKSTKLRLATGLRN
VPSIQSRGLFGAIAGFIEGGWTGMVDGWYGYHHQNEQGSGYAADLKSTQNAIDGITNKVNSVIEKMNTQFTAVGKEFNHL
EKRIENLNKKVDDGFLDIWTYNAELLVLLENERTLDYHDSNVKNLYEKVRSQLKNNAKEIGNGCFEFYHKCDNTCMESVK
NGTYDYPKYSEEAKLNREEIDSGR
;
;GDTLCIGYHANNSTDTVDTVLEKNVTVTHSVNLLEDKHNGKLCDLDGVKPLILRDCSVAGWLLGNPMCDEFINVPEWSYI
VEKANPVNDLCYPGDFNDYEELKHLLSRINHFEKIQIIPKSSWSSHEASLGVSSACPYQGKSSFFRNVVWLIKKNSTYPT
IKRSYNNTNQEDLLVLWGIHHPNDAAEQTKLYQNPTTYISVGTSTLNQRLVPRIATRSKVNGQSGRMEFFWTILKPNDAI
NFESNGNFIAPEYAYKIVKKGDSTIMKSELEYGNCNTTCQTPKGAINTSLPFQNIHPITIGKCPKYVKSTKLRLATGLRN
VPSIQSRGLFGAIAGFIEGGWTGMVDGWYGYHHQNEQGSGYAADLKSTQNAIDGITNKVNSVIEKMNTQFTAVGKEFNHL
EKRIENLNKKVDDGFLDIWTYNAELLVLLENERTLDYHDSNVKNLYEKVRSQLKNNAKEIGNGCFEFYHKCDNTCMESVK
NGTYDYPKYSEEAKLNREEIDSGR
;
B,A ? 
2 'polypeptide(L)' no no 
;QVQLVQSGAEVKKPGASVKVSCKASGYSFSSYGISWVRQAPGQGLEWMGWISAYNGNTNYAQKLQGRVTMTTDTSTSTAY
MELRSLRSDDTAVFYCARDRPHILTGFDFDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVT
VSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKS
;
;QVQLVQSGAEVKKPGASVKVSCKASGYSFSSYGISWVRQAPGQGLEWMGWISAYNGNTNYAQKLQGRVTMTTDTSTSTAY
MELRSLRSDDTAVFYCARDRPHILTGFDFDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVT
VSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKS
;
H   ? 
3 'polypeptide(L)' no no 
;DVVMTQSPVSLPVTLGQPASISCRSSQGLVYIDGNTYLNWFQQRPGQSPRRLIYNVFTRDSGVPDRFSGSGSGTDFTLKI
TTVEAEDVGVYYCMQGTHWPYTFGQGTKLEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQ
SGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGE
;
;DVVMTQSPVSLPVTLGQPASISCRSSQGLVYIDGNTYLNWFQQRPGQSPRRLIYNVFTRDSGVPDRFSGSGSGTDFTLKI
TTVEAEDVGVYYCMQGTHWPYTFGQGTKLEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQ
SGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGE
;
L   ? 
# 
_pdbx_entity_nonpoly.entity_id   6 
_pdbx_entity_nonpoly.name        2-acetamido-2-deoxy-beta-D-glucopyranose 
_pdbx_entity_nonpoly.comp_id     NAG 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   ASP n 
1 3   THR n 
1 4   LEU n 
1 5   CYS n 
1 6   ILE n 
1 7   GLY n 
1 8   TYR n 
1 9   HIS n 
1 10  ALA n 
1 11  ASN n 
1 12  ASN n 
1 13  SER n 
1 14  THR n 
1 15  ASP n 
1 16  THR n 
1 17  VAL n 
1 18  ASP n 
1 19  THR n 
1 20  VAL n 
1 21  LEU n 
1 22  GLU n 
1 23  LYS n 
1 24  ASN n 
1 25  VAL n 
1 26  THR n 
1 27  VAL n 
1 28  THR n 
1 29  HIS n 
1 30  SER n 
1 31  VAL n 
1 32  ASN n 
1 33  LEU n 
1 34  LEU n 
1 35  GLU n 
1 36  ASP n 
1 37  LYS n 
1 38  HIS n 
1 39  ASN n 
1 40  GLY n 
1 41  LYS n 
1 42  LEU n 
1 43  CYS n 
1 44  ASP n 
1 45  LEU n 
1 46  ASP n 
1 47  GLY n 
1 48  VAL n 
1 49  LYS n 
1 50  PRO n 
1 51  LEU n 
1 52  ILE n 
1 53  LEU n 
1 54  ARG n 
1 55  ASP n 
1 56  CYS n 
1 57  SER n 
1 58  VAL n 
1 59  ALA n 
1 60  GLY n 
1 61  TRP n 
1 62  LEU n 
1 63  LEU n 
1 64  GLY n 
1 65  ASN n 
1 66  PRO n 
1 67  MET n 
1 68  CYS n 
1 69  ASP n 
1 70  GLU n 
1 71  PHE n 
1 72  ILE n 
1 73  ASN n 
1 74  VAL n 
1 75  PRO n 
1 76  GLU n 
1 77  TRP n 
1 78  SER n 
1 79  TYR n 
1 80  ILE n 
1 81  VAL n 
1 82  GLU n 
1 83  LYS n 
1 84  ALA n 
1 85  ASN n 
1 86  PRO n 
1 87  VAL n 
1 88  ASN n 
1 89  ASP n 
1 90  LEU n 
1 91  CYS n 
1 92  TYR n 
1 93  PRO n 
1 94  GLY n 
1 95  ASP n 
1 96  PHE n 
1 97  ASN n 
1 98  ASP n 
1 99  TYR n 
1 100 GLU n 
1 101 GLU n 
1 102 LEU n 
1 103 LYS n 
1 104 HIS n 
1 105 LEU n 
1 106 LEU n 
1 107 SER n 
1 108 ARG n 
1 109 ILE n 
1 110 ASN n 
1 111 HIS n 
1 112 PHE n 
1 113 GLU n 
1 114 LYS n 
1 115 ILE n 
1 116 GLN n 
1 117 ILE n 
1 118 ILE n 
1 119 PRO n 
1 120 LYS n 
1 121 SER n 
1 122 SER n 
1 123 TRP n 
1 124 SER n 
1 125 SER n 
1 126 HIS n 
1 127 GLU n 
1 128 ALA n 
1 129 SER n 
1 130 LEU n 
1 131 GLY n 
1 132 VAL n 
1 133 SER n 
1 134 SER n 
1 135 ALA n 
1 136 CYS n 
1 137 PRO n 
1 138 TYR n 
1 139 GLN n 
1 140 GLY n 
1 141 LYS n 
1 142 SER n 
1 143 SER n 
1 144 PHE n 
1 145 PHE n 
1 146 ARG n 
1 147 ASN n 
1 148 VAL n 
1 149 VAL n 
1 150 TRP n 
1 151 LEU n 
1 152 ILE n 
1 153 LYS n 
1 154 LYS n 
1 155 ASN n 
1 156 SER n 
1 157 THR n 
1 158 TYR n 
1 159 PRO n 
1 160 THR n 
1 161 ILE n 
1 162 LYS n 
1 163 ARG n 
1 164 SER n 
1 165 TYR n 
1 166 ASN n 
1 167 ASN n 
1 168 THR n 
1 169 ASN n 
1 170 GLN n 
1 171 GLU n 
1 172 ASP n 
1 173 LEU n 
1 174 LEU n 
1 175 VAL n 
1 176 LEU n 
1 177 TRP n 
1 178 GLY n 
1 179 ILE n 
1 180 HIS n 
1 181 HIS n 
1 182 PRO n 
1 183 ASN n 
1 184 ASP n 
1 185 ALA n 
1 186 ALA n 
1 187 GLU n 
1 188 GLN n 
1 189 THR n 
1 190 LYS n 
1 191 LEU n 
1 192 TYR n 
1 193 GLN n 
1 194 ASN n 
1 195 PRO n 
1 196 THR n 
1 197 THR n 
1 198 TYR n 
1 199 ILE n 
1 200 SER n 
1 201 VAL n 
1 202 GLY n 
1 203 THR n 
1 204 SER n 
1 205 THR n 
1 206 LEU n 
1 207 ASN n 
1 208 GLN n 
1 209 ARG n 
1 210 LEU n 
1 211 VAL n 
1 212 PRO n 
1 213 ARG n 
1 214 ILE n 
1 215 ALA n 
1 216 THR n 
1 217 ARG n 
1 218 SER n 
1 219 LYS n 
1 220 VAL n 
1 221 ASN n 
1 222 GLY n 
1 223 GLN n 
1 224 SER n 
1 225 GLY n 
1 226 ARG n 
1 227 MET n 
1 228 GLU n 
1 229 PHE n 
1 230 PHE n 
1 231 TRP n 
1 232 THR n 
1 233 ILE n 
1 234 LEU n 
1 235 LYS n 
1 236 PRO n 
1 237 ASN n 
1 238 ASP n 
1 239 ALA n 
1 240 ILE n 
1 241 ASN n 
1 242 PHE n 
1 243 GLU n 
1 244 SER n 
1 245 ASN n 
1 246 GLY n 
1 247 ASN n 
1 248 PHE n 
1 249 ILE n 
1 250 ALA n 
1 251 PRO n 
1 252 GLU n 
1 253 TYR n 
1 254 ALA n 
1 255 TYR n 
1 256 LYS n 
1 257 ILE n 
1 258 VAL n 
1 259 LYS n 
1 260 LYS n 
1 261 GLY n 
1 262 ASP n 
1 263 SER n 
1 264 THR n 
1 265 ILE n 
1 266 MET n 
1 267 LYS n 
1 268 SER n 
1 269 GLU n 
1 270 LEU n 
1 271 GLU n 
1 272 TYR n 
1 273 GLY n 
1 274 ASN n 
1 275 CYS n 
1 276 ASN n 
1 277 THR n 
1 278 THR n 
1 279 CYS n 
1 280 GLN n 
1 281 THR n 
1 282 PRO n 
1 283 LYS n 
1 284 GLY n 
1 285 ALA n 
1 286 ILE n 
1 287 ASN n 
1 288 THR n 
1 289 SER n 
1 290 LEU n 
1 291 PRO n 
1 292 PHE n 
1 293 GLN n 
1 294 ASN n 
1 295 ILE n 
1 296 HIS n 
1 297 PRO n 
1 298 ILE n 
1 299 THR n 
1 300 ILE n 
1 301 GLY n 
1 302 LYS n 
1 303 CYS n 
1 304 PRO n 
1 305 LYS n 
1 306 TYR n 
1 307 VAL n 
1 308 LYS n 
1 309 SER n 
1 310 THR n 
1 311 LYS n 
1 312 LEU n 
1 313 ARG n 
1 314 LEU n 
1 315 ALA n 
1 316 THR n 
1 317 GLY n 
1 318 LEU n 
1 319 ARG n 
1 320 ASN n 
1 321 VAL n 
1 322 PRO n 
1 323 SER n 
1 324 ILE n 
1 325 GLN n 
1 326 SER n 
1 327 ARG n 
1 328 GLY n 
1 329 LEU n 
1 330 PHE n 
1 331 GLY n 
1 332 ALA n 
1 333 ILE n 
1 334 ALA n 
1 335 GLY n 
1 336 PHE n 
1 337 ILE n 
1 338 GLU n 
1 339 GLY n 
1 340 GLY n 
1 341 TRP n 
1 342 THR n 
1 343 GLY n 
1 344 MET n 
1 345 VAL n 
1 346 ASP n 
1 347 GLY n 
1 348 TRP n 
1 349 TYR n 
1 350 GLY n 
1 351 TYR n 
1 352 HIS n 
1 353 HIS n 
1 354 GLN n 
1 355 ASN n 
1 356 GLU n 
1 357 GLN n 
1 358 GLY n 
1 359 SER n 
1 360 GLY n 
1 361 TYR n 
1 362 ALA n 
1 363 ALA n 
1 364 ASP n 
1 365 LEU n 
1 366 LYS n 
1 367 SER n 
1 368 THR n 
1 369 GLN n 
1 370 ASN n 
1 371 ALA n 
1 372 ILE n 
1 373 ASP n 
1 374 GLY n 
1 375 ILE n 
1 376 THR n 
1 377 ASN n 
1 378 LYS n 
1 379 VAL n 
1 380 ASN n 
1 381 SER n 
1 382 VAL n 
1 383 ILE n 
1 384 GLU n 
1 385 LYS n 
1 386 MET n 
1 387 ASN n 
1 388 THR n 
1 389 GLN n 
1 390 PHE n 
1 391 THR n 
1 392 ALA n 
1 393 VAL n 
1 394 GLY n 
1 395 LYS n 
1 396 GLU n 
1 397 PHE n 
1 398 ASN n 
1 399 HIS n 
1 400 LEU n 
1 401 GLU n 
1 402 LYS n 
1 403 ARG n 
1 404 ILE n 
1 405 GLU n 
1 406 ASN n 
1 407 LEU n 
1 408 ASN n 
1 409 LYS n 
1 410 LYS n 
1 411 VAL n 
1 412 ASP n 
1 413 ASP n 
1 414 GLY n 
1 415 PHE n 
1 416 LEU n 
1 417 ASP n 
1 418 ILE n 
1 419 TRP n 
1 420 THR n 
1 421 TYR n 
1 422 ASN n 
1 423 ALA n 
1 424 GLU n 
1 425 LEU n 
1 426 LEU n 
1 427 VAL n 
1 428 LEU n 
1 429 LEU n 
1 430 GLU n 
1 431 ASN n 
1 432 GLU n 
1 433 ARG n 
1 434 THR n 
1 435 LEU n 
1 436 ASP n 
1 437 TYR n 
1 438 HIS n 
1 439 ASP n 
1 440 SER n 
1 441 ASN n 
1 442 VAL n 
1 443 LYS n 
1 444 ASN n 
1 445 LEU n 
1 446 TYR n 
1 447 GLU n 
1 448 LYS n 
1 449 VAL n 
1 450 ARG n 
1 451 SER n 
1 452 GLN n 
1 453 LEU n 
1 454 LYS n 
1 455 ASN n 
1 456 ASN n 
1 457 ALA n 
1 458 LYS n 
1 459 GLU n 
1 460 ILE n 
1 461 GLY n 
1 462 ASN n 
1 463 GLY n 
1 464 CYS n 
1 465 PHE n 
1 466 GLU n 
1 467 PHE n 
1 468 TYR n 
1 469 HIS n 
1 470 LYS n 
1 471 CYS n 
1 472 ASP n 
1 473 ASN n 
1 474 THR n 
1 475 CYS n 
1 476 MET n 
1 477 GLU n 
1 478 SER n 
1 479 VAL n 
1 480 LYS n 
1 481 ASN n 
1 482 GLY n 
1 483 THR n 
1 484 TYR n 
1 485 ASP n 
1 486 TYR n 
1 487 PRO n 
1 488 LYS n 
1 489 TYR n 
1 490 SER n 
1 491 GLU n 
1 492 GLU n 
1 493 ALA n 
1 494 LYS n 
1 495 LEU n 
1 496 ASN n 
1 497 ARG n 
1 498 GLU n 
1 499 GLU n 
1 500 ILE n 
1 501 ASP n 
1 502 SER n 
1 503 GLY n 
1 504 ARG n 
2 1   GLN n 
2 2   VAL n 
2 3   GLN n 
2 4   LEU n 
2 5   VAL n 
2 6   GLN n 
2 7   SER n 
2 8   GLY n 
2 9   ALA n 
2 10  GLU n 
2 11  VAL n 
2 12  LYS n 
2 13  LYS n 
2 14  PRO n 
2 15  GLY n 
2 16  ALA n 
2 17  SER n 
2 18  VAL n 
2 19  LYS n 
2 20  VAL n 
2 21  SER n 
2 22  CYS n 
2 23  LYS n 
2 24  ALA n 
2 25  SER n 
2 26  GLY n 
2 27  TYR n 
2 28  SER n 
2 29  PHE n 
2 30  SER n 
2 31  SER n 
2 32  TYR n 
2 33  GLY n 
2 34  ILE n 
2 35  SER n 
2 36  TRP n 
2 37  VAL n 
2 38  ARG n 
2 39  GLN n 
2 40  ALA n 
2 41  PRO n 
2 42  GLY n 
2 43  GLN n 
2 44  GLY n 
2 45  LEU n 
2 46  GLU n 
2 47  TRP n 
2 48  MET n 
2 49  GLY n 
2 50  TRP n 
2 51  ILE n 
2 52  SER n 
2 53  ALA n 
2 54  TYR n 
2 55  ASN n 
2 56  GLY n 
2 57  ASN n 
2 58  THR n 
2 59  ASN n 
2 60  TYR n 
2 61  ALA n 
2 62  GLN n 
2 63  LYS n 
2 64  LEU n 
2 65  GLN n 
2 66  GLY n 
2 67  ARG n 
2 68  VAL n 
2 69  THR n 
2 70  MET n 
2 71  THR n 
2 72  THR n 
2 73  ASP n 
2 74  THR n 
2 75  SER n 
2 76  THR n 
2 77  SER n 
2 78  THR n 
2 79  ALA n 
2 80  TYR n 
2 81  MET n 
2 82  GLU n 
2 83  LEU n 
2 84  ARG n 
2 85  SER n 
2 86  LEU n 
2 87  ARG n 
2 88  SER n 
2 89  ASP n 
2 90  ASP n 
2 91  THR n 
2 92  ALA n 
2 93  VAL n 
2 94  PHE n 
2 95  TYR n 
2 96  CYS n 
2 97  ALA n 
2 98  ARG n 
2 99  ASP n 
2 100 ARG n 
2 101 PRO n 
2 102 HIS n 
2 103 ILE n 
2 104 LEU n 
2 105 THR n 
2 106 GLY n 
2 107 PHE n 
2 108 ASP n 
2 109 PHE n 
2 110 ASP n 
2 111 TYR n 
2 112 TRP n 
2 113 GLY n 
2 114 GLN n 
2 115 GLY n 
2 116 THR n 
2 117 LEU n 
2 118 VAL n 
2 119 THR n 
2 120 VAL n 
2 121 SER n 
2 122 SER n 
2 123 ALA n 
2 124 SER n 
2 125 THR n 
2 126 LYS n 
2 127 GLY n 
2 128 PRO n 
2 129 SER n 
2 130 VAL n 
2 131 PHE n 
2 132 PRO n 
2 133 LEU n 
2 134 ALA n 
2 135 PRO n 
2 136 SER n 
2 137 SER n 
2 138 LYS n 
2 139 SER n 
2 140 THR n 
2 141 SER n 
2 142 GLY n 
2 143 GLY n 
2 144 THR n 
2 145 ALA n 
2 146 ALA n 
2 147 LEU n 
2 148 GLY n 
2 149 CYS n 
2 150 LEU n 
2 151 VAL n 
2 152 LYS n 
2 153 ASP n 
2 154 TYR n 
2 155 PHE n 
2 156 PRO n 
2 157 GLU n 
2 158 PRO n 
2 159 VAL n 
2 160 THR n 
2 161 VAL n 
2 162 SER n 
2 163 TRP n 
2 164 ASN n 
2 165 SER n 
2 166 GLY n 
2 167 ALA n 
2 168 LEU n 
2 169 THR n 
2 170 SER n 
2 171 GLY n 
2 172 VAL n 
2 173 HIS n 
2 174 THR n 
2 175 PHE n 
2 176 PRO n 
2 177 ALA n 
2 178 VAL n 
2 179 LEU n 
2 180 GLN n 
2 181 SER n 
2 182 SER n 
2 183 GLY n 
2 184 LEU n 
2 185 TYR n 
2 186 SER n 
2 187 LEU n 
2 188 SER n 
2 189 SER n 
2 190 VAL n 
2 191 VAL n 
2 192 THR n 
2 193 VAL n 
2 194 PRO n 
2 195 SER n 
2 196 SER n 
2 197 SER n 
2 198 LEU n 
2 199 GLY n 
2 200 THR n 
2 201 GLN n 
2 202 THR n 
2 203 TYR n 
2 204 ILE n 
2 205 CYS n 
2 206 ASN n 
2 207 VAL n 
2 208 ASN n 
2 209 HIS n 
2 210 LYS n 
2 211 PRO n 
2 212 SER n 
2 213 ASN n 
2 214 THR n 
2 215 LYS n 
2 216 VAL n 
2 217 ASP n 
2 218 LYS n 
2 219 ARG n 
2 220 VAL n 
2 221 GLU n 
2 222 PRO n 
2 223 LYS n 
2 224 SER n 
3 1   ASP n 
3 2   VAL n 
3 3   VAL n 
3 4   MET n 
3 5   THR n 
3 6   GLN n 
3 7   SER n 
3 8   PRO n 
3 9   VAL n 
3 10  SER n 
3 11  LEU n 
3 12  PRO n 
3 13  VAL n 
3 14  THR n 
3 15  LEU n 
3 16  GLY n 
3 17  GLN n 
3 18  PRO n 
3 19  ALA n 
3 20  SER n 
3 21  ILE n 
3 22  SER n 
3 23  CYS n 
3 24  ARG n 
3 25  SER n 
3 26  SER n 
3 27  GLN n 
3 28  GLY n 
3 29  LEU n 
3 30  VAL n 
3 31  TYR n 
3 32  ILE n 
3 33  ASP n 
3 34  GLY n 
3 35  ASN n 
3 36  THR n 
3 37  TYR n 
3 38  LEU n 
3 39  ASN n 
3 40  TRP n 
3 41  PHE n 
3 42  GLN n 
3 43  GLN n 
3 44  ARG n 
3 45  PRO n 
3 46  GLY n 
3 47  GLN n 
3 48  SER n 
3 49  PRO n 
3 50  ARG n 
3 51  ARG n 
3 52  LEU n 
3 53  ILE n 
3 54  TYR n 
3 55  ASN n 
3 56  VAL n 
3 57  PHE n 
3 58  THR n 
3 59  ARG n 
3 60  ASP n 
3 61  SER n 
3 62  GLY n 
3 63  VAL n 
3 64  PRO n 
3 65  ASP n 
3 66  ARG n 
3 67  PHE n 
3 68  SER n 
3 69  GLY n 
3 70  SER n 
3 71  GLY n 
3 72  SER n 
3 73  GLY n 
3 74  THR n 
3 75  ASP n 
3 76  PHE n 
3 77  THR n 
3 78  LEU n 
3 79  LYS n 
3 80  ILE n 
3 81  THR n 
3 82  THR n 
3 83  VAL n 
3 84  GLU n 
3 85  ALA n 
3 86  GLU n 
3 87  ASP n 
3 88  VAL n 
3 89  GLY n 
3 90  VAL n 
3 91  TYR n 
3 92  TYR n 
3 93  CYS n 
3 94  MET n 
3 95  GLN n 
3 96  GLY n 
3 97  THR n 
3 98  HIS n 
3 99  TRP n 
3 100 PRO n 
3 101 TYR n 
3 102 THR n 
3 103 PHE n 
3 104 GLY n 
3 105 GLN n 
3 106 GLY n 
3 107 THR n 
3 108 LYS n 
3 109 LEU n 
3 110 GLU n 
3 111 ILE n 
3 112 LYS n 
3 113 ARG n 
3 114 THR n 
3 115 VAL n 
3 116 ALA n 
3 117 ALA n 
3 118 PRO n 
3 119 SER n 
3 120 VAL n 
3 121 PHE n 
3 122 ILE n 
3 123 PHE n 
3 124 PRO n 
3 125 PRO n 
3 126 SER n 
3 127 ASP n 
3 128 GLU n 
3 129 GLN n 
3 130 LEU n 
3 131 LYS n 
3 132 SER n 
3 133 GLY n 
3 134 THR n 
3 135 ALA n 
3 136 SER n 
3 137 VAL n 
3 138 VAL n 
3 139 CYS n 
3 140 LEU n 
3 141 LEU n 
3 142 ASN n 
3 143 ASN n 
3 144 PHE n 
3 145 TYR n 
3 146 PRO n 
3 147 ARG n 
3 148 GLU n 
3 149 ALA n 
3 150 LYS n 
3 151 VAL n 
3 152 GLN n 
3 153 TRP n 
3 154 LYS n 
3 155 VAL n 
3 156 ASP n 
3 157 ASN n 
3 158 ALA n 
3 159 LEU n 
3 160 GLN n 
3 161 SER n 
3 162 GLY n 
3 163 ASN n 
3 164 SER n 
3 165 GLN n 
3 166 GLU n 
3 167 SER n 
3 168 VAL n 
3 169 THR n 
3 170 GLU n 
3 171 GLN n 
3 172 ASP n 
3 173 SER n 
3 174 LYS n 
3 175 ASP n 
3 176 SER n 
3 177 THR n 
3 178 TYR n 
3 179 SER n 
3 180 LEU n 
3 181 SER n 
3 182 SER n 
3 183 THR n 
3 184 LEU n 
3 185 THR n 
3 186 LEU n 
3 187 SER n 
3 188 LYS n 
3 189 ALA n 
3 190 ASP n 
3 191 TYR n 
3 192 GLU n 
3 193 LYS n 
3 194 HIS n 
3 195 LYS n 
3 196 VAL n 
3 197 TYR n 
3 198 ALA n 
3 199 CYS n 
3 200 GLU n 
3 201 VAL n 
3 202 THR n 
3 203 HIS n 
3 204 GLN n 
3 205 GLY n 
3 206 LEU n 
3 207 SER n 
3 208 SER n 
3 209 PRO n 
3 210 VAL n 
3 211 THR n 
3 212 LYS n 
3 213 SER n 
3 214 PHE n 
3 215 ASN n 
3 216 ARG n 
3 217 GLY n 
3 218 GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 504 ?     ? HA ? ? ? ? ? ? 'Influenza A virus' 11320 ? ? ? ? ? ? ? 'cabbage looper'  
'Trichoplusia ni'    7111  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 224 human ? ?  ? ? ? ? ? ? 'Homo sapiens'      9606  ? ? ? ? ? ? ? 'Chinese hamster' 
'Cricetulus griseus' 10029 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 218 human ? ?  ? ? ? ? ? ? 'Homo sapiens'      9606  ? ? ? ? ? ? ? 'Chinese hamster' 
'Cricetulus griseus' 10029 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_pdbx_entity_branch.entity_id 
_pdbx_entity_branch.type 
4 oligosaccharide 
5 oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 4 DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH                                          'Glycam Condensed Sequence' GMML       1.0   
2 4 'WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1' WURCS                       PDB2Glycan 1.1.0 
3 4 '[][D-1-deoxy-GlcpNAc]{[(4+1)][a-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}'           LINUCS                      PDB-CARE   ?     
4 5 DGlcpNAcb1-4DGlcpNAcb1-ROH                                                   'Glycam Condensed Sequence' GMML       1.0   
5 5 'WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1'                        WURCS                       PDB2Glycan 1.1.0 
6 5 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}'                              LINUCS                      PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 4 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2 4 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
3 5 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking'          y ALANINE                                  ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking'          y ARGININE                                 ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking'          y ASPARAGINE                               ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking'          y 'ASPARTIC ACID'                          ? 'C4 H7 N O4'     133.103 
BMA 'D-saccharide, beta linking' . beta-D-mannopyranose                     'beta-D-mannose; D-mannose; mannose' 'C6 H12 O6'      
180.156 
CYS 'L-peptide linking'          y CYSTEINE                                 ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking'          y GLUTAMINE                                ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'          y 'GLUTAMIC ACID'                          ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'            y GLYCINE                                  ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking'          y HISTIDINE                                ? 'C6 H10 N3 O2 1' 156.162 
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 
NAG 'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
PHE 'L-peptide linking'          y PHENYLALANINE                            ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking'          y PROLINE                                  ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking'          y SERINE                                   ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking'          y THREONINE                                ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking'          y TRYPTOPHAN                               ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking'          y TYROSINE                                 ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking'          y VALINE                                   ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
BMA 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpb                         
BMA 'COMMON NAME'                         GMML     1.0 b-D-mannopyranose              
BMA 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Manp                       
BMA 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -326 ?   ?   ?   B . n 
A 1 2   ASP 2   -325 ?   ?   ?   B . n 
A 1 3   THR 3   -324 ?   ?   ?   B . n 
A 1 4   LEU 4   -323 ?   ?   ?   B . n 
A 1 5   CYS 5   -322 ?   ?   ?   B . n 
A 1 6   ILE 6   -321 ?   ?   ?   B . n 
A 1 7   GLY 7   -320 ?   ?   ?   B . n 
A 1 8   TYR 8   -319 ?   ?   ?   B . n 
A 1 9   HIS 9   -318 ?   ?   ?   B . n 
A 1 10  ALA 10  -317 ?   ?   ?   B . n 
A 1 11  ASN 11  -316 ?   ?   ?   B . n 
A 1 12  ASN 12  -315 ?   ?   ?   B . n 
A 1 13  SER 13  -314 ?   ?   ?   B . n 
A 1 14  THR 14  -313 ?   ?   ?   B . n 
A 1 15  ASP 15  -312 ?   ?   ?   B . n 
A 1 16  THR 16  -311 ?   ?   ?   B . n 
A 1 17  VAL 17  -310 ?   ?   ?   B . n 
A 1 18  ASP 18  -309 ?   ?   ?   B . n 
A 1 19  THR 19  -308 ?   ?   ?   B . n 
A 1 20  VAL 20  -307 ?   ?   ?   B . n 
A 1 21  LEU 21  -306 ?   ?   ?   B . n 
A 1 22  GLU 22  -305 ?   ?   ?   B . n 
A 1 23  LYS 23  -304 ?   ?   ?   B . n 
A 1 24  ASN 24  -303 ?   ?   ?   B . n 
A 1 25  VAL 25  -302 ?   ?   ?   B . n 
A 1 26  THR 26  -301 ?   ?   ?   B . n 
A 1 27  VAL 27  -300 ?   ?   ?   B . n 
A 1 28  THR 28  -299 ?   ?   ?   B . n 
A 1 29  HIS 29  -298 ?   ?   ?   B . n 
A 1 30  SER 30  -297 ?   ?   ?   B . n 
A 1 31  VAL 31  -296 ?   ?   ?   B . n 
A 1 32  ASN 32  -295 ?   ?   ?   B . n 
A 1 33  LEU 33  -294 ?   ?   ?   B . n 
A 1 34  LEU 34  -293 ?   ?   ?   B . n 
A 1 35  GLU 35  -292 ?   ?   ?   B . n 
A 1 36  ASP 36  -291 ?   ?   ?   B . n 
A 1 37  LYS 37  -290 ?   ?   ?   B . n 
A 1 38  HIS 38  -289 ?   ?   ?   B . n 
A 1 39  ASN 39  -288 ?   ?   ?   B . n 
A 1 40  GLY 40  -287 ?   ?   ?   B . n 
A 1 41  LYS 41  -286 ?   ?   ?   B . n 
A 1 42  LEU 42  -285 ?   ?   ?   B . n 
A 1 43  CYS 43  -284 ?   ?   ?   B . n 
A 1 44  ASP 44  -283 ?   ?   ?   B . n 
A 1 45  LEU 45  -282 ?   ?   ?   B . n 
A 1 46  ASP 46  -281 ?   ?   ?   B . n 
A 1 47  GLY 47  -280 ?   ?   ?   B . n 
A 1 48  VAL 48  -279 ?   ?   ?   B . n 
A 1 49  LYS 49  -278 ?   ?   ?   B . n 
A 1 50  PRO 50  -277 ?   ?   ?   B . n 
A 1 51  LEU 51  -276 ?   ?   ?   B . n 
A 1 52  ILE 52  -275 ?   ?   ?   B . n 
A 1 53  LEU 53  -274 ?   ?   ?   B . n 
A 1 54  ARG 54  -273 ?   ?   ?   B . n 
A 1 55  ASP 55  -272 ?   ?   ?   B . n 
A 1 56  CYS 56  -271 ?   ?   ?   B . n 
A 1 57  SER 57  -270 ?   ?   ?   B . n 
A 1 58  VAL 58  -269 ?   ?   ?   B . n 
A 1 59  ALA 59  -268 ?   ?   ?   B . n 
A 1 60  GLY 60  -267 ?   ?   ?   B . n 
A 1 61  TRP 61  -266 ?   ?   ?   B . n 
A 1 62  LEU 62  -265 ?   ?   ?   B . n 
A 1 63  LEU 63  -264 ?   ?   ?   B . n 
A 1 64  GLY 64  -263 ?   ?   ?   B . n 
A 1 65  ASN 65  -262 ?   ?   ?   B . n 
A 1 66  PRO 66  -261 ?   ?   ?   B . n 
A 1 67  MET 67  -260 ?   ?   ?   B . n 
A 1 68  CYS 68  -259 ?   ?   ?   B . n 
A 1 69  ASP 69  -258 ?   ?   ?   B . n 
A 1 70  GLU 70  -257 ?   ?   ?   B . n 
A 1 71  PHE 71  -256 ?   ?   ?   B . n 
A 1 72  ILE 72  -255 ?   ?   ?   B . n 
A 1 73  ASN 73  -254 ?   ?   ?   B . n 
A 1 74  VAL 74  -253 ?   ?   ?   B . n 
A 1 75  PRO 75  -252 ?   ?   ?   B . n 
A 1 76  GLU 76  -251 ?   ?   ?   B . n 
A 1 77  TRP 77  -250 ?   ?   ?   B . n 
A 1 78  SER 78  -249 ?   ?   ?   B . n 
A 1 79  TYR 79  -248 ?   ?   ?   B . n 
A 1 80  ILE 80  -247 ?   ?   ?   B . n 
A 1 81  VAL 81  -246 ?   ?   ?   B . n 
A 1 82  GLU 82  -245 ?   ?   ?   B . n 
A 1 83  LYS 83  -244 ?   ?   ?   B . n 
A 1 84  ALA 84  -243 ?   ?   ?   B . n 
A 1 85  ASN 85  -242 ?   ?   ?   B . n 
A 1 86  PRO 86  -241 ?   ?   ?   B . n 
A 1 87  VAL 87  -240 ?   ?   ?   B . n 
A 1 88  ASN 88  -239 ?   ?   ?   B . n 
A 1 89  ASP 89  -238 ?   ?   ?   B . n 
A 1 90  LEU 90  -237 ?   ?   ?   B . n 
A 1 91  CYS 91  -236 ?   ?   ?   B . n 
A 1 92  TYR 92  -235 ?   ?   ?   B . n 
A 1 93  PRO 93  -234 ?   ?   ?   B . n 
A 1 94  GLY 94  -233 ?   ?   ?   B . n 
A 1 95  ASP 95  -232 ?   ?   ?   B . n 
A 1 96  PHE 96  -231 ?   ?   ?   B . n 
A 1 97  ASN 97  -230 ?   ?   ?   B . n 
A 1 98  ASP 98  -229 ?   ?   ?   B . n 
A 1 99  TYR 99  -228 ?   ?   ?   B . n 
A 1 100 GLU 100 -227 ?   ?   ?   B . n 
A 1 101 GLU 101 -226 ?   ?   ?   B . n 
A 1 102 LEU 102 -225 ?   ?   ?   B . n 
A 1 103 LYS 103 -224 ?   ?   ?   B . n 
A 1 104 HIS 104 -223 ?   ?   ?   B . n 
A 1 105 LEU 105 -222 ?   ?   ?   B . n 
A 1 106 LEU 106 -221 ?   ?   ?   B . n 
A 1 107 SER 107 -220 ?   ?   ?   B . n 
A 1 108 ARG 108 -219 ?   ?   ?   B . n 
A 1 109 ILE 109 -218 ?   ?   ?   B . n 
A 1 110 ASN 110 -217 ?   ?   ?   B . n 
A 1 111 HIS 111 -216 ?   ?   ?   B . n 
A 1 112 PHE 112 -215 ?   ?   ?   B . n 
A 1 113 GLU 113 -214 ?   ?   ?   B . n 
A 1 114 LYS 114 -213 ?   ?   ?   B . n 
A 1 115 ILE 115 -212 ?   ?   ?   B . n 
A 1 116 GLN 116 -211 ?   ?   ?   B . n 
A 1 117 ILE 117 -210 ?   ?   ?   B . n 
A 1 118 ILE 118 -209 ?   ?   ?   B . n 
A 1 119 PRO 119 -208 ?   ?   ?   B . n 
A 1 120 LYS 120 -207 ?   ?   ?   B . n 
A 1 121 SER 121 -206 ?   ?   ?   B . n 
A 1 122 SER 122 -205 ?   ?   ?   B . n 
A 1 123 TRP 123 -204 ?   ?   ?   B . n 
A 1 124 SER 124 -203 ?   ?   ?   B . n 
A 1 125 SER 125 -202 ?   ?   ?   B . n 
A 1 126 HIS 126 -201 ?   ?   ?   B . n 
A 1 127 GLU 127 -200 ?   ?   ?   B . n 
A 1 128 ALA 128 -199 ?   ?   ?   B . n 
A 1 129 SER 129 -198 ?   ?   ?   B . n 
A 1 130 LEU 130 -197 ?   ?   ?   B . n 
A 1 131 GLY 131 -196 ?   ?   ?   B . n 
A 1 132 VAL 132 -195 ?   ?   ?   B . n 
A 1 133 SER 133 -194 ?   ?   ?   B . n 
A 1 134 SER 134 -193 ?   ?   ?   B . n 
A 1 135 ALA 135 -192 ?   ?   ?   B . n 
A 1 136 CYS 136 -191 ?   ?   ?   B . n 
A 1 137 PRO 137 -190 ?   ?   ?   B . n 
A 1 138 TYR 138 -189 ?   ?   ?   B . n 
A 1 139 GLN 139 -188 ?   ?   ?   B . n 
A 1 140 GLY 140 -187 ?   ?   ?   B . n 
A 1 141 LYS 141 -186 ?   ?   ?   B . n 
A 1 142 SER 142 -185 ?   ?   ?   B . n 
A 1 143 SER 143 -184 ?   ?   ?   B . n 
A 1 144 PHE 144 -183 ?   ?   ?   B . n 
A 1 145 PHE 145 -182 ?   ?   ?   B . n 
A 1 146 ARG 146 -181 ?   ?   ?   B . n 
A 1 147 ASN 147 -180 ?   ?   ?   B . n 
A 1 148 VAL 148 -179 ?   ?   ?   B . n 
A 1 149 VAL 149 -178 ?   ?   ?   B . n 
A 1 150 TRP 150 -177 ?   ?   ?   B . n 
A 1 151 LEU 151 -176 ?   ?   ?   B . n 
A 1 152 ILE 152 -175 ?   ?   ?   B . n 
A 1 153 LYS 153 -174 ?   ?   ?   B . n 
A 1 154 LYS 154 -173 ?   ?   ?   B . n 
A 1 155 ASN 155 -172 ?   ?   ?   B . n 
A 1 156 SER 156 -171 ?   ?   ?   B . n 
A 1 157 THR 157 -170 ?   ?   ?   B . n 
A 1 158 TYR 158 -169 ?   ?   ?   B . n 
A 1 159 PRO 159 -168 ?   ?   ?   B . n 
A 1 160 THR 160 -167 ?   ?   ?   B . n 
A 1 161 ILE 161 -166 ?   ?   ?   B . n 
A 1 162 LYS 162 -165 ?   ?   ?   B . n 
A 1 163 ARG 163 -164 ?   ?   ?   B . n 
A 1 164 SER 164 -163 ?   ?   ?   B . n 
A 1 165 TYR 165 -162 ?   ?   ?   B . n 
A 1 166 ASN 166 -161 ?   ?   ?   B . n 
A 1 167 ASN 167 -160 ?   ?   ?   B . n 
A 1 168 THR 168 -159 ?   ?   ?   B . n 
A 1 169 ASN 169 -158 ?   ?   ?   B . n 
A 1 170 GLN 170 -157 ?   ?   ?   B . n 
A 1 171 GLU 171 -156 ?   ?   ?   B . n 
A 1 172 ASP 172 -155 ?   ?   ?   B . n 
A 1 173 LEU 173 -154 ?   ?   ?   B . n 
A 1 174 LEU 174 -153 ?   ?   ?   B . n 
A 1 175 VAL 175 -152 ?   ?   ?   B . n 
A 1 176 LEU 176 -151 ?   ?   ?   B . n 
A 1 177 TRP 177 -150 ?   ?   ?   B . n 
A 1 178 GLY 178 -149 ?   ?   ?   B . n 
A 1 179 ILE 179 -148 ?   ?   ?   B . n 
A 1 180 HIS 180 -147 ?   ?   ?   B . n 
A 1 181 HIS 181 -146 ?   ?   ?   B . n 
A 1 182 PRO 182 -145 ?   ?   ?   B . n 
A 1 183 ASN 183 -144 ?   ?   ?   B . n 
A 1 184 ASP 184 -143 ?   ?   ?   B . n 
A 1 185 ALA 185 -142 ?   ?   ?   B . n 
A 1 186 ALA 186 -141 ?   ?   ?   B . n 
A 1 187 GLU 187 -140 ?   ?   ?   B . n 
A 1 188 GLN 188 -139 ?   ?   ?   B . n 
A 1 189 THR 189 -138 ?   ?   ?   B . n 
A 1 190 LYS 190 -137 ?   ?   ?   B . n 
A 1 191 LEU 191 -136 ?   ?   ?   B . n 
A 1 192 TYR 192 -135 ?   ?   ?   B . n 
A 1 193 GLN 193 -134 ?   ?   ?   B . n 
A 1 194 ASN 194 -133 ?   ?   ?   B . n 
A 1 195 PRO 195 -132 ?   ?   ?   B . n 
A 1 196 THR 196 -131 ?   ?   ?   B . n 
A 1 197 THR 197 -130 ?   ?   ?   B . n 
A 1 198 TYR 198 -129 ?   ?   ?   B . n 
A 1 199 ILE 199 -128 ?   ?   ?   B . n 
A 1 200 SER 200 -127 ?   ?   ?   B . n 
A 1 201 VAL 201 -126 ?   ?   ?   B . n 
A 1 202 GLY 202 -125 ?   ?   ?   B . n 
A 1 203 THR 203 -124 ?   ?   ?   B . n 
A 1 204 SER 204 -123 ?   ?   ?   B . n 
A 1 205 THR 205 -122 ?   ?   ?   B . n 
A 1 206 LEU 206 -121 ?   ?   ?   B . n 
A 1 207 ASN 207 -120 ?   ?   ?   B . n 
A 1 208 GLN 208 -119 ?   ?   ?   B . n 
A 1 209 ARG 209 -118 ?   ?   ?   B . n 
A 1 210 LEU 210 -117 ?   ?   ?   B . n 
A 1 211 VAL 211 -116 ?   ?   ?   B . n 
A 1 212 PRO 212 -115 ?   ?   ?   B . n 
A 1 213 ARG 213 -114 ?   ?   ?   B . n 
A 1 214 ILE 214 -113 ?   ?   ?   B . n 
A 1 215 ALA 215 -112 ?   ?   ?   B . n 
A 1 216 THR 216 -111 ?   ?   ?   B . n 
A 1 217 ARG 217 -110 ?   ?   ?   B . n 
A 1 218 SER 218 -109 ?   ?   ?   B . n 
A 1 219 LYS 219 -108 ?   ?   ?   B . n 
A 1 220 VAL 220 -107 ?   ?   ?   B . n 
A 1 221 ASN 221 -106 ?   ?   ?   B . n 
A 1 222 GLY 222 -105 ?   ?   ?   B . n 
A 1 223 GLN 223 -104 ?   ?   ?   B . n 
A 1 224 SER 224 -103 ?   ?   ?   B . n 
A 1 225 GLY 225 -102 ?   ?   ?   B . n 
A 1 226 ARG 226 -101 ?   ?   ?   B . n 
A 1 227 MET 227 -100 ?   ?   ?   B . n 
A 1 228 GLU 228 -99  ?   ?   ?   B . n 
A 1 229 PHE 229 -98  ?   ?   ?   B . n 
A 1 230 PHE 230 -97  ?   ?   ?   B . n 
A 1 231 TRP 231 -96  ?   ?   ?   B . n 
A 1 232 THR 232 -95  ?   ?   ?   B . n 
A 1 233 ILE 233 -94  ?   ?   ?   B . n 
A 1 234 LEU 234 -93  ?   ?   ?   B . n 
A 1 235 LYS 235 -92  ?   ?   ?   B . n 
A 1 236 PRO 236 -91  ?   ?   ?   B . n 
A 1 237 ASN 237 -90  ?   ?   ?   B . n 
A 1 238 ASP 238 -89  ?   ?   ?   B . n 
A 1 239 ALA 239 -88  ?   ?   ?   B . n 
A 1 240 ILE 240 -87  ?   ?   ?   B . n 
A 1 241 ASN 241 -86  ?   ?   ?   B . n 
A 1 242 PHE 242 -85  ?   ?   ?   B . n 
A 1 243 GLU 243 -84  ?   ?   ?   B . n 
A 1 244 SER 244 -83  ?   ?   ?   B . n 
A 1 245 ASN 245 -82  ?   ?   ?   B . n 
A 1 246 GLY 246 -81  ?   ?   ?   B . n 
A 1 247 ASN 247 -80  ?   ?   ?   B . n 
A 1 248 PHE 248 -79  ?   ?   ?   B . n 
A 1 249 ILE 249 -78  ?   ?   ?   B . n 
A 1 250 ALA 250 -77  ?   ?   ?   B . n 
A 1 251 PRO 251 -76  ?   ?   ?   B . n 
A 1 252 GLU 252 -75  ?   ?   ?   B . n 
A 1 253 TYR 253 -74  ?   ?   ?   B . n 
A 1 254 ALA 254 -73  ?   ?   ?   B . n 
A 1 255 TYR 255 -72  ?   ?   ?   B . n 
A 1 256 LYS 256 -71  ?   ?   ?   B . n 
A 1 257 ILE 257 -70  ?   ?   ?   B . n 
A 1 258 VAL 258 -69  ?   ?   ?   B . n 
A 1 259 LYS 259 -68  ?   ?   ?   B . n 
A 1 260 LYS 260 -67  ?   ?   ?   B . n 
A 1 261 GLY 261 -66  ?   ?   ?   B . n 
A 1 262 ASP 262 -65  ?   ?   ?   B . n 
A 1 263 SER 263 -64  ?   ?   ?   B . n 
A 1 264 THR 264 -63  ?   ?   ?   B . n 
A 1 265 ILE 265 -62  ?   ?   ?   B . n 
A 1 266 MET 266 -61  ?   ?   ?   B . n 
A 1 267 LYS 267 -60  ?   ?   ?   B . n 
A 1 268 SER 268 -59  ?   ?   ?   B . n 
A 1 269 GLU 269 -58  ?   ?   ?   B . n 
A 1 270 LEU 270 -57  ?   ?   ?   B . n 
A 1 271 GLU 271 -56  ?   ?   ?   B . n 
A 1 272 TYR 272 -55  ?   ?   ?   B . n 
A 1 273 GLY 273 -54  ?   ?   ?   B . n 
A 1 274 ASN 274 -53  ?   ?   ?   B . n 
A 1 275 CYS 275 -52  ?   ?   ?   B . n 
A 1 276 ASN 276 -51  ?   ?   ?   B . n 
A 1 277 THR 277 -50  ?   ?   ?   B . n 
A 1 278 THR 278 -49  ?   ?   ?   B . n 
A 1 279 CYS 279 -48  ?   ?   ?   B . n 
A 1 280 GLN 280 -47  ?   ?   ?   B . n 
A 1 281 THR 281 -46  ?   ?   ?   B . n 
A 1 282 PRO 282 -45  ?   ?   ?   B . n 
A 1 283 LYS 283 -44  ?   ?   ?   B . n 
A 1 284 GLY 284 -43  ?   ?   ?   B . n 
A 1 285 ALA 285 -42  ?   ?   ?   B . n 
A 1 286 ILE 286 -41  ?   ?   ?   B . n 
A 1 287 ASN 287 -40  ?   ?   ?   B . n 
A 1 288 THR 288 -39  ?   ?   ?   B . n 
A 1 289 SER 289 -38  ?   ?   ?   B . n 
A 1 290 LEU 290 -37  ?   ?   ?   B . n 
A 1 291 PRO 291 -36  ?   ?   ?   B . n 
A 1 292 PHE 292 -35  ?   ?   ?   B . n 
A 1 293 GLN 293 -34  ?   ?   ?   B . n 
A 1 294 ASN 294 -33  ?   ?   ?   B . n 
A 1 295 ILE 295 -32  ?   ?   ?   B . n 
A 1 296 HIS 296 -31  ?   ?   ?   B . n 
A 1 297 PRO 297 -30  ?   ?   ?   B . n 
A 1 298 ILE 298 -29  ?   ?   ?   B . n 
A 1 299 THR 299 -28  ?   ?   ?   B . n 
A 1 300 ILE 300 -27  ?   ?   ?   B . n 
A 1 301 GLY 301 -26  ?   ?   ?   B . n 
A 1 302 LYS 302 -25  ?   ?   ?   B . n 
A 1 303 CYS 303 -24  ?   ?   ?   B . n 
A 1 304 PRO 304 -23  ?   ?   ?   B . n 
A 1 305 LYS 305 -22  ?   ?   ?   B . n 
A 1 306 TYR 306 -21  ?   ?   ?   B . n 
A 1 307 VAL 307 -20  ?   ?   ?   B . n 
A 1 308 LYS 308 -19  ?   ?   ?   B . n 
A 1 309 SER 309 -18  ?   ?   ?   B . n 
A 1 310 THR 310 -17  ?   ?   ?   B . n 
A 1 311 LYS 311 -16  ?   ?   ?   B . n 
A 1 312 LEU 312 -15  ?   ?   ?   B . n 
A 1 313 ARG 313 -14  ?   ?   ?   B . n 
A 1 314 LEU 314 -13  ?   ?   ?   B . n 
A 1 315 ALA 315 -12  ?   ?   ?   B . n 
A 1 316 THR 316 -11  ?   ?   ?   B . n 
A 1 317 GLY 317 -10  ?   ?   ?   B . n 
A 1 318 LEU 318 -9   ?   ?   ?   B . n 
A 1 319 ARG 319 -8   ?   ?   ?   B . n 
A 1 320 ASN 320 -7   ?   ?   ?   B . n 
A 1 321 VAL 321 -6   ?   ?   ?   B . n 
A 1 322 PRO 322 -5   ?   ?   ?   B . n 
A 1 323 SER 323 -4   ?   ?   ?   B . n 
A 1 324 ILE 324 -3   ?   ?   ?   B . n 
A 1 325 GLN 325 -2   ?   ?   ?   B . n 
A 1 326 SER 326 -1   ?   ?   ?   B . n 
A 1 327 ARG 327 0    ?   ?   ?   B . n 
A 1 328 GLY 328 1    ?   ?   ?   B . n 
A 1 329 LEU 329 2    ?   ?   ?   B . n 
A 1 330 PHE 330 3    ?   ?   ?   B . n 
A 1 331 GLY 331 4    ?   ?   ?   B . n 
A 1 332 ALA 332 5    ?   ?   ?   B . n 
A 1 333 ILE 333 6    ?   ?   ?   B . n 
A 1 334 ALA 334 7    ?   ?   ?   B . n 
A 1 335 GLY 335 8    ?   ?   ?   B . n 
A 1 336 PHE 336 9    ?   ?   ?   B . n 
A 1 337 ILE 337 10   10  ILE ILE B . n 
A 1 338 GLU 338 11   11  GLU GLU B . n 
A 1 339 GLY 339 12   12  GLY GLY B . n 
A 1 340 GLY 340 13   13  GLY GLY B . n 
A 1 341 TRP 341 14   14  TRP TRP B . n 
A 1 342 THR 342 15   15  THR THR B . n 
A 1 343 GLY 343 16   16  GLY GLY B . n 
A 1 344 MET 344 17   17  MET MET B . n 
A 1 345 VAL 345 18   18  VAL VAL B . n 
A 1 346 ASP 346 19   19  ASP ASP B . n 
A 1 347 GLY 347 20   20  GLY GLY B . n 
A 1 348 TRP 348 21   21  TRP TRP B . n 
A 1 349 TYR 349 22   22  TYR TYR B . n 
A 1 350 GLY 350 23   23  GLY GLY B . n 
A 1 351 TYR 351 24   24  TYR TYR B . n 
A 1 352 HIS 352 25   25  HIS HIS B . n 
A 1 353 HIS 353 26   26  HIS HIS B . n 
A 1 354 GLN 354 27   27  GLN GLN B . n 
A 1 355 ASN 355 28   28  ASN ASN B . n 
A 1 356 GLU 356 29   29  GLU GLU B . n 
A 1 357 GLN 357 30   30  GLN GLN B . n 
A 1 358 GLY 358 31   31  GLY GLY B . n 
A 1 359 SER 359 32   32  SER SER B . n 
A 1 360 GLY 360 33   33  GLY GLY B . n 
A 1 361 TYR 361 34   34  TYR TYR B . n 
A 1 362 ALA 362 35   35  ALA ALA B . n 
A 1 363 ALA 363 36   36  ALA ALA B . n 
A 1 364 ASP 364 37   37  ASP ASP B . n 
A 1 365 LEU 365 38   38  LEU LEU B . n 
A 1 366 LYS 366 39   39  LYS LYS B . n 
A 1 367 SER 367 40   40  SER SER B . n 
A 1 368 THR 368 41   41  THR THR B . n 
A 1 369 GLN 369 42   42  GLN GLN B . n 
A 1 370 ASN 370 43   43  ASN ASN B . n 
A 1 371 ALA 371 44   44  ALA ALA B . n 
A 1 372 ILE 372 45   45  ILE ILE B . n 
A 1 373 ASP 373 46   46  ASP ASP B . n 
A 1 374 GLY 374 47   47  GLY GLY B . n 
A 1 375 ILE 375 48   48  ILE ILE B . n 
A 1 376 THR 376 49   49  THR THR B . n 
A 1 377 ASN 377 50   50  ASN ASN B . n 
A 1 378 LYS 378 51   51  LYS LYS B . n 
A 1 379 VAL 379 52   52  VAL VAL B . n 
A 1 380 ASN 380 53   53  ASN ASN B . n 
A 1 381 SER 381 54   54  SER SER B . n 
A 1 382 VAL 382 55   55  VAL VAL B . n 
A 1 383 ILE 383 56   56  ILE ILE B . n 
A 1 384 GLU 384 57   57  GLU GLU B . n 
A 1 385 LYS 385 58   58  LYS LYS B . n 
A 1 386 MET 386 59   59  MET MET B . n 
A 1 387 ASN 387 60   60  ASN ASN B . n 
A 1 388 THR 388 61   61  THR THR B . n 
A 1 389 GLN 389 62   62  GLN GLN B . n 
A 1 390 PHE 390 63   63  PHE PHE B . n 
A 1 391 THR 391 64   64  THR THR B . n 
A 1 392 ALA 392 65   65  ALA ALA B . n 
A 1 393 VAL 393 66   66  VAL VAL B . n 
A 1 394 GLY 394 67   67  GLY GLY B . n 
A 1 395 LYS 395 68   68  LYS LYS B . n 
A 1 396 GLU 396 69   69  GLU GLU B . n 
A 1 397 PHE 397 70   70  PHE PHE B . n 
A 1 398 ASN 398 71   71  ASN ASN B . n 
A 1 399 HIS 399 72   72  HIS HIS B . n 
A 1 400 LEU 400 73   73  LEU LEU B . n 
A 1 401 GLU 401 74   74  GLU GLU B . n 
A 1 402 LYS 402 75   75  LYS LYS B . n 
A 1 403 ARG 403 76   76  ARG ARG B . n 
A 1 404 ILE 404 77   77  ILE ILE B . n 
A 1 405 GLU 405 78   78  GLU GLU B . n 
A 1 406 ASN 406 79   79  ASN ASN B . n 
A 1 407 LEU 407 80   80  LEU LEU B . n 
A 1 408 ASN 408 81   81  ASN ASN B . n 
A 1 409 LYS 409 82   82  LYS LYS B . n 
A 1 410 LYS 410 83   83  LYS LYS B . n 
A 1 411 VAL 411 84   84  VAL VAL B . n 
A 1 412 ASP 412 85   85  ASP ASP B . n 
A 1 413 ASP 413 86   86  ASP ASP B . n 
A 1 414 GLY 414 87   87  GLY GLY B . n 
A 1 415 PHE 415 88   88  PHE PHE B . n 
A 1 416 LEU 416 89   89  LEU LEU B . n 
A 1 417 ASP 417 90   90  ASP ASP B . n 
A 1 418 ILE 418 91   91  ILE ILE B . n 
A 1 419 TRP 419 92   92  TRP TRP B . n 
A 1 420 THR 420 93   93  THR THR B . n 
A 1 421 TYR 421 94   94  TYR TYR B . n 
A 1 422 ASN 422 95   95  ASN ASN B . n 
A 1 423 ALA 423 96   96  ALA ALA B . n 
A 1 424 GLU 424 97   97  GLU GLU B . n 
A 1 425 LEU 425 98   98  LEU LEU B . n 
A 1 426 LEU 426 99   99  LEU LEU B . n 
A 1 427 VAL 427 100  100 VAL VAL B . n 
A 1 428 LEU 428 101  101 LEU LEU B . n 
A 1 429 LEU 429 102  102 LEU LEU B . n 
A 1 430 GLU 430 103  103 GLU GLU B . n 
A 1 431 ASN 431 104  104 ASN ASN B . n 
A 1 432 GLU 432 105  105 GLU GLU B . n 
A 1 433 ARG 433 106  106 ARG ARG B . n 
A 1 434 THR 434 107  107 THR THR B . n 
A 1 435 LEU 435 108  108 LEU LEU B . n 
A 1 436 ASP 436 109  109 ASP ASP B . n 
A 1 437 TYR 437 110  110 TYR TYR B . n 
A 1 438 HIS 438 111  111 HIS HIS B . n 
A 1 439 ASP 439 112  112 ASP ASP B . n 
A 1 440 SER 440 113  113 SER SER B . n 
A 1 441 ASN 441 114  114 ASN ASN B . n 
A 1 442 VAL 442 115  115 VAL VAL B . n 
A 1 443 LYS 443 116  116 LYS LYS B . n 
A 1 444 ASN 444 117  117 ASN ASN B . n 
A 1 445 LEU 445 118  118 LEU LEU B . n 
A 1 446 TYR 446 119  119 TYR TYR B . n 
A 1 447 GLU 447 120  120 GLU GLU B . n 
A 1 448 LYS 448 121  121 LYS LYS B . n 
A 1 449 VAL 449 122  122 VAL VAL B . n 
A 1 450 ARG 450 123  123 ARG ARG B . n 
A 1 451 SER 451 124  124 SER SER B . n 
A 1 452 GLN 452 125  125 GLN GLN B . n 
A 1 453 LEU 453 126  126 LEU LEU B . n 
A 1 454 LYS 454 127  127 LYS LYS B . n 
A 1 455 ASN 455 128  128 ASN ASN B . n 
A 1 456 ASN 456 129  129 ASN ASN B . n 
A 1 457 ALA 457 130  130 ALA ALA B . n 
A 1 458 LYS 458 131  131 LYS LYS B . n 
A 1 459 GLU 459 132  132 GLU GLU B . n 
A 1 460 ILE 460 133  133 ILE ILE B . n 
A 1 461 GLY 461 134  134 GLY GLY B . n 
A 1 462 ASN 462 135  135 ASN ASN B . n 
A 1 463 GLY 463 136  136 GLY GLY B . n 
A 1 464 CYS 464 137  137 CYS CYS B . n 
A 1 465 PHE 465 138  138 PHE PHE B . n 
A 1 466 GLU 466 139  139 GLU GLU B . n 
A 1 467 PHE 467 140  140 PHE PHE B . n 
A 1 468 TYR 468 141  141 TYR TYR B . n 
A 1 469 HIS 469 142  142 HIS HIS B . n 
A 1 470 LYS 470 143  143 LYS LYS B . n 
A 1 471 CYS 471 144  144 CYS CYS B . n 
A 1 472 ASP 472 145  145 ASP ASP B . n 
A 1 473 ASN 473 146  146 ASN ASN B . n 
A 1 474 THR 474 147  147 THR THR B . n 
A 1 475 CYS 475 148  148 CYS CYS B . n 
A 1 476 MET 476 149  149 MET MET B . n 
A 1 477 GLU 477 150  150 GLU GLU B . n 
A 1 478 SER 478 151  151 SER SER B . n 
A 1 479 VAL 479 152  152 VAL VAL B . n 
A 1 480 LYS 480 153  153 LYS LYS B . n 
A 1 481 ASN 481 154  154 ASN ASN B . n 
A 1 482 GLY 482 155  155 GLY GLY B . n 
A 1 483 THR 483 156  156 THR THR B . n 
A 1 484 TYR 484 157  157 TYR TYR B . n 
A 1 485 ASP 485 158  158 ASP ASP B . n 
A 1 486 TYR 486 159  159 TYR TYR B . n 
A 1 487 PRO 487 160  160 PRO PRO B . n 
A 1 488 LYS 488 161  161 LYS LYS B . n 
A 1 489 TYR 489 162  162 TYR TYR B . n 
A 1 490 SER 490 163  163 SER SER B . n 
A 1 491 GLU 491 164  164 GLU GLU B . n 
A 1 492 GLU 492 165  165 GLU GLU B . n 
A 1 493 ALA 493 166  166 ALA ALA B . n 
A 1 494 LYS 494 167  167 LYS LYS B . n 
A 1 495 LEU 495 168  168 LEU LEU B . n 
A 1 496 ASN 496 169  169 ASN ASN B . n 
A 1 497 ARG 497 170  170 ARG ARG B . n 
A 1 498 GLU 498 171  171 GLU GLU B . n 
A 1 499 GLU 499 172  172 GLU GLU B . n 
A 1 500 ILE 500 173  173 ILE ILE B . n 
A 1 501 ASP 501 174  174 ASP ASP B . n 
A 1 502 SER 502 175  ?   ?   ?   B . n 
A 1 503 GLY 503 176  ?   ?   ?   B . n 
A 1 504 ARG 504 177  ?   ?   ?   B . n 
B 2 1   GLN 1   1    1   GLN GLN H . n 
B 2 2   VAL 2   2    2   VAL VAL H . n 
B 2 3   GLN 3   3    3   GLN GLN H . n 
B 2 4   LEU 4   4    4   LEU LEU H . n 
B 2 5   VAL 5   5    5   VAL VAL H . n 
B 2 6   GLN 6   6    6   GLN GLN H . n 
B 2 7   SER 7   7    7   SER SER H . n 
B 2 8   GLY 8   8    8   GLY GLY H . n 
B 2 9   ALA 9   9    9   ALA ALA H . n 
B 2 10  GLU 10  10   10  GLU GLU H . n 
B 2 11  VAL 11  11   11  VAL VAL H . n 
B 2 12  LYS 12  12   12  LYS LYS H . n 
B 2 13  LYS 13  13   13  LYS LYS H . n 
B 2 14  PRO 14  14   14  PRO PRO H . n 
B 2 15  GLY 15  15   15  GLY GLY H . n 
B 2 16  ALA 16  16   16  ALA ALA H . n 
B 2 17  SER 17  17   17  SER SER H . n 
B 2 18  VAL 18  18   18  VAL VAL H . n 
B 2 19  LYS 19  19   19  LYS LYS H . n 
B 2 20  VAL 20  20   20  VAL VAL H . n 
B 2 21  SER 21  21   21  SER SER H . n 
B 2 22  CYS 22  22   22  CYS CYS H . n 
B 2 23  LYS 23  23   23  LYS LYS H . n 
B 2 24  ALA 24  24   24  ALA ALA H . n 
B 2 25  SER 25  25   25  SER SER H . n 
B 2 26  GLY 26  26   26  GLY GLY H . n 
B 2 27  TYR 27  27   27  TYR TYR H . n 
B 2 28  SER 28  28   28  SER SER H . n 
B 2 29  PHE 29  29   29  PHE PHE H . n 
B 2 30  SER 30  30   30  SER SER H . n 
B 2 31  SER 31  31   31  SER SER H . n 
B 2 32  TYR 32  32   32  TYR TYR H . n 
B 2 33  GLY 33  33   33  GLY GLY H . n 
B 2 34  ILE 34  34   34  ILE ILE H . n 
B 2 35  SER 35  35   35  SER SER H . n 
B 2 36  TRP 36  36   36  TRP TRP H . n 
B 2 37  VAL 37  37   37  VAL VAL H . n 
B 2 38  ARG 38  38   38  ARG ARG H . n 
B 2 39  GLN 39  39   39  GLN GLN H . n 
B 2 40  ALA 40  40   40  ALA ALA H . n 
B 2 41  PRO 41  41   41  PRO PRO H . n 
B 2 42  GLY 42  42   42  GLY GLY H . n 
B 2 43  GLN 43  43   43  GLN GLN H . n 
B 2 44  GLY 44  44   44  GLY GLY H . n 
B 2 45  LEU 45  45   45  LEU LEU H . n 
B 2 46  GLU 46  46   46  GLU GLU H . n 
B 2 47  TRP 47  47   47  TRP TRP H . n 
B 2 48  MET 48  48   48  MET MET H . n 
B 2 49  GLY 49  49   49  GLY GLY H . n 
B 2 50  TRP 50  50   50  TRP TRP H . n 
B 2 51  ILE 51  51   51  ILE ILE H . n 
B 2 52  SER 52  52   52  SER SER H . n 
B 2 53  ALA 53  53   53  ALA ALA H . n 
B 2 54  TYR 54  54   54  TYR TYR H . n 
B 2 55  ASN 55  55   55  ASN ASN H . n 
B 2 56  GLY 56  56   56  GLY GLY H . n 
B 2 57  ASN 57  57   57  ASN ASN H . n 
B 2 58  THR 58  58   58  THR THR H . n 
B 2 59  ASN 59  59   59  ASN ASN H . n 
B 2 60  TYR 60  60   60  TYR TYR H . n 
B 2 61  ALA 61  61   61  ALA ALA H . n 
B 2 62  GLN 62  62   62  GLN GLN H . n 
B 2 63  LYS 63  63   63  LYS LYS H . n 
B 2 64  LEU 64  64   64  LEU LEU H . n 
B 2 65  GLN 65  65   65  GLN GLN H . n 
B 2 66  GLY 66  66   66  GLY GLY H . n 
B 2 67  ARG 67  67   67  ARG ARG H . n 
B 2 68  VAL 68  68   68  VAL VAL H . n 
B 2 69  THR 69  69   69  THR THR H . n 
B 2 70  MET 70  70   70  MET MET H . n 
B 2 71  THR 71  71   71  THR THR H . n 
B 2 72  THR 72  72   72  THR THR H . n 
B 2 73  ASP 73  73   73  ASP ASP H . n 
B 2 74  THR 74  74   74  THR THR H . n 
B 2 75  SER 75  75   75  SER SER H . n 
B 2 76  THR 76  76   76  THR THR H . n 
B 2 77  SER 77  77   77  SER SER H . n 
B 2 78  THR 78  78   78  THR THR H . n 
B 2 79  ALA 79  79   79  ALA ALA H . n 
B 2 80  TYR 80  80   80  TYR TYR H . n 
B 2 81  MET 81  81   81  MET MET H . n 
B 2 82  GLU 82  82   82  GLU GLU H . n 
B 2 83  LEU 83  83   83  LEU LEU H . n 
B 2 84  ARG 84  84   84  ARG ARG H . n 
B 2 85  SER 85  85   85  SER SER H . n 
B 2 86  LEU 86  86   86  LEU LEU H . n 
B 2 87  ARG 87  87   87  ARG ARG H . n 
B 2 88  SER 88  88   88  SER SER H . n 
B 2 89  ASP 89  89   89  ASP ASP H . n 
B 2 90  ASP 90  90   90  ASP ASP H . n 
B 2 91  THR 91  91   91  THR THR H . n 
B 2 92  ALA 92  92   92  ALA ALA H . n 
B 2 93  VAL 93  93   93  VAL VAL H . n 
B 2 94  PHE 94  94   94  PHE PHE H . n 
B 2 95  TYR 95  95   95  TYR TYR H . n 
B 2 96  CYS 96  96   96  CYS CYS H . n 
B 2 97  ALA 97  97   97  ALA ALA H . n 
B 2 98  ARG 98  98   98  ARG ARG H . n 
B 2 99  ASP 99  99   99  ASP ASP H . n 
B 2 100 ARG 100 100  100 ARG ARG H . n 
B 2 101 PRO 101 101  101 PRO PRO H . n 
B 2 102 HIS 102 102  102 HIS HIS H . n 
B 2 103 ILE 103 103  103 ILE ILE H . n 
B 2 104 LEU 104 104  104 LEU LEU H . n 
B 2 105 THR 105 105  105 THR THR H . n 
B 2 106 GLY 106 106  106 GLY GLY H . n 
B 2 107 PHE 107 107  107 PHE PHE H . n 
B 2 108 ASP 108 108  108 ASP ASP H . n 
B 2 109 PHE 109 109  109 PHE PHE H . n 
B 2 110 ASP 110 110  110 ASP ASP H . n 
B 2 111 TYR 111 111  111 TYR TYR H . n 
B 2 112 TRP 112 112  112 TRP TRP H . n 
B 2 113 GLY 113 113  113 GLY GLY H . n 
B 2 114 GLN 114 114  114 GLN GLN H . n 
B 2 115 GLY 115 115  115 GLY GLY H . n 
B 2 116 THR 116 116  116 THR THR H . n 
B 2 117 LEU 117 117  117 LEU LEU H . n 
B 2 118 VAL 118 118  118 VAL VAL H . n 
B 2 119 THR 119 119  119 THR THR H . n 
B 2 120 VAL 120 120  120 VAL VAL H . n 
B 2 121 SER 121 121  121 SER SER H . n 
B 2 122 SER 122 122  122 SER SER H . n 
B 2 123 ALA 123 123  123 ALA ALA H . n 
B 2 124 SER 124 124  124 SER SER H . n 
B 2 125 THR 125 125  125 THR THR H . n 
B 2 126 LYS 126 126  126 LYS LYS H . n 
B 2 127 GLY 127 127  127 GLY GLY H . n 
B 2 128 PRO 128 128  128 PRO PRO H . n 
B 2 129 SER 129 129  129 SER SER H . n 
B 2 130 VAL 130 130  130 VAL VAL H . n 
B 2 131 PHE 131 131  131 PHE PHE H . n 
B 2 132 PRO 132 132  132 PRO PRO H . n 
B 2 133 LEU 133 133  133 LEU LEU H . n 
B 2 134 ALA 134 134  134 ALA ALA H . n 
B 2 135 PRO 135 135  135 PRO PRO H . n 
B 2 136 SER 136 136  136 SER SER H . n 
B 2 137 SER 137 137  137 SER SER H . n 
B 2 138 LYS 138 138  138 LYS LYS H . n 
B 2 139 SER 139 139  139 SER SER H . n 
B 2 140 THR 140 140  140 THR THR H . n 
B 2 141 SER 141 141  141 SER SER H . n 
B 2 142 GLY 142 142  142 GLY GLY H . n 
B 2 143 GLY 143 143  143 GLY GLY H . n 
B 2 144 THR 144 144  144 THR THR H . n 
B 2 145 ALA 145 145  145 ALA ALA H . n 
B 2 146 ALA 146 146  146 ALA ALA H . n 
B 2 147 LEU 147 147  147 LEU LEU H . n 
B 2 148 GLY 148 148  148 GLY GLY H . n 
B 2 149 CYS 149 149  149 CYS CYS H . n 
B 2 150 LEU 150 150  150 LEU LEU H . n 
B 2 151 VAL 151 151  151 VAL VAL H . n 
B 2 152 LYS 152 152  152 LYS LYS H . n 
B 2 153 ASP 153 153  153 ASP ASP H . n 
B 2 154 TYR 154 154  154 TYR TYR H . n 
B 2 155 PHE 155 155  155 PHE PHE H . n 
B 2 156 PRO 156 156  156 PRO PRO H . n 
B 2 157 GLU 157 157  157 GLU GLU H . n 
B 2 158 PRO 158 158  158 PRO PRO H . n 
B 2 159 VAL 159 159  159 VAL VAL H . n 
B 2 160 THR 160 160  160 THR THR H . n 
B 2 161 VAL 161 161  161 VAL VAL H . n 
B 2 162 SER 162 162  162 SER SER H . n 
B 2 163 TRP 163 163  163 TRP TRP H . n 
B 2 164 ASN 164 164  164 ASN ASN H . n 
B 2 165 SER 165 165  165 SER SER H . n 
B 2 166 GLY 166 166  166 GLY GLY H . n 
B 2 167 ALA 167 167  167 ALA ALA H . n 
B 2 168 LEU 168 168  168 LEU LEU H . n 
B 2 169 THR 169 169  169 THR THR H . n 
B 2 170 SER 170 170  170 SER SER H . n 
B 2 171 GLY 171 171  171 GLY GLY H . n 
B 2 172 VAL 172 172  172 VAL VAL H . n 
B 2 173 HIS 173 173  173 HIS HIS H . n 
B 2 174 THR 174 174  174 THR THR H . n 
B 2 175 PHE 175 175  175 PHE PHE H . n 
B 2 176 PRO 176 176  176 PRO PRO H . n 
B 2 177 ALA 177 177  177 ALA ALA H . n 
B 2 178 VAL 178 178  178 VAL VAL H . n 
B 2 179 LEU 179 179  179 LEU LEU H . n 
B 2 180 GLN 180 180  180 GLN GLN H . n 
B 2 181 SER 181 181  181 SER SER H . n 
B 2 182 SER 182 182  182 SER SER H . n 
B 2 183 GLY 183 183  183 GLY GLY H . n 
B 2 184 LEU 184 184  184 LEU LEU H . n 
B 2 185 TYR 185 185  185 TYR TYR H . n 
B 2 186 SER 186 186  186 SER SER H . n 
B 2 187 LEU 187 187  187 LEU LEU H . n 
B 2 188 SER 188 188  188 SER SER H . n 
B 2 189 SER 189 189  189 SER SER H . n 
B 2 190 VAL 190 190  190 VAL VAL H . n 
B 2 191 VAL 191 191  191 VAL VAL H . n 
B 2 192 THR 192 192  192 THR THR H . n 
B 2 193 VAL 193 193  193 VAL VAL H . n 
B 2 194 PRO 194 194  194 PRO PRO H . n 
B 2 195 SER 195 195  195 SER SER H . n 
B 2 196 SER 196 196  196 SER SER H . n 
B 2 197 SER 197 197  197 SER SER H . n 
B 2 198 LEU 198 198  198 LEU LEU H . n 
B 2 199 GLY 199 199  199 GLY GLY H . n 
B 2 200 THR 200 200  200 THR THR H . n 
B 2 201 GLN 201 201  201 GLN GLN H . n 
B 2 202 THR 202 202  202 THR THR H . n 
B 2 203 TYR 203 203  203 TYR TYR H . n 
B 2 204 ILE 204 204  204 ILE ILE H . n 
B 2 205 CYS 205 205  205 CYS CYS H . n 
B 2 206 ASN 206 206  206 ASN ASN H . n 
B 2 207 VAL 207 207  207 VAL VAL H . n 
B 2 208 ASN 208 208  208 ASN ASN H . n 
B 2 209 HIS 209 209  209 HIS HIS H . n 
B 2 210 LYS 210 210  210 LYS LYS H . n 
B 2 211 PRO 211 211  211 PRO PRO H . n 
B 2 212 SER 212 212  212 SER SER H . n 
B 2 213 ASN 213 213  213 ASN ASN H . n 
B 2 214 THR 214 214  214 THR THR H . n 
B 2 215 LYS 215 215  215 LYS LYS H . n 
B 2 216 VAL 216 216  216 VAL VAL H . n 
B 2 217 ASP 217 217  217 ASP ASP H . n 
B 2 218 LYS 218 218  218 LYS LYS H . n 
B 2 219 ARG 219 219  219 ARG ARG H . n 
B 2 220 VAL 220 220  220 VAL VAL H . n 
B 2 221 GLU 221 221  221 GLU GLU H . n 
B 2 222 PRO 222 222  222 PRO PRO H . n 
B 2 223 LYS 223 223  223 LYS LYS H . n 
B 2 224 SER 224 224  224 SER SER H . n 
C 3 1   ASP 1   1    1   ASP ASP L . n 
C 3 2   VAL 2   2    2   VAL VAL L . n 
C 3 3   VAL 3   3    3   VAL VAL L . n 
C 3 4   MET 4   4    4   MET MET L . n 
C 3 5   THR 5   5    5   THR THR L . n 
C 3 6   GLN 6   6    6   GLN GLN L . n 
C 3 7   SER 7   7    7   SER SER L . n 
C 3 8   PRO 8   8    8   PRO PRO L . n 
C 3 9   VAL 9   9    9   VAL VAL L . n 
C 3 10  SER 10  10   10  SER SER L . n 
C 3 11  LEU 11  11   11  LEU LEU L . n 
C 3 12  PRO 12  12   12  PRO PRO L . n 
C 3 13  VAL 13  13   13  VAL VAL L . n 
C 3 14  THR 14  14   14  THR THR L . n 
C 3 15  LEU 15  15   15  LEU LEU L . n 
C 3 16  GLY 16  16   16  GLY GLY L . n 
C 3 17  GLN 17  17   17  GLN GLN L . n 
C 3 18  PRO 18  18   18  PRO PRO L . n 
C 3 19  ALA 19  19   19  ALA ALA L . n 
C 3 20  SER 20  20   20  SER SER L . n 
C 3 21  ILE 21  21   21  ILE ILE L . n 
C 3 22  SER 22  22   22  SER SER L . n 
C 3 23  CYS 23  23   23  CYS CYS L . n 
C 3 24  ARG 24  24   24  ARG ARG L . n 
C 3 25  SER 25  25   25  SER SER L . n 
C 3 26  SER 26  26   26  SER SER L . n 
C 3 27  GLN 27  27   27  GLN GLN L . n 
C 3 28  GLY 28  28   28  GLY GLY L . n 
C 3 29  LEU 29  29   29  LEU LEU L . n 
C 3 30  VAL 30  30   30  VAL VAL L . n 
C 3 31  TYR 31  31   31  TYR TYR L . n 
C 3 32  ILE 32  32   32  ILE ILE L . n 
C 3 33  ASP 33  33   33  ASP ASP L . n 
C 3 34  GLY 34  34   34  GLY GLY L . n 
C 3 35  ASN 35  35   35  ASN ASN L . n 
C 3 36  THR 36  36   36  THR THR L . n 
C 3 37  TYR 37  37   37  TYR TYR L . n 
C 3 38  LEU 38  38   38  LEU LEU L . n 
C 3 39  ASN 39  39   39  ASN ASN L . n 
C 3 40  TRP 40  40   40  TRP TRP L . n 
C 3 41  PHE 41  41   41  PHE PHE L . n 
C 3 42  GLN 42  42   42  GLN GLN L . n 
C 3 43  GLN 43  43   43  GLN GLN L . n 
C 3 44  ARG 44  44   44  ARG ARG L . n 
C 3 45  PRO 45  45   45  PRO PRO L . n 
C 3 46  GLY 46  46   46  GLY GLY L . n 
C 3 47  GLN 47  47   47  GLN GLN L . n 
C 3 48  SER 48  48   48  SER SER L . n 
C 3 49  PRO 49  49   49  PRO PRO L . n 
C 3 50  ARG 50  50   50  ARG ARG L . n 
C 3 51  ARG 51  51   51  ARG ARG L . n 
C 3 52  LEU 52  52   52  LEU LEU L . n 
C 3 53  ILE 53  53   53  ILE ILE L . n 
C 3 54  TYR 54  54   54  TYR TYR L . n 
C 3 55  ASN 55  55   55  ASN ASN L . n 
C 3 56  VAL 56  56   56  VAL VAL L . n 
C 3 57  PHE 57  57   57  PHE PHE L . n 
C 3 58  THR 58  58   58  THR THR L . n 
C 3 59  ARG 59  59   59  ARG ARG L . n 
C 3 60  ASP 60  60   60  ASP ASP L . n 
C 3 61  SER 61  61   61  SER SER L . n 
C 3 62  GLY 62  62   62  GLY GLY L . n 
C 3 63  VAL 63  63   63  VAL VAL L . n 
C 3 64  PRO 64  64   64  PRO PRO L . n 
C 3 65  ASP 65  65   65  ASP ASP L . n 
C 3 66  ARG 66  66   66  ARG ARG L . n 
C 3 67  PHE 67  67   67  PHE PHE L . n 
C 3 68  SER 68  68   68  SER SER L . n 
C 3 69  GLY 69  69   69  GLY GLY L . n 
C 3 70  SER 70  70   70  SER SER L . n 
C 3 71  GLY 71  71   71  GLY GLY L . n 
C 3 72  SER 72  72   72  SER SER L . n 
C 3 73  GLY 73  73   73  GLY GLY L . n 
C 3 74  THR 74  74   74  THR THR L . n 
C 3 75  ASP 75  75   75  ASP ASP L . n 
C 3 76  PHE 76  76   76  PHE PHE L . n 
C 3 77  THR 77  77   77  THR THR L . n 
C 3 78  LEU 78  78   78  LEU LEU L . n 
C 3 79  LYS 79  79   79  LYS LYS L . n 
C 3 80  ILE 80  80   80  ILE ILE L . n 
C 3 81  THR 81  81   81  THR THR L . n 
C 3 82  THR 82  82   82  THR THR L . n 
C 3 83  VAL 83  83   83  VAL VAL L . n 
C 3 84  GLU 84  84   84  GLU GLU L . n 
C 3 85  ALA 85  85   85  ALA ALA L . n 
C 3 86  GLU 86  86   86  GLU GLU L . n 
C 3 87  ASP 87  87   87  ASP ASP L . n 
C 3 88  VAL 88  88   88  VAL VAL L . n 
C 3 89  GLY 89  89   89  GLY GLY L . n 
C 3 90  VAL 90  90   90  VAL VAL L . n 
C 3 91  TYR 91  91   91  TYR TYR L . n 
C 3 92  TYR 92  92   92  TYR TYR L . n 
C 3 93  CYS 93  93   93  CYS CYS L . n 
C 3 94  MET 94  94   94  MET MET L . n 
C 3 95  GLN 95  95   95  GLN GLN L . n 
C 3 96  GLY 96  96   96  GLY GLY L . n 
C 3 97  THR 97  97   97  THR THR L . n 
C 3 98  HIS 98  98   98  HIS HIS L . n 
C 3 99  TRP 99  99   99  TRP TRP L . n 
C 3 100 PRO 100 100  100 PRO PRO L . n 
C 3 101 TYR 101 101  101 TYR TYR L . n 
C 3 102 THR 102 102  102 THR THR L . n 
C 3 103 PHE 103 103  103 PHE PHE L . n 
C 3 104 GLY 104 104  104 GLY GLY L . n 
C 3 105 GLN 105 105  105 GLN GLN L . n 
C 3 106 GLY 106 106  106 GLY GLY L . n 
C 3 107 THR 107 107  107 THR THR L . n 
C 3 108 LYS 108 108  108 LYS LYS L . n 
C 3 109 LEU 109 109  109 LEU LEU L . n 
C 3 110 GLU 110 110  110 GLU GLU L . n 
C 3 111 ILE 111 111  111 ILE ILE L . n 
C 3 112 LYS 112 112  112 LYS LYS L . n 
C 3 113 ARG 113 113  113 ARG ARG L . n 
C 3 114 THR 114 114  114 THR THR L . n 
C 3 115 VAL 115 115  115 VAL VAL L . n 
C 3 116 ALA 116 116  116 ALA ALA L . n 
C 3 117 ALA 117 117  117 ALA ALA L . n 
C 3 118 PRO 118 118  118 PRO PRO L . n 
C 3 119 SER 119 119  119 SER SER L . n 
C 3 120 VAL 120 120  120 VAL VAL L . n 
C 3 121 PHE 121 121  121 PHE PHE L . n 
C 3 122 ILE 122 122  122 ILE ILE L . n 
C 3 123 PHE 123 123  123 PHE PHE L . n 
C 3 124 PRO 124 124  124 PRO PRO L . n 
C 3 125 PRO 125 125  125 PRO PRO L . n 
C 3 126 SER 126 126  126 SER SER L . n 
C 3 127 ASP 127 127  127 ASP ASP L . n 
C 3 128 GLU 128 128  128 GLU GLU L . n 
C 3 129 GLN 129 129  129 GLN GLN L . n 
C 3 130 LEU 130 130  130 LEU LEU L . n 
C 3 131 LYS 131 131  131 LYS LYS L . n 
C 3 132 SER 132 132  132 SER SER L . n 
C 3 133 GLY 133 133  133 GLY GLY L . n 
C 3 134 THR 134 134  134 THR THR L . n 
C 3 135 ALA 135 135  135 ALA ALA L . n 
C 3 136 SER 136 136  136 SER SER L . n 
C 3 137 VAL 137 137  137 VAL VAL L . n 
C 3 138 VAL 138 138  138 VAL VAL L . n 
C 3 139 CYS 139 139  139 CYS CYS L . n 
C 3 140 LEU 140 140  140 LEU LEU L . n 
C 3 141 LEU 141 141  141 LEU LEU L . n 
C 3 142 ASN 142 142  142 ASN ASN L . n 
C 3 143 ASN 143 143  143 ASN ASN L . n 
C 3 144 PHE 144 144  144 PHE PHE L . n 
C 3 145 TYR 145 145  145 TYR TYR L . n 
C 3 146 PRO 146 146  146 PRO PRO L . n 
C 3 147 ARG 147 147  147 ARG ARG L . n 
C 3 148 GLU 148 148  148 GLU GLU L . n 
C 3 149 ALA 149 149  149 ALA ALA L . n 
C 3 150 LYS 150 150  150 LYS LYS L . n 
C 3 151 VAL 151 151  151 VAL VAL L . n 
C 3 152 GLN 152 152  152 GLN GLN L . n 
C 3 153 TRP 153 153  153 TRP TRP L . n 
C 3 154 LYS 154 154  154 LYS LYS L . n 
C 3 155 VAL 155 155  155 VAL VAL L . n 
C 3 156 ASP 156 156  156 ASP ASP L . n 
C 3 157 ASN 157 157  157 ASN ASN L . n 
C 3 158 ALA 158 158  158 ALA ALA L . n 
C 3 159 LEU 159 159  159 LEU LEU L . n 
C 3 160 GLN 160 160  160 GLN GLN L . n 
C 3 161 SER 161 161  161 SER SER L . n 
C 3 162 GLY 162 162  162 GLY GLY L . n 
C 3 163 ASN 163 163  163 ASN ASN L . n 
C 3 164 SER 164 164  164 SER SER L . n 
C 3 165 GLN 165 165  165 GLN GLN L . n 
C 3 166 GLU 166 166  166 GLU GLU L . n 
C 3 167 SER 167 167  167 SER SER L . n 
C 3 168 VAL 168 168  168 VAL VAL L . n 
C 3 169 THR 169 169  169 THR THR L . n 
C 3 170 GLU 170 170  170 GLU GLU L . n 
C 3 171 GLN 171 171  171 GLN GLN L . n 
C 3 172 ASP 172 172  172 ASP ASP L . n 
C 3 173 SER 173 173  173 SER SER L . n 
C 3 174 LYS 174 174  174 LYS LYS L . n 
C 3 175 ASP 175 175  175 ASP ASP L . n 
C 3 176 SER 176 176  176 SER SER L . n 
C 3 177 THR 177 177  177 THR THR L . n 
C 3 178 TYR 178 178  178 TYR TYR L . n 
C 3 179 SER 179 179  179 SER SER L . n 
C 3 180 LEU 180 180  180 LEU LEU L . n 
C 3 181 SER 181 181  181 SER SER L . n 
C 3 182 SER 182 182  182 SER SER L . n 
C 3 183 THR 183 183  183 THR THR L . n 
C 3 184 LEU 184 184  184 LEU LEU L . n 
C 3 185 THR 185 185  185 THR THR L . n 
C 3 186 LEU 186 186  186 LEU LEU L . n 
C 3 187 SER 187 187  187 SER SER L . n 
C 3 188 LYS 188 188  188 LYS LYS L . n 
C 3 189 ALA 189 189  189 ALA ALA L . n 
C 3 190 ASP 190 190  190 ASP ASP L . n 
C 3 191 TYR 191 191  191 TYR TYR L . n 
C 3 192 GLU 192 192  192 GLU GLU L . n 
C 3 193 LYS 193 193  193 LYS LYS L . n 
C 3 194 HIS 194 194  194 HIS HIS L . n 
C 3 195 LYS 195 195  195 LYS LYS L . n 
C 3 196 VAL 196 196  196 VAL VAL L . n 
C 3 197 TYR 197 197  197 TYR TYR L . n 
C 3 198 ALA 198 198  198 ALA ALA L . n 
C 3 199 CYS 199 199  199 CYS CYS L . n 
C 3 200 GLU 200 200  200 GLU GLU L . n 
C 3 201 VAL 201 201  201 VAL VAL L . n 
C 3 202 THR 202 202  202 THR THR L . n 
C 3 203 HIS 203 203  203 HIS HIS L . n 
C 3 204 GLN 204 204  204 GLN GLN L . n 
C 3 205 GLY 205 205  205 GLY GLY L . n 
C 3 206 LEU 206 206  206 LEU LEU L . n 
C 3 207 SER 207 207  207 SER SER L . n 
C 3 208 SER 208 208  208 SER SER L . n 
C 3 209 PRO 209 209  209 PRO PRO L . n 
C 3 210 VAL 210 210  210 VAL VAL L . n 
C 3 211 THR 211 211  211 THR THR L . n 
C 3 212 LYS 212 212  212 LYS LYS L . n 
C 3 213 SER 213 213  213 SER SER L . n 
C 3 214 PHE 214 214  214 PHE PHE L . n 
C 3 215 ASN 215 215  215 ASN ASN L . n 
C 3 216 ARG 216 216  216 ARG ARG L . n 
C 3 217 GLY 217 217  217 GLY GLY L . n 
C 3 218 GLU 218 218  218 GLU GLU L . n 
D 1 1   GLY 1   10   10  GLY GLY A . n 
D 1 2   ASP 2   11   11  ASP ASP A . n 
D 1 3   THR 3   12   12  THR THR A . n 
D 1 4   LEU 4   13   13  LEU LEU A . n 
D 1 5   CYS 5   14   14  CYS CYS A . n 
D 1 6   ILE 6   15   15  ILE ILE A . n 
D 1 7   GLY 7   16   16  GLY GLY A . n 
D 1 8   TYR 8   17   17  TYR TYR A . n 
D 1 9   HIS 9   18   18  HIS HIS A . n 
D 1 10  ALA 10  19   19  ALA ALA A . n 
D 1 11  ASN 11  20   20  ASN ASN A . n 
D 1 12  ASN 12  21   21  ASN ASN A . n 
D 1 13  SER 13  22   22  SER SER A . n 
D 1 14  THR 14  23   23  THR THR A . n 
D 1 15  ASP 15  24   24  ASP ASP A . n 
D 1 16  THR 16  25   25  THR THR A . n 
D 1 17  VAL 17  26   26  VAL VAL A . n 
D 1 18  ASP 18  27   27  ASP ASP A . n 
D 1 19  THR 19  28   28  THR THR A . n 
D 1 20  VAL 20  29   29  VAL VAL A . n 
D 1 21  LEU 21  30   30  LEU LEU A . n 
D 1 22  GLU 22  31   31  GLU GLU A . n 
D 1 23  LYS 23  32   32  LYS LYS A . n 
D 1 24  ASN 24  33   33  ASN ASN A . n 
D 1 25  VAL 25  34   34  VAL VAL A . n 
D 1 26  THR 26  35   35  THR THR A . n 
D 1 27  VAL 27  36   36  VAL VAL A . n 
D 1 28  THR 28  37   37  THR THR A . n 
D 1 29  HIS 29  38   38  HIS HIS A . n 
D 1 30  SER 30  39   39  SER SER A . n 
D 1 31  VAL 31  40   40  VAL VAL A . n 
D 1 32  ASN 32  41   41  ASN ASN A . n 
D 1 33  LEU 33  42   42  LEU LEU A . n 
D 1 34  LEU 34  43   43  LEU LEU A . n 
D 1 35  GLU 35  44   44  GLU GLU A . n 
D 1 36  ASP 36  45   45  ASP ASP A . n 
D 1 37  LYS 37  46   46  LYS LYS A . n 
D 1 38  HIS 38  47   47  HIS HIS A . n 
D 1 39  ASN 39  48   48  ASN ASN A . n 
D 1 40  GLY 40  49   49  GLY GLY A . n 
D 1 41  LYS 41  50   50  LYS LYS A . n 
D 1 42  LEU 42  51   51  LEU LEU A . n 
D 1 43  CYS 43  52   52  CYS CYS A . n 
D 1 44  ASP 44  53   53  ASP ASP A . n 
D 1 45  LEU 45  54   54  LEU LEU A . n 
D 1 46  ASP 46  55   55  ASP ASP A . n 
D 1 47  GLY 47  55   55  GLY GLY A a n 
D 1 48  VAL 48  56   56  VAL VAL A . n 
D 1 49  LYS 49  57   57  LYS LYS A . n 
D 1 50  PRO 50  58   58  PRO PRO A . n 
D 1 51  LEU 51  59   59  LEU LEU A . n 
D 1 52  ILE 52  60   60  ILE ILE A . n 
D 1 53  LEU 53  61   61  LEU LEU A . n 
D 1 54  ARG 54  62   62  ARG ARG A . n 
D 1 55  ASP 55  63   63  ASP ASP A . n 
D 1 56  CYS 56  64   64  CYS CYS A . n 
D 1 57  SER 57  65   65  SER SER A . n 
D 1 58  VAL 58  66   66  VAL VAL A . n 
D 1 59  ALA 59  67   67  ALA ALA A . n 
D 1 60  GLY 60  68   68  GLY GLY A . n 
D 1 61  TRP 61  69   69  TRP TRP A . n 
D 1 62  LEU 62  70   70  LEU LEU A . n 
D 1 63  LEU 63  71   71  LEU LEU A . n 
D 1 64  GLY 64  72   72  GLY GLY A . n 
D 1 65  ASN 65  73   73  ASN ASN A . n 
D 1 66  PRO 66  74   74  PRO PRO A . n 
D 1 67  MET 67  75   75  MET MET A . n 
D 1 68  CYS 68  76   76  CYS CYS A . n 
D 1 69  ASP 69  77   77  ASP ASP A . n 
D 1 70  GLU 70  78   78  GLU GLU A . n 
D 1 71  PHE 71  79   79  PHE PHE A . n 
D 1 72  ILE 72  80   80  ILE ILE A . n 
D 1 73  ASN 73  81   81  ASN ASN A . n 
D 1 74  VAL 74  82   82  VAL VAL A . n 
D 1 75  PRO 75  83   83  PRO PRO A . n 
D 1 76  GLU 76  83   83  GLU GLU A a n 
D 1 77  TRP 77  84   84  TRP TRP A . n 
D 1 78  SER 78  85   85  SER SER A . n 
D 1 79  TYR 79  86   86  TYR TYR A . n 
D 1 80  ILE 80  87   87  ILE ILE A . n 
D 1 81  VAL 81  88   88  VAL VAL A . n 
D 1 82  GLU 82  89   89  GLU GLU A . n 
D 1 83  LYS 83  90   90  LYS LYS A . n 
D 1 84  ALA 84  91   91  ALA ALA A . n 
D 1 85  ASN 85  92   92  ASN ASN A . n 
D 1 86  PRO 86  93   93  PRO PRO A . n 
D 1 87  VAL 87  94   94  VAL VAL A . n 
D 1 88  ASN 88  95   95  ASN ASN A . n 
D 1 89  ASP 89  96   96  ASP ASP A . n 
D 1 90  LEU 90  96   96  LEU LEU A a n 
D 1 91  CYS 91  97   97  CYS CYS A . n 
D 1 92  TYR 92  98   98  TYR TYR A . n 
D 1 93  PRO 93  99   99  PRO PRO A . n 
D 1 94  GLY 94  100  100 GLY GLY A . n 
D 1 95  ASP 95  101  101 ASP ASP A . n 
D 1 96  PHE 96  102  102 PHE PHE A . n 
D 1 97  ASN 97  103  103 ASN ASN A . n 
D 1 98  ASP 98  104  104 ASP ASP A . n 
D 1 99  TYR 99  105  105 TYR TYR A . n 
D 1 100 GLU 100 106  106 GLU GLU A . n 
D 1 101 GLU 101 107  107 GLU GLU A . n 
D 1 102 LEU 102 108  108 LEU LEU A . n 
D 1 103 LYS 103 109  109 LYS LYS A . n 
D 1 104 HIS 104 110  110 HIS HIS A . n 
D 1 105 LEU 105 111  111 LEU LEU A . n 
D 1 106 LEU 106 112  112 LEU LEU A . n 
D 1 107 SER 107 113  113 SER SER A . n 
D 1 108 ARG 108 114  114 ARG ARG A . n 
D 1 109 ILE 109 115  115 ILE ILE A . n 
D 1 110 ASN 110 116  116 ASN ASN A . n 
D 1 111 HIS 111 117  117 HIS HIS A . n 
D 1 112 PHE 112 118  118 PHE PHE A . n 
D 1 113 GLU 113 119  119 GLU GLU A . n 
D 1 114 LYS 114 120  120 LYS LYS A . n 
D 1 115 ILE 115 121  121 ILE ILE A . n 
D 1 116 GLN 116 122  122 GLN GLN A . n 
D 1 117 ILE 117 123  123 ILE ILE A . n 
D 1 118 ILE 118 124  124 ILE ILE A . n 
D 1 119 PRO 119 125  125 PRO PRO A . n 
D 1 120 LYS 120 125  125 LYS LYS A a n 
D 1 121 SER 121 125  125 SER SER A b n 
D 1 122 SER 122 126  126 SER SER A . n 
D 1 123 TRP 123 127  127 TRP TRP A . n 
D 1 124 SER 124 128  128 SER SER A . n 
D 1 125 SER 125 129  129 SER SER A . n 
D 1 126 HIS 126 130  130 HIS HIS A . n 
D 1 127 GLU 127 131  131 GLU GLU A . n 
D 1 128 ALA 128 132  132 ALA ALA A . n 
D 1 129 SER 129 133  133 SER SER A . n 
D 1 130 LEU 130 133  133 LEU LEU A a n 
D 1 131 GLY 131 134  134 GLY GLY A . n 
D 1 132 VAL 132 135  135 VAL VAL A . n 
D 1 133 SER 133 136  136 SER SER A . n 
D 1 134 SER 134 137  137 SER SER A . n 
D 1 135 ALA 135 138  138 ALA ALA A . n 
D 1 136 CYS 136 139  139 CYS CYS A . n 
D 1 137 PRO 137 140  140 PRO PRO A . n 
D 1 138 TYR 138 141  141 TYR TYR A . n 
D 1 139 GLN 139 142  142 GLN GLN A . n 
D 1 140 GLY 140 143  143 GLY GLY A . n 
D 1 141 LYS 141 144  144 LYS LYS A . n 
D 1 142 SER 142 145  145 SER SER A . n 
D 1 143 SER 143 146  146 SER SER A . n 
D 1 144 PHE 144 147  147 PHE PHE A . n 
D 1 145 PHE 145 148  148 PHE PHE A . n 
D 1 146 ARG 146 149  149 ARG ARG A . n 
D 1 147 ASN 147 150  150 ASN ASN A . n 
D 1 148 VAL 148 151  151 VAL VAL A . n 
D 1 149 VAL 149 152  152 VAL VAL A . n 
D 1 150 TRP 150 153  153 TRP TRP A . n 
D 1 151 LEU 151 154  154 LEU LEU A . n 
D 1 152 ILE 152 155  155 ILE ILE A . n 
D 1 153 LYS 153 156  156 LYS LYS A . n 
D 1 154 LYS 154 157  157 LYS LYS A . n 
D 1 155 ASN 155 158  158 ASN ASN A . n 
D 1 156 SER 156 159  159 SER SER A . n 
D 1 157 THR 157 160  160 THR THR A . n 
D 1 158 TYR 158 161  161 TYR TYR A . n 
D 1 159 PRO 159 162  162 PRO PRO A . n 
D 1 160 THR 160 163  163 THR THR A . n 
D 1 161 ILE 161 164  164 ILE ILE A . n 
D 1 162 LYS 162 165  165 LYS LYS A . n 
D 1 163 ARG 163 166  166 ARG ARG A . n 
D 1 164 SER 164 167  167 SER SER A . n 
D 1 165 TYR 165 168  168 TYR TYR A . n 
D 1 166 ASN 166 169  169 ASN ASN A . n 
D 1 167 ASN 167 170  170 ASN ASN A . n 
D 1 168 THR 168 171  171 THR THR A . n 
D 1 169 ASN 169 172  172 ASN ASN A . n 
D 1 170 GLN 170 173  173 GLN GLN A . n 
D 1 171 GLU 171 174  174 GLU GLU A . n 
D 1 172 ASP 172 175  175 ASP ASP A . n 
D 1 173 LEU 173 176  176 LEU LEU A . n 
D 1 174 LEU 174 177  177 LEU LEU A . n 
D 1 175 VAL 175 178  178 VAL VAL A . n 
D 1 176 LEU 176 179  179 LEU LEU A . n 
D 1 177 TRP 177 180  180 TRP TRP A . n 
D 1 178 GLY 178 181  181 GLY GLY A . n 
D 1 179 ILE 179 182  182 ILE ILE A . n 
D 1 180 HIS 180 183  183 HIS HIS A . n 
D 1 181 HIS 181 184  184 HIS HIS A . n 
D 1 182 PRO 182 185  185 PRO PRO A . n 
D 1 183 ASN 183 186  186 ASN ASN A . n 
D 1 184 ASP 184 187  187 ASP ASP A . n 
D 1 185 ALA 185 188  188 ALA ALA A . n 
D 1 186 ALA 186 189  189 ALA ALA A . n 
D 1 187 GLU 187 190  190 GLU GLU A . n 
D 1 188 GLN 188 191  191 GLN GLN A . n 
D 1 189 THR 189 192  192 THR THR A . n 
D 1 190 LYS 190 193  193 LYS LYS A . n 
D 1 191 LEU 191 194  194 LEU LEU A . n 
D 1 192 TYR 192 195  195 TYR TYR A . n 
D 1 193 GLN 193 196  196 GLN GLN A . n 
D 1 194 ASN 194 197  197 ASN ASN A . n 
D 1 195 PRO 195 198  198 PRO PRO A . n 
D 1 196 THR 196 199  199 THR THR A . n 
D 1 197 THR 197 200  200 THR THR A . n 
D 1 198 TYR 198 201  201 TYR TYR A . n 
D 1 199 ILE 199 202  202 ILE ILE A . n 
D 1 200 SER 200 203  203 SER SER A . n 
D 1 201 VAL 201 204  204 VAL VAL A . n 
D 1 202 GLY 202 205  205 GLY GLY A . n 
D 1 203 THR 203 206  206 THR THR A . n 
D 1 204 SER 204 207  207 SER SER A . n 
D 1 205 THR 205 208  208 THR THR A . n 
D 1 206 LEU 206 209  209 LEU LEU A . n 
D 1 207 ASN 207 210  210 ASN ASN A . n 
D 1 208 GLN 208 211  211 GLN GLN A . n 
D 1 209 ARG 209 212  212 ARG ARG A . n 
D 1 210 LEU 210 213  213 LEU LEU A . n 
D 1 211 VAL 211 214  214 VAL VAL A . n 
D 1 212 PRO 212 215  215 PRO PRO A . n 
D 1 213 ARG 213 216  216 ARG ARG A . n 
D 1 214 ILE 214 217  217 ILE ILE A . n 
D 1 215 ALA 215 218  218 ALA ALA A . n 
D 1 216 THR 216 219  219 THR THR A . n 
D 1 217 ARG 217 220  220 ARG ARG A . n 
D 1 218 SER 218 221  221 SER SER A . n 
D 1 219 LYS 219 222  222 LYS LYS A . n 
D 1 220 VAL 220 223  223 VAL VAL A . n 
D 1 221 ASN 221 224  224 ASN ASN A . n 
D 1 222 GLY 222 225  225 GLY GLY A . n 
D 1 223 GLN 223 226  226 GLN GLN A . n 
D 1 224 SER 224 227  227 SER SER A . n 
D 1 225 GLY 225 228  228 GLY GLY A . n 
D 1 226 ARG 226 229  229 ARG ARG A . n 
D 1 227 MET 227 230  230 MET MET A . n 
D 1 228 GLU 228 231  231 GLU GLU A . n 
D 1 229 PHE 229 232  232 PHE PHE A . n 
D 1 230 PHE 230 233  233 PHE PHE A . n 
D 1 231 TRP 231 234  234 TRP TRP A . n 
D 1 232 THR 232 235  235 THR THR A . n 
D 1 233 ILE 233 236  236 ILE ILE A . n 
D 1 234 LEU 234 237  237 LEU LEU A . n 
D 1 235 LYS 235 238  238 LYS LYS A . n 
D 1 236 PRO 236 239  239 PRO PRO A . n 
D 1 237 ASN 237 240  240 ASN ASN A . n 
D 1 238 ASP 238 241  241 ASP ASP A . n 
D 1 239 ALA 239 242  242 ALA ALA A . n 
D 1 240 ILE 240 243  243 ILE ILE A . n 
D 1 241 ASN 241 244  244 ASN ASN A . n 
D 1 242 PHE 242 245  245 PHE PHE A . n 
D 1 243 GLU 243 246  246 GLU GLU A . n 
D 1 244 SER 244 247  247 SER SER A . n 
D 1 245 ASN 245 248  248 ASN ASN A . n 
D 1 246 GLY 246 249  249 GLY GLY A . n 
D 1 247 ASN 247 250  250 ASN ASN A . n 
D 1 248 PHE 248 251  251 PHE PHE A . n 
D 1 249 ILE 249 252  252 ILE ILE A . n 
D 1 250 ALA 250 253  253 ALA ALA A . n 
D 1 251 PRO 251 254  254 PRO PRO A . n 
D 1 252 GLU 252 255  255 GLU GLU A . n 
D 1 253 TYR 253 256  256 TYR TYR A . n 
D 1 254 ALA 254 257  257 ALA ALA A . n 
D 1 255 TYR 255 258  258 TYR TYR A . n 
D 1 256 LYS 256 259  259 LYS LYS A . n 
D 1 257 ILE 257 260  260 ILE ILE A . n 
D 1 258 VAL 258 260  260 VAL VAL A a n 
D 1 259 LYS 259 261  261 LYS LYS A . n 
D 1 260 LYS 260 262  262 LYS LYS A . n 
D 1 261 GLY 261 263  263 GLY GLY A . n 
D 1 262 ASP 262 264  264 ASP ASP A . n 
D 1 263 SER 263 265  265 SER SER A . n 
D 1 264 THR 264 266  266 THR THR A . n 
D 1 265 ILE 265 267  267 ILE ILE A . n 
D 1 266 MET 266 268  268 MET MET A . n 
D 1 267 LYS 267 269  269 LYS LYS A . n 
D 1 268 SER 268 270  270 SER SER A . n 
D 1 269 GLU 269 271  271 GLU GLU A . n 
D 1 270 LEU 270 272  272 LEU LEU A . n 
D 1 271 GLU 271 273  273 GLU GLU A . n 
D 1 272 TYR 272 274  274 TYR TYR A . n 
D 1 273 GLY 273 275  275 GLY GLY A . n 
D 1 274 ASN 274 276  276 ASN ASN A . n 
D 1 275 CYS 275 277  277 CYS CYS A . n 
D 1 276 ASN 276 278  278 ASN ASN A . n 
D 1 277 THR 277 279  279 THR THR A . n 
D 1 278 THR 278 280  280 THR THR A . n 
D 1 279 CYS 279 281  281 CYS CYS A . n 
D 1 280 GLN 280 282  282 GLN GLN A . n 
D 1 281 THR 281 283  283 THR THR A . n 
D 1 282 PRO 282 284  284 PRO PRO A . n 
D 1 283 LYS 283 285  285 LYS LYS A . n 
D 1 284 GLY 284 286  286 GLY GLY A . n 
D 1 285 ALA 285 287  287 ALA ALA A . n 
D 1 286 ILE 286 288  288 ILE ILE A . n 
D 1 287 ASN 287 289  289 ASN ASN A . n 
D 1 288 THR 288 290  290 THR THR A . n 
D 1 289 SER 289 291  291 SER SER A . n 
D 1 290 LEU 290 292  292 LEU LEU A . n 
D 1 291 PRO 291 293  293 PRO PRO A . n 
D 1 292 PHE 292 294  294 PHE PHE A . n 
D 1 293 GLN 293 295  295 GLN GLN A . n 
D 1 294 ASN 294 296  296 ASN ASN A . n 
D 1 295 ILE 295 297  297 ILE ILE A . n 
D 1 296 HIS 296 298  298 HIS HIS A . n 
D 1 297 PRO 297 299  299 PRO PRO A . n 
D 1 298 ILE 298 300  300 ILE ILE A . n 
D 1 299 THR 299 301  301 THR THR A . n 
D 1 300 ILE 300 302  302 ILE ILE A . n 
D 1 301 GLY 301 303  303 GLY GLY A . n 
D 1 302 LYS 302 304  304 LYS LYS A . n 
D 1 303 CYS 303 305  305 CYS CYS A . n 
D 1 304 PRO 304 306  306 PRO PRO A . n 
D 1 305 LYS 305 307  307 LYS LYS A . n 
D 1 306 TYR 306 308  308 TYR TYR A . n 
D 1 307 VAL 307 309  309 VAL VAL A . n 
D 1 308 LYS 308 310  310 LYS LYS A . n 
D 1 309 SER 309 311  311 SER SER A . n 
D 1 310 THR 310 312  312 THR THR A . n 
D 1 311 LYS 311 313  313 LYS LYS A . n 
D 1 312 LEU 312 314  314 LEU LEU A . n 
D 1 313 ARG 313 315  315 ARG ARG A . n 
D 1 314 LEU 314 316  316 LEU LEU A . n 
D 1 315 ALA 315 317  317 ALA ALA A . n 
D 1 316 THR 316 318  318 THR THR A . n 
D 1 317 GLY 317 319  319 GLY GLY A . n 
D 1 318 LEU 318 320  320 LEU LEU A . n 
D 1 319 ARG 319 321  321 ARG ARG A . n 
D 1 320 ASN 320 322  322 ASN ASN A . n 
D 1 321 VAL 321 323  323 VAL VAL A . n 
D 1 322 PRO 322 324  324 PRO PRO A . n 
D 1 323 SER 323 325  325 SER SER A . n 
D 1 324 ILE 324 326  ?   ?   ?   A . n 
D 1 325 GLN 325 327  ?   ?   ?   A . n 
D 1 326 SER 326 328  ?   ?   ?   A . n 
D 1 327 ARG 327 329  ?   ?   ?   A . n 
D 1 328 GLY 328 330  ?   ?   ?   A . n 
D 1 329 LEU 329 331  ?   ?   ?   A . n 
D 1 330 PHE 330 332  ?   ?   ?   A . n 
D 1 331 GLY 331 333  ?   ?   ?   A . n 
D 1 332 ALA 332 334  ?   ?   ?   A . n 
D 1 333 ILE 333 335  ?   ?   ?   A . n 
D 1 334 ALA 334 336  ?   ?   ?   A . n 
D 1 335 GLY 335 337  ?   ?   ?   A . n 
D 1 336 PHE 336 338  ?   ?   ?   A . n 
D 1 337 ILE 337 339  ?   ?   ?   A . n 
D 1 338 GLU 338 340  ?   ?   ?   A . n 
D 1 339 GLY 339 341  ?   ?   ?   A . n 
D 1 340 GLY 340 342  ?   ?   ?   A . n 
D 1 341 TRP 341 343  ?   ?   ?   A . n 
D 1 342 THR 342 344  ?   ?   ?   A . n 
D 1 343 GLY 343 345  ?   ?   ?   A . n 
D 1 344 MET 344 346  ?   ?   ?   A . n 
D 1 345 VAL 345 347  ?   ?   ?   A . n 
D 1 346 ASP 346 348  ?   ?   ?   A . n 
D 1 347 GLY 347 349  ?   ?   ?   A . n 
D 1 348 TRP 348 350  ?   ?   ?   A . n 
D 1 349 TYR 349 351  ?   ?   ?   A . n 
D 1 350 GLY 350 352  ?   ?   ?   A . n 
D 1 351 TYR 351 353  ?   ?   ?   A . n 
D 1 352 HIS 352 354  ?   ?   ?   A . n 
D 1 353 HIS 353 355  ?   ?   ?   A . n 
D 1 354 GLN 354 356  ?   ?   ?   A . n 
D 1 355 ASN 355 357  ?   ?   ?   A . n 
D 1 356 GLU 356 358  ?   ?   ?   A . n 
D 1 357 GLN 357 359  ?   ?   ?   A . n 
D 1 358 GLY 358 360  ?   ?   ?   A . n 
D 1 359 SER 359 361  ?   ?   ?   A . n 
D 1 360 GLY 360 362  ?   ?   ?   A . n 
D 1 361 TYR 361 363  ?   ?   ?   A . n 
D 1 362 ALA 362 364  ?   ?   ?   A . n 
D 1 363 ALA 363 365  ?   ?   ?   A . n 
D 1 364 ASP 364 366  ?   ?   ?   A . n 
D 1 365 LEU 365 367  ?   ?   ?   A . n 
D 1 366 LYS 366 368  ?   ?   ?   A . n 
D 1 367 SER 367 369  ?   ?   ?   A . n 
D 1 368 THR 368 370  ?   ?   ?   A . n 
D 1 369 GLN 369 371  ?   ?   ?   A . n 
D 1 370 ASN 370 372  ?   ?   ?   A . n 
D 1 371 ALA 371 373  ?   ?   ?   A . n 
D 1 372 ILE 372 374  ?   ?   ?   A . n 
D 1 373 ASP 373 375  ?   ?   ?   A . n 
D 1 374 GLY 374 376  ?   ?   ?   A . n 
D 1 375 ILE 375 377  ?   ?   ?   A . n 
D 1 376 THR 376 378  ?   ?   ?   A . n 
D 1 377 ASN 377 379  ?   ?   ?   A . n 
D 1 378 LYS 378 380  ?   ?   ?   A . n 
D 1 379 VAL 379 381  ?   ?   ?   A . n 
D 1 380 ASN 380 382  ?   ?   ?   A . n 
D 1 381 SER 381 383  ?   ?   ?   A . n 
D 1 382 VAL 382 384  ?   ?   ?   A . n 
D 1 383 ILE 383 385  ?   ?   ?   A . n 
D 1 384 GLU 384 386  ?   ?   ?   A . n 
D 1 385 LYS 385 387  ?   ?   ?   A . n 
D 1 386 MET 386 388  ?   ?   ?   A . n 
D 1 387 ASN 387 389  ?   ?   ?   A . n 
D 1 388 THR 388 390  ?   ?   ?   A . n 
D 1 389 GLN 389 391  ?   ?   ?   A . n 
D 1 390 PHE 390 392  ?   ?   ?   A . n 
D 1 391 THR 391 393  ?   ?   ?   A . n 
D 1 392 ALA 392 394  ?   ?   ?   A . n 
D 1 393 VAL 393 395  ?   ?   ?   A . n 
D 1 394 GLY 394 396  ?   ?   ?   A . n 
D 1 395 LYS 395 397  ?   ?   ?   A . n 
D 1 396 GLU 396 398  ?   ?   ?   A . n 
D 1 397 PHE 397 399  ?   ?   ?   A . n 
D 1 398 ASN 398 400  ?   ?   ?   A . n 
D 1 399 HIS 399 401  ?   ?   ?   A . n 
D 1 400 LEU 400 402  ?   ?   ?   A . n 
D 1 401 GLU 401 403  ?   ?   ?   A . n 
D 1 402 LYS 402 404  ?   ?   ?   A . n 
D 1 403 ARG 403 405  ?   ?   ?   A . n 
D 1 404 ILE 404 406  ?   ?   ?   A . n 
D 1 405 GLU 405 407  ?   ?   ?   A . n 
D 1 406 ASN 406 408  ?   ?   ?   A . n 
D 1 407 LEU 407 409  ?   ?   ?   A . n 
D 1 408 ASN 408 410  ?   ?   ?   A . n 
D 1 409 LYS 409 411  ?   ?   ?   A . n 
D 1 410 LYS 410 412  ?   ?   ?   A . n 
D 1 411 VAL 411 413  ?   ?   ?   A . n 
D 1 412 ASP 412 414  ?   ?   ?   A . n 
D 1 413 ASP 413 415  ?   ?   ?   A . n 
D 1 414 GLY 414 416  ?   ?   ?   A . n 
D 1 415 PHE 415 417  ?   ?   ?   A . n 
D 1 416 LEU 416 418  ?   ?   ?   A . n 
D 1 417 ASP 417 419  ?   ?   ?   A . n 
D 1 418 ILE 418 420  ?   ?   ?   A . n 
D 1 419 TRP 419 421  ?   ?   ?   A . n 
D 1 420 THR 420 422  ?   ?   ?   A . n 
D 1 421 TYR 421 423  ?   ?   ?   A . n 
D 1 422 ASN 422 424  ?   ?   ?   A . n 
D 1 423 ALA 423 425  ?   ?   ?   A . n 
D 1 424 GLU 424 426  ?   ?   ?   A . n 
D 1 425 LEU 425 427  ?   ?   ?   A . n 
D 1 426 LEU 426 428  ?   ?   ?   A . n 
D 1 427 VAL 427 429  ?   ?   ?   A . n 
D 1 428 LEU 428 430  ?   ?   ?   A . n 
D 1 429 LEU 429 431  ?   ?   ?   A . n 
D 1 430 GLU 430 432  ?   ?   ?   A . n 
D 1 431 ASN 431 433  ?   ?   ?   A . n 
D 1 432 GLU 432 434  ?   ?   ?   A . n 
D 1 433 ARG 433 435  ?   ?   ?   A . n 
D 1 434 THR 434 436  ?   ?   ?   A . n 
D 1 435 LEU 435 437  ?   ?   ?   A . n 
D 1 436 ASP 436 438  ?   ?   ?   A . n 
D 1 437 TYR 437 439  ?   ?   ?   A . n 
D 1 438 HIS 438 440  ?   ?   ?   A . n 
D 1 439 ASP 439 441  ?   ?   ?   A . n 
D 1 440 SER 440 442  ?   ?   ?   A . n 
D 1 441 ASN 441 443  ?   ?   ?   A . n 
D 1 442 VAL 442 444  ?   ?   ?   A . n 
D 1 443 LYS 443 445  ?   ?   ?   A . n 
D 1 444 ASN 444 446  ?   ?   ?   A . n 
D 1 445 LEU 445 447  ?   ?   ?   A . n 
D 1 446 TYR 446 448  ?   ?   ?   A . n 
D 1 447 GLU 447 449  ?   ?   ?   A . n 
D 1 448 LYS 448 450  ?   ?   ?   A . n 
D 1 449 VAL 449 451  ?   ?   ?   A . n 
D 1 450 ARG 450 452  ?   ?   ?   A . n 
D 1 451 SER 451 453  ?   ?   ?   A . n 
D 1 452 GLN 452 454  ?   ?   ?   A . n 
D 1 453 LEU 453 455  ?   ?   ?   A . n 
D 1 454 LYS 454 456  ?   ?   ?   A . n 
D 1 455 ASN 455 457  ?   ?   ?   A . n 
D 1 456 ASN 456 458  ?   ?   ?   A . n 
D 1 457 ALA 457 459  ?   ?   ?   A . n 
D 1 458 LYS 458 460  ?   ?   ?   A . n 
D 1 459 GLU 459 461  ?   ?   ?   A . n 
D 1 460 ILE 460 462  ?   ?   ?   A . n 
D 1 461 GLY 461 463  ?   ?   ?   A . n 
D 1 462 ASN 462 464  ?   ?   ?   A . n 
D 1 463 GLY 463 465  ?   ?   ?   A . n 
D 1 464 CYS 464 466  ?   ?   ?   A . n 
D 1 465 PHE 465 467  ?   ?   ?   A . n 
D 1 466 GLU 466 468  ?   ?   ?   A . n 
D 1 467 PHE 467 469  ?   ?   ?   A . n 
D 1 468 TYR 468 470  ?   ?   ?   A . n 
D 1 469 HIS 469 471  ?   ?   ?   A . n 
D 1 470 LYS 470 472  ?   ?   ?   A . n 
D 1 471 CYS 471 473  ?   ?   ?   A . n 
D 1 472 ASP 472 474  ?   ?   ?   A . n 
D 1 473 ASN 473 475  ?   ?   ?   A . n 
D 1 474 THR 474 476  ?   ?   ?   A . n 
D 1 475 CYS 475 477  ?   ?   ?   A . n 
D 1 476 MET 476 478  ?   ?   ?   A . n 
D 1 477 GLU 477 479  ?   ?   ?   A . n 
D 1 478 SER 478 480  ?   ?   ?   A . n 
D 1 479 VAL 479 481  ?   ?   ?   A . n 
D 1 480 LYS 480 482  ?   ?   ?   A . n 
D 1 481 ASN 481 483  ?   ?   ?   A . n 
D 1 482 GLY 482 484  ?   ?   ?   A . n 
D 1 483 THR 483 485  ?   ?   ?   A . n 
D 1 484 TYR 484 486  ?   ?   ?   A . n 
D 1 485 ASP 485 487  ?   ?   ?   A . n 
D 1 486 TYR 486 488  ?   ?   ?   A . n 
D 1 487 PRO 487 489  ?   ?   ?   A . n 
D 1 488 LYS 488 490  ?   ?   ?   A . n 
D 1 489 TYR 489 491  ?   ?   ?   A . n 
D 1 490 SER 490 492  ?   ?   ?   A . n 
D 1 491 GLU 491 493  ?   ?   ?   A . n 
D 1 492 GLU 492 494  ?   ?   ?   A . n 
D 1 493 ALA 493 495  ?   ?   ?   A . n 
D 1 494 LYS 494 496  ?   ?   ?   A . n 
D 1 495 LEU 495 497  ?   ?   ?   A . n 
D 1 496 ASN 496 498  ?   ?   ?   A . n 
D 1 497 ARG 497 499  ?   ?   ?   A . n 
D 1 498 GLU 498 500  ?   ?   ?   A . n 
D 1 499 GLU 499 501  ?   ?   ?   A . n 
D 1 500 ILE 500 502  ?   ?   ?   A . n 
D 1 501 ASP 501 503  ?   ?   ?   A . n 
D 1 502 SER 502 504  ?   ?   ?   A . n 
D 1 503 GLY 503 505  ?   ?   ?   A . n 
D 1 504 ARG 504 506  ?   ?   ?   A . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
E 4 NAG 1 S NAG 1 S NAG 1 n 
E 4 NAG 2 S NAG 2 S NAG 2 n 
E 4 BMA 3 S BMA 3 S BMA 3 n 
F 5 NAG 1 C NAG 1 C NAG 1 n 
F 5 NAG 2 C NAG 2 C NAG 2 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 BMA ? ? BMA ? ? 'SUBJECT OF INVESTIGATION' ? 
2 NAG ? ? NAG ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
_pdbx_nonpoly_scheme.asym_id         G 
_pdbx_nonpoly_scheme.entity_id       6 
_pdbx_nonpoly_scheme.mon_id          NAG 
_pdbx_nonpoly_scheme.ndb_seq_num     1 
_pdbx_nonpoly_scheme.pdb_seq_num     601 
_pdbx_nonpoly_scheme.auth_seq_num    330 
_pdbx_nonpoly_scheme.pdb_mon_id      NAG 
_pdbx_nonpoly_scheme.auth_mon_id     NAG 
_pdbx_nonpoly_scheme.pdb_strand_id   A 
_pdbx_nonpoly_scheme.pdb_ins_code    . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 N 1 S NAG 1   ? O1 ? E NAG 1 O1 
2 1 N 1 C NAG 1   ? O1 ? F NAG 1 O1 
3 1 N 1 A NAG 601 ? O1 ? G NAG 1 O1 
# 
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   ? ? ? '(1.19.2_4158: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .                    4 
# 
_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                     9C0U 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     162.079 
_cell.length_a_esd                 ? 
_cell.length_b                     162.079 
_cell.length_b_esd                 ? 
_cell.length_c                     162.079 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        24 
_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                         9C0U 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                198 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 3' 
_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                   9C0U 
_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             2.19 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.86 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Tris, pH 8.5, 20% w/v PEG1000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 XE 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-05-25 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979 
_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                        'SSRL BEAMLINE BL12-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL12-2 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9C0U 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.59 
_reflns.d_resolution_low                               48.87 
_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                                     16876 
_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                                39.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    3.59 
_reflns_shell.d_res_low                                     3.61 
_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                             15949 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.52 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_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                                 9C0U 
_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                            3.59 
_refine.ls_d_res_low                             48.87 
_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                     15950 
_refine.ls_number_reflns_R_free                  788 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.63 
_refine.ls_percent_reflns_R_free                 4.94 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2967 
_refine.ls_R_factor_R_free                       0.3435 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2941 
_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            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_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                 44.41 
_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                            0.77 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       3.59 
_refine_hist.d_res_low                        48.87 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               7347 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        7266 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         81 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.005 ? 7447  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.827 ? 10115 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 7.402 ? 1011  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.050 ? 1123  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008 ? 1302  ? 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' 3.59 3.81  . . 116 2222 84.00  . . . . 0.4175 . . . . . . . . . . . 0.4059 
'X-RAY DIFFRACTION' 3.82 4.11  . . 129 2172 83.00  . . . . 0.3979 . . . . . . . . . . . 0.4422 
'X-RAY DIFFRACTION' 4.11 4.52  . . 123 2667 100.00 . . . . 0.3075 . . . . . . . . . . . 0.3520 
'X-RAY DIFFRACTION' 4.52 5.17  . . 130 2659 100.00 . . . . 0.2947 . . . . . . . . . . . 0.3694 
'X-RAY DIFFRACTION' 5.18 6.51  . . 144 2674 100.00 . . . . 0.3157 . . . . . . . . . . . 0.3784 
'X-RAY DIFFRACTION' 6.52 48.87 . . 146 2768 100.00 . . . . 0.2369 . . . . . . . . . . . 0.2832 
# 
_struct.entry_id                     9C0U 
_struct.title                        
'Crystal structure of chimeric hemagglutinin cH5/1 in complex with broad protective antibody 31.b.09' 
_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        9C0U 
_struct_keywords.text            'immune system, VIRAL PROTEIN-IMMUNE SYSTEM complex' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN/IMMUNE SYSTEM' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 1 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 PDB 9C0U 9C0U ? 1 ? 1 
2 PDB 9C0U 9C0U ? 2 ? 1 
3 PDB 9C0U 9C0U ? 3 ? 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 9C0U B 1 ? 504 ? 9C0U -326 ? 177 ? -326 177 
2 2 9C0U H 1 ? 224 ? 9C0U 1    ? 224 ? 1    224 
3 3 9C0U L 1 ? 218 ? 9C0U 1    ? 218 ? 1    218 
4 1 9C0U A 1 ? 504 ? 9C0U 10   ? 506 ? 10   506 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dodecameric 
_pdbx_struct_assembly.oligomeric_count     12 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,D,E,F,G 
1 2 A,B,C,D,E,F,G 
1 3 A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                monomer 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 5_555 z,x,y 0.0000000000 0.0000000000 1.0000000000 0.0000000000 1.0000000000 0.0000000000 
0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 
3 'crystal symmetry operation' 9_555 y,z,x 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 
1.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 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 ASP A 364 ? GLU A 384 ? ASP B 37  GLU B 57  1 ? 21 
HELX_P HELX_P2  AA2 ARG A 403 ? LEU A 416 ? ARG B 76  LEU B 89  1 ? 14 
HELX_P HELX_P3  AA3 ILE A 418 ? LYS A 454 ? ILE B 91  LYS B 127 1 ? 37 
HELX_P HELX_P4  AA4 ASP A 472 ? ASN A 481 ? ASP B 145 ASN B 154 1 ? 10 
HELX_P HELX_P5  AA5 ASP A 485 ? ASP A 501 ? ASP B 158 ASP B 174 1 ? 17 
HELX_P HELX_P6  AA6 GLU C 128 ? GLY C 133 ? GLU L 128 GLY L 133 1 ? 6  
HELX_P HELX_P7  AA7 LYS C 188 ? HIS C 194 ? LYS L 188 HIS L 194 1 ? 7  
HELX_P HELX_P8  AA8 SER D 57  ? GLY D 64  ? SER A 65  GLY A 72  1 ? 8  
HELX_P HELX_P9  AA9 ASP D 98  ? SER D 107 ? ASP A 104 SER A 113 1 ? 10 
HELX_P HELX_P10 AB1 LYS D 120 a SER D 125 ? LYS A 125 SER A 129 1 ? 6  
HELX_P HELX_P11 AB2 ASP D 184 ? TYR D 192 ? ASP A 187 TYR A 195 1 ? 9  
HELX_P HELX_P12 AB3 LYS D 219 ? GLN D 223 ? LYS A 222 GLN A 226 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ?    ? A CYS 464 SG ? ? ? 1_555 D CYS 5   SG ? ? B CYS 137 A CYS 14  1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf2 disulf ?    ? A CYS 471 SG ? ? ? 1_555 A CYS 475 SG ? ? B CYS 144 B CYS 148 1_555 ? ? ? ? ? ? ? 2.257 ? ? 
disulf3 disulf ?    ? B CYS 22  SG ? ? ? 1_555 B CYS 96  SG ? ? H CYS 22  H CYS 96  1_555 ? ? ? ? ? ? ? 2.026 ? ? 
disulf4 disulf ?    ? B CYS 149 SG ? ? ? 1_555 B CYS 205 SG ? ? H CYS 149 H CYS 205 1_555 ? ? ? ? ? ? ? 2.028 ? ? 
disulf5 disulf ?    ? C CYS 23  SG ? ? ? 1_555 C CYS 93  SG ? ? L CYS 23  L CYS 93  1_555 ? ? ? ? ? ? ? 2.027 ? ? 
disulf6 disulf ?    ? D CYS 43  SG ? ? ? 1_555 D CYS 275 SG ? ? A CYS 52  A CYS 277 1_555 ? ? ? ? ? ? ? 2.043 ? ? 
disulf7 disulf ?    ? D CYS 56  SG ? ? ? 1_555 D CYS 68  SG ? ? A CYS 64  A CYS 76  1_555 ? ? ? ? ? ? ? 2.008 ? ? 
covale1 covale both ? E NAG .   O4 ? ? ? 1_555 E NAG .   C1 ? ? S NAG 1   S NAG 2   1_555 ? ? ? ? ? ? ? 1.448 ? ? 
covale2 covale both ? E NAG .   O4 ? ? ? 1_555 E BMA .   C1 ? ? S NAG 2   S BMA 3   1_555 ? ? ? ? ? ? ? 1.438 ? ? 
covale3 covale both ? F NAG .   O4 ? ? ? 1_555 F NAG .   C1 ? ? C NAG 1   C NAG 2   1_555 ? ? ? ? ? ? ? 1.438 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 464 ? CYS D 5   ? CYS B 137 ? 1_555 CYS A 14  ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 471 ? CYS A 475 ? CYS B 144 ? 1_555 CYS B 148 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS B 22  ? CYS B 96  ? CYS H 22  ? 1_555 CYS H 96  ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS B 149 ? CYS B 205 ? CYS H 149 ? 1_555 CYS H 205 ? 1_555 SG SG . . . None 'Disulfide bridge' 
5 CYS C 23  ? CYS C 93  ? CYS L 23  ? 1_555 CYS L 93  ? 1_555 SG SG . . . None 'Disulfide bridge' 
6 CYS D 43  ? CYS D 275 ? CYS A 52  ? 1_555 CYS A 277 ? 1_555 SG SG . . . None 'Disulfide bridge' 
7 CYS D 56  ? CYS D 68  ? CYS A 64  ? 1_555 CYS A 76  ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 4 ? 
AA3 ? 5 ? 
AA4 ? 4 ? 
AA5 ? 3 ? 
AA6 ? 4 ? 
AA7 ? 5 ? 
AA8 ? 4 ? 
AA9 ? 3 ? 
AB1 ? 2 ? 
AB2 ? 2 ? 
AB3 ? 2 ? 
AB4 ? 3 ? 
AB5 ? 3 ? 
AB6 ? 2 ? 
AB7 ? 4 ? 
AB8 ? 4 ? 
AB9 ? 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 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB3 1 2 ? parallel      
AB4 1 2 ? parallel      
AB4 2 3 ? parallel      
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB9 1 2 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 SER A 359 ? ALA A 363 ? SER B 32  ALA B 36  
AA1 2 GLY A 350 ? GLN A 354 ? GLY B 23  GLN B 27  
AA1 3 THR D 3   ? GLY D 7   ? THR A 12  GLY A 16  
AA1 4 CYS A 464 ? PHE A 467 ? CYS B 137 PHE B 140 
AA1 5 ALA A 457 ? ILE A 460 ? ALA B 130 ILE B 133 
AA2 1 GLN B 3   ? GLN B 6   ? GLN H 3   GLN H 6   
AA2 2 VAL B 18  ? SER B 25  ? VAL H 18  SER H 25  
AA2 3 THR B 78  ? LEU B 83  ? THR H 78  LEU H 83  
AA2 4 VAL B 68  ? ASP B 73  ? VAL H 68  ASP H 73  
AA3 1 GLU B 10  ? LYS B 12  ? GLU H 10  LYS H 12  
AA3 2 THR B 116 ? VAL B 120 ? THR H 116 VAL H 120 
AA3 3 ALA B 92  ? ASP B 99  ? ALA H 92  ASP H 99  
AA3 4 GLY B 33  ? GLN B 39  ? GLY H 33  GLN H 39  
AA3 5 LEU B 45  ? ILE B 51  ? LEU H 45  ILE H 51  
AA4 1 SER B 129 ? PRO B 132 ? SER H 129 PRO H 132 
AA4 2 ALA B 145 ? LYS B 152 ? ALA H 145 LYS H 152 
AA4 3 TYR B 185 ? VAL B 193 ? TYR H 185 VAL H 193 
AA4 4 VAL B 178 ? LEU B 179 ? VAL H 178 LEU H 179 
AA5 1 THR B 160 ? TRP B 163 ? THR H 160 TRP H 163 
AA5 2 ILE B 204 ? ASN B 208 ? ILE H 204 ASN H 208 
AA5 3 LYS B 215 ? ARG B 219 ? LYS H 215 ARG H 219 
AA6 1 THR C 5   ? GLN C 6   ? THR L 5   GLN L 6   
AA6 2 ALA C 19  ? ARG C 24  ? ALA L 19  ARG L 24  
AA6 3 ASP C 75  ? ILE C 80  ? ASP L 75  ILE L 80  
AA6 4 PHE C 67  ? GLY C 71  ? PHE L 67  GLY L 71  
AA7 1 SER C 10  ? PRO C 12  ? SER L 10  PRO L 12  
AA7 2 GLY C 106 ? GLU C 110 ? GLY L 106 GLU L 110 
AA7 3 VAL C 90  ? TYR C 92  ? VAL L 90  TYR L 92  
AA7 4 PHE C 41  ? GLN C 43  ? PHE L 41  GLN L 43  
AA7 5 ARG C 50  ? ARG C 51  ? ARG L 50  ARG L 51  
AA8 1 VAL C 120 ? PHE C 123 ? VAL L 120 PHE L 123 
AA8 2 THR C 134 ? LEU C 141 ? THR L 134 LEU L 141 
AA8 3 LEU C 180 ? SER C 187 ? LEU L 180 SER L 187 
AA8 4 SER C 164 ? GLN C 165 ? SER L 164 GLN L 165 
AA9 1 LEU C 159 ? GLN C 160 ? LEU L 159 GLN L 160 
AA9 2 GLN C 152 ? VAL C 155 ? GLN L 152 VAL L 155 
AA9 3 TYR C 197 ? GLU C 200 ? TYR L 197 GLU L 200 
AB1 1 THR D 16  ? VAL D 17  ? THR A 25  VAL A 26  
AB1 2 VAL D 25  ? THR D 26  ? VAL A 34  THR A 35  
AB2 1 SER D 30  ? ASN D 32  ? SER A 39  ASN A 41  
AB2 2 ARG D 313 ? ALA D 315 ? ARG A 315 ALA A 317 
AB3 1 LEU D 42  ? ASP D 44  ? LEU A 51  ASP A 53  
AB3 2 TYR D 272 ? ASN D 276 ? TYR A 274 ASN A 278 
AB4 1 LEU D 51  ? ILE D 52  ? LEU A 59  ILE A 60  
AB4 2 ILE D 80  ? GLU D 82  ? ILE A 87  GLU A 89  
AB4 3 ILE D 265 ? LYS D 267 ? ILE A 267 LYS A 269 
AB5 1 HIS D 111 ? ILE D 115 ? HIS A 117 ILE A 121 
AB5 2 ALA D 254 ? VAL D 258 a ALA A 257 VAL A 260 
AB5 3 LEU D 173 ? LEU D 174 ? LEU A 176 LEU A 177 
AB6 1 GLU D 127 ? ALA D 128 ? GLU A 131 ALA A 132 
AB6 2 ILE D 152 ? LYS D 153 ? ILE A 155 LYS A 156 
AB7 1 VAL D 148 ? TRP D 150 ? VAL A 151 TRP A 153 
AB7 2 PHE D 248 ? PRO D 251 ? PHE A 251 PRO A 254 
AB7 3 GLY D 178 ? HIS D 181 ? GLY A 181 HIS A 184 
AB7 4 ARG D 226 ? PHE D 229 ? ARG A 229 PHE A 232 
AB8 1 ILE D 161 ? ARG D 163 ? ILE A 164 ARG A 166 
AB8 2 PHE D 242 ? SER D 244 ? PHE A 245 SER A 247 
AB8 3 ILE D 199 ? SER D 200 ? ILE A 202 SER A 203 
AB8 4 ARG D 209 ? LEU D 210 ? ARG A 212 LEU A 213 
AB9 1 PHE D 292 ? GLN D 293 ? PHE A 294 GLN A 295 
AB9 2 LYS D 305 ? TYR D 306 ? LYS A 307 TYR A 308 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 362 ? O ALA B 35  N TYR A 351 ? N TYR B 24  
AA1 2 3 N HIS A 352 ? N HIS B 25  O CYS D 5   ? O CYS A 14  
AA1 3 4 O LEU D 4   ? O LEU A 13  N PHE A 465 ? N PHE B 138 
AA1 4 5 O CYS A 464 ? O CYS B 137 N ILE A 460 ? N ILE B 133 
AA2 1 2 N VAL B 5   ? N VAL H 5   O LYS B 23  ? O LYS H 23  
AA2 2 3 N VAL B 20  ? N VAL H 20  O MET B 81  ? O MET H 81  
AA2 3 4 O THR B 78  ? O THR H 78  N ASP B 73  ? N ASP H 73  
AA3 1 2 N LYS B 12  ? N LYS H 12  O THR B 119 ? O THR H 119 
AA3 2 3 O VAL B 118 ? O VAL H 118 N ALA B 92  ? N ALA H 92  
AA3 3 4 O TYR B 95  ? O TYR H 95  N VAL B 37  ? N VAL H 37  
AA3 4 5 N ARG B 38  ? N ARG H 38  O GLU B 46  ? O GLU H 46  
AA4 1 2 N PHE B 131 ? N PHE H 131 O LEU B 150 ? O LEU H 150 
AA4 2 3 N VAL B 151 ? N VAL H 151 O LEU B 187 ? O LEU H 187 
AA4 3 4 O SER B 186 ? O SER H 186 N VAL B 178 ? N VAL H 178 
AA5 1 2 N SER B 162 ? N SER H 162 O ASN B 206 ? O ASN H 206 
AA5 2 3 N CYS B 205 ? N CYS H 205 O LYS B 218 ? O LYS H 218 
AA6 1 2 N THR C 5   ? N THR L 5   O ARG C 24  ? O ARG L 24  
AA6 2 3 N CYS C 23  ? N CYS L 23  O PHE C 76  ? O PHE L 76  
AA6 3 4 O THR C 77  ? O THR L 77  N SER C 70  ? N SER L 70  
AA7 1 2 N LEU C 11  ? N LEU L 11  O LYS C 108 ? O LYS L 108 
AA7 2 3 O THR C 107 ? O THR L 107 N TYR C 91  ? N TYR L 91  
AA7 3 4 O VAL C 90  ? O VAL L 90  N GLN C 43  ? N GLN L 43  
AA7 4 5 N GLN C 42  ? N GLN L 42  O ARG C 50  ? O ARG L 50  
AA8 1 2 N PHE C 121 ? N PHE L 121 O LEU C 140 ? O LEU L 140 
AA8 2 3 N ALA C 135 ? N ALA L 135 O LEU C 186 ? O LEU L 186 
AA8 3 4 O THR C 183 ? O THR L 183 N GLN C 165 ? N GLN L 165 
AA9 1 2 O GLN C 160 ? O GLN L 160 N TRP C 153 ? N TRP L 153 
AA9 2 3 N LYS C 154 ? N LYS L 154 O ALA C 198 ? O ALA L 198 
AB1 1 2 N VAL D 17  ? N VAL A 26  O VAL D 25  ? O VAL A 34  
AB2 1 2 N VAL D 31  ? N VAL A 40  O LEU D 314 ? O LEU A 316 
AB3 1 2 N ASP D 44  ? N ASP A 53  O CYS D 275 ? O CYS A 277 
AB4 1 2 N LEU D 51  ? N LEU A 59  O VAL D 81  ? O VAL A 88  
AB4 2 3 N GLU D 82  ? N GLU A 89  O MET D 266 ? O MET A 268 
AB5 1 2 N GLU D 113 ? N GLU A 119 O LYS D 256 ? O LYS A 259 
AB5 2 3 O TYR D 255 ? O TYR A 258 N LEU D 174 ? N LEU A 177 
AB6 1 2 N ALA D 128 ? N ALA A 132 O ILE D 152 ? O ILE A 155 
AB7 1 2 N VAL D 149 ? N VAL A 152 O ALA D 250 ? O ALA A 253 
AB7 2 3 O ILE D 249 ? O ILE A 252 N GLY D 178 ? N GLY A 181 
AB7 3 4 N HIS D 181 ? N HIS A 184 O ARG D 226 ? O ARG A 229 
AB8 1 2 N ARG D 163 ? N ARG A 166 O PHE D 242 ? O PHE A 245 
AB8 2 3 O GLU D 243 ? O GLU A 246 N SER D 200 ? N SER A 203 
AB8 3 4 N ILE D 199 ? N ILE A 202 O LEU D 210 ? O LEU A 213 
AB9 1 2 N GLN D 293 ? N GLN A 295 O LYS D 305 ? O LYS A 307 
# 
_pdbx_entry_details.entry_id                   9C0U 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   SG 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   CYS 
_pdbx_validate_close_contact.auth_seq_id_1    52 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   CYS 
_pdbx_validate_close_contact.auth_seq_id_2    277 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.89 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            PRO 
_pdbx_validate_rmsd_bond.auth_seq_id_1             198 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            N 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            PRO 
_pdbx_validate_rmsd_bond.auth_seq_id_2             198 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.376 
_pdbx_validate_rmsd_bond.bond_target_value         1.474 
_pdbx_validate_rmsd_bond.bond_deviation            -0.098 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.014 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 N  H ALA 123 ? ? CA H ALA 123 ? ? CB H ALA 123 ? ? 121.47 110.10 11.37  1.40 N 
2  1 CB L ARG 51  ? ? CA L ARG 51  ? ? C  L ARG 51  ? ? 96.43  110.40 -13.97 2.00 N 
3  1 N  L LEU 52  ? ? CA L LEU 52  ? ? CB L LEU 52  ? ? 97.74  110.40 -12.66 2.00 N 
4  1 N  L PRO 100 ? ? CA L PRO 100 ? ? C  L PRO 100 ? ? 95.86  112.10 -16.24 2.60 N 
5  1 CB L ASN 143 ? ? CA L ASN 143 ? ? C  L ASN 143 ? ? 92.05  110.40 -18.35 2.00 N 
6  1 O  L CYS 199 ? ? C  L CYS 199 ? ? N  L GLU 200 ? ? 136.12 122.70 13.42  1.60 Y 
7  1 N  A ASP 55  ? ? CA A ASP 55  ? ? CB A ASP 55  ? ? 122.38 110.60 11.78  1.80 N 
8  1 N  A GLU 131 ? ? CA A GLU 131 ? ? CB A GLU 131 ? ? 97.55  110.60 -13.05 1.80 N 
9  1 CB A GLN 142 ? ? CA A GLN 142 ? ? C  A GLN 142 ? ? 129.06 110.40 18.66  2.00 N 
10 1 N  A ASN 170 ? ? CA A ASN 170 ? ? C  A ASN 170 ? ? 92.38  111.00 -18.62 2.70 N 
11 1 N  A THR 171 ? ? CA A THR 171 ? ? C  A THR 171 ? ? 88.15  111.00 -22.85 2.70 N 
12 1 CB A PRO 254 ? ? CA A PRO 254 ? ? C  A PRO 254 ? ? 97.04  111.70 -14.66 2.10 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 HIS B 72  ? ? 66.71   -0.82   
2  1 ASP B 90  ? ? 72.48   -11.70  
3  1 LYS B 127 ? ? 53.26   -134.75 
4  1 ASN B 154 ? ? -68.93  1.75    
5  1 SER H 25  ? ? -168.86 -168.78 
6  1 PHE H 29  ? ? -102.98 53.75   
7  1 SER H 31  ? ? 59.75   2.99    
8  1 ASN H 55  ? ? -132.87 -156.07 
9  1 LYS H 138 ? ? 64.24   -3.11   
10 1 SER H 139 ? ? 57.52   -138.23 
11 1 ASN L 39  ? ? -53.23  109.07  
12 1 LEU L 52  ? ? -115.42 -80.11  
13 1 ASN L 55  ? ? 58.21   -127.62 
14 1 GLU L 84  ? ? -102.79 -157.21 
15 1 LYS L 112 ? ? -145.26 -157.71 
16 1 VAL L 151 ? ? -69.67  99.87   
17 1 THR L 177 ? ? -163.83 93.26   
18 1 SER L 181 ? ? -150.98 66.27   
19 1 PHE L 214 ? ? 61.17   66.01   
20 1 ASN L 215 ? ? -59.57  172.41  
21 1 ASN A 20  ? ? -126.48 -156.43 
22 1 ASP A 55  ? ? -146.45 46.90   
23 1 ARG A 62  ? ? 40.36   -123.73 
24 1 ILE A 80  ? ? -127.80 -64.80  
25 1 ASN A 81  ? ? -98.80  35.53   
26 1 PRO A 83  ? ? -64.65  -173.44 
27 1 CYS A 97  ? ? 53.91   9.38    
28 1 TYR A 98  ? ? 67.50   164.50  
29 1 ASP A 104 ? ? 38.11   44.15   
30 1 GLU A 131 ? ? -125.69 -160.52 
31 1 GLN A 142 ? ? -139.65 -56.35  
32 1 GLU A 174 ? ? -170.15 148.32  
33 1 THR A 206 ? ? -119.64 -159.20 
34 1 ILE A 217 ? ? -102.44 77.17   
35 1 ALA A 218 ? ? -168.11 116.82  
36 1 THR A 219 ? ? -142.76 -157.76 
37 1 ARG A 220 ? ? -118.42 -157.04 
38 1 SER A 265 ? ? -160.30 -167.77 
39 1 THR A 266 ? ? -163.44 -168.81 
40 1 ASN A 276 ? ? -103.03 66.76   
41 1 THR A 290 ? ? -116.14 -154.93 
42 1 CYS A 305 ? ? -177.30 125.11  
# 
_pdbx_validate_chiral.id              1 
_pdbx_validate_chiral.PDB_model_num   1 
_pdbx_validate_chiral.auth_atom_id    C1 
_pdbx_validate_chiral.label_alt_id    ? 
_pdbx_validate_chiral.auth_asym_id    S 
_pdbx_validate_chiral.auth_comp_id    NAG 
_pdbx_validate_chiral.auth_seq_id     2 
_pdbx_validate_chiral.PDB_ins_code    ? 
_pdbx_validate_chiral.details         'WRONG HAND' 
_pdbx_validate_chiral.omega           . 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG B 76  ? ? 0.203 'SIDE CHAIN' 
2 1 ARG H 98  ? ? 0.230 'SIDE CHAIN' 
3 1 ARG L 50  ? ? 0.126 'SIDE CHAIN' 
4 1 ARG L 51  ? ? 0.131 'SIDE CHAIN' 
5 1 ARG L 113 ? ? 0.283 'SIDE CHAIN' 
6 1 ARG A 216 ? ? 0.088 'SIDE CHAIN' 
# 
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 B GLY -326 ? A GLY 1   
2   1 Y 1 B ASP -325 ? A ASP 2   
3   1 Y 1 B THR -324 ? A THR 3   
4   1 Y 1 B LEU -323 ? A LEU 4   
5   1 Y 1 B CYS -322 ? A CYS 5   
6   1 Y 1 B ILE -321 ? A ILE 6   
7   1 Y 1 B GLY -320 ? A GLY 7   
8   1 Y 1 B TYR -319 ? A TYR 8   
9   1 Y 1 B HIS -318 ? A HIS 9   
10  1 Y 1 B ALA -317 ? A ALA 10  
11  1 Y 1 B ASN -316 ? A ASN 11  
12  1 Y 1 B ASN -315 ? A ASN 12  
13  1 Y 1 B SER -314 ? A SER 13  
14  1 Y 1 B THR -313 ? A THR 14  
15  1 Y 1 B ASP -312 ? A ASP 15  
16  1 Y 1 B THR -311 ? A THR 16  
17  1 Y 1 B VAL -310 ? A VAL 17  
18  1 Y 1 B ASP -309 ? A ASP 18  
19  1 Y 1 B THR -308 ? A THR 19  
20  1 Y 1 B VAL -307 ? A VAL 20  
21  1 Y 1 B LEU -306 ? A LEU 21  
22  1 Y 1 B GLU -305 ? A GLU 22  
23  1 Y 1 B LYS -304 ? A LYS 23  
24  1 Y 1 B ASN -303 ? A ASN 24  
25  1 Y 1 B VAL -302 ? A VAL 25  
26  1 Y 1 B THR -301 ? A THR 26  
27  1 Y 1 B VAL -300 ? A VAL 27  
28  1 Y 1 B THR -299 ? A THR 28  
29  1 Y 1 B HIS -298 ? A HIS 29  
30  1 Y 1 B SER -297 ? A SER 30  
31  1 Y 1 B VAL -296 ? A VAL 31  
32  1 Y 1 B ASN -295 ? A ASN 32  
33  1 Y 1 B LEU -294 ? A LEU 33  
34  1 Y 1 B LEU -293 ? A LEU 34  
35  1 Y 1 B GLU -292 ? A GLU 35  
36  1 Y 1 B ASP -291 ? A ASP 36  
37  1 Y 1 B LYS -290 ? A LYS 37  
38  1 Y 1 B HIS -289 ? A HIS 38  
39  1 Y 1 B ASN -288 ? A ASN 39  
40  1 Y 1 B GLY -287 ? A GLY 40  
41  1 Y 1 B LYS -286 ? A LYS 41  
42  1 Y 1 B LEU -285 ? A LEU 42  
43  1 Y 1 B CYS -284 ? A CYS 43  
44  1 Y 1 B ASP -283 ? A ASP 44  
45  1 Y 1 B LEU -282 ? A LEU 45  
46  1 Y 1 B ASP -281 ? A ASP 46  
47  1 Y 1 B GLY -280 ? A GLY 47  
48  1 Y 1 B VAL -279 ? A VAL 48  
49  1 Y 1 B LYS -278 ? A LYS 49  
50  1 Y 1 B PRO -277 ? A PRO 50  
51  1 Y 1 B LEU -276 ? A LEU 51  
52  1 Y 1 B ILE -275 ? A ILE 52  
53  1 Y 1 B LEU -274 ? A LEU 53  
54  1 Y 1 B ARG -273 ? A ARG 54  
55  1 Y 1 B ASP -272 ? A ASP 55  
56  1 Y 1 B CYS -271 ? A CYS 56  
57  1 Y 1 B SER -270 ? A SER 57  
58  1 Y 1 B VAL -269 ? A VAL 58  
59  1 Y 1 B ALA -268 ? A ALA 59  
60  1 Y 1 B GLY -267 ? A GLY 60  
61  1 Y 1 B TRP -266 ? A TRP 61  
62  1 Y 1 B LEU -265 ? A LEU 62  
63  1 Y 1 B LEU -264 ? A LEU 63  
64  1 Y 1 B GLY -263 ? A GLY 64  
65  1 Y 1 B ASN -262 ? A ASN 65  
66  1 Y 1 B PRO -261 ? A PRO 66  
67  1 Y 1 B MET -260 ? A MET 67  
68  1 Y 1 B CYS -259 ? A CYS 68  
69  1 Y 1 B ASP -258 ? A ASP 69  
70  1 Y 1 B GLU -257 ? A GLU 70  
71  1 Y 1 B PHE -256 ? A PHE 71  
72  1 Y 1 B ILE -255 ? A ILE 72  
73  1 Y 1 B ASN -254 ? A ASN 73  
74  1 Y 1 B VAL -253 ? A VAL 74  
75  1 Y 1 B PRO -252 ? A PRO 75  
76  1 Y 1 B GLU -251 ? A GLU 76  
77  1 Y 1 B TRP -250 ? A TRP 77  
78  1 Y 1 B SER -249 ? A SER 78  
79  1 Y 1 B TYR -248 ? A TYR 79  
80  1 Y 1 B ILE -247 ? A ILE 80  
81  1 Y 1 B VAL -246 ? A VAL 81  
82  1 Y 1 B GLU -245 ? A GLU 82  
83  1 Y 1 B LYS -244 ? A LYS 83  
84  1 Y 1 B ALA -243 ? A ALA 84  
85  1 Y 1 B ASN -242 ? A ASN 85  
86  1 Y 1 B PRO -241 ? A PRO 86  
87  1 Y 1 B VAL -240 ? A VAL 87  
88  1 Y 1 B ASN -239 ? A ASN 88  
89  1 Y 1 B ASP -238 ? A ASP 89  
90  1 Y 1 B LEU -237 ? A LEU 90  
91  1 Y 1 B CYS -236 ? A CYS 91  
92  1 Y 1 B TYR -235 ? A TYR 92  
93  1 Y 1 B PRO -234 ? A PRO 93  
94  1 Y 1 B GLY -233 ? A GLY 94  
95  1 Y 1 B ASP -232 ? A ASP 95  
96  1 Y 1 B PHE -231 ? A PHE 96  
97  1 Y 1 B ASN -230 ? A ASN 97  
98  1 Y 1 B ASP -229 ? A ASP 98  
99  1 Y 1 B TYR -228 ? A TYR 99  
100 1 Y 1 B GLU -227 ? A GLU 100 
101 1 Y 1 B GLU -226 ? A GLU 101 
102 1 Y 1 B LEU -225 ? A LEU 102 
103 1 Y 1 B LYS -224 ? A LYS 103 
104 1 Y 1 B HIS -223 ? A HIS 104 
105 1 Y 1 B LEU -222 ? A LEU 105 
106 1 Y 1 B LEU -221 ? A LEU 106 
107 1 Y 1 B SER -220 ? A SER 107 
108 1 Y 1 B ARG -219 ? A ARG 108 
109 1 Y 1 B ILE -218 ? A ILE 109 
110 1 Y 1 B ASN -217 ? A ASN 110 
111 1 Y 1 B HIS -216 ? A HIS 111 
112 1 Y 1 B PHE -215 ? A PHE 112 
113 1 Y 1 B GLU -214 ? A GLU 113 
114 1 Y 1 B LYS -213 ? A LYS 114 
115 1 Y 1 B ILE -212 ? A ILE 115 
116 1 Y 1 B GLN -211 ? A GLN 116 
117 1 Y 1 B ILE -210 ? A ILE 117 
118 1 Y 1 B ILE -209 ? A ILE 118 
119 1 Y 1 B PRO -208 ? A PRO 119 
120 1 Y 1 B LYS -207 ? A LYS 120 
121 1 Y 1 B SER -206 ? A SER 121 
122 1 Y 1 B SER -205 ? A SER 122 
123 1 Y 1 B TRP -204 ? A TRP 123 
124 1 Y 1 B SER -203 ? A SER 124 
125 1 Y 1 B SER -202 ? A SER 125 
126 1 Y 1 B HIS -201 ? A HIS 126 
127 1 Y 1 B GLU -200 ? A GLU 127 
128 1 Y 1 B ALA -199 ? A ALA 128 
129 1 Y 1 B SER -198 ? A SER 129 
130 1 Y 1 B LEU -197 ? A LEU 130 
131 1 Y 1 B GLY -196 ? A GLY 131 
132 1 Y 1 B VAL -195 ? A VAL 132 
133 1 Y 1 B SER -194 ? A SER 133 
134 1 Y 1 B SER -193 ? A SER 134 
135 1 Y 1 B ALA -192 ? A ALA 135 
136 1 Y 1 B CYS -191 ? A CYS 136 
137 1 Y 1 B PRO -190 ? A PRO 137 
138 1 Y 1 B TYR -189 ? A TYR 138 
139 1 Y 1 B GLN -188 ? A GLN 139 
140 1 Y 1 B GLY -187 ? A GLY 140 
141 1 Y 1 B LYS -186 ? A LYS 141 
142 1 Y 1 B SER -185 ? A SER 142 
143 1 Y 1 B SER -184 ? A SER 143 
144 1 Y 1 B PHE -183 ? A PHE 144 
145 1 Y 1 B PHE -182 ? A PHE 145 
146 1 Y 1 B ARG -181 ? A ARG 146 
147 1 Y 1 B ASN -180 ? A ASN 147 
148 1 Y 1 B VAL -179 ? A VAL 148 
149 1 Y 1 B VAL -178 ? A VAL 149 
150 1 Y 1 B TRP -177 ? A TRP 150 
151 1 Y 1 B LEU -176 ? A LEU 151 
152 1 Y 1 B ILE -175 ? A ILE 152 
153 1 Y 1 B LYS -174 ? A LYS 153 
154 1 Y 1 B LYS -173 ? A LYS 154 
155 1 Y 1 B ASN -172 ? A ASN 155 
156 1 Y 1 B SER -171 ? A SER 156 
157 1 Y 1 B THR -170 ? A THR 157 
158 1 Y 1 B TYR -169 ? A TYR 158 
159 1 Y 1 B PRO -168 ? A PRO 159 
160 1 Y 1 B THR -167 ? A THR 160 
161 1 Y 1 B ILE -166 ? A ILE 161 
162 1 Y 1 B LYS -165 ? A LYS 162 
163 1 Y 1 B ARG -164 ? A ARG 163 
164 1 Y 1 B SER -163 ? A SER 164 
165 1 Y 1 B TYR -162 ? A TYR 165 
166 1 Y 1 B ASN -161 ? A ASN 166 
167 1 Y 1 B ASN -160 ? A ASN 167 
168 1 Y 1 B THR -159 ? A THR 168 
169 1 Y 1 B ASN -158 ? A ASN 169 
170 1 Y 1 B GLN -157 ? A GLN 170 
171 1 Y 1 B GLU -156 ? A GLU 171 
172 1 Y 1 B ASP -155 ? A ASP 172 
173 1 Y 1 B LEU -154 ? A LEU 173 
174 1 Y 1 B LEU -153 ? A LEU 174 
175 1 Y 1 B VAL -152 ? A VAL 175 
176 1 Y 1 B LEU -151 ? A LEU 176 
177 1 Y 1 B TRP -150 ? A TRP 177 
178 1 Y 1 B GLY -149 ? A GLY 178 
179 1 Y 1 B ILE -148 ? A ILE 179 
180 1 Y 1 B HIS -147 ? A HIS 180 
181 1 Y 1 B HIS -146 ? A HIS 181 
182 1 Y 1 B PRO -145 ? A PRO 182 
183 1 Y 1 B ASN -144 ? A ASN 183 
184 1 Y 1 B ASP -143 ? A ASP 184 
185 1 Y 1 B ALA -142 ? A ALA 185 
186 1 Y 1 B ALA -141 ? A ALA 186 
187 1 Y 1 B GLU -140 ? A GLU 187 
188 1 Y 1 B GLN -139 ? A GLN 188 
189 1 Y 1 B THR -138 ? A THR 189 
190 1 Y 1 B LYS -137 ? A LYS 190 
191 1 Y 1 B LEU -136 ? A LEU 191 
192 1 Y 1 B TYR -135 ? A TYR 192 
193 1 Y 1 B GLN -134 ? A GLN 193 
194 1 Y 1 B ASN -133 ? A ASN 194 
195 1 Y 1 B PRO -132 ? A PRO 195 
196 1 Y 1 B THR -131 ? A THR 196 
197 1 Y 1 B THR -130 ? A THR 197 
198 1 Y 1 B TYR -129 ? A TYR 198 
199 1 Y 1 B ILE -128 ? A ILE 199 
200 1 Y 1 B SER -127 ? A SER 200 
201 1 Y 1 B VAL -126 ? A VAL 201 
202 1 Y 1 B GLY -125 ? A GLY 202 
203 1 Y 1 B THR -124 ? A THR 203 
204 1 Y 1 B SER -123 ? A SER 204 
205 1 Y 1 B THR -122 ? A THR 205 
206 1 Y 1 B LEU -121 ? A LEU 206 
207 1 Y 1 B ASN -120 ? A ASN 207 
208 1 Y 1 B GLN -119 ? A GLN 208 
209 1 Y 1 B ARG -118 ? A ARG 209 
210 1 Y 1 B LEU -117 ? A LEU 210 
211 1 Y 1 B VAL -116 ? A VAL 211 
212 1 Y 1 B PRO -115 ? A PRO 212 
213 1 Y 1 B ARG -114 ? A ARG 213 
214 1 Y 1 B ILE -113 ? A ILE 214 
215 1 Y 1 B ALA -112 ? A ALA 215 
216 1 Y 1 B THR -111 ? A THR 216 
217 1 Y 1 B ARG -110 ? A ARG 217 
218 1 Y 1 B SER -109 ? A SER 218 
219 1 Y 1 B LYS -108 ? A LYS 219 
220 1 Y 1 B VAL -107 ? A VAL 220 
221 1 Y 1 B ASN -106 ? A ASN 221 
222 1 Y 1 B GLY -105 ? A GLY 222 
223 1 Y 1 B GLN -104 ? A GLN 223 
224 1 Y 1 B SER -103 ? A SER 224 
225 1 Y 1 B GLY -102 ? A GLY 225 
226 1 Y 1 B ARG -101 ? A ARG 226 
227 1 Y 1 B MET -100 ? A MET 227 
228 1 Y 1 B GLU -99  ? A GLU 228 
229 1 Y 1 B PHE -98  ? A PHE 229 
230 1 Y 1 B PHE -97  ? A PHE 230 
231 1 Y 1 B TRP -96  ? A TRP 231 
232 1 Y 1 B THR -95  ? A THR 232 
233 1 Y 1 B ILE -94  ? A ILE 233 
234 1 Y 1 B LEU -93  ? A LEU 234 
235 1 Y 1 B LYS -92  ? A LYS 235 
236 1 Y 1 B PRO -91  ? A PRO 236 
237 1 Y 1 B ASN -90  ? A ASN 237 
238 1 Y 1 B ASP -89  ? A ASP 238 
239 1 Y 1 B ALA -88  ? A ALA 239 
240 1 Y 1 B ILE -87  ? A ILE 240 
241 1 Y 1 B ASN -86  ? A ASN 241 
242 1 Y 1 B PHE -85  ? A PHE 242 
243 1 Y 1 B GLU -84  ? A GLU 243 
244 1 Y 1 B SER -83  ? A SER 244 
245 1 Y 1 B ASN -82  ? A ASN 245 
246 1 Y 1 B GLY -81  ? A GLY 246 
247 1 Y 1 B ASN -80  ? A ASN 247 
248 1 Y 1 B PHE -79  ? A PHE 248 
249 1 Y 1 B ILE -78  ? A ILE 249 
250 1 Y 1 B ALA -77  ? A ALA 250 
251 1 Y 1 B PRO -76  ? A PRO 251 
252 1 Y 1 B GLU -75  ? A GLU 252 
253 1 Y 1 B TYR -74  ? A TYR 253 
254 1 Y 1 B ALA -73  ? A ALA 254 
255 1 Y 1 B TYR -72  ? A TYR 255 
256 1 Y 1 B LYS -71  ? A LYS 256 
257 1 Y 1 B ILE -70  ? A ILE 257 
258 1 Y 1 B VAL -69  ? A VAL 258 
259 1 Y 1 B LYS -68  ? A LYS 259 
260 1 Y 1 B LYS -67  ? A LYS 260 
261 1 Y 1 B GLY -66  ? A GLY 261 
262 1 Y 1 B ASP -65  ? A ASP 262 
263 1 Y 1 B SER -64  ? A SER 263 
264 1 Y 1 B THR -63  ? A THR 264 
265 1 Y 1 B ILE -62  ? A ILE 265 
266 1 Y 1 B MET -61  ? A MET 266 
267 1 Y 1 B LYS -60  ? A LYS 267 
268 1 Y 1 B SER -59  ? A SER 268 
269 1 Y 1 B GLU -58  ? A GLU 269 
270 1 Y 1 B LEU -57  ? A LEU 270 
271 1 Y 1 B GLU -56  ? A GLU 271 
272 1 Y 1 B TYR -55  ? A TYR 272 
273 1 Y 1 B GLY -54  ? A GLY 273 
274 1 Y 1 B ASN -53  ? A ASN 274 
275 1 Y 1 B CYS -52  ? A CYS 275 
276 1 Y 1 B ASN -51  ? A ASN 276 
277 1 Y 1 B THR -50  ? A THR 277 
278 1 Y 1 B THR -49  ? A THR 278 
279 1 Y 1 B CYS -48  ? A CYS 279 
280 1 Y 1 B GLN -47  ? A GLN 280 
281 1 Y 1 B THR -46  ? A THR 281 
282 1 Y 1 B PRO -45  ? A PRO 282 
283 1 Y 1 B LYS -44  ? A LYS 283 
284 1 Y 1 B GLY -43  ? A GLY 284 
285 1 Y 1 B ALA -42  ? A ALA 285 
286 1 Y 1 B ILE -41  ? A ILE 286 
287 1 Y 1 B ASN -40  ? A ASN 287 
288 1 Y 1 B THR -39  ? A THR 288 
289 1 Y 1 B SER -38  ? A SER 289 
290 1 Y 1 B LEU -37  ? A LEU 290 
291 1 Y 1 B PRO -36  ? A PRO 291 
292 1 Y 1 B PHE -35  ? A PHE 292 
293 1 Y 1 B GLN -34  ? A GLN 293 
294 1 Y 1 B ASN -33  ? A ASN 294 
295 1 Y 1 B ILE -32  ? A ILE 295 
296 1 Y 1 B HIS -31  ? A HIS 296 
297 1 Y 1 B PRO -30  ? A PRO 297 
298 1 Y 1 B ILE -29  ? A ILE 298 
299 1 Y 1 B THR -28  ? A THR 299 
300 1 Y 1 B ILE -27  ? A ILE 300 
301 1 Y 1 B GLY -26  ? A GLY 301 
302 1 Y 1 B LYS -25  ? A LYS 302 
303 1 Y 1 B CYS -24  ? A CYS 303 
304 1 Y 1 B PRO -23  ? A PRO 304 
305 1 Y 1 B LYS -22  ? A LYS 305 
306 1 Y 1 B TYR -21  ? A TYR 306 
307 1 Y 1 B VAL -20  ? A VAL 307 
308 1 Y 1 B LYS -19  ? A LYS 308 
309 1 Y 1 B SER -18  ? A SER 309 
310 1 Y 1 B THR -17  ? A THR 310 
311 1 Y 1 B LYS -16  ? A LYS 311 
312 1 Y 1 B LEU -15  ? A LEU 312 
313 1 Y 1 B ARG -14  ? A ARG 313 
314 1 Y 1 B LEU -13  ? A LEU 314 
315 1 Y 1 B ALA -12  ? A ALA 315 
316 1 Y 1 B THR -11  ? A THR 316 
317 1 Y 1 B GLY -10  ? A GLY 317 
318 1 Y 1 B LEU -9   ? A LEU 318 
319 1 Y 1 B ARG -8   ? A ARG 319 
320 1 Y 1 B ASN -7   ? A ASN 320 
321 1 Y 1 B VAL -6   ? A VAL 321 
322 1 Y 1 B PRO -5   ? A PRO 322 
323 1 Y 1 B SER -4   ? A SER 323 
324 1 Y 1 B ILE -3   ? A ILE 324 
325 1 Y 1 B GLN -2   ? A GLN 325 
326 1 Y 1 B SER -1   ? A SER 326 
327 1 Y 1 B ARG 0    ? A ARG 327 
328 1 Y 1 B GLY 1    ? A GLY 328 
329 1 Y 1 B LEU 2    ? A LEU 329 
330 1 Y 1 B PHE 3    ? A PHE 330 
331 1 Y 1 B GLY 4    ? A GLY 331 
332 1 Y 1 B ALA 5    ? A ALA 332 
333 1 Y 1 B ILE 6    ? A ILE 333 
334 1 Y 1 B ALA 7    ? A ALA 334 
335 1 Y 1 B GLY 8    ? A GLY 335 
336 1 Y 1 B PHE 9    ? A PHE 336 
337 1 Y 1 B SER 175  ? A SER 502 
338 1 Y 1 B GLY 176  ? A GLY 503 
339 1 Y 1 B ARG 177  ? A ARG 504 
340 1 Y 1 A ILE 326  ? D ILE 324 
341 1 Y 1 A GLN 327  ? D GLN 325 
342 1 Y 1 A SER 328  ? D SER 326 
343 1 Y 1 A ARG 329  ? D ARG 327 
344 1 Y 1 A GLY 330  ? D GLY 328 
345 1 Y 1 A LEU 331  ? D LEU 329 
346 1 Y 1 A PHE 332  ? D PHE 330 
347 1 Y 1 A GLY 333  ? D GLY 331 
348 1 Y 1 A ALA 334  ? D ALA 332 
349 1 Y 1 A ILE 335  ? D ILE 333 
350 1 Y 1 A ALA 336  ? D ALA 334 
351 1 Y 1 A GLY 337  ? D GLY 335 
352 1 Y 1 A PHE 338  ? D PHE 336 
353 1 Y 1 A ILE 339  ? D ILE 337 
354 1 Y 1 A GLU 340  ? D GLU 338 
355 1 Y 1 A GLY 341  ? D GLY 339 
356 1 Y 1 A GLY 342  ? D GLY 340 
357 1 Y 1 A TRP 343  ? D TRP 341 
358 1 Y 1 A THR 344  ? D THR 342 
359 1 Y 1 A GLY 345  ? D GLY 343 
360 1 Y 1 A MET 346  ? D MET 344 
361 1 Y 1 A VAL 347  ? D VAL 345 
362 1 Y 1 A ASP 348  ? D ASP 346 
363 1 Y 1 A GLY 349  ? D GLY 347 
364 1 Y 1 A TRP 350  ? D TRP 348 
365 1 Y 1 A TYR 351  ? D TYR 349 
366 1 Y 1 A GLY 352  ? D GLY 350 
367 1 Y 1 A TYR 353  ? D TYR 351 
368 1 Y 1 A HIS 354  ? D HIS 352 
369 1 Y 1 A HIS 355  ? D HIS 353 
370 1 Y 1 A GLN 356  ? D GLN 354 
371 1 Y 1 A ASN 357  ? D ASN 355 
372 1 Y 1 A GLU 358  ? D GLU 356 
373 1 Y 1 A GLN 359  ? D GLN 357 
374 1 Y 1 A GLY 360  ? D GLY 358 
375 1 Y 1 A SER 361  ? D SER 359 
376 1 Y 1 A GLY 362  ? D GLY 360 
377 1 Y 1 A TYR 363  ? D TYR 361 
378 1 Y 1 A ALA 364  ? D ALA 362 
379 1 Y 1 A ALA 365  ? D ALA 363 
380 1 Y 1 A ASP 366  ? D ASP 364 
381 1 Y 1 A LEU 367  ? D LEU 365 
382 1 Y 1 A LYS 368  ? D LYS 366 
383 1 Y 1 A SER 369  ? D SER 367 
384 1 Y 1 A THR 370  ? D THR 368 
385 1 Y 1 A GLN 371  ? D GLN 369 
386 1 Y 1 A ASN 372  ? D ASN 370 
387 1 Y 1 A ALA 373  ? D ALA 371 
388 1 Y 1 A ILE 374  ? D ILE 372 
389 1 Y 1 A ASP 375  ? D ASP 373 
390 1 Y 1 A GLY 376  ? D GLY 374 
391 1 Y 1 A ILE 377  ? D ILE 375 
392 1 Y 1 A THR 378  ? D THR 376 
393 1 Y 1 A ASN 379  ? D ASN 377 
394 1 Y 1 A LYS 380  ? D LYS 378 
395 1 Y 1 A VAL 381  ? D VAL 379 
396 1 Y 1 A ASN 382  ? D ASN 380 
397 1 Y 1 A SER 383  ? D SER 381 
398 1 Y 1 A VAL 384  ? D VAL 382 
399 1 Y 1 A ILE 385  ? D ILE 383 
400 1 Y 1 A GLU 386  ? D GLU 384 
401 1 Y 1 A LYS 387  ? D LYS 385 
402 1 Y 1 A MET 388  ? D MET 386 
403 1 Y 1 A ASN 389  ? D ASN 387 
404 1 Y 1 A THR 390  ? D THR 388 
405 1 Y 1 A GLN 391  ? D GLN 389 
406 1 Y 1 A PHE 392  ? D PHE 390 
407 1 Y 1 A THR 393  ? D THR 391 
408 1 Y 1 A ALA 394  ? D ALA 392 
409 1 Y 1 A VAL 395  ? D VAL 393 
410 1 Y 1 A GLY 396  ? D GLY 394 
411 1 Y 1 A LYS 397  ? D LYS 395 
412 1 Y 1 A GLU 398  ? D GLU 396 
413 1 Y 1 A PHE 399  ? D PHE 397 
414 1 Y 1 A ASN 400  ? D ASN 398 
415 1 Y 1 A HIS 401  ? D HIS 399 
416 1 Y 1 A LEU 402  ? D LEU 400 
417 1 Y 1 A GLU 403  ? D GLU 401 
418 1 Y 1 A LYS 404  ? D LYS 402 
419 1 Y 1 A ARG 405  ? D ARG 403 
420 1 Y 1 A ILE 406  ? D ILE 404 
421 1 Y 1 A GLU 407  ? D GLU 405 
422 1 Y 1 A ASN 408  ? D ASN 406 
423 1 Y 1 A LEU 409  ? D LEU 407 
424 1 Y 1 A ASN 410  ? D ASN 408 
425 1 Y 1 A LYS 411  ? D LYS 409 
426 1 Y 1 A LYS 412  ? D LYS 410 
427 1 Y 1 A VAL 413  ? D VAL 411 
428 1 Y 1 A ASP 414  ? D ASP 412 
429 1 Y 1 A ASP 415  ? D ASP 413 
430 1 Y 1 A GLY 416  ? D GLY 414 
431 1 Y 1 A PHE 417  ? D PHE 415 
432 1 Y 1 A LEU 418  ? D LEU 416 
433 1 Y 1 A ASP 419  ? D ASP 417 
434 1 Y 1 A ILE 420  ? D ILE 418 
435 1 Y 1 A TRP 421  ? D TRP 419 
436 1 Y 1 A THR 422  ? D THR 420 
437 1 Y 1 A TYR 423  ? D TYR 421 
438 1 Y 1 A ASN 424  ? D ASN 422 
439 1 Y 1 A ALA 425  ? D ALA 423 
440 1 Y 1 A GLU 426  ? D GLU 424 
441 1 Y 1 A LEU 427  ? D LEU 425 
442 1 Y 1 A LEU 428  ? D LEU 426 
443 1 Y 1 A VAL 429  ? D VAL 427 
444 1 Y 1 A LEU 430  ? D LEU 428 
445 1 Y 1 A LEU 431  ? D LEU 429 
446 1 Y 1 A GLU 432  ? D GLU 430 
447 1 Y 1 A ASN 433  ? D ASN 431 
448 1 Y 1 A GLU 434  ? D GLU 432 
449 1 Y 1 A ARG 435  ? D ARG 433 
450 1 Y 1 A THR 436  ? D THR 434 
451 1 Y 1 A LEU 437  ? D LEU 435 
452 1 Y 1 A ASP 438  ? D ASP 436 
453 1 Y 1 A TYR 439  ? D TYR 437 
454 1 Y 1 A HIS 440  ? D HIS 438 
455 1 Y 1 A ASP 441  ? D ASP 439 
456 1 Y 1 A SER 442  ? D SER 440 
457 1 Y 1 A ASN 443  ? D ASN 441 
458 1 Y 1 A VAL 444  ? D VAL 442 
459 1 Y 1 A LYS 445  ? D LYS 443 
460 1 Y 1 A ASN 446  ? D ASN 444 
461 1 Y 1 A LEU 447  ? D LEU 445 
462 1 Y 1 A TYR 448  ? D TYR 446 
463 1 Y 1 A GLU 449  ? D GLU 447 
464 1 Y 1 A LYS 450  ? D LYS 448 
465 1 Y 1 A VAL 451  ? D VAL 449 
466 1 Y 1 A ARG 452  ? D ARG 450 
467 1 Y 1 A SER 453  ? D SER 451 
468 1 Y 1 A GLN 454  ? D GLN 452 
469 1 Y 1 A LEU 455  ? D LEU 453 
470 1 Y 1 A LYS 456  ? D LYS 454 
471 1 Y 1 A ASN 457  ? D ASN 455 
472 1 Y 1 A ASN 458  ? D ASN 456 
473 1 Y 1 A ALA 459  ? D ALA 457 
474 1 Y 1 A LYS 460  ? D LYS 458 
475 1 Y 1 A GLU 461  ? D GLU 459 
476 1 Y 1 A ILE 462  ? D ILE 460 
477 1 Y 1 A GLY 463  ? D GLY 461 
478 1 Y 1 A ASN 464  ? D ASN 462 
479 1 Y 1 A GLY 465  ? D GLY 463 
480 1 Y 1 A CYS 466  ? D CYS 464 
481 1 Y 1 A PHE 467  ? D PHE 465 
482 1 Y 1 A GLU 468  ? D GLU 466 
483 1 Y 1 A PHE 469  ? D PHE 467 
484 1 Y 1 A TYR 470  ? D TYR 468 
485 1 Y 1 A HIS 471  ? D HIS 469 
486 1 Y 1 A LYS 472  ? D LYS 470 
487 1 Y 1 A CYS 473  ? D CYS 471 
488 1 Y 1 A ASP 474  ? D ASP 472 
489 1 Y 1 A ASN 475  ? D ASN 473 
490 1 Y 1 A THR 476  ? D THR 474 
491 1 Y 1 A CYS 477  ? D CYS 475 
492 1 Y 1 A MET 478  ? D MET 476 
493 1 Y 1 A GLU 479  ? D GLU 477 
494 1 Y 1 A SER 480  ? D SER 478 
495 1 Y 1 A VAL 481  ? D VAL 479 
496 1 Y 1 A LYS 482  ? D LYS 480 
497 1 Y 1 A ASN 483  ? D ASN 481 
498 1 Y 1 A GLY 484  ? D GLY 482 
499 1 Y 1 A THR 485  ? D THR 483 
500 1 Y 1 A TYR 486  ? D TYR 484 
501 1 Y 1 A ASP 487  ? D ASP 485 
502 1 Y 1 A TYR 488  ? D TYR 486 
503 1 Y 1 A PRO 489  ? D PRO 487 
504 1 Y 1 A LYS 490  ? D LYS 488 
505 1 Y 1 A TYR 491  ? D TYR 489 
506 1 Y 1 A SER 492  ? D SER 490 
507 1 Y 1 A GLU 493  ? D GLU 491 
508 1 Y 1 A GLU 494  ? D GLU 492 
509 1 Y 1 A ALA 495  ? D ALA 493 
510 1 Y 1 A LYS 496  ? D LYS 494 
511 1 Y 1 A LEU 497  ? D LEU 495 
512 1 Y 1 A ASN 498  ? D ASN 496 
513 1 Y 1 A ARG 499  ? D ARG 497 
514 1 Y 1 A GLU 500  ? D GLU 498 
515 1 Y 1 A GLU 501  ? D GLU 499 
516 1 Y 1 A ILE 502  ? D ILE 500 
517 1 Y 1 A ASP 503  ? D ASP 501 
518 1 Y 1 A SER 504  ? D SER 502 
519 1 Y 1 A GLY 505  ? D GLY 503 
520 1 Y 1 A ARG 506  ? D ARG 504 
# 
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  
BMA C1   C N R 74  
BMA C2   C N S 75  
BMA C3   C N S 76  
BMA C4   C N S 77  
BMA C5   C N R 78  
BMA C6   C N N 79  
BMA O1   O N N 80  
BMA O2   O N N 81  
BMA O3   O N N 82  
BMA O4   O N N 83  
BMA O5   O N N 84  
BMA O6   O N N 85  
BMA H1   H N N 86  
BMA H2   H N N 87  
BMA H3   H N N 88  
BMA H4   H N N 89  
BMA H5   H N N 90  
BMA H61  H N N 91  
BMA H62  H N N 92  
BMA HO1  H N N 93  
BMA HO2  H N N 94  
BMA HO3  H N N 95  
BMA HO4  H N N 96  
BMA HO6  H N N 97  
CYS N    N N N 98  
CYS CA   C N R 99  
CYS C    C N N 100 
CYS O    O N N 101 
CYS CB   C N N 102 
CYS SG   S N N 103 
CYS OXT  O N N 104 
CYS H    H N N 105 
CYS H2   H N N 106 
CYS HA   H N N 107 
CYS HB2  H N N 108 
CYS HB3  H N N 109 
CYS HG   H N N 110 
CYS HXT  H N N 111 
GLN N    N N N 112 
GLN CA   C N S 113 
GLN C    C N N 114 
GLN O    O N N 115 
GLN CB   C N N 116 
GLN CG   C N N 117 
GLN CD   C N N 118 
GLN OE1  O N N 119 
GLN NE2  N N N 120 
GLN OXT  O N N 121 
GLN H    H N N 122 
GLN H2   H N N 123 
GLN HA   H N N 124 
GLN HB2  H N N 125 
GLN HB3  H N N 126 
GLN HG2  H N N 127 
GLN HG3  H N N 128 
GLN HE21 H N N 129 
GLN HE22 H N N 130 
GLN HXT  H N N 131 
GLU N    N N N 132 
GLU CA   C N S 133 
GLU C    C N N 134 
GLU O    O N N 135 
GLU CB   C N N 136 
GLU CG   C N N 137 
GLU CD   C N N 138 
GLU OE1  O N N 139 
GLU OE2  O N N 140 
GLU OXT  O N N 141 
GLU H    H N N 142 
GLU H2   H N N 143 
GLU HA   H N N 144 
GLU HB2  H N N 145 
GLU HB3  H N N 146 
GLU HG2  H N N 147 
GLU HG3  H N N 148 
GLU HE2  H N N 149 
GLU HXT  H N N 150 
GLY N    N N N 151 
GLY CA   C N N 152 
GLY C    C N N 153 
GLY O    O N N 154 
GLY OXT  O N N 155 
GLY H    H N N 156 
GLY H2   H N N 157 
GLY HA2  H N N 158 
GLY HA3  H N N 159 
GLY HXT  H N N 160 
HIS N    N N N 161 
HIS CA   C N S 162 
HIS C    C N N 163 
HIS O    O N N 164 
HIS CB   C N N 165 
HIS CG   C Y N 166 
HIS ND1  N Y N 167 
HIS CD2  C Y N 168 
HIS CE1  C Y N 169 
HIS NE2  N Y N 170 
HIS OXT  O N N 171 
HIS H    H N N 172 
HIS H2   H N N 173 
HIS HA   H N N 174 
HIS HB2  H N N 175 
HIS HB3  H N N 176 
HIS HD1  H N N 177 
HIS HD2  H N N 178 
HIS HE1  H N N 179 
HIS HE2  H N N 180 
HIS HXT  H N N 181 
ILE N    N N N 182 
ILE CA   C N S 183 
ILE C    C N N 184 
ILE O    O N N 185 
ILE CB   C N S 186 
ILE CG1  C N N 187 
ILE CG2  C N N 188 
ILE CD1  C N N 189 
ILE OXT  O N N 190 
ILE H    H N N 191 
ILE H2   H N N 192 
ILE HA   H N N 193 
ILE HB   H N N 194 
ILE HG12 H N N 195 
ILE HG13 H N N 196 
ILE HG21 H N N 197 
ILE HG22 H N N 198 
ILE HG23 H N N 199 
ILE HD11 H N N 200 
ILE HD12 H N N 201 
ILE HD13 H N N 202 
ILE HXT  H N N 203 
LEU N    N N N 204 
LEU CA   C N S 205 
LEU C    C N N 206 
LEU O    O N N 207 
LEU CB   C N N 208 
LEU CG   C N N 209 
LEU CD1  C N N 210 
LEU CD2  C N N 211 
LEU OXT  O N N 212 
LEU H    H N N 213 
LEU H2   H N N 214 
LEU HA   H N N 215 
LEU HB2  H N N 216 
LEU HB3  H N N 217 
LEU HG   H N N 218 
LEU HD11 H N N 219 
LEU HD12 H N N 220 
LEU HD13 H N N 221 
LEU HD21 H N N 222 
LEU HD22 H N N 223 
LEU HD23 H N N 224 
LEU HXT  H N N 225 
LYS N    N N N 226 
LYS CA   C N S 227 
LYS C    C N N 228 
LYS O    O N N 229 
LYS CB   C N N 230 
LYS CG   C N N 231 
LYS CD   C N N 232 
LYS CE   C N N 233 
LYS NZ   N N N 234 
LYS OXT  O N N 235 
LYS H    H N N 236 
LYS H2   H N N 237 
LYS HA   H N N 238 
LYS HB2  H N N 239 
LYS HB3  H N N 240 
LYS HG2  H N N 241 
LYS HG3  H N N 242 
LYS HD2  H N N 243 
LYS HD3  H N N 244 
LYS HE2  H N N 245 
LYS HE3  H N N 246 
LYS HZ1  H N N 247 
LYS HZ2  H N N 248 
LYS HZ3  H N N 249 
LYS HXT  H N N 250 
MET N    N N N 251 
MET CA   C N S 252 
MET C    C N N 253 
MET O    O N N 254 
MET CB   C N N 255 
MET CG   C N N 256 
MET SD   S N N 257 
MET CE   C N N 258 
MET OXT  O N N 259 
MET H    H N N 260 
MET H2   H N N 261 
MET HA   H N N 262 
MET HB2  H N N 263 
MET HB3  H N N 264 
MET HG2  H N N 265 
MET HG3  H N N 266 
MET HE1  H N N 267 
MET HE2  H N N 268 
MET HE3  H N N 269 
MET HXT  H N N 270 
NAG C1   C N R 271 
NAG C2   C N R 272 
NAG C3   C N R 273 
NAG C4   C N S 274 
NAG C5   C N R 275 
NAG C6   C N N 276 
NAG C7   C N N 277 
NAG C8   C N N 278 
NAG N2   N N N 279 
NAG O1   O N N 280 
NAG O3   O N N 281 
NAG O4   O N N 282 
NAG O5   O N N 283 
NAG O6   O N N 284 
NAG O7   O N N 285 
NAG H1   H N N 286 
NAG H2   H N N 287 
NAG H3   H N N 288 
NAG H4   H N N 289 
NAG H5   H N N 290 
NAG H61  H N N 291 
NAG H62  H N N 292 
NAG H81  H N N 293 
NAG H82  H N N 294 
NAG H83  H N N 295 
NAG HN2  H N N 296 
NAG HO1  H N N 297 
NAG HO3  H N N 298 
NAG HO4  H N N 299 
NAG HO6  H N N 300 
PHE N    N N N 301 
PHE CA   C N S 302 
PHE C    C N N 303 
PHE O    O N N 304 
PHE CB   C N N 305 
PHE CG   C Y N 306 
PHE CD1  C Y N 307 
PHE CD2  C Y N 308 
PHE CE1  C Y N 309 
PHE CE2  C Y N 310 
PHE CZ   C Y N 311 
PHE OXT  O N N 312 
PHE H    H N N 313 
PHE H2   H N N 314 
PHE HA   H N N 315 
PHE HB2  H N N 316 
PHE HB3  H N N 317 
PHE HD1  H N N 318 
PHE HD2  H N N 319 
PHE HE1  H N N 320 
PHE HE2  H N N 321 
PHE HZ   H N N 322 
PHE HXT  H N N 323 
PRO N    N N N 324 
PRO CA   C N S 325 
PRO C    C N N 326 
PRO O    O N N 327 
PRO CB   C N N 328 
PRO CG   C N N 329 
PRO CD   C N N 330 
PRO OXT  O N N 331 
PRO H    H N N 332 
PRO HA   H N N 333 
PRO HB2  H N N 334 
PRO HB3  H N N 335 
PRO HG2  H N N 336 
PRO HG3  H N N 337 
PRO HD2  H N N 338 
PRO HD3  H N N 339 
PRO HXT  H N N 340 
SER N    N N N 341 
SER CA   C N S 342 
SER C    C N N 343 
SER O    O N N 344 
SER CB   C N N 345 
SER OG   O N N 346 
SER OXT  O N N 347 
SER H    H N N 348 
SER H2   H N N 349 
SER HA   H N N 350 
SER HB2  H N N 351 
SER HB3  H N N 352 
SER HG   H N N 353 
SER HXT  H N N 354 
THR N    N N N 355 
THR CA   C N S 356 
THR C    C N N 357 
THR O    O N N 358 
THR CB   C N R 359 
THR OG1  O N N 360 
THR CG2  C N N 361 
THR OXT  O N N 362 
THR H    H N N 363 
THR H2   H N N 364 
THR HA   H N N 365 
THR HB   H N N 366 
THR HG1  H N N 367 
THR HG21 H N N 368 
THR HG22 H N N 369 
THR HG23 H N N 370 
THR HXT  H N N 371 
TRP N    N N N 372 
TRP CA   C N S 373 
TRP C    C N N 374 
TRP O    O N N 375 
TRP CB   C N N 376 
TRP CG   C Y N 377 
TRP CD1  C Y N 378 
TRP CD2  C Y N 379 
TRP NE1  N Y N 380 
TRP CE2  C Y N 381 
TRP CE3  C Y N 382 
TRP CZ2  C Y N 383 
TRP CZ3  C Y N 384 
TRP CH2  C Y N 385 
TRP OXT  O N N 386 
TRP H    H N N 387 
TRP H2   H N N 388 
TRP HA   H N N 389 
TRP HB2  H N N 390 
TRP HB3  H N N 391 
TRP HD1  H N N 392 
TRP HE1  H N N 393 
TRP HE3  H N N 394 
TRP HZ2  H N N 395 
TRP HZ3  H N N 396 
TRP HH2  H N N 397 
TRP HXT  H N N 398 
TYR N    N N N 399 
TYR CA   C N S 400 
TYR C    C N N 401 
TYR O    O N N 402 
TYR CB   C N N 403 
TYR CG   C Y N 404 
TYR CD1  C Y N 405 
TYR CD2  C Y N 406 
TYR CE1  C Y N 407 
TYR CE2  C Y N 408 
TYR CZ   C Y N 409 
TYR OH   O N N 410 
TYR OXT  O N N 411 
TYR H    H N N 412 
TYR H2   H N N 413 
TYR HA   H N N 414 
TYR HB2  H N N 415 
TYR HB3  H N N 416 
TYR HD1  H N N 417 
TYR HD2  H N N 418 
TYR HE1  H N N 419 
TYR HE2  H N N 420 
TYR HH   H N N 421 
TYR HXT  H N N 422 
VAL N    N N N 423 
VAL CA   C N S 424 
VAL C    C N N 425 
VAL O    O N N 426 
VAL CB   C N N 427 
VAL CG1  C N N 428 
VAL CG2  C N N 429 
VAL OXT  O N N 430 
VAL H    H N N 431 
VAL H2   H N N 432 
VAL HA   H N N 433 
VAL HB   H N N 434 
VAL HG11 H N N 435 
VAL HG12 H N N 436 
VAL HG13 H N N 437 
VAL HG21 H N N 438 
VAL HG22 H N N 439 
VAL HG23 H N N 440 
VAL HXT  H N N 441 
# 
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  
BMA C1  C2   sing N N 70  
BMA C1  O1   sing N N 71  
BMA C1  O5   sing N N 72  
BMA C1  H1   sing N N 73  
BMA C2  C3   sing N N 74  
BMA C2  O2   sing N N 75  
BMA C2  H2   sing N N 76  
BMA C3  C4   sing N N 77  
BMA C3  O3   sing N N 78  
BMA C3  H3   sing N N 79  
BMA C4  C5   sing N N 80  
BMA C4  O4   sing N N 81  
BMA C4  H4   sing N N 82  
BMA C5  C6   sing N N 83  
BMA C5  O5   sing N N 84  
BMA C5  H5   sing N N 85  
BMA C6  O6   sing N N 86  
BMA C6  H61  sing N N 87  
BMA C6  H62  sing N N 88  
BMA O1  HO1  sing N N 89  
BMA O2  HO2  sing N N 90  
BMA O3  HO3  sing N N 91  
BMA O4  HO4  sing N N 92  
BMA O6  HO6  sing N N 93  
CYS N   CA   sing N N 94  
CYS N   H    sing N N 95  
CYS N   H2   sing N N 96  
CYS CA  C    sing N N 97  
CYS CA  CB   sing N N 98  
CYS CA  HA   sing N N 99  
CYS C   O    doub N N 100 
CYS C   OXT  sing N N 101 
CYS CB  SG   sing N N 102 
CYS CB  HB2  sing N N 103 
CYS CB  HB3  sing N N 104 
CYS SG  HG   sing N N 105 
CYS OXT HXT  sing N N 106 
GLN N   CA   sing N N 107 
GLN N   H    sing N N 108 
GLN N   H2   sing N N 109 
GLN CA  C    sing N N 110 
GLN CA  CB   sing N N 111 
GLN CA  HA   sing N N 112 
GLN C   O    doub N N 113 
GLN C   OXT  sing N N 114 
GLN CB  CG   sing N N 115 
GLN CB  HB2  sing N N 116 
GLN CB  HB3  sing N N 117 
GLN CG  CD   sing N N 118 
GLN CG  HG2  sing N N 119 
GLN CG  HG3  sing N N 120 
GLN CD  OE1  doub N N 121 
GLN CD  NE2  sing N N 122 
GLN NE2 HE21 sing N N 123 
GLN NE2 HE22 sing N N 124 
GLN OXT HXT  sing N N 125 
GLU N   CA   sing N N 126 
GLU N   H    sing N N 127 
GLU N   H2   sing N N 128 
GLU CA  C    sing N N 129 
GLU CA  CB   sing N N 130 
GLU CA  HA   sing N N 131 
GLU C   O    doub N N 132 
GLU C   OXT  sing N N 133 
GLU CB  CG   sing N N 134 
GLU CB  HB2  sing N N 135 
GLU CB  HB3  sing N N 136 
GLU CG  CD   sing N N 137 
GLU CG  HG2  sing N N 138 
GLU CG  HG3  sing N N 139 
GLU CD  OE1  doub N N 140 
GLU CD  OE2  sing N N 141 
GLU OE2 HE2  sing N N 142 
GLU OXT HXT  sing N N 143 
GLY N   CA   sing N N 144 
GLY N   H    sing N N 145 
GLY N   H2   sing N N 146 
GLY CA  C    sing N N 147 
GLY CA  HA2  sing N N 148 
GLY CA  HA3  sing N N 149 
GLY C   O    doub N N 150 
GLY C   OXT  sing N N 151 
GLY OXT HXT  sing N N 152 
HIS N   CA   sing N N 153 
HIS N   H    sing N N 154 
HIS N   H2   sing N N 155 
HIS CA  C    sing N N 156 
HIS CA  CB   sing N N 157 
HIS CA  HA   sing N N 158 
HIS C   O    doub N N 159 
HIS C   OXT  sing N N 160 
HIS CB  CG   sing N N 161 
HIS CB  HB2  sing N N 162 
HIS CB  HB3  sing N N 163 
HIS CG  ND1  sing Y N 164 
HIS CG  CD2  doub Y N 165 
HIS ND1 CE1  doub Y N 166 
HIS ND1 HD1  sing N N 167 
HIS CD2 NE2  sing Y N 168 
HIS CD2 HD2  sing N N 169 
HIS CE1 NE2  sing Y N 170 
HIS CE1 HE1  sing N N 171 
HIS NE2 HE2  sing N N 172 
HIS OXT HXT  sing N N 173 
ILE N   CA   sing N N 174 
ILE N   H    sing N N 175 
ILE N   H2   sing N N 176 
ILE CA  C    sing N N 177 
ILE CA  CB   sing N N 178 
ILE CA  HA   sing N N 179 
ILE C   O    doub N N 180 
ILE C   OXT  sing N N 181 
ILE CB  CG1  sing N N 182 
ILE CB  CG2  sing N N 183 
ILE CB  HB   sing N N 184 
ILE CG1 CD1  sing N N 185 
ILE CG1 HG12 sing N N 186 
ILE CG1 HG13 sing N N 187 
ILE CG2 HG21 sing N N 188 
ILE CG2 HG22 sing N N 189 
ILE CG2 HG23 sing N N 190 
ILE CD1 HD11 sing N N 191 
ILE CD1 HD12 sing N N 192 
ILE CD1 HD13 sing N N 193 
ILE OXT HXT  sing N N 194 
LEU N   CA   sing N N 195 
LEU N   H    sing N N 196 
LEU N   H2   sing N N 197 
LEU CA  C    sing N N 198 
LEU CA  CB   sing N N 199 
LEU CA  HA   sing N N 200 
LEU C   O    doub N N 201 
LEU C   OXT  sing N N 202 
LEU CB  CG   sing N N 203 
LEU CB  HB2  sing N N 204 
LEU CB  HB3  sing N N 205 
LEU CG  CD1  sing N N 206 
LEU CG  CD2  sing N N 207 
LEU CG  HG   sing N N 208 
LEU CD1 HD11 sing N N 209 
LEU CD1 HD12 sing N N 210 
LEU CD1 HD13 sing N N 211 
LEU CD2 HD21 sing N N 212 
LEU CD2 HD22 sing N N 213 
LEU CD2 HD23 sing N N 214 
LEU OXT HXT  sing N N 215 
LYS N   CA   sing N N 216 
LYS N   H    sing N N 217 
LYS N   H2   sing N N 218 
LYS CA  C    sing N N 219 
LYS CA  CB   sing N N 220 
LYS CA  HA   sing N N 221 
LYS C   O    doub N N 222 
LYS C   OXT  sing N N 223 
LYS CB  CG   sing N N 224 
LYS CB  HB2  sing N N 225 
LYS CB  HB3  sing N N 226 
LYS CG  CD   sing N N 227 
LYS CG  HG2  sing N N 228 
LYS CG  HG3  sing N N 229 
LYS CD  CE   sing N N 230 
LYS CD  HD2  sing N N 231 
LYS CD  HD3  sing N N 232 
LYS CE  NZ   sing N N 233 
LYS CE  HE2  sing N N 234 
LYS CE  HE3  sing N N 235 
LYS NZ  HZ1  sing N N 236 
LYS NZ  HZ2  sing N N 237 
LYS NZ  HZ3  sing N N 238 
LYS OXT HXT  sing N N 239 
MET N   CA   sing N N 240 
MET N   H    sing N N 241 
MET N   H2   sing N N 242 
MET CA  C    sing N N 243 
MET CA  CB   sing N N 244 
MET CA  HA   sing N N 245 
MET C   O    doub N N 246 
MET C   OXT  sing N N 247 
MET CB  CG   sing N N 248 
MET CB  HB2  sing N N 249 
MET CB  HB3  sing N N 250 
MET CG  SD   sing N N 251 
MET CG  HG2  sing N N 252 
MET CG  HG3  sing N N 253 
MET SD  CE   sing N N 254 
MET CE  HE1  sing N N 255 
MET CE  HE2  sing N N 256 
MET CE  HE3  sing N N 257 
MET OXT HXT  sing N N 258 
NAG C1  C2   sing N N 259 
NAG C1  O1   sing N N 260 
NAG C1  O5   sing N N 261 
NAG C1  H1   sing N N 262 
NAG C2  C3   sing N N 263 
NAG C2  N2   sing N N 264 
NAG C2  H2   sing N N 265 
NAG C3  C4   sing N N 266 
NAG C3  O3   sing N N 267 
NAG C3  H3   sing N N 268 
NAG C4  C5   sing N N 269 
NAG C4  O4   sing N N 270 
NAG C4  H4   sing N N 271 
NAG C5  C6   sing N N 272 
NAG C5  O5   sing N N 273 
NAG C5  H5   sing N N 274 
NAG C6  O6   sing N N 275 
NAG C6  H61  sing N N 276 
NAG C6  H62  sing N N 277 
NAG C7  C8   sing N N 278 
NAG C7  N2   sing N N 279 
NAG C7  O7   doub N N 280 
NAG C8  H81  sing N N 281 
NAG C8  H82  sing N N 282 
NAG C8  H83  sing N N 283 
NAG N2  HN2  sing N N 284 
NAG O1  HO1  sing N N 285 
NAG O3  HO3  sing N N 286 
NAG O4  HO4  sing N N 287 
NAG O6  HO6  sing N N 288 
PHE N   CA   sing N N 289 
PHE N   H    sing N N 290 
PHE N   H2   sing N N 291 
PHE CA  C    sing N N 292 
PHE CA  CB   sing N N 293 
PHE CA  HA   sing N N 294 
PHE C   O    doub N N 295 
PHE C   OXT  sing N N 296 
PHE CB  CG   sing N N 297 
PHE CB  HB2  sing N N 298 
PHE CB  HB3  sing N N 299 
PHE CG  CD1  doub Y N 300 
PHE CG  CD2  sing Y N 301 
PHE CD1 CE1  sing Y N 302 
PHE CD1 HD1  sing N N 303 
PHE CD2 CE2  doub Y N 304 
PHE CD2 HD2  sing N N 305 
PHE CE1 CZ   doub Y N 306 
PHE CE1 HE1  sing N N 307 
PHE CE2 CZ   sing Y N 308 
PHE CE2 HE2  sing N N 309 
PHE CZ  HZ   sing N N 310 
PHE OXT HXT  sing N N 311 
PRO N   CA   sing N N 312 
PRO N   CD   sing N N 313 
PRO N   H    sing N N 314 
PRO CA  C    sing N N 315 
PRO CA  CB   sing N N 316 
PRO CA  HA   sing N N 317 
PRO C   O    doub N N 318 
PRO C   OXT  sing N N 319 
PRO CB  CG   sing N N 320 
PRO CB  HB2  sing N N 321 
PRO CB  HB3  sing N N 322 
PRO CG  CD   sing N N 323 
PRO CG  HG2  sing N N 324 
PRO CG  HG3  sing N N 325 
PRO CD  HD2  sing N N 326 
PRO CD  HD3  sing N N 327 
PRO OXT HXT  sing N N 328 
SER N   CA   sing N N 329 
SER N   H    sing N N 330 
SER N   H2   sing N N 331 
SER CA  C    sing N N 332 
SER CA  CB   sing N N 333 
SER CA  HA   sing N N 334 
SER C   O    doub N N 335 
SER C   OXT  sing N N 336 
SER CB  OG   sing N N 337 
SER CB  HB2  sing N N 338 
SER CB  HB3  sing N N 339 
SER OG  HG   sing N N 340 
SER OXT HXT  sing N N 341 
THR N   CA   sing N N 342 
THR N   H    sing N N 343 
THR N   H2   sing N N 344 
THR CA  C    sing N N 345 
THR CA  CB   sing N N 346 
THR CA  HA   sing N N 347 
THR C   O    doub N N 348 
THR C   OXT  sing N N 349 
THR CB  OG1  sing N N 350 
THR CB  CG2  sing N N 351 
THR CB  HB   sing N N 352 
THR OG1 HG1  sing N N 353 
THR CG2 HG21 sing N N 354 
THR CG2 HG22 sing N N 355 
THR CG2 HG23 sing N N 356 
THR OXT HXT  sing N N 357 
TRP N   CA   sing N N 358 
TRP N   H    sing N N 359 
TRP N   H2   sing N N 360 
TRP CA  C    sing N N 361 
TRP CA  CB   sing N N 362 
TRP CA  HA   sing N N 363 
TRP C   O    doub N N 364 
TRP C   OXT  sing N N 365 
TRP CB  CG   sing N N 366 
TRP CB  HB2  sing N N 367 
TRP CB  HB3  sing N N 368 
TRP CG  CD1  doub Y N 369 
TRP CG  CD2  sing Y N 370 
TRP CD1 NE1  sing Y N 371 
TRP CD1 HD1  sing N N 372 
TRP CD2 CE2  doub Y N 373 
TRP CD2 CE3  sing Y N 374 
TRP NE1 CE2  sing Y N 375 
TRP NE1 HE1  sing N N 376 
TRP CE2 CZ2  sing Y N 377 
TRP CE3 CZ3  doub Y N 378 
TRP CE3 HE3  sing N N 379 
TRP CZ2 CH2  doub Y N 380 
TRP CZ2 HZ2  sing N N 381 
TRP CZ3 CH2  sing Y N 382 
TRP CZ3 HZ3  sing N N 383 
TRP CH2 HH2  sing N N 384 
TRP OXT HXT  sing N N 385 
TYR N   CA   sing N N 386 
TYR N   H    sing N N 387 
TYR N   H2   sing N N 388 
TYR CA  C    sing N N 389 
TYR CA  CB   sing N N 390 
TYR CA  HA   sing N N 391 
TYR C   O    doub N N 392 
TYR C   OXT  sing N N 393 
TYR CB  CG   sing N N 394 
TYR CB  HB2  sing N N 395 
TYR CB  HB3  sing N N 396 
TYR CG  CD1  doub Y N 397 
TYR CG  CD2  sing Y N 398 
TYR CD1 CE1  sing Y N 399 
TYR CD1 HD1  sing N N 400 
TYR CD2 CE2  doub Y N 401 
TYR CD2 HD2  sing N N 402 
TYR CE1 CZ   doub Y N 403 
TYR CE1 HE1  sing N N 404 
TYR CE2 CZ   sing Y N 405 
TYR CE2 HE2  sing N N 406 
TYR CZ  OH   sing N N 407 
TYR OH  HH   sing N N 408 
TYR OXT HXT  sing N N 409 
VAL N   CA   sing N N 410 
VAL N   H    sing N N 411 
VAL N   H2   sing N N 412 
VAL CA  C    sing N N 413 
VAL CA  CB   sing N N 414 
VAL CA  HA   sing N N 415 
VAL C   O    doub N N 416 
VAL C   OXT  sing N N 417 
VAL CB  CG1  sing N N 418 
VAL CB  CG2  sing N N 419 
VAL CB  HB   sing N N 420 
VAL CG1 HG11 sing N N 421 
VAL CG1 HG12 sing N N 422 
VAL CG1 HG13 sing N N 423 
VAL CG2 HG21 sing N N 424 
VAL CG2 HG22 sing N N 425 
VAL CG2 HG23 sing N N 426 
VAL OXT HXT  sing N N 427 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           75N93109C00051 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
4 NAG 1 n 
4 NAG 2 n 
4 BMA 3 n 
5 NAG 1 n 
5 NAG 2 n 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4M4Y 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9C0U 
_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]   0.006170 
_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]   0.006170 
_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]   0.006170 
_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 
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   . ILE A 1 337 ? 2.736   0.012   -10.892 1.00 150.66 ? 10  ILE B N   1 
ATOM   2    C CA  . ILE A 1 337 ? 2.852   0.814   -12.103 1.00 150.88 ? 10  ILE B CA  1 
ATOM   3    C C   . ILE A 1 337 ? 1.449   1.163   -12.586 1.00 170.24 ? 10  ILE B C   1 
ATOM   4    O O   . ILE A 1 337 ? 0.806   0.366   -13.270 1.00 187.51 ? 10  ILE B O   1 
ATOM   5    C CB  . ILE A 1 337 ? 3.645   0.074   -13.196 1.00 145.00 ? 10  ILE B CB  1 
ATOM   6    C CG1 . ILE A 1 337 ? 5.084   -0.170  -12.750 1.00 136.56 ? 10  ILE B CG1 1 
ATOM   7    C CG2 . ILE A 1 337 ? 3.669   0.883   -14.479 1.00 158.04 ? 10  ILE B CG2 1 
ATOM   8    C CD1 . ILE A 1 337 ? 5.824   -1.123  -13.653 1.00 136.21 ? 10  ILE B CD1 1 
ATOM   9    N N   . GLU A 1 338 ? 0.968   2.349   -12.219 1.00 158.13 ? 11  GLU B N   1 
ATOM   10   C CA  . GLU A 1 338 ? -0.372  2.790   -12.581 1.00 171.25 ? 11  GLU B CA  1 
ATOM   11   C C   . GLU A 1 338 ? -0.382  3.759   -13.758 1.00 178.59 ? 11  GLU B C   1 
ATOM   12   O O   . GLU A 1 338 ? -1.431  4.336   -14.058 1.00 173.11 ? 11  GLU B O   1 
ATOM   13   C CB  . GLU A 1 338 ? -1.059  3.432   -11.375 1.00 158.65 ? 11  GLU B CB  1 
ATOM   14   C CG  . GLU A 1 338 ? -1.369  2.463   -10.251 1.00 151.58 ? 11  GLU B CG  1 
ATOM   15   C CD  . GLU A 1 338 ? -1.990  3.152   -9.056  1.00 169.25 ? 11  GLU B CD  1 
ATOM   16   O OE1 . GLU A 1 338 ? -2.003  4.401   -9.034  1.00 167.92 ? 11  GLU B OE1 1 
ATOM   17   O OE2 . GLU A 1 338 ? -2.460  2.448   -8.139  1.00 181.17 ? 11  GLU B OE2 1 
ATOM   18   N N   . GLY A 1 339 ? 0.752   3.949   -14.428 1.00 172.89 ? 12  GLY B N   1 
ATOM   19   C CA  . GLY A 1 339 ? 0.808   4.852   -15.562 1.00 149.74 ? 12  GLY B CA  1 
ATOM   20   C C   . GLY A 1 339 ? 1.472   4.263   -16.792 1.00 134.11 ? 12  GLY B C   1 
ATOM   21   O O   . GLY A 1 339 ? 2.557   3.680   -16.700 1.00 160.96 ? 12  GLY B O   1 
ATOM   22   N N   . GLY A 1 340 ? 0.831   4.416   -17.955 1.00 107.91 ? 13  GLY B N   1 
ATOM   23   C CA  . GLY A 1 340 ? 1.395   3.900   -19.184 1.00 112.68 ? 13  GLY B CA  1 
ATOM   24   C C   . GLY A 1 340 ? 2.475   4.797   -19.760 1.00 110.50 ? 13  GLY B C   1 
ATOM   25   O O   . GLY A 1 340 ? 2.531   5.999   -19.504 1.00 119.55 ? 13  GLY B O   1 
ATOM   26   N N   . TRP A 1 341 ? 3.350   4.187   -20.560 1.00 108.00 ? 14  TRP B N   1 
ATOM   27   C CA  . TRP A 1 341 ? 4.483   4.874   -21.176 1.00 101.14 ? 14  TRP B CA  1 
ATOM   28   C C   . TRP A 1 341 ? 4.237   4.967   -22.677 1.00 122.30 ? 14  TRP B C   1 
ATOM   29   O O   . TRP A 1 341 ? 4.180   3.944   -23.367 1.00 138.68 ? 14  TRP B O   1 
ATOM   30   C CB  . TRP A 1 341 ? 5.794   4.143   -20.884 1.00 116.74 ? 14  TRP B CB  1 
ATOM   31   C CG  . TRP A 1 341 ? 6.317   4.357   -19.495 1.00 98.25  ? 14  TRP B CG  1 
ATOM   32   C CD1 . TRP A 1 341 ? 5.757   5.127   -18.518 1.00 115.34 ? 14  TRP B CD1 1 
ATOM   33   C CD2 . TRP A 1 341 ? 7.498   3.779   -18.922 1.00 89.66  ? 14  TRP B CD2 1 
ATOM   34   N NE1 . TRP A 1 341 ? 6.519   5.072   -17.376 1.00 121.42 ? 14  TRP B NE1 1 
ATOM   35   C CE2 . TRP A 1 341 ? 7.593   4.251   -17.598 1.00 118.90 ? 14  TRP B CE2 1 
ATOM   36   C CE3 . TRP A 1 341 ? 8.486   2.913   -19.402 1.00 106.16 ? 14  TRP B CE3 1 
ATOM   37   C CZ2 . TRP A 1 341 ? 8.635   3.885   -16.748 1.00 137.64 ? 14  TRP B CZ2 1 
ATOM   38   C CZ3 . TRP A 1 341 ? 9.519   2.551   -18.556 1.00 117.00 ? 14  TRP B CZ3 1 
ATOM   39   C CH2 . TRP A 1 341 ? 9.584   3.035   -17.245 1.00 123.94 ? 14  TRP B CH2 1 
ATOM   40   N N   . THR A 1 342 ? 4.096   6.194   -23.182 1.00 121.02 ? 15  THR B N   1 
ATOM   41   C CA  . THR A 1 342 ? 3.924   6.384   -24.617 1.00 108.93 ? 15  THR B CA  1 
ATOM   42   C C   . THR A 1 342 ? 5.242   6.261   -25.370 1.00 98.21  ? 15  THR B C   1 
ATOM   43   O O   . THR A 1 342 ? 5.248   5.836   -26.529 1.00 100.70 ? 15  THR B O   1 
ATOM   44   C CB  . THR A 1 342 ? 3.290   7.746   -24.900 1.00 108.71 ? 15  THR B CB  1 
ATOM   45   O OG1 . THR A 1 342 ? 4.126   8.782   -24.370 1.00 121.86 ? 15  THR B OG1 1 
ATOM   46   C CG2 . THR A 1 342 ? 1.910   7.835   -24.263 1.00 105.70 ? 15  THR B CG2 1 
ATOM   47   N N   . GLY A 1 343 ? 6.359   6.616   -24.731 1.00 101.57 ? 16  GLY B N   1 
ATOM   48   C CA  . GLY A 1 343 ? 7.651   6.566   -25.394 1.00 116.76 ? 16  GLY B CA  1 
ATOM   49   C C   . GLY A 1 343 ? 8.154   5.166   -25.685 1.00 148.28 ? 16  GLY B C   1 
ATOM   50   O O   . GLY A 1 343 ? 9.045   5.003   -26.525 1.00 146.24 ? 16  GLY B O   1 
ATOM   51   N N   . MET A 1 344 ? 7.605   4.153   -25.012 1.00 146.48 ? 17  MET B N   1 
ATOM   52   C CA  . MET A 1 344 ? 8.021   2.761   -25.199 1.00 158.09 ? 17  MET B CA  1 
ATOM   53   C C   . MET A 1 344 ? 7.257   2.088   -26.344 1.00 150.97 ? 17  MET B C   1 
ATOM   54   O O   . MET A 1 344 ? 6.542   1.104   -26.165 1.00 169.26 ? 17  MET B O   1 
ATOM   55   C CB  . MET A 1 344 ? 7.774   1.967   -23.921 1.00 152.56 ? 17  MET B CB  1 
ATOM   56   C CG  . MET A 1 344 ? 8.586   0.680   -23.788 1.00 154.12 ? 17  MET B CG  1 
ATOM   57   S SD  . MET A 1 344 ? 10.363  0.953   -23.685 1.00 225.87 ? 17  MET B SD  1 
ATOM   58   C CE  . MET A 1 344 ? 10.507  1.580   -22.015 1.00 176.42 ? 17  MET B CE  1 
ATOM   59   N N   . VAL A 1 345 ? 7.407   2.665   -27.543 1.00 146.37 ? 18  VAL B N   1 
ATOM   60   C CA  . VAL A 1 345 ? 6.675   2.141   -28.748 1.00 129.31 ? 18  VAL B CA  1 
ATOM   61   C C   . VAL A 1 345 ? 7.377   0.931   -29.391 1.00 145.15 ? 18  VAL B C   1 
ATOM   62   O O   . VAL A 1 345 ? 6.866   0.423   -30.399 1.00 152.42 ? 18  VAL B O   1 
ATOM   63   C CB  . VAL A 1 345 ? 6.273   3.266   -29.691 1.00 131.96 ? 18  VAL B CB  1 
ATOM   64   C CG1 . VAL A 1 345 ? 7.474   4.008   -30.255 1.00 127.93 ? 18  VAL B CG1 1 
ATOM   65   C CG2 . VAL A 1 345 ? 5.373   2.765   -30.809 1.00 135.58 ? 18  VAL B CG2 1 
ATOM   66   N N   . ASP A 1 346 ? 8.519   0.524   -28.847 1.00 131.47 ? 19  ASP B N   1 
ATOM   67   C CA  . ASP A 1 346 ? 9.181   -0.691  -29.362 1.00 133.78 ? 19  ASP B CA  1 
ATOM   68   C C   . ASP A 1 346 ? 8.594   -2.006  -28.841 1.00 133.00 ? 19  ASP B C   1 
ATOM   69   O O   . ASP A 1 346 ? 8.332   -2.900  -29.660 1.00 141.95 ? 19  ASP B O   1 
ATOM   70   C CB  . ASP A 1 346 ? 10.669  -0.598  -28.985 1.00 142.53 ? 19  ASP B CB  1 
ATOM   71   C CG  . ASP A 1 346 ? 11.542  -1.618  -29.695 1.00 178.91 ? 19  ASP B CG  1 
ATOM   72   O OD1 . ASP A 1 346 ? 11.024  -2.318  -30.586 1.00 158.11 ? 19  ASP B OD1 1 
ATOM   73   O OD2 . ASP A 1 346 ? 12.727  -1.717  -29.334 1.00 206.92 ? 19  ASP B OD2 1 
ATOM   74   N N   . GLY A 1 347 ? 8.372   -2.085  -27.531 1.00 134.54 ? 20  GLY B N   1 
ATOM   75   C CA  . GLY A 1 347 ? 7.807   -3.303  -26.926 1.00 124.62 ? 20  GLY B CA  1 
ATOM   76   C C   . GLY A 1 347 ? 6.884   -2.967  -25.772 1.00 124.33 ? 20  GLY B C   1 
ATOM   77   O O   . GLY A 1 347 ? 6.880   -1.803  -25.339 1.00 141.86 ? 20  GLY B O   1 
ATOM   78   N N   . TRP A 1 348 ? 6.134   -3.951  -25.287 1.00 111.41 ? 21  TRP B N   1 
ATOM   79   C CA  . TRP A 1 348 ? 5.169   -3.719  -24.215 1.00 110.41 ? 21  TRP B CA  1 
ATOM   80   C C   . TRP A 1 348 ? 5.873   -3.341  -22.919 1.00 111.35 ? 21  TRP B C   1 
ATOM   81   O O   . TRP A 1 348 ? 5.717   -2.227  -22.405 1.00 102.88 ? 21  TRP B O   1 
ATOM   82   C CB  . TRP A 1 348 ? 4.311   -4.966  -23.997 1.00 114.05 ? 21  TRP B CB  1 
ATOM   83   C CG  . TRP A 1 348 ? 3.348   -5.267  -25.095 1.00 107.23 ? 21  TRP B CG  1 
ATOM   84   C CD1 . TRP A 1 348 ? 2.769   -4.378  -25.953 1.00 109.39 ? 21  TRP B CD1 1 
ATOM   85   C CD2 . TRP A 1 348 ? 2.840   -6.557  -25.449 1.00 123.05 ? 21  TRP B CD2 1 
ATOM   86   N NE1 . TRP A 1 348 ? 1.932   -5.037  -26.822 1.00 106.64 ? 21  TRP B NE1 1 
ATOM   87   C CE2 . TRP A 1 348 ? 1.960   -6.377  -26.533 1.00 115.10 ? 21  TRP B CE2 1 
ATOM   88   C CE3 . TRP A 1 348 ? 3.046   -7.849  -24.955 1.00 121.41 ? 21  TRP B CE3 1 
ATOM   89   C CZ2 . TRP A 1 348 ? 1.291   -7.439  -27.132 1.00 100.15 ? 21  TRP B CZ2 1 
ATOM   90   C CZ3 . TRP A 1 348 ? 2.379   -8.901  -25.549 1.00 97.70  ? 21  TRP B CZ3 1 
ATOM   91   C CH2 . TRP A 1 348 ? 1.509   -8.690  -26.623 1.00 93.15  ? 21  TRP B CH2 1 
ATOM   92   N N   . TYR A 1 349 ? 6.653   -4.269  -22.378 1.00 111.04 ? 22  TYR B N   1 
ATOM   93   C CA  . TYR A 1 349 ? 7.288   -4.107  -21.081 1.00 108.30 ? 22  TYR B CA  1 
ATOM   94   C C   . TYR A 1 349 ? 8.678   -3.514  -21.262 1.00 120.29 ? 22  TYR B C   1 
ATOM   95   O O   . TYR A 1 349 ? 9.480   -4.025  -22.050 1.00 118.35 ? 22  TYR B O   1 
ATOM   96   C CB  . TYR A 1 349 ? 7.368   -5.457  -20.373 1.00 91.38  ? 22  TYR B CB  1 
ATOM   97   C CG  . TYR A 1 349 ? 6.171   -6.344  -20.635 1.00 102.37 ? 22  TYR B CG  1 
ATOM   98   C CD1 . TYR A 1 349 ? 4.897   -5.963  -20.232 1.00 148.71 ? 22  TYR B CD1 1 
ATOM   99   C CD2 . TYR A 1 349 ? 6.314   -7.561  -21.287 1.00 88.01  ? 22  TYR B CD2 1 
ATOM   100  C CE1 . TYR A 1 349 ? 3.800   -6.771  -20.469 1.00 154.67 ? 22  TYR B CE1 1 
ATOM   101  C CE2 . TYR A 1 349 ? 5.225   -8.375  -21.528 1.00 103.59 ? 22  TYR B CE2 1 
ATOM   102  C CZ  . TYR A 1 349 ? 3.970   -7.976  -21.117 1.00 135.39 ? 22  TYR B CZ  1 
ATOM   103  O OH  . TYR A 1 349 ? 2.886   -8.789  -21.358 1.00 148.45 ? 22  TYR B OH  1 
ATOM   104  N N   . GLY A 1 350 ? 8.961   -2.436  -20.530 1.00 125.50 ? 23  GLY B N   1 
ATOM   105  C CA  . GLY A 1 350 ? 10.227  -1.752  -20.693 1.00 126.95 ? 23  GLY B CA  1 
ATOM   106  C C   . GLY A 1 350 ? 10.673  -1.040  -19.435 1.00 110.14 ? 23  GLY B C   1 
ATOM   107  O O   . GLY A 1 350 ? 9.927   -0.903  -18.462 1.00 102.44 ? 23  GLY B O   1 
ATOM   108  N N   . TYR A 1 351 ? 11.918  -0.575  -19.482 1.00 106.59 ? 24  TYR B N   1 
ATOM   109  C CA  . TYR A 1 351 ? 12.566  0.121   -18.383 1.00 118.33 ? 24  TYR B CA  1 
ATOM   110  C C   . TYR A 1 351 ? 12.954  1.520   -18.842 1.00 123.35 ? 24  TYR B C   1 
ATOM   111  O O   . TYR A 1 351 ? 13.364  1.705   -19.992 1.00 124.29 ? 24  TYR B O   1 
ATOM   112  C CB  . TYR A 1 351 ? 13.819  -0.630  -17.924 1.00 132.46 ? 24  TYR B CB  1 
ATOM   113  C CG  . TYR A 1 351 ? 13.558  -2.009  -17.370 1.00 130.84 ? 24  TYR B CG  1 
ATOM   114  C CD1 . TYR A 1 351 ? 13.232  -2.186  -16.040 1.00 150.86 ? 24  TYR B CD1 1 
ATOM   115  C CD2 . TYR A 1 351 ? 13.679  -3.139  -18.171 1.00 112.61 ? 24  TYR B CD2 1 
ATOM   116  C CE1 . TYR A 1 351 ? 12.995  -3.441  -15.522 1.00 165.78 ? 24  TYR B CE1 1 
ATOM   117  C CE2 . TYR A 1 351 ? 13.452  -4.406  -17.657 1.00 142.81 ? 24  TYR B CE2 1 
ATOM   118  C CZ  . TYR A 1 351 ? 13.111  -4.548  -16.328 1.00 169.41 ? 24  TYR B CZ  1 
ATOM   119  O OH  . TYR A 1 351 ? 12.883  -5.797  -15.798 1.00 163.88 ? 24  TYR B OH  1 
ATOM   120  N N   . HIS A 1 352 ? 12.833  2.507   -17.951 1.00 120.86 ? 25  HIS B N   1 
ATOM   121  C CA  . HIS A 1 352 ? 13.286  3.868   -18.251 1.00 114.55 ? 25  HIS B CA  1 
ATOM   122  C C   . HIS A 1 352 ? 14.587  4.110   -17.492 1.00 117.64 ? 25  HIS B C   1 
ATOM   123  O O   . HIS A 1 352 ? 14.588  4.518   -16.330 1.00 124.27 ? 25  HIS B O   1 
ATOM   124  C CB  . HIS A 1 352 ? 12.238  4.917   -17.902 1.00 109.52 ? 25  HIS B CB  1 
ATOM   125  C CG  . HIS A 1 352 ? 12.657  6.312   -18.243 1.00 102.80 ? 25  HIS B CG  1 
ATOM   126  N ND1 . HIS A 1 352 ? 12.708  6.773   -19.541 1.00 123.33 ? 25  HIS B ND1 1 
ATOM   127  C CD2 . HIS A 1 352 ? 13.043  7.347   -17.460 1.00 97.53  ? 25  HIS B CD2 1 
ATOM   128  C CE1 . HIS A 1 352 ? 13.112  8.030   -19.544 1.00 119.49 ? 25  HIS B CE1 1 
ATOM   129  N NE2 . HIS A 1 352 ? 13.320  8.403   -18.294 1.00 117.67 ? 25  HIS B NE2 1 
ATOM   130  N N   . HIS A 1 353 ? 15.702  3.861   -18.172 1.00 131.12 ? 26  HIS B N   1 
ATOM   131  C CA  . HIS A 1 353 ? 17.017  4.026   -17.572 1.00 153.49 ? 26  HIS B CA  1 
ATOM   132  C C   . HIS A 1 353 ? 17.330  5.509   -17.399 1.00 130.27 ? 26  HIS B C   1 
ATOM   133  O O   . HIS A 1 353 ? 17.010  6.327   -18.265 1.00 121.62 ? 26  HIS B O   1 
ATOM   134  C CB  . HIS A 1 353 ? 18.079  3.362   -18.455 1.00 174.91 ? 26  HIS B CB  1 
ATOM   135  C CG  . HIS A 1 353 ? 17.872  1.890   -18.666 1.00 204.78 ? 26  HIS B CG  1 
ATOM   136  N ND1 . HIS A 1 353 ? 18.043  0.959   -17.663 1.00 223.65 ? 26  HIS B ND1 1 
ATOM   137  C CD2 . HIS A 1 353 ? 17.502  1.190   -19.765 1.00 186.80 ? 26  HIS B CD2 1 
ATOM   138  C CE1 . HIS A 1 353 ? 17.796  -0.249  -18.136 1.00 213.72 ? 26  HIS B CE1 1 
ATOM   139  N NE2 . HIS A 1 353 ? 17.463  -0.137  -19.409 1.00 208.25 ? 26  HIS B NE2 1 
ATOM   140  N N   . GLN A 1 354 ? 17.943  5.861   -16.268 1.00 142.03 ? 27  GLN B N   1 
ATOM   141  C CA  . GLN A 1 354 ? 18.404  7.228   -16.034 1.00 155.89 ? 27  GLN B CA  1 
ATOM   142  C C   . GLN A 1 354 ? 19.763  7.177   -15.356 1.00 175.88 ? 27  GLN B C   1 
ATOM   143  O O   . GLN A 1 354 ? 19.882  6.680   -14.233 1.00 196.61 ? 27  GLN B O   1 
ATOM   144  C CB  . GLN A 1 354 ? 17.409  8.033   -15.186 1.00 159.74 ? 27  GLN B CB  1 
ATOM   145  C CG  . GLN A 1 354 ? 17.774  9.502   -15.036 1.00 164.93 ? 27  GLN B CG  1 
ATOM   146  C CD  . GLN A 1 354 ? 16.703  10.317  -14.343 1.00 168.45 ? 27  GLN B CD  1 
ATOM   147  O OE1 . GLN A 1 354 ? 15.620  9.813   -14.040 1.00 178.03 ? 27  GLN B OE1 1 
ATOM   148  N NE2 . GLN A 1 354 ? 16.991  11.586  -14.097 1.00 185.09 ? 27  GLN B NE2 1 
ATOM   149  N N   . ASN A 1 355 ? 20.780  7.683   -16.045 1.00 165.39 ? 28  ASN B N   1 
ATOM   150  C CA  . ASN A 1 355 ? 22.142  7.782   -15.547 1.00 177.90 ? 28  ASN B CA  1 
ATOM   151  C C   . ASN A 1 355 ? 22.542  9.253   -15.523 1.00 177.76 ? 28  ASN B C   1 
ATOM   152  O O   . ASN A 1 355 ? 21.831  10.116  -16.046 1.00 163.41 ? 28  ASN B O   1 
ATOM   153  C CB  . ASN A 1 355 ? 23.097  6.956   -16.425 1.00 167.39 ? 28  ASN B CB  1 
ATOM   154  C CG  . ASN A 1 355 ? 24.486  6.819   -15.827 1.00 176.25 ? 28  ASN B CG  1 
ATOM   155  O OD1 . ASN A 1 355 ? 24.657  6.841   -14.611 1.00 196.92 ? 28  ASN B OD1 1 
ATOM   156  N ND2 . ASN A 1 355 ? 25.487  6.667   -16.687 1.00 154.11 ? 28  ASN B ND2 1 
ATOM   157  N N   . GLU A 1 356 ? 23.688  9.544   -14.894 1.00 197.24 ? 29  GLU B N   1 
ATOM   158  C CA  . GLU A 1 356 ? 24.263  10.883  -15.002 1.00 178.89 ? 29  GLU B CA  1 
ATOM   159  C C   . GLU A 1 356 ? 24.364  11.332  -16.446 1.00 172.93 ? 29  GLU B C   1 
ATOM   160  O O   . GLU A 1 356 ? 24.355  12.537  -16.731 1.00 157.82 ? 29  GLU B O   1 
ATOM   161  C CB  . GLU A 1 356 ? 25.659  10.945  -14.389 1.00 170.40 ? 29  GLU B CB  1 
ATOM   162  C CG  . GLU A 1 356 ? 25.741  10.816  -12.896 1.00 174.16 ? 29  GLU B CG  1 
ATOM   163  C CD  . GLU A 1 356 ? 27.177  10.863  -12.427 1.00 177.08 ? 29  GLU B CD  1 
ATOM   164  O OE1 . GLU A 1 356 ? 28.086  10.773  -13.279 1.00 176.44 ? 29  GLU B OE1 1 
ATOM   165  O OE2 . GLU A 1 356 ? 27.399  11.056  -11.219 1.00 169.68 ? 29  GLU B OE2 1 
ATOM   166  N N   . GLN A 1 357 ? 24.484  10.383  -17.369 1.00 170.09 ? 30  GLN B N   1 
ATOM   167  C CA  . GLN A 1 357 ? 24.636  10.751  -18.766 1.00 166.44 ? 30  GLN B CA  1 
ATOM   168  C C   . GLN A 1 357 ? 23.305  11.159  -19.384 1.00 169.19 ? 30  GLN B C   1 
ATOM   169  O O   . GLN A 1 357 ? 23.257  12.070  -20.219 1.00 173.90 ? 30  GLN B O   1 
ATOM   170  C CB  . GLN A 1 357 ? 25.229  9.591   -19.555 1.00 161.03 ? 30  GLN B CB  1 
ATOM   171  C CG  . GLN A 1 357 ? 24.306  8.427   -19.744 1.00 167.34 ? 30  GLN B CG  1 
ATOM   172  C CD  . GLN A 1 357 ? 24.895  7.408   -20.666 1.00 176.76 ? 30  GLN B CD  1 
ATOM   173  O OE1 . GLN A 1 357 ? 26.113  7.342   -20.843 1.00 180.95 ? 30  GLN B OE1 1 
ATOM   174  N NE2 . GLN A 1 357 ? 24.036  6.614   -21.291 1.00 165.84 ? 30  GLN B NE2 1 
ATOM   175  N N   . GLY A 1 358 ? 22.223  10.487  -18.990 1.00 135.72 ? 31  GLY B N   1 
ATOM   176  C CA  . GLY A 1 358 ? 20.945  10.797  -19.650 1.00 134.28 ? 31  GLY B CA  1 
ATOM   177  C C   . GLY A 1 358 ? 19.785  9.893   -19.303 1.00 143.13 ? 31  GLY B C   1 
ATOM   178  O O   . GLY A 1 358 ? 19.914  9.100   -18.357 1.00 161.47 ? 31  GLY B O   1 
ATOM   179  N N   . SER A 1 359 ? 18.693  10.015  -20.055 1.00 145.30 ? 32  SER B N   1 
ATOM   180  C CA  . SER A 1 359 ? 17.480  9.222   -19.770 1.00 134.39 ? 32  SER B CA  1 
ATOM   181  C C   . SER A 1 359 ? 16.864  8.615   -21.025 1.00 128.85 ? 32  SER B C   1 
ATOM   182  O O   . SER A 1 359 ? 16.643  9.370   -21.987 1.00 137.36 ? 32  SER B O   1 
ATOM   183  C CB  . SER A 1 359 ? 16.478  10.140  -19.146 1.00 150.26 ? 32  SER B CB  1 
ATOM   184  O OG  . SER A 1 359 ? 16.942  10.618  -17.892 1.00 172.20 ? 32  SER B OG  1 
ATOM   185  N N   . GLY A 1 360 ? 16.611  7.308   -21.016 1.00 138.33 ? 33  GLY B N   1 
ATOM   186  C CA  . GLY A 1 360 ? 15.983  6.689   -22.165 1.00 134.04 ? 33  GLY B CA  1 
ATOM   187  C C   . GLY A 1 360 ? 14.960  5.630   -21.798 1.00 123.13 ? 33  GLY B C   1 
ATOM   188  O O   . GLY A 1 360 ? 14.849  5.217   -20.643 1.00 132.09 ? 33  GLY B O   1 
ATOM   189  N N   . TYR A 1 361 ? 14.215  5.192   -22.818 1.00 93.94  ? 34  TYR B N   1 
ATOM   190  C CA  . TYR A 1 361 ? 13.158  4.185   -22.688 1.00 123.79 ? 34  TYR B CA  1 
ATOM   191  C C   . TYR A 1 361 ? 13.587  2.918   -23.429 1.00 144.81 ? 34  TYR B C   1 
ATOM   192  O O   . TYR A 1 361 ? 13.438  2.832   -24.651 1.00 148.49 ? 34  TYR B O   1 
ATOM   193  C CB  . TYR A 1 361 ? 11.837  4.702   -23.258 1.00 140.31 ? 34  TYR B CB  1 
ATOM   194  C CG  . TYR A 1 361 ? 11.092  5.723   -22.423 1.00 135.78 ? 34  TYR B CG  1 
ATOM   195  C CD1 . TYR A 1 361 ? 10.246  5.326   -21.395 1.00 135.37 ? 34  TYR B CD1 1 
ATOM   196  C CD2 . TYR A 1 361 ? 11.197  7.082   -22.696 1.00 126.38 ? 34  TYR B CD2 1 
ATOM   197  C CE1 . TYR A 1 361 ? 9.549   6.255   -20.642 1.00 125.43 ? 34  TYR B CE1 1 
ATOM   198  C CE2 . TYR A 1 361 ? 10.502  8.018   -21.949 1.00 114.17 ? 34  TYR B CE2 1 
ATOM   199  C CZ  . TYR A 1 361 ? 9.681   7.600   -20.924 1.00 121.81 ? 34  TYR B CZ  1 
ATOM   200  O OH  . TYR A 1 361 ? 8.990   8.529   -20.180 1.00 139.57 ? 34  TYR B OH  1 
ATOM   201  N N   . ALA A 1 362 ? 14.081  1.920   -22.695 1.00 136.66 ? 35  ALA B N   1 
ATOM   202  C CA  . ALA A 1 362 ? 14.550  0.667   -23.283 1.00 155.75 ? 35  ALA B CA  1 
ATOM   203  C C   . ALA A 1 362 ? 13.591  -0.467  -22.934 1.00 152.07 ? 35  ALA B C   1 
ATOM   204  O O   . ALA A 1 362 ? 13.394  -0.775  -21.753 1.00 148.42 ? 35  ALA B O   1 
ATOM   205  C CB  . ALA A 1 362 ? 15.962  0.333   -22.803 1.00 166.35 ? 35  ALA B CB  1 
ATOM   206  N N   . ALA A 1 363 ? 13.020  -1.100  -23.957 1.00 108.00 ? 36  ALA B N   1 
ATOM   207  C CA  . ALA A 1 363 ? 12.119  -2.225  -23.749 1.00 111.74 ? 36  ALA B CA  1 
ATOM   208  C C   . ALA A 1 363 ? 12.903  -3.503  -23.473 1.00 112.20 ? 36  ALA B C   1 
ATOM   209  O O   . ALA A 1 363 ? 14.001  -3.709  -23.997 1.00 135.36 ? 36  ALA B O   1 
ATOM   210  C CB  . ALA A 1 363 ? 11.217  -2.426  -24.966 1.00 124.86 ? 36  ALA B CB  1 
ATOM   211  N N   . ASP A 1 364 ? 12.328  -4.368  -22.639 1.00 108.32 ? 37  ASP B N   1 
ATOM   212  C CA  . ASP A 1 364 ? 12.945  -5.658  -22.356 1.00 124.99 ? 37  ASP B CA  1 
ATOM   213  C C   . ASP A 1 364 ? 12.639  -6.614  -23.501 1.00 131.98 ? 37  ASP B C   1 
ATOM   214  O O   . ASP A 1 364 ? 11.471  -6.898  -23.786 1.00 133.41 ? 37  ASP B O   1 
ATOM   215  C CB  . ASP A 1 364 ? 12.451  -6.231  -21.031 1.00 114.84 ? 37  ASP B CB  1 
ATOM   216  C CG  . ASP A 1 364 ? 13.180  -7.505  -20.647 1.00 105.08 ? 37  ASP B CG  1 
ATOM   217  O OD1 . ASP A 1 364 ? 14.377  -7.632  -20.981 1.00 119.96 ? 37  ASP B OD1 1 
ATOM   218  O OD2 . ASP A 1 364 ? 12.554  -8.387  -20.026 1.00 102.56 ? 37  ASP B OD2 1 
ATOM   219  N N   . LEU A 1 365 ? 13.689  -7.123  -24.145 1.00 135.63 ? 38  LEU B N   1 
ATOM   220  C CA  . LEU A 1 365 ? 13.509  -7.835  -25.405 1.00 120.05 ? 38  LEU B CA  1 
ATOM   221  C C   . LEU A 1 365 ? 12.913  -9.219  -25.188 1.00 121.23 ? 38  LEU B C   1 
ATOM   222  O O   . LEU A 1 365 ? 11.972  -9.617  -25.884 1.00 121.22 ? 38  LEU B O   1 
ATOM   223  C CB  . LEU A 1 365 ? 14.845  -7.929  -26.138 1.00 128.35 ? 38  LEU B CB  1 
ATOM   224  C CG  . LEU A 1 365 ? 15.334  -6.545  -26.557 1.00 152.59 ? 38  LEU B CG  1 
ATOM   225  C CD1 . LEU A 1 365 ? 16.716  -6.602  -27.196 1.00 158.58 ? 38  LEU B CD1 1 
ATOM   226  C CD2 . LEU A 1 365 ? 14.309  -5.902  -27.467 1.00 147.09 ? 38  LEU B CD2 1 
ATOM   227  N N   . LYS A 1 366 ? 13.454  -9.970  -24.228 1.00 132.80 ? 39  LYS B N   1 
ATOM   228  C CA  . LYS A 1 366 ? 12.989  -11.334 -24.004 1.00 122.09 ? 39  LYS B CA  1 
ATOM   229  C C   . LYS A 1 366 ? 11.547  -11.360 -23.516 1.00 121.01 ? 39  LYS B C   1 
ATOM   230  O O   . LYS A 1 366 ? 10.741  -12.170 -23.990 1.00 139.96 ? 39  LYS B O   1 
ATOM   231  C CB  . LYS A 1 366 ? 13.911  -12.035 -23.008 1.00 121.08 ? 39  LYS B CB  1 
ATOM   232  C CG  . LYS A 1 366 ? 15.315  -12.254 -23.550 1.00 127.93 ? 39  LYS B CG  1 
ATOM   233  C CD  . LYS A 1 366 ? 16.215  -12.928 -22.532 1.00 119.46 ? 39  LYS B CD  1 
ATOM   234  C CE  . LYS A 1 366 ? 17.603  -13.165 -23.109 1.00 107.58 ? 39  LYS B CE  1 
ATOM   235  N NZ  . LYS A 1 366 ? 18.511  -13.811 -22.122 1.00 156.45 ? 39  LYS B NZ  1 
ATOM   236  N N   . SER A 1 367 ? 11.198  -10.477 -22.582 1.00 96.99  ? 40  SER B N   1 
ATOM   237  C CA  . SER A 1 367 ? 9.833   -10.446 -22.069 1.00 90.03  ? 40  SER B CA  1 
ATOM   238  C C   . SER A 1 367 ? 8.833   -10.153 -23.180 1.00 104.67 ? 40  SER B C   1 
ATOM   239  O O   . SER A 1 367 ? 7.852   -10.886 -23.355 1.00 123.81 ? 40  SER B O   1 
ATOM   240  C CB  . SER A 1 367 ? 9.721   -9.409  -20.954 1.00 84.85  ? 40  SER B CB  1 
ATOM   241  O OG  . SER A 1 367 ? 9.795   -8.099  -21.485 1.00 102.24 ? 40  SER B OG  1 
ATOM   242  N N   . THR A 1 368 ? 9.070   -9.087  -23.950 1.00 101.62 ? 41  THR B N   1 
ATOM   243  C CA  . THR A 1 368 ? 8.142   -8.717  -25.015 1.00 95.82  ? 41  THR B CA  1 
ATOM   244  C C   . THR A 1 368 ? 8.040   -9.812  -26.070 1.00 107.63 ? 41  THR B C   1 
ATOM   245  O O   . THR A 1 368 ? 6.937   -10.204 -26.467 1.00 128.86 ? 41  THR B O   1 
ATOM   246  C CB  . THR A 1 368 ? 8.567   -7.393  -25.656 1.00 92.54  ? 41  THR B CB  1 
ATOM   247  O OG1 . THR A 1 368 ? 9.890   -7.520  -26.194 1.00 119.18 ? 41  THR B OG1 1 
ATOM   248  C CG2 . THR A 1 368 ? 8.523   -6.259  -24.639 1.00 100.69 ? 41  THR B CG2 1 
ATOM   249  N N   . GLN A 1 369 ? 9.183   -10.327 -26.530 1.00 100.77 ? 42  GLN B N   1 
ATOM   250  C CA  . GLN A 1 369 ? 9.166   -11.303 -27.615 1.00 114.37 ? 42  GLN B CA  1 
ATOM   251  C C   . GLN A 1 369 ? 8.467   -12.593 -27.194 1.00 112.59 ? 42  GLN B C   1 
ATOM   252  O O   . GLN A 1 369 ? 7.602   -13.101 -27.915 1.00 130.07 ? 42  GLN B O   1 
ATOM   253  C CB  . GLN A 1 369 ? 10.591  -11.590 -28.090 1.00 110.79 ? 42  GLN B CB  1 
ATOM   254  C CG  . GLN A 1 369 ? 10.703  -12.810 -28.991 1.00 129.63 ? 42  GLN B CG  1 
ATOM   255  C CD  . GLN A 1 369 ? 9.992   -12.619 -30.319 1.00 152.11 ? 42  GLN B CD  1 
ATOM   256  O OE1 . GLN A 1 369 ? 9.755   -11.491 -30.754 1.00 168.82 ? 42  GLN B OE1 1 
ATOM   257  N NE2 . GLN A 1 369 ? 9.646   -13.724 -30.968 1.00 194.55 ? 42  GLN B NE2 1 
ATOM   258  N N   . ASN A 1 370 ? 8.829   -13.139 -26.028 1.00 117.49 ? 43  ASN B N   1 
ATOM   259  C CA  . ASN A 1 370 ? 8.179   -14.360 -25.557 1.00 118.96 ? 43  ASN B CA  1 
ATOM   260  C C   . ASN A 1 370 ? 6.687   -14.150 -25.355 1.00 113.78 ? 43  ASN B C   1 
ATOM   261  O O   . ASN A 1 370 ? 5.877   -15.009 -25.724 1.00 120.79 ? 43  ASN B O   1 
ATOM   262  C CB  . ASN A 1 370 ? 8.822   -14.844 -24.259 1.00 121.10 ? 43  ASN B CB  1 
ATOM   263  C CG  . ASN A 1 370 ? 10.314  -15.040 -24.391 1.00 136.99 ? 43  ASN B CG  1 
ATOM   264  O OD1 . ASN A 1 370 ? 10.808  -15.423 -25.451 1.00 136.98 ? 43  ASN B OD1 1 
ATOM   265  N ND2 . ASN A 1 370 ? 11.044  -14.768 -23.316 1.00 138.07 ? 43  ASN B ND2 1 
ATOM   266  N N   . ALA A 1 371 ? 6.304   -13.015 -24.770 1.00 108.24 ? 44  ALA B N   1 
ATOM   267  C CA  . ALA A 1 371 ? 4.887   -12.727 -24.584 1.00 108.37 ? 44  ALA B CA  1 
ATOM   268  C C   . ALA A 1 371 ? 4.171   -12.609 -25.924 1.00 120.49 ? 44  ALA B C   1 
ATOM   269  O O   . ALA A 1 371 ? 3.060   -13.127 -26.088 1.00 123.01 ? 44  ALA B O   1 
ATOM   270  C CB  . ALA A 1 371 ? 4.711   -11.450 -23.763 1.00 94.33  ? 44  ALA B CB  1 
ATOM   271  N N   . ILE A 1 372 ? 4.795   -11.939 -26.898 1.00 101.84 ? 45  ILE B N   1 
ATOM   272  C CA  . ILE A 1 372 ? 4.195   -11.818 -28.226 1.00 85.19  ? 45  ILE B CA  1 
ATOM   273  C C   . ILE A 1 372 ? 3.987   -13.194 -28.850 1.00 106.64 ? 45  ILE B C   1 
ATOM   274  O O   . ILE A 1 372 ? 2.953   -13.456 -29.476 1.00 120.29 ? 45  ILE B O   1 
ATOM   275  C CB  . ILE A 1 372 ? 5.056   -10.905 -29.122 1.00 75.16  ? 45  ILE B CB  1 
ATOM   276  C CG1 . ILE A 1 372 ? 4.889   -9.438  -28.710 1.00 94.40  ? 45  ILE B CG1 1 
ATOM   277  C CG2 . ILE A 1 372 ? 4.736   -11.111 -30.600 1.00 92.82  ? 45  ILE B CG2 1 
ATOM   278  C CD1 . ILE A 1 372 ? 6.075   -8.570  -29.045 1.00 109.55 ? 45  ILE B CD1 1 
ATOM   279  N N   . ASP A 1 373 ? 4.955   -14.098 -28.677 1.00 112.22 ? 46  ASP B N   1 
ATOM   280  C CA  . ASP A 1 373 ? 4.814   -15.450 -29.213 1.00 117.38 ? 46  ASP B CA  1 
ATOM   281  C C   . ASP A 1 373 ? 3.617   -16.165 -28.597 1.00 107.28 ? 46  ASP B C   1 
ATOM   282  O O   . ASP A 1 373 ? 2.831   -16.808 -29.303 1.00 113.41 ? 46  ASP B O   1 
ATOM   283  C CB  . ASP A 1 373 ? 6.093   -16.251 -28.970 1.00 126.72 ? 46  ASP B CB  1 
ATOM   284  C CG  . ASP A 1 373 ? 7.316   -15.593 -29.572 1.00 156.29 ? 46  ASP B CG  1 
ATOM   285  O OD1 . ASP A 1 373 ? 7.153   -14.688 -30.417 1.00 181.65 ? 46  ASP B OD1 1 
ATOM   286  O OD2 . ASP A 1 373 ? 8.443   -15.984 -29.200 1.00 150.70 ? 46  ASP B OD2 1 
ATOM   287  N N   . GLY A 1 374 ? 3.463   -16.063 -27.275 1.00 103.60 ? 47  GLY B N   1 
ATOM   288  C CA  . GLY A 1 374 ? 2.356   -16.737 -26.615 1.00 115.64 ? 47  GLY B CA  1 
ATOM   289  C C   . GLY A 1 374 ? 1.005   -16.137 -26.957 1.00 97.30  ? 47  GLY B C   1 
ATOM   290  O O   . GLY A 1 374 ? 0.036   -16.865 -27.188 1.00 88.89  ? 47  GLY B O   1 
ATOM   291  N N   . ILE A 1 375 ? 0.918   -14.802 -26.987 1.00 94.61  ? 48  ILE B N   1 
ATOM   292  C CA  . ILE A 1 375 ? -0.344  -14.140 -27.314 1.00 92.80  ? 48  ILE B CA  1 
ATOM   293  C C   . ILE A 1 375 ? -0.765  -14.466 -28.742 1.00 99.82  ? 48  ILE B C   1 
ATOM   294  O O   . ILE A 1 375 ? -1.939  -14.755 -29.007 1.00 97.37  ? 48  ILE B O   1 
ATOM   295  C CB  . ILE A 1 375 ? -0.231  -12.619 -27.087 1.00 85.31  ? 48  ILE B CB  1 
ATOM   296  C CG1 . ILE A 1 375 ? 0.096   -12.310 -25.623 1.00 83.66  ? 48  ILE B CG1 1 
ATOM   297  C CG2 . ILE A 1 375 ? -1.512  -11.902 -27.515 1.00 84.58  ? 48  ILE B CG2 1 
ATOM   298  C CD1 . ILE A 1 375 ? -1.118  -12.258 -24.717 1.00 91.75  ? 48  ILE B CD1 1 
ATOM   299  N N   . THR A 1 376 ? 0.183   -14.432 -29.684 1.00 100.04 ? 49  THR B N   1 
ATOM   300  C CA  . THR A 1 376 ? -0.142  -14.743 -31.073 1.00 94.04  ? 49  THR B CA  1 
ATOM   301  C C   . THR A 1 376 ? -0.655  -16.171 -31.213 1.00 90.25  ? 49  THR B C   1 
ATOM   302  O O   . THR A 1 376 ? -1.625  -16.422 -31.940 1.00 76.53  ? 49  THR B O   1 
ATOM   303  C CB  . THR A 1 376 ? 1.079   -14.519 -31.970 1.00 95.06  ? 49  THR B CB  1 
ATOM   304  O OG1 . THR A 1 376 ? 2.252   -15.059 -31.346 1.00 90.66  ? 49  THR B OG1 1 
ATOM   305  C CG2 . THR A 1 376 ? 1.283   -13.037 -32.233 1.00 102.93 ? 49  THR B CG2 1 
ATOM   306  N N   . ASN A 1 377 ? -0.027  -17.118 -30.514 1.00 106.07 ? 50  ASN B N   1 
ATOM   307  C CA  . ASN A 1 377 ? -0.477  -18.502 -30.587 1.00 97.42  ? 50  ASN B CA  1 
ATOM   308  C C   . ASN A 1 377 ? -1.865  -18.663 -29.977 1.00 92.35  ? 50  ASN B C   1 
ATOM   309  O O   . ASN A 1 377 ? -2.693  -19.419 -30.497 1.00 92.18  ? 50  ASN B O   1 
ATOM   310  C CB  . ASN A 1 377 ? 0.526   -19.416 -29.891 1.00 80.27  ? 50  ASN B CB  1 
ATOM   311  C CG  . ASN A 1 377 ? 0.024   -20.834 -29.772 1.00 112.13 ? 50  ASN B CG  1 
ATOM   312  O OD1 . ASN A 1 377 ? -0.249  -21.493 -30.777 1.00 117.38 ? 50  ASN B OD1 1 
ATOM   313  N ND2 . ASN A 1 377 ? -0.122  -21.308 -28.543 1.00 152.07 ? 50  ASN B ND2 1 
ATOM   314  N N   . LYS A 1 378 ? -2.135  -17.964 -28.868 1.00 87.38  ? 51  LYS B N   1 
ATOM   315  C CA  . LYS A 1 378 ? -3.488  -17.944 -28.319 1.00 76.81  ? 51  LYS B CA  1 
ATOM   316  C C   . LYS A 1 378 ? -4.489  -17.467 -29.360 1.00 88.30  ? 51  LYS B C   1 
ATOM   317  O O   . LYS A 1 378 ? -5.553  -18.070 -29.537 1.00 87.05  ? 51  LYS B O   1 
ATOM   318  C CB  . LYS A 1 378 ? -3.560  -17.047 -27.082 1.00 96.31  ? 51  LYS B CB  1 
ATOM   319  C CG  . LYS A 1 378 ? -2.823  -17.547 -25.853 1.00 124.06 ? 51  LYS B CG  1 
ATOM   320  C CD  . LYS A 1 378 ? -2.997  -16.552 -24.713 1.00 106.41 ? 51  LYS B CD  1 
ATOM   321  C CE  . LYS A 1 378 ? -2.321  -17.009 -23.434 1.00 79.77  ? 51  LYS B CE  1 
ATOM   322  N NZ  . LYS A 1 378 ? -2.510  -15.997 -22.356 1.00 70.54  ? 51  LYS B NZ  1 
ATOM   323  N N   . VAL A 1 379 ? -4.159  -16.382 -30.065 1.00 106.13 ? 52  VAL B N   1 
ATOM   324  C CA  . VAL A 1 379 ? -5.087  -15.812 -31.039 1.00 103.08 ? 52  VAL B CA  1 
ATOM   325  C C   . VAL A 1 379 ? -5.399  -16.823 -32.134 1.00 87.35  ? 52  VAL B C   1 
ATOM   326  O O   . VAL A 1 379 ? -6.564  -17.149 -32.387 1.00 80.66  ? 52  VAL B O   1 
ATOM   327  C CB  . VAL A 1 379 ? -4.521  -14.504 -31.620 1.00 100.11 ? 52  VAL B CB  1 
ATOM   328  C CG1 . VAL A 1 379 ? -5.417  -13.988 -32.734 1.00 113.78 ? 52  VAL B CG1 1 
ATOM   329  C CG2 . VAL A 1 379 ? -4.380  -13.462 -30.525 1.00 88.40  ? 52  VAL B CG2 1 
ATOM   330  N N   . ASN A 1 380 ? -4.361  -17.350 -32.789 1.00 79.35  ? 53  ASN B N   1 
ATOM   331  C CA  . ASN A 1 380 ? -4.587  -18.274 -33.897 1.00 97.23  ? 53  ASN B CA  1 
ATOM   332  C C   . ASN A 1 380 ? -5.286  -19.544 -33.430 1.00 104.89 ? 53  ASN B C   1 
ATOM   333  O O   . ASN A 1 380 ? -6.137  -20.090 -34.142 1.00 126.10 ? 53  ASN B O   1 
ATOM   334  C CB  . ASN A 1 380 ? -3.263  -18.610 -34.580 1.00 107.01 ? 53  ASN B CB  1 
ATOM   335  C CG  . ASN A 1 380 ? -2.546  -17.381 -35.088 1.00 118.42 ? 53  ASN B CG  1 
ATOM   336  O OD1 . ASN A 1 380 ? -3.031  -16.685 -35.981 1.00 99.94  ? 53  ASN B OD1 1 
ATOM   337  N ND2 . ASN A 1 380 ? -1.384  -17.098 -34.512 1.00 130.65 ? 53  ASN B ND2 1 
ATOM   338  N N   . SER A 1 381 ? -4.948  -20.032 -32.235 1.00 84.19  ? 54  SER B N   1 
ATOM   339  C CA  . SER A 1 381 ? -5.598  -21.240 -31.743 1.00 91.87  ? 54  SER B CA  1 
ATOM   340  C C   . SER A 1 381 ? -7.063  -20.981 -31.415 1.00 96.44  ? 54  SER B C   1 
ATOM   341  O O   . SER A 1 381 ? -7.929  -21.805 -31.728 1.00 99.80  ? 54  SER B O   1 
ATOM   342  C CB  . SER A 1 381 ? -4.866  -21.772 -30.516 1.00 96.09  ? 54  SER B CB  1 
ATOM   343  O OG  . SER A 1 381 ? -5.222  -21.019 -29.372 1.00 115.71 ? 54  SER B OG  1 
ATOM   344  N N   . VAL A 1 382 ? -7.344  -19.836 -30.799 1.00 93.97  ? 55  VAL B N   1 
ATOM   345  C CA  . VAL A 1 382 ? -8.763  -19.496 -30.493 1.00 97.99  ? 55  VAL B CA  1 
ATOM   346  C C   . VAL A 1 382 ? -9.555  -19.501 -31.802 1.00 96.50  ? 55  VAL B C   1 
ATOM   347  O O   . VAL A 1 382 ? -10.705 -19.974 -31.792 1.00 93.14  ? 55  VAL B O   1 
ATOM   348  C CB  . VAL A 1 382 ? -8.887  -18.152 -29.754 1.00 85.45  ? 55  VAL B CB  1 
ATOM   349  C CG1 . VAL A 1 382 ? -10.303 -17.604 -29.811 1.00 95.35  ? 55  VAL B CG1 1 
ATOM   350  C CG2 . VAL A 1 382 ? -8.418  -18.262 -28.313 1.00 94.01  ? 55  VAL B CG2 1 
ATOM   351  N N   . ILE A 1 383 ? -8.951  -19.029 -32.894 1.00 97.59  ? 56  ILE B N   1 
ATOM   352  C CA  . ILE A 1 383 ? -9.715  -18.930 -34.170 1.00 85.72  ? 56  ILE B CA  1 
ATOM   353  C C   . ILE A 1 383 ? -10.328 -20.302 -34.450 1.00 101.57 ? 56  ILE B C   1 
ATOM   354  O O   . ILE A 1 383 ? -11.502 -20.350 -34.852 1.00 118.09 ? 56  ILE B O   1 
ATOM   355  C CB  . ILE A 1 383 ? -8.830  -18.474 -35.343 1.00 81.69  ? 56  ILE B CB  1 
ATOM   356  C CG1 . ILE A 1 383 ? -7.976  -17.256 -34.988 1.00 79.82  ? 56  ILE B CG1 1 
ATOM   357  C CG2 . ILE A 1 383 ? -9.674  -18.224 -36.582 1.00 69.95  ? 56  ILE B CG2 1 
ATOM   358  C CD1 . ILE A 1 383 ? -8.758  -16.109 -34.412 1.00 117.54 ? 56  ILE B CD1 1 
ATOM   359  N N   . GLU A 1 384 ? -9.556  -21.371 -34.248 1.00 107.06 ? 57  GLU B N   1 
ATOM   360  C CA  . GLU A 1 384 ? -10.075 -22.724 -34.569 1.00 106.78 ? 57  GLU B CA  1 
ATOM   361  C C   . GLU A 1 384 ? -11.452 -22.711 -33.902 1.00 107.13 ? 57  GLU B C   1 
ATOM   362  O O   . GLU A 1 384 ? -11.515 -22.441 -32.689 1.00 81.60  ? 57  GLU B O   1 
ATOM   363  C CB  . GLU A 1 384 ? -9.084  -23.795 -34.121 1.00 84.76  ? 57  GLU B CB  1 
ATOM   364  C CG  . GLU A 1 384 ? -7.795  -23.780 -34.919 1.00 117.00 ? 57  GLU B CG  1 
ATOM   365  C CD  . GLU A 1 384 ? -6.964  -25.046 -34.803 1.00 164.80 ? 57  GLU B CD  1 
ATOM   366  O OE1 . GLU A 1 384 ? -7.393  -25.969 -34.083 1.00 173.20 ? 57  GLU B OE1 1 
ATOM   367  O OE2 . GLU A 1 384 ? -5.893  -25.109 -35.436 1.00 175.92 ? 57  GLU B OE2 1 
ATOM   368  N N   . LYS A 1 385 ? -12.498 -22.875 -34.710 1.00 108.61 ? 58  LYS B N   1 
ATOM   369  C CA  . LYS A 1 385 ? -13.878 -22.942 -34.175 1.00 97.23  ? 58  LYS B CA  1 
ATOM   370  C C   . LYS A 1 385 ? -14.458 -24.280 -34.621 1.00 112.42 ? 58  LYS B C   1 
ATOM   371  O O   . LYS A 1 385 ? -15.395 -24.766 -33.961 1.00 89.81  ? 58  LYS B O   1 
ATOM   372  C CB  . LYS A 1 385 ? -14.710 -21.770 -34.693 1.00 114.38 ? 58  LYS B CB  1 
ATOM   373  C CG  . LYS A 1 385 ? -14.506 -20.471 -33.928 1.00 111.31 ? 58  LYS B CG  1 
ATOM   374  C CD  . LYS A 1 385 ? -14.484 -20.648 -32.426 1.00 92.44  ? 58  LYS B CD  1 
ATOM   375  C CE  . LYS A 1 385 ? -14.273 -19.346 -31.684 1.00 96.12  ? 58  LYS B CE  1 
ATOM   376  N NZ  . LYS A 1 385 ? -13.033 -18.665 -32.121 1.00 151.41 ? 58  LYS B NZ  1 
ATOM   377  N N   . MET A 1 386 ? -13.925 -24.834 -35.712 1.00 137.74 ? 59  MET B N   1 
ATOM   378  C CA  . MET A 1 386 ? -14.387 -26.184 -36.157 1.00 147.24 ? 59  MET B CA  1 
ATOM   379  C C   . MET A 1 386 ? -15.864 -26.396 -36.029 1.00 152.05 ? 59  MET B C   1 
ATOM   380  O O   . MET A 1 386 ? -16.279 -27.296 -35.273 1.00 134.93 ? 59  MET B O   1 
ATOM   381  C CB  . MET A 1 386 ? -13.633 -27.258 -35.323 1.00 102.69 ? 59  MET B CB  1 
ATOM   382  C CG  . MET A 1 386 ? -12.145 -27.298 -35.590 1.00 108.99 ? 59  MET B CG  1 
ATOM   383  S SD  . MET A 1 386 ? -11.791 -27.666 -37.325 1.00 154.02 ? 59  MET B SD  1 
ATOM   384  C CE  . MET A 1 386 ? -12.383 -29.354 -37.431 1.00 150.46 ? 59  MET B CE  1 
ATOM   385  N N   . ASN A 1 387 ? -16.651 -25.602 -36.757 1.00 131.87 ? 60  ASN B N   1 
ATOM   386  C CA  . ASN A 1 387 ? -18.155 -25.803 -36.785 1.00 156.17 ? 60  ASN B CA  1 
ATOM   387  C C   . ASN A 1 387 ? -18.450 -27.251 -37.155 1.00 188.02 ? 60  ASN B C   1 
ATOM   388  O O   . ASN A 1 387 ? -17.600 -27.909 -37.782 1.00 191.10 ? 60  ASN B O   1 
ATOM   389  C CB  . ASN A 1 387 ? -18.805 -24.870 -37.766 1.00 158.50 ? 60  ASN B CB  1 
ATOM   390  C CG  . ASN A 1 387 ? -18.462 -25.192 -39.205 1.00 150.39 ? 60  ASN B CG  1 
ATOM   391  O OD1 . ASN A 1 387 ? -17.298 -25.143 -39.596 1.00 162.02 ? 60  ASN B OD1 1 
ATOM   392  N ND2 . ASN A 1 387 ? -19.466 -25.529 -39.998 1.00 147.90 ? 60  ASN B ND2 1 
ATOM   393  N N   . THR A 1 388 ? -19.655 -27.713 -36.820 1.00 209.35 ? 61  THR B N   1 
ATOM   394  C CA  . THR A 1 388 ? -20.075 -29.093 -37.181 1.00 225.43 ? 61  THR B CA  1 
ATOM   395  C C   . THR A 1 388 ? -20.002 -29.272 -38.701 1.00 219.37 ? 61  THR B C   1 
ATOM   396  O O   . THR A 1 388 ? -20.112 -28.261 -39.421 1.00 208.96 ? 61  THR B O   1 
ATOM   397  C CB  . THR A 1 388 ? -21.475 -29.410 -36.643 1.00 215.00 ? 61  THR B CB  1 
ATOM   398  O OG1 . THR A 1 388 ? -22.326 -28.309 -36.963 1.00 210.09 ? 61  THR B OG1 1 
ATOM   399  C CG2 . THR A 1 388 ? -21.488 -29.661 -35.152 1.00 182.32 ? 61  THR B CG2 1 
ATOM   400  N N   . GLN A 1 389 ? -19.840 -30.513 -39.163 1.00 226.78 ? 62  GLN B N   1 
ATOM   401  C CA  . GLN A 1 389 ? -19.698 -30.758 -40.626 1.00 228.07 ? 62  GLN B CA  1 
ATOM   402  C C   . GLN A 1 389 ? -20.960 -30.295 -41.315 1.00 233.76 ? 62  GLN B C   1 
ATOM   403  O O   . GLN A 1 389 ? -21.983 -30.135 -40.623 1.00 212.72 ? 62  GLN B O   1 
ATOM   404  C CB  . GLN A 1 389 ? -19.242 -32.226 -40.838 1.00 226.81 ? 62  GLN B CB  1 
ATOM   405  C CG  . GLN A 1 389 ? -19.152 -32.622 -42.305 1.00 218.94 ? 62  GLN B CG  1 
ATOM   406  C CD  . GLN A 1 389 ? -18.852 -34.089 -42.489 1.00 192.44 ? 62  GLN B CD  1 
ATOM   407  O OE1 . GLN A 1 389 ? -18.692 -34.836 -41.527 1.00 175.44 ? 62  GLN B OE1 1 
ATOM   408  N NE2 . GLN A 1 389 ? -18.773 -34.514 -43.739 1.00 177.10 ? 62  GLN B NE2 1 
ATOM   409  N N   . PHE A 1 390 ? -20.896 -30.067 -42.630 1.00 222.70 ? 63  PHE B N   1 
ATOM   410  C CA  . PHE A 1 390 ? -22.103 -29.658 -43.432 1.00 214.41 ? 63  PHE B CA  1 
ATOM   411  C C   . PHE A 1 390 ? -22.695 -31.042 -43.755 1.00 233.71 ? 63  PHE B C   1 
ATOM   412  O O   . PHE A 1 390 ? -22.292 -31.639 -44.772 1.00 271.46 ? 63  PHE B O   1 
ATOM   413  C CB  . PHE A 1 390 ? -21.692 -28.923 -44.693 1.00 217.62 ? 63  PHE B CB  1 
ATOM   414  C CG  . PHE A 1 390 ? -20.946 -27.637 -44.443 1.00 221.64 ? 63  PHE B CG  1 
ATOM   415  C CD1 . PHE A 1 390 ? -21.519 -26.617 -43.701 1.00 220.36 ? 63  PHE B CD1 1 
ATOM   416  C CD2 . PHE A 1 390 ? -19.670 -27.447 -44.947 1.00 225.31 ? 63  PHE B CD2 1 
ATOM   417  C CE1 . PHE A 1 390 ? -20.833 -25.435 -43.471 1.00 217.10 ? 63  PHE B CE1 1 
ATOM   418  C CE2 . PHE A 1 390 ? -18.985 -26.264 -44.716 1.00 212.80 ? 63  PHE B CE2 1 
ATOM   419  C CZ  . PHE A 1 390 ? -19.569 -25.260 -43.980 1.00 208.79 ? 63  PHE B CZ  1 
ATOM   420  N N   . THR A 1 391 ? -23.629 -31.515 -42.925 1.00 236.21 ? 64  THR B N   1 
ATOM   421  C CA  . THR A 1 391 ? -24.177 -32.886 -43.114 1.00 222.28 ? 64  THR B CA  1 
ATOM   422  C C   . THR A 1 391 ? -25.347 -32.884 -44.107 1.00 213.61 ? 64  THR B C   1 
ATOM   423  O O   . THR A 1 391 ? -26.204 -33.777 -43.985 1.00 176.51 ? 64  THR B O   1 
ATOM   424  C CB  . THR A 1 391 ? -24.559 -33.489 -41.757 1.00 190.71 ? 64  THR B CB  1 
ATOM   425  O OG1 . THR A 1 391 ? -25.291 -32.502 -41.032 1.00 187.10 ? 64  THR B OG1 1 
ATOM   426  C CG2 . THR A 1 391 ? -23.357 -33.916 -40.945 1.00 156.49 ? 64  THR B CG2 1 
ATOM   427  N N   . ALA A 1 392 ? -25.357 -31.956 -45.070 1.00 211.60 ? 65  ALA B N   1 
ATOM   428  C CA  . ALA A 1 392 ? -26.430 -31.931 -46.088 1.00 183.03 ? 65  ALA B CA  1 
ATOM   429  C C   . ALA A 1 392 ? -27.749 -32.218 -45.378 1.00 201.30 ? 65  ALA B C   1 
ATOM   430  O O   . ALA A 1 392 ? -28.377 -33.247 -45.691 1.00 202.00 ? 65  ALA B O   1 
ATOM   431  C CB  . ALA A 1 392 ? -26.158 -32.969 -47.143 1.00 159.47 ? 65  ALA B CB  1 
ATOM   432  N N   . VAL A 1 393 ? -28.155 -31.339 -44.462 1.00 217.75 ? 66  VAL B N   1 
ATOM   433  C CA  . VAL A 1 393 ? -29.346 -31.648 -43.670 1.00 208.23 ? 66  VAL B CA  1 
ATOM   434  C C   . VAL A 1 393 ? -30.466 -30.636 -43.929 1.00 210.51 ? 66  VAL B C   1 
ATOM   435  O O   . VAL A 1 393 ? -30.358 -29.469 -43.528 1.00 210.18 ? 66  VAL B O   1 
ATOM   436  C CB  . VAL A 1 393 ? -29.029 -31.731 -42.169 1.00 194.30 ? 66  VAL B CB  1 
ATOM   437  C CG1 . VAL A 1 393 ? -30.283 -31.765 -41.426 1.00 185.37 ? 66  VAL B CG1 1 
ATOM   438  C CG2 . VAL A 1 393 ? -28.299 -33.018 -41.870 1.00 187.77 ? 66  VAL B CG2 1 
ATOM   439  N N   . GLY A 1 394 ? -31.580 -31.117 -44.491 1.00 222.90 ? 67  GLY B N   1 
ATOM   440  C CA  . GLY A 1 394 ? -32.838 -30.358 -44.592 1.00 224.38 ? 67  GLY B CA  1 
ATOM   441  C C   . GLY A 1 394 ? -33.999 -31.341 -44.783 1.00 238.65 ? 67  GLY B C   1 
ATOM   442  O O   . GLY A 1 394 ? -33.877 -32.333 -45.509 1.00 233.04 ? 67  GLY B O   1 
ATOM   443  N N   . LYS A 1 395 ? -35.134 -31.053 -44.128 1.00 228.10 ? 68  LYS B N   1 
ATOM   444  C CA  . LYS A 1 395 ? -36.386 -31.792 -44.306 1.00 236.97 ? 68  LYS B CA  1 
ATOM   445  C C   . LYS A 1 395 ? -37.487 -30.745 -44.126 1.00 255.11 ? 68  LYS B C   1 
ATOM   446  O O   . LYS A 1 395 ? -37.230 -29.612 -43.711 1.00 249.08 ? 68  LYS B O   1 
ATOM   447  C CB  . LYS A 1 395 ? -36.503 -32.935 -43.281 1.00 197.83 ? 68  LYS B CB  1 
ATOM   448  C CG  . LYS A 1 395 ? -37.664 -33.925 -43.491 1.00 192.73 ? 68  LYS B CG  1 
ATOM   449  C CD  . LYS A 1 395 ? -37.798 -34.476 -44.890 1.00 203.01 ? 68  LYS B CD  1 
ATOM   450  C CE  . LYS A 1 395 ? -39.145 -35.178 -45.027 1.00 169.59 ? 68  LYS B CE  1 
ATOM   451  N NZ  . LYS A 1 395 ? -39.475 -35.553 -46.426 1.00 152.83 ? 68  LYS B NZ  1 
ATOM   452  N N   . GLU A 1 396 ? -38.725 -31.114 -44.467 1.00 250.56 ? 69  GLU B N   1 
ATOM   453  C CA  . GLU A 1 396 ? -39.895 -30.267 -44.319 1.00 252.89 ? 69  GLU B CA  1 
ATOM   454  C C   . GLU A 1 396 ? -41.104 -31.104 -43.975 1.00 240.67 ? 69  GLU B C   1 
ATOM   455  O O   . GLU A 1 396 ? -41.031 -32.332 -44.026 1.00 228.53 ? 69  GLU B O   1 
ATOM   456  C CB  . GLU A 1 396 ? -40.141 -29.367 -45.543 1.00 246.10 ? 69  GLU B CB  1 
ATOM   457  C CG  . GLU A 1 396 ? -41.307 -28.366 -45.439 1.00 229.41 ? 69  GLU B CG  1 
ATOM   458  C CD  . GLU A 1 396 ? -42.674 -28.985 -45.693 1.00 237.47 ? 69  GLU B CD  1 
ATOM   459  O OE1 . GLU A 1 396 ? -42.742 -30.016 -46.389 1.00 242.58 ? 69  GLU B OE1 1 
ATOM   460  O OE2 . GLU A 1 396 ? -43.680 -28.436 -45.189 1.00 246.29 ? 69  GLU B OE2 1 
ATOM   461  N N   . PHE A 1 397 ? -42.218 -30.464 -43.597 1.00 272.06 ? 70  PHE B N   1 
ATOM   462  C CA  . PHE A 1 397 ? -43.441 -31.219 -43.326 1.00 250.66 ? 70  PHE B CA  1 
ATOM   463  C C   . PHE A 1 397 ? -43.955 -32.199 -44.378 1.00 262.22 ? 70  PHE B C   1 
ATOM   464  O O   . PHE A 1 397 ? -44.724 -33.104 -44.031 1.00 267.61 ? 70  PHE B O   1 
ATOM   465  C CB  . PHE A 1 397 ? -44.543 -30.222 -42.948 1.00 244.41 ? 70  PHE B CB  1 
ATOM   466  C CG  . PHE A 1 397 ? -44.282 -29.453 -41.684 1.00 222.63 ? 70  PHE B CG  1 
ATOM   467  C CD1 . PHE A 1 397 ? -43.360 -29.905 -40.752 1.00 197.22 ? 70  PHE B CD1 1 
ATOM   468  C CD2 . PHE A 1 397 ? -45.000 -28.303 -41.405 1.00 210.44 ? 70  PHE B CD2 1 
ATOM   469  C CE1 . PHE A 1 397 ? -43.141 -29.209 -39.581 1.00 180.05 ? 70  PHE B CE1 1 
ATOM   470  C CE2 . PHE A 1 397 ? -44.784 -27.602 -40.241 1.00 176.15 ? 70  PHE B CE2 1 
ATOM   471  C CZ  . PHE A 1 397 ? -43.855 -28.056 -39.325 1.00 171.51 ? 70  PHE B CZ  1 
ATOM   472  N N   . ASN A 1 398 ? -43.557 -32.042 -45.645 1.00 251.08 ? 71  ASN B N   1 
ATOM   473  C CA  . ASN A 1 398 ? -43.928 -32.969 -46.729 1.00 254.21 ? 71  ASN B CA  1 
ATOM   474  C C   . ASN A 1 398 ? -45.445 -33.110 -46.832 1.00 267.01 ? 71  ASN B C   1 
ATOM   475  O O   . ASN A 1 398 ? -45.952 -34.132 -47.301 1.00 253.88 ? 71  ASN B O   1 
ATOM   476  C CB  . ASN A 1 398 ? -43.276 -34.351 -46.588 1.00 234.77 ? 71  ASN B CB  1 
