data_9CF4
# 
_entry.id   9CF4 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9CF4         pdb_00009cf4 10.2210/pdb9cf4/pdb 
WWPDB D_1000285056 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-12 ? 
2 'Structure model' 1 1 2025-03-19 ? 
3 'Structure model' 1 2 2025-06-18 ? 
# 
_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' 'Database references' 
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' citation        
2 2 'Structure model' citation_author 
3 3 'Structure model' citation        
4 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' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.pdbx_database_id_DOI'    
6  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
7  2 'Structure model' '_citation.title'                   
8  2 'Structure model' '_citation.year'                    
9  2 'Structure model' '_citation_author.identifier_ORCID' 
10 3 'Structure model' '_citation.journal_volume'          
11 3 'Structure model' '_citation.page_first'              
12 3 'Structure model' '_citation.page_last'               
13 3 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9CF4 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-27 
_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              ingar.leiros@uit.no 
_pdbx_contact_author.name_first         Ingar 
_pdbx_contact_author.name_last          Leiros 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9333-4541 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Skogvold, A.C.'  1 0009-0000-7597-879X 
'Brakestad, H.T.' 2 0000-0003-4995-2224 
'Erlandsen, H.'   3 0000-0002-0716-5460 
'Leiros, I.'      4 0000-0001-9333-4541 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Febs J.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1742-464X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            292 
_citation.language                  ? 
_citation.page_first                2918 
_citation.page_last                 2934 
_citation.title                     
'Crystal structure and biochemical analysis of the dimeric transaminase DoeD provides insights into ectoine degradation.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1111/febs.70043 
_citation.pdbx_database_id_PubMed   40014458 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Skogvold, A.C.A.' 1 ? 
primary 'Brakestad, H.T.'  2 ? 
primary 'Erlandsen, H.'    3 ? 
primary 'Leiros, I.'       4 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man Aminotransferase         51638.148 1    2.6.1.- ? ? ? 
2 polymer     man Aminotransferase         51410.031 1    2.6.1.- ? ? ? 
3 non-polymer syn GLYCEROL                 92.094    5    ?       ? ? ? 
4 non-polymer syn "PYRIDOXAL-5'-PHOSPHATE" 247.142   1    ?       ? ? ? 
5 water       nat water                    18.015    1184 ?       ? ? ? 
# 
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 yes 
;MSQHQNLIDRDRKVTFHASTHLRDFAHGEAPGRVMAGGEGIHVVDKDGREFIDGFAGLYCVNIGYGRTEVAEAIHRQALE
LAYYHTYVGHSNEPQIQLSEKILELAGPGMSKVYYGMSGSDANETQLKIVRYYNNVLGRPQKKKVIARQRGYHGSGIASG
SLTGLKAFHDHFDLPIEGILHTEAPYYYHRGAEREGMSEREFSAHCAAKLEEMILAEGPETVAAFIGEPVLGTGGIVPPP
EGYWEAIQGVLAKYDVLLIADEVVCGFGRIGADFGSHHYAIKPDLITIA(LLP)GLTSAYQPLSGVIIGDRVWQVLEQGT
GEFGPIGHGWTYSGHALGCAAGLANLAIIEREGLTANAAETGAYLQQCMQQTFGEHPLVGEVRGVGMLAALEFSPAPARR
AFFDPALKVGPRVSAAAMSENLIARAMPQGDILGFAPPLVTTRAEVDEIVARAKRAVDKVTDELTRSGDLKAHHHHHH
;
;MSQHQNLIDRDRKVTFHASTHLRDFAHGEAPGRVMAGGEGIHVVDKDGREFIDGFAGLYCVNIGYGRTEVAEAIHRQALE
LAYYHTYVGHSNEPQIQLSEKILELAGPGMSKVYYGMSGSDANETQLKIVRYYNNVLGRPQKKKVIARQRGYHGSGIASG
SLTGLKAFHDHFDLPIEGILHTEAPYYYHRGAEREGMSEREFSAHCAAKLEEMILAEGPETVAAFIGEPVLGTGGIVPPP
EGYWEAIQGVLAKYDVLLIADEVVCGFGRIGADFGSHHYAIKPDLITIAKGLTSAYQPLSGVIIGDRVWQVLEQGTGEFG
PIGHGWTYSGHALGCAAGLANLAIIEREGLTANAAETGAYLQQCMQQTFGEHPLVGEVRGVGMLAALEFSPAPARRAFFD
PALKVGPRVSAAAMSENLIARAMPQGDILGFAPPLVTTRAEVDEIVARAKRAVDKVTDELTRSGDLKAHHHHHH
;
A ? 
2 'polypeptide(L)' no no  
;MSQHQNLIDRDRKVTFHASTHLRDFAHGEAPGRVMAGGEGIHVVDKDGREFIDGFAGLYCVNIGYGRTEVAEAIHRQALE
LAYYHTYVGHSNEPQIQLSEKILELAGPGMSKVYYGMSGSDANETQLKIVRYYNNVLGRPQKKKVIARQRGYHGSGIASG
SLTGLKAFHDHFDLPIEGILHTEAPYYYHRGAEREGMSEREFSAHCAAKLEEMILAEGPETVAAFIGEPVLGTGGIVPPP
EGYWEAIQGVLAKYDVLLIADEVVCGFGRIGADFGSHHYAIKPDLITIAKGLTSAYQPLSGVIIGDRVWQVLEQGTGEFG
PIGHGWTYSGHALGCAAGLANLAIIEREGLTANAAETGAYLQQCMQQTFGEHPLVGEVRGVGMLAALEFSPAPARRAFFD
PALKVGPRVSAAAMSENLIARAMPQGDILGFAPPLVTTRAEVDEIVARAKRAVDKVTDELTRSGDLKAHHHHHH
;
;MSQHQNLIDRDRKVTFHASTHLRDFAHGEAPGRVMAGGEGIHVVDKDGREFIDGFAGLYCVNIGYGRTEVAEAIHRQALE
LAYYHTYVGHSNEPQIQLSEKILELAGPGMSKVYYGMSGSDANETQLKIVRYYNNVLGRPQKKKVIARQRGYHGSGIASG
SLTGLKAFHDHFDLPIEGILHTEAPYYYHRGAEREGMSEREFSAHCAAKLEEMILAEGPETVAAFIGEPVLGTGGIVPPP
EGYWEAIQGVLAKYDVLLIADEVVCGFGRIGADFGSHHYAIKPDLITIAKGLTSAYQPLSGVIIGDRVWQVLEQGTGEFG
PIGHGWTYSGHALGCAAGLANLAIIEREGLTANAAETGAYLQQCMQQTFGEHPLVGEVRGVGMLAALEFSPAPARRAFFD
PALKVGPRVSAAAMSENLIARAMPQGDILGFAPPLVTTRAEVDEIVARAKRAVDKVTDELTRSGDLKAHHHHHH
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 GLYCEROL                 GOL 
4 "PYRIDOXAL-5'-PHOSPHATE" PLP 
5 water                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   GLN n 
1 4   HIS n 
1 5   GLN n 
1 6   ASN n 
1 7   LEU n 
1 8   ILE n 
1 9   ASP n 
1 10  ARG n 
1 11  ASP n 
1 12  ARG n 
1 13  LYS n 
1 14  VAL n 
1 15  THR n 
1 16  PHE n 
1 17  HIS n 
1 18  ALA n 
1 19  SER n 
1 20  THR n 
1 21  HIS n 
1 22  LEU n 
1 23  ARG n 
1 24  ASP n 
1 25  PHE n 
1 26  ALA n 
1 27  HIS n 
1 28  GLY n 
1 29  GLU n 
1 30  ALA n 
1 31  PRO n 
1 32  GLY n 
1 33  ARG n 
1 34  VAL n 
1 35  MET n 
1 36  ALA n 
1 37  GLY n 
1 38  GLY n 
1 39  GLU n 
1 40  GLY n 
1 41  ILE n 
1 42  HIS n 
1 43  VAL n 
1 44  VAL n 
1 45  ASP n 
1 46  LYS n 
1 47  ASP n 
1 48  GLY n 
1 49  ARG n 
1 50  GLU n 
1 51  PHE n 
1 52  ILE n 
1 53  ASP n 
1 54  GLY n 
1 55  PHE n 
1 56  ALA n 
1 57  GLY n 
1 58  LEU n 
1 59  TYR n 
1 60  CYS n 
1 61  VAL n 
1 62  ASN n 
1 63  ILE n 
1 64  GLY n 
1 65  TYR n 
1 66  GLY n 
1 67  ARG n 
1 68  THR n 
1 69  GLU n 
1 70  VAL n 
1 71  ALA n 
1 72  GLU n 
1 73  ALA n 
1 74  ILE n 
1 75  HIS n 
1 76  ARG n 
1 77  GLN n 
1 78  ALA n 
1 79  LEU n 
1 80  GLU n 
1 81  LEU n 
1 82  ALA n 
1 83  TYR n 
1 84  TYR n 
1 85  HIS n 
1 86  THR n 
1 87  TYR n 
1 88  VAL n 
1 89  GLY n 
1 90  HIS n 
1 91  SER n 
1 92  ASN n 
1 93  GLU n 
1 94  PRO n 
1 95  GLN n 
1 96  ILE n 
1 97  GLN n 
1 98  LEU n 
1 99  SER n 
1 100 GLU n 
1 101 LYS n 
1 102 ILE n 
1 103 LEU n 
1 104 GLU n 
1 105 LEU n 
1 106 ALA n 
1 107 GLY n 
1 108 PRO n 
1 109 GLY n 
1 110 MET n 
1 111 SER n 
1 112 LYS n 
1 113 VAL n 
1 114 TYR n 
1 115 TYR n 
1 116 GLY n 
1 117 MET n 
1 118 SER n 
1 119 GLY n 
1 120 SER n 
1 121 ASP n 
1 122 ALA n 
1 123 ASN n 
1 124 GLU n 
1 125 THR n 
1 126 GLN n 
1 127 LEU n 
1 128 LYS n 
1 129 ILE n 
1 130 VAL n 
1 131 ARG n 
1 132 TYR n 
1 133 TYR n 
1 134 ASN n 
1 135 ASN n 
1 136 VAL n 
1 137 LEU n 
1 138 GLY n 
1 139 ARG n 
1 140 PRO n 
1 141 GLN n 
1 142 LYS n 
1 143 LYS n 
1 144 LYS n 
1 145 VAL n 
1 146 ILE n 
1 147 ALA n 
1 148 ARG n 
1 149 GLN n 
1 150 ARG n 
1 151 GLY n 
1 152 TYR n 
1 153 HIS n 
1 154 GLY n 
1 155 SER n 
1 156 GLY n 
1 157 ILE n 
1 158 ALA n 
1 159 SER n 
1 160 GLY n 
1 161 SER n 
1 162 LEU n 
1 163 THR n 
1 164 GLY n 
1 165 LEU n 
1 166 LYS n 
1 167 ALA n 
1 168 PHE n 
1 169 HIS n 
1 170 ASP n 
1 171 HIS n 
1 172 PHE n 
1 173 ASP n 
1 174 LEU n 
1 175 PRO n 
1 176 ILE n 
1 177 GLU n 
1 178 GLY n 
1 179 ILE n 
1 180 LEU n 
1 181 HIS n 
1 182 THR n 
1 183 GLU n 
1 184 ALA n 
1 185 PRO n 
1 186 TYR n 
1 187 TYR n 
1 188 TYR n 
1 189 HIS n 
1 190 ARG n 
1 191 GLY n 
1 192 ALA n 
1 193 GLU n 
1 194 ARG n 
1 195 GLU n 
1 196 GLY n 
1 197 MET n 
1 198 SER n 
1 199 GLU n 
1 200 ARG n 
1 201 GLU n 
1 202 PHE n 
1 203 SER n 
1 204 ALA n 
1 205 HIS n 
1 206 CYS n 
1 207 ALA n 
1 208 ALA n 
1 209 LYS n 
1 210 LEU n 
1 211 GLU n 
1 212 GLU n 
1 213 MET n 
1 214 ILE n 
1 215 LEU n 
1 216 ALA n 
1 217 GLU n 
1 218 GLY n 
1 219 PRO n 
1 220 GLU n 
1 221 THR n 
1 222 VAL n 
1 223 ALA n 
1 224 ALA n 
1 225 PHE n 
1 226 ILE n 
1 227 GLY n 
1 228 GLU n 
1 229 PRO n 
1 230 VAL n 
1 231 LEU n 
1 232 GLY n 
1 233 THR n 
1 234 GLY n 
1 235 GLY n 
1 236 ILE n 
1 237 VAL n 
1 238 PRO n 
1 239 PRO n 
1 240 PRO n 
1 241 GLU n 
1 242 GLY n 
1 243 TYR n 
1 244 TRP n 
1 245 GLU n 
1 246 ALA n 
1 247 ILE n 
1 248 GLN n 
1 249 GLY n 
1 250 VAL n 
1 251 LEU n 
1 252 ALA n 
1 253 LYS n 
1 254 TYR n 
1 255 ASP n 
1 256 VAL n 
1 257 LEU n 
1 258 LEU n 
1 259 ILE n 
1 260 ALA n 
1 261 ASP n 
1 262 GLU n 
1 263 VAL n 
1 264 VAL n 
1 265 CYS n 
1 266 GLY n 
1 267 PHE n 
1 268 GLY n 
1 269 ARG n 
1 270 ILE n 
1 271 GLY n 
1 272 ALA n 
1 273 ASP n 
1 274 PHE n 
1 275 GLY n 
1 276 SER n 
1 277 HIS n 
1 278 HIS n 
1 279 TYR n 
1 280 ALA n 
1 281 ILE n 
1 282 LYS n 
1 283 PRO n 
1 284 ASP n 
1 285 LEU n 
1 286 ILE n 
1 287 THR n 
1 288 ILE n 
1 289 ALA n 
1 290 LLP n 
1 291 GLY n 
1 292 LEU n 
1 293 THR n 
1 294 SER n 
1 295 ALA n 
1 296 TYR n 
1 297 GLN n 
1 298 PRO n 
1 299 LEU n 
1 300 SER n 
1 301 GLY n 
1 302 VAL n 
1 303 ILE n 
1 304 ILE n 
1 305 GLY n 
1 306 ASP n 
1 307 ARG n 
1 308 VAL n 
1 309 TRP n 
1 310 GLN n 
1 311 VAL n 
1 312 LEU n 
1 313 GLU n 
1 314 GLN n 
1 315 GLY n 
1 316 THR n 
1 317 GLY n 
1 318 GLU n 
1 319 PHE n 
1 320 GLY n 
1 321 PRO n 
1 322 ILE n 
1 323 GLY n 
1 324 HIS n 
1 325 GLY n 
1 326 TRP n 
1 327 THR n 
1 328 TYR n 
1 329 SER n 
1 330 GLY n 
1 331 HIS n 
1 332 ALA n 
1 333 LEU n 
1 334 GLY n 
1 335 CYS n 
1 336 ALA n 
1 337 ALA n 
1 338 GLY n 
1 339 LEU n 
1 340 ALA n 
1 341 ASN n 
1 342 LEU n 
1 343 ALA n 
1 344 ILE n 
1 345 ILE n 
1 346 GLU n 
1 347 ARG n 
1 348 GLU n 
1 349 GLY n 
1 350 LEU n 
1 351 THR n 
1 352 ALA n 
1 353 ASN n 
1 354 ALA n 
1 355 ALA n 
1 356 GLU n 
1 357 THR n 
1 358 GLY n 
1 359 ALA n 
1 360 TYR n 
1 361 LEU n 
1 362 GLN n 
1 363 GLN n 
1 364 CYS n 
1 365 MET n 
1 366 GLN n 
1 367 GLN n 
1 368 THR n 
1 369 PHE n 
1 370 GLY n 
1 371 GLU n 
1 372 HIS n 
1 373 PRO n 
1 374 LEU n 
1 375 VAL n 
1 376 GLY n 
1 377 GLU n 
1 378 VAL n 
1 379 ARG n 
1 380 GLY n 
1 381 VAL n 
1 382 GLY n 
1 383 MET n 
1 384 LEU n 
1 385 ALA n 
1 386 ALA n 
1 387 LEU n 
1 388 GLU n 
1 389 PHE n 
1 390 SER n 
1 391 PRO n 
1 392 ALA n 
1 393 PRO n 
1 394 ALA n 
1 395 ARG n 
1 396 ARG n 
1 397 ALA n 
1 398 PHE n 
1 399 PHE n 
1 400 ASP n 
1 401 PRO n 
1 402 ALA n 
1 403 LEU n 
1 404 LYS n 
1 405 VAL n 
1 406 GLY n 
1 407 PRO n 
1 408 ARG n 
1 409 VAL n 
1 410 SER n 
1 411 ALA n 
1 412 ALA n 
1 413 ALA n 
1 414 MET n 
1 415 SER n 
1 416 GLU n 
1 417 ASN n 
1 418 LEU n 
1 419 ILE n 
1 420 ALA n 
1 421 ARG n 
1 422 ALA n 
1 423 MET n 
1 424 PRO n 
1 425 GLN n 
1 426 GLY n 
1 427 ASP n 
1 428 ILE n 
1 429 LEU n 
1 430 GLY n 
1 431 PHE n 
1 432 ALA n 
1 433 PRO n 
1 434 PRO n 
1 435 LEU n 
1 436 VAL n 
1 437 THR n 
1 438 THR n 
1 439 ARG n 
1 440 ALA n 
1 441 GLU n 
1 442 VAL n 
1 443 ASP n 
1 444 GLU n 
1 445 ILE n 
1 446 VAL n 
1 447 ALA n 
1 448 ARG n 
1 449 ALA n 
1 450 LYS n 
1 451 ARG n 
1 452 ALA n 
1 453 VAL n 
1 454 ASP n 
1 455 LYS n 
1 456 VAL n 
1 457 THR n 
1 458 ASP n 
1 459 GLU n 
1 460 LEU n 
1 461 THR n 
1 462 ARG n 
1 463 SER n 
1 464 GLY n 
1 465 ASP n 
1 466 LEU n 
1 467 LYS n 
1 468 ALA n 
1 469 HIS n 
1 470 HIS n 
1 471 HIS n 
1 472 HIS n 
1 473 HIS n 
1 474 HIS n 
2 1   MET n 
2 2   SER n 
2 3   GLN n 
2 4   HIS n 
2 5   GLN n 
2 6   ASN n 
2 7   LEU n 
2 8   ILE n 
2 9   ASP n 
2 10  ARG n 
2 11  ASP n 
2 12  ARG n 
2 13  LYS n 
2 14  VAL n 
2 15  THR n 
2 16  PHE n 
2 17  HIS n 
2 18  ALA n 
2 19  SER n 
2 20  THR n 
2 21  HIS n 
2 22  LEU n 
2 23  ARG n 
2 24  ASP n 
2 25  PHE n 
2 26  ALA n 
2 27  HIS n 
2 28  GLY n 
2 29  GLU n 
2 30  ALA n 
2 31  PRO n 
2 32  GLY n 
2 33  ARG n 
2 34  VAL n 
2 35  MET n 
2 36  ALA n 
2 37  GLY n 
2 38  GLY n 
2 39  GLU n 
2 40  GLY n 
2 41  ILE n 
2 42  HIS n 
2 43  VAL n 
2 44  VAL n 
2 45  ASP n 
2 46  LYS n 
2 47  ASP n 
2 48  GLY n 
2 49  ARG n 
2 50  GLU n 
2 51  PHE n 
2 52  ILE n 
2 53  ASP n 
2 54  GLY n 
2 55  PHE n 
2 56  ALA n 
2 57  GLY n 
2 58  LEU n 
2 59  TYR n 
2 60  CYS n 
2 61  VAL n 
2 62  ASN n 
2 63  ILE n 
2 64  GLY n 
2 65  TYR n 
2 66  GLY n 
2 67  ARG n 
2 68  THR n 
2 69  GLU n 
2 70  VAL n 
2 71  ALA n 
2 72  GLU n 
2 73  ALA n 
2 74  ILE n 
2 75  HIS n 
2 76  ARG n 
2 77  GLN n 
2 78  ALA n 
2 79  LEU n 
2 80  GLU n 
2 81  LEU n 
2 82  ALA n 
2 83  TYR n 
2 84  TYR n 
2 85  HIS n 
2 86  THR n 
2 87  TYR n 
2 88  VAL n 
2 89  GLY n 
2 90  HIS n 
2 91  SER n 
2 92  ASN n 
2 93  GLU n 
2 94  PRO n 
2 95  GLN n 
2 96  ILE n 
2 97  GLN n 
2 98  LEU n 
2 99  SER n 
2 100 GLU n 
2 101 LYS n 
2 102 ILE n 
2 103 LEU n 
2 104 GLU n 
2 105 LEU n 
2 106 ALA n 
2 107 GLY n 
2 108 PRO n 
2 109 GLY n 
2 110 MET n 
2 111 SER n 
2 112 LYS n 
2 113 VAL n 
2 114 TYR n 
2 115 TYR n 
2 116 GLY n 
2 117 MET n 
2 118 SER n 
2 119 GLY n 
2 120 SER n 
2 121 ASP n 
2 122 ALA n 
2 123 ASN n 
2 124 GLU n 
2 125 THR n 
2 126 GLN n 
2 127 LEU n 
2 128 LYS n 
2 129 ILE n 
2 130 VAL n 
2 131 ARG n 
2 132 TYR n 
2 133 TYR n 
2 134 ASN n 
2 135 ASN n 
2 136 VAL n 
2 137 LEU n 
2 138 GLY n 
2 139 ARG n 
2 140 PRO n 
2 141 GLN n 
2 142 LYS n 
2 143 LYS n 
2 144 LYS n 
2 145 VAL n 
2 146 ILE n 
2 147 ALA n 
2 148 ARG n 
2 149 GLN n 
2 150 ARG n 
2 151 GLY n 
2 152 TYR n 
2 153 HIS n 
2 154 GLY n 
2 155 SER n 
2 156 GLY n 
2 157 ILE n 
2 158 ALA n 
2 159 SER n 
2 160 GLY n 
2 161 SER n 
2 162 LEU n 
2 163 THR n 
2 164 GLY n 
2 165 LEU n 
2 166 LYS n 
2 167 ALA n 
2 168 PHE n 
2 169 HIS n 
2 170 ASP n 
2 171 HIS n 
2 172 PHE n 
2 173 ASP n 
2 174 LEU n 
2 175 PRO n 
2 176 ILE n 
2 177 GLU n 
2 178 GLY n 
2 179 ILE n 
2 180 LEU n 
2 181 HIS n 
2 182 THR n 
2 183 GLU n 
2 184 ALA n 
2 185 PRO n 
2 186 TYR n 
2 187 TYR n 
2 188 TYR n 
2 189 HIS n 
2 190 ARG n 
2 191 GLY n 
2 192 ALA n 
2 193 GLU n 
2 194 ARG n 
2 195 GLU n 
2 196 GLY n 
2 197 MET n 
2 198 SER n 
2 199 GLU n 
2 200 ARG n 
2 201 GLU n 
2 202 PHE n 
2 203 SER n 
2 204 ALA n 
2 205 HIS n 
2 206 CYS n 
2 207 ALA n 
2 208 ALA n 
2 209 LYS n 
2 210 LEU n 
2 211 GLU n 
2 212 GLU n 
2 213 MET n 
2 214 ILE n 
2 215 LEU n 
2 216 ALA n 
2 217 GLU n 
2 218 GLY n 
2 219 PRO n 
2 220 GLU n 
2 221 THR n 
2 222 VAL n 
2 223 ALA n 
2 224 ALA n 
2 225 PHE n 
2 226 ILE n 
2 227 GLY n 
2 228 GLU n 
2 229 PRO n 
2 230 VAL n 
2 231 LEU n 
2 232 GLY n 
2 233 THR n 
2 234 GLY n 
2 235 GLY n 
2 236 ILE n 
2 237 VAL n 
2 238 PRO n 
2 239 PRO n 
2 240 PRO n 
2 241 GLU n 
2 242 GLY n 
2 243 TYR n 
2 244 TRP n 
2 245 GLU n 
2 246 ALA n 
2 247 ILE n 
2 248 GLN n 
2 249 GLY n 
2 250 VAL n 
2 251 LEU n 
2 252 ALA n 
2 253 LYS n 
2 254 TYR n 
2 255 ASP n 
2 256 VAL n 
2 257 LEU n 
2 258 LEU n 
2 259 ILE n 
2 260 ALA n 
2 261 ASP n 
2 262 GLU n 
2 263 VAL n 
2 264 VAL n 
2 265 CYS n 
2 266 GLY n 
2 267 PHE n 
2 268 GLY n 
2 269 ARG n 
2 270 ILE n 
2 271 GLY n 
2 272 ALA n 
2 273 ASP n 
2 274 PHE n 
2 275 GLY n 
2 276 SER n 
2 277 HIS n 
2 278 HIS n 
2 279 TYR n 
2 280 ALA n 
2 281 ILE n 
2 282 LYS n 
2 283 PRO n 
2 284 ASP n 
2 285 LEU n 
2 286 ILE n 
2 287 THR n 
2 288 ILE n 
2 289 ALA n 
2 290 LYS n 
2 291 GLY n 
2 292 LEU n 
2 293 THR n 
2 294 SER n 
2 295 ALA n 
2 296 TYR n 
2 297 GLN n 
2 298 PRO n 
2 299 LEU n 
2 300 SER n 
2 301 GLY n 
2 302 VAL n 
2 303 ILE n 
2 304 ILE n 
2 305 GLY n 
2 306 ASP n 
2 307 ARG n 
2 308 VAL n 
2 309 TRP n 
2 310 GLN n 
2 311 VAL n 
2 312 LEU n 
2 313 GLU n 
2 314 GLN n 
2 315 GLY n 
2 316 THR n 
2 317 GLY n 
2 318 GLU n 
2 319 PHE n 
2 320 GLY n 
2 321 PRO n 
2 322 ILE n 
2 323 GLY n 
2 324 HIS n 
2 325 GLY n 
2 326 TRP n 
2 327 THR n 
2 328 TYR n 
2 329 SER n 
2 330 GLY n 
2 331 HIS n 
2 332 ALA n 
2 333 LEU n 
2 334 GLY n 
2 335 CYS n 
2 336 ALA n 
2 337 ALA n 
2 338 GLY n 
2 339 LEU n 
2 340 ALA n 
2 341 ASN n 
2 342 LEU n 
2 343 ALA n 
2 344 ILE n 
2 345 ILE n 
2 346 GLU n 
2 347 ARG n 
2 348 GLU n 
2 349 GLY n 
2 350 LEU n 
2 351 THR n 
2 352 ALA n 
2 353 ASN n 
2 354 ALA n 
2 355 ALA n 
2 356 GLU n 
2 357 THR n 
2 358 GLY n 
2 359 ALA n 
2 360 TYR n 
2 361 LEU n 
2 362 GLN n 
2 363 GLN n 
2 364 CYS n 
2 365 MET n 
2 366 GLN n 
2 367 GLN n 
2 368 THR n 
2 369 PHE n 
2 370 GLY n 
2 371 GLU n 
2 372 HIS n 
2 373 PRO n 
2 374 LEU n 
2 375 VAL n 
2 376 GLY n 
2 377 GLU n 
2 378 VAL n 
2 379 ARG n 
2 380 GLY n 
2 381 VAL n 
2 382 GLY n 
2 383 MET n 
2 384 LEU n 
2 385 ALA n 
2 386 ALA n 
2 387 LEU n 
2 388 GLU n 
2 389 PHE n 
2 390 SER n 
2 391 PRO n 
2 392 ALA n 
2 393 PRO n 
2 394 ALA n 
2 395 ARG n 
2 396 ARG n 
2 397 ALA n 
2 398 PHE n 
2 399 PHE n 
2 400 ASP n 
2 401 PRO n 
2 402 ALA n 
2 403 LEU n 
2 404 LYS n 
2 405 VAL n 
2 406 GLY n 
2 407 PRO n 
2 408 ARG n 
2 409 VAL n 
2 410 SER n 
2 411 ALA n 
2 412 ALA n 
2 413 ALA n 
2 414 MET n 
2 415 SER n 
2 416 GLU n 
2 417 ASN n 
2 418 LEU n 
2 419 ILE n 
2 420 ALA n 
2 421 ARG n 
2 422 ALA n 
2 423 MET n 
2 424 PRO n 
2 425 GLN n 
2 426 GLY n 
2 427 ASP n 
2 428 ILE n 
2 429 LEU n 
2 430 GLY n 
2 431 PHE n 
2 432 ALA n 
2 433 PRO n 
2 434 PRO n 
2 435 LEU n 
2 436 VAL n 
2 437 THR n 
2 438 THR n 
2 439 ARG n 
2 440 ALA n 
2 441 GLU n 
2 442 VAL n 
2 443 ASP n 
2 444 GLU n 
2 445 ILE n 
2 446 VAL n 
2 447 ALA n 
2 448 ARG n 
2 449 ALA n 
2 450 LYS n 
2 451 ARG n 
2 452 ALA n 
2 453 VAL n 
2 454 ASP n 
2 455 LYS n 
2 456 VAL n 
2 457 THR n 
2 458 ASP n 
2 459 GLU n 
2 460 LEU n 
2 461 THR n 
2 462 ARG n 
2 463 SER n 
2 464 GLY n 
2 465 ASP n 
2 466 LEU n 
2 467 LYS n 
2 468 ALA n 
2 469 HIS n 
2 470 HIS n 
2 471 HIS n 
2 472 HIS n 
2 473 HIS n 
2 474 HIS 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' 1 474 ? ? Csal_2724 ? 'C. salexigens DSM 3043' ? ? ? ? 'Chromohalobacter israelensis DSM 3043' 
290398 ? ? ? ? ? ? ? ? 'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 474 ? ? Csal_2724 ? 'C. salexigens DSM 3043' ? ? ? ? 'Chromohalobacter israelensis DSM 3043' 
290398 ? ? ? ? ? ? ? ? 'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                                                 
?                                      'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE                                                                                                
?                                      'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                                              
?                                      'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                                         
?                                      'C4 H7 N O4'      133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                                                
?                                      'C3 H7 N O2 S'    121.158 
GLN 'L-peptide linking' y GLUTAMINE                                                                                               
?                                      'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                                         
?                                      'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE                                                                                                 
?                                      'C2 H5 N O2'      75.067  
GOL non-polymer         . GLYCEROL                                                                                                
'GLYCERIN; PROPANE-1,2,3-TRIOL'        'C3 H8 O3'        92.094  
HIS 'L-peptide linking' y HISTIDINE                                                                                               
?                                      'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER                                                                                                   
?                                      'H2 O'            18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                                              
?                                      'C6 H13 N O2'     131.173 
LEU 'L-peptide linking' y LEUCINE                                                                                                 
?                                      'C6 H13 N O2'     131.173 
LLP 'L-peptide linking' n '(2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid' 
"N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE" 'C14 H22 N3 O7 P' 375.314 
LYS 'L-peptide linking' y LYSINE                                                                                                  
?                                      'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE                                                                                              
?                                      'C5 H11 N O2 S'   149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                                                           
?                                      'C9 H11 N O2'     165.189 
PLP non-polymer         . "PYRIDOXAL-5'-PHOSPHATE"                                                                                
'VITAMIN B6 Phosphate'                 'C8 H10 N O6 P'   247.142 
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_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   2   SER SER A . n 
A 1 3   GLN 3   3   3   GLN GLN A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   GLN 5   5   5   GLN GLN A . n 
A 1 6   ASN 6   6   6   ASN ASN A . n 
A 1 7   LEU 7   7   7   LEU LEU A . n 
A 1 8   ILE 8   8   8   ILE ILE A . n 
A 1 9   ASP 9   9   9   ASP ASP A . n 
A 1 10  ARG 10  10  10  ARG ARG A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  ARG 12  12  12  ARG ARG A . n 
A 1 13  LYS 13  13  13  LYS LYS A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  THR 15  15  15  THR THR A . n 
A 1 16  PHE 16  16  16  PHE PHE A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  ALA 18  18  18  ALA ALA A . n 
A 1 19  SER 19  19  19  SER SER A . n 
A 1 20  THR 20  20  20  THR THR A . n 
A 1 21  HIS 21  21  21  HIS HIS A . n 
A 1 22  LEU 22  22  22  LEU LEU A . n 
A 1 23  ARG 23  23  23  ARG ARG A . n 
A 1 24  ASP 24  24  24  ASP ASP A . n 
A 1 25  PHE 25  25  25  PHE PHE A . n 
A 1 26  ALA 26  26  26  ALA ALA A . n 
A 1 27  HIS 27  27  27  HIS HIS A . n 
A 1 28  GLY 28  28  28  GLY GLY A . n 
A 1 29  GLU 29  29  29  GLU GLU A . n 
A 1 30  ALA 30  30  30  ALA ALA A . n 
A 1 31  PRO 31  31  31  PRO PRO A . n 
A 1 32  GLY 32  32  32  GLY GLY A . n 
A 1 33  ARG 33  33  33  ARG ARG A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  MET 35  35  35  MET MET A . n 
A 1 36  ALA 36  36  36  ALA ALA A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  GLY 38  38  38  GLY GLY A . n 
A 1 39  GLU 39  39  39  GLU GLU A . n 
A 1 40  GLY 40  40  40  GLY GLY A . n 
A 1 41  ILE 41  41  41  ILE ILE A . n 
A 1 42  HIS 42  42  42  HIS HIS A . n 
A 1 43  VAL 43  43  43  VAL VAL A . n 
A 1 44  VAL 44  44  44  VAL VAL A . n 
A 1 45  ASP 45  45  45  ASP ASP A . n 
A 1 46  LYS 46  46  46  LYS LYS A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  ARG 49  49  49  ARG ARG A . n 
A 1 50  GLU 50  50  50  GLU GLU A . n 
A 1 51  PHE 51  51  51  PHE PHE A . n 
A 1 52  ILE 52  52  52  ILE ILE A . n 
A 1 53  ASP 53  53  53  ASP ASP A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  PHE 55  55  55  PHE PHE A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  TYR 59  59  59  TYR TYR A . n 
A 1 60  CYS 60  60  60  CYS CYS A . n 
A 1 61  VAL 61  61  61  VAL VAL A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  ILE 63  63  63  ILE ILE A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  TYR 65  65  65  TYR TYR A . n 
A 1 66  GLY 66  66  66  GLY GLY A . n 
A 1 67  ARG 67  67  67  ARG ARG A . n 
A 1 68  THR 68  68  68  THR THR A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  VAL 70  70  70  VAL VAL A . n 
A 1 71  ALA 71  71  71  ALA ALA A . n 
A 1 72  GLU 72  72  72  GLU GLU A . n 
A 1 73  ALA 73  73  73  ALA ALA A . n 
A 1 74  ILE 74  74  74  ILE ILE A . n 
A 1 75  HIS 75  75  75  HIS HIS A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  GLN 77  77  77  GLN GLN A . n 
A 1 78  ALA 78  78  78  ALA ALA A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  GLU 80  80  80  GLU GLU A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  TYR 83  83  83  TYR TYR A . n 
A 1 84  TYR 84  84  84  TYR TYR A . n 
A 1 85  HIS 85  85  85  HIS HIS A . n 
A 1 86  THR 86  86  86  THR THR A . n 
A 1 87  TYR 87  87  87  TYR TYR A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  GLY 89  89  89  GLY GLY A . n 
A 1 90  HIS 90  90  90  HIS HIS A . n 
A 1 91  SER 91  91  91  SER SER A . n 
A 1 92  ASN 92  92  92  ASN ASN A . n 
A 1 93  GLU 93  93  93  GLU GLU A . n 
A 1 94  PRO 94  94  94  PRO PRO A . n 
A 1 95  GLN 95  95  95  GLN GLN A . n 
A 1 96  ILE 96  96  96  ILE ILE A . n 
A 1 97  GLN 97  97  97  GLN GLN A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 LYS 101 101 101 LYS LYS A . n 
A 1 102 ILE 102 102 102 ILE ILE A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 ALA 106 106 106 ALA ALA A . n 
A 1 107 GLY 107 107 107 GLY GLY A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 MET 110 110 110 MET MET A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 VAL 113 113 113 VAL VAL A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 TYR 115 115 115 TYR TYR A . n 
A 1 116 GLY 116 116 116 GLY GLY A . n 
A 1 117 MET 117 117 117 MET MET A . n 
A 1 118 SER 118 118 118 SER SER A . n 
A 1 119 GLY 119 119 119 GLY GLY A . n 
A 1 120 SER 120 120 120 SER SER A . n 
A 1 121 ASP 121 121 121 ASP ASP A . n 
A 1 122 ALA 122 122 122 ALA ALA A . n 
A 1 123 ASN 123 123 123 ASN ASN A . n 
A 1 124 GLU 124 124 124 GLU GLU A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 GLN 126 126 126 GLN GLN A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 ILE 129 129 129 ILE ILE A . n 
A 1 130 VAL 130 130 130 VAL VAL A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 TYR 132 132 132 TYR TYR A . n 
A 1 133 TYR 133 133 133 TYR TYR A . n 
A 1 134 ASN 134 134 134 ASN ASN A . n 
A 1 135 ASN 135 135 135 ASN ASN A . n 
A 1 136 VAL 136 136 136 VAL VAL A . n 
A 1 137 LEU 137 137 137 LEU LEU A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ARG 139 139 139 ARG ARG A . n 
A 1 140 PRO 140 140 140 PRO PRO A . n 
A 1 141 GLN 141 141 141 GLN GLN A . n 
A 1 142 LYS 142 142 142 LYS LYS A . n 
A 1 143 LYS 143 143 143 LYS LYS A . n 
A 1 144 LYS 144 144 144 LYS LYS A . n 
A 1 145 VAL 145 145 145 VAL VAL A . n 
A 1 146 ILE 146 146 146 ILE ILE A . n 
A 1 147 ALA 147 147 147 ALA ALA A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 GLN 149 149 149 GLN GLN A . n 
A 1 150 ARG 150 150 150 ARG ARG A . n 
A 1 151 GLY 151 151 151 GLY GLY A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 HIS 153 153 153 HIS HIS A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 GLY 156 156 156 GLY GLY A . n 
A 1 157 ILE 157 157 157 ILE ILE A . n 
A 1 158 ALA 158 158 158 ALA ALA A . n 
A 1 159 SER 159 159 159 SER SER A . n 
A 1 160 GLY 160 160 160 GLY GLY A . n 
A 1 161 SER 161 161 161 SER SER A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 THR 163 163 163 THR THR A . n 
A 1 164 GLY 164 164 164 GLY GLY A . n 
A 1 165 LEU 165 165 165 LEU LEU A . n 
A 1 166 LYS 166 166 166 LYS LYS A . n 
A 1 167 ALA 167 167 167 ALA ALA A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 HIS 169 169 169 HIS HIS A . n 
A 1 170 ASP 170 170 170 ASP ASP A . n 
A 1 171 HIS 171 171 171 HIS HIS A . n 
A 1 172 PHE 172 172 172 PHE PHE A . n 
A 1 173 ASP 173 173 173 ASP ASP A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 PRO 175 175 175 PRO PRO A . n 
A 1 176 ILE 176 176 176 ILE ILE A . n 
A 1 177 GLU 177 177 177 GLU GLU A . n 
A 1 178 GLY 178 178 178 GLY GLY A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 HIS 181 181 181 HIS HIS A . n 
A 1 182 THR 182 182 182 THR THR A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 ALA 184 184 184 ALA ALA A . n 
A 1 185 PRO 185 185 185 PRO PRO A . n 
A 1 186 TYR 186 186 186 TYR TYR A . n 
A 1 187 TYR 187 187 187 TYR TYR A . n 
A 1 188 TYR 188 188 188 TYR TYR A . n 
A 1 189 HIS 189 189 189 HIS HIS A . n 
A 1 190 ARG 190 190 190 ARG ARG A . n 
A 1 191 GLY 191 191 191 GLY GLY A . n 
A 1 192 ALA 192 192 192 ALA ALA A . n 
A 1 193 GLU 193 193 193 GLU GLU A . n 
A 1 194 ARG 194 194 194 ARG ARG A . n 
A 1 195 GLU 195 195 195 GLU GLU A . n 
A 1 196 GLY 196 196 196 GLY GLY A . n 
A 1 197 MET 197 197 197 MET MET A . n 
A 1 198 SER 198 198 198 SER SER A . n 
A 1 199 GLU 199 199 199 GLU GLU A . n 
A 1 200 ARG 200 200 200 ARG ARG A . n 
A 1 201 GLU 201 201 201 GLU GLU A . n 
A 1 202 PHE 202 202 202 PHE PHE A . n 
A 1 203 SER 203 203 203 SER SER A . n 
A 1 204 ALA 204 204 204 ALA ALA A . n 
A 1 205 HIS 205 205 205 HIS HIS A . n 
A 1 206 CYS 206 206 206 CYS CYS A . n 
A 1 207 ALA 207 207 207 ALA ALA A . n 
A 1 208 ALA 208 208 208 ALA ALA A . n 
A 1 209 LYS 209 209 209 LYS LYS A . n 
A 1 210 LEU 210 210 210 LEU LEU A . n 
A 1 211 GLU 211 211 211 GLU GLU A . n 
A 1 212 GLU 212 212 212 GLU GLU A . n 
A 1 213 MET 213 213 213 MET MET A . n 
A 1 214 ILE 214 214 214 ILE ILE A . n 
A 1 215 LEU 215 215 215 LEU LEU A . n 
A 1 216 ALA 216 216 216 ALA ALA A . n 
A 1 217 GLU 217 217 217 GLU GLU A . n 
A 1 218 GLY 218 218 218 GLY GLY A . n 
A 1 219 PRO 219 219 219 PRO PRO A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 THR 221 221 221 THR THR A . n 
A 1 222 VAL 222 222 222 VAL VAL A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 PHE 225 225 225 PHE PHE A . n 
A 1 226 ILE 226 226 226 ILE ILE A . n 
A 1 227 GLY 227 227 227 GLY GLY A . n 
A 1 228 GLU 228 228 228 GLU GLU A . n 
A 1 229 PRO 229 229 229 PRO PRO A . n 
A 1 230 VAL 230 230 230 VAL VAL A . n 
A 1 231 LEU 231 231 231 LEU LEU A . n 
A 1 232 GLY 232 232 232 GLY GLY A . n 
A 1 233 THR 233 233 233 THR THR A . n 
A 1 234 GLY 234 234 234 GLY GLY A . n 
A 1 235 GLY 235 235 235 GLY GLY A . n 
A 1 236 ILE 236 236 236 ILE ILE A . n 
A 1 237 VAL 237 237 237 VAL VAL A . n 
A 1 238 PRO 238 238 238 PRO PRO A . n 
A 1 239 PRO 239 239 239 PRO PRO A . n 
A 1 240 PRO 240 240 240 PRO PRO A . n 
A 1 241 GLU 241 241 241 GLU GLU A . n 
A 1 242 GLY 242 242 242 GLY GLY A . n 
A 1 243 TYR 243 243 243 TYR TYR A . n 
A 1 244 TRP 244 244 244 TRP TRP A . n 
A 1 245 GLU 245 245 245 GLU GLU A . n 
A 1 246 ALA 246 246 246 ALA ALA A . n 
A 1 247 ILE 247 247 247 ILE ILE A . n 
A 1 248 GLN 248 248 248 GLN GLN A . n 
A 1 249 GLY 249 249 249 GLY GLY A . n 
A 1 250 VAL 250 250 250 VAL VAL A . n 
A 1 251 LEU 251 251 251 LEU LEU A . n 
A 1 252 ALA 252 252 252 ALA ALA A . n 
A 1 253 LYS 253 253 253 LYS LYS A . n 
A 1 254 TYR 254 254 254 TYR TYR A . n 
A 1 255 ASP 255 255 255 ASP ASP A . n 
A 1 256 VAL 256 256 256 VAL VAL A . n 
A 1 257 LEU 257 257 257 LEU LEU A . n 
A 1 258 LEU 258 258 258 LEU LEU A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 ASP 261 261 261 ASP ASP A . n 
A 1 262 GLU 262 262 262 GLU GLU A . n 
A 1 263 VAL 263 263 263 VAL VAL A . n 
A 1 264 VAL 264 264 264 VAL VAL A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 GLY 266 266 266 GLY GLY A . n 
A 1 267 PHE 267 267 267 PHE PHE A . n 
A 1 268 GLY 268 268 268 GLY GLY A . n 
A 1 269 ARG 269 269 269 ARG ARG A . n 
A 1 270 ILE 270 270 270 ILE ILE A . n 
A 1 271 GLY 271 271 271 GLY GLY A . n 
A 1 272 ALA 272 272 272 ALA ALA A . n 
A 1 273 ASP 273 273 273 ASP ASP A . n 
A 1 274 PHE 274 274 274 PHE PHE A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 SER 276 276 276 SER SER A . n 
A 1 277 HIS 277 277 277 HIS HIS A . n 
A 1 278 HIS 278 278 278 HIS HIS A . n 
A 1 279 TYR 279 279 279 TYR TYR A . n 
A 1 280 ALA 280 280 280 ALA ALA A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 LYS 282 282 282 LYS LYS A . n 
A 1 283 PRO 283 283 283 PRO PRO A . n 
A 1 284 ASP 284 284 284 ASP ASP A . n 
A 1 285 LEU 285 285 285 LEU LEU A . n 
A 1 286 ILE 286 286 286 ILE ILE A . n 
A 1 287 THR 287 287 287 THR THR A . n 
A 1 288 ILE 288 288 288 ILE ILE A . n 
A 1 289 ALA 289 289 289 ALA ALA A . n 
A 1 290 LLP 290 290 2   LLP PLP A . n 
A 1 291 GLY 291 291 291 GLY GLY A . n 
A 1 292 LEU 292 292 292 LEU LEU A . n 
A 1 293 THR 293 293 293 THR THR A . n 
A 1 294 SER 294 294 294 SER SER A . n 
A 1 295 ALA 295 295 295 ALA ALA A . n 
A 1 296 TYR 296 296 296 TYR TYR A . n 
A 1 297 GLN 297 297 297 GLN GLN A . n 
A 1 298 PRO 298 298 298 PRO PRO A . n 
A 1 299 LEU 299 299 299 LEU LEU A . n 
A 1 300 SER 300 300 300 SER SER A . n 
A 1 301 GLY 301 301 301 GLY GLY A . n 
A 1 302 VAL 302 302 302 VAL VAL A . n 
A 1 303 ILE 303 303 303 ILE ILE A . n 
A 1 304 ILE 304 304 304 ILE ILE A . n 
A 1 305 GLY 305 305 305 GLY GLY A . n 
A 1 306 ASP 306 306 306 ASP ASP A . n 
A 1 307 ARG 307 307 307 ARG ARG A . n 
A 1 308 VAL 308 308 308 VAL VAL A . n 
A 1 309 TRP 309 309 309 TRP TRP A . n 
A 1 310 GLN 310 310 310 GLN GLN A . n 
A 1 311 VAL 311 311 311 VAL VAL A . n 
A 1 312 LEU 312 312 312 LEU LEU A . n 
A 1 313 GLU 313 313 313 GLU GLU A . n 
A 1 314 GLN 314 314 314 GLN GLN A . n 
A 1 315 GLY 315 315 315 GLY GLY A . n 
A 1 316 THR 316 316 316 THR THR A . n 
A 1 317 GLY 317 317 317 GLY GLY A . n 
A 1 318 GLU 318 318 318 GLU GLU A . n 
A 1 319 PHE 319 319 319 PHE PHE A . n 
A 1 320 GLY 320 320 320 GLY GLY A . n 
A 1 321 PRO 321 321 321 PRO PRO A . n 
A 1 322 ILE 322 322 322 ILE ILE A . n 
A 1 323 GLY 323 323 323 GLY GLY A . n 
A 1 324 HIS 324 324 324 HIS HIS A . n 
A 1 325 GLY 325 325 325 GLY GLY A . n 
A 1 326 TRP 326 326 326 TRP TRP A . n 
A 1 327 THR 327 327 327 THR THR A . n 
A 1 328 TYR 328 328 328 TYR TYR A . n 
A 1 329 SER 329 329 329 SER SER A . n 
A 1 330 GLY 330 330 330 GLY GLY A . n 
A 1 331 HIS 331 331 331 HIS HIS A . n 
A 1 332 ALA 332 332 332 ALA ALA A . n 
A 1 333 LEU 333 333 333 LEU LEU A . n 
A 1 334 GLY 334 334 334 GLY GLY A . n 
A 1 335 CYS 335 335 335 CYS CYS A . n 
A 1 336 ALA 336 336 336 ALA ALA A . n 
A 1 337 ALA 337 337 337 ALA ALA A . n 
A 1 338 GLY 338 338 338 GLY GLY A . n 
A 1 339 LEU 339 339 339 LEU LEU A . n 
A 1 340 ALA 340 340 340 ALA ALA A . n 
A 1 341 ASN 341 341 341 ASN ASN A . n 
A 1 342 LEU 342 342 342 LEU LEU A . n 
A 1 343 ALA 343 343 343 ALA ALA A . n 
A 1 344 ILE 344 344 344 ILE ILE A . n 
A 1 345 ILE 345 345 345 ILE ILE A . n 
A 1 346 GLU 346 346 346 GLU GLU A . n 
A 1 347 ARG 347 347 347 ARG ARG A . n 
A 1 348 GLU 348 348 348 GLU GLU A . n 
A 1 349 GLY 349 349 349 GLY GLY A . n 
A 1 350 LEU 350 350 350 LEU LEU A . n 
A 1 351 THR 351 351 351 THR THR A . n 
A 1 352 ALA 352 352 352 ALA ALA A . n 
A 1 353 ASN 353 353 353 ASN ASN A . n 
A 1 354 ALA 354 354 354 ALA ALA A . n 
A 1 355 ALA 355 355 355 ALA ALA A . n 
A 1 356 GLU 356 356 356 GLU GLU A . n 
A 1 357 THR 357 357 357 THR THR A . n 
A 1 358 GLY 358 358 358 GLY GLY A . n 
A 1 359 ALA 359 359 359 ALA ALA A . n 
A 1 360 TYR 360 360 360 TYR TYR A . n 
A 1 361 LEU 361 361 361 LEU LEU A . n 
A 1 362 GLN 362 362 362 GLN GLN A . n 
A 1 363 GLN 363 363 363 GLN GLN A . n 
A 1 364 CYS 364 364 364 CYS CYS A . n 
A 1 365 MET 365 365 365 MET MET A . n 
A 1 366 GLN 366 366 366 GLN GLN A . n 
A 1 367 GLN 367 367 367 GLN GLN A . n 
A 1 368 THR 368 368 368 THR THR A . n 
A 1 369 PHE 369 369 369 PHE PHE A . n 
A 1 370 GLY 370 370 370 GLY GLY A . n 
A 1 371 GLU 371 371 371 GLU GLU A . n 
A 1 372 HIS 372 372 372 HIS HIS A . n 
A 1 373 PRO 373 373 373 PRO PRO A . n 
A 1 374 LEU 374 374 374 LEU LEU A . n 
A 1 375 VAL 375 375 375 VAL VAL A . n 
A 1 376 GLY 376 376 376 GLY GLY A . n 
A 1 377 GLU 377 377 377 GLU GLU A . n 
A 1 378 VAL 378 378 378 VAL VAL A . n 
A 1 379 ARG 379 379 379 ARG ARG A . n 
A 1 380 GLY 380 380 380 GLY GLY A . n 
A 1 381 VAL 381 381 381 VAL VAL A . n 
A 1 382 GLY 382 382 382 GLY GLY A . n 
A 1 383 MET 383 383 383 MET MET A . n 
A 1 384 LEU 384 384 384 LEU LEU A . n 
A 1 385 ALA 385 385 385 ALA ALA A . n 
A 1 386 ALA 386 386 386 ALA ALA A . n 
A 1 387 LEU 387 387 387 LEU LEU A . n 
A 1 388 GLU 388 388 388 GLU GLU A . n 
A 1 389 PHE 389 389 389 PHE PHE A . n 
A 1 390 SER 390 390 390 SER SER A . n 
A 1 391 PRO 391 391 391 PRO PRO A . n 
A 1 392 ALA 392 392 392 ALA ALA A . n 
A 1 393 PRO 393 393 393 PRO PRO A . n 
A 1 394 ALA 394 394 394 ALA ALA A . n 
A 1 395 ARG 395 395 395 ARG ARG A . n 
A 1 396 ARG 396 396 396 ARG ARG A . n 
A 1 397 ALA 397 397 397 ALA ALA A . n 
A 1 398 PHE 398 398 398 PHE PHE A . n 
A 1 399 PHE 399 399 399 PHE PHE A . n 
A 1 400 ASP 400 400 400 ASP ASP A . n 
A 1 401 PRO 401 401 401 PRO PRO A . n 
A 1 402 ALA 402 402 402 ALA ALA A . n 
A 1 403 LEU 403 403 403 LEU LEU A . n 
A 1 404 LYS 404 404 404 LYS LYS A . n 
A 1 405 VAL 405 405 405 VAL VAL A . n 
A 1 406 GLY 406 406 406 GLY GLY A . n 
A 1 407 PRO 407 407 407 PRO PRO A . n 
A 1 408 ARG 408 408 408 ARG ARG A . n 
A 1 409 VAL 409 409 409 VAL VAL A . n 
A 1 410 SER 410 410 410 SER SER A . n 
A 1 411 ALA 411 411 411 ALA ALA A . n 
A 1 412 ALA 412 412 412 ALA ALA A . n 
A 1 413 ALA 413 413 413 ALA ALA A . n 
A 1 414 MET 414 414 414 MET MET A . n 
A 1 415 SER 415 415 415 SER SER A . n 
A 1 416 GLU 416 416 416 GLU GLU A . n 
A 1 417 ASN 417 417 417 ASN ASN A . n 
A 1 418 LEU 418 418 418 LEU LEU A . n 
A 1 419 ILE 419 419 419 ILE ILE A . n 
A 1 420 ALA 420 420 420 ALA ALA A . n 
A 1 421 ARG 421 421 421 ARG ARG A . n 
A 1 422 ALA 422 422 422 ALA ALA A . n 
A 1 423 MET 423 423 423 MET MET A . n 
A 1 424 PRO 424 424 424 PRO PRO A . n 
A 1 425 GLN 425 425 425 GLN GLN A . n 
A 1 426 GLY 426 426 426 GLY GLY A . n 
A 1 427 ASP 427 427 427 ASP ASP A . n 
A 1 428 ILE 428 428 428 ILE ILE A . n 
A 1 429 LEU 429 429 429 LEU LEU A . n 
A 1 430 GLY 430 430 430 GLY GLY A . n 
A 1 431 PHE 431 431 431 PHE PHE A . n 
A 1 432 ALA 432 432 432 ALA ALA A . n 
A 1 433 PRO 433 433 433 PRO PRO A . n 
A 1 434 PRO 434 434 434 PRO PRO A . n 
A 1 435 LEU 435 435 435 LEU LEU A . n 
A 1 436 VAL 436 436 436 VAL VAL A . n 
A 1 437 THR 437 437 437 THR THR A . n 
A 1 438 THR 438 438 438 THR THR A . n 
A 1 439 ARG 439 439 439 ARG ARG A . n 
A 1 440 ALA 440 440 440 ALA ALA A . n 
A 1 441 GLU 441 441 441 GLU GLU A . n 
A 1 442 VAL 442 442 442 VAL VAL A . n 
A 1 443 ASP 443 443 443 ASP ASP A . n 
A 1 444 GLU 444 444 444 GLU GLU A . n 
A 1 445 ILE 445 445 445 ILE ILE A . n 
A 1 446 VAL 446 446 446 VAL VAL A . n 
A 1 447 ALA 447 447 447 ALA ALA A . n 
A 1 448 ARG 448 448 448 ARG ARG A . n 
A 1 449 ALA 449 449 449 ALA ALA A . n 
A 1 450 LYS 450 450 450 LYS LYS A . n 
A 1 451 ARG 451 451 451 ARG ARG A . n 
A 1 452 ALA 452 452 452 ALA ALA A . n 
A 1 453 VAL 453 453 453 VAL VAL A . n 
A 1 454 ASP 454 454 454 ASP ASP A . n 
A 1 455 LYS 455 455 455 LYS LYS A . n 
A 1 456 VAL 456 456 456 VAL VAL A . n 
A 1 457 THR 457 457 457 THR THR A . n 
A 1 458 ASP 458 458 458 ASP ASP A . n 
A 1 459 GLU 459 459 459 GLU GLU A . n 
A 1 460 LEU 460 460 460 LEU LEU A . n 
A 1 461 THR 461 461 461 THR THR A . n 
A 1 462 ARG 462 462 462 ARG ARG A . n 
A 1 463 SER 463 463 463 SER SER A . n 
A 1 464 GLY 464 464 464 GLY GLY A . n 
A 1 465 ASP 465 465 465 ASP ASP A . n 
A 1 466 LEU 466 466 466 LEU LEU A . n 
A 1 467 LYS 467 467 ?   ?   ?   A . n 
A 1 468 ALA 468 468 ?   ?   ?   A . n 
A 1 469 HIS 469 469 ?   ?   ?   A . n 
A 1 470 HIS 470 470 ?   ?   ?   A . n 
A 1 471 HIS 471 471 ?   ?   ?   A . n 
A 1 472 HIS 472 472 ?   ?   ?   A . n 
A 1 473 HIS 473 473 ?   ?   ?   A . n 
A 1 474 HIS 474 474 ?   ?   ?   A . n 
B 2 1   MET 1   1   ?   ?   ?   B . n 
B 2 2   SER 2   2   2   SER SER B . n 
B 2 3   GLN 3   3   3   GLN GLN B . n 
B 2 4   HIS 4   4   4   HIS HIS B . n 
B 2 5   GLN 5   5   5   GLN GLN B . n 
B 2 6   ASN 6   6   6   ASN ASN B . n 
B 2 7   LEU 7   7   7   LEU LEU B . n 
B 2 8   ILE 8   8   8   ILE ILE B . n 
B 2 9   ASP 9   9   9   ASP ASP B . n 
B 2 10  ARG 10  10  10  ARG ARG B . n 
B 2 11  ASP 11  11  11  ASP ASP B . n 
B 2 12  ARG 12  12  12  ARG ARG B . n 
B 2 13  LYS 13  13  13  LYS LYS B . n 
B 2 14  VAL 14  14  14  VAL VAL B . n 
B 2 15  THR 15  15  15  THR THR B . n 
B 2 16  PHE 16  16  16  PHE PHE B . n 
B 2 17  HIS 17  17  17  HIS HIS B . n 
B 2 18  ALA 18  18  18  ALA ALA B . n 
B 2 19  SER 19  19  19  SER SER B . n 
B 2 20  THR 20  20  20  THR THR B . n 
B 2 21  HIS 21  21  21  HIS HIS B . n 
B 2 22  LEU 22  22  22  LEU LEU B . n 
B 2 23  ARG 23  23  23  ARG ARG B . n 
B 2 24  ASP 24  24  24  ASP ASP B . n 
B 2 25  PHE 25  25  25  PHE PHE B . n 
B 2 26  ALA 26  26  26  ALA ALA B . n 
B 2 27  HIS 27  27  27  HIS HIS B . n 
B 2 28  GLY 28  28  28  GLY GLY B . n 
B 2 29  GLU 29  29  29  GLU GLU B . n 
B 2 30  ALA 30  30  30  ALA ALA B . n 
B 2 31  PRO 31  31  31  PRO PRO B . n 
B 2 32  GLY 32  32  32  GLY GLY B . n 
B 2 33  ARG 33  33  33  ARG ARG B . n 
B 2 34  VAL 34  34  34  VAL VAL B . n 
B 2 35  MET 35  35  35  MET MET B . n 
B 2 36  ALA 36  36  36  ALA ALA B . n 
B 2 37  GLY 37  37  37  GLY GLY B . n 
B 2 38  GLY 38  38  38  GLY GLY B . n 
B 2 39  GLU 39  39  39  GLU GLU B . n 
B 2 40  GLY 40  40  40  GLY GLY B . n 
B 2 41  ILE 41  41  41  ILE ILE B . n 
B 2 42  HIS 42  42  42  HIS HIS B . n 
B 2 43  VAL 43  43  43  VAL VAL B . n 
B 2 44  VAL 44  44  44  VAL VAL B . n 
B 2 45  ASP 45  45  45  ASP ASP B . n 
B 2 46  LYS 46  46  46  LYS LYS B . n 
B 2 47  ASP 47  47  47  ASP ASP B . n 
B 2 48  GLY 48  48  48  GLY GLY B . n 
B 2 49  ARG 49  49  49  ARG ARG B . n 
B 2 50  GLU 50  50  50  GLU GLU B . n 
B 2 51  PHE 51  51  51  PHE PHE B . n 
B 2 52  ILE 52  52  52  ILE ILE B . n 
B 2 53  ASP 53  53  53  ASP ASP B . n 
B 2 54  GLY 54  54  54  GLY GLY B . n 
B 2 55  PHE 55  55  55  PHE PHE B . n 
B 2 56  ALA 56  56  56  ALA ALA B . n 
B 2 57  GLY 57  57  57  GLY GLY B . n 
B 2 58  LEU 58  58  58  LEU LEU B . n 
B 2 59  TYR 59  59  59  TYR TYR B . n 
B 2 60  CYS 60  60  60  CYS CYS B . n 
B 2 61  VAL 61  61  61  VAL VAL B . n 
B 2 62  ASN 62  62  62  ASN ASN B . n 
B 2 63  ILE 63  63  63  ILE ILE B . n 
B 2 64  GLY 64  64  64  GLY GLY B . n 
B 2 65  TYR 65  65  65  TYR TYR B . n 
B 2 66  GLY 66  66  66  GLY GLY B . n 
B 2 67  ARG 67  67  67  ARG ARG B . n 
B 2 68  THR 68  68  68  THR THR B . n 
B 2 69  GLU 69  69  69  GLU GLU B . n 
B 2 70  VAL 70  70  70  VAL VAL B . n 
B 2 71  ALA 71  71  71  ALA ALA B . n 
B 2 72  GLU 72  72  72  GLU GLU B . n 
B 2 73  ALA 73  73  73  ALA ALA B . n 
B 2 74  ILE 74  74  74  ILE ILE B . n 
B 2 75  HIS 75  75  75  HIS HIS B . n 
B 2 76  ARG 76  76  76  ARG ARG B . n 
B 2 77  GLN 77  77  77  GLN GLN B . n 
B 2 78  ALA 78  78  78  ALA ALA B . n 
B 2 79  LEU 79  79  79  LEU LEU B . n 
B 2 80  GLU 80  80  80  GLU GLU B . n 
B 2 81  LEU 81  81  81  LEU LEU B . n 
B 2 82  ALA 82  82  82  ALA ALA B . n 
B 2 83  TYR 83  83  83  TYR TYR B . n 
B 2 84  TYR 84  84  84  TYR TYR B . n 
B 2 85  HIS 85  85  85  HIS HIS B . n 
B 2 86  THR 86  86  86  THR THR B . n 
B 2 87  TYR 87  87  87  TYR TYR B . n 
B 2 88  VAL 88  88  88  VAL VAL B . n 
B 2 89  GLY 89  89  89  GLY GLY B . n 
B 2 90  HIS 90  90  90  HIS HIS B . n 
B 2 91  SER 91  91  91  SER SER B . n 
B 2 92  ASN 92  92  92  ASN ASN B . n 
B 2 93  GLU 93  93  93  GLU GLU B . n 
B 2 94  PRO 94  94  94  PRO PRO B . n 
B 2 95  GLN 95  95  95  GLN GLN B . n 
B 2 96  ILE 96  96  96  ILE ILE B . n 
B 2 97  GLN 97  97  97  GLN GLN B . n 
B 2 98  LEU 98  98  98  LEU LEU B . n 
B 2 99  SER 99  99  99  SER SER B . n 
B 2 100 GLU 100 100 100 GLU GLU B . n 
B 2 101 LYS 101 101 101 LYS LYS B . n 
B 2 102 ILE 102 102 102 ILE ILE B . n 
B 2 103 LEU 103 103 103 LEU LEU B . n 
B 2 104 GLU 104 104 104 GLU GLU B . n 
B 2 105 LEU 105 105 105 LEU LEU B . n 
B 2 106 ALA 106 106 106 ALA ALA B . n 
B 2 107 GLY 107 107 107 GLY GLY B . n 
B 2 108 PRO 108 108 108 PRO PRO B . n 
B 2 109 GLY 109 109 109 GLY GLY B . n 
B 2 110 MET 110 110 110 MET MET B . n 
B 2 111 SER 111 111 111 SER SER B . n 
B 2 112 LYS 112 112 112 LYS LYS B . n 
B 2 113 VAL 113 113 113 VAL VAL B . n 
B 2 114 TYR 114 114 114 TYR TYR B . n 
B 2 115 TYR 115 115 115 TYR TYR B . n 
B 2 116 GLY 116 116 116 GLY GLY B . n 
B 2 117 MET 117 117 117 MET MET B . n 
B 2 118 SER 118 118 118 SER SER B . n 
B 2 119 GLY 119 119 119 GLY GLY B . n 
B 2 120 SER 120 120 120 SER SER B . n 
B 2 121 ASP 121 121 121 ASP ASP B . n 
B 2 122 ALA 122 122 122 ALA ALA B . n 
B 2 123 ASN 123 123 123 ASN ASN B . n 
B 2 124 GLU 124 124 124 GLU GLU B . n 
B 2 125 THR 125 125 125 THR THR B . n 
B 2 126 GLN 126 126 126 GLN GLN B . n 
B 2 127 LEU 127 127 127 LEU LEU B . n 
B 2 128 LYS 128 128 128 LYS LYS B . n 
B 2 129 ILE 129 129 129 ILE ILE B . n 
B 2 130 VAL 130 130 130 VAL VAL B . n 
B 2 131 ARG 131 131 131 ARG ARG B . n 
B 2 132 TYR 132 132 132 TYR TYR B . n 
B 2 133 TYR 133 133 133 TYR TYR B . n 
B 2 134 ASN 134 134 134 ASN ASN B . n 
B 2 135 ASN 135 135 135 ASN ASN B . n 
B 2 136 VAL 136 136 136 VAL VAL B . n 
B 2 137 LEU 137 137 137 LEU LEU B . n 
B 2 138 GLY 138 138 138 GLY GLY B . n 
B 2 139 ARG 139 139 139 ARG ARG B . n 
B 2 140 PRO 140 140 140 PRO PRO B . n 
B 2 141 GLN 141 141 141 GLN GLN B . n 
B 2 142 LYS 142 142 142 LYS LYS B . n 
B 2 143 LYS 143 143 143 LYS LYS B . n 
B 2 144 LYS 144 144 144 LYS LYS B . n 
B 2 145 VAL 145 145 145 VAL VAL B . n 
B 2 146 ILE 146 146 146 ILE ILE B . n 
B 2 147 ALA 147 147 147 ALA ALA B . n 
B 2 148 ARG 148 148 148 ARG ARG B . n 
B 2 149 GLN 149 149 149 GLN GLN B . n 
B 2 150 ARG 150 150 150 ARG ARG B . n 
B 2 151 GLY 151 151 151 GLY GLY B . n 
B 2 152 TYR 152 152 152 TYR TYR B . n 
B 2 153 HIS 153 153 153 HIS HIS B . n 
B 2 154 GLY 154 154 154 GLY GLY B . n 
B 2 155 SER 155 155 155 SER SER B . n 
B 2 156 GLY 156 156 156 GLY GLY B . n 
B 2 157 ILE 157 157 157 ILE ILE B . n 
B 2 158 ALA 158 158 158 ALA ALA B . n 
B 2 159 SER 159 159 159 SER SER B . n 
B 2 160 GLY 160 160 160 GLY GLY B . n 
B 2 161 SER 161 161 161 SER SER B . n 
B 2 162 LEU 162 162 162 LEU LEU B . n 
B 2 163 THR 163 163 163 THR THR B . n 
B 2 164 GLY 164 164 164 GLY GLY B . n 
B 2 165 LEU 165 165 165 LEU LEU B . n 
B 2 166 LYS 166 166 166 LYS LYS B . n 
B 2 167 ALA 167 167 167 ALA ALA B . n 
B 2 168 PHE 168 168 168 PHE PHE B . n 
B 2 169 HIS 169 169 169 HIS HIS B . n 
B 2 170 ASP 170 170 170 ASP ASP B . n 
B 2 171 HIS 171 171 171 HIS HIS B . n 
B 2 172 PHE 172 172 172 PHE PHE B . n 
B 2 173 ASP 173 173 173 ASP ASP B . n 
B 2 174 LEU 174 174 174 LEU LEU B . n 
B 2 175 PRO 175 175 175 PRO PRO B . n 
B 2 176 ILE 176 176 176 ILE ILE B . n 
B 2 177 GLU 177 177 177 GLU GLU B . n 
B 2 178 GLY 178 178 178 GLY GLY B . n 
B 2 179 ILE 179 179 179 ILE ILE B . n 
B 2 180 LEU 180 180 180 LEU LEU B . n 
B 2 181 HIS 181 181 181 HIS HIS B . n 
B 2 182 THR 182 182 182 THR THR B . n 
B 2 183 GLU 183 183 183 GLU GLU B . n 
B 2 184 ALA 184 184 184 ALA ALA B . n 
B 2 185 PRO 185 185 185 PRO PRO B . n 
B 2 186 TYR 186 186 186 TYR TYR B . n 
B 2 187 TYR 187 187 187 TYR TYR B . n 
B 2 188 TYR 188 188 188 TYR TYR B . n 
B 2 189 HIS 189 189 189 HIS HIS B . n 
B 2 190 ARG 190 190 190 ARG ARG B . n 
B 2 191 GLY 191 191 191 GLY GLY B . n 
B 2 192 ALA 192 192 192 ALA ALA B . n 
B 2 193 GLU 193 193 193 GLU GLU B . n 
B 2 194 ARG 194 194 194 ARG ARG B . n 
B 2 195 GLU 195 195 195 GLU GLU B . n 
B 2 196 GLY 196 196 196 GLY GLY B . n 
B 2 197 MET 197 197 197 MET MET B . n 
B 2 198 SER 198 198 198 SER SER B . n 
B 2 199 GLU 199 199 199 GLU GLU B . n 
B 2 200 ARG 200 200 200 ARG ARG B . n 
B 2 201 GLU 201 201 201 GLU GLU B . n 
B 2 202 PHE 202 202 202 PHE PHE B . n 
B 2 203 SER 203 203 203 SER SER B . n 
B 2 204 ALA 204 204 204 ALA ALA B . n 
B 2 205 HIS 205 205 205 HIS HIS B . n 
B 2 206 CYS 206 206 206 CYS CYS B . n 
B 2 207 ALA 207 207 207 ALA ALA B . n 
B 2 208 ALA 208 208 208 ALA ALA B . n 
B 2 209 LYS 209 209 209 LYS LYS B . n 
B 2 210 LEU 210 210 210 LEU LEU B . n 
B 2 211 GLU 211 211 211 GLU GLU B . n 
B 2 212 GLU 212 212 212 GLU GLU B . n 
B 2 213 MET 213 213 213 MET MET B . n 
B 2 214 ILE 214 214 214 ILE ILE B . n 
B 2 215 LEU 215 215 215 LEU LEU B . n 
B 2 216 ALA 216 216 216 ALA ALA B . n 
B 2 217 GLU 217 217 217 GLU GLU B . n 
B 2 218 GLY 218 218 218 GLY GLY B . n 
B 2 219 PRO 219 219 219 PRO PRO B . n 
B 2 220 GLU 220 220 220 GLU GLU B . n 
B 2 221 THR 221 221 221 THR THR B . n 
B 2 222 VAL 222 222 222 VAL VAL B . n 
B 2 223 ALA 223 223 223 ALA ALA B . n 
B 2 224 ALA 224 224 224 ALA ALA B . n 
B 2 225 PHE 225 225 225 PHE PHE B . n 
B 2 226 ILE 226 226 226 ILE ILE B . n 
B 2 227 GLY 227 227 227 GLY GLY B . n 
B 2 228 GLU 228 228 228 GLU GLU B . n 
B 2 229 PRO 229 229 229 PRO PRO B . n 
B 2 230 VAL 230 230 230 VAL VAL B . n 
B 2 231 LEU 231 231 231 LEU LEU B . n 
B 2 232 GLY 232 232 232 GLY GLY B . n 
B 2 233 THR 233 233 233 THR THR B . n 
B 2 234 GLY 234 234 234 GLY GLY B . n 
B 2 235 GLY 235 235 235 GLY GLY B . n 
B 2 236 ILE 236 236 236 ILE ILE B . n 
B 2 237 VAL 237 237 237 VAL VAL B . n 
B 2 238 PRO 238 238 238 PRO PRO B . n 
B 2 239 PRO 239 239 239 PRO PRO B . n 
B 2 240 PRO 240 240 240 PRO PRO B . n 
B 2 241 GLU 241 241 241 GLU GLU B . n 
B 2 242 GLY 242 242 242 GLY GLY B . n 
B 2 243 TYR 243 243 243 TYR TYR B . n 
B 2 244 TRP 244 244 244 TRP TRP B . n 
B 2 245 GLU 245 245 245 GLU GLU B . n 
B 2 246 ALA 246 246 246 ALA ALA B . n 
B 2 247 ILE 247 247 247 ILE ILE B . n 
B 2 248 GLN 248 248 248 GLN GLN B . n 
B 2 249 GLY 249 249 249 GLY GLY B . n 
B 2 250 VAL 250 250 250 VAL VAL B . n 
B 2 251 LEU 251 251 251 LEU LEU B . n 
B 2 252 ALA 252 252 252 ALA ALA B . n 
B 2 253 LYS 253 253 253 LYS LYS B . n 
B 2 254 TYR 254 254 254 TYR TYR B . n 
B 2 255 ASP 255 255 255 ASP ASP B . n 
B 2 256 VAL 256 256 256 VAL VAL B . n 
B 2 257 LEU 257 257 257 LEU LEU B . n 
B 2 258 LEU 258 258 258 LEU LEU B . n 
B 2 259 ILE 259 259 259 ILE ILE B . n 
B 2 260 ALA 260 260 260 ALA ALA B . n 
B 2 261 ASP 261 261 261 ASP ASP B . n 
B 2 262 GLU 262 262 262 GLU GLU B . n 
B 2 263 VAL 263 263 263 VAL VAL B . n 
B 2 264 VAL 264 264 264 VAL VAL B . n 
B 2 265 CYS 265 265 265 CYS CYS B . n 
B 2 266 GLY 266 266 266 GLY GLY B . n 
B 2 267 PHE 267 267 267 PHE PHE B . n 
B 2 268 GLY 268 268 268 GLY GLY B . n 
B 2 269 ARG 269 269 269 ARG ARG B . n 
B 2 270 ILE 270 270 270 ILE ILE B . n 
B 2 271 GLY 271 271 271 GLY GLY B . n 
B 2 272 ALA 272 272 272 ALA ALA B . n 
B 2 273 ASP 273 273 273 ASP ASP B . n 
B 2 274 PHE 274 274 274 PHE PHE B . n 
B 2 275 GLY 275 275 275 GLY GLY B . n 
B 2 276 SER 276 276 276 SER SER B . n 
B 2 277 HIS 277 277 277 HIS HIS B . n 
B 2 278 HIS 278 278 278 HIS HIS B . n 
B 2 279 TYR 279 279 279 TYR TYR B . n 
B 2 280 ALA 280 280 280 ALA ALA B . n 
B 2 281 ILE 281 281 281 ILE ILE B . n 
B 2 282 LYS 282 282 282 LYS LYS B . n 
B 2 283 PRO 283 283 283 PRO PRO B . n 
B 2 284 ASP 284 284 284 ASP ASP B . n 
B 2 285 LEU 285 285 285 LEU LEU B . n 
B 2 286 ILE 286 286 286 ILE ILE B . n 
B 2 287 THR 287 287 287 THR THR B . n 
B 2 288 ILE 288 288 288 ILE ILE B . n 
B 2 289 ALA 289 289 289 ALA ALA B . n 
B 2 290 LYS 290 290 290 LYS LYS B . n 
B 2 291 GLY 291 291 291 GLY GLY B . n 
B 2 292 LEU 292 292 292 LEU LEU B . n 
B 2 293 THR 293 293 293 THR THR B . n 
B 2 294 SER 294 294 294 SER SER B . n 
B 2 295 ALA 295 295 295 ALA ALA B . n 
B 2 296 TYR 296 296 296 TYR TYR B . n 
B 2 297 GLN 297 297 297 GLN GLN B . n 
B 2 298 PRO 298 298 298 PRO PRO B . n 
B 2 299 LEU 299 299 299 LEU LEU B . n 
B 2 300 SER 300 300 300 SER SER B . n 
B 2 301 GLY 301 301 301 GLY GLY B . n 
B 2 302 VAL 302 302 302 VAL VAL B . n 
B 2 303 ILE 303 303 303 ILE ILE B . n 
B 2 304 ILE 304 304 304 ILE ILE B . n 
B 2 305 GLY 305 305 305 GLY GLY B . n 
B 2 306 ASP 306 306 306 ASP ASP B . n 
B 2 307 ARG 307 307 307 ARG ARG B . n 
B 2 308 VAL 308 308 308 VAL VAL B . n 
B 2 309 TRP 309 309 309 TRP TRP B . n 
B 2 310 GLN 310 310 310 GLN GLN B . n 
B 2 311 VAL 311 311 311 VAL VAL B . n 
B 2 312 LEU 312 312 312 LEU LEU B . n 
B 2 313 GLU 313 313 313 GLU GLU B . n 
B 2 314 GLN 314 314 314 GLN GLN B . n 
B 2 315 GLY 315 315 315 GLY GLY B . n 
B 2 316 THR 316 316 316 THR THR B . n 
B 2 317 GLY 317 317 317 GLY GLY B . n 
B 2 318 GLU 318 318 318 GLU GLU B . n 
B 2 319 PHE 319 319 319 PHE PHE B . n 
B 2 320 GLY 320 320 320 GLY GLY B . n 
B 2 321 PRO 321 321 321 PRO PRO B . n 
B 2 322 ILE 322 322 322 ILE ILE B . n 
B 2 323 GLY 323 323 323 GLY GLY B . n 
B 2 324 HIS 324 324 324 HIS HIS B . n 
B 2 325 GLY 325 325 325 GLY GLY B . n 
B 2 326 TRP 326 326 326 TRP TRP B . n 
B 2 327 THR 327 327 327 THR THR B . n 
B 2 328 TYR 328 328 328 TYR TYR B . n 
B 2 329 SER 329 329 329 SER SER B . n 
B 2 330 GLY 330 330 330 GLY GLY B . n 
B 2 331 HIS 331 331 331 HIS HIS B . n 
B 2 332 ALA 332 332 332 ALA ALA B . n 
B 2 333 LEU 333 333 333 LEU LEU B . n 
B 2 334 GLY 334 334 334 GLY GLY B . n 
B 2 335 CYS 335 335 335 CYS CYS B . n 
B 2 336 ALA 336 336 336 ALA ALA B . n 
B 2 337 ALA 337 337 337 ALA ALA B . n 
B 2 338 GLY 338 338 338 GLY GLY B . n 
B 2 339 LEU 339 339 339 LEU LEU B . n 
B 2 340 ALA 340 340 340 ALA ALA B . n 
B 2 341 ASN 341 341 341 ASN ASN B . n 
B 2 342 LEU 342 342 342 LEU LEU B . n 
B 2 343 ALA 343 343 343 ALA ALA B . n 
B 2 344 ILE 344 344 344 ILE ILE B . n 
B 2 345 ILE 345 345 345 ILE ILE B . n 
B 2 346 GLU 346 346 346 GLU GLU B . n 
B 2 347 ARG 347 347 347 ARG ARG B . n 
B 2 348 GLU 348 348 348 GLU GLU B . n 
B 2 349 GLY 349 349 349 GLY GLY B . n 
B 2 350 LEU 350 350 350 LEU LEU B . n 
B 2 351 THR 351 351 351 THR THR B . n 
B 2 352 ALA 352 352 352 ALA ALA B . n 
B 2 353 ASN 353 353 353 ASN ASN B . n 
B 2 354 ALA 354 354 354 ALA ALA B . n 
B 2 355 ALA 355 355 355 ALA ALA B . n 
B 2 356 GLU 356 356 356 GLU GLU B . n 
B 2 357 THR 357 357 357 THR THR B . n 
B 2 358 GLY 358 358 358 GLY GLY B . n 
B 2 359 ALA 359 359 359 ALA ALA B . n 
B 2 360 TYR 360 360 360 TYR TYR B . n 
B 2 361 LEU 361 361 361 LEU LEU B . n 
B 2 362 GLN 362 362 362 GLN GLN B . n 
B 2 363 GLN 363 363 363 GLN GLN B . n 
B 2 364 CYS 364 364 364 CYS CYS B . n 
B 2 365 MET 365 365 365 MET MET B . n 
B 2 366 GLN 366 366 366 GLN GLN B . n 
B 2 367 GLN 367 367 367 GLN GLN B . n 
B 2 368 THR 368 368 368 THR THR B . n 
B 2 369 PHE 369 369 369 PHE PHE B . n 
B 2 370 GLY 370 370 370 GLY GLY B . n 
B 2 371 GLU 371 371 371 GLU GLU B . n 
B 2 372 HIS 372 372 372 HIS HIS B . n 
B 2 373 PRO 373 373 373 PRO PRO B . n 
B 2 374 LEU 374 374 374 LEU LEU B . n 
B 2 375 VAL 375 375 375 VAL VAL B . n 
B 2 376 GLY 376 376 376 GLY GLY B . n 
B 2 377 GLU 377 377 377 GLU GLU B . n 
B 2 378 VAL 378 378 378 VAL VAL B . n 
B 2 379 ARG 379 379 379 ARG ARG B . n 
B 2 380 GLY 380 380 380 GLY GLY B . n 
B 2 381 VAL 381 381 381 VAL VAL B . n 
B 2 382 GLY 382 382 382 GLY GLY B . n 
B 2 383 MET 383 383 383 MET MET B . n 
B 2 384 LEU 384 384 384 LEU LEU B . n 
B 2 385 ALA 385 385 385 ALA ALA B . n 
B 2 386 ALA 386 386 386 ALA ALA B . n 
B 2 387 LEU 387 387 387 LEU LEU B . n 
B 2 388 GLU 388 388 388 GLU GLU B . n 
B 2 389 PHE 389 389 389 PHE PHE B . n 
B 2 390 SER 390 390 390 SER SER B . n 
B 2 391 PRO 391 391 391 PRO PRO B . n 
B 2 392 ALA 392 392 392 ALA ALA B . n 
B 2 393 PRO 393 393 393 PRO PRO B . n 
B 2 394 ALA 394 394 394 ALA ALA B . n 
B 2 395 ARG 395 395 395 ARG ARG B . n 
B 2 396 ARG 396 396 396 ARG ARG B . n 
B 2 397 ALA 397 397 397 ALA ALA B . n 
B 2 398 PHE 398 398 398 PHE PHE B . n 
B 2 399 PHE 399 399 399 PHE PHE B . n 
B 2 400 ASP 400 400 400 ASP ASP B . n 
B 2 401 PRO 401 401 401 PRO PRO B . n 
B 2 402 ALA 402 402 402 ALA ALA B . n 
B 2 403 LEU 403 403 403 LEU LEU B . n 
B 2 404 LYS 404 404 404 LYS LYS B . n 
B 2 405 VAL 405 405 405 VAL VAL B . n 
B 2 406 GLY 406 406 406 GLY GLY B . n 
B 2 407 PRO 407 407 407 PRO PRO B . n 
B 2 408 ARG 408 408 408 ARG ARG B . n 
B 2 409 VAL 409 409 409 VAL VAL B . n 
B 2 410 SER 410 410 410 SER SER B . n 
B 2 411 ALA 411 411 411 ALA ALA B . n 
B 2 412 ALA 412 412 412 ALA ALA B . n 
B 2 413 ALA 413 413 413 ALA ALA B . n 
B 2 414 MET 414 414 414 MET MET B . n 
B 2 415 SER 415 415 415 SER SER B . n 
B 2 416 GLU 416 416 416 GLU GLU B . n 
B 2 417 ASN 417 417 417 ASN ASN B . n 
B 2 418 LEU 418 418 418 LEU LEU B . n 
B 2 419 ILE 419 419 419 ILE ILE B . n 
B 2 420 ALA 420 420 420 ALA ALA B . n 
B 2 421 ARG 421 421 421 ARG ARG B . n 
B 2 422 ALA 422 422 422 ALA ALA B . n 
B 2 423 MET 423 423 423 MET MET B . n 
B 2 424 PRO 424 424 424 PRO PRO B . n 
B 2 425 GLN 425 425 425 GLN GLN B . n 
B 2 426 GLY 426 426 426 GLY GLY B . n 
B 2 427 ASP 427 427 427 ASP ASP B . n 
B 2 428 ILE 428 428 428 ILE ILE B . n 
B 2 429 LEU 429 429 429 LEU LEU B . n 
B 2 430 GLY 430 430 430 GLY GLY B . n 
B 2 431 PHE 431 431 431 PHE PHE B . n 
B 2 432 ALA 432 432 432 ALA ALA B . n 
B 2 433 PRO 433 433 433 PRO PRO B . n 
B 2 434 PRO 434 434 434 PRO PRO B . n 
B 2 435 LEU 435 435 435 LEU LEU B . n 
B 2 436 VAL 436 436 436 VAL VAL B . n 
B 2 437 THR 437 437 437 THR THR B . n 
B 2 438 THR 438 438 438 THR THR B . n 
B 2 439 ARG 439 439 439 ARG ARG B . n 
B 2 440 ALA 440 440 440 ALA ALA B . n 
B 2 441 GLU 441 441 441 GLU GLU B . n 
B 2 442 VAL 442 442 442 VAL VAL B . n 
B 2 443 ASP 443 443 443 ASP ASP B . n 
B 2 444 GLU 444 444 444 GLU GLU B . n 
B 2 445 ILE 445 445 445 ILE ILE B . n 
B 2 446 VAL 446 446 446 VAL VAL B . n 
B 2 447 ALA 447 447 447 ALA ALA B . n 
B 2 448 ARG 448 448 448 ARG ARG B . n 
B 2 449 ALA 449 449 449 ALA ALA B . n 
B 2 450 LYS 450 450 450 LYS LYS B . n 
B 2 451 ARG 451 451 451 ARG ARG B . n 
B 2 452 ALA 452 452 452 ALA ALA B . n 
B 2 453 VAL 453 453 453 VAL VAL B . n 
B 2 454 ASP 454 454 454 ASP ASP B . n 
B 2 455 LYS 455 455 455 LYS LYS B . n 
B 2 456 VAL 456 456 456 VAL VAL B . n 
B 2 457 THR 457 457 457 THR THR B . n 
B 2 458 ASP 458 458 458 ASP ASP B . n 
B 2 459 GLU 459 459 459 GLU GLU B . n 
B 2 460 LEU 460 460 460 LEU LEU B . n 
B 2 461 THR 461 461 461 THR THR B . n 
B 2 462 ARG 462 462 462 ARG ARG B . n 
B 2 463 SER 463 463 463 SER SER B . n 
B 2 464 GLY 464 464 464 GLY GLY B . n 
B 2 465 ASP 465 465 465 ASP ASP B . n 
B 2 466 LEU 466 466 466 LEU LEU B . n 
B 2 467 LYS 467 467 ?   ?   ?   B . n 
B 2 468 ALA 468 468 ?   ?   ?   B . n 
B 2 469 HIS 469 469 ?   ?   ?   B . n 
B 2 470 HIS 470 470 ?   ?   ?   B . n 
B 2 471 HIS 471 471 ?   ?   ?   B . n 
B 2 472 HIS 472 472 ?   ?   ?   B . n 
B 2 473 HIS 473 473 ?   ?   ?   B . n 
B 2 474 HIS 474 474 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        LLP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   LLP 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 GOL 1   501  1    GOL GOL A . 
D 3 GOL 1   502  2    GOL GOL A . 
E 3 GOL 1   503  5    GOL GOL A . 
F 3 GOL 1   504  6    GOL GOL A . 
G 3 GOL 1   501  9    GOL GOL B . 
H 4 PLP 1   502  1    PLP PLP B . 
I 5 HOH 1   601  820  HOH HOH A . 
I 5 HOH 2   602  1148 HOH HOH A . 
I 5 HOH 3   603  935  HOH HOH A . 
I 5 HOH 4   604  1072 HOH HOH A . 
I 5 HOH 5   605  1057 HOH HOH A . 
I 5 HOH 6   606  1100 HOH HOH A . 
I 5 HOH 7   607  969  HOH HOH A . 
I 5 HOH 8   608  674  HOH HOH A . 
I 5 HOH 9   609  1089 HOH HOH A . 
I 5 HOH 10  610  945  HOH HOH A . 
I 5 HOH 11  611  1227 HOH HOH A . 
I 5 HOH 12  612  1111 HOH HOH A . 
I 5 HOH 13  613  54   HOH HOH A . 
I 5 HOH 14  614  1202 HOH HOH A . 
I 5 HOH 15  615  1081 HOH HOH A . 
I 5 HOH 16  616  439  HOH HOH A . 
I 5 HOH 17  617  1235 HOH HOH A . 
I 5 HOH 18  618  737  HOH HOH A . 
I 5 HOH 19  619  521  HOH HOH A . 
I 5 HOH 20  620  733  HOH HOH A . 
I 5 HOH 21  621  894  HOH HOH A . 
I 5 HOH 22  622  477  HOH HOH A . 
I 5 HOH 23  623  817  HOH HOH A . 
I 5 HOH 24  624  905  HOH HOH A . 
I 5 HOH 25  625  607  HOH HOH A . 
I 5 HOH 26  626  1114 HOH HOH A . 
I 5 HOH 27  627  898  HOH HOH A . 
I 5 HOH 28  628  124  HOH HOH A . 
I 5 HOH 29  629  455  HOH HOH A . 
I 5 HOH 30  630  313  HOH HOH A . 
I 5 HOH 31  631  1239 HOH HOH A . 
I 5 HOH 32  632  144  HOH HOH A . 
I 5 HOH 33  633  664  HOH HOH A . 
I 5 HOH 34  634  99   HOH HOH A . 
I 5 HOH 35  635  456  HOH HOH A . 
I 5 HOH 36  636  409  HOH HOH A . 
I 5 HOH 37  637  560  HOH HOH A . 
I 5 HOH 38  638  355  HOH HOH A . 
I 5 HOH 39  639  778  HOH HOH A . 
I 5 HOH 40  640  235  HOH HOH A . 
I 5 HOH 41  641  6    HOH HOH A . 
I 5 HOH 42  642  344  HOH HOH A . 
I 5 HOH 43  643  240  HOH HOH A . 
I 5 HOH 44  644  698  HOH HOH A . 
I 5 HOH 45  645  391  HOH HOH A . 
I 5 HOH 46  646  471  HOH HOH A . 
I 5 HOH 47  647  236  HOH HOH A . 
I 5 HOH 48  648  637  HOH HOH A . 
I 5 HOH 49  649  227  HOH HOH A . 
I 5 HOH 50  650  873  HOH HOH A . 
I 5 HOH 51  651  742  HOH HOH A . 
I 5 HOH 52  652  579  HOH HOH A . 
I 5 HOH 53  653  520  HOH HOH A . 
I 5 HOH 54  654  798  HOH HOH A . 
I 5 HOH 55  655  857  HOH HOH A . 
I 5 HOH 56  656  353  HOH HOH A . 
I 5 HOH 57  657  403  HOH HOH A . 
I 5 HOH 58  658  370  HOH HOH A . 
I 5 HOH 59  659  190  HOH HOH A . 
I 5 HOH 60  660  365  HOH HOH A . 
I 5 HOH 61  661  842  HOH HOH A . 
I 5 HOH 62  662  257  HOH HOH A . 
I 5 HOH 63  663  15   HOH HOH A . 
I 5 HOH 64  664  1126 HOH HOH A . 
I 5 HOH 65  665  406  HOH HOH A . 
I 5 HOH 66  666  303  HOH HOH A . 
I 5 HOH 67  667  553  HOH HOH A . 
I 5 HOH 68  668  132  HOH HOH A . 
I 5 HOH 69  669  338  HOH HOH A . 
I 5 HOH 70  670  165  HOH HOH A . 
I 5 HOH 71  671  533  HOH HOH A . 
I 5 HOH 72  672  369  HOH HOH A . 
I 5 HOH 73  673  592  HOH HOH A . 
I 5 HOH 74  674  279  HOH HOH A . 
I 5 HOH 75  675  68   HOH HOH A . 
I 5 HOH 76  676  361  HOH HOH A . 
I 5 HOH 77  677  423  HOH HOH A . 
I 5 HOH 78  678  334  HOH HOH A . 
I 5 HOH 79  679  93   HOH HOH A . 
I 5 HOH 80  680  511  HOH HOH A . 
I 5 HOH 81  681  156  HOH HOH A . 
I 5 HOH 82  682  411  HOH HOH A . 
I 5 HOH 83  683  1152 HOH HOH A . 
I 5 HOH 84  684  701  HOH HOH A . 
I 5 HOH 85  685  77   HOH HOH A . 
I 5 HOH 86  686  1144 HOH HOH A . 
I 5 HOH 87  687  1237 HOH HOH A . 
I 5 HOH 88  688  310  HOH HOH A . 
I 5 HOH 89  689  79   HOH HOH A . 
I 5 HOH 90  690  383  HOH HOH A . 
I 5 HOH 91  691  999  HOH HOH A . 
I 5 HOH 92  692  495  HOH HOH A . 
I 5 HOH 93  693  37   HOH HOH A . 
I 5 HOH 94  694  87   HOH HOH A . 
I 5 HOH 95  695  297  HOH HOH A . 
I 5 HOH 96  696  1067 HOH HOH A . 
I 5 HOH 97  697  502  HOH HOH A . 
I 5 HOH 98  698  586  HOH HOH A . 
I 5 HOH 99  699  290  HOH HOH A . 
I 5 HOH 100 700  890  HOH HOH A . 
I 5 HOH 101 701  101  HOH HOH A . 
I 5 HOH 102 702  16   HOH HOH A . 
I 5 HOH 103 703  189  HOH HOH A . 
I 5 HOH 104 704  652  HOH HOH A . 
I 5 HOH 105 705  26   HOH HOH A . 
I 5 HOH 106 706  643  HOH HOH A . 
I 5 HOH 107 707  89   HOH HOH A . 
I 5 HOH 108 708  304  HOH HOH A . 
I 5 HOH 109 709  670  HOH HOH A . 
I 5 HOH 110 710  785  HOH HOH A . 
I 5 HOH 111 711  287  HOH HOH A . 
I 5 HOH 112 712  237  HOH HOH A . 
I 5 HOH 113 713  105  HOH HOH A . 
I 5 HOH 114 714  1174 HOH HOH A . 
I 5 HOH 115 715  206  HOH HOH A . 
I 5 HOH 116 716  212  HOH HOH A . 
I 5 HOH 117 717  834  HOH HOH A . 
I 5 HOH 118 718  95   HOH HOH A . 
I 5 HOH 119 719  8    HOH HOH A . 
I 5 HOH 120 720  1199 HOH HOH A . 
I 5 HOH 121 721  1064 HOH HOH A . 
I 5 HOH 122 722  281  HOH HOH A . 
I 5 HOH 123 723  700  HOH HOH A . 
I 5 HOH 124 724  538  HOH HOH A . 
I 5 HOH 125 725  358  HOH HOH A . 
I 5 HOH 126 726  510  HOH HOH A . 
I 5 HOH 127 727  252  HOH HOH A . 
I 5 HOH 128 728  27   HOH HOH A . 
I 5 HOH 129 729  844  HOH HOH A . 
I 5 HOH 130 730  505  HOH HOH A . 
I 5 HOH 131 731  5    HOH HOH A . 
I 5 HOH 132 732  50   HOH HOH A . 
I 5 HOH 133 733  273  HOH HOH A . 
I 5 HOH 134 734  345  HOH HOH A . 
I 5 HOH 135 735  265  HOH HOH A . 
I 5 HOH 136 736  86   HOH HOH A . 
I 5 HOH 137 737  609  HOH HOH A . 
I 5 HOH 138 738  154  HOH HOH A . 
I 5 HOH 139 739  1065 HOH HOH A . 
I 5 HOH 140 740  608  HOH HOH A . 
I 5 HOH 141 741  1223 HOH HOH A . 
I 5 HOH 142 742  45   HOH HOH A . 
I 5 HOH 143 743  300  HOH HOH A . 
I 5 HOH 144 744  414  HOH HOH A . 
I 5 HOH 145 745  573  HOH HOH A . 
I 5 HOH 146 746  108  HOH HOH A . 
I 5 HOH 147 747  574  HOH HOH A . 
I 5 HOH 148 748  128  HOH HOH A . 
I 5 HOH 149 749  81   HOH HOH A . 
I 5 HOH 150 750  320  HOH HOH A . 
I 5 HOH 151 751  942  HOH HOH A . 
I 5 HOH 152 752  192  HOH HOH A . 
I 5 HOH 153 753  1123 HOH HOH A . 
I 5 HOH 154 754  938  HOH HOH A . 
I 5 HOH 155 755  384  HOH HOH A . 
I 5 HOH 156 756  276  HOH HOH A . 
I 5 HOH 157 757  751  HOH HOH A . 
I 5 HOH 158 758  90   HOH HOH A . 
I 5 HOH 159 759  76   HOH HOH A . 
I 5 HOH 160 760  91   HOH HOH A . 
I 5 HOH 161 761  7    HOH HOH A . 
I 5 HOH 162 762  336  HOH HOH A . 
I 5 HOH 163 763  659  HOH HOH A . 
I 5 HOH 164 764  268  HOH HOH A . 
I 5 HOH 165 765  52   HOH HOH A . 
I 5 HOH 166 766  517  HOH HOH A . 
I 5 HOH 167 767  1205 HOH HOH A . 
I 5 HOH 168 768  283  HOH HOH A . 
I 5 HOH 169 769  168  HOH HOH A . 
I 5 HOH 170 770  160  HOH HOH A . 
I 5 HOH 171 771  759  HOH HOH A . 
I 5 HOH 172 772  743  HOH HOH A . 
I 5 HOH 173 773  428  HOH HOH A . 
I 5 HOH 174 774  65   HOH HOH A . 
I 5 HOH 175 775  371  HOH HOH A . 
I 5 HOH 176 776  1079 HOH HOH A . 
I 5 HOH 177 777  74   HOH HOH A . 
I 5 HOH 178 778  957  HOH HOH A . 
I 5 HOH 179 779  634  HOH HOH A . 
I 5 HOH 180 780  444  HOH HOH A . 
I 5 HOH 181 781  222  HOH HOH A . 
I 5 HOH 182 782  1107 HOH HOH A . 
I 5 HOH 183 783  509  HOH HOH A . 
I 5 HOH 184 784  216  HOH HOH A . 
I 5 HOH 185 785  182  HOH HOH A . 
I 5 HOH 186 786  928  HOH HOH A . 
I 5 HOH 187 787  67   HOH HOH A . 
I 5 HOH 188 788  32   HOH HOH A . 
I 5 HOH 189 789  556  HOH HOH A . 
I 5 HOH 190 790  134  HOH HOH A . 
I 5 HOH 191 791  308  HOH HOH A . 
I 5 HOH 192 792  218  HOH HOH A . 
I 5 HOH 193 793  584  HOH HOH A . 
I 5 HOH 194 794  558  HOH HOH A . 
I 5 HOH 195 795  426  HOH HOH A . 
I 5 HOH 196 796  261  HOH HOH A . 
I 5 HOH 197 797  465  HOH HOH A . 
I 5 HOH 198 798  658  HOH HOH A . 
I 5 HOH 199 799  170  HOH HOH A . 
I 5 HOH 200 800  501  HOH HOH A . 
I 5 HOH 201 801  198  HOH HOH A . 
I 5 HOH 202 802  71   HOH HOH A . 
I 5 HOH 203 803  822  HOH HOH A . 
I 5 HOH 204 804  454  HOH HOH A . 
I 5 HOH 205 805  366  HOH HOH A . 
I 5 HOH 206 806  121  HOH HOH A . 
I 5 HOH 207 807  339  HOH HOH A . 
I 5 HOH 208 808  263  HOH HOH A . 
I 5 HOH 209 809  254  HOH HOH A . 
I 5 HOH 210 810  133  HOH HOH A . 
I 5 HOH 211 811  269  HOH HOH A . 
I 5 HOH 212 812  161  HOH HOH A . 
I 5 HOH 213 813  1086 HOH HOH A . 
I 5 HOH 214 814  451  HOH HOH A . 
I 5 HOH 215 815  402  HOH HOH A . 
I 5 HOH 216 816  562  HOH HOH A . 
I 5 HOH 217 817  253  HOH HOH A . 
I 5 HOH 218 818  639  HOH HOH A . 
I 5 HOH 219 819  535  HOH HOH A . 
I 5 HOH 220 820  430  HOH HOH A . 
I 5 HOH 221 821  18   HOH HOH A . 
I 5 HOH 222 822  407  HOH HOH A . 
I 5 HOH 223 823  83   HOH HOH A . 
I 5 HOH 224 824  1051 HOH HOH A . 
I 5 HOH 225 825  1087 HOH HOH A . 
I 5 HOH 226 826  4    HOH HOH A . 
I 5 HOH 227 827  64   HOH HOH A . 
I 5 HOH 228 828  199  HOH HOH A . 
I 5 HOH 229 829  620  HOH HOH A . 
I 5 HOH 230 830  1178 HOH HOH A . 
I 5 HOH 231 831  38   HOH HOH A . 
I 5 HOH 232 832  490  HOH HOH A . 
I 5 HOH 233 833  478  HOH HOH A . 
I 5 HOH 234 834  1154 HOH HOH A . 
I 5 HOH 235 835  475  HOH HOH A . 
I 5 HOH 236 836  622  HOH HOH A . 
I 5 HOH 237 837  719  HOH HOH A . 
I 5 HOH 238 838  260  HOH HOH A . 
I 5 HOH 239 839  958  HOH HOH A . 
I 5 HOH 240 840  135  HOH HOH A . 
I 5 HOH 241 841  193  HOH HOH A . 
I 5 HOH 242 842  332  HOH HOH A . 
I 5 HOH 243 843  364  HOH HOH A . 
I 5 HOH 244 844  321  HOH HOH A . 
I 5 HOH 245 845  845  HOH HOH A . 
I 5 HOH 246 846  618  HOH HOH A . 
I 5 HOH 247 847  267  HOH HOH A . 
I 5 HOH 248 848  69   HOH HOH A . 
I 5 HOH 249 849  102  HOH HOH A . 
I 5 HOH 250 850  311  HOH HOH A . 
I 5 HOH 251 851  19   HOH HOH A . 
I 5 HOH 252 852  959  HOH HOH A . 
I 5 HOH 253 853  885  HOH HOH A . 
I 5 HOH 254 854  591  HOH HOH A . 
I 5 HOH 255 855  322  HOH HOH A . 
I 5 HOH 256 856  13   HOH HOH A . 
I 5 HOH 257 857  256  HOH HOH A . 
I 5 HOH 258 858  151  HOH HOH A . 
I 5 HOH 259 859  518  HOH HOH A . 
I 5 HOH 260 860  39   HOH HOH A . 
I 5 HOH 261 861  413  HOH HOH A . 
I 5 HOH 262 862  1068 HOH HOH A . 
I 5 HOH 263 863  82   HOH HOH A . 
I 5 HOH 264 864  20   HOH HOH A . 
I 5 HOH 265 865  457  HOH HOH A . 
I 5 HOH 266 866  270  HOH HOH A . 
I 5 HOH 267 867  155  HOH HOH A . 
I 5 HOH 268 868  823  HOH HOH A . 
I 5 HOH 269 869  909  HOH HOH A . 
I 5 HOH 270 870  306  HOH HOH A . 
I 5 HOH 271 871  9    HOH HOH A . 
I 5 HOH 272 872  259  HOH HOH A . 
I 5 HOH 273 873  379  HOH HOH A . 
I 5 HOH 274 874  707  HOH HOH A . 
I 5 HOH 275 875  644  HOH HOH A . 
I 5 HOH 276 876  1040 HOH HOH A . 
I 5 HOH 277 877  800  HOH HOH A . 
I 5 HOH 278 878  768  HOH HOH A . 
I 5 HOH 279 879  109  HOH HOH A . 
I 5 HOH 280 880  696  HOH HOH A . 
I 5 HOH 281 881  581  HOH HOH A . 
I 5 HOH 282 882  191  HOH HOH A . 
I 5 HOH 283 883  624  HOH HOH A . 
I 5 HOH 284 884  837  HOH HOH A . 
I 5 HOH 285 885  1085 HOH HOH A . 
I 5 HOH 286 886  152  HOH HOH A . 
I 5 HOH 287 887  499  HOH HOH A . 
I 5 HOH 288 888  153  HOH HOH A . 
I 5 HOH 289 889  710  HOH HOH A . 
I 5 HOH 290 890  335  HOH HOH A . 
I 5 HOH 291 891  234  HOH HOH A . 
I 5 HOH 292 892  80   HOH HOH A . 
I 5 HOH 293 893  625  HOH HOH A . 
I 5 HOH 294 894  1228 HOH HOH A . 
I 5 HOH 295 895  1192 HOH HOH A . 
I 5 HOH 296 896  46   HOH HOH A . 
I 5 HOH 297 897  130  HOH HOH A . 
I 5 HOH 298 898  211  HOH HOH A . 
I 5 HOH 299 899  207  HOH HOH A . 
I 5 HOH 300 900  744  HOH HOH A . 
I 5 HOH 301 901  291  HOH HOH A . 
I 5 HOH 302 902  1203 HOH HOH A . 
I 5 HOH 303 903  775  HOH HOH A . 
I 5 HOH 304 904  389  HOH HOH A . 
I 5 HOH 305 905  342  HOH HOH A . 
I 5 HOH 306 906  285  HOH HOH A . 
I 5 HOH 307 907  1069 HOH HOH A . 
I 5 HOH 308 908  319  HOH HOH A . 
I 5 HOH 309 909  158  HOH HOH A . 
I 5 HOH 310 910  871  HOH HOH A . 
I 5 HOH 311 911  122  HOH HOH A . 
I 5 HOH 312 912  1029 HOH HOH A . 
I 5 HOH 313 913  1037 HOH HOH A . 
I 5 HOH 314 914  316  HOH HOH A . 
I 5 HOH 315 915  667  HOH HOH A . 
I 5 HOH 316 916  1210 HOH HOH A . 
I 5 HOH 317 917  171  HOH HOH A . 
I 5 HOH 318 918  286  HOH HOH A . 
I 5 HOH 319 919  280  HOH HOH A . 
I 5 HOH 320 920  1000 HOH HOH A . 
I 5 HOH 321 921  461  HOH HOH A . 
I 5 HOH 322 922  1171 HOH HOH A . 
I 5 HOH 323 923  202  HOH HOH A . 
I 5 HOH 324 924  231  HOH HOH A . 
I 5 HOH 325 925  850  HOH HOH A . 
I 5 HOH 326 926  1234 HOH HOH A . 
I 5 HOH 327 927  453  HOH HOH A . 
I 5 HOH 328 928  1218 HOH HOH A . 
I 5 HOH 329 929  174  HOH HOH A . 
I 5 HOH 330 930  918  HOH HOH A . 
I 5 HOH 331 931  196  HOH HOH A . 
I 5 HOH 332 932  246  HOH HOH A . 
I 5 HOH 333 933  173  HOH HOH A . 
I 5 HOH 334 934  70   HOH HOH A . 
I 5 HOH 335 935  360  HOH HOH A . 
I 5 HOH 336 936  662  HOH HOH A . 
I 5 HOH 337 937  325  HOH HOH A . 
I 5 HOH 338 938  47   HOH HOH A . 
I 5 HOH 339 939  146  HOH HOH A . 
I 5 HOH 340 940  740  HOH HOH A . 
I 5 HOH 341 941  1175 HOH HOH A . 
I 5 HOH 342 942  922  HOH HOH A . 
I 5 HOH 343 943  463  HOH HOH A . 
I 5 HOH 344 944  424  HOH HOH A . 
I 5 HOH 345 945  641  HOH HOH A . 
I 5 HOH 346 946  519  HOH HOH A . 
I 5 HOH 347 947  203  HOH HOH A . 
I 5 HOH 348 948  657  HOH HOH A . 
I 5 HOH 349 949  392  HOH HOH A . 
I 5 HOH 350 950  214  HOH HOH A . 
I 5 HOH 351 951  1134 HOH HOH A . 
I 5 HOH 352 952  474  HOH HOH A . 
I 5 HOH 353 953  258  HOH HOH A . 
I 5 HOH 354 954  116  HOH HOH A . 
I 5 HOH 355 955  1135 HOH HOH A . 
I 5 HOH 356 956  131  HOH HOH A . 
I 5 HOH 357 957  755  HOH HOH A . 
I 5 HOH 358 958  588  HOH HOH A . 
I 5 HOH 359 959  57   HOH HOH A . 
I 5 HOH 360 960  385  HOH HOH A . 
I 5 HOH 361 961  985  HOH HOH A . 
I 5 HOH 362 962  1181 HOH HOH A . 
I 5 HOH 363 963  595  HOH HOH A . 
I 5 HOH 364 964  88   HOH HOH A . 
I 5 HOH 365 965  1108 HOH HOH A . 
I 5 HOH 366 966  684  HOH HOH A . 
I 5 HOH 367 967  459  HOH HOH A . 
I 5 HOH 368 968  1043 HOH HOH A . 
I 5 HOH 369 969  956  HOH HOH A . 
I 5 HOH 370 970  638  HOH HOH A . 
I 5 HOH 371 971  1170 HOH HOH A . 
I 5 HOH 372 972  745  HOH HOH A . 
I 5 HOH 373 973  995  HOH HOH A . 
I 5 HOH 374 974  630  HOH HOH A . 
I 5 HOH 375 975  754  HOH HOH A . 
I 5 HOH 376 976  357  HOH HOH A . 
I 5 HOH 377 977  1023 HOH HOH A . 
I 5 HOH 378 978  726  HOH HOH A . 
I 5 HOH 379 979  688  HOH HOH A . 
I 5 HOH 380 980  1062 HOH HOH A . 
I 5 HOH 381 981  566  HOH HOH A . 
I 5 HOH 382 982  635  HOH HOH A . 
I 5 HOH 383 983  570  HOH HOH A . 
I 5 HOH 384 984  1182 HOH HOH A . 
I 5 HOH 385 985  488  HOH HOH A . 
I 5 HOH 386 986  677  HOH HOH A . 
I 5 HOH 387 987  541  HOH HOH A . 
I 5 HOH 388 988  140  HOH HOH A . 
I 5 HOH 389 989  417  HOH HOH A . 
I 5 HOH 390 990  788  HOH HOH A . 
I 5 HOH 391 991  301  HOH HOH A . 
I 5 HOH 392 992  1039 HOH HOH A . 
I 5 HOH 393 993  882  HOH HOH A . 
I 5 HOH 394 994  172  HOH HOH A . 
I 5 HOH 395 995  163  HOH HOH A . 
I 5 HOH 396 996  1124 HOH HOH A . 
I 5 HOH 397 997  1014 HOH HOH A . 
I 5 HOH 398 998  805  HOH HOH A . 
I 5 HOH 399 999  33   HOH HOH A . 
I 5 HOH 400 1000 920  HOH HOH A . 
I 5 HOH 401 1001 872  HOH HOH A . 
I 5 HOH 402 1002 982  HOH HOH A . 
I 5 HOH 403 1003 145  HOH HOH A . 
I 5 HOH 404 1004 927  HOH HOH A . 
I 5 HOH 405 1005 720  HOH HOH A . 
I 5 HOH 406 1006 783  HOH HOH A . 
I 5 HOH 407 1007 963  HOH HOH A . 
I 5 HOH 408 1008 1176 HOH HOH A . 
I 5 HOH 409 1009 911  HOH HOH A . 
I 5 HOH 410 1010 1032 HOH HOH A . 
I 5 HOH 411 1011 1179 HOH HOH A . 
I 5 HOH 412 1012 489  HOH HOH A . 
I 5 HOH 413 1013 896  HOH HOH A . 
I 5 HOH 414 1014 449  HOH HOH A . 
I 5 HOH 415 1015 647  HOH HOH A . 
I 5 HOH 416 1016 758  HOH HOH A . 
I 5 HOH 417 1017 142  HOH HOH A . 
I 5 HOH 418 1018 1172 HOH HOH A . 
I 5 HOH 419 1019 179  HOH HOH A . 
I 5 HOH 420 1020 460  HOH HOH A . 
I 5 HOH 421 1021 767  HOH HOH A . 
I 5 HOH 422 1022 809  HOH HOH A . 
I 5 HOH 423 1023 1197 HOH HOH A . 
I 5 HOH 424 1024 692  HOH HOH A . 
I 5 HOH 425 1025 1050 HOH HOH A . 
I 5 HOH 426 1026 632  HOH HOH A . 
I 5 HOH 427 1027 1238 HOH HOH A . 
I 5 HOH 428 1028 971  HOH HOH A . 
I 5 HOH 429 1029 929  HOH HOH A . 
I 5 HOH 430 1030 739  HOH HOH A . 
I 5 HOH 431 1031 1169 HOH HOH A . 
I 5 HOH 432 1032 777  HOH HOH A . 
I 5 HOH 433 1033 717  HOH HOH A . 
I 5 HOH 434 1034 1025 HOH HOH A . 
I 5 HOH 435 1035 2    HOH HOH A . 
I 5 HOH 436 1036 1055 HOH HOH A . 
I 5 HOH 437 1037 781  HOH HOH A . 
I 5 HOH 438 1038 997  HOH HOH A . 
I 5 HOH 439 1039 1073 HOH HOH A . 
I 5 HOH 440 1040 924  HOH HOH A . 
I 5 HOH 441 1041 331  HOH HOH A . 
I 5 HOH 442 1042 757  HOH HOH A . 
I 5 HOH 443 1043 912  HOH HOH A . 
I 5 HOH 444 1044 1187 HOH HOH A . 
I 5 HOH 445 1045 516  HOH HOH A . 
I 5 HOH 446 1046 831  HOH HOH A . 
I 5 HOH 447 1047 716  HOH HOH A . 
I 5 HOH 448 1048 1150 HOH HOH A . 
I 5 HOH 449 1049 1219 HOH HOH A . 
I 5 HOH 450 1050 864  HOH HOH A . 
I 5 HOH 451 1051 732  HOH HOH A . 
I 5 HOH 452 1052 972  HOH HOH A . 
I 5 HOH 453 1053 1191 HOH HOH A . 
I 5 HOH 454 1054 869  HOH HOH A . 
I 5 HOH 455 1055 649  HOH HOH A . 
I 5 HOH 456 1056 44   HOH HOH A . 
I 5 HOH 457 1057 1117 HOH HOH A . 
I 5 HOH 458 1058 367  HOH HOH A . 
I 5 HOH 459 1059 904  HOH HOH A . 
I 5 HOH 460 1060 989  HOH HOH A . 
I 5 HOH 461 1061 672  HOH HOH A . 
I 5 HOH 462 1062 921  HOH HOH A . 
I 5 HOH 463 1063 1122 HOH HOH A . 
I 5 HOH 464 1064 694  HOH HOH A . 
I 5 HOH 465 1065 797  HOH HOH A . 
I 5 HOH 466 1066 1046 HOH HOH A . 
I 5 HOH 467 1067 965  HOH HOH A . 
I 5 HOH 468 1068 480  HOH HOH A . 
I 5 HOH 469 1069 1221 HOH HOH A . 
I 5 HOH 470 1070 594  HOH HOH A . 
I 5 HOH 471 1071 998  HOH HOH A . 
I 5 HOH 472 1072 913  HOH HOH A . 
I 5 HOH 473 1073 1027 HOH HOH A . 
I 5 HOH 474 1074 217  HOH HOH A . 
I 5 HOH 475 1075 983  HOH HOH A . 
I 5 HOH 476 1076 1196 HOH HOH A . 
I 5 HOH 477 1077 977  HOH HOH A . 
I 5 HOH 478 1078 580  HOH HOH A . 
I 5 HOH 479 1079 1164 HOH HOH A . 
I 5 HOH 480 1080 1007 HOH HOH A . 
I 5 HOH 481 1081 675  HOH HOH A . 
I 5 HOH 482 1082 838  HOH HOH A . 
I 5 HOH 483 1083 337  HOH HOH A . 
I 5 HOH 484 1084 1083 HOH HOH A . 
I 5 HOH 485 1085 722  HOH HOH A . 
I 5 HOH 486 1086 704  HOH HOH A . 
I 5 HOH 487 1087 886  HOH HOH A . 
I 5 HOH 488 1088 867  HOH HOH A . 
I 5 HOH 489 1089 1095 HOH HOH A . 
I 5 HOH 490 1090 706  HOH HOH A . 
I 5 HOH 491 1091 340  HOH HOH A . 
I 5 HOH 492 1092 974  HOH HOH A . 
I 5 HOH 493 1093 547  HOH HOH A . 
I 5 HOH 494 1094 852  HOH HOH A . 
I 5 HOH 495 1095 497  HOH HOH A . 
I 5 HOH 496 1096 923  HOH HOH A . 
I 5 HOH 497 1097 729  HOH HOH A . 
I 5 HOH 498 1098 271  HOH HOH A . 
I 5 HOH 499 1099 862  HOH HOH A . 
I 5 HOH 500 1100 1143 HOH HOH A . 
I 5 HOH 501 1101 727  HOH HOH A . 
I 5 HOH 502 1102 1200 HOH HOH A . 
I 5 HOH 503 1103 1102 HOH HOH A . 
I 5 HOH 504 1104 479  HOH HOH A . 
I 5 HOH 505 1105 877  HOH HOH A . 
I 5 HOH 506 1106 512  HOH HOH A . 
I 5 HOH 507 1107 468  HOH HOH A . 
I 5 HOH 508 1108 568  HOH HOH A . 
I 5 HOH 509 1109 1013 HOH HOH A . 
I 5 HOH 510 1110 978  HOH HOH A . 
I 5 HOH 511 1111 669  HOH HOH A . 
I 5 HOH 512 1112 561  HOH HOH A . 
I 5 HOH 513 1113 500  HOH HOH A . 
I 5 HOH 514 1114 448  HOH HOH A . 
I 5 HOH 515 1115 427  HOH HOH A . 
I 5 HOH 516 1116 1024 HOH HOH A . 
I 5 HOH 517 1117 812  HOH HOH A . 
I 5 HOH 518 1118 1231 HOH HOH A . 
I 5 HOH 519 1119 1003 HOH HOH A . 
I 5 HOH 520 1120 818  HOH HOH A . 
I 5 HOH 521 1121 1146 HOH HOH A . 
I 5 HOH 522 1122 828  HOH HOH A . 
I 5 HOH 523 1123 1015 HOH HOH A . 
I 5 HOH 524 1124 1173 HOH HOH A . 
I 5 HOH 525 1125 736  HOH HOH A . 
I 5 HOH 526 1126 565  HOH HOH A . 
I 5 HOH 527 1127 747  HOH HOH A . 
I 5 HOH 528 1128 1004 HOH HOH A . 
I 5 HOH 529 1129 810  HOH HOH A . 
I 5 HOH 530 1130 1211 HOH HOH A . 
I 5 HOH 531 1131 1133 HOH HOH A . 
I 5 HOH 532 1132 901  HOH HOH A . 
I 5 HOH 533 1133 1084 HOH HOH A . 
I 5 HOH 534 1134 917  HOH HOH A . 
I 5 HOH 535 1135 801  HOH HOH A . 
I 5 HOH 536 1136 779  HOH HOH A . 
I 5 HOH 537 1137 514  HOH HOH A . 
I 5 HOH 538 1138 537  HOH HOH A . 
I 5 HOH 539 1139 1020 HOH HOH A . 
I 5 HOH 540 1140 702  HOH HOH A . 
I 5 HOH 541 1141 861  HOH HOH A . 
I 5 HOH 542 1142 324  HOH HOH A . 
I 5 HOH 543 1143 1066 HOH HOH A . 
I 5 HOH 544 1144 1011 HOH HOH A . 
I 5 HOH 545 1145 1048 HOH HOH A . 
I 5 HOH 546 1146 860  HOH HOH A . 
I 5 HOH 547 1147 976  HOH HOH A . 
I 5 HOH 548 1148 491  HOH HOH A . 
I 5 HOH 549 1149 708  HOH HOH A . 
I 5 HOH 550 1150 1216 HOH HOH A . 
I 5 HOH 551 1151 897  HOH HOH A . 
I 5 HOH 552 1152 764  HOH HOH A . 
I 5 HOH 553 1153 859  HOH HOH A . 
I 5 HOH 554 1154 431  HOH HOH A . 
I 5 HOH 555 1155 159  HOH HOH A . 
I 5 HOH 556 1156 429  HOH HOH A . 
I 5 HOH 557 1157 614  HOH HOH A . 
I 5 HOH 558 1158 902  HOH HOH A . 
I 5 HOH 559 1159 1049 HOH HOH A . 
I 5 HOH 560 1160 855  HOH HOH A . 
I 5 HOH 561 1161 816  HOH HOH A . 
I 5 HOH 562 1162 760  HOH HOH A . 
I 5 HOH 563 1163 943  HOH HOH A . 
I 5 HOH 564 1164 169  HOH HOH A . 
I 5 HOH 565 1165 277  HOH HOH A . 
I 5 HOH 566 1166 703  HOH HOH A . 
I 5 HOH 567 1167 1041 HOH HOH A . 
I 5 HOH 568 1168 841  HOH HOH A . 
I 5 HOH 569 1169 868  HOH HOH A . 
I 5 HOH 570 1170 996  HOH HOH A . 
I 5 HOH 571 1171 302  HOH HOH A . 
I 5 HOH 572 1172 880  HOH HOH A . 
I 5 HOH 573 1173 874  HOH HOH A . 
I 5 HOH 574 1174 673  HOH HOH A . 
I 5 HOH 575 1175 1042 HOH HOH A . 
I 5 HOH 576 1176 1207 HOH HOH A . 
I 5 HOH 577 1177 654  HOH HOH A . 
I 5 HOH 578 1178 1162 HOH HOH A . 
I 5 HOH 579 1179 765  HOH HOH A . 
I 5 HOH 580 1180 545  HOH HOH A . 
I 5 HOH 581 1181 776  HOH HOH A . 
I 5 HOH 582 1182 915  HOH HOH A . 
I 5 HOH 583 1183 255  HOH HOH A . 
I 5 HOH 584 1184 330  HOH HOH A . 
I 5 HOH 585 1185 598  HOH HOH A . 
I 5 HOH 586 1186 1151 HOH HOH A . 
I 5 HOH 587 1187 604  HOH HOH A . 
I 5 HOH 588 1188 1118 HOH HOH A . 
I 5 HOH 589 1189 699  HOH HOH A . 
I 5 HOH 590 1190 735  HOH HOH A . 
I 5 HOH 591 1191 853  HOH HOH A . 
I 5 HOH 592 1192 1214 HOH HOH A . 
I 5 HOH 593 1193 1180 HOH HOH A . 
I 5 HOH 594 1194 415  HOH HOH A . 
I 5 HOH 595 1195 513  HOH HOH A . 
I 5 HOH 596 1196 970  HOH HOH A . 
I 5 HOH 597 1197 879  HOH HOH A . 
I 5 HOH 598 1198 555  HOH HOH A . 
I 5 HOH 599 1199 582  HOH HOH A . 
I 5 HOH 600 1200 194  HOH HOH A . 
I 5 HOH 601 1201 284  HOH HOH A . 
I 5 HOH 602 1202 504  HOH HOH A . 
I 5 HOH 603 1203 799  HOH HOH A . 
I 5 HOH 604 1204 651  HOH HOH A . 
I 5 HOH 605 1205 1189 HOH HOH A . 
I 5 HOH 606 1206 772  HOH HOH A . 
I 5 HOH 607 1207 730  HOH HOH A . 
I 5 HOH 608 1208 262  HOH HOH A . 
I 5 HOH 609 1209 187  HOH HOH A . 
I 5 HOH 610 1210 681  HOH HOH A . 
I 5 HOH 611 1211 312  HOH HOH A . 
I 5 HOH 612 1212 552  HOH HOH A . 
I 5 HOH 613 1213 443  HOH HOH A . 
I 5 HOH 614 1214 1201 HOH HOH A . 
I 5 HOH 615 1215 605  HOH HOH A . 
I 5 HOH 616 1216 1139 HOH HOH A . 
I 5 HOH 617 1217 808  HOH HOH A . 
I 5 HOH 618 1218 847  HOH HOH A . 
I 5 HOH 619 1219 1047 HOH HOH A . 
I 5 HOH 620 1220 419  HOH HOH A . 
I 5 HOH 621 1221 241  HOH HOH A . 
I 5 HOH 622 1222 746  HOH HOH A . 
I 5 HOH 623 1223 1130 HOH HOH A . 
I 5 HOH 624 1224 543  HOH HOH A . 
I 5 HOH 625 1225 1019 HOH HOH A . 
I 5 HOH 626 1226 865  HOH HOH A . 
I 5 HOH 627 1227 611  HOH HOH A . 
J 5 HOH 1   601  1208 HOH HOH B . 
J 5 HOH 2   602  1110 HOH HOH B . 
J 5 HOH 3   603  646  HOH HOH B . 
J 5 HOH 4   604  96   HOH HOH B . 
J 5 HOH 5   605  952  HOH HOH B . 
J 5 HOH 6   606  1193 HOH HOH B . 
J 5 HOH 7   607  1141 HOH HOH B . 
J 5 HOH 8   608  445  HOH HOH B . 
J 5 HOH 9   609  167  HOH HOH B . 
J 5 HOH 10  610  713  HOH HOH B . 
J 5 HOH 11  611  587  HOH HOH B . 
J 5 HOH 12  612  1183 HOH HOH B . 
J 5 HOH 13  613  766  HOH HOH B . 
J 5 HOH 14  614  1012 HOH HOH B . 
J 5 HOH 15  615  1204 HOH HOH B . 
J 5 HOH 16  616  123  HOH HOH B . 
J 5 HOH 17  617  1119 HOH HOH B . 
J 5 HOH 18  618  633  HOH HOH B . 
J 5 HOH 19  619  496  HOH HOH B . 
J 5 HOH 20  620  774  HOH HOH B . 
J 5 HOH 21  621  1026 HOH HOH B . 
J 5 HOH 22  622  56   HOH HOH B . 
J 5 HOH 23  623  53   HOH HOH B . 
J 5 HOH 24  624  323  HOH HOH B . 
J 5 HOH 25  625  907  HOH HOH B . 
J 5 HOH 26  626  416  HOH HOH B . 
J 5 HOH 27  627  773  HOH HOH B . 
J 5 HOH 28  628  476  HOH HOH B . 
J 5 HOH 29  629  529  HOH HOH B . 
J 5 HOH 30  630  1131 HOH HOH B . 
J 5 HOH 31  631  347  HOH HOH B . 
J 5 HOH 32  632  425  HOH HOH B . 
J 5 HOH 33  633  749  HOH HOH B . 
J 5 HOH 34  634  709  HOH HOH B . 
J 5 HOH 35  635  266  HOH HOH B . 
J 5 HOH 36  636  544  HOH HOH B . 
J 5 HOH 37  637  197  HOH HOH B . 
J 5 HOH 38  638  849  HOH HOH B . 
J 5 HOH 39  639  73   HOH HOH B . 
J 5 HOH 40  640  1236 HOH HOH B . 
J 5 HOH 41  641  784  HOH HOH B . 
J 5 HOH 42  642  522  HOH HOH B . 
J 5 HOH 43  643  761  HOH HOH B . 
J 5 HOH 44  644  613  HOH HOH B . 
J 5 HOH 45  645  215  HOH HOH B . 
J 5 HOH 46  646  835  HOH HOH B . 
J 5 HOH 47  647  293  HOH HOH B . 
J 5 HOH 48  648  603  HOH HOH B . 
J 5 HOH 49  649  1161 HOH HOH B . 
J 5 HOH 50  650  1145 HOH HOH B . 
J 5 HOH 51  651  63   HOH HOH B . 
J 5 HOH 52  652  750  HOH HOH B . 
J 5 HOH 53  653  249  HOH HOH B . 
J 5 HOH 54  654  1074 HOH HOH B . 
J 5 HOH 55  655  141  HOH HOH B . 
J 5 HOH 56  656  693  HOH HOH B . 
J 5 HOH 57  657  991  HOH HOH B . 
J 5 HOH 58  658  195  HOH HOH B . 
J 5 HOH 59  659  888  HOH HOH B . 
J 5 HOH 60  660  62   HOH HOH B . 
J 5 HOH 61  661  441  HOH HOH B . 
J 5 HOH 62  662  523  HOH HOH B . 
J 5 HOH 63  663  483  HOH HOH B . 
J 5 HOH 64  664  1009 HOH HOH B . 
J 5 HOH 65  665  75   HOH HOH B . 
J 5 HOH 66  666  28   HOH HOH B . 
J 5 HOH 67  667  473  HOH HOH B . 
J 5 HOH 68  668  129  HOH HOH B . 
J 5 HOH 69  669  636  HOH HOH B . 
J 5 HOH 70  670  55   HOH HOH B . 
J 5 HOH 71  671  157  HOH HOH B . 
J 5 HOH 72  672  30   HOH HOH B . 
J 5 HOH 73  673  1077 HOH HOH B . 
J 5 HOH 74  674  233  HOH HOH B . 
J 5 HOH 75  675  961  HOH HOH B . 
J 5 HOH 76  676  1155 HOH HOH B . 
J 5 HOH 77  677  60   HOH HOH B . 
J 5 HOH 78  678  14   HOH HOH B . 
J 5 HOH 79  679  329  HOH HOH B . 
J 5 HOH 80  680  78   HOH HOH B . 
J 5 HOH 81  681  35   HOH HOH B . 
J 5 HOH 82  682  804  HOH HOH B . 
J 5 HOH 83  683  590  HOH HOH B . 
J 5 HOH 84  684  309  HOH HOH B . 
J 5 HOH 85  685  437  HOH HOH B . 
J 5 HOH 86  686  466  HOH HOH B . 
J 5 HOH 87  687  452  HOH HOH B . 
J 5 HOH 88  688  10   HOH HOH B . 
J 5 HOH 89  689  333  HOH HOH B . 
J 5 HOH 90  690  494  HOH HOH B . 
J 5 HOH 91  691  436  HOH HOH B . 
J 5 HOH 92  692  563  HOH HOH B . 
J 5 HOH 93  693  114  HOH HOH B . 
J 5 HOH 94  694  221  HOH HOH B . 
J 5 HOH 95  695  225  HOH HOH B . 
J 5 HOH 96  696  137  HOH HOH B . 
J 5 HOH 97  697  185  HOH HOH B . 
J 5 HOH 98  698  846  HOH HOH B . 
J 5 HOH 99  699  126  HOH HOH B . 
J 5 HOH 100 700  470  HOH HOH B . 
J 5 HOH 101 701  118  HOH HOH B . 
J 5 HOH 102 702  515  HOH HOH B . 
J 5 HOH 103 703  107  HOH HOH B . 
J 5 HOH 104 704  294  HOH HOH B . 
J 5 HOH 105 705  29   HOH HOH B . 
J 5 HOH 106 706  314  HOH HOH B . 
J 5 HOH 107 707  645  HOH HOH B . 
J 5 HOH 108 708  546  HOH HOH B . 
J 5 HOH 109 709  571  HOH HOH B . 
J 5 HOH 110 710  994  HOH HOH B . 
J 5 HOH 111 711  166  HOH HOH B . 
J 5 HOH 112 712  931  HOH HOH B . 
J 5 HOH 113 713  125  HOH HOH B . 
J 5 HOH 114 714  612  HOH HOH B . 
J 5 HOH 115 715  208  HOH HOH B . 
J 5 HOH 116 716  61   HOH HOH B . 
J 5 HOH 117 717  42   HOH HOH B . 
J 5 HOH 118 718  481  HOH HOH B . 
J 5 HOH 119 719  117  HOH HOH B . 
J 5 HOH 120 720  440  HOH HOH B . 
J 5 HOH 121 721  307  HOH HOH B . 
J 5 HOH 122 722  940  HOH HOH B . 
J 5 HOH 123 723  405  HOH HOH B . 
J 5 HOH 124 724  498  HOH HOH B . 
J 5 HOH 125 725  248  HOH HOH B . 
J 5 HOH 126 726  97   HOH HOH B . 
J 5 HOH 127 727  100  HOH HOH B . 
J 5 HOH 128 728  802  HOH HOH B . 
J 5 HOH 129 729  25   HOH HOH B . 
J 5 HOH 130 730  947  HOH HOH B . 
J 5 HOH 131 731  318  HOH HOH B . 
J 5 HOH 132 732  469  HOH HOH B . 
J 5 HOH 133 733  1185 HOH HOH B . 
J 5 HOH 134 734  181  HOH HOH B . 
J 5 HOH 135 735  112  HOH HOH B . 
J 5 HOH 136 736  113  HOH HOH B . 
J 5 HOH 137 737  540  HOH HOH B . 
J 5 HOH 138 738  136  HOH HOH B . 
J 5 HOH 139 739  164  HOH HOH B . 
J 5 HOH 140 740  1184 HOH HOH B . 
J 5 HOH 141 741  619  HOH HOH B . 
J 5 HOH 142 742  243  HOH HOH B . 
J 5 HOH 143 743  432  HOH HOH B . 
J 5 HOH 144 744  162  HOH HOH B . 
J 5 HOH 145 745  328  HOH HOH B . 
J 5 HOH 146 746  648  HOH HOH B . 
J 5 HOH 147 747  275  HOH HOH B . 
J 5 HOH 148 748  954  HOH HOH B . 
J 5 HOH 149 749  11   HOH HOH B . 
J 5 HOH 150 750  120  HOH HOH B . 
J 5 HOH 151 751  524  HOH HOH B . 
J 5 HOH 152 752  66   HOH HOH B . 
J 5 HOH 153 753  840  HOH HOH B . 
J 5 HOH 154 754  298  HOH HOH B . 
J 5 HOH 155 755  492  HOH HOH B . 
J 5 HOH 156 756  23   HOH HOH B . 
J 5 HOH 157 757  180  HOH HOH B . 
J 5 HOH 158 758  386  HOH HOH B . 
J 5 HOH 159 759  92   HOH HOH B . 
J 5 HOH 160 760  527  HOH HOH B . 
J 5 HOH 161 761  278  HOH HOH B . 
J 5 HOH 162 762  380  HOH HOH B . 
J 5 HOH 163 763  119  HOH HOH B . 
J 5 HOH 164 764  854  HOH HOH B . 
J 5 HOH 165 765  295  HOH HOH B . 
J 5 HOH 166 766  85   HOH HOH B . 
J 5 HOH 167 767  1212 HOH HOH B . 
J 5 HOH 168 768  400  HOH HOH B . 
J 5 HOH 169 769  450  HOH HOH B . 
J 5 HOH 170 770  48   HOH HOH B . 
J 5 HOH 171 771  487  HOH HOH B . 
J 5 HOH 172 772  21   HOH HOH B . 
J 5 HOH 173 773  12   HOH HOH B . 
J 5 HOH 174 774  59   HOH HOH B . 
J 5 HOH 175 775  631  HOH HOH B . 
J 5 HOH 176 776  1002 HOH HOH B . 
J 5 HOH 177 777  34   HOH HOH B . 
J 5 HOH 178 778  682  HOH HOH B . 
J 5 HOH 179 779  84   HOH HOH B . 
J 5 HOH 180 780  914  HOH HOH B . 
J 5 HOH 181 781  341  HOH HOH B . 
J 5 HOH 182 782  40   HOH HOH B . 
J 5 HOH 183 783  41   HOH HOH B . 
J 5 HOH 184 784  404  HOH HOH B . 
J 5 HOH 185 785  401  HOH HOH B . 
J 5 HOH 186 786  534  HOH HOH B . 
J 5 HOH 187 787  229  HOH HOH B . 
J 5 HOH 188 788  793  HOH HOH B . 
J 5 HOH 189 789  420  HOH HOH B . 
J 5 HOH 190 790  973  HOH HOH B . 
J 5 HOH 191 791  422  HOH HOH B . 
J 5 HOH 192 792  376  HOH HOH B . 
J 5 HOH 193 793  583  HOH HOH B . 
J 5 HOH 194 794  72   HOH HOH B . 
J 5 HOH 195 795  382  HOH HOH B . 
J 5 HOH 196 796  186  HOH HOH B . 
J 5 HOH 197 797  354  HOH HOH B . 
J 5 HOH 198 798  1149 HOH HOH B . 
J 5 HOH 199 799  24   HOH HOH B . 
J 5 HOH 200 800  350  HOH HOH B . 
J 5 HOH 201 801  575  HOH HOH B . 
J 5 HOH 202 802  731  HOH HOH B . 
J 5 HOH 203 803  58   HOH HOH B . 
J 5 HOH 204 804  396  HOH HOH B . 
J 5 HOH 205 805  139  HOH HOH B . 
J 5 HOH 206 806  1008 HOH HOH B . 
J 5 HOH 207 807  22   HOH HOH B . 
J 5 HOH 208 808  626  HOH HOH B . 
J 5 HOH 209 809  1226 HOH HOH B . 
J 5 HOH 210 810  412  HOH HOH B . 
J 5 HOH 211 811  242  HOH HOH B . 
J 5 HOH 212 812  3    HOH HOH B . 
J 5 HOH 213 813  201  HOH HOH B . 
J 5 HOH 214 814  748  HOH HOH B . 
J 5 HOH 215 815  960  HOH HOH B . 
J 5 HOH 216 816  596  HOH HOH B . 
J 5 HOH 217 817  51   HOH HOH B . 
J 5 HOH 218 818  576  HOH HOH B . 
J 5 HOH 219 819  824  HOH HOH B . 
J 5 HOH 220 820  305  HOH HOH B . 
J 5 HOH 221 821  346  HOH HOH B . 
J 5 HOH 222 822  264  HOH HOH B . 
J 5 HOH 223 823  359  HOH HOH B . 
J 5 HOH 224 824  615  HOH HOH B . 
J 5 HOH 225 825  486  HOH HOH B . 
J 5 HOH 226 826  585  HOH HOH B . 
J 5 HOH 227 827  1103 HOH HOH B . 
J 5 HOH 228 828  381  HOH HOH B . 
J 5 HOH 229 829  272  HOH HOH B . 
J 5 HOH 230 830  230  HOH HOH B . 
J 5 HOH 231 831  653  HOH HOH B . 
J 5 HOH 232 832  908  HOH HOH B . 
J 5 HOH 233 833  1138 HOH HOH B . 
J 5 HOH 234 834  219  HOH HOH B . 
J 5 HOH 235 835  650  HOH HOH B . 
J 5 HOH 236 836  843  HOH HOH B . 
J 5 HOH 237 837  462  HOH HOH B . 
J 5 HOH 238 838  1018 HOH HOH B . 
J 5 HOH 239 839  589  HOH HOH B . 
J 5 HOH 240 840  282  HOH HOH B . 
J 5 HOH 241 841  213  HOH HOH B . 
J 5 HOH 242 842  418  HOH HOH B . 
J 5 HOH 243 843  734  HOH HOH B . 
J 5 HOH 244 844  106  HOH HOH B . 
J 5 HOH 245 845  17   HOH HOH B . 
J 5 HOH 246 846  790  HOH HOH B . 
J 5 HOH 247 847  177  HOH HOH B . 
J 5 HOH 248 848  247  HOH HOH B . 
J 5 HOH 249 849  251  HOH HOH B . 
J 5 HOH 250 850  683  HOH HOH B . 
J 5 HOH 251 851  183  HOH HOH B . 
J 5 HOH 252 852  642  HOH HOH B . 
J 5 HOH 253 853  178  HOH HOH B . 
J 5 HOH 254 854  679  HOH HOH B . 
J 5 HOH 255 855  530  HOH HOH B . 
J 5 HOH 256 856  557  HOH HOH B . 
J 5 HOH 257 857  209  HOH HOH B . 
J 5 HOH 258 858  368  HOH HOH B . 
J 5 HOH 259 859  676  HOH HOH B . 
J 5 HOH 260 860  532  HOH HOH B . 
J 5 HOH 261 861  147  HOH HOH B . 
J 5 HOH 262 862  362  HOH HOH B . 
J 5 HOH 263 863  815  HOH HOH B . 
J 5 HOH 264 864  1217 HOH HOH B . 
J 5 HOH 265 865  410  HOH HOH B . 
J 5 HOH 266 866  110  HOH HOH B . 
J 5 HOH 267 867  188  HOH HOH B . 
J 5 HOH 268 868  949  HOH HOH B . 
J 5 HOH 269 869  891  HOH HOH B . 
J 5 HOH 270 870  94   HOH HOH B . 
J 5 HOH 271 871  1186 HOH HOH B . 
J 5 HOH 272 872  36   HOH HOH B . 
J 5 HOH 273 873  600  HOH HOH B . 
J 5 HOH 274 874  210  HOH HOH B . 
J 5 HOH 275 875  288  HOH HOH B . 
J 5 HOH 276 876  792  HOH HOH B . 
J 5 HOH 277 877  1115 HOH HOH B . 
J 5 HOH 278 878  616  HOH HOH B . 
J 5 HOH 279 879  564  HOH HOH B . 
J 5 HOH 280 880  689  HOH HOH B . 
J 5 HOH 281 881  127  HOH HOH B . 
J 5 HOH 282 882  714  HOH HOH B . 
J 5 HOH 283 883  1033 HOH HOH B . 
J 5 HOH 284 884  238  HOH HOH B . 
J 5 HOH 285 885  175  HOH HOH B . 
J 5 HOH 286 886  388  HOH HOH B . 
J 5 HOH 287 887  398  HOH HOH B . 
J 5 HOH 288 888  223  HOH HOH B . 
J 5 HOH 289 889  446  HOH HOH B . 
J 5 HOH 290 890  1082 HOH HOH B . 
J 5 HOH 291 891  378  HOH HOH B . 
J 5 HOH 292 892  447  HOH HOH B . 
J 5 HOH 293 893  148  HOH HOH B . 
J 5 HOH 294 894  226  HOH HOH B . 
J 5 HOH 295 895  715  HOH HOH B . 
J 5 HOH 296 896  686  HOH HOH B . 
J 5 HOH 297 897  374  HOH HOH B . 
J 5 HOH 298 898  875  HOH HOH B . 
J 5 HOH 299 899  348  HOH HOH B . 
J 5 HOH 300 900  946  HOH HOH B . 
J 5 HOH 301 901  756  HOH HOH B . 
J 5 HOH 302 902  887  HOH HOH B . 
J 5 HOH 303 903  1120 HOH HOH B . 
J 5 HOH 304 904  525  HOH HOH B . 
J 5 HOH 305 905  1147 HOH HOH B . 
J 5 HOH 306 906  1128 HOH HOH B . 
J 5 HOH 307 907  948  HOH HOH B . 
J 5 HOH 308 908  327  HOH HOH B . 
J 5 HOH 309 909  433  HOH HOH B . 
J 5 HOH 310 910  1168 HOH HOH B . 
J 5 HOH 311 911  762  HOH HOH B . 
J 5 HOH 312 912  910  HOH HOH B . 
J 5 HOH 313 913  434  HOH HOH B . 
J 5 HOH 314 914  1232 HOH HOH B . 
J 5 HOH 315 915  98   HOH HOH B . 
J 5 HOH 316 916  352  HOH HOH B . 
J 5 HOH 317 917  507  HOH HOH B . 
J 5 HOH 318 918  250  HOH HOH B . 
J 5 HOH 319 919  640  HOH HOH B . 
J 5 HOH 320 920  993  HOH HOH B . 
J 5 HOH 321 921  919  HOH HOH B . 
J 5 HOH 322 922  326  HOH HOH B . 
J 5 HOH 323 923  895  HOH HOH B . 
J 5 HOH 324 924  1225 HOH HOH B . 
J 5 HOH 325 925  1233 HOH HOH B . 
J 5 HOH 326 926  458  HOH HOH B . 
J 5 HOH 327 927  629  HOH HOH B . 
J 5 HOH 328 928  526  HOH HOH B . 
J 5 HOH 329 929  721  HOH HOH B . 
J 5 HOH 330 930  968  HOH HOH B . 
J 5 HOH 331 931  317  HOH HOH B . 
J 5 HOH 332 932  536  HOH HOH B . 
J 5 HOH 333 933  150  HOH HOH B . 
J 5 HOH 334 934  435  HOH HOH B . 
J 5 HOH 335 935  601  HOH HOH B . 
J 5 HOH 336 936  104  HOH HOH B . 
J 5 HOH 337 937  606  HOH HOH B . 
J 5 HOH 338 938  43   HOH HOH B . 
J 5 HOH 339 939  986  HOH HOH B . 
J 5 HOH 340 940  806  HOH HOH B . 
J 5 HOH 341 941  967  HOH HOH B . 
J 5 HOH 342 942  143  HOH HOH B . 
J 5 HOH 343 943  49   HOH HOH B . 
J 5 HOH 344 944  176  HOH HOH B . 
J 5 HOH 345 945  723  HOH HOH B . 
J 5 HOH 346 946  1190 HOH HOH B . 
J 5 HOH 347 947  482  HOH HOH B . 
J 5 HOH 348 948  1038 HOH HOH B . 
J 5 HOH 349 949  531  HOH HOH B . 
J 5 HOH 350 950  244  HOH HOH B . 
J 5 HOH 351 951  856  HOH HOH B . 
J 5 HOH 352 952  224  HOH HOH B . 
J 5 HOH 353 953  296  HOH HOH B . 
J 5 HOH 354 954  1093 HOH HOH B . 
J 5 HOH 355 955  377  HOH HOH B . 
J 5 HOH 356 956  741  HOH HOH B . 
J 5 HOH 357 957  1195 HOH HOH B . 
J 5 HOH 358 958  1132 HOH HOH B . 
J 5 HOH 359 959  1116 HOH HOH B . 
J 5 HOH 360 960  814  HOH HOH B . 
J 5 HOH 361 961  602  HOH HOH B . 
J 5 HOH 362 962  1101 HOH HOH B . 
J 5 HOH 363 963  663  HOH HOH B . 
J 5 HOH 364 964  893  HOH HOH B . 
J 5 HOH 365 965  115  HOH HOH B . 
J 5 HOH 366 966  807  HOH HOH B . 
J 5 HOH 367 967  554  HOH HOH B . 
J 5 HOH 368 968  559  HOH HOH B . 
J 5 HOH 369 969  990  HOH HOH B . 
J 5 HOH 370 970  485  HOH HOH B . 
J 5 HOH 371 971  138  HOH HOH B . 
J 5 HOH 372 972  1198 HOH HOH B . 
J 5 HOH 373 973  680  HOH HOH B . 
J 5 HOH 374 974  892  HOH HOH B . 
J 5 HOH 375 975  833  HOH HOH B . 
J 5 HOH 376 976  711  HOH HOH B . 
J 5 HOH 377 977  149  HOH HOH B . 
J 5 HOH 378 978  1021 HOH HOH B . 
J 5 HOH 379 979  569  HOH HOH B . 
J 5 HOH 380 980  31   HOH HOH B . 
J 5 HOH 381 981  299  HOH HOH B . 
J 5 HOH 382 982  399  HOH HOH B . 
J 5 HOH 383 983  204  HOH HOH B . 
J 5 HOH 384 984  103  HOH HOH B . 
J 5 HOH 385 985  955  HOH HOH B . 
J 5 HOH 386 986  771  HOH HOH B . 
J 5 HOH 387 987  964  HOH HOH B . 
J 5 HOH 388 988  1112 HOH HOH B . 
J 5 HOH 389 989  467  HOH HOH B . 
J 5 HOH 390 990  1035 HOH HOH B . 
J 5 HOH 391 991  944  HOH HOH B . 
J 5 HOH 392 992  289  HOH HOH B . 
J 5 HOH 393 993  962  HOH HOH B . 
J 5 HOH 394 994  1213 HOH HOH B . 
J 5 HOH 395 995  705  HOH HOH B . 
J 5 HOH 396 996  811  HOH HOH B . 
J 5 HOH 397 997  881  HOH HOH B . 
J 5 HOH 398 998  899  HOH HOH B . 
J 5 HOH 399 999  1036 HOH HOH B . 
J 5 HOH 400 1000 1188 HOH HOH B . 
J 5 HOH 401 1001 393  HOH HOH B . 
J 5 HOH 402 1002 789  HOH HOH B . 
J 5 HOH 403 1003 1160 HOH HOH B . 
J 5 HOH 404 1004 551  HOH HOH B . 
J 5 HOH 405 1005 926  HOH HOH B . 
J 5 HOH 406 1006 725  HOH HOH B . 
J 5 HOH 407 1007 617  HOH HOH B . 
J 5 HOH 408 1008 1159 HOH HOH B . 
J 5 HOH 409 1009 628  HOH HOH B . 
J 5 HOH 410 1010 394  HOH HOH B . 
J 5 HOH 411 1011 1096 HOH HOH B . 
J 5 HOH 412 1012 903  HOH HOH B . 
J 5 HOH 413 1013 858  HOH HOH B . 
J 5 HOH 414 1014 819  HOH HOH B . 
J 5 HOH 415 1015 763  HOH HOH B . 
J 5 HOH 416 1016 1045 HOH HOH B . 
J 5 HOH 417 1017 245  HOH HOH B . 
J 5 HOH 418 1018 932  HOH HOH B . 
J 5 HOH 419 1019 900  HOH HOH B . 
J 5 HOH 420 1020 661  HOH HOH B . 
J 5 HOH 421 1021 728  HOH HOH B . 
J 5 HOH 422 1022 876  HOH HOH B . 
J 5 HOH 423 1023 375  HOH HOH B . 
J 5 HOH 424 1024 1163 HOH HOH B . 
J 5 HOH 425 1025 1209 HOH HOH B . 
J 5 HOH 426 1026 442  HOH HOH B . 
J 5 HOH 427 1027 1142 HOH HOH B . 
J 5 HOH 428 1028 1031 HOH HOH B . 
J 5 HOH 429 1029 220  HOH HOH B . 
J 5 HOH 430 1030 906  HOH HOH B . 
J 5 HOH 431 1031 205  HOH HOH B . 
J 5 HOH 432 1032 550  HOH HOH B . 
J 5 HOH 433 1033 1099 HOH HOH B . 
J 5 HOH 434 1034 506  HOH HOH B . 
J 5 HOH 435 1035 848  HOH HOH B . 
J 5 HOH 436 1036 627  HOH HOH B . 
J 5 HOH 437 1037 981  HOH HOH B . 
J 5 HOH 438 1038 980  HOH HOH B . 
J 5 HOH 439 1039 770  HOH HOH B . 
J 5 HOH 440 1040 1215 HOH HOH B . 
J 5 HOH 441 1041 610  HOH HOH B . 
J 5 HOH 442 1042 621  HOH HOH B . 
J 5 HOH 443 1043 356  HOH HOH B . 
J 5 HOH 444 1044 753  HOH HOH B . 
J 5 HOH 445 1045 724  HOH HOH B . 
J 5 HOH 446 1046 1137 HOH HOH B . 
J 5 HOH 447 1047 548  HOH HOH B . 
J 5 HOH 448 1048 780  HOH HOH B . 
J 5 HOH 449 1049 794  HOH HOH B . 
J 5 HOH 450 1050 528  HOH HOH B . 
J 5 HOH 451 1051 884  HOH HOH B . 
J 5 HOH 452 1052 1206 HOH HOH B . 
J 5 HOH 453 1053 184  HOH HOH B . 
J 5 HOH 454 1054 795  HOH HOH B . 
J 5 HOH 455 1055 1098 HOH HOH B . 
J 5 HOH 456 1056 1034 HOH HOH B . 
J 5 HOH 457 1057 839  HOH HOH B . 
J 5 HOH 458 1058 343  HOH HOH B . 
J 5 HOH 459 1059 1220 HOH HOH B . 
J 5 HOH 460 1060 712  HOH HOH B . 
J 5 HOH 461 1061 691  HOH HOH B . 
J 5 HOH 462 1062 678  HOH HOH B . 
J 5 HOH 463 1063 1016 HOH HOH B . 
J 5 HOH 464 1064 666  HOH HOH B . 
J 5 HOH 465 1065 933  HOH HOH B . 
J 5 HOH 466 1066 863  HOH HOH B . 
J 5 HOH 467 1067 1001 HOH HOH B . 
J 5 HOH 468 1068 979  HOH HOH B . 
J 5 HOH 469 1069 791  HOH HOH B . 
J 5 HOH 470 1070 1028 HOH HOH B . 
J 5 HOH 471 1071 656  HOH HOH B . 
J 5 HOH 472 1072 787  HOH HOH B . 
J 5 HOH 473 1073 738  HOH HOH B . 
J 5 HOH 474 1074 397  HOH HOH B . 
J 5 HOH 475 1075 813  HOH HOH B . 
J 5 HOH 476 1076 1022 HOH HOH B . 
J 5 HOH 477 1077 930  HOH HOH B . 
J 5 HOH 478 1078 1167 HOH HOH B . 
J 5 HOH 479 1079 1010 HOH HOH B . 
J 5 HOH 480 1080 1222 HOH HOH B . 
J 5 HOH 481 1081 695  HOH HOH B . 
J 5 HOH 482 1082 1044 HOH HOH B . 
J 5 HOH 483 1083 916  HOH HOH B . 
J 5 HOH 484 1084 769  HOH HOH B . 
J 5 HOH 485 1085 1006 HOH HOH B . 
J 5 HOH 486 1086 1080 HOH HOH B . 
J 5 HOH 487 1087 1156 HOH HOH B . 
J 5 HOH 488 1088 1092 HOH HOH B . 
J 5 HOH 489 1089 821  HOH HOH B . 
J 5 HOH 490 1090 421  HOH HOH B . 
J 5 HOH 491 1091 508  HOH HOH B . 
J 5 HOH 492 1092 315  HOH HOH B . 
J 5 HOH 493 1093 1109 HOH HOH B . 
J 5 HOH 494 1094 825  HOH HOH B . 
J 5 HOH 495 1095 1097 HOH HOH B . 
J 5 HOH 496 1096 950  HOH HOH B . 
J 5 HOH 497 1097 373  HOH HOH B . 
J 5 HOH 498 1098 668  HOH HOH B . 
J 5 HOH 499 1099 1005 HOH HOH B . 
J 5 HOH 500 1100 390  HOH HOH B . 
J 5 HOH 501 1101 503  HOH HOH B . 
J 5 HOH 502 1102 984  HOH HOH B . 
J 5 HOH 503 1103 660  HOH HOH B . 
J 5 HOH 504 1104 870  HOH HOH B . 
J 5 HOH 505 1105 1125 HOH HOH B . 
J 5 HOH 506 1106 966  HOH HOH B . 
J 5 HOH 507 1107 472  HOH HOH B . 
J 5 HOH 508 1108 372  HOH HOH B . 
J 5 HOH 509 1109 685  HOH HOH B . 
J 5 HOH 510 1110 578  HOH HOH B . 
J 5 HOH 511 1111 387  HOH HOH B . 
J 5 HOH 512 1112 1136 HOH HOH B . 
J 5 HOH 513 1113 878  HOH HOH B . 
J 5 HOH 514 1114 395  HOH HOH B . 
J 5 HOH 515 1115 803  HOH HOH B . 
J 5 HOH 516 1116 687  HOH HOH B . 
J 5 HOH 517 1117 883  HOH HOH B . 
J 5 HOH 518 1118 671  HOH HOH B . 
J 5 HOH 519 1119 1166 HOH HOH B . 
J 5 HOH 520 1120 572  HOH HOH B . 
J 5 HOH 521 1121 1140 HOH HOH B . 
J 5 HOH 522 1122 599  HOH HOH B . 
J 5 HOH 523 1123 623  HOH HOH B . 
J 5 HOH 524 1124 866  HOH HOH B . 
J 5 HOH 525 1125 1153 HOH HOH B . 
J 5 HOH 526 1126 786  HOH HOH B . 
J 5 HOH 527 1127 1129 HOH HOH B . 
J 5 HOH 528 1128 718  HOH HOH B . 
J 5 HOH 529 1129 752  HOH HOH B . 
J 5 HOH 530 1130 1121 HOH HOH B . 
J 5 HOH 531 1131 593  HOH HOH B . 
J 5 HOH 532 1132 1157 HOH HOH B . 
J 5 HOH 533 1133 1224 HOH HOH B . 
J 5 HOH 534 1134 539  HOH HOH B . 
J 5 HOH 535 1135 796  HOH HOH B . 
J 5 HOH 536 1136 697  HOH HOH B . 
J 5 HOH 537 1137 975  HOH HOH B . 
J 5 HOH 538 1138 988  HOH HOH B . 
J 5 HOH 539 1139 925  HOH HOH B . 
J 5 HOH 540 1140 577  HOH HOH B . 
J 5 HOH 541 1141 438  HOH HOH B . 
J 5 HOH 542 1142 987  HOH HOH B . 
J 5 HOH 543 1143 349  HOH HOH B . 
J 5 HOH 544 1144 239  HOH HOH B . 
J 5 HOH 545 1145 228  HOH HOH B . 
J 5 HOH 546 1146 690  HOH HOH B . 
J 5 HOH 547 1147 567  HOH HOH B . 
J 5 HOH 548 1148 493  HOH HOH B . 
J 5 HOH 549 1149 1017 HOH HOH B . 
J 5 HOH 550 1150 782  HOH HOH B . 
J 5 HOH 551 1151 939  HOH HOH B . 
J 5 HOH 552 1152 934  HOH HOH B . 
J 5 HOH 553 1153 665  HOH HOH B . 
J 5 HOH 554 1154 484  HOH HOH B . 
J 5 HOH 555 1155 292  HOH HOH B . 
J 5 HOH 556 1156 1030 HOH HOH B . 
J 5 HOH 557 1157 1165 HOH HOH B . 
# 
_pdbx_unobs_or_zero_occ_atoms.id               1 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag     N 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id     B 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id     PLP 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id      502 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id     O4A 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id     ? 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id    H 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id    PLP 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id     1 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id    O4A 
# 
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  ? ? ? '(1.13_2998: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                  2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .                  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                     9CF4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     82.383 
_cell.length_a_esd                 ? 
_cell.length_b                     94.102 
_cell.length_b_esd                 ? 
_cell.length_c                     219.984 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9CF4 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9CF4 
_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             2.07 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.67 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    'Minimum light exposure' 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;0.1 M TRIS pH 8, 
19.28 % (w/v) PEG 6000 
and 0.3 M MgCl2
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293.15 
# 
_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 PILATUS 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-11-15 
_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   0.9184 
_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                        'BESSY BEAMLINE 14.2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9184 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   14.2 
_diffrn_source.pdbx_synchrotron_site       BESSY 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9CF4 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.499 
_reflns.d_resolution_low                               35.913 
_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                                     136251 
_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                           99.72 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          17.20 
_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                                0.02988 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.499 
_reflns_shell.d_res_low                                     1.553 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.93 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             13274 
_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                               10.2 
_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                               0.3451 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          98.12 
_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                                 9CF4 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.499 
_refine.ls_d_res_low                             35.913 
_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                     136228 
_refine.ls_number_reflns_R_free                  2290 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.69 
_refine.ls_percent_reflns_R_free                 1.68 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1130 
_refine.ls_R_factor_R_free                       0.1512 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1124 
_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                          1.35 
_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            0.1512 
_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                 14.65 
_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                            0.13 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.499 
_refine_hist.d_res_low                        35.913 
_refine_hist.number_atoms_solvent             1184 
_refine_hist.number_atoms_total               8320 
_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        7076 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         60 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  ? 7454  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.101  ? 10112 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 18.046 ? 2717  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.078  ? 1074  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 1344  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.499  1.5313 . . 136 8020 96.00  . . . . 0.1902 . . . . . . . . . . . 0.2610 
'X-RAY DIFFRACTION' 1.5313 1.5669 . . 140 8314 100.00 . . . . 0.1680 . . . . . . . . . . . 0.2337 
'X-RAY DIFFRACTION' 1.5669 1.6061 . . 126 8338 100.00 . . . . 0.1483 . . . . . . . . . . . 0.2391 
'X-RAY DIFFRACTION' 1.6061 1.6495 . . 166 8300 100.00 . . . . 0.1402 . . . . . . . . . . . 0.1976 
'X-RAY DIFFRACTION' 1.6495 1.6981 . . 135 8298 100.00 . . . . 0.1304 . . . . . . . . . . . 0.1769 
'X-RAY DIFFRACTION' 1.6981 1.7529 . . 147 8312 100.00 . . . . 0.1225 . . . . . . . . . . . 0.1854 
'X-RAY DIFFRACTION' 1.7529 1.8155 . . 141 8351 100.00 . . . . 0.1148 . . . . . . . . . . . 0.1760 
'X-RAY DIFFRACTION' 1.8155 1.8882 . . 152 8369 100.00 . . . . 0.1093 . . . . . . . . . . . 0.1701 
'X-RAY DIFFRACTION' 1.8882 1.9742 . . 135 8355 100.00 . . . . 0.1085 . . . . . . . . . . . 0.1498 
'X-RAY DIFFRACTION' 1.9742 2.0782 . . 141 8390 100.00 . . . . 0.0971 . . . . . . . . . . . 0.1626 
'X-RAY DIFFRACTION' 2.0782 2.2084 . . 136 8365 100.00 . . . . 0.0917 . . . . . . . . . . . 0.1236 
'X-RAY DIFFRACTION' 2.2084 2.3789 . . 154 8386 100.00 . . . . 0.0916 . . . . . . . . . . . 0.1393 
'X-RAY DIFFRACTION' 2.3789 2.6182 . . 121 8474 100.00 . . . . 0.0969 . . . . . . . . . . . 0.1437 
'X-RAY DIFFRACTION' 2.6182 2.9969 . . 147 8446 100.00 . . . . 0.1003 . . . . . . . . . . . 0.1129 
'X-RAY DIFFRACTION' 2.9969 3.7752 . . 151 8509 100.00 . . . . 0.1019 . . . . . . . . . . . 0.1243 
'X-RAY DIFFRACTION' 3.7752 35.913 . . 162 8711 100.00 . . . . 0.1306 . . . . . . . . . . . 0.1566 
# 
_struct.entry_id                     9CF4 
_struct.title                        'Crystal structure of the dimeric transaminase DoeD from C. salexigens DSM 3043.' 
_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        9CF4 
_struct_keywords.text            'Transaminase, L-2, 4-diaminobutyric acid, ectoine, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q1QTY7_CHRSD 
_struct_ref.pdbx_db_accession          Q1QTY7 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSQHQNLIDRDRKVTFHASTHLRDFAHGEAPGRVMAGGEGIHVVDKDGREFIDGFAGLYCVNIGYGRTEVAEAIHRQALE
LAYYHTYVGHSNEPQIQLSEKILELAGPGMSKVYYGMSGSDANETQLKIVRYYNNVLGRPQKKKVIARQRGYHGSGIASG
SLTGLKAFHDHFDLPIEGILHTEAPYYYHRGAEREGMSEREFSAHCAAKLEEMILAEGPETVAAFIGEPVLGTGGIVPPP
EGYWEAIQGVLAKYDVLLIADEVVCGFGRIGADFGSHHYAIKPDLITIAKGLTSAYQPLSGVIIGDRVWQVLEQGTGEFG
PIGHGWTYSGHALGCAAGLANLAIIEREGLTANAAETGAYLQQCMQQTFGEHPLVGEVRGVGMLAALEFSPAPARRAFFD
PALKVGPRVSAAAMSENLIARAMPQGDILGFAPPLVTTRAEVDEIVARAKRAVDKVTDELTRSGDLKA
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9CF4 A 1 ? 468 ? Q1QTY7 1 ? 468 ? 1 468 
2 1 9CF4 B 1 ? 468 ? Q1QTY7 1 ? 468 ? 1 468 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9CF4 HIS A 469 ? UNP Q1QTY7 ? ? 'expression tag' 469 1  
1 9CF4 HIS A 470 ? UNP Q1QTY7 ? ? 'expression tag' 470 2  
1 9CF4 HIS A 471 ? UNP Q1QTY7 ? ? 'expression tag' 471 3  
1 9CF4 HIS A 472 ? UNP Q1QTY7 ? ? 'expression tag' 472 4  
1 9CF4 HIS A 473 ? UNP Q1QTY7 ? ? 'expression tag' 473 5  
1 9CF4 HIS A 474 ? UNP Q1QTY7 ? ? 'expression tag' 474 6  
2 9CF4 HIS B 469 ? UNP Q1QTY7 ? ? 'expression tag' 469 7  
2 9CF4 HIS B 470 ? UNP Q1QTY7 ? ? 'expression tag' 470 8  
2 9CF4 HIS B 471 ? UNP Q1QTY7 ? ? 'expression tag' 471 9  
2 9CF4 HIS B 472 ? UNP Q1QTY7 ? ? 'expression tag' 472 10 
2 9CF4 HIS B 473 ? UNP Q1QTY7 ? ? 'expression tag' 473 11 
2 9CF4 HIS B 474 ? UNP Q1QTY7 ? ? 'expression tag' 474 12 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 12780 ? 
1 MORE         -76   ? 
1 'SSA (A^2)'  29660 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 SER A 2   ? LYS A 13  ? SER A 2   LYS A 13  1 ? 12 
HELX_P HELX_P2  AA2 HIS A 21  ? HIS A 27  ? HIS A 21  HIS A 27  1 ? 7  
HELX_P HELX_P3  AA3 PHE A 55  ? CYS A 60  ? PHE A 55  CYS A 60  1 ? 6  
HELX_P HELX_P4  AA4 ARG A 67  ? LEU A 79  ? ARG A 67  LEU A 79  1 ? 13 
HELX_P HELX_P5  AA5 ASN A 92  ? GLY A 107 ? ASN A 92  GLY A 107 1 ? 16 
HELX_P HELX_P6  AA6 SER A 118 ? LEU A 137 ? SER A 118 LEU A 137 1 ? 20 
HELX_P HELX_P7  AA7 ILE A 157 ? THR A 163 ? ILE A 157 THR A 163 1 ? 7  
HELX_P HELX_P8  AA8 LEU A 165 ? HIS A 169 ? LEU A 165 HIS A 169 5 ? 5  
HELX_P HELX_P9  AA9 TYR A 186 ? ARG A 190 ? TYR A 186 ARG A 190 5 ? 5  
HELX_P HELX_P10 AB1 GLY A 191 ? GLU A 195 ? GLY A 191 GLU A 195 5 ? 5  
HELX_P HELX_P11 AB2 SER A 198 ? GLY A 218 ? SER A 198 GLY A 218 1 ? 21 
HELX_P HELX_P12 AB3 GLY A 242 ? TYR A 254 ? GLY A 242 TYR A 254 1 ? 13 
HELX_P HELX_P13 AB4 PHE A 274 ? ALA A 280 ? PHE A 274 ALA A 280 1 ? 7  
HELX_P HELX_P14 AB5 ALA A 289 ? THR A 293 ? ALA A 289 THR A 293 5 ? 5  
HELX_P HELX_P15 AB6 ASP A 306 ? GLY A 320 ? ASP A 306 GLY A 320 1 ? 15 
HELX_P HELX_P16 AB7 HIS A 331 ? GLU A 348 ? HIS A 331 GLU A 348 1 ? 18 
HELX_P HELX_P17 AB8 GLY A 349 ? GLY A 370 ? GLY A 349 GLY A 370 1 ? 22 
HELX_P HELX_P18 AB9 ALA A 392 ? ARG A 396 ? ALA A 392 ARG A 396 5 ? 5  
HELX_P HELX_P19 AC1 ASP A 400 ? LEU A 403 ? ASP A 400 LEU A 403 5 ? 4  
HELX_P HELX_P20 AC2 LYS A 404 ? GLU A 416 ? LYS A 404 GLU A 416 1 ? 13 
HELX_P HELX_P21 AC3 THR A 438 ? SER A 463 ? THR A 438 SER A 463 1 ? 26 
HELX_P HELX_P22 AC4 GLN B 3   ? LYS B 13  ? GLN B 3   LYS B 13  1 ? 11 
HELX_P HELX_P23 AC5 HIS B 21  ? HIS B 27  ? HIS B 21  HIS B 27  1 ? 7  
HELX_P HELX_P24 AC6 PHE B 55  ? CYS B 60  ? PHE B 55  CYS B 60  1 ? 6  
HELX_P HELX_P25 AC7 ARG B 67  ? LEU B 81  ? ARG B 67  LEU B 81  1 ? 15 
HELX_P HELX_P26 AC8 ASN B 92  ? GLY B 107 ? ASN B 92  GLY B 107 1 ? 16 
HELX_P HELX_P27 AC9 SER B 118 ? LEU B 137 ? SER B 118 LEU B 137 1 ? 20 
HELX_P HELX_P28 AD1 ILE B 157 ? THR B 163 ? ILE B 157 THR B 163 1 ? 7  
HELX_P HELX_P29 AD2 LEU B 165 ? HIS B 169 ? LEU B 165 HIS B 169 5 ? 5  
HELX_P HELX_P30 AD3 TYR B 186 ? ARG B 190 ? TYR B 186 ARG B 190 5 ? 5  
HELX_P HELX_P31 AD4 GLY B 191 ? GLU B 195 ? GLY B 191 GLU B 195 5 ? 5  
HELX_P HELX_P32 AD5 SER B 198 ? GLY B 218 ? SER B 198 GLY B 218 1 ? 21 
HELX_P HELX_P33 AD6 GLY B 242 ? TYR B 254 ? GLY B 242 TYR B 254 1 ? 13 
HELX_P HELX_P34 AD7 PHE B 274 ? ALA B 280 ? PHE B 274 ALA B 280 1 ? 7  
HELX_P HELX_P35 AD8 ALA B 289 ? THR B 293 ? ALA B 289 THR B 293 5 ? 5  
HELX_P HELX_P36 AD9 ASP B 306 ? GLY B 320 ? ASP B 306 GLY B 320 1 ? 15 
HELX_P HELX_P37 AE1 HIS B 331 ? GLU B 348 ? HIS B 331 GLU B 348 1 ? 18 
HELX_P HELX_P38 AE2 GLY B 349 ? GLY B 370 ? GLY B 349 GLY B 370 1 ? 22 
HELX_P HELX_P39 AE3 ALA B 392 ? ARG B 396 ? ALA B 392 ARG B 396 5 ? 5  
HELX_P HELX_P40 AE4 ASP B 400 ? LEU B 403 ? ASP B 400 LEU B 403 5 ? 4  
HELX_P HELX_P41 AE5 LYS B 404 ? GLU B 416 ? LYS B 404 GLU B 416 1 ? 13 
HELX_P HELX_P42 AE6 THR B 438 ? SER B 463 ? THR B 438 SER B 463 1 ? 26 
# 
_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 
covale1 covale both ? A ALA 289 C ? ? ? 1_555 A LLP 290 N ? ? A ALA 289 A LLP 290 1_555 ? ? ? ? ? ? ? 1.336 ? ? 
covale2 covale both ? A LLP 290 C ? ? ? 1_555 A GLY 291 N ? ? A LLP 290 A GLY 291 1_555 ? ? ? ? ? ? ? 1.333 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      LLP 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       290 
_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                       LLP 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        290 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_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                LYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        LLP 
_pdbx_modification_feature.type                               'Pyridoxal phosphate' 
_pdbx_modification_feature.category                           'Named protein modification' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 LEU 174 A . ? LEU 174 A PRO 175 A ? PRO 175 A 1 4.27 
2 LEU 174 B . ? LEU 174 B PRO 175 B ? PRO 175 B 1 5.59 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 7 ? 
AA4 ? 4 ? 
AA5 ? 7 ? 
AA6 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA3 6 7 ? 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 
AA5 3 4 ? parallel      
AA5 4 5 ? parallel      
AA5 5 6 ? parallel      
AA5 6 7 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 418 ? ILE A 419 ? LEU A 418 ILE A 419 
AA1 2 GLU A 50  ? ASP A 53  ? GLU A 50  ASP A 53  
AA1 3 HIS A 42  ? ASP A 45  ? HIS A 42  ASP A 45  
AA1 4 ARG A 33  ? GLU A 39  ? ARG A 33  GLU A 39  
AA1 5 HIS B 90  ? SER B 91  ? HIS B 90  SER B 91  
AA2 1 HIS A 90  ? SER A 91  ? HIS A 90  SER A 91  
AA2 2 ARG B 33  ? GLU B 39  ? ARG B 33  GLU B 39  
AA2 3 HIS B 42  ? ASP B 45  ? HIS B 42  ASP B 45  
AA2 4 GLU B 50  ? ASP B 53  ? GLU B 50  ASP B 53  
AA2 5 LEU B 418 ? ILE B 419 ? LEU B 418 ILE B 419 
AA3 1 MET A 110 ? GLY A 116 ? MET A 110 GLY A 116 
AA3 2 SER A 300 ? GLY A 305 ? SER A 300 GLY A 305 
AA3 3 LEU A 285 ? ILE A 288 ? LEU A 285 ILE A 288 
AA3 4 LEU A 257 ? ASP A 261 ? LEU A 257 ASP A 261 
AA3 5 VAL A 222 ? GLY A 227 ? VAL A 222 GLY A 227 
AA3 6 LYS A 144 ? ARG A 148 ? LYS A 144 ARG A 148 
AA3 7 ILE A 179 ? THR A 182 ? ILE A 179 THR A 182 
AA4 1 VAL A 375 ? VAL A 381 ? VAL A 375 VAL A 381 
AA4 2 LEU A 384 ? PHE A 389 ? LEU A 384 PHE A 389 
AA4 3 ILE A 428 ? PHE A 431 ? ILE A 428 PHE A 431 
AA4 4 ARG A 421 ? ALA A 422 ? ARG A 421 ALA A 422 
AA5 1 MET B 110 ? GLY B 116 ? MET B 110 GLY B 116 
AA5 2 SER B 300 ? GLY B 305 ? SER B 300 GLY B 305 
AA5 3 LEU B 285 ? ILE B 288 ? LEU B 285 ILE B 288 
AA5 4 LEU B 257 ? ASP B 261 ? LEU B 257 ASP B 261 
AA5 5 VAL B 222 ? GLY B 227 ? VAL B 222 GLY B 227 
AA5 6 LYS B 144 ? ARG B 148 ? LYS B 144 ARG B 148 
AA5 7 ILE B 179 ? THR B 182 ? ILE B 179 THR B 182 
AA6 1 VAL B 375 ? VAL B 381 ? VAL B 375 VAL B 381 
AA6 2 LEU B 384 ? PHE B 389 ? LEU B 384 PHE B 389 
AA6 3 ILE B 428 ? PHE B 431 ? ILE B 428 PHE B 431 
AA6 4 ARG B 421 ? ALA B 422 ? ARG B 421 ALA B 422 
# 
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 ILE A 419 ? O ILE A 419 N ILE A 52  ? N ILE A 52  
AA1 2 3 O PHE A 51  ? O PHE A 51  N VAL A 43  ? N VAL A 43  
AA1 3 4 O VAL A 44  ? O VAL A 44  N ALA A 36  ? N ALA A 36  
AA1 4 5 N MET A 35  ? N MET A 35  O SER B 91  ? O SER B 91  
AA2 1 2 N SER A 91  ? N SER A 91  O ARG B 33  ? O ARG B 33  
AA2 2 3 N ALA B 36  ? N ALA B 36  O VAL B 44  ? O VAL B 44  
AA2 3 4 N VAL B 43  ? N VAL B 43  O PHE B 51  ? O PHE B 51  
AA2 4 5 N ILE B 52  ? N ILE B 52  O ILE B 419 ? O ILE B 419 
AA3 1 2 N SER A 111 ? N SER A 111 O ILE A 304 ? O ILE A 304 
AA3 2 3 O ILE A 303 ? O ILE A 303 N ILE A 286 ? N ILE A 286 
AA3 3 4 O LEU A 285 ? O LEU A 285 N ALA A 260 ? N ALA A 260 
AA3 4 5 O ILE A 259 ? O ILE A 259 N PHE A 225 ? N PHE A 225 
AA3 5 6 O ALA A 224 ? O ALA A 224 N ILE A 146 ? N ILE A 146 
AA3 6 7 N ALA A 147 ? N ALA A 147 O LEU A 180 ? O LEU A 180 
AA4 1 2 N GLU A 377 ? N GLU A 377 O GLU A 388 ? O GLU A 388 
AA4 2 3 N ALA A 385 ? N ALA A 385 O PHE A 431 ? O PHE A 431 
AA4 3 4 O GLY A 430 ? O GLY A 430 N ARG A 421 ? N ARG A 421 
AA5 1 2 N SER B 111 ? N SER B 111 O ILE B 304 ? O ILE B 304 
AA5 2 3 O ILE B 303 ? O ILE B 303 N ILE B 286 ? N ILE B 286 
AA5 3 4 O LEU B 285 ? O LEU B 285 N ALA B 260 ? N ALA B 260 
AA5 4 5 O ILE B 259 ? O ILE B 259 N PHE B 225 ? N PHE B 225 
AA5 5 6 O ALA B 224 ? O ALA B 224 N ILE B 146 ? N ILE B 146 
AA5 6 7 N ALA B 147 ? N ALA B 147 O LEU B 180 ? O LEU B 180 
AA6 1 2 N GLU B 377 ? N GLU B 377 O GLU B 388 ? O GLU B 388 
AA6 2 3 N ALA B 385 ? N ALA B 385 O PHE B 431 ? O PHE B 431 
AA6 3 4 O GLY B 430 ? O GLY B 430 N ARG B 421 ? N ARG B 421 
# 
_pdbx_entry_details.entry_id                   9CF4 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1   1 O    A HOH 951  ? ? O   A HOH 962  ? ? 1.45 
2   1 H    A GLY 109  ? ? O   A HOH 610  ? ? 1.46 
3   1 O    B HOH 740  ? ? O   B HOH 787  ? ? 1.50 
4   1 OP3  A LLP 290  ? ? H   B THR 327  ? ? 1.54 
5   1 O    B HOH 740  ? ? O   B HOH 805  ? ? 1.55 
6   1 HZ3  A LYS 282  ? ? O   A HOH 612  ? ? 1.56 
7   1 HO1  A GOL 504  ? ? O   A HOH 601  ? ? 1.57 
8   1 HE21 A GLN 366  ? ? O   A HOH 615  ? ? 1.57 
9   1 HE22 B GLN 95   ? B O   B HOH 602  ? ? 1.58 
10  1 HH22 A ARG 421  ? A O   A HOH 606  ? ? 1.59 
11  1 O    A HOH 894  ? ? O   A HOH 969  ? ? 1.68 
12  1 O    A HOH 995  ? ? O   A HOH 1008 ? ? 1.74 
13  1 O    A HOH 739  ? ? O   A HOH 754  ? ? 1.74 
14  1 O    A HOH 615  ? ? O   A HOH 944  ? ? 1.75 
15  1 O    A HOH 738  ? ? O   A HOH 1053 ? ? 1.75 
16  1 O    B HOH 871  ? ? O   B HOH 933  ? ? 1.77 
17  1 O    A HOH 964  ? ? O   A HOH 1023 ? ? 1.77 
18  1 O    A HOH 830  ? ? O   A HOH 970  ? ? 1.78 
19  1 O    B HOH 628  ? ? O   B HOH 654  ? ? 1.81 
20  1 O    A HOH 622  ? ? O   A HOH 894  ? ? 1.82 
21  1 O    B HOH 765  ? ? O   B HOH 864  ? ? 1.83 
22  1 O    A HOH 906  ? ? O   A HOH 941  ? ? 1.85 
23  1 O    B HOH 946  ? ? O   B HOH 1023 ? ? 1.87 
24  1 O    A HOH 933  ? ? O   A HOH 1039 ? ? 1.87 
25  1 O    A HOH 839  ? ? O   A HOH 1186 ? ? 1.88 
26  1 O    B HOH 741  ? ? O   B HOH 858  ? ? 1.88 
27  1 O    A HOH 714  ? ? O   A HOH 905  ? ? 1.88 
28  1 O    A HOH 696  ? ? O   A HOH 1143 ? ? 1.89 
29  1 NZ   B LYS 290  ? ? C4A B PLP 502  ? ? 1.91 
30  1 O    B HOH 1024 ? ? O   B HOH 1040 ? ? 1.91 
31  1 O    A HOH 1062 ? ? O   A HOH 1121 ? ? 1.92 
32  1 O    B HOH 810  ? ? O   B HOH 905  ? ? 1.92 
33  1 O    B HOH 1059 ? ? O   B HOH 1078 ? ? 1.93 
34  1 O    A HOH 802  ? ? O   B HOH 602  ? ? 1.95 
35  1 O    B HOH 798  ? ? O   B HOH 865  ? ? 1.96 
36  1 O    A HOH 1075 ? ? O   A HOH 1109 ? ? 1.96 
37  1 O    A HOH 610  ? ? O   A HOH 1143 ? ? 1.97 
38  1 O    B HOH 902  ? ? O   B HOH 1018 ? ? 1.97 
39  1 O    A HOH 640  ? ? O   A HOH 1103 ? ? 1.98 
40  1 O    B HOH 625  ? ? O   B HOH 1065 ? ? 1.98 
41  1 O    A HOH 753  ? ? O   A HOH 907  ? ? 1.98 
42  1 O    A HOH 984  ? ? O   A HOH 1141 ? ? 1.99 
43  1 O    A HOH 1023 ? ? O   A HOH 1075 ? ? 1.99 
44  1 O    A HOH 607  ? ? O   A HOH 778  ? ? 1.99 
45  1 O    A HOH 1039 ? ? O   B HOH 1064 ? ? 1.99 
46  1 O    A HOH 920  ? ? O   A HOH 973  ? ? 1.99 
47  1 O    A HOH 813  ? ? O   A HOH 1071 ? ? 1.99 
48  1 O    A HOH 1027 ? ? O   A HOH 1069 ? ? 2.00 
49  1 O    B HOH 1070 ? ? O   B HOH 1102 ? ? 2.00 
50  1 O    B HOH 664  ? ? O   B HOH 900  ? ? 2.01 
51  1 O    A HOH 776  ? ? O   A HOH 916  ? ? 2.02 
52  1 O    A HOH 676  ? ? O   A HOH 1103 ? ? 2.02 
53  1 OE1  B GLN 3    ? ? O   B HOH 601  ? ? 2.03 
54  1 O    B HOH 1025 ? ? O   B HOH 1063 ? ? 2.03 
55  1 NE2  B GLN 95   ? B O   B HOH 602  ? ? 2.04 
56  1 O    B HOH 1012 ? ? O   B HOH 1115 ? ? 2.04 
57  1 O    A HOH 920  ? ? O   B HOH 762  ? ? 2.05 
58  1 O    A HOH 1139 ? ? O   A HOH 1176 ? ? 2.06 
59  1 O    A HOH 970  ? ? O   A HOH 992  ? ? 2.06 
60  1 O    A HOH 911  ? ? O   A HOH 941  ? ? 2.06 
61  1 O    A HOH 609  ? ? O   A HOH 915  ? ? 2.06 
62  1 O    A HOH 887  ? ? O   A HOH 1052 ? ? 2.07 
63  1 O1   A GOL 504  ? ? O   A HOH 601  ? ? 2.07 
64  1 O    B HOH 896  ? ? O   B HOH 1026 ? ? 2.07 
65  1 O    B HOH 902  ? ? O   B HOH 1027 ? ? 2.08 
66  1 O    B HOH 929  ? ? O   B HOH 1060 ? ? 2.08 
67  1 O    A HOH 1036 ? ? O   A HOH 1100 ? ? 2.09 
68  1 O    A HOH 603  ? ? O   A HOH 1163 ? ? 2.09 
69  1 OE1  A GLU 245  ? ? O   A HOH 602  ? ? 2.10 
70  1 O    A HOH 1058 ? ? O   A HOH 1131 ? ? 2.10 
71  1 O    A HOH 989  ? ? O   A HOH 1138 ? ? 2.10 
72  1 O    A HOH 884  ? ? O   A HOH 902  ? ? 2.11 
73  1 O    B HOH 990  ? ? O   B HOH 1102 ? ? 2.11 
74  1 O    B HOH 964  ? ? O   B HOH 1075 ? ? 2.11 
75  1 O    A HOH 877  ? ? O   A HOH 1060 ? ? 2.11 
76  1 O    A HOH 609  ? ? O   A HOH 980  ? ? 2.12 
77  1 O    A HOH 894  ? ? O   A HOH 907  ? ? 2.12 
78  1 O    A HOH 1005 ? ? O   A HOH 1118 ? ? 2.12 
79  1 O    A HOH 830  ? ? O   A HOH 992  ? ? 2.12 
80  1 O    A HOH 772  ? ? O   A HOH 1118 ? ? 2.13 
81  1 O    A HOH 916  ? ? O   A HOH 1184 ? ? 2.13 
82  1 O    B HOH 718  ? ? O   B HOH 1063 ? ? 2.13 
83  1 O    A HOH 676  ? ? O   A HOH 1092 ? ? 2.14 
84  1 O    A HOH 1036 ? ? O   B HOH 910  ? ? 2.14 
85  1 O    B HOH 995  ? ? O   B HOH 1037 ? ? 2.14 
86  1 OE1  A GLU 318  ? ? O   A HOH 603  ? ? 2.15 
87  1 O    A HOH 991  ? ? O   A HOH 1084 ? ? 2.15 
88  1 O    B HOH 871  ? ? O   B HOH 1026 ? ? 2.16 
89  1 O    B HOH 890  ? ? O   B HOH 978  ? ? 2.16 
90  1 O    B HOH 762  ? ? O   B HOH 957  ? ? 2.17 
91  1 O    B HOH 662  ? ? O   B HOH 780  ? ? 2.17 
92  1 O    B HOH 676  ? ? O   B HOH 1131 ? ? 2.17 
93  1 O    A HOH 884  ? ? O   B HOH 698  ? ? 2.17 
94  1 O    A HOH 611  ? ? O   B HOH 631  ? ? 2.17 
95  1 O    A HOH 682  ? ? O   A HOH 1048 ? ? 2.18 
96  1 O    B HOH 751  ? ? O   B HOH 1000 ? ? 2.18 
97  1 O    A HOH 1067 ? ? O   A HOH 1123 ? ? 2.18 
98  1 O    B HOH 673  ? ? O   B HOH 1035 ? ? 2.19 
99  1 O    B HOH 990  ? ? O   B HOH 1005 ? ? 2.19 
100 1 O    A HOH 681  ? ? O   A HOH 1132 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1  1 O A HOH 1053 ? ? 1_555 O B HOH 1057 ? ? 5_445 1.88 
2  1 O A HOH 1094 ? ? 1_555 O A HOH 1143 ? ? 8_445 1.91 
3  1 O A HOH 609  ? ? 1_555 O A HOH 665  ? ? 5_455 2.01 
4  1 O B HOH 954  ? ? 1_555 O B HOH 1125 ? ? 5_555 2.09 
5  1 O B HOH 660  ? ? 1_555 O B HOH 896  ? ? 3_554 2.12 
6  1 O A HOH 609  ? ? 1_555 O A HOH 833  ? ? 5_455 2.13 
7  1 O B HOH 946  ? ? 1_555 O B HOH 959  ? ? 3_554 2.14 
8  1 O A HOH 686  ? ? 1_555 O B HOH 818  ? ? 1_455 2.16 
9  1 O A HOH 890  ? ? 1_555 O A HOH 1131 ? ? 4_545 2.16 
10 1 O A HOH 1016 ? ? 1_555 O B HOH 689  ? ? 8_445 2.17 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 C A ILE 176 ? ? N A GLU 177 ? ? 1.180 1.336 -0.156 0.023 Y 
2 1 C A GLU 177 ? ? N A GLY 178 ? ? 1.547 1.336 0.211  0.023 Y 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A PHE 16  ? ? CG A PHE 16  ? ? CD1 A PHE 16  ? ? 125.18 120.80 4.38   0.70 N 
2 1 CA A GLU 177 ? ? C  A GLU 177 ? ? N   A GLY 178 ? ? 99.19  116.20 -17.01 2.00 Y 
3 1 O  A GLU 177 ? ? C  A GLU 177 ? ? N   A GLY 178 ? ? 138.82 123.20 15.62  1.70 Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 GLU A 80  ? ? -97.42  -66.30  
2  1 LYS A 143 ? ? -141.56 -18.68  
3  1 ALA A 147 ? ? -108.19 -166.99 
4  1 HIS A 171 ? ? 75.49   -1.85   
5  1 ILE A 236 ? ? 55.70   71.82   
6  1 LYS A 282 ? ? -117.37 79.61   
7  1 ALA A 289 ? ? -169.43 -143.14 
8  1 LLP A 290 ? ? 41.92   -99.52  
9  1 MET A 383 ? ? -91.10  35.83   
10 1 ALA A 392 ? ? -154.41 79.63   
11 1 GLU B 80  ? ? -95.32  -64.68  
12 1 LEU B 81  ? ? -160.03 115.22  
13 1 LYS B 143 ? ? -140.57 -16.77  
14 1 ALA B 147 ? ? -107.77 -167.61 
15 1 HIS B 171 ? ? 75.56   -4.55   
16 1 ILE B 236 ? ? 58.03   71.79   
17 1 ALA B 289 ? ? -166.41 -140.45 
18 1 LYS B 290 ? ? 34.22   -94.31  
19 1 MET B 383 ? A -96.62  35.14   
20 1 MET B 383 ? B -96.64  34.21   
21 1 ALA B 392 ? ? -158.43 83.82   
# 
_pdbx_validate_polymer_linkage.id               1 
_pdbx_validate_polymer_linkage.PDB_model_num    1 
_pdbx_validate_polymer_linkage.auth_atom_id_1   C 
_pdbx_validate_polymer_linkage.auth_asym_id_1   A 
_pdbx_validate_polymer_linkage.auth_comp_id_1   ILE 
_pdbx_validate_polymer_linkage.auth_seq_id_1    176 
_pdbx_validate_polymer_linkage.PDB_ins_code_1   ? 
_pdbx_validate_polymer_linkage.label_alt_id_1   ? 
_pdbx_validate_polymer_linkage.auth_atom_id_2   N 
_pdbx_validate_polymer_linkage.auth_asym_id_2   A 
_pdbx_validate_polymer_linkage.auth_comp_id_2   GLU 
_pdbx_validate_polymer_linkage.auth_seq_id_2    177 
_pdbx_validate_polymer_linkage.PDB_ins_code_2   ? 
_pdbx_validate_polymer_linkage.label_alt_id_2   ? 
_pdbx_validate_polymer_linkage.dist             1.18 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     1191 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   I 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 1226 ? 6.01 . 
2 1 O ? A HOH 1227 ? 6.08 . 