ATOM   477  C CG  . ASN A 1 398 ? -43.417 -35.214 -47.850 1.00 214.96 ? 71  ASN B CG  1 
ATOM   478  O OD1 . ASN A 1 398 ? -43.460 -34.693 -48.966 1.00 205.89 ? 71  ASN B OD1 1 
ATOM   479  N ND2 . ASN A 1 398 ? -43.505 -36.530 -47.673 1.00 221.79 ? 71  ASN B ND2 1 
ATOM   480  N N   . HIS A 1 399 ? -46.178 -32.090 -46.380 1.00 284.71 ? 72  HIS B N   1 
ATOM   481  C CA  . HIS A 1 399 ? -47.638 -32.027 -46.362 1.00 266.87 ? 72  HIS B CA  1 
ATOM   482  C C   . HIS A 1 399 ? -48.240 -33.049 -45.393 1.00 271.24 ? 72  HIS B C   1 
ATOM   483  O O   . HIS A 1 399 ? -49.470 -33.113 -45.259 1.00 277.18 ? 72  HIS B O   1 
ATOM   484  C CB  . HIS A 1 399 ? -48.230 -32.204 -47.772 1.00 246.60 ? 72  HIS B CB  1 
ATOM   485  C CG  . HIS A 1 399 ? -49.713 -32.023 -47.845 1.00 220.16 ? 72  HIS B CG  1 
ATOM   486  N ND1 . HIS A 1 399 ? -50.346 -30.875 -47.420 1.00 232.65 ? 72  HIS B ND1 1 
ATOM   487  C CD2 . HIS A 1 399 ? -50.689 -32.847 -48.293 1.00 210.29 ? 72  HIS B CD2 1 
ATOM   488  C CE1 . HIS A 1 399 ? -51.648 -31.000 -47.603 1.00 219.60 ? 72  HIS B CE1 1 
ATOM   489  N NE2 . HIS A 1 399 ? -51.883 -32.188 -48.131 1.00 197.82 ? 72  HIS B NE2 1 
ATOM   490  N N   . LEU A 1 400 ? -47.378 -33.836 -44.739 1.00 284.63 ? 73  LEU B N   1 
ATOM   491  C CA  . LEU A 1 400 ? -47.850 -34.866 -43.775 1.00 243.29 ? 73  LEU B CA  1 
ATOM   492  C C   . LEU A 1 400 ? -47.312 -34.525 -42.381 1.00 243.76 ? 73  LEU B C   1 
ATOM   493  O O   . LEU A 1 400 ? -47.090 -35.465 -41.594 1.00 219.14 ? 73  LEU B O   1 
ATOM   494  C CB  . LEU A 1 400 ? -47.349 -36.236 -44.237 1.00 203.15 ? 73  LEU B CB  1 
ATOM   495  C CG  . LEU A 1 400 ? -47.763 -36.645 -45.649 1.00 191.31 ? 73  LEU B CG  1 
ATOM   496  C CD1 . LEU A 1 400 ? -47.365 -38.085 -45.931 1.00 178.05 ? 73  LEU B CD1 1 
ATOM   497  C CD2 . LEU A 1 400 ? -49.260 -36.462 -45.850 1.00 172.39 ? 73  LEU B CD2 1 
ATOM   498  N N   . GLU A 1 401 ? -47.091 -33.238 -42.105 1.00 207.62 ? 74  GLU B N   1 
ATOM   499  C CA  . GLU A 1 401 ? -46.601 -32.793 -40.771 1.00 188.10 ? 74  GLU B CA  1 
ATOM   500  C C   . GLU A 1 401 ? -45.308 -33.530 -40.403 1.00 208.77 ? 74  GLU B C   1 
ATOM   501  O O   . GLU A 1 401 ? -45.176 -33.920 -39.228 1.00 235.58 ? 74  GLU B O   1 
ATOM   502  C CB  . GLU A 1 401 ? -47.678 -32.998 -39.703 1.00 169.49 ? 74  GLU B CB  1 
ATOM   503  C CG  . GLU A 1 401 ? -48.887 -32.098 -39.893 1.00 179.90 ? 74  GLU B CG  1 
ATOM   504  C CD  . GLU A 1 401 ? -50.015 -32.315 -38.899 1.00 171.65 ? 74  GLU B CD  1 
ATOM   505  O OE1 . GLU A 1 401 ? -49.956 -33.307 -38.149 1.00 156.65 ? 74  GLU B OE1 1 
ATOM   506  O OE2 . GLU A 1 401 ? -50.952 -31.492 -38.883 1.00 178.82 ? 74  GLU B OE2 1 
ATOM   507  N N   . LYS A 1 402 ? -44.375 -33.647 -41.351 1.00 222.03 ? 75  LYS B N   1 
ATOM   508  C CA  . LYS A 1 402 ? -43.049 -34.227 -41.017 1.00 196.18 ? 75  LYS B CA  1 
ATOM   509  C C   . LYS A 1 402 ? -42.258 -33.118 -40.323 1.00 189.10 ? 75  LYS B C   1 
ATOM   510  O O   . LYS A 1 402 ? -41.445 -32.459 -40.996 1.00 181.23 ? 75  LYS B O   1 
ATOM   511  C CB  . LYS A 1 402 ? -42.355 -34.754 -42.275 1.00 180.20 ? 75  LYS B CB  1 
ATOM   512  C CG  . LYS A 1 402 ? -43.130 -35.840 -43.007 1.00 186.64 ? 75  LYS B CG  1 
ATOM   513  C CD  . LYS A 1 402 ? -42.352 -36.509 -44.115 1.00 176.36 ? 75  LYS B CD  1 
ATOM   514  C CE  . LYS A 1 402 ? -43.169 -37.540 -44.863 1.00 139.67 ? 75  LYS B CE  1 
ATOM   515  N NZ  . LYS A 1 402 ? -42.423 -38.093 -46.018 1.00 131.17 ? 75  LYS B NZ  1 
ATOM   516  N N   . ARG A 1 403 ? -42.485 -32.936 -39.021 1.00 165.34 ? 76  ARG B N   1 
ATOM   517  C CA  . ARG A 1 403 ? -41.836 -31.834 -38.262 1.00 164.23 ? 76  ARG B CA  1 
ATOM   518  C C   . ARG A 1 403 ? -40.313 -32.000 -38.289 1.00 158.65 ? 76  ARG B C   1 
ATOM   519  O O   . ARG A 1 403 ? -39.620 -31.117 -37.757 1.00 174.92 ? 76  ARG B O   1 
ATOM   520  C CB  . ARG A 1 403 ? -42.370 -31.824 -36.826 1.00 171.82 ? 76  ARG B CB  1 
ATOM   521  C CG  . ARG A 1 403 ? -43.839 -31.452 -36.697 1.00 182.73 ? 76  ARG B CG  1 
ATOM   522  C CD  . ARG A 1 403 ? -44.316 -31.507 -35.259 1.00 181.06 ? 76  ARG B CD  1 
ATOM   523  N NE  . ARG A 1 403 ? -45.717 -31.126 -35.144 1.00 176.97 ? 76  ARG B NE  1 
ATOM   524  C CZ  . ARG A 1 403 ? -46.741 -31.947 -35.353 1.00 205.52 ? 76  ARG B CZ  1 
ATOM   525  N NH1 . ARG A 1 403 ? -47.761 -31.960 -34.514 1.00 230.14 ? 76  ARG B NH1 1 
ATOM   526  N NH2 . ARG A 1 403 ? -46.737 -32.755 -36.398 1.00 206.38 ? 76  ARG B NH2 1 
ATOM   527  N N   . ILE A 1 404 ? -39.806 -33.072 -38.903 1.00 160.26 ? 77  ILE B N   1 
ATOM   528  C CA  . ILE A 1 404 ? -38.329 -33.205 -39.036 1.00 152.67 ? 77  ILE B CA  1 
ATOM   529  C C   . ILE A 1 404 ? -37.836 -31.813 -39.417 1.00 140.12 ? 77  ILE B C   1 
ATOM   530  O O   . ILE A 1 404 ? -36.794 -31.389 -38.896 1.00 114.77 ? 77  ILE B O   1 
ATOM   531  C CB  . ILE A 1 404 ? -37.970 -34.257 -40.098 1.00 146.19 ? 77  ILE B CB  1 
ATOM   532  C CG1 . ILE A 1 404 ? -38.381 -35.663 -39.655 1.00 142.30 ? 77  ILE B CG1 1 
ATOM   533  C CG2 . ILE A 1 404 ? -36.494 -34.182 -40.456 1.00 137.28 ? 77  ILE B CG2 1 
ATOM   534  C CD1 . ILE A 1 404 ? -38.298 -36.700 -40.749 1.00 143.11 ? 77  ILE B CD1 1 
ATOM   535  N N   . GLU A 1 405 ? -38.578 -31.133 -40.287 1.00 151.40 ? 78  GLU B N   1 
ATOM   536  C CA  . GLU A 1 405 ? -38.221 -29.724 -40.613 1.00 164.36 ? 78  GLU B CA  1 
ATOM   537  C C   . GLU A 1 405 ? -38.123 -28.831 -39.407 1.00 139.93 ? 78  GLU B C   1 
ATOM   538  O O   . GLU A 1 405 ? -37.071 -28.190 -39.245 1.00 147.26 ? 78  GLU B O   1 
ATOM   539  C CB  . GLU A 1 405 ? -39.370 -29.131 -41.453 1.00 193.60 ? 78  GLU B CB  1 
ATOM   540  C CG  . GLU A 1 405 ? -39.111 -27.713 -41.917 1.00 199.53 ? 78  GLU B CG  1 
ATOM   541  C CD  . GLU A 1 405 ? -40.247 -27.148 -42.751 1.00 224.59 ? 78  GLU B CD  1 
ATOM   542  O OE1 . GLU A 1 405 ? -41.254 -27.858 -42.921 1.00 236.28 ? 78  GLU B OE1 1 
ATOM   543  O OE2 . GLU A 1 405 ? -40.117 -26.009 -43.238 1.00 229.23 ? 78  GLU B OE2 1 
ATOM   544  N N   . ASN A 1 406 ? -39.154 -28.810 -38.561 1.00 157.39 ? 79  ASN B N   1 
ATOM   545  C CA  . ASN A 1 406 ? -39.133 -27.856 -37.426 1.00 158.78 ? 79  ASN B CA  1 
ATOM   546  C C   . ASN A 1 406 ? -38.173 -28.386 -36.400 1.00 160.54 ? 79  ASN B C   1 
ATOM   547  O O   . ASN A 1 406 ? -37.623 -27.593 -35.629 1.00 159.00 ? 79  ASN B O   1 
ATOM   548  C CB  . ASN A 1 406 ? -40.537 -27.698 -36.819 1.00 155.62 ? 79  ASN B CB  1 
ATOM   549  C CG  . ASN A 1 406 ? -41.328 -26.562 -37.443 1.00 142.93 ? 79  ASN B CG  1 
ATOM   550  O OD1 . ASN A 1 406 ? -40.976 -26.055 -38.506 1.00 115.82 ? 79  ASN B OD1 1 
ATOM   551  N ND2 . ASN A 1 406 ? -42.390 -26.139 -36.764 1.00 150.48 ? 79  ASN B ND2 1 
ATOM   552  N N   . LEU A 1 407 ? -37.953 -29.699 -36.349 1.00 148.11 ? 80  LEU B N   1 
ATOM   553  C CA  . LEU A 1 407 ? -36.884 -30.240 -35.521 1.00 133.94 ? 80  LEU B CA  1 
ATOM   554  C C   . LEU A 1 407 ? -35.529 -29.777 -36.036 1.00 134.46 ? 80  LEU B C   1 
ATOM   555  O O   . LEU A 1 407 ? -34.800 -29.084 -35.318 1.00 141.34 ? 80  LEU B O   1 
ATOM   556  C CB  . LEU A 1 407 ? -36.935 -31.764 -35.479 1.00 132.31 ? 80  LEU B CB  1 
ATOM   557  C CG  . LEU A 1 407 ? -38.218 -32.395 -34.956 1.00 152.06 ? 80  LEU B CG  1 
ATOM   558  C CD1 . LEU A 1 407 ? -37.972 -33.859 -34.711 1.00 161.99 ? 80  LEU B CD1 1 
ATOM   559  C CD2 . LEU A 1 407 ? -38.636 -31.705 -33.675 1.00 134.29 ? 80  LEU B CD2 1 
ATOM   560  N N   . ASN A 1 408 ? -35.186 -30.151 -37.275 1.00 116.67 ? 81  ASN B N   1 
ATOM   561  C CA  . ASN A 1 408 ? -33.905 -29.738 -37.844 1.00 122.06 ? 81  ASN B CA  1 
ATOM   562  C C   . ASN A 1 408 ? -33.748 -28.223 -37.839 1.00 128.77 ? 81  ASN B C   1 
ATOM   563  O O   . ASN A 1 408 ? -32.631 -27.712 -37.701 1.00 155.16 ? 81  ASN B O   1 
ATOM   564  C CB  . ASN A 1 408 ? -33.744 -30.274 -39.267 1.00 128.08 ? 81  ASN B CB  1 
ATOM   565  C CG  . ASN A 1 408 ? -32.579 -29.636 -39.998 1.00 138.63 ? 81  ASN B CG  1 
ATOM   566  O OD1 . ASN A 1 408 ? -31.437 -29.693 -39.542 1.00 144.91 ? 81  ASN B OD1 1 
ATOM   567  N ND2 . ASN A 1 408 ? -32.866 -29.003 -41.127 1.00 155.48 ? 81  ASN B ND2 1 
ATOM   568  N N   . LYS A 1 409 ? -34.850 -27.486 -37.993 1.00 107.71 ? 82  LYS B N   1 
ATOM   569  C CA  . LYS A 1 409 ? -34.788 -26.032 -37.889 1.00 128.59 ? 82  LYS B CA  1 
ATOM   570  C C   . LYS A 1 409 ? -34.279 -25.607 -36.517 1.00 156.15 ? 82  LYS B C   1 
ATOM   571  O O   . LYS A 1 409 ? -33.188 -25.035 -36.421 1.00 181.86 ? 82  LYS B O   1 
ATOM   572  C CB  . LYS A 1 409 ? -36.149 -25.396 -38.168 1.00 146.32 ? 82  LYS B CB  1 
ATOM   573  C CG  . LYS A 1 409 ? -36.446 -25.194 -39.641 1.00 166.03 ? 82  LYS B CG  1 
ATOM   574  C CD  . LYS A 1 409 ? -37.860 -24.685 -39.852 1.00 168.73 ? 82  LYS B CD  1 
ATOM   575  C CE  . LYS A 1 409 ? -38.115 -24.349 -41.311 1.00 165.30 ? 82  LYS B CE  1 
ATOM   576  N NZ  . LYS A 1 409 ? -39.525 -23.922 -41.523 1.00 163.72 ? 82  LYS B NZ  1 
ATOM   577  N N   . LYS A 1 410 ? -35.053 -25.877 -35.460 1.00 138.28 ? 83  LYS B N   1 
ATOM   578  C CA  . LYS A 1 410 ? -34.601 -25.622 -34.093 1.00 143.32 ? 83  LYS B CA  1 
ATOM   579  C C   . LYS A 1 410 ? -33.170 -26.070 -33.845 1.00 150.95 ? 83  LYS B C   1 
ATOM   580  O O   . LYS A 1 410 ? -32.399 -25.349 -33.208 1.00 168.28 ? 83  LYS B O   1 
ATOM   581  C CB  . LYS A 1 410 ? -35.455 -26.343 -33.057 1.00 136.58 ? 83  LYS B CB  1 
ATOM   582  C CG  . LYS A 1 410 ? -36.836 -25.872 -32.805 1.00 155.81 ? 83  LYS B CG  1 
ATOM   583  C CD  . LYS A 1 410 ? -37.351 -26.806 -31.737 1.00 171.46 ? 83  LYS B CD  1 
ATOM   584  C CE  . LYS A 1 410 ? -38.714 -26.454 -31.280 1.00 194.65 ? 83  LYS B CE  1 
ATOM   585  N NZ  . LYS A 1 410 ? -39.272 -27.389 -30.266 1.00 181.34 ? 83  LYS B NZ  1 
ATOM   586  N N   . VAL A 1 411 ? -32.834 -27.279 -34.302 1.00 166.49 ? 84  VAL B N   1 
ATOM   587  C CA  . VAL A 1 411 ? -31.513 -27.847 -34.037 1.00 160.46 ? 84  VAL B CA  1 
ATOM   588  C C   . VAL A 1 411 ? -30.419 -26.903 -34.525 1.00 165.97 ? 84  VAL B C   1 
ATOM   589  O O   . VAL A 1 411 ? -29.442 -26.630 -33.814 1.00 173.09 ? 84  VAL B O   1 
ATOM   590  C CB  . VAL A 1 411 ? -31.397 -29.239 -34.685 1.00 171.53 ? 84  VAL B CB  1 
ATOM   591  C CG1 . VAL A 1 411 ? -29.939 -29.643 -34.846 1.00 171.34 ? 84  VAL B CG1 1 
ATOM   592  C CG2 . VAL A 1 411 ? -32.174 -30.275 -33.878 1.00 177.76 ? 84  VAL B CG2 1 
ATOM   593  N N   . ASP A 1 412 ? -30.572 -26.379 -35.742 1.00 153.32 ? 85  ASP B N   1 
ATOM   594  C CA  . ASP A 1 412 ? -29.601 -25.420 -36.257 1.00 158.17 ? 85  ASP B CA  1 
ATOM   595  C C   . ASP A 1 412 ? -29.738 -24.070 -35.562 1.00 151.81 ? 85  ASP B C   1 
ATOM   596  O O   . ASP A 1 412 ? -28.731 -23.452 -35.196 1.00 158.64 ? 85  ASP B O   1 
ATOM   597  C CB  . ASP A 1 412 ? -29.760 -25.271 -37.771 1.00 153.98 ? 85  ASP B CB  1 
ATOM   598  C CG  . ASP A 1 412 ? -29.281 -26.496 -38.535 1.00 165.51 ? 85  ASP B CG  1 
ATOM   599  O OD1 . ASP A 1 412 ? -28.570 -27.334 -37.939 1.00 150.30 ? 85  ASP B OD1 1 
ATOM   600  O OD2 . ASP A 1 412 ? -29.621 -26.624 -39.730 1.00 178.40 ? 85  ASP B OD2 1 
ATOM   601  N N   . ASP A 1 413 ? -30.975 -23.599 -35.370 1.00 142.31 ? 86  ASP B N   1 
ATOM   602  C CA  . ASP A 1 413 ? -31.193 -22.348 -34.648 1.00 136.19 ? 86  ASP B CA  1 
ATOM   603  C C   . ASP A 1 413 ? -30.752 -22.457 -33.195 1.00 143.94 ? 86  ASP B C   1 
ATOM   604  O O   . ASP A 1 413 ? -30.306 -21.465 -32.605 1.00 152.72 ? 86  ASP B O   1 
ATOM   605  C CB  . ASP A 1 413 ? -32.669 -21.943 -34.718 1.00 155.45 ? 86  ASP B CB  1 
ATOM   606  C CG  . ASP A 1 413 ? -33.199 -21.880 -36.143 1.00 155.48 ? 86  ASP B CG  1 
ATOM   607  O OD1 . ASP A 1 413 ? -32.389 -21.717 -37.080 1.00 145.95 ? 86  ASP B OD1 1 
ATOM   608  O OD2 . ASP A 1 413 ? -34.432 -21.985 -36.326 1.00 140.82 ? 86  ASP B OD2 1 
ATOM   609  N N   . GLY A 1 414 ? -30.872 -23.648 -32.602 1.00 167.19 ? 87  GLY B N   1 
ATOM   610  C CA  . GLY A 1 414 ? -30.437 -23.841 -31.230 1.00 164.85 ? 87  GLY B CA  1 
ATOM   611  C C   . GLY A 1 414 ? -28.945 -24.042 -31.086 1.00 146.07 ? 87  GLY B C   1 
ATOM   612  O O   . GLY A 1 414 ? -28.362 -23.631 -30.081 1.00 136.43 ? 87  GLY B O   1 
ATOM   613  N N   . PHE A 1 415 ? -28.304 -24.680 -32.067 1.00 135.01 ? 88  PHE B N   1 
ATOM   614  C CA  . PHE A 1 415 ? -26.845 -24.731 -32.061 1.00 142.08 ? 88  PHE B CA  1 
ATOM   615  C C   . PHE A 1 415 ? -26.254 -23.333 -32.186 1.00 140.14 ? 88  PHE B C   1 
ATOM   616  O O   . PHE A 1 415 ? -25.303 -22.990 -31.475 1.00 140.13 ? 88  PHE B O   1 
ATOM   617  C CB  . PHE A 1 415 ? -26.340 -25.652 -33.170 1.00 170.78 ? 88  PHE B CB  1 
ATOM   618  C CG  . PHE A 1 415 ? -26.437 -27.113 -32.832 1.00 171.71 ? 88  PHE B CG  1 
ATOM   619  C CD1 . PHE A 1 415 ? -26.904 -27.521 -31.592 1.00 142.44 ? 88  PHE B CD1 1 
ATOM   620  C CD2 . PHE A 1 415 ? -26.065 -28.077 -33.753 1.00 182.39 ? 88  PHE B CD2 1 
ATOM   621  C CE1 . PHE A 1 415 ? -26.994 -28.864 -31.277 1.00 127.15 ? 88  PHE B CE1 1 
ATOM   622  C CE2 . PHE A 1 415 ? -26.155 -29.421 -33.444 1.00 170.22 ? 88  PHE B CE2 1 
ATOM   623  C CZ  . PHE A 1 415 ? -26.620 -29.814 -32.206 1.00 142.41 ? 88  PHE B CZ  1 
ATOM   624  N N   . LEU A 1 416 ? -26.875 -22.489 -33.006 1.00 134.77 ? 89  LEU B N   1 
ATOM   625  C CA  . LEU A 1 416 ? -26.424 -21.077 -33.001 1.00 120.92 ? 89  LEU B CA  1 
ATOM   626  C C   . LEU A 1 416 ? -27.148 -20.393 -31.841 1.00 135.07 ? 89  LEU B C   1 
ATOM   627  O O   . LEU A 1 416 ? -28.200 -20.910 -31.436 1.00 145.71 ? 89  LEU B O   1 
ATOM   628  C CB  . LEU A 1 416 ? -26.925 -20.360 -34.254 1.00 129.91 ? 89  LEU B CB  1 
ATOM   629  C CG  . LEU A 1 416 ? -26.202 -20.728 -35.547 1.00 145.74 ? 89  LEU B CG  1 
ATOM   630  C CD1 . LEU A 1 416 ? -26.383 -19.639 -36.593 1.00 145.01 ? 89  LEU B CD1 1 
ATOM   631  C CD2 . LEU A 1 416 ? -24.725 -20.975 -35.285 1.00 137.29 ? 89  LEU B CD2 1 
ATOM   632  N N   . ASP A 1 417 ? -26.675 -19.226 -31.404 1.00 142.08 ? 90  ASP B N   1 
ATOM   633  C CA  . ASP A 1 417 ? -27.282 -18.511 -30.204 1.00 147.17 ? 90  ASP B CA  1 
ATOM   634  C C   . ASP A 1 417 ? -26.853 -19.329 -28.967 1.00 139.94 ? 90  ASP B C   1 
ATOM   635  O O   . ASP A 1 417 ? -27.058 -18.806 -27.860 1.00 129.93 ? 90  ASP B O   1 
ATOM   636  C CB  . ASP A 1 417 ? -28.794 -18.642 -30.077 1.00 143.56 ? 90  ASP B CB  1 
ATOM   637  C CG  . ASP A 1 417 ? -29.531 -17.532 -30.801 1.00 135.34 ? 90  ASP B CG  1 
ATOM   638  O OD1 . ASP A 1 417 ? -28.851 -16.638 -31.331 1.00 155.03 ? 90  ASP B OD1 1 
ATOM   639  O OD2 . ASP A 1 417 ? -30.775 -17.576 -30.834 1.00 133.78 ? 90  ASP B OD2 1 
ATOM   640  N N   . ILE A 1 418 ? -26.308 -20.529 -29.165 1.00 129.30 ? 91  ILE B N   1 
ATOM   641  C CA  . ILE A 1 418 ? -25.726 -21.284 -28.018 1.00 104.25 ? 91  ILE B CA  1 
ATOM   642  C C   . ILE A 1 418 ? -24.216 -21.236 -28.246 1.00 105.53 ? 91  ILE B C   1 
ATOM   643  O O   . ILE A 1 418 ? -23.507 -20.707 -27.374 1.00 126.44 ? 91  ILE B O   1 
ATOM   644  C CB  . ILE A 1 418 ? -26.275 -22.722 -27.930 1.00 115.83 ? 91  ILE B CB  1 
ATOM   645  C CG1 . ILE A 1 418 ? -27.600 -22.767 -27.165 1.00 141.98 ? 91  ILE B CG1 1 
ATOM   646  C CG2 . ILE A 1 418 ? -25.248 -23.661 -27.317 1.00 115.28 ? 91  ILE B CG2 1 
ATOM   647  C CD1 . ILE A 1 418 ? -28.087 -24.165 -26.864 1.00 142.92 ? 91  ILE B CD1 1 
ATOM   648  N N   . TRP A 1 419 ? -23.764 -21.693 -29.417 1.00 111.38 ? 92  TRP B N   1 
ATOM   649  C CA  . TRP A 1 419 ? -22.320 -21.617 -29.761 1.00 122.67 ? 92  TRP B CA  1 
ATOM   650  C C   . TRP A 1 419 ? -21.891 -20.147 -29.792 1.00 116.73 ? 92  TRP B C   1 
ATOM   651  O O   . TRP A 1 419 ? -20.800 -19.844 -29.282 1.00 111.01 ? 92  TRP B O   1 
ATOM   652  C CB  . TRP A 1 419 ? -22.061 -22.302 -31.106 1.00 124.66 ? 92  TRP B CB  1 
ATOM   653  C CG  . TRP A 1 419 ? -22.394 -23.761 -31.116 1.00 143.34 ? 92  TRP B CG  1 
ATOM   654  C CD1 . TRP A 1 419 ? -22.720 -24.542 -30.044 1.00 139.93 ? 92  TRP B CD1 1 
ATOM   655  C CD2 . TRP A 1 419 ? -22.478 -24.613 -32.271 1.00 166.14 ? 92  TRP B CD2 1 
ATOM   656  N NE1 . TRP A 1 419 ? -22.977 -25.823 -30.450 1.00 147.04 ? 92  TRP B NE1 1 
ATOM   657  C CE2 . TRP A 1 419 ? -22.838 -25.897 -31.811 1.00 170.16 ? 92  TRP B CE2 1 
ATOM   658  C CE3 . TRP A 1 419 ? -22.274 -24.419 -33.641 1.00 169.84 ? 92  TRP B CE3 1 
ATOM   659  C CZ2 . TRP A 1 419 ? -22.994 -26.978 -32.675 1.00 190.90 ? 92  TRP B CZ2 1 
ATOM   660  C CZ3 . TRP A 1 419 ? -22.431 -25.487 -34.495 1.00 178.92 ? 92  TRP B CZ3 1 
ATOM   661  C CH2 . TRP A 1 419 ? -22.789 -26.747 -34.016 1.00 199.82 ? 92  TRP B CH2 1 
ATOM   662  N N   . THR A 1 420 ? -22.724 -19.277 -30.374 1.00 99.94  ? 93  THR B N   1 
ATOM   663  C CA  . THR A 1 420 ? -22.403 -17.826 -30.429 1.00 88.15  ? 93  THR B CA  1 
ATOM   664  C C   . THR A 1 420 ? -22.202 -17.310 -29.001 1.00 102.16 ? 93  THR B C   1 
ATOM   665  O O   . THR A 1 420 ? -21.136 -16.721 -28.738 1.00 110.72 ? 93  THR B O   1 
ATOM   666  C CB  . THR A 1 420 ? -23.484 -17.032 -31.174 1.00 94.16  ? 93  THR B CB  1 
ATOM   667  O OG1 . THR A 1 420 ? -24.620 -16.914 -30.317 1.00 125.79 ? 93  THR B OG1 1 
ATOM   668  C CG2 . THR A 1 420 ? -23.882 -17.667 -32.488 1.00 85.97  ? 93  THR B CG2 1 
ATOM   669  N N   . TYR A 1 421 ? -23.182 -17.527 -28.117 1.00 99.38  ? 94  TYR B N   1 
ATOM   670  C CA  . TYR A 1 421 ? -23.005 -17.124 -26.703 1.00 106.79 ? 94  TYR B CA  1 
ATOM   671  C C   . TYR A 1 421 ? -21.711 -17.748 -26.191 1.00 110.95 ? 94  TYR B C   1 
ATOM   672  O O   . TYR A 1 421 ? -20.850 -17.022 -25.671 1.00 137.41 ? 94  TYR B O   1 
ATOM   673  C CB  . TYR A 1 421 ? -24.211 -17.589 -25.889 1.00 115.89 ? 94  TYR B CB  1 
ATOM   674  C CG  . TYR A 1 421 ? -24.070 -17.478 -24.394 1.00 116.65 ? 94  TYR B CG  1 
ATOM   675  C CD1 . TYR A 1 421 ? -23.820 -16.261 -23.786 1.00 105.47 ? 94  TYR B CD1 1 
ATOM   676  C CD2 . TYR A 1 421 ? -24.201 -18.594 -23.585 1.00 129.29 ? 94  TYR B CD2 1 
ATOM   677  C CE1 . TYR A 1 421 ? -23.698 -16.154 -22.411 1.00 118.76 ? 94  TYR B CE1 1 
ATOM   678  C CE2 . TYR A 1 421 ? -24.084 -18.505 -22.209 1.00 142.08 ? 94  TYR B CE2 1 
ATOM   679  C CZ  . TYR A 1 421 ? -23.831 -17.280 -21.620 1.00 141.17 ? 94  TYR B CZ  1 
ATOM   680  O OH  . TYR A 1 421 ? -23.712 -17.187 -20.255 1.00 144.02 ? 94  TYR B OH  1 
ATOM   681  N N   . ASN A 1 422 ? -21.574 -19.057 -26.367 1.00 94.62  ? 95  ASN B N   1 
ATOM   682  C CA  . ASN A 1 422 ? -20.391 -19.749 -25.867 1.00 110.30 ? 95  ASN B CA  1 
ATOM   683  C C   . ASN A 1 422 ? -19.119 -19.131 -26.426 1.00 106.79 ? 95  ASN B C   1 
ATOM   684  O O   . ASN A 1 422 ? -18.108 -19.026 -25.721 1.00 106.50 ? 95  ASN B O   1 
ATOM   685  C CB  . ASN A 1 422 ? -20.459 -21.233 -26.219 1.00 107.64 ? 95  ASN B CB  1 
ATOM   686  C CG  . ASN A 1 422 ? -21.362 -22.002 -25.290 1.00 114.28 ? 95  ASN B CG  1 
ATOM   687  O OD1 . ASN A 1 422 ? -20.932 -22.485 -24.244 1.00 118.11 ? 95  ASN B OD1 1 
ATOM   688  N ND2 . ASN A 1 422 ? -22.628 -22.117 -25.663 1.00 123.00 ? 95  ASN B ND2 1 
ATOM   689  N N   . ALA A 1 423 ? -19.150 -18.713 -27.692 1.00 85.09  ? 96  ALA B N   1 
ATOM   690  C CA  . ALA A 1 423 ? -17.975 -18.093 -28.291 1.00 86.92  ? 96  ALA B CA  1 
ATOM   691  C C   . ALA A 1 423 ? -17.718 -16.712 -27.703 1.00 107.24 ? 96  ALA B C   1 
ATOM   692  O O   . ALA A 1 423 ? -16.562 -16.340 -27.470 1.00 125.25 ? 96  ALA B O   1 
ATOM   693  C CB  . ALA A 1 423 ? -18.138 -18.012 -29.807 1.00 80.20  ? 96  ALA B CB  1 
ATOM   694  N N   . GLU A 1 424 ? -18.781 -15.935 -27.464 1.00 102.09 ? 97  GLU B N   1 
ATOM   695  C CA  . GLU A 1 424 ? -18.625 -14.647 -26.794 1.00 105.03 ? 97  GLU B CA  1 
ATOM   696  C C   . GLU A 1 424 ? -17.933 -14.814 -25.450 1.00 109.90 ? 97  GLU B C   1 
ATOM   697  O O   . GLU A 1 424 ? -17.094 -13.993 -25.063 1.00 107.79 ? 97  GLU B O   1 
ATOM   698  C CB  . GLU A 1 424 ? -19.986 -13.978 -26.599 1.00 101.05 ? 97  GLU B CB  1 
ATOM   699  C CG  . GLU A 1 424 ? -20.685 -13.547 -27.876 1.00 101.23 ? 97  GLU B CG  1 
ATOM   700  C CD  . GLU A 1 424 ? -22.064 -12.970 -27.609 1.00 122.13 ? 97  GLU B CD  1 
ATOM   701  O OE1 . GLU A 1 424 ? -22.541 -13.072 -26.458 1.00 142.67 ? 97  GLU B OE1 1 
ATOM   702  O OE2 . GLU A 1 424 ? -22.670 -12.411 -28.546 1.00 102.63 ? 97  GLU B OE2 1 
ATOM   703  N N   . LEU A 1 425 ? -18.273 -15.882 -24.727 1.00 95.06  ? 98  LEU B N   1 
ATOM   704  C CA  . LEU A 1 425 ? -17.631 -16.150 -23.447 1.00 87.81  ? 98  LEU B CA  1 
ATOM   705  C C   . LEU A 1 425 ? -16.148 -16.443 -23.628 1.00 94.47  ? 98  LEU B C   1 
ATOM   706  O O   . LEU A 1 425 ? -15.312 -15.937 -22.870 1.00 113.66 ? 98  LEU B O   1 
ATOM   707  C CB  . LEU A 1 425 ? -18.329 -17.320 -22.755 1.00 96.44  ? 98  LEU B CB  1 
ATOM   708  C CG  . LEU A 1 425 ? -19.782 -17.050 -22.370 1.00 110.11 ? 98  LEU B CG  1 
ATOM   709  C CD1 . LEU A 1 425 ? -20.446 -18.296 -21.791 1.00 111.06 ? 98  LEU B CD1 1 
ATOM   710  C CD2 . LEU A 1 425 ? -19.863 -15.872 -21.418 1.00 102.74 ? 98  LEU B CD2 1 
ATOM   711  N N   . LEU A 1 426 ? -15.803 -17.250 -24.635 1.00 93.65  ? 99  LEU B N   1 
ATOM   712  C CA  . LEU A 1 426 ? -14.406 -17.615 -24.854 1.00 84.52  ? 99  LEU B CA  1 
ATOM   713  C C   . LEU A 1 426 ? -13.571 -16.396 -25.218 1.00 95.48  ? 99  LEU B C   1 
ATOM   714  O O   . LEU A 1 426 ? -12.411 -16.279 -24.804 1.00 107.60 ? 99  LEU B O   1 
ATOM   715  C CB  . LEU A 1 426 ? -14.308 -18.678 -25.947 1.00 70.23  ? 99  LEU B CB  1 
ATOM   716  C CG  . LEU A 1 426 ? -12.920 -19.196 -26.324 1.00 72.78  ? 99  LEU B CG  1 
ATOM   717  C CD1 . LEU A 1 426 ? -12.127 -19.564 -25.079 1.00 104.98 ? 99  LEU B CD1 1 
ATOM   718  C CD2 . LEU A 1 426 ? -13.035 -20.387 -27.264 1.00 95.12  ? 99  LEU B CD2 1 
ATOM   719  N N   . VAL A 1 427 ? -14.138 -15.482 -26.007 1.00 91.61  ? 100 VAL B N   1 
ATOM   720  C CA  . VAL A 1 427 ? -13.472 -14.211 -26.279 1.00 101.43 ? 100 VAL B CA  1 
ATOM   721  C C   . VAL A 1 427 ? -13.211 -13.467 -24.975 1.00 110.08 ? 100 VAL B C   1 
ATOM   722  O O   . VAL A 1 427 ? -12.072 -13.104 -24.662 1.00 107.90 ? 100 VAL B O   1 
ATOM   723  C CB  . VAL A 1 427 ? -14.307 -13.362 -27.253 1.00 97.61  ? 100 VAL B CB  1 
ATOM   724  C CG1 . VAL A 1 427 ? -13.590 -12.065 -27.584 1.00 105.07 ? 100 VAL B CG1 1 
ATOM   725  C CG2 . VAL A 1 427 ? -14.569 -14.148 -28.524 1.00 81.59  ? 100 VAL B CG2 1 
ATOM   726  N N   . LEU A 1 428 ? -14.268 -13.254 -24.185 1.00 105.11 ? 101 LEU B N   1 
ATOM   727  C CA  . LEU A 1 428 ? -14.130 -12.551 -22.913 1.00 110.74 ? 101 LEU B CA  1 
ATOM   728  C C   . LEU A 1 428 ? -13.111 -13.240 -22.014 1.00 116.47 ? 101 LEU B C   1 
ATOM   729  O O   . LEU A 1 428 ? -12.281 -12.585 -21.374 1.00 129.32 ? 101 LEU B O   1 
ATOM   730  C CB  . LEU A 1 428 ? -15.489 -12.475 -22.219 1.00 96.73  ? 101 LEU B CB  1 
ATOM   731  C CG  . LEU A 1 428 ? -16.588 -11.688 -22.930 1.00 100.64 ? 101 LEU B CG  1 
ATOM   732  C CD1 . LEU A 1 428 ? -17.941 -12.033 -22.333 1.00 80.52  ? 101 LEU B CD1 1 
ATOM   733  C CD2 . LEU A 1 428 ? -16.331 -10.193 -22.862 1.00 130.35 ? 101 LEU B CD2 1 
ATOM   734  N N   . LEU A 1 429 ? -13.171 -14.571 -21.958 1.00 107.28 ? 102 LEU B N   1 
ATOM   735  C CA  . LEU A 1 429 ? -12.214 -15.357 -21.187 1.00 106.23 ? 102 LEU B CA  1 
ATOM   736  C C   . LEU A 1 429 ? -10.782 -15.057 -21.609 1.00 131.25 ? 102 LEU B C   1 
ATOM   737  O O   . LEU A 1 429 ? -9.963  -14.596 -20.806 1.00 151.85 ? 102 LEU B O   1 
ATOM   738  C CB  . LEU A 1 429 ? -12.515 -16.842 -21.372 1.00 109.95 ? 102 LEU B CB  1 
ATOM   739  C CG  . LEU A 1 429 ? -13.602 -17.494 -20.531 1.00 111.91 ? 102 LEU B CG  1 
ATOM   740  C CD1 . LEU A 1 429 ? -14.148 -18.681 -21.285 1.00 130.33 ? 102 LEU B CD1 1 
ATOM   741  C CD2 . LEU A 1 429 ? -13.031 -17.940 -19.208 1.00 117.92 ? 102 LEU B CD2 1 
ATOM   742  N N   . GLU A 1 430 ? -10.464 -15.332 -22.878 1.00 118.13 ? 103 GLU B N   1 
ATOM   743  C CA  . GLU A 1 430 ? -9.114  -15.099 -23.376 1.00 109.88 ? 103 GLU B CA  1 
ATOM   744  C C   . GLU A 1 430 ? -8.694  -13.648 -23.209 1.00 112.97 ? 103 GLU B C   1 
ATOM   745  O O   . GLU A 1 430 ? -7.512  -13.370 -22.988 1.00 128.38 ? 103 GLU B O   1 
ATOM   746  C CB  . GLU A 1 430 ? -9.014  -15.512 -24.845 1.00 119.86 ? 103 GLU B CB  1 
ATOM   747  C CG  . GLU A 1 430 ? -7.608  -15.896 -25.295 1.00 138.87 ? 103 GLU B CG  1 
ATOM   748  C CD  . GLU A 1 430 ? -6.995  -17.001 -24.453 1.00 150.28 ? 103 GLU B CD  1 
ATOM   749  O OE1 . GLU A 1 430 ? -7.454  -18.158 -24.561 1.00 143.76 ? 103 GLU B OE1 1 
ATOM   750  O OE2 . GLU A 1 430 ? -6.045  -16.717 -23.693 1.00 173.09 ? 103 GLU B OE2 1 
ATOM   751  N N   . ASN A 1 431 ? -9.662  -12.749 -23.359 1.00 96.13  ? 104 ASN B N   1 
ATOM   752  C CA  . ASN A 1 431 ? -9.352  -11.312 -23.196 1.00 87.97  ? 104 ASN B CA  1 
ATOM   753  C C   . ASN A 1 431 ? -8.710  -11.136 -21.819 1.00 105.53 ? 104 ASN B C   1 
ATOM   754  O O   . ASN A 1 431 ? -7.569  -10.647 -21.758 1.00 124.64 ? 104 ASN B O   1 
ATOM   755  C CB  . ASN A 1 431 ? -10.596 -10.454 -23.417 1.00 91.43  ? 104 ASN B CB  1 
ATOM   756  C CG  . ASN A 1 431 ? -11.007 -10.400 -24.871 1.00 100.73 ? 104 ASN B CG  1 
ATOM   757  O OD1 . ASN A 1 431 ? -10.296 -10.902 -25.737 1.00 112.54 ? 104 ASN B OD1 1 
ATOM   758  N ND2 . ASN A 1 431 ? -12.147 -9.792  -25.149 1.00 112.70 ? 104 ASN B ND2 1 
ATOM   759  N N   . GLU A 1 432 ? -9.405  -11.549 -20.761 1.00 105.38 ? 105 GLU B N   1 
ATOM   760  C CA  . GLU A 1 432 ? -8.875  -11.326 -19.392 1.00 114.08 ? 105 GLU B CA  1 
ATOM   761  C C   . GLU A 1 432 ? -7.527  -12.023 -19.226 1.00 116.72 ? 105 GLU B C   1 
ATOM   762  O O   . GLU A 1 432 ? -6.603  -11.406 -18.674 1.00 124.20 ? 105 GLU B O   1 
ATOM   763  C CB  . GLU A 1 432 ? -9.873  -11.819 -18.346 1.00 113.42 ? 105 GLU B CB  1 
ATOM   764  C CG  . GLU A 1 432 ? -10.986 -10.828 -18.066 1.00 117.26 ? 105 GLU B CG  1 
ATOM   765  C CD  . GLU A 1 432 ? -10.581 -9.658  -17.186 1.00 150.29 ? 105 GLU B CD  1 
ATOM   766  O OE1 . GLU A 1 432 ? -11.413 -8.754  -16.988 1.00 165.23 ? 105 GLU B OE1 1 
ATOM   767  O OE2 . GLU A 1 432 ? -9.440  -9.663  -16.684 1.00 167.09 ? 105 GLU B OE2 1 
ATOM   768  N N   . ARG A 1 433 ? -7.424  -13.257 -19.702 1.00 100.33 ? 106 ARG B N   1 
ATOM   769  C CA  . ARG A 1 433 ? -6.197  -14.023 -19.519 1.00 113.63 ? 106 ARG B CA  1 
ATOM   770  C C   . ARG A 1 433 ? -4.999  -13.313 -20.139 1.00 113.29 ? 106 ARG B C   1 
ATOM   771  O O   . ARG A 1 433 ? -3.899  -13.331 -19.574 1.00 120.20 ? 106 ARG B O   1 
ATOM   772  C CB  . ARG A 1 433 ? -6.346  -15.423 -20.111 1.00 117.11 ? 106 ARG B CB  1 
ATOM   773  C CG  . ARG A 1 433 ? -7.352  -16.283 -19.365 1.00 123.71 ? 106 ARG B CG  1 
ATOM   774  C CD  . ARG A 1 433 ? -7.444  -17.685 -19.945 1.00 114.77 ? 106 ARG B CD  1 
ATOM   775  N NE  . ARG A 1 433 ? -8.447  -18.526 -19.305 1.00 141.40 ? 106 ARG B NE  1 
ATOM   776  C CZ  . ARG A 1 433 ? -8.774  -19.740 -19.724 1.00 158.45 ? 106 ARG B CZ  1 
ATOM   777  N NH1 . ARG A 1 433 ? -8.206  -20.277 -20.790 1.00 155.45 ? 106 ARG B NH1 1 
ATOM   778  N NH2 . ARG A 1 433 ? -9.706  -20.427 -19.068 1.00 162.10 ? 106 ARG B NH2 1 
ATOM   779  N N   . THR A 1 434 ? -5.195  -12.661 -21.287 1.00 107.32 ? 107 THR B N   1 
ATOM   780  C CA  . THR A 1 434 ? -4.114  -11.864 -21.855 1.00 100.73 ? 107 THR B CA  1 
ATOM   781  C C   . THR A 1 434 ? -3.821  -10.668 -20.953 1.00 112.88 ? 107 THR B C   1 
ATOM   782  O O   . THR A 1 434 ? -2.655  -10.319 -20.739 1.00 139.43 ? 107 THR B O   1 
ATOM   783  C CB  . THR A 1 434 ? -4.434  -11.402 -23.276 1.00 100.85 ? 107 THR B CB  1 
ATOM   784  O OG1 . THR A 1 434 ? -5.533  -10.484 -23.250 1.00 111.71 ? 107 THR B OG1 1 
ATOM   785  C CG2 . THR A 1 434 ? -4.773  -12.596 -24.167 1.00 106.52 ? 107 THR B CG2 1 
ATOM   786  N N   . LEU A 1 435 ? -4.862  -10.039 -20.398 1.00 106.07 ? 108 LEU B N   1 
ATOM   787  C CA  . LEU A 1 435 ? -4.647  -8.846  -19.580 1.00 99.41  ? 108 LEU B CA  1 
ATOM   788  C C   . LEU A 1 435 ? -3.900  -9.171  -18.291 1.00 105.28 ? 108 LEU B C   1 
ATOM   789  O O   . LEU A 1 435 ? -2.967  -8.452  -17.915 1.00 109.39 ? 108 LEU B O   1 
ATOM   790  C CB  . LEU A 1 435 ? -5.981  -8.166  -19.272 1.00 94.03  ? 108 LEU B CB  1 
ATOM   791  C CG  . LEU A 1 435 ? -6.742  -7.553  -20.449 1.00 88.10  ? 108 LEU B CG  1 
ATOM   792  C CD1 . LEU A 1 435 ? -7.918  -6.733  -19.948 1.00 120.93 ? 108 LEU B CD1 1 
ATOM   793  C CD2 . LEU A 1 435 ? -5.822  -6.702  -21.313 1.00 118.28 ? 108 LEU B CD2 1 
ATOM   794  N N   . ASP A 1 436 ? -4.291  -10.244 -17.597 1.00 101.23 ? 109 ASP B N   1 
ATOM   795  C CA  . ASP A 1 436 ? -3.598  -10.609 -16.365 1.00 104.91 ? 109 ASP B CA  1 
ATOM   796  C C   . ASP A 1 436 ? -2.227  -11.203 -16.642 1.00 119.90 ? 109 ASP B C   1 
ATOM   797  O O   . ASP A 1 436 ? -1.315  -11.057 -15.820 1.00 139.39 ? 109 ASP B O   1 
ATOM   798  C CB  . ASP A 1 436 ? -4.436  -11.589 -15.552 1.00 112.72 ? 109 ASP B CB  1 
ATOM   799  C CG  . ASP A 1 436 ? -5.626  -10.927 -14.912 1.00 147.13 ? 109 ASP B CG  1 
ATOM   800  O OD1 . ASP A 1 436 ? -5.642  -9.679  -14.860 1.00 131.99 ? 109 ASP B OD1 1 
ATOM   801  O OD2 . ASP A 1 436 ? -6.539  -11.646 -14.462 1.00 177.19 ? 109 ASP B OD2 1 
ATOM   802  N N   . TYR A 1 437 ? -2.072  -11.897 -17.773 1.00 115.90 ? 110 TYR B N   1 
ATOM   803  C CA  . TYR A 1 437 ? -0.746  -12.308 -18.223 1.00 131.76 ? 110 TYR B CA  1 
ATOM   804  C C   . TYR A 1 437 ? 0.177   -11.100 -18.334 1.00 135.32 ? 110 TYR B C   1 
ATOM   805  O O   . TYR A 1 437 ? 1.325   -11.134 -17.876 1.00 130.86 ? 110 TYR B O   1 
ATOM   806  C CB  . TYR A 1 437 ? -0.855  -13.045 -19.564 1.00 132.05 ? 110 TYR B CB  1 
ATOM   807  C CG  . TYR A 1 437 ? 0.467   -13.442 -20.202 1.00 106.99 ? 110 TYR B CG  1 
ATOM   808  C CD1 . TYR A 1 437 ? 1.427   -14.148 -19.489 1.00 139.18 ? 110 TYR B CD1 1 
ATOM   809  C CD2 . TYR A 1 437 ? 0.747   -13.118 -21.527 1.00 98.54  ? 110 TYR B CD2 1 
ATOM   810  C CE1 . TYR A 1 437 ? 2.636   -14.513 -20.074 1.00 146.83 ? 110 TYR B CE1 1 
ATOM   811  C CE2 . TYR A 1 437 ? 1.952   -13.479 -22.120 1.00 117.06 ? 110 TYR B CE2 1 
ATOM   812  C CZ  . TYR A 1 437 ? 2.892   -14.176 -21.388 1.00 132.77 ? 110 TYR B CZ  1 
ATOM   813  O OH  . TYR A 1 437 ? 4.090   -14.537 -21.969 1.00 135.19 ? 110 TYR B OH  1 
ATOM   814  N N   . HIS A 1 438 ? -0.327  -10.009 -18.920 1.00 133.79 ? 111 HIS B N   1 
ATOM   815  C CA  . HIS A 1 438 ? 0.461   -8.785  -19.038 1.00 132.44 ? 111 HIS B CA  1 
ATOM   816  C C   . HIS A 1 438 ? 0.859   -8.253  -17.665 1.00 129.02 ? 111 HIS B C   1 
ATOM   817  O O   . HIS A 1 438 ? 2.029   -7.933  -17.427 1.00 139.09 ? 111 HIS B O   1 
ATOM   818  C CB  . HIS A 1 438 ? -0.327  -7.725  -19.814 1.00 120.30 ? 111 HIS B CB  1 
ATOM   819  C CG  . HIS A 1 438 ? -0.607  -8.086  -21.243 1.00 120.75 ? 111 HIS B CG  1 
ATOM   820  N ND1 . HIS A 1 438 ? 0.251   -8.846  -22.010 1.00 136.00 ? 111 HIS B ND1 1 
ATOM   821  C CD2 . HIS A 1 438 ? -1.657  -7.784  -22.043 1.00 115.73 ? 111 HIS B CD2 1 
ATOM   822  C CE1 . HIS A 1 438 ? -0.258  -8.995  -23.221 1.00 113.70 ? 111 HIS B CE1 1 
ATOM   823  N NE2 . HIS A 1 438 ? -1.417  -8.362  -23.266 1.00 117.15 ? 111 HIS B NE2 1 
ATOM   824  N N   . ASP A 1 439 ? -0.106  -8.150  -16.746 1.00 104.75 ? 112 ASP B N   1 
ATOM   825  C CA  . ASP A 1 439 ? 0.202   -7.673  -15.401 1.00 99.88  ? 112 ASP B CA  1 
ATOM   826  C C   . ASP A 1 439 ? 1.220   -8.572  -14.715 1.00 105.55 ? 112 ASP B C   1 
ATOM   827  O O   . ASP A 1 439 ? 2.061   -8.095  -13.945 1.00 125.23 ? 112 ASP B O   1 
ATOM   828  C CB  . ASP A 1 439 ? -1.071  -7.587  -14.564 1.00 110.91 ? 112 ASP B CB  1 
ATOM   829  C CG  . ASP A 1 439 ? -2.080  -6.637  -15.150 1.00 136.73 ? 112 ASP B CG  1 
ATOM   830  O OD1 . ASP A 1 439 ? -1.853  -6.169  -16.285 1.00 141.97 ? 112 ASP B OD1 1 
ATOM   831  O OD2 . ASP A 1 439 ? -3.095  -6.356  -14.478 1.00 146.75 ? 112 ASP B OD2 1 
ATOM   832  N N   . SER A 1 440 ? 1.158   -9.878  -14.980 1.00 86.16  ? 113 SER B N   1 
ATOM   833  C CA  . SER A 1 440 ? 2.110   -10.792 -14.361 1.00 95.62  ? 113 SER B CA  1 
ATOM   834  C C   . SER A 1 440 ? 3.519   -10.568 -14.895 1.00 108.33 ? 113 SER B C   1 
ATOM   835  O O   . SER A 1 440 ? 4.487   -10.594 -14.127 1.00 130.74 ? 113 SER B O   1 
ATOM   836  C CB  . SER A 1 440 ? 1.673   -12.240 -14.581 1.00 112.58 ? 113 SER B CB  1 
ATOM   837  O OG  . SER A 1 440 ? 0.451   -12.509 -13.915 1.00 136.66 ? 113 SER B OG  1 
ATOM   838  N N   . ASN A 1 441 ? 3.656   -10.344 -16.205 1.00 100.48 ? 114 ASN B N   1 
ATOM   839  C CA  . ASN A 1 441 ? 4.976   -10.069 -16.770 1.00 102.64 ? 114 ASN B CA  1 
ATOM   840  C C   . ASN A 1 441 ? 5.571   -8.799  -16.181 1.00 108.23 ? 114 ASN B C   1 
ATOM   841  O O   . ASN A 1 441 ? 6.775   -8.737  -15.906 1.00 109.05 ? 114 ASN B O   1 
ATOM   842  C CB  . ASN A 1 441 ? 4.892   -9.955  -18.290 1.00 112.74 ? 114 ASN B CB  1 
ATOM   843  C CG  . ASN A 1 441 ? 4.336   -11.201 -18.935 1.00 130.65 ? 114 ASN B CG  1 
ATOM   844  O OD1 . ASN A 1 441 ? 3.387   -11.140 -19.715 1.00 146.16 ? 114 ASN B OD1 1 
ATOM   845  N ND2 . ASN A 1 441 ? 4.930   -12.345 -18.617 1.00 116.90 ? 114 ASN B ND2 1 
ATOM   846  N N   . VAL A 1 442 ? 4.741   -7.772  -15.993 1.00 102.34 ? 115 VAL B N   1 
ATOM   847  C CA  . VAL A 1 442 ? 5.179   -6.552  -15.317 1.00 97.27  ? 115 VAL B CA  1 
ATOM   848  C C   . VAL A 1 442 ? 5.803   -6.891  -13.970 1.00 108.82 ? 115 VAL B C   1 
ATOM   849  O O   . VAL A 1 442 ? 6.958   -6.552  -13.689 1.00 124.81 ? 115 VAL B O   1 
ATOM   850  C CB  . VAL A 1 442 ? 3.999   -5.582  -15.146 1.00 89.37  ? 115 VAL B CB  1 
ATOM   851  C CG1 . VAL A 1 442 ? 4.418   -4.383  -14.319 1.00 94.11  ? 115 VAL B CG1 1 
ATOM   852  C CG2 . VAL A 1 442 ? 3.468   -5.147  -16.503 1.00 95.46  ? 115 VAL B CG2 1 
ATOM   853  N N   . LYS A 1 443 ? 5.040   -7.585  -13.123 1.00 101.81 ? 116 LYS B N   1 
ATOM   854  C CA  . LYS A 1 443 ? 5.485   -7.856  -11.762 1.00 94.77  ? 116 LYS B CA  1 
ATOM   855  C C   . LYS A 1 443 ? 6.699   -8.773  -11.739 1.00 116.23 ? 116 LYS B C   1 
ATOM   856  O O   . LYS A 1 443 ? 7.542   -8.665  -10.840 1.00 131.64 ? 116 LYS B O   1 
ATOM   857  C CB  . LYS A 1 443 ? 4.329   -8.460  -10.966 1.00 84.87  ? 116 LYS B CB  1 
ATOM   858  C CG  . LYS A 1 443 ? 3.173   -7.489  -10.774 1.00 102.18 ? 116 LYS B CG  1 
ATOM   859  C CD  . LYS A 1 443 ? 2.016   -8.107  -10.006 1.00 139.46 ? 116 LYS B CD  1 
ATOM   860  C CE  . LYS A 1 443 ? 0.891   -7.095  -9.816  1.00 132.21 ? 116 LYS B CE  1 
ATOM   861  N NZ  . LYS A 1 443 ? -0.273  -7.663  -9.080  1.00 128.86 ? 116 LYS B NZ  1 
ATOM   862  N N   . ASN A 1 444 ? 6.810   -9.675  -12.718 1.00 103.90 ? 117 ASN B N   1 
ATOM   863  C CA  . ASN A 1 444 ? 7.977   -10.548 -12.786 1.00 116.45 ? 117 ASN B CA  1 
ATOM   864  C C   . ASN A 1 444 ? 9.244   -9.754  -13.071 1.00 125.83 ? 117 ASN B C   1 
ATOM   865  O O   . ASN A 1 444 ? 10.298  -10.028 -12.487 1.00 145.53 ? 117 ASN B O   1 
ATOM   866  C CB  . ASN A 1 444 ? 7.775   -11.623 -13.851 1.00 111.78 ? 117 ASN B CB  1 
ATOM   867  C CG  . ASN A 1 444 ? 6.613   -12.535 -13.538 1.00 127.44 ? 117 ASN B CG  1 
ATOM   868  O OD1 . ASN A 1 444 ? 6.352   -12.846 -12.375 1.00 111.60 ? 117 ASN B OD1 1 
ATOM   869  N ND2 . ASN A 1 444 ? 5.906   -12.973 -14.573 1.00 143.76 ? 117 ASN B ND2 1 
ATOM   870  N N   . LEU A 1 445 ? 9.161   -8.769  -13.967 1.00 125.07 ? 118 LEU B N   1 
ATOM   871  C CA  . LEU A 1 445 ? 10.327  -7.943  -14.262 1.00 135.78 ? 118 LEU B CA  1 
ATOM   872  C C   . LEU A 1 445 ? 10.715  -7.085  -13.067 1.00 136.40 ? 118 LEU B C   1 
ATOM   873  O O   . LEU A 1 445 ? 11.905  -6.874  -12.805 1.00 128.02 ? 118 LEU B O   1 
ATOM   874  C CB  . LEU A 1 445 ? 10.049  -7.063  -15.477 1.00 132.99 ? 118 LEU B CB  1 
ATOM   875  C CG  . LEU A 1 445 ? 9.844   -7.809  -16.790 1.00 152.30 ? 118 LEU B CG  1 
ATOM   876  C CD1 . LEU A 1 445 ? 9.448   -6.836  -17.876 1.00 162.41 ? 118 LEU B CD1 1 
ATOM   877  C CD2 . LEU A 1 445 ? 11.108  -8.560  -17.170 1.00 145.04 ? 118 LEU B CD2 1 
ATOM   878  N N   . TYR A 1 446 ? 9.723   -6.580  -12.334 1.00 119.39 ? 119 TYR B N   1 
ATOM   879  C CA  . TYR A 1 446 ? 10.014  -5.761  -11.165 1.00 117.20 ? 119 TYR B CA  1 
ATOM   880  C C   . TYR A 1 446 ? 10.696  -6.584  -10.080 1.00 125.90 ? 119 TYR B C   1 
ATOM   881  O O   . TYR A 1 446 ? 11.593  -6.091  -9.390  1.00 126.41 ? 119 TYR B O   1 
ATOM   882  C CB  . TYR A 1 446 ? 8.722   -5.116  -10.663 1.00 115.98 ? 119 TYR B CB  1 
ATOM   883  C CG  . TYR A 1 446 ? 8.832   -4.326  -9.379  1.00 138.76 ? 119 TYR B CG  1 
ATOM   884  C CD1 . TYR A 1 446 ? 9.494   -3.106  -9.347  1.00 143.16 ? 119 TYR B CD1 1 
ATOM   885  C CD2 . TYR A 1 446 ? 8.199   -4.757  -8.220  1.00 143.98 ? 119 TYR B CD2 1 
ATOM   886  C CE1 . TYR A 1 446 ? 9.575   -2.367  -8.182  1.00 156.22 ? 119 TYR B CE1 1 
ATOM   887  C CE2 . TYR A 1 446 ? 8.263   -4.018  -7.053  1.00 161.14 ? 119 TYR B CE2 1 
ATOM   888  C CZ  . TYR A 1 446 ? 8.958   -2.827  -7.039  1.00 172.75 ? 119 TYR B CZ  1 
ATOM   889  O OH  . TYR A 1 446 ? 9.031   -2.091  -5.878  1.00 180.29 ? 119 TYR B OH  1 
ATOM   890  N N   . GLU A 1 447 ? 10.308  -7.853  -9.937  1.00 136.70 ? 120 GLU B N   1 
ATOM   891  C CA  . GLU A 1 447 ? 10.997  -8.726  -8.992  1.00 138.79 ? 120 GLU B CA  1 
ATOM   892  C C   . GLU A 1 447 ? 12.407  -9.056  -9.471  1.00 146.74 ? 120 GLU B C   1 
ATOM   893  O O   . GLU A 1 447 ? 13.324  -9.209  -8.654  1.00 152.12 ? 120 GLU B O   1 
ATOM   894  C CB  . GLU A 1 447 ? 10.192  -10.006 -8.770  1.00 149.98 ? 120 GLU B CB  1 
ATOM   895  C CG  . GLU A 1 447 ? 8.885   -9.806  -8.030  1.00 164.97 ? 120 GLU B CG  1 
ATOM   896  C CD  . GLU A 1 447 ? 8.101   -11.097 -7.892  1.00 179.50 ? 120 GLU B CD  1 
ATOM   897  O OE1 . GLU A 1 447 ? 8.486   -12.094 -8.538  1.00 186.82 ? 120 GLU B OE1 1 
ATOM   898  O OE2 . GLU A 1 447 ? 7.109   -11.122 -7.132  1.00 178.11 ? 120 GLU B OE2 1 
ATOM   899  N N   . LYS A 1 448 ? 12.594  -9.186  -10.790 1.00 150.01 ? 121 LYS B N   1 
ATOM   900  C CA  . LYS A 1 448 ? 13.925  -9.425  -11.343 1.00 146.65 ? 121 LYS B CA  1 
ATOM   901  C C   . LYS A 1 448 ? 14.890  -8.318  -10.942 1.00 142.42 ? 121 LYS B C   1 
ATOM   902  O O   . LYS A 1 448 ? 16.011  -8.581  -10.491 1.00 144.53 ? 121 LYS B O   1 
ATOM   903  C CB  . LYS A 1 448 ? 13.853  -9.530  -12.868 1.00 123.58 ? 121 LYS B CB  1 
ATOM   904  C CG  . LYS A 1 448 ? 15.198  -9.818  -13.529 1.00 119.72 ? 121 LYS B CG  1 
ATOM   905  C CD  . LYS A 1 448 ? 15.066  -9.949  -15.041 1.00 130.41 ? 121 LYS B CD  1 
ATOM   906  C CE  . LYS A 1 448 ? 16.416  -10.203 -15.704 1.00 114.61 ? 121 LYS B CE  1 
ATOM   907  N NZ  . LYS A 1 448 ? 16.300  -10.332 -17.186 1.00 106.48 ? 121 LYS B NZ  1 
ATOM   908  N N   . VAL A 1 449 ? 14.466  -7.067  -11.106 1.00 141.03 ? 122 VAL B N   1 
ATOM   909  C CA  . VAL A 1 449 ? 15.340  -5.940  -10.811 1.00 134.72 ? 122 VAL B CA  1 
ATOM   910  C C   . VAL A 1 449 ? 15.529  -5.786  -9.306  1.00 136.96 ? 122 VAL B C   1 
ATOM   911  O O   . VAL A 1 449 ? 16.612  -5.417  -8.839  1.00 138.95 ? 122 VAL B O   1 
ATOM   912  C CB  . VAL A 1 449 ? 14.775  -4.668  -11.463 1.00 134.91 ? 122 VAL B CB  1 
ATOM   913  C CG1 . VAL A 1 449 ? 15.694  -3.494  -11.229 1.00 138.27 ? 122 VAL B CG1 1 
ATOM   914  C CG2 . VAL A 1 449 ? 14.584  -4.905  -12.945 1.00 144.55 ? 122 VAL B CG2 1 
ATOM   915  N N   . ARG A 1 450 ? 14.487  -6.076  -8.523  1.00 128.53 ? 123 ARG B N   1 
ATOM   916  C CA  . ARG A 1 450 ? 14.630  -6.083  -7.070  1.00 119.19 ? 123 ARG B CA  1 
ATOM   917  C C   . ARG A 1 450 ? 15.639  -7.129  -6.621  1.00 120.21 ? 123 ARG B C   1 
ATOM   918  O O   . ARG A 1 450 ? 16.485  -6.863  -5.760  1.00 134.56 ? 123 ARG B O   1 
ATOM   919  C CB  . ARG A 1 450 ? 13.281  -6.343  -6.407  1.00 123.26 ? 123 ARG B CB  1 
ATOM   920  C CG  . ARG A 1 450 ? 12.300  -5.217  -6.550  1.00 147.04 ? 123 ARG B CG  1 
ATOM   921  C CD  . ARG A 1 450 ? 10.951  -5.617  -6.002  1.00 180.37 ? 123 ARG B CD  1 
ATOM   922  N NE  . ARG A 1 450 ? 10.966  -5.924  -4.578  1.00 174.00 ? 123 ARG B NE  1 
ATOM   923  C CZ  . ARG A 1 450 ? 9.908   -6.358  -3.909  1.00 172.13 ? 123 ARG B CZ  1 
ATOM   924  N NH1 . ARG A 1 450 ? 8.741   -6.539  -4.506  1.00 178.67 ? 123 ARG B NH1 1 
ATOM   925  N NH2 . ARG A 1 450 ? 10.021  -6.616  -2.609  1.00 172.29 ? 123 ARG B NH2 1 
ATOM   926  N N   . SER A 1 451 ? 15.555  -8.334  -7.189  1.00 121.47 ? 124 SER B N   1 
ATOM   927  C CA  . SER A 1 451 ? 16.455  -9.409  -6.788  1.00 137.05 ? 124 SER B CA  1 
ATOM   928  C C   . SER A 1 451 ? 17.909  -9.053  -7.072  1.00 157.86 ? 124 SER B C   1 
ATOM   929  O O   . SER A 1 451 ? 18.795  -9.324  -6.253  1.00 171.29 ? 124 SER B O   1 
ATOM   930  C CB  . SER A 1 451 ? 16.073  -10.702 -7.506  1.00 133.92 ? 124 SER B CB  1 
ATOM   931  O OG  . SER A 1 451 ? 16.532  -10.682 -8.846  1.00 134.21 ? 124 SER B OG  1 
ATOM   932  N N   . GLN A 1 452 ? 18.175  -8.443  -8.226  1.00 151.92 ? 125 GLN B N   1 
ATOM   933  C CA  . GLN A 1 452 ? 19.545  -8.071  -8.558  1.00 137.83 ? 125 GLN B CA  1 
ATOM   934  C C   . GLN A 1 452 ? 20.031  -6.915  -7.693  1.00 142.56 ? 125 GLN B C   1 
ATOM   935  O O   . GLN A 1 452 ? 21.138  -6.962  -7.144  1.00 160.93 ? 125 GLN B O   1 
ATOM   936  C CB  . GLN A 1 452 ? 19.650  -7.714  -10.039 1.00 123.23 ? 125 GLN B CB  1 
ATOM   937  C CG  . GLN A 1 452 ? 19.509  -8.895  -10.973 1.00 129.10 ? 125 GLN B CG  1 
ATOM   938  C CD  . GLN A 1 452 ? 20.444  -8.791  -12.154 1.00 147.19 ? 125 GLN B CD  1 
ATOM   939  O OE1 . GLN A 1 452 ? 21.539  -9.353  -12.146 1.00 150.75 ? 125 GLN B OE1 1 
ATOM   940  N NE2 . GLN A 1 452 ? 20.023  -8.057  -13.176 1.00 145.89 ? 125 GLN B NE2 1 
ATOM   941  N N   . LEU A 1 453 ? 19.210  -5.870  -7.547  1.00 143.24 ? 126 LEU B N   1 
ATOM   942  C CA  . LEU A 1 453 ? 19.676  -4.663  -6.870  1.00 137.32 ? 126 LEU B CA  1 
ATOM   943  C C   . LEU A 1 453 ? 19.716  -4.827  -5.356  1.00 152.58 ? 126 LEU B C   1 
ATOM   944  O O   . LEU A 1 453 ? 20.628  -4.306  -4.705  1.00 174.71 ? 126 LEU B O   1 
ATOM   945  C CB  . LEU A 1 453 ? 18.802  -3.465  -7.238  1.00 125.67 ? 126 LEU B CB  1 
ATOM   946  C CG  . LEU A 1 453 ? 18.853  -3.055  -8.707  1.00 140.57 ? 126 LEU B CG  1 
ATOM   947  C CD1 . LEU A 1 453 ? 17.882  -1.912  -8.972  1.00 136.24 ? 126 LEU B CD1 1 
ATOM   948  C CD2 . LEU A 1 453 ? 20.274  -2.717  -9.136  1.00 132.90 ? 126 LEU B CD2 1 
ATOM   949  N N   . LYS A 1 454 ? 18.739  -5.529  -4.779  1.00 137.99 ? 127 LYS B N   1 
ATOM   950  C CA  . LYS A 1 454 ? 18.647  -5.753  -3.324  1.00 140.17 ? 127 LYS B CA  1 
ATOM   951  C C   . LYS A 1 454 ? 18.711  -4.396  -2.620  1.00 158.42 ? 127 LYS B C   1 
ATOM   952  O O   . LYS A 1 454 ? 18.037  -3.451  -3.055  1.00 143.86 ? 127 LYS B O   1 
ATOM   953  C CB  . LYS A 1 454 ? 19.707  -6.751  -2.876  1.00 143.16 ? 127 LYS B CB  1 
ATOM   954  C CG  . LYS A 1 454 ? 19.519  -8.175  -3.354  1.00 122.75 ? 127 LYS B CG  1 
ATOM   955  C CD  . LYS A 1 454 ? 20.648  -9.059  -2.843  1.00 129.59 ? 127 LYS B CD  1 
ATOM   956  C CE  . LYS A 1 454 ? 20.471  -10.506 -3.278  1.00 144.59 ? 127 LYS B CE  1 
ATOM   957  N NZ  . LYS A 1 454 ? 21.594  -11.355 -2.790  1.00 151.56 ? 127 LYS B NZ  1 
ATOM   958  N N   . ASN A 1 455 ? 19.498  -4.255  -1.550  1.00 164.82 ? 128 ASN B N   1 
ATOM   959  C CA  . ASN A 1 455 ? 19.603  -3.024  -0.784  1.00 172.37 ? 128 ASN B CA  1 
ATOM   960  C C   . ASN A 1 455 ? 20.600  -2.034  -1.367  1.00 174.15 ? 128 ASN B C   1 
ATOM   961  O O   . ASN A 1 455 ? 21.025  -1.119  -0.653  1.00 175.22 ? 128 ASN B O   1 
ATOM   962  C CB  . ASN A 1 455 ? 19.976  -3.337  0.665   1.00 169.34 ? 128 ASN B CB  1 
ATOM   963  C CG  . ASN A 1 455 ? 18.847  -3.992  1.422   1.00 193.03 ? 128 ASN B CG  1 
ATOM   964  O OD1 . ASN A 1 455 ? 17.681  -3.852  1.055   1.00 204.47 ? 128 ASN B OD1 1 
ATOM   965  N ND2 . ASN A 1 455 ? 19.182  -4.710  2.487   1.00 208.70 ? 128 ASN B ND2 1 
ATOM   966  N N   . ASN A 1 456 ? 20.997  -2.198  -2.627  1.00 187.20 ? 129 ASN B N   1 
ATOM   967  C CA  . ASN A 1 456 ? 21.819  -1.206  -3.310  1.00 174.08 ? 129 ASN B CA  1 
ATOM   968  C C   . ASN A 1 456 ? 20.995  -0.075  -3.916  1.00 173.25 ? 129 ASN B C   1 
ATOM   969  O O   . ASN A 1 456 ? 21.556  0.759   -4.635  1.00 175.21 ? 129 ASN B O   1 
ATOM   970  C CB  . ASN A 1 456 ? 22.661  -1.870  -4.405  1.00 175.15 ? 129 ASN B CB  1 
ATOM   971  C CG  . ASN A 1 456 ? 24.047  -2.265  -3.925  1.00 180.54 ? 129 ASN B CG  1 
ATOM   972  O OD1 . ASN A 1 456 ? 24.428  -1.989  -2.787  1.00 178.16 ? 129 ASN B OD1 1 
ATOM   973  N ND2 . ASN A 1 456 ? 24.806  -2.925  -4.794  1.00 185.81 ? 129 ASN B ND2 1 
ATOM   974  N N   . ALA A 1 457 ? 19.693  -0.024  -3.637  1.00 162.04 ? 130 ALA B N   1 
ATOM   975  C CA  . ALA A 1 457 ? 18.823  1.010   -4.182  1.00 155.11 ? 130 ALA B CA  1 
ATOM   976  C C   . ALA A 1 457 ? 17.591  1.134   -3.294  1.00 140.63 ? 130 ALA B C   1 
ATOM   977  O O   . ALA A 1 457 ? 17.323  0.279   -2.446  1.00 130.08 ? 130 ALA B O   1 
ATOM   978  C CB  . ALA A 1 457 ? 18.428  0.701   -5.630  1.00 155.77 ? 130 ALA B CB  1 
ATOM   979  N N   . LYS A 1 458 ? 16.842  2.219   -3.499  1.00 142.52 ? 131 LYS B N   1 
ATOM   980  C CA  . LYS A 1 458 ? 15.583  2.467   -2.805  1.00 140.64 ? 131 LYS B CA  1 
ATOM   981  C C   . LYS A 1 458 ? 14.414  2.245   -3.755  1.00 144.73 ? 131 LYS B C   1 
ATOM   982  O O   . LYS A 1 458 ? 14.428  2.740   -4.887  1.00 150.12 ? 131 LYS B O   1 
ATOM   983  C CB  . LYS A 1 458 ? 15.514  3.893   -2.246  1.00 122.69 ? 131 LYS B CB  1 
ATOM   984  C CG  . LYS A 1 458 ? 16.439  4.183   -1.079  1.00 115.50 ? 131 LYS B CG  1 
ATOM   985  C CD  . LYS A 1 458 ? 16.321  5.632   -0.622  1.00 107.44 ? 131 LYS B CD  1 
ATOM   986  C CE  . LYS A 1 458 ? 17.208  5.912   0.582   1.00 116.00 ? 131 LYS B CE  1 
ATOM   987  N NZ  . LYS A 1 458 ? 17.129  7.332   1.016   1.00 125.72 ? 131 LYS B NZ  1 
ATOM   988  N N   . GLU A 1 459 ? 13.405  1.513   -3.289  1.00 146.57 ? 132 GLU B N   1 
ATOM   989  C CA  . GLU A 1 459 ? 12.141  1.384   -4.006  1.00 145.87 ? 132 GLU B CA  1 
ATOM   990  C C   . GLU A 1 459 ? 11.330  2.651   -3.771  1.00 150.06 ? 132 GLU B C   1 
ATOM   991  O O   . GLU A 1 459 ? 10.828  2.873   -2.665  1.00 155.37 ? 132 GLU B O   1 
ATOM   992  C CB  . GLU A 1 459 ? 11.371  0.160   -3.523  1.00 129.19 ? 132 GLU B CB  1 
ATOM   993  C CG  . GLU A 1 459 ? 12.011  -1.176  -3.829  1.00 154.40 ? 132 GLU B CG  1 
ATOM   994  C CD  . GLU A 1 459 ? 11.220  -2.327  -3.242  1.00 183.08 ? 132 GLU B CD  1 
ATOM   995  O OE1 . GLU A 1 459 ? 10.289  -2.065  -2.450  1.00 179.53 ? 132 GLU B OE1 1 
ATOM   996  O OE2 . GLU A 1 459 ? 11.524  -3.491  -3.573  1.00 196.58 ? 132 GLU B OE2 1 
ATOM   997  N N   . ILE A 1 460 ? 11.196  3.488   -4.799  1.00 141.82 ? 133 ILE B N   1 
ATOM   998  C CA  . ILE A 1 460 ? 10.516  4.773   -4.670  1.00 139.43 ? 133 ILE B CA  1 
ATOM   999  C C   . ILE A 1 460 ? 9.678   5.025   -5.919  1.00 152.98 ? 133 ILE B C   1 
ATOM   1000 O O   . ILE A 1 460 ? 10.016  4.576   -7.017  1.00 172.11 ? 133 ILE B O   1 
ATOM   1001 C CB  . ILE A 1 460 ? 11.535  5.917   -4.406  1.00 145.24 ? 133 ILE B CB  1 
ATOM   1002 C CG1 . ILE A 1 460 ? 12.126  5.773   -2.996  1.00 161.75 ? 133 ILE B CG1 1 
ATOM   1003 C CG2 . ILE A 1 460 ? 10.916  7.297   -4.602  1.00 144.58 ? 133 ILE B CG2 1 
ATOM   1004 C CD1 . ILE A 1 460 ? 13.280  6.688   -2.701  1.00 164.11 ? 133 ILE B CD1 1 
ATOM   1005 N N   . GLY A 1 461 ? 8.552   5.719   -5.737  1.00 138.04 ? 134 GLY B N   1 
ATOM   1006 C CA  . GLY A 1 461 ? 7.677   6.021   -6.855  1.00 138.22 ? 134 GLY B CA  1 
ATOM   1007 C C   . GLY A 1 461 ? 6.823   4.824   -7.243  1.00 139.83 ? 134 GLY B C   1 
ATOM   1008 O O   . GLY A 1 461 ? 6.559   3.929   -6.439  1.00 133.16 ? 134 GLY B O   1 
ATOM   1009 N N   . ASN A 1 462 ? 6.381   4.819   -8.500  1.00 131.43 ? 135 ASN B N   1 
ATOM   1010 C CA  . ASN A 1 462 ? 5.631   3.697   -9.065  1.00 129.18 ? 135 ASN B CA  1 
ATOM   1011 C C   . ASN A 1 462 ? 6.610   2.849   -9.867  1.00 133.81 ? 135 ASN B C   1 
ATOM   1012 O O   . ASN A 1 462 ? 6.748   3.001   -11.081 1.00 105.90 ? 135 ASN B O   1 
ATOM   1013 C CB  . ASN A 1 462 ? 4.468   4.180   -9.923  1.00 122.03 ? 135 ASN B CB  1 
ATOM   1014 C CG  . ASN A 1 462 ? 3.341   4.762   -9.098  1.00 139.01 ? 135 ASN B CG  1 
ATOM   1015 O OD1 . ASN A 1 462 ? 3.196   4.451   -7.915  1.00 170.87 ? 135 ASN B OD1 1 
ATOM   1016 N ND2 . ASN A 1 462 ? 2.534   5.614   -9.719  1.00 128.00 ? 135 ASN B ND2 1 
ATOM   1017 N N   . GLY A 1 463 ? 7.295   1.945   -9.171  1.00 152.55 ? 136 GLY B N   1 
ATOM   1018 C CA  . GLY A 1 463 ? 8.274   1.084   -9.800  1.00 141.81 ? 136 GLY B CA  1 
ATOM   1019 C C   . GLY A 1 463 ? 9.497   1.829   -10.290 1.00 141.31 ? 136 GLY B C   1 
ATOM   1020 O O   . GLY A 1 463 ? 9.843   1.755   -11.472 1.00 139.56 ? 136 GLY B O   1 
ATOM   1021 N N   . CYS A 1 464 ? 10.155  2.562   -9.397  1.00 151.49 ? 137 CYS B N   1 
ATOM   1022 C CA  . CYS A 1 464 ? 11.404  3.235   -9.722  1.00 138.03 ? 137 CYS B CA  1 
ATOM   1023 C C   . CYS A 1 464 ? 12.449  2.853   -8.685  1.00 132.29 ? 137 CYS B C   1 
ATOM   1024 O O   . CYS A 1 464 ? 12.152  2.778   -7.489  1.00 143.61 ? 137 CYS B O   1 
ATOM   1025 C CB  . CYS A 1 464 ? 11.233  4.762   -9.775  1.00 129.99 ? 137 CYS B CB  1 
ATOM   1026 S SG  . CYS A 1 464 ? 10.317  5.384   -11.208 1.00 142.07 ? 137 CYS B SG  1 
ATOM   1027 N N   . PHE A 1 465 ? 13.665  2.592   -9.149  1.00 118.33 ? 138 PHE B N   1 
ATOM   1028 C CA  . PHE A 1 465 ? 14.779  2.206   -8.290  1.00 144.25 ? 138 PHE B CA  1 
ATOM   1029 C C   . PHE A 1 465 ? 15.776  3.357   -8.261  1.00 177.08 ? 138 PHE B C   1 
ATOM   1030 O O   . PHE A 1 465 ? 16.460  3.612   -9.258  1.00 166.07 ? 138 PHE B O   1 
ATOM   1031 C CB  . PHE A 1 465 ? 15.453  0.933   -8.797  1.00 137.32 ? 138 PHE B CB  1 
ATOM   1032 C CG  . PHE A 1 465 ? 14.563  -0.275  -8.800  1.00 133.39 ? 138 PHE B CG  1 
ATOM   1033 C CD1 . PHE A 1 465 ? 13.711  -0.518  -9.862  1.00 132.42 ? 138 PHE B CD1 1 
ATOM   1034 C CD2 . PHE A 1 465 ? 14.600  -1.183  -7.755  1.00 147.80 ? 138 PHE B CD2 1 
ATOM   1035 C CE1 . PHE A 1 465 ? 12.897  -1.631  -9.873  1.00 145.53 ? 138 PHE B CE1 1 
ATOM   1036 C CE2 . PHE A 1 465 ? 13.789  -2.301  -7.763  1.00 143.72 ? 138 PHE B CE2 1 
ATOM   1037 C CZ  . PHE A 1 465 ? 12.937  -2.525  -8.825  1.00 133.58 ? 138 PHE B CZ  1 
ATOM   1038 N N   . GLU A 1 466 ? 15.863  4.054   -7.128  1.00 182.51 ? 139 GLU B N   1 
ATOM   1039 C CA  . GLU A 1 466 ? 16.864  5.105   -6.961  1.00 174.35 ? 139 GLU B CA  1 
ATOM   1040 C C   . GLU A 1 466 ? 18.154  4.461   -6.474  1.00 180.51 ? 139 GLU B C   1 
ATOM   1041 O O   . GLU A 1 466 ? 18.228  3.977   -5.340  1.00 168.08 ? 139 GLU B O   1 
ATOM   1042 C CB  . GLU A 1 466 ? 16.413  6.192   -5.988  1.00 165.99 ? 139 GLU B CB  1 
ATOM   1043 C CG  . GLU A 1 466 ? 15.224  7.011   -6.447  1.00 171.28 ? 139 GLU B CG  1 
ATOM   1044 C CD  . GLU A 1 466 ? 14.840  8.086   -5.448  1.00 168.21 ? 139 GLU B CD  1 
ATOM   1045 O OE1 . GLU A 1 466 ? 15.414  8.105   -4.338  1.00 195.85 ? 139 GLU B OE1 1 
ATOM   1046 O OE2 . GLU A 1 466 ? 13.949  8.901   -5.767  1.00 152.99 ? 139 GLU B OE2 1 
ATOM   1047 N N   . PHE A 1 467 ? 19.167  4.461   -7.332  1.00 182.00 ? 140 PHE B N   1 
ATOM   1048 C CA  . PHE A 1 467 ? 20.451  3.873   -6.989  1.00 187.17 ? 140 PHE B CA  1 
ATOM   1049 C C   . PHE A 1 467 ? 21.181  4.757   -5.985  1.00 182.60 ? 140 PHE B C   1 
ATOM   1050 O O   . PHE A 1 467 ? 21.332  5.963   -6.203  1.00 185.74 ? 140 PHE B O   1 
ATOM   1051 C CB  . PHE A 1 467 ? 21.302  3.711   -8.249  1.00 195.34 ? 140 PHE B CB  1 
ATOM   1052 C CG  . PHE A 1 467 ? 20.727  2.766   -9.266  1.00 182.88 ? 140 PHE B CG  1 
ATOM   1053 C CD1 . PHE A 1 467 ? 20.971  1.406   -9.189  1.00 187.91 ? 140 PHE B CD1 1 
ATOM   1054 C CD2 . PHE A 1 467 ? 19.958  3.245   -10.315 1.00 163.53 ? 140 PHE B CD2 1 
ATOM   1055 C CE1 . PHE A 1 467 ? 20.449  0.542   -10.133 1.00 155.78 ? 140 PHE B CE1 1 
ATOM   1056 C CE2 . PHE A 1 467 ? 19.434  2.385   -11.259 1.00 154.37 ? 140 PHE B CE2 1 
ATOM   1057 C CZ  . PHE A 1 467 ? 19.679  1.031   -11.167 1.00 154.24 ? 140 PHE B CZ  1 
ATOM   1058 N N   . TYR A 1 468 ? 21.646  4.157   -4.884  1.00 171.08 ? 141 TYR B N   1 
ATOM   1059 C CA  . TYR A 1 468 ? 22.481  4.931   -3.931  1.00 172.69 ? 141 TYR B CA  1 
ATOM   1060 C C   . TYR A 1 468 ? 23.790  5.258   -4.646  1.00 174.21 ? 141 TYR B C   1 
ATOM   1061 O O   . TYR A 1 468 ? 24.287  6.393   -4.516  1.00 181.77 ? 141 TYR B O   1 
ATOM   1062 C CB  . TYR A 1 468 ? 22.824  4.107   -2.692  1.00 181.36 ? 141 TYR B CB  1 
ATOM   1063 C CG  . TYR A 1 468 ? 21.654  3.636   -1.868  1.00 167.46 ? 141 TYR B CG  1 
ATOM   1064 C CD1 . TYR A 1 468 ? 20.828  4.533   -1.215  1.00 143.35 ? 141 TYR B CD1 1 
ATOM   1065 C CD2 . TYR A 1 468 ? 21.381  2.286   -1.733  1.00 169.53 ? 141 TYR B CD2 1 
ATOM   1066 C CE1 . TYR A 1 468 ? 19.761  4.099   -0.448  1.00 136.55 ? 141 TYR B CE1 1 
ATOM   1067 C CE2 . TYR A 1 468 ? 20.312  1.836   -0.978  1.00 161.53 ? 141 TYR B CE2 1 
ATOM   1068 C CZ  . TYR A 1 468 ? 19.498  2.746   -0.331  1.00 155.08 ? 141 TYR B CZ  1 
ATOM   1069 O OH  . TYR A 1 468 ? 18.442  2.297   0.423   1.00 158.06 ? 141 TYR B OH  1 
ATOM   1070 N N   . HIS A 1 469 ? 24.324  4.279   -5.382  1.00 170.39 ? 142 HIS B N   1 
ATOM   1071 C CA  . HIS A 1 469 ? 25.586  4.477   -6.114  1.00 150.29 ? 142 HIS B CA  1 
ATOM   1072 C C   . HIS A 1 469 ? 25.240  4.890   -7.562  1.00 151.47 ? 142 HIS B C   1 
ATOM   1073 O O   . HIS A 1 469 ? 24.039  5.018   -7.889  1.00 163.94 ? 142 HIS B O   1 
ATOM   1074 C CB  . HIS A 1 469 ? 26.317  3.136   -6.308  1.00 146.18 ? 142 HIS B CB  1 
ATOM   1075 C CG  . HIS A 1 469 ? 25.517  2.132   -7.073  1.00 161.53 ? 142 HIS B CG  1 
ATOM   1076 N ND1 . HIS A 1 469 ? 25.869  1.709   -8.336  1.00 181.26 ? 142 HIS B ND1 1 
ATOM   1077 C CD2 . HIS A 1 469 ? 24.374  1.498   -6.777  1.00 174.09 ? 142 HIS B CD2 1 
ATOM   1078 C CE1 . HIS A 1 469 ? 24.973  0.835   -8.771  1.00 197.93 ? 142 HIS B CE1 1 
ATOM   1079 N NE2 . HIS A 1 469 ? 24.057  0.690   -7.838  1.00 206.38 ? 142 HIS B NE2 1 
ATOM   1080 N N   . LYS A 1 470 ? 26.263  5.093   -8.397  1.00 156.87 ? 143 LYS B N   1 
ATOM   1081 C CA  . LYS A 1 470 ? 26.022  5.472   -9.797  1.00 162.57 ? 143 LYS B CA  1 
ATOM   1082 C C   . LYS A 1 470 ? 26.100  4.296   -10.799 1.00 194.19 ? 143 LYS B C   1 
ATOM   1083 O O   . LYS A 1 470 ? 27.225  3.890   -11.148 1.00 189.28 ? 143 LYS B O   1 
ATOM   1084 C CB  . LYS A 1 470 ? 27.083  6.525   -10.154 1.00 158.38 ? 143 LYS B CB  1 
ATOM   1085 C CG  . LYS A 1 470 ? 27.206  7.660   -9.147  1.00 159.98 ? 143 LYS B CG  1 
ATOM   1086 C CD  . LYS A 1 470 ? 28.419  8.533   -9.377  1.00 151.54 ? 143 LYS B CD  1 
ATOM   1087 C CE  . LYS A 1 470 ? 28.566  9.628   -8.342  1.00 170.69 ? 143 LYS B CE  1 
ATOM   1088 N NZ  . LYS A 1 470 ? 29.738  10.491  -8.621  1.00 170.67 ? 143 LYS B NZ  1 
ATOM   1089 N N   . CYS A 1 471 ? 24.944  3.773   -11.221 1.00 209.24 ? 144 CYS B N   1 
ATOM   1090 C CA  . CYS A 1 471 ? 24.928  2.670   -12.222 1.00 203.37 ? 144 CYS B CA  1 
ATOM   1091 C C   . CYS A 1 471 ? 25.288  3.224   -13.603 1.00 183.15 ? 144 CYS B C   1 
ATOM   1092 O O   . CYS A 1 471 ? 24.470  3.971   -14.167 1.00 183.39 ? 144 CYS B O   1 
ATOM   1093 C CB  . CYS A 1 471 ? 23.540  2.038   -12.225 1.00 206.23 ? 144 CYS B CB  1 
ATOM   1094 S SG  . CYS A 1 471 ? 23.300  0.608   -13.312 1.00 259.94 ? 144 CYS B SG  1 
ATOM   1095 N N   . ASP A 1 472 ? 26.461  2.859   -14.125 1.00 181.05 ? 145 ASP B N   1 
ATOM   1096 C CA  . ASP A 1 472 ? 26.927  3.384   -15.435 1.00 164.36 ? 145 ASP B CA  1 
ATOM   1097 C C   . ASP A 1 472 ? 26.053  2.827   -16.558 1.00 167.29 ? 145 ASP B C   1 
ATOM   1098 O O   . ASP A 1 472 ? 25.294  1.877   -16.305 1.00 184.93 ? 145 ASP B O   1 
ATOM   1099 C CB  . ASP A 1 472 ? 28.387  3.017   -15.694 1.00 146.80 ? 145 ASP B CB  1 
ATOM   1100 C CG  . ASP A 1 472 ? 29.331  3.498   -14.607 1.00 167.49 ? 145 ASP B CG  1 
ATOM   1101 O OD1 . ASP A 1 472 ? 28.846  4.138   -13.654 1.00 182.97 ? 145 ASP B OD1 1 
ATOM   1102 O OD2 . ASP A 1 472 ? 30.542  3.226   -14.722 1.00 163.45 ? 145 ASP B OD2 1 
ATOM   1103 N N   . ASN A 1 473 ? 26.184  3.391   -17.758 1.00 146.01 ? 146 ASN B N   1 
ATOM   1104 C CA  . ASN A 1 473 ? 25.410  2.875   -18.914 1.00 147.86 ? 146 ASN B CA  1 
ATOM   1105 C C   . ASN A 1 473 ? 25.572  1.353   -18.956 1.00 167.51 ? 146 ASN B C   1 
ATOM   1106 O O   . ASN A 1 473 ? 24.543  0.658   -19.005 1.00 180.68 ? 146 ASN B O   1 
ATOM   1107 C CB  . ASN A 1 473 ? 25.839  3.541   -20.222 1.00 150.29 ? 146 ASN B CB  1 
ATOM   1108 C CG  . ASN A 1 473 ? 27.338  3.532   -20.432 1.00 155.17 ? 146 ASN B CG  1 
ATOM   1109 O OD1 . ASN A 1 473 ? 28.088  3.061   -19.579 1.00 122.30 ? 146 ASN B OD1 1 
ATOM   1110 N ND2 . ASN A 1 473 ? 27.784  4.056   -21.561 1.00 178.98 ? 146 ASN B ND2 1 
ATOM   1111 N N   . THR A 1 474 ? 26.812  0.860   -18.914 1.00 174.39 ? 147 THR B N   1 
ATOM   1112 C CA  . THR A 1 474 ? 27.043  -0.609  -18.875 1.00 172.87 ? 147 THR B CA  1 
ATOM   1113 C C   . THR A 1 474 ? 26.261  -1.184  -17.693 1.00 187.36 ? 147 THR B C   1 
ATOM   1114 O O   . THR A 1 474 ? 25.391  -2.034  -17.924 1.00 194.14 ? 147 THR B O   1 
ATOM   1115 C CB  . THR A 1 474 ? 28.539  -0.932  -18.806 1.00 170.31 ? 147 THR B CB  1 
ATOM   1116 O OG1 . THR A 1 474 ? 29.047  -0.382  -17.590 1.00 200.80 ? 147 THR B OG1 1 
ATOM   1117 C CG2 . THR A 1 474 ? 29.311  -0.378  -19.982 1.00 144.80 ? 147 THR B CG2 1 
ATOM   1118 N N   . CYS A 1 475 ? 26.577  -0.755  -16.473 1.00 176.03 ? 148 CYS B N   1 
ATOM   1119 C CA  . CYS A 1 475 ? 25.797  -1.195  -15.317 1.00 174.67 ? 148 CYS B CA  1 
ATOM   1120 C C   . CYS A 1 475 ? 24.297  -1.227  -15.538 1.00 178.23 ? 148 CYS B C   1 
ATOM   1121 O O   . CYS A 1 475 ? 23.614  -2.130  -15.038 1.00 178.50 ? 148 CYS B O   1 
ATOM   1122 C CB  . CYS A 1 475 ? 26.036  -0.218  -14.153 1.00 178.76 ? 148 CYS B CB  1 
ATOM   1123 S SG  . CYS A 1 475 ? 25.097  -0.601  -12.678 1.00 225.64 ? 148 CYS B SG  1 
ATOM   1124 N N   . MET A 1 476 ? 23.745  -0.264  -16.281 1.00 176.02 ? 149 MET B N   1 
ATOM   1125 C CA  . MET A 1 476 ? 22.320  -0.291  -16.601 1.00 160.47 ? 149 MET B CA  1 
ATOM   1126 C C   . MET A 1 476 ? 22.007  -1.444  -17.524 1.00 155.41 ? 149 MET B C   1 
ATOM   1127 O O   . MET A 1 476 ? 20.975  -2.107  -17.372 1.00 156.82 ? 149 MET B O   1 
ATOM   1128 C CB  . MET A 1 476 ? 21.899  1.043   -17.241 1.00 176.34 ? 149 MET B CB  1 
ATOM   1129 C CG  . MET A 1 476 ? 22.071  2.287   -16.365 1.00 190.11 ? 149 MET B CG  1 
ATOM   1130 S SD  . MET A 1 476 ? 21.196  2.354   -14.784 1.00 212.78 ? 149 MET B SD  1 
ATOM   1131 C CE  . MET A 1 476 ? 19.486  2.488   -15.282 1.00 144.21 ? 149 MET B CE  1 
ATOM   1132 N N   . GLU A 1 477 ? 22.889  -1.705  -18.491 1.00 155.32 ? 150 GLU B N   1 
ATOM   1133 C CA  . GLU A 1 477 ? 22.760  -2.891  -19.329 1.00 138.60 ? 150 GLU B CA  1 
ATOM   1134 C C   . GLU A 1 477 ? 22.840  -4.163  -18.497 1.00 147.79 ? 150 GLU B C   1 
ATOM   1135 O O   . GLU A 1 477 ? 22.047  -5.092  -18.692 1.00 161.73 ? 150 GLU B O   1 
ATOM   1136 C CB  . GLU A 1 477 ? 23.852  -2.887  -20.396 1.00 140.48 ? 150 GLU B CB  1 
ATOM   1137 C CG  . GLU A 1 477 ? 23.865  -1.637  -21.256 1.00 169.39 ? 150 GLU B CG  1 
ATOM   1138 C CD  . GLU A 1 477 ? 25.269  -1.197  -21.601 1.00 171.10 ? 150 GLU B CD  1 
ATOM   1139 O OE1 . GLU A 1 477 ? 26.164  -2.065  -21.680 1.00 155.36 ? 150 GLU B OE1 1 
ATOM   1140 O OE2 . GLU A 1 477 ? 25.476  0.019   -21.790 1.00 144.57 ? 150 GLU B OE2 1 
ATOM   1141 N N   . SER A 1 478 ? 23.781  -4.216  -17.549 1.00 144.22 ? 151 SER B N   1 
ATOM   1142 C CA  . SER A 1 478 ? 23.965  -5.419  -16.741 1.00 156.35 ? 151 SER B CA  1 
ATOM   1143 C C   . SER A 1 478 ? 22.709  -5.760  -15.950 1.00 157.83 ? 151 SER B C   1 
ATOM   1144 O O   . SER A 1 478 ? 22.347  -6.936  -15.825 1.00 165.80 ? 151 SER B O   1 
ATOM   1145 C CB  . SER A 1 478 ? 25.156  -5.246  -15.798 1.00 165.22 ? 151 SER B CB  1 
ATOM   1146 O OG  . SER A 1 478 ? 24.915  -4.225  -14.845 1.00 168.69 ? 151 SER B OG  1 
ATOM   1147 N N   . VAL A 1 479 ? 22.037  -4.747  -15.396 1.00 143.16 ? 152 VAL B N   1 
ATOM   1148 C CA  . VAL A 1 479 ? 20.759  -4.986  -14.728 1.00 133.19 ? 152 VAL B CA  1 
ATOM   1149 C C   . VAL A 1 479 ? 19.738  -5.515  -15.728 1.00 120.84 ? 152 VAL B C   1 
ATOM   1150 O O   . VAL A 1 479 ? 19.002  -6.470  -15.450 1.00 99.15  ? 152 VAL B O   1 
ATOM   1151 C CB  . VAL A 1 479 ? 20.262  -3.702  -14.036 1.00 114.84 ? 152 VAL B CB  1 
ATOM   1152 C CG1 . VAL A 1 479 ? 19.028  -3.990  -13.187 1.00 91.33  ? 152 VAL B CG1 1 
ATOM   1153 C CG2 . VAL A 1 479 ? 21.363  -3.098  -13.182 1.00 146.33 ? 152 VAL B CG2 1 
ATOM   1154 N N   . LYS A 1 480 ? 19.695  -4.911  -16.917 1.00 129.10 ? 153 LYS B N   1 
ATOM   1155 C CA  . LYS A 1 480 ? 18.762  -5.355  -17.947 1.00 133.67 ? 153 LYS B CA  1 
ATOM   1156 C C   . LYS A 1 480 ? 19.096  -6.764  -18.423 1.00 148.69 ? 153 LYS B C   1 
ATOM   1157 O O   . LYS A 1 480 ? 18.225  -7.640  -18.463 1.00 153.43 ? 153 LYS B O   1 
ATOM   1158 C CB  . LYS A 1 480 ? 18.771  -4.377  -19.121 1.00 139.18 ? 153 LYS B CB  1 
ATOM   1159 C CG  . LYS A 1 480 ? 17.777  -4.734  -20.207 1.00 148.36 ? 153 LYS B CG  1 
ATOM   1160 C CD  . LYS A 1 480 ? 17.791  -3.718  -21.331 1.00 162.66 ? 153 LYS B CD  1 
ATOM   1161 C CE  . LYS A 1 480 ? 16.813  -4.107  -22.425 1.00 149.20 ? 153 LYS B CE  1 
ATOM   1162 N NZ  . LYS A 1 480 ? 16.811  -3.125  -23.544 1.00 179.57 ? 153 LYS B NZ  1 
ATOM   1163 N N   . ASN A 1 481 ? 20.359  -7.002  -18.788 1.00 148.62 ? 154 ASN B N   1 
ATOM   1164 C CA  . ASN A 1 481 ? 20.782  -8.325  -19.239 1.00 141.55 ? 154 ASN B CA  1 
ATOM   1165 C C   . ASN A 1 481 ? 20.782  -9.367  -18.127 1.00 136.95 ? 154 ASN B C   1 
ATOM   1166 O O   . ASN A 1 481 ? 21.153  -10.517 -18.388 1.00 154.55 ? 154 ASN B O   1 
ATOM   1167 C CB  . ASN A 1 481 ? 22.182  -8.261  -19.863 1.00 137.47 ? 154 ASN B CB  1 
ATOM   1168 C CG  . ASN A 1 481 ? 22.332  -7.125  -20.855 1.00 158.04 ? 154 ASN B CG  1 
ATOM   1169 O OD1 . ASN A 1 481 ? 23.314  -6.381  -20.821 1.00 170.44 ? 154 ASN B OD1 1 
ATOM   1170 N ND2 . ASN A 1 481 ? 21.354  -6.978  -21.739 1.00 168.03 ? 154 ASN B ND2 1 
ATOM   1171 N N   . GLY A 1 482 ? 20.381  -9.008  -16.909 1.00 140.54 ? 155 GLY B N   1 
ATOM   1172 C CA  . GLY A 1 482 ? 20.452  -9.932  -15.796 1.00 140.20 ? 155 GLY B CA  1 
ATOM   1173 C C   . GLY A 1 482 ? 21.846  -10.201 -15.284 1.00 143.62 ? 155 GLY B C   1 
ATOM   1174 O O   . GLY A 1 482 ? 22.020  -11.081 -14.436 1.00 156.41 ? 155 GLY B O   1 
ATOM   1175 N N   . THR A 1 483 ? 22.848  -9.466  -15.769 1.00 141.93 ? 156 THR B N   1 
ATOM   1176 C CA  . THR A 1 483 ? 24.239  -9.680  -15.396 1.00 156.96 ? 156 THR B CA  1 
ATOM   1177 C C   . THR A 1 483 ? 24.730  -8.676  -14.356 1.00 155.82 ? 156 THR B C   1 
ATOM   1178 O O   . THR A 1 483 ? 25.943  -8.526  -14.175 1.00 159.83 ? 156 THR B O   1 
ATOM   1179 C CB  . THR A 1 483 ? 25.129  -9.634  -16.642 1.00 162.02 ? 156 THR B CB  1 
ATOM   1180 O OG1 . THR A 1 483 ? 24.992  -8.363  -17.289 1.00 154.67 ? 156 THR B OG1 1 
ATOM   1181 C CG2 . THR A 1 483 ? 24.731  -10.728 -17.623 1.00 136.77 ? 156 THR B CG2 1 
ATOM   1182 N N   . TYR A 1 484 ? 23.819  -7.992  -13.665 1.00 149.97 ? 157 TYR B N   1 
ATOM   1183 C CA  . TYR A 1 484 ? 24.226  -7.034  -12.644 1.00 155.32 ? 157 TYR B CA  1 
ATOM   1184 C C   . TYR A 1 484 ? 24.877  -7.748  -11.465 1.00 168.15 ? 157 TYR B C   1 
ATOM   1185 O O   . TYR A 1 484 ? 24.478  -8.855  -11.090 1.00 161.39 ? 157 TYR B O   1 
ATOM   1186 C CB  . TYR A 1 484 ? 23.027  -6.217  -12.162 1.00 150.09 ? 157 TYR B CB  1 
ATOM   1187 C CG  . TYR A 1 484 ? 23.324  -5.388  -10.932 1.00 161.28 ? 157 TYR B CG  1 
ATOM   1188 C CD1 . TYR A 1 484 ? 24.107  -4.243  -11.013 1.00 145.40 ? 157 TYR B CD1 1 
ATOM   1189 C CD2 . TYR A 1 484 ? 22.834  -5.759  -9.687  1.00 177.38 ? 157 TYR B CD2 1 
ATOM   1190 C CE1 . TYR A 1 484 ? 24.386  -3.488  -9.889  1.00 158.92 ? 157 TYR B CE1 1 
ATOM   1191 C CE2 . TYR A 1 484 ? 23.108  -5.011  -8.560  1.00 174.86 ? 157 TYR B CE2 1 
ATOM   1192 C CZ  . TYR A 1 484 ? 23.883  -3.878  -8.665  1.00 168.22 ? 157 TYR B CZ  1 
ATOM   1193 O OH  . TYR A 1 484 ? 24.154  -3.136  -7.539  1.00 168.54 ? 157 TYR B OH  1 
ATOM   1194 N N   . ASP A 1 485 ? 25.884  -7.105  -10.876 1.00 167.63 ? 158 ASP B N   1 
ATOM   1195 C CA  . ASP A 1 485 ? 26.640  -7.667  -9.763  1.00 177.50 ? 158 ASP B CA  1 
ATOM   1196 C C   . ASP A 1 485 ? 26.546  -6.722  -8.572  1.00 178.37 ? 158 ASP B C   1 
ATOM   1197 O O   . ASP A 1 485 ? 27.002  -5.576  -8.645  1.00 181.73 ? 158 ASP B O   1 
ATOM   1198 C CB  . ASP A 1 485 ? 28.100  -7.908  -10.159 1.00 187.94 ? 158 ASP B CB  1 
ATOM   1199 C CG  . ASP A 1 485 ? 28.960  -8.351  -8.988  1.00 184.48 ? 158 ASP B CG  1 
ATOM   1200 O OD1 . ASP A 1 485 ? 28.888  -9.542  -8.619  1.00 191.58 ? 158 ASP B OD1 1 
ATOM   1201 O OD2 . ASP A 1 485 ? 29.717  -7.517  -8.446  1.00 172.86 ? 158 ASP B OD2 1 
ATOM   1202 N N   . TYR A 1 486 ? 25.951  -7.210  -7.482  1.00 173.04 ? 159 TYR B N   1 
ATOM   1203 C CA  . TYR A 1 486 ? 25.785  -6.401  -6.274  1.00 173.91 ? 159 TYR B CA  1 
ATOM   1204 C C   . TYR A 1 486 ? 27.106  -5.989  -5.630  1.00 178.37 ? 159 TYR B C   1 
ATOM   1205 O O   . TYR A 1 486 ? 27.245  -4.805  -5.274  1.00 185.15 ? 159 TYR B O   1 
ATOM   1206 C CB  . TYR A 1 486 ? 24.896  -7.166  -5.283  1.00 173.68 ? 159 TYR B CB  1 
ATOM   1207 C CG  . TYR A 1 486 ? 24.488  -6.396  -4.040  1.00 177.20 ? 159 TYR B CG  1 
ATOM   1208 C CD1 . TYR A 1 486 ? 25.331  -6.311  -2.938  1.00 172.44 ? 159 TYR B CD1 1 
ATOM   1209 C CD2 . TYR A 1 486 ? 23.246  -5.782  -3.957  1.00 185.20 ? 159 TYR B CD2 1 
ATOM   1210 C CE1 . TYR A 1 486 ? 24.956  -5.617  -1.799  1.00 178.27 ? 159 TYR B CE1 1 
ATOM   1211 C CE2 . TYR A 1 486 ? 22.862  -5.090  -2.821  1.00 178.81 ? 159 TYR B CE2 1 
ATOM   1212 C CZ  . TYR A 1 486 ? 23.720  -5.008  -1.748  1.00 176.07 ? 159 TYR B CZ  1 
ATOM   1213 O OH  . TYR A 1 486 ? 23.339  -4.316  -0.620  1.00 199.97 ? 159 TYR B OH  1 
ATOM   1214 N N   . PRO A 1 487 ? 28.094  -6.879  -5.436  1.00 171.34 ? 160 PRO B N   1 
ATOM   1215 C CA  . PRO A 1 487 ? 29.255  -6.507  -4.602  1.00 175.68 ? 160 PRO B CA  1 
ATOM   1216 C C   . PRO A 1 487 ? 30.036  -5.284  -5.065  1.00 173.16 ? 160 PRO B C   1 
ATOM   1217 O O   . PRO A 1 487 ? 30.425  -4.471  -4.217  1.00 158.21 ? 160 PRO B O   1 
ATOM   1218 C CB  . PRO A 1 487 ? 30.116  -7.775  -4.654  1.00 184.45 ? 160 PRO B CB  1 
ATOM   1219 C CG  . PRO A 1 487 ? 29.112  -8.861  -4.743  1.00 164.91 ? 160 PRO B CG  1 
ATOM   1220 C CD  . PRO A 1 487 ? 28.100  -8.328  -5.719  1.00 150.68 ? 160 PRO B CD  1 
ATOM   1221 N N   . LYS A 1 488 ? 30.296  -5.134  -6.369  1.00 169.04 ? 161 LYS B N   1 
ATOM   1222 C CA  . LYS A 1 488 ? 31.161  -4.049  -6.835  1.00 149.86 ? 161 LYS B CA  1 
ATOM   1223 C C   . LYS A 1 488 ? 30.681  -2.693  -6.337  1.00 159.94 ? 161 LYS B C   1 
ATOM   1224 O O   . LYS A 1 488 ? 31.470  -1.885  -5.833  1.00 163.70 ? 161 LYS B O   1 
ATOM   1225 C CB  . LYS A 1 488 ? 31.247  -4.045  -8.362  1.00 132.72 ? 161 LYS B CB  1 
ATOM   1226 C CG  . LYS A 1 488 ? 31.986  -5.222  -8.966  1.00 133.47 ? 161 LYS B CG  1 
ATOM   1227 C CD  . LYS A 1 488 ? 32.013  -5.107  -10.483 1.00 143.48 ? 161 LYS B CD  1 
ATOM   1228 C CE  . LYS A 1 488 ? 32.781  -6.251  -11.126 1.00 134.05 ? 161 LYS B CE  1 
ATOM   1229 N NZ  . LYS A 1 488 ? 32.790  -6.141  -12.613 1.00 115.44 ? 161 LYS B NZ  1 
ATOM   1230 N N   . TYR A 1 489 ? 29.388  -2.427  -6.468  1.00 166.05 ? 162 TYR B N   1 
ATOM   1231 C CA  . TYR A 1 489 ? 28.808  -1.160  -6.051  1.00 174.29 ? 162 TYR B CA  1 
ATOM   1232 C C   . TYR A 1 489 ? 28.253  -1.200  -4.634  1.00 163.79 ? 162 TYR B C   1 
ATOM   1233 O O   . TYR A 1 489 ? 27.670  -0.206  -4.185  1.00 150.05 ? 162 TYR B O   1 
ATOM   1234 C CB  . TYR A 1 489 ? 27.701  -0.756  -7.024  1.00 172.96 ? 162 TYR B CB  1 
ATOM   1235 C CG  . TYR A 1 489 ? 28.093  -0.847  -8.482  1.00 166.05 ? 162 TYR B CG  1 
ATOM   1236 C CD1 . TYR A 1 489 ? 29.027  0.025   -9.025  1.00 169.03 ? 162 TYR B CD1 1 
ATOM   1237 C CD2 . TYR A 1 489 ? 27.532  -1.807  -9.313  1.00 166.22 ? 162 TYR B CD2 1 
ATOM   1238 C CE1 . TYR A 1 489 ? 29.384  -0.050  -10.357 1.00 176.08 ? 162 TYR B CE1 1 
ATOM   1239 C CE2 . TYR A 1 489 ? 27.885  -1.891  -10.647 1.00 173.81 ? 162 TYR B CE2 1 
ATOM   1240 C CZ  . TYR A 1 489 ? 28.811  -1.010  -11.163 1.00 171.23 ? 162 TYR B CZ  1 
ATOM   1241 O OH  . TYR A 1 489 ? 29.164  -1.091  -12.491 1.00 159.02 ? 162 TYR B OH  1 
ATOM   1242 N N   . SER A 1 490 ? 28.427  -2.315  -3.924  1.00 163.22 ? 163 SER B N   1 
ATOM   1243 C CA  . SER A 1 490 ? 27.777  -2.492  -2.630  1.00 173.18 ? 163 SER B CA  1 
ATOM   1244 C C   . SER A 1 490 ? 28.279  -1.474  -1.613  1.00 171.66 ? 163 SER B C   1 
ATOM   1245 O O   . SER A 1 490 ? 27.493  -0.722  -1.028  1.00 159.23 ? 163 SER B O   1 
ATOM   1246 C CB  . SER A 1 490 ? 28.004  -3.918  -2.125  1.00 168.78 ? 163 SER B CB  1 
ATOM   1247 O OG  . SER A 1 490 ? 29.376  -4.152  -1.861  1.00 172.19 ? 163 SER B OG  1 
ATOM   1248 N N   . GLU A 1 491 ? 29.597  -1.437  -1.395  1.00 184.05 ? 164 GLU B N   1 
ATOM   1249 C CA  . GLU A 1 491 ? 30.157  -0.620  -0.323  1.00 182.03 ? 164 GLU B CA  1 
ATOM   1250 C C   . GLU A 1 491 ? 29.873  0.860   -0.546  1.00 176.25 ? 164 GLU B C   1 
ATOM   1251 O O   . GLU A 1 491 ? 29.538  1.585   0.399   1.00 191.34 ? 164 GLU B O   1 
ATOM   1252 C CB  . GLU A 1 491 ? 31.662  -0.862  -0.220  1.00 183.96 ? 164 GLU B CB  1 
ATOM   1253 C CG  . GLU A 1 491 ? 32.374  -0.818  -1.564  1.00 183.21 ? 164 GLU B CG  1 
ATOM   1254 C CD  . GLU A 1 491 ? 32.557  -2.186  -2.180  1.00 192.49 ? 164 GLU B CD  1 
ATOM   1255 O OE1 . GLU A 1 491 ? 31.790  -3.106  -1.825  1.00 214.96 ? 164 GLU B OE1 1 
ATOM   1256 O OE2 . GLU A 1 491 ? 33.468  -2.340  -3.020  1.00 179.01 ? 164 GLU B OE2 1 
ATOM   1257 N N   . GLU A 1 492 ? 30.011  1.327   -1.789  1.00 172.29 ? 165 GLU B N   1 
ATOM   1258 C CA  . GLU A 1 492 ? 29.697  2.715   -2.103  1.00 166.72 ? 165 GLU B CA  1 
ATOM   1259 C C   . GLU A 1 492 ? 28.260  3.038   -1.733  1.00 176.18 ? 165 GLU B C   1 
ATOM   1260 O O   . GLU A 1 492 ? 27.985  4.037   -1.060  1.00 181.94 ? 165 GLU B O   1 
ATOM   1261 C CB  . GLU A 1 492 ? 29.933  2.976   -3.588  1.00 155.53 ? 165 GLU B CB  1 
ATOM   1262 C CG  . GLU A 1 492 ? 31.375  2.856   -4.018  1.00 166.64 ? 165 GLU B CG  1 
ATOM   1263 C CD  . GLU A 1 492 ? 31.529  3.016   -5.511  1.00 177.25 ? 165 GLU B CD  1 
ATOM   1264 O OE1 . GLU A 1 492 ? 30.495  3.032   -6.211  1.00 172.76 ? 165 GLU B OE1 1 
ATOM   1265 O OE2 . GLU A 1 492 ? 32.678  3.128   -5.985  1.00 201.49 ? 165 GLU B OE2 1 
ATOM   1266 N N   . ALA A 1 493 ? 27.328  2.182   -2.159  1.00 176.14 ? 166 ALA B N   1 
ATOM   1267 C CA  . ALA A 1 493 ? 25.920  2.380   -1.841  1.00 184.96 ? 166 ALA B CA  1 
ATOM   1268 C C   . ALA A 1 493 ? 25.682  2.387   -0.336  1.00 184.49 ? 166 ALA B C   1 
ATOM   1269 O O   . ALA A 1 493 ? 24.963  3.249   0.181   1.00 193.74 ? 166 ALA B O   1 
ATOM   1270 C CB  . ALA A 1 493 ? 25.083  1.292   -2.515  1.00 184.01 ? 166 ALA B CB  1 
ATOM   1271 N N   . LYS A 1 494 ? 26.295  1.442   0.384   1.00 184.05 ? 167 LYS B N   1 
ATOM   1272 C CA  . LYS A 1 494 ? 26.093  1.335   1.828   1.00 189.76 ? 167 LYS B CA  1 
ATOM   1273 C C   . LYS A 1 494 ? 26.462  2.626   2.548   1.00 182.92 ? 167 LYS B C   1 
ATOM   1274 O O   . LYS A 1 494 ? 25.727  3.087   3.430   1.00 195.02 ? 167 LYS B O   1 
ATOM   1275 C CB  . LYS A 1 494 ? 26.912  0.168   2.377   1.00 192.19 ? 167 LYS B CB  1 
ATOM   1276 C CG  . LYS A 1 494 ? 26.451  -1.198  1.899   1.00 180.85 ? 167 LYS B CG  1 
ATOM   1277 C CD  . LYS A 1 494 ? 27.349  -2.290  2.448   1.00 176.73 ? 167 LYS B CD  1 
ATOM   1278 C CE  . LYS A 1 494 ? 26.898  -3.663  1.987   1.00 168.07 ? 167 LYS B CE  1 
ATOM   1279 N NZ  . LYS A 1 494 ? 27.804  -4.725  2.501   1.00 178.04 ? 167 LYS B NZ  1 
ATOM   1280 N N   . LEU A 1 495 ? 27.599  3.224   2.187   1.00 170.99 ? 168 LEU B N   1 
ATOM   1281 C CA  . LEU A 1 495 ? 28.023  4.459   2.839   1.00 161.66 ? 168 LEU B CA  1 
ATOM   1282 C C   . LEU A 1 495 ? 27.053  5.598   2.548   1.00 178.76 ? 168 LEU B C   1 
ATOM   1283 O O   . LEU A 1 495 ? 26.803  6.443   3.415   1.00 184.43 ? 168 LEU B O   1 
ATOM   1284 C CB  . LEU A 1 495 ? 29.439  4.822   2.393   1.00 144.28 ? 168 LEU B CB  1 
ATOM   1285 C CG  . LEU A 1 495 ? 30.527  3.835   2.825   1.00 155.79 ? 168 LEU B CG  1 
ATOM   1286 C CD1 . LEU A 1 495 ? 31.868  4.205   2.217   1.00 154.72 ? 168 LEU B CD1 1 
ATOM   1287 C CD2 . LEU A 1 495 ? 30.626  3.760   4.344   1.00 170.58 ? 168 LEU B CD2 1 
ATOM   1288 N N   . ASN A 1 496 ? 26.491  5.633   1.335   1.00 182.43 ? 169 ASN B N   1 
ATOM   1289 C CA  . ASN A 1 496 ? 25.521  6.671   0.992   1.00 182.50 ? 169 ASN B CA  1 
ATOM   1290 C C   . ASN A 1 496 ? 24.266  6.563   1.853   1.00 187.80 ? 169 ASN B C   1 
ATOM   1291 O O   . ASN A 1 496 ? 23.762  7.572   2.359   1.00 182.53 ? 169 ASN B O   1 
ATOM   1292 C CB  . ASN A 1 496 ? 25.161  6.598   -0.495  1.00 164.21 ? 169 ASN B CB  1 
ATOM   1293 C CG  . ASN A 1 496 ? 26.381  6.515   -1.397  1.00 176.24 ? 169 ASN B CG  1 
ATOM   1294 O OD1 . ASN A 1 496 ? 27.465  6.979   -1.043  1.00 184.76 ? 169 ASN B OD1 1 
ATOM   1295 N ND2 . ASN A 1 496 ? 26.205  5.926   -2.576  1.00 179.79 ? 169 ASN B ND2 1 
ATOM   1296 N N   . ARG A 1 497 ? 23.736  5.345   2.016   1.00 186.23 ? 170 ARG B N   1 
ATOM   1297 C CA  . ARG A 1 497 ? 22.609  5.142   2.923   1.00 190.88 ? 170 ARG B CA  1 
ATOM   1298 C C   . ARG A 1 497 ? 22.926  5.690   4.307   1.00 185.68 ? 170 ARG B C   1 
ATOM   1299 O O   . ARG A 1 497 ? 22.157  6.477   4.870   1.00 189.35 ? 170 ARG B O   1 
ATOM   1300 C CB  . ARG A 1 497 ? 22.256  3.657   3.026   1.00 180.32 ? 170 ARG B CB  1 
ATOM   1301 C CG  . ARG A 1 497 ? 22.354  2.853   1.746   1.00 175.60 ? 170 ARG B CG  1 
ATOM   1302 C CD  . ARG A 1 497 ? 21.964  1.400   1.994   1.00 182.79 ? 170 ARG B CD  1 
ATOM   1303 N NE  . ARG A 1 497 ? 23.023  0.664   2.675   1.00 185.42 ? 170 ARG B NE  1 
ATOM   1304 C CZ  . ARG A 1 497 ? 23.130  0.537   3.992   1.00 187.71 ? 170 ARG B CZ  1 
ATOM   1305 N NH1 . ARG A 1 497 ? 22.221  1.040   4.811   1.00 192.28 ? 170 ARG B NH1 1 
ATOM   1306 N NH2 . ARG A 1 497 ? 24.176  -0.110  4.500   1.00 186.57 ? 170 ARG B NH2 1 
ATOM   1307 N N   . GLU A 1 498 ? 24.071  5.285   4.864   1.00 181.37 ? 171 GLU B N   1 
ATOM   1308 C CA  . GLU A 1 498 ? 24.451  5.729   6.201   1.00 198.57 ? 171 GLU B CA  1 
ATOM   1309 C C   . GLU A 1 498 ? 24.577  7.246   6.281   1.00 214.79 ? 171 GLU B C   1 
ATOM   1310 O O   . GLU A 1 498 ? 24.392  7.825   7.357   1.00 215.64 ? 171 GLU B O   1 
ATOM   1311 C CB  . GLU A 1 498 ? 25.761  5.062   6.625   1.00 169.26 ? 171 GLU B CB  1 
ATOM   1312 C CG  . GLU A 1 498 ? 25.646  3.566   6.879   1.00 163.81 ? 171 GLU B CG  1 
ATOM   1313 C CD  . GLU A 1 498 ? 26.806  2.786   6.293   1.00 161.19 ? 171 GLU B CD  1 
ATOM   1314 O OE1 . GLU A 1 498 ? 27.937  3.314   6.295   1.00 149.38 ? 171 GLU B OE1 1 
ATOM   1315 O OE2 . GLU A 1 498 ? 26.587  1.645   5.834   1.00 160.19 ? 171 GLU B OE2 1 
ATOM   1316 N N   . GLU A 1 499 ? 24.884  7.905   5.161   1.00 198.14 ? 172 GLU B N   1 
ATOM   1317 C CA  . GLU A 1 499 ? 24.961  9.363   5.162   1.00 200.23 ? 172 GLU B CA  1 
ATOM   1318 C C   . GLU A 1 499 ? 23.586  9.993   5.354   1.00 193.20 ? 172 GLU B C   1 
ATOM   1319 O O   . GLU A 1 499 ? 23.441  10.963  6.106   1.00 185.37 ? 172 GLU B O   1 
ATOM   1320 C CB  . GLU A 1 499 ? 25.602  9.859   3.867   1.00 193.93 ? 172 GLU B CB  1 
ATOM   1321 C CG  . GLU A 1 499 ? 27.099  9.612   3.785   1.00 206.40 ? 172 GLU B CG  1 
ATOM   1322 C CD  . GLU A 1 499 ? 27.563  9.286   2.379   1.00 208.31 ? 172 GLU B CD  1 
ATOM   1323 O OE1 . GLU A 1 499 ? 26.949  9.792   1.415   1.00 205.55 ? 172 GLU B OE1 1 
ATOM   1324 O OE2 . GLU A 1 499 ? 28.539  8.520   2.237   1.00 229.49 ? 172 GLU B OE2 1 
ATOM   1325 N N   . ILE A 1 500 ? 22.565  9.459   4.680   1.00 199.19 ? 173 ILE B N   1 
ATOM   1326 C CA  . ILE A 1 500 ? 21.207  9.969   4.848   1.00 190.78 ? 173 ILE B CA  1 
ATOM   1327 C C   . ILE A 1 500 ? 20.507  9.315   6.038   1.00 194.50 ? 173 ILE B C   1 
ATOM   1328 O O   . ILE A 1 500 ? 19.551  9.887   6.580   1.00 177.63 ? 173 ILE B O   1 
ATOM   1329 C CB  . ILE A 1 500 ? 20.421  9.788   3.533   1.00 169.35 ? 173 ILE B CB  1 
ATOM   1330 C CG1 . ILE A 1 500 ? 21.020  10.677  2.439   1.00 165.68 ? 173 ILE B CG1 1 
ATOM   1331 C CG2 . ILE A 1 500 ? 18.944  10.125  3.698   1.00 127.40 ? 173 ILE B CG2 1 
ATOM   1332 C CD1 . ILE A 1 500 ? 20.471  10.398  1.051   1.00 114.33 ? 173 ILE B CD1 1 
ATOM   1333 N N   . ASP A 1 501 ? 20.977  8.150   6.483   1.00 209.34 ? 174 ASP B N   1 
ATOM   1334 C CA  . ASP A 1 501 ? 20.421  7.482   7.662   1.00 214.75 ? 174 ASP B CA  1 
ATOM   1335 C C   . ASP A 1 501 ? 20.444  8.390   8.892   1.00 205.05 ? 174 ASP B C   1 
ATOM   1336 O O   . ASP A 1 501 ? 21.385  9.159   9.097   1.00 216.71 ? 174 ASP B O   1 
ATOM   1337 C CB  . ASP A 1 501 ? 21.187  6.185   7.964   1.00 220.91 ? 174 ASP B CB  1 
ATOM   1338 C CG  . ASP A 1 501 ? 20.787  5.036   7.049   1.00 213.04 ? 174 ASP B CG  1 
ATOM   1339 O OD1 . ASP A 1 501 ? 19.763  5.155   6.343   1.00 223.05 ? 174 ASP B OD1 1 
ATOM   1340 O OD2 . ASP A 1 501 ? 21.502  4.011   7.036   1.00 207.70 ? 174 ASP B OD2 1 
ATOM   1341 N N   . GLN B 2 1   ? 13.544  7.929   -54.067 1.00 104.52 ? 1   GLN H N   1 
ATOM   1342 C CA  . GLN B 2 1   ? 12.567  7.013   -53.489 1.00 129.54 ? 1   GLN H CA  1 
ATOM   1343 C C   . GLN B 2 1   ? 13.198  5.663   -53.150 1.00 157.33 ? 1   GLN H C   1 
ATOM   1344 O O   . GLN B 2 1   ? 13.873  5.530   -52.137 1.00 164.15 ? 1   GLN H O   1 
ATOM   1345 C CB  . GLN B 2 1   ? 11.391  6.813   -54.443 1.00 116.80 ? 1   GLN H CB  1 
ATOM   1346 C CG  . GLN B 2 1   ? 10.545  8.052   -54.652 1.00 143.02 ? 1   GLN H CG  1 
ATOM   1347 C CD  . GLN B 2 1   ? 9.447   7.826   -55.665 1.00 151.06 ? 1   GLN H CD  1 
ATOM   1348 O OE1 . GLN B 2 1   ? 9.557   6.957   -56.531 1.00 123.44 ? 1   GLN H OE1 1 
ATOM   1349 N NE2 . GLN B 2 1   ? 8.382   8.613   -55.572 1.00 172.92 ? 1   GLN H NE2 1 
ATOM   1350 N N   . VAL B 2 2   ? 12.974  4.666   -54.005 1.00 168.88 ? 2   VAL H N   1 
ATOM   1351 C CA  . VAL B 2 2   ? 13.475  3.313   -53.773 1.00 173.30 ? 2   VAL H CA  1 
ATOM   1352 C C   . VAL B 2 2   ? 14.971  3.306   -54.065 1.00 174.72 ? 2   VAL H C   1 
ATOM   1353 O O   . VAL B 2 2   ? 15.376  3.315   -55.230 1.00 180.51 ? 2   VAL H O   1 
ATOM   1354 C CB  . VAL B 2 2   ? 12.741  2.286   -54.644 1.00 168.33 ? 2   VAL H CB  1 
ATOM   1355 C CG1 . VAL B 2 2   ? 13.298  0.877   -54.412 1.00 154.55 ? 2   VAL H CG1 1 
ATOM   1356 C CG2 . VAL B 2 2   ? 11.246  2.351   -54.418 1.00 164.17 ? 2   VAL H CG2 1 
ATOM   1357 N N   . GLN B 2 3   ? 15.805  3.281   -53.020 1.00 141.70 ? 3   GLN H N   1 
ATOM   1358 C CA  . GLN B 2 3   ? 17.272  3.181   -53.263 1.00 158.41 ? 3   GLN H CA  1 
ATOM   1359 C C   . GLN B 2 3   ? 17.948  2.334   -52.180 1.00 140.69 ? 3   GLN H C   1 
ATOM   1360 O O   . GLN B 2 3   ? 18.457  2.927   -51.207 1.00 147.64 ? 3   GLN H O   1 
ATOM   1361 C CB  . GLN B 2 3   ? 17.928  4.564   -53.326 1.00 173.29 ? 3   GLN H CB  1 
ATOM   1362 C CG  . GLN B 2 3   ? 17.478  5.422   -54.500 1.00 164.12 ? 3   GLN H CG  1 
ATOM   1363 C CD  . GLN B 2 3   ? 18.282  6.692   -54.624 1.00 178.05 ? 3   GLN H CD  1 
ATOM   1364 O OE1 . GLN B 2 3   ? 19.209  6.942   -53.857 1.00 191.18 ? 3   GLN H OE1 1 
ATOM   1365 N NE2 . GLN B 2 3   ? 17.935  7.507   -55.607 1.00 165.83 ? 3   GLN H NE2 1 
ATOM   1366 N N   . LEU B 2 4   ? 17.957  1.008   -52.342 1.00 124.94 ? 4   LEU H N   1 
ATOM   1367 C CA  . LEU B 2 4   ? 18.697  0.136   -51.389 1.00 111.61 ? 4   LEU H CA  1 
ATOM   1368 C C   . LEU B 2 4   ? 19.983  -0.322  -52.083 1.00 116.27 ? 4   LEU H C   1 
ATOM   1369 O O   . LEU B 2 4   ? 19.946  -1.370  -52.755 1.00 115.44 ? 4   LEU H O   1 
ATOM   1370 C CB  . LEU B 2 4   ? 17.820  -1.056  -50.995 1.00 120.92 ? 4   LEU H CB  1 
ATOM   1371 C CG  . LEU B 2 4   ? 16.648  -0.736  -50.069 1.00 141.95 ? 4   LEU H CG  1 
ATOM   1372 C CD1 . LEU B 2 4   ? 16.189  -1.983  -49.329 1.00 136.77 ? 4   LEU H CD1 1 
ATOM   1373 C CD2 . LEU B 2 4   ? 17.020  0.360   -49.081 1.00 124.46 ? 4   LEU H CD2 1 
ATOM   1374 N N   . VAL B 2 5   ? 21.069  0.441   -51.936 1.00 106.11 ? 5   VAL H N   1 
ATOM   1375 C CA  . VAL B 2 5   ? 22.335  0.115   -52.661 1.00 97.61  ? 5   VAL H CA  1 
ATOM   1376 C C   . VAL B 2 5   ? 23.134  -0.914  -51.858 1.00 108.42 ? 5   VAL H C   1 
ATOM   1377 O O   . VAL B 2 5   ? 23.582  -0.571  -50.748 1.00 113.63 ? 5   VAL H O   1 
ATOM   1378 C CB  . VAL B 2 5   ? 23.166  1.386   -52.920 1.00 97.64  ? 5   VAL H CB  1 
ATOM   1379 C CG1 . VAL B 2 5   ? 24.465  1.072   -53.647 1.00 110.19 ? 5   VAL H CG1 1 
ATOM   1380 C CG2 . VAL B 2 5   ? 22.366  2.433   -53.678 1.00 109.62 ? 5   VAL H CG2 1 
ATOM   1381 N N   . GLN B 2 6   ? 23.313  -2.121  -52.404 1.00 109.67 ? 6   GLN H N   1 
ATOM   1382 C CA  . GLN B 2 6   ? 24.116  -3.125  -51.729 1.00 101.99 ? 6   GLN H CA  1 
ATOM   1383 C C   . GLN B 2 6   ? 25.599  -2.908  -52.024 1.00 101.17 ? 6   GLN H C   1 
ATOM   1384 O O   . GLN B 2 6   ? 25.985  -2.065  -52.837 1.00 104.69 ? 6   GLN H O   1 
ATOM   1385 C CB  . GLN B 2 6   ? 23.673  -4.524  -52.151 1.00 101.96 ? 6   GLN H CB  1 
ATOM   1386 C CG  . GLN B 2 6   ? 22.227  -4.819  -51.805 1.00 108.32 ? 6   GLN H CG  1 
ATOM   1387 C CD  . GLN B 2 6   ? 21.923  -6.299  -51.773 1.00 111.02 ? 6   GLN H CD  1 
ATOM   1388 O OE1 . GLN B 2 6   ? 22.775  -7.110  -51.413 1.00 107.60 ? 6   GLN H OE1 1 
ATOM   1389 N NE2 . GLN B 2 6   ? 20.691  -6.657  -52.112 1.00 113.95 ? 6   GLN H NE2 1 
ATOM   1390 N N   . SER B 2 7   ? 26.440  -3.682  -51.344 1.00 107.55 ? 7   SER H N   1 
ATOM   1391 C CA  . SER B 2 7   ? 27.874  -3.548  -51.531 1.00 107.24 ? 7   SER H CA  1 
ATOM   1392 C C   . SER B 2 7   ? 28.322  -4.288  -52.792 1.00 120.45 ? 7   SER H C   1 
ATOM   1393 O O   . SER B 2 7   ? 27.540  -4.964  -53.465 1.00 122.05 ? 7   SER H O   1 
ATOM   1394 C CB  . SER B 2 7   ? 28.627  -4.076  -50.311 1.00 120.83 ? 7   SER H CB  1 
ATOM   1395 O OG  . SER B 2 7   ? 28.429  -5.469  -50.156 1.00 134.16 ? 7   SER H OG  1 
ATOM   1396 N N   . GLY B 2 8   ? 29.608  -4.148  -53.107 1.00 126.18 ? 8   GLY H N   1 
ATOM   1397 C CA  . GLY B 2 8   ? 30.153  -4.797  -54.280 1.00 129.00 ? 8   GLY H CA  1 
ATOM   1398 C C   . GLY B 2 8   ? 30.320  -6.291  -54.091 1.00 116.95 ? 8   GLY H C   1 
ATOM   1399 O O   . GLY B 2 8   ? 30.370  -6.810  -52.974 1.00 129.24 ? 8   GLY H O   1 
ATOM   1400 N N   . ALA B 2 9   ? 30.400  -6.993  -55.220 1.00 103.68 ? 9   ALA H N   1 
ATOM   1401 C CA  . ALA B 2 9   ? 30.578  -8.438  -55.195 1.00 113.02 ? 9   ALA H CA  1 
ATOM   1402 C C   . ALA B 2 9   ? 31.864  -8.802  -54.465 1.00 118.11 ? 9   ALA H C   1 
ATOM   1403 O O   . ALA B 2 9   ? 32.886  -8.122  -54.594 1.00 121.49 ? 9   ALA H O   1 
ATOM   1404 C CB  . ALA B 2 9   ? 30.599  -8.993  -56.620 1.00 110.22 ? 9   ALA H CB  1 
ATOM   1405 N N   . GLU B 2 10  ? 31.810  -9.883  -53.688 1.00 111.96 ? 10  GLU H N   1 
ATOM   1406 C CA  . GLU B 2 10  ? 32.904  -10.254 -52.803 1.00 111.30 ? 10  GLU H CA  1 
ATOM   1407 C C   . GLU B 2 10  ? 33.271  -11.718 -52.984 1.00 124.32 ? 10  GLU H C   1 
ATOM   1408 O O   . GLU B 2 10  ? 32.400  -12.577 -53.158 1.00 119.61 ? 10  GLU H O   1 
ATOM   1409 C CB  . GLU B 2 10  ? 32.544  -9.963  -51.343 1.00 138.25 ? 10  GLU H CB  1 
ATOM   1410 C CG  . GLU B 2 10  ? 32.436  -8.471  -51.067 1.00 168.93 ? 10  GLU H CG  1 
ATOM   1411 C CD  . GLU B 2 10  ? 32.008  -8.147  -49.654 1.00 186.16 ? 10  GLU H CD  1 
ATOM   1412 O OE1 . GLU B 2 10  ? 31.596  -9.069  -48.922 1.00 184.34 ? 10  GLU H OE1 1 
ATOM   1413 O OE2 . GLU B 2 10  ? 32.086  -6.960  -49.277 1.00 193.72 ? 10  GLU H OE2 1 
ATOM   1414 N N   . VAL B 2 11  ? 34.573  -11.988 -52.937 1.00 125.47 ? 11  VAL H N   1 
ATOM   1415 C CA  . VAL B 2 11  ? 35.136  -13.305 -53.200 1.00 126.72 ? 11  VAL H CA  1 
ATOM   1416 C C   . VAL B 2 11  ? 36.103  -13.635 -52.073 1.00 129.31 ? 11  VAL H C   1 
ATOM   1417 O O   . VAL B 2 11  ? 37.017  -12.851 -51.790 1.00 119.14 ? 11  VAL H O   1 
ATOM   1418 C CB  . VAL B 2 11  ? 35.859  -13.347 -54.559 1.00 121.71 ? 11  VAL H CB  1 
ATOM   1419 C CG1 . VAL B 2 11  ? 36.528  -14.683 -54.753 1.00 128.75 ? 11  VAL H CG1 1 
ATOM   1420 C CG2 . VAL B 2 11  ? 34.893  -13.042 -55.702 1.00 112.79 ? 11  VAL H CG2 1 
ATOM   1421 N N   . LYS B 2 12  ? 35.902  -14.784 -51.427 1.00 136.66 ? 12  LYS H N   1 
ATOM   1422 C CA  . LYS B 2 12  ? 36.745  -15.190 -50.309 1.00 147.66 ? 12  LYS H CA  1 
ATOM   1423 C C   . LYS B 2 12  ? 36.914  -16.703 -50.313 1.00 151.07 ? 12  LYS H C   1 
ATOM   1424 O O   . LYS B 2 12  ? 36.307  -17.421 -51.112 1.00 153.20 ? 12  LYS H O   1 
ATOM   1425 C CB  . LYS B 2 12  ? 36.175  -14.702 -48.969 1.00 133.20 ? 12  LYS H CB  1 
ATOM   1426 C CG  . LYS B 2 12  ? 36.242  -13.194 -48.832 1.00 129.40 ? 12  LYS H CG  1 
ATOM   1427 C CD  . LYS B 2 12  ? 35.666  -12.653 -47.551 1.00 118.76 ? 12  LYS H CD  1 
ATOM   1428 C CE  . LYS B 2 12  ? 35.833  -11.143 -47.564 1.00 119.46 ? 12  LYS H CE  1 
ATOM   1429 N NZ  . LYS B 2 12  ? 35.289  -10.473 -46.363 1.00 152.86 ? 12  LYS H NZ  1 
ATOM   1430 N N   . LYS B 2 13  ? 37.785  -17.182 -49.401 1.00 143.52 ? 13  LYS H N   1 
ATOM   1431 C CA  . LYS B 2 13  ? 38.139  -18.560 -49.111 1.00 137.94 ? 13  LYS H CA  1 
ATOM   1432 C C   . LYS B 2 13  ? 37.445  -19.022 -47.836 1.00 138.38 ? 13  LYS H C   1 
ATOM   1433 O O   . LYS B 2 13  ? 37.126  -18.202 -46.969 1.00 137.53 ? 13  LYS H O   1 
ATOM   1434 C CB  . LYS B 2 13  ? 39.657  -18.706 -48.956 1.00 147.97 ? 13  LYS H CB  1 
ATOM   1435 C CG  . LYS B 2 13  ? 40.424  -18.465 -50.249 1.00 154.95 ? 13  LYS H CG  1 
ATOM   1436 C CD  . LYS B 2 13  ? 41.926  -18.590 -50.056 1.00 132.48 ? 13  LYS H CD  1 
ATOM   1437 C CE  . LYS B 2 13  ? 42.661  -18.367 -51.370 1.00 123.23 ? 13  LYS H CE  1 
ATOM   1438 N NZ  . LYS B 2 13  ? 44.138  -18.461 -51.208 1.00 115.63 ? 13  LYS H NZ  1 
ATOM   1439 N N   . PRO B 2 14  ? 37.181  -20.323 -47.702 1.00 160.65 ? 14  PRO H N   1 
ATOM   1440 C CA  . PRO B 2 14  ? 36.437  -20.802 -46.531 1.00 151.96 ? 14  PRO H CA  1 
ATOM   1441 C C   . PRO B 2 14  ? 37.135  -20.438 -45.230 1.00 155.84 ? 14  PRO H C   1 
ATOM   1442 O O   . PRO B 2 14  ? 38.360  -20.521 -45.112 1.00 146.64 ? 14  PRO H O   1 
ATOM   1443 C CB  . PRO B 2 14  ? 36.392  -22.319 -46.742 1.00 150.08 ? 14  PRO H CB  1 
ATOM   1444 C CG  . PRO B 2 14  ? 36.474  -22.477 -48.223 1.00 164.39 ? 14  PRO H CG  1 
ATOM   1445 C CD  . PRO B 2 14  ? 37.451  -21.416 -48.653 1.00 166.62 ? 14  PRO H CD  1 
ATOM   1446 N N   . GLY B 2 15  ? 36.337  -20.014 -44.254 1.00 154.12 ? 15  GLY H N   1 
ATOM   1447 C CA  . GLY B 2 15  ? 36.854  -19.668 -42.947 1.00 156.93 ? 15  GLY H CA  1 
ATOM   1448 C C   . GLY B 2 15  ? 37.289  -18.232 -42.775 1.00 151.64 ? 15  GLY H C   1 
ATOM   1449 O O   . GLY B 2 15  ? 37.987  -17.928 -41.801 1.00 177.26 ? 15  GLY H O   1 
ATOM   1450 N N   . ALA B 2 16  ? 36.908  -17.338 -43.682 1.00 150.84 ? 16  ALA H N   1 
ATOM   1451 C CA  . ALA B 2 16  ? 37.247  -15.927 -43.583 1.00 153.04 ? 16  ALA H CA  1 
ATOM   1452 C C   . ALA B 2 16  ? 35.977  -15.107 -43.417 1.00 143.91 ? 16  ALA H C   1 
ATOM   1453 O O   . ALA B 2 16  ? 34.919  -15.463 -43.941 1.00 156.02 ? 16  ALA H O   1 
ATOM   1454 C CB  . ALA B 2 16  ? 38.021  -15.447 -44.816 1.00 153.80 ? 16  ALA H CB  1 
ATOM   1455 N N   . SER B 2 17  ? 36.087  -14.004 -42.686 1.00 114.92 ? 17  SER H N   1 
ATOM   1456 C CA  . SER B 2 17  ? 34.926  -13.170 -42.414 1.00 137.76 ? 17  SER H CA  1 
ATOM   1457 C C   . SER B 2 17  ? 34.532  -12.376 -43.652 1.00 139.93 ? 17  SER H C   1 
ATOM   1458 O O   . SER B 2 17  ? 35.389  -11.902 -44.404 1.00 130.47 ? 17  SER H O   1 
ATOM   1459 C CB  . SER B 2 17  ? 35.213  -12.224 -41.249 1.00 159.53 ? 17  SER H CB  1 
ATOM   1460 O OG  . SER B 2 17  ? 35.474  -12.954 -40.064 1.00 143.43 ? 17  SER H OG  1 
ATOM   1461 N N   . VAL B 2 18  ? 33.224  -12.236 -43.862 1.00 128.23 ? 18  VAL H N   1 
ATOM   1462 C CA  . VAL B 2 18  ? 32.672  -11.489 -44.984 1.00 117.43 ? 18  VAL H CA  1 
ATOM   1463 C C   . VAL B 2 18  ? 31.810  -10.361 -44.434 1.00 114.72 ? 18  VAL H C   1 
ATOM   1464 O O   . VAL B 2 18  ? 31.118  -10.536 -43.428 1.00 111.96 ? 18  VAL H O   1 
ATOM   1465 C CB  . VAL B 2 18  ? 31.864  -12.402 -45.932 1.00 125.21 ? 18  VAL H CB  1 
ATOM   1466 C CG1 . VAL B 2 18  ? 30.657  -12.990 -45.229 1.00 130.62 ? 18  VAL H CG1 1 
ATOM   1467 C CG2 . VAL B 2 18  ? 31.446  -11.650 -47.178 1.00 125.77 ? 18  VAL H CG2 1 
ATOM   1468 N N   . LYS B 2 19  ? 31.867  -9.197  -45.083 1.00 133.05 ? 19  LYS H N   1 
ATOM   1469 C CA  . LYS B 2 19  ? 31.135  -8.010  -44.645 1.00 132.57 ? 19  LYS H CA  1 
ATOM   1470 C C   . LYS B 2 19  ? 30.399  -7.403  -45.833 1.00 130.24 ? 19  LYS H C   1 
ATOM   1471 O O   . LYS B 2 19  ? 31.031  -6.883  -46.757 1.00 147.46 ? 19  LYS H O   1 
ATOM   1472 C CB  . LYS B 2 19  ? 32.076  -6.980  -44.022 1.00 135.10 ? 19  LYS H CB  1 
ATOM   1473 C CG  . LYS B 2 19  ? 31.375  -5.731  -43.507 1.00 119.02 ? 19  LYS H CG  1 
ATOM   1474 C CD  . LYS B 2 19  ? 32.363  -4.772  -42.860 1.00 137.54 ? 19  LYS H CD  1 
ATOM   1475 C CE  . LYS B 2 19  ? 31.675  -3.507  -42.368 1.00 141.66 ? 19  LYS H CE  1 
ATOM   1476 N NZ  . LYS B 2 19  ? 32.635  -2.557  -41.737 1.00 154.03 ? 19  LYS H NZ  1 
ATOM   1477 N N   . VAL B 2 20  ? 29.070  -7.447  -45.797 1.00 113.54 ? 20  VAL H N   1 
ATOM   1478 C CA  . VAL B 2 20  ? 28.226  -6.867  -46.834 1.00 120.79 ? 20  VAL H CA  1 
ATOM   1479 C C   . VAL B 2 20  ? 27.570  -5.616  -46.267 1.00 111.42 ? 20  VAL H C   1 
ATOM   1480 O O   . VAL B 2 20  ? 27.216  -5.572  -45.083 1.00 117.59 ? 20  VAL H O   1 
ATOM   1481 C CB  . VAL B 2 20  ? 27.170  -7.875  -47.328 1.00 127.03 ? 20  VAL H CB  1 
ATOM   1482 C CG1 . VAL B 2 20  ? 26.494  -7.378  -48.602 1.00 110.26 ? 20  VAL H CG1 1 
ATOM   1483 C CG2 . VAL B 2 20  ? 27.806  -9.235  -47.550 1.00 136.96 ? 20  VAL H CG2 1 
ATOM   1484 N N   . SER B 2 21  ? 27.418  -4.597  -47.108 1.00 94.94  ? 21  SER H N   1 
ATOM   1485 C CA  . SER B 2 21  ? 26.848  -3.326  -46.689 1.00 97.85  ? 21  SER H CA  1 
ATOM   1486 C C   . SER B 2 21  ? 25.688  -2.964  -47.602 1.00 110.92 ? 21  SER H C   1 
ATOM   1487 O O   . SER B 2 21  ? 25.796  -3.088  -48.827 1.00 117.67 ? 21  SER H O   1 
ATOM   1488 C CB  . SER B 2 21  ? 27.901  -2.219  -46.714 1.00 119.99 ? 21  SER H CB  1 
ATOM   1489 O OG  . SER B 2 21  ? 28.111  -1.762  -48.037 1.00 156.75 ? 21  SER H OG  1 
ATOM   1490 N N   . CYS B 2 22  ? 24.595  -2.495  -47.002 1.00 112.86 ? 22  CYS H N   1 
ATOM   1491 C CA  . CYS B 2 22  ? 23.440  -2.026  -47.807 1.00 116.25 ? 22  CYS H CA  1 
ATOM   1492 C C   . CYS B 2 22  ? 23.173  -0.579  -47.395 1.00 121.32 ? 22  CYS H C   1 
ATOM   1493 O O   . CYS B 2 22  ? 22.643  -0.375  -46.290 1.00 131.21 ? 22  CYS H O   1 
ATOM   1494 C CB  . CYS B 2 22  ? 22.221  -2.907  -47.574 1.00 107.25 ? 22  CYS H CB  1 
ATOM   1495 S SG  . CYS B 2 22  ? 22.344  -4.470  -48.481 1.00 179.98 ? 22  CYS H SG  1 
ATOM   1496 N N   . LYS B 2 23  ? 23.607  0.377   -48.217 1.00 112.99 ? 23  LYS H N   1 
ATOM   1497 C CA  . LYS B 2 23  ? 23.419  1.811   -47.879 1.00 119.52 ? 23  LYS H CA  1 
ATOM   1498 C C   . LYS B 2 23  ? 22.046  2.224   -48.400 1.00 138.61 ? 23  LYS H C   1 
ATOM   1499 O O   . LYS B 2 23  ? 21.687  1.787   -49.506 1.00 141.09 ? 23  LYS H O   1 
ATOM   1500 C CB  . LYS B 2 23  ? 24.532  2.683   -48.465 1.00 123.51 ? 23  LYS H CB  1 
ATOM   1501 C CG  . LYS B 2 23  ? 24.469  4.166   -48.121 1.00 145.32 ? 23  LYS H CG  1 
ATOM   1502 C CD  . LYS B 2 23  ? 25.721  4.931   -48.499 1.00 159.35 ? 23  LYS H CD  1 
ATOM   1503 C CE  . LYS B 2 23  ? 25.884  5.102   -49.994 1.00 182.26 ? 23  LYS H CE  1 
ATOM   1504 N NZ  . LYS B 2 23  ? 27.007  6.011   -50.323 1.00 200.91 ? 23  LYS H NZ  1 
ATOM   1505 N N   . ALA B 2 24  ? 21.299  2.981   -47.597 1.00 137.33 ? 24  ALA H N   1 
ATOM   1506 C CA  . ALA B 2 24  ? 19.908  3.295   -47.982 1.00 146.93 ? 24  ALA H CA  1 
ATOM   1507 C C   . ALA B 2 24  ? 19.654  4.798   -47.939 1.00 168.24 ? 24  ALA H C   1 
ATOM   1508 O O   . ALA B 2 24  ? 20.195  5.460   -47.034 1.00 173.04 ? 24  ALA H O   1 
ATOM   1509 C CB  . ALA B 2 24  ? 18.994  2.587   -47.022 1.00 159.66 ? 24  ALA H CB  1 
ATOM   1510 N N   . SER B 2 25  ? 18.838  5.295   -48.868 1.00 179.92 ? 25  SER H N   1 
ATOM   1511 C CA  . SER B 2 25  ? 18.466  6.730   -48.879 1.00 186.09 ? 25  SER H CA  1 
ATOM   1512 C C   . SER B 2 25  ? 17.323  6.918   -49.874 1.00 196.59 ? 25  SER H C   1 
ATOM   1513 O O   . SER B 2 25  ? 16.754  5.905   -50.321 1.00 210.61 ? 25  SER H O   1 
ATOM   1514 C CB  . SER B 2 25  ? 19.633  7.605   -49.230 1.00 189.82 ? 25  SER H CB  1 
ATOM   1515 O OG  . SER B 2 25  ? 19.299  8.977   -49.080 1.00 191.56 ? 25  SER H OG  1 
ATOM   1516 N N   . GLY B 2 26  ? 17.003  8.170   -50.196 1.00 195.93 ? 26  GLY H N   1 
ATOM   1517 C CA  . GLY B 2 26  ? 15.889  8.446   -51.119 1.00 193.36 ? 26  GLY H CA  1 
ATOM   1518 C C   . GLY B 2 26  ? 14.560  8.145   -50.453 1.00 202.51 ? 26  GLY H C   1 
ATOM   1519 O O   . GLY B 2 26  ? 13.520  8.284   -51.127 1.00 211.21 ? 26  GLY H O   1 
ATOM   1520 N N   . TYR B 2 27  ? 14.596  7.712   -49.191 1.00 209.72 ? 27  TYR H N   1 
ATOM   1521 C CA  . TYR B 2 27  ? 13.350  7.378   -48.455 1.00 185.83 ? 27  TYR H CA  1 
ATOM   1522 C C   . TYR B 2 27  ? 13.591  7.586   -46.958 1.00 185.98 ? 27  TYR H C   1 
ATOM   1523 O O   . TYR B 2 27  ? 14.713  7.310   -46.488 1.00 213.36 ? 27  TYR H O   1 
ATOM   1524 C CB  . TYR B 2 27  ? 12.909  5.948   -48.773 1.00 188.51 ? 27  TYR H CB  1 
ATOM   1525 C CG  . TYR B 2 27  ? 11.435  5.695   -48.583 1.00 198.48 ? 27  TYR H CG  1 
ATOM   1526 C CD1 . TYR B 2 27  ? 10.490  6.458   -49.248 1.00 225.53 ? 27  TYR H CD1 1 
ATOM   1527 C CD2 . TYR B 2 27  ? 10.983  4.688   -47.748 1.00 200.21 ? 27  TYR H CD2 1 
ATOM   1528 C CE1 . TYR B 2 27  ? 9.134   6.233   -49.082 1.00 224.57 ? 27  TYR H CE1 1 
ATOM   1529 C CE2 . TYR B 2 27  ? 9.631   4.448   -47.571 1.00 218.20 ? 27  TYR H CE2 1 
ATOM   1530 C CZ  . TYR B 2 27  ? 8.702   5.223   -48.241 1.00 216.45 ? 27  TYR H CZ  1 
ATOM   1531 O OH  . TYR B 2 27  ? 7.359   4.991   -48.072 1.00 170.14 ? 27  TYR H OH  1 
ATOM   1532 N N   . SER B 2 28  ? 12.570  8.054   -46.236 1.00 177.00 ? 28  SER H N   1 
ATOM   1533 C CA  . SER B 2 28  ? 12.738  8.346   -44.790 1.00 185.10 ? 28  SER H CA  1 
ATOM   1534 C C   . SER B 2 28  ? 13.344  7.133   -44.080 1.00 166.84 ? 28  SER H C   1 
ATOM   1535 O O   . SER B 2 28  ? 12.797  6.025   -44.241 1.00 168.73 ? 28  SER H O   1 
ATOM   1536 C CB  . SER B 2 28  ? 11.427  8.741   -44.162 1.00 171.46 ? 28  SER H CB  1 
ATOM   1537 O OG  . SER B 2 28  ? 11.564  8.872   -42.755 1.00 121.00 ? 28  SER H OG  1 
ATOM   1538 N N   . PHE B 2 29  ? 14.435  7.336   -43.336 1.00 157.74 ? 29  PHE H N   1 
ATOM   1539 C CA  . PHE B 2 29  ? 15.024  6.227   -42.541 1.00 134.98 ? 29  PHE H CA  1 
ATOM   1540 C C   . PHE B 2 29  ? 14.626  6.433   -41.077 1.00 141.60 ? 29  PHE H C   1 
ATOM   1541 O O   . PHE B 2 29  ? 15.514  6.474   -40.204 1.00 161.28 ? 29  PHE H O   1 
ATOM   1542 C CB  . PHE B 2 29  ? 16.544  6.168   -42.714 1.00 134.24 ? 29  PHE H CB  1 
ATOM   1543 C CG  . PHE B 2 29  ? 17.185  4.908   -42.187 1.00 120.94 ? 29  PHE H CG  1 
ATOM   1544 C CD1 . PHE B 2 29  ? 16.869  3.672   -42.728 1.00 94.58  ? 29  PHE H CD1 1 
ATOM   1545 C CD2 . PHE B 2 29  ? 18.091  4.954   -41.140 1.00 136.59 ? 29  PHE H CD2 1 
ATOM   1546 C CE1 . PHE B 2 29  ? 17.454  2.513   -42.242 1.00 114.06 ? 29  PHE H CE1 1 
ATOM   1547 C CE2 . PHE B 2 29  ? 18.675  3.795   -40.654 1.00 124.33 ? 29  PHE H CE2 1 
ATOM   1548 C CZ  . PHE B 2 29  ? 18.356  2.576   -41.207 1.00 125.83 ? 29  PHE H CZ  1 
ATOM   1549 N N   . SER B 2 30  ? 13.322  6.574   -40.823 1.00 151.00 ? 30  SER H N   1 
ATOM   1550 C CA  . SER B 2 30  ? 12.832  6.774   -39.435 1.00 152.49 ? 30  SER H CA  1 
ATOM   1551 C C   . SER B 2 30  ? 12.970  5.461   -38.661 1.00 145.37 ? 30  SER H C   1 
ATOM   1552 O O   . SER B 2 30  ? 11.938  4.791   -38.457 1.00 160.72 ? 30  SER H O   1 
ATOM   1553 C CB  . SER B 2 30  ? 11.412  7.277   -39.424 1.00 166.23 ? 30  SER H CB  1 
ATOM   1554 O OG  . SER B 2 30  ? 10.939  7.415   -38.093 1.00 203.32 ? 30  SER H OG  1 
ATOM   1555 N N   . SER B 2 31  ? 14.199  5.106   -38.275 1.00 136.25 ? 31  SER H N   1 
ATOM   1556 C CA  . SER B 2 31  ? 14.447  3.879   -37.471 1.00 130.03 ? 31  SER H CA  1 
ATOM   1557 C C   . SER B 2 31  ? 13.973  2.620   -38.209 1.00 136.29 ? 31  SER H C   1 
ATOM   1558 O O   . SER B 2 31  ? 14.079  1.531   -37.614 1.00 158.00 ? 31  SER H O   1 
ATOM   1559 C CB  . SER B 2 31  ? 13.808  3.987   -36.110 1.00 149.83 ? 31  SER H CB  1 
ATOM   1560 O OG  . SER B 2 31  ? 12.418  3.701   -36.178 1.00 190.89 ? 31  SER H OG  1 
ATOM   1561 N N   . TYR B 2 32  ? 13.478  2.751   -39.446 1.00 125.39 ? 32  TYR H N   1 
ATOM   1562 C CA  . TYR B 2 32  ? 12.936  1.559   -40.144 1.00 106.91 ? 32  TYR H CA  1 
ATOM   1563 C C   . TYR B 2 32  ? 13.994  0.458   -40.117 1.00 104.25 ? 32  TYR H C   1 
ATOM   1564 O O   . TYR B 2 32  ? 15.187  0.768   -40.272 1.00 108.47 ? 32  TYR H O   1 
ATOM   1565 C CB  . TYR B 2 32  ? 12.561  1.902   -41.585 1.00 92.81  ? 32  TYR H CB  1 
ATOM   1566 C CG  . TYR B 2 32  ? 11.436  2.891   -41.738 1.00 116.14 ? 32  TYR H CG  1 
ATOM   1567 C CD1 . TYR B 2 32  ? 10.117  2.473   -41.757 1.00 127.69 ? 32  TYR H CD1 1 
ATOM   1568 C CD2 . TYR B 2 32  ? 11.690  4.244   -41.876 1.00 143.71 ? 32  TYR H CD2 1 
ATOM   1569 C CE1 . TYR B 2 32  ? 9.077   3.376   -41.901 1.00 155.13 ? 32  TYR H CE1 1 
ATOM   1570 C CE2 . TYR B 2 32  ? 10.663  5.160   -42.023 1.00 164.75 ? 32  TYR H CE2 1 
ATOM   1571 C CZ  . TYR B 2 32  ? 9.351   4.724   -42.035 1.00 171.08 ? 32  TYR H CZ  1 
ATOM   1572 O OH  . TYR B 2 32  ? 8.325   5.625   -42.179 1.00 182.76 ? 32  TYR H OH  1 
ATOM   1573 N N   . GLY B 2 33  ? 13.568  -0.791  -39.951 1.00 115.21 ? 33  GLY H N   1 
ATOM   1574 C CA  . GLY B 2 33  ? 14.539  -1.890  -39.820 1.00 107.54 ? 33  GLY H CA  1 
ATOM   1575 C C   . GLY B 2 33  ? 14.992  -2.436  -41.156 1.00 105.01 ? 33  GLY H C   1 
ATOM   1576 O O   . GLY B 2 33  ? 14.400  -2.054  -42.178 1.00 113.54 ? 33  GLY H O   1 
ATOM   1577 N N   . ILE B 2 34  ? 16.003  -3.302  -41.144 1.00 100.68 ? 34  ILE H N   1 
ATOM   1578 C CA  . ILE B 2 34  ? 16.533  -3.908  -42.361 1.00 104.81 ? 34  ILE H CA  1 
ATOM   1579 C C   . ILE B 2 34  ? 16.798  -5.383  -42.101 1.00 96.14  ? 34  ILE H C   1 
ATOM   1580 O O   . ILE B 2 34  ? 17.448  -5.738  -41.113 1.00 97.13  ? 34  ILE H O   1 
ATOM   1581 C CB  . ILE B 2 34  ? 17.824  -3.216  -42.837 1.00 108.54 ? 34  ILE H CB  1 
ATOM   1582 C CG1 . ILE B 2 34  ? 17.530  -1.763  -43.217 1.00 131.18 ? 34  ILE H CG1 1 
ATOM   1583 C CG2 . ILE B 2 34  ? 18.437  -3.988  -44.006 1.00 94.38  ? 34  ILE H CG2 1 
ATOM   1584 C CD1 . ILE B 2 34  ? 18.737  -0.986  -43.687 1.00 150.37 ? 34  ILE H CD1 1 
ATOM   1585 N N   . SER B 2 35  ? 16.306  -6.235  -42.994 1.00 97.46  ? 35  SER H N   1 
ATOM   1586 C CA  . SER B 2 35  ? 16.541  -7.666  -42.932 1.00 91.60  ? 35  SER H CA  1 
ATOM   1587 C C   . SER B 2 35  ? 17.330  -8.094  -44.163 1.00 106.63 ? 35  SER H C   1 
ATOM   1588 O O   . SER B 2 35  ? 17.270  -7.448  -45.214 1.00 122.48 ? 35  SER H O   1 
ATOM   1589 C CB  . SER B 2 35  ? 15.213  -8.435  -42.835 1.00 92.38  ? 35  SER H CB  1 
ATOM   1590 O OG  . SER B 2 35  ? 15.400  -9.830  -42.988 1.00 119.07 ? 35  SER H OG  1 
ATOM   1591 N N   . TRP B 2 36  ? 18.083  -9.182  -44.023 1.00 89.54  ? 36  TRP H N   1 
ATOM   1592 C CA  . TRP B 2 36  ? 18.954  -9.681  -45.078 1.00 89.86  ? 36  TRP H CA  1 
ATOM   1593 C C   . TRP B 2 36  ? 18.523  -11.084 -45.480 1.00 97.34  ? 36  TRP H C   1 
ATOM   1594 O O   . TRP B 2 36  ? 18.231  -11.920 -44.619 1.00 101.59 ? 36  TRP H O   1 
ATOM   1595 C CB  . TRP B 2 36  ? 20.409  -9.694  -44.617 1.00 74.06  ? 36  TRP H CB  1 
ATOM   1596 C CG  . TRP B 2 36  ? 20.938  -8.347  -44.276 1.00 103.35 ? 36  TRP H CG  1 
ATOM   1597 C CD1 . TRP B 2 36  ? 20.468  -7.499  -43.318 1.00 110.43 ? 36  TRP H CD1 1 
ATOM   1598 C CD2 . TRP B 2 36  ? 22.054  -7.691  -44.878 1.00 108.44 ? 36  TRP H CD2 1 
ATOM   1599 N NE1 . TRP B 2 36  ? 21.217  -6.351  -43.289 1.00 107.54 ? 36  TRP H NE1 1 
ATOM   1600 C CE2 . TRP B 2 36  ? 22.199  -6.443  -44.239 1.00 121.18 ? 36  TRP H CE2 1 
ATOM   1601 C CE3 . TRP B 2 36  ? 22.943  -8.034  -45.899 1.00 95.30  ? 36  TRP H CE3 1 
ATOM   1602 C CZ2 . TRP B 2 36  ? 23.197  -5.540  -44.588 1.00 120.64 ? 36  TRP H CZ2 1 
ATOM   1603 C CZ3 . TRP B 2 36  ? 23.932  -7.137  -46.242 1.00 125.06 ? 36  TRP H CZ3 1 
ATOM   1604 C CH2 . TRP B 2 36  ? 24.052  -5.904  -45.590 1.00 128.74 ? 36  TRP H CH2 1 
ATOM   1605 N N   . VAL B 2 37  ? 18.492  -11.339 -46.792 1.00 90.00  ? 37  VAL H N   1 
ATOM   1606 C CA  . VAL B 2 37  ? 18.010  -12.594 -47.358 1.00 91.95  ? 37  VAL H CA  1 
ATOM   1607 C C   . VAL B 2 37  ? 19.085  -13.175 -48.265 1.00 110.95 ? 37  VAL H C   1 
ATOM   1608 O O   . VAL B 2 37  ? 19.813  -12.442 -48.942 1.00 112.59 ? 37  VAL H O   1 
ATOM   1609 C CB  . VAL B 2 37  ? 16.687  -12.393 -48.141 1.00 101.68 ? 37  VAL H CB  1 
ATOM   1610 C CG1 . VAL B 2 37  ? 16.165  -13.714 -48.699 1.00 115.70 ? 37  VAL H CG1 1 
ATOM   1611 C CG2 . VAL B 2 37  ? 15.634  -11.727 -47.264 1.00 118.23 ? 37  VAL H CG2 1 
ATOM   1612 N N   . ARG B 2 38  ? 19.178  -14.505 -48.288 1.00 119.59 ? 38  ARG H N   1 
ATOM   1613 C CA  . ARG B 2 38  ? 20.162  -15.214 -49.095 1.00 129.32 ? 38  ARG H CA  1 
ATOM   1614 C C   . ARG B 2 38  ? 19.449  -16.103 -50.102 1.00 134.84 ? 38  ARG H C   1 
ATOM   1615 O O   . ARG B 2 38  ? 18.499  -16.807 -49.749 1.00 140.64 ? 38  ARG H O   1 
ATOM   1616 C CB  . ARG B 2 38  ? 21.094  -16.065 -48.224 1.00 121.49 ? 38  ARG H CB  1 
ATOM   1617 C CG  . ARG B 2 38  ? 21.981  -17.007 -49.032 1.00 136.75 ? 38  ARG H CG  1 
ATOM   1618 C CD  . ARG B 2 38  ? 22.413  -18.237 -48.248 1.00 148.08 ? 38  ARG H CD  1 
ATOM   1619 N NE  . ARG B 2 38  ? 23.075  -17.906 -46.992 1.00 140.07 ? 38  ARG H NE  1 
ATOM   1620 C CZ  . ARG B 2 38  ? 24.341  -18.189 -46.719 1.00 128.51 ? 38  ARG H CZ  1 
ATOM   1621 N NH1 . ARG B 2 38  ? 25.129  -18.752 -47.617 1.00 140.20 ? 38  ARG H NH1 1 
ATOM   1622 N NH2 . ARG B 2 38  ? 24.828  -17.894 -45.516 1.00 112.49 ? 38  ARG H NH2 1 
ATOM   1623 N N   . GLN B 2 39  ? 19.905  -16.068 -51.353 1.00 128.01 ? 39  GLN H N   1 
ATOM   1624 C CA  . GLN B 2 39  ? 19.436  -16.978 -52.394 1.00 127.37 ? 39  GLN H CA  1 
ATOM   1625 C C   . GLN B 2 39  ? 20.619  -17.817 -52.856 1.00 127.12 ? 39  GLN H C   1 
ATOM   1626 O O   . GLN B 2 39  ? 21.516  -17.307 -53.537 1.00 137.07 ? 39  GLN H O   1 
ATOM   1627 C CB  . GLN B 2 39  ? 18.825  -16.221 -53.574 1.00 124.12 ? 39  GLN H CB  1 
ATOM   1628 C CG  . GLN B 2 39  ? 18.188  -17.132 -54.627 1.00 148.13 ? 39  GLN H CG  1 
ATOM   1629 C CD  . GLN B 2 39  ? 17.574  -16.364 -55.784 1.00 154.09 ? 39  GLN H CD  1 
ATOM   1630 O OE1 . GLN B 2 39  ? 17.657  -15.139 -55.842 1.00 162.10 ? 39  GLN H OE1 1 
ATOM   1631 N NE2 . GLN B 2 39  ? 16.951  -17.086 -56.713 1.00 165.59 ? 39  GLN H NE2 1 
ATOM   1632 N N   . ALA B 2 40  ? 20.612  -19.100 -52.503 1.00 137.71 ? 40  ALA H N   1 
ATOM   1633 C CA  . ALA B 2 40  ? 21.684  -19.996 -52.989 1.00 142.88 ? 40  ALA H CA  1 
ATOM   1634 C C   . ALA B 2 40  ? 21.681  -19.966 -54.519 1.00 153.39 ? 40  ALA H C   1 
ATOM   1635 O O   . ALA B 2 40  ? 20.616  -19.690 -55.103 1.00 171.11 ? 40  ALA H O   1 
ATOM   1636 C CB  . ALA B 2 40  ? 21.468  -21.387 -52.451 1.00 150.97 ? 40  ALA H CB  1 
ATOM   1637 N N   . PRO B 2 41  ? 22.805  -20.256 -55.205 1.00 141.66 ? 41  PRO H N   1 
ATOM   1638 C CA  . PRO B 2 41  ? 22.854  -20.140 -56.658 1.00 154.72 ? 41  PRO H CA  1 
ATOM   1639 C C   . PRO B 2 41  ? 21.627  -20.822 -57.274 1.00 149.31 ? 41  PRO H C   1 
ATOM   1640 O O   . PRO B 2 41  ? 21.444  -22.001 -57.055 1.00 141.35 ? 41  PRO H O   1 
ATOM   1641 C CB  . PRO B 2 41  ? 24.145  -20.874 -57.049 1.00 149.19 ? 41  PRO H CB  1 
ATOM   1642 C CG  . PRO B 2 41  ? 24.605  -21.572 -55.783 1.00 140.71 ? 41  PRO H CG  1 
ATOM   1643 C CD  . PRO B 2 41  ? 24.063  -20.737 -54.643 1.00 139.13 ? 41  PRO H CD  1 
ATOM   1644 N N   . GLY B 2 42  ? 20.820  -20.059 -58.012 1.00 136.28 ? 42  GLY H N   1 
ATOM   1645 C CA  . GLY B 2 42  ? 19.633  -20.631 -58.672 1.00 113.56 ? 42  GLY H CA  1 
ATOM   1646 C C   . GLY B 2 42  ? 18.908  -21.598 -57.757 1.00 133.62 ? 42  GLY H C   1 
ATOM   1647 O O   . GLY B 2 42  ? 18.661  -22.737 -58.185 1.00 153.16 ? 42  GLY H O   1 
ATOM   1648 N N   . GLN B 2 43  ? 18.582  -21.161 -56.539 1.00 141.32 ? 43  GLN H N   1 
ATOM   1649 C CA  . GLN B 2 43  ? 17.875  -22.038 -55.571 1.00 122.82 ? 43  GLN H CA  1 
ATOM   1650 C C   . GLN B 2 43  ? 16.966  -21.167 -54.704 1.00 107.36 ? 43  GLN H C   1 
ATOM   1651 O O   . GLN B 2 43  ? 16.795  -19.983 -55.039 1.00 82.17  ? 43  GLN H O   1 
ATOM   1652 C CB  . GLN B 2 43  ? 18.872  -22.706 -54.625 1.00 131.71 ? 43  GLN H CB  1 
ATOM   1653 C CG  . GLN B 2 43  ? 19.646  -23.850 -55.263 1.00 143.91 ? 43  GLN H CG  1 
ATOM   1654 C CD  . GLN B 2 43  ? 20.869  -24.220 -54.463 1.00 164.11 ? 43  GLN H CD  1 
ATOM   1655 O OE1 . GLN B 2 43  ? 20.780  -24.622 -53.305 1.00 168.49 ? 43  GLN H OE1 1 
ATOM   1656 N NE2 . GLN B 2 43  ? 22.030  -24.083 -55.081 1.00 159.39 ? 43  GLN H NE2 1 
ATOM   1657 N N   . GLY B 2 44  ? 16.416  -21.737 -53.630 1.00 122.78 ? 44  GLY H N   1 
ATOM   1658 C CA  . GLY B 2 44  ? 15.479  -21.010 -52.803 1.00 118.67 ? 44  GLY H CA  1 
ATOM   1659 C C   . GLY B 2 44  ? 15.965  -19.773 -52.069 1.00 119.85 ? 44  GLY H C   1 
ATOM   1660 O O   . GLY B 2 44  ? 17.162  -19.513 -51.932 1.00 122.78 ? 44  GLY H O   1 
ATOM   1661 N N   . LEU B 2 45  ? 14.991  -19.008 -51.587 1.00 119.12 ? 45  LEU H N   1 
ATOM   1662 C CA  . LEU B 2 45  ? 15.223  -17.815 -50.784 1.00 115.12 ? 45  LEU H CA  1 
ATOM   1663 C C   . LEU B 2 45  ? 15.124  -18.153 -49.301 1.00 120.63 ? 45  LEU H C   1 
ATOM   1664 O O   . LEU B 2 45  ? 14.069  -18.580 -48.816 1.00 111.81 ? 45  LEU H O   1 
ATOM   1665 C CB  . LEU B 2 45  ? 14.238  -16.711 -51.169 1.00 110.61 ? 45  LEU H CB  1 
ATOM   1666 C CG  . LEU B 2 45  ? 14.415  -16.194 -52.602 1.00 132.34 ? 45  LEU H CG  1 
ATOM   1667 C CD1 . LEU B 2 45  ? 13.332  -15.208 -52.994 1.00 129.72 ? 45  LEU H CD1 1 
ATOM   1668 C CD2 . LEU B 2 45  ? 15.767  -15.535 -52.714 1.00 130.39 ? 45  LEU H CD2 1 
ATOM   1669 N N   . GLU B 2 46  ? 16.227  -17.948 -48.586 1.00 132.81 ? 46  GLU H N   1 
ATOM   1670 C CA  . GLU B 2 46  ? 16.327  -18.243 -47.165 1.00 116.34 ? 46  GLU H CA  1 
ATOM   1671 C C   . GLU B 2 46  ? 16.599  -16.944 -46.425 1.00 116.62 ? 46  GLU H C   1 
ATOM   1672 O O   . GLU B 2 46  ? 17.575  -16.246 -46.724 1.00 110.11 ? 46  GLU H O   1 
ATOM   1673 C CB  . GLU B 2 46  ? 17.424  -19.275 -46.898 1.00 99.94  ? 46  GLU H CB  1 
ATOM   1674 C CG  . GLU B 2 46  ? 18.759  -18.967 -47.561 1.00 131.30 ? 46  GLU H CG  1 
ATOM   1675 C CD  . GLU B 2 46  ? 19.747  -20.106 -47.437 1.00 143.72 ? 46  GLU H CD  1 
ATOM   1676 O OE1 . GLU B 2 46  ? 20.093  -20.468 -46.294 1.00 148.23 ? 46  GLU H OE1 1 
ATOM   1677 O OE2 . GLU B 2 46  ? 20.195  -20.625 -48.482 1.00 125.01 ? 46  GLU H OE2 1 
ATOM   1678 N N   . TRP B 2 47  ? 15.714  -16.622 -45.478 1.00 126.87 ? 47  TRP H N   1 
ATOM   1679 C CA  . TRP B 2 47  ? 15.896  -15.406 -44.647 1.00 120.15 ? 47  TRP H CA  1 
ATOM   1680 C C   . TRP B 2 47  ? 17.059  -15.648 -43.689 1.00 127.14 ? 47  TRP H C   1 
ATOM   1681 O O   . TRP B 2 47  ? 17.150  -16.762 -43.148 1.00 122.09 ? 47  TRP H O   1 
ATOM   1682 C CB  . TRP B 2 47  ? 14.614  -15.094 -43.879 1.00 107.52 ? 47  TRP H CB  1 
ATOM   1683 C CG  . TRP B 2 47  ? 14.832  -14.191 -42.707 1.00 124.89 ? 47  TRP H CG  1 
ATOM   1684 C CD1 . TRP B 2 47  ? 15.173  -12.871 -42.731 1.00 131.85 ? 47  TRP H CD1 1 
ATOM   1685 C CD2 . TRP B 2 47  ? 14.768  -14.564 -41.322 1.00 129.18 ? 47  TRP H CD2 1 
ATOM   1686 N NE1 . TRP B 2 47  ? 15.296  -12.391 -41.456 1.00 108.16 ? 47  TRP H NE1 1 
ATOM   1687 C CE2 . TRP B 2 47  ? 15.059  -13.408 -40.571 1.00 113.08 ? 47  TRP H CE2 1 
ATOM   1688 C CE3 . TRP B 2 47  ? 14.483  -15.756 -40.650 1.00 139.77 ? 47  TRP H CE3 1 
ATOM   1689 C CZ2 . TRP B 2 47  ? 15.071  -13.414 -39.179 1.00 122.68 ? 47  TRP H CZ2 1 
ATOM   1690 C CZ3 . TRP B 2 47  ? 14.495  -15.762 -39.275 1.00 123.92 ? 47  TRP H CZ3 1 
ATOM   1691 C CH2 . TRP B 2 47  ? 14.789  -14.606 -38.554 1.00 121.68 ? 47  TRP H CH2 1 
ATOM   1692 N N   . MET B 2 48  ? 17.908  -14.643 -43.490 1.00 121.39 ? 48  MET H N   1 
ATOM   1693 C CA  . MET B 2 48  ? 19.110  -14.843 -42.647 1.00 91.84  ? 48  MET H CA  1 
ATOM   1694 C C   . MET B 2 48  ? 18.950  -14.064 -41.342 1.00 104.56 ? 48  MET H C   1 
ATOM   1695 O O   . MET B 2 48  ? 19.240  -14.644 -40.282 1.00 123.12 ? 48  MET H O   1 
ATOM   1696 C CB  . MET B 2 48  ? 20.357  -14.353 -43.382 1.00 94.30  ? 48  MET H CB  1 
ATOM   1697 C CG  . MET B 2 48  ? 20.817  -15.271 -44.489 1.00 94.37  ? 48  MET H CG  1 
ATOM   1698 S SD  . MET B 2 48  ? 22.129  -14.486 -45.450 0.59 141.54 ? 48  MET H SD  1 
ATOM   1699 C CE  . MET B 2 48  ? 23.508  -14.684 -44.325 1.00 137.58 ? 48  MET H CE  1 
ATOM   1700 N N   . GLY B 2 49  ? 18.507  -12.806 -41.407 1.00 103.71 ? 49  GLY H N   1 
ATOM   1701 C CA  . GLY B 2 49  ? 18.451  -12.017 -40.163 1.00 100.24 ? 49  GLY H CA  1 
ATOM   1702 C C   . GLY B 2 49  ? 17.725  -10.697 -40.301 1.00 105.52 ? 49  GLY H C   1 
ATOM   1703 O O   . GLY B 2 49  ? 17.397  -10.329 -41.438 1.00 116.73 ? 49  GLY H O   1 
ATOM   1704 N N   . TRP B 2 50  ? 17.499  -10.008 -39.180 1.00 96.62  ? 50  TRP H N   1 
ATOM   1705 C CA  . TRP B 2 50  ? 16.810  -8.727  -39.173 1.00 96.12  ? 50  TRP H CA  1 
ATOM   1706 C C   . TRP B 2 50  ? 17.386  -7.902  -38.033 1.00 101.92 ? 50  TRP H C   1 
ATOM   1707 O O   . TRP B 2 50  ? 17.671  -8.435  -36.958 1.00 107.58 ? 50  TRP H O   1 
ATOM   1708 C CB  . TRP B 2 50  ? 15.304  -8.903  -38.945 1.00 109.50 ? 50  TRP H CB  1 
ATOM   1709 C CG  . TRP B 2 50  ? 14.634  -7.667  -38.430 1.00 110.70 ? 50  TRP H CG  1 
ATOM   1710 C CD1 . TRP B 2 50  ? 14.349  -6.535  -39.137 1.00 106.81 ? 50  TRP H CD1 1 
ATOM   1711 C CD2 . TRP B 2 50  ? 14.209  -7.416  -37.085 1.00 120.36 ? 50  TRP H CD2 1 
ATOM   1712 N NE1 . TRP B 2 50  ? 13.745  -5.608  -38.323 1.00 111.58 ? 50  TRP H NE1 1 
ATOM   1713 C CE2 . TRP B 2 50  ? 13.653  -6.123  -37.057 1.00 114.42 ? 50  TRP H CE2 1 
ATOM   1714 C CE3 . TRP B 2 50  ? 14.236  -8.164  -35.904 1.00 128.35 ? 50  TRP H CE3 1 
ATOM   1715 C CZ2 . TRP B 2 50  ? 13.128  -5.562  -35.897 1.00 117.76 ? 50  TRP H CZ2 1 
ATOM   1716 C CZ3 . TRP B 2 50  ? 13.717  -7.602  -34.751 1.00 125.66 ? 50  TRP H CZ3 1 
ATOM   1717 C CH2 . TRP B 2 50  ? 13.170  -6.315  -34.757 1.00 129.28 ? 50  TRP H CH2 1 
ATOM   1718 N N   . ILE B 2 51  ? 17.565  -6.600  -38.280 1.00 109.75 ? 51  ILE H N   1 
ATOM   1719 C CA  . ILE B 2 51  ? 18.059  -5.677  -37.217 1.00 107.76 ? 51  ILE H CA  1 
ATOM   1720 C C   . ILE B 2 51  ? 17.190  -4.416  -37.242 1.00 113.42 ? 51  ILE H C   1 
ATOM   1721 O O   . ILE B 2 51  ? 16.919  -3.904  -38.343 1.00 112.25 ? 51  ILE H O   1 
ATOM   1722 C CB  . ILE B 2 51  ? 19.551  -5.346  -37.402 1.00 99.54  ? 51  ILE H CB  1 
ATOM   1723 C CG1 . ILE B 2 51  ? 20.026  -4.307  -36.383 1.00 92.56  ? 51  ILE H CG1 1 
ATOM   1724 C CG2 . ILE B 2 51  ? 19.849  -4.911  -38.828 1.00 101.48 ? 51  ILE H CG2 1 
ATOM   1725 C CD1 . ILE B 2 51  ? 21.484  -4.432  -36.019 1.00 112.25 ? 51  ILE H CD1 1 
ATOM   1726 N N   . SER B 2 52  ? 16.741  -3.964  -36.071 1.00 109.02 ? 52  SER H N   1 
ATOM   1727 C CA  . SER B 2 52  ? 15.903  -2.745  -35.985 1.00 103.18 ? 52  SER H CA  1 
ATOM   1728 C C   . SER B 2 52  ? 16.813  -1.546  -35.757 1.00 109.05 ? 52  SER H C   1 
ATOM   1729 O O   . SER B 2 52  ? 17.488  -1.526  -34.727 1.00 119.29 ? 52  SER H O   1 
ATOM   1730 C CB  . SER B 2 52  ? 14.909  -2.856  -34.872 1.00 94.56  ? 52  SER H CB  1 
ATOM   1731 O OG  . SER B 2 52  ? 14.899  -1.680  -34.080 1.00 103.72 ? 52  SER H OG  1 
ATOM   1732 N N   . ALA B 2 53  ? 16.820  -0.588  -36.679 1.00 94.55  ? 53  ALA H N   1 
ATOM   1733 C CA  . ALA B 2 53  ? 17.612  0.637   -36.448 1.00 115.65 ? 53  ALA H CA  1 
ATOM   1734 C C   . ALA B 2 53  ? 17.087  1.322   -35.186 1.00 134.20 ? 53  ALA H C   1 
ATOM   1735 O O   . ALA B 2 53  ? 17.899  1.903   -34.449 1.00 141.72 ? 53  ALA H O   1 
ATOM   1736 C CB  . ALA B 2 53  ? 17.511  1.538   -37.645 1.00 113.74 ? 53  ALA H CB  1 
ATOM   1737 N N   . TYR B 2 54  ? 15.778  1.240   -34.945 1.00 130.78 ? 54  TYR H N   1 
ATOM   1738 C CA  . TYR B 2 54  ? 15.179  1.830   -33.722 1.00 132.40 ? 54  TYR H CA  1 
ATOM   1739 C C   . TYR B 2 54  ? 15.901  1.291   -32.489 1.00 149.43 ? 54  TYR H C   1 
ATOM   1740 O O   . TYR B 2 54  ? 16.134  2.068   -31.549 1.00 196.02 ? 54  TYR H O   1 
ATOM   1741 C CB  . TYR B 2 54  ? 13.695  1.474   -33.636 1.00 136.17 ? 54  TYR H CB  1 
ATOM   1742 C CG  . TYR B 2 54  ? 12.908  2.244   -32.608 1.00 162.43 ? 54  TYR H CG  1 
ATOM   1743 C CD1 . TYR B 2 54  ? 12.370  3.484   -32.904 1.00 165.56 ? 54  TYR H CD1 1 
ATOM   1744 C CD2 . TYR B 2 54  ? 12.691  1.730   -31.341 1.00 185.21 ? 54  TYR H CD2 1 
ATOM   1745 C CE1 . TYR B 2 54  ? 11.643  4.200   -31.969 1.00 162.63 ? 54  TYR H CE1 1 
ATOM   1746 C CE2 . TYR B 2 54  ? 11.969  2.434   -30.392 1.00 190.12 ? 54  TYR H CE2 1 
ATOM   1747 C CZ  . TYR B 2 54  ? 11.442  3.672   -30.708 1.00 178.68 ? 54  TYR H CZ  1 
ATOM   1748 O OH  . TYR B 2 54  ? 10.724  4.377   -29.774 1.00 163.48 ? 54  TYR H OH  1 
ATOM   1749 N N   . ASN B 2 55  ? 16.238  0.002   -32.491 1.00 131.42 ? 55  ASN H N   1 
ATOM   1750 C CA  . ASN B 2 55  ? 16.850  -0.601  -31.282 1.00 140.15 ? 55  ASN H CA  1 
ATOM   1751 C C   . ASN B 2 55  ? 18.064  -1.407  -31.733 1.00 125.74 ? 55  ASN H C   1 
ATOM   1752 O O   . ASN B 2 55  ? 18.658  -1.054  -32.763 1.00 128.51 ? 55  ASN H O   1 
ATOM   1753 C CB  . ASN B 2 55  ? 15.892  -1.599  -30.636 1.00 155.02 ? 55  ASN H CB  1 
ATOM   1754 C CG  . ASN B 2 55  ? 15.994  -1.621  -29.127 1.00 184.61 ? 55  ASN H CG  1 
ATOM   1755 O OD1 . ASN B 2 55  ? 16.114  -0.576  -28.494 1.00 204.14 ? 55  ASN H OD1 1 
ATOM   1756 N ND2 . ASN B 2 55  ? 15.951  -2.808  -28.545 1.00 192.00 ? 55  ASN H ND2 1 
ATOM   1757 N N   . GLY B 2 56  ? 18.461  -2.394  -30.937 1.00 118.87 ? 56  GLY H N   1 
ATOM   1758 C CA  . GLY B 2 56  ? 19.546  -3.313  -31.322 1.00 114.58 ? 56  GLY H CA  1 
ATOM   1759 C C   . GLY B 2 56  ? 18.979  -4.710  -31.340 1.00 129.89 ? 56  GLY H C   1 
ATOM   1760 O O   . GLY B 2 56  ? 19.673  -5.651  -30.918 1.00 122.56 ? 56  GLY H O   1 
ATOM   1761 N N   . ASN B 2 57  ? 17.740  -4.825  -31.808 1.00 137.13 ? 57  ASN H N   1 
ATOM   1762 C CA  . ASN B 2 57  ? 17.041  -6.102  -31.748 1.00 144.37 ? 57  ASN H CA  1 
ATOM   1763 C C   . ASN B 2 57  ? 17.347  -7.038  -32.913 1.00 129.62 ? 57  ASN H C   1 
ATOM   1764 O O   . ASN B 2 57  ? 16.552  -7.074  -33.862 1.00 151.09 ? 57  ASN H O   1 
ATOM   1765 C CB  . ASN B 2 57  ? 15.523  -5.849  -31.659 1.00 157.34 ? 57  ASN H CB  1 
ATOM   1766 C CG  . ASN B 2 57  ? 14.753  -7.100  -31.304 1.00 163.71 ? 57  ASN H CG  1 
ATOM   1767 O OD1 . ASN B 2 57  ? 15.266  -7.963  -30.597 1.00 188.51 ? 57  ASN H OD1 1 
ATOM   1768 N ND2 . ASN B 2 57  ? 13.533  -7.215  -31.801 1.00 164.16 ? 57  ASN H ND2 1 
ATOM   1769 N N   . THR B 2 58  ? 18.478  -7.734  -32.856 1.00 122.00 ? 58  THR H N   1 
ATOM   1770 C CA  . THR B 2 58  ? 18.842  -8.655  -33.918 1.00 107.60 ? 58  THR H CA  1 
ATOM   1771 C C   . THR B 2 58  ? 18.090  -9.962  -33.725 1.00 113.93 ? 58  THR H C   1 
ATOM   1772 O O   . THR B 2 58  ? 17.742  -10.349 -32.604 1.00 125.45 ? 58  THR H O   1 
ATOM   1773 C CB  . THR B 2 58  ? 20.345  -8.929  -33.933 1.00 100.36 ? 58  THR H CB  1 
ATOM   1774 O OG1 . THR B 2 58  ? 20.716  -9.646  -32.748 1.00 130.76 ? 58  THR H OG1 1 
ATOM   1775 C CG2 . THR B 2 58  ? 21.127  -7.627  -33.970 1.00 122.36 ? 58  THR H CG2 1 
ATOM   1776 N N   . ASN B 2 59  ? 17.802  -10.624 -34.837 1.00 106.76 ? 59  ASN H N   1 
ATOM   1777 C CA  . ASN B 2 59  ? 17.184  -11.948 -34.825 1.00 87.25  ? 59  ASN H CA  1 
ATOM   1778 C C   . ASN B 2 59  ? 17.872  -12.765 -35.918 1.00 117.11 ? 59  ASN H C   1 
ATOM   1779 O O   . ASN B 2 59  ? 17.413  -12.852 -37.062 1.00 145.23 ? 59  ASN H O   1 
ATOM   1780 C CB  . ASN B 2 59  ? 15.671  -11.875 -34.991 1.00 109.36 ? 59  ASN H CB  1 
ATOM   1781 C CG  . ASN B 2 59  ? 15.029  -13.260 -35.027 1.00 140.29 ? 59  ASN H CG  1 
ATOM   1782 O OD1 . ASN B 2 59  ? 15.301  -14.102 -34.174 1.00 143.53 ? 59  ASN H OD1 1 
ATOM   1783 N ND2 . ASN B 2 59  ? 14.081  -13.459 -35.948 1.00 145.70 ? 59  ASN H ND2 1 
ATOM   1784 N N   . TYR B 2 60  ? 18.997  -13.361 -35.547 1.00 106.15 ? 60  TYR H N   1 
ATOM   1785 C CA  . TYR B 2 60  ? 19.720  -14.237 -36.449 1.00 120.08 ? 60  TYR H CA  1 
ATOM   1786 C C   . TYR B 2 60  ? 19.002  -15.576 -36.536 1.00 123.08 ? 60  TYR H C   1 
ATOM   1787 O O   . TYR B 2 60  ? 18.515  -16.103 -35.532 1.00 128.68 ? 60  TYR H O   1 
ATOM   1788 C CB  . TYR B 2 60  ? 21.155  -14.422 -35.964 1.00 122.53 ? 60  TYR H CB  1 
ATOM   1789 C CG  . TYR B 2 60  ? 21.851  -13.106 -35.720 1.00 104.94 ? 60  TYR H CG  1 
ATOM   1790 C CD1 . TYR B 2 60  ? 21.969  -12.167 -36.733 1.00 118.35 ? 60  TYR H CD1 1 
ATOM   1791 C CD2 . TYR B 2 60  ? 22.354  -12.786 -34.467 1.00 106.17 ? 60  TYR H CD2 1 
ATOM   1792 C CE1 . TYR B 2 60  ? 22.591  -10.955 -36.516 1.00 125.92 ? 60  TYR H CE1 1 
ATOM   1793 C CE2 . TYR B 2 60  ? 22.976  -11.574 -34.236 1.00 120.78 ? 60  TYR H CE2 1 
ATOM   1794 C CZ  . TYR B 2 60  ? 23.093  -10.660 -35.269 1.00 114.47 ? 60  TYR H CZ  1 
ATOM   1795 O OH  . TYR B 2 60  ? 23.708  -9.445  -35.061 1.00 92.72  ? 60  TYR H OH  1 
ATOM   1796 N N   . ALA B 2 61  ? 18.930  -16.130 -37.746 1.00 105.63 ? 61  ALA H N   1 
ATOM   1797 C CA  . ALA B 2 61  ? 18.246  -17.427 -37.940 1.00 109.49 ? 61  ALA H CA  1 
ATOM   1798 C C   . ALA B 2 61  ? 18.874  -18.606 -37.198 1.00 129.92 ? 61  ALA H C   1 
ATOM   1799 O O   . ALA B 2 61  ? 20.104  -18.700 -37.196 1.00 143.15 ? 61  ALA H O   1 
ATOM   1800 C CB  . ALA B 2 61  ? 18.149  -17.732 -39.410 1.00 95.10  ? 61  ALA H CB  1 
ATOM   1801 N N   . GLN B 2 62  ? 18.072  -19.433 -36.530 1.00 30.00  ? 62  GLN H N   1 
ATOM   1802 C CA  . GLN B 2 62  ? 18.658  -20.525 -35.708 1.00 30.00  ? 62  GLN H CA  1 
ATOM   1803 C C   . GLN B 2 62  ? 19.805  -21.178 -36.480 1.00 30.00  ? 62  GLN H C   1 
ATOM   1804 O O   . GLN B 2 62  ? 20.923  -21.237 -35.938 1.00 30.00  ? 62  GLN H O   1 
ATOM   1805 C CB  . GLN B 2 62  ? 17.599  -21.568 -35.355 1.00 30.00  ? 62  GLN H CB  1 
ATOM   1806 C CG  . GLN B 2 62  ? 18.137  -22.706 -34.501 1.00 30.00  ? 62  GLN H CG  1 
ATOM   1807 C CD  . GLN B 2 62  ? 18.856  -22.200 -33.275 1.00 30.00  ? 62  GLN H CD  1 
ATOM   1808 O OE1 . GLN B 2 62  ? 20.072  -22.326 -33.146 1.00 30.00  ? 62  GLN H OE1 1 
ATOM   1809 N NE2 . GLN B 2 62  ? 18.102  -21.619 -32.357 1.00 30.00  ? 62  GLN H NE2 1 
ATOM   1810 N N   . LYS B 2 63  ? 19.533  -21.635 -37.702 1.00 114.49 ? 63  LYS H N   1 
ATOM   1811 C CA  . LYS B 2 63  ? 20.563  -22.342 -38.505 1.00 120.09 ? 63  LYS H CA  1 
ATOM   1812 C C   . LYS B 2 63  ? 21.908  -21.631 -38.358 1.00 122.32 ? 63  LYS H C   1 
ATOM   1813 O O   . LYS B 2 63  ? 22.897  -22.304 -38.023 1.00 129.56 ? 63  LYS H O   1 
ATOM   1814 C CB  . LYS B 2 63  ? 20.131  -22.392 -39.971 1.00 109.77 ? 63  LYS H CB  1 
ATOM   1815 C CG  . LYS B 2 63  ? 21.220  -22.781 -40.961 1.00 112.79 ? 63  LYS H CG  1 
ATOM   1816 C CD  . LYS B 2 63  ? 20.763  -22.706 -42.401 1.00 115.44 ? 63  LYS H CD  1 
ATOM   1817 C CE  . LYS B 2 63  ? 19.266  -22.870 -42.553 1.00 128.04 ? 63  LYS H CE  1 
ATOM   1818 N NZ  . LYS B 2 63  ? 18.909  -24.213 -43.067 1.00 87.94  ? 63  LYS H NZ  1 
ATOM   1819 N N   . LEU B 2 64  ? 21.939  -20.322 -38.602 1.00 151.81 ? 64  LEU H N   1 
ATOM   1820 C CA  . LEU B 2 64  ? 23.225  -19.583 -38.559 1.00 145.23 ? 64  LEU H CA  1 
ATOM   1821 C C   . LEU B 2 64  ? 23.140  -18.492 -37.493 1.00 147.79 ? 64  LEU H C   1 
ATOM   1822 O O   . LEU B 2 64  ? 22.697  -17.381 -37.824 1.00 155.09 ? 64  LEU H O   1 
ATOM   1823 C CB  . LEU B 2 64  ? 23.481  -18.979 -39.940 1.00 128.55 ? 64  LEU H CB  1 
ATOM   1824 C CG  . LEU B 2 64  ? 24.227  -19.891 -40.911 1.00 150.83 ? 64  LEU H CG  1 
ATOM   1825 C CD1 . LEU B 2 64  ? 24.756  -19.103 -42.098 1.00 136.30 ? 64  LEU H CD1 1 
ATOM   1826 C CD2 . LEU B 2 64  ? 25.360  -20.618 -40.204 1.00 143.96 ? 64  LEU H CD2 1 
ATOM   1827 N N   . GLN B 2 65  ? 23.542  -18.809 -36.265 1.00 127.58 ? 65  GLN H N   1 
ATOM   1828 C CA  . GLN B 2 65  ? 23.481  -17.836 -35.177 1.00 126.85 ? 65  GLN H CA  1 
ATOM   1829 C C   . GLN B 2 65  ? 24.842  -17.338 -34.721 1.00 134.97 ? 65  GLN H C   1 
ATOM   1830 O O   . GLN B 2 65  ? 25.009  -16.135 -34.508 1.00 142.47 ? 65  GLN H O   1 
ATOM   1831 C CB  . GLN B 2 65  ? 22.740  -18.428 -33.973 1.00 121.23 ? 65  GLN H CB  1 
ATOM   1832 C CG  . GLN B 2 65  ? 21.233  -18.242 -34.034 1.00 134.29 ? 65  GLN H CG  1 
ATOM   1833 C CD  . GLN B 2 65  ? 20.539  -18.620 -32.747 1.00 143.82 ? 65  GLN H CD  1 
ATOM   1834 O OE1 . GLN B 2 65  ? 21.175  -19.040 -31.781 1.00 146.43 ? 65  GLN H OE1 1 
ATOM   1835 N NE2 . GLN B 2 65  ? 19.221  -18.472 -32.727 1.00 149.57 ? 65  GLN H NE2 1 
ATOM   1836 N N   . GLY B 2 66  ? 25.829  -18.223 -34.574 1.00 146.39 ? 66  GLY H N   1 
ATOM   1837 C CA  . GLY B 2 66  ? 27.130  -17.785 -34.093 1.00 154.59 ? 66  GLY H CA  1 
ATOM   1838 C C   . GLY B 2 66  ? 27.872  -16.929 -35.103 1.00 150.24 ? 66  GLY H C   1 
ATOM   1839 O O   . GLY B 2 66  ? 28.333  -15.831 -34.782 1.00 163.42 ? 66  GLY H O   1 
ATOM   1840 N N   . ARG B 2 67  ? 27.989  -17.418 -36.341 1.00 147.80 ? 67  ARG H N   1 
ATOM   1841 C CA  . ARG B 2 67  ? 28.755  -16.704 -37.361 1.00 138.94 ? 67  ARG H CA  1 
ATOM   1842 C C   . ARG B 2 67  ? 28.163  -15.331 -37.654 1.00 140.67 ? 67  ARG H C   1 
ATOM   1843 O O   . ARG B 2 67  ? 28.886  -14.329 -37.706 1.00 134.21 ? 67  ARG H O   1 
ATOM   1844 C CB  . ARG B 2 67  ? 28.825  -17.530 -38.646 1.00 141.07 ? 67  ARG H CB  1 
ATOM   1845 C CG  . ARG B 2 67  ? 29.164  -18.994 -38.459 1.00 150.50 ? 67  ARG H CG  1 
ATOM   1846 C CD  . ARG B 2 67  ? 29.006  -19.747 -39.769 1.00 157.13 ? 67  ARG H CD  1 
ATOM   1847 N NE  . ARG B 2 67  ? 29.713  -21.021 -39.756 1.00 176.14 ? 67  ARG H NE  1 
ATOM   1848 C CZ  . ARG B 2 67  ? 29.770  -21.855 -40.785 1.00 167.80 ? 67  ARG H CZ  1 
ATOM   1849 N NH1 . ARG B 2 67  ? 29.126  -21.604 -41.913 1.00 178.46 ? 67  ARG H NH1 1 
ATOM   1850 N NH2 . ARG B 2 67  ? 30.502  -22.960 -40.684 1.00 177.74 ? 67  ARG H NH2 1 
ATOM   1851 N N   . VAL B 2 68  ? 26.846  -15.268 -37.852 1.00 147.63 ? 68  VAL H N   1 
ATOM   1852 C CA  . VAL B 2 68  ? 26.211  -14.059 -38.364 1.00 136.32 ? 68  VAL H CA  1 
ATOM   1853 C C   . VAL B 2 68  ? 26.256  -12.961 -37.311 1.00 139.64 ? 68  VAL H C   1 
ATOM   1854 O O   . VAL B 2 68  ? 25.869  -13.169 -36.154 1.00 148.03 ? 68  VAL H O   1 
ATOM   1855 C CB  . VAL B 2 68  ? 24.768  -14.356 -38.796 1.00 147.21 ? 68  VAL H CB  1 
ATOM   1856 C CG1 . VAL B 2 68  ? 24.142  -13.134 -39.458 1.00 142.25 ? 68  VAL H CG1 1 
ATOM   1857 C CG2 . VAL B 2 68  ? 24.722  -15.570 -39.708 1.00 160.82 ? 68  VAL H CG2 1 
ATOM   1858 N N   . THR B 2 69  ? 26.732  -11.782 -37.710 1.00 133.46 ? 69  THR H N   1 
ATOM   1859 C CA  . THR B 2 69  ? 26.715  -10.587 -36.875 1.00 128.30 ? 69  THR H CA  1 
ATOM   1860 C C   . THR B 2 69  ? 26.241  -9.403  -37.705 1.00 131.29 ? 69  THR H C   1 
ATOM   1861 O O   . THR B 2 69  ? 26.799  -9.131  -38.773 1.00 125.48 ? 69  THR H O   1 
ATOM   1862 C CB  . THR B 2 69  ? 28.089  -10.304 -36.248 1.00 116.27 ? 69  THR H CB  1 
ATOM   1863 O OG1 . THR B 2 69  ? 29.076  -10.192 -37.281 1.00 150.80 ? 69  THR H OG1 1 
ATOM   1864 C CG2 . THR B 2 69  ? 28.487  -11.410 -35.273 1.00 83.30  ? 69  THR H CG2 1 
ATOM   1865 N N   . MET B 2 70  ? 25.214  -8.711  -37.217 1.00 121.86 ? 70  MET H N   1 
ATOM   1866 C CA  . MET B 2 70  ? 24.567  -7.623  -37.935 1.00 99.13  ? 70  MET H CA  1 
ATOM   1867 C C   . MET B 2 70  ? 24.659  -6.302  -37.182 1.00 84.23  ? 70  MET H C   1 
ATOM   1868 O O   . MET B 2 70  ? 24.577  -6.265  -35.950 1.00 98.10  ? 70  MET H O   1 
ATOM   1869 C CB  . MET B 2 70  ? 23.089  -7.966  -38.178 1.00 91.86  ? 70  MET H CB  1 
ATOM   1870 C CG  . MET B 2 70  ? 22.867  -9.122  -39.148 1.00 79.97  ? 70  MET H CG  1 
ATOM   1871 S SD  . MET B 2 70  ? 21.131  -9.567  -39.355 1.00 110.47 ? 70  MET H SD  1 
ATOM   1872 C CE  . MET B 2 70  ? 20.542  -8.174  -40.307 1.00 121.31 ? 70  MET H CE  1 
ATOM   1873 N N   . THR B 2 71  ? 24.840  -5.214  -37.931 1.00 91.66  ? 71  THR H N   1 
ATOM   1874 C CA  . THR B 2 71  ? 25.018  -3.891  -37.347 1.00 97.89  ? 71  THR H CA  1 
ATOM   1875 C C   . THR B 2 71  ? 24.283  -2.848  -38.181 1.00 104.22 ? 71  THR H C   1 
ATOM   1876 O O   . THR B 2 71  ? 23.881  -3.097  -39.321 1.00 95.82  ? 71  THR H O   1 
ATOM   1877 C CB  . THR B 2 71  ? 26.497  -3.499  -37.185 1.00 99.80  ? 71  THR H CB  1 
ATOM   1878 O OG1 . THR B 2 71  ? 27.165  -3.592  -38.449 1.00 119.71 ? 71  THR H OG1 1 
ATOM   1879 C CG2 . THR B 2 71  ? 27.197  -4.400  -36.169 1.00 106.05 ? 71  THR H CG2 1 
ATOM   1880 N N   . THR B 2 72  ? 24.106  -1.666  -37.588 1.00 98.90  ? 72  THR H N   1 
ATOM   1881 C CA  . THR B 2 72  ? 23.475  -0.533  -38.255 1.00 83.55  ? 72  THR H CA  1 
ATOM   1882 C C   . THR B 2 72  ? 24.189  0.753   -37.871 1.00 88.22  ? 72  THR H C   1 
ATOM   1883 O O   . THR B 2 72  ? 24.473  0.981   -36.691 1.00 85.92  ? 72  THR H O   1 
ATOM   1884 C CB  . THR B 2 72  ? 21.992  -0.411  -37.888 1.00 91.89  ? 72  THR H CB  1 
ATOM   1885 O OG1 . THR B 2 72  ? 21.827  -0.611  -36.479 1.00 111.56 ? 72  THR H OG1 1 
ATOM   1886 C CG2 . THR B 2 72  ? 21.174  -1.434  -38.646 1.00 106.44 ? 72  THR H CG2 1 
ATOM   1887 N N   . ASP B 2 73  ? 24.457  1.593   -38.866 1.00 94.01  ? 73  ASP H N   1 
ATOM   1888 C CA  . ASP B 2 73  ? 25.012  2.929   -38.665 1.00 91.93  ? 73  ASP H CA  1 
ATOM   1889 C C   . ASP B 2 73  ? 23.911  3.930   -38.997 1.00 97.78  ? 73  ASP H C   1 
ATOM   1890 O O   . ASP B 2 73  ? 23.745  4.331   -40.149 1.00 115.32 ? 73  ASP H O   1 
ATOM   1891 C CB  . ASP B 2 73  ? 26.243  3.157   -39.531 1.00 105.34 ? 73  ASP H CB  1 
ATOM   1892 C CG  . ASP B 2 73  ? 26.969  4.446   -39.186 1.00 110.58 ? 73  ASP H CG  1 
ATOM   1893 O OD1 . ASP B 2 73  ? 26.540  5.147   -38.244 1.00 99.39  ? 73  ASP H OD1 1 
ATOM   1894 O OD2 . ASP B 2 73  ? 27.963  4.764   -39.870 1.00 122.07 ? 73  ASP H OD2 1 
ATOM   1895 N N   . THR B 2 74  ? 23.160  4.336   -37.971 1.00 77.38  ? 74  THR H N   1 
ATOM   1896 C CA  . THR B 2 74  ? 22.066  5.280   -38.174 1.00 90.32  ? 74  THR H CA  1 
ATOM   1897 C C   . THR B 2 74  ? 22.552  6.569   -38.821 1.00 109.85 ? 74  THR H C   1 
ATOM   1898 O O   . THR B 2 74  ? 21.850  7.162   -39.648 1.00 119.71 ? 74  THR H O   1 
ATOM   1899 C CB  . THR B 2 74  ? 21.397  5.589   -36.838 1.00 111.29 ? 74  THR H CB  1 
ATOM   1900 O OG1 . THR B 2 74  ? 22.374  6.128   -35.938 1.00 116.84 ? 74  THR H OG1 1 
ATOM   1901 C CG2 . THR B 2 74  ? 20.814  4.323   -36.241 1.00 115.29 ? 74  THR H CG2 1 
ATOM   1902 N N   . SER B 2 75  ? 23.755  7.016   -38.452 1.00 119.20 ? 75  SER H N   1 
ATOM   1903 C CA  . SER B 2 75  ? 24.286  8.269   -38.980 1.00 122.17 ? 75  SER H CA  1 
ATOM   1904 C C   . SER B 2 75  ? 24.404  8.220   -40.497 1.00 129.03 ? 75  SER H C   1 
ATOM   1905 O O   . SER B 2 75  ? 24.051  9.182   -41.188 1.00 128.67 ? 75  SER H O   1 
ATOM   1906 C CB  . SER B 2 75  ? 25.645  8.564   -38.352 1.00 109.66 ? 75  SER H CB  1 
ATOM   1907 O OG  . SER B 2 75  ? 26.580  7.570   -38.728 1.00 127.03 ? 75  SER H OG  1 
ATOM   1908 N N   . THR B 2 76  ? 24.913  7.113   -41.032 1.00 128.45 ? 76  THR H N   1 
ATOM   1909 C CA  . THR B 2 76  ? 24.974  6.907   -42.472 1.00 117.68 ? 76  THR H CA  1 
ATOM   1910 C C   . THR B 2 76  ? 23.794  6.100   -43.001 1.00 121.44 ? 76  THR H C   1 
ATOM   1911 O O   . THR B 2 76  ? 23.716  5.874   -44.212 1.00 120.66 ? 76  THR H O   1 
ATOM   1912 C CB  . THR B 2 76  ? 26.287  6.213   -42.863 1.00 114.70 ? 76  THR H CB  1 
ATOM   1913 O OG1 . THR B 2 76  ? 26.331  4.899   -42.293 1.00 116.75 ? 76  THR H OG1 1 
ATOM   1914 C CG2 . THR B 2 76  ? 27.491  7.014   -42.375 1.00 124.44 ? 76  THR H CG2 1 
ATOM   1915 N N   . SER B 2 77  ? 22.878  5.676   -42.126 1.00 126.58 ? 77  SER H N   1 
ATOM   1916 C CA  . SER B 2 77  ? 21.705  4.880   -42.500 1.00 118.87 ? 77  SER H CA  1 
ATOM   1917 C C   . SER B 2 77  ? 22.109  3.654   -43.316 1.00 132.62 ? 77  SER H C   1 
ATOM   1918 O O   . SER B 2 77  ? 21.537  3.353   -44.366 1.00 153.10 ? 77  SER H O   1 
ATOM   1919 C CB  . SER B 2 77  ? 20.682  5.728   -43.255 1.00 130.21 ? 77  SER H CB  1 
ATOM   1920 O OG  . SER B 2 77  ? 21.149  6.057   -44.551 1.00 164.14 ? 77  SER H OG  1 
ATOM   1921 N N   . THR B 2 78  ? 23.115  2.939   -42.815 1.00 119.68 ? 78  THR H N   1 
ATOM   1922 C CA  . THR B 2 78  ? 23.683  1.789   -43.503 1.00 106.40 ? 78  THR H CA  1 
ATOM   1923 C C   . THR B 2 78  ? 23.650  0.582   -42.580 1.00 105.59 ? 78  THR H C   1 
ATOM   1924 O O   . THR B 2 78  ? 24.019  0.685   -41.405 1.00 113.49 ? 78  THR H O   1 
ATOM   1925 C CB  . THR B 2 78  ? 25.125  2.061   -43.945 1.00 119.81 ? 78  THR H CB  1 
ATOM   1926 O OG1 . THR B 2 78  ? 25.200  3.346   -44.574 1.00 136.83 ? 78  THR H OG1 1 
ATOM   1927 C CG2 . THR B 2 78  ? 25.586  0.998   -44.931 1.00 131.22 ? 78  THR H CG2 1 
ATOM   1928 N N   . ALA B 2 79  ? 23.214  -0.554  -43.113 1.00 104.52 ? 79  ALA H N   1 
ATOM   1929 C CA  . ALA B 2 79  ? 23.215  -1.820  -42.398 1.00 113.99 ? 79  ALA H CA  1 
ATOM   1930 C C   . ALA B 2 79  ? 24.369  -2.693  -42.879 1.00 122.84 ? 79  ALA H C   1 
ATOM   1931 O O   . ALA B 2 79  ? 24.897  -2.517  -43.981 1.00 134.60 ? 79  ALA H O   1 
ATOM   1932 C CB  . ALA B 2 79  ? 21.884  -2.552  -42.587 1.00 114.11 ? 79  ALA H CB  1 
ATOM   1933 N N   . TYR B 2 80  ? 24.759  -3.645  -42.034 1.00 97.66  ? 80  TYR H N   1 
ATOM   1934 C CA  . TYR B 2 80  ? 25.911  -4.491  -42.312 1.00 92.06  ? 80  TYR H CA  1 
ATOM   1935 C C   . TYR B 2 80  ? 25.619  -5.906  -41.847 1.00 103.06 ? 80  TYR H C   1 
ATOM   1936 O O   . TYR B 2 80  ? 25.114  -6.105  -40.740 1.00 103.56 ? 80  TYR H O   1 
ATOM   1937 C CB  . TYR B 2 80  ? 27.171  -3.961  -41.615 1.00 109.75 ? 80  TYR H CB  1 
ATOM   1938 C CG  . TYR B 2 80  ? 27.513  -2.526  -41.953 1.00 105.89 ? 80  TYR H CG  1 
ATOM   1939 C CD1 . TYR B 2 80  ? 28.030  -2.182  -43.196 1.00 125.41 ? 80  TYR H CD1 1 
ATOM   1940 C CD2 . TYR B 2 80  ? 27.304  -1.511  -41.029 1.00 94.53  ? 80  TYR H CD2 1 
ATOM   1941 C CE1 . TYR B 2 80  ? 28.339  -0.865  -43.503 1.00 128.76 ? 80  TYR H CE1 1 
ATOM   1942 C CE2 . TYR B 2 80  ? 27.607  -0.195  -41.328 1.00 104.43 ? 80  TYR H CE2 1 
ATOM   1943 C CZ  . TYR B 2 80  ? 28.124  0.124   -42.565 1.00 123.12 ? 80  TYR H CZ  1 
ATOM   1944 O OH  . TYR B 2 80  ? 28.425  1.437   -42.859 1.00 135.13 ? 80  TYR H OH  1 
ATOM   1945 N N   . MET B 2 81  ? 25.980  -6.878  -42.688 1.00 110.03 ? 81  MET H N   1 
ATOM   1946 C CA  . MET B 2 81  ? 25.828  -8.310  -42.333 1.00 101.35 ? 81  MET H CA  1 
ATOM   1947 C C   . MET B 2 81  ? 27.221  -8.927  -42.365 1.00 116.94 ? 81  MET H C   1 
ATOM   1948 O O   . MET B 2 81  ? 27.923  -8.716  -43.368 1.00 134.77 ? 81  MET H O   1 
ATOM   1949 C CB  . MET B 2 81  ? 24.981  -9.036  -43.374 1.00 83.73  ? 81  MET H CB  1 
ATOM   1950 C CG  . MET B 2 81  ? 24.729  -10.474 -43.037 1.00 109.82 ? 81  MET H CG  1 
ATOM   1951 S SD  . MET B 2 81  ? 23.713  -10.640 -41.564 0.57 114.47 ? 81  MET H SD  1 
ATOM   1952 C CE  . MET B 2 81  ? 22.122  -10.193 -42.254 1.00 112.31 ? 81  MET H CE  1 
ATOM   1953 N N   . GLU B 2 82  ? 27.611  -9.652  -41.322 1.00 108.24 ? 82  GLU H N   1 
ATOM   1954 C CA  . GLU B 2 82  ? 28.995  -10.185 -41.287 1.00 120.56 ? 82  GLU H CA  1 
ATOM   1955 C C   . GLU B 2 82  ? 28.945  -11.675 -40.951 1.00 135.74 ? 82  GLU H C   1 
ATOM   1956 O O   . GLU B 2 82  ? 28.509  -12.010 -39.837 1.00 147.64 ? 82  GLU H O   1 
ATOM   1957 C CB  . GLU B 2 82  ? 29.829  -9.411  -40.268 1.00 136.51 ? 82  GLU H CB  1 
ATOM   1958 C CG  . GLU B 2 82  ? 29.984  -7.941  -40.612 1.00 148.35 ? 82  GLU H CG  1 
ATOM   1959 C CD  . GLU B 2 82  ? 30.008  -7.001  -39.418 1.00 154.71 ? 82  GLU H CD  1 
ATOM   1960 O OE1 . GLU B 2 82  ? 29.875  -7.490  -38.279 1.00 152.11 ? 82  GLU H OE1 1 
ATOM   1961 O OE2 . GLU B 2 82  ? 30.160  -5.782  -39.631 1.00 143.45 ? 82  GLU H OE2 1 
ATOM   1962 N N   . LEU B 2 83  ? 29.385  -12.537 -41.873 1.00 147.11 ? 83  LEU H N   1 
ATOM   1963 C CA  . LEU B 2 83  ? 29.450  -13.994 -41.576 1.00 142.34 ? 83  LEU H CA  1 
ATOM   1964 C C   . LEU B 2 83  ? 30.884  -14.331 -41.153 1.00 133.16 ? 83  LEU H C   1 
ATOM   1965 O O   . LEU B 2 83  ? 31.758  -14.384 -42.040 1.00 121.69 ? 83  LEU H O   1 
ATOM   1966 C CB  . LEU B 2 83  ? 29.026  -14.781 -42.819 1.00 115.07 ? 83  LEU H CB  1 
ATOM   1967 C CG  . LEU B 2 83  ? 28.735  -16.264 -42.594 1.00 130.52 ? 83  LEU H CG  1 
ATOM   1968 C CD1 . LEU B 2 83  ? 27.493  -16.442 -41.736 1.00 133.79 ? 83  LEU H CD1 1 
ATOM   1969 C CD2 . LEU B 2 83  ? 28.561  -16.984 -43.921 1.00 138.89 ? 83  LEU H CD2 1 
ATOM   1970 N N   . ARG B 2 84  ? 31.112  -14.547 -39.854 1.00 125.53 ? 84  ARG H N   1 
ATOM   1971 C CA  . ARG B 2 84  ? 32.489  -14.792 -39.343 1.00 133.51 ? 84  ARG H CA  1 
ATOM   1972 C C   . ARG B 2 84  ? 33.112  -16.007 -40.038 1.00 145.22 ? 84  ARG H C   1 
ATOM   1973 O O   . ARG B 2 84  ? 34.248  -15.879 -40.535 1.00 153.95 ? 84  ARG H O   1 
ATOM   1974 C CB  . ARG B 2 84  ? 32.449  -15.006 -37.828 1.00 145.53 ? 84  ARG H CB  1 
ATOM   1975 C CG  . ARG B 2 84  ? 32.099  -13.758 -37.031 1.00 138.23 ? 84  ARG H CG  1 
ATOM   1976 C CD  . ARG B 2 84  ? 31.408  -14.111 -35.729 1.00 133.04 ? 84  ARG H CD  1 
ATOM   1977 N NE  . ARG B 2 84  ? 32.001  -15.278 -35.093 1.00 128.53 ? 84  ARG H NE  1 
ATOM   1978 C CZ  . ARG B 2 84  ? 31.566  -15.820 -33.962 1.00 145.63 ? 84  ARG H CZ  1 
ATOM   1979 N NH1 . ARG B 2 84  ? 30.558  -15.268 -33.311 1.00 152.30 ? 84  ARG H NH1 1 
ATOM   1980 N NH2 . ARG B 2 84  ? 32.138  -16.913 -33.488 1.00 157.81 ? 84  ARG H NH2 1 
ATOM   1981 N N   . SER B 2 85  ? 32.402  -17.139 -40.065 1.00 123.73 ? 85  SER H N   1 
ATOM   1982 C CA  . SER B 2 85  ? 32.969  -18.378 -40.660 1.00 120.60 ? 85  SER H CA  1 
ATOM   1983 C C   . SER B 2 85  ? 32.363  -18.614 -42.046 1.00 135.31 ? 85  SER H C   1 
ATOM   1984 O O   . SER B 2 85  ? 31.127  -18.529 -42.172 1.00 157.43 ? 85  SER H O   1 
ATOM   1985 C CB  . SER B 2 85  ? 32.750  -19.563 -39.756 1.00 150.66 ? 85  SER H CB  1 
ATOM   1986 O OG  . SER B 2 85  ? 33.168  -20.762 -40.391 1.00 173.53 ? 85  SER H OG  1 
ATOM   1987 N N   . LEU B 2 86  ? 33.206  -18.903 -43.042 1.00 133.89 ? 86  LEU H N   1 
ATOM   1988 C CA  . LEU B 2 86  ? 32.704  -19.090 -44.430 1.00 135.48 ? 86  LEU H CA  1 
ATOM   1989 C C   . LEU B 2 86  ? 32.759  -20.569 -44.819 1.00 150.87 ? 86  LEU H C   1 
ATOM   1990 O O   . LEU B 2 86  ? 33.625  -21.289 -44.285 1.00 156.45 ? 86  LEU H O   1 
ATOM   1991 C CB  . LEU B 2 86  ? 33.525  -18.222 -45.389 1.00 122.41 ? 86  LEU H CB  1 
ATOM   1992 C CG  . LEU B 2 86  ? 32.950  -16.827 -45.634 1.00 109.92 ? 86  LEU H CG  1 
ATOM   1993 C CD1 . LEU B 2 86  ? 33.698  -16.113 -46.748 1.00 106.69 ? 86  LEU H CD1 1 
ATOM   1994 C CD2 . LEU B 2 86  ? 31.463  -16.895 -45.938 1.00 137.78 ? 86  LEU H CD2 1 
ATOM   1995 N N   . ARG B 2 87  ? 31.869  -20.994 -45.718 1.00 142.54 ? 87  ARG H N   1 
ATOM   1996 C CA  . ARG B 2 87  ? 31.794  -22.383 -46.143 1.00 132.47 ? 87  ARG H CA  1 
ATOM   1997 C C   . ARG B 2 87  ? 31.576  -22.349 -47.648 1.00 137.41 ? 87  ARG H C   1 
ATOM   1998 O O   . ARG B 2 87  ? 30.997  -21.405 -48.193 1.00 146.40 ? 87  ARG H O   1 
ATOM   1999 C CB  . ARG B 2 87  ? 30.716  -23.267 -45.507 1.00 119.17 ? 87  ARG H CB  1 
ATOM   2000 C CG  . ARG B 2 87  ? 31.030  -23.784 -44.124 1.00 137.25 ? 87  ARG H CG  1 
ATOM   2001 C CD  . ARG B 2 87  ? 29.913  -24.706 -43.677 1.00 150.43 ? 87  ARG H CD  1 
ATOM   2002 N NE  . ARG B 2 87  ? 30.180  -25.322 -42.384 1.00 191.45 ? 87  ARG H NE  1 
ATOM   2003 C CZ  . ARG B 2 87  ? 29.353  -26.159 -41.773 1.00 212.17 ? 87  ARG H CZ  1 
ATOM   2004 N NH1 . ARG B 2 87  ? 28.202  -26.516 -42.319 1.00 210.48 ? 87  ARG H NH1 1 
ATOM   2005 N NH2 . ARG B 2 87  ? 29.691  -26.653 -40.585 1.00 222.46 ? 87  ARG H NH2 1 
ATOM   2006 N N   . SER B 2 88  ? 32.039  -23.409 -48.317 1.00 136.57 ? 88  SER H N   1 
ATOM   2007 C CA  . SER B 2 88  ? 31.730  -23.576 -49.733 1.00 140.26 ? 88  SER H CA  1 
ATOM   2008 C C   . SER B 2 88  ? 30.224  -23.641 -49.956 1.00 140.89 ? 88  SER H C   1 
ATOM   2009 O O   . SER B 2 88  ? 29.713  -23.133 -50.962 1.00 146.58 ? 88  SER H O   1 
ATOM   2010 C CB  . SER B 2 88  ? 32.409  -24.833 -50.280 1.00 140.67 ? 88  SER H CB  1 
ATOM   2011 O OG  . SER B 2 88  ? 33.819  -24.758 -50.147 1.00 147.07 ? 88  SER H OG  1 
ATOM   2012 N N   . ASP B 2 89  ? 29.496  -24.253 -49.018 1.00 131.23 ? 89  ASP H N   1 
ATOM   2013 C CA  . ASP B 2 89  ? 28.041  -24.284 -49.106 1.00 132.33 ? 89  ASP H CA  1 
ATOM   2014 C C   . ASP B 2 89  ? 27.442  -22.892 -48.974 1.00 123.74 ? 89  ASP H C   1 
ATOM   2015 O O   . ASP B 2 89  ? 26.374  -22.621 -49.534 1.00 99.02  ? 89  ASP H O   1 
ATOM   2016 C CB  . ASP B 2 89  ? 27.476  -25.202 -48.026 1.00 106.92 ? 89  ASP H CB  1 
ATOM   2017 C CG  . ASP B 2 89  ? 27.756  -26.657 -48.305 1.00 124.39 ? 89  ASP H CG  1 
ATOM   2018 O OD1 . ASP B 2 89  ? 28.128  -26.974 -49.454 1.00 138.90 ? 89  ASP H OD1 1 
ATOM   2019 O OD2 . ASP B 2 89  ? 27.613  -27.480 -47.378 1.00 135.62 ? 89  ASP H OD2 1 
ATOM   2020 N N   . ASP B 2 90  ? 28.113  -21.999 -48.241 1.00 136.93 ? 90  ASP H N   1 
ATOM   2021 C CA  . ASP B 2 90  ? 27.601  -20.648 -48.045 1.00 130.05 ? 90  ASP H CA  1 
ATOM   2022 C C   . ASP B 2 90  ? 27.680  -19.800 -49.306 1.00 129.35 ? 90  ASP H C   1 
ATOM   2023 O O   . ASP B 2 90  ? 27.013  -18.761 -49.377 1.00 138.84 ? 90  ASP H O   1 
ATOM   2024 C CB  . ASP B 2 90  ? 28.356  -19.943 -46.916 1.00 123.30 ? 90  ASP H CB  1 
ATOM   2025 C CG  . ASP B 2 90  ? 28.288  -20.698 -45.606 1.00 131.03 ? 90  ASP H CG  1 
ATOM   2026 O OD1 . ASP B 2 90  ? 27.632  -21.759 -45.566 1.00 144.17 ? 90  ASP H OD1 1 
ATOM   2027 O OD2 . ASP B 2 90  ? 28.883  -20.224 -44.614 1.00 119.33 ? 90  ASP H OD2 1 
ATOM   2028 N N   . THR B 2 91  ? 28.489  -20.205 -50.286 1.00 112.54 ? 91  THR H N   1 
ATOM   2029 C CA  . THR B 2 91  ? 28.620  -19.491 -51.551 1.00 120.79 ? 91  THR H CA  1 
ATOM   2030 C C   . THR B 2 91  ? 27.265  -19.222 -52.192 1.00 115.69 ? 91  THR H C   1 
ATOM   2031 O O   . THR B 2 91  ? 26.592  -20.163 -52.631 1.00 123.95 ? 91  THR H O   1 
ATOM   2032 C CB  . THR B 2 91  ? 29.494  -20.291 -52.516 1.00 126.49 ? 91  THR H CB  1 
ATOM   2033 O OG1 . THR B 2 91  ? 30.796  -20.495 -51.947 1.00 129.52 ? 91  THR H OG1 1 
ATOM   2034 C CG2 . THR B 2 91  ? 29.623  -19.577 -53.847 1.00 121.85 ? 91  THR H CG2 1 
ATOM   2035 N N   . ALA B 2 92  ? 26.866  -17.953 -52.268 1.00 107.90 ? 92  ALA H N   1 
ATOM   2036 C CA  . ALA B 2 92  ? 25.547  -17.573 -52.768 1.00 110.99 ? 92  ALA H CA  1 
ATOM   2037 C C   . ALA B 2 92  ? 25.583  -16.055 -52.935 1.00 112.54 ? 92  ALA H C   1 
ATOM   2038 O O   . ALA B 2 92  ? 26.611  -15.408 -52.713 1.00 118.92 ? 92  ALA H O   1 
ATOM   2039 C CB  . ALA B 2 92  ? 24.445  -18.045 -51.821 1.00 115.69 ? 92  ALA H CB  1 
ATOM   2040 N N   . VAL B 2 93  ? 24.439  -15.490 -53.326 1.00 99.63  ? 93  VAL H N   1 
ATOM   2041 C CA  . VAL B 2 93  ? 24.258  -14.042 -53.424 1.00 116.91 ? 93  VAL H CA  1 
ATOM   2042 C C   . VAL B 2 93  ? 23.354  -13.627 -52.273 1.00 132.19 ? 93  VAL H C   1 
ATOM   2043 O O   . VAL B 2 93  ? 22.441  -14.369 -51.887 1.00 140.10 ? 93  VAL H O   1 
ATOM   2044 C CB  . VAL B 2 93  ? 23.690  -13.622 -54.797 1.00 124.70 ? 93  VAL H CB  1 
ATOM   2045 C CG1 . VAL B 2 93  ? 22.311  -14.216 -55.035 1.00 142.99 ? 93  VAL H CG1 1 
ATOM   2046 C CG2 . VAL B 2 93  ? 23.663  -12.099 -54.938 1.00 110.17 ? 93  VAL H CG2 1 
ATOM   2047 N N   . PHE B 2 94  ? 23.625  -12.458 -51.699 1.00 128.01 ? 94  PHE H N   1 
ATOM   2048 C CA  . PHE B 2 94  ? 22.891  -11.946 -50.550 1.00 110.39 ? 94  PHE H CA  1 
ATOM   2049 C C   . PHE B 2 94  ? 22.048  -10.743 -50.959 1.00 115.45 ? 94  PHE H C   1 
ATOM   2050 O O   . PHE B 2 94  ? 22.439  -9.973  -51.842 1.00 132.84 ? 94  PHE H O   1 
ATOM   2051 C CB  . PHE B 2 94  ? 23.915  -11.546 -49.476 1.00 114.08 ? 94  PHE H CB  1 
ATOM   2052 C CG  . PHE B 2 94  ? 24.738  -12.701 -48.942 1.00 118.02 ? 94  PHE H CG  1 
ATOM   2053 C CD1 . PHE B 2 94  ? 24.439  -14.014 -49.277 1.00 135.34 ? 94  PHE H CD1 1 
ATOM   2054 C CD2 . PHE B 2 94  ? 25.832  -12.464 -48.125 1.00 126.40 ? 94  PHE H CD2 1 
ATOM   2055 C CE1 . PHE B 2 94  ? 25.201  -15.065 -48.794 1.00 134.11 ? 94  PHE H CE1 1 
ATOM   2056 C CE2 . PHE B 2 94  ? 26.597  -13.512 -47.639 1.00 135.11 ? 94  PHE H CE2 1 
ATOM   2057 C CZ  . PHE B 2 94  ? 26.281  -14.813 -47.975 1.00 132.30 ? 94  PHE H CZ  1 
ATOM   2058 N N   . TYR B 2 95  ? 20.885  -10.592 -50.322 1.00 103.40 ? 95  TYR H N   1 
ATOM   2059 C CA  . TYR B 2 95  ? 19.928  -9.546  -50.663 1.00 117.17 ? 95  TYR H CA  1 
ATOM   2060 C C   . TYR B 2 95  ? 19.490  -8.808  -49.404 1.00 120.45 ? 95  TYR H C   1 
ATOM   2061 O O   . TYR B 2 95  ? 19.440  -9.383  -48.313 1.00 120.22 ? 95  TYR H O   1 
ATOM   2062 C CB  . TYR B 2 95  ? 18.695  -10.129 -51.382 1.00 108.55 ? 95  TYR H CB  1 
ATOM   2063 C CG  . TYR B 2 95  ? 18.796  -10.138 -52.895 1.00 113.99 ? 95  TYR H CG  1 
ATOM   2064 C CD1 . TYR B 2 95  ? 18.814  -8.953  -53.621 1.00 109.71 ? 95  TYR H CD1 1 
ATOM   2065 C CD2 . TYR B 2 95  ? 18.883  -11.335 -53.597 1.00 134.78 ? 95  TYR H CD2 1 
ATOM   2066 C CE1 . TYR B 2 95  ? 18.908  -8.961  -55.005 1.00 118.34 ? 95  TYR H CE1 1 
ATOM   2067 C CE2 . TYR B 2 95  ? 18.980  -11.352 -54.977 1.00 126.12 ? 95  TYR H CE2 1 
ATOM   2068 C CZ  . TYR B 2 95  ? 18.993  -10.164 -55.676 1.00 123.34 ? 95  TYR H CZ  1 
ATOM   2069 O OH  . TYR B 2 95  ? 19.090  -10.178 -57.049 1.00 122.54 ? 95  TYR H OH  1 
ATOM   2070 N N   . CYS B 2 96  ? 19.171  -7.525  -49.568 1.00 116.49 ? 96  CYS H N   1 
ATOM   2071 C CA  . CYS B 2 96  ? 18.673  -6.680  -48.491 1.00 90.91  ? 96  CYS H CA  1 
ATOM   2072 C C   . CYS B 2 96  ? 17.232  -6.268  -48.739 1.00 101.02 ? 96  CYS H C   1 
ATOM   2073 O O   . CYS B 2 96  ? 16.755  -6.220  -49.876 1.00 116.90 ? 96  CYS H O   1 
ATOM   2074 C CB  . CYS B 2 96  ? 19.522  -5.421  -48.321 1.00 111.32 ? 96  CYS H CB  1 
ATOM   2075 S SG  . CYS B 2 96  ? 21.082  -5.750  -47.546 1.00 193.55 ? 96  CYS H SG  1 
ATOM   2076 N N   . ALA B 2 97  ? 16.551  -5.939  -47.640 1.00 63.54  ? 97  ALA H N   1 
ATOM   2077 C CA  . ALA B 2 97  ? 15.139  -5.523  -47.741 1.00 114.75 ? 97  ALA H CA  1 
ATOM   2078 C C   . ALA B 2 97  ? 14.815  -4.716  -46.486 1.00 65.88  ? 97  ALA H C   1 
ATOM   2079 O O   . ALA B 2 97  ? 15.363  -5.039  -45.422 1.00 195.30 ? 97  ALA H O   1 
ATOM   2080 C CB  . ALA B 2 97  ? 14.270  -6.740  -47.847 1.00 78.83  ? 97  ALA H CB  1 
ATOM   2081 N N   . ARG B 2 98  ? 13.954  -3.709  -46.618 1.00 100.52 ? 98  ARG H N   1 
ATOM   2082 C CA  . ARG B 2 98  ? 13.542  -2.907  -45.440 1.00 91.65  ? 98  ARG H CA  1 
ATOM   2083 C C   . ARG B 2 98  ? 12.618  -3.764  -44.586 1.00 104.01 ? 98  ARG H C   1 
ATOM   2084 O O   . ARG B 2 98  ? 12.049  -4.718  -45.128 1.00 124.77 ? 98  ARG H O   1 
ATOM   2085 C CB  . ARG B 2 98  ? 12.810  -1.637  -45.870 1.00 100.50 ? 98  ARG H CB  1 
ATOM   2086 C CG  . ARG B 2 98  ? 12.360  -0.768  -44.707 1.00 162.17 ? 98  ARG H CG  1 
ATOM   2087 C CD  . ARG B 2 98  ? 11.594  0.460   -45.161 1.00 205.57 ? 98  ARG H CD  1 
ATOM   2088 N NE  . ARG B 2 98  ? 12.457  1.379   -45.889 1.00 233.42 ? 98  ARG H NE  1 
ATOM   2089 C CZ  . ARG B 2 98  ? 12.041  2.499   -46.468 1.00 235.45 ? 98  ARG H CZ  1 
ATOM   2090 N NH1 . ARG B 2 98  ? 11.028  2.468   -47.316 1.00 254.56 ? 98  ARG H NH1 1 
ATOM   2091 N NH2 . ARG B 2 98  ? 12.647  3.643   -46.206 1.00 229.06 ? 98  ARG H NH2 1 
ATOM   2092 N N   . ASP B 2 99  ? 12.504  -3.439  -43.302 1.00 104.76 ? 99  ASP H N   1 
ATOM   2093 C CA  . ASP B 2 99  ? 11.586  -4.177  -42.402 1.00 105.55 ? 99  ASP H CA  1 
ATOM   2094 C C   . ASP B 2 99  ? 11.061  -3.167  -41.390 1.00 113.74 ? 99  ASP H C   1 
ATOM   2095 O O   . ASP B 2 99  ? 11.704  -2.121  -41.223 1.00 131.40 ? 99  ASP H O   1 
ATOM   2096 C CB  . ASP B 2 99  ? 12.335  -5.299  -41.687 1.00 106.17 ? 99  ASP H CB  1 
ATOM   2097 C CG  . ASP B 2 99  ? 11.442  -6.477  -41.353 1.00 125.66 ? 99  ASP H CG  1 
ATOM   2098 O OD1 . ASP B 2 99  ? 10.264  -6.430  -41.741 1.00 138.18 ? 99  ASP H OD1 1 
ATOM   2099 O OD2 . ASP B 2 99  ? 11.929  -7.425  -40.710 1.00 123.01 ? 99  ASP H OD2 1 
ATOM   2100 N N   . ARG B 2 100 ? 9.939   -3.460  -40.743 1.00 120.56 ? 100 ARG H N   1 
ATOM   2101 C CA  . ARG B 2 100 ? 9.492   -2.520  -39.717 1.00 125.06 ? 100 ARG H CA  1 
ATOM   2102 C C   . ARG B 2 100 ? 10.302  -2.690  -38.435 1.00 122.84 ? 100 ARG H C   1 
ATOM   2103 O O   . ARG B 2 100 ? 10.636  -3.815  -38.047 1.00 109.73 ? 100 ARG H O   1 
ATOM   2104 C CB  . ARG B 2 100 ? 8.001   -2.680  -39.412 1.00 139.55 ? 100 ARG H CB  1 
ATOM   2105 C CG  . ARG B 2 100 ? 7.145   -2.374  -40.611 1.00 128.13 ? 100 ARG H CG  1 
ATOM   2106 C CD  . ARG B 2 100 ? 5.657   -2.449  -40.346 1.00 127.50 ? 100 ARG H CD  1 
ATOM   2107 N NE  . ARG B 2 100 ? 4.916   -2.352  -41.597 1.00 144.93 ? 100 ARG H NE  1 
ATOM   2108 C CZ  . ARG B 2 100 ? 3.603   -2.495  -41.704 1.00 133.10 ? 100 ARG H CZ  1 
ATOM   2109 N NH1 . ARG B 2 100 ? 2.846   -2.726  -40.644 1.00 129.43 ? 100 ARG H NH1 1 
ATOM   2110 N NH2 . ARG B 2 100 ? 3.037   -2.398  -42.901 1.00 129.41 ? 100 ARG H NH2 1 
ATOM   2111 N N   . PRO B 2 101 ? 10.650  -1.608  -37.699 1.00 113.49 ? 101 PRO H N   1 
ATOM   2112 C CA  . PRO B 2 101 ? 11.510  -1.754  -36.521 1.00 96.32  ? 101 PRO H CA  1 
ATOM   2113 C C   . PRO B 2 101 ? 10.814  -2.345  -35.288 1.00 100.76 ? 101 PRO H C   1 
ATOM   2114 O O   . PRO B 2 101 ? 11.372  -3.234  -34.686 1.00 95.64  ? 101 PRO H O   1 
ATOM   2115 C CB  . PRO B 2 101 ? 11.913  -0.311  -36.201 1.00 108.56 ? 101 PRO H CB  1 
ATOM   2116 C CG  . PRO B 2 101 ? 10.772  0.531   -36.714 1.00 104.07 ? 101 PRO H CG  1 
ATOM   2117 C CD  . PRO B 2 101 ? 10.276  -0.204  -37.939 1.00 113.78 ? 101 PRO H CD  1 
ATOM   2118 N N   . HIS B 2 102 ? 9.633   -1.840  -34.937 1.00 114.18 ? 102 HIS H N   1 
ATOM   2119 C CA  . HIS B 2 102 ? 8.946   -2.293  -33.700 1.00 88.31  ? 102 HIS H CA  1 
ATOM   2120 C C   . HIS B 2 102 ? 8.503   -3.747  -33.853 1.00 105.34 ? 102 HIS H C   1 
ATOM   2121 O O   . HIS B 2 102 ? 7.825   -4.065  -34.847 1.00 117.76 ? 102 HIS H O   1 
ATOM   2122 C CB  . HIS B 2 102 ? 7.733   -1.406  -33.422 1.00 87.69  ? 102 HIS H CB  1 
ATOM   2123 C CG  . HIS B 2 102 ? 8.056   0.036   -33.229 1.00 132.55 ? 102 HIS H CG  1 
ATOM   2124 N ND1 . HIS B 2 102 ? 8.741   0.486   -32.121 1.00 168.86 ? 102 HIS H ND1 1 
ATOM   2125 C CD2 . HIS B 2 102 ? 7.771   1.125   -33.954 1.00 148.41 ? 102 HIS H CD2 1 
ATOM   2126 C CE1 . HIS B 2 102 ? 8.876   1.802   -32.195 1.00 187.66 ? 102 HIS H CE1 1 
ATOM   2127 N NE2 . HIS B 2 102 ? 8.295   2.211   -33.302 1.00 176.68 ? 102 HIS H NE2 1 
ATOM   2128 N N   . ILE B 2 103 ? 8.858   -4.598  -32.891 1.00 105.78 ? 103 ILE H N   1 
ATOM   2129 C CA  . ILE B 2 103 ? 8.396   -6.016  -32.917 1.00 96.68  ? 103 ILE H CA  1 
ATOM   2130 C C   . ILE B 2 103 ? 6.872   -6.005  -32.821 1.00 98.23  ? 103 ILE H C   1 
ATOM   2131 O O   . ILE B 2 103 ? 6.232   -6.836  -33.484 1.00 115.81 ? 103 ILE H O   1 
ATOM   2132 C CB  . ILE B 2 103 ? 9.022   -6.811  -31.757 1.00 83.86  ? 103 ILE H CB  1 
ATOM   2133 C CG1 . ILE B 2 103 ? 10.525  -6.550  -31.644 1.00 117.88 ? 103 ILE H CG1 1 
ATOM   2134 C CG2 . ILE B 2 103 ? 8.712   -8.294  -31.886 1.00 78.00  ? 103 ILE H CG2 1 
ATOM   2135 C CD1 . ILE B 2 103 ? 11.169  -7.199  -30.444 1.00 135.04 ? 103 ILE H CD1 1 
ATOM   2136 N N   . LEU B 2 104 ? 6.323   -5.106  -32.003 1.00 91.01  ? 104 LEU H N   1 
ATOM   2137 C CA  . LEU B 2 104 ? 4.850   -4.982  -31.887 1.00 86.58  ? 104 LEU H CA  1 
ATOM   2138 C C   . LEU B 2 104 ? 4.285   -4.840  -33.298 1.00 116.05 ? 104 LEU H C   1 
ATOM   2139 O O   . LEU B 2 104 ? 3.350   -5.578  -33.632 1.00 151.62 ? 104 LEU H O   1 
ATOM   2140 C CB  . LEU B 2 104 ? 4.521   -3.751  -31.045 1.00 86.91  ? 104 LEU H CB  1 
ATOM   2141 C CG  . LEU B 2 104 ? 5.127   -3.733  -29.644 1.00 95.39  ? 104 LEU H CG  1 
ATOM   2142 C CD1 . LEU B 2 104 ? 4.584   -2.565  -28.838 1.00 132.95 ? 104 LEU H CD1 1 
ATOM   2143 C CD2 . LEU B 2 104 ? 4.859   -5.044  -28.924 1.00 100.12 ? 104 LEU H CD2 1 
ATOM   2144 N N   . THR B 2 105 ? 4.873   -3.963  -34.120 1.00 121.77 ? 105 THR H N   1 
ATOM   2145 C CA  . THR B 2 105 ? 4.406   -3.779  -35.523 1.00 132.97 ? 105 THR H CA  1 
ATOM   2146 C C   . THR B 2 105 ? 4.799   -4.995  -36.372 1.00 135.62 ? 105 THR H C   1 
ATOM   2147 O O   . THR B 2 105 ? 5.656   -5.775  -35.923 1.00 130.89 ? 105 THR H O   1 
ATOM   2148 C CB  . THR B 2 105 ? 4.950   -2.481  -36.131 1.00 123.40 ? 105 THR H CB  1 
ATOM   2149 O OG1 . THR B 2 105 ? 6.362   -2.615  -36.292 1.00 136.48 ? 105 THR H OG1 1 
ATOM   2150 C CG2 . THR B 2 105 ? 4.638   -1.262  -35.290 1.00 113.84 ? 105 THR H CG2 1 
ATOM   2151 N N   . GLY B 2 106 ? 4.196   -5.141  -37.556 1.00 139.67 ? 106 GLY H N   1 
ATOM   2152 C CA  . GLY B 2 106 ? 4.484   -6.299  -38.426 1.00 140.32 ? 106 GLY H CA  1 
ATOM   2153 C C   . GLY B 2 106 ? 5.782   -6.128  -39.197 1.00 129.56 ? 106 GLY H C   1 
ATOM   2154 O O   . GLY B 2 106 ? 6.754   -5.608  -38.614 1.00 126.69 ? 106 GLY H O   1 
ATOM   2155 N N   . PHE B 2 107 ? 5.803   -6.555  -40.463 1.00 121.02 ? 107 PHE H N   1 
ATOM   2156 C CA  . PHE B 2 107 ? 7.042   -6.465  -41.282 1.00 107.12 ? 107 PHE H CA  1 
ATOM   2157 C C   . PHE B 2 107 ? 6.709   -5.893  -42.665 1.00 106.16 ? 107 PHE H C   1 
ATOM   2158 O O   . PHE B 2 107 ? 5.581   -6.116  -43.148 1.00 130.69 ? 107 PHE H O   1 
ATOM   2159 C CB  . PHE B 2 107 ? 7.741   -7.828  -41.349 1.00 127.23 ? 107 PHE H CB  1 
ATOM   2160 C CG  . PHE B 2 107 ? 6.872   -9.022  -41.655 1.00 155.15 ? 107 PHE H CG  1 
ATOM   2161 C CD1 . PHE B 2 107 ? 6.193   -9.126  -42.858 1.00 140.91 ? 107 PHE H CD1 1 
ATOM   2162 C CD2 . PHE B 2 107 ? 6.754   -10.059 -40.743 1.00 153.00 ? 107 PHE H CD2 1 
ATOM   2163 C CE1 . PHE B 2 107 ? 5.403   -10.231 -43.135 1.00 117.76 ? 107 PHE H CE1 1 
ATOM   2164 C CE2 . PHE B 2 107 ? 5.966   -11.164 -41.021 1.00 126.52 ? 107 PHE H CE2 1 
ATOM   2165 C CZ  . PHE B 2 107 ? 5.294   -11.248 -42.217 1.00 104.92 ? 107 PHE H CZ  1 
ATOM   2166 N N   . ASP B 2 108 ? 7.654   -5.164  -43.272 1.00 104.32 ? 108 ASP H N   1 
ATOM   2167 C CA  . ASP B 2 108 ? 7.430   -4.632  -44.645 1.00 117.87 ? 108 ASP H CA  1 
ATOM   2168 C C   . ASP B 2 108 ? 8.745   -4.622  -45.436 1.00 125.49 ? 108 ASP H C   1 
ATOM   2169 O O   . ASP B 2 108 ? 9.524   -3.668  -45.283 1.00 128.35 ? 108 ASP H O   1 
ATOM   2170 C CB  . ASP B 2 108 ? 6.729   -3.266  -44.630 1.00 118.80 ? 108 ASP H CB  1 
ATOM   2171 C CG  . ASP B 2 108 ? 7.436   -2.175  -43.843 1.00 123.40 ? 108 ASP H CG  1 
ATOM   2172 O OD1 . ASP B 2 108 ? 8.485   -2.464  -43.235 1.00 110.32 ? 108 ASP H OD1 1 
ATOM   2173 O OD2 . ASP B 2 108 ? 6.929   -1.036  -43.846 1.00 125.91 ? 108 ASP H OD2 1 
ATOM   2174 N N   . PHE B 2 109 ? 8.940   -5.646  -46.270 1.00 123.61 ? 109 PHE H N   1 
ATOM   2175 C CA  . PHE B 2 109 ? 10.140  -5.708  -47.139 1.00 114.85 ? 109 PHE H CA  1 
ATOM   2176 C C   . PHE B 2 109 ? 9.616   -4.942  -48.350 1.00 104.91 ? 109 PHE H C   1 
ATOM   2177 O O   . PHE B 2 109 ? 9.495   -5.539  -49.430 1.00 108.40 ? 109 PHE H O   1 
ATOM   2178 C CB  . PHE B 2 109 ? 10.428  -7.167  -47.493 1.00 117.62 ? 109 PHE H CB  1 
ATOM   2179 C CG  . PHE B 2 109 ? 10.978  -7.987  -46.353 1.00 127.04 ? 109 PHE H CG  1 
ATOM   2180 C CD1 . PHE B 2 109 ? 10.334  -8.026  -45.127 1.00 141.07 ? 109 PHE H CD1 1 
ATOM   2181 C CD2 . PHE B 2 109 ? 12.130  -8.738  -46.509 1.00 131.44 ? 109 PHE H CD2 1 
ATOM   2182 C CE1 . PHE B 2 109 ? 10.842  -8.775  -44.079 1.00 144.49 ? 109 PHE H CE1 1 
ATOM   2183 C CE2 . PHE B 2 109 ? 12.638  -9.490  -45.461 1.00 127.76 ? 109 PHE H CE2 1 
ATOM   2184 C CZ  . PHE B 2 109 ? 11.994  -9.506  -44.248 1.00 135.09 ? 109 PHE H CZ  1 
ATOM   2185 N N   . ASP B 2 110 ? 9.353   -3.641  -48.176 1.00 117.28 ? 110 ASP H N   1 
ATOM   2186 C CA  . ASP B 2 110 ? 8.824   -2.804  -49.288 1.00 138.96 ? 110 ASP H CA  1 
ATOM   2187 C C   . ASP B 2 110 ? 9.922   -2.612  -50.335 1.00 143.92 ? 110 ASP H C   1 
ATOM   2188 O O   . ASP B 2 110 ? 9.643   -2.826  -51.531 1.00 147.25 ? 110 ASP H O   1 
ATOM   2189 C CB  . ASP B 2 110 ? 8.271   -1.469  -48.780 1.00 138.44 ? 110 ASP H CB  1 
ATOM   2190 C CG  . ASP B 2 110 ? 9.220   -0.721  -47.860 1.00 148.75 ? 110 ASP H CG  1 
ATOM   2191 O OD1 . ASP B 2 110 ? 9.539   -1.263  -46.786 1.00 142.46 ? 110 ASP H OD1 1 
ATOM   2192 O OD2 . ASP B 2 110 ? 9.633   0.396   -48.227 1.00 152.91 ? 110 ASP H OD2 1 
ATOM   2193 N N   . TYR B 2 111 ? 11.121  -2.228  -49.893 1.00 130.79 ? 111 TYR H N   1 
ATOM   2194 C CA  . TYR B 2 111 ? 12.238  -1.976  -50.838 1.00 132.47 ? 111 TYR H CA  1 
ATOM   2195 C C   . TYR B 2 111 ? 13.221  -3.147  -50.766 1.00 117.67 ? 111 TYR H C   1 
ATOM   2196 O O   . TYR B 2 111 ? 13.492  -3.621  -49.648 1.00 125.12 ? 111 TYR H O   1 
ATOM   2197 C CB  . TYR B 2 111 ? 12.926  -0.649  -50.510 1.00 148.58 ? 111 TYR H CB  1 
ATOM   2198 C CG  . TYR B 2 111 ? 12.078  0.578   -50.728 1.00 161.71 ? 111 TYR H CG  1 
ATOM   2199 C CD1 . TYR B 2 111 ? 10.789  0.477   -51.224 1.00 166.58 ? 111 TYR H CD1 1 
ATOM   2200 C CD2 . TYR B 2 111 ? 12.561  1.843   -50.440 1.00 166.90 ? 111 TYR H CD2 1 
ATOM   2201 C CE1 . TYR B 2 111 ? 9.998   1.595   -51.422 1.00 179.46 ? 111 TYR H CE1 1 
ATOM   2202 C CE2 . TYR B 2 111 ? 11.787  2.974   -50.638 1.00 161.16 ? 111 TYR H CE2 1 
ATOM   2203 C CZ  . TYR B 2 111 ? 10.501  2.850   -51.131 1.00 176.77 ? 111 TYR H CZ  1 
ATOM   2204 O OH  . TYR B 2 111 ? 9.717   3.957   -51.341 1.00 195.14 ? 111 TYR H OH  1 
ATOM   2205 N N   . TRP B 2 112 ? 13.708  -3.613  -51.919 1.00 123.47 ? 112 TRP H N   1 
ATOM   2206 C CA  . TRP B 2 112 ? 14.737  -4.687  -51.924 1.00 113.73 ? 112 TRP H CA  1 
ATOM   2207 C C   . TRP B 2 112 ? 16.043  -4.116  -52.483 1.00 111.81 ? 112 TRP H C   1 
ATOM   2208 O O   . TRP B 2 112 ? 15.988  -3.044  -53.118 1.00 113.67 ? 112 TRP H O   1 
ATOM   2209 C CB  . TRP B 2 112 ? 14.261  -5.917  -52.707 1.00 114.52 ? 112 TRP H CB  1 
ATOM   2210 C CG  . TRP B 2 112 ? 13.331  -6.788  -51.921 1.00 112.77 ? 112 TRP H CG  1 
ATOM   2211 C CD1 . TRP B 2 112 ? 12.071  -6.479  -51.499 1.00 122.24 ? 112 TRP H CD1 1 
ATOM   2212 C CD2 . TRP B 2 112 ? 13.608  -8.108  -51.420 1.00 109.11 ? 112 TRP H CD2 1 
ATOM   2213 N NE1 . TRP B 2 112 ? 11.537  -7.522  -50.791 1.00 124.43 ? 112 TRP H NE1 1 
ATOM   2214 C CE2 . TRP B 2 112 ? 12.457  -8.535  -50.725 1.00 118.97 ? 112 TRP H CE2 1 
ATOM   2215 C CE3 . TRP B 2 112 ? 14.707  -8.971  -51.498 1.00 118.74 ? 112 TRP H CE3 1 
ATOM   2216 C CZ2 . TRP B 2 112 ? 12.378  -9.785  -50.114 1.00 140.24 ? 112 TRP H CZ2 1 
ATOM   2217 C CZ3 . TRP B 2 112 ? 14.627  -10.206 -50.896 1.00 107.75 ? 112 TRP H CZ3 1 
ATOM   2218 C CH2 . TRP B 2 112 ? 13.477  -10.606 -50.214 1.00 114.86 ? 112 TRP H CH2 1 
ATOM   2219 N N   . GLY B 2 113 ? 17.168  -4.797  -52.253 1.00 110.41 ? 113 GLY H N   1 
ATOM   2220 C CA  . GLY B 2 113 ? 18.467  -4.233  -52.684 1.00 103.74 ? 113 GLY H CA  1 
ATOM   2221 C C   . GLY B 2 113 ? 19.040  -4.855  -53.950 1.00 107.82 ? 113 GLY H C   1 
ATOM   2222 O O   . GLY B 2 113 ? 18.335  -5.676  -54.570 1.00 103.27 ? 113 GLY H O   1 
ATOM   2223 N N   . GLN B 2 114 ? 20.274  -4.479  -54.323 1.00 107.99 ? 114 GLN H N   1 
ATOM   2224 C CA  . GLN B 2 114 ? 20.957  -5.057  -55.538 1.00 111.40 ? 114 GLN H CA  1 
ATOM   2225 C C   . GLN B 2 114 ? 21.662  -6.237  -54.927 1.00 97.93  ? 114 GLN H C   1 
ATOM   2226 O O   . GLN B 2 114 ? 22.378  -6.054  -53.929 1.00 91.98  ? 114 GLN H O   1 
ATOM   2227 C CB  . GLN B 2 114 ? 21.754  -3.930  -56.235 1.00 118.78 ? 114 GLN H CB  1 
ATOM   2228 C CG  . GLN B 2 114 ? 22.341  -2.908  -55.274 1.00 138.75 ? 114 GLN H CG  1 
ATOM   2229 C CD  . GLN B 2 114 ? 23.305  -1.961  -55.944 1.00 162.44 ? 114 GLN H CD  1 
ATOM   2230 O OE1 . GLN B 2 114 ? 22.944  -1.218  -56.855 1.00 166.98 ? 114 GLN H OE1 1 
ATOM   2231 N NE2 . GLN B 2 114 ? 24.547  -1.978  -55.490 1.00 167.19 ? 114 GLN H NE2 1 
ATOM   2232 N N   . GLY B 2 115 ? 21.543  -7.410  -55.549 1.00 93.21  ? 115 GLY H N   1 
ATOM   2233 C CA  . GLY B 2 115 ? 22.097  -8.700  -54.995 1.00 93.35  ? 115 GLY H CA  1 
ATOM   2234 C C   . GLY B 2 115 ? 23.605  -8.663  -54.966 1.00 88.46  ? 115 GLY H C   1 
ATOM   2235 O O   . GLY B 2 115 ? 24.209  -8.691  -56.055 1.00 102.84 ? 115 GLY H O   1 
ATOM   2236 N N   . THR B 2 116 ? 24.207  -8.641  -53.771 1.00 93.46  ? 116 THR H N   1 
ATOM   2237 C CA  . THR B 2 116 ? 25.687  -8.834  -53.651 1.00 107.14 ? 116 THR H CA  1 
ATOM   2238 C C   . THR B 2 116 ? 25.950  -10.334 -53.614 1.00 112.46 ? 116 THR H C   1 
ATOM   2239 O O   . THR B 2 116 ? 25.651  -10.967 -52.582 1.00 114.10 ? 116 THR H O   1 
ATOM   2240 C CB  . THR B 2 116 ? 26.115  -8.196  -52.315 1.00 103.39 ? 116 THR H CB  1 
ATOM   2241 O OG1 . THR B 2 116 ? 25.842  -6.797  -52.379 1.00 119.09 ? 116 THR H OG1 1 
ATOM   2242 C CG2 . THR B 2 116 ? 27.583  -8.411  -52.019 1.00 101.67 ? 116 THR H CG2 1 
ATOM   2243 N N   . LEU B 2 117 ? 26.488  -10.880 -54.708 1.00 109.11 ? 117 LEU H N   1 
ATOM   2244 C CA  . LEU B 2 117 ? 26.857  -12.305 -54.676 1.00 119.71 ? 117 LEU H CA  1 
ATOM   2245 C C   . LEU B 2 117 ? 28.154  -12.472 -53.917 1.00 119.90 ? 117 LEU H C   1 
ATOM   2246 O O   . LEU B 2 117 ? 29.030  -11.606 -54.006 1.00 131.74 ? 117 LEU H O   1 
ATOM   2247 C CB  . LEU B 2 117 ? 26.982  -12.822 -56.109 1.00 125.14 ? 117 LEU H CB  1 
ATOM   2248 C CG  . LEU B 2 117 ? 28.014  -12.187 -57.042 1.00 163.11 ? 117 LEU H CG  1 
ATOM   2249 C CD1 . LEU B 2 117 ? 29.394  -12.752 -56.761 1.00 158.20 ? 117 LEU H CD1 1 
ATOM   2250 C CD2 . LEU B 2 117 ? 27.645  -12.447 -58.482 1.00 178.46 ? 117 LEU H CD2 1 
ATOM   2251 N N   . VAL B 2 118 ? 28.272  -13.537 -53.127 1.00 88.99  ? 118 VAL H N   1 
ATOM   2252 C CA  . VAL B 2 118 ? 29.487  -13.813 -52.368 1.00 101.71 ? 118 VAL H CA  1 
ATOM   2253 C C   . VAL B 2 118 ? 29.900  -15.233 -52.730 1.00 130.49 ? 118 VAL H C   1 
ATOM   2254 O O   . VAL B 2 118 ? 29.109  -16.173 -52.580 1.00 112.46 ? 118 VAL H O   1 
ATOM   2255 C CB  . VAL B 2 118 ? 29.102  -13.723 -50.883 1.00 86.49  ? 118 VAL H CB  1 
ATOM   2256 C CG1 . VAL B 2 118 ? 30.152  -14.411 -50.027 1.00 105.23 ? 118 VAL H CG1 1 
ATOM   2257 C CG2 . VAL B 2 118 ? 28.943  -12.271 -50.468 1.00 108.02 ? 118 VAL H CG2 1 
ATOM   2258 N N   . THR B 2 119 ? 31.134  -15.391 -53.199 1.00 142.78 ? 119 THR H N   1 
ATOM   2259 C CA  . THR B 2 119 ? 31.680  -16.692 -53.558 1.00 128.36 ? 119 THR H CA  1 
ATOM   2260 C C   . THR B 2 119 ? 32.675  -17.143 -52.498 1.00 131.13 ? 119 THR H C   1 
ATOM   2261 O O   . THR B 2 119 ? 33.516  -16.356 -52.052 1.00 148.32 ? 119 THR H O   1 
ATOM   2262 C CB  . THR B 2 119 ? 32.360  -16.647 -54.929 1.00 134.02 ? 119 THR H CB  1 
ATOM   2263 O OG1 . THR B 2 119 ? 33.429  -15.695 -54.901 1.00 137.72 ? 119 THR H OG1 1 
ATOM   2264 C CG2 . THR B 2 119 ? 31.363  -16.237 -56.001 1.00 148.75 ? 119 THR H CG2 1 
ATOM   2265 N N   . VAL B 2 120 ? 32.577  -18.410 -52.093 1.00 140.45 ? 120 VAL H N   1 
ATOM   2266 C CA  . VAL B 2 120 ? 33.440  -18.936 -51.041 1.00 147.24 ? 120 VAL H CA  1 
ATOM   2267 C C   . VAL B 2 120 ? 34.000  -20.292 -51.453 1.00 151.03 ? 120 VAL H C   1 
ATOM   2268 O O   . VAL B 2 120 ? 33.338  -21.321 -51.286 1.00 144.92 ? 120 VAL H O   1 
ATOM   2269 C CB  . VAL B 2 120 ? 32.683  -19.052 -49.703 1.00 136.26 ? 120 VAL H CB  1 
ATOM   2270 C CG1 . VAL B 2 120 ? 33.580  -19.671 -48.635 1.00 141.07 ? 120 VAL H CG1 1 
ATOM   2271 C CG2 . VAL B 2 120 ? 32.142  -17.705 -49.261 1.00 133.48 ? 120 VAL H CG2 1 
ATOM   2272 N N   . SER B 2 121 ? 35.217  -20.305 -51.994 1.00 162.61 ? 121 SER H N   1 
ATOM   2273 C CA  . SER B 2 121 ? 35.922  -21.552 -52.256 1.00 172.09 ? 121 SER H CA  1 
ATOM   2274 C C   . SER B 2 121 ? 37.417  -21.271 -52.259 1.00 168.82 ? 121 SER H C   1 
ATOM   2275 O O   . SER B 2 121 ? 37.855  -20.126 -52.392 1.00 179.31 ? 121 SER H O   1 
ATOM   2276 C CB  . SER B 2 121 ? 35.489  -22.207 -53.576 1.00 179.82 ? 121 SER H CB  1 
ATOM   2277 O OG  . SER B 2 121 ? 35.836  -21.418 -54.696 1.00 157.03 ? 121 SER H OG  1 
ATOM   2278 N N   . SER B 2 122 ? 38.196  -22.337 -52.113 1.00 147.95 ? 122 SER H N   1 
ATOM   2279 C CA  . SER B 2 122 ? 39.639  -22.224 -51.906 1.00 164.20 ? 122 SER H CA  1 
ATOM   2280 C C   . SER B 2 122 ? 40.114  -22.289 -53.355 1.00 159.29 ? 122 SER H C   1 
ATOM   2281 O O   . SER B 2 122 ? 40.440  -23.356 -53.870 1.00 174.82 ? 122 SER H O   1 
ATOM   2282 C CB  . SER B 2 122 ? 40.122  -23.406 -51.078 1.00 178.86 ? 122 SER H CB  1 
ATOM   2283 O OG  . SER B 2 122 ? 39.919  -24.617 -51.784 1.00 177.16 ? 122 SER H OG  1 
ATOM   2284 N N   . ALA B 2 123 ? 40.170  -21.139 -54.024 1.00 141.82 ? 123 ALA H N   1 
ATOM   2285 C CA  . ALA B 2 123 ? 40.606  -21.068 -55.410 1.00 152.08 ? 123 ALA H CA  1 
ATOM   2286 C C   . ALA B 2 123 ? 40.925  -19.597 -55.621 1.00 157.17 ? 123 ALA H C   1 
ATOM   2287 O O   . ALA B 2 123 ? 40.152  -18.722 -55.221 1.00 163.80 ? 123 ALA H O   1 
ATOM   2288 C CB  . ALA B 2 123 ? 39.723  -21.580 -56.554 1.00 154.17 ? 123 ALA H CB  1 
ATOM   2289 N N   . SER B 2 124 ? 42.065  -19.329 -56.246 1.00 159.72 ? 124 SER H N   1 
ATOM   2290 C CA  . SER B 2 124 ? 42.444  -17.968 -56.583 1.00 160.67 ? 124 SER H CA  1 
ATOM   2291 C C   . SER B 2 124 ? 41.863  -17.578 -57.940 1.00 158.80 ? 124 SER H C   1 
ATOM   2292 O O   . SER B 2 124 ? 41.405  -18.419 -58.717 1.00 162.80 ? 124 SER H O   1 
ATOM   2293 C CB  . SER B 2 124 ? 43.964  -17.821 -56.590 1.00 173.10 ? 124 SER H CB  1 
ATOM   2294 O OG  . SER B 2 124 ? 44.540  -18.627 -57.604 1.00 174.95 ? 124 SER H OG  1 
ATOM   2295 N N   . THR B 2 125 ? 41.888  -16.278 -58.220 1.00 169.38 ? 125 THR H N   1 
ATOM   2296 C CA  . THR B 2 125 ? 41.355  -15.771 -59.477 1.00 173.91 ? 125 THR H CA  1 
ATOM   2297 C C   . THR B 2 125 ? 42.200  -16.267 -60.646 1.00 176.95 ? 125 THR H C   1 
ATOM   2298 O O   . THR B 2 125 ? 43.430  -16.309 -60.569 1.00 183.68 ? 125 THR H O   1 
ATOM   2299 C CB  . THR B 2 125 ? 41.321  -14.240 -59.462 1.00 147.69 ? 125 THR H CB  1 
ATOM   2300 O OG1 . THR B 2 125 ? 42.648  -13.729 -59.286 1.00 128.13 ? 125 THR H OG1 1 
ATOM   2301 C CG2 . THR B 2 125 ? 40.453  -13.739 -58.316 1.00 124.02 ? 125 THR H CG2 1 
ATOM   2302 N N   . LYS B 2 126 ? 41.532  -16.660 -61.730 1.00 162.94 ? 126 LYS H N   1 
ATOM   2303 C CA  . LYS B 2 126 ? 42.219  -17.132 -62.925 1.00 158.67 ? 126 LYS H CA  1 
ATOM   2304 C C   . LYS B 2 126 ? 41.594  -16.505 -64.162 1.00 142.59 ? 126 LYS H C   1 
ATOM   2305 O O   . LYS B 2 126 ? 40.377  -16.317 -64.227 1.00 150.63 ? 126 LYS H O   1 
ATOM   2306 C CB  . LYS B 2 126 ? 42.169  -18.661 -63.044 1.00 160.86 ? 126 LYS H CB  1 
ATOM   2307 C CG  . LYS B 2 126 ? 42.962  -19.395 -61.978 1.00 177.60 ? 126 LYS H CG  1 
ATOM   2308 C CD  . LYS B 2 126 ? 42.851  -20.896 -62.159 1.00 183.18 ? 126 LYS H CD  1 
ATOM   2309 C CE  . LYS B 2 126 ? 43.652  -21.645 -61.112 1.00 191.35 ? 126 LYS H CE  1 
ATOM   2310 N NZ  . LYS B 2 126 ? 43.511  -23.116 -61.285 1.00 191.24 ? 126 LYS H NZ  1 
ATOM   2311 N N   . GLY B 2 127 ? 42.437  -16.187 -65.141 1.00 127.27 ? 127 GLY H N   1 
ATOM   2312 C CA  . GLY B 2 127 ? 41.979  -15.648 -66.398 1.00 145.02 ? 127 GLY H CA  1 
ATOM   2313 C C   . GLY B 2 127 ? 41.342  -16.711 -67.270 1.00 165.34 ? 127 GLY H C   1 
ATOM   2314 O O   . GLY B 2 127 ? 41.795  -17.859 -67.322 1.00 176.09 ? 127 GLY H O   1 
ATOM   2315 N N   . PRO B 2 128 ? 40.273  -16.345 -67.972 1.00 160.44 ? 128 PRO H N   1 
ATOM   2316 C CA  . PRO B 2 128 ? 39.560  -17.326 -68.793 1.00 152.11 ? 128 PRO H CA  1 
ATOM   2317 C C   . PRO B 2 128 ? 40.338  -17.709 -70.040 1.00 154.72 ? 128 PRO H C   1 
ATOM   2318 O O   . PRO B 2 128 ? 41.155  -16.945 -70.560 1.00 157.43 ? 128 PRO H O   1 
ATOM   2319 C CB  . PRO B 2 128 ? 38.261  -16.599 -69.157 1.00 135.64 ? 128 PRO H CB  1 
ATOM   2320 C CG  . PRO B 2 128 ? 38.637  -15.159 -69.123 1.00 131.52 ? 128 PRO H CG  1 
ATOM   2321 C CD  . PRO B 2 128 ? 39.582  -15.048 -67.957 1.00 155.46 ? 128 PRO H CD  1 
ATOM   2322 N N   . SER B 2 129 ? 40.063  -18.912 -70.524 1.00 144.95 ? 129 SER H N   1 
ATOM   2323 C CA  . SER B 2 129 ? 40.685  -19.444 -71.730 1.00 138.58 ? 129 SER H CA  1 
ATOM   2324 C C   . SER B 2 129 ? 39.599  -19.516 -72.800 1.00 152.44 ? 129 SER H C   1 
ATOM   2325 O O   . SER B 2 129 ? 38.810  -20.464 -72.835 1.00 159.10 ? 129 SER H O   1 
ATOM   2326 C CB  . SER B 2 129 ? 41.317  -20.806 -71.459 1.00 143.07 ? 129 SER H CB  1 
ATOM   2327 O OG  . SER B 2 129 ? 40.382  -21.697 -70.876 1.00 162.87 ? 129 SER H OG  1 
ATOM   2328 N N   . VAL B 2 130 ? 39.554  -18.501 -73.658 1.00 145.55 ? 130 VAL H N   1 
ATOM   2329 C CA  . VAL B 2 130 ? 38.543  -18.419 -74.708 1.00 159.12 ? 130 VAL H CA  1 
ATOM   2330 C C   . VAL B 2 130 ? 38.923  -19.355 -75.847 1.00 189.00 ? 130 VAL H C   1 
ATOM   2331 O O   . VAL B 2 130 ? 40.068  -19.350 -76.316 1.00 200.67 ? 130 VAL H O   1 
ATOM   2332 C CB  . VAL B 2 130 ? 38.395  -16.974 -75.206 1.00 130.15 ? 130 VAL H CB  1 
ATOM   2333 C CG1 . VAL B 2 130 ? 37.437  -16.911 -76.377 1.00 133.55 ? 130 VAL H CG1 1 
ATOM   2334 C CG2 . VAL B 2 130 ? 37.904  -16.085 -74.079 1.00 129.61 ? 130 VAL H CG2 1 
ATOM   2335 N N   . PHE B 2 131 ? 37.955  -20.151 -76.309 1.00 173.59 ? 131 PHE H N   1 
ATOM   2336 C CA  . PHE B 2 131 ? 38.181  -21.121 -77.377 1.00 184.13 ? 131 PHE H CA  1 
ATOM   2337 C C   . PHE B 2 131 ? 36.988  -21.108 -78.330 1.00 183.35 ? 131 PHE H C   1 
ATOM   2338 O O   . PHE B 2 131 ? 35.833  -21.133 -77.871 1.00 206.17 ? 131 PHE H O   1 
ATOM   2339 C CB  . PHE B 2 131 ? 38.399  -22.523 -76.804 1.00 194.17 ? 131 PHE H CB  1 
ATOM   2340 C CG  . PHE B 2 131 ? 39.603  -22.634 -75.903 1.00 218.92 ? 131 PHE H CG  1 
ATOM   2341 C CD1 . PHE B 2 131 ? 40.877  -22.359 -76.379 1.00 227.00 ? 131 PHE H CD1 1 
ATOM   2342 C CD2 . PHE B 2 131 ? 39.458  -23.012 -74.578 1.00 210.30 ? 131 PHE H CD2 1 
ATOM   2343 C CE1 . PHE B 2 131 ? 41.984  -22.465 -75.550 1.00 203.67 ? 131 PHE H CE1 1 
ATOM   2344 C CE2 . PHE B 2 131 ? 40.558  -23.126 -73.749 1.00 211.94 ? 131 PHE H CE2 1 
ATOM   2345 C CZ  . PHE B 2 131 ? 41.822  -22.848 -74.233 1.00 210.13 ? 131 PHE H CZ  1 
ATOM   2346 N N   . PRO B 2 132 ? 37.222  -21.082 -79.639 1.00 178.83 ? 132 PRO H N   1 
ATOM   2347 C CA  . PRO B 2 132 ? 36.133  -20.895 -80.599 1.00 166.05 ? 132 PRO H CA  1 
ATOM   2348 C C   . PRO B 2 132 ? 35.506  -22.211 -81.046 1.00 159.29 ? 132 PRO H C   1 
ATOM   2349 O O   . PRO B 2 132 ? 36.011  -23.303 -80.777 1.00 165.27 ? 132 PRO H O   1 
ATOM   2350 C CB  . PRO B 2 132 ? 36.842  -20.210 -81.772 1.00 166.59 ? 132 PRO H CB  1 
ATOM   2351 C CG  . PRO B 2 132 ? 38.200  -20.842 -81.762 1.00 179.26 ? 132 PRO H CG  1 
ATOM   2352 C CD  . PRO B 2 132 ? 38.535  -21.117 -80.306 1.00 191.28 ? 132 PRO H CD  1 
ATOM   2353 N N   . LEU B 2 133 ? 34.385  -22.077 -81.746 1.00 161.79 ? 133 LEU H N   1 
ATOM   2354 C CA  . LEU B 2 133 ? 33.677  -23.198 -82.350 1.00 158.15 ? 133 LEU H CA  1 
ATOM   2355 C C   . LEU B 2 133 ? 33.635  -22.984 -83.859 1.00 145.83 ? 133 LEU H C   1 
ATOM   2356 O O   . LEU B 2 133 ? 34.087  -21.959 -84.373 1.00 144.67 ? 133 LEU H O   1 
ATOM   2357 C CB  . LEU B 2 133 ? 32.271  -23.338 -81.759 1.00 149.40 ? 133 LEU H CB  1 
ATOM   2358 C CG  . LEU B 2 133 ? 32.252  -23.706 -80.270 1.00 139.20 ? 133 LEU H CG  1 
ATOM   2359 C CD1 . LEU B 2 133 ? 30.832  -23.700 -79.714 1.00 137.15 ? 133 LEU H CD1 1 
ATOM   2360 C CD2 . LEU B 2 133 ? 32.978  -25.018 -79.958 1.00 126.52 ? 133 LEU H CD2 1 
ATOM   2361 N N   . ALA B 2 134 ? 33.076  -23.953 -84.577 1.00 129.34 ? 134 ALA H N   1 
ATOM   2362 C CA  . ALA B 2 134 ? 33.117  -23.934 -86.035 1.00 141.32 ? 134 ALA H CA  1 
ATOM   2363 C C   . ALA B 2 134 ? 31.966  -24.781 -86.562 1.00 152.44 ? 134 ALA H C   1 
ATOM   2364 O O   . ALA B 2 134 ? 31.487  -25.688 -85.870 1.00 155.72 ? 134 ALA H O   1 
ATOM   2365 C CB  . ALA B 2 134 ? 34.466  -24.460 -86.564 1.00 150.89 ? 134 ALA H CB  1 
ATOM   2366 N N   . PRO B 2 135 ? 31.500  -24.511 -87.791 1.00 153.69 ? 135 PRO H N   1 
ATOM   2367 C CA  . PRO B 2 135 ? 30.421  -25.317 -88.399 1.00 167.98 ? 135 PRO H CA  1 
ATOM   2368 C C   . PRO B 2 135 ? 30.996  -26.513 -89.150 1.00 192.53 ? 135 PRO H C   1 
ATOM   2369 O O   . PRO B 2 135 ? 31.005  -26.568 -90.389 1.00 212.12 ? 135 PRO H O   1 
ATOM   2370 C CB  . PRO B 2 135 ? 29.753  -24.311 -89.335 1.00 163.16 ? 135 PRO H CB  1 
ATOM   2371 C CG  . PRO B 2 135 ? 30.873  -23.419 -89.757 1.00 154.44 ? 135 PRO H CG  1 
ATOM   2372 C CD  . PRO B 2 135 ? 31.800  -23.306 -88.584 1.00 144.01 ? 135 PRO H CD  1 
ATOM   2373 N N   . SER B 2 136 ? 31.504  -27.490 -88.396 1.00 193.10 ? 136 SER H N   1 
ATOM   2374 C CA  . SER B 2 136 ? 32.222  -28.609 -89.001 1.00 216.15 ? 136 SER H CA  1 
ATOM   2375 C C   . SER B 2 136 ? 31.351  -29.350 -90.007 1.00 217.97 ? 136 SER H C   1 
ATOM   2376 O O   . SER B 2 136 ? 31.692  -29.447 -91.192 1.00 225.91 ? 136 SER H O   1 
ATOM   2377 C CB  . SER B 2 136 ? 32.722  -29.561 -87.915 1.00 230.15 ? 136 SER H CB  1 
ATOM   2378 O OG  . SER B 2 136 ? 33.754  -28.954 -87.157 1.00 250.55 ? 136 SER H OG  1 
ATOM   2379 N N   . SER B 2 137 ? 30.219  -29.878 -89.556 1.00 232.69 ? 137 SER H N   1 
ATOM   2380 C CA  . SER B 2 137 ? 29.277  -30.514 -90.464 1.00 216.79 ? 137 SER H CA  1 
ATOM   2381 C C   . SER B 2 137 ? 28.366  -29.515 -91.149 1.00 214.43 ? 137 SER H C   1 
ATOM   2382 O O   . SER B 2 137 ? 27.318  -29.918 -91.670 1.00 207.03 ? 137 SER H O   1 
ATOM   2383 C CB  . SER B 2 137 ? 28.426  -31.538 -89.715 1.00 204.60 ? 137 SER H CB  1 
ATOM   2384 O OG  . SER B 2 137 ? 27.697  -30.901 -88.682 1.00 181.63 ? 137 SER H OG  1 
ATOM   2385 N N   . LYS B 2 138 ? 28.727  -28.229 -91.127 1.00 211.50 ? 138 LYS H N   1 
ATOM   2386 C CA  . LYS B 2 138 ? 27.911  -27.140 -91.656 1.00 213.10 ? 138 LYS H CA  1 
ATOM   2387 C C   . LYS B 2 138 ? 26.602  -26.982 -90.887 1.00 215.90 ? 138 LYS H C   1 
ATOM   2388 O O   . LYS B 2 138 ? 25.829  -26.060 -91.170 1.00 232.89 ? 138 LYS H O   1 
ATOM   2389 C CB  . LYS B 2 138 ? 27.632  -27.340 -93.150 1.00 215.42 ? 138 LYS H CB  1 
ATOM   2390 C CG  . LYS B 2 138 ? 28.859  -27.208 -94.037 1.00 203.79 ? 138 LYS H CG  1 
ATOM   2391 C CD  . LYS B 2 138 ? 28.512  -27.432 -95.501 1.00 208.34 ? 138 LYS H CD  1 
ATOM   2392 C CE  . LYS B 2 138 ? 29.736  -27.270 -96.388 1.00 225.59 ? 138 LYS H CE  1 
ATOM   2393 N NZ  . LYS B 2 138 ? 29.416  -27.509 -97.822 1.00 224.54 ? 138 LYS H NZ  1 
ATOM   2394 N N   . SER B 2 139 ? 26.351  -27.858 -89.919 1.00 212.94 ? 139 SER H N   1 
ATOM   2395 C CA  . SER B 2 139 ? 25.195  -27.779 -89.004 1.00 197.82 ? 139 SER H CA  1 
ATOM   2396 C C   . SER B 2 139 ? 23.917  -27.775 -89.853 1.00 210.46 ? 139 SER H C   1 
ATOM   2397 O O   . SER B 2 139 ? 23.819  -28.550 -90.817 1.00 235.51 ? 139 SER H O   1 
ATOM   2398 C CB  . SER B 2 139 ? 25.383  -26.592 -88.086 1.00 191.80 ? 139 SER H CB  1 
ATOM   2399 O OG  . SER B 2 139 ? 25.380  -25.374 -88.803 1.00 219.73 ? 139 SER H OG  1 
ATOM   2400 N N   . THR B 2 140 ? 22.916  -26.951 -89.529 1.00 201.98 ? 140 THR H N   1 
ATOM   2401 C CA  . THR B 2 140 ? 21.757  -26.779 -90.409 1.00 200.51 ? 140 THR H CA  1 
ATOM   2402 C C   . THR B 2 140 ? 22.102  -25.688 -91.416 1.00 230.04 ? 140 THR H C   1 
ATOM   2403 O O   . THR B 2 140 ? 21.770  -24.511 -91.252 1.00 234.22 ? 140 THR H O   1 
ATOM   2404 C CB  . THR B 2 140 ? 20.496  -26.433 -89.624 1.00 186.74 ? 140 THR H CB  1 
ATOM   2405 O OG1 . THR B 2 140 ? 20.713  -25.238 -88.865 1.00 217.18 ? 140 THR H OG1 1 
ATOM   2406 C CG2 . THR B 2 140 ? 20.103  -27.573 -88.697 1.00 153.86 ? 140 THR H CG2 1 
ATOM   2407 N N   . SER B 2 141 ? 22.797  -26.102 -92.478 1.00 261.06 ? 141 SER H N   1 
ATOM   2408 C CA  . SER B 2 141 ? 23.222  -25.164 -93.514 1.00 261.44 ? 141 SER H CA  1 
ATOM   2409 C C   . SER B 2 141 ? 22.030  -24.425 -94.110 1.00 250.69 ? 141 SER H C   1 
ATOM   2410 O O   . SER B 2 141 ? 22.050  -23.195 -94.246 1.00 233.19 ? 141 SER H O   1 
ATOM   2411 C CB  . SER B 2 141 ? 23.998  -25.909 -94.601 1.00 277.52 ? 141 SER H CB  1 
ATOM   2412 O OG  . SER B 2 141 ? 23.173  -26.857 -95.258 1.00 286.02 ? 141 SER H OG  1 
ATOM   2413 N N   . GLY B 2 142 ? 20.977  -25.160 -94.466 1.00 272.48 ? 142 GLY H N   1 
ATOM   2414 C CA  . GLY B 2 142 ? 19.757  -24.544 -94.956 1.00 268.69 ? 142 GLY H CA  1 
ATOM   2415 C C   . GLY B 2 142 ? 19.014  -23.720 -93.927 1.00 262.68 ? 142 GLY H C   1 
ATOM   2416 O O   . GLY B 2 142 ? 18.082  -22.996 -94.295 1.00 245.85 ? 142 GLY H O   1 
ATOM   2417 N N   . GLY B 2 143 ? 19.395  -23.818 -92.655 1.00 238.22 ? 143 GLY H N   1 
ATOM   2418 C CA  . GLY B 2 143 ? 18.809  -22.999 -91.614 1.00 234.29 ? 143 GLY H CA  1 
ATOM   2419 C C   . GLY B 2 143 ? 19.770  -21.937 -91.123 1.00 237.06 ? 143 GLY H C   1 
ATOM   2420 O O   . GLY B 2 143 ? 19.846  -20.846 -91.696 1.00 227.15 ? 143 GLY H O   1 
ATOM   2421 N N   . THR B 2 144 ? 20.517  -22.246 -90.063 1.00 227.40 ? 144 THR H N   1 
ATOM   2422 C CA  . THR B 2 144 ? 21.506  -21.327 -89.508 1.00 220.90 ? 144 THR H CA  1 
ATOM   2423 C C   . THR B 2 144 ? 22.736  -22.115 -89.084 1.00 232.15 ? 144 THR H C   1 
ATOM   2424 O O   . THR B 2 144 ? 22.631  -23.040 -88.273 1.00 286.79 ? 144 THR H O   1 
ATOM   2425 C CB  . THR B 2 144 ? 20.940  -20.542 -88.316 1.00 214.00 ? 144 THR H CB  1 
ATOM   2426 O OG1 . THR B 2 144 ? 20.225  -21.429 -87.445 1.00 232.18 ? 144 THR H OG1 1 
ATOM   2427 C CG2 . THR B 2 144 ? 20.013  -19.426 -88.785 1.00 212.86 ? 144 THR H CG2 1 
ATOM   2428 N N   . ALA B 2 145 ? 23.895  -21.755 -89.634 1.00 246.30 ? 145 ALA H N   1 
ATOM   2429 C CA  . ALA B 2 145 ? 25.154  -22.289 -89.134 1.00 242.72 ? 145 ALA H CA  1 
ATOM   2430 C C   . ALA B 2 145 ? 25.449  -21.683 -87.770 1.00 224.22 ? 145 ALA H C   1 
ATOM   2431 O O   . ALA B 2 145 ? 25.320  -20.471 -87.578 1.00 234.15 ? 145 ALA H O   1 
ATOM   2432 C CB  . ALA B 2 145 ? 26.294  -21.988 -90.106 1.00 244.68 ? 145 ALA H CB  1 
ATOM   2433 N N   . ALA B 2 146 ? 25.835  -22.519 -86.816 1.00 211.08 ? 146 ALA H N   1 
ATOM   2434 C CA  . ALA B 2 146 ? 26.012  -22.066 -85.446 1.00 187.65 ? 146 ALA H CA  1 
ATOM   2435 C C   . ALA B 2 146 ? 27.493  -21.949 -85.108 1.00 166.35 ? 146 ALA H C   1 
ATOM   2436 O O   . ALA B 2 146 ? 28.295  -22.819 -85.456 1.00 169.18 ? 146 ALA H O   1 
ATOM   2437 C CB  . ALA B 2 146 ? 25.304  -23.006 -84.469 1.00 178.00 ? 146 ALA H CB  1 
ATOM   2438 N N   . LEU B 2 147 ? 27.845  -20.851 -84.441 1.00 146.53 ? 147 LEU H N   1 
ATOM   2439 C CA  . LEU B 2 147 ? 29.222  -20.509 -84.113 1.00 154.03 ? 147 LEU H CA  1 
ATOM   2440 C C   . LEU B 2 147 ? 29.293  -20.060 -82.664 1.00 160.62 ? 147 LEU H C   1 
ATOM   2441 O O   . LEU B 2 147 ? 28.453  -19.274 -82.218 1.00 170.14 ? 147 LEU H O   1 
ATOM   2442 C CB  . LEU B 2 147 ? 29.739  -19.401 -85.032 1.00 162.84 ? 147 LEU H CB  1 
ATOM   2443 C CG  . LEU B 2 147 ? 29.895  -19.841 -86.479 1.00 175.90 ? 147 LEU H CG  1 
ATOM   2444 C CD1 . LEU B 2 147 ? 30.249  -18.677 -87.358 1.00 184.19 ? 147 LEU H CD1 1 
ATOM   2445 C CD2 . LEU B 2 147 ? 31.007  -20.836 -86.488 1.00 147.45 ? 147 LEU H CD2 1 
ATOM   2446 N N   . GLY B 2 148 ? 30.302  -20.544 -81.934 1.00 143.89 ? 148 GLY H N   1 
ATOM   2447 C CA  . GLY B 2 148 ? 30.390  -20.266 -80.519 1.00 144.59 ? 148 GLY H CA  1 
ATOM   2448 C C   . GLY B 2 148 ? 31.819  -20.084 -80.047 1.00 167.87 ? 148 GLY H C   1 
ATOM   2449 O O   . GLY B 2 148 ? 32.783  -20.394 -80.752 1.00 168.01 ? 148 GLY H O   1 
ATOM   2450 N N   . CYS B 2 149 ? 31.927  -19.555 -78.829 1.00 163.29 ? 149 CYS H N   1 
ATOM   2451 C CA  . CYS B 2 149 ? 33.180  -19.456 -78.096 1.00 162.15 ? 149 CYS H CA  1 
ATOM   2452 C C   . CYS B 2 149 ? 32.975  -19.965 -76.681 1.00 149.21 ? 149 CYS H C   1 
ATOM   2453 O O   . CYS B 2 149 ? 31.905  -19.786 -76.092 1.00 135.21 ? 149 CYS H O   1 
ATOM   2454 C CB  . CYS B 2 149 ? 33.713  -18.026 -78.046 1.00 162.19 ? 149 CYS H CB  1 
ATOM   2455 S SG  . CYS B 2 149 ? 34.206  -17.375 -79.640 1.00 209.01 ? 149 CYS H SG  1 
ATOM   2456 N N   . LEU B 2 150 ? 34.012  -20.589 -76.139 1.00 163.03 ? 150 LEU H N   1 
ATOM   2457 C CA  . LEU B 2 150 ? 33.959  -21.229 -74.832 1.00 146.92 ? 150 LEU H CA  1 
ATOM   2458 C C   . LEU B 2 150 ? 34.881  -20.469 -73.891 1.00 141.29 ? 150 LEU H C   1 
ATOM   2459 O O   . LEU B 2 150 ? 36.102  -20.467 -74.073 1.00 160.97 ? 150 LEU H O   1 
ATOM   2460 C CB  . LEU B 2 150 ? 34.349  -22.701 -74.936 1.00 170.76 ? 150 LEU H CB  1 
ATOM   2461 C CG  . LEU B 2 150 ? 33.519  -23.520 -75.927 1.00 198.11 ? 150 LEU H CG  1 
ATOM   2462 C CD1 . LEU B 2 150 ? 33.959  -24.978 -75.972 1.00 194.39 ? 150 LEU H CD1 1 
ATOM   2463 C CD2 . LEU B 2 150 ? 32.044  -23.415 -75.576 1.00 192.51 ? 150 LEU H CD2 1 
ATOM   2464 N N   . VAL B 2 151 ? 34.294  -19.824 -72.893 1.00 126.80 ? 151 VAL H N   1 
ATOM   2465 C CA  . VAL B 2 151 ? 35.031  -19.045 -71.910 1.00 119.00 ? 151 VAL H CA  1 
ATOM   2466 C C   . VAL B 2 151 ? 35.155  -19.905 -70.660 1.00 124.32 ? 151 VAL H C   1 
ATOM   2467 O O   . VAL B 2 151 ? 34.179  -20.093 -69.926 1.00 132.57 ? 151 VAL H O   1 
ATOM   2468 C CB  . VAL B 2 151 ? 34.330  -17.711 -71.621 1.00 124.18 ? 151 VAL H CB  1 
ATOM   2469 C CG1 . VAL B 2 151 ? 35.036  -16.974 -70.506 1.00 139.09 ? 151 VAL H CG1 1 
ATOM   2470 C CG2 . VAL B 2 151 ? 34.251  -16.866 -72.883 1.00 121.92 ? 151 VAL H CG2 1 
ATOM   2471 N N   . LYS B 2 152 ? 36.348  -20.442 -70.413 1.00 123.61 ? 152 LYS H N   1 
ATOM   2472 C CA  . LYS B 2 152 ? 36.529  -21.495 -69.424 1.00 120.28 ? 152 LYS H CA  1 
ATOM   2473 C C   . LYS B 2 152 ? 37.728  -21.200 -68.534 1.00 128.61 ? 152 LYS H C   1 
ATOM   2474 O O   . LYS B 2 152 ? 38.504  -20.275 -68.783 1.00 143.98 ? 152 LYS H O   1 
ATOM   2475 C CB  . LYS B 2 152 ? 36.712  -22.848 -70.115 1.00 138.68 ? 152 LYS H CB  1 
ATOM   2476 C CG  . LYS B 2 152 ? 35.475  -23.285 -70.850 1.00 158.74 ? 152 LYS H CG  1 
ATOM   2477 C CD  . LYS B 2 152 ? 35.680  -24.593 -71.559 1.00 203.19 ? 152 LYS H CD  1 
ATOM   2478 C CE  . LYS B 2 152 ? 34.402  -24.988 -72.259 1.00 195.63 ? 152 LYS H CE  1 
ATOM   2479 N NZ  . LYS B 2 152 ? 34.557  -26.251 -73.003 1.00 212.63 ? 152 LYS H NZ  1 
ATOM   2480 N N   . ASP B 2 153 ? 37.866  -22.013 -67.485 1.00 139.89 ? 153 ASP H N   1 
ATOM   2481 C CA  . ASP B 2 153 ? 39.017  -21.991 -66.580 1.00 169.94 ? 153 ASP H CA  1 
ATOM   2482 C C   . ASP B 2 153 ? 39.233  -20.600 -65.979 1.00 170.16 ? 153 ASP H C   1 
ATOM   2483 O O   . ASP B 2 153 ? 40.255  -19.945 -66.190 1.00 166.92 ? 153 ASP H O   1 
ATOM   2484 C CB  . ASP B 2 153 ? 40.277  -22.491 -67.293 1.00 173.21 ? 153 ASP H CB  1 
ATOM   2485 C CG  . ASP B 2 153 ? 40.234  -23.983 -67.589 1.00 175.32 ? 153 ASP H CG  1 
ATOM   2486 O OD1 . ASP B 2 153 ? 39.372  -24.682 -67.015 1.00 178.29 ? 153 ASP H OD1 1 
ATOM   2487 O OD2 . ASP B 2 153 ? 41.065  -24.458 -68.392 1.00 168.46 ? 153 ASP H OD2 1 
ATOM   2488 N N   . TYR B 2 154 ? 38.241  -20.161 -65.208 1.00 152.29 ? 154 TYR H N   1 
ATOM   2489 C CA  . TYR B 2 154 ? 38.284  -18.863 -64.551 1.00 149.22 ? 154 TYR H CA  1 
ATOM   2490 C C   . TYR B 2 154 ? 37.488  -18.961 -63.259 1.00 162.21 ? 154 TYR H C   1 
ATOM   2491 O O   . TYR B 2 154 ? 36.491  -19.683 -63.189 1.00 165.46 ? 154 TYR H O   1 
ATOM   2492 C CB  . TYR B 2 154 ? 37.729  -17.758 -65.459 1.00 148.84 ? 154 TYR H CB  1 
ATOM   2493 C CG  . TYR B 2 154 ? 36.253  -17.892 -65.748 1.00 154.57 ? 154 TYR H CG  1 
ATOM   2494 C CD1 . TYR B 2 154 ? 35.791  -18.728 -66.759 1.00 147.43 ? 154 TYR H CD1 1 
ATOM   2495 C CD2 . TYR B 2 154 ? 35.319  -17.196 -64.998 1.00 162.90 ? 154 TYR H CD2 1 
ATOM   2496 C CE1 . TYR B 2 154 ? 34.439  -18.850 -67.018 1.00 137.39 ? 154 TYR H CE1 1 
ATOM   2497 C CE2 . TYR B 2 154 ? 33.973  -17.316 -65.245 1.00 152.90 ? 154 TYR H CE2 1 
ATOM   2498 C CZ  . TYR B 2 154 ? 33.537  -18.135 -66.258 1.00 140.24 ? 154 TYR H CZ  1 
ATOM   2499 O OH  . TYR B 2 154 ? 32.189  -18.247 -66.485 1.00 145.51 ? 154 TYR H OH  1 
ATOM   2500 N N   . PHE B 2 155 ? 37.926  -18.224 -62.235 1.00 162.95 ? 155 PHE H N   1 
ATOM   2501 C CA  . PHE B 2 155 ? 37.366  -18.475 -60.910 1.00 169.42 ? 155 PHE H CA  1 
ATOM   2502 C C   . PHE B 2 155 ? 36.296  -17.481 -60.455 1.00 168.71 ? 155 PHE H C   1 
ATOM   2503 O O   . PHE B 2 155 ? 35.337  -17.895 -59.795 1.00 169.10 ? 155 PHE H O   1 
ATOM   2504 C CB  . PHE B 2 155 ? 38.474  -18.532 -59.858 1.00 169.71 ? 155 PHE H CB  1 
ATOM   2505 C CG  . PHE B 2 155 ? 37.953  -18.485 -58.461 1.00 169.80 ? 155 PHE H CG  1 
ATOM   2506 C CD1 . PHE B 2 155 ? 37.163  -19.511 -57.973 1.00 171.16 ? 155 PHE H CD1 1 
ATOM   2507 C CD2 . PHE B 2 155 ? 38.212  -17.401 -57.649 1.00 162.93 ? 155 PHE H CD2 1 
ATOM   2508 C CE1 . PHE B 2 155 ? 36.659  -19.461 -56.698 1.00 155.03 ? 155 PHE H CE1 1 
ATOM   2509 C CE2 . PHE B 2 155 ? 37.714  -17.350 -56.369 1.00 164.66 ? 155 PHE H CE2 1 
ATOM   2510 C CZ  . PHE B 2 155 ? 36.936  -18.382 -55.890 1.00 148.53 ? 155 PHE H CZ  1 
ATOM   2511 N N   . PRO B 2 156 ? 36.415  -16.182 -60.707 1.00 161.03 ? 156 PRO H N   1 
ATOM   2512 C CA  . PRO B 2 156 ? 35.300  -15.294 -60.365 1.00 149.18 ? 156 PRO H CA  1 
ATOM   2513 C C   . PRO B 2 156 ? 34.182  -15.365 -61.395 1.00 157.45 ? 156 PRO H C   1 
ATOM   2514 O O   . PRO B 2 156 ? 34.412  -15.557 -62.590 1.00 173.53 ? 156 PRO H O   1 
ATOM   2515 C CB  . PRO B 2 156 ? 35.948  -13.909 -60.346 1.00 140.11 ? 156 PRO H CB  1 
ATOM   2516 C CG  . PRO B 2 156 ? 37.373  -14.174 -60.055 1.00 155.58 ? 156 PRO H CG  1 
ATOM   2517 C CD  . PRO B 2 156 ? 37.667  -15.416 -60.844 1.00 151.44 ? 156 PRO H CD  1 
ATOM   2518 N N   . GLU B 2 157 ? 32.953  -15.192 -60.908 1.00 140.58 ? 157 GLU H N   1 
ATOM   2519 C CA  . GLU B 2 157 ? 31.738  -15.369 -61.703 1.00 148.98 ? 157 GLU H CA  1 
ATOM   2520 C C   . GLU B 2 157 ? 31.482  -14.297 -62.767 1.00 162.39 ? 157 GLU H C   1 
ATOM   2521 O O   . GLU B 2 157 ? 31.072  -14.649 -63.882 1.00 180.61 ? 157 GLU H O   1 
ATOM   2522 C CB  . GLU B 2 157 ? 30.525  -15.457 -60.774 1.00 162.00 ? 157 GLU H CB  1 
ATOM   2523 C CG  . GLU B 2 157 ? 30.497  -16.713 -59.926 1.00 180.04 ? 157 GLU H CG  1 
ATOM   2524 C CD  . GLU B 2 157 ? 29.320  -16.752 -58.974 1.00 214.36 ? 157 GLU H CD  1 
ATOM   2525 O OE1 . GLU B 2 157 ? 28.630  -15.720 -58.833 1.00 215.55 ? 157 GLU H OE1 1 
ATOM   2526 O OE2 . GLU B 2 157 ? 29.086  -17.818 -58.367 1.00 219.25 ? 157 GLU H OE2 1 
ATOM   2527 N N   . PRO B 2 158 ? 31.671  -13.003 -62.485 1.00 144.82 ? 158 PRO H N   1 
ATOM   2528 C CA  . PRO B 2 158 ? 31.282  -11.973 -63.467 1.00 150.61 ? 158 PRO H CA  1 
ATOM   2529 C C   . PRO B 2 158 ? 32.100  -12.059 -64.750 1.00 170.06 ? 158 PRO H C   1 
ATOM   2530 O O   . PRO B 2 158 ? 33.326  -11.941 -64.724 1.00 177.85 ? 158 PRO H O   1 
ATOM   2531 C CB  . PRO B 2 158 ? 31.548  -10.659 -62.720 1.00 170.13 ? 158 PRO H CB  1 
ATOM   2532 C CG  . PRO B 2 158 ? 31.486  -11.030 -61.277 1.00 174.14 ? 158 PRO H CG  1 
ATOM   2533 C CD  . PRO B 2 158 ? 32.121  -12.381 -61.225 1.00 156.69 ? 158 PRO H CD  1 
ATOM   2534 N N   . VAL B 2 159 ? 31.411  -12.248 -65.878 1.00 170.87 ? 159 VAL H N   1 
ATOM   2535 C CA  . VAL B 2 159 ? 32.024  -12.235 -67.207 1.00 172.88 ? 159 VAL H CA  1 
ATOM   2536 C C   . VAL B 2 159 ? 31.088  -11.506 -68.164 1.00 161.11 ? 159 VAL H C   1 
ATOM   2537 O O   . VAL B 2 159 ? 29.864  -11.656 -68.085 1.00 153.23 ? 159 VAL H O   1 
ATOM   2538 C CB  . VAL B 2 159 ? 32.325  -13.660 -67.726 1.00 158.59 ? 159 VAL H CB  1 
ATOM   2539 C CG1 . VAL B 2 159 ? 32.833  -13.624 -69.167 1.00 159.24 ? 159 VAL H CG1 1 
ATOM   2540 C CG2 . VAL B 2 159 ? 33.339  -14.356 -66.843 1.00 169.65 ? 159 VAL H CG2 1 
ATOM   2541 N N   . THR B 2 160 ? 31.662  -10.712 -69.070 1.00 160.50 ? 160 THR H N   1 
ATOM   2542 C CA  . THR B 2 160 ? 30.899  -9.966  -70.064 1.00 159.69 ? 160 THR H CA  1 
ATOM   2543 C C   . THR B 2 160 ? 31.411  -10.313 -71.455 1.00 173.60 ? 160 THR H C   1 
ATOM   2544 O O   . THR B 2 160 ? 32.598  -10.130 -71.749 1.00 176.48 ? 160 THR H O   1 
ATOM   2545 C CB  . THR B 2 160 ? 30.992  -8.460  -69.813 1.00 160.10 ? 160 THR H CB  1 
ATOM   2546 O OG1 . THR B 2 160 ? 32.365  -8.047  -69.833 1.00 160.27 ? 160 THR H OG1 1 
ATOM   2547 C CG2 . THR B 2 160 ? 30.373  -8.116  -68.470 1.00 174.06 ? 160 THR H CG2 1 
ATOM   2548 N N   . VAL B 2 161 ? 30.519  -10.843 -72.301 1.00 165.52 ? 161 VAL H N   1 
ATOM   2549 C CA  . VAL B 2 161 ? 30.936  -11.294 -73.661 1.00 154.55 ? 161 VAL H CA  1 
ATOM   2550 C C   . VAL B 2 161 ? 30.370  -10.340 -74.711 1.00 160.28 ? 161 VAL H C   1 
ATOM   2551 O O   . VAL B 2 161 ? 29.139  -10.156 -74.733 1.00 144.22 ? 161 VAL H O   1 
ATOM   2552 C CB  . VAL B 2 161 ? 30.464  -12.732 -73.940 1.00 136.65 ? 161 VAL H CB  1 
ATOM   2553 C CG1 . VAL B 2 161 ? 30.762  -13.155 -75.370 1.00 125.48 ? 161 VAL H CG1 1 
ATOM   2554 C CG2 . VAL B 2 161 ? 31.057  -13.722 -72.951 1.00 164.04 ? 161 VAL H CG2 1 
ATOM   2555 N N   . SER B 2 162 ? 31.239  -9.771  -75.550 1.00 180.63 ? 162 SER H N   1 
ATOM   2556 C CA  . SER B 2 162 ? 30.777  -8.879  -76.643 1.00 174.26 ? 162 SER H CA  1 
ATOM   2557 C C   . SER B 2 162 ? 30.938  -9.618  -77.970 1.00 170.44 ? 162 SER H C   1 
ATOM   2558 O O   . SER B 2 162 ? 32.059  -10.058 -78.268 1.00 170.34 ? 162 SER H O   1 
ATOM   2559 C CB  . SER B 2 162 ? 31.543  -7.588  -76.653 1.00 180.03 ? 162 SER H CB  1 
ATOM   2560 O OG  . SER B 2 162 ? 31.449  -6.937  -75.396 1.00 183.90 ? 162 SER H OG  1 
ATOM   2561 N N   . TRP B 2 163 ? 29.850  -9.759  -78.722 1.00 182.93 ? 163 TRP H N   1 
ATOM   2562 C CA  . TRP B 2 163 ? 29.923  -10.521 -79.993 1.00 199.85 ? 163 TRP H CA  1 
ATOM   2563 C C   . TRP B 2 163 ? 30.148  -9.547  -81.151 1.00 201.20 ? 163 TRP H C   1 
ATOM   2564 O O   . TRP B 2 163 ? 29.277  -8.684  -81.371 1.00 199.47 ? 163 TRP H O   1 
ATOM   2565 C CB  . TRP B 2 163 ? 28.659  -11.367 -80.172 1.00 203.74 ? 163 TRP H CB  1 
ATOM   2566 C CG  . TRP B 2 163 ? 28.831  -12.798 -79.765 1.00 199.11 ? 163 TRP H CG  1 
ATOM   2567 C CD1 . TRP B 2 163 ? 28.459  -13.364 -78.581 1.00 175.94 ? 163 TRP H CD1 1 
ATOM   2568 C CD2 . TRP B 2 163 ? 29.394  -13.860 -80.555 1.00 202.43 ? 163 TRP H CD2 1 
ATOM   2569 N NE1 . TRP B 2 163 ? 28.759  -14.699 -78.575 1.00 178.74 ? 163 TRP H NE1 1 
ATOM   2570 C CE2 . TRP B 2 163 ? 29.334  -15.033 -79.772 1.00 187.92 ? 163 TRP H CE2 1 
ATOM   2571 C CE3 . TRP B 2 163 ? 29.946  -13.936 -81.838 1.00 212.25 ? 163 TRP H CE3 1 
ATOM   2572 C CZ2 . TRP B 2 163 ? 29.800  -16.261 -80.235 1.00 185.07 ? 163 TRP H CZ2 1 
ATOM   2573 C CZ3 . TRP B 2 163 ? 30.406  -15.151 -82.295 1.00 208.29 ? 163 TRP H CZ3 1 
ATOM   2574 C CH2 . TRP B 2 163 ? 30.332  -16.297 -81.503 1.00 192.33 ? 163 TRP H CH2 1 
ATOM   2575 N N   . ASN B 2 164 ? 31.286  -9.675  -81.840 1.00 193.00 ? 164 ASN H N   1 
ATOM   2576 C CA  . ASN B 2 164 ? 31.587  -8.788  -82.992 1.00 200.54 ? 164 ASN H CA  1 
ATOM   2577 C C   . ASN B 2 164 ? 31.460  -7.333  -82.542 1.00 213.77 ? 164 ASN H C   1 
ATOM   2578 O O   . ASN B 2 164 ? 30.520  -6.662  -82.999 1.00 228.66 ? 164 ASN H O   1 
ATOM   2579 C CB  . ASN B 2 164 ? 30.671  -9.093  -84.177 1.00 211.07 ? 164 ASN H CB  1 
ATOM   2580 C CG  . ASN B 2 164 ? 31.096  -10.340 -84.917 1.00 206.81 ? 164 ASN H CG  1 
ATOM   2581 O OD1 . ASN B 2 164 ? 30.386  -11.342 -84.916 1.00 207.20 ? 164 ASN H OD1 1 
ATOM   2582 N ND2 . ASN B 2 164 ? 32.267  -10.292 -85.529 1.00 210.56 ? 164 ASN H ND2 1 
ATOM   2583 N N   . SER B 2 165 ? 32.356  -6.881  -81.662 1.00 199.98 ? 165 SER H N   1 
ATOM   2584 C CA  . SER B 2 165 ? 32.297  -5.494  -81.129 1.00 202.09 ? 165 SER H CA  1 
ATOM   2585 C C   . SER B 2 165 ? 30.927  -5.250  -80.490 1.00 206.02 ? 165 SER H C   1 
ATOM   2586 O O   . SER B 2 165 ? 30.460  -4.098  -80.521 1.00 221.17 ? 165 SER H O   1 
ATOM   2587 C CB  . SER B 2 165 ? 32.601  -4.473  -82.196 1.00 196.32 ? 165 SER H CB  1 
ATOM   2588 O OG  . SER B 2 165 ? 31.519  -4.347  -83.106 1.00 215.05 ? 165 SER H OG  1 
ATOM   2589 N N   . GLY B 2 166 ? 30.348  -6.295  -79.892 1.00 200.12 ? 166 GLY H N   1 
ATOM   2590 C CA  . GLY B 2 166 ? 29.031  -6.168  -79.242 1.00 189.35 ? 166 GLY H CA  1 
ATOM   2591 C C   . GLY B 2 166 ? 27.968  -5.865  -80.276 1.00 191.34 ? 166 GLY H C   1 
ATOM   2592 O O   . GLY B 2 166 ? 26.775  -5.968  -79.945 1.00 179.85 ? 166 GLY H O   1 
ATOM   2593 N N   . ALA B 2 167 ? 28.395  -5.492  -81.483 1.00 197.81 ? 167 ALA H N   1 
ATOM   2594 C CA  . ALA B 2 167 ? 27.429  -5.107  -82.535 1.00 189.62 ? 167 ALA H CA  1 
ATOM   2595 C C   . ALA B 2 167 ? 26.472  -6.271  -82.791 1.00 199.15 ? 167 ALA H C   1 
ATOM   2596 O O   . ALA B 2 167 ? 25.266  -6.019  -82.961 1.00 199.87 ? 167 ALA H O   1 
ATOM   2597 C CB  . ALA B 2 167 ? 28.162  -4.716  -83.791 1.00 179.68 ? 167 ALA H CB  1 
ATOM   2598 N N   . LEU B 2 168 ? 26.997  -7.496  -82.803 1.00 210.80 ? 168 LEU H N   1 
ATOM   2599 C CA  . LEU B 2 168 ? 26.100  -8.666  -82.975 1.00 211.98 ? 168 LEU H CA  1 
ATOM   2600 C C   . LEU B 2 168 ? 24.978  -8.546  -81.942 1.00 208.96 ? 168 LEU H C   1 
ATOM   2601 O O   . LEU B 2 168 ? 25.295  -8.495  -80.738 1.00 231.76 ? 168 LEU H O   1 
ATOM   2602 C CB  . LEU B 2 168 ? 26.907  -9.952  -82.791 1.00 209.78 ? 168 LEU H CB  1 
ATOM   2603 C CG  . LEU B 2 168 ? 26.195  -11.237 -83.210 1.00 216.62 ? 168 LEU H CG  1 
ATOM   2604 C CD1 . LEU B 2 168 ? 25.322  -10.994 -84.433 1.00 218.61 ? 168 LEU H CD1 1 
ATOM   2605 C CD2 . LEU B 2 168 ? 27.204  -12.336 -83.497 1.00 216.44 ? 168 LEU H CD2 1 
ATOM   2606 N N   . THR B 2 169 ? 23.722  -8.546  -82.396 1.00 216.54 ? 169 THR H N   1 
ATOM   2607 C CA  . THR B 2 169 ? 22.563  -8.443  -81.469 1.00 200.03 ? 169 THR H CA  1 
ATOM   2608 C C   . THR B 2 169 ? 21.622  -9.630  -81.239 1.00 203.50 ? 169 THR H C   1 
ATOM   2609 O O   . THR B 2 169 ? 21.329  -9.923  -80.063 1.00 198.37 ? 169 THR H O   1 
ATOM   2610 C CB  . THR B 2 169 ? 21.575  -7.366  -81.937 1.00 173.67 ? 169 THR H CB  1 
ATOM   2611 O OG1 . THR B 2 169 ? 21.210  -7.659  -83.286 1.00 169.27 ? 169 THR H OG1 1 
ATOM   2612 C CG2 . THR B 2 169 ? 22.145  -5.967  -81.854 1.00 159.86 ? 169 THR H CG2 1 
ATOM   2613 N N   . SER B 2 170 ? 21.174  -10.285 -82.315 1.00 216.92 ? 170 SER H N   1 
ATOM   2614 C CA  . SER B 2 170 ? 20.193  -11.398 -82.190 1.00 210.21 ? 170 SER H CA  1 
ATOM   2615 C C   . SER B 2 170 ? 21.069  -12.609 -82.532 1.00 211.14 ? 170 SER H C   1 
ATOM   2616 O O   . SER B 2 170 ? 22.145  -12.411 -83.130 1.00 223.02 ? 170 SER H O   1 
ATOM   2617 C CB  . SER B 2 170 ? 18.979  -11.339 -83.080 1.00 219.39 ? 170 SER H CB  1 
ATOM   2618 O OG  . SER B 2 170 ? 19.359  -11.161 -84.437 1.00 233.07 ? 170 SER H OG  1 
ATOM   2619 N N   . GLY B 2 171 ? 20.618  -13.812 -82.161 1.00 212.48 ? 171 GLY H N   1 
ATOM   2620 C CA  . GLY B 2 171 ? 21.372  -15.047 -82.460 1.00 201.08 ? 171 GLY H CA  1 
ATOM   2621 C C   . GLY B 2 171 ? 22.264  -15.452 -81.301 1.00 201.34 ? 171 GLY H C   1 
ATOM   2622 O O   . GLY B 2 171 ? 22.565  -16.655 -81.185 1.00 201.00 ? 171 GLY H O   1 
ATOM   2623 N N   . VAL B 2 172 ? 22.650  -14.490 -80.458 1.00 209.34 ? 172 VAL H N   1 
ATOM   2624 C CA  . VAL B 2 172 ? 23.567  -14.776 -79.315 1.00 216.39 ? 172 VAL H CA  1 
ATOM   2625 C C   . VAL B 2 172 ? 22.755  -15.372 -78.160 1.00 200.93 ? 172 VAL H C   1 
ATOM   2626 O O   . VAL B 2 172 ? 21.778  -14.724 -77.738 1.00 235.59 ? 172 VAL H O   1 
ATOM   2627 C CB  . VAL B 2 172 ? 24.307  -13.501 -78.869 1.00 218.81 ? 172 VAL H CB  1 
ATOM   2628 C CG1 . VAL B 2 172 ? 25.233  -13.770 -77.694 1.00 201.07 ? 172 VAL H CG1 1 
ATOM   2629 C CG2 . VAL B 2 172 ? 25.063  -12.855 -80.018 1.00 221.36 ? 172 VAL H CG2 1 
ATOM   2630 N N   . HIS B 2 173 ? 23.146  -16.553 -77.669 1.00 207.80 ? 173 HIS H N   1 
ATOM   2631 C CA  . HIS B 2 173 ? 22.454  -17.146 -76.496 1.00 180.63 ? 173 HIS H CA  1 
ATOM   2632 C C   . HIS B 2 173 ? 23.496  -17.489 -75.430 1.00 175.87 ? 173 HIS H C   1 
ATOM   2633 O O   . HIS B 2 173 ? 23.638  -18.679 -75.095 1.00 175.63 ? 173 HIS H O   1 
ATOM   2634 C CB  . HIS B 2 173 ? 21.622  -18.358 -76.928 1.00 162.03 ? 173 HIS H CB  1 
ATOM   2635 C CG  . HIS B 2 173 ? 20.716  -18.082 -78.082 1.00 183.98 ? 173 HIS H CG  1 
ATOM   2636 N ND1 . HIS B 2 173 ? 20.803  -18.759 -79.279 1.00 178.65 ? 173 HIS H ND1 1 
ATOM   2637 C CD2 . HIS B 2 173 ? 19.716  -17.205 -78.226 1.00 192.53 ? 173 HIS H CD2 1 
ATOM   2638 C CE1 . HIS B 2 173 ? 19.879  -18.299 -80.110 1.00 162.78 ? 173 HIS H CE1 1 
ATOM   2639 N NE2 . HIS B 2 173 ? 19.208  -17.353 -79.491 1.00 180.32 ? 173 HIS H NE2 1 
ATOM   2640 N N   . THR B 2 174 ? 24.206  -16.483 -74.913 1.00 168.00 ? 174 THR H N   1 
ATOM   2641 C CA  . THR B 2 174 ? 25.150  -16.752 -73.839 1.00 149.38 ? 174 THR H CA  1 
ATOM   2642 C C   . THR B 2 174 ? 24.467  -17.587 -72.763 1.00 144.72 ? 174 THR H C   1 
ATOM   2643 O O   . THR B 2 174 ? 23.321  -17.325 -72.387 1.00 144.41 ? 174 THR H O   1 
ATOM   2644 C CB  . THR B 2 174 ? 25.672  -15.441 -73.252 1.00 148.29 ? 174 THR H CB  1 
ATOM   2645 O OG1 . THR B 2 174 ? 24.572  -14.676 -72.743 1.00 155.09 ? 174 THR H OG1 1 
ATOM   2646 C CG2 . THR B 2 174 ? 26.393  -14.627 -74.318 1.00 154.89 ? 174 THR H CG2 1 
ATOM   2647 N N   . PHE B 2 175 ? 25.171  -18.609 -72.276 1.00 146.10 ? 175 PHE H N   1 
ATOM   2648 C CA  . PHE B 2 175 ? 24.588  -19.590 -71.372 1.00 138.34 ? 175 PHE H CA  1 
ATOM   2649 C C   . PHE B 2 175 ? 25.083  -19.383 -69.943 1.00 142.19 ? 175 PHE H C   1 
ATOM   2650 O O   . PHE B 2 175 ? 26.169  -18.838 -69.733 1.00 154.09 ? 175 PHE H O   1 
ATOM   2651 C CB  . PHE B 2 175 ? 24.934  -21.009 -71.836 1.00 144.90 ? 175 PHE H CB  1 
ATOM   2652 C CG  . PHE B 2 175 ? 24.084  -21.489 -72.974 1.00 145.06 ? 175 PHE H CG  1 
ATOM   2653 C CD1 . PHE B 2 175 ? 22.798  -21.953 -72.750 1.00 148.87 ? 175 PHE H CD1 1 
ATOM   2654 C CD2 . PHE B 2 175 ? 24.555  -21.438 -74.274 1.00 157.91 ? 175 PHE H CD2 1 
ATOM   2655 C CE1 . PHE B 2 175 ? 22.009  -22.386 -73.800 1.00 167.06 ? 175 PHE H CE1 1 
ATOM   2656 C CE2 . PHE B 2 175 ? 23.770  -21.864 -75.329 1.00 168.63 ? 175 PHE H CE2 1 
ATOM   2657 C CZ  . PHE B 2 175 ? 22.496  -22.339 -75.092 1.00 167.55 ? 175 PHE H CZ  1 
ATOM   2658 N N   . PRO B 2 176 ? 24.306  -19.791 -68.938 1.00 120.70 ? 176 PRO H N   1 
ATOM   2659 C CA  . PRO B 2 176 ? 24.759  -19.625 -67.552 1.00 106.79 ? 176 PRO H CA  1 
ATOM   2660 C C   . PRO B 2 176 ? 25.975  -20.490 -67.260 1.00 134.35 ? 176 PRO H C   1 
ATOM   2661 O O   . PRO B 2 176 ? 26.068  -21.636 -67.707 1.00 131.52 ? 176 PRO H O   1 
ATOM   2662 C CB  . PRO B 2 176 ? 23.546  -20.071 -66.725 1.00 87.30  ? 176 PRO H CB  1 
ATOM   2663 C CG  . PRO B 2 176 ? 22.384  -19.919 -67.648 1.00 110.37 ? 176 PRO H CG  1 
ATOM   2664 C CD  . PRO B 2 176 ? 22.921  -20.287 -69.001 1.00 118.59 ? 176 PRO H CD  1 
ATOM   2665 N N   . ALA B 2 177 ? 26.909  -19.925 -66.498 1.00 145.39 ? 177 ALA H N   1 
ATOM   2666 C CA  . ALA B 2 177 ? 28.139  -20.624 -66.156 1.00 157.26 ? 177 ALA H CA  1 
ATOM   2667 C C   . ALA B 2 177 ? 27.853  -21.846 -65.292 1.00 157.25 ? 177 ALA H C   1 
ATOM   2668 O O   . ALA B 2 177 ? 26.911  -21.870 -64.497 1.00 172.52 ? 177 ALA H O   1 
ATOM   2669 C CB  . ALA B 2 177 ? 29.098  -19.690 -65.420 1.00 169.12 ? 177 ALA H CB  1 
ATOM   2670 N N   . VAL B 2 178 ? 28.685  -22.870 -65.457 1.00 138.74 ? 178 VAL H N   1 
ATOM   2671 C CA  . VAL B 2 178 ? 28.623  -24.081 -64.646 1.00 146.07 ? 178 VAL H CA  1 
ATOM   2672 C C   . VAL B 2 178 ? 29.966  -24.247 -63.955 1.00 152.21 ? 178 VAL H C   1 
ATOM   2673 O O   . VAL B 2 178 ? 31.011  -24.270 -64.617 1.00 160.05 ? 178 VAL H O   1 
ATOM   2674 C CB  . VAL B 2 178 ? 28.280  -25.322 -65.486 1.00 158.75 ? 178 VAL H CB  1 
ATOM   2675 C CG1 . VAL B 2 178 ? 28.340  -26.577 -64.625 1.00 156.52 ? 178 VAL H CG1 1 
ATOM   2676 C CG2 . VAL B 2 178 ? 26.904  -25.172 -66.116 1.00 159.11 ? 178 VAL H CG2 1 
ATOM   2677 N N   . LEU B 2 179 ? 29.938  -24.333 -62.626 1.00 142.26 ? 179 LEU H N   1 
ATOM   2678 C CA  . LEU B 2 179 ? 31.115  -24.699 -61.855 1.00 126.64 ? 179 LEU H CA  1 
ATOM   2679 C C   . LEU B 2 179 ? 31.747  -25.969 -62.399 1.00 141.76 ? 179 LEU H C   1 
ATOM   2680 O O   . LEU B 2 179 ? 31.147  -27.046 -62.314 1.00 129.24 ? 179 LEU H O   1 
ATOM   2681 C CB  . LEU B 2 179 ? 30.752  -24.897 -60.382 1.00 134.68 ? 179 LEU H CB  1 
ATOM   2682 C CG  . LEU B 2 179 ? 30.380  -23.669 -59.562 1.00 158.07 ? 179 LEU H CG  1 
ATOM   2683 C CD1 . LEU B 2 179 ? 29.811  -24.092 -58.231 1.00 167.09 ? 179 LEU H CD1 1 
ATOM   2684 C CD2 . LEU B 2 179 ? 31.645  -22.891 -59.332 1.00 144.68 ? 179 LEU H CD2 1 
ATOM   2685 N N   . GLN B 2 180 ? 32.937  -25.859 -62.982 1.00 154.74 ? 180 GLN H N   1 
ATOM   2686 C CA  . GLN B 2 180 ? 33.721  -27.061 -63.211 1.00 165.23 ? 180 GLN H CA  1 
ATOM   2687 C C   . GLN B 2 180 ? 33.998  -27.712 -61.864 1.00 166.56 ? 180 GLN H C   1 
ATOM   2688 O O   . GLN B 2 180 ? 34.319  -27.029 -60.887 1.00 163.50 ? 180 GLN H O   1 
ATOM   2689 C CB  . GLN B 2 180 ? 35.031  -26.739 -63.933 1.00 161.41 ? 180 GLN H CB  1 
ATOM   2690 C CG  . GLN B 2 180 ? 34.862  -26.220 -65.351 1.00 146.22 ? 180 GLN H CG  1 
ATOM   2691 C CD  . GLN B 2 180 ? 36.188  -25.908 -66.026 1.00 138.89 ? 180 GLN H CD  1 
ATOM   2692 O OE1 . GLN B 2 180 ? 37.196  -25.670 -65.364 1.00 141.86 ? 180 GLN H OE1 1 
ATOM   2693 N NE2 . GLN B 2 180 ? 36.187  -25.907 -67.352 1.00 138.63 ? 180 GLN H NE2 1 
ATOM   2694 N N   . SER B 2 181 ? 33.847  -29.038 -61.809 1.00 157.70 ? 181 SER H N   1 
ATOM   2695 C CA  . SER B 2 181 ? 33.965  -29.761 -60.546 1.00 162.20 ? 181 SER H CA  1 
ATOM   2696 C C   . SER B 2 181 ? 35.269  -29.458 -59.814 1.00 173.19 ? 181 SER H C   1 
ATOM   2697 O O   . SER B 2 181 ? 35.329  -29.601 -58.586 1.00 174.49 ? 181 SER H O   1 
ATOM   2698 C CB  . SER B 2 181 ? 33.840  -31.263 -60.805 1.00 167.67 ? 181 SER H CB  1 
ATOM   2699 O OG  . SER B 2 181 ? 34.856  -31.711 -61.687 1.00 189.90 ? 181 SER H OG  1 
ATOM   2700 N N   . SER B 2 182 ? 36.309  -29.037 -60.533 1.00 172.85 ? 182 SER H N   1 
ATOM   2701 C CA  . SER B 2 182 ? 37.576  -28.628 -59.939 1.00 161.15 ? 182 SER H CA  1 
ATOM   2702 C C   . SER B 2 182 ? 37.553  -27.195 -59.411 1.00 158.78 ? 182 SER H C   1 
ATOM   2703 O O   . SER B 2 182 ? 38.604  -26.675 -59.020 1.00 167.85 ? 182 SER H O   1 
ATOM   2704 C CB  . SER B 2 182 ? 38.708  -28.792 -60.958 1.00 168.90 ? 182 SER H CB  1 
ATOM   2705 O OG  . SER B 2 182 ? 38.483  -27.993 -62.109 1.00 157.71 ? 182 SER H OG  1 
ATOM   2706 N N   . GLY B 2 183 ? 36.389  -26.547 -59.392 1.00 156.02 ? 183 GLY H N   1 
ATOM   2707 C CA  . GLY B 2 183 ? 36.249  -25.226 -58.822 1.00 151.59 ? 183 GLY H CA  1 
ATOM   2708 C C   . GLY B 2 183 ? 36.226  -24.087 -59.820 1.00 149.42 ? 183 GLY H C   1 
ATOM   2709 O O   . GLY B 2 183 ? 35.873  -22.965 -59.437 1.00 168.03 ? 183 GLY H O   1 
ATOM   2710 N N   . LEU B 2 184 ? 36.585  -24.332 -61.078 1.00 152.97 ? 184 LEU H N   1 
ATOM   2711 C CA  . LEU B 2 184 ? 36.609  -23.286 -62.089 1.00 160.99 ? 184 LEU H CA  1 
ATOM   2712 C C   . LEU B 2 184 ? 35.216  -23.117 -62.702 1.00 166.63 ? 184 LEU H C   1 
ATOM   2713 O O   . LEU B 2 184 ? 34.232  -23.697 -62.232 1.00 164.42 ? 184 LEU H O   1 
ATOM   2714 C CB  . LEU B 2 184 ? 37.668  -23.602 -63.143 1.00 166.04 ? 184 LEU H CB  1 
ATOM   2715 C CG  . LEU B 2 184 ? 39.118  -23.626 -62.660 1.00 163.23 ? 184 LEU H CG  1 
ATOM   2716 C CD1 . LEU B 2 184 ? 40.046  -24.107 -63.764 1.00 166.92 ? 184 LEU H CD1 1 
ATOM   2717 C CD2 . LEU B 2 184 ? 39.532  -22.250 -62.167 1.00 142.92 ? 184 LEU H CD2 1 
ATOM   2718 N N   . TYR B 2 185 ? 35.121  -22.314 -63.761 1.00 156.59 ? 185 TYR H N   1 
ATOM   2719 C CA  . TYR B 2 185 ? 33.861  -21.999 -64.420 1.00 147.49 ? 185 TYR H CA  1 
ATOM   2720 C C   . TYR B 2 185 ? 34.001  -22.194 -65.925 1.00 145.13 ? 185 TYR H C   1 
ATOM   2721 O O   . TYR B 2 185 ? 35.108  -22.262 -66.467 1.00 142.15 ? 185 TYR H O   1 
ATOM   2722 C CB  . TYR B 2 185 ? 33.419  -20.561 -64.127 1.00 144.96 ? 185 TYR H CB  1 
ATOM   2723 C CG  . TYR B 2 185 ? 32.949  -20.305 -62.716 1.00 163.60 ? 185 TYR H CG  1 
ATOM   2724 C CD1 . TYR B 2 185 ? 33.858  -20.101 -61.693 1.00 159.18 ? 185 TYR H CD1 1 
ATOM   2725 C CD2 . TYR B 2 185 ? 31.597  -20.195 -62.419 1.00 175.10 ? 185 TYR H CD2 1 
ATOM   2726 C CE1 . TYR B 2 185 ? 33.438  -19.861 -60.406 1.00 156.63 ? 185 TYR H CE1 1 
ATOM   2727 C CE2 . TYR B 2 185 ? 31.168  -19.936 -61.129 1.00 167.56 ? 185 TYR H CE2 1 
ATOM   2728 C CZ  . TYR B 2 185 ? 32.100  -19.761 -60.128 1.00 168.28 ? 185 TYR H CZ  1 
ATOM   2729 O OH  . TYR B 2 185 ? 31.702  -19.511 -58.834 1.00 174.57 ? 185 TYR H OH  1 
ATOM   2730 N N   . SER B 2 186 ? 32.857  -22.269 -66.602 1.00 139.14 ? 186 SER H N   1 
ATOM   2731 C CA  . SER B 2 186 ? 32.842  -22.452 -68.049 1.00 123.12 ? 186 SER H CA  1 
ATOM   2732 C C   . SER B 2 186 ? 31.576  -21.828 -68.610 1.00 113.19 ? 186 SER H C   1 
ATOM   2733 O O   . SER B 2 186 ? 30.471  -22.275 -68.293 1.00 132.49 ? 186 SER H O   1 
ATOM   2734 C CB  . SER B 2 186 ? 32.924  -23.935 -68.418 1.00 128.31 ? 186 SER H CB  1 
ATOM   2735 O OG  . SER B 2 186 ? 34.164  -24.495 -68.017 1.00 138.92 ? 186 SER H OG  1 
ATOM   2736 N N   . LEU B 2 187 ? 31.738  -20.794 -69.427 1.00 117.68 ? 187 LEU H N   1 
ATOM   2737 C CA  . LEU B 2 187 ? 30.643  -20.223 -70.195 1.00 127.63 ? 187 LEU H CA  1 
ATOM   2738 C C   . LEU B 2 187 ? 30.705  -20.699 -71.636 1.00 144.43 ? 187 LEU H C   1 
ATOM   2739 O O   . LEU B 2 187 ? 31.773  -21.013 -72.168 1.00 153.64 ? 187 LEU H O   1 
ATOM   2740 C CB  . LEU B 2 187 ? 30.671  -18.695 -70.179 1.00 135.17 ? 187 LEU H CB  1 
ATOM   2741 C CG  . LEU B 2 187 ? 30.347  -17.945 -68.894 1.00 172.79 ? 187 LEU H CG  1 
ATOM   2742 C CD1 . LEU B 2 187 ? 30.661  -16.487 -69.080 1.00 186.09 ? 187 LEU H CD1 1 
ATOM   2743 C CD2 . LEU B 2 187 ? 28.893  -18.103 -68.558 1.00 155.89 ? 187 LEU H CD2 1 
ATOM   2744 N N   . SER B 2 188 ? 29.539  -20.734 -72.267 1.00 127.56 ? 188 SER H N   1 
ATOM   2745 C CA  . SER B 2 188 ? 29.418  -21.043 -73.683 1.00 139.56 ? 188 SER H CA  1 
ATOM   2746 C C   . SER B 2 188 ? 28.540  -19.978 -74.318 1.00 144.06 ? 188 SER H C   1 
ATOM   2747 O O   . SER B 2 188 ? 27.398  -19.780 -73.892 1.00 145.91 ? 188 SER H O   1 
ATOM   2748 C CB  . SER B 2 188 ? 28.838  -22.444 -73.885 1.00 141.07 ? 188 SER H CB  1 
ATOM   2749 O OG  . SER B 2 188 ? 27.527  -22.522 -73.358 1.00 131.85 ? 188 SER H OG  1 
ATOM   2750 N N   . SER B 2 189 ? 29.081  -19.278 -75.313 1.00 161.35 ? 189 SER H N   1 
ATOM   2751 C CA  . SER B 2 189 ? 28.376  -18.207 -76.008 1.00 153.13 ? 189 SER H CA  1 
ATOM   2752 C C   . SER B 2 189 ? 28.304  -18.559 -77.486 1.00 149.29 ? 189 SER H C   1 
ATOM   2753 O O   . SER B 2 189 ? 29.338  -18.624 -78.158 1.00 153.58 ? 189 SER H O   1 
ATOM   2754 C CB  . SER B 2 189 ? 29.086  -16.865 -75.809 1.00 163.58 ? 189 SER H CB  1 
ATOM   2755 O OG  . SER B 2 189 ? 28.995  -16.430 -74.464 1.00 155.91 ? 189 SER H OG  1 
ATOM   2756 N N   . VAL B 2 190 ? 27.088  -18.774 -77.994 1.00 160.20 ? 190 VAL H N   1 
ATOM   2757 C CA  . VAL B 2 190 ? 26.889  -19.265 -79.352 1.00 171.11 ? 190 VAL H CA  1 
ATOM   2758 C C   . VAL B 2 190 ? 25.974  -18.323 -80.125 1.00 181.25 ? 190 VAL H C   1 
ATOM   2759 O O   . VAL B 2 190 ? 25.203  -17.551 -79.550 1.00 196.81 ? 190 VAL H O   1 
ATOM   2760 C CB  . VAL B 2 190 ? 26.316  -20.699 -79.369 1.00 172.19 ? 190 VAL H CB  1 
ATOM   2761 C CG1 . VAL B 2 190 ? 27.366  -21.694 -78.894 1.00 190.23 ? 190 VAL H CG1 1 
ATOM   2762 C CG2 . VAL B 2 190 ? 25.060  -20.783 -78.517 1.00 171.23 ? 190 VAL H CG2 1 
ATOM   2763 N N   . VAL B 2 191 ? 26.070  -18.404 -81.455 1.00 171.35 ? 191 VAL H N   1 
ATOM   2764 C CA  . VAL B 2 191 ? 25.308  -17.564 -82.372 1.00 160.86 ? 191 VAL H CA  1 
ATOM   2765 C C   . VAL B 2 191 ? 24.773  -18.449 -83.490 1.00 163.27 ? 191 VAL H C   1 
ATOM   2766 O O   . VAL B 2 191 ? 25.415  -19.424 -83.890 1.00 173.65 ? 191 VAL H O   1 
ATOM   2767 C CB  . VAL B 2 191 ? 26.175  -16.416 -82.950 1.00 177.45 ? 191 VAL H CB  1 
ATOM   2768 C CG1 . VAL B 2 191 ? 25.390  -15.568 -83.940 1.00 165.78 ? 191 VAL H CG1 1 
ATOM   2769 C CG2 . VAL B 2 191 ? 26.733  -15.556 -81.843 1.00 212.63 ? 191 VAL H CG2 1 
ATOM   2770 N N   . THR B 2 192 ? 23.587  -18.109 -83.996 1.00 161.99 ? 192 THR H N   1 
ATOM   2771 C CA  . THR B 2 192 ? 22.962  -18.828 -85.106 1.00 166.32 ? 192 THR H CA  1 
ATOM   2772 C C   . THR B 2 192 ? 22.782  -17.861 -86.276 1.00 153.53 ? 192 THR H C   1 
ATOM   2773 O O   . THR B 2 192 ? 21.877  -17.021 -86.266 1.00 143.46 ? 192 THR H O   1 
ATOM   2774 C CB  . THR B 2 192 ? 21.631  -19.447 -84.683 1.00 158.05 ? 192 THR H CB  1 
ATOM   2775 O OG1 . THR B 2 192 ? 20.742  -18.420 -84.227 1.00 163.28 ? 192 THR H OG1 1 
ATOM   2776 C CG2 . THR B 2 192 ? 21.846  -20.458 -83.563 1.00 138.56 ? 192 THR H CG2 1 
ATOM   2777 N N   . VAL B 2 193 ? 23.647  -17.983 -87.280 1.00 160.89 ? 193 VAL H N   1 
ATOM   2778 C CA  . VAL B 2 193 ? 23.600  -17.165 -88.491 1.00 179.99 ? 193 VAL H CA  1 
ATOM   2779 C C   . VAL B 2 193 ? 23.523  -18.106 -89.690 1.00 212.33 ? 193 VAL H C   1 
ATOM   2780 O O   . VAL B 2 193 ? 24.254  -19.107 -89.728 1.00 235.91 ? 193 VAL H O   1 
ATOM   2781 C CB  . VAL B 2 193 ? 24.819  -16.228 -88.576 1.00 181.01 ? 193 VAL H CB  1 
ATOM   2782 C CG1 . VAL B 2 193 ? 24.835  -15.465 -89.891 1.00 190.75 ? 193 VAL H CG1 1 
ATOM   2783 C CG2 . VAL B 2 193 ? 24.820  -15.255 -87.412 1.00 170.98 ? 193 VAL H CG2 1 
ATOM   2784 N N   . PRO B 2 194 ? 22.654  -17.845 -90.670 1.00 207.42 ? 194 PRO H N   1 
ATOM   2785 C CA  . PRO B 2 194 ? 22.523  -18.758 -91.815 1.00 202.98 ? 194 PRO H CA  1 
ATOM   2786 C C   . PRO B 2 194 ? 23.858  -19.026 -92.495 1.00 208.47 ? 194 PRO H C   1 
ATOM   2787 O O   . PRO B 2 194 ? 24.693  -18.132 -92.647 1.00 205.70 ? 194 PRO H O   1 
ATOM   2788 C CB  . PRO B 2 194 ? 21.560  -18.015 -92.750 1.00 183.40 ? 194 PRO H CB  1 
ATOM   2789 C CG  . PRO B 2 194 ? 21.504  -16.601 -92.225 1.00 201.25 ? 194 PRO H CG  1 
ATOM   2790 C CD  . PRO B 2 194 ? 21.686  -16.742 -90.753 1.00 200.82 ? 194 PRO H CD  1 
ATOM   2791 N N   . SER B 2 195 ? 24.047  -20.278 -92.922 1.00 216.10 ? 195 SER H N   1 
ATOM   2792 C CA  . SER B 2 195 ? 25.296  -20.694 -93.552 1.00 211.78 ? 195 SER H CA  1 
ATOM   2793 C C   . SER B 2 195 ? 25.592  -19.947 -94.846 1.00 216.08 ? 195 SER H C   1 
ATOM   2794 O O   . SER B 2 195 ? 26.685  -20.113 -95.398 1.00 207.36 ? 195 SER H O   1 
ATOM   2795 C CB  . SER B 2 195 ? 25.262  -22.195 -93.831 1.00 206.73 ? 195 SER H CB  1 
ATOM   2796 O OG  . SER B 2 195 ? 24.522  -22.469 -95.007 1.00 219.65 ? 195 SER H OG  1 
ATOM   2797 N N   . SER B 2 196 ? 24.647  -19.151 -95.349 1.00 203.16 ? 196 SER H N   1 
ATOM   2798 C CA  . SER B 2 196 ? 24.911  -18.317 -96.515 1.00 187.22 ? 196 SER H CA  1 
ATOM   2799 C C   . SER B 2 196 ? 26.103  -17.395 -96.276 1.00 195.66 ? 196 SER H C   1 
ATOM   2800 O O   . SER B 2 196 ? 27.019  -17.314 -97.104 1.00 182.60 ? 196 SER H O   1 
ATOM   2801 C CB  . SER B 2 196 ? 23.662  -17.505 -96.856 1.00 177.90 ? 196 SER H CB  1 
ATOM   2802 O OG  . SER B 2 196 ? 23.365  -16.589 -95.816 1.00 187.47 ? 196 SER H OG  1 
ATOM   2803 N N   . SER B 2 197 ? 26.114  -16.705 -95.137 1.00 212.36 ? 197 SER H N   1 
ATOM   2804 C CA  . SER B 2 197 ? 27.148  -15.716 -94.835 1.00 213.51 ? 197 SER H CA  1 
ATOM   2805 C C   . SER B 2 197 ? 28.249  -16.345 -93.981 1.00 207.55 ? 197 SER H C   1 
ATOM   2806 O O   . SER B 2 197 ? 28.420  -16.044 -92.799 1.00 222.47 ? 197 SER H O   1 
ATOM   2807 C CB  . SER B 2 197 ? 26.527  -14.500 -94.150 1.00 205.20 ? 197 SER H CB  1 
ATOM   2808 O OG  . SER B 2 197 ? 25.981  -14.844 -92.890 1.00 209.67 ? 197 SER H OG  1 
ATOM   2809 N N   . LEU B 2 198 ? 29.012  -17.235 -94.616 1.00 201.45 ? 198 LEU H N   1 
ATOM   2810 C CA  . LEU B 2 198 ? 30.169  -17.837 -93.963 1.00 199.56 ? 198 LEU H CA  1 
ATOM   2811 C C   . LEU B 2 198 ? 31.397  -16.948 -93.809 1.00 212.52 ? 198 LEU H C   1 
ATOM   2812 O O   . LEU B 2 198 ? 31.957  -16.838 -92.714 1.00 215.67 ? 198 LEU H O   1 
ATOM   2813 C CB  . LEU B 2 198 ? 30.669  -19.052 -94.748 1.00 189.86 ? 198 LEU H CB  1 
ATOM   2814 C CG  . LEU B 2 198 ? 29.753  -20.270 -94.831 1.00 169.51 ? 198 LEU H CG  1 
ATOM   2815 C CD1 . LEU B 2 198 ? 30.348  -21.307 -95.767 1.00 154.95 ? 198 LEU H CD1 1 
ATOM   2816 C CD2 . LEU B 2 198 ? 29.521  -20.860 -93.447 1.00 155.99 ? 198 LEU H CD2 1 
ATOM   2817 N N   . GLY B 2 199 ? 31.819  -16.311 -94.900 1.00 217.06 ? 199 GLY H N   1 
ATOM   2818 C CA  . GLY B 2 199 ? 33.018  -15.495 -94.893 1.00 203.84 ? 199 GLY H CA  1 
ATOM   2819 C C   . GLY B 2 199 ? 32.658  -14.023 -94.893 1.00 201.24 ? 199 GLY H C   1 
ATOM   2820 O O   . GLY B 2 199 ? 33.436  -13.192 -94.413 1.00 187.54 ? 199 GLY H O   1 
ATOM   2821 N N   . THR B 2 200 ? 31.483  -13.683 -95.429 1.00 205.00 ? 200 THR H N   1 
ATOM   2822 C CA  . THR B 2 200 ? 31.072  -12.282 -95.488 1.00 200.04 ? 200 THR H CA  1 
ATOM   2823 C C   . THR B 2 200 ? 30.880  -11.705 -94.089 1.00 213.71 ? 200 THR H C   1 
ATOM   2824 O O   . THR B 2 200 ? 31.376  -10.616 -93.781 1.00 215.85 ? 200 THR H O   1 
ATOM   2825 C CB  . THR B 2 200 ? 29.790  -12.142 -96.311 1.00 184.57 ? 200 THR H CB  1 
ATOM   2826 O OG1 . THR B 2 200 ? 28.750  -12.927 -95.717 1.00 203.28 ? 200 THR H OG1 1 
ATOM   2827 C CG2 . THR B 2 200 ? 30.017  -12.623 -97.736 1.00 181.92 ? 200 THR H CG2 1 
ATOM   2828 N N   . GLN B 2 201 ? 30.166  -12.425 -93.226 1.00 226.08 ? 201 GLN H N   1 
ATOM   2829 C CA  . GLN B 2 201 ? 29.959  -11.971 -91.857 1.00 213.73 ? 201 GLN H CA  1 
ATOM   2830 C C   . GLN B 2 201 ? 31.162  -12.333 -90.998 1.00 209.88 ? 201 GLN H C   1 
ATOM   2831 O O   . GLN B 2 201 ? 31.576  -13.495 -90.951 1.00 218.26 ? 201 GLN H O   1 
ATOM   2832 C CB  . GLN B 2 201 ? 28.688  -12.585 -91.270 1.00 213.35 ? 201 GLN H CB  1 
ATOM   2833 C CG  . GLN B 2 201 ? 28.319  -12.028 -89.903 1.00 208.37 ? 201 GLN H CG  1 
ATOM   2834 C CD  . GLN B 2 201 ? 26.905  -12.378 -89.493 1.00 208.68 ? 201 GLN H CD  1 
ATOM   2835 O OE1 . GLN B 2 201 ? 26.649  -12.733 -88.342 1.00 193.33 ? 201 GLN H OE1 1 
ATOM   2836 N NE2 . GLN B 2 201 ? 25.975  -12.272 -90.434 1.00 217.62 ? 201 GLN H NE2 1 
ATOM   2837 N N   . THR B 2 202 ? 31.728  -11.335 -90.325 1.00 223.66 ? 202 THR H N   1 
ATOM   2838 C CA  . THR B 2 202 ? 32.825  -11.574 -89.401 1.00 229.93 ? 202 THR H CA  1 
ATOM   2839 C C   . THR B 2 202 ? 32.288  -12.075 -88.062 1.00 229.81 ? 202 THR H C   1 
ATOM   2840 O O   . THR B 2 202 ? 31.191  -11.705 -87.631 1.00 208.16 ? 202 THR H O   1 
ATOM   2841 C CB  . THR B 2 202 ? 33.651  -10.299 -89.208 1.00 208.92 ? 202 THR H CB  1 
ATOM   2842 O OG1 . THR B 2 202 ? 32.811  -9.247  -88.714 1.00 196.02 ? 202 THR H OG1 1 
ATOM   2843 C CG2 . THR B 2 202 ? 34.275  -9.860  -90.533 1.00 176.68 ? 202 THR H CG2 1 
ATOM   2844 N N   . TYR B 2 203 ? 33.067  -12.941 -87.411 1.00 219.57 ? 203 TYR H N   1 
ATOM   2845 C CA  . TYR B 2 203 ? 32.679  -13.568 -86.147 1.00 201.69 ? 203 TYR H CA  1 
ATOM   2846 C C   . TYR B 2 203 ? 33.808  -13.393 -85.137 1.00 184.22 ? 203 TYR H C   1 
ATOM   2847 O O   . TYR B 2 203 ? 34.882  -13.984 -85.295 1.00 171.11 ? 203 TYR H O   1 
ATOM   2848 C CB  . TYR B 2 203 ? 32.354  -15.048 -86.347 1.00 195.39 ? 203 TYR H CB  1 
ATOM   2849 C CG  . TYR B 2 203 ? 31.223  -15.289 -87.312 1.00 193.55 ? 203 TYR H CG  1 
ATOM   2850 C CD1 . TYR B 2 203 ? 29.907  -15.067 -86.934 1.00 184.33 ? 203 TYR H CD1 1 
ATOM   2851 C CD2 . TYR B 2 203 ? 31.471  -15.727 -88.605 1.00 201.79 ? 203 TYR H CD2 1 
ATOM   2852 C CE1 . TYR B 2 203 ? 28.868  -15.280 -87.812 1.00 194.23 ? 203 TYR H CE1 1 
ATOM   2853 C CE2 . TYR B 2 203 ? 30.437  -15.946 -89.493 1.00 219.31 ? 203 TYR H CE2 1 
ATOM   2854 C CZ  . TYR B 2 203 ? 29.139  -15.720 -89.091 1.00 214.89 ? 203 TYR H CZ  1 
ATOM   2855 O OH  . TYR B 2 203 ? 28.105  -15.934 -89.972 1.00 225.94 ? 203 TYR H OH  1 
ATOM   2856 N N   . ILE B 2 204 ? 33.563  -12.590 -84.101 1.00 187.73 ? 204 ILE H N   1 
ATOM   2857 C CA  . ILE B 2 204 ? 34.559  -12.273 -83.080 1.00 185.78 ? 204 ILE H CA  1 
ATOM   2858 C C   . ILE B 2 204 ? 33.877  -12.273 -81.716 1.00 186.16 ? 204 ILE H C   1 
ATOM   2859 O O   . ILE B 2 204 ? 32.868  -11.587 -81.523 1.00 175.12 ? 204 ILE H O   1 
ATOM   2860 C CB  . ILE B 2 204 ? 35.237  -10.909 -83.343 1.00 190.74 ? 204 ILE H CB  1 
ATOM   2861 C CG1 . ILE B 2 204 ? 35.796  -10.817 -84.767 1.00 192.83 ? 204 ILE H CG1 1 
ATOM   2862 C CG2 . ILE B 2 204 ? 36.362  -10.668 -82.361 1.00 184.27 ? 204 ILE H CG2 1 
ATOM   2863 C CD1 . ILE B 2 204 ? 37.108  -11.547 -84.971 1.00 176.28 ? 204 ILE H CD1 1 
ATOM   2864 N N   . CYS B 2 205 ? 34.426  -13.043 -80.770 1.00 189.63 ? 205 CYS H N   1 
ATOM   2865 C CA  . CYS B 2 205 ? 33.963  -13.054 -79.383 1.00 188.20 ? 205 CYS H CA  1 
ATOM   2866 C C   . CYS B 2 205 ? 34.872  -12.151 -78.561 1.00 194.33 ? 205 CYS H C   1 
ATOM   2867 O O   . CYS B 2 205 ? 36.009  -12.520 -78.249 1.00 200.25 ? 205 CYS H O   1 
ATOM   2868 C CB  . CYS B 2 205 ? 33.954  -14.468 -78.807 1.00 169.20 ? 205 CYS H CB  1 
ATOM   2869 S SG  . CYS B 2 205 ? 33.117  -15.675 -79.830 1.00 213.36 ? 205 CYS H SG  1 
ATOM   2870 N N   . ASN B 2 206 ? 34.371  -10.976 -78.203 1.00 174.96 ? 206 ASN H N   1 
ATOM   2871 C CA  . ASN B 2 206 ? 35.130  -10.013 -77.414 1.00 180.37 ? 206 ASN H CA  1 
ATOM   2872 C C   . ASN B 2 206 ? 34.685  -10.173 -75.967 1.00 167.15 ? 206 ASN H C   1 
ATOM   2873 O O   . ASN B 2 206 ? 33.673  -9.607  -75.547 1.00 154.48 ? 206 ASN H O   1 
ATOM   2874 C CB  . ASN B 2 206 ? 34.912  -8.598  -77.934 1.00 179.29 ? 206 ASN H CB  1 
ATOM   2875 C CG  . ASN B 2 206 ? 35.503  -8.394  -79.309 1.00 179.87 ? 206 ASN H CG  1 
ATOM   2876 O OD1 . ASN B 2 206 ? 36.386  -9.137  -79.725 1.00 174.83 ? 206 ASN H OD1 1 
ATOM   2877 N ND2 . ASN B 2 206 ? 35.010  -7.395  -80.029 1.00 194.53 ? 206 ASN H ND2 1 
ATOM   2878 N N   . VAL B 2 207 ? 35.439  -10.963 -75.213 1.00 172.81 ? 207 VAL H N   1 
ATOM   2879 C CA  . VAL B 2 207 ? 35.099  -11.324 -73.845 1.00 163.34 ? 207 VAL H CA  1 
ATOM   2880 C C   . VAL B 2 207 ? 35.988  -10.537 -72.893 1.00 167.63 ? 207 VAL H C   1 
ATOM   2881 O O   . VAL B 2 207 ? 37.114  -10.158 -73.234 1.00 173.82 ? 207 VAL H O   1 
ATOM   2882 C CB  . VAL B 2 207 ? 35.259  -12.846 -73.633 1.00 161.85 ? 207 VAL H CB  1 
ATOM   2883 C CG1 . VAL B 2 207 ? 34.777  -13.262 -72.254 1.00 172.16 ? 207 VAL H CG1 1 
ATOM   2884 C CG2 . VAL B 2 207 ? 34.524  -13.614 -74.723 1.00 156.96 ? 207 VAL H CG2 1 
ATOM   2885 N N   . ASN B 2 208 ? 35.471  -10.280 -71.691 1.00 175.16 ? 208 ASN H N   1 
ATOM   2886 C CA  . ASN B 2 208 ? 36.270  -9.695  -70.623 1.00 168.54 ? 208 ASN H CA  1 
ATOM   2887 C C   . ASN B 2 208 ? 35.847  -10.287 -69.288 1.00 166.37 ? 208 ASN H C   1 
ATOM   2888 O O   . ASN B 2 208 ? 34.652  -10.356 -68.985 1.00 162.44 ? 208 ASN H O   1 
ATOM   2889 C CB  . ASN B 2 208 ? 36.138  -8.169  -70.583 1.00 176.03 ? 208 ASN H CB  1 
ATOM   2890 C CG  . ASN B 2 208 ? 36.833  -7.558  -69.379 1.00 170.65 ? 208 ASN H CG  1 
ATOM   2891 O OD1 . ASN B 2 208 ? 37.959  -7.930  -69.046 1.00 164.92 ? 208 ASN H OD1 1 
ATOM   2892 N ND2 . ASN B 2 208 ? 36.165  -6.618  -68.720 1.00 183.68 ? 208 ASN H ND2 1 
ATOM   2893 N N   . HIS B 2 209 ? 36.831  -10.712 -68.501 1.00 171.21 ? 209 HIS H N   1 
ATOM   2894 C CA  . HIS B 2 209 ? 36.629  -11.187 -67.132 1.00 166.94 ? 209 HIS H CA  1 
ATOM   2895 C C   . HIS B 2 209 ? 36.977  -10.014 -66.219 1.00 181.95 ? 209 HIS H C   1 
ATOM   2896 O O   . HIS B 2 209 ? 38.129  -9.835  -65.827 1.00 193.29 ? 209 HIS H O   1 
ATOM   2897 C CB  . HIS B 2 209 ? 37.502  -12.409 -66.860 1.00 157.04 ? 209 HIS H CB  1 
ATOM   2898 C CG  . HIS B 2 209 ? 37.130  -13.182 -65.633 1.00 164.67 ? 209 HIS H CG  1 
ATOM   2899 N ND1 . HIS B 2 209 ? 37.905  -14.214 -65.151 1.00 168.75 ? 209 HIS H ND1 1 
ATOM   2900 C CD2 . HIS B 2 209 ? 36.061  -13.097 -64.808 1.00 170.19 ? 209 HIS H CD2 1 
ATOM   2901 C CE1 . HIS B 2 209 ? 37.339  -14.720 -64.070 1.00 163.80 ? 209 HIS H CE1 1 
ATOM   2902 N NE2 . HIS B 2 209 ? 36.218  -14.061 -63.841 1.00 173.12 ? 209 HIS H NE2 1 
ATOM   2903 N N   . LYS B 2 210 ? 35.963  -9.207  -65.888 1.00 172.64 ? 210 LYS H N   1 
ATOM   2904 C CA  . LYS B 2 210 ? 36.169  -7.960  -65.146 1.00 172.54 ? 210 LYS H CA  1 
ATOM   2905 C C   . LYS B 2 210 ? 37.022  -8.083  -63.885 1.00 184.40 ? 210 LYS H C   1 
ATOM   2906 O O   . LYS B 2 210 ? 37.899  -7.228  -63.686 1.00 190.06 ? 210 LYS H O   1 
ATOM   2907 C CB  . LYS B 2 210 ? 34.813  -7.329  -64.801 1.00 171.34 ? 210 LYS H CB  1 
ATOM   2908 C CG  . LYS B 2 210 ? 34.055  -6.773  -65.993 1.00 185.39 ? 210 LYS H CG  1 
ATOM   2909 C CD  . LYS B 2 210 ? 32.726  -6.178  -65.559 1.00 193.47 ? 210 LYS H CD  1 
ATOM   2910 C CE  . LYS B 2 210 ? 31.983  -5.562  -66.730 1.00 181.61 ? 210 LYS H CE  1 
ATOM   2911 N NZ  . LYS B 2 210 ? 30.663  -5.009  -66.321 1.00 169.62 ? 210 LYS H NZ  1 
ATOM   2912 N N   . PRO B 2 211 ? 36.824  -9.065  -62.997 1.00 181.50 ? 211 PRO H N   1 
ATOM   2913 C CA  . PRO B 2 211 ? 37.676  -9.122  -61.793 1.00 173.52 ? 211 PRO H CA  1 
ATOM   2914 C C   . PRO B 2 211 ? 39.157  -9.308  -62.088 1.00 173.99 ? 211 PRO H C   1 
ATOM   2915 O O   . PRO B 2 211 ? 39.998  -8.817  -61.323 1.00 200.26 ? 211 PRO H O   1 
ATOM   2916 C CB  . PRO B 2 211 ? 37.096  -10.309 -61.018 1.00 172.83 ? 211 PRO H CB  1 
ATOM   2917 C CG  . PRO B 2 211 ? 36.490  -11.151 -62.065 1.00 178.92 ? 211 PRO H CG  1 
ATOM   2918 C CD  . PRO B 2 211 ? 35.904  -10.215 -63.057 1.00 172.58 ? 211 PRO H CD  1 
ATOM   2919 N N   . SER B 2 212 ? 39.509  -10.003 -63.168 1.00 184.91 ? 212 SER H N   1 
ATOM   2920 C CA  . SER B 2 212 ? 40.896  -10.097 -63.602 1.00 176.61 ? 212 SER H CA  1 
ATOM   2921 C C   . SER B 2 212 ? 41.195  -9.225  -64.817 1.00 186.46 ? 212 SER H C   1 
ATOM   2922 O O   . SER B 2 212 ? 42.340  -9.207  -65.277 1.00 171.63 ? 212 SER H O   1 
ATOM   2923 C CB  . SER B 2 212 ? 41.263  -11.556 -63.903 1.00 163.35 ? 212 SER H CB  1 
ATOM   2924 O OG  . SER B 2 212 ? 40.265  -12.184 -64.686 1.00 158.88 ? 212 SER H OG  1 
ATOM   2925 N N   . ASN B 2 213 ? 40.196  -8.505  -65.340 1.00 187.90 ? 213 ASN H N   1 
ATOM   2926 C CA  . ASN B 2 213 ? 40.378  -7.577  -66.465 1.00 175.31 ? 213 ASN H CA  1 
ATOM   2927 C C   . ASN B 2 213 ? 41.081  -8.238  -67.649 1.00 174.47 ? 213 ASN H C   1 
ATOM   2928 O O   . ASN B 2 213 ? 41.982  -7.662  -68.263 1.00 165.77 ? 213 ASN H O   1 
ATOM   2929 C CB  . ASN B 2 213 ? 41.125  -6.316  -66.025 1.00 168.41 ? 213 ASN H CB  1 
ATOM   2930 C CG  . ASN B 2 213 ? 40.260  -5.379  -65.203 1.00 203.38 ? 213 ASN H CG  1 
ATOM   2931 O OD1 . ASN B 2 213 ? 39.034  -5.397  -65.304 1.00 225.67 ? 213 ASN H OD1 1 
ATOM   2932 N ND2 . ASN B 2 213 ? 40.898  -4.560  -64.374 1.00 224.43 ? 213 ASN H ND2 1 
ATOM   2933 N N   . THR B 2 214 ? 40.655  -9.453  -67.988 1.00 182.11 ? 214 THR H N   1 
ATOM   2934 C CA  . THR B 2 214 ? 41.251  -10.199 -69.086 1.00 166.06 ? 214 THR H CA  1 
ATOM   2935 C C   . THR B 2 214 ? 40.308  -9.725  -70.208 1.00 150.39 ? 214 THR H C   1 
ATOM   2936 O O   . THR B 2 214 ? 39.219  -10.262 -70.411 1.00 152.95 ? 214 THR H O   1 
ATOM   2937 C CB  . THR B 2 214 ? 41.245  -11.687 -68.816 1.00 162.83 ? 214 THR H CB  1 
ATOM   2938 O OG1 . THR B 2 214 ? 39.891  -12.121 -68.670 1.00 169.37 ? 214 THR H OG1 1 
ATOM   2939 C CG2 . THR B 2 214 ? 42.001  -11.991 -67.536 1.00 145.10 ? 214 THR H CG2 1 
ATOM   2940 N N   . LYS B 2 215 ? 40.747  -8.689  -70.918 1.00 140.47 ? 215 LYS H N   1 
ATOM   2941 C CA  . LYS B 2 215 ? 40.001  -8.188  -72.046 1.00 161.05 ? 215 LYS H CA  1 
ATOM   2942 C C   . LYS B 2 215 ? 40.672  -8.926  -73.209 1.00 168.66 ? 215 LYS H C   1 
ATOM   2943 O O   . LYS B 2 215 ? 41.842  -8.677  -73.521 1.00 167.92 ? 215 LYS H O   1 
ATOM   2944 C CB  . LYS B 2 215 ? 40.148  -6.667  -72.224 1.00 161.54 ? 215 LYS H CB  1 
ATOM   2945 C CG  . LYS B 2 215 ? 39.338  -5.859  -71.219 1.00 149.67 ? 215 LYS H CG  1 
ATOM   2946 C CD  . LYS B 2 215 ? 39.552  -4.362  -71.402 1.00 147.77 ? 215 LYS H CD  1 
ATOM   2947 C CE  . LYS B 2 215 ? 38.726  -3.556  -70.407 1.00 131.32 ? 215 LYS H CE  1 
ATOM   2948 N NZ  . LYS B 2 215 ? 38.935  -2.086  -70.545 1.00 135.42 ? 215 LYS H NZ  1 
ATOM   2949 N N   . VAL B 2 216 ? 39.948  -9.859  -73.822 1.00 154.57 ? 216 VAL H N   1 
ATOM   2950 C CA  . VAL B 2 216 ? 40.491  -10.722 -74.864 1.00 152.26 ? 216 VAL H CA  1 
ATOM   2951 C C   . VAL B 2 216 ? 39.502  -10.757 -76.019 1.00 158.11 ? 216 VAL H C   1 
ATOM   2952 O O   . VAL B 2 216 ? 38.330  -11.105 -75.829 1.00 166.25 ? 216 VAL H O   1 
ATOM   2953 C CB  . VAL B 2 216 ? 40.769  -12.145 -74.352 1.00 151.94 ? 216 VAL H CB  1 
ATOM   2954 C CG1 . VAL B 2 216 ? 41.198  -13.040 -75.503 1.00 146.33 ? 216 VAL H CG1 1 
ATOM   2955 C CG2 . VAL B 2 216 ? 41.831  -12.123 -73.263 1.00 138.81 ? 216 VAL H CG2 1 
ATOM   2956 N N   . ASP B 2 217 ? 39.974  -10.402 -77.211 1.00 168.30 ? 217 ASP H N   1 
ATOM   2957 C CA  . ASP B 2 217 ? 39.176  -10.440 -78.436 1.00 176.27 ? 217 ASP H CA  1 
ATOM   2958 C C   . ASP B 2 217 ? 39.522  -11.720 -79.191 1.00 182.41 ? 217 ASP H C   1 
ATOM   2959 O O   . ASP B 2 217 ? 40.581  -11.821 -79.816 1.00 186.05 ? 217 ASP H O   1 
ATOM   2960 C CB  . ASP B 2 217 ? 39.431  -9.198  -79.284 1.00 186.15 ? 217 ASP H CB  1 
ATOM   2961 C CG  . ASP B 2 217 ? 38.896  -7.930  -78.639 1.00 203.89 ? 217 ASP H CG  1 
ATOM   2962 O OD1 . ASP B 2 217 ? 38.307  -8.017  -77.540 1.00 197.30 ? 217 ASP H OD1 1 
ATOM   2963 O OD2 . ASP B 2 217 ? 39.058  -6.846  -79.237 1.00 200.00 ? 217 ASP H OD2 1 
ATOM   2964 N N   . LYS B 2 218 ? 38.621  -12.696 -79.133 1.00 183.68 ? 218 LYS H N   1 
ATOM   2965 C CA  . LYS B 2 218 ? 38.834  -14.006 -79.729 1.00 179.23 ? 218 LYS H CA  1 
ATOM   2966 C C   . LYS B 2 218 ? 38.305  -14.194 -81.145 1.00 165.83 ? 218 LYS H C   1 
ATOM   2967 O O   . LYS B 2 218 ? 37.262  -13.649 -81.514 1.00 172.30 ? 218 LYS H O   1 
ATOM   2968 C CB  . LYS B 2 218 ? 38.274  -15.108 -78.826 1.00 181.53 ? 218 LYS H CB  1 
ATOM   2969 C CG  . LYS B 2 218 ? 38.798  -16.498 -79.144 1.00 189.55 ? 218 LYS H CG  1 
ATOM   2970 C CD  . LYS B 2 218 ? 40.302  -16.562 -78.945 1.00 206.99 ? 218 LYS H CD  1 
ATOM   2971 C CE  . LYS B 2 218 ? 40.870  -17.908 -79.358 1.00 215.84 ? 218 LYS H CE  1 
ATOM   2972 N NZ  . LYS B 2 218 ? 40.648  -18.192 -80.804 1.00 238.51 ? 218 LYS H NZ  1 
ATOM   2973 N N   . ARG B 2 219 ? 39.032  -14.978 -81.934 1.00 165.17 ? 219 ARG H N   1 
ATOM   2974 C CA  . ARG B 2 219 ? 38.638  -15.253 -83.315 1.00 173.91 ? 219 ARG H CA  1 
ATOM   2975 C C   . ARG B 2 219 ? 37.820  -16.496 -83.610 1.00 180.00 ? 219 ARG H C   1 
ATOM   2976 O O   . ARG B 2 219 ? 38.229  -17.600 -83.236 1.00 180.06 ? 219 ARG H O   1 
ATOM   2977 C CB  . ARG B 2 219 ? 39.921  -15.396 -84.136 1.00 30.00  ? 219 ARG H CB  1 
ATOM   2978 C CG  . ARG B 2 219 ? 40.725  -16.646 -83.818 1.00 30.00  ? 219 ARG H CG  1 
ATOM   2979 C CD  . ARG B 2 219 ? 42.047  -16.741 -84.563 1.00 30.00  ? 219 ARG H CD  1 
ATOM   2980 N NE  . ARG B 2 219 ? 42.759  -17.979 -84.260 1.00 30.00  ? 219 ARG H NE  1 
ATOM   2981 C CZ  . ARG B 2 219 ? 43.526  -18.155 -83.194 1.00 30.00  ? 219 ARG H CZ  1 
ATOM   2982 N NH1 . ARG B 2 219 ? 43.683  -17.172 -82.317 1.00 30.00  ? 219 ARG H NH1 1 
ATOM   2983 N NH2 . ARG B 2 219 ? 44.138  -19.316 -82.998 1.00 30.00  ? 219 ARG H NH2 1 
ATOM   2984 N N   . VAL B 2 220 ? 36.651  -16.315 -84.221 1.00 184.00 ? 220 VAL H N   1 
ATOM   2985 C CA  . VAL B 2 220 ? 35.766  -17.414 -84.589 1.00 184.19 ? 220 VAL H CA  1 
ATOM   2986 C C   . VAL B 2 220 ? 36.067  -17.728 -86.045 1.00 183.76 ? 220 VAL H C   1 
ATOM   2987 O O   . VAL B 2 220 ? 35.959  -16.851 -86.911 1.00 181.83 ? 220 VAL H O   1 
ATOM   2988 C CB  . VAL B 2 220 ? 34.254  -17.228 -84.377 1.00 179.26 ? 220 VAL H CB  1 
ATOM   2989 C CG1 . VAL B 2 220 ? 33.526  -18.563 -84.495 1.00 173.18 ? 220 VAL H CG1 1 
ATOM   2990 C CG2 . VAL B 2 220 ? 33.982  -16.562 -83.053 1.00 182.53 ? 220 VAL H CG2 1 
ATOM   2991 N N   . GLU B 2 221 ? 36.430  -18.978 -86.320 1.00 187.80 ? 221 GLU H N   1 
ATOM   2992 C CA  . GLU B 2 221 ? 36.835  -19.367 -87.658 1.00 198.64 ? 221 GLU H CA  1 
ATOM   2993 C C   . GLU B 2 221 ? 35.974  -20.535 -88.124 1.00 199.90 ? 221 GLU H C   1 
ATOM   2994 O O   . GLU B 2 221 ? 35.758  -21.490 -87.358 1.00 184.91 ? 221 GLU H O   1 
ATOM   2995 C CB  . GLU B 2 221 ? 38.321  -19.738 -87.684 1.00 193.47 ? 221 GLU H CB  1 
ATOM   2996 C CG  . GLU B 2 221 ? 39.238  -18.533 -87.789 1.00 189.90 ? 221 GLU H CG  1 
ATOM   2997 C CD  . GLU B 2 221 ? 39.193  -17.886 -89.156 1.00 192.36 ? 221 GLU H CD  1 
ATOM   2998 O OE1 . GLU B 2 221 ? 39.983  -18.293 -90.034 1.00 195.20 ? 221 GLU H OE1 1 
ATOM   2999 O OE2 . GLU B 2 221 ? 38.367  -16.968 -89.352 1.00 192.09 ? 221 GLU H OE2 1 
ATOM   3000 N N   . PRO B 2 222 ? 35.413  -20.512 -89.361 1.00 204.01 ? 222 PRO H N   1 
ATOM   3001 C CA  . PRO B 2 222 ? 34.477  -21.559 -89.796 1.00 183.04 ? 222 PRO H CA  1 
ATOM   3002 C C   . PRO B 2 222 ? 35.139  -22.839 -90.328 1.00 185.48 ? 222 PRO H C   1 
ATOM   3003 O O   . PRO B 2 222 ? 34.975  -23.135 -91.498 1.00 210.25 ? 222 PRO H O   1 
ATOM   3004 C CB  . PRO B 2 222 ? 33.705  -20.869 -90.932 1.00 182.83 ? 222 PRO H CB  1 
ATOM   3005 C CG  . PRO B 2 222 ? 34.728  -19.956 -91.566 1.00 188.73 ? 222 PRO H CG  1 
ATOM   3006 C CD  . PRO B 2 222 ? 35.624  -19.515 -90.427 1.00 193.81 ? 222 PRO H CD  1 
ATOM   3007 N N   . LYS B 2 223 ? 35.848  -23.571 -89.465 1.00 171.38 ? 223 LYS H N   1 
ATOM   3008 C CA  . LYS B 2 223 ? 36.440  -24.868 -89.890 1.00 191.06 ? 223 LYS H CA  1 
ATOM   3009 C C   . LYS B 2 223 ? 35.302  -25.850 -90.191 1.00 204.10 ? 223 LYS H C   1 
ATOM   3010 O O   . LYS B 2 223 ? 34.435  -26.036 -89.316 1.00 202.49 ? 223 LYS H O   1 
ATOM   3011 C CB  . LYS B 2 223 ? 37.373  -25.418 -88.806 1.00 178.28 ? 223 LYS H CB  1 
ATOM   3012 C CG  . LYS B 2 223 ? 37.815  -26.862 -89.003 1.00 170.36 ? 223 LYS H CG  1 
ATOM   3013 C CD  . LYS B 2 223 ? 38.487  -27.109 -90.337 1.00 176.52 ? 223 LYS H CD  1 
ATOM   3014 C CE  . LYS B 2 223 ? 38.732  -28.577 -90.612 1.00 170.18 ? 223 LYS H CE  1 
ATOM   3015 N NZ  . LYS B 2 223 ? 39.270  -28.797 -91.975 1.00 184.93 ? 223 LYS H NZ  1 
ATOM   3016 N N   . SER B 2 224 ? 35.307  -26.446 -91.386 1.00 215.88 ? 224 SER H N   1 
ATOM   3017 C CA  . SER B 2 224 ? 34.239  -27.406 -91.772 1.00 220.06 ? 224 SER H CA  1 
ATOM   3018 C C   . SER B 2 224 ? 34.848  -28.787 -92.034 1.00 241.61 ? 224 SER H C   1 
ATOM   3019 O O   . SER B 2 224 ? 35.834  -28.860 -92.793 1.00 251.74 ? 224 SER H O   1 
ATOM   3020 C CB  . SER B 2 224 ? 33.474  -26.907 -92.969 1.00 231.33 ? 224 SER H CB  1 
ATOM   3021 O OG  . SER B 2 224 ? 34.337  -26.747 -94.086 1.00 264.69 ? 224 SER H OG  1 
ATOM   3022 N N   . ASP C 3 1   ? 8.268   -23.390 -35.495 1.00 108.12 ? 1   ASP L N   1 
ATOM   3023 C CA  . ASP C 3 1   ? 8.708   -23.189 -36.871 1.00 135.80 ? 1   ASP L CA  1 
ATOM   3024 C C   . ASP C 3 1   ? 7.502   -23.201 -37.817 1.00 156.25 ? 1   ASP L C   1 
ATOM   3025 O O   . ASP C 3 1   ? 6.453   -23.754 -37.484 1.00 155.73 ? 1   ASP L O   1 
ATOM   3026 C CB  . ASP C 3 1   ? 9.723   -24.265 -37.271 1.00 128.69 ? 1   ASP L CB  1 
ATOM   3027 C CG  . ASP C 3 1   ? 10.303  -24.035 -38.654 1.00 135.89 ? 1   ASP L CG  1 
ATOM   3028 O OD1 . ASP C 3 1   ? 10.511  -22.859 -39.020 1.00 116.11 ? 1   ASP L OD1 1 
ATOM   3029 O OD2 . ASP C 3 1   ? 10.542  -25.025 -39.379 0.21 131.97 ? 1   ASP L OD2 1 
ATOM   3030 N N   . VAL C 3 2   ? 7.655   -22.591 -38.992 1.00 146.57 ? 2   VAL L N   1 
ATOM   3031 C CA  . VAL C 3 2   ? 6.583   -22.449 -39.971 1.00 125.64 ? 2   VAL L CA  1 
ATOM   3032 C C   . VAL C 3 2   ? 6.973   -23.204 -41.234 1.00 129.33 ? 2   VAL L C   1 
ATOM   3033 O O   . VAL C 3 2   ? 8.148   -23.228 -41.615 1.00 123.32 ? 2   VAL L O   1 
ATOM   3034 C CB  . VAL C 3 2   ? 6.303   -20.962 -40.281 1.00 126.77 ? 2   VAL L CB  1 
ATOM   3035 C CG1 . VAL C 3 2   ? 5.247   -20.810 -41.375 1.00 129.48 ? 2   VAL L CG1 1 
ATOM   3036 C CG2 . VAL C 3 2   ? 5.884   -20.233 -39.023 1.00 130.79 ? 2   VAL L CG2 1 
ATOM   3037 N N   . VAL C 3 3   ? 5.987   -23.822 -41.882 1.00 132.62 ? 3   VAL L N   1 
ATOM   3038 C CA  . VAL C 3 3   ? 6.190   -24.546 -43.131 1.00 124.17 ? 3   VAL L CA  1 
ATOM   3039 C C   . VAL C 3 3   ? 5.240   -23.958 -44.165 1.00 119.46 ? 3   VAL L C   1 
ATOM   3040 O O   . VAL C 3 3   ? 4.018   -24.143 -44.075 1.00 115.41 ? 3   VAL L O   1 
ATOM   3041 C CB  . VAL C 3 3   ? 5.960   -26.055 -42.969 1.00 118.76 ? 3   VAL L CB  1 
ATOM   3042 C CG1 . VAL C 3 3   ? 5.903   -26.730 -44.331 1.00 116.67 ? 3   VAL L CG1 1 
ATOM   3043 C CG2 . VAL C 3 3   ? 7.052   -26.666 -42.110 1.00 116.59 ? 3   VAL L CG2 1 
ATOM   3044 N N   . MET C 3 4   ? 5.794   -23.247 -45.144 1.00 93.23  ? 4   MET L N   1 
ATOM   3045 C CA  . MET C 3 4   ? 5.026   -22.698 -46.257 1.00 107.64 ? 4   MET L CA  1 
ATOM   3046 C C   . MET C 3 4   ? 5.139   -23.655 -47.437 1.00 112.27 ? 4   MET L C   1 
ATOM   3047 O O   . MET C 3 4   ? 6.188   -23.732 -48.085 1.00 123.06 ? 4   MET L O   1 
ATOM   3048 C CB  . MET C 3 4   ? 5.520   -21.305 -46.643 1.00 126.81 ? 4   MET L CB  1 
ATOM   3049 C CG  . MET C 3 4   ? 5.397   -20.252 -45.553 1.00 127.34 ? 4   MET L CG  1 
ATOM   3050 S SD  . MET C 3 4   ? 3.776   -20.210 -44.770 1.00 117.74 ? 4   MET L SD  1 
ATOM   3051 C CE  . MET C 3 4   ? 2.771   -19.617 -46.129 1.00 132.28 ? 4   MET L CE  1 
ATOM   3052 N N   . THR C 3 5   ? 4.064   -24.380 -47.713 1.00 113.31 ? 5   THR L N   1 
ATOM   3053 C CA  . THR C 3 5   ? 4.007   -25.304 -48.837 1.00 121.96 ? 5   THR L CA  1 
ATOM   3054 C C   . THR C 3 5   ? 3.352   -24.588 -50.010 1.00 121.92 ? 5   THR L C   1 
ATOM   3055 O O   . THR C 3 5   ? 2.292   -23.973 -49.850 1.00 120.08 ? 5   THR L O   1 
ATOM   3056 C CB  . THR C 3 5   ? 3.204   -26.551 -48.467 1.00 121.32 ? 5   THR L CB  1 
ATOM   3057 O OG1 . THR C 3 5   ? 1.874   -26.169 -48.090 1.00 148.66 ? 5   THR L OG1 1 
ATOM   3058 C CG2 . THR C 3 5   ? 3.863   -27.284 -47.310 1.00 86.32  ? 5   THR L CG2 1 
ATOM   3059 N N   . GLN C 3 6   ? 4.073   -24.553 -51.133 1.00 105.16 ? 6   GLN L N   1 
ATOM   3060 C CA  . GLN C 3 6   ? 3.549   -23.911 -52.363 1.00 125.91 ? 6   GLN L CA  1 
ATOM   3061 C C   . GLN C 3 6   ? 3.093   -25.045 -53.275 1.00 133.82 ? 6   GLN L C   1 
ATOM   3062 O O   . GLN C 3 6   ? 3.968   -25.762 -53.789 1.00 135.68 ? 6   GLN L O   1 
ATOM   3063 C CB  . GLN C 3 6   ? 4.643   -23.070 -53.017 1.00 123.98 ? 6   GLN L CB  1 
ATOM   3064 C CG  . GLN C 3 6   ? 4.215   -21.645 -53.326 1.00 119.79 ? 6   GLN L CG  1 
ATOM   3065 C CD  . GLN C 3 6   ? 5.353   -20.670 -53.156 1.00 136.20 ? 6   GLN L CD  1 
ATOM   3066 O OE1 . GLN C 3 6   ? 5.806   -20.408 -52.045 1.00 138.59 ? 6   GLN L OE1 1 
ATOM   3067 N NE2 . GLN C 3 6   ? 5.831   -20.123 -54.261 1.00 165.40 ? 6   GLN L NE2 1 
ATOM   3068 N N   . SER C 3 7   ? 1.784   -25.207 -53.461 1.00 131.69 ? 7   SER L N   1 
ATOM   3069 C CA  . SER C 3 7   ? 1.291   -26.388 -54.220 1.00 128.40 ? 7   SER L CA  1 
ATOM   3070 C C   . SER C 3 7   ? 1.733   -26.375 -55.685 1.00 153.53 ? 7   SER L C   1 
ATOM   3071 O O   . SER C 3 7   ? 2.443   -27.317 -56.077 1.00 162.34 ? 7   SER L O   1 
ATOM   3072 C CB  . SER C 3 7   ? -0.202  -26.545 -54.098 1.00 125.30 ? 7   SER L CB  1 
ATOM   3073 O OG  . SER C 3 7   ? -0.673  -25.945 -52.901 1.00 141.24 ? 7   SER L OG  1 
ATOM   3074 N N   . PRO C 3 8   ? 1.380   -25.378 -56.521 1.00 142.69 ? 8   PRO L N   1 
ATOM   3075 C CA  . PRO C 3 8   ? 1.690   -25.456 -57.947 1.00 133.02 ? 8   PRO L CA  1 
ATOM   3076 C C   . PRO C 3 8   ? 3.061   -24.862 -58.298 1.00 128.96 ? 8   PRO L C   1 
ATOM   3077 O O   . PRO C 3 8   ? 3.117   -23.777 -58.810 1.00 137.85 ? 8   PRO L O   1 
ATOM   3078 C CB  . PRO C 3 8   ? 0.517   -24.660 -58.529 1.00 157.30 ? 8   PRO L CB  1 
ATOM   3079 C CG  . PRO C 3 8   ? 0.193   -23.601 -57.490 1.00 158.23 ? 8   PRO L CG  1 
ATOM   3080 C CD  . PRO C 3 8   ? 0.746   -24.106 -56.175 1.00 143.80 ? 8   PRO L CD  1 
ATOM   3081 N N   . VAL C 3 9   ? 4.131   -25.608 -58.026 1.00 124.44 ? 9   VAL L N   1 
ATOM   3082 C CA  . VAL C 3 9   ? 5.504   -25.118 -58.339 1.00 125.79 ? 9   VAL L CA  1 
ATOM   3083 C C   . VAL C 3 9   ? 5.597   -24.835 -59.841 1.00 138.11 ? 9   VAL L C   1 
ATOM   3084 O O   . VAL C 3 9   ? 5.895   -23.687 -60.207 1.00 133.14 ? 9   VAL L O   1 
ATOM   3085 C CB  . VAL C 3 9   ? 6.570   -26.135 -57.893 1.00 111.09 ? 9   VAL L CB  1 
ATOM   3086 C CG1 . VAL C 3 9   ? 7.950   -25.779 -58.422 1.00 130.69 ? 9   VAL L CG1 1 
ATOM   3087 C CG2 . VAL C 3 9   ? 6.596   -26.286 -56.381 1.00 109.00 ? 9   VAL L CG2 1 
ATOM   3088 N N   . SER C 3 10  ? 5.343   -25.840 -60.678 1.00 147.09 ? 10  SER L N   1 
ATOM   3089 C CA  . SER C 3 10  ? 5.469   -25.665 -62.121 1.00 130.01 ? 10  SER L CA  1 
ATOM   3090 C C   . SER C 3 10  ? 4.117   -25.247 -62.685 1.00 128.36 ? 10  SER L C   1 
ATOM   3091 O O   . SER C 3 10  ? 3.146   -26.007 -62.603 1.00 156.20 ? 10  SER L O   1 
ATOM   3092 C CB  . SER C 3 10  ? 5.954   -26.953 -62.785 1.00 122.03 ? 10  SER L CB  1 
ATOM   3093 O OG  . SER C 3 10  ? 5.015   -28.003 -62.613 1.00 135.29 ? 10  SER L OG  1 
ATOM   3094 N N   . LEU C 3 11  ? 4.056   -24.045 -63.261 1.00 129.00 ? 11  LEU L N   1 
ATOM   3095 C CA  . LEU C 3 11  ? 2.810   -23.480 -63.784 1.00 147.51 ? 11  LEU L CA  1 
ATOM   3096 C C   . LEU C 3 11  ? 3.000   -22.859 -65.163 1.00 150.53 ? 11  LEU L C   1 
ATOM   3097 O O   . LEU C 3 11  ? 3.204   -21.644 -65.290 1.00 146.46 ? 11  LEU L O   1 
ATOM   3098 C CB  . LEU C 3 11  ? 2.222   -22.451 -62.821 1.00 160.63 ? 11  LEU L CB  1 
ATOM   3099 C CG  . LEU C 3 11  ? 1.678   -23.024 -61.518 1.00 164.44 ? 11  LEU L CG  1 
ATOM   3100 C CD1 . LEU C 3 11  ? 1.279   -21.922 -60.560 1.00 169.24 ? 11  LEU L CD1 1 
ATOM   3101 C CD2 . LEU C 3 11  ? 0.482   -23.883 -61.860 1.00 152.23 ? 11  LEU L CD2 1 
ATOM   3102 N N   . PRO C 3 12  ? 2.932   -23.661 -66.219 1.00 156.27 ? 12  PRO L N   1 
ATOM   3103 C CA  . PRO C 3 12  ? 2.788   -23.085 -67.560 1.00 148.75 ? 12  PRO L CA  1 
ATOM   3104 C C   . PRO C 3 12  ? 1.377   -22.553 -67.771 1.00 143.61 ? 12  PRO L C   1 
ATOM   3105 O O   . PRO C 3 12  ? 0.392   -23.159 -67.342 1.00 160.39 ? 12  PRO L O   1 
ATOM   3106 C CB  . PRO C 3 12  ? 3.097   -24.264 -68.490 1.00 163.94 ? 12  PRO L CB  1 
ATOM   3107 C CG  . PRO C 3 12  ? 2.810   -25.476 -67.664 1.00 164.07 ? 12  PRO L CG  1 
ATOM   3108 C CD  . PRO C 3 12  ? 3.175   -25.112 -66.260 1.00 168.70 ? 12  PRO L CD  1 
ATOM   3109 N N   . VAL C 3 13  ? 1.290   -21.397 -68.430 1.00 152.51 ? 13  VAL L N   1 
ATOM   3110 C CA  . VAL C 3 13  ? 0.028   -20.711 -68.672 1.00 161.71 ? 13  VAL L CA  1 
ATOM   3111 C C   . VAL C 3 13  ? 0.032   -20.284 -70.135 1.00 168.81 ? 13  VAL L C   1 
ATOM   3112 O O   . VAL C 3 13  ? 1.065   -20.318 -70.804 1.00 170.42 ? 13  VAL L O   1 
ATOM   3113 C CB  . VAL C 3 13  ? -0.148  -19.502 -67.706 1.00 145.34 ? 13  VAL L CB  1 
ATOM   3114 C CG1 . VAL C 3 13  ? -1.437  -18.722 -67.962 1.00 145.11 ? 13  VAL L CG1 1 
ATOM   3115 C CG2 . VAL C 3 13  ? -0.095  -19.964 -66.256 1.00 148.61 ? 13  VAL L CG2 1 
ATOM   3116 N N   . THR C 3 14  ? -1.146  -19.940 -70.650 1.00 162.48 ? 14  THR L N   1 
ATOM   3117 C CA  . THR C 3 14  ? -1.287  -19.285 -71.943 1.00 153.84 ? 14  THR L CA  1 
ATOM   3118 C C   . THR C 3 14  ? -1.772  -17.857 -71.726 1.00 160.11 ? 14  THR L C   1 
ATOM   3119 O O   . THR C 3 14  ? -2.586  -17.604 -70.834 1.00 168.89 ? 14  THR L O   1 
ATOM   3120 C CB  . THR C 3 14  ? -2.266  -20.039 -72.849 1.00 155.51 ? 14  THR L CB  1 
ATOM   3121 O OG1 . THR C 3 14  ? -3.599  -19.884 -72.348 1.00 157.65 ? 14  THR L OG1 1 
ATOM   3122 C CG2 . THR C 3 14  ? -1.922  -21.515 -72.896 1.00 175.37 ? 14  THR L CG2 1 
ATOM   3123 N N   . LEU C 3 15  ? -1.242  -16.922 -72.519 1.00 154.13 ? 15  LEU L N   1 
ATOM   3124 C CA  . LEU C 3 15  ? -1.586  -15.483 -72.343 1.00 150.07 ? 15  LEU L CA  1 
ATOM   3125 C C   . LEU C 3 15  ? -3.088  -15.314 -72.087 1.00 160.77 ? 15  LEU L C   1 
ATOM   3126 O O   . LEU C 3 15  ? -3.886  -15.836 -72.891 1.00 180.68 ? 15  LEU L O   1 
ATOM   3127 C CB  . LEU C 3 15  ? -1.151  -14.721 -73.599 1.00 146.95 ? 15  LEU L CB  1 
ATOM   3128 C CG  . LEU C 3 15  ? 0.355   -14.693 -73.854 1.00 157.83 ? 15  LEU L CG  1 
ATOM   3129 C CD1 . LEU C 3 15  ? 0.691   -13.768 -75.013 1.00 147.79 ? 15  LEU L CD1 1 
ATOM   3130 C CD2 . LEU C 3 15  ? 1.108   -14.269 -72.602 1.00 177.00 ? 15  LEU L CD2 1 
ATOM   3131 N N   . GLY C 3 16  ? -3.451  -14.596 -71.019 1.00 154.99 ? 16  GLY L N   1 
ATOM   3132 C CA  . GLY C 3 16  ? -4.873  -14.328 -70.726 1.00 170.11 ? 16  GLY L CA  1 
ATOM   3133 C C   . GLY C 3 16  ? -5.567  -15.509 -70.071 1.00 166.32 ? 16  GLY L C   1 
ATOM   3134 O O   . GLY C 3 16  ? -6.792  -15.645 -70.260 1.00 159.54 ? 16  GLY L O   1 
ATOM   3135 N N   . GLN C 3 17  ? -4.823  -16.335 -69.328 1.00 164.03 ? 17  GLN L N   1 
ATOM   3136 C CA  . GLN C 3 17  ? -5.439  -17.477 -68.600 1.00 160.70 ? 17  GLN L CA  1 
ATOM   3137 C C   . GLN C 3 17  ? -5.260  -17.268 -67.091 1.00 149.91 ? 17  GLN L C   1 
ATOM   3138 O O   . GLN C 3 17  ? -4.205  -17.659 -66.557 1.00 158.79 ? 17  GLN L O   1 
ATOM   3139 C CB  . GLN C 3 17  ? -4.822  -18.799 -69.058 1.00 158.32 ? 17  GLN L CB  1 
ATOM   3140 C CG  . GLN C 3 17  ? -5.301  -20.006 -68.266 1.00 160.67 ? 17  GLN L CG  1 
ATOM   3141 C CD  . GLN C 3 17  ? -4.461  -21.229 -68.538 1.00 164.23 ? 17  GLN L CD  1 
ATOM   3142 O OE1 . GLN C 3 17  ? -3.549  -21.212 -69.362 1.00 155.49 ? 17  GLN L OE1 1 
ATOM   3143 N NE2 . GLN C 3 17  ? -4.770  -22.310 -67.841 1.00 170.25 ? 17  GLN L NE2 1 
ATOM   3144 N N   . PRO C 3 18  ? -6.245  -16.673 -66.383 1.00 152.45 ? 18  PRO L N   1 
ATOM   3145 C CA  . PRO C 3 18  ? -6.114  -16.421 -64.960 1.00 165.55 ? 18  PRO L CA  1 
ATOM   3146 C C   . PRO C 3 18  ? -5.645  -17.740 -64.350 1.00 163.95 ? 18  PRO L C   1 
ATOM   3147 O O   . PRO C 3 18  ? -6.315  -18.735 -64.556 1.00 170.75 ? 18  PRO L O   1 
ATOM   3148 C CB  . PRO C 3 18  ? -7.532  -15.964 -64.543 1.00 178.93 ? 18  PRO L CB  1 
ATOM   3149 C CG  . PRO C 3 18  ? -8.107  -15.374 -65.811 1.00 172.59 ? 18  PRO L CG  1 
ATOM   3150 C CD  . PRO C 3 18  ? -7.527  -16.218 -66.926 1.00 165.74 ? 18  PRO L CD  1 
ATOM   3151 N N   . ALA C 3 19  ? -4.514  -17.729 -63.637 1.00 153.28 ? 19  ALA L N   1 
ATOM   3152 C CA  . ALA C 3 19  ? -4.009  -18.954 -63.016 1.00 167.30 ? 19  ALA L CA  1 
ATOM   3153 C C   . ALA C 3 19  ? -3.777  -18.508 -61.560 1.00 177.40 ? 19  ALA L C   1 
ATOM   3154 O O   . ALA C 3 19  ? -3.684  -17.316 -61.256 1.00 163.45 ? 19  ALA L O   1 
ATOM   3155 C CB  . ALA C 3 19  ? -2.744  -19.555 -63.608 1.00 141.89 ? 19  ALA L CB  1 
ATOM   3156 N N   . SER C 3 20  ? -3.674  -19.495 -60.662 1.00 179.58 ? 20  SER L N   1 
ATOM   3157 C CA  . SER C 3 20  ? -3.594  -19.250 -59.226 1.00 173.01 ? 20  SER L CA  1 
ATOM   3158 C C   . SER C 3 20  ? -2.429  -20.016 -58.609 1.00 169.64 ? 20  SER L C   1 
ATOM   3159 O O   . SER C 3 20  ? -2.077  -21.111 -59.058 1.00 158.82 ? 20  SER L O   1 
ATOM   3160 C CB  . SER C 3 20  ? -4.907  -19.637 -58.519 1.00 186.94 ? 20  SER L CB  1 
ATOM   3161 O OG  . SER C 3 20  ? -5.166  -21.027 -58.622 1.00 209.03 ? 20  SER L OG  1 
ATOM   3162 N N   . ILE C 3 21  ? -1.842  -19.431 -57.562 1.00 170.80 ? 21  ILE L N   1 
ATOM   3163 C CA  . ILE C 3 21  ? -0.721  -20.012 -56.822 1.00 154.05 ? 21  ILE L CA  1 
ATOM   3164 C C   . ILE C 3 21  ? -1.133  -20.122 -55.361 1.00 160.61 ? 21  ILE L C   1 
ATOM   3165 O O   . ILE C 3 21  ? -1.490  -19.115 -54.737 1.00 161.79 ? 21  ILE L O   1 
ATOM   3166 C CB  . ILE C 3 21  ? 0.549   -19.157 -56.958 1.00 148.94 ? 21  ILE L CB  1 
ATOM   3167 C CG1 . ILE C 3 21  ? 1.032   -19.139 -58.405 1.00 155.04 ? 21  ILE L CG1 1 
ATOM   3168 C CG2 . ILE C 3 21  ? 1.654   -19.678 -56.043 1.00 144.10 ? 21  ILE L CG2 1 
ATOM   3169 C CD1 . ILE C 3 21  ? 2.108   -18.116 -58.676 1.00 169.25 ? 21  ILE L CD1 1 
ATOM   3170 N N   . SER C 3 22  ? -1.063  -21.331 -54.807 1.00 156.80 ? 22  SER L N   1 
ATOM   3171 C CA  . SER C 3 22  ? -1.566  -21.603 -53.465 1.00 144.17 ? 22  SER L CA  1 
ATOM   3172 C C   . SER C 3 22  ? -0.418  -21.725 -52.469 1.00 123.93 ? 22  SER L C   1 
ATOM   3173 O O   . SER C 3 22  ? 0.531   -22.485 -52.694 1.00 113.08 ? 22  SER L O   1 
ATOM   3174 C CB  . SER C 3 22  ? -2.411  -22.878 -53.450 1.00 146.69 ? 22  SER L CB  1 
ATOM   3175 O OG  . SER C 3 22  ? -1.743  -23.942 -54.101 1.00 148.93 ? 22  SER L OG  1 
ATOM   3176 N N   . CYS C 3 23  ? -0.513  -20.976 -51.372 1.00 131.46 ? 23  CYS L N   1 
ATOM   3177 C CA  . CYS C 3 23  ? 0.407   -21.071 -50.245 1.00 127.59 ? 23  CYS L CA  1 
ATOM   3178 C C   . CYS C 3 23  ? -0.348  -21.596 -49.033 1.00 106.00 ? 23  CYS L C   1 
ATOM   3179 O O   . CYS C 3 23  ? -1.394  -21.050 -48.665 1.00 102.90 ? 23  CYS L O   1 
ATOM   3180 C CB  . CYS C 3 23  ? 1.036   -19.714 -49.919 1.00 143.01 ? 23  CYS L CB  1 
ATOM   3181 S SG  . CYS C 3 23  ? 2.369   -19.189 -51.019 1.00 201.24 ? 23  CYS L SG  1 
ATOM   3182 N N   . ARG C 3 24  ? 0.177   -22.650 -48.417 1.00 103.45 ? 24  ARG L N   1 
ATOM   3183 C CA  . ARG C 3 24  ? -0.460  -23.259 -47.258 1.00 119.94 ? 24  ARG L CA  1 
ATOM   3184 C C   . ARG C 3 24  ? 0.514   -23.270 -46.092 1.00 114.60 ? 24  ARG L C   1 
ATOM   3185 O O   . ARG C 3 24  ? 1.658   -23.715 -46.233 1.00 110.00 ? 24  ARG L O   1 
ATOM   3186 C CB  . ARG C 3 24  ? -0.951  -24.677 -47.564 1.00 137.68 ? 24  ARG L CB  1 
ATOM   3187 C CG  . ARG C 3 24  ? -1.577  -24.837 -48.943 1.00 150.46 ? 24  ARG L CG  1 
ATOM   3188 C CD  . ARG C 3 24  ? -1.538  -26.280 -49.411 1.00 169.87 ? 24  ARG L CD  1 
ATOM   3189 N NE  . ARG C 3 24  ? -2.309  -27.136 -48.518 1.00 174.33 ? 24  ARG L NE  1 
ATOM   3190 C CZ  . ARG C 3 24  ? -2.758  -28.344 -48.832 1.00 166.59 ? 24  ARG L CZ  1 
ATOM   3191 N NH1 . ARG C 3 24  ? -2.524  -28.883 -50.018 1.00 170.13 ? 24  ARG L NH1 1 
ATOM   3192 N NH2 . ARG C 3 24  ? -3.467  -29.026 -47.937 1.00 162.73 ? 24  ARG L NH2 1 
ATOM   3193 N N   . SER C 3 25  ? 0.052   -22.784 -44.947 1.00 111.84 ? 25  SER L N   1 
ATOM   3194 C CA  . SER C 3 25  ? 0.872   -22.628 -43.759 1.00 99.70  ? 25  SER L CA  1 
ATOM   3195 C C   . SER C 3 25  ? 0.617   -23.757 -42.768 1.00 116.21 ? 25  SER L C   1 
ATOM   3196 O O   . SER C 3 25  ? -0.411  -24.440 -42.812 1.00 119.16 ? 25  SER L O   1 
ATOM   3197 C CB  . SER C 3 25  ? 0.593   -21.277 -43.097 1.00 89.52  ? 25  SER L CB  1 
ATOM   3198 O OG  . SER C 3 25  ? -0.540  -21.354 -42.250 1.00 109.38 ? 25  SER L OG  1 
ATOM   3199 N N   . SER C 3 26  ? 1.581   -23.946 -41.865 1.00 114.54 ? 26  SER L N   1 
ATOM   3200 C CA  . SER C 3 26  ? 1.429   -24.929 -40.798 1.00 125.63 ? 26  SER L CA  1 
ATOM   3201 C C   . SER C 3 26  ? 0.586   -24.393 -39.649 1.00 126.29 ? 26  SER L C   1 
ATOM   3202 O O   . SER C 3 26  ? -0.133  -25.162 -39.001 1.00 133.91 ? 26  SER L O   1 
ATOM   3203 C CB  . SER C 3 26  ? 2.802   -25.360 -40.278 1.00 132.99 ? 26  SER L CB  1 
ATOM   3204 O OG  . SER C 3 26  ? 3.488   -24.273 -39.680 1.00 138.48 ? 26  SER L OG  1 
ATOM   3205 N N   . GLN C 3 27  ? 0.659   -23.092 -39.383 1.00 122.87 ? 27  GLN L N   1 
ATOM   3206 C CA  . GLN C 3 27  ? -0.104  -22.457 -38.322 1.00 129.15 ? 27  GLN L CA  1 
ATOM   3207 C C   . GLN C 3 27  ? -0.769  -21.202 -38.872 1.00 119.29 ? 27  GLN L C   1 
ATOM   3208 O O   . GLN C 3 27  ? -0.397  -20.698 -39.935 1.00 116.28 ? 27  GLN L O   1 
ATOM   3209 C CB  . GLN C 3 27  ? 0.793   -22.109 -37.124 1.00 131.84 ? 27  GLN L CB  1 
ATOM   3210 C CG  . GLN C 3 27  ? 1.349   -23.323 -36.390 1.00 136.55 ? 27  GLN L CG  1 
ATOM   3211 C CD  . GLN C 3 27  ? 2.302   -22.945 -35.271 1.00 159.62 ? 27  GLN L CD  1 
ATOM   3212 O OE1 . GLN C 3 27  ? 2.918   -21.880 -35.297 1.00 142.80 ? 27  GLN L OE1 1 
ATOM   3213 N NE2 . GLN C 3 27  ? 2.417   -23.815 -34.274 1.00 173.98 ? 27  GLN L NE2 1 
ATOM   3214 N N   . GLY C 3 28  ? -1.770  -20.706 -38.146 1.00 111.30 ? 28  GLY L N   1 
ATOM   3215 C CA  . GLY C 3 28  ? -2.401  -19.458 -38.536 1.00 121.05 ? 28  GLY L CA  1 
ATOM   3216 C C   . GLY C 3 28  ? -1.410  -18.309 -38.548 1.00 131.02 ? 28  GLY L C   1 
ATOM   3217 O O   . GLY C 3 28  ? -0.494  -18.242 -37.727 1.00 148.15 ? 28  GLY L O   1 
ATOM   3218 N N   . LEU C 3 29  ? -1.600  -17.387 -39.496 1.00 131.21 ? 29  LEU L N   1 
ATOM   3219 C CA  . LEU C 3 29  ? -0.631  -16.328 -39.766 1.00 129.00 ? 29  LEU L CA  1 
ATOM   3220 C C   . LEU C 3 29  ? -1.142  -14.938 -39.383 1.00 127.00 ? 29  LEU L C   1 
ATOM   3221 O O   . LEU C 3 29  ? -0.762  -13.941 -40.001 1.00 124.14 ? 29  LEU L O   1 
ATOM   3222 C CB  . LEU C 3 29  ? -0.214  -16.357 -41.236 1.00 124.73 ? 29  LEU L CB  1 
ATOM   3223 C CG  . LEU C 3 29  ? 0.548   -17.619 -41.651 1.00 136.66 ? 29  LEU L CG  1 
ATOM   3224 C CD1 . LEU C 3 29  ? 1.055   -17.523 -43.079 1.00 143.56 ? 29  LEU L CD1 1 
ATOM   3225 C CD2 . LEU C 3 29  ? 1.697   -17.892 -40.691 1.00 133.88 ? 29  LEU L CD2 1 
ATOM   3226 N N   . VAL C 3 30  ? -1.986  -14.854 -38.354 1.00 124.31 ? 30  VAL L N   1 
ATOM   3227 C CA  . VAL C 3 30  ? -2.473  -13.577 -37.840 1.00 112.06 ? 30  VAL L CA  1 
ATOM   3228 C C   . VAL C 3 30  ? -1.442  -13.070 -36.838 1.00 115.58 ? 30  VAL L C   1 
ATOM   3229 O O   . VAL C 3 30  ? -0.590  -13.838 -36.380 1.00 129.56 ? 30  VAL L O   1 
ATOM   3230 C CB  . VAL C 3 30  ? -3.876  -13.740 -37.216 1.00 104.36 ? 30  VAL L CB  1 
ATOM   3231 C CG1 . VAL C 3 30  ? -4.397  -12.435 -36.612 1.00 97.41  ? 30  VAL L CG1 1 
ATOM   3232 C CG2 . VAL C 3 30  ? -4.849  -14.280 -38.248 1.00 127.21 ? 30  VAL L CG2 1 
ATOM   3233 N N   . TYR C 3 31  ? -1.489  -11.784 -36.494 1.00 104.21 ? 31  TYR L N   1 
ATOM   3234 C CA  . TYR C 3 31  ? -0.513  -11.209 -35.582 1.00 109.22 ? 31  TYR L CA  1 
ATOM   3235 C C   . TYR C 3 31  ? -1.234  -10.277 -34.612 1.00 93.66  ? 31  TYR L C   1 
ATOM   3236 O O   . TYR C 3 31  ? -2.418  -9.966  -34.779 1.00 79.87  ? 31  TYR L O   1 
ATOM   3237 C CB  . TYR C 3 31  ? 0.598   -10.487 -36.362 1.00 109.89 ? 31  TYR L CB  1 
ATOM   3238 C CG  . TYR C 3 31  ? 1.875   -10.229 -35.584 1.00 108.16 ? 31  TYR L CG  1 
ATOM   3239 C CD1 . TYR C 3 31  ? 2.584   -11.274 -35.005 1.00 123.64 ? 31  TYR L CD1 1 
ATOM   3240 C CD2 . TYR C 3 31  ? 2.382   -8.943  -35.447 1.00 118.74 ? 31  TYR L CD2 1 
ATOM   3241 C CE1 . TYR C 3 31  ? 3.756   -11.044 -34.296 1.00 129.08 ? 31  TYR L CE1 1 
ATOM   3242 C CE2 . TYR C 3 31  ? 3.555   -8.704  -34.740 1.00 127.75 ? 31  TYR L CE2 1 
ATOM   3243 C CZ  . TYR C 3 31  ? 4.237   -9.757  -34.167 1.00 119.56 ? 31  TYR L CZ  1 
ATOM   3244 O OH  . TYR C 3 31  ? 5.401   -9.527  -33.465 1.00 100.08 ? 31  TYR L OH  1 
ATOM   3245 N N   . ILE C 3 32  ? -0.503  -9.840  -33.581 1.00 96.26  ? 32  ILE L N   1 
ATOM   3246 C CA  . ILE C 3 32  ? -1.078  -8.990  -32.537 1.00 89.26  ? 32  ILE L CA  1 
ATOM   3247 C C   . ILE C 3 32  ? -1.656  -7.713  -33.132 1.00 104.27 ? 32  ILE L C   1 
ATOM   3248 O O   . ILE C 3 32  ? -2.679  -7.200  -32.658 1.00 100.77 ? 32  ILE L O   1 
ATOM   3249 C CB  . ILE C 3 32  ? -0.016  -8.686  -31.464 1.00 83.04  ? 32  ILE L CB  1 
ATOM   3250 C CG1 . ILE C 3 32  ? 0.329   -9.962  -30.697 1.00 91.82  ? 32  ILE L CG1 1 
ATOM   3251 C CG2 . ILE C 3 32  ? -0.474  -7.576  -30.530 1.00 89.77  ? 32  ILE L CG2 1 
ATOM   3252 C CD1 . ILE C 3 32  ? 1.527   -9.825  -29.821 1.00 95.38  ? 32  ILE L CD1 1 
ATOM   3253 N N   . ASP C 3 33  ? -1.006  -7.176  -34.169 1.00 114.21 ? 33  ASP L N   1 
ATOM   3254 C CA  . ASP C 3 33  ? -1.525  -6.002  -34.867 1.00 110.36 ? 33  ASP L CA  1 
ATOM   3255 C C   . ASP C 3 33  ? -2.990  -6.184  -35.229 1.00 104.00 ? 33  ASP L C   1 
ATOM   3256 O O   . ASP C 3 33  ? -3.819  -5.295  -35.005 1.00 122.04 ? 33  ASP L O   1 
ATOM   3257 C CB  . ASP C 3 33  ? -0.709  -5.742  -36.132 1.00 126.78 ? 33  ASP L CB  1 
ATOM   3258 C CG  . ASP C 3 33  ? 0.680   -5.231  -35.838 1.00 163.09 ? 33  ASP L CG  1 
ATOM   3259 O OD1 . ASP C 3 33  ? 0.935   -4.778  -34.702 1.00 168.71 ? 33  ASP L OD1 1 
ATOM   3260 O OD2 . ASP C 3 33  ? 1.522   -5.302  -36.755 1.00 174.24 ? 33  ASP L OD2 1 
ATOM   3261 N N   . GLY C 3 34  ? -3.327  -7.338  -35.787 1.00 90.75  ? 34  GLY L N   1 
ATOM   3262 C CA  . GLY C 3 34  ? -4.695  -7.595  -36.163 1.00 93.47  ? 34  GLY L CA  1 
ATOM   3263 C C   . GLY C 3 34  ? -4.794  -8.147  -37.564 1.00 105.49 ? 34  GLY L C   1 
ATOM   3264 O O   . GLY C 3 34  ? -5.692  -8.940  -37.858 1.00 128.41 ? 34  GLY L O   1 
ATOM   3265 N N   . ASN C 3 35  ? -3.838  -7.756  -38.413 1.00 95.99  ? 35  ASN L N   1 
ATOM   3266 C CA  . ASN C 3 35  ? -3.891  -8.149  -39.843 1.00 112.48 ? 35  ASN L CA  1 
ATOM   3267 C C   . ASN C 3 35  ? -3.027  -9.382  -40.104 1.00 118.37 ? 35  ASN L C   1 
ATOM   3268 O O   . ASN C 3 35  ? -2.033  -9.563  -39.382 1.00 134.65 ? 35  ASN L O   1 
ATOM   3269 C CB  . ASN C 3 35  ? -3.419  -7.006  -40.740 1.00 95.38  ? 35  ASN L CB  1 
ATOM   3270 C CG  . ASN C 3 35  ? -4.397  -5.852  -40.803 1.00 122.06 ? 35  ASN L CG  1 
ATOM   3271 O OD1 . ASN C 3 35  ? -5.586  -6.024  -40.549 1.00 165.78 ? 35  ASN L OD1 1 
ATOM   3272 N ND2 . ASN C 3 35  ? -3.906  -4.672  -41.143 1.00 104.39 ? 35  ASN L ND2 1 
ATOM   3273 N N   . THR C 3 36  ? -3.392  -10.183 -41.107 1.00 119.30 ? 36  THR L N   1 
ATOM   3274 C CA  . THR C 3 36  ? -2.573  -11.362 -41.492 1.00 127.75 ? 36  THR L CA  1 
ATOM   3275 C C   . THR C 3 36  ? -1.360  -10.843 -42.269 1.00 132.65 ? 36  THR L C   1 
ATOM   3276 O O   . THR C 3 36  ? -1.406  -9.673  -42.678 1.00 137.93 ? 36  THR L O   1 
ATOM   3277 C CB  . THR C 3 36  ? -3.426  -12.351 -42.292 1.00 126.47 ? 36  THR L CB  1 
ATOM   3278 O OG1 . THR C 3 36  ? -4.670  -12.498 -41.609 1.00 124.32 ? 36  THR L OG1 1 
ATOM   3279 C CG2 . THR C 3 36  ? -2.776  -13.707 -42.466 1.00 125.25 ? 36  THR L CG2 1 
ATOM   3280 N N   . TYR C 3 37  ? -0.346  -11.680 -42.519 1.00 110.94 ? 37  TYR L N   1 
ATOM   3281 C CA  . TYR C 3 37  ? 0.885   -11.163 -43.178 1.00 125.05 ? 37  TYR L CA  1 
ATOM   3282 C C   . TYR C 3 37  ? 1.441   -12.124 -44.238 1.00 127.74 ? 37  TYR L C   1 
ATOM   3283 O O   . TYR C 3 37  ? 2.366   -12.891 -43.904 1.00 92.27  ? 37  TYR L O   1 
ATOM   3284 C CB  . TYR C 3 37  ? 1.957   -10.870 -42.125 1.00 116.97 ? 37  TYR L CB  1 
ATOM   3285 C CG  . TYR C 3 37  ? 1.744   -9.584  -41.368 1.00 137.23 ? 37  TYR L CG  1 
ATOM   3286 C CD1 . TYR C 3 37  ? 1.727   -8.365  -42.026 1.00 148.70 ? 37  TYR L CD1 1 
ATOM   3287 C CD2 . TYR C 3 37  ? 1.544   -9.582  -39.998 1.00 113.85 ? 37  TYR L CD2 1 
ATOM   3288 C CE1 . TYR C 3 37  ? 1.527   -7.178  -41.343 1.00 157.90 ? 37  TYR L CE1 1 
ATOM   3289 C CE2 . TYR C 3 37  ? 1.343   -8.404  -39.299 1.00 106.12 ? 37  TYR L CE2 1 
ATOM   3290 C CZ  . TYR C 3 37  ? 1.333   -7.197  -39.974 1.00 151.40 ? 37  TYR L CZ  1 
ATOM   3291 O OH  . TYR C 3 37  ? 1.134   -6.023  -39.289 1.00 149.62 ? 37  TYR L OH  1 
ATOM   3292 N N   . LEU C 3 38  ? 0.901   -12.062 -45.452 1.00 132.01 ? 38  LEU L N   1 
ATOM   3293 C CA  . LEU C 3 38  ? 1.397   -12.938 -46.540 1.00 131.55 ? 38  LEU L CA  1 
ATOM   3294 C C   . LEU C 3 38  ? 1.706   -12.083 -47.764 1.00 158.37 ? 38  LEU L C   1 
ATOM   3295 O O   . LEU C 3 38  ? 1.330   -12.490 -48.872 1.00 187.22 ? 38  LEU L O   1 
ATOM   3296 C CB  . LEU C 3 38  ? 0.330   -13.970 -46.891 1.00 144.13 ? 38  LEU L CB  1 
ATOM   3297 C CG  . LEU C 3 38  ? 0.427   -15.263 -46.095 1.00 143.65 ? 38  LEU L CG  1 
ATOM   3298 C CD1 . LEU C 3 38  ? -0.659  -15.292 -45.039 1.00 133.99 ? 38  LEU L CD1 1 
ATOM   3299 C CD2 . LEU C 3 38  ? 0.346   -16.471 -47.013 1.00 145.76 ? 38  LEU L CD2 1 
ATOM   3300 N N   . ASN C 3 39  ? 2.403   -10.971 -47.569 1.00 148.68 ? 39  ASN L N   1 
ATOM   3301 C CA  . ASN C 3 39  ? 2.766   -10.167 -48.758 1.00 154.35 ? 39  ASN L CA  1 
ATOM   3302 C C   . ASN C 3 39  ? 3.477   -11.041 -49.798 1.00 152.91 ? 39  ASN L C   1 
ATOM   3303 O O   . ASN C 3 39  ? 4.637   -11.420 -49.579 1.00 144.45 ? 39  ASN L O   1 
ATOM   3304 C CB  . ASN C 3 39  ? 3.518   -8.895  -48.384 1.00 162.69 ? 39  ASN L CB  1 
ATOM   3305 C CG  . ASN C 3 39  ? 4.796   -9.066  -47.599 1.00 172.99 ? 39  ASN L CG  1 
ATOM   3306 O OD1 . ASN C 3 39  ? 5.874   -9.124  -48.184 1.00 159.98 ? 39  ASN L OD1 1 
ATOM   3307 N ND2 . ASN C 3 39  ? 4.689   -9.045  -46.281 1.00 166.99 ? 39  ASN L ND2 1 
ATOM   3308 N N   . TRP C 3 40  ? 2.794   -11.319 -50.907 1.00 165.32 ? 40  TRP L N   1 
ATOM   3309 C CA  . TRP C 3 40  ? 3.381   -12.168 -51.973 1.00 132.86 ? 40  TRP L CA  1 
ATOM   3310 C C   . TRP C 3 40  ? 4.536   -11.427 -52.641 1.00 122.95 ? 40  TRP L C   1 
ATOM   3311 O O   . TRP C 3 40  ? 4.459   -10.195 -52.757 1.00 120.52 ? 40  TRP L O   1 
ATOM   3312 C CB  . TRP C 3 40  ? 2.317   -12.544 -53.005 1.00 158.12 ? 40  TRP L CB  1 
ATOM   3313 C CG  . TRP C 3 40  ? 1.155   -13.309 -52.454 1.00 178.97 ? 40  TRP L CG  1 
ATOM   3314 C CD1 . TRP C 3 40  ? 0.120   -12.821 -51.709 1.00 186.43 ? 40  TRP L CD1 1 
ATOM   3315 C CD2 . TRP C 3 40  ? 0.897   -14.712 -52.626 1.00 164.41 ? 40  TRP L CD2 1 
ATOM   3316 N NE1 . TRP C 3 40  ? -0.754  -13.825 -51.394 1.00 184.57 ? 40  TRP L NE1 1 
ATOM   3317 C CE2 . TRP C 3 40  ? -0.305  -14.996 -51.945 1.00 186.74 ? 40  TRP L CE2 1 
ATOM   3318 C CE3 . TRP C 3 40  ? 1.565   -15.751 -53.280 1.00 130.55 ? 40  TRP L CE3 1 
ATOM   3319 C CZ2 . TRP C 3 40  ? -0.847  -16.278 -51.900 1.00 174.24 ? 40  TRP L CZ2 1 
ATOM   3320 C CZ3 . TRP C 3 40  ? 1.021   -17.014 -53.245 1.00 130.20 ? 40  TRP L CZ3 1 
ATOM   3321 C CH2 . TRP C 3 40  ? -0.167  -17.272 -52.561 1.00 156.27 ? 40  TRP L CH2 1 
ATOM   3322 N N   . PHE C 3 41  ? 5.549   -12.165 -53.080 1.00 109.20 ? 41  PHE L N   1 
ATOM   3323 C CA  . PHE C 3 41  ? 6.702   -11.560 -53.788 1.00 114.86 ? 41  PHE L CA  1 
ATOM   3324 C C   . PHE C 3 41  ? 6.831   -12.135 -55.197 1.00 129.87 ? 41  PHE L C   1 
ATOM   3325 O O   . PHE C 3 41  ? 6.349   -13.257 -55.430 1.00 129.17 ? 41  PHE L O   1 
ATOM   3326 C CB  . PHE C 3 41  ? 8.010   -11.870 -53.066 1.00 128.59 ? 41  PHE L CB  1 
ATOM   3327 C CG  . PHE C 3 41  ? 8.288   -11.044 -51.840 1.00 134.68 ? 41  PHE L CG  1 
ATOM   3328 C CD1 . PHE C 3 41  ? 8.342   -9.664  -51.914 1.00 111.73 ? 41  PHE L CD1 1 
ATOM   3329 C CD2 . PHE C 3 41  ? 8.528   -11.653 -50.621 1.00 161.37 ? 41  PHE L CD2 1 
ATOM   3330 C CE1 . PHE C 3 41  ? 8.609   -8.907  -50.786 1.00 114.14 ? 41  PHE L CE1 1 
ATOM   3331 C CE2 . PHE C 3 41  ? 8.800   -10.895 -49.495 1.00 157.67 ? 41  PHE L CE2 1 
ATOM   3332 C CZ  . PHE C 3 41  ? 8.836   -9.525  -49.581 1.00 132.30 ? 41  PHE L CZ  1 
ATOM   3333 N N   . GLN C 3 42  ? 7.477   -11.392 -56.097 1.00 129.71 ? 42  GLN L N   1 
ATOM   3334 C CA  . GLN C 3 42  ? 7.739   -11.913 -57.463 1.00 127.20 ? 42  GLN L CA  1 
ATOM   3335 C C   . GLN C 3 42  ? 9.155   -11.506 -57.856 1.00 114.66 ? 42  GLN L C   1 
ATOM   3336 O O   . GLN C 3 42  ? 9.442   -10.297 -57.861 1.00 111.77 ? 42  GLN L O   1 
ATOM   3337 C CB  . GLN C 3 42  ? 6.774   -11.345 -58.499 1.00 139.36 ? 42  GLN L CB  1 
ATOM   3338 C CG  . GLN C 3 42  ? 7.026   -11.881 -59.902 1.00 145.27 ? 42  GLN L CG  1 
ATOM   3339 C CD  . GLN C 3 42  ? 6.156   -11.230 -60.949 1.00 129.06 ? 42  GLN L CD  1 
ATOM   3340 O OE1 . GLN C 3 42  ? 5.382   -10.319 -60.664 1.00 168.44 ? 42  GLN L OE1 1 
ATOM   3341 N NE2 . GLN C 3 42  ? 6.285   -11.692 -62.182 1.00 137.00 ? 42  GLN L NE2 1 
ATOM   3342 N N   . GLN C 3 43  ? 9.996   -12.487 -58.164 1.00 111.96 ? 43  GLN L N   1 
ATOM   3343 C CA  . GLN C 3 43  ? 11.358  -12.176 -58.588 1.00 125.36 ? 43  GLN L CA  1 
ATOM   3344 C C   . GLN C 3 43  ? 11.427  -12.522 -60.071 1.00 141.53 ? 43  GLN L C   1 
ATOM   3345 O O   . GLN C 3 43  ? 11.665  -13.679 -60.437 1.00 137.34 ? 43  GLN L O   1 
ATOM   3346 C CB  . GLN C 3 43  ? 12.387  -12.972 -57.792 1.00 130.50 ? 43  GLN L CB  1 
ATOM   3347 C CG  . GLN C 3 43  ? 13.829  -12.660 -58.173 1.00 128.19 ? 43  GLN L CG  1 
ATOM   3348 C CD  . GLN C 3 43  ? 14.824  -13.686 -57.655 1.00 126.04 ? 43  GLN L CD  1 
ATOM   3349 O OE1 . GLN C 3 43  ? 14.453  -14.653 -56.989 1.00 119.90 ? 43  GLN L OE1 1 
ATOM   3350 N NE2 . GLN C 3 43  ? 16.099  -13.480 -57.969 1.00 136.81 ? 43  GLN L NE2 1 
ATOM   3351 N N   . ARG C 3 44  ? 11.199  -11.529 -60.919 1.00 155.28 ? 44  ARG L N   1 
ATOM   3352 C CA  . ARG C 3 44  ? 11.317  -11.721 -62.357 1.00 161.94 ? 44  ARG L CA  1 
ATOM   3353 C C   . ARG C 3 44  ? 12.756  -12.126 -62.661 1.00 166.39 ? 44  ARG L C   1 
ATOM   3354 O O   . ARG C 3 44  ? 13.685  -11.421 -62.239 1.00 171.40 ? 44  ARG L O   1 
ATOM   3355 C CB  . ARG C 3 44  ? 10.935  -10.434 -63.079 1.00 164.43 ? 44  ARG L CB  1 
ATOM   3356 C CG  . ARG C 3 44  ? 10.991  -10.561 -64.593 1.00 161.71 ? 44  ARG L CG  1 
ATOM   3357 C CD  . ARG C 3 44  ? 10.372  -9.346  -65.274 1.00 158.18 ? 44  ARG L CD  1 
ATOM   3358 N NE  . ARG C 3 44  ? 8.938   -9.239  -65.027 1.00 197.21 ? 44  ARG L NE  1 
ATOM   3359 C CZ  . ARG C 3 44  ? 8.372   -8.345  -64.224 1.00 204.28 ? 44  ARG L CZ  1 
ATOM   3360 N NH1 . ARG C 3 44  ? 9.092   -7.452  -63.565 1.00 217.08 ? 44  ARG L NH1 1 
ATOM   3361 N NH2 . ARG C 3 44  ? 7.050   -8.349  -64.081 1.00 199.78 ? 44  ARG L NH2 1 
ATOM   3362 N N   . PRO C 3 45  ? 13.038  -13.258 -63.350 1.00 160.70 ? 45  PRO L N   1 
ATOM   3363 C CA  . PRO C 3 45  ? 14.423  -13.707 -63.541 1.00 142.35 ? 45  PRO L CA  1 
ATOM   3364 C C   . PRO C 3 45  ? 15.393  -12.603 -63.984 1.00 150.06 ? 45  PRO L C   1 
ATOM   3365 O O   . PRO C 3 45  ? 15.046  -11.843 -64.866 1.00 147.63 ? 45  PRO L O   1 
ATOM   3366 C CB  . PRO C 3 45  ? 14.299  -14.761 -64.650 1.00 150.89 ? 45  PRO L CB  1 
ATOM   3367 C CG  . PRO C 3 45  ? 12.889  -14.610 -65.180 1.00 179.42 ? 45  PRO L CG  1 
ATOM   3368 C CD  . PRO C 3 45  ? 12.083  -14.084 -64.012 1.00 168.30 ? 45  PRO L CD  1 
ATOM   3369 N N   . GLY C 3 46  ? 16.576  -12.552 -63.368 1.00 144.53 ? 46  GLY L N   1 
ATOM   3370 C CA  . GLY C 3 46  ? 17.576  -11.521 -63.707 1.00 123.03 ? 46  GLY L CA  1 
ATOM   3371 C C   . GLY C 3 46  ? 17.357  -10.256 -62.899 1.00 123.95 ? 46  GLY L C   1 
ATOM   3372 O O   . GLY C 3 46  ? 18.257  -9.399  -62.897 1.00 120.41 ? 46  GLY L O   1 
ATOM   3373 N N   . GLN C 3 47  ? 16.206  -10.149 -62.230 1.00 153.15 ? 47  GLN L N   1 
ATOM   3374 C CA  . GLN C 3 47  ? 15.879  -8.939  -61.431 1.00 152.42 ? 47  GLN L CA  1 
ATOM   3375 C C   . GLN C 3 47  ? 15.760  -9.324  -59.954 1.00 144.60 ? 47  GLN L C   1 
ATOM   3376 O O   . GLN C 3 47  ? 15.621  -10.525 -59.669 1.00 140.07 ? 47  GLN L O   1 
ATOM   3377 C CB  . GLN C 3 47  ? 14.568  -8.316  -61.910 1.00 141.58 ? 47  GLN L CB  1 
ATOM   3378 C CG  . GLN C 3 47  ? 14.470  -8.174  -63.421 1.00 125.01 ? 47  GLN L CG  1 
ATOM   3379 C CD  . GLN C 3 47  ? 15.582  -7.324  -63.982 1.00 150.98 ? 47  GLN L CD  1 
ATOM   3380 O OE1 . GLN C 3 47  ? 16.370  -7.768  -64.814 1.00 171.35 ? 47  GLN L OE1 1 
ATOM   3381 N NE2 . GLN C 3 47  ? 15.653  -6.084  -63.525 1.00 136.00 ? 47  GLN L NE2 1 
ATOM   3382 N N   . SER C 3 48  ? 15.764  -8.333  -59.062 1.00 151.11 ? 48  SER L N   1 
ATOM   3383 C CA  . SER C 3 48  ? 15.682  -8.600  -57.603 1.00 122.26 ? 48  SER L CA  1 
ATOM   3384 C C   . SER C 3 48  ? 14.224  -8.766  -57.187 1.00 127.48 ? 48  SER L C   1 
ATOM   3385 O O   . SER C 3 48  ? 13.360  -8.098  -57.776 1.00 147.61 ? 48  SER L O   1 
ATOM   3386 C CB  . SER C 3 48  ? 16.319  -7.486  -56.836 1.00 128.54 ? 48  SER L CB  1 
ATOM   3387 O OG  . SER C 3 48  ? 15.440  -7.005  -55.829 1.00 152.84 ? 48  SER L OG  1 
ATOM   3388 N N   . PRO C 3 49  ? 13.839  -9.543  -56.144 1.00 106.96 ? 49  PRO L N   1 
ATOM   3389 C CA  . PRO C 3 49  ? 12.408  -9.719  -55.835 1.00 109.70 ? 49  PRO L CA  1 
ATOM   3390 C C   . PRO C 3 49  ? 11.580  -8.436  -55.642 1.00 111.76 ? 49  PRO L C   1 
ATOM   3391 O O   . PRO C 3 49  ? 12.146  -7.440  -55.240 1.00 108.42 ? 49  PRO L O   1 
ATOM   3392 C CB  . PRO C 3 49  ? 12.443  -10.454 -54.492 1.00 102.69 ? 49  PRO L CB  1 
ATOM   3393 C CG  . PRO C 3 49  ? 13.711  -11.258 -54.550 1.00 106.48 ? 49  PRO L CG  1 
ATOM   3394 C CD  . PRO C 3 49  ? 14.688  -10.316 -55.214 1.00 117.05 ? 49  PRO L CD  1 
ATOM   3395 N N   . ARG C 3 50  ? 10.264  -8.500  -55.892 1.00 109.52 ? 50  ARG L N   1 
ATOM   3396 C CA  . ARG C 3 50  ? 9.361   -7.328  -55.708 1.00 109.06 ? 50  ARG L CA  1 
ATOM   3397 C C   . ARG C 3 50  ? 8.149   -7.730  -54.861 1.00 119.13 ? 50  ARG L C   1 
ATOM   3398 O O   . ARG C 3 50  ? 7.843   -8.925  -54.852 1.00 129.56 ? 50  ARG L O   1 
ATOM   3399 C CB  . ARG C 3 50  ? 8.857   -6.817  -57.058 1.00 104.88 ? 50  ARG L CB  1 
ATOM   3400 C CG  . ARG C 3 50  ? 9.929   -6.707  -58.132 1.00 141.54 ? 50  ARG L CG  1 
ATOM   3401 C CD  . ARG C 3 50  ? 9.521   -5.765  -59.249 1.00 161.10 ? 50  ARG L CD  1 
ATOM   3402 N NE  . ARG C 3 50  ? 8.260   -5.087  -58.980 1.00 199.06 ? 50  ARG L NE  1 
ATOM   3403 C CZ  . ARG C 3 50  ? 8.118   -3.770  -58.900 1.00 205.14 ? 50  ARG L CZ  1 
ATOM   3404 N NH1 . ARG C 3 50  ? 9.142   -3.014  -58.548 1.00 185.46 ? 50  ARG L NH1 1 
ATOM   3405 N NH2 . ARG C 3 50  ? 6.948   -3.214  -59.164 1.00 216.74 ? 50  ARG L NH2 1 
ATOM   3406 N N   . ARG C 3 51  ? 7.520   -6.776  -54.176 1.00 108.87 ? 51  ARG L N   1 
ATOM   3407 C CA  . ARG C 3 51  ? 6.310   -7.071  -53.367 1.00 116.30 ? 51  ARG L CA  1 
ATOM   3408 C C   . ARG C 3 51  ? 5.004   -6.837  -54.120 1.00 115.10 ? 51  ARG L C   1 
ATOM   3409 O O   . ARG C 3 51  ? 4.956   -5.893  -54.919 1.00 141.91 ? 51  ARG L O   1 
ATOM   3410 C CB  . ARG C 3 51  ? 6.101   -5.980  -52.319 1.00 129.72 ? 51  ARG L CB  1 
ATOM   3411 C CG  . ARG C 3 51  ? 7.211   -4.939  -52.310 1.00 129.78 ? 51  ARG L CG  1 
ATOM   3412 C CD  . ARG C 3 51  ? 6.905   -3.697  -53.128 1.00 136.58 ? 51  ARG L CD  1 
ATOM   3413 N NE  . ARG C 3 51  ? 6.093   -3.961  -54.305 1.00 152.50 ? 51  ARG L NE  1 
ATOM   3414 C CZ  . ARG C 3 51  ? 6.524   -3.839  -55.553 1.00 171.01 ? 51  ARG L CZ  1 
ATOM   3415 N NH1 . ARG C 3 51  ? 5.981   -4.564  -56.513 1.00 184.51 ? 51  ARG L NH1 1 
ATOM   3416 N NH2 . ARG C 3 51  ? 7.493   -2.985  -55.833 1.00 167.29 ? 51  ARG L NH2 1 
ATOM   3417 N N   . LEU C 3 52  ? 3.979   -7.640  -53.841 1.00 118.01 ? 52  LEU L N   1 
ATOM   3418 C CA  . LEU C 3 52  ? 2.697   -7.600  -54.550 1.00 128.88 ? 52  LEU L CA  1 
ATOM   3419 C C   . LEU C 3 52  ? 1.608   -7.203  -53.680 1.00 131.18 ? 52  LEU L C   1 
ATOM   3420 O O   . LEU C 3 52  ? 1.211   -6.024  -53.683 1.00 129.05 ? 52  LEU L O   1 
ATOM   3421 C CB  . LEU C 3 52  ? 2.727   -9.034  -55.114 1.00 130.19 ? 52  LEU L CB  1 
ATOM   3422 C CG  . LEU C 3 52  ? 2.578   -9.285  -56.614 1.00 118.92 ? 52  LEU L CG  1 
ATOM   3423 C CD1 . LEU C 3 52  ? 3.248   -8.199  -57.435 1.00 126.44 ? 52  LEU L CD1 1 
ATOM   3424 C CD2 . LEU C 3 52  ? 3.150   -10.646 -56.978 1.00 129.69 ? 52  LEU L CD2 1 
ATOM   3425 N N   . ILE C 3 53  ? 1.116   -8.165  -52.895 1.00 120.69 ? 53  ILE L N   1 
ATOM   3426 C CA  . ILE C 3 53  ? -0.079  -7.905  -51.934 1.00 124.81 ? 53  ILE L CA  1 
ATOM   3427 C C   . ILE C 3 53  ? 0.260   -7.746  -50.527 1.00 144.47 ? 53  ILE L C   1 
ATOM   3428 O O   . ILE C 3 53  ? 0.465   -8.776  -49.889 1.00 154.11 ? 53  ILE L O   1 
ATOM   3429 C CB  . ILE C 3 53  ? -0.995  -9.082  -52.286 1.00 118.18 ? 53  ILE L CB  1 
ATOM   3430 C CG1 . ILE C 3 53  ? -1.011  -9.469  -53.767 1.00 122.08 ? 53  ILE L CG1 1 
ATOM   3431 C CG2 . ILE C 3 53  ? -2.393  -8.788  -51.766 1.00 151.61 ? 53  ILE L CG2 1 
ATOM   3432 C CD1 . ILE C 3 53  ? -1.768  -8.502  -54.648 1.00 129.25 ? 53  ILE L CD1 1 
ATOM   3433 N N   . TYR C 3 54  ? 0.180   -6.533  -49.977 1.00 149.81 ? 54  TYR L N   1 
ATOM   3434 C CA  . TYR C 3 54  ? 0.521   -6.265  -48.562 1.00 150.20 ? 54  TYR L CA  1 
ATOM   3435 C C   . TYR C 3 54  ? -0.510  -6.995  -47.672 1.00 147.78 ? 54  TYR L C   1 
ATOM   3436 O O   . TYR C 3 54  ? -1.702  -7.007  -48.031 1.00 159.92 ? 54  TYR L O   1 
ATOM   3437 C CB  . TYR C 3 54  ? 0.679   -4.770  -48.313 1.00 135.31 ? 54  TYR L CB  1 
ATOM   3438 C CG  . TYR C 3 54  ? 1.995   -4.269  -48.848 1.00 151.72 ? 54  TYR L CG  1 
ATOM   3439 C CD1 . TYR C 3 54  ? 2.229   -4.209  -50.211 1.00 162.48 ? 54  TYR L CD1 1 
ATOM   3440 C CD2 . TYR C 3 54  ? 3.027   -3.911  -47.998 1.00 139.97 ? 54  TYR L CD2 1 
ATOM   3441 C CE1 . TYR C 3 54  ? 3.442   -3.778  -50.718 1.00 192.71 ? 54  TYR L CE1 1 
ATOM   3442 C CE2 . TYR C 3 54  ? 4.246   -3.474  -48.488 1.00 158.93 ? 54  TYR L CE2 1 
ATOM   3443 C CZ  . TYR C 3 54  ? 4.453   -3.406  -49.853 1.00 189.32 ? 54  TYR L CZ  1 
ATOM   3444 O OH  . TYR C 3 54  ? 5.651   -2.976  -50.363 1.00 187.08 ? 54  TYR L OH  1 
ATOM   3445 N N   . ASN C 3 55  ? -0.042  -7.626  -46.602 1.00 138.46 ? 55  ASN L N   1 
ATOM   3446 C CA  . ASN C 3 55  ? -0.893  -8.410  -45.737 1.00 127.71 ? 55  ASN L CA  1 
ATOM   3447 C C   . ASN C 3 55  ? -1.495  -9.447  -46.639 1.00 144.00 ? 55  ASN L C   1 
ATOM   3448 O O   . ASN C 3 55  ? -0.721  -10.080 -47.341 1.00 166.33 ? 55  ASN L O   1 
ATOM   3449 C CB  . ASN C 3 55  ? -1.982  -7.506  -45.079 1.00 134.66 ? 55  ASN L CB  1 
ATOM   3450 C CG  . ASN C 3 55  ? -1.392  -6.353  -44.297 1.00 149.20 ? 55  ASN L CG  1 
ATOM   3451 O OD1 . ASN C 3 55  ? -0.174  -6.236  -44.182 1.00 145.77 ? 55  ASN L OD1 1 
ATOM   3452 N ND2 . ASN C 3 55  ? -2.245  -5.501  -43.753 1.00 142.72 ? 55  ASN L ND2 1 
ATOM   3453 N N   . VAL C 3 56  ? -2.822  -9.594  -46.653 1.00 144.72 ? 56  VAL L N   1 
ATOM   3454 C CA  . VAL C 3 56  ? -3.453  -10.678 -47.467 1.00 156.00 ? 56  VAL L CA  1 
ATOM   3455 C C   . VAL C 3 56  ? -4.356  -10.062 -48.542 1.00 184.17 ? 56  VAL L C   1 
ATOM   3456 O O   . VAL C 3 56  ? -4.614  -10.747 -49.551 1.00 187.83 ? 56  VAL L O   1 
ATOM   3457 C CB  . VAL C 3 56  ? -4.227  -11.675 -46.584 1.00 170.30 ? 56  VAL L CB  1 
ATOM   3458 C CG1 . VAL C 3 56  ? -3.293  -12.667 -45.910 1.00 177.53 ? 56  VAL L CG1 1 
ATOM   3459 C CG2 . VAL C 3 56  ? -5.099  -10.966 -45.559 1.00 144.41 ? 56  VAL L CG2 1 
ATOM   3460 N N   . PHE C 3 57  ? -4.817  -8.824  -48.335 1.00 170.17 ? 57  PHE L N   1 
ATOM   3461 C CA  . PHE C 3 57  ? -5.756  -8.191  -49.299 1.00 164.87 ? 57  PHE L CA  1 
ATOM   3462 C C   . PHE C 3 57  ? -5.386  -6.719  -49.507 1.00 153.40 ? 57  PHE L C   1 
ATOM   3463 O O   . PHE C 3 57  ? -6.230  -5.849  -49.216 1.00 149.03 ? 57  PHE L O   1 
ATOM   3464 C CB  . PHE C 3 57  ? -7.197  -8.334  -48.803 1.00 175.85 ? 57  PHE L CB  1 
ATOM   3465 C CG  . PHE C 3 57  ? -7.780  -9.715  -48.962 1.00 203.91 ? 57  PHE L CG  1 
ATOM   3466 C CD1 . PHE C 3 57  ? -7.975  -10.260 -50.221 1.00 202.81 ? 57  PHE L CD1 1 
ATOM   3467 C CD2 . PHE C 3 57  ? -8.116  -10.478 -47.856 1.00 207.03 ? 57  PHE L CD2 1 
ATOM   3468 C CE1 . PHE C 3 57  ? -8.508  -11.530 -50.369 1.00 221.57 ? 57  PHE L CE1 1 
ATOM   3469 C CE2 . PHE C 3 57  ? -8.645  -11.750 -48.007 1.00 222.60 ? 57  PHE L CE2 1 
ATOM   3470 C CZ  . PHE C 3 57  ? -8.841  -12.274 -49.262 1.00 230.86 ? 57  PHE L CZ  1 
ATOM   3471 N N   . THR C 3 58  ? -4.170  -6.450  -49.995 1.00 145.62 ? 58  THR L N   1 
ATOM   3472 C CA  . THR C 3 58  ? -3.755  -5.050  -50.286 1.00 145.44 ? 58  THR L CA  1 
ATOM   3473 C C   . THR C 3 58  ? -2.770  -5.041  -51.461 1.00 135.51 ? 58  THR L C   1 
ATOM   3474 O O   . THR C 3 58  ? -1.556  -5.126  -51.212 1.00 134.56 ? 58  THR L O   1 
ATOM   3475 C CB  . THR C 3 58  ? -3.148  -4.375  -49.048 1.00 147.92 ? 58  THR L CB  1 
ATOM   3476 O OG1 . THR C 3 58  ? -4.041  -4.539  -47.946 1.00 146.75 ? 58  THR L OG1 1 
ATOM   3477 C CG2 . THR C 3 58  ? -2.871  -2.902  -49.260 1.00 138.68 ? 58  THR L CG2 1 
ATOM   3478 N N   . ARG C 3 59  ? -3.251  -4.733  -52.665 1.00 143.01 ? 59  ARG L N   1 
ATOM   3479 C CA  . ARG C 3 59  ? -2.349  -4.595  -53.841 1.00 146.31 ? 59  ARG L CA  1 
ATOM   3480 C C   . ARG C 3 59  ? -1.310  -3.503  -53.571 1.00 150.09 ? 59  ARG L C   1 
ATOM   3481 O O   . ARG C 3 59  ? -1.644  -2.533  -52.870 1.00 161.98 ? 59  ARG L O   1 
ATOM   3482 C CB  . ARG C 3 59  ? -3.176  -4.221  -55.073 1.00 144.58 ? 59  ARG L CB  1 
ATOM   3483 C CG  . ARG C 3 59  ? -2.427  -4.310  -56.393 1.00 140.88 ? 59  ARG L CG  1 
ATOM   3484 C CD  . ARG C 3 59  ? -3.378  -4.324  -57.572 1.00 139.31 ? 59  ARG L CD  1 
ATOM   3485 N NE  . ARG C 3 59  ? -4.129  -5.567  -57.641 1.00 167.64 ? 59  ARG L NE  1 
ATOM   3486 C CZ  . ARG C 3 59  ? -5.452  -5.648  -57.562 1.00 184.19 ? 59  ARG L CZ  1 
ATOM   3487 N NH1 . ARG C 3 59  ? -6.177  -4.547  -57.485 1.00 193.49 ? 59  ARG L NH1 1 
ATOM   3488 N NH2 . ARG C 3 59  ? -6.043  -6.830  -57.566 1.00 190.85 ? 59  ARG L NH2 1 
ATOM   3489 N N   . ASP C 3 60  ? -0.105  -3.645  -54.131 1.00 138.27 ? 60  ASP L N   1 
ATOM   3490 C CA  . ASP C 3 60  ? 0.969   -2.638  -53.931 1.00 155.82 ? 60  ASP L CA  1 
ATOM   3491 C C   . ASP C 3 60  ? 0.836   -1.535  -54.980 1.00 165.37 ? 60  ASP L C   1 
ATOM   3492 O O   . ASP C 3 60  ? 0.299   -1.823  -56.061 1.00 158.74 ? 60  ASP L O   1 
ATOM   3493 C CB  . ASP C 3 60  ? 2.356   -3.274  -53.999 1.00 165.22 ? 60  ASP L CB  1 
ATOM   3494 C CG  . ASP C 3 60  ? 3.473   -2.294  -54.305 1.00 189.21 ? 60  ASP L CG  1 
ATOM   3495 O OD1 . ASP C 3 60  ? 3.927   -1.615  -53.365 1.00 206.40 ? 60  ASP L OD1 1 
ATOM   3496 O OD2 . ASP C 3 60  ? 3.876   -2.214  -55.482 1.00 181.35 ? 60  ASP L OD2 1 
ATOM   3497 N N   . SER C 3 61  ? 1.319   -0.331  -54.667 1.00 174.13 ? 61  SER L N   1 
ATOM   3498 C CA  . SER C 3 61  ? 1.225   0.824   -55.598 1.00 170.82 ? 61  SER L CA  1 
ATOM   3499 C C   . SER C 3 61  ? 1.516   0.553   -57.076 1.00 172.97 ? 61  SER L C   1 
ATOM   3500 O O   . SER C 3 61  ? 0.722   1.000   -57.925 1.00 182.48 ? 61  SER L O   1 
ATOM   3501 C CB  . SER C 3 61  ? 2.192   1.902   -55.196 1.00 204.08 ? 61  SER L CB  1 
ATOM   3502 O OG  . SER C 3 61  ? 1.796   2.498   -53.970 1.00 259.63 ? 61  SER L OG  1 
ATOM   3503 N N   . GLY C 3 62  ? 2.628   -0.117  -57.375 1.00 157.65 ? 62  GLY L N   1 
ATOM   3504 C CA  . GLY C 3 62  ? 2.998   -0.327  -58.786 1.00 157.41 ? 62  GLY L CA  1 
ATOM   3505 C C   . GLY C 3 62  ? 2.678   -1.778  -59.085 1.00 162.63 ? 62  GLY L C   1 
ATOM   3506 O O   . GLY C 3 62  ? 3.556   -2.459  -59.646 1.00 155.79 ? 62  GLY L O   1 
ATOM   3507 N N   . VAL C 3 63  ? 1.472   -2.246  -58.742 1.00 165.38 ? 63  VAL L N   1 
ATOM   3508 C CA  . VAL C 3 63  ? 1.137   -3.649  -59.130 1.00 165.56 ? 63  VAL L CA  1 
ATOM   3509 C C   . VAL C 3 63  ? -0.124  -3.641  -60.000 1.00 151.48 ? 63  VAL L C   1 
ATOM   3510 O O   . VAL C 3 63  ? -1.114  -2.995  -59.605 1.00 156.35 ? 63  VAL L O   1 
ATOM   3511 C CB  . VAL C 3 63  ? 0.966   -4.545  -57.889 1.00 168.60 ? 63  VAL L CB  1 
ATOM   3512 C CG1 . VAL C 3 63  ? 0.342   -5.889  -58.230 1.00 159.47 ? 63  VAL L CG1 1 
ATOM   3513 C CG2 . VAL C 3 63  ? 2.286   -4.737  -57.166 1.00 161.94 ? 63  VAL L CG2 1 
ATOM   3514 N N   . PRO C 3 64  ? -0.128  -4.332  -61.162 1.00 161.65 ? 64  PRO L N   1 
ATOM   3515 C CA  . PRO C 3 64  ? -1.312  -4.403  -62.022 1.00 187.80 ? 64  PRO L CA  1 
ATOM   3516 C C   . PRO C 3 64  ? -2.503  -5.047  -61.299 1.00 192.93 ? 64  PRO L C   1 
ATOM   3517 O O   . PRO C 3 64  ? -2.286  -5.922  -60.479 1.00 189.53 ? 64  PRO L O   1 
ATOM   3518 C CB  . PRO C 3 64  ? -0.869  -5.313  -63.176 1.00 184.79 ? 64  PRO L CB  1 
ATOM   3519 C CG  . PRO C 3 64  ? 0.638   -5.197  -63.181 1.00 185.22 ? 64  PRO L CG  1 
ATOM   3520 C CD  . PRO C 3 64  ? 1.013   -5.060  -61.721 1.00 164.34 ? 64  PRO L CD  1 
ATOM   3521 N N   . ASP C 3 65  ? -3.723  -4.613  -61.631 1.00 194.39 ? 65  ASP L N   1 
ATOM   3522 C CA  . ASP C 3 65  ? -4.944  -5.178  -60.995 1.00 186.71 ? 65  ASP L CA  1 
ATOM   3523 C C   . ASP C 3 65  ? -5.019  -6.678  -61.293 1.00 177.52 ? 65  ASP L C   1 
ATOM   3524 O O   . ASP C 3 65  ? -5.648  -7.404  -60.501 1.00 183.17 ? 65  ASP L O   1 
ATOM   3525 C CB  . ASP C 3 65  ? -6.202  -4.440  -61.460 1.00 189.79 ? 65  ASP L CB  1 
ATOM   3526 C CG  . ASP C 3 65  ? -6.190  -2.962  -61.112 1.00 192.89 ? 65  ASP L CG  1 
ATOM   3527 O OD1 . ASP C 3 65  ? -5.198  -2.513  -60.503 1.00 202.55 ? 65  ASP L OD1 1 
ATOM   3528 O OD2 . ASP C 3 65  ? -7.172  -2.273  -61.451 1.00 187.54 ? 65  ASP L OD2 1 
ATOM   3529 N N   . ARG C 3 66  ? -4.398  -7.120  -62.391 1.00 165.83 ? 66  ARG L N   1 
ATOM   3530 C CA  . ARG C 3 66  ? -4.378  -8.567  -62.729 1.00 161.79 ? 66  ARG L CA  1 
ATOM   3531 C C   . ARG C 3 66  ? -3.940  -9.349  -61.490 1.00 163.46 ? 66  ARG L C   1 
ATOM   3532 O O   . ARG C 3 66  ? -4.653  -10.296 -61.107 1.00 138.76 ? 66  ARG L O   1 
ATOM   3533 C CB  . ARG C 3 66  ? -3.403  -8.824  -63.880 1.00 153.31 ? 66  ARG L CB  1 
ATOM   3534 C CG  . ARG C 3 66  ? -3.447  -7.774  -64.980 1.00 160.15 ? 66  ARG L CG  1 
ATOM   3535 C CD  . ARG C 3 66  ? -2.438  -8.053  -66.078 1.00 174.21 ? 66  ARG L CD  1 
ATOM   3536 N NE  . ARG C 3 66  ? -1.072  -8.139  -65.583 1.00 159.30 ? 66  ARG L NE  1 
ATOM   3537 C CZ  . ARG C 3 66  ? -0.088  -7.331  -65.959 1.00 155.03 ? 66  ARG L CZ  1 
ATOM   3538 N NH1 . ARG C 3 66  ? -0.345  -6.296  -66.739 1.00 165.99 ? 66  ARG L NH1 1 
ATOM   3539 N NH2 . ARG C 3 66  ? 1.147   -7.553  -65.545 1.00 128.96 ? 66  ARG L NH2 1 
ATOM   3540 N N   . PHE C 3 67  ? -2.822  -8.946  -60.878 1.00 168.56 ? 67  PHE L N   1 
ATOM   3541 C CA  . PHE C 3 67  ? -2.309  -9.633  -59.665 1.00 159.76 ? 67  PHE L CA  1 
ATOM   3542 C C   . PHE C 3 67  ? -3.295  -9.411  -58.514 1.00 153.98 ? 67  PHE L C   1 
ATOM   3543 O O   . PHE C 3 67  ? -3.623  -8.243  -58.228 1.00 157.64 ? 67  PHE L O   1 
ATOM   3544 C CB  . PHE C 3 67  ? -0.920  -9.108  -59.294 1.00 143.47 ? 67  PHE L CB  1 
ATOM   3545 C CG  . PHE C 3 67  ? 0.151   -9.312  -60.336 1.00 137.55 ? 67  PHE L CG  1 
ATOM   3546 C CD1 . PHE C 3 67  ? 0.052   -8.733  -61.592 1.00 131.43 ? 67  PHE L CD1 1 
ATOM   3547 C CD2 . PHE C 3 67  ? 1.271   -10.077 -60.056 1.00 151.58 ? 67  PHE L CD2 1 
ATOM   3548 C CE1 . PHE C 3 67  ? 1.040   -8.924  -62.544 1.00 160.24 ? 67  PHE L CE1 1 
ATOM   3549 C CE2 . PHE C 3 67  ? 2.260   -10.265 -61.008 1.00 151.59 ? 67  PHE L CE2 1 
ATOM   3550 C CZ  . PHE C 3 67  ? 2.144   -9.688  -62.250 1.00 160.93 ? 67  PHE L CZ  1 
ATOM   3551 N N   . SER C 3 68  ? -3.745  -10.497 -57.877 1.00 151.50 ? 68  SER L N   1 
ATOM   3552 C CA  . SER C 3 68  ? -4.727  -10.381 -56.767 1.00 148.81 ? 68  SER L CA  1 
ATOM   3553 C C   . SER C 3 68  ? -4.418  -11.410 -55.674 1.00 144.91 ? 68  SER L C   1 
ATOM   3554 O O   . SER C 3 68  ? -4.539  -12.619 -55.955 1.00 147.81 ? 68  SER L O   1 
ATOM   3555 C CB  . SER C 3 68  ? -6.136  -10.537 -57.276 1.00 143.60 ? 68  SER L CB  1 
ATOM   3556 O OG  . SER C 3 68  ? -6.335  -11.833 -57.820 1.00 158.41 ? 68  SER L OG  1 
ATOM   3557 N N   . GLY C 3 69  ? -4.039  -10.946 -54.479 1.00 114.97 ? 69  GLY L N   1 
ATOM   3558 C CA  . GLY C 3 69  ? -3.798  -11.868 -53.352 1.00 132.64 ? 69  GLY L CA  1 
ATOM   3559 C C   . GLY C 3 69  ? -5.110  -12.283 -52.712 1.00 141.69 ? 69  GLY L C   1 
ATOM   3560 O O   . GLY C 3 69  ? -5.983  -11.407 -52.552 1.00 138.52 ? 69  GLY L O   1 
ATOM   3561 N N   . SER C 3 70  ? -5.254  -13.564 -52.363 1.00 138.22 ? 70  SER L N   1 
ATOM   3562 C CA  . SER C 3 70  ? -6.540  -14.062 -51.807 1.00 140.35 ? 70  SER L CA  1 
ATOM   3563 C C   . SER C 3 70  ? -6.283  -15.102 -50.712 1.00 150.42 ? 70  SER L C   1 
ATOM   3564 O O   . SER C 3 70  ? -5.105  -15.425 -50.467 1.00 160.32 ? 70  SER L O   1 
ATOM   3565 C CB  . SER C 3 70  ? -7.419  -14.615 -52.900 1.00 133.68 ? 70  SER L CB  1 
ATOM   3566 O OG  . SER C 3 70  ? -6.692  -15.511 -53.727 1.00 137.63 ? 70  SER L OG  1 
ATOM   3567 N N   . GLY C 3 71  ? -7.350  -15.594 -50.075 1.00 142.87 ? 71  GLY L N   1 
ATOM   3568 C CA  . GLY C 3 71  ? -7.208  -16.584 -48.989 1.00 128.46 ? 71  GLY L CA  1 
ATOM   3569 C C   . GLY C 3 71  ? -7.456  -15.955 -47.629 1.00 139.85 ? 71  GLY L C   1 
ATOM   3570 O O   . GLY C 3 71  ? -7.131  -14.762 -47.465 1.00 151.56 ? 71  GLY L O   1 
ATOM   3571 N N   . SER C 3 72  ? -8.012  -16.726 -46.690 1.00 129.73 ? 72  SER L N   1 
ATOM   3572 C CA  . SER C 3 72  ? -8.289  -16.210 -45.323 1.00 130.48 ? 72  SER L CA  1 
ATOM   3573 C C   . SER C 3 72  ? -7.695  -17.163 -44.281 1.00 125.23 ? 72  SER L C   1 
ATOM   3574 O O   . SER C 3 72  ? -7.032  -16.673 -43.346 1.00 134.02 ? 72  SER L O   1 
ATOM   3575 C CB  . SER C 3 72  ? -9.767  -16.017 -45.110 1.00 147.88 ? 72  SER L CB  1 
ATOM   3576 O OG  . SER C 3 72  ? -10.457 -17.251 -45.237 1.00 159.18 ? 72  SER L OG  1 
ATOM   3577 N N   . GLY C 3 73  ? -7.912  -18.471 -44.457 1.00 134.27 ? 73  GLY L N   1 
ATOM   3578 C CA  . GLY C 3 73  ? -7.318  -19.470 -43.547 1.00 129.16 ? 73  GLY L CA  1 
ATOM   3579 C C   . GLY C 3 73  ? -5.930  -19.867 -44.017 1.00 120.40 ? 73  GLY L C   1 
ATOM   3580 O O   . GLY C 3 73  ? -5.466  -19.274 -45.006 1.00 119.99 ? 73  GLY L O   1 
ATOM   3581 N N   . THR C 3 74  ? -5.317  -20.878 -43.394 1.00 109.34 ? 74  THR L N   1 
ATOM   3582 C CA  . THR C 3 74  ? -3.918  -21.267 -43.728 1.00 113.68 ? 74  THR L CA  1 
ATOM   3583 C C   . THR C 3 74  ? -3.708  -21.325 -45.246 1.00 117.03 ? 74  THR L C   1 
ATOM   3584 O O   . THR C 3 74  ? -2.568  -21.076 -45.683 1.00 115.66 ? 74  THR L O   1 
ATOM   3585 C CB  . THR C 3 74  ? -3.554  -22.614 -43.094 1.00 100.22 ? 74  THR L CB  1 
ATOM   3586 O OG1 . THR C 3 74  ? -4.395  -23.613 -43.672 1.00 96.87  ? 74  THR L OG1 1 
ATOM   3587 C CG2 . THR C 3 74  ? -3.708  -22.616 -41.588 1.00 111.51 ? 74  THR L CG2 1 
ATOM   3588 N N   . ASP C 3 75  ? -4.748  -21.662 -46.014 1.00 127.00 ? 75  ASP L N   1 
ATOM   3589 C CA  . ASP C 3 75  ? -4.594  -21.814 -47.487 1.00 126.11 ? 75  ASP L CA  1 
ATOM   3590 C C   . ASP C 3 75  ? -4.850  -20.476 -48.189 1.00 115.37 ? 75  ASP L C   1 
ATOM   3591 O O   . ASP C 3 75  ? -6.032  -20.112 -48.341 1.00 115.97 ? 75  ASP L O   1 
ATOM   3592 C CB  . ASP C 3 75  ? -5.495  -22.929 -48.024 1.00 137.53 ? 75  ASP L CB  1 
ATOM   3593 C CG  . ASP C 3 75  ? -5.190  -24.285 -47.413 1.00 137.47 ? 75  ASP L CG  1 
ATOM   3594 O OD1 . ASP C 3 75  ? -4.281  -24.353 -46.561 1.00 153.80 ? 75  ASP L OD1 1 
ATOM   3595 O OD2 . ASP C 3 75  ? -5.862  -25.263 -47.794 1.00 130.63 ? 75  ASP L OD2 1 
ATOM   3596 N N   . PHE C 3 76  ? -3.787  -19.773 -48.594 1.00 115.82 ? 76  PHE L N   1 
ATOM   3597 C CA  . PHE C 3 76  ? -3.932  -18.535 -49.336 1.00 124.25 ? 76  PHE L CA  1 
ATOM   3598 C C   . PHE C 3 76  ? -3.563  -18.725 -50.796 1.00 123.32 ? 76  PHE L C   1 
ATOM   3599 O O   . PHE C 3 76  ? -2.793  -19.625 -51.137 1.00 126.65 ? 76  PHE L O   1 
ATOM   3600 C CB  . PHE C 3 76  ? -2.981  -17.551 -48.680 1.00 116.29 ? 76  PHE L CB  1 
ATOM   3601 C CG  . PHE C 3 76  ? -3.288  -17.288 -47.241 1.00 123.70 ? 76  PHE L CG  1 
ATOM   3602 C CD1 . PHE C 3 76  ? -4.220  -16.339 -46.885 1.00 126.53 ? 76  PHE L CD1 1 
ATOM   3603 C CD2 . PHE C 3 76  ? -2.645  -17.996 -46.239 1.00 127.58 ? 76  PHE L CD2 1 
ATOM   3604 C CE1 . PHE C 3 76  ? -4.501  -16.080 -45.560 1.00 152.56 ? 76  PHE L CE1 1 
ATOM   3605 C CE2 . PHE C 3 76  ? -2.921  -17.743 -44.912 1.00 132.13 ? 76  PHE L CE2 1 
ATOM   3606 C CZ  . PHE C 3 76  ? -3.853  -16.783 -44.573 1.00 152.57 ? 76  PHE L CZ  1 
ATOM   3607 N N   . THR C 3 77  ? -4.120  -17.884 -51.665 1.00 127.59 ? 77  THR L N   1 
ATOM   3608 C CA  . THR C 3 77  ? -3.878  -18.021 -53.095 1.00 148.39 ? 77  THR L CA  1 
ATOM   3609 C C   . THR C 3 77  ? -3.615  -16.659 -53.724 1.00 158.83 ? 77  THR L C   1 
ATOM   3610 O O   . THR C 3 77  ? -3.886  -15.607 -53.137 1.00 148.30 ? 77  THR L O   1 
ATOM   3611 C CB  . THR C 3 77  ? -5.045  -18.718 -53.811 1.00 179.31 ? 77  THR L CB  1 
ATOM   3612 O OG1 . THR C 3 77  ? -6.251  -17.972 -53.611 1.00 189.34 ? 77  THR L OG1 1 
ATOM   3613 C CG2 . THR C 3 77  ? -5.230  -20.146 -53.301 1.00 166.73 ? 77  THR L CG2 1 
ATOM   3614 N N   . LEU C 3 78  ? -3.077  -16.703 -54.945 1.00 176.46 ? 78  LEU L N   1 
ATOM   3615 C CA  . LEU C 3 78  ? -2.725  -15.518 -55.727 1.00 160.86 ? 78  LEU L CA  1 
ATOM   3616 C C   . LEU C 3 78  ? -3.092  -15.782 -57.182 1.00 168.90 ? 78  LEU L C   1 
ATOM   3617 O O   . LEU C 3 78  ? -2.449  -16.605 -57.841 1.00 166.59 ? 78  LEU L O   1 
ATOM   3618 C CB  . LEU C 3 78  ? -1.235  -15.193 -55.593 1.00 165.58 ? 78  LEU L CB  1 
ATOM   3619 C CG  . LEU C 3 78  ? -0.670  -14.062 -56.459 1.00 160.22 ? 78  LEU L CG  1 
ATOM   3620 C CD1 . LEU C 3 78  ? -0.957  -12.696 -55.853 1.00 169.19 ? 78  LEU L CD1 1 
ATOM   3621 C CD2 . LEU C 3 78  ? 0.827   -14.250 -56.689 1.00 163.29 ? 78  LEU L CD2 1 
ATOM   3622 N N   . LYS C 3 79  ? -4.111  -15.084 -57.684 1.00 182.81 ? 79  LYS L N   1 
ATOM   3623 C CA  . LYS C 3 79  ? -4.605  -15.266 -59.045 1.00 191.47 ? 79  LYS L CA  1 
ATOM   3624 C C   . LYS C 3 79  ? -4.340  -14.013 -59.871 1.00 175.39 ? 79  LYS L C   1 
ATOM   3625 O O   . LYS C 3 79  ? -4.676  -12.901 -59.450 1.00 157.85 ? 79  LYS L O   1 
ATOM   3626 C CB  . LYS C 3 79  ? -6.103  -15.596 -59.053 1.00 186.84 ? 79  LYS L CB  1 
ATOM   3627 C CG  . LYS C 3 79  ? -6.621  -16.241 -57.770 1.00 187.95 ? 79  LYS L CG  1 
ATOM   3628 C CD  . LYS C 3 79  ? -8.016  -16.839 -57.948 1.00 167.97 ? 79  LYS L CD  1 
ATOM   3629 C CE  . LYS C 3 79  ? -8.546  -17.409 -56.635 1.00 146.04 ? 79  LYS L CE  1 
ATOM   3630 N NZ  . LYS C 3 79  ? -7.720  -18.547 -56.138 1.00 179.36 ? 79  LYS L NZ  1 
ATOM   3631 N N   . ILE C 3 80  ? -3.722  -14.212 -61.036 1.00 165.66 ? 80  ILE L N   1 
ATOM   3632 C CA  . ILE C 3 80  ? -3.412  -13.071 -61.940 1.00 160.89 ? 80  ILE L CA  1 
ATOM   3633 C C   . ILE C 3 80  ? -4.189  -13.284 -63.237 1.00 176.64 ? 80  ILE L C   1 
ATOM   3634 O O   . ILE C 3 80  ? -3.861  -14.235 -63.966 1.00 186.81 ? 80  ILE L O   1 
ATOM   3635 C CB  . ILE C 3 80  ? -1.900  -12.999 -62.215 1.00 160.65 ? 80  ILE L CB  1 
ATOM   3636 C CG1 . ILE C 3 80  ? -1.084  -13.054 -60.921 1.00 170.33 ? 80  ILE L CG1 1 
ATOM   3637 C CG2 . ILE C 3 80  ? -1.565  -11.771 -63.047 1.00 157.51 ? 80  ILE L CG2 1 
ATOM   3638 C CD1 . ILE C 3 80  ? 0.384   -13.323 -61.140 1.00 182.73 ? 80  ILE L CD1 1 
ATOM   3639 N N   . THR C 3 81  ? -5.178  -12.433 -63.506 1.00 178.99 ? 81  THR L N   1 
ATOM   3640 C CA  . THR C 3 81  ? -5.942  -12.538 -64.774 1.00 170.76 ? 81  THR L CA  1 
ATOM   3641 C C   . THR C 3 81  ? -5.063  -12.067 -65.931 1.00 173.81 ? 81  THR L C   1 
ATOM   3642 O O   . THR C 3 81  ? -4.036  -11.423 -65.659 1.00 182.83 ? 81  THR L O   1 
ATOM   3643 C CB  . THR C 3 81  ? -7.220  -11.699 -64.718 1.00 171.76 ? 81  THR L CB  1 
ATOM   3644 O OG1 . THR C 3 81  ? -6.842  -10.325 -64.795 1.00 178.33 ? 81  THR L OG1 1 
ATOM   3645 C CG2 . THR C 3 81  ? -8.027  -11.946 -63.463 1.00 173.56 ? 81  THR L CG2 1 
ATOM   3646 N N   . THR C 3 82  ? -5.482  -12.359 -67.160 1.00 157.41 ? 82  THR L N   1 
ATOM   3647 C CA  . THR C 3 82  ? -4.714  -11.893 -68.339 1.00 173.15 ? 82  THR L CA  1 
ATOM   3648 C C   . THR C 3 82  ? -3.227  -12.094 -68.048 1.00 178.22 ? 82  THR L C   1 
ATOM   3649 O O   . THR C 3 82  ? -2.471  -11.110 -68.128 1.00 170.94 ? 82  THR L O   1 
ATOM   3650 C CB  . THR C 3 82  ? -5.039  -10.430 -68.658 1.00 185.14 ? 82  THR L CB  1 
ATOM   3651 O OG1 . THR C 3 82  ? -4.712  -9.646  -67.511 1.00 173.26 ? 82  THR L OG1 1 
ATOM   3652 C CG2 . THR C 3 82  ? -6.489  -10.215 -69.035 1.00 173.70 ? 82  THR L CG2 1 
ATOM   3653 N N   . VAL C 3 83  ? -2.832  -13.321 -67.707 1.00 164.83 ? 83  VAL L N   1 
ATOM   3654 C CA  . VAL C 3 83  ? -1.382  -13.596 -67.506 1.00 156.52 ? 83  VAL L CA  1 
ATOM   3655 C C   . VAL C 3 83  ? -0.642  -13.001 -68.704 1.00 159.19 ? 83  VAL L C   1 
ATOM   3656 O O   . VAL C 3 83  ? -0.903  -13.449 -69.832 1.00 173.45 ? 83  VAL L O   1 
ATOM   3657 C CB  . VAL C 3 83  ? -1.114  -15.105 -67.377 1.00 148.45 ? 83  VAL L CB  1 
ATOM   3658 C CG1 . VAL C 3 83  ? 0.375   -15.409 -67.327 1.00 154.95 ? 83  VAL L CG1 1 
ATOM   3659 C CG2 . VAL C 3 83  ? -1.825  -15.694 -66.171 1.00 156.55 ? 83  VAL L CG2 1 
ATOM   3660 N N   . GLU C 3 84  ? 0.260   -12.044 -68.457 1.00 156.80 ? 84  GLU L N   1 
ATOM   3661 C CA  . GLU C 3 84  ? 1.041   -11.408 -69.554 1.00 162.06 ? 84  GLU L CA  1 
ATOM   3662 C C   . GLU C 3 84  ? 2.462   -11.981 -69.579 1.00 174.90 ? 84  GLU L C   1 
ATOM   3663 O O   . GLU C 3 84  ? 2.654   -13.103 -69.068 1.00 188.31 ? 84  GLU L O   1 
ATOM   3664 C CB  . GLU C 3 84  ? 1.068   -9.888  -69.385 1.00 167.12 ? 84  GLU L CB  1 
ATOM   3665 C CG  . GLU C 3 84  ? -0.295  -9.243  -69.543 1.00 159.87 ? 84  GLU L CG  1 
ATOM   3666 C CD  . GLU C 3 84  ? -0.282  -7.725  -69.589 1.00 167.23 ? 84  GLU L CD  1 
ATOM   3667 O OE1 . GLU C 3 84  ? 0.818   -7.143  -69.523 1.00 174.15 ? 84  GLU L OE1 1 
ATOM   3668 O OE2 . GLU C 3 84  ? -1.373  -7.130  -69.684 1.00 175.82 ? 84  GLU L OE2 1 
ATOM   3669 N N   . ALA C 3 85  ? 3.416   -11.238 -70.150 1.00 159.94 ? 85  ALA L N   1 
ATOM   3670 C CA  . ALA C 3 85  ? 4.804   -11.744 -70.280 1.00 140.91 ? 85  ALA L CA  1 
ATOM   3671 C C   . ALA C 3 85  ? 5.805   -11.377 -69.178 1.00 134.86 ? 85  ALA L C   1 
ATOM   3672 O O   . ALA C 3 85  ? 6.721   -12.176 -68.928 1.00 145.63 ? 85  ALA L O   1 
ATOM   3673 C CB  . ALA C 3 85  ? 5.454   -11.139 -71.500 1.00 152.42 ? 85  ALA L CB  1 
ATOM   3674 N N   . GLU C 3 86  ? 5.637   -10.207 -68.556 1.00 162.48 ? 86  GLU L N   1 
ATOM   3675 C CA  . GLU C 3 86  ? 6.578   -9.756  -67.495 1.00 174.49 ? 86  GLU L CA  1 
ATOM   3676 C C   . GLU C 3 86  ? 6.051   -10.529 -66.282 1.00 170.15 ? 86  GLU L C   1 
ATOM   3677 O O   . GLU C 3 86  ? 6.800   -10.660 -65.294 1.00 132.26 ? 86  GLU L O   1 
ATOM   3678 C CB  . GLU C 3 86  ? 6.498   -8.244  -67.275 1.00 176.01 ? 86  GLU L CB  1 
ATOM   3679 C CG  . GLU C 3 86  ? 5.145   -7.760  -66.781 1.00 177.93 ? 86  GLU L CG  1 
ATOM   3680 C CD  . GLU C 3 86  ? 4.037   -7.686  -67.818 1.00 180.64 ? 86  GLU L CD  1 
ATOM   3681 O OE1 . GLU C 3 86  ? 2.912   -7.300  -67.447 1.00 171.89 ? 86  GLU L OE1 1 
ATOM   3682 O OE2 . GLU C 3 86  ? 4.300   -8.006  -68.994 1.00 184.08 ? 86  GLU L OE2 1 
ATOM   3683 N N   . ASP C 3 87  ? 4.816   -11.030 -66.365 1.00 156.24 ? 87  ASP L N   1 
ATOM   3684 C CA  . ASP C 3 87  ? 4.196   -11.772 -65.240 1.00 147.81 ? 87  ASP L CA  1 
ATOM   3685 C C   . ASP C 3 87  ? 4.996   -13.056 -64.998 1.00 147.13 ? 87  ASP L C   1 
ATOM   3686 O O   . ASP C 3 87  ? 5.053   -13.502 -63.839 1.00 162.34 ? 87  ASP L O   1 
ATOM   3687 C CB  . ASP C 3 87  ? 2.715   -12.028 -65.520 1.00 163.53 ? 87  ASP L CB  1 
ATOM   3688 C CG  . ASP C 3 87  ? 1.931   -10.756 -65.791 1.00 159.72 ? 87  ASP L CG  1 
ATOM   3689 O OD1 . ASP C 3 87  ? 2.547   -9.673  -65.765 1.00 172.27 ? 87  ASP L OD1 1 
ATOM   3690 O OD2 . ASP C 3 87  ? 0.712   -10.857 -66.024 1.00 158.91 ? 87  ASP L OD2 1 
ATOM   3691 N N   . VAL C 3 88  ? 5.603   -13.613 -66.047 1.00 157.83 ? 88  VAL L N   1 
ATOM   3692 C CA  . VAL C 3 88  ? 6.383   -14.836 -65.908 1.00 158.91 ? 88  VAL L CA  1 
ATOM   3693 C C   . VAL C 3 88  ? 7.546   -14.637 -64.943 1.00 142.41 ? 88  VAL L C   1 
ATOM   3694 O O   . VAL C 3 88  ? 8.218   -13.595 -64.942 1.00 144.51 ? 88  VAL L O   1 
ATOM   3695 C CB  . VAL C 3 88  ? 6.875   -15.268 -67.298 1.00 157.08 ? 88  VAL L CB  1 
ATOM   3696 C CG1 . VAL C 3 88  ? 7.743   -16.500 -67.216 1.00 145.53 ? 88  VAL L CG1 1 
ATOM   3697 C CG2 . VAL C 3 88  ? 5.671   -15.564 -68.162 1.00 160.08 ? 88  VAL L CG2 1 
ATOM   3698 N N   . GLY C 3 89  ? 7.784   -15.640 -64.114 1.00 131.09 ? 89  GLY L N   1 
ATOM   3699 C CA  . GLY C 3 89  ? 8.893   -15.612 -63.190 1.00 124.40 ? 89  GLY L CA  1 
ATOM   3700 C C   . GLY C 3 89  ? 8.620   -16.501 -61.994 1.00 140.03 ? 89  GLY L C   1 
ATOM   3701 O O   . GLY C 3 89  ? 7.717   -17.330 -62.011 1.00 147.14 ? 89  GLY L O   1 
ATOM   3702 N N   . VAL C 3 90  ? 9.430   -16.296 -60.960 1.00 134.18 ? 90  VAL L N   1 
ATOM   3703 C CA  . VAL C 3 90  ? 9.363   -17.073 -59.730 1.00 130.31 ? 90  VAL L CA  1 
ATOM   3704 C C   . VAL C 3 90  ? 8.606   -16.261 -58.689 1.00 128.04 ? 90  VAL L C   1 
ATOM   3705 O O   . VAL C 3 90  ? 8.698   -15.028 -58.644 1.00 128.74 ? 90  VAL L O   1 
ATOM   3706 C CB  . VAL C 3 90  ? 10.778  -17.453 -59.240 1.00 148.86 ? 90  VAL L CB  1 
ATOM   3707 C CG1 . VAL C 3 90  ? 10.722  -18.179 -57.906 1.00 121.52 ? 90  VAL L CG1 1 
ATOM   3708 C CG2 . VAL C 3 90  ? 11.495  -18.293 -60.285 1.00 159.00 ? 90  VAL L CG2 1 
ATOM   3709 N N   . TYR C 3 91  ? 7.792   -16.956 -57.887 1.00 139.09 ? 91  TYR L N   1 
ATOM   3710 C CA  . TYR C 3 91  ? 7.017   -16.286 -56.810 1.00 142.18 ? 91  TYR L CA  1 
ATOM   3711 C C   . TYR C 3 91  ? 7.251   -17.043 -55.500 1.00 134.71 ? 91  TYR L C   1 
ATOM   3712 O O   . TYR C 3 91  ? 7.470   -18.269 -55.554 1.00 145.36 ? 91  TYR L O   1 
ATOM   3713 C CB  . TYR C 3 91  ? 5.518   -16.284 -57.116 1.00 130.02 ? 91  TYR L CB  1 
ATOM   3714 C CG  . TYR C 3 91  ? 5.076   -15.480 -58.313 1.00 144.52 ? 91  TYR L CG  1 
ATOM   3715 C CD1 . TYR C 3 91  ? 5.461   -15.825 -59.598 1.00 141.97 ? 91  TYR L CD1 1 
ATOM   3716 C CD2 . TYR C 3 91  ? 4.253   -14.377 -58.160 1.00 155.29 ? 91  TYR L CD2 1 
ATOM   3717 C CE1 . TYR C 3 91  ? 5.050   -15.092 -60.698 1.00 145.29 ? 91  TYR L CE1 1 
ATOM   3718 C CE2 . TYR C 3 91  ? 3.829   -13.634 -59.249 1.00 163.92 ? 91  TYR L CE2 1 
ATOM   3719 C CZ  . TYR C 3 91  ? 4.229   -13.992 -60.523 1.00 154.84 ? 91  TYR L CZ  1 
ATOM   3720 O OH  . TYR C 3 91  ? 3.814   -13.258 -61.607 1.00 154.36 ? 91  TYR L OH  1 
ATOM   3721 N N   . TYR C 3 92  ? 7.192   -16.341 -54.365 1.00 123.02 ? 92  TYR L N   1 
ATOM   3722 C CA  . TYR C 3 92  ? 7.367   -17.004 -53.047 1.00 131.14 ? 92  TYR L CA  1 
ATOM   3723 C C   . TYR C 3 92  ? 6.250   -16.587 -52.088 1.00 118.04 ? 92  TYR L C   1 
ATOM   3724 O O   . TYR C 3 92  ? 5.715   -15.471 -52.246 1.00 112.21 ? 92  TYR L O   1 
ATOM   3725 C CB  . TYR C 3 92  ? 8.719   -16.652 -52.420 1.00 148.10 ? 92  TYR L CB  1 
ATOM   3726 C CG  . TYR C 3 92  ? 9.894   -17.441 -52.938 1.00 156.66 ? 92  TYR L CG  1 
ATOM   3727 C CD1 . TYR C 3 92  ? 10.360  -17.266 -54.229 1.00 148.19 ? 92  TYR L CD1 1 
ATOM   3728 C CD2 . TYR C 3 92  ? 10.561  -18.342 -52.125 1.00 155.42 ? 92  TYR L CD2 1 
ATOM   3729 C CE1 . TYR C 3 92  ? 11.445  -17.981 -54.706 1.00 149.22 ? 92  TYR L CE1 1 
ATOM   3730 C CE2 . TYR C 3 92  ? 11.645  -19.068 -52.588 1.00 149.63 ? 92  TYR L CE2 1 
ATOM   3731 C CZ  . TYR C 3 92  ? 12.089  -18.886 -53.884 1.00 145.60 ? 92  TYR L CZ  1 
ATOM   3732 O OH  . TYR C 3 92  ? 13.165  -19.592 -54.363 1.00 135.18 ? 92  TYR L OH  1 
ATOM   3733 N N   . CYS C 3 93  ? 5.913   -17.452 -51.124 1.00 98.22  ? 93  CYS L N   1 
ATOM   3734 C CA  . CYS C 3 93  ? 4.921   -17.068 -50.089 1.00 116.83 ? 93  CYS L CA  1 
ATOM   3735 C C   . CYS C 3 93  ? 5.575   -16.006 -49.208 1.00 148.69 ? 93  CYS L C   1 
ATOM   3736 O O   . CYS C 3 93  ? 6.788   -15.765 -49.374 1.00 173.02 ? 93  CYS L O   1 
ATOM   3737 C CB  . CYS C 3 93  ? 4.570   -18.232 -49.173 1.00 142.06 ? 93  CYS L CB  1 
ATOM   3738 S SG  . CYS C 3 93  ? 4.056   -19.736 -50.038 1.00 172.44 ? 93  CYS L SG  1 
ATOM   3739 N N   . MET C 3 94  ? 4.823   -15.421 -48.279 1.00 131.98 ? 94  MET L N   1 
ATOM   3740 C CA  . MET C 3 94  ? 5.503   -14.471 -47.362 1.00 146.90 ? 94  MET L CA  1 
ATOM   3741 C C   . MET C 3 94  ? 5.861   -15.168 -46.050 1.00 157.86 ? 94  MET L C   1 
ATOM   3742 O O   . MET C 3 94  ? 5.218   -16.184 -45.720 1.00 163.53 ? 94  MET L O   1 
ATOM   3743 C CB  . MET C 3 94  ? 4.615   -13.262 -47.061 1.00 141.59 ? 94  MET L CB  1 
ATOM   3744 C CG  . MET C 3 94  ? 5.345   -12.134 -46.364 1.00 163.52 ? 94  MET L CG  1 
ATOM   3745 S SD  . MET C 3 94  ? 6.978   -11.874 -47.092 1.00 231.44 ? 94  MET L SD  1 
ATOM   3746 C CE  . MET C 3 94  ? 7.632   -10.600 -46.015 1.00 180.27 ? 94  MET L CE  1 
ATOM   3747 N N   . GLN C 3 95  ? 6.847   -14.625 -45.336 1.00 165.10 ? 95  GLN L N   1 
ATOM   3748 C CA  . GLN C 3 95  ? 7.269   -15.195 -44.033 1.00 168.94 ? 95  GLN L CA  1 
ATOM   3749 C C   . GLN C 3 95  ? 6.071   -15.222 -43.083 1.00 134.70 ? 95  GLN L C   1 
ATOM   3750 O O   . GLN C 3 95  ? 5.286   -14.253 -43.094 1.00 109.14 ? 95  GLN L O   1 
ATOM   3751 C CB  . GLN C 3 95  ? 8.391   -14.318 -43.487 1.00 180.59 ? 95  GLN L CB  1 
ATOM   3752 C CG  . GLN C 3 95  ? 9.221   -13.693 -44.597 1.00 173.69 ? 95  GLN L CG  1 
ATOM   3753 C CD  . GLN C 3 95  ? 10.033  -12.520 -44.113 1.00 184.45 ? 95  GLN L CD  1 
ATOM   3754 O OE1 . GLN C 3 95  ? 9.510   -11.595 -43.495 0.52 184.69 ? 95  GLN L OE1 1 
ATOM   3755 N NE2 . GLN C 3 95  ? 11.329  -12.564 -44.372 1.00 196.88 ? 95  GLN L NE2 1 
ATOM   3756 N N   . GLY C 3 96  ? 5.942   -16.290 -42.292 1.00 122.43 ? 96  GLY L N   1 
ATOM   3757 C CA  . GLY C 3 96  ? 4.845   -16.371 -41.309 1.00 142.78 ? 96  GLY L CA  1 
ATOM   3758 C C   . GLY C 3 96  ? 5.009   -15.325 -40.222 1.00 143.21 ? 96  GLY L C   1 
ATOM   3759 O O   . GLY C 3 96  ? 6.137   -14.822 -40.053 1.00 110.23 ? 96  GLY L O   1 
ATOM   3760 N N   . THR C 3 97  ? 3.926   -15.000 -39.510 1.00 142.52 ? 97  THR L N   1 
ATOM   3761 C CA  . THR C 3 97  ? 4.020   -14.036 -38.380 1.00 104.11 ? 97  THR L CA  1 
ATOM   3762 C C   . THR C 3 97  ? 5.030   -14.576 -37.361 1.00 133.42 ? 97  THR L C   1 
ATOM   3763 O O   . THR C 3 97  ? 5.740   -13.753 -36.750 1.00 154.92 ? 97  THR L O   1 
ATOM   3764 C CB  . THR C 3 97  ? 2.640   -13.759 -37.773 1.00 105.80 ? 97  THR L CB  1 
ATOM   3765 O OG1 . THR C 3 97  ? 1.975   -15.008 -37.583 1.00 137.17 ? 97  THR L OG1 1 
ATOM   3766 C CG2 . THR C 3 97  ? 1.798   -12.859 -38.650 1.00 116.18 ? 97  THR L CG2 1 
ATOM   3767 N N   . HIS C 3 98  ? 5.151   -15.897 -37.234 1.00 132.06 ? 98  HIS L N   1 
ATOM   3768 C CA  . HIS C 3 98  ? 6.206   -16.449 -36.344 1.00 151.80 ? 98  HIS L CA  1 
ATOM   3769 C C   . HIS C 3 98  ? 7.527   -15.767 -36.712 1.00 155.92 ? 98  HIS L C   1 
ATOM   3770 O O   . HIS C 3 98  ? 7.685   -15.385 -37.875 1.00 139.18 ? 98  HIS L O   1 
ATOM   3771 C CB  . HIS C 3 98  ? 6.291   -17.968 -36.500 1.00 146.37 ? 98  HIS L CB  1 
ATOM   3772 C CG  . HIS C 3 98  ? 6.797   -18.696 -35.302 1.00 159.23 ? 98  HIS L CG  1 
ATOM   3773 N ND1 . HIS C 3 98  ? 7.140   -20.030 -35.341 1.00 144.21 ? 98  HIS L ND1 1 
ATOM   3774 C CD2 . HIS C 3 98  ? 7.024   -18.292 -34.047 1.00 146.36 ? 98  HIS L CD2 1 
ATOM   3775 C CE1 . HIS C 3 98  ? 7.558   -20.408 -34.142 1.00 127.00 ? 98  HIS L CE1 1 
ATOM   3776 N NE2 . HIS C 3 98  ? 7.496   -19.368 -33.341 1.00 118.85 ? 98  HIS L NE2 1 
ATOM   3777 N N   . TRP C 3 99  ? 8.409   -15.521 -35.745 1.00 160.98 ? 99  TRP L N   1 
ATOM   3778 C CA  . TRP C 3 99  ? 9.693   -14.902 -36.172 1.00 154.72 ? 99  TRP L CA  1 
ATOM   3779 C C   . TRP C 3 99  ? 10.406  -15.814 -37.176 1.00 147.57 ? 99  TRP L C   1 
ATOM   3780 O O   . TRP C 3 99  ? 11.047  -15.252 -38.080 1.00 154.73 ? 99  TRP L O   1 
ATOM   3781 C CB  . TRP C 3 99  ? 10.548  -14.447 -34.983 1.00 172.50 ? 99  TRP L CB  1 
ATOM   3782 C CG  . TRP C 3 99  ? 10.231  -13.015 -34.686 1.00 190.48 ? 99  TRP L CG  1 
ATOM   3783 C CD1 . TRP C 3 99  ? 9.365   -12.544 -33.744 1.00 205.15 ? 99  TRP L CD1 1 
ATOM   3784 C CD2 . TRP C 3 99  ? 10.689  -11.864 -35.416 1.00 200.69 ? 99  TRP L CD2 1 
ATOM   3785 N NE1 . TRP C 3 99  ? 9.295   -11.178 -33.799 1.00 211.17 ? 99  TRP L NE1 1 
ATOM   3786 C CE2 . TRP C 3 99  ? 10.095  -10.733 -34.817 1.00 204.44 ? 99  TRP L CE2 1 
ATOM   3787 C CE3 . TRP C 3 99  ? 11.558  -11.675 -36.496 1.00 190.68 ? 99  TRP L CE3 1 
ATOM   3788 C CZ2 . TRP C 3 99  ? 10.344  -9.437  -35.263 1.00 198.61 ? 99  TRP L CZ2 1 
ATOM   3789 C CZ3 . TRP C 3 99  ? 11.810  -10.395 -36.930 1.00 188.88 ? 99  TRP L CZ3 1 
ATOM   3790 C CH2 . TRP C 3 99  ? 11.199  -9.294  -36.330 1.00 191.27 ? 99  TRP L CH2 1 
ATOM   3791 N N   . PRO C 3 100 ? 10.402  -17.165 -37.050 1.00 131.00 ? 100 PRO L N   1 
ATOM   3792 C CA  . PRO C 3 100 ? 10.918  -18.032 -38.112 1.00 111.76 ? 100 PRO L CA  1 
ATOM   3793 C C   . PRO C 3 100 ? 10.140  -17.363 -39.252 1.00 122.23 ? 100 PRO L C   1 
ATOM   3794 O O   . PRO C 3 100 ? 8.924   -17.359 -39.201 1.00 124.97 ? 100 PRO L O   1 
ATOM   3795 C CB  . PRO C 3 100 ? 10.448  -19.428 -37.696 1.00 120.44 ? 100 PRO L CB  1 
ATOM   3796 C CG  . PRO C 3 100 ? 10.490  -19.376 -36.191 1.00 120.57 ? 100 PRO L CG  1 
ATOM   3797 C CD  . PRO C 3 100 ? 10.116  -17.950 -35.842 1.00 130.49 ? 100 PRO L CD  1 
ATOM   3798 N N   . TYR C 3 101 ? 10.852  -16.793 -40.225 1.00 128.33 ? 101 TYR L N   1 
ATOM   3799 C CA  . TYR C 3 101 ? 10.220  -16.082 -41.364 1.00 130.65 ? 101 TYR L CA  1 
ATOM   3800 C C   . TYR C 3 101 ? 10.331  -17.163 -42.435 1.00 149.78 ? 101 TYR L C   1 
ATOM   3801 O O   . TYR C 3 101 ? 11.441  -17.716 -42.564 1.00 159.25 ? 101 TYR L O   1 
ATOM   3802 C CB  . TYR C 3 101 ? 11.027  -14.834 -41.714 1.00 120.37 ? 101 TYR L CB  1 
ATOM   3803 C CG  . TYR C 3 101 ? 10.604  -13.602 -40.956 1.00 120.75 ? 101 TYR L CG  1 
ATOM   3804 C CD1 . TYR C 3 101 ? 9.402   -13.573 -40.269 1.00 126.63 ? 101 TYR L CD1 1 
ATOM   3805 C CD2 . TYR C 3 101 ? 11.391  -12.463 -40.935 1.00 132.98 ? 101 TYR L CD2 1 
ATOM   3806 C CE1 . TYR C 3 101 ? 8.994   -12.450 -39.573 1.00 132.22 ? 101 TYR L CE1 1 
ATOM   3807 C CE2 . TYR C 3 101 ? 10.993  -11.327 -40.252 1.00 137.98 ? 101 TYR L CE2 1 
ATOM   3808 C CZ  . TYR C 3 101 ? 9.791   -11.321 -39.568 1.00 131.93 ? 101 TYR L CZ  1 
ATOM   3809 O OH  . TYR C 3 101 ? 9.383   -10.204 -38.881 1.00 131.26 ? 101 TYR L OH  1 
ATOM   3810 N N   . THR C 3 102 ? 9.257   -17.459 -43.197 1.00 144.78 ? 102 THR L N   1 
ATOM   3811 C CA  . THR C 3 102 ? 9.487   -18.582 -44.105 1.00 151.53 ? 102 THR L CA  1 
ATOM   3812 C C   . THR C 3 102 ? 8.969   -18.150 -45.470 1.00 148.27 ? 102 THR L C   1 
ATOM   3813 O O   . THR C 3 102 ? 7.782   -17.839 -45.619 1.00 161.78 ? 102 THR L O   1 
ATOM   3814 C CB  . THR C 3 102 ? 8.640   -19.727 -43.548 1.00 153.51 ? 102 THR L CB  1 
ATOM   3815 O OG1 . THR C 3 102 ? 7.350   -19.229 -43.172 1.00 134.69 ? 102 THR L OG1 1 
ATOM   3816 C CG2 . THR C 3 102 ? 9.317   -20.345 -42.336 1.00 169.45 ? 102 THR L CG2 1 
ATOM   3817 N N   . PHE C 3 103 ? 9.864   -18.118 -46.459 1.00 156.25 ? 103 PHE L N   1 
ATOM   3818 C CA  . PHE C 3 103 ? 9.462   -17.739 -47.837 1.00 153.66 ? 103 PHE L CA  1 
ATOM   3819 C C   . PHE C 3 103 ? 8.842   -18.956 -48.520 1.00 155.82 ? 103 PHE L C   1 
ATOM   3820 O O   . PHE C 3 103 ? 7.991   -18.781 -49.410 1.00 161.64 ? 103 PHE L O   1 
ATOM   3821 C CB  . PHE C 3 103 ? 10.673  -17.261 -48.638 1.00 155.28 ? 103 PHE L CB  1 
ATOM   3822 C CG  . PHE C 3 103 ? 11.291  -15.977 -48.150 1.00 156.02 ? 103 PHE L CG  1 
ATOM   3823 C CD1 . PHE C 3 103 ? 10.575  -14.793 -48.170 1.00 154.38 ? 103 PHE L CD1 1 
ATOM   3824 C CD2 . PHE C 3 103 ? 12.588  -15.955 -47.667 1.00 168.62 ? 103 PHE L CD2 1 
ATOM   3825 C CE1 . PHE C 3 103 ? 11.144  -13.614 -47.719 1.00 168.74 ? 103 PHE L CE1 1 
ATOM   3826 C CE2 . PHE C 3 103 ? 13.156  -14.775 -47.216 1.00 172.85 ? 103 PHE L CE2 1 
ATOM   3827 C CZ  . PHE C 3 103 ? 12.433  -13.607 -47.243 1.00 175.49 ? 103 PHE L CZ  1 
ATOM   3828 N N   . GLY C 3 104 ? 9.265   -20.151 -48.110 1.00 138.50 ? 104 GLY L N   1 
ATOM   3829 C CA  . GLY C 3 104 ? 8.762   -21.379 -48.750 1.00 122.89 ? 104 GLY L CA  1 
ATOM   3830 C C   . GLY C 3 104 ? 9.517   -21.666 -50.031 1.00 133.04 ? 104 GLY L C   1 
ATOM   3831 O O   . GLY C 3 104 ? 10.601  -21.085 -50.219 1.00 133.69 ? 104 GLY L O   1 
ATOM   3832 N N   . GLN C 3 105 ? 8.963   -22.527 -50.884 1.00 141.89 ? 105 GLN L N   1 
ATOM   3833 C CA  . GLN C 3 105 ? 9.625   -22.889 -52.164 1.00 139.03 ? 105 GLN L CA  1 
ATOM   3834 C C   . GLN C 3 105 ? 9.123   -21.889 -53.205 1.00 144.44 ? 105 GLN L C   1 
ATOM   3835 O O   . GLN C 3 105 ? 8.433   -20.939 -52.813 1.00 150.14 ? 105 GLN L O   1 
ATOM   3836 C CB  . GLN C 3 105 ? 9.134   -24.258 -52.633 1.00 138.64 ? 105 GLN L CB  1 
ATOM   3837 C CG  . GLN C 3 105 ? 9.571   -25.399 -51.726 1.00 143.41 ? 105 GLN L CG  1 
ATOM   3838 C CD  . GLN C 3 105 ? 9.012   -26.727 -52.173 1.00 146.11 ? 105 GLN L CD  1 
ATOM   3839 O OE1 . GLN C 3 105 ? 7.980   -26.797 -52.835 1.00 158.11 ? 105 GLN L OE1 1 
ATOM   3840 N NE2 . GLN C 3 105 ? 9.692   -27.799 -51.803 1.00 166.49 ? 105 GLN L NE2 1 
ATOM   3841 N N   . GLY C 3 106 ? 9.435   -22.116 -54.482 1.00 140.14 ? 106 GLY L N   1 
ATOM   3842 C CA  . GLY C 3 106 ? 9.032   -21.172 -55.542 1.00 146.41 ? 106 GLY L CA  1 
ATOM   3843 C C   . GLY C 3 106 ? 8.041   -21.679 -56.572 1.00 135.21 ? 106 GLY L C   1 
ATOM   3844 O O   . GLY C 3 106 ? 7.881   -22.905 -56.672 1.00 149.62 ? 106 GLY L O   1 
ATOM   3845 N N   . THR C 3 107 ? 7.393   -20.772 -57.305 1.00 136.49 ? 107 THR L N   1 
ATOM   3846 C CA  . THR C 3 107 ? 6.463   -21.191 -58.385 1.00 137.65 ? 107 THR L CA  1 
ATOM   3847 C C   . THR C 3 107 ? 6.856   -20.476 -59.679 1.00 140.81 ? 107 THR L C   1 
ATOM   3848 O O   . THR C 3 107 ? 6.907   -19.233 -59.662 1.00 132.50 ? 107 THR L O   1 
ATOM   3849 C CB  . THR C 3 107 ? 5.009   -20.915 -57.994 1.00 139.69 ? 107 THR L CB  1 
ATOM   3850 O OG1 . THR C 3 107 ? 4.914   -19.527 -57.678 1.00 149.95 ? 107 THR L OG1 1 
ATOM   3851 C CG2 . THR C 3 107 ? 4.550   -21.741 -56.813 1.00 137.45 ? 107 THR L CG2 1 
ATOM   3852 N N   . LYS C 3 108 ? 7.121   -21.231 -60.748 1.00 125.67 ? 108 LYS L N   1 
ATOM   3853 C CA  . LYS C 3 108 ? 7.585   -20.623 -62.023 1.00 127.45 ? 108 LYS L CA  1 
ATOM   3854 C C   . LYS C 3 108 ? 6.444   -20.576 -63.041 1.00 133.16 ? 108 LYS L C   1 
ATOM   3855 O O   . LYS C 3 108 ? 5.633   -21.518 -63.064 1.00 135.79 ? 108 LYS L O   1 
ATOM   3856 C CB  . LYS C 3 108 ? 8.766   -21.416 -62.584 1.00 114.13 ? 108 LYS L CB  1 
ATOM   3857 C CG  . LYS C 3 108 ? 9.937   -21.613 -61.632 1.00 115.10 ? 108 LYS L CG  1 
ATOM   3858 C CD  . LYS C 3 108 ? 11.051  -22.435 -62.240 1.00 98.19  ? 108 LYS L CD  1 
ATOM   3859 C CE  . LYS C 3 108 ? 12.222  -22.635 -61.302 1.00 113.09 ? 108 LYS L CE  1 
ATOM   3860 N NZ  . LYS C 3 108 ? 13.289  -23.451 -61.928 1.00 103.48 ? 108 LYS L NZ  1 
ATOM   3861 N N   . LEU C 3 109 ? 6.399   -19.522 -63.858 1.00 143.46 ? 109 LEU L N   1 
ATOM   3862 C CA  . LEU C 3 109 ? 5.306   -19.383 -64.860 1.00 136.51 ? 109 LEU L CA  1 
ATOM   3863 C C   . LEU C 3 109 ? 5.865   -19.592 -66.267 1.00 146.75 ? 109 LEU L C   1 
ATOM   3864 O O   . LEU C 3 109 ? 7.054   -19.298 -66.465 1.00 156.19 ? 109 LEU L O   1 
ATOM   3865 C CB  . LEU C 3 109 ? 4.652   -18.004 -64.751 1.00 30.00  ? 109 LEU L CB  1 
ATOM   3866 C CG  . LEU C 3 109 ? 3.920   -17.703 -63.440 1.00 30.00  ? 109 LEU L CG  1 
ATOM   3867 C CD1 . LEU C 3 109 ? 3.449   -16.257 -63.409 1.00 30.00  ? 109 LEU L CD1 1 
ATOM   3868 C CD2 . LEU C 3 109 ? 2.752   -18.656 -63.244 1.00 30.00  ? 109 LEU L CD2 1 
ATOM   3869 N N   . GLU C 3 110 ? 5.030   -20.007 -67.227 1.00 144.90 ? 110 GLU L N   1 
ATOM   3870 C CA  . GLU C 3 110 ? 5.490   -20.112 -68.641 1.00 145.71 ? 110 GLU L CA  1 
ATOM   3871 C C   . GLU C 3 110 ? 4.673   -19.128 -69.490 1.00 153.78 ? 110 GLU L C   1 
ATOM   3872 O O   . GLU C 3 110 ? 3.551   -18.786 -69.068 1.00 152.62 ? 110 GLU L O   1 
ATOM   3873 C CB  . GLU C 3 110 ? 5.396   -21.537 -69.188 1.00 165.00 ? 110 GLU L CB  1 
ATOM   3874 C CG  . GLU C 3 110 ? 6.423   -22.479 -68.587 1.00 152.01 ? 110 GLU L CG  1 
ATOM   3875 C CD  . GLU C 3 110 ? 6.621   -23.768 -69.364 1.00 162.30 ? 110 GLU L CD  1 
ATOM   3876 O OE1 . GLU C 3 110 ? 5.949   -23.940 -70.401 1.00 174.96 ? 110 GLU L OE1 1 
ATOM   3877 O OE2 . GLU C 3 110 ? 7.448   -24.596 -68.934 1.00 152.40 ? 110 GLU L OE2 1 
ATOM   3878 N N   . ILE C 3 111 ? 5.211   -18.694 -70.637 1.00 166.38 ? 111 ILE L N   1 
ATOM   3879 C CA  . ILE C 3 111 ? 4.510   -17.691 -71.482 1.00 167.66 ? 111 ILE L CA  1 
ATOM   3880 C C   . ILE C 3 111 ? 3.213   -18.129 -72.148 1.00 174.60 ? 111 ILE L C   1 
ATOM   3881 O O   . ILE C 3 111 ? 2.225   -17.373 -72.076 1.00 177.18 ? 111 ILE L O   1 
ATOM   3882 C CB  . ILE C 3 111 ? 5.426   -17.219 -72.646 1.00 185.02 ? 111 ILE L CB  1 
ATOM   3883 C CG1 . ILE C 3 111 ? 6.676   -16.492 -72.146 1.00 185.01 ? 111 ILE L CG1 1 
ATOM   3884 C CG2 . ILE C 3 111 ? 4.648   -16.367 -73.637 1.00 199.00 ? 111 ILE L CG2 1 
ATOM   3885 C CD1 . ILE C 3 111 ? 6.406   -15.106 -71.612 1.00 157.46 ? 111 ILE L CD1 1 
ATOM   3886 N N   . LYS C 3 112 ? 3.275   -19.288 -72.810 1.00 181.06 ? 112 LYS L N   1 
ATOM   3887 C CA  . LYS C 3 112 ? 2.106   -19.865 -73.518 1.00 186.60 ? 112 LYS L CA  1 
ATOM   3888 C C   . LYS C 3 112 ? 2.236   -21.380 -73.359 1.00 193.67 ? 112 LYS L C   1 
ATOM   3889 O O   . LYS C 3 112 ? 2.946   -21.813 -72.432 1.00 202.77 ? 112 LYS L O   1 
ATOM   3890 C CB  . LYS C 3 112 ? 2.118   -19.468 -74.995 1.00 179.67 ? 112 LYS L CB  1 
ATOM   3891 C CG  . LYS C 3 112 ? 0.749   -19.350 -75.652 1.00 170.84 ? 112 LYS L CG  1 
ATOM   3892 C CD  . LYS C 3 112 ? 0.070   -18.033 -75.373 1.00 176.15 ? 112 LYS L CD  1 
ATOM   3893 C CE  . LYS C 3 112 ? -1.173  -17.821 -76.211 1.00 183.20 ? 112 LYS L CE  1 
ATOM   3894 N NZ  . LYS C 3 112 ? -2.363  -17.541 -75.374 1.00 202.54 ? 112 LYS L NZ  1 
ATOM   3895 N N   . ARG C 3 113 ? 1.609   -22.149 -74.244 1.00 190.67 ? 113 ARG L N   1 
ATOM   3896 C CA  . ARG C 3 113 ? 1.740   -23.627 -74.190 1.00 195.81 ? 113 ARG L CA  1 
ATOM   3897 C C   . ARG C 3 113 ? 1.744   -24.173 -75.621 1.00 217.43 ? 113 ARG L C   1 
ATOM   3898 O O   . ARG C 3 113 ? 0.768   -24.845 -76.002 1.00 243.69 ? 113 ARG L O   1 
ATOM   3899 C CB  . ARG C 3 113 ? 0.617   -24.217 -73.332 1.00 186.12 ? 113 ARG L CB  1 
ATOM   3900 C CG  . ARG C 3 113 ? 1.036   -24.512 -71.900 1.00 190.02 ? 113 ARG L CG  1 
ATOM   3901 C CD  . ARG C 3 113 ? -0.131  -24.920 -71.026 1.00 203.54 ? 113 ARG L CD  1 
ATOM   3902 N NE  . ARG C 3 113 ? -0.685  -23.791 -70.298 1.00 200.71 ? 113 ARG L NE  1 
ATOM   3903 C CZ  . ARG C 3 113 ? -1.872  -23.796 -69.705 1.00 185.29 ? 113 ARG L CZ  1 
ATOM   3904 N NH1 . ARG C 3 113 ? -2.973  -23.718 -70.431 1.00 171.81 ? 113 ARG L NH1 1 
ATOM   3905 N NH2 . ARG C 3 113 ? -1.956  -23.880 -68.389 1.00 179.52 ? 113 ARG L NH2 1 
ATOM   3906 N N   . THR C 3 114 ? 2.804   -23.885 -76.378 1.00 192.72 ? 114 THR L N   1 
ATOM   3907 C CA  . THR C 3 114 ? 2.921   -24.399 -77.767 1.00 183.33 ? 114 THR L CA  1 
ATOM   3908 C C   . THR C 3 114 ? 3.631   -25.754 -77.727 1.00 182.78 ? 114 THR L C   1 
ATOM   3909 O O   . THR C 3 114 ? 3.782   -26.305 -76.621 1.00 184.80 ? 114 THR L O   1 
ATOM   3910 C CB  . THR C 3 114 ? 3.666   -23.391 -78.648 1.00 165.06 ? 114 THR L CB  1 
ATOM   3911 O OG1 . THR C 3 114 ? 5.062   -23.675 -78.561 1.00 156.17 ? 114 THR L OG1 1 
ATOM   3912 C CG2 . THR C 3 114 ? 3.417   -21.956 -78.237 1.00 114.22 ? 114 THR L CG2 1 
ATOM   3913 N N   . VAL C 3 115 ? 4.063   -26.263 -78.882 1.00 158.72 ? 115 VAL L N   1 
ATOM   3914 C CA  . VAL C 3 115 ? 4.840   -27.538 -78.889 1.00 143.25 ? 115 VAL L CA  1 
ATOM   3915 C C   . VAL C 3 115 ? 6.310   -27.220 -79.167 1.00 167.11 ? 115 VAL L C   1 
ATOM   3916 O O   . VAL C 3 115 ? 6.619   -26.043 -79.424 1.00 167.60 ? 115 VAL L O   1 
ATOM   3917 C CB  . VAL C 3 115 ? 4.389   -28.483 -80.015 1.00 139.13 ? 115 VAL L CB  1 
ATOM   3918 C CG1 . VAL C 3 115 ? 4.209   -29.906 -79.511 1.00 116.20 ? 115 VAL L CG1 1 
ATOM   3919 C CG2 . VAL C 3 115 ? 3.119   -27.988 -80.689 1.00 119.97 ? 115 VAL L CG2 1 
ATOM   3920 N N   . ALA C 3 116 ? 7.176   -28.234 -79.133 1.00 167.93 ? 116 ALA L N   1 
ATOM   3921 C CA  . ALA C 3 116 ? 8.630   -28.005 -79.299 1.00 176.47 ? 116 ALA L CA  1 
ATOM   3922 C C   . ALA C 3 116 ? 9.155   -28.114 -80.731 1.00 192.22 ? 116 ALA L C   1 
ATOM   3923 O O   . ALA C 3 116 ? 8.640   -28.971 -81.471 1.00 218.13 ? 116 ALA L O   1 
ATOM   3924 C CB  . ALA C 3 116 ? 9.280   -29.051 -78.434 1.00 165.44 ? 116 ALA L CB  1 
ATOM   3925 N N   . ALA C 3 117 ? 10.148  -27.299 -81.104 1.00 196.78 ? 117 ALA L N   1 
ATOM   3926 C CA  . ALA C 3 117 ? 10.752  -27.478 -82.448 1.00 188.68 ? 117 ALA L CA  1 
ATOM   3927 C C   . ALA C 3 117 ? 12.253  -27.180 -82.352 1.00 197.49 ? 117 ALA L C   1 
ATOM   3928 O O   . ALA C 3 117 ? 12.692  -26.176 -82.947 1.00 194.03 ? 117 ALA L O   1 
ATOM   3929 C CB  . ALA C 3 117 ? 10.069  -26.577 -83.446 1.00 169.63 ? 117 ALA L CB  1 
ATOM   3930 N N   . PRO C 3 118 ? 13.059  -27.990 -81.629 1.00 198.20 ? 118 PRO L N   1 
ATOM   3931 C CA  . PRO C 3 118 ? 14.489  -27.692 -81.406 1.00 187.70 ? 118 PRO L CA  1 
ATOM   3932 C C   . PRO C 3 118 ? 15.467  -27.879 -82.570 1.00 191.58 ? 118 PRO L C   1 
ATOM   3933 O O   . PRO C 3 118 ? 15.354  -28.858 -83.284 1.00 194.61 ? 118 PRO L O   1 
ATOM   3934 C CB  . PRO C 3 118 ? 14.893  -28.697 -80.311 1.00 170.91 ? 118 PRO L CB  1 
ATOM   3935 C CG  . PRO C 3 118 ? 13.579  -29.143 -79.722 1.00 181.46 ? 118 PRO L CG  1 
ATOM   3936 C CD  . PRO C 3 118 ? 12.646  -29.192 -80.912 1.00 180.24 ? 118 PRO L CD  1 
ATOM   3937 N N   . SER C 3 119 ? 16.401  -26.936 -82.717 1.00 188.36 ? 119 SER L N   1 
ATOM   3938 C CA  . SER C 3 119 ? 17.463  -27.093 -83.741 1.00 168.30 ? 119 SER L CA  1 
ATOM   3939 C C   . SER C 3 119 ? 18.698  -27.636 -83.025 1.00 162.13 ? 119 SER L C   1 
ATOM   3940 O O   . SER C 3 119 ? 19.355  -26.859 -82.312 1.00 178.32 ? 119 SER L O   1 
ATOM   3941 C CB  . SER C 3 119 ? 17.742  -25.807 -84.466 1.00 177.31 ? 119 SER L CB  1 
ATOM   3942 O OG  . SER C 3 119 ? 18.314  -24.847 -83.595 1.00 199.21 ? 119 SER L OG  1 
ATOM   3943 N N   . VAL C 3 120 ? 18.976  -28.924 -83.187 1.00 160.41 ? 120 VAL L N   1 
ATOM   3944 C CA  . VAL C 3 120 ? 20.083  -29.581 -82.498 1.00 158.35 ? 120 VAL L CA  1 
ATOM   3945 C C   . VAL C 3 120 ? 21.372  -29.351 -83.275 1.00 166.93 ? 120 VAL L C   1 
ATOM   3946 O O   . VAL C 3 120 ? 21.386  -29.393 -84.513 1.00 188.53 ? 120 VAL L O   1 
ATOM   3947 C CB  . VAL C 3 120 ? 19.807  -31.086 -82.309 1.00 145.28 ? 120 VAL L CB  1 
ATOM   3948 C CG1 . VAL C 3 120 ? 20.951  -31.750 -81.561 1.00 134.78 ? 120 VAL L CG1 1 
ATOM   3949 C CG2 . VAL C 3 120 ? 18.501  -31.288 -81.554 1.00 142.85 ? 120 VAL L CG2 1 
ATOM   3950 N N   . PHE C 3 121 ? 22.455  -29.089 -82.543 1.00 165.49 ? 121 PHE L N   1 
ATOM   3951 C CA  . PHE C 3 121 ? 23.776  -28.914 -83.124 1.00 130.25 ? 121 PHE L CA  1 
ATOM   3952 C C   . PHE C 3 121 ? 24.801  -29.513 -82.175 1.00 134.40 ? 121 PHE L C   1 
ATOM   3953 O O   . PHE C 3 121 ? 24.516  -29.755 -81.000 1.00 144.34 ? 121 PHE L O   1 
ATOM   3954 C CB  . PHE C 3 121 ? 24.108  -27.437 -83.365 1.00 142.75 ? 121 PHE L CB  1 
ATOM   3955 C CG  . PHE C 3 121 ? 23.138  -26.738 -84.265 1.00 162.07 ? 121 PHE L CG  1 
ATOM   3956 C CD1 . PHE C 3 121 ? 23.213  -26.885 -85.632 1.00 180.15 ? 121 PHE L CD1 1 
ATOM   3957 C CD2 . PHE C 3 121 ? 22.158  -25.916 -83.736 1.00 173.03 ? 121 PHE L CD2 1 
ATOM   3958 C CE1 . PHE C 3 121 ? 22.326  -26.233 -86.459 1.00 202.98 ? 121 PHE L CE1 1 
ATOM   3959 C CE2 . PHE C 3 121 ? 21.266  -25.264 -84.556 1.00 181.59 ? 121 PHE L CE2 1 
ATOM   3960 C CZ  . PHE C 3 121 ? 21.348  -25.422 -85.918 1.00 201.93 ? 121 PHE L CZ  1 
ATOM   3961 N N   . ILE C 3 122 ? 26.005  -29.749 -82.693 1.00 118.80 ? 122 ILE L N   1 
ATOM   3962 C CA  . ILE C 3 122 ? 27.130  -30.184 -81.874 1.00 140.61 ? 122 ILE L CA  1 
ATOM   3963 C C   . ILE C 3 122 ? 28.378  -29.471 -82.373 1.00 143.30 ? 122 ILE L C   1 
ATOM   3964 O O   . ILE C 3 122 ? 28.503  -29.158 -83.561 1.00 153.57 ? 122 ILE L O   1 
ATOM   3965 C CB  . ILE C 3 122 ? 27.326  -31.715 -81.907 1.00 132.32 ? 122 ILE L CB  1 
ATOM   3966 C CG1 . ILE C 3 122 ? 26.135  -32.435 -81.300 1.00 135.16 ? 122 ILE L CG1 1 
ATOM   3967 C CG2 . ILE C 3 122 ? 28.559  -32.141 -81.133 1.00 143.88 ? 122 ILE L CG2 1 
ATOM   3968 C CD1 . ILE C 3 122 ? 26.184  -33.891 -81.571 1.00 145.12 ? 122 ILE L CD1 1 
ATOM   3969 N N   . PHE C 3 123 ? 29.307  -29.218 -81.459 1.00 147.12 ? 123 PHE L N   1 
ATOM   3970 C CA  . PHE C 3 123 ? 30.510  -28.448 -81.761 1.00 156.39 ? 123 PHE L CA  1 
ATOM   3971 C C   . PHE C 3 123 ? 31.752  -29.203 -81.317 1.00 162.31 ? 123 PHE L C   1 
ATOM   3972 O O   . PHE C 3 123 ? 32.003  -29.312 -80.098 1.00 155.88 ? 123 PHE L O   1 
ATOM   3973 C CB  . PHE C 3 123 ? 30.435  -27.089 -81.080 1.00 152.76 ? 123 PHE L CB  1 
ATOM   3974 C CG  . PHE C 3 123 ? 29.287  -26.265 -81.541 1.00 144.08 ? 123 PHE L CG  1 
ATOM   3975 C CD1 . PHE C 3 123 ? 29.272  -25.725 -82.814 1.00 147.60 ? 123 PHE L CD1 1 
ATOM   3976 C CD2 . PHE C 3 123 ? 28.202  -26.057 -80.711 1.00 139.73 ? 123 PHE L CD2 1 
ATOM   3977 C CE1 . PHE C 3 123 ? 28.204  -24.974 -83.239 1.00 146.49 ? 123 PHE L CE1 1 
ATOM   3978 C CE2 . PHE C 3 123 ? 27.133  -25.309 -81.131 1.00 142.15 ? 123 PHE L CE2 1 
ATOM   3979 C CZ  . PHE C 3 123 ? 27.134  -24.768 -82.393 1.00 150.47 ? 123 PHE L CZ  1 
ATOM   3980 N N   . PRO C 3 124 ? 32.551  -29.724 -82.242 1.00 162.23 ? 124 PRO L N   1 
ATOM   3981 C CA  . PRO C 3 124 ? 33.804  -30.372 -81.860 1.00 152.97 ? 124 PRO L CA  1 
ATOM   3982 C C   . PRO C 3 124 ? 34.789  -29.351 -81.323 1.00 167.14 ? 124 PRO L C   1 
ATOM   3983 O O   . PRO C 3 124 ? 34.693  -28.156 -81.642 1.00 175.44 ? 124 PRO L O   1 
ATOM   3984 C CB  . PRO C 3 124 ? 34.292  -30.989 -83.179 1.00 144.64 ? 124 PRO L CB  1 
ATOM   3985 C CG  . PRO C 3 124 ? 33.721  -30.094 -84.220 1.00 153.17 ? 124 PRO L CG  1 
ATOM   3986 C CD  . PRO C 3 124 ? 32.360  -29.714 -83.703 1.00 164.08 ? 124 PRO L CD  1 
ATOM   3987 N N   . PRO C 3 125 ? 35.745  -29.775 -80.500 1.00 163.90 ? 125 PRO L N   1 
ATOM   3988 C CA  . PRO C 3 125 ? 36.675  -28.814 -79.898 1.00 175.87 ? 125 PRO L CA  1 
ATOM   3989 C C   . PRO C 3 125 ? 37.720  -28.330 -80.892 1.00 183.29 ? 125 PRO L C   1 
ATOM   3990 O O   . PRO C 3 125 ? 38.274  -29.107 -81.674 1.00 186.87 ? 125 PRO L O   1 
ATOM   3991 C CB  . PRO C 3 125 ? 37.318  -29.622 -78.765 1.00 177.89 ? 125 PRO L CB  1 
ATOM   3992 C CG  . PRO C 3 125 ? 37.298  -31.024 -79.273 1.00 165.66 ? 125 PRO L CG  1 
ATOM   3993 C CD  . PRO C 3 125 ? 36.014  -31.156 -80.058 1.00 157.73 ? 125 PRO L CD  1 
ATOM   3994 N N   . SER C 3 126 ? 37.979  -27.024 -80.860 1.00 189.95 ? 126 SER L N   1 
ATOM   3995 C CA  . SER C 3 126 ? 39.077  -26.466 -81.635 1.00 180.97 ? 126 SER L CA  1 
ATOM   3996 C C   . SER C 3 126 ? 40.405  -26.994 -81.106 1.00 189.59 ? 126 SER L C   1 
ATOM   3997 O O   . SER C 3 126 ? 40.538  -27.330 -79.927 1.00 201.66 ? 126 SER L O   1 
ATOM   3998 C CB  . SER C 3 126 ? 39.059  -24.938 -81.578 1.00 175.89 ? 126 SER L CB  1 
ATOM   3999 O OG  . SER C 3 126 ? 39.566  -24.462 -80.342 1.00 199.71 ? 126 SER L OG  1 
ATOM   4000 N N   . ASP C 3 127 ? 41.399  -27.070 -81.996 1.00 184.15 ? 127 ASP L N   1 
ATOM   4001 C CA  . ASP C 3 127 ? 42.711  -27.567 -81.592 1.00 188.90 ? 127 ASP L CA  1 
ATOM   4002 C C   . ASP C 3 127 ? 43.373  -26.683 -80.544 1.00 208.76 ? 127 ASP L C   1 
ATOM   4003 O O   . ASP C 3 127 ? 44.309  -27.132 -79.874 1.00 226.02 ? 127 ASP L O   1 
ATOM   4004 C CB  . ASP C 3 127 ? 43.632  -27.705 -82.807 1.00 189.60 ? 127 ASP L CB  1 
ATOM   4005 C CG  . ASP C 3 127 ? 43.049  -28.600 -83.883 1.00 170.42 ? 127 ASP L CG  1 
ATOM   4006 O OD1 . ASP C 3 127 ? 41.924  -29.110 -83.692 1.00 171.29 ? 127 ASP L OD1 1 
ATOM   4007 O OD2 . ASP C 3 127 ? 43.719  -28.796 -84.918 1.00 173.94 ? 127 ASP L OD2 1 
ATOM   4008 N N   . GLU C 3 128 ? 42.903  -25.445 -80.380 1.00 185.94 ? 128 GLU L N   1 
ATOM   4009 C CA  . GLU C 3 128 ? 43.513  -24.531 -79.421 1.00 186.21 ? 128 GLU L CA  1 
ATOM   4010 C C   . GLU C 3 128 ? 43.351  -25.048 -77.993 1.00 190.32 ? 128 GLU L C   1 
ATOM   4011 O O   . GLU C 3 128 ? 44.333  -25.187 -77.254 1.00 194.05 ? 128 GLU L O   1 
ATOM   4012 C CB  . GLU C 3 128 ? 42.903  -23.137 -79.586 1.00 193.15 ? 128 GLU L CB  1 
ATOM   4013 C CG  . GLU C 3 128 ? 42.904  -22.636 -81.031 1.00 161.18 ? 128 GLU L CG  1 
ATOM   4014 C CD  . GLU C 3 128 ? 42.149  -21.332 -81.196 1.00 169.35 ? 128 GLU L CD  1 
ATOM   4015 O OE1 . GLU C 3 128 ? 41.623  -20.828 -80.185 1.00 213.65 ? 128 GLU L OE1 1 
ATOM   4016 O OE2 . GLU C 3 128 ? 42.061  -20.825 -82.335 1.00 114.31 ? 128 GLU L OE2 1 
ATOM   4017 N N   . GLN C 3 129 ? 42.111  -25.349 -77.588 1.00 192.21 ? 129 GLN L N   1 
ATOM   4018 C CA  . GLN C 3 129 ? 41.899  -25.988 -76.292 1.00 189.97 ? 129 GLN L CA  1 
ATOM   4019 C C   . GLN C 3 129 ? 42.385  -27.429 -76.297 1.00 196.54 ? 129 GLN L C   1 
ATOM   4020 O O   . GLN C 3 129 ? 42.788  -27.947 -75.250 1.00 198.68 ? 129 GLN L O   1 
ATOM   4021 C CB  . GLN C 3 129 ? 40.426  -25.940 -75.889 1.00 184.35 ? 129 GLN L CB  1 
ATOM   4022 C CG  . GLN C 3 129 ? 39.454  -26.465 -76.924 1.00 205.88 ? 129 GLN L CG  1 
ATOM   4023 C CD  . GLN C 3 129 ? 38.019  -26.350 -76.456 1.00 194.18 ? 129 GLN L CD  1 
ATOM   4024 O OE1 . GLN C 3 129 ? 37.756  -25.904 -75.340 1.00 154.54 ? 129 GLN L OE1 1 
ATOM   4025 N NE2 . GLN C 3 129 ? 37.082  -26.743 -77.308 1.00 223.52 ? 129 GLN L NE2 1 
ATOM   4026 N N   . LEU C 3 130 ? 42.358  -28.086 -77.460 1.00 216.82 ? 130 LEU L N   1 
ATOM   4027 C CA  . LEU C 3 130 ? 42.912  -29.422 -77.622 1.00 205.66 ? 130 LEU L CA  1 
ATOM   4028 C C   . LEU C 3 130 ? 44.416  -29.463 -77.385 1.00 208.77 ? 130 LEU L C   1 
ATOM   4029 O O   . LEU C 3 130 ? 45.004  -30.543 -77.481 1.00 208.98 ? 130 LEU L O   1 
ATOM   4030 C CB  . LEU C 3 130 ? 42.584  -29.965 -79.022 1.00 196.18 ? 130 LEU L CB  1 
ATOM   4031 C CG  . LEU C 3 130 ? 41.183  -30.545 -79.214 1.00 188.13 ? 130 LEU L CG  1 
ATOM   4032 C CD1 . LEU C 3 130 ? 41.080  -31.227 -80.565 1.00 174.34 ? 130 LEU L CD1 1 
ATOM   4033 C CD2 . LEU C 3 130 ? 40.814  -31.484 -78.072 1.00 187.65 ? 130 LEU L CD2 1 
ATOM   4034 N N   . LYS C 3 131 ? 45.048  -28.316 -77.112 1.00 184.29 ? 131 LYS L N   1 
ATOM   4035 C CA  . LYS C 3 131 ? 46.449  -28.232 -76.713 1.00 193.58 ? 131 LYS L CA  1 
ATOM   4036 C C   . LYS C 3 131 ? 46.622  -27.834 -75.257 1.00 182.70 ? 131 LYS L C   1 
ATOM   4037 O O   . LYS C 3 131 ? 47.641  -28.171 -74.654 1.00 162.23 ? 131 LYS L O   1 
ATOM   4038 C CB  . LYS C 3 131 ? 47.186  -27.217 -77.600 1.00 188.27 ? 131 LYS L CB  1 
ATOM   4039 C CG  . LYS C 3 131 ? 47.342  -27.667 -79.047 1.00 194.64 ? 131 LYS L CG  1 
ATOM   4040 C CD  . LYS C 3 131 ? 47.920  -26.573 -79.930 1.00 199.93 ? 131 LYS L CD  1 
ATOM   4041 C CE  . LYS C 3 131 ? 47.996  -27.036 -81.379 1.00 215.98 ? 131 LYS L CE  1 
ATOM   4042 N NZ  . LYS C 3 131 ? 48.540  -25.982 -82.278 1.00 208.63 ? 131 LYS L NZ  1 
ATOM   4043 N N   . SER C 3 132 ? 45.642  -27.123 -74.687 1.00 198.10 ? 132 SER L N   1 
ATOM   4044 C CA  . SER C 3 132 ? 45.704  -26.752 -73.277 1.00 176.10 ? 132 SER L CA  1 
ATOM   4045 C C   . SER C 3 132 ? 45.625  -27.974 -72.374 1.00 176.83 ? 132 SER L C   1 
ATOM   4046 O O   . SER C 3 132 ? 46.160  -27.956 -71.260 1.00 185.95 ? 132 SER L O   1 
ATOM   4047 C CB  . SER C 3 132 ? 44.576  -25.774 -72.938 1.00 163.60 ? 132 SER L CB  1 
ATOM   4048 O OG  . SER C 3 132 ? 43.307  -26.409 -72.977 1.00 149.28 ? 132 SER L OG  1 
ATOM   4049 N N   . GLY C 3 133 ? 44.966  -29.036 -72.827 1.00 193.38 ? 133 GLY L N   1 
ATOM   4050 C CA  . GLY C 3 133 ? 44.815  -30.229 -72.018 1.00 173.24 ? 133 GLY L CA  1 
ATOM   4051 C C   . GLY C 3 133 ? 43.369  -30.651 -71.894 1.00 157.49 ? 133 GLY L C   1 
ATOM   4052 O O   . GLY C 3 133 ? 43.054  -31.845 -71.876 1.00 160.01 ? 133 GLY L O   1 
ATOM   4053 N N   . THR C 3 134 ? 42.479  -29.669 -71.812 1.00 148.77 ? 134 THR L N   1 
ATOM   4054 C CA  . THR C 3 134 ? 41.056  -29.937 -71.687 1.00 149.10 ? 134 THR L CA  1 
ATOM   4055 C C   . THR C 3 134 ? 40.439  -30.176 -73.059 1.00 171.54 ? 134 THR L C   1 
ATOM   4056 O O   . THR C 3 134 ? 40.790  -29.515 -74.040 1.00 186.99 ? 134 THR L O   1 
ATOM   4057 C CB  . THR C 3 134 ? 40.356  -28.770 -70.991 1.00 175.53 ? 134 THR L CB  1 
ATOM   4058 O OG1 . THR C 3 134 ? 40.546  -27.573 -71.755 1.00 197.84 ? 134 THR L OG1 1 
ATOM   4059 C CG2 . THR C 3 134 ? 40.928  -28.567 -69.594 1.00 150.56 ? 134 THR L CG2 1 
ATOM   4060 N N   . ALA C 3 135 ? 39.517  -31.134 -73.124 1.00 161.46 ? 135 ALA L N   1 
ATOM   4061 C CA  . ALA C 3 135 ? 38.821  -31.481 -74.359 1.00 154.20 ? 135 ALA L CA  1 
ATOM   4062 C C   . ALA C 3 135 ? 37.331  -31.538 -74.060 1.00 153.36 ? 135 ALA L C   1 
ATOM   4063 O O   . ALA C 3 135 ? 36.876  -32.422 -73.327 1.00 169.37 ? 135 ALA L O   1 
ATOM   4064 C CB  . ALA C 3 135 ? 39.319  -32.813 -74.920 1.00 148.40 ? 135 ALA L CB  1 
ATOM   4065 N N   . SER C 3 136 ? 36.570  -30.605 -74.627 1.00 144.31 ? 136 SER L N   1 
ATOM   4066 C CA  . SER C 3 136 ? 35.149  -30.501 -74.338 1.00 157.22 ? 136 SER L CA  1 
ATOM   4067 C C   . SER C 3 136 ? 34.346  -30.373 -75.622 1.00 140.61 ? 136 SER L C   1 
ATOM   4068 O O   . SER C 3 136 ? 34.775  -29.714 -76.574 1.00 151.72 ? 136 SER L O   1 
ATOM   4069 C CB  . SER C 3 136 ? 34.858  -29.313 -73.432 1.00 171.21 ? 136 SER L CB  1 
ATOM   4070 O OG  . SER C 3 136 ? 35.196  -28.103 -74.083 1.00 211.72 ? 136 SER L OG  1 
ATOM   4071 N N   . VAL C 3 137 ? 33.173  -31.001 -75.633 1.00 118.45 ? 137 VAL L N   1 
ATOM   4072 C CA  . VAL C 3 137 ? 32.270  -30.991 -76.775 1.00 146.68 ? 137 VAL L CA  1 
ATOM   4073 C C   . VAL C 3 137 ? 30.906  -30.514 -76.296 1.00 150.72 ? 137 VAL L C   1 
ATOM   4074 O O   . VAL C 3 137 ? 30.448  -30.903 -75.216 1.00 157.75 ? 137 VAL L O   1 
ATOM   4075 C CB  . VAL C 3 137 ? 32.173  -32.385 -77.431 1.00 147.71 ? 137 VAL L CB  1 
ATOM   4076 C CG1 . VAL C 3 137 ? 31.143  -32.388 -78.546 1.00 148.11 ? 137 VAL L CG1 1 
ATOM   4077 C CG2 . VAL C 3 137 ? 33.534  -32.815 -77.957 1.00 136.17 ? 137 VAL L CG2 1 
ATOM   4078 N N   . VAL C 3 138 ? 30.259  -29.670 -77.095 1.00 146.35 ? 138 VAL L N   1 
ATOM   4079 C CA  . VAL C 3 138 ? 29.019  -29.008 -76.712 1.00 140.30 ? 138 VAL L CA  1 
ATOM   4080 C C   . VAL C 3 138 ? 27.891  -29.501 -77.610 1.00 150.71 ? 138 VAL L C   1 
ATOM   4081 O O   . VAL C 3 138 ? 28.039  -29.536 -78.837 1.00 181.77 ? 138 VAL L O   1 
ATOM   4082 C CB  . VAL C 3 138 ? 29.156  -27.477 -76.800 1.00 149.11 ? 138 VAL L CB  1 
ATOM   4083 C CG1 . VAL C 3 138 ? 27.836  -26.807 -76.476 1.00 152.46 ? 138 VAL L CG1 1 
ATOM   4084 C CG2 . VAL C 3 138 ? 30.257  -26.984 -75.870 1.00 160.40 ? 138 VAL L CG2 1 
ATOM   4085 N N   . CYS C 3 139 ? 26.771  -29.887 -76.996 1.00 145.36 ? 139 CYS L N   1 
ATOM   4086 C CA  . CYS C 3 139 ? 25.571  -30.247 -77.792 1.00 141.22 ? 139 CYS L CA  1 
ATOM   4087 C C   . CYS C 3 139 ? 24.612  -29.068 -77.655 1.00 135.42 ? 139 CYS L C   1 
ATOM   4088 O O   . CYS C 3 139 ? 24.433  -28.604 -76.518 1.00 159.18 ? 139 CYS L O   1 
ATOM   4089 C CB  . CYS C 3 139 ? 24.903  -31.504 -77.257 1.00 152.78 ? 139 CYS L CB  1 
ATOM   4090 S SG  . CYS C 3 139 ? 23.374  -31.926 -78.132 1.00 125.30 ? 139 CYS L SG  1 
ATOM   4091 N N   . LEU C 3 140 ? 24.032  -28.588 -78.752 1.00 123.28 ? 140 LEU L N   1 
ATOM   4092 C CA  . LEU C 3 140 ? 23.201  -27.361 -78.642 1.00 138.24 ? 140 LEU L CA  1 
ATOM   4093 C C   . LEU C 3 140 ? 21.741  -27.661 -78.973 1.00 122.04 ? 140 LEU L C   1 
ATOM   4094 O O   . LEU C 3 140 ? 21.499  -28.381 -79.952 1.00 125.91 ? 140 LEU L O   1 
ATOM   4095 C CB  . LEU C 3 140 ? 23.761  -26.299 -79.590 1.00 146.13 ? 140 LEU L CB  1 
ATOM   4096 C CG  . LEU C 3 140 ? 22.953  -25.005 -79.675 1.00 139.71 ? 140 LEU L CG  1 
ATOM   4097 C CD1 . LEU C 3 140 ? 23.089  -24.197 -78.395 1.00 139.46 ? 140 LEU L CD1 1 
ATOM   4098 C CD2 . LEU C 3 140 ? 23.387  -24.175 -80.872 1.00 143.20 ? 140 LEU L CD2 1 
ATOM   4099 N N   . LEU C 3 141 ? 20.817  -27.118 -78.182 1.00 124.46 ? 141 LEU L N   1 
ATOM   4100 C CA  . LEU C 3 141 ? 19.369  -27.278 -78.459 1.00 128.57 ? 141 LEU L CA  1 
ATOM   4101 C C   . LEU C 3 141 ? 18.765  -25.875 -78.426 1.00 135.48 ? 141 LEU L C   1 
ATOM   4102 O O   . LEU C 3 141 ? 18.910  -25.214 -77.388 1.00 150.52 ? 141 LEU L O   1 
ATOM   4103 C CB  . LEU C 3 141 ? 18.749  -28.160 -77.374 1.00 131.90 ? 141 LEU L CB  1 
ATOM   4104 C CG  . LEU C 3 141 ? 19.234  -29.608 -77.320 1.00 125.58 ? 141 LEU L CG  1 
ATOM   4105 C CD1 . LEU C 3 141 ? 18.657  -30.335 -76.116 1.00 128.48 ? 141 LEU L CD1 1 
ATOM   4106 C CD2 . LEU C 3 141 ? 18.863  -30.339 -78.599 1.00 138.43 ? 141 LEU L CD2 1 
ATOM   4107 N N   . ASN C 3 142 ? 18.322  -25.340 -79.569 1.00 142.94 ? 142 ASN L N   1 
ATOM   4108 C CA  . ASN C 3 142 ? 17.954  -23.892 -79.617 1.00 147.31 ? 142 ASN L CA  1 
ATOM   4109 C C   . ASN C 3 142 ? 16.545  -23.571 -79.105 1.00 152.34 ? 142 ASN L C   1 
ATOM   4110 O O   . ASN C 3 142 ? 16.419  -22.529 -78.443 1.00 155.71 ? 142 ASN L O   1 
ATOM   4111 C CB  . ASN C 3 142 ? 18.166  -23.303 -81.015 1.00 152.80 ? 142 ASN L CB  1 
ATOM   4112 C CG  . ASN C 3 142 ? 17.669  -21.880 -81.150 1.00 159.60 ? 142 ASN L CG  1 
ATOM   4113 O OD1 . ASN C 3 142 ? 18.121  -20.989 -80.435 1.00 164.67 ? 142 ASN L OD1 1 
ATOM   4114 N ND2 . ASN C 3 142 ? 16.737  -21.658 -82.062 1.00 158.49 ? 142 ASN L ND2 1 
ATOM   4115 N N   . ASN C 3 143 ? 15.528  -24.356 -79.460 1.00 163.58 ? 143 ASN L N   1 
ATOM   4116 C CA  . ASN C 3 143 ? 14.140  -24.002 -79.057 1.00 165.05 ? 143 ASN L CA  1 
ATOM   4117 C C   . ASN C 3 143 ? 13.173  -25.168 -78.838 1.00 183.38 ? 143 ASN L C   1 
ATOM   4118 O O   . ASN C 3 143 ? 13.189  -26.046 -79.713 1.00 193.51 ? 143 ASN L O   1 
ATOM   4119 C CB  . ASN C 3 143 ? 13.321  -23.473 -80.239 1.00 145.94 ? 143 ASN L CB  1 
ATOM   4120 C CG  . ASN C 3 143 ? 13.731  -22.096 -80.718 1.00 149.20 ? 143 ASN L CG  1 
ATOM   4121 O OD1 . ASN C 3 143 ? 14.574  -21.440 -80.113 1.00 139.78 ? 143 ASN L OD1 1 
ATOM   4122 N ND2 . ASN C 3 143 ? 13.116  -21.637 -81.796 1.00 159.63 ? 143 ASN L ND2 1 
ATOM   4123 N N   . PHE C 3 144 ? 12.418  -25.189 -77.727 1.00 172.27 ? 144 PHE L N   1 
ATOM   4124 C CA  . PHE C 3 144 ? 11.344  -26.164 -77.411 1.00 169.17 ? 144 PHE L CA  1 
ATOM   4125 C C   . PHE C 3 144 ? 10.612  -25.735 -76.142 1.00 171.33 ? 144 PHE L C   1 
ATOM   4126 O O   . PHE C 3 144 ? 11.159  -24.878 -75.419 1.00 186.08 ? 144 PHE L O   1 
ATOM   4127 C CB  . PHE C 3 144 ? 12.031  -27.534 -77.305 1.00 169.37 ? 144 PHE L CB  1 
ATOM   4128 C CG  . PHE C 3 144 ? 13.095  -27.696 -76.249 1.00 155.43 ? 144 PHE L CG  1 
ATOM   4129 C CD1 . PHE C 3 144 ? 12.777  -28.087 -74.959 1.00 165.29 ? 144 PHE L CD1 1 
ATOM   4130 C CD2 . PHE C 3 144 ? 14.421  -27.437 -76.549 1.00 153.70 ? 144 PHE L CD2 1 
ATOM   4131 C CE1 . PHE C 3 144 ? 13.763  -28.219 -73.996 1.00 166.47 ? 144 PHE L CE1 1 
ATOM   4132 C CE2 . PHE C 3 144 ? 15.407  -27.571 -75.587 1.00 154.49 ? 144 PHE L CE2 1 
ATOM   4133 C CZ  . PHE C 3 144 ? 15.076  -27.975 -74.316 1.00 155.60 ? 144 PHE L CZ  1 
ATOM   4134 N N   . TYR C 3 145 ? 9.418   -26.282 -75.882 1.00 182.55 ? 145 TYR L N   1 
ATOM   4135 C CA  . TYR C 3 145 ? 8.605   -25.841 -74.712 1.00 198.91 ? 145 TYR L CA  1 
ATOM   4136 C C   . TYR C 3 145 ? 9.181   -26.113 -73.311 1.00 196.93 ? 145 TYR L C   1 
ATOM   4137 O O   . TYR C 3 145 ? 8.999   -25.227 -72.457 1.00 205.31 ? 145 TYR L O   1 
ATOM   4138 C CB  . TYR C 3 145 ? 7.194   -26.422 -74.879 1.00 200.89 ? 145 TYR L CB  1 
ATOM   4139 C CG  . TYR C 3 145 ? 7.053   -27.884 -74.543 1.00 200.15 ? 145 TYR L CG  1 
ATOM   4140 C CD1 . TYR C 3 145 ? 7.475   -28.867 -75.422 1.00 197.70 ? 145 TYR L CD1 1 
ATOM   4141 C CD2 . TYR C 3 145 ? 6.468   -28.286 -73.354 1.00 195.15 ? 145 TYR L CD2 1 
ATOM   4142 C CE1 . TYR C 3 145 ? 7.357   -30.211 -75.111 1.00 191.07 ? 145 TYR L CE1 1 
ATOM   4143 C CE2 . TYR C 3 145 ? 6.335   -29.626 -73.030 1.00 185.25 ? 145 TYR L CE2 1 
ATOM   4144 C CZ  . TYR C 3 145 ? 6.778   -30.592 -73.914 1.00 187.18 ? 145 TYR L CZ  1 
ATOM   4145 O OH  . TYR C 3 145 ? 6.641   -31.922 -73.598 1.00 190.09 ? 145 TYR L OH  1 
ATOM   4146 N N   . PRO C 3 146 ? 9.825   -27.262 -72.988 1.00 171.28 ? 146 PRO L N   1 
ATOM   4147 C CA  . PRO C 3 146 ? 10.302  -27.515 -71.628 1.00 157.48 ? 146 PRO L CA  1 
ATOM   4148 C C   . PRO C 3 146 ? 11.740  -27.009 -71.459 1.00 169.97 ? 146 PRO L C   1 
ATOM   4149 O O   . PRO C 3 146 ? 12.218  -26.325 -72.341 1.00 172.29 ? 146 PRO L O   1 
ATOM   4150 C CB  . PRO C 3 146 ? 10.252  -29.044 -71.531 1.00 130.27 ? 146 PRO L CB  1 
ATOM   4151 C CG  . PRO C 3 146 ? 10.590  -29.510 -72.930 1.00 152.40 ? 146 PRO L CG  1 
ATOM   4152 C CD  . PRO C 3 146 ? 10.156  -28.394 -73.859 1.00 157.57 ? 146 PRO L CD  1 
ATOM   4153 N N   . ARG C 3 147 ? 12.382  -27.348 -70.338 1.00 179.75 ? 147 ARG L N   1 
ATOM   4154 C CA  . ARG C 3 147 ? 13.770  -26.882 -70.075 1.00 167.60 ? 147 ARG L CA  1 
ATOM   4155 C C   . ARG C 3 147 ? 14.735  -28.070 -70.132 1.00 167.39 ? 147 ARG L C   1 
ATOM   4156 O O   . ARG C 3 147 ? 15.942  -27.850 -69.919 1.00 177.89 ? 147 ARG L O   1 
ATOM   4157 C CB  . ARG C 3 147 ? 13.851  -26.201 -68.706 1.00 168.21 ? 147 ARG L CB  1 
ATOM   4158 C CG  . ARG C 3 147 ? 13.339  -27.064 -67.562 1.00 157.90 ? 147 ARG L CG  1 
ATOM   4159 C CD  . ARG C 3 147 ? 13.837  -26.583 -66.213 1.00 147.57 ? 147 ARG L CD  1 
ATOM   4160 N NE  . ARG C 3 147 ? 15.273  -26.776 -66.063 1.00 152.24 ? 147 ARG L NE  1 
ATOM   4161 C CZ  . ARG C 3 147 ? 16.146  -25.798 -65.853 1.00 149.75 ? 147 ARG L CZ  1 
ATOM   4162 N NH1 . ARG C 3 147 ? 17.368  -26.081 -65.441 1.00 151.27 ? 147 ARG L NH1 1 
ATOM   4163 N NH2 . ARG C 3 147 ? 15.792  -24.540 -66.050 1.00 132.04 ? 147 ARG L NH2 1 
ATOM   4164 N N   . GLU C 3 148 ? 14.224  -29.283 -70.360 1.00 154.66 ? 148 GLU L N   1 
ATOM   4165 C CA  . GLU C 3 148 ? 15.102  -30.483 -70.325 1.00 167.76 ? 148 GLU L CA  1 
ATOM   4166 C C   . GLU C 3 148 ? 14.887  -31.330 -71.582 1.00 185.49 ? 148 GLU L C   1 
ATOM   4167 O O   . GLU C 3 148 ? 13.720  -31.491 -71.990 1.00 195.49 ? 148 GLU L O   1 
ATOM   4168 C CB  . GLU C 3 148 ? 14.814  -31.317 -69.075 1.00 166.86 ? 148 GLU L CB  1 
ATOM   4169 C CG  . GLU C 3 148 ? 15.065  -30.579 -67.771 1.00 171.98 ? 148 GLU L CG  1 
ATOM   4170 C CD  . GLU C 3 148 ? 16.494  -30.106 -67.567 1.00 172.39 ? 148 GLU L CD  1 
ATOM   4171 O OE1 . GLU C 3 148 ? 16.690  -28.893 -67.355 1.00 161.20 ? 148 GLU L OE1 1 
ATOM   4172 O OE2 . GLU C 3 148 ? 17.408  -30.952 -67.626 1.00 178.47 ? 148 GLU L OE2 1 
ATOM   4173 N N   . ALA C 3 149 ? 15.972  -31.845 -72.168 1.00 182.77 ? 149 ALA L N   1 
ATOM   4174 C CA  . ALA C 3 149 ? 15.853  -32.736 -73.347 1.00 183.88 ? 149 ALA L CA  1 
ATOM   4175 C C   . ALA C 3 149 ? 16.719  -33.989 -73.182 1.00 168.98 ? 149 ALA L C   1 
ATOM   4176 O O   . ALA C 3 149 ? 17.113  -34.572 -74.212 1.00 167.75 ? 149 ALA L O   1 
ATOM   4177 C CB  . ALA C 3 149 ? 16.213  -31.991 -74.606 1.00 187.39 ? 149 ALA L CB  1 
ATOM   4178 N N   . LYS C 3 150 ? 17.037  -34.362 -71.938 1.00 164.72 ? 150 LYS L N   1 
ATOM   4179 C CA  . LYS C 3 150 ? 17.801  -35.614 -71.679 1.00 143.20 ? 150 LYS L CA  1 
ATOM   4180 C C   . LYS C 3 150 ? 18.911  -35.813 -72.717 1.00 146.75 ? 150 LYS L C   1 
ATOM   4181 O O   . LYS C 3 150 ? 18.943  -36.893 -73.340 1.00 170.99 ? 150 LYS L O   1 
ATOM   4182 C CB  . LYS C 3 150 ? 16.852  -36.816 -71.667 1.00 141.29 ? 150 LYS L CB  1 
ATOM   4183 C CG  . LYS C 3 150 ? 15.860  -36.847 -70.514 1.00 130.86 ? 150 LYS L CG  1 
ATOM   4184 C CD  . LYS C 3 150 ? 14.931  -38.041 -70.563 1.00 126.40 ? 150 LYS L CD  1 
ATOM   4185 C CE  . LYS C 3 150 ? 13.964  -38.077 -69.400 1.00 109.33 ? 150 LYS L CE  1 
ATOM   4186 N NZ  . LYS C 3 150 ? 13.048  -39.240 -69.478 1.00 102.75 ? 150 LYS L NZ  1 
ATOM   4187 N N   . VAL C 3 151 ? 19.781  -34.816 -72.897 1.00 142.47 ? 151 VAL L N   1 
ATOM   4188 C CA  . VAL C 3 151 ? 20.933  -34.974 -73.835 1.00 145.12 ? 151 VAL L CA  1 
ATOM   4189 C C   . VAL C 3 151 ? 21.853  -35.986 -73.145 1.00 152.88 ? 151 VAL L C   1 
ATOM   4190 O O   . VAL C 3 151 ? 22.593  -35.577 -72.229 1.00 167.52 ? 151 VAL L O   1 
ATOM   4191 C CB  . VAL C 3 151 ? 21.725  -33.674 -74.063 1.00 135.84 ? 151 VAL L CB  1 
ATOM   4192 C CG1 . VAL C 3 151 ? 22.859  -33.878 -75.055 1.00 111.60 ? 151 VAL L CG1 1 
ATOM   4193 C CG2 . VAL C 3 151 ? 20.822  -32.537 -74.508 1.00 131.79 ? 151 VAL L CG2 1 
ATOM   4194 N N   . GLN C 3 152 ? 21.795  -37.253 -73.561 1.00 166.79 ? 152 GLN L N   1 
ATOM   4195 C CA  . GLN C 3 152 ? 22.697  -38.271 -72.937 1.00 177.09 ? 152 GLN L CA  1 
ATOM   4196 C C   . GLN C 3 152 ? 23.925  -38.510 -73.803 1.00 156.72 ? 152 GLN L C   1 
ATOM   4197 O O   . GLN C 3 152 ? 23.792  -38.350 -75.026 1.00 167.20 ? 152 GLN L O   1 
ATOM   4198 C CB  . GLN C 3 152 ? 21.933  -39.564 -72.661 1.00 207.16 ? 152 GLN L CB  1 
ATOM   4199 C CG  . GLN C 3 152 ? 20.849  -39.426 -71.603 1.00 230.67 ? 152 GLN L CG  1 
ATOM   4200 C CD  . GLN C 3 152 ? 21.419  -39.108 -70.243 1.00 226.24 ? 152 GLN L CD  1 
ATOM   4201 O OE1 . GLN C 3 152 ? 21.420  -37.960 -69.801 0.72 211.65 ? 152 GLN L OE1 1 
ATOM   4202 N NE2 . GLN C 3 152 ? 21.916  -40.129 -69.564 1.00 214.47 ? 152 GLN L NE2 1 
ATOM   4203 N N   . TRP C 3 153 ? 25.078  -38.810 -73.206 1.00 161.09 ? 153 TRP L N   1 
ATOM   4204 C CA  . TRP C 3 153 ? 26.314  -38.949 -74.016 1.00 151.86 ? 153 TRP L CA  1 
ATOM   4205 C C   . TRP C 3 153 ? 26.883  -40.346 -74.255 1.00 162.44 ? 153 TRP L C   1 
ATOM   4206 O O   . TRP C 3 153 ? 27.135  -41.045 -73.262 1.00 162.55 ? 153 TRP L O   1 
ATOM   4207 C CB  . TRP C 3 153 ? 27.293  -38.125 -73.174 1.00 157.13 ? 153 TRP L CB  1 
ATOM   4208 C CG  . TRP C 3 153 ? 27.040  -36.649 -73.181 1.00 165.59 ? 153 TRP L CG  1 
ATOM   4209 C CD1 . TRP C 3 153 ? 26.326  -35.929 -72.268 1.00 160.63 ? 153 TRP L CD1 1 
ATOM   4210 C CD2 . TRP C 3 153 ? 27.498  -35.703 -74.164 1.00 169.30 ? 153 TRP L CD2 1 
ATOM   4211 N NE1 . TRP C 3 153 ? 26.316  -34.604 -72.608 1.00 163.97 ? 153 TRP L NE1 1 
ATOM   4212 C CE2 . TRP C 3 153 ? 27.026  -34.435 -73.768 1.00 160.98 ? 153 TRP L CE2 1 
ATOM   4213 C CE3 . TRP C 3 153 ? 28.257  -35.801 -75.336 1.00 171.50 ? 153 TRP L CE3 1 
ATOM   4214 C CZ2 . TRP C 3 153 ? 27.291  -33.280 -74.501 1.00 160.32 ? 153 TRP L CZ2 1 
ATOM   4215 C CZ3 . TRP C 3 153 ? 28.523  -34.659 -76.057 1.00 159.82 ? 153 TRP L CZ3 1 
ATOM   4216 C CH2 . TRP C 3 153 ? 28.043  -33.416 -75.645 1.00 148.06 ? 153 TRP L CH2 1 
ATOM   4217 N N   . LYS C 3 154 ? 27.047  -40.739 -75.519 1.00 169.82 ? 154 LYS L N   1 
ATOM   4218 C CA  . LYS C 3 154 ? 27.631  -42.068 -75.838 1.00 166.61 ? 154 LYS L CA  1 
ATOM   4219 C C   . LYS C 3 154 ? 29.051  -41.999 -76.399 1.00 162.94 ? 154 LYS L C   1 
ATOM   4220 O O   . LYS C 3 154 ? 29.201  -41.573 -77.556 1.00 177.40 ? 154 LYS L O   1 
ATOM   4221 C CB  . LYS C 3 154 ? 26.790  -42.869 -76.834 1.00 152.71 ? 154 LYS L CB  1 
ATOM   4222 C CG  . LYS C 3 154 ? 25.373  -43.200 -76.389 1.00 167.62 ? 154 LYS L CG  1 
ATOM   4223 C CD  . LYS C 3 154 ? 24.632  -44.053 -77.394 1.00 154.91 ? 154 LYS L CD  1 
ATOM   4224 C CE  . LYS C 3 154 ? 25.147  -45.475 -77.462 1.00 184.23 ? 154 LYS L CE  1 
ATOM   4225 N NZ  . LYS C 3 154 ? 24.851  -46.223 -76.218 1.00 175.00 ? 154 LYS L NZ  1 
ATOM   4226 N N   . VAL C 3 155 ? 30.048  -42.383 -75.603 1.00 163.05 ? 155 VAL L N   1 
ATOM   4227 C CA  . VAL C 3 155 ? 31.446  -42.413 -76.122 1.00 155.78 ? 155 VAL L CA  1 
ATOM   4228 C C   . VAL C 3 155 ? 31.695  -43.808 -76.691 1.00 167.57 ? 155 VAL L C   1 
ATOM   4229 O O   . VAL C 3 155 ? 31.623  -44.775 -75.917 1.00 179.00 ? 155 VAL L O   1 
ATOM   4230 C CB  . VAL C 3 155 ? 32.514  -42.024 -75.087 1.00 143.62 ? 155 VAL L CB  1 
ATOM   4231 C CG1 . VAL C 3 155 ? 33.919  -42.141 -75.653 1.00 135.72 ? 155 VAL L CG1 1 
ATOM   4232 C CG2 . VAL C 3 155 ? 32.275  -40.625 -74.540 1.00 166.68 ? 155 VAL L CG2 1 
ATOM   4233 N N   . ASP C 3 156 ? 31.946  -43.906 -77.996 1.00 156.79 ? 156 ASP L N   1 
ATOM   4234 C CA  . ASP C 3 156 ? 32.093  -45.246 -78.617 1.00 153.54 ? 156 ASP L CA  1 
ATOM   4235 C C   . ASP C 3 156 ? 30.927  -46.118 -78.142 1.00 183.13 ? 156 ASP L C   1 
ATOM   4236 O O   . ASP C 3 156 ? 31.186  -47.252 -77.699 1.00 199.80 ? 156 ASP L O   1 
ATOM   4237 C CB  . ASP C 3 156 ? 33.469  -45.852 -78.334 1.00 158.22 ? 156 ASP L CB  1 
ATOM   4238 C CG  . ASP C 3 156 ? 34.579  -45.189 -79.131 1.00 169.47 ? 156 ASP L CG  1 
ATOM   4239 O OD1 . ASP C 3 156 ? 34.301  -44.159 -79.775 1.00 180.91 ? 156 ASP L OD1 1 
ATOM   4240 O OD2 . ASP C 3 156 ? 35.702  -45.727 -79.131 1.00 160.24 ? 156 ASP L OD2 1 
ATOM   4241 N N   . ASN C 3 157 ? 29.700  -45.593 -78.215 1.00 185.69 ? 157 ASN L N   1 
ATOM   4242 C CA  . ASN C 3 157 ? 28.485  -46.365 -77.830 1.00 182.14 ? 157 ASN L CA  1 
ATOM   4243 C C   . ASN C 3 157 ? 28.531  -46.734 -76.343 1.00 189.03 ? 157 ASN L C   1 
ATOM   4244 O O   . ASN C 3 157 ? 28.021  -47.816 -75.997 1.00 185.22 ? 157 ASN L O   1 
ATOM   4245 C CB  . ASN C 3 157 ? 28.285  -47.589 -78.726 1.00 176.73 ? 157 ASN L CB  1 
ATOM   4246 C CG  . ASN C 3 157 ? 28.094  -47.220 -80.182 1.00 190.28 ? 157 ASN L CG  1 
ATOM   4247 O OD1 . ASN C 3 157 ? 28.105  -46.043 -80.534 1.00 192.51 ? 157 ASN L OD1 1 
ATOM   4248 N ND2 . ASN C 3 157 ? 27.918  -48.218 -81.033 1.00 169.02 ? 157 ASN L ND2 1 
ATOM   4249 N N   . ALA C 3 158 ? 29.108  -45.874 -75.501 1.00 181.87 ? 158 ALA L N   1 
ATOM   4250 C CA  . ALA C 3 158 ? 29.093  -46.122 -74.039 1.00 184.42 ? 158 ALA L CA  1 
ATOM   4251 C C   . ALA C 3 158 ? 28.534  -44.880 -73.341 1.00 180.97 ? 158 ALA L C   1 
ATOM   4252 O O   . ALA C 3 158 ? 29.207  -43.832 -73.380 1.00 191.30 ? 158 ALA L O   1 
ATOM   4253 C CB  . ALA C 3 158 ? 30.476  -46.461 -73.546 1.00 190.36 ? 158 ALA L CB  1 
ATOM   4254 N N   . LEU C 3 159 ? 27.353  -44.994 -72.729 1.00 177.13 ? 159 LEU L N   1 
ATOM   4255 C CA  . LEU C 3 159 ? 26.707  -43.810 -72.104 1.00 160.69 ? 159 LEU L CA  1 
ATOM   4256 C C   . LEU C 3 159 ? 27.678  -43.171 -71.110 1.00 157.36 ? 159 LEU L C   1 
ATOM   4257 O O   . LEU C 3 159 ? 28.251  -43.907 -70.287 1.00 166.39 ? 159 LEU L O   1 
ATOM   4258 C CB  . LEU C 3 159 ? 25.412  -44.245 -71.414 1.00 157.03 ? 159 LEU L CB  1 
ATOM   4259 C CG  . LEU C 3 159 ? 24.323  -44.769 -72.348 1.00 153.92 ? 159 LEU L CG  1 
ATOM   4260 C CD1 . LEU C 3 159 ? 23.143  -45.308 -71.555 1.00 153.78 ? 159 LEU L CD1 1 
ATOM   4261 C CD2 . LEU C 3 159 ? 23.863  -43.677 -73.300 1.00 146.17 ? 159 LEU L CD2 1 
ATOM   4262 N N   . GLN C 3 160 ? 27.845  -41.851 -71.194 1.00 156.35 ? 160 GLN L N   1 
ATOM   4263 C CA  . GLN C 3 160 ? 28.750  -41.128 -70.265 1.00 154.09 ? 160 GLN L CA  1 
ATOM   4264 C C   . GLN C 3 160 ? 27.916  -40.251 -69.330 1.00 148.93 ? 160 GLN L C   1 
ATOM   4265 O O   . GLN C 3 160 ? 27.175  -39.389 -69.837 1.00 150.57 ? 160 GLN L O   1 
ATOM   4266 C CB  . GLN C 3 160 ? 29.754  -40.288 -71.052 1.00 149.65 ? 160 GLN L CB  1 
ATOM   4267 C CG  . GLN C 3 160 ? 30.562  -41.093 -72.055 1.00 155.57 ? 160 GLN L CG  1 
ATOM   4268 C CD  . GLN C 3 160 ? 31.426  -42.128 -71.378 1.00 172.91 ? 160 GLN L CD  1 
ATOM   4269 O OE1 . GLN C 3 160 ? 32.279  -41.808 -70.554 1.00 165.72 ? 160 GLN L OE1 1 
ATOM   4270 N NE2 . GLN C 3 160 ? 31.206  -43.386 -71.723 1.00 174.76 ? 160 GLN L NE2 1 
ATOM   4271 N N   . SER C 3 161 ? 28.029  -40.493 -68.023 1.00 132.30 ? 161 SER L N   1 
ATOM   4272 C CA  . SER C 3 161 ? 27.252  -39.719 -67.024 1.00 136.17 ? 161 SER L CA  1 
ATOM   4273 C C   . SER C 3 161 ? 28.220  -39.011 -66.076 1.00 151.60 ? 161 SER L C   1 
ATOM   4274 O O   . SER C 3 161 ? 29.315  -39.554 -65.843 1.00 159.69 ? 161 SER L O   1 
ATOM   4275 C CB  . SER C 3 161 ? 26.331  -40.625 -66.268 1.00 137.32 ? 161 SER L CB  1 
ATOM   4276 O OG  . SER C 3 161 ? 27.034  -41.757 -65.781 1.00 146.94 ? 161 SER L OG  1 
ATOM   4277 N N   . GLY C 3 162 ? 27.831  -37.844 -65.559 1.00 151.73 ? 162 GLY L N   1 
ATOM   4278 C CA  . GLY C 3 162 ? 28.718  -37.071 -64.669 1.00 152.40 ? 162 GLY L CA  1 
ATOM   4279 C C   . GLY C 3 162 ? 29.627  -36.151 -65.462 1.00 143.11 ? 162 GLY L C   1 
ATOM   4280 O O   . GLY C 3 162 ? 29.621  -34.936 -65.192 1.00 140.98 ? 162 GLY L O   1 
ATOM   4281 N N   . ASN C 3 163 ? 30.380  -36.707 -66.408 1.00 30.00  ? 163 ASN L N   1 
ATOM   4282 C CA  . ASN C 3 163 ? 31.242  -35.865 -67.273 1.00 30.00  ? 163 ASN L CA  1 
ATOM   4283 C C   . ASN C 3 163 ? 30.369  -34.841 -68.003 1.00 30.00  ? 163 ASN L C   1 
ATOM   4284 O O   . ASN C 3 163 ? 30.931  -33.848 -68.491 1.00 30.00  ? 163 ASN L O   1 
ATOM   4285 C CB  . ASN C 3 163 ? 32.056  -36.711 -68.250 1.00 30.00  ? 163 ASN L CB  1 
ATOM   4286 C CG  . ASN C 3 163 ? 31.349  -37.991 -68.635 1.00 30.00  ? 163 ASN L CG  1 
ATOM   4287 O OD1 . ASN C 3 163 ? 30.122  -38.050 -68.633 1.00 30.00  ? 163 ASN L OD1 1 
ATOM   4288 N ND2 . ASN C 3 163 ? 32.115  -39.018 -68.966 1.00 30.00  ? 163 ASN L ND2 1 
ATOM   4289 N N   . SER C 3 164 ? 29.051  -35.058 -68.064 1.00 30.00  ? 164 SER L N   1 
ATOM   4290 C CA  . SER C 3 164 ? 28.202  -34.016 -68.697 1.00 30.00  ? 164 SER L CA  1 
ATOM   4291 C C   . SER C 3 164 ? 27.723  -32.863 -67.813 1.00 30.00  ? 164 SER L C   1 
ATOM   4292 O O   . SER C 3 164 ? 27.541  -33.092 -66.606 1.00 30.00  ? 164 SER L O   1 
ATOM   4293 C CB  . SER C 3 164 ? 27.028  -34.762 -69.254 1.00 30.00  ? 164 SER L CB  1 
ATOM   4294 O OG  . SER C 3 164 ? 27.237  -36.166 -69.176 1.00 30.00  ? 164 SER L OG  1 
ATOM   4295 N N   . GLN C 3 165 ? 27.516  -31.678 -68.398 1.00 153.56 ? 165 GLN L N   1 
ATOM   4296 C CA  . GLN C 3 165 ? 27.004  -30.536 -67.649 1.00 144.08 ? 165 GLN L CA  1 
ATOM   4297 C C   . GLN C 3 165 ? 26.051  -29.773 -68.555 1.00 146.64 ? 165 GLN L C   1 
ATOM   4298 O O   . GLN C 3 165 ? 26.375  -29.517 -69.718 1.00 171.46 ? 165 GLN L O   1 
ATOM   4299 C CB  . GLN C 3 165 ? 28.169  -29.632 -67.231 1.00 170.81 ? 165 GLN L CB  1 
ATOM   4300 C CG  . GLN C 3 165 ? 29.153  -30.273 -66.266 1.00 185.22 ? 165 GLN L CG  1 
ATOM   4301 C CD  . GLN C 3 165 ? 30.280  -30.997 -66.980 1.00 178.36 ? 165 GLN L CD  1 
ATOM   4302 O OE1 . GLN C 3 165 ? 30.494  -30.807 -68.178 1.00 187.17 ? 165 GLN L OE1 1 
ATOM   4303 N NE2 . GLN C 3 165 ? 31.008  -31.830 -66.246 1.00 151.16 ? 165 GLN L NE2 1 
ATOM   4304 N N   . GLU C 3 166 ? 24.887  -29.404 -68.028 1.00 136.92 ? 166 GLU L N   1 
ATOM   4305 C CA  . GLU C 3 166 ? 23.839  -28.775 -68.820 1.00 136.77 ? 166 GLU L CA  1 
ATOM   4306 C C   . GLU C 3 166 ? 23.491  -27.409 -68.242 1.00 130.95 ? 166 GLU L C   1 
ATOM   4307 O O   . GLU C 3 166 ? 23.302  -27.273 -67.028 1.00 127.14 ? 166 GLU L O   1 
ATOM   4308 C CB  . GLU C 3 166 ? 22.594  -29.666 -68.882 1.00 133.21 ? 166 GLU L CB  1 
ATOM   4309 C CG  . GLU C 3 166 ? 22.903  -31.158 -68.847 1.00 131.50 ? 166 GLU L CG  1 
ATOM   4310 C CD  . GLU C 3 166 ? 21.704  -32.011 -69.209 1.00 150.99 ? 166 GLU L CD  1 
ATOM   4311 O OE1 . GLU C 3 166 ? 20.574  -31.633 -68.838 1.00 159.26 ? 166 GLU L OE1 1 
ATOM   4312 O OE2 . GLU C 3 166 ? 21.892  -33.060 -69.861 1.00 165.91 ? 166 GLU L OE2 1 
ATOM   4313 N N   . SER C 3 167 ? 23.414  -26.402 -69.114 1.00 135.11 ? 167 SER L N   1 
ATOM   4314 C CA  . SER C 3 167 ? 23.010  -25.054 -68.742 1.00 127.10 ? 167 SER L CA  1 
ATOM   4315 C C   . SER C 3 167 ? 21.827  -24.637 -69.604 1.00 131.43 ? 167 SER L C   1 
ATOM   4316 O O   . SER C 3 167 ? 21.708  -25.050 -70.761 1.00 153.93 ? 167 SER L O   1 
ATOM   4317 C CB  . SER C 3 167 ? 24.168  -24.049 -68.892 1.00 127.80 ? 167 SER L CB  1 
ATOM   4318 O OG  . SER C 3 167 ? 24.675  -24.027 -70.213 1.00 138.18 ? 167 SER L OG  1 
ATOM   4319 N N   . VAL C 3 168 ? 20.946  -23.819 -69.032 1.00 129.36 ? 168 VAL L N   1 
ATOM   4320 C CA  . VAL C 3 168 ? 19.627  -23.582 -69.603 1.00 132.25 ? 168 VAL L CA  1 
ATOM   4321 C C   . VAL C 3 168 ? 19.384  -22.082 -69.673 1.00 141.90 ? 168 VAL L C   1 
ATOM   4322 O O   . VAL C 3 168 ? 19.695  -21.357 -68.722 1.00 141.16 ? 168 VAL L O   1 
ATOM   4323 C CB  . VAL C 3 168 ? 18.531  -24.268 -68.755 1.00 147.56 ? 168 VAL L CB  1 
ATOM   4324 C CG1 . VAL C 3 168 ? 17.157  -24.069 -69.380 1.00 147.92 ? 168 VAL L CG1 1 
ATOM   4325 C CG2 . VAL C 3 168 ? 18.861  -25.740 -68.472 1.00 143.69 ? 168 VAL L CG2 1 
ATOM   4326 N N   . THR C 3 169 ? 18.811  -21.616 -70.784 1.00 150.02 ? 169 THR L N   1 
ATOM   4327 C CA  . THR C 3 169 ? 18.389  -20.227 -70.896 1.00 142.70 ? 169 THR L CA  1 
ATOM   4328 C C   . THR C 3 169 ? 16.925  -20.089 -70.475 1.00 144.48 ? 169 THR L C   1 
ATOM   4329 O O   . THR C 3 169 ? 16.277  -21.050 -70.056 1.00 144.88 ? 169 THR L O   1 
ATOM   4330 C CB  . THR C 3 169 ? 18.592  -19.696 -72.317 1.00 142.99 ? 169 THR L CB  1 
ATOM   4331 O OG1 . THR C 3 169 ? 17.868  -20.507 -73.252 1.00 167.57 ? 169 THR L OG1 1 
ATOM   4332 C CG2 . THR C 3 169 ? 20.067  -19.682 -72.683 1.00 157.33 ? 169 THR L CG2 1 
ATOM   4333 N N   . GLU C 3 170 ? 16.398  -18.874 -70.588 1.00 142.97 ? 170 GLU L N   1 
ATOM   4334 C CA  . GLU C 3 170 ? 15.013  -18.586 -70.249 1.00 144.08 ? 170 GLU L CA  1 
ATOM   4335 C C   . GLU C 3 170 ? 14.164  -18.505 -71.513 1.00 144.12 ? 170 GLU L C   1 
ATOM   4336 O O   . GLU C 3 170 ? 14.668  -18.521 -72.639 1.00 148.77 ? 170 GLU L O   1 
ATOM   4337 C CB  . GLU C 3 170 ? 14.915  -17.282 -69.445 1.00 168.77 ? 170 GLU L CB  1 
ATOM   4338 C CG  . GLU C 3 170 ? 14.703  -16.022 -70.280 1.00 200.63 ? 170 GLU L CG  1 
ATOM   4339 C CD  . GLU C 3 170 ? 15.995  -15.432 -70.820 1.00 250.93 ? 170 GLU L CD  1 
ATOM   4340 O OE1 . GLU C 3 170 ? 16.954  -16.195 -71.061 1.00 259.27 ? 170 GLU L OE1 1 
ATOM   4341 O OE2 . GLU C 3 170 ? 16.051  -14.197 -71.001 1.00 268.96 ? 170 GLU L OE2 1 
ATOM   4342 N N   . GLN C 3 171 ? 12.849  -18.428 -71.310 1.00 138.22 ? 171 GLN L N   1 
ATOM   4343 C CA  . GLN C 3 171 ? 11.907  -18.300 -72.414 1.00 148.79 ? 171 GLN L CA  1 
ATOM   4344 C C   . GLN C 3 171 ? 12.160  -17.025 -73.202 1.00 162.90 ? 171 GLN L C   1 
ATOM   4345 O O   . GLN C 3 171 ? 11.999  -15.921 -72.669 1.00 162.36 ? 171 GLN L O   1 
ATOM   4346 C CB  . GLN C 3 171 ? 10.472  -18.316 -71.891 1.00 129.76 ? 171 GLN L CB  1 
ATOM   4347 C CG  . GLN C 3 171 ? 9.829   -19.675 -71.942 1.00 148.64 ? 171 GLN L CG  1 
ATOM   4348 C CD  . GLN C 3 171 ? 8.528   -19.719 -71.182 1.00 165.68 ? 171 GLN L CD  1 
ATOM   4349 O OE1 . GLN C 3 171 ? 8.157   -18.759 -70.507 1.00 173.28 ? 171 GLN L OE1 1 
ATOM   4350 N NE2 . GLN C 3 171 ? 7.831   -20.840 -71.275 1.00 163.78 ? 171 GLN L NE2 1 
ATOM   4351 N N   . ASP C 3 172 ? 12.558  -17.190 -74.466 1.00 164.99 ? 172 ASP L N   1 
ATOM   4352 C CA  . ASP C 3 172 ? 12.792  -16.014 -75.342 1.00 160.66 ? 172 ASP L CA  1 
ATOM   4353 C C   . ASP C 3 172 ? 11.538  -15.144 -75.324 1.00 151.08 ? 172 ASP L C   1 
ATOM   4354 O O   . ASP C 3 172 ? 10.440  -15.676 -75.551 1.00 141.28 ? 172 ASP L O   1 
ATOM   4355 C CB  . ASP C 3 172 ? 13.154  -16.436 -76.765 1.00 170.69 ? 172 ASP L CB  1 
ATOM   4356 C CG  . ASP C 3 172 ? 14.424  -17.264 -76.842 1.00 186.99 ? 172 ASP L CG  1 
ATOM   4357 O OD1 . ASP C 3 172 ? 15.038  -17.493 -75.781 1.00 180.28 ? 172 ASP L OD1 1 
ATOM   4358 O OD2 . ASP C 3 172 ? 14.784  -17.679 -77.961 1.00 179.86 ? 172 ASP L OD2 1 
ATOM   4359 N N   . SER C 3 173 ? 11.707  -13.853 -75.060 1.00 150.30 ? 173 SER L N   1 
ATOM   4360 C CA  . SER C 3 173 ? 10.527  -12.964 -74.955 1.00 160.36 ? 173 SER L CA  1 
ATOM   4361 C C   . SER C 3 173 ? 9.704   -13.071 -76.240 1.00 177.67 ? 173 SER L C   1 
ATOM   4362 O O   . SER C 3 173 ? 8.471   -13.196 -76.140 1.00 188.16 ? 173 SER L O   1 
ATOM   4363 C CB  . SER C 3 173 ? 10.963  -11.552 -74.700 1.00 155.55 ? 173 SER L CB  1 
ATOM   4364 O OG  . SER C 3 173 ? 11.921  -11.144 -75.664 1.00 163.51 ? 173 SER L OG  1 
ATOM   4365 N N   . LYS C 3 174 ? 10.367  -13.046 -77.397 1.00 181.71 ? 174 LYS L N   1 
ATOM   4366 C CA  . LYS C 3 174 ? 9.637   -13.066 -78.691 1.00 172.46 ? 174 LYS L CA  1 
ATOM   4367 C C   . LYS C 3 174 ? 8.760   -14.316 -78.744 1.00 175.43 ? 174 LYS L C   1 
ATOM   4368 O O   . LYS C 3 174 ? 7.553   -14.179 -79.012 1.00 186.08 ? 174 LYS L O   1 
ATOM   4369 C CB  . LYS C 3 174 ? 10.622  -13.067 -79.863 1.00 177.68 ? 174 LYS L CB  1 
ATOM   4370 C CG  . LYS C 3 174 ? 11.633  -11.927 -79.876 1.00 179.44 ? 174 LYS L CG  1 
ATOM   4371 C CD  . LYS C 3 174 ? 12.879  -12.208 -79.060 1.00 186.38 ? 174 LYS L CD  1 
ATOM   4372 C CE  . LYS C 3 174 ? 13.827  -11.030 -79.000 1.00 223.04 ? 174 LYS L CE  1 
ATOM   4373 N NZ  . LYS C 3 174 ? 15.025  -11.330 -78.181 1.00 258.00 ? 174 LYS L NZ  1 
ATOM   4374 N N   . ASP C 3 175 ? 9.351   -15.489 -78.502 1.00 170.07 ? 175 ASP L N   1 
ATOM   4375 C CA  . ASP C 3 175 ? 8.586   -16.764 -78.530 1.00 171.67 ? 175 ASP L CA  1 
ATOM   4376 C C   . ASP C 3 175 ? 9.082   -17.662 -77.393 1.00 175.94 ? 175 ASP L C   1 
ATOM   4377 O O   . ASP C 3 175 ? 10.298  -17.924 -77.345 1.00 183.54 ? 175 ASP L O   1 
ATOM   4378 C CB  . ASP C 3 175 ? 8.712   -17.459 -79.888 1.00 166.86 ? 175 ASP L CB  1 
ATOM   4379 C CG  . ASP C 3 175 ? 7.821   -18.681 -80.039 1.00 191.59 ? 175 ASP L CG  1 
ATOM   4380 O OD1 . ASP C 3 175 ? 7.059   -18.976 -79.097 1.00 190.16 ? 175 ASP L OD1 1 
ATOM   4381 O OD2 . ASP C 3 175 ? 7.900   -19.331 -81.100 1.00 198.08 ? 175 ASP L OD2 1 
ATOM   4382 N N   . SER C 3 176 ? 8.172   -18.115 -76.526 1.00 150.92 ? 176 SER L N   1 
ATOM   4383 C CA  . SER C 3 176 ? 8.558   -18.990 -75.388 1.00 156.25 ? 176 SER L CA  1 
ATOM   4384 C C   . SER C 3 176 ? 9.398   -20.057 -76.096 1.00 158.91 ? 176 SER L C   1 
ATOM   4385 O O   . SER C 3 176 ? 8.820   -20.831 -76.884 1.00 172.21 ? 176 SER L O   1 
ATOM   4386 C CB  . SER C 3 176 ? 7.341   -19.475 -74.648 1.00 164.85 ? 176 SER L CB  1 
ATOM   4387 O OG  . SER C 3 176 ? 6.446   -20.139 -75.529 1.00 186.21 ? 176 SER L OG  1 