3 1 O ? B HOH 1157 ? 5.96 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A LYS 467 ? A LYS 467 
3  1 Y 1 A ALA 468 ? A ALA 468 
4  1 Y 1 A HIS 469 ? A HIS 469 
5  1 Y 1 A HIS 470 ? A HIS 470 
6  1 Y 1 A HIS 471 ? A HIS 471 
7  1 Y 1 A HIS 472 ? A HIS 472 
8  1 Y 1 A HIS 473 ? A HIS 473 
9  1 Y 1 A HIS 474 ? A HIS 474 
10 1 Y 1 B MET 1   ? B MET 1   
11 1 Y 1 B LYS 467 ? B LYS 467 
12 1 Y 1 B ALA 468 ? B ALA 468 
13 1 Y 1 B HIS 469 ? B HIS 469 
14 1 Y 1 B HIS 470 ? B HIS 470 
15 1 Y 1 B HIS 471 ? B HIS 471 
16 1 Y 1 B HIS 472 ? B HIS 472 
17 1 Y 1 B HIS 473 ? B HIS 473 
18 1 Y 1 B HIS 474 ? B HIS 474 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ARG N      N N N 14  
ARG CA     C N S 15  
ARG C      C N N 16  
ARG O      O N N 17  
ARG CB     C N N 18  
ARG CG     C N N 19  
ARG CD     C N N 20  
ARG NE     N N N 21  
ARG CZ     C N N 22  
ARG NH1    N N N 23  
ARG NH2    N N N 24  
ARG OXT    O N N 25  
ARG H      H N N 26  
ARG H2     H N N 27  
ARG HA     H N N 28  
ARG HB2    H N N 29  
ARG HB3    H N N 30  
ARG HG2    H N N 31  
ARG HG3    H N N 32  
ARG HD2    H N N 33  
ARG HD3    H N N 34  
ARG HE     H N N 35  
ARG HH11   H N N 36  
ARG HH12   H N N 37  
ARG HH21   H N N 38  
ARG HH22   H N N 39  
ARG HXT    H N N 40  
ASN N      N N N 41  
ASN CA     C N S 42  
ASN C      C N N 43  
ASN O      O N N 44  
ASN CB     C N N 45  
ASN CG     C N N 46  
ASN OD1    O N N 47  
ASN ND2    N N N 48  
ASN OXT    O N N 49  
ASN H      H N N 50  
ASN H2     H N N 51  
ASN HA     H N N 52  
ASN HB2    H N N 53  
ASN HB3    H N N 54  
ASN HD21   H N N 55  
ASN HD22   H N N 56  
ASN HXT    H N N 57  
ASP N      N N N 58  
ASP CA     C N S 59  
ASP C      C N N 60  
ASP O      O N N 61  
ASP CB     C N N 62  
ASP CG     C N N 63  
ASP OD1    O N N 64  
ASP OD2    O N N 65  
ASP OXT    O N N 66  
ASP H      H N N 67  
ASP H2     H N N 68  
ASP HA     H N N 69  
ASP HB2    H N N 70  
ASP HB3    H N N 71  
ASP HD2    H N N 72  
ASP HXT    H N N 73  
CYS N      N N N 74  
CYS CA     C N R 75  
CYS C      C N N 76  
CYS O      O N N 77  
CYS CB     C N N 78  
CYS SG     S N N 79  
CYS OXT    O N N 80  
CYS H      H N N 81  
CYS H2     H N N 82  
CYS HA     H N N 83  
CYS HB2    H N N 84  
CYS HB3    H N N 85  
CYS HG     H N N 86  
CYS HXT    H N N 87  
GLN N      N N N 88  
GLN CA     C N S 89  
GLN C      C N N 90  
GLN O      O N N 91  
GLN CB     C N N 92  
GLN CG     C N N 93  
GLN CD     C N N 94  
GLN OE1    O N N 95  
GLN NE2    N N N 96  
GLN OXT    O N N 97  
GLN H      H N N 98  
GLN H2     H N N 99  
GLN HA     H N N 100 
GLN HB2    H N N 101 
GLN HB3    H N N 102 
GLN HG2    H N N 103 
GLN HG3    H N N 104 
GLN HE21   H N N 105 
GLN HE22   H N N 106 
GLN HXT    H N N 107 
GLU N      N N N 108 
GLU CA     C N S 109 
GLU C      C N N 110 
GLU O      O N N 111 
GLU CB     C N N 112 
GLU CG     C N N 113 
GLU CD     C N N 114 
GLU OE1    O N N 115 
GLU OE2    O N N 116 
GLU OXT    O N N 117 
GLU H      H N N 118 
GLU H2     H N N 119 
GLU HA     H N N 120 
GLU HB2    H N N 121 
GLU HB3    H N N 122 
GLU HG2    H N N 123 
GLU HG3    H N N 124 
GLU HE2    H N N 125 
GLU HXT    H N N 126 
GLY N      N N N 127 
GLY CA     C N N 128 
GLY C      C N N 129 
GLY O      O N N 130 
GLY OXT    O N N 131 
GLY H      H N N 132 
GLY H2     H N N 133 
GLY HA2    H N N 134 
GLY HA3    H N N 135 
GLY HXT    H N N 136 
GOL C1     C N N 137 
GOL O1     O N N 138 
GOL C2     C N N 139 
GOL O2     O N N 140 
GOL C3     C N N 141 
GOL O3     O N N 142 
GOL H11    H N N 143 
GOL H12    H N N 144 
GOL HO1    H N N 145 
GOL H2     H N N 146 
GOL HO2    H N N 147 
GOL H31    H N N 148 
GOL H32    H N N 149 
GOL HO3    H N N 150 
HIS N      N N N 151 
HIS CA     C N S 152 
HIS C      C N N 153 
HIS O      O N N 154 
HIS CB     C N N 155 
HIS CG     C Y N 156 
HIS ND1    N Y N 157 
HIS CD2    C Y N 158 
HIS CE1    C Y N 159 
HIS NE2    N Y N 160 
HIS OXT    O N N 161 
HIS H      H N N 162 
HIS H2     H N N 163 
HIS HA     H N N 164 
HIS HB2    H N N 165 
HIS HB3    H N N 166 
HIS HD1    H N N 167 
HIS HD2    H N N 168 
HIS HE1    H N N 169 
HIS HE2    H N N 170 
HIS HXT    H N N 171 
HOH O      O N N 172 
HOH H1     H N N 173 
HOH H2     H N N 174 
ILE N      N N N 175 
ILE CA     C N S 176 
ILE C      C N N 177 
ILE O      O N N 178 
ILE CB     C N S 179 
ILE CG1    C N N 180 
ILE CG2    C N N 181 
ILE CD1    C N N 182 
ILE OXT    O N N 183 
ILE H      H N N 184 
ILE H2     H N N 185 
ILE HA     H N N 186 
ILE HB     H N N 187 
ILE HG12   H N N 188 
ILE HG13   H N N 189 
ILE HG21   H N N 190 
ILE HG22   H N N 191 
ILE HG23   H N N 192 
ILE HD11   H N N 193 
ILE HD12   H N N 194 
ILE HD13   H N N 195 
ILE HXT    H N N 196 
LEU N      N N N 197 
LEU CA     C N S 198 
LEU C      C N N 199 
LEU O      O N N 200 
LEU CB     C N N 201 
LEU CG     C N N 202 
LEU CD1    C N N 203 
LEU CD2    C N N 204 
LEU OXT    O N N 205 
LEU H      H N N 206 
LEU H2     H N N 207 
LEU HA     H N N 208 
LEU HB2    H N N 209 
LEU HB3    H N N 210 
LEU HG     H N N 211 
LEU HD11   H N N 212 
LEU HD12   H N N 213 
LEU HD13   H N N 214 
LEU HD21   H N N 215 
LEU HD22   H N N 216 
LEU HD23   H N N 217 
LEU HXT    H N N 218 
LLP N1     N Y N 219 
LLP C2     C Y N 220 
LLP "C2'"  C N N 221 
LLP C3     C Y N 222 
LLP O3     O N N 223 
LLP C4     C Y N 224 
LLP "C4'"  C N N 225 
LLP C5     C Y N 226 
LLP C6     C Y N 227 
LLP "C5'"  C N N 228 
LLP OP4    O N N 229 
LLP P      P N N 230 
LLP OP1    O N N 231 
LLP OP2    O N N 232 
LLP OP3    O N N 233 
LLP N      N N N 234 
LLP CA     C N S 235 
LLP CB     C N N 236 
LLP CG     C N N 237 
LLP CD     C N N 238 
LLP CE     C N N 239 
LLP NZ     N N N 240 
LLP C      C N N 241 
LLP O      O N N 242 
LLP OXT    O N N 243 
LLP "H2'1" H N N 244 
LLP "H2'2" H N N 245 
LLP "H2'3" H N N 246 
LLP HO3    H N N 247 
LLP "H4'1" H N N 248 
LLP H6     H N N 249 
LLP "H5'1" H N N 250 
LLP "H5'2" H N N 251 
LLP HOP2   H N N 252 
LLP HOP3   H N N 253 
LLP H      H N N 254 
LLP H2     H N N 255 
LLP HA     H N N 256 
LLP HB2    H N N 257 
LLP HB3    H N N 258 
LLP HG2    H N N 259 
LLP HG3    H N N 260 
LLP HD2    H N N 261 
LLP HD3    H N N 262 
LLP HE2    H N N 263 
LLP HE3    H N N 264 
LLP HXT    H N N 265 
LYS N      N N N 266 
LYS CA     C N S 267 
LYS C      C N N 268 
LYS O      O N N 269 
LYS CB     C N N 270 
LYS CG     C N N 271 
LYS CD     C N N 272 
LYS CE     C N N 273 
LYS NZ     N N N 274 
LYS OXT    O N N 275 
LYS H      H N N 276 
LYS H2     H N N 277 
LYS HA     H N N 278 
LYS HB2    H N N 279 
LYS HB3    H N N 280 
LYS HG2    H N N 281 
LYS HG3    H N N 282 
LYS HD2    H N N 283 
LYS HD3    H N N 284 
LYS HE2    H N N 285 
LYS HE3    H N N 286 
LYS HZ1    H N N 287 
LYS HZ2    H N N 288 
LYS HZ3    H N N 289 
LYS HXT    H N N 290 
MET N      N N N 291 
MET CA     C N S 292 
MET C      C N N 293 
MET O      O N N 294 
MET CB     C N N 295 
MET CG     C N N 296 
MET SD     S N N 297 
MET CE     C N N 298 
MET OXT    O N N 299 
MET H      H N N 300 
MET H2     H N N 301 
MET HA     H N N 302 
MET HB2    H N N 303 
MET HB3    H N N 304 
MET HG2    H N N 305 
MET HG3    H N N 306 
MET HE1    H N N 307 
MET HE2    H N N 308 
MET HE3    H N N 309 
MET HXT    H N N 310 
PHE N      N N N 311 
PHE CA     C N S 312 
PHE C      C N N 313 
PHE O      O N N 314 
PHE CB     C N N 315 
PHE CG     C Y N 316 
PHE CD1    C Y N 317 
PHE CD2    C Y N 318 
PHE CE1    C Y N 319 
PHE CE2    C Y N 320 
PHE CZ     C Y N 321 
PHE OXT    O N N 322 
PHE H      H N N 323 
PHE H2     H N N 324 
PHE HA     H N N 325 
PHE HB2    H N N 326 
PHE HB3    H N N 327 
PHE HD1    H N N 328 
PHE HD2    H N N 329 
PHE HE1    H N N 330 
PHE HE2    H N N 331 
PHE HZ     H N N 332 
PHE HXT    H N N 333 
PLP N1     N Y N 334 
PLP C2     C Y N 335 
PLP C2A    C N N 336 
PLP C3     C Y N 337 
PLP O3     O N N 338 
PLP C4     C Y N 339 
PLP C4A    C N N 340 
PLP O4A    O N N 341 
PLP C5     C Y N 342 
PLP C6     C Y N 343 
PLP C5A    C N N 344 
PLP O4P    O N N 345 
PLP P      P N N 346 
PLP O1P    O N N 347 
PLP O2P    O N N 348 
PLP O3P    O N N 349 
PLP H2A1   H N N 350 
PLP H2A2   H N N 351 
PLP H2A3   H N N 352 
PLP HO3    H N N 353 
PLP H4A    H N N 354 
PLP H6     H N N 355 
PLP H5A1   H N N 356 
PLP H5A2   H N N 357 
PLP HOP2   H N N 358 
PLP HOP3   H N N 359 
PRO N      N N N 360 
PRO CA     C N S 361 
PRO C      C N N 362 
PRO O      O N N 363 
PRO CB     C N N 364 
PRO CG     C N N 365 
PRO CD     C N N 366 
PRO OXT    O N N 367 
PRO H      H N N 368 
PRO HA     H N N 369 
PRO HB2    H N N 370 
PRO HB3    H N N 371 
PRO HG2    H N N 372 
PRO HG3    H N N 373 
PRO HD2    H N N 374 
PRO HD3    H N N 375 
PRO HXT    H N N 376 
SER N      N N N 377 
SER CA     C N S 378 
SER C      C N N 379 
SER O      O N N 380 
SER CB     C N N 381 
SER OG     O N N 382 
SER OXT    O N N 383 
SER H      H N N 384 
SER H2     H N N 385 
SER HA     H N N 386 
SER HB2    H N N 387 
SER HB3    H N N 388 
SER HG     H N N 389 
SER HXT    H N N 390 
THR N      N N N 391 
THR CA     C N S 392 
THR C      C N N 393 
THR O      O N N 394 
THR CB     C N R 395 
THR OG1    O N N 396 
THR CG2    C N N 397 
THR OXT    O N N 398 
THR H      H N N 399 
THR H2     H N N 400 
THR HA     H N N 401 
THR HB     H N N 402 
THR HG1    H N N 403 
THR HG21   H N N 404 
THR HG22   H N N 405 
THR HG23   H N N 406 
THR HXT    H N N 407 
TRP N      N N N 408 
TRP CA     C N S 409 
TRP C      C N N 410 
TRP O      O N N 411 
TRP CB     C N N 412 
TRP CG     C Y N 413 
TRP CD1    C Y N 414 
TRP CD2    C Y N 415 
TRP NE1    N Y N 416 
TRP CE2    C Y N 417 
TRP CE3    C Y N 418 
TRP CZ2    C Y N 419 
TRP CZ3    C Y N 420 
TRP CH2    C Y N 421 
TRP OXT    O N N 422 
TRP H      H N N 423 
TRP H2     H N N 424 
TRP HA     H N N 425 
TRP HB2    H N N 426 
TRP HB3    H N N 427 
TRP HD1    H N N 428 
TRP HE1    H N N 429 
TRP HE3    H N N 430 
TRP HZ2    H N N 431 
TRP HZ3    H N N 432 
TRP HH2    H N N 433 
TRP HXT    H N N 434 
TYR N      N N N 435 
TYR CA     C N S 436 
TYR C      C N N 437 
TYR O      O N N 438 
TYR CB     C N N 439 
TYR CG     C Y N 440 
TYR CD1    C Y N 441 
TYR CD2    C Y N 442 
TYR CE1    C Y N 443 
TYR CE2    C Y N 444 
TYR CZ     C Y N 445 
TYR OH     O N N 446 
TYR OXT    O N N 447 
TYR H      H N N 448 
TYR H2     H N N 449 
TYR HA     H N N 450 
TYR HB2    H N N 451 
TYR HB3    H N N 452 
TYR HD1    H N N 453 
TYR HD2    H N N 454 
TYR HE1    H N N 455 
TYR HE2    H N N 456 
TYR HH     H N N 457 
TYR HXT    H N N 458 
VAL N      N N N 459 
VAL CA     C N S 460 
VAL C      C N N 461 
VAL O      O N N 462 
VAL CB     C N N 463 
VAL CG1    C N N 464 
VAL CG2    C N N 465 
VAL OXT    O N N 466 
VAL H      H N N 467 
VAL H2     H N N 468 
VAL HA     H N N 469 
VAL HB     H N N 470 
VAL HG11   H N N 471 
VAL HG12   H N N 472 
VAL HG13   H N N 473 
VAL HG21   H N N 474 
VAL HG22   H N N 475 
VAL HG23   H N N 476 
VAL HXT    H N N 477 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
GLN N     CA     sing N N 83  
GLN N     H      sing N N 84  
GLN N     H2     sing N N 85  
GLN CA    C      sing N N 86  
GLN CA    CB     sing N N 87  
GLN CA    HA     sing N N 88  
GLN C     O      doub N N 89  
GLN C     OXT    sing N N 90  
GLN CB    CG     sing N N 91  
GLN CB    HB2    sing N N 92  
GLN CB    HB3    sing N N 93  
GLN CG    CD     sing N N 94  
GLN CG    HG2    sing N N 95  
GLN CG    HG3    sing N N 96  
GLN CD    OE1    doub N N 97  
GLN CD    NE2    sing N N 98  
GLN NE2   HE21   sing N N 99  
GLN NE2   HE22   sing N N 100 
GLN OXT   HXT    sing N N 101 
GLU N     CA     sing N N 102 
GLU N     H      sing N N 103 
GLU N     H2     sing N N 104 
GLU CA    C      sing N N 105 
GLU CA    CB     sing N N 106 
GLU CA    HA     sing N N 107 
GLU C     O      doub N N 108 
GLU C     OXT    sing N N 109 
GLU CB    CG     sing N N 110 
GLU CB    HB2    sing N N 111 
GLU CB    HB3    sing N N 112 
GLU CG    CD     sing N N 113 
GLU CG    HG2    sing N N 114 
GLU CG    HG3    sing N N 115 
GLU CD    OE1    doub N N 116 
GLU CD    OE2    sing N N 117 
GLU OE2   HE2    sing N N 118 
GLU OXT   HXT    sing N N 119 
GLY N     CA     sing N N 120 
GLY N     H      sing N N 121 
GLY N     H2     sing N N 122 
GLY CA    C      sing N N 123 
GLY CA    HA2    sing N N 124 
GLY CA    HA3    sing N N 125 
GLY C     O      doub N N 126 
GLY C     OXT    sing N N 127 
GLY OXT   HXT    sing N N 128 
GOL C1    O1     sing N N 129 
GOL C1    C2     sing N N 130 
GOL C1    H11    sing N N 131 
GOL C1    H12    sing N N 132 
GOL O1    HO1    sing N N 133 
GOL C2    O2     sing N N 134 
GOL C2    C3     sing N N 135 
GOL C2    H2     sing N N 136 
GOL O2    HO2    sing N N 137 
GOL C3    O3     sing N N 138 
GOL C3    H31    sing N N 139 
GOL C3    H32    sing N N 140 
GOL O3    HO3    sing N N 141 
HIS N     CA     sing N N 142 
HIS N     H      sing N N 143 
HIS N     H2     sing N N 144 
HIS CA    C      sing N N 145 
HIS CA    CB     sing N N 146 
HIS CA    HA     sing N N 147 
HIS C     O      doub N N 148 
HIS C     OXT    sing N N 149 
HIS CB    CG     sing N N 150 
HIS CB    HB2    sing N N 151 
HIS CB    HB3    sing N N 152 
HIS CG    ND1    sing Y N 153 
HIS CG    CD2    doub Y N 154 
HIS ND1   CE1    doub Y N 155 
HIS ND1   HD1    sing N N 156 
HIS CD2   NE2    sing Y N 157 
HIS CD2   HD2    sing N N 158 
HIS CE1   NE2    sing Y N 159 
HIS CE1   HE1    sing N N 160 
HIS NE2   HE2    sing N N 161 
HIS OXT   HXT    sing N N 162 
HOH O     H1     sing N N 163 
HOH O     H2     sing N N 164 
ILE N     CA     sing N N 165 
ILE N     H      sing N N 166 
ILE N     H2     sing N N 167 
ILE CA    C      sing N N 168 
ILE CA    CB     sing N N 169 
ILE CA    HA     sing N N 170 
ILE C     O      doub N N 171 
ILE C     OXT    sing N N 172 
ILE CB    CG1    sing N N 173 
ILE CB    CG2    sing N N 174 
ILE CB    HB     sing N N 175 
ILE CG1   CD1    sing N N 176 
ILE CG1   HG12   sing N N 177 
ILE CG1   HG13   sing N N 178 
ILE CG2   HG21   sing N N 179 
ILE CG2   HG22   sing N N 180 
ILE CG2   HG23   sing N N 181 
ILE CD1   HD11   sing N N 182 
ILE CD1   HD12   sing N N 183 
ILE CD1   HD13   sing N N 184 
ILE OXT   HXT    sing N N 185 
LEU N     CA     sing N N 186 
LEU N     H      sing N N 187 
LEU N     H2     sing N N 188 
LEU CA    C      sing N N 189 
LEU CA    CB     sing N N 190 
LEU CA    HA     sing N N 191 
LEU C     O      doub N N 192 
LEU C     OXT    sing N N 193 
LEU CB    CG     sing N N 194 
LEU CB    HB2    sing N N 195 
LEU CB    HB3    sing N N 196 
LEU CG    CD1    sing N N 197 
LEU CG    CD2    sing N N 198 
LEU CG    HG     sing N N 199 
LEU CD1   HD11   sing N N 200 
LEU CD1   HD12   sing N N 201 
LEU CD1   HD13   sing N N 202 
LEU CD2   HD21   sing N N 203 
LEU CD2   HD22   sing N N 204 
LEU CD2   HD23   sing N N 205 
LEU OXT   HXT    sing N N 206 
LLP N1    C2     doub Y N 207 
LLP N1    C6     sing Y N 208 
LLP C2    "C2'"  sing N N 209 
LLP C2    C3     sing Y N 210 
LLP C3    O3     sing N N 211 
LLP C3    C4     doub Y N 212 
LLP C4    "C4'"  sing N N 213 
LLP C4    C5     sing Y N 214 
LLP "C4'" NZ     doub N N 215 
LLP C5    C6     doub Y N 216 
LLP C5    "C5'"  sing N N 217 
LLP "C5'" OP4    sing N N 218 
LLP OP4   P      sing N N 219 
LLP P     OP1    doub N N 220 
LLP P     OP2    sing N N 221 
LLP P     OP3    sing N N 222 
LLP N     CA     sing N N 223 
LLP CA    CB     sing N N 224 
LLP CA    C      sing N N 225 
LLP CB    CG     sing N N 226 
LLP CG    CD     sing N N 227 
LLP CD    CE     sing N N 228 
LLP CE    NZ     sing N N 229 
LLP C     O      doub N N 230 
LLP C     OXT    sing N N 231 
LLP "C2'" "H2'1" sing N N 232 
LLP "C2'" "H2'2" sing N N 233 
LLP "C2'" "H2'3" sing N N 234 
LLP O3    HO3    sing N N 235 
LLP "C4'" "H4'1" sing N N 236 
LLP C6    H6     sing N N 237 
LLP "C5'" "H5'1" sing N N 238 
LLP "C5'" "H5'2" sing N N 239 
LLP OP2   HOP2   sing N N 240 
LLP OP3   HOP3   sing N N 241 
LLP N     H      sing N N 242 
LLP N     H2     sing N N 243 
LLP CA    HA     sing N N 244 
LLP CB    HB2    sing N N 245 
LLP CB    HB3    sing N N 246 
LLP CG    HG2    sing N N 247 
LLP CG    HG3    sing N N 248 
LLP CD    HD2    sing N N 249 
LLP CD    HD3    sing N N 250 
LLP CE    HE2    sing N N 251 
LLP CE    HE3    sing N N 252 
LLP OXT   HXT    sing N N 253 
LYS N     CA     sing N N 254 
LYS N     H      sing N N 255 
LYS N     H2     sing N N 256 
LYS CA    C      sing N N 257 
LYS CA    CB     sing N N 258 
LYS CA    HA     sing N N 259 
LYS C     O      doub N N 260 
LYS C     OXT    sing N N 261 
LYS CB    CG     sing N N 262 
LYS CB    HB2    sing N N 263 
LYS CB    HB3    sing N N 264 
LYS CG    CD     sing N N 265 
LYS CG    HG2    sing N N 266 
LYS CG    HG3    sing N N 267 
LYS CD    CE     sing N N 268 
LYS CD    HD2    sing N N 269 
LYS CD    HD3    sing N N 270 
LYS CE    NZ     sing N N 271 
LYS CE    HE2    sing N N 272 
LYS CE    HE3    sing N N 273 
LYS NZ    HZ1    sing N N 274 
LYS NZ    HZ2    sing N N 275 
LYS NZ    HZ3    sing N N 276 
LYS OXT   HXT    sing N N 277 
MET N     CA     sing N N 278 
MET N     H      sing N N 279 
MET N     H2     sing N N 280 
MET CA    C      sing N N 281 
MET CA    CB     sing N N 282 
MET CA    HA     sing N N 283 
MET C     O      doub N N 284 
MET C     OXT    sing N N 285 
MET CB    CG     sing N N 286 
MET CB    HB2    sing N N 287 
MET CB    HB3    sing N N 288 
MET CG    SD     sing N N 289 
MET CG    HG2    sing N N 290 
MET CG    HG3    sing N N 291 
MET SD    CE     sing N N 292 
MET CE    HE1    sing N N 293 
MET CE    HE2    sing N N 294 
MET CE    HE3    sing N N 295 
MET OXT   HXT    sing N N 296 
PHE N     CA     sing N N 297 
PHE N     H      sing N N 298 
PHE N     H2     sing N N 299 
PHE CA    C      sing N N 300 
PHE CA    CB     sing N N 301 
PHE CA    HA     sing N N 302 
PHE C     O      doub N N 303 
PHE C     OXT    sing N N 304 
PHE CB    CG     sing N N 305 
PHE CB    HB2    sing N N 306 
PHE CB    HB3    sing N N 307 
PHE CG    CD1    doub Y N 308 
PHE CG    CD2    sing Y N 309 
PHE CD1   CE1    sing Y N 310 
PHE CD1   HD1    sing N N 311 
PHE CD2   CE2    doub Y N 312 
PHE CD2   HD2    sing N N 313 
PHE CE1   CZ     doub Y N 314 
PHE CE1   HE1    sing N N 315 
PHE CE2   CZ     sing Y N 316 
PHE CE2   HE2    sing N N 317 
PHE CZ    HZ     sing N N 318 
PHE OXT   HXT    sing N N 319 
PLP N1    C2     doub Y N 320 
PLP N1    C6     sing Y N 321 
PLP C2    C2A    sing N N 322 
PLP C2    C3     sing Y N 323 
PLP C2A   H2A1   sing N N 324 
PLP C2A   H2A2   sing N N 325 
PLP C2A   H2A3   sing N N 326 
PLP C3    O3     sing N N 327 
PLP C3    C4     doub Y N 328 
PLP O3    HO3    sing N N 329 
PLP C4    C4A    sing N N 330 
PLP C4    C5     sing Y N 331 
PLP C4A   O4A    doub N N 332 
PLP C4A   H4A    sing N N 333 
PLP C5    C6     doub Y N 334 
PLP C5    C5A    sing N N 335 
PLP C6    H6     sing N N 336 
PLP C5A   O4P    sing N N 337 
PLP C5A   H5A1   sing N N 338 
PLP C5A   H5A2   sing N N 339 
PLP O4P   P      sing N N 340 
PLP P     O1P    doub N N 341 
PLP P     O2P    sing N N 342 
PLP P     O3P    sing N N 343 
PLP O2P   HOP2   sing N N 344 
PLP O3P   HOP3   sing N N 345 
PRO N     CA     sing N N 346 
PRO N     CD     sing N N 347 
PRO N     H      sing N N 348 
PRO CA    C      sing N N 349 
PRO CA    CB     sing N N 350 
PRO CA    HA     sing N N 351 
PRO C     O      doub N N 352 
PRO C     OXT    sing N N 353 
PRO CB    CG     sing N N 354 
PRO CB    HB2    sing N N 355 
PRO CB    HB3    sing N N 356 
PRO CG    CD     sing N N 357 
PRO CG    HG2    sing N N 358 
PRO CG    HG3    sing N N 359 
PRO CD    HD2    sing N N 360 
PRO CD    HD3    sing N N 361 
PRO OXT   HXT    sing N N 362 
SER N     CA     sing N N 363 
SER N     H      sing N N 364 
SER N     H2     sing N N 365 
SER CA    C      sing N N 366 
SER CA    CB     sing N N 367 
SER CA    HA     sing N N 368 
SER C     O      doub N N 369 
SER C     OXT    sing N N 370 
SER CB    OG     sing N N 371 
SER CB    HB2    sing N N 372 
SER CB    HB3    sing N N 373 
SER OG    HG     sing N N 374 
SER OXT   HXT    sing N N 375 
THR N     CA     sing N N 376 
THR N     H      sing N N 377 
THR N     H2     sing N N 378 
THR CA    C      sing N N 379 
THR CA    CB     sing N N 380 
THR CA    HA     sing N N 381 
THR C     O      doub N N 382 
THR C     OXT    sing N N 383 
THR CB    OG1    sing N N 384 
THR CB    CG2    sing N N 385 
THR CB    HB     sing N N 386 
THR OG1   HG1    sing N N 387 
THR CG2   HG21   sing N N 388 
THR CG2   HG22   sing N N 389 
THR CG2   HG23   sing N N 390 
THR OXT   HXT    sing N N 391 
TRP N     CA     sing N N 392 
TRP N     H      sing N N 393 
TRP N     H2     sing N N 394 
TRP CA    C      sing N N 395 
TRP CA    CB     sing N N 396 
TRP CA    HA     sing N N 397 
TRP C     O      doub N N 398 
TRP C     OXT    sing N N 399 
TRP CB    CG     sing N N 400 
TRP CB    HB2    sing N N 401 
TRP CB    HB3    sing N N 402 
TRP CG    CD1    doub Y N 403 
TRP CG    CD2    sing Y N 404 
TRP CD1   NE1    sing Y N 405 
TRP CD1   HD1    sing N N 406 
TRP CD2   CE2    doub Y N 407 
TRP CD2   CE3    sing Y N 408 
TRP NE1   CE2    sing Y N 409 
TRP NE1   HE1    sing N N 410 
TRP CE2   CZ2    sing Y N 411 
TRP CE3   CZ3    doub Y N 412 
TRP CE3   HE3    sing N N 413 
TRP CZ2   CH2    doub Y N 414 
TRP CZ2   HZ2    sing N N 415 
TRP CZ3   CH2    sing Y N 416 
TRP CZ3   HZ3    sing N N 417 
TRP CH2   HH2    sing N N 418 
TRP OXT   HXT    sing N N 419 
TYR N     CA     sing N N 420 
TYR N     H      sing N N 421 
TYR N     H2     sing N N 422 
TYR CA    C      sing N N 423 
TYR CA    CB     sing N N 424 
TYR CA    HA     sing N N 425 
TYR C     O      doub N N 426 
TYR C     OXT    sing N N 427 
TYR CB    CG     sing N N 428 
TYR CB    HB2    sing N N 429 
TYR CB    HB3    sing N N 430 
TYR CG    CD1    doub Y N 431 
TYR CG    CD2    sing Y N 432 
TYR CD1   CE1    sing Y N 433 
TYR CD1   HD1    sing N N 434 
TYR CD2   CE2    doub Y N 435 
TYR CD2   HD2    sing N N 436 
TYR CE1   CZ     doub Y N 437 
TYR CE1   HE1    sing N N 438 
TYR CE2   CZ     sing Y N 439 
TYR CE2   HE2    sing N N 440 
TYR CZ    OH     sing N N 441 
TYR OH    HH     sing N N 442 
TYR OXT   HXT    sing N N 443 
VAL N     CA     sing N N 444 
VAL N     H      sing N N 445 
VAL N     H2     sing N N 446 
VAL CA    C      sing N N 447 
VAL CA    CB     sing N N 448 
VAL CA    HA     sing N N 449 
VAL C     O      doub N N 450 
VAL C     OXT    sing N N 451 
VAL CB    CG1    sing N N 452 
VAL CB    CG2    sing N N 453 
VAL CB    HB     sing N N 454 
VAL CG1   HG11   sing N N 455 
VAL CG1   HG12   sing N N 456 
VAL CG1   HG13   sing N N 457 
VAL CG2   HG21   sing N N 458 
VAL CG2   HG22   sing N N 459 
VAL CG2   HG23   sing N N 460 
VAL OXT   HXT    sing N N 461 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                Norway 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_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   5KR6 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9CF4 
_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]   0.012138 
_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]   0.010627 
_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]   0.004546 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
H 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N N      . SER A 1 2   ? -18.054 1.851   -39.776 1.00 39.41  ?  2    SER A N      1 
ATOM   2     C CA     . SER A 1 2   ? -17.159 2.505   -38.837 1.00 37.90  ?  2    SER A CA     1 
ATOM   3     C C      . SER A 1 2   ? -15.701 2.167   -39.099 1.00 34.62  ?  2    SER A C      1 
ATOM   4     O O      . SER A 1 2   ? -15.384 1.196   -39.806 1.00 33.55  ?  2    SER A O      1 
ATOM   5     C CB     . SER A 1 2   ? -17.492 2.068   -37.404 1.00 38.82  ?  2    SER A CB     1 
ATOM   6     O OG     . SER A 1 2   ? -17.268 0.671   -37.247 1.00 37.62  ?  2    SER A OG     1 
ATOM   7     H HA     . SER A 1 2   ? -17.278 3.463   -38.936 1.00 45.48  ?  2    SER A HA     1 
ATOM   8     H HB2    . SER A 1 2   ? -16.923 2.552   -36.784 1.00 46.58  ?  2    SER A HB2    1 
ATOM   9     H HB3    . SER A 1 2   ? -18.424 2.263   -37.220 1.00 46.58  ?  2    SER A HB3    1 
ATOM   10    H HG     . SER A 1 2   ? -17.756 0.240   -37.778 1.00 45.14  ?  2    SER A HG     1 
ATOM   11    N N      . GLN A 1 3   ? -14.814 2.977   -38.513 1.00 34.19  ?  3    GLN A N      1 
ATOM   12    C CA     . GLN A 1 3   ? -13.397 2.636   -38.505 1.00 34.63  ?  3    GLN A CA     1 
ATOM   13    C C      . GLN A 1 3   ? -13.178 1.273   -37.864 1.00 27.45  ?  3    GLN A C      1 
ATOM   14    O O      . GLN A 1 3   ? -12.338 0.497   -38.317 1.00 25.77  ?  3    GLN A O      1 
ATOM   15    C CB     . GLN A 1 3   ? -12.602 3.687   -37.737 1.00 39.68  ?  3    GLN A CB     1 
ATOM   16    C CG     . GLN A 1 3   ? -12.275 4.943   -38.526 1.00 46.00  ?  3    GLN A CG     1 
ATOM   17    C CD     . GLN A 1 3   ? -11.491 5.946   -37.692 1.00 51.90  ?  3    GLN A CD     1 
ATOM   18    O OE1    . GLN A 1 3   ? -11.123 5.670   -36.549 1.00 53.85  ?  3    GLN A OE1    1 
ATOM   19    N NE2    . GLN A 1 3   ? -11.236 7.122   -38.265 1.00 54.61  ?  3    GLN A NE2    1 
ATOM   20    H H      . GLN A 1 3   ? -15.004 3.718   -38.119 1.00 41.02  ?  3    GLN A H      1 
ATOM   21    H HA     . GLN A 1 3   ? -13.079 2.618   -39.421 1.00 41.55  ?  3    GLN A HA     1 
ATOM   22    H HB2    . GLN A 1 3   ? -13.118 3.956   -36.961 1.00 47.61  ?  3    GLN A HB2    1 
ATOM   23    H HB3    . GLN A 1 3   ? -11.762 3.291   -37.457 1.00 47.61  ?  3    GLN A HB3    1 
ATOM   24    H HG2    . GLN A 1 3   ? -11.738 4.705   -39.298 1.00 55.20  ?  3    GLN A HG2    1 
ATOM   25    H HG3    . GLN A 1 3   ? -13.100 5.365   -38.812 1.00 55.20  ?  3    GLN A HG3    1 
ATOM   26    H HE21   . GLN A 1 3   ? -11.512 7.280   -39.064 1.00 65.53  ?  3    GLN A HE21   1 
ATOM   27    H HE22   . GLN A 1 3   ? -10.796 7.724   -37.836 1.00 65.53  ?  3    GLN A HE22   1 
ATOM   28    N N      . HIS A 1 4   ? -13.911 0.977   -36.790 1.00 25.21  ?  4    HIS A N      1 
ATOM   29    C CA     . HIS A 1 4   ? -13.781 -0.320  -36.134 1.00 23.02  ?  4    HIS A CA     1 
ATOM   30    C C      . HIS A 1 4   ? -14.060 -1.461  -37.112 1.00 22.39  ?  4    HIS A C      1 
ATOM   31    O O      . HIS A 1 4   ? -13.267 -2.407  -37.234 1.00 20.96  ?  4    HIS A O      1 
ATOM   32    C CB     . HIS A 1 4   ? -14.735 -0.382  -34.948 1.00 23.48  ?  4    HIS A CB     1 
ATOM   33    C CG     . HIS A 1 4   ? -14.484 -1.538  -34.026 1.00 20.87  ?  4    HIS A CG     1 
ATOM   34    N ND1    . HIS A 1 4   ? -15.250 -1.768  -32.903 1.00 20.06  ?  4    HIS A ND1    1 
ATOM   35    C CD2    . HIS A 1 4   ? -13.546 -2.511  -34.047 1.00 20.18  ?  4    HIS A CD2    1 
ATOM   36    C CE1    . HIS A 1 4   ? -14.789 -2.835  -32.273 1.00 18.30  ?  4    HIS A CE1    1 
ATOM   37    N NE2    . HIS A 1 4   ? -13.758 -3.302  -32.949 1.00 18.62  ?  4    HIS A NE2    1 
ATOM   38    H H      . HIS A 1 4   ? -14.485 1.503   -36.425 1.00 30.25  ?  4    HIS A H      1 
ATOM   39    H HA     . HIS A 1 4   ? -12.874 -0.425  -35.807 1.00 27.62  ?  4    HIS A HA     1 
ATOM   40    H HB2    . HIS A 1 4   ? -14.642 0.434   -34.431 1.00 28.17  ?  4    HIS A HB2    1 
ATOM   41    H HB3    . HIS A 1 4   ? -15.643 -0.461  -35.281 1.00 28.17  ?  4    HIS A HB3    1 
ATOM   42    H HD1    . HIS A 1 4   ? -15.921 -1.292  -32.652 1.00 24.06  ?  4    HIS A HD1    1 
ATOM   43    H HD2    . HIS A 1 4   ? -12.881 -2.623  -34.688 1.00 24.22  ?  4    HIS A HD2    1 
ATOM   44    H HE1    . HIS A 1 4   ? -15.133 -3.194  -31.488 1.00 21.95  ?  4    HIS A HE1    1 
ATOM   45    N N      . GLN A 1 5   ? -15.182 -1.393  -37.831 1.00 24.30  ?  5    GLN A N      1 
ATOM   46    C CA     . GLN A 1 5   ? -15.499 -2.489  -38.741 1.00 26.02  ?  5    GLN A CA     1 
ATOM   47    C C      . GLN A 1 5   ? -14.559 -2.497  -39.944 1.00 24.15  ?  5    GLN A C      1 
ATOM   48    O O      . GLN A 1 5   ? -14.253 -3.574  -40.474 1.00 23.44  ?  5    GLN A O      1 
ATOM   49    C CB     . GLN A 1 5   ? -16.967 -2.449  -39.165 1.00 29.77  ?  5    GLN A CB     1 
ATOM   50    C CG     . GLN A 1 5   ? -17.980 -2.705  -38.030 1.00 34.30  ?  5    GLN A CG     1 
ATOM   51    C CD     . GLN A 1 5   ? -17.683 -3.949  -37.169 1.00 37.80  ?  5    GLN A CD     1 
ATOM   52    O OE1    . GLN A 1 5   ? -17.422 -5.045  -37.681 1.00 37.40  ?  5    GLN A OE1    1 
ATOM   53    N NE2    . GLN A 1 5   ? -17.735 -3.773  -35.847 1.00 39.24  ?  5    GLN A NE2    1 
ATOM   54    H H      . GLN A 1 5   ? -15.753 -0.750  -37.812 1.00 29.16  ?  5    GLN A H      1 
ATOM   55    H HA     . GLN A 1 5   ? -15.381 -3.330  -38.272 1.00 31.22  ?  5    GLN A HA     1 
ATOM   56    H HB2    . GLN A 1 5   ? -17.157 -1.571  -39.531 1.00 35.72  ?  5    GLN A HB2    1 
ATOM   57    H HB3    . GLN A 1 5   ? -17.110 -3.128  -39.842 1.00 35.72  ?  5    GLN A HB3    1 
ATOM   58    H HG2    . GLN A 1 5   ? -17.982 -1.936  -37.440 1.00 41.16  ?  5    GLN A HG2    1 
ATOM   59    H HG3    . GLN A 1 5   ? -18.858 -2.826  -38.423 1.00 41.16  ?  5    GLN A HG3    1 
ATOM   60    H HE21   . GLN A 1 5   ? -17.925 -2.999  -35.523 1.00 47.08  ?  5    GLN A HE21   1 
ATOM   61    H HE22   . GLN A 1 5   ? -17.578 -4.433  -35.319 1.00 47.08  ?  5    GLN A HE22   1 
ATOM   62    N N      . ASN A 1 6   ? -14.077 -1.320  -40.379 1.00 25.38  ?  6    ASN A N      1 
ATOM   63    C CA     . ASN A 1 6   ? -13.076 -1.289  -41.444 1.00 23.33  ?  6    ASN A CA     1 
ATOM   64    C C      . ASN A 1 6   ? -11.792 -1.998  -41.017 1.00 20.90  ?  6    ASN A C      1 
ATOM   65    O O      . ASN A 1 6   ? -11.182 -2.722  -41.814 1.00 21.08  ?  6    ASN A O      1 
ATOM   66    C CB     . ASN A 1 6   ? -12.750 0.150   -41.855 1.00 27.38  ?  6    ASN A CB     1 
ATOM   67    C CG     . ASN A 1 6   ? -13.913 0.844   -42.541 1.00 33.07  ?  6    ASN A CG     1 
ATOM   68    O OD1    . ASN A 1 6   ? -14.920 0.213   -42.880 1.00 35.24  ?  6    ASN A OD1    1 
ATOM   69    N ND2    . ASN A 1 6   ? -13.773 2.148   -42.774 1.00 35.45  ?  6    ASN A ND2    1 
ATOM   70    H H      . ASN A 1 6   ? -14.309 -0.547  -40.080 1.00 30.45  ?  6    ASN A H      1 
ATOM   71    H HA     . ASN A 1 6   ? -13.451 -1.745  -42.214 1.00 27.99  ?  6    ASN A HA     1 
ATOM   72    H HB2    . ASN A 1 6   ? -12.521 0.661   -41.063 1.00 32.85  ?  6    ASN A HB2    1 
ATOM   73    H HB3    . ASN A 1 6   ? -12.002 0.141   -42.472 1.00 32.85  ?  6    ASN A HB3    1 
ATOM   74    H HD21   . ASN A 1 6   ? -14.404 2.586   -43.160 1.00 42.53  ?  6    ASN A HD21   1 
ATOM   75    H HD22   . ASN A 1 6   ? -13.051 2.551   -42.539 1.00 42.53  ?  6    ASN A HD22   1 
ATOM   76    N N      . LEU A 1 7   ? -11.358 -1.787  -39.768 1.00 19.64  ?  7    LEU A N      1 
ATOM   77    C CA     . LEU A 1 7   ? -10.165 -2.471  -39.270 1.00 18.45  ?  7    LEU A CA     1 
ATOM   78    C C      . LEU A 1 7   ? -10.379 -3.982  -39.194 1.00 18.62  ?  7    LEU A C      1 
ATOM   79    O O      . LEU A 1 7   ? -9.518  -4.774  -39.601 1.00 17.25  ?  7    LEU A O      1 
ATOM   80    C CB     . LEU A 1 7   ? -9.753  -1.921  -37.909 1.00 19.33  ?  7    LEU A CB     1 
ATOM   81    C CG     . LEU A 1 7   ? -8.996  -0.598  -37.894 1.00 24.06  ?  7    LEU A CG     1 
ATOM   82    C CD1    . LEU A 1 7   ? -8.936  -0.049  -36.480 1.00 26.51  ?  7    LEU A CD1    1 
ATOM   83    C CD2    . LEU A 1 7   ? -7.590  -0.780  -38.475 1.00 27.12  ?  7    LEU A CD2    1 
ATOM   84    H H      . LEU A 1 7   ? -11.730 -1.261  -39.199 1.00 23.57  ?  7    LEU A H      1 
ATOM   85    H HA     . LEU A 1 7   ? -9.440  -2.297  -39.890 1.00 22.14  ?  7    LEU A HA     1 
ATOM   86    H HB2    . LEU A 1 7   ? -10.558 -1.792  -37.384 1.00 23.20  ?  7    LEU A HB2    1 
ATOM   87    H HB3    . LEU A 1 7   ? -9.181  -2.579  -37.483 1.00 23.20  ?  7    LEU A HB3    1 
ATOM   88    H HG     . LEU A 1 7   ? -9.460  0.049   -38.448 1.00 28.87  ?  7    LEU A HG     1 
ATOM   89    H HD11   . LEU A 1 7   ? -8.447  0.788   -36.487 1.00 31.81  ?  7    LEU A HD11   1 
ATOM   90    H HD12   . LEU A 1 7   ? -9.839  0.097   -36.160 1.00 31.81  ?  7    LEU A HD12   1 
ATOM   91    H HD13   . LEU A 1 7   ? -8.483  -0.692  -35.911 1.00 31.81  ?  7    LEU A HD13   1 
ATOM   92    H HD21   . LEU A 1 7   ? -7.080  0.032   -38.328 1.00 32.54  ?  7    LEU A HD21   1 
ATOM   93    H HD22   . LEU A 1 7   ? -7.159  -1.527  -38.030 1.00 32.54  ?  7    LEU A HD22   1 
ATOM   94    H HD23   . LEU A 1 7   ? -7.662  -0.958  -39.426 1.00 32.54  ?  7    LEU A HD23   1 
ATOM   95    N N      . ILE A 1 8   ? -11.526 -4.411  -38.663 1.00 16.79  ?  8    ILE A N      1 
ATOM   96    C CA     . ILE A 1 8   ? -11.840 -5.837  -38.631 1.00 16.19  ?  8    ILE A CA     1 
ATOM   97    C C      . ILE A 1 8   ? -11.785 -6.415  -40.037 1.00 17.78  ?  8    ILE A C      1 
ATOM   98    O O      . ILE A 1 8   ? -11.192 -7.477  -40.272 1.00 18.00  ?  8    ILE A O      1 
ATOM   99    C CB     . ILE A 1 8   ? -13.203 -6.076  -37.961 1.00 16.59  ?  8    ILE A CB     1 
ATOM   100   C CG1    . ILE A 1 8   ? -13.139 -5.697  -36.479 1.00 17.62  ?  8    ILE A CG1    1 
ATOM   101   C CG2    . ILE A 1 8   ? -13.598 -7.525  -38.072 1.00 20.37  ?  8    ILE A CG2    1 
ATOM   102   C CD1    . ILE A 1 8   ? -14.485 -5.582  -35.803 1.00 21.22  ?  8    ILE A CD1    1 
ATOM   103   H H      . ILE A 1 8   ? -12.130 -3.904  -38.319 1.00 20.14  ?  8    ILE A H      1 
ATOM   104   H HA     . ILE A 1 8   ? -11.171 -6.292  -38.097 1.00 19.43  ?  8    ILE A HA     1 
ATOM   105   H HB     . ILE A 1 8   ? -13.858 -5.523  -38.414 1.00 19.90  ?  8    ILE A HB     1 
ATOM   106   H HG12   . ILE A 1 8   ? -12.631 -6.376  -36.008 1.00 21.14  ?  8    ILE A HG12   1 
ATOM   107   H HG13   . ILE A 1 8   ? -12.696 -4.837  -36.399 1.00 21.14  ?  8    ILE A HG13   1 
ATOM   108   H HG21   . ILE A 1 8   ? -14.339 -7.697  -37.470 1.00 24.44  ?  8    ILE A HG21   1 
ATOM   109   H HG22   . ILE A 1 8   ? -13.863 -7.711  -38.986 1.00 24.44  ?  8    ILE A HG22   1 
ATOM   110   H HG23   . ILE A 1 8   ? -12.839 -8.079  -37.829 1.00 24.44  ?  8    ILE A HG23   1 
ATOM   111   H HD11   . ILE A 1 8   ? -14.367 -5.175  -34.930 1.00 25.46  ?  8    ILE A HD11   1 
ATOM   112   H HD12   . ILE A 1 8   ? -15.067 -5.030  -36.349 1.00 25.46  ?  8    ILE A HD12   1 
ATOM   113   H HD13   . ILE A 1 8   ? -14.866 -6.469  -35.706 1.00 25.46  ?  8    ILE A HD13   1 
ATOM   114   N N      . ASP A 1 9   ? -12.406 -5.726  -41.001 1.00 17.38  ?  9    ASP A N      1 
ATOM   115   C CA     . ASP A 1 9   ? -12.453 -6.278  -42.353 1.00 18.83  ?  9    ASP A CA     1 
ATOM   116   C C      . ASP A 1 9   ? -11.059 -6.367  -42.966 1.00 17.56  ?  9    ASP A C      1 
ATOM   117   O O      . ASP A 1 9   ? -10.784 -7.287  -43.747 1.00 19.21  ?  9    ASP A O      1 
ATOM   118   C CB     . ASP A 1 9   ? -13.433 -5.485  -43.216 1.00 20.88  ?  9    ASP A CB     1 
ATOM   119   C CG     . ASP A 1 9   ? -14.888 -5.731  -42.827 1.00 24.13  ?  9    ASP A CG     1 
ATOM   120   O OD1    . ASP A 1 9   ? -15.196 -6.691  -42.059 1.00 23.53  ?  9    ASP A OD1    1 
ATOM   121   O OD2    . ASP A 1 9   ? -15.737 -4.956  -43.295 1.00 26.55  -1 9    ASP A OD2    1 
ATOM   122   H H      . ASP A 1 9   ? -12.793 -4.965  -40.902 1.00 20.85  ?  9    ASP A H      1 
ATOM   123   H HA     . ASP A 1 9   ? -12.798 -7.184  -42.324 1.00 22.60  ?  9    ASP A HA     1 
ATOM   124   H HB2    . ASP A 1 9   ? -13.250 -4.537  -43.113 1.00 25.05  ?  9    ASP A HB2    1 
ATOM   125   H HB3    . ASP A 1 9   ? -13.321 -5.746  -44.143 1.00 25.05  ?  9    ASP A HB3    1 
ATOM   126   N N      . ARG A 1 10  ? -10.171 -5.425  -42.635 1.00 16.09  ?  10   ARG A N      1 
ATOM   127   C CA     . ARG A 1 10  ? -8.778  -5.559  -43.048 1.00 16.53  ?  10   ARG A CA     1 
ATOM   128   C C      . ARG A 1 10  ? -8.155  -6.805  -42.418 1.00 16.97  ?  10   ARG A C      1 
ATOM   129   O O      . ARG A 1 10  ? -7.465  -7.582  -43.093 1.00 16.35  ?  10   ARG A O      1 
ATOM   130   C CB     . ARG A 1 10  ? -7.992  -4.317  -42.641 1.00 16.77  ?  10   ARG A CB     1 
ATOM   131   C CG     . ARG A 1 10  ? -8.202  -3.125  -43.582 1.00 17.39  ?  10   ARG A CG     1 
ATOM   132   C CD     . ARG A 1 10  ? -7.715  -1.817  -42.983 1.00 18.69  ?  10   ARG A CD     1 
ATOM   133   N NE     . ARG A 1 10  ? -6.280  -1.847  -42.714 1.00 20.06  ?  10   ARG A NE     1 
ATOM   134   C CZ     . ARG A 1 10  ? -5.622  -0.907  -42.050 1.00 21.33  ?  10   ARG A CZ     1 
ATOM   135   N NH1    . ARG A 1 10  ? -6.272  0.154   -41.576 1.00 22.21  ?  10   ARG A NH1    1 
ATOM   136   N NH2    . ARG A 1 10  ? -4.321  -1.025  -41.843 1.00 22.27  ?  10   ARG A NH2    1 
ATOM   137   H H      . ARG A 1 10  ? -10.346 -4.715  -42.182 1.00 19.31  ?  10   ARG A H      1 
ATOM   138   H HA     . ARG A 1 10  ? -8.739  -5.642  -44.013 1.00 19.84  ?  10   ARG A HA     1 
ATOM   139   H HB2    . ARG A 1 10  ? -8.273  -4.047  -41.752 1.00 20.12  ?  10   ARG A HB2    1 
ATOM   140   H HB3    . ARG A 1 10  ? -7.046  -4.531  -42.640 1.00 20.12  ?  10   ARG A HB3    1 
ATOM   141   H HG2    . ARG A 1 10  ? -7.712  -3.280  -44.404 1.00 20.86  ?  10   ARG A HG2    1 
ATOM   142   H HG3    . ARG A 1 10  ? -9.149  -3.034  -43.772 1.00 20.86  ?  10   ARG A HG3    1 
ATOM   143   H HD2    . ARG A 1 10  ? -7.892  -1.094  -43.606 1.00 22.43  ?  10   ARG A HD2    1 
ATOM   144   H HD3    . ARG A 1 10  ? -8.178  -1.655  -42.147 1.00 22.43  ?  10   ARG A HD3    1 
ATOM   145   H HE     . ARG A 1 10  ? -5.831  -2.521  -43.005 1.00 24.07  ?  10   ARG A HE     1 
ATOM   146   H HH11   . ARG A 1 10  ? -7.119  0.230   -41.701 1.00 26.65  ?  10   ARG A HH11   1 
ATOM   147   H HH12   . ARG A 1 10  ? -5.844  0.763   -41.146 1.00 26.65  ?  10   ARG A HH12   1 
ATOM   148   H HH21   . ARG A 1 10  ? -3.899  -1.713  -42.139 1.00 26.72  ?  10   ARG A HH21   1 
ATOM   149   H HH22   . ARG A 1 10  ? -3.897  -0.414  -41.412 1.00 26.72  ?  10   ARG A HH22   1 
ATOM   150   N N      . ASP A 1 11  ? -8.404  -7.012  -41.120 1.00 16.26  ?  11   ASP A N      1 
ATOM   151   C CA     . ASP A 1 11  ? -7.826  -8.147  -40.402 1.00 13.95  ?  11   ASP A CA     1 
ATOM   152   C C      . ASP A 1 11  ? -8.311  -9.469  -40.985 1.00 13.97  ?  11   ASP A C      1 
ATOM   153   O O      . ASP A 1 11  ? -7.560  -10.453 -41.034 1.00 15.38  ?  11   ASP A O      1 
ATOM   154   C CB     . ASP A 1 11  ? -8.212  -8.014  -38.928 1.00 16.60  ?  11   ASP A CB     1 
ATOM   155   C CG     . ASP A 1 11  ? -7.451  -8.965  -38.029 1.00 16.99  ?  11   ASP A CG     1 
ATOM   156   O OD1    . ASP A 1 11  ? -6.219  -9.076  -38.170 1.00 17.05  ?  11   ASP A OD1    1 
ATOM   157   O OD2    . ASP A 1 11  ? -8.090  -9.578  -37.151 1.00 17.24  -1 11   ASP A OD2    1 
ATOM   158   H H      . ASP A 1 11  ? -8.904  -6.510  -40.631 1.00 19.50  ?  11   ASP A H      1 
ATOM   159   H HA     . ASP A 1 11  ? -6.859  -8.143  -40.478 1.00 16.74  ?  11   ASP A HA     1 
ATOM   160   H HB2    . ASP A 1 11  ? -8.024  -7.109  -38.633 1.00 19.92  ?  11   ASP A HB2    1 
ATOM   161   H HB3    . ASP A 1 11  ? -9.158  -8.205  -38.832 1.00 19.92  ?  11   ASP A HB3    1 
ATOM   162   N N      . ARG A 1 12  ? -9.564  -9.521  -41.423 1.00 15.12  ?  12   ARG A N      1 
ATOM   163   C CA     . ARG A 1 12  ? -10.069 -10.771 -41.978 1.00 15.83  ?  12   ARG A CA     1 
ATOM   164   C C      . ARG A 1 12  ? -9.238  -11.253 -43.159 1.00 16.20  ?  12   ARG A C      1 
ATOM   165   O O      . ARG A 1 12  ? -9.175  -12.466 -43.430 1.00 16.24  ?  12   ARG A O      1 
ATOM   166   C CB     . ARG A 1 12  ? -11.508 -10.591 -42.464 1.00 15.38  ?  12   ARG A CB     1 
ATOM   167   C CG     . ARG A 1 12  ? -12.529 -10.251 -41.408 1.00 17.30  ?  12   ARG A CG     1 
ATOM   168   C CD     . ARG A 1 12  ? -13.925 -10.164 -42.041 1.00 17.94  ?  12   ARG A CD     1 
ATOM   169   N NE     . ARG A 1 12  ? -14.887 -9.569  -41.135 1.00 18.47  ?  12   ARG A NE     1 
ATOM   170   C CZ     . ARG A 1 12  ? -15.485 -10.228 -40.149 1.00 18.21  ?  12   ARG A CZ     1 
ATOM   171   N NH1    . ARG A 1 12  ? -15.222 -11.511 -39.980 1.00 17.95  ?  12   ARG A NH1    1 
ATOM   172   N NH2    . ARG A 1 12  ? -16.347 -9.606  -39.353 1.00 20.10  ?  12   ARG A NH2    1 
ATOM   173   H H      . ARG A 1 12  ? -10.127 -8.871  -41.412 1.00 18.14  ?  12   ARG A H      1 
ATOM   174   H HA     . ARG A 1 12  ? -10.039 -11.434 -41.271 1.00 19.00  ?  12   ARG A HA     1 
ATOM   175   H HB2    . ARG A 1 12  ? -11.520 -9.871  -43.115 1.00 18.45  ?  12   ARG A HB2    1 
ATOM   176   H HB3    . ARG A 1 12  ? -11.792 -11.419 -42.881 1.00 18.45  ?  12   ARG A HB3    1 
ATOM   177   H HG2    . ARG A 1 12  ? -12.538 -10.941 -40.727 1.00 20.76  ?  12   ARG A HG2    1 
ATOM   178   H HG3    . ARG A 1 12  ? -12.314 -9.393  -41.009 1.00 20.76  ?  12   ARG A HG3    1 
ATOM   179   H HD2    . ARG A 1 12  ? -13.881 -9.617  -42.841 1.00 21.52  ?  12   ARG A HD2    1 
ATOM   180   H HD3    . ARG A 1 12  ? -14.230 -11.057 -42.267 1.00 21.52  ?  12   ARG A HD3    1 
ATOM   181   H HE     . ARG A 1 12  ? -15.083 -8.739  -41.243 1.00 22.16  ?  12   ARG A HE     1 
ATOM   182   H HH11   . ARG A 1 12  ? -14.670 -11.910 -40.505 1.00 21.54  ?  12   ARG A HH11   1 
ATOM   183   H HH12   . ARG A 1 12  ? -15.603 -11.948 -39.344 1.00 21.54  ?  12   ARG A HH12   1 
ATOM   184   H HH21   . ARG A 1 12  ? -16.521 -8.773  -39.475 1.00 24.11  ?  12   ARG A HH21   1 
ATOM   185   H HH22   . ARG A 1 12  ? -16.731 -10.037 -38.716 1.00 24.11  ?  12   ARG A HH22   1 
ATOM   186   N N      . LYS A 1 13  ? -8.653  -10.321 -43.914 1.00 16.98  ?  13   LYS A N      1 
ATOM   187   C CA     . LYS A 1 13  ? -7.895  -10.683 -45.097 1.00 16.18  ?  13   LYS A CA     1 
ATOM   188   C C      . LYS A 1 13  ? -6.479  -11.157 -44.802 1.00 16.01  ?  13   LYS A C      1 
ATOM   189   O O      . LYS A 1 13  ? -5.840  -11.724 -45.699 1.00 16.21  ?  13   LYS A O      1 
ATOM   190   C CB     . LYS A 1 13  ? -7.799  -9.487  -46.023 1.00 18.28  ?  13   LYS A CB     1 
ATOM   191   C CG     . LYS A 1 13  ? -9.125  -9.071  -46.563 1.00 21.91  ?  13   LYS A CG     1 
ATOM   192   C CD     . LYS A 1 13  ? -8.969  -7.892  -47.466 1.00 27.87  ?  13   LYS A CD     1 
ATOM   193   C CE     . LYS A 1 13  ? -10.327 -7.472  -47.951 1.00 34.85  ?  13   LYS A CE     1 
ATOM   194   N NZ     . LYS A 1 13  ? -10.954 -8.524  -48.747 1.00 41.47  ?  13   LYS A NZ     1 
ATOM   195   H H      . LYS A 1 13  ? -8.685  -9.476  -43.758 1.00 20.38  ?  13   LYS A H      1 
ATOM   196   H HA     . LYS A 1 13  ? -8.368  -11.405 -45.539 1.00 19.41  ?  13   LYS A HA     1 
ATOM   197   H HB2    . LYS A 1 13  ? -7.425  -8.738  -45.534 1.00 21.93  ?  13   LYS A HB2    1 
ATOM   198   H HB3    . LYS A 1 13  ? -7.226  -9.713  -46.772 1.00 21.93  ?  13   LYS A HB3    1 
ATOM   199   H HG2    . LYS A 1 13  ? -9.513  -9.801  -47.070 1.00 26.28  ?  13   LYS A HG2    1 
ATOM   200   H HG3    . LYS A 1 13  ? -9.712  -8.826  -45.832 1.00 26.28  ?  13   LYS A HG3    1 
ATOM   201   H HD2    . LYS A 1 13  ? -8.564  -7.155  -46.983 1.00 33.44  ?  13   LYS A HD2    1 
ATOM   202   H HD3    . LYS A 1 13  ? -8.420  -8.129  -48.230 1.00 33.44  ?  13   LYS A HD3    1 
ATOM   203   H HE2    . LYS A 1 13  ? -10.897 -7.284  -47.189 1.00 41.82  ?  13   LYS A HE2    1 
ATOM   204   H HE3    . LYS A 1 13  ? -10.241 -6.680  -48.504 1.00 41.82  ?  13   LYS A HE3    1 
ATOM   205   H HZ1    . LYS A 1 13  ? -11.839 -8.422  -48.743 1.00 49.76  ?  13   LYS A HZ1    1 
ATOM   206   H HZ2    . LYS A 1 13  ? -10.663 -8.484  -49.587 1.00 49.76  ?  13   LYS A HZ2    1 
ATOM   207   H HZ3    . LYS A 1 13  ? -10.754 -9.322  -48.408 1.00 49.76  ?  13   LYS A HZ3    1 
ATOM   208   N N      . VAL A 1 14  ? -5.969  -10.955 -43.589 1.00 15.23  ?  14   VAL A N      1 
ATOM   209   C CA     . VAL A 1 14  ? -4.534  -11.085 -43.362 1.00 14.48  ?  14   VAL A CA     1 
ATOM   210   C C      . VAL A 1 14  ? -4.146  -11.899 -42.141 1.00 14.41  ?  14   VAL A C      1 
ATOM   211   O O      . VAL A 1 14  ? -2.993  -12.357 -42.095 1.00 14.75  ?  14   VAL A O      1 
ATOM   212   C CB     . VAL A 1 14  ? -3.827  -9.705  -43.328 1.00 14.83  ?  14   VAL A CB     1 
ATOM   213   C CG1    . VAL A 1 14  ? -3.903  -9.060  -44.703 1.00 16.31  ?  14   VAL A CG1    1 
ATOM   214   C CG2    . VAL A 1 14  ? -4.430  -8.777  -42.249 1.00 13.93  ?  14   VAL A CG2    1 
ATOM   215   H H      . VAL A 1 14  ? -6.427  -10.746 -42.892 1.00 18.27  ?  14   VAL A H      1 
ATOM   216   H HA     . VAL A 1 14  ? -4.185  -11.568 -44.128 1.00 17.37  ?  14   VAL A HA     1 
ATOM   217   H HB     . VAL A 1 14  ? -2.896  -9.838  -43.091 1.00 17.79  ?  14   VAL A HB     1 
ATOM   218   H HG11   . VAL A 1 14  ? -3.351  -8.262  -44.709 1.00 19.56  ?  14   VAL A HG11   1 
ATOM   219   H HG12   . VAL A 1 14  ? -3.579  -9.690  -45.366 1.00 19.56  ?  14   VAL A HG12   1 
ATOM   220   H HG13   . VAL A 1 14  ? -4.825  -8.825  -44.892 1.00 19.56  ?  14   VAL A HG13   1 
ATOM   221   H HG21   . VAL A 1 14  ? -3.943  -7.938  -42.246 1.00 16.71  ?  14   VAL A HG21   1 
ATOM   222   H HG22   . VAL A 1 14  ? -5.364  -8.617  -42.456 1.00 16.71  ?  14   VAL A HG22   1 
ATOM   223   H HG23   . VAL A 1 14  ? -4.352  -9.207  -41.383 1.00 16.71  ?  14   VAL A HG23   1 
ATOM   224   N N      . THR A 1 15  ? -4.982  -12.083 -41.113 1.00 13.14  ?  15   THR A N      1 
ATOM   225   C CA     . THR A 1 15  ? -4.524  -12.681 -39.864 1.00 13.32  ?  15   THR A CA     1 
ATOM   226   C C      . THR A 1 15  ? -5.234  -13.994 -39.559 1.00 15.04  ?  15   THR A C      1 
ATOM   227   O O      . THR A 1 15  ? -6.466  -14.074 -39.610 1.00 15.82  ?  15   THR A O      1 
ATOM   228   C CB     . THR A 1 15  ? -4.703  -11.706 -38.682 1.00 14.44  ?  15   THR A CB     1 
ATOM   229   O OG1    . THR A 1 15  ? -4.025  -10.472 -38.954 1.00 14.95  ?  15   THR A OG1    1 
ATOM   230   C CG2    . THR A 1 15  ? -4.159  -12.339 -37.400 1.00 17.00  ?  15   THR A CG2    1 
ATOM   231   H H      . THR A 1 15  ? -5.814  -11.867 -41.122 1.00 15.76  ?  15   THR A H      1 
ATOM   232   H HA     . THR A 1 15  ? -3.584  -12.892 -39.975 1.00 15.98  ?  15   THR A HA     1 
ATOM   233   H HB     . THR A 1 15  ? -5.644  -11.513 -38.552 1.00 17.32  ?  15   THR A HB     1 
ATOM   234   H HG1    . THR A 1 15  ? -4.482  -9.826  -38.673 1.00 17.93  ?  15   THR A HG1    1 
ATOM   235   H HG21   . THR A 1 15  ? -4.131  -11.679 -36.690 1.00 20.40  ?  15   THR A HG21   1 
ATOM   236   H HG22   . THR A 1 15  ? -4.729  -13.074 -37.125 1.00 20.40  ?  15   THR A HG22   1 
ATOM   237   H HG23   . THR A 1 15  ? -3.262  -12.677 -37.551 1.00 20.40  ?  15   THR A HG23   1 
ATOM   238   N N      . PHE A 1 16  ? -4.442  -15.016 -39.219 1.00 13.58  ?  16   PHE A N      1 
ATOM   239   C CA     . PHE A 1 16  ? -4.901  -16.289 -38.634 1.00 12.82  ?  16   PHE A CA     1 
ATOM   240   C C      . PHE A 1 16  ? -4.860  -16.080 -37.128 1.00 13.89  ?  16   PHE A C      1 
ATOM   241   O O      . PHE A 1 16  ? -3.792  -15.919 -36.550 1.00 13.63  ?  16   PHE A O      1 
ATOM   242   C CB     . PHE A 1 16  ? -3.950  -17.383 -39.124 1.00 12.12  ?  16   PHE A CB     1 
ATOM   243   C CG     . PHE A 1 16  ? -4.047  -18.766 -38.474 1.00 12.41  ?  16   PHE A CG     1 
ATOM   244   C CD1    . PHE A 1 16  ? -4.672  -19.039 -37.270 1.00 13.59  ?  16   PHE A CD1    1 
ATOM   245   C CD2    . PHE A 1 16  ? -3.387  -19.806 -39.109 1.00 14.46  ?  16   PHE A CD2    1 
ATOM   246   C CE1    . PHE A 1 16  ? -4.621  -20.324 -36.731 1.00 16.12  ?  16   PHE A CE1    1 
ATOM   247   C CE2    . PHE A 1 16  ? -3.363  -21.089 -38.590 1.00 15.33  ?  16   PHE A CE2    1 
ATOM   248   C CZ     . PHE A 1 16  ? -3.969  -21.338 -37.405 1.00 15.56  ?  16   PHE A CZ     1 
ATOM   249   H H      . PHE A 1 16  ? -3.588  -14.998 -39.321 1.00 16.30  ?  16   PHE A H      1 
ATOM   250   H HA     . PHE A 1 16  ? -5.805  -16.544 -38.879 1.00 15.38  ?  16   PHE A HA     1 
ATOM   251   H HB2    . PHE A 1 16  ? -4.109  -17.510 -40.073 1.00 14.55  ?  16   PHE A HB2    1 
ATOM   252   H HB3    . PHE A 1 16  ? -3.043  -17.071 -38.980 1.00 14.55  ?  16   PHE A HB3    1 
ATOM   253   H HD1    . PHE A 1 16  ? -5.126  -18.364 -36.819 1.00 16.31  ?  16   PHE A HD1    1 
ATOM   254   H HD2    . PHE A 1 16  ? -2.945  -19.636 -39.910 1.00 17.35  ?  16   PHE A HD2    1 
ATOM   255   H HE1    . PHE A 1 16  ? -5.029  -20.500 -35.914 1.00 19.33  ?  16   PHE A HE1    1 
ATOM   256   H HE2    . PHE A 1 16  ? -2.935  -21.773 -39.051 1.00 18.39  ?  16   PHE A HE2    1 
ATOM   257   H HZ     . PHE A 1 16  ? -3.946  -22.195 -37.044 1.00 18.67  ?  16   PHE A HZ     1 
ATOM   258   N N      . HIS A 1 17  ? -6.028  -16.057 -36.507 1.00 14.61  ?  17   HIS A N      1 
ATOM   259   C CA     . HIS A 1 17  ? -6.138  -15.880 -35.071 1.00 12.25  ?  17   HIS A CA     1 
ATOM   260   C C      . HIS A 1 17  ? -6.279  -17.199 -34.331 1.00 12.77  ?  17   HIS A C      1 
ATOM   261   O O      . HIS A 1 17  ? -6.926  -18.142 -34.801 1.00 13.11  ?  17   HIS A O      1 
ATOM   262   C CB     . HIS A 1 17  ? -7.372  -15.033 -34.725 1.00 12.95  ?  17   HIS A CB     1 
ATOM   263   C CG     . HIS A 1 17  ? -7.214  -13.586 -35.014 1.00 12.69  ?  17   HIS A CG     1 
ATOM   264   N ND1    . HIS A 1 17  ? -6.547  -12.742 -34.160 1.00 14.28  ?  17   HIS A ND1    1 
ATOM   265   C CD2    . HIS A 1 17  ? -7.631  -12.826 -36.057 1.00 13.34  ?  17   HIS A CD2    1 
ATOM   266   C CE1    . HIS A 1 17  ? -6.554  -11.519 -34.661 1.00 13.83  ?  17   HIS A CE1    1 
ATOM   267   N NE2    . HIS A 1 17  ? -7.211  -11.543 -35.812 1.00 14.73  ?  17   HIS A NE2    1 
ATOM   268   H H      . HIS A 1 17  ? -6.785  -16.143 -36.906 1.00 17.53  ?  17   HIS A H      1 
ATOM   269   H HA     . HIS A 1 17  ? -5.324  -15.446 -34.773 1.00 14.70  ?  17   HIS A HA     1 
ATOM   270   H HB2    . HIS A 1 17  ? -8.125  -15.357 -35.244 1.00 15.53  ?  17   HIS A HB2    1 
ATOM   271   H HB3    . HIS A 1 17  ? -7.556  -15.127 -33.778 1.00 15.53  ?  17   HIS A HB3    1 
ATOM   272   H HD1    . HIS A 1 17  ? -6.183  -12.973 -33.416 1.00 17.13  ?  17   HIS A HD1    1 
ATOM   273   H HD2    . HIS A 1 17  ? -8.111  -13.119 -36.798 1.00 16.00  ?  17   HIS A HD2    1 
ATOM   274   H HE1    . HIS A 1 17  ? -6.165  -10.770 -34.273 1.00 16.60  ?  17   HIS A HE1    1 
ATOM   275   H HE2    . HIS A 1 17  ? -7.351  -10.864 -36.321 1.00 17.67  ?  17   HIS A HE2    1 
ATOM   276   N N      . ALA A 1 18  ? -5.684  -17.231 -33.142 1.00 13.23  ?  18   ALA A N      1 
ATOM   277   C CA     . ALA A 1 18  ? -5.896  -18.331 -32.214 1.00 13.29  ?  18   ALA A CA     1 
ATOM   278   C C      . ALA A 1 18  ? -7.376  -18.600 -31.979 1.00 11.44  ?  18   ALA A C      1 
ATOM   279   O O      . ALA A 1 18  ? -8.200  -17.681 -31.909 1.00 13.26  ?  18   ALA A O      1 
ATOM   280   C CB     . ALA A 1 18  ? -5.230  -17.986 -30.875 1.00 13.69  ?  18   ALA A CB     1 
ATOM   281   H H      . ALA A 1 18  ? -5.149  -16.625 -32.848 1.00 15.88  ?  18   ALA A H      1 
ATOM   282   H HA     . ALA A 1 18  ? -5.505  -19.136 -32.588 1.00 15.95  ?  18   ALA A HA     1 
ATOM   283   H HB1    . ALA A 1 18  ? -5.422  -18.690 -30.236 1.00 16.42  ?  18   ALA A HB1    1 
ATOM   284   H HB2    . ALA A 1 18  ? -4.272  -17.913 -31.008 1.00 16.42  ?  18   ALA A HB2    1 
ATOM   285   H HB3    . ALA A 1 18  ? -5.584  -17.142 -30.554 1.00 16.42  ?  18   ALA A HB3    1 
ATOM   286   N N      A SER A 1 19  ? -7.717  -19.889 -31.911 0.48 12.20  ?  19   SER A N      1 
ATOM   287   N N      B SER A 1 19  ? -7.705  -19.881 -31.832 0.52 12.27  ?  19   SER A N      1 
ATOM   288   C CA     A SER A 1 19  ? -9.025  -20.332 -31.426 0.48 14.00  ?  19   SER A CA     1 
ATOM   289   C CA     B SER A 1 19  ? -9.045  -20.321 -31.446 0.52 14.39  ?  19   SER A CA     1 
ATOM   290   C C      A SER A 1 19  ? -10.184 -19.705 -32.199 0.48 14.29  ?  19   SER A C      1 
ATOM   291   C C      B SER A 1 19  ? -10.132 -19.559 -32.189 0.52 14.86  ?  19   SER A C      1 
ATOM   292   O O      A SER A 1 19  ? -11.250 -19.441 -31.640 0.48 15.26  ?  19   SER A O      1 
ATOM   293   O O      B SER A 1 19  ? -11.078 -19.033 -31.599 0.52 16.75  ?  19   SER A O      1 
ATOM   294   C CB     A SER A 1 19  ? -9.142  -20.057 -29.923 0.48 15.72  ?  19   SER A CB     1 
ATOM   295   C CB     B SER A 1 19  ? -9.241  -20.196 -29.936 0.52 16.14  ?  19   SER A CB     1 
ATOM   296   O OG     A SER A 1 19  ? -10.223 -20.760 -29.347 0.48 15.58  ?  19   SER A OG     1 
ATOM   297   O OG     B SER A 1 19  ? -8.312  -20.997 -29.251 0.52 17.07  ?  19   SER A OG     1 
ATOM   298   H H      A SER A 1 19  ? -7.198  -20.534 -32.143 0.48 14.64  ?  19   SER A H      1 
ATOM   299   H H      B SER A 1 19  ? -7.154  -20.530 -31.954 0.52 14.72  ?  19   SER A H      1 
ATOM   300   H HA     A SER A 1 19  ? -9.100  -21.287 -31.579 0.48 16.79  ?  19   SER A HA     1 
ATOM   301   H HA     B SER A 1 19  ? -9.127  -21.254 -31.696 0.52 17.26  ?  19   SER A HA     1 
ATOM   302   H HB2    A SER A 1 19  ? -8.321  -20.338 -29.489 0.48 18.86  ?  19   SER A HB2    1 
ATOM   303   H HB2    B SER A 1 19  ? -9.114  -19.270 -29.676 0.52 19.37  ?  19   SER A HB2    1 
ATOM   304   H HB3    A SER A 1 19  ? -9.280  -19.107 -29.789 0.48 18.86  ?  19   SER A HB3    1 
ATOM   305   H HB3    B SER A 1 19  ? -10.138 -20.484 -29.708 0.52 19.37  ?  19   SER A HB3    1 
ATOM   306   H HG     A SER A 1 19  ? -10.166 -21.577 -29.533 0.48 18.70  ?  19   SER A HG     1 
ATOM   307   H HG     B SER A 1 19  ? -8.357  -20.849 -28.426 0.52 20.48  ?  19   SER A HG     1 
ATOM   308   N N      . THR A 1 20  ? -9.994  -19.507 -33.502 1.00 13.15  ?  20   THR A N      1 
ATOM   309   C CA     . THR A 1 20  ? -10.949 -18.805 -34.353 1.00 12.99  ?  20   THR A CA     1 
ATOM   310   C C      . THR A 1 20  ? -11.485 -19.729 -35.433 1.00 13.90  ?  20   THR A C      1 
ATOM   311   O O      . THR A 1 20  ? -10.796 -20.637 -35.907 1.00 13.77  ?  20   THR A O      1 
ATOM   312   C CB     . THR A 1 20  ? -10.272 -17.551 -34.955 1.00 13.86  ?  20   THR A CB     1 
ATOM   313   O OG1    . THR A 1 20  ? -9.937  -16.637 -33.894 1.00 13.87  ?  20   THR A OG1    1 
ATOM   314   C CG2    . THR A 1 20  ? -11.139 -16.835 -35.967 1.00 16.07  ?  20   THR A CG2    1 
ATOM   315   H H      A THR A 1 20  ? -9.297  -19.780 -33.926 0.48 15.78  ?  20   THR A H      1 
ATOM   316   H H      B THR A 1 20  ? -9.346  -19.876 -33.932 0.52 15.78  ?  20   THR A H      1 
ATOM   317   H HA     . THR A 1 20  ? -11.725 -18.524 -33.844 1.00 15.59  ?  20   THR A HA     1 
ATOM   318   H HB     . THR A 1 20  ? -9.475  -17.841 -35.426 1.00 16.63  ?  20   THR A HB     1 
ATOM   319   H HG1    . THR A 1 20  ? -9.402  -17.002 -33.359 1.00 16.64  ?  20   THR A HG1    1 
ATOM   320   H HG21   . THR A 1 20  ? -10.701 -16.021 -36.262 1.00 19.28  ?  20   THR A HG21   1 
ATOM   321   H HG22   . THR A 1 20  ? -11.292 -17.407 -36.736 1.00 19.28  ?  20   THR A HG22   1 
ATOM   322   H HG23   . THR A 1 20  ? -11.993 -16.607 -35.570 1.00 19.28  ?  20   THR A HG23   1 
ATOM   323   N N      . HIS A 1 21  ? -12.754 -19.516 -35.774 1.00 13.56  ?  21   HIS A N      1 
ATOM   324   C CA     . HIS A 1 21  ? -13.364 -20.191 -36.906 1.00 13.98  ?  21   HIS A CA     1 
ATOM   325   C C      . HIS A 1 21  ? -12.771 -19.564 -38.165 1.00 13.39  ?  21   HIS A C      1 
ATOM   326   O O      . HIS A 1 21  ? -13.245 -18.517 -38.630 1.00 15.13  ?  21   HIS A O      1 
ATOM   327   C CB     . HIS A 1 21  ? -14.867 -20.008 -36.885 1.00 16.25  ?  21   HIS A CB     1 
ATOM   328   C CG     . HIS A 1 21  ? -15.577 -20.968 -37.776 1.00 16.14  ?  21   HIS A CG     1 
ATOM   329   N ND1    . HIS A 1 21  ? -15.338 -21.030 -39.132 1.00 16.31  ?  21   HIS A ND1    1 
ATOM   330   C CD2    . HIS A 1 21  ? -16.509 -21.913 -37.510 1.00 17.53  ?  21   HIS A CD2    1 
ATOM   331   C CE1    . HIS A 1 21  ? -16.110 -21.965 -39.662 1.00 16.38  ?  21   HIS A CE1    1 
ATOM   332   N NE2    . HIS A 1 21  ? -16.814 -22.526 -38.697 1.00 17.32  ?  21   HIS A NE2    1 
ATOM   333   H H      . HIS A 1 21  ? -13.284 -18.980 -35.361 1.00 16.27  ?  21   HIS A H      1 
ATOM   334   H HA     . HIS A 1 21  ? -13.197 -21.146 -36.884 1.00 16.77  ?  21   HIS A HA     1 
ATOM   335   H HB2    . HIS A 1 21  ? -15.189 -20.144 -35.980 1.00 19.50  ?  21   HIS A HB2    1 
ATOM   336   H HB3    . HIS A 1 21  ? -15.079 -19.110 -37.182 1.00 19.50  ?  21   HIS A HB3    1 
ATOM   337   H HD2    . HIS A 1 21  ? -16.875 -22.110 -36.677 1.00 21.03  ?  21   HIS A HD2    1 
ATOM   338   H HE1    . HIS A 1 21  ? -16.150 -22.189 -40.563 1.00 19.65  ?  21   HIS A HE1    1 
ATOM   339   H HE2    . HIS A 1 21  ? -17.373 -23.172 -38.797 1.00 20.78  ?  21   HIS A HE2    1 
ATOM   340   N N      . LEU A 1 22  ? -11.697 -20.156 -38.672 1.00 13.33  ?  22   LEU A N      1 
ATOM   341   C CA     . LEU A 1 22  ? -10.888 -19.478 -39.683 1.00 14.59  ?  22   LEU A CA     1 
ATOM   342   C C      . LEU A 1 22  ? -11.701 -19.171 -40.934 1.00 14.41  ?  22   LEU A C      1 
ATOM   343   O O      . LEU A 1 22  ? -11.582 -18.083 -41.496 1.00 15.76  ?  22   LEU A O      1 
ATOM   344   C CB     . LEU A 1 22  ? -9.656  -20.323 -40.016 1.00 13.70  ?  22   LEU A CB     1 
ATOM   345   C CG     . LEU A 1 22  ? -8.711  -20.547 -38.827 1.00 13.83  ?  22   LEU A CG     1 
ATOM   346   C CD1    . LEU A 1 22  ? -7.495  -21.363 -39.273 1.00 15.13  ?  22   LEU A CD1    1 
ATOM   347   C CD2    . LEU A 1 22  ? -8.273  -19.232 -38.170 1.00 13.45  ?  22   LEU A CD2    1 
ATOM   348   H H      . LEU A 1 22  ? -11.414 -20.939 -38.454 1.00 15.99  ?  22   LEU A H      1 
ATOM   349   H HA     . LEU A 1 22  ? -10.579 -18.632 -39.324 1.00 17.51  ?  22   LEU A HA     1 
ATOM   350   H HB2    . LEU A 1 22  ? -9.952  -21.193 -40.327 1.00 16.44  ?  22   LEU A HB2    1 
ATOM   351   H HB3    . LEU A 1 22  ? -9.153  -19.875 -40.714 1.00 16.44  ?  22   LEU A HB3    1 
ATOM   352   H HG     . LEU A 1 22  ? -9.194  -21.044 -38.148 1.00 16.59  ?  22   LEU A HG     1 
ATOM   353   H HD11   . LEU A 1 22  ? -7.048  -21.719 -38.489 1.00 18.16  ?  22   LEU A HD11   1 
ATOM   354   H HD12   . LEU A 1 22  ? -7.794  -22.090 -39.842 1.00 18.16  ?  22   LEU A HD12   1 
ATOM   355   H HD13   . LEU A 1 22  ? -6.890  -20.786 -39.765 1.00 18.16  ?  22   LEU A HD13   1 
ATOM   356   H HD21   . LEU A 1 22  ? -7.653  -19.429 -37.451 1.00 16.14  ?  22   LEU A HD21   1 
ATOM   357   H HD22   . LEU A 1 22  ? -7.841  -18.674 -38.836 1.00 16.14  ?  22   LEU A HD22   1 
ATOM   358   H HD23   . LEU A 1 22  ? -9.055  -18.779 -37.817 1.00 16.14  ?  22   LEU A HD23   1 
ATOM   359   N N      . ARG A 1 23  ? -12.531 -20.113 -41.387 1.00 15.40  ?  23   ARG A N      1 
ATOM   360   C CA     . ARG A 1 23  ? -13.331 -19.863 -42.579 1.00 15.79  ?  23   ARG A CA     1 
ATOM   361   C C      . ARG A 1 23  ? -14.326 -18.737 -42.334 1.00 16.03  ?  23   ARG A C      1 
ATOM   362   O O      . ARG A 1 23  ? -14.428 -17.797 -43.136 1.00 16.96  ?  23   ARG A O      1 
ATOM   363   C CB     . ARG A 1 23  ? -14.062 -21.133 -43.015 1.00 17.57  ?  23   ARG A CB     1 
ATOM   364   C CG     . ARG A 1 23  ? -14.821 -20.955 -44.333 1.00 20.74  ?  23   ARG A CG     1 
ATOM   365   C CD     . ARG A 1 23  ? -15.881 -22.028 -44.540 1.00 24.53  ?  23   ARG A CD     1 
ATOM   366   N NE     . ARG A 1 23  ? -16.927 -21.925 -43.527 1.00 26.63  ?  23   ARG A NE     1 
ATOM   367   C CZ     . ARG A 1 23  ? -17.927 -22.787 -43.394 1.00 30.06  ?  23   ARG A CZ     1 
ATOM   368   N NH1    . ARG A 1 23  ? -18.020 -23.822 -44.221 1.00 31.71  ?  23   ARG A NH1    1 
ATOM   369   N NH2    . ARG A 1 23  ? -18.824 -22.616 -42.432 1.00 29.58  ?  23   ARG A NH2    1 
ATOM   370   H H      . ARG A 1 23  ? -12.647 -20.887 -41.030 1.00 18.48  ?  23   ARG A H      1 
ATOM   371   H HA     . ARG A 1 23  ? -12.736 -19.602 -43.299 1.00 18.94  ?  23   ARG A HA     1 
ATOM   372   H HB2    . ARG A 1 23  ? -13.414 -21.845 -43.136 1.00 21.08  ?  23   ARG A HB2    1 
ATOM   373   H HB3    . ARG A 1 23  ? -14.703 -21.380 -42.330 1.00 21.08  ?  23   ARG A HB3    1 
ATOM   374   H HG2    . ARG A 1 23  ? -15.263 -20.092 -44.331 1.00 24.88  ?  23   ARG A HG2    1 
ATOM   375   H HG3    . ARG A 1 23  ? -14.194 -21.005 -45.071 1.00 24.88  ?  23   ARG A HG3    1 
ATOM   376   H HD2    . ARG A 1 23  ? -16.287 -21.917 -45.414 1.00 29.43  ?  23   ARG A HD2    1 
ATOM   377   H HD3    . ARG A 1 23  ? -15.471 -22.905 -44.473 1.00 29.43  ?  23   ARG A HD3    1 
ATOM   378   H HE     . ARG A 1 23  ? -16.893 -21.262 -42.980 1.00 31.95  ?  23   ARG A HE     1 
ATOM   379   H HH11   . ARG A 1 23  ? -17.433 -23.932 -44.840 1.00 38.04  ?  23   ARG A HH11   1 
ATOM   380   H HH12   . ARG A 1 23  ? -18.667 -24.382 -44.137 1.00 38.04  ?  23   ARG A HH12   1 
ATOM   381   H HH21   . ARG A 1 23  ? -18.758 -21.947 -41.896 1.00 35.50  ?  23   ARG A HH21   1 
ATOM   382   H HH22   . ARG A 1 23  ? -19.473 -23.174 -42.345 1.00 35.50  ?  23   ARG A HH22   1 
ATOM   383   N N      . ASP A 1 24  ? -15.106 -18.834 -41.246 1.00 14.63  ?  24   ASP A N      1 
ATOM   384   C CA     . ASP A 1 24  ? -16.143 -17.827 -41.032 1.00 15.97  ?  24   ASP A CA     1 
ATOM   385   C C      . ASP A 1 24  ? -15.540 -16.442 -40.789 1.00 16.22  ?  24   ASP A C      1 
ATOM   386   O O      . ASP A 1 24  ? -16.118 -15.434 -41.218 1.00 17.68  ?  24   ASP A O      1 
ATOM   387   C CB     . ASP A 1 24  ? -17.078 -18.210 -39.888 1.00 18.21  ?  24   ASP A CB     1 
ATOM   388   C CG     . ASP A 1 24  ? -18.027 -19.344 -40.243 1.00 20.18  ?  24   ASP A CG     1 
ATOM   389   O OD1    . ASP A 1 24  ? -18.052 -19.790 -41.424 1.00 21.35  ?  24   ASP A OD1    1 
ATOM   390   O OD2    . ASP A 1 24  ? -18.743 -19.805 -39.320 1.00 22.72  -1 24   ASP A OD2    1 
ATOM   391   H H      . ASP A 1 24  ? -15.055 -19.447 -40.644 1.00 17.55  ?  24   ASP A H      1 
ATOM   392   H HA     . ASP A 1 24  ? -16.687 -17.790 -41.835 1.00 19.16  ?  24   ASP A HA     1 
ATOM   393   H HB2    . ASP A 1 24  ? -16.546 -18.494 -39.129 1.00 21.85  ?  24   ASP A HB2    1 
ATOM   394   H HB3    . ASP A 1 24  ? -17.613 -17.438 -39.648 1.00 21.85  ?  24   ASP A HB3    1 
ATOM   395   N N      . PHE A 1 25  ? -14.387 -16.362 -40.127 1.00 14.00  ?  25   PHE A N      1 
ATOM   396   C CA     . PHE A 1 25  ? -13.785 -15.044 -39.917 1.00 16.19  ?  25   PHE A CA     1 
ATOM   397   C C      . PHE A 1 25  ? -13.263 -14.449 -41.225 1.00 15.93  ?  25   PHE A C      1 
ATOM   398   O O      . PHE A 1 25  ? -13.506 -13.277 -41.523 1.00 16.69  ?  25   PHE A O      1 
ATOM   399   C CB     . PHE A 1 25  ? -12.689 -15.116 -38.860 1.00 16.61  ?  25   PHE A CB     1 
ATOM   400   C CG     . PHE A 1 25  ? -12.148 -13.773 -38.478 1.00 15.56  ?  25   PHE A CG     1 
ATOM   401   C CD1    . PHE A 1 25  ? -12.889 -12.922 -37.675 1.00 16.55  ?  25   PHE A CD1    1 
ATOM   402   C CD2    . PHE A 1 25  ? -10.918 -13.352 -38.938 1.00 15.23  ?  25   PHE A CD2    1 
ATOM   403   C CE1    . PHE A 1 25  ? -12.391 -11.666 -37.340 1.00 16.90  ?  25   PHE A CE1    1 
ATOM   404   C CE2    . PHE A 1 25  ? -10.424 -12.119 -38.593 1.00 16.14  ?  25   PHE A CE2    1 
ATOM   405   C CZ     . PHE A 1 25  ? -11.161 -11.281 -37.803 1.00 16.16  ?  25   PHE A CZ     1 
ATOM   406   H H      . PHE A 1 25  ? -13.947 -17.025 -39.801 1.00 16.79  ?  25   PHE A H      1 
ATOM   407   H HA     . PHE A 1 25  ? -14.468 -14.444 -39.578 1.00 19.43  ?  25   PHE A HA     1 
ATOM   408   H HB2    . PHE A 1 25  ? -13.051 -15.531 -38.061 1.00 19.93  ?  25   PHE A HB2    1 
ATOM   409   H HB3    . PHE A 1 25  ? -11.954 -15.647 -39.205 1.00 19.93  ?  25   PHE A HB3    1 
ATOM   410   H HD1    . PHE A 1 25  ? -13.721 -13.191 -37.359 1.00 19.85  ?  25   PHE A HD1    1 
ATOM   411   H HD2    . PHE A 1 25  ? -10.417 -13.910 -39.489 1.00 18.28  ?  25   PHE A HD2    1 
ATOM   412   H HE1    . PHE A 1 25  ? -12.891 -11.092 -36.806 1.00 20.28  ?  25   PHE A HE1    1 
ATOM   413   H HE2    . PHE A 1 25  ? -9.587  -11.853 -38.897 1.00 19.36  ?  25   PHE A HE2    1 
ATOM   414   H HZ     . PHE A 1 25  ? -10.825 -10.443 -37.579 1.00 19.39  ?  25   PHE A HZ     1 
ATOM   415   N N      . ALA A 1 26  ? -12.560 -15.243 -42.033 1.00 16.63  ?  26   ALA A N      1 
ATOM   416   C CA     . ALA A 1 26  ? -12.050 -14.729 -43.303 1.00 15.72  ?  26   ALA A CA     1 
ATOM   417   C C      . ALA A 1 26  ? -13.169 -14.280 -44.238 1.00 16.56  ?  26   ALA A C      1 
ATOM   418   O O      . ALA A 1 26  ? -12.992 -13.328 -45.019 1.00 17.84  ?  26   ALA A O      1 
ATOM   419   C CB     . ALA A 1 26  ? -11.191 -15.789 -43.987 1.00 15.13  ?  26   ALA A CB     1 
ATOM   420   H H      . ALA A 1 26  ? -12.366 -16.066 -41.875 1.00 19.95  ?  26   ALA A H      1 
ATOM   421   H HA     . ALA A 1 26  ? -11.496 -13.955 -43.116 1.00 18.86  ?  26   ALA A HA     1 
ATOM   422   H HB1    . ALA A 1 26  ? -10.944 -15.474 -44.870 1.00 18.16  ?  26   ALA A HB1    1 
ATOM   423   H HB2    . ALA A 1 26  ? -10.395 -15.942 -43.455 1.00 18.16  ?  26   ALA A HB2    1 
ATOM   424   H HB3    . ALA A 1 26  ? -11.702 -16.610 -44.061 1.00 18.16  ?  26   ALA A HB3    1 
ATOM   425   N N      . HIS A 1 27  ? -14.325 -14.925 -44.158 1.00 18.15  ?  27   HIS A N      1 
ATOM   426   C CA     . HIS A 1 27  ? -15.414 -14.676 -45.099 1.00 18.62  ?  27   HIS A CA     1 
ATOM   427   C C      . HIS A 1 27  ? -16.487 -13.737 -44.552 1.00 20.59  ?  27   HIS A C      1 
ATOM   428   O O      . HIS A 1 27  ? -17.506 -13.526 -45.215 1.00 23.04  ?  27   HIS A O      1 
ATOM   429   C CB     . HIS A 1 27  ? -16.034 -15.993 -45.566 1.00 20.55  ?  27   HIS A CB     1 
ATOM   430   C CG     . HIS A 1 27  ? -15.150 -16.766 -46.488 1.00 23.26  ?  27   HIS A CG     1 
ATOM   431   N ND1    . HIS A 1 27  ? -15.199 -16.630 -47.859 1.00 28.48  ?  27   HIS A ND1    1 
ATOM   432   C CD2    . HIS A 1 27  ? -14.171 -17.660 -46.234 1.00 22.30  ?  27   HIS A CD2    1 
ATOM   433   C CE1    . HIS A 1 27  ? -14.300 -17.428 -48.408 1.00 28.48  ?  27   HIS A CE1    1 
ATOM   434   N NE2    . HIS A 1 27  ? -13.670 -18.070 -47.442 1.00 24.79  ?  27   HIS A NE2    1 
ATOM   435   H H      . HIS A 1 27  ? -14.505 -15.518 -43.562 1.00 21.77  ?  27   HIS A H      1 
ATOM   436   H HA     . HIS A 1 27  ? -15.036 -14.243 -45.880 1.00 22.34  ?  27   HIS A HA     1 
ATOM   437   H HB2    . HIS A 1 27  ? -16.214 -16.547 -44.790 1.00 24.66  ?  27   HIS A HB2    1 
ATOM   438   H HB3    . HIS A 1 27  ? -16.861 -15.801 -46.035 1.00 24.66  ?  27   HIS A HB3    1 
ATOM   439   H HD2    . HIS A 1 27  ? -13.888 -17.944 -45.395 1.00 26.75  ?  27   HIS A HD2    1 
ATOM   440   H HE1    . HIS A 1 27  ? -14.139 -17.522 -49.319 1.00 34.17  ?  27   HIS A HE1    1 
ATOM   441   H HE2    . HIS A 1 27  ? -13.047 -18.652 -47.553 1.00 29.75  ?  27   HIS A HE2    1 
ATOM   442   N N      . GLY A 1 28  ? -16.269 -13.141 -43.383 1.00 19.38  ?  28   GLY A N      1 
ATOM   443   C CA     . GLY A 1 28  ? -17.138 -12.093 -42.893 1.00 21.60  ?  28   GLY A CA     1 
ATOM   444   C C      . GLY A 1 28  ? -18.307 -12.538 -42.042 1.00 21.88  ?  28   GLY A C      1 
ATOM   445   O O      . GLY A 1 28  ? -19.131 -11.689 -41.660 1.00 24.31  ?  28   GLY A O      1 
ATOM   446   H H      . GLY A 1 28  ? -15.617 -13.332 -42.856 1.00 23.25  ?  28   GLY A H      1 
ATOM   447   H HA2    . GLY A 1 28  ? -16.607 -11.481 -42.359 1.00 25.92  ?  28   GLY A HA2    1 
ATOM   448   H HA3    . GLY A 1 28  ? -17.500 -11.615 -43.655 1.00 25.92  ?  28   GLY A HA3    1 
ATOM   449   N N      . GLU A 1 29  ? -18.405 -13.829 -41.715 1.00 23.11  ?  29   GLU A N      1 
ATOM   450   C CA     . GLU A 1 29  ? -19.539 -14.320 -40.948 1.00 26.60  ?  29   GLU A CA     1 
ATOM   451   C C      . GLU A 1 29  ? -19.291 -14.346 -39.445 1.00 25.11  ?  29   GLU A C      1 
ATOM   452   O O      . GLU A 1 29  ? -20.244 -14.212 -38.671 1.00 32.24  ?  29   GLU A O      1 
ATOM   453   C CB     . GLU A 1 29  ? -19.944 -15.725 -41.398 1.00 33.29  ?  29   GLU A CB     1 
ATOM   454   C CG     . GLU A 1 29  ? -20.930 -15.771 -42.554 1.00 43.51  ?  29   GLU A CG     1 
ATOM   455   C CD     . GLU A 1 29  ? -20.243 -15.881 -43.880 1.00 50.82  ?  29   GLU A CD     1 
ATOM   456   O OE1    . GLU A 1 29  ? -19.219 -15.187 -44.061 1.00 53.82  ?  29   GLU A OE1    1 
ATOM   457   O OE2    . GLU A 1 29  ? -20.713 -16.669 -44.735 1.00 52.85  -1 29   GLU A OE2    1 
ATOM   458   H H      . GLU A 1 29  ? -17.830 -14.432 -41.926 1.00 27.73  ?  29   GLU A H      1 
ATOM   459   H HA     . GLU A 1 29  ? -20.283 -13.723 -41.124 1.00 31.92  ?  29   GLU A HA     1 
ATOM   460   H HB2    . GLU A 1 29  ? -19.146 -16.199 -41.678 1.00 39.95  ?  29   GLU A HB2    1 
ATOM   461   H HB3    . GLU A 1 29  ? -20.355 -16.181 -40.647 1.00 39.95  ?  29   GLU A HB3    1 
ATOM   462   H HG2    . GLU A 1 29  ? -21.509 -16.542 -42.448 1.00 52.21  ?  29   GLU A HG2    1 
ATOM   463   H HG3    . GLU A 1 29  ? -21.459 -14.957 -42.554 1.00 52.21  ?  29   GLU A HG3    1 
ATOM   464   N N      . ALA A 1 30  ? -18.083 -14.496 -39.014 1.00 20.64  ?  30   ALA A N      1 
ATOM   465   C CA     . ALA A 1 30  ? -17.814 -14.510 -37.583 1.00 19.34  ?  30   ALA A CA     1 
ATOM   466   C C      . ALA A 1 30  ? -17.385 -13.128 -37.124 1.00 19.39  ?  30   ALA A C      1 
ATOM   467   O O      . ALA A 1 30  ? -16.741 -12.393 -37.879 1.00 18.82  ?  30   ALA A O      1 
ATOM   468   C CB     . ALA A 1 30  ? -16.681 -15.483 -37.254 1.00 20.09  ?  30   ALA A CB     1 
ATOM   469   H H      . ALA A 1 30  ? -17.389 -14.593 -39.513 1.00 24.76  ?  30   ALA A H      1 
ATOM   470   H HA     . ALA A 1 30  ? -18.612 -14.786 -37.106 1.00 23.20  ?  30   ALA A HA     1 
ATOM   471   H HB1    . ALA A 1 30  ? -16.538 -15.488 -36.295 1.00 24.11  ?  30   ALA A HB1    1 
ATOM   472   H HB2    . ALA A 1 30  ? -16.930 -16.370 -37.556 1.00 24.11  ?  30   ALA A HB2    1 
ATOM   473   H HB3    . ALA A 1 30  ? -15.874 -15.193 -37.707 1.00 24.11  ?  30   ALA A HB3    1 
ATOM   474   N N      . PRO A 1 31  ? -17.711 -12.733 -35.897 1.00 18.69  ?  31   PRO A N      1 
ATOM   475   C CA     . PRO A 1 31  ? -17.406 -11.369 -35.456 1.00 18.36  ?  31   PRO A CA     1 
ATOM   476   C C      . PRO A 1 31  ? -15.940 -11.192 -35.081 1.00 16.06  ?  31   PRO A C      1 
ATOM   477   O O      . PRO A 1 31  ? -15.231 -12.129 -34.698 1.00 17.99  ?  31   PRO A O      1 
ATOM   478   C CB     . PRO A 1 31  ? -18.286 -11.204 -34.214 1.00 21.26  ?  31   PRO A CB     1 
ATOM   479   C CG     . PRO A 1 31  ? -18.397 -12.576 -33.655 1.00 21.67  ?  31   PRO A CG     1 
ATOM   480   C CD     . PRO A 1 31  ? -18.475 -13.488 -34.882 1.00 20.26  ?  31   PRO A CD     1 
ATOM   481   H HA     . PRO A 1 31  ? -17.649 -10.728 -36.142 1.00 22.03  ?  31   PRO A HA     1 
ATOM   482   H HB2    . PRO A 1 31  ? -17.862 -10.602 -33.583 1.00 25.50  ?  31   PRO A HB2    1 
ATOM   483   H HB3    . PRO A 1 31  ? -19.157 -10.858 -34.467 1.00 25.50  ?  31   PRO A HB3    1 
ATOM   484   H HG2    . PRO A 1 31  ? -17.615 -12.780 -33.118 1.00 26.01  ?  31   PRO A HG2    1 
ATOM   485   H HG3    . PRO A 1 31  ? -19.199 -12.650 -33.114 1.00 26.01  ?  31   PRO A HG3    1 
ATOM   486   H HD2    . PRO A 1 31  ? -18.061 -14.346 -34.703 1.00 24.30  ?  31   PRO A HD2    1 
ATOM   487   H HD3    . PRO A 1 31  ? -19.395 -13.615 -35.162 1.00 24.30  ?  31   PRO A HD3    1 
ATOM   488   N N      . GLY A 1 32  ? -15.499 -9.935  -35.172 1.00 15.52  ?  32   GLY A N      1 
ATOM   489   C CA     . GLY A 1 32  ? -14.201 -9.533  -34.683 1.00 16.80  ?  32   GLY A CA     1 
ATOM   490   C C      . GLY A 1 32  ? -14.366 -8.454  -33.628 1.00 15.22  ?  32   GLY A C      1 
ATOM   491   O O      . GLY A 1 32  ? -15.476 -7.958  -33.385 1.00 17.03  ?  32   GLY A O      1 
ATOM   492   H H      . GLY A 1 32  ? -15.952 -9.293  -35.522 1.00 18.62  ?  32   GLY A H      1 
ATOM   493   H HA2    . GLY A 1 32  ? -13.743 -10.293 -34.291 1.00 20.16  ?  32   GLY A HA2    1 
ATOM   494   H HA3    . GLY A 1 32  ? -13.665 -9.183  -35.412 1.00 20.16  ?  32   GLY A HA3    1 
ATOM   495   N N      . ARG A 1 33  ? -13.255 -8.102  -32.987 1.00 16.64  ?  33   ARG A N      1 
ATOM   496   C CA     . ARG A 1 33  ? -13.256 -6.937  -32.101 1.00 16.34  ?  33   ARG A CA     1 
ATOM   497   C C      . ARG A 1 33  ? -11.824 -6.455  -31.963 1.00 17.65  ?  33   ARG A C      1 
ATOM   498   O O      . ARG A 1 33  ? -10.927 -7.263  -31.696 1.00 16.94  ?  33   ARG A O      1 
ATOM   499   C CB     . ARG A 1 33  ? -13.824 -7.232  -30.709 1.00 16.95  ?  33   ARG A CB     1 
ATOM   500   C CG     . ARG A 1 33  ? -14.033 -5.959  -29.867 1.00 19.41  ?  33   ARG A CG     1 
ATOM   501   C CD     . ARG A 1 33  ? -14.706 -6.228  -28.547 1.00 20.58  ?  33   ARG A CD     1 
ATOM   502   N NE     . ARG A 1 33  ? -15.987 -6.927  -28.675 1.00 19.81  ?  33   ARG A NE     1 
ATOM   503   C CZ     . ARG A 1 33  ? -17.159 -6.344  -28.903 1.00 23.29  ?  33   ARG A CZ     1 
ATOM   504   N NH1    . ARG A 1 33  ? -17.255 -5.018  -29.044 1.00 22.62  ?  33   ARG A NH1    1 
ATOM   505   N NH2    . ARG A 1 33  ? -18.244 -7.094  -29.002 1.00 25.87  ?  33   ARG A NH2    1 
ATOM   506   H H      . ARG A 1 33  ? -12.502 -8.511  -33.046 1.00 19.97  ?  33   ARG A H      1 
ATOM   507   H HA     . ARG A 1 33  ? -13.813 -6.252  -32.502 1.00 19.61  ?  33   ARG A HA     1 