ATOM   4388 N N   . THR C 3 177 ? 10.705  -20.096 -75.819 1.00 154.64 ? 177 THR L N   1 
ATOM   4389 C CA  . THR C 3 177 ? 11.611  -21.061 -76.500 1.00 167.58 ? 177 THR L CA  1 
ATOM   4390 C C   . THR C 3 177 ? 12.902  -21.119 -75.679 1.00 170.26 ? 177 THR L C   1 
ATOM   4391 O O   . THR C 3 177 ? 13.793  -20.286 -75.926 1.00 170.18 ? 177 THR L O   1 
ATOM   4392 C CB  . THR C 3 177 ? 11.921  -20.823 -77.984 1.00 167.44 ? 177 THR L CB  1 
ATOM   4393 O OG1 . THR C 3 177 ? 12.400  -19.486 -78.127 1.00 162.68 ? 177 THR L OG1 1 
ATOM   4394 C CG2 . THR C 3 177 ? 10.725  -21.033 -78.886 1.00 169.93 ? 177 THR L CG2 1 
ATOM   4395 N N   . TYR C 3 178 ? 12.993  -22.069 -74.745 1.00 158.40 ? 178 TYR L N   1 
ATOM   4396 C CA  . TYR C 3 178 ? 14.220  -22.236 -73.924 1.00 155.68 ? 178 TYR L CA  1 
ATOM   4397 C C   . TYR C 3 178 ? 15.351  -22.745 -74.821 1.00 163.81 ? 178 TYR L C   1 
ATOM   4398 O O   . TYR C 3 178 ? 15.050  -23.352 -75.866 1.00 178.91 ? 178 TYR L O   1 
ATOM   4399 C CB  . TYR C 3 178 ? 13.970  -23.235 -72.793 1.00 161.56 ? 178 TYR L CB  1 
ATOM   4400 C CG  . TYR C 3 178 ? 12.969  -22.802 -71.752 1.00 160.11 ? 178 TYR L CG  1 
ATOM   4401 C CD1 . TYR C 3 178 ? 13.238  -21.751 -70.892 1.00 156.55 ? 178 TYR L CD1 1 
ATOM   4402 C CD2 . TYR C 3 178 ? 11.746  -23.440 -71.628 1.00 163.49 ? 178 TYR L CD2 1 
ATOM   4403 C CE1 . TYR C 3 178 ? 12.325  -21.353 -69.929 1.00 154.85 ? 178 TYR L CE1 1 
ATOM   4404 C CE2 . TYR C 3 178 ? 10.821  -23.054 -70.674 1.00 155.30 ? 178 TYR L CE2 1 
ATOM   4405 C CZ  . TYR C 3 178 ? 11.110  -22.006 -69.821 1.00 158.27 ? 178 TYR L CZ  1 
ATOM   4406 O OH  . TYR C 3 178 ? 10.195  -21.615 -68.874 1.00 169.31 ? 178 TYR L OH  1 
ATOM   4407 N N   . SER C 3 179 ? 16.607  -22.498 -74.439 1.00 155.94 ? 179 SER L N   1 
ATOM   4408 C CA  . SER C 3 179 ? 17.746  -23.063 -75.212 1.00 147.83 ? 179 SER L CA  1 
ATOM   4409 C C   . SER C 3 179 ? 18.676  -23.813 -74.254 1.00 154.21 ? 179 SER L C   1 
ATOM   4410 O O   . SER C 3 179 ? 18.715  -23.439 -73.065 1.00 159.88 ? 179 SER L O   1 
ATOM   4411 C CB  . SER C 3 179 ? 18.474  -22.009 -76.013 1.00 142.42 ? 179 SER L CB  1 
ATOM   4412 O OG  . SER C 3 179 ? 19.345  -21.252 -75.192 1.00 168.74 ? 179 SER L OG  1 
ATOM   4413 N N   . LEU C 3 180 ? 19.362  -24.854 -74.745 1.00 161.85 ? 180 LEU L N   1 
ATOM   4414 C CA  . LEU C 3 180 ? 20.232  -25.695 -73.875 1.00 146.20 ? 180 LEU L CA  1 
ATOM   4415 C C   . LEU C 3 180 ? 21.655  -25.747 -74.438 1.00 132.97 ? 180 LEU L C   1 
ATOM   4416 O O   . LEU C 3 180 ? 21.817  -25.491 -75.646 1.00 135.96 ? 180 LEU L O   1 
ATOM   4417 C CB  . LEU C 3 180 ? 19.657  -27.114 -73.819 1.00 153.05 ? 180 LEU L CB  1 
ATOM   4418 C CG  . LEU C 3 180 ? 18.325  -27.276 -73.092 1.00 185.38 ? 180 LEU L CG  1 
ATOM   4419 C CD1 . LEU C 3 180 ? 18.064  -28.739 -72.768 1.00 212.25 ? 180 LEU L CD1 1 
ATOM   4420 C CD2 . LEU C 3 180 ? 18.300  -26.443 -71.823 1.00 168.29 ? 180 LEU L CD2 1 
ATOM   4421 N N   . SER C 3 181 ? 22.637  -26.090 -73.596 1.00 134.80 ? 181 SER L N   1 
ATOM   4422 C CA  . SER C 3 181 ? 24.040  -26.242 -74.069 1.00 141.93 ? 181 SER L CA  1 
ATOM   4423 C C   . SER C 3 181 ? 24.769  -27.271 -73.198 1.00 145.03 ? 181 SER L C   1 
ATOM   4424 O O   . SER C 3 181 ? 25.706  -26.877 -72.479 1.00 144.78 ? 181 SER L O   1 
ATOM   4425 C CB  . SER C 3 181 ? 24.766  -24.926 -74.062 1.00 146.72 ? 181 SER L CB  1 
ATOM   4426 O OG  . SER C 3 181 ? 24.947  -24.459 -72.734 1.00 152.92 ? 181 SER L OG  1 
ATOM   4427 N N   . SER C 3 182 ? 24.352  -28.539 -73.264 1.00 140.35 ? 182 SER L N   1 
ATOM   4428 C CA  . SER C 3 182 ? 25.038  -29.606 -72.488 1.00 144.34 ? 182 SER L CA  1 
ATOM   4429 C C   . SER C 3 182 ? 26.498  -29.707 -72.944 1.00 146.61 ? 182 SER L C   1 
ATOM   4430 O O   . SER C 3 182 ? 26.728  -29.784 -74.167 1.00 159.60 ? 182 SER L O   1 
ATOM   4431 C CB  . SER C 3 182 ? 24.325  -30.924 -72.624 1.00 152.06 ? 182 SER L CB  1 
ATOM   4432 O OG  . SER C 3 182 ? 24.942  -31.913 -71.812 1.00 152.48 ? 182 SER L OG  1 
ATOM   4433 N N   . THR C 3 183 ? 27.442  -29.693 -71.996 1.00 133.73 ? 183 THR L N   1 
ATOM   4434 C CA  . THR C 3 183 ? 28.879  -29.772 -72.354 1.00 128.17 ? 183 THR L CA  1 
ATOM   4435 C C   . THR C 3 183 ? 29.397  -31.030 -71.663 1.00 145.26 ? 183 THR L C   1 
ATOM   4436 O O   . THR C 3 183 ? 28.923  -31.323 -70.552 1.00 168.57 ? 183 THR L O   1 
ATOM   4437 C CB  . THR C 3 183 ? 29.650  -28.566 -71.815 1.00 130.83 ? 183 THR L CB  1 
ATOM   4438 O OG1 . THR C 3 183 ? 29.661  -28.659 -70.390 1.00 143.25 ? 183 THR L OG1 1 
ATOM   4439 C CG2 . THR C 3 183 ? 29.047  -27.245 -72.237 1.00 132.11 ? 183 THR L CG2 1 
ATOM   4440 N N   . LEU C 3 184 ? 30.320  -31.745 -72.304 1.00 150.10 ? 184 LEU L N   1 
ATOM   4441 C CA  . LEU C 3 184 ? 30.975  -32.901 -71.637 1.00 151.22 ? 184 LEU L CA  1 
ATOM   4442 C C   . LEU C 3 184 ? 32.476  -32.641 -71.790 1.00 156.19 ? 184 LEU L C   1 
ATOM   4443 O O   . LEU C 3 184 ? 32.951  -32.604 -72.937 1.00 153.88 ? 184 LEU L O   1 
ATOM   4444 C CB  . LEU C 3 184 ? 30.533  -34.210 -72.295 1.00 143.42 ? 184 LEU L CB  1 
ATOM   4445 C CG  . LEU C 3 184 ? 30.992  -35.492 -71.599 1.00 156.22 ? 184 LEU L CG  1 
ATOM   4446 C CD1 . LEU C 3 184 ? 29.956  -36.593 -71.756 1.00 153.85 ? 184 LEU L CD1 1 
ATOM   4447 C CD2 . LEU C 3 184 ? 32.331  -35.964 -72.140 1.00 145.35 ? 184 LEU L CD2 1 
ATOM   4448 N N   . THR C 3 185 ? 33.169  -32.425 -70.672 1.00 168.42 ? 185 THR L N   1 
ATOM   4449 C CA  . THR C 3 185 ? 34.610  -32.067 -70.720 1.00 168.74 ? 185 THR L CA  1 
ATOM   4450 C C   . THR C 3 185 ? 35.395  -33.317 -70.324 1.00 173.23 ? 185 THR L C   1 
ATOM   4451 O O   . THR C 3 185 ? 34.986  -33.985 -69.357 1.00 168.34 ? 185 THR L O   1 
ATOM   4452 C CB  . THR C 3 185 ? 34.864  -30.939 -69.716 1.00 177.14 ? 185 THR L CB  1 
ATOM   4453 O OG1 . THR C 3 185 ? 34.564  -31.444 -68.416 1.00 194.04 ? 185 THR L OG1 1 
ATOM   4454 C CG2 . THR C 3 185 ? 34.033  -29.705 -69.992 1.00 180.73 ? 185 THR L CG2 1 
ATOM   4455 N N   . LEU C 3 186 ? 36.478  -33.606 -71.044 1.00 171.29 ? 186 LEU L N   1 
ATOM   4456 C CA  . LEU C 3 186 ? 37.305  -34.800 -70.739 1.00 156.26 ? 186 LEU L CA  1 
ATOM   4457 C C   . LEU C 3 186 ? 38.776  -34.482 -71.008 1.00 157.57 ? 186 LEU L C   1 
ATOM   4458 O O   . LEU C 3 186 ? 39.052  -33.442 -71.631 1.00 156.67 ? 186 LEU L O   1 
ATOM   4459 C CB  . LEU C 3 186 ? 36.825  -35.961 -71.612 1.00 146.24 ? 186 LEU L CB  1 
ATOM   4460 C CG  . LEU C 3 186 ? 35.735  -36.834 -70.994 1.00 151.74 ? 186 LEU L CG  1 
ATOM   4461 C CD1 . LEU C 3 186 ? 35.530  -38.101 -71.809 1.00 157.84 ? 186 LEU L CD1 1 
ATOM   4462 C CD2 . LEU C 3 186 ? 36.079  -37.178 -69.554 1.00 151.50 ? 186 LEU L CD2 1 
ATOM   4463 N N   . SER C 3 187 ? 39.680  -35.346 -70.545 1.00 157.83 ? 187 SER L N   1 
ATOM   4464 C CA  . SER C 3 187 ? 41.105  -35.148 -70.775 1.00 141.56 ? 187 SER L CA  1 
ATOM   4465 C C   . SER C 3 187 ? 41.462  -35.458 -72.227 1.00 150.47 ? 187 SER L C   1 
ATOM   4466 O O   . SER C 3 187 ? 40.704  -36.111 -72.950 1.00 165.02 ? 187 SER L O   1 
ATOM   4467 C CB  . SER C 3 187 ? 41.927  -36.028 -69.832 1.00 124.54 ? 187 SER L CB  1 
ATOM   4468 O OG  . SER C 3 187 ? 41.708  -37.406 -70.096 1.00 164.26 ? 187 SER L OG  1 
ATOM   4469 N N   . LYS C 3 188 ? 42.635  -34.972 -72.654 1.00 156.31 ? 188 LYS L N   1 
ATOM   4470 C CA  . LYS C 3 188 ? 43.130  -35.310 -73.987 1.00 154.91 ? 188 LYS L CA  1 
ATOM   4471 C C   . LYS C 3 188 ? 43.203  -36.814 -74.180 1.00 158.61 ? 188 LYS L C   1 
ATOM   4472 O O   . LYS C 3 188 ? 42.918  -37.320 -75.271 1.00 158.84 ? 188 LYS L O   1 
ATOM   4473 C CB  . LYS C 3 188 ? 44.520  -34.726 -74.235 1.00 144.63 ? 188 LYS L CB  1 
ATOM   4474 C CG  . LYS C 3 188 ? 44.639  -33.233 -74.379 1.00 126.63 ? 188 LYS L CG  1 
ATOM   4475 C CD  . LYS C 3 188 ? 46.108  -32.923 -74.627 1.00 138.69 ? 188 LYS L CD  1 
ATOM   4476 C CE  . LYS C 3 188 ? 46.383  -31.453 -74.844 1.00 174.35 ? 188 LYS L CE  1 
ATOM   4477 N NZ  . LYS C 3 188 ? 47.833  -31.208 -75.083 1.00 159.52 ? 188 LYS L NZ  1 
ATOM   4478 N N   . ALA C 3 189 ? 43.624  -37.536 -73.138 1.00 166.56 ? 189 ALA L N   1 
ATOM   4479 C CA  . ALA C 3 189 ? 43.724  -38.988 -73.213 1.00 163.09 ? 189 ALA L CA  1 
ATOM   4480 C C   . ALA C 3 189 ? 42.452  -39.693 -73.667 1.00 185.97 ? 189 ALA L C   1 
ATOM   4481 O O   . ALA C 3 189 ? 42.488  -40.573 -74.534 1.00 199.95 ? 189 ALA L O   1 
ATOM   4482 C CB  . ALA C 3 189 ? 44.064  -39.555 -71.832 1.00 133.77 ? 189 ALA L CB  1 
ATOM   4483 N N   . ASP C 3 190 ? 41.306  -39.275 -73.122 1.00 177.89 ? 190 ASP L N   1 
ATOM   4484 C CA  . ASP C 3 190 ? 40.036  -39.904 -73.474 1.00 184.58 ? 190 ASP L CA  1 
ATOM   4485 C C   . ASP C 3 190 ? 39.667  -39.454 -74.885 1.00 189.97 ? 190 ASP L C   1 
ATOM   4486 O O   . ASP C 3 190 ? 39.040  -40.206 -75.640 1.00 198.05 ? 190 ASP L O   1 
ATOM   4487 C CB  . ASP C 3 190 ? 38.942  -39.508 -72.479 1.00 177.31 ? 190 ASP L CB  1 
ATOM   4488 C CG  . ASP C 3 190 ? 39.080  -40.216 -71.139 1.00 184.42 ? 190 ASP L CG  1 
ATOM   4489 O OD1 . ASP C 3 190 ? 39.834  -41.207 -71.056 1.00 183.28 ? 190 ASP L OD1 1 
ATOM   4490 O OD2 . ASP C 3 190 ? 38.431  -39.779 -70.166 1.00 187.10 ? 190 ASP L OD2 1 
ATOM   4491 N N   . TYR C 3 191 ? 40.045  -38.225 -75.258 1.00 187.24 ? 191 TYR L N   1 
ATOM   4492 C CA  . TYR C 3 191 ? 39.776  -37.745 -76.612 1.00 185.87 ? 191 TYR L CA  1 
ATOM   4493 C C   . TYR C 3 191 ? 40.500  -38.596 -77.648 1.00 200.55 ? 191 TYR L C   1 
ATOM   4494 O O   . TYR C 3 191 ? 39.921  -38.967 -78.676 1.00 214.78 ? 191 TYR L O   1 
ATOM   4495 C CB  . TYR C 3 191 ? 40.185  -36.275 -76.742 1.00 168.94 ? 191 TYR L CB  1 
ATOM   4496 C CG  . TYR C 3 191 ? 39.667  -35.598 -77.995 1.00 167.64 ? 191 TYR L CG  1 
ATOM   4497 C CD1 . TYR C 3 191 ? 38.312  -35.340 -78.161 1.00 172.68 ? 191 TYR L CD1 1 
ATOM   4498 C CD2 . TYR C 3 191 ? 40.532  -35.229 -79.017 1.00 171.26 ? 191 TYR L CD2 1 
ATOM   4499 C CE1 . TYR C 3 191 ? 37.832  -34.725 -79.308 1.00 176.81 ? 191 TYR L CE1 1 
ATOM   4500 C CE2 . TYR C 3 191 ? 40.064  -34.615 -80.167 1.00 177.05 ? 191 TYR L CE2 1 
ATOM   4501 C CZ  . TYR C 3 191 ? 38.714  -34.365 -80.308 1.00 183.02 ? 191 TYR L CZ  1 
ATOM   4502 O OH  . TYR C 3 191 ? 38.248  -33.754 -81.451 1.00 185.37 ? 191 TYR L OH  1 
ATOM   4503 N N   . GLU C 3 192 ? 41.763  -38.934 -77.384 1.00 193.78 ? 192 GLU L N   1 
ATOM   4504 C CA  . GLU C 3 192 ? 42.546  -39.755 -78.298 1.00 185.91 ? 192 GLU L CA  1 
ATOM   4505 C C   . GLU C 3 192 ? 42.219  -41.243 -78.189 1.00 198.53 ? 192 GLU L C   1 
ATOM   4506 O O   . GLU C 3 192 ? 42.463  -41.989 -79.144 1.00 197.33 ? 192 GLU L O   1 
ATOM   4507 C CB  . GLU C 3 192 ? 44.036  -39.519 -78.038 1.00 167.31 ? 192 GLU L CB  1 
ATOM   4508 C CG  . GLU C 3 192 ? 44.970  -40.130 -79.062 1.00 165.07 ? 192 GLU L CG  1 
ATOM   4509 C CD  . GLU C 3 192 ? 46.414  -40.101 -78.610 1.00 178.09 ? 192 GLU L CD  1 
ATOM   4510 O OE1 . GLU C 3 192 ? 46.679  -39.625 -77.485 1.00 166.69 ? 192 GLU L OE1 1 
ATOM   4511 O OE2 . GLU C 3 192 ? 47.284  -40.551 -79.383 1.00 180.54 ? 192 GLU L OE2 1 
ATOM   4512 N N   . LYS C 3 193 ? 41.664  -41.686 -77.056 1.00 196.36 ? 193 LYS L N   1 
ATOM   4513 C CA  . LYS C 3 193 ? 41.331  -43.097 -76.872 1.00 182.50 ? 193 LYS L CA  1 
ATOM   4514 C C   . LYS C 3 193 ? 40.169  -43.530 -77.755 1.00 179.46 ? 193 LYS L C   1 
ATOM   4515 O O   . LYS C 3 193 ? 40.139  -44.673 -78.230 1.00 160.67 ? 193 LYS L O   1 
ATOM   4516 C CB  . LYS C 3 193 ? 40.973  -43.363 -75.408 1.00 177.48 ? 193 LYS L CB  1 
ATOM   4517 C CG  . LYS C 3 193 ? 42.120  -43.199 -74.431 1.00 186.21 ? 193 LYS L CG  1 
ATOM   4518 C CD  . LYS C 3 193 ? 41.661  -43.412 -72.999 1.00 183.13 ? 193 LYS L CD  1 
ATOM   4519 C CE  . LYS C 3 193 ? 42.811  -43.227 -72.025 1.00 176.06 ? 193 LYS L CE  1 
ATOM   4520 N NZ  . LYS C 3 193 ? 42.365  -43.398 -70.619 1.00 162.82 ? 193 LYS L NZ  1 
ATOM   4521 N N   . HIS C 3 194 ? 39.202  -42.643 -77.974 1.00 181.54 ? 194 HIS L N   1 
ATOM   4522 C CA  . HIS C 3 194 ? 37.925  -43.003 -78.572 1.00 178.67 ? 194 HIS L CA  1 
ATOM   4523 C C   . HIS C 3 194 ? 37.587  -41.979 -79.640 1.00 172.05 ? 194 HIS L C   1 
ATOM   4524 O O   . HIS C 3 194 ? 37.502  -40.783 -79.346 1.00 181.85 ? 194 HIS L O   1 
ATOM   4525 C CB  . HIS C 3 194 ? 36.836  -43.059 -77.501 1.00 166.76 ? 194 HIS L CB  1 
ATOM   4526 C CG  . HIS C 3 194 ? 37.107  -44.071 -76.433 1.00 168.73 ? 194 HIS L CG  1 
ATOM   4527 N ND1 . HIS C 3 194 ? 37.083  -45.428 -76.671 1.00 168.28 ? 194 HIS L ND1 1 
ATOM   4528 C CD2 . HIS C 3 194 ? 37.426  -43.924 -75.125 1.00 162.77 ? 194 HIS L CD2 1 
ATOM   4529 C CE1 . HIS C 3 194 ? 37.371  -46.074 -75.555 1.00 179.48 ? 194 HIS L CE1 1 
ATOM   4530 N NE2 . HIS C 3 194 ? 37.582  -45.184 -74.601 1.00 180.30 ? 194 HIS L NE2 1 
ATOM   4531 N N   . LYS C 3 195 ? 37.396  -42.443 -80.876 1.00 155.82 ? 195 LYS L N   1 
ATOM   4532 C CA  . LYS C 3 195 ? 37.175  -41.510 -81.973 1.00 156.86 ? 195 LYS L CA  1 
ATOM   4533 C C   . LYS C 3 195 ? 35.746  -40.995 -82.029 1.00 168.56 ? 195 LYS L C   1 
ATOM   4534 O O   . LYS C 3 195 ? 35.522  -39.871 -82.488 1.00 184.81 ? 195 LYS L O   1 
ATOM   4535 C CB  . LYS C 3 195 ? 37.529  -42.153 -83.315 1.00 171.28 ? 195 LYS L CB  1 
ATOM   4536 C CG  . LYS C 3 195 ? 38.852  -42.878 -83.325 1.00 166.47 ? 195 LYS L CG  1 
ATOM   4537 C CD  . LYS C 3 195 ? 39.161  -43.428 -84.703 1.00 146.78 ? 195 LYS L CD  1 
ATOM   4538 C CE  . LYS C 3 195 ? 40.481  -44.175 -84.714 1.00 126.62 ? 195 LYS L CE  1 
ATOM   4539 N NZ  . LYS C 3 195 ? 40.805  -44.695 -86.070 1.00 111.27 ? 195 LYS L NZ  1 
ATOM   4540 N N   . VAL C 3 196 ? 34.775  -41.770 -81.570 1.00 175.61 ? 196 VAL L N   1 
ATOM   4541 C CA  . VAL C 3 196 ? 33.385  -41.520 -81.919 1.00 172.43 ? 196 VAL L CA  1 
ATOM   4542 C C   . VAL C 3 196 ? 32.615  -40.956 -80.738 1.00 160.50 ? 196 VAL L C   1 
ATOM   4543 O O   . VAL C 3 196 ? 32.672  -41.480 -79.618 1.00 163.37 ? 196 VAL L O   1 
ATOM   4544 C CB  . VAL C 3 196 ? 32.733  -42.787 -82.473 1.00 180.90 ? 196 VAL L CB  1 
ATOM   4545 C CG1 . VAL C 3 196 ? 31.238  -42.594 -82.653 1.00 172.35 ? 196 VAL L CG1 1 
ATOM   4546 C CG2 . VAL C 3 196 ? 33.381  -43.036 -83.810 1.00 166.31 ? 196 VAL L CG2 1 
ATOM   4547 N N   . TYR C 3 197 ? 31.896  -39.844 -80.943 1.00 146.08 ? 197 TYR L N   1 
ATOM   4548 C CA  . TYR C 3 197 ? 31.243  -39.176 -79.780 1.00 143.47 ? 197 TYR L CA  1 
ATOM   4549 C C   . TYR C 3 197 ? 29.757  -38.888 -80.028 1.00 166.65 ? 197 TYR L C   1 
ATOM   4550 O O   . TYR C 3 197 ? 29.386  -37.697 -80.038 1.00 183.53 ? 197 TYR L O   1 
ATOM   4551 C CB  . TYR C 3 197 ? 31.944  -37.848 -79.486 1.00 156.02 ? 197 TYR L CB  1 
ATOM   4552 C CG  . TYR C 3 197 ? 33.450  -37.901 -79.527 1.00 161.24 ? 197 TYR L CG  1 
ATOM   4553 C CD1 . TYR C 3 197 ? 34.165  -38.637 -78.597 1.00 147.45 ? 197 TYR L CD1 1 
ATOM   4554 C CD2 . TYR C 3 197 ? 34.161  -37.230 -80.508 1.00 172.06 ? 197 TYR L CD2 1 
ATOM   4555 C CE1 . TYR C 3 197 ? 35.548  -38.690 -78.631 1.00 151.83 ? 197 TYR L CE1 1 
ATOM   4556 C CE2 . TYR C 3 197 ? 35.544  -37.277 -80.559 1.00 178.22 ? 197 TYR L CE2 1 
ATOM   4557 C CZ  . TYR C 3 197 ? 36.241  -38.011 -79.617 1.00 179.24 ? 197 TYR L CZ  1 
ATOM   4558 O OH  . TYR C 3 197 ? 37.612  -38.067 -79.658 1.00 189.32 ? 197 TYR L OH  1 
ATOM   4559 N N   . ALA C 3 198 ? 28.928  -39.925 -80.173 1.00 142.91 ? 198 ALA L N   1 
ATOM   4560 C CA  . ALA C 3 198 ? 27.492  -39.717 -80.485 1.00 152.44 ? 198 ALA L CA  1 
ATOM   4561 C C   . ALA C 3 198 ? 26.722  -39.265 -79.237 1.00 145.51 ? 198 ALA L C   1 
ATOM   4562 O O   . ALA C 3 198 ? 26.967  -39.836 -78.158 1.00 150.25 ? 198 ALA L O   1 
ATOM   4563 C CB  . ALA C 3 198 ? 26.906  -40.983 -81.059 1.00 157.29 ? 198 ALA L CB  1 
ATOM   4564 N N   . CYS C 3 199 ? 25.822  -38.284 -79.380 1.00 132.56 ? 199 CYS L N   1 
ATOM   4565 C CA  . CYS C 3 199 ? 24.968  -37.844 -78.241 1.00 128.15 ? 199 CYS L CA  1 
ATOM   4566 C C   . CYS C 3 199 ? 23.628  -38.566 -78.398 1.00 150.29 ? 199 CYS L C   1 
ATOM   4567 O O   . CYS C 3 199 ? 23.616  -39.523 -79.170 1.00 167.16 ? 199 CYS L O   1 
ATOM   4568 C CB  . CYS C 3 199 ? 24.763  -36.335 -78.262 1.00 146.42 ? 199 CYS L CB  1 
ATOM   4569 S SG  . CYS C 3 199 ? 26.313  -35.398 -78.252 0.74 180.42 ? 199 CYS L SG  1 
ATOM   4570 N N   . GLU C 3 200 ? 22.871  -38.118 -77.491 1.00 30.00  ? 200 GLU L N   1 
ATOM   4571 C CA  . GLU C 3 200 ? 21.479  -38.440 -77.779 1.00 30.00  ? 200 GLU L CA  1 
ATOM   4572 C C   . GLU C 3 200 ? 20.484  -37.438 -77.205 1.00 30.00  ? 200 GLU L C   1 
ATOM   4573 O O   . GLU C 3 200 ? 20.325  -37.242 -76.013 1.00 30.00  ? 200 GLU L O   1 
ATOM   4574 C CB  . GLU C 3 200 ? 21.168  -39.826 -77.210 1.00 30.00  ? 200 GLU L CB  1 
ATOM   4575 C CG  . GLU C 3 200 ? 19.764  -40.323 -77.517 1.00 30.00  ? 200 GLU L CG  1 
ATOM   4576 C CD  . GLU C 3 200 ? 19.511  -41.718 -76.978 1.00 30.00  ? 200 GLU L CD  1 
ATOM   4577 O OE1 . GLU C 3 200 ? 20.418  -42.281 -76.332 1.00 30.00  ? 200 GLU L OE1 1 
ATOM   4578 O OE2 . GLU C 3 200 ? 18.404  -42.252 -77.203 1.00 30.00  ? 200 GLU L OE2 1 
ATOM   4579 N N   . VAL C 3 201 ? 19.711  -36.814 -78.110 1.00 30.00  ? 201 VAL L N   1 
ATOM   4580 C CA  . VAL C 3 201 ? 18.682  -35.820 -77.698 1.00 30.00  ? 201 VAL L CA  1 
ATOM   4581 C C   . VAL C 3 201 ? 17.320  -36.514 -77.663 1.00 30.00  ? 201 VAL L C   1 
ATOM   4582 O O   . VAL C 3 201 ? 17.051  -37.319 -78.573 1.00 30.00  ? 201 VAL L O   1 
ATOM   4583 C CB  . VAL C 3 201 ? 18.669  -34.592 -78.624 1.00 30.00  ? 201 VAL L CB  1 
ATOM   4584 C CG1 . VAL C 3 201 ? 17.495  -33.669 -78.337 1.00 30.00  ? 201 VAL L CG1 1 
ATOM   4585 C CG2 . VAL C 3 201 ? 19.985  -33.836 -78.552 1.00 30.00  ? 201 VAL L CG2 1 
ATOM   4586 N N   . THR C 3 202 ? 16.502  -36.214 -76.652 1.00 161.86 ? 202 THR L N   1 
ATOM   4587 C CA  . THR C 3 202 ? 15.155  -36.828 -76.531 1.00 159.05 ? 202 THR L CA  1 
ATOM   4588 C C   . THR C 3 202 ? 14.179  -35.801 -75.958 1.00 181.86 ? 202 THR L C   1 
ATOM   4589 O O   . THR C 3 202 ? 14.488  -35.249 -74.901 1.00 182.40 ? 202 THR L O   1 
ATOM   4590 C CB  . THR C 3 202 ? 15.200  -38.052 -75.613 1.00 132.78 ? 202 THR L CB  1 
ATOM   4591 O OG1 . THR C 3 202 ? 16.214  -37.823 -74.634 1.00 145.24 ? 202 THR L OG1 1 
ATOM   4592 C CG2 . THR C 3 202 ? 15.482  -39.340 -76.352 1.00 131.01 ? 202 THR L CG2 1 
ATOM   4593 N N   . HIS C 3 203 ? 13.053  -35.551 -76.629 1.00 186.38 ? 203 HIS L N   1 
ATOM   4594 C CA  . HIS C 3 203 ? 12.017  -34.643 -76.064 1.00 163.60 ? 203 HIS L CA  1 
ATOM   4595 C C   . HIS C 3 203 ? 10.677  -34.938 -76.744 1.00 153.93 ? 203 HIS L C   1 
ATOM   4596 O O   . HIS C 3 203 ? 10.573  -35.973 -77.436 1.00 164.37 ? 203 HIS L O   1 
ATOM   4597 C CB  . HIS C 3 203 ? 12.430  -33.175 -76.211 1.00 173.40 ? 203 HIS L CB  1 
ATOM   4598 C CG  . HIS C 3 203 ? 12.610  -32.755 -77.626 1.00 201.69 ? 203 HIS L CG  1 
ATOM   4599 N ND1 . HIS C 3 203 ? 11.557  -32.463 -78.464 1.00 212.79 ? 203 HIS L ND1 1 
ATOM   4600 C CD2 . HIS C 3 203 ? 13.722  -32.557 -78.338 1.00 233.18 ? 203 HIS L CD2 1 
ATOM   4601 C CE1 . HIS C 3 203 ? 12.033  -32.109 -79.648 1.00 247.88 ? 203 HIS L CE1 1 
ATOM   4602 N NE2 . HIS C 3 203 ? 13.345  -32.155 -79.590 1.00 265.33 ? 203 HIS L NE2 1 
ATOM   4603 N N   . GLN C 3 204 ? 9.686   -34.061 -76.566 1.00 177.50 ? 204 GLN L N   1 
ATOM   4604 C CA  . GLN C 3 204 ? 8.328   -34.326 -77.111 1.00 193.36 ? 204 GLN L CA  1 
ATOM   4605 C C   . GLN C 3 204 ? 8.279   -34.165 -78.633 1.00 191.65 ? 204 GLN L C   1 
ATOM   4606 O O   . GLN C 3 204 ? 7.846   -35.120 -79.305 1.00 210.46 ? 204 GLN L O   1 
ATOM   4607 C CB  . GLN C 3 204 ? 7.320   -33.370 -76.476 1.00 200.13 ? 204 GLN L CB  1 
ATOM   4608 C CG  . GLN C 3 204 ? 5.889   -33.605 -76.936 1.00 203.02 ? 204 GLN L CG  1 
ATOM   4609 C CD  . GLN C 3 204 ? 4.918   -32.653 -76.282 1.00 198.61 ? 204 GLN L CD  1 
ATOM   4610 O OE1 . GLN C 3 204 ? 5.007   -31.439 -76.442 1.00 212.03 ? 204 GLN L OE1 1 
ATOM   4611 N NE2 . GLN C 3 204 ? 3.973   -33.205 -75.539 1.00 192.51 ? 204 GLN L NE2 1 
ATOM   4612 N N   . GLY C 3 205 ? 8.716   -33.022 -79.163 1.00 186.24 ? 205 GLY L N   1 
ATOM   4613 C CA  . GLY C 3 205 ? 8.586   -32.761 -80.611 1.00 181.35 ? 205 GLY L CA  1 
ATOM   4614 C C   . GLY C 3 205 ? 9.235   -33.826 -81.476 1.00 176.02 ? 205 GLY L C   1 
ATOM   4615 O O   . GLY C 3 205 ? 8.902   -33.887 -82.673 1.00 136.74 ? 205 GLY L O   1 
ATOM   4616 N N   . LEU C 3 206 ? 10.097  -34.656 -80.887 1.00 155.15 ? 206 LEU L N   1 
ATOM   4617 C CA  . LEU C 3 206 ? 10.833  -35.680 -81.674 1.00 174.20 ? 206 LEU L CA  1 
ATOM   4618 C C   . LEU C 3 206 ? 10.291  -37.075 -81.360 1.00 172.70 ? 206 LEU L C   1 
ATOM   4619 O O   . LEU C 3 206 ? 10.504  -37.544 -80.227 1.00 190.68 ? 206 LEU L O   1 
ATOM   4620 C CB  . LEU C 3 206 ? 12.319  -35.604 -81.314 1.00 200.72 ? 206 LEU L CB  1 
ATOM   4621 C CG  . LEU C 3 206 ? 13.120  -34.519 -82.028 1.00 199.12 ? 206 LEU L CG  1 
ATOM   4622 C CD1 . LEU C 3 206 ? 14.605  -34.674 -81.739 1.00 213.19 ? 206 LEU L CD1 1 
ATOM   4623 C CD2 . LEU C 3 206 ? 12.863  -34.558 -83.526 1.00 188.62 ? 206 LEU L CD2 1 
ATOM   4624 N N   . SER C 3 207 ? 9.626   -37.712 -82.325 1.00 156.10 ? 207 SER L N   1 
ATOM   4625 C CA  . SER C 3 207 ? 9.179   -39.111 -82.115 1.00 149.67 ? 207 SER L CA  1 
ATOM   4626 C C   . SER C 3 207 ? 10.404  -40.021 -82.211 1.00 153.84 ? 207 SER L C   1 
ATOM   4627 O O   . SER C 3 207 ? 10.364  -41.129 -81.645 1.00 121.27 ? 207 SER L O   1 
ATOM   4628 C CB  . SER C 3 207 ? 8.134   -39.498 -83.116 1.00 30.00  ? 207 SER L CB  1 
ATOM   4629 O OG  . SER C 3 207 ? 7.742   -40.850 -82.937 1.00 30.00  ? 207 SER L OG  1 
ATOM   4630 N N   . SER C 3 208 ? 11.447  -39.559 -82.908 1.00 193.38 ? 208 SER L N   1 
ATOM   4631 C CA  . SER C 3 208 ? 12.692  -40.355 -83.068 1.00 192.49 ? 208 SER L CA  1 
ATOM   4632 C C   . SER C 3 208 ? 13.852  -39.665 -82.344 1.00 205.55 ? 208 SER L C   1 
ATOM   4633 O O   . SER C 3 208 ? 14.096  -38.476 -82.622 1.00 223.75 ? 208 SER L O   1 
ATOM   4634 C CB  . SER C 3 208 ? 13.017  -40.551 -84.523 1.00 188.75 ? 208 SER L CB  1 
ATOM   4635 O OG  . SER C 3 208 ? 14.299  -41.141 -84.675 1.00 181.46 ? 208 SER L OG  1 
ATOM   4636 N N   . PRO C 3 209 ? 14.583  -40.354 -81.443 1.00 201.18 ? 209 PRO L N   1 
ATOM   4637 C CA  . PRO C 3 209 ? 15.746  -39.755 -80.789 1.00 199.72 ? 209 PRO L CA  1 
ATOM   4638 C C   . PRO C 3 209 ? 16.827  -39.415 -81.825 1.00 213.09 ? 209 PRO L C   1 
ATOM   4639 O O   . PRO C 3 209 ? 17.149  -40.268 -82.627 1.00 213.02 ? 209 PRO L O   1 
ATOM   4640 C CB  . PRO C 3 209 ? 16.239  -40.857 -79.842 1.00 173.84 ? 209 PRO L CB  1 
ATOM   4641 C CG  . PRO C 3 209 ? 15.656  -42.136 -80.406 1.00 170.53 ? 209 PRO L CG  1 
ATOM   4642 C CD  . PRO C 3 209 ? 14.331  -41.728 -81.012 1.00 169.61 ? 209 PRO L CD  1 
ATOM   4643 N N   . VAL C 3 210 ? 17.349  -38.186 -81.788 1.00 207.44 ? 210 VAL L N   1 
ATOM   4644 C CA  . VAL C 3 210 ? 18.410  -37.757 -82.747 1.00 192.24 ? 210 VAL L CA  1 
ATOM   4645 C C   . VAL C 3 210 ? 19.774  -37.830 -82.056 1.00 184.73 ? 210 VAL L C   1 
ATOM   4646 O O   . VAL C 3 210 ? 19.998  -37.046 -81.118 1.00 197.43 ? 210 VAL L O   1 
ATOM   4647 C CB  . VAL C 3 210 ? 18.137  -36.342 -83.288 1.00 177.00 ? 210 VAL L CB  1 
ATOM   4648 C CG1 . VAL C 3 210 ? 19.307  -35.815 -84.104 1.00 153.93 ? 210 VAL L CG1 1 
ATOM   4649 C CG2 . VAL C 3 210 ? 16.852  -36.292 -84.099 1.00 196.36 ? 210 VAL L CG2 1 
ATOM   4650 N N   . THR C 3 211 ? 20.690  -38.657 -82.574 1.00 185.52 ? 211 THR L N   1 
ATOM   4651 C CA  . THR C 3 211 ? 22.088  -38.683 -82.063 1.00 161.47 ? 211 THR L CA  1 
ATOM   4652 C C   . THR C 3 211 ? 22.962  -38.136 -83.193 1.00 157.01 ? 211 THR L C   1 
ATOM   4653 O O   . THR C 3 211 ? 22.844  -38.671 -84.309 1.00 180.15 ? 211 THR L O   1 
ATOM   4654 C CB  . THR C 3 211 ? 22.502  -40.095 -81.648 1.00 161.75 ? 211 THR L CB  1 
ATOM   4655 O OG1 . THR C 3 211 ? 22.899  -40.801 -82.824 1.00 190.88 ? 211 THR L OG1 1 
ATOM   4656 C CG2 . THR C 3 211 ? 21.394  -40.849 -80.946 1.00 174.10 ? 211 THR L CG2 1 
ATOM   4657 N N   . LYS C 3 212 ? 23.885  -37.212 -82.911 1.00 159.51 ? 212 LYS L N   1 
ATOM   4658 C CA  . LYS C 3 212 ? 24.844  -36.783 -83.971 1.00 163.35 ? 212 LYS L CA  1 
ATOM   4659 C C   . LYS C 3 212 ? 26.221  -37.364 -83.624 1.00 162.07 ? 212 LYS L C   1 
ATOM   4660 O O   . LYS C 3 212 ? 26.786  -36.942 -82.598 1.00 156.47 ? 212 LYS L O   1 
ATOM   4661 C CB  . LYS C 3 212 ? 24.867  -35.260 -84.124 1.00 143.11 ? 212 LYS L CB  1 
ATOM   4662 C CG  . LYS C 3 212 ? 23.556  -34.619 -84.558 1.00 144.27 ? 212 LYS L CG  1 
ATOM   4663 C CD  . LYS C 3 212 ? 23.693  -33.138 -84.832 1.00 123.75 ? 212 LYS L CD  1 
ATOM   4664 C CE  . LYS C 3 212 ? 22.442  -32.522 -85.419 1.00 137.95 ? 212 LYS L CE  1 
ATOM   4665 N NZ  . LYS C 3 212 ? 22.684  -31.136 -85.884 1.00 145.85 ? 212 LYS L NZ  1 
ATOM   4666 N N   . SER C 3 213 ? 26.745  -38.282 -84.446 1.00 170.35 ? 213 SER L N   1 
ATOM   4667 C CA  . SER C 3 213 ? 28.021  -38.981 -84.120 1.00 165.33 ? 213 SER L CA  1 
ATOM   4668 C C   . SER C 3 213 ? 29.182  -38.004 -83.893 1.00 183.77 ? 213 SER L C   1 
ATOM   4669 O O   . SER C 3 213 ? 29.653  -37.931 -82.743 1.00 207.03 ? 213 SER L O   1 
ATOM   4670 C CB  . SER C 3 213 ? 28.367  -39.983 -85.194 1.00 158.89 ? 213 SER L CB  1 
ATOM   4671 O OG  . SER C 3 213 ? 29.605  -40.619 -84.911 1.00 149.08 ? 213 SER L OG  1 
ATOM   4672 N N   . PHE C 3 214 ? 29.633  -37.303 -84.940 1.00 176.41 ? 214 PHE L N   1 
ATOM   4673 C CA  . PHE C 3 214 ? 30.810  -36.397 -84.821 1.00 188.64 ? 214 PHE L CA  1 
ATOM   4674 C C   . PHE C 3 214 ? 32.114  -37.099 -84.419 1.00 178.42 ? 214 PHE L C   1 
ATOM   4675 O O   . PHE C 3 214 ? 32.623  -36.821 -83.318 1.00 175.64 ? 214 PHE L O   1 
ATOM   4676 C CB  . PHE C 3 214 ? 30.524  -35.238 -83.860 1.00 205.85 ? 214 PHE L CB  1 
ATOM   4677 C CG  . PHE C 3 214 ? 29.701  -34.116 -84.440 1.00 211.85 ? 214 PHE L CG  1 
ATOM   4678 C CD1 . PHE C 3 214 ? 28.400  -34.331 -84.866 1.00 213.83 ? 214 PHE L CD1 1 
ATOM   4679 C CD2 . PHE C 3 214 ? 30.233  -32.843 -84.569 1.00 217.00 ? 214 PHE L CD2 1 
ATOM   4680 C CE1 . PHE C 3 214 ? 27.649  -33.297 -85.401 1.00 232.04 ? 214 PHE L CE1 1 
ATOM   4681 C CE2 . PHE C 3 214 ? 29.481  -31.811 -85.106 1.00 230.40 ? 214 PHE L CE2 1 
ATOM   4682 C CZ  . PHE C 3 214 ? 28.190  -32.038 -85.520 1.00 242.66 ? 214 PHE L CZ  1 
ATOM   4683 N N   . ASN C 3 215 ? 32.642  -37.971 -85.287 1.00 162.95 ? 215 ASN L N   1 
ATOM   4684 C CA  . ASN C 3 215 ? 33.890  -38.726 -84.979 1.00 161.36 ? 215 ASN L CA  1 
ATOM   4685 C C   . ASN C 3 215 ? 35.102  -37.825 -84.711 1.00 170.76 ? 215 ASN L C   1 
ATOM   4686 O O   . ASN C 3 215 ? 34.982  -36.601 -84.920 1.00 186.04 ? 215 ASN L O   1 
ATOM   4687 C CB  . ASN C 3 215 ? 34.182  -39.753 -86.075 1.00 187.83 ? 215 ASN L CB  1 
ATOM   4688 C CG  . ASN C 3 215 ? 32.989  -40.634 -86.380 1.00 203.55 ? 215 ASN L CG  1 
ATOM   4689 O OD1 . ASN C 3 215 ? 31.928  -40.481 -85.778 1.00 211.05 ? 215 ASN L OD1 1 
ATOM   4690 N ND2 . ASN C 3 215 ? 33.153  -41.559 -87.311 1.00 210.97 ? 215 ASN L ND2 1 
ATOM   4691 N N   . ARG C 3 216 ? 36.229  -38.404 -84.274 1.00 156.84 ? 216 ARG L N   1 
ATOM   4692 C CA  . ARG C 3 216 ? 37.399  -37.561 -83.907 1.00 145.75 ? 216 ARG L CA  1 
ATOM   4693 C C   . ARG C 3 216 ? 38.007  -36.989 -85.192 1.00 159.04 ? 216 ARG L C   1 
ATOM   4694 O O   . ARG C 3 216 ? 38.269  -35.771 -85.227 1.00 161.79 ? 216 ARG L O   1 
ATOM   4695 C CB  . ARG C 3 216 ? 38.439  -38.351 -83.105 1.00 137.81 ? 216 ARG L CB  1 
ATOM   4696 C CG  . ARG C 3 216 ? 39.608  -37.500 -82.630 1.00 134.94 ? 216 ARG L CG  1 
ATOM   4697 C CD  . ARG C 3 216 ? 40.553  -38.202 -81.675 1.00 120.51 ? 216 ARG L CD  1 
ATOM   4698 N NE  . ARG C 3 216 ? 41.198  -39.370 -82.255 1.00 143.57 ? 216 ARG L NE  1 
ATOM   4699 C CZ  . ARG C 3 216 ? 41.116  -40.597 -81.754 1.00 186.31 ? 216 ARG L CZ  1 
ATOM   4700 N NH1 . ARG C 3 216 ? 40.311  -40.841 -80.735 1.00 208.07 ? 216 ARG L NH1 1 
ATOM   4701 N NH2 . ARG C 3 216 ? 41.843  -41.573 -82.269 1.00 190.36 ? 216 ARG L NH2 1 
ATOM   4702 N N   . GLY C 3 217 ? 38.209  -37.837 -86.204 1.00 161.86 ? 217 GLY L N   1 
ATOM   4703 C CA  . GLY C 3 217 ? 38.753  -37.370 -87.494 1.00 157.51 ? 217 GLY L CA  1 
ATOM   4704 C C   . GLY C 3 217 ? 37.646  -37.136 -88.507 1.00 182.72 ? 217 GLY L C   1 
ATOM   4705 O O   . GLY C 3 217 ? 36.886  -38.087 -88.777 1.00 193.14 ? 217 GLY L O   1 
ATOM   4706 N N   . GLU C 3 218 ? 37.552  -35.915 -89.042 1.00 193.35 ? 218 GLU L N   1 
ATOM   4707 C CA  . GLU C 3 218 ? 36.496  -35.579 -90.035 1.00 209.72 ? 218 GLU L CA  1 
ATOM   4708 C C   . GLU C 3 218 ? 37.154  -35.041 -91.311 1.00 254.57 ? 218 GLU L C   1 
ATOM   4709 O O   . GLU C 3 218 ? 38.256  -34.472 -91.184 1.00 258.23 ? 218 GLU L O   1 
ATOM   4710 C CB  . GLU C 3 218 ? 35.520  -34.558 -89.448 1.00 195.93 ? 218 GLU L CB  1 
ATOM   4711 C CG  . GLU C 3 218 ? 34.864  -35.023 -88.161 1.00 180.83 ? 218 GLU L CG  1 
ATOM   4712 C CD  . GLU C 3 218 ? 33.891  -34.030 -87.552 1.00 199.03 ? 218 GLU L CD  1 
ATOM   4713 O OE1 . GLU C 3 218 ? 33.699  -32.951 -88.146 1.00 201.37 ? 218 GLU L OE1 1 
ATOM   4714 O OE2 . GLU C 3 218 ? 33.330  -34.337 -86.483 1.00 207.20 ? 218 GLU L OE2 1 
ATOM   4715 N N   . GLY D 1 1   ? 19.879  11.634  -8.142  1.00 130.95 ? 10  GLY A N   1 
ATOM   4716 C CA  . GLY D 1 1   ? 20.516  10.330  -8.132  1.00 139.34 ? 10  GLY A CA  1 
ATOM   4717 C C   . GLY D 1 1   ? 20.169  9.465   -9.328  1.00 144.44 ? 10  GLY A C   1 
ATOM   4718 O O   . GLY D 1 1   ? 19.186  9.712   -10.025 1.00 154.43 ? 10  GLY A O   1 
ATOM   4719 N N   . ASP D 1 2   ? 20.992  8.447   -9.568  1.00 148.49 ? 11  ASP A N   1 
ATOM   4720 C CA  . ASP D 1 2   ? 20.749  7.520   -10.666 1.00 169.07 ? 11  ASP A CA  1 
ATOM   4721 C C   . ASP D 1 2   ? 19.528  6.678   -10.314 1.00 166.83 ? 11  ASP A C   1 
ATOM   4722 O O   . ASP D 1 2   ? 19.411  6.183   -9.191  1.00 174.96 ? 11  ASP A O   1 
ATOM   4723 C CB  . ASP D 1 2   ? 21.954  6.600   -10.847 1.00 179.01 ? 11  ASP A CB  1 
ATOM   4724 C CG  . ASP D 1 2   ? 23.078  7.252   -11.630 1.00 199.87 ? 11  ASP A CG  1 
ATOM   4725 O OD1 . ASP D 1 2   ? 23.032  8.483   -11.844 1.00 200.09 ? 11  ASP A OD1 1 
ATOM   4726 O OD2 . ASP D 1 2   ? 24.023  6.532   -12.010 1.00 213.82 ? 11  ASP A OD2 1 
ATOM   4727 N N   . THR D 1 3   ? 18.610  6.523   -11.269 1.00 186.29 ? 12  THR A N   1 
ATOM   4728 C CA  . THR D 1 3   ? 17.371  5.805   -11.026 1.00 165.16 ? 12  THR A CA  1 
ATOM   4729 C C   . THR D 1 3   ? 17.006  4.986   -12.249 1.00 153.08 ? 12  THR A C   1 
ATOM   4730 O O   . THR D 1 3   ? 17.408  5.307   -13.371 1.00 149.50 ? 12  THR A O   1 
ATOM   4731 C CB  . THR D 1 3   ? 16.199  6.708   -10.609 1.00 152.51 ? 12  THR A CB  1 
ATOM   4732 O OG1 . THR D 1 3   ? 15.099  5.897   -10.186 1.00 148.69 ? 12  THR A OG1 1 
ATOM   4733 C CG2 . THR D 1 3   ? 15.757  7.589   -11.765 1.00 185.77 ? 12  THR A CG2 1 
ATOM   4734 N N   . LEU D 1 4   ? 16.243  3.920   -12.018 1.00 151.36 ? 13  LEU A N   1 
ATOM   4735 C CA  . LEU D 1 4   ? 15.692  3.071   -13.065 1.00 142.72 ? 13  LEU A CA  1 
ATOM   4736 C C   . LEU D 1 4   ? 14.218  2.837   -12.770 1.00 135.29 ? 13  LEU A C   1 
ATOM   4737 O O   . LEU D 1 4   ? 13.860  2.470   -11.646 1.00 151.19 ? 13  LEU A O   1 
ATOM   4738 C CB  . LEU D 1 4   ? 16.453  1.740   -13.068 1.00 124.75 ? 13  LEU A CB  1 
ATOM   4739 C CG  . LEU D 1 4   ? 15.789  0.617   -13.866 1.00 103.71 ? 13  LEU A CG  1 
ATOM   4740 C CD1 . LEU D 1 4   ? 15.812  0.936   -15.345 1.00 126.79 ? 13  LEU A CD1 1 
ATOM   4741 C CD2 . LEU D 1 4   ? 16.476  -0.713  -13.598 1.00 114.04 ? 13  LEU A CD2 1 
ATOM   4742 N N   . CYS D 1 5   ? 13.370  3.043   -13.773 1.00 109.69 ? 14  CYS A N   1 
ATOM   4743 C CA  . CYS D 1 5   ? 11.929  2.934   -13.610 1.00 128.42 ? 14  CYS A CA  1 
ATOM   4744 C C   . CYS D 1 5   ? 11.367  1.866   -14.540 1.00 130.05 ? 14  CYS A C   1 
ATOM   4745 O O   . CYS D 1 5   ? 11.964  1.530   -15.566 1.00 117.02 ? 14  CYS A O   1 
ATOM   4746 C CB  . CYS D 1 5   ? 11.247  4.279   -13.874 1.00 129.69 ? 14  CYS A CB  1 
ATOM   4747 S SG  . CYS D 1 5   ? 11.709  5.547   -12.678 1.00 181.45 ? 14  CYS A SG  1 
ATOM   4748 N N   . ILE D 1 6   ? 10.200  1.340   -14.172 1.00 128.94 ? 15  ILE A N   1 
ATOM   4749 C CA  . ILE D 1 6   ? 9.570   0.227   -14.873 1.00 107.09 ? 15  ILE A CA  1 
ATOM   4750 C C   . ILE D 1 6   ? 8.262   0.729   -15.468 1.00 110.82 ? 15  ILE A C   1 
ATOM   4751 O O   . ILE D 1 6   ? 7.574   1.550   -14.852 1.00 134.26 ? 15  ILE A O   1 
ATOM   4752 C CB  . ILE D 1 6   ? 9.296   -0.961  -13.928 1.00 111.87 ? 15  ILE A CB  1 
ATOM   4753 C CG1 . ILE D 1 6   ? 10.598  -1.585  -13.420 1.00 131.01 ? 15  ILE A CG1 1 
ATOM   4754 C CG2 . ILE D 1 6   ? 8.443   -2.011  -14.625 1.00 105.87 ? 15  ILE A CG2 1 
ATOM   4755 C CD1 . ILE D 1 6   ? 10.440  -2.567  -12.309 1.00 131.46 ? 15  ILE A CD1 1 
ATOM   4756 N N   . GLY D 1 7   ? 7.908   0.233   -16.655 1.00 100.57 ? 16  GLY A N   1 
ATOM   4757 C CA  . GLY D 1 7   ? 6.690   0.699   -17.299 1.00 116.82 ? 16  GLY A CA  1 
ATOM   4758 C C   . GLY D 1 7   ? 6.165   -0.096  -18.483 1.00 112.50 ? 16  GLY A C   1 
ATOM   4759 O O   . GLY D 1 7   ? 6.928   -0.753  -19.198 1.00 87.16  ? 16  GLY A O   1 
ATOM   4760 N N   . TYR D 1 8   ? 4.852   -0.030  -18.699 1.00 104.59 ? 17  TYR A N   1 
ATOM   4761 C CA  . TYR D 1 8   ? 4.188   -0.684  -19.818 1.00 95.74  ? 17  TYR A CA  1 
ATOM   4762 C C   . TYR D 1 8   ? 3.820   0.259   -20.962 1.00 109.99 ? 17  TYR A C   1 
ATOM   4763 O O   . TYR D 1 8   ? 3.862   1.486   -20.834 1.00 126.05 ? 17  TYR A O   1 
ATOM   4764 C CB  . TYR D 1 8   ? 2.912   -1.399  -19.353 1.00 108.97 ? 17  TYR A CB  1 
ATOM   4765 C CG  . TYR D 1 8   ? 1.867   -0.495  -18.730 1.00 121.77 ? 17  TYR A CG  1 
ATOM   4766 C CD1 . TYR D 1 8   ? 1.957   -0.109  -17.400 1.00 126.63 ? 17  TYR A CD1 1 
ATOM   4767 C CD2 . TYR D 1 8   ? 0.790   -0.031  -19.474 1.00 135.25 ? 17  TYR A CD2 1 
ATOM   4768 C CE1 . TYR D 1 8   ? 1.002   0.714   -16.824 1.00 158.11 ? 17  TYR A CE1 1 
ATOM   4769 C CE2 . TYR D 1 8   ? -0.168  0.792   -18.909 1.00 145.59 ? 17  TYR A CE2 1 
ATOM   4770 C CZ  . TYR D 1 8   ? -0.057  1.163   -17.583 1.00 161.19 ? 17  TYR A CZ  1 
ATOM   4771 O OH  . TYR D 1 8   ? -1.010  1.983   -17.020 1.00 182.49 ? 17  TYR A OH  1 
ATOM   4772 N N   . HIS D 1 9   ? 3.439   -0.334  -22.090 1.00 100.73 ? 18  HIS A N   1 
ATOM   4773 C CA  . HIS D 1 9   ? 3.187   0.426   -23.310 1.00 107.93 ? 18  HIS A CA  1 
ATOM   4774 C C   . HIS D 1 9   ? 1.842   1.127   -23.409 1.00 112.33 ? 18  HIS A C   1 
ATOM   4775 O O   . HIS D 1 9   ? 0.841   0.658   -22.864 1.00 116.63 ? 18  HIS A O   1 
ATOM   4776 C CB  . HIS D 1 9   ? 3.296   -0.524  -24.504 1.00 107.86 ? 18  HIS A CB  1 
ATOM   4777 C CG  . HIS D 1 9   ? 3.153   0.158   -25.827 1.00 127.37 ? 18  HIS A CG  1 
ATOM   4778 N ND1 . HIS D 1 9   ? 4.031   1.128   -26.259 1.00 169.24 ? 18  HIS A ND1 1 
ATOM   4779 C CD2 . HIS D 1 9   ? 2.243   0.005   -26.819 1.00 85.07  ? 18  HIS A CD2 1 
ATOM   4780 C CE1 . HIS D 1 9   ? 3.660   1.554   -27.453 1.00 154.80 ? 18  HIS A CE1 1 
ATOM   4781 N NE2 . HIS D 1 9   ? 2.581   0.885   -27.818 1.00 116.22 ? 18  HIS A NE2 1 
ATOM   4782 N N   . ALA D 1 10  ? 1.808   2.250   -24.126 1.00 128.74 ? 19  ALA A N   1 
ATOM   4783 C CA  . ALA D 1 10  ? 0.533   2.976   -24.317 1.00 127.42 ? 19  ALA A CA  1 
ATOM   4784 C C   . ALA D 1 10  ? 0.545   3.711   -25.661 1.00 130.73 ? 19  ALA A C   1 
ATOM   4785 O O   . ALA D 1 10  ? 1.553   4.375   -25.958 1.00 131.16 ? 19  ALA A O   1 
ATOM   4786 C CB  . ALA D 1 10  ? 0.207   3.904   -23.180 1.00 120.28 ? 19  ALA A CB  1 
ATOM   4787 N N   . ASN D 1 11  ? -0.527  3.582   -26.446 1.00 123.82 ? 20  ASN A N   1 
ATOM   4788 C CA  . ASN D 1 11  ? -0.578  4.219   -27.788 1.00 108.99 ? 20  ASN A CA  1 
ATOM   4789 C C   . ASN D 1 11  ? -1.845  5.068   -27.882 1.00 120.73 ? 20  ASN A C   1 
ATOM   4790 O O   . ASN D 1 11  ? -2.375  5.448   -26.828 1.00 130.13 ? 20  ASN A O   1 
ATOM   4791 C CB  . ASN D 1 11  ? -0.512  3.189   -28.915 1.00 121.73 ? 20  ASN A CB  1 
ATOM   4792 C CG  . ASN D 1 11  ? -1.587  2.128   -28.824 1.00 134.61 ? 20  ASN A CG  1 
ATOM   4793 O OD1 . ASN D 1 11  ? -2.402  2.138   -27.906 1.00 141.28 ? 20  ASN A OD1 1 
ATOM   4794 N ND2 . ASN D 1 11  ? -1.594  1.206   -29.772 1.00 117.46 ? 20  ASN A ND2 1 
ATOM   4795 N N   . ASN D 1 12  ? -2.341  5.333   -29.094 1.00 110.46 ? 21  ASN A N   1 
ATOM   4796 C CA  . ASN D 1 12  ? -3.623  6.080   -29.219 1.00 112.81 ? 21  ASN A CA  1 
ATOM   4797 C C   . ASN D 1 12  ? -4.660  5.211   -29.943 1.00 125.74 ? 21  ASN A C   1 
ATOM   4798 O O   . ASN D 1 12  ? -5.421  5.760   -30.764 1.00 152.37 ? 21  ASN A O   1 
ATOM   4799 C CB  . ASN D 1 12  ? -3.428  7.452   -29.872 1.00 122.53 ? 21  ASN A CB  1 
ATOM   4800 C CG  . ASN D 1 12  ? -2.775  7.389   -31.236 1.00 146.27 ? 21  ASN A CG  1 
ATOM   4801 O OD1 . ASN D 1 12  ? -2.490  6.309   -31.748 1.00 146.14 ? 21  ASN A OD1 1 
ATOM   4802 N ND2 . ASN D 1 12  ? -2.543  8.545   -31.836 1.00 148.64 ? 21  ASN A ND2 1 
ATOM   4803 N N   . SER D 1 13  ? -4.694  3.911   -29.636 1.00 128.97 ? 22  SER A N   1 
ATOM   4804 C CA  . SER D 1 13  ? -5.695  3.001   -30.253 1.00 133.72 ? 22  SER A CA  1 
ATOM   4805 C C   . SER D 1 13  ? -6.994  3.042   -29.443 1.00 148.85 ? 22  SER A C   1 
ATOM   4806 O O   . SER D 1 13  ? -7.016  2.473   -28.333 1.00 151.98 ? 22  SER A O   1 
ATOM   4807 C CB  . SER D 1 13  ? -5.160  1.600   -30.351 1.00 130.99 ? 22  SER A CB  1 
ATOM   4808 O OG  . SER D 1 13  ? -4.817  1.110   -29.064 1.00 143.64 ? 22  SER A OG  1 
ATOM   4809 N N   . THR D 1 14  ? -8.032  3.689   -29.981 1.00 138.70 ? 23  THR A N   1 
ATOM   4810 C CA  . THR D 1 14  ? -9.329  3.808   -29.262 1.00 138.97 ? 23  THR A CA  1 
ATOM   4811 C C   . THR D 1 14  ? -10.052 2.457   -29.286 1.00 137.57 ? 23  THR A C   1 
ATOM   4812 O O   . THR D 1 14  ? -11.192 2.394   -28.787 1.00 144.24 ? 23  THR A O   1 
ATOM   4813 C CB  . THR D 1 14  ? -10.194 4.917   -29.872 1.00 142.52 ? 23  THR A CB  1 
ATOM   4814 O OG1 . THR D 1 14  ? -10.530 4.529   -31.204 1.00 132.24 ? 23  THR A OG1 1 
ATOM   4815 C CG2 . THR D 1 14  ? -9.501  6.261   -29.887 1.00 150.24 ? 23  THR A CG2 1 
ATOM   4816 N N   . ASP D 1 15  ? -9.411  1.425   -29.844 1.00 133.62 ? 24  ASP A N   1 
ATOM   4817 C CA  . ASP D 1 15  ? -10.021 0.074   -29.901 1.00 123.68 ? 24  ASP A CA  1 
ATOM   4818 C C   . ASP D 1 15  ? -10.669 -0.266  -28.560 1.00 131.47 ? 24  ASP A C   1 
ATOM   4819 O O   . ASP D 1 15  ? -9.973  -0.164  -27.540 1.00 128.17 ? 24  ASP A O   1 
ATOM   4820 C CB  . ASP D 1 15  ? -8.973  -0.971  -30.281 1.00 120.54 ? 24  ASP A CB  1 
ATOM   4821 C CG  . ASP D 1 15  ? -8.313  -0.699  -31.621 1.00 145.52 ? 24  ASP A CG  1 
ATOM   4822 O OD1 . ASP D 1 15  ? -8.662  0.318   -32.249 1.00 153.26 ? 24  ASP A OD1 1 
ATOM   4823 O OD2 . ASP D 1 15  ? -7.460  -1.510  -32.029 1.00 150.73 ? 24  ASP A OD2 1 
ATOM   4824 N N   . THR D 1 16  ? -11.947 -0.650  -28.567 1.00 131.13 ? 25  THR A N   1 
ATOM   4825 C CA  . THR D 1 16  ? -12.620 -1.076  -27.347 1.00 106.62 ? 25  THR A CA  1 
ATOM   4826 C C   . THR D 1 16  ? -12.770 -2.591  -27.369 1.00 95.84  ? 25  THR A C   1 
ATOM   4827 O O   . THR D 1 16  ? -13.235 -3.158  -28.363 1.00 127.19 ? 25  THR A O   1 
ATOM   4828 C CB  . THR D 1 16  ? -13.992 -0.407  -27.202 1.00 108.09 ? 25  THR A CB  1 
ATOM   4829 O OG1 . THR D 1 16  ? -14.764 -0.620  -28.391 1.00 123.79 ? 25  THR A OG1 1 
ATOM   4830 C CG2 . THR D 1 16  ? -13.838 1.088   -26.963 1.00 109.99 ? 25  THR A CG2 1 
ATOM   4831 N N   . VAL D 1 17  ? -12.359 -3.241  -26.282 1.00 81.71  ? 26  VAL A N   1 
ATOM   4832 C CA  . VAL D 1 17  ? -12.449 -4.690  -26.143 1.00 91.11  ? 26  VAL A CA  1 
ATOM   4833 C C   . VAL D 1 17  ? -13.068 -5.003  -24.789 1.00 100.23 ? 26  VAL A C   1 
ATOM   4834 O O   . VAL D 1 17  ? -12.627 -4.473  -23.762 1.00 112.16 ? 26  VAL A O   1 
ATOM   4835 C CB  . VAL D 1 17  ? -11.074 -5.371  -26.281 1.00 104.01 ? 26  VAL A CB  1 
ATOM   4836 C CG1 . VAL D 1 17  ? -11.198 -6.867  -26.051 1.00 100.48 ? 26  VAL A CG1 1 
ATOM   4837 C CG2 . VAL D 1 17  ? -10.480 -5.097  -27.655 1.00 116.46 ? 26  VAL A CG2 1 
ATOM   4838 N N   . ASP D 1 18  ? -14.089 -5.855  -24.788 1.00 103.54 ? 27  ASP A N   1 
ATOM   4839 C CA  . ASP D 1 18  ? -14.805 -6.204  -23.570 1.00 109.80 ? 27  ASP A CA  1 
ATOM   4840 C C   . ASP D 1 18  ? -14.162 -7.403  -22.882 1.00 102.75 ? 27  ASP A C   1 
ATOM   4841 O O   . ASP D 1 18  ? -13.497 -8.230  -23.512 1.00 101.69 ? 27  ASP A O   1 
ATOM   4842 C CB  . ASP D 1 18  ? -16.276 -6.505  -23.872 1.00 113.28 ? 27  ASP A CB  1 
ATOM   4843 C CG  . ASP D 1 18  ? -17.028 -5.296  -24.415 1.00 118.53 ? 27  ASP A CG  1 
ATOM   4844 O OD1 . ASP D 1 18  ? -16.401 -4.238  -24.634 1.00 130.78 ? 27  ASP A OD1 1 
ATOM   4845 O OD2 . ASP D 1 18  ? -18.255 -5.408  -24.623 1.00 102.61 ? 27  ASP A OD2 1 
ATOM   4846 N N   . THR D 1 19  ? -14.365 -7.481  -21.570 1.00 119.97 ? 28  THR A N   1 
ATOM   4847 C CA  . THR D 1 19  ? -13.860 -8.564  -20.740 1.00 118.07 ? 28  THR A CA  1 
ATOM   4848 C C   . THR D 1 19  ? -15.000 -9.085  -19.874 1.00 124.29 ? 28  THR A C   1 
ATOM   4849 O O   . THR D 1 19  ? -16.131 -8.594  -19.931 1.00 128.45 ? 28  THR A O   1 
ATOM   4850 C CB  . THR D 1 19  ? -12.691 -8.103  -19.859 1.00 130.83 ? 28  THR A CB  1 
ATOM   4851 O OG1 . THR D 1 19  ? -13.122 -7.034  -19.006 1.00 131.45 ? 28  THR A OG1 1 
ATOM   4852 C CG2 . THR D 1 19  ? -11.521 -7.630  -20.712 1.00 107.49 ? 28  THR A CG2 1 
ATOM   4853 N N   . VAL D 1 20  ? -14.692 -10.095 -19.062 1.00 111.00 ? 29  VAL A N   1 
ATOM   4854 C CA  . VAL D 1 20  ? -15.662 -10.575 -18.084 1.00 127.98 ? 29  VAL A CA  1 
ATOM   4855 C C   . VAL D 1 20  ? -15.851 -9.550  -16.973 1.00 133.20 ? 29  VAL A C   1 
ATOM   4856 O O   . VAL D 1 20  ? -16.980 -9.273  -16.552 1.00 129.34 ? 29  VAL A O   1 
ATOM   4857 C CB  . VAL D 1 20  ? -15.226 -11.942 -17.528 1.00 120.65 ? 29  VAL A CB  1 
ATOM   4858 C CG1 . VAL D 1 20  ? -16.129 -12.368 -16.390 1.00 146.65 ? 29  VAL A CG1 1 
ATOM   4859 C CG2 . VAL D 1 20  ? -15.217 -12.982 -18.635 1.00 122.47 ? 29  VAL A CG2 1 
ATOM   4860 N N   . LEU D 1 21  ? -14.755 -8.961  -16.484 1.00 135.41 ? 30  LEU A N   1 
ATOM   4861 C CA  . LEU D 1 21  ? -14.869 -7.985  -15.404 1.00 132.62 ? 30  LEU A CA  1 
ATOM   4862 C C   . LEU D 1 21  ? -15.404 -6.655  -15.919 1.00 135.97 ? 30  LEU A C   1 
ATOM   4863 O O   . LEU D 1 21  ? -16.366 -6.109  -15.369 1.00 142.98 ? 30  LEU A O   1 
ATOM   4864 C CB  . LEU D 1 21  ? -13.519 -7.782  -14.715 1.00 133.75 ? 30  LEU A CB  1 
ATOM   4865 C CG  . LEU D 1 21  ? -12.906 -8.950  -13.938 1.00 136.58 ? 30  LEU A CG  1 
ATOM   4866 C CD1 . LEU D 1 21  ? -11.504 -8.601  -13.450 1.00 157.94 ? 30  LEU A CD1 1 
ATOM   4867 C CD2 . LEU D 1 21  ? -13.797 -9.387  -12.784 1.00 144.79 ? 30  LEU A CD2 1 
ATOM   4868 N N   . GLU D 1 22  ? -14.792 -6.115  -16.968 1.00 112.53 ? 31  GLU A N   1 
ATOM   4869 C CA  . GLU D 1 22  ? -15.124 -4.788  -17.461 1.00 120.73 ? 31  GLU A CA  1 
ATOM   4870 C C   . GLU D 1 22  ? -15.449 -4.853  -18.950 1.00 116.19 ? 31  GLU A C   1 
ATOM   4871 O O   . GLU D 1 22  ? -15.170 -5.846  -19.628 1.00 117.07 ? 31  GLU A O   1 
ATOM   4872 C CB  . GLU D 1 22  ? -13.974 -3.805  -17.192 1.00 138.66 ? 31  GLU A CB  1 
ATOM   4873 C CG  . GLU D 1 22  ? -13.740 -3.524  -15.709 1.00 152.32 ? 31  GLU A CG  1 
ATOM   4874 C CD  . GLU D 1 22  ? -12.551 -2.612  -15.461 1.00 153.65 ? 31  GLU A CD  1 
ATOM   4875 O OE1 . GLU D 1 22  ? -11.792 -2.345  -16.417 1.00 141.22 ? 31  GLU A OE1 1 
ATOM   4876 O OE2 . GLU D 1 22  ? -12.370 -2.167  -14.307 1.00 152.69 ? 31  GLU A OE2 1 
ATOM   4877 N N   . LYS D 1 23  ? -16.042 -3.775  -19.464 1.00 130.82 ? 32  LYS A N   1 
ATOM   4878 C CA  . LYS D 1 23  ? -16.367 -3.716  -20.913 1.00 113.45 ? 32  LYS A CA  1 
ATOM   4879 C C   . LYS D 1 23  ? -15.843 -2.392  -21.474 1.00 115.04 ? 32  LYS A C   1 
ATOM   4880 O O   . LYS D 1 23  ? -15.401 -1.549  -20.671 1.00 121.74 ? 32  LYS A O   1 
ATOM   4881 C CB  . LYS D 1 23  ? -17.875 -3.858  -21.136 1.00 113.52 ? 32  LYS A CB  1 
ATOM   4882 C CG  . LYS D 1 23  ? -18.682 -2.569  -21.050 1.00 111.56 ? 32  LYS A CG  1 
ATOM   4883 C CD  . LYS D 1 23  ? -18.789 -1.994  -19.654 1.00 104.84 ? 32  LYS A CD  1 
ATOM   4884 C CE  . LYS D 1 23  ? -19.436 -0.626  -19.630 1.00 142.34 ? 32  LYS A CE  1 
ATOM   4885 N NZ  . LYS D 1 23  ? -20.783 -0.646  -20.247 1.00 181.05 ? 32  LYS A NZ  1 
ATOM   4886 N N   . ASN D 1 24  ? -15.884 -2.225  -22.797 1.00 123.08 ? 33  ASN A N   1 
ATOM   4887 C CA  . ASN D 1 24  ? -15.421 -0.964  -23.434 1.00 120.97 ? 33  ASN A CA  1 
ATOM   4888 C C   . ASN D 1 24  ? -14.004 -0.639  -22.946 1.00 109.77 ? 33  ASN A C   1 
ATOM   4889 O O   . ASN D 1 24  ? -13.679 0.557   -22.835 1.00 118.37 ? 33  ASN A O   1 
ATOM   4890 C CB  . ASN D 1 24  ? -16.380 0.193   -23.154 1.00 131.29 ? 33  ASN A CB  1 
ATOM   4891 C CG  . ASN D 1 24  ? -17.695 0.063   -23.891 1.00 130.51 ? 33  ASN A CG  1 
ATOM   4892 O OD1 . ASN D 1 24  ? -17.776 -0.617  -24.911 1.00 112.46 ? 33  ASN A OD1 1 
ATOM   4893 N ND2 . ASN D 1 24  ? -18.734 0.699   -23.374 1.00 147.21 ? 33  ASN A ND2 1 
ATOM   4894 N N   . VAL D 1 25  ? -13.196 -1.665  -22.668 1.00 100.58 ? 34  VAL A N   1 
ATOM   4895 C CA  . VAL D 1 25  ? -11.792 -1.449  -22.212 1.00 97.51  ? 34  VAL A CA  1 
ATOM   4896 C C   . VAL D 1 25  ? -10.934 -1.135  -23.439 1.00 104.52 ? 34  VAL A C   1 
ATOM   4897 O O   . VAL D 1 25  ? -10.948 -1.943  -24.384 1.00 117.55 ? 34  VAL A O   1 
ATOM   4898 C CB  . VAL D 1 25  ? -11.254 -2.677  -21.457 1.00 79.28  ? 34  VAL A CB  1 
ATOM   4899 C CG1 . VAL D 1 25  ? -9.812  -2.481  -21.016 1.00 89.45  ? 34  VAL A CG1 1 
ATOM   4900 C CG2 . VAL D 1 25  ? -12.135 -3.042  -20.274 1.00 106.67 ? 34  VAL A CG2 1 
ATOM   4901 N N   . THR D 1 26  ? -10.225 -0.005  -23.424 1.00 93.39  ? 35  THR A N   1 
ATOM   4902 C CA  . THR D 1 26  ? -9.367  0.344   -24.546 1.00 106.30 ? 35  THR A CA  1 
ATOM   4903 C C   . THR D 1 26  ? -8.012  -0.326  -24.370 1.00 119.15 ? 35  THR A C   1 
ATOM   4904 O O   . THR D 1 26  ? -7.367  -0.177  -23.327 1.00 124.56 ? 35  THR A O   1 
ATOM   4905 C CB  . THR D 1 26  ? -9.208  1.859   -24.666 1.00 101.36 ? 35  THR A CB  1 
ATOM   4906 O OG1 . THR D 1 26  ? -8.648  2.380   -23.456 1.00 131.64 ? 35  THR A OG1 1 
ATOM   4907 C CG2 . THR D 1 26  ? -10.561 2.513   -24.931 1.00 105.78 ? 35  THR A CG2 1 
ATOM   4908 N N   . VAL D 1 27  ? -7.594  -1.078  -25.385 1.00 114.11 ? 36  VAL A N   1 
ATOM   4909 C CA  . VAL D 1 27  ? -6.335  -1.804  -25.349 1.00 105.03 ? 36  VAL A CA  1 
ATOM   4910 C C   . VAL D 1 27  ? -5.405  -1.230  -26.411 1.00 110.71 ? 36  VAL A C   1 
ATOM   4911 O O   . VAL D 1 27  ? -5.839  -0.604  -27.382 1.00 127.88 ? 36  VAL A O   1 
ATOM   4912 C CB  . VAL D 1 27  ? -6.535  -3.318  -25.559 1.00 114.95 ? 36  VAL A CB  1 
ATOM   4913 C CG1 . VAL D 1 27  ? -7.382  -3.895  -24.435 1.00 104.09 ? 36  VAL A CG1 1 
ATOM   4914 C CG2 . VAL D 1 27  ? -7.179  -3.583  -26.908 1.00 122.56 ? 36  VAL A CG2 1 
ATOM   4915 N N   . THR D 1 28  ? -4.103  -1.455  -26.213 1.00 108.97 ? 37  THR A N   1 
ATOM   4916 C CA  . THR D 1 28  ? -3.110  -0.932  -27.147 1.00 108.32 ? 37  THR A CA  1 
ATOM   4917 C C   . THR D 1 28  ? -3.233  -1.601  -28.509 1.00 100.41 ? 37  THR A C   1 
ATOM   4918 O O   . THR D 1 28  ? -3.238  -0.928  -29.545 1.00 104.54 ? 37  THR A O   1 
ATOM   4919 C CB  . THR D 1 28  ? -1.699  -1.134  -26.597 1.00 106.47 ? 37  THR A CB  1 
ATOM   4920 O OG1 . THR D 1 28  ? -1.544  -2.492  -26.168 1.00 98.38  ? 37  THR A OG1 1 
ATOM   4921 C CG2 . THR D 1 28  ? -1.458  -0.216  -25.416 1.00 118.33 ? 37  THR A CG2 1 
ATOM   4922 N N   . HIS D 1 29  ? -3.316  -2.929  -28.528 1.00 75.24  ? 38  HIS A N   1 
ATOM   4923 C CA  . HIS D 1 29  ? -3.424  -3.678  -29.771 1.00 94.69  ? 38  HIS A CA  1 
ATOM   4924 C C   . HIS D 1 29  ? -4.479  -4.761  -29.620 1.00 95.42  ? 38  HIS A C   1 
ATOM   4925 O O   . HIS D 1 29  ? -4.558  -5.417  -28.578 1.00 111.32 ? 38  HIS A O   1 
ATOM   4926 C CB  . HIS D 1 29  ? -2.080  -4.302  -30.158 1.00 88.87  ? 38  HIS A CB  1 
ATOM   4927 C CG  . HIS D 1 29  ? -0.989  -3.297  -30.345 1.00 93.03  ? 38  HIS A CG  1 
ATOM   4928 N ND1 . HIS D 1 29  ? -0.970  -2.408  -31.399 1.00 123.40 ? 38  HIS A ND1 1 
ATOM   4929 C CD2 . HIS D 1 29  ? 0.103   -3.017  -29.596 1.00 91.48  ? 38  HIS A CD2 1 
ATOM   4930 C CE1 . HIS D 1 29  ? 0.098   -1.637  -31.301 1.00 126.41 ? 38  HIS A CE1 1 
ATOM   4931 N NE2 . HIS D 1 29  ? 0.765   -1.985  -30.215 1.00 122.18 ? 38  HIS A NE2 1 
ATOM   4932 N N   . SER D 1 30  ? -5.282  -4.952  -30.664 1.00 86.22  ? 39  SER A N   1 
ATOM   4933 C CA  . SER D 1 30  ? -6.338  -5.951  -30.614 1.00 100.40 ? 39  SER A CA  1 
ATOM   4934 C C   . SER D 1 30  ? -6.559  -6.540  -31.999 1.00 111.94 ? 39  SER A C   1 
ATOM   4935 O O   . SER D 1 30  ? -6.156  -5.967  -33.015 1.00 115.66 ? 39  SER A O   1 
ATOM   4936 C CB  . SER D 1 30  ? -7.649  -5.364  -30.078 1.00 106.24 ? 39  SER A CB  1 
ATOM   4937 O OG  . SER D 1 30  ? -8.085  -4.279  -30.877 1.00 123.51 ? 39  SER A OG  1 
ATOM   4938 N N   . VAL D 1 31  ? -7.214  -7.698  -32.020 1.00 98.73  ? 40  VAL A N   1 
ATOM   4939 C CA  . VAL D 1 31  ? -7.613  -8.376  -33.246 1.00 84.97  ? 40  VAL A CA  1 
ATOM   4940 C C   . VAL D 1 31  ? -9.132  -8.455  -33.268 1.00 96.66  ? 40  VAL A C   1 
ATOM   4941 O O   . VAL D 1 31  ? -9.762  -8.703  -32.234 1.00 110.38 ? 40  VAL A O   1 
ATOM   4942 C CB  . VAL D 1 31  ? -6.987  -9.784  -33.349 1.00 72.28  ? 40  VAL A CB  1 
ATOM   4943 C CG1 . VAL D 1 31  ? -7.504  -10.519 -34.576 1.00 88.78  ? 40  VAL A CG1 1 
ATOM   4944 C CG2 . VAL D 1 31  ? -5.469  -9.692  -33.383 1.00 94.74  ? 40  VAL A CG2 1 
ATOM   4945 N N   . ASN D 1 32  ? -9.722  -8.234  -34.440 1.00 93.83  ? 41  ASN A N   1 
ATOM   4946 C CA  . ASN D 1 32  ? -11.167 -8.290  -34.613 1.00 95.11  ? 41  ASN A CA  1 
ATOM   4947 C C   . ASN D 1 32  ? -11.533 -9.528  -35.420 1.00 93.85  ? 41  ASN A C   1 
ATOM   4948 O O   . ASN D 1 32  ? -10.920 -9.800  -36.458 1.00 111.73 ? 41  ASN A O   1 
ATOM   4949 C CB  . ASN D 1 32  ? -11.689 -7.029  -35.304 1.00 95.18  ? 41  ASN A CB  1 
ATOM   4950 C CG  . ASN D 1 32  ? -13.202 -6.952  -35.302 1.00 117.66 ? 41  ASN A CG  1 
ATOM   4951 O OD1 . ASN D 1 32  ? -13.869 -7.643  -34.530 1.00 118.42 ? 41  ASN A OD1 1 
ATOM   4952 N ND2 . ASN D 1 32  ? -13.753 -6.109  -36.167 1.00 112.46 ? 41  ASN A ND2 1 
ATOM   4953 N N   . LEU D 1 33  ? -12.533 -10.270 -34.943 1.00 83.49  ? 42  LEU A N   1 
ATOM   4954 C CA  . LEU D 1 33  ? -12.951 -11.506 -35.591 1.00 84.78  ? 42  LEU A CA  1 
ATOM   4955 C C   . LEU D 1 33  ? -14.245 -11.370 -36.381 1.00 101.36 ? 42  LEU A C   1 
ATOM   4956 O O   . LEU D 1 33  ? -14.431 -12.093 -37.366 1.00 120.63 ? 42  LEU A O   1 
ATOM   4957 C CB  . LEU D 1 33  ? -13.110 -12.623 -34.554 1.00 77.74  ? 42  LEU A CB  1 
ATOM   4958 C CG  . LEU D 1 33  ? -11.825 -13.048 -33.838 1.00 70.81  ? 42  LEU A CG  1 
ATOM   4959 C CD1 . LEU D 1 33  ? -12.120 -14.081 -32.759 1.00 72.91  ? 42  LEU A CD1 1 
ATOM   4960 C CD2 . LEU D 1 33  ? -10.800 -13.567 -34.831 1.00 89.22  ? 42  LEU A CD2 1 
ATOM   4961 N N   . LEU D 1 34  ? -15.144 -10.477 -35.974 1.00 104.36 ? 43  LEU A N   1 
ATOM   4962 C CA  . LEU D 1 34  ? -16.359 -10.213 -36.731 1.00 107.66 ? 43  LEU A CA  1 
ATOM   4963 C C   . LEU D 1 34  ? -16.142 -9.062  -37.705 1.00 108.17 ? 43  LEU A C   1 
ATOM   4964 O O   . LEU D 1 34  ? -15.155 -8.326  -37.638 1.00 95.40  ? 43  LEU A O   1 
ATOM   4965 C CB  . LEU D 1 34  ? -17.532 -9.890  -35.807 1.00 104.16 ? 43  LEU A CB  1 
ATOM   4966 C CG  . LEU D 1 34  ? -18.081 -11.004 -34.922 1.00 129.30 ? 43  LEU A CG  1 
ATOM   4967 C CD1 . LEU D 1 34  ? -19.128 -10.439 -33.979 1.00 127.83 ? 43  LEU A CD1 1 
ATOM   4968 C CD2 . LEU D 1 34  ? -18.666 -12.113 -35.773 1.00 143.99 ? 43  LEU A CD2 1 
ATOM   4969 N N   . GLU D 1 35  ? -17.100 -8.900  -38.613 1.00 104.16 ? 44  GLU A N   1 
ATOM   4970 C CA  . GLU D 1 35  ? -16.997 -7.859  -39.620 1.00 121.64 ? 44  GLU A CA  1 
ATOM   4971 C C   . GLU D 1 35  ? -18.367 -7.595  -40.221 1.00 107.25 ? 44  GLU A C   1 
ATOM   4972 O O   . GLU D 1 35  ? -19.162 -8.521  -40.405 1.00 92.23  ? 44  GLU A O   1 
ATOM   4973 C CB  . GLU D 1 35  ? -16.004 -8.253  -40.709 1.00 137.00 ? 44  GLU A CB  1 
ATOM   4974 C CG  . GLU D 1 35  ? -15.777 -7.179  -41.727 1.00 139.71 ? 44  GLU A CG  1 
ATOM   4975 C CD  . GLU D 1 35  ? -14.760 -7.592  -42.745 1.00 138.77 ? 44  GLU A CD  1 
ATOM   4976 O OE1 . GLU D 1 35  ? -14.272 -8.737  -42.670 1.00 148.03 ? 44  GLU A OE1 1 
ATOM   4977 O OE2 . GLU D 1 35  ? -14.446 -6.782  -43.630 1.00 136.24 ? 44  GLU A OE2 1 
ATOM   4978 N N   . ASP D 1 36  ? -18.625 -6.327  -40.540 1.00 104.41 ? 45  ASP A N   1 
ATOM   4979 C CA  . ASP D 1 36  ? -19.917 -5.899  -41.057 1.00 115.69 ? 45  ASP A CA  1 
ATOM   4980 C C   . ASP D 1 36  ? -19.791 -5.226  -42.419 1.00 122.04 ? 45  ASP A C   1 
ATOM   4981 O O   . ASP D 1 36  ? -20.696 -4.492  -42.832 1.00 118.68 ? 45  ASP A O   1 
ATOM   4982 C CB  . ASP D 1 36  ? -20.589 -4.959  -40.057 1.00 130.53 ? 45  ASP A CB  1 
ATOM   4983 C CG  . ASP D 1 36  ? -21.022 -5.672  -38.788 1.00 144.89 ? 45  ASP A CG  1 
ATOM   4984 O OD1 . ASP D 1 36  ? -21.074 -6.922  -38.791 1.00 130.28 ? 45  ASP A OD1 1 
ATOM   4985 O OD2 . ASP D 1 36  ? -21.295 -4.984  -37.782 1.00 152.81 ? 45  ASP A OD2 1 
ATOM   4986 N N   . LYS D 1 37  ? -18.688 -5.482  -43.128 1.00 124.08 ? 46  LYS A N   1 
ATOM   4987 C CA  . LYS D 1 37  ? -18.452 -4.776  -44.418 1.00 147.87 ? 46  LYS A CA  1 
ATOM   4988 C C   . LYS D 1 37  ? -19.188 -5.471  -45.569 1.00 144.37 ? 46  LYS A C   1 
ATOM   4989 O O   . LYS D 1 37  ? -18.820 -6.617  -45.893 1.00 133.61 ? 46  LYS A O   1 
ATOM   4990 C CB  . LYS D 1 37  ? -16.950 -4.682  -44.706 1.00 141.79 ? 46  LYS A CB  1 
ATOM   4991 C CG  . LYS D 1 37  ? -16.153 -3.850  -43.710 1.00 132.52 ? 46  LYS A CG  1 
ATOM   4992 C CD  . LYS D 1 37  ? -14.711 -3.644  -44.118 1.00 158.71 ? 46  LYS A CD  1 
ATOM   4993 C CE  . LYS D 1 37  ? -13.899 -2.906  -43.075 1.00 151.98 ? 46  LYS A CE  1 
ATOM   4994 N NZ  . LYS D 1 37  ? -12.485 -2.752  -43.490 1.00 139.33 ? 46  LYS A NZ  1 
ATOM   4995 N N   . HIS D 1 38  ? -20.184 -4.802  -46.160 1.00 146.83 ? 47  HIS A N   1 
ATOM   4996 C CA  . HIS D 1 38  ? -20.893 -5.356  -47.349 1.00 139.62 ? 47  HIS A CA  1 
ATOM   4997 C C   . HIS D 1 38  ? -21.259 -4.179  -48.261 1.00 141.18 ? 47  HIS A C   1 
ATOM   4998 O O   . HIS D 1 38  ? -21.789 -3.167  -47.751 1.00 134.19 ? 47  HIS A O   1 
ATOM   4999 C CB  . HIS D 1 38  ? -22.096 -6.216  -46.937 1.00 136.62 ? 47  HIS A CB  1 
ATOM   5000 C CG  . HIS D 1 38  ? -23.117 -5.516  -46.104 1.00 153.92 ? 47  HIS A CG  1 
ATOM   5001 N ND1 . HIS D 1 38  ? -22.859 -5.030  -44.841 1.00 165.94 ? 47  HIS A ND1 1 
ATOM   5002 C CD2 . HIS D 1 38  ? -24.404 -5.242  -46.350 1.00 146.40 ? 47  HIS A CD2 1 
ATOM   5003 C CE1 . HIS D 1 38  ? -23.958 -4.472  -44.355 1.00 169.50 ? 47  HIS A CE1 1 
ATOM   5004 N NE2 . HIS D 1 38  ? -24.909 -4.590  -45.255 1.00 177.47 ? 47  HIS A NE2 1 
ATOM   5005 N N   . ASN D 1 39  ? -20.986 -4.298  -49.566 1.00 143.22 ? 48  ASN A N   1 
ATOM   5006 C CA  . ASN D 1 39  ? -21.226 -3.164  -50.503 1.00 131.82 ? 48  ASN A CA  1 
ATOM   5007 C C   . ASN D 1 39  ? -22.713 -2.798  -50.545 1.00 126.33 ? 48  ASN A C   1 
ATOM   5008 O O   . ASN D 1 39  ? -23.022 -1.593  -50.452 1.00 150.96 ? 48  ASN A O   1 
ATOM   5009 C CB  . ASN D 1 39  ? -20.704 -3.472  -51.908 1.00 124.80 ? 48  ASN A CB  1 
ATOM   5010 C CG  . ASN D 1 39  ? -21.423 -4.630  -52.564 1.00 134.07 ? 48  ASN A CG  1 
ATOM   5011 O OD1 . ASN D 1 39  ? -22.617 -4.828  -52.352 1.00 147.45 ? 48  ASN A OD1 1 
ATOM   5012 N ND2 . ASN D 1 39  ? -20.699 -5.409  -53.350 1.00 166.07 ? 48  ASN A ND2 1 
ATOM   5013 N N   . GLY D 1 40  ? -23.595 -3.791  -50.686 1.00 138.82 ? 49  GLY A N   1 
ATOM   5014 C CA  . GLY D 1 40  ? -25.043 -3.519  -50.782 1.00 135.81 ? 49  GLY A CA  1 
ATOM   5015 C C   . GLY D 1 40  ? -25.603 -3.809  -52.164 1.00 148.59 ? 49  GLY A C   1 
ATOM   5016 O O   . GLY D 1 40  ? -26.796 -4.149  -52.247 1.00 148.41 ? 49  GLY A O   1 
ATOM   5017 N N   . LYS D 1 41  ? -24.785 -3.676  -53.213 1.00 142.85 ? 50  LYS A N   1 
ATOM   5018 C CA  . LYS D 1 41  ? -25.238 -4.031  -54.585 1.00 128.28 ? 50  LYS A CA  1 
ATOM   5019 C C   . LYS D 1 41  ? -24.789 -5.473  -54.831 1.00 128.39 ? 50  LYS A C   1 
ATOM   5020 O O   . LYS D 1 41  ? -23.605 -5.763  -54.573 1.00 141.80 ? 50  LYS A O   1 
ATOM   5021 C CB  . LYS D 1 41  ? -24.648 -3.064  -55.615 1.00 127.04 ? 50  LYS A CB  1 
ATOM   5022 C CG  . LYS D 1 41  ? -25.039 -1.604  -55.431 1.00 143.46 ? 50  LYS A CG  1 
ATOM   5023 C CD  . LYS D 1 41  ? -24.392 -0.681  -56.440 1.00 141.51 ? 50  LYS A CD  1 
ATOM   5024 C CE  . LYS D 1 41  ? -22.880 -0.748  -56.416 1.00 149.05 ? 50  LYS A CE  1 
ATOM   5025 N NZ  . LYS D 1 41  ? -22.336 -0.398  -55.082 1.00 144.42 ? 50  LYS A NZ  1 
ATOM   5026 N N   . LEU D 1 42  ? -25.711 -6.392  -55.123 1.00 133.83 ? 51  LEU A N   1 
ATOM   5027 C CA  . LEU D 1 42  ? -25.323 -7.828  -55.218 1.00 129.71 ? 51  LEU A CA  1 
ATOM   5028 C C   . LEU D 1 42  ? -24.403 -8.018  -56.425 1.00 135.86 ? 51  LEU A C   1 
ATOM   5029 O O   . LEU D 1 42  ? -24.891 -7.867  -57.554 1.00 144.03 ? 51  LEU A O   1 
ATOM   5030 C CB  . LEU D 1 42  ? -26.585 -8.684  -55.326 1.00 106.43 ? 51  LEU A CB  1 
ATOM   5031 C CG  . LEU D 1 42  ? -27.492 -8.668  -54.100 1.00 76.63  ? 51  LEU A CG  1 
ATOM   5032 C CD1 . LEU D 1 42  ? -28.779 -9.429  -54.373 1.00 109.36 ? 51  LEU A CD1 1 
ATOM   5033 C CD2 . LEU D 1 42  ? -26.775 -9.258  -52.899 1.00 107.71 ? 51  LEU A CD2 1 
ATOM   5034 N N   . CYS D 1 43  ? -23.132 -8.351  -56.191 1.00 30.00  ? 52  CYS A N   1 
ATOM   5035 C CA  . CYS D 1 43  ? -22.160 -8.455  -57.312 1.00 30.00  ? 52  CYS A CA  1 
ATOM   5036 C C   . CYS D 1 43  ? -22.025 -9.904  -57.779 1.00 30.00  ? 52  CYS A C   1 
ATOM   5037 O O   . CYS D 1 43  ? -22.947 -10.699 -57.522 1.00 30.00  ? 52  CYS A O   1 
ATOM   5038 C CB  . CYS D 1 43  ? -20.791 -7.974  -56.854 1.00 30.00  ? 52  CYS A CB  1 
ATOM   5039 S SG  . CYS D 1 43  ? -19.541 -8.011  -58.165 1.00 30.00  ? 52  CYS A SG  1 
ATOM   5040 N N   . ASP D 1 44  ? -20.945 -10.218 -58.495 1.00 186.64 ? 53  ASP A N   1 
ATOM   5041 C CA  . ASP D 1 44  ? -20.771 -11.582 -59.057 1.00 183.58 ? 53  ASP A CA  1 
ATOM   5042 C C   . ASP D 1 44  ? -19.952 -12.426 -58.079 1.00 169.74 ? 53  ASP A C   1 
ATOM   5043 O O   . ASP D 1 44  ? -19.475 -11.864 -57.075 1.00 144.95 ? 53  ASP A O   1 
ATOM   5044 C CB  . ASP D 1 44  ? -20.114 -11.516 -60.435 1.00 30.00  ? 53  ASP A CB  1 
ATOM   5045 C CG  . ASP D 1 44  ? -20.565 -12.633 -61.356 1.00 30.00  ? 53  ASP A CG  1 
ATOM   5046 O OD1 . ASP D 1 44  ? -21.776 -12.712 -61.621 1.00 30.00  ? 53  ASP A OD1 1 
ATOM   5047 O OD2 . ASP D 1 44  ? -19.704 -13.413 -61.790 1.00 30.00  ? 53  ASP A OD2 1 
ATOM   5048 N N   . LEU D 1 45  ? -19.802 -13.723 -58.364 1.00 184.24 ? 54  LEU A N   1 
ATOM   5049 C CA  . LEU D 1 45  ? -18.972 -14.602 -57.500 1.00 190.00 ? 54  LEU A CA  1 
ATOM   5050 C C   . LEU D 1 45  ? -17.587 -15.120 -57.903 1.00 194.12 ? 54  LEU A C   1 
ATOM   5051 O O   . LEU D 1 45  ? -16.616 -14.836 -57.175 1.00 177.68 ? 54  LEU A O   1 
ATOM   5052 C CB  . LEU D 1 45  ? -19.722 -15.913 -57.244 1.00 30.00  ? 54  LEU A CB  1 
ATOM   5053 C CG  . LEU D 1 45  ? -19.116 -16.805 -56.162 1.00 30.00  ? 54  LEU A CG  1 
ATOM   5054 C CD1 . LEU D 1 45  ? -19.398 -16.245 -54.777 1.00 30.00  ? 54  LEU A CD1 1 
ATOM   5055 C CD2 . LEU D 1 45  ? -19.630 -18.231 -56.284 1.00 30.00  ? 54  LEU A CD2 1 
ATOM   5056 N N   . ASP D 1 46  ? -17.504 -15.837 -59.027 1.00 181.54 ? 55  ASP A N   1 
ATOM   5057 C CA  . ASP D 1 46  ? -16.203 -16.370 -59.508 1.00 170.84 ? 55  ASP A CA  1 
ATOM   5058 C C   . ASP D 1 46  ? -16.457 -16.268 -61.015 1.00 183.96 ? 55  ASP A C   1 
ATOM   5059 O O   . ASP D 1 46  ? -16.180 -17.267 -61.718 1.00 182.69 ? 55  ASP A O   1 
ATOM   5060 C CB  . ASP D 1 46  ? -15.676 -17.746 -59.091 1.00 170.72 ? 55  ASP A CB  1 
ATOM   5061 C CG  . ASP D 1 46  ? -14.229 -17.985 -59.486 1.00 183.99 ? 55  ASP A CG  1 
ATOM   5062 O OD1 . ASP D 1 46  ? -13.364 -17.207 -59.037 1.00 206.35 ? 55  ASP A OD1 1 
ATOM   5063 O OD2 . ASP D 1 46  ? -13.979 -18.947 -60.238 1.00 190.70 ? 55  ASP A OD2 1 
ATOM   5064 N N   . GLY D 1 47  a -16.971 -15.118 -61.477 1.00 177.98 ? 55  GLY A N   1 
ATOM   5065 C CA  . GLY D 1 47  a -17.256 -14.911 -62.910 1.00 178.66 ? 55  GLY A CA  1 
ATOM   5066 C C   . GLY D 1 47  a -18.473 -15.710 -63.339 1.00 161.38 ? 55  GLY A C   1 
ATOM   5067 O O   . GLY D 1 47  a -18.525 -16.114 -64.517 1.00 156.36 ? 55  GLY A O   1 
ATOM   5068 N N   . VAL D 1 48  ? -19.418 -15.933 -62.418 1.00 149.88 ? 56  VAL A N   1 
ATOM   5069 C CA  . VAL D 1 48  ? -20.610 -16.770 -62.735 1.00 163.70 ? 56  VAL A CA  1 
ATOM   5070 C C   . VAL D 1 48  ? -21.849 -15.980 -62.305 1.00 136.65 ? 56  VAL A C   1 
ATOM   5071 O O   . VAL D 1 48  ? -22.115 -15.908 -61.094 1.00 130.80 ? 56  VAL A O   1 
ATOM   5072 C CB  . VAL D 1 48  ? -20.519 -18.151 -62.064 1.00 181.52 ? 56  VAL A CB  1 
ATOM   5073 C CG1 . VAL D 1 48  ? -21.785 -18.964 -62.280 1.00 173.19 ? 56  VAL A CG1 1 
ATOM   5074 C CG2 . VAL D 1 48  ? -19.297 -18.921 -62.540 1.00 183.64 ? 56  VAL A CG2 1 
ATOM   5075 N N   . LYS D 1 49  ? -22.576 -15.421 -63.271 1.00 152.30 ? 57  LYS A N   1 
ATOM   5076 C CA  . LYS D 1 49  ? -23.765 -14.585 -62.959 1.00 148.28 ? 57  LYS A CA  1 
ATOM   5077 C C   . LYS D 1 49  ? -24.842 -15.435 -62.284 1.00 148.42 ? 57  LYS A C   1 
ATOM   5078 O O   . LYS D 1 49  ? -24.967 -16.620 -62.636 1.00 174.85 ? 57  LYS A O   1 
ATOM   5079 C CB  . LYS D 1 49  ? -24.275 -14.000 -64.278 1.00 148.61 ? 57  LYS A CB  1 
ATOM   5080 C CG  . LYS D 1 49  ? -25.516 -13.124 -64.171 1.00 149.47 ? 57  LYS A CG  1 
ATOM   5081 C CD  . LYS D 1 49  ? -25.969 -12.551 -65.496 1.00 135.91 ? 57  LYS A CD  1 
ATOM   5082 C CE  . LYS D 1 49  ? -27.204 -11.684 -65.372 1.00 134.48 ? 57  LYS A CE  1 
ATOM   5083 N NZ  . LYS D 1 49  ? -27.619 -11.130 -66.683 1.00 151.99 ? 57  LYS A NZ  1 
ATOM   5084 N N   . PRO D 1 50  ? -25.622 -14.884 -61.331 1.00 126.03 ? 58  PRO A N   1 
ATOM   5085 C CA  . PRO D 1 50  ? -26.705 -15.632 -60.700 1.00 122.23 ? 58  PRO A CA  1 
ATOM   5086 C C   . PRO D 1 50  ? -28.039 -15.585 -61.450 1.00 131.22 ? 58  PRO A C   1 
ATOM   5087 O O   . PRO D 1 50  ? -28.216 -14.709 -62.268 1.00 145.93 ? 58  PRO A O   1 
ATOM   5088 C CB  . PRO D 1 50  ? -26.900 -14.867 -59.391 1.00 121.06 ? 58  PRO A CB  1 
ATOM   5089 C CG  . PRO D 1 50  ? -26.566 -13.438 -59.745 1.00 127.01 ? 58  PRO A CG  1 
ATOM   5090 C CD  . PRO D 1 50  ? -25.456 -13.542 -60.769 1.00 129.51 ? 58  PRO A CD  1 
ATOM   5091 N N   . LEU D 1 51  ? -28.938 -16.520 -61.144 1.00 119.77 ? 59  LEU A N   1 
ATOM   5092 C CA  . LEU D 1 51  ? -30.282 -16.540 -61.767 1.00 119.56 ? 59  LEU A CA  1 
ATOM   5093 C C   . LEU D 1 51  ? -31.119 -15.527 -60.995 1.00 114.32 ? 59  LEU A C   1 
ATOM   5094 O O   . LEU D 1 51  ? -31.883 -15.946 -60.112 1.00 122.11 ? 59  LEU A O   1 
ATOM   5095 C CB  . LEU D 1 51  ? -30.867 -17.945 -61.651 1.00 140.95 ? 59  LEU A CB  1 
ATOM   5096 C CG  . LEU D 1 51  ? -32.286 -18.101 -62.189 1.00 181.70 ? 59  LEU A CG  1 
ATOM   5097 C CD1 . LEU D 1 51  ? -32.330 -17.819 -63.680 1.00 160.83 ? 59  LEU A CD1 1 
ATOM   5098 C CD2 . LEU D 1 51  ? -32.830 -19.490 -61.892 1.00 184.19 ? 59  LEU A CD2 1 
ATOM   5099 N N   . ILE D 1 52  ? -30.940 -14.235 -61.280 1.00 132.74 ? 60  ILE A N   1 
ATOM   5100 C CA  . ILE D 1 52  ? -31.677 -13.198 -60.519 1.00 132.92 ? 60  ILE A CA  1 
ATOM   5101 C C   . ILE D 1 52  ? -33.086 -13.463 -60.997 1.00 142.00 ? 60  ILE A C   1 
ATOM   5102 O O   . ILE D 1 52  ? -33.358 -13.209 -62.188 1.00 156.23 ? 60  ILE A O   1 
ATOM   5103 C CB  . ILE D 1 52  ? -31.053 -11.791 -60.743 1.00 142.25 ? 60  ILE A CB  1 
ATOM   5104 C CG1 . ILE D 1 52  ? -29.527 -11.812 -60.626 1.00 140.70 ? 60  ILE A CG1 1 
ATOM   5105 C CG2 . ILE D 1 52  ? -31.673 -10.763 -59.808 1.00 137.71 ? 60  ILE A CG2 1 
ATOM   5106 C CD1 . ILE D 1 52  ? -28.876 -10.464 -60.827 1.00 146.00 ? 60  ILE A CD1 1 
ATOM   5107 N N   . LEU D 1 53  ? -33.932 -14.029 -60.135 1.00 132.78 ? 61  LEU A N   1 
ATOM   5108 C CA  . LEU D 1 53  ? -35.299 -14.416 -60.571 1.00 142.12 ? 61  LEU A CA  1 
ATOM   5109 C C   . LEU D 1 53  ? -36.221 -13.198 -60.519 1.00 140.88 ? 61  LEU A C   1 
ATOM   5110 O O   . LEU D 1 53  ? -37.447 -13.396 -60.437 1.00 118.18 ? 61  LEU A O   1 
ATOM   5111 C CB  . LEU D 1 53  ? -35.819 -15.528 -59.658 1.00 140.29 ? 61  LEU A CB  1 
ATOM   5112 C CG  . LEU D 1 53  ? -35.540 -16.950 -60.137 1.00 120.90 ? 61  LEU A CG  1 
ATOM   5113 C CD1 . LEU D 1 53  ? -36.391 -17.948 -59.371 1.00 123.12 ? 61  LEU A CD1 1 
ATOM   5114 C CD2 . LEU D 1 53  ? -35.800 -17.069 -61.630 1.00 133.58 ? 61  LEU A CD2 1 
ATOM   5115 N N   . ARG D 1 54  ? -35.654 -11.993 -60.566 1.00 144.48 ? 62  ARG A N   1 
ATOM   5116 C CA  . ARG D 1 54  ? -36.512 -10.784 -60.600 1.00 135.23 ? 62  ARG A CA  1 
ATOM   5117 C C   . ARG D 1 54  ? -37.680 -11.004 -59.641 1.00 143.48 ? 62  ARG A C   1 
ATOM   5118 O O   . ARG D 1 54  ? -37.425 -11.307 -58.465 1.00 145.60 ? 62  ARG A O   1 
ATOM   5119 C CB  . ARG D 1 54  ? -37.031 -10.520 -62.014 1.00 145.66 ? 62  ARG A CB  1 
ATOM   5120 C CG  . ARG D 1 54  ? -35.945 -10.113 -62.998 1.00 170.59 ? 62  ARG A CG  1 
ATOM   5121 C CD  . ARG D 1 54  ? -36.503 -9.724  -64.352 1.00 190.84 ? 62  ARG A CD  1 
ATOM   5122 N NE  . ARG D 1 54  ? -35.444 -9.343  -65.274 1.00 201.06 ? 62  ARG A NE  1 
ATOM   5123 C CZ  . ARG D 1 54  ? -35.641 -8.970  -66.532 1.00 215.76 ? 62  ARG A CZ  1 
ATOM   5124 N NH1 . ARG D 1 54  ? -36.857 -9.000  -67.048 1.00 225.05 ? 62  ARG A NH1 1 
ATOM   5125 N NH2 . ARG D 1 54  ? -34.621 -8.570  -67.271 1.00 212.38 ? 62  ARG A NH2 1 
ATOM   5126 N N   . ASP D 1 55  ? -38.911 -10.892 -60.139 1.00 148.97 ? 63  ASP A N   1 
ATOM   5127 C CA  . ASP D 1 55  ? -40.092 -11.005 -59.244 1.00 167.11 ? 63  ASP A CA  1 
ATOM   5128 C C   . ASP D 1 55  ? -40.670 -12.398 -58.987 1.00 168.27 ? 63  ASP A C   1 
ATOM   5129 O O   . ASP D 1 55  ? -41.189 -12.623 -57.878 1.00 162.30 ? 63  ASP A O   1 
ATOM   5130 C CB  . ASP D 1 55  ? -41.281 -10.239 -59.824 1.00 182.15 ? 63  ASP A CB  1 
ATOM   5131 C CG  . ASP D 1 55  ? -40.969 -8.776  -60.084 1.00 181.34 ? 63  ASP A CG  1 
ATOM   5132 O OD1 . ASP D 1 55  ? -39.828 -8.362  -59.798 1.00 183.81 ? 63  ASP A OD1 1 
ATOM   5133 O OD2 . ASP D 1 55  ? -41.866 -8.064  -60.572 1.00 199.36 ? 63  ASP A OD2 1 
ATOM   5134 N N   . CYS D 1 56  ? -40.644 -13.224 -60.021 1.00 158.15 ? 64  CYS A N   1 
ATOM   5135 C CA  . CYS D 1 56  ? -41.253 -14.577 -59.998 1.00 172.94 ? 64  CYS A CA  1 
ATOM   5136 C C   . CYS D 1 56  ? -40.551 -15.432 -58.942 1.00 167.19 ? 64  CYS A C   1 
ATOM   5137 O O   . CYS D 1 56  ? -39.305 -15.486 -58.933 1.00 173.29 ? 64  CYS A O   1 
ATOM   5138 C CB  . CYS D 1 56  ? -41.148 -15.053 -61.434 1.00 173.09 ? 64  CYS A CB  1 
ATOM   5139 S SG  . CYS D 1 56  ? -42.167 -13.878 -62.360 1.00 182.46 ? 64  CYS A SG  1 
ATOM   5140 N N   . SER D 1 57  ? -41.362 -16.081 -58.101 1.00 165.02 ? 65  SER A N   1 
ATOM   5141 C CA  . SER D 1 57  ? -40.819 -16.954 -57.033 1.00 160.15 ? 65  SER A CA  1 
ATOM   5142 C C   . SER D 1 57  ? -40.092 -18.162 -57.620 1.00 150.77 ? 65  SER A C   1 
ATOM   5143 O O   . SER D 1 57  ? -40.289 -18.459 -58.816 1.00 146.90 ? 65  SER A O   1 
ATOM   5144 C CB  . SER D 1 57  ? -41.922 -17.410 -56.115 1.00 140.05 ? 65  SER A CB  1 
ATOM   5145 O OG  . SER D 1 57  ? -42.873 -18.192 -56.823 1.00 142.11 ? 65  SER A OG  1 
ATOM   5146 N N   . VAL D 1 58  ? -39.303 -18.841 -56.793 1.00 143.24 ? 66  VAL A N   1 
ATOM   5147 C CA  . VAL D 1 58  ? -38.555 -20.010 -57.247 1.00 141.53 ? 66  VAL A CA  1 
ATOM   5148 C C   . VAL D 1 58  ? -39.517 -21.060 -57.787 1.00 125.84 ? 66  VAL A C   1 
ATOM   5149 O O   . VAL D 1 58  ? -39.268 -21.684 -58.827 1.00 134.01 ? 66  VAL A O   1 
ATOM   5150 C CB  . VAL D 1 58  ? -37.665 -20.544 -56.111 1.00 149.52 ? 66  VAL A CB  1 
ATOM   5151 C CG1 . VAL D 1 58  ? -38.513 -21.020 -54.946 1.00 168.13 ? 66  VAL A CG1 1 
ATOM   5152 C CG2 . VAL D 1 58  ? -36.781 -21.670 -56.623 1.00 170.56 ? 66  VAL A CG2 1 
ATOM   5153 N N   . ALA D 1 59  ? -40.649 -21.245 -57.103 1.00 111.10 ? 67  ALA A N   1 
ATOM   5154 C CA  . ALA D 1 59  ? -41.689 -22.138 -57.601 1.00 128.60 ? 67  ALA A CA  1 
ATOM   5155 C C   . ALA D 1 59  ? -42.127 -21.793 -59.019 1.00 136.46 ? 67  ALA A C   1 
ATOM   5156 O O   . ALA D 1 59  ? -42.212 -22.670 -59.884 1.00 142.07 ? 67  ALA A O   1 
ATOM   5157 C CB  . ALA D 1 59  ? -42.880 -22.098 -56.642 1.00 140.38 ? 67  ALA A CB  1 
ATOM   5158 N N   . GLY D 1 60  ? -42.389 -20.509 -59.278 1.00 134.73 ? 68  GLY A N   1 
ATOM   5159 C CA  . GLY D 1 60  ? -42.806 -20.101 -60.612 1.00 129.21 ? 68  GLY A CA  1 
ATOM   5160 C C   . GLY D 1 60  ? -41.792 -20.463 -61.679 1.00 119.16 ? 68  GLY A C   1 
ATOM   5161 O O   . GLY D 1 60  ? -42.143 -21.014 -62.725 1.00 142.77 ? 68  GLY A O   1 
ATOM   5162 N N   . TRP D 1 61  ? -40.518 -20.155 -61.429 1.00 93.99  ? 69  TRP A N   1 
ATOM   5163 C CA  . TRP D 1 61  ? -39.459 -20.533 -62.360 1.00 98.78  ? 69  TRP A CA  1 
ATOM   5164 C C   . TRP D 1 61  ? -39.469 -22.034 -62.622 1.00 114.32 ? 69  TRP A C   1 
ATOM   5165 O O   . TRP D 1 61  ? -39.350 -22.480 -63.769 1.00 128.68 ? 69  TRP A O   1 
ATOM   5166 C CB  . TRP D 1 61  ? -38.104 -20.089 -61.810 1.00 111.87 ? 69  TRP A CB  1 
ATOM   5167 C CG  . TRP D 1 61  ? -36.937 -20.761 -62.459 1.00 145.88 ? 69  TRP A CG  1 
ATOM   5168 C CD1 . TRP D 1 61  ? -36.632 -20.779 -63.789 1.00 179.07 ? 69  TRP A CD1 1 
ATOM   5169 C CD2 . TRP D 1 61  ? -35.918 -21.520 -61.802 1.00 153.27 ? 69  TRP A CD2 1 
ATOM   5170 N NE1 . TRP D 1 61  ? -35.482 -21.502 -64.000 1.00 200.60 ? 69  TRP A NE1 1 
ATOM   5171 C CE2 . TRP D 1 61  ? -35.024 -21.968 -62.795 1.00 182.68 ? 69  TRP A CE2 1 
ATOM   5172 C CE3 . TRP D 1 61  ? -35.673 -21.865 -60.469 1.00 138.59 ? 69  TRP A CE3 1 
ATOM   5173 C CZ2 . TRP D 1 61  ? -33.905 -22.742 -62.496 1.00 184.39 ? 69  TRP A CZ2 1 
ATOM   5174 C CZ3 . TRP D 1 61  ? -34.563 -22.632 -60.175 1.00 162.66 ? 69  TRP A CZ3 1 
ATOM   5175 C CH2 . TRP D 1 61  ? -33.692 -23.062 -61.184 1.00 179.42 ? 69  TRP A CH2 1 
ATOM   5176 N N   . LEU D 1 62  ? -39.626 -22.830 -61.564 1.00 114.46 ? 70  LEU A N   1 
ATOM   5177 C CA  . LEU D 1 62  ? -39.676 -24.279 -61.722 1.00 105.64 ? 70  LEU A CA  1 
ATOM   5178 C C   . LEU D 1 62  ? -40.989 -24.719 -62.358 1.00 110.95 ? 70  LEU A C   1 
ATOM   5179 O O   . LEU D 1 62  ? -40.995 -25.490 -63.324 1.00 104.35 ? 70  LEU A O   1 
ATOM   5180 C CB  . LEU D 1 62  ? -39.485 -24.959 -60.369 1.00 100.59 ? 70  LEU A CB  1 
ATOM   5181 C CG  . LEU D 1 62  ? -38.092 -24.833 -59.763 1.00 114.26 ? 70  LEU A CG  1 
ATOM   5182 C CD1 . LEU D 1 62  ? -38.007 -25.648 -58.488 1.00 126.78 ? 70  LEU A CD1 1 
ATOM   5183 C CD2 . LEU D 1 62  ? -37.041 -25.281 -60.767 1.00 142.40 ? 70  LEU A CD2 1 
ATOM   5184 N N   . LEU D 1 63  ? -42.114 -24.238 -61.824 1.00 113.40 ? 71  LEU A N   1 
ATOM   5185 C CA  . LEU D 1 63  ? -43.435 -24.624 -62.308 1.00 110.85 ? 71  LEU A CA  1 
ATOM   5186 C C   . LEU D 1 63  ? -43.772 -24.022 -63.664 1.00 117.01 ? 71  LEU A C   1 
ATOM   5187 O O   . LEU D 1 63  ? -44.836 -24.336 -64.208 1.00 129.22 ? 71  LEU A O   1 
ATOM   5188 C CB  . LEU D 1 63  ? -44.503 -24.226 -61.288 1.00 111.34 ? 71  LEU A CB  1 
ATOM   5189 C CG  . LEU D 1 63  ? -44.458 -24.991 -59.964 1.00 115.77 ? 71  LEU A CG  1 
ATOM   5190 C CD1 . LEU D 1 63  ? -45.607 -24.591 -59.048 1.00 145.13 ? 71  LEU A CD1 1 
ATOM   5191 C CD2 . LEU D 1 63  ? -44.465 -26.489 -60.216 1.00 117.30 ? 71  LEU A CD2 1 
ATOM   5192 N N   . GLY D 1 64  ? -42.908 -23.174 -64.216 1.00 122.19 ? 72  GLY A N   1 
ATOM   5193 C CA  . GLY D 1 64  ? -43.146 -22.593 -65.522 1.00 137.91 ? 72  GLY A CA  1 
ATOM   5194 C C   . GLY D 1 64  ? -44.313 -21.629 -65.556 1.00 140.57 ? 72  GLY A C   1 
ATOM   5195 O O   . GLY D 1 64  ? -45.261 -21.825 -66.324 1.00 129.22 ? 72  GLY A O   1 
ATOM   5196 N N   . ASN D 1 65  ? -44.255 -20.588 -64.723 1.00 141.98 ? 73  ASN A N   1 
ATOM   5197 C CA  . ASN D 1 65  ? -45.276 -19.551 -64.751 1.00 139.50 ? 73  ASN A CA  1 
ATOM   5198 C C   . ASN D 1 65  ? -45.186 -18.772 -66.062 1.00 143.92 ? 73  ASN A C   1 
ATOM   5199 O O   . ASN D 1 65  ? -44.084 -18.469 -66.530 1.00 166.00 ? 73  ASN A O   1 
ATOM   5200 C CB  . ASN D 1 65  ? -45.127 -18.600 -63.554 1.00 154.16 ? 73  ASN A CB  1 
ATOM   5201 C CG  . ASN D 1 65  ? -43.771 -17.901 -63.510 1.00 183.82 ? 73  ASN A CG  1 
ATOM   5202 O OD1 . ASN D 1 65  ? -42.735 -18.504 -63.785 1.00 227.18 ? 73  ASN A OD1 1 
ATOM   5203 N ND2 . ASN D 1 65  ? -43.779 -16.617 -63.157 1.00 208.31 ? 73  ASN A ND2 1 
ATOM   5204 N N   . PRO D 1 66  ? -46.324 -18.442 -66.681 1.00 140.40 ? 74  PRO A N   1 
ATOM   5205 C CA  . PRO D 1 66  ? -46.265 -17.770 -67.994 1.00 147.29 ? 74  PRO A CA  1 
ATOM   5206 C C   . PRO D 1 66  ? -45.589 -16.411 -67.934 1.00 164.48 ? 74  PRO A C   1 
ATOM   5207 O O   . PRO D 1 66  ? -44.711 -16.122 -68.757 1.00 170.56 ? 74  PRO A O   1 
ATOM   5208 C CB  . PRO D 1 66  ? -47.743 -17.675 -68.399 1.00 179.76 ? 74  PRO A CB  1 
ATOM   5209 C CG  . PRO D 1 66  ? -48.489 -17.729 -67.113 1.00 198.59 ? 74  PRO A CG  1 
ATOM   5210 C CD  . PRO D 1 66  ? -47.708 -18.649 -66.226 1.00 171.78 ? 74  PRO A CD  1 
ATOM   5211 N N   . MET D 1 67  ? -45.936 -15.612 -66.930 1.00 163.56 ? 75  MET A N   1 
ATOM   5212 C CA  . MET D 1 67  ? -45.181 -14.350 -66.761 1.00 151.57 ? 75  MET A CA  1 
ATOM   5213 C C   . MET D 1 67  ? -43.808 -14.774 -66.236 1.00 151.66 ? 75  MET A C   1 
ATOM   5214 O O   . MET D 1 67  ? -43.736 -15.833 -65.597 1.00 160.17 ? 75  MET A O   1 
ATOM   5215 C CB  . MET D 1 67  ? -45.867 -13.421 -65.757 1.00 141.97 ? 75  MET A CB  1 
ATOM   5216 C CG  . MET D 1 67  ? -47.093 -12.730 -66.317 1.00 134.43 ? 75  MET A CG  1 
ATOM   5217 S SD  . MET D 1 67  ? -46.707 -11.620 -67.694 1.00 176.00 ? 75  MET A SD  1 
ATOM   5218 C CE  . MET D 1 67  ? -45.208 -10.847 -67.090 1.00 140.38 ? 75  MET A CE  1 
ATOM   5219 N N   . CYS D 1 68  ? -42.752 -14.025 -66.545 1.00 169.16 ? 76  CYS A N   1 
ATOM   5220 C CA  . CYS D 1 68  ? -41.387 -14.453 -66.137 1.00 182.69 ? 76  CYS A CA  1 
ATOM   5221 C C   . CYS D 1 68  ? -41.077 -15.811 -66.770 1.00 168.54 ? 76  CYS A C   1 
ATOM   5222 O O   . CYS D 1 68  ? -40.685 -16.732 -66.031 1.00 156.99 ? 76  CYS A O   1 
ATOM   5223 C CB  . CYS D 1 68  ? -41.254 -14.540 -64.622 1.00 171.31 ? 76  CYS A CB  1 
ATOM   5224 S SG  . CYS D 1 68  ? -41.167 -12.921 -63.815 1.00 166.26 ? 76  CYS A SG  1 
ATOM   5225 N N   . ASP D 1 69  ? -41.247 -15.919 -68.088 1.00 160.15 ? 77  ASP A N   1 
ATOM   5226 C CA  . ASP D 1 69  ? -40.890 -17.166 -68.809 1.00 158.15 ? 77  ASP A CA  1 
ATOM   5227 C C   . ASP D 1 69  ? -39.484 -17.000 -69.386 1.00 159.71 ? 77  ASP A C   1 
ATOM   5228 O O   . ASP D 1 69  ? -38.892 -18.007 -69.795 1.00 167.03 ? 77  ASP A O   1 
ATOM   5229 C CB  . ASP D 1 69  ? -41.889 -17.448 -69.929 1.00 161.04 ? 77  ASP A CB  1 
ATOM   5230 C CG  . ASP D 1 69  ? -42.192 -16.221 -70.771 1.00 153.65 ? 77  ASP A CG  1 
ATOM   5231 O OD1 . ASP D 1 69  ? -41.667 -15.140 -70.444 1.00 150.67 ? 77  ASP A OD1 1 
ATOM   5232 O OD2 . ASP D 1 69  ? -42.946 -16.357 -71.751 1.00 141.47 ? 77  ASP A OD2 1 
ATOM   5233 N N   . GLU D 1 70  ? -38.990 -15.761 -69.430 1.00 147.27 ? 78  GLU A N   1 
ATOM   5234 C CA  . GLU D 1 70  ? -37.650 -15.470 -70.002 1.00 143.70 ? 78  GLU A CA  1 
ATOM   5235 C C   . GLU D 1 70  ? -36.601 -16.405 -69.403 1.00 142.32 ? 78  GLU A C   1 
ATOM   5236 O O   . GLU D 1 70  ? -35.754 -16.898 -70.164 1.00 150.08 ? 78  GLU A O   1 
ATOM   5237 C CB  . GLU D 1 70  ? -37.277 -14.023 -69.694 1.00 162.61 ? 78  GLU A CB  1 
ATOM   5238 C CG  . GLU D 1 70  ? -37.665 -13.594 -68.290 1.00 187.24 ? 78  GLU A CG  1 
ATOM   5239 C CD  . GLU D 1 70  ? -37.223 -12.196 -67.895 1.00 211.52 ? 78  GLU A CD  1 
ATOM   5240 O OE1 . GLU D 1 70  ? -36.550 -11.537 -68.710 1.00 202.90 ? 78  GLU A OE1 1 
ATOM   5241 O OE2 . GLU D 1 70  ? -37.563 -11.768 -66.777 1.00 219.42 ? 78  GLU A OE2 1 
ATOM   5242 N N   . PHE D 1 71  ? -36.699 -16.689 -68.100 1.00 143.03 ? 79  PHE A N   1 
ATOM   5243 C CA  . PHE D 1 71  ? -35.732 -17.596 -67.426 1.00 132.87 ? 79  PHE A CA  1 
ATOM   5244 C C   . PHE D 1 71  ? -36.164 -19.054 -67.616 1.00 147.24 ? 79  PHE A C   1 
ATOM   5245 O O   . PHE D 1 71  ? -36.921 -19.563 -66.766 1.00 141.66 ? 79  PHE A O   1 
ATOM   5246 C CB  . PHE D 1 71  ? -35.631 -17.261 -65.936 1.00 124.85 ? 79  PHE A CB  1 
ATOM   5247 C CG  . PHE D 1 71  ? -35.409 -15.803 -65.624 1.00 147.24 ? 79  PHE A CG  1 
ATOM   5248 C CD1 . PHE D 1 71  ? -34.307 -15.129 -66.124 1.00 175.84 ? 79  PHE A CD1 1 
ATOM   5249 C CD2 . PHE D 1 71  ? -36.300 -15.105 -64.825 1.00 142.51 ? 79  PHE A CD2 1 
ATOM   5250 C CE1 . PHE D 1 71  ? -34.104 -13.788 -65.835 1.00 168.97 ? 79  PHE A CE1 1 
ATOM   5251 C CE2 . PHE D 1 71  ? -36.095 -13.766 -64.535 1.00 141.94 ? 79  PHE A CE2 1 
ATOM   5252 C CZ  . PHE D 1 71  ? -34.998 -13.110 -65.041 1.00 154.01 ? 79  PHE A CZ  1 
ATOM   5253 N N   . ILE D 1 72  ? -35.778 -19.647 -68.746 1.00 142.90 ? 80  ILE A N   1 
ATOM   5254 C CA  . ILE D 1 72  ? -36.126 -21.068 -69.024 1.00 134.22 ? 80  ILE A CA  1 
ATOM   5255 C C   . ILE D 1 72  ? -34.827 -21.789 -69.381 1.00 131.47 ? 80  ILE A C   1 
ATOM   5256 O O   . ILE D 1 72  ? -34.407 -22.664 -68.603 1.00 149.59 ? 80  ILE A O   1 
ATOM   5257 C CB  . ILE D 1 72  ? -37.185 -21.179 -70.138 1.00 153.99 ? 80  ILE A CB  1 
ATOM   5258 C CG1 . ILE D 1 72  ? -38.600 -21.017 -69.582 1.00 160.75 ? 80  ILE A CG1 1 
ATOM   5259 C CG2 . ILE D 1 72  ? -37.058 -22.488 -70.901 1.00 166.20 ? 80  ILE A CG2 1 
ATOM   5260 C CD1 . ILE D 1 72  ? -39.683 -21.212 -70.614 1.00 171.76 ? 80  ILE A CD1 1 
ATOM   5261 N N   . ASN D 1 73  ? -34.203 -21.408 -70.495 1.00 114.59 ? 81  ASN A N   1 
ATOM   5262 C CA  . ASN D 1 73  ? -32.972 -22.113 -70.931 1.00 119.55 ? 81  ASN A CA  1 
ATOM   5263 C C   . ASN D 1 73  ? -31.778 -21.274 -70.480 1.00 127.54 ? 81  ASN A C   1 
ATOM   5264 O O   . ASN D 1 73  ? -30.796 -21.179 -71.234 1.00 144.98 ? 81  ASN A O   1 
ATOM   5265 C CB  . ASN D 1 73  ? -33.006 -22.432 -72.424 1.00 102.14 ? 81  ASN A CB  1 
ATOM   5266 C CG  . ASN D 1 73  ? -33.872 -23.635 -72.725 1.00 108.12 ? 81  ASN A CG  1 
ATOM   5267 O OD1 . ASN D 1 73  ? -33.687 -24.698 -72.138 1.00 122.44 ? 81  ASN A OD1 1 
ATOM   5268 N ND2 . ASN D 1 73  ? -34.828 -23.473 -73.624 1.00 108.95 ? 81  ASN A ND2 1 
ATOM   5269 N N   . VAL D 1 74  ? -31.842 -20.617 -69.323 1.00 115.41 ? 82  VAL A N   1 
ATOM   5270 C CA  . VAL D 1 74  ? -30.641 -19.805 -68.964 1.00 122.70 ? 82  VAL A CA  1 
ATOM   5271 C C   . VAL D 1 74  ? -29.525 -20.787 -68.584 1.00 124.08 ? 82  VAL A C   1 
ATOM   5272 O O   . VAL D 1 74  ? -29.835 -21.794 -67.921 1.00 142.44 ? 82  VAL A O   1 
ATOM   5273 C CB  . VAL D 1 74  ? -30.959 -18.774 -67.864 1.00 129.07 ? 82  VAL A CB  1 
ATOM   5274 C CG1 . VAL D 1 74  ? -29.809 -17.805 -67.633 1.00 167.56 ? 82  VAL A CG1 1 
ATOM   5275 C CG2 . VAL D 1 74  ? -32.241 -18.014 -68.164 1.00 130.97 ? 82  VAL A CG2 1 
ATOM   5276 N N   . PRO D 1 75  ? -28.237 -20.575 -68.964 1.00 122.43 ? 83  PRO A N   1 
ATOM   5277 C CA  . PRO D 1 75  ? -27.174 -21.536 -68.646 1.00 131.17 ? 83  PRO A CA  1 
ATOM   5278 C C   . PRO D 1 75  ? -26.917 -21.674 -67.137 1.00 140.24 ? 83  PRO A C   1 
ATOM   5279 O O   . PRO D 1 75  ? -27.636 -21.079 -66.361 1.00 129.46 ? 83  PRO A O   1 
ATOM   5280 C CB  . PRO D 1 75  ? -25.914 -20.954 -69.306 1.00 129.45 ? 83  PRO A CB  1 
ATOM   5281 C CG  . PRO D 1 75  ? -26.449 -20.030 -70.372 1.00 126.34 ? 83  PRO A CG  1 
ATOM   5282 C CD  . PRO D 1 75  ? -27.709 -19.456 -69.763 1.00 111.11 ? 83  PRO A CD  1 
ATOM   5283 N N   . GLU D 1 76  a -25.878 -22.424 -66.759 1.00 30.00  ? 83  GLU A N   1 
ATOM   5284 C CA  . GLU D 1 76  a -25.603 -22.676 -65.318 1.00 30.00  ? 83  GLU A CA  1 
ATOM   5285 C C   . GLU D 1 76  a -25.477 -21.390 -64.493 1.00 30.00  ? 83  GLU A C   1 
ATOM   5286 O O   . GLU D 1 76  a -24.835 -20.436 -64.978 1.00 30.00  ? 83  GLU A O   1 
ATOM   5287 C CB  . GLU D 1 76  a -24.375 -23.576 -65.162 1.00 30.00  ? 83  GLU A CB  1 
ATOM   5288 C CG  . GLU D 1 76  a -23.165 -23.091 -65.937 1.00 30.00  ? 83  GLU A CG  1 
ATOM   5289 C CD  . GLU D 1 76  a -21.954 -24.003 -65.840 1.00 30.00  ? 83  GLU A CD  1 
ATOM   5290 O OE1 . GLU D 1 76  a -21.480 -24.235 -64.711 1.00 30.00  ? 83  GLU A OE1 1 
ATOM   5291 O OE2 . GLU D 1 76  a -21.489 -24.478 -66.895 1.00 30.00  ? 83  GLU A OE2 1 
ATOM   5292 N N   . TRP D 1 77  ? -26.070 -21.369 -63.295 1.00 30.00  ? 84  TRP A N   1 
ATOM   5293 C CA  . TRP D 1 77  ? -25.908 -20.213 -62.373 1.00 30.00  ? 84  TRP A CA  1 
ATOM   5294 C C   . TRP D 1 77  ? -25.155 -20.549 -61.087 1.00 30.00  ? 84  TRP A C   1 
ATOM   5295 O O   . TRP D 1 77  ? -25.448 -21.612 -60.504 1.00 30.00  ? 84  TRP A O   1 
ATOM   5296 C CB  . TRP D 1 77  ? -27.297 -19.677 -62.002 1.00 30.00  ? 84  TRP A CB  1 
ATOM   5297 C CG  . TRP D 1 77  ? -28.175 -20.646 -61.272 1.00 30.00  ? 84  TRP A CG  1 
ATOM   5298 C CD1 . TRP D 1 77  ? -28.288 -20.789 -59.920 1.00 30.00  ? 84  TRP A CD1 1 
ATOM   5299 C CD2 . TRP D 1 77  ? -29.019 -21.657 -61.854 1.00 30.00  ? 84  TRP A CD2 1 
ATOM   5300 N NE1 . TRP D 1 77  ? -29.168 -21.793 -59.621 1.00 30.00  ? 84  TRP A NE1 1 
ATOM   5301 C CE2 . TRP D 1 77  ? -29.632 -22.346 -60.785 1.00 30.00  ? 84  TRP A CE2 1 
ATOM   5302 C CE3 . TRP D 1 77  ? -29.329 -22.036 -63.163 1.00 30.00  ? 84  TRP A CE3 1 
ATOM   5303 C CZ2 . TRP D 1 77  ? -30.534 -23.388 -60.991 1.00 30.00  ? 84  TRP A CZ2 1 
ATOM   5304 C CZ3 . TRP D 1 77  ? -30.223 -23.064 -63.366 1.00 30.00  ? 84  TRP A CZ3 1 
ATOM   5305 C CH2 . TRP D 1 77  ? -30.816 -23.728 -62.293 1.00 30.00  ? 84  TRP A CH2 1 
ATOM   5306 N N   . SER D 1 78  ? -24.219 -19.691 -60.671 1.00 30.00  ? 85  SER A N   1 
ATOM   5307 C CA  . SER D 1 78  ? -23.433 -19.951 -59.437 1.00 30.00  ? 85  SER A CA  1 
ATOM   5308 C C   . SER D 1 78  ? -24.450 -19.988 -58.293 1.00 30.00  ? 85  SER A C   1 
ATOM   5309 O O   . SER D 1 78  ? -24.324 -20.870 -57.424 1.00 30.00  ? 85  SER A O   1 
ATOM   5310 C CB  . SER D 1 78  ? -22.342 -18.961 -59.149 1.00 30.00  ? 85  SER A CB  1 
ATOM   5311 O OG  . SER D 1 78  ? -22.844 -17.635 -59.190 1.00 30.00  ? 85  SER A OG  1 
ATOM   5312 N N   . TYR D 1 79  ? -25.411 -19.058 -58.297 1.00 156.70 ? 86  TYR A N   1 
ATOM   5313 C CA  . TYR D 1 79  ? -26.462 -19.060 -57.244 1.00 149.10 ? 86  TYR A CA  1 
ATOM   5314 C C   . TYR D 1 79  ? -27.816 -18.616 -57.809 1.00 138.00 ? 86  TYR A C   1 
ATOM   5315 O O   . TYR D 1 79  ? -27.897 -18.307 -59.014 1.00 151.51 ? 86  TYR A O   1 
ATOM   5316 C CB  . TYR D 1 79  ? -26.046 -18.221 -56.028 1.00 121.00 ? 86  TYR A CB  1 
ATOM   5317 C CG  . TYR D 1 79  ? -25.658 -16.788 -56.293 1.00 110.14 ? 86  TYR A CG  1 
ATOM   5318 C CD1 . TYR D 1 79  ? -24.495 -16.470 -56.973 1.00 111.79 ? 86  TYR A CD1 1 
ATOM   5319 C CD2 . TYR D 1 79  ? -26.423 -15.741 -55.806 1.00 107.85 ? 86  TYR A CD2 1 
ATOM   5320 C CE1 . TYR D 1 79  ? -24.122 -15.156 -57.202 1.00 108.68 ? 86  TYR A CE1 1 
ATOM   5321 C CE2 . TYR D 1 79  ? -26.066 -14.421 -56.023 1.00 131.60 ? 86  TYR A CE2 1 
ATOM   5322 C CZ  . TYR D 1 79  ? -24.911 -14.126 -56.724 1.00 118.89 ? 86  TYR A CZ  1 
ATOM   5323 O OH  . TYR D 1 79  ? -24.548 -12.819 -56.945 1.00 103.99 ? 86  TYR A OH  1 
ATOM   5324 N N   . ILE D 1 80  ? -28.843 -18.595 -56.957 1.00 110.42 ? 87  ILE A N   1 
ATOM   5325 C CA  . ILE D 1 80  ? -30.231 -18.227 -57.368 1.00 126.82 ? 87  ILE A CA  1 
ATOM   5326 C C   . ILE D 1 80  ? -30.737 -17.100 -56.469 1.00 103.22 ? 87  ILE A C   1 
ATOM   5327 O O   . ILE D 1 80  ? -30.726 -17.279 -55.242 1.00 104.08 ? 87  ILE A O   1 
ATOM   5328 C CB  . ILE D 1 80  ? -31.161 -19.453 -57.322 1.00 117.82 ? 87  ILE A CB  1 
ATOM   5329 C CG1 . ILE D 1 80  ? -30.600 -20.613 -58.148 1.00 130.26 ? 87  ILE A CG1 1 
ATOM   5330 C CG2 . ILE D 1 80  ? -32.568 -19.079 -57.759 1.00 124.16 ? 87  ILE A CG2 1 
ATOM   5331 C CD1 . ILE D 1 80  ? -31.486 -21.834 -58.167 1.00 113.63 ? 87  ILE A CD1 1 
ATOM   5332 N N   . VAL D 1 81  ? -31.163 -15.988 -57.066 1.00 96.77  ? 88  VAL A N   1 
ATOM   5333 C CA  . VAL D 1 81  ? -31.630 -14.847 -56.285 1.00 86.31  ? 88  VAL A CA  1 
ATOM   5334 C C   . VAL D 1 81  ? -33.138 -14.728 -56.463 1.00 107.21 ? 88  VAL A C   1 
ATOM   5335 O O   . VAL D 1 81  ? -33.624 -14.564 -57.589 1.00 119.63 ? 88  VAL A O   1 
ATOM   5336 C CB  . VAL D 1 81  ? -30.944 -13.539 -56.706 1.00 93.18  ? 88  VAL A CB  1 
ATOM   5337 C CG1 . VAL D 1 81  ? -31.557 -12.366 -55.954 1.00 78.51  ? 88  VAL A CG1 1 
ATOM   5338 C CG2 . VAL D 1 81  ? -29.453 -13.612 -56.468 1.00 118.46 ? 88  VAL A CG2 1 
ATOM   5339 N N   . GLU D 1 82  ? -33.870 -14.785 -55.355 1.00 118.90 ? 89  GLU A N   1 
ATOM   5340 C CA  . GLU D 1 82  ? -35.318 -14.611 -55.339 1.00 106.46 ? 89  GLU A CA  1 
ATOM   5341 C C   . GLU D 1 82  ? -35.654 -13.358 -54.543 1.00 120.05 ? 89  GLU A C   1 
ATOM   5342 O O   . GLU D 1 82  ? -35.272 -13.245 -53.373 1.00 130.79 ? 89  GLU A O   1 
ATOM   5343 C CB  . GLU D 1 82  ? -36.012 -15.823 -54.717 1.00 98.80  ? 89  GLU A CB  1 
ATOM   5344 C CG  . GLU D 1 82  ? -37.537 -15.755 -54.750 1.00 139.68 ? 89  GLU A CG  1 
ATOM   5345 C CD  . GLU D 1 82  ? -38.198 -16.969 -54.118 1.00 175.10 ? 89  GLU A CD  1 
ATOM   5346 O OE1 . GLU D 1 82  ? -37.473 -17.836 -53.588 1.00 196.99 ? 89  GLU A OE1 1 
ATOM   5347 O OE2 . GLU D 1 82  ? -39.445 -17.049 -54.138 1.00 203.43 ? 89  GLU A OE2 1 
ATOM   5348 N N   . LYS D 1 83  ? -36.434 -12.460 -55.144 1.00 140.31 ? 90  LYS A N   1 
ATOM   5349 C CA  . LYS D 1 83  ? -36.892 -11.269 -54.389 1.00 138.55 ? 90  LYS A CA  1 
ATOM   5350 C C   . LYS D 1 83  ? -37.910 -11.728 -53.350 1.00 128.65 ? 90  LYS A C   1 
ATOM   5351 O O   . LYS D 1 83  ? -38.762 -12.562 -53.692 1.00 137.45 ? 90  LYS A O   1 
ATOM   5352 C CB  . LYS D 1 83  ? -37.559 -10.253 -55.316 1.00 145.56 ? 90  LYS A CB  1 
ATOM   5353 C CG  . LYS D 1 83  ? -36.614 -9.400  -56.150 1.00 157.22 ? 90  LYS A CG  1 
ATOM   5354 C CD  . LYS D 1 83  ? -37.346 -8.377  -56.992 1.00 143.48 ? 90  LYS A CD  1 
ATOM   5355 C CE  . LYS D 1 83  ? -36.440 -7.624  -57.942 1.00 150.48 ? 90  LYS A CE  1 
ATOM   5356 N NZ  . LYS D 1 83  ? -37.211 -6.726  -58.834 1.00 140.58 ? 90  LYS A NZ  1 
ATOM   5357 N N   . ALA D 1 84  ? -37.826 -11.191 -52.136 1.00 106.78 ? 91  ALA A N   1 
ATOM   5358 C CA  . ALA D 1 84  ? -38.822 -11.536 -51.101 1.00 107.86 ? 91  ALA A CA  1 
ATOM   5359 C C   . ALA D 1 84  ? -40.182 -11.001 -51.542 1.00 119.07 ? 91  ALA A C   1 
ATOM   5360 O O   . ALA D 1 84  ? -40.213 -10.098 -52.395 1.00 133.29 ? 91  ALA A O   1 
ATOM   5361 C CB  . ALA D 1 84  ? -38.410 -10.953 -49.779 1.00 118.53 ? 91  ALA A CB  1 
ATOM   5362 N N   . ASN D 1 85  ? -41.258 -11.543 -50.975 1.00 112.56 ? 92  ASN A N   1 
ATOM   5363 C CA  . ASN D 1 85  ? -42.621 -11.122 -51.383 1.00 130.21 ? 92  ASN A CA  1 
ATOM   5364 C C   . ASN D 1 85  ? -42.705 -11.154 -52.910 1.00 142.22 ? 92  ASN A C   1 
ATOM   5365 O O   . ASN D 1 85  ? -42.964 -10.095 -53.506 1.00 148.15 ? 92  ASN A O   1 
ATOM   5366 C CB  . ASN D 1 85  ? -42.972 -9.734  -50.848 1.00 145.40 ? 92  ASN A CB  1 
ATOM   5367 C CG  . ASN D 1 85  ? -42.752 -9.607  -49.356 1.00 159.82 ? 92  ASN A CG  1 
ATOM   5368 O OD1 . ASN D 1 85  ? -42.327 -10.558 -48.704 1.00 173.76 ? 92  ASN A OD1 1 
ATOM   5369 N ND2 . ASN D 1 85  ? -43.036 -8.437  -48.809 1.00 175.74 ? 92  ASN A ND2 1 
ATOM   5370 N N   . PRO D 1 86  ? -42.554 -12.310 -53.606 1.00 131.67 ? 93  PRO A N   1 
ATOM   5371 C CA  . PRO D 1 86  ? -42.744 -12.345 -55.062 1.00 109.86 ? 93  PRO A CA  1 
ATOM   5372 C C   . PRO D 1 86  ? -44.110 -11.745 -55.425 1.00 131.91 ? 93  PRO A C   1 
ATOM   5373 O O   . PRO D 1 86  ? -45.109 -12.297 -55.001 1.00 151.77 ? 93  PRO A O   1 
ATOM   5374 C CB  . PRO D 1 86  ? -42.714 -13.841 -55.395 1.00 134.73 ? 93  PRO A CB  1 
ATOM   5375 C CG  . PRO D 1 86  ? -41.825 -14.422 -54.324 1.00 150.17 ? 93  PRO A CG  1 
ATOM   5376 C CD  . PRO D 1 86  ? -42.192 -13.639 -53.082 1.00 148.35 ? 93  PRO A CD  1 
ATOM   5377 N N   . VAL D 1 87  ? -44.126 -10.649 -56.190 1.00 136.30 ? 94  VAL A N   1 
ATOM   5378 C CA  . VAL D 1 87  ? -45.414 -9.958  -56.504 1.00 132.44 ? 94  VAL A CA  1 
ATOM   5379 C C   . VAL D 1 87  ? -45.909 -10.374 -57.894 1.00 135.74 ? 94  VAL A C   1 
ATOM   5380 O O   . VAL D 1 87  ? -47.065 -10.832 -57.989 1.00 129.67 ? 94  VAL A O   1 
ATOM   5381 C CB  . VAL D 1 87  ? -45.262 -8.427  -56.408 1.00 138.71 ? 94  VAL A CB  1 
ATOM   5382 C CG1 . VAL D 1 87  ? -46.504 -7.701  -56.901 1.00 150.55 ? 94  VAL A CG1 1 
ATOM   5383 C CG2 . VAL D 1 87  ? -44.905 -7.981  -54.998 1.00 155.24 ? 94  VAL A CG2 1 
ATOM   5384 N N   . ASN D 1 88  ? -45.070 -10.234 -58.925 1.00 153.04 ? 95  ASN A N   1 
ATOM   5385 C CA  . ASN D 1 88  ? -45.520 -10.526 -60.314 1.00 151.20 ? 95  ASN A CA  1 
ATOM   5386 C C   . ASN D 1 88  ? -46.080 -11.949 -60.392 1.00 176.41 ? 95  ASN A C   1 
ATOM   5387 O O   . ASN D 1 88  ? -47.142 -12.128 -61.020 1.00 189.48 ? 95  ASN A O   1 
ATOM   5388 C CB  . ASN D 1 88  ? -44.395 -10.326 -61.333 1.00 131.62 ? 95  ASN A CB  1 
ATOM   5389 C CG  . ASN D 1 88  ? -44.783 -10.751 -62.734 1.00 130.37 ? 95  ASN A CG  1 
ATOM   5390 O OD1 . ASN D 1 88  ? -45.729 -10.219 -63.310 1.00 142.41 ? 95  ASN A OD1 1 
ATOM   5391 N ND2 . ASN D 1 88  ? -44.060 -11.710 -63.288 1.00 113.23 ? 95  ASN A ND2 1 
ATOM   5392 N N   . ASP D 1 89  ? -45.396 -12.918 -59.777 1.00 171.01 ? 96  ASP A N   1 
ATOM   5393 C CA  . ASP D 1 89  ? -45.836 -14.335 -59.878 1.00 166.63 ? 96  ASP A CA  1 
ATOM   5394 C C   . ASP D 1 89  ? -46.673 -14.707 -58.649 1.00 190.50 ? 96  ASP A C   1 
ATOM   5395 O O   . ASP D 1 89  ? -46.095 -14.788 -57.547 1.00 186.94 ? 96  ASP A O   1 
ATOM   5396 C CB  . ASP D 1 89  ? -44.636 -15.262 -60.085 1.00 144.44 ? 96  ASP A CB  1 
ATOM   5397 C CG  . ASP D 1 89  ? -45.010 -16.718 -60.294 1.00 158.54 ? 96  ASP A CG  1 
ATOM   5398 O OD1 . ASP D 1 89  ? -46.219 -17.019 -60.299 1.00 175.91 ? 96  ASP A OD1 1 
ATOM   5399 O OD2 . ASP D 1 89  ? -44.087 -17.533 -60.477 1.00 149.26 ? 96  ASP A OD2 1 
ATOM   5400 N N   . LEU D 1 90  a -47.980 -14.920 -58.838 1.00 30.00  ? 96  LEU A N   1 
ATOM   5401 C CA  . LEU D 1 90  a -48.864 -15.347 -57.720 1.00 30.00  ? 96  LEU A CA  1 
ATOM   5402 C C   . LEU D 1 90  a -48.817 -16.874 -57.627 1.00 30.00  ? 96  LEU A C   1 
ATOM   5403 O O   . LEU D 1 90  a -49.396 -17.420 -56.667 1.00 30.00  ? 96  LEU A O   1 
ATOM   5404 C CB  . LEU D 1 90  a -50.288 -14.853 -57.994 1.00 30.00  ? 96  LEU A CB  1 
ATOM   5405 C CG  . LEU D 1 90  a -50.468 -13.335 -58.005 1.00 30.00  ? 96  LEU A CG  1 
ATOM   5406 C CD1 . LEU D 1 90  a -49.445 -12.676 -58.916 1.00 30.00  ? 96  LEU A CD1 1 
ATOM   5407 C CD2 . LEU D 1 90  a -51.879 -12.957 -58.430 1.00 30.00  ? 96  LEU A CD2 1 
ATOM   5408 N N   . CYS D 1 91  ? -48.158 -17.526 -58.591 1.00 30.00  ? 97  CYS A N   1 
ATOM   5409 C CA  . CYS D 1 91  ? -48.014 -19.003 -58.594 1.00 30.00  ? 97  CYS A CA  1 
ATOM   5410 C C   . CYS D 1 91  ? -49.404 -19.627 -58.482 1.00 30.00  ? 97  CYS A C   1 
ATOM   5411 O O   . CYS D 1 91  ? -49.471 -20.837 -58.197 1.00 30.00  ? 97  CYS A O   1 
ATOM   5412 C CB  . CYS D 1 91  ? -47.161 -19.473 -57.424 1.00 30.00  ? 97  CYS A CB  1 
ATOM   5413 S SG  . CYS D 1 91  ? -45.701 -18.442 -57.136 1.00 30.00  ? 97  CYS A SG  1 
ATOM   5414 N N   . TYR D 1 92  ? -50.464 -18.819 -58.597 1.00 197.64 ? 98  TYR A N   1 
ATOM   5415 C CA  . TYR D 1 92  ? -51.862 -19.323 -58.498 1.00 186.27 ? 98  TYR A CA  1 
ATOM   5416 C C   . TYR D 1 92  ? -52.136 -19.800 -57.063 1.00 178.52 ? 98  TYR A C   1 
ATOM   5417 O O   . TYR D 1 92  ? -51.180 -19.965 -56.280 1.00 169.30 ? 98  TYR A O   1 
ATOM   5418 C CB  . TYR D 1 92  ? -52.123 -20.430 -59.527 1.00 174.02 ? 98  TYR A CB  1 
ATOM   5419 C CG  . TYR D 1 92  ? -51.776 -20.108 -60.962 1.00 184.23 ? 98  TYR A CG  1 
ATOM   5420 C CD1 . TYR D 1 92  ? -51.265 -18.875 -61.330 1.00 171.10 ? 98  TYR A CD1 1 
ATOM   5421 C CD2 . TYR D 1 92  ? -51.964 -21.048 -61.962 1.00 203.34 ? 98  TYR A CD2 1 
ATOM   5422 C CE1 . TYR D 1 92  ? -50.937 -18.587 -62.644 1.00 192.40 ? 98  TYR A CE1 1 
ATOM   5423 C CE2 . TYR D 1 92  ? -51.647 -20.775 -63.282 1.00 201.89 ? 98  TYR A CE2 1 
ATOM   5424 C CZ  . TYR D 1 92  ? -51.134 -19.539 -63.626 1.00 205.31 ? 98  TYR A CZ  1 
ATOM   5425 O OH  . TYR D 1 92  ? -50.819 -19.253 -64.932 1.00 232.57 ? 98  TYR A OH  1 
ATOM   5426 N N   . PRO D 1 93  ? -53.406 -20.004 -56.648 1.00 183.30 ? 99  PRO A N   1 
ATOM   5427 C CA  . PRO D 1 93  ? -53.696 -20.545 -55.314 1.00 177.37 ? 99  PRO A CA  1 
ATOM   5428 C C   . PRO D 1 93  ? -53.167 -21.981 -55.176 1.00 191.53 ? 99  PRO A C   1 
ATOM   5429 O O   . PRO D 1 93  ? -53.537 -22.809 -55.987 1.00 208.47 ? 99  PRO A O   1 
ATOM   5430 C CB  . PRO D 1 93  ? -55.230 -20.544 -55.240 1.00 181.24 ? 99  PRO A CB  1 
ATOM   5431 C CG  . PRO D 1 93  ? -55.661 -19.555 -56.302 1.00 181.91 ? 99  PRO A CG  1 
ATOM   5432 C CD  . PRO D 1 93  ? -54.623 -19.683 -57.397 1.00 190.83 ? 99  PRO A CD  1 
ATOM   5433 N N   . GLY D 1 94  ? -52.325 -22.239 -54.168 1.00 187.02 ? 100 GLY A N   1 
ATOM   5434 C CA  . GLY D 1 94  ? -51.761 -23.587 -53.963 1.00 180.94 ? 100 GLY A CA  1 
ATOM   5435 C C   . GLY D 1 94  ? -50.615 -23.608 -52.966 1.00 185.25 ? 100 GLY A C   1 
ATOM   5436 O O   . GLY D 1 94  ? -49.982 -22.552 -52.773 1.00 178.38 ? 100 GLY A O   1 
ATOM   5437 N N   . ASP D 1 95  ? -50.346 -24.773 -52.365 1.00 168.92 ? 101 ASP A N   1 
ATOM   5438 C CA  . ASP D 1 95  ? -49.272 -24.891 -51.341 1.00 168.16 ? 101 ASP A CA  1 
ATOM   5439 C C   . ASP D 1 95  ? -48.202 -25.881 -51.815 1.00 150.75 ? 101 ASP A C   1 
ATOM   5440 O O   . ASP D 1 95  ? -48.481 -27.093 -51.809 1.00 169.11 ? 101 ASP A O   1 
ATOM   5441 C CB  . ASP D 1 95  ? -49.829 -25.337 -49.985 1.00 178.35 ? 101 ASP A CB  1 
ATOM   5442 C CG  . ASP D 1 95  ? -50.654 -24.279 -49.272 1.00 180.86 ? 101 ASP A CG  1 
ATOM   5443 O OD1 . ASP D 1 95  ? -50.574 -23.101 -49.674 1.00 181.89 ? 101 ASP A OD1 1 
ATOM   5444 O OD2 . ASP D 1 95  ? -51.369 -24.642 -48.317 1.00 185.54 ? 101 ASP A OD2 1 
ATOM   5445 N N   . PHE D 1 96  ? -47.012 -25.389 -52.177 1.00 115.09 ? 102 PHE A N   1 
ATOM   5446 C CA  . PHE D 1 96  ? -45.907 -26.301 -52.574 1.00 116.99 ? 102 PHE A CA  1 
ATOM   5447 C C   . PHE D 1 96  ? -45.508 -27.164 -51.372 1.00 133.57 ? 102 PHE A C   1 
ATOM   5448 O O   . PHE D 1 96  ? -45.684 -26.708 -50.225 1.00 145.12 ? 102 PHE A O   1 
ATOM   5449 C CB  . PHE D 1 96  ? -44.718 -25.505 -53.115 1.00 122.26 ? 102 PHE A CB  1 
ATOM   5450 C CG  . PHE D 1 96  ? -43.814 -26.300 -54.020 1.00 151.39 ? 102 PHE A CG  1 
ATOM   5451 C CD1 . PHE D 1 96  ? -44.299 -26.853 -55.194 1.00 158.11 ? 102 PHE A CD1 1 
ATOM   5452 C CD2 . PHE D 1 96  ? -42.484 -26.506 -53.694 1.00 158.70 ? 102 PHE A CD2 1 
ATOM   5453 C CE1 . PHE D 1 96  ? -43.473 -27.589 -56.027 1.00 152.16 ? 102 PHE A CE1 1 
ATOM   5454 C CE2 . PHE D 1 96  ? -41.660 -27.242 -54.529 1.00 142.73 ? 102 PHE A CE2 1 
ATOM   5455 C CZ  . PHE D 1 96  ? -42.154 -27.780 -55.694 1.00 145.22 ? 102 PHE A CZ  1 
ATOM   5456 N N   . ASN D 1 97  ? -44.971 -28.361 -51.624 1.00 151.42 ? 103 ASN A N   1 
ATOM   5457 C CA  . ASN D 1 97  ? -44.656 -29.289 -50.506 1.00 141.34 ? 103 ASN A CA  1 
ATOM   5458 C C   . ASN D 1 97  ? -43.156 -29.592 -50.501 1.00 138.75 ? 103 ASN A C   1 
ATOM   5459 O O   . ASN D 1 97  ? -42.484 -29.243 -51.483 1.00 138.15 ? 103 ASN A O   1 
ATOM   5460 C CB  . ASN D 1 97  ? -45.517 -30.551 -50.571 1.00 155.10 ? 103 ASN A CB  1 
ATOM   5461 C CG  . ASN D 1 97  ? -46.962 -30.268 -50.221 1.00 173.46 ? 103 ASN A CG  1 
ATOM   5462 O OD1 . ASN D 1 97  ? -47.259 -29.287 -49.543 1.00 179.55 ? 103 ASN A OD1 1 
ATOM   5463 N ND2 . ASN D 1 97  ? -47.868 -31.107 -50.693 1.00 170.39 ? 103 ASN A ND2 1 
ATOM   5464 N N   . ASP D 1 98  ? -42.659 -30.207 -49.429 1.00 147.91 ? 104 ASP A N   1 
ATOM   5465 C CA  . ASP D 1 98  ? -41.232 -30.494 -49.309 1.00 173.82 ? 104 ASP A CA  1 
ATOM   5466 C C   . ASP D 1 98  ? -40.401 -29.344 -49.879 1.00 158.71 ? 104 ASP A C   1 
ATOM   5467 O O   . ASP D 1 98  ? -39.421 -29.540 -50.602 1.00 149.87 ? 104 ASP A O   1 
ATOM   5468 C CB  . ASP D 1 98  ? -40.878 -31.825 -49.984 1.00 181.64 ? 104 ASP A CB  1 
ATOM   5469 C CG  . ASP D 1 98  ? -40.781 -32.983 -49.000 1.00 209.25 ? 104 ASP A CG  1 
ATOM   5470 O OD1 . ASP D 1 98  ? -40.894 -32.735 -47.786 1.00 241.55 ? 104 ASP A OD1 1 
ATOM   5471 O OD2 . ASP D 1 98  ? -40.608 -34.140 -49.437 1.00 193.89 ? 104 ASP A OD2 1 
ATOM   5472 N N   . TYR D 1 99  ? -40.812 -28.119 -49.530 1.00 138.81 ? 105 TYR A N   1 
ATOM   5473 C CA  . TYR D 1 99  ? -40.258 -26.902 -50.146 1.00 117.51 ? 105 TYR A CA  1 
ATOM   5474 C C   . TYR D 1 99  ? -38.813 -26.588 -49.774 1.00 117.66 ? 105 TYR A C   1 
ATOM   5475 O O   . TYR D 1 99  ? -37.975 -26.429 -50.665 1.00 100.65 ? 105 TYR A O   1 
ATOM   5476 C CB  . TYR D 1 99  ? -41.065 -25.680 -49.754 1.00 121.07 ? 105 TYR A CB  1 
ATOM   5477 C CG  . TYR D 1 99  ? -40.465 -24.397 -50.284 1.00 164.85 ? 105 TYR A CG  1 
ATOM   5478 C CD1 . TYR D 1 99  ? -40.607 -24.036 -51.621 1.00 166.73 ? 105 TYR A CD1 1 
ATOM   5479 C CD2 . TYR D 1 99  ? -39.746 -23.552 -49.455 1.00 183.88 ? 105 TYR A CD2 1 
ATOM   5480 C CE1 . TYR D 1 99  ? -40.057 -22.867 -52.113 1.00 202.90 ? 105 TYR A CE1 1 
ATOM   5481 C CE2 . TYR D 1 99  ? -39.192 -22.381 -49.935 1.00 201.59 ? 105 TYR A CE2 1 
ATOM   5482 C CZ  . TYR D 1 99  ? -39.350 -22.042 -51.263 1.00 212.61 ? 105 TYR A CZ  1 
ATOM   5483 O OH  . TYR D 1 99  ? -38.794 -20.874 -51.737 1.00 222.78 ? 105 TYR A OH  1 
ATOM   5484 N N   . GLU D 1 100 ? -38.515 -26.463 -48.477 1.00 155.43 ? 106 GLU A N   1 
ATOM   5485 C CA  . GLU D 1 100 ? -37.162 -26.086 -48.089 1.00 164.01 ? 106 GLU A CA  1 
ATOM   5486 C C   . GLU D 1 100 ? -36.270 -27.302 -48.366 1.00 152.08 ? 106 GLU A C   1 
ATOM   5487 O O   . GLU D 1 100 ? -35.073 -27.142 -48.633 1.00 162.95 ? 106 GLU A O   1 
ATOM   5488 C CB  . GLU D 1 100 ? -37.097 -25.722 -46.597 1.00 196.21 ? 106 GLU A CB  1 
ATOM   5489 C CG  . GLU D 1 100 ? -35.704 -25.334 -46.112 1.00 201.32 ? 106 GLU A CG  1 
ATOM   5490 C CD  . GLU D 1 100 ? -35.194 -24.049 -46.745 1.00 199.25 ? 106 GLU A CD  1 
ATOM   5491 O OE1 . GLU D 1 100 ? -35.845 -22.997 -46.572 1.00 183.65 ? 106 GLU A OE1 1 
ATOM   5492 O OE2 . GLU D 1 100 ? -34.137 -24.091 -47.411 1.00 199.13 ? 106 GLU A OE2 1 
ATOM   5493 N N   . GLU D 1 101 ? -36.844 -28.509 -48.340 1.00 170.02 ? 107 GLU A N   1 
ATOM   5494 C CA  . GLU D 1 101 ? -36.108 -29.686 -48.787 1.00 167.48 ? 107 GLU A CA  1 
ATOM   5495 C C   . GLU D 1 101 ? -35.664 -29.515 -50.230 1.00 145.07 ? 107 GLU A C   1 
ATOM   5496 O O   . GLU D 1 101 ? -34.491 -29.726 -50.562 1.00 153.36 ? 107 GLU A O   1 
ATOM   5497 C CB  . GLU D 1 101 ? -36.968 -30.941 -48.612 1.00 193.03 ? 107 GLU A CB  1 
ATOM   5498 C CG  . GLU D 1 101 ? -36.265 -32.248 -48.984 1.00 230.40 ? 107 GLU A CG  1 
ATOM   5499 C CD  . GLU D 1 101 ? -37.120 -33.482 -48.757 1.00 236.58 ? 107 GLU A CD  1 
ATOM   5500 O OE1 . GLU D 1 101 ? -38.287 -33.336 -48.342 1.00 217.73 ? 107 GLU A OE1 1 
ATOM   5501 O OE2 . GLU D 1 101 ? -36.619 -34.601 -49.001 1.00 255.57 ? 107 GLU A OE2 1 
ATOM   5502 N N   . LEU D 1 102 ? -36.586 -29.092 -51.095 1.00 141.68 ? 108 LEU A N   1 
ATOM   5503 C CA  . LEU D 1 102 ? -36.227 -28.785 -52.473 1.00 131.75 ? 108 LEU A CA  1 
ATOM   5504 C C   . LEU D 1 102 ? -35.222 -27.642 -52.524 1.00 128.45 ? 108 LEU A C   1 
ATOM   5505 O O   . LEU D 1 102 ? -34.305 -27.651 -53.352 1.00 127.70 ? 108 LEU A O   1 
ATOM   5506 C CB  . LEU D 1 102 ? -37.477 -28.422 -53.267 1.00 125.02 ? 108 LEU A CB  1 
ATOM   5507 C CG  . LEU D 1 102 ? -37.242 -28.144 -54.744 1.00 119.21 ? 108 LEU A CG  1 
ATOM   5508 C CD1 . LEU D 1 102 ? -36.811 -29.414 -55.467 1.00 140.74 ? 108 LEU A CD1 1 
ATOM   5509 C CD2 . LEU D 1 102 ? -38.488 -27.549 -55.355 1.00 123.91 ? 108 LEU A CD2 1 
ATOM   5510 N N   . LYS D 1 103 ? -35.386 -26.641 -51.653 1.00 127.96 ? 109 LYS A N   1 
ATOM   5511 C CA  . LYS D 1 103 ? -34.466 -25.507 -51.654 1.00 129.24 ? 109 LYS A CA  1 
ATOM   5512 C C   . LYS D 1 103 ? -33.032 -25.962 -51.415 1.00 133.00 ? 109 LYS A C   1 
ATOM   5513 O O   . LYS D 1 103 ? -32.107 -25.507 -52.100 1.00 140.83 ? 109 LYS A O   1 
ATOM   5514 C CB  . LYS D 1 103 ? -34.894 -24.470 -50.612 1.00 141.59 ? 109 LYS A CB  1 
ATOM   5515 C CG  . LYS D 1 103 ? -36.296 -23.908 -50.815 1.00 148.82 ? 109 LYS A CG  1 
ATOM   5516 C CD  . LYS D 1 103 ? -36.428 -23.239 -52.176 1.00 148.94 ? 109 LYS A CD  1 
ATOM   5517 C CE  . LYS D 1 103 ? -35.631 -21.948 -52.249 1.00 140.19 ? 109 LYS A CE  1 
ATOM   5518 N NZ  . LYS D 1 103 ? -35.884 -21.203 -53.512 1.00 139.39 ? 109 LYS A NZ  1 
ATOM   5519 N N   . HIS D 1 104 ? -32.824 -26.869 -50.456 1.00 145.80 ? 110 HIS A N   1 
ATOM   5520 C CA  . HIS D 1 104 ? -31.480 -27.380 -50.211 1.00 142.43 ? 110 HIS A CA  1 
ATOM   5521 C C   . HIS D 1 104 ? -30.999 -28.301 -51.324 1.00 139.08 ? 110 HIS A C   1 
ATOM   5522 O O   . HIS D 1 104 ? -29.792 -28.392 -51.574 1.00 145.40 ? 110 HIS A O   1 
ATOM   5523 C CB  . HIS D 1 104 ? -31.444 -28.107 -48.870 1.00 155.54 ? 110 HIS A CB  1 
ATOM   5524 C CG  . HIS D 1 104 ? -30.076 -28.194 -48.270 1.00 167.02 ? 110 HIS A CG  1 
ATOM   5525 N ND1 . HIS D 1 104 ? -29.604 -27.275 -47.358 1.00 163.33 ? 110 HIS A ND1 1 
ATOM   5526 C CD2 . HIS D 1 104 ? -29.078 -29.090 -48.453 1.00 174.43 ? 110 HIS A CD2 1 
ATOM   5527 C CE1 . HIS D 1 104 ? -28.374 -27.602 -47.004 1.00 144.90 ? 110 HIS A CE1 1 
ATOM   5528 N NE2 . HIS D 1 104 ? -28.031 -28.699 -47.654 1.00 162.35 ? 110 HIS A NE2 1 
ATOM   5529 N N   . LEU D 1 105 ? -31.920 -29.004 -51.985 1.00 131.70 ? 111 LEU A N   1 
ATOM   5530 C CA  . LEU D 1 105 ? -31.570 -29.699 -53.217 1.00 138.06 ? 111 LEU A CA  1 
ATOM   5531 C C   . LEU D 1 105 ? -31.021 -28.716 -54.238 1.00 124.70 ? 111 LEU A C   1 
ATOM   5532 O O   . LEU D 1 105 ? -29.970 -28.950 -54.845 1.00 116.28 ? 111 LEU A O   1 
ATOM   5533 C CB  . LEU D 1 105 ? -32.794 -30.421 -53.770 1.00 128.85 ? 111 LEU A CB  1 
ATOM   5534 C CG  . LEU D 1 105 ? -33.352 -31.529 -52.883 1.00 151.62 ? 111 LEU A CG  1 
ATOM   5535 C CD1 . LEU D 1 105 ? -34.655 -32.001 -53.452 1.00 156.00 ? 111 LEU A CD1 1 
ATOM   5536 C CD2 . LEU D 1 105 ? -32.375 -32.687 -52.781 1.00 129.71 ? 111 LEU A CD2 1 
ATOM   5537 N N   . LEU D 1 106 ? -31.716 -27.590 -54.415 1.00 124.14 ? 112 LEU A N   1 
ATOM   5538 C CA  . LEU D 1 106 ? -31.253 -26.563 -55.340 1.00 131.35 ? 112 LEU A CA  1 
ATOM   5539 C C   . LEU D 1 106 ? -29.935 -25.952 -54.883 1.00 141.89 ? 112 LEU A C   1 
ATOM   5540 O O   . LEU D 1 106 ? -29.157 -25.466 -55.712 1.00 154.25 ? 112 LEU A O   1 
ATOM   5541 C CB  . LEU D 1 106 ? -32.318 -25.476 -55.485 1.00 112.78 ? 112 LEU A CB  1 
ATOM   5542 C CG  . LEU D 1 106 ? -33.661 -25.927 -56.063 1.00 130.53 ? 112 LEU A CG  1 
ATOM   5543 C CD1 . LEU D 1 106 ? -34.672 -24.794 -56.034 1.00 133.68 ? 112 LEU A CD1 1 
ATOM   5544 C CD2 . LEU D 1 106 ? -33.514 -26.482 -57.459 1.00 132.00 ? 112 LEU A CD2 1 
ATOM   5545 N N   . SER D 1 107 ? -29.664 -25.971 -53.574 1.00 127.63 ? 113 SER A N   1 
ATOM   5546 C CA  . SER D 1 107 ? -28.402 -25.460 -53.051 1.00 111.83 ? 113 SER A CA  1 
ATOM   5547 C C   . SER D 1 107 ? -27.210 -26.272 -53.526 1.00 111.12 ? 113 SER A C   1 
ATOM   5548 O O   . SER D 1 107 ? -26.070 -25.879 -53.263 1.00 118.97 ? 113 SER A O   1 
ATOM   5549 C CB  . SER D 1 107 ? -28.426 -25.449 -51.523 1.00 111.52 ? 113 SER A CB  1 
ATOM   5550 O OG  . SER D 1 107 ? -29.552 -24.735 -51.050 1.00 117.39 ? 113 SER A OG  1 
ATOM   5551 N N   . ARG D 1 108 ? -27.444 -27.396 -54.202 1.00 110.55 ? 114 ARG A N   1 
ATOM   5552 C CA  . ARG D 1 108 ? -26.378 -28.191 -54.791 1.00 127.65 ? 114 ARG A CA  1 
ATOM   5553 C C   . ARG D 1 108 ? -26.552 -28.388 -56.295 1.00 133.43 ? 114 ARG A C   1 
ATOM   5554 O O   . ARG D 1 108 ? -25.899 -29.262 -56.871 1.00 132.00 ? 114 ARG A O   1 
ATOM   5555 C CB  . ARG D 1 108 ? -26.270 -29.546 -54.092 1.00 138.09 ? 114 ARG A CB  1 
ATOM   5556 C CG  . ARG D 1 108 ? -25.652 -29.488 -52.714 1.00 139.45 ? 114 ARG A CG  1 
ATOM   5557 C CD  . ARG D 1 108 ? -25.530 -30.881 -52.141 1.00 161.76 ? 114 ARG A CD  1 
ATOM   5558 N NE  . ARG D 1 108 ? -24.844 -30.875 -50.858 1.00 174.32 ? 114 ARG A NE  1 
ATOM   5559 C CZ  . ARG D 1 108 ? -24.686 -31.938 -50.083 1.00 170.66 ? 114 ARG A CZ  1 
ATOM   5560 N NH1 . ARG D 1 108 ? -25.257 -33.098 -50.372 1.00 158.33 ? 114 ARG A NH1 1 
ATOM   5561 N NH2 . ARG D 1 108 ? -23.918 -31.840 -49.003 1.00 166.43 ? 114 ARG A NH2 1 
ATOM   5562 N N   . ILE D 1 109 ? -27.398 -27.596 -56.955 1.00 136.29 ? 115 ILE A N   1 
ATOM   5563 C CA  . ILE D 1 109 ? -27.583 -27.686 -58.401 1.00 131.92 ? 115 ILE A CA  1 
ATOM   5564 C C   . ILE D 1 109 ? -27.176 -26.354 -59.019 1.00 129.01 ? 115 ILE A C   1 
ATOM   5565 O O   . ILE D 1 109 ? -27.613 -25.294 -58.555 1.00 125.90 ? 115 ILE A O   1 
ATOM   5566 C CB  . ILE D 1 109 ? -29.036 -28.016 -58.793 1.00 141.21 ? 115 ILE A CB  1 
ATOM   5567 C CG1 . ILE D 1 109 ? -29.669 -29.103 -57.916 1.00 139.20 ? 115 ILE A CG1 1 
ATOM   5568 C CG2 . ILE D 1 109 ? -29.065 -28.496 -60.232 1.00 136.61 ? 115 ILE A CG2 1 
ATOM   5569 C CD1 . ILE D 1 109 ? -28.858 -30.356 -57.721 1.00 133.67 ? 115 ILE A CD1 1 
ATOM   5570 N N   . ASN D 1 110 ? -26.359 -26.404 -60.075 1.00 131.61 ? 116 ASN A N   1 
ATOM   5571 C CA  . ASN D 1 110 ? -25.971 -25.199 -60.800 1.00 137.23 ? 116 ASN A CA  1 
ATOM   5572 C C   . ASN D 1 110 ? -26.609 -25.063 -62.173 1.00 127.27 ? 116 ASN A C   1 
ATOM   5573 O O   . ASN D 1 110 ? -26.779 -23.936 -62.641 1.00 135.94 ? 116 ASN A O   1 
ATOM   5574 C CB  . ASN D 1 110 ? -24.446 -25.124 -60.975 1.00 139.21 ? 116 ASN A CB  1 
ATOM   5575 C CG  . ASN D 1 110 ? -23.738 -24.579 -59.748 1.00 129.90 ? 116 ASN A CG  1 
ATOM   5576 O OD1 . ASN D 1 110 ? -24.352 -23.946 -58.889 1.00 121.35 ? 116 ASN A OD1 1 
ATOM   5577 N ND2 . ASN D 1 110 ? -22.427 -24.785 -59.685 1.00 132.24 ? 116 ASN A ND2 1 
ATOM   5578 N N   . HIS D 1 111 ? -26.951 -26.162 -62.843 1.00 105.62 ? 117 HIS A N   1 
ATOM   5579 C CA  . HIS D 1 111 ? -27.490 -26.066 -64.192 1.00 115.53 ? 117 HIS A CA  1 
ATOM   5580 C C   . HIS D 1 111 ? -28.659 -27.025 -64.370 1.00 115.80 ? 117 HIS A C   1 
ATOM   5581 O O   . HIS D 1 111 ? -28.594 -28.183 -63.949 1.00 122.36 ? 117 HIS A O   1 
ATOM   5582 C CB  . HIS D 1 111 ? -26.419 -26.359 -65.247 1.00 116.39 ? 117 HIS A CB  1 
ATOM   5583 C CG  . HIS D 1 111 ? -26.918 -26.225 -66.650 1.00 115.18 ? 117 HIS A CG  1 
ATOM   5584 N ND1 . HIS D 1 111 ? -27.389 -25.033 -67.156 1.00 111.38 ? 117 HIS A ND1 1 
ATOM   5585 C CD2 . HIS D 1 111 ? -27.028 -27.128 -67.651 1.00 125.17 ? 117 HIS A CD2 1 
ATOM   5586 C CE1 . HIS D 1 111 ? -27.762 -25.206 -68.411 1.00 107.69 ? 117 HIS A CE1 1 
ATOM   5587 N NE2 . HIS D 1 111 ? -27.554 -26.469 -68.736 1.00 114.65 ? 117 HIS A NE2 1 
ATOM   5588 N N   . PHE D 1 112 ? -29.725 -26.529 -65.000 1.00 112.96 ? 118 PHE A N   1 
ATOM   5589 C CA  . PHE D 1 112 ? -30.889 -27.324 -65.363 1.00 108.27 ? 118 PHE A CA  1 
ATOM   5590 C C   . PHE D 1 112 ? -31.106 -27.257 -66.868 1.00 133.99 ? 118 PHE A C   1 
ATOM   5591 O O   . PHE D 1 112 ? -30.652 -26.328 -67.544 1.00 141.88 ? 118 PHE A O   1 
ATOM   5592 C CB  . PHE D 1 112 ? -32.167 -26.837 -64.668 1.00 127.62 ? 118 PHE A CB  1 
ATOM   5593 C CG  . PHE D 1 112 ? -32.143 -26.942 -63.175 1.00 144.07 ? 118 PHE A CG  1 
ATOM   5594 C CD1 . PHE D 1 112 ? -32.462 -28.126 -62.535 1.00 142.68 ? 118 PHE A CD1 1 
ATOM   5595 C CD2 . PHE D 1 112 ? -31.841 -25.837 -62.410 1.00 171.62 ? 118 PHE A CD2 1 
ATOM   5596 C CE1 . PHE D 1 112 ? -32.447 -28.199 -61.154 1.00 176.14 ? 118 PHE A CE1 1 
ATOM   5597 C CE2 . PHE D 1 112 ? -31.816 -25.902 -61.042 1.00 181.52 ? 118 PHE A CE2 1 
ATOM   5598 C CZ  . PHE D 1 112 ? -32.123 -27.080 -60.412 1.00 187.09 ? 118 PHE A CZ  1 
ATOM   5599 N N   . GLU D 1 113 ? -31.834 -28.248 -67.382 1.00 125.94 ? 119 GLU A N   1 
ATOM   5600 C CA  . GLU D 1 113 ? -32.216 -28.312 -68.789 1.00 107.16 ? 119 GLU A CA  1 
ATOM   5601 C C   . GLU D 1 113 ? -33.591 -28.956 -68.874 1.00 114.91 ? 119 GLU A C   1 
ATOM   5602 O O   . GLU D 1 113 ? -33.761 -30.108 -68.465 1.00 103.61 ? 119 GLU A O   1 
ATOM   5603 C CB  . GLU D 1 113 ? -31.192 -29.108 -69.608 1.00 108.17 ? 119 GLU A CB  1 
ATOM   5604 C CG  . GLU D 1 113 ? -29.820 -28.447 -69.714 1.00 113.65 ? 119 GLU A CG  1 
ATOM   5605 C CD  . GLU D 1 113 ? -28.834 -29.268 -70.523 1.00 150.47 ? 119 GLU A CD  1 
ATOM   5606 O OE1 . GLU D 1 113 ? -29.227 -30.339 -71.031 1.00 163.36 ? 119 GLU A OE1 1 
ATOM   5607 O OE2 . GLU D 1 113 ? -27.658 -28.856 -70.629 1.00 165.33 ? 119 GLU A OE2 1 
ATOM   5608 N N   . LYS D 1 114 ? -34.568 -28.215 -69.393 1.00 103.36 ? 120 LYS A N   1 
ATOM   5609 C CA  . LYS D 1 114 ? -35.928 -28.727 -69.499 1.00 110.49 ? 120 LYS A CA  1 
ATOM   5610 C C   . LYS D 1 114 ? -36.010 -29.840 -70.535 1.00 125.86 ? 120 LYS A C   1 
ATOM   5611 O O   . LYS D 1 114 ? -35.248 -29.878 -71.504 1.00 133.34 ? 120 LYS A O   1 
ATOM   5612 C CB  . LYS D 1 114 ? -36.898 -27.607 -69.879 1.00 104.00 ? 120 LYS A CB  1 
ATOM   5613 C CG  . LYS D 1 114 ? -37.188 -26.599 -68.781 1.00 115.07 ? 120 LYS A CG  1 
ATOM   5614 C CD  . LYS D 1 114 ? -38.406 -25.758 -69.133 1.00 148.07 ? 120 LYS A CD  1 
ATOM   5615 C CE  . LYS D 1 114 ? -38.680 -24.714 -68.071 1.00 140.27 ? 120 LYS A CE  1 
ATOM   5616 N NZ  . LYS D 1 114 ? -39.885 -23.898 -68.372 1.00 145.68 ? 120 LYS A NZ  1 
ATOM   5617 N N   . ILE D 1 115 ? -37.003 -30.719 -70.365 1.00 128.13 ? 121 ILE A N   1 
ATOM   5618 C CA  . ILE D 1 115 ? -37.240 -31.799 -71.370 1.00 131.92 ? 121 ILE A CA  1 
ATOM   5619 C C   . ILE D 1 115 ? -38.748 -32.063 -71.431 1.00 137.27 ? 121 ILE A C   1 
ATOM   5620 O O   . ILE D 1 115 ? -39.442 -31.722 -70.457 1.00 131.33 ? 121 ILE A O   1 
ATOM   5621 C CB  . ILE D 1 115 ? -36.463 -33.078 -71.016 1.00 142.38 ? 121 ILE A CB  1 
ATOM   5622 C CG1 . ILE D 1 115 ? -36.268 -33.978 -72.239 1.00 159.03 ? 121 ILE A CG1 1 
ATOM   5623 C CG2 . ILE D 1 115 ? -37.136 -33.820 -69.873 1.00 145.73 ? 121 ILE A CG2 1 
ATOM   5624 C CD1 . ILE D 1 115 ? -35.660 -35.322 -71.921 1.00 164.03 ? 121 ILE A CD1 1 
ATOM   5625 N N   . GLN D 1 116 ? -39.230 -32.639 -72.535 1.00 150.17 ? 122 GLN A N   1 
ATOM   5626 C CA  . GLN D 1 116 ? -40.674 -32.962 -72.672 1.00 143.83 ? 122 GLN A CA  1 
ATOM   5627 C C   . GLN D 1 116 ? -40.911 -34.398 -72.200 1.00 153.11 ? 122 GLN A C   1 
ATOM   5628 O O   . GLN D 1 116 ? -40.879 -35.309 -73.045 1.00 149.21 ? 122 GLN A O   1 
ATOM   5629 C CB  . GLN D 1 116 ? -41.124 -32.807 -74.124 1.00 144.47 ? 122 GLN A CB  1 
ATOM   5630 C CG  . GLN D 1 116 ? -40.528 -31.593 -74.821 1.00 154.64 ? 122 GLN A CG  1 
ATOM   5631 C CD  . GLN D 1 116 ? -41.231 -31.289 -76.121 1.00 153.92 ? 122 GLN A CD  1 
ATOM   5632 O OE1 . GLN D 1 116 ? -41.299 -32.123 -77.021 1.00 167.67 ? 122 GLN A OE1 1 
ATOM   5633 N NE2 . GLN D 1 116 ? -41.770 -30.086 -76.225 1.00 142.50 ? 122 GLN A NE2 1 
ATOM   5634 N N   . ILE D 1 117 ? -41.140 -34.584 -70.899 1.00 154.34 ? 123 ILE A N   1 
ATOM   5635 C CA  . ILE D 1 117 ? -41.345 -35.950 -70.340 1.00 156.40 ? 123 ILE A CA  1 
ATOM   5636 C C   . ILE D 1 117 ? -42.602 -36.557 -70.960 1.00 178.14 ? 123 ILE A C   1 
ATOM   5637 O O   . ILE D 1 117 ? -42.514 -37.683 -71.480 1.00 195.48 ? 123 ILE A O   1 
ATOM   5638 C CB  . ILE D 1 117 ? -41.476 -35.892 -68.807 1.00 148.97 ? 123 ILE A CB  1 
ATOM   5639 C CG1 . ILE D 1 117 ? -40.125 -35.688 -68.121 1.00 154.46 ? 123 ILE A CG1 1 
ATOM   5640 C CG2 . ILE D 1 117 ? -42.181 -37.128 -68.273 1.00 157.10 ? 123 ILE A CG2 1 
ATOM   5641 C CD1 . ILE D 1 117 ? -40.163 -35.983 -66.642 1.00 168.93 ? 123 ILE A CD1 1 
ATOM   5642 N N   . ILE D 1 118 ? -43.719 -35.825 -70.926 1.00 142.32 ? 124 ILE A N   1 
ATOM   5643 C CA  . ILE D 1 118 ? -45.014 -36.360 -71.435 1.00 150.01 ? 124 ILE A CA  1 
ATOM   5644 C C   . ILE D 1 118 ? -45.596 -35.340 -72.414 1.00 142.68 ? 124 ILE A C   1 
ATOM   5645 O O   . ILE D 1 118 ? -45.307 -34.153 -72.241 1.00 143.23 ? 124 ILE A O   1 
ATOM   5646 C CB  . ILE D 1 118 ? -45.954 -36.630 -70.243 1.00 158.16 ? 124 ILE A CB  1 
ATOM   5647 C CG1 . ILE D 1 118 ? -45.483 -37.829 -69.417 1.00 180.56 ? 124 ILE A CG1 1 
ATOM   5648 C CG2 . ILE D 1 118 ? -47.400 -36.795 -70.684 1.00 154.29 ? 124 ILE A CG2 1 
ATOM   5649 C CD1 . ILE D 1 118 ? -45.364 -39.109 -70.210 1.00 171.62 ? 124 ILE A CD1 1 
ATOM   5650 N N   . PRO D 1 119 ? -46.355 -35.718 -73.475 1.00 30.00  ? 125 PRO A N   1 
ATOM   5651 C CA  . PRO D 1 119 ? -46.995 -34.730 -74.350 1.00 30.00  ? 125 PRO A CA  1 
ATOM   5652 C C   . PRO D 1 119 ? -48.447 -34.432 -73.951 1.00 30.00  ? 125 PRO A C   1 
ATOM   5653 O O   . PRO D 1 119 ? -48.925 -35.022 -72.998 1.00 30.00  ? 125 PRO A O   1 
ATOM   5654 C CB  . PRO D 1 119 ? -46.989 -35.458 -75.698 1.00 30.00  ? 125 PRO A CB  1 
ATOM   5655 C CG  . PRO D 1 119 ? -47.268 -36.894 -75.320 1.00 30.00  ? 125 PRO A CG  1 
ATOM   5656 C CD  . PRO D 1 119 ? -46.590 -37.085 -73.978 1.00 30.00  ? 125 PRO A CD  1 
ATOM   5657 N N   . LYS D 1 120 a -49.111 -33.528 -74.679 1.00 149.82 ? 125 LYS A N   1 
ATOM   5658 C CA  . LYS D 1 120 a -50.545 -33.236 -74.405 1.00 144.55 ? 125 LYS A CA  1 
ATOM   5659 C C   . LYS D 1 120 a -51.414 -34.245 -75.163 1.00 131.13 ? 125 LYS A C   1 
ATOM   5660 O O   . LYS D 1 120 a -52.580 -34.433 -74.765 1.00 172.57 ? 125 LYS A O   1 
ATOM   5661 C CB  . LYS D 1 120 a -50.897 -31.797 -74.794 1.00 150.41 ? 125 LYS A CB  1 
ATOM   5662 C CG  . LYS D 1 120 a -50.543 -30.745 -73.752 1.00 170.39 ? 125 LYS A CG  1 
ATOM   5663 C CD  . LYS D 1 120 a -50.964 -29.344 -74.139 1.00 168.33 ? 125 LYS A CD  1 
ATOM   5664 C CE  . LYS D 1 120 a -50.520 -28.300 -73.136 1.00 175.74 ? 125 LYS A CE  1 
ATOM   5665 N NZ  . LYS D 1 120 a -50.970 -28.633 -71.764 1.00 170.93 ? 125 LYS A NZ  1 
ATOM   5666 N N   . SER D 1 121 b -50.859 -34.875 -76.203 1.00 162.55 ? 125 SER A N   1 
ATOM   5667 C CA  . SER D 1 121 b -51.609 -35.913 -76.957 1.00 177.22 ? 125 SER A CA  1 
ATOM   5668 C C   . SER D 1 121 b -51.986 -37.048 -76.002 1.00 201.23 ? 125 SER A C   1 
ATOM   5669 O O   . SER D 1 121 b -53.030 -37.692 -76.229 1.00 172.22 ? 125 SER A O   1 
ATOM   5670 C CB  . SER D 1 121 b -50.804 -36.421 -78.122 1.00 176.21 ? 125 SER A CB  1 
ATOM   5671 O OG  . SER D 1 121 b -50.450 -35.356 -78.992 1.00 156.17 ? 125 SER A OG  1 
ATOM   5672 N N   . SER D 1 122 ? -51.084 -37.345 -75.065 1.00 30.00  ? 126 SER A N   1 
ATOM   5673 C CA  . SER D 1 122 ? -51.338 -38.428 -74.089 1.00 30.00  ? 126 SER A CA  1 
ATOM   5674 C C   . SER D 1 122 ? -52.697 -38.173 -73.444 1.00 30.00  ? 126 SER A C   1 
ATOM   5675 O O   . SER D 1 122 ? -53.522 -39.095 -73.408 1.00 30.00  ? 126 SER A O   1 
ATOM   5676 C CB  . SER D 1 122 ? -50.248 -38.479 -73.061 1.00 30.00  ? 126 SER A CB  1 
ATOM   5677 O OG  . SER D 1 122 ? -50.333 -39.671 -72.296 1.00 30.00  ? 126 SER A OG  1 
ATOM   5678 N N   . TRP D 1 123 ? -52.911 -36.949 -72.969 1.00 172.25 ? 127 TRP A N   1 
ATOM   5679 C CA  . TRP D 1 123 ? -54.178 -36.667 -72.254 1.00 139.51 ? 127 TRP A CA  1 
ATOM   5680 C C   . TRP D 1 123 ? -55.345 -36.188 -73.112 1.00 138.79 ? 127 TRP A C   1 
ATOM   5681 O O   . TRP D 1 123 ? -56.477 -36.251 -72.620 1.00 140.27 ? 127 TRP A O   1 
ATOM   5682 C CB  . TRP D 1 123 ? -54.018 -35.460 -71.331 1.00 140.63 ? 127 TRP A CB  1 
ATOM   5683 C CG  . TRP D 1 123 ? -53.053 -35.765 -70.231 1.00 178.75 ? 127 TRP A CG  1 
ATOM   5684 C CD1 . TRP D 1 123 ? -53.237 -36.621 -69.185 1.00 197.28 ? 127 TRP A CD1 1 
ATOM   5685 C CD2 . TRP D 1 123 ? -51.718 -35.256 -70.100 1.00 198.66 ? 127 TRP A CD2 1 
ATOM   5686 N NE1 . TRP D 1 123 ? -52.114 -36.667 -68.405 1.00 211.28 ? 127 TRP A NE1 1 
ATOM   5687 C CE2 . TRP D 1 123 ? -51.166 -35.837 -68.941 1.00 210.56 ? 127 TRP A CE2 1 
ATOM   5688 C CE3 . TRP D 1 123 ? -50.947 -34.356 -70.837 1.00 190.85 ? 127 TRP A CE3 1 
ATOM   5689 C CZ2 . TRP D 1 123 ? -49.872 -35.553 -68.514 1.00 209.53 ? 127 TRP A CZ2 1 
ATOM   5690 C CZ3 . TRP D 1 123 ? -49.670 -34.080 -70.409 1.00 187.52 ? 127 TRP A CZ3 1 
ATOM   5691 C CH2 . TRP D 1 123 ? -49.154 -34.641 -69.246 1.00 201.11 ? 127 TRP A CH2 1 
ATOM   5692 N N   . SER D 1 124 ? -55.073 -35.769 -74.349 1.00 158.89 ? 128 SER A N   1 
ATOM   5693 C CA  . SER D 1 124 ? -56.162 -35.337 -75.262 1.00 152.62 ? 128 SER A CA  1 
ATOM   5694 C C   . SER D 1 124 ? -56.859 -36.669 -75.537 1.00 147.75 ? 128 SER A C   1 
ATOM   5695 O O   . SER D 1 124 ? -58.104 -36.705 -75.481 1.00 140.91 ? 128 SER A O   1 
ATOM   5696 C CB  . SER D 1 124 ? -55.538 -34.795 -76.511 1.00 149.88 ? 128 SER A CB  1 
ATOM   5697 O OG  . SER D 1 124 ? -54.612 -33.764 -76.204 1.00 161.63 ? 128 SER A OG  1 
ATOM   5698 N N   . SER D 1 125 ? -56.078 -37.716 -75.810 1.00 139.57 ? 129 SER A N   1 
ATOM   5699 C CA  . SER D 1 125 ? -56.645 -39.066 -76.051 1.00 145.88 ? 129 SER A CA  1 
ATOM   5700 C C   . SER D 1 125 ? -57.850 -39.426 -75.179 1.00 160.49 ? 129 SER A C   1 
ATOM   5701 O O   . SER D 1 125 ? -58.824 -39.976 -75.725 1.00 189.70 ? 129 SER A O   1 
ATOM   5702 C CB  . SER D 1 125 ? -55.617 -40.122 -75.765 1.00 140.96 ? 129 SER A CB  1 
ATOM   5703 O OG  . SER D 1 125 ? -55.501 -40.339 -74.367 1.00 148.13 ? 129 SER A OG  1 
ATOM   5704 N N   . HIS D 1 126 ? -57.792 -39.138 -73.877 1.00 159.11 ? 130 HIS A N   1 
ATOM   5705 C CA  . HIS D 1 126 ? -58.983 -39.391 -73.025 1.00 164.29 ? 130 HIS A CA  1 
ATOM   5706 C C   . HIS D 1 126 ? -59.340 -38.196 -72.138 1.00 160.87 ? 130 HIS A C   1 
ATOM   5707 O O   . HIS D 1 126 ? -60.256 -38.318 -71.302 1.00 170.29 ? 130 HIS A O   1 
ATOM   5708 C CB  . HIS D 1 126 ? -58.701 -40.637 -72.182 1.00 181.71 ? 130 HIS A CB  1 
ATOM   5709 C CG  . HIS D 1 126 ? -59.774 -41.663 -72.299 1.00 198.03 ? 130 HIS A CG  1 
ATOM   5710 N ND1 . HIS D 1 126 ? -61.094 -41.322 -72.500 1.00 206.08 ? 130 HIS A ND1 1 
ATOM   5711 C CD2 . HIS D 1 126 ? -59.739 -43.000 -72.251 1.00 208.30 ? 130 HIS A CD2 1 
ATOM   5712 C CE1 . HIS D 1 126 ? -61.824 -42.426 -72.566 1.00 203.32 ? 130 HIS A CE1 1 
ATOM   5713 N NE2 . HIS D 1 126 ? -61.021 -43.457 -72.418 1.00 213.19 ? 130 HIS A NE2 1 
ATOM   5714 N N   . GLU D 1 127 ? -58.647 -37.075 -72.316 1.00 154.48 ? 131 GLU A N   1 
ATOM   5715 C CA  . GLU D 1 127 ? -59.009 -35.815 -71.518 1.00 153.45 ? 131 GLU A CA  1 
ATOM   5716 C C   . GLU D 1 127 ? -59.288 -34.541 -72.299 1.00 162.25 ? 131 GLU A C   1 
ATOM   5717 O O   . GLU D 1 127 ? -59.592 -34.623 -73.502 1.00 182.55 ? 131 GLU A O   1 
ATOM   5718 C CB  . GLU D 1 127 ? -57.700 -35.692 -70.731 1.00 157.32 ? 131 GLU A CB  1 
ATOM   5719 C CG  . GLU D 1 127 ? -57.711 -36.441 -69.413 1.00 176.27 ? 131 GLU A CG  1 
ATOM   5720 C CD  . GLU D 1 127 ? -58.865 -36.097 -68.488 1.00 195.06 ? 131 GLU A CD  1 
ATOM   5721 O OE1 . GLU D 1 127 ? -58.685 -35.209 -67.638 1.00 237.94 ? 131 GLU A OE1 1 
ATOM   5722 O OE2 . GLU D 1 127 ? -59.935 -36.723 -68.611 1.00 176.95 ? 131 GLU A OE2 1 
ATOM   5723 N N   . ALA D 1 128 ? -59.205 -33.388 -71.625 1.00 121.94 ? 132 ALA A N   1 
ATOM   5724 C CA  . ALA D 1 128 ? -59.445 -32.070 -72.263 1.00 136.83 ? 132 ALA A CA  1 
ATOM   5725 C C   . ALA D 1 128 ? -58.254 -31.156 -71.939 1.00 130.94 ? 132 ALA A C   1 
ATOM   5726 O O   . ALA D 1 128 ? -57.818 -31.155 -70.782 1.00 130.09 ? 132 ALA A O   1 
ATOM   5727 C CB  . ALA D 1 128 ? -60.748 -31.435 -71.861 1.00 30.00  ? 132 ALA A CB  1 
ATOM   5728 N N   . SER D 1 129 ? -57.816 -30.335 -72.897 1.00 128.76 ? 133 SER A N   1 
ATOM   5729 C CA  . SER D 1 129 ? -56.633 -29.446 -72.766 1.00 107.66 ? 133 SER A CA  1 
ATOM   5730 C C   . SER D 1 129 ? -56.776 -28.601 -71.498 1.00 126.12 ? 133 SER A C   1 
ATOM   5731 O O   . SER D 1 129 ? -57.925 -28.400 -71.052 1.00 131.94 ? 133 SER A O   1 
ATOM   5732 C CB  . SER D 1 129 ? -56.471 -28.579 -73.985 1.00 30.00  ? 133 SER A CB  1 
ATOM   5733 O OG  . SER D 1 129 ? -57.593 -27.724 -74.146 1.00 30.00  ? 133 SER A OG  1 
ATOM   5734 N N   . LEU D 1 130 a -55.633 -28.111 -70.983 1.00 126.77 ? 133 LEU A N   1 
ATOM   5735 C CA  . LEU D 1 130 a -55.605 -27.229 -69.784 1.00 148.02 ? 133 LEU A CA  1 
ATOM   5736 C C   . LEU D 1 130 a -56.436 -25.973 -70.066 1.00 180.67 ? 133 LEU A C   1 
ATOM   5737 O O   . LEU D 1 130 a -56.413 -25.482 -71.214 1.00 213.96 ? 133 LEU A O   1 
ATOM   5738 C CB  . LEU D 1 130 a -54.143 -26.918 -69.428 1.00 30.00  ? 133 LEU A CB  1 
ATOM   5739 C CG  . LEU D 1 130 a -53.462 -25.753 -70.147 1.00 30.00  ? 133 LEU A CG  1 
ATOM   5740 C CD1 . LEU D 1 130 a -52.130 -25.436 -69.487 1.00 30.00  ? 133 LEU A CD1 1 
ATOM   5741 C CD2 . LEU D 1 130 a -53.243 -26.058 -71.622 1.00 30.00  ? 133 LEU A CD2 1 
ATOM   5742 N N   . GLY D 1 131 ? -57.192 -25.515 -69.070 1.00 163.86 ? 134 GLY A N   1 
ATOM   5743 C CA  . GLY D 1 131 ? -58.062 -24.342 -69.267 1.00 175.35 ? 134 GLY A CA  1 
ATOM   5744 C C   . GLY D 1 131 ? -57.322 -23.050 -68.988 1.00 185.03 ? 134 GLY A C   1 
ATOM   5745 O O   . GLY D 1 131 ? -56.270 -22.822 -69.620 1.00 186.62 ? 134 GLY A O   1 
ATOM   5746 N N   . VAL D 1 132 ? -57.839 -22.234 -68.067 1.00 178.39 ? 135 VAL A N   1 
ATOM   5747 C CA  . VAL D 1 132 ? -57.221 -20.900 -67.817 1.00 188.02 ? 135 VAL A CA  1 
ATOM   5748 C C   . VAL D 1 132 ? -57.081 -20.670 -66.311 1.00 195.48 ? 135 VAL A C   1 
ATOM   5749 O O   . VAL D 1 132 ? -57.229 -21.644 -65.546 1.00 192.18 ? 135 VAL A O   1 
ATOM   5750 C CB  . VAL D 1 132 ? -58.069 -19.785 -68.458 1.00 180.96 ? 135 VAL A CB  1 
ATOM   5751 C CG1 . VAL D 1 132 ? -58.133 -19.912 -69.972 1.00 167.04 ? 135 VAL A CG1 1 
ATOM   5752 C CG2 . VAL D 1 132 ? -59.471 -19.737 -67.870 1.00 154.57 ? 135 VAL A CG2 1 
ATOM   5753 N N   . SER D 1 133 ? -56.766 -19.437 -65.917 1.00 181.82 ? 136 SER A N   1 
ATOM   5754 C CA  . SER D 1 133 ? -56.717 -19.112 -64.471 1.00 192.37 ? 136 SER A CA  1 
ATOM   5755 C C   . SER D 1 133 ? -57.247 -17.687 -64.280 1.00 195.48 ? 136 SER A C   1 
ATOM   5756 O O   . SER D 1 133 ? -56.727 -16.772 -64.945 1.00 192.70 ? 136 SER A O   1 
ATOM   5757 C CB  . SER D 1 133 ? -55.337 -19.298 -63.897 1.00 191.24 ? 136 SER A CB  1 
ATOM   5758 O OG  . SER D 1 133 ? -54.776 -20.540 -64.295 1.00 206.09 ? 136 SER A OG  1 
ATOM   5759 N N   . SER D 1 134 ? -58.276 -17.525 -63.444 1.00 201.70 ? 137 SER A N   1 
ATOM   5760 C CA  . SER D 1 134 ? -58.883 -16.187 -63.219 1.00 182.64 ? 137 SER A CA  1 
ATOM   5761 C C   . SER D 1 134 ? -57.777 -15.166 -62.949 1.00 188.96 ? 137 SER A C   1 
ATOM   5762 O O   . SER D 1 134 ? -56.947 -15.424 -62.052 1.00 173.86 ? 137 SER A O   1 
ATOM   5763 C CB  . SER D 1 134 ? -59.879 -16.216 -62.094 1.00 185.50 ? 137 SER A CB  1 
ATOM   5764 O OG  . SER D 1 134 ? -59.992 -14.933 -61.497 1.00 198.70 ? 137 SER A OG  1 
ATOM   5765 N N   . ALA D 1 135 ? -57.762 -14.069 -63.712 1.00 196.28 ? 138 ALA A N   1 
ATOM   5766 C CA  . ALA D 1 135 ? -56.734 -13.015 -63.541 1.00 223.14 ? 138 ALA A CA  1 
ATOM   5767 C C   . ALA D 1 135 ? -55.330 -13.625 -63.620 1.00 218.88 ? 138 ALA A C   1 
ATOM   5768 O O   . ALA D 1 135 ? -54.418 -13.072 -62.975 1.00 240.02 ? 138 ALA A O   1 
ATOM   5769 C CB  . ALA D 1 135 ? -56.956 -12.273 -62.243 1.00 239.90 ? 138 ALA A CB  1 
ATOM   5770 N N   . CYS D 1 136 ? -55.157 -14.716 -64.377 1.00 218.80 ? 139 CYS A N   1 
ATOM   5771 C CA  . CYS D 1 136 ? -53.793 -15.283 -64.575 1.00 201.59 ? 139 CYS A CA  1 
ATOM   5772 C C   . CYS D 1 136 ? -53.540 -15.569 -66.062 1.00 181.55 ? 139 CYS A C   1 
ATOM   5773 O O   . CYS D 1 136 ? -53.306 -16.744 -66.405 1.00 180.24 ? 139 CYS A O   1 
ATOM   5774 C CB  . CYS D 1 136 ? -53.581 -16.538 -63.737 1.00 203.78 ? 139 CYS A CB  1 
ATOM   5775 S SG  . CYS D 1 136 ? -53.969 -16.319 -61.980 1.00 258.84 ? 139 CYS A SG  1 
ATOM   5776 N N   . PRO D 1 137 ? -53.579 -14.556 -66.956 1.00 175.58 ? 140 PRO A N   1 
ATOM   5777 C CA  . PRO D 1 137 ? -53.229 -14.716 -68.371 1.00 163.63 ? 140 PRO A CA  1 
ATOM   5778 C C   . PRO D 1 137 ? -51.737 -15.026 -68.556 1.00 188.82 ? 140 PRO A C   1 
ATOM   5779 O O   . PRO D 1 137 ? -50.960 -14.682 -67.684 1.00 201.98 ? 140 PRO A O   1 
ATOM   5780 C CB  . PRO D 1 137 ? -53.540 -13.345 -68.989 1.00 128.48 ? 140 PRO A CB  1 
ATOM   5781 C CG  . PRO D 1 137 ? -53.380 -12.382 -67.841 1.00 140.78 ? 140 PRO A CG  1 
ATOM   5782 C CD  . PRO D 1 137 ? -53.894 -13.150 -66.642 1.00 150.48 ? 140 PRO A CD  1 
ATOM   5783 N N   . TYR D 1 138 ? -51.373 -15.658 -69.676 1.00 179.06 ? 141 TYR A N   1 
ATOM   5784 C CA  . TYR D 1 138 ? -49.932 -15.906 -69.943 1.00 193.70 ? 141 TYR A CA  1 
ATOM   5785 C C   . TYR D 1 138 ? -49.232 -14.547 -70.043 1.00 200.85 ? 141 TYR A C   1 
ATOM   5786 O O   . TYR D 1 138 ? -48.256 -14.329 -69.299 1.00 193.43 ? 141 TYR A O   1 
ATOM   5787 C CB  . TYR D 1 138 ? -49.735 -16.805 -71.171 1.00 203.90 ? 141 TYR A CB  1 
ATOM   5788 C CG  . TYR D 1 138 ? -49.930 -16.149 -72.515 1.00 210.93 ? 141 TYR A CG  1 
ATOM   5789 C CD1 . TYR D 1 138 ? -51.162 -15.650 -72.901 1.00 194.27 ? 141 TYR A CD1 1 
ATOM   5790 C CD2 . TYR D 1 138 ? -48.882 -16.043 -73.413 1.00 218.87 ? 141 TYR A CD2 1 
ATOM   5791 C CE1 . TYR D 1 138 ? -51.344 -15.048 -74.134 1.00 190.63 ? 141 TYR A CE1 1 
ATOM   5792 C CE2 . TYR D 1 138 ? -49.046 -15.444 -74.650 1.00 184.05 ? 141 TYR A CE2 1 
ATOM   5793 C CZ  . TYR D 1 138 ? -50.283 -14.945 -75.014 1.00 174.01 ? 141 TYR A CZ  1 
ATOM   5794 O OH  . TYR D 1 138 ? -50.460 -14.352 -76.240 1.00 162.42 ? 141 TYR A OH  1 
ATOM   5795 N N   . GLN D 1 139 ? -49.740 -13.661 -70.902 1.00 230.30 ? 142 GLN A N   1 
ATOM   5796 C CA  . GLN D 1 139 ? -49.209 -12.294 -71.044 1.00 232.43 ? 142 GLN A CA  1 
ATOM   5797 C C   . GLN D 1 139 ? -50.519 -11.548 -71.186 1.00 237.56 ? 142 GLN A C   1 
ATOM   5798 O O   . GLN D 1 139 ? -50.774 -10.632 -70.381 1.00 236.02 ? 142 GLN A O   1 
ATOM   5799 C CB  . GLN D 1 139 ? -47.966 -12.271 -71.971 1.00 227.34 ? 142 GLN A CB  1 
ATOM   5800 C CG  . GLN D 1 139 ? -46.749 -12.990 -71.402 1.00 210.67 ? 142 GLN A CG  1 
ATOM   5801 C CD  . GLN D 1 139 ? -45.572 -13.019 -72.347 1.00 195.80 ? 142 GLN A CD  1 
ATOM   5802 O OE1 . GLN D 1 139 ? -45.722 -12.933 -73.564 1.00 197.22 ? 142 GLN A OE1 1 
ATOM   5803 N NE2 . GLN D 1 139 ? -44.378 -13.133 -71.788 1.00 174.33 ? 142 GLN A NE2 1 
ATOM   5804 N N   . GLY D 1 140 ? -51.329 -11.942 -72.175 1.00 210.49 ? 143 GLY A N   1 
ATOM   5805 C CA  . GLY D 1 140 ? -52.672 -11.289 -72.403 1.00 165.45 ? 143 GLY A CA  1 
ATOM   5806 C C   . GLY D 1 140 ? -53.860 -12.158 -72.687 1.00 159.39 ? 143 GLY A C   1 
ATOM   5807 O O   . GLY D 1 140 ? -54.866 -11.607 -73.176 1.00 162.94 ? 143 GLY A O   1 
ATOM   5808 N N   . LYS D 1 141 ? -53.775 -13.462 -72.401 1.00 170.22 ? 144 LYS A N   1 
ATOM   5809 C CA  . LYS D 1 141 ? -54.908 -14.386 -72.676 1.00 175.26 ? 144 LYS A CA  1 
ATOM   5810 C C   . LYS D 1 141 ? -54.792 -15.310 -71.431 1.00 195.84 ? 144 LYS A C   1 
ATOM   5811 O O   . LYS D 1 141 ? -53.708 -15.894 -71.237 1.00 204.01 ? 144 LYS A O   1 
ATOM   5812 C CB  . LYS D 1 141 ? -54.910 -15.214 -73.951 1.00 163.61 ? 144 LYS A CB  1 
ATOM   5813 C CG  . LYS D 1 141 ? -54.728 -14.404 -75.228 1.00 140.21 ? 144 LYS A CG  1 
ATOM   5814 C CD  . LYS D 1 141 ? -54.464 -15.262 -76.445 1.00 131.48 ? 144 LYS A CD  1 
ATOM   5815 C CE  . LYS D 1 141 ? -54.143 -14.450 -77.682 1.00 146.19 ? 144 LYS A CE  1 
ATOM   5816 N NZ  . LYS D 1 141 ? -53.855 -15.318 -78.848 1.00 161.13 ? 144 LYS A NZ  1 
ATOM   5817 N N   . SER D 1 142 ? -55.869 -15.442 -70.651 1.00 180.08 ? 145 SER A N   1 
ATOM   5818 C CA  . SER D 1 142 ? -55.834 -16.250 -69.404 1.00 179.87 ? 145 SER A CA  1 
ATOM   5819 C C   . SER D 1 142 ? -55.158 -17.587 -69.713 1.00 199.81 ? 145 SER A C   1 
ATOM   5820 O O   . SER D 1 142 ? -55.447 -18.150 -70.785 1.00 197.79 ? 145 SER A O   1 
ATOM   5821 C CB  . SER D 1 142 ? -57.218 -16.437 -68.859 1.00 159.77 ? 145 SER A CB  1 
ATOM   5822 O OG  . SER D 1 142 ? -57.766 -15.192 -68.450 1.00 157.71 ? 145 SER A OG  1 
ATOM   5823 N N   . SER D 1 143 ? -54.321 -18.097 -68.804 1.00 193.94 ? 146 SER A N   1 
ATOM   5824 C CA  . SER D 1 143 ? -53.558 -19.305 -69.114 1.00 194.82 ? 146 SER A CA  1 
ATOM   5825 C C   . SER D 1 143 ? -53.185 -20.004 -67.809 1.00 172.05 ? 146 SER A C   1 
ATOM   5826 O O   . SER D 1 143 ? -53.770 -19.741 -66.753 1.00 187.55 ? 146 SER A O   1 
ATOM   5827 C CB  . SER D 1 143 ? -52.324 -18.932 -69.955 1.00 212.91 ? 146 SER A CB  1 
ATOM   5828 O OG  . SER D 1 143 ? -52.701 -18.440 -71.229 1.00 223.50 ? 146 SER A OG  1 
ATOM   5829 N N   . PHE D 1 144 ? -52.199 -20.900 -67.889 1.00 158.96 ? 147 PHE A N   1 
ATOM   5830 C CA  . PHE D 1 144 ? -51.795 -21.764 -66.789 1.00 141.22 ? 147 PHE A CA  1 
ATOM   5831 C C   . PHE D 1 144 ? -50.280 -21.919 -66.820 1.00 124.76 ? 147 PHE A C   1 
ATOM   5832 O O   . PHE D 1 144 ? -49.596 -21.367 -67.689 1.00 128.73 ? 147 PHE A O   1 
ATOM   5833 C CB  . PHE D 1 144 ? -52.485 -23.131 -66.890 1.00 146.22 ? 147 PHE A CB  1 
ATOM   5834 C CG  . PHE D 1 144 ? -52.474 -23.922 -65.614 1.00 134.78 ? 147 PHE A CG  1 
ATOM   5835 C CD1 . PHE D 1 144 ? -53.226 -23.519 -64.525 1.00 155.82 ? 147 PHE A CD1 1 
ATOM   5836 C CD2 . PHE D 1 144 ? -51.702 -25.068 -65.503 1.00 116.89 ? 147 PHE A CD2 1 
ATOM   5837 C CE1 . PHE D 1 144 ? -53.215 -24.246 -63.351 1.00 164.97 ? 147 PHE A CE1 1 
ATOM   5838 C CE2 . PHE D 1 144 ? -51.682 -25.796 -64.332 1.00 108.95 ? 147 PHE A CE2 1 
ATOM   5839 C CZ  . PHE D 1 144 ? -52.442 -25.387 -63.254 1.00 146.84 ? 147 PHE A CZ  1 
ATOM   5840 N N   . PHE D 1 145 ? -49.754 -22.684 -65.865 1.00 109.50 ? 148 PHE A N   1 
ATOM   5841 C CA  . PHE D 1 145 ? -48.335 -23.006 -65.851 1.00 92.54  ? 148 PHE A CA  1 
ATOM   5842 C C   . PHE D 1 145 ? -47.962 -23.789 -67.103 1.00 95.39  ? 148 PHE A C   1 
ATOM   5843 O O   . PHE D 1 145 ? -48.743 -24.605 -67.602 1.00 100.41 ? 148 PHE A O   1 
ATOM   5844 C CB  . PHE D 1 145 ? -47.994 -23.813 -64.598 1.00 105.55 ? 148 PHE A CB  1 
ATOM   5845 C CG  . PHE D 1 145 ? -48.115 -23.030 -63.323 1.00 110.55 ? 148 PHE A CG  1 
ATOM   5846 C CD1 . PHE D 1 145 ? -47.355 -21.892 -63.119 1.00 109.85 ? 148 PHE A CD1 1 
ATOM   5847 C CD2 . PHE D 1 145 ? -48.992 -23.431 -62.330 1.00 145.65 ? 148 PHE A CD2 1 
ATOM   5848 C CE1 . PHE D 1 145 ? -47.467 -21.169 -61.947 1.00 151.17 ? 148 PHE A CE1 1 
ATOM   5849 C CE2 . PHE D 1 145 ? -49.109 -22.713 -61.155 1.00 177.50 ? 148 PHE A CE2 1 
ATOM   5850 C CZ  . PHE D 1 145 ? -48.345 -21.580 -60.963 1.00 176.93 ? 148 PHE A CZ  1 
ATOM   5851 N N   . ARG D 1 146 ? -46.760 -23.536 -67.619 1.00 96.45  ? 149 ARG A N   1 
ATOM   5852 C CA  . ARG D 1 146 ? -46.353 -24.134 -68.885 1.00 111.54 ? 149 ARG A CA  1 
ATOM   5853 C C   . ARG D 1 146 ? -45.698 -25.497 -68.728 1.00 131.28 ? 149 ARG A C   1 
ATOM   5854 O O   . ARG D 1 146 ? -45.561 -26.219 -69.723 1.00 143.37 ? 149 ARG A O   1 
ATOM   5855 C CB  . ARG D 1 146 ? -45.384 -23.209 -69.629 1.00 83.21  ? 149 ARG A CB  1 
ATOM   5856 C CG  . ARG D 1 146 ? -45.910 -21.801 -69.848 1.00 134.94 ? 149 ARG A CG  1 
ATOM   5857 C CD  . ARG D 1 146 ? -44.958 -20.984 -70.711 1.00 130.54 ? 149 ARG A CD  1 
ATOM   5858 N NE  . ARG D 1 146 ? -45.435 -19.618 -70.893 1.00 143.38 ? 149 ARG A NE  1 
ATOM   5859 C CZ  . ARG D 1 146 ? -44.821 -18.700 -71.627 1.00 154.78 ? 149 ARG A CZ  1 
ATOM   5860 N NH1 . ARG D 1 146 ? -43.713 -18.977 -72.295 1.00 160.11 ? 149 ARG A NH1 1 
ATOM   5861 N NH2 . ARG D 1 146 ? -45.329 -17.472 -71.690 1.00 155.87 ? 149 ARG A NH2 1 
ATOM   5862 N N   . ASN D 1 147 ? -45.283 -25.865 -67.519 1.00 106.73 ? 150 ASN A N   1 
ATOM   5863 C CA  . ASN D 1 147 ? -44.609 -27.135 -67.287 1.00 89.86  ? 150 ASN A CA  1 
ATOM   5864 C C   . ASN D 1 147 ? -45.536 -28.217 -66.755 1.00 88.96  ? 150 ASN A C   1 
ATOM   5865 O O   . ASN D 1 147 ? -45.082 -29.342 -66.531 1.00 92.82  ? 150 ASN A O   1 
ATOM   5866 C CB  . ASN D 1 147 ? -43.437 -26.941 -66.319 1.00 81.58  ? 150 ASN A CB  1 
ATOM   5867 C CG  . ASN D 1 147 ? -42.331 -26.085 -66.906 1.00 104.46 ? 150 ASN A CG  1 
ATOM   5868 O OD1 . ASN D 1 147 ? -42.406 -25.652 -68.056 1.00 121.93 ? 150 ASN A OD1 1 
ATOM   5869 N ND2 . ASN D 1 147 ? -41.297 -25.833 -66.112 1.00 112.51 ? 150 ASN A ND2 1 
ATOM   5870 N N   . VAL D 1 148 ? -46.816 -27.908 -66.536 1.00 76.69  ? 151 VAL A N   1 
ATOM   5871 C CA  . VAL D 1 148 ? -47.769 -28.871 -66.002 1.00 75.77  ? 151 VAL A CA  1 
ATOM   5872 C C   . VAL D 1 148 ? -49.079 -28.690 -66.761 1.00 98.02  ? 151 VAL A C   1 
ATOM   5873 O O   . VAL D 1 148 ? -49.348 -27.629 -67.326 1.00 112.21 ? 151 VAL A O   1 
ATOM   5874 C CB  . VAL D 1 148 ? -47.964 -28.690 -64.474 1.00 83.15  ? 151 VAL A CB  1 
ATOM   5875 C CG1 . VAL D 1 148 ? -48.912 -29.720 -63.913 1.00 75.43  ? 151 VAL A CG1 1 
ATOM   5876 C CG2 . VAL D 1 148 ? -46.632 -28.739 -63.737 1.00 93.75  ? 151 VAL A CG2 1 
ATOM   5877 N N   . VAL D 1 149 ? -49.899 -29.742 -66.779 1.00 103.89 ? 152 VAL A N   1 
ATOM   5878 C CA  . VAL D 1 149 ? -51.135 -29.773 -67.558 1.00 101.94 ? 152 VAL A CA  1 
ATOM   5879 C C   . VAL D 1 149 ? -52.329 -29.694 -66.614 1.00 116.75 ? 152 VAL A C   1 
ATOM   5880 O O   . VAL D 1 149 ? -52.527 -30.583 -65.777 1.00 113.14 ? 152 VAL A O   1 
ATOM   5881 C CB  . VAL D 1 149 ? -51.226 -31.034 -68.428 1.00 98.61  ? 152 VAL A CB  1 
ATOM   5882 C CG1 . VAL D 1 149 ? -52.399 -30.914 -69.384 1.00 127.47 ? 152 VAL A CG1 1 
ATOM   5883 C CG2 . VAL D 1 149 ? -49.934 -31.259 -69.181 1.00 118.34 ? 152 VAL A CG2 1 
ATOM   5884 N N   . TRP D 1 150 ? -53.133 -28.637 -66.752 1.00 133.22 ? 153 TRP A N   1 
ATOM   5885 C CA  . TRP D 1 150 ? -54.361 -28.525 -65.921 1.00 131.44 ? 153 TRP A CA  1 
ATOM   5886 C C   . TRP D 1 150 ? -55.403 -29.396 -66.633 1.00 130.96 ? 153 TRP A C   1 
ATOM   5887 O O   . TRP D 1 150 ? -56.264 -28.827 -67.333 1.00 146.80 ? 153 TRP A O   1 
ATOM   5888 C CB  . TRP D 1 150 ? -54.832 -27.069 -65.837 1.00 157.82 ? 153 TRP A CB  1 
ATOM   5889 C CG  . TRP D 1 150 ? -55.875 -26.845 -64.786 1.00 173.03 ? 153 TRP A CG  1 
ATOM   5890 C CD1 . TRP D 1 150 ? -55.791 -27.170 -63.463 1.00 164.90 ? 153 TRP A CD1 1 
ATOM   5891 C CD2 . TRP D 1 150 ? -57.161 -26.228 -64.966 1.00 189.10 ? 153 TRP A CD2 1 
ATOM   5892 N NE1 . TRP D 1 150 ? -56.938 -26.809 -62.811 1.00 147.58 ? 153 TRP A NE1 1 
ATOM   5893 C CE2 . TRP D 1 150 ? -57.796 -26.226 -63.706 1.00 167.64 ? 153 TRP A CE2 1 
ATOM   5894 C CE3 . TRP D 1 150 ? -57.836 -25.681 -66.062 1.00 186.06 ? 153 TRP A CE3 1 
ATOM   5895 C CZ2 . TRP D 1 150 ? -59.072 -25.699 -63.519 1.00 171.19 ? 153 TRP A CZ2 1 
ATOM   5896 C CZ3 . TRP D 1 150 ? -59.096 -25.159 -65.875 1.00 176.66 ? 153 TRP A CZ3 1 
ATOM   5897 C CH2 . TRP D 1 150 ? -59.704 -25.171 -64.620 1.00 174.41 ? 153 TRP A CH2 1 
ATOM   5898 N N   . LEU D 1 151 ? -55.309 -30.721 -66.487 1.00 117.08 ? 154 LEU A N   1 
ATOM   5899 C CA  . LEU D 1 151 ? -56.246 -31.622 -67.247 1.00 118.50 ? 154 LEU A CA  1 
ATOM   5900 C C   . LEU D 1 151 ? -57.703 -31.356 -66.896 1.00 116.23 ? 154 LEU A C   1 
ATOM   5901 O O   . LEU D 1 151 ? -57.946 -30.944 -65.745 1.00 127.66 ? 154 LEU A O   1 
ATOM   5902 C CB  . LEU D 1 151 ? -55.846 -33.069 -66.941 1.00 133.09 ? 154 LEU A CB  1 
ATOM   5903 C CG  . LEU D 1 151 ? -55.935 -33.474 -65.471 1.00 127.50 ? 154 LEU A CG  1 
ATOM   5904 C CD1 . LEU D 1 151 ? -57.369 -33.797 -65.084 1.00 150.89 ? 154 LEU A CD1 1 
ATOM   5905 C CD2 . LEU D 1 151 ? -55.028 -34.660 -65.183 1.00 117.48 ? 154 LEU A CD2 1 
ATOM   5906 N N   . ILE D 1 152 ? -58.627 -31.545 -67.848 1.00 106.42 ? 155 ILE A N   1 
ATOM   5907 C CA  . ILE D 1 152 ? -60.084 -31.333 -67.590 1.00 114.46 ? 155 ILE A CA  1 
ATOM   5908 C C   . ILE D 1 152 ? -60.787 -32.539 -68.226 1.00 116.18 ? 155 ILE A C   1 
ATOM   5909 O O   . ILE D 1 152 ? -60.141 -33.216 -69.044 1.00 125.33 ? 155 ILE A O   1 
ATOM   5910 C CB  . ILE D 1 152 ? -60.433 -30.013 -68.308 1.00 109.88 ? 155 ILE A CB  1 
ATOM   5911 C CG1 . ILE D 1 152 ? -59.775 -28.803 -67.642 1.00 127.00 ? 155 ILE A CG1 1 
ATOM   5912 C CG2 . ILE D 1 152 ? -61.939 -29.823 -68.417 1.00 102.11 ? 155 ILE A CG2 1 
ATOM   5913 C CD1 . ILE D 1 152 ? -60.449 -27.498 -67.982 1.00 126.94 ? 155 ILE A CD1 1 
ATOM   5914 N N   . LYS D 1 153 ? -62.049 -32.799 -67.872 1.00 105.32 ? 156 LYS A N   1 
ATOM   5915 C CA  . LYS D 1 153 ? -62.770 -33.999 -68.382 1.00 109.49 ? 156 LYS A CA  1 
ATOM   5916 C C   . LYS D 1 153 ? -63.187 -33.811 -69.846 1.00 120.65 ? 156 LYS A C   1 
ATOM   5917 O O   . LYS D 1 153 ? -63.443 -32.656 -70.241 1.00 123.17 ? 156 LYS A O   1 
ATOM   5918 C CB  . LYS D 1 153 ? -64.003 -34.269 -67.515 1.00 119.27 ? 156 LYS A CB  1 
ATOM   5919 C CG  . LYS D 1 153 ? -65.016 -33.133 -67.467 1.00 143.60 ? 156 LYS A CG  1 
ATOM   5920 C CD  . LYS D 1 153 ? -66.149 -33.370 -66.497 1.00 159.56 ? 156 LYS A CD  1 
ATOM   5921 C CE  . LYS D 1 153 ? -67.237 -32.323 -66.606 1.00 148.22 ? 156 LYS A CE  1 
ATOM   5922 N NZ  . LYS D 1 153 ? -68.312 -32.537 -65.609 1.00 148.35 ? 156 LYS A NZ  1 
ATOM   5923 N N   . LYS D 1 154 ? -63.252 -34.903 -70.617 1.00 141.17 ? 157 LYS A N   1 
ATOM   5924 C CA  . LYS D 1 154 ? -63.721 -34.845 -72.027 1.00 133.37 ? 157 LYS A CA  1 
ATOM   5925 C C   . LYS D 1 154 ? -65.190 -35.249 -72.192 1.00 134.86 ? 157 LYS A C   1 
ATOM   5926 O O   . LYS D 1 154 ? -65.505 -36.422 -71.930 1.00 152.83 ? 157 LYS A O   1 
ATOM   5927 C CB  . LYS D 1 154 ? -62.795 -35.788 -72.801 1.00 138.82 ? 157 LYS A CB  1 
ATOM   5928 C CG  . LYS D 1 154 ? -63.022 -35.850 -74.305 1.00 140.81 ? 157 LYS A CG  1 
ATOM   5929 C CD  . LYS D 1 154 ? -61.989 -36.695 -75.016 1.00 147.90 ? 157 LYS A CD  1 
ATOM   5930 C CE  . LYS D 1 154 ? -62.317 -36.948 -76.472 1.00 152.25 ? 157 LYS A CE  1 
ATOM   5931 N NZ  . LYS D 1 154 ? -61.337 -37.866 -77.100 1.00 173.72 ? 157 LYS A NZ  1 
ATOM   5932 N N   . ASN D 1 155 ? -66.046 -34.309 -72.607 1.00 121.28 ? 158 ASN A N   1 
ATOM   5933 C CA  . ASN D 1 155 ? -67.482 -34.625 -72.834 1.00 141.22 ? 158 ASN A CA  1 
ATOM   5934 C C   . ASN D 1 155 ? -68.037 -35.285 -71.567 1.00 151.09 ? 158 ASN A C   1 
ATOM   5935 O O   . ASN D 1 155 ? -68.669 -36.352 -71.690 1.00 151.85 ? 158 ASN A O   1 
ATOM   5936 C CB  . ASN D 1 155 ? -67.683 -35.486 -74.084 1.00 158.15 ? 158 ASN A CB  1 
ATOM   5937 C CG  . ASN D 1 155 ? -69.129 -35.563 -74.527 1.00 154.17 ? 158 ASN A CG  1 
ATOM   5938 O OD1 . ASN D 1 155 ? -69.745 -34.545 -74.832 1.00 153.90 ? 158 ASN A OD1 1 
ATOM   5939 N ND2 . ASN D 1 155 ? -69.679 -36.766 -74.560 1.00 130.01 ? 158 ASN A ND2 1 
ATOM   5940 N N   . SER D 1 156 ? -67.800 -34.677 -70.400 1.00 164.41 ? 159 SER A N   1 
ATOM   5941 C CA  . SER D 1 156 ? -68.287 -35.220 -69.127 1.00 157.82 ? 159 SER A CA  1 
ATOM   5942 C C   . SER D 1 156 ? -67.815 -36.655 -68.903 1.00 170.24 ? 159 SER A C   1 
ATOM   5943 O O   . SER D 1 156 ? -68.467 -37.436 -68.204 1.00 177.18 ? 159 SER A O   1 
ATOM   5944 C CB  . SER D 1 156 ? -69.815 -35.137 -69.025 1.00 144.61 ? 159 SER A CB  1 
ATOM   5945 O OG  . SER D 1 156 ? -70.438 -36.193 -69.737 1.00 164.66 ? 159 SER A OG  1 
ATOM   5946 N N   . THR D 1 157 ? -66.678 -37.012 -69.508 1.00 160.01 ? 160 THR A N   1 
ATOM   5947 C CA  . THR D 1 157 ? -66.115 -38.372 -69.283 1.00 159.82 ? 160 THR A CA  1 
ATOM   5948 C C   . THR D 1 157 ? -64.655 -38.259 -68.832 1.00 162.52 ? 160 THR A C   1 
ATOM   5949 O O   . THR D 1 157 ? -63.780 -38.107 -69.707 1.00 177.39 ? 160 THR A O   1 
ATOM   5950 C CB  . THR D 1 157 ? -66.251 -39.270 -70.522 1.00 178.81 ? 160 THR A CB  1 
ATOM   5951 O OG1 . THR D 1 157 ? -65.321 -38.841 -71.517 1.00 199.06 ? 160 THR A OG1 1 
ATOM   5952 C CG2 . THR D 1 157 ? -67.651 -39.280 -71.098 1.00 187.35 ? 160 THR A CG2 1 
ATOM   5953 N N   . TYR D 1 158 ? -64.408 -38.318 -67.520 1.00 166.45 ? 161 TYR A N   1 
ATOM   5954 C CA  . TYR D 1 158 ? -63.011 -38.311 -67.013 1.00 163.98 ? 161 TYR A CA  1 
ATOM   5955 C C   . TYR D 1 158 ? -62.723 -39.677 -66.380 1.00 167.76 ? 161 TYR A C   1 
ATOM   5956 O O   . TYR D 1 158 ? -63.058 -39.879 -65.196 1.00 167.01 ? 161 TYR A O   1 
ATOM   5957 C CB  . TYR D 1 158 ? -62.793 -37.174 -66.012 1.00 156.42 ? 161 TYR A CB  1 
ATOM   5958 C CG  . TYR D 1 158 ? -61.370 -37.017 -65.536 1.00 155.58 ? 161 TYR A CG  1 
ATOM   5959 C CD1 . TYR D 1 158 ? -60.342 -37.769 -66.081 1.00 155.06 ? 161 TYR A CD1 1 
ATOM   5960 C CD2 . TYR D 1 158 ? -61.043 -36.104 -64.550 1.00 154.60 ? 161 TYR A CD2 1 
ATOM   5961 C CE1 . TYR D 1 158 ? -59.034 -37.634 -65.648 1.00 141.98 ? 161 TYR A CE1 1 
ATOM   5962 C CE2 . TYR D 1 158 ? -59.738 -35.954 -64.109 1.00 151.70 ? 161 TYR A CE2 1 
ATOM   5963 C CZ  . TYR D 1 158 ? -58.728 -36.719 -64.660 1.00 134.74 ? 161 TYR A CZ  1 
ATOM   5964 O OH  . TYR D 1 158 ? -57.433 -36.571 -64.226 1.00 128.17 ? 161 TYR A OH  1 
ATOM   5965 N N   . PRO D 1 159 ? -62.114 -40.626 -67.123 1.00 172.71 ? 162 PRO A N   1 
ATOM   5966 C CA  . PRO D 1 159 ? -61.838 -41.963 -66.595 1.00 158.90 ? 162 PRO A CA  1 
ATOM   5967 C C   . PRO D 1 159 ? -60.557 -41.999 -65.752 1.00 140.74 ? 162 PRO A C   1 
ATOM   5968 O O   . PRO D 1 159 ? -59.877 -40.991 -65.676 1.00 136.65 ? 162 PRO A O   1 
ATOM   5969 C CB  . PRO D 1 159 ? -61.633 -42.785 -67.874 1.00 167.76 ? 162 PRO A CB  1 
ATOM   5970 C CG  . PRO D 1 159 ? -61.024 -41.798 -68.845 1.00 179.25 ? 162 PRO A CG  1 
ATOM   5971 C CD  . PRO D 1 159 ? -61.675 -40.471 -68.513 1.00 175.41 ? 162 PRO A CD  1 
ATOM   5972 N N   . THR D 1 160 ? -60.264 -43.148 -65.140 1.00 138.27 ? 163 THR A N   1 
ATOM   5973 C CA  . THR D 1 160 ? -59.044 -43.284 -64.358 1.00 132.75 ? 163 THR A CA  1 
ATOM   5974 C C   . THR D 1 160 ? -57.899 -43.450 -65.340 1.00 129.43 ? 163 THR A C   1 
ATOM   5975 O O   . THR D 1 160 ? -57.899 -44.377 -66.156 1.00 130.51 ? 163 THR A O   1 
ATOM   5976 C CB  . THR D 1 160 ? -59.113 -44.502 -63.440 1.00 121.17 ? 163 THR A CB  1 
ATOM   5977 O OG1 . THR D 1 160 ? -59.291 -45.684 -64.230 1.00 134.94 ? 163 THR A OG1 1 
ATOM   5978 C CG2 . THR D 1 160 ? -60.267 -44.372 -62.468 1.00 143.88 ? 163 THR A CG2 1 
ATOM   5979 N N   . ILE D 1 161 ? -56.936 -42.543 -65.284 1.00 127.87 ? 164 ILE A N   1 
ATOM   5980 C CA  . ILE D 1 161 ? -55.879 -42.472 -66.281 1.00 121.57 ? 164 ILE A CA  1 
ATOM   5981 C C   . ILE D 1 161 ? -54.569 -42.842 -65.604 1.00 127.94 ? 164 ILE A C   1 
ATOM   5982 O O   . ILE D 1 161 ? -54.214 -42.279 -64.561 1.00 133.30 ? 164 ILE A O   1 
ATOM   5983 C CB  . ILE D 1 161 ? -55.835 -41.096 -66.960 1.00 125.49 ? 164 ILE A CB  1 
ATOM   5984 C CG1 . ILE D 1 161 ? -55.535 -40.035 -65.897 1.00 133.92 ? 164 ILE A CG1 1 
ATOM   5985 C CG2 . ILE D 1 161 ? -57.125 -40.834 -67.696 1.00 143.71 ? 164 ILE A CG2 1 
ATOM   5986 C CD1 . ILE D 1 161 ? -54.117 -39.586 -65.850 1.00 151.49 ? 164 ILE A CD1 1 
ATOM   5987 N N   . LYS D 1 162 ? -53.859 -43.790 -66.209 1.00 124.12 ? 165 LYS A N   1 
ATOM   5988 C CA  . LYS D 1 162 ? -52.651 -44.385 -65.658 1.00 127.04 ? 165 LYS A CA  1 
ATOM   5989 C C   . LYS D 1 162 ? -51.554 -44.203 -66.693 1.00 129.03 ? 165 LYS A C   1 
ATOM   5990 O O   . LYS D 1 162 ? -51.719 -44.617 -67.845 1.00 138.83 ? 165 LYS A O   1 
ATOM   5991 C CB  . LYS D 1 162 ? -52.889 -45.873 -65.411 1.00 139.37 ? 165 LYS A CB  1 
ATOM   5992 C CG  . LYS D 1 162 ? -53.900 -46.192 -64.335 1.00 156.13 ? 165 LYS A CG  1 
ATOM   5993 C CD  . LYS D 1 162 ? -54.104 -47.695 -64.233 1.00 164.64 ? 165 LYS A CD  1 
ATOM   5994 C CE  . LYS D 1 162 ? -55.110 -48.056 -63.153 1.00 162.53 ? 165 LYS A CE  1 
ATOM   5995 N NZ  . LYS D 1 162 ? -55.342 -49.526 -63.062 1.00 148.35 ? 165 LYS A NZ  1 
ATOM   5996 N N   . ARG D 1 163 ? -50.441 -43.594 -66.293 1.00 104.23 ? 166 ARG A N   1 
ATOM   5997 C CA  . ARG D 1 163 ? -49.323 -43.424 -67.211 1.00 110.36 ? 166 ARG A CA  1 
ATOM   5998 C C   . ARG D 1 163 ? -48.022 -43.478 -66.423 1.00 107.04 ? 166 ARG A C   1 
ATOM   5999 O O   . ARG D 1 163 ? -48.015 -43.365 -65.194 1.00 118.95 ? 166 ARG A O   1 
ATOM   6000 C CB  . ARG D 1 163 ? -49.433 -42.112 -68.002 1.00 133.78 ? 166 ARG A CB  1 
ATOM   6001 C CG  . ARG D 1 163 ? -50.244 -42.240 -69.283 1.00 142.95 ? 166 ARG A CG  1 
ATOM   6002 C CD  . ARG D 1 163 ? -51.267 -41.120 -69.434 1.00 175.80 ? 166 ARG A CD  1 
ATOM   6003 N NE  . ARG D 1 163 ? -52.303 -41.467 -70.402 1.00 183.30 ? 166 ARG A NE  1 
ATOM   6004 C CZ  . ARG D 1 163 ? -53.317 -40.681 -70.739 1.00 185.81 ? 166 ARG A CZ  1 
ATOM   6005 N NH1 . ARG D 1 163 ? -53.428 -39.451 -70.263 1.00 192.66 ? 166 ARG A NH1 1 
ATOM   6006 N NH2 . ARG D 1 163 ? -54.243 -41.140 -71.574 1.00 183.78 ? 166 ARG A NH2 1 
ATOM   6007 N N   . SER D 1 164 ? -46.916 -43.656 -67.145 1.00 101.70 ? 167 SER A N   1 
ATOM   6008 C CA  . SER D 1 164 ? -45.617 -43.785 -66.502 1.00 113.26 ? 167 SER A CA  1 
ATOM   6009 C C   . SER D 1 164 ? -44.517 -43.315 -67.445 1.00 141.63 ? 167 SER A C   1 
ATOM   6010 O O   . SER D 1 164 ? -44.662 -43.369 -68.669 1.00 163.47 ? 167 SER A O   1 
ATOM   6011 C CB  . SER D 1 164 ? -45.358 -45.229 -66.055 1.00 136.01 ? 167 SER A CB  1 
ATOM   6012 O OG  . SER D 1 164 ? -44.193 -45.322 -65.256 1.00 154.99 ? 167 SER A OG  1 
ATOM   6013 N N   . TYR D 1 165 ? -43.404 -42.860 -66.862 1.00 117.73 ? 168 TYR A N   1 
ATOM   6014 C CA  . TYR D 1 165 ? -42.257 -42.388 -67.681 1.00 113.06 ? 168 TYR A CA  1 
ATOM   6015 C C   . TYR D 1 165 ? -40.953 -42.896 -67.066 1.00 104.77 ? 168 TYR A C   1 
ATOM   6016 O O   . TYR D 1 165 ? -40.849 -42.922 -65.829 1.00 112.50 ? 168 TYR A O   1 
ATOM   6017 C CB  . TYR D 1 165 ? -42.227 -40.862 -67.749 1.00 118.61 ? 168 TYR A CB  1 
ATOM   6018 C CG  . TYR D 1 165 ? -40.909 -40.286 -68.200 1.00 171.76 ? 168 TYR A CG  1 
ATOM   6019 C CD1 . TYR D 1 165 ? -40.586 -40.217 -69.544 1.00 197.57 ? 168 TYR A CD1 1 
ATOM   6020 C CD2 . TYR D 1 165 ? -39.982 -39.812 -67.286 1.00 204.32 ? 168 TYR A CD2 1 
ATOM   6021 C CE1 . TYR D 1 165 ? -39.378 -39.691 -69.970 1.00 207.10 ? 168 TYR A CE1 1 
ATOM   6022 C CE2 . TYR D 1 165 ? -38.768 -39.289 -67.695 1.00 220.45 ? 168 TYR A CE2 1 
ATOM   6023 C CZ  . TYR D 1 165 ? -38.466 -39.223 -69.043 1.00 222.16 ? 168 TYR A CZ  1 
ATOM   6024 O OH  . TYR D 1 165 ? -37.266 -38.705 -69.461 1.00 231.04 ? 168 TYR A OH  1 
ATOM   6025 N N   . ASN D 1 166 ? -39.984 -43.252 -67.911 1.00 146.83 ? 169 ASN A N   1 
ATOM   6026 C CA  . ASN D 1 166 ? -38.679 -43.752 -67.412 1.00 142.36 ? 169 ASN A CA  1 
ATOM   6027 C C   . ASN D 1 166 ? -37.592 -42.711 -67.677 1.00 136.46 ? 169 ASN A C   1 
ATOM   6028 O O   . ASN D 1 166 ? -37.542 -42.210 -68.812 1.00 126.49 ? 169 ASN A O   1 
ATOM   6029 C CB  . ASN D 1 166 ? -38.287 -45.080 -68.061 1.00 144.43 ? 169 ASN A CB  1 
ATOM   6030 C CG  . ASN D 1 166 ? -37.033 -45.684 -67.466 1.00 169.53 ? 169 ASN A CG  1 
ATOM   6031 O OD1 . ASN D 1 166 ? -36.241 -44.986 -66.839 1.00 193.88 ? 169 ASN A OD1 1 
ATOM   6032 N ND2 . ASN D 1 166 ? -36.848 -46.979 -67.656 1.00 158.70 ? 169 ASN A ND2 1 
ATOM   6033 N N   . ASN D 1 167 ? -36.779 -42.387 -66.667 1.00 134.58 ? 170 ASN A N   1 
ATOM   6034 C CA  . ASN D 1 167 ? -35.629 -41.476 -66.905 1.00 133.21 ? 170 ASN A CA  1 
ATOM   6035 C C   . ASN D 1 167 ? -34.924 -42.495 -67.795 1.00 147.97 ? 170 ASN A C   1 
ATOM   6036 O O   . ASN D 1 167 ? -34.444 -43.509 -67.264 1.00 152.99 ? 170 ASN A O   1 
ATOM   6037 C CB  . ASN D 1 167 ? -34.963 -41.066 -65.593 1.00 137.66 ? 170 ASN A CB  1 
ATOM   6038 C CG  . ASN D 1 167 ? -34.324 -39.696 -65.646 1.00 171.87 ? 170 ASN A CG  1 
ATOM   6039 O OD1 . ASN D 1 167 ? -34.212 -39.097 -66.713 1.00 170.66 ? 170 ASN A OD1 1 
ATOM   6040 N ND2 . ASN D 1 167 ? -33.898 -39.194 -64.498 1.00 184.56 ? 170 ASN A ND2 1 
ATOM   6041 N N   . THR D 1 168 ? -34.861 -42.228 -69.099 1.00 160.48 ? 171 THR A N   1 
ATOM   6042 C CA  . THR D 1 168 ? -34.328 -43.218 -70.071 1.00 162.96 ? 171 THR A CA  1 
ATOM   6043 C C   . THR D 1 168 ? -33.039 -42.396 -70.126 1.00 156.42 ? 171 THR A C   1 
ATOM   6044 O O   . THR D 1 168 ? -31.954 -43.007 -70.191 1.00 164.04 ? 171 THR A O   1 
ATOM   6045 C CB  . THR D 1 168 ? -35.005 -43.293 -71.444 1.00 148.54 ? 171 THR A CB  1 
ATOM   6046 O OG1 . THR D 1 168 ? -35.207 -41.956 -71.905 1.00 163.23 ? 171 THR A OG1 1 
ATOM   6047 C CG2 . THR D 1 168 ? -36.327 -44.028 -71.409 1.00 121.07 ? 171 THR A CG2 1 
ATOM   6048 N N   . ASN D 1 169 ? -33.161 -41.066 -70.096 1.00 139.20 ? 172 ASN A N   1 
ATOM   6049 C CA  . ASN D 1 169 ? -31.980 -40.221 -70.147 1.00 139.67 ? 172 ASN A CA  1 
ATOM   6050 C C   . ASN D 1 169 ? -31.110 -40.457 -68.919 1.00 155.03 ? 172 ASN A C   1 
ATOM   6051 O O   . ASN D 1 169 ? -31.609 -40.538 -67.793 1.00 159.71 ? 172 ASN A O   1 
ATOM   6052 C CB  . ASN D 1 169 ? -32.384 -38.755 -70.241 1.00 135.61 ? 172 ASN A CB  1 
ATOM   6053 C CG  . ASN D 1 169 ? -31.217 -37.861 -70.586 1.00 158.16 ? 172 ASN A CG  1 
ATOM   6054 O OD1 . ASN D 1 169 ? -30.289 -38.270 -71.284 1.00 147.95 ? 172 ASN A OD1 1 
ATOM   6055 N ND2 . ASN D 1 169 ? -31.256 -36.629 -70.100 1.00 173.73 ? 172 ASN A ND2 1 
ATOM   6056 N N   . GLN D 1 170 ? -29.799 -40.556 -69.143 1.00 167.39 ? 173 GLN A N   1 
ATOM   6057 C CA  . GLN D 1 170 ? -28.860 -40.943 -68.096 1.00 168.28 ? 173 GLN A CA  1 
ATOM   6058 C C   . GLN D 1 170 ? -28.517 -39.621 -67.420 1.00 177.46 ? 173 GLN A C   1 
ATOM   6059 O O   . GLN D 1 170 ? -27.404 -39.106 -67.576 1.00 165.87 ? 173 GLN A O   1 
ATOM   6060 C CB  . GLN D 1 170 ? -27.603 -41.559 -68.715 1.00 161.75 ? 173 GLN A CB  1 
ATOM   6061 C CG  . GLN D 1 170 ? -27.817 -42.947 -69.303 1.00 148.58 ? 173 GLN A CG  1 
ATOM   6062 C CD  . GLN D 1 170 ? -28.685 -43.831 -68.426 1.00 160.16 ? 173 GLN A CD  1 
ATOM   6063 O OE1 . GLN D 1 170 ? -28.293 -44.209 -67.322 1.00 164.48 ? 173 GLN A OE1 1 
ATOM   6064 N NE2 . GLN D 1 170 ? -29.877 -44.158 -68.913 1.00 166.91 ? 173 GLN A NE2 1 
ATOM   6065 N N   . GLU D 1 171 ? -29.466 -39.066 -66.667 1.00 177.10 ? 174 GLU A N   1 
ATOM   6066 C CA  . GLU D 1 171 ? -29.271 -37.807 -65.963 1.00 161.10 ? 174 GLU A CA  1 
ATOM   6067 C C   . GLU D 1 171 ? -30.470 -37.650 -65.038 1.00 156.25 ? 174 GLU A C   1 
ATOM   6068 O O   . GLU D 1 171 ? -31.579 -38.096 -65.345 1.00 192.90 ? 174 GLU A O   1 
ATOM   6069 C CB  . GLU D 1 171 ? -29.067 -36.529 -66.790 1.00 145.63 ? 174 GLU A CB  1 
ATOM   6070 C CG  . GLU D 1 171 ? -27.784 -36.500 -67.609 1.00 153.10 ? 174 GLU A CG  1 
ATOM   6071 C CD  . GLU D 1 171 ? -27.671 -35.267 -68.485 1.00 154.63 ? 174 GLU A CD  1 
ATOM   6072 O OE1 . GLU D 1 171 ? -28.668 -34.526 -68.603 1.00 134.23 ? 174 GLU A OE1 1 
ATOM   6073 O OE2 . GLU D 1 171 ? -26.584 -35.040 -69.059 1.00 182.99 ? 174 GLU A OE2 1 
ATOM   6074 N N   . ASP D 1 172 ? -30.232 -37.004 -63.898 1.00 135.36 ? 175 ASP A N   1 
ATOM   6075 C CA  . ASP D 1 172 ? -31.311 -36.716 -62.964 1.00 140.29 ? 175 ASP A CA  1 
ATOM   6076 C C   . ASP D 1 172 ? -32.276 -35.705 -63.568 1.00 147.63 ? 175 ASP A C   1 
ATOM   6077 O O   . ASP D 1 172 ? -31.869 -34.781 -64.277 1.00 154.59 ? 175 ASP A O   1 
ATOM   6078 C CB  . ASP D 1 172 ? -30.750 -36.188 -61.648 1.00 128.14 ? 175 ASP A CB  1 
ATOM   6079 C CG  . ASP D 1 172 ? -30.064 -37.265 -60.842 1.00 141.94 ? 175 ASP A CG  1 
ATOM   6080 O OD1 . ASP D 1 172 ? -30.270 -38.456 -61.155 1.00 148.55 ? 175 ASP A OD1 1 
ATOM   6081 O OD2 . ASP D 1 172 ? -29.326 -36.924 -59.895 1.00 142.72 ? 175 ASP A OD2 1 
ATOM   6082 N N   . LEU D 1 173 ? -33.568 -35.879 -63.280 1.00 130.97 ? 176 LEU A N   1 
ATOM   6083 C CA  . LEU D 1 173 ? -34.619 -35.109 -63.950 1.00 126.08 ? 176 LEU A CA  1 
ATOM   6084 C C   . LEU D 1 173 ? -35.699 -34.753 -62.927 1.00 128.75 ? 176 LEU A C   1 
ATOM   6085 O O   . LEU D 1 173 ? -36.600 -35.549 -62.647 1.00 135.99 ? 176 LEU A O   1 
ATOM   6086 C CB  . LEU D 1 173 ? -35.171 -35.899 -65.132 1.00 129.91 ? 176 LEU A CB  1 
ATOM   6087 C CG  . LEU D 1 173 ? -36.441 -35.462 -65.855 1.00 143.01 ? 176 LEU A CG  1 
ATOM   6088 C CD1 . LEU D 1 173 ? -36.247 -34.098 -66.468 1.00 142.94 ? 176 LEU A CD1 1 
ATOM   6089 C CD2 . LEU D 1 173 ? -36.773 -36.474 -66.935 1.00 143.44 ? 176 LEU A CD2 1 
ATOM   6090 N N   . LEU D 1 174 ? -35.593 -33.545 -62.372 1.00 142.43 ? 177 LEU A N   1 
ATOM   6091 C CA  . LEU D 1 174 ? -36.583 -33.008 -61.447 1.00 130.81 ? 177 LEU A CA  1 
ATOM   6092 C C   . LEU D 1 174 ? -37.947 -32.913 -62.116 1.00 138.27 ? 177 LEU A C   1 
ATOM   6093 O O   . LEU D 1 174 ? -38.146 -32.070 -62.995 1.00 145.94 ? 177 LEU A O   1 
ATOM   6094 C CB  . LEU D 1 174 ? -36.156 -31.625 -60.959 1.00 109.17 ? 177 LEU A CB  1 
ATOM   6095 C CG  . LEU D 1 174 ? -37.103 -30.865 -60.031 1.00 115.93 ? 177 LEU A CG  1 
ATOM   6096 C CD1 . LEU D 1 174 ? -37.277 -31.633 -58.734 1.00 117.08 ? 177 LEU A CD1 1 
ATOM   6097 C CD2 . LEU D 1 174 ? -36.685 -29.422 -59.759 1.00 120.01 ? 177 LEU A CD2 1 
ATOM   6098 N N   . VAL D 1 175 ? -38.895 -33.747 -61.695 1.00 96.88  ? 178 VAL A N   1 
ATOM   6099 C CA  . VAL D 1 175 ? -40.228 -33.795 -62.285 1.00 118.39 ? 178 VAL A CA  1 
ATOM   6100 C C   . VAL D 1 175 ? -41.235 -33.303 -61.255 1.00 109.29 ? 178 VAL A C   1 
ATOM   6101 O O   . VAL D 1 175 ? -41.079 -33.550 -60.052 1.00 106.84 ? 178 VAL A O   1 
ATOM   6102 C CB  . VAL D 1 175 ? -40.573 -35.217 -62.769 1.00 135.06 ? 178 VAL A CB  1 
ATOM   6103 C CG1 . VAL D 1 175 ? -40.415 -36.204 -61.637 1.00 127.97 ? 178 VAL A CG1 1 
ATOM   6104 C CG2 . VAL D 1 175 ? -41.976 -35.273 -63.358 1.00 152.33 ? 178 VAL A CG2 1 
ATOM   6105 N N   . LEU D 1 176 ? -42.274 -32.613 -61.727 1.00 140.23 ? 179 LEU A N   1 
ATOM   6106 C CA  . LEU D 1 176 ? -43.181 -31.888 -60.849 1.00 118.94 ? 179 LEU A CA  1 
ATOM   6107 C C   . LEU D 1 176 ? -44.622 -32.105 -61.288 1.00 111.91 ? 179 LEU A C   1 
ATOM   6108 O O   . LEU D 1 176 ? -44.919 -32.120 -62.486 1.00 128.23 ? 179 LEU A O   1 
ATOM   6109 C CB  . LEU D 1 176 ? -42.863 -30.389 -60.861 1.00 132.02 ? 179 LEU A CB  1 
ATOM   6110 C CG  . LEU D 1 176 ? -41.504 -29.964 -60.297 1.00 132.78 ? 179 LEU A CG  1 
ATOM   6111 C CD1 . LEU D 1 176 ? -41.284 -28.474 -60.517 1.00 118.02 ? 179 LEU A CD1 1 
ATOM   6112 C CD2 . LEU D 1 176 ? -41.380 -30.311 -58.823 1.00 116.26 ? 179 LEU A CD2 1 
ATOM   6113 N N   . TRP D 1 177 ? -45.518 -32.249 -60.309 1.00 97.09  ? 180 TRP A N   1 
ATOM   6114 C CA  . TRP D 1 177 ? -46.950 -32.372 -60.559 1.00 104.19 ? 180 TRP A CA  1 
ATOM   6115 C C   . TRP D 1 177 ? -47.710 -31.613 -59.479 1.00 111.89 ? 180 TRP A C   1 
ATOM   6116 O O   . TRP D 1 177 ? -47.118 -30.972 -58.606 1.00 124.20 ? 180 TRP A O   1 
ATOM   6117 C CB  . TRP D 1 177 ? -47.387 -33.840 -60.615 1.00 109.11 ? 180 TRP A CB  1 
ATOM   6118 C CG  . TRP D 1 177 ? -47.568 -34.493 -59.282 1.00 123.48 ? 180 TRP A CG  1 
ATOM   6119 C CD1 . TRP D 1 177 ? -48.743 -34.700 -58.620 1.00 130.56 ? 180 TRP A CD1 1 
ATOM   6120 C CD2 . TRP D 1 177 ? -46.538 -35.050 -58.455 1.00 124.13 ? 180 TRP A CD2 1 
ATOM   6121 N NE1 . TRP D 1 177 ? -48.507 -35.342 -57.427 1.00 130.54 ? 180 TRP A NE1 1 
ATOM   6122 C CE2 . TRP D 1 177 ? -47.162 -35.570 -57.303 1.00 125.28 ? 180 TRP A CE2 1 
ATOM   6123 C CE3 . TRP D 1 177 ? -45.148 -35.155 -58.575 1.00 121.28 ? 180 TRP A CE3 1 
ATOM   6124 C CZ2 . TRP D 1 177 ? -46.443 -36.185 -56.278 1.00 140.09 ? 180 TRP A CZ2 1 
ATOM   6125 C CZ3 . TRP D 1 177 ? -44.438 -35.764 -57.557 1.00 112.66 ? 180 TRP A CZ3 1 
ATOM   6126 C CH2 . TRP D 1 177 ? -45.086 -36.270 -56.424 1.00 143.78 ? 180 TRP A CH2 1 
ATOM   6127 N N   . GLY D 1 178 ? -49.040 -31.689 -59.543 1.00 107.05 ? 181 GLY A N   1 
ATOM   6128 C CA  . GLY D 1 178 ? -49.879 -30.981 -58.591 1.00 120.09 ? 181 GLY A CA  1 
ATOM   6129 C C   . GLY D 1 178 ? -51.235 -31.634 -58.437 1.00 106.73 ? 181 GLY A C   1 
ATOM   6130 O O   . GLY D 1 178 ? -51.590 -32.574 -59.152 1.00 100.89 ? 181 GLY A O   1 
ATOM   6131 N N   . ILE D 1 179 ? -51.998 -31.109 -57.477 1.00 108.30 ? 182 ILE A N   1 
ATOM   6132 C CA  . ILE D 1 179 ? -53.325 -31.608 -57.129 1.00 108.49 ? 182 ILE A CA  1 
ATOM   6133 C C   . ILE D 1 179 ? -54.257 -30.413 -57.000 1.00 132.90 ? 182 ILE A C   1 
ATOM   6134 O O   . ILE D 1 179 ? -53.909 -29.428 -56.344 1.00 129.25 ? 182 ILE A O   1 
ATOM   6135 C CB  . ILE D 1 179 ? -53.307 -32.399 -55.807 1.00 133.77 ? 182 ILE A CB  1 
ATOM   6136 C CG1 . ILE D 1 179 ? -52.323 -33.571 -55.879 1.00 131.51 ? 182 ILE A CG1 1 
ATOM   6137 C CG2 . ILE D 1 179 ? -54.709 -32.881 -55.467 1.00 149.15 ? 182 ILE A CG2 1 
ATOM   6138 C CD1 . ILE D 1 179 ? -52.343 -34.472 -54.657 1.00 137.13 ? 182 ILE A CD1 1 
ATOM   6139 N N   . HIS D 1 180 ? -55.445 -30.501 -57.599 1.00 131.98 ? 183 HIS A N   1 
ATOM   6140 C CA  . HIS D 1 180 ? -56.426 -29.422 -57.525 1.00 138.20 ? 183 HIS A CA  1 
ATOM   6141 C C   . HIS D 1 180 ? -57.357 -29.651 -56.337 1.00 152.62 ? 183 HIS A C   1 
ATOM   6142 O O   . HIS D 1 180 ? -58.048 -30.673 -56.271 1.00 156.25 ? 183 HIS A O   1 
ATOM   6143 C CB  . HIS D 1 180 ? -57.229 -29.316 -58.823 1.00 128.93 ? 183 HIS A CB  1 
ATOM   6144 C CG  . HIS D 1 180 ? -58.399 -28.383 -58.740 1.00 131.54 ? 183 HIS A CG  1 
ATOM   6145 N ND1 . HIS D 1 180 ? -58.288 -27.084 -58.291 1.00 101.29 ? 183 HIS A ND1 1 
ATOM   6146 C CD2 . HIS D 1 180 ? -59.704 -28.559 -59.058 1.00 158.68 ? 183 HIS A CD2 1 
ATOM   6147 C CE1 . HIS D 1 180 ? -59.474 -26.503 -58.331 1.00 132.23 ? 183 HIS A CE1 1 
ATOM   6148 N NE2 . HIS D 1 180 ? -60.351 -27.376 -58.793 1.00 166.97 ? 183 HIS A NE2 1 
ATOM   6149 N N   . HIS D 1 181 ? -57.373 -28.696 -55.400 1.00 174.35 ? 184 HIS A N   1 
ATOM   6150 C CA  . HIS D 1 181 ? -58.240 -28.753 -54.232 1.00 159.54 ? 184 HIS A CA  1 
ATOM   6151 C C   . HIS D 1 181 ? -59.384 -27.761 -54.414 1.00 151.19 ? 184 HIS A C   1 
ATOM   6152 O O   . HIS D 1 181 ? -59.219 -26.572 -54.103 1.00 142.74 ? 184 HIS A O   1 
ATOM   6153 C CB  . HIS D 1 181 ? -57.460 -28.439 -52.950 1.00 158.37 ? 184 HIS A CB  1 
ATOM   6154 C CG  . HIS D 1 181 ? -56.284 -29.337 -52.705 1.00 156.90 ? 184 HIS A CG  1 
ATOM   6155 N ND1 . HIS D 1 181 ? -56.215 -30.196 -51.630 1.00 152.12 ? 184 HIS A ND1 1 
ATOM   6156 C CD2 . HIS D 1 181 ? -55.123 -29.495 -53.385 1.00 172.07 ? 184 HIS A CD2 1 
ATOM   6157 C CE1 . HIS D 1 181 ? -55.067 -30.846 -51.658 1.00 163.59 ? 184 HIS A CE1 1 
ATOM   6158 N NE2 . HIS D 1 181 ? -54.386 -30.441 -52.715 1.00 172.74 ? 184 HIS A NE2 1 
ATOM   6159 N N   . PRO D 1 182 ? -60.589 -28.183 -54.876 1.00 134.55 ? 185 PRO A N   1 
ATOM   6160 C CA  . PRO D 1 182 ? -61.720 -27.263 -55.017 1.00 152.29 ? 185 PRO A CA  1 
ATOM   6161 C C   . PRO D 1 182 ? -62.325 -26.879 -53.659 1.00 195.80 ? 185 PRO A C   1 
ATOM   6162 O O   . PRO D 1 182 ? -61.858 -27.369 -52.647 1.00 208.51 ? 185 PRO A O   1 
ATOM   6163 C CB  . PRO D 1 182 ? -62.747 -28.063 -55.831 1.00 154.08 ? 185 PRO A CB  1 
ATOM   6164 C CG  . PRO D 1 182 ? -62.476 -29.493 -55.443 1.00 155.21 ? 185 PRO A CG  1 
ATOM   6165 C CD  . PRO D 1 182 ? -60.973 -29.553 -55.266 1.00 142.60 ? 185 PRO A CD  1 
ATOM   6166 N N   . ASN D 1 183 ? -63.341 -26.011 -53.673 1.00 170.39 ? 186 ASN A N   1 
ATOM   6167 C CA  . ASN D 1 183 ? -64.000 -25.577 -52.413 1.00 196.71 ? 186 ASN A CA  1 
ATOM   6168 C C   . ASN D 1 183 ? -65.474 -25.990 -52.459 1.00 200.27 ? 186 ASN A C   1 
ATOM   6169 O O   . ASN D 1 183 ? -66.097 -26.072 -51.383 1.00 212.69 ? 186 ASN A O   1 
ATOM   6170 C CB  . ASN D 1 183 ? -63.836 -24.072 -52.191 1.00 199.58 ? 186 ASN A CB  1 
ATOM   6171 C CG  . ASN D 1 183 ? -63.859 -23.677 -50.729 1.00 197.24 ? 186 ASN A CG  1 
ATOM   6172 O OD1 . ASN D 1 183 ? -63.982 -24.528 -49.852 1.00 204.67 ? 186 ASN A OD1 1 
ATOM   6173 N ND2 . ASN D 1 183 ? -63.731 -22.388 -50.459 1.00 193.23 ? 186 ASN A ND2 1 
ATOM   6174 N N   . ASP D 1 184 ? -66.003 -26.247 -53.660 1.00 218.92 ? 187 ASP A N   1 
ATOM   6175 C CA  . ASP D 1 184 ? -67.452 -26.637 -53.833 1.00 208.86 ? 187 ASP A CA  1 
ATOM   6176 C C   . ASP D 1 184 ? -67.463 -28.010 -54.485 1.00 183.74 ? 187 ASP A C   1 
ATOM   6177 O O   . ASP D 1 184 ? -66.402 -28.453 -54.967 1.00 179.36 ? 187 ASP A O   1 
ATOM   6178 C CB  . ASP D 1 184 ? -68.227 -25.516 -54.500 1.00 209.13 ? 187 ASP A CB  1 
ATOM   6179 C CG  . ASP D 1 184 ? -69.732 -25.723 -54.482 1.00 206.47 ? 187 ASP A CG  1 
ATOM   6180 O OD1 . ASP D 1 184 ? -70.183 -26.720 -53.885 1.00 211.39 ? 187 ASP A OD1 1 
ATOM   6181 O OD2 . ASP D 1 184 ? -70.442 -24.885 -55.072 1.00 204.46 ? 187 ASP A OD2 1 
ATOM   6182 N N   . ALA D 1 185 ? -68.631 -28.661 -54.513 1.00 176.98 ? 188 ALA A N   1 
ATOM   6183 C CA  . ALA D 1 185 ? -68.753 -29.950 -55.211 1.00 162.80 ? 188 ALA A CA  1 
ATOM   6184 C C   . ALA D 1 185 ? -69.009 -29.621 -56.653 1.00 174.61 ? 188 ALA A C   1 
ATOM   6185 O O   . ALA D 1 185 ? -68.607 -30.373 -57.548 1.00 180.70 ? 188 ALA A O   1 
ATOM   6186 C CB  . ALA D 1 185 ? -69.860 -30.806 -54.621 1.00 155.53 ? 188 ALA A CB  1 
ATOM   6187 N N   . ALA D 1 186 ? -69.701 -28.507 -56.879 1.00 163.74 ? 189 ALA A N   1 
ATOM   6188 C CA  . ALA D 1 186 ? -69.941 -28.084 -58.272 1.00 168.93 ? 189 ALA A CA  1 
ATOM   6189 C C   . ALA D 1 186 ? -68.574 -27.938 -58.934 1.00 168.58 ? 189 ALA A C   1 
ATOM   6190 O O   . ALA D 1 186 ? -68.381 -28.486 -60.032 1.00 176.00 ? 189 ALA A O   1 
ATOM   6191 C CB  . ALA D 1 186 ? -70.705 -26.791 -58.293 1.00 173.01 ? 189 ALA A CB  1 
ATOM   6192 N N   . GLU D 1 187 ? -67.651 -27.262 -58.249 1.00 177.17 ? 190 GLU A N   1 
ATOM   6193 C CA  . GLU D 1 187 ? -66.317 -27.023 -58.851 1.00 182.81 ? 190 GLU A CA  1 
ATOM   6194 C C   . GLU D 1 187 ? -65.763 -28.372 -59.308 1.00 178.37 ? 190 GLU A C   1 
ATOM   6195 O O   . GLU D 1 187 ? -65.374 -28.485 -60.481 1.00 176.85 ? 190 GLU A O   1 
ATOM   6196 C CB  . GLU D 1 187 ? -65.382 -26.362 -57.840 1.00 198.67 ? 190 GLU A CB  1 
ATOM   6197 C CG  . GLU D 1 187 ? -64.253 -25.587 -58.489 1.00 199.41 ? 190 GLU A CG  1 
ATOM   6198 C CD  . GLU D 1 187 ? -64.729 -24.437 -59.359 1.00 219.71 ? 190 GLU A CD  1 
ATOM   6199 O OE1 . GLU D 1 187 ? -65.411 -23.539 -58.826 1.00 214.07 ? 190 GLU A OE1 1 
ATOM   6200 O OE2 . GLU D 1 187 ? -64.421 -24.444 -60.567 1.00 226.43 ? 190 GLU A OE2 1 
ATOM   6201 N N   . GLN D 1 188 ? -65.767 -29.359 -58.414 1.00 178.73 ? 191 GLN A N   1 
ATOM   6202 C CA  . GLN D 1 188 ? -65.211 -30.685 -58.771 1.00 161.92 ? 191 GLN A CA  1 
ATOM   6203 C C   . GLN D 1 188 ? -66.042 -31.242 -59.924 1.00 159.38 ? 191 GLN A C   1 
ATOM   6204 O O   . GLN D 1 188 ? -65.461 -31.529 -60.971 1.00 174.75 ? 191 GLN A O   1 
ATOM   6205 C CB  . GLN D 1 188 ? -65.239 -31.631 -57.574 1.00 155.74 ? 191 GLN A CB  1 
ATOM   6206 C CG  . GLN D 1 188 ? -64.340 -32.848 -57.738 1.00 144.38 ? 191 GLN A CG  1 
ATOM   6207 C CD  . GLN D 1 188 ? -64.335 -33.709 -56.499 1.00 162.62 ? 191 GLN A CD  1 
ATOM   6208 O OE1 . GLN D 1 188 ? -65.032 -33.435 -55.526 1.00 188.52 ? 191 GLN A OE1 1 
ATOM   6209 N NE2 . GLN D 1 188 ? -63.547 -34.770 -56.529 1.00 136.11 ? 191 GLN A NE2 1 
ATOM   6210 N N   . THR D 1 189 ? -67.360 -31.311 -59.755 1.00 156.11 ? 192 THR A N   1 
ATOM   6211 C CA  . THR D 1 189 ? -68.208 -31.926 -60.807 1.00 160.61 ? 192 THR A CA  1 
ATOM   6212 C C   . THR D 1 189 ? -67.888 -31.268 -62.151 1.00 162.44 ? 192 THR A C   1 
ATOM   6213 O O   . THR D 1 189 ? -67.662 -32.002 -63.130 1.00 127.31 ? 192 THR A O   1 
ATOM   6214 C CB  . THR D 1 189 ? -69.692 -31.789 -60.458 1.00 158.59 ? 192 THR A CB  1 
ATOM   6215 O OG1 . THR D 1 189 ? -69.858 -32.203 -59.102 1.00 182.79 ? 192 THR A OG1 1 
ATOM   6216 C CG2 . THR D 1 189 ? -70.587 -32.606 -61.363 1.00 127.75 ? 192 THR A CG2 1 
ATOM   6217 N N   . LYS D 1 190 ? -67.851 -29.936 -62.185 1.00 147.42 ? 193 LYS A N   1 
ATOM   6218 C CA  . LYS D 1 190 ? -67.599 -29.211 -63.456 1.00 150.78 ? 193 LYS A CA  1 
ATOM   6219 C C   . LYS D 1 190 ? -66.189 -29.520 -63.957 1.00 140.73 ? 193 LYS A C   1 
ATOM   6220 O O   . LYS D 1 190 ? -66.026 -29.657 -65.180 1.00 137.01 ? 193 LYS A O   1 
ATOM   6221 C CB  . LYS D 1 190 ? -67.721 -27.702 -63.243 1.00 167.19 ? 193 LYS A CB  1 
ATOM   6222 C CG  . LYS D 1 190 ? -69.082 -27.205 -62.776 1.00 151.60 ? 193 LYS A CG  1 
ATOM   6223 C CD  . LYS D 1 190 ? -69.074 -25.735 -62.417 1.00 141.21 ? 193 LYS A CD  1 
ATOM   6224 C CE  . LYS D 1 190 ? -70.421 -25.227 -61.950 1.00 138.89 ? 193 LYS A CE  1 
ATOM   6225 N NZ  . LYS D 1 190 ? -70.392 -23.770 -61.679 1.00 135.61 ? 193 LYS A NZ  1 
ATOM   6226 N N   . LEU D 1 191 ? -65.214 -29.627 -63.053 1.00 166.95 ? 194 LEU A N   1 
ATOM   6227 C CA  . LEU D 1 191 ? -63.805 -29.801 -63.497 1.00 149.33 ? 194 LEU A CA  1 
ATOM   6228 C C   . LEU D 1 191 ? -63.406 -31.280 -63.521 1.00 131.71 ? 194 LEU A C   1 
ATOM   6229 O O   . LEU D 1 191 ? -62.466 -31.591 -64.250 1.00 130.29 ? 194 LEU A O   1 
ATOM   6230 C CB  . LEU D 1 191 ? -62.895 -29.010 -62.556 1.00 156.23 ? 194 LEU A CB  1 
ATOM   6231 C CG  . LEU D 1 191 ? -63.086 -27.495 -62.585 1.00 174.91 ? 194 LEU A CG  1 
ATOM   6232 C CD1 . LEU D 1 191 ? -61.957 -26.794 -61.847 1.00 189.96 ? 194 LEU A CD1 1 
ATOM   6233 C CD2 . LEU D 1 191 ? -63.178 -26.991 -64.016 1.00 146.71 ? 194 LEU A CD2 1 
ATOM   6234 N N   . TYR D 1 192 ? -64.075 -32.140 -62.750 1.00 152.34 ? 195 TYR A N   1 
ATOM   6235 C CA  . TYR D 1 192 ? -63.724 -33.584 -62.674 1.00 145.62 ? 195 TYR A CA  1 
ATOM   6236 C C   . TYR D 1 192 ? -64.987 -34.384 -62.339 1.00 180.13 ? 195 TYR A C   1 
ATOM   6237 O O   . TYR D 1 192 ? -65.481 -34.252 -61.204 1.00 202.10 ? 195 TYR A O   1 
ATOM   6238 C CB  . TYR D 1 192 ? -62.645 -33.792 -61.610 1.00 151.10 ? 195 TYR A CB  1 
ATOM   6239 C CG  . TYR D 1 192 ? -61.412 -32.947 -61.801 1.00 151.28 ? 195 TYR A CG  1 
ATOM   6240 C CD1 . TYR D 1 192 ? -60.482 -33.250 -62.782 1.00 165.33 ? 195 TYR A CD1 1 
ATOM   6241 C CD2 . TYR D 1 192 ? -61.201 -31.812 -61.037 1.00 141.19 ? 195 TYR A CD2 1 
ATOM   6242 C CE1 . TYR D 1 192 ? -59.357 -32.467 -62.976 1.00 165.43 ? 195 TYR A CE1 1 
ATOM   6243 C CE2 . TYR D 1 192 ? -60.085 -31.014 -61.224 1.00 160.63 ? 195 TYR A CE2 1 
ATOM   6244 C CZ  . TYR D 1 192 ? -59.157 -31.344 -62.195 1.00 168.35 ? 195 TYR A CZ  1 
ATOM   6245 O OH  . TYR D 1 192 ? -58.044 -30.562 -62.382 1.00 165.25 ? 195 TYR A OH  1 
ATOM   6246 N N   . GLN D 1 193 ? -65.550 -35.083 -63.329 1.00 153.41 ? 196 GLN A N   1 
ATOM   6247 C CA  . GLN D 1 193 ? -66.840 -35.797 -63.120 1.00 162.99 ? 196 GLN A CA  1 
ATOM   6248 C C   . GLN D 1 193 ? -66.993 -36.772 -61.952 1.00 155.30 ? 196 GLN A C   1 
ATOM   6249 O O   . GLN D 1 193 ? -67.997 -36.673 -61.222 1.00 160.37 ? 196 GLN A O   1 
ATOM   6250 C CB  . GLN D 1 193 ? -67.169 -36.683 -64.321 1.00 154.46 ? 196 GLN A CB  1 
ATOM   6251 C CG  . GLN D 1 193 ? -68.197 -36.076 -65.263 1.00 153.61 ? 196 GLN A CG  1 
ATOM   6252 C CD  . GLN D 1 193 ? -69.565 -35.995 -64.632 1.00 156.72 ? 196 GLN A CD  1 
ATOM   6253 O OE1 . GLN D 1 193 ? -70.137 -37.000 -64.216 1.00 149.13 ? 196 GLN A OE1 1 
ATOM   6254 N NE2 . GLN D 1 193 ? -70.102 -34.789 -64.553 1.00 162.24 ? 196 GLN A NE2 1 
ATOM   6255 N N   . ASN D 1 194 ? -66.035 -37.684 -61.803 1.00 169.61 ? 197 ASN A N   1 
ATOM   6256 C CA  . ASN D 1 194 ? -66.096 -38.620 -60.650 1.00 161.87 ? 197 ASN A CA  1 
ATOM   6257 C C   . ASN D 1 194 ? -65.887 -37.656 -59.483 1.00 165.98 ? 197 ASN A C   1 
ATOM   6258 O O   . ASN D 1 194 ? -64.921 -36.876 -59.537 1.00 174.87 ? 197 ASN A O   1 
ATOM   6259 C CB  . ASN D 1 194 ? -65.015 -39.695 -60.770 1.00 170.38 ? 197 ASN A CB  1 
ATOM   6260 C CG  . ASN D 1 194 ? -65.208 -40.604 -61.966 1.00 151.82 ? 197 ASN A CG  1 
ATOM   6261 O OD1 . ASN D 1 194 ? -64.268 -40.851 -62.718 1.00 107.05 ? 197 ASN A OD1 1 
ATOM   6262 N ND2 . ASN D 1 194 ? -66.415 -41.112 -62.149 1.00 173.98 ? 197 ASN A ND2 1 
ATOM   6263 N N   . PRO D 1 195 ? -66.747 -37.635 -58.431 1.00 161.21 ? 198 PRO A N   1 
ATOM   6264 C CA  . PRO D 1 195 ? -66.510 -36.779 -57.262 1.00 173.83 ? 198 PRO A CA  1 
ATOM   6265 C C   . PRO D 1 195 ? -65.544 -37.416 -56.253 1.00 165.42 ? 198 PRO A C   1 
ATOM   6266 O O   . PRO D 1 195 ? -64.803 -36.687 -55.624 1.00 163.09 ? 198 PRO A O   1 
ATOM   6267 C CB  . PRO D 1 195 ? -67.937 -36.735 -56.702 1.00 157.93 ? 198 PRO A CB  1 
ATOM   6268 C CG  . PRO D 1 195 ? -68.529 -38.072 -57.089 1.00 138.28 ? 198 PRO A CG  1 
ATOM   6269 C CD  . PRO D 1 195 ? -67.852 -38.454 -58.391 1.00 129.29 ? 198 PRO A CD  1 
ATOM   6270 N N   . THR D 1 196 ? -65.581 -38.744 -56.108 1.00 147.27 ? 199 THR A N   1 
ATOM   6271 C CA  . THR D 1 196 ? -64.608 -39.437 -55.222 1.00 151.72 ? 199 THR A CA  1 
ATOM   6272 C C   . THR D 1 196 ? -63.379 -39.771 -56.069 1.00 160.18 ? 199 THR A C   1 
ATOM   6273 O O   . THR D 1 196 ? -63.482 -40.688 -56.908 1.00 173.23 ? 199 THR A O   1 
ATOM   6274 C CB  . THR D 1 196 ? -65.233 -40.681 -54.579 1.00 157.92 ? 199 THR A CB  1 
ATOM   6275 O OG1 . THR D 1 196 ? -65.598 -41.584 -55.623 1.00 169.71 ? 199 THR A OG1 1 
ATOM   6276 C CG2 . THR D 1 196 ? -66.447 -40.358 -53.737 1.00 173.76 ? 199 THR A CG2 1 
ATOM   6277 N N   . THR D 1 197 ? -62.270 -39.052 -55.873 1.00 137.39 ? 200 THR A N   1 
ATOM   6278 C CA  . THR D 1 197 ? -61.097 -39.263 -56.764 1.00 144.75 ? 200 THR A CA  1 
ATOM   6279 C C   . THR D 1 197 ? -59.840 -39.617 -55.968 1.00 139.83 ? 200 THR A C   1 
ATOM   6280 O O   . THR D 1 197 ? -59.957 -39.849 -54.749 1.00 146.93 ? 200 THR A O   1 
ATOM   6281 C CB  . THR D 1 197 ? -60.826 -38.021 -57.623 1.00 156.54 ? 200 THR A CB  1 
ATOM   6282 O OG1 . THR D 1 197 ? -60.041 -37.104 -56.861 1.00 140.14 ? 200 THR A OG1 1 
ATOM   6283 C CG2 . THR D 1 197 ? -62.093 -37.342 -58.094 1.00 159.97 ? 200 THR A CG2 1 
ATOM   6284 N N   . TYR D 1 198 ? -58.688 -39.641 -56.643 1.00 135.18 ? 201 TYR A N   1 
ATOM   6285 C CA  . TYR D 1 198 ? -57.416 -39.984 -56.016 1.00 133.54 ? 201 TYR A CA  1 
ATOM   6286 C C   . TYR D 1 198 ? -56.423 -39.585 -57.099 1.00 138.95 ? 201 TYR A C   1 
ATOM   6287 O O   . TYR D 1 198 ? -56.792 -39.354 -58.251 1.00 138.89 ? 201 TYR A O   1 
ATOM   6288 C CB  . TYR D 1 198 ? -57.317 -41.484 -55.705 1.00 149.33 ? 201 TYR A CB  1 
ATOM   6289 C CG  . TYR D 1 198 ? -57.373 -42.380 -56.926 1.00 154.83 ? 201 TYR A CG  1 
ATOM   6290 C CD1 . TYR D 1 198 ? -58.589 -42.761 -57.480 1.00 150.91 ? 201 TYR A CD1 1 
ATOM   6291 C CD2 . TYR D 1 198 ? -56.209 -42.832 -57.533 1.00 157.42 ? 201 TYR A CD2 1 
ATOM   6292 C CE1 . TYR D 1 198 ? -58.641 -43.583 -58.592 1.00 151.03 ? 201 TYR A CE1 1 
ATOM   6293 C CE2 . TYR D 1 198 ? -56.254 -43.645 -58.648 1.00 175.43 ? 201 TYR A CE2 1 
ATOM   6294 C CZ  . TYR D 1 198 ? -57.472 -44.016 -59.176 1.00 175.61 ? 201 TYR A CZ  1 
ATOM   6295 O OH  . TYR D 1 198 ? -57.522 -44.827 -60.287 1.00 180.06 ? 201 TYR A OH  1 
ATOM   6296 N N   . ILE D 1 199 ? -55.147 -39.515 -56.707 1.00 151.33 ? 202 ILE A N   1 
ATOM   6297 C CA  . ILE D 1 199 ? -54.010 -39.331 -57.599 1.00 155.39 ? 202 ILE A CA  1 
ATOM   6298 C C   . ILE D 1 199 ? -53.004 -40.287 -56.937 1.00 170.18 ? 202 ILE A C   1 
ATOM   6299 O O   . ILE D 1 199 ? -52.601 -40.086 -55.786 1.00 175.50 ? 202 ILE A O   1 
ATOM   6300 C CB  . ILE D 1 199 ? -53.540 -37.862 -57.634 1.00 148.96 ? 202 ILE A CB  1 
ATOM   6301 C CG1 . ILE D 1 199 ? -53.049 -37.387 -56.268 1.00 138.48 ? 202 ILE A CG1 1 
ATOM   6302 C CG2 . ILE D 1 199 ? -54.670 -36.958 -58.110 1.00 145.56 ? 202 ILE A CG2 1 
ATOM   6303 C CD1 . ILE D 1 199 ? -51.566 -37.392 -56.129 1.00 151.08 ? 202 ILE A CD1 1 
ATOM   6304 N N   . SER D 1 200 ? -52.700 -41.394 -57.608 1.00 174.19 ? 203 SER A N   1 
ATOM   6305 C CA  . SER D 1 200 ? -51.904 -42.449 -56.984 1.00 172.93 ? 203 SER A CA  1 
ATOM   6306 C C   . SER D 1 200 ? -50.623 -42.201 -57.778 1.00 159.75 ? 203 SER A C   1 
ATOM   6307 O O   . SER D 1 200 ? -50.621 -42.279 -59.010 1.00 160.37 ? 203 SER A O   1 
ATOM   6308 C CB  . SER D 1 200 ? -52.488 -43.823 -57.303 1.00 184.64 ? 203 SER A CB  1 
ATOM   6309 O OG  . SER D 1 200 ? -51.489 -44.826 -57.245 1.00 194.66 ? 203 SER A OG  1 
ATOM   6310 N N   . VAL D 1 201 ? -49.531 -41.916 -57.064 1.00 142.72 ? 204 VAL A N   1 
ATOM   6311 C CA  . VAL D 1 201 ? -48.211 -41.708 -57.727 1.00 143.06 ? 204 VAL A CA  1 
ATOM   6312 C C   . VAL D 1 201 ? -47.323 -42.902 -57.374 1.00 157.71 ? 204 VAL A C   1 
ATOM   6313 O O   . VAL D 1 201 ? -47.533 -43.477 -56.294 1.00 173.86 ? 204 VAL A O   1 
ATOM   6314 C CB  . VAL D 1 201 ? -47.565 -40.394 -57.261 1.00 149.33 ? 204 VAL A CB  1 
ATOM   6315 C CG1 . VAL D 1 201 ? -46.219 -40.146 -57.923 1.00 142.33 ? 204 VAL A CG1 1 
ATOM   6316 C CG2 . VAL D 1 201 ? -48.495 -39.207 -57.455 1.00 153.63 ? 204 VAL A CG2 1 
ATOM   6317 N N   . GLY D 1 202 ? -46.376 -43.259 -58.246 1.00 153.21 ? 205 GLY A N   1 
ATOM   6318 C CA  . GLY D 1 202 ? -45.535 -44.446 -57.994 1.00 162.44 ? 205 GLY A CA  1 
ATOM   6319 C C   . GLY D 1 202 ? -44.155 -44.334 -58.619 1.00 148.20 ? 205 GLY A C   1 
ATOM   6320 O O   . GLY D 1 202 ? -44.059 -44.418 -59.853 1.00 143.04 ? 205 GLY A O   1 
ATOM   6321 N N   . THR D 1 203 ? -43.120 -44.175 -57.791 1.00 159.57 ? 206 THR A N   1 
ATOM   6322 C CA  . THR D 1 203 ? -41.738 -44.031 -58.311 1.00 165.64 ? 206 THR A CA  1 
ATOM   6323 C C   . THR D 1 203 ? -40.865 -45.161 -57.776 1.00 156.85 ? 206 THR A C   1 
ATOM   6324 O O   . THR D 1 203 ? -41.420 -46.194 -57.364 1.00 140.11 ? 206 THR A O   1 
ATOM   6325 C CB  . THR D 1 203 ? -41.104 -42.706 -57.880 1.00 166.05 ? 206 THR A CB  1 
ATOM   6326 O OG1 . THR D 1 203 ? -41.095 -42.671 -56.452 1.00 143.50 ? 206 THR A OG1 1 
ATOM   6327 C CG2 . THR D 1 203 ? -41.826 -41.498 -58.434 1.00 172.49 ? 206 THR A CG2 1 
ATOM   6328 N N   . SER D 1 204 ? -39.548 -44.958 -57.785 1.00 156.46 ? 207 SER A N   1 
ATOM   6329 C CA  . SER D 1 204 ? -38.644 -45.973 -57.197 1.00 157.67 ? 207 SER A CA  1 
ATOM   6330 C C   . SER D 1 204 ? -39.096 -46.226 -55.765 1.00 156.37 ? 207 SER A C   1 
ATOM   6331 O O   . SER D 1 204 ? -39.336 -47.393 -55.411 1.00 157.79 ? 207 SER A O   1 
ATOM   6332 C CB  . SER D 1 204 ? -37.232 -45.482 -57.192 1.00 151.41 ? 207 SER A CB  1 
ATOM   6333 O OG  . SER D 1 204 ? -36.376 -46.420 -56.561 1.00 162.13 ? 207 SER A OG  1 
ATOM   6334 N N   . THR D 1 205 ? -39.218 -45.152 -54.988 1.00 156.85 ? 208 THR A N   1 
ATOM   6335 C CA  . THR D 1 205 ? -39.585 -45.297 -53.562 1.00 150.45 ? 208 THR A CA  1 
ATOM   6336 C C   . THR D 1 205 ? -40.819 -44.445 -53.286 1.00 144.98 ? 208 THR A C   1 
ATOM   6337 O O   . THR D 1 205 ? -41.643 -44.853 -52.450 1.00 152.93 ? 208 THR A O   1 
ATOM   6338 C CB  . THR D 1 205 ? -38.421 -44.836 -52.683 1.00 155.32 ? 208 THR A CB  1 
ATOM   6339 O OG1 . THR D 1 205 ? -38.197 -43.456 -52.968 1.00 128.32 ? 208 THR A OG1 1 
ATOM   6340 C CG2 . THR D 1 205 ? -37.150 -45.619 -52.927 1.00 151.58 ? 208 THR A CG2 1 
ATOM   6341 N N   . LEU D 1 206 ? -40.936 -43.312 -53.976 1.00 135.67 ? 209 LEU A N   1 
ATOM   6342 C CA  . LEU D 1 206 ? -42.058 -42.385 -53.686 1.00 141.39 ? 209 LEU A CA  1 
ATOM   6343 C C   . LEU D 1 206 ? -43.343 -42.920 -54.314 1.00 159.96 ? 209 LEU A C   1 
ATOM   6344 O O   . LEU D 1 206 ? -43.826 -42.303 -55.277 1.00 168.41 ? 209 LEU A O   1 
ATOM   6345 C CB  . LEU D 1 206 ? -41.710 -40.997 -54.227 1.00 143.04 ? 209 LEU A CB  1 
ATOM   6346 C CG  . LEU D 1 206 ? -40.560 -40.295 -53.508 1.00 160.23 ? 209 LEU A CG  1 
ATOM   6347 C CD1 . LEU D 1 206 ? -40.665 -38.786 -53.662 1.00 138.87 ? 209 LEU A CD1 1 
ATOM   6348 C CD2 . LEU D 1 206 ? -40.528 -40.677 -52.036 1.00 157.18 ? 209 LEU A CD2 1 
ATOM   6349 N N   . ASN D 1 207 ? -43.864 -44.031 -53.793 1.00 159.52 ? 210 ASN A N   1 
ATOM   6350 C CA  . ASN D 1 207 ? -45.154 -44.520 -54.279 1.00 176.15 ? 210 ASN A CA  1 
ATOM   6351 C C   . ASN D 1 207 ? -46.260 -43.772 -53.533 1.00 171.80 ? 210 ASN A C   1 
ATOM   6352 O O   . ASN D 1 207 ? -46.955 -44.302 -52.664 1.00 151.58 ? 210 ASN A O   1 
ATOM   6353 C CB  . ASN D 1 207 ? -45.253 -46.030 -54.096 1.00 177.78 ? 210 ASN A CB  1 
ATOM   6354 C CG  . ASN D 1 207 ? -44.330 -46.800 -55.031 1.00 164.09 ? 210 ASN A CG  1 
ATOM   6355 O OD1 . ASN D 1 207 ? -43.916 -46.298 -56.076 1.00 165.21 ? 210 ASN A OD1 1 
ATOM   6356 N ND2 . ASN D 1 207 ? -44.002 -48.029 -54.650 1.00 155.14 ? 210 ASN A ND2 1 
ATOM   6357 N N   . GLN D 1 208 ? -46.403 -42.498 -53.898 1.00 170.47 ? 211 GLN A N   1 
ATOM   6358 C CA  . GLN D 1 208 ? -47.156 -41.517 -53.115 1.00 164.27 ? 211 GLN A CA  1 
ATOM   6359 C C   . GLN D 1 208 ? -48.604 -41.492 -53.590 1.00 169.90 ? 211 GLN A C   1 
ATOM   6360 O O   . GLN D 1 208 ? -48.995 -40.668 -54.415 1.00 212.69 ? 211 GLN A O   1 
ATOM   6361 C CB  . GLN D 1 208 ? -46.496 -40.147 -53.243 1.00 159.11 ? 211 GLN A CB  1 
ATOM   6362 C CG  . GLN D 1 208 ? -47.043 -39.067 -52.337 1.00 147.50 ? 211 GLN A CG  1 
ATOM   6363 C CD  . GLN D 1 208 ? -46.253 -37.771 -52.429 1.00 150.55 ? 211 GLN A CD  1 
ATOM   6364 O OE1 . GLN D 1 208 ? -45.236 -37.691 -53.121 1.00 147.99 ? 211 GLN A OE1 1 
ATOM   6365 N NE2 . GLN D 1 208 ? -46.724 -36.746 -51.732 1.00 177.88 ? 211 GLN A NE2 1 
ATOM   6366 N N   . ARG D 1 209 ? -49.421 -42.395 -53.050 1.00 169.46 ? 212 ARG A N   1 
ATOM   6367 C CA  . ARG D 1 209 ? -50.841 -42.459 -53.403 1.00 177.30 ? 212 ARG A CA  1 
ATOM   6368 C C   . ARG D 1 209 ? -51.572 -41.378 -52.607 1.00 170.23 ? 212 ARG A C   1 
ATOM   6369 O O   . ARG D 1 209 ? -51.843 -41.543 -51.416 1.00 140.79 ? 212 ARG A O   1 
ATOM   6370 C CB  . ARG D 1 209 ? -51.410 -43.837 -53.080 1.00 191.40 ? 212 ARG A CB  1 
ATOM   6371 C CG  . ARG D 1 209 ? -50.833 -44.972 -53.928 1.00 189.17 ? 212 ARG A CG  1 
ATOM   6372 C CD  . ARG D 1 209 ? -51.512 -46.303 -53.623 1.00 185.66 ? 212 ARG A CD  1 
ATOM   6373 N NE  . ARG D 1 209 ? -50.913 -47.413 -54.357 1.00 170.20 ? 212 ARG A NE  1 
ATOM   6374 C CZ  . ARG D 1 209 ? -51.258 -48.685 -54.203 1.00 172.74 ? 212 ARG A CZ  1 
ATOM   6375 N NH1 . ARG D 1 209 ? -52.201 -49.046 -53.349 1.00 180.71 ? 212 ARG A NH1 1 
ATOM   6376 N NH2 . ARG D 1 209 ? -50.640 -49.617 -54.924 1.00 162.85 ? 212 ARG A NH2 1 
ATOM   6377 N N   . LEU D 1 210 ? -51.910 -40.276 -53.274 1.00 163.13 ? 213 LEU A N   1 
ATOM   6378 C CA  . LEU D 1 210 ? -52.466 -39.088 -52.641 1.00 157.82 ? 213 LEU A CA  1 
ATOM   6379 C C   . LEU D 1 210 ? -53.947 -38.937 -52.964 1.00 155.13 ? 213 LEU A C   1 
ATOM   6380 O O   . LEU D 1 210 ? -54.518 -39.667 -53.780 1.00 179.52 ? 213 LEU A O   1 
ATOM   6381 C CB  . LEU D 1 210 ? -51.689 -37.838 -53.055 1.00 161.45 ? 213 LEU A CB  1 
ATOM   6382 C CG  . LEU D 1 210 ? -50.236 -37.775 -52.587 1.00 175.01 ? 213 LEU A CG  1 
ATOM   6383 C CD1 . LEU D 1 210 ? -49.516 -36.574 -53.169 1.00 162.71 ? 213 LEU A CD1 1 
ATOM   6384 C CD2 . LEU D 1 210 ? -50.193 -37.736 -51.071 1.00 168.67 ? 213 LEU A CD2 1 
ATOM   6385 N N   . VAL D 1 211 ? -54.569 -37.960 -52.308 1.00 149.25 ? 214 VAL A N   1 
ATOM   6386 C CA  . VAL D 1 211 ? -55.997 -37.674 -52.425 1.00 139.92 ? 214 VAL A CA  1 
ATOM   6387 C C   . VAL D 1 211 ? -56.201 -36.155 -52.426 1.00 142.30 ? 214 VAL A C   1 
ATOM   6388 O O   . VAL D 1 211 ? -55.472 -35.437 -51.725 1.00 161.03 ? 214 VAL A O   1 
ATOM   6389 C CB  . VAL D 1 211 ? -56.742 -38.342 -51.249 1.00 131.92 ? 214 VAL A CB  1 
ATOM   6390 C CG1 . VAL D 1 211 ? -58.212 -37.946 -51.226 1.00 95.95  ? 214 VAL A CG1 1 
ATOM   6391 C CG2 . VAL D 1 211 ? -56.643 -39.859 -51.336 1.00 155.14 ? 214 VAL A CG2 1 
ATOM   6392 N N   . PRO D 1 212 ? -57.176 -35.609 -53.193 1.00 133.47 ? 215 PRO A N   1 
ATOM   6393 C CA  . PRO D 1 212 ? -57.454 -34.169 -53.105 1.00 151.77 ? 215 PRO A CA  1 
ATOM   6394 C C   . PRO D 1 212 ? -58.277 -33.971 -51.842 1.00 141.43 ? 215 PRO A C   1 
ATOM   6395 O O   . PRO D 1 212 ? -58.427 -34.892 -51.035 1.00 128.00 ? 215 PRO A O   1 
ATOM   6396 C CB  . PRO D 1 212 ? -58.253 -33.883 -54.382 1.00 152.45 ? 215 PRO A CB  1 
ATOM   6397 C CG  . PRO D 1 212 ? -58.976 -35.135 -54.637 1.00 133.85 ? 215 PRO A CG  1 
ATOM   6398 C CD  . PRO D 1 212 ? -57.987 -36.231 -54.257 1.00 126.87 ? 215 PRO A CD  1 
ATOM   6399 N N   . ARG D 1 213 ? -58.726 -32.746 -51.597 1.00 152.57 ? 216 ARG A N   1 
ATOM   6400 C CA  . ARG D 1 213 ? -59.508 -32.478 -50.385 1.00 153.22 ? 216 ARG A CA  1 
ATOM   6401 C C   . ARG D 1 213 ? -60.335 -31.313 -50.904 1.00 158.92 ? 216 ARG A C   1 
ATOM   6402 O O   . ARG D 1 213 ? -59.759 -30.461 -51.601 1.00 183.19 ? 216 ARG A O   1 
ATOM   6403 C CB  . ARG D 1 213 ? -58.609 -32.318 -49.158 1.00 156.87 ? 216 ARG A CB  1 
ATOM   6404 C CG  . ARG D 1 213 ? -59.361 -32.149 -47.845 1.00 141.18 ? 216 ARG A CG  1 
ATOM   6405 C CD  . ARG D 1 213 ? -58.375 -32.000 -46.704 1.00 151.41 ? 216 ARG A CD  1 
ATOM   6406 N NE  . ARG D 1 213 ? -57.600 -30.775 -46.837 1.00 181.52 ? 216 ARG A NE  1 
ATOM   6407 C CZ  . ARG D 1 213 ? -56.332 -30.725 -47.228 1.00 198.11 ? 216 ARG A CZ  1 
ATOM   6408 N NH1 . ARG D 1 213 ? -55.581 -31.812 -47.181 1.00 211.03 ? 216 ARG A NH1 1 
ATOM   6409 N NH2 . ARG D 1 213 ? -55.816 -29.586 -47.656 1.00 204.49 ? 216 ARG A NH2 1 
ATOM   6410 N N   . ILE D 1 214 ? -61.641 -31.280 -50.622 1.00 142.83 ? 217 ILE A N   1 
ATOM   6411 C CA  . ILE D 1 214 ? -62.565 -30.293 -51.239 1.00 174.66 ? 217 ILE A CA  1 
ATOM   6412 C C   . ILE D 1 214 ? -62.767 -29.244 -50.098 1.00 191.88 ? 217 ILE A C   1 
ATOM   6413 O O   . ILE D 1 214 ? -63.809 -29.342 -49.425 1.00 205.63 ? 217 ILE A O   1 
ATOM   6414 C CB  . ILE D 1 214 ? -63.872 -30.934 -51.632 1.00 182.40 ? 217 ILE A CB  1 
ATOM   6415 C CG1 . ILE D 1 214 ? -63.685 -31.910 -52.796 1.00 164.40 ? 217 ILE A CG1 1 
ATOM   6416 C CG2 . ILE D 1 214 ? -64.903 -29.868 -51.962 1.00 182.07 ? 217 ILE A CG2 1 
ATOM   6417 C CD1 . ILE D 1 214 ? -64.893 -32.775 -53.065 1.00 149.46 ? 217 ILE A CD1 1 
ATOM   6418 N N   . ALA D 1 215 ? -61.797 -28.354 -49.862 1.00 180.20 ? 218 ALA A N   1 
ATOM   6419 C CA  . ALA D 1 215 ? -61.917 -27.401 -48.730 1.00 202.86 ? 218 ALA A CA  1 
ATOM   6420 C C   . ALA D 1 215 ? -60.851 -26.308 -48.837 1.00 245.76 ? 218 ALA A C   1 
ATOM   6421 O O   . ALA D 1 215 ? -59.653 -26.645 -48.762 1.00 252.51 ? 218 ALA A O   1 
ATOM   6422 C CB  . ALA D 1 215 ? -61.796 -28.143 -47.421 1.00 183.92 ? 218 ALA A CB  1 
ATOM   6423 N N   . THR D 1 216 ? -61.274 -25.050 -49.001 1.00 254.31 ? 219 THR A N   1 
ATOM   6424 C CA  . THR D 1 216 ? -60.314 -23.918 -49.099 1.00 253.96 ? 219 THR A CA  1 
ATOM   6425 C C   . THR D 1 216 ? -60.888 -22.690 -48.386 1.00 239.13 ? 219 THR A C   1 
ATOM   6426 O O   . THR D 1 216 ? -61.767 -22.870 -47.521 1.00 235.26 ? 219 THR A O   1 
ATOM   6427 C CB  . THR D 1 216 ? -59.997 -23.578 -50.560 1.00 256.85 ? 219 THR A CB  1 
ATOM   6428 O OG1 . THR D 1 216 ? -61.047 -22.745 -51.048 1.00 268.80 ? 219 THR A OG1 1 
ATOM   6429 C CG2 . THR D 1 216 ? -59.856 -24.800 -51.441 1.00 264.66 ? 219 THR A CG2 1 
ATOM   6430 N N   . ARG D 1 217 ? -60.410 -21.493 -48.745 1.00 269.37 ? 220 ARG A N   1 
ATOM   6431 C CA  . ARG D 1 217 ? -60.926 -20.182 -48.135 1.00 229.76 ? 220 ARG A CA  1 
ATOM   6432 C C   . ARG D 1 217 ? -61.500 -19.406 -49.263 1.00 231.98 ? 220 ARG A C   1 
ATOM   6433 O O   . ARG D 1 217 ? -61.885 -20.005 -50.284 1.00 248.36 ? 220 ARG A O   1 
ATOM   6434 C CB  . ARG D 1 217 ? -59.744 -19.435 -47.530 1.00 199.91 ? 220 ARG A CB  1 
ATOM   6435 C CG  . ARG D 1 217 ? -59.119 -20.070 -46.296 1.00 203.54 ? 220 ARG A CG  1 
ATOM   6436 C CD  . ARG D 1 217 ? -57.899 -19.311 -45.812 1.00 175.75 ? 220 ARG A CD  1 
ATOM   6437 N NE  . ARG D 1 217 ? -57.267 -19.969 -44.677 1.00 190.52 ? 220 ARG A NE  1 
ATOM   6438 C CZ  . ARG D 1 217 ? -56.181 -19.522 -44.057 1.00 192.18 ? 220 ARG A CZ  1 
ATOM   6439 N NH1 . ARG D 1 217 ? -55.677 -20.195 -43.039 1.00 194.85 ? 220 ARG A NH1 1 
ATOM   6440 N NH2 . ARG D 1 217 ? -55.602 -18.403 -44.459 1.00 167.81 ? 220 ARG A NH2 1 
ATOM   6441 N N   . SER D 1 218 ? -61.574 -18.083 -49.087 1.00 244.47 ? 221 SER A N   1 
ATOM   6442 C CA  . SER D 1 218 ? -62.175 -17.134 -50.138 1.00 249.06 ? 221 SER A CA  1 
ATOM   6443 C C   . SER D 1 218 ? -61.452 -17.215 -51.485 1.00 255.19 ? 221 SER A C   1 
ATOM   6444 O O   . SER D 1 218 ? -60.330 -17.754 -51.561 1.00 253.17 ? 221 SER A O   1 
ATOM   6445 C CB  . SER D 1 218 ? -62.240 -15.787 -49.583 1.00 228.56 ? 221 SER A CB  1 
ATOM   6446 O OG  . SER D 1 218 ? -60.943 -15.239 -49.404 1.00 189.71 ? 221 SER A OG  1 
ATOM   6447 N N   . LYS D 1 219 ? -62.090 -16.647 -52.513 1.00 250.69 ? 222 LYS A N   1 
ATOM   6448 C CA  . LYS D 1 219 ? -61.496 -16.628 -53.878 1.00 249.83 ? 222 LYS A CA  1 
ATOM   6449 C C   . LYS D 1 219 ? -60.183 -15.841 -53.860 1.00 248.31 ? 222 LYS A C   1 
ATOM   6450 O O   . LYS D 1 219 ? -60.243 -14.600 -53.767 1.00 245.37 ? 222 LYS A O   1 
ATOM   6451 C CB  . LYS D 1 219 ? -62.471 -16.012 -54.886 1.00 242.71 ? 222 LYS A CB  1 
ATOM   6452 C CG  . LYS D 1 219 ? -63.686 -16.864 -55.221 1.00 222.70 ? 222 LYS A CG  1 
ATOM   6453 C CD  . LYS D 1 219 ? -64.469 -16.343 -56.405 1.00 186.40 ? 222 LYS A CD  1 
ATOM   6454 C CE  . LYS D 1 219 ? -65.621 -17.245 -56.794 1.00 179.83 ? 222 LYS A CE  1 
ATOM   6455 N NZ  . LYS D 1 219 ? -66.353 -16.722 -57.972 1.00 183.19 ? 222 LYS A NZ  1 
ATOM   6456 N N   . VAL D 1 220 ? -59.046 -16.537 -53.953 1.00 242.90 ? 223 VAL A N   1 
ATOM   6457 C CA  . VAL D 1 220 ? -57.731 -15.837 -54.020 1.00 242.46 ? 223 VAL A CA  1 
ATOM   6458 C C   . VAL D 1 220 ? -57.466 -15.514 -55.492 1.00 261.65 ? 223 VAL A C   1 
ATOM   6459 O O   . VAL D 1 220 ? -57.467 -16.456 -56.309 1.00 268.62 ? 223 VAL A O   1 
ATOM   6460 C CB  . VAL D 1 220 ? -56.605 -16.700 -53.421 1.00 217.56 ? 223 VAL A CB  1 
ATOM   6461 C CG1 . VAL D 1 220 ? -55.264 -15.983 -53.458 1.00 190.44 ? 223 VAL A CG1 1 
ATOM   6462 C CG2 . VAL D 1 220 ? -56.936 -17.154 -52.008 1.00 197.27 ? 223 VAL A CG2 1 
ATOM   6463 N N   . ASN D 1 221 ? -57.282 -14.232 -55.818 1.00 235.15 ? 224 ASN A N   1 
ATOM   6464 C CA  . ASN D 1 221 ? -57.076 -13.822 -57.232 1.00 245.26 ? 224 ASN A CA  1 
ATOM   6465 C C   . ASN D 1 221 ? -58.231 -14.369 -58.076 1.00 261.84 ? 224 ASN A C   1 
ATOM   6466 O O   . ASN D 1 221 ? -57.972 -14.802 -59.214 1.00 272.78 ? 224 ASN A O   1 
ATOM   6467 C CB  . ASN D 1 221 ? -55.714 -14.267 -57.771 1.00 239.60 ? 224 ASN A CB  1 
ATOM   6468 C CG  . ASN D 1 221 ? -55.248 -13.425 -58.939 1.00 231.59 ? 224 ASN A CG  1 
ATOM   6469 O OD1 . ASN D 1 221 ? -55.022 -13.939 -60.032 1.00 244.90 ? 224 ASN A OD1 1 
ATOM   6470 N ND2 . ASN D 1 221 ? -55.106 -12.128 -58.718 1.00 219.81 ? 224 ASN A ND2 1 
ATOM   6471 N N   . GLY D 1 222 ? -59.451 -14.368 -57.530 1.00 248.89 ? 225 GLY A N   1 
ATOM   6472 C CA  . GLY D 1 222 ? -60.630 -14.791 -58.312 1.00 234.49 ? 225 GLY A CA  1 
ATOM   6473 C C   . GLY D 1 222 ? -60.852 -16.294 -58.307 1.00 227.14 ? 225 GLY A C   1 
ATOM   6474 O O   . GLY D 1 222 ? -61.774 -16.745 -59.014 1.00 222.50 ? 225 GLY A O   1 
ATOM   6475 N N   . GLN D 1 223 ? -60.044 -17.052 -57.561 1.00 242.66 ? 226 GLN A N   1 
ATOM   6476 C CA  . GLN D 1 223 ? -60.252 -18.525 -57.475 1.00 231.69 ? 226 GLN A CA  1 
ATOM   6477 C C   . GLN D 1 223 ? -60.220 -18.972 -56.009 1.00 221.56 ? 226 GLN A C   1 
ATOM   6478 O O   . GLN D 1 223 ? -59.151 -18.851 -55.378 1.00 223.55 ? 226 GLN A O   1 
ATOM   6479 C CB  . GLN D 1 223 ? -59.222 -19.261 -58.335 1.00 220.55 ? 226 GLN A CB  1 
ATOM   6480 C CG  . GLN D 1 223 ? -59.296 -18.892 -59.809 1.00 204.79 ? 226 GLN A CG  1 
ATOM   6481 C CD  . GLN D 1 223 ? -58.358 -19.688 -60.684 1.00 204.24 ? 226 GLN A CD  1 
ATOM   6482 O OE1 . GLN D 1 223 ? -58.267 -19.462 -61.888 1.00 205.48 ? 226 GLN A OE1 1 
ATOM   6483 N NE2 . GLN D 1 223 ? -57.647 -20.626 -60.082 1.00 197.93 ? 226 GLN A NE2 1 
ATOM   6484 N N   . SER D 1 224 ? -61.348 -19.476 -55.498 1.00 220.29 ? 227 SER A N   1 
ATOM   6485 C CA  . SER D 1 224 ? -61.441 -19.876 -54.069 1.00 223.14 ? 227 SER A CA  1 
ATOM   6486 C C   . SER D 1 224 ? -60.667 -21.170 -53.802 1.00 224.04 ? 227 SER A C   1 
ATOM   6487 O O   . SER D 1 224 ? -60.117 -21.285 -52.694 1.00 227.01 ? 227 SER A O   1 
ATOM   6488 C CB  . SER D 1 224 ? -62.880 -20.022 -53.644 1.00 230.16 ? 227 SER A CB  1 
ATOM   6489 O OG  . SER D 1 224 ? -62.964 -20.424 -52.285 1.00 252.76 ? 227 SER A OG  1 
ATOM   6490 N N   . GLY D 1 225 ? -60.622 -22.094 -54.768 1.00 229.71 ? 228 GLY A N   1 
ATOM   6491 C CA  . GLY D 1 225 ? -59.985 -23.411 -54.551 1.00 204.69 ? 228 GLY A CA  1 
ATOM   6492 C C   . GLY D 1 225 ? -58.465 -23.366 -54.524 1.00 182.93 ? 228 GLY A C   1 
ATOM   6493 O O   . GLY D 1 225 ? -57.893 -22.307 -54.850 1.00 186.20 ? 228 GLY A O   1 
ATOM   6494 N N   . ARG D 1 226 ? -57.818 -24.466 -54.127 1.00 190.93 ? 229 ARG A N   1 
ATOM   6495 C CA  . ARG D 1 226 ? -56.335 -24.471 -53.990 1.00 189.34 ? 229 ARG A CA  1 
ATOM   6496 C C   . ARG D 1 226 ? -55.717 -25.461 -54.983 1.00 171.47 ? 229 ARG A C   1 
ATOM   6497 O O   . ARG D 1 226 ? -56.465 -26.298 -55.522 1.00 176.78 ? 229 ARG A O   1 
ATOM   6498 C CB  . ARG D 1 226 ? -55.934 -24.826 -52.555 1.00 195.79 ? 229 ARG A CB  1 
ATOM   6499 C CG  . ARG D 1 226 ? -56.344 -23.785 -51.524 1.00 207.36 ? 229 ARG A CG  1 
ATOM   6500 C CD  . ARG D 1 226 ? -56.244 -24.314 -50.107 1.00 199.99 ? 229 ARG A CD  1 
ATOM   6501 N NE  . ARG D 1 226 ? -56.800 -23.379 -49.139 1.00 185.01 ? 229 ARG A NE  1 
ATOM   6502 C CZ  . ARG D 1 226 ? -56.888 -23.610 -47.835 1.00 210.41 ? 229 ARG A CZ  1 
ATOM   6503 N NH1 . ARG D 1 226 ? -56.487 -24.767 -47.340 1.00 216.55 ? 229 ARG A NH1 1 
ATOM   6504 N NH2 . ARG D 1 226 ? -57.383 -22.685 -47.031 1.00 228.18 ? 229 ARG A NH2 1 
ATOM   6505 N N   . MET D 1 227 ? -54.406 -25.353 -55.219 1.00 161.41 ? 230 MET A N   1 
ATOM   6506 C CA  . MET D 1 227 ? -53.703 -26.289 -56.139 1.00 166.77 ? 230 MET A CA  1 
ATOM   6507 C C   . MET D 1 227 ? -52.290 -26.544 -55.605 1.00 179.99 ? 230 MET A C   1 
ATOM   6508 O O   . MET D 1 227 ? -51.345 -25.912 -56.116 1.00 195.98 ? 230 MET A O   1 
ATOM   6509 C CB  . MET D 1 227 ? -53.611 -25.711 -57.554 1.00 167.73 ? 230 MET A CB  1 
ATOM   6510 C CG  . MET D 1 227 ? -54.856 -25.948 -58.389 1.00 166.02 ? 230 MET A CG  1 
ATOM   6511 S SD  . MET D 1 227 ? -54.833 -25.018 -59.943 1.00 175.67 ? 230 MET A SD  1 
ATOM   6512 C CE  . MET D 1 227 ? -56.564 -24.576 -60.087 1.00 190.18 ? 230 MET A CE  1 
ATOM   6513 N N   . GLU D 1 228 ? -52.158 -27.427 -54.611 1.00 154.93 ? 231 GLU A N   1 
ATOM   6514 C CA  . GLU D 1 228 ? -50.822 -27.764 -54.051 1.00 169.27 ? 231 GLU A CA  1 
ATOM   6515 C C   . GLU D 1 228 ? -49.994 -28.470 -55.129 1.00 150.16 ? 231 GLU A C   1 
ATOM   6516 O O   . GLU D 1 228 ? -50.531 -29.395 -55.768 1.00 156.67 ? 231 GLU A O   1 
ATOM   6517 C CB  . GLU D 1 228 ? -50.969 -28.663 -52.824 1.00 172.90 ? 231 GLU A CB  1 
ATOM   6518 C CG  . GLU D 1 228 ? -51.863 -28.076 -51.748 1.00 192.38 ? 231 GLU A CG  1 
ATOM   6519 C CD  . GLU D 1 228 ? -52.105 -29.010 -50.576 1.00 208.64 ? 231 GLU A CD  1 
ATOM   6520 O OE1 . GLU D 1 228 ? -51.561 -30.132 -50.597 1.00 202.29 ? 231 GLU A OE1 1 
ATOM   6521 O OE2 . GLU D 1 228 ? -52.838 -28.615 -49.648 1.00 226.77 ? 231 GLU A OE2 1 
ATOM   6522 N N   . PHE D 1 229 ? -48.737 -28.053 -55.315 1.00 150.76 ? 232 PHE A N   1 
ATOM   6523 C CA  . PHE D 1 229 ? -47.889 -28.694 -56.310 1.00 143.94 ? 232 PHE A CA  1 
ATOM   6524 C C   . PHE D 1 229 ? -46.819 -29.543 -55.629 1.00 140.64 ? 232 PHE A C   1 
ATOM   6525 O O   . PHE D 1 229 ? -46.533 -29.390 -54.438 1.00 143.59 ? 232 PHE A O   1 
ATOM   6526 C CB  . PHE D 1 229 ? -47.240 -27.655 -57.231 1.00 152.66 ? 232 PHE A CB  1 
ATOM   6527 C CG  . PHE D 1 229 ? -48.075 -27.309 -58.435 1.00 153.37 ? 232 PHE A CG  1 
ATOM   6528 C CD1 . PHE D 1 229 ? -49.071 -26.349 -58.349 1.00 148.66 ? 232 PHE A CD1 1 
ATOM   6529 C CD2 . PHE D 1 229 ? -47.877 -27.953 -59.646 1.00 158.93 ? 232 PHE A CD2 1 
ATOM   6530 C CE1 . PHE D 1 229 ? -49.848 -26.030 -59.449 1.00 152.95 ? 232 PHE A CE1 1 
ATOM   6531 C CE2 . PHE D 1 229 ? -48.652 -27.639 -60.750 1.00 159.78 ? 232 PHE A CE2 1 
ATOM   6532 C CZ  . PHE D 1 229 ? -49.638 -26.676 -60.651 1.00 157.64 ? 232 PHE A CZ  1 
ATOM   6533 N N   . PHE D 1 230 ? -46.235 -30.457 -56.401 1.00 141.89 ? 233 PHE A N   1 
ATOM   6534 C CA  . PHE D 1 230 ? -45.287 -31.425 -55.871 1.00 124.34 ? 233 PHE A CA  1 
ATOM   6535 C C   . PHE D 1 230 ? -44.031 -31.460 -56.725 1.00 130.09 ? 233 PHE A C   1 
ATOM   6536 O O   . PHE D 1 230 ? -43.916 -30.785 -57.751 1.00 152.55 ? 233 PHE A O   1 
ATOM   6537 C CB  . PHE D 1 230 ? -45.890 -32.833 -55.800 1.00 125.04 ? 233 PHE A CB  1 
ATOM   6538 C CG  . PHE D 1 230 ? -47.000 -32.966 -54.811 1.00 126.77 ? 233 PHE A CG  1 
ATOM   6539 C CD1 . PHE D 1 230 ? -48.252 -32.436 -55.072 1.00 124.69 ? 233 PHE A CD1 1 
ATOM   6540 C CD2 . PHE D 1 230 ? -46.785 -33.609 -53.607 1.00 125.39 ? 233 PHE A CD2 1 
ATOM   6541 C CE1 . PHE D 1 230 ? -49.271 -32.557 -54.153 1.00 133.03 ? 233 PHE A CE1 1 
ATOM   6542 C CE2 . PHE D 1 230 ? -47.796 -33.732 -52.685 1.00 133.66 ? 233 PHE A CE2 1 
ATOM   6543 C CZ  . PHE D 1 230 ? -49.044 -33.207 -52.958 1.00 139.54 ? 233 PHE A CZ  1 
ATOM   6544 N N   . TRP D 1 231 ? -43.092 -32.286 -56.284 1.00 113.28 ? 234 TRP A N   1 
ATOM   6545 C CA  . TRP D 1 231 ? -41.813 -32.464 -56.951 1.00 150.19 ? 234 TRP A CA  1 
ATOM   6546 C C   . TRP D 1 231 ? -41.247 -33.792 -56.479 1.00 149.22 ? 234 TRP A C   1 
ATOM   6547 O O   . TRP D 1 231 ? -41.701 -34.359 -55.481 1.00 119.04 ? 234 TRP A O   1 
ATOM   6548 C CB  . TRP D 1 231 ? -40.852 -31.315 -56.635 1.00 145.37 ? 234 TRP A CB  1 
ATOM   6549 C CG  . TRP D 1 231 ? -40.486 -31.270 -55.184 1.00 130.03 ? 234 TRP A CG  1 
ATOM   6550 C CD1 . TRP D 1 231 ? -41.056 -30.494 -54.223 1.00 146.53 ? 234 TRP A CD1 1 
ATOM   6551 C CD2 . TRP D 1 231 ? -39.465 -32.035 -54.528 1.00 140.37 ? 234 TRP A CD2 1 
ATOM   6552 N NE1 . TRP D 1 231 ? -40.460 -30.731 -53.008 1.00 150.58 ? 234 TRP A NE1 1 
ATOM   6553 C CE2 . TRP D 1 231 ? -39.479 -31.674 -53.171 1.00 148.61 ? 234 TRP A CE2 1 
ATOM   6554 C CE3 . TRP D 1 231 ? -38.537 -32.984 -54.959 1.00 142.87 ? 234 TRP A CE3 1 
ATOM   6555 C CZ2 . TRP D 1 231 ? -38.602 -32.233 -52.245 1.00 155.74 ? 234 TRP A CZ2 1 
ATOM   6556 C CZ3 . TRP D 1 231 ? -37.686 -33.548 -54.040 1.00 150.92 ? 234 TRP A CZ3 1 
ATOM   6557 C CH2 . TRP D 1 231 ? -37.722 -33.171 -52.698 1.00 147.79 ? 234 TRP A CH2 1 
ATOM   6558 N N   . THR D 1 232 ? -40.230 -34.268 -57.201 1.00 152.29 ? 235 THR A N   1 
ATOM   6559 C CA  . THR D 1 232 ? -39.496 -35.464 -56.813 1.00 125.33 ? 235 THR A CA  1 
ATOM   6560 C C   . THR D 1 232 ? -38.215 -35.407 -57.650 1.00 149.44 ? 235 THR A C   1 
ATOM   6561 O O   . THR D 1 232 ? -38.245 -35.222 -58.873 1.00 172.08 ? 235 THR A O   1 
ATOM   6562 C CB  . THR D 1 232 ? -40.409 -36.685 -56.893 1.00 132.61 ? 235 THR A CB  1 
ATOM   6563 O OG1 . THR D 1 232 ? -40.918 -36.847 -58.223 1.00 182.75 ? 235 THR A OG1 1 
ATOM   6564 C CG2 . THR D 1 232 ? -41.506 -36.632 -55.822 1.00 117.66 ? 235 THR A CG2 1 
ATOM   6565 N N   . ILE D 1 233 ? -37.076 -35.662 -57.010 1.00 161.40 ? 236 ILE A N   1 
ATOM   6566 C CA  . ILE D 1 233 ? -35.826 -35.748 -57.818 1.00 184.73 ? 236 ILE A CA  1 
ATOM   6567 C C   . ILE D 1 233 ? -35.955 -37.180 -58.336 1.00 184.09 ? 236 ILE A C   1 
ATOM   6568 O O   . ILE D 1 233 ? -36.358 -38.057 -57.549 1.00 153.29 ? 236 ILE A O   1 
ATOM   6569 C CB  . ILE D 1 233 ? -34.568 -35.561 -56.949 1.00 173.04 ? 236 ILE A CB  1 
ATOM   6570 C CG1 . ILE D 1 233 ? -34.373 -34.098 -56.548 1.00 178.45 ? 236 ILE A CG1 1 
ATOM   6571 C CG2 . ILE D 1 233 ? -33.335 -36.109 -57.651 1.00 161.95 ? 236 ILE A CG2 1 
ATOM   6572 C CD1 . ILE D 1 233 ? -33.319 -33.880 -55.489 1.00 175.48 ? 236 ILE A CD1 1 
ATOM   6573 N N   . LEU D 1 234 ? -35.651 -37.400 -59.613 1.00 158.38 ? 237 LEU A N   1 
ATOM   6574 C CA  . LEU D 1 234 ? -35.828 -38.749 -60.207 1.00 150.06 ? 237 LEU A CA  1 
ATOM   6575 C C   . LEU D 1 234 ? -34.474 -39.276 -60.685 1.00 155.79 ? 237 LEU A C   1 
ATOM   6576 O O   . LEU D 1 234 ? -33.752 -38.521 -61.359 1.00 167.33 ? 237 LEU A O   1 
ATOM   6577 C CB  . LEU D 1 234 ? -36.817 -38.632 -61.368 1.00 168.58 ? 237 LEU A CB  1 
ATOM   6578 C CG  . LEU D 1 234 ? -36.860 -39.826 -62.315 1.00 175.88 ? 237 LEU A CG  1 
ATOM   6579 C CD1 . LEU D 1 234 ? -37.238 -41.084 -61.557 1.00 166.76 ? 237 LEU A CD1 1 
ATOM   6580 C CD2 . LEU D 1 234 ? -37.839 -39.576 -63.451 1.00 181.95 ? 237 LEU A CD2 1 
ATOM   6581 N N   . LYS D 1 235 ? -34.151 -40.523 -60.341 1.00 167.90 ? 238 LYS A N   1 
ATOM   6582 C CA  . LYS D 1 235 ? -32.867 -41.135 -60.767 1.00 144.60 ? 238 LYS A CA  1 
ATOM   6583 C C   . LYS D 1 235 ? -33.044 -41.687 -62.182 1.00 138.44 ? 238 LYS A C   1 
ATOM   6584 O O   . LYS D 1 235 ? -34.188 -41.968 -62.564 1.00 143.46 ? 238 LYS A O   1 
ATOM   6585 C CB  . LYS D 1 235 ? -32.454 -42.242 -59.794 1.00 138.62 ? 238 LYS A CB  1 
ATOM   6586 C CG  . LYS D 1 235 ? -32.222 -41.802 -58.354 1.00 136.51 ? 238 LYS A CG  1 
ATOM   6587 C CD  . LYS D 1 235 ? -31.066 -40.835 -58.196 1.00 95.42  ? 238 LYS A CD  1 
ATOM   6588 C CE  . LYS D 1 235 ? -30.795 -40.458 -56.755 1.00 126.89 ? 238 LYS A CE  1 
ATOM   6589 N NZ  . LYS D 1 235 ? -29.675 -39.493 -56.643 1.00 151.04 ? 238 LYS A NZ  1 
ATOM   6590 N N   . PRO D 1 236 ? -31.970 -41.835 -62.982 1.00 143.60 ? 239 PRO A N   1 
ATOM   6591 C CA  . PRO D 1 236 ? -32.079 -42.415 -64.323 1.00 147.14 ? 239 PRO A CA  1 
ATOM   6592 C C   . PRO D 1 236 ? -32.597 -43.845 -64.274 1.00 154.65 ? 239 PRO A C   1 
ATOM   6593 O O   . PRO D 1 236 ? -32.431 -44.556 -63.280 1.00 144.32 ? 239 PRO A O   1 
ATOM   6594 C CB  . PRO D 1 236 ? -30.639 -42.363 -64.846 1.00 130.34 ? 239 PRO A CB  1 
ATOM   6595 C CG  . PRO D 1 236 ? -30.016 -41.242 -64.078 1.00 137.41 ? 239 PRO A CG  1 
ATOM   6596 C CD  . PRO D 1 236 ? -30.601 -41.367 -62.706 1.00 146.71 ? 239 PRO A CD  1 
ATOM   6597 N N   . ASN D 1 237 ? -33.228 -44.257 -65.377 1.00 167.04 ? 240 ASN A N   1 
ATOM   6598 C CA  . ASN D 1 237 ? -33.799 -45.598 -65.527 1.00 155.39 ? 240 ASN A CA  1 
ATOM   6599 C C   . ASN D 1 237 ? -34.794 -45.911 -64.411 1.00 156.51 ? 240 ASN A C   1 
ATOM   6600 O O   . ASN D 1 237 ? -34.824 -47.019 -63.871 1.00 162.83 ? 240 ASN A O   1 
ATOM   6601 C CB  . ASN D 1 237 ? -32.704 -46.666 -65.596 1.00 135.63 ? 240 ASN A CB  1 
ATOM   6602 C CG  . ASN D 1 237 ? -31.897 -46.759 -64.309 1.00 166.80 ? 240 ASN A CG  1 
ATOM   6603 O OD1 . ASN D 1 237 ? -32.424 -46.561 -63.213 1.00 187.28 ? 240 ASN A OD1 1 
ATOM   6604 N ND2 . ASN D 1 237 ? -30.610 -47.061 -64.440 1.00 170.42 ? 240 ASN A ND2 1 
ATOM   6605 N N   . ASP D 1 238 ? -35.620 -44.925 -64.067 1.00 126.70 ? 241 ASP A N   1 
ATOM   6606 C CA  . ASP D 1 238 ? -36.636 -45.076 -63.037 1.00 137.06 ? 241 ASP A CA  1 
ATOM   6607 C C   . ASP D 1 238 ? -37.994 -44.664 -63.591 1.00 141.22 ? 241 ASP A C   1 
ATOM   6608 O O   . ASP D 1 238 ? -38.093 -43.754 -64.418 1.00 139.63 ? 241 ASP A O   1 
ATOM   6609 C CB  . ASP D 1 238 ? -36.293 -44.248 -61.799 1.00 146.88 ? 241 ASP A CB  1 
ATOM   6610 C CG  . ASP D 1 238 ? -37.277 -44.459 -60.678 1.00 168.12 ? 241 ASP A CG  1 
ATOM   6611 O OD1 . ASP D 1 238 ? -38.213 -45.264 -60.863 1.00 168.93 ? 241 ASP A OD1 1 
ATOM   6612 O OD2 . ASP D 1 238 ? -37.111 -43.823 -59.616 1.00 177.10 ? 241 ASP A OD2 1 
ATOM   6613 N N   . ALA D 1 239 ? -39.041 -45.337 -63.119 1.00 140.68 ? 242 ALA A N   1 
ATOM   6614 C CA  . ALA D 1 239 ? -40.383 -45.200 -63.668 1.00 166.56 ? 242 ALA A CA  1 
ATOM   6615 C C   . ALA D 1 239 ? -41.295 -44.469 -62.691 1.00 158.86 ? 242 ALA A C   1 
ATOM   6616 O O   . ALA D 1 239 ? -41.205 -44.667 -61.476 1.00 145.97 ? 242 ALA A O   1 
ATOM   6617 C CB  . ALA D 1 239 ? -40.976 -46.570 -64.002 1.00 190.98 ? 242 ALA A CB  1 
ATOM   6618 N N   . ILE D 1 240 ? -42.184 -43.634 -63.228 1.00 137.83 ? 243 ILE A N   1 
ATOM   6619 C CA  . ILE D 1 240 ? -43.066 -42.793 -62.422 1.00 131.32 ? 243 ILE A CA  1 
ATOM   6620 C C   . ILE D 1 240 ? -44.497 -43.141 -62.800 1.00 133.75 ? 243 ILE A C   1 
ATOM   6621 O O   . ILE D 1 240 ? -45.019 -42.642 -63.803 1.00 117.95 ? 243 ILE A O   1 
ATOM   6622 C CB  . ILE D 1 240 ? -42.795 -41.301 -62.630 1.00 127.26 ? 243 ILE A CB  1 
ATOM   6623 C CG1 . ILE D 1 240 ? -41.406 -40.943 -62.103 1.00 131.52 ? 243 ILE A CG1 1 
ATOM   6624 C CG2 . ILE D 1 240 ? -43.883 -40.464 -61.972 1.00 131.16 ? 243 ILE A CG2 1 
ATOM   6625 C CD1 . ILE D 1 240 ? -40.952 -39.570 -62.497 1.00 160.74 ? 243 ILE A CD1 1 
ATOM   6626 N N   . ASN D 1 241 ? -45.152 -43.961 -61.986 1.00 149.16 ? 244 ASN A N   1 
ATOM   6627 C CA  . ASN D 1 241 ? -46.498 -44.442 -62.289 1.00 139.81 ? 244 ASN A CA  1 
ATOM   6628 C C   . ASN D 1 241 ? -47.521 -43.461 -61.726 1.00 126.95 ? 244 ASN A C   1 
ATOM   6629 O O   . ASN D 1 241 ? -47.840 -43.492 -60.536 1.00 136.82 ? 244 ASN A O   1 
ATOM   6630 C CB  . ASN D 1 241 ? -46.694 -45.846 -61.729 1.00 152.35 ? 244 ASN A CB  1 
ATOM   6631 C CG  . ASN D 1 241 ? -45.902 -46.886 -62.493 1.00 180.67 ? 244 ASN A CG  1 
ATOM   6632 O OD1 . ASN D 1 241 ? -45.549 -46.679 -63.653 1.00 187.02 ? 244 ASN A OD1 1 
ATOM   6633 N ND2 . ASN D 1 241 ? -45.611 -48.009 -61.845 1.00 198.34 ? 244 ASN A ND2 1 
ATOM   6634 N N   . PHE D 1 242 ? -48.036 -42.588 -62.589 1.00 120.88 ? 245 PHE A N   1 
ATOM   6635 C CA  . PHE D 1 242 ? -49.078 -41.636 -62.216 1.00 131.58 ? 245 PHE A CA  1 
ATOM   6636 C C   . PHE D 1 242 ? -50.443 -42.228 -62.553 1.00 139.16 ? 245 PHE A C   1 
ATOM   6637 O O   . PHE D 1 242 ? -50.703 -42.582 -63.708 1.00 137.21 ? 245 PHE A O   1 
ATOM   6638 C CB  . PHE D 1 242 ? -48.888 -40.300 -62.940 1.00 113.35 ? 245 PHE A CB  1 
ATOM   6639 C CG  . PHE D 1 242 ? -47.859 -39.383 -62.313 1.00 117.77 ? 245 PHE A CG  1 
ATOM   6640 C CD1 . PHE D 1 242 ? -48.036 -38.877 -61.034 1.00 144.86 ? 245 PHE A CD1 1 
ATOM   6641 C CD2 . PHE D 1 242 ? -46.724 -39.014 -63.017 1.00 118.91 ? 245 PHE A CD2 1 
ATOM   6642 C CE1 . PHE D 1 242 ? -47.096 -38.020 -60.472 1.00 151.42 ? 245 PHE A CE1 1 
ATOM   6643 C CE2 . PHE D 1 242 ? -45.782 -38.164 -62.458 1.00 134.29 ? 245 PHE A CE2 1 
ATOM   6644 C CZ  . PHE D 1 242 ? -45.967 -37.669 -61.184 1.00 140.08 ? 245 PHE A CZ  1 
ATOM   6645 N N   . GLU D 1 243 ? -51.311 -42.337 -61.548 1.00 138.24 ? 246 GLU A N   1 
ATOM   6646 C CA  . GLU D 1 243 ? -52.674 -42.818 -61.743 1.00 147.42 ? 246 GLU A CA  1 
ATOM   6647 C C   . GLU D 1 243 ? -53.626 -41.936 -60.948 1.00 164.63 ? 246 GLU A C   1 
ATOM   6648 O O   . GLU D 1 243 ? -53.413 -41.716 -59.752 1.00 185.00 ? 246 GLU A O   1 
ATOM   6649 C CB  . GLU D 1 243 ? -52.818 -44.281 -61.309 1.00 165.40 ? 246 GLU A CB  1 
ATOM   6650 C CG  . GLU D 1 243 ? -54.258 -44.736 -61.197 1.00 185.62 ? 246 GLU A CG  1 
ATOM   6651 C CD  . GLU D 1 243 ? -54.405 -46.054 -60.469 1.00 197.42 ? 246 GLU A CD  1 
ATOM   6652 O OE1 . GLU D 1 243 ? -53.374 -46.632 -60.063 1.00 204.77 ? 246 GLU A OE1 1 
ATOM   6653 O OE2 . GLU D 1 243 ? -55.554 -46.515 -60.309 1.00 207.58 ? 246 GLU A OE2 1 
ATOM   6654 N N   . SER D 1 244 ? -54.675 -41.436 -61.603 1.00 145.93 ? 247 SER A N   1 
ATOM   6655 C CA  . SER D 1 244 ? -55.564 -40.488 -60.946 1.00 136.98 ? 247 SER A CA  1 
ATOM   6656 C C   . SER D 1 244 ? -56.847 -40.589 -61.760 1.00 137.04 ? 247 SER A C   1 
ATOM   6657 O O   . SER D 1 244 ? -56.824 -40.911 -62.952 1.00 134.86 ? 247 SER A O   1 
ATOM   6658 C CB  . SER D 1 244 ? -55.028 -39.059 -61.050 1.00 130.07 ? 247 SER A CB  1 
ATOM   6659 O OG  . SER D 1 244 ? -55.940 -38.147 -60.469 1.00 127.75 ? 247 SER A OG  1 
ATOM   6660 N N   . ASN D 1 245 ? -57.968 -40.287 -61.096 1.00 138.13 ? 248 ASN A N   1 
ATOM   6661 C CA  . ASN D 1 245 ? -59.272 -40.076 -61.713 1.00 145.81 ? 248 ASN A CA  1 
ATOM   6662 C C   . ASN D 1 245 ? -60.019 -38.742 -61.183 1.00 156.33 ? 248 ASN A C   1 
ATOM   6663 O O   . ASN D 1 245 ? -61.212 -38.589 -60.897 1.00 182.11 ? 248 ASN A O   1 
ATOM   6664 C CB  . ASN D 1 245 ? -60.244 -41.181 -61.299 1.00 151.14 ? 248 ASN A CB  1 
ATOM   6665 C CG  . ASN D 1 245 ? -60.526 -41.187 -59.803 1.00 162.75 ? 248 ASN A CG  1 
ATOM   6666 O OD1 . ASN D 1 245 ? -59.830 -40.532 -59.024 1.00 191.71 ? 248 ASN A OD1 1 
ATOM   6667 N ND2 . ASN D 1 245 ? -61.553 -41.924 -59.397 1.00 182.58 ? 248 ASN A ND2 1 
ATOM   6668 N N   . GLY D 1 246 ? -59.145 -37.756 -61.086 1.00 166.15 ? 249 GLY A N   1 
ATOM   6669 C CA  . GLY D 1 246 ? -59.585 -36.408 -60.773 1.00 174.15 ? 249 GLY A CA  1 
ATOM   6670 C C   . GLY D 1 246 ? -58.700 -35.502 -59.949 1.00 146.74 ? 249 GLY A C   1 
ATOM   6671 O O   . GLY D 1 246 ? -57.847 -35.946 -59.187 1.00 144.73 ? 249 GLY A O   1 
ATOM   6672 N N   . ASN D 1 247 ? -58.926 -34.200 -60.127 1.00 142.34 ? 250 ASN A N   1 
ATOM   6673 C CA  . ASN D 1 247 ? -58.254 -33.156 -59.355 1.00 145.00 ? 250 ASN A CA  1 
ATOM   6674 C C   . ASN D 1 247 ? -56.739 -33.224 -59.513 1.00 136.20 ? 250 ASN A C   1 
ATOM   6675 O O   . ASN D 1 247 ? -55.993 -32.898 -58.587 1.00 114.25 ? 250 ASN A O   1 
ATOM   6676 C CB  . ASN D 1 247 ? -58.648 -33.231 -57.877 1.00 142.94 ? 250 ASN A CB  1 
ATOM   6677 C CG  . ASN D 1 247 ? -60.147 -33.125 -57.672 1.00 146.13 ? 250 ASN A CG  1 
ATOM   6678 O OD1 . ASN D 1 247 ? -60.861 -34.127 -57.694 1.00 146.64 ? 250 ASN A OD1 1 
ATOM   6679 N ND2 . ASN D 1 247 ? -60.634 -31.905 -57.491 1.00 149.85 ? 250 ASN A ND2 1 
ATOM   6680 N N   . PHE D 1 248 ? -56.274 -33.635 -60.690 1.00 133.84 ? 251 PHE A N   1 
ATOM   6681 C CA  . PHE D 1 248 ? -54.866 -33.920 -60.921 1.00 127.06 ? 251 PHE A CA  1 
ATOM   6682 C C   . PHE D 1 248 ? -54.322 -32.987 -61.990 1.00 110.22 ? 251 PHE A C   1 
ATOM   6683 O O   . PHE D 1 248 ? -54.888 -32.891 -63.085 1.00 115.41 ? 251 PHE A O   1 
ATOM   6684 C CB  . PHE D 1 248 ? -54.668 -35.380 -61.336 1.00 137.57 ? 251 PHE A CB  1 
ATOM   6685 C CG  . PHE D 1 248 ? -53.239 -35.745 -61.633 1.00 127.71 ? 251 PHE A CG  1 
ATOM   6686 C CD1 . PHE D 1 248 ? -52.225 -35.403 -60.752 1.00 127.03 ? 251 PHE A CD1 1 
ATOM   6687 C CD2 . PHE D 1 248 ? -52.913 -36.456 -62.777 1.00 104.38 ? 251 PHE A CD2 1 
ATOM   6688 C CE1 . PHE D 1 248 ? -50.912 -35.747 -61.016 1.00 129.91 ? 251 PHE A CE1 1 
ATOM   6689 C CE2 . PHE D 1 248 ? -51.600 -36.806 -63.043 1.00 87.20  ? 251 PHE A CE2 1 
ATOM   6690 C CZ  . PHE D 1 248 ? -50.599 -36.449 -62.163 1.00 117.55 ? 251 PHE A CZ  1 
ATOM   6691 N N   . ILE D 1 249 ? -53.228 -32.305 -61.669 1.00 99.65  ? 252 ILE A N   1 
ATOM   6692 C CA  . ILE D 1 249 ? -52.537 -31.430 -62.604 1.00 99.13  ? 252 ILE A CA  1 
ATOM   6693 C C   . ILE D 1 249 ? -51.288 -32.198 -63.031 1.00 106.36 ? 252 ILE A C   1 
ATOM   6694 O O   . ILE D 1 249 ? -50.293 -32.248 -62.298 1.00 101.22 ? 252 ILE A O   1 
ATOM   6695 C CB  . ILE D 1 249 ? -52.199 -30.078 -61.972 1.00 102.24 ? 252 ILE A CB  1 
ATOM   6696 C CG1 . ILE D 1 249 ? -53.469 -29.299 -61.655 1.00 117.14 ? 252 ILE A CG1 1 
ATOM   6697 C CG2 . ILE D 1 249 ? -51.465 -29.217 -62.954 1.00 121.40 ? 252 ILE A CG2 1 
ATOM   6698 C CD1 . ILE D 1 249 ? -53.219 -28.080 -60.795 1.00 119.44 ? 252 ILE A CD1 1 
ATOM   6699 N N   . ALA D 1 250 ? -51.391 -32.893 -64.172 1.00 106.69 ? 253 ALA A N   1 
ATOM   6700 C CA  . ALA D 1 250 ? -50.310 -33.812 -64.610 1.00 100.02 ? 253 ALA A CA  1 
ATOM   6701 C C   . ALA D 1 250 ? -49.067 -33.089 -65.132 1.00 94.31  ? 253 ALA A C   1 
ATOM   6702 O O   . ALA D 1 250 ? -49.215 -32.048 -65.794 1.00 95.34  ? 253 ALA A O   1 
ATOM   6703 C CB  . ALA D 1 250 ? -50.857 -34.742 -65.668 1.00 95.02  ? 253 ALA A CB  1 
ATOM   6704 N N   . PRO D 1 251 ? -47.856 -33.646 -64.912 1.00 107.52 ? 254 PRO A N   1 
ATOM   6705 C CA  . PRO D 1 251 ? -46.626 -33.058 -65.438 1.00 97.83  ? 254 PRO A CA  1 
ATOM   6706 C C   . PRO D 1 251 ? -46.327 -33.321 -66.918 1.00 100.15 ? 254 PRO A C   1 
ATOM   6707 O O   . PRO D 1 251 ? -46.395 -34.464 -67.334 1.00 116.91 ? 254 PRO A O   1 
ATOM   6708 C CB  . PRO D 1 251 ? -45.500 -33.928 -64.861 1.00 83.22  ? 254 PRO A CB  1 
ATOM   6709 C CG  . PRO D 1 251 ? -46.150 -34.755 -63.770 1.00 95.66  ? 254 PRO A CG  1 
ATOM   6710 C CD  . PRO D 1 251 ? -47.610 -34.871 -64.152 1.00 117.73 ? 254 PRO A CD  1 
ATOM   6711 N N   . GLU D 1 252 ? -45.995 -32.269 -67.667 1.00 97.73  ? 255 GLU A N   1 
ATOM   6712 C CA  . GLU D 1 252 ? -45.613 -32.438 -69.094 1.00 125.20 ? 255 GLU A CA  1 
ATOM   6713 C C   . GLU D 1 252 ? -44.195 -31.992 -69.450 1.00 132.27 ? 255 GLU A C   1 
ATOM   6714 O O   . GLU D 1 252 ? -43.777 -32.203 -70.605 1.00 150.55 ? 255 GLU A O   1 
ATOM   6715 C CB  . GLU D 1 252 ? -46.571 -31.495 -69.821 1.00 131.49 ? 255 GLU A CB  1 
ATOM   6716 C CG  . GLU D 1 252 ? -46.617 -31.722 -71.320 1.00 162.06 ? 255 GLU A CG  1 
ATOM   6717 C CD  . GLU D 1 252 ? -47.385 -30.680 -72.112 1.00 165.48 ? 255 GLU A CD  1 
ATOM   6718 O OE1 . GLU D 1 252 ? -47.955 -29.763 -71.488 1.00 147.60 ? 255 GLU A OE1 1 
ATOM   6719 O OE2 . GLU D 1 252 ? -47.393 -30.777 -73.355 1.00 168.94 ? 255 GLU A OE2 1 
ATOM   6720 N N   . TYR D 1 253 ? -43.481 -31.416 -68.479 1.00 117.00 ? 256 TYR A N   1 
ATOM   6721 C CA  . TYR D 1 253 ? -42.147 -30.913 -68.739 1.00 116.13 ? 256 TYR A CA  1 
ATOM   6722 C C   . TYR D 1 253 ? -41.428 -31.011 -67.405 1.00 108.59 ? 256 TYR A C   1 
ATOM   6723 O O   . TYR D 1 253 ? -42.049 -30.975 -66.340 1.00 102.25 ? 256 TYR A O   1 
ATOM   6724 C CB  . TYR D 1 253 ? -42.040 -29.498 -69.315 1.00 128.68 ? 256 TYR A CB  1 
ATOM   6725 C CG  . TYR D 1 253 ? -42.697 -29.371 -70.670 1.00 131.20 ? 256 TYR A CG  1 
ATOM   6726 C CD1 . TYR D 1 253 ? -42.009 -29.672 -71.837 1.00 121.50 ? 256 TYR A CD1 1 
ATOM   6727 C CD2 . TYR D 1 253 ? -44.020 -28.964 -70.777 1.00 137.38 ? 256 TYR A CD2 1 
ATOM   6728 C CE1 . TYR D 1 253 ? -42.622 -29.560 -73.073 1.00 128.44 ? 256 TYR A CE1 1 
ATOM   6729 C CE2 . TYR D 1 253 ? -44.636 -28.849 -72.004 1.00 144.24 ? 256 TYR A CE2 1 
ATOM   6730 C CZ  . TYR D 1 253 ? -43.933 -29.149 -73.152 1.00 141.50 ? 256 TYR A CZ  1 
ATOM   6731 O OH  . TYR D 1 253 ? -44.543 -29.036 -74.381 1.00 128.88 ? 256 TYR A OH  1 
ATOM   6732 N N   . ALA D 1 254 ? -40.108 -31.150 -67.466 1.00 94.50  ? 257 ALA A N   1 
ATOM   6733 C CA  . ALA D 1 254 ? -39.350 -31.320 -66.239 1.00 114.01 ? 257 ALA A CA  1 
ATOM   6734 C C   . ALA D 1 254 ? -37.909 -30.892 -66.469 1.00 114.58 ? 257 ALA A C   1 
ATOM   6735 O O   . ALA D 1 254 ? -37.435 -30.810 -67.604 1.00 123.05 ? 257 ALA A O   1 
ATOM   6736 C CB  . ALA D 1 254 ? -39.422 -32.765 -65.739 1.00 105.42 ? 257 ALA A CB  1 
ATOM   6737 N N   . TYR D 1 255 ? -37.225 -30.541 -65.374 1.00 94.81  ? 258 TYR A N   1 
ATOM   6738 C CA  . TYR D 1 255 ? -35.838 -30.018 -65.482 1.00 96.00  ? 258 TYR A CA  1 
ATOM   6739 C C   . TYR D 1 255 ? -34.820 -31.150 -65.347 1.00 111.42 ? 258 TYR A C   1 
ATOM   6740 O O   . TYR D 1 255 ? -34.780 -31.789 -64.279 1.00 118.41 ? 258 TYR A O   1 
ATOM   6741 C CB  . TYR D 1 255 ? -35.574 -29.000 -64.371 1.00 120.34 ? 258 TYR A CB  1 
ATOM   6742 C CG  . TYR D 1 255 ? -35.978 -27.579 -64.669 1.00 119.30 ? 258 TYR A CG  1 
ATOM   6743 C CD1 . TYR D 1 255 ? -35.344 -26.845 -65.658 1.00 131.83 ? 258 TYR A CD1 1 
ATOM   6744 C CD2 . TYR D 1 255 ? -36.991 -26.961 -63.955 1.00 111.22 ? 258 TYR A CD2 1 
ATOM   6745 C CE1 . TYR D 1 255 ? -35.700 -25.533 -65.924 1.00 142.91 ? 258 TYR A CE1 1 
ATOM   6746 C CE2 . TYR D 1 255 ? -37.365 -25.654 -64.214 1.00 128.43 ? 258 TYR A CE2 1 
ATOM   6747 C CZ  . TYR D 1 255 ? -36.717 -24.935 -65.202 1.00 155.85 ? 258 TYR A CZ  1 
ATOM   6748 O OH  . TYR D 1 255 ? -37.086 -23.638 -65.462 1.00 171.66 ? 258 TYR A OH  1 
ATOM   6749 N N   . LYS D 1 256 ? -33.998 -31.370 -66.376 1.00 115.92 ? 259 LYS A N   1 
ATOM   6750 C CA  . LYS D 1 256 ? -32.911 -32.378 -66.258 1.00 113.04 ? 259 LYS A CA  1 
ATOM   6751 C C   . LYS D 1 256 ? -31.786 -31.760 -65.422 1.00 100.41 ? 259 LYS A C   1 
ATOM   6752 O O   . LYS D 1 256 ? -31.189 -30.770 -65.885 1.00 108.05 ? 259 LYS A O   1 
ATOM   6753 C CB  . LYS D 1 256 ? -32.404 -32.802 -67.639 1.00 105.19 ? 259 LYS A CB  1 
ATOM   6754 C CG  . LYS D 1 256 ? -33.433 -33.489 -68.526 1.00 125.06 ? 259 LYS A CG  1 
ATOM   6755 C CD  . LYS D 1 256 ? -32.965 -33.676 -69.952 1.00 129.37 ? 259 LYS A CD  1 
ATOM   6756 C CE  . LYS D 1 256 ? -32.708 -32.366 -70.665 1.00 170.44 ? 259 LYS A CE  1 
ATOM   6757 N NZ  . LYS D 1 256 ? -32.304 -32.578 -72.075 1.00 162.83 ? 259 LYS A NZ  1 
ATOM   6758 N N   . ILE D 1 257 ? -31.534 -32.308 -64.231 1.00 111.42 ? 260 ILE A N   1 
ATOM   6759 C CA  . ILE D 1 257 ? -30.474 -31.765 -63.331 1.00 113.50 ? 260 ILE A CA  1 
ATOM   6760 C C   . ILE D 1 257 ? -29.108 -31.996 -63.986 1.00 109.58 ? 260 ILE A C   1 
ATOM   6761 O O   . ILE D 1 257 ? -28.813 -33.157 -64.333 1.00 138.77 ? 260 ILE A O   1 
ATOM   6762 C CB  . ILE D 1 257 ? -30.568 -32.427 -61.943 1.00 113.22 ? 260 ILE A CB  1 
ATOM   6763 C CG1 . ILE D 1 257 ? -31.974 -32.297 -61.352 1.00 105.20 ? 260 ILE A CG1 1 
ATOM   6764 C CG2 . ILE D 1 257 ? -29.508 -31.872 -61.007 1.00 112.89 ? 260 ILE A CG2 1 
ATOM   6765 C CD1 . ILE D 1 257 ? -32.136 -32.953 -60.001 1.00 117.12 ? 260 ILE A CD1 1 
ATOM   6766 N N   . VAL D 1 258 a -28.313 -30.932 -64.150 1.00 97.21  ? 260 VAL A N   1 
ATOM   6767 C CA  . VAL D 1 258 a -26.984 -31.047 -64.824 1.00 118.11 ? 260 VAL A CA  1 
ATOM   6768 C C   . VAL D 1 258 a -25.945 -30.265 -64.012 1.00 126.43 ? 260 VAL A C   1 
ATOM   6769 O O   . VAL D 1 258 a -26.351 -29.379 -63.238 1.00 135.60 ? 260 VAL A O   1 
ATOM   6770 C CB  . VAL D 1 258 a -27.049 -30.538 -66.279 1.00 114.69 ? 260 VAL A CB  1 
ATOM   6771 C CG1 . VAL D 1 258 a -25.777 -30.850 -67.053 1.00 137.79 ? 260 VAL A CG1 1 
ATOM   6772 C CG2 . VAL D 1 258 a -28.259 -31.077 -67.025 1.00 138.51 ? 260 VAL A CG2 1 
ATOM   6773 N N   . LYS D 1 259 ? -24.659 -30.603 -64.147 1.00 116.18 ? 261 LYS A N   1 
ATOM   6774 C CA  . LYS D 1 259 ? -23.584 -29.825 -63.472 1.00 112.60 ? 261 LYS A CA  1 
ATOM   6775 C C   . LYS D 1 259 ? -23.995 -29.485 -62.035 1.00 124.52 ? 261 LYS A C   1 
ATOM   6776 O O   . LYS D 1 259 ? -23.967 -28.288 -61.689 1.00 140.97 ? 261 LYS A O   1 
ATOM   6777 C CB  . LYS D 1 259 ? -23.300 -28.539 -64.254 1.00 111.62 ? 261 LYS A CB  1 
ATOM   6778 C CG  . LYS D 1 259 ? -23.150 -28.715 -65.759 1.00 119.52 ? 261 LYS A CG  1 
ATOM   6779 C CD  . LYS D 1 259 ? -23.229 -27.411 -66.523 1.00 152.20 ? 261 LYS A CD  1 
ATOM   6780 C CE  . LYS D 1 259 ? -23.390 -27.609 -68.015 1.00 154.45 ? 261 LYS A CE  1 
ATOM   6781 N NZ  . LYS D 1 259 ? -23.627 -26.324 -68.715 1.00 165.25 ? 261 LYS A NZ  1 
ATOM   6782 N N   . LYS D 1 260 ? -24.354 -30.490 -61.233 1.00 125.14 ? 262 LYS A N   1 
ATOM   6783 C CA  . LYS D 1 260 ? -24.683 -30.233 -59.805 1.00 148.02 ? 262 LYS A CA  1 
ATOM   6784 C C   . LYS D 1 260 ? -23.532 -29.446 -59.169 1.00 150.77 ? 262 LYS A C   1 
ATOM   6785 O O   . LYS D 1 260 ? -22.385 -29.928 -59.237 1.00 131.48 ? 262 LYS A O   1 
ATOM   6786 C CB  . LYS D 1 260 ? -24.919 -31.550 -59.060 1.00 135.38 ? 262 LYS A CB  1 
ATOM   6787 C CG  . LYS D 1 260 ? -26.150 -32.333 -59.495 1.00 141.56 ? 262 LYS A CG  1 
ATOM   6788 C CD  . LYS D 1 260 ? -26.433 -33.525 -58.609 1.00 138.48 ? 262 LYS A CD  1 
ATOM   6789 C CE  . LYS D 1 260 ? -27.711 -34.248 -58.976 1.00 143.13 ? 262 LYS A CE  1 
ATOM   6790 N NZ  . LYS D 1 260 ? -27.980 -35.384 -58.064 1.00 149.24 ? 262 LYS A NZ  1 
ATOM   6791 N N   . GLY D 1 261 ? -23.829 -28.285 -58.578 1.00 146.86 ? 263 GLY A N   1 
ATOM   6792 C CA  . GLY D 1 261 ? -22.770 -27.440 -57.990 1.00 125.81 ? 263 GLY A CA  1 
ATOM   6793 C C   . GLY D 1 261 ? -23.292 -26.592 -56.844 1.00 144.53 ? 263 GLY A C   1 
ATOM   6794 O O   . GLY D 1 261 ? -24.500 -26.286 -56.845 1.00 168.93 ? 263 GLY A O   1 
ATOM   6795 N N   . ASP D 1 262 ? -22.417 -26.199 -55.913 1.00 142.20 ? 264 ASP A N   1 
ATOM   6796 C CA  . ASP D 1 262 ? -22.871 -25.460 -54.740 1.00 139.64 ? 264 ASP A CA  1 
ATOM   6797 C C   . ASP D 1 262 ? -23.605 -24.181 -55.135 1.00 141.30 ? 264 ASP A C   1 
ATOM   6798 O O   . ASP D 1 262 ? -23.171 -23.442 -56.022 1.00 151.22 ? 264 ASP A O   1 
ATOM   6799 C CB  . ASP D 1 262 ? -21.676 -25.128 -53.847 1.00 153.72 ? 264 ASP A CB  1 
ATOM   6800 C CG  . ASP D 1 262 ? -20.539 -24.489 -54.618 1.00 174.69 ? 264 ASP A CG  1 
ATOM   6801 O OD1 . ASP D 1 262 ? -20.049 -25.120 -55.579 1.00 158.40 ? 264 ASP A OD1 1 
ATOM   6802 O OD2 . ASP D 1 262 ? -20.134 -23.361 -54.267 1.00 205.51 ? 264 ASP A OD2 1 
ATOM   6803 N N   . SER D 1 263 ? -24.727 -23.929 -54.468 1.00 124.44 ? 265 SER A N   1 
ATOM   6804 C CA  . SER D 1 263 ? -25.537 -22.738 -54.704 1.00 119.00 ? 265 SER A CA  1 
ATOM   6805 C C   . SER D 1 263 ? -26.424 -22.524 -53.483 1.00 132.27 ? 265 SER A C   1 
ATOM   6806 O O   . SER D 1 263 ? -26.224 -23.149 -52.436 1.00 148.52 ? 265 SER A O   1 
ATOM   6807 C CB  . SER D 1 263 ? -26.359 -22.874 -55.991 1.00 114.61 ? 265 SER A CB  1 
ATOM   6808 O OG  . SER D 1 263 ? -27.297 -23.932 -55.891 1.00 131.77 ? 265 SER A OG  1 
ATOM   6809 N N   . THR D 1 264 ? -27.405 -21.639 -53.617 1.00 122.88 ? 266 THR A N   1 
ATOM   6810 C CA  . THR D 1 264 ? -28.423 -21.431 -52.592 1.00 138.96 ? 266 THR A CA  1 
ATOM   6811 C C   . THR D 1 264 ? -29.578 -20.681 -53.241 1.00 141.91 ? 266 THR A C   1 
ATOM   6812 O O   . THR D 1 264 ? -29.632 -20.529 -54.468 1.00 146.33 ? 266 THR A O   1 
ATOM   6813 C CB  . THR D 1 264 ? -27.866 -20.669 -51.386 1.00 142.48 ? 266 THR A CB  1 
ATOM   6814 O OG1 . THR D 1 264 ? -28.865 -20.614 -50.360 1.00 159.91 ? 266 THR A OG1 1 
ATOM   6815 C CG2 . THR D 1 264 ? -27.529 -19.256 -51.786 1.00 127.31 ? 266 THR A CG2 1 
ATOM   6816 N N   . ILE D 1 265 ? -30.500 -20.198 -52.411 1.00 126.04 ? 267 ILE A N   1 
ATOM   6817 C CA  . ILE D 1 265 ? -31.647 -19.413 -52.856 1.00 140.39 ? 267 ILE A CA  1 
ATOM   6818 C C   . ILE D 1 265 ? -31.659 -18.142 -52.015 1.00 140.91 ? 267 ILE A C   1 
ATOM   6819 O O   . ILE D 1 265 ? -32.029 -18.164 -50.833 1.00 150.07 ? 267 ILE A O   1 
ATOM   6820 C CB  . ILE D 1 265 ? -32.966 -20.184 -52.749 1.00 142.23 ? 267 ILE A CB  1 
ATOM   6821 C CG1 . ILE D 1 265 ? -33.221 -20.536 -51.283 1.00 140.69 ? 267 ILE A CG1 1 
ATOM   6822 C CG2 . ILE D 1 265 ? -32.925 -21.438 -53.609 1.00 172.16 ? 267 ILE A CG2 1 
ATOM   6823 C CD1 . ILE D 1 265 ? -34.188 -19.625 -50.597 1.00 145.94 ? 267 ILE A CD1 1 
ATOM   6824 N N   . MET D 1 266 ? -31.260 -17.032 -52.629 1.00 119.31 ? 268 MET A N   1 
ATOM   6825 C CA  . MET D 1 266 ? -31.071 -15.758 -51.956 1.00 113.93 ? 268 MET A CA  1 
ATOM   6826 C C   . MET D 1 266 ? -32.397 -15.013 -51.893 1.00 118.40 ? 268 MET A C   1 
ATOM   6827 O O   . MET D 1 266 ? -33.153 -14.993 -52.868 1.00 135.56 ? 268 MET A O   1 
ATOM   6828 C CB  . MET D 1 266 ? -30.049 -14.936 -52.740 1.00 113.41 ? 268 MET A CB  1 
ATOM   6829 C CG  . MET D 1 266 ? -28.701 -15.628 -52.854 1.00 117.96 ? 268 MET A CG  1 
ATOM   6830 S SD  . MET D 1 266 ? -27.802 -15.866 -51.315 1.00 163.10 ? 268 MET A SD  1 
ATOM   6831 C CE  . MET D 1 266 ? -27.289 -14.203 -50.987 1.00 109.93 ? 268 MET A CE  1 
ATOM   6832 N N   . LYS D 1 267 ? -32.677 -14.393 -50.752 1.00 112.74 ? 269 LYS A N   1 
ATOM   6833 C CA  . LYS D 1 267 ? -33.972 -13.716 -50.515 1.00 113.66 ? 269 LYS A CA  1 
ATOM   6834 C C   . LYS D 1 267 ? -33.513 -12.293 -50.250 1.00 104.87 ? 269 LYS A C   1 
ATOM   6835 O O   . LYS D 1 267 ? -33.215 -11.923 -49.111 1.00 118.50 ? 269 LYS A O   1 
ATOM   6836 C CB  . LYS D 1 267 ? -34.744 -14.408 -49.392 1.00 120.03 ? 269 LYS A CB  1 
ATOM   6837 C CG  . LYS D 1 267 ? -35.218 -15.811 -49.736 1.00 149.09 ? 269 LYS A CG  1 
ATOM   6838 C CD  . LYS D 1 267 ? -35.979 -16.440 -48.580 1.00 159.00 ? 269 LYS A CD  1 
ATOM   6839 C CE  . LYS D 1 267 ? -36.471 -17.835 -48.934 1.00 151.09 ? 269 LYS A CE  1 
ATOM   6840 N NZ  . LYS D 1 267 ? -37.200 -18.467 -47.798 1.00 129.48 ? 269 LYS A NZ  1 
ATOM   6841 N N   . SER D 1 268 ? -33.495 -11.475 -51.298 1.00 103.79 ? 270 SER A N   1 
ATOM   6842 C CA  . SER D 1 268 ? -33.242 -10.041 -51.151 1.00 111.95 ? 270 SER A CA  1 
ATOM   6843 C C   . SER D 1 268 ? -33.610 -9.435  -52.495 1.00 129.18 ? 270 SER A C   1 
ATOM   6844 O O   . SER D 1 268 ? -33.778 -10.128 -53.501 1.00 138.94 ? 270 SER A O   1 
ATOM   6845 C CB  . SER D 1 268 ? -31.823 -9.620  -50.745 1.00 113.62 ? 270 SER A CB  1 
ATOM   6846 O OG  . SER D 1 268 ? -30.878 -9.974  -51.738 1.00 121.96 ? 270 SER A OG  1 
ATOM   6847 N N   . GLU D 1 269 ? -33.739 -8.113  -52.498 1.00 136.46 ? 271 GLU A N   1 
ATOM   6848 C CA  . GLU D 1 269 ? -34.148 -7.353  -53.679 1.00 147.57 ? 271 GLU A CA  1 
ATOM   6849 C C   . GLU D 1 269 ? -32.999 -6.424  -54.054 1.00 136.65 ? 271 GLU A C   1 
ATOM   6850 O O   . GLU D 1 269 ? -32.999 -5.245  -53.695 1.00 131.46 ? 271 GLU A O   1 
ATOM   6851 C CB  . GLU D 1 269 ? -35.437 -6.571  -53.400 1.00 151.58 ? 271 GLU A CB  1 
ATOM   6852 C CG  . GLU D 1 269 ? -36.664 -7.436  -53.168 1.00 150.83 ? 271 GLU A CG  1 
ATOM   6853 C CD  . GLU D 1 269 ? -37.891 -6.614  -52.830 1.00 150.35 ? 271 GLU A CD  1 
ATOM   6854 O OE1 . GLU D 1 269 ? -37.739 -5.396  -52.599 1.00 149.90 ? 271 GLU A OE1 1 
ATOM   6855 O OE2 . GLU D 1 269 ? -39.004 -7.181  -52.790 1.00 134.16 ? 271 GLU A OE2 1 
ATOM   6856 N N   . LEU D 1 270 ? -32.018 -6.956  -54.783 1.00 133.61 ? 272 LEU A N   1 
ATOM   6857 C CA  . LEU D 1 270 ? -30.829 -6.191  -55.125 1.00 160.78 ? 272 LEU A CA  1 
ATOM   6858 C C   . LEU D 1 270 ? -30.434 -6.452  -56.571 1.00 155.18 ? 272 LEU A C   1 
ATOM   6859 O O   . LEU D 1 270 ? -30.738 -7.503  -57.140 1.00 143.51 ? 272 LEU A O   1 
ATOM   6860 C CB  . LEU D 1 270 ? -29.660 -6.518  -54.192 1.00 152.91 ? 272 LEU A CB  1 
ATOM   6861 C CG  . LEU D 1 270 ? -29.875 -6.114  -52.732 1.00 141.14 ? 272 LEU A CG  1 
ATOM   6862 C CD1 . LEU D 1 270 ? -28.746 -6.628  -51.863 1.00 133.33 ? 272 LEU A CD1 1 
ATOM   6863 C CD2 . LEU D 1 270 ? -30.015 -4.605  -52.607 1.00 158.36 ? 272 LEU A CD2 1 
ATOM   6864 N N   . GLU D 1 271 ? -29.758 -5.476  -57.186 1.00 151.51 ? 273 GLU A N   1 
ATOM   6865 C CA  . GLU D 1 271 ? -29.421 -5.590  -58.633 1.00 148.68 ? 273 GLU A CA  1 
ATOM   6866 C C   . GLU D 1 271 ? -28.193 -6.482  -58.852 1.00 139.37 ? 273 GLU A C   1 
ATOM   6867 O O   . GLU D 1 271 ? -27.727 -7.102  -57.876 1.00 143.08 ? 273 GLU A O   1 
ATOM   6868 C CB  . GLU D 1 271 ? -29.197 -4.197  -59.224 1.00 172.56 ? 273 GLU A CB  1 
ATOM   6869 C CG  . GLU D 1 271 ? -30.459 -3.355  -59.265 1.00 193.68 ? 273 GLU A CG  1 
ATOM   6870 C CD  . GLU D 1 271 ? -30.261 -1.939  -59.779 1.00 220.72 ? 273 GLU A CD  1 
ATOM   6871 O OE1 . GLU D 1 271 ? -29.094 -1.527  -59.938 1.00 221.49 ? 273 GLU A OE1 1 
ATOM   6872 O OE2 . GLU D 1 271 ? -31.273 -1.252  -60.017 1.00 230.45 ? 273 GLU A OE2 1 
ATOM   6873 N N   . TYR D 1 272 ? -27.695 -6.536  -60.092 1.00 118.63 ? 274 TYR A N   1 
ATOM   6874 C CA  . TYR D 1 272 ? -26.541 -7.410  -60.430 1.00 113.36 ? 274 TYR A CA  1 
ATOM   6875 C C   . TYR D 1 272 ? -25.247 -6.594  -60.468 1.00 110.67 ? 274 TYR A C   1 
ATOM   6876 O O   . TYR D 1 272 ? -25.293 -5.420  -60.886 1.00 108.55 ? 274 TYR A O   1 
ATOM   6877 C CB  . TYR D 1 272 ? -26.760 -8.068  -61.794 1.00 136.87 ? 274 TYR A CB  1 
ATOM   6878 C CG  . TYR D 1 272 ? -25.556 -8.778  -62.358 1.00 154.68 ? 274 TYR A CG  1 
ATOM   6879 C CD1 . TYR D 1 272 ? -24.996 -9.867  -61.710 1.00 150.96 ? 274 TYR A CD1 1 
ATOM   6880 C CD2 . TYR D 1 272 ? -24.965 -8.353  -63.536 1.00 159.79 ? 274 TYR A CD2 1 
ATOM   6881 C CE1 . TYR D 1 272 ? -23.886 -10.518 -62.222 1.00 173.56 ? 274 TYR A CE1 1 
ATOM   6882 C CE2 . TYR D 1 272 ? -23.856 -8.992  -64.061 1.00 167.54 ? 274 TYR A CE2 1 
ATOM   6883 C CZ  . TYR D 1 272 ? -23.314 -10.080 -63.402 1.00 184.19 ? 274 TYR A CZ  1 
ATOM   6884 O OH  . TYR D 1 272 ? -22.214 -10.717 -63.922 1.00 168.83 ? 274 TYR A OH  1 
ATOM   6885 N N   . GLY D 1 273 ? -24.131 -7.154  -60.018 1.00 133.66 ? 275 GLY A N   1 
ATOM   6886 C CA  . GLY D 1 273 ? -22.898 -6.349  -59.968 1.00 137.66 ? 275 GLY A CA  1 
ATOM   6887 C C   . GLY D 1 273 ? -22.008 -6.637  -61.158 1.00 147.70 ? 275 GLY A C   1 
ATOM   6888 O O   . GLY D 1 273 ? -21.865 -7.822  -61.508 1.00 155.46 ? 275 GLY A O   1 
ATOM   6889 N N   . ASN D 1 274 ? -21.241 -5.652  -61.626 1.00 160.64 ? 276 ASN A N   1 
ATOM   6890 C CA  . ASN D 1 274 ? -20.233 -5.956  -62.678 1.00 180.63 ? 276 ASN A CA  1 
ATOM   6891 C C   . ASN D 1 274 ? -18.856 -6.010  -62.000 1.00 186.74 ? 276 ASN A C   1 
ATOM   6892 O O   . ASN D 1 274 ? -18.033 -5.121  -62.295 1.00 183.46 ? 276 ASN A O   1 
ATOM   6893 C CB  . ASN D 1 274 ? -20.275 -4.941  -63.823 1.00 173.25 ? 276 ASN A CB  1 
ATOM   6894 C CG  . ASN D 1 274 ? -19.998 -3.524  -63.367 1.00 177.61 ? 276 ASN A CG  1 
ATOM   6895 O OD1 . ASN D 1 274 ? -20.721 -2.982  -62.535 1.00 187.55 ? 276 ASN A OD1 1 
ATOM   6896 N ND2 . ASN D 1 274 ? -18.953 -2.917  -63.907 1.00 186.38 ? 276 ASN A ND2 1 
ATOM   6897 N N   . CYS D 1 275 ? -18.608 -6.999  -61.124 1.00 207.56 ? 277 CYS A N   1 
ATOM   6898 C CA  . CYS D 1 275 ? -17.331 -7.001  -60.353 1.00 206.78 ? 277 CYS A CA  1 
ATOM   6899 C C   . CYS D 1 275 ? -17.275 -8.466  -59.898 1.00 198.48 ? 277 CYS A C   1 
ATOM   6900 O O   . CYS D 1 275 ? -18.222 -8.875  -59.198 1.00 194.12 ? 277 CYS A O   1 
ATOM   6901 C CB  . CYS D 1 275 ? -17.442 -5.994  -59.216 1.00 199.40 ? 277 CYS A CB  1 
ATOM   6902 S SG  . CYS D 1 275 ? -19.047 -6.040  -58.373 1.00 239.78 ? 277 CYS A SG  1 
ATOM   6903 N N   . ASN D 1 276 ? -16.235 -9.223  -60.256 1.00 206.02 ? 278 ASN A N   1 
ATOM   6904 C CA  . ASN D 1 276 ? -16.175 -10.666 -59.847 1.00 204.28 ? 278 ASN A CA  1 
ATOM   6905 C C   . ASN D 1 276 ? -15.731 -10.678 -58.372 1.00 212.16 ? 278 ASN A C   1 
ATOM   6906 O O   . ASN D 1 276 ? -14.515 -10.575 -58.119 1.00 214.69 ? 278 ASN A O   1 
ATOM   6907 C CB  . ASN D 1 276 ? -15.102 -11.389 -60.670 1.00 188.80 ? 278 ASN A CB  1 
ATOM   6908 C CG  . ASN D 1 276 ? -13.693 -10.910 -60.389 1.00 176.85 ? 278 ASN A CG  1 
ATOM   6909 O OD1 . ASN D 1 276 ? -13.494 -9.876  -59.756 1.00 202.94 ? 278 ASN A OD1 1 
ATOM   6910 N ND2 . ASN D 1 276 ? -12.707 -11.655 -60.861 1.00 140.71 ? 278 ASN A ND2 1 
ATOM   6911 N N   . THR D 1 277 ? -16.690 -10.718 -57.437 1.00 204.87 ? 279 THR A N   1 
ATOM   6912 C CA  . THR D 1 277 ? -16.386 -10.660 -55.978 1.00 195.08 ? 279 THR A CA  1 
ATOM   6913 C C   . THR D 1 277 ? -16.359 -12.053 -55.345 1.00 182.03 ? 279 THR A C   1 
ATOM   6914 O O   . THR D 1 277 ? -17.306 -12.815 -55.566 1.00 163.37 ? 279 THR A O   1 
ATOM   6915 C CB  . THR D 1 277 ? -17.204 -9.688  -55.116 1.00 193.15 ? 279 THR A CB  1 
ATOM   6916 O OG1 . THR D 1 277 ? -17.268 -8.437  -55.802 1.00 195.69 ? 279 THR A OG1 1 
ATOM   6917 C CG2 . THR D 1 277 ? -16.627 -9.486  -53.732 1.00 210.08 ? 279 THR A CG2 1 
ATOM   6918 N N   . THR D 1 278 ? -15.360 -12.340 -54.510 1.00 164.03 ? 280 THR A N   1 
ATOM   6919 C CA  . THR D 1 278 ? -15.211 -13.705 -53.937 1.00 148.17 ? 280 THR A CA  1 
ATOM   6920 C C   . THR D 1 278 ? -16.453 -14.135 -53.143 1.00 152.10 ? 280 THR A C   1 
ATOM   6921 O O   . THR D 1 278 ? -16.510 -15.328 -52.783 1.00 163.33 ? 280 THR A O   1 
ATOM   6922 C CB  . THR D 1 278 ? -13.960 -13.792 -53.053 1.00 138.63 ? 280 THR A CB  1 
ATOM   6923 O OG1 . THR D 1 278 ? -13.868 -15.124 -52.546 1.00 139.64 ? 280 THR A OG1 1 
ATOM   6924 C CG2 . THR D 1 278 ? -13.982 -12.808 -51.904 1.00 126.99 ? 280 THR A CG2 1 
ATOM   6925 N N   . CYS D 1 279 ? -17.405 -13.233 -52.870 1.00 163.45 ? 281 CYS A N   1 
ATOM   6926 C CA  . CYS D 1 279 ? -18.544 -13.649 -52.003 1.00 143.02 ? 281 CYS A CA  1 
ATOM   6927 C C   . CYS D 1 279 ? -19.829 -12.849 -52.251 1.00 153.89 ? 281 CYS A C   1 
ATOM   6928 O O   . CYS D 1 279 ? -19.735 -11.766 -52.853 1.00 166.89 ? 281 CYS A O   1 
ATOM   6929 C CB  . CYS D 1 279 ? -18.164 -13.494 -50.534 1.00 119.72 ? 281 CYS A CB  1 
ATOM   6930 S SG  . CYS D 1 279 ? -19.522 -13.839 -49.386 1.00 176.62 ? 281 CYS A SG  1 
ATOM   6931 N N   . GLN D 1 280 ? -20.979 -13.389 -51.831 1.00 139.71 ? 282 GLN A N   1 
ATOM   6932 C CA  . GLN D 1 280 ? -22.295 -12.700 -51.903 1.00 122.90 ? 282 GLN A CA  1 
ATOM   6933 C C   . GLN D 1 280 ? -23.175 -13.072 -50.708 1.00 125.62 ? 282 GLN A C   1 
ATOM   6934 O O   . GLN D 1 280 ? -23.273 -14.273 -50.403 1.00 127.36 ? 282 GLN A O   1 
ATOM   6935 C CB  . GLN D 1 280 ? -23.020 -13.057 -53.198 1.00 115.57 ? 282 GLN A CB  1 
ATOM   6936 C CG  . GLN D 1 280 ? -23.956 -11.961 -53.675 1.00 121.46 ? 282 GLN A CG  1 
ATOM   6937 C CD  . GLN D 1 280 ? -23.223 -10.647 -53.784 1.00 124.99 ? 282 GLN A CD  1 
ATOM   6938 O OE1 . GLN D 1 280 ? -23.612 -9.644  -53.191 1.00 126.11 ? 282 GLN A OE1 1 
ATOM   6939 N NE2 . GLN D 1 280 ? -22.147 -10.647 -54.554 1.00 147.67 ? 282 GLN A NE2 1 
ATOM   6940 N N   . THR D 1 281 ? -23.787 -12.073 -50.068 1.00 115.79 ? 283 THR A N   1 
ATOM   6941 C CA  . THR D 1 281 ? -24.710 -12.310 -48.929 1.00 111.17 ? 283 THR A CA  1 
ATOM   6942 C C   . THR D 1 281 ? -26.000 -11.554 -49.232 1.00 135.10 ? 283 THR A C   1 
ATOM   6943 O O   . THR D 1 281 ? -25.923 -10.529 -49.929 1.00 127.68 ? 283 THR A O   1 
ATOM   6944 C CB  . THR D 1 281 ? -24.110 -11.822 -47.610 1.00 96.87  ? 283 THR A CB  1 
ATOM   6945 O OG1 . THR D 1 281 ? -24.040 -10.399 -47.685 1.00 133.14 ? 283 THR A OG1 1 
ATOM   6946 C CG2 . THR D 1 281 ? -22.741 -12.400 -47.332 1.00 117.04 ? 283 THR A CG2 1 
ATOM   6947 N N   . PRO D 1 282 ? -27.178 -11.997 -48.750 1.00 139.21 ? 284 PRO A N   1 
ATOM   6948 C CA  . PRO D 1 282 ? -28.438 -11.355 -49.123 1.00 147.92 ? 284 PRO A CA  1 
ATOM   6949 C C   . PRO D 1 282 ? -28.332 -9.827  -49.087 1.00 150.45 ? 284 PRO A C   1 
ATOM   6950 O O   . PRO D 1 282 ? -29.041 -9.183  -49.823 1.00 162.68 ? 284 PRO A O   1 
ATOM   6951 C CB  . PRO D 1 282 ? -29.381 -11.861 -48.027 1.00 132.63 ? 284 PRO A CB  1 
ATOM   6952 C CG  . PRO D 1 282 ? -28.869 -13.250 -47.740 1.00 136.89 ? 284 PRO A CG  1 
ATOM   6953 C CD  . PRO D 1 282 ? -27.363 -13.108 -47.813 1.00 138.91 ? 284 PRO A CD  1 
ATOM   6954 N N   . LYS D 1 283 ? -27.439 -9.288  -48.262 1.00 129.36 ? 285 LYS A N   1 
ATOM   6955 C CA  . LYS D 1 283 ? -27.348 -7.848  -48.111 1.00 125.23 ? 285 LYS A CA  1 
ATOM   6956 C C   . LYS D 1 283 ? -26.184 -7.233  -48.880 1.00 118.22 ? 285 LYS A C   1 
ATOM   6957 O O   . LYS D 1 283 ? -26.063 -6.006  -48.908 1.00 135.15 ? 285 LYS A O   1 
ATOM   6958 C CB  . LYS D 1 283 ? -27.231 -7.500  -46.625 1.00 145.82 ? 285 LYS A CB  1 
ATOM   6959 C CG  . LYS D 1 283 ? -28.277 -8.209  -45.770 1.00 158.82 ? 285 LYS A CG  1 
ATOM   6960 C CD  . LYS D 1 283 ? -28.023 -8.018  -44.285 1.00 165.50 ? 285 LYS A CD  1 
ATOM   6961 C CE  . LYS D 1 283 ? -29.017 -8.809  -43.444 1.00 156.73 ? 285 LYS A CE  1 
ATOM   6962 N NZ  . LYS D 1 283 ? -28.713 -8.721  -41.987 1.00 158.99 ? 285 LYS A NZ  1 
ATOM   6963 N N   . GLY D 1 284 ? -25.336 -8.042  -49.500 1.00 126.20 ? 286 GLY A N   1 
ATOM   6964 C CA  . GLY D 1 284 ? -24.208 -7.503  -50.238 1.00 107.36 ? 286 GLY A CA  1 
ATOM   6965 C C   . GLY D 1 284 ? -23.103 -8.538  -50.375 1.00 116.44 ? 286 GLY A C   1 
ATOM   6966 O O   . GLY D 1 284 ? -23.313 -9.723  -50.139 1.00 135.86 ? 286 GLY A O   1 
ATOM   6967 N N   . ALA D 1 285 ? -21.907 -8.070  -50.748 1.00 115.77 ? 287 ALA A N   1 
ATOM   6968 C CA  . ALA D 1 285 ? -20.773 -8.996  -50.982 1.00 127.04 ? 287 ALA A CA  1 
ATOM   6969 C C   . ALA D 1 285 ? -19.648 -8.738  -49.975 1.00 127.99 ? 287 ALA A C   1 
ATOM   6970 O O   . ALA D 1 285 ? -19.648 -7.656  -49.355 1.00 133.68 ? 287 ALA A O   1 
ATOM   6971 C CB  . ALA D 1 285 ? -20.279 -8.817  -52.394 1.00 142.45 ? 287 ALA A CB  1 
ATOM   6972 N N   . ILE D 1 286 ? -18.723 -9.693  -49.829 1.00 125.15 ? 288 ILE A N   1 
ATOM   6973 C CA  . ILE D 1 286 ? -17.556 -9.521  -48.911 1.00 120.15 ? 288 ILE A CA  1 
ATOM   6974 C C   . ILE D 1 286 ? -16.219 -9.973  -49.511 1.00 130.63 ? 288 ILE A C   1 
ATOM   6975 O O   . ILE D 1 286 ? -16.154 -11.121 -49.992 1.00 143.90 ? 288 ILE A O   1 
ATOM   6976 C CB  . ILE D 1 286 ? -17.695 -10.421 -47.667 1.00 134.77 ? 288 ILE A CB  1 
ATOM   6977 C CG1 . ILE D 1 286 ? -19.114 -10.395 -47.094 1.00 153.90 ? 288 ILE A CG1 1 
ATOM   6978 C CG2 . ILE D 1 286 ? -16.659 -10.057 -46.613 1.00 158.15 ? 288 ILE A CG2 1 
ATOM   6979 C CD1 . ILE D 1 286 ? -19.294 -11.267 -45.876 1.00 161.50 ? 288 ILE A CD1 1 
ATOM   6980 N N   . ASN D 1 287 ? -15.201 -9.107  -49.494 1.00 154.09 ? 289 ASN A N   1 
ATOM   6981 C CA  . ASN D 1 287 ? -13.898 -9.449  -50.126 1.00 154.59 ? 289 ASN A CA  1 
ATOM   6982 C C   . ASN D 1 287 ? -12.763 -9.258  -49.113 1.00 161.60 ? 289 ASN A C   1 
ATOM   6983 O O   . ASN D 1 287 ? -11.682 -8.785  -49.520 1.00 170.22 ? 289 ASN A O   1 
ATOM   6984 C CB  . ASN D 1 287 ? -13.661 -8.632  -51.399 1.00 142.72 ? 289 ASN A CB  1 
ATOM   6985 C CG  . ASN D 1 287 ? -13.839 -7.145  -51.182 1.00 148.98 ? 289 ASN A CG  1 
ATOM   6986 O OD1 . ASN D 1 287 ? -14.916 -6.693  -50.798 1.00 150.44 ? 289 ASN A OD1 1 
ATOM   6987 N ND2 . ASN D 1 287 ? -12.789 -6.377  -51.420 1.00 136.19 ? 289 ASN A ND2 1 
ATOM   6988 N N   . THR D 1 288 ? -13.000 -9.621  -47.850 1.00 164.50 ? 290 THR A N   1 
ATOM   6989 C CA  . THR D 1 288 ? -11.963 -9.472  -46.794 1.00 143.46 ? 290 THR A CA  1 
ATOM   6990 C C   . THR D 1 288 ? -11.572 -10.855 -46.262 1.00 140.34 ? 290 THR A C   1 
ATOM   6991 O O   . THR D 1 288 ? -11.741 -11.836 -47.013 1.00 148.57 ? 290 THR A O   1 
ATOM   6992 C CB  . THR D 1 288 ? -12.444 -8.533  -45.682 1.00 148.31 ? 290 THR A CB  1 
ATOM   6993 O OG1 . THR D 1 288 ? -13.684 -9.048  -45.198 1.00 156.70 ? 290 THR A OG1 1 
ATOM   6994 C CG2 . THR D 1 288 ? -12.626 -7.110  -46.161 1.00 154.41 ? 290 THR A CG2 1 
ATOM   6995 N N   . SER D 1 289 ? -11.076 -10.931 -45.022 1.00 144.89 ? 291 SER A N   1 
ATOM   6996 C CA  . SER D 1 289 ? -10.588 -12.233 -44.495 1.00 159.49 ? 291 SER A CA  1 
ATOM   6997 C C   . SER D 1 289 ? -11.003 -12.444 -43.033 1.00 167.18 ? 291 SER A C   1 
ATOM   6998 O O   . SER D 1 289 ? -10.669 -13.515 -42.490 1.00 159.56 ? 291 SER A O   1 
ATOM   6999 C CB  . SER D 1 289 ? -9.091  -12.340 -44.647 1.00 158.51 ? 291 SER A CB  1 
ATOM   7000 O OG  . SER D 1 289 ? -8.438  -11.277 -43.970 1.00 152.01 ? 291 SER A OG  1 
ATOM   7001 N N   . LEU D 1 290 ? -11.692 -11.479 -42.413 1.00 158.70 ? 292 LEU A N   1 
ATOM   7002 C CA  . LEU D 1 290 ? -12.016 -11.651 -41.003 1.00 133.54 ? 292 LEU A CA  1 
ATOM   7003 C C   . LEU D 1 290 ? -12.832 -12.929 -40.807 1.00 121.80 ? 292 LEU A C   1 
ATOM   7004 O O   . LEU D 1 290 ? -13.709 -13.236 -41.622 1.00 141.38 ? 292 LEU A O   1 
ATOM   7005 C CB  . LEU D 1 290 ? -12.779 -10.433 -40.478 1.00 119.95 ? 292 LEU A CB  1 
ATOM   7006 C CG  . LEU D 1 290 ? -11.972 -9.128  -40.390 1.00 124.75 ? 292 LEU A CG  1 
ATOM   7007 C CD1 . LEU D 1 290 ? -12.584 -8.156  -39.395 1.00 117.13 ? 292 LEU A CD1 1 
ATOM   7008 C CD2 . LEU D 1 290 ? -10.512 -9.393  -40.040 1.00 119.49 ? 292 LEU A CD2 1 
ATOM   7009 N N   . PRO D 1 291 ? -12.571 -13.693 -39.741 1.00 114.48 ? 293 PRO A N   1 
ATOM   7010 C CA  . PRO D 1 291 ? -13.075 -15.078 -39.687 1.00 113.98 ? 293 PRO A CA  1 
ATOM   7011 C C   . PRO D 1 291 ? -14.589 -15.224 -39.685 1.00 115.75 ? 293 PRO A C   1 
ATOM   7012 O O   . PRO D 1 291 ? -15.090 -16.231 -40.202 1.00 129.88 ? 293 PRO A O   1 
ATOM   7013 C CB  . PRO D 1 291 ? -12.471 -15.604 -38.378 1.00 112.37 ? 293 PRO A CB  1 
ATOM   7014 C CG  . PRO D 1 291 ? -11.207 -14.837 -38.234 1.00 126.91 ? 293 PRO A CG  1 
ATOM   7015 C CD  . PRO D 1 291 ? -11.561 -13.443 -38.698 1.00 128.85 ? 293 PRO A CD  1 
ATOM   7016 N N   . PHE D 1 292 ? -15.338 -14.284 -39.114 1.00 101.39 ? 294 PHE A N   1 
ATOM   7017 C CA  . PHE D 1 292 ? -16.762 -14.495 -38.896 1.00 103.73 ? 294 PHE A CA  1 
ATOM   7018 C C   . PHE D 1 292 ? -17.569 -13.291 -39.369 1.00 114.29 ? 294 PHE A C   1 
ATOM   7019 O O   . PHE D 1 292 ? -17.050 -12.180 -39.501 1.00 118.82 ? 294 PHE A O   1 
ATOM   7020 C CB  . PHE D 1 292 ? -17.052 -14.785 -37.415 1.00 98.64  ? 294 PHE A CB  1 
ATOM   7021 C CG  . PHE D 1 292 ? -16.175 -15.856 -36.819 1.00 115.72 ? 294 PHE A CG  1 
ATOM   7022 C CD1 . PHE D 1 292 ? -16.189 -17.147 -37.322 1.00 126.32 ? 294 PHE A CD1 1 
ATOM   7023 C CD2 . PHE D 1 292 ? -15.336 -15.568 -35.753 1.00 131.23 ? 294 PHE A CD2 1 
ATOM   7024 C CE1 . PHE D 1 292 ? -15.382 -18.132 -36.773 1.00 144.79 ? 294 PHE A CE1 1 
ATOM   7025 C CE2 . PHE D 1 292 ? -14.529 -16.547 -35.200 1.00 139.59 ? 294 PHE A CE2 1 
ATOM   7026 C CZ  . PHE D 1 292 ? -14.551 -17.829 -35.711 1.00 143.05 ? 294 PHE A CZ  1 
ATOM   7027 N N   . GLN D 1 293 ? -18.860 -13.529 -39.624 1.00 109.91 ? 295 GLN A N   1 
ATOM   7028 C CA  . GLN D 1 293 ? -19.782 -12.508 -40.103 1.00 94.09  ? 295 GLN A CA  1 
ATOM   7029 C C   . GLN D 1 293 ? -20.893 -12.244 -39.098 1.00 85.51  ? 295 GLN A C   1 
ATOM   7030 O O   . GLN D 1 293 ? -21.163 -13.047 -38.200 1.00 102.63 ? 295 GLN A O   1 
ATOM   7031 C CB  . GLN D 1 293 ? -20.458 -12.899 -41.422 1.00 112.26 ? 295 GLN A CB  1 
ATOM   7032 C CG  . GLN D 1 293 ? -19.562 -13.432 -42.500 1.00 167.28 ? 295 GLN A CG  1 
ATOM   7033 C CD  . GLN D 1 293 ? -20.362 -13.967 -43.668 1.00 196.73 ? 295 GLN A CD  1 
ATOM   7034 O OE1 . GLN D 1 293 ? -21.593 -13.914 -43.667 1.00 213.75 ? 295 GLN A OE1 1 
ATOM   7035 N NE2 . GLN D 1 293 ? -19.669 -14.475 -44.677 1.00 212.17 ? 295 GLN A NE2 1 
ATOM   7036 N N   . ASN D 1 294 ? -21.559 -11.107 -39.294 1.00 83.11  ? 296 ASN A N   1 
ATOM   7037 C CA  . ASN D 1 294 ? -22.830 -10.813 -38.652 1.00 89.79  ? 296 ASN A CA  1 
ATOM   7038 C C   . ASN D 1 294 ? -23.914 -10.483 -39.660 1.00 101.35 ? 296 ASN A C   1 
ATOM   7039 O O   . ASN D 1 294 ? -25.053 -10.209 -39.262 1.00 105.69 ? 296 ASN A O   1 
ATOM   7040 C CB  . ASN D 1 294 ? -22.685 -9.647  -37.671 1.00 89.06  ? 296 ASN A CB  1 
ATOM   7041 C CG  . ASN D 1 294 ? -21.566 -9.860  -36.695 1.00 104.87 ? 296 ASN A CG  1 
ATOM   7042 O OD1 . ASN D 1 294 ? -21.537 -10.865 -35.989 1.00 130.95 ? 296 ASN A OD1 1 
ATOM   7043 N ND2 . ASN D 1 294 ? -20.638 -8.914  -36.639 1.00 96.07  ? 296 ASN A ND2 1 
ATOM   7044 N N   . ILE D 1 295 ? -23.592 -10.505 -40.949 1.00 95.41  ? 297 ILE A N   1 
ATOM   7045 C CA  . ILE D 1 295 ? -24.511 -10.062 -42.019 1.00 113.66 ? 297 ILE A CA  1 
ATOM   7046 C C   . ILE D 1 295 ? -25.701 -10.978 -42.181 1.00 110.25 ? 297 ILE A C   1 
ATOM   7047 O O   . ILE D 1 295 ? -26.850 -10.558 -42.000 1.00 105.45 ? 297 ILE A O   1 
ATOM   7048 C CB  . ILE D 1 295 ? -23.757 -9.934  -43.334 1.00 116.78 ? 297 ILE A CB  1 
ATOM   7049 C CG1 . ILE D 1 295 ? -22.451 -9.162  -43.136 1.00 130.58 ? 297 ILE A CG1 1 
ATOM   7050 C CG2 . ILE D 1 295 ? -24.640 -9.264  -44.367 1.00 129.30 ? 297 ILE A CG2 1 
ATOM   7051 C CD1 . ILE D 1 295 ? -21.670 -8.954  -44.408 1.00 138.66 ? 297 ILE A CD1 1 
ATOM   7052 N N   . HIS D 1 296 ? -25.445 -12.238 -42.541 1.00 114.38 ? 298 HIS A N   1 
ATOM   7053 C CA  . HIS D 1 296 ? -26.541 -13.147 -42.901 1.00 111.80 ? 298 HIS A CA  1 
ATOM   7054 C C   . HIS D 1 296 ? -25.972 -14.552 -42.983 1.00 121.02 ? 298 HIS A C   1 
ATOM   7055 O O   . HIS D 1 296 ? -24.874 -14.722 -43.532 1.00 128.79 ? 298 HIS A O   1 
ATOM   7056 C CB  . HIS D 1 296 ? -27.246 -12.747 -44.173 1.00 112.92 ? 298 HIS A CB  1 
ATOM   7057 C CG  . HIS D 1 296 ? -28.607 -13.346 -44.327 1.00 115.18 ? 298 HIS A CG  1 
ATOM   7058 N ND1 . HIS D 1 296 ? -28.810 -14.690 -44.553 1.00 121.21 ? 298 HIS A ND1 1 
ATOM   7059 C CD2 . HIS D 1 296 ? -29.838 -12.782 -44.287 1.00 124.06 ? 298 HIS A CD2 1 
ATOM   7060 C CE1 . HIS D 1 296 ? -30.106 -14.928 -44.645 1.00 126.09 ? 298 HIS A CE1 1 
ATOM   7061 N NE2 . HIS D 1 296 ? -30.752 -13.787 -44.487 1.00 129.05 ? 298 HIS A NE2 1 
ATOM   7062 N N   . PRO D 1 297 ? -26.632 -15.606 -42.449 1.00 122.59 ? 299 PRO A N   1 
ATOM   7063 C CA  . PRO D 1 297 ? -26.127 -16.967 -42.625 1.00 115.42 ? 299 PRO A CA  1 
ATOM   7064 C C   . PRO D 1 297 ? -26.031 -17.368 -44.101 1.00 105.42 ? 299 PRO A C   1 
ATOM   7065 O O   . PRO D 1 297 ? -24.976 -17.790 -44.518 1.00 105.65 ? 299 PRO A O   1 
ATOM   7066 C CB  . PRO D 1 297 ? -27.175 -17.854 -41.941 1.00 117.15 ? 299 PRO A CB  1 
ATOM   7067 C CG  . PRO D 1 297 ? -28.402 -16.981 -41.822 1.00 117.57 ? 299 PRO A CG  1 
ATOM   7068 C CD  . PRO D 1 297 ? -27.854 -15.584 -41.633 1.00 117.42 ? 299 PRO A CD  1 
ATOM   7069 N N   . ILE D 1 298 ? -27.135 -17.242 -44.843 1.00 96.83  ? 300 ILE A N   1 
ATOM   7070 C CA  . ILE D 1 298 ? -27.150 -17.632 -46.285 1.00 96.96  ? 300 ILE A CA  1 
ATOM   7071 C C   . ILE D 1 298 ? -25.988 -16.930 -46.993 1.00 87.90  ? 300 ILE A C   1 
ATOM   7072 O O   . ILE D 1 298 ? -25.962 -15.686 -46.983 1.00 106.14 ? 300 ILE A O   1 
ATOM   7073 C CB  . ILE D 1 298 ? -28.508 -17.295 -46.931 1.00 108.93 ? 300 ILE A CB  1 
ATOM   7074 C CG1 . ILE D 1 298 ? -29.667 -17.969 -46.191 1.00 92.31  ? 300 ILE A CG1 1 
ATOM   7075 C CG2 . ILE D 1 298 ? -28.507 -17.651 -48.409 1.00 108.92 ? 300 ILE A CG2 1 
ATOM   7076 C CD1 . ILE D 1 298 ? -29.585 -19.477 -46.172 1.00 80.13  ? 300 ILE A CD1 1 
ATOM   7077 N N   . THR D 1 299 ? -25.063 -17.702 -47.572 1.00 81.42  ? 301 THR A N   1 
ATOM   7078 C CA  . THR D 1 299 ? -23.881 -17.121 -48.266 1.00 105.67 ? 301 THR A CA  1 
ATOM   7079 C C   . THR D 1 299 ? -23.533 -17.994 -49.477 1.00 121.78 ? 301 THR A C   1 
ATOM   7080 O O   . THR D 1 299 ? -24.275 -18.965 -49.725 1.00 129.57 ? 301 THR A O   1 
ATOM   7081 C CB  . THR D 1 299 ? -22.687 -17.006 -47.311 1.00 126.46 ? 301 THR A CB  1 
ATOM   7082 O OG1 . THR D 1 299 ? -22.571 -18.244 -46.609 1.00 152.99 ? 301 THR A OG1 1 
ATOM   7083 C CG2 . THR D 1 299 ? -22.819 -15.871 -46.320 1.00 116.43 ? 301 THR A CG2 1 
ATOM   7084 N N   . ILE D 1 300 ? -22.474 -17.634 -50.216 1.00 109.39 ? 302 ILE A N   1 
ATOM   7085 C CA  . ILE D 1 300 ? -22.111 -18.371 -51.465 1.00 123.29 ? 302 ILE A CA  1 
ATOM   7086 C C   . ILE D 1 300 ? -20.642 -18.801 -51.402 1.00 152.62 ? 302 ILE A C   1 
ATOM   7087 O O   . ILE D 1 300 ? -19.785 -17.916 -51.222 1.00 153.68 ? 302 ILE A O   1 
ATOM   7088 C CB  . ILE D 1 300 ? -22.351 -17.490 -52.709 1.00 133.89 ? 302 ILE A CB  1 
ATOM   7089 C CG1 . ILE D 1 300 ? -23.610 -16.629 -52.583 1.00 132.66 ? 302 ILE A CG1 1 
ATOM   7090 C CG2 . ILE D 1 300 ? -22.371 -18.336 -53.973 1.00 157.69 ? 302 ILE A CG2 1 
ATOM   7091 C CD1 . ILE D 1 300 ? -24.893 -17.394 -52.764 1.00 148.47 ? 302 ILE A CD1 1 
ATOM   7092 N N   . GLY D 1 301 ? -20.364 -20.100 -51.555 1.00 160.10 ? 303 GLY A N   1 
ATOM   7093 C CA  . GLY D 1 301 ? -18.967 -20.580 -51.605 1.00 159.73 ? 303 GLY A CA  1 
ATOM   7094 C C   . GLY D 1 301 ? -18.078 -19.894 -50.583 1.00 158.76 ? 303 GLY A C   1 
ATOM   7095 O O   . GLY D 1 301 ? -18.395 -19.970 -49.381 1.00 158.31 ? 303 GLY A O   1 
ATOM   7096 N N   . LYS D 1 302 ? -16.994 -19.260 -51.044 1.00 156.53 ? 304 LYS A N   1 
ATOM   7097 C CA  . LYS D 1 302 ? -16.063 -18.550 -50.126 1.00 133.26 ? 304 LYS A CA  1 
ATOM   7098 C C   . LYS D 1 302 ? -16.851 -17.482 -49.363 1.00 132.10 ? 304 LYS A C   1 
ATOM   7099 O O   . LYS D 1 302 ? -17.414 -16.591 -50.028 1.00 148.32 ? 304 LYS A O   1 
ATOM   7100 C CB  . LYS D 1 302 ? -14.907 -17.927 -50.914 1.00 116.78 ? 304 LYS A CB  1 
ATOM   7101 C CG  . LYS D 1 302 ? -14.091 -18.902 -51.751 1.00 135.55 ? 304 LYS A CG  1 
ATOM   7102 C CD  . LYS D 1 302 ? -12.908 -18.255 -52.439 1.00 134.64 ? 304 LYS A CD  1 
ATOM   7103 C CE  . LYS D 1 302 ? -12.088 -19.227 -53.260 1.00 112.30 ? 304 LYS A CE  1 
ATOM   7104 N NZ  . LYS D 1 302 ? -10.924 -18.563 -53.892 1.00 95.21  ? 304 LYS A NZ  1 
ATOM   7105 N N   . CYS D 1 303 ? -16.868 -17.560 -48.029 1.00 132.95 ? 305 CYS A N   1 
ATOM   7106 C CA  . CYS D 1 303 ? -17.676 -16.616 -47.213 1.00 146.44 ? 305 CYS A CA  1 
ATOM   7107 C C   . CYS D 1 303 ? -17.445 -16.905 -45.726 1.00 147.44 ? 305 CYS A C   1 
ATOM   7108 O O   . CYS D 1 303 ? -17.621 -18.073 -45.325 1.00 152.17 ? 305 CYS A O   1 
ATOM   7109 C CB  . CYS D 1 303 ? -19.157 -16.813 -47.499 1.00 170.59 ? 305 CYS A CB  1 
ATOM   7110 S SG  . CYS D 1 303 ? -19.684 -18.537 -47.314 1.00 227.35 ? 305 CYS A SG  1 
ATOM   7111 N N   . PRO D 1 304 ? -17.036 -15.920 -44.895 1.00 142.98 ? 306 PRO A N   1 
ATOM   7112 C CA  . PRO D 1 304 ? -16.764 -16.193 -43.485 1.00 135.64 ? 306 PRO A CA  1 
ATOM   7113 C C   . PRO D 1 304 ? -17.994 -16.806 -42.798 1.00 132.90 ? 306 PRO A C   1 
ATOM   7114 O O   . PRO D 1 304 ? -19.089 -16.655 -43.309 1.00 156.22 ? 306 PRO A O   1 
ATOM   7115 C CB  . PRO D 1 304 ? -16.464 -14.803 -42.909 1.00 119.38 ? 306 PRO A CB  1 
ATOM   7116 C CG  . PRO D 1 304 ? -15.937 -14.018 -44.092 1.00 104.40 ? 306 PRO A CG  1 
ATOM   7117 C CD  . PRO D 1 304 ? -16.695 -14.551 -45.290 1.00 116.66 ? 306 PRO A CD  1 
ATOM   7118 N N   . LYS D 1 305 ? -17.794 -17.479 -41.666 1.00 103.69 ? 307 LYS A N   1 
ATOM   7119 C CA  . LYS D 1 305 ? -18.886 -18.118 -40.882 1.00 112.60 ? 307 LYS A CA  1 
ATOM   7120 C C   . LYS D 1 305 ? -19.856 -17.029 -40.356 1.00 108.39 ? 307 LYS A C   1 
ATOM   7121 O O   . LYS D 1 305 ? -19.538 -15.837 -40.495 1.00 122.79 ? 307 LYS A O   1 
ATOM   7122 C CB  . LYS D 1 305 ? -18.276 -18.867 -39.669 1.00 102.61 ? 307 LYS A CB  1 
ATOM   7123 C CG  . LYS D 1 305 ? -18.660 -20.338 -39.581 1.00 125.07 ? 307 LYS A CG  1 
ATOM   7124 C CD  . LYS D 1 305 ? -20.140 -20.561 -39.357 1.00 141.13 ? 307 LYS A CD  1 
ATOM   7125 C CE  . LYS D 1 305 ? -20.526 -22.024 -39.337 1.00 156.83 ? 307 LYS A CE  1 
ATOM   7126 N NZ  . LYS D 1 305 ? -21.974 -22.206 -39.077 1.00 150.13 ? 307 LYS A NZ  1 
ATOM   7127 N N   . TYR D 1 306 ? -20.986 -17.441 -39.769 1.00 92.55  ? 308 TYR A N   1 
ATOM   7128 C CA  . TYR D 1 306 ? -22.001 -16.485 -39.344 1.00 107.70 ? 308 TYR A CA  1 
ATOM   7129 C C   . TYR D 1 306 ? -22.171 -16.533 -37.831 1.00 97.95  ? 308 TYR A C   1 
ATOM   7130 O O   . TYR D 1 306 ? -22.368 -17.609 -37.258 1.00 91.45  ? 308 TYR A O   1 
ATOM   7131 C CB  . TYR D 1 306 ? -23.346 -16.753 -40.019 1.00 115.51 ? 308 TYR A CB  1 
ATOM   7132 C CG  . TYR D 1 306 ? -24.438 -15.838 -39.514 1.00 112.35 ? 308 TYR A CG  1 
ATOM   7133 C CD1 . TYR D 1 306 ? -24.368 -14.467 -39.725 1.00 114.98 ? 308 TYR A CD1 1 
ATOM   7134 C CD2 . TYR D 1 306 ? -25.516 -16.336 -38.794 1.00 121.69 ? 308 TYR A CD2 1 
ATOM   7135 C CE1 . TYR D 1 306 ? -25.353 -13.620 -39.257 1.00 125.63 ? 308 TYR A CE1 1 
ATOM   7136 C CE2 . TYR D 1 306 ? -26.507 -15.495 -38.318 1.00 126.89 ? 308 TYR A CE2 1 
ATOM   7137 C CZ  . TYR D 1 306 ? -26.420 -14.138 -38.553 1.00 128.65 ? 308 TYR A CZ  1 
ATOM   7138 O OH  . TYR D 1 306 ? -27.401 -13.295 -38.084 1.00 136.99 ? 308 TYR A OH  1 
ATOM   7139 N N   . VAL D 1 307 ? -22.106 -15.362 -37.194 1.00 115.98 ? 309 VAL A N   1 
ATOM   7140 C CA  . VAL D 1 307 ? -22.281 -15.214 -35.754 1.00 111.21 ? 309 VAL A CA  1 
ATOM   7141 C C   . VAL D 1 307 ? -23.287 -14.099 -35.500 1.00 111.30 ? 309 VAL A C   1 
ATOM   7142 O O   . VAL D 1 307 ? -23.317 -13.098 -36.226 1.00 123.61 ? 309 VAL A O   1 
ATOM   7143 C CB  . VAL D 1 307 ? -20.944 -14.905 -35.043 1.00 97.60  ? 309 VAL A CB  1 
ATOM   7144 C CG1 . VAL D 1 307 ? -21.150 -14.738 -33.543 1.00 103.11 ? 309 VAL A CG1 1 
ATOM   7145 C CG2 . VAL D 1 307 ? -19.920 -15.986 -35.327 1.00 133.44 ? 309 VAL A CG2 1 
ATOM   7146 N N   . LYS D 1 308 ? -24.106 -14.266 -34.466 1.00 100.50 ? 310 LYS A N   1 
ATOM   7147 C CA  . LYS D 1 308 ? -25.121 -13.278 -34.130 1.00 99.93  ? 310 LYS A CA  1 
ATOM   7148 C C   . LYS D 1 308 ? -24.623 -12.200 -33.177 1.00 99.05  ? 310 LYS A C   1 
ATOM   7149 O O   . LYS D 1 308 ? -25.420 -11.357 -32.752 1.00 105.37 ? 310 LYS A O   1 
ATOM   7150 C CB  . LYS D 1 308 ? -26.341 -13.968 -33.520 1.00 83.89  ? 310 LYS A CB  1 
ATOM   7151 C CG  . LYS D 1 308 ? -27.135 -14.798 -34.508 1.00 102.31 ? 310 LYS A CG  1 
ATOM   7152 C CD  . LYS D 1 308 ? -28.489 -15.156 -33.922 1.00 108.61 ? 310 LYS A CD  1 
ATOM   7153 C CE  . LYS D 1 308 ? -29.214 -16.191 -34.768 1.00 120.12 ? 310 LYS A CE  1 
ATOM   7154 N NZ  . LYS D 1 308 ? -30.486 -16.658 -34.140 1.00 95.64  ? 310 LYS A NZ  1 
ATOM   7155 N N   . SER D 1 309 ? -23.324 -12.202 -32.879 1.00 78.86  ? 311 SER A N   1 
ATOM   7156 C CA  . SER D 1 309 ? -22.775 -11.220 -31.909 1.00 86.63  ? 311 SER A CA  1 
ATOM   7157 C C   . SER D 1 309 ? -22.725 -9.832  -32.547 1.00 93.22  ? 311 SER A C   1 
ATOM   7158 O O   . SER D 1 309 ? -22.760 -9.750  -33.783 1.00 110.01 ? 311 SER A O   1 
ATOM   7159 C CB  . SER D 1 309 ? -21.420 -11.632 -31.433 1.00 99.07  ? 311 SER A CB  1 
ATOM   7160 O OG  . SER D 1 309 ? -20.845 -10.613 -30.630 1.00 110.64 ? 311 SER A OG  1 
ATOM   7161 N N   . THR D 1 310 ? -22.633 -8.786  -31.726 1.00 81.32  ? 312 THR A N   1 
ATOM   7162 C CA  . THR D 1 310 ? -22.541 -7.405  -32.260 1.00 60.76  ? 312 THR A CA  1 
ATOM   7163 C C   . THR D 1 310 ? -21.069 -7.038  -32.402 1.00 85.24  ? 312 THR A C   1 
ATOM   7164 O O   . THR D 1 310 ? -20.768 -6.155  -33.221 1.00 101.05 ? 312 THR A O   1 
ATOM   7165 C CB  . THR D 1 310 ? -23.242 -6.406  -31.342 1.00 66.70  ? 312 THR A CB  1 
ATOM   7166 O OG1 . THR D 1 310 ? -22.532 -6.410  -30.105 1.00 111.19 ? 312 THR A OG1 1 
ATOM   7167 C CG2 . THR D 1 310 ? -24.697 -6.744  -31.106 1.00 99.50  ? 312 THR A CG2 1 
ATOM   7168 N N   . LYS D 1 311 ? -20.199 -7.695  -31.632 1.00 91.91  ? 313 LYS A N   1 
ATOM   7169 C CA  . LYS D 1 311 ? -18.740 -7.451  -31.774 1.00 94.90  ? 313 LYS A CA  1 
ATOM   7170 C C   . LYS D 1 311 ? -17.944 -8.591  -31.137 1.00 100.11 ? 313 LYS A C   1 
ATOM   7171 O O   . LYS D 1 311 ? -18.291 -8.991  -30.013 1.00 96.88  ? 313 LYS A O   1 
ATOM   7172 C CB  . LYS D 1 311 ? -18.342 -6.119  -31.136 1.00 108.47 ? 313 LYS A CB  1 
ATOM   7173 C CG  . LYS D 1 311 ? -19.042 -4.892  -31.708 1.00 116.07 ? 313 LYS A CG  1 
ATOM   7174 C CD  . LYS D 1 311 ? -18.814 -4.688  -33.194 1.00 86.00  ? 313 LYS A CD  1 
ATOM   7175 C CE  . LYS D 1 311 ? -17.400 -4.274  -33.545 1.00 100.20 ? 313 LYS A CE  1 
ATOM   7176 N NZ  . LYS D 1 311 ? -17.268 -3.926  -34.980 1.00 105.72 ? 313 LYS A NZ  1 
ATOM   7177 N N   . LEU D 1 312 ? -16.920 -9.086  -31.839 1.00 106.63 ? 314 LEU A N   1 
ATOM   7178 C CA  . LEU D 1 312 ? -16.036 -10.142 -31.278 1.00 102.81 ? 314 LEU A CA  1 
ATOM   7179 C C   . LEU D 1 312 ? -14.588 -9.702  -31.484 1.00 90.98  ? 314 LEU A C   1 
ATOM   7180 O O   . LEU D 1 312 ? -14.040 -9.967  -32.566 1.00 79.17  ? 314 LEU A O   1 
ATOM   7181 C CB  . LEU D 1 312 ? -16.308 -11.478 -31.971 1.00 89.61  ? 314 LEU A CB  1 
ATOM   7182 C CG  . LEU D 1 312 ? -17.698 -12.068 -31.741 1.00 108.70 ? 314 LEU A CG  1 
ATOM   7183 C CD1 . LEU D 1 312 ? -17.901 -13.311 -32.592 1.00 124.23 ? 314 LEU A CD1 1 
ATOM   7184 C CD2 . LEU D 1 312 ? -17.912 -12.388 -30.271 1.00 113.60 ? 314 LEU A CD2 1 
ATOM   7185 N N   . ARG D 1 313 ? -14.011 -9.039  -30.485 1.00 82.13  ? 315 ARG A N   1 
ATOM   7186 C CA  . ARG D 1 313 ? -12.635 -8.572  -30.575 1.00 95.14  ? 315 ARG A CA  1 
ATOM   7187 C C   . ARG D 1 313 ? -11.813 -9.255  -29.496 1.00 88.41  ? 315 ARG A C   1 
ATOM   7188 O O   . ARG D 1 313 ? -12.107 -9.116  -28.304 1.00 85.62  ? 315 ARG A O   1 
ATOM   7189 C CB  . ARG D 1 313 ? -12.549 -7.053  -30.425 1.00 105.99 ? 315 ARG A CB  1 
ATOM   7190 C CG  . ARG D 1 313 ? -13.401 -6.293  -31.414 1.00 120.99 ? 315 ARG A CG  1 
ATOM   7191 C CD  . ARG D 1 313 ? -12.931 -4.862  -31.540 1.00 143.31 ? 315 ARG A CD  1 
ATOM   7192 N NE  . ARG D 1 313 ? -11.578 -4.797  -32.075 1.00 135.35 ? 315 ARG A NE  1 
ATOM   7193 C CZ  . ARG D 1 313 ? -10.927 -3.671  -32.330 1.00 157.75 ? 315 ARG A CZ  1 
ATOM   7194 N NH1 . ARG D 1 313 ? -11.471 -2.489  -32.090 1.00 161.39 ? 315 ARG A NH1 1 
ATOM   7195 N NH2 . ARG D 1 313 ? -9.704  -3.732  -32.848 1.00 155.15 ? 315 ARG A NH2 1 
ATOM   7196 N N   . LEU D 1 314 ? -10.794 -9.995  -29.917 1.00 100.21 ? 316 LEU A N   1 
ATOM   7197 C CA  . LEU D 1 314 ? -9.838  -10.568 -28.987 1.00 108.72 ? 316 LEU A CA  1 
ATOM   7198 C C   . LEU D 1 314 ? -8.834  -9.505  -28.560 1.00 112.56 ? 316 LEU A C   1 
ATOM   7199 O O   . LEU D 1 314 ? -8.405  -8.674  -29.367 1.00 107.17 ? 316 LEU A O   1 
ATOM   7200 C CB  . LEU D 1 314 ? -9.113  -11.751 -29.629 1.00 110.22 ? 316 LEU A CB  1 
ATOM   7201 C CG  . LEU D 1 314 ? -9.916  -13.040 -29.796 1.00 113.74 ? 316 LEU A CG  1 
ATOM   7202 C CD1 . LEU D 1 314 ? -9.068  -14.104 -30.471 1.00 104.92 ? 316 LEU A CD1 1 
ATOM   7203 C CD2 . LEU D 1 314 ? -10.417 -13.531 -28.449 1.00 102.54 ? 316 LEU A CD2 1 
ATOM   7204 N N   . ALA D 1 315 ? -8.467  -9.531  -27.283 1.00 111.99 ? 317 ALA A N   1 
ATOM   7205 C CA  . ALA D 1 315 ? -7.511  -8.581  -26.733 1.00 107.90 ? 317 ALA A CA  1 
ATOM   7206 C C   . ALA D 1 315 ? -6.097  -9.124  -26.896 1.00 107.29 ? 317 ALA A C   1 
ATOM   7207 O O   . ALA D 1 315 ? -5.805  -10.250 -26.481 1.00 105.60 ? 317 ALA A O   1 
ATOM   7208 C CB  . ALA D 1 315 ? -7.810  -8.306  -25.259 1.00 110.12 ? 317 ALA A CB  1 
ATOM   7209 N N   . THR D 1 316 ? -5.223  -8.321  -27.510 1.00 91.06  ? 318 THR A N   1 
ATOM   7210 C CA  . THR D 1 316 ? -3.846  -8.729  -27.764 1.00 85.56  ? 318 THR A CA  1 
ATOM   7211 C C   . THR D 1 316 ? -2.825  -7.734  -27.228 1.00 88.19  ? 318 THR A C   1 
ATOM   7212 O O   . THR D 1 316 ? -1.628  -7.899  -27.485 1.00 116.49 ? 318 THR A O   1 
ATOM   7213 C CB  . THR D 1 316 ? -3.605  -8.934  -29.266 1.00 85.96  ? 318 THR A CB  1 
ATOM   7214 O OG1 . THR D 1 316 ? -3.705  -7.678  -29.948 1.00 72.29  ? 318 THR A OG1 1 
ATOM   7215 C CG2 . THR D 1 316 ? -4.622  -9.895  -29.841 1.00 104.04 ? 318 THR A CG2 1 
ATOM   7216 N N   . GLY D 1 317 ? -3.255  -6.709  -26.496 1.00 86.62  ? 319 GLY A N   1 
ATOM   7217 C CA  . GLY D 1 317 ? -2.349  -5.682  -26.027 1.00 101.04 ? 319 GLY A CA  1 
ATOM   7218 C C   . GLY D 1 317 ? -2.646  -5.285  -24.596 1.00 106.18 ? 319 GLY A C   1 
ATOM   7219 O O   . GLY D 1 317 ? -3.541  -5.831  -23.947 1.00 101.55 ? 319 GLY A O   1 
ATOM   7220 N N   . LEU D 1 318 ? -1.870  -4.316  -24.119 1.00 105.53 ? 320 LEU A N   1 
ATOM   7221 C CA  . LEU D 1 318 ? -2.005  -3.800  -22.768 1.00 110.36 ? 320 LEU A CA  1 
ATOM   7222 C C   . LEU D 1 318 ? -3.155  -2.798  -22.695 1.00 120.26 ? 320 LEU A C   1 
ATOM   7223 O O   . LEU D 1 318 ? -3.607  -2.253  -23.707 1.00 115.75 ? 320 LEU A O   1 
ATOM   7224 C CB  . LEU D 1 318 ? -0.702  -3.131  -22.320 1.00 119.00 ? 320 LEU A CB  1 
ATOM   7225 C CG  . LEU D 1 318 ? 0.533   -4.028  -22.172 1.00 110.91 ? 320 LEU A CG  1 
ATOM   7226 C CD1 . LEU D 1 318 ? 1.782   -3.218  -21.866 1.00 85.66  ? 320 LEU A CD1 1 
ATOM   7227 C CD2 . LEU D 1 318 ? 0.316   -5.071  -21.097 1.00 132.60 ? 320 LEU A CD2 1 
ATOM   7228 N N   . ARG D 1 319 ? -3.629  -2.561  -21.473 1.00 116.54 ? 321 ARG A N   1 
ATOM   7229 C CA  . ARG D 1 319 ? -4.604  -1.502  -21.241 1.00 107.44 ? 321 ARG A CA  1 
ATOM   7230 C C   . ARG D 1 319 ? -3.997  -0.153  -21.606 1.00 109.02 ? 321 ARG A C   1 
ATOM   7231 O O   . ARG D 1 319 ? -3.012  0.280   -20.999 1.00 104.02 ? 321 ARG A O   1 
ATOM   7232 C CB  . ARG D 1 319 ? -5.054  -1.504  -19.781 1.00 85.36  ? 321 ARG A CB  1 
ATOM   7233 C CG  . ARG D 1 319 ? -6.230  -2.418  -19.474 1.00 110.55 ? 321 ARG A CG  1 
ATOM   7234 C CD  . ARG D 1 319 ? -6.695  -2.207  -18.040 1.00 105.28 ? 321 ARG A CD  1 
ATOM   7235 N NE  . ARG D 1 319 ? -7.999  -2.799  -17.766 1.00 119.67 ? 321 ARG A NE  1 
ATOM   7236 C CZ  . ARG D 1 319 ? -8.221  -3.730  -16.847 1.00 135.50 ? 321 ARG A CZ  1 
ATOM   7237 N NH1 . ARG D 1 319 ? -7.240  -4.216  -16.104 1.00 136.26 ? 321 ARG A NH1 1 
ATOM   7238 N NH2 . ARG D 1 319 ? -9.460  -4.178  -16.664 1.00 153.17 ? 321 ARG A NH2 1 
ATOM   7239 N N   . ASN D 1 320 ? -4.584  0.512   -22.597 1.00 117.31 ? 322 ASN A N   1 
ATOM   7240 C CA  . ASN D 1 320 ? -4.029  1.759   -23.117 1.00 127.86 ? 322 ASN A CA  1 
ATOM   7241 C C   . ASN D 1 320 ? -4.374  2.893   -22.162 1.00 129.11 ? 322 ASN A C   1 
ATOM   7242 O O   . ASN D 1 320 ? -5.487  3.424   -22.181 1.00 120.06 ? 322 ASN A O   1 
ATOM   7243 C CB  . ASN D 1 320 ? -4.554  2.039   -24.520 1.00 131.92 ? 322 ASN A CB  1 
ATOM   7244 C CG  . ASN D 1 320 ? -3.722  3.070   -25.254 1.00 135.14 ? 322 ASN A CG  1 
ATOM   7245 O OD1 . ASN D 1 320 ? -2.718  3.558   -24.733 1.00 125.04 ? 322 ASN A OD1 1 
ATOM   7246 N ND2 . ASN D 1 320 ? -4.133  3.407   -26.470 1.00 160.48 ? 322 ASN A ND2 1 
ATOM   7247 N N   . VAL D 1 321 ? -3.414  3.268   -21.323 1.00 130.01 ? 323 VAL A N   1 
ATOM   7248 C CA  . VAL D 1 321 ? -3.589  4.377   -20.389 1.00 128.82 ? 323 VAL A CA  1 
ATOM   7249 C C   . VAL D 1 321 ? -2.509  5.422   -20.642 1.00 136.54 ? 323 VAL A C   1 
ATOM   7250 O O   . VAL D 1 321 ? -1.411  5.329   -20.073 1.00 137.21 ? 323 VAL A O   1 
ATOM   7251 C CB  . VAL D 1 321 ? -3.552  3.895   -18.931 1.00 115.72 ? 323 VAL A CB  1 
ATOM   7252 C CG1 . VAL D 1 321 ? -3.836  5.056   -17.986 1.00 112.07 ? 323 VAL A CG1 1 
ATOM   7253 C CG2 . VAL D 1 321 ? -4.550  2.770   -18.720 1.00 129.80 ? 323 VAL A CG2 1 
ATOM   7254 N N   . PRO D 1 322 ? -2.766  6.421   -21.480 1.00 141.95 ? 324 PRO A N   1 
ATOM   7255 C CA  . PRO D 1 322 ? -1.787  7.498   -21.653 1.00 125.86 ? 324 PRO A CA  1 
ATOM   7256 C C   . PRO D 1 322 ? -1.752  8.401   -20.428 1.00 155.95 ? 324 PRO A C   1 
ATOM   7257 O O   . PRO D 1 322 ? -2.750  8.553   -19.718 1.00 154.98 ? 324 PRO A O   1 
ATOM   7258 C CB  . PRO D 1 322 ? -2.298  8.244   -22.890 1.00 116.75 ? 324 PRO A CB  1 
ATOM   7259 C CG  . PRO D 1 322 ? -3.774  7.985   -22.886 1.00 123.17 ? 324 PRO A CG  1 
ATOM   7260 C CD  . PRO D 1 322 ? -3.945  6.592   -22.347 1.00 139.12 ? 324 PRO A CD  1 
ATOM   7261 N N   . SER D 1 323 ? -0.575  8.985   -20.188 1.00 175.37 ? 325 SER A N   1 
ATOM   7262 C CA  . SER D 1 323 ? -0.294  9.914   -19.076 1.00 161.15 ? 325 SER A CA  1 
ATOM   7263 C C   . SER D 1 323 ? -1.152  9.734   -17.820 1.00 170.87 ? 325 SER A C   1 
ATOM   7264 O O   . SER D 1 323 ? -2.104  10.482  -17.589 1.00 167.43 ? 325 SER A O   1 
ATOM   7265 C CB  . SER D 1 323 ? -0.418  11.364  -19.564 1.00 144.36 ? 325 SER A CB  1 
ATOM   7266 O OG  . SER D 1 323 ? -1.712  11.642  -20.070 1.00 158.41 ? 325 SER A OG  1 
HETATM 7267 C C1  . NAG E 4 .   ? -37.739 -49.126 -69.980 1.00 30.00  ? 1   NAG S C1  1 
HETATM 7268 C C2  . NAG E 4 .   ? -37.244 -48.273 -71.147 1.00 30.00  ? 1   NAG S C2  1 
HETATM 7269 C C3  . NAG E 4 .   ? -35.945 -48.854 -71.689 1.00 30.00  ? 1   NAG S C3  1 
HETATM 7270 C C4  . NAG E 4 .   ? -34.915 -49.025 -70.581 1.00 30.00  ? 1   NAG S C4  1 
HETATM 7271 C C5  . NAG E 4 .   ? -35.504 -49.847 -69.437 1.00 30.00  ? 1   NAG S C5  1 
HETATM 7272 C C6  . NAG E 4 .   ? -34.605 -49.897 -68.222 1.00 30.00  ? 1   NAG S C6  1 
HETATM 7273 C C7  . NAG E 4 .   ? -39.489 -47.826 -72.036 1.00 30.00  ? 1   NAG S C7  1 
HETATM 7274 C C8  . NAG E 4 .   ? -39.711 -46.507 -71.361 1.00 30.00  ? 1   NAG S C8  1 
HETATM 7275 N N2  . NAG E 4 .   ? -38.218 -48.189 -72.214 1.00 30.00  ? 1   NAG S N2  1 
HETATM 7276 O O3  . NAG E 4 .   ? -35.450 -48.007 -72.716 1.00 30.00  ? 1   NAG S O3  1 
HETATM 7277 O O4  . NAG E 4 .   ? -33.793 -49.712 -71.135 1.00 30.00  ? 1   NAG S O4  1 
HETATM 7278 O O5  . NAG E 4 .   ? -36.745 -49.272 -68.979 1.00 30.00  ? 1   NAG S O5  1 
HETATM 7279 O O6  . NAG E 4 .   ? -35.150 -50.753 -67.222 1.00 30.00  ? 1   NAG S O6  1 
HETATM 7280 O O7  . NAG E 4 .   ? -40.421 -48.528 -72.417 1.00 30.00  ? 1   NAG S O7  1 
HETATM 7281 C C1  . NAG E 4 .   ? -34.039 -51.130 -71.294 1.00 30.00  ? 2   NAG S C1  1 
HETATM 7282 C C2  . NAG E 4 .   ? -32.808 -51.971 -70.974 1.00 30.00  ? 2   NAG S C2  1 
HETATM 7283 C C3  . NAG E 4 .   ? -33.202 -53.440 -70.854 1.00 30.00  ? 2   NAG S C3  1 
HETATM 7284 C C4  . NAG E 4 .   ? -34.011 -53.896 -72.067 1.00 30.00  ? 2   NAG S C4  1 
HETATM 7285 C C5  . NAG E 4 .   ? -35.194 -52.965 -72.346 1.00 30.00  ? 2   NAG S C5  1 
HETATM 7286 C C6  . NAG E 4 .   ? -36.300 -53.031 -71.314 1.00 30.00  ? 2   NAG S C6  1 
HETATM 7287 C C7  . NAG E 4 .   ? -30.540 -52.181 -71.926 1.00 30.00  ? 2   NAG S C7  1 
HETATM 7288 C C8  . NAG E 4 .   ? -29.707 -51.942 -73.147 1.00 30.00  ? 2   NAG S C8  1 
HETATM 7289 N N2  . NAG E 4 .   ? -31.806 -51.766 -71.998 1.00 30.00  ? 2   NAG S N2  1 
HETATM 7290 O O3  . NAG E 4 .   ? -33.894 -53.662 -69.632 1.00 30.00  ? 2   NAG S O3  1 
HETATM 7291 O O4  . NAG E 4 .   ? -33.164 -53.925 -73.212 1.00 30.00  ? 2   NAG S O4  1 
HETATM 7292 O O5  . NAG E 4 .   ? -34.768 -51.588 -72.421 1.00 30.00  ? 2   NAG S O5  1 
HETATM 7293 O O6  . NAG E 4 .   ? -36.760 -54.367 -71.140 1.00 30.00  ? 2   NAG S O6  1 
HETATM 7294 O O7  . NAG E 4 .   ? -30.084 -52.720 -70.923 1.00 30.00  ? 2   NAG S O7  1 
HETATM 7295 C C1  . BMA E 4 .   ? -32.311 -55.078 -73.113 1.00 30.00  ? 3   BMA S C1  1 
HETATM 7296 C C2  . BMA E 4 .   ? -33.078 -56.335 -73.458 1.00 30.00  ? 3   BMA S C2  1 
HETATM 7297 C C3  . BMA E 4 .   ? -32.176 -57.544 -73.374 1.00 30.00  ? 3   BMA S C3  1 
HETATM 7298 C C4  . BMA E 4 .   ? -30.958 -57.343 -74.256 1.00 30.00  ? 3   BMA S C4  1 
HETATM 7299 C C5  . BMA E 4 .   ? -30.240 -56.048 -73.885 1.00 30.00  ? 3   BMA S C5  1 
HETATM 7300 C C6  . BMA E 4 .   ? -29.104 -55.714 -74.823 1.00 30.00  ? 3   BMA S C6  1 
HETATM 7301 O O2  . BMA E 4 .   ? -33.655 -56.219 -74.755 1.00 30.00  ? 3   BMA S O2  1 
HETATM 7302 O O3  . BMA E 4 .   ? -32.893 -58.704 -73.791 1.00 30.00  ? 3   BMA S O3  1 
HETATM 7303 O O4  . BMA E 4 .   ? -30.061 -58.437 -74.094 1.00 30.00  ? 3   BMA S O4  1 
HETATM 7304 O O5  . BMA E 4 .   ? -31.162 -54.943 -73.951 1.00 30.00  ? 3   BMA S O5  1 
HETATM 7305 O O6  . BMA E 4 .   ? -28.136 -56.758 -74.868 1.00 30.00  ? 3   BMA S O6  1 
HETATM 7306 C C1  . NAG F 5 .   ? -20.186 2.846   -21.374 1.00 30.00  ? 1   NAG C C1  1 
HETATM 7307 C C2  . NAG F 5 .   ? -20.675 3.642   -22.587 1.00 30.00  ? 1   NAG C C2  1 
HETATM 7308 C C3  . NAG F 5 .   ? -19.546 3.884   -23.584 1.00 30.00  ? 1   NAG C C3  1 
HETATM 7309 C C4  . NAG F 5 .   ? -18.273 4.369   -22.904 1.00 30.00  ? 1   NAG C C4  1 
HETATM 7310 C C5  . NAG F 5 .   ? -17.918 3.423   -21.762 1.00 30.00  ? 1   NAG C C5  1 
HETATM 7311 C C6  . NAG F 5 .   ? -16.678 3.823   -20.999 1.00 30.00  ? 1   NAG C C6  1 
HETATM 7312 C C7  . NAG F 5 .   ? -22.026 1.702   -23.295 1.00 30.00  ? 1   NAG C C7  1 
HETATM 7313 C C8  . NAG F 5 .   ? -23.206 1.225   -22.504 1.00 30.00  ? 1   NAG C C8  1 
HETATM 7314 N N2  . NAG F 5 .   ? -21.795 3.015   -23.262 1.00 30.00  ? 1   NAG C N2  1 
HETATM 7315 O O3  . NAG F 5 .   ? -20.006 4.830   -24.538 1.00 30.00  ? 1   NAG C O3  1 
HETATM 7316 O O4  . NAG F 5 .   ? -17.230 4.341   -23.873 1.00 30.00  ? 1   NAG C O4  1 
HETATM 7317 O O5  . NAG F 5 .   ? -19.005 3.401   -20.819 1.00 30.00  ? 1   NAG C O5  1 
HETATM 7318 O O6  . NAG F 5 .   ? -15.994 2.676   -20.503 1.00 30.00  ? 1   NAG C O6  1 
HETATM 7319 O O7  . NAG F 5 .   ? -21.327 0.934   -23.948 1.00 30.00  ? 1   NAG C O7  1 
HETATM 7320 C C1  . NAG F 5 .   ? -16.638 5.645   -24.003 1.00 30.00  ? 2   NAG C C1  1 
HETATM 7321 C C2  . NAG F 5 .   ? -15.185 5.584   -24.466 1.00 30.00  ? 2   NAG C C2  1 
HETATM 7322 C C3  . NAG F 5 .   ? -14.841 6.889   -25.168 1.00 30.00  ? 2   NAG C C3  1 
HETATM 7323 C C4  . NAG F 5 .   ? -15.735 7.081   -26.385 1.00 30.00  ? 2   NAG C C4  1 
HETATM 7324 C C5  . NAG F 5 .   ? -17.207 6.888   -26.019 1.00 30.00  ? 2   NAG C C5  1 
HETATM 7325 C C6  . NAG F 5 .   ? -17.861 5.726   -26.731 1.00 30.00  ? 2   NAG C C6  1 
HETATM 7326 C C7  . NAG F 5 .   ? -13.689 4.143   -23.212 1.00 30.00  ? 2   NAG C C7  1 
HETATM 7327 C C8  . NAG F 5 .   ? -12.848 3.983   -21.983 1.00 30.00  ? 2   NAG C C8  1 
HETATM 7328 N N2  . NAG F 5 .   ? -14.275 5.328   -23.371 1.00 30.00  ? 2   NAG C N2  1 
HETATM 7329 O O3  . NAG F 5 .   ? -13.470 6.885   -25.537 1.00 30.00  ? 2   NAG C O3  1 
HETATM 7330 O O4  . NAG F 5 .   ? -15.556 8.404   -26.881 1.00 30.00  ? 2   NAG C O4  1 
HETATM 7331 O O5  . NAG F 5 .   ? -17.401 6.684   -24.600 1.00 30.00  ? 2   NAG C O5  1 
HETATM 7332 O O6  . NAG F 5 .   ? -19.274 5.892   -26.794 1.00 30.00  ? 2   NAG C O6  1 
HETATM 7333 O O7  . NAG F 5 .   ? -13.834 3.238   -24.027 1.00 30.00  ? 2   NAG C O7  1 
HETATM 7334 C C1  . NAG G 6 .   ? -1.035  6.691   -35.003 1.00 161.76 ? 601 NAG A C1  1 
HETATM 7335 C C2  . NAG G 6 .   ? -1.442  7.734   -36.044 1.00 161.76 ? 601 NAG A C2  1 
HETATM 7336 C C3  . NAG G 6 .   ? -1.385  9.132   -35.434 1.00 161.76 ? 601 NAG A C3  1 
HETATM 7337 C C4  . NAG G 6 .   ? -0.003  9.427   -34.865 1.00 161.76 ? 601 NAG A C4  1 
HETATM 7338 C C5  . NAG G 6 .   ? 0.473   8.253   -34.016 1.00 161.76 ? 601 NAG A C5  1 
HETATM 7339 C C6  . NAG G 6 .   ? 0.950   8.677   -32.648 1.00 161.76 ? 601 NAG A C6  1 
HETATM 7340 C C7  . NAG G 6 .   ? -1.000  8.144   -38.413 1.00 161.76 ? 601 NAG A C7  1 
HETATM 7341 C C8  . NAG G 6 .   ? 0.084   8.722   -39.270 1.00 161.76 ? 601 NAG A C8  1 
HETATM 7342 N N2  . NAG G 6 .   ? -0.615  7.662   -37.230 1.00 161.76 ? 601 NAG A N2  1 
HETATM 7343 O O3  . NAG G 6 .   ? -2.385  9.247   -34.432 1.00 161.76 ? 601 NAG A O3  1 
HETATM 7344 O O4  . NAG G 6 .   ? 0.917   9.622   -35.934 1.00 161.76 ? 601 NAG A O4  1 
HETATM 7345 O O5  . NAG G 6 .   ? -0.615  7.332   -33.810 1.00 161.76 ? 601 NAG A O5  1 
HETATM 7346 O O6  . NAG G 6 .   ? 0.036   9.594   -32.050 1.00 161.76 ? 601 NAG A O6  1 
HETATM 7347 O O7  . NAG G 6 .   ? -2.171  8.114   -38.776 1.00 161.76 ? 601 NAG A O7  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   . ILE A 337 ? 2.0865 1.8801 1.7576 -0.0449 -0.0185 -0.0786 10  ILE B N   
2    C CA  . ILE A 337 ? 2.0884 1.8755 1.7687 -0.0385 -0.0205 -0.0790 10  ILE B CA  
3    C C   . ILE A 337 ? 2.3288 2.1256 2.0140 -0.0331 -0.0162 -0.0851 10  ILE B C   
4    O O   . ILE A 337 ? 2.5435 2.3469 2.2339 -0.0333 -0.0132 -0.0823 10  ILE B O   
5    C CB  . ILE A 337 ? 2.0136 1.7951 1.7007 -0.0405 -0.0223 -0.0701 10  ILE B CB  
6    C CG1 . ILE A 337 ? 1.9112 1.6825 1.5949 -0.0452 -0.0270 -0.0643 10  ILE B CG1 
7    C CG2 . ILE A 337 ? 2.1773 1.9536 1.8738 -0.0343 -0.0241 -0.0704 10  ILE B CG2 
8    C CD1 . ILE A 337 ? 1.9059 1.6737 1.5956 -0.0482 -0.0280 -0.0557 10  ILE B CD1 
9    N N   . GLU A 338 ? 2.1757 1.9734 1.8594 -0.0283 -0.0160 -0.0936 11  GLU B N   
10   C CA  . GLU A 338 ? 2.3371 2.1439 2.0259 -0.0228 -0.0122 -0.1001 11  GLU B CA  
11   C C   . GLU A 338 ? 2.4287 2.2293 2.1278 -0.0162 -0.0148 -0.1010 11  GLU B C   
12   O O   . GLU A 338 ? 2.3554 2.1623 2.0598 -0.0111 -0.0125 -0.1066 11  GLU B O   
13   C CB  . GLU A 338 ? 2.1777 1.9905 1.8597 -0.0212 -0.0100 -0.1096 11  GLU B CB  
14   C CG  . GLU A 338 ? 2.0882 1.9107 1.7604 -0.0276 -0.0063 -0.1094 11  GLU B CG  
15   C CD  . GLU A 338 ? 2.3123 2.1410 1.9774 -0.0261 -0.0041 -0.1192 11  GLU B CD  
16   O OE1 . GLU A 338 ? 2.2964 2.1198 1.9639 -0.0202 -0.0062 -0.1261 11  GLU B OE1 
17   O OE2 . GLU A 338 ? 2.4625 2.3016 2.1198 -0.0308 -0.0004 -0.1200 11  GLU B OE2 
18   N N   . GLY A 339 ? 2.3592 2.1481 2.0616 -0.0163 -0.0198 -0.0954 12  GLY B N   
19   C CA  . GLY A 339 ? 2.0648 1.8478 1.7768 -0.0107 -0.0229 -0.0954 12  GLY B CA  
20   C C   . GLY A 339 ? 1.8663 1.6448 1.5843 -0.0124 -0.0246 -0.0866 12  GLY B C   
21   O O   . GLY A 339 ? 2.2095 1.9816 1.9245 -0.0169 -0.0268 -0.0804 12  GLY B O   
22   N N   . GLY A 340 ? 1.5305 1.3124 1.2572 -0.0088 -0.0236 -0.0860 13  GLY B N   
23   C CA  . GLY A 340 ? 1.5901 1.3687 1.3226 -0.0102 -0.0249 -0.0783 13  GLY B CA  
24   C C   . GLY A 340 ? 1.5650 1.3318 1.3018 -0.0081 -0.0308 -0.0754 13  GLY B C   
25   O O   . GLY A 340 ? 1.6809 1.4426 1.4186 -0.0042 -0.0341 -0.0799 13  GLY B O   
26   N N   . TRP A 341 ? 1.5337 1.2965 1.2735 -0.0107 -0.0322 -0.0678 14  TRP B N   
27   C CA  . TRP A 341 ? 1.4489 1.2012 1.1927 -0.0096 -0.0377 -0.0636 14  TRP B CA  
28   C C   . TRP A 341 ? 1.7133 1.4675 1.4662 -0.0073 -0.0380 -0.0603 14  TRP B C   
29   O O   . TRP A 341 ? 1.9190 1.6769 1.6735 -0.0101 -0.0355 -0.0556 14  TRP B O   
30   C CB  . TRP A 341 ? 1.6501 1.3959 1.3898 -0.0150 -0.0395 -0.0573 14  TRP B CB  
31   C CG  . TRP A 341 ? 1.4202 1.1612 1.1517 -0.0170 -0.0413 -0.0597 14  TRP B CG  
32   C CD1 . TRP A 341 ? 1.6378 1.3799 1.3649 -0.0146 -0.0413 -0.0671 14  TRP B CD1 
33   C CD2 . TRP A 341 ? 1.3151 1.0497 1.0418 -0.0221 -0.0434 -0.0546 14  TRP B CD2 
34   N NE1 . TRP A 341 ? 1.7191 1.4559 1.4383 -0.0181 -0.0433 -0.0671 14  TRP B NE1 
35   C CE2 . TRP A 341 ? 1.6889 1.4209 1.4079 -0.0228 -0.0447 -0.0592 14  TRP B CE2 
36   C CE3 . TRP A 341 ? 1.5247 1.2557 1.2534 -0.0262 -0.0443 -0.0468 14  TRP B CE3 
37   C CZ2 . TRP A 341 ? 1.9304 1.6562 1.6433 -0.0277 -0.0472 -0.0557 14  TRP B CZ2 
38   C CZ3 . TRP A 341 ? 1.6658 1.3906 1.3892 -0.0307 -0.0467 -0.0434 14  TRP B CZ3 
39   C CH2 . TRP A 341 ? 1.7572 1.4794 1.4727 -0.0316 -0.0482 -0.0476 14  TRP B CH2 
40   N N   . THR A 342 ? 1.6959 1.4474 1.4548 -0.0023 -0.0412 -0.0627 15  THR B N   
41   C CA  . THR A 342 ? 1.5395 1.2924 1.3070 -0.0004 -0.0422 -0.0591 15  THR B CA  
42   C C   . THR A 342 ? 1.4054 1.1512 1.1750 -0.0029 -0.0455 -0.0513 15  THR B C   
43   O O   . THR A 342 ? 1.4343 1.1831 1.2085 -0.0038 -0.0445 -0.0468 15  THR B O   
44   C CB  . THR A 342 ? 1.5347 1.2867 1.3088 0.0053  -0.0453 -0.0634 15  THR B CB  
45   O OG1 . THR A 342 ? 1.7049 1.4468 1.4782 0.0067  -0.0508 -0.0643 15  THR B OG1 
46   C CG2 . THR A 342 ? 1.4943 1.2544 1.2674 0.0081  -0.0415 -0.0713 15  THR B CG2 
47   N N   . GLY A 343 ? 1.4520 1.1886 1.2184 -0.0042 -0.0495 -0.0497 16  GLY B N   
48   C CA  . GLY A 343 ? 1.6459 1.3757 1.4149 -0.0063 -0.0529 -0.0424 16  GLY B CA  
49   C C   . GLY A 343 ? 2.0446 1.7772 1.8120 -0.0111 -0.0496 -0.0371 16  GLY B C   
50   O O   . GLY A 343 ? 2.0185 1.7481 1.7898 -0.0125 -0.0512 -0.0311 16  GLY B O   
51   N N   . MET A 344 ? 2.0218 1.7601 1.7839 -0.0137 -0.0450 -0.0392 17  MET B N   
52   C CA  . MET A 344 ? 2.1685 1.9092 1.9293 -0.0185 -0.0420 -0.0346 17  MET B CA  
53   C C   . MET A 344 ? 2.0739 1.8226 1.8397 -0.0181 -0.0385 -0.0334 17  MET B C   
54   O O   . MET A 344 ? 2.3037 2.0597 2.0677 -0.0200 -0.0341 -0.0345 17  MET B O   
55   C CB  . MET A 344 ? 2.1001 1.8433 1.8533 -0.0219 -0.0393 -0.0369 17  MET B CB  
56   C CG  . MET A 344 ? 2.1207 1.8627 1.8725 -0.0273 -0.0383 -0.0315 17  MET B CG  
57   S SD  . MET A 344 ? 3.0332 2.7631 2.7857 -0.0291 -0.0437 -0.0256 17  MET B SD  
58   C CE  . MET A 344 ? 2.4115 2.1363 2.1555 -0.0298 -0.0462 -0.0296 17  MET B CE  
59   N N   . VAL A 345 ? 2.0138 1.7614 1.7861 -0.0158 -0.0407 -0.0309 18  VAL B N   
60   C CA  . VAL A 345 ? 1.7937 1.5488 1.5707 -0.0154 -0.0378 -0.0298 18  VAL B CA  
61   C C   . VAL A 345 ? 1.9936 1.7505 1.7709 -0.0196 -0.0353 -0.0252 18  VAL B C   
62   O O   . VAL A 345 ? 2.0826 1.8464 1.8622 -0.0201 -0.0320 -0.0250 18  VAL B O   
63   C CB  . VAL A 345 ? 1.8254 1.5791 1.6091 -0.0119 -0.0414 -0.0284 18  VAL B CB  
64   C CG1 . VAL A 345 ? 1.7703 1.5316 1.5587 -0.0118 -0.0388 -0.0268 18  VAL B CG1 
65   C CG2 . VAL A 345 ? 1.8714 1.6239 1.6558 -0.0075 -0.0438 -0.0336 18  VAL B CG2 
66   N N   . ASP A 346 ? 1.8232 1.5737 1.5983 -0.0227 -0.0369 -0.0218 19  ASP B N   
67   C CA  . ASP A 346 ? 1.8517 1.6031 1.6281 -0.0265 -0.0349 -0.0175 19  ASP B CA  
68   C C   . ASP A 346 ? 1.8407 1.5984 1.6140 -0.0292 -0.0305 -0.0193 19  ASP B C   
69   O O   . ASP A 346 ? 1.9511 1.7153 1.7271 -0.0299 -0.0274 -0.0191 19  ASP B O   
70   C CB  . ASP A 346 ? 1.9657 1.7084 1.7412 -0.0290 -0.0381 -0.0133 19  ASP B CB  
71   C CG  . ASP A 346 ? 2.4253 2.1685 2.2038 -0.0326 -0.0364 -0.0088 19  ASP B CG  
72   O OD1 . ASP A 346 ? 2.1587 1.9088 1.9397 -0.0332 -0.0329 -0.0091 19  ASP B OD1 
73   O OD2 . ASP A 346 ? 2.7821 2.5188 2.5609 -0.0349 -0.0388 -0.0051 19  ASP B OD2 
74   N N   . GLY A 347 ? 1.8628 1.6186 1.6304 -0.0312 -0.0305 -0.0210 20  GLY B N   
75   C CA  . GLY A 347 ? 1.7363 1.4978 1.5009 -0.0344 -0.0270 -0.0220 20  GLY B CA  
76   C C   . GLY A 347 ? 1.7333 1.4983 1.4922 -0.0334 -0.0258 -0.0271 20  GLY B C   
77   O O   . GLY A 347 ? 1.9571 1.7188 1.7141 -0.0304 -0.0281 -0.0302 20  GLY B O   
78   N N   . TRP A 348 ? 1.5681 1.3402 1.3248 -0.0360 -0.0223 -0.0282 21  TRP B N   
79   C CA  . TRP A 348 ? 1.5557 1.3326 1.3068 -0.0356 -0.0206 -0.0330 21  TRP B CA  
80   C C   . TRP A 348 ? 1.5717 1.3426 1.3166 -0.0375 -0.0232 -0.0334 21  TRP B C   
81   O O   . TRP A 348 ? 1.4657 1.2365 1.2068 -0.0350 -0.0238 -0.0381 21  TRP B O   
82   C CB  . TRP A 348 ? 1.5992 1.3849 1.3493 -0.0389 -0.0167 -0.0330 21  TRP B CB  
83   C CG  . TRP A 348 ? 1.5086 1.3018 1.2636 -0.0369 -0.0138 -0.0340 21  TRP B CG  
84   C CD1 . TRP A 348 ? 1.5342 1.3292 1.2928 -0.0321 -0.0137 -0.0366 21  TRP B CD1 
85   C CD2 . TRP A 348 ? 1.7062 1.5060 1.4630 -0.0399 -0.0109 -0.0323 21  TRP B CD2 
86   N NE1 . TRP A 348 ? 1.4957 1.2982 1.2579 -0.0320 -0.0108 -0.0365 21  TRP B NE1 
87   C CE2 . TRP A 348 ? 1.6022 1.4077 1.3634 -0.0367 -0.0090 -0.0341 21  TRP B CE2 
88   C CE3 . TRP A 348 ? 1.6852 1.4867 1.4409 -0.0451 -0.0100 -0.0293 21  TRP B CE3 
89   C CZ2 . TRP A 348 ? 1.4097 1.2221 1.1735 -0.0385 -0.0062 -0.0331 21  TRP B CZ2 
90   C CZ3 . TRP A 348 ? 1.3817 1.1899 1.1405 -0.0467 -0.0074 -0.0284 21  TRP B CZ3 
91   C CH2 . TRP A 348 ? 1.3209 1.1346 1.0836 -0.0434 -0.0055 -0.0304 21  TRP B CH2 
92   N N   . TYR A 349 ? 1.5698 1.3357 1.3138 -0.0419 -0.0248 -0.0286 22  TYR B N   
93   C CA  . TYR A 349 ? 1.5387 1.2998 1.2764 -0.0450 -0.0271 -0.0282 22  TYR B CA  
94   C C   . TYR A 349 ? 1.6937 1.4440 1.4328 -0.0446 -0.0317 -0.0249 22  TYR B C   
95   O O   . TYR A 349 ? 1.6687 1.4152 1.4128 -0.0462 -0.0328 -0.0199 22  TYR B O   
96   C CB  . TYR A 349 ? 1.3242 1.0883 1.0598 -0.0511 -0.0257 -0.0248 22  TYR B CB  
97   C CG  . TYR A 349 ? 1.4605 1.2353 1.1941 -0.0513 -0.0216 -0.0282 22  TYR B CG  
98   C CD1 . TYR A 349 ? 2.0484 1.8273 1.7749 -0.0517 -0.0206 -0.0325 22  TYR B CD1 
99   C CD2 . TYR A 349 ? 1.2747 1.0559 1.0136 -0.0510 -0.0186 -0.0275 22  TYR B CD2 
100  C CE1 . TYR A 349 ? 2.1209 1.9101 1.8460 -0.0517 -0.0167 -0.0356 22  TYR B CE1 
101  C CE2 . TYR A 349 ? 1.4692 1.2604 1.2066 -0.0511 -0.0150 -0.0305 22  TYR B CE2 
102  C CZ  . TYR A 349 ? 1.8728 1.6680 1.6034 -0.0514 -0.0140 -0.0344 22  TYR B CZ  
103  O OH  . TYR A 349 ? 2.0353 1.8409 1.7643 -0.0516 -0.0104 -0.0374 22  TYR B OH  
104  N N   . GLY A 350 ? 1.7626 1.5081 1.4974 -0.0426 -0.0343 -0.0280 23  GLY B N   
105  C CA  . GLY A 350 ? 1.7840 1.5191 1.5202 -0.0420 -0.0391 -0.0250 23  GLY B CA  
106  C C   . GLY A 350 ? 1.5754 1.3051 1.3043 -0.0430 -0.0421 -0.0272 23  GLY B C   
107  O O   . GLY A 350 ? 1.4783 1.2127 1.2011 -0.0430 -0.0403 -0.0323 23  GLY B O   
108  N N   . TYR A 351 ? 1.5334 1.2534 1.2631 -0.0439 -0.0466 -0.0232 24  TYR B N   
109  C CA  . TYR A 351 ? 1.6866 1.3994 1.4101 -0.0449 -0.0505 -0.0243 24  TYR B CA  
110  C C   . TYR A 351 ? 1.7514 1.4572 1.4781 -0.0400 -0.0546 -0.0255 24  TYR B C   
111  O O   . TYR A 351 ? 1.7616 1.4651 1.4957 -0.0381 -0.0557 -0.0219 24  TYR B O   
112  C CB  . TYR A 351 ? 1.8678 1.5745 1.5903 -0.0506 -0.0531 -0.0178 24  TYR B CB  
113  C CG  . TYR A 351 ? 1.8463 1.5591 1.5660 -0.0560 -0.0501 -0.0159 24  TYR B CG  
114  C CD1 . TYR A 351 ? 2.1019 1.8170 1.8129 -0.0594 -0.0498 -0.0184 24  TYR B CD1 
115  C CD2 . TYR A 351 ? 1.6121 1.3285 1.3381 -0.0581 -0.0477 -0.0116 24  TYR B CD2 
116  C CE1 . TYR A 351 ? 2.2897 2.0107 1.9985 -0.0647 -0.0475 -0.0161 24  TYR B CE1 
117  C CE2 . TYR A 351 ? 1.9933 1.7151 1.7175 -0.0632 -0.0455 -0.0097 24  TYR B CE2 
118  C CZ  . TYR A 351 ? 2.3324 2.0564 2.0480 -0.0666 -0.0456 -0.0117 24  TYR B CZ  
119  O OH  . TYR A 351 ? 2.2610 1.9906 1.9750 -0.0721 -0.0438 -0.0092 24  TYR B OH  
120  N N   . HIS A 352 ? 1.7228 1.4252 1.4442 -0.0381 -0.0569 -0.0306 25  HIS B N   
121  C CA  . HIS A 352 ? 1.6444 1.3389 1.3691 -0.0339 -0.0618 -0.0313 25  HIS B CA  
122  C C   . HIS A 352 ? 1.6881 1.3724 1.4093 -0.0371 -0.0669 -0.0276 25  HIS B C   
123  O O   . HIS A 352 ? 1.7755 1.4573 1.4890 -0.0383 -0.0684 -0.0313 25  HIS B O   
124  C CB  . HIS A 352 ? 1.5804 1.2773 1.3034 -0.0288 -0.0616 -0.0397 25  HIS B CB  
125  C CG  . HIS A 352 ? 1.4966 1.1853 1.2239 -0.0245 -0.0671 -0.0403 25  HIS B CG  
126  N ND1 . HIS A 352 ? 1.7538 1.4419 1.4901 -0.0212 -0.0684 -0.0375 25  HIS B ND1 
127  C CD2 . HIS A 352 ? 1.4336 1.1144 1.1576 -0.0231 -0.0719 -0.0434 25  HIS B CD2 
128  C CE1 . HIS A 352 ? 1.7070 1.3873 1.4458 -0.0180 -0.0740 -0.0383 25  HIS B CE1 
129  N NE2 . HIS A 352 ? 1.6880 1.3634 1.4195 -0.0189 -0.0762 -0.0421 25  HIS B NE2 
130  N N   . HIS A 353 ? 1.8588 1.5374 1.5856 -0.0386 -0.0695 -0.0203 26  HIS B N   
131  C CA  . HIS A 353 ? 2.1461 1.8148 1.8709 -0.0418 -0.0746 -0.0157 26  HIS B CA  
132  C C   . HIS A 353 ? 1.8548 1.5153 1.5797 -0.0380 -0.0801 -0.0181 26  HIS B C   
133  O O   . HIS A 353 ? 1.7432 1.4039 1.4740 -0.0332 -0.0811 -0.0195 26  HIS B O   
134  C CB  . HIS A 353 ? 2.4159 2.0820 2.1479 -0.0442 -0.0753 -0.0073 26  HIS B CB  
135  C CG  . HIS A 353 ? 2.7915 2.4648 2.5245 -0.0479 -0.0705 -0.0047 26  HIS B CG  
136  N ND1 . HIS A 353 ? 3.0321 2.7059 2.7595 -0.0533 -0.0698 -0.0034 26  HIS B ND1 
137  C CD2 . HIS A 353 ? 2.5595 2.2395 2.2986 -0.0473 -0.0665 -0.0032 26  HIS B CD2 
138  C CE1 . HIS A 353 ? 2.9032 2.5835 2.6337 -0.0557 -0.0657 -0.0012 26  HIS B CE1 
139  N NE2 . HIS A 353 ? 2.8303 2.5143 2.5678 -0.0520 -0.0636 -0.0012 26  HIS B NE2 
140  N N   . GLN A 354 ? 2.0083 1.6616 1.7266 -0.0404 -0.0840 -0.0185 27  GLN B N   
141  C CA  . GLN A 354 ? 2.1869 1.8310 1.9052 -0.0374 -0.0901 -0.0201 27  GLN B CA  
142  C C   . GLN A 354 ? 2.4442 2.0787 2.1597 -0.0419 -0.0951 -0.0145 27  GLN B C   
143  O O   . GLN A 354 ? 2.7096 2.3437 2.4169 -0.0462 -0.0949 -0.0154 27  GLN B O   
144  C CB  . GLN A 354 ? 2.2372 1.8829 1.9493 -0.0342 -0.0899 -0.0298 27  GLN B CB  
145  C CG  . GLN A 354 ? 2.2987 1.9530 2.0149 -0.0290 -0.0859 -0.0356 27  GLN B CG  
146  C CD  . GLN A 354 ? 2.3444 2.0008 2.0552 -0.0257 -0.0854 -0.0455 27  GLN B CD  
147  O OE1 . GLN A 354 ? 2.4630 2.1230 2.1785 -0.0204 -0.0845 -0.0505 27  GLN B OE1 
148  N NE2 . GLN A 354 ? 2.5590 2.2133 2.2602 -0.0288 -0.0861 -0.0485 27  GLN B NE2 
149  N N   . ASN A 355 ? 2.3116 1.9387 2.0338 -0.0412 -0.0997 -0.0084 28  ASN B N   
150  C CA  . ASN A 355 ? 2.4737 2.0908 2.1948 -0.0449 -0.1053 -0.0025 28  ASN B CA  
151  C C   . ASN A 355 ? 2.4742 2.0824 2.1973 -0.0412 -0.1119 -0.0036 28  ASN B C   
152  O O   . ASN A 355 ? 2.2906 1.9005 2.0177 -0.0359 -0.1122 -0.0077 28  ASN B O   
153  C CB  . ASN A 355 ? 2.3382 1.9551 2.0668 -0.0478 -0.1048 0.0067  28  ASN B CB  
154  C CG  . ASN A 355 ? 2.4538 2.0615 2.1813 -0.0525 -0.1098 0.0133  28  ASN B CG  
155  O OD1 . ASN A 355 ? 2.7197 2.3234 2.4390 -0.0554 -0.1120 0.0115  28  ASN B OD1 
156  N ND2 . ASN A 355 ? 2.1715 1.7764 1.9074 -0.0533 -0.1115 0.0211  28  ASN B ND2 
157  N N   . GLU A 356 ? 2.7251 2.3233 2.4457 -0.0442 -0.1177 0.0004  29  GLU B N   
158  C CA  . GLU A 356 ? 2.4947 2.0835 2.2188 -0.0412 -0.1248 0.0012  29  GLU B CA  
159  C C   . GLU A 356 ? 2.4149 2.0052 2.1502 -0.0375 -0.1255 0.0052  29  GLU B C   
160  O O   . GLU A 356 ? 2.2239 1.8092 1.9632 -0.0336 -0.1304 0.0041  29  GLU B O   
161  C CB  . GLU A 356 ? 2.3912 1.9696 2.1136 -0.0455 -0.1308 0.0076  29  GLU B CB  
162  C CG  . GLU A 356 ? 2.4437 2.0183 2.1550 -0.0493 -0.1324 0.0042  29  GLU B CG  
163  C CD  . GLU A 356 ? 2.4822 2.0510 2.1950 -0.0531 -0.1377 0.0118  29  GLU B CD  
164  O OE1 . GLU A 356 ? 2.4663 2.0450 2.1926 -0.0521 -0.1373 0.0194  29  GLU B OE1 
165  O OE2 . GLU A 356 ? 2.3940 1.9558 2.0973 -0.0562 -0.1412 0.0095  29  GLU B OE2 
166  N N   . GLN A 357 ? 2.3750 1.9719 2.1157 -0.0389 -0.1209 0.0101  30  GLN B N   
167  C CA  . GLN A 357 ? 2.3249 1.9235 2.0756 -0.0358 -0.1216 0.0141  30  GLN B CA  
168  C C   . GLN A 357 ? 2.3565 1.9628 2.1093 -0.0308 -0.1183 0.0075  30  GLN B C   
169  O O   . GLN A 357 ? 2.4141 2.0194 2.1737 -0.0270 -0.1213 0.0082  30  GLN B O   
170  C CB  . GLN A 357 ? 2.2515 1.8579 2.0090 -0.0385 -0.1173 0.0211  30  GLN B CB  
171  C CG  . GLN A 357 ? 2.3300 1.9436 2.0845 -0.0396 -0.1103 0.0184  30  GLN B CG  
172  C CD  . GLN A 357 ? 2.4458 2.0634 2.2069 -0.0420 -0.1073 0.0252  30  GLN B CD  
173  O OE1 . GLN A 357 ? 2.4932 2.1184 2.2638 -0.0430 -0.1082 0.0308  30  GLN B OE1 
174  N NE2 . GLN A 357 ? 2.3037 1.9310 2.0665 -0.0413 -0.1011 0.0231  30  GLN B NE2 
175  N N   . GLY A 358 ? 1.9317 1.5459 1.6793 -0.0309 -0.1122 0.0016  31  GLY B N   
176  C CA  . GLY A 358 ? 1.9100 1.5322 1.6600 -0.0264 -0.1086 -0.0041 31  GLY B CA  
177  C C   . GLY A 358 ? 2.0206 1.6523 1.7653 -0.0278 -0.1014 -0.0087 31  GLY B C   
178  O O   . GLY A 358 ? 2.2552 1.8869 1.9931 -0.0320 -0.0996 -0.0086 31  GLY B O   
179  N N   . SER A 359 ? 2.0442 1.6842 1.7925 -0.0244 -0.0974 -0.0123 32  SER B N   
180  C CA  . SER A 359 ? 1.9046 1.5536 1.6479 -0.0240 -0.0914 -0.0189 32  SER B CA  
181  C C   . SER A 359 ? 1.8293 1.4877 1.5788 -0.0221 -0.0866 -0.0185 32  SER B C   
182  O O   . SER A 359 ? 1.9347 1.5944 1.6900 -0.0177 -0.0880 -0.0203 32  SER B O   
183  C CB  . SER A 359 ? 2.1075 1.7552 1.8465 -0.0204 -0.0930 -0.0277 32  SER B CB  
184  O OG  . SER A 359 ? 2.3832 2.0298 2.1297 -0.0151 -0.0960 -0.0294 32  SER B OG  
185  N N   . GLY A 360 ? 1.9475 1.6126 1.6959 -0.0254 -0.0813 -0.0164 33  GLY B N   
186  C CA  . GLY A 360 ? 1.8885 1.5623 1.6422 -0.0242 -0.0768 -0.0157 33  GLY B CA  
187  C C   . GLY A 360 ? 1.7487 1.4316 1.4980 -0.0261 -0.0704 -0.0191 33  GLY B C   
188  O O   . GLY A 360 ? 1.8646 1.5474 1.6066 -0.0289 -0.0693 -0.0213 33  GLY B O   
189  N N   . TYR A 361 ? 1.3747 1.0658 1.1286 -0.0247 -0.0664 -0.0193 34  TYR B N   
190  C CA  . TYR A 361 ? 1.7505 1.4513 1.5017 -0.0259 -0.0603 -0.0224 34  TYR B CA  
191  C C   . TYR A 361 ? 2.0143 1.7186 1.7690 -0.0293 -0.0573 -0.0168 34  TYR B C   
192  O O   . TYR A 361 ? 2.0576 1.7659 1.8183 -0.0277 -0.0559 -0.0151 34  TYR B O   
193  C CB  . TYR A 361 ? 1.9564 1.6642 1.7105 -0.0213 -0.0581 -0.0277 34  TYR B CB  
194  C CG  . TYR A 361 ? 1.9004 1.6076 1.6510 -0.0178 -0.0594 -0.0350 34  TYR B CG  
195  C CD1 . TYR A 361 ? 1.8956 1.6082 1.6395 -0.0186 -0.0558 -0.0406 34  TYR B CD1 
196  C CD2 . TYR A 361 ? 1.7816 1.4836 1.5365 -0.0135 -0.0641 -0.0366 34  TYR B CD2 
197  C CE1 . TYR A 361 ? 1.7706 1.4835 1.5118 -0.0152 -0.0565 -0.0479 34  TYR B CE1 
198  C CE2 . TYR A 361 ? 1.6280 1.3294 1.3806 -0.0099 -0.0653 -0.0439 34  TYR B CE2 
199  C CZ  . TYR A 361 ? 1.7252 1.4322 1.4708 -0.0107 -0.0613 -0.0498 34  TYR B CZ  
200  O OH  . TYR A 361 ? 1.9508 1.6579 1.6944 -0.0070 -0.0621 -0.0577 34  TYR B OH  
201  N N   . ALA A 362 ? 1.9127 1.6160 1.6636 -0.0341 -0.0563 -0.0143 35  ALA B N   
202  C CA  . ALA A 362 ? 2.1524 1.8582 1.9070 -0.0375 -0.0539 -0.0092 35  ALA B CA  
203  C C   . ALA A 362 ? 2.1040 1.8183 1.8556 -0.0398 -0.0489 -0.0116 35  ALA B C   
204  O O   . ALA A 362 ? 2.0598 1.7743 1.8051 -0.0427 -0.0485 -0.0132 35  ALA B O   
205  C CB  . ALA A 362 ? 2.2894 1.9873 2.0439 -0.0415 -0.0572 -0.0035 35  ALA B CB  
206  N N   . ALA A 363 ? 1.5419 1.2635 1.2980 -0.0389 -0.0452 -0.0117 36  ALA B N   
207  C CA  . ALA A 363 ? 1.5873 1.3170 1.3415 -0.0413 -0.0407 -0.0133 36  ALA B CA  
208  C C   . ALA A 363 ? 1.5934 1.3215 1.3481 -0.0467 -0.0404 -0.0086 36  ALA B C   
209  O O   . ALA A 363 ? 1.8871 1.6097 1.6461 -0.0480 -0.0426 -0.0037 36  ALA B O   
210  C CB  . ALA A 363 ? 1.7491 1.4866 1.5083 -0.0389 -0.0372 -0.0146 36  ALA B CB  
211  N N   . ASP A 364 ? 1.5439 1.2771 1.2946 -0.0499 -0.0379 -0.0098 37  ASP B N   
212  C CA  . ASP A 364 ? 1.7549 1.4875 1.5068 -0.0553 -0.0378 -0.0053 37  ASP B CA  
213  C C   . ASP A 364 ? 1.8394 1.5776 1.5979 -0.0555 -0.0345 -0.0040 37  ASP B C   
214  O O   . ASP A 364 ? 1.8549 1.6011 1.6130 -0.0545 -0.0311 -0.0072 37  ASP B O   
215  C CB  . ASP A 364 ? 1.6275 1.3633 1.3726 -0.0592 -0.0370 -0.0067 37  ASP B CB  
216  C CG  . ASP A 364 ? 1.5038 1.2381 1.2508 -0.0651 -0.0378 -0.0014 37  ASP B CG  
217  O OD1 . ASP A 364 ? 1.6929 1.4204 1.4446 -0.0662 -0.0404 0.0032  37  ASP B OD1 
218  O OD2 . ASP A 364 ? 1.4709 1.2109 1.2152 -0.0687 -0.0360 -0.0016 37  ASP B OD2 
219  N N   . LEU A 365 ? 1.8848 1.6191 1.6496 -0.0569 -0.0357 0.0006  38  LEU B N   
220  C CA  . LEU A 365 ? 1.6836 1.4226 1.4551 -0.0563 -0.0329 0.0013  38  LEU B CA  
221  C C   . LEU A 365 ? 1.6963 1.4416 1.4683 -0.0598 -0.0301 0.0012  38  LEU B C   
222  O O   . LEU A 365 ? 1.6933 1.4458 1.4667 -0.0585 -0.0268 -0.0014 38  LEU B O   
223  C CB  . LEU A 365 ? 1.7884 1.5219 1.5665 -0.0570 -0.0347 0.0059  38  LEU B CB  
224  C CG  . LEU A 365 ? 2.0969 1.8257 1.8750 -0.0531 -0.0373 0.0060  38  LEU B CG  
225  C CD1 . LEU A 365 ? 2.1727 1.8959 1.9569 -0.0537 -0.0395 0.0108  38  LEU B CD1 
226  C CD2 . LEU A 365 ? 2.0251 1.7601 1.8036 -0.0489 -0.0350 0.0021  38  LEU B CD2 
227  N N   . LYS A 366 ? 1.8440 1.5866 1.6152 -0.0646 -0.0316 0.0042  39  LYS B N   
228  C CA  . LYS A 366 ? 1.7060 1.4539 1.4790 -0.0684 -0.0297 0.0050  39  LYS B CA  
229  C C   . LYS A 366 ? 1.6915 1.4474 1.4588 -0.0681 -0.0271 0.0009  39  LYS B C   
230  O O   . LYS A 366 ? 1.9283 1.6911 1.6982 -0.0684 -0.0242 -0.0003 39  LYS B O   
231  C CB  . LYS A 366 ? 1.6947 1.4376 1.4679 -0.0738 -0.0327 0.0095  39  LYS B CB  
232  C CG  . LYS A 366 ? 1.7814 1.5173 1.5618 -0.0746 -0.0350 0.0139  39  LYS B CG  
233  C CD  . LYS A 366 ? 1.6756 1.4065 1.4568 -0.0801 -0.0383 0.0186  39  LYS B CD  
234  C CE  . LYS A 366 ? 1.5245 1.2489 1.3140 -0.0807 -0.0404 0.0228  39  LYS B CE  
235  N NZ  . LYS A 366 ? 2.1447 1.8639 1.9357 -0.0862 -0.0440 0.0278  39  LYS B NZ  
236  N N   . SER A 367 ? 1.3900 1.1453 1.1497 -0.0674 -0.0280 -0.0015 40  SER B N   
237  C CA  . SER A 367 ? 1.3010 1.0645 1.0553 -0.0669 -0.0253 -0.0056 40  SER B CA  
238  C C   . SER A 367 ? 1.4835 1.2530 1.2406 -0.0623 -0.0221 -0.0092 40  SER B C   
239  O O   . SER A 367 ? 1.7229 1.5001 1.4811 -0.0632 -0.0192 -0.0103 40  SER B O   
240  C CB  . SER A 367 ? 1.2387 1.0002 0.9849 -0.0660 -0.0267 -0.0084 40  SER B CB  
241  O OG  . SER A 367 ? 1.4602 1.2180 1.2065 -0.0606 -0.0276 -0.0112 40  SER B OG  
242  N N   . THR A 368 ? 1.4455 1.2116 1.2041 -0.0576 -0.0229 -0.0108 41  THR B N   
243  C CA  . THR A 368 ? 1.3693 1.1409 1.1307 -0.0534 -0.0204 -0.0139 41  THR B CA  
244  C C   . THR A 368 ? 1.5155 1.2909 1.2831 -0.0546 -0.0183 -0.0120 41  THR B C   
245  O O   . THR A 368 ? 1.7816 1.5647 1.5499 -0.0539 -0.0154 -0.0143 41  THR B O   
246  C CB  . THR A 368 ? 1.3290 1.0955 1.0919 -0.0488 -0.0224 -0.0146 41  THR B CB  
247  O OG1 . THR A 368 ? 1.6671 1.4269 1.4345 -0.0499 -0.0247 -0.0102 41  THR B OG1 
248  C CG2 . THR A 368 ? 1.4353 1.1983 1.1922 -0.0471 -0.0245 -0.0173 41  THR B CG2 
249  N N   . GLN A 369 ? 1.4287 1.1990 1.2011 -0.0566 -0.0198 -0.0080 42  GLN B N   
250  C CA  . GLN A 369 ? 1.5977 1.3713 1.3766 -0.0574 -0.0179 -0.0069 42  GLN B CA  
251  C C   . GLN A 369 ? 1.5731 1.3526 1.3521 -0.0611 -0.0160 -0.0068 42  GLN B C   
252  O O   . GLN A 369 ? 1.7916 1.5776 1.5729 -0.0604 -0.0134 -0.0086 42  GLN B O   
253  C CB  . GLN A 369 ? 1.5528 1.3197 1.3371 -0.0588 -0.0199 -0.0029 42  GLN B CB  
254  C CG  . GLN A 369 ? 1.7881 1.5579 1.5792 -0.0606 -0.0182 -0.0018 42  GLN B CG  
255  C CD  . GLN A 369 ? 2.0702 1.8454 1.8638 -0.0573 -0.0156 -0.0043 42  GLN B CD  
256  O OE1 . GLN A 369 ? 2.2825 2.0578 2.0742 -0.0536 -0.0158 -0.0058 42  GLN B OE1 
257  N NE2 . GLN A 369 ? 2.6048 2.3845 2.4027 -0.0588 -0.0135 -0.0047 42  GLN B NE2 
258  N N   . ASN A 370 ? 1.6366 1.4141 1.4134 -0.0654 -0.0176 -0.0046 43  ASN B N   
259  C CA  . ASN A 370 ? 1.6533 1.4364 1.4304 -0.0694 -0.0165 -0.0038 43  ASN B CA  
260  C C   . ASN A 370 ? 1.5863 1.3781 1.3590 -0.0679 -0.0137 -0.0076 43  ASN B C   
261  O O   . ASN A 370 ? 1.6720 1.4703 1.4472 -0.0690 -0.0116 -0.0082 43  ASN B O   
262  C CB  . ASN A 370 ? 1.6823 1.4617 1.4572 -0.0744 -0.0192 -0.0004 43  ASN B CB  
263  C CG  . ASN A 370 ? 1.8849 1.6555 1.6646 -0.0759 -0.0221 0.0037  43  ASN B CG  
264  O OD1 . ASN A 370 ? 1.8830 1.6521 1.6697 -0.0749 -0.0217 0.0045  43  ASN B OD1 
265  N ND2 . ASN A 370 ? 1.9017 1.6668 1.6777 -0.0784 -0.0251 0.0060  43  ASN B ND2 
266  N N   . ALA A 371 ? 1.5182 1.3100 1.2846 -0.0654 -0.0137 -0.0105 44  ALA B N   
267  C CA  . ALA A 371 ? 1.5183 1.3185 1.2809 -0.0635 -0.0110 -0.0144 44  ALA B CA  
268  C C   . ALA A 371 ? 1.6689 1.4736 1.4358 -0.0598 -0.0086 -0.0167 44  ALA B C   
269  O O   . ALA A 371 ? 1.6980 1.5107 1.4652 -0.0600 -0.0061 -0.0182 44  ALA B O   
270  C CB  . ALA A 371 ? 1.3431 1.1418 1.0991 -0.0610 -0.0116 -0.0176 44  ALA B CB  
271  N N   . ILE A 372 ? 1.4331 1.2330 1.2033 -0.0564 -0.0095 -0.0166 45  ILE B N   
272  C CA  . ILE A 372 ? 1.2196 1.0236 0.9938 -0.0533 -0.0076 -0.0183 45  ILE B CA  
273  C C   . ILE A 372 ? 1.4883 1.2962 1.2672 -0.0561 -0.0062 -0.0168 45  ILE B C   
274  O O   . ILE A 372 ? 1.6585 1.4733 1.4388 -0.0551 -0.0039 -0.0186 45  ILE B O   
275  C CB  . ILE A 372 ? 1.0936 0.8918 0.8705 -0.0499 -0.0093 -0.0178 45  ILE B CB  
276  C CG1 . ILE A 372 ? 1.3393 1.1350 1.1124 -0.0462 -0.0107 -0.0202 45  ILE B CG1 
277  C CG2 . ILE A 372 ? 1.3143 1.1164 1.0959 -0.0480 -0.0077 -0.0184 45  ILE B CG2 
278  C CD1 . ILE A 372 ? 1.5334 1.3210 1.3081 -0.0445 -0.0137 -0.0183 45  ILE B CD1 
279  N N   . ASP A 373 ? 1.5595 1.3629 1.3414 -0.0596 -0.0076 -0.0134 46  ASP B N   
280  C CA  . ASP A 373 ? 1.6221 1.4287 1.4091 -0.0625 -0.0066 -0.0122 46  ASP B CA  
281  C C   . ASP A 373 ? 1.4922 1.3066 1.2771 -0.0648 -0.0051 -0.0130 46  ASP B C   
282  O O   . ASP A 373 ? 1.5671 1.3875 1.3545 -0.0645 -0.0031 -0.0143 46  ASP B O   
283  C CB  . ASP A 373 ? 1.7411 1.5415 1.5320 -0.0662 -0.0089 -0.0084 46  ASP B CB  
284  C CG  . ASP A 373 ? 2.1172 1.9104 1.9106 -0.0642 -0.0104 -0.0072 46  ASP B CG  
285  O OD1 . ASP A 373 ? 2.4383 2.2319 2.2314 -0.0602 -0.0096 -0.0091 46  ASP B OD1 
286  O OD2 . ASP A 373 ? 2.0475 1.8348 1.8433 -0.0668 -0.0126 -0.0041 46  ASP B OD2 
287  N N   . GLY A 374 ? 1.4473 1.2619 1.2273 -0.0672 -0.0059 -0.0122 47  GLY B N   
288  C CA  . GLY A 374 ? 1.5978 1.4205 1.3756 -0.0698 -0.0045 -0.0126 47  GLY B CA  
289  C C   . GLY A 374 ? 1.3637 1.1939 1.1395 -0.0661 -0.0017 -0.0165 47  GLY B C   
290  O O   . GLY A 374 ? 1.2541 1.0915 1.0318 -0.0673 0.0000  -0.0168 47  GLY B O   
291  N N   . ILE A 375 ? 1.3311 1.1598 1.1038 -0.0617 -0.0014 -0.0193 48  ILE B N   
292  C CA  . ILE A 375 ? 1.3063 1.1419 1.0777 -0.0580 0.0011  -0.0231 48  ILE B CA  
293  C C   . ILE A 375 ? 1.3925 1.2309 1.1694 -0.0563 0.0023  -0.0235 48  ILE B C   
294  O O   . ILE A 375 ? 1.3586 1.2048 1.1362 -0.0559 0.0044  -0.0250 48  ILE B O   
295  C CB  . ILE A 375 ? 1.2136 1.0460 0.9816 -0.0535 0.0005  -0.0261 48  ILE B CB  
296  C CG1 . ILE A 375 ? 1.1955 1.0256 0.9574 -0.0554 -0.0007 -0.0262 48  ILE B CG1 
297  C CG2 . ILE A 375 ? 1.2021 1.0413 0.9703 -0.0494 0.0027  -0.0300 48  ILE B CG2 
298  C CD1 . ILE A 375 ? 1.2965 1.1354 1.0540 -0.0558 0.0016  -0.0290 48  ILE B CD1 
299  N N   . THR A 376 ? 1.3960 1.2285 1.1766 -0.0554 0.0010  -0.0222 49  THR B N   
300  C CA  . THR A 376 ? 1.3175 1.1527 1.1028 -0.0541 0.0022  -0.0226 49  THR B CA  
301  C C   . THR A 376 ? 1.2669 1.1068 1.0552 -0.0579 0.0031  -0.0214 49  THR B C   
302  O O   . THR A 376 ? 1.0905 0.9364 0.8808 -0.0571 0.0047  -0.0227 49  THR B O   
303  C CB  . THR A 376 ? 1.3317 1.1599 1.1202 -0.0531 0.0007  -0.0213 49  THR B CB  
304  O OG1 . THR A 376 ? 1.2779 1.0999 1.0670 -0.0562 -0.0012 -0.0185 49  THR B OG1 
305  C CG2 . THR A 376 ? 1.4330 1.2582 1.2198 -0.0488 -0.0002 -0.0226 49  THR B CG2 
306  N N   . ASN A 377 ? 1.4680 1.3051 1.2571 -0.0621 0.0017  -0.0187 50  ASN B N   
307  C CA  . ASN A 377 ? 1.3559 1.1973 1.1485 -0.0658 0.0021  -0.0173 50  ASN B CA  
308  C C   . ASN A 377 ? 1.2896 1.1398 1.0794 -0.0666 0.0037  -0.0183 50  ASN B C   
309  O O   . ASN A 377 ? 1.2846 1.1405 1.0772 -0.0675 0.0048  -0.0186 50  ASN B O   
310  C CB  . ASN A 377 ? 1.1396 0.9761 0.9342 -0.0704 -0.0003 -0.0139 50  ASN B CB  
311  C CG  . ASN A 377 ? 1.5403 1.3814 1.3386 -0.0746 -0.0005 -0.0122 50  ASN B CG  
312  O OD1 . ASN A 377 ? 1.6046 1.4477 1.4077 -0.0746 0.0001  -0.0130 50  ASN B OD1 
313  N ND2 . ASN A 377 ? 2.0463 1.8893 1.8425 -0.0786 -0.0016 -0.0098 50  ASN B ND2 
314  N N   . LYS A 378 ? 1.2280 1.0796 1.0122 -0.0663 0.0040  -0.0190 51  LYS B N   
315  C CA  . LYS A 378 ? 1.0920 0.9528 0.8734 -0.0664 0.0060  -0.0204 51  LYS B CA  
316  C C   . LYS A 378 ? 1.2352 1.1011 1.0185 -0.0623 0.0081  -0.0233 51  LYS B C   
317  O O   . LYS A 378 ? 1.2164 1.0898 1.0013 -0.0634 0.0095  -0.0234 51  LYS B O   
318  C CB  . LYS A 378 ? 1.3409 1.2024 1.1159 -0.0657 0.0063  -0.0218 51  LYS B CB  
319  C CG  . LYS A 378 ? 1.6943 1.5529 1.4664 -0.0704 0.0043  -0.0188 51  LYS B CG  
320  C CD  . LYS A 378 ? 1.4726 1.3324 1.2378 -0.0691 0.0049  -0.0212 51  LYS B CD  
321  C CE  . LYS A 378 ? 1.1372 0.9948 0.8986 -0.0742 0.0029  -0.0181 51  LYS B CE  
322  N NZ  . LYS A 378 ? 1.0223 0.8813 0.7764 -0.0729 0.0036  -0.0210 51  LYS B NZ  
323  N N   . VAL A 379 ? 1.4625 1.3243 1.2457 -0.0579 0.0080  -0.0253 52  VAL B N   
324  C CA  . VAL A 379 ? 1.4218 1.2881 1.2068 -0.0541 0.0095  -0.0278 52  VAL B CA  
325  C C   . VAL A 379 ? 1.2200 1.0890 1.0099 -0.0558 0.0099  -0.0267 52  VAL B C   
326  O O   . VAL A 379 ? 1.1325 1.0089 0.9235 -0.0557 0.0114  -0.0274 52  VAL B O   
327  C CB  . VAL A 379 ? 1.3860 1.2466 1.1710 -0.0498 0.0086  -0.0293 52  VAL B CB  
328  C CG1 . VAL A 379 ? 1.5567 1.4219 1.3445 -0.0464 0.0096  -0.0311 52  VAL B CG1 
329  C CG2 . VAL A 379 ? 1.2399 1.0986 1.0204 -0.0478 0.0082  -0.0310 52  VAL B CG2 
330  N N   . ASN A 380 ? 1.1197 0.9827 0.9125 -0.0572 0.0085  -0.0250 53  ASN B N   
331  C CA  . ASN A 380 ? 1.3440 1.2092 1.1413 -0.0585 0.0087  -0.0247 53  ASN B CA  
332  C C   . ASN A 380 ? 1.4387 1.3093 1.2375 -0.0625 0.0090  -0.0233 53  ASN B C   
333  O O   . ASN A 380 ? 1.7047 1.5808 1.5059 -0.0628 0.0099  -0.0238 53  ASN B O   
334  C CB  . ASN A 380 ? 1.4692 1.3271 1.2695 -0.0593 0.0073  -0.0236 53  ASN B CB  
335  C CG  . ASN A 380 ? 1.6158 1.4688 1.4150 -0.0556 0.0068  -0.0244 53  ASN B CG  
336  O OD1 . ASN A 380 ? 1.3808 1.2362 1.1802 -0.0527 0.0076  -0.0259 53  ASN B OD1 
337  N ND2 . ASN A 380 ? 1.7733 1.6193 1.5715 -0.0560 0.0053  -0.0231 53  ASN B ND2 
338  N N   . SER A 381 ? 1.1773 1.0468 0.9748 -0.0659 0.0080  -0.0212 54  SER B N   
339  C CA  . SER A 381 ? 1.2722 1.1472 1.0713 -0.0701 0.0078  -0.0193 54  SER B CA  
340  C C   . SER A 381 ? 1.3277 1.2121 1.1247 -0.0691 0.0099  -0.0205 54  SER B C   
341  O O   . SER A 381 ? 1.3673 1.2576 1.1671 -0.0710 0.0102  -0.0198 54  SER B O   
342  C CB  . SER A 381 ? 1.3271 1.1992 1.1249 -0.0741 0.0060  -0.0164 54  SER B CB  
343  O OG  . SER A 381 ? 1.5765 1.4516 1.3684 -0.0735 0.0069  -0.0170 54  SER B OG  
344  N N   . VAL A 382 ? 1.2973 1.1832 1.0898 -0.0660 0.0112  -0.0225 55  VAL B N   
345  C CA  . VAL A 382 ? 1.3457 1.2408 1.1367 -0.0644 0.0134  -0.0242 55  VAL B CA  
346  C C   . VAL A 382 ? 1.3246 1.2229 1.1192 -0.0618 0.0144  -0.0257 55  VAL B C   
347  O O   . VAL A 382 ? 1.2789 1.1845 1.0755 -0.0631 0.0153  -0.0252 55  VAL B O   
348  C CB  . VAL A 382 ? 1.1885 1.0838 0.9746 -0.0611 0.0145  -0.0268 55  VAL B CB  
349  C CG1 . VAL A 382 ? 1.3108 1.2152 1.0968 -0.0583 0.0170  -0.0293 55  VAL B CG1 
350  C CG2 . VAL A 382 ? 1.2984 1.1933 1.0803 -0.0645 0.0139  -0.0252 55  VAL B CG2 
351  N N   . ILE A 383 ? 1.3399 1.2328 1.1354 -0.0584 0.0139  -0.0272 56  ILE B N   
352  C CA  . ILE A 383 ? 1.1877 1.0830 0.9863 -0.0562 0.0144  -0.0283 56  ILE B CA  
353  C C   . ILE A 383 ? 1.3862 1.2848 1.1884 -0.0598 0.0141  -0.0267 56  ILE B C   
354  O O   . ILE A 383 ? 1.5927 1.4976 1.3968 -0.0593 0.0150  -0.0272 56  ILE B O   
355  C CB  . ILE A 383 ? 1.1388 1.0269 0.9381 -0.0536 0.0134  -0.0290 56  ILE B CB  
356  C CG1 . ILE A 383 ? 1.1172 1.0022 0.9135 -0.0500 0.0133  -0.0306 56  ILE B CG1 
357  C CG2 . ILE A 383 ? 0.9881 0.8792 0.7904 -0.0522 0.0137  -0.0298 56  ILE B CG2 
358  C CD1 . ILE A 383 ? 1.5971 1.4748 1.3940 -0.0479 0.0118  -0.0306 56  ILE B CD1 
359  N N   . GLU A 384 ? 1.4566 1.3509 1.2602 -0.0634 0.0126  -0.0247 57  GLU B N   
360  C CA  . GLU A 384 ? 1.4510 1.3479 1.2585 -0.0672 0.0118  -0.0231 57  GLU B CA  
361  C C   . GLU A 384 ? 1.4527 1.3582 1.2598 -0.0694 0.0125  -0.0218 57  GLU B C   
362  O O   . GLU A 384 ? 1.1295 1.0354 0.9356 -0.0727 0.0117  -0.0196 57  GLU B O   
363  C CB  . GLU A 384 ? 1.1736 1.0636 0.9834 -0.0704 0.0097  -0.0214 57  GLU B CB  
364  C CG  . GLU A 384 ? 1.5838 1.4666 1.3951 -0.0686 0.0091  -0.0228 57  GLU B CG  
365  C CD  . GLU A 384 ? 2.1918 2.0667 2.0031 -0.0697 0.0077  -0.0215 57  GLU B CD  
366  O OE1 . GLU A 384 ? 2.2982 2.1725 2.1103 -0.0733 0.0063  -0.0192 57  GLU B OE1 
367  O OE2 . GLU A 384 ? 2.3346 2.2041 2.1454 -0.0672 0.0076  -0.0226 57  GLU B OE2 
368  N N   . LYS A 385 ? 1.4688 1.3814 1.2766 -0.0678 0.0139  -0.0228 58  LYS B N   
369  C CA  . LYS A 385 ? 1.3215 1.2434 1.1295 -0.0697 0.0148  -0.0215 58  LYS B CA  
370  C C   . LYS A 385 ? 1.5110 1.4371 1.3232 -0.0707 0.0145  -0.0211 58  LYS B C   
371  O O   . LYS A 385 ? 1.2232 1.1534 1.0359 -0.0678 0.0157  -0.0227 58  LYS B O   
372  C CB  . LYS A 385 ? 1.5379 1.4654 1.3427 -0.0663 0.0172  -0.0234 58  LYS B CB  
373  C CG  . LYS A 385 ? 1.5015 1.4261 1.3017 -0.0656 0.0177  -0.0240 58  LYS B CG  
374  C CD  . LYS A 385 ? 1.2614 1.1918 1.0592 -0.0617 0.0201  -0.0268 58  LYS B CD  
375  C CE  . LYS A 385 ? 1.3106 1.2379 1.1034 -0.0612 0.0204  -0.0278 58  LYS B CE  
376  N NZ  . LYS A 385 ? 2.0100 1.9424 1.8005 -0.0572 0.0227  -0.0312 58  LYS B NZ  
377  N N   . MET A 386 ? 1.8310 1.7559 1.6466 -0.0748 0.0124  -0.0190 59  MET B N   
378  C CA  . MET A 386 ? 1.9488 1.8774 1.7684 -0.0762 0.0117  -0.0186 59  MET B CA  
379  C C   . MET A 386 ? 2.0061 1.9446 1.8265 -0.0782 0.0123  -0.0164 59  MET B C   
380  O O   . MET A 386 ? 1.7885 1.7292 1.6093 -0.0820 0.0113  -0.0136 59  MET B O   
381  C CB  . MET A 386 ? 1.3851 1.3081 1.2088 -0.0795 0.0090  -0.0177 59  MET B CB  
382  C CG  . MET A 386 ? 1.4679 1.3821 1.2914 -0.0774 0.0087  -0.0201 59  MET B CG  
383  S SD  . MET A 386 ? 2.0382 1.9534 1.8607 -0.0731 0.0103  -0.0232 59  MET B SD  
384  C CE  . MET A 386 ? 1.9901 1.9096 1.8171 -0.0760 0.0089  -0.0229 59  MET B CE  
385  N N   . ASN A 387 ? 1.7482 1.6931 1.5691 -0.0759 0.0138  -0.0174 60  ASN B N   
386  C CA  . ASN A 387 ? 2.0522 2.0074 1.8741 -0.0774 0.0147  -0.0155 60  ASN B CA  
387  C C   . ASN A 387 ? 2.4532 2.4107 2.2799 -0.0809 0.0125  -0.0134 60  ASN B C   
388  O O   . ASN A 387 ? 2.4908 2.4504 2.3195 -0.0796 0.0125  -0.0144 60  ASN B O   
389  C CB  . ASN A 387 ? 2.0801 2.0411 1.9011 -0.0730 0.0173  -0.0177 60  ASN B CB  
390  C CG  . ASN A 387 ? 1.9790 1.9393 1.7957 -0.0698 0.0194  -0.0197 60  ASN B CG  
391  O OD1 . ASN A 387 ? 2.1278 2.0862 1.9417 -0.0716 0.0193  -0.0188 60  ASN B OD1 
392  N ND2 . ASN A 387 ? 1.9471 1.9087 1.7634 -0.0651 0.0211  -0.0224 60  ASN B ND2 
393  N N   . THR A 388 ? 2.7229 2.6800 2.5517 -0.0857 0.0102  -0.0104 61  THR B N   
394  C CA  . THR A 388 ? 2.9246 2.8824 2.7585 -0.0894 0.0074  -0.0084 61  THR B CA  
395  C C   . THR A 388 ? 2.8493 2.8011 2.6849 -0.0876 0.0065  -0.0113 61  THR B C   
396  O O   . THR A 388 ? 2.7206 2.6647 2.5544 -0.0854 0.0068  -0.0139 61  THR B O   
397  C CB  . THR A 388 ? 2.7882 2.7568 2.6242 -0.0910 0.0077  -0.0059 61  THR B CB  
398  O OG1 . THR A 388 ? 2.7250 2.6976 2.5601 -0.0869 0.0101  -0.0082 61  THR B OG1 
399  C CG2 . THR A 388 ? 2.3726 2.3483 2.2066 -0.0931 0.0089  -0.0031 61  THR B CG2 
400  N N   . GLN A 389 ? 2.9408 2.8963 2.7796 -0.0887 0.0054  -0.0109 62  GLN B N   
401  C CA  . GLN A 389 ? 2.9583 2.9091 2.7984 -0.0876 0.0045  -0.0136 62  GLN B CA  
402  C C   . GLN A 389 ? 3.0275 2.9854 2.8690 -0.0871 0.0047  -0.0133 62  GLN B C   
403  O O   . GLN A 389 ? 2.7580 2.7242 2.6002 -0.0877 0.0055  -0.0108 62  GLN B O   
404  C CB  . GLN A 389 ? 2.9429 2.8878 2.7873 -0.0912 0.0012  -0.0135 62  GLN B CB  
405  C CG  . GLN A 389 ? 2.8460 2.7829 2.6899 -0.0915 0.0006  -0.0141 62  GLN B CG  
406  C CD  . GLN A 389 ? 2.5103 2.4418 2.3597 -0.0951 -0.0028 -0.0140 62  GLN B CD  
407  O OE1 . GLN A 389 ? 2.2925 2.2270 2.1464 -0.0983 -0.0053 -0.0123 62  GLN B OE1 
408  N NE2 . GLN A 389 ? 2.3187 2.2421 2.1684 -0.0945 -0.0032 -0.0159 62  GLN B NE2 
409  N N   . PHE A 390 ? 2.8883 2.8431 2.7302 -0.0860 0.0041  -0.0158 63  PHE B N   
410  C CA  . PHE A 390 ? 2.7808 2.7412 2.6245 -0.0863 0.0035  -0.0153 63  PHE B CA  
411  C C   . PHE A 390 ? 3.0234 2.9847 2.8718 -0.0909 0.0002  -0.0134 63  PHE B C   
412  O O   . PHE A 390 ? 3.5028 3.4582 3.3532 -0.0932 -0.0019 -0.0138 63  PHE B O   
413  C CB  . PHE A 390 ? 2.8232 2.7799 2.6652 -0.0840 0.0038  -0.0186 63  PHE B CB  
414  C CG  . PHE A 390 ? 2.8758 2.8315 2.7140 -0.0796 0.0064  -0.0203 63  PHE B CG  
415  C CD1 . PHE A 390 ? 2.8576 2.8197 2.6953 -0.0770 0.0079  -0.0195 63  PHE B CD1 
416  C CD2 . PHE A 390 ? 2.9256 2.8739 2.7613 -0.0780 0.0070  -0.0225 63  PHE B CD2 
417  C CE1 . PHE A 390 ? 2.8177 2.7784 2.6527 -0.0729 0.0098  -0.0211 63  PHE B CE1 
418  C CE2 . PHE A 390 ? 2.7686 2.7157 2.6011 -0.0740 0.0089  -0.0238 63  PHE B CE2 
419  C CZ  . PHE A 390 ? 2.7159 2.6690 2.5482 -0.0715 0.0102  -0.0231 63  PHE B CZ  
420  N N   . THR A 391 ? 3.0519 3.0204 2.9026 -0.0921 -0.0005 -0.0113 64  THR B N   
421  C CA  . THR A 391 ? 2.8738 2.8428 2.7291 -0.0961 -0.0041 -0.0100 64  THR B CA  
422  C C   . THR A 391 ? 2.7626 2.7349 2.6186 -0.0959 -0.0048 -0.0106 64  THR B C   
423  O O   . THR A 391 ? 2.2917 2.2636 2.1513 -0.0991 -0.0080 -0.0101 64  THR B O   
424  C CB  . THR A 391 ? 2.4707 2.4457 2.3296 -0.0998 -0.0056 -0.0053 64  THR B CB  
425  O OG1 . THR A 391 ? 2.4223 2.4066 2.2801 -0.0983 -0.0031 -0.0030 64  THR B OG1 
426  C CG2 . THR A 391 ? 2.0386 2.0099 1.8974 -0.1013 -0.0059 -0.0042 64  THR B CG2 
427  N N   . ALA A 392 ? 2.7369 2.7128 2.5902 -0.0924 -0.0023 -0.0113 65  ALA B N   
428  C CA  . ALA A 392 ? 2.3744 2.3523 2.2276 -0.0918 -0.0030 -0.0122 65  ALA B CA  
429  C C   . ALA A 392 ? 2.6016 2.5886 2.4584 -0.0934 -0.0039 -0.0084 65  ALA B C   
430  O O   . ALA A 392 ? 2.6093 2.5972 2.4687 -0.0962 -0.0067 -0.0077 65  ALA B O   
431  C CB  . ALA A 392 ? 2.0779 2.0497 1.9317 -0.0940 -0.0057 -0.0149 65  ALA B CB  
432  N N   . VAL A 393 ? 2.8076 2.8014 2.6646 -0.0918 -0.0015 -0.0061 66  VAL B N   
433  C CA  . VAL A 393 ? 2.6830 2.6849 2.5441 -0.0946 -0.0025 -0.0018 66  VAL B CA  
434  C C   . VAL A 393 ? 2.7083 2.7198 2.5704 -0.0921 0.0002  0.0000  66  VAL B C   
435  O O   . VAL A 393 ? 2.7039 2.7180 2.5642 -0.0895 0.0033  -0.0003 66  VAL B O   
436  C CB  . VAL A 393 ? 2.5069 2.5073 2.3685 -0.0971 -0.0029 -0.0003 66  VAL B CB  
437  C CG1 . VAL A 393 ? 2.3897 2.3986 2.2548 -0.0999 -0.0037 0.0042  66  VAL B CG1 
438  C CG2 . VAL A 393 ? 2.4261 2.4189 2.2894 -0.1004 -0.0066 -0.0012 66  VAL B CG2 
439  N N   . GLY A 394 ? 2.8625 2.8791 2.7275 -0.0928 -0.0011 0.0017  67  GLY B N   
440  C CA  . GLY A 394 ? 2.8776 2.9031 2.7446 -0.0903 0.0011  0.0032  67  GLY B CA  
441  C C   . GLY A 394 ? 3.0542 3.0870 2.9263 -0.0936 -0.0014 0.0073  67  GLY B C   
442  O O   . GLY A 394 ? 2.9839 3.0133 2.8572 -0.0970 -0.0050 0.0079  67  GLY B O   
443  N N   . LYS A 395 ? 2.9160 2.9592 2.7914 -0.0925 0.0006  0.0099  68  LYS B N   
444  C CA  . LYS A 395 ? 3.0239 3.0753 2.9045 -0.0957 -0.0014 0.0145  68  LYS B CA  
445  C C   . LYS A 395 ? 3.2492 3.3104 3.1335 -0.0928 0.0010  0.0159  68  LYS B C   
446  O O   . LYS A 395 ? 3.1725 3.2356 3.0557 -0.0885 0.0046  0.0136  68  LYS B O   
447  C CB  . LYS A 395 ? 2.5261 2.5820 2.4084 -0.0993 -0.0018 0.0179  68  LYS B CB  
448  C CG  . LYS A 395 ? 2.4567 2.5215 2.3448 -0.1031 -0.0042 0.0231  68  LYS B CG  
449  C CD  . LYS A 395 ? 2.5879 2.6476 2.4778 -0.1066 -0.0092 0.0240  68  LYS B CD  
450  C CE  . LYS A 395 ? 2.1598 2.2282 2.0557 -0.1108 -0.0120 0.0298  68  LYS B CE  
451  N NZ  . LYS A 395 ? 1.9480 2.0125 1.8463 -0.1141 -0.0171 0.0308  68  LYS B NZ  
452  N N   . GLU A 396 ? 3.1878 3.2553 3.0770 -0.0954 -0.0013 0.0197  69  GLU B N   
453  C CA  . GLU A 396 ? 3.2121 3.2901 3.1065 -0.0935 0.0002  0.0220  69  GLU B CA  
454  C C   . GLU A 396 ? 3.0519 3.1411 2.9514 -0.0965 0.0001  0.0271  69  GLU B C   
455  O O   . GLU A 396 ? 2.8981 2.9870 2.7979 -0.1009 -0.0023 0.0297  69  GLU B O   
456  C CB  . GLU A 396 ? 3.1261 3.2022 3.0224 -0.0937 -0.0027 0.0224  69  GLU B CB  
457  C CG  . GLU A 396 ? 2.9189 2.9867 2.8108 -0.0903 -0.0018 0.0179  69  GLU B CG  
458  C CD  . GLU A 396 ? 3.0197 3.0913 2.9119 -0.0853 0.0026  0.0159  69  GLU B CD  
459  O OE1 . GLU A 396 ? 3.0794 3.1606 2.9769 -0.0837 0.0043  0.0179  69  GLU B OE1 
460  O OE2 . GLU A 396 ? 3.1348 3.2007 3.0224 -0.0833 0.0046  0.0126  69  GLU B OE2 
461  N N   . PHE A 397 ? 3.4444 3.5439 3.3487 -0.0940 0.0027  0.0286  70  PHE B N   
462  C CA  . PHE A 397 ? 3.1675 3.2786 3.0778 -0.0970 0.0021  0.0340  70  PHE B CA  
463  C C   . PHE A 397 ? 3.3137 3.4228 3.2268 -0.1014 -0.0033 0.0375  70  PHE B C   
464  O O   . PHE A 397 ? 3.3779 3.4946 3.2954 -0.1052 -0.0051 0.0425  70  PHE B O   
465  C CB  . PHE A 397 ? 3.0826 3.2053 2.9985 -0.0933 0.0056  0.0347  70  PHE B CB  
466  C CG  . PHE A 397 ? 2.8060 2.9326 2.7202 -0.0889 0.0111  0.0312  70  PHE B CG  
467  C CD1 . PHE A 397 ? 2.4815 2.6164 2.3955 -0.0904 0.0137  0.0328  70  PHE B CD1 
468  C CD2 . PHE A 397 ? 2.6530 2.7764 2.5665 -0.0835 0.0135  0.0267  70  PHE B CD2 
469  C CE1 . PHE A 397 ? 2.2633 2.4022 2.1755 -0.0864 0.0188  0.0292  70  PHE B CE1 
470  C CE2 . PHE A 397 ? 2.2178 2.3448 2.1301 -0.0793 0.0183  0.0232  70  PHE B CE2 
471  C CZ  . PHE A 397 ? 2.1568 2.2916 2.0683 -0.0807 0.0210  0.0242  70  PHE B CZ  
472  N N   . ASN A 398 ? 3.1766 3.2760 3.0871 -0.1011 -0.0060 0.0350  71  ASN B N   
473  C CA  . ASN A 398 ? 3.2168 3.3128 3.1289 -0.1053 -0.0113 0.0373  71  ASN B CA  
474  C C   . ASN A 398 ? 3.3732 3.4796 3.2924 -0.1065 -0.0125 0.0423  71  ASN B C   
475  O O   . ASN A 398 ? 3.2057 3.3128 3.1278 -0.1109 -0.0169 0.0460  71  ASN B O   
476  C CB  . ASN A 398 ? 2.9726 3.0642 2.8834 -0.1102 -0.0147 0.0387  71  ASN B CB  
477  C CG  . ASN A 398 ? 2.7245 2.8081 2.6347 -0.1136 -0.0201 0.0384  71  ASN B CG  
478  O OD1 . ASN A 398 ? 2.6116 2.6899 2.5211 -0.1173 -0.0233 0.0386  71  ASN B OD1 
479  N ND2 . ASN A 398 ? 2.8111 2.8939 2.7218 -0.1127 -0.0214 0.0379  71  ASN B ND2 
480  N N   . HIS A 399 ? 3.5935 3.7082 3.5163 -0.1024 -0.0086 0.0424  72  HIS B N   
481  C CA  . HIS A 399 ? 3.3613 3.4870 3.2918 -0.1028 -0.0090 0.0470  72  HIS B CA  
482  C C   . HIS A 399 ? 3.4122 3.5471 3.3469 -0.1069 -0.0098 0.0524  72  HIS B C   
483  O O   . HIS A 399 ? 3.4817 3.6270 3.4232 -0.1078 -0.0100 0.0568  72  HIS B O   
484  C CB  . HIS A 399 ? 3.1055 3.2270 3.0374 -0.1045 -0.0135 0.0482  72  HIS B CB  
485  C CG  . HIS A 399 ? 2.7643 2.8964 2.7044 -0.1047 -0.0141 0.0529  72  HIS B CG  
486  N ND1 . HIS A 399 ? 2.9172 3.0597 2.8628 -0.1008 -0.0097 0.0534  72  HIS B ND1 
487  C CD2 . HIS A 399 ? 2.6373 2.7714 2.5816 -0.1085 -0.0187 0.0573  72  HIS B CD2 
488  C CE1 . HIS A 399 ? 2.7467 2.8973 2.6998 -0.1020 -0.0115 0.0581  72  HIS B CE1 
489  N NE2 . HIS A 399 ? 2.4728 2.6184 2.4251 -0.1067 -0.0170 0.0607  72  HIS B NE2 
490  N N   . LEU A 400 ? 3.5841 3.7154 3.5150 -0.1097 -0.0105 0.0522  73  LEU B N   
491  C CA  . LEU A 400 ? 3.0565 3.1966 2.9910 -0.1138 -0.0112 0.0575  73  LEU B CA  
492  C C   . LEU A 400 ? 3.0604 3.2077 2.9936 -0.1117 -0.0059 0.0566  73  LEU B C   
493  O O   . LEU A 400 ? 2.7465 2.8993 2.6807 -0.1154 -0.0064 0.0602  73  LEU B O   
494  C CB  . LEU A 400 ? 2.5516 2.6832 2.4839 -0.1190 -0.0166 0.0588  73  LEU B CB  
495  C CG  . LEU A 400 ? 2.4031 2.5289 2.3371 -0.1218 -0.0223 0.0600  73  LEU B CG  
496  C CD1 . LEU A 400 ? 2.2389 2.3554 2.1708 -0.1264 -0.0274 0.0600  73  LEU B CD1 
497  C CD2 . LEU A 400 ? 2.1570 2.2942 2.0988 -0.1239 -0.0239 0.0662  73  LEU B CD2 
498  N N   . GLU A 401 ? 2.6031 2.7509 2.5344 -0.1061 -0.0010 0.0519  74  GLU B N   
499  C CA  . GLU A 401 ? 2.3551 2.5078 2.2838 -0.1036 0.0042  0.0496  74  GLU B CA  
500  C C   . GLU A 401 ? 2.6213 2.7668 2.5442 -0.1068 0.0028  0.0491  74  GLU B C   
501  O O   . GLU A 401 ? 2.9588 3.1111 2.8809 -0.1084 0.0049  0.0508  74  GLU B O   
502  C CB  . GLU A 401 ? 2.1119 2.2813 2.0466 -0.1040 0.0073  0.0536  74  GLU B CB  
503  C CG  . GLU A 401 ? 2.2393 2.4160 2.1802 -0.0998 0.0097  0.0531  74  GLU B CG  
504  C CD  . GLU A 401 ? 2.1267 2.3207 2.0743 -0.1001 0.0128  0.0570  74  GLU B CD  
505  O OE1 . GLU A 401 ? 1.9346 2.1352 1.8821 -0.1045 0.0125  0.0610  74  GLU B OE1 
506  O OE2 . GLU A 401 ? 2.2132 2.4145 2.1666 -0.0961 0.0156  0.0561  74  GLU B OE2 
507  N N   . LYS A 402 ? 2.7951 2.9270 2.7139 -0.1078 -0.0008 0.0467  75  LYS B N   
508  C CA  . LYS A 402 ? 2.4721 2.5959 2.3859 -0.1103 -0.0022 0.0457  75  LYS B CA  
509  C C   . LYS A 402 ? 2.3850 2.5067 2.2934 -0.1062 0.0027  0.0409  75  LYS B C   
510  O O   . LYS A 402 ? 2.2891 2.4030 2.1940 -0.1019 0.0041  0.0358  75  LYS B O   
511  C CB  . LYS A 402 ? 2.2751 2.3853 2.1865 -0.1121 -0.0070 0.0438  75  LYS B CB  
512  C CG  . LYS A 402 ? 2.3547 2.4658 2.2709 -0.1170 -0.0125 0.0484  75  LYS B CG  
513  C CD  . LYS A 402 ? 2.2300 2.3275 2.1433 -0.1184 -0.0167 0.0454  75  LYS B CD  
514  C CE  . LYS A 402 ? 1.7637 1.8615 1.6817 -0.1233 -0.0226 0.0495  75  LYS B CE  
515  N NZ  . LYS A 402 ? 1.6614 1.7461 1.5764 -0.1244 -0.0265 0.0458  75  LYS B NZ  
516  N N   . ARG A 403 ? 2.0817 2.2107 1.9895 -0.1078 0.0048  0.0428  76  ARG B N   
517  C CA  . ARG A 403 ? 2.0694 2.1983 1.9722 -0.1045 0.0095  0.0388  76  ARG B CA  
518  C C   . ARG A 403 ? 2.0057 2.1199 1.9023 -0.1026 0.0089  0.0338  76  ARG B C   
519  O O   . ARG A 403 ? 2.2138 2.3259 2.1065 -0.0982 0.0127  0.0293  76  ARG B O   
520  C CB  . ARG A 403 ? 2.1628 2.3002 2.0654 -0.1086 0.0102  0.0427  76  ARG B CB  
521  C CG  . ARG A 403 ? 2.3028 2.4399 2.2000 -0.1058 0.0145  0.0388  76  ARG B CG  
522  C CD  . ARG A 403 ? 2.2788 2.4253 2.1754 -0.1097 0.0156  0.0425  76  ARG B CD  
523  N NE  . ARG A 403 ? 2.2299 2.3738 2.1203 -0.1063 0.0197  0.0375  76  ARG B NE  
524  C CZ  . ARG A 403 ? 2.5894 2.7420 2.4772 -0.1076 0.0228  0.0383  76  ARG B CZ  
525  N NH1 . ARG A 403 ? 2.8957 3.0614 2.7869 -0.1120 0.0227  0.0439  76  ARG B NH1 
526  N NH2 . ARG A 403 ? 2.6034 2.7525 2.4854 -0.1040 0.0263  0.0331  76  ARG B NH2 
527  N N   . ILE A 404 ? 2.0298 2.1339 1.9257 -0.1058 0.0041  0.0344  77  ILE B N   
528  C CA  . ILE A 404 ? 1.9398 2.0311 1.8301 -0.1052 0.0033  0.0305  77  ILE B CA  
529  C C   . ILE A 404 ? 1.7840 1.8693 1.6708 -0.0993 0.0062  0.0248  77  ILE B C   
530  O O   . ILE A 404 ? 1.4670 1.5449 1.3488 -0.0974 0.0076  0.0212  77  ILE B O   
531  C CB  . ILE A 404 ? 1.8602 1.9426 1.7517 -0.1093 -0.0024 0.0317  77  ILE B CB  
532  C CG1 . ILE A 404 ? 1.8079 1.8956 1.7034 -0.1154 -0.0058 0.0376  77  ILE B CG1 
533  C CG2 . ILE A 404 ? 1.7533 1.8231 1.6398 -0.1087 -0.0030 0.0276  77  ILE B CG2 
534  C CD1 . ILE A 404 ? 1.8197 1.8999 1.7179 -0.1194 -0.0118 0.0388  77  ILE B CD1 
535  N N   . GLU A 405 ? 1.9246 2.0135 1.8143 -0.0964 0.0071  0.0242  78  GLU B N   
536  C CA  . GLU A 405 ? 2.0907 2.1761 1.9780 -0.0907 0.0101  0.0194  78  GLU B CA  
537  C C   . GLU A 405 ? 1.7805 1.8707 1.6656 -0.0875 0.0148  0.0172  78  GLU B C   
538  O O   . GLU A 405 ? 1.8774 1.9602 1.7577 -0.0847 0.0163  0.0132  78  GLU B O   
539  C CB  . GLU A 405 ? 2.4577 2.5483 2.3500 -0.0885 0.0100  0.0201  78  GLU B CB  
540  C CG  . GLU A 405 ? 2.5344 2.6215 2.4254 -0.0828 0.0124  0.0157  78  GLU B CG  
541  C CD  . GLU A 405 ? 2.8485 2.9399 2.7449 -0.0812 0.0116  0.0168  78  GLU B CD  
542  O OE1 . GLU A 405 ? 2.9932 3.0902 2.8940 -0.0844 0.0093  0.0209  78  GLU B OE1 
543  O OE2 . GLU A 405 ? 2.9079 2.9972 2.8045 -0.0767 0.0130  0.0137  78  GLU B OE2 
544  N N   . ASN A 406 ? 1.9961 2.0991 1.8848 -0.0877 0.0173  0.0196  79  ASN B N   
545  C CA  . ASN A 406 ? 2.0126 2.1212 1.8993 -0.0845 0.0221  0.0170  79  ASN B CA  
546  C C   . ASN A 406 ? 2.0382 2.1426 1.9192 -0.0871 0.0222  0.0168  79  ASN B C   
547  O O   . ASN A 406 ? 2.0212 2.1226 1.8977 -0.0840 0.0250  0.0129  79  ASN B O   
548  C CB  . ASN A 406 ? 1.9655 2.0897 1.8577 -0.0846 0.0248  0.0198  79  ASN B CB  
549  C CG  . ASN A 406 ? 1.8018 1.9302 1.6989 -0.0796 0.0267  0.0177  79  ASN B CG  
550  O OD1 . ASN A 406 ? 1.4613 1.5811 1.3583 -0.0771 0.0251  0.0154  79  ASN B OD1 
551  N ND2 . ASN A 406 ? 1.8911 2.0331 1.7933 -0.0786 0.0298  0.0190  79  ASN B ND2 
552  N N   . LEU A 407 ? 1.8809 1.9844 1.7623 -0.0929 0.0187  0.0211  80  LEU B N   
553  C CA  . LEU A 407 ? 1.7050 1.8022 1.5817 -0.0959 0.0175  0.0213  80  LEU B CA  
554  C C   . LEU A 407 ? 1.7179 1.8016 1.5895 -0.0928 0.0174  0.0163  80  LEU B C   
555  O O   . LEU A 407 ? 1.8069 1.8891 1.6741 -0.0906 0.0202  0.0134  80  LEU B O   
556  C CB  . LEU A 407 ? 1.6842 1.7796 1.5634 -0.1022 0.0124  0.0262  80  LEU B CB  
557  C CG  . LEU A 407 ? 1.9285 2.0367 1.8122 -0.1067 0.0117  0.0323  80  LEU B CG  
558  C CD1 . LEU A 407 ? 2.0546 2.1588 1.9415 -0.1124 0.0059  0.0366  80  LEU B CD1 
559  C CD2 . LEU A 407 ? 1.7027 1.8169 1.5829 -0.1082 0.0144  0.0331  80  LEU B CD2 
560  N N   . ASN A 408 ? 1.4956 1.5697 1.3677 -0.0928 0.0142  0.0153  81  ASN B N   
561  C CA  . ASN A 408 ? 1.5694 1.6315 1.4369 -0.0897 0.0144  0.0107  81  ASN B CA  
562  C C   . ASN A 408 ? 1.6551 1.7175 1.5203 -0.0838 0.0183  0.0063  81  ASN B C   
563  O O   . ASN A 408 ? 1.9931 2.0486 1.8537 -0.0819 0.0195  0.0032  81  ASN B O   
564  C CB  . ASN A 408 ? 1.6480 1.7021 1.5165 -0.0895 0.0113  0.0095  81  ASN B CB  
565  C CG  . ASN A 408 ? 1.7871 1.8296 1.6509 -0.0869 0.0114  0.0052  81  ASN B CG  
566  O OD1 . ASN A 408 ? 1.8692 1.9074 1.7295 -0.0874 0.0121  0.0043  81  ASN B OD1 
567  N ND2 . ASN A 408 ? 2.0020 2.0400 1.8655 -0.0841 0.0111  0.0027  81  ASN B ND2 
568  N N   . LYS A 409 ? 1.3850 1.4536 1.2540 -0.0807 0.0198  0.0059  82  LYS B N   
569  C CA  . LYS A 409 ? 1.6498 1.7184 1.5177 -0.0750 0.0231  0.0017  82  LYS B CA  
570  C C   . LYS A 409 ? 1.9988 2.0709 1.8633 -0.0739 0.0265  0.0000  82  LYS B C   
571  O O   . LYS A 409 ? 2.3281 2.3933 2.1884 -0.0710 0.0277  -0.0037 82  LYS B O   
572  C CB  . LYS A 409 ? 1.8696 1.9465 1.7434 -0.0722 0.0242  0.0020  82  LYS B CB  
573  C CG  . LYS A 409 ? 2.1199 2.1921 1.9962 -0.0725 0.0209  0.0029  82  LYS B CG  
574  C CD  . LYS A 409 ? 2.1490 2.2301 2.0318 -0.0700 0.0219  0.0037  82  LYS B CD  
575  C CE  . LYS A 409 ? 2.1061 2.1830 1.9913 -0.0704 0.0185  0.0047  82  LYS B CE  
576  N NZ  . LYS A 409 ? 2.0808 2.1667 1.9730 -0.0682 0.0193  0.0060  82  LYS B NZ  
577  N N   . LYS A 410 ? 1.7685 1.8512 1.6344 -0.0768 0.0278  0.0030  83  LYS B N   
578  C CA  . LYS A 410 ? 1.8326 1.9187 1.6943 -0.0766 0.0308  0.0016  83  LYS B CA  
579  C C   . LYS A 410 ? 1.9345 2.0102 1.7906 -0.0792 0.0289  0.0015  83  LYS B C   
580  O O   . LYS A 410 ? 2.1563 2.2296 2.0078 -0.0773 0.0310  -0.0015 83  LYS B O   
581  C CB  . LYS A 410 ? 1.7419 1.8418 1.6058 -0.0802 0.0323  0.0055  83  LYS B CB  
582  C CG  . LYS A 410 ? 1.9795 2.0919 1.8487 -0.0776 0.0353  0.0054  83  LYS B CG  
583  C CD  . LYS A 410 ? 2.1730 2.2982 2.0435 -0.0822 0.0363  0.0099  83  LYS B CD  
584  C CE  . LYS A 410 ? 2.4600 2.5995 2.3362 -0.0799 0.0396  0.0100  83  LYS B CE  
585  N NZ  . LYS A 410 ? 2.2866 2.4394 2.1641 -0.0849 0.0405  0.0149  83  LYS B NZ  
586  N N   . VAL A 411 ? 2.1331 2.2030 1.9899 -0.0836 0.0248  0.0046  84  VAL B N   
587  C CA  . VAL A 411 ? 2.0611 2.1219 1.9137 -0.0863 0.0228  0.0048  84  VAL B CA  
588  C C   . VAL A 411 ? 2.1360 2.1856 1.9846 -0.0821 0.0234  0.0000  84  VAL B C   
589  O O   . VAL A 411 ? 2.2291 2.2746 2.0731 -0.0817 0.0245  -0.0017 84  VAL B O   
590  C CB  . VAL A 411 ? 2.2018 2.2584 2.0572 -0.0915 0.0181  0.0086  84  VAL B CB  
591  C CG1 . VAL A 411 ? 2.2046 2.2489 2.0567 -0.0929 0.0158  0.0075  84  VAL B CG1 
592  C CG2 . VAL A 411 ? 2.2763 2.3432 2.1347 -0.0967 0.0170  0.0141  84  VAL B CG2 
593  N N   . ASP A 412 ? 1.9768 2.0218 1.8270 -0.0789 0.0228  -0.0022 85  ASP B N   
594  C CA  . ASP A 412 ? 2.0426 2.0777 1.8896 -0.0748 0.0232  -0.0064 85  ASP B CA  
595  C C   . ASP A 412 ? 1.9615 2.0000 1.8068 -0.0699 0.0270  -0.0099 85  ASP B C   
596  O O   . ASP A 412 ? 2.0517 2.0834 1.8927 -0.0680 0.0277  -0.0127 85  ASP B O   
597  C CB  . ASP A 412 ? 1.9903 2.0206 1.8397 -0.0733 0.0212  -0.0072 85  ASP B CB  
598  C CG  . ASP A 412 ? 2.1382 2.1622 1.9882 -0.0776 0.0174  -0.0052 85  ASP B CG  
599  O OD1 . ASP A 412 ? 1.9471 1.9680 1.7956 -0.0810 0.0161  -0.0038 85  ASP B OD1 
600  O OD2 . ASP A 412 ? 2.3013 2.3237 2.1536 -0.0775 0.0156  -0.0052 85  ASP B OD2 
601  N N   . ASP A 413 ? 1.8365 1.8854 1.6854 -0.0678 0.0293  -0.0100 86  ASP B N   
602  C CA  . ASP A 413 ? 1.7579 1.8107 1.6062 -0.0630 0.0329  -0.0138 86  ASP B CA  
603  C C   . ASP A 413 ? 1.8569 1.9120 1.7003 -0.0643 0.0350  -0.0145 86  ASP B C   
604  O O   . ASP A 413 ? 1.9697 2.0229 1.8102 -0.0605 0.0371  -0.0185 86  ASP B O   
605  C CB  . ASP A 413 ? 1.9960 2.0605 1.8501 -0.0608 0.0350  -0.0136 86  ASP B CB  
606  C CG  . ASP A 413 ? 1.9952 2.0583 1.8543 -0.0601 0.0326  -0.0124 86  ASP B CG  
607  O OD1 . ASP A 413 ? 1.8784 1.9312 1.7361 -0.0596 0.0301  -0.0132 86  ASP B OD1 
608  O OD2 . ASP A 413 ? 1.8045 1.8772 1.6691 -0.0603 0.0332  -0.0104 86  ASP B OD2 
609  N N   . GLY A 414 ? 2.1501 2.2096 1.9928 -0.0697 0.0341  -0.0105 87  GLY B N   
610  C CA  . GLY A 414 ? 2.1209 2.1838 1.9590 -0.0719 0.0358  -0.0102 87  GLY B CA  
611  C C   . GLY A 414 ? 1.8885 1.9397 1.7217 -0.0738 0.0335  -0.0103 87  GLY B C   
612  O O   . GLY A 414 ? 1.7685 1.8187 1.5967 -0.0735 0.0351  -0.0122 87  GLY B O   
613  N N   . PHE A 415 ? 1.7510 1.7932 1.5854 -0.0759 0.0299  -0.0085 88  PHE B N   
614  C CA  . PHE A 415 ? 1.8460 1.8760 1.6764 -0.0763 0.0280  -0.0097 88  PHE B CA  
615  C C   . PHE A 415 ? 1.8243 1.8484 1.6519 -0.0705 0.0298  -0.0147 88  PHE B C   
616  O O   . PHE A 415 ? 1.8275 1.8461 1.6505 -0.0701 0.0302  -0.0163 88  PHE B O   
617  C CB  . PHE A 415 ? 2.2114 2.2331 2.0442 -0.0787 0.0241  -0.0078 88  PHE B CB  
618  C CG  . PHE A 415 ? 2.2217 2.2459 2.0566 -0.0850 0.0214  -0.0029 88  PHE B CG  
619  C CD1 . PHE A 415 ? 1.8481 1.8815 1.6823 -0.0884 0.0224  0.0000  88  PHE B CD1 
620  C CD2 . PHE A 415 ? 2.3583 2.3757 2.1960 -0.0876 0.0177  -0.0014 88  PHE B CD2 
621  C CE1 . PHE A 415 ? 1.6529 1.6886 1.4896 -0.0944 0.0193  0.0050  88  PHE B CE1 
622  C CE2 . PHE A 415 ? 2.2026 2.2219 2.0431 -0.0934 0.0147  0.0031  88  PHE B CE2 
623  C CZ  . PHE A 415 ? 1.8475 1.8758 1.6877 -0.0968 0.0153  0.0065  88  PHE B CZ  
624  N N   . LEU A 416 ? 1.7549 1.7801 1.5856 -0.0662 0.0307  -0.0170 89  LEU B N   
625  C CA  . LEU A 416 ? 1.5810 1.6034 1.4101 -0.0606 0.0327  -0.0216 89  LEU B CA  
626  C C   . LEU A 416 ? 1.7574 1.7895 1.5853 -0.0590 0.0363  -0.0235 89  LEU B C   
627  O O   . LEU A 416 ? 1.8885 1.9306 1.7173 -0.0621 0.0375  -0.0210 89  LEU B O   
628  C CB  . LEU A 416 ? 1.6938 1.7151 1.5273 -0.0568 0.0321  -0.0230 89  LEU B CB  
629  C CG  . LEU A 416 ? 1.8974 1.9089 1.7312 -0.0580 0.0288  -0.0218 89  LEU B CG  
630  C CD1 . LEU A 416 ? 1.8865 1.8986 1.7247 -0.0551 0.0281  -0.0225 89  LEU B CD1 
631  C CD2 . LEU A 416 ? 1.7957 1.7961 1.6248 -0.0572 0.0279  -0.0237 89  LEU B CD2 
632  N N   . ASP A 417 ? 1.8476 1.8770 1.6737 -0.0542 0.0380  -0.0280 90  ASP B N   
633  C CA  . ASP A 417 ? 1.9105 1.9472 1.7341 -0.0526 0.0414  -0.0309 90  ASP B CA  
634  C C   . ASP A 417 ? 1.8213 1.8570 1.6388 -0.0572 0.0412  -0.0291 90  ASP B C   
635  O O   . ASP A 417 ? 1.6976 1.7289 1.5103 -0.0556 0.0420  -0.0321 90  ASP B O   
636  C CB  . ASP A 417 ? 1.8585 1.9095 1.6867 -0.0521 0.0442  -0.0307 90  ASP B CB  
637  C CG  . ASP A 417 ? 1.7518 1.8044 1.5862 -0.0467 0.0448  -0.0334 90  ASP B CG  
638  O OD1 . ASP A 417 ? 2.0042 2.0476 1.8386 -0.0429 0.0435  -0.0361 90  ASP B OD1 
639  O OD2 . ASP A 417 ? 1.7268 1.7899 1.5664 -0.0464 0.0464  -0.0324 90  ASP B OD2 
640  N N   . ILE A 418 ? 1.6852 1.7244 1.5030 -0.0630 0.0398  -0.0241 91  ILE B N   
641  C CA  . ILE A 418 ? 1.3704 1.4074 1.1830 -0.0679 0.0388  -0.0217 91  ILE B CA  
642  C C   . ILE A 418 ? 1.3925 1.4150 1.2020 -0.0675 0.0361  -0.0225 91  ILE B C   
643  O O   . ILE A 418 ? 1.6604 1.6791 1.4647 -0.0673 0.0366  -0.0242 91  ILE B O   
644  C CB  . ILE A 418 ? 1.5144 1.5570 1.3293 -0.0743 0.0369  -0.0157 91  ILE B CB  
645  C CG1 . ILE A 418 ? 1.8398 1.8981 1.6567 -0.0755 0.0398  -0.0145 91  ILE B CG1 
646  C CG2 . ILE A 418 ? 1.5106 1.5481 1.3213 -0.0796 0.0345  -0.0127 91  ILE B CG2 
647  C CD1 . ILE A 418 ? 1.8485 1.9128 1.6690 -0.0815 0.0375  -0.0083 91  ILE B CD1 
648  N N   . TRP A 419 ? 1.4684 1.4829 1.2809 -0.0674 0.0334  -0.0213 92  TRP B N   
649  C CA  . TRP A 419 ? 1.6166 1.6179 1.4267 -0.0671 0.0310  -0.0220 92  TRP B CA  
650  C C   . TRP A 419 ? 1.5438 1.5400 1.3516 -0.0614 0.0324  -0.0268 92  TRP B C   
651  O O   . TRP A 419 ? 1.4754 1.4635 1.2792 -0.0613 0.0315  -0.0278 92  TRP B O   
652  C CB  . TRP A 419 ? 1.6425 1.6376 1.4566 -0.0678 0.0282  -0.0203 92  TRP B CB  
653  C CG  . TRP A 419 ? 1.8783 1.8737 1.6944 -0.0737 0.0256  -0.0158 92  TRP B CG  
654  C CD1 . TRP A 419 ? 1.8351 1.8323 1.6494 -0.0786 0.0247  -0.0127 92  TRP B CD1 
655  C CD2 . TRP A 419 ? 2.1662 2.1596 1.9868 -0.0754 0.0232  -0.0138 92  TRP B CD2 
656  N NE1 . TRP A 419 ? 1.9241 1.9206 1.7422 -0.0831 0.0217  -0.0088 92  TRP B NE1 
657  C CE2 . TRP A 419 ? 2.2166 2.2106 2.0384 -0.0812 0.0208  -0.0098 92  TRP B CE2 
658  C CE3 . TRP A 419 ? 2.2127 2.2041 2.0364 -0.0729 0.0226  -0.0151 92  TRP B CE3 
659  C CZ2 . TRP A 419 ? 2.4783 2.4706 2.3046 -0.0841 0.0179  -0.0074 92  TRP B CZ2 
660  C CZ3 . TRP A 419 ? 2.3269 2.3169 2.1543 -0.0760 0.0199  -0.0128 92  TRP B CZ3 
661  C CH2 . TRP A 419 ? 2.5911 2.5813 2.4198 -0.0814 0.0176  -0.0093 92  TRP B CH2 
662  N N   . THR A 420 ? 1.3286 1.3293 1.1393 -0.0568 0.0342  -0.0297 93  THR B N   
663  C CA  . THR A 420 ? 1.1813 1.1772 0.9907 -0.0513 0.0350  -0.0343 93  THR B CA  
664  C C   . THR A 420 ? 1.3598 1.3577 1.1640 -0.0508 0.0370  -0.0368 93  THR B C   
665  O O   . THR A 420 ? 1.4722 1.4616 1.2729 -0.0490 0.0362  -0.0390 93  THR B O   
666  C CB  . THR A 420 ? 1.2538 1.2554 1.0686 -0.0466 0.0364  -0.0367 93  THR B CB  
667  O OG1 . THR A 420 ? 1.6502 1.6636 1.4656 -0.0460 0.0397  -0.0382 93  THR B OG1 
668  C CG2 . THR A 420 ? 1.1481 1.1506 0.9678 -0.0482 0.0347  -0.0336 93  THR B CG2 
669  N N   . TYR A 421 ? 1.3211 1.3302 1.1246 -0.0528 0.0395  -0.0365 94  TYR B N   
670  C CA  . TYR A 421 ? 1.4157 1.4281 1.2137 -0.0528 0.0417  -0.0390 94  TYR B CA  
671  C C   . TYR A 421 ? 1.4726 1.4782 1.2650 -0.0575 0.0395  -0.0362 94  TYR B C   
672  O O   . TYR A 421 ? 1.8109 1.8119 1.5983 -0.0565 0.0397  -0.0388 94  TYR B O   
673  C CB  . TYR A 421 ? 1.5256 1.5531 1.3245 -0.0541 0.0450  -0.0390 94  TYR B CB  
674  C CG  . TYR A 421 ? 1.5354 1.5686 1.3283 -0.0549 0.0475  -0.0414 94  TYR B CG  
675  C CD1 . TYR A 421 ? 1.3933 1.4320 1.1823 -0.0613 0.0475  -0.0375 94  TYR B CD1 
676  C CD2 . TYR A 421 ? 1.6958 1.7295 1.4873 -0.0496 0.0498  -0.0477 94  TYR B CD2 
677  C CE1 . TYR A 421 ? 1.5616 1.6063 1.3445 -0.0625 0.0499  -0.0396 94  TYR B CE1 
678  C CE2 . TYR A 421 ? 1.8579 1.8972 1.6434 -0.0505 0.0523  -0.0505 94  TYR B CE2 
679  C CZ  . TYR A 421 ? 1.8460 1.8910 1.6270 -0.0571 0.0524  -0.0463 94  TYR B CZ  
680  O OH  . TYR A 421 ? 1.8822 1.9333 1.6566 -0.0584 0.0548  -0.0489 94  TYR B OH  
681  N N   . ASN A 422 ? 1.2656 1.2701 1.0593 -0.0628 0.0372  -0.0310 95  ASN B N   
682  C CA  . ASN A 422 ? 1.4678 1.4651 1.2577 -0.0674 0.0346  -0.0279 95  ASN B CA  
683  C C   . ASN A 422 ? 1.4284 1.4120 1.2170 -0.0646 0.0326  -0.0298 95  ASN B C   
684  O O   . ASN A 422 ? 1.4283 1.4061 1.2121 -0.0658 0.0317  -0.0299 95  ASN B O   
685  C CB  . ASN A 422 ? 1.4327 1.4308 1.2261 -0.0729 0.0321  -0.0223 95  ASN B CB  
686  C CG  . ASN A 422 ? 1.5127 1.5234 1.3059 -0.0776 0.0333  -0.0190 95  ASN B CG  
687  O OD1 . ASN A 422 ? 1.5620 1.5742 1.3515 -0.0822 0.0325  -0.0165 95  ASN B OD1 
688  N ND2 . ASN A 422 ? 1.6185 1.6388 1.4161 -0.0767 0.0349  -0.0188 95  ASN B ND2 
689  N N   . ALA A 423 ? 1.1540 1.1324 0.9466 -0.0610 0.0317  -0.0309 96  ALA B N   
690  C CA  . ALA A 423 ? 1.1816 1.1478 0.9734 -0.0583 0.0298  -0.0324 96  ALA B CA  
691  C C   . ALA A 423 ? 1.4406 1.4049 1.2291 -0.0537 0.0312  -0.0371 96  ALA B C   
692  O O   . ALA A 423 ? 1.6728 1.6280 1.4581 -0.0532 0.0296  -0.0377 96  ALA B O   
693  C CB  . ALA A 423 ? 1.0959 1.0586 0.8928 -0.0560 0.0286  -0.0323 96  ALA B CB  
694  N N   . GLU A 424 ? 1.3722 1.3447 1.1620 -0.0501 0.0339  -0.0405 97  GLU B N   
695  C CA  . GLU A 424 ? 1.4107 1.3824 1.1975 -0.0460 0.0353  -0.0454 97  GLU B CA  
696  C C   . GLU A 424 ? 1.4749 1.4460 1.2549 -0.0492 0.0355  -0.0452 97  GLU B C   
697  O O   . GLU A 424 ? 1.4520 1.4155 1.2283 -0.0474 0.0345  -0.0475 97  GLU B O   
698  C CB  . GLU A 424 ? 1.3557 1.3384 1.1455 -0.0424 0.0385  -0.0490 97  GLU B CB  
699  C CG  . GLU A 424 ? 1.3555 1.3386 1.1523 -0.0385 0.0381  -0.0496 97  GLU B CG  
700  C CD  . GLU A 424 ? 1.6150 1.6097 1.4158 -0.0352 0.0413  -0.0529 97  GLU B CD  
701  O OE1 . GLU A 424 ? 1.8732 1.8766 1.6711 -0.0365 0.0441  -0.0543 97  GLU B OE1 
702  O OE2 . GLU A 424 ? 1.3658 1.3611 1.1726 -0.0315 0.0410  -0.0540 97  GLU B OE2 
703  N N   . LEU A 425 ? 1.2849 1.2639 1.0631 -0.0544 0.0364  -0.0421 98  LEU B N   
704  C CA  . LEU A 425 ? 1.1953 1.1743 0.9669 -0.0585 0.0362  -0.0411 98  LEU B CA  
705  C C   . LEU A 425 ? 1.2846 1.2507 1.0543 -0.0607 0.0326  -0.0384 98  LEU B C   
706  O O   . LEU A 425 ? 1.5311 1.4922 1.2954 -0.0610 0.0319  -0.0396 98  LEU B O   
707  C CB  . LEU A 425 ? 1.3011 1.2911 1.0721 -0.0643 0.0372  -0.0372 98  LEU B CB  
708  C CG  . LEU A 425 ? 1.4692 1.4732 1.2414 -0.0625 0.0412  -0.0398 98  LEU B CG  
709  C CD1 . LEU A 425 ? 1.4775 1.4926 1.2498 -0.0687 0.0418  -0.0350 98  LEU B CD1 
710  C CD2 . LEU A 425 ? 1.3767 1.3833 1.1439 -0.0592 0.0438  -0.0457 98  LEU B CD2 
711  N N   . LEU A 426 ? 1.2744 1.2352 1.0484 -0.0623 0.0302  -0.0347 99  LEU B N   
712  C CA  . LEU A 426 ? 1.1631 1.1121 0.9362 -0.0645 0.0269  -0.0322 99  LEU B CA  
713  C C   . LEU A 426 ? 1.3055 1.2449 1.0773 -0.0595 0.0261  -0.0357 99  LEU B C   
714  O O   . LEU A 426 ? 1.4629 1.3943 1.2311 -0.0607 0.0243  -0.0351 99  LEU B O   
715  C CB  . LEU A 426 ? 0.9812 0.9273 0.7599 -0.0667 0.0248  -0.0284 99  LEU B CB  
716  C CG  . LEU A 426 ? 1.0171 0.9517 0.7964 -0.0689 0.0215  -0.0258 99  LEU B CG  
717  C CD1 . LEU A 426 ? 1.4272 1.3596 1.2020 -0.0733 0.0202  -0.0235 99  LEU B CD1 
718  C CD2 . LEU A 426 ? 1.2983 1.2325 1.0833 -0.0718 0.0199  -0.0224 99  LEU B CD2 
719  N N   . VAL A 427 ? 1.2553 1.1953 1.0303 -0.0541 0.0272  -0.0390 100 VAL B N   
720  C CA  . VAL A 427 ? 1.3825 1.3146 1.1568 -0.0491 0.0264  -0.0425 100 VAL B CA  
721  C C   . VAL A 427 ? 1.4941 1.4262 1.2623 -0.0485 0.0272  -0.0456 100 VAL B C   
722  O O   . VAL A 427 ? 1.4706 1.3936 1.2357 -0.0484 0.0251  -0.0456 100 VAL B O   
723  C CB  . VAL A 427 ? 1.3315 1.2665 1.1107 -0.0438 0.0275  -0.0455 100 VAL B CB  
724  C CG1 . VAL A 427 ? 1.4288 1.3553 1.2081 -0.0389 0.0259  -0.0485 100 VAL B CG1 
725  C CG2 . VAL A 427 ? 1.1270 1.0617 0.9114 -0.0449 0.0265  -0.0424 100 VAL B CG2 
726  N N   . LEU A 428 ? 1.4282 1.3708 1.1948 -0.0480 0.0302  -0.0483 101 LEU B N   
727  C CA  . LEU A 428 ? 1.5011 1.4449 1.2617 -0.0471 0.0313  -0.0520 101 LEU B CA  
728  C C   . LEU A 428 ? 1.5772 1.5164 1.3319 -0.0526 0.0294  -0.0487 101 LEU B C   
729  O O   . LEU A 428 ? 1.7437 1.6760 1.4939 -0.0518 0.0281  -0.0506 101 LEU B O   
730  C CB  . LEU A 428 ? 1.3192 1.2768 1.0793 -0.0467 0.0352  -0.0550 101 LEU B CB  
731  C CG  . LEU A 428 ? 1.3649 1.3279 1.1312 -0.0410 0.0372  -0.0588 101 LEU B CG  
732  C CD1 . LEU A 428 ? 1.1049 1.0827 0.8717 -0.0420 0.0410  -0.0599 101 LEU B CD1 
733  C CD2 . LEU A 428 ? 1.7428 1.7004 1.5094 -0.0348 0.0369  -0.0646 101 LEU B CD2 
734  N N   . LEU A 429 ? 1.4594 1.4021 1.2146 -0.0584 0.0289  -0.0435 102 LEU B N   
735  C CA  . LEU A 429 ? 1.4487 1.3878 1.1996 -0.0643 0.0267  -0.0394 102 LEU B CA  
736  C C   . LEU A 429 ? 1.7703 1.6953 1.5212 -0.0638 0.0233  -0.0381 102 LEU B C   
737  O O   . LEU A 429 ? 2.0347 1.9545 1.7804 -0.0647 0.0220  -0.0387 102 LEU B O   
738  C CB  . LEU A 429 ? 1.4930 1.4373 1.2471 -0.0699 0.0261  -0.0338 102 LEU B CB  
739  C CG  . LEU A 429 ? 1.5137 1.4719 1.2664 -0.0737 0.0285  -0.0325 102 LEU B CG  
740  C CD1 . LEU A 429 ? 1.7437 1.7053 1.5028 -0.0764 0.0277  -0.0281 102 LEU B CD1 
741  C CD2 . LEU A 429 ? 1.5913 1.5514 1.3378 -0.0796 0.0275  -0.0298 102 LEU B CD2 
742  N N   . GLU A 430 ? 1.6041 1.5233 1.3609 -0.0624 0.0217  -0.0363 103 GLU B N   
743  C CA  . GLU A 430 ? 1.5036 1.4101 1.2611 -0.0617 0.0187  -0.0350 103 GLU B CA  
744  C C   . GLU A 430 ? 1.5455 1.4463 1.3003 -0.0566 0.0184  -0.0394 103 GLU B C   
745  O O   . GLU A 430 ? 1.7446 1.6360 1.4972 -0.0571 0.0159  -0.0384 103 GLU B O   
746  C CB  . GLU A 430 ? 1.6289 1.5319 1.3932 -0.0605 0.0177  -0.0332 103 GLU B CB  
747  C CG  . GLU A 430 ? 1.8728 1.7648 1.6387 -0.0623 0.0145  -0.0300 103 GLU B CG  
748  C CD  . GLU A 430 ? 2.0182 1.9090 1.7826 -0.0687 0.0127  -0.0256 103 GLU B CD  
749  O OE1 . GLU A 430 ? 1.9330 1.8288 1.7005 -0.0725 0.0127  -0.0227 103 GLU B OE1 
750  O OE2 . GLU A 430 ? 2.3103 2.1952 2.0710 -0.0700 0.0110  -0.0249 103 GLU B OE2 
751  N N   . ASN A 431 ? 1.3303 1.2363 1.0857 -0.0518 0.0207  -0.0441 104 ASN B N   
752  C CA  . ASN A 431 ? 1.2294 1.1300 0.9830 -0.0468 0.0201  -0.0486 104 ASN B CA  
753  C C   . ASN A 431 ? 1.4547 1.3537 1.2010 -0.0488 0.0196  -0.0498 104 ASN B C   
754  O O   . ASN A 431 ? 1.7007 1.5900 1.4448 -0.0480 0.0170  -0.0499 104 ASN B O   
755  C CB  . ASN A 431 ? 1.2698 1.1776 1.0263 -0.0415 0.0227  -0.0536 104 ASN B CB  
756  C CG  . ASN A 431 ? 1.3853 1.2926 1.1491 -0.0388 0.0223  -0.0526 104 ASN B CG  
757  O OD1 . ASN A 431 ? 1.5366 1.4366 1.3028 -0.0398 0.0200  -0.0492 104 ASN B OD1 
758  N ND2 . ASN A 431 ? 1.5331 1.4485 1.3004 -0.0354 0.0246  -0.0556 104 ASN B ND2 
759  N N   . GLU A 432 ? 1.4510 1.3599 1.1933 -0.0518 0.0221  -0.0505 105 GLU B N   
760  C CA  . GLU A 432 ? 1.5640 1.4720 1.2985 -0.0546 0.0216  -0.0513 105 GLU B CA  
761  C C   . GLU A 432 ? 1.6008 1.5004 1.3336 -0.0599 0.0181  -0.0456 105 GLU B C   
762  O O   . GLU A 432 ? 1.6994 1.5926 1.4270 -0.0608 0.0161  -0.0460 105 GLU B O   
763  C CB  . GLU A 432 ? 1.5527 1.4738 1.2831 -0.0577 0.0248  -0.0525 105 GLU B CB  
764  C CG  . GLU A 432 ? 1.5984 1.5277 1.3294 -0.0525 0.0283  -0.0591 105 GLU B CG  
765  C CD  . GLU A 432 ? 2.0135 1.9566 1.7405 -0.0557 0.0317  -0.0600 105 GLU B CD  
766  O OE1 . GLU A 432 ? 2.2020 2.1490 1.9271 -0.0622 0.0312  -0.0546 105 GLU B OE1 
767  O OE2 . GLU A 432 ? 2.2241 2.1744 1.9502 -0.0518 0.0348  -0.0661 105 GLU B OE2 
768  N N   . ARG A 433 ? 1.3917 1.2913 1.1289 -0.0635 0.0172  -0.0403 106 ARG B N   
769  C CA  . ARG A 433 ? 1.5630 1.4546 1.2998 -0.0684 0.0137  -0.0350 106 ARG B CA  
770  C C   . ARG A 433 ? 1.5626 1.4414 1.3005 -0.0653 0.0109  -0.0352 106 ARG B C   
771  O O   . ARG A 433 ? 1.6536 1.5254 1.3880 -0.0679 0.0083  -0.0333 106 ARG B O   
772  C CB  . ARG A 433 ? 1.6044 1.4983 1.3469 -0.0723 0.0131  -0.0299 106 ARG B CB  
773  C CG  . ARG A 433 ? 1.6847 1.5904 1.4254 -0.0768 0.0150  -0.0282 106 ARG B CG  
774  C CD  . ARG A 433 ? 1.5695 1.4757 1.3156 -0.0819 0.0131  -0.0223 106 ARG B CD  
775  N NE  . ARG A 433 ? 1.9046 1.8099 1.6579 -0.0792 0.0135  -0.0222 106 ARG B NE  
776  C CZ  . ARG A 433 ? 2.1165 2.0310 1.8726 -0.0783 0.0159  -0.0231 106 ARG B CZ  
777  N NH1 . ARG A 433 ? 2.0760 2.0016 1.8287 -0.0795 0.0184  -0.0242 106 ARG B NH1 
778  N NH2 . ARG A 433 ? 2.1611 2.0741 1.9236 -0.0765 0.0157  -0.0226 106 ARG B NH2 
779  N N   . THR A 434 ? 1.4863 1.3622 1.2291 -0.0600 0.0112  -0.0374 107 THR B N   
780  C CA  . THR A 434 ? 1.4061 1.2707 1.1502 -0.0569 0.0086  -0.0376 107 THR B CA  
781  C C   . THR A 434 ? 1.5631 1.4242 1.3015 -0.0545 0.0079  -0.0415 107 THR B C   
782  O O   . THR A 434 ? 1.9031 1.7549 1.6396 -0.0552 0.0049  -0.0400 107 THR B O   
783  C CB  . THR A 434 ? 1.4060 1.2694 1.1564 -0.0520 0.0090  -0.0389 107 THR B CB  
784  O OG1 . THR A 434 ? 1.5416 1.4111 1.2918 -0.0473 0.0113  -0.0441 107 THR B OG1 
785  C CG2 . THR A 434 ? 1.4748 1.3418 1.2305 -0.0544 0.0097  -0.0356 107 THR B CG2 
786  N N   . LEU A 435 ? 1.4753 1.3440 1.2110 -0.0517 0.0105  -0.0466 108 LEU B N   
787  C CA  . LEU A 435 ? 1.3937 1.2593 1.1242 -0.0490 0.0099  -0.0513 108 LEU B CA  
788  C C   . LEU A 435 ? 1.4712 1.3343 1.1945 -0.0543 0.0083  -0.0492 108 LEU B C   
789  O O   . LEU A 435 ? 1.5273 1.3814 1.2475 -0.0538 0.0054  -0.0496 108 LEU B O   
790  C CB  . LEU A 435 ? 1.3225 1.1980 1.0521 -0.0453 0.0134  -0.0575 108 LEU B CB  
791  C CG  . LEU A 435 ? 1.2442 1.1219 0.9811 -0.0395 0.0146  -0.0603 108 LEU B CG  
792  C CD1 . LEU A 435 ? 1.6575 1.5439 1.3935 -0.0355 0.0177  -0.0670 108 LEU B CD1 
793  C CD2 . LEU A 435 ? 1.6291 1.4954 1.3697 -0.0356 0.0112  -0.0600 108 LEU B CD2 
794  N N   . ASP A 436 ? 1.4183 1.2893 1.1389 -0.0598 0.0098  -0.0466 109 ASP B N   
795  C CA  . ASP A 436 ? 1.4676 1.3372 1.1813 -0.0655 0.0081  -0.0441 109 ASP B CA  
796  C C   . ASP A 436 ? 1.6604 1.5193 1.3762 -0.0690 0.0040  -0.0379 109 ASP B C   
797  O O   . ASP A 436 ? 1.9108 1.7636 1.6218 -0.0717 0.0013  -0.0366 109 ASP B O   
798  C CB  . ASP A 436 ? 1.5634 1.4453 1.2742 -0.0708 0.0105  -0.0425 109 ASP B CB  
799  C CG  . ASP A 436 ? 1.9969 1.8896 1.7037 -0.0681 0.0145  -0.0489 109 ASP B CG  
800  O OD1 . ASP A 436 ? 1.8067 1.6965 1.5119 -0.0627 0.0149  -0.0548 109 ASP B OD1 
801  O OD2 . ASP A 436 ? 2.3741 2.2784 2.0799 -0.0714 0.0171  -0.0480 109 ASP B OD2 
802  N N   . TYR A 437 ? 1.6079 1.4647 1.3311 -0.0693 0.0035  -0.0341 110 TYR B N   
803  C CA  . TYR A 437 ? 1.8111 1.6574 1.5378 -0.0713 -0.0002 -0.0292 110 TYR B CA  
804  C C   . TYR A 437 ? 1.8601 1.6959 1.5855 -0.0674 -0.0026 -0.0312 110 TYR B C   
805  O O   . TYR A 437 ? 1.8069 1.6346 1.5305 -0.0701 -0.0058 -0.0281 110 TYR B O   
806  C CB  . TYR A 437 ? 1.8120 1.6582 1.5471 -0.0704 0.0003  -0.0267 110 TYR B CB  
807  C CG  . TYR A 437 ? 1.4964 1.3324 1.2363 -0.0717 -0.0030 -0.0223 110 TYR B CG  
808  C CD1 . TYR A 437 ? 1.9059 1.7375 1.6448 -0.0773 -0.0058 -0.0176 110 TYR B CD1 
809  C CD2 . TYR A 437 ? 1.3890 1.2202 1.1348 -0.0675 -0.0032 -0.0228 110 TYR B CD2 
810  C CE1 . TYR A 437 ? 2.0041 1.8266 1.7481 -0.0784 -0.0086 -0.0137 110 TYR B CE1 
811  C CE2 . TYR A 437 ? 1.6249 1.4476 1.3752 -0.0686 -0.0058 -0.0190 110 TYR B CE2 
812  C CZ  . TYR A 437 ? 1.8255 1.6439 1.5752 -0.0739 -0.0084 -0.0146 110 TYR B CZ  
813  O OH  . TYR A 437 ? 1.8572 1.6674 1.6121 -0.0749 -0.0109 -0.0110 110 TYR B OH  
814  N N   . HIS A 438 ? 1.8402 1.6762 1.5672 -0.0610 -0.0013 -0.0361 111 HIS B N   
815  C CA  . HIS A 438 ? 1.8265 1.6533 1.5526 -0.0570 -0.0037 -0.0383 111 HIS B CA  
816  C C   . HIS A 438 ? 1.7867 1.6109 1.5047 -0.0588 -0.0053 -0.0400 111 HIS B C   
817  O O   . HIS A 438 ? 1.9179 1.7324 1.6345 -0.0599 -0.0088 -0.0376 111 HIS B O   
818  C CB  . HIS A 438 ? 1.6709 1.5000 1.4002 -0.0502 -0.0021 -0.0435 111 HIS B CB  
819  C CG  . HIS A 438 ? 1.6736 1.5038 1.4107 -0.0482 -0.0012 -0.0417 111 HIS B CG  
820  N ND1 . HIS A 438 ? 1.8633 1.7003 1.6038 -0.0440 0.0013  -0.0453 111 HIS B ND1 
821  C CD2 . HIS A 438 ? 1.6099 1.4354 1.3521 -0.0497 -0.0027 -0.0370 111 HIS B CD2 
822  C CE1 . HIS A 438 ? 1.5790 1.4154 1.3257 -0.0434 0.0013  -0.0427 111 HIS B CE1 
823  N NE2 . HIS A 438 ? 1.6246 1.4542 1.3724 -0.0467 -0.0009 -0.0378 111 HIS B NE2 
824  N N   . ASP A 439 ? 1.4782 1.3113 1.1907 -0.0591 -0.0026 -0.0442 112 ASP B N   
825  C CA  . ASP A 439 ? 1.4198 1.2514 1.1238 -0.0609 -0.0038 -0.0465 112 ASP B CA  
826  C C   . ASP A 439 ? 1.4942 1.3212 1.1951 -0.0680 -0.0067 -0.0403 112 ASP B C   
827  O O   . ASP A 439 ? 1.7475 1.5669 1.4437 -0.0692 -0.0098 -0.0400 112 ASP B O   
828  C CB  . ASP A 439 ? 1.5572 1.4010 1.2560 -0.0609 0.0002  -0.0518 112 ASP B CB  
829  C CG  . ASP A 439 ? 1.8815 1.7297 1.5840 -0.0537 0.0029  -0.0583 112 ASP B CG  
830  O OD1 . ASP A 439 ? 1.9475 1.7899 1.6568 -0.0494 0.0017  -0.0580 112 ASP B OD1 
831  O OD2 . ASP A 439 ? 2.0064 1.8641 1.7052 -0.0526 0.0062  -0.0636 112 ASP B OD2 
832  N N   . SER A 440 ? 1.2461 1.0774 0.9501 -0.0727 -0.0061 -0.0350 113 SER B N   
833  C CA  . SER A 440 ? 1.3678 1.1951 1.0703 -0.0797 -0.0092 -0.0285 113 SER B CA  
834  C C   . SER A 440 ? 1.5318 1.3460 1.2383 -0.0790 -0.0133 -0.0250 113 SER B C   
835  O O   . SER A 440 ? 1.8189 1.6268 1.5219 -0.0829 -0.0166 -0.0218 113 SER B O   
836  C CB  . SER A 440 ? 1.5788 1.4131 1.2856 -0.0843 -0.0080 -0.0238 113 SER B CB  
837  O OG  . SER A 440 ? 1.8810 1.7279 1.5835 -0.0859 -0.0046 -0.0262 113 SER B OG  
838  N N   . ASN A 441 ? 1.4312 1.2416 1.1452 -0.0744 -0.0131 -0.0251 114 ASN B N   
839  C CA  . ASN A 441 ? 1.4611 1.2597 1.1791 -0.0734 -0.0167 -0.0219 114 ASN B CA  
840  C C   . ASN A 441 ? 1.5361 1.3275 1.2487 -0.0711 -0.0192 -0.0248 114 ASN B C   
841  O O   . ASN A 441 ? 1.5497 1.3323 1.2615 -0.0736 -0.0229 -0.0211 114 ASN B O   
842  C CB  . ASN A 441 ? 1.5868 1.3840 1.3131 -0.0687 -0.0157 -0.0222 114 ASN B CB  
843  C CG  . ASN A 441 ? 1.8095 1.6133 1.5413 -0.0708 -0.0134 -0.0197 114 ASN B CG  
844  O OD1 . ASN A 441 ? 2.0030 1.8128 1.7379 -0.0674 -0.0106 -0.0224 114 ASN B OD1 
845  N ND2 . ASN A 441 ? 1.6351 1.4377 1.3688 -0.0766 -0.0151 -0.0143 114 ASN B ND2 
846  N N   . VAL A 442 ? 1.4614 1.2563 1.1706 -0.0662 -0.0173 -0.0314 115 VAL B N   
847  C CA  . VAL A 442 ? 1.4011 1.1900 1.1046 -0.0641 -0.0196 -0.0350 115 VAL B CA  
848  C C   . VAL A 442 ? 1.5505 1.3372 1.2468 -0.0704 -0.0220 -0.0322 115 VAL B C   
849  O O   . VAL A 442 ? 1.7568 1.5335 1.4519 -0.0717 -0.0261 -0.0295 115 VAL B O   
850  C CB  . VAL A 442 ? 1.3000 1.0958 0.9999 -0.0594 -0.0167 -0.0430 115 VAL B CB  
851  C CG1 . VAL A 442 ? 1.3641 1.1536 1.0578 -0.0579 -0.0194 -0.0469 115 VAL B CG1 
852  C CG2 . VAL A 442 ? 1.3740 1.1718 1.0812 -0.0531 -0.0148 -0.0458 115 VAL B CG2 
853  N N   . LYS A 443 ? 1.4604 1.2567 1.1514 -0.0745 -0.0195 -0.0329 116 LYS B N   
854  C CA  . LYS A 443 ? 1.3740 1.1700 1.0567 -0.0805 -0.0215 -0.0312 116 LYS B CA  
855  C C   . LYS A 443 ? 1.6473 1.4362 1.3329 -0.0864 -0.0254 -0.0228 116 LYS B C   
856  O O   . LYS A 443 ? 1.8461 1.6289 1.5266 -0.0900 -0.0289 -0.0207 116 LYS B O   
857  C CB  . LYS A 443 ? 1.2459 1.0553 0.9233 -0.0839 -0.0178 -0.0332 116 LYS B CB  
858  C CG  . LYS A 443 ? 1.4641 1.2806 1.1377 -0.0784 -0.0141 -0.0420 116 LYS B CG  
859  C CD  . LYS A 443 ? 1.9332 1.7638 1.6019 -0.0820 -0.0101 -0.0436 116 LYS B CD  
860  C CE  . LYS A 443 ? 1.8399 1.6779 1.5054 -0.0763 -0.0063 -0.0528 116 LYS B CE  
861  N NZ  . LYS A 443 ? 1.7942 1.6469 1.4550 -0.0798 -0.0022 -0.0543 116 LYS B NZ  
862  N N   . ASN A 444 ? 1.4881 1.2775 1.1822 -0.0872 -0.0249 -0.0182 117 ASN B N   
863  C CA  . ASN A 444 ? 1.6479 1.4303 1.3465 -0.0921 -0.0286 -0.0106 117 ASN B CA  
864  C C   . ASN A 444 ? 1.7702 1.5400 1.4707 -0.0898 -0.0325 -0.0094 117 ASN B C   
865  O O   . ASN A 444 ? 2.0225 1.7854 1.7217 -0.0943 -0.0364 -0.0046 117 ASN B O   
866  C CB  . ASN A 444 ? 1.5846 1.3699 1.2928 -0.0924 -0.0271 -0.0072 117 ASN B CB  
867  C CG  . ASN A 444 ? 1.7792 1.5765 1.4863 -0.0956 -0.0239 -0.0073 117 ASN B CG  
868  O OD1 . ASN A 444 ? 1.5791 1.3816 1.2795 -0.1008 -0.0242 -0.0064 117 ASN B OD1 
869  N ND2 . ASN A 444 ? 1.9821 1.7845 1.6956 -0.0928 -0.0210 -0.0083 117 ASN B ND2 
870  N N   . LEU A 445 ? 1.7606 1.5272 1.4644 -0.0829 -0.0317 -0.0132 118 LEU B N   
871  C CA  . LEU A 445 ? 1.8995 1.6545 1.6050 -0.0805 -0.0355 -0.0120 118 LEU B CA  
872  C C   . LEU A 445 ? 1.9119 1.6625 1.6082 -0.0818 -0.0383 -0.0140 118 LEU B C   
873  O O   . LEU A 445 ? 1.8089 1.5502 1.5051 -0.0840 -0.0426 -0.0101 118 LEU B O   
874  C CB  . LEU A 445 ? 1.8630 1.6167 1.5734 -0.0730 -0.0342 -0.0158 118 LEU B CB  
875  C CG  . LEU A 445 ? 2.1036 1.8602 1.8232 -0.0716 -0.0320 -0.0136 118 LEU B CG  
876  C CD1 . LEU A 445 ? 2.2304 1.9868 1.9537 -0.0646 -0.0308 -0.0176 118 LEU B CD1 
877  C CD2 . LEU A 445 ? 2.0118 1.7614 1.7376 -0.0749 -0.0348 -0.0067 118 LEU B CD2 
878  N N   . TYR A 446 ? 1.6967 1.4541 1.3856 -0.0804 -0.0359 -0.0204 119 TYR B N   
879  C CA  . TYR A 446 ? 1.6732 1.4270 1.3530 -0.0816 -0.0384 -0.0231 119 TYR B CA  
880  C C   . TYR A 446 ? 1.7854 1.5378 1.4604 -0.0898 -0.0411 -0.0174 119 TYR B C   
881  O O   . TYR A 446 ? 1.7960 1.5399 1.4671 -0.0918 -0.0454 -0.0156 119 TYR B O   
882  C CB  . TYR A 446 ? 1.6571 1.4195 1.3303 -0.0783 -0.0348 -0.0316 119 TYR B CB  
883  C CG  . TYR A 446 ? 1.9496 1.7103 1.6123 -0.0797 -0.0366 -0.0358 119 TYR B CG  
884  C CD1 . TYR A 446 ? 2.0091 1.7598 1.6706 -0.0760 -0.0402 -0.0385 119 TYR B CD1 
885  C CD2 . TYR A 446 ? 2.0156 1.7855 1.6696 -0.0844 -0.0345 -0.0378 119 TYR B CD2 
886  C CE1 . TYR A 446 ? 2.1783 1.9273 1.8301 -0.0770 -0.0419 -0.0430 119 TYR B CE1 
887  C CE2 . TYR A 446 ? 2.2366 2.0056 1.8805 -0.0855 -0.0358 -0.0423 119 TYR B CE2 
888  C CZ  . TYR A 446 ? 2.3877 2.1459 2.0304 -0.0818 -0.0396 -0.0451 119 TYR B CZ  
889  O OH  . TYR A 446 ? 2.4869 2.2441 2.1195 -0.0830 -0.0411 -0.0499 119 TYR B OH  
890  N N   . GLU A 447 ? 1.9191 1.6794 1.5954 -0.0949 -0.0392 -0.0137 120 GLU B N   
891  C CA  . GLU A 447 ? 1.9471 1.7059 1.6204 -0.1031 -0.0424 -0.0072 120 GLU B CA  
892  C C   . GLU A 447 ? 2.0491 1.7967 1.7298 -0.1049 -0.0469 0.0000  120 GLU B C   
893  O O   . GLU A 447 ? 2.1201 1.8621 1.7976 -0.1102 -0.0511 0.0044  120 GLU B O   
894  C CB  . GLU A 447 ? 2.0849 1.8547 1.7589 -0.1082 -0.0398 -0.0044 120 GLU B CB  
895  C CG  . GLU A 447 ? 2.2736 2.0555 1.9392 -0.1085 -0.0358 -0.0102 120 GLU B CG  
896  C CD  . GLU A 447 ? 2.4533 2.2460 2.1208 -0.1136 -0.0336 -0.0066 120 GLU B CD  
897  O OE1 . GLU A 447 ? 2.5438 2.3343 2.2202 -0.1157 -0.0348 -0.0006 120 GLU B OE1 
898  O OE2 . GLU A 447 ? 2.4346 2.2380 2.0949 -0.1155 -0.0307 -0.0099 120 GLU B OE2 
899  N N   . LYS A 448 ? 2.0880 1.8328 1.7789 -0.1008 -0.0460 0.0014  121 LYS B N   
900  C CA  . LYS A 448 ? 2.0463 1.7808 1.7448 -0.1018 -0.0499 0.0076  121 LYS B CA  
901  C C   . LYS A 448 ? 1.9975 1.7218 1.6918 -0.1005 -0.0541 0.0071  121 LYS B C   
902  O O   . LYS A 448 ? 2.0267 1.7437 1.7210 -0.1051 -0.0585 0.0127  121 LYS B O   
903  C CB  . LYS A 448 ? 1.7509 1.4850 1.4597 -0.0966 -0.0478 0.0075  121 LYS B CB  
904  C CG  . LYS A 448 ? 1.7021 1.4269 1.4198 -0.0972 -0.0511 0.0135  121 LYS B CG  
905  C CD  . LYS A 448 ? 1.8340 1.5600 1.5610 -0.0922 -0.0484 0.0127  121 LYS B CD  
906  C CE  . LYS A 448 ? 1.6337 1.3514 1.3697 -0.0925 -0.0512 0.0182  121 LYS B CE  
907  N NZ  . LYS A 448 ? 1.5271 1.2469 1.2717 -0.0879 -0.0483 0.0172  121 LYS B NZ  
908  N N   . VAL A 449 ? 1.9813 1.7048 1.6725 -0.0942 -0.0530 0.0006  122 VAL B N   
909  C CA  . VAL A 449 ? 1.9058 1.6191 1.5938 -0.0923 -0.0572 -0.0002 122 VAL B CA  
910  C C   . VAL A 449 ? 1.9381 1.6504 1.6155 -0.0976 -0.0598 -0.0004 122 VAL B C   
911  O O   . VAL A 449 ? 1.9669 1.6698 1.6427 -0.0999 -0.0647 0.0031  122 VAL B O   
912  C CB  . VAL A 449 ? 1.9083 1.6214 1.5964 -0.0844 -0.0556 -0.0072 122 VAL B CB  
913  C CG1 . VAL A 449 ? 1.9553 1.6575 1.6411 -0.0824 -0.0604 -0.0077 122 VAL B CG1 
914  C CG2 . VAL A 449 ? 2.0264 1.7409 1.7249 -0.0801 -0.0532 -0.0062 122 VAL B CG2 
915  N N   . ARG A 450 ? 1.8305 1.5527 1.5002 -0.0998 -0.0567 -0.0043 123 ARG B N   
916  C CA  . ARG A 450 ? 1.7156 1.4383 1.3747 -0.1057 -0.0590 -0.0041 123 ARG B CA  
917  C C   . ARG A 450 ? 1.7292 1.4478 1.3904 -0.1136 -0.0629 0.0051  123 ARG B C   
918  O O   . ARG A 450 ? 1.9149 1.6268 1.5710 -0.1175 -0.0674 0.0077  123 ARG B O   
919  C CB  . ARG A 450 ? 1.7652 1.5010 1.4169 -0.1072 -0.0544 -0.0092 123 ARG B CB  
920  C CG  . ARG A 450 ? 2.0662 1.8060 1.7144 -0.1001 -0.0510 -0.0188 123 ARG B CG  
921  C CD  . ARG A 450 ? 2.4857 2.2395 2.1280 -0.1015 -0.0460 -0.0234 123 ARG B CD  
922  N NE  . ARG A 450 ? 2.4072 2.1653 2.0386 -0.1085 -0.0470 -0.0230 123 ARG B NE  
923  C CZ  . ARG A 450 ? 2.3812 2.1522 2.0066 -0.1111 -0.0430 -0.0260 123 ARG B CZ  
924  N NH1 . ARG A 450 ? 2.4597 2.2402 2.0887 -0.1068 -0.0378 -0.0302 123 ARG B NH1 
925  N NH2 . ARG A 450 ? 2.3852 2.1601 2.0008 -0.1183 -0.0444 -0.0246 123 ARG B NH2 
926  N N   . SER A 451 ? 1.7411 1.4639 1.4103 -0.1161 -0.0614 0.0101  124 SER B N   
927  C CA  . SER A 451 ? 1.9384 1.6580 1.6109 -0.1237 -0.0652 0.0189  124 SER B CA  
928  C C   . SER A 451 ? 2.2046 1.9111 1.8824 -0.1234 -0.0703 0.0237  124 SER B C   
929  O O   . SER A 451 ? 2.3773 2.0783 2.0526 -0.1293 -0.0750 0.0290  124 SER B O   
930  C CB  . SER A 451 ? 1.8935 1.6194 1.5753 -0.1254 -0.0628 0.0227  124 SER B CB  
931  O OG  . SER A 451 ? 1.8952 1.6159 1.5882 -0.1204 -0.0623 0.0239  124 SER B OG  
932  N N   . GLN A 452 ? 2.1285 1.8301 1.8137 -0.1166 -0.0695 0.0221  125 GLN B N   
933  C CA  . GLN A 452 ? 1.9522 1.6419 1.6428 -0.1160 -0.0742 0.0267  125 GLN B CA  
934  C C   . GLN A 452 ? 2.0176 1.7002 1.6989 -0.1160 -0.0780 0.0245  125 GLN B C   
935  O O   . GLN A 452 ? 2.2530 1.9277 1.9340 -0.1205 -0.0831 0.0301  125 GLN B O   
936  C CB  . GLN A 452 ? 1.7650 1.4520 1.4653 -0.1090 -0.0724 0.0257  125 GLN B CB  
937  C CG  . GLN A 452 ? 1.8343 1.5258 1.5451 -0.1095 -0.0697 0.0290  125 GLN B CG  
938  C CD  . GLN A 452 ? 2.0620 1.7467 1.7838 -0.1062 -0.0709 0.0324  125 GLN B CD  
939  O OE1 . GLN A 452 ? 2.1070 1.7858 1.8350 -0.1099 -0.0743 0.0390  125 GLN B OE1 
940  N NE2 . GLN A 452 ? 2.0444 1.7299 1.7688 -0.0993 -0.0683 0.0280  125 GLN B NE2 
941  N N   . LEU A 453 ? 2.0277 1.7129 1.7018 -0.1111 -0.0759 0.0164  126 LEU B N   
942  C CA  . LEU A 453 ? 1.9578 1.6352 1.6245 -0.1101 -0.0798 0.0137  126 LEU B CA  
943  C C   . LEU A 453 ? 2.1545 1.8331 1.8099 -0.1171 -0.0822 0.0142  126 LEU B C   
944  O O   . LEU A 453 ? 2.4391 2.1088 2.0904 -0.1193 -0.0873 0.0162  126 LEU B O   
945  C CB  . LEU A 453 ? 1.8105 1.4900 1.4742 -0.1023 -0.0771 0.0045  126 LEU B CB  
946  C CG  . LEU A 453 ? 1.9966 1.6737 1.6706 -0.0953 -0.0758 0.0040  126 LEU B CG  
947  C CD1 . LEU A 453 ? 1.9418 1.6220 1.6128 -0.0882 -0.0732 -0.0051 126 LEU B CD1 
948  C CD2 . LEU A 453 ? 1.9014 1.5665 1.5818 -0.0950 -0.0810 0.0099  126 LEU B CD2 
949  N N   . LYS A 454 ? 1.9678 1.6573 1.6178 -0.1209 -0.0787 0.0126  127 LYS B N   
950  C CA  . LYS A 454 ? 1.9981 1.6910 1.6365 -0.1277 -0.0803 0.0125  127 LYS B CA  
951  C C   . LYS A 454 ? 2.2342 1.9223 1.8625 -0.1253 -0.0824 0.0060  127 LYS B C   
952  O O   . LYS A 454 ? 2.0498 1.7390 1.6772 -0.1180 -0.0797 -0.0020 127 LYS B O   
953  C CB  . LYS A 454 ? 2.0368 1.7248 1.6776 -0.1362 -0.0853 0.0226  127 LYS B CB  
954  C CG  . LYS A 454 ? 1.7734 1.4676 1.4230 -0.1397 -0.0834 0.0286  127 LYS B CG  
955  C CD  . LYS A 454 ? 1.8605 1.5495 1.5138 -0.1480 -0.0887 0.0387  127 LYS B CD  
956  C CE  . LYS A 454 ? 2.0451 1.7405 1.7080 -0.1513 -0.0870 0.0441  127 LYS B CE  
957  N NZ  . LYS A 454 ? 2.1334 1.8237 1.8015 -0.1593 -0.0925 0.0541  127 LYS B NZ  
958  N N   . ASN A 455 ? 2.3196 2.0024 1.9406 -0.1314 -0.0873 0.0091  128 ASN B N   
959  C CA  . ASN A 455 ? 2.4203 2.0983 2.0309 -0.1298 -0.0897 0.0028  128 ASN B CA  
960  C C   . ASN A 455 ? 2.4456 2.1101 2.0614 -0.1248 -0.0942 0.0034  128 ASN B C   
961  O O   . ASN A 455 ? 2.4638 2.1220 2.0717 -0.1247 -0.0977 -0.0001 128 ASN B O   
962  C CB  . ASN A 455 ? 2.3854 2.0640 1.9848 -0.1388 -0.0931 0.0056  128 ASN B CB  
963  C CG  . ASN A 455 ? 2.6832 2.3765 2.2746 -0.1431 -0.0886 0.0027  128 ASN B CG  
964  O OD1 . ASN A 455 ? 2.8251 2.5276 2.4165 -0.1381 -0.0827 -0.0042 128 ASN B OD1 
965  N ND2 . ASN A 455 ? 2.8833 2.5789 2.4677 -0.1524 -0.0913 0.0079  128 ASN B ND2 
966  N N   . ASN A 456 ? 2.6080 2.2680 2.2365 -0.1210 -0.0942 0.0077  129 ASN B N   
967  C CA  . ASN A 456 ? 2.4438 2.0923 2.0779 -0.1157 -0.0979 0.0080  129 ASN B CA  
968  C C   . ASN A 456 ? 2.4328 2.0828 2.0670 -0.1069 -0.0951 -0.0012 129 ASN B C   
969  O O   . ASN A 456 ? 2.4586 2.1000 2.0983 -0.1018 -0.0980 -0.0013 129 ASN B O   
970  C CB  . ASN A 456 ? 2.4543 2.0983 2.1022 -0.1153 -0.0989 0.0164  129 ASN B CB  
971  C CG  . ASN A 456 ? 2.5249 2.1599 2.1747 -0.1217 -0.1050 0.0255  129 ASN B CG  
972  O OD1 . ASN A 456 ? 2.4991 2.1304 2.1396 -0.1265 -0.1089 0.0260  129 ASN B OD1 
973  N ND2 . ASN A 456 ? 2.5888 2.2206 2.2506 -0.1220 -0.1057 0.0328  129 ASN B ND2 
974  N N   . ALA A 457 ? 2.2891 1.9500 1.9177 -0.1050 -0.0898 -0.0089 130 ALA B N   
975  C CA  . ALA A 457 ? 2.2003 1.8634 1.8296 -0.0967 -0.0870 -0.0179 130 ALA B CA  
976  C C   . ALA A 457 ? 2.0169 1.6907 1.6357 -0.0970 -0.0828 -0.0266 130 ALA B C   
977  O O   . ALA A 457 ? 1.8831 1.5640 1.4951 -0.1035 -0.0813 -0.0249 130 ALA B O   
978  C CB  . ALA A 457 ? 2.2035 1.8702 1.8447 -0.0915 -0.0832 -0.0168 130 ALA B CB  
979  N N   . LYS A 458 ? 2.0408 1.7157 1.6586 -0.0899 -0.0812 -0.0358 131 LYS B N   
980  C CA  . LYS A 458 ? 2.0163 1.7018 1.6258 -0.0885 -0.0766 -0.0454 131 LYS B CA  
981  C C   . LYS A 458 ? 2.0624 1.7578 1.6789 -0.0831 -0.0704 -0.0489 131 LYS B C   
982  O O   . LYS A 458 ? 2.1289 1.8203 1.7548 -0.0767 -0.0706 -0.0494 131 LYS B O   
983  C CB  . LYS A 458 ? 1.7928 1.4728 1.3962 -0.0842 -0.0792 -0.0542 131 LYS B CB  
984  C CG  . LYS A 458 ? 1.7075 1.3797 1.3014 -0.0896 -0.0848 -0.0529 131 LYS B CG  
985  C CD  . LYS A 458 ? 1.6089 1.2755 1.1978 -0.0845 -0.0875 -0.0625 131 LYS B CD  
986  C CE  . LYS A 458 ? 1.7234 1.3823 1.3019 -0.0904 -0.0931 -0.0614 131 LYS B CE  
987  N NZ  . LYS A 458 ? 1.8503 1.5028 1.4237 -0.0858 -0.0964 -0.0707 131 LYS B NZ  
988  N N   . GLU A 459 ? 2.0829 1.7913 1.6948 -0.0859 -0.0651 -0.0512 132 GLU B N   
989  C CA  . GLU A 459 ? 2.0688 1.7877 1.6857 -0.0810 -0.0590 -0.0558 132 GLU B CA  
990  C C   . GLU A 459 ? 2.1223 1.8431 1.7361 -0.0742 -0.0575 -0.0672 132 GLU B C   
991  O O   . GLU A 459 ? 2.1911 1.9176 1.7947 -0.0760 -0.0561 -0.0735 132 GLU B O   
992  C CB  . GLU A 459 ? 1.8545 1.5867 1.4673 -0.0866 -0.0542 -0.0542 132 GLU B CB  
993  C CG  . GLU A 459 ? 2.1723 1.9042 1.7899 -0.0928 -0.0552 -0.0435 132 GLU B CG  
994  C CD  . GLU A 459 ? 2.5326 2.2778 2.1456 -0.0986 -0.0511 -0.0422 132 GLU B CD  
995  O OE1 . GLU A 459 ? 2.4873 2.2419 2.0921 -0.0986 -0.0477 -0.0494 132 GLU B OE1 