ATOM   508   H HB2    . ARG A 1 33  ? -14.683 -7.673  -30.806 1.00 20.34  ?  33   ARG A HB2    1 
ATOM   509   H HB3    . ARG A 1 33  ? -13.207 -7.809  -30.233 1.00 20.34  ?  33   ARG A HB3    1 
ATOM   510   H HG2    . ARG A 1 33  ? -13.170 -5.556  -29.685 1.00 23.29  ?  33   ARG A HG2    1 
ATOM   511   H HG3    . ARG A 1 33  ? -14.589 -5.340  -30.365 1.00 23.29  ?  33   ARG A HG3    1 
ATOM   512   H HD2    . ARG A 1 33  ? -14.121 -6.779  -28.003 1.00 24.69  ?  33   ARG A HD2    1 
ATOM   513   H HD3    . ARG A 1 33  ? -14.873 -5.382  -28.103 1.00 24.69  ?  33   ARG A HD3    1 
ATOM   514   H HE     . ARG A 1 33  ? -15.979 -7.783  -28.595 1.00 23.77  ?  33   ARG A HE     1 
ATOM   515   H HH11   . ARG A 1 33  ? -16.551 -4.528  -28.988 1.00 27.14  ?  33   ARG A HH11   1 
ATOM   516   H HH12   . ARG A 1 33  ? -18.021 -4.656  -29.192 1.00 27.14  ?  33   ARG A HH12   1 
ATOM   517   H HH21   . ARG A 1 33  ? -18.186 -7.948  -28.919 1.00 31.05  ?  33   ARG A HH21   1 
ATOM   518   H HH22   . ARG A 1 33  ? -19.008 -6.727  -29.150 1.00 31.05  ?  33   ARG A HH22   1 
ATOM   519   N N      . VAL A 1 34  ? -11.617 -5.158  -32.180 1.00 16.23  ?  34   VAL A N      1 
ATOM   520   C CA     . VAL A 1 34  ? -10.317 -4.514  -32.046 1.00 15.06  ?  34   VAL A CA     1 
ATOM   521   C C      . VAL A 1 34  ? -10.274 -3.873  -30.665 1.00 15.57  ?  34   VAL A C      1 
ATOM   522   O O      . VAL A 1 34  ? -11.034 -2.930  -30.385 1.00 17.44  ?  34   VAL A O      1 
ATOM   523   C CB     . VAL A 1 34  ? -10.108 -3.454  -33.134 1.00 14.89  ?  34   VAL A CB     1 
ATOM   524   C CG1    . VAL A 1 34  ? -8.754  -2.810  -32.930 1.00 19.29  ?  34   VAL A CG1    1 
ATOM   525   C CG2    . VAL A 1 34  ? -10.215 -4.051  -34.514 1.00 15.95  ?  34   VAL A CG2    1 
ATOM   526   H H      . VAL A 1 34  ? -12.240 -4.614  -32.415 1.00 19.47  ?  34   VAL A H      1 
ATOM   527   H HA     . VAL A 1 34  ? -9.615  -5.180  -32.116 1.00 18.07  ?  34   VAL A HA     1 
ATOM   528   H HB     . VAL A 1 34  ? -10.802 -2.779  -33.067 1.00 17.86  ?  34   VAL A HB     1 
ATOM   529   H HG11   . VAL A 1 34  ? -8.527  -2.294  -33.720 1.00 23.14  ?  34   VAL A HG11   1 
ATOM   530   H HG12   . VAL A 1 34  ? -8.794  -2.228  -32.155 1.00 23.14  ?  34   VAL A HG12   1 
ATOM   531   H HG13   . VAL A 1 34  ? -8.092  -3.505  -32.787 1.00 23.14  ?  34   VAL A HG13   1 
ATOM   532   H HG21   . VAL A 1 34  ? -10.170 -3.339  -35.171 1.00 19.14  ?  34   VAL A HG21   1 
ATOM   533   H HG22   . VAL A 1 34  ? -9.481  -4.671  -34.648 1.00 19.14  ?  34   VAL A HG22   1 
ATOM   534   H HG23   . VAL A 1 34  ? -11.061 -4.519  -34.591 1.00 19.14  ?  34   VAL A HG23   1 
ATOM   535   N N      A MET A 1 35  ? -9.364  -4.346  -29.815 0.39 15.70  ?  35   MET A N      1 
ATOM   536   N N      B MET A 1 35  ? -9.384  -4.359  -29.800 0.61 15.76  ?  35   MET A N      1 
ATOM   537   C CA     A MET A 1 35  ? -9.156  -3.752  -28.498 0.39 15.56  ?  35   MET A CA     1 
ATOM   538   C CA     B MET A 1 35  ? -9.179  -3.746  -28.489 0.61 15.86  ?  35   MET A CA     1 
ATOM   539   C C      A MET A 1 35  ? -8.124  -2.641  -28.608 0.39 16.68  ?  35   MET A C      1 
ATOM   540   C C      B MET A 1 35  ? -8.142  -2.639  -28.614 0.61 16.89  ?  35   MET A C      1 
ATOM   541   O O      A MET A 1 35  ? -7.107  -2.788  -29.293 0.39 17.83  ?  35   MET A O      1 
ATOM   542   O O      B MET A 1 35  ? -7.145  -2.785  -29.326 0.61 18.32  ?  35   MET A O      1 
ATOM   543   C CB     A MET A 1 35  ? -8.693  -4.823  -27.515 0.39 16.77  ?  35   MET A CB     1 
ATOM   544   C CB     B MET A 1 35  ? -8.746  -4.804  -27.476 0.61 18.98  ?  35   MET A CB     1 
ATOM   545   C CG     A MET A 1 35  ? -9.635  -6.003  -27.466 0.39 17.00  ?  35   MET A CG     1 
ATOM   546   C CG     B MET A 1 35  ? -9.860  -5.777  -27.152 0.61 19.91  ?  35   MET A CG     1 
ATOM   547   S SD     A MET A 1 35  ? -11.360 -5.502  -27.284 0.39 18.70  ?  35   MET A SD     1 
ATOM   548   S SD     B MET A 1 35  ? -11.330 -4.957  -26.459 0.61 21.88  ?  35   MET A SD     1 
ATOM   549   C CE     A MET A 1 35  ? -11.291 -4.615  -25.723 0.39 17.44  ?  35   MET A CE     1 
ATOM   550   C CE     B MET A 1 35  ? -12.088 -6.327  -25.604 0.61 22.24  ?  35   MET A CE     1 
ATOM   551   H H      A MET A 1 35  ? -8.851  -5.016  -29.980 0.39 18.83  ?  35   MET A H      1 
ATOM   552   H H      B MET A 1 35  ? -8.887  -5.044  -29.950 0.61 18.91  ?  35   MET A H      1 
ATOM   553   H HA     A MET A 1 35  ? -9.985  -3.380  -28.158 0.39 18.67  ?  35   MET A HA     1 
ATOM   554   H HA     B MET A 1 35  ? -10.005 -3.362  -28.158 0.61 19.03  ?  35   MET A HA     1 
ATOM   555   H HB2    A MET A 1 35  ? -7.819  -5.145  -27.785 0.39 20.12  ?  35   MET A HB2    1 
ATOM   556   H HB2    B MET A 1 35  ? -8.002  -5.307  -27.841 0.61 22.77  ?  35   MET A HB2    1 
ATOM   557   H HB3    A MET A 1 35  ? -8.645  -4.438  -26.626 0.39 20.12  ?  35   MET A HB3    1 
ATOM   558   H HB3    B MET A 1 35  ? -8.479  -4.365  -26.654 0.61 22.77  ?  35   MET A HB3    1 
ATOM   559   H HG2    A MET A 1 35  ? -9.553  -6.509  -28.289 0.39 20.39  ?  35   MET A HG2    1 
ATOM   560   H HG2    B MET A 1 35  ? -10.127 -6.235  -27.964 0.61 23.89  ?  35   MET A HG2    1 
ATOM   561   H HG3    A MET A 1 35  ? -9.403  -6.563  -26.708 0.39 20.39  ?  35   MET A HG3    1 
ATOM   562   H HG3    B MET A 1 35  ? -9.539  -6.419  -26.499 0.61 23.89  ?  35   MET A HG3    1 
ATOM   563   H HE1    A MET A 1 35  ? -12.189 -4.354  -25.468 0.39 20.93  ?  35   MET A HE1    1 
ATOM   564   H HE1    B MET A 1 35  ? -12.910 -6.024  -25.189 0.61 26.69  ?  35   MET A HE1    1 
ATOM   565   H HE2    A MET A 1 35  ? -10.910 -5.196  -25.046 0.39 20.93  ?  35   MET A HE2    1 
ATOM   566   H HE2    B MET A 1 35  ? -12.280 -7.031  -26.244 0.61 26.69  ?  35   MET A HE2    1 
ATOM   567   H HE3    A MET A 1 35  ? -10.736 -3.827  -25.832 0.39 20.93  ?  35   MET A HE3    1 
ATOM   568   H HE3    B MET A 1 35  ? -11.476 -6.655  -24.927 0.61 26.69  ?  35   MET A HE3    1 
ATOM   569   N N      . ALA A 1 36  ? -8.390  -1.524  -27.936 1.00 16.86  ?  36   ALA A N      1 
ATOM   570   C CA     . ALA A 1 36  ? -7.600  -0.315  -28.136 1.00 18.65  ?  36   ALA A CA     1 
ATOM   571   C C      . ALA A 1 36  ? -7.090  0.346   -26.867 1.00 18.25  ?  36   ALA A C      1 
ATOM   572   O O      . ALA A 1 36  ? -6.113  1.112   -26.953 1.00 20.35  ?  36   ALA A O      1 
ATOM   573   C CB     . ALA A 1 36  ? -8.418  0.720   -28.930 1.00 22.63  ?  36   ALA A CB     1 
ATOM   574   H H      A ALA A 1 36  ? -9.024  -1.442  -27.360 0.39 20.23  ?  36   ALA A H      1 
ATOM   575   H H      B ALA A 1 36  ? -9.015  -1.442  -27.351 0.61 20.23  ?  36   ALA A H      1 
ATOM   576   H HA     . ALA A 1 36  ? -6.817  -0.556  -28.654 1.00 22.38  ?  36   ALA A HA     1 
ATOM   577   H HB1    . ALA A 1 36  ? -7.869  1.504   -29.086 1.00 27.16  ?  36   ALA A HB1    1 
ATOM   578   H HB2    . ALA A 1 36  ? -8.685  0.329   -29.777 1.00 27.16  ?  36   ALA A HB2    1 
ATOM   579   H HB3    . ALA A 1 36  ? -9.204  0.964   -28.416 1.00 27.16  ?  36   ALA A HB3    1 
ATOM   580   N N      . GLY A 1 37  ? -7.704  0.115   -25.713 1.00 17.49  ?  37   GLY A N      1 
ATOM   581   C CA     . GLY A 1 37  ? -7.262  0.755   -24.499 1.00 17.83  ?  37   GLY A CA     1 
ATOM   582   C C      . GLY A 1 37  ? -7.692  -0.017  -23.266 1.00 16.86  ?  37   GLY A C      1 
ATOM   583   O O      . GLY A 1 37  ? -8.268  -1.105  -23.355 1.00 16.62  ?  37   GLY A O      1 
ATOM   584   H H      . GLY A 1 37  ? -8.378  -0.410  -25.613 1.00 20.99  ?  37   GLY A H      1 
ATOM   585   H HA2    . GLY A 1 37  ? -6.294  0.818   -24.500 1.00 21.40  ?  37   GLY A HA2    1 
ATOM   586   H HA3    . GLY A 1 37  ? -7.637  1.648   -24.449 1.00 21.40  ?  37   GLY A HA3    1 
ATOM   587   N N      . GLY A 1 38  ? -7.421  0.572   -22.117 1.00 16.43  ?  38   GLY A N      1 
ATOM   588   C CA     . GLY A 1 38  ? -7.872  0.010   -20.864 1.00 17.29  ?  38   GLY A CA     1 
ATOM   589   C C      . GLY A 1 38  ? -7.098  0.547   -19.685 1.00 15.71  ?  38   GLY A C      1 
ATOM   590   O O      . GLY A 1 38  ? -5.951  0.995   -19.789 1.00 17.29  ?  38   GLY A O      1 
ATOM   591   H H      . GLY A 1 38  ? -6.974  1.303   -22.037 1.00 19.71  ?  38   GLY A H      1 
ATOM   592   H HA2    . GLY A 1 38  ? -8.810  0.220   -20.736 1.00 20.74  ?  38   GLY A HA2    1 
ATOM   593   H HA3    . GLY A 1 38  ? -7.765  -0.954  -20.886 1.00 20.74  ?  38   GLY A HA3    1 
ATOM   594   N N      . GLU A 1 39  ? -7.745  0.477   -18.531 1.00 18.24  ?  39   GLU A N      1 
ATOM   595   C CA     . GLU A 1 39  ? -7.163  0.900   -17.273 1.00 18.07  ?  39   GLU A CA     1 
ATOM   596   C C      . GLU A 1 39  ? -7.844  0.117   -16.164 1.00 17.23  ?  39   GLU A C      1 
ATOM   597   O O      . GLU A 1 39  ? -9.061  -0.041  -16.179 1.00 17.60  ?  39   GLU A O      1 
ATOM   598   C CB     . GLU A 1 39  ? -7.373  2.399   -17.039 1.00 23.61  ?  39   GLU A CB     1 
ATOM   599   C CG     . GLU A 1 39  ? -6.704  2.919   -15.782 1.00 31.47  ?  39   GLU A CG     1 
ATOM   600   C CD     . GLU A 1 39  ? -7.560  2.763   -14.524 1.00 41.13  ?  39   GLU A CD     1 
ATOM   601   O OE1    . GLU A 1 39  ? -6.996  2.857   -13.415 1.00 44.07  ?  39   GLU A OE1    1 
ATOM   602   O OE2    . GLU A 1 39  ? -8.790  2.548   -14.640 1.00 44.13  -1 39   GLU A OE2    1 
ATOM   603   H H      . GLU A 1 39  ? -8.547  0.179   -18.451 1.00 21.88  ?  39   GLU A H      1 
ATOM   604   H HA     . GLU A 1 39  ? -6.211  0.717   -17.266 1.00 21.69  ?  39   GLU A HA     1 
ATOM   605   H HB2    . GLU A 1 39  ? -7.008  2.886   -17.793 1.00 28.32  ?  39   GLU A HB2    1 
ATOM   606   H HB3    . GLU A 1 39  ? -8.325  2.572   -16.961 1.00 28.32  ?  39   GLU A HB3    1 
ATOM   607   H HG2    . GLU A 1 39  ? -5.878  2.430   -15.642 1.00 37.76  ?  39   GLU A HG2    1 
ATOM   608   H HG3    . GLU A 1 39  ? -6.514  3.864   -15.896 1.00 37.76  ?  39   GLU A HG3    1 
ATOM   609   N N      . GLY A 1 40  ? -7.057  -0.355  -15.210 1.00 17.46  ?  40   GLY A N      1 
ATOM   610   C CA     . GLY A 1 40  ? -7.641  -1.034  -14.066 1.00 16.71  ?  40   GLY A CA     1 
ATOM   611   C C      . GLY A 1 40  ? -8.170  -2.379  -14.507 1.00 14.84  ?  40   GLY A C      1 
ATOM   612   O O      . GLY A 1 40  ? -7.441  -3.181  -15.099 1.00 16.34  ?  40   GLY A O      1 
ATOM   613   H H      . GLY A 1 40  ? -6.199  -0.299  -15.198 1.00 20.95  ?  40   GLY A H      1 
ATOM   614   H HA2    . GLY A 1 40  ? -6.971  -1.164  -13.377 1.00 20.04  ?  40   GLY A HA2    1 
ATOM   615   H HA3    . GLY A 1 40  ? -8.370  -0.508  -13.701 1.00 20.04  ?  40   GLY A HA3    1 
ATOM   616   N N      . ILE A 1 41  ? -9.445  -2.656  -14.211 1.00 15.51  ?  41   ILE A N      1 
ATOM   617   C CA     . ILE A 1 41  ? -10.069 -3.900  -14.637 1.00 15.32  ?  41   ILE A CA     1 
ATOM   618   C C      . ILE A 1 41  ? -10.837 -3.749  -15.939 1.00 15.65  ?  41   ILE A C      1 
ATOM   619   O O      . ILE A 1 41  ? -11.513 -4.700  -16.361 1.00 18.02  ?  41   ILE A O      1 
ATOM   620   C CB     . ILE A 1 41  ? -10.954 -4.521  -13.549 1.00 16.63  ?  41   ILE A CB     1 
ATOM   621   C CG1    . ILE A 1 41  ? -12.253 -3.748  -13.371 1.00 18.65  ?  41   ILE A CG1    1 
ATOM   622   C CG2    . ILE A 1 41  ? -10.179 -4.618  -12.267 1.00 16.24  ?  41   ILE A CG2    1 
ATOM   623   C CD1    . ILE A 1 41  ? -13.238 -4.378  -12.387 1.00 20.78  ?  41   ILE A CD1    1 
ATOM   624   H H      . ILE A 1 41  ? -9.963  -2.134  -13.765 1.00 18.61  ?  41   ILE A H      1 
ATOM   625   H HA     . ILE A 1 41  ? -9.345  -4.524  -14.801 1.00 18.38  ?  41   ILE A HA     1 
ATOM   626   H HB     . ILE A 1 41  ? -11.207 -5.415  -13.829 1.00 19.95  ?  41   ILE A HB     1 
ATOM   627   H HG12   . ILE A 1 41  ? -12.041 -2.859  -13.044 1.00 22.38  ?  41   ILE A HG12   1 
ATOM   628   H HG13   . ILE A 1 41  ? -12.697 -3.687  -14.231 1.00 22.38  ?  41   ILE A HG13   1 
ATOM   629   H HG21   . ILE A 1 41  ? -10.664 -5.185  -11.646 1.00 19.48  ?  41   ILE A HG21   1 
ATOM   630   H HG22   . ILE A 1 41  ? -9.307  -5.002  -12.453 1.00 19.48  ?  41   ILE A HG22   1 
ATOM   631   H HG23   . ILE A 1 41  ? -10.075 -3.730  -11.892 1.00 19.48  ?  41   ILE A HG23   1 
ATOM   632   H HD11   . ILE A 1 41  ? -14.053 -3.851  -12.375 1.00 24.93  ?  41   ILE A HD11   1 
ATOM   633   H HD12   . ILE A 1 41  ? -13.434 -5.283  -12.673 1.00 24.93  ?  41   ILE A HD12   1 
ATOM   634   H HD13   . ILE A 1 41  ? -12.838 -4.389  -11.503 1.00 24.93  ?  41   ILE A HD13   1 
ATOM   635   N N      . HIS A 1 42  ? -10.737 -2.602  -16.596 1.00 16.36  ?  42   HIS A N      1 
ATOM   636   C CA     . HIS A 1 42  ? -11.515 -2.325  -17.794 1.00 18.23  ?  42   HIS A CA     1 
ATOM   637   C C      . HIS A 1 42  ? -10.651 -2.375  -19.046 1.00 18.22  ?  42   HIS A C      1 
ATOM   638   O O      . HIS A 1 42  ? -9.483  -1.960  -19.024 1.00 17.24  ?  42   HIS A O      1 
ATOM   639   C CB     . HIS A 1 42  ? -12.157 -0.924  -17.712 1.00 19.64  ?  42   HIS A CB     1 
ATOM   640   C CG     . HIS A 1 42  ? -13.094 -0.743  -16.560 1.00 22.73  ?  42   HIS A CG     1 
ATOM   641   N ND1    . HIS A 1 42  ? -12.695 -0.190  -15.364 1.00 27.41  ?  42   HIS A ND1    1 
ATOM   642   C CD2    . HIS A 1 42  ? -14.409 -1.026  -16.423 1.00 24.69  ?  42   HIS A CD2    1 
ATOM   643   C CE1    . HIS A 1 42  ? -13.723 -0.154  -14.533 1.00 26.59  ?  42   HIS A CE1    1 
ATOM   644   N NE2    . HIS A 1 42  ? -14.777 -0.649  -15.154 1.00 25.10  ?  42   HIS A NE2    1 
ATOM   645   H H      . HIS A 1 42  ? -10.216 -1.959  -16.361 1.00 19.62  ?  42   HIS A H      1 
ATOM   646   H HA     . HIS A 1 42  ? -12.202 -3.006  -17.871 1.00 21.88  ?  42   HIS A HA     1 
ATOM   647   H HB2    . HIS A 1 42  ? -11.451 -0.265  -17.624 1.00 23.57  ?  42   HIS A HB2    1 
ATOM   648   H HB3    . HIS A 1 42  ? -12.659 -0.765  -18.527 1.00 23.57  ?  42   HIS A HB3    1 
ATOM   649   H HD1    . HIS A 1 42  ? -11.902 0.089   -15.185 1.00 32.89  ?  42   HIS A HD1    1 
ATOM   650   H HD2    . HIS A 1 42  ? -14.962 -1.406  -17.067 1.00 29.62  ?  42   HIS A HD2    1 
ATOM   651   H HE1    . HIS A 1 42  ? -13.705 0.165   -13.659 1.00 31.90  ?  42   HIS A HE1    1 
ATOM   652   N N      A VAL A 1 43  ? -11.228 -2.896  -20.125 0.67 17.30  ?  43   VAL A N      1 
ATOM   653   N N      B VAL A 1 43  ? -11.244 -2.867  -20.136 0.33 17.01  ?  43   VAL A N      1 
ATOM   654   C CA     A VAL A 1 43  ? -10.634 -2.834  -21.454 0.67 17.46  ?  43   VAL A CA     1 
ATOM   655   C CA     B VAL A 1 43  ? -10.648 -2.859  -21.467 0.33 16.17  ?  43   VAL A CA     1 
ATOM   656   C C      A VAL A 1 43  ? -11.619 -2.133  -22.374 0.67 18.62  ?  43   VAL A C      1 
ATOM   657   C C      B VAL A 1 43  ? -11.626 -2.155  -22.396 0.33 17.30  ?  43   VAL A C      1 
ATOM   658   O O      A VAL A 1 43  ? -12.837 -2.224  -22.181 0.67 19.53  ?  43   VAL A O      1 
ATOM   659   O O      B VAL A 1 43  ? -12.846 -2.258  -22.227 0.33 17.79  ?  43   VAL A O      1 
ATOM   660   C CB     A VAL A 1 43  ? -10.266 -4.215  -22.036 0.67 19.08  ?  43   VAL A CB     1 
ATOM   661   C CB     B VAL A 1 43  ? -10.363 -4.283  -21.988 0.33 15.68  ?  43   VAL A CB     1 
ATOM   662   C CG1    A VAL A 1 43  ? -9.051  -4.740  -21.367 0.67 20.26  ?  43   VAL A CG1    1 
ATOM   663   C CG1    B VAL A 1 43  ? -9.299  -4.270  -23.090 0.33 11.16  ?  43   VAL A CG1    1 
ATOM   664   C CG2    A VAL A 1 43  ? -11.421 -5.216  -21.923 0.67 16.27  ?  43   VAL A CG2    1 
ATOM   665   C CG2    B VAL A 1 43  ? -9.938  -5.177  -20.871 0.33 17.15  ?  43   VAL A CG2    1 
ATOM   666   H H      A VAL A 1 43  ? -11.986 -3.302  -20.109 0.67 20.76  ?  43   VAL A H      1 
ATOM   667   H H      B VAL A 1 43  ? -12.026 -3.224  -20.125 0.33 20.41  ?  43   VAL A H      1 
ATOM   668   H HA     A VAL A 1 43  ? -9.813  -2.322  -21.392 0.67 20.95  ?  43   VAL A HA     1 
ATOM   669   H HA     B VAL A 1 43  ? -9.807  -2.375  -21.442 0.33 19.40  ?  43   VAL A HA     1 
ATOM   670   H HB     A VAL A 1 43  ? -10.084 -4.105  -22.982 0.67 22.90  ?  43   VAL A HB     1 
ATOM   671   H HB     B VAL A 1 43  ? -11.183 -4.634  -22.369 0.33 18.82  ?  43   VAL A HB     1 
ATOM   672   H HG11   A VAL A 1 43  ? -8.835  -5.608  -21.740 0.67 24.31  ?  43   VAL A HG11   1 
ATOM   673   H HG11   B VAL A 1 43  ? -9.143  -5.179  -23.390 0.33 13.39  ?  43   VAL A HG11   1 
ATOM   674   H HG12   A VAL A 1 43  ? -8.317  -4.123  -21.516 0.67 24.31  ?  43   VAL A HG12   1 
ATOM   675   H HG12   B VAL A 1 43  ? -9.616  -3.727  -23.828 0.33 13.39  ?  43   VAL A HG12   1 
ATOM   676   H HG13   A VAL A 1 43  ? -9.225  -4.822  -20.416 0.67 24.31  ?  43   VAL A HG13   1 
ATOM   677   H HG13   B VAL A 1 43  ? -8.479  -3.894  -22.732 0.33 13.39  ?  43   VAL A HG13   1 
ATOM   678   H HG21   A VAL A 1 43  ? -11.135 -6.070  -22.285 0.67 19.52  ?  43   VAL A HG21   1 
ATOM   679   H HG21   B VAL A 1 43  ? -9.747  -6.059  -21.227 0.33 20.58  ?  43   VAL A HG21   1 
ATOM   680   H HG22   A VAL A 1 43  ? -11.661 -5.317  -20.989 0.67 19.52  ?  43   VAL A HG22   1 
ATOM   681   H HG22   B VAL A 1 43  ? -9.142  -4.808  -20.456 0.33 20.58  ?  43   VAL A HG22   1 
ATOM   682   H HG23   A VAL A 1 43  ? -12.179 -4.881  -22.425 0.67 19.52  ?  43   VAL A HG23   1 
ATOM   683   H HG23   B VAL A 1 43  ? -10.655 -5.231  -20.220 0.33 20.58  ?  43   VAL A HG23   1 
ATOM   684   N N      . VAL A 1 44  ? -11.087 -1.452  -23.391 1.00 16.58  ?  44   VAL A N      1 
ATOM   685   C CA     . VAL A 1 44  ? -11.876 -0.588  -24.264 1.00 18.02  ?  44   VAL A CA     1 
ATOM   686   C C      . VAL A 1 44  ? -11.611 -0.954  -25.720 1.00 17.79  ?  44   VAL A C      1 
ATOM   687   O O      . VAL A 1 44  ? -10.459 -1.127  -26.123 1.00 18.17  ?  44   VAL A O      1 
ATOM   688   C CB     . VAL A 1 44  ? -11.520 0.892   -24.019 1.00 20.73  ?  44   VAL A CB     1 
ATOM   689   C CG1    . VAL A 1 44  ? -12.402 1.809   -24.848 1.00 20.85  ?  44   VAL A CG1    1 
ATOM   690   C CG2    . VAL A 1 44  ? -11.654 1.219   -22.532 1.00 22.52  ?  44   VAL A CG2    1 
ATOM   691   H H      A VAL A 1 44  ? -10.253 -1.478  -23.596 0.67 19.89  ?  44   VAL A H      1 
ATOM   692   H H      B VAL A 1 44  ? -10.249 -1.462  -23.582 0.33 19.89  ?  44   VAL A H      1 
ATOM   693   H HA     . VAL A 1 44  ? -12.819 -0.737  -24.094 1.00 21.62  ?  44   VAL A HA     1 
ATOM   694   H HB     . VAL A 1 44  ? -10.602 1.044   -24.291 1.00 24.87  ?  44   VAL A HB     1 
ATOM   695   H HG11   . VAL A 1 44  ? -12.244 2.727   -24.579 1.00 25.02  ?  44   VAL A HG11   1 
ATOM   696   H HG12   . VAL A 1 44  ? -12.180 1.696   -25.786 1.00 25.02  ?  44   VAL A HG12   1 
ATOM   697   H HG13   . VAL A 1 44  ? -13.331 1.574   -24.698 1.00 25.02  ?  44   VAL A HG13   1 
ATOM   698   H HG21   . VAL A 1 44  ? -11.517 2.171   -22.405 1.00 27.02  ?  44   VAL A HG21   1 
ATOM   699   H HG22   . VAL A 1 44  ? -12.542 0.969   -22.233 1.00 27.02  ?  44   VAL A HG22   1 
ATOM   700   H HG23   . VAL A 1 44  ? -10.986 0.719   -22.038 1.00 27.02  ?  44   VAL A HG23   1 
ATOM   701   N N      . ASP A 1 45  ? -12.674 -1.070  -26.514 1.00 18.39  ?  45   ASP A N      1 
ATOM   702   C CA     . ASP A 1 45  ? -12.523 -1.407  -27.915 1.00 17.35  ?  45   ASP A CA     1 
ATOM   703   C C      . ASP A 1 45  ? -12.358 -0.140  -28.747 1.00 18.33  ?  45   ASP A C      1 
ATOM   704   O O      . ASP A 1 45  ? -12.365 0.982   -28.230 1.00 19.36  ?  45   ASP A O      1 
ATOM   705   C CB     . ASP A 1 45  ? -13.632 -2.344  -28.407 1.00 17.62  ?  45   ASP A CB     1 
ATOM   706   C CG     . ASP A 1 45  ? -14.953 -1.656  -28.681 1.00 19.73  ?  45   ASP A CG     1 
ATOM   707   O OD1    . ASP A 1 45  ? -15.033 -0.408  -28.699 1.00 19.21  ?  45   ASP A OD1    1 
ATOM   708   O OD2    . ASP A 1 45  ? -15.934 -2.411  -28.884 1.00 20.30  -1 45   ASP A OD2    1 
ATOM   709   H H      . ASP A 1 45  ? -13.487 -0.957  -26.259 1.00 22.07  ?  45   ASP A H      1 
ATOM   710   H HA     . ASP A 1 45  ? -11.705 -1.917  -28.022 1.00 20.81  ?  45   ASP A HA     1 
ATOM   711   H HB2    . ASP A 1 45  ? -13.342 -2.761  -29.233 1.00 21.14  ?  45   ASP A HB2    1 
ATOM   712   H HB3    . ASP A 1 45  ? -13.789 -3.021  -27.730 1.00 21.14  ?  45   ASP A HB3    1 
ATOM   713   N N      . LYS A 1 46  ? -12.199 -0.323  -30.056 1.00 18.20  ?  46   LYS A N      1 
ATOM   714   C CA     . LYS A 1 46  ? -11.902 0.793   -30.953 1.00 19.75  ?  46   LYS A CA     1 
ATOM   715   C C      . LYS A 1 46  ? -13.030 1.810   -31.003 1.00 23.33  ?  46   LYS A C      1 
ATOM   716   O O      . LYS A 1 46  ? -12.770 2.970   -31.340 1.00 25.56  ?  46   LYS A O      1 
ATOM   717   C CB     . LYS A 1 46  ? -11.588 0.223   -32.343 1.00 21.97  ?  46   LYS A CB     1 
ATOM   718   C CG     . LYS A 1 46  ? -11.317 1.244   -33.415 1.00 24.06  ?  46   LYS A CG     1 
ATOM   719   C CD     . LYS A 1 46  ? -10.007 1.997   -33.200 1.00 26.23  ?  46   LYS A CD     1 
ATOM   720   C CE     . LYS A 1 46  ? -9.804  3.038   -34.295 1.00 28.94  ?  46   LYS A CE     1 
ATOM   721   N NZ     . LYS A 1 46  ? -8.489  3.714   -34.193 1.00 32.95  ?  46   LYS A NZ     1 
ATOM   722   H H      . LYS A 1 46  ? -12.257 -1.084  -30.453 1.00 21.83  ?  46   LYS A H      1 
ATOM   723   H HA     . LYS A 1 46  ? -11.121 1.279   -30.644 1.00 23.69  ?  46   LYS A HA     1 
ATOM   724   H HB2    . LYS A 1 46  ? -10.799 -0.338  -32.271 1.00 26.36  ?  46   LYS A HB2    1 
ATOM   725   H HB3    . LYS A 1 46  ? -12.346 -0.307  -32.633 1.00 26.36  ?  46   LYS A HB3    1 
ATOM   726   H HG2    . LYS A 1 46  ? -11.266 0.795   -34.273 1.00 28.86  ?  46   LYS A HG2    1 
ATOM   727   H HG3    . LYS A 1 46  ? -12.037 1.893   -33.422 1.00 28.86  ?  46   LYS A HG3    1 
ATOM   728   H HD2    . LYS A 1 46  ? -10.030 2.450   -32.343 1.00 31.48  ?  46   LYS A HD2    1 
ATOM   729   H HD3    . LYS A 1 46  ? -9.266  1.372   -33.226 1.00 31.48  ?  46   LYS A HD3    1 
ATOM   730   H HE2    . LYS A 1 46  ? -9.852  2.603   -35.160 1.00 34.73  ?  46   LYS A HE2    1 
ATOM   731   H HE3    . LYS A 1 46  ? -10.496 3.714   -34.223 1.00 34.73  ?  46   LYS A HE3    1 
ATOM   732   H HZ1    . LYS A 1 46  ? -8.397  4.302   -34.854 1.00 39.53  ?  46   LYS A HZ1    1 
ATOM   733   H HZ2    . LYS A 1 46  ? -8.426  4.142   -33.415 1.00 39.53  ?  46   LYS A HZ2    1 
ATOM   734   H HZ3    . LYS A 1 46  ? -7.833  3.114   -34.246 1.00 39.53  ?  46   LYS A HZ3    1 
ATOM   735   N N      . ASP A 1 47  ? -14.262 1.418   -30.673 1.00 22.42  ?  47   ASP A N      1 
ATOM   736   C CA     . ASP A 1 47  ? -15.364 2.365   -30.639 1.00 23.68  ?  47   ASP A CA     1 
ATOM   737   C C      . ASP A 1 47  ? -15.445 3.124   -29.323 1.00 24.65  ?  47   ASP A C      1 
ATOM   738   O O      . ASP A 1 47  ? -16.297 4.016   -29.183 1.00 26.95  ?  47   ASP A O      1 
ATOM   739   C CB     . ASP A 1 47  ? -16.707 1.650   -30.828 1.00 25.40  ?  47   ASP A CB     1 
ATOM   740   C CG     . ASP A 1 47  ? -16.951 1.208   -32.252 1.00 25.98  ?  47   ASP A CG     1 
ATOM   741   O OD1    . ASP A 1 47  ? -16.786 2.021   -33.176 1.00 28.35  ?  47   ASP A OD1    1 
ATOM   742   O OD2    . ASP A 1 47  ? -17.319 0.032   -32.439 1.00 25.80  -1 47   ASP A OD2    1 
ATOM   743   H H      . ASP A 1 47  ? -14.480 0.611   -30.466 1.00 26.90  ?  47   ASP A H      1 
ATOM   744   H HA     . ASP A 1 47  ? -15.231 2.986   -31.372 1.00 28.42  ?  47   ASP A HA     1 
ATOM   745   H HB2    . ASP A 1 47  ? -16.726 0.862   -30.263 1.00 30.48  ?  47   ASP A HB2    1 
ATOM   746   H HB3    . ASP A 1 47  ? -17.423 2.255   -30.578 1.00 30.48  ?  47   ASP A HB3    1 
ATOM   747   N N      . GLY A 1 48  ? -14.612 2.783   -28.353 1.00 23.28  ?  48   GLY A N      1 
ATOM   748   C CA     . GLY A 1 48  ? -14.723 3.343   -27.032 1.00 23.36  ?  48   GLY A CA     1 
ATOM   749   C C      . GLY A 1 48  ? -15.640 2.585   -26.103 1.00 22.66  ?  48   GLY A C      1 
ATOM   750   O O      . GLY A 1 48  ? -15.908 3.069   -24.994 1.00 24.32  ?  48   GLY A O      1 
ATOM   751   H H      . GLY A 1 48  ? -13.967 2.221   -28.443 1.00 27.93  ?  48   GLY A H      1 
ATOM   752   H HA2    . GLY A 1 48  ? -13.842 3.365   -26.628 1.00 28.03  ?  48   GLY A HA2    1 
ATOM   753   H HA3    . GLY A 1 48  ? -15.059 4.250   -27.106 1.00 28.03  ?  48   GLY A HA3    1 
ATOM   754   N N      . ARG A 1 49  ? -16.121 1.414   -26.516 1.00 20.42  ?  49   ARG A N      1 
ATOM   755   C CA     . ARG A 1 49  ? -16.986 0.612   -25.666 1.00 19.56  ?  49   ARG A CA     1 
ATOM   756   C C      . ARG A 1 49  ? -16.155 -0.038  -24.559 1.00 18.41  ?  49   ARG A C      1 
ATOM   757   O O      . ARG A 1 49  ? -15.161 -0.714  -24.824 1.00 20.31  ?  49   ARG A O      1 
ATOM   758   C CB     . ARG A 1 49  ? -17.688 -0.444  -26.516 1.00 20.79  ?  49   ARG A CB     1 
ATOM   759   C CG     . ARG A 1 49  ? -18.728 -1.217  -25.781 1.00 22.32  ?  49   ARG A CG     1 
ATOM   760   C CD     . ARG A 1 49  ? -19.511 -2.136  -26.699 1.00 23.88  ?  49   ARG A CD     1 
ATOM   761   N NE     . ARG A 1 49  ? -20.304 -3.074  -25.913 1.00 26.69  ?  49   ARG A NE     1 
ATOM   762   C CZ     . ARG A 1 49  ? -20.815 -4.212  -26.377 1.00 28.42  ?  49   ARG A CZ     1 
ATOM   763   N NH1    . ARG A 1 49  ? -20.638 -4.558  -27.643 1.00 29.48  ?  49   ARG A NH1    1 
ATOM   764   N NH2    . ARG A 1 49  ? -21.502 -5.002  -25.563 1.00 29.38  ?  49   ARG A NH2    1 
ATOM   765   H H      . ARG A 1 49  ? -15.961 1.063   -27.285 1.00 24.50  ?  49   ARG A H      1 
ATOM   766   H HA     . ARG A 1 49  ? -17.665 1.164   -25.248 1.00 23.47  ?  49   ARG A HA     1 
ATOM   767   H HB2    . ARG A 1 49  ? -18.121 -0.004  -27.264 1.00 24.95  ?  49   ARG A HB2    1 
ATOM   768   H HB3    . ARG A 1 49  ? -17.026 -1.074  -26.840 1.00 24.95  ?  49   ARG A HB3    1 
ATOM   769   H HG2    . ARG A 1 49  ? -18.299 -1.762  -25.102 1.00 26.78  ?  49   ARG A HG2    1 
ATOM   770   H HG3    . ARG A 1 49  ? -19.351 -0.600  -25.367 1.00 26.78  ?  49   ARG A HG3    1 
ATOM   771   H HD2    . ARG A 1 49  ? -20.110 -1.611  -27.253 1.00 28.65  ?  49   ARG A HD2    1 
ATOM   772   H HD3    . ARG A 1 49  ? -18.898 -2.639  -27.258 1.00 28.65  ?  49   ARG A HD3    1 
ATOM   773   H HE     . ARG A 1 49  ? -20.451 -2.878  -25.089 1.00 32.02  ?  49   ARG A HE     1 
ATOM   774   H HH11   . ARG A 1 49  ? -20.190 -4.047  -28.170 1.00 35.37  ?  49   ARG A HH11   1 
ATOM   775   H HH12   . ARG A 1 49  ? -20.971 -5.294  -27.938 1.00 35.37  ?  49   ARG A HH12   1 
ATOM   776   H HH21   . ARG A 1 49  ? -21.615 -4.778  -24.740 1.00 35.25  ?  49   ARG A HH21   1 
ATOM   777   H HH22   . ARG A 1 49  ? -21.835 -5.738  -25.857 1.00 35.25  ?  49   ARG A HH22   1 
ATOM   778   N N      . GLU A 1 50  ? -16.570 0.170   -23.318 1.00 21.40  ?  50   GLU A N      1 
ATOM   779   C CA     . GLU A 1 50  ? -15.779 -0.232  -22.165 1.00 20.05  ?  50   GLU A CA     1 
ATOM   780   C C      . GLU A 1 50  ? -16.360 -1.484  -21.514 1.00 20.35  ?  50   GLU A C      1 
ATOM   781   O O      . GLU A 1 50  ? -17.570 -1.553  -21.247 1.00 20.28  ?  50   GLU A O      1 
ATOM   782   C CB     . GLU A 1 50  ? -15.712 0.913   -21.147 1.00 20.62  ?  50   GLU A CB     1 
ATOM   783   C CG     . GLU A 1 50  ? -14.824 0.588   -19.969 1.00 24.41  ?  50   GLU A CG     1 
ATOM   784   C CD     . GLU A 1 50  ? -14.508 1.802   -19.127 1.00 29.02  ?  50   GLU A CD     1 
ATOM   785   O OE1    . GLU A 1 50  ? -15.402 2.289   -18.415 1.00 28.49  ?  50   GLU A OE1    1 
ATOM   786   O OE2    . GLU A 1 50  ? -13.358 2.284   -19.199 1.00 32.82  -1 50   GLU A OE2    1 
ATOM   787   H H      . GLU A 1 50  ? -17.316 0.547   -23.118 1.00 25.67  ?  50   GLU A H      1 
ATOM   788   H HA     . GLU A 1 50  ? -14.882 -0.453  -22.459 1.00 24.05  ?  50   GLU A HA     1 
ATOM   789   H HB2    . GLU A 1 50  ? -15.358 1.703   -21.583 1.00 24.74  ?  50   GLU A HB2    1 
ATOM   790   H HB3    . GLU A 1 50  ? -16.605 1.091   -20.811 1.00 24.74  ?  50   GLU A HB3    1 
ATOM   791   H HG2    . GLU A 1 50  ? -15.273 -0.061  -19.404 1.00 29.29  ?  50   GLU A HG2    1 
ATOM   792   H HG3    . GLU A 1 50  ? -13.987 0.222   -20.295 1.00 29.29  ?  50   GLU A HG3    1 
ATOM   793   N N      . PHE A 1 51  ? -15.491 -2.460  -21.247 1.00 18.32  ?  51   PHE A N      1 
ATOM   794   C CA     . PHE A 1 51  ? -15.875 -3.722  -20.638 1.00 16.68  ?  51   PHE A CA     1 
ATOM   795   C C      . PHE A 1 51  ? -15.150 -3.914  -19.311 1.00 15.50  ?  51   PHE A C      1 
ATOM   796   O O      . PHE A 1 51  ? -13.970 -3.578  -19.184 1.00 17.33  ?  51   PHE A O      1 
ATOM   797   C CB     . PHE A 1 51  ? -15.499 -4.904  -21.548 1.00 15.87  ?  51   PHE A CB     1 
ATOM   798   C CG     . PHE A 1 51  ? -16.198 -4.889  -22.877 1.00 18.19  ?  51   PHE A CG     1 
ATOM   799   C CD1    . PHE A 1 51  ? -15.678 -4.178  -23.936 1.00 18.79  ?  51   PHE A CD1    1 
ATOM   800   C CD2    . PHE A 1 51  ? -17.384 -5.571  -23.063 1.00 18.88  ?  51   PHE A CD2    1 
ATOM   801   C CE1    . PHE A 1 51  ? -16.312 -4.167  -25.145 1.00 19.10  ?  51   PHE A CE1    1 
ATOM   802   C CE2    . PHE A 1 51  ? -18.028 -5.531  -24.272 1.00 20.13  ?  51   PHE A CE2    1 
ATOM   803   C CZ     . PHE A 1 51  ? -17.483 -4.821  -25.311 1.00 19.70  ?  51   PHE A CZ     1 
ATOM   804   H H      . PHE A 1 51  ? -14.650 -2.406  -21.418 1.00 21.98  ?  51   PHE A H      1 
ATOM   805   H HA     . PHE A 1 51  ? -16.832 -3.709  -20.480 1.00 20.02  ?  51   PHE A HA     1 
ATOM   806   H HB2    . PHE A 1 51  ? -14.544 -4.878  -21.715 1.00 19.04  ?  51   PHE A HB2    1 
ATOM   807   H HB3    . PHE A 1 51  ? -15.735 -5.731  -21.099 1.00 19.04  ?  51   PHE A HB3    1 
ATOM   808   H HD1    . PHE A 1 51  ? -14.888 -3.701  -23.826 1.00 22.55  ?  51   PHE A HD1    1 
ATOM   809   H HD2    . PHE A 1 51  ? -17.749 -6.062  -22.363 1.00 22.66  ?  51   PHE A HD2    1 
ATOM   810   H HE1    . PHE A 1 51  ? -15.935 -3.707  -25.860 1.00 22.92  ?  51   PHE A HE1    1 
ATOM   811   H HE2    . PHE A 1 51  ? -18.832 -5.983  -24.387 1.00 24.15  ?  51   PHE A HE2    1 
ATOM   812   H HZ     . PHE A 1 51  ? -17.921 -4.789  -26.131 1.00 23.64  ?  51   PHE A HZ     1 
ATOM   813   N N      . ILE A 1 52  ? -15.862 -4.448  -18.322 1.00 16.10  ?  52   ILE A N      1 
ATOM   814   C CA     . ILE A 1 52  ? -15.185 -5.051  -17.181 1.00 17.22  ?  52   ILE A CA     1 
ATOM   815   C C      . ILE A 1 52  ? -14.601 -6.374  -17.659 1.00 16.30  ?  52   ILE A C      1 
ATOM   816   O O      . ILE A 1 52  ? -15.338 -7.241  -18.150 1.00 15.78  ?  52   ILE A O      1 
ATOM   817   C CB     . ILE A 1 52  ? -16.159 -5.283  -16.027 1.00 18.25  ?  52   ILE A CB     1 
ATOM   818   C CG1    . ILE A 1 52  ? -16.655 -3.966  -15.439 1.00 19.21  ?  52   ILE A CG1    1 
ATOM   819   C CG2    . ILE A 1 52  ? -15.473 -6.105  -14.945 1.00 19.16  ?  52   ILE A CG2    1 
ATOM   820   C CD1    . ILE A 1 52  ? -17.791 -4.121  -14.427 1.00 20.70  ?  52   ILE A CD1    1 
ATOM   821   H H      . ILE A 1 52  ? -16.721 -4.474  -18.288 1.00 19.31  ?  52   ILE A H      1 
ATOM   822   H HA     . ILE A 1 52  ? -14.477 -4.467  -16.867 1.00 20.66  ?  52   ILE A HA     1 
ATOM   823   H HB     . ILE A 1 52  ? -16.928 -5.762  -16.374 1.00 21.90  ?  52   ILE A HB     1 
ATOM   824   H HG12   . ILE A 1 52  ? -15.916 -3.530  -14.988 1.00 23.05  ?  52   ILE A HG12   1 
ATOM   825   H HG13   . ILE A 1 52  ? -16.979 -3.406  -16.162 1.00 23.05  ?  52   ILE A HG13   1 
ATOM   826   H HG21   . ILE A 1 52  ? -16.048 -6.141  -14.164 1.00 22.99  ?  52   ILE A HG21   1 
ATOM   827   H HG22   . ILE A 1 52  ? -15.314 -7.000  -15.281 1.00 22.99  ?  52   ILE A HG22   1 
ATOM   828   H HG23   . ILE A 1 52  ? -14.630 -5.683  -14.715 1.00 22.99  ?  52   ILE A HG23   1 
ATOM   829   H HD11   . ILE A 1 52  ? -18.204 -3.256  -14.282 1.00 24.83  ?  52   ILE A HD11   1 
ATOM   830   H HD12   . ILE A 1 52  ? -18.445 -4.745  -14.780 1.00 24.83  ?  52   ILE A HD12   1 
ATOM   831   H HD13   . ILE A 1 52  ? -17.427 -4.459  -13.594 1.00 24.83  ?  52   ILE A HD13   1 
ATOM   832   N N      . ASP A 1 53  ? -13.283 -6.529  -17.539 1.00 15.38  ?  53   ASP A N      1 
ATOM   833   C CA     . ASP A 1 53  ? -12.638 -7.760  -17.979 1.00 15.16  ?  53   ASP A CA     1 
ATOM   834   C C      . ASP A 1 53  ? -12.573 -8.714  -16.804 1.00 15.02  ?  53   ASP A C      1 
ATOM   835   O O      . ASP A 1 53  ? -11.603 -8.729  -16.043 1.00 14.99  ?  53   ASP A O      1 
ATOM   836   C CB     . ASP A 1 53  ? -11.251 -7.525  -18.551 1.00 14.54  ?  53   ASP A CB     1 
ATOM   837   C CG     . ASP A 1 53  ? -10.655 -8.802  -19.127 1.00 13.30  ?  53   ASP A CG     1 
ATOM   838   O OD1    . ASP A 1 53  ? -11.378 -9.829  -19.144 1.00 14.59  ?  53   ASP A OD1    1 
ATOM   839   O OD2    . ASP A 1 53  ? -9.472  -8.766  -19.579 1.00 13.75  -1 53   ASP A OD2    1 
ATOM   840   H H      . ASP A 1 53  ? -12.750 -5.939  -17.210 1.00 18.45  ?  53   ASP A H      1 
ATOM   841   H HA     . ASP A 1 53  ? -13.191 -8.140  -18.680 1.00 18.19  ?  53   ASP A HA     1 
ATOM   842   H HB2    . ASP A 1 53  ? -11.305 -6.868  -19.262 1.00 17.44  ?  53   ASP A HB2    1 
ATOM   843   H HB3    . ASP A 1 53  ? -10.664 -7.205  -17.848 1.00 17.44  ?  53   ASP A HB3    1 
ATOM   844   N N      . GLY A 1 54  ? -13.621 -9.524  -16.672 1.00 14.38  ?  54   GLY A N      1 
ATOM   845   C CA     . GLY A 1 54  ? -13.674 -10.525 -15.640 1.00 14.59  ?  54   GLY A CA     1 
ATOM   846   C C      . GLY A 1 54  ? -12.745 -11.698 -15.835 1.00 14.81  ?  54   GLY A C      1 
ATOM   847   O O      . GLY A 1 54  ? -12.758 -12.591 -14.987 1.00 15.09  ?  54   GLY A O      1 
ATOM   848   H H      . GLY A 1 54  ? -14.316 -9.505  -17.178 1.00 17.25  ?  54   GLY A H      1 
ATOM   849   H HA2    . GLY A 1 54  ? -13.449 -10.108 -14.794 1.00 17.51  ?  54   GLY A HA2    1 
ATOM   850   H HA3    . GLY A 1 54  ? -14.579 -10.871 -15.591 1.00 17.51  ?  54   GLY A HA3    1 
ATOM   851   N N      . PHE A 1 55  ? -11.912 -11.695 -16.886 1.00 13.54  ?  55   PHE A N      1 
ATOM   852   C CA     . PHE A 1 55  ? -10.967 -12.781 -17.147 1.00 12.21  ?  55   PHE A CA     1 
ATOM   853   C C      . PHE A 1 55  ? -9.520  -12.305 -17.232 1.00 11.98  ?  55   PHE A C      1 
ATOM   854   O O      . PHE A 1 55  ? -8.635  -13.118 -17.513 1.00 13.72  ?  55   PHE A O      1 
ATOM   855   C CB     . PHE A 1 55  ? -11.357 -13.547 -18.420 1.00 13.42  ?  55   PHE A CB     1 
ATOM   856   C CG     . PHE A 1 55  ? -11.150 -15.036 -18.304 1.00 13.65  ?  55   PHE A CG     1 
ATOM   857   C CD1    . PHE A 1 55  ? -11.938 -15.806 -17.460 1.00 13.62  ?  55   PHE A CD1    1 
ATOM   858   C CD2    . PHE A 1 55  ? -10.155 -15.669 -19.038 1.00 15.01  ?  55   PHE A CD2    1 
ATOM   859   C CE1    . PHE A 1 55  ? -11.725 -17.176 -17.344 1.00 14.84  ?  55   PHE A CE1    1 
ATOM   860   C CE2    . PHE A 1 55  ? -9.950  -17.021 -18.927 1.00 14.85  ?  55   PHE A CE2    1 
ATOM   861   C CZ     . PHE A 1 55  ? -10.738 -17.777 -18.077 1.00 14.19  ?  55   PHE A CZ     1 
ATOM   862   H H      . PHE A 1 55  ? -11.878 -11.063 -17.468 1.00 16.24  ?  55   PHE A H      1 
ATOM   863   H HA     . PHE A 1 55  ? -11.016 -13.417 -16.416 1.00 14.65  ?  55   PHE A HA     1 
ATOM   864   H HB2    . PHE A 1 55  ? -12.296 -13.390 -18.605 1.00 16.10  ?  55   PHE A HB2    1 
ATOM   865   H HB3    . PHE A 1 55  ? -10.815 -13.227 -19.158 1.00 16.10  ?  55   PHE A HB3    1 
ATOM   866   H HD1    . PHE A 1 55  ? -12.615 -15.402 -16.967 1.00 16.34  ?  55   PHE A HD1    1 
ATOM   867   H HD2    . PHE A 1 55  ? -9.620  -15.170 -19.613 1.00 18.01  ?  55   PHE A HD2    1 
ATOM   868   H HE1    . PHE A 1 55  ? -12.252 -17.683 -16.770 1.00 17.81  ?  55   PHE A HE1    1 
ATOM   869   H HE2    . PHE A 1 55  ? -9.279  -17.431 -19.424 1.00 17.82  ?  55   PHE A HE2    1 
ATOM   870   H HZ     . PHE A 1 55  ? -10.597 -18.694 -18.003 1.00 17.03  ?  55   PHE A HZ     1 
ATOM   871   N N      . ALA A 1 56  ? -9.262  -11.014 -17.006 1.00 13.97  ?  56   ALA A N      1 
ATOM   872   C CA     . ALA A 1 56  ? -7.899  -10.472 -17.004 1.00 14.52  ?  56   ALA A CA     1 
ATOM   873   C C      . ALA A 1 56  ? -7.113  -10.949 -18.226 1.00 14.14  ?  56   ALA A C      1 
ATOM   874   O O      . ALA A 1 56  ? -5.993  -11.466 -18.122 1.00 13.31  ?  56   ALA A O      1 
ATOM   875   C CB     . ALA A 1 56  ? -7.168  -10.831 -15.711 1.00 15.00  ?  56   ALA A CB     1 
ATOM   876   H H      . ALA A 1 56  ? -9.868  -10.424 -16.849 1.00 16.76  ?  56   ALA A H      1 
ATOM   877   H HA     . ALA A 1 56  ? -7.959  -9.506  -17.056 1.00 17.42  ?  56   ALA A HA     1 
ATOM   878   H HB1    . ALA A 1 56  ? -6.310  -10.379 -15.698 1.00 18.00  ?  56   ALA A HB1    1 
ATOM   879   H HB2    . ALA A 1 56  ? -7.704  -10.546 -14.956 1.00 18.00  ?  56   ALA A HB2    1 
ATOM   880   H HB3    . ALA A 1 56  ? -7.035  -11.792 -15.679 1.00 18.00  ?  56   ALA A HB3    1 
ATOM   881   N N      . GLY A 1 57  ? -7.673  -10.706 -19.404 1.00 13.00  ?  57   GLY A N      1 
ATOM   882   C CA     . GLY A 1 57  ? -7.063  -11.223 -20.618 1.00 13.56  ?  57   GLY A CA     1 
ATOM   883   C C      . GLY A 1 57  ? -7.332  -12.711 -20.715 1.00 12.49  ?  57   GLY A C      1 
ATOM   884   O O      . GLY A 1 57  ? -8.442  -13.129 -21.043 1.00 12.54  ?  57   GLY A O      1 
ATOM   885   H H      . GLY A 1 57  ? -8.393  -10.253 -19.525 1.00 15.59  ?  57   GLY A H      1 
ATOM   886   H HA2    . GLY A 1 57  ? -7.438  -10.779 -21.394 1.00 16.27  ?  57   GLY A HA2    1 
ATOM   887   H HA3    . GLY A 1 57  ? -6.105  -11.071 -20.600 1.00 16.27  ?  57   GLY A HA3    1 
ATOM   888   N N      . LEU A 1 58  ? -6.320  -13.494 -20.416 1.00 12.15  ?  58   LEU A N      1 
ATOM   889   C CA     . LEU A 1 58  ? -6.423  -14.943 -20.232 1.00 12.11  ?  58   LEU A CA     1 
ATOM   890   C C      . LEU A 1 58  ? -5.689  -15.258 -18.926 1.00 13.29  ?  58   LEU A C      1 
ATOM   891   O O      . LEU A 1 58  ? -4.541  -15.704 -18.933 1.00 14.82  ?  58   LEU A O      1 
ATOM   892   C CB     . LEU A 1 58  ? -5.825  -15.695 -21.432 1.00 12.89  ?  58   LEU A CB     1 
ATOM   893   C CG     . LEU A 1 58  ? -6.571  -15.493 -22.755 1.00 14.10  ?  58   LEU A CG     1 
ATOM   894   C CD1    . LEU A 1 58  ? -5.758  -16.040 -23.925 1.00 16.06  ?  58   LEU A CD1    1 
ATOM   895   C CD2    . LEU A 1 58  ? -7.948  -16.168 -22.690 1.00 14.99  ?  58   LEU A CD2    1 
ATOM   896   H H      . LEU A 1 58  ? -5.518  -13.202 -20.306 1.00 14.58  ?  58   LEU A H      1 
ATOM   897   H HA     . LEU A 1 58  ? -7.353  -15.209 -20.152 1.00 14.53  ?  58   LEU A HA     1 
ATOM   898   H HB2    . LEU A 1 58  ? -4.913  -15.390 -21.561 1.00 15.47  ?  58   LEU A HB2    1 
ATOM   899   H HB3    . LEU A 1 58  ? -5.832  -16.644 -21.235 1.00 15.47  ?  58   LEU A HB3    1 
ATOM   900   H HG     . LEU A 1 58  ? -6.700  -14.543 -22.904 1.00 16.91  ?  58   LEU A HG     1 
ATOM   901   H HD11   . LEU A 1 58  ? -6.253  -15.897 -24.747 1.00 19.27  ?  58   LEU A HD11   1 
ATOM   902   H HD12   . LEU A 1 58  ? -4.909  -15.573 -23.966 1.00 19.27  ?  58   LEU A HD12   1 
ATOM   903   H HD13   . LEU A 1 58  ? -5.608  -16.988 -23.790 1.00 19.27  ?  58   LEU A HD13   1 
ATOM   904   H HD21   . LEU A 1 58  ? -8.423  -15.995 -23.518 1.00 17.98  ?  58   LEU A HD21   1 
ATOM   905   H HD22   . LEU A 1 58  ? -7.827  -17.122 -22.571 1.00 17.98  ?  58   LEU A HD22   1 
ATOM   906   H HD23   . LEU A 1 58  ? -8.445  -15.801 -21.942 1.00 17.98  ?  58   LEU A HD23   1 
ATOM   907   N N      . TYR A 1 59  ? -6.361  -14.997 -17.806 1.00 13.29  ?  59   TYR A N      1 
ATOM   908   C CA     . TYR A 1 59  ? -5.799  -15.232 -16.474 1.00 13.09  ?  59   TYR A CA     1 
ATOM   909   C C      . TYR A 1 59  ? -4.448  -14.546 -16.306 1.00 13.10  ?  59   TYR A C      1 
ATOM   910   O O      . TYR A 1 59  ? -3.548  -15.088 -15.663 1.00 14.28  ?  59   TYR A O      1 
ATOM   911   C CB     . TYR A 1 59  ? -5.579  -16.721 -16.109 1.00 15.18  ?  59   TYR A CB     1 
ATOM   912   C CG     . TYR A 1 59  ? -6.497  -17.784 -16.635 1.00 15.18  ?  59   TYR A CG     1 
ATOM   913   C CD1    . TYR A 1 59  ? -6.322  -18.312 -17.900 1.00 17.05  ?  59   TYR A CD1    1 
ATOM   914   C CD2    . TYR A 1 59  ? -7.489  -18.347 -15.830 1.00 15.63  ?  59   TYR A CD2    1 
ATOM   915   C CE1    . TYR A 1 59  ? -7.142  -19.288 -18.371 1.00 18.22  ?  59   TYR A CE1    1 
ATOM   916   C CE2    . TYR A 1 59  ? -8.298  -19.328 -16.300 1.00 17.45  ?  59   TYR A CE2    1 
ATOM   917   C CZ     . TYR A 1 59  ? -8.122  -19.814 -17.556 1.00 17.11  ?  59   TYR A CZ     1 
ATOM   918   O OH     . TYR A 1 59  ? -8.953  -20.800 -18.031 1.00 20.87  ?  59   TYR A OH     1 
ATOM   919   H H      . TYR A 1 59  ? -7.159  -14.677 -17.789 1.00 15.95  ?  59   TYR A H      1 
ATOM   920   H HA     . TYR A 1 59  ? -6.469  -14.864 -15.877 1.00 15.71  ?  59   TYR A HA     1 
ATOM   921   H HB2    . TYR A 1 59  ? -4.691  -16.961 -16.417 1.00 18.21  ?  59   TYR A HB2    1 
ATOM   922   H HB3    . TYR A 1 59  ? -5.624  -16.786 -15.142 1.00 18.21  ?  59   TYR A HB3    1 
ATOM   923   H HD1    . TYR A 1 59  ? -5.633  -17.994 -18.438 1.00 20.45  ?  59   TYR A HD1    1 
ATOM   924   H HD2    . TYR A 1 59  ? -7.596  -18.044 -14.957 1.00 18.75  ?  59   TYR A HD2    1 
ATOM   925   H HE1    . TYR A 1 59  ? -7.041  -19.601 -19.241 1.00 21.86  ?  59   TYR A HE1    1 
ATOM   926   H HE2    . TYR A 1 59  ? -8.975  -19.669 -15.761 1.00 20.94  ?  59   TYR A HE2    1 
ATOM   927   H HH     . TYR A 1 59  ? -8.811  -20.926 -18.849 1.00 25.04  ?  59   TYR A HH     1 
ATOM   928   N N      . CYS A 1 60  ? -4.252  -13.374 -16.910 1.00 12.56  ?  60   CYS A N      1 
ATOM   929   C CA     . CYS A 1 60  ? -2.881  -12.888 -16.944 1.00 12.17  ?  60   CYS A CA     1 
ATOM   930   C C      . CYS A 1 60  ? -2.662  -11.399 -16.693 1.00 12.48  ?  60   CYS A C      1 
ATOM   931   O O      . CYS A 1 60  ? -1.541  -11.051 -16.306 1.00 14.45  ?  60   CYS A O      1 
ATOM   932   C CB     . CYS A 1 60  ? -2.184  -13.290 -18.257 1.00 14.38  ?  60   CYS A CB     1 
ATOM   933   S SG     . CYS A 1 60  ? -2.964  -12.704 -19.786 1.00 14.21  ?  60   CYS A SG     1 
ATOM   934   H H      . CYS A 1 60  ? -4.853  -12.881 -17.278 1.00 15.07  ?  60   CYS A H      1 
ATOM   935   H HA     . CYS A 1 60  ? -2.420  -13.334 -16.216 1.00 14.60  ?  60   CYS A HA     1 
ATOM   936   H HB2    . CYS A 1 60  ? -1.281  -12.934 -18.241 1.00 17.26  ?  60   CYS A HB2    1 
ATOM   937   H HB3    . CYS A 1 60  ? -2.158  -14.258 -18.302 1.00 17.26  ?  60   CYS A HB3    1 
ATOM   938   H HG     . CYS A 1 60  ? -2.302  -13.058 -20.722 1.00 17.05  ?  60   CYS A HG     1 
ATOM   939   N N      . VAL A 1 61  ? -3.632  -10.512 -16.895 1.00 13.02  ?  61   VAL A N      1 
ATOM   940   C CA     . VAL A 1 61  ? -3.412  -9.083  -16.665 1.00 13.05  ?  61   VAL A CA     1 
ATOM   941   C C      . VAL A 1 61  ? -3.633  -8.827  -15.178 1.00 14.40  ?  61   VAL A C      1 
ATOM   942   O O      . VAL A 1 61  ? -4.594  -8.158  -14.758 1.00 14.26  ?  61   VAL A O      1 
ATOM   943   C CB     . VAL A 1 61  ? -4.269  -8.203  -17.587 1.00 13.86  ?  61   VAL A CB     1 
ATOM   944   C CG1    . VAL A 1 61  ? -3.891  -6.748  -17.409 1.00 16.67  ?  61   VAL A CG1    1 
ATOM   945   C CG2    . VAL A 1 61  ? -4.097  -8.647  -19.067 1.00 15.06  ?  61   VAL A CG2    1 
ATOM   946   H H      . VAL A 1 61  ? -4.424  -10.710 -17.165 1.00 15.62  ?  61   VAL A H      1 
ATOM   947   H HA     . VAL A 1 61  ? -2.498  -8.839  -16.878 1.00 15.66  ?  61   VAL A HA     1 
ATOM   948   H HB     . VAL A 1 61  ? -5.205  -8.303  -17.353 1.00 16.63  ?  61   VAL A HB     1 
ATOM   949   H HG11   . VAL A 1 61  ? -4.424  -6.207  -18.013 1.00 20.00  ?  61   VAL A HG11   1 
ATOM   950   H HG12   . VAL A 1 61  ? -4.062  -6.487  -16.491 1.00 20.00  ?  61   VAL A HG12   1 
ATOM   951   H HG13   . VAL A 1 61  ? -2.949  -6.640  -17.614 1.00 20.00  ?  61   VAL A HG13   1 
ATOM   952   H HG21   . VAL A 1 61  ? -4.575  -8.027  -19.640 1.00 18.07  ?  61   VAL A HG21   1 
ATOM   953   H HG22   . VAL A 1 61  ? -3.153  -8.643  -19.290 1.00 18.07  ?  61   VAL A HG22   1 
ATOM   954   H HG23   . VAL A 1 61  ? -4.459  -9.541  -19.173 1.00 18.07  ?  61   VAL A HG23   1 
ATOM   955   N N      . ASN A 1 62  ? -2.732  -9.362  -14.365 1.00 14.48  ?  62   ASN A N      1 
ATOM   956   C CA     . ASN A 1 62  ? -3.030  -9.553  -12.951 1.00 13.11  ?  62   ASN A CA     1 
ATOM   957   C C      . ASN A 1 62  ? -2.958  -8.254  -12.176 1.00 13.53  ?  62   ASN A C      1 
ATOM   958   O O      . ASN A 1 62  ? -3.746  -8.059  -11.250 1.00 14.20  ?  62   ASN A O      1 
ATOM   959   C CB     . ASN A 1 62  ? -2.120  -10.639 -12.359 1.00 13.26  ?  62   ASN A CB     1 
ATOM   960   C CG     . ASN A 1 62  ? -2.592  -12.022 -12.732 1.00 13.65  ?  62   ASN A CG     1 
ATOM   961   O OD1    . ASN A 1 62  ? -3.564  -12.155 -13.476 1.00 14.25  ?  62   ASN A OD1    1 
ATOM   962   N ND2    . ASN A 1 62  ? -1.928  -13.039 -12.230 1.00 13.50  ?  62   ASN A ND2    1 
ATOM   963   H H      . ASN A 1 62  ? -1.947  -9.622  -14.602 1.00 17.37  ?  62   ASN A H      1 
ATOM   964   H HA     . ASN A 1 62  ? -3.940  -9.874  -12.859 1.00 15.73  ?  62   ASN A HA     1 
ATOM   965   H HB2    . ASN A 1 62  ? -1.219  -10.522 -12.698 1.00 15.91  ?  62   ASN A HB2    1 
ATOM   966   H HB3    . ASN A 1 62  ? -2.123  -10.567 -11.391 1.00 15.91  ?  62   ASN A HB3    1 
ATOM   967   H HD21   . ASN A 1 62  ? -2.166  -13.843 -12.420 1.00 16.20  ?  62   ASN A HD21   1 
ATOM   968   H HD22   . ASN A 1 62  ? -1.256  -12.900 -11.712 1.00 16.20  ?  62   ASN A HD22   1 
ATOM   969   N N      . ILE A 1 63  ? -2.033  -7.355  -12.537 1.00 14.05  ?  63   ILE A N      1 
ATOM   970   C CA     . ILE A 1 63  ? -1.948  -6.054  -11.882 1.00 13.74  ?  63   ILE A CA     1 
ATOM   971   C C      . ILE A 1 63  ? -2.884  -5.033  -12.507 1.00 15.62  ?  63   ILE A C      1 
ATOM   972   O O      . ILE A 1 63  ? -2.883  -3.867  -12.081 1.00 16.69  ?  63   ILE A O      1 
ATOM   973   C CB     . ILE A 1 63  ? -0.513  -5.477  -11.829 1.00 15.06  ?  63   ILE A CB     1 
ATOM   974   C CG1    . ILE A 1 63  ? 0.023   -5.251  -13.245 1.00 14.96  ?  63   ILE A CG1    1 
ATOM   975   C CG2    . ILE A 1 63  ? 0.392   -6.373  -10.989 1.00 15.60  ?  63   ILE A CG2    1 
ATOM   976   C CD1    . ILE A 1 63  ? 1.404   -4.621  -13.283 1.00 15.13  ?  63   ILE A CD1    1 
ATOM   977   H H      . ILE A 1 63  ? -1.449  -7.478  -13.156 1.00 16.86  ?  63   ILE A H      1 
ATOM   978   H HA     . ILE A 1 63  ? -2.214  -6.205  -10.961 1.00 16.48  ?  63   ILE A HA     1 
ATOM   979   H HB     . ILE A 1 63  ? -0.534  -4.611  -11.394 1.00 18.07  ?  63   ILE A HB     1 
ATOM   980   H HG12   . ILE A 1 63  ? 0.075   -6.106  -13.699 1.00 17.95  ?  63   ILE A HG12   1 
ATOM   981   H HG13   . ILE A 1 63  ? -0.584  -4.660  -13.718 1.00 17.95  ?  63   ILE A HG13   1 
ATOM   982   H HG21   . ILE A 1 63  ? 1.242   -5.926  -10.855 1.00 18.71  ?  63   ILE A HG21   1 
ATOM   983   H HG22   . ILE A 1 63  ? -0.033  -6.538  -10.133 1.00 18.71  ?  63   ILE A HG22   1 
ATOM   984   H HG23   . ILE A 1 63  ? 0.529   -7.211  -11.458 1.00 18.71  ?  63   ILE A HG23   1 
ATOM   985   H HD11   . ILE A 1 63  ? 1.632   -4.415  -14.203 1.00 18.15  ?  63   ILE A HD11   1 
ATOM   986   H HD12   . ILE A 1 63  ? 1.396   -3.808  -12.754 1.00 18.15  ?  63   ILE A HD12   1 
ATOM   987   H HD13   . ILE A 1 63  ? 2.047   -5.248  -12.916 1.00 18.15  ?  63   ILE A HD13   1 
ATOM   988   N N      . GLY A 1 64  ? -3.694  -5.436  -13.486 1.00 15.40  ?  64   GLY A N      1 
ATOM   989   C CA     . GLY A 1 64  ? -4.602  -4.534  -14.168 1.00 15.82  ?  64   GLY A CA     1 
ATOM   990   C C      . GLY A 1 64  ? -3.967  -3.870  -15.375 1.00 14.30  ?  64   GLY A C      1 
ATOM   991   O O      . GLY A 1 64  ? -2.752  -3.951  -15.613 1.00 14.17  ?  64   GLY A O      1 
ATOM   992   H H      . GLY A 1 64  ? -3.731  -6.245  -13.775 1.00 18.47  ?  64   GLY A H      1 
ATOM   993   H HA2    . GLY A 1 64  ? -5.381  -5.029  -14.467 1.00 18.98  ?  64   GLY A HA2    1 
ATOM   994   H HA3    . GLY A 1 64  ? -4.887  -3.840  -13.553 1.00 18.98  ?  64   GLY A HA3    1 
ATOM   995   N N      . TYR A 1 65  ? -4.820  -3.198  -16.148 1.00 14.78  ?  65   TYR A N      1 
ATOM   996   C CA     . TYR A 1 65  ? -4.464  -2.545  -17.393 1.00 14.64  ?  65   TYR A CA     1 
ATOM   997   C C      . TYR A 1 65  ? -3.937  -1.133  -17.168 1.00 16.41  ?  65   TYR A C      1 
ATOM   998   O O      . TYR A 1 65  ? -4.248  -0.466  -16.180 1.00 16.97  ?  65   TYR A O      1 
ATOM   999   C CB     . TYR A 1 65  ? -5.701  -2.451  -18.323 1.00 15.40  ?  65   TYR A CB     1 
ATOM   1000  C CG     . TYR A 1 65  ? -6.176  -3.797  -18.841 1.00 14.43  ?  65   TYR A CG     1 
ATOM   1001  C CD1    . TYR A 1 65  ? -5.622  -4.320  -19.996 1.00 16.53  ?  65   TYR A CD1    1 
ATOM   1002  C CD2    . TYR A 1 65  ? -7.147  -4.544  -18.178 1.00 13.84  ?  65   TYR A CD2    1 
ATOM   1003  C CE1    . TYR A 1 65  ? -6.013  -5.546  -20.484 1.00 16.19  ?  65   TYR A CE1    1 
ATOM   1004  C CE2    . TYR A 1 65  ? -7.533  -5.772  -18.652 1.00 14.35  ?  65   TYR A CE2    1 
ATOM   1005  C CZ     . TYR A 1 65  ? -6.953  -6.267  -19.813 1.00 12.83  ?  65   TYR A CZ     1 
ATOM   1006  O OH     . TYR A 1 65  ? -7.353  -7.492  -20.339 1.00 14.75  ?  65   TYR A OH     1 
ATOM   1007  H H      . TYR A 1 65  ? -5.653  -3.105  -15.956 1.00 17.74  ?  65   TYR A H      1 
ATOM   1008  H HA     . TYR A 1 65  ? -3.765  -3.071  -17.814 1.00 17.57  ?  65   TYR A HA     1 
ATOM   1009  H HB2    . TYR A 1 65  ? -6.432  -2.047  -17.830 1.00 18.48  ?  65   TYR A HB2    1 
ATOM   1010  H HB3    . TYR A 1 65  ? -5.474  -1.902  -19.090 1.00 18.48  ?  65   TYR A HB3    1 
ATOM   1011  H HD1    . TYR A 1 65  ? -4.973  -3.833  -20.450 1.00 19.83  ?  65   TYR A HD1    1 
ATOM   1012  H HD2    . TYR A 1 65  ? -7.538  -4.206  -17.404 1.00 16.60  ?  65   TYR A HD2    1 
ATOM   1013  H HE1    . TYR A 1 65  ? -5.639  -5.880  -21.267 1.00 19.43  ?  65   TYR A HE1    1 
ATOM   1014  H HE2    . TYR A 1 65  ? -8.177  -6.269  -18.200 1.00 17.22  ?  65   TYR A HE2    1 
ATOM   1015  H HH     . TYR A 1 65  ? -7.922  -7.849  -19.834 1.00 17.70  ?  65   TYR A HH     1 
ATOM   1016  N N      . GLY A 1 66  ? -3.148  -0.667  -18.131 1.00 16.29  ?  66   GLY A N      1 
ATOM   1017  C CA     . GLY A 1 66  ? -2.751  0.722   -18.141 1.00 17.18  ?  66   GLY A CA     1 
ATOM   1018  C C      . GLY A 1 66  ? -1.694  1.110   -17.149 1.00 17.96  ?  66   GLY A C      1 
ATOM   1019  O O      . GLY A 1 66  ? -1.652  2.273   -16.718 1.00 19.57  ?  66   GLY A O      1 
ATOM   1020  H H      . GLY A 1 66  ? -2.834  -1.135  -18.782 1.00 19.54  ?  66   GLY A H      1 
ATOM   1021  H HA2    . GLY A 1 66  ? -2.414  0.938   -19.025 1.00 20.62  ?  66   GLY A HA2    1 
ATOM   1022  H HA3    . GLY A 1 66  ? -3.533  1.265   -17.959 1.00 20.62  ?  66   GLY A HA3    1 
ATOM   1023  N N      . ARG A 1 67  ? -0.835  0.169   -16.768 1.00 17.51  ?  67   ARG A N      1 
ATOM   1024  C CA     . ARG A 1 67  ? 0.235   0.443   -15.808 1.00 18.44  ?  67   ARG A CA     1 
ATOM   1025  C C      . ARG A 1 67  ? 1.381   1.187   -16.479 1.00 18.26  ?  67   ARG A C      1 
ATOM   1026  O O      . ARG A 1 67  ? 2.323   0.587   -17.003 1.00 17.09  ?  67   ARG A O      1 
ATOM   1027  C CB     . ARG A 1 67  ? 0.728   -0.851  -15.187 1.00 18.49  ?  67   ARG A CB     1 
ATOM   1028  C CG     . ARG A 1 67  ? -0.272  -1.491  -14.264 1.00 18.34  ?  67   ARG A CG     1 
ATOM   1029  C CD     . ARG A 1 67  ? -0.252  -0.838  -12.895 1.00 19.76  ?  67   ARG A CD     1 
ATOM   1030  N NE     . ARG A 1 67  ? -1.042  -1.611  -11.965 1.00 18.98  ?  67   ARG A NE     1 
ATOM   1031  C CZ     . ARG A 1 67  ? -1.053  -1.417  -10.653 1.00 18.37  ?  67   ARG A CZ     1 
ATOM   1032  N NH1    . ARG A 1 67  ? -0.294  -0.459  -10.108 1.00 18.80  ?  67   ARG A NH1    1 
ATOM   1033  N NH2    . ARG A 1 67  ? -1.821  -2.181  -9.887  1.00 17.69  ?  67   ARG A NH2    1 
ATOM   1034  H H      . ARG A 1 67  ? -0.852  -0.643  -17.052 1.00 21.01  ?  67   ARG A H      1 
ATOM   1035  H HA     . ARG A 1 67  ? -0.125  1.027   -15.122 1.00 22.12  ?  67   ARG A HA     1 
ATOM   1036  H HB2    . ARG A 1 67  ? 0.925   -1.483  -15.896 1.00 22.18  ?  67   ARG A HB2    1 
ATOM   1037  H HB3    . ARG A 1 67  ? 1.531   -0.667  -14.675 1.00 22.18  ?  67   ARG A HB3    1 
ATOM   1038  H HG2    . ARG A 1 67  ? -1.163  -1.393  -14.636 1.00 22.00  ?  67   ARG A HG2    1 
ATOM   1039  H HG3    . ARG A 1 67  ? -0.058  -2.431  -14.158 1.00 22.00  ?  67   ARG A HG3    1 
ATOM   1040  H HD2    . ARG A 1 67  ? 0.660   -0.795  -12.567 1.00 23.71  ?  67   ARG A HD2    1 
ATOM   1041  H HD3    . ARG A 1 67  ? -0.625  0.055   -12.953 1.00 23.71  ?  67   ARG A HD3    1 
ATOM   1042  H HE     . ARG A 1 67  ? -1.537  -2.238  -12.283 1.00 22.78  ?  67   ARG A HE     1 
ATOM   1043  H HH11   . ARG A 1 67  ? 0.202   0.033   -10.609 1.00 22.55  ?  67   ARG A HH11   1 
ATOM   1044  H HH12   . ARG A 1 67  ? -0.304  -0.335  -9.257  1.00 22.55  ?  67   ARG A HH12   1 
ATOM   1045  H HH21   . ARG A 1 67  ? -2.306  -2.796  -10.242 1.00 21.22  ?  67   ARG A HH21   1 
ATOM   1046  H HH22   . ARG A 1 67  ? -1.834  -2.061  -9.036  1.00 21.22  ?  67   ARG A HH22   1 
ATOM   1047  N N      A THR A 1 68  ? 1.319   2.519   -16.456 0.43 18.37  ?  68   THR A N      1 
ATOM   1048  N N      B THR A 1 68  ? 1.296   2.520   -16.439 0.57 18.58  ?  68   THR A N      1 
ATOM   1049  C CA     A THR A 1 68  ? 2.417   3.305   -17.010 0.43 18.37  ?  68   THR A CA     1 
ATOM   1050  C CA     B THR A 1 68  ? 2.378   3.361   -16.937 0.57 18.91  ?  68   THR A CA     1 
ATOM   1051  C C      A THR A 1 68  ? 3.723   3.063   -16.265 0.43 18.74  ?  68   THR A C      1 
ATOM   1052  C C      B THR A 1 68  ? 3.701   2.999   -16.284 0.57 18.79  ?  68   THR A C      1 
ATOM   1053  O O      A THR A 1 68  ? 4.797   3.261   -16.843 0.43 18.94  ?  68   THR A O      1 
ATOM   1054  O O      B THR A 1 68  ? 4.760   3.060   -16.919 0.57 18.07  ?  68   THR A O      1 
ATOM   1055  C CB     A THR A 1 68  ? 2.060   4.789   -17.006 0.43 18.53  ?  68   THR A CB     1 
ATOM   1056  C CB     B THR A 1 68  ? 2.060   4.825   -16.639 0.57 20.55  ?  68   THR A CB     1 
ATOM   1057  O OG1    A THR A 1 68  ? 1.709   5.184   -15.679 0.43 19.91  ?  68   THR A OG1    1 
ATOM   1058  O OG1    B THR A 1 68  ? 0.737   5.140   -17.089 0.57 22.82  ?  68   THR A OG1    1 
ATOM   1059  C CG2    A THR A 1 68  ? 0.899   5.049   -17.951 0.43 18.91  ?  68   THR A CG2    1 
ATOM   1060  C CG2    B THR A 1 68  ? 3.065   5.730   -17.322 0.57 20.86  ?  68   THR A CG2    1 
ATOM   1061  H H      A THR A 1 68  ? 0.669   2.981   -16.135 0.43 22.04  ?  68   THR A H      1 
ATOM   1062  H H      B THR A 1 68  ? 0.625   2.960   -16.131 0.57 22.30  ?  68   THR A H      1 
ATOM   1063  H HA     A THR A 1 68  ? 2.555   3.046   -17.934 0.43 22.04  ?  68   THR A HA     1 
ATOM   1064  H HA     B THR A 1 68  ? 2.456   3.235   -17.895 0.57 22.69  ?  68   THR A HA     1 
ATOM   1065  H HB     A THR A 1 68  ? 2.816   5.317   -17.305 0.43 22.23  ?  68   THR A HB     1 
ATOM   1066  H HB     B THR A 1 68  ? 2.109   4.980   -15.683 0.57 24.66  ?  68   THR A HB     1 
ATOM   1067  H HG1    A THR A 1 68  ? 1.605   6.016   -15.645 0.43 23.89  ?  68   THR A HG1    1 
ATOM   1068  H HG1    B THR A 1 68  ? 0.638   5.973   -17.128 0.57 27.37  ?  68   THR A HG1    1 
ATOM   1069  H HG21   A THR A 1 68  ? 0.687   5.996   -17.963 0.43 22.69  ?  68   THR A HG21   1 
ATOM   1070  H HG21   B THR A 1 68  ? 2.744   6.646   -17.316 0.57 25.03  ?  68   THR A HG21   1 
ATOM   1071  H HG22   A THR A 1 68  ? 1.133   4.768   -18.849 0.43 22.69  ?  68   THR A HG22   1 
ATOM   1072  H HG22   B THR A 1 68  ? 3.915   5.691   -16.857 0.57 25.03  ?  68   THR A HG22   1 
ATOM   1073  H HG23   A THR A 1 68  ? 0.117   4.555   -17.660 0.43 22.69  ?  68   THR A HG23   1 
ATOM   1074  H HG23   B THR A 1 68  ? 3.195   5.448   -18.241 0.57 25.03  ?  68   THR A HG23   1 
ATOM   1075  N N      . GLU A 1 69  ? 3.659   2.628   -15.003 1.00 18.42  ?  69   GLU A N      1 
ATOM   1076  C CA     . GLU A 1 69  ? 4.876   2.285   -14.285 1.00 19.07  ?  69   GLU A CA     1 
ATOM   1077  C C      . GLU A 1 69  ? 5.627   1.166   -14.991 1.00 16.89  ?  69   GLU A C      1 
ATOM   1078  O O      . GLU A 1 69  ? 6.864   1.187   -15.065 1.00 17.50  ?  69   GLU A O      1 
ATOM   1079  C CB     . GLU A 1 69  ? 4.526   1.865   -12.857 1.00 21.09  ?  69   GLU A CB     1 
ATOM   1080  C CG     . GLU A 1 69  ? 5.720   1.415   -12.034 1.00 23.82  ?  69   GLU A CG     1 
ATOM   1081  C CD     . GLU A 1 69  ? 5.367   1.123   -10.577 1.00 25.66  ?  69   GLU A CD     1 
ATOM   1082  O OE1    . GLU A 1 69  ? 4.219   1.358   -10.170 1.00 26.84  ?  69   GLU A OE1    1 
ATOM   1083  O OE2    . GLU A 1 69  ? 6.247   0.645   -9.846  1.00 27.96  -1 69   GLU A OE2    1 
ATOM   1084  H H      A GLU A 1 69  ? 2.935   2.525   -14.551 0.43 22.10  ?  69   GLU A H      1 
ATOM   1085  H H      B GLU A 1 69  ? 2.942   2.568   -14.531 0.57 22.10  ?  69   GLU A H      1 
ATOM   1086  H HA     . GLU A 1 69  ? 5.454   3.063   -14.246 1.00 22.88  ?  69   GLU A HA     1 
ATOM   1087  H HB2    . GLU A 1 69  ? 4.122   2.621   -12.402 1.00 25.30  ?  69   GLU A HB2    1 
ATOM   1088  H HB3    . GLU A 1 69  ? 3.899   1.127   -12.895 1.00 25.30  ?  69   GLU A HB3    1 
ATOM   1089  H HG2    . GLU A 1 69  ? 6.082   0.603   -12.422 1.00 28.59  ?  69   GLU A HG2    1 
ATOM   1090  H HG3    . GLU A 1 69  ? 6.392   2.115   -12.043 1.00 28.59  ?  69   GLU A HG3    1 
ATOM   1091  N N      . VAL A 1 70  ? 4.900   0.168   -15.497 1.00 16.36  ?  70   VAL A N      1 
ATOM   1092  C CA     . VAL A 1 70  ? 5.553   -0.930  -16.201 1.00 15.23  ?  70   VAL A CA     1 
ATOM   1093  C C      . VAL A 1 70  ? 6.064   -0.466  -17.557 1.00 16.32  ?  70   VAL A C      1 
ATOM   1094  O O      . VAL A 1 70  ? 7.173   -0.829  -17.970 1.00 17.64  ?  70   VAL A O      1 
ATOM   1095  C CB     . VAL A 1 70  ? 4.618   -2.149  -16.303 1.00 14.88  ?  70   VAL A CB     1 
ATOM   1096  C CG1    . VAL A 1 70  ? 5.317   -3.264  -17.054 1.00 16.10  ?  70   VAL A CG1    1 
ATOM   1097  C CG2    . VAL A 1 70  ? 4.200   -2.617  -14.903 1.00 16.26  ?  70   VAL A CG2    1 
ATOM   1098  H H      . VAL A 1 70  ? 4.044   0.104   -15.448 1.00 19.63  ?  70   VAL A H      1 
ATOM   1099  H HA     . VAL A 1 70  ? 6.324   -1.210  -15.684 1.00 18.27  ?  70   VAL A HA     1 
ATOM   1100  H HB     . VAL A 1 70  ? 3.815   -1.903  -16.789 1.00 17.85  ?  70   VAL A HB     1 
ATOM   1101  H HG11   . VAL A 1 70  ? 4.851   -4.098  -16.887 1.00 19.32  ?  70   VAL A HG11   1 
ATOM   1102  H HG12   . VAL A 1 70  ? 5.305   -3.062  -18.002 1.00 19.32  ?  70   VAL A HG12   1 
ATOM   1103  H HG13   . VAL A 1 70  ? 6.233   -3.330  -16.741 1.00 19.32  ?  70   VAL A HG13   1 
ATOM   1104  H HG21   . VAL A 1 70  ? 3.647   -3.410  -14.988 1.00 19.51  ?  70   VAL A HG21   1 
ATOM   1105  H HG22   . VAL A 1 70  ? 4.996   -2.823  -14.388 1.00 19.51  ?  70   VAL A HG22   1 
ATOM   1106  H HG23   . VAL A 1 70  ? 3.699   -1.909  -14.470 1.00 19.51  ?  70   VAL A HG23   1 
ATOM   1107  N N      . ALA A 1 71  ? 5.274   0.334   -18.275 1.00 16.34  ?  71   ALA A N      1 
ATOM   1108  C CA     . ALA A 1 71  ? 5.763   0.886   -19.533 1.00 17.44  ?  71   ALA A CA     1 
ATOM   1109  C C      . ALA A 1 71  ? 7.062   1.654   -19.321 1.00 17.06  ?  71   ALA A C      1 
ATOM   1110  O O      . ALA A 1 71  ? 7.995   1.536   -20.122 1.00 17.96  ?  71   ALA A O      1 
ATOM   1111  C CB     . ALA A 1 71  ? 4.703   1.782   -20.172 1.00 19.01  ?  71   ALA A CB     1 
ATOM   1112  H H      . ALA A 1 71  ? 4.474   0.567   -18.062 1.00 19.60  ?  71   ALA A H      1 
ATOM   1113  H HA     . ALA A 1 71  ? 5.938   0.156   -20.147 1.00 20.93  ?  71   ALA A HA     1 
ATOM   1114  H HB1    . ALA A 1 71  ? 5.026   2.088   -21.034 1.00 22.81  ?  71   ALA A HB1    1 
ATOM   1115  H HB2    . ALA A 1 71  ? 3.886   1.271   -20.286 1.00 22.81  ?  71   ALA A HB2    1 
ATOM   1116  H HB3    . ALA A 1 71  ? 4.540   2.541   -19.591 1.00 22.81  ?  71   ALA A HB3    1 
ATOM   1117  N N      . GLU A 1 72  ? 7.156   2.427   -18.229 1.00 17.98  ?  72   GLU A N      1 
ATOM   1118  C CA     . GLU A 1 72  ? 8.362   3.216   -17.991 1.00 19.64  ?  72   GLU A CA     1 
ATOM   1119  C C      . GLU A 1 72  ? 9.549   2.321   -17.645 1.00 18.37  ?  72   GLU A C      1 
ATOM   1120  O O      . GLU A 1 72  ? 10.681  2.590   -18.073 1.00 18.31  ?  72   GLU A O      1 
ATOM   1121  C CB     . GLU A 1 72  ? 8.101   4.261   -16.907 1.00 22.80  ?  72   GLU A CB     1 
ATOM   1122  C CG     . GLU A 1 72  ? 7.111   5.334   -17.361 1.00 29.28  ?  72   GLU A CG     1 
ATOM   1123  C CD     . GLU A 1 72  ? 6.760   6.342   -16.294 1.00 37.25  ?  72   GLU A CD     1 
ATOM   1124  O OE1    . GLU A 1 72  ? 7.027   6.096   -15.092 1.00 39.04  ?  72   GLU A OE1    1 
ATOM   1125  O OE2    . GLU A 1 72  ? 6.203   7.397   -16.672 1.00 40.87  -1 72   GLU A OE2    1 
ATOM   1126  H H      . GLU A 1 72  ? 6.549   2.508   -17.625 1.00 21.57  ?  72   GLU A H      1 
ATOM   1127  H HA     . GLU A 1 72  ? 8.593   3.697   -18.801 1.00 23.57  ?  72   GLU A HA     1 
ATOM   1128  H HB2    . GLU A 1 72  ? 7.733   3.821   -16.124 1.00 27.36  ?  72   GLU A HB2    1 
ATOM   1129  H HB3    . GLU A 1 72  ? 8.937   4.697   -16.679 1.00 27.36  ?  72   GLU A HB3    1 
ATOM   1130  H HG2    . GLU A 1 72  ? 7.497   5.818   -18.107 1.00 35.13  ?  72   GLU A HG2    1 
ATOM   1131  H HG3    . GLU A 1 72  ? 6.288   4.900   -17.637 1.00 35.13  ?  72   GLU A HG3    1 
ATOM   1132  N N      . ALA A 1 73  ? 9.305   1.225   -16.917 1.00 16.69  ?  73   ALA A N      1 
ATOM   1133  C CA     . ALA A 1 73  ? 10.381  0.281   -16.640 1.00 16.30  ?  73   ALA A CA     1 
ATOM   1134  C C      . ALA A 1 73  ? 10.916  -0.330  -17.926 1.00 16.84  ?  73   ALA A C      1 
ATOM   1135  O O      . ALA A 1 73  ? 12.137  -0.490  -18.094 1.00 19.28  ?  73   ALA A O      1 
ATOM   1136  C CB     . ALA A 1 73  ? 9.900   -0.831  -15.705 1.00 16.39  ?  73   ALA A CB     1 
ATOM   1137  H H      . ALA A 1 73  ? 8.542   1.011   -16.581 1.00 20.03  ?  73   ALA A H      1 
ATOM   1138  H HA     . ALA A 1 73  ? 11.096  0.762   -16.195 1.00 19.55  ?  73   ALA A HA     1 
ATOM   1139  H HB1    . ALA A 1 73  ? 10.627  -1.456  -15.558 1.00 19.67  ?  73   ALA A HB1    1 
ATOM   1140  H HB2    . ALA A 1 73  ? 9.627   -0.438  -14.861 1.00 19.67  ?  73   ALA A HB2    1 
ATOM   1141  H HB3    . ALA A 1 73  ? 9.150   -1.287  -16.116 1.00 19.67  ?  73   ALA A HB3    1 
ATOM   1142  N N      . ILE A 1 74  ? 10.016  -0.732  -18.822 1.00 15.71  ?  74   ILE A N      1 
ATOM   1143  C CA     . ILE A 1 74  ? 10.446  -1.265  -20.107 1.00 16.25  ?  74   ILE A CA     1 
ATOM   1144  C C      . ILE A 1 74  ? 11.247  -0.217  -20.864 1.00 16.17  ?  74   ILE A C      1 
ATOM   1145  O O      . ILE A 1 74  ? 12.316  -0.507  -21.419 1.00 16.56  ?  74   ILE A O      1 
ATOM   1146  C CB     . ILE A 1 74  ? 9.211   -1.714  -20.902 1.00 15.71  ?  74   ILE A CB     1 
ATOM   1147  C CG1    . ILE A 1 74  ? 8.572   -2.942  -20.260 1.00 15.30  ?  74   ILE A CG1    1 
ATOM   1148  C CG2    . ILE A 1 74  ? 9.579   -2.042  -22.354 1.00 15.93  ?  74   ILE A CG2    1 
ATOM   1149  C CD1    . ILE A 1 74  ? 7.202   -3.243  -20.796 1.00 16.04  ?  74   ILE A CD1    1 
ATOM   1150  H H      . ILE A 1 74  ? 9.164   -0.706  -18.712 1.00 18.85  ?  74   ILE A H      1 
ATOM   1151  H HA     . ILE A 1 74  ? 11.021  -2.034  -19.966 1.00 19.49  ?  74   ILE A HA     1 
ATOM   1152  H HB     . ILE A 1 74  ? 8.579   -0.977  -20.892 1.00 18.85  ?  74   ILE A HB     1 
ATOM   1153  H HG12   . ILE A 1 74  ? 9.135   -3.714  -20.429 1.00 18.36  ?  74   ILE A HG12   1 
ATOM   1154  H HG13   . ILE A 1 74  ? 8.493   -2.792  -19.305 1.00 18.36  ?  74   ILE A HG13   1 
ATOM   1155  H HG21   . ILE A 1 74  ? 8.841   -2.517  -22.767 1.00 19.11  ?  74   ILE A HG21   1 
ATOM   1156  H HG22   . ILE A 1 74  ? 9.749   -1.215  -22.831 1.00 19.11  ?  74   ILE A HG22   1 
ATOM   1157  H HG23   . ILE A 1 74  ? 10.374  -2.597  -22.360 1.00 19.11  ?  74   ILE A HG23   1 
ATOM   1158  H HD11   . ILE A 1 74  ? 6.798   -3.939  -20.255 1.00 19.25  ?  74   ILE A HD11   1 
ATOM   1159  H HD12   . ILE A 1 74  ? 6.664   -2.438  -20.756 1.00 19.25  ?  74   ILE A HD12   1 
ATOM   1160  H HD13   . ILE A 1 74  ? 7.282   -3.542  -21.715 1.00 19.25  ?  74   ILE A HD13   1 
ATOM   1161  N N      . HIS A 1 75  ? 10.762  1.024   -20.868 1.00 17.21  ?  75   HIS A N      1 
ATOM   1162  C CA     . HIS A 1 75  ? 11.411  2.060   -21.656 1.00 18.27  ?  75   HIS A CA     1 
ATOM   1163  C C      . HIS A 1 75  ? 12.806  2.358   -21.123 1.00 16.62  ?  75   HIS A C      1 
ATOM   1164  O O      . HIS A 1 75  ? 13.765  2.475   -21.900 1.00 17.47  ?  75   HIS A O      1 
ATOM   1165  C CB     . HIS A 1 75  ? 10.549  3.319   -21.665 1.00 18.77  ?  75   HIS A CB     1 
ATOM   1166  C CG     . HIS A 1 75  ? 10.969  4.307   -22.702 1.00 21.02  ?  75   HIS A CG     1 
ATOM   1167  N ND1    . HIS A 1 75  ? 10.939  4.010   -24.048 1.00 24.89  ?  75   HIS A ND1    1 
ATOM   1168  C CD2    . HIS A 1 75  ? 11.469  5.559   -22.603 1.00 26.12  ?  75   HIS A CD2    1 
ATOM   1169  C CE1    . HIS A 1 75  ? 11.376  5.049   -24.735 1.00 25.98  ?  75   HIS A CE1    1 
ATOM   1170  N NE2    . HIS A 1 75  ? 11.706  6.001   -23.883 1.00 25.66  ?  75   HIS A NE2    1 
ATOM   1171  H H      . HIS A 1 75  ? 10.070  1.287   -20.431 1.00 20.65  ?  75   HIS A H      1 
ATOM   1172  H HA     . HIS A 1 75  ? 11.503  1.756   -22.572 1.00 21.92  ?  75   HIS A HA     1 
ATOM   1173  H HB2    . HIS A 1 75  ? 9.629   3.069   -21.845 1.00 22.52  ?  75   HIS A HB2    1 
ATOM   1174  H HB3    . HIS A 1 75  ? 10.612  3.750   -20.798 1.00 22.52  ?  75   HIS A HB3    1 
ATOM   1175  H HD2    . HIS A 1 75  ? 11.624  6.032   -21.818 1.00 31.34  ?  75   HIS A HD2    1 
ATOM   1176  H HE1    . HIS A 1 75  ? 11.440  5.102   -25.661 1.00 31.17  ?  75   HIS A HE1    1 
ATOM   1177  H HE2    . HIS A 1 75  ? 12.019  6.773   -24.094 1.00 30.79  ?  75   HIS A HE2    1 
ATOM   1178  N N      . ARG A 1 76  ? 12.946  2.467   -19.798 1.00 16.33  ?  76   ARG A N      1 
ATOM   1179  C CA     . ARG A 1 76  ? 14.256  2.733   -19.225 1.00 19.25  ?  76   ARG A CA     1 
ATOM   1180  C C      . ARG A 1 76  ? 15.251  1.661   -19.639 1.00 19.23  ?  76   ARG A C      1 
ATOM   1181  O O      . ARG A 1 76  ? 16.397  1.972   -20.009 1.00 19.04  ?  76   ARG A O      1 
ATOM   1182  C CB     . ARG A 1 76  ? 14.160  2.814   -17.709 1.00 25.81  ?  76   ARG A CB     1 
ATOM   1183  C CG     . ARG A 1 76  ? 13.656  4.145   -17.185 1.00 31.51  ?  76   ARG A CG     1 
ATOM   1184  C CD     . ARG A 1 76  ? 13.938  4.329   -15.681 1.00 34.94  ?  76   ARG A CD     1 
ATOM   1185  N NE     . ARG A 1 76  ? 13.374  3.241   -14.891 1.00 42.62  ?  76   ARG A NE     1 
ATOM   1186  C CZ     . ARG A 1 76  ? 12.109  3.193   -14.472 1.00 46.11  ?  76   ARG A CZ     1 
ATOM   1187  N NH1    . ARG A 1 76  ? 11.263  4.177   -14.753 1.00 47.34  ?  76   ARG A NH1    1 
ATOM   1188  N NH2    . ARG A 1 76  ? 11.694  2.157   -13.767 1.00 47.42  ?  76   ARG A NH2    1 
ATOM   1189  H H      . ARG A 1 76  ? 12.310  2.392   -19.224 1.00 19.59  ?  76   ARG A H      1 
ATOM   1190  H HA     . ARG A 1 76  ? 14.575  3.590   -19.548 1.00 23.10  ?  76   ARG A HA     1 
ATOM   1191  H HB2    . ARG A 1 76  ? 13.550  2.126   -17.400 1.00 30.97  ?  76   ARG A HB2    1 
ATOM   1192  H HB3    . ARG A 1 76  ? 15.043  2.666   -17.334 1.00 30.97  ?  76   ARG A HB3    1 
ATOM   1193  H HG2    . ARG A 1 76  ? 14.098  4.863   -17.664 1.00 37.81  ?  76   ARG A HG2    1 
ATOM   1194  H HG3    . ARG A 1 76  ? 12.697  4.197   -17.319 1.00 37.81  ?  76   ARG A HG3    1 
ATOM   1195  H HD2    . ARG A 1 76  ? 14.897  4.346   -15.535 1.00 41.93  ?  76   ARG A HD2    1 
ATOM   1196  H HD3    . ARG A 1 76  ? 13.541  5.161   -15.380 1.00 41.93  ?  76   ARG A HD3    1 
ATOM   1197  H HE     . ARG A 1 76  ? 13.892  2.587   -14.682 1.00 51.14  ?  76   ARG A HE     1 
ATOM   1198  H HH11   . ARG A 1 76  ? 11.529  4.855   -15.210 1.00 56.80  ?  76   ARG A HH11   1 
ATOM   1199  H HH12   . ARG A 1 76  ? 10.449  4.136   -14.477 1.00 56.80  ?  76   ARG A HH12   1 
ATOM   1200  H HH21   . ARG A 1 76  ? 12.239  1.518   -13.581 1.00 56.90  ?  76   ARG A HH21   1 
ATOM   1201  H HH22   . ARG A 1 76  ? 10.880  2.121   -13.494 1.00 56.90  ?  76   ARG A HH22   1 
ATOM   1202  N N      . GLN A 1 77  ? 14.829  0.391   -19.614 1.00 17.28  ?  77   GLN A N      1 
ATOM   1203  C CA     . GLN A 1 77  ? 15.739  -0.667  -20.044 1.00 14.05  ?  77   GLN A CA     1 
ATOM   1204  C C      . GLN A 1 77  ? 16.000  -0.605  -21.550 1.00 17.93  ?  77   GLN A C      1 
ATOM   1205  O O      . GLN A 1 77  ? 17.116  -0.894  -21.997 1.00 17.70  ?  77   GLN A O      1 
ATOM   1206  C CB     . GLN A 1 77  ? 15.233  -2.043  -19.629 1.00 14.75  ?  77   GLN A CB     1 
ATOM   1207  C CG     . GLN A 1 77  ? 16.210  -3.153  -19.965 1.00 15.79  ?  77   GLN A CG     1 
ATOM   1208  C CD     . GLN A 1 77  ? 17.581  -2.970  -19.325 1.00 16.73  ?  77   GLN A CD     1 
ATOM   1209  O OE1    . GLN A 1 77  ? 17.716  -2.540  -18.167 1.00 18.36  ?  77   GLN A OE1    1 
ATOM   1210  N NE2    . GLN A 1 77  ? 18.612  -3.355  -20.071 1.00 15.84  ?  77   GLN A NE2    1 
ATOM   1211  H H      . GLN A 1 77  ? 14.051  0.126   -19.362 1.00 20.73  ?  77   GLN A H      1 
ATOM   1212  H HA     . GLN A 1 77  ? 16.585  -0.533  -19.589 1.00 16.85  ?  77   GLN A HA     1 
ATOM   1213  H HB2    . GLN A 1 77  ? 15.089  -2.050  -18.669 1.00 17.69  ?  77   GLN A HB2    1 
ATOM   1214  H HB3    . GLN A 1 77  ? 14.400  -2.226  -20.091 1.00 17.69  ?  77   GLN A HB3    1 
ATOM   1215  H HG2    . GLN A 1 77  ? 15.846  -3.996  -19.653 1.00 18.94  ?  77   GLN A HG2    1 
ATOM   1216  H HG3    . GLN A 1 77  ? 16.333  -3.180  -20.927 1.00 18.94  ?  77   GLN A HG3    1 
ATOM   1217  H HE21   . GLN A 1 77  ? 18.477  -3.680  -20.855 1.00 19.00  ?  77   GLN A HE21   1 
ATOM   1218  H HE22   . GLN A 1 77  ? 19.413  -3.279  -19.768 1.00 19.00  ?  77   GLN A HE22   1 
ATOM   1219  N N      . ALA A 1 78  ? 14.989  -0.234  -22.347 1.00 16.73  ?  78   ALA A N      1 
ATOM   1220  C CA     . ALA A 1 78  ? 15.191  -0.155  -23.790 1.00 16.32  ?  78   ALA A CA     1 
ATOM   1221  C C      . ALA A 1 78  ? 16.206  0.924   -24.161 1.00 18.24  ?  78   ALA A C      1 
ATOM   1222  O O      . ALA A 1 78  ? 16.939  0.783   -25.153 1.00 21.56  ?  78   ALA A O      1 
ATOM   1223  C CB     . ALA A 1 78  ? 13.867  0.113   -24.498 1.00 17.06  ?  78   ALA A CB     1 
ATOM   1224  H H      . ALA A 1 78  ? 14.197  -0.029  -22.082 1.00 20.08  ?  78   ALA A H      1 
ATOM   1225  H HA     . ALA A 1 78  ? 15.530  -1.010  -24.097 1.00 19.58  ?  78   ALA A HA     1 
ATOM   1226  H HB1    . ALA A 1 78  ? 14.011  0.089   -25.456 1.00 20.46  ?  78   ALA A HB1    1 
ATOM   1227  H HB2    . ALA A 1 78  ? 13.228  -0.571  -24.242 1.00 20.46  ?  78   ALA A HB2    1 
ATOM   1228  H HB3    . ALA A 1 78  ? 13.539  0.987   -24.234 1.00 20.46  ?  78   ALA A HB3    1 
ATOM   1229  N N      . LEU A 1 79  ? 16.279  1.997   -23.382 1.00 18.34  ?  79   LEU A N      1 
ATOM   1230  C CA     . LEU A 1 79  ? 17.277  3.018   -23.656 1.00 19.70  ?  79   LEU A CA     1 
ATOM   1231  C C      . LEU A 1 79  ? 18.684  2.604   -23.226 1.00 21.04  ?  79   LEU A C      1 
ATOM   1232  O O      . LEU A 1 79  ? 19.644  3.284   -23.581 1.00 23.92  ?  79   LEU A O      1 
ATOM   1233  C CB     . LEU A 1 79  ? 16.886  4.326   -22.987 1.00 20.80  ?  79   LEU A CB     1 
ATOM   1234  C CG     . LEU A 1 79  ? 15.567  4.935   -23.471 1.00 26.59  ?  79   LEU A CG     1 
ATOM   1235  C CD1    . LEU A 1 79  ? 15.271  6.212   -22.677 1.00 29.01  ?  79   LEU A CD1    1 
ATOM   1236  C CD2    . LEU A 1 79  ? 15.577  5.225   -24.957 1.00 27.62  ?  79   LEU A CD2    1 
ATOM   1237  H H      . LEU A 1 79  ? 15.773  2.151   -22.704 1.00 22.00  ?  79   LEU A H      1 
ATOM   1238  H HA     . LEU A 1 79  ? 17.303  3.181   -24.612 1.00 23.64  ?  79   LEU A HA     1 
ATOM   1239  H HB2    . LEU A 1 79  ? 16.801  4.169   -22.033 1.00 24.96  ?  79   LEU A HB2    1 
ATOM   1240  H HB3    . LEU A 1 79  ? 17.585  4.977   -23.154 1.00 24.96  ?  79   LEU A HB3    1 
ATOM   1241  H HG     . LEU A 1 79  ? 14.859  4.289   -23.322 1.00 31.90  ?  79   LEU A HG     1 
ATOM   1242  H HD11   . LEU A 1 79  ? 14.424  6.579   -22.974 1.00 34.80  ?  79   LEU A HD11   1 
ATOM   1243  H HD12   . LEU A 1 79  ? 15.225  5.993   -21.733 1.00 34.80  ?  79   LEU A HD12   1 
ATOM   1244  H HD13   . LEU A 1 79  ? 15.983  6.853   -22.834 1.00 34.80  ?  79   LEU A HD13   1 
ATOM   1245  H HD21   . LEU A 1 79  ? 14.771  5.714   -25.189 1.00 33.14  ?  79   LEU A HD21   1 
ATOM   1246  H HD22   . LEU A 1 79  ? 16.359  5.757   -25.170 1.00 33.14  ?  79   LEU A HD22   1 
ATOM   1247  H HD23   . LEU A 1 79  ? 15.605  4.386   -25.443 1.00 33.14  ?  79   LEU A HD23   1 
ATOM   1248  N N      . GLU A 1 80  ? 18.821  1.503   -22.475 1.00 21.04  ?  80   GLU A N      1 
ATOM   1249  C CA     . GLU A 1 80  ? 20.132  0.962   -22.133 1.00 22.56  ?  80   GLU A CA     1 
ATOM   1250  C C      . GLU A 1 80  ? 20.516  -0.175  -23.077 1.00 19.91  ?  80   GLU A C      1 
ATOM   1251  O O      . GLU A 1 80  ? 21.468  -0.037  -23.865 1.00 20.43  ?  80   GLU A O      1 