996  O OE2 . GLU A 459 ? 2.7014 2.4482 2.3196 -0.1033 -0.0512 -0.0341 132 GLU B OE2 
997  N N   . ILE A 460 ? 2.0164 1.7330 1.6392 -0.0665 -0.0579 -0.0699 133 ILE B N   
998  C CA  . ILE A 460 ? 1.9862 1.7032 1.6082 -0.0596 -0.0574 -0.0804 133 ILE B CA  
999  C C   . ILE A 460 ? 2.1529 1.8741 1.7856 -0.0525 -0.0541 -0.0829 133 ILE B C   
1000 O O   . ILE A 460 ? 2.3929 2.1119 2.0346 -0.0519 -0.0543 -0.0761 133 ILE B O   
1001 C CB  . ILE A 460 ? 2.0650 1.7678 1.6857 -0.0577 -0.0643 -0.0816 133 ILE B CB  
1002 C CG1 . ILE A 460 ? 2.2789 1.9796 1.8871 -0.0646 -0.0668 -0.0813 133 ILE B CG1 
1003 C CG2 . ILE A 460 ? 2.0563 1.7577 1.6794 -0.0496 -0.0646 -0.0918 133 ILE B CG2 
1004 C CD1 . ILE A 460 ? 2.3142 2.0006 1.9205 -0.0646 -0.0741 -0.0803 133 ILE B CD1 
1005 N N   . GLY A 461 ? 1.9618 1.6899 1.5933 -0.0474 -0.0508 -0.0929 134 GLY B N   
1006 C CA  . GLY A 461 ? 1.9591 1.6920 1.6004 -0.0406 -0.0477 -0.0962 134 GLY B CA  
1007 C C   . GLY A 461 ? 1.9747 1.7202 1.6180 -0.0428 -0.0416 -0.0935 134 GLY B C   
1008 O O   . GLY A 461 ? 1.8900 1.6439 1.5256 -0.0485 -0.0385 -0.0928 134 GLY B O   
1009 N N   . ASN A 462 ? 1.8643 1.6111 1.5181 -0.0386 -0.0402 -0.0916 135 ASN B N   
1010 C CA  . ASN A 462 ? 1.8312 1.5885 1.4885 -0.0403 -0.0351 -0.0881 135 ASN B CA  
1011 C C   . ASN A 462 ? 1.8902 1.6411 1.5528 -0.0438 -0.0375 -0.0775 135 ASN B C   
1012 O O   . ASN A 462 ? 1.5350 1.2819 1.2069 -0.0402 -0.0387 -0.0746 135 ASN B O   
1013 C CB  . ASN A 462 ? 1.7358 1.4998 1.4010 -0.0335 -0.0317 -0.0935 135 ASN B CB  
1014 C CG  . ASN A 462 ? 1.9495 1.7224 1.6098 -0.0306 -0.0281 -0.1040 135 ASN B CG  
1015 O OD1 . ASN A 462 ? 2.3547 2.1327 2.0050 -0.0350 -0.0264 -0.1064 135 ASN B OD1 
1016 N ND2 . ASN A 462 ? 1.8068 1.5822 1.4743 -0.0235 -0.0268 -0.1101 135 ASN B ND2 
1017 N N   . GLY A 463 ? 2.1298 1.8801 1.7866 -0.0511 -0.0384 -0.0717 136 GLY B N   
1018 C CA  . GLY A 463 ? 1.9942 1.7385 1.6557 -0.0549 -0.0408 -0.0619 136 GLY B CA  
1019 C C   . GLY A 463 ? 1.9910 1.7215 1.6567 -0.0528 -0.0467 -0.0588 136 GLY B C   
1020 O O   . GLY A 463 ? 1.9672 1.6938 1.6418 -0.0507 -0.0477 -0.0542 136 GLY B O   
1021 N N   . CYS A 464 ? 2.1245 1.8477 1.7838 -0.0534 -0.0507 -0.0613 137 CYS B N   
1022 C CA  . CYS A 464 ? 1.9574 1.6672 1.6200 -0.0524 -0.0568 -0.0574 137 CYS B CA  
1023 C C   . CYS A 464 ? 1.8891 1.5930 1.5443 -0.0594 -0.0605 -0.0525 137 CYS B C   
1024 O O   . CYS A 464 ? 2.0343 1.7426 1.6798 -0.0631 -0.0595 -0.0558 137 CYS B O   
1025 C CB  . CYS A 464 ? 1.8571 1.5615 1.5204 -0.0458 -0.0595 -0.0647 137 CYS B CB  
1026 S SG  . CYS A 464 ? 2.0050 1.7130 1.6800 -0.0374 -0.0573 -0.0682 137 CYS B SG  
1027 N N   . PHE A 465 ? 1.7137 1.4085 1.3739 -0.0615 -0.0645 -0.0444 138 PHE B N   
1028 C CA  . PHE A 465 ? 2.0458 1.7339 1.7009 -0.0681 -0.0687 -0.0386 138 PHE B CA  
1029 C C   . PHE A 465 ? 2.4658 2.1411 2.1213 -0.0658 -0.0750 -0.0384 138 PHE B C   
1030 O O   . PHE A 465 ? 2.3256 1.9942 1.9900 -0.0630 -0.0775 -0.0341 138 PHE B O   
1031 C CB  . PHE A 465 ? 1.9562 1.6438 1.6174 -0.0728 -0.0686 -0.0289 138 PHE B CB  
1032 C CG  . PHE A 465 ? 1.9024 1.6020 1.5637 -0.0757 -0.0631 -0.0282 138 PHE B CG  
1033 C CD1 . PHE A 465 ? 1.8855 1.5920 1.5539 -0.0714 -0.0587 -0.0299 138 PHE B CD1 
1034 C CD2 . PHE A 465 ? 2.0857 1.7895 1.7403 -0.0830 -0.0628 -0.0254 138 PHE B CD2 
1035 C CE1 . PHE A 465 ? 2.0478 1.7650 1.7165 -0.0742 -0.0540 -0.0290 138 PHE B CE1 
1036 C CE2 . PHE A 465 ? 2.0303 1.7450 1.6854 -0.0859 -0.0582 -0.0243 138 PHE B CE2 
1037 C CZ  . PHE A 465 ? 1.8973 1.6186 1.5595 -0.0814 -0.0538 -0.0262 138 PHE B CZ  
1038 N N   . GLU A 466 ? 2.5389 2.2108 2.1850 -0.0671 -0.0776 -0.0429 139 GLU B N   
1039 C CA  . GLU A 466 ? 2.4398 2.0989 2.0858 -0.0656 -0.0843 -0.0424 139 GLU B CA  
1040 C C   . GLU A 466 ? 2.5209 2.1728 2.1649 -0.0728 -0.0886 -0.0334 139 GLU B C   
1041 O O   . GLU A 466 ? 2.3659 2.0199 2.0007 -0.0788 -0.0888 -0.0331 139 GLU B O   
1042 C CB  . GLU A 466 ? 2.3371 1.9951 1.9746 -0.0632 -0.0857 -0.0520 139 GLU B CB  
1043 C CG  . GLU A 466 ? 2.4012 2.0647 2.0419 -0.0555 -0.0824 -0.0613 139 GLU B CG  
1044 C CD  . GLU A 466 ? 2.3656 2.0277 1.9980 -0.0533 -0.0839 -0.0712 139 GLU B CD  
1045 O OE1 . GLU A 466 ? 2.7200 2.3784 2.3429 -0.0582 -0.0868 -0.0711 139 GLU B OE1 
1046 O OE2 . GLU A 466 ? 2.1708 1.8358 1.8065 -0.0466 -0.0824 -0.0792 139 GLU B OE2 
1047 N N   . PHE A 467 ? 2.5394 2.1834 2.1925 -0.0722 -0.0920 -0.0260 140 PHE B N   
1048 C CA  . PHE A 467 ? 2.6074 2.2439 2.2605 -0.0785 -0.0963 -0.0170 140 PHE B CA  
1049 C C   . PHE A 467 ? 2.5552 2.1821 2.2006 -0.0801 -0.1024 -0.0185 140 PHE B C   
1050 O O   . PHE A 467 ? 2.5967 2.2170 2.2435 -0.0750 -0.1057 -0.0224 140 PHE B O   
1051 C CB  . PHE A 467 ? 2.7085 2.3395 2.3739 -0.0767 -0.0981 -0.0094 140 PHE B CB  
1052 C CG  . PHE A 467 ? 2.5453 2.1850 2.2185 -0.0757 -0.0926 -0.0073 140 PHE B CG  
1053 C CD1 . PHE A 467 ? 2.6071 2.2505 2.2821 -0.0814 -0.0909 -0.0010 140 PHE B CD1 
1054 C CD2 . PHE A 467 ? 2.2968 1.9409 1.9758 -0.0691 -0.0895 -0.0115 140 PHE B CD2 
1055 C CE1 . PHE A 467 ? 2.1953 1.8462 1.8774 -0.0804 -0.0860 0.0007  140 PHE B CE1 
1056 C CE2 . PHE A 467 ? 2.1759 1.8278 1.8617 -0.0682 -0.0846 -0.0097 140 PHE B CE2 
1057 C CZ  . PHE A 467 ? 2.1726 1.8279 1.8598 -0.0738 -0.0828 -0.0038 140 PHE B CZ  
1058 N N   . TYR A 468 ? 2.4122 2.0382 2.0496 -0.0875 -0.1043 -0.0153 141 TYR B N   
1059 C CA  . TYR A 468 ? 2.4382 2.0532 2.0700 -0.0901 -0.1111 -0.0139 141 TYR B CA  
1060 C C   . TYR A 468 ? 2.4577 2.0619 2.0994 -0.0896 -0.1163 -0.0054 141 TYR B C   
1061 O O   . TYR A 468 ? 2.5558 2.1510 2.1994 -0.0856 -0.1209 -0.0068 141 TYR B O   
1062 C CB  . TYR A 468 ? 2.5507 2.1673 2.1727 -0.0989 -0.1123 -0.0108 141 TYR B CB  
1063 C CG  . TYR A 468 ? 2.3739 2.0026 1.9862 -0.1012 -0.1070 -0.0172 141 TYR B CG  
1064 C CD1 . TYR A 468 ? 2.0703 1.7021 1.6741 -0.0978 -0.1057 -0.0279 141 TYR B CD1 
1065 C CD2 . TYR A 468 ? 2.3972 2.0346 2.0093 -0.1070 -0.1036 -0.0124 141 TYR B CD2 
1066 C CE1 . TYR A 468 ? 1.9832 1.6269 1.5781 -0.1001 -0.1007 -0.0336 141 TYR B CE1 
1067 C CE2 . TYR A 468 ? 2.2949 1.9440 1.8983 -0.1095 -0.0989 -0.0177 141 TYR B CE2 
1068 C CZ  . TYR A 468 ? 2.2150 1.8676 1.8096 -0.1061 -0.0973 -0.0282 141 TYR B CZ  
1069 O OH  . TYR A 468 ? 2.2515 1.9167 1.8373 -0.1088 -0.0924 -0.0334 141 TYR B OH  
1070 N N   . HIS A 469 ? 2.4070 2.0118 2.0553 -0.0937 -0.1157 0.0035  142 HIS B N   
1071 C CA  . HIS A 469 ? 2.1514 1.7482 1.8107 -0.0927 -0.1192 0.0116  142 HIS B CA  
1072 C C   . HIS A 469 ? 2.1628 1.7612 1.8311 -0.0848 -0.1170 0.0087  142 HIS B C   
1073 O O   . HIS A 469 ? 2.3189 1.9245 1.9855 -0.0803 -0.1127 0.0010  142 HIS B O   
1074 C CB  . HIS A 469 ? 2.0967 1.6958 1.7619 -0.0984 -0.1180 0.0205  142 HIS B CB  
1075 C CG  . HIS A 469 ? 2.2855 1.8956 1.9564 -0.0966 -0.1112 0.0196  142 HIS B CG  
1076 N ND1 . HIS A 469 ? 2.5313 2.1421 2.2138 -0.0926 -0.1093 0.0225  142 HIS B ND1 
1077 C CD2 . HIS A 469 ? 2.4426 2.0633 2.1089 -0.0987 -0.1060 0.0164  142 HIS B CD2 
1078 C CE1 . HIS A 469 ? 2.7382 2.3593 2.4231 -0.0921 -0.1033 0.0208  142 HIS B CE1 
1079 N NE2 . HIS A 469 ? 2.8463 2.4735 2.5217 -0.0957 -0.1012 0.0173  142 HIS B NE2 
1080 N N   . LYS A 470 ? 2.2301 1.8218 1.9082 -0.0833 -0.1201 0.0153  143 LYS B N   
1081 C CA  . LYS A 470 ? 2.2990 1.8916 1.9861 -0.0765 -0.1188 0.0140  143 LYS B CA  
1082 C C   . LYS A 470 ? 2.6944 2.2926 2.3914 -0.0771 -0.1147 0.0198  143 LYS B C   
1083 O O   . LYS A 470 ? 2.6316 2.2248 2.3354 -0.0796 -0.1173 0.0279  143 LYS B O   
1084 C CB  . LYS A 470 ? 2.2485 1.8299 1.9394 -0.0739 -0.1256 0.0165  143 LYS B CB  
1085 C CG  . LYS A 470 ? 2.2734 1.8496 1.9554 -0.0722 -0.1294 0.0093  143 LYS B CG  
1086 C CD  . LYS A 470 ? 2.1689 1.7336 1.8552 -0.0699 -0.1367 0.0123  143 LYS B CD  
1087 C CE  . LYS A 470 ? 2.4161 1.9754 2.0939 -0.0679 -0.1407 0.0045  143 LYS B CE  
1088 N NZ  . LYS A 470 ? 2.4173 1.9667 2.1005 -0.0655 -0.1481 0.0078  143 LYS B NZ  
1089 N N   . CYS A 471 ? 2.8813 2.4899 2.5789 -0.0749 -0.1084 0.0154  144 CYS B N   
1090 C CA  . CYS A 471 ? 2.8021 2.4171 2.5079 -0.0757 -0.1040 0.0198  144 CYS B CA  
1091 C C   . CYS A 471 ? 2.5430 2.1567 2.2590 -0.0704 -0.1042 0.0216  144 CYS B C   
1092 O O   . CYS A 471 ? 2.5442 2.1623 2.2615 -0.0651 -0.1018 0.0163  144 CYS B O   
1093 C CB  . CYS A 471 ? 2.8357 2.4622 2.5377 -0.0757 -0.0975 0.0144  144 CYS B CB  
1094 S SG  . CYS A 471 ? 3.5102 3.1453 3.2210 -0.0773 -0.0920 0.0188  144 CYS B SG  
1095 N N   . ASP A 472 ? 2.5162 2.1237 2.2395 -0.0721 -0.1075 0.0295  145 ASP B N   
1096 C CA  . ASP A 472 ? 2.2987 1.9116 2.0346 -0.0669 -0.1071 0.0318  145 ASP B CA  
1097 C C   . ASP A 472 ? 2.3334 1.9505 2.0725 -0.0653 -0.1017 0.0309  145 ASP B C   
1098 O O   . ASP A 472 ? 2.5557 2.1797 2.2911 -0.0669 -0.0971 0.0277  145 ASP B O   
1099 C CB  . ASP A 472 ? 2.0678 1.6919 1.8183 -0.0671 -0.1078 0.0383  145 ASP B CB  
1100 C CG  . ASP A 472 ? 2.3312 1.9521 2.0807 -0.0676 -0.1134 0.0393  145 ASP B CG  
1101 O OD1 . ASP A 472 ? 2.5343 2.1444 2.2734 -0.0665 -0.1171 0.0351  145 ASP B OD1 
1102 O OD2 . ASP A 472 ? 2.2741 1.9030 2.0334 -0.0689 -0.1142 0.0440  145 ASP B OD2 
1103 N N   . ASN A 473 ? 2.0579 1.6817 1.8083 -0.0609 -0.1006 0.0327  146 ASN B N   
1104 C CA  . ASN A 473 ? 2.0783 1.7070 1.8328 -0.0597 -0.0956 0.0325  146 ASN B CA  
1105 C C   . ASN A 473 ? 2.3240 1.9592 2.0814 -0.0638 -0.0916 0.0353  146 ASN B C   
1106 O O   . ASN A 473 ? 2.4916 2.1296 2.2438 -0.0652 -0.0878 0.0319  146 ASN B O   
1107 C CB  . ASN A 473 ? 2.1020 1.7388 1.8697 -0.0556 -0.0952 0.0356  146 ASN B CB  
1108 C CG  . ASN A 473 ? 2.1662 1.7976 1.9321 -0.0512 -0.0983 0.0327  146 ASN B CG  
1109 O OD1 . ASN A 473 ? 1.7546 1.3809 1.5115 -0.0498 -0.0985 0.0268  146 ASN B OD1 
1110 N ND2 . ASN A 473 ? 2.4619 2.0996 2.2388 -0.0484 -0.0998 0.0360  146 ASN B ND2 
1111 N N   . THR A 474 ? 2.4037 2.0486 2.1735 -0.0646 -0.0915 0.0402  147 THR B N   
1112 C CA  . THR A 474 ? 2.3803 2.0323 2.1556 -0.0681 -0.0886 0.0430  147 THR B CA  
1113 C C   . THR A 474 ? 2.5701 2.2158 2.3329 -0.0731 -0.0888 0.0412  147 THR B C   
1114 O O   . THR A 474 ? 2.6553 2.3035 2.4176 -0.0758 -0.0853 0.0413  147 THR B O   
1115 C CB  . THR A 474 ? 2.3410 2.0012 2.1289 -0.0684 -0.0901 0.0476  147 THR B CB  
1116 O OG1 . THR A 474 ? 2.7307 2.3863 2.5123 -0.0713 -0.0943 0.0480  147 THR B OG1 
1117 C CG2 . THR A 474 ? 2.0134 1.6775 1.8107 -0.0640 -0.0910 0.0489  147 THR B CG2 
1118 N N   . CYS A 475 ? 2.4331 2.0700 2.1852 -0.0745 -0.0928 0.0394  148 CYS B N   
1119 C CA  . CYS A 475 ? 2.4230 2.0527 2.1610 -0.0797 -0.0931 0.0371  148 CYS B CA  
1120 C C   . CYS A 475 ? 2.4656 2.1053 2.2009 -0.0764 -0.0874 0.0301  148 CYS B C   
1121 O O   . CYS A 475 ? 2.4677 2.1140 2.2004 -0.0794 -0.0840 0.0289  148 CYS B O   
1122 C CB  . CYS A 475 ? 2.4802 2.1027 2.2091 -0.0806 -0.0980 0.0352  148 CYS B CB  
1123 S SG  . CYS A 475 ? 3.0766 2.7038 2.7929 -0.0848 -0.0964 0.0303  148 CYS B SG  
1124 N N   . MET A 476 ? 2.4371 2.0780 2.1730 -0.0705 -0.0866 0.0257  149 MET B N   
1125 C CA  . MET A 476 ? 2.2378 1.8880 1.9712 -0.0674 -0.0816 0.0189  149 MET B CA  
1126 C C   . MET A 476 ? 2.1689 1.8269 1.9090 -0.0680 -0.0766 0.0207  149 MET B C   
1127 O O   . MET A 476 ? 2.1852 1.8511 1.9223 -0.0692 -0.0725 0.0175  149 MET B O   
1128 C CB  . MET A 476 ? 2.4387 2.0881 2.1733 -0.0610 -0.0823 0.0147  149 MET B CB  
1129 C CG  . MET A 476 ? 2.6178 2.2598 2.3458 -0.0597 -0.0873 0.0116  149 MET B CG  
1130 S SD  . MET A 476 ? 2.9086 2.5526 2.6236 -0.0617 -0.0867 0.0047  149 MET B SD  
1131 C CE  . MET A 476 ? 2.0367 1.6919 1.7509 -0.0567 -0.0808 -0.0037 149 MET B CE  
1132 N N   . GLU A 477 ? 2.1654 1.8214 1.9146 -0.0675 -0.0771 0.0257  150 GLU B N   
1133 C CA  . GLU A 477 ? 1.9493 1.6114 1.7056 -0.0687 -0.0731 0.0280  150 GLU B CA  
1134 C C   . GLU A 477 ? 2.0657 1.7293 1.8204 -0.0746 -0.0724 0.0304  150 GLU B C   
1135 O O   . GLU A 477 ? 2.2396 1.9109 1.9948 -0.0756 -0.0683 0.0286  150 GLU B O   
1136 C CB  . GLU A 477 ? 1.9711 1.6296 1.7370 -0.0678 -0.0745 0.0335  150 GLU B CB  
1137 C CG  . GLU A 477 ? 2.3370 1.9941 2.1052 -0.0624 -0.0758 0.0322  150 GLU B CG  
1138 C CD  . GLU A 477 ? 2.3576 2.0103 2.1331 -0.0622 -0.0797 0.0379  150 GLU B CD  
1139 O OE1 . GLU A 477 ? 2.1523 1.8132 1.9377 -0.0638 -0.0785 0.0416  150 GLU B OE1 
1140 O OE2 . GLU A 477 ? 2.0225 1.6725 1.7982 -0.0588 -0.0828 0.0374  150 GLU B OE2 
1141 N N   . SER A 478 ? 2.0236 1.6799 1.7764 -0.0788 -0.0768 0.0347  151 SER B N   
1142 C CA  . SER A 478 ? 2.1771 1.8343 1.9292 -0.0850 -0.0770 0.0379  151 SER B CA  
1143 C C   . SER A 478 ? 2.1963 1.8607 1.9399 -0.0865 -0.0742 0.0330  151 SER B C   
1144 O O   . SER A 478 ? 2.2947 1.9649 2.0401 -0.0898 -0.0716 0.0340  151 SER B O   
1145 C CB  . SER A 478 ? 2.2928 1.9417 2.0434 -0.0889 -0.0827 0.0428  151 SER B CB  
1146 O OG  . SER A 478 ? 2.3417 1.9861 2.0816 -0.0886 -0.0854 0.0394  151 SER B OG  
1147 N N   . VAL A 479 ? 2.0135 1.6778 1.7482 -0.0841 -0.0746 0.0276  152 VAL B N   
1148 C CA  . VAL A 479 ? 1.8871 1.5596 1.6140 -0.0848 -0.0713 0.0221  152 VAL B CA  
1149 C C   . VAL A 479 ? 1.7260 1.4078 1.4576 -0.0818 -0.0658 0.0193  152 VAL B C   
1150 O O   . VAL A 479 ? 1.4492 1.1382 1.1798 -0.0848 -0.0628 0.0189  152 VAL B O   
1151 C CB  . VAL A 479 ? 1.6583 1.3292 1.3759 -0.0818 -0.0725 0.0160  152 VAL B CB  
1152 C CG1 . VAL A 479 ? 1.3604 1.0401 1.0696 -0.0834 -0.0691 0.0108  152 VAL B CG1 
1153 C CG2 . VAL A 479 ? 2.0618 1.7227 1.7754 -0.0845 -0.0784 0.0189  152 VAL B CG2 
1154 N N   . LYS A 480 ? 1.8288 1.5105 1.5657 -0.0762 -0.0646 0.0176  153 LYS B N   
1155 C CA  . LYS A 480 ? 1.8825 1.5727 1.6237 -0.0734 -0.0596 0.0149  153 LYS B CA  
1156 C C   . LYS A 480 ? 2.0693 1.7622 1.8180 -0.0769 -0.0580 0.0195  153 LYS B C   
1157 O O   . LYS A 480 ? 2.1268 1.8275 1.8754 -0.0782 -0.0544 0.0179  153 LYS B O   
1158 C CB  . LYS A 480 ? 1.9510 1.6401 1.6969 -0.0673 -0.0594 0.0132  153 LYS B CB  
1159 C CG  . LYS A 480 ? 2.0631 1.7609 1.8130 -0.0642 -0.0546 0.0103  153 LYS B CG  
1160 C CD  . LYS A 480 ? 2.2431 1.9399 1.9972 -0.0587 -0.0549 0.0090  153 LYS B CD  
1161 C CE  . LYS A 480 ? 2.0684 1.7739 1.8264 -0.0561 -0.0503 0.0064  153 LYS B CE  
1162 N NZ  . LYS A 480 ? 2.4518 2.1569 2.2141 -0.0511 -0.0508 0.0056  153 LYS B NZ  
1163 N N   . ASN A 481 ? 2.0682 1.7548 1.8238 -0.0784 -0.0606 0.0251  154 ASN B N   
1164 C CA  . ASN A 481 ? 1.9753 1.6639 1.7390 -0.0815 -0.0594 0.0292  154 ASN B CA  
1165 C C   . ASN A 481 ? 1.9175 1.6072 1.6788 -0.0879 -0.0603 0.0318  154 ASN B C   
1166 O O   . ASN A 481 ? 2.1375 1.8285 1.9062 -0.0909 -0.0598 0.0353  154 ASN B O   
1167 C CB  . ASN A 481 ? 1.9232 1.6048 1.6953 -0.0814 -0.0620 0.0345  154 ASN B CB  
1168 C CG  . ASN A 481 ? 2.1836 1.8635 1.9578 -0.0758 -0.0621 0.0330  154 ASN B CG  
1169 O OD1 . ASN A 481 ? 2.3427 2.0152 2.1181 -0.0753 -0.0659 0.0361  154 ASN B OD1 
1170 N ND2 . ASN A 481 ? 2.3077 1.9944 2.0825 -0.0718 -0.0582 0.0287  154 ASN B ND2 
1171 N N   . GLY A 482 ? 1.9663 1.6558 1.7179 -0.0901 -0.0618 0.0301  155 GLY B N   
1172 C CA  . GLY A 482 ? 1.9626 1.6530 1.7115 -0.0968 -0.0634 0.0333  155 GLY B CA  
1173 C C   . GLY A 482 ? 2.0075 1.6893 1.7600 -0.1013 -0.0684 0.0401  155 GLY B C   
1174 O O   . GLY A 482 ? 2.1696 1.8518 1.9215 -0.1074 -0.0702 0.0439  155 GLY B O   
1175 N N   . THR A 483 ? 1.9874 1.6615 1.7439 -0.0986 -0.0708 0.0421  156 THR B N   
1176 C CA  . THR A 483 ? 2.1782 1.8457 1.9401 -0.1019 -0.0754 0.0486  156 THR B CA  
1177 C C   . THR A 483 ? 2.1685 1.8299 1.9222 -0.1030 -0.0799 0.0489  156 THR B C   
1178 O O   . THR A 483 ? 2.2147 1.8804 1.9778 -0.1016 -0.0825 0.0518  156 THR B O   
1179 C CB  . THR A 483 ? 2.2349 1.9088 2.0124 -0.0959 -0.0740 0.0494  156 THR B CB  
1180 O OG1 . THR A 483 ? 2.1451 1.8135 1.9183 -0.0912 -0.0741 0.0466  156 THR B OG1 
1181 C CG2 . THR A 483 ? 1.9103 1.5901 1.6963 -0.0953 -0.0699 0.0491  156 THR B CG2 
1182 N N   . TYR A 484 ? 2.0986 1.7599 1.8399 -0.1027 -0.0794 0.0439  157 TYR B N   
1183 C CA  . TYR A 484 ? 2.1715 1.8262 1.9040 -0.1040 -0.0837 0.0437  157 TYR B CA  
1184 C C   . TYR A 484 ? 2.3357 1.9873 2.0659 -0.1119 -0.0877 0.0493  157 TYR B C   
1185 O O   . TYR A 484 ? 2.2480 1.9054 1.9787 -0.1164 -0.0863 0.0510  157 TYR B O   
1186 C CB  . TYR A 484 ? 2.1072 1.7668 1.8287 -0.1012 -0.0815 0.0358  157 TYR B CB  
1187 C CG  . TYR A 484 ? 2.2543 1.9081 1.9656 -0.1035 -0.0858 0.0348  157 TYR B CG  
1188 C CD1 . TYR A 484 ? 2.0563 1.7010 1.7673 -0.1006 -0.0898 0.0351  157 TYR B CD1 
1189 C CD2 . TYR A 484 ? 2.4600 2.1178 2.1618 -0.1087 -0.0859 0.0338  157 TYR B CD2 
1190 C CE1 . TYR A 484 ? 2.2326 1.8716 1.9341 -0.1027 -0.0940 0.0340  157 TYR B CE1 
1191 C CE2 . TYR A 484 ? 2.4330 2.0859 2.1250 -0.1110 -0.0898 0.0325  157 TYR B CE2 
1192 C CZ  . TYR A 484 ? 2.3523 1.9954 2.0441 -0.1079 -0.0938 0.0325  157 TYR B CZ  
1193 O OH  . TYR A 484 ? 2.3614 1.9993 2.0432 -0.1102 -0.0979 0.0309  157 TYR B OH  
1194 N N   . ASP A 485 ? 2.3307 1.9778 2.0607 -0.1123 -0.0924 0.0517  158 ASP B N   
1195 C CA  . ASP A 485 ? 2.4538 2.1048 2.1855 -0.1174 -0.0958 0.0559  158 ASP B CA  
1196 C C   . ASP A 485 ? 2.4739 2.1142 2.1891 -0.1212 -0.1000 0.0546  158 ASP B C   
1197 O O   . ASP A 485 ? 2.5185 2.1536 2.2326 -0.1173 -0.1025 0.0531  158 ASP B O   
1198 C CB  . ASP A 485 ? 2.5763 2.2372 2.3273 -0.1136 -0.0969 0.0595  158 ASP B CB  
1199 C CG  . ASP A 485 ? 2.5307 2.1949 2.2838 -0.1184 -0.1009 0.0636  158 ASP B CG  
1200 O OD1 . ASP A 485 ? 2.6172 2.2875 2.3743 -0.1225 -0.1005 0.0662  158 ASP B OD1 
1201 O OD2 . ASP A 485 ? 2.3852 2.0461 2.1363 -0.1179 -0.1048 0.0642  158 ASP B OD2 
1202 N N   . TYR A 486 ? 2.4103 2.0503 2.1141 -0.1281 -0.1005 0.0548  159 TYR B N   
1203 C CA  . TYR A 486 ? 2.4265 2.0644 2.1168 -0.1302 -0.1031 0.0514  159 TYR B CA  
1204 C C   . TYR A 486 ? 2.4868 2.1141 2.1764 -0.1336 -0.1099 0.0569  159 TYR B C   
1205 O O   . TYR A 486 ? 2.5771 2.1981 2.2594 -0.1313 -0.1125 0.0534  159 TYR B O   
1206 C CB  . TYR A 486 ? 2.4233 2.0705 2.1052 -0.1359 -0.1012 0.0502  159 TYR B CB  
1207 C CG  . TYR A 486 ? 2.4726 2.1206 2.1395 -0.1380 -0.1026 0.0453  159 TYR B CG  
1208 C CD1 . TYR A 486 ? 2.4165 2.0581 2.0774 -0.1445 -0.1084 0.0498  159 TYR B CD1 
1209 C CD2 . TYR A 486 ? 2.5741 2.2297 2.2330 -0.1337 -0.0980 0.0362  159 TYR B CD2 
1210 C CE1 . TYR A 486 ? 2.4946 2.1373 2.1413 -0.1466 -0.1095 0.0450  159 TYR B CE1 
1211 C CE2 . TYR A 486 ? 2.4972 2.1541 2.1425 -0.1356 -0.0990 0.0311  159 TYR B CE2 
1212 C CZ  . TYR A 486 ? 2.4668 2.1173 2.1057 -0.1420 -0.1046 0.0353  159 TYR B CZ  
1213 O OH  . TYR A 486 ? 2.7736 2.4258 2.3986 -0.1440 -0.1055 0.0298  159 TYR B OH  
1214 N N   . PRO A 487 ? 2.3893 2.0279 2.0932 -0.1346 -0.1114 0.0621  160 PRO B N   
1215 C CA  . PRO A 487 ? 2.4436 2.0822 2.1493 -0.1360 -0.1168 0.0649  160 PRO B CA  
1216 C C   . PRO A 487 ? 2.4113 2.0465 2.1217 -0.1295 -0.1188 0.0633  160 PRO B C   
1217 O O   . PRO A 487 ? 2.2273 1.8553 1.9287 -0.1316 -0.1234 0.0631  160 PRO B O   
1218 C CB  . PRO A 487 ? 2.5441 2.1965 2.2679 -0.1366 -0.1167 0.0699  160 PRO B CB  
1219 C CG  . PRO A 487 ? 2.2961 1.9522 2.0178 -0.1404 -0.1132 0.0702  160 PRO B CG  
1220 C CD  . PRO A 487 ? 2.1195 1.7699 1.8358 -0.1362 -0.1089 0.0655  160 PRO B CD  
1221 N N   . LYS A 488 ? 2.3525 1.9931 2.0771 -0.1220 -0.1157 0.0625  161 LYS B N   
1222 C CA  . LYS A 488 ? 2.1077 1.7474 1.8389 -0.1161 -0.1176 0.0619  161 LYS B CA  
1223 C C   . LYS A 488 ? 2.2458 1.8714 1.9598 -0.1163 -0.1209 0.0578  161 LYS B C   
1224 O O   . LYS A 488 ? 2.2950 1.9170 2.0076 -0.1161 -0.1254 0.0585  161 LYS B O   
1225 C CB  . LYS A 488 ? 1.8835 1.5299 1.6292 -0.1089 -0.1132 0.0610  161 LYS B CB  
1226 C CG  . LYS A 488 ? 1.8823 1.5420 1.6469 -0.1075 -0.1102 0.0645  161 LYS B CG  
1227 C CD  . LYS A 488 ? 2.0037 1.6681 1.7797 -0.1009 -0.1059 0.0631  161 LYS B CD  
1228 C CE  . LYS A 488 ? 1.8742 1.5505 1.6685 -0.0994 -0.1025 0.0661  161 LYS B CE  
1229 N NZ  . LYS A 488 ? 1.6341 1.3143 1.4378 -0.0936 -0.0984 0.0647  161 LYS B NZ  
1230 N N   . TYR A 489 ? 2.3304 1.9473 2.0314 -0.1166 -0.1186 0.0533  162 TYR B N   
1231 C CA  . TYR A 489 ? 2.4450 2.0473 2.1297 -0.1164 -0.1211 0.0479  162 TYR B CA  
1232 C C   . TYR A 489 ? 2.3186 1.9178 1.9866 -0.1231 -0.1226 0.0452  162 TYR B C   
1233 O O   . TYR A 489 ? 2.1477 1.7470 1.8065 -0.1201 -0.1225 0.0375  162 TYR B O   
1234 C CB  . TYR A 489 ? 2.4281 2.0314 2.1121 -0.1105 -0.1163 0.0415  162 TYR B CB  
1235 C CG  . TYR A 489 ? 2.3338 1.9417 2.0334 -0.1045 -0.1139 0.0439  162 TYR B CG  
1236 C CD1 . TYR A 489 ? 2.3673 1.9779 2.0772 -0.0988 -0.1162 0.0449  162 TYR B CD1 
1237 C CD2 . TYR A 489 ? 2.3316 1.9465 2.0375 -0.1038 -0.1087 0.0444  162 TYR B CD2 
1238 C CE1 . TYR A 489 ? 2.4481 2.0681 2.1738 -0.0930 -0.1132 0.0462  162 TYR B CE1 
1239 C CE2 . TYR A 489 ? 2.4196 2.0432 2.1410 -0.0977 -0.1057 0.0455  162 TYR B CE2 
1240 C CZ  . TYR A 489 ? 2.3830 2.0091 2.1139 -0.0925 -0.1079 0.0464  162 TYR B CZ  
1241 O OH  . TYR A 489 ? 2.2205 1.8554 1.9661 -0.0873 -0.1049 0.0475  162 TYR B OH  
1242 N N   . SER A 490 ? 2.3110 1.9130 1.9776 -0.1308 -0.1233 0.0505  163 SER B N   
1243 C CA  . SER A 490 ? 2.4397 2.0471 2.0931 -0.1360 -0.1229 0.0471  163 SER B CA  
1244 C C   . SER A 490 ? 2.4267 2.0261 2.0694 -0.1377 -0.1284 0.0451  163 SER B C   
1245 O O   . SER A 490 ? 2.2718 1.8745 1.9035 -0.1359 -0.1269 0.0366  163 SER B O   
1246 C CB  . SER A 490 ? 2.3820 1.9933 2.0374 -0.1444 -0.1235 0.0546  163 SER B CB  
1247 O OG  . SER A 490 ? 2.4226 2.0328 2.0868 -0.1466 -0.1287 0.0617  163 SER B OG  
1248 N N   . GLU A 491 ? 2.5861 2.1748 2.2321 -0.1412 -0.1349 0.0526  164 GLU B N   
1249 C CA  . GLU A 491 ? 2.5667 2.1475 2.2023 -0.1445 -0.1408 0.0520  164 GLU B CA  
1250 C C   . GLU A 491 ? 2.4964 2.0728 2.1275 -0.1372 -0.1415 0.0436  164 GLU B C   
1251 O O   . GLU A 491 ? 2.6918 2.2678 2.3103 -0.1381 -0.1429 0.0372  164 GLU B O   
1252 C CB  . GLU A 491 ? 2.5843 2.1715 2.2340 -0.1441 -0.1450 0.0595  164 GLU B CB  
1253 C CG  . GLU A 491 ? 2.5636 2.1618 2.2359 -0.1347 -0.1425 0.0609  164 GLU B CG  
1254 C CD  . GLU A 491 ? 2.6705 2.2838 2.3596 -0.1341 -0.1381 0.0647  164 GLU B CD  
1255 O OE1 . GLU A 491 ? 2.9567 2.5713 2.6397 -0.1395 -0.1359 0.0654  164 GLU B OE1 
1256 O OE2 . GLU A 491 ? 2.4898 2.1135 2.1983 -0.1285 -0.1368 0.0668  164 GLU B OE2 
1257 N N   . GLU A 492 ? 2.4440 2.0170 2.0854 -0.1300 -0.1407 0.0434  165 GLU B N   
1258 C CA  . GLU A 492 ? 2.3754 1.9446 2.0147 -0.1226 -0.1414 0.0358  165 GLU B CA  
1259 C C   . GLU A 492 ? 2.4953 2.0739 2.1249 -0.1197 -0.1362 0.0247  165 GLU B C   
1260 O O   . GLU A 492 ? 2.5724 2.1484 2.1922 -0.1184 -0.1383 0.0177  165 GLU B O   
1261 C CB  . GLU A 492 ? 2.2296 1.7972 1.8826 -0.1159 -0.1399 0.0379  165 GLU B CB  
1262 C CG  . GLU A 492 ? 2.3608 1.9388 2.0321 -0.1129 -0.1417 0.0457  165 GLU B CG  
1263 C CD  . GLU A 492 ? 2.4863 2.0737 2.1747 -0.1050 -0.1380 0.0462  165 GLU B CD  
1264 O OE1 . GLU A 492 ? 2.4311 2.0162 2.1170 -0.1023 -0.1341 0.0422  165 GLU B OE1 
1265 O OE2 . GLU A 492 ? 2.7847 2.3820 2.4890 -0.1018 -0.1388 0.0503  165 GLU B OE2 
1266 N N   . ALA A 493 ? 2.4900 2.0798 2.1227 -0.1186 -0.1295 0.0231  166 ALA B N   
1267 C CA  . ALA A 493 ? 2.6009 2.2011 2.2258 -0.1159 -0.1239 0.0131  166 ALA B CA  
1268 C C   . ALA A 493 ? 2.5989 2.2017 2.2091 -0.1219 -0.1251 0.0097  166 ALA B C   
1269 O O   . ALA A 493 ? 2.7182 2.3236 2.3194 -0.1190 -0.1238 0.0002  166 ALA B O   
1270 C CB  . ALA A 493 ? 2.5831 2.1945 2.2142 -0.1154 -0.1172 0.0140  166 ALA B CB  
1271 N N   . LYS A 494 ? 2.5942 2.1967 2.2021 -0.1305 -0.1274 0.0175  167 LYS B N   
1272 C CA  . LYS A 494 ? 2.6701 2.2757 2.2639 -0.1374 -0.1288 0.0154  167 LYS B CA  
1273 C C   . LYS A 494 ? 2.5895 2.1862 2.1743 -0.1362 -0.1339 0.0103  167 LYS B C   
1274 O O   . LYS A 494 ? 2.7452 2.3467 2.3179 -0.1363 -0.1324 0.0015  167 LYS B O   
1275 C CB  . LYS A 494 ? 2.7009 2.3053 2.2960 -0.1470 -0.1321 0.0264  167 LYS B CB  
1276 C CG  . LYS A 494 ? 2.5516 2.1657 2.1541 -0.1494 -0.1275 0.0312  167 LYS B CG  
1277 C CD  . LYS A 494 ? 2.4994 2.1110 2.1042 -0.1589 -0.1318 0.0422  167 LYS B CD  
1278 C CE  . LYS A 494 ? 2.3840 2.0048 1.9968 -0.1615 -0.1277 0.0470  167 LYS B CE  
1279 N NZ  . LYS A 494 ? 2.5100 2.1280 2.1265 -0.1707 -0.1325 0.0580  167 LYS B NZ  
1280 N N   . LEU A 495 ? 2.4407 2.0245 2.0315 -0.1351 -0.1400 0.0155  168 LEU B N   
1281 C CA  . LEU A 495 ? 2.3283 1.9024 1.9116 -0.1339 -0.1456 0.0111  168 LEU B CA  
1282 C C   . LEU A 495 ? 2.5449 2.1213 2.1258 -0.1252 -0.1426 -0.0010 168 LEU B C   
1283 O O   . LEU A 495 ? 2.6208 2.1958 2.1908 -0.1249 -0.1443 -0.0089 168 LEU B O   
1284 C CB  . LEU A 495 ? 2.1098 1.6701 1.7018 -0.1339 -0.1526 0.0195  168 LEU B CB  
1285 C CG  . LEU A 495 ? 2.2564 1.8125 1.8504 -0.1428 -0.1570 0.0313  168 LEU B CG  
1286 C CD1 . LEU A 495 ? 2.2435 1.7869 1.8480 -0.1415 -0.1631 0.0393  168 LEU B CD1 
1287 C CD2 . LEU A 495 ? 2.4487 2.0045 2.0279 -0.1509 -0.1604 0.0306  168 LEU B CD2 
1288 N N   . ASN A 496 ? 2.5867 2.1668 2.1781 -0.1181 -0.1382 -0.0027 169 ASN B N   
1289 C CA  . ASN A 496 ? 2.5870 2.1699 2.1774 -0.1097 -0.1354 -0.0140 169 ASN B CA  
1290 C C   . ASN A 496 ? 2.6541 2.2487 2.2326 -0.1108 -0.1301 -0.0235 169 ASN B C   
1291 O O   . ASN A 496 ? 2.5902 2.1842 2.1610 -0.1076 -0.1307 -0.0333 169 ASN B O   
1292 C CB  . ASN A 496 ? 2.3498 1.9358 1.9536 -0.1028 -0.1314 -0.0132 169 ASN B CB  
1293 C CG  . ASN A 496 ? 2.5013 2.0780 2.1171 -0.1026 -0.1357 -0.0031 169 ASN B CG  
1294 O OD1 . ASN A 496 ? 2.6132 2.1787 2.2283 -0.1049 -0.1425 0.0014  169 ASN B OD1 
1295 N ND2 . ASN A 496 ? 2.5410 2.1224 2.1679 -0.0999 -0.1316 0.0007  169 ASN B ND2 
1296 N N   . ARG A 497 ? 2.6308 2.2367 2.2084 -0.1152 -0.1249 -0.0207 170 ARG B N   
1297 C CA  . ARG A 497 ? 2.6894 2.3075 2.2556 -0.1172 -0.1198 -0.0286 170 ARG B CA  
1298 C C   . ARG A 497 ? 2.6294 2.2439 2.1814 -0.1220 -0.1240 -0.0324 170 ARG B C   
1299 O O   . ARG A 497 ? 2.6774 2.2958 2.2210 -0.1189 -0.1222 -0.0434 170 ARG B O   
1300 C CB  . ARG A 497 ? 2.5519 2.1809 2.1185 -0.1235 -0.1155 -0.0225 170 ARG B CB  
1301 C CG  . ARG A 497 ? 2.4869 2.1172 2.0678 -0.1215 -0.1132 -0.0153 170 ARG B CG  
1302 C CD  . ARG A 497 ? 2.5745 2.2157 2.1548 -0.1281 -0.1093 -0.0102 170 ARG B CD  
1303 N NE  . ARG A 497 ? 2.6102 2.2463 2.1883 -0.1372 -0.1145 -0.0006 170 ARG B NE  
1304 C CZ  . ARG A 497 ? 2.6429 2.2807 2.2085 -0.1444 -0.1168 -0.0008 170 ARG B CZ  
1305 N NH1 . ARG A 497 ? 2.7018 2.3484 2.2556 -0.1443 -0.1134 -0.0101 170 ARG B NH1 
1306 N NH2 . ARG A 497 ? 2.6309 2.2618 2.1961 -0.1520 -0.1227 0.0085  170 ARG B NH2 
1307 N N   . GLU A 498 ? 2.5781 2.1854 2.1276 -0.1297 -0.1298 -0.0234 171 GLU B N   
1308 C CA  . GLU A 498 ? 2.8018 2.4054 2.3374 -0.1351 -0.1342 -0.0261 171 GLU B CA  
1309 C C   . GLU A 498 ? 3.0112 2.6055 2.5441 -0.1288 -0.1380 -0.0348 171 GLU B C   
1310 O O   . GLU A 498 ? 3.0260 2.6212 2.5460 -0.1303 -0.1390 -0.0427 171 GLU B O   
1311 C CB  . GLU A 498 ? 2.4333 2.0288 1.9690 -0.1439 -0.1407 -0.0140 171 GLU B CB  
1312 C CG  . GLU A 498 ? 2.3611 1.9659 1.8969 -0.1519 -0.1380 -0.0059 171 GLU B CG  
1313 C CD  . GLU A 498 ? 2.3265 1.9236 1.8742 -0.1554 -0.1421 0.0074  171 GLU B CD  
1314 O OE1 . GLU A 498 ? 2.1806 1.7646 1.7306 -0.1559 -0.1489 0.0118  171 GLU B OE1 
1315 O OE2 . GLU A 498 ? 2.3091 1.9132 1.8642 -0.1576 -0.1386 0.0133  171 GLU B OE2 
1316 N N   . GLU A 499 ? 2.7994 2.3848 2.3443 -0.1217 -0.1403 -0.0335 172 GLU B N   
1317 C CA  . GLU A 499 ? 2.8290 2.4058 2.3729 -0.1151 -0.1440 -0.0417 172 GLU B CA  
1318 C C   . GLU A 499 ? 2.7385 2.3248 2.2773 -0.1091 -0.1382 -0.0556 172 GLU B C   
1319 O O   . GLU A 499 ? 2.6433 2.2268 2.1731 -0.1077 -0.1404 -0.0648 172 GLU B O   
1320 C CB  . GLU A 499 ? 2.7476 2.3145 2.3064 -0.1088 -0.1473 -0.0368 172 GLU B CB  
1321 C CG  . GLU A 499 ? 2.9080 2.4629 2.4713 -0.1137 -0.1544 -0.0247 172 GLU B CG  
1322 C CD  . GLU A 499 ? 2.9278 2.4799 2.5072 -0.1102 -0.1541 -0.0164 172 GLU B CD  
1323 O OE1 . GLU A 499 ? 2.8895 2.4440 2.4767 -0.1023 -0.1511 -0.0211 172 GLU B OE1 
1324 O OE2 . GLU A 499 ? 3.1958 2.7438 2.7802 -0.1154 -0.1569 -0.0052 172 GLU B OE2 
1325 N N   . ILE A 500 ? 2.8087 2.4063 2.3535 -0.1055 -0.1309 -0.0574 173 ILE B N   
1326 C CA  . ILE A 500 ? 2.7003 2.3080 2.2405 -0.1001 -0.1252 -0.0706 173 ILE B CA  
1327 C C   . ILE A 500 ? 2.7480 2.3680 2.2742 -0.1066 -0.1208 -0.0747 173 ILE B C   
1328 O O   . ILE A 500 ? 2.5342 2.1615 2.0534 -0.1034 -0.1172 -0.0865 173 ILE B O   
1329 C CB  . ILE A 500 ? 2.4226 2.0366 1.9754 -0.0928 -0.1196 -0.0717 173 ILE B CB  
1330 C CG1 . ILE A 500 ? 2.3761 1.9780 1.9410 -0.0859 -0.1244 -0.0699 173 ILE B CG1 
1331 C CG2 . ILE A 500 ? 1.8886 1.5143 1.4376 -0.0876 -0.1131 -0.0845 173 ILE B CG2 
1332 C CD1 . ILE A 500 ? 1.7198 1.3265 1.2978 -0.0798 -0.1200 -0.0684 173 ILE B CD1 
1333 N N   . ASP A 501 ? 2.9364 2.5590 2.4585 -0.1158 -0.1214 -0.0653 174 ASP B N   
1334 C CA  . ASP A 501 ? 3.0054 2.6400 2.5141 -0.1230 -0.1179 -0.0679 174 ASP B CA  
1335 C C   . ASP A 501 ? 2.8868 2.5207 2.3833 -0.1240 -0.1201 -0.0767 174 ASP B C   
1336 O O   . ASP A 501 ? 3.0383 2.6601 2.5354 -0.1234 -0.1266 -0.0755 174 ASP B O   
1337 C CB  . ASP A 501 ? 3.0835 2.7187 2.5912 -0.1331 -0.1199 -0.0549 174 ASP B CB  
1338 C CG  . ASP A 501 ? 2.9776 2.6208 2.4961 -0.1330 -0.1149 -0.0480 174 ASP B CG  
1339 O OD1 . ASP A 501 ? 3.1000 2.7508 2.6241 -0.1261 -0.1090 -0.0541 174 ASP B OD1 
1340 O OD2 . ASP A 501 ? 2.9093 2.5511 2.4310 -0.1399 -0.1171 -0.0366 174 ASP B OD2 
1341 N N   . GLN B 1   ? 1.4248 1.2669 1.2793 -0.0428 -0.0686 0.0657  1   GLN H N   
1342 C CA  . GLN B 1   ? 1.7437 1.5839 1.5943 -0.0406 -0.0638 0.0580  1   GLN H CA  
1343 C C   . GLN B 1   ? 2.0975 1.9366 1.9436 -0.0410 -0.0570 0.0538  1   GLN H C   
1344 O O   . GLN B 1   ? 2.1868 2.0176 2.0325 -0.0394 -0.0570 0.0527  1   GLN H O   
1345 C CB  . GLN B 1   ? 1.5796 1.4289 1.4293 -0.0421 -0.0622 0.0568  1   GLN H CB  
1346 C CG  . GLN B 1   ? 1.9097 1.7596 1.7646 -0.0412 -0.0688 0.0600  1   GLN H CG  
1347 C CD  . GLN B 1   ? 2.0087 1.8680 1.8629 -0.0432 -0.0674 0.0595  1   GLN H CD  
1348 O OE1 . GLN B 1   ? 1.6575 1.5248 1.5077 -0.0464 -0.0626 0.0588  1   GLN H OE1 
1349 N NE2 . GLN B 1   ? 2.2845 2.1429 2.1428 -0.0414 -0.0718 0.0596  1   GLN H NE2 
1350 N N   . VAL B 2   ? 2.2421 2.0896 2.0850 -0.0435 -0.0516 0.0515  2   VAL H N   
1351 C CA  . VAL B 2   ? 2.2992 2.1467 2.1385 -0.0441 -0.0451 0.0472  2   VAL H CA  
1352 C C   . VAL B 2   ? 2.3164 2.1648 2.1574 -0.0461 -0.0450 0.0514  2   VAL H C   
1353 O O   . VAL B 2   ? 2.3865 2.2439 2.2279 -0.0493 -0.0442 0.0548  2   VAL H O   
1354 C CB  . VAL B 2   ? 2.2343 2.0910 2.0704 -0.0462 -0.0398 0.0434  2   VAL H CB  
1355 C CG1 . VAL B 2   ? 2.0607 1.9170 1.8943 -0.0469 -0.0335 0.0390  2   VAL H CG1 
1356 C CG2 . VAL B 2   ? 2.1818 2.0389 2.0168 -0.0446 -0.0402 0.0400  2   VAL H CG2 
1357 N N   . GLN B 3   ? 1.9009 1.7404 1.7426 -0.0445 -0.0455 0.0514  3   GLN H N   
1358 C CA  . GLN B 3   ? 2.1116 1.9515 1.9556 -0.0462 -0.0458 0.0558  3   GLN H CA  
1359 C C   . GLN B 3   ? 1.8901 1.7221 1.7333 -0.0449 -0.0429 0.0525  3   GLN H C   
1360 O O   . GLN B 3   ? 1.9806 1.8035 1.8254 -0.0434 -0.0464 0.0544  3   GLN H O   
1361 C CB  . GLN B 3   ? 2.2996 2.1368 2.1477 -0.0462 -0.0530 0.0630  3   GLN H CB  
1362 C CG  . GLN B 3   ? 2.1800 2.0258 2.0300 -0.0482 -0.0566 0.0678  3   GLN H CG  
1363 C CD  . GLN B 3   ? 2.3561 2.1980 2.2111 -0.0480 -0.0645 0.0750  3   GLN H CD  
1364 O OE1 . GLN B 3   ? 2.5254 2.3568 2.3819 -0.0454 -0.0679 0.0750  3   GLN H OE1 
1365 N NE2 . GLN B 3   ? 2.1976 2.0480 2.0552 -0.0510 -0.0676 0.0812  3   GLN H NE2 
1366 N N   . LEU B 4   ? 1.6903 1.5255 1.5313 -0.0458 -0.0367 0.0476  4   LEU H N   
1367 C CA  . LEU B 4   ? 1.5235 1.3526 1.3647 -0.0453 -0.0337 0.0450  4   LEU H CA  
1368 C C   . LEU B 4   ? 1.5798 1.4148 1.4234 -0.0478 -0.0308 0.0472  4   LEU H C   
1369 O O   . LEU B 4   ? 1.5667 1.4103 1.4094 -0.0496 -0.0261 0.0445  4   LEU H O   
1370 C CB  . LEU B 4   ? 1.6429 1.4709 1.4808 -0.0445 -0.0291 0.0379  4   LEU H CB  
1371 C CG  . LEU B 4   ? 1.9119 1.7344 1.7472 -0.0420 -0.0311 0.0350  4   LEU H CG  
1372 C CD1 . LEU B 4   ? 1.8468 1.6707 1.6794 -0.0419 -0.0262 0.0286  4   LEU H CD1 
1373 C CD2 . LEU B 4   ? 1.6939 1.5053 1.5298 -0.0399 -0.0350 0.0363  4   LEU H CD2 
1374 N N   . VAL B 5   ? 1.4514 1.2821 1.2984 -0.0479 -0.0335 0.0519  5   VAL H N   
1375 C CA  . VAL B 5   ? 1.3405 1.1775 1.1907 -0.0503 -0.0315 0.0551  5   VAL H CA  
1376 C C   . VAL B 5   ? 1.4785 1.3101 1.3309 -0.0499 -0.0284 0.0528  5   VAL H C   
1377 O O   . VAL B 5   ? 1.5473 1.3691 1.4011 -0.0486 -0.0316 0.0548  5   VAL H O   
1378 C CB  . VAL B 5   ? 1.3397 1.1771 1.1931 -0.0511 -0.0371 0.0631  5   VAL H CB  
1379 C CG1 . VAL B 5   ? 1.4952 1.3393 1.3523 -0.0535 -0.0346 0.0663  5   VAL H CG1 
1380 C CG2 . VAL B 5   ? 1.4898 1.3333 1.3420 -0.0518 -0.0404 0.0657  5   VAL H CG2 
1381 N N   . GLN B 6   ? 1.4921 1.3298 1.3450 -0.0512 -0.0224 0.0486  6   GLN H N   
1382 C CA  . GLN B 6   ? 1.3955 1.2282 1.2513 -0.0509 -0.0195 0.0461  6   GLN H CA  
1383 C C   . GLN B 6   ? 1.3830 1.2171 1.2441 -0.0521 -0.0200 0.0511  6   GLN H C   
1384 O O   . GLN B 6   ? 1.4252 1.2650 1.2875 -0.0533 -0.0222 0.0564  6   GLN H O   
1385 C CB  . GLN B 6   ? 1.3937 1.2316 1.2487 -0.0515 -0.0133 0.0391  6   GLN H CB  
1386 C CG  . GLN B 6   ? 1.4764 1.3127 1.3265 -0.0504 -0.0129 0.0343  6   GLN H CG  
1387 C CD  . GLN B 6   ? 1.5101 1.3479 1.3604 -0.0507 -0.0077 0.0276  6   GLN H CD  
1388 O OE1 . GLN B 6   ? 1.4663 1.3013 1.3207 -0.0509 -0.0055 0.0263  6   GLN H OE1 
1389 N NE2 . GLN B 6   ? 1.5472 1.3890 1.3936 -0.0507 -0.0060 0.0235  6   GLN H NE2 
1390 N N   . SER B 7   ? 1.4641 1.2933 1.3290 -0.0519 -0.0180 0.0497  7   SER H N   
1391 C CA  . SER B 7   ? 1.4580 1.2881 1.3288 -0.0529 -0.0182 0.0543  7   SER H CA  
1392 C C   . SER B 7   ? 1.6202 1.4626 1.4938 -0.0547 -0.0125 0.0521  7   SER H C   
1393 O O   . SER B 7   ? 1.6391 1.4883 1.5101 -0.0552 -0.0084 0.0467  7   SER H O   
1394 C CB  . SER B 7   ? 1.6323 1.4521 1.5067 -0.0522 -0.0188 0.0540  7   SER H CB  
1395 O OG  . SER B 7   ? 1.8006 1.6207 1.6761 -0.0521 -0.0139 0.0475  7   SER H OG  
1396 N N   . GLY B 8   ? 1.6899 1.5353 1.5691 -0.0558 -0.0123 0.0564  8   GLY H N   
1397 C CA  . GLY B 8   ? 1.7205 1.5780 1.6029 -0.0574 -0.0069 0.0544  8   GLY H CA  
1398 C C   . GLY B 8   ? 1.5669 1.4238 1.4527 -0.0569 -0.0014 0.0473  8   GLY H C   
1399 O O   . GLY B 8   ? 1.7254 1.5722 1.6129 -0.0556 -0.0023 0.0455  8   GLY H O   
1400 N N   . ALA B 9   ? 1.3946 1.2631 1.2815 -0.0581 0.0041  0.0432  9   ALA H N   
1401 C CA  . ALA B 9   ? 1.5112 1.3805 1.4023 -0.0577 0.0094  0.0359  9   ALA H CA  
1402 C C   . ALA B 9   ? 1.5750 1.4381 1.4746 -0.0571 0.0093  0.0377  9   ALA H C   
1403 O O   . ALA B 9   ? 1.6161 1.4804 1.5195 -0.0577 0.0075  0.0438  9   ALA H O   
1404 C CB  . ALA B 9   ? 1.4709 1.3546 1.3621 -0.0592 0.0152  0.0315  9   ALA H CB  
1405 N N   . GLU B 10  ? 1.4982 1.3546 1.4011 -0.0561 0.0109  0.0327  10  GLU H N   
1406 C CA  . GLU B 10  ? 1.4899 1.3384 1.4008 -0.0556 0.0099  0.0345  10  GLU H CA  
1407 C C   . GLU B 10  ? 1.6515 1.5026 1.5697 -0.0554 0.0151  0.0276  10  GLU H C   
1408 O O   . GLU B 10  ? 1.5921 1.4445 1.5082 -0.0552 0.0178  0.0209  10  GLU H O   
1409 C CB  . GLU B 10  ? 1.8368 1.6712 1.7450 -0.0548 0.0047  0.0370  10  GLU H CB  
1410 C CG  . GLU B 10  ? 2.2282 2.0591 2.1314 -0.0547 -0.0010 0.0443  10  GLU H CG  
1411 C CD  . GLU B 10  ? 2.4519 2.2696 2.3516 -0.0538 -0.0060 0.0461  10  GLU H CD  
1412 O OE1 . GLU B 10  ? 2.4308 2.2428 2.3306 -0.0534 -0.0051 0.0417  10  GLU H OE1 
1413 O OE2 . GLU B 10  ? 2.5501 2.3634 2.4471 -0.0536 -0.0110 0.0519  10  GLU H OE2 
1414 N N   . VAL B 11  ? 1.6626 1.5144 1.5901 -0.0556 0.0162  0.0295  11  VAL H N   
1415 C CA  . VAL B 11  ? 1.6743 1.5295 1.6110 -0.0553 0.0211  0.0236  11  VAL H CA  
1416 C C   . VAL B 11  ? 1.7077 1.5525 1.6531 -0.0549 0.0185  0.0268  11  VAL H C   
1417 O O   . VAL B 11  ? 1.5788 1.4211 1.5269 -0.0553 0.0155  0.0339  11  VAL H O   
1418 C CB  . VAL B 11  ? 1.6048 1.4742 1.5454 -0.0560 0.0260  0.0224  11  VAL H CB  
1419 C CG1 . VAL B 11  ? 1.6894 1.5616 1.6408 -0.0553 0.0308  0.0161  11  VAL H CG1 
1420 C CG2 . VAL B 11  ? 1.4913 1.3714 1.4229 -0.0568 0.0284  0.0196  11  VAL H CG2 
1421 N N   . LYS B 12  ? 1.8011 1.6399 1.7512 -0.0545 0.0192  0.0219  12  LYS H N   
1422 C CA  . LYS B 12  ? 1.9410 1.7697 1.8997 -0.0545 0.0164  0.0248  12  LYS H CA  
1423 C C   . LYS B 12  ? 1.9806 1.8100 1.9491 -0.0542 0.0201  0.0177  12  LYS H C   
1424 O O   . LYS B 12  ? 2.0052 1.8423 1.9732 -0.0538 0.0246  0.0104  12  LYS H O   
1425 C CB  . LYS B 12  ? 1.7642 1.5801 1.7165 -0.0548 0.0106  0.0287  12  LYS H CB  
1426 C CG  . LYS B 12  ? 1.7191 1.5331 1.6641 -0.0550 0.0063  0.0360  12  LYS H CG  
1427 C CD  . LYS B 12  ? 1.5906 1.3928 1.5287 -0.0551 0.0007  0.0394  12  LYS H CD  
1428 C CE  . LYS B 12  ? 1.6016 1.4033 1.5340 -0.0551 -0.0032 0.0462  12  LYS H CE  
1429 N NZ  . LYS B 12  ? 2.0305 1.8215 1.9557 -0.0550 -0.0089 0.0497  12  LYS H NZ  
1430 N N   . LYS B 13  ? 1.8847 1.7059 1.8626 -0.0544 0.0178  0.0200  13  LYS H N   
1431 C CA  . LYS B 13  ? 1.8111 1.6296 1.8003 -0.0543 0.0194  0.0153  13  LYS H CA  
1432 C C   . LYS B 13  ? 1.8213 1.6280 1.8083 -0.0551 0.0151  0.0157  13  LYS H C   
1433 O O   . LYS B 13  ? 1.8157 1.6148 1.7950 -0.0557 0.0104  0.0213  13  LYS H O   
1434 C CB  . LYS B 13  ? 1.9340 1.7518 1.9363 -0.0543 0.0193  0.0189  13  LYS H CB  
1435 C CG  . LYS B 13  ? 2.0167 1.8476 2.0231 -0.0535 0.0243  0.0176  13  LYS H CG  
1436 C CD  . LYS B 13  ? 1.7278 1.5580 1.7477 -0.0535 0.0242  0.0215  13  LYS H CD  
1437 C CE  . LYS B 13  ? 1.6046 1.4490 1.6285 -0.0529 0.0296  0.0199  13  LYS H CE  
1438 N NZ  . LYS B 13  ? 1.5038 1.3484 1.5413 -0.0528 0.0296  0.0238  13  LYS H NZ  
1439 N N   . PRO B 14  ? 2.1016 1.9069 2.0954 -0.0551 0.0165  0.0097  14  PRO H N   
1440 C CA  . PRO B 14  ? 1.9958 1.7909 1.9869 -0.0563 0.0125  0.0101  14  PRO H CA  
1441 C C   . PRO B 14  ? 2.0477 1.8319 2.0416 -0.0576 0.0069  0.0179  14  PRO H C   
1442 O O   . PRO B 14  ? 1.9282 1.7112 1.9322 -0.0578 0.0064  0.0212  14  PRO H O   
1443 C CB  . PRO B 14  ? 1.9681 1.7646 1.9696 -0.0562 0.0151  0.0029  14  PRO H CB  
1444 C CG  . PRO B 14  ? 2.1447 1.9537 2.1477 -0.0547 0.0212  -0.0034 14  PRO H CG  
1445 C CD  . PRO B 14  ? 2.1713 1.9847 2.1746 -0.0542 0.0219  0.0019  14  PRO H CD  
1446 N N   . GLY B 15  ? 2.0317 1.8082 2.0162 -0.0587 0.0027  0.0209  15  GLY H N   
1447 C CA  . GLY B 15  ? 2.0705 1.8363 2.0560 -0.0604 -0.0029 0.0279  15  GLY H CA  
1448 C C   . GLY B 15  ? 2.0062 1.7699 1.9856 -0.0602 -0.0058 0.0349  15  GLY H C   
1449 O O   . GLY B 15  ? 2.3325 2.0878 2.3148 -0.0616 -0.0102 0.0410  15  GLY H O   
1450 N N   . ALA B 16  ? 1.9965 1.7671 1.9677 -0.0588 -0.0038 0.0345  16  ALA H N   
1451 C CA  . ALA B 16  ? 2.0270 1.7959 1.9921 -0.0586 -0.0068 0.0411  16  ALA H CA  
1452 C C   . ALA B 16  ? 1.9164 1.6843 1.8674 -0.0582 -0.0085 0.0409  16  ALA H C   
1453 O O   . ALA B 16  ? 2.0698 1.8424 2.0159 -0.0576 -0.0057 0.0352  16  ALA H O   
1454 C CB  . ALA B 16  ? 2.0320 1.8107 2.0009 -0.0575 -0.0034 0.0419  16  ALA H CB  
1455 N N   . SER B 17  ? 1.5533 1.3148 1.4981 -0.0584 -0.0132 0.0469  17  SER H N   
1456 C CA  . SER B 17  ? 1.8474 1.6070 1.7797 -0.0579 -0.0153 0.0466  17  SER H CA  
1457 C C   . SER B 17  ? 1.8735 1.6426 1.8005 -0.0564 -0.0129 0.0456  17  SER H C   
1458 O O   . SER B 17  ? 1.7506 1.5250 1.6816 -0.0561 -0.0119 0.0484  17  SER H O   
1459 C CB  . SER B 17  ? 2.1280 1.8773 2.0560 -0.0586 -0.0214 0.0529  17  SER H CB  
1460 O OG  . SER B 17  ? 1.9257 1.6665 1.8575 -0.0605 -0.0240 0.0539  17  SER H OG  
1461 N N   . VAL B 18  ? 1.7276 1.4991 1.6457 -0.0557 -0.0120 0.0419  18  VAL H N   
1462 C CA  . VAL B 18  ? 1.5896 1.3700 1.5022 -0.0546 -0.0101 0.0409  18  VAL H CA  
1463 C C   . VAL B 18  ? 1.5602 1.3361 1.4627 -0.0539 -0.0142 0.0431  18  VAL H C   
1464 O O   . VAL B 18  ? 1.5289 1.2984 1.4268 -0.0540 -0.0160 0.0416  18  VAL H O   
1465 C CB  . VAL B 18  ? 1.6852 1.4746 1.5976 -0.0543 -0.0047 0.0337  18  VAL H CB  
1466 C CG1 . VAL B 18  ? 1.7567 1.5423 1.6642 -0.0544 -0.0049 0.0295  18  VAL H CG1 
1467 C CG2 . VAL B 18  ? 1.6907 1.4899 1.5980 -0.0537 -0.0028 0.0334  18  VAL H CG2 
1468 N N   . LYS B 19  ? 1.7920 1.5717 1.6915 -0.0533 -0.0156 0.0468  19  LYS H N   
1469 C CA  . LYS B 19  ? 1.7900 1.5657 1.6814 -0.0525 -0.0200 0.0494  19  LYS H CA  
1470 C C   . LYS B 19  ? 1.7587 1.5440 1.6458 -0.0518 -0.0184 0.0483  19  LYS H C   
1471 O O   . LYS B 19  ? 1.9737 1.7657 1.8635 -0.0522 -0.0177 0.0513  19  LYS H O   
1472 C CB  . LYS B 19  ? 1.8238 1.5925 1.7168 -0.0527 -0.0253 0.0565  19  LYS H CB  
1473 C CG  . LYS B 19  ? 1.6245 1.3881 1.5097 -0.0516 -0.0303 0.0588  19  LYS H CG  
1474 C CD  . LYS B 19  ? 1.8610 1.6170 1.7480 -0.0519 -0.0359 0.0657  19  LYS H CD  
1475 C CE  . LYS B 19  ? 1.9173 1.6681 1.7972 -0.0507 -0.0410 0.0674  19  LYS H CE  
1476 N NZ  . LYS B 19  ? 2.0759 1.8189 1.9576 -0.0510 -0.0469 0.0740  19  LYS H NZ  
1477 N N   . VAL B 20  ? 1.5492 1.3351 1.4295 -0.0510 -0.0180 0.0444  20  VAL H N   
1478 C CA  . VAL B 20  ? 1.6398 1.4341 1.5155 -0.0505 -0.0169 0.0433  20  VAL H CA  
1479 C C   . VAL B 20  ? 1.5250 1.3138 1.3945 -0.0493 -0.0221 0.0459  20  VAL H C   
1480 O O   . VAL B 20  ? 1.6069 1.3872 1.4735 -0.0487 -0.0245 0.0451  20  VAL H O   
1481 C CB  . VAL B 20  ? 1.7176 1.5177 1.5910 -0.0506 -0.0122 0.0363  20  VAL H CB  
1482 C CG1 . VAL B 20  ? 1.5031 1.3133 1.3729 -0.0506 -0.0107 0.0355  20  VAL H CG1 
1483 C CG2 . VAL B 20  ? 1.8403 1.6428 1.7205 -0.0515 -0.0078 0.0329  20  VAL H CG2 
1484 N N   . SER B 21  ? 1.3150 1.1090 1.1830 -0.0491 -0.0239 0.0491  21  SER H N   
1485 C CA  . SER B 21  ? 1.3551 1.1444 1.2184 -0.0479 -0.0291 0.0517  21  SER H CA  
1486 C C   . SER B 21  ? 1.5193 1.3166 1.3786 -0.0475 -0.0282 0.0497  21  SER H C   
1487 O O   . SER B 21  ? 1.6010 1.4081 1.4618 -0.0487 -0.0257 0.0504  21  SER H O   
1488 C CB  . SER B 21  ? 1.6355 1.4218 1.5018 -0.0481 -0.0341 0.0590  21  SER H CB  
1489 O OG  . SER B 21  ? 2.0972 1.8933 1.9653 -0.0491 -0.0336 0.0621  21  SER H OG  
1490 N N   . CYS B 22  ? 1.5468 1.3401 1.4012 -0.0460 -0.0302 0.0474  22  CYS H N   
1491 C CA  . CYS B 22  ? 1.5889 1.3883 1.4398 -0.0454 -0.0305 0.0463  22  CYS H CA  
1492 C C   . CYS B 22  ? 1.6555 1.4492 1.5048 -0.0438 -0.0368 0.0499  22  CYS H C   
1493 O O   . CYS B 22  ? 1.7844 1.5695 1.6313 -0.0422 -0.0393 0.0484  22  CYS H O   
1494 C CB  . CYS B 22  ? 1.4756 1.2767 1.3227 -0.0448 -0.0269 0.0397  22  CYS H CB  
1495 S SG  . CYS B 22  ? 2.3928 2.2034 2.2420 -0.0468 -0.0201 0.0358  22  CYS H SG  
1496 N N   . LYS B 23  ? 1.5477 1.3467 1.3988 -0.0445 -0.0395 0.0546  23  LYS H N   
1497 C CA  . LYS B 23  ? 1.6318 1.4265 1.4828 -0.0432 -0.0459 0.0586  23  LYS H CA  
1498 C C   . LYS B 23  ? 1.8735 1.6718 1.7213 -0.0421 -0.0462 0.0556  23  LYS H C   
1499 O O   . LYS B 23  ? 1.9017 1.7098 1.7494 -0.0434 -0.0441 0.0555  23  LYS H O   
1500 C CB  . LYS B 23  ? 1.6794 1.4789 1.5346 -0.0449 -0.0487 0.0657  23  LYS H CB  
1501 C CG  . LYS B 23  ? 1.9555 1.7515 1.8147 -0.0459 -0.0489 0.0693  23  LYS H CG  
1502 C CD  . LYS B 23  ? 2.1297 1.9317 1.9932 -0.0478 -0.0514 0.0765  23  LYS H CD  
1503 C CE  . LYS B 23  ? 2.4196 2.2180 2.2875 -0.0488 -0.0516 0.0802  23  LYS H CE  
1504 N NZ  . LYS B 23  ? 2.6520 2.4571 2.5244 -0.0509 -0.0539 0.0875  23  LYS H NZ  
1505 N N   . ALA B 24  ? 1.8606 1.6514 1.7058 -0.0397 -0.0485 0.0527  24  ALA H N   
1506 C CA  . ALA B 24  ? 1.9820 1.7751 1.8254 -0.0382 -0.0504 0.0510  24  ALA H CA  
1507 C C   . ALA B 24  ? 2.2505 2.0441 2.0975 -0.0382 -0.0567 0.0572  24  ALA H C   
1508 O O   . ALA B 24  ? 2.3128 2.0996 2.1621 -0.0378 -0.0612 0.0612  24  ALA H O   
1509 C CB  . ALA B 24  ? 2.1469 1.9321 1.9871 -0.0356 -0.0512 0.0462  24  ALA H CB  
1510 N N   . SER B 25  ? 2.3956 2.1974 2.2432 -0.0389 -0.0571 0.0583  25  SER H N   
1511 C CA  . SER B 25  ? 2.4719 2.2752 2.3233 -0.0392 -0.0634 0.0643  25  SER H CA  
1512 C C   . SER B 25  ? 2.6032 2.4122 2.4540 -0.0386 -0.0640 0.0624  25  SER H C   
1513 O O   . SER B 25  ? 2.7803 2.5942 2.6278 -0.0389 -0.0588 0.0575  25  SER H O   
1514 C CB  . SER B 25  ? 2.5160 2.3259 2.3705 -0.0423 -0.0637 0.0707  25  SER H CB  
1515 O OG  . SER B 25  ? 2.5348 2.3558 2.3878 -0.0448 -0.0582 0.0693  25  SER H OG  
1516 N N   . GLY B 26  ? 2.5941 2.4017 2.4485 -0.0378 -0.0706 0.0663  26  GLY H N   
1517 C CA  . GLY B 26  ? 2.5601 2.3717 2.4151 -0.0369 -0.0721 0.0647  26  GLY H CA  
1518 C C   . GLY B 26  ? 2.6785 2.4859 2.5300 -0.0339 -0.0693 0.0571  26  GLY H C   
1519 O O   . GLY B 26  ? 2.7871 2.6001 2.6378 -0.0338 -0.0677 0.0544  26  GLY H O   
1520 N N   . TYR B 27  ? 2.7736 2.5716 2.6232 -0.0317 -0.0690 0.0538  27  TYR H N   
1521 C CA  . TYR B 27  ? 2.4735 2.2683 2.3189 -0.0296 -0.0650 0.0465  27  TYR H CA  
1522 C C   . TYR B 27  ? 2.4778 2.2643 2.3241 -0.0259 -0.0694 0.0440  27  TYR H C   
1523 O O   . TYR B 27  ? 2.8258 2.6057 2.6750 -0.0249 -0.0751 0.0472  27  TYR H O   
1524 C CB  . TYR B 27  ? 2.5096 2.3011 2.3516 -0.0306 -0.0604 0.0445  27  TYR H CB  
1525 C CG  . TYR B 27  ? 2.6383 2.4211 2.4820 -0.0301 -0.0646 0.0480  27  TYR H CG  
1526 C CD1 . TYR B 27  ? 2.9845 2.7578 2.8267 -0.0276 -0.0670 0.0453  27  TYR H CD1 
1527 C CD2 . TYR B 27  ? 2.6585 2.4430 2.5054 -0.0323 -0.0666 0.0543  27  TYR H CD2 
1528 C CE1 . TYR B 27  ? 2.9746 2.7396 2.8182 -0.0274 -0.0712 0.0486  27  TYR H CE1 
1529 C CE2 . TYR B 27  ? 2.8885 2.6650 2.7372 -0.0320 -0.0707 0.0579  27  TYR H CE2 
1530 C CZ  . TYR B 27  ? 2.8702 2.6367 2.7171 -0.0295 -0.0731 0.0549  27  TYR H CZ  
1531 O OH  . TYR B 27  ? 2.2858 2.0442 2.1343 -0.0294 -0.0774 0.0584  27  TYR H OH  
1532 N N   . SER B 28  ? 2.3648 2.1517 2.2085 -0.0239 -0.0668 0.0379  28  SER H N   
1533 C CA  . SER B 28  ? 2.4697 2.2495 2.3137 -0.0203 -0.0698 0.0341  28  SER H CA  
1534 C C   . SER B 28  ? 2.2423 2.0158 2.0811 -0.0194 -0.0665 0.0292  28  SER H C   
1535 O O   . SER B 28  ? 2.2675 2.0396 2.1040 -0.0171 -0.0650 0.0235  28  SER H O   
1536 C CB  . SER B 28  ? 2.2947 2.0796 2.1403 -0.0185 -0.0697 0.0308  28  SER H CB  
1537 O OG  . SER B 28  ? 1.6549 1.4460 1.4965 -0.0196 -0.0632 0.0269  28  SER H OG  
1538 N N   . PHE B 29  ? 2.1287 1.8990 1.9658 -0.0214 -0.0653 0.0315  29  PHE H N   
1539 C CA  . PHE B 29  ? 1.8439 1.6082 1.6766 -0.0215 -0.0627 0.0285  29  PHE H CA  
1540 C C   . PHE B 29  ? 1.9308 1.6877 1.7616 -0.0185 -0.0652 0.0242  29  PHE H C   
1541 O O   . PHE B 29  ? 2.1822 1.9315 2.0143 -0.0173 -0.0703 0.0261  29  PHE H O   
1542 C CB  . PHE B 29  ? 1.8354 1.5957 1.6694 -0.0235 -0.0644 0.0338  29  PHE H CB  
1543 C CG  . PHE B 29  ? 1.6701 1.4243 1.5007 -0.0244 -0.0624 0.0324  29  PHE H CG  
1544 C CD1 . PHE B 29  ? 1.3358 1.0937 1.1642 -0.0266 -0.0566 0.0308  29  PHE H CD1 
1545 C CD2 . PHE B 29  ? 1.8715 1.6162 1.7020 -0.0236 -0.0669 0.0339  29  PHE H CD2 
1546 C CE1 . PHE B 29  ? 1.5851 1.3375 1.4113 -0.0279 -0.0552 0.0303  29  PHE H CE1 
1547 C CE2 . PHE B 29  ? 1.7190 1.4582 1.5467 -0.0250 -0.0654 0.0335  29  PHE H CE2 
1548 C CZ  . PHE B 29  ? 1.7373 1.4804 1.5631 -0.0272 -0.0597 0.0319  29  PHE H CZ  
1549 N N   . SER B 30  ? 2.0500 1.8094 1.8778 -0.0171 -0.0618 0.0184  30  SER H N   
1550 C CA  . SER B 30  ? 2.0722 1.8252 1.8966 -0.0149 -0.0625 0.0136  30  SER H CA  
1551 C C   . SER B 30  ? 1.9849 1.7339 1.8045 -0.0171 -0.0595 0.0128  30  SER H C   
1552 O O   . SER B 30  ? 2.1808 1.9300 1.9959 -0.0170 -0.0561 0.0082  30  SER H O   
1553 C CB  . SER B 30  ? 2.2449 2.0029 2.0683 -0.0128 -0.0599 0.0079  30  SER H CB  
1554 O OG  . SER B 30  ? 2.7113 2.4739 2.5400 -0.0114 -0.0625 0.0094  30  SER H OG  
1555 N N   . SER B 31  ? 1.8700 1.6159 1.6909 -0.0192 -0.0609 0.0179  31  SER H N   
1556 C CA  . SER B 31  ? 1.7931 1.5364 1.6110 -0.0219 -0.0579 0.0184  31  SER H CA  
1557 C C   . SER B 31  ? 1.8706 1.6211 1.6865 -0.0236 -0.0515 0.0156  31  SER H C   
1558 O O   . SER B 31  ? 2.1474 1.8964 1.9595 -0.0248 -0.0486 0.0129  31  SER H O   
1559 C CB  . SER B 31  ? 2.0481 1.7828 1.8619 -0.0212 -0.0598 0.0160  31  SER H CB  
1560 O OG  . SER B 31  ? 2.5689 2.3049 2.3792 -0.0192 -0.0583 0.0100  31  SER H OG  
1561 N N   . TYR B 32  ? 1.7290 1.4876 1.5476 -0.0240 -0.0496 0.0165  32  TYR H N   
1562 C CA  . TYR B 32  ? 1.4931 1.2588 1.3102 -0.0256 -0.0439 0.0140  32  TYR H CA  
1563 C C   . TYR B 32  ? 1.4597 1.2245 1.2766 -0.0286 -0.0411 0.0155  32  TYR H C   
1564 O O   . TYR B 32  ? 1.5142 1.2741 1.3329 -0.0296 -0.0433 0.0194  32  TYR H O   
1565 C CB  . TYR B 32  ? 1.3106 1.0849 1.1307 -0.0257 -0.0430 0.0152  32  TYR H CB  
1566 C CG  . TYR B 32  ? 1.6049 1.3814 1.4263 -0.0230 -0.0455 0.0136  32  TYR H CG  
1567 C CD1 . TYR B 32  ? 1.7525 1.5277 1.5713 -0.0208 -0.0449 0.0086  32  TYR H CD1 
1568 C CD2 . TYR B 32  ? 1.9515 1.7316 1.7770 -0.0227 -0.0485 0.0172  32  TYR H CD2 
1569 C CE1 . TYR B 32  ? 2.0987 1.8760 1.9195 -0.0181 -0.0472 0.0069  32  TYR H CE1 
1570 C CE2 . TYR B 32  ? 2.2167 1.9987 2.0443 -0.0203 -0.0512 0.0160  32  TYR H CE2 
1571 C CZ  . TYR B 32  ? 2.2981 2.0785 2.1236 -0.0178 -0.0504 0.0107  32  TYR H CZ  
1572 O OH  . TYR B 32  ? 2.4444 2.2267 2.2730 -0.0152 -0.0531 0.0092  32  TYR H OH  
1573 N N   . GLY B 33  ? 1.5975 1.3670 1.4129 -0.0300 -0.0363 0.0125  33  GLY H N   
1574 C CA  . GLY B 33  ? 1.5002 1.2694 1.3164 -0.0328 -0.0334 0.0135  33  GLY H CA  
1575 C C   . GLY B 33  ? 1.4648 1.2405 1.2846 -0.0343 -0.0313 0.0156  33  GLY H C   
1576 O O   . GLY B 33  ? 1.5705 1.3520 1.3915 -0.0336 -0.0315 0.0161  33  GLY H O   
1577 N N   . ILE B 34  ? 1.4095 1.1844 1.2313 -0.0365 -0.0292 0.0167  34  ILE H N   
1578 C CA  . ILE B 34  ? 1.4586 1.2398 1.2838 -0.0382 -0.0264 0.0179  34  ILE H CA  
1579 C C   . ILE B 34  ? 1.3484 1.1297 1.1746 -0.0402 -0.0227 0.0156  34  ILE H C   
1580 O O   . ILE B 34  ? 1.3630 1.1377 1.1895 -0.0411 -0.0236 0.0164  34  ILE H O   
1581 C CB  . ILE B 34  ? 1.5051 1.2848 1.3340 -0.0386 -0.0291 0.0231  34  ILE H CB  
1582 C CG1 . ILE B 34  ? 1.7907 1.5734 1.6199 -0.0372 -0.0322 0.0256  34  ILE H CG1 
1583 C CG2 . ILE B 34  ? 1.3228 1.1074 1.1555 -0.0407 -0.0256 0.0239  34  ILE H CG2 
1584 C CD1 . ILE B 34  ? 2.0345 1.8126 1.8663 -0.0369 -0.0369 0.0310  34  ILE H CD1 
1585 N N   . SER B 35  ? 1.3625 1.1510 1.1895 -0.0412 -0.0188 0.0129  35  SER H N   
1586 C CA  . SER B 35  ? 1.2873 1.0763 1.1169 -0.0433 -0.0155 0.0112  35  SER H CA  
1587 C C   . SER B 35  ? 1.4744 1.2688 1.3083 -0.0444 -0.0134 0.0123  35  SER H C   
1588 O O   . SER B 35  ? 1.6734 1.4727 1.5076 -0.0439 -0.0140 0.0142  35  SER H O   
1589 C CB  . SER B 35  ? 1.2965 1.0894 1.1241 -0.0438 -0.0124 0.0065  35  SER H CB  
1590 O OG  . SER B 35  ? 1.6320 1.4330 1.4592 -0.0435 -0.0106 0.0051  35  SER H OG  
1591 N N   . TRP B 36  ? 1.2569 1.0508 1.0946 -0.0460 -0.0110 0.0110  36  TRP H N   
1592 C CA  . TRP B 36  ? 1.2577 1.0562 1.1004 -0.0472 -0.0085 0.0113  36  TRP H CA  
1593 C C   . TRP B 36  ? 1.3506 1.1528 1.1952 -0.0485 -0.0045 0.0066  36  TRP H C   
1594 O O   . TRP B 36  ? 1.4058 1.2038 1.2505 -0.0491 -0.0045 0.0048  36  TRP H O   
1595 C CB  . TRP B 36  ? 1.0581 0.8508 0.9052 -0.0478 -0.0102 0.0151  36  TRP H CB  
1596 C CG  . TRP B 36  ? 1.4307 1.2198 1.2765 -0.0467 -0.0143 0.0200  36  TRP H CG  
1597 C CD1 . TRP B 36  ? 1.5238 1.3065 1.3655 -0.0454 -0.0181 0.0214  36  TRP H CD1 
1598 C CD2 . TRP B 36  ? 1.4934 1.2843 1.3426 -0.0468 -0.0154 0.0243  36  TRP H CD2 
1599 N NE1 . TRP B 36  ? 1.4879 1.2681 1.3302 -0.0447 -0.0218 0.0262  36  TRP H NE1 
1600 C CE2 . TRP B 36  ? 1.6575 1.4426 1.5045 -0.0457 -0.0203 0.0284  36  TRP H CE2 
1601 C CE3 . TRP B 36  ? 1.3233 1.1205 1.1773 -0.0479 -0.0128 0.0250  36  TRP H CE3 
1602 C CZ2 . TRP B 36  ? 1.6497 1.4350 1.4993 -0.0457 -0.0229 0.0335  36  TRP H CZ2 
1603 C CZ3 . TRP B 36  ? 1.6992 1.4972 1.5556 -0.0480 -0.0150 0.0301  36  TRP H CZ3 
1604 C CH2 . TRP B 36  ? 1.7485 1.5404 1.6028 -0.0469 -0.0201 0.0346  36  TRP H CH2 
1605 N N   . VAL B 37  ? 1.2543 1.0646 1.1006 -0.0490 -0.0015 0.0047  37  VAL H N   
1606 C CA  . VAL B 37  ? 1.2768 1.0924 1.1245 -0.0501 0.0023  -0.0004 37  VAL H CA  
1607 C C   . VAL B 37  ? 1.5141 1.3338 1.3677 -0.0510 0.0050  -0.0011 37  VAL H C   
1608 O O   . VAL B 37  ? 1.5339 1.3553 1.3889 -0.0509 0.0044  0.0023  37  VAL H O   
1609 C CB  . VAL B 37  ? 1.3993 1.2220 1.2420 -0.0497 0.0033  -0.0026 37  VAL H CB  
1610 C CG1 . VAL B 37  ? 1.5746 1.4029 1.4187 -0.0509 0.0071  -0.0079 37  VAL H CG1 
1611 C CG2 . VAL B 37  ? 1.6119 1.4309 1.4495 -0.0485 0.0008  -0.0022 37  VAL H CG2 
1612 N N   . ARG B 38  ? 1.6216 1.4432 1.4791 -0.0520 0.0080  -0.0056 38  ARG H N   
1613 C CA  . ARG B 38  ? 1.7413 1.5676 1.6049 -0.0528 0.0111  -0.0075 38  ARG H CA  
1614 C C   . ARG B 38  ? 1.8086 1.6430 1.6718 -0.0535 0.0148  -0.0132 38  ARG H C   
1615 O O   . ARG B 38  ? 1.8827 1.7163 1.7449 -0.0538 0.0153  -0.0167 38  ARG H O   
1616 C CB  . ARG B 38  ? 1.6417 1.4617 1.5128 -0.0533 0.0109  -0.0075 38  ARG H CB  
1617 C CG  . ARG B 38  ? 1.8368 1.6499 1.7094 -0.0530 0.0076  -0.0017 38  ARG H CG  
1618 C CD  . ARG B 38  ? 1.9801 1.7864 1.8601 -0.0538 0.0069  -0.0011 38  ARG H CD  
1619 N NE  . ARG B 38  ? 1.8744 1.6851 1.7625 -0.0543 0.0103  -0.0042 38  ARG H NE  
1620 C CZ  . ARG B 38  ? 1.7267 1.5331 1.6233 -0.0550 0.0102  -0.0046 38  ARG H CZ  
1621 N NH1 . ARG B 38  ? 1.8772 1.6746 1.7754 -0.0556 0.0066  -0.0007 38  ARG H NH1 
1622 N NH2 . ARG B 38  ? 1.5197 1.3309 1.4235 -0.0553 0.0137  -0.0091 38  ARG H NH2 
1623 N N   . GLN B 39  ? 1.7191 1.5616 1.5831 -0.0539 0.0173  -0.0140 39  GLN H N   
1624 C CA  . GLN B 39  ? 1.7080 1.5586 1.5728 -0.0548 0.0212  -0.0199 39  GLN H CA  
1625 C C   . GLN B 39  ? 1.7017 1.5535 1.5749 -0.0551 0.0239  -0.0224 39  GLN H C   
1626 O O   . GLN B 39  ? 1.8259 1.6808 1.7015 -0.0551 0.0247  -0.0198 39  GLN H O   
1627 C CB  . GLN B 39  ? 1.6656 1.5256 1.5248 -0.0553 0.0222  -0.0193 39  GLN H CB  
1628 C CG  . GLN B 39  ? 1.9722 1.8319 1.8240 -0.0550 0.0197  -0.0173 39  GLN H CG  
1629 C CD  . GLN B 39  ? 2.0463 1.9152 1.8933 -0.0558 0.0201  -0.0160 39  GLN H CD  
1630 O OE1 . GLN B 39  ? 2.1453 2.0199 1.9938 -0.0566 0.0213  -0.0144 39  GLN H OE1 
1631 N NE2 . GLN B 39  ? 2.1932 2.0638 2.0346 -0.0559 0.0189  -0.0162 39  GLN H NE2 
1632 N N   . ALA B 40  ? 1.8348 1.6843 1.7131 -0.0554 0.0253  -0.0272 40  ALA H N   
1633 C CA  . ALA B 40  ? 1.8965 1.7489 1.7833 -0.0556 0.0284  -0.0311 40  ALA H CA  
1634 C C   . ALA B 40  ? 2.0267 1.8905 1.9110 -0.0562 0.0323  -0.0350 40  ALA H C   
1635 O O   . ALA B 40  ? 2.2520 2.1205 2.1290 -0.0568 0.0325  -0.0363 40  ALA H O   
1636 C CB  . ALA B 40  ? 1.9985 1.8462 1.8914 -0.0560 0.0286  -0.0358 40  ALA H CB  
1637 N N   . PRO B 41  ? 1.8744 1.7434 1.7647 -0.0563 0.0353  -0.0368 41  PRO H N   
1638 C CA  . PRO B 41  ? 2.0368 1.9177 1.9241 -0.0572 0.0390  -0.0400 41  PRO H CA  
1639 C C   . PRO B 41  ? 1.9678 1.8534 1.8518 -0.0579 0.0410  -0.0468 41  PRO H C   
1640 O O   . PRO B 41  ? 1.8651 1.7505 1.7551 -0.0579 0.0431  -0.0532 41  PRO H O   
1641 C CB  . PRO B 41  ? 1.9626 1.8468 1.8593 -0.0569 0.0422  -0.0425 41  PRO H CB  
1642 C CG  . PRO B 41  ? 1.8558 1.7294 1.7612 -0.0559 0.0403  -0.0420 41  PRO H CG  
1643 C CD  . PRO B 41  ? 1.8405 1.7052 1.7406 -0.0557 0.0354  -0.0357 41  PRO H CD  
1644 N N   . GLY B 42  ? 1.8046 1.6941 1.6793 -0.0587 0.0400  -0.0452 42  GLY H N   
1645 C CA  . GLY B 42  ? 1.5167 1.4104 1.3875 -0.0597 0.0414  -0.0509 42  GLY H CA  
1646 C C   . GLY B 42  ? 1.7728 1.6583 1.6459 -0.0592 0.0397  -0.0535 42  GLY H C   
1647 O O   . GLY B 42  ? 2.0190 1.9069 1.8934 -0.0598 0.0415  -0.0599 42  GLY H O   
1648 N N   . GLN B 43  ? 1.8732 1.7494 1.7468 -0.0583 0.0361  -0.0485 43  GLN H N   
1649 C CA  . GLN B 43  ? 1.6408 1.5094 1.5165 -0.0581 0.0341  -0.0500 43  GLN H CA  
1650 C C   . GLN B 43  ? 1.4487 1.3131 1.3174 -0.0579 0.0306  -0.0451 43  GLN H C   
1651 O O   . GLN B 43  ? 1.1307 0.9994 0.9922 -0.0579 0.0301  -0.0424 43  GLN H O   
1652 C CB  . GLN B 43  ? 1.7526 1.6137 1.6380 -0.0576 0.0333  -0.0497 43  GLN H CB  
1653 C CG  . GLN B 43  ? 1.9031 1.7674 1.7973 -0.0577 0.0366  -0.0563 43  GLN H CG  
1654 C CD  . GLN B 43  ? 2.1573 2.0176 2.0607 -0.0570 0.0366  -0.0544 43  GLN H CD  
1655 O OE1 . GLN B 43  ? 2.2133 2.0654 2.1231 -0.0569 0.0343  -0.0533 43  GLN H OE1 
1656 N NE2 . GLN B 43  ? 2.0951 1.9616 1.9995 -0.0567 0.0391  -0.0538 43  GLN H NE2 
1657 N N   . GLY B 44  ? 1.6460 1.5021 1.5169 -0.0577 0.0281  -0.0439 44  GLY H N   
1658 C CA  . GLY B 44  ? 1.5973 1.4499 1.4618 -0.0574 0.0252  -0.0405 44  GLY H CA  
1659 C C   . GLY B 44  ? 1.6146 1.4629 1.4761 -0.0564 0.0225  -0.0339 44  GLY H C   
1660 O O   . GLY B 44  ? 1.6516 1.4959 1.5174 -0.0560 0.0218  -0.0311 44  GLY H O   
1661 N N   . LEU B 45  ? 1.6076 1.4566 1.4618 -0.0559 0.0208  -0.0314 45  LEU H N   
1662 C CA  . LEU B 45  ? 1.5596 1.4041 1.4105 -0.0548 0.0177  -0.0257 45  LEU H CA  
1663 C C   . LEU B 45  ? 1.6316 1.4672 1.4845 -0.0546 0.0153  -0.0241 45  LEU H C   
1664 O O   . LEU B 45  ? 1.5208 1.3550 1.3725 -0.0551 0.0149  -0.0260 45  LEU H O   
1665 C CB  . LEU B 45  ? 1.5036 1.3519 1.3472 -0.0543 0.0166  -0.0243 45  LEU H CB  
1666 C CG  . LEU B 45  ? 1.7805 1.6276 1.6203 -0.0531 0.0138  -0.0190 45  LEU H CG  
1667 C CD1 . LEU B 45  ? 1.7458 1.5951 1.5881 -0.0532 0.0143  -0.0166 45  LEU H CD1 
1668 C CD2 . LEU B 45  ? 1.7560 1.6084 1.5900 -0.0529 0.0132  -0.0187 45  LEU H CD2 
1669 N N   . GLU B 46  ? 1.7869 1.6166 1.6425 -0.0542 0.0136  -0.0203 46  GLU H N   
1670 C CA  . GLU B 46  ? 1.5804 1.4017 1.4381 -0.0545 0.0113  -0.0185 46  GLU H CA  
1671 C C   . GLU B 46  ? 1.5870 1.4033 1.4408 -0.0534 0.0081  -0.0133 46  GLU H C   
1672 O O   . GLU B 46  ? 1.5042 1.3204 1.3589 -0.0527 0.0075  -0.0103 46  GLU H O   
1673 C CB  . GLU B 46  ? 1.3709 1.1890 1.2373 -0.0554 0.0119  -0.0191 46  GLU H CB  
1674 C CG  . GLU B 46  ? 1.7651 1.5868 1.6367 -0.0565 0.0145  -0.0246 46  GLU H CG  
1675 C CD  . GLU B 46  ? 1.9202 1.7389 1.8015 -0.0571 0.0151  -0.0254 46  GLU H CD  
1676 O OE1 . GLU B 46  ? 1.9778 1.7926 1.8616 -0.0567 0.0138  -0.0215 46  GLU H OE1 
1677 O OE2 . GLU B 46  ? 1.6809 1.5010 1.5679 -0.0580 0.0166  -0.0299 46  GLU H OE2 
1678 N N   . TRP B 47  ? 1.7195 1.5319 1.5692 -0.0532 0.0060  -0.0124 47  TRP H N   
1679 C CA  . TRP B 47  ? 1.6374 1.4445 1.4833 -0.0521 0.0028  -0.0082 47  TRP H CA  
1680 C C   . TRP B 47  ? 1.7270 1.5266 1.5772 -0.0529 0.0009  -0.0053 47  TRP H C   
1681 O O   . TRP B 47  ? 1.6630 1.4594 1.5166 -0.0545 0.0009  -0.0064 47  TRP H O   
1682 C CB  . TRP B 47  ? 1.4796 1.2858 1.3198 -0.0516 0.0015  -0.0087 47  TRP H CB  
1683 C CG  . TRP B 47  ? 1.7029 1.5027 1.5398 -0.0507 -0.0018 -0.0052 47  TRP H CG  
1684 C CD1 . TRP B 47  ? 1.7923 1.5917 1.6257 -0.0488 -0.0037 -0.0028 47  TRP H CD1 
1685 C CD2 . TRP B 47  ? 1.7595 1.5525 1.5963 -0.0517 -0.0038 -0.0038 47  TRP H CD2 
1686 N NE1 . TRP B 47  ? 1.4953 1.2879 1.3265 -0.0483 -0.0067 -0.0005 47  TRP H NE1 
1687 C CE2 . TRP B 47  ? 1.5584 1.3471 1.3912 -0.0502 -0.0067 -0.0010 47  TRP H CE2 
1688 C CE3 . TRP B 47  ? 1.8935 1.6837 1.7335 -0.0539 -0.0037 -0.0045 47  TRP H CE3 
1689 C CZ2 . TRP B 47  ? 1.6828 1.4647 1.5138 -0.0509 -0.0092 0.0008  47  TRP H CZ2 
1690 C CZ3 . TRP B 47  ? 1.6955 1.4792 1.5338 -0.0549 -0.0063 -0.0022 47  TRP H CZ3 
1691 C CH2 . TRP B 47  ? 1.6700 1.4498 1.5036 -0.0534 -0.0089 0.0003  47  TRP H CH2 
1692 N N   . MET B 48  ? 1.6552 1.4518 1.5055 -0.0520 -0.0010 -0.0015 48  MET H N   
1693 C CA  . MET B 48  ? 1.2820 1.0712 1.1362 -0.0528 -0.0032 0.0019  48  MET H CA  
1694 C C   . MET B 48  ? 1.4471 1.2295 1.2964 -0.0526 -0.0067 0.0044  48  MET H C   
1695 O O   . MET B 48  ? 1.6834 1.4614 1.5333 -0.0541 -0.0077 0.0044  48  MET H O   
1696 C CB  . MET B 48  ? 1.3118 1.1017 1.1694 -0.0522 -0.0034 0.0049  48  MET H CB  
1697 C CG  . MET B 48  ? 1.3088 1.1050 1.1719 -0.0527 0.0002  0.0022  48  MET H CG  
1698 S SD  . MET B 48  ? 1.9050 1.6972 1.7759 -0.0547 0.0009  0.0001  48  MET H SD  
1699 C CE  . MET B 48  ? 1.8565 1.6400 1.7310 -0.0550 -0.0026 0.0061  48  MET H CE  
1700 N N   . GLY B 49  ? 1.4381 1.2198 1.2827 -0.0509 -0.0087 0.0066  49  GLY H N   
1701 C CA  . GLY B 49  ? 1.3978 1.1725 1.2383 -0.0506 -0.0122 0.0090  49  GLY H CA  
1702 C C   . GLY B 49  ? 1.4662 1.2419 1.3010 -0.0483 -0.0140 0.0095  49  GLY H C   
1703 O O   . GLY B 49  ? 1.6066 1.3872 1.4415 -0.0470 -0.0134 0.0098  49  GLY H O   
1704 N N   . TRP B 50  ? 1.3566 1.1277 1.1867 -0.0478 -0.0163 0.0096  50  TRP H N   
1705 C CA  . TRP B 50  ? 1.3519 1.1230 1.1771 -0.0454 -0.0183 0.0097  50  TRP H CA  
1706 C C   . TRP B 50  ? 1.4288 1.1917 1.2521 -0.0450 -0.0224 0.0127  50  TRP H C   
1707 O O   . TRP B 50  ? 1.5026 1.2606 1.3242 -0.0464 -0.0234 0.0126  50  TRP H O   
1708 C CB  . TRP B 50  ? 1.5217 1.2966 1.3424 -0.0447 -0.0169 0.0059  50  TRP H CB  
1709 C CG  . TRP B 50  ? 1.5391 1.3118 1.3552 -0.0424 -0.0196 0.0058  50  TRP H CG  
1710 C CD1 . TRP B 50  ? 1.4893 1.2644 1.3047 -0.0400 -0.0210 0.0063  50  TRP H CD1 
1711 C CD2 . TRP B 50  ? 1.6645 1.4324 1.4762 -0.0422 -0.0214 0.0049  50  TRP H CD2 
1712 N NE1 . TRP B 50  ? 1.5520 1.3238 1.3636 -0.0381 -0.0235 0.0055  50  TRP H NE1 
1713 C CE2 . TRP B 50  ? 1.5903 1.3578 1.3992 -0.0394 -0.0237 0.0044  50  TRP H CE2 
1714 C CE3 . TRP B 50  ? 1.7675 1.5317 1.5776 -0.0444 -0.0215 0.0046  50  TRP H CE3 
1715 C CZ2 . TRP B 50  ? 1.6354 1.3990 1.4398 -0.0383 -0.0256 0.0029  50  TRP H CZ2 
1716 C CZ3 . TRP B 50  ? 1.7362 1.4970 1.5412 -0.0437 -0.0234 0.0035  50  TRP H CZ3 
1717 C CH2 . TRP B 50  ? 1.7832 1.5437 1.5853 -0.0406 -0.0253 0.0024  50  TRP H CH2 
1718 N N   . ILE B 51  ? 1.5284 1.2897 1.3520 -0.0434 -0.0251 0.0155  51  ILE H N   
1719 C CA  . ILE B 51  ? 1.5065 1.2603 1.3278 -0.0425 -0.0295 0.0178  51  ILE H CA  
1720 C C   . ILE B 51  ? 1.5789 1.3343 1.3965 -0.0397 -0.0311 0.0162  51  ILE H C   
1721 O O   . ILE B 51  ? 1.5616 1.3235 1.3799 -0.0385 -0.0297 0.0153  51  ILE H O   
1722 C CB  . ILE B 51  ? 1.4022 1.1522 1.2278 -0.0429 -0.0320 0.0228  51  ILE H CB  
1723 C CG1 . ILE B 51  ? 1.3175 1.0589 1.1405 -0.0420 -0.0370 0.0253  51  ILE H CG1 
1724 C CG2 . ILE B 51  ? 1.4238 1.1799 1.2521 -0.0418 -0.0315 0.0243  51  ILE H CG2 
1725 C CD1 . ILE B 51  ? 1.5701 1.3054 1.3897 -0.0434 -0.0380 0.0243  51  ILE H CD1 
1726 N N   . SER B 52  ? 1.5264 1.2759 1.3400 -0.0387 -0.0341 0.0157  52  SER H N   
1727 C CA  . SER B 52  ? 1.4532 1.2026 1.2646 -0.0357 -0.0367 0.0146  52  SER H CA  
1728 C C   . SER B 52  ? 1.5299 1.2717 1.3420 -0.0350 -0.0417 0.0183  52  SER H C   
1729 O O   . SER B 52  ? 1.6616 1.3972 1.4739 -0.0367 -0.0432 0.0207  52  SER H O   
1730 C CB  . SER B 52  ? 1.3456 1.0954 1.1518 -0.0347 -0.0359 0.0100  52  SER H CB  
1731 O OG  . SER B 52  ? 1.4650 1.2081 1.2680 -0.0359 -0.0375 0.0099  52  SER H OG  
1732 N N   . ALA B 53  ? 1.3458 1.0878 1.1588 -0.0325 -0.0448 0.0192  53  ALA H N   
1733 C CA  . ALA B 53  ? 1.6153 1.3499 1.4291 -0.0316 -0.0502 0.0225  53  ALA H CA  
1734 C C   . ALA B 53  ? 1.8531 1.5832 1.6629 -0.0291 -0.0532 0.0192  53  ALA H C   
1735 O O   . ALA B 53  ? 1.9508 1.6735 1.7604 -0.0284 -0.0579 0.0211  53  ALA H O   
1736 C CB  . ALA B 53  ? 1.5886 1.3257 1.4073 -0.0309 -0.0525 0.0268  53  ALA H CB  
1737 N N   . TYR B 54  ? 1.8090 1.5438 1.6161 -0.0276 -0.0506 0.0142  54  TYR H N   
1738 C CA  . TYR B 54  ? 1.8324 1.5633 1.6349 -0.0258 -0.0522 0.0100  54  TYR H CA  
1739 C C   . TYR B 54  ? 2.0516 1.7758 1.8502 -0.0280 -0.0529 0.0101  54  TYR H C   
1740 O O   . TYR B 54  ? 2.6448 2.3618 2.4413 -0.0271 -0.0569 0.0100  54  TYR H O   
1741 C CB  . TYR B 54  ? 1.8785 1.6166 1.6787 -0.0247 -0.0482 0.0047  54  TYR H CB  
1742 C CG  . TYR B 54  ? 2.2135 1.9491 2.0090 -0.0230 -0.0490 -0.0002 54  TYR H CG  
1743 C CD1 . TYR B 54  ? 2.2536 1.9870 2.0498 -0.0195 -0.0526 -0.0023 54  TYR H CD1 
1744 C CD2 . TYR B 54  ? 2.5038 2.2391 2.2942 -0.0251 -0.0463 -0.0027 54  TYR H CD2 
1745 C CE1 . TYR B 54  ? 2.2186 1.9499 2.0105 -0.0178 -0.0531 -0.0074 54  TYR H CE1 
1746 C CE2 . TYR B 54  ? 2.5681 2.3018 2.3537 -0.0238 -0.0468 -0.0073 54  TYR H CE2 
1747 C CZ  . TYR B 54  ? 2.4236 2.1554 2.2098 -0.0200 -0.0500 -0.0100 54  TYR H CZ  
1748 O OH  . TYR B 54  ? 2.2330 1.9637 2.0145 -0.0186 -0.0501 -0.0152 54  TYR H OH  
1749 N N   . ASN B 55  ? 1.8230 1.5495 1.6209 -0.0311 -0.0491 0.0105  55  ASN H N   
1750 C CA  . ASN B 55  ? 1.9364 1.6572 1.7313 -0.0339 -0.0496 0.0115  55  ASN H CA  
1751 C C   . ASN B 55  ? 1.7521 1.4745 1.5510 -0.0370 -0.0472 0.0150  55  ASN H C   
1752 O O   . ASN B 55  ? 1.7838 1.5132 1.5858 -0.0371 -0.0438 0.0147  55  ASN H O   
1753 C CB  . ASN B 55  ? 2.1262 1.8487 1.9151 -0.0344 -0.0474 0.0066  55  ASN H CB  
1754 C CG  . ASN B 55  ? 2.5044 2.2205 2.2895 -0.0374 -0.0490 0.0076  55  ASN H CG  
1755 O OD1 . ASN B 55  ? 2.7541 2.4626 2.5396 -0.0378 -0.0531 0.0109  55  ASN H OD1 
1756 N ND2 . ASN B 55  ? 2.5983 2.3173 2.3796 -0.0397 -0.0461 0.0053  55  ASN H ND2 
1757 N N   . GLY B 56  ? 1.6672 1.3831 1.4662 -0.0396 -0.0492 0.0182  56  GLY H N   
1758 C CA  . GLY B 56  ? 1.6109 1.3277 1.4149 -0.0424 -0.0474 0.0217  56  GLY H CA  
1759 C C   . GLY B 56  ? 1.8029 1.5253 1.6070 -0.0445 -0.0427 0.0193  56  GLY H C   
1760 O O   . GLY B 56  ? 1.7096 1.4306 1.5167 -0.0475 -0.0419 0.0216  56  GLY H O   
1761 N N   . ASN B 57  ? 1.8933 1.6221 1.6948 -0.0431 -0.0399 0.0149  57  ASN H N   
1762 C CA  . ASN B 57  ? 1.9835 1.7175 1.7845 -0.0451 -0.0359 0.0125  57  ASN H CA  
1763 C C   . ASN B 57  ? 1.7930 1.5318 1.6002 -0.0461 -0.0330 0.0137  57  ASN H C   
1764 O O   . ASN B 57  ? 2.0625 1.8066 1.8717 -0.0441 -0.0315 0.0129  57  ASN H O   
1765 C CB  . ASN B 57  ? 2.1473 1.8870 1.9440 -0.0431 -0.0339 0.0077  57  ASN H CB  
1766 C CG  . ASN B 57  ? 2.2314 1.9672 2.0217 -0.0425 -0.0361 0.0056  57  ASN H CG  
1767 O OD1 . ASN B 57  ? 2.5482 2.2776 2.3366 -0.0445 -0.0386 0.0075  57  ASN H OD1 
1768 N ND2 . ASN B 57  ? 2.2367 1.9766 2.0240 -0.0398 -0.0352 0.0014  57  ASN H ND2 
1769 N N   . THR B 58  ? 1.6960 1.4331 1.5064 -0.0492 -0.0322 0.0156  58  THR H N   
1770 C CA  . THR B 58  ? 1.5100 1.2514 1.3270 -0.0502 -0.0294 0.0162  58  THR H CA  
1771 C C   . THR B 58  ? 1.5885 1.3345 1.4058 -0.0522 -0.0262 0.0134  58  THR H C   
1772 O O   . THR B 58  ? 1.7363 1.4800 1.5504 -0.0542 -0.0269 0.0130  58  THR H O   
1773 C CB  . THR B 58  ? 1.4183 1.1543 1.2408 -0.0522 -0.0311 0.0206  58  THR H CB  
1774 O OG1 . THR B 58  ? 1.8054 1.5361 1.6268 -0.0551 -0.0328 0.0218  58  THR H OG1 
1775 C CG2 . THR B 58  ? 1.6983 1.4298 1.5210 -0.0505 -0.0345 0.0239  58  THR H CG2 
1776 N N   . ASN B 59  ? 1.4943 1.2468 1.3152 -0.0518 -0.0229 0.0116  59  ASN H N   
1777 C CA  . ASN B 59  ? 1.2452 1.0016 1.0683 -0.0540 -0.0201 0.0095  59  ASN H CA  
1778 C C   . ASN B 59  ? 1.6201 1.3791 1.4506 -0.0546 -0.0181 0.0099  59  ASN H C   
1779 O O   . ASN B 59  ? 1.9741 1.7382 1.8057 -0.0527 -0.0163 0.0087  59  ASN H O   
1780 C CB  . ASN B 59  ? 1.5244 1.2874 1.3434 -0.0528 -0.0178 0.0055  59  ASN H CB  
1781 C CG  . ASN B 59  ? 1.9137 1.6812 1.7356 -0.0550 -0.0151 0.0034  59  ASN H CG  
1782 O OD1 . ASN B 59  ? 1.9544 1.7191 1.7799 -0.0579 -0.0156 0.0047  59  ASN H OD1 
1783 N ND2 . ASN B 59  ? 1.9803 1.7547 1.8011 -0.0538 -0.0125 0.0002  59  ASN H ND2 
1784 N N   . TYR B 60  ? 1.4805 1.2363 1.3164 -0.0572 -0.0185 0.0115  60  TYR H N   
1785 C CA  . TYR B 60  ? 1.6536 1.4114 1.4975 -0.0579 -0.0166 0.0115  60  TYR H CA  
1786 C C   . TYR B 60  ? 1.6892 1.4513 1.5361 -0.0596 -0.0141 0.0082  60  TYR H C   
1787 O O   . TYR B 60  ? 1.7612 1.5224 1.6058 -0.0614 -0.0148 0.0077  60  TYR H O   
1788 C CB  . TYR B 60  ? 1.6850 1.4361 1.5345 -0.0597 -0.0190 0.0155  60  TYR H CB  
1789 C CG  . TYR B 60  ? 1.4644 1.2108 1.3120 -0.0583 -0.0218 0.0192  60  TYR H CG  
1790 C CD1 . TYR B 60  ? 1.6331 1.3829 1.4809 -0.0558 -0.0210 0.0195  60  TYR H CD1 
1791 C CD2 . TYR B 60  ? 1.4832 1.2219 1.3287 -0.0597 -0.0256 0.0226  60  TYR H CD2 
1792 C CE1 . TYR B 60  ? 1.7307 1.4763 1.5773 -0.0547 -0.0240 0.0231  60  TYR H CE1 
1793 C CE2 . TYR B 60  ? 1.6703 1.4044 1.5142 -0.0584 -0.0286 0.0260  60  TYR H CE2 
1794 C CZ  . TYR B 60  ? 1.5891 1.3266 1.4338 -0.0559 -0.0278 0.0263  60  TYR H CZ  
1795 O OH  . TYR B 60  ? 1.3154 1.0483 1.1591 -0.0548 -0.0312 0.0300  60  TYR H OH  
1796 N N   . ALA B 61  ? 1.4647 1.2319 1.3167 -0.0591 -0.0112 0.0060  61  ALA H N   
1797 C CA  . ALA B 61  ? 1.5110 1.2822 1.3668 -0.0606 -0.0090 0.0026  61  ALA H CA  
1798 C C   . ALA B 61  ? 1.7693 1.5354 1.6314 -0.0636 -0.0107 0.0044  61  ALA H C   
1799 O O   . ALA B 61  ? 1.9371 1.6981 1.8036 -0.0644 -0.0126 0.0076  61  ALA H O   
1800 C CB  . ALA B 61  ? 1.3252 1.1025 1.1855 -0.0594 -0.0057 -0.0003 61  ALA H CB  
1810 N N   . LYS B 63  ? 1.5662 1.3339 1.4498 -0.0678 -0.0088 0.0003  63  LYS H N   
1811 C CA  . LYS B 63  ? 1.6337 1.4012 1.5279 -0.0679 -0.0077 -0.0006 63  LYS H CA  
1812 C C   . LYS B 63  ? 1.6624 1.4263 1.5587 -0.0669 -0.0086 0.0029  63  LYS H C   
1813 O O   . LYS B 63  ? 1.7514 1.5137 1.6574 -0.0674 -0.0085 0.0032  63  LYS H O   
1814 C CB  . LYS B 63  ? 1.4999 1.2750 1.3956 -0.0661 -0.0037 -0.0061 63  LYS H CB  
1815 C CG  . LYS B 63  ? 1.5369 1.3155 1.4329 -0.0673 -0.0029 -0.0099 63  LYS H CG  
1816 C CD  . LYS B 63  ? 1.5677 1.3538 1.4645 -0.0655 0.0010  -0.0153 63  LYS H CD  
1817 C CE  . LYS B 63  ? 1.7260 1.5154 1.6235 -0.0668 0.0015  -0.0191 63  LYS H CE  
1818 N NZ  . LYS B 63  ? 1.2157 1.0123 1.1133 -0.0653 0.0052  -0.0245 63  LYS H NZ  
1819 N N   . LEU B 64  ? 2.0392 1.8018 1.9273 -0.0655 -0.0097 0.0055  64  LEU H N   
1820 C CA  . LEU B 64  ? 1.9562 1.7165 1.8455 -0.0642 -0.0104 0.0088  64  LEU H CA  
1821 C C   . LEU B 64  ? 1.9930 1.7470 1.8754 -0.0645 -0.0141 0.0133  64  LEU H C   
1822 O O   . LEU B 64  ? 2.0871 1.8409 1.9649 -0.0626 -0.0146 0.0151  64  LEU H O   
1823 C CB  . LEU B 64  ? 1.7434 1.5106 1.6303 -0.0614 -0.0071 0.0064  64  LEU H CB  
1824 C CG  . LEU B 64  ? 2.0211 1.7945 1.9152 -0.0612 -0.0034 0.0017  64  LEU H CG  
1825 C CD1 . LEU B 64  ? 1.8358 1.6169 1.7260 -0.0590 -0.0002 -0.0008 64  LEU H CD1 
1826 C CD2 . LEU B 64  ? 1.9313 1.7020 1.8364 -0.0619 -0.0035 0.0030  64  LEU H CD2 
1827 N N   . GLN B 65  ? 1.7389 1.4879 1.6206 -0.0671 -0.0169 0.0153  65  GLN H N   
1828 C CA  . GLN B 65  ? 1.7339 1.4770 1.6088 -0.0677 -0.0204 0.0192  65  GLN H CA  
1829 C C   . GLN B 65  ? 1.8372 1.5742 1.7168 -0.0682 -0.0230 0.0239  65  GLN H C   
1830 O O   . GLN B 65  ? 1.9347 1.6692 1.8094 -0.0667 -0.0246 0.0263  65  GLN H O   
1831 C CB  . GLN B 65  ? 1.6645 1.4049 1.5367 -0.0708 -0.0226 0.0199  65  GLN H CB  
1832 C CG  . GLN B 65  ? 1.8301 1.5762 1.6961 -0.0704 -0.0206 0.0160  65  GLN H CG  
1833 C CD  . GLN B 65  ? 1.9521 1.6963 1.8161 -0.0739 -0.0227 0.0171  65  GLN H CD  
1834 O OE1 . GLN B 65  ? 1.9848 1.7245 1.8545 -0.0771 -0.0253 0.0202  65  GLN H OE1 
1835 N NE2 . GLN B 65  ? 2.0262 1.7743 1.8823 -0.0734 -0.0218 0.0149  65  GLN H NE2 
1836 N N   . GLY B 66  ? 1.9794 1.7139 1.8690 -0.0703 -0.0237 0.0253  66  GLY H N   
1837 C CA  . GLY B 66  ? 2.0836 1.8118 1.9784 -0.0713 -0.0266 0.0303  66  GLY H CA  
1838 C C   . GLY B 66  ? 2.0275 1.7573 1.9236 -0.0685 -0.0255 0.0314  66  GLY H C   
1839 O O   . GLY B 66  ? 2.1973 1.9225 2.0895 -0.0681 -0.0283 0.0353  66  GLY H O   
1840 N N   . ARG B 67  ? 1.9926 1.7292 1.8938 -0.0667 -0.0215 0.0279  67  ARG H N   
1841 C CA  . ARG B 67  ? 1.8785 1.6175 1.7830 -0.0647 -0.0202 0.0293  67  ARG H CA  
1842 C C   . ARG B 67  ? 1.9030 1.6438 1.7980 -0.0624 -0.0206 0.0301  67  ARG H C   
1843 O O   . ARG B 67  ? 1.8212 1.5609 1.7172 -0.0614 -0.0217 0.0336  67  ARG H O   
1844 C CB  . ARG B 67  ? 1.9004 1.6471 1.8123 -0.0636 -0.0156 0.0248  67  ARG H CB  
1845 C CG  . ARG B 67  ? 2.0166 1.7612 1.9404 -0.0655 -0.0156 0.0244  67  ARG H CG  
1846 C CD  . ARG B 67  ? 2.0955 1.8478 2.0267 -0.0642 -0.0109 0.0193  67  ARG H CD  
1847 N NE  . ARG B 67  ? 2.3330 2.0828 2.2768 -0.0659 -0.0114 0.0188  67  ARG H NE  
1848 C CZ  . ARG B 67  ? 2.2225 1.9776 2.1753 -0.0653 -0.0079 0.0140  67  ARG H CZ  
1849 N NH1 . ARG B 67  ? 2.3556 2.1192 2.3057 -0.0632 -0.0035 0.0089  67  ARG H NH1 
1850 N NH2 . ARG B 67  ? 2.3454 2.0971 2.3106 -0.0668 -0.0090 0.0142  67  ARG H NH2 
1851 N N   . VAL B 68  ? 1.9931 1.7367 1.8795 -0.0615 -0.0197 0.0271  68  VAL H N   
1852 C CA  . VAL B 68  ? 1.8513 1.5982 1.7300 -0.0590 -0.0195 0.0268  68  VAL H CA  
1853 C C   . VAL B 68  ? 1.8979 1.6377 1.7701 -0.0589 -0.0240 0.0308  68  VAL H C   
1854 O O   . VAL B 68  ? 2.0070 1.7418 1.8754 -0.0605 -0.0262 0.0310  68  VAL H O   
1855 C CB  . VAL B 68  ? 1.9890 1.7421 1.8620 -0.0581 -0.0167 0.0218  68  VAL H CB  
1856 C CG1 . VAL B 68  ? 1.9276 1.6839 1.7933 -0.0556 -0.0169 0.0219  68  VAL H CG1 
1857 C CG2 . VAL B 68  ? 2.1572 1.9171 2.0362 -0.0583 -0.0125 0.0174  68  VAL H CG2 
1858 N N   . THR B 69  ? 1.8202 1.5598 1.6907 -0.0572 -0.0254 0.0336  69  THR H N   
1859 C CA  . THR B 69  ? 1.7591 1.4930 1.6225 -0.0565 -0.0296 0.0362  69  THR H CA  
1860 C C   . THR B 69  ? 1.7968 1.5353 1.6561 -0.0538 -0.0294 0.0361  69  THR H C   
1861 O O   . THR B 69  ? 1.7203 1.4635 1.5839 -0.0531 -0.0281 0.0374  69  THR H O   
1862 C CB  . THR B 69  ? 1.6084 1.3343 1.4749 -0.0577 -0.0337 0.0418  69  THR H CB  
1863 O OG1 . THR B 69  ? 2.0424 1.7709 1.9162 -0.0573 -0.0328 0.0445  69  THR H OG1 
1864 C CG2 . THR B 69  ? 1.1919 0.9120 1.0609 -0.0607 -0.0351 0.0427  69  THR H CG2 
1865 N N   . MET B 70  ? 1.6804 1.4176 1.5319 -0.0526 -0.0311 0.0346  70  MET H N   
1866 C CA  . MET B 70  ? 1.3926 1.1338 1.2402 -0.0501 -0.0314 0.0342  70  MET H CA  
1867 C C   . MET B 70  ? 1.2075 0.9416 1.0513 -0.0491 -0.0366 0.0374  70  MET H C   
1868 O O   . MET B 70  ? 1.3865 1.1136 1.2271 -0.0500 -0.0391 0.0378  70  MET H O   
1869 C CB  . MET B 70  ? 1.3005 1.0468 1.1429 -0.0491 -0.0289 0.0291  70  MET H CB  
1870 C CG  . MET B 70  ? 1.1463 0.9001 0.9922 -0.0499 -0.0241 0.0257  70  MET H CG  
1871 S SD  . MET B 70  ? 1.5323 1.2922 1.3729 -0.0491 -0.0211 0.0200  70  MET H SD  
1872 C CE  . MET B 70  ? 1.6690 1.4340 1.5063 -0.0465 -0.0219 0.0202  70  MET H CE  
1873 N N   . THR B 71  ? 1.3009 1.0368 1.1450 -0.0475 -0.0383 0.0399  71  THR H N   
1874 C CA  . THR B 71  ? 1.3831 1.1124 1.2239 -0.0462 -0.0435 0.0427  71  THR H CA  
1875 C C   . THR B 71  ? 1.4623 1.1965 1.3009 -0.0438 -0.0443 0.0420  71  THR H C   
1876 O O   . THR B 71  ? 1.3526 1.0950 1.1933 -0.0435 -0.0413 0.0412  71  THR H O   
1877 C CB  . THR B 71  ? 1.4074 1.1315 1.2531 -0.0472 -0.0470 0.0487  71  THR H CB  
1878 O OG1 . THR B 71  ? 1.6555 1.3864 1.5067 -0.0472 -0.0451 0.0510  71  THR H OG1 
1879 C CG2 . THR B 71  ? 1.4875 1.2061 1.3359 -0.0498 -0.0469 0.0498  71  THR H CG2 
1880 N N   . THR B 72  ? 1.3981 1.1270 1.2326 -0.0422 -0.0486 0.0422  72  THR H N   
1881 C CA  . THR B 72  ? 1.2031 0.9348 1.0366 -0.0399 -0.0508 0.0426  72  THR H CA  
1882 C C   . THR B 72  ? 1.2645 0.9889 1.0988 -0.0391 -0.0569 0.0472  72  THR H C   
1883 O O   . THR B 72  ? 1.2388 0.9548 1.0709 -0.0395 -0.0600 0.0476  72  THR H O   
1884 C CB  . THR B 72  ? 1.3099 1.0434 1.1381 -0.0380 -0.0500 0.0374  72  THR H CB  
1885 O OG1 . THR B 72  ? 1.5632 1.2890 1.3868 -0.0378 -0.0521 0.0354  72  THR H OG1 
1886 C CG2 . THR B 72  ? 1.4915 1.2333 1.3194 -0.0385 -0.0443 0.0333  72  THR H CG2 
1887 N N   . ASP B 73  ? 1.3354 1.0635 1.1729 -0.0383 -0.0590 0.0506  73  ASP H N   
1888 C CA  . ASP B 73  ? 1.3106 1.0330 1.1494 -0.0373 -0.0653 0.0550  73  ASP H CA  
1889 C C   . ASP B 73  ? 1.3844 1.1093 1.2214 -0.0348 -0.0674 0.0528  73  ASP H C   
1890 O O   . ASP B 73  ? 1.6031 1.3360 1.4425 -0.0346 -0.0662 0.0539  73  ASP H O   
1891 C CB  . ASP B 73  ? 1.4775 1.2025 1.3224 -0.0388 -0.0665 0.0614  73  ASP H CB  
1892 C CG  . ASP B 73  ? 1.5454 1.2641 1.3922 -0.0381 -0.0735 0.0666  73  ASP H CG  
1893 O OD1 . ASP B 73  ? 1.4076 1.1180 1.2509 -0.0367 -0.0776 0.0650  73  ASP H OD1 
1894 O OD2 . ASP B 73  ? 1.6881 1.4102 1.5399 -0.0391 -0.0751 0.0722  73  ASP H OD2 
1895 N N   . THR B 74  ? 1.1296 0.8478 0.9625 -0.0329 -0.0704 0.0497  74  THR H N   
1896 C CA  . THR B 74  ? 1.2933 1.0132 1.1253 -0.0302 -0.0727 0.0474  74  THR H CA  
1897 C C   . THR B 74  ? 1.5391 1.2585 1.3759 -0.0296 -0.0784 0.0530  74  THR H C   
1898 O O   . THR B 74  ? 1.6616 1.3864 1.5004 -0.0283 -0.0793 0.0530  74  THR H O   
1899 C CB  . THR B 74  ? 1.5629 1.2756 1.3898 -0.0283 -0.0747 0.0426  74  THR H CB  
1900 O OG1 . THR B 74  ? 1.6363 1.3393 1.4635 -0.0284 -0.0802 0.0457  74  THR H OG1 
1901 C CG2 . THR B 74  ? 1.6149 1.3284 1.4371 -0.0294 -0.0695 0.0377  74  THR H CG2 
1902 N N   . SER B 75  ? 1.6589 1.3719 1.4982 -0.0306 -0.0825 0.0581  75  SER H N   
1903 C CA  . SER B 75  ? 1.6953 1.4072 1.5396 -0.0303 -0.0885 0.0642  75  SER H CA  
1904 C C   . SER B 75  ? 1.7771 1.4999 1.6256 -0.0317 -0.0864 0.0677  75  SER H C   
1905 O O   . SER B 75  ? 1.7706 1.4972 1.6213 -0.0306 -0.0891 0.0689  75  SER H O   
1906 C CB  . SER B 75  ? 1.5388 1.2429 1.3851 -0.0318 -0.0925 0.0694  75  SER H CB  
1907 O OG  . SER B 75  ? 1.7565 1.4650 1.6052 -0.0346 -0.0883 0.0725  75  SER H OG  
1908 N N   . THR B 76  ? 1.7676 1.4956 1.6175 -0.0342 -0.0817 0.0695  76  THR H N   
1909 C CA  . THR B 76  ? 1.6263 1.3655 1.4794 -0.0357 -0.0787 0.0721  76  THR H CA  
1910 C C   . THR B 76  ? 1.6725 1.4195 1.5224 -0.0353 -0.0730 0.0662  76  THR H C   
1911 O O   . THR B 76  ? 1.6587 1.4155 1.5105 -0.0364 -0.0707 0.0676  76  THR H O   
1912 C CB  . THR B 76  ? 1.5866 1.3288 1.4429 -0.0384 -0.0757 0.0758  76  THR H CB  
1913 O OG1 . THR B 76  ? 1.6142 1.3541 1.4678 -0.0389 -0.0708 0.0714  76  THR H OG1 
1914 C CG2 . THR B 76  ? 1.7109 1.4464 1.5710 -0.0391 -0.0816 0.0826  76  THR H CG2 
1915 N N   . SER B 77  ? 1.7404 1.4836 1.5856 -0.0339 -0.0707 0.0599  77  SER H N   
1916 C CA  . SER B 77  ? 1.6415 1.3914 1.4836 -0.0335 -0.0652 0.0542  77  SER H CA  
1917 C C   . SER B 77  ? 1.8126 1.5704 1.6560 -0.0360 -0.0592 0.0542  77  SER H C   
1918 O O   . SER B 77  ? 2.0689 1.8359 1.9124 -0.0365 -0.0560 0.0529  77  SER H O   
1919 C CB  . SER B 77  ? 1.7833 1.5384 1.6259 -0.0320 -0.0670 0.0536  77  SER H CB  
1920 O OG  . SER B 77  ? 2.2089 1.9726 2.0552 -0.0339 -0.0668 0.0581  77  SER H OG  
1921 N N   . THR B 78  ? 1.6494 1.4037 1.4941 -0.0375 -0.0579 0.0557  78  THR H N   
1922 C CA  . THR B 78  ? 1.4783 1.2393 1.3252 -0.0397 -0.0524 0.0555  78  THR H CA  
1923 C C   . THR B 78  ? 1.4699 1.2272 1.3147 -0.0401 -0.0487 0.0509  78  THR H C   
1924 O O   . THR B 78  ? 1.5733 1.3216 1.4170 -0.0399 -0.0511 0.0513  78  THR H O   
1925 C CB  . THR B 78  ? 1.6461 1.4076 1.4983 -0.0413 -0.0540 0.0618  78  THR H CB  
1926 O OG1 . THR B 78  ? 1.8607 1.6234 1.7148 -0.0409 -0.0591 0.0668  78  THR H OG1 
1927 C CG2 . THR B 78  ? 1.7866 1.5575 1.6417 -0.0433 -0.0482 0.0613  78  THR H CG2 
1928 N N   . ALA B 79  ? 1.4543 1.2185 1.2984 -0.0408 -0.0431 0.0467  79  ALA H N   
1929 C CA  . ALA B 79  ? 1.5754 1.3371 1.4185 -0.0417 -0.0395 0.0428  79  ALA H CA  
1930 C C   . ALA B 79  ? 1.6847 1.4493 1.5332 -0.0437 -0.0365 0.0445  79  ALA H C   
1931 O O   . ALA B 79  ? 1.8303 1.6019 1.6821 -0.0444 -0.0353 0.0468  79  ALA H O   
1932 C CB  . ALA B 79  ? 1.5764 1.3434 1.4160 -0.0412 -0.0356 0.0370  79  ALA H CB  
1933 N N   . TYR B 80  ? 1.3672 1.1267 1.2168 -0.0448 -0.0353 0.0433  80  TYR H N   
1934 C CA  . TYR B 80  ? 1.2938 1.0546 1.1495 -0.0465 -0.0329 0.0448  80  TYR H CA  
1935 C C   . TYR B 80  ? 1.4331 1.1931 1.2896 -0.0477 -0.0293 0.0405  80  TYR H C   
1936 O O   . TYR B 80  ? 1.4426 1.1965 1.2957 -0.0477 -0.0305 0.0387  80  TYR H O   
1937 C CB  . TYR B 80  ? 1.5191 1.2725 1.3782 -0.0471 -0.0371 0.0505  80  TYR H CB  
1938 C CG  . TYR B 80  ? 1.4713 1.2226 1.3294 -0.0461 -0.0422 0.0552  80  TYR H CG  
1939 C CD1 . TYR B 80  ? 1.7226 1.4663 1.5759 -0.0447 -0.0468 0.0555  80  TYR H CD1 
1940 C CD2 . TYR B 80  ? 1.3241 1.0814 1.1863 -0.0465 -0.0425 0.0595  80  TYR H CD2 
1941 C CE1 . TYR B 80  ? 1.7660 1.5073 1.6191 -0.0437 -0.0519 0.0597  80  TYR H CE1 
1942 C CE2 . TYR B 80  ? 1.4501 1.2056 1.3121 -0.0457 -0.0477 0.0643  80  TYR H CE2 
1943 C CZ  . TYR B 80  ? 1.6911 1.4381 1.5487 -0.0442 -0.0526 0.0643  80  TYR H CZ  
1944 O OH  . TYR B 80  ? 1.8439 1.5886 1.7019 -0.0434 -0.0582 0.0689  80  TYR H OH  
1945 N N   . MET B 81  ? 1.5175 1.2840 1.3790 -0.0487 -0.0249 0.0388  81  MET H N   
1946 C CA  . MET B 81  ? 1.4066 1.1727 1.2715 -0.0500 -0.0217 0.0353  81  MET H CA  
1947 C C   . MET B 81  ? 1.6023 1.3659 1.4750 -0.0513 -0.0217 0.0384  81  MET H C   
1948 O O   . MET B 81  ? 1.8253 1.5930 1.7021 -0.0513 -0.0213 0.0413  81  MET H O   
1949 C CB  . MET B 81  ? 1.1800 0.9554 1.0458 -0.0502 -0.0166 0.0304  81  MET H CB  
1950 C CG  . MET B 81  ? 1.5116 1.2902 1.3708 -0.0492 -0.0158 0.0268  81  MET H CG  
1951 S SD  . MET B 81  ? 1.5745 1.3466 1.4282 -0.0491 -0.0173 0.0241  81  MET H SD  
1952 C CE  . MET B 81  ? 1.5450 1.3177 1.4043 -0.0510 -0.0137 0.0206  81  MET H CE  
1953 N N   . GLU B 82  ? 1.4932 1.2509 1.3686 -0.0527 -0.0220 0.0377  82  GLU H N   
1954 C CA  . GLU B 82  ? 1.6471 1.4025 1.5311 -0.0540 -0.0218 0.0402  82  GLU H CA  
1955 C C   . GLU B 82  ? 1.8380 1.5933 1.7262 -0.0554 -0.0191 0.0362  82  GLU H C   
1956 O O   . GLU B 82  ? 1.9916 1.7414 1.8767 -0.0563 -0.0208 0.0352  82  GLU H O   
1957 C CB  . GLU B 82  ? 1.8524 1.5980 1.7364 -0.0547 -0.0271 0.0459  82  GLU H CB  
1958 C CG  . GLU B 82  ? 2.0022 1.7483 1.8862 -0.0538 -0.0297 0.0509  82  GLU H CG  
1959 C CD  . GLU B 82  ? 2.0861 1.8306 1.9615 -0.0522 -0.0327 0.0513  82  GLU H CD  
1960 O OE1 . GLU B 82  ? 2.0553 1.7993 1.9247 -0.0517 -0.0322 0.0472  82  GLU H OE1 
1961 O OE2 . GLU B 82  ? 1.9438 1.6876 1.8189 -0.0515 -0.0359 0.0557  82  GLU H OE2 
1962 N N   . LEU B 83  ? 1.9775 1.7393 1.8728 -0.0555 -0.0151 0.0337  83  LEU H N   
1963 C CA  . LEU B 83  ? 1.9150 1.6769 1.8166 -0.0568 -0.0127 0.0299  83  LEU H CA  
1964 C C   . LEU B 83  ? 1.7966 1.5547 1.7083 -0.0579 -0.0136 0.0332  83  LEU H C   
1965 O O   . LEU B 83  ? 1.6482 1.4105 1.5651 -0.0574 -0.0122 0.0348  83  LEU H O   
1966 C CB  . LEU B 83  ? 1.5657 1.3375 1.4689 -0.0561 -0.0075 0.0240  83  LEU H CB  
1967 C CG  . LEU B 83  ? 1.7626 1.5395 1.6571 -0.0551 -0.0059 0.0202  83  LEU H CG  
1968 C CD1 . LEU B 83  ? 1.7998 1.5869 1.6969 -0.0547 -0.0009 0.0150  83  LEU H CD1 
1969 C CD2 . LEU B 83  ? 1.8716 1.6436 1.7620 -0.0559 -0.0074 0.0183  83  LEU H CD2 
1970 N N   . ARG B 84  ? 1.7014 1.4519 1.6163 -0.0598 -0.0161 0.0344  84  ARG H N   
1971 C CA  . ARG B 84  ? 1.8012 1.5466 1.7250 -0.0610 -0.0182 0.0389  84  ARG H CA  
1972 C C   . ARG B 84  ? 1.9439 1.6941 1.8797 -0.0611 -0.0146 0.0359  84  ARG H C   
1973 O O   . ARG B 84  ? 2.0508 1.8070 1.9914 -0.0600 -0.0120 0.0361  84  ARG H O   
1974 C CB  . ARG B 84  ? 1.9572 1.6924 1.8799 -0.0632 -0.0230 0.0423  84  ARG H CB  
1975 C CG  . ARG B 84  ? 1.8696 1.5992 1.7832 -0.0629 -0.0273 0.0467  84  ARG H CG  
1976 C CD  . ARG B 84  ? 1.8078 1.5276 1.7194 -0.0654 -0.0320 0.0500  84  ARG H CD  
1977 N NE  . ARG B 84  ? 1.7517 1.4709 1.6610 -0.0669 -0.0315 0.0465  84  ARG H NE  
1978 C CZ  . ARG B 84  ? 1.9721 1.6899 1.8712 -0.0670 -0.0326 0.0450  84  ARG H CZ  
1979 N NH1 . ARG B 84  ? 2.0595 1.7773 1.9497 -0.0651 -0.0338 0.0455  84  ARG H NH1 
1980 N NH2 . ARG B 84  ? 2.1270 1.8436 2.0254 -0.0691 -0.0328 0.0431  84  ARG H NH2 
1981 N N   . SER B 85  ? 1.6708 1.4187 1.6118 -0.0626 -0.0142 0.0331  85  SER H N   
1982 C CA  . SER B 85  ? 1.6256 1.3779 1.5789 -0.0626 -0.0109 0.0296  85  SER H CA  
1983 C C   . SER B 85  ? 1.8094 1.5714 1.7604 -0.0609 -0.0058 0.0226  85  SER H C   
1984 O O   . SER B 85  ? 2.0912 1.8539 2.0368 -0.0612 -0.0053 0.0189  85  SER H O   
1985 C CB  . SER B 85  ? 2.0059 1.7516 1.9670 -0.0650 -0.0133 0.0298  85  SER H CB  
1986 O OG  . SER B 85  ? 2.2983 2.0424 2.2529 -0.0660 -0.0141 0.0272  85  SER H OG  
1987 N N   . LEU B 86  ? 1.7875 1.5574 1.7422 -0.0594 -0.0020 0.0210  86  LEU H N   
1988 C CA  . LEU B 86  ? 1.8052 1.5850 1.7571 -0.0581 0.0028  0.0145  86  LEU H CA  
1989 C C   . LEU B 86  ? 1.9953 1.7788 1.9583 -0.0581 0.0062  0.0084  86  LEU H C   
1990 O O   . LEU B 86  ? 2.0632 1.8434 2.0377 -0.0588 0.0056  0.0094  86  LEU H O   
1991 C CB  . LEU B 86  ? 1.6381 1.4258 1.5868 -0.0567 0.0051  0.0158  86  LEU H CB  
1992 C CG  . LEU B 86  ? 1.4844 1.2701 1.4219 -0.0564 0.0020  0.0209  86  LEU H CG  
1993 C CD1 . LEU B 86  ? 1.4409 1.2348 1.3777 -0.0555 0.0040  0.0228  86  LEU H CD1 
1994 C CD2 . LEU B 86  ? 1.8405 1.6267 1.7676 -0.0561 0.0019  0.0178  86  LEU H CD2 
1995 N N   . ARG B 87  ? 1.8886 1.6790 1.8481 -0.0574 0.0098  0.0020  87  ARG H N   
1996 C CA  . ARG B 87  ? 1.7567 1.5511 1.7254 -0.0573 0.0131  -0.0049 87  ARG H CA  
1997 C C   . ARG B 87  ? 1.8166 1.6224 1.7820 -0.0559 0.0183  -0.0107 87  ARG H C   
1998 O O   . ARG B 87  ? 1.9328 1.7427 1.8872 -0.0555 0.0188  -0.0098 87  ARG H O   
1999 C CB  . ARG B 87  ? 1.5902 1.3794 1.5583 -0.0586 0.0111  -0.0075 87  ARG H CB  
2000 C CG  . ARG B 87  ? 1.8208 1.5996 1.7946 -0.0605 0.0062  -0.0027 87  ARG H CG  
2001 C CD  . ARG B 87  ? 1.9893 1.7643 1.9622 -0.0621 0.0043  -0.0049 87  ARG H CD  
2002 N NE  . ARG B 87  ? 2.5101 2.2757 2.4884 -0.0645 -0.0006 0.0001  87  ARG H NE  
2003 C CZ  . ARG B 87  ? 2.7745 2.5351 2.7518 -0.0667 -0.0037 0.0006  87  ARG H CZ  
2004 N NH1 . ARG B 87  ? 2.7547 2.5183 2.7243 -0.0667 -0.0028 -0.0029 87  ARG H NH1 
2005 N NH2 . ARG B 87  ? 2.9050 2.6579 2.8894 -0.0691 -0.0080 0.0051  87  ARG H NH2 
2006 N N   . SER B 88  ? 1.8009 1.6119 1.7762 -0.0554 0.0220  -0.0168 88  SER H N   
2007 C CA  . SER B 88  ? 1.8448 1.6670 1.8174 -0.0544 0.0272  -0.0232 88  SER H CA  
2008 C C   . SER B 88  ? 1.8556 1.6795 1.8178 -0.0547 0.0273  -0.0265 88  SER H C   
2009 O O   . SER B 88  ? 1.9277 1.7597 1.8817 -0.0543 0.0299  -0.0285 88  SER H O   
2010 C CB  . SER B 88  ? 1.8441 1.6705 1.8300 -0.0538 0.0308  -0.0300 88  SER H CB  
2011 O OG  . SER B 88  ? 1.9219 1.7484 1.9177 -0.0533 0.0312  -0.0271 88  SER H OG  
2012 N N   . ASP B 89  ? 1.7358 1.5522 1.6982 -0.0557 0.0242  -0.0268 89  ASP H N   
2013 C CA  . ASP B 89  ? 1.7526 1.5700 1.7053 -0.0561 0.0239  -0.0292 89  ASP H CA  
2014 C C   . ASP B 89  ? 1.6482 1.4655 1.5880 -0.0559 0.0222  -0.0240 89  ASP H C   
2015 O O   . ASP B 89  ? 1.3365 1.1584 1.2673 -0.0558 0.0232  -0.0262 89  ASP H O   
2016 C CB  . ASP B 89  ? 1.4324 1.2416 1.3885 -0.0574 0.0205  -0.0294 89  ASP H CB  
2017 C CG  . ASP B 89  ? 1.6492 1.4593 1.6177 -0.0576 0.0221  -0.0357 89  ASP H CG  
2018 O OD1 . ASP B 89  ? 1.8291 1.6470 1.8015 -0.0564 0.0264  -0.0414 89  ASP H OD1 
2019 O OD2 . ASP B 89  ? 1.7918 1.5948 1.7663 -0.0589 0.0189  -0.0351 89  ASP H OD2 
2020 N N   . ASP B 90  ? 1.8172 1.6293 1.7563 -0.0560 0.0192  -0.0171 90  ASP H N   
2021 C CA  . ASP B 90  ? 1.7341 1.5452 1.6620 -0.0557 0.0170  -0.0120 90  ASP H CA  
2022 C C   . ASP B 90  ? 1.7237 1.5441 1.6469 -0.0549 0.0197  -0.0118 90  ASP H C   
2023 O O   . ASP B 90  ? 1.8468 1.6671 1.7612 -0.0546 0.0178  -0.0078 90  ASP H O   
2024 C CB  . ASP B 90  ? 1.6512 1.4533 1.5802 -0.0561 0.0126  -0.0048 90  ASP H CB  
2025 C CG  . ASP B 90  ? 1.7518 1.5448 1.6817 -0.0575 0.0091  -0.0036 90  ASP H CG  
2026 O OD1 . ASP B 90  ? 1.9188 1.7125 1.8464 -0.0579 0.0096  -0.0077 90  ASP H OD1 
2027 O OD2 . ASP B 90  ? 1.6053 1.3907 1.5381 -0.0583 0.0056  0.0015  90  ASP H OD2 
2028 N N   . THR B 91  ? 1.5062 1.3347 1.4351 -0.0545 0.0240  -0.0161 91  THR H N   
2029 C CA  . THR B 91  ? 1.6088 1.4472 1.5334 -0.0542 0.0267  -0.0157 91  THR H CA  
2030 C C   . THR B 91  ? 1.5460 1.3896 1.4601 -0.0544 0.0273  -0.0181 91  THR H C   
2031 O O   . THR B 91  ? 1.6495 1.4967 1.5634 -0.0546 0.0299  -0.0245 91  THR H O   
2032 C CB  . THR B 91  ? 1.6754 1.5220 1.6089 -0.0540 0.0314  -0.0208 91  THR H CB  
2033 O OG1 . THR B 91  ? 1.7119 1.5540 1.6555 -0.0538 0.0306  -0.0177 91  THR H OG1 
2034 C CG2 . THR B 91  ? 1.6144 1.4726 1.5427 -0.0542 0.0345  -0.0209 91  THR H CG2 
2035 N N   . ALA B 92  ? 1.4502 1.2938 1.3558 -0.0544 0.0249  -0.0129 92  ALA H N   
2036 C CA  . ALA B 92  ? 1.4913 1.3387 1.3873 -0.0545 0.0248  -0.0143 92  ALA H CA  
2037 C C   . ALA B 92  ? 1.5126 1.3618 1.4017 -0.0544 0.0223  -0.0081 92  ALA H C   
2038 O O   . ALA B 92  ? 1.5936 1.4399 1.4851 -0.0542 0.0203  -0.0025 92  ALA H O   
2039 C CB  . ALA B 92  ? 1.5544 1.3941 1.4474 -0.0544 0.0224  -0.0155 92  ALA H CB  
2040 N N   . VAL B 93  ? 1.3502 1.2041 1.2312 -0.0547 0.0223  -0.0089 93  VAL H N   
2041 C CA  . VAL B 93  ? 1.5707 1.4256 1.4456 -0.0546 0.0192  -0.0030 93  VAL H CA  
2042 C C   . VAL B 93  ? 1.7689 1.6144 1.6393 -0.0537 0.0150  -0.0006 93  VAL H C   
2043 O O   . VAL B 93  ? 1.8706 1.7126 1.7399 -0.0535 0.0152  -0.0043 93  VAL H O   
2044 C CB  . VAL B 93  ? 1.6676 1.5335 1.5368 -0.0556 0.0211  -0.0045 93  VAL H CB  
2045 C CG1 . VAL B 93  ? 1.9002 1.7673 1.7653 -0.0558 0.0224  -0.0100 93  VAL H CG1 
2046 C CG2 . VAL B 93  ? 1.4851 1.3517 1.3491 -0.0556 0.0173  0.0021  93  VAL H CG2 
2047 N N   . PHE B 94  ? 1.7181 1.5594 1.5863 -0.0531 0.0110  0.0056  94  PHE H N   
2048 C CA  . PHE B 94  ? 1.4992 1.3315 1.3636 -0.0521 0.0069  0.0079  94  PHE H CA  
2049 C C   . PHE B 94  ? 1.5645 1.3998 1.4223 -0.0516 0.0044  0.0107  94  PHE H C   
2050 O O   . PHE B 94  ? 1.7827 1.6244 1.6403 -0.0522 0.0043  0.0137  94  PHE H O   
2051 C CB  . PHE B 94  ? 1.5477 1.3710 1.4158 -0.0517 0.0036  0.0127  94  PHE H CB  
2052 C CG  . PHE B 94  ? 1.5961 1.4163 1.4718 -0.0522 0.0055  0.0109  94  PHE H CG  
2053 C CD1 . PHE B 94  ? 1.8137 1.6364 1.6922 -0.0528 0.0091  0.0049  94  PHE H CD1 
2054 C CD2 . PHE B 94  ? 1.7027 1.5166 1.5833 -0.0523 0.0032  0.0154  94  PHE H CD2 
2055 C CE1 . PHE B 94  ? 1.7964 1.6162 1.6831 -0.0532 0.0104  0.0032  94  PHE H CE1 
2056 C CE2 . PHE B 94  ? 1.8114 1.6223 1.6999 -0.0529 0.0046  0.0140  94  PHE H CE2 
2057 C CZ  . PHE B 94  ? 1.7738 1.5875 1.6656 -0.0533 0.0081  0.0078  94  PHE H CZ  
2058 N N   . TYR B 95  ? 1.4149 1.2459 1.2679 -0.0507 0.0024  0.0098  95  TYR H N   
2059 C CA  . TYR B 95  ? 1.5902 1.4239 1.4378 -0.0501 0.0000  0.0118  95  TYR H CA  
2060 C C   . TYR B 95  ? 1.6357 1.4603 1.4805 -0.0485 -0.0042 0.0140  95  TYR H C   
2061 O O   . TYR B 95  ? 1.6350 1.4526 1.4802 -0.0482 -0.0045 0.0124  95  TYR H O   
2062 C CB  . TYR B 95  ? 1.4799 1.3206 1.3238 -0.0507 0.0026  0.0072  95  TYR H CB  
2063 C CG  . TYR B 95  ? 1.5450 1.3965 1.3893 -0.0523 0.0057  0.0062  95  TYR H CG  
2064 C CD1 . TYR B 95  ? 1.4897 1.3475 1.3313 -0.0529 0.0040  0.0097  95  TYR H CD1 
2065 C CD2 . TYR B 95  ? 1.8058 1.6615 1.6535 -0.0534 0.0101  0.0016  95  TYR H CD2 
2066 C CE1 . TYR B 95  ? 1.5955 1.4639 1.4370 -0.0548 0.0068  0.0089  95  TYR H CE1 
2067 C CE2 . TYR B 95  ? 1.6927 1.5588 1.5403 -0.0550 0.0131  0.0002  95  TYR H CE2 
2068 C CZ  . TYR B 95  ? 1.6565 1.5291 1.5006 -0.0558 0.0115  0.0039  95  TYR H CZ  
2069 O OH  . TYR B 95  ? 1.6429 1.5266 1.4865 -0.0578 0.0145  0.0026  95  TYR H OH  
2070 N N   . CYS B 96  ? 1.5863 1.4115 1.4282 -0.0477 -0.0076 0.0175  96  CYS H N   
2071 C CA  . CYS B 96  ? 1.2657 1.0833 1.1049 -0.0460 -0.0119 0.0193  96  CYS H CA  
2072 C C   . CYS B 96  ? 1.3942 1.2151 1.2290 -0.0451 -0.0125 0.0175  96  CYS H C   
2073 O O   . CYS B 96  ? 1.5929 1.4215 1.4270 -0.0457 -0.0121 0.0181  96  CYS H O   
2074 C CB  . CYS B 96  ? 1.5250 1.3390 1.3657 -0.0454 -0.0163 0.0253  96  CYS H CB  
2075 S SG  . CYS B 96  ? 2.5665 2.3751 2.4123 -0.0463 -0.0162 0.0277  96  CYS H SG  
2076 N N   . ALA B 97  ? 0.9223 0.7375 0.7545 -0.0437 -0.0137 0.0154  97  ALA H N   
2077 C CA  . ALA B 97  ? 1.5711 1.3890 1.3999 -0.0425 -0.0146 0.0138  97  ALA H CA  
2078 C C   . ALA B 97  ? 0.9555 0.7653 0.7824 -0.0404 -0.0183 0.0144  97  ALA H C   
2079 O O   . ALA B 97  ? 2.5969 2.3996 2.4239 -0.0402 -0.0188 0.0142  97  ALA H O   
2080 C CB  . ALA B 97  ? 1.1152 0.9378 0.9423 -0.0433 -0.0106 0.0087  97  ALA H CB  
2081 N N   . ARG B 98  ? 1.3943 1.2054 1.2197 -0.0388 -0.0210 0.0152  98  ARG H N   
2082 C CA  . ARG B 98  ? 1.2848 1.0890 1.1086 -0.0365 -0.0244 0.0150  98  ARG H CA  
2083 C C   . ARG B 98  ? 1.4427 1.2457 1.2635 -0.0360 -0.0220 0.0102  98  ARG H C   
2084 O O   . ARG B 98  ? 1.7041 1.5122 1.5243 -0.0373 -0.0182 0.0072  98  ARG H O   
2085 C CB  . ARG B 98  ? 1.3961 1.2022 1.2203 -0.0348 -0.0282 0.0170  98  ARG H CB  
2086 C CG  . ARG B 98  ? 2.1759 1.9825 2.0033 -0.0354 -0.0316 0.0226  98  ARG H CG  
2087 C CD  . ARG B 98  ? 2.7247 2.5327 2.5535 -0.0339 -0.0361 0.0249  98  ARG H CD  
2088 N NE  . ARG B 98  ? 3.0758 2.8852 2.9079 -0.0350 -0.0394 0.0308  98  ARG H NE  
2089 C CZ  . ARG B 98  ? 3.1000 2.9113 2.9346 -0.0344 -0.0440 0.0342  98  ARG H CZ  
2090 N NH1 . ARG B 98  ? 3.3422 3.1531 3.1768 -0.0323 -0.0461 0.0323  98  ARG H NH1 
2091 N NH2 . ARG B 98  ? 3.0172 2.8311 2.8548 -0.0361 -0.0466 0.0400  98  ARG H NH2 
2092 N N   . ASP B 99  ? 1.4550 1.2515 1.2739 -0.0343 -0.0242 0.0094  99  ASP H N   
2093 C CA  . ASP B 99  ? 1.4664 1.2619 1.2823 -0.0342 -0.0221 0.0052  99  ASP H CA  
2094 C C   . ASP B 99  ? 1.5726 1.3629 1.3864 -0.0317 -0.0253 0.0043  99  ASP H C   
2095 O O   . ASP B 99  ? 1.7973 1.5832 1.6121 -0.0303 -0.0292 0.0070  99  ASP H O   
2096 C CB  . ASP B 99  ? 1.4752 1.2676 1.2914 -0.0364 -0.0198 0.0047  99  ASP H CB  
2097 C CG  . ASP B 99  ? 1.7229 1.5154 1.5363 -0.0368 -0.0176 0.0009  99  ASP H CG  
2098 O OD1 . ASP B 99  ? 1.8812 1.6768 1.6925 -0.0353 -0.0174 -0.0014 99  ASP H OD1 
2099 O OD2 . ASP B 99  ? 1.6900 1.4802 1.5038 -0.0388 -0.0160 0.0004  99  ASP H OD2 
2100 N N   . ARG B 100 ? 1.6596 1.4508 1.4703 -0.0311 -0.0235 0.0003  100 ARG H N   
2101 C CA  . ARG B 100 ? 1.7186 1.5055 1.5276 -0.0285 -0.0265 -0.0009 100 ARG H CA  
2102 C C   . ARG B 100 ? 1.6940 1.4729 1.5006 -0.0292 -0.0277 -0.0006 100 ARG H C   
2103 O O   . ARG B 100 ? 1.5285 1.3068 1.3341 -0.0316 -0.0252 -0.0010 100 ARG H O   
2104 C CB  . ARG B 100 ? 1.9014 1.6928 1.7083 -0.0271 -0.0246 -0.0052 100 ARG H CB  
2105 C CG  . ARG B 100 ? 1.7534 1.5522 1.5627 -0.0263 -0.0240 -0.0053 100 ARG H CG  
2106 C CD  . ARG B 100 ? 1.7442 1.5480 1.5524 -0.0248 -0.0224 -0.0092 100 ARG H CD  
2107 N NE  . ARG B 100 ? 1.9617 1.7727 1.7725 -0.0249 -0.0218 -0.0086 100 ARG H NE  
2108 C CZ  . ARG B 100 ? 1.8097 1.6267 1.6208 -0.0240 -0.0202 -0.0111 100 ARG H CZ  
2109 N NH1 . ARG B 100 ? 1.7639 1.5809 1.5731 -0.0225 -0.0192 -0.0147 100 ARG H NH1 
2110 N NH2 . ARG B 100 ? 1.7601 1.5836 1.5733 -0.0249 -0.0196 -0.0100 100 ARG H NH2 
2111 N N   . PRO B 101 ? 1.5777 1.3506 1.3839 -0.0273 -0.0317 0.0002  101 PRO H N   
2112 C CA  . PRO B 101 ? 1.3636 1.1286 1.1673 -0.0283 -0.0334 0.0010  101 PRO H CA  
2113 C C   . PRO B 101 ? 1.4214 1.1863 1.2207 -0.0291 -0.0311 -0.0027 101 PRO H C   
2114 O O   . PRO B 101 ? 1.3577 1.1202 1.1558 -0.0319 -0.0299 -0.0019 101 PRO H O   
2115 C CB  . PRO B 101 ? 1.5204 1.2797 1.3246 -0.0256 -0.0385 0.0021  101 PRO H CB  
2116 C CG  . PRO B 101 ? 1.4612 1.2258 1.2673 -0.0229 -0.0389 0.0002  101 PRO H CG  
2117 C CD  . PRO B 101 ? 1.5807 1.3533 1.3889 -0.0244 -0.0354 0.0009  101 PRO H CD  
2118 N N   . HIS B 102 ? 1.5911 1.3591 1.3882 -0.0270 -0.0305 -0.0067 102 HIS H N   
2119 C CA  . HIS B 102 ? 1.2650 1.0331 1.0574 -0.0277 -0.0287 -0.0102 102 HIS H CA  
2120 C C   . HIS B 102 ? 1.4788 1.2529 1.2710 -0.0304 -0.0243 -0.0110 102 HIS H C   
2121 O O   . HIS B 102 ? 1.6331 1.4137 1.4276 -0.0301 -0.0221 -0.0116 102 HIS H O   
2122 C CB  . HIS B 102 ? 1.2569 1.0274 1.0478 -0.0243 -0.0292 -0.0145 102 HIS H CB  
2123 C CG  . HIS B 102 ? 1.8267 1.5912 1.6185 -0.0214 -0.0339 -0.0142 102 HIS H CG  
2124 N ND1 . HIS B 102 ? 2.2902 2.0469 2.0790 -0.0217 -0.0367 -0.0139 102 HIS H ND1 
2125 C CD2 . HIS B 102 ? 2.0262 1.7911 1.8219 -0.0183 -0.0366 -0.0140 102 HIS H CD2 
2126 C CE1 . HIS B 102 ? 2.5290 2.2814 2.3198 -0.0188 -0.0410 -0.0137 102 HIS H CE1 
2127 N NE2 . HIS B 102 ? 2.3869 2.1442 2.1822 -0.0167 -0.0411 -0.0137 102 HIS H NE2 
2128 N N   . ILE B 103 ? 1.4860 1.2578 1.2754 -0.0333 -0.0234 -0.0109 103 ILE H N   
2129 C CA  . ILE B 103 ? 1.3688 1.1461 1.1582 -0.0360 -0.0197 -0.0118 103 ILE H CA  
2130 C C   . ILE B 103 ? 1.3867 1.1712 1.1743 -0.0345 -0.0173 -0.0158 103 ILE H C   
2131 O O   . ILE B 103 ? 1.6068 1.3975 1.3959 -0.0356 -0.0145 -0.0165 103 ILE H O   
2132 C CB  . ILE B 103 ? 1.2087 0.9818 0.9955 -0.0395 -0.0199 -0.0107 103 ILE H CB  
2133 C CG1 . ILE B 103 ? 1.6406 1.4074 1.4306 -0.0413 -0.0220 -0.0064 103 ILE H CG1 
2134 C CG2 . ILE B 103 ? 1.1326 0.9115 0.9193 -0.0423 -0.0167 -0.0118 103 ILE H CG2 
2135 C CD1 . ILE B 103 ? 1.8605 1.6220 1.6482 -0.0445 -0.0232 -0.0047 103 ILE H CD1 
2136 N N   . LEU B 104 ? 1.2964 1.0803 1.0811 -0.0319 -0.0186 -0.0186 104 LEU H N   
2137 C CA  . LEU B 104 ? 1.2383 1.0292 1.0219 -0.0300 -0.0164 -0.0225 104 LEU H CA  
2138 C C   . LEU B 104 ? 1.6083 1.4049 1.3962 -0.0284 -0.0153 -0.0224 104 LEU H C   
2139 O O   . LEU B 104 ? 2.0564 1.8594 1.8451 -0.0298 -0.0123 -0.0232 104 LEU H O   
2140 C CB  . LEU B 104 ? 1.2441 1.0327 1.0252 -0.0267 -0.0185 -0.0256 104 LEU H CB  
2141 C CG  . LEU B 104 ? 1.3549 1.1389 1.1306 -0.0283 -0.0193 -0.0265 104 LEU H CG  
2142 C CD1 . LEU B 104 ? 1.8322 1.6134 1.6059 -0.0247 -0.0216 -0.0300 104 LEU H CD1 
2143 C CD2 . LEU B 104 ? 1.4139 1.2037 1.1863 -0.0313 -0.0159 -0.0279 104 LEU H CD2 
2144 N N   . THR B 105 ? 1.6805 1.4748 1.4714 -0.0258 -0.0180 -0.0213 105 THR H N   
2145 C CA  . THR B 105 ? 1.8192 1.6189 1.6142 -0.0248 -0.0174 -0.0205 105 THR H CA  
2146 C C   . THR B 105 ? 1.8514 1.6533 1.6480 -0.0280 -0.0152 -0.0181 105 THR H C   
2147 O O   . THR B 105 ? 1.7931 1.5906 1.5893 -0.0304 -0.0154 -0.0160 105 THR H O   
2148 C CB  . THR B 105 ? 1.6981 1.4943 1.4962 -0.0222 -0.0213 -0.0186 105 THR H CB  
2149 O OG1 . THR B 105 ? 1.8658 1.6554 1.6642 -0.0237 -0.0234 -0.0150 105 THR H OG1 
2150 C CG2 . THR B 105 ? 1.5778 1.3721 1.3754 -0.0187 -0.0236 -0.0216 105 THR H CG2 
2151 N N   . GLY B 106 ? 1.8998 1.7085 1.6985 -0.0281 -0.0133 -0.0186 106 GLY H N   
2152 C CA  . GLY B 106 ? 1.9065 1.7179 1.7071 -0.0308 -0.0114 -0.0170 106 GLY H CA  
2153 C C   . GLY B 106 ? 1.7707 1.5784 1.5737 -0.0312 -0.0134 -0.0135 106 GLY H C   
2154 O O   . GLY B 106 ? 1.7363 1.5381 1.5392 -0.0298 -0.0164 -0.0119 106 GLY H O   
2155 N N   . PHE B 107 ? 1.6606 1.4718 1.4659 -0.0330 -0.0118 -0.0123 107 PHE H N   
2156 C CA  . PHE B 107 ? 1.4848 1.2930 1.2924 -0.0338 -0.0131 -0.0090 107 PHE H CA  
2157 C C   . PHE B 107 ? 1.4698 1.2842 1.2797 -0.0342 -0.0124 -0.0080 107 PHE H C   
2158 O O   . PHE B 107 ? 1.7785 1.5988 1.5886 -0.0355 -0.0096 -0.0098 107 PHE H O   
2159 C CB  . PHE B 107 ? 1.7405 1.5454 1.5485 -0.0365 -0.0116 -0.0084 107 PHE H CB  
2160 C CG  . PHE B 107 ? 2.0970 1.8958 1.9024 -0.0368 -0.0126 -0.0088 107 PHE H CG  
2161 C CD1 . PHE B 107 ? 1.9191 1.7108 1.7241 -0.0360 -0.0157 -0.0066 107 PHE H CD1 
2162 C CD2 . PHE B 107 ? 2.0698 1.8704 1.8733 -0.0381 -0.0106 -0.0112 107 PHE H CD2 
2163 C CE1 . PHE B 107 ? 1.6286 1.4151 1.4308 -0.0366 -0.0168 -0.0070 107 PHE H CE1 
2164 C CE2 . PHE B 107 ? 1.7369 1.5327 1.5376 -0.0389 -0.0115 -0.0114 107 PHE H CE2 
2165 C CZ  . PHE B 107 ? 1.4660 1.2547 1.2658 -0.0381 -0.0146 -0.0093 107 PHE H CZ  
2166 N N   . ASP B 108 ? 1.4461 1.2596 1.2578 -0.0331 -0.0152 -0.0050 108 ASP H N   
2167 C CA  . ASP B 108 ? 1.6149 1.4348 1.4286 -0.0336 -0.0151 -0.0035 108 ASP H CA  
2168 C C   . ASP B 108 ? 1.7111 1.5299 1.5269 -0.0350 -0.0160 0.0000  108 ASP H C   
2169 O O   . ASP B 108 ? 1.7489 1.5620 1.5656 -0.0341 -0.0190 0.0028  108 ASP H O   
2170 C CB  . ASP B 108 ? 1.6259 1.4476 1.4405 -0.0312 -0.0182 -0.0027 108 ASP H CB  
2171 C CG  . ASP B 108 ? 1.6862 1.5009 1.5015 -0.0291 -0.0225 -0.0007 108 ASP H CG  
2172 O OD1 . ASP B 108 ? 1.5229 1.3313 1.3373 -0.0294 -0.0230 -0.0001 108 ASP H OD1 
2173 O OD2 . ASP B 108 ? 1.7171 1.5326 1.5343 -0.0271 -0.0257 0.0004  108 ASP H OD2 
2174 N N   . PHE B 109 ? 1.6852 1.5096 1.5019 -0.0372 -0.0133 -0.0001 109 PHE H N   
2175 C CA  . PHE B 109 ? 1.5732 1.3988 1.3921 -0.0387 -0.0134 0.0029  109 PHE H CA  
2176 C C   . PHE B 109 ? 1.4448 1.2770 1.2645 -0.0389 -0.0149 0.0052  109 PHE H C   
2177 O O   . PHE B 109 ? 1.4866 1.3256 1.3067 -0.0409 -0.0127 0.0052  109 PHE H O   
2178 C CB  . PHE B 109 ? 1.6072 1.4351 1.4269 -0.0410 -0.0094 0.0008  109 PHE H CB  
2179 C CG  . PHE B 109 ? 1.7286 1.5501 1.5482 -0.0412 -0.0085 -0.0008 109 PHE H CG  
2180 C CD1 . PHE B 109 ? 1.9069 1.7284 1.7247 -0.0411 -0.0070 -0.0042 109 PHE H CD1 
2181 C CD2 . PHE B 109 ? 1.7858 1.6013 1.6073 -0.0414 -0.0097 0.0015  109 PHE H CD2 
2182 C CE1 . PHE B 109 ? 1.9521 1.7681 1.7698 -0.0416 -0.0066 -0.0052 109 PHE H CE1 
2183 C CE2 . PHE B 109 ? 1.7412 1.5508 1.5626 -0.0418 -0.0094 0.0004  109 PHE H CE2 
2184 C CZ  . PHE B 109 ? 1.8345 1.6444 1.6539 -0.0420 -0.0078 -0.0028 109 PHE H CZ  
2185 N N   . ASP B 110 ? 1.6020 1.4322 1.4220 -0.0368 -0.0187 0.0070  110 ASP H N   
2186 C CA  . ASP B 110 ? 1.8742 1.7100 1.6956 -0.0369 -0.0212 0.0098  110 ASP H CA  
2187 C C   . ASP B 110 ? 1.9351 1.7753 1.7580 -0.0394 -0.0210 0.0133  110 ASP H C   
2188 O O   . ASP B 110 ? 1.9747 1.8229 1.7974 -0.0412 -0.0200 0.0139  110 ASP H O   
2189 C CB  . ASP B 110 ? 1.8688 1.6998 1.6918 -0.0342 -0.0262 0.0119  110 ASP H CB  
2190 C CG  . ASP B 110 ? 2.0002 1.8298 1.8221 -0.0319 -0.0263 0.0082  110 ASP H CG  
2191 O OD1 . ASP B 110 ? 1.9215 1.7466 1.7449 -0.0293 -0.0301 0.0089  110 ASP H OD1 
2192 O OD2 . ASP B 110 ? 2.0523 1.8854 1.8722 -0.0325 -0.0226 0.0045  110 ASP H OD2 
2193 N N   . TYR B 111 ? 1.7699 1.6053 1.5942 -0.0395 -0.0221 0.0159  111 TYR H N   
2194 C CA  . TYR B 111 ? 1.7891 1.6287 1.6154 -0.0416 -0.0225 0.0199  111 TYR H CA  
2195 C C   . TYR B 111 ? 1.6020 1.4402 1.4288 -0.0430 -0.0188 0.0186  111 TYR H C   
2196 O O   . TYR B 111 ? 1.6986 1.5305 1.5249 -0.0420 -0.0176 0.0161  111 TYR H O   
2197 C CB  . TYR B 111 ? 1.9936 1.8294 1.8224 -0.0406 -0.0280 0.0254  111 TYR H CB  
2198 C CG  . TYR B 111 ? 2.1591 1.9966 1.9887 -0.0394 -0.0320 0.0268  111 TYR H CG  
2199 C CD1 . TYR B 111 ? 2.2220 2.0534 2.0539 -0.0372 -0.0375 0.0299  111 TYR H CD1 
2200 C CD2 . TYR B 111 ? 2.2227 2.0675 2.0511 -0.0402 -0.0305 0.0249  111 TYR H CD2 
2201 C CE1 . TYR B 111 ? 2.3841 2.2168 2.2179 -0.0359 -0.0414 0.0309  111 TYR H CE1 
2202 C CE2 . TYR B 111 ? 2.1490 1.9952 1.9790 -0.0390 -0.0343 0.0263  111 TYR H CE2 
2203 C CZ  . TYR B 111 ? 2.3478 2.1880 2.1808 -0.0367 -0.0398 0.0292  111 TYR H CZ  
2204 O OH  . TYR B 111 ? 2.5792 2.4205 2.4148 -0.0354 -0.0439 0.0305  111 TYR H OH  
2205 N N   . TRP B 112 ? 1.6728 1.5175 1.5009 -0.0453 -0.0172 0.0204  112 TRP H N   
2206 C CA  . TRP B 112 ? 1.5490 1.3939 1.3784 -0.0466 -0.0133 0.0186  112 TRP H CA  
2207 C C   . TRP B 112 ? 1.5228 1.3700 1.3552 -0.0480 -0.0143 0.0235  112 TRP H C   
2208 O O   . TRP B 112 ? 1.5446 1.3968 1.3773 -0.0489 -0.0169 0.0276  112 TRP H O   
2209 C CB  . TRP B 112 ? 1.5569 1.4094 1.3848 -0.0484 -0.0084 0.0139  112 TRP H CB  
2210 C CG  . TRP B 112 ? 1.5364 1.3856 1.3625 -0.0474 -0.0064 0.0087  112 TRP H CG  
2211 C CD1 . TRP B 112 ? 1.6574 1.5059 1.4811 -0.0461 -0.0077 0.0073  112 TRP H CD1 
2212 C CD2 . TRP B 112 ? 1.4906 1.3372 1.3178 -0.0479 -0.0029 0.0046  112 TRP H CD2 
2213 N NE1 . TRP B 112 ? 1.6863 1.5322 1.5090 -0.0458 -0.0052 0.0028  112 TRP H NE1 
2214 C CE2 . TRP B 112 ? 1.6169 1.4615 1.4419 -0.0470 -0.0024 0.0012  112 TRP H CE2 
2215 C CE3 . TRP B 112 ? 1.6116 1.4577 1.4421 -0.0489 -0.0003 0.0037  112 TRP H CE3 
2216 C CZ2 . TRP B 112 ? 1.8869 1.7289 1.7127 -0.0474 0.0002  -0.0028 112 TRP H CZ2 
2217 C CZ3 . TRP B 112 ? 1.4730 1.3161 1.3048 -0.0492 0.0022  -0.0005 112 TRP H CZ3 
2218 C CH2 . TRP B 112 ? 1.5645 1.4056 1.3938 -0.0485 0.0023  -0.0035 112 TRP H CH2 
2219 N N   . GLY B 113 ? 1.5056 1.3491 1.3405 -0.0482 -0.0126 0.0232  113 GLY H N   
2220 C CA  . GLY B 113 ? 1.4194 1.2644 1.2577 -0.0494 -0.0135 0.0278  113 GLY H CA  
2221 C C   . GLY B 113 ? 1.4672 1.3231 1.3063 -0.0519 -0.0095 0.0270  113 GLY H C   
2222 O O   . GLY B 113 ? 1.4083 1.2700 1.2455 -0.0528 -0.0057 0.0223  113 GLY H O   
2223 N N   . GLN B 114 ? 1.4674 1.3264 1.3095 -0.0531 -0.0105 0.0318  114 GLN H N   
2224 C CA  . GLN B 114 ? 1.5066 1.3770 1.3493 -0.0557 -0.0071 0.0318  114 GLN H CA  
2225 C C   . GLN B 114 ? 1.3344 1.2066 1.1799 -0.0562 -0.0015 0.0267  114 GLN H C   
2226 O O   . GLN B 114 ? 1.2559 1.1379 1.1010 -0.0581 0.0025  0.0241  114 GLN H O   
2227 C CB  . GLN B 114 ? 1.5980 1.4719 1.4433 -0.0570 -0.0102 0.0390  114 GLN H CB  
2228 C CG  . GLN B 114 ? 1.8512 1.7260 1.6947 -0.0572 -0.0158 0.0442  114 GLN H CG  
2229 C CD  . GLN B 114 ? 2.1493 2.0270 1.9959 -0.0586 -0.0195 0.0520  114 GLN H CD  
2230 O OE1 . GLN B 114 ? 2.2063 2.0817 2.0567 -0.0587 -0.0191 0.0542  114 GLN H OE1 
2231 N NE2 . GLN B 114 ? 2.2080 2.0911 2.0536 -0.0600 -0.0234 0.0566  114 GLN H NE2 
2232 N N   . GLY B 115 ? 1.2768 1.1397 1.1252 -0.0547 -0.0013 0.0254  115 GLY H N   
2233 C CA  . GLY B 115 ? 1.2771 1.1406 1.1291 -0.0550 0.0034  0.0204  115 GLY H CA  
2234 C C   . GLY B 115 ? 1.2133 1.0765 1.0713 -0.0554 0.0041  0.0233  115 GLY H C   
2235 O O   . GLY B 115 ? 1.3927 1.2629 1.2517 -0.0567 0.0038  0.0274  115 GLY H O   
2236 N N   . THR B 116 ? 1.2779 1.1333 1.1401 -0.0544 0.0048  0.0216  116 THR H N   
2237 C CA  . THR B 116 ? 1.4493 1.3036 1.3182 -0.0547 0.0053  0.0242  116 THR H CA  
2238 C C   . THR B 116 ? 1.5146 1.3698 1.3886 -0.0548 0.0101  0.0181  116 THR H C   
2239 O O   . THR B 116 ? 1.5376 1.3853 1.4124 -0.0540 0.0101  0.0150  116 THR H O   
2240 C CB  . THR B 116 ? 1.4052 1.2479 1.2755 -0.0535 0.0003  0.0294  116 THR H CB  
2241 O OG1 . THR B 116 ? 1.6052 1.4477 1.4720 -0.0534 -0.0043 0.0351  116 THR H OG1 
2242 C CG2 . THR B 116 ? 1.3813 1.2225 1.2592 -0.0539 0.0010  0.0319  116 THR H CG2 
2243 N N   . LEU B 117 ? 1.4678 1.3324 1.3455 -0.0560 0.0142  0.0164  117 LEU H N   
2244 C CA  . LEU B 117 ? 1.5995 1.4658 1.4833 -0.0560 0.0189  0.0103  117 LEU H CA  
2245 C C   . LEU B 117 ? 1.6019 1.4602 1.4936 -0.0553 0.0177  0.0128  117 LEU H C   
2246 O O   . LEU B 117 ? 1.7509 1.6093 1.6453 -0.0555 0.0158  0.0187  117 LEU H O   
2247 C CB  . LEU B 117 ? 1.6633 1.5431 1.5484 -0.0574 0.0237  0.0074  117 LEU H CB  
2248 C CG  . LEU B 117 ? 2.1433 2.0328 2.0215 -0.0586 0.0259  0.0039  117 LEU H CG  
2249 C CD1 . LEU B 117 ? 2.0760 1.9790 1.9558 -0.0603 0.0301  0.0027  117 LEU H CD1 
2250 C CD2 . LEU B 117 ? 2.3385 2.2261 2.2160 -0.0581 0.0283  -0.0038 117 LEU H CD2 
2251 N N   . VAL B 118 ? 1.2114 1.0630 1.1071 -0.0547 0.0184  0.0088  118 VAL H N   
2252 C CA  . VAL B 118 ? 1.3720 1.2164 1.2762 -0.0543 0.0175  0.0106  118 VAL H CA  
2253 C C   . VAL B 118 ? 1.7326 1.5808 1.6446 -0.0544 0.0223  0.0038  118 VAL H C   
2254 O O   . VAL B 118 ? 1.5049 1.3522 1.4161 -0.0543 0.0238  -0.0020 118 VAL H O   
2255 C CB  . VAL B 118 ? 1.1840 1.0155 1.0867 -0.0538 0.0129  0.0130  118 VAL H CB  
2256 C CG1 . VAL B 118 ? 1.4206 1.2452 1.3327 -0.0539 0.0124  0.0139  118 VAL H CG1 
2257 C CG2 . VAL B 118 ? 1.4601 1.2875 1.3567 -0.0535 0.0081  0.0198  118 VAL H CG2 
2258 N N   . THR B 119 ? 1.8841 1.7368 1.8039 -0.0545 0.0246  0.0045  119 THR H N   
2259 C CA  . THR B 119 ? 1.6972 1.5534 1.6263 -0.0543 0.0290  -0.0018 119 THR H CA  
2260 C C   . THR B 119 ? 1.7322 1.5790 1.6711 -0.0540 0.0269  0.0007  119 THR H C   
2261 O O   . THR B 119 ? 1.9508 1.7935 1.8911 -0.0541 0.0238  0.0077  119 THR H O   
2262 C CB  . THR B 119 ? 1.7636 1.6330 1.6955 -0.0548 0.0337  -0.0038 119 THR H CB  
2263 O OG1 . THR B 119 ? 1.8093 1.6794 1.7438 -0.0550 0.0320  0.0035  119 THR H OG1 
2264 C CG2 . THR B 119 ? 1.9502 1.8293 1.8724 -0.0556 0.0356  -0.0061 119 THR H CG2 
2265 N N   . VAL B 120 ? 1.8492 1.6925 1.7949 -0.0537 0.0282  -0.0047 120 VAL H N   
2266 C CA  . VAL B 120 ? 1.9350 1.7690 1.8905 -0.0537 0.0257  -0.0024 120 VAL H CA  
2267 C C   . VAL B 120 ? 1.9779 1.8152 1.9453 -0.0533 0.0297  -0.0092 120 VAL H C   
2268 O O   . VAL B 120 ? 1.9007 1.7351 1.8705 -0.0534 0.0300  -0.0144 120 VAL H O   
2269 C CB  . VAL B 120 ? 1.8012 1.6235 1.7527 -0.0542 0.0210  -0.0005 120 VAL H CB  
2270 C CG1 . VAL B 120 ? 1.8616 1.6747 1.8236 -0.0547 0.0184  0.0019  120 VAL H CG1 
2271 C CG2 . VAL B 120 ? 1.7708 1.5894 1.7114 -0.0544 0.0170  0.0058  120 VAL H CG2 
2272 N N   . SER B 121 ? 2.1197 1.9635 2.0952 -0.0529 0.0326  -0.0092 121 SER H N   
2273 C CA  . SER B 121 ? 2.2346 2.0805 2.2235 -0.0523 0.0359  -0.0151 121 SER H CA  
2274 C C   . SER B 121 ? 2.1895 2.0365 2.1883 -0.0520 0.0362  -0.0107 121 SER H C   
2275 O O   . SER B 121 ? 2.3230 2.1723 2.3176 -0.0523 0.0351  -0.0042 121 SER H O   
2276 C CB  . SER B 121 ? 2.3288 2.1862 2.3174 -0.0517 0.0418  -0.0242 121 SER H CB  
2277 O OG  . SER B 121 ? 2.0376 1.9065 2.0223 -0.0518 0.0450  -0.0231 121 SER H OG  
2278 N N   . SER B 122 ? 1.9212 1.7665 1.9340 -0.0514 0.0375  -0.0142 122 SER H N   
2279 C CA  . SER B 122 ? 2.1232 1.9680 2.1477 -0.0512 0.0373  -0.0100 122 SER H CA  
2280 C C   . SER B 122 ? 2.0550 1.9138 2.0837 -0.0503 0.0432  -0.0129 122 SER H C   
2281 O O   . SER B 122 ? 2.2461 2.1077 2.2886 -0.0495 0.0458  -0.0156 122 SER H O   
2282 C CB  . SER B 122 ? 2.3069 2.1437 2.3455 -0.0510 0.0358  -0.0123 122 SER H CB  
2283 O OG  . SER B 122 ? 2.2810 2.1239 2.3265 -0.0499 0.0404  -0.0223 122 SER H OG  
2284 N N   . ALA B 123 ? 1.8343 1.7023 1.8518 -0.0507 0.0453  -0.0123 123 ALA H N   
2285 C CA  . ALA B 123 ? 1.9585 1.8411 1.9785 -0.0504 0.0510  -0.0150 123 ALA H CA  
2286 C C   . ALA B 123 ? 2.0243 1.9109 2.0364 -0.0515 0.0493  -0.0063 123 ALA H C   
2287 O O   . ALA B 123 ? 2.1138 1.9958 2.1141 -0.0524 0.0453  -0.0013 123 ALA H O   
2288 C CB  . ALA B 123 ? 1.9835 1.8763 1.9978 -0.0502 0.0561  -0.0245 123 ALA H CB  
2289 N N   . SER B 124 ? 2.0513 1.9468 2.0706 -0.0515 0.0522  -0.0044 124 SER H N   
2290 C CA  . SER B 124 ? 2.0636 1.9645 2.0768 -0.0527 0.0508  0.0039  124 SER H CA  
2291 C C   . SER B 124 ? 2.0383 1.9535 2.0417 -0.0537 0.0550  0.0006  124 SER H C   
2292 O O   . SER B 124 ? 2.0866 2.0092 2.0897 -0.0533 0.0600  -0.0087 124 SER H O   
2293 C CB  . SER B 124 ? 2.2157 2.1201 2.2412 -0.0525 0.0519  0.0082  124 SER H CB  
2294 O OG  . SER B 124 ? 2.2320 2.1491 2.2661 -0.0517 0.0590  0.0004  124 SER H OG  
2295 N N   . THR B 125 ? 2.1737 2.0929 2.1691 -0.0552 0.0527  0.0084  125 THR H N   
2296 C CA  . THR B 125 ? 2.2296 2.1626 2.2155 -0.0568 0.0558  0.0069  125 THR H CA  
2297 C C   . THR B 125 ? 2.2604 2.2092 2.2535 -0.0569 0.0630  0.0017  125 THR H C   
2298 O O   . THR B 125 ? 2.3413 2.2923 2.3452 -0.0564 0.0642  0.0042  125 THR H O   
2299 C CB  . THR B 125 ? 1.9001 1.8336 1.8777 -0.0585 0.0511  0.0174  125 THR H CB  
2300 O OG1 . THR B 125 ? 1.6492 1.5837 1.6352 -0.0588 0.0499  0.0245  125 THR H OG1 
2301 C CG2 . THR B 125 ? 1.6078 1.5262 1.5781 -0.0582 0.0442  0.0218  125 THR H CG2 
2302 N N   . LYS B 126 ? 2.0812 2.0413 2.0683 -0.0576 0.0678  -0.0058 126 LYS H N   
2303 C CA  . LYS B 126 ? 2.0200 1.9964 2.0124 -0.0579 0.0751  -0.0118 126 LYS H CA  
2304 C C   . LYS B 126 ? 1.8155 1.8061 1.7959 -0.0606 0.0774  -0.0120 126 LYS H C   
2305 O O   . LYS B 126 ? 1.9218 1.9102 1.8913 -0.0614 0.0756  -0.0135 126 LYS H O   
2306 C CB  . LYS B 126 ? 2.0449 2.0214 2.0456 -0.0558 0.0799  -0.0239 126 LYS H CB  
2307 C CG  . LYS B 126 ? 2.2560 2.2209 2.2711 -0.0535 0.0784  -0.0242 126 LYS H CG  
2308 C CD  . LYS B 126 ? 2.3237 2.2890 2.3472 -0.0516 0.0828  -0.0363 126 LYS H CD  
2309 C CE  . LYS B 126 ? 2.4258 2.3798 2.4647 -0.0495 0.0809  -0.0364 126 LYS H CE  
2310 N NZ  . LYS B 126 ? 2.4214 2.3753 2.4695 -0.0476 0.0846  -0.0482 126 LYS H NZ  
2311 N N   . GLY B 127 ? 1.6157 1.6215 1.5985 -0.0621 0.0813  -0.0103 127 GLY H N   
2312 C CA  . GLY B 127 ? 1.8388 1.8601 1.8112 -0.0650 0.0840  -0.0106 127 GLY H CA  
2313 C C   . GLY B 127 ? 2.0942 2.1238 2.0641 -0.0649 0.0901  -0.0231 127 GLY H C   
2314 O O   . GLY B 127 ? 2.2267 2.2576 2.2062 -0.0628 0.0949  -0.0321 127 GLY H O   
2315 N N   . PRO B 128 ? 2.0348 2.0696 1.9917 -0.0672 0.0897  -0.0239 128 PRO H N   
2316 C CA  . PRO B 128 ? 1.9281 1.9700 1.8813 -0.0673 0.0948  -0.0357 128 PRO H CA  
2317 C C   . PRO B 128 ? 1.9538 2.0149 1.9100 -0.0686 0.1025  -0.0416 128 PRO H C   
2318 O O   . PRO B 128 ? 1.9846 2.0577 1.9394 -0.0711 0.1034  -0.0352 128 PRO H O   
2319 C CB  . PRO B 128 ? 1.7245 1.7666 1.6628 -0.0698 0.0913  -0.0325 128 PRO H CB  
2320 C CG  . PRO B 128 ? 1.6730 1.7168 1.6075 -0.0720 0.0866  -0.0198 128 PRO H CG  
2321 C CD  . PRO B 128 ? 1.9762 2.0089 1.9216 -0.0696 0.0837  -0.0142 128 PRO H CD  
2322 N N   . SER B 129 ? 1.8275 1.8917 1.7880 -0.0670 0.1079  -0.0540 129 SER H N   
2323 C CA  . SER B 129 ? 1.7401 1.8227 1.7026 -0.0680 0.1158  -0.0623 129 SER H CA  
2324 C C   . SER B 129 ? 1.9172 2.0080 1.8668 -0.0705 0.1177  -0.0685 129 SER H C   
2325 O O   . SER B 129 ? 2.0054 2.0870 1.9525 -0.0691 0.1166  -0.0749 129 SER H O   
2326 C CB  . SER B 129 ? 1.7927 1.8729 1.7704 -0.0642 0.1203  -0.0723 129 SER H CB  
2327 O OG  . SER B 129 ? 2.0471 2.1156 2.0254 -0.0621 0.1191  -0.0803 129 SER H OG  
2328 N N   . VAL B 130 ? 1.8272 1.9349 1.7682 -0.0744 0.1201  -0.0658 130 VAL H N   
2329 C CA  . VAL B 130 ? 2.0009 2.1168 1.9279 -0.0777 0.1208  -0.0690 130 VAL H CA  
2330 C C   . VAL B 130 ? 2.3733 2.5067 2.3009 -0.0787 0.1293  -0.0809 130 VAL H C   
2331 O O   . VAL B 130 ? 2.5147 2.6600 2.4496 -0.0788 0.1342  -0.0819 130 VAL H O   
2332 C CB  . VAL B 130 ? 1.6355 1.7577 1.5516 -0.0821 0.1165  -0.0565 130 VAL H CB  
2333 C CG1 . VAL B 130 ? 1.6800 1.8120 1.5822 -0.0860 0.1173  -0.0595 130 VAL H CG1 
2334 C CG2 . VAL B 130 ? 1.6347 1.7391 1.5505 -0.0808 0.1080  -0.0456 130 VAL H CG2 
2335 N N   . PHE B 131 ? 2.1801 2.3151 2.1004 -0.0794 0.1311  -0.0901 131 PHE H N   
2336 C CA  . PHE B 131 ? 2.3082 2.4575 2.2301 -0.0796 0.1391  -0.1033 131 PHE H CA  
2337 C C   . PHE B 131 ? 2.3004 2.4581 2.2080 -0.0832 0.1401  -0.1082 131 PHE H C   
2338 O O   . PHE B 131 ? 2.5951 2.7410 2.4973 -0.0827 0.1360  -0.1095 131 PHE H O   
2339 C CB  . PHE B 131 ? 2.4344 2.5732 2.3697 -0.0745 0.1413  -0.1142 131 PHE H CB  
2340 C CG  . PHE B 131 ? 2.7454 2.8769 2.6955 -0.0712 0.1407  -0.1100 131 PHE H CG  
2341 C CD1 . PHE B 131 ? 2.8404 2.9851 2.7995 -0.0708 0.1466  -0.1126 131 PHE H CD1 
2342 C CD2 . PHE B 131 ? 2.6410 2.7528 2.5965 -0.0684 0.1343  -0.1039 131 PHE H CD2 
2343 C CE1 . PHE B 131 ? 2.5422 2.6805 2.5155 -0.0678 0.1459  -0.1084 131 PHE H CE1 
2344 C CE2 . PHE B 131 ? 2.6594 2.7647 2.6286 -0.0656 0.1335  -0.1001 131 PHE H CE2 
2345 C CZ  . PHE B 131 ? 2.6291 2.7473 2.6073 -0.0653 0.1392  -0.1021 131 PHE H CZ  
2346 N N   . PRO B 132 ? 2.2386 2.4166 2.1395 -0.0872 0.1453  -0.1110 132 PRO H N   
2347 C CA  . PRO B 132 ? 2.0791 2.2652 1.9648 -0.0916 0.1449  -0.1126 132 PRO H CA  
2348 C C   . PRO B 132 ? 1.9936 2.1801 1.8784 -0.0903 0.1490  -0.1279 132 PRO H C   
2349 O O   . PRO B 132 ? 2.0662 2.2508 1.9624 -0.0864 0.1534  -0.1384 132 PRO H O   
2350 C CB  . PRO B 132 ? 2.0803 2.2889 1.9603 -0.0965 0.1491  -0.1092 132 PRO H CB  
2351 C CG  . PRO B 132 ? 2.2341 2.4494 2.1275 -0.0936 0.1556  -0.1156 132 PRO H CG  
2352 C CD  . PRO B 132 ? 2.3885 2.5839 2.2953 -0.0881 0.1518  -0.1127 132 PRO H CD  
2353 N N   . LEU B 133 ? 2.0289 2.2181 1.9004 -0.0938 0.1472  -0.1288 133 LEU H N   
2354 C CA  . LEU B 133 ? 1.9832 2.1746 1.8513 -0.0936 0.1506  -0.1426 133 LEU H CA  
2355 C C   . LEU B 133 ? 1.8244 2.0367 1.6797 -0.0995 0.1546  -0.1451 133 LEU H C   
2356 O O   . LEU B 133 ? 1.8095 2.0310 1.6562 -0.1041 0.1525  -0.1344 133 LEU H O   
2357 C CB  . LEU B 133 ? 1.8794 2.0533 1.7436 -0.0923 0.1445  -0.1422 133 LEU H CB  
2358 C CG  . LEU B 133 ? 1.7534 1.9066 1.6290 -0.0872 0.1399  -0.1382 133 LEU H CG  
2359 C CD1 . LEU B 133 ? 1.7345 1.8716 1.6050 -0.0865 0.1334  -0.1360 133 LEU H CD1 
2360 C CD2 . LEU B 133 ? 1.5888 1.7388 1.4797 -0.0824 0.1445  -0.1491 133 LEU H CD2 
2361 N N   . ALA B 134 ? 1.6134 1.8334 1.4675 -0.0995 0.1601  -0.1593 134 ALA H N   
2362 C CA  . ALA B 134 ? 1.7614 2.0031 1.6049 -0.1048 0.1654  -0.1640 134 ALA H CA  
2363 C C   . ALA B 134 ? 1.9051 2.1468 1.7401 -0.1062 0.1660  -0.1748 134 ALA H C   
2364 O O   . ALA B 134 ? 1.9496 2.1766 1.7906 -0.1020 0.1646  -0.1823 134 ALA H O   
2365 C CB  . ALA B 134 ? 1.8746 2.1316 1.7268 -0.1037 0.1738  -0.1721 134 ALA H CB  
2366 N N   . PRO B 135 ? 1.9201 2.1784 1.7411 -0.1123 0.1679  -0.1757 135 PRO H N   
2367 C CA  . PRO B 135 ? 2.1037 2.3630 1.9159 -0.1141 0.1685  -0.1860 135 PRO H CA  
2368 C C   . PRO B 135 ? 2.4095 2.6796 2.2263 -0.1126 0.1769  -0.2032 135 PRO H C   
2369 O O   . PRO B 135 ? 2.6547 2.9432 2.4618 -0.1172 0.1817  -0.2092 135 PRO H O   
2370 C CB  . PRO B 135 ? 2.0437 2.3166 1.8392 -0.1217 0.1663  -0.1775 135 PRO H CB  
2371 C CG  . PRO B 135 ? 1.9280 2.2156 1.7246 -0.1242 0.1691  -0.1696 135 PRO H CG  
2372 C CD  . PRO B 135 ? 1.7951 2.0700 1.6069 -0.1184 0.1678  -0.1648 135 PRO H CD  
2373 N N   . SER B 136 ? 2.4154 2.6742 2.2474 -0.1061 0.1787  -0.2113 136 SER H N   
2374 C CA  . SER B 136 ? 2.7017 2.9697 2.5413 -0.1037 0.1866  -0.2277 136 SER H CA  
2375 C C   . SER B 136 ? 2.7259 3.0004 2.5556 -0.1064 0.1881  -0.2388 136 SER H C   
2376 O O   . SER B 136 ? 2.8224 3.1123 2.6488 -0.1088 0.1908  -0.2417 136 SER H O   
2377 C CB  . SER B 136 ? 2.8785 3.1296 2.7364 -0.0962 0.1863  -0.2338 136 SER H CB  
2378 O OG  . SER B 136 ? 3.1345 3.3821 3.0030 -0.0936 0.1857  -0.2245 136 SER H OG  
2379 N N   . SER B 137 ? 2.9181 3.1774 2.7457 -0.1051 0.1834  -0.2418 137 SER H N   
2380 C CA  . SER B 137 ? 2.7187 2.9788 2.5396 -0.1068 0.1809  -0.2477 137 SER H CA  
2381 C C   . SER B 137 ? 2.6922 2.9586 2.4964 -0.1133 0.1761  -0.2367 137 SER H C   
2382 O O   . SER B 137 ? 2.6018 2.8651 2.3993 -0.1150 0.1725  -0.2394 137 SER H O   
2383 C CB  . SER B 137 ? 2.5687 2.8099 2.3952 -0.1027 0.1775  -0.2551 137 SER H CB  
2384 O OG  . SER B 137 ? 2.2836 2.5110 2.1065 -0.1029 0.1724  -0.2458 137 SER H OG  
2385 N N   . LYS B 138 ? 2.6544 2.9291 2.4526 -0.1170 0.1757  -0.2242 138 LYS H N   
2386 C CA  . LYS B 138 ? 2.6777 2.9579 2.4615 -0.1233 0.1705  -0.2120 138 LYS H CA  
2387 C C   . LYS B 138 ? 2.7204 2.9845 2.4983 -0.1236 0.1638  -0.2071 138 LYS H C   
2388 O O   . LYS B 138 ? 2.9385 3.2049 2.7055 -0.1285 0.1588  -0.1965 138 LYS H O   
2389 C CB  . LYS B 138 ? 2.7046 2.9992 2.4812 -0.1274 0.1711  -0.2154 138 LYS H CB  
2390 C CG  . LYS B 138 ? 2.5502 2.8634 2.3297 -0.1287 0.1770  -0.2173 138 LYS H CG  
2391 C CD  . LYS B 138 ? 2.6060 2.9325 2.3776 -0.1331 0.1773  -0.2210 138 LYS H CD  
2392 C CE  . LYS B 138 ? 2.8173 3.1629 2.5914 -0.1346 0.1831  -0.2227 138 LYS H CE  
2393 N NZ  . LYS B 138 ? 2.8021 3.1612 2.5684 -0.1391 0.1836  -0.2269 138 LYS H NZ  
2394 N N   . SER B 139 ? 2.6856 2.9337 2.4713 -0.1186 0.1634  -0.2147 139 SER H N   
2395 C CA  . SER B 139 ? 2.5009 2.7312 2.2841 -0.1176 0.1567  -0.2091 139 SER H CA  
2396 C C   . SER B 139 ? 2.6643 2.8971 2.4351 -0.1221 0.1526  -0.2084 139 SER H C   
2397 O O   . SER B 139 ? 2.9794 3.2185 2.7502 -0.1224 0.1542  -0.2171 139 SER H O   
2398 C CB  . SER B 139 ? 2.4261 2.6494 2.2119 -0.1171 0.1517  -0.1928 139 SER H CB  
2399 O OG  . SER B 139 ? 2.7789 3.0164 2.5535 -0.1232 0.1509  -0.1826 139 SER H OG  
2400 N N   . THR B 140 ? 2.5618 2.7889 2.3235 -0.1252 0.1466  -0.1975 140 THR H N   
2401 C CA  . THR B 140 ? 2.5455 2.7761 2.2967 -0.1297 0.1419  -0.1941 140 THR H CA  
2402 C C   . THR B 140 ? 2.9163 3.1643 2.6599 -0.1354 0.1420  -0.1851 140 THR H C   
2403 O O   . THR B 140 ? 2.9711 3.2201 2.7079 -0.1391 0.1377  -0.1723 140 THR H O   
2404 C CB  . THR B 140 ? 2.3776 2.5940 2.1236 -0.1302 0.1353  -0.1869 140 THR H CB  
2405 O OG1 . THR B 140 ? 2.7641 2.9768 2.5108 -0.1303 0.1321  -0.1734 140 THR H OG1 
2406 C CG2 . THR B 140 ? 1.9643 2.1637 1.7180 -0.1248 0.1347  -0.1959 140 THR H CG2 
2407 N N   . SER B 141 ? 3.3040 3.5659 3.0495 -0.1362 0.1469  -0.1920 141 SER H N   
2408 C CA  . SER B 141 ? 3.3048 3.5846 3.0441 -0.1417 0.1475  -0.1846 141 SER H CA  
2409 C C   . SER B 141 ? 3.1717 3.4539 2.8995 -0.1476 0.1411  -0.1753 141 SER H C   
2410 O O   . SER B 141 ? 2.9499 3.2381 2.6724 -0.1518 0.1379  -0.1625 141 SER H O   
2411 C CB  . SER B 141 ? 3.5030 3.7962 3.2454 -0.1416 0.1535  -0.1956 141 SER H CB  
2412 O OG  . SER B 141 ? 3.6123 3.9033 3.3521 -0.1418 0.1524  -0.2044 141 SER H OG  
2413 N N   . GLY B 142 ? 3.4504 3.7279 3.1748 -0.1480 0.1388  -0.1813 142 GLY H N   
2414 C CA  . GLY B 142 ? 3.4054 3.6837 3.1198 -0.1532 0.1325  -0.1730 142 GLY H CA  
2415 C C   . GLY B 142 ? 3.3343 3.5999 3.0463 -0.1531 0.1264  -0.1623 142 GLY H C   
2416 O O   . GLY B 142 ? 3.1234 3.3901 2.8277 -0.1576 0.1208  -0.1537 142 GLY H O   
2417 N N   . GLY B 143 ? 3.0264 3.2800 2.7449 -0.1482 0.1274  -0.1627 143 GLY H N   
2418 C CA  . GLY B 143 ? 2.9811 3.2232 2.6975 -0.1481 0.1220  -0.1523 143 GLY H CA  
2419 C C   . GLY B 143 ? 3.0146 3.2599 2.7327 -0.1484 0.1227  -0.1428 143 GLY H C   
2420 O O   . GLY B 143 ? 2.8874 3.1428 2.6004 -0.1533 0.1200  -0.1318 143 GLY H O   
2421 N N   . THR B 144 ? 2.8924 3.1293 2.6186 -0.1434 0.1260  -0.1466 144 THR H N   
2422 C CA  . THR B 144 ? 2.8078 3.0446 2.5409 -0.1418 0.1255  -0.1366 144 THR H CA  
2423 C C   . THR B 144 ? 2.9469 3.1818 2.6922 -0.1361 0.1316  -0.1456 144 THR H C   
2424 O O   . THR B 144 ? 3.6409 3.8611 3.3948 -0.1304 0.1316  -0.1525 144 THR H O   
2425 C CB  . THR B 144 ? 2.7247 2.9445 2.4618 -0.1391 0.1177  -0.1244 144 THR H CB  
2426 O OG1 . THR B 144 ? 2.9593 3.1614 2.7013 -0.1340 0.1158  -0.1303 144 THR H OG1 
2427 C CG2 . THR B 144 ? 2.7122 2.9367 2.4388 -0.1450 0.1116  -0.1127 144 THR H CG2 
2428 N N   . ALA B 145 ? 3.1206 3.3706 2.8671 -0.1379 0.1365  -0.1452 145 ALA H N   
2429 C CA  . ALA B 145 ? 3.0717 3.3192 2.8313 -0.1325 0.1413  -0.1500 145 ALA H CA  
2430 C C   . ALA B 145 ? 2.8399 3.0708 2.6087 -0.1281 0.1360  -0.1392 145 ALA H C   
2431 O O   . ALA B 145 ? 2.9670 3.1975 2.7322 -0.1306 0.1307  -0.1256 145 ALA H O   
2432 C CB  . ALA B 145 ? 3.0900 3.3586 2.8483 -0.1360 0.1474  -0.1504 145 ALA H CB  
2433 N N   . ALA B 146 ? 2.6741 2.8910 2.4552 -0.1215 0.1370  -0.1454 146 ALA H N   
2434 C CA  . ALA B 146 ? 2.3798 2.5799 2.1701 -0.1169 0.1322  -0.1367 146 ALA H CA  
2435 C C   . ALA B 146 ? 2.1053 2.3087 1.9066 -0.1142 0.1361  -0.1358 146 ALA H C   
2436 O O   . ALA B 146 ? 2.1368 2.3475 1.9440 -0.1124 0.1427  -0.1467 146 ALA H O   
2437 C CB  . ALA B 146 ? 2.2620 2.4429 2.0584 -0.1118 0.1297  -0.1427 146 ALA H CB  
2438 N N   . LEU B 147 ? 1.8550 2.0531 1.6592 -0.1137 0.1317  -0.1227 147 LEU H N   
2439 C CA  . LEU B 147 ? 1.9457 2.1472 1.7595 -0.1118 0.1342  -0.1189 147 LEU H CA  
2440 C C   . LEU B 147 ? 2.0326 2.2154 1.8548 -0.1075 0.1284  -0.1101 147 LEU H C   
2441 O O   . LEU B 147 ? 2.1577 2.3322 1.9747 -0.1086 0.1217  -0.1002 147 LEU H O   
2442 C CB  . LEU B 147 ? 2.0535 2.2733 1.8605 -0.1175 0.1349  -0.1101 147 LEU H CB  
2443 C CG  . LEU B 147 ? 2.2145 2.4551 2.0139 -0.1221 0.1415  -0.1190 147 LEU H CG  
2444 C CD1 . LEU B 147 ? 2.3161 2.5749 2.1075 -0.1286 0.1414  -0.1093 147 LEU H CD1 
2445 C CD2 . LEU B 147 ? 1.8493 2.0933 1.6597 -0.1180 0.1490  -0.1307 147 LEU H CD2 
2446 N N   . GLY B 148 ? 1.8185 1.9950 1.6537 -0.1026 0.1309  -0.1136 148 GLY H N   
2447 C CA  . GLY B 148 ? 1.8309 1.9887 1.6744 -0.0983 0.1257  -0.1067 148 GLY H CA  
2448 C C   . GLY B 148 ? 2.1216 2.2801 1.9765 -0.0959 0.1276  -0.1030 148 GLY H C   
2449 O O   . GLY B 148 ? 2.1175 2.2900 1.9763 -0.0966 0.1338  -0.1079 148 GLY H O   
2450 N N   . CYS B 149 ? 2.0670 2.2102 1.9272 -0.0932 0.1219  -0.0939 149 CYS H N   
2451 C CA  . CYS B 149 ? 2.0500 2.1886 1.9224 -0.0901 0.1223  -0.0901 149 CYS H CA  
2452 C C   . CYS B 149 ? 1.8904 2.0079 1.7710 -0.0852 0.1182  -0.0902 149 CYS H C   
2453 O O   . CYS B 149 ? 1.7188 1.8244 1.5942 -0.0849 0.1128  -0.0870 149 CYS H O   
2454 C CB  . CYS B 149 ? 2.0497 2.1928 1.9199 -0.0927 0.1186  -0.0759 149 CYS H CB  
2455 S SG  . CYS B 149 ? 2.6367 2.8057 2.4992 -0.0988 0.1232  -0.0738 149 CYS H SG  
2456 N N   . LEU B 150 ? 2.0623 2.1756 1.9562 -0.0814 0.1207  -0.0937 150 LEU H N   
2457 C CA  . LEU B 150 ? 1.8614 1.9560 1.7649 -0.0769 0.1177  -0.0951 150 LEU H CA  
2458 C C   . LEU B 150 ? 1.7898 1.8774 1.7011 -0.0753 0.1145  -0.0848 150 LEU H C   
2459 O O   . LEU B 150 ? 2.0337 2.1292 1.9532 -0.0748 0.1183  -0.0849 150 LEU H O   
2460 C CB  . LEU B 150 ? 2.1598 2.2548 2.0735 -0.0739 0.1232  -0.1088 150 LEU H CB  
2461 C CG  . LEU B 150 ? 2.5059 2.6086 2.4127 -0.0753 0.1269  -0.1204 150 LEU H CG  
2462 C CD1 . LEU B 150 ? 2.4551 2.5571 2.3737 -0.0719 0.1319  -0.1339 150 LEU H CD1 
2463 C CD2 . LEU B 150 ? 2.4416 2.5341 2.3387 -0.0762 0.1215  -0.1184 150 LEU H CD2 
2464 N N   . VAL B 151 ? 1.6120 1.6853 1.5208 -0.0747 0.1075  -0.0759 151 VAL H N   
2465 C CA  . VAL B 151 ? 1.5139 1.5788 1.4289 -0.0733 0.1034  -0.0655 151 VAL H CA  
2466 C C   . VAL B 151 ? 1.5833 1.6314 1.5090 -0.0691 0.1016  -0.0687 151 VAL H C   
2467 O O   . VAL B 151 ? 1.6933 1.7282 1.6158 -0.0681 0.0971  -0.0679 151 VAL H O   
2468 C CB  . VAL B 151 ? 1.5843 1.6446 1.4895 -0.0755 0.0967  -0.0537 151 VAL H CB  
2469 C CG1 . VAL B 151 ? 1.7746 1.8242 1.6862 -0.0739 0.0919  -0.0436 151 VAL H CG1 
2470 C CG2 . VAL B 151 ? 1.5531 1.6307 1.4488 -0.0801 0.0981  -0.0499 151 VAL H CG2 
2471 N N   . LYS B 152 ? 1.5698 1.6183 1.5085 -0.0668 0.1049  -0.0721 152 LYS H N   
2472 C CA  . LYS B 152 ? 1.5286 1.5632 1.4783 -0.0631 0.1040  -0.0771 152 LYS H CA  
2473 C C   . LYS B 152 ? 1.6330 1.6600 1.5936 -0.0613 0.1016  -0.0696 152 LYS H C   
2474 O O   . LYS B 152 ? 1.8261 1.8589 1.7858 -0.0628 0.1009  -0.0611 152 LYS H O   
2475 C CB  . LYS B 152 ? 1.7569 1.7986 1.7138 -0.0617 0.1105  -0.0908 152 LYS H CB  
2476 C CG  . LYS B 152 ? 2.0129 2.0593 1.9593 -0.0633 0.1120  -0.0983 152 LYS H CG  
2477 C CD  . LYS B 152 ? 2.5713 2.6248 2.5243 -0.0620 0.1183  -0.1123 152 LYS H CD  
2478 C CE  . LYS B 152 ? 2.4781 2.5354 2.4198 -0.0639 0.1189  -0.1189 152 LYS H CE  
2479 N NZ  . LYS B 152 ? 2.6891 2.7536 2.6365 -0.0627 0.1248  -0.1330 152 LYS H NZ  
2480 N N   . ASP B 153 ? 1.7768 1.7906 1.7479 -0.0583 0.0999  -0.0726 153 ASP H N   
2481 C CA  . ASP B 153 ? 2.1557 2.1619 2.1394 -0.0564 0.0982  -0.0675 153 ASP H CA  
2482 C C   . ASP B 153 ? 2.1618 2.1631 2.1406 -0.0577 0.0927  -0.0539 153 ASP H C   
2483 O O   . ASP B 153 ? 2.1172 2.1253 2.0998 -0.0584 0.0936  -0.0481 153 ASP H O   
2484 C CB  . ASP B 153 ? 2.1892 2.2078 2.1844 -0.0555 0.1048  -0.0730 153 ASP H CB  
2485 C CG  . ASP B 153 ? 2.2127 2.2323 2.2166 -0.0533 0.1093  -0.0866 153 ASP H CG  
2486 O OD1 . ASP B 153 ? 2.2541 2.2625 2.2576 -0.0522 0.1066  -0.0906 153 ASP H OD1 
2487 O OD2 . ASP B 153 ? 2.1191 2.1512 2.1305 -0.0527 0.1156  -0.0934 153 ASP H OD2 
2488 N N   . TYR B 154 ? 1.9421 1.9318 1.9126 -0.0580 0.0868  -0.0490 154 TYR H N   
2489 C CA  . TYR B 154 ? 1.9069 1.8903 1.8724 -0.0591 0.0808  -0.0368 154 TYR H CA  
2490 C C   . TYR B 154 ? 2.0780 2.0438 2.0414 -0.0578 0.0748  -0.0342 154 TYR H C   
2491 O O   . TYR B 154 ? 2.1218 2.0838 2.0810 -0.0575 0.0748  -0.0403 154 TYR H O   
2492 C CB  . TYR B 154 ? 1.9028 1.8970 1.8553 -0.0621 0.0805  -0.0321 154 TYR H CB  
2493 C CG  . TYR B 154 ? 1.9795 1.9729 1.9204 -0.0631 0.0796  -0.0360 154 TYR H CG  
2494 C CD1 . TYR B 154 ? 1.8867 1.8899 1.8251 -0.0637 0.0849  -0.0462 154 TYR H CD1 
2495 C CD2 . TYR B 154 ? 2.0913 2.0740 2.0243 -0.0634 0.0733  -0.0297 154 TYR H CD2 
2496 C CE1 . TYR B 154 ? 1.7633 1.7655 1.6914 -0.0647 0.0837  -0.0494 154 TYR H CE1 
2497 C CE2 . TYR B 154 ? 1.9681 1.9500 1.8915 -0.0642 0.0724  -0.0330 154 TYR H CE2 
2498 C CZ  . TYR B 154 ? 1.8053 1.7969 1.7261 -0.0650 0.0775  -0.0425 154 TYR H CZ  
2499 O OH  . TYR B 154 ? 1.8757 1.8660 1.7869 -0.0659 0.0761  -0.0452 154 TYR H OH  
2500 N N   . PHE B 155 ? 2.0900 2.0454 2.0562 -0.0574 0.0696  -0.0252 155 PHE H N   
2501 C CA  . PHE B 155 ? 2.1775 2.1162 2.1438 -0.0561 0.0644  -0.0235 155 PHE H CA  
2502 C C   . PHE B 155 ? 2.1748 2.1069 2.1288 -0.0571 0.0588  -0.0170 155 PHE H C   
2503 O O   . PHE B 155 ? 2.1841 2.1061 2.1350 -0.0564 0.0560  -0.0188 155 PHE H O   
2504 C CB  . PHE B 155 ? 2.1806 2.1095 2.1583 -0.0548 0.0617  -0.0188 155 PHE H CB  
2505 C CG  . PHE B 155 ? 2.1877 2.1002 2.1638 -0.0541 0.0555  -0.0148 155 PHE H CG  
2506 C CD1 . PHE B 155 ? 2.2072 2.1124 2.1838 -0.0533 0.0551  -0.0211 155 PHE H CD1 
2507 C CD2 . PHE B 155 ? 2.1043 2.0089 2.0777 -0.0546 0.0499  -0.0048 155 PHE H CD2 
2508 C CE1 . PHE B 155 ? 2.0083 1.8994 1.9827 -0.0531 0.0496  -0.0174 155 PHE H CE1 
2509 C CE2 . PHE B 155 ? 2.1317 2.0219 2.1029 -0.0542 0.0445  -0.0016 155 PHE H CE2 
2510 C CZ  . PHE B 155 ? 1.9295 1.8132 1.9010 -0.0535 0.0444  -0.0078 155 PHE H CZ  
2511 N N   . PRO B 156 ? 2.0781 2.0147 2.0256 -0.0587 0.0565  -0.0091 156 PRO H N   
2512 C CA  . PRO B 156 ? 1.9336 1.8646 1.8698 -0.0594 0.0515  -0.0043 156 PRO H CA  
2513 C C   . PRO B 156 ? 2.0385 1.9786 1.9651 -0.0608 0.0540  -0.0093 156 PRO H C   
2514 O O   . PRO B 156 ? 2.2378 2.1916 2.1638 -0.0621 0.0589  -0.0134 156 PRO H O   
2515 C CB  . PRO B 156 ? 1.8187 1.7514 1.7533 -0.0606 0.0479  0.0062  156 PRO H CB  
2516 C CG  . PRO B 156 ? 2.0110 1.9429 1.9575 -0.0598 0.0492  0.0079  156 PRO H CG  
2517 C CD  . PRO B 156 ? 1.9534 1.8944 1.9063 -0.0593 0.0562  -0.0020 156 PRO H CD  
2518 N N   . GLU B 157 ? 1.8301 1.7624 1.7491 -0.0606 0.0505  -0.0093 157 GLU H N   
2519 C CA  . GLU B 157 ? 1.9374 1.8760 1.8474 -0.0618 0.0521  -0.0141 157 GLU H CA  
2520 C C   . GLU B 157 ? 2.1061 2.0562 2.0078 -0.0644 0.0519  -0.0096 157 GLU H C   
2521 O O   . GLU B 157 ? 2.3345 2.2959 2.2319 -0.0660 0.0558  -0.0149 157 GLU H O   
2522 C CB  . GLU B 157 ? 2.1079 2.0346 2.0128 -0.0608 0.0481  -0.0144 157 GLU H CB  
2523 C CG  . GLU B 157 ? 2.3373 2.2546 2.2490 -0.0589 0.0487  -0.0203 157 GLU H CG  
2524 C CD  . GLU B 157 ? 2.7774 2.6837 2.6838 -0.0582 0.0446  -0.0199 157 GLU H CD  
2525 O OE1 . GLU B 157 ? 2.7957 2.7004 2.6940 -0.0587 0.0409  -0.0145 157 GLU H OE1 
2526 O OE2 . GLU B 157 ? 2.8401 2.7397 2.7507 -0.0571 0.0450  -0.0249 157 GLU H OE2 
2527 N N   . PRO B 158 ? 1.8850 1.8330 1.7842 -0.0651 0.0471  0.0000  158 PRO H N   
2528 C CA  . PRO B 158 ? 1.9575 1.9161 1.8489 -0.0679 0.0461  0.0047  158 PRO H CA  
2529 C C   . PRO B 158 ? 2.1977 2.1727 2.0909 -0.0700 0.0514  0.0030  158 PRO H C   
2530 O O   . PRO B 158 ? 2.2930 2.2708 2.1934 -0.0699 0.0527  0.0057  158 PRO H O   
2531 C CB  . PRO B 158 ? 2.2072 2.1584 2.0985 -0.0677 0.0396  0.0153  158 PRO H CB  
2532 C CG  . PRO B 158 ? 2.2621 2.1972 2.1570 -0.0649 0.0366  0.0149  158 PRO H CG  
2533 C CD  . PRO B 158 ? 2.0384 1.9737 1.9412 -0.0636 0.0418  0.0072  158 PRO H CD  
2534 N N   . VAL B 159 ? 2.2066 2.1928 2.0929 -0.0723 0.0543  -0.0012 159 VAL H N   
2535 C CA  . VAL B 159 ? 2.2264 2.2300 2.1122 -0.0750 0.0592  -0.0027 159 VAL H CA  
2536 C C   . VAL B 159 ? 2.0778 2.0907 1.9530 -0.0785 0.0577  0.0001  159 VAL H C   
2537 O O   . VAL B 159 ? 1.9815 1.9904 1.8504 -0.0785 0.0561  -0.0027 159 VAL H O   
2538 C CB  . VAL B 159 ? 2.0421 2.0516 1.9323 -0.0742 0.0664  -0.0143 159 VAL H CB  
2539 C CG1 . VAL B 159 ? 2.0445 2.0731 1.9328 -0.0773 0.0716  -0.0163 159 VAL H CG1 
2540 C CG2 . VAL B 159 ? 2.1809 2.1824 2.0829 -0.0710 0.0677  -0.0164 159 VAL H CG2 
2541 N N   . THR B 160 ? 2.0662 2.0921 1.9400 -0.0817 0.0580  0.0059  160 THR H N   
2542 C CA  . THR B 160 ? 2.0557 2.0919 1.9200 -0.0857 0.0563  0.0095  160 THR H CA  
2543 C C   . THR B 160 ? 2.2260 2.2812 2.0887 -0.0890 0.0625  0.0056  160 THR H C   
2544 O O   . THR B 160 ? 2.2580 2.3213 2.1260 -0.0899 0.0648  0.0084  160 THR H O   
2545 C CB  . THR B 160 ? 2.0621 2.0959 1.9250 -0.0871 0.0492  0.0219  160 THR H CB  
2546 O OG1 . THR B 160 ? 2.0604 2.0989 1.9301 -0.0876 0.0498  0.0274  160 THR H OG1 
2547 C CG2 . THR B 160 ? 2.2448 2.2602 2.1084 -0.0839 0.0432  0.0248  160 THR H CG2 
2548 N N   . VAL B 161 ? 2.1235 2.1864 1.9790 -0.0911 0.0652  -0.0007 161 VAL H N   
2549 C CA  . VAL B 161 ? 1.9795 2.0606 1.8321 -0.0944 0.0715  -0.0060 161 VAL H CA  
2550 C C   . VAL B 161 ? 2.0517 2.1438 1.8943 -0.0994 0.0688  -0.0004 161 VAL H C   
2551 O O   . VAL B 161 ? 1.8522 1.9390 1.6884 -0.0999 0.0654  -0.0004 161 VAL H O   
2552 C CB  . VAL B 161 ? 1.7525 1.8340 1.6054 -0.0927 0.0775  -0.0195 161 VAL H CB  
2553 C CG1 . VAL B 161 ? 1.6059 1.7069 1.4548 -0.0964 0.0838  -0.0252 161 VAL H CG1 
2554 C CG2 . VAL B 161 ? 2.0994 2.1702 1.9632 -0.0879 0.0798  -0.0248 161 VAL H CG2 
2555 N N   . SER B 162 ? 2.3046 2.4122 2.1462 -0.1034 0.0702  0.0047  162 SER H N   
2556 C CA  . SER B 162 ? 2.2223 2.3441 2.0546 -0.1091 0.0690  0.0087  162 SER H CA  
2557 C C   . SER B 162 ? 2.1690 2.3084 1.9985 -0.1119 0.0770  -0.0001 162 SER H C   
2558 O O   . SER B 162 ? 2.1643 2.3073 2.0005 -0.1099 0.0829  -0.0062 162 SER H O   
2559 C CB  . SER B 162 ? 2.2935 2.4204 2.1262 -0.1123 0.0636  0.0222  162 SER H CB  
2560 O OG  . SER B 162 ? 2.3374 2.4733 2.1766 -0.1127 0.0674  0.0239  162 SER H OG  
2561 N N   . TRP B 163 ? 2.3268 2.4772 2.1465 -0.1165 0.0773  -0.0010 163 TRP H N   
2562 C CA  . TRP B 163 ? 2.5367 2.7045 2.3521 -0.1196 0.0846  -0.0096 163 TRP H CA  
2563 C C   . TRP B 163 ? 2.5499 2.7361 2.3589 -0.1265 0.0834  -0.0012 163 TRP H C   
2564 O O   . TRP B 163 ? 2.5300 2.7175 2.3316 -0.1301 0.0781  0.0052  163 TRP H O   
2565 C CB  . TRP B 163 ? 2.5890 2.7542 2.3980 -0.1194 0.0864  -0.0197 163 TRP H CB  
2566 C CG  . TRP B 163 ? 2.5310 2.6886 2.3459 -0.1144 0.0919  -0.0326 163 TRP H CG  
2567 C CD1 . TRP B 163 ? 2.2418 2.3807 2.0623 -0.1090 0.0898  -0.0356 163 TRP H CD1 
2568 C CD2 . TRP B 163 ? 2.5687 2.7379 2.3847 -0.1146 0.1002  -0.0444 163 TRP H CD2 
2569 N NE1 . TRP B 163 ? 2.2761 2.4138 2.1016 -0.1059 0.0959  -0.0481 163 TRP H NE1 
2570 C CE2 . TRP B 163 ? 2.3870 2.5429 2.2101 -0.1090 0.1024  -0.0539 163 TRP H CE2 
2571 C CE3 . TRP B 163 ? 2.6877 2.8774 2.4994 -0.1190 0.1059  -0.0479 163 TRP H CE3 
2572 C CZ2 . TRP B 163 ? 2.3477 2.5096 2.1745 -0.1075 0.1098  -0.0670 163 TRP H CZ2 
2573 C CZ3 . TRP B 163 ? 2.6344 2.8304 2.4492 -0.1174 0.1137  -0.0613 163 TRP H CZ3 
2574 C CH2 . TRP B 163 ? 2.4344 2.6163 2.2570 -0.1115 0.1155  -0.0707 163 TRP H CH2 
2575 N N   . ASN B 164 ? 2.4400 2.6405 2.2523 -0.1283 0.0883  -0.0010 164 ASN H N   
2576 C CA  . ASN B 164 ? 2.5310 2.7498 2.3387 -0.1349 0.0872  0.0082  164 ASN H CA  
2577 C C   . ASN B 164 ? 2.7011 2.9128 2.5084 -0.1366 0.0775  0.0231  164 ASN H C   
2578 O O   . ASN B 164 ? 2.8911 3.1063 2.6906 -0.1409 0.0726  0.0287  164 ASN H O   
2579 C CB  . ASN B 164 ? 2.6625 2.8979 2.4590 -0.1406 0.0906  0.0030  164 ASN H CB  
2580 C CG  . ASN B 164 ? 2.6047 2.8511 2.4018 -0.1398 0.1006  -0.0108 164 ASN H CG  
2581 O OD1 . ASN B 164 ? 2.6121 2.8529 2.4075 -0.1373 0.1038  -0.0223 164 ASN H OD1 
2582 N ND2 . ASN B 164 ? 2.6459 2.9087 2.4455 -0.1424 0.1053  -0.0097 164 ASN H ND2 
2583 N N   . SER B 165 ? 2.5268 2.7283 2.3432 -0.1330 0.0746  0.0292  165 SER H N   
2584 C CA  . SER B 165 ? 2.5559 2.7484 2.3743 -0.1335 0.0653  0.0427  165 SER H CA  
2585 C C   . SER B 165 ? 2.6121 2.7894 2.4264 -0.1318 0.0591  0.0433  165 SER H C   
2586 O O   . SER B 165 ? 2.8057 2.9790 2.6189 -0.1336 0.0512  0.0540  165 SER H O   
2587 C CB  . SER B 165 ? 2.4783 2.6880 2.2929 -0.1406 0.0622  0.0541  165 SER H CB  
2588 O OG  . SER B 165 ? 2.7151 2.9365 2.5194 -0.1460 0.0622  0.0530  165 SER H OG  
2589 N N   . GLY B 166 ? 2.5406 2.7094 2.3534 -0.1282 0.0626  0.0321  166 GLY H N   
2590 C CA  . GLY B 166 ? 2.4097 2.5666 2.2179 -0.1270 0.0577  0.0317  166 GLY H CA  
2591 C C   . GLY B 166 ? 2.4344 2.6029 2.2325 -0.1329 0.0562  0.0331  166 GLY H C   
2592 O O   . GLY B 166 ? 2.2932 2.4528 2.0875 -0.1323 0.0521  0.0330  166 GLY H O   
2593 N N   . ALA B 167 ? 2.5112 2.6997 2.3050 -0.1387 0.0593  0.0346  167 ALA H N   
2594 C CA  . ALA B 167 ? 2.4069 2.6074 2.1906 -0.1449 0.0578  0.0363  167 ALA H CA  
2595 C C   . ALA B 167 ? 2.5300 2.7288 2.3080 -0.1439 0.0622  0.0239  167 ALA H C   
2596 O O   . ALA B 167 ? 2.5411 2.7411 2.3119 -0.1470 0.0587  0.0252  167 ALA H O   
2597 C CB  . ALA B 167 ? 2.2746 2.4978 2.0548 -0.1516 0.0608  0.0401  167 ALA H CB  
2598 N N   . LEU B 168 ? 2.6774 2.8733 2.4588 -0.1397 0.0693  0.0120  168 LEU H N   
2599 C CA  . LEU B 168 ? 2.6951 2.8873 2.4721 -0.1381 0.0729  0.0001  168 LEU H CA  
2600 C C   . LEU B 168 ? 2.6630 2.8347 2.4421 -0.1334 0.0674  0.0009  168 LEU H C   
2601 O O   . LEU B 168 ? 2.9539 3.1112 2.7410 -0.1276 0.0673  -0.0009 168 LEU H O   
2602 C CB  . LEU B 168 ? 2.6650 2.8593 2.4464 -0.1347 0.0816  -0.0127 168 LEU H CB  
2603 C CG  . LEU B 168 ? 2.7454 2.9604 2.5249 -0.1386 0.0886  -0.0165 168 LEU H CG  
2604 C CD1 . LEU B 168 ? 2.7693 2.9812 2.5558 -0.1335 0.0960  -0.0291 168 LEU H CD1 
2605 C CD2 . LEU B 168 ? 2.7418 2.9725 2.5096 -0.1451 0.0900  -0.0191 168 LEU H CD2 
2606 N N   . THR B 169 ? 2.7616 2.9324 2.5338 -0.1362 0.0629  0.0036  169 THR H N   
2607 C CA  . THR B 169 ? 2.5579 2.7109 2.3315 -0.1324 0.0572  0.0053  169 THR H CA  
2608 C C   . THR B 169 ? 2.6049 2.7527 2.3744 -0.1309 0.0596  -0.0052 169 THR H C   
2609 O O   . THR B 169 ? 2.5443 2.6775 2.3153 -0.1275 0.0557  -0.0048 169 THR H O   
2610 C CB  . THR B 169 ? 2.2248 2.3785 1.9954 -0.1361 0.0489  0.0177  169 THR H CB  
2611 O OG1 . THR B 169 ? 2.1670 2.3359 1.9285 -0.1427 0.0492  0.0180  169 THR H OG1 
2612 C CG2 . THR B 169 ? 2.0473 2.2037 1.8230 -0.1371 0.0454  0.0288  169 THR H CG2 
2613 N N   . SER B 170 ? 2.7725 2.9322 2.5370 -0.1334 0.0659  -0.0144 170 SER H N   
2614 C CA  . SER B 170 ? 2.6902 2.8465 2.4501 -0.1329 0.0677  -0.0239 170 SER H CA  
2615 C C   . SER B 170 ? 2.7002 2.8598 2.4624 -0.1306 0.0759  -0.0371 170 SER H C   
2616 O O   . SER B 170 ? 2.8463 3.0177 2.6098 -0.1321 0.0808  -0.0392 170 SER H O   
2617 C CB  . SER B 170 ? 2.8058 2.9746 2.5552 -0.1396 0.0658  -0.0216 170 SER H CB  
2618 O OG  . SER B 170 ? 2.9742 3.1622 2.7190 -0.1448 0.0704  -0.0230 170 SER H OG  
2619 N N   . GLY B 171 ? 2.7204 2.8693 2.4836 -0.1270 0.0771  -0.0461 171 GLY H N   
2620 C CA  . GLY B 171 ? 2.5745 2.7250 2.3406 -0.1246 0.0842  -0.0591 171 GLY H CA  
2621 C C   . GLY B 171 ? 2.5775 2.7173 2.3550 -0.1187 0.0860  -0.0610 171 GLY H C   
2622 O O   . GLY B 171 ? 2.5732 2.7079 2.3558 -0.1150 0.0902  -0.0714 171 GLY H O   
2623 N N   . VAL B 172 ? 2.6785 2.8148 2.4605 -0.1178 0.0825  -0.0507 172 VAL H N   
2624 C CA  . VAL B 172 ? 2.7676 2.8938 2.5605 -0.1125 0.0836  -0.0510 172 VAL H CA  
2625 C C   . VAL B 172 ? 2.5767 2.6839 2.3737 -0.1076 0.0807  -0.0537 172 VAL H C   
2626 O O   . VAL B 172 ? 3.0195 3.1180 2.8137 -0.1074 0.0747  -0.0472 172 VAL H O   
2627 C CB  . VAL B 172 ? 2.7970 2.9236 2.5931 -0.1132 0.0797  -0.0385 172 VAL H CB  
2628 C CG1 . VAL B 172 ? 2.5725 2.6875 2.3797 -0.1078 0.0803  -0.0387 172 VAL H CG1 
2629 C CG2 . VAL B 172 ? 2.8243 2.9704 2.6161 -0.1187 0.0820  -0.0347 172 VAL H CG2 
2630 N N   . HIS B 173 ? 2.6634 2.7646 2.4674 -0.1036 0.0848  -0.0632 173 HIS H N   
2631 C CA  . HIS B 173 ? 2.3236 2.4071 2.1323 -0.0989 0.0823  -0.0659 173 HIS H CA  
2632 C C   . HIS B 173 ? 2.2623 2.3375 2.0825 -0.0944 0.0839  -0.0670 173 HIS H C   
2633 O O   . HIS B 173 ? 2.2576 2.3316 2.0839 -0.0921 0.0884  -0.0766 173 HIS H O   
2634 C CB  . HIS B 173 ? 2.0892 2.1720 1.8951 -0.0988 0.0847  -0.0768 173 HIS H CB  
2635 C CG  . HIS B 173 ? 2.3680 2.4598 2.1626 -0.1036 0.0834  -0.0762 173 HIS H CG  
2636 N ND1 . HIS B 173 ? 2.2984 2.4015 2.0880 -0.1063 0.0880  -0.0854 173 HIS H ND1 
2637 C CD2 . HIS B 173 ? 2.4788 2.5700 2.2666 -0.1061 0.0779  -0.0676 173 HIS H CD2 
2638 C CE1 . HIS B 173 ? 2.0987 2.2077 1.8785 -0.1106 0.0852  -0.0821 173 HIS H CE1 
2639 N NE2 . HIS B 173 ? 2.3235 2.4255 2.1024 -0.1105 0.0791  -0.0712 173 HIS H NE2 
2640 N N   . THR B 174 ? 2.1635 2.2329 1.9871 -0.0934 0.0800  -0.0571 174 THR H N   
2641 C CA  . THR B 174 ? 1.9276 1.9863 1.7619 -0.0890 0.0801  -0.0568 174 THR H CA  
2642 C C   . THR B 174 ? 1.8726 1.9158 1.7105 -0.0853 0.0784  -0.0617 174 THR H C   
2643 O O   . THR B 174 ? 1.8727 1.9091 1.7053 -0.0854 0.0742  -0.0593 174 THR H O   
2644 C CB  . THR B 174 ? 1.9147 1.9691 1.7507 -0.0888 0.0752  -0.0447 174 THR H CB  
2645 O OG1 . THR B 174 ? 2.0053 2.0515 1.8359 -0.0891 0.0690  -0.0383 174 THR H OG1 
2646 C CG2 . THR B 174 ? 1.9940 2.0642 1.8272 -0.0928 0.0767  -0.0393 174 THR H CG2 
2647 N N   . PHE B 175 ? 1.8886 1.9267 1.7357 -0.0821 0.0816  -0.0683 175 PHE H N   
2648 C CA  . PHE B 175 ? 1.7933 1.8182 1.6447 -0.0789 0.0805  -0.0738 175 PHE H CA  
2649 C C   . PHE B 175 ? 1.8442 1.8548 1.7035 -0.0756 0.0769  -0.0683 175 PHE H C   
2650 O O   . PHE B 175 ? 1.9929 2.0047 1.8570 -0.0751 0.0771  -0.0631 175 PHE H O   
2651 C CB  . PHE B 175 ? 1.8732 1.9020 1.7302 -0.0779 0.0862  -0.0861 175 PHE H CB  
2652 C CG  . PHE B 175 ? 1.8747 1.9133 1.7237 -0.0807 0.0887  -0.0933 175 PHE H CG  
2653 C CD1 . PHE B 175 ? 1.9267 1.9585 1.7713 -0.0806 0.0862  -0.0962 175 PHE H CD1 
2654 C CD2 . PHE B 175 ? 2.0333 2.0882 1.8785 -0.0836 0.0935  -0.0968 175 PHE H CD2 
2655 C CE1 . PHE B 175 ? 2.1567 2.1973 1.9937 -0.0834 0.0883  -0.1026 175 PHE H CE1 
2656 C CE2 . PHE B 175 ? 2.1687 2.2327 2.0060 -0.0865 0.0957  -0.1034 175 PHE H CE2 
2657 C CZ  . PHE B 175 ? 2.1588 2.2153 1.9919 -0.0864 0.0930  -0.1063 175 PHE H CZ  
2658 N N   . PRO B 176 ? 1.5760 1.5734 1.4366 -0.0734 0.0736  -0.0689 176 PRO H N   
2659 C CA  . PRO B 176 ? 1.4020 1.3859 1.2696 -0.0705 0.0702  -0.0638 176 PRO H CA  
2660 C C   . PRO B 176 ? 1.7478 1.7299 1.6272 -0.0683 0.0735  -0.0686 176 PRO H C   
2661 O O   . PRO B 176 ? 1.7095 1.6949 1.5930 -0.0678 0.0776  -0.0781 176 PRO H O   
2662 C CB  . PRO B 176 ? 1.1597 1.1321 1.0252 -0.0693 0.0667  -0.0650 176 PRO H CB  
2663 C CG  . PRO B 176 ? 1.4528 1.4327 1.3082 -0.0719 0.0667  -0.0666 176 PRO H CG  
2664 C CD  . PRO B 176 ? 1.5525 1.5467 1.4070 -0.0740 0.0721  -0.0727 176 PRO H CD  
2665 N N   . ALA B 177 ? 1.8875 1.8641 1.7727 -0.0669 0.0716  -0.0619 177 ALA H N   
2666 C CA  . ALA B 177 ? 2.0344 2.0092 1.9316 -0.0649 0.0743  -0.0652 177 ALA H CA  
2667 C C   . ALA B 177 ? 2.0358 1.9992 1.9400 -0.0625 0.0736  -0.0712 177 ALA H C   
2668 O O   . ALA B 177 ? 2.2336 2.1869 2.1345 -0.0620 0.0696  -0.0692 177 ALA H O   
2669 C CB  . ALA B 177 ? 2.1848 2.1550 2.0862 -0.0642 0.0715  -0.0558 177 ALA H CB  
2670 N N   . VAL B 178 ? 1.7971 1.7626 1.7115 -0.0612 0.0776  -0.0785 178 VAL H N   
2671 C CA  . VAL B 178 ? 1.8904 1.8454 1.8140 -0.0590 0.0768  -0.0839 178 VAL H CA  
2672 C C   . VAL B 178 ? 1.9656 1.9160 1.9017 -0.0572 0.0770  -0.0817 178 VAL H C   
2673 O O   . VAL B 178 ? 2.0600 2.0197 2.0015 -0.0571 0.0812  -0.0838 178 VAL H O   
2674 C CB  . VAL B 178 ? 2.0485 2.0091 1.9741 -0.0590 0.0810  -0.0957 178 VAL H CB  
2675 C CG1 . VAL B 178 ? 2.0201 1.9699 1.9570 -0.0568 0.0797  -0.1007 178 VAL H CG1 
2676 C CG2 . VAL B 178 ? 2.0559 2.0204 1.9689 -0.0611 0.0803  -0.0973 178 VAL H CG2 
2677 N N   . LEU B 179 ? 1.8426 1.7793 1.7832 -0.0559 0.0724  -0.0769 179 LEU H N   
2678 C CA  . LEU B 179 ? 1.6425 1.5728 1.5964 -0.0542 0.0719  -0.0757 179 LEU H CA  
2679 C C   . LEU B 179 ? 1.8285 1.7636 1.7939 -0.0529 0.0767  -0.0858 179 LEU H C   
2680 O O   . LEU B 179 ? 1.6701 1.6018 1.6387 -0.0524 0.0768  -0.0931 179 LEU H O   
2681 C CB  . LEU B 179 ? 1.7486 1.6634 1.7050 -0.0534 0.0663  -0.0716 179 LEU H CB  
2682 C CG  . LEU B 179 ? 2.0500 1.9581 1.9978 -0.0541 0.0612  -0.0613 179 LEU H CG  
2683 C CD1 . LEU B 179 ? 2.1685 2.0627 2.1175 -0.0536 0.0562  -0.0588 179 LEU H CD1 
2684 C CD2 . LEU B 179 ? 1.8785 1.7871 1.8316 -0.0538 0.0610  -0.0547 179 LEU H CD2 
2685 N N   . GLN B 180 ? 1.9879 1.9313 1.9602 -0.0525 0.0805  -0.0866 180 GLN H N   
2686 C CA  . GLN B 180 ? 2.1154 2.0611 2.1016 -0.0507 0.0844  -0.0955 180 GLN H CA  
2687 C C   . GLN B 180 ? 2.1333 2.0643 2.1310 -0.0492 0.0801  -0.0938 180 GLN H C   
2688 O O   . GLN B 180 ? 2.0971 2.0197 2.0954 -0.0492 0.0759  -0.0845 180 GLN H O   
2689 C CB  . GLN B 180 ? 2.0611 2.0182 2.0534 -0.0504 0.0891  -0.0956 180 GLN H CB  
2690 C CG  . GLN B 180 ? 1.8668 1.8401 1.8489 -0.0523 0.0939  -0.0981 180 GLN H CG  
2691 C CD  . GLN B 180 ? 1.7679 1.7530 1.7563 -0.0522 0.0985  -0.0977 180 GLN H CD  
2692 O OE1 . GLN B 180 ? 1.8039 1.7845 1.8015 -0.0511 0.0971  -0.0921 180 GLN H OE1 
2693 N NE2 . GLN B 180 ? 1.7610 1.7618 1.7444 -0.0535 0.1041  -0.1036 180 GLN H NE2 
2694 N N   . SER B 181 ? 2.0191 1.9470 2.0257 -0.0480 0.0810  -0.1026 181 SER H N   
2695 C CA  . SER B 181 ? 2.0772 1.9913 2.0945 -0.0470 0.0764  -0.1012 181 SER H CA  
2696 C C   . SER B 181 ? 2.2143 2.1238 2.2424 -0.0462 0.0750  -0.0946 181 SER H C   
2697 O O   . SER B 181 ? 2.2333 2.1304 2.2663 -0.0462 0.0698  -0.0891 181 SER H O   
2698 C CB  . SER B 181 ? 2.1431 2.0567 2.1711 -0.0458 0.0781  -0.1124 181 SER H CB  
2699 O OG  . SER B 181 ? 2.4179 2.3413 2.4560 -0.0444 0.0838  -0.1195 181 SER H OG  
2700 N N   . SER B 182 ? 2.2053 2.1250 2.2371 -0.0457 0.0793  -0.0949 182 SER H N   
2701 C CA  . SER B 182 ? 2.0550 1.9716 2.0963 -0.0450 0.0782  -0.0881 182 SER H CA  
2702 C C   . SER B 182 ? 2.0294 1.9431 2.0602 -0.0465 0.0745  -0.0760 182 SER H C   
2703 O O   . SER B 182 ? 2.1425 2.0554 2.1794 -0.0462 0.0738  -0.0697 182 SER H O   
2704 C CB  . SER B 182 ? 2.1458 2.0753 2.1963 -0.0439 0.0846  -0.0935 182 SER H CB  
2705 O OG  . SER B 182 ? 2.0034 1.9466 2.0420 -0.0451 0.0887  -0.0941 182 SER H OG  
2706 N N   . GLY B 183 ? 2.0001 1.9121 2.0158 -0.0479 0.0721  -0.0728 183 GLY H N   
2707 C CA  . GLY B 183 ? 1.9487 1.8563 1.9548 -0.0491 0.0678  -0.0619 183 GLY H CA  
2708 C C   . GLY B 183 ? 1.9209 1.8403 1.9159 -0.0504 0.0702  -0.0588 183 GLY H C   
2709 O O   . GLY B 183 ? 2.1610 2.0771 2.1462 -0.0515 0.0664  -0.0505 183 GLY H O   
2710 N N   . LEU B 184 ? 1.9608 1.8941 1.9574 -0.0504 0.0763  -0.0652 184 LEU H N   
2711 C CA  . LEU B 184 ? 2.0614 2.0072 2.0482 -0.0521 0.0786  -0.0620 184 LEU H CA  
2712 C C   . LEU B 184 ? 2.1364 2.0858 2.1090 -0.0536 0.0786  -0.0646 184 LEU H C   
2713 O O   . LEU B 184 ? 2.1121 2.0532 2.0818 -0.0533 0.0761  -0.0673 184 LEU H O   
2714 C CB  . LEU B 184 ? 2.1181 2.0779 2.1126 -0.0518 0.0851  -0.0673 184 LEU H CB  
2715 C CG  . LEU B 184 ? 2.0784 2.0365 2.0870 -0.0504 0.0855  -0.0640 184 LEU H CG  
2716 C CD1 . LEU B 184 ? 2.1176 2.0906 2.1341 -0.0499 0.0927  -0.0712 184 LEU H CD1 
2717 C CD2 . LEU B 184 ? 1.8236 1.7789 1.8278 -0.0516 0.0813  -0.0514 184 LEU H CD2 
2718 N N   . TYR B 185 ? 2.0079 1.9701 1.9716 -0.0555 0.0812  -0.0633 185 TYR H N   
2719 C CA  . TYR B 185 ? 1.8955 1.8627 1.8455 -0.0574 0.0810  -0.0645 185 TYR H CA  
2720 C C   . TYR B 185 ? 1.8610 1.8453 1.8078 -0.0589 0.0872  -0.0711 185 TYR H C   
2721 O O   . TYR B 185 ? 1.8180 1.8120 1.7709 -0.0590 0.0912  -0.0718 185 TYR H O   
2722 C CB  . TYR B 185 ? 1.8678 1.8323 1.8076 -0.0590 0.0760  -0.0534 185 TYR H CB  
2723 C CG  . TYR B 185 ? 2.1095 2.0578 2.0485 -0.0579 0.0695  -0.0473 185 TYR H CG  
2724 C CD1 . TYR B 185 ? 2.0585 2.0004 1.9891 -0.0582 0.0665  -0.0479 185 TYR H CD1 
2725 C CD2 . TYR B 185 ? 2.2554 2.1947 2.2026 -0.0567 0.0667  -0.0414 185 TYR H CD2 
2726 C CE1 . TYR B 185 ? 2.0311 1.9590 1.9608 -0.0574 0.0609  -0.0426 185 TYR H CE1 
2727 C CE2 . TYR B 185 ? 2.1651 2.0901 2.1113 -0.0560 0.0610  -0.0363 185 TYR H CE2 
2728 C CZ  . TYR B 185 ? 2.1790 2.0985 2.1164 -0.0563 0.0582  -0.0369 185 TYR H CZ  
2729 O OH  . TYR B 185 ? 2.2634 2.1694 2.1999 -0.0556 0.0528  -0.0318 185 TYR H OH  
2730 N N   . SER B 186 ? 1.7871 1.7756 1.7240 -0.0604 0.0879  -0.0757 186 SER H N   
2731 C CA  . SER B 186 ? 1.5805 1.5852 1.5124 -0.0623 0.0935  -0.0823 186 SER H CA  
2732 C C   . SER B 186 ? 1.4584 1.4665 1.3757 -0.0650 0.0915  -0.0803 186 SER H C   
2733 O O   . SER B 186 ? 1.7067 1.7072 1.6203 -0.0646 0.0893  -0.0836 186 SER H O   
2734 C CB  . SER B 186 ? 1.6427 1.6498 1.5827 -0.0607 0.0983  -0.0953 186 SER H CB  
2735 O OG  . SER B 186 ? 1.7727 1.7786 1.7272 -0.0583 0.1005  -0.0973 186 SER H OG  
2736 N N   . LEU B 187 ? 1.5143 1.5334 1.4237 -0.0678 0.0919  -0.0745 187 LEU H N   
2737 C CA  . LEU B 187 ? 1.6423 1.6686 1.5383 -0.0710 0.0909  -0.0731 187 LEU H CA  
2738 C C   . LEU B 187 ? 1.8506 1.8939 1.7432 -0.0733 0.0972  -0.0812 187 LEU H C   
2739 O O   . LEU B 187 ? 1.9619 2.0149 1.8607 -0.0732 0.1021  -0.0843 187 LEU H O   
2740 C CB  . LEU B 187 ? 1.7393 1.7674 1.6289 -0.0731 0.0867  -0.0608 187 LEU H CB  
2741 C CG  . LEU B 187 ? 2.2210 2.2341 2.1101 -0.0717 0.0798  -0.0515 187 LEU H CG  
2742 C CD1 . LEU B 187 ? 2.3893 2.4071 2.2741 -0.0740 0.0766  -0.0404 187 LEU H CD1 
2743 C CD2 . LEU B 187 ? 2.0118 2.0178 1.8933 -0.0719 0.0765  -0.0529 187 LEU H CD2 
2744 N N   . SER B 188 ? 1.6390 1.6862 1.5213 -0.0755 0.0970  -0.0844 188 SER H N   
2745 C CA  . SER B 188 ? 1.7875 1.8512 1.6638 -0.0785 0.1022  -0.0913 188 SER H CA  
2746 C C   . SER B 188 ? 1.8467 1.9171 1.7097 -0.0826 0.0992  -0.0842 188 SER H C   
2747 O O   . SER B 188 ? 1.8750 1.9367 1.7321 -0.0828 0.0945  -0.0813 188 SER H O   
2748 C CB  . SER B 188 ? 1.8067 1.8687 1.6844 -0.0773 0.1051  -0.1040 188 SER H CB  
2749 O OG  . SER B 188 ? 1.6954 1.7470 1.5671 -0.0772 0.1004  -0.1030 188 SER H OG  
2750 N N   . SER B 189 ? 2.0619 2.1479 1.9206 -0.0861 0.1017  -0.0811 189 SER H N   
2751 C CA  . SER B 189 ? 1.9592 2.0531 1.8061 -0.0906 0.0987  -0.0735 189 SER H CA  
2752 C C   . SER B 189 ? 1.9068 2.0187 1.7468 -0.0945 0.1040  -0.0804 189 SER H C   
2753 O O   . SER B 189 ? 1.9559 2.0807 1.7989 -0.0956 0.1092  -0.0829 189 SER H O   
2754 C CB  . SER B 189 ? 2.0905 2.1865 1.9383 -0.0918 0.0954  -0.0609 189 SER H CB  
2755 O OG  . SER B 189 ? 1.9975 2.0766 1.8498 -0.0887 0.0897  -0.0541 189 SER H OG  
2756 N N   . VAL B 190 ? 2.0477 2.1610 1.8784 -0.0968 0.1029  -0.0836 190 VAL H N   
2757 C CA  . VAL B 190 ? 2.1830 2.3121 2.0065 -0.1004 0.1078  -0.0916 190 VAL H CA  
2758 C C   . VAL B 190 ? 2.3131 2.4497 2.1239 -0.1057 0.1042  -0.0846 190 VAL H C   
2759 O O   . VAL B 190 ? 2.5144 2.6415 2.3221 -0.1058 0.0978  -0.0760 190 VAL H O   
2760 C CB  . VAL B 190 ? 2.1977 2.3221 2.0229 -0.0982 0.1109  -0.1050 190 VAL H CB  
2761 C CG1 . VAL B 190 ? 2.4228 2.5439 2.2611 -0.0938 0.1155  -0.1131 190 VAL H CG1 
2762 C CG2 . VAL B 190 ? 2.1914 2.2998 2.0148 -0.0964 0.1051  -0.1032 190 VAL H CG2 
2763 N N   . VAL B 191 ? 2.1842 2.3385 1.9878 -0.1103 0.1084  -0.0886 191 VAL H N   
2764 C CA  . VAL B 191 ? 2.0517 2.2168 1.8433 -0.1163 0.1058  -0.0823 191 VAL H CA  
2765 C C   . VAL B 191 ? 2.0810 2.2573 1.8654 -0.1192 0.1105  -0.0935 191 VAL H C   
2766 O O   . VAL B 191 ? 2.2091 2.3913 1.9976 -0.1178 0.1170  -0.1045 191 VAL H O   
2767 C CB  . VAL B 191 ? 2.2576 2.4367 2.0479 -0.1202 0.1059  -0.0727 191 VAL H CB  
2768 C CG1 . VAL B 191 ? 2.1098 2.3010 1.8879 -0.1270 0.1029  -0.0661 191 VAL H CG1 
2769 C CG2 . VAL B 191 ? 2.7042 2.8724 2.5024 -0.1172 0.1015  -0.0623 191 VAL H CG2 
2770 N N   . THR B 192 ? 2.0673 2.2465 1.8410 -0.1234 0.1070  -0.0909 192 THR H N   
2771 C CA  . THR B 192 ? 2.1214 2.3113 1.8867 -0.1269 0.1107  -0.1006 192 THR H CA  
2772 C C   . THR B 192 ? 1.9573 2.1646 1.7115 -0.1344 0.1097  -0.0935 192 THR H C   
2773 O O   . THR B 192 ? 1.8326 2.0374 1.5807 -0.1373 0.1034  -0.0844 192 THR H O   
2774 C CB  . THR B 192 ? 2.0217 2.1988 1.7846 -0.1253 0.1074  -0.1050 192 THR H CB  
2775 O OG1 . THR B 192 ? 2.0917 2.2616 1.8505 -0.1267 0.0999  -0.0933 192 THR H OG1 
2776 C CG2 . THR B 192 ? 1.7765 1.9375 1.5507 -0.1183 0.1084  -0.1120 192 THR H CG2 
2777 N N   . VAL B 193 ? 2.0453 2.2705 1.7973 -0.1375 0.1157  -0.0978 193 VAL H N   
2778 C CA  . VAL B 193 ? 2.2845 2.5283 2.0260 -0.1452 0.1154  -0.0915 193 VAL H CA  
2779 C C   . VAL B 193 ? 2.6914 2.9503 2.4257 -0.1486 0.1219  -0.1040 193 VAL H C   
2780 O O   . VAL B 193 ? 2.9871 3.2492 2.7271 -0.1455 0.1287  -0.1153 193 VAL H O   
2781 C CB  . VAL B 193 ? 2.2929 2.5462 2.0384 -0.1466 0.1161  -0.0823 193 VAL H CB  
2782 C CG1 . VAL B 193 ? 2.4128 2.6870 2.1477 -0.1550 0.1161  -0.0763 193 VAL H CG1 
2783 C CG2 . VAL B 193 ? 2.1687 2.4069 1.9209 -0.1435 0.1090  -0.0699 193 VAL H CG2 
2784 N N   . PRO B 194 ? 2.6303 2.8986 2.3523 -0.1549 0.1199  -0.1026 194 PRO H N   
2785 C CA  . PRO B 194 ? 2.5717 2.8513 2.2894 -0.1571 0.1244  -0.1140 194 PRO H CA  
2786 C C   . PRO B 194 ? 2.6348 2.9290 2.3574 -0.1569 0.1314  -0.1194 194 PRO H C   
2787 O O   . PRO B 194 ? 2.5961 2.9001 2.3197 -0.1593 0.1317  -0.1107 194 PRO H O   
2788 C CB  . PRO B 194 ? 2.3241 2.6110 2.0332 -0.1634 0.1183  -0.1052 194 PRO H CB  
2789 C CG  . PRO B 194 ? 2.5514 2.8362 2.2589 -0.1659 0.1124  -0.0893 194 PRO H CG  
2790 C CD  . PRO B 194 ? 2.5495 2.8165 2.2644 -0.1595 0.1120  -0.0896 194 PRO H CD  
2791 N N   . SER B 195 ? 2.7296 3.0253 2.4560 -0.1540 0.1368  -0.1339 195 SER H N   
2792 C CA  . SER B 195 ? 2.6685 2.9777 2.4003 -0.1532 0.1438  -0.1408 195 SER H CA  
2793 C C   . SER B 195 ? 2.7185 3.0467 2.4448 -0.1596 0.1432  -0.1339 195 SER H C   
2794 O O   . SER B 195 ? 2.6024 2.9434 2.3327 -0.1597 0.1486  -0.1372 195 SER H O   
2795 C CB  . SER B 195 ? 2.6039 2.9110 2.3399 -0.1494 0.1486  -0.1574 195 SER H CB  
2796 O OG  . SER B 195 ? 2.7673 3.0822 2.4962 -0.1534 0.1470  -0.1602 195 SER H OG  
2797 N N   . SER B 196 ? 2.5570 2.8874 2.2747 -0.1650 0.1367  -0.1247 196 SER H N   
2798 C CA  . SER B 196 ? 2.3509 2.6988 2.0636 -0.1716 0.1351  -0.1164 196 SER H CA  
2799 C C   . SER B 196 ? 2.4538 2.8097 2.1707 -0.1723 0.1365  -0.1075 196 SER H C   
2800 O O   . SER B 196 ? 2.2826 2.6543 2.0009 -0.1744 0.1406  -0.1088 196 SER H O   
2801 C CB  . SER B 196 ? 2.2363 2.5823 1.9408 -0.1768 0.1268  -0.1058 196 SER H CB  
2802 O OG  . SER B 196 ? 2.3610 2.6959 2.0661 -0.1760 0.1215  -0.0945 196 SER H OG  
2803 N N   . SER B 197 ? 2.6682 3.0134 2.3872 -0.1707 0.1330  -0.0982 197 SER H N   
2804 C CA  . SER B 197 ? 2.6794 3.0311 2.4020 -0.1719 0.1330  -0.0875 197 SER H CA  
2805 C C   . SER B 197 ? 2.6022 2.9498 2.3342 -0.1659 0.1399  -0.0949 197 SER H C   
2806 O O   . SER B 197 ? 2.7935 3.1300 2.5295 -0.1630 0.1389  -0.0902 197 SER H O   
2807 C CB  . SER B 197 ? 2.5779 2.9210 2.2977 -0.1741 0.1247  -0.0723 197 SER H CB  
2808 O OG  . SER B 197 ? 2.6404 2.9646 2.3618 -0.1692 0.1236  -0.0747 197 SER H OG  
2809 N N   . LEU B 198 ? 2.5203 2.8776 2.2564 -0.1642 0.1472  -0.1068 198 LEU H N   
2810 C CA  . LEU B 198 ? 2.4933 2.8494 2.2397 -0.1588 0.1542  -0.1142 198 LEU H CA  
2811 C C   . LEU B 198 ? 2.6531 3.0185 2.4033 -0.1606 0.1548  -0.1029 198 LEU H C   
2812 O O   . LEU B 198 ? 2.6946 3.0509 2.4493 -0.1584 0.1538  -0.0968 198 LEU H O   
2813 C CB  . LEU B 198 ? 2.3664 2.7309 2.1168 -0.1565 0.1615  -0.1298 198 LEU H CB  
2814 C CG  . LEU B 198 ? 2.1121 2.4673 1.8614 -0.1536 0.1622  -0.1432 198 LEU H CG  
2815 C CD1 . LEU B 198 ? 1.9227 2.2892 1.6758 -0.1523 0.1690  -0.1569 198 LEU H CD1 
2816 C CD2 . LEU B 198 ? 1.9454 2.2810 1.7007 -0.1475 0.1624  -0.1482 198 LEU H CD2 
2817 N N   . GLY B 199 ? 2.7050 3.0888 2.4536 -0.1650 0.1561  -0.0999 199 GLY H N   
2818 C CA  . GLY B 199 ? 2.5325 2.9270 2.2854 -0.1670 0.1569  -0.0897 199 GLY H CA  
2819 C C   . GLY B 199 ? 2.5010 2.8966 2.2485 -0.1724 0.1484  -0.0717 199 GLY H C   
2820 O O   . GLY B 199 ? 2.3254 2.7227 2.0774 -0.1729 0.1473  -0.0613 199 GLY H O   
2821 N N   . THR B 200 ? 2.5519 2.9466 2.2906 -0.1766 0.1421  -0.0677 200 THR H N   
2822 C CA  . THR B 200 ? 2.4901 2.8859 2.2245 -0.1819 0.1334  -0.0507 200 THR H CA  
2823 C C   . THR B 200 ? 2.6679 3.0471 2.4050 -0.1792 0.1291  -0.0422 200 THR H C   
2824 O O   . THR B 200 ? 2.6935 3.0747 2.4330 -0.1813 0.1251  -0.0287 200 THR H O   
2825 C CB  . THR B 200 ? 2.2968 2.6935 2.0223 -0.1865 0.1277  -0.0493 200 THR H CB  
2826 O OG1 . THR B 200 ? 2.5400 2.9206 2.2632 -0.1826 0.1272  -0.0575 200 THR H OG1 
2827 C CG2 . THR B 200 ? 2.2585 2.6727 1.9808 -0.1901 0.1316  -0.0566 200 THR H CG2 
2828 N N   . GLN B 201 ? 2.8302 3.1928 2.5670 -0.1745 0.1297  -0.0498 201 GLN H N   
2829 C CA  . GLN B 201 ? 2.6785 3.0206 2.4215 -0.1699 0.1239  -0.0424 201 GLN H CA  
2830 C C   . GLN B 201 ? 2.6275 2.9625 2.3842 -0.1631 0.1277  -0.0453 201 GLN H C   
2831 O O   . GLN B 201 ? 2.7323 3.0667 2.4938 -0.1588 0.1349  -0.0589 201 GLN H O   
2832 C CB  . GLN B 201 ? 2.6804 3.0043 2.4214 -0.1662 0.1208  -0.0486 201 GLN H CB  
2833 C CG  . GLN B 201 ? 2.6226 2.9238 2.3707 -0.1612 0.1129  -0.0401 201 GLN H CG  
2834 C CD  . GLN B 201 ? 2.6328 2.9191 2.3767 -0.1594 0.1087  -0.0434 201 GLN H CD  
2835 O OE1 . GLN B 201 ? 2.4395 2.7333 2.1729 -0.1647 0.1073  -0.0438 201 GLN H OE1 
2836 N NE2 . GLN B 201 ? 2.7503 3.0158 2.5024 -0.1523 0.1066  -0.0455 201 GLN H NE2 
2837 N N   . THR B 202 ? 2.8016 3.1312 2.5650 -0.1623 0.1226  -0.0325 202 THR H N   
2838 C CA  . THR B 202 ? 2.8794 3.2005 2.6561 -0.1560 0.1250  -0.0335 202 THR H CA  
2839 C C   . THR B 202 ? 2.8842 3.1797 2.6678 -0.1485 0.1215  -0.0368 202 THR H C   
2840 O O   . THR B 202 ? 2.6156 2.8985 2.3951 -0.1484 0.1146  -0.0319 202 THR H O   
2841 C CB  . THR B 202 ? 2.6104 2.9360 2.3916 -0.1583 0.1206  -0.0182 202 THR H CB  
2842 O OG1 . THR B 202 ? 2.4518 2.7656 2.2303 -0.1596 0.1105  -0.0057 202 THR H OG1 
2843 C CG2 . THR B 202 ? 2.1952 2.5474 1.9702 -0.1659 0.1243  -0.0148 202 THR H CG2 
2844 N N   . TYR B 203 ? 2.7534 3.0416 2.5478 -0.1422 0.1264  -0.0451 203 TYR H N   
2845 C CA  . TYR B 203 ? 2.5322 2.7972 2.3338 -0.1351 0.1241  -0.0497 203 TYR H CA  
2846 C C   . TYR B 203 ? 2.3096 2.5655 2.1245 -0.1302 0.1237  -0.0454 203 TYR H C   
2847 O O   . TYR B 203 ? 2.1385 2.4021 1.9608 -0.1284 0.1303  -0.0515 203 TYR H O   
2848 C CB  . TYR B 203 ? 2.4529 2.7163 2.2546 -0.1321 0.1303  -0.0664 203 TYR H CB  
2849 C CG  . TYR B 203 ? 2.4313 2.7029 2.2200 -0.1368 0.1306  -0.0712 203 TYR H CG  
2850 C CD1 . TYR B 203 ? 2.3207 2.5797 2.1032 -0.1372 0.1240  -0.0678 203 TYR H CD1 
2851 C CD2 . TYR B 203 ? 2.5309 2.8229 2.3134 -0.1411 0.1376  -0.0794 203 TYR H CD2 
2852 C CE1 . TYR B 203 ? 2.4476 2.7138 2.2185 -0.1416 0.1240  -0.0719 203 TYR H CE1 
2853 C CE2 . TYR B 203 ? 2.7544 3.0536 2.5246 -0.1456 0.1377  -0.0838 203 TYR H CE2 
2854 C CZ  . TYR B 203 ? 2.7047 2.9909 2.4693 -0.1459 0.1307  -0.0798 203 TYR H CZ  
2855 O OH  . TYR B 203 ? 2.8462 3.1396 2.5989 -0.1506 0.1306  -0.0839 203 TYR H OH  
2856 N N   . ILE B 204 ? 2.3585 2.5980 2.1764 -0.1281 0.1159  -0.0351 204 ILE H N   
2857 C CA  . ILE B 204 ? 2.3332 2.5628 2.1628 -0.1239 0.1141  -0.0292 204 ILE H CA  
2858 C C   . ILE B 204 ? 2.3449 2.5503 2.1780 -0.1189 0.1078  -0.0272 204 ILE H C   
2859 O O   . ILE B 204 ? 2.2096 2.4080 2.0361 -0.1205 0.1012  -0.0207 204 ILE H O   
2860 C CB  . ILE B 204 ? 2.3931 2.6319 2.2225 -0.1281 0.1101  -0.0145 204 ILE H CB  
2861 C CG1 . ILE B 204 ? 2.4127 2.6771 2.2369 -0.1342 0.1158  -0.0153 204 ILE H CG1 
2862 C CG2 . ILE B 204 ? 2.3098 2.5402 2.1516 -0.1240 0.1092  -0.0096 204 ILE H CG2 
2863 C CD1 . ILE B 204 ? 2.1968 2.4712 2.0299 -0.1321 0.1241  -0.0226 204 ILE H CD1 
2864 N N   . CYS B 205 ? 2.3893 2.5824 2.2332 -0.1130 0.1098  -0.0328 205 CYS H N   
2865 C CA  . CYS B 205 ? 2.3772 2.5476 2.2259 -0.1081 0.1042  -0.0305 205 CYS H CA  
2866 C C   . CYS B 205 ? 2.4542 2.6186 2.3108 -0.1067 0.1001  -0.0194 205 CYS H C   
2867 O O   . CYS B 205 ? 2.5255 2.6909 2.3921 -0.1042 0.1038  -0.0213 205 CYS H O   
2868 C CB  . CYS B 205 ? 2.1376 2.2980 1.9933 -0.1029 0.1084  -0.0433 205 CYS H CB  
2869 S SG  . CYS B 205 ? 2.6964 2.8659 2.5445 -0.1044 0.1143  -0.0578 205 CYS H SG  
2870 N N   . ASN B 206 ? 2.2122 2.3705 2.0648 -0.1084 0.0924  -0.0077 206 ASN H N   
2871 C CA  . ASN B 206 ? 2.2808 2.4326 2.1398 -0.1075 0.0874  0.0038  206 ASN H CA  
2872 C C   . ASN B 206 ? 2.1195 2.2484 1.9829 -0.1023 0.0824  0.0042  206 ASN H C   
2873 O O   . ASN B 206 ? 1.9641 2.0835 1.8219 -0.1025 0.0762  0.0088  206 ASN H O   
2874 C CB  . ASN B 206 ? 2.2666 2.4266 2.1190 -0.1127 0.0817  0.0164  206 ASN H CB  
2875 C CG  . ASN B 206 ? 2.2673 2.4508 2.1162 -0.1182 0.0864  0.0171  206 ASN H CG  
2876 O OD1 . ASN B 206 ? 2.1986 2.3918 2.0522 -0.1175 0.0938  0.0100  206 ASN H OD1 
2877 N ND2 . ASN B 206 ? 2.4525 2.6455 2.2933 -0.1237 0.0822  0.0257  206 ASN H ND2 
2878 N N   . VAL B 207 ? 2.1907 2.3111 2.0642 -0.0978 0.0852  -0.0007 207 VAL H N   
2879 C CA  . VAL B 207 ? 2.0763 2.1760 1.9541 -0.0931 0.0815  -0.0019 207 VAL H CA  
2880 C C   . VAL B 207 ? 2.1312 2.2217 2.0164 -0.0914 0.0766  0.0082  207 VAL H C   
2881 O O   . VAL B 207 ? 2.2049 2.3048 2.0948 -0.0929 0.0779  0.0133  207 VAL H O   
2882 C CB  . VAL B 207 ? 2.0567 2.1519 1.9409 -0.0892 0.0873  -0.0149 207 VAL H CB  
2883 C CG1 . VAL B 207 ? 2.1931 2.2674 2.0808 -0.0849 0.0832  -0.0160 207 VAL H CG1 
2884 C CG2 . VAL B 207 ? 1.9935 2.0997 1.8705 -0.0912 0.0925  -0.0251 207 VAL H CG2 
2885 N N   . ASN B 208 ? 2.2322 2.3045 2.1184 -0.0885 0.0708  0.0112  208 ASN H N   
2886 C CA  . ASN B 208 ? 2.1497 2.2106 2.0435 -0.0863 0.0663  0.0190  208 ASN H CA  
2887 C C   . ASN B 208 ? 2.1275 2.1691 2.0246 -0.0819 0.0639  0.0153  208 ASN H C   
2888 O O   . ASN B 208 ? 2.0825 2.1164 1.9731 -0.0813 0.0613  0.0132  208 ASN H O   
2889 C CB  . ASN B 208 ? 2.2460 2.3066 2.1357 -0.0888 0.0590  0.0319  208 ASN H CB  
2890 C CG  . ASN B 208 ? 2.1801 2.2268 2.0769 -0.0864 0.0536  0.0397  208 ASN H CG  
2891 O OD1 . ASN B 208 ? 2.1047 2.1506 2.0108 -0.0846 0.0562  0.0391  208 ASN H OD1 
2892 N ND2 . ASN B 208 ? 2.3500 2.3859 2.2430 -0.0862 0.0460  0.0468  208 ASN H ND2 
2893 N N   . HIS B 209 ? 2.1878 2.2221 2.0952 -0.0790 0.0648  0.0148  209 HIS H N   
2894 C CA  . HIS B 209 ? 2.1384 2.1541 2.0502 -0.0752 0.0618  0.0131  209 HIS H CA  
2895 C C   . HIS B 209 ? 2.3313 2.3373 2.2445 -0.0749 0.0546  0.0247  209 HIS H C   
2896 O O   . HIS B 209 ? 2.4728 2.4769 2.3944 -0.0741 0.0542  0.0288  209 HIS H O   
2897 C CB  . HIS B 209 ? 2.0098 2.0242 1.9328 -0.0725 0.0670  0.0057  209 HIS H CB  
2898 C CG  . HIS B 209 ? 2.1107 2.1082 2.0378 -0.0691 0.0651  0.0016  209 HIS H CG  
2899 N ND1 . HIS B 209 ? 2.1600 2.1533 2.0983 -0.0666 0.0682  -0.0038 209 HIS H ND1 
2900 C CD2 . HIS B 209 ? 2.1868 2.1712 2.1085 -0.0680 0.0606  0.0019  209 HIS H CD2 
2901 C CE1 . HIS B 209 ? 2.1019 2.0802 2.0415 -0.0643 0.0653  -0.0061 209 HIS H CE1 
2902 N NE2 . HIS B 209 ? 2.2251 2.1980 2.1545 -0.0651 0.0608  -0.0028 209 HIS H NE2 
2903 N N   . LYS B 210 ? 2.2182 2.2180 2.1234 -0.0756 0.0487  0.0297  210 LYS H N   
2904 C CA  . LYS B 210 ? 2.2198 2.2106 2.1253 -0.0756 0.0413  0.0404  210 LYS H CA  
2905 C C   . LYS B 210 ? 2.3717 2.3488 2.2859 -0.0727 0.0390  0.0428  210 LYS H C   
2906 O O   . LYS B 210 ? 2.4422 2.4189 2.3604 -0.0734 0.0356  0.0514  210 LYS H O   
2907 C CB  . LYS B 210 ? 2.2102 2.1931 2.1069 -0.0756 0.0357  0.0427  210 LYS H CB  
2908 C CG  . LYS B 210 ? 2.3867 2.3823 2.2750 -0.0792 0.0357  0.0442  210 LYS H CG  
2909 C CD  . LYS B 210 ? 2.4944 2.4810 2.3754 -0.0788 0.0301  0.0462  210 LYS H CD  
2910 C CE  . LYS B 210 ? 2.3428 2.3416 2.2160 -0.0825 0.0292  0.0485  210 LYS H CE  
2911 N NZ  . LYS B 210 ? 2.1958 2.1860 2.0628 -0.0819 0.0238  0.0501  210 LYS H NZ  
2912 N N   . PRO B 211 ? 2.3376 2.3034 2.2552 -0.0698 0.0401  0.0364  211 PRO H N   
2913 C CA  . PRO B 211 ? 2.2379 2.1913 2.1639 -0.0676 0.0374  0.0396  211 PRO H CA  
2914 C C   . PRO B 211 ? 2.2381 2.1989 2.1741 -0.0679 0.0406  0.0416  211 PRO H C   
2915 O O   . PRO B 211 ? 2.5712 2.5252 2.5125 -0.0675 0.0366  0.0489  211 PRO H O   
2916 C CB  . PRO B 211 ? 2.2319 2.1751 2.1597 -0.0650 0.0390  0.0312  211 PRO H CB  
2917 C CG  . PRO B 211 ? 2.3064 2.2607 2.2310 -0.0658 0.0451  0.0222  211 PRO H CG  
2918 C CD  . PRO B 211 ? 2.2258 2.1905 2.1411 -0.0686 0.0441  0.0259  211 PRO H CD  
2919 N N   . SER B 212 ? 2.3709 2.3455 2.3096 -0.0687 0.0476  0.0351  212 SER H N   
2920 C CA  . SER B 212 ? 2.2594 2.2435 2.2074 -0.0692 0.0512  0.0369  212 SER H CA  
2921 C C   . SER B 212 ? 2.3800 2.3809 2.3239 -0.0728 0.0523  0.0421  212 SER H C   
2922 O O   . SER B 212 ? 2.1863 2.1976 2.1373 -0.0736 0.0557  0.0437  212 SER H O   
2923 C CB  . SER B 212 ? 2.0875 2.0760 2.0433 -0.0675 0.0585  0.0261  212 SER H CB  
2924 O OG  . SER B 212 ? 2.0308 2.0260 1.9799 -0.0680 0.0627  0.0171  212 SER H OG  
2925 N N   . ASN B 213 ? 2.4008 2.4048 2.3340 -0.0749 0.0494  0.0450  213 ASN H N   
2926 C CA  . ASN B 213 ? 2.2376 2.2573 2.1662 -0.0789 0.0493  0.0510  213 ASN H CA  
2927 C C   . ASN B 213 ? 2.2198 2.2578 2.1517 -0.0804 0.0575  0.0454  213 ASN H C   
2928 O O   . ASN B 213 ? 2.1045 2.1546 2.0394 -0.0828 0.0585  0.0513  213 ASN H O   
2929 C CB  . ASN B 213 ? 2.1504 2.1669 2.0817 -0.0800 0.0428  0.0636  213 ASN H CB  
2930 C CG  . ASN B 213 ? 2.6000 2.6022 2.5256 -0.0794 0.0344  0.0698  213 ASN H CG  
2931 O OD1 . ASN B 213 ? 2.8860 2.8850 2.8036 -0.0793 0.0333  0.0663  213 ASN H OD1 
2932 N ND2 . ASN B 213 ? 2.8679 2.8615 2.7979 -0.0790 0.0283  0.0789  213 ASN H ND2 
2933 N N   . THR B 214 ? 2.3157 2.3563 2.2473 -0.0791 0.0636  0.0337  214 THR H N   
2934 C CA  . THR B 214 ? 2.1056 2.1634 2.0404 -0.0802 0.0718  0.0266  214 THR H CA  
2935 C C   . THR B 214 ? 1.9056 1.9788 1.8295 -0.0842 0.0739  0.0254  214 THR H C   
2936 O O   . THR B 214 ? 1.9375 2.0164 1.8574 -0.0843 0.0788  0.0155  214 THR H O   
2937 C CB  . THR B 214 ? 2.0642 2.1173 2.0053 -0.0768 0.0772  0.0143  214 THR H CB  
2938 O OG1 . THR B 214 ? 2.1522 2.1978 2.0853 -0.0761 0.0760  0.0085  214 THR H OG1 
2939 C CG2 . THR B 214 ? 1.8408 1.8791 1.7931 -0.0733 0.0749  0.0161  214 THR H CG2 
2940 N N   . LYS B 215 ? 1.7794 1.8589 1.6986 -0.0877 0.0695  0.0361  215 LYS H N   
2941 C CA  . LYS B 215 ? 2.0380 2.1335 1.9475 -0.0922 0.0708  0.0369  215 LYS H CA  
2942 C C   . LYS B 215 ? 2.1273 2.2417 2.0390 -0.0938 0.0797  0.0295  215 LYS H C   
2943 O O   . LYS B 215 ? 2.1125 2.2363 2.0312 -0.0947 0.0821  0.0331  215 LYS H O   
2944 C CB  . LYS B 215 ? 2.0440 2.1431 1.9504 -0.0958 0.0641  0.0507  215 LYS H CB  
2945 C CG  . LYS B 215 ? 1.9006 1.9825 1.8035 -0.0946 0.0551  0.0575  215 LYS H CG  
2946 C CD  . LYS B 215 ? 1.8758 1.9617 1.7770 -0.0981 0.0483  0.0710  215 LYS H CD  
2947 C CE  . LYS B 215 ? 1.6742 1.7430 1.5723 -0.0967 0.0394  0.0771  215 LYS H CE  
2948 N NZ  . LYS B 215 ? 1.7253 1.7970 1.6228 -0.0999 0.0321  0.0903  215 LYS H NZ  
2949 N N   . VAL B 216 ? 1.9488 2.0690 1.8551 -0.0941 0.0848  0.0187  216 VAL H N   
2950 C CA  . VAL B 216 ? 1.9132 2.0504 1.8216 -0.0951 0.0938  0.0094  216 VAL H CA  
2951 C C   . VAL B 216 ? 1.9870 2.1371 1.8832 -0.0991 0.0959  0.0054  216 VAL H C   
2952 O O   . VAL B 216 ? 2.0948 2.2371 1.9848 -0.0982 0.0947  0.0000  216 VAL H O   
2953 C CB  . VAL B 216 ? 1.9088 2.0384 1.8259 -0.0902 0.0989  -0.0029 216 VAL H CB  
2954 C CG1 . VAL B 216 ? 1.8313 1.9789 1.7497 -0.0912 0.1082  -0.0135 216 VAL H CG1 
2955 C CG2 . VAL B 216 ? 1.7420 1.8603 1.6719 -0.0866 0.0971  0.0013  216 VAL H CG2 
2956 N N   . ASP B 217 ? 2.1105 2.2808 2.0034 -0.1038 0.0991  0.0082  217 ASP H N   
2957 C CA  . ASP B 217 ? 2.2106 2.3953 2.0916 -0.1086 0.1009  0.0058  217 ASP H CA  
2958 C C   . ASP B 217 ? 2.2830 2.4823 2.1653 -0.1086 0.1108  -0.0073 217 ASP H C   
2959 O O   . ASP B 217 ? 2.3224 2.5383 2.2082 -0.1107 0.1157  -0.0068 217 ASP H O   
2960 C CB  . ASP B 217 ? 2.3329 2.5309 2.2088 -0.1144 0.0972  0.0185  217 ASP H CB  
2961 C CG  . ASP B 217 ? 2.5631 2.7473 2.4363 -0.1148 0.0869  0.0308  217 ASP H CG  
2962 O OD1 . ASP B 217 ? 2.4859 2.6518 2.3587 -0.1111 0.0831  0.0287  217 ASP H OD1 
2963 O OD2 . ASP B 217 ? 2.5118 2.7039 2.3834 -0.1189 0.0827  0.0425  217 ASP H OD2 
2964 N N   . LYS B 218 ? 2.3018 2.4956 2.1816 -0.1063 0.1137  -0.0192 218 LYS H N   
2965 C CA  . LYS B 218 ? 2.2407 2.4452 2.1242 -0.1052 0.1228  -0.0329 218 LYS H CA  
2966 C C   . LYS B 218 ? 2.0704 2.2887 1.9416 -0.1094 0.1262  -0.0397 218 LYS H C   
2967 O O   . LYS B 218 ? 2.1571 2.3713 2.0182 -0.1117 0.1212  -0.0362 218 LYS H O   
2968 C CB  . LYS B 218 ? 2.2724 2.4600 2.1651 -0.0989 0.1241  -0.0424 218 LYS H CB  
2969 C CG  . LYS B 218 ? 2.3687 2.5664 2.2670 -0.0973 0.1330  -0.0563 218 LYS H CG  
2970 C CD  . LYS B 218 ? 2.5914 2.7732 2.5001 -0.0914 0.1338  -0.0649 218 LYS H CD  
2971 C CE  . LYS B 218 ? 2.6976 2.8914 2.6119 -0.0902 0.1428  -0.0788 218 LYS H CE  
2972 N NZ  . LYS B 218 ? 2.9858 3.1649 2.9117 -0.0845 0.1437  -0.0877 218 LYS H NZ  
2973 N N   . ARG B 219 ? 2.0560 2.2912 1.9284 -0.1105 0.1346  -0.0494 219 ARG H N   
2974 C CA  . ARG B 219 ? 2.1649 2.4172 2.0255 -0.1154 0.1385  -0.0550 219 ARG H CA  
2975 C C   . ARG B 219 ? 2.2439 2.4918 2.1033 -0.1127 0.1426  -0.0705 219 ARG H C   
2976 O O   . ARG B 219 ? 2.2435 2.4843 2.1136 -0.1075 0.1465  -0.0799 219 ARG H O   
2984 N N   . VAL B 220 ? 2.2976 2.5496 2.1442 -0.1164 0.1415  -0.0727 220 VAL H N   
2985 C CA  . VAL B 220 ? 2.3015 2.5521 2.1451 -0.1150 0.1454  -0.0872 220 VAL H CA  
2986 C C   . VAL B 220 ? 2.2902 2.5644 2.1275 -0.1194 0.1530  -0.0951 220 VAL H C   
2987 O O   . VAL B 220 ? 2.2641 2.5533 2.0914 -0.1257 0.1521  -0.0878 220 VAL H O   
2988 C CB  . VAL B 220 ? 2.2462 2.4851 2.0799 -0.1161 0.1390  -0.0849 220 VAL H CB  
2989 C CG1 . VAL B 220 ? 2.1712 2.4048 2.0042 -0.1135 0.1423  -0.0998 220 VAL H CG1 
2990 C CG2 . VAL B 220 ? 2.2928 2.5119 2.1306 -0.1132 0.1308  -0.0741 220 VAL H CG2 
2991 N N   . GLU B 221 ? 2.3382 2.6160 2.1814 -0.1164 0.1603  -0.1099 221 GLU H N   
2992 C CA  . GLU B 221 ? 2.4694 2.7701 2.3078 -0.1201 0.1683  -0.1186 221 GLU H CA  
2993 C C   . GLU B 221 ? 2.4871 2.7876 2.3205 -0.1195 0.1717  -0.1337 221 GLU H C   
2994 O O   . GLU B 221 ? 2.2994 2.5849 2.1413 -0.1138 0.1720  -0.1425 221 GLU H O   
2995 C CB  . GLU B 221 ? 2.3965 2.7065 2.2478 -0.1173 0.1752  -0.1230 221 GLU H CB  
2996 C CG  . GLU B 221 ? 2.3474 2.6682 2.1997 -0.1207 0.1740  -0.1091 221 GLU H CG  
2997 C CD  . GLU B 221 ? 2.3749 2.7197 2.2141 -0.1285 0.1766  -0.1063 221 GLU H CD  
2998 O OE1 . GLU B 221 ? 2.4040 2.7679 2.2448 -0.1299 0.1848  -0.1142 221 GLU H OE1 
2999 O OE2 . GLU B 221 ? 2.3753 2.7202 2.2030 -0.1334 0.1704  -0.0962 221 GLU H OE2 
3000 N N   . PRO B 222 ? 2.5380 2.8551 2.3583 -0.1253 0.1743  -0.1371 222 PRO H N   
3001 C CA  . PRO B 222 ? 2.2741 2.5913 2.0894 -0.1249 0.1775  -0.1518 222 PRO H CA  
3002 C C   . PRO B 222 ? 2.2986 2.6277 2.1211 -0.1226 0.1871  -0.1677 222 PRO H C   
3003 O O   . PRO B 222 ? 2.6067 2.9578 2.4242 -0.1268 0.1932  -0.1708 222 PRO H O   
3004 C CB  . PRO B 222 ? 2.2730 2.6031 2.0708 -0.1328 0.1753  -0.1469 222 PRO H CB  
3005 C CG  . PRO B 222 ? 2.3424 2.6905 2.1380 -0.1377 0.1764  -0.1356 222 PRO H CG  
3006 C CD  . PRO B 222 ? 2.4042 2.7442 2.2154 -0.1324 0.1764  -0.1306 222 PRO H CD  
3007 N N   . LYS B 223 ? 2.1208 2.4353 1.9556 -0.1158 0.1884  -0.1777 223 LYS H N   
3008 C CA  . LYS B 223 ? 2.3648 2.6873 2.2073 -0.1128 0.1968  -0.1947 223 LYS H CA  
3009 C C   . LYS B 223 ? 2.5325 2.8573 2.3649 -0.1147 0.1982  -0.2067 223 LYS H C   
3010 O O   . LYS B 223 ? 2.5180 2.8253 2.3504 -0.1122 0.1933  -0.2090 223 LYS H O   
3011 C CB  . LYS B 223 ? 2.2025 2.5078 2.0636 -0.1049 0.1968  -0.1994 223 LYS H CB  
3012 C CG  . LYS B 223 ? 2.0988 2.4028 1.9712 -0.1028 0.1962  -0.1890 223 LYS H CG  
3013 C CD  . LYS B 223 ? 2.1768 2.4628 2.0673 -0.0953 0.1956  -0.1938 223 LYS H CD  
3014 C CE  . LYS B 223 ? 2.0932 2.3773 1.9954 -0.0932 0.1949  -0.1835 223 LYS H CE  
3015 N NZ  . LYS B 223 ? 2.2802 2.5464 2.2000 -0.0862 0.1938  -0.1877 223 LYS H NZ  
3016 N N   . SER B 224 ? 2.6779 3.0202 2.5043 -0.1182 0.2014  -0.2112 224 SER H N   
3017 C CA  . SER B 224 ? 2.7336 3.0754 2.5525 -0.1195 0.1993  -0.2187 224 SER H CA  
3018 C C   . SER B 224 ? 3.0034 3.3434 2.8335 -0.1141 0.2041  -0.2358 224 SER H C   
3019 O O   . SER B 224 ? 3.1269 3.4677 2.9706 -0.1096 0.2093  -0.2419 224 SER H O   
3020 C CB  . SER B 224 ? 2.8744 3.2340 2.6812 -0.1262 0.1982  -0.2126 224 SER H CB  
3021 O OG  . SER B 224 ? 3.2894 3.6659 3.1018 -0.1263 0.2044  -0.2164 224 SER H OG  
3022 N N   . ASP C 1   ? 1.4876 1.2908 1.3297 -0.0731 -0.0051 -0.0113 1   ASP L N   
3023 C CA  . ASP C 1   ? 1.8369 1.6410 1.6817 -0.0705 -0.0031 -0.0139 1   ASP L CA  
3024 C C   . ASP C 1   ? 2.0944 1.9056 1.9367 -0.0690 -0.0008 -0.0173 1   ASP L C   
3025 O O   . ASP C 1   ? 2.0869 1.9019 1.9283 -0.0705 -0.0008 -0.0177 1   ASP L O   
3026 C CB  . ASP C 1   ? 1.7447 1.5458 1.5990 -0.0721 -0.0037 -0.0143 1   ASP L CB  
3027 C CG  . ASP C 1   ? 1.8347 1.6370 1.6916 -0.0696 -0.0014 -0.0171 1   ASP L CG  
3028 O OD1 . ASP C 1   ? 1.5856 1.3881 1.4378 -0.0669 -0.0005 -0.0169 1   ASP L OD1 
3029 O OD2 . ASP C 1   ? 1.7823 1.5858 1.6461 -0.0704 -0.0007 -0.0197 1   ASP L OD2 
3030 N N   . VAL C 2   ? 1.9716 1.7847 1.8128 -0.0662 0.0011  -0.0193 2   VAL L N   
3031 C CA  . VAL C 2   ? 1.7052 1.5249 1.5437 -0.0647 0.0032  -0.0222 2   VAL L CA  
3032 C C   . VAL C 2   ? 1.7494 1.5710 1.5935 -0.0649 0.0047  -0.0253 2   VAL L C   
3033 O O   . VAL C 2   ? 1.6730 1.4916 1.5211 -0.0645 0.0049  -0.0253 2   VAL L O   
3034 C CB  . VAL C 2   ? 1.7211 1.5425 1.5533 -0.0615 0.0039  -0.0220 2   VAL L CB  
3035 C CG1 . VAL C 2   ? 1.7537 1.5820 1.5839 -0.0602 0.0058  -0.0247 2   VAL L CG1 
3036 C CG2 . VAL C 2   ? 1.7743 1.5941 1.6012 -0.0611 0.0026  -0.0198 2   VAL L CG2 
3037 N N   . VAL C 3   ? 1.7892 1.6160 1.6336 -0.0655 0.0057  -0.0279 3   VAL L N   
3038 C CA  . VAL C 3   ? 1.6798 1.5093 1.5287 -0.0656 0.0073  -0.0316 3   VAL L CA  
3039 C C   . VAL C 3   ? 1.6198 1.4556 1.4636 -0.0640 0.0091  -0.0336 3   VAL L C   
3040 O O   . VAL C 3   ? 1.5681 1.4078 1.4092 -0.0645 0.0090  -0.0339 3   VAL L O   
3041 C CB  . VAL C 3   ? 1.6093 1.4386 1.4645 -0.0685 0.0063  -0.0331 3   VAL L CB  
3042 C CG1 . VAL C 3   ? 1.5804 1.4135 1.4390 -0.0684 0.0080  -0.0377 3   VAL L CG1 
3043 C CG2 . VAL C 3   ? 1.5817 1.4046 1.4434 -0.0702 0.0043  -0.0311 3   VAL L CG2 
3044 N N   . MET C 4   ? 1.2875 1.1249 1.1302 -0.0623 0.0105  -0.0346 4   MET L N   
3045 C CA  . MET C 4   ? 1.4693 1.3129 1.3078 -0.0611 0.0120  -0.0363 4   MET L CA  
3046 C C   . MET C 4   ? 1.5255 1.3725 1.3678 -0.0622 0.0136  -0.0405 4   MET L C   
3047 O O   . MET C 4   ? 1.6614 1.5076 1.5068 -0.0620 0.0147  -0.0418 4   MET L O   
3048 C CB  . MET C 4   ? 1.7133 1.5571 1.5480 -0.0589 0.0123  -0.0344 4   MET L CB  
3049 C CG  . MET C 4   ? 1.7224 1.5629 1.5533 -0.0574 0.0106  -0.0308 4   MET L CG  
3050 S SD  . MET C 4   ? 1.6011 1.4444 1.4282 -0.0576 0.0099  -0.0305 4   MET L SD  
3051 C CE  . MET C 4   ? 1.7839 1.6348 1.6076 -0.0564 0.0111  -0.0320 4   MET L CE  
3052 N N   . THR C 5   ? 1.5374 1.3883 1.3796 -0.0634 0.0137  -0.0427 5   THR L N   
3053 C CA  . THR C 5   ? 1.6448 1.4990 1.4901 -0.0646 0.0150  -0.0472 5   THR L CA  
3054 C C   . THR C 5   ? 1.6440 1.5046 1.4839 -0.0638 0.0165  -0.0485 5   THR L C   
3055 O O   . THR C 5   ? 1.6212 1.4848 1.4564 -0.0633 0.0159  -0.0467 5   THR L O   
3056 C CB  . THR C 5   ? 1.6355 1.4900 1.4840 -0.0667 0.0138  -0.0487 5   THR L CB  
3057 O OG1 . THR C 5   ? 1.9824 1.8402 1.8259 -0.0667 0.0132  -0.0468 5   THR L OG1 
3058 C CG2 . THR C 5   ? 1.1924 1.0408 1.0466 -0.0680 0.0120  -0.0469 5   THR L CG2 