ATOM   1252  C CB     . GLU A 1 80  ? 20.150  0.488   -20.686 1.00 25.22  ?  80   GLU A CB     1 
ATOM   1253  C CG     . GLU A 1 80  ? 19.784  1.565   -19.671 1.00 29.51  ?  80   GLU A CG     1 
ATOM   1254  C CD     . GLU A 1 80  ? 20.741  2.738   -19.668 1.00 35.22  ?  80   GLU A CD     1 
ATOM   1255  O OE1    . GLU A 1 80  ? 21.927  2.552   -20.022 1.00 37.35  ?  80   GLU A OE1    1 
ATOM   1256  O OE2    . GLU A 1 80  ? 20.297  3.854   -19.322 1.00 39.56  -1 80   GLU A OE2    1 
ATOM   1257  H H      . GLU A 1 80  ? 18.164  1.053   -22.152 1.00 25.24  ?  80   GLU A H      1 
ATOM   1258  H HA     . GLU A 1 80  ? 20.798  1.661   -22.228 1.00 27.07  ?  80   GLU A HA     1 
ATOM   1259  H HB2    . GLU A 1 80  ? 19.512  -0.236  -20.589 1.00 30.26  ?  80   GLU A HB2    1 
ATOM   1260  H HB3    . GLU A 1 80  ? 21.042  0.175   -20.473 1.00 30.26  ?  80   GLU A HB3    1 
ATOM   1261  H HG2    . GLU A 1 80  ? 18.899  1.904   -19.878 1.00 35.41  ?  80   GLU A HG2    1 
ATOM   1262  H HG3    . GLU A 1 80  ? 19.790  1.174   -18.783 1.00 35.41  ?  80   GLU A HG3    1 
ATOM   1263  N N      . LEU A 1 81  ? 19.774  -1.286  -23.003 1.00 18.45  ?  81   LEU A N      1 
ATOM   1264  C CA     . LEU A 1 81  ? 19.971  -2.430  -23.900 1.00 16.42  ?  81   LEU A CA     1 
ATOM   1265  C C      . LEU A 1 81  ? 18.673  -3.228  -23.959 1.00 16.74  ?  81   LEU A C      1 
ATOM   1266  O O      . LEU A 1 81  ? 18.265  -3.818  -22.958 1.00 16.97  ?  81   LEU A O      1 
ATOM   1267  C CB     . LEU A 1 81  ? 21.106  -3.313  -23.403 1.00 18.44  ?  81   LEU A CB     1 
ATOM   1268  C CG     . LEU A 1 81  ? 21.436  -4.543  -24.248 1.00 19.60  ?  81   LEU A CG     1 
ATOM   1269  C CD1    . LEU A 1 81  ? 21.951  -4.160  -25.639 1.00 19.51  ?  81   LEU A CD1    1 
ATOM   1270  C CD2    . LEU A 1 81  ? 22.451  -5.414  -23.511 1.00 22.23  ?  81   LEU A CD2    1 
ATOM   1271  H H      . LEU A 1 81  ? 19.141  -1.403  -22.434 1.00 22.14  ?  81   LEU A H      1 
ATOM   1272  H HA     . LEU A 1 81  ? 20.179  -2.100  -24.787 1.00 19.69  ?  81   LEU A HA     1 
ATOM   1273  H HB2    . LEU A 1 81  ? 21.910  -2.773  -23.361 1.00 22.12  ?  81   LEU A HB2    1 
ATOM   1274  H HB3    . LEU A 1 81  ? 20.872  -3.631  -22.517 1.00 22.12  ?  81   LEU A HB3    1 
ATOM   1275  H HG     . LEU A 1 81  ? 20.624  -5.054  -24.386 1.00 23.52  ?  81   LEU A HG     1 
ATOM   1276  H HD11   . LEU A 1 81  ? 22.232  -4.964  -26.104 1.00 23.41  ?  81   LEU A HD11   1 
ATOM   1277  H HD12   . LEU A 1 81  ? 21.237  -3.726  -26.131 1.00 23.41  ?  81   LEU A HD12   1 
ATOM   1278  H HD13   . LEU A 1 81  ? 22.702  -3.555  -25.542 1.00 23.41  ?  81   LEU A HD13   1 
ATOM   1279  H HD21   . LEU A 1 81  ? 22.669  -6.181  -24.064 1.00 26.68  ?  81   LEU A HD21   1 
ATOM   1280  H HD22   . LEU A 1 81  ? 23.250  -4.892  -23.340 1.00 26.68  ?  81   LEU A HD22   1 
ATOM   1281  H HD23   . LEU A 1 81  ? 22.063  -5.710  -22.673 1.00 26.68  ?  81   LEU A HD23   1 
ATOM   1282  N N      . ALA A 1 82  ? 18.026  -3.251  -25.124 1.00 16.98  ?  82   ALA A N      1 
ATOM   1283  C CA     . ALA A 1 82  ? 16.784  -4.006  -25.273 1.00 15.50  ?  82   ALA A CA     1 
ATOM   1284  C C      . ALA A 1 82  ? 17.052  -5.501  -25.278 1.00 15.36  ?  82   ALA A C      1 
ATOM   1285  O O      . ALA A 1 82  ? 16.289  -6.274  -24.691 1.00 15.23  ?  82   ALA A O      1 
ATOM   1286  C CB     . ALA A 1 82  ? 16.094  -3.599  -26.570 1.00 16.96  ?  82   ALA A CB     1 
ATOM   1287  H H      . ALA A 1 82  ? 18.281  -2.844  -25.838 1.00 20.37  ?  82   ALA A H      1 
ATOM   1288  H HA     . ALA A 1 82  ? 16.197  -3.801  -24.528 1.00 18.60  ?  82   ALA A HA     1 
ATOM   1289  H HB1    . ALA A 1 82  ? 15.262  -4.090  -26.653 1.00 20.35  ?  82   ALA A HB1    1 
ATOM   1290  H HB2    . ALA A 1 82  ? 15.915  -2.646  -26.547 1.00 20.35  ?  82   ALA A HB2    1 
ATOM   1291  H HB3    . ALA A 1 82  ? 16.677  -3.808  -27.317 1.00 20.35  ?  82   ALA A HB3    1 
ATOM   1292  N N      . TYR A 1 83  ? 18.129  -5.931  -25.942 1.00 15.52  ?  83   TYR A N      1 
ATOM   1293  C CA     . TYR A 1 83  ? 18.393  -7.350  -26.135 1.00 13.35  ?  83   TYR A CA     1 
ATOM   1294  C C      . TYR A 1 83  ? 19.876  -7.630  -26.382 1.00 12.96  ?  83   TYR A C      1 
ATOM   1295  O O      . TYR A 1 83  ? 20.529  -6.973  -27.190 1.00 14.71  ?  83   TYR A O      1 
ATOM   1296  C CB     . TYR A 1 83  ? 17.614  -7.924  -27.329 1.00 14.26  ?  83   TYR A CB     1 
ATOM   1297  C CG     . TYR A 1 83  ? 18.066  -9.316  -27.729 1.00 13.38  ?  83   TYR A CG     1 
ATOM   1298  C CD1    . TYR A 1 83  ? 17.555  -10.447 -27.094 1.00 12.81  ?  83   TYR A CD1    1 
ATOM   1299  C CD2    . TYR A 1 83  ? 19.012  -9.513  -28.736 1.00 13.53  ?  83   TYR A CD2    1 
ATOM   1300  C CE1    . TYR A 1 83  ? 17.979  -11.711 -27.448 1.00 12.55  ?  83   TYR A CE1    1 
ATOM   1301  C CE2    . TYR A 1 83  ? 19.453  -10.779 -29.082 1.00 12.28  ?  83   TYR A CE2    1 
ATOM   1302  C CZ     . TYR A 1 83  ? 18.946  -11.872 -28.436 1.00 12.96  ?  83   TYR A CZ     1 
ATOM   1303  O OH     . TYR A 1 83  ? 19.379  -13.126 -28.813 1.00 15.40  ?  83   TYR A OH     1 
ATOM   1304  H H      . TYR A 1 83  ? 18.722  -5.415  -26.291 1.00 18.62  ?  83   TYR A H      1 
ATOM   1305  H HA     . TYR A 1 83  ? 18.132  -7.784  -25.307 1.00 16.02  ?  83   TYR A HA     1 
ATOM   1306  H HB2    . TYR A 1 83  ? 16.674  -7.971  -27.096 1.00 17.10  ?  83   TYR A HB2    1 
ATOM   1307  H HB3    . TYR A 1 83  ? 17.738  -7.340  -28.093 1.00 17.10  ?  83   TYR A HB3    1 
ATOM   1308  H HD1    . TYR A 1 83  ? 16.919  -10.348 -26.423 1.00 15.37  ?  83   TYR A HD1    1 
ATOM   1309  H HD2    . TYR A 1 83  ? 19.355  -8.775  -29.186 1.00 16.23  ?  83   TYR A HD2    1 
ATOM   1310  H HE1    . TYR A 1 83  ? 17.618  -12.457 -27.026 1.00 15.05  ?  83   TYR A HE1    1 
ATOM   1311  H HE2    . TYR A 1 83  ? 20.092  -10.885 -29.750 1.00 14.73  ?  83   TYR A HE2    1 
ATOM   1312  H HH     . TYR A 1 83  ? 18.991  -13.713 -28.355 1.00 18.48  ?  83   TYR A HH     1 
ATOM   1313  N N      . TYR A 1 84  ? 20.377  -8.671  -25.720 1.00 13.43  ?  84   TYR A N      1 
ATOM   1314  C CA     . TYR A 1 84  ? 21.519  -9.458  -26.177 1.00 12.08  ?  84   TYR A CA     1 
ATOM   1315  C C      . TYR A 1 84  ? 21.191  -10.895 -25.779 1.00 14.00  ?  84   TYR A C      1 
ATOM   1316  O O      . TYR A 1 84  ? 20.345  -11.135 -24.917 1.00 14.29  ?  84   TYR A O      1 
ATOM   1317  C CB     . TYR A 1 84  ? 22.873  -8.963  -25.624 1.00 14.07  ?  84   TYR A CB     1 
ATOM   1318  C CG     . TYR A 1 84  ? 24.044  -9.640  -26.320 1.00 15.20  ?  84   TYR A CG     1 
ATOM   1319  C CD1    . TYR A 1 84  ? 24.410  -9.305  -27.625 1.00 15.01  ?  84   TYR A CD1    1 
ATOM   1320  C CD2    . TYR A 1 84  ? 24.730  -10.654 -25.699 1.00 15.06  ?  84   TYR A CD2    1 
ATOM   1321  C CE1    . TYR A 1 84  ? 25.448  -9.960  -28.262 1.00 14.83  ?  84   TYR A CE1    1 
ATOM   1322  C CE2    . TYR A 1 84  ? 25.776  -11.301 -26.315 1.00 15.24  ?  84   TYR A CE2    1 
ATOM   1323  C CZ     . TYR A 1 84  ? 26.128  -10.959 -27.588 1.00 14.52  ?  84   TYR A CZ     1 
ATOM   1324  O OH     . TYR A 1 84  ? 27.143  -11.634 -28.209 1.00 15.92  ?  84   TYR A OH     1 
ATOM   1325  H H      . TYR A 1 84  ? 20.059  -8.952  -24.971 1.00 16.11  ?  84   TYR A H      1 
ATOM   1326  H HA     . TYR A 1 84  ? 21.638  -9.402  -27.138 1.00 14.49  ?  84   TYR A HA     1 
ATOM   1327  H HB2    . TYR A 1 84  ? 22.947  -8.006  -25.765 1.00 16.88  ?  84   TYR A HB2    1 
ATOM   1328  H HB3    . TYR A 1 84  ? 22.925  -9.164  -24.676 1.00 16.88  ?  84   TYR A HB3    1 
ATOM   1329  H HD1    . TYR A 1 84  ? 23.949  -8.633  -28.072 1.00 18.01  ?  84   TYR A HD1    1 
ATOM   1330  H HD2    . TYR A 1 84  ? 24.481  -10.910 -24.840 1.00 18.07  ?  84   TYR A HD2    1 
ATOM   1331  H HE1    . TYR A 1 84  ? 25.685  -9.732  -29.132 1.00 17.79  ?  84   TYR A HE1    1 
ATOM   1332  H HE2    . TYR A 1 84  ? 26.241  -11.969 -25.866 1.00 18.28  ?  84   TYR A HE2    1 
ATOM   1333  H HH     . TYR A 1 84  ? 27.179  -11.415 -29.019 1.00 19.10  ?  84   TYR A HH     1 
ATOM   1334  N N      . HIS A 1 85  ? 21.822  -11.867 -26.431 1.00 14.00  ?  85   HIS A N      1 
ATOM   1335  C CA     . HIS A 1 85  ? 21.505  -13.235 -26.037 1.00 13.72  ?  85   HIS A CA     1 
ATOM   1336  C C      . HIS A 1 85  ? 22.010  -13.506 -24.621 1.00 13.06  ?  85   HIS A C      1 
ATOM   1337  O O      . HIS A 1 85  ? 22.860  -12.781 -24.080 1.00 14.43  ?  85   HIS A O      1 
ATOM   1338  C CB     . HIS A 1 85  ? 22.040  -14.245 -27.042 1.00 14.83  ?  85   HIS A CB     1 
ATOM   1339  C CG     . HIS A 1 85  ? 23.526  -14.406 -27.039 1.00 15.21  ?  85   HIS A CG     1 
ATOM   1340  N ND1    . HIS A 1 85  ? 24.220  -14.965 -25.985 1.00 15.38  ?  85   HIS A ND1    1 
ATOM   1341  C CD2    . HIS A 1 85  ? 24.448  -14.129 -27.995 1.00 15.41  ?  85   HIS A CD2    1 
ATOM   1342  C CE1    . HIS A 1 85  ? 25.500  -15.024 -26.292 1.00 14.62  ?  85   HIS A CE1    1 
ATOM   1343  N NE2    . HIS A 1 85  ? 25.670  -14.513 -27.500 1.00 17.01  ?  85   HIS A NE2    1 
ATOM   1344  H H      . HIS A 1 85  ? 22.398  -11.769 -27.062 1.00 16.80  ?  85   HIS A H      1 
ATOM   1345  H HA     . HIS A 1 85  ? 20.543  -13.360 -26.028 1.00 16.47  ?  85   HIS A HA     1 
ATOM   1346  H HB2    . HIS A 1 85  ? 21.653  -15.112 -26.843 1.00 17.79  ?  85   HIS A HB2    1 
ATOM   1347  H HB3    . HIS A 1 85  ? 21.779  -13.961 -27.932 1.00 17.79  ?  85   HIS A HB3    1 
ATOM   1348  H HD2    . HIS A 1 85  ? 24.283  -13.751 -28.829 1.00 18.49  ?  85   HIS A HD2    1 
ATOM   1349  H HE1    . HIS A 1 85  ? 26.173  -15.367 -25.749 1.00 17.54  ?  85   HIS A HE1    1 
ATOM   1350  H HE2    . HIS A 1 85  ? 26.422  -14.434 -27.909 1.00 20.41  ?  85   HIS A HE2    1 
ATOM   1351  N N      . THR A 1 86  ? 21.447  -14.549 -24.000 1.00 12.00  ?  86   THR A N      1 
ATOM   1352  C CA     . THR A 1 86  ? 21.869  -15.001 -22.676 1.00 12.37  ?  86   THR A CA     1 
ATOM   1353  C C      . THR A 1 86  ? 22.396  -16.428 -22.716 1.00 13.20  ?  86   THR A C      1 
ATOM   1354  O O      . THR A 1 86  ? 22.208  -17.198 -21.766 1.00 14.30  ?  86   THR A O      1 
ATOM   1355  C CB     . THR A 1 86  ? 20.794  -14.805 -21.594 1.00 13.95  ?  86   THR A CB     1 
ATOM   1356  O OG1    . THR A 1 86  ? 19.654  -15.664 -21.802 1.00 14.77  ?  86   THR A OG1    1 
ATOM   1357  C CG2    . THR A 1 86  ? 20.342  -13.338 -21.560 1.00 14.67  ?  86   THR A CG2    1 
ATOM   1358  H H      . THR A 1 86  ? 20.808  -15.016 -24.336 1.00 14.40  ?  86   THR A H      1 
ATOM   1359  H HA     . THR A 1 86  ? 22.602  -14.430 -22.397 1.00 14.84  ?  86   THR A HA     1 
ATOM   1360  H HB     . THR A 1 86  ? 21.179  -15.041 -20.736 1.00 16.74  ?  86   THR A HB     1 
ATOM   1361  H HG1    . THR A 1 86  ? 19.256  -15.447 -22.509 1.00 17.73  ?  86   THR A HG1    1 
ATOM   1362  H HG21   . THR A 1 86  ? 19.679  -13.212 -20.863 1.00 17.60  ?  86   THR A HG21   1 
ATOM   1363  H HG22   . THR A 1 86  ? 21.101  -12.762 -21.380 1.00 17.60  ?  86   THR A HG22   1 
ATOM   1364  H HG23   . THR A 1 86  ? 19.954  -13.091 -22.413 1.00 17.60  ?  86   THR A HG23   1 
ATOM   1365  N N      . TYR A 1 87  ? 23.064  -16.771 -23.820 1.00 12.85  ?  87   TYR A N      1 
ATOM   1366  C CA     . TYR A 1 87  ? 23.707  -18.060 -23.995 1.00 13.86  ?  87   TYR A CA     1 
ATOM   1367  C C      . TYR A 1 87  ? 25.127  -17.998 -23.421 1.00 14.88  ?  87   TYR A C      1 
ATOM   1368  O O      . TYR A 1 87  ? 25.721  -16.928 -23.285 1.00 13.67  ?  87   TYR A O      1 
ATOM   1369  C CB     . TYR A 1 87  ? 23.823  -18.400 -25.486 1.00 12.45  ?  87   TYR A CB     1 
ATOM   1370  C CG     . TYR A 1 87  ? 22.568  -18.815 -26.231 1.00 12.57  ?  87   TYR A CG     1 
ATOM   1371  C CD1    . TYR A 1 87  ? 21.360  -18.153 -26.065 1.00 13.32  ?  87   TYR A CD1    1 
ATOM   1372  C CD2    . TYR A 1 87  ? 22.614  -19.857 -27.156 1.00 15.12  ?  87   TYR A CD2    1 
ATOM   1373  C CE1    . TYR A 1 87  ? 20.224  -18.549 -26.765 1.00 13.69  ?  87   TYR A CE1    1 
ATOM   1374  C CE2    . TYR A 1 87  ? 21.480  -20.245 -27.868 1.00 16.03  ?  87   TYR A CE2    1 
ATOM   1375  C CZ     . TYR A 1 87  ? 20.285  -19.594 -27.663 1.00 13.79  ?  87   TYR A CZ     1 
ATOM   1376  O OH     . TYR A 1 87  ? 19.152  -19.987 -28.383 1.00 16.08  ?  87   TYR A OH     1 
ATOM   1377  H H      . TYR A 1 87  ? 23.158  -16.253 -24.500 1.00 15.41  ?  87   TYR A H      1 
ATOM   1378  H HA     . TYR A 1 87  ? 23.186  -18.744 -23.546 1.00 16.63  ?  87   TYR A HA     1 
ATOM   1379  H HB2    . TYR A 1 87  ? 24.167  -17.615 -25.941 1.00 14.94  ?  87   TYR A HB2    1 
ATOM   1380  H HB3    . TYR A 1 87  ? 24.450  -19.135 -25.572 1.00 14.94  ?  87   TYR A HB3    1 
ATOM   1381  H HD1    . TYR A 1 87  ? 21.308  -17.434 -25.477 1.00 15.98  ?  87   TYR A HD1    1 
ATOM   1382  H HD2    . TYR A 1 87  ? 23.418  -20.303 -27.300 1.00 18.14  ?  87   TYR A HD2    1 
ATOM   1383  H HE1    . TYR A 1 87  ? 19.418  -18.106 -26.626 1.00 16.42  ?  87   TYR A HE1    1 
ATOM   1384  H HE2    . TYR A 1 87  ? 21.531  -20.942 -28.481 1.00 19.23  ?  87   TYR A HE2    1 
ATOM   1385  H HH     . TYR A 1 87  ? 19.321  -20.677 -28.831 1.00 19.29  ?  87   TYR A HH     1 
ATOM   1386  N N      . VAL A 1 88  ? 25.667  -19.173 -23.118 1.00 15.00  ?  88   VAL A N      1 
ATOM   1387  C CA     . VAL A 1 88  ? 27.062  -19.350 -22.721 1.00 15.18  ?  88   VAL A CA     1 
ATOM   1388  C C      . VAL A 1 88  ? 27.422  -18.339 -21.635 1.00 14.41  ?  88   VAL A C      1 
ATOM   1389  O O      . VAL A 1 88  ? 28.404  -17.600 -21.746 1.00 16.51  ?  88   VAL A O      1 
ATOM   1390  C CB     . VAL A 1 88  ? 28.043  -19.295 -23.915 1.00 16.50  ?  88   VAL A CB     1 
ATOM   1391  C CG1    . VAL A 1 88  ? 29.349  -19.978 -23.529 1.00 16.05  ?  88   VAL A CG1    1 
ATOM   1392  C CG2    . VAL A 1 88  ? 27.459  -19.929 -25.154 1.00 19.86  ?  88   VAL A CG2    1 
ATOM   1393  H H      . VAL A 1 88  ? 25.230  -19.914 -23.136 1.00 17.99  ?  88   VAL A H      1 
ATOM   1394  H HA     . VAL A 1 88  ? 27.149  -20.238 -22.339 1.00 18.21  ?  88   VAL A HA     1 
ATOM   1395  H HB     . VAL A 1 88  ? 28.216  -18.365 -24.130 1.00 19.79  ?  88   VAL A HB     1 
ATOM   1396  H HG11   . VAL A 1 88  ? 29.965  -19.926 -24.277 1.00 19.26  ?  88   VAL A HG11   1 
ATOM   1397  H HG12   . VAL A 1 88  ? 29.726  -19.528 -22.758 1.00 19.26  ?  88   VAL A HG12   1 
ATOM   1398  H HG13   . VAL A 1 88  ? 29.168  -20.907 -23.314 1.00 19.26  ?  88   VAL A HG13   1 
ATOM   1399  H HG21   . VAL A 1 88  ? 28.157  -20.021 -25.821 1.00 23.83  ?  88   VAL A HG21   1 
ATOM   1400  H HG22   . VAL A 1 88  ? 27.104  -20.803 -24.925 1.00 23.83  ?  88   VAL A HG22   1 
ATOM   1401  H HG23   . VAL A 1 88  ? 26.748  -19.363 -25.494 1.00 23.83  ?  88   VAL A HG23   1 
ATOM   1402  N N      . GLY A 1 89  ? 26.646  -18.327 -20.551 1.00 15.73  ?  89   GLY A N      1 
ATOM   1403  C CA     . GLY A 1 89  ? 26.986  -17.486 -19.422 1.00 16.57  ?  89   GLY A CA     1 
ATOM   1404  C C      . GLY A 1 89  ? 26.772  -15.995 -19.593 1.00 16.11  ?  89   GLY A C      1 
ATOM   1405  O O      . GLY A 1 89  ? 27.142  -15.223 -18.697 1.00 16.48  ?  89   GLY A O      1 
ATOM   1406  H H      . GLY A 1 89  ? 25.929  -18.791 -20.452 1.00 18.88  ?  89   GLY A H      1 
ATOM   1407  H HA2    . GLY A 1 89  ? 26.452  -17.768 -18.663 1.00 19.88  ?  89   GLY A HA2    1 
ATOM   1408  H HA3    . GLY A 1 89  ? 27.924  -17.621 -19.216 1.00 19.88  ?  89   GLY A HA3    1 
ATOM   1409  N N      . HIS A 1 90  ? 26.204  -15.558 -20.714 1.00 14.85  ?  90   HIS A N      1 
ATOM   1410  C CA     . HIS A 1 90  ? 25.871  -14.154 -20.902 1.00 13.08  ?  90   HIS A CA     1 
ATOM   1411  C C      . HIS A 1 90  ? 24.556  -13.824 -20.207 1.00 14.29  ?  90   HIS A C      1 
ATOM   1412  O O      . HIS A 1 90  ? 23.633  -14.641 -20.164 1.00 14.50  ?  90   HIS A O      1 
ATOM   1413  C CB     . HIS A 1 90  ? 25.757  -13.810 -22.384 1.00 15.47  ?  90   HIS A CB     1 
ATOM   1414  C CG     . HIS A 1 90  ? 27.067  -13.751 -23.107 1.00 15.46  ?  90   HIS A CG     1 
ATOM   1415  N ND1    . HIS A 1 90  ? 27.771  -14.875 -23.473 1.00 17.24  ?  90   HIS A ND1    1 
ATOM   1416  C CD2    . HIS A 1 90  ? 27.803  -12.696 -23.529 1.00 16.88  ?  90   HIS A CD2    1 
ATOM   1417  C CE1    . HIS A 1 90  ? 28.871  -14.520 -24.117 1.00 18.03  ?  90   HIS A CE1    1 
ATOM   1418  N NE2    . HIS A 1 90  ? 28.926  -13.199 -24.149 1.00 18.13  ?  90   HIS A NE2    1 
ATOM   1419  H H      . HIS A 1 90  ? 26.000  -16.059 -21.383 1.00 17.81  ?  90   HIS A H      1 
ATOM   1420  H HA     . HIS A 1 90  ? 26.577  -13.609 -20.521 1.00 15.69  ?  90   HIS A HA     1 
ATOM   1421  H HB2    . HIS A 1 90  ? 25.213  -14.486 -22.818 1.00 18.57  ?  90   HIS A HB2    1 
ATOM   1422  H HB3    . HIS A 1 90  ? 25.335  -12.941 -22.469 1.00 18.57  ?  90   HIS A HB3    1 
ATOM   1423  H HD1    . HIS A 1 90  ? 27.533  -15.685 -23.309 1.00 20.68  ?  90   HIS A HD1    1 
ATOM   1424  H HD2    . HIS A 1 90  ? 27.590  -11.797 -23.420 1.00 20.26  ?  90   HIS A HD2    1 
ATOM   1425  H HE1    . HIS A 1 90  ? 29.498  -15.100 -24.484 1.00 21.64  ?  90   HIS A HE1    1 
ATOM   1426  N N      . SER A 1 91  ? 24.482  -12.611 -19.656 1.00 13.61  ?  91   SER A N      1 
ATOM   1427  C CA     . SER A 1 91  ? 23.328  -12.202 -18.867 1.00 14.10  ?  91   SER A CA     1 
ATOM   1428  C C      . SER A 1 91  ? 23.073  -10.712 -19.062 1.00 13.32  ?  91   SER A C      1 
ATOM   1429  O O      . SER A 1 91  ? 23.832  -9.998  -19.716 1.00 15.41  ?  91   SER A O      1 
ATOM   1430  C CB     . SER A 1 91  ? 23.551  -12.502 -17.380 1.00 15.20  ?  91   SER A CB     1 
ATOM   1431  O OG     . SER A 1 91  ? 24.689  -11.793 -16.902 1.00 16.57  ?  91   SER A OG     1 
ATOM   1432  H H      . SER A 1 91  ? 25.090  -12.007 -19.728 1.00 16.33  ?  91   SER A H      1 
ATOM   1433  H HA     . SER A 1 91  ? 22.550  -12.686 -19.184 1.00 16.91  ?  91   SER A HA     1 
ATOM   1434  H HB2    . SER A 1 91  ? 22.768  -12.223 -16.878 1.00 18.23  ?  91   SER A HB2    1 
ATOM   1435  H HB3    . SER A 1 91  ? 23.697  -13.454 -17.265 1.00 18.23  ?  91   SER A HB3    1 
ATOM   1436  H HG     . SER A 1 91  ? 25.364  -11.992 -17.361 1.00 19.88  ?  91   SER A HG     1 
ATOM   1437  N N      . ASN A 1 92  ? 21.981  -10.246 -18.482 1.00 15.20  ?  92   ASN A N      1 
ATOM   1438  C CA     . ASN A 1 92  ? 21.737  -8.823  -18.315 1.00 15.69  ?  92   ASN A CA     1 
ATOM   1439  C C      . ASN A 1 92  ? 21.280  -8.603  -16.879 1.00 13.86  ?  92   ASN A C      1 
ATOM   1440  O O      . ASN A 1 92  ? 20.816  -9.530  -16.208 1.00 15.40  ?  92   ASN A O      1 
ATOM   1441  C CB     . ASN A 1 92  ? 20.714  -8.283  -19.311 1.00 15.06  ?  92   ASN A CB     1 
ATOM   1442  C CG     . ASN A 1 92  ? 19.387  -8.982  -19.238 1.00 15.49  ?  92   ASN A CG     1 
ATOM   1443  O OD1    . ASN A 1 92  ? 18.569  -8.685  -18.373 1.00 16.12  ?  92   ASN A OD1    1 
ATOM   1444  N ND2    . ASN A 1 92  ? 19.160  -9.921  -20.153 1.00 16.26  ?  92   ASN A ND2    1 
ATOM   1445  H H      . ASN A 1 92  ? 21.353  -10.744 -18.170 1.00 18.23  ?  92   ASN A H      1 
ATOM   1446  H HA     . ASN A 1 92  ? 22.551  -8.318  -18.470 1.00 18.83  ?  92   ASN A HA     1 
ATOM   1447  H HB2    . ASN A 1 92  ? 20.565  -7.342  -19.130 1.00 18.07  ?  92   ASN A HB2    1 
ATOM   1448  H HB3    . ASN A 1 92  ? 21.061  -8.396  -20.210 1.00 18.07  ?  92   ASN A HB3    1 
ATOM   1449  H HD21   . ASN A 1 92  ? 18.415  -10.350 -20.153 1.00 19.51  ?  92   ASN A HD21   1 
ATOM   1450  H HD22   . ASN A 1 92  ? 19.759  -10.099 -20.744 1.00 19.51  ?  92   ASN A HD22   1 
ATOM   1451  N N      . GLU A 1 93  ? 21.432  -7.354  -16.400 1.00 14.54  ?  93   GLU A N      1 
ATOM   1452  C CA     . GLU A 1 93  ? 21.154  -7.083  -14.988 1.00 16.71  ?  93   GLU A CA     1 
ATOM   1453  C C      . GLU A 1 93  ? 19.706  -7.360  -14.597 1.00 16.18  ?  93   GLU A C      1 
ATOM   1454  O O      . GLU A 1 93  ? 19.478  -7.987  -13.544 1.00 16.02  ?  93   GLU A O      1 
ATOM   1455  C CB     . GLU A 1 93  ? 21.603  -5.663  -14.633 1.00 18.92  ?  93   GLU A CB     1 
ATOM   1456  C CG     . GLU A 1 93  ? 21.745  -5.460  -13.137 1.00 23.51  ?  93   GLU A CG     1 
ATOM   1457  C CD     . GLU A 1 93  ? 22.718  -4.338  -12.733 1.00 26.71  ?  93   GLU A CD     1 
ATOM   1458  O OE1    . GLU A 1 93  ? 23.405  -3.735  -13.592 1.00 26.73  ?  93   GLU A OE1    1 
ATOM   1459  O OE2    . GLU A 1 93  ? 22.802  -4.080  -11.520 1.00 29.49  -1 93   GLU A OE2    1 
ATOM   1460  H H      . GLU A 1 93  ? 21.686  -6.671  -16.858 1.00 17.45  ?  93   GLU A H      1 
ATOM   1461  H HA     . GLU A 1 93  ? 21.696  -7.693  -14.462 1.00 20.05  ?  93   GLU A HA     1 
ATOM   1462  H HB2    . GLU A 1 93  ? 22.464  -5.490  -15.044 1.00 22.70  ?  93   GLU A HB2    1 
ATOM   1463  H HB3    . GLU A 1 93  ? 20.945  -5.031  -14.962 1.00 22.70  ?  93   GLU A HB3    1 
ATOM   1464  H HG2    . GLU A 1 93  ? 20.874  -5.237  -12.772 1.00 28.21  ?  93   GLU A HG2    1 
ATOM   1465  H HG3    . GLU A 1 93  ? 22.069  -6.285  -12.743 1.00 28.21  ?  93   GLU A HG3    1 
ATOM   1466  N N      . PRO A 1 94  ? 18.689  -6.932  -15.360 1.00 14.89  ?  94   PRO A N      1 
ATOM   1467  C CA     . PRO A 1 94  ? 17.306  -7.307  -14.980 1.00 15.65  ?  94   PRO A CA     1 
ATOM   1468  C C      . PRO A 1 94  ? 17.084  -8.802  -14.872 1.00 15.21  ?  94   PRO A C      1 
ATOM   1469  O O      . PRO A 1 94  ? 16.375  -9.251  -13.968 1.00 15.05  ?  94   PRO A O      1 
ATOM   1470  C CB     . PRO A 1 94  ? 16.446  -6.669  -16.079 1.00 16.20  ?  94   PRO A CB     1 
ATOM   1471  C CG     . PRO A 1 94  ? 17.287  -5.578  -16.646 1.00 18.57  ?  94   PRO A CG     1 
ATOM   1472  C CD     . PRO A 1 94  ? 18.722  -6.001  -16.498 1.00 16.21  ?  94   PRO A CD     1 
ATOM   1473  H HA     . PRO A 1 94  ? 17.086  -6.895  -14.129 1.00 18.77  ?  94   PRO A HA     1 
ATOM   1474  H HB2    . PRO A 1 94  ? 16.234  -7.330  -16.756 1.00 19.44  ?  94   PRO A HB2    1 
ATOM   1475  H HB3    . PRO A 1 94  ? 15.630  -6.314  -15.694 1.00 19.44  ?  94   PRO A HB3    1 
ATOM   1476  H HG2    . PRO A 1 94  ? 17.065  -5.454  -17.582 1.00 22.28  ?  94   PRO A HG2    1 
ATOM   1477  H HG3    . PRO A 1 94  ? 17.123  -4.758  -16.155 1.00 22.28  ?  94   PRO A HG3    1 
ATOM   1478  H HD2    . PRO A 1 94  ? 19.034  -6.448  -17.300 1.00 19.44  ?  94   PRO A HD2    1 
ATOM   1479  H HD3    . PRO A 1 94  ? 19.288  -5.238  -16.303 1.00 19.44  ?  94   PRO A HD3    1 
ATOM   1480  N N      . GLN A 1 95  ? 17.678  -9.594  -15.772 1.00 13.60  ?  95   GLN A N      1 
ATOM   1481  C CA     . GLN A 1 95  ? 17.511  -11.042 -15.715 1.00 14.41  ?  95   GLN A CA     1 
ATOM   1482  C C      . GLN A 1 95  ? 18.058  -11.608 -14.415 1.00 15.00  ?  95   GLN A C      1 
ATOM   1483  O O      . GLN A 1 95  ? 17.432  -12.484 -13.799 1.00 14.90  ?  95   GLN A O      1 
ATOM   1484  C CB     . GLN A 1 95  ? 18.186  -11.682 -16.926 1.00 13.92  ?  95   GLN A CB     1 
ATOM   1485  C CG     . GLN A 1 95  ? 18.245  -13.187 -16.859 1.00 18.03  ?  95   GLN A CG     1 
ATOM   1486  C CD     . GLN A 1 95  ? 19.241  -13.780 -17.837 1.00 21.14  ?  95   GLN A CD     1 
ATOM   1487  O OE1    . GLN A 1 95  ? 20.359  -13.281 -17.993 1.00 20.58  ?  95   GLN A OE1    1 
ATOM   1488  N NE2    . GLN A 1 95  ? 18.821  -14.868 -18.532 1.00 23.14  ?  95   GLN A NE2    1 
ATOM   1489  H H      . GLN A 1 95  ? 18.176  -9.320  -16.417 1.00 16.32  ?  95   GLN A H      1 
ATOM   1490  H HA     . GLN A 1 95  ? 16.566  -11.259 -15.751 1.00 17.29  ?  95   GLN A HA     1 
ATOM   1491  H HB2    . GLN A 1 95  ? 17.690  -11.439 -17.724 1.00 16.70  ?  95   GLN A HB2    1 
ATOM   1492  H HB3    . GLN A 1 95  ? 19.096  -11.352 -16.987 1.00 16.70  ?  95   GLN A HB3    1 
ATOM   1493  H HG2    . GLN A 1 95  ? 18.508  -13.454 -15.965 1.00 21.63  ?  95   GLN A HG2    1 
ATOM   1494  H HG3    . GLN A 1 95  ? 17.369  -13.547 -17.069 1.00 21.63  ?  95   GLN A HG3    1 
ATOM   1495  H HE21   . GLN A 1 95  ? 18.030  -15.181 -18.405 1.00 27.77  ?  95   GLN A HE21   1 
ATOM   1496  H HE22   . GLN A 1 95  ? 19.346  -15.244 -19.100 1.00 27.77  ?  95   GLN A HE22   1 
ATOM   1497  N N      . ILE A 1 96  ? 19.233  -11.138 -13.995 1.00 14.89  ?  96   ILE A N      1 
ATOM   1498  C CA     . ILE A 1 96  ? 19.832  -11.597 -12.741 1.00 13.02  ?  96   ILE A CA     1 
ATOM   1499  C C      . ILE A 1 96  ? 18.938  -11.242 -11.564 1.00 14.06  ?  96   ILE A C      1 
ATOM   1500  O O      . ILE A 1 96  ? 18.646  -12.079 -10.696 1.00 14.40  ?  96   ILE A O      1 
ATOM   1501  C CB     . ILE A 1 96  ? 21.239  -11.001 -12.584 1.00 14.29  ?  96   ILE A CB     1 
ATOM   1502  C CG1    . ILE A 1 96  ? 22.134  -11.443 -13.740 1.00 15.03  ?  96   ILE A CG1    1 
ATOM   1503  C CG2    . ILE A 1 96  ? 21.835  -11.437 -11.267 1.00 15.83  ?  96   ILE A CG2    1 
ATOM   1504  C CD1    . ILE A 1 96  ? 23.477  -10.695 -13.816 1.00 15.76  ?  96   ILE A CD1    1 
ATOM   1505  H H      A ILE A 1 96  ? 19.705  -10.554 -14.415 0.74 17.87  ?  96   ILE A H      1 
ATOM   1506  H H      B ILE A 1 96  ? 19.705  -10.554 -14.415 0.26 17.87  ?  96   ILE A H      1 
ATOM   1507  H HA     . ILE A 1 96  ? 19.912  -12.563 -12.767 1.00 15.62  ?  96   ILE A HA     1 
ATOM   1508  H HB     . ILE A 1 96  ? 21.171  -10.034 -12.598 1.00 17.14  ?  96   ILE A HB     1 
ATOM   1509  H HG12   . ILE A 1 96  ? 22.328  -12.388 -13.639 1.00 18.03  ?  96   ILE A HG12   1 
ATOM   1510  H HG13   . ILE A 1 96  ? 21.663  -11.289 -14.574 1.00 18.03  ?  96   ILE A HG13   1 
ATOM   1511  H HG21   . ILE A 1 96  ? 22.772  -11.187 -11.247 1.00 19.00  ?  96   ILE A HG21   1 
ATOM   1512  H HG22   . ILE A 1 96  ? 21.360  -10.998 -10.545 1.00 19.00  ?  96   ILE A HG22   1 
ATOM   1513  H HG23   . ILE A 1 96  ? 21.748  -12.400 -11.184 1.00 19.00  ?  96   ILE A HG23   1 
ATOM   1514  H HD11   . ILE A 1 96  ? 23.934  -10.949 -14.633 1.00 18.91  ?  96   ILE A HD11   1 
ATOM   1515  H HD12   . ILE A 1 96  ? 23.306  -9.740  -13.815 1.00 18.91  ?  96   ILE A HD12   1 
ATOM   1516  H HD13   . ILE A 1 96  ? 24.016  -10.935 -13.047 1.00 18.91  ?  96   ILE A HD13   1 
ATOM   1517  N N      . GLN A 1 97  ? 18.500  -9.983  -11.510 1.00 13.81  ?  97   GLN A N      1 
ATOM   1518  C CA     . GLN A 1 97  ? 17.632  -9.552  -10.419 1.00 14.11  ?  97   GLN A CA     1 
ATOM   1519  C C      . GLN A 1 97  ? 16.336  -10.348 -10.395 1.00 13.77  ?  97   GLN A C      1 
ATOM   1520  O O      . GLN A 1 97  ? 15.839  -10.714 -9.315  1.00 14.73  ?  97   GLN A O      1 
ATOM   1521  C CB     . GLN A 1 97  ? 17.356  -8.056  -10.572 1.00 15.21  ?  97   GLN A CB     1 
ATOM   1522  C CG     . GLN A 1 97  ? 18.590  -7.171  -10.399 1.00 17.79  ?  97   GLN A CG     1 
ATOM   1523  C CD     . GLN A 1 97  ? 18.370  -5.745  -10.851 1.00 23.84  ?  97   GLN A CD     1 
ATOM   1524  O OE1    . GLN A 1 97  ? 17.565  -5.482  -11.746 1.00 26.96  ?  97   GLN A OE1    1 
ATOM   1525  N NE2    . GLN A 1 97  ? 19.116  -4.822  -10.280 1.00 25.04  ?  97   GLN A NE2    1 
ATOM   1526  H H      . GLN A 1 97  ? 18.688  -9.368  -12.081 1.00 16.57  ?  97   GLN A H      1 
ATOM   1527  H HA     . GLN A 1 97  ? 18.075  -9.700  -9.569  1.00 16.93  ?  97   GLN A HA     1 
ATOM   1528  H HB2    . GLN A 1 97  ? 17.001  -7.895  -11.461 1.00 18.25  ?  97   GLN A HB2    1 
ATOM   1529  H HB3    . GLN A 1 97  ? 16.707  -7.790  -9.903  1.00 18.25  ?  97   GLN A HB3    1 
ATOM   1530  H HG2    . GLN A 1 97  ? 18.834  -7.152  -9.461  1.00 21.35  ?  97   GLN A HG2    1 
ATOM   1531  H HG3    . GLN A 1 97  ? 19.318  -7.540  -10.924 1.00 21.35  ?  97   GLN A HG3    1 
ATOM   1532  H HE21   . GLN A 1 97  ? 19.693  -5.044  -9.683  1.00 30.04  ?  97   GLN A HE21   1 
ATOM   1533  H HE22   . GLN A 1 97  ? 19.026  -3.997  -10.505 1.00 30.04  ?  97   GLN A HE22   1 
ATOM   1534  N N      . LEU A 1 98  ? 15.770  -10.631 -11.573 1.00 12.35  ?  98   LEU A N      1 
ATOM   1535  C CA     . LEU A 1 98  ? 14.493  -11.318 -11.616 1.00 13.65  ?  98   LEU A CA     1 
ATOM   1536  C C      . LEU A 1 98  ? 14.627  -12.768 -11.162 1.00 13.26  ?  98   LEU A C      1 
ATOM   1537  O O      . LEU A 1 98  ? 13.746  -13.295 -10.486 1.00 13.14  ?  98   LEU A O      1 
ATOM   1538  C CB     . LEU A 1 98  ? 13.898  -11.232 -13.021 1.00 14.45  ?  98   LEU A CB     1 
ATOM   1539  C CG     . LEU A 1 98  ? 12.510  -11.852 -13.166 1.00 14.00  ?  98   LEU A CG     1 
ATOM   1540  C CD1    . LEU A 1 98  ? 11.510  -11.225 -12.211 1.00 13.90  ?  98   LEU A CD1    1 
ATOM   1541  C CD2    . LEU A 1 98  ? 12.002  -11.716 -14.573 1.00 13.03  ?  98   LEU A CD2    1 
ATOM   1542  H H      . LEU A 1 98  ? 16.102  -10.438 -12.342 1.00 14.82  ?  98   LEU A H      1 
ATOM   1543  H HA     . LEU A 1 98  ? 13.877  -10.878 -11.010 1.00 16.38  ?  98   LEU A HA     1 
ATOM   1544  H HB2    . LEU A 1 98  ? 13.829  -10.297 -13.268 1.00 17.34  ?  98   LEU A HB2    1 
ATOM   1545  H HB3    . LEU A 1 98  ? 14.491  -11.694 -13.634 1.00 17.34  ?  98   LEU A HB3    1 
ATOM   1546  H HG     . LEU A 1 98  ? 12.591  -12.793 -12.948 1.00 16.80  ?  98   LEU A HG     1 
ATOM   1547  H HD11   . LEU A 1 98  ? 10.627  -11.579 -12.400 1.00 16.68  ?  98   LEU A HD11   1 
ATOM   1548  H HD12   . LEU A 1 98  ? 11.765  -11.441 -11.300 1.00 16.68  ?  98   LEU A HD12   1 
ATOM   1549  H HD13   . LEU A 1 98  ? 11.514  -10.263 -12.336 1.00 16.68  ?  98   LEU A HD13   1 
ATOM   1550  H HD21   . LEU A 1 98  ? 11.160  -12.191 -14.652 1.00 15.64  ?  98   LEU A HD21   1 
ATOM   1551  H HD22   . LEU A 1 98  ? 11.872  -10.776 -14.773 1.00 15.64  ?  98   LEU A HD22   1 
ATOM   1552  H HD23   . LEU A 1 98  ? 12.654  -12.097 -15.183 1.00 15.64  ?  98   LEU A HD23   1 
ATOM   1553  N N      . SER A 1 99  ? 15.730  -13.426 -11.508 1.00 12.93  ?  99   SER A N      1 
ATOM   1554  C CA     . SER A 1 99  ? 15.940  -14.788 -11.038 1.00 12.86  ?  99   SER A CA     1 
ATOM   1555  C C      . SER A 1 99  ? 15.939  -14.821 -9.521  1.00 14.93  ?  99   SER A C      1 
ATOM   1556  O O      . SER A 1 99  ? 15.310  -15.700 -8.917  1.00 14.18  ?  99   SER A O      1 
ATOM   1557  C CB     . SER A 1 99  ? 17.237  -15.341 -11.613 1.00 13.83  ?  99   SER A CB     1 
ATOM   1558  O OG     . SER A 1 99  ? 17.089  -15.523 -13.009 1.00 14.00  ?  99   SER A OG     1 
ATOM   1559  H H      . SER A 1 99  ? 16.359  -13.115 -12.005 1.00 15.52  ?  99   SER A H      1 
ATOM   1560  H HA     . SER A 1 99  ? 15.224  -15.363 -11.351 1.00 15.43  ?  99   SER A HA     1 
ATOM   1561  H HB2    . SER A 1 99  ? 17.958  -14.714 -11.444 1.00 16.59  ?  99   SER A HB2    1 
ATOM   1562  H HB3    . SER A 1 99  ? 17.436  -16.195 -11.196 1.00 16.59  ?  99   SER A HB3    1 
ATOM   1563  H HG     . SER A 1 99  ? 17.798  -15.834 -13.335 1.00 16.80  ?  99   SER A HG     1 
ATOM   1564  N N      . GLU A 1 100 ? 16.630  -13.860 -8.887  1.00 14.09  ?  100  GLU A N      1 
ATOM   1565  C CA     . GLU A 1 100 ? 16.623  -13.759 -7.431  1.00 14.27  ?  100  GLU A CA     1 
ATOM   1566  C C      . GLU A 1 100 ? 15.213  -13.586 -6.870  1.00 13.72  ?  100  GLU A C      1 
ATOM   1567  O O      . GLU A 1 100 ? 14.835  -14.247 -5.895  1.00 14.28  ?  100  GLU A O      1 
ATOM   1568  C CB     . GLU A 1 100 ? 17.547  -12.612 -6.987  1.00 14.20  ?  100  GLU A CB     1 
ATOM   1569  C CG     . GLU A 1 100 ? 19.010  -12.856 -7.343  1.00 15.31  ?  100  GLU A CG     1 
ATOM   1570  C CD     . GLU A 1 100 ? 19.923  -11.681 -7.044  1.00 14.89  ?  100  GLU A CD     1 
ATOM   1571  O OE1    . GLU A 1 100 ? 21.136  -11.922 -6.884  1.00 14.54  ?  100  GLU A OE1    1 
ATOM   1572  O OE2    . GLU A 1 100 ? 19.419  -10.526 -6.969  1.00 17.19  -1 100  GLU A OE2    1 
ATOM   1573  H H      . GLU A 1 100 ? 17.107  -13.260 -9.278  1.00 16.90  ?  100  GLU A H      1 
ATOM   1574  H HA     . GLU A 1 100 ? 16.970  -14.587 -7.063  1.00 17.12  ?  100  GLU A HA     1 
ATOM   1575  H HB2    . GLU A 1 100 ? 17.265  -11.793 -7.423  1.00 17.03  ?  100  GLU A HB2    1 
ATOM   1576  H HB3    . GLU A 1 100 ? 17.485  -12.512 -6.024  1.00 17.03  ?  100  GLU A HB3    1 
ATOM   1577  H HG2    . GLU A 1 100 ? 19.332  -13.616 -6.834  1.00 18.36  ?  100  GLU A HG2    1 
ATOM   1578  H HG3    . GLU A 1 100 ? 19.072  -13.043 -8.293  1.00 18.36  ?  100  GLU A HG3    1 
ATOM   1579  N N      . LYS A 1 101 ? 14.420  -12.696 -7.462  1.00 14.67  ?  101  LYS A N      1 
ATOM   1580  C CA     . LYS A 1 101 ? 13.075  -12.441 -6.950  1.00 13.73  ?  101  LYS A CA     1 
ATOM   1581  C C      . LYS A 1 101 ? 12.170  -13.659 -7.118  1.00 14.48  ?  101  LYS A C      1 
ATOM   1582  O O      . LYS A 1 101 ? 11.361  -13.961 -6.244  1.00 15.52  ?  101  LYS A O      1 
ATOM   1583  C CB     . LYS A 1 101 ? 12.435  -11.254 -7.678  1.00 15.29  ?  101  LYS A CB     1 
ATOM   1584  C CG     . LYS A 1 101 ? 13.071  -9.915  -7.413  1.00 18.69  ?  101  LYS A CG     1 
ATOM   1585  C CD     . LYS A 1 101 ? 12.819  -9.402  -6.016  1.00 23.79  ?  101  LYS A CD     1 
ATOM   1586  C CE     . LYS A 1 101 ? 13.305  -7.962  -5.895  1.00 28.61  ?  101  LYS A CE     1 
ATOM   1587  N NZ     . LYS A 1 101 ? 13.239  -7.491  -4.504  1.00 33.46  ?  101  LYS A NZ     1 
ATOM   1588  H H      . LYS A 1 101 ? 14.631  -12.230 -8.153  1.00 17.60  ?  101  LYS A H      1 
ATOM   1589  H HA     . LYS A 1 101 ? 13.158  -12.230 -6.007  1.00 16.48  ?  101  LYS A HA     1 
ATOM   1590  H HB2    . LYS A 1 101 ? 12.489  -11.416 -8.633  1.00 18.35  ?  101  LYS A HB2    1 
ATOM   1591  H HB3    . LYS A 1 101 ? 11.506  -11.193 -7.404  1.00 18.35  ?  101  LYS A HB3    1 
ATOM   1592  H HG2    . LYS A 1 101 ? 14.030  -9.994  -7.532  1.00 22.42  ?  101  LYS A HG2    1 
ATOM   1593  H HG3    . LYS A 1 101 ? 12.710  -9.267  -8.038  1.00 22.42  ?  101  LYS A HG3    1 
ATOM   1594  H HD2    . LYS A 1 101 ? 11.868  -9.426  -5.825  1.00 28.55  ?  101  LYS A HD2    1 
ATOM   1595  H HD3    . LYS A 1 101 ? 13.300  -9.948  -5.375  1.00 28.55  ?  101  LYS A HD3    1 
ATOM   1596  H HE2    . LYS A 1 101 ? 14.226  -7.907  -6.193  1.00 34.32  ?  101  LYS A HE2    1 
ATOM   1597  H HE3    . LYS A 1 101 ? 12.745  -7.386  -6.440  1.00 34.32  ?  101  LYS A HE3    1 
ATOM   1598  H HZ1    . LYS A 1 101 ? 13.515  -6.646  -4.456  1.00 40.15  ?  101  LYS A HZ1    1 
ATOM   1599  H HZ2    . LYS A 1 101 ? 12.402  -7.539  -4.206  1.00 40.15  ?  101  LYS A HZ2    1 
ATOM   1600  H HZ3    . LYS A 1 101 ? 13.760  -7.995  -3.987  1.00 40.15  ?  101  LYS A HZ3    1 
ATOM   1601  N N      . ILE A 1 102 ? 12.248  -14.322 -8.262  1.00 14.37  ?  102  ILE A N      1 
ATOM   1602  C CA     . ILE A 1 102 ? 11.436  -15.510 -8.479  1.00 14.40  ?  102  ILE A CA     1 
ATOM   1603  C C      . ILE A 1 102 ? 11.761  -16.563 -7.434  1.00 13.45  ?  102  ILE A C      1 
ATOM   1604  O O      . ILE A 1 102 ? 10.865  -17.176 -6.843  1.00 14.69  ?  102  ILE A O      1 
ATOM   1605  C CB     . ILE A 1 102 ? 11.644  -16.048 -9.902  1.00 12.84  ?  102  ILE A CB     1 
ATOM   1606  C CG1    . ILE A 1 102 ? 11.037  -15.082 -10.921 1.00 13.02  ?  102  ILE A CG1    1 
ATOM   1607  C CG2    . ILE A 1 102 ? 11.048  -17.434 -10.030 1.00 14.36  ?  102  ILE A CG2    1 
ATOM   1608  C CD1    . ILE A 1 102 ? 11.450  -15.424 -12.345 1.00 15.02  ?  102  ILE A CD1    1 
ATOM   1609  H H      . ILE A 1 102 ? 12.757  -14.111 -8.922  1.00 17.24  ?  102  ILE A H      1 
ATOM   1610  H HA     . ILE A 1 102 ? 10.501  -15.269 -8.384  1.00 17.28  ?  102  ILE A HA     1 
ATOM   1611  H HB     . ILE A 1 102 ? 12.595  -16.115 -10.081 1.00 15.40  ?  102  ILE A HB     1 
ATOM   1612  H HG12   . ILE A 1 102 ? 10.070  -15.127 -10.866 1.00 15.63  ?  102  ILE A HG12   1 
ATOM   1613  H HG13   . ILE A 1 102 ? 11.340  -14.181 -10.725 1.00 15.63  ?  102  ILE A HG13   1 
ATOM   1614  H HG21   . ILE A 1 102 ? 11.028  -17.685 -10.967 1.00 17.23  ?  102  ILE A HG21   1 
ATOM   1615  H HG22   . ILE A 1 102 ? 11.596  -18.061 -9.531  1.00 17.23  ?  102  ILE A HG22   1 
ATOM   1616  H HG23   . ILE A 1 102 ? 10.146  -17.425 -9.671  1.00 17.23  ?  102  ILE A HG23   1 
ATOM   1617  H HD11   . ILE A 1 102 ? 11.157  -14.715 -12.938 1.00 18.03  ?  102  ILE A HD11   1 
ATOM   1618  H HD12   . ILE A 1 102 ? 12.416  -15.508 -12.382 1.00 18.03  ?  102  ILE A HD12   1 
ATOM   1619  H HD13   . ILE A 1 102 ? 11.035  -16.263 -12.601 1.00 18.03  ?  102  ILE A HD13   1 
ATOM   1620  N N      . LEU A 1 103 ? 13.050  -16.811 -7.209  1.00 12.86  ?  103  LEU A N      1 
ATOM   1621  C CA     . LEU A 1 103 ? 13.443  -17.848 -6.261  1.00 14.58  ?  103  LEU A CA     1 
ATOM   1622  C C      . LEU A 1 103 ? 13.034  -17.483 -4.835  1.00 13.74  ?  103  LEU A C      1 
ATOM   1623  O O      . LEU A 1 103 ? 12.669  -18.365 -4.042  1.00 15.73  ?  103  LEU A O      1 
ATOM   1624  C CB     . LEU A 1 103 ? 14.948  -18.113 -6.373  1.00 13.66  ?  103  LEU A CB     1 
ATOM   1625  C CG     . LEU A 1 103 ? 15.330  -18.805 -7.686  1.00 13.93  ?  103  LEU A CG     1 
ATOM   1626  C CD1    . LEU A 1 103 ? 16.820  -18.832 -7.941  1.00 15.10  ?  103  LEU A CD1    1 
ATOM   1627  C CD2    . LEU A 1 103 ? 14.799  -20.238 -7.709  1.00 15.61  ?  103  LEU A CD2    1 
ATOM   1628  H H      . LEU A 1 103 ? 13.707  -16.402 -7.584  1.00 15.43  ?  103  LEU A H      1 
ATOM   1629  H HA     . LEU A 1 103 ? 12.987  -18.675 -6.482  1.00 17.50  ?  103  LEU A HA     1 
ATOM   1630  H HB2    . LEU A 1 103 ? 15.420  -17.267 -6.330  1.00 16.39  ?  103  LEU A HB2    1 
ATOM   1631  H HB3    . LEU A 1 103 ? 15.223  -18.685 -5.640  1.00 16.39  ?  103  LEU A HB3    1 
ATOM   1632  H HG     . LEU A 1 103 ? 14.927  -18.284 -8.398  1.00 16.71  ?  103  LEU A HG     1 
ATOM   1633  H HD11   . LEU A 1 103 ? 16.990  -19.304 -8.770  1.00 18.12  ?  103  LEU A HD11   1 
ATOM   1634  H HD12   . LEU A 1 103 ? 17.146  -17.920 -8.006  1.00 18.12  ?  103  LEU A HD12   1 
ATOM   1635  H HD13   . LEU A 1 103 ? 17.258  -19.287 -7.205  1.00 18.12  ?  103  LEU A HD13   1 
ATOM   1636  H HD21   . LEU A 1 103 ? 15.179  -20.704 -8.471  1.00 18.72  ?  103  LEU A HD21   1 
ATOM   1637  H HD22   . LEU A 1 103 ? 15.056  -20.684 -6.887  1.00 18.72  ?  103  LEU A HD22   1 
ATOM   1638  H HD23   . LEU A 1 103 ? 13.832  -20.216 -7.785  1.00 18.72  ?  103  LEU A HD23   1 
ATOM   1639  N N      . GLU A 1 104 ? 13.115  -16.204 -4.481  1.00 15.04  ?  104  GLU A N      1 
ATOM   1640  C CA     . GLU A 1 104 ? 12.669  -15.782 -3.158  1.00 16.50  ?  104  GLU A CA     1 
ATOM   1641  C C      . GLU A 1 104 ? 11.204  -16.131 -2.959  1.00 15.31  ?  104  GLU A C      1 
ATOM   1642  O O      . GLU A 1 104 ? 10.805  -16.616 -1.884  1.00 17.10  ?  104  GLU A O      1 
ATOM   1643  C CB     . GLU A 1 104 ? 12.890  -14.279 -3.026  1.00 18.63  ?  104  GLU A CB     1 
ATOM   1644  C CG     . GLU A 1 104 ? 12.430  -13.669 -1.731  1.00 28.10  ?  104  GLU A CG     1 
ATOM   1645  C CD     . GLU A 1 104 ? 12.789  -12.188 -1.640  1.00 37.24  ?  104  GLU A CD     1 
ATOM   1646  O OE1    . GLU A 1 104 ? 12.649  -11.467 -2.657  1.00 38.69  ?  104  GLU A OE1    1 
ATOM   1647  O OE2    . GLU A 1 104 ? 13.220  -11.761 -0.549  1.00 42.68  -1 104  GLU A OE2    1 
ATOM   1648  H H      . GLU A 1 104 ? 13.418  -15.570 -4.977  1.00 18.05  ?  104  GLU A H      1 
ATOM   1649  H HA     . GLU A 1 104 ? 13.182  -16.232 -2.468  1.00 19.79  ?  104  GLU A HA     1 
ATOM   1650  H HB2    . GLU A 1 104 ? 13.840  -14.102 -3.106  1.00 22.35  ?  104  GLU A HB2    1 
ATOM   1651  H HB3    . GLU A 1 104 ? 12.408  -13.836 -3.741  1.00 22.35  ?  104  GLU A HB3    1 
ATOM   1652  H HG2    . GLU A 1 104 ? 11.466  -13.752 -1.664  1.00 33.72  ?  104  GLU A HG2    1 
ATOM   1653  H HG3    . GLU A 1 104 ? 12.855  -14.131 -0.991  1.00 33.72  ?  104  GLU A HG3    1 
ATOM   1654  N N      . LEU A 1 105 ? 10.382  -15.910 -3.996  1.00 13.73  ?  105  LEU A N      1 
ATOM   1655  C CA     . LEU A 1 105 ? 8.953   -16.194 -3.889  1.00 14.49  ?  105  LEU A CA     1 
ATOM   1656  C C      . LEU A 1 105 ? 8.685   -17.694 -3.899  1.00 15.80  ?  105  LEU A C      1 
ATOM   1657  O O      . LEU A 1 105 ? 7.804   -18.175 -3.174  1.00 16.66  ?  105  LEU A O      1 
ATOM   1658  C CB     . LEU A 1 105 ? 8.198   -15.538 -5.045  1.00 15.87  ?  105  LEU A CB     1 
ATOM   1659  C CG     . LEU A 1 105 ? 8.066   -14.020 -4.951  1.00 17.88  ?  105  LEU A CG     1 
ATOM   1660  C CD1    . LEU A 1 105 ? 7.774   -13.411 -6.304  1.00 19.33  ?  105  LEU A CD1    1 
ATOM   1661  C CD2    . LEU A 1 105 ? 6.966   -13.657 -3.951  1.00 21.29  ?  105  LEU A CD2    1 
ATOM   1662  H H      . LEU A 1 105 ? 10.625  -15.601 -4.761  1.00 16.47  ?  105  LEU A H      1 
ATOM   1663  H HA     . LEU A 1 105 ? 8.632   -15.822 -3.053  1.00 17.38  ?  105  LEU A HA     1 
ATOM   1664  H HB2    . LEU A 1 105 ? 8.666   -15.739 -5.871  1.00 19.04  ?  105  LEU A HB2    1 
ATOM   1665  H HB3    . LEU A 1 105 ? 7.301   -15.907 -5.074  1.00 19.04  ?  105  LEU A HB3    1 
ATOM   1666  H HG     . LEU A 1 105 ? 8.907   -13.648 -4.641  1.00 21.46  ?  105  LEU A HG     1 
ATOM   1667  H HD11   . LEU A 1 105 ? 7.649   -12.455 -6.200  1.00 23.20  ?  105  LEU A HD11   1 
ATOM   1668  H HD12   . LEU A 1 105 ? 8.522   -13.584 -6.896  1.00 23.20  ?  105  LEU A HD12   1 
ATOM   1669  H HD13   . LEU A 1 105 ? 6.968   -13.813 -6.664  1.00 23.20  ?  105  LEU A HD13   1 
ATOM   1670  H HD21   . LEU A 1 105 ? 6.856   -12.693 -3.939  1.00 25.54  ?  105  LEU A HD21   1 
ATOM   1671  H HD22   . LEU A 1 105 ? 6.138   -14.081 -4.225  1.00 25.54  ?  105  LEU A HD22   1 
ATOM   1672  H HD23   . LEU A 1 105 ? 7.224   -13.972 -3.071  1.00 25.54  ?  105  LEU A HD23   1 
ATOM   1673  N N      . ALA A 1 106 ? 9.444   -18.450 -4.686  1.00 16.72  ?  106  ALA A N      1 
ATOM   1674  C CA     . ALA A 1 106 ? 9.156   -19.872 -4.830  1.00 16.78  ?  106  ALA A CA     1 
ATOM   1675  C C      . ALA A 1 106 ? 9.510   -20.629 -3.568  1.00 17.92  ?  106  ALA A C      1 
ATOM   1676  O O      . ALA A 1 106 ? 8.797   -21.562 -3.164  1.00 19.53  ?  106  ALA A O      1 
ATOM   1677  C CB     . ALA A 1 106 ? 9.920   -20.453 -6.020  1.00 17.78  ?  106  ALA A CB     1 
ATOM   1678  H H      . ALA A 1 106 ? 10.120  -18.172 -5.139  1.00 20.07  ?  106  ALA A H      1 
ATOM   1679  H HA     . ALA A 1 106 ? 8.207   -19.978 -5.001  1.00 20.14  ?  106  ALA A HA     1 
ATOM   1680  H HB1    . ALA A 1 106 ? 9.691   -21.391 -6.114  1.00 21.33  ?  106  ALA A HB1    1 
ATOM   1681  H HB2    . ALA A 1 106 ? 9.670   -19.970 -6.823  1.00 21.33  ?  106  ALA A HB2    1 
ATOM   1682  H HB3    . ALA A 1 106 ? 10.872  -20.360 -5.861  1.00 21.33  ?  106  ALA A HB3    1 
ATOM   1683  N N      . GLY A 1 107 ? 10.605  -20.240 -2.934  1.00 17.10  ?  107  GLY A N      1 
ATOM   1684  C CA     . GLY A 1 107 ? 10.928  -20.724 -1.627  1.00 19.65  ?  107  GLY A CA     1 
ATOM   1685  C C      . GLY A 1 107 ? 12.102  -21.666 -1.610  1.00 21.49  ?  107  GLY A C      1 
ATOM   1686  O O      . GLY A 1 107 ? 12.713  -21.990 -2.646  1.00 20.85  ?  107  GLY A O      1 
ATOM   1687  H H      . GLY A 1 107 ? 11.180  -19.687 -3.256  1.00 20.51  ?  107  GLY A H      1 
ATOM   1688  H HA2    . GLY A 1 107 ? 11.139  -19.971 -1.053  1.00 23.57  ?  107  GLY A HA2    1 
ATOM   1689  H HA3    . GLY A 1 107 ? 10.161  -21.193 -1.263  1.00 23.57  ?  107  GLY A HA3    1 
ATOM   1690  N N      . PRO A 1 108 ? 12.424  -22.136 -0.411  1.00 25.01  ?  108  PRO A N      1 
ATOM   1691  C CA     . PRO A 1 108 ? 13.478  -23.127 -0.277  1.00 28.39  ?  108  PRO A CA     1 
ATOM   1692  C C      . PRO A 1 108 ? 13.155  -24.363 -1.087  1.00 27.03  ?  108  PRO A C      1 
ATOM   1693  O O      . PRO A 1 108 ? 11.992  -24.765 -1.269  1.00 28.76  ?  108  PRO A O      1 
ATOM   1694  C CB     . PRO A 1 108 ? 13.493  -23.436 1.224   1.00 29.61  ?  108  PRO A CB     1 
ATOM   1695  C CG     . PRO A 1 108 ? 12.878  -22.283 1.844   1.00 27.85  ?  108  PRO A CG     1 
ATOM   1696  C CD     . PRO A 1 108 ? 11.841  -21.790 0.891   1.00 25.55  ?  108  PRO A CD     1 
ATOM   1697  H HA     . PRO A 1 108 ? 14.338  -22.764 -0.544  1.00 34.07  ?  108  PRO A HA     1 
ATOM   1698  H HB2    . PRO A 1 108 ? 12.981  -24.240 1.402   1.00 35.53  ?  108  PRO A HB2    1 
ATOM   1699  H HB3    . PRO A 1 108 ? 14.406  -23.549 1.530   1.00 35.53  ?  108  PRO A HB3    1 
ATOM   1700  H HG2    . PRO A 1 108 ? 12.471  -22.546 2.684   1.00 33.41  ?  108  PRO A HG2    1 
ATOM   1701  H HG3    . PRO A 1 108 ? 13.550  -21.601 1.999   1.00 33.41  ?  108  PRO A HG3    1 
ATOM   1702  H HD2    . PRO A 1 108 ? 10.996  -22.247 1.028   1.00 30.65  ?  108  PRO A HD2    1 
ATOM   1703  H HD3    . PRO A 1 108 ? 11.718  -20.832 0.975   1.00 30.65  ?  108  PRO A HD3    1 
ATOM   1704  N N      . GLY A 1 109 ? 14.208  -24.952 -1.583  1.00 22.39  ?  109  GLY A N      1 
ATOM   1705  C CA     . GLY A 1 109 ? 14.095  -26.116 -2.413  1.00 18.63  ?  109  GLY A CA     1 
ATOM   1706  C C      . GLY A 1 109 ? 14.164  -25.802 -3.872  1.00 15.26  ?  109  GLY A C      1 
ATOM   1707  O O      . GLY A 1 109 ? 14.351  -26.722 -4.659  1.00 17.72  ?  109  GLY A O      1 
ATOM   1708  H H      . GLY A 1 109 ? 15.016  -24.690 -1.449  1.00 26.87  ?  109  GLY A H      1 
ATOM   1709  H HA2    . GLY A 1 109 ? 14.815  -26.731 -2.200  1.00 22.35  ?  109  GLY A HA2    1 
ATOM   1710  H HA3    . GLY A 1 109 ? 13.246  -26.551 -2.236  1.00 22.35  ?  109  GLY A HA3    1 
ATOM   1711  N N      . MET A 1 110 ? 14.021  -24.543 -4.261  1.00 15.10  ?  110  MET A N      1 
ATOM   1712  C CA     . MET A 1 110 ? 14.158  -24.149 -5.655  1.00 13.25  ?  110  MET A CA     1 
ATOM   1713  C C      . MET A 1 110 ? 15.530  -23.528 -5.873  1.00 13.02  ?  110  MET A C      1 
ATOM   1714  O O      . MET A 1 110 ? 16.023  -22.768 -5.031  1.00 15.77  ?  110  MET A O      1 
ATOM   1715  C CB     . MET A 1 110 ? 13.042  -23.217 -6.106  1.00 14.29  ?  110  MET A CB     1 
ATOM   1716  C CG     . MET A 1 110 ? 11.681  -23.905 -6.229  1.00 14.64  ?  110  MET A CG     1 
ATOM   1717  S SD     . MET A 1 110 ? 11.683  -25.078 -7.616  1.00 16.04  ?  110  MET A SD     1 
ATOM   1718  C CE     . MET A 1 110 ? 11.090  -26.540 -6.809  1.00 19.10  ?  110  MET A CE     1 
ATOM   1719  H H      . MET A 1 110 ? 13.842  -23.892 -3.729  1.00 18.11  ?  110  MET A H      1 
ATOM   1720  H HA     . MET A 1 110 ? 14.079  -24.936 -6.217  1.00 15.89  ?  110  MET A HA     1 
ATOM   1721  H HB2    . MET A 1 110 ? 12.954  -22.498 -5.460  1.00 17.15  ?  110  MET A HB2    1 
ATOM   1722  H HB3    . MET A 1 110 ? 13.270  -22.854 -6.977  1.00 17.15  ?  110  MET A HB3    1 
ATOM   1723  H HG2    . MET A 1 110 ? 11.489  -24.392 -5.412  1.00 17.56  ?  110  MET A HG2    1 
ATOM   1724  H HG3    . MET A 1 110 ? 10.993  -23.239 -6.387  1.00 17.56  ?  110  MET A HG3    1 
ATOM   1725  H HE1    . MET A 1 110 ? 11.099  -27.275 -7.441  1.00 22.91  ?  110  MET A HE1    1 
ATOM   1726  H HE2    . MET A 1 110 ? 11.668  -26.742 -6.057  1.00 22.91  ?  110  MET A HE2    1 
ATOM   1727  H HE3    . MET A 1 110 ? 10.185  -26.383 -6.497  1.00 22.91  ?  110  MET A HE3    1 
ATOM   1728  N N      . SER A 1 111 ? 16.147  -23.872 -7.006  1.00 13.58  ?  111  SER A N      1 
ATOM   1729  C CA     . SER A 1 111 ? 17.549  -23.558 -7.248  1.00 12.65  ?  111  SER A CA     1 
ATOM   1730  C C      . SER A 1 111 ? 17.806  -22.561 -8.370  1.00 13.90  ?  111  SER A C      1 
ATOM   1731  O O      . SER A 1 111 ? 18.650  -21.686 -8.195  1.00 13.46  ?  111  SER A O      1 
ATOM   1732  C CB     . SER A 1 111 ? 18.313  -24.847 -7.550  1.00 14.55  ?  111  SER A CB     1 
ATOM   1733  O OG     . SER A 1 111 ? 19.722  -24.619 -7.639  1.00 15.40  ?  111  SER A OG     1 
ATOM   1734  H H      . SER A 1 111 ? 15.766  -24.291 -7.653  1.00 16.29  ?  111  SER A H      1 
ATOM   1735  H HA     . SER A 1 111 ? 17.893  -23.153 -6.436  1.00 15.18  ?  111  SER A HA     1 
ATOM   1736  H HB2    . SER A 1 111 ? 18.144  -25.484 -6.839  1.00 17.46  ?  111  SER A HB2    1 
ATOM   1737  H HB3    . SER A 1 111 ? 18.001  -25.203 -8.397  1.00 17.46  ?  111  SER A HB3    1 
ATOM   1738  H HG     . SER A 1 111 ? 20.106  -25.305 -7.937  1.00 18.48  ?  111  SER A HG     1 
ATOM   1739  N N      . LYS A 1 112 ? 17.175  -22.718 -9.544  1.00 13.54  ?  112  LYS A N      1 
ATOM   1740  C CA     . LYS A 1 112 ? 17.541  -21.942 -10.721 1.00 12.73  ?  112  LYS A CA     1 
ATOM   1741  C C      . LYS A 1 112 ? 16.301  -21.651 -11.554 1.00 12.51  ?  112  LYS A C      1 
ATOM   1742  O O      . LYS A 1 112 ? 15.289  -22.335 -11.431 1.00 13.29  ?  112  LYS A O      1 
ATOM   1743  C CB     . LYS A 1 112 ? 18.536  -22.706 -11.623 1.00 13.31  ?  112  LYS A CB     1 
ATOM   1744  C CG     . LYS A 1 112 ? 19.838  -23.113 -10.954 1.00 12.80  ?  112  LYS A CG     1 
ATOM   1745  C CD     . LYS A 1 112 ? 20.767  -21.930 -10.662 1.00 13.40  ?  112  LYS A CD     1 
ATOM   1746  C CE     . LYS A 1 112 ? 21.986  -22.365 -9.849  1.00 13.84  ?  112  LYS A CE     1 
ATOM   1747  N NZ     . LYS A 1 112 ? 21.653  -22.670 -8.396  1.00 15.34  ?  112  LYS A NZ     1 
ATOM   1748  H H      . LYS A 1 112 ? 16.531  -23.272 -9.677  1.00 16.25  ?  112  LYS A H      1 
ATOM   1749  H HA     . LYS A 1 112 ? 17.932  -21.110 -10.414 1.00 15.27  ?  112  LYS A HA     1 
ATOM   1750  H HB2    . LYS A 1 112 ? 18.105  -23.516 -11.937 1.00 15.97  ?  112  LYS A HB2    1 
ATOM   1751  H HB3    . LYS A 1 112 ? 18.763  -22.138 -12.377 1.00 15.97  ?  112  LYS A HB3    1 
ATOM   1752  H HG2    . LYS A 1 112 ? 19.636  -23.548 -10.111 1.00 15.35  ?  112  LYS A HG2    1 
ATOM   1753  H HG3    . LYS A 1 112 ? 20.313  -23.726 -11.538 1.00 15.35  ?  112  LYS A HG3    1 
ATOM   1754  H HD2    . LYS A 1 112 ? 21.078  -21.551 -11.499 1.00 16.08  ?  112  LYS A HD2    1 
ATOM   1755  H HD3    . LYS A 1 112 ? 20.284  -21.260 -10.153 1.00 16.08  ?  112  LYS A HD3    1 
ATOM   1756  H HE2    . LYS A 1 112 ? 22.359  -23.168 -10.245 1.00 16.61  ?  112  LYS A HE2    1 
ATOM   1757  H HE3    . LYS A 1 112 ? 22.644  -21.652 -9.862  1.00 16.61  ?  112  LYS A HE3    1 
ATOM   1758  H HZ1    . LYS A 1 112 ? 22.388  -22.925 -7.962  1.00 18.41  ?  112  LYS A HZ1    1 
ATOM   1759  H HZ2    . LYS A 1 112 ? 21.322  -21.944 -8.000  1.00 18.41  ?  112  LYS A HZ2    1 
ATOM   1760  H HZ3    . LYS A 1 112 ? 21.051  -23.323 -8.352  1.00 18.41  ?  112  LYS A HZ3    1 
ATOM   1761  N N      . VAL A 1 113 ? 16.411  -20.637 -12.424 1.00 12.54  ?  113  VAL A N      1 
ATOM   1762  C CA     . VAL A 1 113 ? 15.369  -20.256 -13.368 1.00 12.01  ?  113  VAL A CA     1 
ATOM   1763  C C      . VAL A 1 113 ? 15.926  -20.290 -14.789 1.00 12.54  ?  113  VAL A C      1 
ATOM   1764  O O      . VAL A 1 113 ? 17.010  -19.764 -15.052 1.00 12.84  ?  113  VAL A O      1 
ATOM   1765  C CB     . VAL A 1 113 ? 14.801  -18.860 -13.053 1.00 11.83  ?  113  VAL A CB     1 
ATOM   1766  C CG1    . VAL A 1 113 ? 13.699  -18.473 -14.041 1.00 12.76  ?  113  VAL A CG1    1 
ATOM   1767  C CG2    . VAL A 1 113 ? 14.287  -18.796 -11.601 1.00 13.66  ?  113  VAL A CG2    1 
ATOM   1768  H H      . VAL A 1 113 ? 17.111  -20.141 -12.481 1.00 15.05  ?  113  VAL A H      1 
ATOM   1769  H HA     . VAL A 1 113 ? 14.656  -20.912 -13.313 1.00 14.41  ?  113  VAL A HA     1 
ATOM   1770  H HB     . VAL A 1 113 ? 15.516  -18.211 -13.148 1.00 14.19  ?  113  VAL A HB     1 
ATOM   1771  H HG11   . VAL A 1 113 ? 13.310  -17.629 -13.765 1.00 15.31  ?  113  VAL A HG11   1 
ATOM   1772  H HG12   . VAL A 1 113 ? 14.085  -18.386 -14.926 1.00 15.31  ?  113  VAL A HG12   1 
ATOM   1773  H HG13   . VAL A 1 113 ? 13.020  -19.165 -14.043 1.00 15.31  ?  113  VAL A HG13   1 
ATOM   1774  H HG21   . VAL A 1 113 ? 13.925  -17.912 -11.433 1.00 16.39  ?  113  VAL A HG21   1 
ATOM   1775  H HG22   . VAL A 1 113 ? 13.595  -19.465 -11.481 1.00 16.39  ?  113  VAL A HG22   1 
ATOM   1776  H HG23   . VAL A 1 113 ? 15.025  -18.972 -10.997 1.00 16.39  ?  113  VAL A HG23   1 
ATOM   1777  N N      . TYR A 1 114 ? 15.159  -20.887 -15.712 1.00 12.55  ?  114  TYR A N      1 
ATOM   1778  C CA     . TYR A 1 114 ? 15.449  -20.818 -17.149 1.00 12.73  ?  114  TYR A CA     1 
ATOM   1779  C C      . TYR A 1 114 ? 14.310  -20.070 -17.835 1.00 11.50  ?  114  TYR A C      1 
ATOM   1780  O O      . TYR A 1 114 ? 13.143  -20.396 -17.601 1.00 12.49  ?  114  TYR A O      1 
ATOM   1781  C CB     . TYR A 1 114 ? 15.575  -22.208 -17.791 1.00 13.88  ?  114  TYR A CB     1 
ATOM   1782  C CG     . TYR A 1 114 ? 15.739  -22.105 -19.301 1.00 11.68  ?  114  TYR A CG     1 
ATOM   1783  C CD1    . TYR A 1 114 ? 16.958  -21.788 -19.861 1.00 13.01  ?  114  TYR A CD1    1 
ATOM   1784  C CD2    . TYR A 1 114 ? 14.648  -22.280 -20.147 1.00 11.31  ?  114  TYR A CD2    1 
ATOM   1785  C CE1    . TYR A 1 114 ? 17.101  -21.655 -21.232 1.00 13.31  ?  114  TYR A CE1    1 
ATOM   1786  C CE2    . TYR A 1 114 ? 14.773  -22.139 -21.524 1.00 12.62  ?  114  TYR A CE2    1 
ATOM   1787  C CZ     . TYR A 1 114 ? 16.019  -21.816 -22.046 1.00 12.98  ?  114  TYR A CZ     1 
ATOM   1788  O OH     . TYR A 1 114 ? 16.204  -21.665 -23.412 1.00 15.27  ?  114  TYR A OH     1 
ATOM   1789  H H      . TYR A 1 114 ? 14.456  -21.344 -15.523 1.00 15.05  ?  114  TYR A H      1 
ATOM   1790  H HA     . TYR A 1 114 ? 16.289  -20.349 -17.271 1.00 15.27  ?  114  TYR A HA     1 
ATOM   1791  H HB2    . TYR A 1 114 ? 16.352  -22.661 -17.428 1.00 16.66  ?  114  TYR A HB2    1 
ATOM   1792  H HB3    . TYR A 1 114 ? 14.774  -22.722 -17.604 1.00 16.66  ?  114  TYR A HB3    1 
ATOM   1793  H HD1    . TYR A 1 114 ? 17.697  -21.662 -19.310 1.00 15.61  ?  114  TYR A HD1    1 
ATOM   1794  H HD2    . TYR A 1 114 ? 13.820  -22.495 -19.784 1.00 13.57  ?  114  TYR A HD2    1 
ATOM   1795  H HE1    . TYR A 1 114 ? 17.933  -21.456 -21.597 1.00 15.97  ?  114  TYR A HE1    1 
ATOM   1796  H HE2    . TYR A 1 114 ? 14.039  -22.259 -22.083 1.00 15.14  ?  114  TYR A HE2    1 
ATOM   1797  H HH     . TYR A 1 114 ? 15.469  -21.743 -23.811 1.00 18.32  ?  114  TYR A HH     1 
ATOM   1798  N N      . TYR A 1 115 ? 14.633  -19.107 -18.709 1.00 11.41  ?  115  TYR A N      1 
ATOM   1799  C CA     . TYR A 1 115 ? 13.634  -18.216 -19.289 1.00 11.73  ?  115  TYR A CA     1 
ATOM   1800  C C      . TYR A 1 115 ? 13.230  -18.551 -20.719 1.00 12.32  ?  115  TYR A C      1 
ATOM   1801  O O      . TYR A 1 115 ? 14.076  -18.824 -21.589 1.00 12.13  ?  115  TYR A O      1 
ATOM   1802  C CB     . TYR A 1 115 ? 14.106  -16.758 -19.273 1.00 12.56  ?  115  TYR A CB     1 
ATOM   1803  C CG     . TYR A 1 115 ? 14.270  -16.190 -17.888 1.00 11.85  ?  115  TYR A CG     1 
ATOM   1804  C CD1    . TYR A 1 115 ? 13.198  -15.628 -17.224 1.00 11.88  ?  115  TYR A CD1    1 
ATOM   1805  C CD2    . TYR A 1 115 ? 15.501  -16.219 -17.246 1.00 11.86  ?  115  TYR A CD2    1 
ATOM   1806  C CE1    . TYR A 1 115 ? 13.319  -15.138 -15.937 1.00 13.63  ?  115  TYR A CE1    1 
ATOM   1807  C CE2    . TYR A 1 115 ? 15.647  -15.697 -15.970 1.00 13.19  ?  115  TYR A CE2    1 
ATOM   1808  C CZ     . TYR A 1 115 ? 14.546  -15.162 -15.327 1.00 13.56  ?  115  TYR A CZ     1 
ATOM   1809  O OH     . TYR A 1 115 ? 14.677  -14.663 -14.056 1.00 15.17  ?  115  TYR A OH     1 
ATOM   1810  H H      . TYR A 1 115 ? 15.435  -18.955 -18.981 1.00 13.69  ?  115  TYR A H      1 
ATOM   1811  H HA     . TYR A 1 115 ? 12.844  -18.337 -18.738 1.00 14.07  ?  115  TYR A HA     1 
ATOM   1812  H HB2    . TYR A 1 115 ? 14.965  -16.703 -19.719 1.00 15.07  ?  115  TYR A HB2    1 
ATOM   1813  H HB3    . TYR A 1 115 ? 13.454  -16.213 -19.741 1.00 15.07  ?  115  TYR A HB3    1 
ATOM   1814  H HD1    . TYR A 1 115 ? 12.375  -15.577 -17.653 1.00 14.25  ?  115  TYR A HD1    1 
ATOM   1815  H HD2    . TYR A 1 115 ? 16.236  -16.592 -17.677 1.00 14.23  ?  115  TYR A HD2    1 
ATOM   1816  H HE1    . TYR A 1 115 ? 12.578  -14.796 -15.492 1.00 16.36  ?  115  TYR A HE1    1 
ATOM   1817  H HE2    . TYR A 1 115 ? 16.477  -15.707 -15.551 1.00 15.82  ?  115  TYR A HE2    1 
ATOM   1818  H HH     . TYR A 1 115 ? 15.444  -14.832 -13.759 1.00 18.21  ?  115  TYR A HH     1 
ATOM   1819  N N      . GLY A 1 116 ? 11.925  -18.448 -20.957 1.00 11.74  ?  116  GLY A N      1 
ATOM   1820  C CA     . GLY A 1 116 ? 11.347  -18.476 -22.284 1.00 12.68  ?  116  GLY A CA     1 
ATOM   1821  C C      . GLY A 1 116 ? 10.306  -17.386 -22.446 1.00 11.95  ?  116  GLY A C      1 
ATOM   1822  O O      . GLY A 1 116 ? 10.361  -16.356 -21.759 1.00 13.25  ?  116  GLY A O      1 
ATOM   1823  H H      . GLY A 1 116 ? 11.334  -18.357 -20.339 1.00 14.09  ?  116  GLY A H      1 
ATOM   1824  H HA2    . GLY A 1 116 ? 12.043  -18.342 -22.946 1.00 15.21  ?  116  GLY A HA2    1 
ATOM   1825  H HA3    . GLY A 1 116 ? 10.925  -19.335 -22.438 1.00 15.21  ?  116  GLY A HA3    1 
ATOM   1826  N N      A MET A 1 117 ? 9.337   -17.611 -23.342 0.52 12.66  ?  117  MET A N      1 
ATOM   1827  N N      B MET A 1 117 ? 9.353   -17.594 -23.349 0.48 12.14  ?  117  MET A N      1 
ATOM   1828  C CA     A MET A 1 117 ? 8.379   -16.589 -23.728 0.52 13.67  ?  117  MET A CA     1 
ATOM   1829  C CA     B MET A 1 117 ? 8.362   -16.577 -23.671 0.48 12.40  ?  117  MET A CA     1 
ATOM   1830  C C      A MET A 1 117 ? 6.922   -16.990 -23.559 0.52 14.30  ?  117  MET A C      1 
ATOM   1831  C C      B MET A 1 117 ? 6.948   -16.978 -23.292 0.48 12.95  ?  117  MET A C      1 
ATOM   1832  O O      A MET A 1 117 ? 6.049   -16.114 -23.640 0.52 15.16  ?  117  MET A O      1 
ATOM   1833  O O      B MET A 1 117 ? 6.158   -16.113 -22.904 0.48 13.61  ?  117  MET A O      1 
ATOM   1834  C CB     A MET A 1 117 ? 8.596   -16.179 -25.197 0.52 15.44  ?  117  MET A CB     1 
ATOM   1835  C CB     B MET A 1 117 ? 8.425   -16.256 -25.170 0.48 12.89  ?  117  MET A CB     1 
ATOM   1836  C CG     A MET A 1 117 ? 9.851   -15.337 -25.427 0.52 15.28  ?  117  MET A CG     1 
ATOM   1837  C CG     B MET A 1 117 ? 9.711   -15.487 -25.556 0.48 14.13  ?  117  MET A CG     1 
ATOM   1838  S SD     A MET A 1 117 ? 11.416  -16.229 -25.341 0.52 15.49  ?  117  MET A SD     1 
ATOM   1839  S SD     B MET A 1 117 ? 10.591  -16.072 -27.039 0.48 15.55  ?  117  MET A SD     1 
ATOM   1840  C CE     A MET A 1 117 ? 11.178  -17.491 -26.583 0.52 16.79  ?  117  MET A CE     1 
ATOM   1841  C CE     B MET A 1 117 ? 11.428  -17.515 -26.364 0.48 17.17  ?  117  MET A CE     1 
ATOM   1842  H H      A MET A 1 117 ? 9.220   -18.362 -23.744 0.52 15.18  ?  117  MET A H      1 
ATOM   1843  H H      B MET A 1 117 ? 9.260   -18.325 -23.793 0.48 14.57  ?  117  MET A H      1 
ATOM   1844  H HA     A MET A 1 117 ? 8.543   -15.814 -23.167 0.52 16.40  ?  117  MET A HA     1 
ATOM   1845  H HA     B MET A 1 117 ? 8.572   -15.759 -23.194 0.48 14.88  ?  117  MET A HA     1 
ATOM   1846  H HB2    A MET A 1 117 ? 8.677   -16.982 -25.735 0.52 18.53  ?  117  MET A HB2    1 
ATOM   1847  H HB2    B MET A 1 117 ? 8.407   -17.085 -25.673 0.48 15.46  ?  117  MET A HB2    1 
ATOM   1848  H HB3    A MET A 1 117 ? 7.833   -15.659 -25.491 0.52 18.53  ?  117  MET A HB3    1 
ATOM   1849  H HB3    B MET A 1 117 ? 7.662   -15.707 -25.409 0.48 15.46  ?  117  MET A HB3    1 
ATOM   1850  H HG2    A MET A 1 117 ? 9.794   -14.940 -26.310 0.52 18.33  ?  117  MET A HG2    1 
ATOM   1851  H HG2    B MET A 1 117 ? 9.472   -14.560 -25.715 0.48 16.96  ?  117  MET A HG2    1 
ATOM   1852  H HG3    A MET A 1 117 ? 9.879   -14.641 -24.751 0.52 18.33  ?  117  MET A HG3    1 
ATOM   1853  H HG3    B MET A 1 117 ? 10.333  -15.547 -24.814 0.48 16.96  ?  117  MET A HG3    1 
ATOM   1854  H HE1    A MET A 1 117 ? 12.015  -17.960 -26.722 0.52 20.15  ?  117  MET A HE1    1 
ATOM   1855  H HE1    B MET A 1 117 ? 11.876  -17.987 -27.084 0.48 20.60  ?  117  MET A HE1    1 
ATOM   1856  H HE2    A MET A 1 117 ? 10.498  -18.111 -26.277 0.52 20.15  ?  117  MET A HE2    1 
ATOM   1857  H HE2    B MET A 1 117 ? 12.078  -17.224 -25.705 0.48 20.60  ?  117  MET A HE2    1 
ATOM   1858  H HE3    A MET A 1 117 ? 10.893  -17.070 -27.410 0.52 20.15  ?  117  MET A HE3    1 
ATOM   1859  H HE3    B MET A 1 117 ? 10.772  -18.095 -25.947 0.48 20.60  ?  117  MET A HE3    1 
ATOM   1860  N N      . SER A 1 118 ? 6.632   -18.273 -23.358 1.00 12.87  ?  118  SER A N      1 
ATOM   1861  C CA     . SER A 1 118 ? 5.267   -18.743 -23.209 1.00 12.29  ?  118  SER A CA     1 
ATOM   1862  C C      . SER A 1 118 ? 5.250   -19.912 -22.229 1.00 12.63  ?  118  SER A C      1 
ATOM   1863  O O      . SER A 1 118 ? 6.253   -20.609 -22.035 1.00 13.23  ?  118  SER A O      1 
ATOM   1864  C CB     . SER A 1 118 ? 4.729   -19.216 -24.557 1.00 12.94  ?  118  SER A CB     1 
ATOM   1865  O OG     . SER A 1 118 ? 5.458   -20.362 -25.032 1.00 14.57  ?  118  SER A OG     1 
ATOM   1866  H H      A SER A 1 118 ? 7.221   -18.897 -23.304 0.52 15.44  ?  118  SER A H      1 
ATOM   1867  H H      B SER A 1 118 ? 7.205   -18.900 -23.491 0.48 15.44  ?  118  SER A H      1 
ATOM   1868  H HA     . SER A 1 118 ? 4.702   -18.036 -22.859 1.00 14.74  ?  118  SER A HA     1 
ATOM   1869  H HB2    . SER A 1 118 ? 3.795   -19.457 -24.457 1.00 15.52  ?  118  SER A HB2    1 
ATOM   1870  H HB3    . SER A 1 118 ? 4.819   -18.497 -25.202 1.00 15.52  ?  118  SER A HB3    1 
ATOM   1871  H HG     . SER A 1 118 ? 5.174   -20.590 -25.788 1.00 17.48  ?  118  SER A HG     1 
ATOM   1872  N N      . GLY A 1 119 ? 4.095   -20.135 -21.606 1.00 12.42  ?  119  GLY A N      1 
ATOM   1873  C CA     . GLY A 1 119 ? 3.950   -21.337 -20.797 1.00 11.79  ?  119  GLY A CA     1 
ATOM   1874  C C      . GLY A 1 119 ? 4.170   -22.606 -21.597 1.00 12.01  ?  119  GLY A C      1 
ATOM   1875  O O      . GLY A 1 119 ? 4.681   -23.603 -21.077 1.00 14.19  ?  119  GLY A O      1 
ATOM   1876  H H      . GLY A 1 119 ? 3.403   -19.625 -21.634 1.00 14.90  ?  119  GLY A H      1 
ATOM   1877  H HA2    . GLY A 1 119 ? 4.595   -21.316 -20.073 1.00 14.14  ?  119  GLY A HA2    1 
ATOM   1878  H HA3    . GLY A 1 119 ? 3.055   -21.364 -20.422 1.00 14.14  ?  119  GLY A HA3    1 
ATOM   1879  N N      . SER A 1 120 ? 3.761   -22.597 -22.866 1.00 11.70  ?  120  SER A N      1 
ATOM   1880  C CA     . SER A 1 120 ? 3.985   -23.744 -23.741 1.00 12.01  ?  120  SER A CA     1 
ATOM   1881  C C      . SER A 1 120 ? 5.470   -24.046 -23.881 1.00 11.70  ?  120  SER A C      1 
ATOM   1882  O O      . SER A 1 120 ? 5.880   -25.191 -23.774 1.00 12.03  ?  120  SER A O      1 
ATOM   1883  C CB     . SER A 1 120 ? 3.360   -23.501 -25.122 1.00 12.32  ?  120  SER A CB     1 
ATOM   1884  O OG     . SER A 1 120 ? 1.938   -23.441 -25.063 1.00 12.15  ?  120  SER A OG     1 
ATOM   1885  H H      . SER A 1 120 ? 3.351   -21.942 -23.245 1.00 14.04  ?  120  SER A H      1 
ATOM   1886  H HA     . SER A 1 120 ? 3.550   -24.515 -23.346 1.00 14.41  ?  120  SER A HA     1 
ATOM   1887  H HB2    . SER A 1 120 ? 3.693   -22.659 -25.470 1.00 14.78  ?  120  SER A HB2    1 
ATOM   1888  H HB3    . SER A 1 120 ? 3.616   -24.228 -25.712 1.00 14.78  ?  120  SER A HB3    1 
ATOM   1889  H HG     . SER A 1 120 ? 1.697   -22.793 -24.585 1.00 14.58  ?  120  SER A HG     1 
ATOM   1890  N N      . ASP A 1 121 ? 6.292   -23.037 -24.182 1.00 12.40  ?  121  ASP A N      1 
ATOM   1891  C CA     . ASP A 1 121 ? 7.729   -23.291 -24.339 1.00 10.45  ?  121  ASP A CA     1 
ATOM   1892  C C      . ASP A 1 121 ? 8.373   -23.698 -23.024 1.00 10.92  ?  121  ASP A C      1 
ATOM   1893  O O      . ASP A 1 121 ? 9.305   -24.506 -23.025 1.00 10.92  ?  121  ASP A O      1 
ATOM   1894  C CB     . ASP A 1 121 ? 8.425   -22.174 -25.140 1.00 11.39  ?  121  ASP A CB     1 
ATOM   1895  C CG     . ASP A 1 121 ? 8.775   -20.918 -24.370 1.00 12.52  ?  121  ASP A CG     1 
ATOM   1896  O OD1    . ASP A 1 121 ? 9.097   -20.929 -23.171 1.00 13.33  ?  121  ASP A OD1    1 
ATOM   1897  O OD2    . ASP A 1 121 ? 8.790   -19.850 -25.044 1.00 14.76  -1 121  ASP A OD2    1 
ATOM   1898  H H      . ASP A 1 121 ? 6.054   -22.219 -24.299 1.00 14.88  ?  121  ASP A H      1 
ATOM   1899  H HA     . ASP A 1 121 ? 7.874   -24.058 -24.913 1.00 12.53  ?  121  ASP A HA     1 
ATOM   1900  H HB2    . ASP A 1 121 ? 9.253   -22.529 -25.499 1.00 13.66  ?  121  ASP A HB2    1 
ATOM   1901  H HB3    . ASP A 1 121 ? 7.836   -21.909 -25.865 1.00 13.66  ?  121  ASP A HB3    1 
ATOM   1902  N N      . ALA A 1 122 ? 7.844   -23.215 -21.895 1.00 11.79  ?  122  ALA A N      1 
ATOM   1903  C CA     . ALA A 1 122 ? 8.360   -23.621 -20.603 1.00 11.24  ?  122  ALA A CA     1 
ATOM   1904  C C      . ALA A 1 122 ? 8.111   -25.106 -20.386 1.00 10.84  ?  122  ALA A C      1 
ATOM   1905  O O      . ALA A 1 122 ? 8.979   -25.819 -19.880 1.00 12.82  ?  122  ALA A O      1 
ATOM   1906  C CB     . ALA A 1 122 ? 7.745   -22.763 -19.501 1.00 12.41  ?  122  ALA A CB     1 
ATOM   1907  H H      . ALA A 1 122 ? 7.191   -22.657 -21.855 1.00 14.15  ?  122  ALA A H      1 
ATOM   1908  H HA     . ALA A 1 122 ? 9.318   -23.473 -20.561 1.00 13.48  ?  122  ALA A HA     1 
ATOM   1909  H HB1    . ALA A 1 122 ? 8.096   -23.050 -18.644 1.00 14.89  ?  122  ALA A HB1    1 
ATOM   1910  H HB2    . ALA A 1 122 ? 7.974   -21.834 -19.659 1.00 14.89  ?  122  ALA A HB2    1 
ATOM   1911  H HB3    . ALA A 1 122 ? 6.781   -22.873 -19.516 1.00 14.89  ?  122  ALA A HB3    1 
ATOM   1912  N N      . ASN A 1 123 ? 6.952   -25.613 -20.823 1.00 11.26  ?  123  ASN A N      1 
ATOM   1913  C CA     . ASN A 1 123 ? 6.706   -27.047 -20.702 1.00 10.70  ?  123  ASN A CA     1 
ATOM   1914  C C      . ASN A 1 123 ? 7.489   -27.871 -21.720 1.00 11.62  ?  123  ASN A C      1 
ATOM   1915  O O      . ASN A 1 123 ? 7.816   -29.029 -21.432 1.00 11.79  ?  123  ASN A O      1 
ATOM   1916  C CB     . ASN A 1 123 ? 5.200   -27.337 -20.700 1.00 11.36  ?  123  ASN A CB     1 
ATOM   1917  C CG     . ASN A 1 123 ? 4.558   -26.976 -19.374 1.00 11.25  ?  123  ASN A CG     1 
ATOM   1918  O OD1    . ASN A 1 123 ? 5.187   -27.125 -18.327 1.00 11.47  ?  123  ASN A OD1    1 
ATOM   1919  N ND2    . ASN A 1 123 ? 3.299   -26.522 -19.406 1.00 11.14  ?  123  ASN A ND2    1 
ATOM   1920  H H      . ASN A 1 123 ? 6.314   -25.162 -21.182 1.00 13.51  ?  123  ASN A H      1 
ATOM   1921  H HA     . ASN A 1 123 ? 7.030   -27.350 -19.839 1.00 12.83  ?  123  ASN A HA     1 
ATOM   1922  H HB2    . ASN A 1 123 ? 4.773   -26.814 -21.397 1.00 13.62  ?  123  ASN A HB2    1 
ATOM   1923  H HB3    . ASN A 1 123 ? 5.056   -28.283 -20.860 1.00 13.62  ?  123  ASN A HB3    1 
ATOM   1924  H HD21   . ASN A 1 123 ? 2.901   -26.307 -18.674 1.00 13.36  ?  123  ASN A HD21   1 
ATOM   1925  H HD22   . ASN A 1 123 ? 2.888   -26.445 -20.157 1.00 13.36  ?  123  ASN A HD22   1 
ATOM   1926  N N      . GLU A 1 124 ? 7.809   -27.312 -22.893 1.00 11.09  ?  124  GLU A N      1 
ATOM   1927  C CA     . GLU A 1 124 ? 8.788   -27.972 -23.759 1.00 10.86  ?  124  GLU A CA     1 
ATOM   1928  C C      . GLU A 1 124 ? 10.109  -28.155 -23.022 1.00 11.64  ?  124  GLU A C      1 
ATOM   1929  O O      . GLU A 1 124 ? 10.727  -29.234 -23.067 1.00 12.73  ?  124  GLU A O      1 
ATOM   1930  C CB     . GLU A 1 124 ? 9.049   -27.158 -25.028 1.00 11.18  ?  124  GLU A CB     1 
ATOM   1931  C CG     . GLU A 1 124 ? 7.865   -26.936 -25.938 1.00 12.04  ?  124  GLU A CG     1 
ATOM   1932  C CD     . GLU A 1 124 ? 7.390   -28.168 -26.669 1.00 13.59  ?  124  GLU A CD     1 
ATOM   1933  O OE1    . GLU A 1 124 ? 6.155   -28.269 -26.903 1.00 13.19  ?  124  GLU A OE1    1 
ATOM   1934  O OE2    . GLU A 1 124 ? 8.237   -29.007 -27.045 1.00 13.30  -1 124  GLU A OE2    1 
ATOM   1935  H H      . GLU A 1 124 ? 7.486   -26.577 -23.201 1.00 13.30  ?  124  GLU A H      1 
ATOM   1936  H HA     . GLU A 1 124 ? 8.422   -28.832 -24.020 1.00 13.03  ?  124  GLU A HA     1 
ATOM   1937  H HB2    . GLU A 1 124 ? 9.372   -26.283 -24.763 1.00 13.41  ?  124  GLU A HB2    1 
ATOM   1938  H HB3    . GLU A 1 124 ? 9.725   -27.618 -25.548 1.00 13.41  ?  124  GLU A HB3    1 
ATOM   1939  H HG2    . GLU A 1 124 ? 7.123   -26.610 -25.405 1.00 14.45  ?  124  GLU A HG2    1 
ATOM   1940  H HG3    . GLU A 1 124 ? 8.109   -26.277 -26.606 1.00 14.45  ?  124  GLU A HG3    1 
ATOM   1941  N N      . THR A 1 125 ? 10.554  -27.101 -22.337 1.00 11.41  ?  125  THR A N      1 
ATOM   1942  C CA     . THR A 1 125 ? 11.785  -27.184 -21.560 1.00 11.97  ?  125  THR A CA     1 
ATOM   1943  C C      . THR A 1 125 ? 11.669  -28.237 -20.464 1.00 12.58  ?  125  THR A C      1 
ATOM   1944  O O      . THR A 1 125 ? 12.597  -29.025 -20.265 1.00 12.54  ?  125  THR A O      1 
ATOM   1945  C CB     . THR A 1 125 ? 12.111  -25.806 -20.984 1.00 12.14  ?  125  THR A CB     1 
ATOM   1946  O OG1    . THR A 1 125 ? 12.359  -24.903 -22.059 1.00 11.30  ?  125  THR A OG1    1 
ATOM   1947  C CG2    . THR A 1 125 ? 13.356  -25.853 -20.091 1.00 14.80  ?  125  THR A CG2    1 
ATOM   1948  H H      . THR A 1 125 ? 10.167  -26.333 -22.306 1.00 13.69  ?  125  THR A H      1 
ATOM   1949  H HA     . THR A 1 125 ? 12.520  -27.448 -22.135 1.00 14.36  ?  125  THR A HA     1 
ATOM   1950  H HB     . THR A 1 125 ? 11.365  -25.503 -20.444 1.00 14.56  ?  125  THR A HB     1 
ATOM   1951  H HG1    . THR A 1 125 ? 11.687  -24.864 -22.562 1.00 13.56  ?  125  THR A HG1    1 
ATOM   1952  H HG21   . THR A 1 125 ? 13.613  -24.954 -19.834 1.00 17.76  ?  125  THR A HG21   1 
ATOM   1953  H HG22   . THR A 1 125 ? 13.171  -26.369 -19.291 1.00 17.76  ?  125  THR A HG22   1 
ATOM   1954  H HG23   . THR A 1 125 ? 14.092  -26.266 -20.570 1.00 17.76  ?  125  THR A HG23   1 
ATOM   1955  N N      . GLN A 1 126 ? 10.537  -28.281 -19.757 1.00 11.69  ?  126  GLN A N      1 
ATOM   1956  C CA     . GLN A 1 126 ? 10.355  -29.277 -18.710 1.00 10.80  ?  126  GLN A CA     1 
ATOM   1957  C C      . GLN A 1 126 ? 10.559  -30.682 -19.268 1.00 11.17  ?  126  GLN A C      1 
ATOM   1958  O O      . GLN A 1 126 ? 11.227  -31.522 -18.652 1.00 10.91  ?  126  GLN A O      1 
ATOM   1959  C CB     . GLN A 1 126 ? 8.946   -29.200 -18.113 1.00 11.31  ?  126  GLN A CB     1 
ATOM   1960  C CG     . GLN A 1 126 ? 8.578   -27.909 -17.421 1.00 10.52  ?  126  GLN A CG     1 
ATOM   1961  C CD     . GLN A 1 126 ? 9.237   -27.709 -16.073 1.00 12.24  ?  126  GLN A CD     1 
ATOM   1962  O OE1    . GLN A 1 126 ? 10.301  -28.260 -15.780 1.00 14.01  ?  126  GLN A OE1    1 
ATOM   1963  N NE2    . GLN A 1 126 ? 8.598   -26.898 -15.243 1.00 11.91  ?  126  GLN A NE2    1 
ATOM   1964  H H      . GLN A 1 126 ? 9.868   -27.751 -19.864 1.00 14.02  ?  126  GLN A H      1 
ATOM   1965  H HA     . GLN A 1 126 ? 11.003  -29.091 -18.012 1.00 12.95  ?  126  GLN A HA     1 
ATOM   1966  H HB2    . GLN A 1 126 ? 8.307   -29.329 -18.831 1.00 13.57  ?  126  GLN A HB2    1 
ATOM   1967  H HB3    . GLN A 1 126 ? 8.857   -29.909 -17.458 1.00 13.57  ?  126  GLN A HB3    1 
ATOM   1968  H HG2    . GLN A 1 126 ? 8.842   -27.168 -17.989 1.00 12.62  ?  126  GLN A HG2    1 
ATOM   1969  H HG3    . GLN A 1 126 ? 7.619   -27.895 -17.282 1.00 12.62  ?  126  GLN A HG3    1 
ATOM   1970  H HE21   . GLN A 1 126 ? 7.861   -26.528 -15.487 1.00 14.29  ?  126  GLN A HE21   1 
ATOM   1971  H HE22   . GLN A 1 126 ? 8.920   -26.742 -14.461 1.00 14.29  ?  126  GLN A HE22   1 
ATOM   1972  N N      . LEU A 1 127 ? 9.970   -30.967 -20.424 1.00 11.89  ?  127  LEU A N      1 
ATOM   1973  C CA     . LEU A 1 127 ? 10.073  -32.306 -20.982 1.00 11.51  ?  127  LEU A CA     1 
ATOM   1974  C C      . LEU A 1 127 ? 11.509  -32.643 -21.344 1.00 11.21  ?  127  LEU A C      1 
ATOM   1975  O O      . LEU A 1 127 ? 11.964  -33.765 -21.110 1.00 12.87  ?  127  LEU A O      1 
ATOM   1976  C CB     . LEU A 1 127 ? 9.148   -32.453 -22.184 1.00 12.50  ?  127  LEU A CB     1 
ATOM   1977  C CG     . LEU A 1 127 ? 7.675   -32.409 -21.819 1.00 12.40  ?  127  LEU A CG     1 
ATOM   1978  C CD1    . LEU A 1 127 ? 6.847   -32.387 -23.097 1.00 15.35  ?  127  LEU A CD1    1 
ATOM   1979  C CD2    . LEU A 1 127 ? 7.281   -33.572 -20.921 1.00 14.13  ?  127  LEU A CD2    1 
ATOM   1980  H H      . LEU A 1 127 ? 9.512   -30.414 -20.897 1.00 14.26  ?  127  LEU A H      1 
ATOM   1981  H HA     . LEU A 1 127 ? 9.781   -32.947 -20.315 1.00 13.81  ?  127  LEU A HA     1 
ATOM   1982  H HB2    . LEU A 1 127 ? 9.324   -31.728 -22.805 1.00 15.00  ?  127  LEU A HB2    1 
ATOM   1983  H HB3    . LEU A 1 127 ? 9.324   -33.306 -22.612 1.00 15.00  ?  127  LEU A HB3    1 
ATOM   1984  H HG     . LEU A 1 127 ? 7.492   -31.603 -21.311 1.00 14.88  ?  127  LEU A HG     1 
ATOM   1985  H HD11   . LEU A 1 127 ? 5.907   -32.334 -22.863 1.00 18.42  ?  127  LEU A HD11   1 
ATOM   1986  H HD12   . LEU A 1 127 ? 7.100   -31.613 -23.624 1.00 18.42  ?  127  LEU A HD12   1 
ATOM   1987  H HD13   . LEU A 1 127 ? 7.018   -33.199 -23.598 1.00 18.42  ?  127  LEU A HD13   1 
ATOM   1988  H HD21   . LEU A 1 127 ? 6.313   -33.619 -20.871 1.00 16.95  ?  127  LEU A HD21   1 
ATOM   1989  H HD22   . LEU A 1 127 ? 7.633   -34.394 -21.296 1.00 16.95  ?  127  LEU A HD22   1 
ATOM   1990  H HD23   . LEU A 1 127 ? 7.651   -33.427 -20.036 1.00 16.95  ?  127  LEU A HD23   1 
ATOM   1991  N N      . LYS A 1 128 ? 12.250  -31.686 -21.905 1.00 11.51  ?  128  LYS A N      1 
ATOM   1992  C CA     . LYS A 1 128 ? 13.664  -31.950 -22.177 1.00 11.12  ?  128  LYS A CA     1 
ATOM   1993  C C      . LYS A 1 128 ? 14.442  -32.207 -20.891 1.00 13.36  ?  128  LYS A C      1 
ATOM   1994  O O      . LYS A 1 128 ? 15.293  -33.103 -20.843 1.00 13.17  ?  128  LYS A O      1 
ATOM   1995  C CB     . LYS A 1 128 ? 14.275  -30.801 -22.979 1.00 13.61  ?  128  LYS A CB     1 
ATOM   1996  C CG     . LYS A 1 128 ? 13.889  -30.811 -24.459 1.00 13.77  ?  128  LYS A CG     1 
ATOM   1997  C CD     . LYS A 1 128 ? 14.524  -29.670 -25.265 1.00 11.81  ?  128  LYS A CD     1 
ATOM   1998  C CE     . LYS A 1 128 ? 16.019  -29.803 -25.348 1.00 11.63  ?  128  LYS A CE     1 
ATOM   1999  N NZ     . LYS A 1 128 ? 16.625  -28.808 -26.266 1.00 11.53  ?  128  LYS A NZ     1 
ATOM   2000  H H      . LYS A 1 128 ? 11.973  -30.904 -22.131 1.00 13.81  ?  128  LYS A H      1 
ATOM   2001  H HA     . LYS A 1 128 ? 13.731  -32.751 -22.721 1.00 13.35  ?  128  LYS A HA     1 
ATOM   2002  H HB2    . LYS A 1 128 ? 13.973  -29.961 -22.600 1.00 16.33  ?  128  LYS A HB2    1 
ATOM   2003  H HB3    . LYS A 1 128 ? 15.241  -30.862 -22.924 1.00 16.33  ?  128  LYS A HB3    1 
ATOM   2004  H HG2    . LYS A 1 128 ? 14.179  -31.648 -24.853 1.00 16.52  ?  128  LYS A HG2    1 
ATOM   2005  H HG3    . LYS A 1 128 ? 12.926  -30.725 -24.532 1.00 16.52  ?  128  LYS A HG3    1 
ATOM   2006  H HD2    . LYS A 1 128 ? 14.168  -29.680 -26.167 1.00 14.17  ?  128  LYS A HD2    1 
ATOM   2007  H HD3    . LYS A 1 128 ? 14.319  -28.824 -24.837 1.00 14.17  ?  128  LYS A HD3    1 
ATOM   2008  H HE2    . LYS A 1 128 ? 16.399  -29.671 -24.466 1.00 13.95  ?  128  LYS A HE2    1 
ATOM   2009  H HE3    . LYS A 1 128 ? 16.241  -30.689 -25.675 1.00 13.95  ?  128  LYS A HE3    1 
ATOM   2010  H HZ1    . LYS A 1 128 ? 17.433  -28.576 -25.973 1.00 13.84  ?  128  LYS A HZ1    1 
ATOM   2011  H HZ2    . LYS A 1 128 ? 16.702  -29.153 -27.082 1.00 13.84  ?  128  LYS A HZ2    1 
ATOM   2012  H HZ3    . LYS A 1 128 ? 16.113  -28.081 -26.307 1.00 13.84  ?  128  LYS A HZ3    1 
ATOM   2013  N N      . ILE A 1 129 ? 14.155  -31.438 -19.836 1.00 12.71  ?  129  ILE A N      1 
ATOM   2014  C CA     . ILE A 1 129 ? 14.824  -31.640 -18.547 1.00 11.72  ?  129  ILE A CA     1 
ATOM   2015  C C      . ILE A 1 129 ? 14.553  -33.044 -17.999 1.00 12.04  ?  129  ILE A C      1 
ATOM   2016  O O      . ILE A 1 129 ? 15.459  -33.716 -17.504 1.00 13.24  ?  129  ILE A O      1 
ATOM   2017  C CB     . ILE A 1 129 ? 14.411  -30.555 -17.539 1.00 12.42  ?  129  ILE A CB     1 
ATOM   2018  C CG1    . ILE A 1 129 ? 15.034  -29.210 -17.924 1.00 12.45  ?  129  ILE A CG1    1 
ATOM   2019  C CG2    . ILE A 1 129 ? 14.822  -30.949 -16.122 1.00 12.98  ?  129  ILE A CG2    1 
ATOM   2020  C CD1    . ILE A 1 129 ? 14.498  -27.994 -17.161 1.00 13.36  ?  129  ILE A CD1    1 
ATOM   2021  H H      . ILE A 1 129 ? 13.582  -30.797 -19.837 1.00 15.25  ?  129  ILE A H      1 
ATOM   2022  H HA     . ILE A 1 129 ? 15.780  -31.563 -18.698 1.00 14.06  ?  129  ILE A HA     1 
ATOM   2023  H HB     . ILE A 1 129 ? 13.446  -30.469 -17.563 1.00 14.90  ?  129  ILE A HB     1 
ATOM   2024  H HG12   . ILE A 1 129 ? 15.989  -29.257 -17.758 1.00 14.94  ?  129  ILE A HG12   1 
ATOM   2025  H HG13   . ILE A 1 129 ? 14.868  -29.056 -18.867 1.00 14.94  ?  129  ILE A HG13   1 
ATOM   2026  H HG21   . ILE A 1 129 ? 14.745  -30.174 -15.543 1.00 15.58  ?  129  ILE A HG21   1 
ATOM   2027  H HG22   . ILE A 1 129 ? 14.236  -31.655 -15.808 1.00 15.58  ?  129  ILE A HG22   1 
ATOM   2028  H HG23   . ILE A 1 129 ? 15.740  -31.261 -16.134 1.00 15.58  ?  129  ILE A HG23   1 
ATOM   2029  H HD11   . ILE A 1 129 ? 14.929  -27.194 -17.499 1.00 16.03  ?  129  ILE A HD11   1 
ATOM   2030  H HD12   . ILE A 1 129 ? 13.539  -27.935 -17.295 1.00 16.03  ?  129  ILE A HD12   1 
ATOM   2031  H HD13   . ILE A 1 129 ? 14.694  -28.102 -16.217 1.00 16.03  ?  129  ILE A HD13   1 
ATOM   2032  N N      . VAL A 1 130 ? 13.296  -33.490 -18.046 1.00 11.78  ?  130  VAL A N      1 
ATOM   2033  C CA     . VAL A 1 130 ? 12.941  -34.817 -17.535 1.00 13.97  ?  130  VAL A CA     1 
ATOM   2034  C C      . VAL A 1 130 ? 13.691  -35.926 -18.277 1.00 14.62  ?  130  VAL A C      1 
ATOM   2035  O O      . VAL A 1 130 ? 14.198  -36.878 -17.663 1.00 14.00  ?  130  VAL A O      1 
ATOM   2036  C CB     . VAL A 1 130 ? 11.420  -34.998 -17.607 1.00 14.38  ?  130  VAL A CB     1 
ATOM   2037  C CG1    . VAL A 1 130 ? 11.033  -36.426 -17.337 1.00 17.02  ?  130  VAL A CG1    1 
ATOM   2038  C CG2    . VAL A 1 130 ? 10.734  -34.066 -16.607 1.00 15.79  ?  130  VAL A CG2    1 
ATOM   2039  H H      . VAL A 1 130 ? 12.631  -33.049 -18.366 1.00 14.13  ?  130  VAL A H      1 
ATOM   2040  H HA     . VAL A 1 130 ? 13.218  -34.875 -16.607 1.00 16.76  ?  130  VAL A HA     1 
ATOM   2041  H HB     . VAL A 1 130 ? 11.123  -34.772 -18.503 1.00 17.25  ?  130  VAL A HB     1 
ATOM   2042  H HG11   . VAL A 1 130 ? 10.095  -36.458 -17.089 1.00 20.42  ?  130  VAL A HG11   1 
ATOM   2043  H HG12   . VAL A 1 130 ? 11.181  -36.951 -18.139 1.00 20.42  ?  130  VAL A HG12   1 
ATOM   2044  H HG13   . VAL A 1 130 ? 11.578  -36.769 -16.611 1.00 20.42  ?  130  VAL A HG13   1 
ATOM   2045  H HG21   . VAL A 1 130 ? 9.775   -34.212 -16.646 1.00 18.94  ?  130  VAL A HG21   1 
ATOM   2046  H HG22   . VAL A 1 130 ? 11.062  -34.263 -15.716 1.00 18.94  ?  130  VAL A HG22   1 
ATOM   2047  H HG23   . VAL A 1 130 ? 10.939  -33.147 -16.839 1.00 18.94  ?  130  VAL A HG23   1 
ATOM   2048  N N      . ARG A 1 131 ? 13.777  -35.824 -19.581 1.00 14.32  ?  131  ARG A N      1 
ATOM   2049  C CA     . ARG A 1 131 ? 14.493  -36.799 -20.389 1.00 14.95  ?  131  ARG A CA     1 
ATOM   2050  C C      . ARG A 1 131 ? 15.993  -36.786 -20.060 1.00 12.86  ?  131  ARG A C      1 
ATOM   2051  O O      . ARG A 1 131 ? 16.567  -37.797 -19.888 1.00 12.87  ?  131  ARG A O      1 
ATOM   2052  C CB     . ARG A 1 131 ? 14.258  -36.544 -21.898 1.00 15.08  ?  131  ARG A CB     1 
ATOM   2053  C CG     . ARG A 1 131 ? 12.848  -36.889 -22.388 1.00 16.69  ?  131  ARG A CG     1 
ATOM   2054  C CD     . ARG A 1 131 ? 12.467  -36.093 -23.633 1.00 20.91  ?  131  ARG A CD     1 
ATOM   2055  N NE     . ARG A 1 131 ? 11.127  -36.471 -24.083 1.00 22.37  ?  131  ARG A NE     1 
ATOM   2056  C CZ     . ARG A 1 131 ? 10.829  -36.921 -25.289 1.00 19.23  ?  131  ARG A CZ     1 
ATOM   2057  N NH1    . ARG A 1 131 ? 11.770  -37.099 -26.164 1.00 18.34  ?  131  ARG A NH1    1 
ATOM   2058  N NH2    . ARG A 1 131 ? 9.593   -37.264 -25.581 1.00 20.64  ?  131  ARG A NH2    1 
ATOM   2059  H H      . ARG A 1 131 ? 13.423  -35.188 -20.038 1.00 17.18  ?  131  ARG A H      1 
ATOM   2060  H HA     . ARG A 1 131 ? 14.149  -37.693 -20.180 1.00 17.94  ?  131  ARG A HA     1 
ATOM   2061  H HB2    . ARG A 1 131 ? 14.412  -35.605 -22.082 1.00 18.09  ?  131  ARG A HB2    1 
ATOM   2062  H HB3    . ARG A 1 131 ? 14.885  -37.084 -22.405 1.00 18.09  ?  131  ARG A HB3    1 
ATOM   2063  H HG2    . ARG A 1 131 ? 12.810  -37.833 -22.608 1.00 20.02  ?  131  ARG A HG2    1 
ATOM   2064  H HG3    . ARG A 1 131 ? 12.208  -36.682 -21.688 1.00 20.02  ?  131  ARG A HG3    1 
ATOM   2065  H HD2    . ARG A 1 131 ? 12.467  -35.146 -23.426 1.00 25.09  ?  131  ARG A HD2    1 
ATOM   2066  H HD3    . ARG A 1 131 ? 13.097  -36.285 -24.346 1.00 25.09  ?  131  ARG A HD3    1 
ATOM   2067  H HE     . ARG A 1 131 ? 10.403  -36.394 -23.443 1.00 26.84  ?  131  ARG A HE     1 
ATOM   2068  H HH11   . ARG A 1 131 ? 12.581  -36.889 -25.971 1.00 22.01  ?  131  ARG A HH11   1 
ATOM   2069  H HH12   . ARG A 1 131 ? 11.578  -37.400 -26.946 1.00 22.01  ?  131  ARG A HH12   1 
ATOM   2070  H HH21   . ARG A 1 131 ? 8.968   -37.154 -25.000 1.00 24.77  ?  131  ARG A HH21   1 
ATOM   2071  H HH22   . ARG A 1 131 ? 9.403   -37.560 -26.366 1.00 24.77  ?  131  ARG A HH22   1 
ATOM   2072  N N      . TYR A 1 132 ? 16.581  -35.606 -20.009 1.00 12.84  ?  132  TYR A N      1 
ATOM   2073  C CA     . TYR A 1 132 ? 18.002  -35.471 -19.718 1.00 13.15  ?  132  TYR A CA     1 
ATOM   2074  C C      . TYR A 1 132 ? 18.315  -36.007 -18.334 1.00 13.06  ?  132  TYR A C      1 
ATOM   2075  O O      . TYR A 1 132 ? 19.296  -36.744 -18.158 1.00 14.40  ?  132  TYR A O      1 
ATOM   2076  C CB     . TYR A 1 132 ? 18.350  -33.988 -19.821 1.00 12.76  ?  132  TYR A CB     1 
ATOM   2077  C CG     . TYR A 1 132 ? 19.815  -33.617 -19.726 1.00 12.62  ?  132  TYR A CG     1 
ATOM   2078  C CD1    . TYR A 1 132 ? 20.607  -33.560 -20.850 1.00 14.31  ?  132  TYR A CD1    1 
ATOM   2079  C CD2    . TYR A 1 132 ? 20.398  -33.316 -18.501 1.00 14.22  ?  132  TYR A CD2    1 
ATOM   2080  C CE1    . TYR A 1 132 ? 21.949  -33.211 -20.775 1.00 14.49  ?  132  TYR A CE1    1 
ATOM   2081  C CE2    . TYR A 1 132 ? 21.731  -32.962 -18.415 1.00 14.42  ?  132  TYR A CE2    1 
ATOM   2082  C CZ     . TYR A 1 132 ? 22.498  -32.914 -19.540 1.00 13.54  ?  132  TYR A CZ     1 
ATOM   2083  O OH     . TYR A 1 132 ? 23.819  -32.568 -19.447 1.00 15.42  ?  132  TYR A OH     1 
ATOM   2084  H H      . TYR A 1 132 ? 16.181  -34.856 -20.137 1.00 15.41  ?  132  TYR A H      1 
ATOM   2085  H HA     . TYR A 1 132 ? 18.539  -35.972 -20.352 1.00 15.78  ?  132  TYR A HA     1 
ATOM   2086  H HB2    . TYR A 1 132 ? 18.033  -33.666 -20.679 1.00 15.31  ?  132  TYR A HB2    1 
ATOM   2087  H HB3    . TYR A 1 132 ? 17.894  -33.524 -19.102 1.00 15.31  ?  132  TYR A HB3    1 
ATOM   2088  H HD1    . TYR A 1 132 ? 20.235  -33.760 -21.679 1.00 17.17  ?  132  TYR A HD1    1 
ATOM   2089  H HD2    . TYR A 1 132 ? 19.883  -33.352 -17.727 1.00 17.06  ?  132  TYR A HD2    1 
ATOM   2090  H HE1    . TYR A 1 132 ? 22.471  -33.178 -21.544 1.00 17.38  ?  132  TYR A HE1    1 
ATOM   2091  H HE2    . TYR A 1 132 ? 22.105  -32.757 -17.589 1.00 17.30  ?  132  TYR A HE2    1 
ATOM   2092  H HH     . TYR A 1 132 ? 23.975  -32.226 -18.696 1.00 18.50  ?  132  TYR A HH     1 
ATOM   2093  N N      . TYR A 1 133 ? 17.475  -35.662 -17.348 1.00 13.30  ?  133  TYR A N      1 
ATOM   2094  C CA     . TYR A 1 133 ? 17.650  -36.110 -15.970 1.00 12.95  ?  133  TYR A CA     1 
ATOM   2095  C C      . TYR A 1 133 ? 17.797  -37.629 -15.908 1.00 15.62  ?  133  TYR A C      1 
ATOM   2096  O O      . TYR A 1 133 ? 18.741  -38.161 -15.311 1.00 14.67  ?  133  TYR A O      1 
ATOM   2097  C CB     . TYR A 1 133 ? 16.433  -35.622 -15.171 1.00 12.84  ?  133  TYR A CB     1 
ATOM   2098  C CG     . TYR A 1 133 ? 16.317  -36.032 -13.713 1.00 13.25  ?  133  TYR A CG     1 
ATOM   2099  C CD1    . TYR A 1 133 ? 16.963  -35.316 -12.713 1.00 15.11  ?  133  TYR A CD1    1 
ATOM   2100  C CD2    . TYR A 1 133 ? 15.533  -37.116 -13.322 1.00 14.14  ?  133  TYR A CD2    1 
ATOM   2101  C CE1    . TYR A 1 133 ? 16.852  -35.685 -11.377 1.00 15.75  ?  133  TYR A CE1    1 
ATOM   2102  C CE2    . TYR A 1 133 ? 15.418  -37.478 -11.996 1.00 15.16  ?  133  TYR A CE2    1 
ATOM   2103  C CZ     . TYR A 1 133 ? 16.086  -36.763 -11.026 1.00 15.29  ?  133  TYR A CZ     1 
ATOM   2104  O OH     . TYR A 1 133 ? 16.005  -37.112 -9.695  1.00 18.48  ?  133  TYR A OH     1 
ATOM   2105  H H      . TYR A 1 133 ? 16.785  -35.159 -17.455 1.00 15.96  ?  133  TYR A H      1 
ATOM   2106  H HA     . TYR A 1 133 ? 18.455  -35.737 -15.578 1.00 15.54  ?  133  TYR A HA     1 
ATOM   2107  H HB2    . TYR A 1 133 ? 16.442  -34.652 -15.185 1.00 15.41  ?  133  TYR A HB2    1 
ATOM   2108  H HB3    . TYR A 1 133 ? 15.637  -35.953 -15.615 1.00 15.41  ?  133  TYR A HB3    1 
ATOM   2109  H HD1    . TYR A 1 133 ? 17.481  -34.578 -12.942 1.00 18.13  ?  133  TYR A HD1    1 
ATOM   2110  H HD2    . TYR A 1 133 ? 15.078  -37.605 -13.969 1.00 16.96  ?  133  TYR A HD2    1 
ATOM   2111  H HE1    . TYR A 1 133 ? 17.297  -35.198 -10.722 1.00 18.90  ?  133  TYR A HE1    1 
ATOM   2112  H HE2    . TYR A 1 133 ? 14.891  -38.206 -11.756 1.00 18.18  ?  133  TYR A HE2    1 
ATOM   2113  H HH     . TYR A 1 133 ? 16.496  -36.608 -9.235  1.00 22.18  ?  133  TYR A HH     1 
ATOM   2114  N N      . ASN A 1 134 ? 16.877  -38.344 -16.549 1.00 13.89  ?  134  ASN A N      1 
ATOM   2115  C CA     . ASN A 1 134 ? 16.906  -39.804 -16.482 1.00 13.97  ?  134  ASN A CA     1 
ATOM   2116  C C      . ASN A 1 134 ? 18.014  -40.407 -17.327 1.00 14.46  ?  134  ASN A C      1 
ATOM   2117  O O      . ASN A 1 134 ? 18.610  -41.416 -16.928 1.00 14.74  ?  134  ASN A O      1 
ATOM   2118  C CB     . ASN A 1 134 ? 15.524  -40.346 -16.780 1.00 13.17  ?  134  ASN A CB     1 
ATOM   2119  C CG     . ASN A 1 134 ? 14.635  -40.246 -15.561 1.00 14.61  ?  134  ASN A CG     1 
ATOM   2120  O OD1    . ASN A 1 134 ? 14.854  -40.982 -14.608 1.00 17.01  ?  134  ASN A OD1    1 
ATOM   2121  N ND2    . ASN A 1 134 ? 13.683  -39.314 -15.557 1.00 15.99  ?  134  ASN A ND2    1 
ATOM   2122  H H      . ASN A 1 134 ? 16.237  -38.018 -17.023 1.00 16.66  ?  134  ASN A H      1 
ATOM   2123  H HA     . ASN A 1 134 ? 17.116  -40.093 -15.580 1.00 16.76  ?  134  ASN A HA     1 
ATOM   2124  H HB2    . ASN A 1 134 ? 15.122  -39.833 -17.497 1.00 15.80  ?  134  ASN A HB2    1 
ATOM   2125  H HB3    . ASN A 1 134 ? 15.591  -41.279 -17.037 1.00 15.80  ?  134  ASN A HB3    1 
ATOM   2126  H HD21   . ASN A 1 134 ? 13.162  -39.234 -14.877 1.00 19.18  ?  134  ASN A HD21   1 
ATOM   2127  H HD22   . ASN A 1 134 ? 13.588  -38.793 -16.235 1.00 19.18  ?  134  ASN A HD22   1 
ATOM   2128  N N      . ASN A 1 135 ? 18.347  -39.806 -18.463 1.00 13.60  ?  135  ASN A N      1 
ATOM   2129  C CA     . ASN A 1 135 ? 19.497  -40.307 -19.211 1.00 13.26  ?  135  ASN A CA     1 
ATOM   2130  C C      . ASN A 1 135 ? 20.787  -40.151 -18.410 1.00 14.92  ?  135  ASN A C      1 
ATOM   2131  O O      . ASN A 1 135 ? 21.623  -41.063 -18.379 1.00 15.74  ?  135  ASN A O      1 
ATOM   2132  C CB     . ASN A 1 135 ? 19.569  -39.608 -20.565 1.00 15.72  ?  135  ASN A CB     1 
ATOM   2133  C CG     . ASN A 1 135 ? 18.595  -40.211 -21.557 1.00 15.34  ?  135  ASN A CG     1 
ATOM   2134  O OD1    . ASN A 1 135 ? 18.346  -41.425 -21.546 1.00 16.65  ?  135  ASN A OD1    1 
ATOM   2135  N ND2    . ASN A 1 135 ? 18.046  -39.386 -22.416 1.00 17.17  ?  135  ASN A ND2    1 
ATOM   2136  H H      . ASN A 1 135 ? 17.943  -39.133 -18.813 1.00 16.31  ?  135  ASN A H      1 
ATOM   2137  H HA     . ASN A 1 135 ? 19.389  -41.256 -19.383 1.00 15.90  ?  135  ASN A HA     1 
ATOM   2138  H HB2    . ASN A 1 135 ? 19.349  -38.670 -20.454 1.00 18.86  ?  135  ASN A HB2    1 
ATOM   2139  H HB3    . ASN A 1 135 ? 20.465  -39.698 -20.925 1.00 18.86  ?  135  ASN A HB3    1 
ATOM   2140  H HD21   . ASN A 1 135 ? 17.487  -39.681 -22.999 1.00 20.60  ?  135  ASN A HD21   1 
ATOM   2141  H HD22   . ASN A 1 135 ? 18.245  -38.549 -22.396 1.00 20.60  ?  135  ASN A HD22   1 
ATOM   2142  N N      . VAL A 1 136 ? 20.969  -39.002 -17.756 1.00 14.40  ?  136  VAL A N      1 
ATOM   2143  C CA     . VAL A 1 136 ? 22.177  -38.789 -16.956 1.00 15.29  ?  136  VAL A CA     1 
ATOM   2144  C C      . VAL A 1 136 ? 22.266  -39.792 -15.817 1.00 16.03  ?  136  VAL A C      1 
ATOM   2145  O O      . VAL A 1 136 ? 23.360  -40.260 -15.474 1.00 17.42  ?  136  VAL A O      1 
ATOM   2146  C CB     . VAL A 1 136 ? 22.221  -37.337 -16.447 1.00 19.13  ?  136  VAL A CB     1 
ATOM   2147  C CG1    . VAL A 1 136 ? 23.310  -37.185 -15.391 1.00 19.23  ?  136  VAL A CG1    1 
ATOM   2148  C CG2    . VAL A 1 136 ? 22.466  -36.432 -17.622 1.00 20.57  ?  136  VAL A CG2    1 
ATOM   2149  H H      . VAL A 1 136 ? 20.420  -38.341 -17.756 1.00 17.27  ?  136  VAL A H      1 
ATOM   2150  H HA     . VAL A 1 136 ? 22.949  -38.935 -17.525 1.00 18.35  ?  136  VAL A HA     1 
ATOM   2151  H HB     . VAL A 1 136 ? 21.381  -37.090 -16.030 1.00 22.95  ?  136  VAL A HB     1 
ATOM   2152  H HG11   . VAL A 1 136 ? 23.497  -36.242 -15.263 1.00 23.07  ?  136  VAL A HG11   1 
ATOM   2153  H HG12   . VAL A 1 136 ? 23.000  -37.577 -14.560 1.00 23.07  ?  136  VAL A HG12   1 
ATOM   2154  H HG13   . VAL A 1 136 ? 24.110  -37.643 -15.694 1.00 23.07  ?  136  VAL A HG13   1 
ATOM   2155  H HG21   . VAL A 1 136 ? 22.401  -35.509 -17.330 1.00 24.68  ?  136  VAL A HG21   1 
ATOM   2156  H HG22   . VAL A 1 136 ? 23.354  -36.605 -17.974 1.00 24.68  ?  136  VAL A HG22   1 
ATOM   2157  H HG23   . VAL A 1 136 ? 21.800  -36.611 -18.303 1.00 24.68  ?  136  VAL A HG23   1 
ATOM   2158  N N      . LEU A 1 137 ? 21.136  -40.119 -15.203 1.00 17.55  ?  137  LEU A N      1 
ATOM   2159  C CA     . LEU A 1 137 ? 21.114  -41.063 -14.095 1.00 16.02  ?  137  LEU A CA     1 
ATOM   2160  C C      . LEU A 1 137 ? 21.236  -42.515 -14.542 1.00 17.23  ?  137  LEU A C      1 
ATOM   2161  O O      . LEU A 1 137 ? 21.232  -43.407 -13.690 1.00 19.91  ?  137  LEU A O      1 
ATOM   2162  C CB     . LEU A 1 137 ? 19.805  -40.904 -13.305 1.00 17.15  ?  137  LEU A CB     1 
ATOM   2163  C CG     . LEU A 1 137 ? 19.691  -39.635 -12.452 1.00 16.76  ?  137  LEU A CG     1 
ATOM   2164  C CD1    . LEU A 1 137 ? 18.317  -39.522 -11.825 1.00 18.94  ?  137  LEU A CD1    1 
ATOM   2165  C CD2    . LEU A 1 137 ? 20.759  -39.612 -11.371 1.00 18.98  ?  137  LEU A CD2    1 
ATOM   2166  H H      . LEU A 1 137 ? 20.363  -39.806 -15.412 1.00 21.05  ?  137  LEU A H      1 
ATOM   2167  H HA     . LEU A 1 137 ? 21.861  -40.862 -13.511 1.00 19.22  ?  137  LEU A HA     1 
ATOM   2168  H HB2    . LEU A 1 137 ? 19.068  -40.894 -13.936 1.00 20.57  ?  137  LEU A HB2    1 
ATOM   2169  H HB3    . LEU A 1 137 ? 19.718  -41.662 -12.706 1.00 20.57  ?  137  LEU A HB3    1 
ATOM   2170  H HG     . LEU A 1 137 ? 19.823  -38.868 -13.031 1.00 20.10  ?  137  LEU A HG     1 
ATOM   2171  H HD11   . LEU A 1 137 ? 18.278  -38.712 -11.292 1.00 22.73  ?  137  LEU A HD11   1 
ATOM   2172  H HD12   . LEU A 1 137 ? 17.650  -39.486 -12.529 1.00 22.73  ?  137  LEU A HD12   1 
ATOM   2173  H HD13   . LEU A 1 137 ? 18.162  -40.296 -11.262 1.00 22.73  ?  137  LEU A HD13   1 
ATOM   2174  H HD21   . LEU A 1 137 ? 20.581  -38.875 -10.766 1.00 22.77  ?  137  LEU A HD21   1 
ATOM   2175  H HD22   . LEU A 1 137 ? 20.736  -40.451 -10.886 1.00 22.77  ?  137  LEU A HD22   1 
ATOM   2176  H HD23   . LEU A 1 137 ? 21.628  -39.495 -11.787 1.00 22.77  ?  137  LEU A HD23   1 
ATOM   2177  N N      . GLY A 1 138 ? 21.322  -42.771 -15.841 1.00 16.69  ?  138  GLY A N      1 
ATOM   2178  C CA     . GLY A 1 138 ? 21.398  -44.139 -16.318 1.00 18.18  ?  138  GLY A CA     1 
ATOM   2179  C C      . GLY A 1 138 ? 20.094  -44.897 -16.258 1.00 18.14  ?  138  GLY A C      1 
ATOM   2180  O O      . GLY A 1 138 ? 20.093  -46.111 -16.014 1.00 18.60  ?  138  GLY A O      1 
ATOM   2181  H H      . GLY A 1 138 ? 21.338  -42.175 -16.461 1.00 20.02  ?  138  GLY A H      1 
ATOM   2182  H HA2    . GLY A 1 138 ? 21.695  -44.131 -17.242 1.00 21.82  ?  138  GLY A HA2    1 
ATOM   2183  H HA3    . GLY A 1 138 ? 22.047  -44.621 -15.782 1.00 21.82  ?  138  GLY A HA3    1 
ATOM   2184  N N      . ARG A 1 139 ? 18.970  -44.209 -16.465 1.00 16.86  ?  139  ARG A N      1 
ATOM   2185  C CA     . ARG A 1 139 ? 17.632  -44.802 -16.452 1.00 16.37  ?  139  ARG A CA     1 
ATOM   2186  C C      . ARG A 1 139 ? 16.981  -44.505 -17.799 1.00 16.22  ?  139  ARG A C      1 
ATOM   2187  O O      . ARG A 1 139 ? 16.000  -43.750 -17.894 1.00 15.66  ?  139  ARG A O      1 
ATOM   2188  C CB     . ARG A 1 139 ? 16.805  -44.273 -15.283 1.00 17.00  ?  139  ARG A CB     1 
ATOM   2189  C CG     . ARG A 1 139 ? 17.540  -44.397 -13.954 1.00 18.21  ?  139  ARG A CG     1 
ATOM   2190  C CD     . ARG A 1 139 ? 16.692  -44.108 -12.732 1.00 17.02  ?  139  ARG A CD     1 
ATOM   2191  N NE     . ARG A 1 139 ? 16.040  -42.803 -12.750 1.00 16.90  ?  139  ARG A NE     1 
ATOM   2192  C CZ     . ARG A 1 139 ? 15.378  -42.315 -11.716 1.00 16.36  ?  139  ARG A CZ     1 
ATOM   2193  N NH1    . ARG A 1 139 ? 15.343  -42.988 -10.573 1.00 20.97  ?  139  ARG A NH1    1 
ATOM   2194  N NH2    . ARG A 1 139 ? 14.761  -41.156 -11.824 1.00 16.73  ?  139  ARG A NH2    1 
ATOM   2195  H H      . ARG A 1 139 ? 18.960  -43.363 -16.621 1.00 20.23  ?  139  ARG A H      1 
ATOM   2196  H HA     . ARG A 1 139 ? 17.687  -45.765 -16.347 1.00 19.64  ?  139  ARG A HA     1 
ATOM   2197  H HB2    . ARG A 1 139 ? 16.606  -43.336 -15.433 1.00 20.39  ?  139  ARG A HB2    1 
ATOM   2198  H HB3    . ARG A 1 139 ? 15.980  -44.781 -15.222 1.00 20.39  ?  139  ARG A HB3    1 
ATOM   2199  H HG2    . ARG A 1 139 ? 17.873  -45.304 -13.869 1.00 21.84  ?  139  ARG A HG2    1 
ATOM   2200  H HG3    . ARG A 1 139 ? 18.279  -43.770 -13.951 1.00 21.84  ?  139  ARG A HG3    1 
ATOM   2201  H HD2    . ARG A 1 139 ? 15.997  -44.782 -12.669 1.00 20.42  ?  139  ARG A HD2    1 
ATOM   2202  H HD3    . ARG A 1 139 ? 17.259  -44.142 -11.945 1.00 20.42  ?  139  ARG A HD3    1 
ATOM   2203  H HE     . ARG A 1 139 ? 16.089  -42.329 -13.466 1.00 20.28  ?  139  ARG A HE     1 
ATOM   2204  H HH11   . ARG A 1 139 ? 15.751  -43.742 -10.505 1.00 25.17  ?  139  ARG A HH11   1 
ATOM   2205  H HH12   . ARG A 1 139 ? 14.912  -42.670 -9.900  1.00 25.17  ?  139  ARG A HH12   1 
ATOM   2206  H HH21   . ARG A 1 139 ? 14.790  -40.720 -12.565 1.00 20.08  ?  139  ARG A HH21   1 
ATOM   2207  H HH22   . ARG A 1 139 ? 14.329  -40.834 -11.154 1.00 20.08  ?  139  ARG A HH22   1 
ATOM   2208  N N      . PRO A 1 140 ? 17.509  -45.100 -18.868 1.00 17.36  ?  140  PRO A N      1 
ATOM   2209  C CA     . PRO A 1 140 ? 17.022  -44.763 -20.215 1.00 18.09  ?  140  PRO A CA     1 
ATOM   2210  C C      . PRO A 1 140 ? 15.553  -45.077 -20.445 1.00 16.80  ?  140  PRO A C      1 
ATOM   2211  O O      . PRO A 1 140 ? 14.942  -44.455 -21.321 1.00 18.11  ?  140  PRO A O      1 
ATOM   2212  C CB     . PRO A 1 140 ? 17.936  -45.567 -21.148 1.00 20.75  ?  140  PRO A CB     1 
ATOM   2213  C CG     . PRO A 1 140 ? 18.454  -46.689 -20.274 1.00 20.18  ?  140  PRO A CG     1 
ATOM   2214  C CD     . PRO A 1 140 ? 18.569  -46.109 -18.888 1.00 19.82  ?  140  PRO A CD     1 
ATOM   2215  H HA     . PRO A 1 140 ? 17.165  -43.818 -20.381 1.00 21.71  ?  140  PRO A HA     1 
ATOM   2216  H HB2    . PRO A 1 140 ? 17.428  -45.913 -21.899 1.00 24.89  ?  140  PRO A HB2    1 
ATOM   2217  H HB3    . PRO A 1 140 ? 18.662  -45.008 -21.468 1.00 24.89  ?  140  PRO A HB3    1 
ATOM   2218  H HG2    . PRO A 1 140 ? 17.827  -47.429 -20.286 1.00 24.21  ?  140  PRO A HG2    1 
ATOM   2219  H HG3    . PRO A 1 140 ? 19.320  -46.982 -20.597 1.00 24.21  ?  140  PRO A HG3    1 
ATOM   2220  H HD2    . PRO A 1 140 ? 18.414  -46.788 -18.213 1.00 23.79  ?  140  PRO A HD2    1 
ATOM   2221  H HD3    . PRO A 1 140 ? 19.439  -45.700 -18.753 1.00 23.79  ?  140  PRO A HD3    1 
ATOM   2222  N N      . GLN A 1 141 ? 14.971  -46.020 -19.720 1.00 14.93  ?  141  GLN A N      1 
ATOM   2223  C CA     . GLN A 1 141 ? 13.558  -46.309 -19.898 1.00 13.95  ?  141  GLN A CA     1 
ATOM   2224  C C      . GLN A 1 141 ? 12.642  -45.389 -19.106 1.00 14.54  ?  141  GLN A C      1 
ATOM   2225  O O      . GLN A 1 141 ? 11.438  -45.361 -19.378 1.00 16.05  ?  141  GLN A O      1 
ATOM   2226  C CB     . GLN A 1 141 ? 13.238  -47.747 -19.489 1.00 18.03  ?  141  GLN A CB     1 
ATOM   2227  C CG     . GLN A 1 141 ? 13.910  -48.820 -20.303 1.00 21.16  ?  141  GLN A CG     1 
ATOM   2228  C CD     . GLN A 1 141 ? 13.357  -50.192 -19.958 1.00 23.62  ?  141  GLN A CD     1 
ATOM   2229  O OE1    . GLN A 1 141 ? 12.165  -50.444 -20.121 1.00 26.02  ?  141  GLN A OE1    1 
ATOM   2230  N NE2    . GLN A 1 141 ? 14.200  -51.064 -19.453 1.00 23.80  ?  141  GLN A NE2    1 
ATOM   2231  H H      . GLN A 1 141 ? 15.368  -46.499 -19.126 1.00 17.92  ?  141  GLN A H      1 
ATOM   2232  H HA     . GLN A 1 141 ? 13.364  -46.204 -20.843 1.00 16.74  ?  141  GLN A HA     1 
ATOM   2233  H HB2    . GLN A 1 141 ? 13.513  -47.869 -18.567 1.00 21.63  ?  141  GLN A HB2    1 
ATOM   2234  H HB3    . GLN A 1 141 ? 12.281  -47.880 -19.570 1.00 21.63  ?  141  GLN A HB3    1 
ATOM   2235  H HG2    . GLN A 1 141 ? 13.755  -48.654 -21.246 1.00 25.39  ?  141  GLN A HG2    1 
ATOM   2236  H HG3    . GLN A 1 141 ? 14.862  -48.817 -20.117 1.00 25.39  ?  141  GLN A HG3    1 
ATOM   2237  H HE21   . GLN A 1 141 ? 15.023  -50.846 -19.331 1.00 28.56  ?  141  GLN A HE21   1 
ATOM   2238  H HE22   . GLN A 1 141 ? 13.928  -51.853 -19.244 1.00 28.56  ?  141  GLN A HE22   1 
ATOM   2239  N N      . LYS A 1 142 ? 13.165  -44.642 -18.134 1.00 14.57  ?  142  LYS A N      1 
ATOM   2240  C CA     . LYS A 1 142 ? 12.323  -43.872 -17.219 1.00 13.81  ?  142  LYS A CA     1 
ATOM   2241  C C      . LYS A 1 142 ? 12.026  -42.523 -17.856 1.00 13.52  ?  142  LYS A C      1 
ATOM   2242  O O      . LYS A 1 142 ? 12.694  -41.515 -17.604 1.00 13.54  ?  142  LYS A O      1 
ATOM   2243  C CB     . LYS A 1 142 ? 12.976  -43.769 -15.844 1.00 14.22  ?  142  LYS A CB     1 
ATOM   2244  C CG     . LYS A 1 142 ? 11.975  -43.392 -14.745 1.00 15.17  ?  142  LYS A CG     1 
ATOM   2245  C CD     . LYS A 1 142 ? 12.564  -43.613 -13.381 1.00 15.60  ?  142  LYS A CD     1 
ATOM   2246  C CE     . LYS A 1 142 ? 11.699  -43.052 -12.256 1.00 15.01  ?  142  LYS A CE     1 
ATOM   2247  N NZ     . LYS A 1 142 ? 10.495  -43.865 -11.923 1.00 14.49  ?  142  LYS A NZ     1 
ATOM   2248  H H      . LYS A 1 142 ? 14.009  -44.566 -17.985 1.00 17.48  ?  142  LYS A H      1 
ATOM   2249  H HA     . LYS A 1 142 ? 11.471  -44.320 -17.100 1.00 16.57  ?  142  LYS A HA     1 
ATOM   2250  H HB2    . LYS A 1 142 ? 13.366  -44.627 -15.615 1.00 17.06  ?  142  LYS A HB2    1 
ATOM   2251  H HB3    . LYS A 1 142 ? 13.665  -43.087 -15.872 1.00 17.06  ?  142  LYS A HB3    1 
ATOM   2252  H HG2    . LYS A 1 142 ? 11.740  -42.454 -14.829 1.00 18.20  ?  142  LYS A HG2    1 
ATOM   2253  H HG3    . LYS A 1 142 ? 11.180  -43.942 -14.828 1.00 18.20  ?  142  LYS A HG3    1 
ATOM   2254  H HD2    . LYS A 1 142 ? 12.664  -44.566 -13.232 1.00 18.72  ?  142  LYS A HD2    1 
ATOM   2255  H HD3    . LYS A 1 142 ? 13.429  -43.177 -13.337 1.00 18.72  ?  142  LYS A HD3    1 
ATOM   2256  H HE2    . LYS A 1 142 ? 12.240  -42.992 -11.453 1.00 18.00  ?  142  LYS A HE2    1 
ATOM   2257  H HE3    . LYS A 1 142 ? 11.391  -42.169 -12.515 1.00 18.00  ?  142  LYS A HE3    1 
ATOM   2258  H HZ1    . LYS A 1 142 ? 10.063  -43.502 -11.235 1.00 17.39  ?  142  LYS A HZ1    1 
ATOM   2259  H HZ2    . LYS A 1 142 ? 9.946   -43.898 -12.624 1.00 17.39  ?  142  LYS A HZ2    1 
ATOM   2260  H HZ3    . LYS A 1 142 ? 10.737  -44.694 -11.707 1.00 17.39  ?  142  LYS A HZ3    1 
ATOM   2261  N N      . LYS A 1 143 ? 10.970  -42.507 -18.674 1.00 12.95  ?  143  LYS A N      1 
ATOM   2262  C CA     . LYS A 1 143 ? 10.727  -41.391 -19.576 1.00 14.01  ?  143  LYS A CA     1 
ATOM   2263  C C      . LYS A 1 143 ? 9.275   -40.998 -19.736 1.00 14.96  ?  143  LYS A C      1 
ATOM   2264  O O      . LYS A 1 143 ? 9.024   -39.897 -20.233 1.00 15.64  ?  143  LYS A O      1 
ATOM   2265  C CB     . LYS A 1 143 ? 11.277  -41.723 -20.977 1.00 14.95  ?  143  LYS A CB     1 
ATOM   2266  C CG     . LYS A 1 143 ? 12.777  -41.986 -21.026 1.00 13.59  ?  143  LYS A CG     1 
ATOM   2267  C CD     . LYS A 1 143 ? 13.592  -40.761 -20.640 1.00 15.60  ?  143  LYS A CD     1 
ATOM   2268  C CE     . LYS A 1 143 ? 15.080  -41.102 -20.545 1.00 14.15  ?  143  LYS A CE     1 
ATOM   2269  N NZ     . LYS A 1 143 ? 15.572  -41.789 -21.781 1.00 15.96  ?  143  LYS A NZ     1 
ATOM   2270  H H      . LYS A 1 143 ? 10.383  -43.133 -18.723 1.00 15.54  ?  143  LYS A H      1 
ATOM   2271  H HA     . LYS A 1 143 ? 11.196  -40.618 -19.223 1.00 16.81  ?  143  LYS A HA     1 
ATOM   2272  H HB2    . LYS A 1 143 ? 10.830  -42.520 -21.302 1.00 17.94  ?  143  LYS A HB2    1 
ATOM   2273  H HB3    . LYS A 1 143 ? 11.092  -40.975 -21.566 1.00 17.94  ?  143  LYS A HB3    1 
ATOM   2274  H HG2    . LYS A 1 143 ? 12.995  -42.700 -20.407 1.00 16.30  ?  143  LYS A HG2    1 
ATOM   2275  H HG3    . LYS A 1 143 ? 13.025  -42.241 -21.928 1.00 16.30  ?  143  LYS A HG3    1 
ATOM   2276  H HD2    . LYS A 1 143 ? 13.477  -40.071 -21.313 1.00 18.72  ?  143  LYS A HD2    1 
ATOM   2277  H HD3    . LYS A 1 143 ? 13.295  -40.434 -19.776 1.00 18.72  ?  143  LYS A HD3    1 
ATOM   2278  H HE2    . LYS A 1 143 ? 15.589  -40.284 -20.429 1.00 16.98  ?  143  LYS A HE2    1 
ATOM   2279  H HE3    . LYS A 1 143 ? 15.226  -41.693 -19.790 1.00 16.98  ?  143  LYS A HE3    1 
ATOM   2280  H HZ1    . LYS A 1 143 ? 16.455  -41.896 -21.740 1.00 19.15  ?  143  LYS A HZ1    1 
ATOM   2281  H HZ2    . LYS A 1 143 ? 15.188  -42.588 -21.858 1.00 19.15  ?  143  LYS A HZ2    1 
ATOM   2282  H HZ3    . LYS A 1 143 ? 15.374  -41.303 -22.500 1.00 19.15  ?  143  LYS A HZ3    1 
ATOM   2283  N N      . LYS A 1 144 ? 8.300   -41.841 -19.400 1.00 12.88  ?  144  LYS A N      1 
ATOM   2284  C CA     . LYS A 1 144 ? 6.909   -41.489 -19.643 1.00 12.80  ?  144  LYS A CA     1 
ATOM   2285  C C      . LYS A 1 144 ? 6.489   -40.364 -18.717 1.00 12.57  ?  144  LYS A C      1 
ATOM   2286  O O      . LYS A 1 144 ? 6.942   -40.265 -17.574 1.00 13.84  ?  144  LYS A O      1 
ATOM   2287  C CB     . LYS A 1 144 ? 5.995   -42.688 -19.446 1.00 14.53  ?  144  LYS A CB     1 
ATOM   2288  C CG     . LYS A 1 144 ? 6.285   -43.833 -20.409 1.00 14.26  ?  144  LYS A CG     1 
ATOM   2289  C CD     . LYS A 1 144 ? 5.640   -45.118 -19.969 1.00 14.53  ?  144  LYS A CD     1 
ATOM   2290  C CE     . LYS A 1 144 ? 6.046   -46.260 -20.875 1.00 14.54  ?  144  LYS A CE     1 
ATOM   2291  N NZ     . LYS A 1 144 ? 5.582   -47.578 -20.347 1.00 16.55  ?  144  LYS A NZ     1 
ATOM   2292  H H      . LYS A 1 144 ? 8.418   -42.611 -19.035 1.00 15.46  ?  144  LYS A H      1 
ATOM   2293  H HA     . LYS A 1 144 ? 6.809   -41.197 -20.562 1.00 15.35  ?  144  LYS A HA     1 
ATOM   2294  H HB2    . LYS A 1 144 ? 6.108   -43.022 -18.542 1.00 17.43  ?  144  LYS A HB2    1 
ATOM   2295  H HB3    . LYS A 1 144 ? 5.077   -42.407 -19.584 1.00 17.43  ?  144  LYS A HB3    1 
ATOM   2296  H HG2    . LYS A 1 144 ? 5.940   -43.607 -21.287 1.00 17.11  ?  144  LYS A HG2    1 
ATOM   2297  H HG3    . LYS A 1 144 ? 7.243   -43.976 -20.455 1.00 17.11  ?  144  LYS A HG3    1 
ATOM   2298  H HD2    . LYS A 1 144 ? 5.920   -45.329 -19.065 1.00 17.43  ?  144  LYS A HD2    1 
ATOM   2299  H HD3    . LYS A 1 144 ? 4.675   -45.026 -20.005 1.00 17.43  ?  144  LYS A HD3    1 
ATOM   2300  H HE2    . LYS A 1 144 ? 5.652   -46.129 -21.752 1.00 17.45  ?  144  LYS A HE2    1 
ATOM   2301  H HE3    . LYS A 1 144 ? 7.013   -46.284 -20.946 1.00 17.45  ?  144  LYS A HE3    1 
ATOM   2302  H HZ1    . LYS A 1 144 ? 5.768   -48.223 -20.932 1.00 19.86  ?  144  LYS A HZ1    1 
ATOM   2303  H HZ2    . LYS A 1 144 ? 5.992   -47.759 -19.578 1.00 19.86  ?  144  LYS A HZ2    1 
ATOM   2304  H HZ3    . LYS A 1 144 ? 4.703   -47.558 -20.208 1.00 19.86  ?  144  LYS A HZ3    1 
ATOM   2305  N N      . VAL A 1 145 ? 5.628   -39.485 -19.228 1.00 12.02  ?  145  VAL A N      1 
ATOM   2306  C CA     . VAL A 1 145 ? 5.101   -38.360 -18.469 1.00 12.53  ?  145  VAL A CA     1 
ATOM   2307  C C      . VAL A 1 145 ? 3.594   -38.491 -18.387 1.00 12.09  ?  145  VAL A C      1 
ATOM   2308  O O      . VAL A 1 145 ? 2.924   -38.656 -19.417 1.00 12.80  ?  145  VAL A O      1 
ATOM   2309  C CB     . VAL A 1 145 ? 5.512   -37.006 -19.084 1.00 13.45  ?  145  VAL A CB     1 
ATOM   2310  C CG1    . VAL A 1 145 ? 4.891   -35.859 -18.315 1.00 12.54  ?  145  VAL A CG1    1 
ATOM   2311  C CG2    . VAL A 1 145 ? 7.031   -36.895 -19.091 1.00 15.18  ?  145  VAL A CG2    1 
ATOM   2312  H H      . VAL A 1 145 ? 5.330   -39.526 -20.034 1.00 14.42  ?  145  VAL A H      1 
ATOM   2313  H HA     . VAL A 1 145 ? 5.452   -38.396 -17.565 1.00 15.03  ?  145  VAL A HA     1 
ATOM   2314  H HB     . VAL A 1 145 ? 5.190   -36.953 -19.997 1.00 16.14  ?  145  VAL A HB     1 
ATOM   2315  H HG11   . VAL A 1 145 ? 5.266   -35.024 -18.635 1.00 15.04  ?  145  VAL A HG11   1 
ATOM   2316  H HG12   . VAL A 1 145 ? 3.932   -35.866 -18.456 1.00 15.04  ?  145  VAL A HG12   1 
ATOM   2317  H HG13   . VAL A 1 145 ? 5.087   -35.969 -17.371 1.00 15.04  ?  145  VAL A HG13   1 
ATOM   2318  H HG21   . VAL A 1 145 ? 7.283   -36.042 -19.477 1.00 18.21  ?  145  VAL A HG21   1 
ATOM   2319  H HG22   . VAL A 1 145 ? 7.356   -36.954 -18.179 1.00 18.21  ?  145  VAL A HG22   1 
ATOM   2320  H HG23   . VAL A 1 145 ? 7.398   -37.620 -19.621 1.00 18.21  ?  145  VAL A HG23   1 
ATOM   2321  N N      . ILE A 1 146 ? 3.070   -38.375 -17.168 1.00 11.30  ?  146  ILE A N      1 
ATOM   2322  C CA     . ILE A 1 146 ? 1.648   -38.510 -16.890 1.00 10.45  ?  146  ILE A CA     1 
ATOM   2323  C C      . ILE A 1 146 ? 1.075   -37.123 -16.639 1.00 10.82  ?  146  ILE A C      1 
ATOM   2324  O O      . ILE A 1 146 ? 1.483   -36.433 -15.701 1.00 11.94  ?  146  ILE A O      1 
ATOM   2325  C CB     . ILE A 1 146 ? 1.397   -39.421 -15.685 1.00 11.14  ?  146  ILE A CB     1 
ATOM   2326  C CG1    . ILE A 1 146 ? 1.920   -40.828 -15.960 1.00 14.50  ?  146  ILE A CG1    1 
ATOM   2327  C CG2    . ILE A 1 146 ? -0.078  -39.488 -15.363 1.00 12.78  ?  146  ILE A CG2    1 
ATOM   2328  C CD1    . ILE A 1 146 ? 1.819   -41.777 -14.782 1.00 13.59  ?  146  ILE A CD1    1 
ATOM   2329  H H      . ILE A 1 146 ? 3.538   -38.212 -16.465 1.00 13.55  ?  146  ILE A H      1 
ATOM   2330  H HA     . ILE A 1 146 ? 1.211   -38.892 -17.667 1.00 12.54  ?  146  ILE A HA     1 
ATOM   2331  H HB     . ILE A 1 146 ? 1.871   -39.045 -14.926 1.00 13.36  ?  146  ILE A HB     1 
ATOM   2332  H HG12   . ILE A 1 146 ? 1.409   -41.211 -16.690 1.00 17.40  ?  146  ILE A HG12   1 
ATOM   2333  H HG13   . ILE A 1 146 ? 2.856   -40.767 -16.207 1.00 17.40  ?  146  ILE A HG13   1 
ATOM   2334  H HG21   . ILE A 1 146 ? -0.219  -40.138 -14.657 1.00 15.34  ?  146  ILE A HG21   1 
ATOM   2335  H HG22   . ILE A 1 146 ? -0.378  -38.612 -15.071 1.00 15.34  ?  146  ILE A HG22   1 
ATOM   2336  H HG23   . ILE A 1 146 ? -0.563  -39.754 -16.160 1.00 15.34  ?  146  ILE A HG23   1 
ATOM   2337  H HD11   . ILE A 1 146 ? 2.293   -42.596 -14.995 1.00 16.30  ?  146  ILE A HD11   1 
ATOM   2338  H HD12   . ILE A 1 146 ? 2.217   -41.357 -14.003 1.00 16.30  ?  146  ILE A HD12   1 
ATOM   2339  H HD13   . ILE A 1 146 ? 0.884   -41.971 -14.612 1.00 16.30  ?  146  ILE A HD13   1 
ATOM   2340  N N      . ALA A 1 147 ? 0.115   -36.724 -17.473 1.00 12.26  ?  147  ALA A N      1 
ATOM   2341  C CA     . ALA A 1 147 ? -0.732  -35.565 -17.261 1.00 12.09  ?  147  ALA A CA     1 
ATOM   2342  C C      . ALA A 1 147 ? -2.137  -36.059 -16.910 1.00 11.09  ?  147  ALA A C      1 
ATOM   2343  O O      . ALA A 1 147 ? -2.342  -37.234 -16.624 1.00 12.07  ?  147  ALA A O      1 
ATOM   2344  C CB     . ALA A 1 147 ? -0.724  -34.658 -18.502 1.00 13.47  ?  147  ALA A CB     1 
ATOM   2345  H H      . ALA A 1 147 ? -0.068  -37.136 -18.205 1.00 14.71  ?  147  ALA A H      1 
ATOM   2346  H HA     . ALA A 1 147 ? -0.385  -35.038 -16.524 1.00 14.50  ?  147  ALA A HA     1 
ATOM   2347  H HB1    . ALA A 1 147 ? -1.216  -33.845 -18.302 1.00 16.16  ?  147  ALA A HB1    1 
ATOM   2348  H HB2    . ALA A 1 147 ? 0.193   -34.442 -18.730 1.00 16.16  ?  147  ALA A HB2    1 
ATOM   2349  H HB3    . ALA A 1 147 ? -1.147  -35.127 -19.239 1.00 16.16  ?  147  ALA A HB3    1 
ATOM   2350  N N      . ARG A 1 148 ? -3.109  -35.153 -16.943 1.00 12.08  ?  148  ARG A N      1 
ATOM   2351  C CA     . ARG A 1 148 ? -4.464  -35.480 -16.532 1.00 12.94  ?  148  ARG A CA     1 
ATOM   2352  C C      . ARG A 1 148 ? -5.475  -35.055 -17.575 1.00 12.01  ?  148  ARG A C      1 
ATOM   2353  O O      . ARG A 1 148 ? -5.307  -34.041 -18.256 1.00 12.13  ?  148  ARG A O      1 
ATOM   2354  C CB     . ARG A 1 148 ? -4.806  -34.783 -15.226 1.00 13.21  ?  148  ARG A CB     1 
ATOM   2355  C CG     . ARG A 1 148 ? -3.836  -35.182 -14.148 1.00 13.60  ?  148  ARG A CG     1 
ATOM   2356  C CD     . ARG A 1 148 ? -4.034  -34.406 -12.888 1.00 15.36  ?  148  ARG A CD     1 
ATOM   2357  N NE     . ARG A 1 148 ? -3.919  -32.969 -13.086 1.00 13.73  ?  148  ARG A NE     1 
ATOM   2358  C CZ     . ARG A 1 148 ? -4.125  -32.088 -12.121 1.00 12.88  ?  148  ARG A CZ     1 
ATOM   2359  N NH1    . ARG A 1 148 ? -4.365  -32.528 -10.892 1.00 12.55  ?  148  ARG A NH1    1 
ATOM   2360  N NH2    . ARG A 1 148 ? -4.073  -30.787 -12.377 1.00 14.73  ?  148  ARG A NH2    1 
ATOM   2361  H H      . ARG A 1 148 ? -3.003  -34.339 -17.201 1.00 14.49  ?  148  ARG A H      1 
ATOM   2362  H HA     . ARG A 1 148 ? -4.530  -36.443 -16.433 1.00 15.53  ?  148  ARG A HA     1 
ATOM   2363  H HB2    . ARG A 1 148 ? -4.756  -33.822 -15.349 1.00 15.84  ?  148  ARG A HB2    1 
ATOM   2364  H HB3    . ARG A 1 148 ? -5.700  -35.035 -14.948 1.00 15.84  ?  148  ARG A HB3    1 
ATOM   2365  H HG2    . ARG A 1 148 ? -3.957  -36.122 -13.944 1.00 16.31  ?  148  ARG A HG2    1 
ATOM   2366  H HG3    . ARG A 1 148 ? -2.931  -35.023 -14.460 1.00 16.31  ?  148  ARG A HG3    1 
ATOM   2367  H HD2    . ARG A 1 148 ? -4.920  -34.590 -12.540 1.00 18.43  ?  148  ARG A HD2    1 
ATOM   2368  H HD3    . ARG A 1 148 ? -3.361  -34.674 -12.243 1.00 18.43  ?  148  ARG A HD3    1 
ATOM   2369  H HE     . ARG A 1 148 ? -3.706  -32.679 -13.867 1.00 16.47  ?  148  ARG A HE     1 
ATOM   2370  H HH11   . ARG A 1 148 ? -4.385  -33.373 -10.735 1.00 15.05  ?  148  ARG A HH11   1 
ATOM   2371  H HH12   . ARG A 1 148 ? -4.501  -31.968 -10.254 1.00 15.05  ?  148  ARG A HH12   1 
ATOM   2372  H HH21   . ARG A 1 148 ? -3.904  -30.512 -13.175 1.00 17.68  ?  148  ARG A HH21   1 
ATOM   2373  H HH22   . ARG A 1 148 ? -4.208  -30.219 -11.746 1.00 17.68  ?  148  ARG A HH22   1 
ATOM   2374  N N      . GLN A 1 149 ? -6.536  -35.858 -17.695 1.00 11.62  ?  149  GLN A N      1 
ATOM   2375  C CA     . GLN A 1 149 ? -7.687  -35.408 -18.461 1.00 13.06  ?  149  GLN A CA     1 
ATOM   2376  C C      . GLN A 1 149 ? -8.099  -34.025 -17.963 1.00 11.33  ?  149  GLN A C      1 
ATOM   2377  O O      . GLN A 1 149 ? -8.131  -33.770 -16.755 1.00 12.63  ?  149  GLN A O      1 
ATOM   2378  C CB     . GLN A 1 149 ? -8.846  -36.397 -18.340 1.00 14.18  ?  149  GLN A CB     1 
ATOM   2379  C CG     . GLN A 1 149 ? -8.531  -37.754 -18.911 1.00 17.74  ?  149  GLN A CG     1 
ATOM   2380  C CD     . GLN A 1 149 ? -8.297  -37.784 -20.399 1.00 26.67  ?  149  GLN A CD     1 
ATOM   2381  O OE1    . GLN A 1 149 ? -8.313  -36.754 -21.069 1.00 32.17  ?  149  GLN A OE1    1 
ATOM   2382  N NE2    . GLN A 1 149 ? -8.078  -38.990 -20.937 1.00 29.50  ?  149  GLN A NE2    1 
ATOM   2383  H H      . GLN A 1 149 ? -6.609  -36.643 -17.350 1.00 13.94  ?  149  GLN A H      1 
ATOM   2384  H HA     . GLN A 1 149 ? -7.463  -35.357 -19.404 1.00 15.67  ?  149  GLN A HA     1 
ATOM   2385  H HB2    . GLN A 1 149 ? -9.064  -36.511 -17.402 1.00 17.02  ?  149  GLN A HB2    1 
ATOM   2386  H HB3    . GLN A 1 149 ? -9.612  -36.043 -18.818 1.00 17.02  ?  149  GLN A HB3    1 
ATOM   2387  H HG2    . GLN A 1 149 ? -7.726  -38.087 -18.484 1.00 21.29  ?  149  GLN A HG2    1 
ATOM   2388  H HG3    . GLN A 1 149 ? -9.276  -38.346 -18.722 1.00 21.29  ?  149  GLN A HG3    1 
ATOM   2389  H HE21   . GLN A 1 149 ? -8.077  -39.690 -20.437 1.00 35.40  ?  149  GLN A HE21   1 
ATOM   2390  H HE22   . GLN A 1 149 ? -7.939  -39.066 -21.782 1.00 35.40  ?  149  GLN A HE22   1 
ATOM   2391  N N      . ARG A 1 150 ? -8.374  -33.117 -18.902 1.00 12.91  ?  150  ARG A N      1 
ATOM   2392  C CA     . ARG A 1 150 ? -8.775  -31.726 -18.669 1.00 13.01  ?  150  ARG A CA     1 
ATOM   2393  C C      . ARG A 1 150 ? -7.671  -30.823 -18.138 1.00 12.21  ?  150  ARG A C      1 
ATOM   2394  O O      . ARG A 1 150 ? -7.936  -29.639 -17.903 1.00 13.44  ?  150  ARG A O      1 
ATOM   2395  C CB     . ARG A 1 150 ? -10.051 -31.609 -17.811 1.00 14.78  ?  150  ARG A CB     1 
ATOM   2396  C CG     . ARG A 1 150 ? -11.199 -32.429 -18.428 1.00 15.30  ?  150  ARG A CG     1 
ATOM   2397  C CD     . ARG A 1 150 ? -12.529 -32.034 -17.930 1.00 17.06  ?  150  ARG A CD     1 
ATOM   2398  N NE     . ARG A 1 150 ? -12.885 -30.672 -18.263 1.00 16.78  ?  150  ARG A NE     1 
ATOM   2399  C CZ     . ARG A 1 150 ? -13.861 -30.318 -19.079 1.00 17.76  ?  150  ARG A CZ     1 
ATOM   2400  N NH1    . ARG A 1 150 ? -14.564 -31.238 -19.726 1.00 20.54  ?  150  ARG A NH1    1 
ATOM   2401  N NH2    . ARG A 1 150 ? -14.117 -29.033 -19.267 1.00 18.37  ?  150  ARG A NH2    1 
ATOM   2402  H H      . ARG A 1 150 ? -8.328  -33.295 -19.744 1.00 15.49  ?  150  ARG A H      1 
ATOM   2403  H HA     . ARG A 1 150 ? -8.991  -31.350 -19.537 1.00 15.61  ?  150  ARG A HA     1 
ATOM   2404  H HB2    . ARG A 1 150 ? -9.874  -31.947 -16.920 1.00 17.73  ?  150  ARG A HB2    1 
ATOM   2405  H HB3    . ARG A 1 150 ? -10.325 -30.679 -17.765 1.00 17.73  ?  150  ARG A HB3    1 
ATOM   2406  H HG2    . ARG A 1 150 ? -11.193 -32.305 -19.390 1.00 18.36  ?  150  ARG A HG2    1 
ATOM   2407  H HG3    . ARG A 1 150 ? -11.068 -33.366 -18.213 1.00 18.36  ?  150  ARG A HG3    1 
ATOM   2408  H HD2    . ARG A 1 150 ? -13.197 -32.619 -18.319 1.00 20.47  ?  150  ARG A HD2    1 
ATOM   2409  H HD3    . ARG A 1 150 ? -12.539 -32.115 -16.963 1.00 20.47  ?  150  ARG A HD3    1 
ATOM   2410  H HE     . ARG A 1 150 ? -12.425 -30.042 -17.900 1.00 20.14  ?  150  ARG A HE     1 
ATOM   2411  H HH11   . ARG A 1 150 ? -14.386 -32.072 -19.616 1.00 24.64  ?  150  ARG A HH11   1 
ATOM   2412  H HH12   . ARG A 1 150 ? -15.198 -31.000 -20.256 1.00 24.64  ?  150  ARG A HH12   1 
ATOM   2413  H HH21   . ARG A 1 150 ? -13.649 -28.438 -18.860 1.00 22.04  ?  150  ARG A HH21   1 
ATOM   2414  H HH22   . ARG A 1 150 ? -14.751 -28.795 -19.797 1.00 22.04  ?  150  ARG A HH22   1 
ATOM   2415  N N      . GLY A 1 151 ? -6.438  -31.301 -17.992 1.00 11.41  ?  151  GLY A N      1 
ATOM   2416  C CA     . GLY A 1 151 ? -5.331  -30.404 -17.755 1.00 11.45  ?  151  GLY A CA     1 
ATOM   2417  C C      . GLY A 1 151 ? -5.061  -29.529 -18.964 1.00 11.41  ?  151  GLY A C      1 
ATOM   2418  O O      . GLY A 1 151 ? -5.425  -29.860 -20.098 1.00 12.03  ?  151  GLY A O      1 
ATOM   2419  H H      . GLY A 1 151 ? -6.223  -32.133 -18.026 1.00 13.69  ?  151  GLY A H      1 
ATOM   2420  H HA2    . GLY A 1 151 ? -5.532  -29.833 -16.998 1.00 13.74  ?  151  GLY A HA2    1 
ATOM   2421  H HA3    . GLY A 1 151 ? -4.532  -30.918 -17.561 1.00 13.74  ?  151  GLY A HA3    1 
ATOM   2422  N N      . TYR A 1 152 ? -4.424  -28.384 -18.721 1.00 10.42  ?  152  TYR A N      1 
ATOM   2423  C CA     . TYR A 1 152 ? -4.004  -27.503 -19.806 1.00 10.08  ?  152  TYR A CA     1 
ATOM   2424  C C      . TYR A 1 152 ? -2.560  -27.094 -19.580 1.00 11.42  ?  152  TYR A C      1 
ATOM   2425  O O      . TYR A 1 152 ? -2.238  -26.512 -18.541 1.00 12.31  ?  152  TYR A O      1 
ATOM   2426  C CB     . TYR A 1 152 ? -4.906  -26.268 -19.981 1.00 11.95  ?  152  TYR A CB     1 
ATOM   2427  C CG     . TYR A 1 152 ? -4.489  -25.529 -21.231 1.00 12.17  ?  152  TYR A CG     1 
ATOM   2428  C CD1    . TYR A 1 152 ? -4.879  -25.980 -22.485 1.00 12.09  ?  152  TYR A CD1    1 
ATOM   2429  C CD2    . TYR A 1 152 ? -3.653  -24.431 -21.164 1.00 13.45  ?  152  TYR A CD2    1 
ATOM   2430  C CE1    . TYR A 1 152 ? -4.466  -25.333 -23.632 1.00 13.62  ?  152  TYR A CE1    1 
ATOM   2431  C CE2    . TYR A 1 152 ? -3.231  -23.768 -22.322 1.00 13.98  ?  152  TYR A CE2    1 
ATOM   2432  C CZ     . TYR A 1 152 ? -3.637  -24.233 -23.548 1.00 13.83  ?  152  TYR A CZ     1 
ATOM   2433  O OH     . TYR A 1 152 ? -3.218  -23.625 -24.714 1.00 14.85  ?  152  TYR A OH     1 
ATOM   2434  H H      . TYR A 1 152 ? -4.225  -28.099 -17.934 1.00 12.51  ?  152  TYR A H      1 
ATOM   2435  H HA     . TYR A 1 152 ? -4.060  -28.007 -20.634 1.00 12.09  ?  152  TYR A HA     1 
ATOM   2436  H HB2    . TYR A 1 152 ? -5.831  -26.545 -20.071 1.00 14.33  ?  152  TYR A HB2    1 
ATOM   2437  H HB3    . TYR A 1 152 ? -4.809  -25.678 -19.217 1.00 14.33  ?  152  TYR A HB3    1 
ATOM   2438  H HD1    . TYR A 1 152 ? -5.427  -26.728 -22.552 1.00 14.51  ?  152  TYR A HD1    1 
ATOM   2439  H HD2    . TYR A 1 152 ? -3.366  -24.127 -20.334 1.00 16.14  ?  152  TYR A HD2    1 
ATOM   2440  H HE1    . TYR A 1 152 ? -4.748  -25.639 -24.464 1.00 16.34  ?  152  TYR A HE1    1 
ATOM   2441  H HE2    . TYR A 1 152 ? -2.682  -23.020 -22.262 1.00 16.77  ?  152  TYR A HE2    1 
ATOM   2442  H HH     . TYR A 1 152 ? -2.650  -23.031 -24.541 1.00 17.82  ?  152  TYR A HH     1 
ATOM   2443  N N      . HIS A 1 153 ? -1.702  -27.418 -20.543 1.00 11.03  ?  153  HIS A N      1 
ATOM   2444  C CA     . HIS A 1 153 ? -0.261  -27.242 -20.430 1.00 10.57  ?  153  HIS A CA     1 
ATOM   2445  C C      . HIS A 1 153 ? 0.336   -26.586 -21.669 1.00 11.69  ?  153  HIS A C      1 
ATOM   2446  O O      . HIS A 1 153 ? 1.571   -26.498 -21.786 1.00 12.60  ?  153  HIS A O      1 
ATOM   2447  C CB     . HIS A 1 153 ? 0.377   -28.590 -20.101 1.00 11.06  ?  153  HIS A CB     1 
ATOM   2448  C CG     . HIS A 1 153 ? -0.129  -29.177 -18.821 1.00 10.99  ?  153  HIS A CG     1 
ATOM   2449  N ND1    . HIS A 1 153 ? 0.120   -28.604 -17.588 1.00 11.32  ?  153  HIS A ND1    1 
ATOM   2450  C CD2    . HIS A 1 153 ? -0.920  -30.249 -18.584 1.00 11.29  ?  153  HIS A CD2    1 
ATOM   2451  C CE1    . HIS A 1 153 ? -0.480  -29.312 -16.649 1.00 12.82  ?  153  HIS A CE1    1 
ATOM   2452  N NE2    . HIS A 1 153 ? -1.147  -30.293 -17.229 1.00 11.42  ?  153  HIS A NE2    1 
ATOM   2453  H H      . HIS A 1 153 ? -1.940  -27.754 -21.298 1.00 13.24  ?  153  HIS A H      1 
ATOM   2454  H HA     . HIS A 1 153 ? -0.039  -26.645 -19.699 1.00 12.68  ?  153  HIS A HA     1 
ATOM   2455  H HB2    . HIS A 1 153 ? 0.179   -29.215 -20.816 1.00 13.26  ?  153  HIS A HB2    1 
ATOM   2456  H HB3    . HIS A 1 153 ? 1.336   -28.473 -20.019 1.00 13.26  ?  153  HIS A HB3    1 
ATOM   2457  H HD1    . HIS A 1 153 ? 0.591   -27.897 -17.454 1.00 13.57  ?  153  HIS A HD1    1 
ATOM   2458  H HD2    . HIS A 1 153 ? -1.248  -30.845 -19.218 1.00 13.55  ?  153  HIS A HD2    1 
ATOM   2459  H HE1    . HIS A 1 153 ? -0.440  -29.148 -15.734 1.00 15.38  ?  153  HIS A HE1    1 
ATOM   2460  N N      . GLY A 1 154 ? -0.491  -26.088 -22.578 1.00 11.41  ?  154  GLY A N      1 
ATOM   2461  C CA     . GLY A 1 154 ? 0.003   -25.421 -23.774 1.00 12.02  ?  154  GLY A CA     1 
ATOM   2462  C C      . GLY A 1 154 ? -0.563  -26.042 -25.044 1.00 11.18  ?  154  GLY A C      1 
ATOM   2463  O O      . GLY A 1 154 ? -1.388  -26.955 -25.018 1.00 10.94  ?  154  GLY A O      1 
ATOM   2464  H H      . GLY A 1 154 ? -1.349  -26.125 -22.521 1.00 13.68  ?  154  GLY A H      1 
ATOM   2465  H HA2    . GLY A 1 154 ? -0.250  -24.485 -23.751 1.00 14.43  ?  154  GLY A HA2    1 
ATOM   2466  H HA3    . GLY A 1 154 ? 0.970   -25.486 -23.805 1.00 14.43  ?  154  GLY A HA3    1 
ATOM   2467  N N      . SER A 1 155 ? -0.070  -25.515 -26.175 1.00 11.97  ?  155  SER A N      1 
ATOM   2468  C CA     . SER A 1 155 ? -0.713  -25.675 -27.478 1.00 10.24  ?  155  SER A CA     1 
ATOM   2469  C C      . SER A 1 155 ? 0.263   -26.043 -28.602 1.00 11.90  ?  155  SER A C      1 
ATOM   2470  O O      . SER A 1 155 ? -0.056  -25.881 -29.793 1.00 12.01  ?  155  SER A O      1 
ATOM   2471  C CB     . SER A 1 155 ? -1.444  -24.375 -27.792 1.00 10.95  ?  155  SER A CB     1 
ATOM   2472  O OG     . SER A 1 155 ? -2.197  -24.428 -28.995 1.00 11.99  ?  155  SER A OG     1 
ATOM   2473  H H      . SER A 1 155 ? 0.653   -25.051 -26.209 1.00 14.36  ?  155  SER A H      1 
ATOM   2474  H HA     . SER A 1 155 ? -1.341  -26.413 -27.445 1.00 12.28  ?  155  SER A HA     1 
ATOM   2475  H HB2    . SER A 1 155 ? -2.051  -24.180 -27.061 1.00 13.14  ?  155  SER A HB2    1 
ATOM   2476  H HB3    . SER A 1 155 ? -0.786  -23.667 -27.875 1.00 13.14  ?  155  SER A HB3    1 
ATOM   2477  H HG     . SER A 1 155 ? -1.686  -24.565 -29.648 1.00 14.38  ?  155  SER A HG     1 
ATOM   2478  N N      . GLY A 1 156 ? 1.426   -26.559 -28.270 1.00 11.49  ?  156  GLY A N      1 
ATOM   2479  C CA     . GLY A 1 156 ? 2.364   -27.068 -29.249 1.00 12.02  ?  156  GLY A CA     1 
ATOM   2480  C C      . GLY A 1 156 ? 2.176   -28.556 -29.502 1.00 11.61  ?  156  GLY A C      1 
ATOM   2481  O O      . GLY A 1 156 ? 1.146   -29.150 -29.174 1.00 12.35  ?  156  GLY A O      1 
ATOM   2482  H H      . GLY A 1 156 ? 1.704   -26.627 -27.459 1.00 13.79  ?  156  GLY A H      1 
ATOM   2483  H HA2    . GLY A 1 156 ? 2.241   -26.597 -30.088 1.00 14.42  ?  156  GLY A HA2    1 
ATOM   2484  H HA3    . GLY A 1 156 ? 3.269   -26.922 -28.935 1.00 14.42  ?  156  GLY A HA3    1 
ATOM   2485  N N      . ILE A 1 157 ? 3.220   -29.183 -30.054 1.00 13.58  ?  157  ILE A N      1 
ATOM   2486  C CA     . ILE A 1 157 ? 3.168   -30.636 -30.275 1.00 12.23  ?  157  ILE A CA     1 
ATOM   2487  C C      . ILE A 1 157 ? 3.326   -31.371 -28.946 1.00 11.26  ?  157  ILE A C      1 
ATOM   2488  O O      . ILE A 1 157 ? 2.411   -32.051 -28.490 1.00 11.96  ?  157  ILE A O      1 
ATOM   2489  C CB     . ILE A 1 157 ? 4.214   -31.079 -31.312 1.00 10.54  ?  157  ILE A CB     1 
ATOM   2490  C CG1    . ILE A 1 157 ? 3.900   -30.474 -32.690 1.00 11.74  ?  157  ILE A CG1    1 
ATOM   2491  C CG2    . ILE A 1 157 ? 4.281   -32.589 -31.436 1.00 11.60  ?  157  ILE A CG2    1 
ATOM   2492  C CD1    . ILE A 1 157 ? 2.671   -31.019 -33.353 1.00 12.48  ?  157  ILE A CD1    1 
ATOM   2493  H H      . ILE A 1 157 ? 3.951   -28.804 -30.304 1.00 16.30  ?  157  ILE A H      1 
ATOM   2494  H HA     . ILE A 1 157 ? 2.298   -30.862 -30.639 1.00 14.67  ?  157  ILE A HA     1 
ATOM   2495  H HB     . ILE A 1 157 ? 5.074   -30.756 -30.999 1.00 12.65  ?  157  ILE A HB     1 
ATOM   2496  H HG12   . ILE A 1 157 ? 3.774   -29.518 -32.584 1.00 14.09  ?  157  ILE A HG12   1 
ATOM   2497  H HG13   . ILE A 1 157 ? 4.650   -30.647 -33.280 1.00 14.09  ?  157  ILE A HG13   1 
ATOM   2498  H HG21   . ILE A 1 157 ? 4.809   -32.818 -32.217 1.00 13.92  ?  157  ILE A HG21   1 
ATOM   2499  H HG22   . ILE A 1 157 ? 4.695   -32.953 -30.638 1.00 13.92  ?  157  ILE A HG22   1 
ATOM   2500  H HG23   . ILE A 1 157 ? 3.381   -32.938 -31.530 1.00 13.92  ?  157  ILE A HG23   1 
ATOM   2501  H HD11   . ILE A 1 157 ? 2.500   -30.514 -34.163 1.00 14.98  ?  157  ILE A HD11   1 
ATOM   2502  H HD12   . ILE A 1 157 ? 2.818   -31.953 -33.570 1.00 14.98  ?  157  ILE A HD12   1 
ATOM   2503  H HD13   . ILE A 1 157 ? 1.920   -30.934 -32.745 1.00 14.98  ?  157  ILE A HD13   1 
ATOM   2504  N N      . ALA A 1 158 ? 4.458   -31.171 -28.260 1.00 11.53  ?  158  ALA A N      1 
ATOM   2505  C CA     . ALA A 1 158 ? 4.666   -31.851 -26.981 1.00 11.06  ?  158  ALA A CA     1 
ATOM   2506  C C      . ALA A 1 158 ? 3.853   -31.182 -25.870 1.00 10.84  ?  158  ALA A C      1 
ATOM   2507  O O      . ALA A 1 158 ? 3.156   -31.863 -25.111 1.00 12.98  ?  158  ALA A O      1 
ATOM   2508  C CB     . ALA A 1 158 ? 6.149   -31.899 -26.631 1.00 11.87  ?  158  ALA A CB     1 
ATOM   2509  H H      . ALA A 1 158 ? 5.104   -30.660 -28.507 1.00 13.84  ?  158  ALA A H      1 
ATOM   2510  H HA     . ALA A 1 158 ? 4.366   -32.770 -27.060 1.00 13.27  ?  158  ALA A HA     1 
ATOM   2511  H HB1    . ALA A 1 158 ? 6.257   -32.336 -25.772 1.00 14.24  ?  158  ALA A HB1    1 
ATOM   2512  H HB2    . ALA A 1 158 ? 6.619   -32.397 -27.317 1.00 14.24  ?  158  ALA A HB2    1 
ATOM   2513  H HB3    . ALA A 1 158 ? 6.493   -30.993 -26.586 1.00 14.24  ?  158  ALA A HB3    1 
ATOM   2514  N N      . SER A 1 159 ? 3.885   -29.847 -25.779 1.00 11.66  ?  159  SER A N      1 
ATOM   2515  C CA     . SER A 1 159 ? 3.094   -29.192 -24.740 1.00 11.35  ?  159  SER A CA     1 
ATOM   2516  C C      . SER A 1 159 ? 1.601   -29.468 -24.916 1.00 11.94  ?  159  SER A C      1 
ATOM   2517  O O      . SER A 1 159 ? 0.884   -29.669 -23.930 1.00 12.16  ?  159  SER A O      1 
ATOM   2518  C CB     . SER A 1 159 ? 3.397   -27.697 -24.692 1.00 12.89  ?  159  SER A CB     1 
ATOM   2519  O OG     . SER A 1 159 ? 2.981   -27.017 -25.874 1.00 13.42  ?  159  SER A OG     1 
ATOM   2520  H H      . SER A 1 159 ? 4.338   -29.319 -26.286 1.00 13.99  ?  159  SER A H      1 
ATOM   2521  H HA     . SER A 1 159 ? 3.351   -29.555 -23.878 1.00 13.62  ?  159  SER A HA     1 
ATOM   2522  H HB2    . SER A 1 159 ? 2.932   -27.311 -23.933 1.00 15.47  ?  159  SER A HB2    1 
ATOM   2523  H HB3    . SER A 1 159 ? 4.355   -27.579 -24.589 1.00 15.47  ?  159  SER A HB3    1 
ATOM   2524  H HG     . SER A 1 159 ? 3.428   -27.285 -26.533 1.00 16.10  ?  159  SER A HG     1 
ATOM   2525  N N      . GLY A 1 160 ? 1.117   -29.486 -26.160 1.00 12.03  ?  160  GLY A N      1 
ATOM   2526  C CA     . GLY A 1 160 ? -0.283  -29.800 -26.395 1.00 10.77  ?  160  GLY A CA     1 
ATOM   2527  C C      . GLY A 1 160 ? -0.624  -31.259 -26.169 1.00 10.98  ?  160  GLY A C      1 
ATOM   2528  O O      . GLY A 1 160 ? -1.770  -31.577 -25.883 1.00 12.75  ?  160  GLY A O      1 
ATOM   2529  H H      . GLY A 1 160 ? 1.571   -29.322 -26.871 1.00 14.44  ?  160  GLY A H      1 
ATOM   2530  H HA2    . GLY A 1 160 ? -0.831  -29.267 -25.799 1.00 12.93  ?  160  GLY A HA2    1 
ATOM   2531  H HA3    . GLY A 1 160 ? -0.506  -29.578 -27.313 1.00 12.93  ?  160  GLY A HA3    1 
ATOM   2532  N N      . SER A 1 161 ? 0.363   -32.149 -26.274 1.00 10.65  ?  161  SER A N      1 
ATOM   2533  C CA     . SER A 1 161 ? 0.187   -33.546 -25.887 1.00 11.35  ?  161  SER A CA     1 
ATOM   2534  C C      . SER A 1 161 ? -0.062  -33.665 -24.389 1.00 11.32  ?  161  SER A C      1 
ATOM   2535  O O      . SER A 1 161 ? -0.857  -34.499 -23.951 1.00 11.27  ?  161  SER A O      1 
ATOM   2536  C CB     . SER A 1 161 ? 1.430   -34.358 -26.246 1.00 11.68  ?  161  SER A CB     1 
ATOM   2537  O OG     . SER A 1 161 ? 1.562   -34.519 -27.652 1.00 11.85  ?  161  SER A OG     1 
ATOM   2538  H H      . SER A 1 161 ? 1.151   -31.971 -26.567 1.00 12.78  ?  161  SER A H      1 
ATOM   2539  H HA     . SER A 1 161 ? -0.573  -33.903 -26.373 1.00 13.62  ?  161  SER A HA     1 
ATOM   2540  H HB2    . SER A 1 161 ? 2.213   -33.895 -25.909 1.00 14.01  ?  161  SER A HB2    1 
ATOM   2541  H HB3    . SER A 1 161 ? 1.361   -35.234 -25.836 1.00 14.01  ?  161  SER A HB3    1 
ATOM   2542  H HG     . SER A 1 161 ? 1.642   -33.768 -28.021 1.00 14.22  ?  161  SER A HG     1 
ATOM   2543  N N      . LEU A 1 162 ? 0.653   -32.866 -23.592 1.00 12.01  ?  162  LEU A N      1 
ATOM   2544  C CA     . LEU A 1 162 ? 0.419   -32.829 -22.145 1.00 11.99  ?  162  LEU A CA     1 
ATOM   2545  C C      . LEU A 1 162 ? -0.996  -32.353 -21.817 1.00 11.37  ?  162  LEU A C      1 
ATOM   2546  O O      . LEU A 1 162 ? -1.665  -32.907 -20.943 1.00 11.36  ?  162  LEU A O      1 
ATOM   2547  C CB     . LEU A 1 162 ? 1.458   -31.926 -21.484 1.00 12.19  ?  162  LEU A CB     1 
ATOM   2548  C CG     . LEU A 1 162 ? 2.913   -32.373 -21.550 1.00 11.22  ?  162  LEU A CG     1 
ATOM   2549  C CD1    . LEU A 1 162 ? 3.836   -31.278 -20.962 1.00 12.92  ?  162  LEU A CD1    1 
ATOM   2550  C CD2    . LEU A 1 162 ? 3.113   -33.697 -20.811 1.00 12.85  ?  162  LEU A CD2    1 
ATOM   2551  H H      . LEU A 1 162 ? 1.276   -32.337 -23.859 1.00 14.40  ?  162  LEU A H      1 
ATOM   2552  H HA     . LEU A 1 162 ? 0.518   -33.725 -21.786 1.00 14.38  ?  162  LEU A HA     1 
ATOM   2553  H HB2    . LEU A 1 162 ? 1.410   -31.057 -21.911 1.00 14.63  ?  162  LEU A HB2    1 
ATOM   2554  H HB3    . LEU A 1 162 ? 1.229   -31.848 -20.545 1.00 14.63  ?  162  LEU A HB3    1 
ATOM   2555  H HG     . LEU A 1 162 ? 3.157   -32.514 -22.478 1.00 13.47  ?  162  LEU A HG     1 
ATOM   2556  H HD11   . LEU A 1 162 ? 4.753   -31.594 -20.981 1.00 15.50  ?  162  LEU A HD11   1 
ATOM   2557  H HD12   . LEU A 1 162 ? 3.752   -30.474 -21.498 1.00 15.50  ?  162  LEU A HD12   1 
ATOM   2558  H HD13   . LEU A 1 162 ? 3.567   -31.096 -20.048 1.00 15.50  ?  162  LEU A HD13   1 
ATOM   2559  H HD21   . LEU A 1 162 ? 4.053   -33.937 -20.843 1.00 15.42  ?  162  LEU A HD21   1 
ATOM   2560  H HD22   . LEU A 1 162 ? 2.830   -33.590 -19.889 1.00 15.42  ?  162  LEU A HD22   1 
ATOM   2561  H HD23   . LEU A 1 162 ? 2.581   -34.383 -21.243 1.00 15.42  ?  162  LEU A HD23   1 
ATOM   2562  N N      . THR A 1 163 ? -1.455  -31.308 -22.486 1.00 10.40  ?  163  THR A N      1 
ATOM   2563  C CA     . THR A 1 163 ? -2.840  -30.864 -22.359 1.00 11.17  ?  163  THR A CA     1 
ATOM   2564  C C      . THR A 1 163 ? -3.793  -32.033 -22.538 1.00 11.24  ?  163  THR A C      1 
ATOM   2565  O O      . THR A 1 163 ? -3.546  -32.949 -23.339 1.00 11.95  ?  163  THR A O      1 
ATOM   2566  C CB     . THR A 1 163 ? -3.049  -29.774 -23.419 1.00 11.98  ?  163  THR A CB     1 
ATOM   2567  O OG1    . THR A 1 163 ? -2.296  -28.618 -23.005 1.00 12.74  ?  163  THR A OG1    1 
ATOM   2568  C CG2    . THR A 1 163 ? -4.504  -29.407 -23.601 1.00 13.00  ?  163  THR A CG2    1 
ATOM   2569  H H      . THR A 1 163 ? -0.986  -30.832 -23.026 1.00 12.48  ?  163  THR A H      1 
ATOM   2570  H HA     . THR A 1 163 ? -3.033  -30.497 -21.482 1.00 13.41  ?  163  THR A HA     1 
ATOM   2571  H HB     . THR A 1 163 ? -2.750  -30.096 -24.284 1.00 14.38  ?  163  THR A HB     1 
ATOM   2572  H HG1    . THR A 1 163 ? -2.286  -28.046 -23.620 1.00 15.29  ?  163  THR A HG1    1 
ATOM   2573  H HG21   . THR A 1 163 ? -4.577  -28.577 -24.098 1.00 15.60  ?  163  THR A HG21   1 
ATOM   2574  H HG22   . THR A 1 163 ? -4.965  -30.108 -24.088 1.00 15.60  ?  163  THR A HG22   1 
ATOM   2575  H HG23   . THR A 1 163 ? -4.928  -29.294 -22.735 1.00 15.60  ?  163  THR A HG23   1 
ATOM   2576  N N      . GLY A 1 164 ? -4.861  -32.021 -21.740 1.00 12.40  ?  164  GLY A N      1 
ATOM   2577  C CA     . GLY A 1 164 ? -5.829  -33.088 -21.727 1.00 11.54  ?  164  GLY A CA     1 
ATOM   2578  C C      . GLY A 1 164 ? -7.208  -32.703 -22.211 1.00 13.76  ?  164  GLY A C      1 
ATOM   2579  O O      . GLY A 1 164 ? -8.217  -33.212 -21.713 1.00 14.44  ?  164  GLY A O      1 
ATOM   2580  H H      . GLY A 1 164 ? -5.043  -31.387 -21.189 1.00 14.87  ?  164  GLY A H      1 
ATOM   2581  H HA2    . GLY A 1 164 ? -5.508  -33.807 -22.294 1.00 13.84  ?  164  GLY A HA2    1 
ATOM   2582  H HA3    . GLY A 1 164 ? -5.916  -33.418 -20.819 1.00 13.84  ?  164  GLY A HA3    1 
ATOM   2583  N N      . LEU A 1 165 ? -7.260  -31.773 -23.158 1.00 13.94  ?  165  LEU A N      1 
ATOM   2584  C CA     . LEU A 1 165 ? -8.488  -31.286 -23.756 1.00 14.35  ?  165  LEU A CA     1 
ATOM   2585  C C      . LEU A 1 165 ? -8.487  -31.596 -25.243 1.00 12.17  ?  165  LEU A C      1 
ATOM   2586  O O      . LEU A 1 165 ? -7.480  -31.404 -25.936 1.00 12.80  ?  165  LEU A O      1 
ATOM   2587  C CB     . LEU A 1 165 ? -8.619  -29.789 -23.530 1.00 13.74  ?  165  LEU A CB     1 
ATOM   2588  C CG     . LEU A 1 165 ? -8.844  -29.386 -22.074 1.00 13.38  ?  165  LEU A CG     1 
ATOM   2589  C CD1    . LEU A 1 165 ? -8.606  -27.897 -21.861 1.00 15.05  ?  165  LEU A CD1    1 
ATOM   2590  C CD2    . LEU A 1 165 ? -10.246 -29.757 -21.592 1.00 13.16  ?  165  LEU A CD2    1 
ATOM   2591  H H      . LEU A 1 165 ? -6.559  -31.394 -23.482 1.00 16.72  ?  165  LEU A H      1 
ATOM   2592  H HA     . LEU A 1 165 ? -9.257  -31.729 -23.364 1.00 17.22  ?  165  LEU A HA     1 
ATOM   2593  H HB2    . LEU A 1 165 ? -7.803  -29.359 -23.831 1.00 16.48  ?  165  LEU A HB2    1 
ATOM   2594  H HB3    . LEU A 1 165 ? -9.374  -29.463 -24.044 1.00 16.48  ?  165  LEU A HB3    1 
ATOM   2595  H HG     . LEU A 1 165 ? -8.200  -29.879 -21.541 1.00 16.05  ?  165  LEU A HG     1 
ATOM   2596  H HD11   . LEU A 1 165 ? -8.711  -27.693 -20.918 1.00 18.05  ?  165  LEU A HD11   1 
ATOM   2597  H HD12   . LEU A 1 165 ? -7.707  -27.676 -22.149 1.00 18.05  ?  165  LEU A HD12   1 
ATOM   2598  H HD13   . LEU A 1 165 ? -9.254  -27.397 -22.382 1.00 18.05  ?  165  LEU A HD13   1 
ATOM   2599  H HD21   . LEU A 1 165 ? -10.343 -29.488 -20.665 1.00 15.79  ?  165  LEU A HD21   1 
ATOM   2600  H HD22   . LEU A 1 165 ? -10.901 -29.295 -22.139 1.00 15.79  ?  165  LEU A HD22   1 
ATOM   2601  H HD23   . LEU A 1 165 ? -10.365 -30.716 -21.673 1.00 15.79  ?  165  LEU A HD23   1 
ATOM   2602  N N      . LYS A 1 166 ? -9.627  -32.082 -25.727 1.00 13.33  ?  166  LYS A N      1 
ATOM   2603  C CA     . LYS A 1 166 ? -9.730  -32.627 -27.083 1.00 14.87  ?  166  LYS A CA     1 
ATOM   2604  C C      . LYS A 1 166 ? -9.332  -31.623 -28.159 1.00 14.36  ?  166  LYS A C      1 
ATOM   2605  O O      . LYS A 1 166 ? -8.774  -32.003 -29.197 1.00 15.43  ?  166  LYS A O      1 
ATOM   2606  C CB     . LYS A 1 166 ? -11.175 -33.077 -27.349 1.00 19.63  ?  166  LYS A CB     1 
ATOM   2607  C CG     . LYS A 1 166 ? -11.632 -34.246 -26.533 1.00 26.65  ?  166  LYS A CG     1 
ATOM   2608  C CD     . LYS A 1 166 ? -13.100 -34.601 -26.857 1.00 34.76  ?  166  LYS A CD     1 
ATOM   2609  C CE     . LYS A 1 166 ? -13.596 -35.801 -26.065 1.00 42.62  ?  166  LYS A CE     1 
ATOM   2610  N NZ     . LYS A 1 166 ? -15.034 -36.156 -26.344 1.00 47.05  ?  166  LYS A NZ     1 
ATOM   2611  H H      . LYS A 1 166 ? -10.367 -32.111 -25.291 1.00 15.99  ?  166  LYS A H      1 
ATOM   2612  H HA     . LYS A 1 166 ? -9.124  -33.383 -27.136 1.00 17.85  ?  166  LYS A HA     1 
ATOM   2613  H HB2    . LYS A 1 166 ? -11.769 -32.336 -27.152 1.00 23.56  ?  166  LYS A HB2    1 
ATOM   2614  H HB3    . LYS A 1 166 ? -11.253 -33.325 -28.283 1.00 23.56  ?  166  LYS A HB3    1 
ATOM   2615  H HG2    . LYS A 1 166 ? -11.077 -35.016 -26.732 1.00 31.98  ?  166  LYS A HG2    1 
ATOM   2616  H HG3    . LYS A 1 166 ? -11.569 -34.027 -25.590 1.00 31.98  ?  166  LYS A HG3    1 
ATOM   2617  H HD2    . LYS A 1 166 ? -13.665 -33.843 -26.640 1.00 41.71  ?  166  LYS A HD2    1 
ATOM   2618  H HD3    . LYS A 1 166 ? -13.175 -34.811 -27.801 1.00 41.71  ?  166  LYS A HD3    1 
ATOM   2619  H HE2    . LYS A 1 166 ? -13.052 -36.571 -26.291 1.00 51.14  ?  166  LYS A HE2    1 
ATOM   2620  H HE3    . LYS A 1 166 ? -13.518 -35.605 -25.118 1.00 51.14  ?  166  LYS A HE3    1 
ATOM   2621  H HZ1    . LYS A 1 166 ? -15.269 -36.871 -25.870 1.00 56.45  ?  166  LYS A HZ1    1 
ATOM   2622  H HZ2    . LYS A 1 166 ? -15.565 -35.477 -26.123 1.00 56.45  ?  166  LYS A HZ2    1 
ATOM   2623  H HZ3    . LYS A 1 166 ? -15.141 -36.337 -27.209 1.00 56.45  ?  166  LYS A HZ3    1 
ATOM   2624  N N      . ALA A 1 167 ? -9.653  -30.345 -27.963 1.00 13.11  ?  167  ALA A N      1 
ATOM   2625  C CA     . ALA A 1 167 ? -9.423  -29.365 -29.021 1.00 13.92  ?  167  ALA A CA     1 
ATOM   2626  C C      . ALA A 1 167 ? -7.960  -29.282 -29.411 1.00 14.55  ?  167  ALA A C      1 
ATOM   2627  O O      . ALA A 1 167 ? -7.630  -28.906 -30.550 1.00 15.05  ?  167  ALA A O      1 
ATOM   2628  C CB     . ALA A 1 167 ? -9.904  -27.980 -28.586 1.00 16.54  ?  167  ALA A CB     1 
ATOM   2629  H H      . ALA A 1 167 ? -9.998  -30.024 -27.243 1.00 15.73  ?  167  ALA A H      1 
ATOM   2630  H HA     . ALA A 1 167 ? -9.937  -29.642 -29.796 1.00 16.70  ?  167  ALA A HA     1 
ATOM   2631  H HB1    . ALA A 1 167 ? -9.703  -27.341 -29.287 1.00 19.84  ?  167  ALA A HB1    1 
ATOM   2632  H HB2    . ALA A 1 167 ? -10.861 -28.012 -28.432 1.00 19.84  ?  167  ALA A HB2    1 
ATOM   2633  H HB3    . ALA A 1 167 ? -9.446  -27.729 -27.769 1.00 19.84  ?  167  ALA A HB3    1 
ATOM   2634  N N      . PHE A 1 168 ? -7.062  -29.599 -28.477 1.00 12.29  ?  168  PHE A N      1 
ATOM   2635  C CA     . PHE A 1 168 ? -5.623  -29.500 -28.709 1.00 11.15  ?  168  PHE A CA     1 
ATOM   2636  C C      . PHE A 1 168 ? -5.020  -30.790 -29.226 1.00 12.48  ?  168  PHE A C      1 
ATOM   2637  O O      . PHE A 1 168 ? -3.818  -30.811 -29.515 1.00 14.82  ?  168  PHE A O      1 
ATOM   2638  C CB     . PHE A 1 168 ? -4.948  -28.966 -27.438 1.00 12.71  ?  168  PHE A CB     1 
ATOM   2639  C CG     . PHE A 1 168 ? -5.418  -27.580 -27.108 1.00 12.77  ?  168  PHE A CG     1 
ATOM   2640  C CD1    . PHE A 1 168 ? -6.524  -27.379 -26.296 1.00 13.39  ?  168  PHE A CD1    1 
ATOM   2641  C CD2    . PHE A 1 168 ? -4.824  -26.469 -27.676 1.00 13.83  ?  168  PHE A CD2    1 
ATOM   2642  C CE1    . PHE A 1 168 ? -6.994  -26.121 -26.057 1.00 14.60  ?  168  PHE A CE1    1 
ATOM   2643  C CE2    . PHE A 1 168 ? -5.282  -25.204 -27.421 1.00 16.21  ?  168  PHE A CE2    1 
ATOM   2644  C CZ     . PHE A 1 168 ? -6.366  -25.019 -26.632 1.00 16.63  ?  168  PHE A CZ     1 
ATOM   2645  H H      . PHE A 1 168 ? -7.267  -29.879 -27.690 1.00 14.75  ?  168  PHE A H      1 
ATOM   2646  H HA     . PHE A 1 168 ? -5.427  -28.848 -29.400 1.00 13.38  ?  168  PHE A HA     1 
ATOM   2647  H HB2    . PHE A 1 168 ? -5.163  -29.548 -26.692 1.00 15.24  ?  168  PHE A HB2    1 
ATOM   2648  H HB3    . PHE A 1 168 ? -3.988  -28.940 -27.572 1.00 15.24  ?  168  PHE A HB3    1 
ATOM   2649  H HD1    . PHE A 1 168 ? -6.950  -28.110 -25.910 1.00 16.06  ?  168  PHE A HD1    1 
ATOM   2650  H HD2    . PHE A 1 168 ? -4.097  -26.584 -28.244 1.00 16.59  ?  168  PHE A HD2    1 
ATOM   2651  H HE1    . PHE A 1 168 ? -7.735  -26.000 -25.508 1.00 17.52  ?  168  PHE A HE1    1 
ATOM   2652  H HE2    . PHE A 1 168 ? -4.847  -24.471 -27.792 1.00 19.45  ?  168  PHE A HE2    1 
ATOM   2653  H HZ     . PHE A 1 168 ? -6.689  -24.161 -26.474 1.00 19.96  ?  168  PHE A HZ     1 
ATOM   2654  N N      . HIS A 1 169 ? -5.842  -31.835 -29.386 1.00 11.84  ?  169  HIS A N      1 
ATOM   2655  C CA     . HIS A 1 169 ? -5.389  -33.129 -29.887 1.00 12.21  ?  169  HIS A CA     1 
ATOM   2656  C C      . HIS A 1 169 ? -6.057  -33.509 -31.197 1.00 13.27  ?  169  HIS A C      1 
ATOM   2657  O O      . HIS A 1 169 ? -5.378  -33.980 -32.111 1.00 14.46  ?  169  HIS A O      1 
ATOM   2658  C CB     . HIS A 1 169 ? -5.718  -34.245 -28.886 1.00 12.50  ?  169  HIS A CB     1 
ATOM   2659  C CG     . HIS A 1 169 ? -4.969  -34.160 -27.607 1.00 11.95  ?  169  HIS A CG     1 
ATOM   2660  N ND1    . HIS A 1 169 ? -5.266  -34.962 -26.523 1.00 14.44  ?  169  HIS A ND1    1 
ATOM   2661  C CD2    . HIS A 1 169 ? -3.954  -33.353 -27.219 1.00 11.65  ?  169  HIS A CD2    1 
ATOM   2662  C CE1    . HIS A 1 169 ? -4.446  -34.665 -25.531 1.00 14.45  ?  169  HIS A CE1    1 
ATOM   2663  N NE2    . HIS A 1 169 ? -3.642  -33.691 -25.927 1.00 13.34  ?  169  HIS A NE2    1 
ATOM   2664  H H      . HIS A 1 169 ? -6.683  -31.812 -29.206 1.00 14.20  ?  169  HIS A H      1 
ATOM   2665  H HA     . HIS A 1 169 ? -4.428  -33.068 -30.006 1.00 14.65  ?  169  HIS A HA     1 
ATOM   2666  H HB2    . HIS A 1 169 ? -6.664  -34.202 -28.676 1.00 15.00  ?  169  HIS A HB2    1 
ATOM   2667  H HB3    . HIS A 1 169 ? -5.507  -35.099 -29.294 1.00 15.00  ?  169  HIS A HB3    1 
ATOM   2668  H HD2    . HIS A 1 169 ? -3.545  -32.693 -27.731 1.00 13.98  ?  169  HIS A HD2    1 
ATOM   2669  H HE1    . HIS A 1 169 ? -4.436  -35.071 -24.695 1.00 17.34  ?  169  HIS A HE1    1 
ATOM   2670  H HE2    . HIS A 1 169 ? -3.024  -33.329 -25.451 1.00 16.01  ?  169  HIS A HE2    1 
ATOM   2671  N N      . ASP A 1 170 ? -7.380  -33.360 -31.287 1.00 13.63  ?  170  ASP A N      1 
ATOM   2672  C CA     . ASP A 1 170 ? -8.134  -33.830 -32.441 1.00 15.73  ?  170  ASP A CA     1 
ATOM   2673  C C      . ASP A 1 170 ? -7.623  -33.144 -33.704 1.00 14.60  ?  170  ASP A C      1 
ATOM   2674  O O      . ASP A 1 170 ? -7.387  -31.937 -33.709 1.00 15.83  ?  170  ASP A O      1 
ATOM   2675  C CB     . ASP A 1 170 ? -9.625  -33.556 -32.235 1.00 17.51  ?  170  ASP A CB     1 
ATOM   2676  C CG     . ASP A 1 170 ? -10.255 -34.450 -31.154 1.00 20.61  ?  170  ASP A CG     1 
ATOM   2677  O OD1    . ASP A 1 170 ? -9.572  -35.348 -30.633 1.00 22.08  ?  170  ASP A OD1    1 
ATOM   2678  O OD2    . ASP A 1 170 ? -11.448 -34.261 -30.839 1.00 23.77  -1 170  ASP A OD2    1 
ATOM   2679  H H      . ASP A 1 170 ? -7.869  -32.987 -30.686 1.00 16.35  ?  170  ASP A H      1 
ATOM   2680  H HA     . ASP A 1 170 ? -8.021  -34.788 -32.547 1.00 18.88  ?  170  ASP A HA     1 
ATOM   2681  H HB2    . ASP A 1 170 ? -9.741  -32.632 -31.965 1.00 21.00  ?  170  ASP A HB2    1 
ATOM   2682  H HB3    . ASP A 1 170 ? -10.093 -33.719 -33.069 1.00 21.00  ?  170  ASP A HB3    1 
ATOM   2683  N N      . HIS A 1 171 ? -7.427  -33.922 -34.761 1.00 14.21  ?  171  HIS A N      1 
ATOM   2684  C CA     . HIS A 1 171 ? -6.962  -33.461 -36.063 1.00 14.27  ?  171  HIS A CA     1 
ATOM   2685  C C      . HIS A 1 171 ? -5.463  -33.153 -36.054 1.00 13.54  ?  171  HIS A C      1 
ATOM   2686  O O      . HIS A 1 171 ? -4.909  -32.856 -37.112 1.00 14.14  ?  171  HIS A O      1 
ATOM   2687  C CB     . HIS A 1 171 ? -7.758  -32.244 -36.546 1.00 14.92  ?  171  HIS A CB     1 
ATOM   2688  C CG     . HIS A 1 171 ? -9.233  -32.391 -36.368 1.00 16.59  ?  171  HIS A CG     1 
ATOM   2689  N ND1    . HIS A 1 171 ? -9.967  -33.384 -36.983 1.00 19.01  ?  171  HIS A ND1    1 
ATOM   2690  C CD2    . HIS A 1 171 ? -10.105 -31.698 -35.599 1.00 18.99  ?  171  HIS A CD2    1 
ATOM   2691  C CE1    . HIS A 1 171 ? -11.237 -33.275 -36.619 1.00 20.99  ?  171  HIS A CE1    1 
ATOM   2692  N NE2    . HIS A 1 171 ? -11.342 -32.268 -35.768 1.00 20.65  ?  171  HIS A NE2    1 
ATOM   2693  H H      . HIS A 1 171 ? -7.566  -34.775 -34.733 1.00 17.05  ?  171  HIS A H      1 
ATOM   2694  H HA     . HIS A 1 171 ? -7.086  -34.164 -36.720 1.00 17.12  ?  171  HIS A HA     1 
ATOM   2695  H HB2    . HIS A 1 171 ? -7.473  -31.464 -36.044 1.00 17.90  ?  171  HIS A HB2    1 
ATOM   2696  H HB3    . HIS A 1 171 ? -7.584  -32.111 -37.491 1.00 17.90  ?  171  HIS A HB3    1 
ATOM   2697  H HD1    . HIS A 1 171 ? -9.650  -33.979 -37.517 1.00 22.81  ?  171  HIS A HD1    1 
ATOM   2698  H HD2    . HIS A 1 171 ? -9.903  -30.970 -35.057 1.00 22.78  ?  171  HIS A HD2    1 
ATOM   2699  H HE1    . HIS A 1 171 ? -11.935 -33.815 -36.911 1.00 25.18  ?  171  HIS A HE1    1 
ATOM   2700  N N      . PHE A 1 172 ? -4.778  -33.289 -34.920 1.00 13.12  ?  172  PHE A N      1 
ATOM   2701  C CA     . PHE A 1 172 ? -3.348  -33.024 -34.843 1.00 14.33  ?  172  PHE A CA     1 
ATOM   2702  C C      . PHE A 1 172 ? -2.517  -34.259 -34.521 1.00 14.33  ?  172  PHE A C      1 
ATOM   2703  O O      . PHE A 1 172 ? -1.300  -34.145 -34.360 1.00 13.04  ?  172  PHE A O      1 
ATOM   2704  C CB     . PHE A 1 172 ? -3.082  -31.964 -33.761 1.00 13.96  ?  172  PHE A CB     1 
ATOM   2705  C CG     . PHE A 1 172 ? -3.762  -30.645 -34.007 1.00 11.64  ?  172  PHE A CG     1 
ATOM   2706  C CD1    . PHE A 1 172 ? -3.509  -29.912 -35.143 1.00 12.20  ?  172  PHE A CD1    1 
ATOM   2707  C CD2    . PHE A 1 172 ? -4.673  -30.138 -33.078 1.00 13.12  ?  172  PHE A CD2    1 
ATOM   2708  C CE1    . PHE A 1 172 ? -4.136  -28.683 -35.349 1.00 12.34  ?  172  PHE A CE1    1 
ATOM   2709  C CE2    . PHE A 1 172 ? -5.315  -28.960 -33.301 1.00 13.62  ?  172  PHE A CE2    1 
ATOM   2710  C CZ     . PHE A 1 172 ? -5.027  -28.213 -34.425 1.00 12.45  ?  172  PHE A CZ     1 
ATOM   2711  H H      . PHE A 1 172 ? -5.127  -33.538 -34.174 1.00 15.74  ?  172  PHE A H      1 
ATOM   2712  H HA     . PHE A 1 172 ? -3.057  -32.685 -35.705 1.00 17.19  ?  172  PHE A HA     1 
ATOM   2713  H HB2    . PHE A 1 172 ? -3.399  -32.305 -32.910 1.00 16.75  ?  172  PHE A HB2    1 
ATOM   2714  H HB3    . PHE A 1 172 ? -2.127  -31.799 -33.717 1.00 16.75  ?  172  PHE A HB3    1 
ATOM   2715  H HD1    . PHE A 1 172 ? -2.914  -30.239 -35.779 1.00 14.63  ?  172  PHE A HD1    1 
ATOM   2716  H HD2    . PHE A 1 172 ? -4.843  -30.611 -32.296 1.00 15.74  ?  172  PHE A HD2    1 
ATOM   2717  H HE1    . PHE A 1 172 ? -3.949  -28.186 -36.112 1.00 14.80  ?  172  PHE A HE1    1 
ATOM   2718  H HE2    . PHE A 1 172 ? -5.951  -28.656 -32.693 1.00 16.34  ?  172  PHE A HE2    1 
ATOM   2719  H HZ     . PHE A 1 172 ? -5.440  -27.390 -34.554 1.00 14.94  ?  172  PHE A HZ     1 
ATOM   2720  N N      . ASP A 1 173 ? -3.135  -35.431 -34.400 1.00 13.40  ?  173  ASP A N      1 
ATOM   2721  C CA     . ASP A 1 173 ? -2.426  -36.675 -34.112 1.00 13.79  ?  173  ASP A CA     1 
ATOM   2722  C C      . ASP A 1 173 ? -1.703  -36.651 -32.761 1.00 14.90  ?  173  ASP A C      1 
ATOM   2723  O O      . ASP A 1 173 ? -0.660  -37.283 -32.601 1.00 18.63  ?  173  ASP A O      1 
ATOM   2724  C CB     . ASP A 1 173 ? -1.431  -37.051 -35.217 1.00 13.67  ?  173  ASP A CB     1 
ATOM   2725  C CG     . ASP A 1 173 ? -2.060  -37.196 -36.571 1.00 15.53  ?  173  ASP A CG     1 
ATOM   2726  O OD1    . ASP A 1 173 ? -3.310  -37.269 -36.689 1.00 15.89  ?  173  ASP A OD1    1 
ATOM   2727  O OD2    . ASP A 1 173 ? -1.279  -37.241 -37.529 1.00 18.63  -1 173  ASP A OD2    1 
ATOM   2728  H H      . ASP A 1 173 ? -3.985  -35.533 -34.482 1.00 16.08  ?  173  ASP A H      1 
ATOM   2729  H HA     . ASP A 1 173 ? -3.106  -37.365 -34.069 1.00 16.54  ?  173  ASP A HA     1 
ATOM   2730  H HB2    . ASP A 1 173 ? -0.754  -36.359 -35.277 1.00 16.41  ?  173  ASP A HB2    1 
ATOM   2731  H HB3    . ASP A 1 173 ? -1.018  -37.899 -34.990 1.00 16.41  ?  173  ASP A HB3    1 
ATOM   2732  N N      . LEU A 1 174 ? -2.272  -35.959 -31.766 1.00 13.12  ?  174  LEU A N      1 
ATOM   2733  C CA     . LEU A 1 174 ? -1.688  -35.865 -30.435 1.00 12.62  ?  174  LEU A CA     1 
ATOM   2734  C C      . LEU A 1 174 ? -2.544  -36.679 -29.462 1.00 12.55  ?  174  LEU A C      1 
ATOM   2735  O O      . LEU A 1 174 ? -3.733  -36.890 -29.712 1.00 14.90  ?  174  LEU A O      1 
ATOM   2736  C CB     . LEU A 1 174 ? -1.635  -34.408 -29.971 1.00 12.42  ?  174  LEU A CB     1 
ATOM   2737  C CG     . LEU A 1 174 ? -0.838  -33.479 -30.913 1.00 13.61  ?  174  LEU A CG     1 
ATOM   2738  C CD1    . LEU A 1 174 ? -0.812  -32.028 -30.412 1.00 14.30  ?  174  LEU A CD1    1 
ATOM   2739  C CD2    . LEU A 1 174 ? 0.609   -34.002 -31.147 1.00 15.12  ?  174  LEU A CD2    1 
ATOM   2740  H H      . LEU A 1 174 ? -3.012  -35.529 -31.845 1.00 15.75  ?  174  LEU A H      1 