3059 N N   . GLN C 6   ? 1.4304 1.2938 1.2714 -0.0638 0.0183  -0.0514 6   GLN L N   
3060 C CA  . GLN C 6   ? 1.6928 1.5627 1.5286 -0.0636 0.0195  -0.0521 6   GLN L CA  
3061 C C   . GLN C 6   ? 1.7911 1.6655 1.6279 -0.0653 0.0206  -0.0571 6   GLN L C   
3062 O O   . GLN C 6   ? 1.8133 1.6863 1.6555 -0.0661 0.0214  -0.0609 6   GLN L O   
3063 C CB  . GLN C 6   ? 1.6684 1.5396 1.5028 -0.0625 0.0207  -0.0512 6   GLN L CB  
3064 C CG  . GLN C 6   ? 1.6171 1.4843 1.4500 -0.0608 0.0194  -0.0464 6   GLN L CG  
3065 C CD  . GLN C 6   ? 1.8247 1.6934 1.6568 -0.0600 0.0203  -0.0451 6   GLN L CD  
3066 O OE1 . GLN C 6   ? 1.8534 1.7251 1.6875 -0.0608 0.0223  -0.0481 6   GLN L OE1 
3067 N NE2 . GLN C 6   ? 2.1962 2.0628 2.0255 -0.0585 0.0188  -0.0406 6   GLN L NE2 
3068 N N   . SER C 7   ? 1.7639 1.6440 1.5958 -0.0657 0.0206  -0.0572 7   SER L N   
3069 C CA  . SER C 7   ? 1.7207 1.6058 1.5522 -0.0675 0.0216  -0.0618 7   SER L CA  
3070 C C   . SER C 7   ? 2.0389 1.9307 1.8640 -0.0677 0.0220  -0.0606 7   SER L C   
3071 O O   . SER C 7   ? 2.1515 2.0434 1.9732 -0.0664 0.0209  -0.0561 7   SER L O   
3072 C CB  . SER C 7   ? 1.6809 1.5652 1.5146 -0.0688 0.0201  -0.0631 7   SER L CB  
3073 O OG  . SER C 7   ? 1.8837 1.7692 1.7136 -0.0684 0.0186  -0.0592 7   SER L OG  
3074 N N   . PRO C 8   ? 1.9003 1.7975 1.7238 -0.0692 0.0234  -0.0645 8   PRO L N   
3075 C CA  . PRO C 8   ? 1.7765 1.6734 1.6044 -0.0700 0.0253  -0.0698 8   PRO L CA  
3076 C C   . PRO C 8   ? 1.7248 1.6222 1.5529 -0.0690 0.0271  -0.0691 8   PRO L C   
3077 O O   . PRO C 8   ? 1.8377 1.7393 1.6609 -0.0688 0.0272  -0.0660 8   PRO L O   
3078 C CB  . PRO C 8   ? 2.0827 1.9861 1.9080 -0.0721 0.0260  -0.0743 8   PRO L CB  
3079 C CG  . PRO C 8   ? 2.0953 2.0004 1.9165 -0.0727 0.0239  -0.0712 8   PRO L CG  
3080 C CD  . PRO C 8   ? 1.9138 1.8173 1.7327 -0.0708 0.0229  -0.0650 8   PRO L CD  
3081 N N   . VAL C 9   ? 1.6668 1.5601 1.5011 -0.0684 0.0281  -0.0714 9   VAL L N   
3082 C CA  . VAL C 9   ? 1.6834 1.5772 1.5188 -0.0675 0.0298  -0.0706 9   VAL L CA  
3083 C C   . VAL C 9   ? 1.8378 1.7401 1.6694 -0.0687 0.0322  -0.0735 9   VAL L C   
3084 O O   . VAL C 9   ? 1.7748 1.6800 1.6040 -0.0684 0.0330  -0.0707 9   VAL L O   
3085 C CB  . VAL C 9   ? 1.4963 1.3843 1.3402 -0.0668 0.0304  -0.0732 9   VAL L CB  
3086 C CG1 . VAL C 9   ? 1.7436 1.6327 1.5894 -0.0660 0.0324  -0.0729 9   VAL L CG1 
3087 C CG2 . VAL C 9   ? 1.4716 1.3516 1.3184 -0.0659 0.0277  -0.0691 9   VAL L CG2 
3088 N N   . SER C 10  ? 1.9505 1.8572 1.7811 -0.0705 0.0331  -0.0788 10  SER L N   
3089 C CA  . SER C 10  ? 1.7326 1.6482 1.5590 -0.0722 0.0354  -0.0821 10  SER L CA  
3090 C C   . SER C 10  ? 1.7124 1.6328 1.5316 -0.0739 0.0339  -0.0804 10  SER L C   
3091 O O   . SER C 10  ? 2.0652 1.9848 1.8846 -0.0748 0.0327  -0.0826 10  SER L O   
3092 C CB  . SER C 10  ? 1.6295 1.5465 1.4605 -0.0730 0.0377  -0.0903 10  SER L CB  
3093 O OG  . SER C 10  ? 1.7976 1.7121 1.6304 -0.0738 0.0361  -0.0934 10  SER L OG  
3094 N N   . LEU C 11  ? 1.7207 1.6464 1.5342 -0.0745 0.0337  -0.0761 11  LEU L N   
3095 C CA  . LEU C 11  ? 1.9557 1.8863 1.7629 -0.0761 0.0319  -0.0733 11  LEU L CA  
3096 C C   . LEU C 11  ? 1.9927 1.9327 1.7942 -0.0784 0.0332  -0.0733 11  LEU L C   
3097 O O   . LEU C 11  ? 1.9412 1.8837 1.7400 -0.0784 0.0322  -0.0676 11  LEU L O   
3098 C CB  . LEU C 11  ? 2.1235 2.0499 1.9297 -0.0743 0.0290  -0.0662 11  LEU L CB  
3099 C CG  . LEU C 11  ? 2.1730 2.0916 1.9834 -0.0727 0.0274  -0.0660 11  LEU L CG  
3100 C CD1 . LEU C 11  ? 2.2353 2.1501 2.0448 -0.0707 0.0250  -0.0595 11  LEU L CD1 
3101 C CD2 . LEU C 11  ? 2.0181 1.9389 1.8271 -0.0745 0.0267  -0.0691 11  LEU L CD2 
3102 N N   . PRO C 12  ? 2.0640 2.0098 1.8638 -0.0807 0.0352  -0.0794 12  PRO L N   
3103 C CA  . PRO C 12  ? 1.9677 1.9235 1.7608 -0.0838 0.0358  -0.0789 12  PRO L CA  
3104 C C   . PRO C 12  ? 1.9034 1.8615 1.6916 -0.0853 0.0327  -0.0749 12  PRO L C   
3105 O O   . PRO C 12  ? 2.1168 2.0710 1.9062 -0.0850 0.0311  -0.0759 12  PRO L O   
3106 C CB  . PRO C 12  ? 2.1585 2.1189 1.9516 -0.0856 0.0389  -0.0876 12  PRO L CB  
3107 C CG  . PRO C 12  ? 2.1608 2.1134 1.9599 -0.0840 0.0384  -0.0920 12  PRO L CG  
3108 C CD  . PRO C 12  ? 2.2206 2.1643 2.0249 -0.0808 0.0370  -0.0872 12  PRO L CD  
3109 N N   . VAL C 13  ? 2.0156 1.9803 1.7988 -0.0872 0.0316  -0.0700 13  VAL L N   
3110 C CA  . VAL C 13  ? 2.1326 2.0999 1.9118 -0.0886 0.0283  -0.0652 13  VAL L CA  
3111 C C   . VAL C 13  ? 2.2210 2.1991 1.9939 -0.0927 0.0286  -0.0646 13  VAL L C   
3112 O O   . VAL C 13  ? 2.2401 2.2232 2.0118 -0.0939 0.0313  -0.0668 13  VAL L O   
3113 C CB  . VAL C 13  ? 1.9262 1.8883 1.7076 -0.0860 0.0254  -0.0575 13  VAL L CB  
3114 C CG1 . VAL C 13  ? 1.9234 1.8884 1.7017 -0.0873 0.0219  -0.0524 13  VAL L CG1 
3115 C CG2 . VAL C 13  ? 1.9691 1.9212 1.7562 -0.0823 0.0253  -0.0583 13  VAL L CG2 
3116 N N   . THR C 14  ? 2.1408 2.1229 1.9096 -0.0951 0.0260  -0.0618 14  THR L N   
3117 C CA  . THR C 14  ? 2.0300 2.0223 1.7929 -0.0993 0.0250  -0.0589 14  THR L CA  
3118 C C   . THR C 14  ? 2.1094 2.1014 1.8726 -0.0988 0.0210  -0.0498 14  THR L C   
3119 O O   . THR C 14  ? 2.2218 2.2064 1.9889 -0.0957 0.0189  -0.0469 14  THR L O   
3120 C CB  . THR C 14  ? 2.0509 2.0485 1.8090 -0.1030 0.0245  -0.0623 14  THR L CB  
3121 O OG1 . THR C 14  ? 2.0792 2.0717 1.8391 -0.1018 0.0214  -0.0599 14  THR L OG1 
3122 C CG2 . THR C 14  ? 2.3024 2.3003 2.0604 -0.1035 0.0281  -0.0718 14  THR L CG2 
3123 N N   . LEU C 15  ? 2.0322 2.0324 1.7915 -0.1020 0.0199  -0.0454 15  LEU L N   
3124 C CA  . LEU C 15  ? 1.9805 1.9803 1.7411 -0.1016 0.0155  -0.0367 15  LEU L CA  
3125 C C   . LEU C 15  ? 2.1165 2.1145 1.8774 -0.1017 0.0123  -0.0348 15  LEU L C   
3126 O O   . LEU C 15  ? 2.3687 2.3700 2.1263 -0.1043 0.0126  -0.0385 15  LEU L O   
3127 C CB  . LEU C 15  ? 1.9391 1.9488 1.6957 -0.1058 0.0140  -0.0315 15  LEU L CB  
3128 C CG  . LEU C 15  ? 2.0755 2.0902 1.8311 -0.1069 0.0159  -0.0303 15  LEU L CG  
3129 C CD1 . LEU C 15  ? 1.9462 1.9720 1.6973 -0.1122 0.0131  -0.0243 15  LEU L CD1 
3130 C CD2 . LEU C 15  ? 2.3189 2.3260 2.0803 -0.1026 0.0153  -0.0267 15  LEU L CD2 
3131 N N   . GLY C 16  ? 2.0437 2.0366 1.8087 -0.0990 0.0090  -0.0290 16  GLY L N   
3132 C CA  . GLY C 16  ? 2.2354 2.2265 2.0018 -0.0986 0.0059  -0.0269 16  GLY L CA  
3133 C C   . GLY C 16  ? 2.1887 2.1747 1.9563 -0.0969 0.0078  -0.0328 16  GLY L C   
3134 O O   . GLY C 16  ? 2.1025 2.0906 1.8688 -0.0987 0.0063  -0.0332 16  GLY L O   
3135 N N   . GLN C 17  ? 2.1610 2.1404 1.9313 -0.0938 0.0108  -0.0371 17  GLN L N   
3136 C CA  . GLN C 17  ? 2.1198 2.0938 1.8923 -0.0921 0.0122  -0.0422 17  GLN L CA  
3137 C C   . GLN C 17  ? 1.9844 1.9493 1.7622 -0.0873 0.0124  -0.0411 17  GLN L C   
3138 O O   . GLN C 17  ? 2.0977 2.0584 1.8775 -0.0856 0.0149  -0.0443 17  GLN L O   
3139 C CB  . GLN C 17  ? 2.0898 2.0655 1.8603 -0.0938 0.0158  -0.0498 17  GLN L CB  
3140 C CG  . GLN C 17  ? 2.1205 2.0912 1.8933 -0.0927 0.0167  -0.0550 17  GLN L CG  
3141 C CD  . GLN C 17  ? 2.1654 2.1384 1.9365 -0.0947 0.0197  -0.0627 17  GLN L CD  
3142 O OE1 . GLN C 17  ? 2.0538 2.0329 1.8214 -0.0970 0.0215  -0.0645 17  GLN L OE1 
3143 N NE2 . GLN C 17  ? 2.2422 2.2105 2.0162 -0.0939 0.0202  -0.0674 17  GLN L NE2 
3144 N N   . PRO C 18  ? 2.0167 1.9788 1.7971 -0.0853 0.0096  -0.0366 18  PRO L N   
3145 C CA  . PRO C 18  ? 2.1838 2.1377 1.9688 -0.0810 0.0096  -0.0355 18  PRO L CA  
3146 C C   . PRO C 18  ? 2.1647 2.1130 1.9519 -0.0795 0.0122  -0.0409 18  PRO L C   
3147 O O   . PRO C 18  ? 2.2508 2.1989 2.0382 -0.0803 0.0124  -0.0437 18  PRO L O   
3148 C CB  . PRO C 18  ? 2.3527 2.3063 2.1397 -0.0798 0.0065  -0.0316 18  PRO L CB  
3149 C CG  . PRO C 18  ? 2.2708 2.2320 2.0550 -0.0831 0.0041  -0.0282 18  PRO L CG  
3150 C CD  . PRO C 18  ? 2.1837 2.1507 1.9632 -0.0870 0.0061  -0.0316 18  PRO L CD  
3151 N N   . ALA C 19  ? 2.0304 1.9740 1.8195 -0.0776 0.0140  -0.0420 19  ALA L N   
3152 C CA  . ALA C 19  ? 2.2089 2.1467 2.0010 -0.0762 0.0161  -0.0464 19  ALA L CA  
3153 C C   . ALA C 19  ? 2.3381 2.2685 2.1339 -0.0726 0.0154  -0.0438 19  ALA L C   
3154 O O   . ALA C 19  ? 2.1616 2.0911 1.9576 -0.0710 0.0137  -0.0392 19  ALA L O   
3155 C CB  . ALA C 19  ? 1.8869 1.8256 1.6788 -0.0773 0.0190  -0.0507 19  ALA L CB  
3156 N N   . SER C 20  ? 2.3664 2.2914 2.1652 -0.0716 0.0165  -0.0469 20  SER L N   
3157 C CA  . SER C 20  ? 2.2844 2.2027 2.0864 -0.0687 0.0158  -0.0449 20  SER L CA  
3158 C C   . SER C 20  ? 2.2425 2.1552 2.0476 -0.0680 0.0176  -0.0476 20  SER L C   
3159 O O   . SER C 20  ? 2.1049 2.0182 1.9112 -0.0695 0.0192  -0.0521 20  SER L O   
3160 C CB  . SER C 20  ? 2.4608 2.3783 2.2638 -0.0684 0.0147  -0.0448 20  SER L CB  
3161 O OG  . SER C 20  ? 2.7415 2.6536 2.5469 -0.0658 0.0140  -0.0426 20  SER L OG  
3162 N N   . ILE C 21  ? 2.2585 2.1657 2.0654 -0.0656 0.0171  -0.0449 21  ILE L N   
3163 C CA  . ILE C 21  ? 2.0472 1.9485 1.8576 -0.0647 0.0182  -0.0464 21  ILE L CA  
3164 C C   . ILE C 21  ? 2.1315 2.0271 1.9440 -0.0631 0.0171  -0.0448 21  ILE L C   
3165 O O   . ILE C 21  ? 2.1473 2.0417 1.9586 -0.0613 0.0156  -0.0412 21  ILE L O   
3166 C CB  . ILE C 21  ? 1.9828 1.8830 1.7932 -0.0637 0.0185  -0.0442 21  ILE L CB  
3167 C CG1 . ILE C 21  ? 2.0587 1.9654 1.8670 -0.0657 0.0200  -0.0459 21  ILE L CG1 
3168 C CG2 . ILE C 21  ? 1.9225 1.8159 1.7369 -0.0626 0.0193  -0.0450 21  ILE L CG2 
3169 C CD1 . ILE C 21  ? 2.2386 2.1459 2.0462 -0.0650 0.0199  -0.0426 21  ILE L CD1 
3170 N N   . SER C 22  ? 2.0831 1.9755 1.8989 -0.0638 0.0176  -0.0475 22  SER L N   
3171 C CA  . SER C 22  ? 1.9239 1.8121 1.7415 -0.0630 0.0165  -0.0462 22  SER L CA  
3172 C C   . SER C 22  ? 1.6688 1.5502 1.4896 -0.0621 0.0166  -0.0455 22  SER L C   
3173 O O   . SER C 22  ? 1.5309 1.4104 1.3549 -0.0630 0.0177  -0.0481 22  SER L O   
3174 C CB  . SER C 22  ? 1.9548 1.8443 1.7742 -0.0649 0.0164  -0.0489 22  SER L CB  
3175 O OG  . SER C 22  ? 1.9822 1.8718 1.8044 -0.0666 0.0175  -0.0531 22  SER L OG  
3176 N N   . CYS C 23  ? 1.7656 1.6434 1.5857 -0.0605 0.0154  -0.0422 23  CYS L N   
3177 C CA  . CYS C 23  ? 1.7180 1.5893 1.5405 -0.0597 0.0149  -0.0408 23  CYS L CA  
3178 C C   . CYS C 23  ? 1.4450 1.3143 1.2684 -0.0602 0.0140  -0.0401 23  CYS L C   
3179 O O   . CYS C 23  ? 1.4058 1.2775 1.2265 -0.0594 0.0133  -0.0385 23  CYS L O   
3180 C CB  . CYS C 23  ? 1.9149 1.7840 1.7350 -0.0575 0.0141  -0.0374 23  CYS L CB  
3181 S SG  . CYS C 23  ? 2.6522 2.5221 2.4719 -0.0570 0.0148  -0.0369 23  CYS L SG  
3182 N N   . ARG C 24  ? 1.4125 1.2779 1.2401 -0.0617 0.0137  -0.0410 24  ARG L N   
3183 C CA  . ARG C 24  ? 1.6215 1.4855 1.4502 -0.0627 0.0126  -0.0398 24  ARG L CA  
3184 C C   . ARG C 24  ? 1.5554 1.4130 1.3860 -0.0627 0.0116  -0.0377 24  ARG L C   
3185 O O   . ARG C 24  ? 1.4971 1.3509 1.3315 -0.0633 0.0117  -0.0385 24  ARG L O   
3186 C CB  . ARG C 24  ? 1.8443 1.7101 1.6767 -0.0652 0.0124  -0.0424 24  ARG L CB  
3187 C CG  . ARG C 24  ? 2.0047 1.8762 1.8359 -0.0657 0.0134  -0.0453 24  ARG L CG  
3188 C CD  . ARG C 24  ? 2.2489 2.1204 2.0850 -0.0680 0.0132  -0.0488 24  ARG L CD  
3189 N NE  . ARG C 24  ? 2.3047 2.1757 2.1432 -0.0698 0.0115  -0.0477 24  ARG L NE  
3190 C CZ  . ARG C 24  ? 2.2050 2.0771 2.0474 -0.0720 0.0107  -0.0500 24  ARG L CZ  
3191 N NH1 . ARG C 24  ? 2.2488 2.1223 2.0932 -0.0726 0.0114  -0.0543 24  ARG L NH1 
3192 N NH2 . ARG C 24  ? 2.1554 2.0277 1.9999 -0.0737 0.0089  -0.0482 24  ARG L NH2 
3193 N N   . SER C 25  ? 1.5215 1.3781 1.3496 -0.0622 0.0107  -0.0351 25  SER L N   
3194 C CA  . SER C 25  ? 1.3696 1.2204 1.1982 -0.0622 0.0095  -0.0327 25  SER L CA  
3195 C C   . SER C 25  ? 1.5781 1.4276 1.4097 -0.0650 0.0083  -0.0319 25  SER L C   
3196 O O   . SER C 25  ? 1.6138 1.4675 1.4461 -0.0665 0.0082  -0.0326 25  SER L O   
3197 C CB  . SER C 25  ? 1.2424 1.0930 1.0659 -0.0599 0.0092  -0.0305 25  SER L CB  
3198 O OG  . SER C 25  ? 1.4936 1.3472 1.3150 -0.0604 0.0089  -0.0298 25  SER L OG  
3199 N N   . SER C 26  ? 1.5581 1.4019 1.3919 -0.0660 0.0070  -0.0300 26  SER L N   
3200 C CA  . SER C 26  ? 1.6980 1.5404 1.5349 -0.0690 0.0053  -0.0284 26  SER L CA  
3201 C C   . SER C 26  ? 1.7075 1.5518 1.5394 -0.0691 0.0048  -0.0260 26  SER L C   
3202 O O   . SER C 26  ? 1.8028 1.6496 1.6358 -0.0716 0.0039  -0.0250 26  SER L O   
3203 C CB  . SER C 26  ? 1.7920 1.6276 1.6336 -0.0703 0.0039  -0.0270 26  SER L CB  
3204 O OG  . SER C 26  ? 1.8640 1.6958 1.7020 -0.0687 0.0036  -0.0248 26  SER L OG  
3205 N N   . GLN C 27  ? 1.6661 1.5096 1.4929 -0.0664 0.0053  -0.0252 27  GLN L N   
3206 C CA  . GLN C 27  ? 1.7465 1.5922 1.5683 -0.0660 0.0052  -0.0238 27  GLN L CA  
3207 C C   . GLN C 27  ? 1.6220 1.4711 1.4394 -0.0624 0.0066  -0.0251 27  GLN L C   
3208 O O   . GLN C 27  ? 1.5839 1.4325 1.4016 -0.0604 0.0072  -0.0262 27  GLN L O   
3209 C CB  . GLN C 27  ? 1.7830 1.6230 1.6034 -0.0666 0.0037  -0.0213 27  GLN L CB  
3210 C CG  . GLN C 27  ? 1.8423 1.6791 1.6671 -0.0706 0.0018  -0.0192 27  GLN L CG  
3211 C CD  . GLN C 27  ? 2.1369 1.9679 1.9600 -0.0714 0.0001  -0.0166 27  GLN L CD  
3212 O OE1 . GLN C 27  ? 1.9260 1.7537 1.7462 -0.0688 0.0003  -0.0165 27  GLN L OE1 
3213 N NE2 . GLN C 27  ? 2.3185 2.1485 2.1437 -0.0753 -0.0018 -0.0140 27  GLN L NE2 
3214 N N   . GLY C 28  ? 1.5206 1.3739 1.3344 -0.0617 0.0070  -0.0248 28  GLY L N   
3215 C CA  . GLY C 28  ? 1.6443 1.5005 1.4546 -0.0582 0.0079  -0.0259 28  GLY L CA  
3216 C C   . GLY C 28  ? 1.7729 1.6238 1.5815 -0.0556 0.0072  -0.0255 28  GLY L C   
3217 O O   . GLY C 28  ? 1.9920 1.8374 1.7999 -0.0563 0.0061  -0.0240 28  GLY L O   
3218 N N   . LEU C 29  ? 1.7750 1.6274 1.5829 -0.0528 0.0076  -0.0264 29  LEU L N   
3219 C CA  . LEU C 29  ? 1.7490 1.5965 1.5561 -0.0505 0.0066  -0.0256 29  LEU L CA  
3220 C C   . LEU C 29  ? 1.7244 1.5727 1.5285 -0.0472 0.0061  -0.0259 29  LEU L C   
3221 O O   . LEU C 29  ? 1.6885 1.5357 1.4925 -0.0449 0.0053  -0.0256 29  LEU L O   
3222 C CB  . LEU C 29  ? 1.6938 1.5421 1.5032 -0.0502 0.0070  -0.0261 29  LEU L CB  
3223 C CG  . LEU C 29  ? 1.8443 1.6909 1.6574 -0.0530 0.0074  -0.0264 29  LEU L CG  
3224 C CD1 . LEU C 29  ? 1.9307 1.7785 1.7456 -0.0526 0.0080  -0.0271 29  LEU L CD1 
3225 C CD2 . LEU C 29  ? 1.8110 1.6508 1.6252 -0.0543 0.0063  -0.0247 29  LEU L CD2 
3226 N N   . VAL C 30  ? 1.6903 1.5410 1.4921 -0.0471 0.0064  -0.0265 30  VAL L N   
3227 C CA  . VAL C 30  ? 1.5358 1.3870 1.3351 -0.0439 0.0060  -0.0273 30  VAL L CA  
3228 C C   . VAL C 30  ? 1.5834 1.4276 1.3804 -0.0436 0.0044  -0.0264 30  VAL L C   
3229 O O   . VAL C 30  ? 1.7618 1.6017 1.5593 -0.0462 0.0039  -0.0249 30  VAL L O   
3230 C CB  . VAL C 30  ? 1.4363 1.2944 1.2345 -0.0439 0.0075  -0.0288 30  VAL L CB  
3231 C CG1 . VAL C 30  ? 1.3487 1.2077 1.1448 -0.0403 0.0072  -0.0305 30  VAL L CG1 
3232 C CG2 . VAL C 30  ? 1.7228 1.5873 1.5234 -0.0444 0.0087  -0.0294 30  VAL L CG2 
3233 N N   . TYR C 31  ? 1.4406 1.2833 1.2357 -0.0405 0.0034  -0.0273 31  TYR L N   
3234 C CA  . TYR C 31  ? 1.5071 1.3428 1.2999 -0.0400 0.0016  -0.0265 31  TYR L CA  
3235 C C   . TYR C 31  ? 1.3106 1.1477 1.1004 -0.0375 0.0014  -0.0288 31  TYR L C   
3236 O O   . TYR C 31  ? 1.1337 0.9769 0.9241 -0.0356 0.0026  -0.0308 31  TYR L O   
3237 C CB  . TYR C 31  ? 1.5168 1.3470 1.3115 -0.0386 -0.0004 -0.0248 31  TYR L CB  
3238 C CG  . TYR C 31  ? 1.4980 1.3202 1.2912 -0.0391 -0.0025 -0.0231 31  TYR L CG  
3239 C CD1 . TYR C 31  ? 1.6953 1.5143 1.4882 -0.0426 -0.0024 -0.0215 31  TYR L CD1 
3240 C CD2 . TYR C 31  ? 1.6339 1.4514 1.4263 -0.0363 -0.0049 -0.0228 31  TYR L CD2 
3241 C CE1 . TYR C 31  ? 1.7670 1.5786 1.5588 -0.0433 -0.0046 -0.0197 31  TYR L CE1 
3242 C CE2 . TYR C 31  ? 1.7509 1.5609 1.5420 -0.0369 -0.0071 -0.0211 31  TYR L CE2 
3243 C CZ  . TYR C 31  ? 1.6483 1.4554 1.4390 -0.0404 -0.0068 -0.0195 31  TYR L CZ  
3244 O OH  . TYR C 31  ? 1.4044 1.2040 1.1940 -0.0412 -0.0092 -0.0175 31  TYR L OH  
3245 N N   . ILE C 32  ? 1.3464 1.1779 1.1332 -0.0376 0.0000  -0.0286 32  ILE L N   
3246 C CA  . ILE C 32  ? 1.2586 1.0909 1.0420 -0.0353 -0.0002 -0.0313 32  ILE L CA  
3247 C C   . ILE C 32  ? 1.4476 1.2812 1.2331 -0.0308 -0.0010 -0.0332 32  ILE L C   
3248 O O   . ILE C 32  ? 1.4019 1.2401 1.1867 -0.0285 0.0000  -0.0364 32  ILE L O   
3249 C CB  . ILE C 32  ? 1.1834 1.0083 0.9634 -0.0363 -0.0022 -0.0304 32  ILE L CB  
3250 C CG1 . ILE C 32  ? 1.2953 1.1201 1.0734 -0.0410 -0.0015 -0.0285 32  ILE L CG1 
3251 C CG2 . ILE C 32  ? 1.2698 1.0945 1.0464 -0.0333 -0.0028 -0.0338 32  ILE L CG2 
3252 C CD1 . ILE C 32  ? 1.3438 1.1609 1.1192 -0.0426 -0.0038 -0.0268 32  ILE L CD1 
3253 N N   . ASP C 33  ? 1.5737 1.4034 1.3623 -0.0295 -0.0030 -0.0314 33  ASP L N   
3254 C CA  . ASP C 33  ? 1.5236 1.3545 1.3151 -0.0256 -0.0044 -0.0325 33  ASP L CA  
3255 C C   . ASP C 33  ? 1.4394 1.2790 1.2328 -0.0246 -0.0022 -0.0345 33  ASP L C   
3256 O O   . ASP C 33  ? 1.6667 1.5089 1.4613 -0.0213 -0.0025 -0.0371 33  ASP L O   
3257 C CB  . ASP C 33  ? 1.7316 1.5592 1.5263 -0.0256 -0.0064 -0.0293 33  ASP L CB  
3258 C CG  . ASP C 33  ? 2.1946 2.0137 1.9883 -0.0257 -0.0091 -0.0272 33  ASP L CG  
3259 O OD1 . ASP C 33  ? 2.2681 2.0834 2.0587 -0.0250 -0.0101 -0.0287 33  ASP L OD1 
3260 O OD2 . ASP C 33  ? 2.3360 2.1525 2.1317 -0.0268 -0.0102 -0.0242 33  ASP L OD2 
3261 N N   . GLY C 34  ? 1.2698 1.1140 1.0641 -0.0273 -0.0001 -0.0333 34  GLY L N   
3262 C CA  . GLY C 34  ? 1.3009 1.1535 1.0971 -0.0268 0.0019  -0.0349 34  GLY L CA  
3263 C C   . GLY C 34  ? 1.4510 1.3067 1.2502 -0.0283 0.0024  -0.0330 34  GLY L C   
3264 O O   . GLY C 34  ? 1.7389 1.6010 1.5389 -0.0297 0.0044  -0.0335 34  GLY L O   
3265 N N   . ASN C 35  ? 1.3316 1.1833 1.1324 -0.0281 0.0004  -0.0308 35  ASN L N   
3266 C CA  . ASN C 35  ? 1.5385 1.3935 1.3419 -0.0293 0.0006  -0.0293 35  ASN L CA  
3267 C C   . ASN C 35  ? 1.6141 1.4666 1.4168 -0.0328 0.0015  -0.0276 35  ASN L C   
3268 O O   . ASN C 35  ? 1.8229 1.6691 1.6244 -0.0335 0.0005  -0.0265 35  ASN L O   
3269 C CB  . ASN C 35  ? 1.3215 1.1751 1.1276 -0.0271 -0.0021 -0.0278 35  ASN L CB  
3270 C CG  . ASN C 35  ? 1.6574 1.5147 1.4659 -0.0238 -0.0031 -0.0293 35  ASN L CG  
3271 O OD1 . ASN C 35  ? 2.2091 2.0719 2.0179 -0.0234 -0.0012 -0.0314 35  ASN L OD1 
3272 N ND2 . ASN C 35  ? 1.4337 1.2882 1.2447 -0.0213 -0.0062 -0.0282 35  ASN L ND2 
3273 N N   . THR C 36  ? 1.6239 1.4813 1.4278 -0.0350 0.0031  -0.0276 36  THR L N   
3274 C CA  . THR C 36  ? 1.7314 1.5869 1.5357 -0.0380 0.0038  -0.0266 36  THR L CA  
3275 C C   . THR C 36  ? 1.7939 1.6468 1.5995 -0.0376 0.0023  -0.0248 36  THR L C   
3276 O O   . THR C 36  ? 1.8594 1.7152 1.6662 -0.0362 0.0013  -0.0242 36  THR L O   
3277 C CB  . THR C 36  ? 1.7128 1.5744 1.5181 -0.0403 0.0057  -0.0275 36  THR L CB  
3278 O OG1 . THR C 36  ? 1.6846 1.5497 1.4891 -0.0406 0.0069  -0.0288 36  THR L OG1 
3279 C CG2 . THR C 36  ? 1.6976 1.5572 1.5039 -0.0434 0.0065  -0.0272 36  THR L CG2 
3280 N N   . TYR C 37  ? 1.5207 1.3683 1.3263 -0.0390 0.0021  -0.0236 37  TYR L N   
3281 C CA  . TYR C 37  ? 1.6999 1.5446 1.5067 -0.0387 0.0007  -0.0216 37  TYR L CA  
3282 C C   . TYR C 37  ? 1.7326 1.5798 1.5410 -0.0414 0.0023  -0.0217 37  TYR L C   
3283 O O   . TYR C 37  ? 1.2839 1.1288 1.0930 -0.0434 0.0035  -0.0223 37  TYR L O   
3284 C CB  . TYR C 37  ? 1.6004 1.4375 1.4065 -0.0382 -0.0009 -0.0202 37  TYR L CB  
3285 C CG  . TYR C 37  ? 1.8584 1.6925 1.6633 -0.0352 -0.0033 -0.0199 37  TYR L CG  
3286 C CD1 . TYR C 37  ? 2.0037 1.8362 1.8099 -0.0334 -0.0058 -0.0179 37  TYR L CD1 
3287 C CD2 . TYR C 37  ? 1.5632 1.3966 1.3658 -0.0343 -0.0030 -0.0217 37  TYR L CD2 
3288 C CE1 . TYR C 37  ? 2.1214 1.9508 1.9272 -0.0305 -0.0083 -0.0179 37  TYR L CE1 
3289 C CE2 . TYR C 37  ? 1.4664 1.2973 1.2682 -0.0314 -0.0051 -0.0221 37  TYR L CE2 
3290 C CZ  . TYR C 37  ? 2.0401 1.8686 1.8436 -0.0294 -0.0079 -0.0204 37  TYR L CZ  
3291 O OH  . TYR C 37  ? 2.0187 1.8442 1.8220 -0.0264 -0.0104 -0.0210 37  TYR L OH  
3292 N N   . LEU C 38  ? 1.7849 1.6366 1.5941 -0.0414 0.0023  -0.0213 38  LEU L N   
3293 C CA  . LEU C 38  ? 1.7776 1.6325 1.5880 -0.0438 0.0039  -0.0219 38  LEU L CA  
3294 C C   . LEU C 38  ? 2.1162 1.9740 1.9270 -0.0436 0.0029  -0.0201 38  LEU L C   
3295 O O   . LEU C 38  ? 2.4796 2.3434 2.2903 -0.0447 0.0036  -0.0206 38  LEU L O   
3296 C CB  . LEU C 38  ? 1.9352 1.7955 1.7455 -0.0453 0.0057  -0.0243 38  LEU L CB  
3297 C CG  . LEU C 38  ? 1.9296 1.7884 1.7399 -0.0464 0.0069  -0.0259 38  LEU L CG  
3298 C CD1 . LEU C 38  ? 1.8051 1.6701 1.6156 -0.0476 0.0080  -0.0276 38  LEU L CD1 
3299 C CD2 . LEU C 38  ? 1.9570 1.8119 1.7693 -0.0485 0.0077  -0.0264 38  LEU L CD2 
3300 N N   . ASN C 39  ? 1.9948 1.8485 1.8061 -0.0425 0.0010  -0.0176 39  ASN L N   
3301 C CA  . ASN C 39  ? 2.0656 1.9217 1.8775 -0.0426 -0.0004 -0.0150 39  ASN L CA  
3302 C C   . ASN C 39  ? 2.0458 1.9060 1.8583 -0.0452 0.0018  -0.0157 39  ASN L C   
3303 O O   . ASN C 39  ? 1.9392 1.7965 1.7529 -0.0460 0.0027  -0.0155 39  ASN L O   
3304 C CB  . ASN C 39  ? 2.1730 2.0228 1.9857 -0.0411 -0.0028 -0.0123 39  ASN L CB  
3305 C CG  . ASN C 39  ? 2.3054 2.1504 2.1173 -0.0386 -0.0045 -0.0125 39  ASN L CG  
3306 O OD1 . ASN C 39  ? 2.1399 1.9876 1.9510 -0.0376 -0.0044 -0.0141 39  ASN L OD1 
3307 N ND2 . ASN C 39  ? 2.2317 2.0698 2.0436 -0.0378 -0.0059 -0.0112 39  ASN L ND2 
3308 N N   . TRP C 40  ? 2.2008 2.0681 2.0125 -0.0465 0.0025  -0.0165 40  TRP L N   
3309 C CA  . TRP C 40  ? 1.7882 1.6599 1.6000 -0.0491 0.0052  -0.0188 40  TRP L CA  
3310 C C   . TRP C 40  ? 1.6620 1.5349 1.4746 -0.0501 0.0053  -0.0169 40  TRP L C   
3311 O O   . TRP C 40  ? 1.6306 1.5061 1.4428 -0.0499 0.0032  -0.0136 40  TRP L O   
3312 C CB  . TRP C 40  ? 2.1062 1.9852 1.9165 -0.0503 0.0056  -0.0200 40  TRP L CB  
3313 C CG  . TRP C 40  ? 2.3702 2.2495 2.1803 -0.0506 0.0070  -0.0231 40  TRP L CG  
3314 C CD1 . TRP C 40  ? 2.4650 2.3440 2.2747 -0.0491 0.0060  -0.0230 40  TRP L CD1 
3315 C CD2 . TRP C 40  ? 2.1853 2.0657 1.9958 -0.0526 0.0096  -0.0268 40  TRP L CD2 
3316 N NE1 . TRP C 40  ? 2.4411 2.3211 2.2508 -0.0502 0.0077  -0.0259 40  TRP L NE1 
3317 C CE2 . TRP C 40  ? 2.4682 2.3489 2.2785 -0.0524 0.0097  -0.0282 40  TRP L CE2 
3318 C CE3 . TRP C 40  ? 1.7558 1.6372 1.5673 -0.0545 0.0117  -0.0291 40  TRP L CE3 
3319 C CZ2 . TRP C 40  ? 2.3093 2.1908 2.1205 -0.0541 0.0114  -0.0314 40  TRP L CZ2 
3320 C CZ3 . TRP C 40  ? 1.7508 1.6328 1.5635 -0.0561 0.0134  -0.0329 40  TRP L CZ3 
3321 C CH2 . TRP C 40  ? 2.0811 1.9630 1.8936 -0.0559 0.0131  -0.0338 40  TRP L CH2 
3322 N N   . PHE C 41  ? 1.4878 1.3593 1.3020 -0.0513 0.0076  -0.0189 41  PHE L N   
3323 C CA  . PHE C 41  ? 1.5586 1.4316 1.3740 -0.0522 0.0081  -0.0173 41  PHE L CA  
3324 C C   . PHE C 41  ? 1.7462 1.6275 1.5607 -0.0547 0.0104  -0.0193 41  PHE L C   
3325 O O   . PHE C 41  ? 1.7366 1.6204 1.5509 -0.0560 0.0127  -0.0235 41  PHE L O   
3326 C CB  . PHE C 41  ? 1.7334 1.6005 1.5519 -0.0521 0.0093  -0.0182 41  PHE L CB  
3327 C CG  . PHE C 41  ? 1.8129 1.6722 1.6322 -0.0501 0.0069  -0.0154 41  PHE L CG  
3328 C CD1 . PHE C 41  ? 1.5228 1.3809 1.3415 -0.0488 0.0038  -0.0110 41  PHE L CD1 
3329 C CD2 . PHE C 41  ? 2.1525 2.0055 1.9734 -0.0497 0.0074  -0.0169 41  PHE L CD2 
3330 C CE1 . PHE C 41  ? 1.5557 1.4061 1.3749 -0.0470 0.0014  -0.0088 41  PHE L CE1 
3331 C CE2 . PHE C 41  ? 2.1080 1.9538 1.9291 -0.0482 0.0050  -0.0144 41  PHE L CE2 
3332 C CZ  . PHE C 41  ? 1.7874 1.6318 1.6075 -0.0467 0.0021  -0.0105 41  PHE L CZ  
3333 N N   . GLN C 42  ? 1.7429 1.6282 1.5572 -0.0556 0.0097  -0.0163 42  GLN L N   
3334 C CA  . GLN C 42  ? 1.7087 1.6022 1.5221 -0.0581 0.0120  -0.0178 42  GLN L CA  
3335 C C   . GLN C 42  ? 1.5491 1.4431 1.3643 -0.0585 0.0121  -0.0149 42  GLN L C   
3336 O O   . GLN C 42  ? 1.5132 1.4046 1.3290 -0.0574 0.0090  -0.0099 42  GLN L O   
3337 C CB  . GLN C 42  ? 1.8613 1.7625 1.6713 -0.0597 0.0107  -0.0162 42  GLN L CB  
3338 C CG  . GLN C 42  ? 1.9336 1.8441 1.7417 -0.0629 0.0133  -0.0184 42  GLN L CG  
3339 C CD  . GLN C 42  ? 1.7270 1.6451 1.5315 -0.0649 0.0118  -0.0169 42  GLN L CD  
3340 O OE1 . GLN C 42  ? 2.2265 2.1429 2.0305 -0.0638 0.0089  -0.0145 42  GLN L OE1 
3341 N NE2 . GLN C 42  ? 1.8255 1.7523 1.6276 -0.0680 0.0137  -0.0183 42  GLN L NE2 
3342 N N   . GLN C 43  ? 1.5133 1.4110 1.3299 -0.0600 0.0155  -0.0181 43  GLN L N   
3343 C CA  . GLN C 43  ? 1.6814 1.5819 1.4999 -0.0608 0.0163  -0.0159 43  GLN L CA  
3344 C C   . GLN C 43  ? 1.8833 1.7949 1.6996 -0.0638 0.0189  -0.0179 43  GLN L C   
3345 O O   . GLN C 43  ? 1.8291 1.7435 1.6460 -0.0647 0.0225  -0.0237 43  GLN L O   
3346 C CB  . GLN C 43  ? 1.7469 1.6415 1.5703 -0.0597 0.0182  -0.0180 43  GLN L CB  
3347 C CG  . GLN C 43  ? 1.7160 1.6126 1.5422 -0.0602 0.0186  -0.0148 43  GLN L CG  
3348 C CD  . GLN C 43  ? 1.6888 1.5798 1.5206 -0.0592 0.0205  -0.0169 43  GLN L CD  
3349 O OE1 . GLN C 43  ? 1.6114 1.4989 1.4453 -0.0588 0.0222  -0.0216 43  GLN L OE1 
3350 N NE2 . GLN C 43  ? 1.8245 1.7147 1.6592 -0.0590 0.0198  -0.0130 43  GLN L NE2 
3351 N N   . ARG C 44  ? 2.0561 1.9741 1.8698 -0.0653 0.0169  -0.0134 44  ARG L N   
3352 C CA  . ARG C 44  ? 2.1376 2.0668 1.9487 -0.0686 0.0193  -0.0147 44  ARG L CA  
3353 C C   . ARG C 44  ? 2.1921 2.1231 2.0067 -0.0689 0.0226  -0.0164 44  ARG L C   
3354 O O   . ARG C 44  ? 2.2556 2.1838 2.0730 -0.0680 0.0211  -0.0118 44  ARG L O   
3355 C CB  . ARG C 44  ? 2.1678 2.1036 1.9760 -0.0706 0.0160  -0.0085 44  ARG L CB  
3356 C CG  . ARG C 44  ? 2.1344 2.0700 1.9397 -0.0706 0.0130  -0.0072 44  ARG L CG  
3357 C CD  . ARG C 44  ? 2.0878 2.0321 1.8903 -0.0735 0.0101  -0.0018 44  ARG L CD  
3358 N NE  . ARG C 44  ? 2.5817 2.5247 2.3866 -0.0731 0.0063  0.0053  44  ARG L NE  
3359 C CZ  . ARG C 44  ? 2.6728 2.6092 2.4796 -0.0709 0.0016  0.0099  44  ARG L CZ  
3360 N NH1 . ARG C 44  ? 2.8369 2.7673 2.6437 -0.0686 0.0004  0.0080  44  ARG L NH1 
3361 N NH2 . ARG C 44  ? 2.6152 2.5512 2.4243 -0.0710 -0.0020 0.0164  44  ARG L NH2 
3362 N N   . PRO C 45  ? 2.1185 2.0540 1.9335 -0.0700 0.0271  -0.0230 45  PRO L N   
3363 C CA  . PRO C 45  ? 1.8844 1.8199 1.7043 -0.0696 0.0304  -0.0256 45  PRO L CA  
3364 C C   . PRO C 45  ? 1.9798 1.9217 1.8001 -0.0710 0.0303  -0.0206 45  PRO L C   
3365 O O   . PRO C 45  ? 1.9472 1.8988 1.7633 -0.0738 0.0300  -0.0183 45  PRO L O   
3366 C CB  . PRO C 45  ? 1.9908 1.9321 1.8102 -0.0710 0.0348  -0.0338 45  PRO L CB  
3367 C CG  . PRO C 45  ? 2.3521 2.3000 2.1649 -0.0733 0.0338  -0.0339 45  PRO L CG  
3368 C CD  . PRO C 45  ? 2.2141 2.1550 2.0255 -0.0718 0.0291  -0.0286 45  PRO L CD  
3369 N N   . GLY C 46  ? 1.9098 1.8464 1.7355 -0.0693 0.0302  -0.0185 46  GLY L N   
3370 C CA  . GLY C 46  ? 1.6356 1.5765 1.4626 -0.0702 0.0292  -0.0125 46  GLY L CA  
3371 C C   . GLY C 46  ? 1.6495 1.5835 1.4768 -0.0689 0.0237  -0.0046 46  GLY L C   
3372 O O   . GLY C 46  ? 1.6034 1.5388 1.4330 -0.0692 0.0223  0.0008  46  GLY L O   
3373 N N   . GLN C 47  ? 2.0223 1.9491 1.8475 -0.0673 0.0205  -0.0039 47  GLN L N   
3374 C CA  . GLN C 47  ? 2.0153 1.9351 1.8408 -0.0658 0.0151  0.0029  47  GLN L CA  
3375 C C   . GLN C 47  ? 1.9197 1.8268 1.7477 -0.0626 0.0139  0.0015  47  GLN L C   
3376 O O   . GLN C 47  ? 1.8625 1.7662 1.6933 -0.0617 0.0170  -0.0035 47  GLN L O   
3377 C CB  . GLN C 47  ? 1.8784 1.8017 1.6993 -0.0669 0.0118  0.0057  47  GLN L CB  
3378 C CG  . GLN C 47  ? 1.6653 1.6018 1.4826 -0.0706 0.0133  0.0059  47  GLN L CG  
3379 C CD  . GLN C 47  ? 1.9947 1.9341 1.8078 -0.0718 0.0103  0.0077  47  GLN L CD  
3380 O OE1 . GLN C 47  ? 2.2550 2.1869 2.0684 -0.0695 0.0069  0.0091  47  GLN L OE1 
3381 N NE2 . GLN C 47  ? 1.8023 1.7532 1.6118 -0.0754 0.0114  0.0078  47  GLN L NE2 
3382 N N   . SER C 48  ? 2.0046 1.9049 1.8319 -0.0609 0.0092  0.0059  48  SER L N   
3383 C CA  . SER C 48  ? 1.6425 1.5313 1.4714 -0.0581 0.0076  0.0052  48  SER L CA  
3384 C C   . SER C 48  ? 1.7105 1.5971 1.5361 -0.0572 0.0066  0.0027  48  SER L C   
3385 O O   . SER C 48  ? 1.9647 1.8569 1.7871 -0.0582 0.0053  0.0038  48  SER L O   
3386 C CB  . SER C 48  ? 1.7237 1.6059 1.5545 -0.0567 0.0030  0.0115  48  SER L CB  
3387 O OG  . SER C 48  ? 2.0315 1.9159 1.8600 -0.0568 -0.0011 0.0159  48  SER L OG  
3388 N N   . PRO C 49  ? 1.4529 1.3317 1.2793 -0.0554 0.0071  -0.0005 49  PRO L N   
3389 C CA  . PRO C 49  ? 1.4891 1.3663 1.3126 -0.0546 0.0065  -0.0031 49  PRO L CA  
3390 C C   . PRO C 49  ? 1.5163 1.3921 1.3379 -0.0534 0.0021  0.0012  49  PRO L C   
3391 O O   . PRO C 49  ? 1.4749 1.3466 1.2979 -0.0523 -0.0012 0.0058  49  PRO L O   
3392 C CB  . PRO C 49  ? 1.4026 1.2709 1.2281 -0.0530 0.0072  -0.0058 49  PRO L CB  
3393 C CG  . PRO C 49  ? 1.4493 1.3176 1.2788 -0.0538 0.0099  -0.0072 49  PRO L CG  
3394 C CD  . PRO C 49  ? 1.5816 1.4539 1.4120 -0.0546 0.0088  -0.0025 49  PRO L CD  
3395 N N   . ARG C 50  ? 1.4877 1.3671 1.3065 -0.0537 0.0019  -0.0005 50  ARG L N   
3396 C CA  . ARG C 50  ? 1.4824 1.3610 1.3002 -0.0524 -0.0022 0.0028  50  ARG L CA  
3397 C C   . ARG C 50  ? 1.6109 1.4882 1.4270 -0.0514 -0.0016 -0.0008 50  ARG L C   
3398 O O   . ARG C 50  ? 1.7422 1.6235 1.5568 -0.0528 0.0015  -0.0049 50  ARG L O   
3399 C CB  . ARG C 50  ? 1.4270 1.3142 1.2437 -0.0546 -0.0038 0.0063  50  ARG L CB  
3400 C CG  . ARG C 50  ? 1.8901 1.7790 1.7087 -0.0556 -0.0053 0.0112  50  ARG L CG  
3401 C CD  . ARG C 50  ? 2.1351 2.0332 1.9526 -0.0582 -0.0073 0.0152  50  ARG L CD  
3402 N NE  . ARG C 50  ? 2.6144 2.5149 2.4338 -0.0595 -0.0088 0.0202  50  ARG L NE  
3403 C CZ  . ARG C 50  ? 2.6887 2.5980 2.5077 -0.0624 -0.0105 0.0245  50  ARG L CZ  
3404 N NH1 . ARG C 50  ? 2.4379 2.3544 2.2543 -0.0645 -0.0108 0.0243  50  ARG L NH1 
3405 N NH2 . ARG C 50  ? 2.8342 2.7453 2.6553 -0.0636 -0.0119 0.0293  50  ARG L NH2 
3406 N N   . ARG C 51  ? 1.4829 1.3547 1.2992 -0.0489 -0.0047 0.0006  51  ARG L N   
3407 C CA  . ARG C 51  ? 1.5777 1.4487 1.3927 -0.0479 -0.0040 -0.0027 51  ARG L CA  
3408 C C   . ARG C 51  ? 1.5605 1.4387 1.3743 -0.0488 -0.0051 -0.0021 51  ARG L C   
3409 O O   . ARG C 51  ? 1.8983 1.7816 1.7123 -0.0502 -0.0070 0.0014  51  ARG L O   
3410 C CB  . ARG C 51  ? 1.7500 1.6132 1.5656 -0.0449 -0.0065 -0.0021 51  ARG L CB  
3411 C CG  . ARG C 51  ? 1.7531 1.6085 1.5695 -0.0439 -0.0059 -0.0028 51  ARG L CG  
3412 C CD  . ARG C 51  ? 1.8414 1.6909 1.6574 -0.0412 -0.0082 -0.0029 51  ARG L CD  
3413 N NE  . ARG C 51  ? 2.0455 1.8872 1.8618 -0.0403 -0.0084 -0.0032 51  ARG L NE  
3414 C CZ  . ARG C 51  ? 2.2810 2.1202 2.0965 -0.0408 -0.0059 -0.0063 51  ARG L CZ  
3415 N NH1 . ARG C 51  ? 2.4505 2.2939 2.2661 -0.0428 -0.0026 -0.0090 51  ARG L NH1 
3416 N NH2 . ARG C 51  ? 2.2364 2.0689 2.0512 -0.0395 -0.0069 -0.0067 51  ARG L NH2 
3417 N N   . LEU C 52  ? 1.5974 1.4762 1.4101 -0.0483 -0.0040 -0.0052 52  LEU L N   
3418 C CA  . LEU C 52  ? 1.7331 1.6189 1.5448 -0.0495 -0.0046 -0.0052 52  LEU L CA  
3419 C C   . LEU C 52  ? 1.7628 1.6465 1.5750 -0.0472 -0.0057 -0.0064 52  LEU L C   
3420 O O   . LEU C 52  ? 1.7344 1.6213 1.5475 -0.0468 -0.0083 -0.0044 52  LEU L O   
3421 C CB  . LEU C 52  ? 1.7484 1.6400 1.5581 -0.0523 -0.0009 -0.0087 52  LEU L CB  
3422 C CG  . LEU C 52  ? 1.6046 1.5002 1.4137 -0.0548 0.0006  -0.0080 52  LEU L CG  
3423 C CD1 . LEU C 52  ? 1.6988 1.5991 1.5061 -0.0572 0.0043  -0.0126 52  LEU L CD1 
3424 C CD2 . LEU C 52  ? 1.7391 1.6405 1.5481 -0.0563 -0.0024 -0.0032 52  LEU L CD2 
3425 N N   . ILE C 53  ? 1.6317 1.5104 1.4436 -0.0458 -0.0039 -0.0095 53  ILE L N   
3426 C CA  . ILE C 53  ? 1.6841 1.5617 1.4963 -0.0439 -0.0042 -0.0112 53  ILE L CA  
3427 C C   . ILE C 53  ? 1.9357 1.8053 1.7483 -0.0414 -0.0047 -0.0116 53  ILE L C   
3428 O O   . ILE C 53  ? 2.0591 1.9254 1.8709 -0.0419 -0.0024 -0.0139 53  ILE L O   
3429 C CB  . ILE C 53  ? 1.5994 1.4806 1.4102 -0.0455 -0.0011 -0.0149 53  ILE L CB  
3430 C CG1 . ILE C 53  ? 1.6466 1.5354 1.4564 -0.0483 -0.0006 -0.0147 53  ILE L CG1 
3431 C CG2 . ILE C 53  ? 2.0228 1.9037 1.8340 -0.0436 -0.0015 -0.0162 53  ILE L CG2 
3432 C CD1 . ILE C 53  ? 1.7355 1.6291 1.5461 -0.0480 -0.0033 -0.0123 53  ILE L CD1 
3433 N N   . TYR C 54  ? 2.0039 1.8703 1.8180 -0.0390 -0.0080 -0.0094 54  TYR L N   
3434 C CA  . TYR C 54  ? 2.0113 1.8706 1.8252 -0.0366 -0.0086 -0.0102 54  TYR L CA  
3435 C C   . TYR C 54  ? 1.9807 1.8408 1.7935 -0.0361 -0.0064 -0.0138 54  TYR L C   
3436 O O   . TYR C 54  ? 2.1325 1.9980 1.9457 -0.0362 -0.0059 -0.0148 54  TYR L O   
3437 C CB  . TYR C 54  ? 1.8228 1.6794 1.6389 -0.0337 -0.0127 -0.0082 54  TYR L CB  
3438 C CG  . TYR C 54  ? 2.0303 1.8861 1.8484 -0.0337 -0.0161 -0.0039 54  TYR L CG  
3439 C CD1 . TYR C 54  ? 2.1645 2.0233 1.9856 -0.0327 -0.0196 -0.0016 54  TYR L CD1 
3440 C CD2 . TYR C 54  ? 1.8827 1.7351 1.7005 -0.0348 -0.0163 -0.0019 54  TYR L CD2 
3441 C CE1 . TYR C 54  ? 2.5468 2.4053 2.3702 -0.0330 -0.0233 0.0028  54  TYR L CE1 
3442 C CE2 . TYR C 54  ? 2.1222 1.9744 1.9421 -0.0350 -0.0197 0.0025  54  TYR L CE2 
3443 C CZ  . TYR C 54  ? 2.5051 2.3604 2.3277 -0.0342 -0.0233 0.0049  54  TYR L CZ  
3444 O OH  . TYR C 54  ? 2.4759 2.3314 2.3011 -0.0347 -0.0272 0.0097  54  TYR L OH  
3445 N N   . ASN C 55  ? 1.8648 1.7196 1.6763 -0.0357 -0.0052 -0.0154 55  ASN L N   
3446 C CA  . ASN C 55  ? 1.7287 1.5847 1.5390 -0.0357 -0.0031 -0.0184 55  ASN L CA  
3447 C C   . ASN C 55  ? 1.9329 1.7953 1.7431 -0.0381 -0.0008 -0.0197 55  ASN L C   
3448 O O   . ASN C 55  ? 2.2152 2.0791 2.0255 -0.0402 0.0002  -0.0193 55  ASN L O   
3449 C CB  . ASN C 55  ? 1.8163 1.6729 1.6271 -0.0328 -0.0045 -0.0192 55  ASN L CB  
3450 C CG  . ASN C 55  ? 2.0028 1.8527 1.8133 -0.0304 -0.0066 -0.0189 55  ASN L CG  
3451 O OD1 . ASN C 55  ? 1.9616 1.8062 1.7708 -0.0313 -0.0064 -0.0183 55  ASN L OD1 
3452 N ND2 . ASN C 55  ? 1.9203 1.7703 1.7322 -0.0275 -0.0086 -0.0194 55  ASN L ND2 
3453 N N   . VAL C 56  ? 1.9407 1.8071 1.7509 -0.0377 0.0001  -0.0215 56  VAL L N   
3454 C CA  . VAL C 56  ? 2.0818 1.9537 1.8918 -0.0401 0.0021  -0.0229 56  VAL L CA  
3455 C C   . VAL C 56  ? 2.4362 2.3141 2.2474 -0.0400 0.0009  -0.0217 56  VAL L C   
3456 O O   . VAL C 56  ? 2.4811 2.3636 2.2920 -0.0424 0.0019  -0.0220 56  VAL L O   
3457 C CB  . VAL C 56  ? 2.2627 2.1357 2.0722 -0.0403 0.0039  -0.0251 56  VAL L CB  
3458 C CG1 . VAL C 56  ? 2.3522 2.2309 2.1620 -0.0428 0.0055  -0.0263 56  VAL L CG1 
3459 C CG2 . VAL C 56  ? 1.9370 1.8043 1.7455 -0.0410 0.0047  -0.0256 56  VAL L CG2 
3460 N N   . PHE C 57  ? 2.2583 2.1363 2.0711 -0.0374 -0.0014 -0.0205 57  PHE L N   
3461 C CA  . PHE C 57  ? 2.1885 2.0725 2.0033 -0.0372 -0.0029 -0.0193 57  PHE L CA  
3462 C C   . PHE C 57  ? 2.0430 1.9256 1.8601 -0.0352 -0.0065 -0.0164 57  PHE L C   
3463 O O   . PHE C 57  ? 1.9859 1.8706 1.8060 -0.0332 -0.0084 -0.0160 57  PHE L O   
3464 C CB  . PHE C 57  ? 2.3262 2.2135 2.1420 -0.0359 -0.0021 -0.0212 57  PHE L CB  
3465 C CG  . PHE C 57  ? 2.6806 2.5721 2.4952 -0.0385 0.0005  -0.0229 57  PHE L CG  
3466 C CD1 . PHE C 57  ? 2.6645 2.5618 2.4795 -0.0407 0.0004  -0.0222 57  PHE L CD1 
3467 C CD2 . PHE C 57  ? 2.7210 2.6109 2.5343 -0.0390 0.0028  -0.0250 57  PHE L CD2 
3468 C CE1 . PHE C 57  ? 2.9013 2.8021 2.7153 -0.0431 0.0024  -0.0239 57  PHE L CE1 
3469 C CE2 . PHE C 57  ? 2.9172 2.8108 2.7299 -0.0414 0.0047  -0.0264 57  PHE L CE2 
3470 C CZ  . PHE C 57  ? 3.0199 2.9188 2.8330 -0.0434 0.0045  -0.0260 57  PHE L CZ  
3471 N N   . THR C 58  ? 1.9456 1.8251 1.7622 -0.0359 -0.0077 -0.0143 58  THR L N   
3472 C CA  . THR C 58  ? 1.9428 1.8212 1.7621 -0.0345 -0.0116 -0.0110 58  THR L CA  
3473 C C   . THR C 58  ? 1.8167 1.6966 1.6353 -0.0372 -0.0123 -0.0081 58  THR L C   
3474 O O   . THR C 58  ? 1.8065 1.6828 1.6233 -0.0381 -0.0111 -0.0081 58  THR L O   
3475 C CB  . THR C 58  ? 1.9762 1.8474 1.7964 -0.0314 -0.0133 -0.0112 58  THR L CB  
3476 O OG1 . THR C 58  ? 1.9640 1.8302 1.7814 -0.0323 -0.0115 -0.0119 58  THR L OG1 
3477 C CG2 . THR C 58  ? 1.8591 1.7298 1.6803 -0.0285 -0.0129 -0.0142 58  THR L CG2 
3478 N N   . ARG C 59  ? 1.9093 1.7948 1.7295 -0.0385 -0.0145 -0.0053 59  ARG L N   
3479 C CA  . ARG C 59  ? 1.9504 1.8387 1.7700 -0.0413 -0.0155 -0.0021 59  ARG L CA  
3480 C C   . ARG C 59  ? 1.9995 1.8824 1.8207 -0.0399 -0.0184 0.0009  59  ARG L C   
3481 O O   . ARG C 59  ? 2.1504 2.0294 1.9747 -0.0369 -0.0215 0.0019  59  ARG L O   
3482 C CB  . ARG C 59  ? 1.9255 1.8210 1.7469 -0.0430 -0.0180 0.0008  59  ARG L CB  
3483 C CG  . ARG C 59  ? 1.8772 1.7788 1.6966 -0.0452 -0.0154 -0.0016 59  ARG L CG  
3484 C CD  . ARG C 59  ? 1.8544 1.7630 1.6756 -0.0472 -0.0184 0.0017  59  ARG L CD  
3485 N NE  . ARG C 59  ? 2.2120 2.1261 2.0314 -0.0493 -0.0162 -0.0005 59  ARG L NE  
3486 C CZ  . ARG C 59  ? 2.4190 2.3394 2.2398 -0.0511 -0.0183 0.0017  59  ARG L CZ  
3487 N NH1 . ARG C 59  ? 2.5350 2.4571 2.3596 -0.0511 -0.0229 0.0064  59  ARG L NH1 
3488 N NH2 . ARG C 59  ? 2.5026 2.4276 2.3212 -0.0532 -0.0161 -0.0005 59  ARG L NH2 
3489 N N   . ASP C 60  ? 1.8505 1.7333 1.6699 -0.0420 -0.0174 0.0023  60  ASP L N   
3490 C CA  . ASP C 60  ? 2.0737 1.9521 1.8948 -0.0413 -0.0202 0.0058  60  ASP L CA  
3491 C C   . ASP C 60  ? 2.1922 2.0755 2.0157 -0.0429 -0.0243 0.0110  60  ASP L C   
3492 O O   . ASP C 60  ? 2.1059 1.9967 1.9288 -0.0454 -0.0241 0.0119  60  ASP L O   
3493 C CB  . ASP C 60  ? 2.1941 2.0705 2.0129 -0.0428 -0.0172 0.0049  60  ASP L CB  
3494 C CG  . ASP C 60  ? 2.4990 2.3704 2.3195 -0.0420 -0.0199 0.0086  60  ASP L CG  
3495 O OD1 . ASP C 60  ? 2.7165 2.5856 2.5400 -0.0403 -0.0244 0.0117  60  ASP L OD1 
3496 O OD2 . ASP C 60  ? 2.4005 2.2702 2.2199 -0.0432 -0.0177 0.0083  60  ASP L OD2 
3497 N N   . SER C 61  ? 2.3036 2.1826 2.1300 -0.0415 -0.0283 0.0146  61  SER L N   
3498 C CA  . SER C 61  ? 2.2592 2.1424 2.0886 -0.0432 -0.0329 0.0204  61  SER L CA  
3499 C C   . SER C 61  ? 2.2851 2.1752 2.1117 -0.0474 -0.0309 0.0224  61  SER L C   
3500 O O   . SER C 61  ? 2.4069 2.2954 2.2309 -0.0482 -0.0275 0.0208  61  SER L O   
3501 C CB  . SER C 61  ? 2.6815 2.5580 2.5147 -0.0409 -0.0376 0.0238  61  SER L CB  
3502 O OG  . SER C 61  ? 3.3871 3.2592 3.2184 -0.0411 -0.0359 0.0239  61  SER L OG  
3503 N N   . GLY C 62  ? 2.0883 1.9862 1.9157 -0.0503 -0.0331 0.0260  62  GLY L N   
3504 C CA  . GLY C 62  ? 2.0836 1.9894 1.9079 -0.0547 -0.0311 0.0277  62  GLY L CA  
3505 C C   . GLY C 62  ? 2.1502 2.0593 1.9697 -0.0563 -0.0251 0.0221  62  GLY L C   
3506 O O   . GLY C 62  ? 2.0634 1.9756 1.8802 -0.0586 -0.0219 0.0214  62  GLY L O   
3507 N N   . VAL C 63  ? 2.1855 2.0941 2.0042 -0.0550 -0.0235 0.0182  63  VAL L N   
3508 C CA  . VAL C 63  ? 2.1882 2.0996 2.0030 -0.0564 -0.0183 0.0128  63  VAL L CA  
3509 C C   . VAL C 63  ? 2.0078 1.9260 1.8219 -0.0584 -0.0190 0.0128  63  VAL L C   
3510 O O   . VAL C 63  ? 2.0689 1.9859 1.8860 -0.0565 -0.0220 0.0140  63  VAL L O   
3511 C CB  . VAL C 63  ? 2.2292 2.1330 2.0438 -0.0531 -0.0155 0.0078  63  VAL L CB  
3512 C CG1 . VAL C 63  ? 2.1136 2.0206 1.9251 -0.0546 -0.0112 0.0027  63  VAL L CG1 
3513 C CG2 . VAL C 63  ? 2.1470 2.0444 1.9617 -0.0519 -0.0144 0.0076  63  VAL L CG2 
3514 N N   . PRO C 64  ? 2.1353 2.0610 1.9457 -0.0622 -0.0165 0.0115  64  PRO L N   
3515 C CA  . PRO C 64  ? 2.4645 2.3971 2.2741 -0.0645 -0.0176 0.0121  64  PRO L CA  
3516 C C   . PRO C 64  ? 2.5302 2.4599 2.3406 -0.0622 -0.0166 0.0084  64  PRO L C   
3517 O O   . PRO C 64  ? 2.4891 2.4133 2.2988 -0.0599 -0.0135 0.0040  64  PRO L O   
3518 C CB  . PRO C 64  ? 2.4256 2.3655 2.2301 -0.0688 -0.0141 0.0100  64  PRO L CB  
3519 C CG  . PRO C 64  ? 2.4315 2.3704 2.2356 -0.0692 -0.0129 0.0110  64  PRO L CG  
3520 C CD  . PRO C 64  ? 2.1695 2.0982 1.9766 -0.0647 -0.0129 0.0099  64  PRO L CD  
3521 N N   . ASP C 65  ? 2.5466 2.4804 2.3588 -0.0630 -0.0195 0.0106  65  ASP L N   
3522 C CA  . ASP C 65  ? 2.4495 2.3818 2.2630 -0.0610 -0.0189 0.0077  65  ASP L CA  
3523 C C   . ASP C 65  ? 2.3340 2.2677 2.1433 -0.0623 -0.0140 0.0022  65  ASP L C   
3524 O O   . ASP C 65  ? 2.4069 2.3362 2.2166 -0.0599 -0.0119 -0.0015 65  ASP L O   
3525 C CB  . ASP C 65  ? 2.4857 2.4235 2.3020 -0.0623 -0.0228 0.0113  65  ASP L CB  
3526 C CG  . ASP C 65  ? 2.5237 2.4596 2.3457 -0.0606 -0.0281 0.0165  65  ASP L CG  
3527 O OD1 . ASP C 65  ? 2.6477 2.5773 2.4712 -0.0578 -0.0286 0.0167  65  ASP L OD1 
3528 O OD2 . ASP C 65  ? 2.4533 2.3939 2.2785 -0.0621 -0.0321 0.0205  65  ASP L OD2 
3529 N N   . ARG C 66  ? 2.1853 2.1251 1.9905 -0.0664 -0.0124 0.0017  66  ARG L N   
3530 C CA  . ARG C 66  ? 2.1348 2.0763 1.9362 -0.0682 -0.0082 -0.0036 66  ARG L CA  
3531 C C   . ARG C 66  ? 2.1583 2.0925 1.9599 -0.0653 -0.0048 -0.0081 66  ARG L C   
3532 O O   . ARG C 66  ? 1.8459 1.7793 1.6469 -0.0652 -0.0026 -0.0121 66  ARG L O   
3533 C CB  . ARG C 66  ? 2.0268 1.9744 1.8240 -0.0723 -0.0066 -0.0039 66  ARG L CB  
3534 C CG  . ARG C 66  ? 2.1111 2.0673 1.9067 -0.0762 -0.0092 -0.0004 66  ARG L CG  
3535 C CD  . ARG C 66  ? 2.2886 2.2512 2.0792 -0.0803 -0.0065 -0.0024 66  ARG L CD  
3536 N NE  . ARG C 66  ? 2.1000 2.0618 1.8907 -0.0801 -0.0060 -0.0007 66  ARG L NE  
3537 C CZ  . ARG C 66  ? 2.0443 2.0107 1.8354 -0.0822 -0.0091 0.0050  66  ARG L CZ  
3538 N NH1 . ARG C 66  ? 2.1811 2.1535 1.9722 -0.0849 -0.0129 0.0096  66  ARG L NH1 
3539 N NH2 . ARG C 66  ? 1.7143 1.6794 1.5060 -0.0817 -0.0086 0.0066  66  ARG L NH2 
3540 N N   . PHE C 67  ? 2.2241 2.1533 2.0269 -0.0635 -0.0047 -0.0072 67  PHE L N   
3541 C CA  . PHE C 67  ? 2.1149 2.0369 1.9184 -0.0609 -0.0021 -0.0107 67  PHE L CA  
3542 C C   . PHE C 67  ? 2.0423 1.9602 1.8480 -0.0579 -0.0028 -0.0116 67  PHE L C   
3543 O O   . PHE C 67  ? 2.0886 2.0040 1.8971 -0.0555 -0.0057 -0.0088 67  PHE L O   
3544 C CB  . PHE C 67  ? 1.9098 1.8269 1.7146 -0.0593 -0.0027 -0.0086 67  PHE L CB  
3545 C CG  . PHE C 67  ? 1.8343 1.7546 1.6372 -0.0619 -0.0008 -0.0089 67  PHE L CG  
3546 C CD1 . PHE C 67  ? 1.7549 1.6824 1.5564 -0.0648 -0.0024 -0.0055 67  PHE L CD1 
3547 C CD2 . PHE C 67  ? 2.0133 1.9300 1.8160 -0.0616 0.0025  -0.0126 67  PHE L CD2 
3548 C CE1 . PHE C 67  ? 2.1192 2.0505 1.9188 -0.0673 -0.0003 -0.0060 67  PHE L CE1 
3549 C CE2 . PHE C 67  ? 2.0126 1.9328 1.8141 -0.0638 0.0046  -0.0133 67  PHE L CE2 
3550 C CZ  . PHE C 67  ? 2.1291 2.0568 1.9288 -0.0666 0.0034  -0.0101 67  PHE L CZ  
3551 N N   . SER C 68  ? 2.0113 1.9288 1.8161 -0.0582 -0.0003 -0.0156 68  SER L N   
3552 C CA  . SER C 68  ? 1.9775 1.8923 1.7842 -0.0557 -0.0005 -0.0167 68  SER L CA  
3553 C C   . SER C 68  ? 1.9301 1.8391 1.7368 -0.0546 0.0022  -0.0201 68  SER L C   
3554 O O   . SER C 68  ? 1.9672 1.8766 1.7724 -0.0566 0.0046  -0.0230 68  SER L O   
3555 C CB  . SER C 68  ? 1.9097 1.8303 1.7161 -0.0575 -0.0006 -0.0175 68  SER L CB  
3556 O OG  . SER C 68  ? 2.0974 2.0200 1.9012 -0.0602 0.0021  -0.0211 68  SER L OG  
3557 N N   . GLY C 69  ? 1.5520 1.4558 1.3605 -0.0515 0.0015  -0.0197 69  GLY L N   
3558 C CA  . GLY C 69  ? 1.7776 1.6759 1.5860 -0.0507 0.0036  -0.0223 69  GLY L CA  
3559 C C   . GLY C 69  ? 1.8919 1.7904 1.7012 -0.0496 0.0041  -0.0238 69  GLY L C   
3560 O O   . GLY C 69  ? 1.8514 1.7497 1.6621 -0.0472 0.0025  -0.0224 69  GLY L O   
3561 N N   . SER C 70  ? 1.8479 1.7471 1.6567 -0.0513 0.0062  -0.0266 70  SER L N   
3562 C CA  . SER C 70  ? 1.8744 1.7743 1.6840 -0.0507 0.0067  -0.0277 70  SER L CA  
3563 C C   . SER C 70  ? 2.0038 1.8978 1.8138 -0.0492 0.0074  -0.0283 70  SER L C   
3564 O O   . SER C 70  ? 2.1308 2.0198 1.9406 -0.0484 0.0072  -0.0277 70  SER L O   
3565 C CB  . SER C 70  ? 1.7888 1.6923 1.5982 -0.0535 0.0081  -0.0300 70  SER L CB  
3566 O OG  . SER C 70  ? 1.8400 1.7401 1.6493 -0.0550 0.0096  -0.0321 70  SER L OG  
3567 N N   . GLY C 71  ? 1.9077 1.8025 1.7183 -0.0491 0.0082  -0.0294 71  GLY L N   
3568 C CA  . GLY C 71  ? 1.7269 1.6166 1.5374 -0.0482 0.0087  -0.0297 71  GLY L CA  
3569 C C   . GLY C 71  ? 1.8704 1.7618 1.6813 -0.0477 0.0093  -0.0303 71  GLY L C   
3570 O O   . GLY C 71  ? 2.0175 1.9121 1.8289 -0.0458 0.0088  -0.0298 71  GLY L O   
3571 N N   . SER C 72  ? 1.7429 1.6322 1.5540 -0.0496 0.0103  -0.0312 72  SER L N   
3572 C CA  . SER C 72  ? 1.7521 1.6424 1.5632 -0.0496 0.0109  -0.0313 72  SER L CA  
3573 C C   . SER C 72  ? 1.6867 1.5731 1.4982 -0.0519 0.0113  -0.0316 72  SER L C   
3574 O O   . SER C 72  ? 1.7974 1.6841 1.6104 -0.0546 0.0115  -0.0324 72  SER L O   
3575 C CB  . SER C 72  ? 1.9697 1.8670 1.7820 -0.0505 0.0113  -0.0316 72  SER L CB  
3576 O OG  . SER C 72  ? 2.1120 2.0110 1.9252 -0.0532 0.0114  -0.0324 72  SER L OG  
3577 N N   . GLY C 73  ? 1.8029 1.6855 1.6132 -0.0511 0.0111  -0.0310 73  GLY L N   
3578 C CA  . GLY C 73  ? 1.7389 1.6185 1.5498 -0.0536 0.0112  -0.0306 73  GLY L CA  
3579 C C   . GLY C 73  ? 1.6296 1.5032 1.4419 -0.0551 0.0107  -0.0306 73  GLY L C   
3580 O O   . GLY C 73  ? 1.6264 1.4948 1.4378 -0.0539 0.0101  -0.0298 73  GLY L O   
3581 N N   . THR C 74  ? 1.4883 1.3626 1.3033 -0.0577 0.0108  -0.0314 74  THR L N   
3582 C CA  . THR C 74  ? 1.5441 1.4133 1.3617 -0.0592 0.0105  -0.0319 74  THR L CA  
3583 C C   . THR C 74  ? 1.5856 1.4563 1.4045 -0.0594 0.0111  -0.0338 74  THR L C   
3584 O O   . THR C 74  ? 1.5691 1.4359 1.3895 -0.0595 0.0112  -0.0343 74  THR L O   
3585 C CB  . THR C 74  ? 1.3731 1.2409 1.1939 -0.0624 0.0099  -0.0316 74  THR L CB  
3586 O OG1 . THR C 74  ? 1.3284 1.2016 1.1507 -0.0641 0.0100  -0.0326 74  THR L OG1 
3587 C CG2 . THR C 74  ? 1.5171 1.3834 1.3364 -0.0628 0.0092  -0.0294 74  THR L CG2 
3588 N N   . ASP C 75  ? 1.7102 1.5867 1.5285 -0.0595 0.0115  -0.0348 75  ASP L N   
3589 C CA  . ASP C 75  ? 1.6980 1.5768 1.5169 -0.0602 0.0121  -0.0368 75  ASP L CA  
3590 C C   . ASP C 75  ? 1.5618 1.4439 1.3778 -0.0580 0.0122  -0.0361 75  ASP L C   
3591 O O   . ASP C 75  ? 1.5686 1.4546 1.3832 -0.0571 0.0119  -0.0351 75  ASP L O   
3592 C CB  . ASP C 75  ? 1.8407 1.7235 1.6615 -0.0626 0.0121  -0.0385 75  ASP L CB  
3593 C CG  . ASP C 75  ? 1.8397 1.7191 1.6646 -0.0650 0.0115  -0.0393 75  ASP L CG  
3594 O OD1 . ASP C 75  ? 2.0478 1.9218 1.8743 -0.0649 0.0114  -0.0390 75  ASP L OD1 
3595 O OD2 . ASP C 75  ? 1.7515 1.6335 1.5785 -0.0671 0.0109  -0.0401 75  ASP L OD2 
3596 N N   . PHE C 76  ? 1.5683 1.4489 1.3837 -0.0574 0.0124  -0.0363 76  PHE L N   
3597 C CA  . PHE C 76  ? 1.6750 1.5579 1.4882 -0.0556 0.0119  -0.0348 76  PHE L CA  
3598 C C   . PHE C 76  ? 1.6623 1.5482 1.4752 -0.0570 0.0125  -0.0363 76  PHE L C   
3599 O O   . PHE C 76  ? 1.7044 1.5889 1.5190 -0.0586 0.0135  -0.0385 76  PHE L O   
3600 C CB  . PHE C 76  ? 1.5762 1.4538 1.3888 -0.0535 0.0112  -0.0328 76  PHE L CB  
3601 C CG  . PHE C 76  ? 1.6711 1.5459 1.4833 -0.0522 0.0106  -0.0317 76  PHE L CG  
3602 C CD1 . PHE C 76  ? 1.7066 1.5838 1.5174 -0.0501 0.0099  -0.0306 76  PHE L CD1 
3603 C CD2 . PHE C 76  ? 1.7214 1.5913 1.5348 -0.0531 0.0107  -0.0317 76  PHE L CD2 
3604 C CE1 . PHE C 76  ? 2.0372 1.9123 1.8473 -0.0488 0.0096  -0.0301 76  PHE L CE1 
3605 C CE2 . PHE C 76  ? 1.7801 1.6479 1.5925 -0.0522 0.0102  -0.0307 76  PHE L CE2 
3606 C CZ  . PHE C 76  ? 2.0387 1.9093 1.8491 -0.0500 0.0098  -0.0301 76  PHE L CZ  
3607 N N   . THR C 77  ? 1.7154 1.6059 1.5265 -0.0565 0.0119  -0.0352 77  THR L N   
3608 C CA  . THR C 77  ? 1.9779 1.8723 1.7880 -0.0582 0.0125  -0.0365 77  THR L CA  
3609 C C   . THR C 77  ? 2.1100 2.0064 1.9184 -0.0572 0.0114  -0.0337 77  THR L C   
3610 O O   . THR C 77  ? 1.9772 1.8722 1.7855 -0.0549 0.0098  -0.0310 77  THR L O   
3611 C CB  . THR C 77  ? 2.3679 2.2679 2.1774 -0.0603 0.0127  -0.0383 77  THR L CB  
3612 O OG1 . THR C 77  ? 2.4940 2.3974 2.3028 -0.0593 0.0114  -0.0361 77  THR L OG1 
3613 C CG2 . THR C 77  ? 2.2083 2.1065 2.0202 -0.0618 0.0135  -0.0410 77  THR L CG2 
3614 N N   . LEU C 78  ? 2.3325 2.2323 2.1398 -0.0589 0.0120  -0.0345 78  LEU L N   
3615 C CA  . LEU C 78  ? 2.1345 2.0370 1.9403 -0.0587 0.0108  -0.0316 78  LEU L CA  
3616 C C   . LEU C 78  ? 2.2347 2.1444 2.0383 -0.0616 0.0112  -0.0328 78  LEU L C   
3617 O O   . LEU C 78  ? 2.2051 2.1162 2.0084 -0.0634 0.0132  -0.0359 78  LEU L O   
3618 C CB  . LEU C 78  ? 2.1953 2.0939 2.0019 -0.0581 0.0113  -0.0309 78  LEU L CB  
3619 C CG  . LEU C 78  ? 2.1268 2.0286 1.9322 -0.0583 0.0100  -0.0277 78  LEU L CG  
3620 C CD1 . LEU C 78  ? 2.2410 2.1403 2.0470 -0.0558 0.0071  -0.0235 78  LEU L CD1 
3621 C CD2 . LEU C 78  ? 2.1660 2.0661 1.9722 -0.0589 0.0115  -0.0282 78  LEU L CD2 
3622 N N   . LYS C 79  ? 2.4097 2.3241 2.2122 -0.0619 0.0094  -0.0306 79  LYS L N   
3623 C CA  . LYS C 79  ? 2.5179 2.4394 2.3179 -0.0650 0.0094  -0.0313 79  LYS L CA  
3624 C C   . LYS C 79  ? 2.3134 2.2388 2.1121 -0.0656 0.0074  -0.0272 79  LYS L C   
3625 O O   . LYS C 79  ? 2.0911 2.0153 1.8913 -0.0636 0.0049  -0.0234 79  LYS L O   
3626 C CB  . LYS C 79  ? 2.4581 2.3827 2.2582 -0.0656 0.0085  -0.0316 79  LYS L CB  
3627 C CG  . LYS C 79  ? 2.4730 2.3929 2.2754 -0.0637 0.0091  -0.0330 79  LYS L CG  
3628 C CD  . LYS C 79  ? 2.2187 2.1423 2.0213 -0.0650 0.0086  -0.0339 79  LYS L CD  
3629 C CE  . LYS C 79  ? 1.9414 1.8611 1.7464 -0.0634 0.0091  -0.0347 79  LYS L CE  
3630 N NZ  . LYS C 79  ? 2.3646 2.2798 2.1706 -0.0639 0.0110  -0.0379 79  LYS L NZ  
3631 N N   . ILE C 80  ? 2.1892 2.1195 1.9855 -0.0684 0.0085  -0.0281 80  ILE L N   
3632 C CA  . ILE C 80  ? 2.1278 2.0627 1.9227 -0.0697 0.0065  -0.0240 80  ILE L CA  
3633 C C   . ILE C 80  ? 2.3256 2.2687 2.1173 -0.0734 0.0059  -0.0241 80  ILE L C   
3634 O O   . ILE C 80  ? 2.4539 2.4008 2.2430 -0.0760 0.0083  -0.0280 80  ILE L O   
3635 C CB  . ILE C 80  ? 2.1250 2.0596 1.9195 -0.0701 0.0081  -0.0241 80  ILE L CB  
3636 C CG1 . ILE C 80  ? 2.2494 2.1754 2.0471 -0.0668 0.0088  -0.0245 80  ILE L CG1 
3637 C CG2 . ILE C 80  ? 2.0839 2.0231 1.8776 -0.0714 0.0055  -0.0187 80  ILE L CG2 
3638 C CD1 . ILE C 80  ? 2.4067 2.3316 2.2047 -0.0673 0.0117  -0.0271 80  ILE L CD1 
3639 N N   . THR C 81  ? 2.3541 2.3002 2.1464 -0.0736 0.0026  -0.0199 81  THR L N   
3640 C CA  . THR C 81  ? 2.2482 2.2023 2.0376 -0.0775 0.0013  -0.0188 81  THR L CA  
3641 C C   . THR C 81  ? 2.2858 2.2458 2.0722 -0.0806 0.0013  -0.0170 81  THR L C   
3642 O O   . THR C 81  ? 2.4007 2.3583 2.1875 -0.0795 0.0027  -0.0171 81  THR L O   
3643 C CB  . THR C 81  ? 2.2595 2.2150 2.0514 -0.0768 -0.0025 -0.0144 81  THR L CB  
3644 O OG1 . THR C 81  ? 2.3424 2.2959 2.1374 -0.0748 -0.0053 -0.0094 81  THR L OG1 
3645 C CG2 . THR C 81  ? 2.2830 2.2340 2.0776 -0.0741 -0.0020 -0.0165 81  THR L CG2 
3646 N N   . THR C 82  ? 2.0764 2.0443 1.8600 -0.0845 -0.0005 -0.0148 82  THR L N   
3647 C CA  . THR C 82  ? 2.2747 2.2504 2.0536 -0.0888 0.0007  -0.0154 82  THR L CA  
3648 C C   . THR C 82  ? 2.3396 2.3136 2.1183 -0.0879 0.0034  -0.0168 82  THR L C   
3649 O O   . THR C 82  ? 2.2466 2.2218 2.0263 -0.0880 0.0015  -0.0119 82  THR L O   
3650 C CB  . THR C 82  ? 2.4246 2.4075 2.2023 -0.0921 -0.0034 -0.0089 82  THR L CB  
3651 O OG1 . THR C 82  ? 2.2737 2.2546 2.0547 -0.0904 -0.0058 -0.0035 82  THR L OG1 
3652 C CG2 . THR C 82  ? 2.2789 2.2624 2.0586 -0.0922 -0.0067 -0.0065 82  THR L CG2 
3653 N N   . VAL C 83  ? 2.1711 2.1422 1.9495 -0.0870 0.0074  -0.0232 83  VAL L N   
3654 C CA  . VAL C 83  ? 2.0663 2.0355 1.8453 -0.0860 0.0104  -0.0254 83  VAL L CA  
3655 C C   . VAL C 83  ? 2.0984 2.0764 1.8740 -0.0897 0.0105  -0.0230 83  VAL L C   
3656 O O   . VAL C 83  ? 2.2777 2.2638 2.0488 -0.0937 0.0114  -0.0250 83  VAL L O   
3657 C CB  . VAL C 83  ? 1.9650 1.9315 1.7441 -0.0855 0.0145  -0.0331 83  VAL L CB  
3658 C CG1 . VAL C 83  ? 2.0473 2.0125 1.8278 -0.0847 0.0176  -0.0354 83  VAL L CG1 
3659 C CG2 . VAL C 83  ? 2.0691 2.0274 1.8517 -0.0823 0.0141  -0.0348 83  VAL L CG2 
3660 N N   . GLU C 84  ? 2.0678 2.0447 1.8454 -0.0886 0.0095  -0.0187 84  GLU L N   
3661 C CA  . GLU C 84  ? 2.1324 2.1179 1.9074 -0.0921 0.0093  -0.0155 84  GLU L CA  
3662 C C   . GLU C 84  ? 2.2949 2.2799 2.0708 -0.0913 0.0133  -0.0187 84  GLU L C   
3663 O O   . GLU C 84  ? 2.4662 2.4436 2.2451 -0.0880 0.0158  -0.0231 84  GLU L O   
3664 C CB  . GLU C 84  ? 2.1957 2.1814 1.9730 -0.0920 0.0043  -0.0069 84  GLU L CB  
3665 C CG  . GLU C 84  ? 2.1031 2.0911 1.8801 -0.0934 0.0000  -0.0030 84  GLU L CG  
3666 C CD  . GLU C 84  ? 2.1954 2.1828 1.9759 -0.0929 -0.0053 0.0053  84  GLU L CD  
3667 O OE1 . GLU C 84  ? 2.2834 2.2671 2.0667 -0.0909 -0.0058 0.0078  84  GLU L OE1 
3668 O OE2 . GLU C 84  ? 2.3029 2.2936 2.0838 -0.0946 -0.0093 0.0094  84  GLU L OE2 
3669 N N   . ALA C 85  ? 2.1033 2.0969 1.8767 -0.0945 0.0138  -0.0163 85  ALA L N   
3670 C CA  . ALA C 85  ? 1.8616 1.8560 1.6363 -0.0940 0.0175  -0.0189 85  ALA L CA  
3671 C C   . ALA C 85  ? 1.7862 1.7712 1.5665 -0.0898 0.0162  -0.0156 85  ALA L C   
3672 O O   . ALA C 85  ? 1.9232 1.9036 1.7064 -0.0875 0.0194  -0.0195 85  ALA L O   
3673 C CB  . ALA C 85  ? 2.0046 2.0112 1.7755 -0.0986 0.0179  -0.0159 85  ALA L CB  
3674 N N   . GLU C 86  ? 2.1365 2.1184 1.9187 -0.0888 0.0113  -0.0085 86  GLU L N   
3675 C CA  . GLU C 86  ? 2.2901 2.2623 2.0773 -0.0847 0.0096  -0.0055 86  GLU L CA  
3676 C C   . GLU C 86  ? 2.2377 2.1998 2.0276 -0.0807 0.0114  -0.0106 86  GLU L C   
3677 O O   . GLU C 86  ? 1.7590 1.7139 1.5524 -0.0778 0.0122  -0.0111 86  GLU L O   
3678 C CB  . GLU C 86  ? 2.3093 2.2800 2.0984 -0.0842 0.0037  0.0023  86  GLU L CB  
3679 C CG  . GLU C 86  ? 2.3310 2.3108 2.1189 -0.0880 0.0011  0.0088  86  GLU L CG  
3680 C CD  . GLU C 86  ? 2.3650 2.3428 2.1557 -0.0875 -0.0053 0.0163  86  GLU L CD  
3681 O OE1 . GLU C 86  ? 2.2559 2.2264 2.0488 -0.0844 -0.0072 0.0156  86  GLU L OE1 
3682 O OE2 . GLU C 86  ? 2.4065 2.3901 2.1976 -0.0902 -0.0085 0.0228  86  GLU L OE2 
3683 N N   . ASP C 87  ? 2.0623 2.0239 1.8504 -0.0808 0.0117  -0.0142 87  ASP L N   
3684 C CA  . ASP C 87  ? 1.9576 1.9102 1.7483 -0.0775 0.0127  -0.0182 87  ASP L CA  
3685 C C   . ASP C 87  ? 1.9491 1.9012 1.7400 -0.0776 0.0174  -0.0255 87  ASP L C   
3686 O O   . ASP C 87  ? 2.1421 2.0941 1.9320 -0.0780 0.0189  -0.0304 87  ASP L O   
3687 C CB  . ASP C 87  ? 2.1572 2.1096 1.9467 -0.0775 0.0105  -0.0180 87  ASP L CB  
3688 C CG  . ASP C 87  ? 2.1089 2.0597 1.9001 -0.0764 0.0056  -0.0113 87  ASP L CG  
3689 O OD1 . ASP C 87  ? 2.2681 2.2158 2.0617 -0.0749 0.0039  -0.0072 87  ASP L OD1 
3690 O OD2 . ASP C 87  ? 2.0983 2.0508 1.8888 -0.0769 0.0034  -0.0101 87  ASP L OD2 
3691 N N   . VAL C 88  ? 2.0841 2.0361 1.8768 -0.0773 0.0196  -0.0261 88  VAL L N   
3692 C CA  . VAL C 88  ? 2.0972 2.0495 1.8913 -0.0774 0.0240  -0.0328 88  VAL L CA  
3693 C C   . VAL C 88  ? 1.8890 1.8339 1.6882 -0.0745 0.0248  -0.0322 88  VAL L C   
3694 O O   . VAL C 88  ? 1.9156 1.8593 1.7160 -0.0738 0.0228  -0.0266 88  VAL L O   
3695 C CB  . VAL C 88  ? 2.0714 2.0350 1.8620 -0.0811 0.0268  -0.0352 88  VAL L CB  
3696 C CG1 . VAL C 88  ? 1.9242 1.8878 1.7174 -0.0808 0.0314  -0.0425 88  VAL L CG1 
3697 C CG2 . VAL C 88  ? 2.1088 2.0793 1.8941 -0.0843 0.0260  -0.0363 88  VAL L CG2 
3698 N N   . GLY C 89  ? 1.7462 1.6859 1.5487 -0.0731 0.0273  -0.0378 89  GLY L N   
3699 C CA  . GLY C 89  ? 1.6619 1.5948 1.4697 -0.0707 0.0282  -0.0377 89  GLY L CA  
3700 C C   . GLY C 89  ? 1.8618 1.7853 1.6733 -0.0684 0.0282  -0.0408 89  GLY L C   
3701 O O   . GLY C 89  ? 1.9519 1.8756 1.7629 -0.0690 0.0292  -0.0455 89  GLY L O   
3702 N N   . VAL C 90  ? 1.7891 1.7046 1.6044 -0.0660 0.0269  -0.0378 90  VAL L N   
3703 C CA  . VAL C 90  ? 1.7419 1.6483 1.5611 -0.0641 0.0267  -0.0398 90  VAL L CA  
3704 C C   . VAL C 90  ? 1.7155 1.6160 1.5333 -0.0623 0.0230  -0.0351 90  VAL L C   
3705 O O   . VAL C 90  ? 1.7249 1.6256 1.5410 -0.0618 0.0207  -0.0299 90  VAL L O   
3706 C CB  . VAL C 90  ? 1.9763 1.8782 1.8013 -0.0630 0.0281  -0.0403 90  VAL L CB  
3707 C CG1 . VAL C 90  ? 1.6319 1.5243 1.4610 -0.0614 0.0272  -0.0413 90  VAL L CG1 
3708 C CG2 . VAL C 90  ? 2.1019 2.0101 1.9291 -0.0645 0.0320  -0.0456 90  VAL L CG2 
3709 N N   . TYR C 91  ? 1.8568 1.7522 1.6756 -0.0615 0.0225  -0.0372 91  TYR L N   
3710 C CA  . TYR C 91  ? 1.8982 1.7884 1.7157 -0.0597 0.0196  -0.0338 91  TYR L CA  
3711 C C   . TYR C 91  ? 1.8052 1.6866 1.6265 -0.0583 0.0193  -0.0343 91  TYR L C   
3712 O O   . TYR C 91  ? 1.9394 1.8190 1.7647 -0.0588 0.0212  -0.0376 91  TYR L O   
3713 C CB  . TYR C 91  ? 1.7440 1.6377 1.5583 -0.0605 0.0190  -0.0351 91  TYR L CB  
3714 C CG  . TYR C 91  ? 1.9263 1.8281 1.7366 -0.0620 0.0184  -0.0333 91  TYR L CG  
3715 C CD1 . TYR C 91  ? 1.8920 1.8012 1.7010 -0.0645 0.0207  -0.0364 91  TYR L CD1 
3716 C CD2 . TYR C 91  ? 2.0632 1.9655 1.8715 -0.0611 0.0154  -0.0286 91  TYR L CD2 
3717 C CE1 . TYR C 91  ? 1.9327 1.8497 1.7378 -0.0664 0.0199  -0.0344 91  TYR L CE1 
3718 C CE2 . TYR C 91  ? 2.1711 2.0808 1.9764 -0.0629 0.0143  -0.0265 91  TYR L CE2 
3719 C CZ  . TYR C 91  ? 2.0543 1.9714 1.8577 -0.0657 0.0166  -0.0292 91  TYR L CZ  
3720 O OH  . TYR C 91  ? 2.0466 1.9715 1.8467 -0.0679 0.0153  -0.0267 91  TYR L OH  
3721 N N   . TYR C 92  ? 1.6591 1.5354 1.4795 -0.0566 0.0168  -0.0311 92  TYR L N   
3722 C CA  . TYR C 92  ? 1.7637 1.6320 1.5871 -0.0555 0.0161  -0.0308 92  TYR L CA  
3723 C C   . TYR C 92  ? 1.5995 1.4645 1.4207 -0.0543 0.0140  -0.0292 92  TYR L C   
3724 O O   . TYR C 92  ? 1.5261 1.3930 1.3443 -0.0533 0.0123  -0.0267 92  TYR L O   
3725 C CB  . TYR C 92  ? 1.9792 1.8430 1.8047 -0.0546 0.0152  -0.0275 92  TYR L CB  
3726 C CG  . TYR C 92  ? 2.0861 1.9502 1.9161 -0.0556 0.0175  -0.0298 92  TYR L CG  
3727 C CD1 . TYR C 92  ? 1.9770 1.8461 1.8073 -0.0561 0.0187  -0.0290 92  TYR L CD1 
3728 C CD2 . TYR C 92  ? 2.0702 1.9303 1.9047 -0.0561 0.0185  -0.0328 92  TYR L CD2 
3729 C CE1 . TYR C 92  ? 1.9882 1.8582 1.8231 -0.0569 0.0211  -0.0315 92  TYR L CE1 
3730 C CE2 . TYR C 92  ? 1.9951 1.8554 1.8347 -0.0568 0.0206  -0.0352 92  TYR L CE2 
3731 C CZ  . TYR C 92  ? 1.9422 1.8077 1.7821 -0.0570 0.0221  -0.0347 92  TYR L CZ  
3732 O OH  . TYR C 92  ? 1.8081 1.6744 1.6536 -0.0576 0.0244  -0.0375 92  TYR L OH  
3733 N N   . CYS C 93  ? 1.3495 1.2096 1.1729 -0.0544 0.0140  -0.0306 93  CYS L N   
3734 C CA  . CYS C 93  ? 1.5864 1.4443 1.4082 -0.0538 0.0128  -0.0302 93  CYS L CA  
3735 C C   . CYS C 93  ? 1.9923 1.8439 1.8134 -0.0521 0.0107  -0.0269 93  CYS L C   
3736 O O   . CYS C 93  ? 2.3014 2.1495 2.1229 -0.0523 0.0101  -0.0271 93  CYS L O   
3737 C CB  . CYS C 93  ? 1.9054 1.7620 1.7300 -0.0554 0.0137  -0.0332 93  CYS L CB  
3738 S SG  . CYS C 93  ? 2.2879 2.1509 2.1132 -0.0575 0.0155  -0.0376 93  CYS L SG  
3739 N N   . MET C 94  ? 1.7815 1.6316 1.6016 -0.0507 0.0092  -0.0239 94  MET L N   
3740 C CA  . MET C 94  ? 1.9729 1.8171 1.7917 -0.0490 0.0070  -0.0213 94  MET L CA  
3741 C C   . MET C 94  ? 2.1131 1.9506 1.9344 -0.0497 0.0067  -0.0210 94  MET L C   
3742 O O   . MET C 94  ? 2.1845 2.0200 2.0091 -0.0505 0.0073  -0.0208 94  MET L O   
3743 C CB  . MET C 94  ? 1.9058 1.7523 1.7217 -0.0479 0.0062  -0.0217 94  MET L CB  
3744 C CG  . MET C 94  ? 2.1828 2.0332 1.9971 -0.0467 0.0052  -0.0203 94  MET L CG  
3745 S SD  . MET C 94  ? 3.0451 2.8888 2.8599 -0.0450 0.0026  -0.0166 94  MET L SD  
3746 C CE  . MET C 94  ? 2.3993 2.2379 2.2122 -0.0434 0.0012  -0.0168 94  MET L CE  
3747 N N   . GLN C 95  ? 2.2063 2.0407 2.0261 -0.0494 0.0058  -0.0209 95  GLN L N   
3748 C CA  . GLN C 95  ? 2.2569 2.0844 2.0774 -0.0497 0.0044  -0.0193 95  GLN L CA  
3749 C C   . GLN C 95  ? 1.8241 1.6518 1.6419 -0.0498 0.0041  -0.0201 95  GLN L C   
3750 O O   . GLN C 95  ? 1.5006 1.3308 1.3152 -0.0480 0.0035  -0.0201 95  GLN L O   
3751 C CB  . GLN C 95  ? 2.4065 2.2295 2.2257 -0.0479 0.0022  -0.0162 95  GLN L CB  
3752 C CG  . GLN C 95  ? 2.3183 2.1411 2.1401 -0.0478 0.0022  -0.0147 95  GLN L CG  
3753 C CD  . GLN C 95  ? 2.4564 2.2749 2.2768 -0.0461 -0.0005 -0.0114 95  GLN L CD  
3754 O OE1 . GLN C 95  ? 2.4608 2.2784 2.2780 -0.0444 -0.0022 -0.0110 95  GLN L OE1 
3755 N NE2 . GLN C 95  ? 2.6139 2.4296 2.4371 -0.0464 -0.0011 -0.0092 95  GLN L NE2 
3756 N N   . GLY C 96  ? 1.6690 1.4945 1.4884 -0.0518 0.0042  -0.0205 96  GLY L N   
3757 C CA  . GLY C 96  ? 1.9275 1.7536 1.7441 -0.0521 0.0038  -0.0207 96  GLY L CA  
3758 C C   . GLY C 96  ? 1.9354 1.7576 1.7483 -0.0502 0.0019  -0.0190 96  GLY L C   
3759 O O   . GLY C 96  ? 1.5193 1.3362 1.3329 -0.0497 0.0005  -0.0170 96  GLY L O   
3760 N N   . THR C 97  ? 1.9269 1.7519 1.7363 -0.0489 0.0019  -0.0198 97  THR L N   
3761 C CA  . THR C 97  ? 1.4429 1.2641 1.2489 -0.0475 0.0002  -0.0189 97  THR L CA  
3762 C C   . THR C 97  ? 1.8159 1.6313 1.6221 -0.0498 -0.0010 -0.0172 97  THR L C   
3763 O O   . THR C 97  ? 2.0907 1.9010 1.8946 -0.0490 -0.0028 -0.0159 97  THR L O   
3764 C CB  . THR C 97  ? 1.4637 1.2897 1.2665 -0.0462 0.0009  -0.0207 97  THR L CB  
3765 O OG1 . THR C 97  ? 1.8595 1.6893 1.6630 -0.0489 0.0024  -0.0216 97  THR L OG1 
3766 C CG2 . THR C 97  ? 1.5934 1.4244 1.3965 -0.0437 0.0014  -0.0218 97  THR L CG2 
3767 N N   . HIS C 98  ? 1.7974 1.6134 1.6066 -0.0528 -0.0002 -0.0172 98  HIS L N   
3768 C CA  . HIS C 98  ? 2.0488 1.8592 1.8597 -0.0556 -0.0016 -0.0151 98  HIS L CA  
3769 C C   . HIS C 98  ? 2.1017 1.9067 1.9159 -0.0552 -0.0026 -0.0133 98  HIS L C   
3770 O O   . HIS C 98  ? 1.8881 1.6950 1.7052 -0.0543 -0.0015 -0.0141 98  HIS L O   
3771 C CB  . HIS C 98  ? 1.9779 1.7910 1.7923 -0.0588 -0.0007 -0.0156 98  HIS L CB  
3772 C CG  . HIS C 98  ? 2.1415 1.9497 1.9587 -0.0621 -0.0025 -0.0132 98  HIS L CG  
3773 N ND1 . HIS C 98  ? 1.9497 1.7559 1.7736 -0.0642 -0.0027 -0.0128 98  HIS L ND1 
3774 C CD2 . HIS C 98  ? 1.9805 1.7855 1.7950 -0.0639 -0.0042 -0.0112 98  HIS L CD2 
3775 C CE1 . HIS C 98  ? 1.7327 1.5344 1.5584 -0.0671 -0.0047 -0.0102 98  HIS L CE1 
3776 N NE2 . HIS C 98  ? 1.6317 1.4327 1.4514 -0.0672 -0.0057 -0.0090 98  HIS L NE2 
3777 N N   . TRP C 99  ? 2.1681 1.9667 1.9818 -0.0561 -0.0047 -0.0109 99  TRP L N   
3778 C CA  . TRP C 99  ? 2.0899 1.8831 1.9057 -0.0552 -0.0061 -0.0088 99  TRP L CA  
3779 C C   . TRP C 99  ? 1.9972 1.7903 1.8197 -0.0562 -0.0051 -0.0086 99  TRP L C   
3780 O O   . TRP C 99  ? 2.0876 1.8797 1.9117 -0.0546 -0.0052 -0.0078 99  TRP L O   
3781 C CB  . TRP C 99  ? 2.3180 2.1043 2.1320 -0.0564 -0.0088 -0.0061 99  TRP L CB  
3782 C CG  . TRP C 99  ? 2.5480 2.3332 2.3561 -0.0539 -0.0101 -0.0063 99  TRP L CG  
3783 C CD1 . TRP C 99  ? 2.7358 2.5164 2.5428 -0.0517 -0.0121 -0.0048 99  TRP L CD1 
3784 C CD2 . TRP C 99  ? 2.6777 2.4670 2.4806 -0.0529 -0.0093 -0.0087 99  TRP L CD2 
3785 N NE1 . TRP C 99  ? 2.8136 2.5946 2.6152 -0.0495 -0.0129 -0.0062 99  TRP L NE1 
3786 C CE2 . TRP C 99  ? 2.7274 2.5139 2.5265 -0.0500 -0.0110 -0.0088 99  TRP L CE2 
3787 C CE3 . TRP C 99  ? 2.5494 2.3445 2.3510 -0.0541 -0.0075 -0.0106 99  TRP L CE3 
3788 C CZ2 . TRP C 99  ? 2.6542 2.4437 2.4485 -0.0483 -0.0107 -0.0112 99  TRP L CZ2 
3789 C CZ3 . TRP C 99  ? 2.5272 2.3256 2.3238 -0.0525 -0.0071 -0.0127 99  TRP L CZ3 
3790 C CH2 . TRP C 99  ? 2.5596 2.3553 2.3527 -0.0495 -0.0086 -0.0132 99  TRP L CH2 
3791 N N   . PRO C 100 ? 1.7854 1.5797 1.6124 -0.0589 -0.0043 -0.0093 100 PRO L N   
3792 C CA  . PRO C 100 ? 1.5390 1.3354 1.3720 -0.0591 -0.0026 -0.0108 100 PRO L CA  
3793 C C   . PRO C 100 ? 1.6703 1.4729 1.5012 -0.0567 -0.0005 -0.0132 100 PRO L C   
3794 O O   . PRO C 100 ? 1.7035 1.5116 1.5333 -0.0569 0.0010  -0.0157 100 PRO L O   
3795 C CB  . PRO C 100 ? 1.6471 1.4448 1.4843 -0.0621 -0.0023 -0.0119 100 PRO L CB  
3796 C CG  . PRO C 100 ? 1.6508 1.4442 1.4861 -0.0642 -0.0047 -0.0092 100 PRO L CG  
3797 C CD  . PRO C 100 ? 1.7791 1.5723 1.6066 -0.0620 -0.0053 -0.0086 100 PRO L CD  
3798 N N   . TYR C 101 ? 1.7478 1.5497 1.5783 -0.0547 -0.0007 -0.0121 101 TYR L N   
3799 C CA  . TYR C 101 ? 1.7759 1.5836 1.6044 -0.0528 0.0008  -0.0136 101 TYR L CA  
3800 C C   . TYR C 101 ? 2.0152 1.8275 1.8481 -0.0538 0.0032  -0.0162 101 TYR L C   
3801 O O   . TYR C 101 ? 2.1341 1.9447 1.9719 -0.0544 0.0037  -0.0159 101 TYR L O   
3802 C CB  . TYR C 101 ? 1.6468 1.4524 1.4742 -0.0508 -0.0006 -0.0110 101 TYR L CB  
3803 C CG  . TYR C 101 ? 1.6544 1.4564 1.4771 -0.0491 -0.0032 -0.0091 101 TYR L CG  
3804 C CD1 . TYR C 101 ? 1.7291 1.5347 1.5477 -0.0471 -0.0034 -0.0100 101 TYR L CD1 
3805 C CD2 . TYR C 101 ? 1.8117 1.6065 1.6343 -0.0494 -0.0056 -0.0064 101 TYR L CD2 
3806 C CE1 . TYR C 101 ? 1.8022 1.6044 1.6170 -0.0452 -0.0058 -0.0088 101 TYR L CE1 
3807 C CE2 . TYR C 101 ? 1.8777 1.6689 1.6959 -0.0478 -0.0080 -0.0051 101 TYR L CE2 
3808 C CZ  . TYR C 101 ? 1.8011 1.5962 1.6156 -0.0456 -0.0080 -0.0066 101 TYR L CZ  
3809 O OH  . TYR C 101 ? 1.7949 1.5865 1.6057 -0.0437 -0.0105 -0.0059 101 TYR L OH  
3810 N N   . THR C 102 ? 1.9504 1.7685 1.7820 -0.0541 0.0048  -0.0191 102 THR L N   
3811 C CA  . THR C 102 ? 2.0332 1.8552 1.8690 -0.0555 0.0070  -0.0222 102 THR L CA  
3812 C C   . THR C 102 ? 1.9903 1.8193 1.8239 -0.0545 0.0087  -0.0241 102 THR L C   
3813 O O   . THR C 102 ? 2.1613 1.9943 1.9911 -0.0540 0.0089  -0.0250 102 THR L O   
3814 C CB  . THR C 102 ? 2.0577 1.8803 1.8947 -0.0574 0.0070  -0.0239 102 THR L CB  
3815 O OG1 . THR C 102 ? 1.8204 1.6453 1.6519 -0.0567 0.0065  -0.0236 102 THR L OG1 
3816 C CG2 . THR C 102 ? 2.2605 2.0767 2.1013 -0.0592 0.0053  -0.0221 102 THR L CG2 
3817 N N   . PHE C 103 ? 2.0899 1.9207 1.9261 -0.0544 0.0100  -0.0246 103 PHE L N   
3818 C CA  . PHE C 103 ? 2.0555 1.8934 1.8896 -0.0540 0.0116  -0.0262 103 PHE L CA  
3819 C C   . PHE C 103 ? 2.0806 1.9235 1.9163 -0.0555 0.0137  -0.0306 103 PHE L C   
3820 O O   . PHE C 103 ? 2.1533 2.0024 1.9860 -0.0555 0.0146  -0.0320 103 PHE L O   
3821 C CB  . PHE C 103 ? 2.0749 1.9140 1.9109 -0.0536 0.0122  -0.0249 103 PHE L CB  
3822 C CG  . PHE C 103 ? 2.0864 1.9212 1.9206 -0.0522 0.0098  -0.0204 103 PHE L CG  
3823 C CD1 . PHE C 103 ? 2.0662 1.9035 1.8960 -0.0508 0.0084  -0.0182 103 PHE L CD1 
3824 C CD2 . PHE C 103 ? 2.2469 2.0752 2.0846 -0.0522 0.0087  -0.0182 103 PHE L CD2 
3825 C CE1 . PHE C 103 ? 2.2499 2.0829 2.0787 -0.0494 0.0059  -0.0142 103 PHE L CE1 
3826 C CE2 . PHE C 103 ? 2.3024 2.1266 2.1386 -0.0509 0.0062  -0.0141 103 PHE L CE2 
3827 C CZ  . PHE C 103 ? 2.3366 2.1630 2.1684 -0.0495 0.0048  -0.0121 103 PHE L CZ  
3828 N N   . GLY C 104 ? 1.8605 1.7007 1.7013 -0.0570 0.0141  -0.0326 104 GLY L N   
3829 C CA  . GLY C 104 ? 1.6606 1.5049 1.5038 -0.0584 0.0158  -0.0371 104 GLY L CA  
3830 C C   . GLY C 104 ? 1.7868 1.6352 1.6327 -0.0586 0.0182  -0.0399 104 GLY L C   
3831 O O   . GLY C 104 ? 1.7950 1.6428 1.6417 -0.0578 0.0185  -0.0382 104 GLY L O   
3832 N N   . GLN C 105 ? 1.8970 1.7498 1.7443 -0.0598 0.0198  -0.0445 105 GLN L N   
3833 C CA  . GLN C 105 ? 1.8584 1.7162 1.7077 -0.0603 0.0224  -0.0483 105 GLN L CA  
3834 C C   . GLN C 105 ? 1.9268 1.7910 1.7700 -0.0598 0.0232  -0.0469 105 GLN L C   
3835 O O   . GLN C 105 ? 2.0008 1.8639 1.8397 -0.0587 0.0215  -0.0425 105 GLN L O   
3836 C CB  . GLN C 105 ? 1.8516 1.7122 1.7036 -0.0617 0.0235  -0.0538 105 GLN L CB  
3837 C CG  . GLN C 105 ? 1.9114 1.7662 1.7712 -0.0625 0.0225  -0.0553 105 GLN L CG  
3838 C CD  . GLN C 105 ? 1.9438 1.8008 1.8066 -0.0640 0.0229  -0.0606 105 GLN L CD  
3839 O OE1 . GLN C 105 ? 2.0958 1.9577 1.9537 -0.0646 0.0232  -0.0621 105 GLN L OE1 
3840 N NE2 . GLN C 105 ? 2.2003 2.0536 2.0717 -0.0647 0.0225  -0.0633 105 GLN L NE2 
3841 N N   . GLY C 106 ? 1.8704 1.7414 1.7130 -0.0607 0.0255  -0.0507 106 GLY L N   
3842 C CA  . GLY C 106 ? 1.9494 1.8273 1.7861 -0.0609 0.0261  -0.0492 106 GLY L CA  
3843 C C   . GLY C 106 ? 1.8061 1.6910 1.6403 -0.0625 0.0276  -0.0538 106 GLY L C   
3844 O O   . GLY C 106 ? 1.9871 1.8727 1.8251 -0.0634 0.0292  -0.0590 106 GLY L O   
3845 N N   . THR C 107 ? 1.8226 1.7127 1.6507 -0.0630 0.0269  -0.0517 107 THR L N   
3846 C CA  . THR C 107 ? 1.8360 1.7334 1.6607 -0.0649 0.0280  -0.0552 107 THR L CA  
3847 C C   . THR C 107 ? 1.8747 1.7798 1.6956 -0.0659 0.0292  -0.0542 107 THR L C   
3848 O O   . THR C 107 ? 1.7701 1.6756 1.5888 -0.0652 0.0277  -0.0489 107 THR L O   
3849 C CB  . THR C 107 ? 1.8630 1.7607 1.6838 -0.0650 0.0259  -0.0536 107 THR L CB  
3850 O OG1 . THR C 107 ? 1.9941 1.8916 1.8116 -0.0639 0.0238  -0.0478 107 THR L OG1 
3851 C CG2 . THR C 107 ? 1.8357 1.7269 1.6600 -0.0644 0.0248  -0.0545 107 THR L CG2 
3852 N N   . LYS C 108 ? 1.6809 1.5926 1.5013 -0.0678 0.0318  -0.0593 108 LYS L N   
3853 C CA  . LYS C 108 ? 1.7018 1.6222 1.5186 -0.0695 0.0333  -0.0591 108 LYS L CA  
3854 C C   . LYS C 108 ? 1.7736 1.7013 1.5845 -0.0719 0.0332  -0.0605 108 LYS L C   
3855 O O   . LYS C 108 ? 1.8069 1.7344 1.6180 -0.0726 0.0334  -0.0649 108 LYS L O   
3856 C CB  . LYS C 108 ? 1.5308 1.4538 1.3517 -0.0699 0.0369  -0.0642 108 LYS L CB  
3857 C CG  . LYS C 108 ? 1.5432 1.4602 1.3700 -0.0678 0.0371  -0.0622 108 LYS L CG  
3858 C CD  . LYS C 108 ? 1.3263 1.2465 1.1580 -0.0682 0.0408  -0.0676 108 LYS L CD  
3859 C CE  . LYS C 108 ? 1.5149 1.4290 1.3529 -0.0663 0.0408  -0.0651 108 LYS L CE  
3860 N NZ  . LYS C 108 ? 1.3902 1.3075 1.2341 -0.0663 0.0444  -0.0706 108 LYS L NZ  
3861 N N   . LEU C 109 ? 1.9034 1.8378 1.7095 -0.0733 0.0324  -0.0566 109 LEU L N   
3862 C CA  . LEU C 109 ? 1.8148 1.7567 1.6151 -0.0760 0.0318  -0.0569 109 LEU L CA  
3863 C C   . LEU C 109 ? 1.9422 1.8940 1.7396 -0.0788 0.0345  -0.0597 109 LEU L C   
3864 O O   . LEU C 109 ? 2.0606 2.0149 1.8591 -0.0787 0.0358  -0.0581 109 LEU L O   
3869 N N   . GLU C 110 ? 1.9180 1.8759 1.7115 -0.0814 0.0354  -0.0640 110 GLU L N   
3870 C CA  . GLU C 110 ? 1.9261 1.8945 1.7156 -0.0846 0.0379  -0.0670 110 GLU L CA  
3871 C C   . GLU C 110 ? 2.0283 2.0040 1.8108 -0.0877 0.0355  -0.0629 110 GLU L C   
3872 O O   . GLU C 110 ? 2.0148 1.9878 1.7961 -0.0877 0.0327  -0.0608 110 GLU L O   
3873 C CB  . GLU C 110 ? 2.1695 2.1393 1.9603 -0.0854 0.0411  -0.0763 110 GLU L CB  
3874 C CG  . GLU C 110 ? 2.0043 1.9689 1.8025 -0.0828 0.0438  -0.0808 110 GLU L CG  
3875 C CD  . GLU C 110 ? 2.1325 2.1029 1.9314 -0.0843 0.0478  -0.0897 110 GLU L CD  
3876 O OE1 . GLU C 110 ? 2.2912 2.2719 2.0844 -0.0873 0.0495  -0.0910 110 GLU L OE1 
3877 O OE2 . GLU C 110 ? 2.0067 1.9716 1.8121 -0.0825 0.0492  -0.0955 110 GLU L OE2 
3878 N N   . ILE C 111 ? 2.1859 2.1714 1.9643 -0.0907 0.0366  -0.0615 111 ILE L N   
3879 C CA  . ILE C 111 ? 2.2015 2.1943 1.9742 -0.0939 0.0337  -0.0558 111 ILE L CA  
3880 C C   . ILE C 111 ? 2.2899 2.2860 2.0581 -0.0965 0.0328  -0.0587 111 ILE L C   
3881 O O   . ILE C 111 ? 2.3238 2.3167 2.0915 -0.0962 0.0293  -0.0548 111 ILE L O   
3882 C CB  . ILE C 111 ? 2.4191 2.4225 2.1883 -0.0971 0.0352  -0.0538 111 ILE L CB  
3883 C CG1 . ILE C 111 ? 2.4185 2.4188 2.1921 -0.0948 0.0349  -0.0487 111 ILE L CG1 
3884 C CG2 . ILE C 111 ? 2.5953 2.6071 2.3585 -0.1012 0.0320  -0.0482 111 ILE L CG2 
3885 C CD1 . ILE C 111 ? 2.0668 2.0774 1.8383 -0.0976 0.0370  -0.0475 111 ILE L CD1 
3886 N N   . LYS C 112 ? 2.3705 2.3734 2.1354 -0.0992 0.0359  -0.0657 112 LYS L N   
3887 C CA  . LYS C 112 ? 2.4409 2.4477 2.2012 -0.1022 0.0352  -0.0690 112 LYS L CA  
3888 C C   . LYS C 112 ? 2.5303 2.5362 2.2920 -0.1019 0.0387  -0.0791 112 LYS L C   
3889 O O   . LYS C 112 ? 2.6439 2.6551 2.4052 -0.1028 0.0425  -0.0842 112 LYS L O   
3890 C CB  . LYS C 112 ? 2.3516 2.3707 2.1044 -0.1074 0.0346  -0.0665 112 LYS L CB  
3891 C CG  . LYS C 112 ? 2.2396 2.2609 1.9906 -0.1087 0.0302  -0.0566 112 LYS L CG  
3892 C CD  . LYS C 112 ? 2.3050 2.3393 2.0486 -0.1145 0.0299  -0.0550 112 LYS L CD  
3893 C CE  . LYS C 112 ? 2.3937 2.4307 2.1362 -0.1162 0.0250  -0.0447 112 LYS L CE  
3894 N NZ  . LYS C 112 ? 2.6367 2.6867 2.3722 -0.1224 0.0241  -0.0421 112 LYS L NZ  
3895 N N   . ARG C 113 ? 2.4938 2.4937 2.2571 -0.1009 0.0373  -0.0820 113 ARG L N   
3896 C CA  . ARG C 113 ? 2.5588 2.5567 2.3244 -0.1005 0.0400  -0.0915 113 ARG L CA  
3897 C C   . ARG C 113 ? 2.8315 2.8391 2.5906 -0.1048 0.0416  -0.0974 113 ARG L C   
3898 O O   . ARG C 113 ? 3.1635 3.1712 2.9245 -0.1047 0.0443  -0.1062 113 ARG L O   
3899 C CB  . ARG C 113 ? 2.4378 2.4265 2.2074 -0.0984 0.0376  -0.0923 113 ARG L CB  
3900 C CG  . ARG C 113 ? 2.4884 2.4674 2.2639 -0.0944 0.0357  -0.0869 113 ARG L CG  
3901 C CD  . ARG C 113 ? 2.6611 2.6344 2.4379 -0.0938 0.0327  -0.0860 113 ARG L CD  
3902 N NE  . ARG C 113 ? 2.6251 2.5984 2.4025 -0.0951 0.0337  -0.0939 113 ARG L NE  
3903 C CZ  . ARG C 113 ? 2.4296 2.3973 2.2132 -0.0931 0.0353  -0.0998 113 ARG L CZ  
3904 N NH1 . ARG C 113 ? 2.2590 2.2202 2.0487 -0.0899 0.0360  -0.0984 113 ARG L NH1 
3905 N NH2 . ARG C 113 ? 2.3561 2.3247 2.1401 -0.0946 0.0359  -0.1072 113 ARG L NH2 
3906 N N   . THR C 114 ? 2.5142 2.5497 2.2586 -0.1140 0.0473  -0.1021 114 THR L N   
3907 C CA  . THR C 114 ? 2.3928 2.4376 2.1352 -0.1157 0.0520  -0.1082 114 THR L CA  
3908 C C   . THR C 114 ? 2.3853 2.4248 2.1347 -0.1124 0.0557  -0.1182 114 THR L C   
3909 O O   . THR C 114 ? 2.4117 2.4408 2.1692 -0.1079 0.0553  -0.1175 114 THR L O   
3910 C CB  . THR C 114 ? 2.1598 2.2093 1.9024 -0.1157 0.0528  -0.1013 114 THR L CB  
3911 O OG1 . THR C 114 ? 2.0480 2.0867 1.7989 -0.1107 0.0521  -0.0979 114 THR L OG1 
3912 C CG2 . THR C 114 ? 1.5161 1.5716 1.2523 -0.1195 0.0488  -0.0916 114 THR L CG2 
3913 N N   . VAL C 115 ? 2.0791 2.1260 1.8254 -0.1147 0.0591  -0.1276 115 VAL L N   
3914 C CA  . VAL C 115 ? 1.8822 1.9254 1.6353 -0.1119 0.0627  -0.1381 115 VAL L CA  
3915 C C   . VAL C 115 ? 2.1814 2.2312 1.9368 -0.1112 0.0674  -0.1400 115 VAL L C   
3916 O O   . VAL C 115 ? 2.1864 2.2451 1.9363 -0.1138 0.0679  -0.1341 115 VAL L O   
3917 C CB  . VAL C 115 ? 1.8301 1.8772 1.5790 -0.1146 0.0635  -0.1478 115 VAL L CB  
3918 C CG1 . VAL C 115 ? 1.5381 1.5823 1.2947 -0.1118 0.0672  -0.1595 115 VAL L CG1 
3919 C CG2 . VAL C 115 ? 1.5901 1.6307 1.3373 -0.1153 0.0586  -0.1449 115 VAL L CG2 
3920 N N   . ALA C 116 ? 2.1904 2.2359 1.9544 -0.1077 0.0706  -0.1477 116 ALA L N   
3921 C CA  . ALA C 116 ? 2.2955 2.3462 2.0632 -0.1065 0.0750  -0.1494 116 ALA L CA  
3922 C C   . ALA C 116 ? 2.4923 2.5585 2.2527 -0.1106 0.0792  -0.1551 116 ALA L C   
3923 O O   . ALA C 116 ? 2.8205 2.8911 2.5762 -0.1131 0.0801  -0.1629 116 ALA L O   
3924 C CB  . ALA C 116 ? 2.1548 2.1968 1.9344 -0.1018 0.0771  -0.1567 116 ALA L CB  
3925 N N   . ALA C 117 ? 2.5477 2.6222 2.3069 -0.1115 0.0818  -0.1511 117 ALA L N   
3926 C CA  . ALA C 117 ? 2.4418 2.5318 2.1953 -0.1151 0.0867  -0.1568 117 ALA L CA  
3927 C C   . ALA C 117 ? 2.5500 2.6430 2.3108 -0.1125 0.0910  -0.1577 117 ALA L C   
3928 O O   . ALA C 117 ? 2.5041 2.6071 2.2611 -0.1149 0.0924  -0.1519 117 ALA L O   
3929 C CB  . ALA C 117 ? 2.2007 2.3021 1.9423 -0.1209 0.0848  -0.1492 117 ALA L CB  
3930 N N   . PRO C 118 ? 2.5579 2.6427 2.3298 -0.1078 0.0931  -0.1647 118 PRO L N   
3931 C CA  . PRO C 118 ? 2.4219 2.5078 2.2020 -0.1049 0.0967  -0.1645 118 PRO L CA  
3932 C C   . PRO C 118 ? 2.4667 2.5685 2.2440 -0.1073 0.1029  -0.1720 118 PRO L C   
3933 O O   . PRO C 118 ? 2.5038 2.6106 2.2798 -0.1083 0.1060  -0.1833 118 PRO L O   
3934 C CB  . PRO C 118 ? 2.2096 2.2818 2.0024 -0.0996 0.0965  -0.1707 118 PRO L CB  
3935 C CG  . PRO C 118 ? 2.3471 2.4097 2.1378 -0.0997 0.0919  -0.1710 118 PRO L CG  
3936 C CD  . PRO C 118 ? 2.3322 2.4058 2.1103 -0.1049 0.0918  -0.1724 118 PRO L CD  
3937 N N   . SER C 119 ? 2.4235 2.5336 2.2000 -0.1084 0.1047  -0.1655 119 SER L N   
3938 C CA  . SER C 119 ? 2.1646 2.2895 1.9408 -0.1099 0.1112  -0.1719 119 SER L CA  
3939 C C   . SER C 119 ? 2.0837 2.2030 1.8738 -0.1047 0.1142  -0.1755 119 SER L C   
3940 O O   . SER C 119 ? 2.2890 2.4016 2.0847 -0.1024 0.1121  -0.1665 119 SER L O   
3941 C CB  . SER C 119 ? 2.2771 2.4155 2.0446 -0.1146 0.1112  -0.1623 119 SER L CB  
3942 O OG  . SER C 119 ? 2.5562 2.6866 2.3264 -0.1132 0.1067  -0.1494 119 SER L OG  
3943 N N   . VAL C 120 ? 2.0590 2.1805 1.8552 -0.1028 0.1189  -0.1886 120 VAL L N   
3944 C CA  . VAL C 120 ? 2.0301 2.1457 1.8407 -0.0977 0.1217  -0.1935 120 VAL L CA  
3945 C C   . VAL C 120 ? 2.1332 2.2643 1.9450 -0.0987 0.1281  -0.1963 120 VAL L C   
3946 O O   . VAL C 120 ? 2.4047 2.5512 2.2075 -0.1028 0.1318  -0.2013 120 VAL L O   
3947 C CB  . VAL C 120 ? 1.8646 1.9722 1.6833 -0.0946 0.1224  -0.2063 120 VAL L CB  
3948 C CG1 . VAL C 120 ? 1.7284 1.8293 1.5632 -0.0894 0.1248  -0.2107 120 VAL L CG1 
3949 C CG2 . VAL C 120 ? 1.8391 1.9325 1.6560 -0.0941 0.1160  -0.2028 120 VAL L CG2 
3950 N N   . PHE C 121 ? 2.1127 2.2401 1.9352 -0.0953 0.1292  -0.1928 121 PHE L N   
3951 C CA  . PHE C 121 ? 1.6607 1.8017 1.4866 -0.0955 0.1353  -0.1954 121 PHE L CA  
3952 C C   . PHE C 121 ? 1.7108 1.8422 1.5535 -0.0899 0.1366  -0.1982 121 PHE L C   
3953 O O   . PHE C 121 ? 1.8399 1.9547 1.6897 -0.0865 0.1321  -0.1955 121 PHE L O   
3954 C CB  . PHE C 121 ? 1.8184 1.9685 1.6369 -0.0991 0.1343  -0.1824 121 PHE L CB  
3955 C CG  . PHE C 121 ? 2.0652 2.2247 1.8679 -0.1050 0.1324  -0.1782 121 PHE L CG  
3956 C CD1 . PHE C 121 ? 2.2911 2.4683 2.0856 -0.1093 0.1374  -0.1852 121 PHE L CD1 
3957 C CD2 . PHE C 121 ? 2.2090 2.3599 2.0055 -0.1064 0.1256  -0.1670 121 PHE L CD2 
3958 C CE1 . PHE C 121 ? 2.5822 2.7681 2.3622 -0.1152 0.1352  -0.1808 121 PHE L CE1 
3959 C CE2 . PHE C 121 ? 2.3192 2.4786 2.1020 -0.1120 0.1235  -0.1627 121 PHE L CE2 
3960 C CZ  . PHE C 121 ? 2.5737 2.7505 2.3482 -0.1165 0.1281  -0.1693 121 PHE L CZ  
3961 N N   . ILE C 122 ? 1.5075 1.6498 1.3567 -0.0890 0.1427  -0.2035 122 ILE L N   
3962 C CA  . ILE C 122 ? 1.7808 1.9154 1.6464 -0.0839 0.1440  -0.2051 122 ILE L CA  
3963 C C   . ILE C 122 ? 1.8095 1.9584 1.6769 -0.0849 0.1490  -0.2022 122 ILE L C   
3964 O O   . ILE C 122 ? 1.9368 2.1031 1.7953 -0.0888 0.1534  -0.2049 122 ILE L O   
3965 C CB  . ILE C 122 ? 1.6735 1.8039 1.5502 -0.0802 0.1470  -0.2203 122 ILE L CB  
3966 C CG1 . ILE C 122 ? 1.7145 1.8300 1.5909 -0.0791 0.1416  -0.2227 122 ILE L CG1 
3967 C CG2 . ILE C 122 ? 1.8161 1.9401 1.7106 -0.0753 0.1485  -0.2219 122 ILE L CG2 
3968 C CD1 . ILE C 122 ? 1.8383 1.9524 1.7233 -0.0766 0.1444  -0.2380 122 ILE L CD1 
3969 N N   . PHE C 123 ? 1.8564 1.9983 1.7353 -0.0815 0.1482  -0.1963 123 PHE L N   
3970 C CA  . PHE C 123 ? 1.9690 2.1229 1.8501 -0.0825 0.1518  -0.1909 123 PHE L CA  
3971 C C   . PHE C 123 ? 2.0388 2.1908 1.9375 -0.0777 0.1557  -0.1974 123 PHE L C   
3972 O O   . PHE C 123 ? 1.9590 2.0953 1.8685 -0.0739 0.1519  -0.1933 123 PHE L O   
3973 C CB  . PHE C 123 ? 1.9266 2.0747 1.8031 -0.0839 0.1460  -0.1743 123 PHE L CB  
3974 C CG  . PHE C 123 ? 1.8209 1.9724 1.6811 -0.0887 0.1422  -0.1676 123 PHE L CG  
3975 C CD1 . PHE C 123 ? 1.8630 2.0331 1.7119 -0.0939 0.1455  -0.1674 123 PHE L CD1 
3976 C CD2 . PHE C 123 ? 1.7722 1.9085 1.6285 -0.0882 0.1354  -0.1619 123 PHE L CD2 
3977 C CE1 . PHE C 123 ? 1.8528 2.0259 1.6874 -0.0985 0.1416  -0.1610 123 PHE L CE1 
3978 C CE2 . PHE C 123 ? 1.8065 1.9458 1.6487 -0.0925 0.1318  -0.1559 123 PHE L CE2 
3979 C CZ  . PHE C 123 ? 1.9094 2.0669 1.7409 -0.0977 0.1348  -0.1553 123 PHE L CZ  
3980 N N   . PRO C 124 ? 2.0314 2.1989 1.9336 -0.0779 0.1632  -0.2075 124 PRO L N   
3981 C CA  . PRO C 124 ? 1.9086 2.0749 1.8285 -0.0733 0.1671  -0.2133 124 PRO L CA  
3982 C C   . PRO C 124 ? 2.0862 2.2532 2.0110 -0.0730 0.1662  -0.2011 124 PRO L C   
3983 O O   . PRO C 124 ? 2.1924 2.3670 2.1063 -0.0770 0.1648  -0.1900 124 PRO L O   
3984 C CB  . PRO C 124 ? 1.7969 1.9822 1.7164 -0.0743 0.1756  -0.2272 124 PRO L CB  
3985 C CG  . PRO C 124 ? 1.9062 2.1062 1.8073 -0.0804 0.1763  -0.2226 124 PRO L CG  
3986 C CD  . PRO C 124 ? 2.0522 2.2390 1.9428 -0.0822 0.1686  -0.2145 124 PRO L CD  
3987 N N   . PRO C 125 ? 2.0423 2.2014 1.9838 -0.0685 0.1666  -0.2017 125 PRO L N   
3988 C CA  . PRO C 125 ? 2.1927 2.3503 2.1394 -0.0681 0.1649  -0.1892 125 PRO L CA  
3989 C C   . PRO C 125 ? 2.2799 2.4583 2.2262 -0.0703 0.1715  -0.1892 125 PRO L C   
3990 O O   . PRO C 125 ? 2.3193 2.5100 2.2710 -0.0694 0.1786  -0.2014 125 PRO L O   
3991 C CB  . PRO C 125 ? 2.2170 2.3595 2.1824 -0.0627 0.1633  -0.1917 125 PRO L CB  
3992 C CG  . PRO C 125 ? 2.0586 2.2044 2.0315 -0.0604 0.1682  -0.2086 125 PRO L CG  
3993 C CD  . PRO C 125 ? 1.9618 2.1122 1.9190 -0.0637 0.1681  -0.2138 125 PRO L CD  
3994 N N   . SER C 126 ? 2.3651 2.5476 2.3048 -0.0732 0.1690  -0.1753 126 SER L N   
3995 C CA  . SER C 126 ? 2.2447 2.4459 2.1854 -0.0753 0.1745  -0.1730 126 SER L CA  
3996 C C   . SER C 126 ? 2.3481 2.5474 2.3080 -0.0706 0.1778  -0.1763 126 SER L C   
3997 O O   . SER C 126 ? 2.5032 2.6847 2.4744 -0.0666 0.1737  -0.1748 126 SER L O   
3998 C CB  . SER C 126 ? 2.1828 2.3864 2.1139 -0.0792 0.1698  -0.1563 126 SER L CB  
3999 O OG  . SER C 126 ? 2.4863 2.6751 2.4268 -0.0764 0.1647  -0.1460 126 SER L OG  
4000 N N   . ASP C 127 ? 2.2716 2.4898 2.2354 -0.0715 0.1851  -0.1807 127 ASP L N   
4001 C CA  . ASP C 127 ? 2.3254 2.5439 2.3079 -0.0673 0.1886  -0.1834 127 ASP L CA  
4002 C C   . ASP C 127 ? 2.5787 2.7852 2.5679 -0.0662 0.1828  -0.1686 127 ASP L C   
4003 O O   . ASP C 127 ? 2.7931 2.9958 2.7989 -0.0624 0.1843  -0.1698 127 ASP L O   
4004 C CB  . ASP C 127 ? 2.3258 2.5685 2.3098 -0.0690 0.1975  -0.1889 127 ASP L CB  
4005 C CG  . ASP C 127 ? 2.0794 2.3331 2.0626 -0.0686 0.2045  -0.2066 127 ASP L CG  
4006 O OD1 . ASP C 127 ? 2.0939 2.3347 2.0798 -0.0658 0.2025  -0.2154 127 ASP L OD1 
4007 O OD2 . ASP C 127 ? 2.1178 2.3931 2.0981 -0.0710 0.2118  -0.2118 127 ASP L OD2 
4008 N N   . GLU C 128 ? 2.2957 2.4959 2.2732 -0.0692 0.1761  -0.1550 128 GLU L N   
4009 C CA  . GLU C 128 ? 2.3010 2.4903 2.2839 -0.0684 0.1704  -0.1408 128 GLU L CA  
4010 C C   . GLU C 128 ? 2.3573 2.5233 2.3508 -0.0638 0.1649  -0.1409 128 GLU L C   
4011 O O   . GLU C 128 ? 2.4019 2.5611 2.4101 -0.0607 0.1643  -0.1383 128 GLU L O   
4012 C CB  . GLU C 128 ? 2.3940 2.5843 2.3608 -0.0731 0.1649  -0.1273 128 GLU L CB  
4013 C CG  . GLU C 128 ? 1.9847 2.1979 1.9418 -0.0783 0.1690  -0.1240 128 GLU L CG  
4014 C CD  . GLU C 128 ? 2.0938 2.3052 2.0357 -0.0828 0.1624  -0.1111 128 GLU L CD  
4015 O OE1 . GLU C 128 ? 2.6618 2.8553 2.6006 -0.0815 0.1558  -0.1075 128 GLU L OE1 
4016 O OE2 . GLU C 128 ? 1.3940 1.6217 1.3276 -0.0875 0.1636  -0.1046 128 GLU L OE2 
4017 N N   . GLN C 129 ? 2.3878 2.5415 2.3740 -0.0636 0.1608  -0.1436 129 GLN L N   
4018 C CA  . GLN C 129 ? 2.3625 2.4962 2.3594 -0.0594 0.1567  -0.1466 129 GLN L CA  
4019 C C   . GLN C 129 ? 2.4392 2.5752 2.4533 -0.0555 0.1623  -0.1590 129 GLN L C   
4020 O O   . GLN C 129 ? 2.4656 2.5891 2.4944 -0.0520 0.1599  -0.1578 129 GLN L O   
4021 C CB  . GLN C 129 ? 2.2978 2.4218 2.2848 -0.0599 0.1531  -0.1506 129 GLN L CB  
4022 C CG  . GLN C 129 ? 2.5775 2.6955 2.5495 -0.0630 0.1466  -0.1387 129 GLN L CG  
4023 C CD  . GLN C 129 ? 2.4354 2.5445 2.3980 -0.0636 0.1432  -0.1425 129 GLN L CD  
4024 O OE1 . GLN C 129 ? 1.9323 2.0446 1.8950 -0.0630 0.1466  -0.1548 129 GLN L OE1 
4025 N NE2 . GLN C 129 ? 2.8136 2.9112 2.7681 -0.0647 0.1362  -0.1319 129 GLN L NE2 
4026 N N   . LEU C 130 ? 2.6911 2.8432 2.7039 -0.0561 0.1696  -0.1711 130 LEU L N   
4027 C CA  . LEU C 130 ? 2.5428 2.6992 2.5720 -0.0523 0.1756  -0.1842 130 LEU L CA  
4028 C C   . LEU C 130 ? 2.5754 2.7387 2.6181 -0.0509 0.1787  -0.1800 130 LEU L C   
4029 O O   . LEU C 130 ? 2.5717 2.7380 2.6304 -0.0474 0.1834  -0.1899 130 LEU L O   
4030 C CB  . LEU C 130 ? 2.4194 2.5929 2.4418 -0.0538 0.1827  -0.1979 130 LEU L CB  
4031 C CG  . LEU C 130 ? 2.3232 2.4899 2.3348 -0.0548 0.1801  -0.2043 130 LEU L CG  
4032 C CD1 . LEU C 130 ? 2.1448 2.3296 2.1496 -0.0565 0.1874  -0.2179 130 LEU L CD1 
4033 C CD2 . LEU C 130 ? 2.3197 2.4665 2.3435 -0.0505 0.1758  -0.2093 130 LEU L CD2 
4034 N N   . LYS C 131 ? 2.2663 2.4326 2.3031 -0.0535 0.1762  -0.1658 131 LYS L N   
4035 C CA  . LYS C 131 ? 2.3789 2.5474 2.4287 -0.0521 0.1771  -0.1589 131 LYS L CA  
4036 C C   . LYS C 131 ? 2.2457 2.3924 2.3038 -0.0498 0.1691  -0.1494 131 LYS L C   
4037 O O   . LYS C 131 ? 1.9822 2.1245 2.0573 -0.0467 0.1695  -0.1490 131 LYS L O   
4038 C CB  . LYS C 131 ? 2.3100 2.4939 2.3494 -0.0565 0.1782  -0.1481 131 LYS L CB  
4039 C CG  . LYS C 131 ? 2.3850 2.5931 2.4175 -0.0593 0.1865  -0.1562 131 LYS L CG  
4040 C CD  . LYS C 131 ? 2.4507 2.6729 2.4728 -0.0642 0.1865  -0.1438 131 LYS L CD  
4041 C CE  . LYS C 131 ? 2.6481 2.8954 2.6627 -0.0675 0.1948  -0.1516 131 LYS L CE  
4042 N NZ  . LYS C 131 ? 2.5536 2.8152 2.5581 -0.0727 0.1943  -0.1388 131 LYS L NZ  
4043 N N   . SER C 132 ? 2.4491 2.5823 2.4954 -0.0514 0.1619  -0.1418 132 SER L N   
4044 C CA  . SER C 132 ? 2.1753 2.2884 2.2272 -0.0498 0.1541  -0.1317 132 SER L CA  
4045 C C   . SER C 132 ? 2.1846 2.2830 2.2514 -0.0456 0.1527  -0.1397 132 SER L C   
4046 O O   . SER C 132 ? 2.2999 2.3866 2.3790 -0.0435 0.1489  -0.1339 132 SER L O   
4047 C CB  . SER C 132 ? 2.0258 2.1294 2.0609 -0.0525 0.1472  -0.1223 132 SER L CB  
4048 O OG  . SER C 132 ? 1.8491 1.9422 1.8806 -0.0515 0.1449  -0.1295 132 SER L OG  
4049 N N   . GLY C 133 ? 2.3943 2.4930 2.4603 -0.0446 0.1550  -0.1524 133 GLY L N   
4050 C CA  . GLY C 133 ? 2.1396 2.2237 2.2188 -0.0410 0.1527  -0.1597 133 GLY L CA  
4051 C C   . GLY C 133 ? 1.9469 2.0211 2.0159 -0.0417 0.1489  -0.1635 133 GLY L C   
4052 O O   . GLY C 133 ? 1.9778 2.0473 2.0545 -0.0395 0.1497  -0.1746 133 GLY L O   
4053 N N   . THR C 134 ? 1.8432 1.9141 1.8955 -0.0447 0.1445  -0.1541 134 THR L N   
4054 C CA  . THR C 134 ? 1.8538 1.9164 1.8951 -0.0457 0.1408  -0.1565 134 THR L CA  
4055 C C   . THR C 134 ? 2.1365 2.2140 2.1671 -0.0476 0.1463  -0.1666 134 THR L C   
4056 O O   . THR C 134 ? 2.3289 2.4231 2.3529 -0.0498 0.1511  -0.1661 134 THR L O   
4057 C CB  . THR C 134 ? 2.1958 2.2493 2.2241 -0.0481 0.1340  -0.1425 134 THR L CB  
4058 O OG1 . THR C 134 ? 2.4776 2.5448 2.4947 -0.0512 0.1361  -0.1358 134 THR L OG1 
4059 C CG2 . THR C 134 ? 1.8808 1.9197 1.9200 -0.0463 0.1287  -0.1333 134 THR L CG2 
4060 N N   . ALA C 135 ? 2.0113 2.0832 2.0402 -0.0469 0.1455  -0.1757 135 ALA L N   
4061 C CA  . ALA C 135 ? 1.9182 2.0030 1.9375 -0.0487 0.1503  -0.1863 135 ALA L CA  
4062 C C   . ALA C 135 ? 1.9150 1.9897 1.9222 -0.0502 0.1451  -0.1853 135 ALA L C   
4063 O O   . ALA C 135 ? 2.1199 2.1814 2.1340 -0.0481 0.1417  -0.1896 135 ALA L O   
4064 C CB  . ALA C 135 ? 1.8383 1.9286 1.8715 -0.0457 0.1560  -0.2019 135 ALA L CB  
4065 N N   . SER C 136 ? 1.8041 1.8853 1.7938 -0.0540 0.1442  -0.1793 136 SER L N   
4066 C CA  . SER C 136 ? 1.9747 2.0466 1.9525 -0.0556 0.1388  -0.1765 136 SER L CA  
4067 C C   . SER C 136 ? 1.7649 1.8502 1.7276 -0.0591 0.1420  -0.1818 136 SER L C   
4068 O O   . SER C 136 ? 1.9024 2.0038 1.8586 -0.0617 0.1464  -0.1808 136 SER L O   
4069 C CB  . SER C 136 ? 2.1573 2.2198 2.1283 -0.0569 0.1324  -0.1612 136 SER L CB  
4070 O OG  . SER C 136 ? 2.6692 2.7445 2.6309 -0.0599 0.1342  -0.1537 136 SER L OG  
4071 N N   . VAL C 137 ? 1.4880 1.5668 1.4455 -0.0594 0.1396  -0.1871 137 VAL L N   
4072 C CA  . VAL C 137 ? 1.8466 1.9361 1.7903 -0.0627 0.1418  -0.1930 137 VAL L CA  
4073 C C   . VAL C 137 ? 1.9052 1.9846 1.8369 -0.0646 0.1353  -0.1857 137 VAL L C   
4074 O O   . VAL C 137 ? 1.9977 2.0611 1.9347 -0.0625 0.1302  -0.1841 137 VAL L O   
4075 C CB  . VAL C 137 ? 1.8564 1.9492 1.8066 -0.0610 0.1460  -0.2093 137 VAL L CB  
4076 C CG1 . VAL C 137 ? 1.8633 1.9657 1.7983 -0.0647 0.1476  -0.2150 137 VAL L CG1 
4077 C CG2 . VAL C 137 ? 1.7025 1.8065 1.6647 -0.0590 0.1529  -0.2171 137 VAL L CG2 
4078 N N   . VAL C 138 ? 1.8518 1.9409 1.7678 -0.0688 0.1353  -0.1814 138 VAL L N   
4079 C CA  . VAL C 138 ? 1.7817 1.8630 1.6860 -0.0710 0.1292  -0.1729 138 VAL L CA  
4080 C C   . VAL C 138 ? 1.9153 2.0019 1.8091 -0.0735 0.1300  -0.1808 138 VAL L C   
4081 O O   . VAL C 138 ? 2.3055 2.4079 2.1931 -0.0761 0.1350  -0.1867 138 VAL L O   
4082 C CB  . VAL C 138 ? 1.8945 1.9816 1.7894 -0.0740 0.1273  -0.1596 138 VAL L CB  
4083 C CG1 . VAL C 138 ? 1.9434 2.0232 1.8264 -0.0761 0.1211  -0.1517 138 VAL L CG1 
4084 C CG2 . VAL C 138 ? 2.0360 2.1176 1.9410 -0.0716 0.1261  -0.1515 138 VAL L CG2 
4085 N N   . CYS C 139 ? 1.8524 1.9264 1.7442 -0.0729 0.1251  -0.1807 139 CYS L N   
4086 C CA  . CYS C 139 ? 1.8028 1.8799 1.6831 -0.0758 0.1243  -0.1852 139 CYS L CA  
4087 C C   . CYS C 139 ? 1.7343 1.8088 1.6022 -0.0787 0.1191  -0.1728 139 CYS L C   
4088 O O   . CYS C 139 ? 2.0388 2.1000 1.9092 -0.0770 0.1138  -0.1645 139 CYS L O   
4089 C CB  . CYS C 139 ? 1.9510 2.0161 1.8380 -0.0733 0.1221  -0.1935 139 CYS L CB  
4090 S SG  . CYS C 139 ? 1.6058 1.6749 1.4801 -0.0766 0.1214  -0.2006 139 CYS L SG  
4091 N N   . LEU C 140 ? 1.5804 1.6680 1.4354 -0.0831 0.1204  -0.1718 140 LEU L N   
4092 C CA  . LEU C 140 ? 1.7740 1.8613 1.6171 -0.0863 0.1157  -0.1604 140 LEU L CA  
4093 C C   . LEU C 140 ? 1.5723 1.6581 1.4064 -0.0884 0.1134  -0.1642 140 LEU L C   
4094 O O   . LEU C 140 ? 1.6196 1.7136 1.4508 -0.0899 0.1170  -0.1747 140 LEU L O   
4095 C CB  . LEU C 140 ? 1.8712 1.9747 1.7063 -0.0902 0.1182  -0.1548 140 LEU L CB  
4096 C CG  . LEU C 140 ? 1.7933 1.8988 1.6162 -0.0942 0.1134  -0.1434 140 LEU L CG  
4097 C CD1 . LEU C 140 ? 1.7940 1.8841 1.6205 -0.0917 0.1073  -0.1326 140 LEU L CD1 
4098 C CD2 . LEU C 140 ? 1.8339 1.9563 1.6506 -0.0982 0.1161  -0.1384 140 LEU L CD2 
4099 N N   . LEU C 141 ? 1.6079 1.6834 1.4377 -0.0886 0.1074  -0.1558 141 LEU L N   
4100 C CA  . LEU C 141 ? 1.6636 1.7360 1.4855 -0.0905 0.1043  -0.1576 141 LEU L CA  
4101 C C   . LEU C 141 ? 1.7541 1.8275 1.5660 -0.0935 0.0998  -0.1453 141 LEU L C   
4102 O O   . LEU C 141 ? 1.9471 2.0102 1.7618 -0.0916 0.0956  -0.1362 141 LEU L O   
4103 C CB  . LEU C 141 ? 1.7085 1.7646 1.5386 -0.0868 0.1010  -0.1604 141 LEU L CB  
4104 C CG  . LEU C 141 ? 1.6266 1.6801 1.4648 -0.0846 0.1037  -0.1737 141 LEU L CG  
4105 C CD1 . LEU C 141 ? 1.6590 1.7127 1.5098 -0.0814 0.1076  -0.1778 141 LEU L CD1 
4106 C CD2 . LEU C 141 ? 1.7931 1.8312 1.6354 -0.0824 0.0987  -0.1726 141 LEU L CD2 
4107 N N   . ASN C 142 ? 1.8483 1.9340 1.6488 -0.0983 0.1004  -0.1447 142 ASN L N   
4108 C CA  . ASN C 142 ? 1.9054 1.9940 1.6978 -0.1013 0.0964  -0.1324 142 ASN L CA  
4109 C C   . ASN C 142 ? 1.9724 2.0611 1.7548 -0.1045 0.0927  -0.1308 142 ASN L C   
4110 O O   . ASN C 142 ? 2.0146 2.1105 1.7915 -0.1071 0.0949  -0.1388 142 ASN L O   
4111 C CB  . ASN C 142 ? 1.9710 2.0757 1.7593 -0.1047 0.0999  -0.1295 142 ASN L CB  
4112 C CG  . ASN C 142 ? 2.0584 2.1667 1.8392 -0.1081 0.0954  -0.1165 142 ASN L CG  
4113 O OD1 . ASN C 142 ? 2.1256 2.2225 1.9086 -0.1061 0.0903  -0.1079 142 ASN L OD1 
4114 N ND2 . ASN C 142 ? 2.0418 2.1661 1.8140 -0.1133 0.0971  -0.1149 142 ASN L ND2 
4115 N N   . ASN C 143 ? 2.1181 2.1987 1.8986 -0.1043 0.0870  -0.1205 143 ASN L N   
4116 C CA  . ASN C 143 ? 2.1396 2.2209 1.9109 -0.1076 0.0827  -0.1161 143 ASN L CA  
4117 C C   . ASN C 143 ? 2.3741 2.4486 2.1450 -0.1068 0.0818  -0.1238 143 ASN L C   
4118 O O   . ASN C 143 ? 2.5016 2.5842 2.2667 -0.1098 0.0841  -0.1312 143 ASN L O   
4119 C CB  . ASN C 143 ? 1.8952 1.9935 1.6563 -0.1135 0.0841  -0.1144 143 ASN L CB  
4120 C CG  . ASN C 143 ? 1.9346 2.0392 1.6952 -0.1150 0.0834  -0.1042 143 ASN L CG  
4121 O OD1 . ASN C 143 ? 1.8167 1.9119 1.5824 -0.1122 0.0800  -0.0962 143 ASN L OD1 
4122 N ND2 . ASN C 143 ? 2.0633 2.1841 1.8178 -0.1196 0.0864  -0.1045 143 ASN L ND2 
4123 N N   . PHE C 144 ? 2.2363 2.2961 2.0130 -0.1030 0.0784  -0.1218 144 PHE L N   
4124 C CA  . PHE C 144 ? 2.1995 2.2519 1.9765 -0.1023 0.0767  -0.1275 144 PHE L CA  
4125 C C   . PHE C 144 ? 2.2304 2.2697 2.0099 -0.0998 0.0713  -0.1197 144 PHE L C   
4126 O O   . PHE C 144 ? 2.4176 2.4501 2.2026 -0.0970 0.0700  -0.1137 144 PHE L O   
4127 C CB  . PHE C 144 ? 2.2005 2.2490 1.9858 -0.0993 0.0803  -0.1390 144 PHE L CB  
4128 C CG  . PHE C 144 ? 2.0225 2.0648 1.8184 -0.0951 0.0819  -0.1383 144 PHE L CG  
4129 C CD1 . PHE C 144 ? 2.1435 2.1947 1.9420 -0.0952 0.0866  -0.1409 144 PHE L CD1 
4130 C CD2 . PHE C 144 ? 2.0029 2.0308 1.8063 -0.0914 0.0786  -0.1348 144 PHE L CD2 
4131 C CE1 . PHE C 144 ? 2.1570 2.2024 1.9657 -0.0915 0.0879  -0.1400 144 PHE L CE1 
4132 C CE2 . PHE C 144 ? 2.0116 2.0338 1.8248 -0.0879 0.0797  -0.1339 144 PHE L CE2 
4133 C CZ  . PHE C 144 ? 2.0218 2.0525 1.8378 -0.0879 0.0843  -0.1364 144 PHE L CZ  
4134 N N   . TYR C 145 ? 2.3749 2.4108 2.1503 -0.1010 0.0682  -0.1200 145 TYR L N   
4135 C CA  . TYR C 145 ? 2.5853 2.6098 2.3625 -0.0989 0.0632  -0.1128 145 TYR L CA  
4136 C C   . TYR C 145 ? 2.5614 2.5733 2.3478 -0.0947 0.0628  -0.1170 145 TYR L C   
4137 O O   . TYR C 145 ? 2.6687 2.6717 2.4605 -0.0916 0.0609  -0.1114 145 TYR L O   
4138 C CB  . TYR C 145 ? 2.6124 2.6390 2.3817 -0.1020 0.0596  -0.1098 145 TYR L CB  
4139 C CG  . TYR C 145 ? 2.6059 2.6209 2.3781 -0.0995 0.0550  -0.1040 145 TYR L CG  
4140 C CD1 . TYR C 145 ? 2.5765 2.5846 2.3505 -0.0986 0.0536  -0.1084 145 TYR L CD1 
4141 C CD2 . TYR C 145 ? 2.5436 2.5546 2.3168 -0.0981 0.0522  -0.0944 145 TYR L CD2 
4142 C CE1 . TYR C 145 ? 2.4949 2.4933 2.2715 -0.0964 0.0496  -0.1031 145 TYR L CE1 
4143 C CE2 . TYR C 145 ? 2.4207 2.4217 2.1964 -0.0957 0.0483  -0.0897 145 TYR L CE2 
4144 C CZ  . TYR C 145 ? 2.4465 2.4416 2.2238 -0.0950 0.0472  -0.0940 145 TYR L CZ  
4145 O OH  . TYR C 145 ? 2.4855 2.4716 2.2653 -0.0928 0.0436  -0.0892 145 TYR L OH  
4146 N N   . PRO C 146 ? 2.2362 2.2466 2.0248 -0.0946 0.0641  -0.1263 146 PRO L N   
4147 C CA  . PRO C 146 ? 2.0620 2.0607 1.8606 -0.0908 0.0635  -0.1298 146 PRO L CA  
4148 C C   . PRO C 146 ? 2.2182 2.2144 2.0252 -0.0878 0.0661  -0.1305 146 PRO L C   
4149 O O   . PRO C 146 ? 2.2447 2.2471 2.0542 -0.0879 0.0704  -0.1376 146 PRO L O   
4150 C CB  . PRO C 146 ? 1.7167 1.7170 1.5158 -0.0918 0.0649  -0.1405 146 PRO L CB  
4151 C CG  . PRO C 146 ? 1.9977 2.0066 1.7859 -0.0960 0.0641  -0.1398 146 PRO L CG  
4152 C CD  . PRO C 146 ? 2.0622 2.0803 1.8445 -0.0980 0.0653  -0.1334 146 PRO L CD  
4153 N N   . ARG C 147 ? 2.3437 2.3312 2.1551 -0.0852 0.0637  -0.1231 147 ARG L N   
4154 C CA  . ARG C 147 ? 2.1880 2.1723 2.0079 -0.0824 0.0657  -0.1231 147 ARG L CA  
4155 C C   . ARG C 147 ? 2.1838 2.1629 2.0134 -0.0804 0.0674  -0.1322 147 ARG L C   
4156 O O   . ARG C 147 ? 2.3143 2.2933 2.1514 -0.0785 0.0702  -0.1349 147 ARG L O   
4157 C CB  . ARG C 147 ? 2.1980 2.1730 2.0204 -0.0802 0.0622  -0.1136 147 ARG L CB  
4158 C CG  . ARG C 147 ? 2.0657 2.0398 1.8941 -0.0783 0.0639  -0.1106 147 ARG L CG  
4159 C CD  . ARG C 147 ? 1.9375 1.9030 1.7667 -0.0765 0.0600  -0.1009 147 ARG L CD  
4160 N NE  . ARG C 147 ? 1.9955 1.9648 1.8243 -0.0765 0.0608  -0.0950 147 ARG L NE  
4161 C CZ  . ARG C 147 ? 1.9654 1.9276 1.7971 -0.0746 0.0582  -0.0877 147 ARG L CZ  
4162 N NH1 . ARG C 147 ? 1.9871 1.9378 1.8228 -0.0724 0.0553  -0.0857 147 ARG L NH1 
4163 N NH2 . ARG C 147 ? 1.7399 1.7068 1.5704 -0.0751 0.0586  -0.0820 147 ARG L NH2 
4164 N N   . GLU C 148 ? 2.0238 1.9987 1.8538 -0.0807 0.0656  -0.1368 148 GLU L N   
4165 C CA  . GLU C 148 ? 2.1881 2.1584 2.0275 -0.0791 0.0666  -0.1458 148 GLU L CA  
4166 C C   . GLU C 148 ? 2.4091 2.3889 2.2499 -0.0797 0.0718  -0.1549 148 GLU L C   
4167 O O   . GLU C 148 ? 2.5351 2.5248 2.3678 -0.0825 0.0736  -0.1588 148 GLU L O   
4168 C CB  . GLU C 148 ? 2.1786 2.1451 2.0162 -0.0802 0.0636  -0.1488 148 GLU L CB  
4169 C CG  . GLU C 148 ? 2.2466 2.2034 2.0843 -0.0793 0.0588  -0.1407 148 GLU L CG  
4170 C CD  . GLU C 148 ? 2.2535 2.2076 2.0890 -0.0807 0.0559  -0.1432 148 GLU L CD  
4171 O OE1 . GLU C 148 ? 2.1108 2.0710 1.9432 -0.0826 0.0574  -0.1505 148 GLU L OE1 
4172 O OE2 . GLU C 148 ? 2.3327 2.2789 2.1696 -0.0799 0.0521  -0.1379 148 GLU L OE2 
4173 N N   . ALA C 149 ? 2.3719 2.3493 2.2233 -0.0771 0.0740  -0.1584 149 ALA L N   
4174 C CA  . ALA C 149 ? 2.3820 2.3690 2.2357 -0.0772 0.0794  -0.1664 149 ALA L CA  
4175 C C   . ALA C 149 ? 2.1906 2.1710 2.0589 -0.0740 0.0805  -0.1724 149 ALA L C   
4176 O O   . ALA C 149 ? 2.1757 2.1469 2.0513 -0.0717 0.0782  -0.1666 149 ALA L O   
4177 C CB  . ALA C 149 ? 2.4253 2.4209 2.2738 -0.0782 0.0818  -0.1602 149 ALA L CB  
4178 N N   . LYS C 150 ? 2.1335 2.1186 2.0064 -0.0738 0.0838  -0.1839 150 LYS L N   
4179 C CA  . LYS C 150 ? 1.8577 1.8375 1.7458 -0.0706 0.0851  -0.1901 150 LYS L CA  
4180 C C   . LYS C 150 ? 1.8979 1.8890 1.7887 -0.0703 0.0913  -0.1977 150 LYS L C   
4181 O O   . LYS C 150 ? 2.2036 2.2049 2.0883 -0.0722 0.0945  -0.2055 150 LYS L O   
4182 C CB  . LYS C 150 ? 1.8337 1.8059 1.7287 -0.0699 0.0824  -0.1977 150 LYS L CB  
4183 C CG  . LYS C 150 ? 1.7056 1.6661 1.6005 -0.0699 0.0763  -0.1903 150 LYS L CG  
4184 C CD  . LYS C 150 ? 1.6489 1.6028 1.5509 -0.0696 0.0736  -0.1979 150 LYS L CD  
4185 C CE  . LYS C 150 ? 1.4363 1.3793 1.3384 -0.0699 0.0676  -0.1903 150 LYS L CE  
4186 N NZ  . LYS C 150 ? 1.3525 1.2896 1.2617 -0.0699 0.0645  -0.1971 150 LYS L NZ  
4187 N N   . VAL C 151 ? 1.8413 1.8311 1.7411 -0.0679 0.0930  -0.1953 151 VAL L N   
4188 C CA  . VAL C 151 ? 1.8699 1.8700 1.7743 -0.0672 0.0990  -0.2018 151 VAL L CA  
4189 C C   . VAL C 151 ? 1.9645 1.9577 1.8865 -0.0636 0.0994  -0.2086 151 VAL L C   
4190 O O   . VAL C 151 ? 2.1509 2.1328 2.0816 -0.0616 0.0960  -0.2027 151 VAL L O   
4191 C CB  . VAL C 151 ? 1.7517 1.7578 1.6519 -0.0677 0.1008  -0.1925 151 VAL L CB  
4192 C CG1 . VAL C 151 ? 1.4391 1.4558 1.3457 -0.0667 0.1070  -0.1992 151 VAL L CG1 
4193 C CG2 . VAL C 151 ? 1.7033 1.7172 1.5869 -0.0714 0.1001  -0.1860 151 VAL L CG2 
4194 N N   . GLN C 152 ? 2.1366 2.1366 2.0639 -0.0630 0.1036  -0.2212 152 GLN L N   
4195 C CA  . GLN C 152 ? 2.2627 2.2582 2.2076 -0.0596 0.1048  -0.2291 152 GLN L CA  
4196 C C   . GLN C 152 ? 1.9995 2.0076 1.9477 -0.0588 0.1117  -0.2342 152 GLN L C   
4197 O O   . GLN C 152 ? 2.1317 2.1529 2.0682 -0.0613 0.1156  -0.2342 152 GLN L O   
4198 C CB  . GLN C 152 ? 2.6429 2.6347 2.5935 -0.0591 0.1036  -0.2407 152 GLN L CB  
4199 C CG  . GLN C 152 ? 2.9455 2.9245 2.8946 -0.0598 0.0966  -0.2357 152 GLN L CG  
4200 C CD  . GLN C 152 ? 2.8880 2.8606 2.8477 -0.0586 0.0944  -0.2462 152 GLN L CD  
4201 O OE1 . GLN C 152 ? 2.7054 2.6658 2.6705 -0.0582 0.0886  -0.2425 152 GLN L OE1 
4202 N NE2 . GLN C 152 ? 2.7350 2.7160 2.6978 -0.0581 0.0988  -0.2592 152 GLN L NE2 
4203 N N   . TRP C 153 ? 2.0505 2.0551 2.0153 -0.0555 0.1130  -0.2383 153 TRP L N   
4204 C CA  . TRP C 153 ? 1.9278 1.9441 1.8983 -0.0543 0.1196  -0.2440 153 TRP L CA  
4205 C C   . TRP C 153 ? 2.0569 2.0708 2.0445 -0.0511 0.1212  -0.2571 153 TRP L C   
4206 O O   . TRP C 153 ? 2.0582 2.0588 2.0591 -0.0488 0.1168  -0.2562 153 TRP L O   
4207 C CB  . TRP C 153 ? 1.9936 2.0085 1.9681 -0.0533 0.1197  -0.2331 153 TRP L CB  
4208 C CG  . TRP C 153 ? 2.1045 2.1240 2.0634 -0.0562 0.1189  -0.2208 153 TRP L CG  
4209 C CD1 . TRP C 153 ? 2.0473 2.0574 1.9985 -0.0575 0.1131  -0.2095 153 TRP L CD1 
4210 C CD2 . TRP C 153 ? 2.1492 2.1833 2.1002 -0.0580 0.1238  -0.2181 153 TRP L CD2 
4211 N NE1 . TRP C 153 ? 2.0913 2.1088 2.0301 -0.0599 0.1139  -0.2004 153 TRP L NE1 
4212 C CE2 . TRP C 153 ? 2.0486 2.0808 1.9872 -0.0604 0.1202  -0.2050 153 TRP L CE2 
4213 C CE3 . TRP C 153 ? 2.1714 2.2203 2.1246 -0.0580 0.1307  -0.2255 153 TRP L CE3 
4214 C CZ2 . TRP C 153 ? 2.0394 2.0837 1.9683 -0.0629 0.1229  -0.1988 153 TRP L CZ2 
4215 C CZ3 . TRP C 153 ? 2.0226 2.0840 1.9658 -0.0605 0.1337  -0.2190 153 TRP L CZ3 
4216 C CH2 . TRP C 153 ? 1.8785 1.9374 1.8097 -0.0630 0.1296  -0.2056 153 TRP L CH2 
4217 N N   . LYS C 154 ? 2.1460 2.1726 2.1335 -0.0511 0.1272  -0.2694 154 LYS L N   
4218 C CA  . LYS C 154 ? 2.1004 2.1257 2.1042 -0.0480 0.1290  -0.2834 154 LYS L CA  
4219 C C   . LYS C 154 ? 2.0471 2.0857 2.0582 -0.0463 0.1366  -0.2903 154 LYS L C   
4220 O O   . LYS C 154 ? 2.2277 2.2806 2.2319 -0.0476 0.1424  -0.2995 154 LYS L O   
4221 C CB  . LYS C 154 ? 1.9256 1.9523 1.9242 -0.0493 0.1285  -0.2945 154 LYS L CB  
4222 C CG  . LYS C 154 ? 2.1201 2.1326 2.1159 -0.0503 0.1208  -0.2892 154 LYS L CG  
4223 C CD  . LYS C 154 ? 1.9602 1.9743 1.9514 -0.0516 0.1203  -0.3004 154 LYS L CD  
4224 C CE  . LYS C 154 ? 2.3367 2.3367 2.3263 -0.0526 0.1124  -0.2948 154 LYS L CE  
4225 N NZ  . LYS C 154 ? 2.2212 2.2219 2.2060 -0.0541 0.1111  -0.3045 154 LYS L NZ  
4226 N N   . VAL C 155 ? 2.0453 2.0790 2.0709 -0.0435 0.1365  -0.2861 155 VAL L N   
4227 C CA  . VAL C 155 ? 1.9463 1.9918 1.9810 -0.0415 0.1434  -0.2920 155 VAL L CA  
4228 C C   . VAL C 155 ? 2.0900 2.1346 2.1422 -0.0380 0.1454  -0.3077 155 VAL L C   
4229 O O   . VAL C 155 ? 2.2347 2.2651 2.3016 -0.0356 0.1403  -0.3087 155 VAL L O   
4230 C CB  . VAL C 155 ? 1.7912 1.8321 1.8338 -0.0401 0.1423  -0.2802 155 VAL L CB  
4231 C CG1 . VAL C 155 ? 1.6834 1.7360 1.7373 -0.0378 0.1493  -0.2865 155 VAL L CG1 
4232 C CG2 . VAL C 155 ? 2.0886 2.1307 2.1139 -0.0435 0.1402  -0.2652 155 VAL L CG2 
4233 N N   . ASP C 156 ? 1.9486 2.0087 1.9998 -0.0378 0.1528  -0.3201 156 ASP L N   
4234 C CA  . ASP C 156 ? 1.9031 1.9646 1.9661 -0.0353 0.1550  -0.3373 156 ASP L CA  
4235 C C   . ASP C 156 ? 2.2822 2.3296 2.3464 -0.0355 0.1479  -0.3399 156 ASP L C   
4236 O O   . ASP C 156 ? 2.4908 2.5278 2.5728 -0.0324 0.1448  -0.3463 156 ASP L O   
4237 C CB  . ASP C 156 ? 1.9549 2.0151 2.0415 -0.0307 0.1573  -0.3437 156 ASP L CB  
4238 C CG  . ASP C 156 ? 2.0914 2.1689 2.1786 -0.0301 0.1659  -0.3463 156 ASP L CG  
4239 O OD1 . ASP C 156 ? 2.2374 2.3294 2.3070 -0.0334 0.1705  -0.3460 156 ASP L OD1 
4240 O OD2 . ASP C 156 ? 1.9683 2.0458 2.0744 -0.0265 0.1681  -0.3498 156 ASP L OD2 
4241 N N   . ASN C 157 ? 2.3210 2.3683 2.3661 -0.0394 0.1453  -0.3345 157 ASN L N   
4242 C CA  . ASN C 157 ? 2.2805 2.3164 2.3235 -0.0402 0.1390  -0.3368 157 ASN L CA  
4243 C C   . ASN C 157 ? 2.3694 2.3866 2.4261 -0.0383 0.1312  -0.3291 157 ASN L C   
4244 O O   . ASN C 157 ? 2.3224 2.3292 2.3860 -0.0377 0.1262  -0.3339 157 ASN L O   
4245 C CB  . ASN C 157 ? 2.2084 2.2491 2.2573 -0.0389 0.1408  -0.3528 157 ASN L CB  
4246 C CG  . ASN C 157 ? 2.3816 2.4367 2.4114 -0.0423 0.1439  -0.3549 157 ASN L CG  
4247 O OD1 . ASN C 157 ? 2.4127 2.4760 2.4256 -0.0458 0.1468  -0.3484 157 ASN L OD1 
4248 N ND2 . ASN C 157 ? 2.1103 2.1687 2.1430 -0.0416 0.1429  -0.3636 157 ASN L ND2 
4249 N N   . ALA C 158 ? 2.2788 2.2917 2.3398 -0.0376 0.1301  -0.3172 158 ALA L N   
4250 C CA  . ALA C 158 ? 2.3129 2.3088 2.3852 -0.0364 0.1227  -0.3082 158 ALA L CA  
4251 C C   . ALA C 158 ? 2.2757 2.2674 2.3328 -0.0392 0.1191  -0.2917 158 ALA L C   
4252 O O   . ALA C 158 ? 2.4066 2.4061 2.4556 -0.0402 0.1225  -0.2844 158 ALA L O   
4253 C CB  . ALA C 158 ? 2.3821 2.3754 2.4751 -0.0327 0.1239  -0.3088 158 ALA L CB  
4254 N N   . LEU C 159 ? 2.2323 2.2123 2.2855 -0.0407 0.1122  -0.2863 159 LEU L N   
4255 C CA  . LEU C 159 ? 2.0302 2.0044 2.0708 -0.0431 0.1081  -0.2709 159 LEU L CA  
4256 C C   . LEU C 159 ? 1.9871 1.9562 2.0356 -0.0417 0.1070  -0.2604 159 LEU L C   
4257 O O   . LEU C 159 ? 2.0984 2.0590 2.1647 -0.0393 0.1047  -0.2613 159 LEU L O   
4258 C CB  . LEU C 159 ? 1.9885 1.9500 2.0278 -0.0444 0.1007  -0.2679 159 LEU L CB  
4259 C CG  . LEU C 159 ? 1.9517 1.9174 1.9790 -0.0466 0.1007  -0.2749 159 LEU L CG  
4260 C CD1 . LEU C 159 ? 1.9533 1.9062 1.9833 -0.0474 0.0933  -0.2732 159 LEU L CD1 
4261 C CD2 . LEU C 159 ? 1.8579 1.8313 1.8644 -0.0497 0.1024  -0.2661 159 LEU L CD2 
4262 N N   . GLN C 160 ? 1.9770 1.9512 2.0123 -0.0435 0.1085  -0.2501 160 GLN L N   
4263 C CA  . GLN C 160 ? 1.9483 1.9183 1.9882 -0.0427 0.1074  -0.2390 160 GLN L CA  
4264 C C   . GLN C 160 ? 1.8896 1.8509 1.9181 -0.0449 0.1016  -0.2255 160 GLN L C   
4265 O O   . GLN C 160 ? 1.9145 1.8808 1.9259 -0.0475 0.1019  -0.2220 160 GLN L O   
4266 C CB  . GLN C 160 ? 1.8889 1.8731 1.9242 -0.0428 0.1140  -0.2383 160 GLN L CB  
4267 C CG  . GLN C 160 ? 1.9578 1.9550 1.9983 -0.0415 0.1210  -0.2527 160 GLN L CG  
4268 C CD  . GLN C 160 ? 2.1710 2.1655 2.2335 -0.0378 0.1224  -0.2592 160 GLN L CD  
4269 O OE1 . GLN C 160 ? 2.0786 2.0681 2.1501 -0.0365 0.1211  -0.2514 160 GLN L OE1 
4270 N NE2 . GLN C 160 ? 2.1902 2.1881 2.2620 -0.0361 0.1250  -0.2737 160 GLN L NE2 
4271 N N   . SER C 161 ? 1.6801 1.6285 1.7182 -0.0439 0.0964  -0.2180 161 SER L N   
4272 C CA  . SER C 161 ? 1.7352 1.6749 1.7638 -0.0457 0.0911  -0.2051 161 SER L CA  
4273 C C   . SER C 161 ? 1.9299 1.8638 1.9661 -0.0447 0.0894  -0.1955 161 SER L C   
4274 O O   . SER C 161 ? 2.0278 1.9591 2.0806 -0.0425 0.0899  -0.1987 161 SER L O   
4275 C CB  . SER C 161 ? 1.7528 1.6810 1.7835 -0.0464 0.0848  -0.2051 161 SER L CB  
4276 O OG  . SER C 161 ? 1.8714 1.7904 1.9211 -0.0445 0.0818  -0.2079 161 SER L OG  
4277 N N   . GLY C 162 ? 1.9362 1.8682 1.9606 -0.0462 0.0873  -0.1838 162 GLY L N   
4278 C CA  . GLY C 162 ? 1.9447 1.8718 1.9740 -0.0456 0.0857  -0.1741 162 GLY L CA  
4279 C C   . GLY C 162 ? 1.8248 1.7635 1.8491 -0.0456 0.0910  -0.1720 162 GLY L C   
4280 O O   . GLY C 162 ? 1.8003 1.7378 1.8185 -0.0463 0.0896  -0.1615 162 GLY L O   
4295 N N   . GLN C 165 ? 1.9685 1.9442 1.9221 -0.0556 0.0970  -0.1546 165 GLN L N   
4296 C CA  . GLN C 165 ? 1.8533 1.8236 1.7977 -0.0568 0.0925  -0.1424 165 GLN L CA  
4297 C C   . GLN C 165 ? 1.8881 1.8674 1.8164 -0.0598 0.0932  -0.1410 165 GLN L C   
4298 O O   . GLN C 165 ? 2.1993 2.1922 2.1232 -0.0612 0.0978  -0.1449 165 GLN L O   
4299 C CB  . GLN C 165 ? 2.1905 2.1611 2.1387 -0.0561 0.0926  -0.1341 165 GLN L CB  
4300 C CG  . GLN C 165 ? 2.3707 2.3320 2.3349 -0.0535 0.0915  -0.1341 165 GLN L CG  
4301 C CD  . GLN C 165 ? 2.2772 2.2469 2.2530 -0.0520 0.0971  -0.1430 165 GLN L CD  
4302 O OE1 . GLN C 165 ? 2.3857 2.3692 2.3568 -0.0530 0.1022  -0.1477 165 GLN L OE1 
4303 N NE2 . GLN C 165 ? 1.9302 1.8919 1.9216 -0.0496 0.0961  -0.1453 165 GLN L NE2 
4304 N N   . GLU C 166 ? 1.7702 1.7424 1.6900 -0.0608 0.0885  -0.1355 166 GLU L N   
4305 C CA  . GLU C 166 ? 1.7707 1.7501 1.6761 -0.0637 0.0882  -0.1341 166 GLU L CA  
4306 C C   . GLU C 166 ? 1.7010 1.6766 1.5981 -0.0646 0.0841  -0.1219 166 GLU L C   
4307 O O   . GLU C 166 ? 1.6556 1.6192 1.5559 -0.0632 0.0797  -0.1160 166 GLU L O   
4308 C CB  . GLU C 166 ? 1.7278 1.7031 1.6305 -0.0642 0.0865  -0.1402 166 GLU L CB  
4309 C CG  . GLU C 166 ? 1.7032 1.6752 1.6180 -0.0622 0.0882  -0.1509 166 GLU L CG  
4310 C CD  . GLU C 166 ? 1.9517 1.9225 1.8630 -0.0632 0.0871  -0.1579 166 GLU L CD  
4311 O OE1 . GLU C 166 ? 2.0607 2.0266 1.9639 -0.0644 0.0831  -0.1527 166 GLU L OE1 
4312 O OE2 . GLU C 166 ? 2.1374 2.1120 2.0546 -0.0626 0.0901  -0.1687 166 GLU L OE2 
4313 N N   . SER C 167 ? 1.7535 1.7398 1.6404 -0.0671 0.0853  -0.1182 167 SER L N   
4314 C CA  . SER C 167 ? 1.6554 1.6398 1.5342 -0.0683 0.0814  -0.1070 167 SER L CA  
4315 C C   . SER C 167 ? 1.7121 1.7038 1.5780 -0.0714 0.0808  -0.1066 167 SER L C   
4316 O O   . SER C 167 ? 1.9945 1.9975 1.8566 -0.0734 0.0847  -0.1132 167 SER L O   
4317 C CB  . SER C 167 ? 1.6618 1.6521 1.5421 -0.0686 0.0827  -0.1006 167 SER L CB  
4318 O OG  . SER C 167 ? 1.7891 1.7945 1.6669 -0.0705 0.0879  -0.1053 167 SER L OG  
4319 N N   . VAL C 168 ? 1.6899 1.6756 1.5495 -0.0719 0.0760  -0.0987 168 VAL L N   
4320 C CA  . VAL C 168 ? 1.7290 1.7178 1.5783 -0.0743 0.0743  -0.0987 168 VAL L CA  
4321 C C   . VAL C 168 ? 1.8530 1.8442 1.6945 -0.0760 0.0710  -0.0883 168 VAL L C   
4322 O O   . VAL C 168 ? 1.8458 1.8282 1.6894 -0.0744 0.0674  -0.0808 168 VAL L O   
4323 C CB  . VAL C 168 ? 1.9263 1.9035 1.7768 -0.0729 0.0710  -0.1006 168 VAL L CB  
4324 C CG1 . VAL C 168 ? 1.9331 1.9138 1.7733 -0.0754 0.0692  -0.1003 168 VAL L CG1 
4325 C CG2 . VAL C 168 ? 1.8755 1.8480 1.7359 -0.0709 0.0730  -0.1097 168 VAL L CG2 
4326 N N   . THR C 169 ? 1.9550 1.9576 1.7874 -0.0795 0.0719  -0.0877 169 THR L N   
4327 C CA  . THR C 169 ? 1.8639 1.8687 1.6891 -0.0814 0.0681  -0.0779 169 THR L CA  
4328 C C   . THR C 169 ? 1.8904 1.8895 1.7097 -0.0819 0.0639  -0.0759 169 THR L C   
4329 O O   . THR C 169 ? 1.8965 1.8924 1.7159 -0.0814 0.0644  -0.0824 169 THR L O   
4330 C CB  . THR C 169 ? 1.8645 1.8850 1.6833 -0.0853 0.0705  -0.0768 169 THR L CB  
4331 O OG1 . THR C 169 ? 2.1750 2.2034 1.9885 -0.0877 0.0732  -0.0848 169 THR L OG1 
4332 C CG2 . THR C 169 ? 2.0422 2.0690 1.8667 -0.0849 0.0743  -0.0772 169 THR L CG2 
4333 N N   . GLU C 170 ? 1.8731 1.8715 1.6877 -0.0828 0.0598  -0.0667 170 GLU L N   
4334 C CA  . GLU C 170 ? 1.8904 1.8842 1.6999 -0.0832 0.0556  -0.0636 170 GLU L CA  
4335 C C   . GLU C 170 ? 1.8900 1.8945 1.6913 -0.0871 0.0564  -0.0664 170 GLU L C   
4336 O O   . GLU C 170 ? 1.9459 1.9619 1.7447 -0.0897 0.0601  -0.0699 170 GLU L O   
4337 C CB  . GLU C 170 ? 2.2048 2.1946 2.0131 -0.0828 0.0507  -0.0531 170 GLU L CB  
4338 C CG  . GLU C 170 ? 2.6099 2.5879 2.4253 -0.0791 0.0490  -0.0499 170 GLU L CG  
4339 C CD  . GLU C 170 ? 3.2485 3.2231 3.0626 -0.0787 0.0442  -0.0400 170 GLU L CD  
4340 O OE1 . GLU C 170 ? 3.3534 3.3358 3.1620 -0.0815 0.0424  -0.0353 170 GLU L OE1 
4341 O OE2 . GLU C 170 ? 3.4787 3.4431 3.2976 -0.0758 0.0421  -0.0368 170 GLU L OE2 
4342 N N   . GLN C 171 ? 1.8179 1.8188 1.6150 -0.0876 0.0530  -0.0647 171 GLN L N   
4343 C CA  . GLN C 171 ? 1.9513 1.9618 1.7402 -0.0916 0.0526  -0.0652 171 GLN L CA  
4344 C C   . GLN C 171 ? 2.1283 2.1486 1.9126 -0.0949 0.0513  -0.0578 171 GLN L C   
4345 O O   . GLN C 171 ? 2.1224 2.1388 1.9078 -0.0940 0.0475  -0.0492 171 GLN L O   
4346 C CB  . GLN C 171 ? 1.7134 1.7174 1.4996 -0.0913 0.0486  -0.0634 171 GLN L CB  
4347 C CG  . GLN C 171 ? 1.9539 1.9502 1.7435 -0.0891 0.0497  -0.0709 171 GLN L CG  
4348 C CD  . GLN C 171 ? 2.1725 2.1626 1.9599 -0.0887 0.0458  -0.0686 171 GLN L CD  
4349 O OE1 . GLN C 171 ? 2.2702 2.2579 2.0560 -0.0885 0.0420  -0.0610 171 GLN L OE1 
4350 N NE2 . GLN C 171 ? 2.1492 2.1369 1.9370 -0.0886 0.0467  -0.0754 171 GLN L NE2 
4351 N N   . ASP C 172 ? 2.1520 2.1854 1.9314 -0.0987 0.0544  -0.0610 172 ASP L N   
4352 C CA  . ASP C 172 ? 2.0953 2.1395 1.8696 -0.1027 0.0529  -0.0536 172 ASP L CA  
4353 C C   . ASP C 172 ? 1.9760 2.0187 1.7457 -0.1045 0.0472  -0.0468 172 ASP L C   
4354 O O   . ASP C 172 ? 1.8535 1.8946 1.6199 -0.1051 0.0464  -0.0503 172 ASP L O   
4355 C CB  . ASP C 172 ? 2.2191 2.2783 1.9882 -0.1070 0.0574  -0.0592 172 ASP L CB  
4356 C CG  . ASP C 172 ? 2.4228 2.4848 2.1972 -0.1053 0.0631  -0.0659 172 ASP L CG  
4357 O OD1 . ASP C 172 ? 2.3384 2.3909 2.1207 -0.1011 0.0632  -0.0652 172 ASP L OD1 
4358 O OD2 . ASP C 172 ? 2.3298 2.4036 2.1007 -0.1082 0.0675  -0.0721 172 ASP L OD2 
4359 N N   . SER C 173 ? 1.9659 2.0088 1.7360 -0.1051 0.0431  -0.0369 173 SER L N   
4360 C CA  . SER C 173 ? 2.0951 2.1353 1.8626 -0.1060 0.0373  -0.0300 173 SER L CA  
4361 C C   . SER C 173 ? 2.3132 2.3646 2.0729 -0.1113 0.0368  -0.0303 173 SER L C   
4362 O O   . SER C 173 ? 2.4479 2.4961 2.2053 -0.1117 0.0337  -0.0296 173 SER L O   
4363 C CB  . SER C 173 ? 2.0337 2.0727 1.8039 -0.1058 0.0329  -0.0196 173 SER L CB  
4364 O OG  . SER C 173 ? 2.1311 2.1831 1.8985 -0.1101 0.0338  -0.0159 173 SER L OG  
4365 N N   . LYS C 174 ? 2.3612 2.4261 2.1167 -0.1156 0.0396  -0.0312 174 LYS L N   
4366 C CA  . LYS C 174 ? 2.2428 2.3195 1.9902 -0.1213 0.0395  -0.0318 174 LYS L CA  
4367 C C   . LYS C 174 ? 2.2824 2.3556 2.0274 -0.1207 0.0410  -0.0403 174 LYS L C   
4368 O O   . LYS C 174 ? 2.4189 2.4897 2.1614 -0.1218 0.0372  -0.0378 174 LYS L O   
4369 C CB  . LYS C 174 ? 2.3053 2.3968 2.0490 -0.1254 0.0439  -0.0341 174 LYS L CB  
4370 C CG  . LYS C 174 ? 2.3250 2.4226 2.0701 -0.1273 0.0419  -0.0247 174 LYS L CG  
4371 C CD  . LYS C 174 ? 2.4089 2.5222 2.1503 -0.1314 0.0469  -0.0276 174 LYS L CD  
4372 C CE  . LYS C 174 ? 2.8705 2.9904 2.6135 -0.1336 0.0445  -0.0175 174 LYS L CE  
4373 N NZ  . LYS C 174 ? 3.3091 3.4451 3.0485 -0.1377 0.0497  -0.0202 174 LYS L NZ  
4374 N N   . ASP C 175 ? 2.2142 2.2870 1.9607 -0.1190 0.0465  -0.0503 175 ASP L N   
4375 C CA  . ASP C 175 ? 2.2363 2.3038 1.9823 -0.1176 0.0481  -0.0590 175 ASP L CA  
4376 C C   . ASP C 175 ? 2.2914 2.3482 2.0454 -0.1120 0.0510  -0.0650 175 ASP L C   
4377 O O   . ASP C 175 ? 2.3856 2.4451 2.1430 -0.1110 0.0549  -0.0677 175 ASP L O   
4378 C CB  . ASP C 175 ? 2.1737 2.2533 1.9127 -0.1221 0.0518  -0.0666 175 ASP L CB  
4379 C CG  . ASP C 175 ? 2.4866 2.5757 2.2173 -0.1279 0.0484  -0.0613 175 ASP L CG  
4380 O OD1 . ASP C 175 ? 2.4698 2.5544 2.2008 -0.1280 0.0429  -0.0528 175 ASP L OD1 
4381 O OD2 . ASP C 175 ? 2.5669 2.6682 2.2909 -0.1326 0.0511  -0.0656 175 ASP L OD2 
4382 N N   . SER C 176 ? 1.9773 2.0222 1.7347 -0.1087 0.0490  -0.0666 176 SER L N   
4383 C CA  . SER C 176 ? 2.0458 2.0801 1.8108 -0.1038 0.0512  -0.0722 176 SER L CA  
4384 C C   . SER C 176 ? 2.0774 2.1170 1.8435 -0.1041 0.0569  -0.0825 176 SER L C   
4385 O O   . SER C 176 ? 2.2462 2.2872 2.0099 -0.1053 0.0583  -0.0900 176 SER L O   
4386 C CB  . SER C 176 ? 2.1577 2.1813 1.9244 -0.1015 0.0484  -0.0732 176 SER L CB  
4387 O OG  . SER C 176 ? 2.4285 2.4567 2.1901 -0.1043 0.0490  -0.0789 176 SER L OG  
4388 N N   . THR C 177 ? 2.0210 2.0637 1.7911 -0.1031 0.0601  -0.0831 177 THR L N   
4389 C CA  . THR C 177 ? 2.1821 2.2317 1.9535 -0.1035 0.0659  -0.0928 177 THR L CA  
4390 C C   . THR C 177 ? 2.2149 2.2587 1.9957 -0.0995 0.0681  -0.0935 177 THR L C   
4391 O O   . THR C 177 ? 2.2116 2.2611 1.9933 -0.1000 0.0694  -0.0893 177 THR L O   
4392 C CB  . THR C 177 ? 2.1775 2.2434 1.9413 -0.1087 0.0681  -0.0925 177 THR L CB  
4393 O OG1 . THR C 177 ? 2.1164 2.1859 1.8788 -0.1100 0.0656  -0.0818 177 THR L OG1 
4394 C CG2 . THR C 177 ? 2.2100 2.2820 1.9648 -0.1129 0.0668  -0.0947 177 THR L CG2 
4395 N N   . TYR C 178 ? 2.0659 2.0985 1.8539 -0.0956 0.0684  -0.0987 178 TYR L N   
4396 C CA  . TYR C 178 ? 2.0304 2.0567 1.8281 -0.0918 0.0703  -0.0999 178 TYR L CA  
4397 C C   . TYR C 178 ? 2.1292 2.1658 1.9290 -0.0926 0.0761  -0.1066 178 TYR L C   
4398 O O   . TYR C 178 ? 2.3187 2.3658 2.1134 -0.0955 0.0791  -0.1130 178 TYR L O   
4399 C CB  . TYR C 178 ? 2.1067 2.1202 1.9116 -0.0882 0.0694  -0.1049 178 TYR L CB  
4400 C CG  . TYR C 178 ? 2.0922 2.0940 1.8972 -0.0865 0.0642  -0.0981 178 TYR L CG  
4401 C CD1 . TYR C 178 ? 2.0482 2.0432 1.8566 -0.0843 0.0616  -0.0900 178 TYR L CD1 
4402 C CD2 . TYR C 178 ? 2.1373 2.1354 1.9393 -0.0870 0.0618  -0.1002 178 TYR L CD2 
4403 C CE1 . TYR C 178 ? 2.0300 2.0149 1.8386 -0.0827 0.0571  -0.0845 178 TYR L CE1 
4404 C CE2 . TYR C 178 ? 2.0367 2.0250 1.8391 -0.0854 0.0574  -0.0944 178 TYR L CE2 
4405 C CZ  . TYR C 178 ? 2.0754 2.0572 1.8810 -0.0832 0.0552  -0.0868 178 TYR L CZ  
4406 O OH  . TYR C 178 ? 2.2181 2.1908 2.0239 -0.0816 0.0510  -0.0815 178 TYR L OH  
4407 N N   . SER C 179 ? 2.0278 2.0616 1.8357 -0.0899 0.0776  -0.1052 179 SER L N   
4408 C CA  . SER C 179 ? 1.9207 1.9635 1.7325 -0.0900 0.0833  -0.1117 179 SER L CA  
4409 C C   . SER C 179 ? 2.0006 2.0337 1.8248 -0.0855 0.0843  -0.1138 179 SER L C   
4410 O O   . SER C 179 ? 2.0747 2.0969 1.9030 -0.0831 0.0807  -0.1069 179 SER L O   
4411 C CB  . SER C 179 ? 1.8495 1.9052 1.6565 -0.0931 0.0846  -0.1056 179 SER L CB  
4412 O OG  . SER C 179 ? 2.1838 2.2336 1.9938 -0.0916 0.0813  -0.0952 179 SER L OG  
4413 N N   . LEU C 180 ? 2.0939 2.1317 1.9241 -0.0845 0.0894  -0.1235 180 LEU L N   
4414 C CA  . LEU C 180 ? 1.8943 1.9234 1.7372 -0.0805 0.0907  -0.1280 180 LEU L CA  
4415 C C   . LEU C 180 ? 1.7216 1.7607 1.5700 -0.0802 0.0962  -0.1321 180 LEU L C   
4416 O O   . LEU C 180 ? 1.7566 1.8095 1.5998 -0.0829 0.1003  -0.1372 180 LEU L O   
4417 C CB  . LEU C 180 ? 1.9817 2.0048 1.8286 -0.0791 0.0910  -0.1381 180 LEU L CB  
4418 C CG  . LEU C 180 ? 2.3959 2.4089 2.2390 -0.0791 0.0859  -0.1354 180 LEU L CG  
4419 C CD1 . LEU C 180 ? 2.7363 2.7451 2.5833 -0.0783 0.0864  -0.1458 180 LEU L CD1 
4420 C CD2 . LEU C 180 ? 2.1823 2.1826 2.0295 -0.0767 0.0814  -0.1264 180 LEU L CD2 
4421 N N   . SER C 181 ? 1.7434 1.7756 1.6026 -0.0770 0.0964  -0.1303 181 SER L N   
4422 C CA  . SER C 181 ? 1.8285 1.8690 1.6952 -0.0762 0.1016  -0.1343 181 SER L CA  
4423 C C   . SER C 181 ? 1.8665 1.8962 1.7477 -0.0720 0.1020  -0.1394 181 SER L C   
4424 O O   . SER C 181 ? 1.8635 1.8855 1.7520 -0.0698 0.1000  -0.1332 181 SER L O   
4425 C CB  . SER C 181 ? 1.8880 1.9339 1.7527 -0.0773 0.1012  -0.1240 181 SER L CB  
4426 O OG  . SER C 181 ? 1.9693 2.0020 1.8391 -0.0749 0.0966  -0.1153 181 SER L OG  
4427 N N   . SER C 182 ? 1.8060 1.8352 1.6916 -0.0710 0.1041  -0.1507 182 SER L N   
4428 C CA  . SER C 182 ? 1.8550 1.8741 1.7551 -0.0673 0.1041  -0.1561 182 SER L CA  
4429 C C   . SER C 182 ? 1.8778 1.9050 1.7878 -0.0658 0.1096  -0.1613 182 SER L C   
4430 O O   . SER C 182 ? 2.0387 2.0787 1.9468 -0.0670 0.1148  -0.1698 182 SER L O   
4431 C CB  . SER C 182 ? 1.9538 1.9685 1.8554 -0.0669 0.1035  -0.1659 182 SER L CB  
4432 O OG  . SER C 182 ? 1.9569 1.9631 1.8735 -0.0635 0.1036  -0.1718 182 SER L OG  
4433 N N   . THR C 183 ? 1.7135 1.7336 1.6340 -0.0634 0.1085  -0.1563 183 THR L N   
4434 C CA  . THR C 183 ? 1.6373 1.6648 1.5677 -0.0619 0.1133  -0.1594 183 THR L CA  
4435 C C   . THR C 183 ? 1.8512 1.8696 1.7982 -0.0583 0.1135  -0.1664 183 THR L C   
4436 O O   . THR C 183 ? 2.1496 2.1535 2.1017 -0.0568 0.1085  -0.1634 183 THR L O   
4437 C CB  . THR C 183 ? 1.6711 1.6988 1.6009 -0.0622 0.1119  -0.1473 183 THR L CB  
4438 O OG1 . THR C 183 ? 1.8323 1.8438 1.7667 -0.0605 0.1060  -0.1396 183 THR L OG1 
4439 C CG2 . THR C 183 ? 1.6896 1.7262 1.6038 -0.0660 0.1111  -0.1400 183 THR L CG2 
4440 N N   . LEU C 184 ? 1.9066 1.9339 1.8626 -0.0570 0.1192  -0.1760 184 LEU L N   
4441 C CA  . LEU C 184 ? 1.9172 1.9373 1.8913 -0.0534 0.1197  -0.1812 184 LEU L CA  
4442 C C   . LEU C 184 ? 1.9754 2.0017 1.9576 -0.0523 0.1229  -0.1777 184 LEU L C   
4443 O O   . LEU C 184 ? 1.9427 1.9842 1.9200 -0.0538 0.1282  -0.1794 184 LEU L O   
4444 C CB  . LEU C 184 ? 1.8144 1.8387 1.7962 -0.0519 0.1236  -0.1963 184 LEU L CB  
4445 C CG  . LEU C 184 ? 1.9785 1.9985 1.9589 -0.0520 0.1221  -0.2054 184 LEU L CG  
4446 C CD1 . LEU C 184 ? 1.9421 1.9713 1.9324 -0.0503 0.1281  -0.2199 184 LEU L CD1 
4447 C CD2 . LEU C 184 ? 1.8440 1.8463 1.8326 -0.0503 0.1156  -0.2027 184 LEU L CD2 
4448 N N   . THR C 185 ? 2.1297 2.1447 2.1248 -0.0498 0.1200  -0.1732 185 THR L N   
4449 C CA  . THR C 185 ? 2.1288 2.1479 2.1347 -0.0483 0.1227  -0.1705 185 THR L CA  
4450 C C   . THR C 185 ? 2.1810 2.1947 2.2063 -0.0448 0.1238  -0.1791 185 THR L C   
4451 O O   . THR C 185 ? 2.1213 2.1211 2.1536 -0.0435 0.1191  -0.1797 185 THR L O   
4452 C CB  . THR C 185 ? 2.2387 2.2489 2.2429 -0.0487 0.1176  -0.1559 185 THR L CB  
4453 O OG1 . THR C 185 ? 2.4569 2.4498 2.4661 -0.0475 0.1114  -0.1528 185 THR L OG1 
4454 C CG2 . THR C 185 ? 2.2884 2.3040 2.2745 -0.0521 0.1162  -0.1472 185 THR L CG2 
4455 N N   . LEU C 186 ? 2.1495 2.1746 2.1842 -0.0435 0.1299  -0.1853 186 LEU L N   
4456 C CA  . LEU C 186 ? 1.9536 1.9757 2.0081 -0.0400 0.1317  -0.1941 186 LEU L CA  
4457 C C   . LEU C 186 ? 1.9639 1.9948 2.0283 -0.0388 0.1360  -0.1921 186 LEU L C   
4458 O O   . LEU C 186 ? 1.9524 1.9930 2.0075 -0.0409 0.1382  -0.1851 186 LEU L O   
4459 C CB  . LEU C 186 ? 1.8235 1.8524 1.8805 -0.0392 0.1359  -0.2098 186 LEU L CB  
4460 C CG  . LEU C 186 ? 1.8985 1.9179 1.9491 -0.0400 0.1315  -0.2133 186 LEU L CG  
4461 C CD1 . LEU C 186 ? 1.9727 2.0006 2.0240 -0.0395 0.1360  -0.2287 186 LEU L CD1 
4462 C CD2 . LEU C 186 ? 1.8969 1.8985 1.9612 -0.0379 0.1252  -0.2102 186 LEU L CD2 
4463 N N   . SER C 187 ? 1.9619 1.9890 2.0459 -0.0356 0.1371  -0.1981 187 SER L N   
4464 C CA  . SER C 187 ? 1.7489 1.7851 1.8445 -0.0341 0.1418  -0.1980 187 SER L CA  
4465 C C   . SER C 187 ? 1.8558 1.9114 1.9499 -0.0340 0.1504  -0.2100 187 SER L C   
4466 O O   . SER C 187 ? 2.0404 2.0998 2.1298 -0.0342 0.1525  -0.2209 187 SER L O   
4467 C CB  . SER C 187 ? 1.5295 1.5548 1.6475 -0.0306 0.1396  -0.2001 187 SER L CB  
4468 O OG  . SER C 187 ? 2.0296 2.0534 2.1581 -0.0284 0.1410  -0.2140 187 SER L OG  
4469 N N   . LYS C 188 ? 1.9243 1.9924 2.0223 -0.0339 0.1555  -0.2080 188 LYS L N   
4470 C CA  . LYS C 188 ? 1.8998 1.9871 1.9991 -0.0336 0.1642  -0.2199 188 LYS L CA  
4471 C C   . LYS C 188 ? 1.9420 2.0277 2.0567 -0.0301 0.1667  -0.2356 188 LYS L C   
4472 O O   . LYS C 188 ? 1.9423 2.0398 2.0530 -0.0303 0.1722  -0.2480 188 LYS L O   
4473 C CB  . LYS C 188 ? 1.7630 1.8625 1.8698 -0.0331 0.1690  -0.2159 188 LYS L CB  
4474 C CG  . LYS C 188 ? 1.5373 1.6437 1.6302 -0.0367 0.1684  -0.2023 188 LYS L CG  
4475 C CD  . LYS C 188 ? 1.6822 1.8003 1.7870 -0.0355 0.1736  -0.2009 188 LYS L CD  
4476 C CE  . LYS C 188 ? 2.1350 2.2617 2.2278 -0.0391 0.1733  -0.1874 188 LYS L CE  
4477 N NZ  . LYS C 188 ? 1.9393 2.0779 2.0437 -0.0382 0.1782  -0.1855 188 LYS L NZ  
4478 N N   . ALA C 189 ? 2.0411 2.1129 2.1744 -0.0269 0.1629  -0.2353 189 ALA L N   
4479 C CA  . ALA C 189 ? 1.9927 2.0611 2.1428 -0.0234 0.1641  -0.2496 189 ALA L CA  
4480 C C   . ALA C 189 ? 2.2863 2.3540 2.4259 -0.0244 0.1637  -0.2591 189 ALA L C   
4481 O O   . ALA C 189 ? 2.4590 2.5385 2.5998 -0.0236 0.1697  -0.2730 189 ALA L O   
4482 C CB  . ALA C 189 ? 1.6216 1.6715 1.7897 -0.0209 0.1574  -0.2449 189 ALA L CB  
4483 N N   . ASP C 190 ? 2.1920 2.2467 2.3204 -0.0265 0.1567  -0.2515 190 ASP L N   
4484 C CA  . ASP C 190 ? 2.2807 2.3334 2.3992 -0.0276 0.1554  -0.2593 190 ASP L CA  
4485 C C   . ASP C 190 ? 2.3485 2.4193 2.4502 -0.0302 0.1618  -0.2654 190 ASP L C   
4486 O O   . ASP C 190 ? 2.4501 2.5254 2.5497 -0.0300 0.1643  -0.2781 190 ASP L O   
4487 C CB  . ASP C 190 ? 2.1974 2.2345 2.3053 -0.0298 0.1470  -0.2481 190 ASP L CB  
4488 C CG  . ASP C 190 ? 2.2881 2.3069 2.4124 -0.0276 0.1402  -0.2446 190 ASP L CG  
4489 O OD1 . ASP C 190 ? 2.2676 2.2848 2.4116 -0.0244 0.1416  -0.2530 190 ASP L OD1 
4490 O OD2 . ASP C 190 ? 2.3284 2.3347 2.4459 -0.0292 0.1335  -0.2335 190 ASP L OD2 
4491 N N   . TYR C 191 ? 2.3145 2.3959 2.4039 -0.0329 0.1643  -0.2562 191 TYR L N   
4492 C CA  . TYR C 191 ? 2.2966 2.3960 2.3697 -0.0360 0.1702  -0.2607 191 TYR L CA  
4493 C C   . TYR C 191 ? 2.4743 2.5889 2.5568 -0.0339 0.1786  -0.2763 191 TYR L C   
4494 O O   . TYR C 191 ? 2.6540 2.7795 2.7271 -0.0355 0.1827  -0.2865 191 TYR L O   
4495 C CB  . TYR C 191 ? 2.0836 2.1911 2.1440 -0.0392 0.1707  -0.2470 191 TYR L CB  
4496 C CG  . TYR C 191 ? 2.0680 2.1923 2.1090 -0.0434 0.1749  -0.2485 191 TYR L CG  
4497 C CD1 . TYR C 191 ? 2.1391 2.2593 2.1625 -0.0467 0.1707  -0.2444 191 TYR L CD1 
4498 C CD2 . TYR C 191 ? 2.1075 2.2520 2.1477 -0.0443 0.1829  -0.2537 191 TYR L CD2 
4499 C CE1 . TYR C 191 ? 2.1922 2.3276 2.1980 -0.0509 0.1741  -0.2453 191 TYR L CE1 
4500 C CE2 . TYR C 191 ? 2.1815 2.3418 2.2036 -0.0487 0.1865  -0.2547 191 TYR L CE2 
4501 C CZ  . TYR C 191 ? 2.2645 2.4199 2.2696 -0.0520 0.1819  -0.2503 191 TYR L CZ  
4502 O OH  . TYR C 191 ? 2.2950 2.4659 2.2824 -0.0567 0.1850  -0.2508 191 TYR L OH  
4503 N N   . GLU C 192 ? 2.3818 2.4976 2.4832 -0.0305 0.1813  -0.2784 192 GLU L N   
4504 C CA  . GLU C 192 ? 2.2736 2.4034 2.3866 -0.0280 0.1893  -0.2938 192 GLU L CA  
4505 C C   . GLU C 192 ? 2.4321 2.5534 2.5577 -0.0247 0.1881  -0.3082 192 GLU L C   
4506 O O   . GLU C 192 ? 2.4118 2.5448 2.5410 -0.0235 0.1944  -0.3234 192 GLU L O   
4507 C CB  . GLU C 192 ? 2.0310 2.1648 2.1611 -0.0253 0.1923  -0.2907 192 GLU L CB  
4508 C CG  . GLU C 192 ? 2.0022 2.1481 2.1215 -0.0284 0.1949  -0.2785 192 GLU L CG  
4509 C CD  . GLU C 192 ? 2.1603 2.3088 2.2974 -0.0258 0.1972  -0.2746 192 GLU L CD  
4510 O OE1 . GLU C 192 ? 2.0125 2.1509 2.1702 -0.0216 0.1956  -0.2794 192 GLU L OE1 
4511 O OE2 . GLU C 192 ? 2.1893 2.3499 2.3203 -0.0280 0.2003  -0.2663 192 GLU L OE2 
4512 N N   . LYS C 193 ? 2.4091 2.5103 2.5415 -0.0235 0.1800  -0.3038 193 LYS L N   
4513 C CA  . LYS C 193 ? 2.2320 2.3236 2.3789 -0.0203 0.1779  -0.3162 193 LYS L CA  
4514 C C   . LYS C 193 ? 2.1965 2.2924 2.3299 -0.0222 0.1790  -0.3266 193 LYS L C   
4515 O O   . LYS C 193 ? 1.9547 2.0520 2.0983 -0.0197 0.1812  -0.3419 193 LYS L O   
4516 C CB  . LYS C 193 ? 2.1729 2.2423 2.3284 -0.0194 0.1684  -0.3069 193 LYS L CB  
4517 C CG  . LYS C 193 ? 2.2800 2.3428 2.4523 -0.0173 0.1665  -0.2981 193 LYS L CG  
4518 C CD  . LYS C 193 ? 2.2461 2.2874 2.4247 -0.0171 0.1568  -0.2887 193 LYS L CD  
4519 C CE  . LYS C 193 ? 2.1534 2.1878 2.3484 -0.0153 0.1544  -0.2797 193 LYS L CE  
4520 N NZ  . LYS C 193 ? 1.9908 2.0049 2.1910 -0.0156 0.1449  -0.2701 193 LYS L NZ  
4521 N N   . HIS C 194 ? 2.2296 2.3274 2.3405 -0.0265 0.1772  -0.3185 194 HIS L N   
4522 C CA  . HIS C 194 ? 2.1979 2.2956 2.2953 -0.0287 0.1759  -0.3252 194 HIS L CA  
4523 C C   . HIS C 194 ? 2.1160 2.2303 2.1909 -0.0332 0.1805  -0.3229 194 HIS L C   
4524 O O   . HIS C 194 ? 2.2430 2.3594 2.3069 -0.0359 0.1793  -0.3090 194 HIS L O   
4525 C CB  . HIS C 194 ? 2.0547 2.1327 2.1488 -0.0296 0.1664  -0.3162 194 HIS L CB  
4526 C CG  . HIS C 194 ? 2.0779 2.1396 2.1936 -0.0258 0.1613  -0.3182 194 HIS L CG  
4527 N ND1 . HIS C 194 ? 2.0684 2.1275 2.1980 -0.0230 0.1617  -0.3332 194 HIS L ND1 
4528 C CD2 . HIS C 194 ? 2.0038 2.0509 2.1297 -0.0247 0.1553  -0.3071 194 HIS L CD2 
4529 C CE1 . HIS C 194 ? 2.2091 2.2530 2.3572 -0.0203 0.1561  -0.3308 194 HIS L CE1 
4530 N NE2 . HIS C 194 ? 2.2227 2.2592 2.3685 -0.0214 0.1521  -0.3150 194 HIS L NE2 
4531 N N   . LYS C 195 ? 1.9086 2.0348 1.9770 -0.0341 0.1855  -0.3366 195 LYS L N   
4532 C CA  . LYS C 195 ? 1.9228 2.0666 1.9706 -0.0387 0.1903  -0.3357 195 LYS L CA  
4533 C C   . LYS C 195 ? 2.0793 2.2177 2.1073 -0.0429 0.1849  -0.3291 195 LYS L C   
4534 O O   . LYS C 195 ? 2.2888 2.4319 2.3011 -0.0468 0.1840  -0.3169 195 LYS L O   
4535 C CB  . LYS C 195 ? 2.0992 2.2601 2.1484 -0.0382 0.1986  -0.3536 195 LYS L CB  
4536 C CG  . LYS C 195 ? 2.0292 2.2005 2.0953 -0.0347 0.2055  -0.3599 195 LYS L CG  
4537 C CD  . LYS C 195 ? 1.7747 1.9608 1.8413 -0.0344 0.2097  -0.3716 195 LYS L CD  
4538 C CE  . LYS C 195 ? 1.5103 1.7073 1.5935 -0.0310 0.2161  -0.3771 195 LYS L CE  
4539 N NZ  . LYS C 195 ? 1.3113 1.5219 1.3945 -0.0309 0.2195  -0.3879 195 LYS L NZ  
4540 N N   . VAL C 196 ? 2.1717 2.3000 2.2007 -0.0423 0.1811  -0.3368 196 VAL L N   
4541 C CA  . VAL C 196 ? 2.1388 2.2635 2.1492 -0.0463 0.1767  -0.3323 196 VAL L CA  
4542 C C   . VAL C 196 ? 1.9940 2.1039 2.0003 -0.0472 0.1690  -0.3150 196 VAL L C   
4543 O O   . VAL C 196 ? 2.0307 2.1253 2.0511 -0.0441 0.1642  -0.3110 196 VAL L O   
4544 C CB  . VAL C 196 ? 2.2473 2.3649 2.2611 -0.0452 0.1745  -0.3454 196 VAL L CB  
4545 C CG1 . VAL C 196 ? 2.1464 2.2614 2.1408 -0.0495 0.1701  -0.3410 196 VAL L CG1 
4546 C CG2 . VAL C 196 ? 2.0561 2.1871 2.0757 -0.0437 0.1794  -0.3582 196 VAL L CG2 
4547 N N   . TYR C 197 ? 1.8162 1.9308 1.8033 -0.0517 0.1677  -0.3046 197 TYR L N   
4548 C CA  . TYR C 197 ? 1.7896 1.8914 1.7701 -0.0531 0.1605  -0.2888 197 TYR L CA  
4549 C C   . TYR C 197 ? 2.0892 2.1916 2.0510 -0.0573 0.1575  -0.2867 197 TYR L C   
4550 O O   . TYR C 197 ? 2.3023 2.4199 2.2510 -0.0607 0.1618  -0.2905 197 TYR L O   
4551 C CB  . TYR C 197 ? 1.9479 2.0552 1.9249 -0.0543 0.1615  -0.2755 197 TYR L CB  
4552 C CG  . TYR C 197 ? 2.0073 2.1178 2.0011 -0.0508 0.1655  -0.2772 197 TYR L CG  
4553 C CD1 . TYR C 197 ? 1.8312 1.9273 1.8437 -0.0465 0.1624  -0.2780 197 TYR L CD1 
4554 C CD2 . TYR C 197 ? 2.1393 2.2675 2.1305 -0.0521 0.1723  -0.2777 197 TYR L CD2 
4555 C CE1 . TYR C 197 ? 1.8805 1.9795 1.9089 -0.0434 0.1659  -0.2793 197 TYR L CE1 
4556 C CE2 . TYR C 197 ? 2.2110 2.3426 2.2178 -0.0489 0.1760  -0.2791 197 TYR L CE2 
4557 C CZ  . TYR C 197 ? 2.2226 2.3394 2.2481 -0.0445 0.1728  -0.2799 197 TYR L CZ  
4558 O OH  . TYR C 197 ? 2.3436 2.4641 2.3853 -0.0415 0.1764  -0.2811 197 TYR L OH  
4559 N N   . ALA C 198 ? 1.7944 1.8809 1.7549 -0.0572 0.1502  -0.2806 198 ALA L N   
4560 C CA  . ALA C 198 ? 1.9205 2.0069 1.8647 -0.0609 0.1472  -0.2795 198 ALA L CA  
4561 C C   . ALA C 198 ? 1.8392 1.9104 1.7794 -0.0615 0.1394  -0.2663 198 ALA L C   
4562 O O   . ALA C 198 ? 1.9000 1.9566 1.8525 -0.0585 0.1351  -0.2634 198 ALA L O   
4563 C CB  . ALA C 198 ? 1.9813 2.0668 1.9284 -0.0603 0.1477  -0.2944 198 ALA L CB  
4564 N N   . CYS C 199 ? 1.6796 1.7548 1.6024 -0.0656 0.1376  -0.2586 199 CYS L N   
4565 C CA  . CYS C 199 ? 1.6299 1.6931 1.5461 -0.0667 0.1306  -0.2464 199 CYS L CA  
4566 C C   . CYS C 199 ? 1.9142 1.9744 1.8218 -0.0688 0.1275  -0.2508 199 CYS L C   
4567 O O   . CYS C 199 ? 2.1278 2.1998 2.0236 -0.0721 0.1303  -0.2558 199 CYS L O   
4568 C CB  . CYS C 199 ? 1.8634 1.9334 1.7667 -0.0699 0.1303  -0.2335 199 CYS L CB  
4569 S SG  . CYS C 199 ? 2.2903 2.3631 2.2017 -0.0680 0.1327  -0.2258 199 CYS L SG  
4586 N N   . THR C 202 ? 2.0885 2.1083 1.9534 -0.0784 0.0979  -0.2202 202 THR L N   
4587 C CA  . THR C 202 ? 2.0564 2.0701 1.9169 -0.0799 0.0934  -0.2211 202 THR L CA  
4588 C C   . THR C 202 ? 2.3496 2.3597 2.2008 -0.0816 0.0890  -0.2081 202 THR L C   
4589 O O   . THR C 202 ? 2.3576 2.3600 2.2129 -0.0797 0.0866  -0.1990 202 THR L O   
4590 C CB  . THR C 202 ? 1.7233 1.7241 1.5976 -0.0768 0.0902  -0.2260 202 THR L CB  
4591 O OG1 . THR C 202 ? 1.8818 1.8723 1.7643 -0.0742 0.0876  -0.2174 202 THR L OG1 
4592 C CG2 . THR C 202 ? 1.6964 1.7005 1.5811 -0.0749 0.0943  -0.2396 202 THR L CG2 
4593 N N   . HIS C 203 ? 2.4092 2.4247 2.2480 -0.0853 0.0878  -0.2075 203 HIS L N   
4594 C CA  . HIS C 203 ? 2.1244 2.1382 1.9535 -0.0873 0.0838  -0.1959 203 HIS L CA  
4595 C C   . HIS C 203 ? 2.0046 2.0173 1.8268 -0.0899 0.0806  -0.1980 203 HIS L C   
4596 O O   . HIS C 203 ? 2.1360 2.1487 1.9607 -0.0901 0.0811  -0.2082 203 HIS L O   
4597 C CB  . HIS C 203 ? 2.2480 2.2739 2.0665 -0.0902 0.0862  -0.1899 203 HIS L CB  
4598 C CG  . HIS C 203 ? 2.6038 2.6322 2.4276 -0.0882 0.0893  -0.1869 203 HIS L CG  
4599 N ND1 . HIS C 203 ? 2.7454 2.7643 2.5754 -0.0855 0.0868  -0.1782 203 HIS L ND1 
4600 C CD2 . HIS C 203 ? 2.9988 3.0386 2.8225 -0.0888 0.0946  -0.1911 203 HIS L CD2 
4601 C CE1 . HIS C 203 ? 3.1869 3.2108 3.0207 -0.0844 0.0903  -0.1772 203 HIS L CE1 
4602 N NE2 . HIS C 203 ? 3.4048 3.4416 3.2351 -0.0864 0.0952  -0.1848 203 HIS L NE2 
4603 N N   . GLN C 204 ? 2.3062 2.3184 2.1194 -0.0920 0.0771  -0.1881 204 GLN L N   
4604 C CA  . GLN C 204 ? 2.5097 2.5217 2.3154 -0.0948 0.0738  -0.1883 204 GLN L CA  
4605 C C   . GLN C 204 ? 2.4870 2.5124 2.2824 -0.0990 0.0766  -0.1942 204 GLN L C   
4606 O O   . GLN C 204 ? 2.7253 2.7517 2.5196 -0.1003 0.0764  -0.2028 204 GLN L O   
4607 C CB  . GLN C 204 ? 2.5985 2.6064 2.3989 -0.0955 0.0694  -0.1757 204 GLN L CB  
4608 C CG  . GLN C 204 ? 2.6361 2.6324 2.4454 -0.0917 0.0671  -0.1691 204 GLN L CG  
4609 C CD  . GLN C 204 ? 2.5835 2.5736 2.3892 -0.0920 0.0622  -0.1593 204 GLN L CD  
4610 O OE1 . GLN C 204 ? 2.7549 2.7496 2.5515 -0.0951 0.0604  -0.1566 204 GLN L OE1 
4611 N NE2 . GLN C 204 ? 2.5072 2.4871 2.3202 -0.0889 0.0599  -0.1540 204 GLN L NE2 
4612 N N   . GLY C 205 ? 2.4176 2.4535 2.2053 -0.1012 0.0790  -0.1895 205 GLY L N   
4613 C CA  . GLY C 205 ? 2.3545 2.4042 2.1317 -0.1057 0.0818  -0.1942 205 GLY L CA  
4614 C C   . GLY C 205 ? 2.2836 2.3402 2.0642 -0.1053 0.0871  -0.2074 205 GLY L C   
4615 O O   . GLY C 205 ? 1.7851 1.8539 1.5567 -0.1092 0.0898  -0.2124 205 GLY L O   
4616 N N   . LEU C 206 ? 2.0174 2.0666 1.8108 -0.1009 0.0886  -0.2133 206 LEU L N   
4617 C CA  . LEU C 206 ? 2.2550 2.3097 2.0540 -0.0998 0.0936  -0.2265 206 LEU L CA  
4618 C C   . LEU C 206 ? 2.2368 2.2830 2.0420 -0.0985 0.0913  -0.2357 206 LEU L C   
4619 O O   . LEU C 206 ? 2.4644 2.4987 2.2819 -0.0946 0.0892  -0.2365 206 LEU L O   
4620 C CB  . LEU C 206 ? 2.5878 2.6406 2.3981 -0.0958 0.0968  -0.2264 206 LEU L CB  
4621 C CG  . LEU C 206 ? 2.5653 2.6294 2.3709 -0.0971 0.1007  -0.2211 206 LEU L CG  
4622 C CD1 . LEU C 206 ? 2.7394 2.8032 2.5576 -0.0931 0.1049  -0.2255 206 LEU L CD1 
4623 C CD2 . LEU C 206 ? 2.4311 2.5114 2.2240 -0.1020 0.1041  -0.2253 206 LEU L CD2 
4624 N N   . SER C 207 ? 2.0274 2.0796 1.8242 -0.1020 0.0912  -0.2423 207 SER L N   
4625 C CA  . SER C 207 ? 1.9464 1.9913 1.7490 -0.1010 0.0889  -0.2519 207 SER L CA  
4626 C C   . SER C 207 ? 1.9951 2.0387 1.8113 -0.0970 0.0925  -0.2633 207 SER L C   
4627 O O   . SER C 207 ? 1.5826 1.6153 1.4097 -0.0943 0.0898  -0.2684 207 SER L O   
4630 N N   . SER C 208 ? 2.4921 2.5466 2.3087 -0.0965 0.0980  -0.2663 208 SER L N   
4631 C CA  . SER C 208 ? 2.4763 2.5310 2.3065 -0.0925 0.1019  -0.2755 208 SER L CA  
4632 C C   . SER C 208 ? 2.6402 2.6952 2.4745 -0.0907 0.1052  -0.2709 208 SER L C   
4633 O O   . SER C 208 ? 2.8711 2.9345 2.6959 -0.0931 0.1069  -0.2626 208 SER L O   
4634 C CB  . SER C 208 ? 2.4251 2.4933 2.2533 -0.0932 0.1058  -0.2831 208 SER L CB  
4635 O OG  . SER C 208 ? 2.3318 2.4137 2.1491 -0.0963 0.1094  -0.2777 208 SER L OG  
4636 N N   . PRO C 209 ? 2.5829 2.6284 2.4329 -0.0861 0.1050  -0.2730 209 PRO L N   
4637 C CA  . PRO C 209 ? 2.5622 2.6079 2.4184 -0.0836 0.1073  -0.2662 209 PRO L CA  
4638 C C   . PRO C 209 ? 2.7273 2.7889 2.5803 -0.0846 0.1144  -0.2717 209 PRO L C   
4639 O O   . PRO C 209 ? 2.7236 2.7929 2.5773 -0.0849 0.1183  -0.2843 209 PRO L O   
4640 C CB  . PRO C 209 ? 2.2325 2.2655 2.1071 -0.0788 0.1055  -0.2702 209 PRO L CB  
4641 C CG  . PRO C 209 ? 2.1902 2.2206 2.0688 -0.0787 0.1044  -0.2828 209 PRO L CG  
4642 C CD  . PRO C 209 ? 2.1826 2.2160 2.0458 -0.0831 0.1018  -0.2803 209 PRO L CD  
4643 N N   . VAL C 210 ? 2.6552 2.7219 2.5046 -0.0852 0.1161  -0.2618 210 VAL L N   
4644 C CA  . VAL C 210 ? 2.4587 2.5412 2.3045 -0.0865 0.1228  -0.2650 210 VAL L CA  
4645 C C   . VAL C 210 ? 2.3595 2.4396 2.2199 -0.0821 0.1255  -0.2651 210 VAL L C   
4646 O O   . VAL C 210 ? 2.5217 2.5925 2.3871 -0.0802 0.1224  -0.2545 210 VAL L O   
4647 C CB  . VAL C 210 ? 2.2675 2.3599 2.0979 -0.0910 0.1227  -0.2539 210 VAL L CB  
4648 C CG1 . VAL C 210 ? 1.9706 2.0794 1.7987 -0.0923 0.1294  -0.2563 210 VAL L CG1 
4649 C CG2 . VAL C 210 ? 2.5160 2.6124 2.3324 -0.0956 0.1204  -0.2550 210 VAL L CG2 
4650 N N   . THR C 211 ? 2.3644 2.4529 2.2317 -0.0806 0.1314  -0.2772 211 THR L N   
4651 C CA  . THR C 211 ? 2.0553 2.1406 1.9392 -0.0761 0.1340  -0.2798 211 THR L CA  
4652 C C   . THR C 211 ? 1.9938 2.0965 1.8752 -0.0771 0.1414  -0.2829 211 THR L C   
4653 O O   . THR C 211 ? 2.2824 2.3935 2.1690 -0.0761 0.1467  -0.2962 211 THR L O   
4654 C CB  . THR C 211 ? 2.0568 2.1340 1.9551 -0.0724 0.1336  -0.2928 211 THR L CB  
4655 O OG1 . THR C 211 ? 2.4233 2.5118 2.3176 -0.0738 0.1377  -0.3057 211 THR L OG1 
4656 C CG2 . THR C 211 ? 2.2181 2.2799 2.1170 -0.0722 0.1263  -0.2895 211 THR L CG2 
4657 N N   . LYS C 212 ? 2.0261 2.1342 1.9004 -0.0791 0.1416  -0.2707 212 LYS L N   
4658 C CA  . LYS C 212 ? 2.0699 2.1956 1.9410 -0.0807 0.1484  -0.2725 212 LYS L CA  
4659 C C   . LYS C 212 ? 2.0484 2.1731 1.9366 -0.0760 0.1521  -0.2763 212 LYS L C   
4660 O O   . LYS C 212 ? 1.9782 2.0895 1.8773 -0.0727 0.1485  -0.2698 212 LYS L O   
4661 C CB  . LYS C 212 ? 1.8156 1.9481 1.6737 -0.0847 0.1472  -0.2580 212 LYS L CB  
4662 C CG  . LYS C 212 ? 1.8345 1.9720 1.6752 -0.0900 0.1447  -0.2552 212 LYS L CG  
4663 C CD  . LYS C 212 ? 1.5763 1.7201 1.4054 -0.0939 0.1429  -0.2405 212 LYS L CD  
4664 C CE  . LYS C 212 ? 1.7600 1.9089 1.5727 -0.0993 0.1402  -0.2384 212 LYS L CE  
4665 N NZ  . LYS C 212 ? 1.8616 2.0165 1.6634 -0.1034 0.1378  -0.2241 212 LYS L NZ  
4666 N N   . SER C 213 ? 2.1475 2.2867 2.0384 -0.0759 0.1593  -0.2873 213 SER L N   
4667 C CA  . SER C 213 ? 2.0781 2.2169 1.9868 -0.0712 0.1632  -0.2938 213 SER L CA  
4668 C C   . SER C 213 ? 2.3065 2.4629 2.2132 -0.0726 0.1699  -0.2923 213 SER L C   
4669 O O   . SER C 213 ? 2.6009 2.7727 2.4929 -0.0773 0.1729  -0.2916 213 SER L O   
4670 C CB  . SER C 213 ? 1.9934 2.1322 1.9118 -0.0685 0.1661  -0.3115 213 SER L CB  
4671 O OG  . SER C 213 ? 1.8668 2.0215 1.7763 -0.0713 0.1693  -0.3166 213 SER L OG  
4672 N N   . PHE C 214 ? 2.2088 2.3630 2.1310 -0.0686 0.1720  -0.2918 214 PHE L N   
4673 C CA  . PHE C 214 ? 2.3579 2.5279 2.2815 -0.0693 0.1782  -0.2902 214 PHE L CA  
4674 C C   . PHE C 214 ? 2.2224 2.3899 2.1668 -0.0638 0.1817  -0.2985 214 PHE L C   
4675 O O   . PHE C 214 ? 2.1877 2.3414 2.1444 -0.0604 0.1779  -0.2916 214 PHE L O   
4676 C CB  . PHE C 214 ? 2.5785 2.7474 2.4954 -0.0714 0.1749  -0.2722 214 PHE L CB  
4677 C CG  . PHE C 214 ? 2.6596 2.8331 2.5566 -0.0770 0.1719  -0.2641 214 PHE L CG  
4678 C CD1 . PHE C 214 ? 2.6915 2.8503 2.5826 -0.0777 0.1645  -0.2572 214 PHE L CD1 
4679 C CD2 . PHE C 214 ? 2.7224 2.9158 2.6066 -0.0819 0.1766  -0.2642 214 PHE L CD2 
4680 C CE1 . PHE C 214 ? 2.9265 3.0899 2.8002 -0.0828 0.1618  -0.2504 214 PHE L CE1 
4681 C CE2 . PHE C 214 ? 2.8967 3.0944 2.7631 -0.0873 0.1735  -0.2567 214 PHE L CE2 
4682 C CZ  . PHE C 214 ? 3.0587 3.2411 2.9201 -0.0876 0.1660  -0.2498 214 PHE L CZ  
4683 N N   . ASN C 215 ? 2.0206 2.2016 1.9692 -0.0630 0.1889  -0.3132 215 ASN L N   
4684 C CA  . ASN C 215 ? 1.9938 2.1744 1.9630 -0.0578 0.1929  -0.3220 215 ASN L CA  
4685 C C   . ASN C 215 ? 2.1088 2.2966 2.0830 -0.0574 0.1957  -0.3124 215 ASN L C   
4686 O O   . ASN C 215 ? 2.3043 2.4989 2.2657 -0.0614 0.1951  -0.3000 215 ASN L O   
4687 C CB  . ASN C 215 ? 2.3239 2.5165 2.2964 -0.0570 0.1979  -0.3373 215 ASN L CB  
4688 C CG  . ASN C 215 ? 2.5262 2.7075 2.5005 -0.0557 0.1925  -0.3447 215 ASN L CG  
4689 O OD1 . ASN C 215 ? 2.6274 2.7940 2.5978 -0.0562 0.1867  -0.3404 215 ASN L OD1 
4690 N ND2 . ASN C 215 ? 2.6159 2.8040 2.5962 -0.0542 0.1945  -0.3557 215 ASN L ND2 
4691 N N   . ARG C 216 ? 1.9264 2.1125 1.9204 -0.0526 0.1986  -0.3181 216 ARG L N   
4692 C CA  . ARG C 216 ? 1.7822 1.9718 1.7839 -0.0516 0.2003  -0.3084 216 ARG L CA  
4693 C C   . ARG C 216 ? 1.9474 2.1591 1.9363 -0.0560 0.2063  -0.3049 216 ARG L C   
4694 O O   . ARG C 216 ? 1.9829 2.1964 1.9680 -0.0578 0.2048  -0.2907 216 ARG L O   
4695 C CB  . ARG C 216 ? 1.6745 1.8619 1.6997 -0.0459 0.2036  -0.3177 216 ARG L CB  
4696 C CG  . ARG C 216 ? 1.6340 1.8251 1.6683 -0.0448 0.2053  -0.3079 216 ARG L CG  
4697 C CD  . ARG C 216 ? 1.4441 1.6319 1.5030 -0.0391 0.2080  -0.3161 216 ARG L CD  
4698 N NE  . ARG C 216 ? 1.7324 1.9245 1.7983 -0.0386 0.2095  -0.3057 216 ARG L NE  
4699 C CZ  . ARG C 216 ? 2.2670 2.4790 2.3330 -0.0395 0.2172  -0.3079 216 ARG L CZ  
4700 N NH1 . ARG C 216 ? 2.5383 2.7679 2.5996 -0.0405 0.2246  -0.3216 216 ARG L NH1 
4701 N NH2 . ARG C 216 ? 2.3160 2.5305 2.3866 -0.0397 0.2173  -0.2960 216 ARG L NH2 
4702 N N   . GLY C 217 ? 1.9798 2.2084 1.9618 -0.0579 0.2129  -0.3175 217 GLY L N   
4703 C CA  . GLY C 217 ? 1.9213 2.1723 1.8909 -0.0625 0.2188  -0.3150 217 GLY L CA  
4704 C C   . GLY C 217 ? 2.2446 2.5032 2.1948 -0.0676 0.2172  -0.3158 217 GLY L C   
4705 O O   . GLY C 217 ? 2.3791 2.6304 2.3287 -0.0666 0.2140  -0.3235 217 GLY L O   
4706 N N   . GLU C 218 ? 2.3795 2.6521 2.3146 -0.0731 0.2182  -0.3058 218 GLU L N   
4707 C CA  . GLU C 218 ? 2.5897 2.8718 2.5069 -0.0784 0.2162  -0.3039 218 GLU L CA  
4708 C C   . GLU C 218 ? 3.1520 3.4561 3.0642 -0.0818 0.2214  -0.3008 218 GLU L C   
4709 O O   . GLU C 218 ? 3.1923 3.5038 3.1155 -0.0797 0.2264  -0.3010 218 GLU L O   
4710 C CB  . GLU C 218 ? 2.4229 2.6970 2.3243 -0.0827 0.2100  -0.2922 218 GLU L CB  
4711 C CG  . GLU C 218 ? 2.2379 2.4946 2.1380 -0.0812 0.2043  -0.2968 218 GLU L CG  
4712 C CD  . GLU C 218 ? 2.4701 2.7079 2.3841 -0.0760 0.2026  -0.2987 218 GLU L CD  
4713 O OE1 . GLU C 218 ? 2.4992 2.7319 2.4201 -0.0746 0.2006  -0.2872 218 GLU L OE1 
4714 O OE2 . GLU C 218 ? 2.5757 2.8004 2.4963 -0.0729 0.1994  -0.3068 218 GLU L OE2 
4715 N N   . GLY D 1   ? 1.9024 1.5072 1.5660 -0.0432 -0.1151 -0.0502 10  GLY A N   
4716 C CA  . GLY D 1   ? 2.0084 1.6146 1.6714 -0.0497 -0.1135 -0.0410 10  GLY A CA  
4717 C C   . GLY D 1   ? 2.0675 1.6815 1.7393 -0.0486 -0.1084 -0.0365 10  GLY A C   
4718 O O   . GLY D 1   ? 2.1903 1.8112 1.8664 -0.0435 -0.1047 -0.0416 10  GLY A O   
4719 N N   . ASP D 2   ? 2.1182 1.7310 1.7929 -0.0534 -0.1085 -0.0272 11  ASP A N   
4720 C CA  . ASP D 2   ? 2.3738 1.9938 2.0563 -0.0533 -0.1036 -0.0226 11  ASP A CA  
4721 C C   . ASP D 2   ? 2.3427 1.9753 2.0207 -0.0542 -0.0965 -0.0275 11  ASP A C   
4722 O O   . ASP D 2   ? 2.4479 2.0833 2.1167 -0.0589 -0.0953 -0.0291 11  ASP A O   
4723 C CB  . ASP D 2   ? 2.5000 2.1159 2.1858 -0.0588 -0.1054 -0.0122 11  ASP A CB  
4724 C CG  . ASP D 2   ? 2.7644 2.3710 2.4587 -0.0570 -0.1108 -0.0060 11  ASP A CG  
4725 O OD1 . ASP D 2   ? 2.7682 2.3698 2.4645 -0.0522 -0.1144 -0.0094 11  ASP A OD1 
4726 O OD2 . ASP D 2   ? 2.9404 2.5444 2.6395 -0.0607 -0.1118 0.0024  11  ASP A OD2 
4727 N N   . THR D 3   ? 2.5846 2.2249 2.2689 -0.0500 -0.0920 -0.0297 12  THR A N   
4728 C CA  . THR D 3   ? 2.3141 1.9665 1.9947 -0.0502 -0.0853 -0.0347 12  THR A CA  
4729 C C   . THR D 3   ? 2.1561 1.8155 1.8450 -0.0495 -0.0809 -0.0307 12  THR A C   
4730 O O   . THR D 3   ? 2.1087 1.7653 1.8066 -0.0463 -0.0822 -0.0274 12  THR A O   
4731 C CB  . THR D 3   ? 2.1535 1.8098 1.8316 -0.0445 -0.0838 -0.0452 12  THR A CB  
4732 O OG1 . THR D 3   ? 2.1027 1.7565 1.7903 -0.0383 -0.0855 -0.0458 12  THR A OG1 
4733 C CG2 . THR D 3   ? 2.5797 2.2300 2.2489 -0.0452 -0.0878 -0.0503 12  THR A CG2 
4734 N N   . LEU D 4   ? 2.1322 1.8011 1.8178 -0.0528 -0.0756 -0.0311 13  LEU A N   
4735 C CA  . LEU D 4   ? 2.0177 1.6948 1.7100 -0.0524 -0.0708 -0.0287 13  LEU A CA  
4736 C C   . LEU D 4   ? 1.9211 1.6098 1.6095 -0.0511 -0.0651 -0.0357 13  LEU A C   
4737 O O   . LEU D 4   ? 2.1240 1.8168 1.8037 -0.0548 -0.0636 -0.0383 13  LEU A O   
4738 C CB  . LEU D 4   ? 1.7897 1.4667 1.4836 -0.0587 -0.0705 -0.0205 13  LEU A CB  
4739 C CG  . LEU D 4   ? 1.5182 1.2047 1.2174 -0.0590 -0.0651 -0.0189 13  LEU A CG  
4740 C CD1 . LEU D 4   ? 1.8076 1.4931 1.5165 -0.0541 -0.0648 -0.0175 13  LEU A CD1 
4741 C CD2 . LEU D 4   ? 1.6488 1.3355 1.3488 -0.0656 -0.0649 -0.0118 13  LEU A CD2 
4742 N N   . CYS D 5   ? 1.5930 1.2873 1.2876 -0.0461 -0.0620 -0.0385 14  CYS A N   
4743 C CA  . CYS D 5   ? 1.8273 1.5326 1.5194 -0.0440 -0.0568 -0.0454 14  CYS A CA  
4744 C C   . CYS D 5   ? 1.8433 1.5570 1.5412 -0.0446 -0.0521 -0.0424 14  CYS A C   
4745 O O   . CYS D 5   ? 1.6768 1.3876 1.3819 -0.0447 -0.0529 -0.0364 14  CYS A O   
4746 C CB  . CYS D 5   ? 1.8429 1.5477 1.5371 -0.0370 -0.0576 -0.0528 14  CYS A CB  
4747 S SG  . CYS D 5   ? 2.5039 2.1999 2.1906 -0.0362 -0.0627 -0.0580 14  CYS A SG  
4748 N N   . ILE D 6   ? 1.8267 1.5512 1.5213 -0.0449 -0.0471 -0.0467 15  ILE A N   
4749 C CA  . ILE D 6   ? 1.5457 1.2787 1.2445 -0.0464 -0.0427 -0.0439 15  ILE A CA  
4750 C C   . ILE D 6   ? 1.5892 1.3302 1.2914 -0.0408 -0.0390 -0.0500 15  ILE A C   
4751 O O   . ILE D 6   ? 1.8865 1.6305 1.5845 -0.0380 -0.0381 -0.0572 15  ILE A O   
4752 C CB  . ILE D 6   ? 1.6062 1.3459 1.2986 -0.0529 -0.0401 -0.0423 15  ILE A CB  
4753 C CG1 . ILE D 6   ? 1.8533 1.5859 1.5387 -0.0581 -0.0441 -0.0394 15  ILE A CG1 
4754 C CG2 . ILE D 6   ? 1.5268 1.2709 1.2250 -0.0557 -0.0377 -0.0365 15  ILE A CG2 
4755 C CD1 . ILE D 6   ? 1.8609 1.5835 1.5506 -0.0607 -0.0483 -0.0316 15  ILE A CD1 
4756 N N   . GLY D 7   ? 1.4556 1.2003 1.1654 -0.0393 -0.0369 -0.0474 16  GLY A N   
4757 C CA  . GLY D 7   ? 1.6577 1.4099 1.3712 -0.0342 -0.0337 -0.0528 16  GLY A CA  
4758 C C   . GLY D 7   ? 1.5985 1.3569 1.3191 -0.0335 -0.0305 -0.0501 16  GLY A C   
4759 O O   . GLY D 7   ? 1.2773 1.0320 1.0025 -0.0353 -0.0317 -0.0439 16  GLY A O   
4760 N N   . TYR D 8   ? 1.4947 1.2626 1.2165 -0.0308 -0.0266 -0.0548 17  TYR A N   
4761 C CA  . TYR D 8   ? 1.3784 1.1528 1.1065 -0.0300 -0.0236 -0.0529 17  TYR A CA  
4762 C C   . TYR D 8   ? 1.5569 1.3298 1.2924 -0.0241 -0.0249 -0.0547 17  TYR A C   
4763 O O   . TYR D 8   ? 1.7616 1.5303 1.4974 -0.0201 -0.0275 -0.0587 17  TYR A O   
4764 C CB  . TYR D 8   ? 1.5428 1.3291 1.2683 -0.0314 -0.0185 -0.0560 17  TYR A CB  
4765 C CG  . TYR D 8   ? 1.7040 1.4958 1.4270 -0.0274 -0.0167 -0.0640 17  TYR A CG  
4766 C CD1 . TYR D 8   ? 1.7684 1.5596 1.4834 -0.0287 -0.0172 -0.0678 17  TYR A CD1 
4767 C CD2 . TYR D 8   ? 1.8708 1.6686 1.5994 -0.0226 -0.0146 -0.0677 17  TYR A CD2 
4768 C CE1 . TYR D 8   ? 2.1659 1.9626 1.8789 -0.0249 -0.0153 -0.0758 17  TYR A CE1 
4769 C CE2 . TYR D 8   ? 2.0004 1.8035 1.7277 -0.0188 -0.0129 -0.0752 17  TYR A CE2 
4770 C CZ  . TYR D 8   ? 2.2008 2.0034 1.9203 -0.0198 -0.0132 -0.0795 17  TYR A CZ  
4771 O OH  . TYR D 8   ? 2.4691 2.2772 2.1874 -0.0159 -0.0113 -0.0877 17  TYR A OH  
4772 N N   . HIS D 9   ? 1.4364 1.2129 1.1781 -0.0237 -0.0232 -0.0517 18  HIS A N   
4773 C CA  . HIS D 9   ? 1.5255 1.3007 1.2746 -0.0191 -0.0248 -0.0518 18  HIS A CA  
4774 C C   . HIS D 9   ? 1.5779 1.3610 1.3294 -0.0148 -0.0223 -0.0577 18  HIS A C   
4775 O O   . HIS D 9   ? 1.6302 1.4221 1.3791 -0.0158 -0.0182 -0.0604 18  HIS A O   
4776 C CB  . HIS D 9   ? 1.5228 1.2984 1.2772 -0.0209 -0.0243 -0.0459 18  HIS A CB  
4777 C CG  . HIS D 9   ? 1.7676 1.5425 1.5293 -0.0168 -0.0261 -0.0452 18  HIS A CG  
4778 N ND1 . HIS D 9   ? 2.2997 2.0667 2.0641 -0.0141 -0.0308 -0.0446 18  HIS A ND1 
4779 C CD2 . HIS D 9   ? 1.2280 1.0092 0.9950 -0.0154 -0.0241 -0.0448 18  HIS A CD2 
4780 C CE1 . HIS D 9   ? 2.1139 1.8828 1.8851 -0.0112 -0.0316 -0.0437 18  HIS A CE1 
4781 N NE2 . HIS D 9   ? 1.6220 1.3993 1.3947 -0.0120 -0.0275 -0.0438 18  HIS A NE2 
4782 N N   . ALA D 10  ? 1.7847 1.5650 1.5420 -0.0100 -0.0251 -0.0593 19  ALA A N   
4783 C CA  . ALA D 10  ? 1.7642 1.5511 1.5260 -0.0054 -0.0236 -0.0644 19  ALA A CA  
4784 C C   . ALA D 10  ? 1.8041 1.5887 1.5744 -0.0025 -0.0264 -0.0616 19  ALA A C   
4785 O O   . ALA D 10  ? 1.8115 1.5882 1.5837 -0.0029 -0.0304 -0.0572 19  ALA A O   
4786 C CB  . ALA D 10  ? 1.6749 1.4606 1.4344 -0.0019 -0.0247 -0.0716 19  ALA A CB  
4787 N N   . ASN D 11  ? 1.7122 1.5044 1.4879 0.0002  -0.0244 -0.0637 20  ASN A N   
4788 C CA  . ASN D 11  ? 1.5220 1.3134 1.3058 0.0026  -0.0269 -0.0608 20  ASN A CA  
4789 C C   . ASN D 11  ? 1.6666 1.4644 1.4561 0.0071  -0.0261 -0.0659 20  ASN A C   
4790 O O   . ASN D 11  ? 1.7853 1.5863 1.5726 0.0092  -0.0244 -0.0722 20  ASN A O   
4791 C CB  . ASN D 11  ? 1.6819 1.4762 1.4669 -0.0011 -0.0250 -0.0548 20  ASN A CB  
4792 C CG  . ASN D 11  ? 1.8427 1.6465 1.6252 -0.0033 -0.0196 -0.0560 20  ASN A CG  
4793 O OD1 . ASN D 11  ? 1.9262 1.7353 1.7064 -0.0022 -0.0170 -0.0611 20  ASN A OD1 
4794 N ND2 . ASN D 11  ? 1.6244 1.4308 1.4078 -0.0066 -0.0179 -0.0513 20  ASN A ND2 
4795 N N   . ASN D 12  ? 1.5334 1.3333 1.3303 0.0086  -0.0274 -0.0632 21  ASN A N   
4796 C CA  . ASN D 12  ? 1.5588 1.3651 1.3626 0.0127  -0.0270 -0.0670 21  ASN A CA  
4797 C C   . ASN D 12  ? 1.7191 1.5347 1.5237 0.0106  -0.0225 -0.0652 21  ASN A C   
4798 O O   . ASN D 12  ? 2.0543 1.8713 1.8637 0.0099  -0.0236 -0.0607 21  ASN A O   
4799 C CB  . ASN D 12  ? 1.6806 1.4822 1.4929 0.0159  -0.0326 -0.0651 21  ASN A CB  
4800 C CG  . ASN D 12  ? 1.9841 1.7770 1.7967 0.0188  -0.0373 -0.0681 21  ASN A CG  
4801 O OD1 . ASN D 12  ? 1.9843 1.7764 1.7919 0.0197  -0.0359 -0.0736 21  ASN A OD1 
4802 N ND2 . ASN D 12  ? 2.0143 1.8007 1.8326 0.0200  -0.0430 -0.0643 21  ASN A ND2 
4803 N N   . SER D 13  ? 1.7592 1.5817 1.5592 0.0094  -0.0177 -0.0686 22  SER A N   
4804 C CA  . SER D 13  ? 1.8162 1.6478 1.6167 0.0072  -0.0134 -0.0671 22  SER A CA  
4805 C C   . SER D 13  ? 2.0043 1.8447 1.8066 0.0100  -0.0102 -0.0732 22  SER A C   
4806 O O   . SER D 13  ? 2.0448 1.8884 1.8413 0.0092  -0.0071 -0.0769 22  SER A O   
4807 C CB  . SER D 13  ? 1.7839 1.6159 1.5771 0.0018  -0.0105 -0.0640 22  SER A CB  
4808 O OG  . SER D 13  ? 1.9473 1.7767 1.7335 0.0008  -0.0098 -0.0668 22  SER A OG  
4809 N N   . THR D 14  ? 1.8715 1.7163 1.6820 0.0132  -0.0109 -0.0740 23  THR A N   
4810 C CA  . THR D 14  ? 1.8708 1.7249 1.6843 0.0158  -0.0075 -0.0791 23  THR A CA  
4811 C C   . THR D 14  ? 1.8512 1.7144 1.6613 0.0122  -0.0024 -0.0777 23  THR A C   
4812 O O   . THR D 14  ? 1.9317 1.8039 1.7448 0.0139  0.0006  -0.0811 23  THR A O   
4813 C CB  . THR D 14  ? 1.9116 1.7677 1.7357 0.0199  -0.0102 -0.0795 23  THR A CB  
4814 O OG1 . THR D 14  ? 1.7803 1.6370 1.6072 0.0173  -0.0112 -0.0730 23  THR A OG1 
4815 C CG2 . THR D 14  ? 2.0108 1.8584 1.8393 0.0238  -0.0156 -0.0813 23  THR A CG2 
4816 N N   . ASP D 15  ? 1.8038 1.6648 1.6084 0.0073  -0.0016 -0.0728 24  ASP A N   
4817 C CA  . ASP D 15  ? 1.6764 1.5450 1.4779 0.0034  0.0026  -0.0709 24  ASP A CA  
4818 C C   . ASP D 15  ? 1.7747 1.6495 1.5711 0.0029  0.0064  -0.0756 24  ASP A C   
4819 O O   . ASP D 15  ? 1.7362 1.6068 1.5268 0.0024  0.0061  -0.0776 24  ASP A O   
4820 C CB  . ASP D 15  ? 1.6398 1.5034 1.4367 -0.0016 0.0021  -0.0653 24  ASP A CB  
4821 C CG  . ASP D 15  ? 1.9557 1.8158 1.7574 -0.0019 -0.0007 -0.0604 24  ASP A CG  
4822 O OD1 . ASP D 15  ? 2.0505 1.9138 1.8589 0.0009  -0.0017 -0.0608 24  ASP A OD1 
4823 O OD2 . ASP D 15  ? 2.0245 1.8791 1.8234 -0.0051 -0.0018 -0.0563 24  ASP A OD2 
4824 N N   . THR D 16  ? 1.7661 1.6514 1.5648 0.0031  0.0100  -0.0771 25  THR A N   
4825 C CA  . THR D 16  ? 1.4545 1.3479 1.2486 0.0020  0.0142  -0.0809 25  THR A CA  
4826 C C   . THR D 16  ? 1.3176 1.2162 1.1079 -0.0036 0.0170  -0.0765 25  THR A C   
4827 O O   . THR D 16  ? 1.7121 1.6142 1.5065 -0.0047 0.0174  -0.0731 25  THR A O   
4828 C CB  . THR D 16  ? 1.4681 1.3705 1.2685 0.0065  0.0163  -0.0860 25  THR A CB  
4829 O OG1 . THR D 16  ? 1.6632 1.5697 1.4706 0.0068  0.0162  -0.0829 25  THR A OG1 
4830 C CG2 . THR D 16  ? 1.4925 1.3898 1.2969 0.0121  0.0135  -0.0912 25  THR A CG2 
4831 N N   . VAL D 17  ? 1.1410 1.0401 0.9236 -0.0072 0.0186  -0.0765 26  VAL A N   
4832 C CA  . VAL D 17  ? 1.2597 1.1634 1.0386 -0.0129 0.0207  -0.0724 26  VAL A CA  
4833 C C   . VAL D 17  ? 1.3740 1.2864 1.1477 -0.0145 0.0243  -0.0756 26  VAL A C   
4834 O O   . VAL D 17  ? 1.5277 1.4374 1.2962 -0.0141 0.0240  -0.0788 26  VAL A O   
4835 C CB  . VAL D 17  ? 1.4274 1.3220 1.2023 -0.0171 0.0182  -0.0673 26  VAL A CB  
4836 C CG1 . VAL D 17  ? 1.3821 1.2816 1.1540 -0.0229 0.0202  -0.0633 26  VAL A CG1 
4837 C CG2 . VAL D 17  ? 1.5859 1.4731 1.3658 -0.0157 0.0151  -0.0641 26  VAL A CG2 
4838 N N   . ASP D 18  ? 1.4121 1.3350 1.1870 -0.0167 0.0274  -0.0745 27  ASP A N   
4839 C CA  . ASP D 18  ? 1.4895 1.4224 1.2600 -0.0186 0.0311  -0.0770 27  ASP A CA  
4840 C C   . ASP D 18  ? 1.4027 1.3351 1.1663 -0.0253 0.0311  -0.0725 27  ASP A C   
4841 O O   . ASP D 18  ? 1.3909 1.3178 1.1549 -0.0286 0.0290  -0.0671 27  ASP A O   
4842 C CB  . ASP D 18  ? 1.5277 1.4729 1.3034 -0.0177 0.0344  -0.0778 27  ASP A CB  
4843 C CG  . ASP D 18  ? 1.5911 1.5381 1.3743 -0.0111 0.0345  -0.0825 27  ASP A CG  
4844 O OD1 . ASP D 18  ? 1.7487 1.6870 1.5334 -0.0072 0.0317  -0.0849 27  ASP A OD1 
4845 O OD2 . ASP D 18  ? 1.3845 1.3416 1.1726 -0.0098 0.0371  -0.0835 27  ASP A OD2 
4846 N N   . THR D 19  ? 1.6207 1.5594 1.3782 -0.0273 0.0334  -0.0750 28  THR A N   
4847 C CA  . THR D 19  ? 1.5984 1.5383 1.3493 -0.0340 0.0334  -0.0709 28  THR A CA  
4848 C C   . THR D 19  ? 1.6729 1.6274 1.4219 -0.0365 0.0375  -0.0719 28  THR A C   
4849 O O   . THR D 19  ? 1.7216 1.6847 1.4741 -0.0327 0.0404  -0.0762 28  THR A O   
4850 C CB  . THR D 19  ? 1.7651 1.6967 1.5089 -0.0351 0.0313  -0.0721 28  THR A CB  
4851 O OG1 . THR D 19  ? 1.7726 1.7083 1.5137 -0.0313 0.0333  -0.0793 28  THR A OG1 
4852 C CG2 . THR D 19  ? 1.4735 1.3910 1.2196 -0.0330 0.0272  -0.0705 28  THR A CG2 
4853 N N   . VAL D 20  ? 1.5055 1.4629 1.2491 -0.0431 0.0376  -0.0677 29  VAL A N   
4854 C CA  . VAL D 20  ? 1.7168 1.6884 1.4573 -0.0462 0.0412  -0.0685 29  VAL A CA  
4855 C C   . VAL D 20  ? 1.7834 1.7590 1.5185 -0.0435 0.0435  -0.0756 29  VAL A C   
4856 O O   . VAL D 20  ? 1.7303 1.7178 1.4662 -0.0415 0.0474  -0.0799 29  VAL A O   
4857 C CB  . VAL D 20  ? 1.6250 1.5981 1.3611 -0.0543 0.0400  -0.0617 29  VAL A CB  
4858 C CG1 . VAL D 20  ? 1.9507 1.9387 1.6825 -0.0581 0.0435  -0.0622 29  VAL A CG1 
4859 C CG2 . VAL D 20  ? 1.6468 1.6174 1.3891 -0.0567 0.0380  -0.0554 29  VAL A CG2 
4860 N N   . LEU D 21  ? 1.8165 1.7822 1.5463 -0.0432 0.0410  -0.0772 30  LEU A N   
4861 C CA  . LEU D 21  ? 1.7820 1.7506 1.5061 -0.0408 0.0429  -0.0844 30  LEU A CA  
4862 C C   . LEU D 21  ? 1.8227 1.7906 1.5528 -0.0325 0.0439  -0.0917 30  LEU A C   
4863 O O   . LEU D 21  ? 1.9078 1.8862 1.6383 -0.0296 0.0477  -0.0977 30  LEU A O   
4864 C CB  . LEU D 21  ? 1.8024 1.7603 1.5191 -0.0434 0.0395  -0.0836 30  LEU A CB  
4865 C CG  . LEU D 21  ? 1.8402 1.7990 1.5502 -0.0518 0.0383  -0.0772 30  LEU A CG  
4866 C CD1 . LEU D 21  ? 2.1168 2.0632 1.8209 -0.0536 0.0343  -0.0762 30  LEU A CD1 
4867 C CD2 . LEU D 21  ? 1.9409 1.9151 1.6454 -0.0556 0.0423  -0.0787 30  LEU A CD2 
4868 N N   . GLU D 22  ? 1.5284 1.4841 1.2634 -0.0287 0.0404  -0.0911 31  GLU A N   
4869 C CA  . GLU D 22  ? 1.6310 1.5841 1.3721 -0.0210 0.0402  -0.0975 31  GLU A CA  
4870 C C   . GLU D 22  ? 1.5712 1.5219 1.3219 -0.0182 0.0389  -0.0944 31  GLU A C   
4871 O O   . GLU D 22  ? 1.5826 1.5312 1.3346 -0.0220 0.0377  -0.0876 31  GLU A O   
4872 C CB  . GLU D 22  ? 1.8635 1.8039 1.6013 -0.0186 0.0366  -0.1004 31  GLU A CB  
4873 C CG  . GLU D 22  ? 2.0387 1.9817 1.7672 -0.0203 0.0378  -0.1050 31  GLU A CG  
4874 C CD  . GLU D 22  ? 2.0611 1.9907 1.7864 -0.0184 0.0337  -0.1072 31  GLU A CD  
4875 O OE1 . GLU D 22  ? 1.9059 1.8241 1.6358 -0.0166 0.0298  -0.1040 31  GLU A OE1 
4876 O OE2 . GLU D 22  ? 2.0510 1.9817 1.7690 -0.0188 0.0344  -0.1122 31  GLU A OE2 
4877 N N   . LYS D 23  ? 1.7540 1.7050 1.5117 -0.0116 0.0391  -0.0995 32  LYS A N   
4878 C CA  . LYS D 23  ? 1.5316 1.4802 1.2987 -0.0086 0.0376  -0.0972 32  LYS A CA  
4879 C C   . LYS D 23  ? 1.5535 1.4921 1.3253 -0.0027 0.0340  -0.1006 32  LYS A C   
4880 O O   . LYS D 23  ? 1.6403 1.5758 1.4096 0.0002  0.0335  -0.1063 32  LYS A O   
4881 C CB  . LYS D 23  ? 1.5260 1.4876 1.2995 -0.0067 0.0413  -0.0989 32  LYS A CB  
4882 C CG  . LYS D 23  ? 1.4987 1.4702 1.2697 -0.0124 0.0441  -0.0941 32  LYS A CG  
4883 C CD  . LYS D 23  ? 1.4071 1.3911 1.1852 -0.0100 0.0475  -0.0960 32  LYS A CD  
4884 C CE  . LYS D 23  ? 1.8793 1.8732 1.6559 -0.0158 0.0499  -0.0908 32  LYS A CE  
4885 N NZ  . LYS D 23  ? 2.3629 2.3694 2.1466 -0.0135 0.0532  -0.0925 32  LYS A NZ  
4886 N N   . ASN D 24  ? 1.6545 1.5884 1.4335 -0.0011 0.0315  -0.0970 33  ASN A N   
4887 C CA  . ASN D 24  ? 1.6292 1.5534 1.4139 0.0039  0.0274  -0.0985 33  ASN A CA  
4888 C C   . ASN D 24  ? 1.4933 1.4055 1.2721 0.0031  0.0239  -0.0983 33  ASN A C   
4889 O O   . ASN D 24  ? 1.6036 1.5087 1.3854 0.0075  0.0209  -0.1017 33  ASN A O   
4890 C CB  . ASN D 24  ? 1.7559 1.6851 1.5474 0.0103  0.0285  -0.1057 33  ASN A CB  
4891 C CG  . ASN D 24  ? 1.7399 1.6800 1.5389 0.0114  0.0313  -0.1054 33  ASN A CG  
4892 O OD1 . ASN D 24  ? 1.5100 1.4547 1.3082 0.0072  0.0327  -0.1000 33  ASN A OD1 
4893 N ND2 . ASN D 24  ? 1.9474 1.8917 1.7542 0.0172  0.0318  -0.1111 33  ASN A ND2 
4894 N N   . VAL D 25  ? 1.3802 1.2901 1.1511 -0.0026 0.0241  -0.0942 34  VAL A N   
4895 C CA  . VAL D 25  ? 1.3470 1.2452 1.1126 -0.0040 0.0205  -0.0927 34  VAL A CA  
4896 C C   . VAL D 25  ? 1.4373 1.3255 1.2083 -0.0027 0.0162  -0.0884 34  VAL A C   
4897 O O   . VAL D 25  ? 1.6006 1.4902 1.3756 -0.0041 0.0162  -0.0837 34  VAL A O   
4898 C CB  . VAL D 25  ? 1.1188 1.0174 0.8760 -0.0108 0.0214  -0.0885 34  VAL A CB  
4899 C CG1 . VAL D 25  ? 1.2534 1.1402 1.0051 -0.0123 0.0178  -0.0872 34  VAL A CG1 
4900 C CG2 . VAL D 25  ? 1.4634 1.3738 1.2156 -0.0127 0.0259  -0.0920 34  VAL A CG2 
4901 N N   . THR D 26  ? 1.2998 1.1780 1.0707 -0.0001 0.0124  -0.0900 35  THR A N   
4902 C CA  . THR D 26  ? 1.4650 1.3335 1.2404 0.0009  0.0080  -0.0857 35  THR A CA  
4903 C C   . THR D 26  ? 1.6325 1.4928 1.4019 -0.0038 0.0060  -0.0805 35  THR A C   
4904 O O   . THR D 26  ? 1.7045 1.5607 1.4675 -0.0051 0.0052  -0.0821 35  THR A O   
4905 C CB  . THR D 26  ? 1.4028 1.2653 1.1830 0.0066  0.0044  -0.0900 35  THR A CB  
4906 O OG1 . THR D 26  ? 1.7900 1.6480 1.5639 0.0069  0.0035  -0.0941 35  THR A OG1 
4907 C CG2 . THR D 26  ? 1.4537 1.3242 1.2414 0.0115  0.0061  -0.0949 35  THR A CG2 
4908 N N   . VAL D 27  ? 1.5686 1.4268 1.3402 -0.0065 0.0052  -0.0744 36  VAL A N   
4909 C CA  . VAL D 27  ? 1.4574 1.3084 1.2247 -0.0111 0.0034  -0.0691 36  VAL A CA  
4910 C C   . VAL D 27  ? 1.5309 1.3728 1.3027 -0.0095 -0.0007 -0.0657 36  VAL A C   
4911 O O   . VAL D 27  ? 1.7459 1.5886 1.5243 -0.0061 -0.0018 -0.0659 36  VAL A O   
4912 C CB  . VAL D 27  ? 1.5816 1.4381 1.3477 -0.0161 0.0061  -0.0647 36  VAL A CB  
4913 C CG1 . VAL D 27  ? 1.4426 1.3083 1.2039 -0.0183 0.0099  -0.0674 36  VAL A CG1 
4914 C CG2 . VAL D 27  ? 1.6744 1.5350 1.4473 -0.0151 0.0068  -0.0627 36  VAL A CG2 
4915 N N   . THR D 28  ? 1.5130 1.3463 1.2813 -0.0121 -0.0032 -0.0624 37  THR A N   
4916 C CA  . THR D 28  ? 1.5063 1.3310 1.2784 -0.0110 -0.0073 -0.0588 37  THR A CA  
4917 C C   . THR D 28  ? 1.4037 1.2310 1.1807 -0.0122 -0.0066 -0.0545 37  THR A C   
4918 O O   . THR D 28  ? 1.4545 1.2803 1.2372 -0.0095 -0.0088 -0.0535 37  THR A O   
4919 C CB  . THR D 28  ? 1.4875 1.3032 1.2548 -0.0140 -0.0097 -0.0558 37  THR A CB  
4920 O OG1 . THR D 28  ? 1.3856 1.2040 1.1487 -0.0192 -0.0073 -0.0531 37  THR A OG1 
4921 C CG2 . THR D 28  ? 1.6405 1.4519 1.4037 -0.0121 -0.0115 -0.0602 37  THR A CG2 
4922 N N   . HIS D 29  ? 1.0842 0.9156 0.8592 -0.0164 -0.0039 -0.0519 38  HIS A N   
4923 C CA  . HIS D 29  ? 1.3283 1.1622 1.1073 -0.0180 -0.0032 -0.0482 38  HIS A CA  
4924 C C   . HIS D 29  ? 1.3348 1.1780 1.1129 -0.0205 0.0008  -0.0486 38  HIS A C   
4925 O O   . HIS D 29  ? 1.5370 1.3824 1.3103 -0.0232 0.0025  -0.0493 38  HIS A O   
4926 C CB  . HIS D 29  ? 1.2572 1.0841 1.0355 -0.0213 -0.0049 -0.0433 38  HIS A CB  
4927 C CG  . HIS D 29  ? 1.3125 1.1305 1.0919 -0.0193 -0.0090 -0.0420 38  HIS A CG  
4928 N ND1 . HIS D 29  ? 1.6959 1.5125 1.4805 -0.0162 -0.0112 -0.0414 38  HIS A ND1 
4929 C CD2 . HIS D 29  ? 1.2966 1.1066 1.0727 -0.0202 -0.0114 -0.0411 38  HIS A CD2 
4930 C CE1 . HIS D 29  ? 1.7367 1.5451 1.5213 -0.0153 -0.0149 -0.0399 38  HIS A CE1 
4931 N NE2 . HIS D 29  ? 1.6862 1.4903 1.4657 -0.0176 -0.0150 -0.0399 38  HIS A NE2 
4932 N N   . SER D 30  ? 1.2148 1.0636 0.9976 -0.0197 0.0020  -0.0480 39  SER A N   
4933 C CA  . SER D 30  ? 1.3913 1.2493 1.1742 -0.0218 0.0054  -0.0483 39  SER A CA  
4934 C C   . SER D 30  ? 1.5353 1.3956 1.3225 -0.0228 0.0056  -0.0454 39  SER A C   
4935 O O   . SER D 30  ? 1.5824 1.4390 1.3731 -0.0211 0.0034  -0.0439 39  SER A O   
4936 C CB  . SER D 30  ? 1.4625 1.3279 1.2462 -0.0186 0.0074  -0.0530 39  SER A CB  
4937 O OG  . SER D 30  ? 1.6794 1.5449 1.4687 -0.0141 0.0058  -0.0545 39  SER A OG  
4938 N N   . VAL D 31  ? 1.3658 1.2326 1.1529 -0.0258 0.0081  -0.0445 40  VAL A N   
4939 C CA  . VAL D 31  ? 1.1891 1.0593 0.9800 -0.0270 0.0086  -0.0422 40  VAL A CA  
4940 C C   . VAL D 31  ? 1.3332 1.2130 1.1265 -0.0258 0.0110  -0.0443 40  VAL A C   
4941 O O   . VAL D 31  ? 1.5062 1.3909 1.2971 -0.0260 0.0130  -0.0464 40  VAL A O   
4942 C CB  . VAL D 31  ? 1.0294 0.8982 0.8190 -0.0319 0.0091  -0.0391 40  VAL A CB  
4943 C CG1 . VAL D 31  ? 1.2357 1.1086 1.0290 -0.0332 0.0098  -0.0375 40  VAL A CG1 
4944 C CG2 . VAL D 31  ? 1.3174 1.1768 1.1055 -0.0329 0.0069  -0.0370 40  VAL A CG2 
4945 N N   . ASN D 32  ? 1.2948 1.1776 1.0926 -0.0245 0.0106  -0.0436 41  ASN A N   
4946 C CA  . ASN D 32  ? 1.3069 1.1989 1.1078 -0.0234 0.0126  -0.0451 41  ASN A CA  
4947 C C   . ASN D 32  ? 1.2892 1.1852 1.0914 -0.0269 0.0136  -0.0424 41  ASN A C   
4948 O O   . ASN D 32  ? 1.5165 1.4089 1.3199 -0.0282 0.0121  -0.0401 41  ASN A O   
4949 C CB  . ASN D 32  ? 1.3059 1.1987 1.1117 -0.0190 0.0111  -0.0466 41  ASN A CB  
4950 C CG  . ASN D 32  ? 1.5863 1.4887 1.3957 -0.0174 0.0131  -0.0485 41  ASN A CG  
4951 O OD1 . ASN D 32  ? 1.5945 1.5029 1.4021 -0.0190 0.0158  -0.0495 41  ASN A OD1 
4952 N ND2 . ASN D 32  ? 1.5180 1.4220 1.3330 -0.0143 0.0115  -0.0488 41  ASN A ND2 
4953 N N   . LEU D 33  ? 1.1555 1.0592 0.9575 -0.0286 0.0160  -0.0429 42  LEU A N   
4954 C CA  . LEU D 33  ? 1.1701 1.0777 0.9735 -0.0321 0.0167  -0.0405 42  LEU A CA  
4955 C C   . LEU D 33  ? 1.3760 1.2913 1.1839 -0.0307 0.0174  -0.0408 42  LEU A C   
4956 O O   . LEU D 33  ? 1.6189 1.5359 1.4286 -0.0330 0.0171  -0.0388 42  LEU A O   
4957 C CB  . LEU D 33  ? 1.0809 0.9916 0.8813 -0.0360 0.0183  -0.0397 42  LEU A CB  
4958 C CG  . LEU D 33  ? 0.9967 0.9005 0.7931 -0.0387 0.0175  -0.0384 42  LEU A CG  
4959 C CD1 . LEU D 33  ? 1.0224 0.9312 0.8167 -0.0425 0.0189  -0.0374 42  LEU A CD1 
4960 C CD2 . LEU D 33  ? 1.2318 1.1289 1.0293 -0.0406 0.0157  -0.0361 42  LEU A CD2 
4961 N N   . LEU D 34  ? 1.4117 1.3316 1.2218 -0.0272 0.0182  -0.0434 43  LEU A N   
4962 C CA  . LEU D 34  ? 1.4495 1.3763 1.2648 -0.0256 0.0185  -0.0435 43  LEU A CA  
4963 C C   . LEU D 34  ? 1.4559 1.3791 1.2749 -0.0222 0.0160  -0.0437 43  LEU A C   
4964 O O   . LEU D 34  ? 1.2970 1.2132 1.1147 -0.0203 0.0142  -0.0443 43  LEU A O   
4965 C CB  . LEU D 34  ? 1.4018 1.3371 1.2187 -0.0237 0.0210  -0.0461 43  LEU A CB  
4966 C CG  . LEU D 34  ? 1.7188 1.6608 1.5333 -0.0271 0.0236  -0.0456 43  LEU A CG  
4967 C CD1 . LEU D 34  ? 1.6968 1.6471 1.5129 -0.0244 0.0261  -0.0489 43  LEU A CD1 
4968 C CD2 . LEU D 34  ? 1.9029 1.8488 1.7193 -0.0306 0.0236  -0.0424 43  LEU A CD2 
4969 N N   . GLU D 35  ? 1.4018 1.3303 1.2257 -0.0215 0.0156  -0.0429 44  GLU A N   
4970 C CA  . GLU D 35  ? 1.6226 1.5485 1.4507 -0.0188 0.0128  -0.0423 44  GLU A CA  
4971 C C   . GLU D 35  ? 1.4358 1.3694 1.2701 -0.0175 0.0127  -0.0421 44  GLU A C   
4972 O O   . GLU D 35  ? 1.2434 1.1829 1.0781 -0.0200 0.0142  -0.0409 44  GLU A O   
4973 C CB  . GLU D 35  ? 1.8197 1.7399 1.6459 -0.0214 0.0107  -0.0393 44  GLU A CB  
4974 C CG  . GLU D 35  ? 1.8537 1.7713 1.6836 -0.0193 0.0076  -0.0382 44  GLU A CG  
4975 C CD  . GLU D 35  ? 1.8441 1.7570 1.6717 -0.0221 0.0061  -0.0354 44  GLU A CD  
4976 O OE1 . GLU D 35  ? 1.9630 1.8748 1.7866 -0.0254 0.0076  -0.0348 44  GLU A OE1 
4977 O OE2 . GLU D 35  ? 1.8119 1.7227 1.6419 -0.0212 0.0033  -0.0338 44  GLU A OE2 
4978 N N   . ASP D 36  ? 1.3983 1.3314 1.2377 -0.0136 0.0106  -0.0431 45  ASP A N   
4979 C CA  . ASP D 36  ? 1.5364 1.4765 1.3829 -0.0117 0.0102  -0.0431 45  ASP A CA  
4980 C C   . ASP D 36  ? 1.6161 1.5540 1.4670 -0.0114 0.0063  -0.0402 45  ASP A C   
4981 O O   . ASP D 36  ? 1.5698 1.5118 1.4277 -0.0090 0.0049  -0.0402 45  ASP A O   
4982 C CB  . ASP D 36  ? 1.7220 1.6652 1.5725 -0.0071 0.0112  -0.0472 45  ASP A CB  
4983 C CG  . ASP D 36  ? 1.9033 1.8516 1.7502 -0.0078 0.0153  -0.0498 45  ASP A CG  
4984 O OD1 . ASP D 36  ? 1.7187 1.6697 1.5618 -0.0119 0.0171  -0.0478 45  ASP A OD1 
4985 O OD2 . ASP D 36  ? 2.0027 1.9527 1.8508 -0.0044 0.0167  -0.0539 45  ASP A OD2 
4986 N N   . LYS D 37  ? 1.6451 1.5770 1.4922 -0.0139 0.0045  -0.0376 46  LYS A N   
4987 C CA  . LYS D 37  ? 1.9461 1.8759 1.7965 -0.0140 0.0007  -0.0346 46  LYS A CA  
4988 C C   . LYS D 37  ? 1.8993 1.8348 1.7511 -0.0173 0.0005  -0.0318 46  LYS A C   
4989 O O   . LYS D 37  ? 1.7650 1.6995 1.6120 -0.0212 0.0012  -0.0301 46  LYS A O   
4990 C CB  . LYS D 37  ? 1.8732 1.7951 1.7189 -0.0155 -0.0009 -0.0331 46  LYS A CB  
4991 C CG  . LYS D 37  ? 1.7585 1.6737 1.6031 -0.0124 -0.0017 -0.0353 46  LYS A CG  
4992 C CD  . LYS D 37  ? 2.0939 2.0020 1.9343 -0.0144 -0.0033 -0.0330 46  LYS A CD  
4993 C CE  . LYS D 37  ? 2.0116 1.9125 1.8506 -0.0118 -0.0045 -0.0347 46  LYS A CE  
4994 N NZ  . LYS D 37  ? 1.8547 1.7492 1.6898 -0.0140 -0.0059 -0.0321 46  LYS A NZ  
4995 N N   . HIS D 38  ? 1.9264 1.8677 1.7850 -0.0157 -0.0006 -0.0313 47  HIS A N   
4996 C CA  . HIS D 38  ? 1.8325 1.7792 1.6933 -0.0186 -0.0015 -0.0283 47  HIS A CA  
4997 C C   . HIS D 38  ? 1.8503 1.7968 1.7171 -0.0177 -0.0060 -0.0255 47  HIS A C   
4998 O O   . HIS D 38  ? 1.7598 1.7060 1.6329 -0.0137 -0.0077 -0.0266 47  HIS A O   
4999 C CB  . HIS D 38  ? 1.7908 1.7455 1.6549 -0.0183 0.0009  -0.0294 47  HIS A CB  
5000 C CG  . HIS D 38  ? 2.0064 1.9643 1.8778 -0.0135 0.0008  -0.0318 47  HIS A CG  
5001 N ND1 . HIS D 38  ? 2.1595 2.1155 2.0300 -0.0102 0.0028  -0.0358 47  HIS A ND1 
5002 C CD2 . HIS D 38  ? 1.9065 1.8695 1.7866 -0.0115 -0.0010 -0.0310 47  HIS A CD2 
5003 C CE1 . HIS D 38  ? 2.2006 2.1606 2.0790 -0.0061 0.0024  -0.0378 47  HIS A CE1 
5004 N NE2 . HIS D 38  ? 2.2981 2.2623 2.1828 -0.0068 0.0000  -0.0349 47  HIS A NE2 
5005 N N   . ASN D 39  ? 1.8766 1.8234 1.7417 -0.0214 -0.0079 -0.0219 48  ASN A N   
5006 C CA  . ASN D 39  ? 1.7309 1.6769 1.6005 -0.0214 -0.0125 -0.0186 48  ASN A CA  
5007 C C   . ASN D 39  ? 1.6563 1.6084 1.5351 -0.0198 -0.0147 -0.0174 48  ASN A C   
5008 O O   . ASN D 39  ? 1.9663 1.9173 1.8519 -0.0171 -0.0183 -0.0163 48  ASN A O   
5009 C CB  . ASN D 39  ? 1.6439 1.5894 1.5083 -0.0263 -0.0137 -0.0153 48  ASN A CB  
5010 C CG  . ASN D 39  ? 1.7592 1.7111 1.6235 -0.0298 -0.0131 -0.0137 48  ASN A CG  
5011 O OD1 . ASN D 39  ? 1.9272 1.8830 1.7923 -0.0294 -0.0105 -0.0155 48  ASN A OD1 
5012 N ND2 . ASN D 39  ? 2.1642 2.1177 2.0277 -0.0334 -0.0158 -0.0101 48  ASN A ND2 
5013 N N   . GLY D 40  ? 1.8122 1.7707 1.6919 -0.0213 -0.0128 -0.0173 49  GLY A N   
5014 C CA  . GLY D 40  ? 1.7689 1.7335 1.6578 -0.0200 -0.0147 -0.0159 49  GLY A CA  
5015 C C   . GLY D 40  ? 1.9291 1.8988 1.8181 -0.0244 -0.0162 -0.0120 49  GLY A C   
5016 O O   . GLY D 40  ? 1.9229 1.8988 1.8172 -0.0243 -0.0160 -0.0115 49  GLY A O   
5017 N N   . LYS D 41  ? 1.8590 1.8263 1.7422 -0.0286 -0.0178 -0.0093 50  LYS A N   
5018 C CA  . LYS D 41  ? 1.6735 1.6452 1.5553 -0.0333 -0.0191 -0.0059 50  LYS A CA  
5019 C C   . LYS D 41  ? 1.6786 1.6489 1.5506 -0.0371 -0.0159 -0.0073 50  LYS A C   
5020 O O   . LYS D 41  ? 1.8512 1.8179 1.7187 -0.0359 -0.0126 -0.0106 50  LYS A O   
5021 C CB  . LYS D 41  ? 1.6572 1.6286 1.5413 -0.0354 -0.0242 -0.0014 50  LYS A CB  
5022 C CG  . LYS D 41  ? 1.8606 1.8342 1.7559 -0.0323 -0.0281 0.0005  50  LYS A CG  
5023 C CD  . LYS D 41  ? 1.8352 1.8087 1.7327 -0.0349 -0.0336 0.0056  50  LYS A CD  
5024 C CE  . LYS D 41  ? 1.9260 1.9015 1.8359 -0.0319 -0.0380 0.0078  50  LYS A CE  
5025 N NZ  . LYS D 41  ? 1.8662 1.8419 1.7791 -0.0348 -0.0439 0.0135  50  LYS A NZ  
5026 N N   . LEU D 42  ? 1.7475 1.7207 1.6167 -0.0418 -0.0172 -0.0047 51  LEU A N   
5027 C CA  . LEU D 42  ? 1.6980 1.6710 1.5595 -0.0454 -0.0145 -0.0062 51  LEU A CA  
5028 C C   . LEU D 42  ? 1.7781 1.7497 1.6342 -0.0495 -0.0164 -0.0042 51  LEU A C   
5029 O O   . LEU D 42  ? 1.8802 1.8560 1.7364 -0.0531 -0.0186 -0.0015 51  LEU A O   
5030 C CB  . LEU D 42  ? 1.4004 1.3795 1.2640 -0.0472 -0.0138 -0.0056 51  LEU A CB  
5031 C CG  . LEU D 42  ? 1.0198 1.0028 0.8890 -0.0441 -0.0118 -0.0070 51  LEU A CG  
5032 C CD1 . LEU D 42  ? 1.4362 1.4164 1.3028 -0.0415 -0.0077 -0.0110 51  LEU A CD1 
5033 C CD2 . LEU D 42  ? 1.4108 1.4001 1.2816 -0.0473 -0.0122 -0.0052 51  LEU A CD2 
5040 N N   . ASP D 44  ? 2.4299 2.3944 2.2671 -0.0565 -0.0115 -0.0089 53  ASP A N   
5041 C CA  . ASP D 44  ? 2.3937 2.3567 2.2246 -0.0597 -0.0092 -0.0115 53  ASP A CA  
5042 C C   . ASP D 44  ? 2.2183 2.1850 2.0460 -0.0643 -0.0111 -0.0099 53  ASP A C   
5043 O O   . ASP D 44  ? 1.9021 1.8738 1.7313 -0.0666 -0.0125 -0.0085 53  ASP A O   
5048 N N   . LEU D 45  ? 2.4041 2.3688 2.2275 -0.0659 -0.0111 -0.0101 54  LEU A N   
5049 C CA  . LEU D 45  ? 2.4777 2.4454 2.2961 -0.0707 -0.0116 -0.0103 54  LEU A CA  
5050 C C   . LEU D 45  ? 2.5329 2.4968 2.3459 -0.0717 -0.0086 -0.0143 54  LEU A C   
5051 O O   . LEU D 45  ? 2.3256 2.2915 2.1340 -0.0754 -0.0085 -0.0154 54  LEU A O   
5056 N N   . ASP D 46  ? 2.3751 2.3335 2.1888 -0.0685 -0.0062 -0.0166 55  ASP A N   
5057 C CA  . ASP D 46  ? 2.2421 2.1967 2.0521 -0.0693 -0.0034 -0.0206 55  ASP A CA  
5058 C C   . ASP D 46  ? 2.4082 2.3651 2.2163 -0.0725 -0.0026 -0.0231 55  ASP A C   
5059 O O   . ASP D 46  ? 2.3931 2.3510 2.1972 -0.0756 -0.0021 -0.0253 55  ASP A O   
5060 C CB  . ASP D 46  ? 2.2419 2.1907 2.0538 -0.0656 -0.0014 -0.0221 55  ASP A CB  
5061 C CG  . ASP D 46  ? 2.4124 2.3567 2.2215 -0.0662 0.0011  -0.0258 55  ASP A CG  
5062 O OD1 . ASP D 46  ? 2.6963 2.6417 2.5021 -0.0693 0.0017  -0.0277 55  ASP A OD1 
5063 O OD2 . ASP D 46  ? 2.4985 2.4383 2.3089 -0.0638 0.0026  -0.0268 55  ASP A OD2 
5064 N N   . GLY D 47  a 2.3311 2.2892 2.1422 -0.0718 -0.0027 -0.0230 55  GLY A N   
5065 C CA  . GLY D 47  a 2.3387 2.3006 2.1491 -0.0750 -0.0033 -0.0238 55  GLY A CA  
5066 C C   . GLY D 47  a 2.1175 2.0852 1.9291 -0.0766 -0.0063 -0.0201 55  GLY A C   
5067 O O   . GLY D 47  a 2.0526 2.0213 1.8673 -0.0745 -0.0078 -0.0168 55  GLY A O   
5068 N N   . VAL D 48  ? 1.9713 1.9427 1.7808 -0.0805 -0.0073 -0.0206 56  VAL A N   
5069 C CA  . VAL D 48  ? 2.1443 2.1214 1.9543 -0.0829 -0.0104 -0.0169 56  VAL A CA  
5070 C C   . VAL D 48  ? 1.7988 1.7779 1.6154 -0.0801 -0.0119 -0.0133 56  VAL A C   
5071 O O   . VAL D 48  ? 1.7239 1.7022 1.5438 -0.0781 -0.0106 -0.0141 56  VAL A O   
5072 C CB  . VAL D 48  ? 2.3699 2.3504 2.1768 -0.0874 -0.0113 -0.0184 56  VAL A CB  
5073 C CG1 . VAL D 48  ? 2.2621 2.2486 2.0698 -0.0901 -0.0148 -0.0142 56  VAL A CG1 
5074 C CG2 . VAL D 48  ? 2.3993 2.3782 2.2000 -0.0900 -0.0097 -0.0227 56  VAL A CG2 
5075 N N   . LYS D 49  ? 1.9952 1.9772 1.8142 -0.0799 -0.0147 -0.0092 57  LYS A N   
5076 C CA  . LYS D 49  ? 1.9412 1.9252 1.7675 -0.0768 -0.0163 -0.0058 57  LYS A CA  
5077 C C   . LYS D 49  ? 1.9409 1.9275 1.7709 -0.0767 -0.0161 -0.0058 57  LYS A C   
5078 O O   . LYS D 49  ? 2.2755 2.2649 2.1033 -0.0804 -0.0168 -0.0061 57  LYS A O   
5079 C CB  . LYS D 49  ? 1.9434 1.9315 1.7717 -0.0786 -0.0204 -0.0011 57  LYS A CB  
5080 C CG  . LYS D 49  ? 1.9555 1.9418 1.7820 -0.0783 -0.0213 0.0002  57  LYS A CG  
5081 C CD  . LYS D 49  ? 1.7812 1.7723 1.6104 -0.0807 -0.0259 0.0055  57  LYS A CD  
5082 C CE  . LYS D 49  ? 1.7640 1.7537 1.5919 -0.0807 -0.0273 0.0075  57  LYS A CE  
5083 N NZ  . LYS D 49  ? 1.9831 1.9778 1.8140 -0.0835 -0.0322 0.0133  57  LYS A NZ  
5084 N N   . PRO D 50  ? 1.6555 1.6419 1.4913 -0.0725 -0.0151 -0.0054 58  PRO A N   
5085 C CA  . PRO D 50  ? 1.6054 1.5945 1.4445 -0.0723 -0.0143 -0.0057 58  PRO A CA  
5086 C C   . PRO D 50  ? 1.7163 1.7114 1.5580 -0.0754 -0.0173 -0.0025 58  PRO A C   
5087 O O   . PRO D 50  ? 1.9013 1.8990 1.7446 -0.0767 -0.0204 0.0008  58  PRO A O   
5088 C CB  . PRO D 50  ? 1.5885 1.5774 1.4339 -0.0671 -0.0131 -0.0054 58  PRO A CB  
5089 C CG  . PRO D 50  ? 1.6640 1.6511 1.5108 -0.0651 -0.0149 -0.0037 58  PRO A CG  
5090 C CD  . PRO D 50  ? 1.6992 1.6829 1.5387 -0.0679 -0.0148 -0.0050 58  PRO A CD  
5091 N N   . LEU D 51  ? 1.5705 1.5677 1.4126 -0.0771 -0.0166 -0.0032 59  LEU A N   
5092 C CA  . LEU D 51  ? 1.5647 1.5677 1.4106 -0.0794 -0.0192 0.0001  59  LEU A CA  
5093 C C   . LEU D 51  ? 1.4943 1.5006 1.3490 -0.0753 -0.0194 0.0025  59  LEU A C   
5094 O O   . LEU D 51  ? 1.5908 1.5995 1.4495 -0.0738 -0.0179 0.0023  59  LEU A O   
5095 C CB  . LEU D 51  ? 1.8358 1.8398 1.6799 -0.0822 -0.0186 -0.0014 59  LEU A CB  
5096 C CG  . LEU D 51  ? 2.3553 2.3566 2.1918 -0.0864 -0.0187 -0.0043 59  LEU A CG  
5097 C CD1 . LEU D 51  ? 2.0911 2.0928 1.9271 -0.0886 -0.0182 -0.0059 59  LEU A CD1 
5098 C CD2 . LEU D 51  ? 2.3868 2.3910 2.2207 -0.0903 -0.0219 -0.0021 59  LEU A CD2 
5099 N N   . ILE D 52  ? 1.7262 1.7329 1.5844 -0.0735 -0.0213 0.0048  60  ILE A N   
5100 C CA  . ILE D 52  ? 1.7243 1.7344 1.5919 -0.0696 -0.0218 0.0068  60  ILE A CA  
5101 C C   . ILE D 52  ? 1.8356 1.8520 1.7080 -0.0722 -0.0246 0.0105  60  ILE A C   
5102 O O   . ILE D 52  ? 2.0151 2.0336 1.8876 -0.0754 -0.0284 0.0138  60  ILE A O   
5103 C CB  . ILE D 52  ? 1.8418 1.8502 1.7129 -0.0667 -0.0235 0.0082  60  ILE A CB  
5104 C CG1 . ILE D 52  ? 1.8255 1.8278 1.6928 -0.0635 -0.0205 0.0045  60  ILE A CG1 
5105 C CG2 . ILE D 52  ? 1.7792 1.7921 1.6612 -0.0632 -0.0249 0.0105  60  ILE A CG2 
5106 C CD1 . ILE D 52  ? 1.8928 1.8924 1.7623 -0.0612 -0.0226 0.0058  60  ILE A CD1 
5107 N N   . LEU D 53  ? 1.7163 1.7361 1.5926 -0.0712 -0.0230 0.0103  61  LEU A N   
5108 C CA  . LEU D 53  ? 1.8301 1.8564 1.7134 -0.0725 -0.0255 0.0141  61  LEU A CA  
5109 C C   . LEU D 53  ? 1.8105 1.8392 1.7031 -0.0688 -0.0272 0.0165  61  LEU A C   
5110 O O   . LEU D 53  ? 1.5226 1.5495 1.4182 -0.0639 -0.0250 0.0142  61  LEU A O   
5111 C CB  . LEU D 53  ? 1.8051 1.8347 1.6908 -0.0719 -0.0230 0.0132  61  LEU A CB  
5112 C CG  . LEU D 53  ? 1.5631 1.5899 1.4407 -0.0754 -0.0215 0.0107  61  LEU A CG  
5113 C CD1 . LEU D 53  ? 1.5886 1.6196 1.4697 -0.0754 -0.0198 0.0109  61  LEU A CD1 
5114 C CD2 . LEU D 53  ? 1.7258 1.7519 1.5978 -0.0809 -0.0248 0.0120  61  LEU A CD2 
5115 N N   . ARG D 54  ? 1.8531 1.8857 1.7505 -0.0712 -0.0315 0.0210  62  ARG A N   
5116 C CA  . ARG D 54  ? 1.7315 1.7668 1.6396 -0.0676 -0.0336 0.0234  62  ARG A CA  
5117 C C   . ARG D 54  ? 1.8318 1.8714 1.7482 -0.0633 -0.0308 0.0222  62  ARG A C   
5118 O O   . ARG D 54  ? 1.8593 1.8968 1.7760 -0.0588 -0.0272 0.0184  62  ARG A O   
5119 C CB  . ARG D 54  ? 1.8610 1.9001 1.7734 -0.0714 -0.0391 0.0290  62  ARG A CB  
5120 C CG  . ARG D 54  ? 2.1802 2.2161 2.0854 -0.0755 -0.0422 0.0306  62  ARG A CG  
5121 C CD  . ARG D 54  ? 2.4335 2.4737 2.3438 -0.0793 -0.0479 0.0366  62  ARG A CD  
5122 N NE  . ARG D 54  ? 2.5661 2.6044 2.4688 -0.0839 -0.0508 0.0384  62  ARG A NE  
5123 C CZ  . ARG D 54  ? 2.7505 2.7923 2.6549 -0.0886 -0.0560 0.0437  62  ARG A CZ  
5124 N NH1 . ARG D 54  ? 2.8632 2.9100 2.7775 -0.0889 -0.0594 0.0481  62  ARG A NH1 
5125 N NH2 . ARG D 54  ? 2.7109 2.7514 2.6069 -0.0931 -0.0580 0.0448  62  ARG A NH2 
5126 N N   . ASP D 55  ? 1.8971 1.9429 1.8199 -0.0647 -0.0323 0.0254  63  ASP A N   
5127 C CA  . ASP D 55  ? 2.1228 2.1736 2.0529 -0.0610 -0.0292 0.0241  63  ASP A CA  
5128 C C   . ASP D 55  ? 2.1378 2.1915 2.0642 -0.0641 -0.0274 0.0241  63  ASP A C   
5129 O O   . ASP D 55  ? 2.0594 2.1172 1.9900 -0.0613 -0.0241 0.0227  63  ASP A O   
5130 C CB  . ASP D 55  ? 2.3068 2.3636 2.2503 -0.0589 -0.0319 0.0276  63  ASP A CB  
5131 C CG  . ASP D 55  ? 2.2953 2.3498 2.2449 -0.0545 -0.0332 0.0269  63  ASP A CG  
5132 O OD1 . ASP D 55  ? 2.3304 2.3791 2.2744 -0.0522 -0.0311 0.0232  63  ASP A OD1 
5133 O OD2 . ASP D 55  ? 2.5187 2.5769 2.4791 -0.0535 -0.0367 0.0303  63  ASP A OD2 
5134 N N   . CYS D 56  ? 2.0127 2.0647 1.9316 -0.0697 -0.0295 0.0256  64  CYS A N   
5135 C CA  . CYS D 56  ? 2.2000 2.2546 2.1162 -0.0729 -0.0286 0.0259  64  CYS A CA  
5136 C C   . CYS D 56  ? 2.1295 2.1818 2.0410 -0.0709 -0.0238 0.0215  64  CYS A C   
5137 O O   . CYS D 56  ? 2.2110 2.2572 2.1159 -0.0697 -0.0219 0.0180  64  CYS A O   
5138 C CB  . CYS D 56  ? 2.2056 2.2576 2.1136 -0.0791 -0.0318 0.0273  64  CYS A CB  
5139 S SG  . CYS D 56  ? 2.3308 2.3743 2.2275 -0.0803 -0.0315 0.0239  64  CYS A SG  
5140 N N   . SER D 57  ? 2.0991 2.1566 2.0143 -0.0707 -0.0220 0.0221  65  SER A N   
5141 C CA  . SER D 57  ? 2.0395 2.0955 1.9499 -0.0702 -0.0181 0.0188  65  SER A CA  
5142 C C   . SER D 57  ? 1.9260 1.9761 1.8262 -0.0749 -0.0192 0.0175  65  SER A C   
5143 O O   . SER D 57  ? 1.8781 1.9275 1.7759 -0.0791 -0.0227 0.0196  65  SER A O   
5144 C CB  . SER D 57  ? 1.7802 1.8440 1.6968 -0.0702 -0.0167 0.0207  65  SER A CB  
5145 O OG  . SER D 57  ? 1.8048 1.8718 1.7228 -0.0748 -0.0202 0.0246  65  SER A OG  
5146 N N   . VAL D 58  ? 1.8342 1.8799 1.7286 -0.0741 -0.0161 0.0138  66  VAL A N   
5147 C CA  . VAL D 58  ? 1.8171 1.8575 1.7031 -0.0783 -0.0168 0.0121  66  VAL A CA  
5148 C C   . VAL D 58  ? 1.6166 1.6609 1.5039 -0.0826 -0.0191 0.0148  66  VAL A C   
5149 O O   . VAL D 58  ? 1.7229 1.7641 1.6049 -0.0869 -0.0217 0.0146  66  VAL A O   
5150 C CB  . VAL D 58  ? 1.9213 1.9573 1.8027 -0.0767 -0.0132 0.0083  66  VAL A CB  
5151 C CG1 . VAL D 58  ? 2.1609 2.1920 2.0352 -0.0809 -0.0142 0.0065  66  VAL A CG1 
5152 C CG2 . VAL D 58  ? 2.1902 2.2213 2.0692 -0.0730 -0.0116 0.0056  66  VAL A CG2 
5153 N N   . ALA D 59  ? 1.4251 1.4765 1.3196 -0.0816 -0.0183 0.0173  67  ALA A N   
5154 C CA  . ALA D 59  ? 1.6444 1.7003 1.5415 -0.0856 -0.0209 0.0206  67  ALA A CA  
5155 C C   . ALA D 59  ? 1.7436 1.8001 1.6413 -0.0886 -0.0252 0.0235  67  ALA A C   
5156 O O   . ALA D 59  ? 1.8169 1.8712 1.7099 -0.0933 -0.0281 0.0239  67  ALA A O   