ATOM   2741  H HA     . LEU A 1 174 ? -0.781  -36.208 -30.429 1.00 15.14  ?  174  LEU A HA     1 
ATOM   2742  H HB2    . LEU A 1 174 ? -2.541  -34.067 -29.915 1.00 14.90  ?  174  LEU A HB2    1 
ATOM   2743  H HB3    . LEU A 1 174 ? -1.214  -34.376 -29.098 1.00 14.90  ?  174  LEU A HB3    1 
ATOM   2744  H HG     . LEU A 1 174 ? -1.298  -33.480 -31.768 1.00 16.33  ?  174  LEU A HG     1 
ATOM   2745  H HD11   . LEU A 1 174 ? -0.320  -31.484 -31.046 1.00 17.16  ?  174  LEU A HD11   1 
ATOM   2746  H HD12   . LEU A 1 174 ? -1.722  -31.704 -30.334 1.00 17.16  ?  174  LEU A HD12   1 
ATOM   2747  H HD13   . LEU A 1 174 ? -0.376  -32.002 -29.545 1.00 17.16  ?  174  LEU A HD13   1 
ATOM   2748  H HD21   . LEU A 1 174 ? 1.091   -33.364 -31.696 1.00 18.14  ?  174  LEU A HD21   1 
ATOM   2749  H HD22   . LEU A 1 174 ? 1.051   -34.101 -30.289 1.00 18.14  ?  174  LEU A HD22   1 
ATOM   2750  H HD23   . LEU A 1 174 ? 0.565   -34.860 -31.598 1.00 18.14  ?  174  LEU A HD23   1 
ATOM   2751  N N      . PRO A 1 175 ? -1.965  -37.173 -28.351 1.00 13.16  ?  175  PRO A N      1 
ATOM   2752  C CA     . PRO A 1 175 ? -0.591  -36.935 -27.925 1.00 12.53  ?  175  PRO A CA     1 
ATOM   2753  C C      . PRO A 1 175 ? 0.467   -37.762 -28.628 1.00 13.21  ?  175  PRO A C      1 
ATOM   2754  O O      . PRO A 1 175 ? 0.193   -38.855 -29.151 1.00 15.17  ?  175  PRO A O      1 
ATOM   2755  C CB     . PRO A 1 175 ? -0.612  -37.365 -26.451 1.00 14.30  ?  175  PRO A CB     1 
ATOM   2756  C CG     . PRO A 1 175 ? -1.623  -38.440 -26.418 1.00 14.62  ?  175  PRO A CG     1 
ATOM   2757  C CD     . PRO A 1 175 ? -2.702  -37.968 -27.348 1.00 14.26  ?  175  PRO A CD     1 
ATOM   2758  H HA     . PRO A 1 175 ? -0.397  -35.993 -28.046 1.00 15.03  ?  175  PRO A HA     1 
ATOM   2759  H HB2    . PRO A 1 175 ? 0.261   -37.693 -26.185 1.00 17.15  ?  175  PRO A HB2    1 
ATOM   2760  H HB3    . PRO A 1 175 ? -0.872  -36.619 -25.888 1.00 17.15  ?  175  PRO A HB3    1 
ATOM   2761  H HG2    . PRO A 1 175 ? -1.233  -39.272 -26.728 1.00 17.54  ?  175  PRO A HG2    1 
ATOM   2762  H HG3    . PRO A 1 175 ? -1.963  -38.549 -25.516 1.00 17.54  ?  175  PRO A HG3    1 
ATOM   2763  H HD2    . PRO A 1 175 ? -3.150  -38.720 -27.766 1.00 17.11  ?  175  PRO A HD2    1 
ATOM   2764  H HD3    . PRO A 1 175 ? -3.347  -37.417 -26.878 1.00 17.11  ?  175  PRO A HD3    1 
ATOM   2765  N N      . ILE A 1 176 ? 1.687   -37.218 -28.640 1.00 13.61  ?  176  ILE A N      1 
ATOM   2766  C CA     . ILE A 1 176 ? 2.853   -37.972 -29.073 1.00 13.76  ?  176  ILE A CA     1 
ATOM   2767  C C      . ILE A 1 176 ? 3.114   -39.140 -28.125 1.00 13.88  ?  176  ILE A C      1 
ATOM   2768  O O      . ILE A 1 176 ? 2.555   -39.223 -27.024 1.00 13.05  ?  176  ILE A O      1 
ATOM   2769  C CB     . ILE A 1 176 ? 4.104   -37.082 -29.208 1.00 12.84  ?  176  ILE A CB     1 
ATOM   2770  C CG1    . ILE A 1 176 ? 4.527   -36.535 -27.842 1.00 14.11  ?  176  ILE A CG1    1 
ATOM   2771  C CG2    . ILE A 1 176 ? 3.861   -35.930 -30.205 1.00 15.31  ?  176  ILE A CG2    1 
ATOM   2772  C CD1    . ILE A 1 176 ? 5.821   -35.755 -27.893 1.00 15.90  ?  176  ILE A CD1    1 
ATOM   2773  H H      . ILE A 1 176 ? 1.860   -36.410 -28.399 1.00 16.32  ?  176  ILE A H      1 
ATOM   2774  H HA     . ILE A 1 176 ? 2.651   -38.340 -29.948 1.00 16.51  ?  176  ILE A HA     1 
ATOM   2775  H HB     . ILE A 1 176 ? 4.824   -37.633 -29.553 1.00 15.41  ?  176  ILE A HB     1 
ATOM   2776  H HG12   . ILE A 1 176 ? 3.833   -35.943 -27.512 1.00 16.93  ?  176  ILE A HG12   1 
ATOM   2777  H HG13   . ILE A 1 176 ? 4.649   -37.277 -27.230 1.00 16.93  ?  176  ILE A HG13   1 
ATOM   2778  H HG21   . ILE A 1 176 ? 4.703   -35.483 -30.382 1.00 18.37  ?  176  ILE A HG21   1 
ATOM   2779  H HG22   . ILE A 1 176 ? 3.502   -36.296 -31.029 1.00 18.37  ?  176  ILE A HG22   1 
ATOM   2780  H HG23   . ILE A 1 176 ? 3.229   -35.305 -29.817 1.00 18.37  ?  176  ILE A HG23   1 
ATOM   2781  H HD11   . ILE A 1 176 ? 6.115   -35.572 -26.987 1.00 19.07  ?  176  ILE A HD11   1 
ATOM   2782  H HD12   . ILE A 1 176 ? 6.489   -36.282 -28.357 1.00 19.07  ?  176  ILE A HD12   1 
ATOM   2783  H HD13   . ILE A 1 176 ? 5.669   -34.922 -28.366 1.00 19.07  ?  176  ILE A HD13   1 
ATOM   2784  N N      . GLU A 1 177 ? 3.856   -39.997 -28.451 1.00 14.82  ?  177  GLU A N      1 
ATOM   2785  C CA     . GLU A 1 177 ? 4.362   -41.111 -27.670 1.00 16.68  ?  177  GLU A CA     1 
ATOM   2786  C C      . GLU A 1 177 ? 5.184   -40.606 -26.486 1.00 14.98  ?  177  GLU A C      1 
ATOM   2787  O O      . GLU A 1 177 ? 5.911   -39.612 -26.582 1.00 16.30  ?  177  GLU A O      1 
ATOM   2788  C CB     . GLU A 1 177 ? 5.226   -42.023 -28.562 1.00 24.62  ?  177  GLU A CB     1 
ATOM   2789  C CG     . GLU A 1 177 ? 4.413   -42.726 -29.631 1.00 38.23  ?  177  GLU A CG     1 
ATOM   2790  C CD     . GLU A 1 177 ? 5.259   -43.574 -30.566 1.00 48.96  ?  177  GLU A CD     1 
ATOM   2791  O OE1    . GLU A 1 177 ? 6.509   -43.472 -30.505 1.00 53.12  ?  177  GLU A OE1    1 
ATOM   2792  O OE2    . GLU A 1 177 ? 4.655   -44.338 -31.359 1.00 53.38  -1 177  GLU A OE2    1 
ATOM   2793  H H      . GLU A 1 177 ? 4.157   -39.970 -29.257 1.00 17.78  ?  177  GLU A H      1 
ATOM   2794  H HA     . GLU A 1 177 ? 3.618   -41.628 -27.326 1.00 20.01  ?  177  GLU A HA     1 
ATOM   2795  H HB2    . GLU A 1 177 ? 5.904   -41.488 -29.001 1.00 29.54  ?  177  GLU A HB2    1 
ATOM   2796  H HB3    . GLU A 1 177 ? 5.646   -42.701 -28.008 1.00 29.54  ?  177  GLU A HB3    1 
ATOM   2797  H HG2    . GLU A 1 177 ? 3.767   -43.309 -29.202 1.00 45.87  ?  177  GLU A HG2    1 
ATOM   2798  H HG3    . GLU A 1 177 ? 3.955   -42.060 -30.165 1.00 45.87  ?  177  GLU A HG3    1 
ATOM   2799  N N      . GLY A 1 178 ? 4.636   -41.546 -25.386 1.00 15.26  ?  178  GLY A N      1 
ATOM   2800  C CA     . GLY A 1 178 ? 5.257   -41.354 -24.086 1.00 15.46  ?  178  GLY A CA     1 
ATOM   2801  C C      . GLY A 1 178 ? 4.516   -40.451 -23.133 1.00 14.49  ?  178  GLY A C      1 
ATOM   2802  O O      . GLY A 1 178 ? 4.983   -40.248 -22.006 1.00 15.53  ?  178  GLY A O      1 
ATOM   2803  H H      . GLY A 1 178 ? 4.053   -42.178 -25.407 1.00 18.31  ?  178  GLY A H      1 
ATOM   2804  H HA2    . GLY A 1 178 ? 5.346   -42.220 -23.658 1.00 18.54  ?  178  GLY A HA2    1 
ATOM   2805  H HA3    . GLY A 1 178 ? 6.140   -40.976 -24.220 1.00 18.54  ?  178  GLY A HA3    1 
ATOM   2806  N N      . ILE A 1 179 ? 3.386   -39.895 -23.549 1.00 14.39  ?  179  ILE A N      1 
ATOM   2807  C CA     . ILE A 1 179 ? 2.592   -38.982 -22.738 1.00 14.17  ?  179  ILE A CA     1 
ATOM   2808  C C      . ILE A 1 179 ? 1.248   -39.651 -22.494 1.00 13.44  ?  179  ILE A C      1 
ATOM   2809  O O      . ILE A 1 179 ? 0.584   -40.102 -23.443 1.00 15.40  ?  179  ILE A O      1 
ATOM   2810  C CB     . ILE A 1 179 ? 2.466   -37.587 -23.392 1.00 13.17  ?  179  ILE A CB     1 
ATOM   2811  C CG1    . ILE A 1 179 ? 3.844   -36.895 -23.323 1.00 15.05  ?  179  ILE A CG1    1 
ATOM   2812  C CG2    . ILE A 1 179 ? 1.406   -36.777 -22.689 1.00 15.51  ?  179  ILE A CG2    1 
ATOM   2813  C CD1    . ILE A 1 179 ? 3.953   -35.573 -24.043 1.00 16.33  ?  179  ILE A CD1    1 
ATOM   2814  H H      . ILE A 1 179 ? 3.048   -40.038 -24.327 1.00 17.26  ?  179  ILE A H      1 
ATOM   2815  H HA     . ILE A 1 179 ? 3.010   -38.839 -21.875 1.00 17.00  ?  179  ILE A HA     1 
ATOM   2816  H HB     . ILE A 1 179 ? 2.197   -37.672 -24.320 1.00 15.80  ?  179  ILE A HB     1 
ATOM   2817  H HG12   . ILE A 1 179 ? 4.056   -36.733 -22.390 1.00 18.05  ?  179  ILE A HG12   1 
ATOM   2818  H HG13   . ILE A 1 179 ? 4.502   -37.491 -23.714 1.00 18.05  ?  179  ILE A HG13   1 
ATOM   2819  H HG21   . ILE A 1 179 ? 1.434   -35.866 -23.020 1.00 18.61  ?  179  ILE A HG21   1 
ATOM   2820  H HG22   . ILE A 1 179 ? 0.538   -37.169 -22.870 1.00 18.61  ?  179  ILE A HG22   1 
ATOM   2821  H HG23   . ILE A 1 179 ? 1.582   -36.788 -21.735 1.00 18.61  ?  179  ILE A HG23   1 
ATOM   2822  H HD11   . ILE A 1 179 ? 4.880   -35.288 -24.041 1.00 19.59  ?  179  ILE A HD11   1 
ATOM   2823  H HD12   . ILE A 1 179 ? 3.643   -35.684 -24.956 1.00 19.59  ?  179  ILE A HD12   1 
ATOM   2824  H HD13   . ILE A 1 179 ? 3.404   -34.917 -23.585 1.00 19.59  ?  179  ILE A HD13   1 
ATOM   2825  N N      . LEU A 1 180 ? 0.869   -39.750 -21.221 1.00 13.13  ?  180  LEU A N      1 
ATOM   2826  C CA     . LEU A 1 180 ? -0.318  -40.470 -20.788 1.00 12.10  ?  180  LEU A CA     1 
ATOM   2827  C C      . LEU A 1 180 ? -1.207  -39.511 -20.010 1.00 13.07  ?  180  LEU A C      1 
ATOM   2828  O O      . LEU A 1 180 ? -0.735  -38.490 -19.508 1.00 13.19  ?  180  LEU A O      1 
ATOM   2829  C CB     . LEU A 1 180 ? 0.058   -41.642 -19.871 1.00 14.66  ?  180  LEU A CB     1 
ATOM   2830  C CG     . LEU A 1 180 ? 1.145   -42.564 -20.406 1.00 20.21  ?  180  LEU A CG     1 
ATOM   2831  C CD1    . LEU A 1 180 ? 1.634   -43.506 -19.355 1.00 23.19  ?  180  LEU A CD1    1 
ATOM   2832  C CD2    . LEU A 1 180 ? 0.591   -43.301 -21.595 1.00 25.19  ?  180  LEU A CD2    1 
ATOM   2833  H H      . LEU A 1 180 ? 1.303   -39.393 -20.570 1.00 15.75  ?  180  LEU A H      1 
ATOM   2834  H HA     . LEU A 1 180 ? -0.798  -40.815 -21.557 1.00 14.51  ?  180  LEU A HA     1 
ATOM   2835  H HB2    . LEU A 1 180 ? 0.372   -41.281 -19.028 1.00 17.58  ?  180  LEU A HB2    1 
ATOM   2836  H HB3    . LEU A 1 180 ? -0.735  -42.182 -19.726 1.00 17.58  ?  180  LEU A HB3    1 
ATOM   2837  H HG     . LEU A 1 180 ? 1.919   -42.046 -20.678 1.00 24.25  ?  180  LEU A HG     1 
ATOM   2838  H HD11   . LEU A 1 180 ? 2.313   -44.082 -19.739 1.00 27.82  ?  180  LEU A HD11   1 
ATOM   2839  H HD12   . LEU A 1 180 ? 2.011   -42.994 -18.622 1.00 27.82  ?  180  LEU A HD12   1 
ATOM   2840  H HD13   . LEU A 1 180 ? 0.889   -44.039 -19.037 1.00 27.82  ?  180  LEU A HD13   1 
ATOM   2841  H HD21   . LEU A 1 180 ? 1.253   -43.936 -21.909 1.00 30.22  ?  180  LEU A HD21   1 
ATOM   2842  H HD22   . LEU A 1 180 ? -0.216  -43.768 -21.329 1.00 30.22  ?  180  LEU A HD22   1 
ATOM   2843  H HD23   . LEU A 1 180 ? 0.388   -42.662 -22.296 1.00 30.22  ?  180  LEU A HD23   1 
ATOM   2844  N N      . HIS A 1 181 ? -2.488  -39.859 -19.869 1.00 13.53  ?  181  HIS A N      1 
ATOM   2845  C CA     . HIS A 1 181 ? -3.451  -39.019 -19.152 1.00 11.85  ?  181  HIS A CA     1 
ATOM   2846  C C      . HIS A 1 181 ? -4.243  -39.840 -18.152 1.00 12.98  ?  181  HIS A C      1 
ATOM   2847  O O      . HIS A 1 181 ? -4.976  -40.766 -18.538 1.00 14.63  ?  181  HIS A O      1 
ATOM   2848  C CB     . HIS A 1 181 ? -4.407  -38.323 -20.132 1.00 10.79  ?  181  HIS A CB     1 
ATOM   2849  C CG     . HIS A 1 181 ? -3.718  -37.354 -21.036 1.00 11.65  ?  181  HIS A CG     1 
ATOM   2850  N ND1    . HIS A 1 181 ? -3.149  -37.743 -22.230 1.00 14.41  ?  181  HIS A ND1    1 
ATOM   2851  C CD2    . HIS A 1 181 ? -3.465  -36.034 -20.902 1.00 12.62  ?  181  HIS A CD2    1 
ATOM   2852  C CE1    . HIS A 1 181 ? -2.563  -36.701 -22.788 1.00 13.85  ?  181  HIS A CE1    1 
ATOM   2853  N NE2    . HIS A 1 181 ? -2.745  -35.651 -22.004 1.00 12.76  ?  181  HIS A NE2    1 
ATOM   2854  H H      . HIS A 1 181 ? -2.825  -40.584 -20.185 1.00 16.23  ?  181  HIS A H      1 
ATOM   2855  H HA     . HIS A 1 181 ? -2.954  -38.355 -18.650 1.00 14.22  ?  181  HIS A HA     1 
ATOM   2856  H HB2    . HIS A 1 181 ? -4.835  -38.995 -20.685 1.00 12.95  ?  181  HIS A HB2    1 
ATOM   2857  H HB3    . HIS A 1 181 ? -5.076  -37.836 -19.626 1.00 12.95  ?  181  HIS A HB3    1 
ATOM   2858  H HD2    . HIS A 1 181 ? -3.729  -35.489 -20.197 1.00 15.14  ?  181  HIS A HD2    1 
ATOM   2859  H HE1    . HIS A 1 181 ? -2.100  -36.703 -23.595 1.00 16.62  ?  181  HIS A HE1    1 
ATOM   2860  H HE2    . HIS A 1 181 ? -2.457  -34.855 -22.161 1.00 15.31  ?  181  HIS A HE2    1 
ATOM   2861  N N      . THR A 1 182 ? -4.103  -39.477 -16.868 1.00 13.38  ?  182  THR A N      1 
ATOM   2862  C CA     . THR A 1 182 ? -4.869  -40.099 -15.794 1.00 12.34  ?  182  THR A CA     1 
ATOM   2863  C C      . THR A 1 182 ? -6.132  -39.272 -15.525 1.00 12.24  ?  182  THR A C      1 
ATOM   2864  O O      . THR A 1 182 ? -6.509  -38.410 -16.321 1.00 13.15  ?  182  THR A O      1 
ATOM   2865  C CB     . THR A 1 182 ? -3.955  -40.343 -14.580 1.00 11.79  ?  182  THR A CB     1 
ATOM   2866  O OG1    . THR A 1 182 ? -4.649  -41.156 -13.620 1.00 14.02  ?  182  THR A OG1    1 
ATOM   2867  C CG2    . THR A 1 182 ? -3.493  -39.050 -13.959 1.00 12.85  ?  182  THR A CG2    1 
ATOM   2868  H H      . THR A 1 182 ? -3.562  -38.866 -16.598 1.00 16.06  ?  182  THR A H      1 
ATOM   2869  H HA     . THR A 1 182 ? -5.185  -40.974 -16.069 1.00 14.80  ?  182  THR A HA     1 
ATOM   2870  H HB     . THR A 1 182 ? -3.153  -40.809 -14.867 1.00 14.15  ?  182  THR A HB     1 
ATOM   2871  H HG1    . THR A 1 182 ? -4.713  -41.944 -13.903 1.00 16.82  ?  182  THR A HG1    1 
ATOM   2872  H HG21   . THR A 1 182 ? -2.843  -39.230 -13.262 1.00 15.42  ?  182  THR A HG21   1 
ATOM   2873  H HG22   . THR A 1 182 ? -3.084  -38.486 -14.634 1.00 15.42  ?  182  THR A HG22   1 
ATOM   2874  H HG23   . THR A 1 182 ? -4.248  -38.580 -13.572 1.00 15.42  ?  182  THR A HG23   1 
ATOM   2875  N N      . GLU A 1 183 ? -6.816  -39.551 -14.414 1.00 13.08  ?  183  GLU A N      1 
ATOM   2876  C CA     . GLU A 1 183 ? -8.161  -39.040 -14.177 1.00 14.61  ?  183  GLU A CA     1 
ATOM   2877  C C      . GLU A 1 183 ? -8.201  -37.519 -14.066 1.00 13.55  ?  183  GLU A C      1 
ATOM   2878  O O      . GLU A 1 183 ? -7.322  -36.898 -13.466 1.00 14.92  ?  183  GLU A O      1 
ATOM   2879  C CB     . GLU A 1 183 ? -8.699  -39.600 -12.846 1.00 15.76  ?  183  GLU A CB     1 
ATOM   2880  C CG     . GLU A 1 183 ? -8.738  -41.089 -12.735 1.00 18.21  ?  183  GLU A CG     1 
ATOM   2881  C CD     . GLU A 1 183 ? -9.549  -41.709 -13.832 1.00 26.36  ?  183  GLU A CD     1 
ATOM   2882  O OE1    . GLU A 1 183 ? -10.768 -41.573 -13.779 1.00 28.25  ?  183  GLU A OE1    1 
ATOM   2883  O OE2    . GLU A 1 183 ? -8.956  -42.302 -14.758 1.00 33.55  -1 183  GLU A OE2    1 
ATOM   2884  H H      . GLU A 1 183 ? -6.520  -40.041 -13.773 1.00 15.69  ?  183  GLU A H      1 
ATOM   2885  H HA     . GLU A 1 183 ? -8.710  -39.315 -14.929 1.00 17.52  ?  183  GLU A HA     1 
ATOM   2886  H HB2    . GLU A 1 183 ? -8.133  -39.273 -12.129 1.00 18.91  ?  183  GLU A HB2    1 
ATOM   2887  H HB3    . GLU A 1 183 ? -9.606  -39.279 -12.726 1.00 18.91  ?  183  GLU A HB3    1 
ATOM   2888  H HG2    . GLU A 1 183 ? -7.834  -41.438 -12.791 1.00 21.85  ?  183  GLU A HG2    1 
ATOM   2889  H HG3    . GLU A 1 183 ? -9.137  -41.336 -11.886 1.00 21.85  ?  183  GLU A HG3    1 
ATOM   2890  N N      . ALA A 1 184 ? -9.293  -36.925 -14.562 1.00 11.56  ?  184  ALA A N      1 
ATOM   2891  C CA     . ALA A 1 184 ? -9.525  -35.508 -14.331 1.00 11.99  ?  184  ALA A CA     1 
ATOM   2892  C C      . ALA A 1 184 ? -9.754  -35.272 -12.845 1.00 12.34  ?  184  ALA A C      1 
ATOM   2893  O O      . ALA A 1 184 ? -10.553 -35.993 -12.225 1.00 14.10  ?  184  ALA A O      1 
ATOM   2894  C CB     . ALA A 1 184 ? -10.733 -35.043 -15.109 1.00 14.48  ?  184  ALA A CB     1 
ATOM   2895  H H      . ALA A 1 184 ? -9.902  -37.317 -15.026 1.00 13.87  ?  184  ALA A H      1 
ATOM   2896  H HA     . ALA A 1 184 ? -8.754  -34.998 -14.624 1.00 14.38  ?  184  ALA A HA     1 
ATOM   2897  H HB1    . ALA A 1 184 ? -10.873 -34.098 -14.939 1.00 17.38  ?  184  ALA A HB1    1 
ATOM   2898  H HB2    . ALA A 1 184 ? -10.574 -35.188 -16.055 1.00 17.38  ?  184  ALA A HB2    1 
ATOM   2899  H HB3    . ALA A 1 184 ? -11.508 -35.550 -14.822 1.00 17.38  ?  184  ALA A HB3    1 
ATOM   2900  N N      . PRO A 1 185 ? -9.108  -34.273 -12.247 1.00 13.11  ?  185  PRO A N      1 
ATOM   2901  C CA     . PRO A 1 185 ? -9.299  -33.982 -10.814 1.00 12.72  ?  185  PRO A CA     1 
ATOM   2902  C C      . PRO A 1 185 ? -10.544 -33.131 -10.600 1.00 14.49  ?  185  PRO A C      1 
ATOM   2903  O O      . PRO A 1 185 ? -10.472 -31.985 -10.170 1.00 14.52  ?  185  PRO A O      1 
ATOM   2904  C CB     . PRO A 1 185 ? -8.004  -33.240 -10.465 1.00 14.52  ?  185  PRO A CB     1 
ATOM   2905  C CG     . PRO A 1 185 ? -7.719  -32.429 -11.729 1.00 13.37  ?  185  PRO A CG     1 
ATOM   2906  C CD     . PRO A 1 185 ? -8.052  -33.425 -12.841 1.00 12.50  ?  185  PRO A CD     1 
ATOM   2907  H HA     . PRO A 1 185 ? -9.351  -34.794 -10.285 1.00 15.27  ?  185  PRO A HA     1 
ATOM   2908  H HB2    . PRO A 1 185 ? -8.142  -32.664 -9.697  1.00 17.42  ?  185  PRO A HB2    1 
ATOM   2909  H HB3    . PRO A 1 185 ? -7.292  -33.872 -10.282 1.00 17.42  ?  185  PRO A HB3    1 
ATOM   2910  H HG2    . PRO A 1 185 ? -8.292  -31.647 -11.768 1.00 16.04  ?  185  PRO A HG2    1 
ATOM   2911  H HG3    . PRO A 1 185 ? -6.788  -32.160 -11.758 1.00 16.04  ?  185  PRO A HG3    1 
ATOM   2912  H HD2    . PRO A 1 185 ? -8.383  -32.963 -13.628 1.00 14.99  ?  185  PRO A HD2    1 
ATOM   2913  H HD3    . PRO A 1 185 ? -7.273  -33.955 -13.072 1.00 14.99  ?  185  PRO A HD3    1 
ATOM   2914  N N      . TYR A 1 186 ? -11.707 -33.712 -10.918 1.00 13.28  ?  186  TYR A N      1 
ATOM   2915  C CA     . TYR A 1 186 ? -12.932 -32.956 -11.224 1.00 12.91  ?  186  TYR A CA     1 
ATOM   2916  C C      . TYR A 1 186 ? -14.118 -33.700 -10.617 1.00 12.77  ?  186  TYR A C      1 
ATOM   2917  O O      . TYR A 1 186 ? -14.822 -34.476 -11.273 1.00 14.18  ?  186  TYR A O      1 
ATOM   2918  C CB     . TYR A 1 186 ? -13.016 -32.797 -12.730 1.00 13.42  ?  186  TYR A CB     1 
ATOM   2919  C CG     . TYR A 1 186 ? -13.866 -31.711 -13.310 1.00 14.50  ?  186  TYR A CG     1 
ATOM   2920  C CD1    . TYR A 1 186 ? -15.072 -31.324 -12.734 1.00 15.11  ?  186  TYR A CD1    1 
ATOM   2921  C CD2    . TYR A 1 186 ? -13.473 -31.082 -14.484 1.00 14.16  ?  186  TYR A CD2    1 
ATOM   2922  C CE1    . TYR A 1 186 ? -15.855 -30.351 -13.333 1.00 14.57  ?  186  TYR A CE1    1 
ATOM   2923  C CE2    . TYR A 1 186 ? -14.242 -30.104 -15.070 1.00 14.69  ?  186  TYR A CE2    1 
ATOM   2924  C CZ     . TYR A 1 186 ? -15.438 -29.743 -14.503 1.00 14.88  ?  186  TYR A CZ     1 
ATOM   2925  O OH     . TYR A 1 186 ? -16.185 -28.779 -15.140 1.00 16.99  ?  186  TYR A OH     1 
ATOM   2926  H H      . TYR A 1 186 ? -11.814 -34.564 -10.964 1.00 15.93  ?  186  TYR A H      1 
ATOM   2927  H HA     . TYR A 1 186 ? -12.932 -32.083 -10.802 1.00 15.48  ?  186  TYR A HA     1 
ATOM   2928  H HB2    . TYR A 1 186 ? -12.116 -32.639 -13.055 1.00 16.10  ?  186  TYR A HB2    1 
ATOM   2929  H HB3    . TYR A 1 186 ? -13.358 -33.630 -13.090 1.00 16.10  ?  186  TYR A HB3    1 
ATOM   2930  H HD1    . TYR A 1 186 ? -15.354 -31.721 -11.942 1.00 18.13  ?  186  TYR A HD1    1 
ATOM   2931  H HD2    . TYR A 1 186 ? -12.670 -31.329 -14.883 1.00 16.98  ?  186  TYR A HD2    1 
ATOM   2932  H HE1    . TYR A 1 186 ? -16.665 -30.106 -12.947 1.00 17.48  ?  186  TYR A HE1    1 
ATOM   2933  H HE2    . TYR A 1 186 ? -13.951 -29.687 -15.850 1.00 17.62  ?  186  TYR A HE2    1 
ATOM   2934  H HH     . TYR A 1 186 ? -16.931 -28.697 -14.762 1.00 20.39  ?  186  TYR A HH     1 
ATOM   2935  N N      . TYR A 1 187 ? -14.357 -33.404 -9.341  1.00 13.69  ?  187  TYR A N      1 
ATOM   2936  C CA     . TYR A 1 187 ? -15.334 -34.117 -8.537  1.00 15.39  ?  187  TYR A CA     1 
ATOM   2937  C C      . TYR A 1 187 ? -16.738 -34.018 -9.125  1.00 14.60  ?  187  TYR A C      1 
ATOM   2938  O O      . TYR A 1 187 ? -17.484 -35.009 -9.129  1.00 14.84  ?  187  TYR A O      1 
ATOM   2939  C CB     . TYR A 1 187 ? -15.275 -33.526 -7.119  1.00 14.67  ?  187  TYR A CB     1 
ATOM   2940  C CG     . TYR A 1 187 ? -16.246 -34.099 -6.122  1.00 14.54  ?  187  TYR A CG     1 
ATOM   2941  C CD1    . TYR A 1 187 ? -16.168 -35.433 -5.710  1.00 16.32  ?  187  TYR A CD1    1 
ATOM   2942  C CD2    . TYR A 1 187 ? -17.237 -33.309 -5.564  1.00 14.69  ?  187  TYR A CD2    1 
ATOM   2943  C CE1    . TYR A 1 187 ? -17.069 -35.954 -4.774  1.00 16.59  ?  187  TYR A CE1    1 
ATOM   2944  C CE2    . TYR A 1 187 ? -18.124 -33.812 -4.632  1.00 15.74  ?  187  TYR A CE2    1 
ATOM   2945  C CZ     . TYR A 1 187 ? -18.039 -35.133 -4.235  1.00 15.73  ?  187  TYR A CZ     1 
ATOM   2946  O OH     . TYR A 1 187 ? -18.949 -35.598 -3.311  1.00 18.80  ?  187  TYR A OH     1 
ATOM   2947  H H      . TYR A 1 187 ? -13.957 -32.778 -8.907  1.00 16.42  ?  187  TYR A H      1 
ATOM   2948  H HA     . TYR A 1 187 ? -15.123 -35.064 -8.507  1.00 18.46  ?  187  TYR A HA     1 
ATOM   2949  H HB2    . TYR A 1 187 ? -14.383 -33.674 -6.766  1.00 17.61  ?  187  TYR A HB2    1 
ATOM   2950  H HB3    . TYR A 1 187 ? -15.455 -32.575 -7.179  1.00 17.61  ?  187  TYR A HB3    1 
ATOM   2951  H HD1    . TYR A 1 187 ? -15.507 -35.983 -6.063  1.00 19.58  ?  187  TYR A HD1    1 
ATOM   2952  H HD2    . TYR A 1 187 ? -17.308 -32.418 -5.822  1.00 17.63  ?  187  TYR A HD2    1 
ATOM   2953  H HE1    . TYR A 1 187 ? -17.014 -36.847 -4.517  1.00 19.91  ?  187  TYR A HE1    1 
ATOM   2954  H HE2    . TYR A 1 187 ? -18.780 -33.260 -4.271  1.00 18.88  ?  187  TYR A HE2    1 
ATOM   2955  H HH     . TYR A 1 187 ? -18.802 -36.408 -3.145  1.00 22.56  ?  187  TYR A HH     1 
ATOM   2956  N N      . TYR A 1 188 ? -17.131 -32.837 -9.600  1.00 13.53  ?  188  TYR A N      1 
ATOM   2957  C CA     . TYR A 1 188 ? -18.478 -32.629 -10.118 1.00 13.65  ?  188  TYR A CA     1 
ATOM   2958  C C      . TYR A 1 188 ? -18.746 -33.454 -11.371 1.00 12.88  ?  188  TYR A C      1 
ATOM   2959  O O      . TYR A 1 188 ? -19.915 -33.679 -11.715 1.00 15.14  ?  188  TYR A O      1 
ATOM   2960  C CB     . TYR A 1 188 ? -18.725 -31.123 -10.341 1.00 15.13  ?  188  TYR A CB     1 
ATOM   2961  C CG     . TYR A 1 188 ? -20.082 -30.789 -10.940 1.00 17.53  ?  188  TYR A CG     1 
ATOM   2962  C CD1    . TYR A 1 188 ? -21.228 -30.844 -10.174 1.00 17.72  ?  188  TYR A CD1    1 
ATOM   2963  C CD2    . TYR A 1 188 ? -20.207 -30.386 -12.263 1.00 17.02  ?  188  TYR A CD2    1 
ATOM   2964  C CE1    . TYR A 1 188 ? -22.458 -30.542 -10.709 1.00 18.69  ?  188  TYR A CE1    1 
ATOM   2965  C CE2    . TYR A 1 188 ? -21.443 -30.088 -12.817 1.00 17.64  ?  188  TYR A CE2    1 
ATOM   2966  C CZ     . TYR A 1 188 ? -22.570 -30.167 -12.033 1.00 18.69  ?  188  TYR A CZ     1 
ATOM   2967  O OH     . TYR A 1 188 ? -23.807 -29.887 -12.574 1.00 20.48  ?  188  TYR A OH     1 
ATOM   2968  H H      . TYR A 1 188 ? -16.634 -32.136 -9.633  1.00 16.23  ?  188  TYR A H      1 
ATOM   2969  H HA     . TYR A 1 188 ? -19.133 -32.918 -9.462  1.00 16.38  ?  188  TYR A HA     1 
ATOM   2970  H HB2    . TYR A 1 188 ? -18.663 -30.670 -9.485  1.00 18.15  ?  188  TYR A HB2    1 
ATOM   2971  H HB3    . TYR A 1 188 ? -18.046 -30.785 -10.945 1.00 18.15  ?  188  TYR A HB3    1 
ATOM   2972  H HD1    . TYR A 1 188 ? -21.168 -31.091 -9.280  1.00 21.26  ?  188  TYR A HD1    1 
ATOM   2973  H HD2    . TYR A 1 188 ? -19.444 -30.315 -12.790 1.00 20.42  ?  188  TYR A HD2    1 
ATOM   2974  H HE1    . TYR A 1 188 ? -23.219 -30.592 -10.176 1.00 22.42  ?  188  TYR A HE1    1 
ATOM   2975  H HE2    . TYR A 1 188 ? -21.508 -29.837 -13.710 1.00 21.17  ?  188  TYR A HE2    1 
ATOM   2976  H HH     . TYR A 1 188 ? -24.406 -30.004 -11.997 1.00 24.57  ?  188  TYR A HH     1 
ATOM   2977  N N      . HIS A 1 189 ? -17.702 -33.943 -12.044 1.00 14.46  ?  189  HIS A N      1 
ATOM   2978  C CA     . HIS A 1 189 ? -17.878 -34.778 -13.231 1.00 14.43  ?  189  HIS A CA     1 
ATOM   2979  C C      . HIS A 1 189 ? -17.750 -36.266 -12.942 1.00 16.62  ?  189  HIS A C      1 
ATOM   2980  O O      . HIS A 1 189 ? -17.705 -37.068 -13.885 1.00 20.70  ?  189  HIS A O      1 
ATOM   2981  C CB     . HIS A 1 189 ? -16.881 -34.403 -14.326 1.00 14.36  ?  189  HIS A CB     1 
ATOM   2982  C CG     . HIS A 1 189 ? -17.250 -33.167 -15.083 1.00 15.78  ?  189  HIS A CG     1 
ATOM   2983  N ND1    . HIS A 1 189 ? -16.530 -32.713 -16.163 1.00 17.51  ?  189  HIS A ND1    1 
ATOM   2984  C CD2    . HIS A 1 189 ? -18.284 -32.302 -14.935 1.00 14.69  ?  189  HIS A CD2    1 
ATOM   2985  C CE1    . HIS A 1 189 ? -17.100 -31.623 -16.648 1.00 18.71  ?  189  HIS A CE1    1 
ATOM   2986  N NE2    . HIS A 1 189 ? -18.156 -31.343 -15.909 1.00 15.87  ?  189  HIS A NE2    1 
ATOM   2987  H H      . HIS A 1 189 ? -16.881 -33.803 -11.829 1.00 17.35  ?  189  HIS A H      1 
ATOM   2988  H HA     . HIS A 1 189 ? -18.772 -34.605 -13.565 1.00 17.31  ?  189  HIS A HA     1 
ATOM   2989  H HB2    . HIS A 1 189 ? -16.014 -34.253 -13.919 1.00 17.23  ?  189  HIS A HB2    1 
ATOM   2990  H HB3    . HIS A 1 189 ? -16.827 -35.134 -14.962 1.00 17.23  ?  189  HIS A HB3    1 
ATOM   2991  H HD2    . HIS A 1 189 ? -18.956 -32.351 -14.293 1.00 17.62  ?  189  HIS A HD2    1 
ATOM   2992  H HE1    . HIS A 1 189 ? -16.806 -31.137 -17.384 1.00 22.45  ?  189  HIS A HE1    1 
ATOM   2993  H HE2    . HIS A 1 189 ? -18.679 -30.669 -16.019 1.00 19.04  ?  189  HIS A HE2    1 
ATOM   2994  N N      . ARG A 1 190 ? -17.689 -36.658 -11.675 1.00 16.01  ?  190  ARG A N      1 
ATOM   2995  C CA     . ARG A 1 190 ? -17.636 -38.076 -11.353 1.00 17.66  ?  190  ARG A CA     1 
ATOM   2996  C C      . ARG A 1 190 ? -18.870 -38.788 -11.893 1.00 20.61  ?  190  ARG A C      1 
ATOM   2997  O O      . ARG A 1 190 ? -19.933 -38.194 -12.090 1.00 21.09  ?  190  ARG A O      1 
ATOM   2998  C CB     . ARG A 1 190 ? -17.495 -38.267 -9.852  1.00 19.02  ?  190  ARG A CB     1 
ATOM   2999  C CG     . ARG A 1 190 ? -18.765 -38.059 -9.040  1.00 18.84  ?  190  ARG A CG     1 
ATOM   3000  C CD     . ARG A 1 190 ? -18.428 -37.888 -7.562  1.00 18.86  ?  190  ARG A CD     1 
ATOM   3001  N NE     . ARG A 1 190 ? -19.628 -37.634 -6.766  1.00 19.61  ?  190  ARG A NE     1 
ATOM   3002  C CZ     . ARG A 1 190 ? -20.237 -36.457 -6.673  1.00 17.49  ?  190  ARG A CZ     1 
ATOM   3003  N NH1    . ARG A 1 190 ? -19.763 -35.391 -7.303  1.00 15.92  ?  190  ARG A NH1    1 
ATOM   3004  N NH2    . ARG A 1 190 ? -21.317 -36.339 -5.928  1.00 19.74  ?  190  ARG A NH2    1 
ATOM   3005  H H      . ARG A 1 190 ? -17.677 -36.133 -10.994 1.00 19.21  ?  190  ARG A H      1 
ATOM   3006  H HA     . ARG A 1 190 ? -16.861 -38.486 -11.769 1.00 21.19  ?  190  ARG A HA     1 
ATOM   3007  H HB2    . ARG A 1 190 ? -17.193 -39.173 -9.687  1.00 22.82  ?  190  ARG A HB2    1 
ATOM   3008  H HB3    . ARG A 1 190 ? -16.837 -37.633 -9.525  1.00 22.82  ?  190  ARG A HB3    1 
ATOM   3009  H HG2    . ARG A 1 190 ? -19.222 -37.260 -9.348  1.00 22.60  ?  190  ARG A HG2    1 
ATOM   3010  H HG3    . ARG A 1 190 ? -19.345 -38.831 -9.138  1.00 22.60  ?  190  ARG A HG3    1 
ATOM   3011  H HD2    . ARG A 1 190 ? -18.009 -38.697 -7.232  1.00 22.62  ?  190  ARG A HD2    1 
ATOM   3012  H HD3    . ARG A 1 190 ? -17.826 -37.135 -7.455  1.00 22.62  ?  190  ARG A HD3    1 
ATOM   3013  H HE     . ARG A 1 190 ? -19.963 -38.293 -6.327  1.00 23.53  ?  190  ARG A HE     1 
ATOM   3014  H HH11   . ARG A 1 190 ? -19.050 -35.455 -7.780  1.00 19.10  ?  190  ARG A HH11   1 
ATOM   3015  H HH12   . ARG A 1 190 ? -20.168 -34.636 -7.234  1.00 19.10  ?  190  ARG A HH12   1 
ATOM   3016  H HH21   . ARG A 1 190 ? -21.625 -37.021 -5.504  1.00 23.69  ?  190  ARG A HH21   1 
ATOM   3017  H HH22   . ARG A 1 190 ? -21.715 -35.579 -5.865  1.00 23.69  ?  190  ARG A HH22   1 
ATOM   3018  N N      . GLY A 1 191 ? -18.721 -40.072 -12.156 1.00 25.07  ?  191  GLY A N      1 
ATOM   3019  C CA     . GLY A 1 191 ? -19.806 -40.831 -12.744 1.00 27.18  ?  191  GLY A CA     1 
ATOM   3020  C C      . GLY A 1 191 ? -21.035 -40.875 -11.855 1.00 28.59  ?  191  GLY A C      1 
ATOM   3021  O O      . GLY A 1 191 ? -20.972 -40.730 -10.639 1.00 29.08  ?  191  GLY A O      1 
ATOM   3022  H H      . GLY A 1 191 ? -18.008 -40.528 -12.006 1.00 30.08  ?  191  GLY A H      1 
ATOM   3023  H HA2    . GLY A 1 191 ? -20.056 -40.428 -13.590 1.00 32.61  ?  191  GLY A HA2    1 
ATOM   3024  H HA3    . GLY A 1 191 ? -19.510 -41.741 -12.902 1.00 32.61  ?  191  GLY A HA3    1 
ATOM   3025  N N      . ALA A 1 192 ? -22.192 -41.074 -12.496 1.00 30.27  ?  192  ALA A N      1 
ATOM   3026  C CA     . ALA A 1 192 ? -23.435 -41.242 -11.748 1.00 34.17  ?  192  ALA A CA     1 
ATOM   3027  C C      . ALA A 1 192 ? -23.295 -42.325 -10.691 1.00 36.54  ?  192  ALA A C      1 
ATOM   3028  O O      . ALA A 1 192 ? -23.828 -42.200 -9.582  1.00 38.17  ?  192  ALA A O      1 
ATOM   3029  C CB     . ALA A 1 192 ? -24.575 -41.604 -12.703 1.00 35.35  ?  192  ALA A CB     1 
ATOM   3030  H H      . ALA A 1 192 ? -22.282 -41.115 -13.350 1.00 36.32  ?  192  ALA A H      1 
ATOM   3031  H HA     . ALA A 1 192 ? -23.649 -40.403 -11.311 1.00 40.99  ?  192  ALA A HA     1 
ATOM   3032  H HB1    . ALA A 1 192 ? -25.396 -41.697 -12.194 1.00 42.42  ?  192  ALA A HB1    1 
ATOM   3033  H HB2    . ALA A 1 192 ? -24.673 -40.898 -13.361 1.00 42.42  ?  192  ALA A HB2    1 
ATOM   3034  H HB3    . ALA A 1 192 ? -24.364 -42.441 -13.145 1.00 42.42  ?  192  ALA A HB3    1 
ATOM   3035  N N      . GLU A 1 193 ? -22.574 -43.400 -11.016 1.00 37.46  ?  193  GLU A N      1 
ATOM   3036  C CA     . GLU A 1 193 ? -22.395 -44.497 -10.070 1.00 40.71  ?  193  GLU A CA     1 
ATOM   3037  C C      . GLU A 1 193 ? -21.601 -44.079 -8.839  1.00 40.00  ?  193  GLU A C      1 
ATOM   3038  O O      . GLU A 1 193 ? -21.638 -44.782 -7.820  1.00 40.61  ?  193  GLU A O      1 
ATOM   3039  C CB     . GLU A 1 193 ? -21.724 -45.687 -10.772 1.00 43.60  ?  193  GLU A CB     1 
ATOM   3040  C CG     . GLU A 1 193 ? -20.232 -45.516 -11.070 1.00 46.27  ?  193  GLU A CG     1 
ATOM   3041  C CD     . GLU A 1 193 ? -19.945 -44.720 -12.335 1.00 48.66  ?  193  GLU A CD     1 
ATOM   3042  O OE1    . GLU A 1 193 ? -20.888 -44.126 -12.913 1.00 48.48  ?  193  GLU A OE1    1 
ATOM   3043  O OE2    . GLU A 1 193 ? -18.765 -44.690 -12.752 1.00 49.72  -1 193  GLU A OE2    1 
ATOM   3044  H H      . GLU A 1 193 ? -22.181 -43.517 -11.772 1.00 44.95  ?  193  GLU A H      1 
ATOM   3045  H HA     . GLU A 1 193 ? -23.265 -44.794 -9.761  1.00 48.85  ?  193  GLU A HA     1 
ATOM   3046  H HB2    . GLU A 1 193 ? -21.817 -46.468 -10.205 1.00 52.32  ?  193  GLU A HB2    1 
ATOM   3047  H HB3    . GLU A 1 193 ? -22.173 -45.835 -11.619 1.00 52.32  ?  193  GLU A HB3    1 
ATOM   3048  H HG2    . GLU A 1 193 ? -19.816 -45.051 -10.328 1.00 55.52  ?  193  GLU A HG2    1 
ATOM   3049  H HG3    . GLU A 1 193 ? -19.833 -46.394 -11.177 1.00 55.52  ?  193  GLU A HG3    1 
ATOM   3050  N N      . ARG A 1 194 ? -20.888 -42.957 -8.909  1.00 36.88  ?  194  ARG A N      1 
ATOM   3051  C CA     . ARG A 1 194 ? -20.073 -42.466 -7.800  1.00 34.33  ?  194  ARG A CA     1 
ATOM   3052  C C      . ARG A 1 194 ? -20.694 -41.243 -7.136  1.00 32.69  ?  194  ARG A C      1 
ATOM   3053  O O      . ARG A 1 194 ? -19.991 -40.468 -6.484  1.00 29.80  ?  194  ARG A O      1 
ATOM   3054  C CB     . ARG A 1 194 ? -18.644 -42.207 -8.285  1.00 38.05  ?  194  ARG A CB     1 
ATOM   3055  C CG     . ARG A 1 194 ? -17.964 -43.467 -8.881  1.00 42.79  ?  194  ARG A CG     1 
ATOM   3056  C CD     . ARG A 1 194 ? -16.485 -43.247 -9.243  1.00 46.82  ?  194  ARG A CD     1 
ATOM   3057  N NE     . ARG A 1 194 ? -15.804 -44.490 -9.632  1.00 50.36  ?  194  ARG A NE     1 
ATOM   3058  C CZ     . ARG A 1 194 ? -15.377 -44.778 -10.863 1.00 53.65  ?  194  ARG A CZ     1 
ATOM   3059  N NH1    . ARG A 1 194 ? -15.549 -43.924 -11.862 1.00 55.55  ?  194  ARG A NH1    1 
ATOM   3060  N NH2    . ARG A 1 194 ? -14.768 -45.936 -11.095 1.00 55.13  ?  194  ARG A NH2    1 
ATOM   3061  H H      . ARG A 1 194 ? -20.860 -42.452 -9.604  1.00 44.25  ?  194  ARG A H      1 
ATOM   3062  H HA     . ARG A 1 194 ? -20.014 -43.145 -7.110  1.00 41.19  ?  194  ARG A HA     1 
ATOM   3063  H HB2    . ARG A 1 194 ? -18.664 -41.525 -8.974  1.00 45.65  ?  194  ARG A HB2    1 
ATOM   3064  H HB3    . ARG A 1 194 ? -18.108 -41.906 -7.535  1.00 45.65  ?  194  ARG A HB3    1 
ATOM   3065  H HG2    . ARG A 1 194 ? -18.008 -44.185 -8.230  1.00 51.35  ?  194  ARG A HG2    1 
ATOM   3066  H HG3    . ARG A 1 194 ? -18.433 -43.723 -9.690  1.00 51.35  ?  194  ARG A HG3    1 
ATOM   3067  H HD2    . ARG A 1 194 ? -16.430 -42.629 -9.989  1.00 56.18  ?  194  ARG A HD2    1 
ATOM   3068  H HD3    . ARG A 1 194 ? -16.022 -42.881 -8.473  1.00 56.18  ?  194  ARG A HD3    1 
ATOM   3069  H HE     . ARG A 1 194 ? -15.670 -45.078 -9.019  1.00 60.43  ?  194  ARG A HE     1 
ATOM   3070  H HH11   . ARG A 1 194 ? -15.940 -43.172 -11.722 1.00 66.65  ?  194  ARG A HH11   1 
ATOM   3071  H HH12   . ARG A 1 194 ? -15.268 -44.123 -12.651 1.00 66.65  ?  194  ARG A HH12   1 
ATOM   3072  H HH21   . ARG A 1 194 ? -14.650 -46.496 -10.453 1.00 66.15  ?  194  ARG A HH21   1 
ATOM   3073  H HH22   . ARG A 1 194 ? -14.491 -46.125 -11.887 1.00 66.15  ?  194  ARG A HH22   1 
ATOM   3074  N N      . GLU A 1 195 ? -22.010 -41.071 -7.268  1.00 31.74  ?  195  GLU A N      1 
ATOM   3075  C CA     . GLU A 1 195 ? -22.687 -39.942 -6.646  1.00 31.07  ?  195  GLU A CA     1 
ATOM   3076  C C      . GLU A 1 195 ? -22.414 -39.886 -5.155  1.00 30.33  ?  195  GLU A C      1 
ATOM   3077  O O      . GLU A 1 195 ? -22.239 -38.801 -4.583  1.00 30.06  ?  195  GLU A O      1 
ATOM   3078  C CB     . GLU A 1 195 ? -24.194 -40.068 -6.875  1.00 32.26  ?  195  GLU A CB     1 
ATOM   3079  C CG     . GLU A 1 195 ? -25.014 -38.982 -6.205  1.00 31.73  ?  195  GLU A CG     1 
ATOM   3080  C CD     . GLU A 1 195 ? -24.828 -37.634 -6.868  1.00 34.55  ?  195  GLU A CD     1 
ATOM   3081  O OE1    . GLU A 1 195 ? -24.439 -37.606 -8.049  1.00 34.61  ?  195  GLU A OE1    1 
ATOM   3082  O OE2    . GLU A 1 195 ? -25.065 -36.614 -6.200  1.00 37.33  -1 195  GLU A OE2    1 
ATOM   3083  H H      . GLU A 1 195 ? -22.531 -41.592 -7.712  1.00 38.08  ?  195  GLU A H      1 
ATOM   3084  H HA     . GLU A 1 195 ? -22.364 -39.122 -7.051  1.00 37.29  ?  195  GLU A HA     1 
ATOM   3085  H HB2    . GLU A 1 195 ? -24.368 -40.024 -7.828  1.00 38.71  ?  195  GLU A HB2    1 
ATOM   3086  H HB3    . GLU A 1 195 ? -24.491 -40.922 -6.522  1.00 38.71  ?  195  GLU A HB3    1 
ATOM   3087  H HG2    . GLU A 1 195 ? -25.954 -39.216 -6.255  1.00 38.07  ?  195  GLU A HG2    1 
ATOM   3088  H HG3    . GLU A 1 195 ? -24.740 -38.903 -5.278  1.00 38.07  ?  195  GLU A HG3    1 
ATOM   3089  N N      . GLY A 1 196 ? -22.392 -41.044 -4.504  1.00 29.99  ?  196  GLY A N      1 
ATOM   3090  C CA     . GLY A 1 196 ? -22.251 -41.109 -3.069  1.00 27.44  ?  196  GLY A CA     1 
ATOM   3091  C C      . GLY A 1 196 ? -20.854 -40.871 -2.548  1.00 25.27  ?  196  GLY A C      1 
ATOM   3092  O O      . GLY A 1 196 ? -20.676 -40.773 -1.327  1.00 26.24  ?  196  GLY A O      1 
ATOM   3093  H H      . GLY A 1 196 ? -22.457 -41.814 -4.882  1.00 35.99  ?  196  GLY A H      1 
ATOM   3094  H HA2    . GLY A 1 196 ? -22.832 -40.442 -2.670  1.00 32.93  ?  196  GLY A HA2    1 
ATOM   3095  H HA3    . GLY A 1 196 ? -22.531 -41.989 -2.770  1.00 32.93  ?  196  GLY A HA3    1 
ATOM   3096  N N      . MET A 1 197 ? -19.870 -40.803 -3.432  1.00 25.55  ?  197  MET A N      1 
ATOM   3097  C CA     . MET A 1 197 ? -18.502 -40.553 -3.013  1.00 23.94  ?  197  MET A CA     1 
ATOM   3098  C C      . MET A 1 197 ? -18.357 -39.150 -2.442  1.00 21.33  ?  197  MET A C      1 
ATOM   3099  O O      . MET A 1 197 ? -18.827 -38.180 -3.039  1.00 22.51  ?  197  MET A O      1 
ATOM   3100  C CB     . MET A 1 197 ? -17.570 -40.612 -4.216  1.00 28.12  ?  197  MET A CB     1 
ATOM   3101  C CG     . MET A 1 197 ? -16.817 -41.867 -4.387  1.00 29.26  ?  197  MET A CG     1 
ATOM   3102  S SD     . MET A 1 197 ? -15.657 -41.689 -5.756  1.00 29.45  ?  197  MET A SD     1 
ATOM   3103  C CE     . MET A 1 197 ? -15.027 -43.370 -5.785  1.00 32.48  ?  197  MET A CE     1 
ATOM   3104  H H      . MET A 1 197 ? -19.968 -40.899 -4.281  1.00 30.66  ?  197  MET A H      1 
ATOM   3105  H HA     . MET A 1 197 ? -18.272 -41.228 -2.355  1.00 28.73  ?  197  MET A HA     1 
ATOM   3106  H HB2    . MET A 1 197 ? -18.101 -40.484 -5.017  1.00 33.74  ?  197  MET A HB2    1 
ATOM   3107  H HB3    . MET A 1 197 ? -16.920 -39.897 -4.131  1.00 33.74  ?  197  MET A HB3    1 
ATOM   3108  H HG2    . MET A 1 197 ? -16.319 -42.064 -3.578  1.00 35.11  ?  197  MET A HG2    1 
ATOM   3109  H HG3    . MET A 1 197 ? -17.428 -42.593 -4.586  1.00 35.11  ?  197  MET A HG3    1 
ATOM   3110  H HE1    . MET A 1 197 ? -14.400 -43.460 -6.519  1.00 38.97  ?  197  MET A HE1    1 
ATOM   3111  H HE2    . MET A 1 197 ? -14.580 -43.555 -4.944  1.00 38.97  ?  197  MET A HE2    1 
ATOM   3112  H HE3    . MET A 1 197 ? -15.769 -43.983 -5.907  1.00 38.97  ?  197  MET A HE3    1 
ATOM   3113  N N      . SER A 1 198 ? -17.661 -39.042 -1.315  1.00 19.19  ?  198  SER A N      1 
ATOM   3114  C CA     . SER A 1 198 ? -17.211 -37.752 -0.828  1.00 18.02  ?  198  SER A CA     1 
ATOM   3115  C C      . SER A 1 198 ? -16.023 -37.286 -1.650  1.00 18.40  ?  198  SER A C      1 
ATOM   3116  O O      . SER A 1 198 ? -15.432 -38.054 -2.403  1.00 17.33  ?  198  SER A O      1 
ATOM   3117  C CB     . SER A 1 198 ? -16.756 -37.856 0.621   1.00 20.44  ?  198  SER A CB     1 
ATOM   3118  O OG     . SER A 1 198 ? -15.618 -38.697 0.713   1.00 20.28  ?  198  SER A OG     1 
ATOM   3119  H H      . SER A 1 198 ? -17.438 -39.705 -0.815  1.00 23.02  ?  198  SER A H      1 
ATOM   3120  H HA     . SER A 1 198 ? -17.944 -37.119 -0.895  1.00 21.62  ?  198  SER A HA     1 
ATOM   3121  H HB2    . SER A 1 198 ? -16.528 -36.972 0.948   1.00 24.52  ?  198  SER A HB2    1 
ATOM   3122  H HB3    . SER A 1 198 ? -17.474 -38.232 1.154   1.00 24.52  ?  198  SER A HB3    1 
ATOM   3123  H HG     . SER A 1 198 ? -15.279 -38.638 1.480   1.00 24.33  ?  198  SER A HG     1 
ATOM   3124  N N      . GLU A 1 199 ? -15.663 -36.011 -1.491  1.00 18.68  ?  199  GLU A N      1 
ATOM   3125  C CA     . GLU A 1 199 ? -14.466 -35.516 -2.156  1.00 16.35  ?  199  GLU A CA     1 
ATOM   3126  C C      . GLU A 1 199 ? -13.246 -36.356 -1.791  1.00 16.27  ?  199  GLU A C      1 
ATOM   3127  O O      . GLU A 1 199 ? -12.416 -36.671 -2.651  1.00 16.47  ?  199  GLU A O      1 
ATOM   3128  C CB     . GLU A 1 199 ? -14.199 -34.049 -1.811  1.00 15.96  ?  199  GLU A CB     1 
ATOM   3129  C CG     . GLU A 1 199 ? -15.151 -33.068 -2.465  1.00 16.76  ?  199  GLU A CG     1 
ATOM   3130  C CD     . GLU A 1 199 ? -14.768 -31.634 -2.236  1.00 17.34  ?  199  GLU A CD     1 
ATOM   3131  O OE1    . GLU A 1 199 ? -15.669 -30.775 -2.281  1.00 20.00  ?  199  GLU A OE1    1 
ATOM   3132  O OE2    . GLU A 1 199 ? -13.563 -31.340 -2.048  1.00 17.63  -1 199  GLU A OE2    1 
ATOM   3133  H H      . GLU A 1 199 ? -16.082 -35.429 -1.017  1.00 22.42  ?  199  GLU A H      1 
ATOM   3134  H HA     . GLU A 1 199 ? -14.618 -35.571 -3.113  1.00 19.61  ?  199  GLU A HA     1 
ATOM   3135  H HB2    . GLU A 1 199 ? -14.277 -33.938 -0.851  1.00 19.15  ?  199  GLU A HB2    1 
ATOM   3136  H HB3    . GLU A 1 199 ? -13.301 -33.822 -2.099  1.00 19.15  ?  199  GLU A HB3    1 
ATOM   3137  H HG2    . GLU A 1 199 ? -15.158 -33.225 -3.422  1.00 20.11  ?  199  GLU A HG2    1 
ATOM   3138  H HG3    . GLU A 1 199 ? -16.040 -33.201 -2.101  1.00 20.11  ?  199  GLU A HG3    1 
ATOM   3139  N N      . ARG A 1 200 ? -13.118 -36.723 -0.516  1.00 15.97  ?  200  ARG A N      1 
ATOM   3140  C CA     . ARG A 1 200 ? -11.936 -37.466 -0.090  1.00 17.98  ?  200  ARG A CA     1 
ATOM   3141  C C      . ARG A 1 200 ? -11.915 -38.863 -0.702  1.00 17.23  ?  200  ARG A C      1 
ATOM   3142  O O      . ARG A 1 200 ? -10.855 -39.345 -1.133  1.00 16.62  ?  200  ARG A O      1 
ATOM   3143  C CB     . ARG A 1 200 ? -11.901 -37.529 1.429   1.00 23.04  ?  200  ARG A CB     1 
ATOM   3144  C CG     . ARG A 1 200 ? -10.566 -37.822 1.978   1.00 27.74  ?  200  ARG A CG     1 
ATOM   3145  C CD     . ARG A 1 200 ? -10.627 -37.946 3.480   1.00 27.51  ?  200  ARG A CD     1 
ATOM   3146  N NE     . ARG A 1 200 ? -10.766 -36.661 4.154   1.00 26.44  ?  200  ARG A NE     1 
ATOM   3147  C CZ     . ARG A 1 200 ? -9.786  -35.773 4.294   1.00 27.52  ?  200  ARG A CZ     1 
ATOM   3148  N NH1    . ARG A 1 200 ? -8.588  -35.997 3.757   1.00 26.93  ?  200  ARG A NH1    1 
ATOM   3149  N NH2    . ARG A 1 200 ? -10.012 -34.656 4.955   1.00 29.69  ?  200  ARG A NH2    1 
ATOM   3150  H H      . ARG A 1 200 ? -13.686 -36.560 0.108   1.00 19.16  ?  200  ARG A H      1 
ATOM   3151  H HA     . ARG A 1 200 ? -11.137 -37.005 -0.390  1.00 21.57  ?  200  ARG A HA     1 
ATOM   3152  H HB2    . ARG A 1 200 ? -12.186 -36.673 1.784   1.00 27.65  ?  200  ARG A HB2    1 
ATOM   3153  H HB3    . ARG A 1 200 ? -12.504 -38.229 1.726   1.00 27.65  ?  200  ARG A HB3    1 
ATOM   3154  H HG2    . ARG A 1 200 ? -10.241 -38.659 1.612   1.00 33.29  ?  200  ARG A HG2    1 
ATOM   3155  H HG3    . ARG A 1 200 ? -9.957  -37.102 1.751   1.00 33.29  ?  200  ARG A HG3    1 
ATOM   3156  H HD2    . ARG A 1 200 ? -11.391 -38.493 3.720   1.00 33.01  ?  200  ARG A HD2    1 
ATOM   3157  H HD3    . ARG A 1 200 ? -9.809  -38.361 3.795   1.00 33.01  ?  200  ARG A HD3    1 
ATOM   3158  H HE     . ARG A 1 200 ? -11.535 -36.463 4.484   1.00 31.72  ?  200  ARG A HE     1 
ATOM   3159  H HH11   . ARG A 1 200 ? -8.443  -36.720 3.315   1.00 32.31  ?  200  ARG A HH11   1 
ATOM   3160  H HH12   . ARG A 1 200 ? -7.959  -35.418 3.852   1.00 32.31  ?  200  ARG A HH12   1 
ATOM   3161  H HH21   . ARG A 1 200 ? -10.788 -34.505 5.291   1.00 35.63  ?  200  ARG A HH21   1 
ATOM   3162  H HH22   . ARG A 1 200 ? -9.382  -34.078 5.049   1.00 35.63  ?  200  ARG A HH22   1 
ATOM   3163  N N      . GLU A 1 201 ? -13.083 -39.501 -0.801  1.00 16.82  ?  201  GLU A N      1 
ATOM   3164  C CA     . GLU A 1 201 ? -13.162 -40.793 -1.469  1.00 15.90  ?  201  GLU A CA     1 
ATOM   3165  C C      . GLU A 1 201 ? -12.814 -40.652 -2.942  1.00 15.53  ?  201  GLU A C      1 
ATOM   3166  O O      . GLU A 1 201 ? -12.158 -41.528 -3.523  1.00 15.90  ?  201  GLU A O      1 
ATOM   3167  C CB     . GLU A 1 201 ? -14.555 -41.392 -1.277  1.00 17.88  ?  201  GLU A CB     1 
ATOM   3168  C CG     . GLU A 1 201 ? -14.754 -41.966 0.127   1.00 21.39  ?  201  GLU A CG     1 
ATOM   3169  C CD     . GLU A 1 201 ? -16.202 -42.256 0.472   1.00 23.43  ?  201  GLU A CD     1 
ATOM   3170  O OE1    . GLU A 1 201 ? -17.120 -41.699 -0.154  1.00 23.95  ?  201  GLU A OE1    1 
ATOM   3171  O OE2    . GLU A 1 201 ? -16.422 -43.047 1.412   1.00 25.60  -1 201  GLU A OE2    1 
ATOM   3172  H H      . GLU A 1 201 ? -13.833 -39.210 -0.496  1.00 20.18  ?  201  GLU A H      1 
ATOM   3173  H HA     . GLU A 1 201 ? -12.527 -41.408 -1.070  1.00 19.07  ?  201  GLU A HA     1 
ATOM   3174  H HB2    . GLU A 1 201 ? -15.220 -40.700 -1.417  1.00 21.45  ?  201  GLU A HB2    1 
ATOM   3175  H HB3    . GLU A 1 201 ? -14.682 -42.110 -1.917  1.00 21.45  ?  201  GLU A HB3    1 
ATOM   3176  H HG2    . GLU A 1 201 ? -14.262 -42.799 0.196   1.00 25.66  ?  201  GLU A HG2    1 
ATOM   3177  H HG3    . GLU A 1 201 ? -14.419 -41.328 0.776   1.00 25.66  ?  201  GLU A HG3    1 
ATOM   3178  N N      . PHE A 1 202 ? -13.228 -39.547 -3.557  1.00 15.02  ?  202  PHE A N      1 
ATOM   3179  C CA     . PHE A 1 202 ? -12.890 -39.311 -4.949  1.00 14.59  ?  202  PHE A CA     1 
ATOM   3180  C C      . PHE A 1 202 ? -11.384 -39.100 -5.127  1.00 14.50  ?  202  PHE A C      1 
ATOM   3181  O O      . PHE A 1 202 ? -10.780 -39.605 -6.091  1.00 15.67  ?  202  PHE A O      1 
ATOM   3182  C CB     . PHE A 1 202 ? -13.682 -38.105 -5.454  1.00 14.28  ?  202  PHE A CB     1 
ATOM   3183  C CG     . PHE A 1 202 ? -13.388 -37.767 -6.889  1.00 14.31  ?  202  PHE A CG     1 
ATOM   3184  C CD1    . PHE A 1 202 ? -13.889 -38.547 -7.919  1.00 15.40  ?  202  PHE A CD1    1 
ATOM   3185  C CD2    . PHE A 1 202 ? -12.601 -36.686 -7.199  1.00 15.38  ?  202  PHE A CD2    1 
ATOM   3186  C CE1    . PHE A 1 202 ? -13.599 -38.239 -9.229  1.00 16.45  ?  202  PHE A CE1    1 
ATOM   3187  C CE2    . PHE A 1 202 ? -12.304 -36.368 -8.512  1.00 15.96  ?  202  PHE A CE2    1 
ATOM   3188  C CZ     . PHE A 1 202 ? -12.799 -37.148 -9.526  1.00 15.25  ?  202  PHE A CZ     1 
ATOM   3189  H H      . PHE A 1 202 ? -13.700 -38.927 -3.194  1.00 18.03  ?  202  PHE A H      1 
ATOM   3190  H HA     . PHE A 1 202 ? -13.136 -40.083 -5.481  1.00 17.50  ?  202  PHE A HA     1 
ATOM   3191  H HB2    . PHE A 1 202 ? -14.630 -38.298 -5.381  1.00 17.13  ?  202  PHE A HB2    1 
ATOM   3192  H HB3    . PHE A 1 202 ? -13.458 -37.332 -4.913  1.00 17.13  ?  202  PHE A HB3    1 
ATOM   3193  H HD1    . PHE A 1 202 ? -14.424 -39.282 -7.725  1.00 18.48  ?  202  PHE A HD1    1 
ATOM   3194  H HD2    . PHE A 1 202 ? -12.260 -36.158 -6.514  1.00 18.45  ?  202  PHE A HD2    1 
ATOM   3195  H HE1    . PHE A 1 202 ? -13.940 -38.765 -9.916  1.00 19.74  ?  202  PHE A HE1    1 
ATOM   3196  H HE2    . PHE A 1 202 ? -11.773 -35.629 -8.706  1.00 19.15  ?  202  PHE A HE2    1 
ATOM   3197  H HZ     . PHE A 1 202 ? -12.597 -36.945 -10.411 1.00 18.30  ?  202  PHE A HZ     1 
ATOM   3198  N N      . SER A 1 203 ? -10.765 -38.348 -4.220  1.00 13.73  ?  203  SER A N      1 
ATOM   3199  C CA     . SER A 1 203 ? -9.320  -38.202 -4.245  1.00 14.00  ?  203  SER A CA     1 
ATOM   3200  C C      . SER A 1 203 ? -8.622  -39.548 -4.112  1.00 13.73  ?  203  SER A C      1 
ATOM   3201  O O      . SER A 1 203 ? -7.623  -39.819 -4.802  1.00 15.12  ?  203  SER A O      1 
ATOM   3202  C CB     . SER A 1 203 ? -8.896  -37.257 -3.131  1.00 14.09  ?  203  SER A CB     1 
ATOM   3203  O OG     . SER A 1 203 ? -9.320  -35.931 -3.412  1.00 15.36  ?  203  SER A OG     1 
ATOM   3204  H H      . SER A 1 203 ? -11.155 -37.916 -3.586  1.00 16.47  ?  203  SER A H      1 
ATOM   3205  H HA     . SER A 1 203 ? -9.048  -37.820 -5.095  1.00 16.80  ?  203  SER A HA     1 
ATOM   3206  H HB2    . SER A 1 203 ? -9.298  -37.548 -2.298  1.00 16.90  ?  203  SER A HB2    1 
ATOM   3207  H HB3    . SER A 1 203 ? -7.929  -37.270 -3.055  1.00 16.90  ?  203  SER A HB3    1 
ATOM   3208  H HG     . SER A 1 203 ? -9.125  -35.425 -2.771  1.00 18.43  ?  203  SER A HG     1 
ATOM   3209  N N      . ALA A 1 204 ? -9.134  -40.415 -3.233  1.00 15.64  ?  204  ALA A N      1 
ATOM   3210  C CA     . ALA A 1 204 ? -8.541  -41.738 -3.096  1.00 16.13  ?  204  ALA A CA     1 
ATOM   3211  C C      . ALA A 1 204 ? -8.659  -42.522 -4.394  1.00 15.79  ?  204  ALA A C      1 
ATOM   3212  O O      . ALA A 1 204 ? -7.729  -43.235 -4.786  1.00 17.91  ?  204  ALA A O      1 
ATOM   3213  C CB     . ALA A 1 204 ? -9.230  -42.480 -1.951  1.00 17.36  ?  204  ALA A CB     1 
ATOM   3214  H H      . ALA A 1 204 ? -9.807  -40.265 -2.719  1.00 18.76  ?  204  ALA A H      1 
ATOM   3215  H HA     . ALA A 1 204 ? -7.599  -41.653 -2.884  1.00 19.35  ?  204  ALA A HA     1 
ATOM   3216  H HB1    . ALA A 1 204 ? -8.795  -43.337 -1.823  1.00 20.82  ?  204  ALA A HB1    1 
ATOM   3217  H HB2    . ALA A 1 204 ? -9.158  -41.949 -1.142  1.00 20.82  ?  204  ALA A HB2    1 
ATOM   3218  H HB3    . ALA A 1 204 ? -10.164 -42.613 -2.177  1.00 20.82  ?  204  ALA A HB3    1 
ATOM   3219  N N      . HIS A 1 205 ? -9.800  -42.404 -5.068  1.00 15.24  ?  205  HIS A N      1 
ATOM   3220  C CA     . HIS A 1 205 ? -9.989  -43.035 -6.362  1.00 16.02  ?  205  HIS A CA     1 
ATOM   3221  C C      . HIS A 1 205 ? -8.979  -42.519 -7.375  1.00 14.68  ?  205  HIS A C      1 
ATOM   3222  O O      . HIS A 1 205 ? -8.371  -43.299 -8.114  1.00 14.77  ?  205  HIS A O      1 
ATOM   3223  C CB     . HIS A 1 205 ? -11.424 -42.798 -6.839  1.00 18.25  ?  205  HIS A CB     1 
ATOM   3224  C CG     . HIS A 1 205 ? -11.647 -43.107 -8.283  1.00 18.91  ?  205  HIS A CG     1 
ATOM   3225  N ND1    . HIS A 1 205 ? -11.802 -44.390 -8.755  1.00 23.16  ?  205  HIS A ND1    1 
ATOM   3226  C CD2    . HIS A 1 205 ? -11.744 -42.294 -9.360  1.00 21.84  ?  205  HIS A CD2    1 
ATOM   3227  C CE1    . HIS A 1 205 ? -11.980 -44.357 -10.063 1.00 23.87  ?  205  HIS A CE1    1 
ATOM   3228  N NE2    . HIS A 1 205 ? -11.954 -43.095 -10.455 1.00 24.18  ?  205  HIS A NE2    1 
ATOM   3229  H H      . HIS A 1 205 ? -10.485 -41.960 -4.796  1.00 18.28  ?  205  HIS A H      1 
ATOM   3230  H HA     . HIS A 1 205 ? -9.855  -43.992 -6.277  1.00 19.22  ?  205  HIS A HA     1 
ATOM   3231  H HB2    . HIS A 1 205 ? -12.020 -43.361 -6.322  1.00 21.90  ?  205  HIS A HB2    1 
ATOM   3232  H HB3    . HIS A 1 205 ? -11.646 -41.864 -6.701  1.00 21.90  ?  205  HIS A HB3    1 
ATOM   3233  H HD1    . HIS A 1 205 ? -11.786 -45.102 -8.273  1.00 27.78  ?  205  HIS A HD1    1 
ATOM   3234  H HD2    . HIS A 1 205 ? -11.680 -41.366 -9.359  1.00 26.20  ?  205  HIS A HD2    1 
ATOM   3235  H HE1    . HIS A 1 205 ? -12.103 -45.096 -10.614 1.00 28.64  ?  205  HIS A HE1    1 
ATOM   3236  N N      . CYS A 1 206 ? -8.791  -41.196 -7.431  1.00 14.56  ?  206  CYS A N      1 
ATOM   3237  C CA     . CYS A 1 206 ? -7.803  -40.639 -8.350  1.00 13.10  ?  206  CYS A CA     1 
ATOM   3238  C C      . CYS A 1 206 ? -6.404  -41.174 -8.064  1.00 13.45  ?  206  CYS A C      1 
ATOM   3239  O O      . CYS A 1 206 ? -5.667  -41.545 -8.994  1.00 13.36  ?  206  CYS A O      1 
ATOM   3240  C CB     . CYS A 1 206 ? -7.815  -39.120 -8.263  1.00 14.36  ?  206  CYS A CB     1 
ATOM   3241  S SG     . CYS A 1 206 ? -9.296  -38.344 -9.024  1.00 15.16  ?  206  CYS A SG     1 
ATOM   3242  H H      . CYS A 1 206 ? -9.212  -40.614 -6.959  1.00 17.46  ?  206  CYS A H      1 
ATOM   3243  H HA     . CYS A 1 206 ? -8.041  -40.899 -9.254  1.00 15.72  ?  206  CYS A HA     1 
ATOM   3244  H HB2    . CYS A 1 206 ? -7.793  -38.861 -7.328  1.00 17.23  ?  206  CYS A HB2    1 
ATOM   3245  H HB3    . CYS A 1 206 ? -7.032  -38.775 -8.721  1.00 17.23  ?  206  CYS A HB3    1 
ATOM   3246  H HG     . CYS A 1 206 ? -9.221  -37.153 -8.900  1.00 18.19  ?  206  CYS A HG     1 
ATOM   3247  N N      . ALA A 1 207 ? -6.016  -41.232 -6.785  1.00 12.89  ?  207  ALA A N      1 
ATOM   3248  C CA     . ALA A 1 207 ? -4.692  -41.723 -6.439  1.00 13.30  ?  207  ALA A CA     1 
ATOM   3249  C C      . ALA A 1 207 ? -4.544  -43.195 -6.800  1.00 13.69  ?  207  ALA A C      1 
ATOM   3250  O O      . ALA A 1 207 ? -3.494  -43.609 -7.287  1.00 15.32  ?  207  ALA A O      1 
ATOM   3251  C CB     . ALA A 1 207 ? -4.422  -41.493 -4.958  1.00 15.86  ?  207  ALA A CB     1 
ATOM   3252  H H      . ALA A 1 207 ? -6.496  -40.996 -6.112  1.00 15.46  ?  207  ALA A H      1 
ATOM   3253  H HA     . ALA A 1 207 ? -4.026  -41.225 -6.940  1.00 15.96  ?  207  ALA A HA     1 
ATOM   3254  H HB1    . ALA A 1 207 ? -3.542  -41.838 -4.740  1.00 19.03  ?  207  ALA A HB1    1 
ATOM   3255  H HB2    . ALA A 1 207 ? -4.458  -40.541 -4.774  1.00 19.03  ?  207  ALA A HB2    1 
ATOM   3256  H HB3    . ALA A 1 207 ? -5.097  -41.956 -4.438  1.00 19.03  ?  207  ALA A HB3    1 
ATOM   3257  N N      . ALA A 1 208 ? -5.592  -43.998 -6.568  1.00 14.68  ?  208  ALA A N      1 
ATOM   3258  C CA     . ALA A 1 208 ? -5.557  -45.412 -6.935  1.00 15.53  ?  208  ALA A CA     1 
ATOM   3259  C C      . ALA A 1 208 ? -5.386  -45.586 -8.438  1.00 14.96  ?  208  ALA A C      1 
ATOM   3260  O O      . ALA A 1 208 ? -4.640  -46.463 -8.887  1.00 15.47  ?  208  ALA A O      1 
ATOM   3261  C CB     . ALA A 1 208 ? -6.841  -46.111 -6.463  1.00 16.85  ?  208  ALA A CB     1 
ATOM   3262  H H      . ALA A 1 208 ? -6.330  -43.750 -6.203  1.00 17.61  ?  208  ALA A H      1 
ATOM   3263  H HA     . ALA A 1 208 ? -4.803  -45.830 -6.491  1.00 18.64  ?  208  ALA A HA     1 
ATOM   3264  H HB1    . ALA A 1 208 ? -6.800  -47.047 -6.712  1.00 20.22  ?  208  ALA A HB1    1 
ATOM   3265  H HB2    . ALA A 1 208 ? -6.909  -46.027 -5.499  1.00 20.22  ?  208  ALA A HB2    1 
ATOM   3266  H HB3    . ALA A 1 208 ? -7.604  -45.688 -6.887  1.00 20.22  ?  208  ALA A HB3    1 
ATOM   3267  N N      . LYS A 1 209 ? -6.103  -44.791 -9.238  1.00 14.08  ?  209  LYS A N      1 
ATOM   3268  C CA     . LYS A 1 209 ? -5.988  -44.917 -10.693 1.00 14.38  ?  209  LYS A CA     1 
ATOM   3269  C C      . LYS A 1 209 ? -4.590  -44.524 -11.169 1.00 15.13  ?  209  LYS A C      1 
ATOM   3270  O O      . LYS A 1 209 ? -4.033  -45.152 -12.073 1.00 14.74  ?  209  LYS A O      1 
ATOM   3271  C CB     . LYS A 1 209 ? -7.067  -44.060 -11.376 1.00 13.34  ?  209  LYS A CB     1 
ATOM   3272  C CG     . LYS A 1 209 ? -8.500  -44.561 -11.261 1.00 18.72  ?  209  LYS A CG     1 
ATOM   3273  C CD     . LYS A 1 209 ? -8.755  -45.862 -12.044 1.00 21.09  ?  209  LYS A CD     1 
ATOM   3274  C CE     . LYS A 1 209 ? -8.827  -45.647 -13.542 1.00 25.55  ?  209  LYS A CE     1 
ATOM   3275  N NZ     . LYS A 1 209 ? -9.171  -46.895 -14.338 1.00 30.95  ?  209  LYS A NZ     1 
ATOM   3276  H H      . LYS A 1 209 ? -6.652  -44.184 -8.972  1.00 16.89  ?  209  LYS A H      1 
ATOM   3277  H HA     . LYS A 1 209 ? -6.137  -45.840 -10.948 1.00 17.25  ?  209  LYS A HA     1 
ATOM   3278  H HB2    . LYS A 1 209 ? -7.042  -43.174 -10.982 1.00 16.00  ?  209  LYS A HB2    1 
ATOM   3279  H HB3    . LYS A 1 209 ? -6.857  -44.009 -12.322 1.00 16.00  ?  209  LYS A HB3    1 
ATOM   3280  H HG2    . LYS A 1 209 ? -8.699  -44.732 -10.328 1.00 22.47  ?  209  LYS A HG2    1 
ATOM   3281  H HG3    . LYS A 1 209 ? -9.099  -43.882 -11.610 1.00 22.47  ?  209  LYS A HG3    1 
ATOM   3282  H HD2    . LYS A 1 209 ? -8.033  -46.484 -11.866 1.00 25.31  ?  209  LYS A HD2    1 
ATOM   3283  H HD3    . LYS A 1 209 ? -9.600  -46.243 -11.756 1.00 25.31  ?  209  LYS A HD3    1 
ATOM   3284  H HE2    . LYS A 1 209 ? -9.510  -44.984 -13.728 1.00 30.66  ?  209  LYS A HE2    1 
ATOM   3285  H HE3    . LYS A 1 209 ? -7.964  -45.331 -13.852 1.00 30.66  ?  209  LYS A HE3    1 
ATOM   3286  H HZ1    . LYS A 1 209 ? -9.183  -46.707 -15.208 1.00 37.14  ?  209  LYS A HZ1    1 
ATOM   3287  H HZ2    . LYS A 1 209 ? -8.564  -47.529 -14.189 1.00 37.14  ?  209  LYS A HZ2    1 
ATOM   3288  H HZ3    . LYS A 1 209 ? -9.971  -47.200 -14.097 1.00 37.14  ?  209  LYS A HZ3    1 
ATOM   3289  N N      . LEU A 1 210 ? -4.006  -43.493 -10.553 1.00 12.85  ?  210  LEU A N      1 
ATOM   3290  C CA     . LEU A 1 210 ? -2.625  -43.120 -10.856 1.00 11.98  ?  210  LEU A CA     1 
ATOM   3291  C C      . LEU A 1 210 ? -1.672  -44.260 -10.547 1.00 13.76  ?  210  LEU A C      1 
ATOM   3292  O O      . LEU A 1 210 ? -0.830  -44.619 -11.378 1.00 14.87  ?  210  LEU A O      1 
ATOM   3293  C CB     . LEU A 1 210 ? -2.248  -41.840 -10.111 1.00 13.13  ?  210  LEU A CB     1 
ATOM   3294  C CG     . LEU A 1 210 ? -0.774  -41.435 -10.230 1.00 14.01  ?  210  LEU A CG     1 
ATOM   3295  C CD1    . LEU A 1 210 ? -0.394  -41.098 -11.686 1.00 13.61  ?  210  LEU A CD1    1 
ATOM   3296  C CD2    . LEU A 1 210 ? -0.456  -40.261 -9.321  1.00 14.71  ?  210  LEU A CD2    1 
ATOM   3297  H H      . LEU A 1 210 ? -4.384  -42.997 -9.960  1.00 15.41  ?  210  LEU A H      1 
ATOM   3298  H HA     . LEU A 1 210 ? -2.548  -42.931 -11.804 1.00 14.38  ?  210  LEU A HA     1 
ATOM   3299  H HB2    . LEU A 1 210 ? -2.781  -41.110 -10.465 1.00 15.76  ?  210  LEU A HB2    1 
ATOM   3300  H HB3    . LEU A 1 210 ? -2.442  -41.964 -9.169  1.00 15.76  ?  210  LEU A HB3    1 
ATOM   3301  H HG     . LEU A 1 210 ? -0.236  -42.192 -9.951  1.00 16.80  ?  210  LEU A HG     1 
ATOM   3302  H HD11   . LEU A 1 210 ? 0.533   -40.815 -11.713 1.00 16.33  ?  210  LEU A HD11   1 
ATOM   3303  H HD12   . LEU A 1 210 ? -0.514  -41.889 -12.234 1.00 16.33  ?  210  LEU A HD12   1 
ATOM   3304  H HD13   . LEU A 1 210 ? -0.968  -40.384 -12.005 1.00 16.33  ?  210  LEU A HD13   1 
ATOM   3305  H HD21   . LEU A 1 210 ? 0.486   -40.045 -9.402  1.00 17.65  ?  210  LEU A HD21   1 
ATOM   3306  H HD22   . LEU A 1 210 ? -0.994  -39.500 -9.589  1.00 17.65  ?  210  LEU A HD22   1 
ATOM   3307  H HD23   . LEU A 1 210 ? -0.662  -40.506 -8.406  1.00 17.65  ?  210  LEU A HD23   1 
ATOM   3308  N N      . GLU A 1 211 ? -1.818  -44.877 -9.370  1.00 13.39  ?  211  GLU A N      1 
ATOM   3309  C CA     . GLU A 1 211 ? -0.947  -45.996 -9.026  1.00 13.18  ?  211  GLU A CA     1 
ATOM   3310  C C      . GLU A 1 211 ? -1.139  -47.161 -9.989  1.00 13.79  ?  211  GLU A C      1 
ATOM   3311  O O      . GLU A 1 211 ? -0.164  -47.788 -10.416 1.00 13.99  ?  211  GLU A O      1 
ATOM   3312  C CB     . GLU A 1 211 ? -1.198  -46.449 -7.595  1.00 14.07  ?  211  GLU A CB     1 
ATOM   3313  C CG     . GLU A 1 211 ? -0.325  -47.632 -7.206  1.00 14.34  ?  211  GLU A CG     1 
ATOM   3314  C CD     . GLU A 1 211 ? -0.154  -47.774 -5.696  1.00 20.60  ?  211  GLU A CD     1 
ATOM   3315  O OE1    . GLU A 1 211 ? 0.807   -48.419 -5.256  1.00 19.65  ?  211  GLU A OE1    1 
ATOM   3316  O OE2    . GLU A 1 211 ? -0.997  -47.229 -4.941  1.00 24.11  -1 211  GLU A OE2    1 
ATOM   3317  H H      . GLU A 1 211 ? -2.398  -44.672 -8.769  1.00 16.07  ?  211  GLU A H      1 
ATOM   3318  H HA     . GLU A 1 211 ? -0.026  -45.696 -9.088  1.00 15.81  ?  211  GLU A HA     1 
ATOM   3319  H HB2    . GLU A 1 211 ? -1.002  -45.716 -6.991  1.00 16.88  ?  211  GLU A HB2    1 
ATOM   3320  H HB3    . GLU A 1 211 ? -2.127  -46.715 -7.505  1.00 16.88  ?  211  GLU A HB3    1 
ATOM   3321  H HG2    . GLU A 1 211 ? -0.732  -48.447 -7.538  1.00 17.20  ?  211  GLU A HG2    1 
ATOM   3322  H HG3    . GLU A 1 211 ? 0.555   -47.517 -7.597  1.00 17.20  ?  211  GLU A HG3    1 
ATOM   3323  N N      . GLU A 1 212 ? -2.397  -47.452 -10.362 1.00 13.52  ?  212  GLU A N      1 
ATOM   3324  C CA     . GLU A 1 212 ? -2.648  -48.526 -11.318 1.00 13.92  ?  212  GLU A CA     1 
ATOM   3325  C C      . GLU A 1 212 ? -1.971  -48.241 -12.645 1.00 13.48  ?  212  GLU A C      1 
ATOM   3326  O O      . GLU A 1 212 ? -1.424  -49.146 -13.287 1.00 14.84  ?  212  GLU A O      1 
ATOM   3327  C CB     . GLU A 1 212 ? -4.151  -48.708 -11.543 1.00 15.35  ?  212  GLU A CB     1 
ATOM   3328  C CG     . GLU A 1 212 ? -4.876  -49.278 -10.361 1.00 17.02  ?  212  GLU A CG     1 
ATOM   3329  C CD     . GLU A 1 212 ? -6.363  -49.419 -10.574 1.00 20.03  ?  212  GLU A CD     1 
ATOM   3330  O OE1    . GLU A 1 212 ? -6.862  -49.145 -11.697 1.00 20.38  ?  212  GLU A OE1    1 
ATOM   3331  O OE2    . GLU A 1 212 ? -7.032  -49.830 -9.600  1.00 20.49  -1 212  GLU A OE2    1 
ATOM   3332  H H      . GLU A 1 212 ? -3.103  -47.050 -10.080 1.00 16.22  ?  212  GLU A H      1 
ATOM   3333  H HA     . GLU A 1 212 ? -2.292  -49.349 -10.949 1.00 16.71  ?  212  GLU A HA     1 
ATOM   3334  H HB2    . GLU A 1 212 ? -4.544  -47.844 -11.743 1.00 18.42  ?  212  GLU A HB2    1 
ATOM   3335  H HB3    . GLU A 1 212 ? -4.284  -49.313 -12.290 1.00 18.42  ?  212  GLU A HB3    1 
ATOM   3336  H HG2    . GLU A 1 212 ? -4.519  -50.159 -10.170 1.00 20.42  ?  212  GLU A HG2    1 
ATOM   3337  H HG3    . GLU A 1 212 ? -4.740  -48.693 -9.600  1.00 20.42  ?  212  GLU A HG3    1 
ATOM   3338  N N      . MET A 1 213 ? -2.015  -46.985 -13.089 1.00 13.54  ?  213  MET A N      1 
ATOM   3339  C CA     . MET A 1 213 ? -1.378  -46.625 -14.347 1.00 13.13  ?  213  MET A CA     1 
ATOM   3340  C C      . MET A 1 213 ? 0.130   -46.844 -14.261 1.00 14.05  ?  213  MET A C      1 
ATOM   3341  O O      . MET A 1 213 ? 0.746   -47.402 -15.177 1.00 13.97  ?  213  MET A O      1 
ATOM   3342  C CB     . MET A 1 213 ? -1.708  -45.170 -14.688 1.00 13.47  ?  213  MET A CB     1 
ATOM   3343  C CG     . MET A 1 213 ? -0.909  -44.644 -15.883 1.00 15.10  ?  213  MET A CG     1 
ATOM   3344  S SD     . MET A 1 213 ? -1.436  -43.011 -16.442 1.00 15.08  ?  213  MET A SD     1 
ATOM   3345  C CE     . MET A 1 213 ? -2.949  -43.382 -17.320 1.00 15.65  ?  213  MET A CE     1 
ATOM   3346  H H      . MET A 1 213 ? -2.402  -46.332 -12.685 1.00 16.24  ?  213  MET A H      1 
ATOM   3347  H HA     . MET A 1 213 ? -1.732  -47.179 -15.061 1.00 15.75  ?  213  MET A HA     1 
ATOM   3348  H HB2    . MET A 1 213 ? -2.651  -45.103 -14.905 1.00 16.16  ?  213  MET A HB2    1 
ATOM   3349  H HB3    . MET A 1 213 ? -1.504  -44.613 -13.921 1.00 16.16  ?  213  MET A HB3    1 
ATOM   3350  H HG2    . MET A 1 213 ? 0.026   -44.584 -15.632 1.00 18.11  ?  213  MET A HG2    1 
ATOM   3351  H HG3    . MET A 1 213 ? -1.014  -45.259 -16.625 1.00 18.11  ?  213  MET A HG3    1 
ATOM   3352  H HE1    . MET A 1 213 ? -3.341  -42.553 -17.638 1.00 18.78  ?  213  MET A HE1    1 
ATOM   3353  H HE2    . MET A 1 213 ? -2.744  -43.960 -18.072 1.00 18.78  ?  213  MET A HE2    1 
ATOM   3354  H HE3    . MET A 1 213 ? -3.563  -43.828 -16.717 1.00 18.78  ?  213  MET A HE3    1 
ATOM   3355  N N      . ILE A 1 214 ? 0.744   -46.385 -13.170 1.00 13.11  ?  214  ILE A N      1 
ATOM   3356  C CA     . ILE A 1 214 ? 2.181   -46.552 -13.004 1.00 13.58  ?  214  ILE A CA     1 
ATOM   3357  C C      . ILE A 1 214 ? 2.559   -48.027 -13.014 1.00 14.61  ?  214  ILE A C      1 
ATOM   3358  O O      . ILE A 1 214 ? 3.542   -48.430 -13.659 1.00 14.93  ?  214  ILE A O      1 
ATOM   3359  C CB     . ILE A 1 214 ? 2.648   -45.818 -11.744 1.00 13.68  ?  214  ILE A CB     1 
ATOM   3360  C CG1    . ILE A 1 214 ? 2.517   -44.292 -11.906 1.00 14.53  ?  214  ILE A CG1    1 
ATOM   3361  C CG2    . ILE A 1 214 ? 4.077   -46.169 -11.427 1.00 13.16  ?  214  ILE A CG2    1 
ATOM   3362  C CD1    . ILE A 1 214 ? 2.665   -43.505 -10.604 1.00 14.81  ?  214  ILE A CD1    1 
ATOM   3363  H H      . ILE A 1 214 ? 0.355   -45.979 -12.519 1.00 15.73  ?  214  ILE A H      1 
ATOM   3364  H HA     . ILE A 1 214 ? 2.638   -46.148 -13.758 1.00 16.29  ?  214  ILE A HA     1 
ATOM   3365  H HB     . ILE A 1 214 ? 2.076   -46.102 -11.015 1.00 16.42  ?  214  ILE A HB     1 
ATOM   3366  H HG12   . ILE A 1 214 ? 3.207   -43.985 -12.515 1.00 17.43  ?  214  ILE A HG12   1 
ATOM   3367  H HG13   . ILE A 1 214 ? 1.640   -44.094 -12.271 1.00 17.43  ?  214  ILE A HG13   1 
ATOM   3368  H HG21   . ILE A 1 214 ? 4.417   -45.545 -10.766 1.00 15.79  ?  214  ILE A HG21   1 
ATOM   3369  H HG22   . ILE A 1 214 ? 4.110   -47.072 -11.076 1.00 15.79  ?  214  ILE A HG22   1 
ATOM   3370  H HG23   . ILE A 1 214 ? 4.605   -46.110 -12.239 1.00 15.79  ?  214  ILE A HG23   1 
ATOM   3371  H HD11   . ILE A 1 214 ? 2.493   -42.567 -10.780 1.00 17.77  ?  214  ILE A HD11   1 
ATOM   3372  H HD12   . ILE A 1 214 ? 2.025   -43.843 -9.957  1.00 17.77  ?  214  ILE A HD12   1 
ATOM   3373  H HD13   . ILE A 1 214 ? 3.567   -43.618 -10.267 1.00 17.77  ?  214  ILE A HD13   1 
ATOM   3374  N N      . LEU A 1 215 ? 1.775   -48.861 -12.323 1.00 14.55  ?  215  LEU A N      1 
ATOM   3375  C CA     . LEU A 1 215 ? 2.082   -50.291 -12.258 1.00 14.81  ?  215  LEU A CA     1 
ATOM   3376  C C      . LEU A 1 215 ? 1.871   -50.980 -13.605 1.00 16.18  ?  215  LEU A C      1 
ATOM   3377  O O      . LEU A 1 215 ? 2.643   -51.876 -13.972 1.00 18.07  ?  215  LEU A O      1 
ATOM   3378  C CB     . LEU A 1 215 ? 1.240   -50.958 -11.170 1.00 15.40  ?  215  LEU A CB     1 
ATOM   3379  C CG     . LEU A 1 215 ? 1.664   -50.655 -9.739  1.00 16.52  ?  215  LEU A CG     1 
ATOM   3380  C CD1    . LEU A 1 215 ? 0.632   -51.162 -8.740  1.00 16.78  ?  215  LEU A CD1    1 
ATOM   3381  C CD2    . LEU A 1 215 ? 3.037   -51.240 -9.444  1.00 18.77  ?  215  LEU A CD2    1 
ATOM   3382  H H      . LEU A 1 215 ? 1.069   -48.629 -11.888 1.00 17.46  ?  215  LEU A H      1 
ATOM   3383  H HA     . LEU A 1 215 ? 3.017   -50.393 -12.023 1.00 17.77  ?  215  LEU A HA     1 
ATOM   3384  H HB2    . LEU A 1 215 ? 0.322   -50.661 -11.269 1.00 18.48  ?  215  LEU A HB2    1 
ATOM   3385  H HB3    . LEU A 1 215 ? 1.292   -51.919 -11.290 1.00 18.48  ?  215  LEU A HB3    1 
ATOM   3386  H HG     . LEU A 1 215 ? 1.724   -49.692 -9.634  1.00 19.82  ?  215  LEU A HG     1 
ATOM   3387  H HD11   . LEU A 1 215 ? 0.932   -50.953 -7.842  1.00 20.13  ?  215  LEU A HD11   1 
ATOM   3388  H HD12   . LEU A 1 215 ? -0.217  -50.726 -8.915  1.00 20.13  ?  215  LEU A HD12   1 
ATOM   3389  H HD13   . LEU A 1 215 ? 0.538   -52.122 -8.843  1.00 20.13  ?  215  LEU A HD13   1 
ATOM   3390  H HD21   . LEU A 1 215 ? 3.188   -51.227 -8.486  1.00 22.53  ?  215  LEU A HD21   1 
ATOM   3391  H HD22   . LEU A 1 215 ? 3.068   -52.153 -9.771  1.00 22.53  ?  215  LEU A HD22   1 
ATOM   3392  H HD23   . LEU A 1 215 ? 3.711   -50.706 -9.892  1.00 22.53  ?  215  LEU A HD23   1 
ATOM   3393  N N      . ALA A 1 216 ? 0.831   -50.582 -14.346 1.00 15.87  ?  216  ALA A N      1 
ATOM   3394  C CA     . ALA A 1 216 ? 0.566   -51.190 -15.646 1.00 17.31  ?  216  ALA A CA     1 
ATOM   3395  C C      . ALA A 1 216 ? 1.653   -50.835 -16.650 1.00 16.88  ?  216  ALA A C      1 
ATOM   3396  O O      . ALA A 1 216 ? 1.995   -51.651 -17.520 1.00 18.00  ?  216  ALA A O      1 
ATOM   3397  C CB     . ALA A 1 216 ? -0.794  -50.720 -16.164 1.00 15.79  ?  216  ALA A CB     1 
ATOM   3398  H H      . ALA A 1 216 ? 0.272   -49.968 -14.122 1.00 19.04  ?  216  ALA A H      1 
ATOM   3399  H HA     . ALA A 1 216 ? 0.545   -52.155 -15.544 1.00 20.77  ?  216  ALA A HA     1 
ATOM   3400  H HB1    . ALA A 1 216 ? -0.931  -51.075 -17.057 1.00 18.94  ?  216  ALA A HB1    1 
ATOM   3401  H HB2    . ALA A 1 216 ? -1.488  -51.044 -15.569 1.00 18.94  ?  216  ALA A HB2    1 
ATOM   3402  H HB3    . ALA A 1 216 ? -0.805  -49.751 -16.189 1.00 18.94  ?  216  ALA A HB3    1 
ATOM   3403  N N      . GLU A 1 217 ? 2.169   -49.606 -16.575 1.00 16.04  ?  217  GLU A N      1 
ATOM   3404  C CA     . GLU A 1 217 ? 3.220   -49.162 -17.469 1.00 15.51  ?  217  GLU A CA     1 
ATOM   3405  C C      . GLU A 1 217 ? 4.577   -49.689 -17.060 1.00 14.13  ?  217  GLU A C      1 
ATOM   3406  O O      . GLU A 1 217 ? 5.456   -49.814 -17.916 1.00 16.89  ?  217  GLU A O      1 
ATOM   3407  C CB     . GLU A 1 217 ? 3.283   -47.638 -17.498 1.00 15.23  ?  217  GLU A CB     1 
ATOM   3408  C CG     . GLU A 1 217 ? 2.063   -46.941 -18.116 1.00 16.00  ?  217  GLU A CG     1 
ATOM   3409  C CD     . GLU A 1 217 ? 1.850   -47.281 -19.576 1.00 18.12  ?  217  GLU A CD     1 
ATOM   3410  O OE1    . GLU A 1 217 ? 2.846   -47.464 -20.301 1.00 19.16  ?  217  GLU A OE1    1 
ATOM   3411  O OE2    . GLU A 1 217 ? 0.676   -47.373 -20.000 1.00 18.97  -1 217  GLU A OE2    1 
ATOM   3412  H H      . GLU A 1 217 ? 1.922   -49.010 -16.007 1.00 19.24  ?  217  GLU A H      1 
ATOM   3413  H HA     . GLU A 1 217 ? 3.013   -49.476 -18.363 1.00 18.61  ?  217  GLU A HA     1 
ATOM   3414  H HB2    . GLU A 1 217 ? 3.368   -47.318 -16.587 1.00 18.27  ?  217  GLU A HB2    1 
ATOM   3415  H HB3    . GLU A 1 217 ? 4.059   -47.375 -18.017 1.00 18.27  ?  217  GLU A HB3    1 
ATOM   3416  H HG2    . GLU A 1 217 ? 1.268   -47.211 -17.629 1.00 19.20  ?  217  GLU A HG2    1 
ATOM   3417  H HG3    . GLU A 1 217 ? 2.183   -45.981 -18.049 1.00 19.20  ?  217  GLU A HG3    1 
ATOM   3418  N N      . GLY A 1 218 ? 4.751   -50.021 -15.771 1.00 15.53  ?  218  GLY A N      1 
ATOM   3419  C CA     . GLY A 1 218 ? 6.041   -50.362 -15.208 1.00 15.88  ?  218  GLY A CA     1 
ATOM   3420  C C      . GLY A 1 218 ? 6.646   -49.113 -14.593 1.00 15.02  ?  218  GLY A C      1 
ATOM   3421  O O      . GLY A 1 218 ? 6.948   -48.147 -15.287 1.00 15.28  ?  218  GLY A O      1 
ATOM   3422  H H      . GLY A 1 218 ? 4.112   -50.054 -15.197 1.00 18.63  ?  218  GLY A H      1 
ATOM   3423  H HA2    . GLY A 1 218 ? 5.939   -51.041 -14.523 1.00 19.06  ?  218  GLY A HA2    1 
ATOM   3424  H HA3    . GLY A 1 218 ? 6.631   -50.698 -15.900 1.00 19.06  ?  218  GLY A HA3    1 
ATOM   3425  N N      . PRO A 1 219 ? 6.787   -49.090 -13.264 1.00 16.07  ?  219  PRO A N      1 
ATOM   3426  C CA     . PRO A 1 219 ? 7.308   -47.872 -12.620 1.00 17.57  ?  219  PRO A CA     1 
ATOM   3427  C C      . PRO A 1 219 ? 8.649   -47.442 -13.161 1.00 16.63  ?  219  PRO A C      1 
ATOM   3428  O O      . PRO A 1 219 ? 8.941   -46.238 -13.202 1.00 17.08  ?  219  PRO A O      1 
ATOM   3429  C CB     . PRO A 1 219 ? 7.415   -48.267 -11.142 1.00 19.52  ?  219  PRO A CB     1 
ATOM   3430  C CG     . PRO A 1 219 ? 6.511   -49.422 -10.993 1.00 22.34  ?  219  PRO A CG     1 
ATOM   3431  C CD     . PRO A 1 219 ? 6.495   -50.151 -12.281 1.00 19.22  ?  219  PRO A CD     1 
ATOM   3432  H HA     . PRO A 1 219 ? 6.666   -47.152 -12.718 1.00 21.09  ?  219  PRO A HA     1 
ATOM   3433  H HB2    . PRO A 1 219 ? 8.329   -48.511 -10.931 1.00 23.43  ?  219  PRO A HB2    1 
ATOM   3434  H HB3    . PRO A 1 219 ? 7.131   -47.528 -10.582 1.00 23.43  ?  219  PRO A HB3    1 
ATOM   3435  H HG2    . PRO A 1 219 ? 6.841   -49.997 -10.285 1.00 26.81  ?  219  PRO A HG2    1 
ATOM   3436  H HG3    . PRO A 1 219 ? 5.620   -49.105 -10.775 1.00 26.81  ?  219  PRO A HG3    1 
ATOM   3437  H HD2    . PRO A 1 219 ? 7.180   -50.837 -12.299 1.00 23.06  ?  219  PRO A HD2    1 
ATOM   3438  H HD3    . PRO A 1 219 ? 5.625   -50.546 -12.446 1.00 23.06  ?  219  PRO A HD3    1 
ATOM   3439  N N      . GLU A 1 220 ? 9.471   -48.397 -13.595 1.00 14.23  ?  220  GLU A N      1 
ATOM   3440  C CA     . GLU A 1 220 ? 10.773  -48.069 -14.145 1.00 14.24  ?  220  GLU A CA     1 
ATOM   3441  C C      . GLU A 1 220 ? 10.673  -47.294 -15.451 1.00 14.01  ?  220  GLU A C      1 
ATOM   3442  O O      . GLU A 1 220 ? 11.699  -46.806 -15.928 1.00 14.78  ?  220  GLU A O      1 
ATOM   3443  C CB     . GLU A 1 220 ? 11.597  -49.347 -14.316 1.00 18.04  ?  220  GLU A CB     1 
ATOM   3444  C CG     . GLU A 1 220 ? 11.233  -50.212 -15.518 1.00 19.75  ?  220  GLU A CG     1 
ATOM   3445  C CD     . GLU A 1 220 ? 9.937   -50.998 -15.360 1.00 19.72  ?  220  GLU A CD     1 
ATOM   3446  O OE1    . GLU A 1 220 ? 9.326   -51.053 -14.265 1.00 18.87  ?  220  GLU A OE1    1 
ATOM   3447  O OE2    . GLU A 1 220 ? 9.523   -51.572 -16.387 1.00 20.62  -1 220  GLU A OE2    1 
ATOM   3448  H H      . GLU A 1 220 ? 9.295   -49.238 -13.580 1.00 17.07  ?  220  GLU A H      1 
ATOM   3449  H HA     . GLU A 1 220 ? 11.257  -47.505 -13.522 1.00 17.08  ?  220  GLU A HA     1 
ATOM   3450  H HB2    . GLU A 1 220 ? 12.529  -49.097 -14.412 1.00 21.65  ?  220  GLU A HB2    1 
ATOM   3451  H HB3    . GLU A 1 220 ? 11.480  -49.893 -13.522 1.00 21.65  ?  220  GLU A HB3    1 
ATOM   3452  H HG2    . GLU A 1 220 ? 11.136  -49.639 -16.294 1.00 23.69  ?  220  GLU A HG2    1 
ATOM   3453  H HG3    . GLU A 1 220 ? 11.947  -50.852 -15.666 1.00 23.69  ?  220  GLU A HG3    1 
ATOM   3454  N N      . THR A 1 221 ? 9.476   -47.179 -16.046 1.00 14.21  ?  221  THR A N      1 
ATOM   3455  C CA     . THR A 1 221 ? 9.302   -46.442 -17.289 1.00 13.89  ?  221  THR A CA     1 
ATOM   3456  C C      . THR A 1 221 ? 8.644   -45.085 -17.086 1.00 13.20  ?  221  THR A C      1 
ATOM   3457  O O      . THR A 1 221 ? 8.475   -44.353 -18.057 1.00 13.47  ?  221  THR A O      1 
ATOM   3458  C CB     . THR A 1 221 ? 8.472   -47.223 -18.333 1.00 13.55  ?  221  THR A CB     1 
ATOM   3459  O OG1    . THR A 1 221 ? 7.079   -47.265 -17.955 1.00 13.50  ?  221  THR A OG1    1 
ATOM   3460  C CG2    . THR A 1 221 ? 9.019   -48.603 -18.557 1.00 15.91  ?  221  THR A CG2    1 
ATOM   3461  H H      . THR A 1 221 ? 8.751   -47.525 -15.738 1.00 17.05  ?  221  THR A H      1 
ATOM   3462  H HA     . THR A 1 221 ? 10.190  -46.325 -17.660 1.00 16.66  ?  221  THR A HA     1 
ATOM   3463  H HB     . THR A 1 221 ? 8.532   -46.761 -19.183 1.00 16.26  ?  221  THR A HB     1 
ATOM   3464  H HG1    . THR A 1 221 ? 6.997   -47.622 -17.199 1.00 16.20  ?  221  THR A HG1    1 
ATOM   3465  H HG21   . THR A 1 221 ? 8.600   -49.004 -19.334 1.00 19.09  ?  221  THR A HG21   1 
ATOM   3466  H HG22   . THR A 1 221 ? 9.977   -48.561 -18.702 1.00 19.09  ?  221  THR A HG22   1 
ATOM   3467  H HG23   . THR A 1 221 ? 8.843   -49.160 -17.782 1.00 19.09  ?  221  THR A HG23   1 
ATOM   3468  N N      . VAL A 1 222 ? 8.263   -44.724 -15.859 1.00 14.52  ?  222  VAL A N      1 
ATOM   3469  C CA     . VAL A 1 222 ? 7.485   -43.508 -15.610 1.00 13.69  ?  222  VAL A CA     1 
ATOM   3470  C C      . VAL A 1 222 ? 8.386   -42.476 -14.942 1.00 13.48  ?  222  VAL A C      1 
ATOM   3471  O O      . VAL A 1 222 ? 8.879   -42.686 -13.822 1.00 14.03  ?  222  VAL A O      1 
ATOM   3472  C CB     . VAL A 1 222 ? 6.245   -43.791 -14.742 1.00 13.81  ?  222  VAL A CB     1 
ATOM   3473  C CG1    . VAL A 1 222 ? 5.499   -42.518 -14.507 1.00 14.07  ?  222  VAL A CG1    1 
ATOM   3474  C CG2    . VAL A 1 222 ? 5.335   -44.818 -15.420 1.00 15.80  ?  222  VAL A CG2    1 
ATOM   3475  H H      . VAL A 1 222 ? 8.446   -45.173 -15.149 1.00 17.42  ?  222  VAL A H      1 
ATOM   3476  H HA     . VAL A 1 222 ? 7.196   -43.148 -16.463 1.00 16.43  ?  222  VAL A HA     1 
ATOM   3477  H HB     . VAL A 1 222 ? 6.528   -44.157 -13.889 1.00 16.57  ?  222  VAL A HB     1 
ATOM   3478  H HG11   . VAL A 1 222 ? 4.627   -42.726 -14.138 1.00 16.88  ?  222  VAL A HG11   1 
ATOM   3479  H HG12   . VAL A 1 222 ? 6.000   -41.968 -13.884 1.00 16.88  ?  222  VAL A HG12   1 
ATOM   3480  H HG13   . VAL A 1 222 ? 5.397   -42.051 -15.352 1.00 16.88  ?  222  VAL A HG13   1 
ATOM   3481  H HG21   . VAL A 1 222 ? 4.563   -44.978 -14.854 1.00 18.96  ?  222  VAL A HG21   1 
ATOM   3482  H HG22   . VAL A 1 222 ? 5.050   -44.469 -16.278 1.00 18.96  ?  222  VAL A HG22   1 
ATOM   3483  H HG23   . VAL A 1 222 ? 5.829   -45.644 -15.546 1.00 18.96  ?  222  VAL A HG23   1 
ATOM   3484  N N      . ALA A 1 223 ? 8.582   -41.340 -15.618 1.00 12.63  ?  223  ALA A N      1 