5157 C CB  . ALA D 59  ? 1.7879 1.8523 1.6936 -0.0835 -0.0191 0.0232  67  ALA A CB  
5158 N N   . GLY D 60  ? 1.7188 1.7782 1.6221 -0.0861 -0.0260 0.0255  68  GLY A N   
5159 C CA  . GLY D 60  ? 1.6481 1.7087 1.5526 -0.0892 -0.0305 0.0289  68  GLY A CA  
5160 C C   . GLY D 60  ? 1.5263 1.5802 1.4211 -0.0928 -0.0325 0.0270  68  GLY A C   
5161 O O   . GLY D 60  ? 1.8260 1.8802 1.7183 -0.0976 -0.0362 0.0289  68  GLY A O   
5162 N N   . TRP D 61  ? 1.2113 1.2595 1.1006 -0.0905 -0.0301 0.0230  69  TRP A N   
5163 C CA  . TRP D 61  ? 1.2771 1.3193 1.1569 -0.0937 -0.0314 0.0205  69  TRP A CA  
5164 C C   . TRP D 61  ? 1.4764 1.5166 1.3506 -0.0981 -0.0321 0.0188  69  TRP A C   
5165 O O   . TRP D 61  ? 1.6603 1.6994 1.5297 -0.1026 -0.0352 0.0191  69  TRP A O   
5166 C CB  . TRP D 61  ? 1.4461 1.4827 1.3217 -0.0903 -0.0282 0.0165  69  TRP A CB  
5167 C CG  . TRP D 61  ? 1.8818 1.9129 1.7483 -0.0931 -0.0290 0.0139  69  TRP A CG  
5168 C CD1 . TRP D 61  ? 2.3031 2.3334 2.1673 -0.0942 -0.0312 0.0150  69  TRP A CD1 
5169 C CD2 . TRP D 61  ? 1.9796 2.0056 1.8384 -0.0951 -0.0277 0.0096  69  TRP A CD2 
5170 N NE1 . TRP D 61  ? 2.5805 2.6060 2.4356 -0.0969 -0.0310 0.0116  69  TRP A NE1 
5171 C CE2 . TRP D 61  ? 2.3555 2.3782 2.2075 -0.0973 -0.0288 0.0080  69  TRP A CE2 
5172 C CE3 . TRP D 61  ? 1.7947 1.8189 1.6524 -0.0955 -0.0259 0.0072  69  TRP A CE3 
5173 C CZ2 . TRP D 61  ? 2.3814 2.3990 2.2257 -0.0995 -0.0278 0.0035  69  TRP A CZ2 
5174 C CZ3 . TRP D 61  ? 2.1038 2.1224 1.9542 -0.0976 -0.0253 0.0030  69  TRP A CZ3 
5175 C CH2 . TRP D 61  ? 2.3192 2.3347 2.1632 -0.0994 -0.0261 0.0009  69  TRP A CH2 
5176 N N   . LEU D 62  ? 1.4780 1.5178 1.3530 -0.0968 -0.0295 0.0171  70  LEU A N   
5177 C CA  . LEU D 62  ? 1.3680 1.4062 1.2396 -0.1008 -0.0306 0.0159  70  LEU A CA  
5178 C C   . LEU D 62  ? 1.4322 1.4756 1.3078 -0.1044 -0.0344 0.0202  70  LEU A C   
5179 O O   . LEU D 62  ? 1.3507 1.3923 1.2218 -0.1090 -0.0375 0.0198  70  LEU A O   
5180 C CB  . LEU D 62  ? 1.3037 1.3414 1.1768 -0.0987 -0.0274 0.0142  70  LEU A CB  
5181 C CG  . LEU D 62  ? 1.4803 1.5120 1.3489 -0.0957 -0.0239 0.0098  70  LEU A CG  
5182 C CD1 . LEU D 62  ? 1.6376 1.6705 1.5089 -0.0939 -0.0212 0.0093  70  LEU A CD1 
5183 C CD2 . LEU D 62  ? 1.8416 1.8667 1.7022 -0.0989 -0.0250 0.0059  70  LEU A CD2 
5184 N N   . LEU D 63  ? 1.4581 1.5082 1.3423 -0.1024 -0.0344 0.0243  71  LEU A N   
5185 C CA  . LEU D 63  ? 1.4223 1.4780 1.3115 -0.1057 -0.0379 0.0290  71  LEU A CA  
5186 C C   . LEU D 63  ? 1.5001 1.5568 1.3888 -0.1084 -0.0419 0.0317  71  LEU A C   
5187 O O   . LEU D 63  ? 1.6518 1.7130 1.5448 -0.1112 -0.0452 0.0360  71  LEU A O   
5188 C CB  . LEU D 63  ? 1.4226 1.4858 1.3220 -0.1024 -0.0363 0.0324  71  LEU A CB  
5189 C CG  . LEU D 63  ? 1.4780 1.5422 1.3786 -0.1008 -0.0329 0.0310  71  LEU A CG  
5190 C CD1 . LEU D 63  ? 1.8438 1.9164 1.7542 -0.0972 -0.0307 0.0340  71  LEU A CD1 
5191 C CD2 . LEU D 63  ? 1.4987 1.5616 1.3965 -0.1056 -0.0353 0.0313  71  LEU A CD2 
5192 N N   . GLY D 64  ? 1.5687 1.6214 1.4524 -0.1079 -0.0418 0.0296  72  GLY A N   
5193 C CA  . GLY D 64  ? 1.7680 1.8217 1.6503 -0.1110 -0.0457 0.0323  72  GLY A CA  
5194 C C   . GLY D 64  ? 1.7961 1.8563 1.6885 -0.1098 -0.0478 0.0380  72  GLY A C   
5195 O O   . GLY D 64  ? 1.6504 1.7142 1.5450 -0.1138 -0.0519 0.0420  72  GLY A O   
5196 N N   . ASN D 65  ? 1.8112 1.8732 1.7101 -0.1044 -0.0451 0.0382  73  ASN A N   
5197 C CA  . ASN D 65  ? 1.7742 1.8423 1.6837 -0.1027 -0.0470 0.0431  73  ASN A CA  
5198 C C   . ASN D 65  ? 1.8310 1.8985 1.7389 -0.1059 -0.0515 0.0459  73  ASN A C   
5199 O O   . ASN D 65  ? 2.1147 2.1774 2.0150 -0.1065 -0.0514 0.0433  73  ASN A O   
5200 C CB  . ASN D 65  ? 1.9573 2.0266 1.8735 -0.0960 -0.0432 0.0416  73  ASN A CB  
5201 C CG  . ASN D 65  ? 2.3369 2.4002 2.2474 -0.0936 -0.0414 0.0379  73  ASN A CG  
5202 O OD1 . ASN D 65  ? 2.8912 2.9488 2.7917 -0.0956 -0.0406 0.0344  73  ASN A OD1 
5203 N ND2 . ASN D 65  ? 2.6443 2.7088 2.5617 -0.0892 -0.0410 0.0386  73  ASN A ND2 
5204 N N   . PRO D 66  ? 1.7822 1.8550 1.6971 -0.1082 -0.0557 0.0515  74  PRO A N   
5205 C CA  . PRO D 66  ? 1.8702 1.9429 1.7832 -0.1122 -0.0604 0.0548  74  PRO A CA  
5206 C C   . PRO D 66  ? 2.0875 2.1587 2.0030 -0.1086 -0.0601 0.0546  74  PRO A C   
5207 O O   . PRO D 66  ? 2.1681 2.2360 2.0763 -0.1113 -0.0618 0.0541  74  PRO A O   
5208 C CB  . PRO D 66  ? 2.2761 2.3554 2.1986 -0.1145 -0.0646 0.0611  74  PRO A CB  
5209 C CG  . PRO D 66  ? 2.5099 2.5933 2.4423 -0.1096 -0.0613 0.0612  74  PRO A CG  
5210 C CD  . PRO D 66  ? 2.1741 2.2535 2.0993 -0.1076 -0.0563 0.0554  74  PRO A CD  
5211 N N   . MET D 67  ? 2.0718 2.1453 1.9975 -0.1028 -0.0579 0.0549  75  MET A N   
5212 C CA  . MET D 67  ? 1.9200 1.9911 1.8477 -0.0987 -0.0570 0.0536  75  MET A CA  
5213 C C   . MET D 67  ? 1.9266 1.9913 1.8443 -0.0967 -0.0525 0.0473  75  MET A C   
5214 O O   . MET D 67  ? 2.0364 2.0997 1.9496 -0.0964 -0.0491 0.0439  75  MET A O   
5215 C CB  . MET D 67  ? 1.7926 1.8678 1.7339 -0.0926 -0.0556 0.0546  75  MET A CB  
5216 C CG  . MET D 67  ? 1.6911 1.7726 1.6440 -0.0940 -0.0603 0.0610  75  MET A CG  
5217 S SD  . MET D 67  ? 2.2178 2.2985 2.1707 -0.0985 -0.0671 0.0661  75  MET A SD  
5218 C CE  . MET D 67  ? 1.7663 1.8436 1.7237 -0.0922 -0.0655 0.0636  75  MET A CE  
5219 N N   . CYS D 68  ? 2.1506 2.2115 2.0654 -0.0956 -0.0528 0.0462  76  CYS A N   
5220 C CA  . CYS D 68  ? 2.3272 2.3818 2.2326 -0.0939 -0.0490 0.0408  76  CYS A CA  
5221 C C   . CYS D 68  ? 2.1528 2.2045 2.0465 -0.0987 -0.0483 0.0380  76  CYS A C   
5222 O O   . CYS D 68  ? 2.0103 2.0574 1.8973 -0.0972 -0.0445 0.0331  76  CYS A O   
5223 C CB  . CYS D 68  ? 2.1820 2.2357 2.0913 -0.0876 -0.0439 0.0369  76  CYS A CB  
5224 S SG  . CYS D 68  ? 2.1131 2.1689 2.0350 -0.0811 -0.0438 0.0381  76  CYS A SG  
5225 N N   . ASP D 69  ? 2.0464 2.1007 1.9380 -0.1044 -0.0521 0.0410  77  ASP A N   
5226 C CA  . ASP D 69  ? 2.0257 2.0772 1.9062 -0.1092 -0.0522 0.0382  77  ASP A CA  
5227 C C   . ASP D 69  ? 2.0499 2.0974 1.9209 -0.1112 -0.0523 0.0358  77  ASP A C   
5228 O O   . ASP D 69  ? 2.1465 2.1917 2.0082 -0.1151 -0.0521 0.0328  77  ASP A O   
5229 C CB  . ASP D 69  ? 2.0608 2.1163 1.9416 -0.1150 -0.0567 0.0422  77  ASP A CB  
5230 C CG  . ASP D 69  ? 1.9659 2.0242 1.8477 -0.1185 -0.0616 0.0471  77  ASP A CG  
5231 O OD1 . ASP D 69  ? 1.9256 1.9849 1.8142 -0.1154 -0.0623 0.0496  77  ASP A OD1 
5232 O OD2 . ASP D 69  ? 1.8135 1.8727 1.6890 -0.1246 -0.0649 0.0484  77  ASP A OD2 
5233 N N   . GLU D 70  ? 1.8917 1.9386 1.7654 -0.1087 -0.0527 0.0371  78  GLU A N   
5234 C CA  . GLU D 70  ? 1.8501 1.8943 1.7155 -0.1111 -0.0533 0.0359  78  GLU A CA  
5235 C C   . GLU D 70  ? 1.8377 1.8764 1.6937 -0.1104 -0.0489 0.0293  78  GLU A C   
5236 O O   . GLU D 70  ? 1.9395 1.9766 1.7865 -0.1139 -0.0492 0.0273  78  GLU A O   
5237 C CB  . GLU D 70  ? 2.0878 2.1319 1.9590 -0.1077 -0.0543 0.0384  78  GLU A CB  
5238 C CG  . GLU D 70  ? 2.3948 2.4443 2.2754 -0.1091 -0.0595 0.0453  78  GLU A CG  
5239 C CD  . GLU D 70  ? 2.7000 2.7490 2.5878 -0.1053 -0.0607 0.0475  78  GLU A CD  
5240 O OE1 . GLU D 70  ? 2.5929 2.6375 2.4791 -0.1009 -0.0571 0.0436  78  GLU A OE1 
5241 O OE2 . GLU D 70  ? 2.7963 2.8491 2.6918 -0.1067 -0.0655 0.0533  78  GLU A OE2 
5242 N N   . PHE D 71  ? 1.8467 1.8830 1.7050 -0.1060 -0.0449 0.0259  79  PHE A N   
5243 C CA  . PHE D 71  ? 1.7222 1.7531 1.5733 -0.1048 -0.0407 0.0200  79  PHE A CA  
5244 C C   . PHE D 71  ? 1.9062 1.9364 1.7519 -0.1085 -0.0405 0.0172  79  PHE A C   
5245 O O   . PHE D 71  ? 1.8368 1.8640 1.6819 -0.1065 -0.0374 0.0136  79  PHE A O   
5246 C CB  . PHE D 71  ? 1.6196 1.6483 1.4758 -0.0986 -0.0369 0.0180  79  PHE A CB  
5247 C CG  . PHE D 71  ? 1.9018 1.9299 1.7627 -0.0945 -0.0368 0.0195  79  PHE A CG  
5248 C CD1 . PHE D 71  ? 2.2673 2.2910 2.1230 -0.0934 -0.0354 0.0171  79  PHE A CD1 
5249 C CD2 . PHE D 71  ? 1.8373 1.8692 1.7084 -0.0914 -0.0380 0.0231  79  PHE A CD2 
5250 C CE1 . PHE D 71  ? 2.1790 2.2019 2.0393 -0.0897 -0.0357 0.0186  79  PHE A CE1 
5251 C CE2 . PHE D 71  ? 1.8287 1.8598 1.7048 -0.0875 -0.0382 0.0241  79  PHE A CE2 
5252 C CZ  . PHE D 71  ? 1.9849 2.0113 1.8556 -0.0866 -0.0373 0.0220  79  PHE A CZ  
5253 N N   . ILE D 72  ? 1.8517 1.8844 1.6936 -0.1141 -0.0440 0.0188  80  ILE A N   
5254 C CA  . ILE D 72  ? 1.7434 1.7752 1.5810 -0.1175 -0.0442 0.0160  80  ILE A CA  
5255 C C   . ILE D 72  ? 1.7132 1.7398 1.5421 -0.1181 -0.0414 0.0096  80  ILE A C   
5256 O O   . ILE D 72  ? 1.9441 1.9675 1.7722 -0.1171 -0.0392 0.0059  80  ILE A O   
5257 C CB  . ILE D 72  ? 1.9930 2.0291 1.8290 -0.1235 -0.0490 0.0195  80  ILE A CB  
5258 C CG1 . ILE D 72  ? 2.0737 2.1147 1.9194 -0.1230 -0.0515 0.0251  80  ILE A CG1 
5259 C CG2 . ILE D 72  ? 2.1511 2.1850 1.9789 -0.1279 -0.0493 0.0150  80  ILE A CG2 
5260 C CD1 . ILE D 72  ? 2.2113 2.2571 2.0576 -0.1281 -0.0567 0.0303  80  ILE A CD1 
5261 N N   . ASN D 73  ? 1.5018 1.5276 1.3244 -0.1198 -0.0415 0.0084  81  ASN A N   
5262 C CA  . ASN D 73  ? 1.5689 1.5903 1.3834 -0.1204 -0.0388 0.0022  81  ASN A CA  
5263 C C   . ASN D 73  ? 1.6710 1.6902 1.4849 -0.1169 -0.0364 0.0017  81  ASN A C   
5264 O O   . ASN D 73  ? 1.8918 1.9134 1.7036 -0.1186 -0.0382 0.0042  81  ASN A O   
5265 C CB  . ASN D 73  ? 1.3504 1.3737 1.1568 -0.1266 -0.0412 0.0006  81  ASN A CB  
5266 C CG  . ASN D 73  ? 1.4263 1.4500 1.2320 -0.1299 -0.0430 -0.0007 81  ASN A CG  
5267 O OD1 . ASN D 73  ? 1.6073 1.6284 1.4166 -0.1277 -0.0416 -0.0025 81  ASN A OD1 
5268 N ND2 . ASN D 73  ? 1.4371 1.4643 1.2382 -0.1355 -0.0465 0.0003  81  ASN A ND2 
5269 N N   . VAL D 74  ? 1.5183 1.5330 1.3340 -0.1124 -0.0327 -0.0013 82  VAL A N   
5270 C CA  . VAL D 74  ? 1.6116 1.6235 1.4269 -0.1088 -0.0304 -0.0020 82  VAL A CA  
5271 C C   . VAL D 74  ? 1.6320 1.6382 1.4445 -0.1065 -0.0265 -0.0078 82  VAL A C   
5272 O O   . VAL D 74  ? 1.8644 1.8687 1.6790 -0.1056 -0.0253 -0.0097 82  VAL A O   
5273 C CB  . VAL D 74  ? 1.6892 1.7022 1.5129 -0.1042 -0.0306 0.0021  82  VAL A CB  
5274 C CG1 . VAL D 74  ? 2.1780 2.1875 2.0013 -0.1005 -0.0284 0.0011  82  VAL A CG1 
5275 C CG2 . VAL D 74  ? 1.7098 1.7284 1.5380 -0.1061 -0.0347 0.0081  82  VAL A CG2 
5276 N N   . PRO D 75  ? 1.6134 1.6170 1.4214 -0.1059 -0.0247 -0.0103 83  PRO A N   
5277 C CA  . PRO D 75  ? 1.7269 1.7250 1.5320 -0.1044 -0.0212 -0.0159 83  PRO A CA  
5278 C C   . PRO D 75  ? 1.8422 1.8361 1.6501 -0.0993 -0.0184 -0.0164 83  PRO A C   
5279 O O   . PRO D 75  ? 1.7081 1.6983 1.5123 -0.0986 -0.0161 -0.0200 83  PRO A O   
5280 C CB  . PRO D 75  ? 1.7075 1.7061 1.5049 -0.1079 -0.0211 -0.0189 83  PRO A CB  
5281 C CG  . PRO D 75  ? 1.6667 1.6696 1.4640 -0.1090 -0.0235 -0.0139 83  PRO A CG  
5282 C CD  . PRO D 75  ? 1.4705 1.4772 1.2738 -0.1091 -0.0265 -0.0088 83  PRO A CD  
5312 N N   . TYR D 79  ? 2.0469 2.0301 1.8771 -0.0777 -0.0081 -0.0155 86  TYR A N   
5313 C CA  . TYR D 79  ? 1.9478 1.9341 1.7834 -0.0757 -0.0075 -0.0139 86  TYR A CA  
5314 C C   . TYR D 79  ? 1.8035 1.7956 1.6442 -0.0751 -0.0096 -0.0101 86  TYR A C   
5315 O O   . TYR D 79  ? 1.9745 1.9679 1.8145 -0.0762 -0.0118 -0.0083 86  TYR A O   
5316 C CB  . TYR D 79  ? 1.5924 1.5757 1.4295 -0.0715 -0.0048 -0.0150 86  TYR A CB  
5317 C CG  . TYR D 79  ? 1.4548 1.4369 1.2930 -0.0681 -0.0049 -0.0141 86  TYR A CG  
5318 C CD1 . TYR D 79  ? 1.4726 1.4583 1.3167 -0.0648 -0.0049 -0.0122 86  TYR A CD1 
5319 C CD2 . TYR D 79  ? 1.4286 1.4064 1.2628 -0.0681 -0.0051 -0.0152 86  TYR A CD2 
5320 C CE1 . TYR D 79  ? 1.4331 1.4174 1.2790 -0.0615 -0.0054 -0.0116 86  TYR A CE1 
5321 C CE2 . TYR D 79  ? 1.7292 1.7059 1.5651 -0.0651 -0.0056 -0.0140 86  TYR A CE2 
5322 C CZ  . TYR D 79  ? 1.5652 1.5449 1.4071 -0.0618 -0.0059 -0.0123 86  TYR A CZ  
5323 O OH  . TYR D 79  ? 1.3761 1.3545 1.2206 -0.0586 -0.0069 -0.0113 86  TYR A OH  
5324 N N   . ILE D 80  ? 1.4512 1.4471 1.2973 -0.0731 -0.0088 -0.0086 87  ILE A N   
5325 C CA  . ILE D 80  ? 1.6547 1.6568 1.5071 -0.0724 -0.0107 -0.0051 87  ILE A CA  
5326 C C   . ILE D 80  ? 1.3536 1.3569 1.2114 -0.0673 -0.0091 -0.0048 87  ILE A C   
5327 O O   . ILE D 80  ? 1.3650 1.3669 1.2228 -0.0650 -0.0062 -0.0068 87  ILE A O   
5328 C CB  . ILE D 80  ? 1.5382 1.5452 1.3932 -0.0751 -0.0115 -0.0035 87  ILE A CB  
5329 C CG1 . ILE D 80  ? 1.6978 1.7037 1.5478 -0.0802 -0.0137 -0.0039 87  ILE A CG1 
5330 C CG2 . ILE D 80  ? 1.6138 1.6275 1.4763 -0.0739 -0.0130 0.0002  87  ILE A CG2 
5331 C CD1 . ILE D 80  ? 1.4856 1.4948 1.3372 -0.0831 -0.0146 -0.0030 87  ILE A CD1 
5332 N N   . VAL D 81  ? 1.2694 1.2755 1.1320 -0.0657 -0.0111 -0.0023 88  VAL A N   
5333 C CA  . VAL D 81  ? 1.1342 1.1421 1.0033 -0.0608 -0.0101 -0.0021 88  VAL A CA  
5334 C C   . VAL D 81  ? 1.3937 1.4090 1.2708 -0.0607 -0.0118 0.0011  88  VAL A C   
5335 O O   . VAL D 81  ? 1.5496 1.5670 1.4289 -0.0626 -0.0152 0.0042  88  VAL A O   
5336 C CB  . VAL D 81  ? 1.2223 1.2266 1.0917 -0.0585 -0.0115 -0.0020 88  VAL A CB  
5337 C CG1 . VAL D 81  ? 1.0331 1.0395 0.9103 -0.0534 -0.0110 -0.0020 88  VAL A CG1 
5338 C CG2 . VAL D 81  ? 1.5472 1.5444 1.4093 -0.0585 -0.0099 -0.0049 88  VAL A CG2 
5339 N N   . GLU D 82  ? 1.5389 1.5584 1.4204 -0.0585 -0.0094 0.0006  89  GLU A N   
5340 C CA  . GLU D 82  ? 1.3760 1.4032 1.2658 -0.0581 -0.0104 0.0034  89  GLU A CA  
5341 C C   . GLU D 82  ? 1.5448 1.5744 1.4423 -0.0526 -0.0094 0.0027  89  GLU A C   
5342 O O   . GLU D 82  ? 1.6813 1.7098 1.5782 -0.0493 -0.0060 -0.0004 89  GLU A O   
5343 C CB  . GLU D 82  ? 1.2775 1.3089 1.1674 -0.0599 -0.0085 0.0035  89  GLU A CB  
5344 C CG  . GLU D 82  ? 1.7896 1.8295 1.6881 -0.0599 -0.0095 0.0068  89  GLU A CG  
5345 C CD  . GLU D 82  ? 2.2368 2.2810 2.1352 -0.0620 -0.0078 0.0073  89  GLU A CD  
5346 O OE1 . GLU D 82  ? 2.5173 2.5580 2.4096 -0.0632 -0.0059 0.0050  89  GLU A OE1 
5347 O OE2 . GLU D 82  ? 2.5910 2.6424 2.4962 -0.0625 -0.0086 0.0102  89  GLU A OE2 
5348 N N   . LYS D 83  ? 1.7977 1.8307 1.7027 -0.0518 -0.0123 0.0055  90  LYS A N   
5349 C CA  . LYS D 83  ? 1.7714 1.8075 1.6854 -0.0464 -0.0115 0.0046  90  LYS A CA  
5350 C C   . LYS D 83  ? 1.6417 1.6854 1.5612 -0.0448 -0.0086 0.0042  90  LYS A C   
5351 O O   . LYS D 83  ? 1.7509 1.7996 1.6720 -0.0480 -0.0093 0.0069  90  LYS A O   
5352 C CB  . LYS D 83  ? 1.8570 1.8949 1.7789 -0.0460 -0.0159 0.0080  90  LYS A CB  
5353 C CG  . LYS D 83  ? 2.0080 2.0395 1.9262 -0.0470 -0.0191 0.0089  90  LYS A CG  
5354 C CD  . LYS D 83  ? 1.8298 1.8643 1.7574 -0.0467 -0.0238 0.0129  90  LYS A CD  
5355 C CE  . LYS D 83  ? 1.9211 1.9503 1.8461 -0.0481 -0.0276 0.0147  90  LYS A CE  
5356 N NZ  . LYS D 83  ? 1.7912 1.8240 1.7262 -0.0484 -0.0327 0.0193  90  LYS A NZ  
5357 N N   . ALA D 84  ? 1.3634 1.4081 1.2856 -0.0401 -0.0052 0.0007  91  ALA A N   
5358 C CA  . ALA D 84  ? 1.3724 1.4253 1.3006 -0.0380 -0.0021 0.0000  91  ALA A CA  
5359 C C   . ALA D 84  ? 1.5080 1.5680 1.4480 -0.0368 -0.0044 0.0029  91  ALA A C   
5360 O O   . ALA D 84  ? 1.6873 1.7453 1.6317 -0.0364 -0.0083 0.0049  91  ALA A O   
5361 C CB  . ALA D 84  ? 1.5075 1.5601 1.4359 -0.0331 0.0019  -0.0048 91  ALA A CB  
5362 N N   . ASN D 85  ? 1.4209 1.4894 1.3664 -0.0362 -0.0021 0.0035  92  ASN A N   
5363 C CA  . ASN D 85  ? 1.6380 1.7144 1.5948 -0.0357 -0.0040 0.0067  92  ASN A CA  
5364 C C   . ASN D 85  ? 1.7908 1.8651 1.7476 -0.0402 -0.0093 0.0116  92  ASN A C   
5365 O O   . ASN D 85  ? 1.8637 1.9377 1.8275 -0.0390 -0.0129 0.0135  92  ASN A O   
5366 C CB  . ASN D 85  ? 1.8259 1.9052 1.7935 -0.0296 -0.0035 0.0044  92  ASN A CB  
5367 C CG  . ASN D 85  ? 2.0063 2.0907 1.9755 -0.0254 0.0021  -0.0003 92  ASN A CG  
5368 O OD1 . ASN D 85  ? 2.1825 2.2714 2.1479 -0.0273 0.0053  -0.0004 92  ASN A OD1 
5369 N ND2 . ASN D 85  ? 2.2060 2.2900 2.1811 -0.0198 0.0030  -0.0042 92  ASN A ND2 
5370 N N   . PRO D 86  ? 1.6604 1.7331 1.6094 -0.0457 -0.0104 0.0139  93  PRO A N   
5371 C CA  . PRO D 86  ? 1.3853 1.4559 1.3330 -0.0504 -0.0154 0.0182  93  PRO A CA  
5372 C C   . PRO D 86  ? 1.6582 1.7362 1.6176 -0.0504 -0.0183 0.0225  93  PRO A C   
5373 O O   . PRO D 86  ? 1.9045 1.9902 1.8716 -0.0483 -0.0161 0.0227  93  PRO A O   
5374 C CB  . PRO D 86  ? 1.7039 1.7729 1.6421 -0.0556 -0.0150 0.0188  93  PRO A CB  
5375 C CG  . PRO D 86  ? 1.8977 1.9714 1.8366 -0.0538 -0.0104 0.0167  93  PRO A CG  
5376 C CD  . PRO D 86  ? 1.8742 1.9469 1.8153 -0.0481 -0.0072 0.0125  93  PRO A CD  
5377 N N   . VAL D 87  ? 1.7140 1.7900 1.6748 -0.0530 -0.0233 0.0261  94  VAL A N   
5378 C CA  . VAL D 87  ? 1.6592 1.7413 1.6316 -0.0532 -0.0268 0.0306  94  VAL A CA  
5379 C C   . VAL D 87  ? 1.7017 1.7847 1.6710 -0.0598 -0.0310 0.0356  94  VAL A C   
5380 O O   . VAL D 87  ? 1.6198 1.7086 1.5983 -0.0609 -0.0339 0.0399  94  VAL A O   
5381 C CB  . VAL D 87  ? 1.7368 1.8168 1.7166 -0.0500 -0.0299 0.0311  94  VAL A CB  
5382 C CG1 . VAL D 87  ? 1.8806 1.9664 1.8732 -0.0506 -0.0343 0.0362  94  VAL A CG1 
5383 C CG2 . VAL D 87  ? 1.9450 2.0245 1.9287 -0.0433 -0.0258 0.0257  94  VAL A CG2 
5384 N N   . ASN D 88  ? 1.9267 2.0043 1.8836 -0.0642 -0.0312 0.0348  95  ASN A N   
5385 C CA  . ASN D 88  ? 1.9049 1.9824 1.8576 -0.0707 -0.0353 0.0388  95  ASN A CA  
5386 C C   . ASN D 88  ? 2.2258 2.3045 2.1724 -0.0740 -0.0334 0.0383  95  ASN A C   
5387 O O   . ASN D 88  ? 2.3953 2.4705 2.3334 -0.0791 -0.0356 0.0390  95  ASN A O   
5388 C CB  . ASN D 88  ? 1.6621 1.7327 1.6060 -0.0737 -0.0381 0.0387  95  ASN A CB  
5389 C CG  . ASN D 88  ? 1.6439 1.7146 1.5949 -0.0724 -0.0419 0.0415  95  ASN A CG  
5390 O OD1 . ASN D 88  ? 1.7961 1.8645 1.7502 -0.0678 -0.0406 0.0391  95  ASN A OD1 
5391 N ND2 . ASN D 88  ? 1.4249 1.4982 1.3789 -0.0768 -0.0471 0.0468  95  ASN A ND2 
5392 N N   . ASP D 89  ? 2.1544 2.2379 2.1054 -0.0712 -0.0297 0.0370  96  ASP A N   
5393 C CA  . ASP D 89  ? 2.0988 2.1853 2.0472 -0.0744 -0.0288 0.0380  96  ASP A CA  
5394 C C   . ASP D 89  ? 2.3946 2.4897 2.3537 -0.0753 -0.0308 0.0429  96  ASP A C   
5395 O O   . ASP D 89  ? 2.3445 2.4442 2.3142 -0.0719 -0.0314 0.0445  96  ASP A O   
5396 C CB  . ASP D 89  ? 1.8186 1.9053 1.7642 -0.0716 -0.0234 0.0339  96  ASP A CB  
5397 C CG  . ASP D 89  ? 1.9965 2.0868 1.9405 -0.0750 -0.0228 0.0353  96  ASP A CG  
5398 O OD1 . ASP D 89  ? 2.2139 2.3090 2.1608 -0.0726 -0.0190 0.0342  96  ASP A OD1 
5399 O OD2 . ASP D 89  ? 1.8810 1.9695 1.8209 -0.0802 -0.0264 0.0377  96  ASP A OD2 
5414 N N   . TYR D 92  ? 2.4765 2.5889 2.4442 -0.0787 -0.0274 0.0479  98  TYR A N   
5415 C CA  . TYR D 92  ? 2.3279 2.4487 2.3009 -0.0785 -0.0249 0.0494  98  TYR A CA  
5416 C C   . TYR D 92  ? 2.2298 2.3519 2.2013 -0.0742 -0.0190 0.0449  98  TYR A C   
5417 O O   . TYR D 92  ? 2.1186 2.2331 2.0811 -0.0736 -0.0174 0.0407  98  TYR A O   
5418 C CB  . TYR D 92  ? 2.1748 2.2948 2.1425 -0.0845 -0.0274 0.0520  98  TYR A CB  
5419 C CG  . TYR D 92  ? 2.3032 2.4237 2.2732 -0.0891 -0.0331 0.0570  98  TYR A CG  
5420 C CD1 . TYR D 92  ? 2.1303 2.2598 2.1108 -0.0898 -0.0346 0.0621  98  TYR A CD1 
5421 C CD2 . TYR D 92  ? 2.5507 2.6630 2.5124 -0.0928 -0.0370 0.0566  98  TYR A CD2 
5422 C CE1 . TYR D 92  ? 2.3993 2.5291 2.3819 -0.0942 -0.0401 0.0669  98  TYR A CE1 
5423 C CE2 . TYR D 92  ? 2.5316 2.6446 2.4948 -0.0974 -0.0423 0.0611  98  TYR A CE2 
5424 C CZ  . TYR D 92  ? 2.5685 2.6900 2.5422 -0.0981 -0.0440 0.0663  98  TYR A CZ  
5425 O OH  . TYR D 92  ? 2.9131 3.0352 2.8884 -0.1028 -0.0497 0.0711  98  TYR A OH  
5426 N N   . PRO D 93  ? 2.2843 2.4162 2.2642 -0.0715 -0.0158 0.0457  99  PRO A N   
5427 C CA  . PRO D 93  ? 2.2093 2.3436 2.1864 -0.0692 -0.0105 0.0422  99  PRO A CA  
5428 C C   . PRO D 93  ? 2.3918 2.5244 2.3613 -0.0741 -0.0109 0.0433  99  PRO A C   
5429 O O   . PRO D 93  ? 2.6070 2.7410 2.5731 -0.0730 -0.0071 0.0408  99  PRO A O   
5430 C CB  . PRO D 93  ? 2.2502 2.3970 2.2393 -0.0658 -0.0075 0.0436  99  PRO A CB  
5431 C CG  . PRO D 93  ? 2.2548 2.4037 2.2533 -0.0644 -0.0106 0.0461  99  PRO A CG  
5432 C CD  . PRO D 93  ? 2.3720 2.5135 2.3651 -0.0698 -0.0164 0.0493  99  PRO A CD  
5433 N N   . GLY D 94  ? 2.3362 2.4663 2.3035 -0.0794 -0.0156 0.0469  100 GLY A N   
5434 C CA  . GLY D 94  ? 2.2624 2.3897 2.2228 -0.0842 -0.0169 0.0477  100 GLY A CA  
5435 C C   . GLY D 94  ? 2.3234 2.4419 2.2736 -0.0836 -0.0148 0.0427  100 GLY A C   
5436 O O   . GLY D 94  ? 2.2415 2.3509 2.1853 -0.0839 -0.0164 0.0401  100 GLY A O   
5437 N N   . ASP D 95  ? 2.1159 2.2376 2.0650 -0.0829 -0.0112 0.0414  101 ASP A N   
5438 C CA  . ASP D 95  ? 2.1116 2.2258 2.0520 -0.0819 -0.0089 0.0368  101 ASP A CA  
5439 C C   . ASP D 95  ? 1.8961 2.0027 1.8290 -0.0872 -0.0122 0.0370  101 ASP A C   
5440 O O   . ASP D 95  ? 2.1272 2.2371 2.0611 -0.0908 -0.0135 0.0399  101 ASP A O   
5441 C CB  . ASP D 95  ? 2.2380 2.3588 2.1800 -0.0795 -0.0040 0.0356  101 ASP A CB  
5442 C CG  . ASP D 95  ? 2.2659 2.3923 2.2138 -0.0736 -0.0002 0.0334  101 ASP A CG  
5443 O OD1 . ASP D 95  ? 2.2751 2.4097 2.2262 -0.0716 0.0039  0.0329  101 ASP A OD1 
5444 O OD2 . ASP D 95  ? 2.3257 2.4488 2.2755 -0.0711 -0.0013 0.0323  101 ASP A OD2 
5445 N N   . PHE D 96  ? 1.4502 1.5467 1.3761 -0.0875 -0.0138 0.0339  102 PHE A N   
5446 C CA  . PHE D 96  ? 1.4798 1.5678 1.3976 -0.0910 -0.0155 0.0319  102 PHE A CA  
5447 C C   . PHE D 96  ? 1.6901 1.7788 1.6059 -0.0913 -0.0129 0.0309  102 PHE A C   
5448 O O   . PHE D 96  ? 1.8346 1.9273 1.7520 -0.0877 -0.0087 0.0296  102 PHE A O   
5449 C CB  . PHE D 96  ? 1.5518 1.6303 1.4630 -0.0896 -0.0159 0.0279  102 PHE A CB  
5450 C CG  . PHE D 96  ? 1.9206 1.9990 1.8323 -0.0841 -0.0120 0.0249  102 PHE A CG  
5451 C CD1 . PHE D 96  ? 2.0081 2.0836 1.9158 -0.0822 -0.0086 0.0217  102 PHE A CD1 
5452 C CD2 . PHE D 96  ? 2.0110 2.0916 1.9272 -0.0811 -0.0121 0.0254  102 PHE A CD2 
5453 C CE1 . PHE D 96  ? 1.9328 2.0078 1.8408 -0.0773 -0.0053 0.0187  102 PHE A CE1 
5454 C CE2 . PHE D 96  ? 1.8088 1.8887 1.7257 -0.0760 -0.0089 0.0224  102 PHE A CE2 
5455 C CZ  . PHE D 96  ? 1.8427 1.9196 1.7552 -0.0741 -0.0055 0.0190  102 PHE A CZ  
5456 N N   . ASN D 97  ? 1.9183 2.0036 1.8312 -0.0958 -0.0156 0.0317  103 ASN A N   
5457 C CA  . ASN D 97  ? 1.7905 1.8770 1.7026 -0.0975 -0.0145 0.0321  103 ASN A CA  
5458 C C   . ASN D 97  ? 1.7638 1.8397 1.6683 -0.0984 -0.0148 0.0280  103 ASN A C   
5459 O O   . ASN D 97  ? 1.7604 1.8283 1.6604 -0.0994 -0.0171 0.0255  103 ASN A O   
5460 C CB  . ASN D 97  ? 1.9618 2.0533 1.8781 -0.1024 -0.0180 0.0370  103 ASN A CB  
5461 C CG  . ASN D 97  ? 2.1878 2.2905 2.1125 -0.1018 -0.0178 0.0417  103 ASN A CG  
5462 O OD1 . ASN D 97  ? 2.2613 2.3711 2.1897 -0.0979 -0.0138 0.0417  103 ASN A OD1 
5463 N ND2 . ASN D 97  ? 2.1474 2.2517 2.0751 -0.1056 -0.0222 0.0454  103 ASN A ND2 
5464 N N   . ASP D 98  ? 1.8802 1.9563 1.7833 -0.0983 -0.0125 0.0273  104 ASP A N   
5465 C CA  . ASP D 98  ? 2.2137 2.2802 2.1104 -0.0985 -0.0122 0.0232  104 ASP A CA  
5466 C C   . ASP D 98  ? 2.0260 2.0859 1.9182 -0.0948 -0.0106 0.0189  104 ASP A C   
5467 O O   . ASP D 98  ? 1.9183 1.9700 1.8060 -0.0959 -0.0126 0.0162  104 ASP A O   
5468 C CB  . ASP D 98  ? 2.3153 2.3756 2.2103 -0.1033 -0.0166 0.0233  104 ASP A CB  
5469 C CG  . ASP D 98  ? 2.6633 2.7265 2.5607 -0.1065 -0.0176 0.0261  104 ASP A CG  
5470 O OD1 . ASP D 98  ? 3.0701 3.1388 2.9687 -0.1049 -0.0142 0.0271  104 ASP A OD1 
5471 O OD2 . ASP D 98  ? 2.4695 2.5297 2.3677 -0.1108 -0.0218 0.0273  104 ASP A OD2 
5472 N N   . TYR D 99  ? 1.7722 1.8361 1.6658 -0.0903 -0.0069 0.0181  105 TYR A N   
5473 C CA  . TYR D 99  ? 1.5044 1.5644 1.3961 -0.0869 -0.0062 0.0154  105 TYR A CA  
5474 C C   . TYR D 99  ? 1.5109 1.5630 1.3966 -0.0844 -0.0040 0.0110  105 TYR A C   
5475 O O   . TYR D 99  ? 1.2996 1.3438 1.1807 -0.0848 -0.0054 0.0085  105 TYR A O   
5476 C CB  . TYR D 99  ? 1.5446 1.6129 1.4424 -0.0833 -0.0043 0.0170  105 TYR A CB  
5477 C CG  . TYR D 99  ? 2.0960 2.1709 1.9966 -0.0798 0.0001  0.0165  105 TYR A CG  
5478 C CD1 . TYR D 99  ? 2.1218 2.1932 2.0197 -0.0754 0.0031  0.0127  105 TYR A CD1 
5479 C CD2 . TYR D 99  ? 2.3316 2.4169 2.2380 -0.0805 0.0012  0.0199  105 TYR A CD2 
5480 C CE1 . TYR D 99  ? 2.5770 2.6547 2.4773 -0.0721 0.0071  0.0118  105 TYR A CE1 
5481 C CE2 . TYR D 99  ? 2.5527 2.6450 2.4616 -0.0773 0.0054  0.0191  105 TYR A CE2 
5482 C CZ  . TYR D 99  ? 2.6947 2.7830 2.6004 -0.0730 0.0084  0.0148  105 TYR A CZ  
5483 O OH  . TYR D 99  ? 2.8205 2.9158 2.7283 -0.0699 0.0126  0.0135  105 TYR A OH  
5484 N N   . GLU D 100 ? 1.9886 2.0429 1.8742 -0.0821 -0.0006 0.0100  106 GLU A N   
5485 C CA  . GLU D 100 ? 2.1016 2.1483 1.9817 -0.0801 0.0013  0.0062  106 GLU A CA  
5486 C C   . GLU D 100 ? 1.9546 1.9934 1.8302 -0.0838 -0.0009 0.0050  106 GLU A C   
5487 O O   . GLU D 100 ? 2.0967 2.1272 1.9675 -0.0828 -0.0006 0.0017  106 GLU A O   
5488 C CB  . GLU D 100 ? 2.5074 2.5591 2.3885 -0.0773 0.0052  0.0057  106 GLU A CB  
5489 C CG  . GLU D 100 ? 2.5758 2.6215 2.4519 -0.0754 0.0075  0.0024  106 GLU A CG  
5490 C CD  . GLU D 100 ? 2.5535 2.5912 2.4260 -0.0724 0.0076  -0.0010 106 GLU A CD  
5491 O OE1 . GLU D 100 ? 2.3543 2.3941 2.2293 -0.0689 0.0083  -0.0016 106 GLU A OE1 
5492 O OE2 . GLU D 100 ? 2.5564 2.5857 2.4239 -0.0735 0.0070  -0.0031 106 GLU A OE2 
5493 N N   . GLU D 101 ? 2.1805 2.2213 2.0582 -0.0881 -0.0035 0.0077  107 GLU A N   
5494 C CA  . GLU D 101 ? 2.1520 2.1850 2.0266 -0.0917 -0.0065 0.0063  107 GLU A CA  
5495 C C   . GLU D 101 ? 1.8710 1.8985 1.7427 -0.0917 -0.0084 0.0041  107 GLU A C   
5496 O O   . GLU D 101 ? 1.9802 1.9996 1.8473 -0.0920 -0.0088 0.0007  107 GLU A O   
5497 C CB  . GLU D 101 ? 2.4732 2.5096 2.3514 -0.0963 -0.0096 0.0097  107 GLU A CB  
5498 C CG  . GLU D 101 ? 2.9419 2.9876 2.8246 -0.0968 -0.0083 0.0136  107 GLU A CG  
5499 C CD  . GLU D 101 ? 3.0187 3.0660 2.9045 -0.1019 -0.0117 0.0169  107 GLU A CD  
5500 O OE1 . GLU D 101 ? 2.7818 2.8238 2.6671 -0.1048 -0.0155 0.0162  107 GLU A OE1 
5501 O OE2 . GLU D 101 ? 3.2558 3.3102 3.1447 -0.1030 -0.0108 0.0202  107 GLU A OE2 
5502 N N   . LEU D 102 ? 1.8255 1.8577 1.6999 -0.0920 -0.0099 0.0062  108 LEU A N   
5503 C CA  . LEU D 102 ? 1.7022 1.7302 1.5737 -0.0924 -0.0118 0.0045  108 LEU A CA  
5504 C C   . LEU D 102 ? 1.6633 1.6864 1.5308 -0.0887 -0.0095 0.0013  108 LEU A C   
5505 O O   . LEU D 102 ? 1.6576 1.6742 1.5204 -0.0894 -0.0105 -0.0015 108 LEU A O   
5506 C CB  . LEU D 102 ? 1.6133 1.6479 1.4891 -0.0929 -0.0136 0.0080  108 LEU A CB  
5507 C CG  . LEU D 102 ? 1.5416 1.5732 1.4147 -0.0947 -0.0165 0.0073  108 LEU A CG  
5508 C CD1 . LEU D 102 ? 1.8183 1.8427 1.6865 -0.0983 -0.0188 0.0043  108 LEU A CD1 
5509 C CD2 . LEU D 102 ? 1.5971 1.6357 1.4752 -0.0963 -0.0190 0.0115  108 LEU A CD2 
5510 N N   . LYS D 103 ? 1.6555 1.6817 1.5248 -0.0847 -0.0064 0.0015  109 LYS A N   
5511 C CA  . LYS D 103 ? 1.6741 1.6959 1.5403 -0.0810 -0.0043 -0.0013 109 LYS A CA  
5512 C C   . LYS D 103 ? 1.7262 1.7399 1.5872 -0.0815 -0.0035 -0.0047 109 LYS A C   
5513 O O   . LYS D 103 ? 1.8288 1.8365 1.6856 -0.0805 -0.0035 -0.0072 109 LYS A O   
5514 C CB  . LYS D 103 ? 1.8276 1.8548 1.6974 -0.0768 -0.0012 -0.0007 109 LYS A CB  
5515 C CG  . LYS D 103 ? 1.9146 1.9493 1.7904 -0.0755 -0.0018 0.0021  109 LYS A CG  
5516 C CD  . LYS D 103 ? 1.9131 1.9531 1.7928 -0.0710 0.0015  0.0018  109 LYS A CD  
5517 C CE  . LYS D 103 ? 1.7973 1.8449 1.6842 -0.0693 0.0010  0.0043  109 LYS A CE  
5518 N NZ  . LYS D 103 ? 1.7841 1.8370 1.6751 -0.0647 0.0044  0.0033  109 LYS A NZ  
5519 N N   . HIS D 104 ? 1.8882 1.9019 1.7496 -0.0830 -0.0029 -0.0044 110 HIS A N   
5520 C CA  . HIS D 104 ? 1.8496 1.8555 1.7068 -0.0837 -0.0025 -0.0073 110 HIS A CA  
5521 C C   . HIS D 104 ? 1.8098 1.8101 1.6646 -0.0870 -0.0053 -0.0091 110 HIS A C   
5522 O O   . HIS D 104 ? 1.8934 1.8866 1.7444 -0.0868 -0.0050 -0.0123 110 HIS A O   
5523 C CB  . HIS D 104 ? 2.0144 2.0221 1.8732 -0.0847 -0.0015 -0.0060 110 HIS A CB  
5524 C CG  . HIS D 104 ? 2.1633 2.1640 2.0187 -0.0840 -0.0002 -0.0086 110 HIS A CG  
5525 N ND1 . HIS D 104 ? 2.1172 2.1177 1.9710 -0.0805 0.0028  -0.0095 110 HIS A ND1 
5526 C CD2 . HIS D 104 ? 2.2601 2.2538 2.1136 -0.0863 -0.0016 -0.0105 110 HIS A CD2 
5527 C CE1 . HIS D 104 ? 1.8870 1.8806 1.7380 -0.0809 0.0031  -0.0115 110 HIS A CE1 
5528 N NE2 . HIS D 104 ? 2.1093 2.0988 1.9603 -0.0843 0.0005  -0.0121 110 HIS A NE2 
5529 N N   . LEU D 105 ? 1.7145 1.7180 1.5715 -0.0902 -0.0081 -0.0072 111 LEU A N   
5530 C CA  . LEU D 105 ? 1.7974 1.7964 1.6520 -0.0932 -0.0108 -0.0094 111 LEU A CA  
5531 C C   . LEU D 105 ? 1.6306 1.6266 1.4810 -0.0914 -0.0103 -0.0117 111 LEU A C   
5532 O O   . LEU D 105 ? 1.5274 1.5171 1.3738 -0.0920 -0.0104 -0.0153 111 LEU A O   
5533 C CB  . LEU D 105 ? 1.6779 1.6819 1.5358 -0.0964 -0.0139 -0.0065 111 LEU A CB  
5534 C CG  . LEU D 105 ? 1.9637 1.9710 1.8261 -0.0990 -0.0153 -0.0037 111 LEU A CG  
5535 C CD1 . LEU D 105 ? 2.0162 2.0292 1.8821 -0.1018 -0.0183 -0.0004 111 LEU A CD1 
5536 C CD2 . LEU D 105 ? 1.6888 1.6895 1.5503 -0.1015 -0.0168 -0.0063 111 LEU A CD2 
5537 N N   . LEU D 106 ? 1.6214 1.6221 1.4732 -0.0893 -0.0098 -0.0095 112 LEU A N   
5538 C CA  . LEU D 106 ? 1.7145 1.7133 1.5631 -0.0878 -0.0096 -0.0108 112 LEU A CA  
5539 C C   . LEU D 106 ? 1.8508 1.8441 1.6962 -0.0848 -0.0071 -0.0136 112 LEU A C   
5540 O O   . LEU D 106 ? 2.0099 1.9996 1.8514 -0.0845 -0.0072 -0.0155 112 LEU A O   
5541 C CB  . LEU D 106 ? 1.4758 1.4811 1.3282 -0.0859 -0.0098 -0.0074 112 LEU A CB  
5542 C CG  . LEU D 106 ? 1.6975 1.7086 1.5535 -0.0888 -0.0126 -0.0042 112 LEU A CG  
5543 C CD1 . LEU D 106 ? 1.7335 1.7512 1.5946 -0.0863 -0.0125 -0.0008 112 LEU A CD1 
5544 C CD2 . LEU D 106 ? 1.7182 1.7268 1.5703 -0.0926 -0.0156 -0.0053 112 LEU A CD2 
5545 N N   . SER D 107 ? 1.6699 1.6629 1.5167 -0.0827 -0.0048 -0.0135 113 SER A N   
5546 C CA  . SER D 107 ? 1.4726 1.4602 1.3165 -0.0801 -0.0026 -0.0160 113 SER A CA  
5547 C C   . SER D 107 ? 1.4673 1.4478 1.3072 -0.0821 -0.0031 -0.0193 113 SER A C   
5548 O O   . SER D 107 ? 1.5693 1.5448 1.4065 -0.0802 -0.0015 -0.0214 113 SER A O   
5549 C CB  . SER D 107 ? 1.4675 1.4565 1.3135 -0.0783 -0.0004 -0.0151 113 SER A CB  
5550 O OG  . SER D 107 ? 1.5381 1.5343 1.3882 -0.0763 0.0004  -0.0125 113 SER A OG  
5551 N N   . ARG D 108 ? 1.4600 1.4400 1.3001 -0.0858 -0.0053 -0.0200 114 ARG A N   
5552 C CA  . ARG D 108 ? 1.6796 1.6535 1.5167 -0.0878 -0.0059 -0.0238 114 ARG A CA  
5553 C C   . ARG D 108 ? 1.7536 1.7279 1.5881 -0.0903 -0.0080 -0.0251 114 ARG A C   
5554 O O   . ARG D 108 ? 1.7374 1.7078 1.5701 -0.0926 -0.0089 -0.0285 114 ARG A O   
5555 C CB  . ARG D 108 ? 1.8118 1.7835 1.6513 -0.0902 -0.0069 -0.0244 114 ARG A CB  
5556 C CG  . ARG D 108 ? 1.8293 1.7990 1.6700 -0.0883 -0.0050 -0.0239 114 ARG A CG  
5557 C CD  . ARG D 108 ? 2.1116 2.0791 1.9552 -0.0912 -0.0066 -0.0242 114 ARG A CD  
5558 N NE  . ARG D 108 ? 2.2711 2.2365 2.1155 -0.0899 -0.0049 -0.0235 114 ARG A NE  
5559 C CZ  . ARG D 108 ? 2.2243 2.1881 2.0718 -0.0921 -0.0062 -0.0228 114 ARG A CZ  
5560 N NH1 . ARG D 108 ? 2.0663 2.0319 1.9173 -0.0955 -0.0091 -0.0216 114 ARG A NH1 
5561 N NH2 . ARG D 108 ? 2.1721 2.1322 2.0193 -0.0910 -0.0048 -0.0231 114 ARG A NH2 
5562 N N   . ILE D 109 ? 1.7883 1.7674 1.6228 -0.0901 -0.0088 -0.0228 115 ILE A N   
5563 C CA  . ILE D 109 ? 1.7336 1.7136 1.5652 -0.0929 -0.0109 -0.0237 115 ILE A CA  
5564 C C   . ILE D 109 ? 1.6976 1.6781 1.5263 -0.0910 -0.0102 -0.0234 115 ILE A C   
5565 O O   . ILE D 109 ? 1.6564 1.6399 1.4876 -0.0882 -0.0095 -0.0204 115 ILE A O   
5566 C CB  . ILE D 109 ? 1.8484 1.8342 1.6830 -0.0952 -0.0136 -0.0205 115 ILE A CB  
5567 C CG1 . ILE D 109 ? 1.8210 1.8080 1.6600 -0.0965 -0.0144 -0.0192 115 ILE A CG1 
5568 C CG2 . ILE D 109 ? 1.7914 1.7768 1.6225 -0.0990 -0.0160 -0.0226 115 ILE A CG2 
5569 C CD1 . ILE D 109 ? 1.7530 1.7346 1.5915 -0.0984 -0.0148 -0.0227 115 ILE A CD1 
5570 N N   . ASN D 110 ? 1.7330 1.7108 1.5569 -0.0925 -0.0104 -0.0264 116 ASN A N   
5571 C CA  . ASN D 110 ? 1.8047 1.7836 1.6259 -0.0915 -0.0102 -0.0255 116 ASN A CA  
5572 C C   . ASN D 110 ? 1.6777 1.6610 1.4969 -0.0948 -0.0130 -0.0241 116 ASN A C   
5573 O O   . ASN D 110 ? 1.7862 1.7728 1.6060 -0.0940 -0.0139 -0.0208 116 ASN A O   
5574 C CB  . ASN D 110 ? 1.8328 1.8067 1.6497 -0.0908 -0.0084 -0.0292 116 ASN A CB  
5575 C CG  . ASN D 110 ? 1.7156 1.6858 1.5341 -0.0869 -0.0059 -0.0292 116 ASN A CG  
5576 O OD1 . ASN D 110 ? 1.6055 1.5776 1.4277 -0.0843 -0.0054 -0.0262 116 ASN A OD1 
5577 N ND2 . ASN D 110 ? 1.7478 1.7131 1.5637 -0.0863 -0.0042 -0.0325 116 ASN A ND2 
5578 N N   . HIS D 111 ? 1.4043 1.3876 1.2213 -0.0986 -0.0146 -0.0264 117 HIS A N   
5579 C CA  . HIS D 111 ? 1.5294 1.5166 1.3435 -0.1023 -0.0172 -0.0255 117 HIS A CA  
5580 C C   . HIS D 111 ? 1.5313 1.5209 1.3478 -0.1052 -0.0199 -0.0244 117 HIS A C   
5581 O O   . HIS D 111 ? 1.6146 1.6017 1.4329 -0.1058 -0.0198 -0.0266 117 HIS A O   
5582 C CB  . HIS D 111 ? 1.5432 1.5284 1.3508 -0.1047 -0.0169 -0.0300 117 HIS A CB  
5583 C CG  . HIS D 111 ? 1.5276 1.5174 1.3313 -0.1079 -0.0192 -0.0283 117 HIS A CG  
5584 N ND1 . HIS D 111 ? 1.4770 1.4717 1.2834 -0.1081 -0.0213 -0.0227 117 HIS A ND1 
5585 C CD2 . HIS D 111 ? 1.6560 1.6467 1.4534 -0.1114 -0.0197 -0.0314 117 HIS A CD2 
5586 C CE1 . HIS D 111 ? 1.4305 1.4287 1.2325 -0.1117 -0.0234 -0.0220 117 HIS A CE1 
5587 N NE2 . HIS D 111 ? 1.5214 1.5175 1.3175 -0.1138 -0.0224 -0.0273 117 HIS A NE2 
5588 N N   . PHE D 112 ? 1.4933 1.4881 1.3103 -0.1072 -0.0225 -0.0206 118 PHE A N   
5589 C CA  . PHE D 112 ? 1.4321 1.4300 1.2514 -0.1103 -0.0255 -0.0187 118 PHE A CA  
5590 C C   . PHE D 112 ? 1.7586 1.7593 1.5730 -0.1147 -0.0283 -0.0186 118 PHE A C   
5591 O O   . PHE D 112 ? 1.8590 1.8613 1.6702 -0.1149 -0.0283 -0.0178 118 PHE A O   
5592 C CB  . PHE D 112 ? 1.6733 1.6759 1.4996 -0.1083 -0.0262 -0.0130 118 PHE A CB  
5593 C CG  . PHE D 112 ? 1.8806 1.8818 1.7116 -0.1044 -0.0235 -0.0126 118 PHE A CG  
5594 C CD1 . PHE D 112 ? 1.8623 1.8627 1.6962 -0.1053 -0.0238 -0.0131 118 PHE A CD1 
5595 C CD2 . PHE D 112 ? 2.2291 2.2298 2.0617 -0.1002 -0.0210 -0.0117 118 PHE A CD2 
5596 C CE1 . PHE D 112 ? 2.2848 2.2847 2.1228 -0.1021 -0.0214 -0.0125 118 PHE A CE1 
5597 C CE2 . PHE D 112 ? 2.3536 2.3534 2.1900 -0.0968 -0.0185 -0.0115 118 PHE A CE2 
5598 C CZ  . PHE D 112 ? 2.4233 2.4229 2.2622 -0.0979 -0.0187 -0.0118 118 PHE A CZ  
5599 N N   . GLU D 113 ? 1.6565 1.6582 1.4705 -0.1185 -0.0311 -0.0193 119 GLU A N   
5600 C CA  . GLU D 113 ? 1.4193 1.4240 1.2285 -0.1232 -0.0341 -0.0191 119 GLU A CA  
5601 C C   . GLU D 113 ? 1.5152 1.5231 1.3280 -0.1260 -0.0378 -0.0157 119 GLU A C   
5602 O O   . GLU D 113 ? 1.3720 1.3778 1.1870 -0.1268 -0.0385 -0.0175 119 GLU A O   
5603 C CB  . GLU D 113 ? 1.4356 1.4369 1.2377 -0.1258 -0.0336 -0.0260 119 GLU A CB  
5604 C CG  . GLU D 113 ? 1.5072 1.5061 1.3051 -0.1237 -0.0303 -0.0292 119 GLU A CG  
5605 C CD  . GLU D 113 ? 1.9764 1.9726 1.7682 -0.1261 -0.0294 -0.0364 119 GLU A CD  
5606 O OE1 . GLU D 113 ? 2.1403 2.1353 1.9316 -0.1289 -0.0313 -0.0395 119 GLU A OE1 
5607 O OE2 . GLU D 113 ? 2.1664 2.1615 1.9542 -0.1250 -0.0269 -0.0391 119 GLU A OE2 
5608 N N   . LYS D 114 ? 1.3666 1.3798 1.1806 -0.1278 -0.0405 -0.0105 120 LYS A N   
5609 C CA  . LYS D 114 ? 1.4542 1.4710 1.2728 -0.1302 -0.0440 -0.0064 120 LYS A CA  
5610 C C   . LYS D 114 ? 1.6508 1.6671 1.4642 -0.1357 -0.0473 -0.0091 120 LYS A C   
5611 O O   . LYS D 114 ? 1.7479 1.7643 1.5540 -0.1387 -0.0479 -0.0118 120 LYS A O   
5612 C CB  . LYS D 114 ? 1.3688 1.3913 1.1913 -0.1301 -0.0459 0.0004  120 LYS A CB  
5613 C CG  . LYS D 114 ? 1.5064 1.5301 1.3357 -0.1248 -0.0434 0.0035  120 LYS A CG  
5614 C CD  . LYS D 114 ? 1.9208 1.9502 1.7549 -0.1251 -0.0459 0.0099  120 LYS A CD  
5615 C CE  . LYS D 114 ? 1.8192 1.8499 1.6606 -0.1195 -0.0434 0.0124  120 LYS A CE  
5616 N NZ  . LYS D 114 ? 1.8838 1.9199 1.7316 -0.1192 -0.0459 0.0184  120 LYS A NZ  
5617 N N   . ILE D 115 ? 1.6782 1.6946 1.4954 -0.1373 -0.0495 -0.0082 121 ILE A N   
5618 C CA  . ILE D 115 ? 1.7281 1.7429 1.5412 -0.1421 -0.0526 -0.0118 121 ILE A CA  
5619 C C   . ILE D 115 ? 1.7931 1.8111 1.6113 -0.1448 -0.0568 -0.0068 121 ILE A C   
5620 O O   . ILE D 115 ? 1.7145 1.7350 1.5405 -0.1423 -0.0566 -0.0019 121 ILE A O   
5621 C CB  . ILE D 115 ? 1.8632 1.8716 1.6748 -0.1412 -0.0508 -0.0188 121 ILE A CB  
5622 C CG1 . ILE D 115 ? 2.0764 2.0819 1.8840 -0.1381 -0.0465 -0.0229 121 ILE A CG1 
5623 C CG2 . ILE D 115 ? 1.9079 1.9142 1.7148 -0.1461 -0.0541 -0.0235 121 ILE A CG2 
5624 C CD1 . ILE D 115 ? 2.1427 2.1483 1.9415 -0.1412 -0.0467 -0.0273 121 ILE A CD1 
5625 N N   . GLN D 116 ? 1.9580 1.9763 1.7716 -0.1499 -0.0607 -0.0084 122 GLN A N   
5626 C CA  . GLN D 116 ? 1.8753 1.8975 1.6923 -0.1536 -0.0654 -0.0032 122 GLN A CA  
5627 C C   . GLN D 116 ? 1.9932 2.0121 1.8123 -0.1554 -0.0678 -0.0056 122 GLN A C   
5628 O O   . GLN D 116 ? 1.9463 1.9628 1.7602 -0.1596 -0.0706 -0.0099 122 GLN A O   
5629 C CB  . GLN D 116 ? 1.8848 1.9096 1.6947 -0.1585 -0.0685 -0.0028 122 GLN A CB  
5630 C CG  . GLN D 116 ? 2.0128 2.0415 1.8214 -0.1573 -0.0671 0.0008  122 GLN A CG  
5631 C CD  . GLN D 116 ? 2.0050 2.0369 1.8066 -0.1629 -0.0706 0.0016  122 GLN A CD  
5632 O OE1 . GLN D 116 ? 2.1820 2.2121 1.9768 -0.1672 -0.0726 -0.0031 122 GLN A OE1 
5633 N NE2 . GLN D 116 ? 1.8581 1.8948 1.6615 -0.1631 -0.0717 0.0077  122 GLN A NE2 
5634 N N   . ILE D 117 ? 2.0060 2.0250 1.8332 -0.1525 -0.0668 -0.0028 123 ILE A N   
5635 C CA  . ILE D 117 ? 2.0319 2.0481 1.8625 -0.1542 -0.0693 -0.0041 123 ILE A CA  
5636 C C   . ILE D 117 ? 2.3053 2.3253 2.1381 -0.1586 -0.0747 0.0008  123 ILE A C   
5637 O O   . ILE D 117 ? 2.5271 2.5452 2.3551 -0.1632 -0.0784 -0.0022 123 ILE A O   
5638 C CB  . ILE D 117 ? 1.9350 1.9514 1.7737 -0.1500 -0.0668 -0.0015 123 ILE A CB  
5639 C CG1 . ILE D 117 ? 2.0067 2.0189 1.8432 -0.1460 -0.0619 -0.0064 123 ILE A CG1 
5640 C CG2 . ILE D 117 ? 2.0370 2.0517 1.8805 -0.1522 -0.0701 -0.0013 123 ILE A CG2 
5641 C CD1 . ILE D 117 ? 2.1873 2.2007 2.0308 -0.1419 -0.0591 -0.0033 123 ILE A CD1 
5642 N N   . ILE D 118 ? 1.8473 1.8727 1.6874 -0.1573 -0.0750 0.0081  124 ILE A N   
5643 C CA  . ILE D 118 ? 1.9417 1.9718 1.7861 -0.1607 -0.0797 0.0144  124 ILE A CA  
5644 C C   . ILE D 118 ? 1.8485 1.8828 1.6898 -0.1626 -0.0811 0.0177  124 ILE A C   
5645 O O   . ILE D 118 ? 1.8562 1.8912 1.6948 -0.1600 -0.0778 0.0171  124 ILE A O   
5646 C CB  . ILE D 118 ? 2.0399 2.0744 1.8949 -0.1578 -0.0788 0.0206  124 ILE A CB  
5647 C CG1 . ILE D 118 ? 2.3238 2.3547 2.1821 -0.1577 -0.0791 0.0183  124 ILE A CG1 
5648 C CG2 . ILE D 118 ? 1.9866 2.0281 1.8476 -0.1595 -0.0819 0.0285  124 ILE A CG2 
5649 C CD1 . ILE D 118 ? 2.2059 2.2413 2.0736 -0.1545 -0.0772 0.0236  124 ILE A CD1 
5657 N N   . LYS D 120 a 1.9380 1.9749 1.7796 -0.1674 -0.0863 0.0214  125 LYS A N   
5658 C CA  . LYS D 120 a 1.8701 1.9117 1.7103 -0.1699 -0.0886 0.0260  125 LYS A CA  
5659 C C   . LYS D 120 a 1.6950 1.7426 1.5447 -0.1709 -0.0919 0.0346  125 LYS A C   
5660 O O   . LYS D 120 a 2.2169 2.2657 2.0743 -0.1690 -0.0916 0.0371  125 LYS A O   
5661 C CB  . LYS D 120 a 1.9485 1.9878 1.7786 -0.1757 -0.0922 0.0220  125 LYS A CB  
5662 C CG  . LYS D 120 a 2.2060 2.2411 2.0267 -0.1748 -0.0887 0.0142  125 LYS A CG  
5663 C CD  . LYS D 120 a 2.1837 2.2177 1.9944 -0.1808 -0.0922 0.0102  125 LYS A CD  
5664 C CE  . LYS D 120 a 2.2816 2.3125 2.0832 -0.1800 -0.0884 0.0025  125 LYS A CE  
5665 N NZ  . LYS D 120 a 2.2243 2.2548 2.0155 -0.1859 -0.0914 -0.0021 125 LYS A NZ  
5666 N N   . SER D 121 b 2.0916 2.1434 1.9410 -0.1739 -0.0951 0.0394  125 SER A N   
5667 C CA  . SER D 121 b 2.2723 2.3301 2.1309 -0.1751 -0.0985 0.0478  125 SER A CA  
5668 C C   . SER D 121 b 2.5762 2.6330 2.4366 -0.1791 -0.1029 0.0486  125 SER A C   
5669 O O   . SER D 121 b 2.2122 2.2659 2.0652 -0.1843 -0.1069 0.0457  125 SER A O   
5670 C CB  . SER D 121 b 2.2588 2.3205 2.1159 -0.1787 -0.1020 0.0524  125 SER A CB  
5671 O OG  . SER D 121 b 2.0091 2.0680 1.8564 -0.1849 -0.1061 0.0492  125 SER A OG  
5678 N N   . TRP D 123 ? 2.2050 2.2647 2.0751 -0.1768 -0.1025 0.0527  127 TRP A N   
5679 C CA  . TRP D 123 ? 1.7897 1.8485 1.6626 -0.1803 -0.1068 0.0540  127 TRP A CA  
5680 C C   . TRP D 123 ? 1.7755 1.8411 1.6570 -0.1827 -0.1111 0.0630  127 TRP A C   
5681 O O   . TRP D 123 ? 1.7899 1.8593 1.6806 -0.1814 -0.1112 0.0675  127 TRP A O   
5682 C CB  . TRP D 123 ? 1.8027 1.8601 1.6806 -0.1767 -0.1038 0.0523  127 TRP A CB  
5683 C CG  . TRP D 123 ? 2.2901 2.3404 2.1612 -0.1749 -0.1006 0.0439  127 TRP A CG  
5684 C CD1 . TRP D 123 ? 2.5255 2.5745 2.3956 -0.1697 -0.0947 0.0405  127 TRP A CD1 
5685 C CD2 . TRP D 123 ? 2.5464 2.5899 2.4120 -0.1780 -0.1032 0.0378  127 TRP A CD2 
5686 N NE1 . TRP D 123 ? 2.7071 2.7491 2.5714 -0.1695 -0.0934 0.0329  127 TRP A NE1 
5687 C CE2 . TRP D 123 ? 2.7001 2.7385 2.5617 -0.1745 -0.0985 0.0309  127 TRP A CE2 
5688 C CE3 . TRP D 123 ? 2.4489 2.4899 2.3128 -0.1835 -0.1093 0.0372  127 TRP A CE3 
5689 C CZ2 . TRP D 123 ? 2.6911 2.7224 2.5478 -0.1760 -0.0996 0.0235  127 TRP A CZ2 
5690 C CZ3 . TRP D 123 ? 2.4109 2.4446 2.2696 -0.1850 -0.1104 0.0296  127 TRP A CZ3 
5691 C CH2 . TRP D 123 ? 2.5856 2.6146 2.4411 -0.1812 -0.1055 0.0228  127 TRP A CH2 
5692 N N   . SER D 124 ? 2.0303 2.0978 1.9088 -0.1864 -0.1146 0.0658  128 SER A N   
5693 C CA  . SER D 124 ? 1.9466 2.0197 1.8324 -0.1899 -0.1197 0.0740  128 SER A CA  
5694 C C   . SER D 124 ? 1.8868 1.9567 1.7701 -0.1957 -0.1257 0.0736  128 SER A C   
5695 O O   . SER D 124 ? 1.7983 1.8713 1.6841 -0.2002 -0.1312 0.0793  128 SER A O   
5696 C CB  . SER D 124 ? 1.9115 1.9876 1.7954 -0.1922 -0.1218 0.0776  128 SER A CB  
5697 O OG  . SER D 124 ? 2.0659 2.1375 1.9378 -0.1975 -0.1251 0.0732  128 SER A OG  
5698 N N   . SER D 125 ? 1.7868 1.8506 1.6654 -0.1956 -0.1249 0.0669  129 SER A N   
5699 C CA  . SER D 125 ? 1.8684 1.9287 1.7456 -0.2006 -0.1306 0.0661  129 SER A CA  
5700 C C   . SER D 125 ? 2.0476 2.1137 1.9364 -0.2019 -0.1342 0.0749  129 SER A C   
5701 O O   . SER D 125 ? 2.4169 2.4845 2.3063 -0.2071 -0.1403 0.0793  129 SER A O   
5702 C CB  . SER D 125 ? 1.8094 1.8630 1.6834 -0.1989 -0.1285 0.0584  129 SER A CB  
5703 O OG  . SER D 125 ? 1.8967 1.9527 1.7787 -0.1935 -0.1238 0.0600  129 SER A OG  
5704 N N   . HIS D 126 ? 2.0260 2.0955 1.9238 -0.1974 -0.1306 0.0776  130 HIS A N   
5705 C CA  . HIS D 126 ? 2.0854 2.1618 1.9951 -0.1978 -0.1330 0.0863  130 HIS A CA  
5706 C C   . HIS D 126 ? 2.0366 2.1206 1.9552 -0.1919 -0.1272 0.0906  130 HIS A C   
5707 O O   . HIS D 126 ? 2.1503 2.2405 2.0793 -0.1905 -0.1269 0.0964  130 HIS A O   
5708 C CB  . HIS D 126 ? 2.3058 2.3796 2.2185 -0.1992 -0.1353 0.0856  130 HIS A CB  
5709 C CG  . HIS D 126 ? 2.5177 2.5840 2.4226 -0.2048 -0.1412 0.0810  130 HIS A CG  
5710 N ND1 . HIS D 126 ? 2.6195 2.6864 2.5240 -0.2106 -0.1481 0.0850  130 HIS A ND1 
5711 C CD2 . HIS D 126 ? 2.6530 2.7109 2.5506 -0.2055 -0.1415 0.0726  130 HIS A CD2 
5712 C CE1 . HIS D 126 ? 2.5897 2.6490 2.4866 -0.2147 -0.1522 0.0789  130 HIS A CE1 
5713 N NE2 . HIS D 126 ? 2.7178 2.7716 2.6106 -0.2116 -0.1483 0.0712  130 HIS A NE2 
5714 N N   . GLU D 127 ? 1.9571 2.0408 1.8718 -0.1884 -0.1227 0.0877  131 GLU A N   
5715 C CA  . GLU D 127 ? 1.9392 2.0293 1.8619 -0.1824 -0.1171 0.0905  131 GLU A CA  
5716 C C   . GLU D 127 ? 2.0517 2.1422 1.9710 -0.1810 -0.1155 0.0900  131 GLU A C   
5717 O O   . GLU D 127 ? 2.3129 2.3986 2.2244 -0.1788 -0.1119 0.0836  131 GLU A O   
5718 C CB  . GLU D 127 ? 1.9891 2.0771 1.9114 -0.1775 -0.1112 0.0856  131 GLU A CB  
5719 C CG  . GLU D 127 ? 2.2239 2.3190 2.1547 -0.1717 -0.1059 0.0888  131 GLU A CG  
5720 C CD  . GLU D 127 ? 2.4622 2.5562 2.3931 -0.1669 -0.1001 0.0846  131 GLU A CD  
5721 O OE1 . GLU D 127 ? 3.0099 3.0969 2.9340 -0.1678 -0.0999 0.0790  131 GLU A OE1 
5722 O OE2 . GLU D 127 ? 2.2281 2.3286 2.1665 -0.1624 -0.0958 0.0874  131 GLU A OE2 
5723 N N   . ALA D 128 ? 1.5369 1.6334 1.4628 -0.1825 -0.1183 0.0969  132 ALA A N   
5724 C CA  . ALA D 128 ? 1.7253 1.8233 1.6504 -0.1809 -0.1171 0.0976  132 ALA A CA  
5725 C C   . ALA D 128 ? 1.6474 1.7489 1.5788 -0.1736 -0.1103 0.0969  132 ALA A C   
5726 O O   . ALA D 128 ? 1.6310 1.7387 1.5730 -0.1703 -0.1081 0.1007  132 ALA A O   
5728 N N   . SER D 129 ? 1.6233 1.7210 1.5480 -0.1710 -0.1069 0.0919  133 SER A N   
5729 C CA  . SER D 129 ? 1.3538 1.4537 1.2831 -0.1640 -0.1006 0.0903  133 SER A CA  
5730 C C   . SER D 129 ? 1.5855 1.6883 1.5183 -0.1626 -0.1008 0.0933  133 SER A C   
5731 O O   . SER D 129 ? 1.6608 1.7627 1.5897 -0.1671 -0.1054 0.0952  133 SER A O   
5734 N N   . LEU D 130 a 1.5899 1.6965 1.5303 -0.1563 -0.0959 0.0935  133 LEU A N   
5735 C CA  . LEU D 130 a 1.8562 1.9659 1.8023 -0.1536 -0.0955 0.0960  133 LEU A CA  
5736 C C   . LEU D 130 a 2.2730 2.3783 2.2134 -0.1492 -0.0907 0.0901  133 LEU A C   
5737 O O   . LEU D 130 a 2.6983 2.7999 2.6316 -0.1511 -0.0924 0.0885  133 LEU A O   
5742 N N   . GLY D 131 ? 2.0586 2.1648 2.0023 -0.1434 -0.0850 0.0870  134 GLY A N   
5743 C CA  . GLY D 131 ? 2.2062 2.3092 2.1469 -0.1384 -0.0804 0.0823  134 GLY A CA  
5744 C C   . GLY D 131 ? 2.3251 2.4316 2.2734 -0.1362 -0.0813 0.0857  134 GLY A C   
5745 O O   . GLY D 131 ? 2.3484 2.4509 2.2913 -0.1357 -0.0812 0.0833  134 GLY A O   
5746 N N   . VAL D 132 ? 2.2342 2.3482 2.1955 -0.1350 -0.0826 0.0914  135 VAL A N   
5747 C CA  . VAL D 132 ? 2.3523 2.4695 2.3221 -0.1331 -0.0843 0.0951  135 VAL A CA  
5748 C C   . VAL D 132 ? 2.4402 2.5640 2.4232 -0.1264 -0.0800 0.0959  135 VAL A C   
5749 O O   . VAL D 132 ? 2.3919 2.5224 2.3876 -0.1256 -0.0820 0.1012  135 VAL A O   
5750 C CB  . VAL D 132 ? 2.2609 2.3809 2.2339 -0.1392 -0.0914 0.1019  135 VAL A CB  
5751 C CG1 . VAL D 132 ? 2.0915 2.2052 2.0501 -0.1460 -0.0952 0.1003  135 VAL A CG1 
5752 C CG2 . VAL D 132 ? 1.9221 2.0457 1.9054 -0.1376 -0.0938 0.1064  135 VAL A CG2 
5753 N N   . SER D 133 ? 2.2686 2.3908 2.2490 -0.1217 -0.0741 0.0904  136 SER A N   
5754 C CA  . SER D 133 ? 2.3964 2.5250 2.3878 -0.1154 -0.0694 0.0900  136 SER A CA  
5755 C C   . SER D 133 ? 2.4331 2.5625 2.4317 -0.1106 -0.0685 0.0897  136 SER A C   
5756 O O   . SER D 133 ? 2.4019 2.5255 2.3945 -0.1113 -0.0702 0.0881  136 SER A O   
5757 C CB  . SER D 133 ? 2.3848 2.5112 2.3701 -0.1124 -0.0636 0.0843  136 SER A CB  
5758 O OG  . SER D 133 ? 2.5760 2.7004 2.5541 -0.1172 -0.0650 0.0844  136 SER A OG  
5759 N N   . SER D 134 ? 2.5049 2.6419 2.5170 -0.1056 -0.0660 0.0911  137 SER A N   
5760 C CA  . SER D 134 ? 2.2601 2.3983 2.2809 -0.1004 -0.0651 0.0904  137 SER A CA  
5761 C C   . SER D 134 ? 2.3434 2.4772 2.3589 -0.0951 -0.0596 0.0834  137 SER A C   
5762 O O   . SER D 134 ? 2.1508 2.2838 2.1714 -0.0910 -0.0592 0.0821  137 SER A O   
5763 C CB  . SER D 134 ? 2.2873 2.4356 2.3253 -0.0967 -0.0644 0.0939  137 SER A CB  
5764 O OG  . SER D 134 ? 2.4520 2.6053 2.4922 -0.0933 -0.0587 0.0912  137 SER A OG  
5765 N N   . ALA D 135 ? 2.4404 2.5714 2.4462 -0.0950 -0.0556 0.0791  138 ALA A N   
5766 C CA  . ALA D 135 ? 2.7835 2.9105 2.7843 -0.0901 -0.0503 0.0726  138 ALA A CA  
5767 C C   . ALA D 135 ? 2.7355 2.8537 2.7272 -0.0911 -0.0521 0.0702  138 ALA A C   
5768 O O   . ALA D 135 ? 3.0038 3.1195 2.9963 -0.0864 -0.0496 0.0667  138 ALA A O   
5769 C CB  . ALA D 135 ? 2.9987 3.1248 2.9916 -0.0905 -0.0463 0.0693  138 ALA A CB  
5770 N N   . CYS D 136 ? 2.7389 2.8526 2.7218 -0.0972 -0.0564 0.0720  139 CYS A N   
5771 C CA  . CYS D 136 ? 2.5263 2.6327 2.5005 -0.0989 -0.0585 0.0704  139 CYS A CA  
5772 C C   . CYS D 136 ? 2.2703 2.3784 2.2493 -0.1028 -0.0648 0.0762  139 CYS A C   
5773 O O   . CYS D 136 ? 2.2540 2.3633 2.2308 -0.1085 -0.0688 0.0800  139 CYS A O   
5774 C CB  . CYS D 136 ? 2.5612 2.6609 2.5204 -0.1031 -0.0581 0.0670  139 CYS A CB  
5775 S SG  . CYS D 136 ? 3.2613 3.3588 3.2144 -0.1001 -0.0516 0.0609  139 CYS A SG  
5776 N N   . PRO D 137 ? 2.1924 2.3006 2.1781 -0.1001 -0.0663 0.0774  140 PRO A N   
5777 C CA  . PRO D 137 ? 2.0388 2.1489 2.0297 -0.1041 -0.0728 0.0836  140 PRO A CA  
5778 C C   . PRO D 137 ? 2.3638 2.4680 2.3425 -0.1097 -0.0765 0.0839  140 PRO A C   
5779 O O   . PRO D 137 ? 2.5288 2.6344 2.5111 -0.1131 -0.0821 0.0891  140 PRO A O   
5780 C CB  . PRO D 137 ? 1.5884 1.7009 1.5924 -0.0982 -0.0726 0.0842  140 PRO A CB  
5781 C CG  . PRO D 137 ? 1.7479 1.8554 1.7458 -0.0932 -0.0673 0.0774  140 PRO A CG  
5782 C CD  . PRO D 137 ? 1.8740 1.9805 1.8631 -0.0934 -0.0625 0.0733  140 PRO A CD  
5783 N N   . TYR D 138 ? 2.2469 2.3451 2.2116 -0.1108 -0.0736 0.0787  141 TYR A N   
5784 C CA  . TYR D 138 ? 2.4379 2.5310 2.3908 -0.1153 -0.0762 0.0779  141 TYR A CA  
5785 C C   . TYR D 138 ? 2.5267 2.6195 2.4854 -0.1134 -0.0785 0.0801  141 TYR A C   
5786 O O   . TYR D 138 ? 2.4300 2.5231 2.3965 -0.1071 -0.0757 0.0783  141 TYR A O   
5787 C CB  . TYR D 138 ? 2.5685 2.6627 2.5160 -0.1232 -0.0812 0.0817  141 TYR A CB  
5788 C CG  . TYR D 138 ? 2.6629 2.7533 2.5983 -0.1291 -0.0845 0.0817  141 TYR A CG  
5789 C CD1 . TYR D 138 ? 2.4501 2.5432 2.3882 -0.1338 -0.0907 0.0878  141 TYR A CD1 
5790 C CD2 . TYR D 138 ? 2.7699 2.8549 2.6915 -0.1305 -0.0817 0.0758  141 TYR A CD2 
5791 C CE1 . TYR D 138 ? 2.4085 2.4992 2.3353 -0.1396 -0.0936 0.0879  141 TYR A CE1 
5792 C CE2 . TYR D 138 ? 2.3334 2.4159 2.2440 -0.1360 -0.0844 0.0754  141 TYR A CE2 
5793 C CZ  . TYR D 138 ? 2.2043 2.2899 2.1173 -0.1406 -0.0903 0.0815  141 TYR A CZ  
5794 O OH  . TYR D 138 ? 2.0618 2.1458 1.9635 -0.1464 -0.0929 0.0812  141 TYR A OH  
5795 N N   . GLN D 139 ? 2.9010 2.9934 2.8560 -0.1190 -0.0838 0.0839  142 GLN A N   
5796 C CA  . GLN D 139 ? 2.9252 3.0184 2.8877 -0.1183 -0.0877 0.0879  142 GLN A CA  
5797 C C   . GLN D 139 ? 2.9828 3.0825 2.9608 -0.1184 -0.0919 0.0945  142 GLN A C   
5798 O O   . GLN D 139 ? 2.9582 3.0602 2.9493 -0.1125 -0.0909 0.0950  142 GLN A O   
5799 C CB  . GLN D 139 ? 2.8652 2.9560 2.8166 -0.1248 -0.0916 0.0895  142 GLN A CB  
5800 C CG  . GLN D 139 ? 2.6606 2.7453 2.5986 -0.1238 -0.0872 0.0828  142 GLN A CG  
5801 C CD  . GLN D 139 ? 2.4767 2.5598 2.4029 -0.1305 -0.0905 0.0838  142 GLN A CD  
5802 O OE1 . GLN D 139 ? 2.4943 2.5804 2.4187 -0.1369 -0.0954 0.0884  142 GLN A OE1 
5803 N NE2 . GLN D 139 ? 2.2091 2.2877 2.1269 -0.1291 -0.0877 0.0795  142 GLN A NE2 
5804 N N   . GLY D 140 ? 2.6394 2.7420 2.6163 -0.1249 -0.0967 0.0995  143 GLY A N   
5805 C CA  . GLY D 140 ? 2.0620 2.1707 2.0536 -0.1256 -0.1012 0.1064  143 GLY A CA  
5806 C C   . GLY D 140 ? 1.9831 2.0958 1.9773 -0.1273 -0.1010 0.1080  143 GLY A C   
5807 O O   . GLY D 140 ? 2.0215 2.1398 2.0298 -0.1262 -0.1033 0.1128  143 GLY A O   
5808 N N   . LYS D 141 ? 2.1254 2.2354 2.1068 -0.1301 -0.0985 0.1042  144 LYS A N   
5809 C CA  . LYS D 141 ? 2.1879 2.3010 2.1703 -0.1325 -0.0988 0.1058  144 LYS A CA  
5810 C C   . LYS D 141 ? 2.4490 2.5615 2.4308 -0.1270 -0.0919 0.1000  144 LYS A C   
5811 O O   . LYS D 141 ? 2.5577 2.6650 2.5290 -0.1253 -0.0876 0.0938  144 LYS A O   
5812 C CB  . LYS D 141 ? 2.0459 2.1563 2.0142 -0.1405 -0.1020 0.1061  144 LYS A CB  
5813 C CG  . LYS D 141 ? 1.7494 1.8612 1.7169 -0.1473 -0.1093 0.1124  144 LYS A CG  
5814 C CD  . LYS D 141 ? 1.6449 1.7539 1.5971 -0.1548 -0.1116 0.1111  144 LYS A CD  
5815 C CE  . LYS D 141 ? 1.8312 1.9420 1.7813 -0.1623 -0.1189 0.1173  144 LYS A CE  
5816 N NZ  . LYS D 141 ? 2.0264 2.1348 1.9611 -0.1697 -0.1210 0.1155  144 LYS A NZ  
5817 N N   . SER D 142 ? 2.2436 2.3619 2.2367 -0.1244 -0.0908 0.1022  145 SER A N   
5818 C CA  . SER D 142 ? 2.2410 2.3599 2.2332 -0.1203 -0.0847 0.0975  145 SER A CA  
5819 C C   . SER D 142 ? 2.5003 2.6143 2.4774 -0.1247 -0.0839 0.0940  145 SER A C   
5820 O O   . SER D 142 ? 2.4768 2.5901 2.4484 -0.1312 -0.0885 0.0969  145 SER A O   
5821 C CB  . SER D 142 ? 1.9791 2.1061 1.9852 -0.1186 -0.0846 0.1016  145 SER A CB  
5822 O OG  . SER D 142 ? 1.9523 2.0816 1.9583 -0.1251 -0.0898 0.1071  145 SER A OG  
5823 N N   . SER D 143 ? 2.4295 2.5397 2.3999 -0.1211 -0.0782 0.0875  146 SER A N   
5824 C CA  . SER D 143 ? 2.4475 2.5517 2.4033 -0.1248 -0.0775 0.0832  146 SER A CA  
5825 C C   . SER D 143 ? 2.1600 2.2632 2.1140 -0.1206 -0.0715 0.0782  146 SER A C   
5826 O O   . SER D 143 ? 2.3513 2.4596 2.3151 -0.1159 -0.0683 0.0788  146 SER A O   
5827 C CB  . SER D 143 ? 2.6822 2.7802 2.6274 -0.1265 -0.0783 0.0804  146 SER A CB  
5828 O OG  . SER D 143 ? 2.8157 2.9149 2.7613 -0.1315 -0.0843 0.0855  146 SER A OG  
5829 N N   . PHE D 144 ? 2.0005 2.0974 1.9420 -0.1224 -0.0699 0.0731  147 PHE A N   
5830 C CA  . PHE D 144 ? 1.7773 1.8727 1.7158 -0.1200 -0.0652 0.0687  147 PHE A CA  
5831 C C   . PHE D 144 ? 1.5754 1.6628 1.5020 -0.1195 -0.0626 0.0624  147 PHE A C   
5832 O O   . PHE D 144 ? 1.6288 1.7127 1.5498 -0.1210 -0.0643 0.0615  147 PHE A O   
5833 C CB  . PHE D 144 ? 1.8405 1.9373 1.7778 -0.1245 -0.0674 0.0706  147 PHE A CB  
5834 C CG  . PHE D 144 ? 1.6949 1.7928 1.6334 -0.1218 -0.0632 0.0682  147 PHE A CG  
5835 C CD1 . PHE D 144 ? 1.9554 2.0603 1.9047 -0.1173 -0.0601 0.0701  147 PHE A CD1 
5836 C CD2 . PHE D 144 ? 1.4733 1.5656 1.4024 -0.1240 -0.0624 0.0639  147 PHE A CD2 
5837 C CE1 . PHE D 144 ? 2.0705 2.1771 2.0206 -0.1154 -0.0563 0.0683  147 PHE A CE1 
5838 C CE2 . PHE D 144 ? 1.3719 1.4654 1.3025 -0.1220 -0.0590 0.0623  147 PHE A CE2 
5839 C CZ  . PHE D 144 ? 1.8458 1.9467 1.7866 -0.1179 -0.0560 0.0647  147 PHE A CZ  
5840 N N   . PHE D 145 ? 1.3840 1.4692 1.3073 -0.1174 -0.0585 0.0581  148 PHE A N   
5841 C CA  . PHE D 145 ? 1.1753 1.2529 1.0877 -0.1171 -0.0561 0.0521  148 PHE A CA  
5842 C C   . PHE D 145 ? 1.2162 1.2894 1.1188 -0.1233 -0.0597 0.0509  148 PHE A C   
5843 O O   . PHE D 145 ? 1.2793 1.3539 1.1818 -0.1274 -0.0627 0.0528  148 PHE A O   
5844 C CB  . PHE D 145 ? 1.3407 1.4173 1.2524 -0.1143 -0.0516 0.0485  148 PHE A CB  
5845 C CG  . PHE D 145 ? 1.3995 1.4807 1.3199 -0.1084 -0.0475 0.0490  148 PHE A CG  
5846 C CD1 . PHE D 145 ? 1.3908 1.4706 1.3123 -0.1038 -0.0450 0.0470  148 PHE A CD1 
5847 C CD2 . PHE D 145 ? 1.8398 1.9270 1.7672 -0.1074 -0.0462 0.0512  148 PHE A CD2 
5848 C CE1 . PHE D 145 ? 1.9101 1.9943 1.8394 -0.0983 -0.0412 0.0468  148 PHE A CE1 
5849 C CE2 . PHE D 145 ? 2.2390 2.3312 2.1739 -0.1021 -0.0421 0.0511  148 PHE A CE2 
5850 C CZ  . PHE D 145 ? 2.2320 2.3226 2.1679 -0.0974 -0.0396 0.0486  148 PHE A CZ  
5851 N N   . ARG D 146 ? 1.2342 1.3022 1.1282 -0.1241 -0.0596 0.0475  149 ARG A N   
5852 C CA  . ARG D 146 ? 1.4296 1.4941 1.3141 -0.1299 -0.0629 0.0459  149 ARG A CA  
5853 C C   . ARG D 146 ? 1.6833 1.7433 1.5615 -0.1316 -0.0617 0.0411  149 ARG A C   
5854 O O   . ARG D 146 ? 1.8380 1.8972 1.7122 -0.1366 -0.0652 0.0411  149 ARG A O   
5855 C CB  . ARG D 146 ? 1.0743 1.1354 0.9517 -0.1303 -0.0628 0.0436  149 ARG A CB  
5856 C CG  . ARG D 146 ? 1.7262 1.7914 1.6093 -0.1301 -0.0655 0.0489  149 ARG A CG  
5857 C CD  . ARG D 146 ? 1.6740 1.7361 1.5496 -0.1312 -0.0658 0.0469  149 ARG A CD  
5858 N NE  . ARG D 146 ? 1.8334 1.8992 1.7151 -0.1310 -0.0686 0.0522  149 ARG A NE  
5859 C CZ  . ARG D 146 ? 1.9796 2.0441 1.8573 -0.1317 -0.0694 0.0521  149 ARG A CZ  
5860 N NH1 . ARG D 146 ? 2.0521 2.1120 1.9193 -0.1326 -0.0673 0.0470  149 ARG A NH1 
5861 N NH2 . ARG D 146 ? 1.9897 2.0578 1.8747 -0.1315 -0.0726 0.0576  149 ARG A NH2 
5862 N N   . ASN D 147 ? 1.3736 1.4306 1.2511 -0.1274 -0.0572 0.0370  150 ASN A N   
5863 C CA  . ASN D 147 ? 1.1637 1.2156 1.0352 -0.1289 -0.0561 0.0321  150 ASN A CA  
5864 C C   . ASN D 147 ? 1.1499 1.2042 1.0261 -0.1307 -0.0577 0.0343  150 ASN A C   
5865 O O   . ASN D 147 ? 1.2015 1.2516 1.0736 -0.1324 -0.0578 0.0307  150 ASN A O   
5866 C CB  . ASN D 147 ? 1.0608 1.1086 0.9303 -0.1241 -0.0510 0.0275  150 ASN A CB  
5867 C CG  . ASN D 147 ? 1.3531 1.3982 1.2178 -0.1224 -0.0495 0.0253  150 ASN A CG  
5868 O OD1 . ASN D 147 ? 1.5750 1.6209 1.4369 -0.1252 -0.0523 0.0268  150 ASN A OD1 
5869 N ND2 . ASN D 147 ? 1.4564 1.4983 1.3202 -0.1180 -0.0452 0.0219  150 ASN A ND2 
5870 N N   . VAL D 148 ? 0.9892 1.0502 0.8744 -0.1303 -0.0591 0.0402  151 VAL A N   
5871 C CA  . VAL D 148 ? 0.9748 1.0389 0.8651 -0.1319 -0.0606 0.0429  151 VAL A CA  
5872 C C   . VAL D 148 ? 1.2525 1.3227 1.1489 -0.1348 -0.0649 0.0493  151 VAL A C   
5873 O O   . VAL D 148 ? 1.4303 1.5035 1.3297 -0.1339 -0.0657 0.0522  151 VAL A O   
5874 C CB  . VAL D 148 ? 1.0651 1.1323 0.9619 -0.1270 -0.0561 0.0432  151 VAL A CB  
5875 C CG1 . VAL D 148 ? 0.9640 1.0353 0.8665 -0.1290 -0.0577 0.0465  151 VAL A CG1 
5876 C CG2 . VAL D 148 ? 1.2033 1.2643 1.0942 -0.1242 -0.0520 0.0371  151 VAL A CG2 
5877 N N   . VAL D 149 ? 1.3257 1.3974 1.2242 -0.1386 -0.0682 0.0517  152 VAL A N   
5878 C CA  . VAL D 149 ? 1.2980 1.3743 1.2007 -0.1426 -0.0733 0.0575  152 VAL A CA  
5879 C C   . VAL D 149 ? 1.4791 1.5633 1.3935 -0.1407 -0.0727 0.0631  152 VAL A C   
5880 O O   . VAL D 149 ? 1.4322 1.5173 1.3490 -0.1407 -0.0719 0.0631  152 VAL A O   
5881 C CB  . VAL D 149 ? 1.2593 1.3315 1.1558 -0.1487 -0.0781 0.0562  152 VAL A CB  
5882 C CG1 . VAL D 149 ? 1.6223 1.6987 1.5220 -0.1533 -0.0836 0.0620  152 VAL A CG1 
5883 C CG2 . VAL D 149 ? 1.5157 1.5802 1.4005 -0.1501 -0.0776 0.0493  152 VAL A CG2 
5884 N N   . TRP D 150 ? 1.6830 1.7734 1.6052 -0.1393 -0.0734 0.0681  153 TRP A N   
5885 C CA  . TRP D 150 ? 1.6536 1.7526 1.5879 -0.1371 -0.0726 0.0735  153 TRP A CA  
5886 C C   . TRP D 150 ? 1.6453 1.7476 1.5831 -0.1425 -0.0783 0.0790  153 TRP A C   
5887 O O   . TRP D 150 ? 1.8436 1.9489 1.7851 -0.1447 -0.0820 0.0835  153 TRP A O   
5888 C CB  . TRP D 150 ? 1.9838 2.0874 1.9253 -0.1325 -0.0704 0.0754  153 TRP A CB  
5889 C CG  . TRP D 150 ? 2.1689 2.2819 2.1234 -0.1295 -0.0689 0.0803  153 TRP A CG  
5890 C CD1 . TRP D 150 ? 2.0627 2.1800 2.0226 -0.1246 -0.0637 0.0791  153 TRP A CD1 
5891 C CD2 . TRP D 150 ? 2.3669 2.4867 2.3312 -0.1309 -0.0724 0.0869  153 TRP A CD2 
5892 N NE1 . TRP D 150 ? 1.8360 1.9629 1.8084 -0.1228 -0.0635 0.0843  153 TRP A NE1 
5893 C CE2 . TRP D 150 ? 2.0885 2.2169 2.0642 -0.1265 -0.0689 0.0892  153 TRP A CE2 
5894 C CE3 . TRP D 150 ? 2.3283 2.4482 2.2930 -0.1356 -0.0783 0.0911  153 TRP A CE3 
5895 C CZ2 . TRP D 150 ? 2.1266 2.2634 2.1146 -0.1265 -0.0710 0.0955  153 TRP A CZ2 
5896 C CZ3 . TRP D 150 ? 2.2025 2.3304 2.1794 -0.1358 -0.0807 0.0978  153 TRP A CZ3 
5897 C CH2 . TRP D 150 ? 2.1674 2.3035 2.1560 -0.1311 -0.0770 0.0998  153 TRP A CH2 
5898 N N   . LEU D 151 ? 1.4701 1.5715 1.4068 -0.1448 -0.0792 0.0787  154 LEU A N   
5899 C CA  . LEU D 151 ? 1.4876 1.5898 1.4252 -0.1507 -0.0850 0.0826  154 LEU A CA  
5900 C C   . LEU D 151 ? 1.4513 1.5633 1.4016 -0.1505 -0.0864 0.0903  154 LEU A C   
5901 O O   . LEU D 151 ? 1.5912 1.7096 1.5496 -0.1459 -0.0821 0.0918  154 LEU A O   
5902 C CB  . LEU D 151 ? 1.6755 1.7731 1.6084 -0.1527 -0.0854 0.0792  154 LEU A CB  
5903 C CG  . LEU D 151 ? 1.6120 1.6996 1.5330 -0.1538 -0.0850 0.0716  154 LEU A CG  
5904 C CD1 . LEU D 151 ? 1.9094 1.9943 1.8296 -0.1550 -0.0853 0.0696  154 LEU A CD1 
5905 C CD2 . LEU D 151 ? 1.4893 1.5721 1.4024 -0.1590 -0.0900 0.0703  154 LEU A CD2 
5906 N N   . ILE D 152 ? 1.3260 1.4394 1.2781 -0.1556 -0.0924 0.0951  155 ILE A N   
5907 C CA  . ILE D 152 ? 1.4207 1.5432 1.3849 -0.1563 -0.0945 0.1029  155 ILE A CA  
5908 C C   . ILE D 152 ? 1.4432 1.5646 1.4064 -0.1628 -0.1008 0.1062  155 ILE A C   
5909 O O   . ILE D 152 ? 1.5650 1.6786 1.5182 -0.1667 -0.1038 0.1023  155 ILE A O   
5910 C CB  . ILE D 152 ? 1.3593 1.4860 1.3295 -0.1557 -0.0961 0.1071  155 ILE A CB  
5911 C CG1 . ILE D 152 ? 1.5746 1.7029 1.5477 -0.1492 -0.0905 0.1045  155 ILE A CG1 
5912 C CG2 . ILE D 152 ? 1.2532 1.3896 1.2370 -0.1562 -0.0983 0.1152  155 ILE A CG2 
5913 C CD1 . ILE D 152 ? 1.5716 1.7022 1.5493 -0.1495 -0.0931 0.1082  155 ILE A CD1 
5914 N N   . LYS D 153 ? 1.2992 1.4290 1.2734 -0.1637 -0.1028 0.1133  156 LYS A N   
5915 C CA  . LYS D 153 ? 1.3512 1.4816 1.3272 -0.1699 -0.1094 0.1183  156 LYS A CA  
5916 C C   . LYS D 153 ? 1.4968 1.6218 1.4656 -0.1751 -0.1153 0.1183  156 LYS A C   
5917 O O   . LYS D 153 ? 1.5300 1.6537 1.4962 -0.1739 -0.1145 0.1170  156 LYS A O   
5918 C CB  . LYS D 153 ? 1.4665 1.6081 1.4570 -0.1691 -0.1100 0.1266  156 LYS A CB  
5919 C CG  . LYS D 153 ? 1.7699 1.9185 1.7678 -0.1644 -0.1043 0.1270  156 LYS A CG  
5920 C CD  . LYS D 153 ? 1.9749 2.1197 1.9680 -0.1670 -0.1054 0.1251  156 LYS A CD  
5921 C CE  . LYS D 153 ? 1.8266 1.9786 1.8264 -0.1632 -0.1003 0.1259  156 LYS A CE  
5922 N NZ  . LYS D 153 ? 1.8303 1.9795 1.8268 -0.1655 -0.1011 0.1246  156 LYS A NZ  
5923 N N   . LYS D 154 ? 1.7586 1.8807 1.7244 -0.1811 -0.1213 0.1200  157 LYS A N   
5924 C CA  . LYS D 154 ? 1.6635 1.7813 1.6227 -0.1870 -0.1276 0.1207  157 LYS A CA  
5925 C C   . LYS D 154 ? 1.6776 1.8008 1.6454 -0.1915 -0.1336 0.1292  157 LYS A C   
5926 O O   . LYS D 154 ? 1.9058 2.0275 1.8734 -0.1949 -0.1371 0.1301  157 LYS A O   
5927 C CB  . LYS D 154 ? 1.7404 1.8480 1.6859 -0.1904 -0.1295 0.1133  157 LYS A CB  
5928 C CG  . LYS D 154 ? 1.7698 1.8731 1.7071 -0.1967 -0.1356 0.1130  157 LYS A CG  
5929 C CD  . LYS D 154 ? 1.8672 1.9609 1.7913 -0.1994 -0.1367 0.1046  157 LYS A CD  
5930 C CE  . LYS D 154 ? 1.9265 2.0165 1.8417 -0.2059 -0.1426 0.1039  157 LYS A CE  
5931 N NZ  . LYS D 154 ? 2.2056 2.2866 2.1082 -0.2083 -0.1434 0.0950  157 LYS A NZ  
5932 N N   . ASN D 155 ? 1.5010 1.6304 1.4767 -0.1916 -0.1352 0.1355  158 ASN A N   
5933 C CA  . ASN D 155 ? 1.7481 1.8839 1.7338 -0.1953 -0.1406 0.1443  158 ASN A CA  
5934 C C   . ASN D 155 ? 1.8678 2.0097 1.8631 -0.1934 -0.1388 0.1477  158 ASN A C   
5935 O O   . ASN D 155 ? 1.8766 2.0191 1.8740 -0.1979 -0.1438 0.1516  158 ASN A O   
5936 C CB  . ASN D 155 ? 1.9671 2.0971 1.9448 -0.2032 -0.1486 0.1451  158 ASN A CB  
5937 C CG  . ASN D 155 ? 1.9114 2.0476 1.8989 -0.2073 -0.1547 0.1547  158 ASN A CG  
5938 O OD1 . ASN D 155 ? 1.9045 2.0451 1.8978 -0.2069 -0.1554 0.1592  158 ASN A OD1 
5939 N ND2 . ASN D 155 ? 1.6044 1.7410 1.5944 -0.2114 -0.1593 0.1582  158 ASN A ND2 
5940 N N   . SER D 156 ? 2.0331 2.1799 2.0340 -0.1868 -0.1317 0.1461  159 SER A N   
5941 C CA  . SER D 156 ? 1.9445 2.0981 1.9540 -0.1845 -0.1288 0.1487  159 SER A CA  
5942 C C   . SER D 156 ? 2.1063 2.2536 2.1085 -0.1876 -0.1309 0.1454  159 SER A C   
5943 O O   . SER D 156 ? 2.1904 2.3425 2.1993 -0.1890 -0.1323 0.1498  159 SER A O   
5944 C CB  . SER D 156 ? 1.7690 1.9330 1.7927 -0.1858 -0.1317 0.1583  159 SER A CB  
5945 O OG  . SER D 156 ? 2.0241 2.1857 2.0466 -0.1927 -0.1394 0.1625  159 SER A OG  
5946 N N   . THR D 157 ? 1.9846 2.1214 1.9736 -0.1889 -0.1313 0.1378  160 THR A N   
5947 C CA  . THR D 157 ? 1.9867 2.1167 1.9688 -0.1911 -0.1326 0.1333  160 THR A CA  
5948 C C   . THR D 157 ? 2.0255 2.1498 1.9995 -0.1866 -0.1264 0.1247  160 THR A C   
5949 O O   . THR D 157 ? 2.2174 2.3378 2.1848 -0.1848 -0.1243 0.1204  160 THR A O   
5950 C CB  . THR D 157 ? 2.2329 2.3546 2.2064 -0.1979 -0.1401 0.1318  160 THR A CB  
5951 O OG1 . THR D 157 ? 2.4957 2.6100 2.4577 -0.1979 -0.1393 0.1251  160 THR A OG1 
5952 C CG2 . THR D 157 ? 2.3371 2.4637 2.3175 -0.2026 -0.1465 0.1403  160 THR A CG2 
5953 N N   . TYR D 158 ? 2.0754 2.1992 2.0498 -0.1849 -0.1239 0.1225  161 TYR A N   
5954 C CA  . TYR D 158 ? 2.0483 2.1666 2.0155 -0.1809 -0.1183 0.1146  161 TYR A CA  
5955 C C   . TYR D 158 ? 2.0980 2.2124 2.0637 -0.1828 -0.1198 0.1126  161 TYR A C   
5956 O O   . TYR D 158 ? 2.0846 2.2045 2.0567 -0.1805 -0.1167 0.1148  161 TYR A O   
5957 C CB  . TYR D 158 ? 1.9482 2.0737 1.9214 -0.1743 -0.1108 0.1151  161 TYR A CB  
5958 C CG  . TYR D 158 ? 1.9415 2.0620 1.9080 -0.1699 -0.1049 0.1076  161 TYR A CG  
5959 C CD1 . TYR D 158 ? 1.9339 2.0556 1.9021 -0.1682 -0.1019 0.1065  161 TYR A CD1 
5960 C CD2 . TYR D 158 ? 1.9339 2.0483 1.8920 -0.1680 -0.1027 0.1018  161 TYR A CD2 
5961 C CE1 . TYR D 158 ? 1.7719 1.8888 1.7340 -0.1645 -0.0969 0.0999  161 TYR A CE1 
5962 C CE2 . TYR D 158 ? 1.9006 2.0105 1.8530 -0.1640 -0.0974 0.0952  161 TYR A CE2 
5963 C CZ  . TYR D 158 ? 1.6848 1.7957 1.6392 -0.1623 -0.0946 0.0942  161 TYR A CZ  
5964 O OH  . TYR D 158 ? 1.6050 1.7112 1.5537 -0.1586 -0.0896 0.0879  161 TYR A OH  
5965 N N   . PRO D 159 ? 2.1663 2.2716 2.1242 -0.1873 -0.1249 0.1086  162 PRO A N   
5966 C CA  . PRO D 159 ? 1.9934 2.0939 1.9500 -0.1891 -0.1267 0.1061  162 PRO A CA  
5967 C C   . PRO D 159 ? 1.7653 1.8633 1.7188 -0.1843 -0.1202 0.1002  162 PRO A C   
5968 O O   . PRO D 159 ? 1.7155 1.8122 1.6643 -0.1802 -0.1151 0.0959  162 PRO A O   
5969 C CB  . PRO D 159 ? 2.1120 2.2024 2.0594 -0.1940 -0.1326 0.1010  162 PRO A CB  
5970 C CG  . PRO D 159 ? 2.2601 2.3491 2.2012 -0.1936 -0.1316 0.0989  162 PRO A CG  
5971 C CD  . PRO D 159 ? 2.2049 2.3044 2.1552 -0.1913 -0.1295 0.1066  162 PRO A CD  
5972 N N   . THR D 160 ? 1.7330 1.8308 1.6898 -0.1848 -0.1208 0.1007  163 THR A N   
5973 C CA  . THR D 160 ? 1.6659 1.7594 1.6187 -0.1814 -0.1160 0.0946  163 THR A CA  
5974 C C   . THR D 160 ? 1.6314 1.7135 1.5729 -0.1819 -0.1165 0.0856  163 THR A C   
5975 O O   . THR D 160 ? 1.6486 1.7242 1.5862 -0.1864 -0.1223 0.0834  163 THR A O   
5976 C CB  . THR D 160 ? 1.5175 1.6112 1.4753 -0.1834 -0.1183 0.0966  163 THR A CB  
5977 O OG1 . THR D 160 ? 1.6946 1.7817 1.6508 -0.1889 -0.1260 0.0959  163 THR A OG1 
5978 C CG2 . THR D 160 ? 1.7973 1.9033 1.7661 -0.1831 -0.1175 0.1056  163 THR A CG2 
5979 N N   . ILE D 161 ? 1.6142 1.6942 1.5503 -0.1774 -0.1105 0.0805  164 ILE A N   
5980 C CA  . ILE D 161 ? 1.5409 1.6117 1.4664 -0.1775 -0.1103 0.0723  164 ILE A CA  
5981 C C   . ILE D 161 ? 1.6250 1.6895 1.5466 -0.1750 -0.1069 0.0656  164 ILE A C   
5982 O O   . ILE D 161 ? 1.6909 1.7588 1.6152 -0.1707 -0.1014 0.0660  164 ILE A O   
5983 C CB  . ILE D 161 ? 1.5911 1.6639 1.5129 -0.1750 -0.1071 0.0718  164 ILE A CB  
5984 C CG1 . ILE D 161 ? 1.6954 1.7727 1.6204 -0.1787 -0.1120 0.0779  164 ILE A CG1 
5985 C CG2 . ILE D 161 ? 1.8284 1.8926 1.7393 -0.1747 -0.1058 0.0634  164 ILE A CG2 
5986 C CD1 . ILE D 161 ? 1.9166 1.9980 1.8414 -0.1766 -0.1095 0.0798  164 ILE A CD1 
5987 N N   . LYS D 162 ? 1.5816 1.6370 1.4973 -0.1778 -0.1103 0.0595  165 LYS A N   
5988 C CA  . LYS D 162 ? 1.6219 1.6702 1.5349 -0.1766 -0.1089 0.0531  165 LYS A CA  
5989 C C   . LYS D 162 ? 1.6534 1.6934 1.5558 -0.1766 -0.1081 0.0443  165 LYS A C   
5990 O O   . LYS D 162 ? 1.7802 1.8165 1.6783 -0.1805 -0.1128 0.0420  165 LYS A O   
5991 C CB  . LYS D 162 ? 1.7776 1.8228 1.6952 -0.1807 -0.1149 0.0541  165 LYS A CB  
5992 C CG  . LYS D 162 ? 1.9837 2.0368 1.9117 -0.1814 -0.1162 0.0626  165 LYS A CG  
5993 C CD  . LYS D 162 ? 2.0915 2.1405 2.0237 -0.1860 -0.1231 0.0633  165 LYS A CD  
5994 C CE  . LYS D 162 ? 2.0582 2.1160 2.0011 -0.1872 -0.1245 0.0724  165 LYS A CE  
5995 N NZ  . LYS D 162 ? 1.8779 1.9325 1.8263 -0.1919 -0.1319 0.0744  165 LYS A NZ  
5996 N N   . ARG D 163 ? 1.3415 1.3790 1.2398 -0.1723 -0.1023 0.0395  166 ARG A N   
5997 C CA  . ARG D 163 ? 1.4244 1.4559 1.3129 -0.1716 -0.1004 0.0318  166 ARG A CA  
5998 C C   . ARG D 163 ? 1.3848 1.4112 1.2711 -0.1680 -0.0959 0.0259  166 ARG A C   
5999 O O   . ARG D 163 ? 1.5331 1.5630 1.4234 -0.1643 -0.0916 0.0285  166 ARG A O   
6000 C CB  . ARG D 163 ? 1.7203 1.7567 1.6060 -0.1697 -0.0974 0.0342  166 ARG A CB  
6001 C CG  . ARG D 163 ? 1.8345 1.8751 1.7218 -0.1736 -0.1022 0.0394  166 ARG A CG  
6002 C CD  . ARG D 163 ? 2.2493 2.2950 2.1353 -0.1716 -0.0995 0.0424  166 ARG A CD  
6003 N NE  . ARG D 163 ? 2.3419 2.3919 2.2306 -0.1757 -0.1045 0.0482  166 ARG A NE  
6004 C CZ  . ARG D 163 ? 2.3711 2.4271 2.2618 -0.1751 -0.1040 0.0532  166 ARG A CZ  
6005 N NH1 . ARG D 163 ? 2.4560 2.5155 2.3485 -0.1702 -0.0986 0.0541  166 ARG A NH1 
6006 N NH2 . ARG D 163 ? 2.3441 2.4027 2.2360 -0.1796 -0.1093 0.0577  166 ARG A NH2 
6007 N N   . SER D 164 ? 1.3220 1.3404 1.2020 -0.1691 -0.0968 0.0179  167 SER A N   
6008 C CA  . SER D 164 ? 1.4705 1.4836 1.3492 -0.1661 -0.0932 0.0123  167 SER A CA  
6009 C C   . SER D 164 ? 1.8348 1.8426 1.7041 -0.1651 -0.0907 0.0042  167 SER A C   
6010 O O   . SER D 164 ? 2.1141 2.1192 1.9779 -0.1684 -0.0939 0.0004  167 SER A O   
6011 C CB  . SER D 164 ? 1.7587 1.7669 1.6422 -0.1683 -0.0973 0.0106  167 SER A CB  
6012 O OG  . SER D 164 ? 2.0005 2.0043 1.8842 -0.1653 -0.0938 0.0062  167 SER A OG  
6013 N N   . TYR D 165 ? 1.5332 1.5397 1.4004 -0.1608 -0.0851 0.0014  168 TYR A N   
6014 C CA  . TYR D 165 ? 1.4784 1.4807 1.3369 -0.1596 -0.0822 -0.0058 168 TYR A CA  
6015 C C   . TYR D 165 ? 1.3752 1.3720 1.2337 -0.1566 -0.0787 -0.0112 168 TYR A C   
6016 O O   . TYR D 165 ? 1.4711 1.4697 1.3336 -0.1532 -0.0752 -0.0083 168 TYR A O   
6017 C CB  . TYR D 165 ? 1.5481 1.5556 1.4030 -0.1575 -0.0786 -0.0029 168 TYR A CB  
6018 C CG  . TYR D 165 ? 2.2214 2.2319 2.0727 -0.1613 -0.0822 -0.0009 168 TYR A CG  
6019 C CD1 . TYR D 165 ? 2.5447 2.5604 2.4016 -0.1637 -0.0860 0.0063  168 TYR A CD1 
6020 C CD2 . TYR D 165 ? 2.6376 2.6458 2.4799 -0.1629 -0.0821 -0.0062 168 TYR A CD2 
6021 C CE1 . TYR D 165 ? 2.6656 2.6839 2.5195 -0.1675 -0.0897 0.0084  168 TYR A CE1 
6022 C CE2 . TYR D 165 ? 2.8421 2.8533 2.6809 -0.1668 -0.0856 -0.0041 168 TYR A CE2 
6023 C CZ  . TYR D 165 ? 2.8602 2.8761 2.7048 -0.1691 -0.0895 0.0032  168 TYR A CZ  
6024 O OH  . TYR D 165 ? 2.9730 2.9916 2.8140 -0.1733 -0.0933 0.0055  168 TYR A OH  
6025 N N   . ASN D 166 ? 1.9116 1.9017 1.7656 -0.1579 -0.0798 -0.0192 169 ASN A N   
6026 C CA  . ASN D 166 ? 1.8572 1.8415 1.7103 -0.1553 -0.0767 -0.0257 169 ASN A CA  
6027 C C   . ASN D 166 ? 1.7845 1.7694 1.6310 -0.1519 -0.0709 -0.0281 169 ASN A C   
6028 O O   . ASN D 166 ? 1.6588 1.6474 1.5000 -0.1523 -0.0701 -0.0268 169 ASN A O   
6029 C CB  . ASN D 166 ? 1.8864 1.8639 1.7376 -0.1581 -0.0801 -0.0338 169 ASN A CB  
6030 C CG  . ASN D 166 ? 2.2024 2.1775 2.0616 -0.1607 -0.0855 -0.0322 169 ASN A CG  
6031 O OD1 . ASN D 166 ? 2.5077 2.4850 2.3741 -0.1597 -0.0857 -0.0263 169 ASN A OD1 
6032 N ND2 . ASN D 166 ? 2.0670 2.0379 1.9252 -0.1642 -0.0902 -0.0374 169 ASN A ND2 
6033 N N   . ASN D 167 ? 1.7616 1.7428 1.6090 -0.1486 -0.0672 -0.0313 170 ASN A N   
6034 C CA  . ASN D 167 ? 1.7467 1.7269 1.5878 -0.1456 -0.0622 -0.0352 170 ASN A CA  
6035 C C   . ASN D 167 ? 1.9371 1.9114 1.7736 -0.1468 -0.0625 -0.0445 170 ASN A C   
6036 O O   . ASN D 167 ? 2.0020 1.9715 1.8393 -0.1446 -0.0601 -0.0492 170 ASN A O   
6037 C CB  . ASN D 167 ? 1.8019 1.7820 1.6464 -0.1412 -0.0579 -0.0330 170 ASN A CB  
6038 C CG  . ASN D 167 ? 2.2368 2.2180 2.0754 -0.1380 -0.0530 -0.0342 170 ASN A CG  
6039 O OD1 . ASN D 167 ? 2.2227 2.2061 2.0553 -0.1392 -0.0529 -0.0351 170 ASN A OD1 
6040 N ND2 . ASN D 167 ? 2.3974 2.3771 2.2378 -0.1343 -0.0491 -0.0340 170 ASN A ND2 
6041 N N   . THR D 168 ? 2.0970 2.0718 1.9288 -0.1505 -0.0657 -0.0471 171 THR A N   
6042 C CA  . THR D 168 ? 2.1317 2.1020 1.9582 -0.1519 -0.0658 -0.0564 171 THR A CA  
6043 C C   . THR D 168 ? 2.0508 2.0202 1.8722 -0.1487 -0.0602 -0.0606 171 THR A C   
6044 O O   . THR D 168 ? 2.1492 2.1136 1.9703 -0.1477 -0.0588 -0.0679 171 THR A O   
6045 C CB  . THR D 168 ? 1.9503 1.9231 1.7704 -0.1563 -0.0691 -0.0578 171 THR A CB  
6046 O OG1 . THR D 168 ? 2.1361 2.1149 1.9510 -0.1560 -0.0669 -0.0532 171 THR A OG1 
6047 C CG2 . THR D 168 ? 1.6005 1.5740 1.4257 -0.1598 -0.0750 -0.0538 171 THR A CG2 
6048 N N   . ASN D 169 ? 1.8322 1.8065 1.6502 -0.1470 -0.0572 -0.0559 172 ASN A N   
6049 C CA  . ASN D 169 ? 1.8398 1.8137 1.6532 -0.1439 -0.0521 -0.0588 172 ASN A CA  
6050 C C   . ASN D 169 ? 2.0340 2.0034 1.8529 -0.1401 -0.0493 -0.0600 172 ASN A C   
6051 O O   . ASN D 169 ? 2.0910 2.0607 1.9164 -0.1386 -0.0497 -0.0546 172 ASN A O   
6052 C CB  . ASN D 169 ? 1.7874 1.7671 1.5979 -0.1427 -0.0501 -0.0524 172 ASN A CB  
6053 C CG  . ASN D 169 ? 2.0749 2.0548 1.8797 -0.1404 -0.0455 -0.0553 172 ASN A CG  
6054 O OD1 . ASN D 169 ? 1.9470 1.9296 1.7447 -0.1426 -0.0454 -0.0574 172 ASN A OD1 
6055 N ND2 . ASN D 169 ? 2.2718 2.2493 2.0797 -0.1363 -0.0420 -0.0551 172 ASN A ND2 
6056 N N   . GLN D 170 ? 2.1928 2.1584 2.0088 -0.1387 -0.0464 -0.0670 173 GLN A N   
6057 C CA  . GLN D 170 ? 2.2040 2.1645 2.0252 -0.1356 -0.0443 -0.0692 173 GLN A CA  
6058 C C   . GLN D 170 ? 2.3197 2.2819 2.1412 -0.1316 -0.0401 -0.0645 173 GLN A C   
6059 O O   . GLN D 170 ? 2.1742 2.1332 1.9950 -0.1290 -0.0367 -0.0679 173 GLN A O   
6060 C CB  . GLN D 170 ? 2.1237 2.0797 1.9424 -0.1356 -0.0429 -0.0787 173 GLN A CB  
6061 C CG  . GLN D 170 ? 1.9572 1.9100 1.7780 -0.1389 -0.0472 -0.0844 173 GLN A CG  
6062 C CD  . GLN D 170 ? 2.1017 2.0524 1.9312 -0.1399 -0.0516 -0.0802 173 GLN A CD  
6063 O OE1 . GLN D 170 ? 2.1552 2.1024 1.9917 -0.1379 -0.0512 -0.0792 173 GLN A OE1 
6064 N NE2 . GLN D 170 ? 2.1864 2.1397 2.0158 -0.1433 -0.0559 -0.0774 173 GLN A NE2 
6065 N N   . GLU D 171 ? 2.3131 2.2801 2.1359 -0.1311 -0.0405 -0.0568 174 GLU A N   
6066 C CA  . GLU D 171 ? 2.1097 2.0786 1.9328 -0.1274 -0.0368 -0.0522 174 GLU A CA  
6067 C C   . GLU D 171 ? 2.0452 2.0180 1.8739 -0.1270 -0.0383 -0.0446 174 GLU A C   
6068 O O   . GLU D 171 ? 2.5079 2.4834 2.3383 -0.1299 -0.0419 -0.0419 174 GLU A O   
6069 C CB  . GLU D 171 ? 1.9148 1.8875 1.7310 -0.1268 -0.0346 -0.0517 174 GLU A CB  
6070 C CG  . GLU D 171 ? 2.0123 1.9824 1.8227 -0.1268 -0.0323 -0.0587 174 GLU A CG  
6071 C CD  . GLU D 171 ? 2.0324 2.0070 1.8360 -0.1270 -0.0307 -0.0574 174 GLU A CD  
6072 O OE1 . GLU D 171 ? 1.7724 1.7519 1.5759 -0.1277 -0.0321 -0.0514 174 GLU A OE1 
6073 O OE2 . GLU D 171 ? 2.3936 2.3671 2.1923 -0.1267 -0.0282 -0.0622 174 GLU A OE2 
6074 N N   . ASP D 172 ? 1.7795 1.7527 1.6110 -0.1235 -0.0354 -0.0412 175 ASP A N   
6075 C CA  . ASP D 172 ? 1.8386 1.8164 1.6753 -0.1227 -0.0360 -0.0342 175 ASP A CA  
6076 C C   . ASP D 172 ? 1.9303 1.9143 1.7649 -0.1230 -0.0364 -0.0297 175 ASP A C   
6077 O O   . ASP D 172 ? 2.0198 2.0047 1.8494 -0.1220 -0.0346 -0.0307 175 ASP A O   
6078 C CB  . ASP D 172 ? 1.6842 1.6610 1.5235 -0.1188 -0.0325 -0.0323 175 ASP A CB  
6079 C CG  . ASP D 172 ? 1.8594 1.8310 1.7029 -0.1189 -0.0329 -0.0347 175 ASP A CG  
6080 O OD1 . ASP D 172 ? 1.9430 1.9124 1.7889 -0.1219 -0.0364 -0.0368 175 ASP A OD1 
6081 O OD2 . ASP D 172 ? 1.8695 1.8392 1.7142 -0.1160 -0.0301 -0.0344 175 ASP A OD2 
6082 N N   . LEU D 173 ? 1.7162 1.7047 1.5554 -0.1245 -0.0390 -0.0245 176 LEU A N   
6083 C CA  . LEU D 173 ? 1.6522 1.6470 1.4912 -0.1251 -0.0401 -0.0196 176 LEU A CA  
6084 C C   . LEU D 173 ? 1.6822 1.6819 1.5276 -0.1227 -0.0389 -0.0134 176 LEU A C   
6085 O O   . LEU D 173 ? 1.7731 1.7716 1.6221 -0.1209 -0.0373 -0.0130 176 LEU A O   
6086 C CB  . LEU D 173 ? 1.7005 1.6964 1.5389 -0.1299 -0.0447 -0.0196 176 LEU A CB  
6087 C CG  . LEU D 173 ? 1.8649 1.8664 1.7023 -0.1322 -0.0473 -0.0154 176 LEU A CG  
6088 C CD1 . LEU D 173 ? 1.8653 1.8684 1.6974 -0.1311 -0.0454 -0.0156 176 LEU A CD1 
6089 C CD2 . LEU D 173 ? 1.8718 1.8714 1.7068 -0.1370 -0.0516 -0.0182 176 LEU A CD2 
6090 N N   . LEU D 174 ? 1.8529 1.8588 1.7000 -0.1228 -0.0398 -0.0085 177 LEU A N   
6091 C CA  . LEU D 174 ? 1.7018 1.7133 1.5549 -0.1200 -0.0381 -0.0031 177 LEU A CA  
6092 C C   . LEU D 174 ? 1.7928 1.8109 1.6500 -0.1223 -0.0413 0.0024  177 LEU A C   
6093 O O   . LEU D 174 ? 1.8882 1.9106 1.7462 -0.1211 -0.0409 0.0055  177 LEU A O   
6094 C CB  . LEU D 174 ? 1.4280 1.4402 1.2797 -0.1157 -0.0343 -0.0030 177 LEU A CB  
6095 C CG  . LEU D 174 ? 1.5165 1.5231 1.3651 -0.1127 -0.0307 -0.0072 177 LEU A CG  
6096 C CD1 . LEU D 174 ? 1.5311 1.5390 1.3785 -0.1089 -0.0278 -0.0065 177 LEU A CD1 
6097 C CD2 . LEU D 174 ? 1.5670 1.5732 1.4198 -0.1114 -0.0293 -0.0065 177 LEU A CD2 
6098 N N   . VAL D 175 ? 1.2673 1.2861 1.1276 -0.1257 -0.0447 0.0038  178 VAL A N   
6099 C CA  . VAL D 175 ? 1.5359 1.5612 1.4010 -0.1278 -0.0477 0.0095  178 VAL A CA  
6100 C C   . VAL D 175 ? 1.4162 1.4484 1.2878 -0.1243 -0.0451 0.0146  178 VAL A C   
6101 O O   . VAL D 175 ? 1.3838 1.4168 1.2587 -0.1223 -0.0428 0.0151  178 VAL A O   
6102 C CB  . VAL D 175 ? 1.7465 1.7710 1.6141 -0.1321 -0.0521 0.0103  178 VAL A CB  
6103 C CG1 . VAL D 175 ? 1.6517 1.6840 1.5265 -0.1332 -0.0541 0.0172  178 VAL A CG1 
6104 C CG2 . VAL D 175 ? 1.9683 1.9891 1.8303 -0.1360 -0.0557 0.0069  178 VAL A CG2 
6105 N N   . LEU D 176 ? 1.8056 1.8431 1.6795 -0.1238 -0.0456 0.0184  179 LEU A N   
6106 C CA  . LEU D 176 ? 1.5312 1.5760 1.4119 -0.1205 -0.0434 0.0230  179 LEU A CA  
6107 C C   . LEU D 176 ? 1.4381 1.4895 1.3247 -0.1234 -0.0470 0.0286  179 LEU A C   
6108 O O   . LEU D 176 ? 1.6451 1.6968 1.5302 -0.1260 -0.0502 0.0298  179 LEU A O   
6109 C CB  . LEU D 176 ? 1.6972 1.7425 1.5765 -0.1171 -0.0410 0.0224  179 LEU A CB  
6110 C CG  . LEU D 176 ? 1.7106 1.7501 1.5845 -0.1138 -0.0373 0.0175  179 LEU A CG  
6111 C CD1 . LEU D 176 ? 1.5237 1.5640 1.3967 -0.1113 -0.0363 0.0178  179 LEU A CD1 
6112 C CD2 . LEU D 176 ? 1.5000 1.5405 1.3770 -0.1104 -0.0336 0.0171  179 LEU A CD2 
6113 N N   . TRP D 177 ? 1.2464 1.3031 1.1396 -0.1233 -0.0468 0.0322  180 TRP A N   
6114 C CA  . TRP D 177 ? 1.3316 1.3955 1.2316 -0.1255 -0.0498 0.0382  180 TRP A CA  
6115 C C   . TRP D 177 ? 1.4237 1.4962 1.3316 -0.1216 -0.0464 0.0420  180 TRP A C   
6116 O O   . TRP D 177 ? 1.5796 1.6521 1.4872 -0.1173 -0.0419 0.0398  180 TRP A O   
6117 C CB  . TRP D 177 ? 1.3936 1.4570 1.2950 -0.1301 -0.0538 0.0397  180 TRP A CB  
6118 C CG  . TRP D 177 ? 1.5729 1.6397 1.4792 -0.1295 -0.0522 0.0416  180 TRP A CG  
6119 C CD1 . TRP D 177 ? 1.6570 1.7325 1.5714 -0.1300 -0.0527 0.0475  180 TRP A CD1 
6120 C CD2 . TRP D 177 ? 1.5836 1.6457 1.4872 -0.1286 -0.0501 0.0379  180 TRP A CD2 
6121 N NE1 . TRP D 177 ? 1.6555 1.7323 1.5720 -0.1297 -0.0510 0.0478  180 TRP A NE1 
6122 C CE2 . TRP D 177 ? 1.5939 1.6623 1.5039 -0.1289 -0.0495 0.0421  180 TRP A CE2 
6123 C CE3 . TRP D 177 ? 1.5527 1.6060 1.4493 -0.1277 -0.0486 0.0318  180 TRP A CE3 
6124 C CZ2 . TRP D 177 ? 1.7823 1.8485 1.6919 -0.1285 -0.0479 0.0405  180 TRP A CZ2 
6125 C CZ3 . TRP D 177 ? 1.4444 1.4953 1.3411 -0.1271 -0.0469 0.0301  180 TRP A CZ3 
6126 C CH2 . TRP D 177 ? 1.8343 1.8914 1.7373 -0.1276 -0.0467 0.0345  180 TRP A CH2 
6127 N N   . GLY D 178 ? 1.3575 1.4375 1.2726 -0.1232 -0.0486 0.0477  181 GLY A N   
6128 C CA  . GLY D 178 ? 1.5167 1.6060 1.4403 -0.1196 -0.0455 0.0513  181 GLY A CA  
6129 C C   . GLY D 178 ? 1.3423 1.4394 1.2736 -0.1225 -0.0483 0.0574  181 GLY A C   
6130 O O   . GLY D 178 ? 1.2692 1.3646 1.1997 -0.1272 -0.0532 0.0594  181 GLY A O   
6131 N N   . ILE D 179 ? 1.3568 1.4627 1.2954 -0.1196 -0.0449 0.0601  182 ILE A N   
6132 C CA  . ILE D 179 ? 1.3531 1.4684 1.3004 -0.1217 -0.0466 0.0663  182 ILE A CA  
6133 C C   . ILE D 179 ? 1.6568 1.7806 1.6123 -0.1182 -0.0447 0.0694  182 ILE A C   
6134 O O   . ILE D 179 ? 1.6091 1.7355 1.5662 -0.1132 -0.0398 0.0670  182 ILE A O   
6135 C CB  . ILE D 179 ? 1.6711 1.7909 1.6206 -0.1217 -0.0441 0.0673  182 ILE A CB  
6136 C CG1 . ILE D 179 ? 1.6479 1.7588 1.5902 -0.1249 -0.0463 0.0643  182 ILE A CG1 
6137 C CG2 . ILE D 179 ? 1.8592 1.9897 1.8180 -0.1238 -0.0458 0.0742  182 ILE A CG2 
6138 C CD1 . ILE D 179 ? 1.7168 1.8320 1.6615 -0.1254 -0.0444 0.0658  182 ILE A CD1 
6139 N N   . HIS D 180 ? 1.6417 1.7700 1.6030 -0.1209 -0.0487 0.0745  183 HIS A N   
6140 C CA  . HIS D 180 ? 1.7139 1.8517 1.6852 -0.1179 -0.0471 0.0781  183 HIS A CA  
6141 C C   . HIS D 180 ? 1.8902 2.0390 1.8697 -0.1169 -0.0444 0.0817  183 HIS A C   
6142 O O   . HIS D 180 ? 1.9353 2.0860 1.9153 -0.1208 -0.0466 0.0846  183 HIS A O   
6143 C CB  . HIS D 180 ? 1.5950 1.7337 1.5700 -0.1212 -0.0526 0.0827  183 HIS A CB  
6144 C CG  . HIS D 180 ? 1.6203 1.7699 1.6076 -0.1189 -0.0518 0.0876  183 HIS A CG  
6145 N ND1 . HIS D 180 ? 1.2345 1.3872 1.2267 -0.1136 -0.0483 0.0860  183 HIS A ND1 
6146 C CD2 . HIS D 180 ? 1.9581 2.1166 1.9545 -0.1211 -0.0540 0.0939  183 HIS A CD2 
6147 C CE1 . HIS D 180 ? 1.6190 1.7819 1.6230 -0.1124 -0.0483 0.0909  183 HIS A CE1 
6148 N NE2 . HIS D 180 ? 2.0569 2.2237 2.0636 -0.1170 -0.0516 0.0959  183 HIS A NE2 
6149 N N   . HIS D 181 ? 2.1607 2.3170 2.1468 -0.1117 -0.0395 0.0812  184 HIS A N   
6150 C CA  . HIS D 181 ? 1.9663 2.1347 1.9607 -0.1102 -0.0361 0.0843  184 HIS A CA  
6151 C C   . HIS D 181 ? 1.8534 2.0315 1.8596 -0.1078 -0.0358 0.0881  184 HIS A C   
6152 O O   . HIS D 181 ? 1.7447 1.9245 1.7544 -0.1026 -0.0324 0.0853  184 HIS A O   
6153 C CB  . HIS D 181 ? 1.9520 2.1216 1.9436 -0.1058 -0.0298 0.0795  184 HIS A CB  
6154 C CG  . HIS D 181 ? 1.9409 2.0996 1.9210 -0.1072 -0.0298 0.0749  184 HIS A CG  
6155 N ND1 . HIS D 181 ? 1.8826 2.0386 1.8588 -0.1121 -0.0327 0.0765  184 HIS A ND1 
6156 C CD2 . HIS D 181 ? 2.1384 2.2884 2.1109 -0.1044 -0.0276 0.0689  184 HIS A CD2 
6157 C CE1 . HIS D 181 ? 2.0342 2.1804 2.0011 -0.1121 -0.0320 0.0714  184 HIS A CE1 
6158 N NE2 . HIS D 181 ? 2.1522 2.2947 2.1164 -0.1075 -0.0289 0.0669  184 HIS A NE2 
6159 N N   . PRO D 182 ? 1.6382 1.8227 1.6515 -0.1115 -0.0395 0.0946  185 PRO A N   
6160 C CA  . PRO D 182 ? 1.8555 2.0496 1.8811 -0.1093 -0.0394 0.0985  185 PRO A CA  
6161 C C   . PRO D 182 ? 2.3993 2.6064 2.4338 -0.1050 -0.0334 0.0988  185 PRO A C   
6162 O O   . PRO D 182 ? 2.5618 2.7691 2.5917 -0.1025 -0.0285 0.0946  185 PRO A O   
6163 C CB  . PRO D 182 ? 1.8765 2.0724 1.9056 -0.1153 -0.0458 0.1054  185 PRO A CB  
6164 C CG  . PRO D 182 ? 1.8940 2.0869 1.9163 -0.1196 -0.0471 0.1058  185 PRO A CG  
6165 C CD  . PRO D 182 ? 1.7411 1.9248 1.7523 -0.1177 -0.0441 0.0986  185 PRO A CD  
6166 N N   . ASN D 183 ? 2.0696 2.2877 2.1166 -0.1043 -0.0336 0.1037  186 ASN A N   
6167 C CA  . ASN D 183 ? 2.3954 2.6270 2.4515 -0.1000 -0.0275 0.1037  186 ASN A CA  
6168 C C   . ASN D 183 ? 2.4335 2.6771 2.4986 -0.1033 -0.0289 0.1110  186 ASN A C   
6169 O O   . ASN D 183 ? 2.5877 2.8397 2.6537 -0.1036 -0.0254 0.1119  186 ASN A O   
6170 C CB  . ASN D 183 ? 2.4276 2.6629 2.4926 -0.0939 -0.0248 0.1014  186 ASN A CB  
6171 C CG  . ASN D 183 ? 2.4037 2.6293 2.4612 -0.0898 -0.0224 0.0941  186 ASN A CG  
6172 O OD1 . ASN D 183 ? 2.5038 2.7224 2.5502 -0.0903 -0.0208 0.0900  186 ASN A OD1 
6173 N ND2 . ASN D 183 ? 2.3506 2.5762 2.4149 -0.0856 -0.0222 0.0926  186 ASN A ND2 
6174 N N   . ASP D 184 ? 2.6669 2.9119 2.7390 -0.1059 -0.0340 0.1166  187 ASP A N   
6175 C CA  . ASP D 184 ? 2.5330 2.7885 2.6143 -0.1096 -0.0365 0.1243  187 ASP A CA  
6176 C C   . ASP D 184 ? 2.2186 2.4661 2.2966 -0.1160 -0.0447 0.1290  187 ASP A C   
6177 O O   . ASP D 184 ? 2.1706 2.4051 2.2392 -0.1175 -0.0480 0.1260  187 ASP A O   
6178 C CB  . ASP D 184 ? 2.5268 2.7955 2.6236 -0.1055 -0.0338 0.1269  187 ASP A CB  
6179 C CG  . ASP D 184 ? 2.4879 2.7678 2.5893 -0.1000 -0.0256 0.1231  187 ASP A CG  
6180 O OD1 . ASP D 184 ? 2.5530 2.8325 2.6462 -0.1005 -0.0224 0.1204  187 ASP A OD1 
6181 O OD2 . ASP D 184 ? 2.4553 2.7445 2.5686 -0.0952 -0.0224 0.1228  187 ASP A OD2 
6182 N N   . ALA D 185 ? 2.1276 2.3833 2.2135 -0.1200 -0.0480 0.1365  188 ALA A N   
6183 C CA  . ALA D 185 ? 1.9512 2.2000 2.0343 -0.1265 -0.0560 0.1413  188 ALA A CA  
6184 C C   . ALA D 185 ? 2.1024 2.3450 2.1869 -0.1262 -0.0599 0.1414  188 ALA A C   
6185 O O   . ALA D 185 ? 2.1859 2.4176 2.2623 -0.1305 -0.0656 0.1415  188 ALA A O   
6186 C CB  . ALA D 185 ? 1.8521 2.1122 1.9450 -0.1304 -0.0587 0.1497  188 ALA A CB  
6187 N N   . ALA D 186 ? 1.9589 2.2085 2.0540 -0.1212 -0.0569 0.1414  189 ALA A N   
6188 C CA  . ALA D 186 ? 2.0256 2.2699 2.1232 -0.1210 -0.0608 0.1421  189 ALA A CA  
6189 C C   . ALA D 186 ? 2.0304 2.2604 2.1146 -0.1206 -0.0615 0.1355  189 ALA A C   
6190 O O   . ALA D 186 ? 2.1294 2.3503 2.2075 -0.1249 -0.0674 0.1366  189 ALA A O   
6191 C CB  . ALA D 186 ? 2.0692 2.3235 2.1812 -0.1151 -0.0570 0.1424  189 ALA A CB  
6192 N N   . GLU D 187 ? 2.1414 2.3696 2.2208 -0.1157 -0.0554 0.1287  190 GLU A N   
6193 C CA  . GLU D 187 ? 2.2210 2.4364 2.2887 -0.1149 -0.0557 0.1226  190 GLU A CA  
6194 C C   . GLU D 187 ? 2.1728 2.3778 2.2267 -0.1204 -0.0594 0.1215  190 GLU A C   
6195 O O   . GLU D 187 ? 2.1601 2.3544 2.2052 -0.1225 -0.0628 0.1191  190 GLU A O   
6196 C CB  . GLU D 187 ? 2.4225 2.6382 2.4880 -0.1085 -0.0485 0.1156  190 GLU A CB  
6197 C CG  . GLU D 187 ? 2.4248 2.6491 2.5027 -0.1022 -0.0445 0.1148  190 GLU A CG  
6198 C CD  . GLU D 187 ? 2.6836 2.9070 2.7573 -0.0966 -0.0377 0.1075  190 GLU A CD  
6199 O OE1 . GLU D 187 ? 2.6182 2.8355 2.6801 -0.0982 -0.0365 0.1042  190 GLU A OE1 
6200 O OE2 . GLU D 187 ? 2.7637 2.9932 2.8464 -0.0908 -0.0338 0.1052  190 GLU A OE2 
6201 N N   . GLN D 188 ? 2.1767 2.3850 2.2290 -0.1228 -0.0587 0.1229  191 GLN A N   
6202 C CA  . GLN D 188 ? 1.9705 2.1697 2.0119 -0.1286 -0.0631 0.1226  191 GLN A CA  
6203 C C   . GLN D 188 ? 1.9396 2.1347 1.9812 -0.1336 -0.0705 0.1270  191 GLN A C   
6204 O O   . GLN D 188 ? 2.1406 2.3255 2.1737 -0.1351 -0.0732 0.1238  191 GLN A O   
6205 C CB  . GLN D 188 ? 1.8899 2.0948 1.9326 -0.1312 -0.0628 0.1256  191 GLN A CB  
6206 C CG  . GLN D 188 ? 1.7536 1.9484 1.7838 -0.1342 -0.0639 0.1216  191 GLN A CG  
6207 C CD  . GLN D 188 ? 1.9818 2.1832 2.0136 -0.1346 -0.0611 0.1229  191 GLN A CD  
6208 O OE1 . GLN D 188 ? 2.3023 2.5162 2.3442 -0.1336 -0.0589 0.1274  191 GLN A OE1 
6209 N NE2 . GLN D 188 ? 1.6520 1.8454 1.6741 -0.1364 -0.0613 0.1190  191 GLN A NE2 
6210 N N   . THR D 189 ? 1.8921 2.0956 1.9436 -0.1364 -0.0737 0.1343  192 THR A N   
6211 C CA  . THR D 189 ? 1.9497 2.1504 2.0023 -0.1417 -0.0811 0.1393  192 THR A CA  
6212 C C   . THR D 189 ? 1.9768 2.1699 2.0254 -0.1415 -0.0834 0.1371  192 THR A C   
6213 O O   . THR D 189 ? 1.5370 1.7221 1.5782 -0.1466 -0.0893 0.1376  192 THR A O   
6214 C CB  . THR D 189 ? 1.9150 2.1281 1.9825 -0.1424 -0.0827 0.1474  192 THR A CB  
6215 O OG1 . THR D 189 ? 2.2151 2.4368 2.2931 -0.1361 -0.0774 0.1470  192 THR A OG1 
6216 C CG2 . THR D 189 ? 1.5211 1.7410 1.5917 -0.1450 -0.0827 0.1513  192 THR A CG2 
6217 N N   . LYS D 190 ? 1.7840 1.9799 1.8375 -0.1357 -0.0791 0.1346  193 LYS A N   
6218 C CA  . LYS D 190 ? 1.8299 2.0191 1.8802 -0.1353 -0.0813 0.1328  193 LYS A CA  
6219 C C   . LYS D 190 ? 1.7122 1.8885 1.7465 -0.1386 -0.0836 0.1277  193 LYS A C   
6220 O O   . LYS D 190 ? 1.6686 1.8391 1.6983 -0.1423 -0.0886 0.1287  193 LYS A O   
6221 C CB  . LYS D 190 ? 2.0348 2.2271 2.0906 -0.1280 -0.0755 0.1291  193 LYS A CB  
6222 C CG  . LYS D 190 ? 1.8276 2.0325 1.9003 -0.1243 -0.0734 0.1334  193 LYS A CG  
6223 C CD  . LYS D 190 ? 1.6938 1.9005 1.7710 -0.1170 -0.0678 0.1285  193 LYS A CD  
6224 C CE  . LYS D 190 ? 1.6543 1.8738 1.7491 -0.1129 -0.0655 0.1321  193 LYS A CE  
6225 N NZ  . LYS D 190 ? 1.6105 1.8318 1.7103 -0.1055 -0.0602 0.1268  193 LYS A NZ  
6226 N N   . LEU D 191 ? 2.0484 2.2206 2.0743 -0.1375 -0.0799 0.1224  194 LEU A N   
6227 C CA  . LEU D 191 ? 1.8341 1.9944 1.8453 -0.1395 -0.0809 0.1165  194 LEU A CA  
6228 C C   . LEU D 191 ? 1.6147 1.7709 1.6189 -0.1443 -0.0836 0.1162  194 LEU A C   
6229 O O   . LEU D 191 ? 1.6030 1.7503 1.5972 -0.1486 -0.0876 0.1139  194 LEU A O   
6230 C CB  . LEU D 191 ? 1.9238 2.0814 1.9308 -0.1336 -0.0742 0.1097  194 LEU A CB  
6231 C CG  . LEU D 191 ? 2.1570 2.3178 2.1709 -0.1287 -0.0721 0.1095  194 LEU A CG  
6232 C CD1 . LEU D 191 ? 2.3493 2.5081 2.3601 -0.1226 -0.0655 0.1030  194 LEU A CD1 
6233 C CD2 . LEU D 191 ? 1.8017 1.9584 1.8144 -0.1318 -0.0775 0.1117  194 LEU A CD2 
6234 N N   . TYR D 192 ? 1.8720 2.0347 1.8816 -0.1436 -0.0814 0.1182  195 TYR A N   
6235 C CA  . TYR D 192 ? 1.7888 1.9494 1.7945 -0.1477 -0.0837 0.1188  195 TYR A CA  
6236 C C   . TYR D 192 ? 2.2178 2.3902 2.2359 -0.1487 -0.0844 0.1263  195 TYR A C   
6237 O O   . TYR D 192 ? 2.4915 2.6718 2.5153 -0.1452 -0.0794 0.1267  195 TYR A O   
6238 C CB  . TYR D 192 ? 1.8618 2.0185 1.8607 -0.1450 -0.0788 0.1127  195 TYR A CB  
6239 C CG  . TYR D 192 ? 1.8716 2.0173 1.8589 -0.1437 -0.0775 0.1053  195 TYR A CG  
6240 C CD1 . TYR D 192 ? 2.0563 2.1919 2.0335 -0.1482 -0.0817 0.1022  195 TYR A CD1 
6241 C CD2 . TYR D 192 ? 1.7438 1.8897 1.7308 -0.1380 -0.0720 0.1012  195 TYR A CD2 
6242 C CE1 . TYR D 192 ? 2.0641 2.1905 2.0310 -0.1470 -0.0803 0.0954  195 TYR A CE1 
6243 C CE2 . TYR D 192 ? 1.9967 2.1330 1.9734 -0.1369 -0.0709 0.0949  195 TYR A CE2 
6244 C CZ  . TYR D 192 ? 2.1009 2.2278 2.0677 -0.1414 -0.0749 0.0921  195 TYR A CZ  
6245 O OH  . TYR D 192 ? 2.0680 2.1860 2.0248 -0.1404 -0.0736 0.0857  195 TYR A OH  
6246 N N   . GLN D 193 ? 1.8776 2.0515 1.8997 -0.1535 -0.0907 0.1322  196 GLN A N   
6247 C CA  . GLN D 193 ? 1.9918 2.1762 2.0250 -0.1554 -0.0924 0.1398  196 GLN A CA  
6248 C C   . GLN D 193 ? 1.8937 2.0806 1.9263 -0.1560 -0.0905 0.1397  196 GLN A C   
6249 O O   . GLN D 193 ? 1.9508 2.1491 1.9932 -0.1544 -0.0876 0.1439  196 GLN A O   
6250 C CB  . GLN D 193 ? 1.8840 2.0665 1.9182 -0.1619 -0.1006 0.1454  196 GLN A CB  
6251 C CG  . GLN D 193 ? 1.8719 2.0547 1.9097 -0.1622 -0.1033 0.1479  196 GLN A CG  
6252 C CD  . GLN D 193 ? 1.9121 2.0925 1.9498 -0.1692 -0.1117 0.1533  196 GLN A CD  
6253 O OE1 . GLN D 193 ? 1.8203 1.9948 1.8512 -0.1739 -0.1158 0.1526  196 GLN A OE1 
6254 N NE2 . GLN D 193 ? 1.9778 2.1630 2.0236 -0.1699 -0.1145 0.1588  196 GLN A NE2 
6255 N N   . ASN D 194 ? 2.0819 2.2587 2.1037 -0.1586 -0.0922 0.1351  197 ASN A N   
6256 C CA  . ASN D 194 ? 1.9837 2.1618 2.0047 -0.1596 -0.0911 0.1349  197 ASN A CA  
6257 C C   . ASN D 194 ? 2.0312 2.2182 2.0570 -0.1539 -0.0833 0.1338  197 ASN A C   
6258 O O   . ASN D 194 ? 2.1469 2.3300 2.1673 -0.1494 -0.0782 0.1276  197 ASN A O   
6259 C CB  . ASN D 194 ? 2.1001 2.2651 2.1086 -0.1616 -0.0928 0.1284  197 ASN A CB  
6260 C CG  . ASN D 194 ? 1.8691 2.0263 1.8733 -0.1679 -0.1008 0.1295  197 ASN A CG  
6261 O OD1 . ASN D 194 ? 1.2981 1.4602 1.3090 -0.1716 -0.1057 0.1362  197 ASN A OD1 
6262 N ND2 . ASN D 194 ? 2.1575 2.3027 2.1504 -0.1691 -0.1023 0.1227  197 ASN A ND2 
6263 N N   . PRO D 195 ? 1.9635 2.1626 1.9991 -0.1542 -0.0821 0.1398  198 PRO A N   
6264 C CA  . PRO D 195 ? 2.1185 2.3273 2.1589 -0.1489 -0.0744 0.1387  198 PRO A CA  
6265 C C   . PRO D 195 ? 2.0153 2.2211 2.0489 -0.1484 -0.0713 0.1346  198 PRO A C   
6266 O O   . PRO D 195 ? 1.9842 2.1945 2.0181 -0.1435 -0.0646 0.1312  198 PRO A O   
6267 C CB  . PRO D 195 ? 1.9079 2.1314 1.9613 -0.1502 -0.0749 0.1471  198 PRO A CB  
6268 C CG  . PRO D 195 ? 1.6605 1.8802 1.7132 -0.1572 -0.0828 0.1520  198 PRO A CG  
6269 C CD  . PRO D 195 ? 1.5548 1.7599 1.5978 -0.1594 -0.0877 0.1479  198 PRO A CD  
6270 N N   . THR D 196 ? 1.7898 1.9882 1.8178 -0.1534 -0.0762 0.1347  199 THR A N   
6271 C CA  . THR D 196 ? 1.8491 2.0442 1.8713 -0.1535 -0.0741 0.1314  199 THR A CA  
6272 C C   . THR D 196 ? 1.9650 2.1446 1.9766 -0.1564 -0.0786 0.1262  199 THR A C   
6273 O O   . THR D 196 ? 2.1320 2.3070 2.1432 -0.1616 -0.0854 0.1289  199 THR A O   
6274 C CB  . THR D 196 ? 1.9223 2.1269 1.9513 -0.1571 -0.0757 0.1381  199 THR A CB  
6275 O OG1 . THR D 196 ? 2.0716 2.2737 2.1029 -0.1631 -0.0836 0.1433  199 THR A OG1 
6276 C CG2 . THR D 196 ? 2.1139 2.3349 2.1534 -0.1541 -0.0706 0.1427  199 THR A CG2 
6277 N N   . THR D 197 ? 1.6819 1.8534 1.6850 -0.1529 -0.0747 0.1187  200 THR A N   
6278 C CA  . THR D 197 ? 1.7832 1.9403 1.7762 -0.1550 -0.0782 0.1130  200 THR A CA  
6279 C C   . THR D 197 ? 1.7249 1.8763 1.7116 -0.1539 -0.0755 0.1079  200 THR A C   
6280 O O   . THR D 197 ? 1.8112 1.9699 1.8015 -0.1527 -0.0719 0.1097  200 THR A O   
6281 C CB  . THR D 197 ? 1.9361 2.0874 1.9243 -0.1522 -0.0772 0.1087  200 THR A CB  
6282 O OG1 . THR D 197 ? 1.7276 1.8817 1.7153 -0.1462 -0.0701 0.1050  200 THR A OG1 
6283 C CG2 . THR D 197 ? 1.9751 2.1326 1.9704 -0.1535 -0.0801 0.1143  200 THR A CG2 
6284 N N   . TYR D 198 ? 1.6733 1.8120 1.6508 -0.1545 -0.0771 0.1015  201 TYR A N   
6285 C CA  . TYR D 198 ? 1.6569 1.7889 1.6283 -0.1533 -0.0747 0.0961  201 TYR A CA  
6286 C C   . TYR D 198 ? 1.7325 1.8527 1.6943 -0.1517 -0.0742 0.0884  201 TYR A C   
6287 O O   . TYR D 198 ? 1.7337 1.8503 1.6932 -0.1528 -0.0771 0.0877  201 TYR A O   
6288 C CB  . TYR D 198 ? 1.8576 1.9865 1.8299 -0.1583 -0.0797 0.0979  201 TYR A CB  
6289 C CG  . TYR D 198 ? 1.9311 2.0512 1.9005 -0.1629 -0.0869 0.0970  201 TYR A CG  
6290 C CD1 . TYR D 198 ? 1.8782 2.0026 1.8532 -0.1667 -0.0921 0.1030  201 TYR A CD1 
6291 C CD2 . TYR D 198 ? 1.9709 2.0783 1.9319 -0.1636 -0.0885 0.0898  201 TYR A CD2 
6292 C CE1 . TYR D 198 ? 1.8834 1.9997 1.8554 -0.1710 -0.0988 0.1018  201 TYR A CE1 
6293 C CE2 . TYR D 198 ? 2.2025 2.3022 2.1607 -0.1677 -0.0949 0.0883  201 TYR A CE2 
6294 C CZ  . TYR D 198 ? 2.2017 2.3057 2.1650 -0.1715 -0.1001 0.0942  201 TYR A CZ  
6295 O OH  . TYR D 198 ? 2.2617 2.3579 2.2218 -0.1758 -0.1066 0.0924  201 TYR A OH  
6296 N N   . ILE D 199 ? 1.8932 2.0076 1.8493 -0.1494 -0.0708 0.0829  202 ILE A N   
6297 C CA  . ILE D 199 ? 1.9514 2.0545 1.8982 -0.1481 -0.0703 0.0754  202 ILE A CA  
6298 C C   . ILE D 199 ? 2.1428 2.2381 2.0854 -0.1493 -0.0709 0.0713  202 ILE A C   
6299 O O   . ILE D 199 ? 2.2114 2.3055 2.1514 -0.1460 -0.0662 0.0681  202 ILE A O   
6300 C CB  . ILE D 199 ? 1.8704 1.9749 1.8148 -0.1424 -0.0642 0.0724  202 ILE A CB  
6301 C CG1 . ILE D 199 ? 1.7340 1.8446 1.6830 -0.1420 -0.0652 0.0764  202 ILE A CG1 
6302 C CG2 . ILE D 199 ? 1.8342 1.9275 1.7691 -0.1410 -0.0632 0.0648  202 ILE A CG2 
6303 C CD1 . ILE D 199 ? 1.8921 2.0064 1.8420 -0.1367 -0.0600 0.0751  202 ILE A CD1 
6304 N N   . SER D 200 ? 2.1954 2.2854 2.1378 -0.1541 -0.0769 0.0715  203 SER A N   
6305 C CA  . SER D 200 ? 2.1825 2.2653 2.1229 -0.1557 -0.0785 0.0682  203 SER A CA  
6306 C C   . SER D 200 ? 2.0225 2.0937 1.9539 -0.1546 -0.0780 0.0599  203 SER A C   
6307 O O   . SER D 200 ? 2.0335 2.0985 1.9616 -0.1573 -0.0823 0.0573  203 SER A O   
6308 C CB  . SER D 200 ? 2.3291 2.4119 2.2746 -0.1613 -0.0854 0.0724  203 SER A CB  
6309 O OG  . SER D 200 ? 2.4575 2.5371 2.4019 -0.1643 -0.0904 0.0725  203 SER A OG  
6310 N N   . VAL D 201 ? 1.8089 1.8777 1.7363 -0.1505 -0.0726 0.0557  204 VAL A N   
6311 C CA  . VAL D 201 ? 1.8193 1.8778 1.7386 -0.1491 -0.0715 0.0478  204 VAL A CA  
6312 C C   . VAL D 201 ? 2.0073 2.0586 1.9266 -0.1514 -0.0742 0.0448  204 VAL A C   
6313 O O   . VAL D 201 ? 2.2087 2.2635 2.1337 -0.1530 -0.0754 0.0488  204 VAL A O   
6314 C CB  . VAL D 201 ? 1.8997 1.9590 1.8153 -0.1436 -0.0647 0.0449  204 VAL A CB  
6315 C CG1 . VAL D 201 ? 1.8171 1.8663 1.7245 -0.1422 -0.0634 0.0371  204 VAL A CG1 
6316 C CG2 . VAL D 201 ? 1.9509 2.0180 1.8685 -0.1413 -0.0623 0.0484  204 VAL A CG2 
6317 N N   . GLY D 202 ? 1.9556 1.9970 1.8688 -0.1518 -0.0755 0.0379  205 GLY A N   
6318 C CA  . GLY D 202 ? 2.0750 2.1088 1.9883 -0.1533 -0.0775 0.0340  205 GLY A CA  
6319 C C   . GLY D 202 ? 1.9003 1.9246 1.8060 -0.1516 -0.0759 0.0255  205 GLY A C   
6320 O O   . GLY D 202 ? 1.8378 1.8579 1.7391 -0.1531 -0.0781 0.0217  205 GLY A O   
6321 N N   . THR D 203 ? 2.0459 2.0670 1.9500 -0.1488 -0.0720 0.0223  206 THR A N   
6322 C CA  . THR D 203 ? 2.1278 2.1403 2.0252 -0.1470 -0.0701 0.0143  206 THR A CA  
6323 C C   . THR D 203 ? 2.0183 2.0234 1.9179 -0.1484 -0.0723 0.0106  206 THR A C   
6324 O O   . THR D 203 ? 1.8045 1.8089 1.7099 -0.1520 -0.0776 0.0128  206 THR A O   
6325 C CB  . THR D 203 ? 2.1340 2.1479 2.0270 -0.1421 -0.0634 0.0129  206 THR A CB  
6326 O OG1 . THR D 203 ? 1.8464 1.8626 1.7431 -0.1405 -0.0610 0.0155  206 THR A OG1 
6327 C CG2 . THR D 203 ? 2.2133 2.2349 2.1057 -0.1405 -0.0614 0.0170  206 THR A CG2 
6328 N N   . SER D 204 ? 2.0165 2.0161 1.9123 -0.1455 -0.0687 0.0053  207 SER A N   
6329 C CA  . SER D 204 ? 2.0332 2.0260 1.9318 -0.1462 -0.0702 0.0020  207 SER A CA  
6330 C C   . SER D 204 ? 2.0126 2.0098 1.9192 -0.1479 -0.0720 0.0086  207 SER A C   
6331 O O   . SER D 204 ? 2.0292 2.0246 1.9417 -0.1517 -0.0776 0.0101  207 SER A O   
6332 C CB  . SER D 204 ? 1.9570 1.9453 1.8507 -0.1422 -0.0649 -0.0033 207 SER A CB  
6333 O OG  . SER D 204 ? 2.0911 2.0850 1.9843 -0.1391 -0.0601 0.0007  207 SER A OG  
6334 N N   . THR D 205 ? 2.0166 2.0198 1.9233 -0.1454 -0.0675 0.0126  208 THR A N   
6335 C CA  . THR D 205 ? 1.9310 1.9410 1.8444 -0.1471 -0.0687 0.0199  208 THR A CA  
6336 C C   . THR D 205 ? 1.8580 1.8789 1.7718 -0.1457 -0.0656 0.0259  208 THR A C   
6337 O O   . THR D 205 ? 1.9542 1.9824 1.8739 -0.1479 -0.0672 0.0325  208 THR A O   
6338 C CB  . THR D 205 ? 1.9930 2.0008 1.9076 -0.1459 -0.0664 0.0196  208 THR A CB  
6339 O OG1 . THR D 205 ? 1.6530 1.6610 1.5614 -0.1412 -0.0600 0.0168  208 THR A OG1 
6340 C CG2 . THR D 205 ? 1.9484 1.9460 1.8649 -0.1477 -0.0701 0.0144  208 THR A CG2 
6341 N N   . LEU D 206 ? 1.7414 1.7638 1.6496 -0.1422 -0.0614 0.0238  209 LEU A N   
6342 C CA  . LEU D 206 ? 1.8101 1.8426 1.7193 -0.1406 -0.0586 0.0289  209 LEU A CA  
6343 C C   . LEU D 206 ? 2.0429 2.0793 1.9557 -0.1440 -0.0633 0.0328  209 LEU A C   
6344 O O   . LEU D 206 ? 2.1511 2.1870 2.0608 -0.1437 -0.0638 0.0314  209 LEU A O   
6345 C CB  . LEU D 206 ? 1.8332 1.8653 1.7362 -0.1360 -0.0534 0.0255  209 LEU A CB  
6346 C CG  . LEU D 206 ? 2.0534 2.0823 1.9524 -0.1320 -0.0483 0.0218  209 LEU A CG  
6347 C CD1 . LEU D 206 ? 1.7851 1.8130 1.6783 -0.1282 -0.0447 0.0186  209 LEU A CD1 
6348 C CD2 . LEU D 206 ? 2.0111 2.0473 1.9136 -0.1308 -0.0453 0.0264  209 LEU A CD2 
6349 N N   . ASN D 207 ? 2.0338 2.0739 1.9534 -0.1477 -0.0673 0.0381  210 ASN A N   
6350 C CA  . ASN D 207 ? 2.2413 2.2863 2.1655 -0.1513 -0.0720 0.0430  210 ASN A CA  
6351 C C   . ASN D 207 ? 2.1808 2.2381 2.1089 -0.1500 -0.0690 0.0498  210 ASN A C   
6352 O O   . ASN D 207 ? 1.9201 1.9847 1.8546 -0.1523 -0.0705 0.0560  210 ASN A O   
6353 C CB  . ASN D 207 ? 2.2609 2.3031 2.1909 -0.1562 -0.0785 0.0451  210 ASN A CB  
6354 C CG  . ASN D 207 ? 2.0925 2.1228 2.0196 -0.1577 -0.0822 0.0381  210 ASN A CG  
6355 O OD1 . ASN D 207 ? 2.1104 2.1357 2.0311 -0.1560 -0.0809 0.0324  210 ASN A OD1 
6356 N ND2 . ASN D 207 ? 1.9788 2.0048 1.9109 -0.1609 -0.0869 0.0384  210 ASN A ND2 
6357 N N   . GLN D 208 ? 2.1642 2.2242 2.0887 -0.1462 -0.0646 0.0484  211 GLN A N   
6358 C CA  . GLN D 208 ? 2.0812 2.1519 2.0085 -0.1434 -0.0600 0.0528  211 GLN A CA  
6359 C C   . GLN D 208 ? 2.1481 2.2267 2.0806 -0.1454 -0.0628 0.0586  211 GLN A C   
6360 O O   . GLN D 208 ? 2.6901 2.7699 2.6212 -0.1438 -0.0620 0.0581  211 GLN A O   
6361 C CB  . GLN D 208 ? 2.0182 2.0873 1.9398 -0.1381 -0.0543 0.0482  211 GLN A CB  
6362 C CG  . GLN D 208 ? 1.8668 1.9461 1.7913 -0.1345 -0.0490 0.0514  211 GLN A CG  
6363 C CD  . GLN D 208 ? 1.9082 1.9848 1.8273 -0.1292 -0.0438 0.0466  211 GLN A CD  
6364 O OE1 . GLN D 208 ? 1.8809 1.9481 1.7939 -0.1284 -0.0438 0.0411  211 GLN A OE1 
6365 N NE2 . GLN D 208 ? 2.2506 2.3357 2.1724 -0.1257 -0.0392 0.0485  211 GLN A NE2 
6366 N N   . ARG D 209 ? 2.1385 2.2228 2.0777 -0.1492 -0.0663 0.0646  212 ARG A N   
6367 C CA  . ARG D 209 ? 2.2331 2.3255 2.1782 -0.1515 -0.0692 0.0708  212 ARG A CA  
6368 C C   . ARG D 209 ? 2.1384 2.2427 2.0871 -0.1479 -0.0637 0.0744  212 ARG A C   
6369 O O   . ARG D 209 ? 1.7611 1.8740 1.7144 -0.1481 -0.0618 0.0787  212 ARG A O   
6370 C CB  . ARG D 209 ? 2.4087 2.5034 2.3602 -0.1569 -0.0751 0.0762  212 ARG A CB  
6371 C CG  . ARG D 209 ? 2.3850 2.4682 2.3344 -0.1606 -0.0814 0.0726  212 ARG A CG  
6372 C CD  . ARG D 209 ? 2.3372 2.4231 2.2940 -0.1661 -0.0879 0.0786  212 ARG A CD  
6373 N NE  . ARG D 209 ? 2.1457 2.2202 2.1011 -0.1694 -0.0939 0.0746  212 ARG A NE  
6374 C CZ  . ARG D 209 ? 2.1761 2.2499 2.1375 -0.1743 -0.1005 0.0784  212 ARG A CZ  
6375 N NH1 . ARG D 209 ? 2.2710 2.3550 2.2401 -0.1769 -0.1021 0.0868  212 ARG A NH1 
6376 N NH2 . ARG D 209 ? 2.0550 2.1177 2.0150 -0.1767 -0.1057 0.0735  212 ARG A NH2 
6377 N N   . LEU D 210 ? 2.0488 2.1539 1.9956 -0.1448 -0.0614 0.0728  213 LEU A N   
6378 C CA  . LEU D 210 ? 1.9772 2.0920 1.9272 -0.1406 -0.0560 0.0747  213 LEU A CA  
6379 C C   . LEU D 210 ? 1.9374 2.0619 1.8950 -0.1421 -0.0580 0.0812  213 LEU A C   
6380 O O   . LEU D 210 ? 2.2460 2.3692 2.2058 -0.1464 -0.0638 0.0842  213 LEU A O   
6381 C CB  . LEU D 210 ? 2.0270 2.1364 1.9710 -0.1359 -0.0522 0.0689  213 LEU A CB  
6382 C CG  . LEU D 210 ? 2.2037 2.3051 2.1409 -0.1337 -0.0491 0.0628  213 LEU A CG  
6383 C CD1 . LEU D 210 ? 2.0518 2.1474 1.9831 -0.1298 -0.0464 0.0574  213 LEU A CD1 
6384 C CD2 . LEU D 210 ? 2.1201 2.2289 2.0598 -0.1316 -0.0445 0.0643  213 LEU A CD2 
6385 N N   . VAL D 211 ? 1.8581 1.9926 1.8201 -0.1383 -0.0532 0.0832  214 VAL A N   
6386 C CA  . VAL D 211 ? 1.7334 1.8790 1.7040 -0.1388 -0.0539 0.0895  214 VAL A CA  
6387 C C   . VAL D 211 ? 1.7615 1.9115 1.7335 -0.1332 -0.0487 0.0876  214 VAL A C   
6388 O O   . VAL D 211 ? 2.0006 2.1489 1.9688 -0.1290 -0.0436 0.0829  214 VAL A O   
6389 C CB  . VAL D 211 ? 1.6259 1.7829 1.6035 -0.1409 -0.0534 0.0955  214 VAL A CB  
6390 C CG1 . VAL D 211 ? 1.1628 1.3326 1.1500 -0.1408 -0.0532 0.1019  214 VAL A CG1 
6391 C CG2 . VAL D 211 ? 1.9216 2.0742 1.8989 -0.1467 -0.0593 0.0979  214 VAL A CG2 
6392 N N   . PRO D 212 ? 1.6462 1.8012 1.6238 -0.1329 -0.0501 0.0910  215 PRO A N   
6393 C CA  . PRO D 212 ? 1.8753 2.0354 1.8561 -0.1274 -0.0453 0.0895  215 PRO A CA  
6394 C C   . PRO D 212 ? 1.7368 1.9110 1.7259 -0.1248 -0.0405 0.0927  215 PRO A C   
6395 O O   . PRO D 212 ? 1.5642 1.7441 1.5553 -0.1272 -0.0404 0.0958  215 PRO A O   
6396 C CB  . PRO D 212 ? 1.8828 2.0426 1.8670 -0.1289 -0.0496 0.0924  215 PRO A CB  
6397 C CG  . PRO D 212 ? 1.6456 1.8074 1.6329 -0.1348 -0.0552 0.0980  215 PRO A CG  
6398 C CD  . PRO D 212 ? 1.5619 1.7162 1.5425 -0.1376 -0.0566 0.0954  215 PRO A CD  
6399 N N   . ARG D 213 ? 1.8743 2.0543 1.8683 -0.1201 -0.0368 0.0920  216 ARG A N   
6400 C CA  . ARG D 213 ? 1.8751 2.0689 1.8774 -0.1169 -0.0317 0.0941  216 ARG A CA  
6401 C C   . ARG D 213 ? 1.9418 2.1428 1.9535 -0.1142 -0.0313 0.0965  216 ARG A C   
6402 O O   . ARG D 213 ? 2.2515 2.4467 2.2619 -0.1113 -0.0313 0.0933  216 ARG A O   
6403 C CB  . ARG D 213 ? 1.9228 2.1165 1.9208 -0.1121 -0.0253 0.0883  216 ARG A CB  
6404 C CG  . ARG D 213 ? 1.7275 1.9177 1.7187 -0.1148 -0.0249 0.0872  216 ARG A CG  
6405 C CD  . ARG D 213 ? 1.8585 2.0487 1.8455 -0.1102 -0.0187 0.0816  216 ARG A CD  
6406 N NE  . ARG D 213 ? 2.2430 2.4299 2.2239 -0.1131 -0.0188 0.0810  216 ARG A NE  
6407 C CZ  . ARG D 213 ? 2.4558 2.6403 2.4311 -0.1105 -0.0146 0.0764  216 ARG A CZ  
6408 N NH1 . ARG D 213 ? 2.6204 2.8034 2.5941 -0.1049 -0.0102 0.0712  216 ARG A NH1 
6409 N NH2 . ARG D 213 ? 2.5381 2.7219 2.5097 -0.1138 -0.0151 0.0773  216 ARG A NH2 
6410 N N   . ILE D 214 ? 1.7305 1.9444 1.7520 -0.1152 -0.0311 0.1023  217 ILE A N   
6411 C CA  . ILE D 214 ? 2.1274 2.3492 2.1596 -0.1135 -0.0315 0.1060  217 ILE A CA  
6412 C C   . ILE D 214 ? 2.3395 2.5727 2.3785 -0.1076 -0.0244 0.1038  217 ILE A C   
6413 O O   . ILE D 214 ? 2.5060 2.7528 2.5541 -0.1076 -0.0223 0.1081  217 ILE A O   
6414 C CB  . ILE D 214 ? 2.2208 2.4496 2.2599 -0.1188 -0.0363 0.1140  217 ILE A CB  
6415 C CG1 . ILE D 214 ? 1.9991 2.2161 2.0312 -0.1246 -0.0435 0.1154  217 ILE A CG1 
6416 C CG2 . ILE D 214 ? 2.2101 2.4469 2.2608 -0.1174 -0.0372 0.1182  217 ILE A CG2 
6417 C CD1 . ILE D 214 ? 1.8061 2.0290 1.8437 -0.1302 -0.0483 0.1230  217 ILE A CD1 
6418 N N   . ALA D 215 ? 2.1947 2.4227 2.2295 -0.1025 -0.0204 0.0971  218 ALA A N   
6419 C CA  . ALA D 215 ? 2.4772 2.7144 2.5161 -0.0969 -0.0132 0.0936  218 ALA A CA  
6420 C C   . ALA D 215 ? 3.0185 3.2557 3.0635 -0.0912 -0.0115 0.0904  218 ALA A C   
6421 O O   . ALA D 215 ? 3.1099 3.3358 3.1486 -0.0893 -0.0124 0.0859  218 ALA A O   
6422 C CB  . ALA D 215 ? 2.2427 2.4743 2.2710 -0.0958 -0.0097 0.0880  218 ALA A CB  
6423 N N   . THR D 216 ? 3.1182 3.3684 3.1758 -0.0883 -0.0090 0.0928  219 THR A N   
6424 C CA  . THR D 216 ? 3.1106 3.3621 3.1766 -0.0831 -0.0080 0.0906  219 THR A CA  
6425 C C   . THR D 216 ? 2.9258 3.1724 2.9875 -0.0772 -0.0033 0.0826  219 THR A C   
6426 O O   . THR D 216 ? 2.8739 3.1281 2.9367 -0.0737 0.0027  0.0790  219 THR A O   
6427 C CB  . THR D 216 ? 3.1367 3.4045 3.2178 -0.0808 -0.0054 0.0941  219 THR A CB  
6428 O OG1 . THR D 216 ? 3.2843 3.5629 3.3660 -0.0787 0.0011  0.0920  219 THR A OG1 
6429 C CG2 . THR D 216 ? 3.2323 3.5046 3.3188 -0.0865 -0.0106 0.1026  219 THR A CG2 
6430 N N   . ARG D 217 ? 3.3147 3.5488 3.3714 -0.0762 -0.0062 0.0797  220 ARG A N   
6431 C CA  . ARG D 217 ? 2.8160 3.0448 2.8691 -0.0707 -0.0024 0.0724  220 ARG A CA  
6432 C C   . ARG D 217 ? 2.8414 3.0690 2.9036 -0.0669 -0.0041 0.0718  220 ARG A C   
6433 O O   . ARG D 217 ? 3.0443 3.2763 3.1158 -0.0684 -0.0077 0.0770  220 ARG A O   
6434 C CB  . ARG D 217 ? 2.4476 2.6621 2.4857 -0.0729 -0.0039 0.0689  220 ARG A CB  
6435 C CG  . ARG D 217 ? 2.4962 2.7113 2.5259 -0.0766 -0.0025 0.0694  220 ARG A CG  
6436 C CD  . ARG D 217 ? 2.1536 2.3546 2.1694 -0.0781 -0.0036 0.0654  220 ARG A CD  
6437 N NE  . ARG D 217 ? 2.3432 2.5438 2.3517 -0.0823 -0.0034 0.0664  220 ARG A NE  
6438 C CZ  . ARG D 217 ? 2.3717 2.5613 2.3689 -0.0844 -0.0045 0.0637  220 ARG A CZ  
6439 N NH1 . ARG D 217 ? 2.4109 2.5905 2.4020 -0.0815 -0.0038 0.0584  220 ARG A NH1 
6440 N NH2 . ARG D 217 ? 2.0648 2.2536 2.0575 -0.0895 -0.0065 0.0664  220 ARG A NH2 
6441 N N   . SER D 218 ? 3.0027 3.2239 3.0622 -0.0622 -0.0021 0.0657  221 SER A N   
6442 C CA  . SER D 218 ? 3.0582 3.2781 3.1268 -0.0583 -0.0039 0.0649  221 SER A CA  
6443 C C   . SER D 218 ? 3.1407 3.3499 3.2055 -0.0624 -0.0109 0.0682  221 SER A C   
6444 O O   . SER D 218 ? 3.1224 3.3222 3.1747 -0.0668 -0.0135 0.0685  221 SER A O   
6445 C CB  . SER D 218 ? 2.8001 3.0167 2.8675 -0.0520 0.0003  0.0573  221 SER A CB  
6446 O OG  . SER D 218 ? 2.3170 2.5209 2.3700 -0.0535 -0.0004 0.0540  221 SER A OG  
6447 N N   . LYS D 219 ? 3.0795 3.2904 3.1553 -0.0609 -0.0140 0.0707  222 LYS A N   
6448 C CA  . LYS D 219 ? 3.0722 3.2746 3.1458 -0.0650 -0.0210 0.0746  222 LYS A CA  
6449 C C   . LYS D 219 ? 3.0593 3.2500 3.1254 -0.0632 -0.0221 0.0701  222 LYS A C   
6450 O O   . LYS D 219 ? 3.0210 3.2090 3.0932 -0.0618 -0.0254 0.0710  222 LYS A O   
6451 C CB  . LYS D 219 ? 2.9744 3.1840 3.0636 -0.0646 -0.0244 0.0798  222 LYS A CB  
6452 C CG  . LYS D 219 ? 2.7151 2.9353 2.8114 -0.0676 -0.0248 0.0857  222 LYS A CG  
6453 C CD  . LYS D 219 ? 2.2478 2.4747 2.3601 -0.0672 -0.0283 0.0909  222 LYS A CD  
6454 C CE  . LYS D 219 ? 2.1587 2.3962 2.2779 -0.0705 -0.0289 0.0971  222 LYS A CE  
6455 N NZ  . LYS D 219 ? 2.1935 2.4380 2.3290 -0.0701 -0.0324 0.1026  222 LYS A NZ  
6456 N N   . VAL D 220 ? 2.9975 3.1811 3.0503 -0.0636 -0.0195 0.0656  223 VAL A N   
6457 C CA  . VAL D 220 ? 2.9982 3.1709 3.0433 -0.0620 -0.0203 0.0613  223 VAL A CA  
6458 C C   . VAL D 220 ? 3.2460 3.4103 3.2851 -0.0675 -0.0268 0.0649  223 VAL A C   
6459 O O   . VAL D 220 ? 3.3368 3.4998 3.3699 -0.0732 -0.0295 0.0683  223 VAL A O   
6460 C CB  . VAL D 220 ? 2.6885 2.8563 2.7214 -0.0610 -0.0158 0.0557  223 VAL A CB  
6461 C CG1 . VAL D 220 ? 2.3516 2.5078 2.3765 -0.0598 -0.0170 0.0519  223 VAL A CG1 
6462 C CG2 . VAL D 220 ? 2.4269 2.6033 2.4653 -0.0556 -0.0093 0.0519  223 VAL A CG2 
6463 N N   . ASN D 221 ? 2.9118 3.0706 2.9525 -0.0659 -0.0295 0.0643  224 ASN A N   
6464 C CA  . ASN D 221 ? 3.0447 3.1954 3.0789 -0.0710 -0.0355 0.0672  224 ASN A CA  
6465 C C   . ASN D 221 ? 3.2512 3.4065 3.2912 -0.0760 -0.0406 0.0742  224 ASN A C   
6466 O O   . ASN D 221 ? 3.3943 3.5443 3.4261 -0.0819 -0.0449 0.0769  224 ASN A O   
6467 C CB  . ASN D 221 ? 2.9815 3.1231 2.9991 -0.0744 -0.0351 0.0642  224 ASN A CB  
6468 C CG  . ASN D 221 ? 2.8843 3.0195 2.8957 -0.0702 -0.0316 0.0580  224 ASN A CG  
6469 O OD1 . ASN D 221 ? 3.0508 3.1858 3.0687 -0.0658 -0.0314 0.0564  224 ASN A OD1 
6470 N ND2 . ASN D 221 ? 2.7407 2.8708 2.7403 -0.0715 -0.0290 0.0545  224 ASN A ND2 
6471 N N   . GLY D 222 ? 3.0790 3.2444 3.1332 -0.0736 -0.0399 0.0771  225 GLY A N   
6472 C CA  . GLY D 222 ? 2.8926 3.0630 2.9539 -0.0780 -0.0446 0.0842  225 GLY A CA  
6473 C C   . GLY D 222 ? 2.8006 2.9735 2.8563 -0.0828 -0.0447 0.0867  225 GLY A C   
6474 O O   . GLY D 222 ? 2.7403 2.9151 2.7986 -0.0877 -0.0495 0.0926  225 GLY A O   
6475 N N   . GLN D 223 ? 2.9997 3.1724 3.0480 -0.0817 -0.0398 0.0826  226 GLN A N   
6476 C CA  . GLN D 223 ? 2.8613 3.0367 2.9053 -0.0861 -0.0399 0.0851  226 GLN A CA  
6477 C C   . GLN D 223 ? 2.7297 2.9126 2.7761 -0.0824 -0.0334 0.0823  226 GLN A C   
6478 O O   . GLN D 223 ? 2.7577 2.9374 2.7987 -0.0786 -0.0289 0.0764  226 GLN A O   
6479 C CB  . GLN D 223 ? 2.7289 2.8938 2.7572 -0.0912 -0.0423 0.0836  226 GLN A CB  
6480 C CG  . GLN D 223 ? 2.5326 2.6912 2.5573 -0.0961 -0.0489 0.0868  226 GLN A CG  
6481 C CD  . GLN D 223 ? 2.5341 2.6827 2.5435 -0.1006 -0.0506 0.0843  226 GLN A CD  
6482 O OE1 . GLN D 223 ? 2.5538 2.6983 2.5553 -0.0990 -0.0468 0.0792  226 GLN A OE1 
6483 N NE2 . GLN D 223 ? 2.4567 2.6017 2.4622 -0.1065 -0.0565 0.0877  226 GLN A NE2 
6484 N N   . SER D 224 ? 2.7076 2.9005 2.7619 -0.0837 -0.0330 0.0867  227 SER A N   
6485 C CA  . SER D 224 ? 2.7391 2.9415 2.7977 -0.0802 -0.0269 0.0848  227 SER A CA  
6486 C C   . SER D 224 ? 2.7557 2.9547 2.8022 -0.0829 -0.0248 0.0827  227 SER A C   
6487 O O   . SER D 224 ? 2.7921 2.9955 2.8378 -0.0796 -0.0192 0.0790  227 SER A O   
6488 C CB  . SER D 224 ? 2.8192 3.0344 2.8913 -0.0808 -0.0273 0.0907  227 SER A CB  
6489 O OG  . SER D 224 ? 3.1006 3.3262 3.1768 -0.0778 -0.0213 0.0891  227 SER A OG  
6490 N N   . GLY D 225 ? 2.8329 3.0245 2.8704 -0.0889 -0.0294 0.0849  228 GLY A N   
6491 C CA  . GLY D 225 ? 2.5215 2.7082 2.5477 -0.0915 -0.0283 0.0826  228 GLY A CA  
6492 C C   . GLY D 225 ? 2.2534 2.4287 2.2685 -0.0897 -0.0269 0.0763  228 GLY A C   
6493 O O   . GLY D 225 ? 2.2955 2.4674 2.3118 -0.0861 -0.0264 0.0734  228 GLY A O   
6494 N N   . ARG D 226 ? 2.3600 2.5296 2.3647 -0.0924 -0.0265 0.0741  229 ARG A N   
6495 C CA  . ARG D 226 ? 2.3472 2.5057 2.3409 -0.0913 -0.0254 0.0683  229 ARG A CA  
6496 C C   . ARG D 226 ? 2.1271 2.2769 2.1108 -0.0971 -0.0295 0.0686  229 ARG A C   
6497 O O   . ARG D 226 ? 2.1931 2.3454 2.1783 -0.1017 -0.0330 0.0731  229 ARG A O   
6498 C CB  . ARG D 226 ? 2.4289 2.5894 2.4206 -0.0870 -0.0192 0.0637  229 ARG A CB  
6499 C CG  . ARG D 226 ? 2.5698 2.7379 2.5708 -0.0808 -0.0151 0.0620  229 ARG A CG  
6500 C CD  . ARG D 226 ? 2.4771 2.6467 2.4749 -0.0768 -0.0091 0.0569  229 ARG A CD  
6501 N NE  . ARG D 226 ? 2.2813 2.4593 2.2889 -0.0709 -0.0051 0.0552  229 ARG A NE  
6502 C CZ  . ARG D 226 ? 2.6017 2.7837 2.6091 -0.0667 0.0005  0.0508  229 ARG A CZ  
6503 N NH1 . ARG D 226 ? 2.6841 2.8620 2.6818 -0.0677 0.0027  0.0480  229 ARG A NH1 
6504 N NH2 . ARG D 226 ? 2.8206 3.0110 2.8380 -0.0615 0.0039  0.0492  229 ARG A NH2 
6505 N N   . MET D 227 ? 2.0066 2.1460 1.9801 -0.0967 -0.0290 0.0636  230 MET A N   
6506 C CA  . MET D 227 ? 2.0808 2.2108 2.0446 -0.1017 -0.0329 0.0628  230 MET A CA  
6507 C C   . MET D 227 ? 2.2541 2.3761 2.2085 -0.1002 -0.0299 0.0569  230 MET A C   
6508 O O   . MET D 227 ? 2.4612 2.5754 2.4096 -0.0988 -0.0298 0.0531  230 MET A O   
6509 C CB  . MET D 227 ? 2.0955 2.2201 2.0573 -0.1040 -0.0376 0.0638  230 MET A CB  
6510 C CG  . MET D 227 ? 2.0691 2.2000 2.0388 -0.1071 -0.0419 0.0700  230 MET A CG  
6511 S SD  . MET D 227 ? 2.1933 2.3195 2.1619 -0.1092 -0.0470 0.0716  230 MET A SD  
6512 C CE  . MET D 227 ? 2.3681 2.5060 2.3519 -0.1082 -0.0484 0.0783  230 MET A CE  
6513 N N   . GLU D 228 ? 1.9364 2.0606 1.8896 -0.1008 -0.0276 0.0566  231 GLU A N   
6514 C CA  . GLU D 228 ? 2.1234 2.2401 2.0680 -0.1000 -0.0253 0.0516  231 GLU A CA  
6515 C C   . GLU D 228 ? 1.8877 1.9940 1.8239 -0.1043 -0.0294 0.0499  231 GLU A C   
6516 O O   . GLU D 228 ? 1.9700 2.0763 1.9064 -0.1091 -0.0334 0.0527  231 GLU A O   
6517 C CB  . GLU D 228 ? 2.1672 2.2892 2.1131 -0.1004 -0.0226 0.0524  231 GLU A CB  
6518 C CG  . GLU D 228 ? 2.4081 2.5405 2.3610 -0.0960 -0.0176 0.0529  231 GLU A CG  
6519 C CD  . GLU D 228 ? 2.6125 2.7499 2.5650 -0.0968 -0.0149 0.0535  231 GLU A CD  
6520 O OE1 . GLU D 228 ? 2.5361 2.6673 2.4827 -0.1004 -0.0169 0.0530  231 GLU A OE1 
6521 O OE2 . GLU D 228 ? 2.8368 2.9844 2.7952 -0.0941 -0.0110 0.0544  231 GLU A OE2 
6522 N N   . PHE D 229 ? 1.9006 1.9982 1.8296 -0.1027 -0.0286 0.0451  232 PHE A N   
6523 C CA  . PHE D 229 ? 1.8200 1.9081 1.7410 -0.1063 -0.0319 0.0426  232 PHE A CA  
6524 C C   . PHE D 229 ? 1.7821 1.8644 1.6972 -0.1070 -0.0305 0.0391  232 PHE A C   
6525 O O   . PHE D 229 ? 1.8183 1.9032 1.7345 -0.1044 -0.0267 0.0382  232 PHE A O   
6526 C CB  . PHE D 229 ? 1.9337 2.0164 1.8506 -0.1045 -0.0322 0.0399  232 PHE A CB  
6527 C CG  . PHE D 229 ? 1.9409 2.0258 1.8607 -0.1068 -0.0362 0.0434  232 PHE A CG  
6528 C CD1 . PHE D 229 ? 1.8759 1.9684 1.8043 -0.1042 -0.0358 0.0469  232 PHE A CD1 
6529 C CD2 . PHE D 229 ? 2.0151 2.0946 1.9292 -0.1114 -0.0406 0.0430  232 PHE A CD2 
6530 C CE1 . PHE D 229 ? 1.9285 2.0230 1.8602 -0.1066 -0.0398 0.0506  232 PHE A CE1 
6531 C CE2 . PHE D 229 ? 2.0243 2.1059 1.9408 -0.1139 -0.0445 0.0465  232 PHE A CE2 
6532 C CZ  . PHE D 229 ? 1.9918 2.0809 1.9171 -0.1116 -0.0443 0.0505  232 PHE A CZ  
6533 N N   . PHE D 230 ? 1.8025 1.8771 1.7114 -0.1107 -0.0337 0.0369  233 PHE A N   
6534 C CA  . PHE D 230 ? 1.5837 1.6524 1.4881 -0.1121 -0.0334 0.0339  233 PHE A CA  
6535 C C   . PHE D 230 ? 1.6628 1.7213 1.5588 -0.1126 -0.0341 0.0285  233 PHE A C   
6536 O O   . PHE D 230 ? 1.9488 2.0053 1.8422 -0.1123 -0.0350 0.0275  233 PHE A O   
6537 C CB  . PHE D 230 ? 1.5911 1.6615 1.4983 -0.1169 -0.0372 0.0369  233 PHE A CB  
6538 C CG  . PHE D 230 ? 1.6070 1.6876 1.5221 -0.1168 -0.0362 0.0422  233 PHE A CG  
6539 C CD1 . PHE D 230 ? 1.5759 1.6646 1.4973 -0.1164 -0.0369 0.0467  233 PHE A CD1 
6540 C CD2 . PHE D 230 ? 1.5884 1.6710 1.5049 -0.1172 -0.0348 0.0429  233 PHE A CD2 
6541 C CE1 . PHE D 230 ? 1.6755 1.7744 1.6045 -0.1162 -0.0357 0.0514  233 PHE A CE1 
6542 C CE2 . PHE D 230 ? 1.6874 1.7803 1.6109 -0.1173 -0.0337 0.0479  233 PHE A CE2 
6543 C CZ  . PHE D 230 ? 1.7568 1.8582 1.6867 -0.1167 -0.0340 0.0520  233 PHE A CZ  
6544 N N   . TRP D 231 ? 1.4530 1.5056 1.3453 -0.1137 -0.0339 0.0253  234 TRP A N   
6545 C CA  . TRP D 231 ? 1.9262 1.9694 1.8110 -0.1143 -0.0344 0.0199  234 TRP A CA  
6546 C C   . TRP D 231 ? 1.9160 1.9540 1.7995 -0.1174 -0.0363 0.0179  234 TRP A C   
6547 O O   . TRP D 231 ? 1.5316 1.5723 1.4190 -0.1178 -0.0359 0.0201  234 TRP A O   
6548 C CB  . TRP D 231 ? 1.8674 1.9074 1.7486 -0.1098 -0.0300 0.0164  234 TRP A CB  
6549 C CG  . TRP D 231 ? 1.6717 1.7136 1.5551 -0.1071 -0.0264 0.0166  234 TRP A CG  
6550 C CD1 . TRP D 231 ? 1.8769 1.9257 1.7647 -0.1037 -0.0233 0.0190  234 TRP A CD1 
6551 C CD2 . TRP D 231 ? 1.8052 1.8420 1.6863 -0.1076 -0.0256 0.0140  234 TRP A CD2 
6552 N NE1 . TRP D 231 ? 1.9283 1.9769 1.8160 -0.1023 -0.0205 0.0181  234 TRP A NE1 
6553 C CE2 . TRP D 231 ? 1.9071 1.9483 1.7909 -0.1048 -0.0220 0.0154  234 TRP A CE2 
6554 C CE3 . TRP D 231 ? 1.8407 1.8697 1.7181 -0.1103 -0.0277 0.0106  234 TRP A CE3 
6555 C CZ2 . TRP D 231 ? 1.9989 2.0370 1.8815 -0.1049 -0.0207 0.0139  234 TRP A CZ2 
6556 C CZ3 . TRP D 231 ? 1.9437 1.9694 1.8209 -0.1101 -0.0264 0.0091  234 TRP A CZ3 
6557 C CH2 . TRP D 231 ? 1.9018 1.9321 1.7814 -0.1076 -0.0231 0.0111  234 TRP A CH2 
6558 N N   . THR D 232 ? 1.9592 1.9899 1.8373 -0.1196 -0.0385 0.0137  235 THR A N   
6559 C CA  . THR D 232 ? 1.6206 1.6446 1.4970 -0.1217 -0.0400 0.0101  235 THR A CA  
6560 C C   . THR D 232 ? 1.9310 1.9470 1.8003 -0.1209 -0.0390 0.0038  235 THR A C   
6561 O O   . THR D 232 ? 2.2193 2.2343 2.0847 -0.1219 -0.0402 0.0023  235 THR A O   
6562 C CB  . THR D 232 ? 1.7120 1.7357 1.5910 -0.1266 -0.0453 0.0115  235 THR A CB  
6563 O OG1 . THR D 232 ? 2.3482 2.3714 2.2240 -0.1287 -0.0480 0.0108  235 THR A OG1 
6564 C CG2 . THR D 232 ? 1.5177 1.5490 1.4041 -0.1279 -0.0466 0.0179  235 THR A CG2 
6565 N N   . ILE D 233 ? 2.0846 2.0954 1.9525 -0.1195 -0.0370 0.0005  236 ILE A N   
6566 C CA  . ILE D 233 ? 2.3846 2.3877 2.2466 -0.1192 -0.0363 -0.0057 236 ILE A CA  
6567 C C   . ILE D 233 ? 2.3779 2.3767 2.2399 -0.1234 -0.0405 -0.0085 236 ILE A C   
6568 O O   . ILE D 233 ? 1.9874 1.9840 1.8531 -0.1249 -0.0422 -0.0086 236 ILE A O   
6569 C CB  . ILE D 233 ? 2.2381 2.2372 2.0994 -0.1163 -0.0328 -0.0082 236 ILE A CB  
6570 C CG1 . ILE D 233 ? 2.3056 2.3083 2.1664 -0.1120 -0.0287 -0.0062 236 ILE A CG1 
6571 C CG2 . ILE D 233 ? 2.1021 2.0934 1.9581 -0.1164 -0.0325 -0.0146 236 ILE A CG2 
6572 C CD1 . ILE D 233 ? 2.2690 2.2685 2.1298 -0.1097 -0.0257 -0.0076 236 ILE A CD1 
6573 N N   . LEU D 234 ? 2.0541 2.0517 1.9119 -0.1254 -0.0425 -0.0110 237 LEU A N   
6574 C CA  . LEU D 234 ? 1.9501 1.9436 1.8078 -0.1294 -0.0467 -0.0142 237 LEU A CA  
6575 C C   . LEU D 234 ? 2.0262 2.0120 1.8812 -0.1289 -0.0457 -0.0211 237 LEU A C   
6576 O O   . LEU D 234 ? 2.1752 2.1583 2.0244 -0.1274 -0.0433 -0.0253 237 LEU A O   
6577 C CB  . LEU D 234 ? 2.1854 2.1805 2.0392 -0.1321 -0.0494 -0.0147 237 LEU A CB  
6578 C CG  . LEU D 234 ? 2.2741 2.2765 2.1320 -0.1333 -0.0514 -0.0078 237 LEU A CG  
6579 C CD1 . LEU D 234 ? 2.1598 2.1632 2.0133 -0.1363 -0.0542 -0.0085 237 LEU A CD1 
6580 C CD2 . LEU D 234 ? 2.3487 2.3513 2.2131 -0.1356 -0.0546 -0.0053 237 LEU A CD2 
6581 N N   . LYS D 235 ? 2.1791 2.1615 2.0387 -0.1303 -0.0479 -0.0219 238 LYS A N   
6582 C CA  . LYS D 235 ? 1.8868 1.8616 1.7455 -0.1305 -0.0480 -0.0285 238 LYS A CA  
6583 C C   . LYS D 235 ? 1.8107 1.7827 1.6667 -0.1338 -0.0515 -0.0335 238 LYS A C   
6584 O O   . LYS D 235 ? 1.8728 1.8475 1.7306 -0.1369 -0.0555 -0.0308 238 LYS A O   
6585 C CB  . LYS D 235 ? 1.8094 1.7820 1.6753 -0.1312 -0.0497 -0.0269 238 LYS A CB  
6586 C CG  . LYS D 235 ? 1.7812 1.7565 1.6489 -0.1280 -0.0460 -0.0228 238 LYS A CG  
6587 C CD  . LYS D 235 ? 1.2591 1.2328 1.1337 -0.1292 -0.0479 -0.0206 238 LYS A CD  
6588 C CE  . LYS D 235 ? 1.6563 1.6331 1.5316 -0.1262 -0.0438 -0.0169 238 LYS A CE  
6589 N NZ  . LYS D 235 ? 1.9602 1.9364 1.8420 -0.1277 -0.0457 -0.0139 238 LYS A NZ  
6590 N N   . PRO D 236 ? 1.8793 1.8462 1.7308 -0.1333 -0.0501 -0.0407 239 PRO A N   
6591 C CA  . PRO D 236 ? 1.9261 1.8906 1.7742 -0.1363 -0.0530 -0.0463 239 PRO A CA  
6592 C C   . PRO D 236 ? 2.0199 1.9824 1.8740 -0.1399 -0.0586 -0.0461 239 PRO A C   
6593 O O   . PRO D 236 ? 1.8880 1.8471 1.7487 -0.1398 -0.0601 -0.0459 239 PRO A O   
6594 C CB  . PRO D 236 ? 1.7162 1.6751 1.5611 -0.1346 -0.0502 -0.0541 239 PRO A CB  
6595 C CG  . PRO D 236 ? 1.8059 1.7665 1.6486 -0.1307 -0.0451 -0.0517 239 PRO A CG  
6596 C CD  . PRO D 236 ? 1.9206 1.8848 1.7689 -0.1297 -0.0453 -0.0438 239 PRO A CD  
6597 N N   . ASN D 237 ? 2.1767 2.1413 2.0286 -0.1432 -0.0622 -0.0459 240 ASN A N   
6598 C CA  . ASN D 237 ? 2.0281 1.9910 1.8852 -0.1469 -0.0681 -0.0459 240 ASN A CA  
6599 C C   . ASN D 237 ? 2.0385 2.0045 1.9038 -0.1473 -0.0702 -0.0378 240 ASN A C   
6600 O O   . ASN D 237 ? 2.1174 2.0801 1.9895 -0.1474 -0.0719 -0.0376 240 ASN A O   
6601 C CB  . ASN D 237 ? 1.7797 1.7348 1.6388 -0.1476 -0.0698 -0.0543 240 ASN A CB  
6602 C CG  . ASN D 237 ? 2.1779 2.1309 2.0290 -0.1482 -0.0688 -0.0627 240 ASN A CG  
6603 O OD1 . ASN D 237 ? 2.4381 2.3951 2.2826 -0.1498 -0.0687 -0.0620 240 ASN A OD1 
6604 N ND2 . ASN D 237 ? 2.2254 2.1724 2.0773 -0.1472 -0.0678 -0.0706 240 ASN A ND2 
6605 N N   . ASP D 238 ? 1.6587 1.6316 1.5236 -0.1477 -0.0702 -0.0308 241 ASP A N   
6606 C CA  . ASP D 238 ? 1.7859 1.7637 1.6582 -0.1480 -0.0716 -0.0226 241 ASP A CA  
6607 C C   . ASP D 238 ? 1.8365 1.8207 1.7085 -0.1503 -0.0741 -0.0170 241 ASP A C   
6608 O O   . ASP D 238 ? 1.8165 1.8050 1.6839 -0.1488 -0.0712 -0.0153 241 ASP A O   
6609 C CB  . ASP D 238 ? 1.9090 1.8896 1.7823 -0.1440 -0.0664 -0.0192 241 ASP A CB  
6610 C CG  . ASP D 238 ? 2.1735 2.1612 2.0531 -0.1443 -0.0671 -0.0105 241 ASP A CG  
6611 O OD1 . ASP D 238 ? 2.1816 2.1699 2.0672 -0.1476 -0.0719 -0.0075 241 ASP A OD1 
6612 O OD2 . ASP D 238 ? 2.2858 2.2787 2.1645 -0.1413 -0.0629 -0.0068 241 ASP A OD2 
6613 N N   . ALA D 239 ? 1.8276 1.8124 1.7051 -0.1540 -0.0796 -0.0140 242 ALA A N   
6614 C CA  . ALA D 239 ? 2.1532 2.1438 2.0314 -0.1566 -0.0827 -0.0084 242 ALA A CA  
6615 C C   . ALA D 239 ? 2.0514 2.0502 1.9345 -0.1548 -0.0804 0.0001  242 ALA A C   
6616 O O   . ALA D 239 ? 1.8850 1.8859 1.7753 -0.1555 -0.0821 0.0046  242 ALA A O   
6617 C CB  . ALA D 239 ? 2.4618 2.4498 2.3446 -0.1612 -0.0897 -0.0083 242 ALA A CB  
6618 N N   . ILE D 240 ? 1.7845 1.7884 1.6640 -0.1526 -0.0769 0.0025  243 ILE A N   
6619 C CA  . ILE D 240 ? 1.6973 1.7099 1.5823 -0.1516 -0.0757 0.0107  243 ILE A CA  
6620 C C   . ILE D 240 ? 1.7257 1.7419 1.6143 -0.1558 -0.0813 0.0154  243 ILE A C   
6621 O O   . ILE D 240 ? 1.5273 1.5427 1.4116 -0.1579 -0.0836 0.0139  243 ILE A O   
6622 C CB  . ILE D 240 ? 1.6456 1.6627 1.5272 -0.1479 -0.0707 0.0121  243 ILE A CB  
6623 C CG1 . ILE D 240 ? 1.7017 1.7155 1.5801 -0.1436 -0.0653 0.0080  243 ILE A CG1 
6624 C CG2 . ILE D 240 ? 1.6897 1.7158 1.5781 -0.1469 -0.0698 0.0199  243 ILE A CG2 
6625 C CD1 . ILE D 240 ? 2.0717 2.0891 1.9466 -0.1405 -0.0614 0.0088  243 ILE A CD1 
6626 N N   . ASN D 241 ? 1.9169 1.9374 1.8134 -0.1572 -0.0836 0.0214  244 ASN A N   
6627 C CA  . ASN D 241 ? 1.7952 1.8204 1.6965 -0.1611 -0.0887 0.0273  244 ASN A CA  
6628 C C   . ASN D 241 ? 1.6276 1.6630 1.5330 -0.1590 -0.0857 0.0346  244 ASN A C   
6629 O O   . ASN D 241 ? 1.7489 1.7896 1.6603 -0.1578 -0.0840 0.0392  244 ASN A O   
6630 C CB  . ASN D 241 ? 1.9522 1.9759 1.8605 -0.1643 -0.0936 0.0294  244 ASN A CB  
6631 C CG  . ASN D 241 ? 2.3151 2.3287 2.2208 -0.1667 -0.0975 0.0221  244 ASN A CG  
6632 O OD1 . ASN D 241 ? 2.3995 2.4083 2.2983 -0.1671 -0.0978 0.0161  244 ASN A OD1 
6633 N ND2 . ASN D 241 ? 2.5378 2.5488 2.4497 -0.1685 -0.1008 0.0228  244 ASN A ND2 
6634 N N   . PHE D 242 ? 1.5507 1.5892 1.4532 -0.1586 -0.0851 0.0357  245 PHE A N   
6635 C CA  . PHE D 242 ? 1.6813 1.7296 1.5886 -0.1568 -0.0828 0.0425  245 PHE A CA  
6636 C C   . PHE D 242 ? 1.7737 1.8269 1.6868 -0.1609 -0.0883 0.0489  245 PHE A C   
6637 O O   . PHE D 242 ? 1.7511 1.8013 1.6612 -0.1644 -0.0928 0.0478  245 PHE A O   
6638 C CB  . PHE D 242 ? 1.4518 1.5012 1.3541 -0.1541 -0.0795 0.0411  245 PHE A CB  
6639 C CG  . PHE D 242 ? 1.5093 1.5573 1.4084 -0.1490 -0.0732 0.0375  245 PHE A CG  
6640 C CD1 . PHE D 242 ? 1.8485 1.9031 1.7526 -0.1453 -0.0689 0.0411  245 PHE A CD1 
6641 C CD2 . PHE D 242 ? 1.5289 1.5696 1.4198 -0.1479 -0.0716 0.0306  245 PHE A CD2 
6642 C CE1 . PHE D 242 ? 1.9330 1.9862 1.8341 -0.1407 -0.0634 0.0377  245 PHE A CE1 
6643 C CE2 . PHE D 242 ? 1.7250 1.7645 1.6131 -0.1434 -0.0661 0.0276  245 PHE A CE2 
6644 C CZ  . PHE D 242 ? 1.7946 1.8400 1.6878 -0.1397 -0.0621 0.0311  245 PHE A CZ  
6645 N N   . GLU D 243 ? 1.7565 1.8179 1.6779 -0.1607 -0.0879 0.0557  246 GLU A N   
6646 C CA  . GLU D 243 ? 1.8685 1.9361 1.7965 -0.1643 -0.0927 0.0628  246 GLU A CA  
6647 C C   . GLU D 243 ? 2.0806 2.1595 2.0151 -0.1616 -0.0890 0.0692  246 GLU A C   
6648 O O   . GLU D 243 ? 2.3361 2.4195 2.2735 -0.1583 -0.0843 0.0702  246 GLU A O   
6649 C CB  . GLU D 243 ? 2.0947 2.1616 2.0280 -0.1680 -0.0972 0.0653  246 GLU A CB  
6650 C CG  . GLU D 243 ? 2.3467 2.4192 2.2867 -0.1722 -0.1028 0.0725  246 GLU A CG  
6651 C CD  . GLU D 243 ? 2.4945 2.5663 2.4402 -0.1759 -0.1076 0.0752  246 GLU A CD  
6652 O OE1 . GLU D 243 ? 2.5912 2.6549 2.5341 -0.1763 -0.1084 0.0698  246 GLU A OE1 
6653 O OE2 . GLU D 243 ? 2.6180 2.6975 2.5716 -0.1784 -0.1106 0.0830  246 GLU A OE2 
6654 N N   . SER D 244 ? 1.8412 1.9249 1.7784 -0.1629 -0.0912 0.0735  247 SER A N   
6655 C CA  . SER D 244 ? 1.7216 1.8165 1.6662 -0.1602 -0.0879 0.0796  247 SER A CA  
6656 C C   . SER D 244 ? 1.7185 1.8192 1.6692 -0.1638 -0.0928 0.0864  247 SER A C   
6657 O O   . SER D 244 ? 1.6937 1.7895 1.6406 -0.1673 -0.0977 0.0856  247 SER A O   
6658 C CB  . SER D 244 ? 1.6350 1.7306 1.5765 -0.1552 -0.0823 0.0767  247 SER A CB  
6659 O OG  . SER D 244 ? 1.5992 1.7057 1.5489 -0.1527 -0.0798 0.0824  247 SER A OG  
6660 N N   . ASN D 245 ? 1.7255 1.8371 1.6856 -0.1629 -0.0915 0.0932  248 ASN A N   
6661 C CA  . ASN D 245 ? 1.8178 1.9371 1.7853 -0.1653 -0.0949 0.1005  248 ASN A CA  
6662 C C   . ASN D 245 ? 1.9466 2.0742 1.9190 -0.1610 -0.0905 0.1031  248 ASN A C   
6663 O O   . ASN D 245 ? 2.2677 2.4034 2.2482 -0.1623 -0.0925 0.1097  248 ASN A O   
6664 C CB  . ASN D 245 ? 1.8801 2.0065 1.8561 -0.1683 -0.0976 0.1072  248 ASN A CB  
6665 C CG  . ASN D 245 ? 2.0241 2.1541 2.0057 -0.1728 -0.1039 0.1138  248 ASN A CG  
6666 O OD1 . ASN D 245 ? 2.3938 2.5188 2.3714 -0.1748 -0.1075 0.1126  248 ASN A OD1 
6667 N ND2 . ASN D 245 ? 2.2689 2.4083 2.2598 -0.1746 -0.1053 0.1211  248 ASN A ND2 
6668 N N   . GLY D 246 ? 2.0729 2.1986 2.0412 -0.1561 -0.0849 0.0980  249 GLY A N   
6669 C CA  . GLY D 246 ? 2.1707 2.3027 2.1435 -0.1522 -0.0815 0.0997  249 GLY A CA  
6670 C C   . GLY D 246 ? 1.8243 1.9563 1.7948 -0.1462 -0.0744 0.0949  249 GLY A C   
6671 O O   . GLY D 246 ? 1.8014 1.9298 1.7677 -0.1451 -0.0718 0.0910  249 GLY A O   
6672 N N   . ASN D 247 ? 1.7661 1.9021 1.7400 -0.1425 -0.0716 0.0953  250 ASN A N   
6673 C CA  . ASN D 247 ? 1.7998 1.9367 1.7729 -0.1364 -0.0650 0.0911  250 ASN A CA  
6674 C C   . ASN D 247 ? 1.6958 1.8216 1.6576 -0.1356 -0.0636 0.0837  250 ASN A C   
6675 O O   . ASN D 247 ? 1.4187 1.5439 1.3784 -0.1317 -0.0586 0.0800  250 ASN A O   
6676 C CB  . ASN D 247 ? 1.7683 1.9147 1.7481 -0.1337 -0.0604 0.0931  250 ASN A CB  
6677 C CG  . ASN D 247 ? 1.8007 1.9592 1.7923 -0.1342 -0.0613 0.1003  250 ASN A CG  
6678 O OD1 . ASN D 247 ? 1.8025 1.9680 1.8010 -0.1302 -0.0582 0.1015  250 ASN A OD1 
6679 N ND2 . ASN D 247 ? 1.8459 2.0070 1.8405 -0.1391 -0.0656 0.1053  250 ASN A ND2 
6680 N N   . PHE D 248 ? 1.6711 1.7883 1.6257 -0.1393 -0.0681 0.0816  251 PHE A N   
6681 C CA  . PHE D 248 ? 1.5924 1.6989 1.5363 -0.1394 -0.0675 0.0746  251 PHE A CA  
6682 C C   . PHE D 248 ? 1.3824 1.4842 1.3210 -0.1383 -0.0676 0.0717  251 PHE A C   
6683 O O   . PHE D 248 ? 1.4474 1.5502 1.3872 -0.1410 -0.0716 0.0747  251 PHE A O   
6684 C CB  . PHE D 248 ? 1.7292 1.8294 1.6685 -0.1448 -0.0726 0.0737  251 PHE A CB  
6685 C CG  . PHE D 248 ? 1.6109 1.7008 1.5405 -0.1447 -0.0716 0.0663  251 PHE A CG  
6686 C CD1 . PHE D 248 ? 1.6035 1.6919 1.5310 -0.1404 -0.0662 0.0624  251 PHE A CD1 
6687 C CD2 . PHE D 248 ? 1.3204 1.4022 1.2431 -0.1490 -0.0761 0.0631  251 PHE A CD2 
6688 C CE1 . PHE D 248 ? 1.6459 1.7250 1.5651 -0.1402 -0.0653 0.0559  251 PHE A CE1 
6689 C CE2 . PHE D 248 ? 1.1086 1.1815 1.0231 -0.1487 -0.0751 0.0561  251 PHE A CE2 
6690 C CZ  . PHE D 248 ? 1.4939 1.5654 1.4069 -0.1443 -0.0697 0.0527  251 PHE A CZ  
6691 N N   . ILE D 249 ? 1.2522 1.3490 1.1850 -0.1348 -0.0635 0.0661  252 ILE A N   
6692 C CA  . ILE D 249 ? 1.2491 1.3411 1.1762 -0.1338 -0.0633 0.0630  252 ILE A CA  
6693 C C   . ILE D 249 ? 1.3475 1.4296 1.2640 -0.1355 -0.0637 0.0566  252 ILE A C   
6694 O O   . ILE D 249 ? 1.2847 1.3633 1.1980 -0.1325 -0.0598 0.0524  252 ILE A O   
6695 C CB  . ILE D 249 ? 1.2864 1.3815 1.2167 -0.1278 -0.0582 0.0621  252 ILE A CB  
6696 C CG1 . ILE D 249 ? 1.4679 1.5733 1.4097 -0.1259 -0.0578 0.0680  252 ILE A CG1 
6697 C CG2 . ILE D 249 ? 1.5318 1.6232 1.4579 -0.1273 -0.0591 0.0604  252 ILE A CG2 
6698 C CD1 . ILE D 249 ? 1.4944 1.6035 1.4405 -0.1197 -0.0524 0.0666  252 ILE A CD1 
6699 N N   . ALA D 250 ? 1.3550 1.4325 1.2662 -0.1404 -0.0685 0.0558  253 ALA A N   
6700 C CA  . ALA D 250 ? 1.2762 1.3452 1.1791 -0.1430 -0.0699 0.0502  253 ALA A CA  
6701 C C   . ALA D 250 ? 1.2090 1.2715 1.1031 -0.1414 -0.0676 0.0442  253 ALA A C   
6702 O O   . ALA D 250 ? 1.2222 1.2857 1.1147 -0.1412 -0.0680 0.0450  253 ALA A O   
6703 C CB  . ALA D 250 ? 1.2140 1.2813 1.1151 -0.1490 -0.0761 0.0515  253 ALA A CB  
6704 N N   . PRO D 251 ? 1.3802 1.4362 1.2688 -0.1405 -0.0655 0.0383  254 PRO A N   
6705 C CA  . PRO D 251 ? 1.2623 1.3123 1.1425 -0.1393 -0.0634 0.0326  254 PRO A CA  
6706 C C   . PRO D 251 ? 1.2946 1.3422 1.1685 -0.1438 -0.0675 0.0313  254 PRO A C   
6707 O O   . PRO D 251 ? 1.5067 1.5544 1.3809 -0.1483 -0.0721 0.0329  254 PRO A O   
6708 C CB  . PRO D 251 ? 1.0805 1.1241 0.9572 -0.1386 -0.0616 0.0271  254 PRO A CB  
6709 C CG  . PRO D 251 ? 1.2344 1.2817 1.1185 -0.1382 -0.0615 0.0306  254 PRO A CG  
6710 C CD  . PRO D 251 ? 1.5097 1.5635 1.3998 -0.1411 -0.0654 0.0369  254 PRO A CD  
6711 N N   . GLU D 252 ? 1.2665 1.3121 1.1347 -0.1427 -0.0659 0.0287  255 GLU A N   
6712 C CA  . GLU D 252 ? 1.6180 1.6608 1.4782 -0.1469 -0.0690 0.0263  255 GLU A CA  
6713 C C   . GLU D 252 ? 1.7122 1.7494 1.5641 -0.1455 -0.0659 0.0196  255 GLU A C   
6714 O O   . GLU D 252 ? 1.9477 1.9804 1.7922 -0.1488 -0.0676 0.0146  255 GLU A O   
6715 C CB  . GLU D 252 ? 1.6950 1.7434 1.5575 -0.1482 -0.0713 0.0319  255 GLU A CB  
6716 C CG  . GLU D 252 ? 2.0840 2.1321 1.9415 -0.1544 -0.0767 0.0324  255 GLU A CG  
6717 C CD  . GLU D 252 ? 2.1255 2.1783 1.9838 -0.1559 -0.0789 0.0373  255 GLU A CD  
6718 O OE1 . GLU D 252 ? 1.8956 1.9522 1.7602 -0.1520 -0.0767 0.0410  255 GLU A OE1 
6719 O OE2 . GLU D 252 ? 2.1712 2.2238 2.0238 -0.1612 -0.0830 0.0374  255 GLU A OE2 
6720 N N   . TYR D 253 ? 1.5183 1.5557 1.3713 -0.1407 -0.0615 0.0192  256 TYR A N   
6721 C CA  . TYR D 253 ? 1.5112 1.5440 1.3571 -0.1390 -0.0585 0.0138  256 TYR A CA  
6722 C C   . TYR D 253 ? 1.4159 1.4458 1.2641 -0.1342 -0.0540 0.0112  256 TYR A C   
6723 O O   . TYR D 253 ? 1.3321 1.3652 1.1876 -0.1316 -0.0527 0.0146  256 TYR A O   
6724 C CB  . TYR D 253 ? 1.6694 1.7052 1.5145 -0.1378 -0.0580 0.0164  256 TYR A CB  
6725 C CG  . TYR D 253 ? 1.7012 1.7399 1.5436 -0.1430 -0.0627 0.0192  256 TYR A CG  
6726 C CD1 . TYR D 253 ? 1.5825 1.6184 1.4154 -0.1467 -0.0640 0.0150  256 TYR A CD1 
6727 C CD2 . TYR D 253 ? 1.7753 1.8198 1.6247 -0.1442 -0.0658 0.0260  256 TYR A CD2 
6728 C CE1 . TYR D 253 ? 1.6704 1.7092 1.5003 -0.1519 -0.0684 0.0175  256 TYR A CE1 
6729 C CE2 . TYR D 253 ? 1.8622 1.9093 1.7090 -0.1493 -0.0704 0.0289  256 TYR A CE2 
6730 C CZ  . TYR D 253 ? 1.8319 1.8760 1.6685 -0.1532 -0.0717 0.0246  256 TYR A CZ  
6731 O OH  . TYR D 253 ? 1.6725 1.7191 1.5053 -0.1588 -0.0763 0.0270  256 TYR A OH  
6732 N N   . ALA D 254 ? 1.2414 1.2656 1.0834 -0.1333 -0.0515 0.0051  257 ALA A N   
6733 C CA  . ALA D 254 ? 1.4887 1.5101 1.3329 -0.1291 -0.0475 0.0030  257 ALA A CA  
6734 C C   . ALA D 254 ? 1.4996 1.5163 1.3375 -0.1272 -0.0444 -0.0023 257 ALA A C   
6735 O O   . ALA D 254 ? 1.6097 1.6247 1.4409 -0.1297 -0.0454 -0.0052 257 ALA A O   
6736 C CB  . ALA D 254 ? 1.3800 1.3988 1.2266 -0.1304 -0.0485 0.0013  257 ALA A CB  
6737 N N   . TYR D 255 ? 1.2493 1.2641 1.0891 -0.1228 -0.0405 -0.0033 258 TYR A N   
6738 C CA  . TYR D 255 ? 1.2674 1.2779 1.1023 -0.1203 -0.0373 -0.0074 258 TYR A CA  
6739 C C   . TYR D 255 ? 1.4658 1.4701 1.2977 -0.1210 -0.0363 -0.0133 258 TYR A C   
6740 O O   . TYR D 255 ? 1.5536 1.5561 1.3895 -0.1191 -0.0349 -0.0136 258 TYR A O   
6741 C CB  . TYR D 255 ? 1.5739 1.5857 1.4128 -0.1152 -0.0338 -0.0053 258 TYR A CB  
6742 C CG  . TYR D 255 ? 1.5585 1.5749 1.3996 -0.1135 -0.0339 -0.0010 258 TYR A CG  
6743 C CD1 . TYR D 255 ? 1.7190 1.7343 1.5556 -0.1130 -0.0333 -0.0020 258 TYR A CD1 
6744 C CD2 . TYR D 255 ? 1.4518 1.4740 1.3002 -0.1124 -0.0346 0.0042  258 TYR A CD2 
6745 C CE1 . TYR D 255 ? 1.8569 1.8764 1.6966 -0.1115 -0.0339 0.0022  258 TYR A CE1 
6746 C CE2 . TYR D 255 ? 1.6673 1.6936 1.5190 -0.1106 -0.0350 0.0080  258 TYR A CE2 
6747 C CZ  . TYR D 255 ? 2.0164 2.0412 1.8639 -0.1102 -0.0348 0.0070  258 TYR A CZ  
6748 O OH  . TYR D 255 ? 2.2140 2.2427 2.0656 -0.1086 -0.0357 0.0111  258 TYR A OH  
6749 N N   . LYS D 256 ? 1.5259 1.5272 1.3514 -0.1236 -0.0372 -0.0181 259 LYS A N   
6750 C CA  . LYS D 256 ? 1.4923 1.4874 1.3153 -0.1234 -0.0356 -0.0244 259 LYS A CA  
6751 C C   . LYS D 256 ? 1.3333 1.3259 1.1558 -0.1190 -0.0314 -0.0256 259 LYS A C   
6752 O O   . LYS D 256 ? 1.4309 1.4246 1.2499 -0.1178 -0.0299 -0.0253 259 LYS A O   
6753 C CB  . LYS D 256 ? 1.3959 1.3890 1.2118 -0.1269 -0.0369 -0.0298 259 LYS A CB  
6754 C CG  . LYS D 256 ? 1.6474 1.6414 1.4630 -0.1315 -0.0412 -0.0304 259 LYS A CG  
6755 C CD  . LYS D 256 ? 1.7051 1.6972 1.5131 -0.1346 -0.0418 -0.0367 259 LYS A CD  
6756 C CE  . LYS D 256 ? 2.2254 2.2179 2.0325 -0.1393 -0.0463 -0.0379 259 LYS A CE  
6757 N NZ  . LYS D 256 ? 2.1321 2.1237 1.9311 -0.1425 -0.0467 -0.0442 259 LYS A NZ  
6758 N N   . ILE D 257 ? 1.4726 1.4619 1.2987 -0.1169 -0.0298 -0.0267 260 ILE A N   
6759 C CA  . ILE D 257 ? 1.5008 1.4860 1.3255 -0.1135 -0.0261 -0.0294 260 ILE A CA  
6760 C C   . ILE D 257 ? 1.4545 1.4356 1.2735 -0.1150 -0.0257 -0.0357 260 ILE A C   
6761 O O   . ILE D 257 ? 1.8251 1.8040 1.6435 -0.1180 -0.0277 -0.0395 260 ILE A O   
6762 C CB  . ILE D 257 ? 1.4964 1.4790 1.3263 -0.1117 -0.0251 -0.0290 260 ILE A CB  
6763 C CG1 . ILE D 257 ? 1.3914 1.3791 1.2265 -0.1098 -0.0248 -0.0230 260 ILE A CG1 
6764 C CG2 . ILE D 257 ? 1.4945 1.4722 1.3226 -0.1089 -0.0218 -0.0324 260 ILE A CG2 
6765 C CD1 . ILE D 257 ? 1.5409 1.5277 1.3812 -0.1092 -0.0245 -0.0217 260 ILE A CD1 
6766 N N   . VAL D 258 a 1.2993 1.2796 1.1144 -0.1130 -0.0230 -0.0371 260 VAL A N   
6767 C CA  . VAL D 258 a 1.5668 1.5442 1.3764 -0.1144 -0.0221 -0.0431 260 VAL A CA  
6768 C C   . VAL D 258 a 1.6738 1.6468 1.4832 -0.1110 -0.0186 -0.0456 260 VAL A C   
6769 O O   . VAL D 258 a 1.7910 1.7592 1.6018 -0.1108 -0.0179 -0.0499 260 VAL A O   
6770 C CB  . VAL D 258 a 1.5240 1.5058 1.3278 -0.1166 -0.0230 -0.0423 260 VAL A CB  
6771 C CG1 . VAL D 258 a 1.8193 1.7991 1.6170 -0.1178 -0.0215 -0.0485 260 VAL A CG1 
6772 C CG2 . VAL D 258 a 1.8244 1.8099 1.6282 -0.1205 -0.0269 -0.0403 260 VAL A CG2 
6773 N N   . LYS D 259 ? 1.5439 1.5183 1.3521 -0.1083 -0.0166 -0.0428 261 LYS A N   
6774 C CA  . LYS D 259 ? 1.4999 1.4703 1.3079 -0.1050 -0.0134 -0.0446 261 LYS A CA  
6775 C C   . LYS D 259 ? 1.6494 1.6196 1.4621 -0.1014 -0.0123 -0.0402 261 LYS A C   
6776 O O   . LYS D 259 ? 1.8568 1.8298 1.6695 -0.0995 -0.0118 -0.0364 261 LYS A O   
6777 C CB  . LYS D 259 ? 1.4889 1.4607 1.2914 -0.1049 -0.0121 -0.0454 261 LYS A CB  
6778 C CG  . LYS D 259 ? 1.5906 1.5628 1.3878 -0.1083 -0.0124 -0.0507 261 LYS A CG  
6779 C CD  . LYS D 259 ? 2.0055 1.9801 1.7973 -0.1085 -0.0111 -0.0508 261 LYS A CD  
6780 C CE  . LYS D 259 ? 2.0355 2.0113 1.8217 -0.1121 -0.0110 -0.0566 261 LYS A CE  
6781 N NZ  . LYS D 259 ? 2.1729 2.1521 1.9535 -0.1128 -0.0098 -0.0564 261 LYS A NZ  
6782 N N   . LYS D 260 ? 1.6569 1.6239 1.4738 -0.1007 -0.0120 -0.0408 262 LYS A N   
6783 C CA  . LYS D 260 ? 1.9453 1.9125 1.7664 -0.0977 -0.0108 -0.0371 262 LYS A CA  
6784 C C   . LYS D 260 ? 1.9817 1.9453 1.8014 -0.0943 -0.0079 -0.0379 262 LYS A C   
6785 O O   . LYS D 260 ? 1.7395 1.7004 1.5557 -0.0943 -0.0068 -0.0413 262 LYS A O   
6786 C CB  . LYS D 260 ? 1.7842 1.7495 1.6099 -0.0984 -0.0117 -0.0372 262 LYS A CB  
6787 C CG  . LYS D 260 ? 1.8603 1.8292 1.6889 -0.1014 -0.0147 -0.0352 262 LYS A CG  
6788 C CD  . LYS D 260 ? 1.8204 1.7871 1.6540 -0.1022 -0.0157 -0.0349 262 LYS A CD  
6789 C CE  . LYS D 260 ? 1.8769 1.8475 1.7139 -0.1053 -0.0190 -0.0324 262 LYS A CE  
6790 N NZ  . LYS D 260 ? 1.9529 1.9222 1.7953 -0.1066 -0.0206 -0.0314 262 LYS A NZ  
6791 N N   . GLY D 261 ? 1.9310 1.8950 1.7539 -0.0914 -0.0067 -0.0349 263 GLY A N   
6792 C CA  . GLY D 261 ? 1.6658 1.6264 1.4880 -0.0882 -0.0043 -0.0352 263 GLY A CA  
6793 C C   . GLY D 261 ? 1.9011 1.8641 1.7263 -0.0852 -0.0034 -0.0313 263 GLY A C   
6794 O O   . GLY D 261 ? 2.2076 2.1759 2.0352 -0.0854 -0.0044 -0.0282 263 GLY A O   
6795 N N   . ASP D 262 ? 1.8728 1.8321 1.6980 -0.0825 -0.0013 -0.0318 264 ASP A N   
6796 C CA  . ASP D 262 ? 1.8390 1.8002 1.6666 -0.0795 -0.0001 -0.0289 264 ASP A CA  
6797 C C   . ASP D 262 ? 1.8584 1.8242 1.6863 -0.0777 -0.0005 -0.0263 264 ASP A C   
6798 O O   . ASP D 262 ? 1.9850 1.9502 1.8104 -0.0773 -0.0008 -0.0266 264 ASP A O   
6799 C CB  . ASP D 262 ? 2.0195 1.9753 1.8461 -0.0771 0.0019  -0.0302 264 ASP A CB  
6800 C CG  . ASP D 262 ? 2.2875 2.2397 2.1104 -0.0763 0.0025  -0.0322 264 ASP A CG  
6801 O OD1 . ASP D 262 ? 2.0823 2.0330 1.9032 -0.0786 0.0018  -0.0347 264 ASP A OD1 
6802 O OD2 . ASP D 262 ? 2.6784 2.6296 2.5006 -0.0733 0.0035  -0.0312 264 ASP A OD2 
6803 N N   . SER D 263 ? 1.6418 1.6126 1.4736 -0.0767 -0.0005 -0.0235 265 SER A N   
6804 C CA  . SER D 263 ? 1.5706 1.5463 1.4044 -0.0749 -0.0011 -0.0208 265 SER A CA  
6805 C C   . SER D 263 ? 1.7359 1.7156 1.5740 -0.0726 0.0001  -0.0188 265 SER A C   
6806 O O   . SER D 263 ? 1.9420 1.9205 1.7806 -0.0726 0.0015  -0.0194 265 SER A O   
6807 C CB  . SER D 263 ? 1.5137 1.4934 1.3476 -0.0779 -0.0036 -0.0195 265 SER A CB  
6808 O OG  . SER D 263 ? 1.7292 1.7119 1.5656 -0.0804 -0.0046 -0.0186 265 SER A OG  
6809 N N   . THR D 264 ? 1.6141 1.5991 1.4557 -0.0709 -0.0004 -0.0164 266 THR A N   
6810 C CA  . THR D 264 ? 1.8143 1.8048 1.6607 -0.0691 0.0008  -0.0146 266 THR A CA  
6811 C C   . THR D 264 ? 1.8483 1.8449 1.6989 -0.0685 -0.0008 -0.0119 266 THR A C   
6812 O O   . THR D 264 ? 1.9046 1.9011 1.7542 -0.0703 -0.0031 -0.0112 266 THR A O   
6813 C CB  . THR D 264 ? 1.8595 1.8483 1.7060 -0.0651 0.0033  -0.0158 266 THR A CB  
6814 O OG1 . THR D 264 ? 2.0768 2.0717 1.9276 -0.0637 0.0048  -0.0145 266 THR A OG1 
6815 C CG2 . THR D 264 ? 1.6675 1.6552 1.5146 -0.0620 0.0029  -0.0158 266 THR A CG2 
6816 N N   . ILE D 265 ? 1.6436 1.6459 1.4994 -0.0660 0.0004  -0.0105 267 ILE A N   
6817 C CA  . ILE D 265 ? 1.8214 1.8299 1.6828 -0.0649 -0.0009 -0.0079 267 ILE A CA  
6818 C C   . ILE D 265 ? 1.8263 1.8362 1.6913 -0.0599 0.0009  -0.0085 267 ILE A C   
6819 O O   . ILE D 265 ? 1.9401 1.9538 1.8079 -0.0579 0.0033  -0.0089 267 ILE A O   
6820 C CB  . ILE D 265 ? 1.8410 1.8564 1.7065 -0.0672 -0.0015 -0.0054 267 ILE A CB  
6821 C CG1 . ILE D 265 ? 1.8234 1.8367 1.6854 -0.0721 -0.0040 -0.0050 267 ILE A CG1 
6822 C CG2 . ILE D 265 ? 2.2155 2.2378 2.0880 -0.0654 -0.0025 -0.0027 267 ILE A CG2 
6823 C CD1 . ILE D 265 ? 1.8870 1.9057 1.7522 -0.0749 -0.0048 -0.0027 267 ILE A CD1 
6824 N N   . MET D 266 ? 1.5537 1.5607 1.4188 -0.0580 -0.0003 -0.0087 268 MET A N   
6825 C CA  . MET D 266 ? 1.4848 1.4913 1.3529 -0.0532 0.0008  -0.0099 268 MET A CA  
6826 C C   . MET D 266 ? 1.5361 1.5499 1.4126 -0.0510 0.0002  -0.0079 268 MET A C   
6827 O O   . MET D 266 ? 1.7513 1.7685 1.6308 -0.0531 -0.0025 -0.0051 268 MET A O   
6828 C CB  . MET D 266 ? 1.4812 1.4816 1.3463 -0.0528 -0.0010 -0.0103 268 MET A CB  
6829 C CG  . MET D 266 ? 1.5439 1.5371 1.4011 -0.0547 -0.0002 -0.0124 268 MET A CG  
6830 S SD  . MET D 266 ? 2.1181 2.1069 1.9720 -0.0525 0.0032  -0.0156 268 MET A SD  
6831 C CE  . MET D 266 ? 1.4447 1.4311 1.3013 -0.0476 0.0029  -0.0163 268 MET A CE  
6832 N N   . LYS D 267 ? 1.4622 1.4787 1.3428 -0.0468 0.0025  -0.0096 269 LYS A N   
6833 C CA  . LYS D 267 ? 1.4683 1.4926 1.3579 -0.0443 0.0024  -0.0082 269 LYS A CA  
6834 C C   . LYS D 267 ? 1.3558 1.3788 1.2501 -0.0392 0.0022  -0.0099 269 LYS A C   
6835 O O   . LYS D 267 ? 1.5262 1.5523 1.4241 -0.0354 0.0048  -0.0123 269 LYS A O   
6836 C CB  . LYS D 267 ? 1.5460 1.5771 1.4377 -0.0441 0.0056  -0.0087 269 LYS A CB  
6837 C CG  . LYS D 267 ? 1.9140 1.9476 1.8033 -0.0491 0.0050  -0.0063 269 LYS A CG  
6838 C CD  . LYS D 267 ? 2.0363 2.0771 1.9280 -0.0489 0.0080  -0.0063 269 LYS A CD  
6839 C CE  . LYS D 267 ? 1.9358 1.9790 1.8259 -0.0540 0.0069  -0.0036 269 LYS A CE  
6840 N NZ  . LYS D 267 ? 1.6587 1.7096 1.5513 -0.0542 0.0096  -0.0030 269 LYS A NZ  
6841 N N   . SER D 268 ? 1.3434 1.3622 1.2379 -0.0394 -0.0011 -0.0086 270 SER A N   
6842 C CA  . SER D 268 ? 1.4453 1.4628 1.3455 -0.0350 -0.0024 -0.0094 270 SER A CA  
6843 C C   . SER D 268 ? 1.6616 1.6799 1.5665 -0.0365 -0.0070 -0.0056 270 SER A C   
6844 O O   . SER D 268 ? 1.7859 1.8050 1.6880 -0.0411 -0.0090 -0.0026 270 SER A O   
6845 C CB  . SER D 268 ? 1.4710 1.4804 1.3655 -0.0332 -0.0017 -0.0122 270 SER A CB  
6846 O OG  . SER D 268 ? 1.5808 1.5845 1.4685 -0.0368 -0.0037 -0.0108 270 SER A OG  
6847 N N   . GLU D 269 ? 1.7515 1.7697 1.6637 -0.0328 -0.0090 -0.0056 271 GLU A N   
6848 C CA  . GLU D 269 ? 1.8898 1.9092 1.8082 -0.0338 -0.0139 -0.0016 271 GLU A CA  
6849 C C   . GLU D 269 ? 1.7544 1.7668 1.6711 -0.0327 -0.0165 -0.0016 271 GLU A C   
6850 O O   . GLU D 269 ? 1.6865 1.6982 1.6103 -0.0283 -0.0176 -0.0027 271 GLU A O   
6851 C CB  . GLU D 269 ? 1.9341 1.9603 1.8650 -0.0303 -0.0146 -0.0010 271 GLU A CB  
6852 C CG  . GLU D 269 ? 1.9209 1.9550 1.8549 -0.0316 -0.0126 0.0000  271 GLU A CG  
6853 C CD  . GLU D 269 ? 1.9082 1.9492 1.8554 -0.0276 -0.0130 0.0002  271 GLU A CD  
6854 O OE1 . GLU D 269 ? 1.9009 1.9401 1.8546 -0.0233 -0.0143 -0.0014 271 GLU A OE1 
6855 O OE2 . GLU D 269 ? 1.6992 1.7474 1.6508 -0.0287 -0.0122 0.0019  271 GLU A OE2 
6856 N N   . LEU D 270 ? 1.7203 1.7280 1.6281 -0.0367 -0.0175 -0.0004 272 LEU A N   
6857 C CA  . LEU D 270 ? 2.0675 2.0688 1.9727 -0.0360 -0.0196 -0.0004 272 LEU A CA  
6858 C C   . LEU D 270 ? 1.9985 1.9986 1.8988 -0.0413 -0.0229 0.0035  272 LEU A C   
6859 O O   . LEU D 270 ? 1.8517 1.8540 1.7470 -0.0456 -0.0224 0.0045  272 LEU A O   
6860 C CB  . LEU D 270 ? 1.9722 1.9676 1.8699 -0.0343 -0.0158 -0.0046 272 LEU A CB  
6861 C CG  . LEU D 270 ? 1.8215 1.8178 1.7234 -0.0290 -0.0127 -0.0086 272 LEU A CG  
6862 C CD1 . LEU D 270 ? 1.7271 1.7180 1.6207 -0.0285 -0.0092 -0.0122 272 LEU A CD1 
6863 C CD2 . LEU D 270 ? 2.0368 2.0323 1.9477 -0.0245 -0.0155 -0.0088 272 LEU A CD2 
6864 N N   . GLU D 271 ? 1.9528 1.9496 1.8544 -0.0411 -0.0264 0.0054  273 GLU A N   
6865 C CA  . GLU D 271 ? 1.9180 1.9149 1.8163 -0.0460 -0.0302 0.0096  273 GLU A CA  
6866 C C   . GLU D 271 ? 1.8054 1.7975 1.6924 -0.0488 -0.0284 0.0080  273 GLU A C   
6867 O O   . GLU D 271 ? 1.8555 1.8431 1.7378 -0.0466 -0.0247 0.0041  273 GLU A O   
6868 C CB  . GLU D 271 ? 2.2181 2.2145 2.1240 -0.0447 -0.0353 0.0131  273 GLU A CB  
6869 C CG  . GLU D 271 ? 2.4797 2.4813 2.3980 -0.0428 -0.0382 0.0155  273 GLU A CG  
6870 C CD  . GLU D 271 ? 2.8197 2.8202 2.7464 -0.0414 -0.0437 0.0189  273 GLU A CD  
6871 O OE1 . GLU D 271 ? 2.8325 2.8278 2.7554 -0.0413 -0.0448 0.0189  273 GLU A OE1 
6872 O OE2 . GLU D 271 ? 2.9380 2.9427 2.8754 -0.0406 -0.0471 0.0217  273 GLU A OE2 
6873 N N   . TYR D 272 ? 1.5438 1.5370 1.4265 -0.0538 -0.0310 0.0112  274 TYR A N   
6874 C CA  . TYR D 272 ? 1.4816 1.4711 1.3542 -0.0568 -0.0297 0.0101  274 TYR A CA  
6875 C C   . TYR D 272 ? 1.4496 1.4336 1.3217 -0.0543 -0.0303 0.0096  274 TYR A C   
6876 O O   . TYR D 272 ? 1.4204 1.4039 1.3001 -0.0512 -0.0332 0.0114  274 TYR A O   
6877 C CB  . TYR D 272 ? 1.7795 1.7725 1.6483 -0.0628 -0.0327 0.0137  274 TYR A CB  
6878 C CG  . TYR D 272 ? 2.0040 2.0018 1.8714 -0.0663 -0.0324 0.0141  274 TYR A CG  
6879 C CD1 . TYR D 272 ? 1.9599 1.9568 1.8190 -0.0690 -0.0292 0.0109  274 TYR A CD1 
6880 C CD2 . TYR D 272 ? 2.0643 2.0674 1.9393 -0.0670 -0.0355 0.0177  274 TYR A CD2 
6881 C CE1 . TYR D 272 ? 2.2451 2.2461 2.1032 -0.0723 -0.0292 0.0113  274 TYR A CE1 
6882 C CE2 . TYR D 272 ? 2.1614 2.1689 2.0353 -0.0703 -0.0355 0.0184  274 TYR A CE2 
6883 C CZ  . TYR D 272 ? 2.3755 2.3818 2.2408 -0.0730 -0.0324 0.0151  274 TYR A CZ  
6884 O OH  . TYR D 272 ? 2.1799 2.1902 2.0444 -0.0764 -0.0327 0.0158  274 TYR A OH  
6885 N N   . GLY D 273 ? 1.7449 1.7248 1.6085 -0.0556 -0.0278 0.0073  275 GLY A N   
6886 C CA  . GLY D 273 ? 1.7978 1.7729 1.6596 -0.0544 -0.0286 0.0075  275 GLY A CA  
6887 C C   . GLY D 273 ? 1.9269 1.9028 1.7820 -0.0594 -0.0299 0.0096  275 GLY A C   
6888 O O   . GLY D 273 ? 2.0245 2.0051 1.8770 -0.0639 -0.0309 0.0113  275 GLY A O   
6889 N N   . ASN D 274 ? 2.0932 2.0648 1.9454 -0.0587 -0.0299 0.0094  276 ASN A N   
6890 C CA  . ASN D 274 ? 2.3480 2.3208 2.1940 -0.0633 -0.0309 0.0114  276 ASN A CA  
6891 C C   . ASN D 274 ? 2.4294 2.3971 2.2688 -0.0629 -0.0276 0.0082  276 ASN A C   
6892 O O   . ASN D 274 ? 2.3890 2.3576 2.2239 -0.0661 -0.0284 0.0097  276 ASN A O   
6893 C CB  . ASN D 274 ? 2.2523 2.2271 2.1031 -0.0644 -0.0364 0.0170  276 ASN A CB  
6894 C CG  . ASN D 274 ? 2.3037 2.2847 2.1597 -0.0668 -0.0403 0.0212  276 ASN A CG  
6895 O OD1 . ASN D 274 ? 2.4292 2.4139 2.2829 -0.0693 -0.0391 0.0203  276 ASN A OD1 
6896 N ND2 . ASN D 274 ? 2.4120 2.3940 2.2755 -0.0661 -0.0454 0.0259  276 ASN A ND2 
6897 N N   . CYS D 275 ? 2.6949 2.6578 2.5337 -0.0593 -0.0240 0.0039  277 CYS A N   
6898 C CA  . CYS D 275 ? 2.6886 2.6463 2.5219 -0.0588 -0.0210 0.0011  277 CYS A CA  
6899 C C   . CYS D 275 ? 2.5853 2.5427 2.4134 -0.0604 -0.0168 -0.0032 277 CYS A C   
6900 O O   . CYS D 275 ? 2.5290 2.4909 2.3560 -0.0632 -0.0167 -0.0034 277 CYS A O   
6901 C CB  . CYS D 275 ? 2.5959 2.5477 2.4329 -0.0537 -0.0209 0.0001  277 CYS A CB  
6902 S SG  . CYS D 275 ? 3.1053 3.0565 2.9489 -0.0519 -0.0263 0.0050  277 CYS A SG  
6903 N N   . ASN D 276 ? 2.6836 2.6356 2.5087 -0.0586 -0.0137 -0.0066 278 ASN A N   
6904 C CA  . ASN D 276 ? 2.6634 2.6142 2.4844 -0.0598 -0.0100 -0.0106 278 ASN A CA  
6905 C C   . ASN D 276 ? 2.7645 2.7098 2.5868 -0.0559 -0.0077 -0.0132 278 ASN A C   
6906 O O   . ASN D 276 ? 2.7985 2.7389 2.6198 -0.0543 -0.0072 -0.0136 278 ASN A O   
6907 C CB  . ASN D 276 ? 2.4694 2.4195 2.2847 -0.0630 -0.0086 -0.0121 278 ASN A CB  
6908 C CG  . ASN D 276 ? 2.3169 2.2731 2.1296 -0.0675 -0.0102 -0.0103 278 ASN A CG  
6909 O OD1 . ASN D 276 ? 2.6452 2.6060 2.4597 -0.0689 -0.0119 -0.0088 278 ASN A OD1 
6910 N ND2 . ASN D 276 ? 1.8605 1.8171 1.6690 -0.0699 -0.0098 -0.0106 278 ASN A ND2 
6911 N N   . THR D 277 ? 2.6710 2.6175 2.4956 -0.0547 -0.0065 -0.0146 279 THR A N   
6912 C CA  . THR D 277 ? 2.5481 2.4903 2.3737 -0.0513 -0.0044 -0.0168 279 THR A CA  
6913 C C   . THR D 277 ? 2.3844 2.3251 2.2068 -0.0529 -0.0013 -0.0200 279 THR A C   
6914 O O   . THR D 277 ? 2.1480 2.0913 1.9683 -0.0562 -0.0009 -0.0207 279 THR A O   
6915 C CB  . THR D 277 ? 2.5210 2.4657 2.3521 -0.0482 -0.0051 -0.0162 279 THR A CB  
6916 O OG1 . THR D 277 ? 2.5508 2.5014 2.3834 -0.0502 -0.0052 -0.0157 279 THR A OG1 
6917 C CG2 . THR D 277 ? 2.7340 2.6788 2.5693 -0.0460 -0.0083 -0.0135 279 THR A CG2 
6918 N N   . THR D 278 ? 2.1579 2.0943 1.9803 -0.0505 0.0005  -0.0217 280 THR A N   
6919 C CA  . THR D 278 ? 1.9587 1.8924 1.7786 -0.0517 0.0030  -0.0243 280 THR A CA  
6920 C C   . THR D 278 ? 2.0068 1.9435 1.8288 -0.0514 0.0042  -0.0251 280 THR A C   
6921 O O   . THR D 278 ? 2.1497 2.0859 1.9703 -0.0535 0.0056  -0.0266 280 THR A O   
6922 C CB  . THR D 278 ? 1.8406 1.7677 1.6591 -0.0498 0.0039  -0.0253 280 THR A CB  
6923 O OG1 . THR D 278 ? 1.8529 1.7791 1.6739 -0.0461 0.0035  -0.0248 280 THR A OG1 
6924 C CG2 . THR D 278 ? 1.6947 1.6192 1.5113 -0.0504 0.0029  -0.0244 280 THR A CG2 
6925 N N   . CYS D 279 ? 2.1483 2.0881 1.9739 -0.0488 0.0036  -0.0240 281 CYS A N   
6926 C CA  . CYS D 279 ? 1.8875 1.8311 1.7154 -0.0484 0.0049  -0.0245 281 CYS A CA  
6927 C C   . CYS D 279 ? 2.0218 1.9708 1.8544 -0.0465 0.0034  -0.0229 281 CYS A C   
6928 O O   . CYS D 279 ? 2.1860 2.1343 2.0207 -0.0443 0.0017  -0.0217 281 CYS A O   
6929 C CB  . CYS D 279 ? 1.5937 1.5340 1.4210 -0.0462 0.0068  -0.0261 281 CYS A CB  
6930 S SG  . CYS D 279 ? 2.3115 2.2576 2.1415 -0.0455 0.0085  -0.0265 281 CYS A SG  
6931 N N   . GLN D 280 ? 1.8396 1.7942 1.6746 -0.0475 0.0040  -0.0225 282 GLN A N   
6932 C CA  . GLN D 280 ? 1.6230 1.5834 1.4634 -0.0460 0.0026  -0.0208 282 GLN A CA  
6933 C C   . GLN D 280 ? 1.6548 1.6198 1.4983 -0.0445 0.0045  -0.0215 282 GLN A C   
6934 O O   . GLN D 280 ? 1.6770 1.6434 1.5188 -0.0468 0.0061  -0.0220 282 GLN A O   
6935 C CB  . GLN D 280 ? 1.5286 1.4929 1.3695 -0.0493 0.0005  -0.0187 282 GLN A CB  
6936 C CG  . GLN D 280 ? 1.5994 1.5690 1.4465 -0.0476 -0.0014 -0.0165 282 GLN A CG  
6937 C CD  . GLN D 280 ? 1.6443 1.6113 1.4933 -0.0453 -0.0036 -0.0154 282 GLN A CD  
6938 O OE1 . GLN D 280 ? 1.6572 1.6240 1.5105 -0.0413 -0.0036 -0.0160 282 GLN A OE1 
6939 N NE2 . GLN D 280 ? 1.9330 1.8986 1.7793 -0.0479 -0.0057 -0.0138 282 GLN A NE2 
6940 N N   . THR D 281 ? 1.5279 1.4954 1.3763 -0.0408 0.0043  -0.0216 283 THR A N   
6941 C CA  . THR D 281 ? 1.4662 1.4394 1.3185 -0.0389 0.0062  -0.0223 283 THR A CA  
6942 C C   . THR D 281 ? 1.7648 1.7444 1.6241 -0.0379 0.0044  -0.0204 283 THR A C   
6943 O O   . THR D 281 ? 1.6705 1.6491 1.5316 -0.0380 0.0015  -0.0186 283 THR A O   
6944 C CB  . THR D 281 ? 1.2857 1.2566 1.1383 -0.0349 0.0079  -0.0249 283 THR A CB  
6945 O OG1 . THR D 281 ? 1.7449 1.7131 1.6006 -0.0318 0.0057  -0.0248 283 THR A OG1 
6946 C CG2 . THR D 281 ? 1.5454 1.5100 1.3916 -0.0361 0.0094  -0.0264 283 THR A CG2 
6947 N N   . PRO D 282 ? 1.8130 1.7996 1.6765 -0.0374 0.0059  -0.0203 284 PRO A N   
6948 C CA  . PRO D 282 ? 1.9188 1.9115 1.7899 -0.0361 0.0041  -0.0184 284 PRO A CA  
6949 C C   . PRO D 282 ? 1.9499 1.9406 1.8257 -0.0319 0.0024  -0.0190 284 PRO A C   
6950 O O   . PRO D 282 ? 2.1026 2.0949 1.9834 -0.0317 -0.0007 -0.0167 284 PRO A O   
6951 C CB  . PRO D 282 ? 1.7216 1.7215 1.5961 -0.0352 0.0068  -0.0191 284 PRO A CB  
6952 C CG  . PRO D 282 ? 1.7781 1.7768 1.6463 -0.0387 0.0087  -0.0194 284 PRO A CG  
6953 C CD  . PRO D 282 ? 1.8088 1.7987 1.6705 -0.0387 0.0088  -0.0212 284 PRO A CD  
6954 N N   . LYS D 283 ? 1.6846 1.6715 1.5588 -0.0286 0.0041  -0.0221 285 LYS A N   
6955 C CA  . LYS D 283 ? 1.6314 1.6161 1.5105 -0.0243 0.0025  -0.0233 285 LYS A CA  
6956 C C   . LYS D 283 ? 1.5454 1.5237 1.4225 -0.0254 -0.0010 -0.0213 285 LYS A C   
6957 O O   . LYS D 283 ? 1.7577 1.7363 1.6408 -0.0237 -0.0043 -0.0197 285 LYS A O   
6958 C CB  . LYS D 283 ? 1.8937 1.8759 1.7707 -0.0210 0.0054  -0.0273 285 LYS A CB  
6959 C CG  . LYS D 283 ? 2.0550 2.0447 1.9347 -0.0195 0.0089  -0.0294 285 LYS A CG  
6960 C CD  . LYS D 283 ? 2.1412 2.1288 2.0180 -0.0167 0.0117  -0.0335 285 LYS A CD  
6961 C CE  . LYS D 283 ? 2.0266 2.0226 1.9058 -0.0155 0.0153  -0.0356 285 LYS A CE  
6962 N NZ  . LYS D 283 ? 2.0570 2.0513 1.9326 -0.0131 0.0180  -0.0397 285 LYS A NZ  
6963 N N   . GLY D 284 ? 1.6510 1.6240 1.5202 -0.0283 -0.0005 -0.0211 286 GLY A N   
6964 C CA  . GLY D 284 ? 1.4148 1.3826 1.2818 -0.0296 -0.0036 -0.0191 286 GLY A CA  
6965 C C   . GLY D 284 ? 1.5346 1.4966 1.3931 -0.0322 -0.0021 -0.0200 286 GLY A C   
6966 O O   . GLY D 284 ? 1.7820 1.7434 1.6365 -0.0328 0.0009  -0.0221 286 GLY A O   
6967 N N   . ALA D 285 ? 1.5281 1.4863 1.3843 -0.0338 -0.0046 -0.0181 287 ALA A N   
6968 C CA  . ALA D 285 ? 1.6749 1.6281 1.5238 -0.0365 -0.0036 -0.0186 287 ALA A CA  
6969 C C   . ALA D 285 ? 1.6899 1.6365 1.5365 -0.0338 -0.0027 -0.0207 287 ALA A C   
6970 O O   . ALA D 285 ? 1.7612 1.7064 1.6117 -0.0300 -0.0038 -0.0213 287 ALA A O   
6971 C CB  . ALA D 285 ? 1.8708 1.8235 1.7180 -0.0396 -0.0064 -0.0158 287 ALA A CB  
6972 N N   . ILE D 286 ? 1.6574 1.5999 1.4980 -0.0358 -0.0008 -0.0219 288 ILE A N   
6973 C CA  . ILE D 286 ? 1.5970 1.5334 1.4349 -0.0338 0.0005  -0.0239 288 ILE A CA  
6974 C C   . ILE D 286 ? 1.7332 1.6646 1.5657 -0.0366 0.0006  -0.0235 288 ILE A C   
6975 O O   . ILE D 286 ? 1.9015 1.8346 1.7315 -0.0401 0.0013  -0.0232 288 ILE A O   
6976 C CB  . ILE D 286 ? 1.7821 1.7198 1.6189 -0.0332 0.0037  -0.0263 288 ILE A CB  
6977 C CG1 . ILE D 286 ? 2.0207 1.9639 1.8630 -0.0302 0.0039  -0.0271 288 ILE A CG1 
6978 C CG2 . ILE D 286 ? 2.0815 2.0129 1.9148 -0.0318 0.0048  -0.0282 288 ILE A CG2 
6979 C CD1 . ILE D 286 ? 2.1159 2.0629 1.9576 -0.0304 0.0069  -0.0288 288 ILE A CD1 
6980 N N   . ASN D 287 ? 2.0327 1.9581 1.8639 -0.0349 -0.0001 -0.0236 289 ASN A N   
6981 C CA  . ASN D 287 ? 2.0419 1.9629 1.8690 -0.0372 -0.0002 -0.0231 289 ASN A CA  
6982 C C   . ASN D 287 ? 2.1338 2.0485 1.9578 -0.0363 0.0014  -0.0248 289 ASN A C   
6983 O O   . ASN D 287 ? 2.2453 2.1557 2.0667 -0.0375 0.0011  -0.0243 289 ASN A O   
6984 C CB  . ASN D 287 ? 1.8915 1.8114 1.7199 -0.0370 -0.0033 -0.0204 289 ASN A CB  
6985 C CG  . ASN D 287 ? 1.9714 1.8870 1.8023 -0.0331 -0.0052 -0.0203 289 ASN A CG  
6986 O OD1 . ASN D 287 ? 1.9883 1.9049 1.8227 -0.0300 -0.0053 -0.0215 289 ASN A OD1 
6987 N ND2 . ASN D 287 ? 1.8115 1.7223 1.6409 -0.0332 -0.0066 -0.0189 289 ASN A ND2 
6988 N N   . THR D 288 ? 2.1706 2.0851 1.9948 -0.0345 0.0030  -0.0268 290 THR A N   
6989 C CA  . THR D 288 ? 1.9068 1.8152 1.7290 -0.0328 0.0036  -0.0280 290 THR A CA  
6990 C C   . THR D 288 ? 1.8688 1.7759 1.6878 -0.0349 0.0061  -0.0294 290 THR A C   
6991 O O   . THR D 288 ? 1.9714 1.8831 1.7906 -0.0365 0.0077  -0.0300 290 THR A O   
6992 C CB  . THR D 288 ? 1.9670 1.8759 1.7922 -0.0287 0.0029  -0.0292 290 THR A CB  
6993 O OG1 . THR D 288 ? 2.0706 1.9857 1.8975 -0.0284 0.0047  -0.0305 290 THR A OG1 
6994 C CG2 . THR D 288 ? 2.0428 1.9522 1.8721 -0.0268 -0.0003 -0.0274 290 THR A CG2 
6995 N N   . SER D 289 ? 1.9294 1.8301 1.7458 -0.0349 0.0062  -0.0297 291 SER A N   
6996 C CA  . SER D 289 ? 2.1161 2.0143 1.9298 -0.0375 0.0079  -0.0303 291 SER A CA  
6997 C C   . SER D 289 ? 2.2139 2.1120 2.0264 -0.0369 0.0094  -0.0317 291 SER A C   
6998 O O   . SER D 289 ? 2.1189 2.0145 1.9294 -0.0392 0.0104  -0.0318 291 SER A O   
6999 C CB  . SER D 289 ? 2.1065 1.9979 1.9183 -0.0383 0.0072  -0.0295 291 SER A CB  
7000 O OG  . SER D 289 ? 2.0260 1.9126 1.8374 -0.0356 0.0060  -0.0295 291 SER A OG  
7001 N N   . LEU D 290 ? 2.1051 2.0061 1.9189 -0.0340 0.0095  -0.0328 292 LEU A N   
7002 C CA  . LEU D 290 ? 1.7867 1.6885 1.5988 -0.0336 0.0111  -0.0343 292 LEU A CA  
7003 C C   . LEU D 290 ? 1.6361 1.5435 1.4483 -0.0367 0.0129  -0.0341 292 LEU A C   
7004 O O   . LEU D 290 ? 1.8816 1.7943 1.6961 -0.0375 0.0130  -0.0335 292 LEU A O   
7005 C CB  . LEU D 290 ? 1.6132 1.5174 1.4271 -0.0296 0.0110  -0.0361 292 LEU A CB  
7006 C CG  . LEU D 290 ? 1.6760 1.5739 1.4901 -0.0266 0.0087  -0.0363 292 LEU A CG  
7007 C CD1 . LEU D 290 ? 1.5779 1.4779 1.3948 -0.0223 0.0081  -0.0385 292 LEU A CD1 
7008 C CD2 . LEU D 290 ? 1.6132 1.5038 1.4231 -0.0276 0.0086  -0.0363 292 LEU A CD2 
7009 N N   . PRO D 291 ? 1.5446 1.4509 1.3542 -0.0387 0.0140  -0.0342 293 PRO A N   
7010 C CA  . PRO D 291 ? 1.5370 1.4470 1.3469 -0.0426 0.0150  -0.0332 293 PRO A CA  
7011 C C   . PRO D 291 ? 1.5557 1.4746 1.3678 -0.0426 0.0163  -0.0334 293 PRO A C   
7012 O O   . PRO D 291 ? 1.7331 1.6554 1.5463 -0.0457 0.0165  -0.0323 293 PRO A O   
7013 C CB  . PRO D 291 ? 1.5187 1.4252 1.3257 -0.0446 0.0154  -0.0330 293 PRO A CB  
7014 C CG  . PRO D 291 ? 1.7059 1.6050 1.5110 -0.0424 0.0143  -0.0334 293 PRO A CG  
7015 C CD  . PRO D 291 ? 1.7294 1.6303 1.5360 -0.0382 0.0139  -0.0348 293 PRO A CD  
7016 N N   . PHE D 292 ? 1.3721 1.2950 1.1854 -0.0392 0.0169  -0.0348 294 PHE A N   
7017 C CA  . PHE D 292 ? 1.3980 1.3298 1.2136 -0.0392 0.0184  -0.0350 294 PHE A CA  
7018 C C   . PHE D 292 ? 1.5292 1.4645 1.3486 -0.0353 0.0180  -0.0361 294 PHE A C   
7019 O O   . PHE D 292 ? 1.5880 1.5188 1.4078 -0.0323 0.0167  -0.0371 294 PHE A O   
7020 C CB  . PHE D 292 ? 1.3331 1.2683 1.1466 -0.0397 0.0203  -0.0359 294 PHE A CB  
7021 C CG  . PHE D 292 ? 1.5518 1.4831 1.3619 -0.0436 0.0202  -0.0345 294 PHE A CG  
7022 C CD1 . PHE D 292 ? 1.6852 1.6182 1.4963 -0.0477 0.0198  -0.0323 294 PHE A CD1 
7023 C CD2 . PHE D 292 ? 1.7513 1.6771 1.5578 -0.0432 0.0201  -0.0353 294 PHE A CD2 
7024 C CE1 . PHE D 292 ? 1.9210 1.8502 1.7301 -0.0514 0.0193  -0.0309 294 PHE A CE1 
7025 C CE2 . PHE D 292 ? 1.8592 1.7813 1.6632 -0.0469 0.0196  -0.0337 294 PHE A CE2 
7026 C CZ  . PHE D 292 ? 1.9019 1.8258 1.7076 -0.0510 0.0191  -0.0314 294 PHE A CZ  
7027 N N   . GLN D 293 ? 1.4699 1.4133 1.2927 -0.0354 0.0189  -0.0358 295 GLN A N   
7028 C CA  . GLN D 293 ? 1.2666 1.2143 1.0941 -0.0321 0.0185  -0.0365 295 GLN A CA  
7029 C C   . GLN D 293 ? 1.1541 1.1106 0.9841 -0.0307 0.0208  -0.0378 295 GLN A C   
7030 O O   . GLN D 293 ? 1.3699 1.3311 1.1986 -0.0334 0.0225  -0.0371 295 GLN A O   
7031 C CB  . GLN D 293 ? 1.4951 1.4447 1.3255 -0.0336 0.0168  -0.0343 295 GLN A CB  
7032 C CG  . GLN D 293 ? 2.1949 2.1373 2.0237 -0.0344 0.0146  -0.0332 295 GLN A CG  
7033 C CD  . GLN D 293 ? 2.5664 2.5112 2.3972 -0.0364 0.0131  -0.0312 295 GLN A CD  
7034 O OE1 . GLN D 293 ? 2.7794 2.7301 2.6119 -0.0385 0.0137  -0.0303 295 GLN A OE1 
7035 N NE2 . GLN D 293 ? 2.7635 2.7040 2.5941 -0.0362 0.0110  -0.0304 295 GLN A NE2 
7036 N N   . ASN D 294 ? 1.1216 1.0806 0.9558 -0.0265 0.0206  -0.0397 296 ASN A N   
7037 C CA  . ASN D 294 ? 1.2018 1.1701 1.0399 -0.0245 0.0228  -0.0413 296 ASN A CA  
7038 C C   . ASN D 294 ? 1.3442 1.3178 1.1890 -0.0233 0.0217  -0.0401 296 ASN A C   
7039 O O   . ASN D 294 ? 1.3950 1.3766 1.2443 -0.0214 0.0234  -0.0413 296 ASN A O   
7040 C CB  . ASN D 294 ? 1.1928 1.1602 1.0311 -0.0201 0.0238  -0.0453 296 ASN A CB  
7041 C CG  . ASN D 294 ? 1.3962 1.3604 1.2279 -0.0215 0.0253  -0.0466 296 ASN A CG  
7042 O OD1 . ASN D 294 ? 1.7275 1.6927 1.5554 -0.0257 0.0262  -0.0446 296 ASN A OD1 
7043 N ND2 . ASN D 294 ? 1.2865 1.2467 1.1171 -0.0181 0.0251  -0.0498 296 ASN A ND2 
7044 N N   . ILE D 295 ? 1.2699 1.2396 1.1156 -0.0246 0.0190  -0.0376 297 ILE A N   
7045 C CA  . ILE D 295 ? 1.4977 1.4709 1.3499 -0.0230 0.0171  -0.0365 297 ILE A CA  
7046 C C   . ILE D 295 ? 1.4508 1.4322 1.3059 -0.0256 0.0179  -0.0343 297 ILE A C   
7047 O O   . ILE D 295 ? 1.3856 1.3744 1.2466 -0.0234 0.0188  -0.0349 297 ILE A O   
7048 C CB  . ILE D 295 ? 1.5397 1.5060 1.3914 -0.0236 0.0137  -0.0345 297 ILE A CB  
7049 C CG1 . ILE D 295 ? 1.7170 1.6765 1.5678 -0.0202 0.0127  -0.0367 297 ILE A CG1 
7050 C CG2 . ILE D 295 ? 1.6950 1.6653 1.5527 -0.0235 0.0114  -0.0323 297 ILE A CG2 
7051 C CD1 . ILE D 295 ? 1.8224 1.7747 1.6715 -0.0210 0.0097  -0.0348 297 ILE A CD1 
7052 N N   . HIS D 296 ? 1.5047 1.4851 1.3561 -0.0301 0.0176  -0.0320 298 HIS A N   
7053 C CA  . HIS D 296 ? 1.4686 1.4567 1.3226 -0.0327 0.0182  -0.0299 298 HIS A CA  
7054 C C   . HIS D 296 ? 1.5879 1.5737 1.4367 -0.0375 0.0184  -0.0285 298 HIS A C   
7055 O O   . HIS D 296 ? 1.6901 1.6685 1.5349 -0.0391 0.0171  -0.0282 298 HIS A O   
7056 C CB  . HIS D 296 ? 1.4803 1.4708 1.3393 -0.0329 0.0157  -0.0277 298 HIS A CB  
7057 C CG  . HIS D 296 ? 1.5044 1.5040 1.3679 -0.0343 0.0163  -0.0259 298 HIS A CG  
7058 N ND1 . HIS D 296 ? 1.5808 1.5821 1.4426 -0.0388 0.0158  -0.0234 298 HIS A ND1 
7059 C CD2 . HIS D 296 ? 1.6120 1.6196 1.4822 -0.0317 0.0174  -0.0262 298 HIS A CD2 
7060 C CE1 . HIS D 296 ? 1.6380 1.6480 1.5050 -0.0391 0.0163  -0.0220 298 HIS A CE1 
7061 N NE2 . HIS D 296 ? 1.6724 1.6865 1.5446 -0.0348 0.0174  -0.0236 298 HIS A NE2 
7062 N N   . PRO D 297 ? 1.6054 1.5977 1.4548 -0.0398 0.0200  -0.0274 299 PRO A N   
7063 C CA  . PRO D 297 ? 1.5167 1.5067 1.3621 -0.0445 0.0197  -0.0258 299 PRO A CA  
7064 C C   . PRO D 297 ? 1.3910 1.3780 1.2363 -0.0474 0.0170  -0.0240 299 PRO A C   
7065 O O   . PRO D 297 ? 1.3973 1.3780 1.2387 -0.0500 0.0162  -0.0240 299 PRO A O   
7066 C CB  . PRO D 297 ? 1.5347 1.5339 1.3824 -0.0463 0.0214  -0.0245 299 PRO A CB  
7067 C CG  . PRO D 297 ? 1.5355 1.5423 1.3891 -0.0427 0.0224  -0.0251 299 PRO A CG  
7068 C CD  . PRO D 297 ? 1.5354 1.5371 1.3888 -0.0382 0.0223  -0.0279 299 PRO A CD  
7069 N N   . ILE D 298 ? 1.2794 1.2707 1.1290 -0.0470 0.0157  -0.0227 300 ILE A N   
7070 C CA  . ILE D 298 ? 1.2817 1.2714 1.1310 -0.0500 0.0132  -0.0210 300 ILE A CA  
7071 C C   . ILE D 298 ? 1.1704 1.1524 1.0168 -0.0490 0.0117  -0.0220 300 ILE A C   
7072 O O   . ILE D 298 ? 1.4007 1.3825 1.2495 -0.0459 0.0110  -0.0222 300 ILE A O   
7073 C CB  . ILE D 298 ? 1.4290 1.4259 1.2838 -0.0500 0.0121  -0.0189 300 ILE A CB  
7074 C CG1 . ILE D 298 ? 1.2150 1.2199 1.0726 -0.0515 0.0135  -0.0175 300 ILE A CG1 
7075 C CG2 . ILE D 298 ? 1.4299 1.4248 1.2837 -0.0532 0.0093  -0.0174 300 ILE A CG2 
7076 C CD1 . ILE D 298 ? 1.0562 1.0685 0.9197 -0.0519 0.0123  -0.0151 300 ILE A CD1 
7077 N N   . THR D 299 ? 1.0919 1.0679 0.9339 -0.0517 0.0111  -0.0224 301 THR A N   
7078 C CA  . THR D 299 ? 1.4025 1.3714 1.2413 -0.0512 0.0100  -0.0234 301 THR A CA  
7079 C C   . THR D 299 ? 1.6085 1.5744 1.4444 -0.0551 0.0087  -0.0233 301 THR A C   
7080 O O   . THR D 299 ? 1.7073 1.6734 1.5424 -0.0580 0.0090  -0.0233 301 THR A O   
7081 C CB  . THR D 299 ? 1.6686 1.6318 1.5045 -0.0492 0.0115  -0.0252 301 THR A CB  
7082 O OG1 . THR D 299 ? 2.0058 1.9677 1.8394 -0.0518 0.0126  -0.0256 301 THR A OG1 
7083 C CG2 . THR D 299 ? 1.5400 1.5057 1.3783 -0.0451 0.0127  -0.0261 301 THR A CG2 
7084 N N   . ILE D 300 ? 1.4529 1.4160 1.2873 -0.0553 0.0071  -0.0232 302 ILE A N   
7085 C CA  . ILE D 300 ? 1.6307 1.5915 1.4623 -0.0589 0.0060  -0.0236 302 ILE A CA  
7086 C C   . ILE D 300 ? 2.0057 1.9596 1.8336 -0.0584 0.0062  -0.0252 302 ILE A C   
7087 O O   . ILE D 300 ? 2.0198 1.9717 1.8476 -0.0558 0.0059  -0.0249 302 ILE A O   
7088 C CB  . ILE D 300 ? 1.7633 1.7280 1.5960 -0.0604 0.0038  -0.0220 302 ILE A CB  
7089 C CG1 . ILE D 300 ? 1.7441 1.7156 1.5806 -0.0614 0.0033  -0.0203 302 ILE A CG1 
7090 C CG2 . ILE D 300 ? 2.0668 2.0289 1.8956 -0.0639 0.0028  -0.0232 302 ILE A CG2 
7091 C CD1 . ILE D 300 ? 1.9427 1.9178 1.7807 -0.0624 0.0009  -0.0183 302 ILE A CD1 
7092 N N   . GLY D 301 ? 2.1024 2.0529 1.9277 -0.0612 0.0064  -0.0268 303 GLY A N   
7093 C CA  . GLY D 301 ? 2.1008 2.0453 1.9230 -0.0611 0.0067  -0.0283 303 GLY A CA  
7094 C C   . GLY D 301 ? 2.0903 2.0300 1.9119 -0.0596 0.0082  -0.0292 303 GLY A C   
7095 O O   . GLY D 301 ? 2.0837 2.0246 1.9067 -0.0593 0.0091  -0.0289 303 GLY A O   
7096 N N   . LYS D 302 ? 2.0645 1.9989 1.8839 -0.0589 0.0084  -0.0301 304 LYS A N   
7097 C CA  . LYS D 302 ? 1.7717 1.7010 1.5905 -0.0573 0.0095  -0.0307 304 LYS A CA  
7098 C C   . LYS D 302 ? 1.7560 1.6869 1.5761 -0.0539 0.0098  -0.0296 304 LYS A C   
7099 O O   . LYS D 302 ? 1.9617 1.8917 1.7818 -0.0514 0.0091  -0.0290 304 LYS A O   
7100 C CB  . LYS D 302 ? 1.5656 1.4892 1.3822 -0.0569 0.0095  -0.0315 304 LYS A CB  
7101 C CG  . LYS D 302 ? 1.8042 1.7259 1.6199 -0.0600 0.0096  -0.0334 304 LYS A CG  
7102 C CD  . LYS D 302 ? 1.7949 1.7118 1.6089 -0.0596 0.0099  -0.0342 304 LYS A CD  
7103 C CE  . LYS D 302 ? 1.5126 1.4279 1.3263 -0.0624 0.0103  -0.0367 304 LYS A CE  
7104 N NZ  . LYS D 302 ? 1.2980 1.2093 1.1103 -0.0620 0.0108  -0.0375 304 LYS A NZ  
7105 N N   . CYS D 303 ? 1.7654 1.6992 1.5869 -0.0539 0.0107  -0.0294 305 CYS A N   
7106 C CA  . CYS D 303 ? 1.9348 1.8715 1.7578 -0.0508 0.0114  -0.0290 305 CYS A CA  
7107 C C   . CYS D 303 ? 1.9487 1.8831 1.7705 -0.0505 0.0128  -0.0296 305 CYS A C   
7108 O O   . CYS D 303 ? 2.0086 1.9432 1.8302 -0.0533 0.0132  -0.0294 305 CYS A O   
7109 C CB  . CYS D 303 ? 2.2370 2.1814 2.0632 -0.0510 0.0113  -0.0279 305 CYS A CB  
7110 S SG  . CYS D 303 ? 2.9542 2.9019 2.7823 -0.0508 0.0093  -0.0267 305 CYS A SG  
7111 N N   . PRO D 304 ? 1.8930 1.8253 1.7142 -0.0473 0.0133  -0.0302 306 PRO A N   
7112 C CA  . PRO D 304 ? 1.8009 1.7321 1.6206 -0.0472 0.0146  -0.0307 306 PRO A CA  
7113 C C   . PRO D 304 ? 1.7630 1.7019 1.5846 -0.0473 0.0159  -0.0304 306 PRO A C   
7114 O O   . PRO D 304 ? 2.0554 2.0003 1.8800 -0.0463 0.0159  -0.0300 306 PRO A O   
7115 C CB  . PRO D 304 ? 1.5969 1.5237 1.4154 -0.0436 0.0144  -0.0317 306 PRO A CB  
7116 C CG  . PRO D 304 ? 1.4057 1.3342 1.2266 -0.0412 0.0131  -0.0314 306 PRO A CG  
7117 C CD  . PRO D 304 ? 1.5605 1.4901 1.3819 -0.0442 0.0122  -0.0303 306 PRO A CD  
7118 N N   . LYS D 305 ? 1.3936 1.3327 1.2136 -0.0489 0.0170  -0.0303 307 LYS A N   
7119 C CA  . LYS D 305 ? 1.5034 1.4502 1.3249 -0.0501 0.0183  -0.0296 307 LYS A CA  
7120 C C   . LYS D 305 ? 1.4476 1.4001 1.2708 -0.0464 0.0197  -0.0308 307 LYS A C   
7121 O O   . LYS D 305 ? 1.6311 1.5806 1.4539 -0.0428 0.0195  -0.0324 307 LYS A O   
7122 C CB  . LYS D 305 ? 1.3781 1.3234 1.1972 -0.0528 0.0188  -0.0289 307 LYS A CB  
7123 C CG  . LYS D 305 ? 1.6642 1.6047 1.4832 -0.0567 0.0173  -0.0277 307 LYS A CG  
7124 C CD  . LYS D 305 ? 1.8687 1.8075 1.6861 -0.0596 0.0173  -0.0266 307 LYS A CD  
7125 C CE  . LYS D 305 ? 2.0688 2.0028 1.8875 -0.0634 0.0155  -0.0256 307 LYS A CE  
7126 N NZ  . LYS D 305 ? 1.9848 1.9168 1.8027 -0.0665 0.0149  -0.0240 307 LYS A NZ  
7127 N N   . TYR D 306 ? 1.2432 1.2042 1.0688 -0.0472 0.0208  -0.0300 308 TYR A N   
7128 C CA  . TYR D 306 ? 1.4320 1.3998 1.2602 -0.0437 0.0224  -0.0313 308 TYR A CA  
7129 C C   . TYR D 306 ? 1.3078 1.2797 1.1341 -0.0438 0.0247  -0.0322 308 TYR A C   
7130 O O   . TYR D 306 ? 1.2248 1.1998 1.0500 -0.0476 0.0252  -0.0304 308 TYR A O   
7131 C CB  . TYR D 306 ? 1.5266 1.5023 1.3597 -0.0442 0.0223  -0.0298 308 TYR A CB  
7132 C CG  . TYR D 306 ? 1.4829 1.4661 1.3198 -0.0406 0.0240  -0.0313 308 TYR A CG  
7133 C CD1 . TYR D 306 ? 1.5161 1.4973 1.3553 -0.0362 0.0234  -0.0332 308 TYR A CD1 
7134 C CD2 . TYR D 306 ? 1.5975 1.5899 1.4361 -0.0415 0.0261  -0.0308 308 TYR A CD2 
7135 C CE1 . TYR D 306 ? 1.6472 1.6351 1.4909 -0.0325 0.0248  -0.0350 308 TYR A CE1 
7136 C CE2 . TYR D 306 ? 1.6595 1.6593 1.5022 -0.0379 0.0279  -0.0326 308 TYR A CE2 
7137 C CZ  . TYR D 306 ? 1.6818 1.6791 1.5272 -0.0333 0.0273  -0.0349 308 TYR A CZ  
7138 O OH  . TYR D 306 ? 1.7833 1.7878 1.6337 -0.0294 0.0289  -0.0371 308 TYR A OH  
7139 N N   . VAL D 307 ? 1.5363 1.5084 1.3623 -0.0398 0.0259  -0.0350 309 VAL A N   
7140 C CA  . VAL D 307 ? 1.4749 1.4518 1.2988 -0.0393 0.0284  -0.0366 309 VAL A CA  
7141 C C   . VAL D 307 ? 1.4726 1.4557 1.3006 -0.0346 0.0299  -0.0395 309 VAL A C   
7142 O O   . VAL D 307 ? 1.6282 1.6089 1.4597 -0.0314 0.0285  -0.0404 309 VAL A O   
7143 C CB  . VAL D 307 ? 1.3071 1.2760 1.1255 -0.0394 0.0281  -0.0379 309 VAL A CB  
7144 C CG1 . VAL D 307 ? 1.3760 1.3501 1.1917 -0.0388 0.0306  -0.0400 309 VAL A CG1 
7145 C CG2 . VAL D 307 ? 1.7638 1.7269 1.5794 -0.0440 0.0265  -0.0350 309 VAL A CG2 
7146 N N   . LYS D 308 ? 1.3329 1.3246 1.1609 -0.0344 0.0327  -0.0408 310 LYS A N   
7147 C CA  . LYS D 308 ? 1.3221 1.3203 1.1545 -0.0297 0.0345  -0.0441 310 LYS A CA  
7148 C C   . LYS D 308 ? 1.3129 1.3080 1.1425 -0.0261 0.0355  -0.0485 310 LYS A C   
7149 O O   . LYS D 308 ? 1.3899 1.3904 1.2232 -0.0220 0.0372  -0.0521 310 LYS A O   
7150 C CB  . LYS D 308 ? 1.1138 1.1248 0.9488 -0.0311 0.0373  -0.0434 310 LYS A CB  
7151 C CG  . LYS D 308 ? 1.3442 1.3596 1.1835 -0.0338 0.0362  -0.0395 310 LYS A CG  
7152 C CD  . LYS D 308 ? 1.4189 1.4471 1.2607 -0.0352 0.0390  -0.0387 310 LYS A CD  
7153 C CE  . LYS D 308 ? 1.5616 1.5944 1.4079 -0.0379 0.0377  -0.0346 310 LYS A CE  
7154 N NZ  . LYS D 308 ? 1.2463 1.2922 1.0954 -0.0394 0.0403  -0.0333 310 LYS A NZ  
7155 N N   . SER D 309 ? 1.0620 1.0486 0.8856 -0.0275 0.0345  -0.0485 311 SER A N   
7156 C CA  . SER D 309 ? 1.1626 1.1457 0.9830 -0.0245 0.0352  -0.0526 311 SER A CA  
7157 C C   . SER D 309 ? 1.2466 1.2242 1.0711 -0.0193 0.0333  -0.0552 311 SER A C   
7158 O O   . SER D 309 ? 1.4601 1.4325 1.2873 -0.0191 0.0306  -0.0530 311 SER A O   
7159 C CB  . SER D 309 ? 1.3253 1.3002 1.1386 -0.0278 0.0340  -0.0512 311 SER A CB  
7160 O OG  . SER D 309 ? 1.4745 1.4446 1.2846 -0.0249 0.0340  -0.0550 311 SER A OG  
7161 N N   . THR D 310 ? 1.0952 1.0742 0.9202 -0.0151 0.0345  -0.0601 312 THR A N   
7162 C CA  . THR D 310 ? 0.8353 0.8086 0.6647 -0.0101 0.0322  -0.0626 312 THR A CA  
7163 C C   . THR D 310 ? 1.1509 1.1119 0.9757 -0.0104 0.0293  -0.0620 312 THR A C   
7164 O O   . THR D 310 ? 1.3523 1.3068 1.1804 -0.0083 0.0262  -0.0612 312 THR A O   
7165 C CB  . THR D 310 ? 0.9076 0.8865 0.7400 -0.0053 0.0343  -0.0685 312 THR A CB  
7166 O OG1 . THR D 310 ? 1.4735 1.4523 1.2987 -0.0063 0.0363  -0.0712 312 THR A OG1 
7167 C CG2 . THR D 310 ? 1.3169 1.3084 1.1552 -0.0046 0.0371  -0.0690 312 THR A CG2 
7168 N N   . LYS D 311 ? 1.2389 1.1969 1.0563 -0.0131 0.0301  -0.0621 313 LYS A N   
7169 C CA  . LYS D 311 ? 1.2821 1.2288 1.0950 -0.0136 0.0276  -0.0615 313 LYS A CA  
7170 C C   . LYS D 311 ? 1.3509 1.2957 1.1571 -0.0191 0.0281  -0.0583 313 LYS A C   
7171 O O   . LYS D 311 ? 1.3091 1.2601 1.1118 -0.0213 0.0307  -0.0590 313 LYS A O   
7172 C CB  . LYS D 311 ? 1.4554 1.3991 1.2669 -0.0096 0.0275  -0.0665 313 LYS A CB  
7173 C CG  . LYS D 311 ? 1.5570 1.4887 1.3645 -0.0097 0.0244  -0.0658 313 LYS A CG  
7174 C CD  . LYS D 311 ? 1.1773 1.1056 0.9849 -0.0051 0.0236  -0.0709 313 LYS A CD  
7175 C CE  . LYS D 311 ? 1.3585 1.2894 1.1592 -0.0065 0.0261  -0.0739 313 LYS A CE  
7176 N NZ  . LYS D 311 ? 1.4300 1.3569 1.2301 -0.0022 0.0251  -0.0794 313 LYS A NZ  
7177 N N   . LEU D 312 ? 1.4366 1.3733 1.2415 -0.0215 0.0256  -0.0547 314 LEU A N   
7178 C CA  . LEU D 312 ? 1.3913 1.3243 1.1908 -0.0265 0.0254  -0.0517 314 LEU A CA  
7179 C C   . LEU D 312 ? 1.2460 1.1675 1.0433 -0.0259 0.0225  -0.0511 314 LEU A C   
7180 O O   . LEU D 312 ? 1.0975 1.0138 0.8966 -0.0267 0.0205  -0.0484 314 LEU A O   
7181 C CB  . LEU D 312 ? 1.2226 1.1584 1.0238 -0.0305 0.0253  -0.0477 314 LEU A CB  
7182 C CG  . LEU D 312 ? 1.4610 1.4068 1.2624 -0.0337 0.0278  -0.0465 314 LEU A CG  
7183 C CD1 . LEU D 312 ? 1.6577 1.6025 1.4598 -0.0383 0.0266  -0.0422 314 LEU A CD1 
7184 C CD2 . LEU D 312 ? 1.5236 1.4729 1.3199 -0.0354 0.0296  -0.0477 314 LEU A CD2 
7185 N N   . ARG D 313 ? 1.1365 1.0541 0.9299 -0.0247 0.0223  -0.0535 315 ARG A N   
7186 C CA  . ARG D 313 ? 1.3056 1.2123 1.0971 -0.0240 0.0194  -0.0529 315 ARG A CA  
7187 C C   . ARG D 313 ? 1.2235 1.1270 1.0086 -0.0277 0.0195  -0.0519 315 ARG A C   
7188 O O   . ARG D 313 ? 1.1877 1.0959 0.9694 -0.0281 0.0214  -0.0543 315 ARG A O   
7189 C CB  . ARG D 313 ? 1.4434 1.3469 1.2366 -0.0187 0.0181  -0.0567 315 ARG A CB  
7190 C CG  . ARG D 313 ? 1.6301 1.5365 1.4304 -0.0150 0.0174  -0.0575 315 ARG A CG  
7191 C CD  . ARG D 313 ? 1.9132 1.8163 1.7155 -0.0100 0.0158  -0.0614 315 ARG A CD  
7192 N NE  . ARG D 313 ? 1.8166 1.7091 1.6171 -0.0098 0.0125  -0.0599 315 ARG A NE  
7193 C CZ  . ARG D 313 ? 2.1022 1.9887 1.9030 -0.0064 0.0101  -0.0624 315 ARG A CZ  
7194 N NH1 . ARG D 313 ? 2.1494 2.0361 1.9466 -0.0051 0.0111  -0.0666 315 ARG A NH1 
7195 N NH2 . ARG D 313 ? 2.0700 1.9503 1.8747 -0.0045 0.0065  -0.0606 315 ARG A NH2 
7196 N N   . LEU D 314 ? 1.3758 1.2720 1.1597 -0.0307 0.0176  -0.0483 316 LEU A N   
7197 C CA  . LEU D 314 ? 1.4867 1.3789 1.2654 -0.0346 0.0171  -0.0466 316 LEU A CA  
7198 C C   . LEU D 314 ? 1.5391 1.4224 1.3151 -0.0325 0.0148  -0.0479 316 LEU A C   
7199 O O   . LEU D 314 ? 1.4721 1.3490 1.2508 -0.0300 0.0126  -0.0475 316 LEU A O   
7200 C CB  . LEU D 314 ? 1.5062 1.3954 1.2861 -0.0389 0.0161  -0.0421 316 LEU A CB  
7201 C CG  . LEU D 314 ? 1.5475 1.4444 1.3297 -0.0419 0.0177  -0.0402 316 LEU A CG  
7202 C CD1 . LEU D 314 ? 1.4368 1.3288 1.2210 -0.0453 0.0161  -0.0365 316 LEU A CD1 
7203 C CD2 . LEU D 314 ? 1.4044 1.3083 1.1832 -0.0451 0.0195  -0.0401 316 LEU A CD2 
7204 N N   . ALA D 315 ? 1.5338 1.4169 1.3044 -0.0338 0.0152  -0.0493 317 ALA A N   
7205 C CA  . ALA D 315 ? 1.4858 1.3606 1.2532 -0.0321 0.0130  -0.0508 317 ALA A CA  
7206 C C   . ALA D 315 ? 1.4815 1.3474 1.2477 -0.0355 0.0105  -0.0464 317 ALA A C   
7207 O O   . ALA D 315 ? 1.4608 1.3274 1.2243 -0.0404 0.0107  -0.0436 317 ALA A O   
7208 C CB  . ALA D 315 ? 1.5145 1.3932 1.2763 -0.0324 0.0145  -0.0543 317 ALA A CB  
7209 N N   . THR D 316 ? 1.2779 1.1356 1.0464 -0.0332 0.0078  -0.0456 318 THR A N   
7210 C CA  . THR D 316 ? 1.2114 1.0603 0.9793 -0.0359 0.0054  -0.0417 318 THR A CA  
7211 C C   . THR D 316 ? 1.2484 1.0888 1.0136 -0.0341 0.0026  -0.0425 318 THR A C   
7212 O O   . THR D 316 ? 1.6093 1.4418 1.3751 -0.0354 0.0002  -0.0394 318 THR A O   
7213 C CB  . THR D 316 ? 1.2153 1.0622 0.9887 -0.0356 0.0046  -0.0390 318 THR A CB  
7214 O OG1 . THR D 316 ? 1.0417 0.8870 0.8181 -0.0308 0.0034  -0.0408 318 THR A OG1 
7215 C CG2 . THR D 316 ? 1.4408 1.2957 1.2168 -0.0375 0.0070  -0.0382 318 THR A CG2 
7216 N N   . GLY D 317 ? 1.2289 1.0706 0.9916 -0.0310 0.0028  -0.0469 319 GLY A N   
7217 C CA  . GLY D 317 ? 1.4150 1.2484 1.1758 -0.0287 -0.0002 -0.0482 319 GLY A CA  
7218 C C   . GLY D 317 ? 1.4815 1.3165 1.2363 -0.0286 0.0004  -0.0522 319 GLY A C   
7219 O O   . GLY D 317 ? 1.4209 1.2645 1.1733 -0.0295 0.0035  -0.0546 319 GLY A O   
7220 N N   . LEU D 318 ? 1.4770 1.3035 1.2292 -0.0276 -0.0027 -0.0528 320 LEU A N   
7221 C CA  . LEU D 318 ? 1.5402 1.3667 1.2863 -0.0272 -0.0027 -0.0570 320 LEU A CA  
7222 C C   . LEU D 318 ? 1.6630 1.4956 1.4109 -0.0221 -0.0010 -0.0634 320 LEU A C   
7223 O O   . LEU D 318 ? 1.6034 1.4369 1.3576 -0.0181 -0.0013 -0.0643 320 LEU A O   
7224 C CB  . LEU D 318 ? 1.6541 1.4693 1.3981 -0.0268 -0.0070 -0.0561 320 LEU A CB  
7225 C CG  . LEU D 318 ? 1.5544 1.3630 1.2966 -0.0319 -0.0090 -0.0500 320 LEU A CG  
7226 C CD1 . LEU D 318 ? 1.2387 1.0361 0.9800 -0.0308 -0.0134 -0.0489 320 LEU A CD1 
7227 C CD2 . LEU D 318 ? 1.8298 1.6428 1.5657 -0.0371 -0.0072 -0.0493 320 LEU A CD2 
7228 N N   . ARG D 319 ? 1.6162 1.4533 1.3584 -0.0223 0.0007  -0.0680 321 ARG A N   
7229 C CA  . ARG D 319 ? 1.4986 1.3410 1.2425 -0.0171 0.0023  -0.0750 321 ARG A CA  
7230 C C   . ARG D 319 ? 1.5206 1.3538 1.2676 -0.0123 -0.0018 -0.0774 321 ARG A C   
7231 O O   . ARG D 319 ? 1.4613 1.2872 1.2037 -0.0127 -0.0045 -0.0783 321 ARG A O   
7232 C CB  . ARG D 319 ? 1.2191 1.0683 0.9557 -0.0187 0.0051  -0.0796 321 ARG A CB  
7233 C CG  . ARG D 319 ? 1.5347 1.3958 1.2697 -0.0223 0.0096  -0.0786 321 ARG A CG  
7234 C CD  . ARG D 319 ? 1.4665 1.3368 1.1968 -0.0215 0.0129  -0.0852 321 ARG A CD  
7235 N NE  . ARG D 319 ? 1.6452 1.5276 1.3739 -0.0253 0.0171  -0.0837 321 ARG A NE  
7236 C CZ  . ARG D 319 ? 1.8457 1.7355 1.5672 -0.0289 0.0196  -0.0855 321 ARG A CZ  
7237 N NH1 . ARG D 319 ? 1.8586 1.7455 1.5732 -0.0290 0.0186  -0.0894 321 ARG A NH1 
7238 N NH2 . ARG D 319 ? 2.0660 1.9668 1.7870 -0.0326 0.0229  -0.0832 321 ARG A NH2 
7239 N N   . ASN D 320 ? 1.6229 1.4565 1.3778 -0.0079 -0.0026 -0.0781 322 ASN A N   
7240 C CA  . ASN D 320 ? 1.7580 1.5829 1.5173 -0.0035 -0.0071 -0.0793 322 ASN A CA  
7241 C C   . ASN D 320 ? 1.7742 1.5994 1.5319 0.0004  -0.0075 -0.0870 322 ASN A C   
7242 O O   . ASN D 320 ? 1.6559 1.4888 1.4170 0.0039  -0.0050 -0.0923 322 ASN A O   
7243 C CB  . ASN D 320 ? 1.8058 1.6322 1.5743 -0.0004 -0.0080 -0.0776 322 ASN A CB  
7244 C CG  . ASN D 320 ? 1.8482 1.6649 1.6216 0.0026  -0.0134 -0.0761 322 ASN A CG  
7245 O OD1 . ASN D 320 ? 1.7242 1.5325 1.4943 0.0025  -0.0166 -0.0763 322 ASN A OD1 
7246 N ND2 . ASN D 320 ? 2.1661 1.9840 1.9475 0.0051  -0.0146 -0.0743 322 ASN A ND2 
7247 N N   . VAL D 321 ? 1.7902 1.6069 1.5429 -0.0001 -0.0106 -0.0879 323 VAL A N   
7248 C CA  . VAL D 321 ? 1.7761 1.5913 1.5272 0.0038  -0.0117 -0.0955 323 VAL A CA  
7249 C C   . VAL D 321 ? 1.8777 1.6801 1.6303 0.0055  -0.0179 -0.0943 323 VAL A C   
7250 O O   . VAL D 321 ? 1.8907 1.6861 1.6368 0.0021  -0.0200 -0.0919 323 VAL A O   
7251 C CB  . VAL D 321 ? 1.6119 1.4319 1.3530 0.0006  -0.0086 -0.0992 323 VAL A CB  
7252 C CG1 . VAL D 321 ? 1.5672 1.3848 1.3063 0.0045  -0.0101 -0.1075 323 VAL A CG1 
7253 C CG2 . VAL D 321 ? 1.7860 1.6196 1.5264 -0.0010 -0.0027 -0.1005 323 VAL A CG2 
7254 N N   . PRO D 322 ? 1.9445 1.7433 1.7057 0.0105  -0.0212 -0.0953 324 PRO A N   
7255 C CA  . PRO D 322 ? 1.7441 1.5309 1.5071 0.0123  -0.0275 -0.0944 324 PRO A CA  
7256 C C   . PRO D 322 ? 2.1278 1.9114 1.8862 0.0145  -0.0288 -0.1019 324 PRO A C   
7257 O O   . PRO D 322 ? 2.1132 1.9039 1.8715 0.0173  -0.0259 -0.1094 324 PRO A O   
7258 C CB  . PRO D 322 ? 1.6252 1.4113 1.3995 0.0169  -0.0303 -0.0937 324 PRO A CB  
7259 C CG  . PRO D 322 ? 1.7014 1.4993 1.4793 0.0189  -0.0254 -0.0976 324 PRO A CG  
7260 C CD  . PRO D 322 ? 1.9036 1.7085 1.6740 0.0137  -0.0201 -0.0952 324 PRO A CD  
7261 N N   . SER D 323 ? 2.3785 2.1513 2.1332 0.0131  -0.0335 -0.0998 325 SER A N   
7262 C CA  . SER D 323 ? 2.2017 1.9692 1.9518 0.0148  -0.0360 -0.1062 325 SER A CA  
7263 C C   . SER D 323 ? 2.3241 2.1007 2.0675 0.0148  -0.0309 -0.1143 325 SER A C   
7264 O O   . SER D 323 ? 2.2787 2.0578 2.0251 0.0198  -0.0308 -0.1226 325 SER A O   
7265 C CB  . SER D 323 ? 1.9883 1.7494 1.7473 0.0209  -0.0414 -0.1097 325 SER A CB  
7266 O OG  . SER D 323 ? 2.1610 1.9302 1.9276 0.0256  -0.0390 -0.1149 325 SER A OG  
# 