ATOM   3485  C CA     . ALA A 1 223 ? 9.508   -40.319 -15.171 1.00 12.99  ?  223  ALA A CA     1 
ATOM   3486  C C      . ALA A 1 223 ? 8.859   -39.197 -14.389 1.00 11.24  ?  223  ALA A C      1 
ATOM   3487  O O      . ALA A 1 223 ? 9.477   -38.665 -13.457 1.00 13.17  ?  223  ALA A O      1 
ATOM   3488  C CB     . ALA A 1 223 ? 10.203  -39.675 -16.376 1.00 14.95  ?  223  ALA A CB     1 
ATOM   3489  H H      . ALA A 1 223 ? 8.177   -41.143 -16.351 1.00 15.15  ?  223  ALA A H      1 
ATOM   3490  H HA     . ALA A 1 223 ? 10.161  -40.755 -14.603 1.00 15.58  ?  223  ALA A HA     1 
ATOM   3491  H HB1    . ALA A 1 223 ? 10.773  -38.955 -16.064 1.00 17.94  ?  223  ALA A HB1    1 
ATOM   3492  H HB2    . ALA A 1 223 ? 10.735  -40.346 -16.829 1.00 17.94  ?  223  ALA A HB2    1 
ATOM   3493  H HB3    . ALA A 1 223 ? 9.529   -39.324 -16.979 1.00 17.94  ?  223  ALA A HB3    1 
ATOM   3494  N N      . ALA A 1 224 ? 7.684   -38.739 -14.809 1.00 12.75  ?  224  ALA A N      1 
ATOM   3495  C CA     . ALA A 1 224 ? 7.162   -37.500 -14.250 1.00 12.24  ?  224  ALA A CA     1 
ATOM   3496  C C      . ALA A 1 224 ? 5.647   -37.445 -14.353 1.00 10.62  ?  224  ALA A C      1 
ATOM   3497  O O      . ALA A 1 224 ? 5.018   -38.143 -15.157 1.00 12.02  ?  224  ALA A O      1 
ATOM   3498  C CB     . ALA A 1 224 ? 7.785   -36.273 -14.922 1.00 12.12  ?  224  ALA A CB     1 
ATOM   3499  H H      . ALA A 1 224 ? 7.185   -39.118 -15.399 1.00 15.30  ?  224  ALA A H      1 
ATOM   3500  H HA     . ALA A 1 224 ? 7.379   -37.493 -13.305 1.00 14.68  ?  224  ALA A HA     1 
ATOM   3501  H HB1    . ALA A 1 224 ? 7.451   -35.472 -14.488 1.00 14.54  ?  224  ALA A HB1    1 
ATOM   3502  H HB2    . ALA A 1 224 ? 8.749   -36.320 -14.833 1.00 14.54  ?  224  ALA A HB2    1 
ATOM   3503  H HB3    . ALA A 1 224 ? 7.539   -36.268 -15.860 1.00 14.54  ?  224  ALA A HB3    1 
ATOM   3504  N N      . PHE A 1 225 ? 5.074   -36.612 -13.498 1.00 11.02  ?  225  PHE A N      1 
ATOM   3505  C CA     . PHE A 1 225 ? 3.654   -36.274 -13.467 1.00 11.39  ?  225  PHE A CA     1 
ATOM   3506  C C      . PHE A 1 225 ? 3.588   -34.753 -13.471 1.00 11.11  ?  225  PHE A C      1 
ATOM   3507  O O      . PHE A 1 225 ? 4.351   -34.097 -12.755 1.00 13.37  ?  225  PHE A O      1 
ATOM   3508  C CB     . PHE A 1 225 ? 3.072   -36.829 -12.169 1.00 12.30  ?  225  PHE A CB     1 
ATOM   3509  C CG     . PHE A 1 225 ? 1.648   -36.422 -11.879 1.00 13.31  ?  225  PHE A CG     1 
ATOM   3510  C CD1    . PHE A 1 225 ? 1.385   -35.239 -11.242 1.00 14.23  ?  225  PHE A CD1    1 
ATOM   3511  C CD2    . PHE A 1 225 ? 0.601   -37.282 -12.142 1.00 16.40  ?  225  PHE A CD2    1 
ATOM   3512  C CE1    . PHE A 1 225 ? 0.092   -34.873 -10.942 1.00 15.40  ?  225  PHE A CE1    1 
ATOM   3513  C CE2    . PHE A 1 225 ? -0.694  -36.935 -11.827 1.00 16.64  ?  225  PHE A CE2    1 
ATOM   3514  C CZ     . PHE A 1 225 ? -0.947  -35.726 -11.214 1.00 16.94  ?  225  PHE A CZ     1 
ATOM   3515  H H      . PHE A 1 225 ? 5.515   -36.202 -12.884 1.00 13.23  ?  225  PHE A H      1 
ATOM   3516  H HA     . PHE A 1 225 ? 3.152   -36.620 -14.221 1.00 13.66  ?  225  PHE A HA     1 
ATOM   3517  H HB2    . PHE A 1 225 ? 3.094   -37.797 -12.212 1.00 14.76  ?  225  PHE A HB2    1 
ATOM   3518  H HB3    . PHE A 1 225 ? 3.618   -36.517 -11.430 1.00 14.76  ?  225  PHE A HB3    1 
ATOM   3519  H HD1    . PHE A 1 225 ? 2.088   -34.676 -11.009 1.00 17.08  ?  225  PHE A HD1    1 
ATOM   3520  H HD2    . PHE A 1 225 ? 0.772   -38.106 -12.538 1.00 19.67  ?  225  PHE A HD2    1 
ATOM   3521  H HE1    . PHE A 1 225 ? -0.078  -34.045 -10.554 1.00 18.48  ?  225  PHE A HE1    1 
ATOM   3522  H HE2    . PHE A 1 225 ? -1.395  -37.513 -12.027 1.00 19.97  ?  225  PHE A HE2    1 
ATOM   3523  H HZ     . PHE A 1 225 ? -1.817  -35.491 -10.986 1.00 20.32  ?  225  PHE A HZ     1 
ATOM   3524  N N      . ILE A 1 226 ? 2.699   -34.192 -14.289 1.00 11.84  ?  226  ILE A N      1 
ATOM   3525  C CA     . ILE A 1 226 ? 2.521   -32.744 -14.368 1.00 10.83  ?  226  ILE A CA     1 
ATOM   3526  C C      . ILE A 1 226 ? 1.078   -32.409 -14.026 1.00 10.27  ?  226  ILE A C      1 
ATOM   3527  O O      . ILE A 1 226 ? 0.150   -33.091 -14.485 1.00 11.87  ?  226  ILE A O      1 
ATOM   3528  C CB     . ILE A 1 226 ? 2.907   -32.177 -15.757 1.00 11.44  ?  226  ILE A CB     1 
ATOM   3529  C CG1    . ILE A 1 226 ? 2.812   -30.651 -15.754 1.00 11.81  ?  226  ILE A CG1    1 
ATOM   3530  C CG2    . ILE A 1 226 ? 2.057   -32.762 -16.905 1.00 11.00  ?  226  ILE A CG2    1 
ATOM   3531  C CD1    . ILE A 1 226 ? 3.390   -29.978 -16.979 1.00 12.32  ?  226  ILE A CD1    1 
ATOM   3532  H H      . ILE A 1 226 ? 2.182   -34.637 -14.812 1.00 14.21  ?  226  ILE A H      1 
ATOM   3533  H HA     . ILE A 1 226 ? 3.095   -32.324 -13.709 1.00 12.99  ?  226  ILE A HA     1 
ATOM   3534  H HB     . ILE A 1 226 ? 3.825   -32.447 -15.918 1.00 13.73  ?  226  ILE A HB     1 
ATOM   3535  H HG12   . ILE A 1 226 ? 1.876   -30.401 -15.698 1.00 14.17  ?  226  ILE A HG12   1 
ATOM   3536  H HG13   . ILE A 1 226 ? 3.292   -30.314 -14.982 1.00 14.17  ?  226  ILE A HG13   1 
ATOM   3537  H HG21   . ILE A 1 226 ? 2.371   -32.399 -17.747 1.00 13.20  ?  226  ILE A HG21   1 
ATOM   3538  H HG22   . ILE A 1 226 ? 2.150   -33.728 -16.906 1.00 13.20  ?  226  ILE A HG22   1 
ATOM   3539  H HG23   . ILE A 1 226 ? 1.128   -32.520 -16.765 1.00 13.20  ?  226  ILE A HG23   1 
ATOM   3540  H HD11   . ILE A 1 226 ? 3.387   -29.017 -16.843 1.00 14.78  ?  226  ILE A HD11   1 
ATOM   3541  H HD12   . ILE A 1 226 ? 4.299   -30.290 -17.112 1.00 14.78  ?  226  ILE A HD12   1 
ATOM   3542  H HD13   . ILE A 1 226 ? 2.846   -30.204 -17.750 1.00 14.78  ?  226  ILE A HD13   1 
ATOM   3543  N N      . GLY A 1 227 ? 0.894   -31.375 -13.223 1.00 10.74  ?  227  GLY A N      1 
ATOM   3544  C CA     . GLY A 1 227 ? -0.432  -30.887 -12.921 1.00 10.76  ?  227  GLY A CA     1 
ATOM   3545  C C      . GLY A 1 227 ? -0.472  -29.436 -12.487 1.00 11.43  ?  227  GLY A C      1 
ATOM   3546  O O      . GLY A 1 227 ? 0.429   -28.956 -11.790 1.00 11.41  ?  227  GLY A O      1 
ATOM   3547  H H      . GLY A 1 227 ? 1.527   -30.938 -12.838 1.00 12.88  ?  227  GLY A H      1 
ATOM   3548  H HA2    . GLY A 1 227 ? -0.987  -30.977 -13.711 1.00 12.91  ?  227  GLY A HA2    1 
ATOM   3549  H HA3    . GLY A 1 227 ? -0.809  -31.423 -12.207 1.00 12.91  ?  227  GLY A HA3    1 
ATOM   3550  N N      . GLU A 1 228 ? -1.539  -28.742 -12.888 1.00 11.02  ?  228  GLU A N      1 
ATOM   3551  C CA     . GLU A 1 228 ? -1.888  -27.463 -12.320 1.00 11.45  ?  228  GLU A CA     1 
ATOM   3552  C C      . GLU A 1 228 ? -2.456  -27.685 -10.921 1.00 12.00  ?  228  GLU A C      1 
ATOM   3553  O O      . GLU A 1 228 ? -3.249  -28.600 -10.711 1.00 12.89  ?  228  GLU A O      1 
ATOM   3554  C CB     . GLU A 1 228 ? -3.003  -26.825 -13.162 1.00 11.64  ?  228  GLU A CB     1 
ATOM   3555  C CG     . GLU A 1 228 ? -2.664  -26.523 -14.616 1.00 11.48  ?  228  GLU A CG     1 
ATOM   3556  C CD     . GLU A 1 228 ? -3.937  -26.469 -15.444 1.00 11.99  ?  228  GLU A CD     1 
ATOM   3557  O OE1    . GLU A 1 228 ? -4.534  -25.378 -15.580 1.00 13.93  ?  228  GLU A OE1    1 
ATOM   3558  O OE2    . GLU A 1 228 ? -4.382  -27.560 -15.918 1.00 12.50  -1 228  GLU A OE2    1 
ATOM   3559  H H      . GLU A 1 228 ? -2.084  -29.002 -13.501 1.00 13.22  ?  228  GLU A H      1 
ATOM   3560  H HA     . GLU A 1 228 ? -1.110  -26.885 -12.288 1.00 13.74  ?  228  GLU A HA     1 
ATOM   3561  H HB2    . GLU A 1 228 ? -3.761  -27.431 -13.167 1.00 13.96  ?  228  GLU A HB2    1 
ATOM   3562  H HB3    . GLU A 1 228 ? -3.252  -25.985 -12.747 1.00 13.96  ?  228  GLU A HB3    1 
ATOM   3563  H HG2    . GLU A 1 228 ? -2.217  -25.664 -14.675 1.00 13.77  ?  228  GLU A HG2    1 
ATOM   3564  H HG3    . GLU A 1 228 ? -2.090  -27.220 -14.970 1.00 13.77  ?  228  GLU A HG3    1 
ATOM   3565  N N      . PRO A 1 229 ? -2.140  -26.824 -9.960  1.00 11.39  ?  229  PRO A N      1 
ATOM   3566  C CA     . PRO A 1 229 ? -2.763  -26.997 -8.640  1.00 10.90  ?  229  PRO A CA     1 
ATOM   3567  C C      . PRO A 1 229 ? -4.271  -26.978 -8.706  1.00 11.06  ?  229  PRO A C      1 
ATOM   3568  O O      . PRO A 1 229 ? -4.936  -27.796 -8.058  1.00 12.06  ?  229  PRO A O      1 
ATOM   3569  C CB     . PRO A 1 229 ? -2.183  -25.834 -7.836  1.00 11.57  ?  229  PRO A CB     1 
ATOM   3570  C CG     . PRO A 1 229 ? -0.819  -25.650 -8.443  1.00 11.77  ?  229  PRO A CG     1 
ATOM   3571  C CD     . PRO A 1 229 ? -1.088  -25.802 -9.936  1.00 11.70  ?  229  PRO A CD     1 
ATOM   3572  H HA     . PRO A 1 229 ? -2.477  -27.826 -8.227  1.00 13.07  ?  229  PRO A HA     1 
ATOM   3573  H HB2    . PRO A 1 229 ? -2.730  -25.040 -7.946  1.00 13.88  ?  229  PRO A HB2    1 
ATOM   3574  H HB3    . PRO A 1 229 ? -2.124  -26.068 -6.897  1.00 13.88  ?  229  PRO A HB3    1 
ATOM   3575  H HG2    . PRO A 1 229 ? -0.470  -24.769 -8.234  1.00 14.13  ?  229  PRO A HG2    1 
ATOM   3576  H HG3    . PRO A 1 229 ? -0.210  -26.333 -8.122  1.00 14.13  ?  229  PRO A HG3    1 
ATOM   3577  H HD2    . PRO A 1 229 ? -1.402  -24.969 -10.321 1.00 14.03  ?  229  PRO A HD2    1 
ATOM   3578  H HD3    . PRO A 1 229 ? -0.295  -26.107 -10.405 1.00 14.03  ?  229  PRO A HD3    1 
ATOM   3579  N N      . VAL A 1 230 ? -4.804  -26.027 -9.471  1.00 11.93  ?  230  VAL A N      1 
ATOM   3580  C CA     . VAL A 1 230 ? -6.217  -25.839 -9.774  1.00 12.63  ?  230  VAL A CA     1 
ATOM   3581  C C      . VAL A 1 230 ? -6.341  -25.899 -11.293 1.00 11.83  ?  230  VAL A C      1 
ATOM   3582  O O      . VAL A 1 230 ? -5.543  -25.276 -11.991 1.00 12.68  ?  230  VAL A O      1 
ATOM   3583  C CB     . VAL A 1 230 ? -6.667  -24.441 -9.307  1.00 12.02  ?  230  VAL A CB     1 
ATOM   3584  C CG1    . VAL A 1 230 ? -8.126  -24.155 -9.702  1.00 13.88  ?  230  VAL A CG1    1 
ATOM   3585  C CG2    . VAL A 1 230 ? -6.424  -24.241 -7.817  1.00 12.71  ?  230  VAL A CG2    1 
ATOM   3586  H H      . VAL A 1 230 ? -4.322  -25.428 -9.857  1.00 14.31  ?  230  VAL A H      1 
ATOM   3587  H HA     . VAL A 1 230 ? -6.757  -26.528 -9.358  1.00 15.15  ?  230  VAL A HA     1 
ATOM   3588  H HB     . VAL A 1 230 ? -6.121  -23.783 -9.767  1.00 14.42  ?  230  VAL A HB     1 
ATOM   3589  H HG11   . VAL A 1 230 ? -8.410  -23.327 -9.283  1.00 16.65  ?  230  VAL A HG11   1 
ATOM   3590  H HG12   . VAL A 1 230 ? -8.182  -24.074 -10.667 1.00 16.65  ?  230  VAL A HG12   1 
ATOM   3591  H HG13   . VAL A 1 230 ? -8.685  -24.888 -9.398  1.00 16.65  ?  230  VAL A HG13   1 
ATOM   3592  H HG21   . VAL A 1 230 ? -6.704  -23.346 -7.568  1.00 15.25  ?  230  VAL A HG21   1 
ATOM   3593  H HG22   . VAL A 1 230 ? -6.939  -24.898 -7.323  1.00 15.25  ?  230  VAL A HG22   1 
ATOM   3594  H HG23   . VAL A 1 230 ? -5.479  -24.355 -7.633  1.00 15.25  ?  230  VAL A HG23   1 
ATOM   3595  N N      . LEU A 1 231 ? -7.313  -26.656 -11.815 1.00 13.04  ?  231  LEU A N      1 
ATOM   3596  C CA     . LEU A 1 231 ? -7.493  -26.639 -13.267 1.00 12.15  ?  231  LEU A CA     1 
ATOM   3597  C C      . LEU A 1 231 ? -7.917  -25.250 -13.720 1.00 12.41  ?  231  LEU A C      1 
ATOM   3598  O O      . LEU A 1 231 ? -8.870  -24.687 -13.187 1.00 13.57  ?  231  LEU A O      1 
ATOM   3599  C CB     . LEU A 1 231 ? -8.566  -27.617 -13.716 1.00 13.75  ?  231  LEU A CB     1 
ATOM   3600  C CG     . LEU A 1 231 ? -8.339  -29.108 -13.495 1.00 13.60  ?  231  LEU A CG     1 
ATOM   3601  C CD1    . LEU A 1 231 ? -9.491  -29.858 -14.145 1.00 13.55  ?  231  LEU A CD1    1 
ATOM   3602  C CD2    . LEU A 1 231 ? -7.019  -29.550 -14.053 1.00 14.05  ?  231  LEU A CD2    1 
ATOM   3603  H H      . LEU A 1 231 ? -7.852  -27.160 -11.373 1.00 15.64  ?  231  LEU A H      1 
ATOM   3604  H HA     . LEU A 1 231 ? -6.649  -26.896 -13.670 1.00 14.58  ?  231  LEU A HA     1 
ATOM   3605  H HB2    . LEU A 1 231 ? -9.382  -27.391 -13.244 1.00 16.50  ?  231  LEU A HB2    1 
ATOM   3606  H HB3    . LEU A 1 231 ? -8.689  -27.496 -14.670 1.00 16.50  ?  231  LEU A HB3    1 
ATOM   3607  H HG     . LEU A 1 231 ? -8.311  -29.308 -12.546 1.00 16.32  ?  231  LEU A HG     1 
ATOM   3608  H HD11   . LEU A 1 231 ? -9.316  -30.810 -14.093 1.00 16.25  ?  231  LEU A HD11   1 
ATOM   3609  H HD12   . LEU A 1 231 ? -10.312 -29.646 -13.673 1.00 16.25  ?  231  LEU A HD12   1 
ATOM   3610  H HD13   . LEU A 1 231 ? -9.562  -29.584 -15.073 1.00 16.25  ?  231  LEU A HD13   1 
ATOM   3611  H HD21   . LEU A 1 231 ? -6.960  -30.517 -13.995 1.00 16.85  ?  231  LEU A HD21   1 
ATOM   3612  H HD22   . LEU A 1 231 ? -6.958  -29.269 -14.979 1.00 16.85  ?  231  LEU A HD22   1 
ATOM   3613  H HD23   . LEU A 1 231 ? -6.306  -29.144 -13.536 1.00 16.85  ?  231  LEU A HD23   1 
ATOM   3614  N N      . GLY A 1 232 ? -7.219  -24.721 -14.727 1.00 12.55  ?  232  GLY A N      1 
ATOM   3615  C CA     . GLY A 1 232 ? -7.609  -23.459 -15.327 1.00 12.78  ?  232  GLY A CA     1 
ATOM   3616  C C      . GLY A 1 232 ? -8.527  -23.653 -16.508 1.00 13.06  ?  232  GLY A C      1 
ATOM   3617  O O      . GLY A 1 232 ? -9.746  -23.754 -16.350 1.00 12.55  ?  232  GLY A O      1 
ATOM   3618  H H      . GLY A 1 232 ? -6.518  -25.077 -15.075 1.00 15.05  ?  232  GLY A H      1 
ATOM   3619  H HA2    . GLY A 1 232 ? -8.068  -22.916 -14.667 1.00 15.33  ?  232  GLY A HA2    1 
ATOM   3620  H HA3    . GLY A 1 232 ? -6.817  -22.987 -15.628 1.00 15.33  ?  232  GLY A HA3    1 
ATOM   3621  N N      . THR A 1 233 ? -7.936  -23.761 -17.699 1.00 12.12  ?  233  THR A N      1 
ATOM   3622  C CA     . THR A 1 233 ? -8.723  -23.836 -18.927 1.00 13.27  ?  233  THR A CA     1 
ATOM   3623  C C      . THR A 1 233 ? -9.634  -25.057 -18.945 1.00 13.56  ?  233  THR A C      1 
ATOM   3624  O O      . THR A 1 233 ? -10.692 -25.031 -19.595 1.00 15.64  ?  233  THR A O      1 
ATOM   3625  C CB     . THR A 1 233 ? -7.761  -23.789 -20.113 1.00 14.56  ?  233  THR A CB     1 
ATOM   3626  O OG1    . THR A 1 233 ? -7.117  -22.496 -20.107 1.00 16.75  ?  233  THR A OG1    1 
ATOM   3627  C CG2    . THR A 1 233 ? -8.459  -23.998 -21.457 1.00 14.80  ?  233  THR A CG2    1 
ATOM   3628  H H      . THR A 1 233 ? -7.086  -23.791 -17.824 1.00 14.54  ?  233  THR A H      1 
ATOM   3629  H HA     . THR A 1 233 ? -9.318  -23.075 -19.002 1.00 15.92  ?  233  THR A HA     1 
ATOM   3630  H HB     . THR A 1 233 ? -7.118  -24.510 -20.027 1.00 17.47  ?  233  THR A HB     1 
ATOM   3631  H HG1    . THR A 1 233 ? -7.695  -21.888 -20.064 1.00 20.10  ?  233  THR A HG1    1 
ATOM   3632  H HG21   . THR A 1 233 ? -7.846  -23.805 -22.183 1.00 17.76  ?  233  THR A HG21   1 
ATOM   3633  H HG22   . THR A 1 233 ? -8.760  -24.917 -21.535 1.00 17.76  ?  233  THR A HG22   1 
ATOM   3634  H HG23   . THR A 1 233 ? -9.226  -23.409 -21.528 1.00 17.76  ?  233  THR A HG23   1 
ATOM   3635  N N      . GLY A 1 234 ? -9.254  -26.123 -18.233 1.00 13.43  ?  234  GLY A N      1 
ATOM   3636  C CA     . GLY A 1 234 ? -10.068 -27.310 -18.076 1.00 13.17  ?  234  GLY A CA     1 
ATOM   3637  C C      . GLY A 1 234 ? -11.301 -27.162 -17.218 1.00 12.75  ?  234  GLY A C      1 
ATOM   3638  O O      . GLY A 1 234 ? -12.024 -28.148 -17.049 1.00 13.12  ?  234  GLY A O      1 
ATOM   3639  H H      . GLY A 1 234 ? -8.501  -26.177 -17.821 1.00 16.11  ?  234  GLY A H      1 
ATOM   3640  H HA2    . GLY A 1 234 ? -10.358 -27.600 -18.955 1.00 15.80  ?  234  GLY A HA2    1 
ATOM   3641  H HA3    . GLY A 1 234 ? -9.520  -28.006 -17.679 1.00 15.80  ?  234  GLY A HA3    1 
ATOM   3642  N N      . GLY A 1 235 ? -11.548 -25.986 -16.634 1.00 12.50  ?  235  GLY A N      1 
ATOM   3643  C CA     . GLY A 1 235 ? -12.832 -25.735 -15.992 1.00 11.86  ?  235  GLY A CA     1 
ATOM   3644  C C      . GLY A 1 235 ? -12.856 -24.877 -14.733 1.00 13.91  ?  235  GLY A C      1 
ATOM   3645  O O      . GLY A 1 235 ? -13.928 -24.692 -14.154 1.00 14.19  ?  235  GLY A O      1 
ATOM   3646  H H      . GLY A 1 235 ? -10.994 -25.330 -16.598 1.00 15.00  ?  235  GLY A H      1 
ATOM   3647  H HA2    . GLY A 1 235 ? -13.408 -25.299 -16.639 1.00 14.23  ?  235  GLY A HA2    1 
ATOM   3648  H HA3    . GLY A 1 235 ? -13.219 -26.593 -15.754 1.00 14.23  ?  235  GLY A HA3    1 
ATOM   3649  N N      . ILE A 1 236 ? -11.710 -24.337 -14.313 1.00 14.40  ?  236  ILE A N      1 
ATOM   3650  C CA     . ILE A 1 236 ? -11.586 -23.593 -13.047 1.00 13.78  ?  236  ILE A CA     1 
ATOM   3651  C C      . ILE A 1 236 ? -12.069 -24.497 -11.919 1.00 12.45  ?  236  ILE A C      1 
ATOM   3652  O O      . ILE A 1 236 ? -13.143 -24.305 -11.322 1.00 12.78  ?  236  ILE A O      1 
ATOM   3653  C CB     . ILE A 1 236 ? -12.264 -22.216 -13.135 1.00 14.05  ?  236  ILE A CB     1 
ATOM   3654  C CG1    . ILE A 1 236 ? -11.467 -21.384 -14.165 1.00 17.93  ?  236  ILE A CG1    1 
ATOM   3655  C CG2    . ILE A 1 236 ? -12.253 -21.485 -11.786 1.00 15.19  ?  236  ILE A CG2    1 
ATOM   3656  C CD1    . ILE A 1 236 ? -12.028 -20.045 -14.461 1.00 20.04  ?  236  ILE A CD1    1 
ATOM   3657  H H      . ILE A 1 236 ? -10.971 -24.387 -14.750 1.00 17.28  ?  236  ILE A H      1 
ATOM   3658  H HA     . ILE A 1 236 ? -10.660 -23.389 -12.844 1.00 16.53  ?  236  ILE A HA     1 
ATOM   3659  H HB     . ILE A 1 236 ? -13.191 -22.333 -13.396 1.00 16.86  ?  236  ILE A HB     1 
ATOM   3660  H HG12   . ILE A 1 236 ? -10.568 -21.254 -13.825 1.00 21.51  ?  236  ILE A HG12   1 
ATOM   3661  H HG13   . ILE A 1 236 ? -11.437 -21.877 -15.000 1.00 21.51  ?  236  ILE A HG13   1 
ATOM   3662  H HG21   . ILE A 1 236 ? -12.639 -20.602 -11.902 1.00 18.22  ?  236  ILE A HG21   1 
ATOM   3663  H HG22   . ILE A 1 236 ? -12.776 -21.993 -11.147 1.00 18.22  ?  236  ILE A HG22   1 
ATOM   3664  H HG23   . ILE A 1 236 ? -11.337 -21.407 -11.476 1.00 18.22  ?  236  ILE A HG23   1 
ATOM   3665  H HD11   . ILE A 1 236 ? -11.575 -19.678 -15.236 1.00 24.05  ?  236  ILE A HD11   1 
ATOM   3666  H HD12   . ILE A 1 236 ? -12.977 -20.133 -14.643 1.00 24.05  ?  236  ILE A HD12   1 
ATOM   3667  H HD13   . ILE A 1 236 ? -11.890 -19.469 -13.693 1.00 24.05  ?  236  ILE A HD13   1 
ATOM   3668  N N      . VAL A 1 237 ? -11.251 -25.504 -11.624 1.00 12.82  ?  237  VAL A N      1 
ATOM   3669  C CA     . VAL A 1 237 ? -11.651 -26.608 -10.758 1.00 11.52  ?  237  VAL A CA     1 
ATOM   3670  C C      . VAL A 1 237 ? -10.634 -26.725 -9.623  1.00 11.59  ?  237  VAL A C      1 
ATOM   3671  O O      . VAL A 1 237 ? -9.547  -27.295 -9.825  1.00 12.89  ?  237  VAL A O      1 
ATOM   3672  C CB     . VAL A 1 237 ? -11.754 -27.933 -11.533 1.00 12.88  ?  237  VAL A CB     1 
ATOM   3673  C CG1    . VAL A 1 237 ? -12.357 -29.008 -10.631 1.00 14.36  ?  237  VAL A CG1    1 
ATOM   3674  C CG2    . VAL A 1 237 ? -12.573 -27.786 -12.804 1.00 14.32  ?  237  VAL A CG2    1 
ATOM   3675  H H      . VAL A 1 237 ? -10.446 -25.571 -11.919 1.00 15.38  ?  237  VAL A H      1 
ATOM   3676  H HA     . VAL A 1 237 ? -12.524 -26.411 -10.383 1.00 13.82  ?  237  VAL A HA     1 
ATOM   3677  H HB     . VAL A 1 237 ? -10.861 -28.201 -11.802 1.00 15.46  ?  237  VAL A HB     1 
ATOM   3678  H HG11   . VAL A 1 237 ? -12.506 -29.812 -11.153 1.00 17.23  ?  237  VAL A HG11   1 
ATOM   3679  H HG12   . VAL A 1 237 ? -11.739 -29.194 -9.906  1.00 17.23  ?  237  VAL A HG12   1 
ATOM   3680  H HG13   . VAL A 1 237 ? -13.198 -28.685 -10.273 1.00 17.23  ?  237  VAL A HG13   1 
ATOM   3681  H HG21   . VAL A 1 237 ? -12.702 -28.663 -13.200 1.00 17.18  ?  237  VAL A HG21   1 
ATOM   3682  H HG22   . VAL A 1 237 ? -13.432 -27.393 -12.583 1.00 17.18  ?  237  VAL A HG22   1 
ATOM   3683  H HG23   . VAL A 1 237 ? -12.096 -27.212 -13.423 1.00 17.18  ?  237  VAL A HG23   1 
ATOM   3684  N N      . PRO A 1 238 ? -10.934 -26.226 -8.426  1.00 13.44  ?  238  PRO A N      1 
ATOM   3685  C CA     . PRO A 1 238 ? -10.067 -26.502 -7.286  1.00 14.60  ?  238  PRO A CA     1 
ATOM   3686  C C      . PRO A 1 238 ? -9.995  -27.999 -7.035  1.00 13.98  ?  238  PRO A C      1 
ATOM   3687  O O      . PRO A 1 238 ? -10.961 -28.735 -7.307  1.00 13.92  ?  238  PRO A O      1 
ATOM   3688  C CB     . PRO A 1 238 ? -10.770 -25.777 -6.127  1.00 13.63  ?  238  PRO A CB     1 
ATOM   3689  C CG     . PRO A 1 238 ? -11.633 -24.726 -6.817  1.00 13.22  ?  238  PRO A CG     1 
ATOM   3690  C CD     . PRO A 1 238 ? -12.108 -25.418 -8.062  1.00 13.71  ?  238  PRO A CD     1 
ATOM   3691  H HA     . PRO A 1 238 ? -9.178  -26.137 -7.420  1.00 17.52  ?  238  PRO A HA     1 
ATOM   3692  H HB2    . PRO A 1 238 ? -11.314 -26.402 -5.623  1.00 16.35  ?  238  PRO A HB2    1 
ATOM   3693  H HB3    . PRO A 1 238 ? -10.113 -25.364 -5.545  1.00 16.35  ?  238  PRO A HB3    1 
ATOM   3694  H HG2    . PRO A 1 238 ? -12.378 -24.477 -6.247  1.00 15.86  ?  238  PRO A HG2    1 
ATOM   3695  H HG3    . PRO A 1 238 ? -11.102 -23.943 -7.031  1.00 15.86  ?  238  PRO A HG3    1 
ATOM   3696  H HD2    . PRO A 1 238 ? -12.877 -25.980 -7.879  1.00 16.45  ?  238  PRO A HD2    1 
ATOM   3697  H HD3    . PRO A 1 238 ? -12.324 -24.778 -8.758  1.00 16.45  ?  238  PRO A HD3    1 
ATOM   3698  N N      . PRO A 1 239 ? -8.873  -28.486 -6.502  1.00 13.10  ?  239  PRO A N      1 
ATOM   3699  C CA     . PRO A 1 239 ? -8.738  -29.930 -6.307  1.00 14.46  ?  239  PRO A CA     1 
ATOM   3700  C C      . PRO A 1 239 ? -9.669  -30.424 -5.197  1.00 13.72  ?  239  PRO A C      1 
ATOM   3701  O O      . PRO A 1 239 ? -9.976  -29.679 -4.258  1.00 16.35  ?  239  PRO A O      1 
ATOM   3702  C CB     . PRO A 1 239 ? -7.260  -30.103 -5.906  1.00 14.70  ?  239  PRO A CB     1 
ATOM   3703  C CG     . PRO A 1 239 ? -6.901  -28.807 -5.286  1.00 14.44  ?  239  PRO A CG     1 
ATOM   3704  C CD     . PRO A 1 239 ? -7.686  -27.750 -6.034  1.00 13.96  ?  239  PRO A CD     1 
ATOM   3705  H HA     . PRO A 1 239 ? -8.921  -30.406 -7.132  1.00 17.35  ?  239  PRO A HA     1 
ATOM   3706  H HB2    . PRO A 1 239 ? -7.168  -30.832 -5.272  1.00 17.64  ?  239  PRO A HB2    1 
ATOM   3707  H HB3    . PRO A 1 239 ? -6.719  -30.277 -6.692  1.00 17.64  ?  239  PRO A HB3    1 
ATOM   3708  H HG2    . PRO A 1 239 ? -7.147  -28.815 -4.348  1.00 17.33  ?  239  PRO A HG2    1 
ATOM   3709  H HG3    . PRO A 1 239 ? -5.948  -28.654 -5.378  1.00 17.33  ?  239  PRO A HG3    1 
ATOM   3710  H HD2    . PRO A 1 239 ? -7.939  -27.024 -5.443  1.00 16.75  ?  239  PRO A HD2    1 
ATOM   3711  H HD3    . PRO A 1 239 ? -7.175  -27.405 -6.783  1.00 16.75  ?  239  PRO A HD3    1 
ATOM   3712  N N      . PRO A 1 240 ? -10.132 -31.664 -5.297  1.00 13.19  ?  240  PRO A N      1 
ATOM   3713  C CA     . PRO A 1 240 ? -10.983 -32.220 -4.232  1.00 14.05  ?  240  PRO A CA     1 
ATOM   3714  C C      . PRO A 1 240 ? -10.184 -32.435 -2.953  1.00 12.27  ?  240  PRO A C      1 
ATOM   3715  O O      . PRO A 1 240 ? -8.967  -32.601 -2.972  1.00 14.62  ?  240  PRO A O      1 
ATOM   3716  C CB     . PRO A 1 240 ? -11.471 -33.550 -4.827  1.00 15.28  ?  240  PRO A CB     1 
ATOM   3717  C CG     . PRO A 1 240 ? -10.407 -33.926 -5.831  1.00 13.51  ?  240  PRO A CG     1 
ATOM   3718  C CD     . PRO A 1 240 ? -9.819  -32.643 -6.350  1.00 13.80  ?  240  PRO A CD     1 
ATOM   3719  H HA     . PRO A 1 240 ? -11.746 -31.649 -4.051  1.00 16.86  ?  240  PRO A HA     1 
ATOM   3720  H HB2    . PRO A 1 240 ? -11.544 -34.219 -4.128  1.00 18.33  ?  240  PRO A HB2    1 
ATOM   3721  H HB3    . PRO A 1 240 ? -12.331 -33.426 -5.258  1.00 18.33  ?  240  PRO A HB3    1 
ATOM   3722  H HG2    . PRO A 1 240 ? -9.725  -34.460 -5.394  1.00 16.21  ?  240  PRO A HG2    1 
ATOM   3723  H HG3    . PRO A 1 240 ? -10.810 -34.432 -6.554  1.00 16.21  ?  240  PRO A HG3    1 
ATOM   3724  H HD2    . PRO A 1 240 ? -8.860  -32.727 -6.467  1.00 16.56  ?  240  PRO A HD2    1 
ATOM   3725  H HD3    . PRO A 1 240 ? -10.234 -32.390 -7.189  1.00 16.56  ?  240  PRO A HD3    1 
ATOM   3726  N N      . GLU A 1 241 ? -10.902 -32.436 -1.826  1.00 14.82  ?  241  GLU A N      1 
ATOM   3727  C CA     . GLU A 1 241 ? -10.272 -32.601 -0.523  1.00 14.97  ?  241  GLU A CA     1 
ATOM   3728  C C      . GLU A 1 241 ? -9.374  -33.840 -0.504  1.00 15.31  ?  241  GLU A C      1 
ATOM   3729  O O      . GLU A 1 241 ? -9.798  -34.933 -0.883  1.00 15.11  ?  241  GLU A O      1 
ATOM   3730  C CB     . GLU A 1 241 ? -11.356 -32.742 0.562   1.00 16.02  ?  241  GLU A CB     1 
ATOM   3731  C CG     . GLU A 1 241 ? -10.811 -32.673 1.960   1.00 17.85  ?  241  GLU A CG     1 
ATOM   3732  C CD     . GLU A 1 241 ? -11.881 -32.525 3.015   1.00 19.82  ?  241  GLU A CD     1 
ATOM   3733  O OE1    . GLU A 1 241 ? -11.615 -31.872 4.055   1.00 21.69  ?  241  GLU A OE1    1 
ATOM   3734  O OE2    . GLU A 1 241 ? -13.002 -33.042 2.785   1.00 21.28  -1 241  GLU A OE2    1 
ATOM   3735  H H      . GLU A 1 241 ? -11.757 -32.342 -1.792  1.00 17.78  ?  241  GLU A H      1 
ATOM   3736  H HA     . GLU A 1 241 ? -9.728  -31.820 -0.334  1.00 17.96  ?  241  GLU A HA     1 
ATOM   3737  H HB2    . GLU A 1 241 ? -11.999 -32.024 0.457   1.00 19.23  ?  241  GLU A HB2    1 
ATOM   3738  H HB3    . GLU A 1 241 ? -11.796 -33.600 0.456   1.00 19.23  ?  241  GLU A HB3    1 
ATOM   3739  H HG2    . GLU A 1 241 ? -10.322 -33.490 2.147   1.00 21.42  ?  241  GLU A HG2    1 
ATOM   3740  H HG3    . GLU A 1 241 ? -10.219 -31.909 2.029   1.00 21.42  ?  241  GLU A HG3    1 
ATOM   3741  N N      . GLY A 1 242 ? -8.140  -33.668 -0.028  1.00 15.09  ?  242  GLY A N      1 
ATOM   3742  C CA     . GLY A 1 242 ? -7.199  -34.754 0.095   1.00 15.18  ?  242  GLY A CA     1 
ATOM   3743  C C      . GLY A 1 242 ? -6.408  -35.088 -1.146  1.00 14.74  ?  242  GLY A C      1 
ATOM   3744  O O      . GLY A 1 242 ? -5.507  -35.941 -1.074  1.00 14.38  ?  242  GLY A O      1 
ATOM   3745  H H      . GLY A 1 242 ? -7.828  -32.911 0.233   1.00 18.11  ?  242  GLY A H      1 
ATOM   3746  H HA2    . GLY A 1 242 ? -6.563  -34.531 0.794   1.00 18.22  ?  242  GLY A HA2    1 
ATOM   3747  H HA3    . GLY A 1 242 ? -7.685  -35.553 0.354   1.00 18.22  ?  242  GLY A HA3    1 
ATOM   3748  N N      . TYR A 1 243 ? -6.682  -34.418 -2.262  1.00 13.85  ?  243  TYR A N      1 
ATOM   3749  C CA     . TYR A 1 243 ? -6.137  -34.836 -3.550  1.00 12.87  ?  243  TYR A CA     1 
ATOM   3750  C C      . TYR A 1 243 ? -4.616  -34.763 -3.583  1.00 12.08  ?  243  TYR A C      1 
ATOM   3751  O O      . TYR A 1 243 ? -3.944  -35.750 -3.898  1.00 13.83  ?  243  TYR A O      1 
ATOM   3752  C CB     . TYR A 1 243 ? -6.708  -33.962 -4.663  1.00 13.93  ?  243  TYR A CB     1 
ATOM   3753  C CG     . TYR A 1 243 ? -6.180  -34.302 -6.049  1.00 13.32  ?  243  TYR A CG     1 
ATOM   3754  C CD1    . TYR A 1 243 ? -6.756  -35.322 -6.799  1.00 13.96  ?  243  TYR A CD1    1 
ATOM   3755  C CD2    . TYR A 1 243 ? -5.116  -33.606 -6.597  1.00 12.77  ?  243  TYR A CD2    1 
ATOM   3756  C CE1    . TYR A 1 243 ? -6.278  -35.644 -8.102  1.00 13.56  ?  243  TYR A CE1    1 
ATOM   3757  C CE2    . TYR A 1 243 ? -4.634  -33.908 -7.851  1.00 13.20  ?  243  TYR A CE2    1 
ATOM   3758  C CZ     . TYR A 1 243 ? -5.205  -34.935 -8.591  1.00 13.43  ?  243  TYR A CZ     1 
ATOM   3759  O OH     . TYR A 1 243 ? -4.668  -35.190 -9.829  1.00 12.70  ?  243  TYR A OH     1 
ATOM   3760  H H      . TYR A 1 243 ? -7.180  -33.718 -2.303  1.00 16.61  ?  243  TYR A H      1 
ATOM   3761  H HA     . TYR A 1 243 ? -6.400  -35.759 -3.692  1.00 15.44  ?  243  TYR A HA     1 
ATOM   3762  H HB2    . TYR A 1 243 ? -7.672  -34.070 -4.680  1.00 16.71  ?  243  TYR A HB2    1 
ATOM   3763  H HB3    . TYR A 1 243 ? -6.481  -33.037 -4.480  1.00 16.71  ?  243  TYR A HB3    1 
ATOM   3764  H HD1    . TYR A 1 243 ? -7.467  -35.804 -6.442  1.00 16.75  ?  243  TYR A HD1    1 
ATOM   3765  H HD2    . TYR A 1 243 ? -4.719  -32.921 -6.108  1.00 15.31  ?  243  TYR A HD2    1 
ATOM   3766  H HE1    . TYR A 1 243 ? -6.679  -36.314 -8.607  1.00 16.27  ?  243  TYR A HE1    1 
ATOM   3767  H HE2    . TYR A 1 243 ? -3.923  -33.422 -8.204  1.00 15.84  ?  243  TYR A HE2    1 
ATOM   3768  H HH     . TYR A 1 243 ? -5.177  -35.696 -10.264 1.00 15.23  ?  243  TYR A HH     1 
ATOM   3769  N N      . TRP A 1 244 ? -4.051  -33.599 -3.289  1.00 12.35  ?  244  TRP A N      1 
ATOM   3770  C CA     . TRP A 1 244 ? -2.617  -33.416 -3.488  1.00 12.41  ?  244  TRP A CA     1 
ATOM   3771  C C      . TRP A 1 244 ? -1.801  -34.269 -2.535  1.00 12.62  ?  244  TRP A C      1 
ATOM   3772  O O      . TRP A 1 244 ? -0.712  -34.734 -2.897  1.00 12.49  ?  244  TRP A O      1 
ATOM   3773  C CB     . TRP A 1 244 ? -2.241  -31.932 -3.458  1.00 13.29  ?  244  TRP A CB     1 
ATOM   3774  C CG     . TRP A 1 244 ? -2.577  -31.297 -4.758  1.00 13.63  ?  244  TRP A CG     1 
ATOM   3775  C CD1    . TRP A 1 244 ? -3.563  -30.373 -5.004  1.00 13.77  ?  244  TRP A CD1    1 
ATOM   3776  C CD2    . TRP A 1 244 ? -1.969  -31.589 -6.016  1.00 12.19  ?  244  TRP A CD2    1 
ATOM   3777  N NE1    . TRP A 1 244 ? -3.591  -30.063 -6.348  1.00 12.17  ?  244  TRP A NE1    1 
ATOM   3778  C CE2    . TRP A 1 244 ? -2.611  -30.784 -6.984  1.00 11.81  ?  244  TRP A CE2    1 
ATOM   3779  C CE3    . TRP A 1 244 ? -0.930  -32.432 -6.418  1.00 14.03  ?  244  TRP A CE3    1 
ATOM   3780  C CZ2    . TRP A 1 244 ? -2.262  -30.818 -8.328  1.00 12.67  ?  244  TRP A CZ2    1 
ATOM   3781  C CZ3    . TRP A 1 244 ? -0.580  -32.458 -7.763  1.00 13.86  ?  244  TRP A CZ3    1 
ATOM   3782  C CH2    . TRP A 1 244 ? -1.244  -31.658 -8.694  1.00 11.95  ?  244  TRP A CH2    1 
ATOM   3783  H H      . TRP A 1 244 ? -4.462  -32.911 -2.978  1.00 14.82  ?  244  TRP A H      1 
ATOM   3784  H HA     . TRP A 1 244 ? -2.378  -33.714 -4.380  1.00 14.89  ?  244  TRP A HA     1 
ATOM   3785  H HB2    . TRP A 1 244 ? -2.737  -31.484 -2.755  1.00 15.94  ?  244  TRP A HB2    1 
ATOM   3786  H HB3    . TRP A 1 244 ? -1.288  -31.839 -3.302  1.00 15.94  ?  244  TRP A HB3    1 
ATOM   3787  H HD1    . TRP A 1 244 ? -4.128  -30.011 -4.361  1.00 16.52  ?  244  TRP A HD1    1 
ATOM   3788  H HE1    . TRP A 1 244 ? -4.131  -29.511 -6.725  1.00 14.60  ?  244  TRP A HE1    1 
ATOM   3789  H HE3    . TRP A 1 244 ? -0.483  -32.964 -5.800  1.00 16.83  ?  244  TRP A HE3    1 
ATOM   3790  H HZ2    . TRP A 1 244 ? -2.702  -30.291 -8.955  1.00 15.20  ?  244  TRP A HZ2    1 
ATOM   3791  H HZ3    . TRP A 1 244 ? 0.107   -33.016 -8.046  1.00 16.62  ?  244  TRP A HZ3    1 
ATOM   3792  H HH2    . TRP A 1 244 ? -0.988  -31.696 -9.587  1.00 14.33  ?  244  TRP A HH2    1 
ATOM   3793  N N      . GLU A 1 245 ? -2.317  -34.525 -1.336  1.00 13.52  ?  245  GLU A N      1 
ATOM   3794  C CA     . GLU A 1 245 ? -1.584  -35.399 -0.421  1.00 14.06  ?  245  GLU A CA     1 
ATOM   3795  C C      . GLU A 1 245 ? -1.582  -36.830 -0.933  1.00 14.65  ?  245  GLU A C      1 
ATOM   3796  O O      . GLU A 1 245 ? -0.554  -37.516 -0.907  1.00 15.24  ?  245  GLU A O      1 
ATOM   3797  C CB     . GLU A 1 245 ? -2.214  -35.319 0.965   1.00 16.38  ?  245  GLU A CB     1 
ATOM   3798  C CG     . GLU A 1 245 ? -1.600  -36.251 1.991   1.00 21.17  ?  245  GLU A CG     1 
ATOM   3799  C CD     . GLU A 1 245 ? -2.292  -36.184 3.324   1.00 31.75  ?  245  GLU A CD     1 
ATOM   3800  O OE1    . GLU A 1 245 ? -3.532  -36.011 3.365   1.00 36.26  ?  245  GLU A OE1    1 
ATOM   3801  O OE2    . GLU A 1 245 ? -1.607  -36.317 4.344   1.00 37.83  -1 245  GLU A OE2    1 
ATOM   3802  H H      . GLU A 1 245 ? -3.062  -34.219 -1.035  1.00 16.22  ?  245  GLU A H      1 
ATOM   3803  H HA     . GLU A 1 245 ? -0.662  -35.105 -0.352  1.00 16.87  ?  245  GLU A HA     1 
ATOM   3804  H HB2    . GLU A 1 245 ? -2.116  -34.413 1.296   1.00 19.65  ?  245  GLU A HB2    1 
ATOM   3805  H HB3    . GLU A 1 245 ? -3.154  -35.546 0.890   1.00 19.65  ?  245  GLU A HB3    1 
ATOM   3806  H HG2    . GLU A 1 245 ? -1.660  -37.163 1.667   1.00 25.40  ?  245  GLU A HG2    1 
ATOM   3807  H HG3    . GLU A 1 245 ? -0.670  -36.006 2.124   1.00 25.40  ?  245  GLU A HG3    1 
ATOM   3808  N N      . ALA A 1 246 ? -2.731  -37.296 -1.434  1.00 12.43  ?  246  ALA A N      1 
ATOM   3809  C CA     . ALA A 1 246 ? -2.806  -38.666 -1.923  1.00 13.46  ?  246  ALA A CA     1 
ATOM   3810  C C      . ALA A 1 246 ? -1.959  -38.849 -3.172  1.00 12.12  ?  246  ALA A C      1 
ATOM   3811  O O      . ALA A 1 246 ? -1.264  -39.859 -3.307  1.00 14.47  ?  246  ALA A O      1 
ATOM   3812  C CB     . ALA A 1 246 ? -4.259  -39.037 -2.212  1.00 14.68  ?  246  ALA A CB     1 
ATOM   3813  H H      . ALA A 1 246 ? -3.463  -36.849 -1.500  1.00 14.91  ?  246  ALA A H      1 
ATOM   3814  H HA     . ALA A 1 246 ? -2.469  -39.263 -1.237  1.00 16.14  ?  246  ALA A HA     1 
ATOM   3815  H HB1    . ALA A 1 246 ? -4.303  -39.974 -2.458  1.00 17.61  ?  246  ALA A HB1    1 
ATOM   3816  H HB2    . ALA A 1 246 ? -4.789  -38.879 -1.415  1.00 17.61  ?  246  ALA A HB2    1 
ATOM   3817  H HB3    . ALA A 1 246 ? -4.586  -38.487 -2.941  1.00 17.61  ?  246  ALA A HB3    1 
ATOM   3818  N N      . ILE A 1 247 ? -2.022  -37.900 -4.100  1.00 12.64  ?  247  ILE A N      1 
ATOM   3819  C CA     . ILE A 1 247 ? -1.240  -37.999 -5.332  1.00 12.15  ?  247  ILE A CA     1 
ATOM   3820  C C      . ILE A 1 247 ? 0.251   -37.999 -5.014  1.00 11.96  ?  247  ILE A C      1 
ATOM   3821  O O      . ILE A 1 247 ? 1.025   -38.813 -5.537  1.00 12.75  ?  247  ILE A O      1 
ATOM   3822  C CB     . ILE A 1 247 ? -1.629  -36.852 -6.290  1.00 14.10  ?  247  ILE A CB     1 
ATOM   3823  C CG1    . ILE A 1 247 ? -3.068  -37.045 -6.781  1.00 16.75  ?  247  ILE A CG1    1 
ATOM   3824  C CG2    . ILE A 1 247 ? -0.629  -36.725 -7.418  1.00 13.56  ?  247  ILE A CG2    1 
ATOM   3825  C CD1    . ILE A 1 247 ? -3.261  -38.161 -7.739  1.00 17.87  ?  247  ILE A CD1    1 
ATOM   3826  H H      . ILE A 1 247 ? -2.506  -37.191 -4.046  1.00 15.16  ?  247  ILE A H      1 
ATOM   3827  H HA     . ILE A 1 247 ? -1.441  -38.840 -5.771  1.00 14.57  ?  247  ILE A HA     1 
ATOM   3828  H HB     . ILE A 1 247 ? -1.601  -36.010 -5.808  1.00 16.92  ?  247  ILE A HB     1 
ATOM   3829  H HG12   . ILE A 1 247 ? -3.633  -37.221 -6.013  1.00 20.10  ?  247  ILE A HG12   1 
ATOM   3830  H HG13   . ILE A 1 247 ? -3.353  -36.230 -7.224  1.00 20.10  ?  247  ILE A HG13   1 
ATOM   3831  H HG21   . ILE A 1 247 ? -1.027  -36.210 -8.137  1.00 16.27  ?  247  ILE A HG21   1 
ATOM   3832  H HG22   . ILE A 1 247 ? 0.164   -36.274 -7.089  1.00 16.27  ?  247  ILE A HG22   1 
ATOM   3833  H HG23   . ILE A 1 247 ? -0.397  -37.612 -7.736  1.00 16.27  ?  247  ILE A HG23   1 
ATOM   3834  H HD11   . ILE A 1 247 ? -4.179  -38.152 -8.053  1.00 21.44  ?  247  ILE A HD11   1 
ATOM   3835  H HD12   . ILE A 1 247 ? -2.655  -38.044 -8.487  1.00 21.44  ?  247  ILE A HD12   1 
ATOM   3836  H HD13   . ILE A 1 247 ? -3.074  -39.000 -7.289  1.00 21.44  ?  247  ILE A HD13   1 
ATOM   3837  N N      . GLN A 1 248 ? 0.685   -37.080 -4.150  1.00 12.73  ?  248  GLN A N      1 
ATOM   3838  C CA     . GLN A 1 248 ? 2.111   -37.009 -3.842  1.00 12.25  ?  248  GLN A CA     1 
ATOM   3839  C C      . GLN A 1 248 ? 2.632   -38.284 -3.190  1.00 13.31  ?  248  GLN A C      1 
ATOM   3840  O O      . GLN A 1 248 ? 3.785   -38.669 -3.420  1.00 13.97  ?  248  GLN A O      1 
ATOM   3841  C CB     . GLN A 1 248 ? 2.407   -35.784 -2.968  1.00 12.45  ?  248  GLN A CB     1 
ATOM   3842  C CG     . GLN A 1 248 ? 2.317   -34.474 -3.746  1.00 12.62  ?  248  GLN A CG     1 
ATOM   3843  C CD     . GLN A 1 248 ? 2.596   -33.275 -2.885  1.00 13.83  ?  248  GLN A CD     1 
ATOM   3844  O OE1    . GLN A 1 248 ? 3.700   -32.739 -2.886  1.00 15.93  ?  248  GLN A OE1    1 
ATOM   3845  N NE2    . GLN A 1 248 ? 1.590   -32.853 -2.109  1.00 13.41  ?  248  GLN A NE2    1 
ATOM   3846  H H      . GLN A 1 248 ? 0.193   -36.504 -3.743  1.00 15.27  ?  248  GLN A H      1 
ATOM   3847  H HA     . GLN A 1 248 ? 2.596   -36.901 -4.675  1.00 14.70  ?  248  GLN A HA     1 
ATOM   3848  H HB2    . GLN A 1 248 ? 1.762   -35.749 -2.244  1.00 14.93  ?  248  GLN A HB2    1 
ATOM   3849  H HB3    . GLN A 1 248 ? 3.305   -35.860 -2.610  1.00 14.93  ?  248  GLN A HB3    1 
ATOM   3850  H HG2    . GLN A 1 248 ? 2.969   -34.486 -4.465  1.00 15.14  ?  248  GLN A HG2    1 
ATOM   3851  H HG3    . GLN A 1 248 ? 1.423   -34.381 -4.110  1.00 15.14  ?  248  GLN A HG3    1 
ATOM   3852  H HE21   . GLN A 1 248 ? 0.835   -33.264 -2.122  1.00 16.09  ?  248  GLN A HE21   1 
ATOM   3853  H HE22   . GLN A 1 248 ? 1.698   -32.170 -1.597  1.00 16.09  ?  248  GLN A HE22   1 
ATOM   3854  N N      . GLY A 1 249 ? 1.809   -38.966 -2.405  1.00 13.88  ?  249  GLY A N      1 
ATOM   3855  C CA     . GLY A 1 249 ? 2.245   -40.220 -1.813  1.00 12.55  ?  249  GLY A CA     1 
ATOM   3856  C C      . GLY A 1 249 ? 2.520   -41.286 -2.852  1.00 13.64  ?  249  GLY A C      1 
ATOM   3857  O O      . GLY A 1 249 ? 3.476   -42.060 -2.731  1.00 14.63  ?  249  GLY A O      1 
ATOM   3858  H H      . GLY A 1 249 ? 1.007   -38.731 -2.200  1.00 16.66  ?  249  GLY A H      1 
ATOM   3859  H HA2    . GLY A 1 249 ? 3.059   -40.070 -1.307  1.00 15.06  ?  249  GLY A HA2    1 
ATOM   3860  H HA3    . GLY A 1 249 ? 1.556   -40.549 -1.213  1.00 15.06  ?  249  GLY A HA3    1 
ATOM   3861  N N      . VAL A 1 250 ? 1.687   -41.344 -3.888  1.00 13.12  ?  250  VAL A N      1 
ATOM   3862  C CA     . VAL A 1 250 ? 1.906   -42.303 -4.963  1.00 13.81  ?  250  VAL A CA     1 
ATOM   3863  C C      . VAL A 1 250 ? 3.167   -41.951 -5.752  1.00 12.59  ?  250  VAL A C      1 
ATOM   3864  O O      . VAL A 1 250 ? 3.981   -42.826 -6.065  1.00 14.00  ?  250  VAL A O      1 
ATOM   3865  C CB     . VAL A 1 250 ? 0.667   -42.374 -5.867  1.00 13.50  ?  250  VAL A CB     1 
ATOM   3866  C CG1    . VAL A 1 250 ? 0.971   -43.200 -7.117  1.00 14.72  ?  250  VAL A CG1    1 
ATOM   3867  C CG2    . VAL A 1 250 ? -0.518  -42.975 -5.099  1.00 14.90  ?  250  VAL A CG2    1 
ATOM   3868  H H      . VAL A 1 250 ? 0.995   -40.845 -3.993  1.00 15.74  ?  250  VAL A H      1 
ATOM   3869  H HA     . VAL A 1 250 ? 2.043   -43.180 -4.572  1.00 16.56  ?  250  VAL A HA     1 
ATOM   3870  H HB     . VAL A 1 250 ? 0.426   -41.477 -6.147  1.00 16.19  ?  250  VAL A HB     1 
ATOM   3871  H HG11   . VAL A 1 250 ? 0.137   -43.417 -7.562  1.00 17.66  ?  250  VAL A HG11   1 
ATOM   3872  H HG12   . VAL A 1 250 ? 1.536   -42.680 -7.709  1.00 17.66  ?  250  VAL A HG12   1 
ATOM   3873  H HG13   . VAL A 1 250 ? 1.427   -44.015 -6.854  1.00 17.66  ?  250  VAL A HG13   1 
ATOM   3874  H HG21   . VAL A 1 250 ? -1.271  -43.066 -5.703  1.00 17.88  ?  250  VAL A HG21   1 
ATOM   3875  H HG22   . VAL A 1 250 ? -0.262  -43.845 -4.755  1.00 17.88  ?  250  VAL A HG22   1 
ATOM   3876  H HG23   . VAL A 1 250 ? -0.751  -42.384 -4.366  1.00 17.88  ?  250  VAL A HG23   1 
ATOM   3877  N N      . LEU A 1 251 ? 3.347   -40.672 -6.089  1.00 12.26  ?  251  LEU A N      1 
ATOM   3878  C CA     . LEU A 1 251 ? 4.518   -40.275 -6.866  1.00 13.05  ?  251  LEU A CA     1 
ATOM   3879  C C      . LEU A 1 251 ? 5.799   -40.607 -6.114  1.00 14.18  ?  251  LEU A C      1 
ATOM   3880  O O      . LEU A 1 251 ? 6.775   -41.083 -6.703  1.00 15.37  ?  251  LEU A O      1 
ATOM   3881  C CB     . LEU A 1 251 ? 4.466   -38.787 -7.207  1.00 12.96  ?  251  LEU A CB     1 
ATOM   3882  C CG     . LEU A 1 251 ? 3.246   -38.396 -8.033  1.00 13.01  ?  251  LEU A CG     1 
ATOM   3883  C CD1    . LEU A 1 251 ? 3.262   -36.882 -8.276  1.00 14.23  ?  251  LEU A CD1    1 
ATOM   3884  C CD2    . LEU A 1 251 ? 3.210   -39.119 -9.389  1.00 12.92  ?  251  LEU A CD2    1 
ATOM   3885  H H      . LEU A 1 251 ? 2.817   -40.026 -5.885  1.00 14.71  ?  251  LEU A H      1 
ATOM   3886  H HA     . LEU A 1 251 ? 4.514   -40.762 -7.704  1.00 15.66  ?  251  LEU A HA     1 
ATOM   3887  H HB2    . LEU A 1 251 ? 4.443   -38.278 -6.381  1.00 15.55  ?  251  LEU A HB2    1 
ATOM   3888  H HB3    . LEU A 1 251 ? 5.258   -38.555 -7.717  1.00 15.55  ?  251  LEU A HB3    1 
ATOM   3889  H HG     . LEU A 1 251 ? 2.451   -38.654 -7.541  1.00 15.61  ?  251  LEU A HG     1 
ATOM   3890  H HD11   . LEU A 1 251 ? 2.561   -36.656 -8.908  1.00 17.07  ?  251  LEU A HD11   1 
ATOM   3891  H HD12   . LEU A 1 251 ? 3.108   -36.425 -7.434  1.00 17.07  ?  251  LEU A HD12   1 
ATOM   3892  H HD13   . LEU A 1 251 ? 4.126   -36.629 -8.636  1.00 17.07  ?  251  LEU A HD13   1 
ATOM   3893  H HD21   . LEU A 1 251 ? 2.489   -38.751 -9.924  1.00 15.50  ?  251  LEU A HD21   1 
ATOM   3894  H HD22   . LEU A 1 251 ? 4.058   -38.986 -9.840  1.00 15.50  ?  251  LEU A HD22   1 
ATOM   3895  H HD23   . LEU A 1 251 ? 3.060   -40.065 -9.238  1.00 15.50  ?  251  LEU A HD23   1 
ATOM   3896  N N      . ALA A 1 252 ? 5.817   -40.369 -4.804  1.00 13.70  ?  252  ALA A N      1 
ATOM   3897  C CA     . ALA A 1 252 ? 7.020   -40.656 -4.031  1.00 14.71  ?  252  ALA A CA     1 
ATOM   3898  C C      . ALA A 1 252 ? 7.297   -42.153 -3.978  1.00 14.92  ?  252  ALA A C      1 
ATOM   3899  O O      . ALA A 1 252 ? 8.458   -42.581 -4.015  1.00 15.31  ?  252  ALA A O      1 
ATOM   3900  C CB     . ALA A 1 252 ? 6.853   -40.089 -2.620  1.00 14.67  ?  252  ALA A CB     1 
ATOM   3901  H H      . ALA A 1 252 ? 5.162   -40.049 -4.347  1.00 16.44  ?  252  ALA A H      1 
ATOM   3902  H HA     . ALA A 1 252 ? 7.784   -40.230 -4.450  1.00 17.64  ?  252  ALA A HA     1 
ATOM   3903  H HB1    . ALA A 1 252 ? 7.647   -40.291 -2.102  1.00 17.60  ?  252  ALA A HB1    1 
ATOM   3904  H HB2    . ALA A 1 252 ? 6.731   -39.128 -2.679  1.00 17.60  ?  252  ALA A HB2    1 
ATOM   3905  H HB3    . ALA A 1 252 ? 6.076   -40.496 -2.206  1.00 17.60  ?  252  ALA A HB3    1 
ATOM   3906  N N      . LYS A 1 253 ? 6.245   -42.966 -3.886  1.00 15.15  ?  253  LYS A N      1 
ATOM   3907  C CA     . LYS A 1 253 ? 6.410   -44.418 -3.815  1.00 14.62  ?  253  LYS A CA     1 
ATOM   3908  C C      . LYS A 1 253 ? 7.154   -44.956 -5.024  1.00 15.42  ?  253  LYS A C      1 
ATOM   3909  O O      . LYS A 1 253 ? 7.943   -45.894 -4.896  1.00 15.56  ?  253  LYS A O      1 
ATOM   3910  C CB     . LYS A 1 253 ? 5.033   -45.066 -3.681  1.00 16.15  ?  253  LYS A CB     1 
ATOM   3911  C CG     . LYS A 1 253 ? 5.036   -46.567 -3.576  1.00 17.09  ?  253  LYS A CG     1 
ATOM   3912  C CD     . LYS A 1 253 ? 3.622   -47.103 -3.342  1.00 16.93  ?  253  LYS A CD     1 
ATOM   3913  C CE     . LYS A 1 253 ? 3.593   -48.625 -3.224  1.00 18.81  ?  253  LYS A CE     1 
ATOM   3914  N NZ     . LYS A 1 253 ? 2.212   -49.123 -2.930  1.00 20.11  ?  253  LYS A NZ     1 
ATOM   3915  H H      . LYS A 1 253 ? 5.426   -42.707 -3.863  1.00 18.17  ?  253  LYS A H      1 
ATOM   3916  H HA     . LYS A 1 253 ? 6.934   -44.651 -3.033  1.00 17.54  ?  253  LYS A HA     1 
ATOM   3917  H HB2    . LYS A 1 253 ? 4.609   -44.721 -2.880  1.00 19.38  ?  253  LYS A HB2    1 
ATOM   3918  H HB3    . LYS A 1 253 ? 4.508   -44.832 -4.462  1.00 19.38  ?  253  LYS A HB3    1 
ATOM   3919  H HG2    . LYS A 1 253 ? 5.377   -46.949 -4.400  1.00 20.50  ?  253  LYS A HG2    1 
ATOM   3920  H HG3    . LYS A 1 253 ? 5.594   -46.838 -2.830  1.00 20.50  ?  253  LYS A HG3    1 
ATOM   3921  H HD2    . LYS A 1 253 ? 3.272   -46.729 -2.518  1.00 20.32  ?  253  LYS A HD2    1 
ATOM   3922  H HD3    . LYS A 1 253 ? 3.057   -46.847 -4.088  1.00 20.32  ?  253  LYS A HD3    1 
ATOM   3923  H HE2    . LYS A 1 253 ? 3.889   -49.019 -4.060  1.00 22.56  ?  253  LYS A HE2    1 
ATOM   3924  H HE3    . LYS A 1 253 ? 4.178   -48.903 -2.501  1.00 22.56  ?  253  LYS A HE3    1 
ATOM   3925  H HZ1    . LYS A 1 253 ? 2.207   -50.013 -2.910  1.00 24.12  ?  253  LYS A HZ1    1 
ATOM   3926  H HZ2    . LYS A 1 253 ? 1.939   -48.814 -2.141  1.00 24.12  ?  253  LYS A HZ2    1 
ATOM   3927  H HZ3    . LYS A 1 253 ? 1.648   -48.845 -3.560  1.00 24.12  ?  253  LYS A HZ3    1 
ATOM   3928  N N      . TYR A 1 254 ? 6.967   -44.344 -6.186  1.00 15.60  ?  254  TYR A N      1 
ATOM   3929  C CA     . TYR A 1 254 ? 7.525   -44.844 -7.438  1.00 16.06  ?  254  TYR A CA     1 
ATOM   3930  C C      . TYR A 1 254 ? 8.604   -43.934 -7.994  1.00 14.35  ?  254  TYR A C      1 
ATOM   3931  O O      . TYR A 1 254 ? 9.009   -44.102 -9.150  1.00 14.00  ?  254  TYR A O      1 
ATOM   3932  C CB     . TYR A 1 254 ? 6.405   -45.081 -8.448  1.00 17.61  ?  254  TYR A CB     1 
ATOM   3933  C CG     . TYR A 1 254 ? 5.458   -46.162 -7.977  1.00 15.23  ?  254  TYR A CG     1 
ATOM   3934  C CD1    . TYR A 1 254 ? 5.844   -47.495 -7.966  1.00 16.26  ?  254  TYR A CD1    1 
ATOM   3935  C CD2    . TYR A 1 254 ? 4.193   -45.854 -7.491  1.00 15.07  ?  254  TYR A CD2    1 
ATOM   3936  C CE1    . TYR A 1 254 ? 4.995   -48.493 -7.512  1.00 16.62  ?  254  TYR A CE1    1 
ATOM   3937  C CE2    . TYR A 1 254 ? 3.340   -46.848 -7.035  1.00 14.38  ?  254  TYR A CE2    1 
ATOM   3938  C CZ     . TYR A 1 254 ? 3.744   -48.165 -7.051  1.00 16.26  ?  254  TYR A CZ     1 
ATOM   3939  O OH     . TYR A 1 254 ? 2.903   -49.160 -6.603  1.00 17.89  ?  254  TYR A OH     1 
ATOM   3940  H H      . TYR A 1 254 ? 6.510   -43.621 -6.276  1.00 18.72  ?  254  TYR A H      1 
ATOM   3941  H HA     . TYR A 1 254 ? 7.946   -45.704 -7.282  1.00 19.27  ?  254  TYR A HA     1 
ATOM   3942  H HB2    . TYR A 1 254 ? 5.900   -44.261 -8.565  1.00 21.13  ?  254  TYR A HB2    1 
ATOM   3943  H HB3    . TYR A 1 254 ? 6.789   -45.357 -9.295  1.00 21.13  ?  254  TYR A HB3    1 
ATOM   3944  H HD1    . TYR A 1 254 ? 6.693   -47.724 -8.271  1.00 19.51  ?  254  TYR A HD1    1 
ATOM   3945  H HD2    . TYR A 1 254 ? 3.915   -44.967 -7.470  1.00 18.08  ?  254  TYR A HD2    1 
ATOM   3946  H HE1    . TYR A 1 254 ? 5.272   -49.380 -7.519  1.00 19.94  ?  254  TYR A HE1    1 
ATOM   3947  H HE2    . TYR A 1 254 ? 2.494   -46.625 -6.718  1.00 17.25  ?  254  TYR A HE2    1 
ATOM   3948  H HH     . TYR A 1 254 ? 2.233   -48.822 -6.227  1.00 21.46  ?  254  TYR A HH     1 
ATOM   3949  N N      . ASP A 1 255 ? 9.103   -43.002 -7.182  1.00 13.84  ?  255  ASP A N      1 
ATOM   3950  C CA     . ASP A 1 255 ? 10.187  -42.111 -7.588  1.00 15.56  ?  255  ASP A CA     1 
ATOM   3951  C C      . ASP A 1 255 ? 9.848   -41.401 -8.902  1.00 14.01  ?  255  ASP A C      1 
ATOM   3952  O O      . ASP A 1 255 ? 10.613  -41.426 -9.861  1.00 15.70  ?  255  ASP A O      1 
ATOM   3953  C CB     . ASP A 1 255 ? 11.510  -42.870 -7.695  1.00 17.60  ?  255  ASP A CB     1 
ATOM   3954  C CG     . ASP A 1 255 ? 12.722  -41.942 -7.817  1.00 23.58  ?  255  ASP A CG     1 
ATOM   3955  O OD1    . ASP A 1 255 ? 12.621  -40.759 -7.432  1.00 22.61  ?  255  ASP A OD1    1 
ATOM   3956  O OD2    . ASP A 1 255 ? 13.788  -42.409 -8.282  1.00 26.49  -1 255  ASP A OD2    1 
ATOM   3957  H H      . ASP A 1 255 ? 8.826   -42.867 -6.379  1.00 16.60  ?  255  ASP A H      1 
ATOM   3958  H HA     . ASP A 1 255 ? 10.292  -41.429 -6.906  1.00 18.67  ?  255  ASP A HA     1 
ATOM   3959  H HB2    . ASP A 1 255 ? 11.628  -43.413 -6.900  1.00 21.12  ?  255  ASP A HB2    1 
ATOM   3960  H HB3    . ASP A 1 255 ? 11.486  -43.436 -8.482  1.00 21.12  ?  255  ASP A HB3    1 
ATOM   3961  N N      . VAL A 1 256 ? 8.686   -40.759 -8.934  1.00 12.85  ?  256  VAL A N      1 
ATOM   3962  C CA     . VAL A 1 256 ? 8.211   -40.016 -10.096 1.00 13.20  ?  256  VAL A CA     1 
ATOM   3963  C C      . VAL A 1 256 ? 8.305   -38.529 -9.800  1.00 13.29  ?  256  VAL A C      1 
ATOM   3964  O O      . VAL A 1 256 ? 7.795   -38.062 -8.776  1.00 14.21  ?  256  VAL A O      1 
ATOM   3965  C CB     . VAL A 1 256 ? 6.768   -40.418 -10.456 1.00 11.61  ?  256  VAL A CB     1 
ATOM   3966  C CG1    . VAL A 1 256 ? 6.242   -39.591 -11.623 1.00 13.98  ?  256  VAL A CG1    1 
ATOM   3967  C CG2    . VAL A 1 256 ? 6.724   -41.898 -10.835 1.00 14.26  ?  256  VAL A CG2    1 
ATOM   3968  H H      . VAL A 1 256 ? 8.138   -40.740 -8.271  1.00 15.42  ?  256  VAL A H      1 
ATOM   3969  H HA     . VAL A 1 256 ? 8.786   -40.205 -10.854 1.00 15.84  ?  256  VAL A HA     1 
ATOM   3970  H HB     . VAL A 1 256 ? 6.203   -40.256 -9.684  1.00 13.93  ?  256  VAL A HB     1 
ATOM   3971  H HG11   . VAL A 1 256 ? 5.437   -40.008 -11.968 1.00 16.77  ?  256  VAL A HG11   1 
ATOM   3972  H HG12   . VAL A 1 256 ? 6.043   -38.695 -11.311 1.00 16.77  ?  256  VAL A HG12   1 
ATOM   3973  H HG13   . VAL A 1 256 ? 6.920   -39.557 -12.316 1.00 16.77  ?  256  VAL A HG13   1 
ATOM   3974  H HG21   . VAL A 1 256 ? 5.805   -42.152 -11.012 1.00 17.11  ?  256  VAL A HG21   1 
ATOM   3975  H HG22   . VAL A 1 256 ? 7.264   -42.037 -11.629 1.00 17.11  ?  256  VAL A HG22   1 
ATOM   3976  H HG23   . VAL A 1 256 ? 7.077   -42.423 -10.100 1.00 17.11  ?  256  VAL A HG23   1 
ATOM   3977  N N      . LEU A 1 257 ? 8.959   -37.793 -10.693 1.00 12.34  ?  257  LEU A N      1 
ATOM   3978  C CA     . LEU A 1 257 ? 9.085   -36.350 -10.548 1.00 12.34  ?  257  LEU A CA     1 
ATOM   3979  C C      . LEU A 1 257 ? 7.718   -35.674 -10.615 1.00 12.74  ?  257  LEU A C      1 
ATOM   3980  O O      . LEU A 1 257 ? 6.813   -36.122 -11.320 1.00 12.65  ?  257  LEU A O      1 
ATOM   3981  C CB     . LEU A 1 257 ? 9.966   -35.764 -11.661 1.00 12.69  ?  257  LEU A CB     1 
ATOM   3982  C CG     . LEU A 1 257 ? 11.464  -36.095 -11.640 1.00 13.76  ?  257  LEU A CG     1 
ATOM   3983  C CD1    . LEU A 1 257 ? 12.079  -35.613 -12.915 1.00 17.02  ?  257  LEU A CD1    1 
ATOM   3984  C CD2    . LEU A 1 257 ? 12.136  -35.450 -10.448 1.00 14.25  ?  257  LEU A CD2    1 
ATOM   3985  H H      . LEU A 1 257 ? 9.342   -38.106 -11.397 1.00 14.80  ?  257  LEU A H      1 
ATOM   3986  H HA     . LEU A 1 257 ? 9.494   -36.166 -9.687  1.00 14.80  ?  257  LEU A HA     1 
ATOM   3987  H HB2    . LEU A 1 257 ? 9.622   -36.084 -12.509 1.00 15.23  ?  257  LEU A HB2    1 
ATOM   3988  H HB3    . LEU A 1 257 ? 9.894   -34.798 -11.617 1.00 15.23  ?  257  LEU A HB3    1 
ATOM   3989  H HG     . LEU A 1 257 ? 11.594  -37.053 -11.563 1.00 16.51  ?  257  LEU A HG     1 
ATOM   3990  H HD11   . LEU A 1 257 ? 13.027  -35.819 -12.906 1.00 20.42  ?  257  LEU A HD11   1 
ATOM   3991  H HD12   . LEU A 1 257 ? 11.651  -36.061 -13.662 1.00 20.42  ?  257  LEU A HD12   1 
ATOM   3992  H HD13   . LEU A 1 257 ? 11.950  -34.655 -12.986 1.00 20.42  ?  257  LEU A HD13   1 
ATOM   3993  H HD21   . LEU A 1 257 ? 13.078  -35.684 -10.451 1.00 17.10  ?  257  LEU A HD21   1 
ATOM   3994  H HD22   . LEU A 1 257 ? 12.035  -34.487 -10.511 1.00 17.10  ?  257  LEU A HD22   1 
ATOM   3995  H HD23   . LEU A 1 257 ? 11.717  -35.774 -9.636  1.00 17.10  ?  257  LEU A HD23   1 
ATOM   3996  N N      . LEU A 1 258 ? 7.596   -34.562 -9.900  1.00 13.37  ?  258  LEU A N      1 
ATOM   3997  C CA     . LEU A 1 258 ? 6.369   -33.777 -9.858  1.00 13.08  ?  258  LEU A CA     1 
ATOM   3998  C C      . LEU A 1 258 ? 6.628   -32.401 -10.450 1.00 11.44  ?  258  LEU A C      1 
ATOM   3999  O O      . LEU A 1 258 ? 7.462   -31.644 -9.934  1.00 13.23  ?  258  LEU A O      1 
ATOM   4000  C CB     . LEU A 1 258 ? 5.860   -33.651 -8.417  1.00 12.38  ?  258  LEU A CB     1 
ATOM   4001  C CG     . LEU A 1 258 ? 4.640   -32.777 -8.156  1.00 16.23  ?  258  LEU A CG     1 
ATOM   4002  C CD1    . LEU A 1 258 ? 3.486   -33.079 -9.080  1.00 16.68  ?  258  LEU A CD1    1 
ATOM   4003  C CD2    . LEU A 1 258 ? 4.189   -32.906 -6.697  1.00 17.86  ?  258  LEU A CD2    1 
ATOM   4004  H H      . LEU A 1 258 ? 8.229   -34.235 -9.418  1.00 16.04  ?  258  LEU A H      1 
ATOM   4005  H HA     . LEU A 1 258 ? 5.691   -34.212 -10.398 1.00 15.69  ?  258  LEU A HA     1 
ATOM   4006  H HB2    . LEU A 1 258 ? 5.634   -34.541 -8.107  1.00 14.85  ?  258  LEU A HB2    1 
ATOM   4007  H HB3    . LEU A 1 258 ? 6.582   -33.286 -7.882  1.00 14.85  ?  258  LEU A HB3    1 
ATOM   4008  H HG     . LEU A 1 258 ? 4.905   -31.860 -8.332  1.00 19.47  ?  258  LEU A HG     1 
ATOM   4009  H HD11   . LEU A 1 258 ? 2.723   -32.540 -8.819  1.00 20.01  ?  258  LEU A HD11   1 
ATOM   4010  H HD12   . LEU A 1 258 ? 3.746   -32.867 -9.990  1.00 20.01  ?  258  LEU A HD12   1 
ATOM   4011  H HD13   . LEU A 1 258 ? 3.265   -34.021 -9.011  1.00 20.01  ?  258  LEU A HD13   1 
ATOM   4012  H HD21   . LEU A 1 258 ? 3.388   -32.375 -6.565  1.00 21.43  ?  258  LEU A HD21   1 
ATOM   4013  H HD22   . LEU A 1 258 ? 4.003   -33.839 -6.505  1.00 21.43  ?  258  LEU A HD22   1 
ATOM   4014  H HD23   . LEU A 1 258 ? 4.898   -32.585 -6.118  1.00 21.43  ?  258  LEU A HD23   1 
ATOM   4015  N N      . ILE A 1 259 ? 5.938   -32.093 -11.545 1.00 12.19  ?  259  ILE A N      1 
ATOM   4016  C CA     . ILE A 1 259 ? 5.990   -30.779 -12.179 1.00 11.48  ?  259  ILE A CA     1 
ATOM   4017  C C      . ILE A 1 259 ? 4.705   -30.057 -11.817 1.00 12.63  ?  259  ILE A C      1 
ATOM   4018  O O      . ILE A 1 259 ? 3.606   -30.518 -12.166 1.00 12.10  ?  259  ILE A O      1 
ATOM   4019  C CB     . ILE A 1 259 ? 6.095   -30.898 -13.708 1.00 12.79  ?  259  ILE A CB     1 
ATOM   4020  C CG1    . ILE A 1 259 ? 7.317   -31.724 -14.141 1.00 13.49  ?  259  ILE A CG1    1 
ATOM   4021  C CG2    . ILE A 1 259 ? 6.178   -29.509 -14.355 1.00 13.69  ?  259  ILE A CG2    1 
ATOM   4022  C CD1    . ILE A 1 259 ? 7.245   -32.167 -15.592 1.00 14.72  ?  259  ILE A CD1    1 
ATOM   4023  H H      . ILE A 1 259 ? 5.419   -32.646 -11.950 1.00 14.63  ?  259  ILE A H      1 
ATOM   4024  H HA     . ILE A 1 259 ? 6.757   -30.289 -11.844 1.00 13.77  ?  259  ILE A HA     1 
ATOM   4025  H HB     . ILE A 1 259 ? 5.294   -31.357 -14.004 1.00 15.34  ?  259  ILE A HB     1 
ATOM   4026  H HG12   . ILE A 1 259 ? 8.116   -31.185 -14.032 1.00 16.18  ?  259  ILE A HG12   1 
ATOM   4027  H HG13   . ILE A 1 259 ? 7.373   -32.518 -13.587 1.00 16.18  ?  259  ILE A HG13   1 
ATOM   4028  H HG21   . ILE A 1 259 ? 6.325   -29.613 -15.309 1.00 16.42  ?  259  ILE A HG21   1 
ATOM   4029  H HG22   . ILE A 1 259 ? 5.344   -29.038 -14.199 1.00 16.42  ?  259  ILE A HG22   1 
ATOM   4030  H HG23   . ILE A 1 259 ? 6.915   -29.019 -13.958 1.00 16.42  ?  259  ILE A HG23   1 
ATOM   4031  H HD11   . ILE A 1 259 ? 7.975   -32.779 -15.771 1.00 17.66  ?  259  ILE A HD11   1 
ATOM   4032  H HD12   . ILE A 1 259 ? 6.396   -32.611 -15.744 1.00 17.66  ?  259  ILE A HD12   1 
ATOM   4033  H HD13   . ILE A 1 259 ? 7.318   -31.387 -16.164 1.00 17.66  ?  259  ILE A HD13   1 
ATOM   4034  N N      . ALA A 1 260 ? 4.826   -28.953 -11.085 1.00 10.92  ?  260  ALA A N      1 
ATOM   4035  C CA     . ALA A 1 260 ? 3.679   -28.103 -10.795 1.00 10.24  ?  260  ALA A CA     1 
ATOM   4036  C C      . ALA A 1 260 ? 3.583   -27.038 -11.875 1.00 12.33  ?  260  ALA A C      1 
ATOM   4037  O O      . ALA A 1 260 ? 4.506   -26.236 -12.025 1.00 11.72  ?  260  ALA A O      1 
ATOM   4038  C CB     . ALA A 1 260 ? 3.823   -27.425 -9.438  1.00 12.35  ?  260  ALA A CB     1 
ATOM   4039  H H      . ALA A 1 260 ? 5.565   -28.676 -10.745 1.00 13.10  ?  260  ALA A H      1 
ATOM   4040  H HA     . ALA A 1 260 ? 2.876   -28.647 -10.787 1.00 12.28  ?  260  ALA A HA     1 
ATOM   4041  H HB1    . ALA A 1 260 ? 3.070   -26.829 -9.301  1.00 14.82  ?  260  ALA A HB1    1 
ATOM   4042  H HB2    . ALA A 1 260 ? 3.838   -28.104 -8.745  1.00 14.82  ?  260  ALA A HB2    1 
ATOM   4043  H HB3    . ALA A 1 260 ? 4.651   -26.920 -9.423  1.00 14.82  ?  260  ALA A HB3    1 
ATOM   4044  N N      . ASP A 1 261 ? 2.493   -27.047 -12.639 1.00 11.30  ?  261  ASP A N      1 
ATOM   4045  C CA     . ASP A 1 261 ? 2.267   -26.036 -13.678 1.00 11.35  ?  261  ASP A CA     1 
ATOM   4046  C C      . ASP A 1 261 ? 1.550   -24.864 -13.025 1.00 12.19  ?  261  ASP A C      1 
ATOM   4047  O O      . ASP A 1 261 ? 0.341   -24.922 -12.785 1.00 11.78  ?  261  ASP A O      1 
ATOM   4048  C CB     . ASP A 1 261 ? 1.485   -26.601 -14.854 1.00 11.79  ?  261  ASP A CB     1 
ATOM   4049  C CG     . ASP A 1 261 ? 1.458   -25.648 -16.025 1.00 12.00  ?  261  ASP A CG     1 
ATOM   4050  O OD1    . ASP A 1 261 ? 1.551   -24.428 -15.747 1.00 13.45  ?  261  ASP A OD1    1 
ATOM   4051  O OD2    . ASP A 1 261 ? 1.311   -26.100 -17.212 1.00 12.73  -1 261  ASP A OD2    1 
ATOM   4052  H H      . ASP A 1 261 ? 1.864   -27.630 -12.575 1.00 13.56  ?  261  ASP A H      1 
ATOM   4053  H HA     . ASP A 1 261 ? 3.121   -25.733 -14.024 1.00 13.62  ?  261  ASP A HA     1 
ATOM   4054  H HB2    . ASP A 1 261 ? 1.900   -27.428 -15.145 1.00 14.15  ?  261  ASP A HB2    1 
ATOM   4055  H HB3    . ASP A 1 261 ? 0.570   -26.768 -14.578 1.00 14.15  ?  261  ASP A HB3    1 
ATOM   4056  N N      . GLU A 1 262 ? 2.317   -23.823 -12.690 1.00 9.94   ?  262  GLU A N      1 
ATOM   4057  C CA     . GLU A 1 262 ? 1.834   -22.642 -12.006 1.00 11.08  ?  262  GLU A CA     1 
ATOM   4058  C C      . GLU A 1 262 ? 1.569   -21.481 -12.952 1.00 11.17  ?  262  GLU A C      1 
ATOM   4059  O O      . GLU A 1 262 ? 1.525   -20.329 -12.515 1.00 12.35  ?  262  GLU A O      1 
ATOM   4060  C CB     . GLU A 1 262 ? 2.851   -22.220 -10.949 1.00 13.17  ?  262  GLU A CB     1 
ATOM   4061  C CG     . GLU A 1 262 ? 3.001   -23.166 -9.795  1.00 13.59  ?  262  GLU A CG     1 
ATOM   4062  C CD     . GLU A 1 262 ? 2.006   -22.947 -8.680  1.00 13.62  ?  262  GLU A CD     1 
ATOM   4063  O OE1    . GLU A 1 262 ? 1.201   -21.987 -8.752  1.00 13.78  ?  262  GLU A OE1    1 
ATOM   4064  O OE2    . GLU A 1 262 ? 2.044   -23.758 -7.717  1.00 13.58  -1 262  GLU A OE2    1 
ATOM   4065  H H      . GLU A 1 262 ? 3.159   -23.786 -12.862 1.00 11.92  ?  262  GLU A H      1 
ATOM   4066  H HA     . GLU A 1 262 ? 0.996   -22.861 -11.570 1.00 13.29  ?  262  GLU A HA     1 
ATOM   4067  H HB2    . GLU A 1 262 ? 3.719   -22.141 -11.374 1.00 15.80  ?  262  GLU A HB2    1 
ATOM   4068  H HB3    . GLU A 1 262 ? 2.579   -21.362 -10.587 1.00 15.80  ?  262  GLU A HB3    1 
ATOM   4069  H HG2    . GLU A 1 262 ? 2.884   -24.072 -10.119 1.00 16.31  ?  262  GLU A HG2    1 
ATOM   4070  H HG3    . GLU A 1 262 ? 3.889   -23.059 -9.420  1.00 16.31  ?  262  GLU A HG3    1 
ATOM   4071  N N      . VAL A 1 263 ? 1.385   -21.750 -14.238 1.00 12.43  ?  263  VAL A N      1 
ATOM   4072  C CA     . VAL A 1 263 ? 1.188   -20.652 -15.180 1.00 11.25  ?  263  VAL A CA     1 
ATOM   4073  C C      . VAL A 1 263 ? -0.016  -19.793 -14.795 1.00 12.38  ?  263  VAL A C      1 
ATOM   4074  O O      . VAL A 1 263 ? 0.051   -18.559 -14.850 1.00 13.37  ?  263  VAL A O      1 
ATOM   4075  C CB     . VAL A 1 263 ? 1.139   -21.164 -16.626 1.00 10.99  ?  263  VAL A CB     1 
ATOM   4076  C CG1    . VAL A 1 263 ? 0.677   -20.065 -17.568 1.00 13.17  ?  263  VAL A CG1    1 
ATOM   4077  C CG2    . VAL A 1 263 ? 2.525   -21.620 -17.031 1.00 11.22  ?  263  VAL A CG2    1 
ATOM   4078  H H      . VAL A 1 263 ? 1.369   -22.537 -14.586 1.00 14.91  ?  263  VAL A H      1 
ATOM   4079  H HA     . VAL A 1 263 ? 1.961   -20.070 -15.124 1.00 13.50  ?  263  VAL A HA     1 
ATOM   4080  H HB     . VAL A 1 263 ? 0.513   -21.902 -16.686 1.00 13.18  ?  263  VAL A HB     1 
ATOM   4081  H HG11   . VAL A 1 263 ? 0.927   -20.301 -18.475 1.00 15.80  ?  263  VAL A HG11   1 
ATOM   4082  H HG12   . VAL A 1 263 ? -0.287  -19.978 -17.503 1.00 15.80  ?  263  VAL A HG12   1 
ATOM   4083  H HG13   . VAL A 1 263 ? 1.102   -19.231 -17.314 1.00 15.80  ?  263  VAL A HG13   1 
ATOM   4084  H HG21   . VAL A 1 263 ? 2.479   -22.027 -17.911 1.00 13.46  ?  263  VAL A HG21   1 
ATOM   4085  H HG22   . VAL A 1 263 ? 3.117   -20.852 -17.053 1.00 13.46  ?  263  VAL A HG22   1 
ATOM   4086  H HG23   . VAL A 1 263 ? 2.847   -22.267 -16.384 1.00 13.46  ?  263  VAL A HG23   1 
ATOM   4087  N N      . VAL A 1 264 ? -1.130  -20.409 -14.397 1.00 12.25  ?  264  VAL A N      1 
ATOM   4088  C CA     . VAL A 1 264 ? -2.269  -19.617 -13.938 1.00 11.67  ?  264  VAL A CA     1 
ATOM   4089  C C      . VAL A 1 264 ? -2.125  -19.251 -12.457 1.00 13.07  ?  264  VAL A C      1 
ATOM   4090  O O      . VAL A 1 264 ? -2.360  -18.107 -12.067 1.00 13.82  ?  264  VAL A O      1 
ATOM   4091  C CB     . VAL A 1 264 ? -3.598  -20.345 -14.204 1.00 13.98  ?  264  VAL A CB     1 
ATOM   4092  C CG1    . VAL A 1 264 ? -4.740  -19.682 -13.449 1.00 13.86  ?  264  VAL A CG1    1 
ATOM   4093  C CG2    . VAL A 1 264 ? -3.903  -20.350 -15.700 1.00 14.08  ?  264  VAL A CG2    1 
ATOM   4094  H H      . VAL A 1 264 ? -1.249  -21.261 -14.383 1.00 14.70  ?  264  VAL A H      1 
ATOM   4095  H HA     . VAL A 1 264 ? -2.276  -18.795 -14.452 1.00 14.00  ?  264  VAL A HA     1 
ATOM   4096  H HB     . VAL A 1 264 ? -3.516  -21.260 -13.893 1.00 16.77  ?  264  VAL A HB     1 
ATOM   4097  H HG11   . VAL A 1 264 ? -5.581  -19.936 -13.860 1.00 16.62  ?  264  VAL A HG11   1 
ATOM   4098  H HG12   . VAL A 1 264 ? -4.721  -19.977 -12.525 1.00 16.62  ?  264  VAL A HG12   1 
ATOM   4099  H HG13   . VAL A 1 264 ? -4.629  -18.719 -13.490 1.00 16.62  ?  264  VAL A HG13   1 
ATOM   4100  H HG21   . VAL A 1 264 ? -4.647  -20.949 -15.868 1.00 16.89  ?  264  VAL A HG21   1 
ATOM   4101  H HG22   . VAL A 1 264 ? -4.133  -19.450 -15.979 1.00 16.89  ?  264  VAL A HG22   1 
ATOM   4102  H HG23   . VAL A 1 264 ? -3.118  -20.655 -16.181 1.00 16.89  ?  264  VAL A HG23   1 
ATOM   4103  N N      . CYS A 1 265 ? -1.780  -20.219 -11.596 1.00 12.92  ?  265  CYS A N      1 
ATOM   4104  C CA     . CYS A 1 265 ? -1.864  -19.960 -10.162 1.00 14.68  ?  265  CYS A CA     1 
ATOM   4105  C C      . CYS A 1 265 ? -0.715  -19.111 -9.620  1.00 14.62  ?  265  CYS A C      1 
ATOM   4106  O O      . CYS A 1 265 ? -0.830  -18.585 -8.511  1.00 15.84  ?  265  CYS A O      1 
ATOM   4107  C CB     . CYS A 1 265 ? -1.945  -21.269 -9.379  1.00 14.17  ?  265  CYS A CB     1 
ATOM   4108  S SG     . CYS A 1 265 ? -3.473  -22.208 -9.622  1.00 16.13  ?  265  CYS A SG     1 
ATOM   4109  H H      . CYS A 1 265 ? -1.505  -21.004 -11.814 1.00 15.50  ?  265  CYS A H      1 
ATOM   4110  H HA     . CYS A 1 265 ? -2.685  -19.468 -10.006 1.00 17.61  ?  265  CYS A HA     1 
ATOM   4111  H HB2    . CYS A 1 265 ? -1.207  -21.837 -9.652  1.00 17.00  ?  265  CYS A HB2    1 
ATOM   4112  H HB3    . CYS A 1 265 ? -1.875  -21.066 -8.433  1.00 17.00  ?  265  CYS A HB3    1 
ATOM   4113  H HG     . CYS A 1 265 ? -3.507  -22.613 -10.751 1.00 19.35  ?  265  CYS A HG     1 
ATOM   4114  N N      . GLY A 1 266 ? 0.367   -18.965 -10.367 1.00 13.90  ?  266  GLY A N      1 
ATOM   4115  C CA     . GLY A 1 266 ? 1.533   -18.287 -9.841  1.00 14.71  ?  266  GLY A CA     1 
ATOM   4116  C C      . GLY A 1 266 ? 1.319   -16.803 -9.613  1.00 14.12  ?  266  GLY A C      1 
ATOM   4117  O O      . GLY A 1 266 ? 0.520   -16.145 -10.270 1.00 13.72  ?  266  GLY A O      1 
ATOM   4118  H H      . GLY A 1 266 ? 0.451   -19.246 -11.175 1.00 16.67  ?  266  GLY A H      1 
ATOM   4119  H HA2    . GLY A 1 266 ? 1.778   -18.690 -8.993  1.00 17.64  ?  266  GLY A HA2    1 
ATOM   4120  H HA3    . GLY A 1 266 ? 2.269   -18.393 -10.465 1.00 17.64  ?  266  GLY A HA3    1 
ATOM   4121  N N      . PHE A 1 267 ? 2.078   -16.284 -8.654  1.00 13.78  ?  267  PHE A N      1 
ATOM   4122  C CA     . PHE A 1 267 ? 2.178   -14.843 -8.408  1.00 13.76  ?  267  PHE A CA     1 
ATOM   4123  C C      . PHE A 1 267 ? 0.855   -14.227 -7.956  1.00 13.68  ?  267  PHE A C      1 
ATOM   4124  O O      . PHE A 1 267 ? 0.496   -13.118 -8.349  1.00 14.88  ?  267  PHE A O      1 
ATOM   4125  C CB     . PHE A 1 267 ? 2.837   -14.119 -9.587  1.00 15.94  ?  267  PHE A CB     1 
ATOM   4126  C CG     . PHE A 1 267 ? 4.154   -14.744 -9.990  1.00 13.73  ?  267  PHE A CG     1 
ATOM   4127  C CD1    . PHE A 1 267 ? 5.291   -14.515 -9.248  1.00 14.31  ?  267  PHE A CD1    1 
ATOM   4128  C CD2    . PHE A 1 267 ? 4.212   -15.631 -11.047 1.00 13.69  ?  267  PHE A CD2    1 
ATOM   4129  C CE1    . PHE A 1 267 ? 6.494   -15.143 -9.579  1.00 15.19  ?  267  PHE A CE1    1 
ATOM   4130  C CE2    . PHE A 1 267 ? 5.401   -16.262 -11.377 1.00 14.25  ?  267  PHE A CE2    1 
ATOM   4131  C CZ     . PHE A 1 267 ? 6.538   -16.008 -10.646 1.00 15.12  ?  267  PHE A CZ     1 
ATOM   4132  H H      . PHE A 1 267 ? 2.558   -16.755 -8.118  1.00 16.53  ?  267  PHE A H      1 
ATOM   4133  H HA     . PHE A 1 267 ? 2.767   -14.705 -7.649  1.00 16.51  ?  267  PHE A HA     1 
ATOM   4134  H HB2    . PHE A 1 267 ? 2.241   -14.153 -10.352 1.00 19.13  ?  267  PHE A HB2    1 
ATOM   4135  H HB3    . PHE A 1 267 ? 3.004   -13.197 -9.338  1.00 19.13  ?  267  PHE A HB3    1 
ATOM   4136  H HD1    . PHE A 1 267 ? 5.257   -13.936 -8.520  1.00 17.16  ?  267  PHE A HD1    1 
ATOM   4137  H HD2    . PHE A 1 267 ? 3.445   -15.808 -11.542 1.00 16.42  ?  267  PHE A HD2    1 
ATOM   4138  H HE1    . PHE A 1 267 ? 7.261   -14.977 -9.080  1.00 18.23  ?  267  PHE A HE1    1 
ATOM   4139  H HE2    . PHE A 1 267 ? 5.431   -16.855 -12.093 1.00 17.10  ?  267  PHE A HE2    1 
ATOM   4140  H HZ     . PHE A 1 267 ? 7.338   -16.423 -10.874 1.00 18.14  ?  267  PHE A HZ     1 
ATOM   4141  N N      . GLY A 1 268 ? 0.160   -14.920 -7.058  1.00 12.58  ?  268  GLY A N      1 
ATOM   4142  C CA     . GLY A 1 268 ? -0.886  -14.322 -6.250  1.00 14.23  ?  268  GLY A CA     1 
ATOM   4143  C C      . GLY A 1 268 ? -2.292  -14.729 -6.599  1.00 13.87  ?  268  GLY A C      1 
ATOM   4144  O O      . GLY A 1 268 ? -3.208  -14.389 -5.853  1.00 15.60  ?  268  GLY A O      1 
ATOM   4145  H H      . GLY A 1 268 ? 0.283   -15.756 -6.899  1.00 15.09  ?  268  GLY A H      1 
ATOM   4146  H HA2    . GLY A 1 268 ? -0.734  -14.563 -5.323  1.00 17.08  ?  268  GLY A HA2    1 
ATOM   4147  H HA3    . GLY A 1 268 ? -0.830  -13.358 -6.339  1.00 17.08  ?  268  GLY A HA3    1 
ATOM   4148  N N      . ARG A 1 269 ? -2.492  -15.455 -7.706  1.00 13.70  ?  269  ARG A N      1 
ATOM   4149  C CA     . ARG A 1 269 ? -3.830  -15.616 -8.281  1.00 13.73  ?  269  ARG A CA     1 
ATOM   4150  C C      . ARG A 1 269 ? -4.834  -16.221 -7.306  1.00 14.35  ?  269  ARG A C      1 
ATOM   4151  O O      . ARG A 1 269 ? -6.007  -15.838 -7.326  1.00 15.47  ?  269  ARG A O      1 
ATOM   4152  C CB     . ARG A 1 269 ? -3.724  -16.411 -9.580  1.00 14.46  ?  269  ARG A CB     1 
ATOM   4153  C CG     . ARG A 1 269 ? -5.002  -16.989 -10.146 1.00 12.67  ?  269  ARG A CG     1 
ATOM   4154  C CD     . ARG A 1 269 ? -6.017  -15.931 -10.447 1.00 13.64  ?  269  ARG A CD     1 
ATOM   4155  N NE     . ARG A 1 269 ? -5.651  -15.060 -11.563 1.00 12.99  ?  269  ARG A NE     1 
ATOM   4156  C CZ     . ARG A 1 269 ? -6.432  -14.092 -12.020 1.00 13.69  ?  269  ARG A CZ     1 
ATOM   4157  N NH1    . ARG A 1 269 ? -7.608  -13.871 -11.442 1.00 13.33  ?  269  ARG A NH1    1 
ATOM   4158  N NH2    . ARG A 1 269 ? -6.043  -13.321 -13.042 1.00 15.12  ?  269  ARG A NH2    1 
ATOM   4159  H H      . ARG A 1 269 ? -1.873  -15.863 -8.142  1.00 16.44  ?  269  ARG A H      1 
ATOM   4160  H HA     . ARG A 1 269 ? -4.187  -14.740 -8.493  1.00 16.48  ?  269  ARG A HA     1 
ATOM   4161  H HB2    . ARG A 1 269 ? -3.356  -15.824 -10.259 1.00 17.35  ?  269  ARG A HB2    1 
ATOM   4162  H HB3    . ARG A 1 269 ? -3.123  -17.156 -9.425  1.00 17.35  ?  269  ARG A HB3    1 
ATOM   4163  H HG2    . ARG A 1 269 ? -4.802  -17.458 -10.971 1.00 15.20  ?  269  ARG A HG2    1 
ATOM   4164  H HG3    . ARG A 1 269 ? -5.388  -17.602 -9.501  1.00 15.20  ?  269  ARG A HG3    1 
ATOM   4165  H HD2    . ARG A 1 269 ? -6.858  -16.359 -10.670 1.00 16.36  ?  269  ARG A HD2    1 
ATOM   4166  H HD3    . ARG A 1 269 ? -6.127  -15.372 -9.661  1.00 16.36  ?  269  ARG A HD3    1 
ATOM   4167  H HE     . ARG A 1 269 ? -4.889  -15.182 -11.943 1.00 15.58  ?  269  ARG A HE     1 
ATOM   4168  H HH11   . ARG A 1 269 ? -7.858  -14.355 -10.776 1.00 15.99  ?  269  ARG A HH11   1 
ATOM   4169  H HH12   . ARG A 1 269 ? -8.120  -13.244 -11.734 1.00 15.99  ?  269  ARG A HH12   1 
ATOM   4170  H HH21   . ARG A 1 269 ? -5.277  -13.450 -13.411 1.00 18.15  ?  269  ARG A HH21   1 
ATOM   4171  H HH22   . ARG A 1 269 ? -6.559  -12.695 -13.329 1.00 18.15  ?  269  ARG A HH22   1 
ATOM   4172  N N      . ILE A 1 270 ? -4.428  -17.186 -6.482  1.00 13.35  ?  270  ILE A N      1 
ATOM   4173  C CA     . ILE A 1 270 ? -5.380  -17.814 -5.571  1.00 14.38  ?  270  ILE A CA     1 
ATOM   4174  C C      . ILE A 1 270 ? -5.136  -17.393 -4.118  1.00 16.62  ?  270  ILE A C      1 
ATOM   4175  O O      . ILE A 1 270 ? -5.609  -18.038 -3.195  1.00 15.79  ?  270  ILE A O      1 
ATOM   4176  C CB     . ILE A 1 270 ? -5.493  -19.339 -5.746  1.00 13.97  ?  270  ILE A CB     1 
ATOM   4177  C CG1    . ILE A 1 270 ? -4.246  -20.097 -5.272  1.00 15.20  ?  270  ILE A CG1    1 
ATOM   4178  C CG2    . ILE A 1 270 ? -5.812  -19.669 -7.208  1.00 14.35  ?  270  ILE A CG2    1 
ATOM   4179  C CD1    . ILE A 1 270 ? -4.527  -21.576 -5.083  1.00 14.65  ?  270  ILE A CD1    1 
ATOM   4180  H H      . ILE A 1 270 ? -3.623  -17.485 -6.436  1.00 16.02  ?  270  ILE A H      1 
ATOM   4181  H HA     . ILE A 1 270 ? -6.256  -17.473 -5.813  1.00 17.25  ?  270  ILE A HA     1 
ATOM   4182  H HB     . ILE A 1 270 ? -6.219  -19.637 -5.176  1.00 16.76  ?  270  ILE A HB     1 
ATOM   4183  H HG12   . ILE A 1 270 ? -3.543  -20.002 -5.933  1.00 18.24  ?  270  ILE A HG12   1 
ATOM   4184  H HG13   . ILE A 1 270 ? -3.954  -19.732 -4.422  1.00 18.24  ?  270  ILE A HG13   1 
ATOM   4185  H HG21   . ILE A 1 270 ? -5.832  -20.633 -7.317  1.00 17.21  ?  270  ILE A HG21   1 
ATOM   4186  H HG22   . ILE A 1 270 ? -6.677  -19.293 -7.436  1.00 17.21  ?  270  ILE A HG22   1 
ATOM   4187  H HG23   . ILE A 1 270 ? -5.125  -19.287 -7.775  1.00 17.21  ?  270  ILE A HG23   1 
ATOM   4188  H HD11   . ILE A 1 270 ? -3.741  -22.001 -4.707  1.00 17.58  ?  270  ILE A HD11   1 
ATOM   4189  H HD12   . ILE A 1 270 ? -5.280  -21.680 -4.481  1.00 17.58  ?  270  ILE A HD12   1 
ATOM   4190  H HD13   . ILE A 1 270 ? -4.736  -21.970 -5.945  1.00 17.58  ?  270  ILE A HD13   1 
ATOM   4191  N N      . GLY A 1 271 ? -4.444  -16.281 -3.917  1.00 15.92  ?  271  GLY A N      1 
ATOM   4192  C CA     . GLY A 1 271 ? -4.236  -15.759 -2.581  1.00 14.23  ?  271  GLY A CA     1 
ATOM   4193  C C      . GLY A 1 271 ? -2.963  -16.202 -1.914  1.00 15.90  ?  271  GLY A C      1 
ATOM   4194  O O      . GLY A 1 271 ? -2.774  -15.917 -0.721  1.00 17.94  ?  271  GLY A O      1 
ATOM   4195  H H      . GLY A 1 271 ? -4.085  -15.811 -4.542  1.00 19.10  ?  271  GLY A H      1 
ATOM   4196  H HA2    . GLY A 1 271 ? -4.224  -14.790 -2.626  1.00 17.07  ?  271  GLY A HA2    1 
ATOM   4197  H HA3    . GLY A 1 271 ? -4.976  -16.041 -2.021  1.00 17.07  ?  271  GLY A HA3    1 
ATOM   4198  N N      . ALA A 1 272 ? -2.094  -16.896 -2.638  1.00 16.65  ?  272  ALA A N      1 
ATOM   4199  C CA     . ALA A 1 272 ? -0.798  -17.335 -2.168  1.00 15.86  ?  272  ALA A CA     1 
ATOM   4200  C C      . ALA A 1 272 ? 0.218   -17.001 -3.247  1.00 14.90  ?  272  ALA A C      1 
ATOM   4201  O O      . ALA A 1 272 ? -0.135  -16.715 -4.397  1.00 16.93  ?  272  ALA A O      1 
ATOM   4202  C CB     . ALA A 1 272 ? -0.780  -18.846 -1.911  1.00 19.93  ?  272  ALA A CB     1 
ATOM   4203  H H      . ALA A 1 272 ? -2.247  -17.135 -3.449  1.00 19.97  ?  272  ALA A H      1 
ATOM   4204  H HA     . ALA A 1 272 ? -0.573  -16.879 -1.342  1.00 19.03  ?  272  ALA A HA     1 
ATOM   4205  H HB1    . ALA A 1 272 ? 0.098   -19.100 -1.584  1.00 23.92  ?  272  ALA A HB1    1 
ATOM   4206  H HB2    . ALA A 1 272 ? -1.455  -19.062 -1.248  1.00 23.92  ?  272  ALA A HB2    1 
ATOM   4207  H HB3    . ALA A 1 272 ? -0.971  -19.310 -2.741  1.00 23.92  ?  272  ALA A HB3    1 
ATOM   4208  N N      . ASP A 1 273 ? 1.500   -17.045 -2.893  1.00 16.02  ?  273  ASP A N      1 
ATOM   4209  C CA     . ASP A 1 273 ? 2.518   -16.751 -3.893  1.00 16.85  ?  273  ASP A CA     1 
ATOM   4210  C C      . ASP A 1 273 ? 2.483   -17.765 -5.030  1.00 14.37  ?  273  ASP A C      1 
ATOM   4211  O O      . ASP A 1 273 ? 2.681   -17.401 -6.193  1.00 14.92  ?  273  ASP A O      1 
ATOM   4212  C CB     . ASP A 1 273 ? 3.899   -16.731 -3.255  1.00 18.11  ?  273  ASP A CB     1 
ATOM   4213  C CG     . ASP A 1 273 ? 4.070   -15.589 -2.271  1.00 20.19  ?  273  ASP A CG     1 
ATOM   4214  O OD1    . ASP A 1 273 ? 3.379   -14.554 -2.408  1.00 22.95  ?  273  ASP A OD1    1 
ATOM   4215  O OD2    . ASP A 1 273 ? 4.903   -15.724 -1.365  1.00 22.56  -1 273  ASP A OD2    1 
ATOM   4216  H H      . ASP A 1 273 ? 1.798   -17.235 -2.109  1.00 19.23  ?  273  ASP A H      1 
ATOM   4217  H HA     . ASP A 1 273 ? 2.342   -15.871 -4.258  1.00 20.22  ?  273  ASP A HA     1 
ATOM   4218  H HB2    . ASP A 1 273 ? 4.041   -17.563 -2.778  1.00 21.73  ?  273  ASP A HB2    1 
ATOM   4219  H HB3    . ASP A 1 273 ? 4.568   -16.630 -3.951  1.00 21.73  ?  273  ASP A HB3    1 
ATOM   4220  N N      . PHE A 1 274 ? 2.217   -19.039 -4.705  1.00 13.98  ?  274  PHE A N      1 
ATOM   4221  C CA     . PHE A 1 274 ? 2.020   -20.108 -5.675  1.00 13.63  ?  274  PHE A CA     1 
ATOM   4222  C C      . PHE A 1 274 ? 0.899   -21.000 -5.188  1.00 13.82  ?  274  PHE A C      1 
ATOM   4223  O O      . PHE A 1 274 ? 0.677   -21.123 -3.976  1.00 14.10  ?  274  PHE A O      1 
ATOM   4224  C CB     . PHE A 1 274 ? 3.300   -20.916 -5.867  1.00 13.07  ?  274  PHE A CB     1 
ATOM   4225  C CG     . PHE A 1 274 ? 4.357   -20.163 -6.608  1.00 13.28  ?  274  PHE A CG     1 
ATOM   4226  C CD1    . PHE A 1 274 ? 4.302   -20.066 -7.983  1.00 14.04  ?  274  PHE A CD1    1 
ATOM   4227  C CD2    . PHE A 1 274 ? 5.357   -19.491 -5.933  1.00 14.25  ?  274  PHE A CD2    1 
ATOM   4228  C CE1    . PHE A 1 274 ? 5.244   -19.341 -8.667  1.00 15.24  ?  274  PHE A CE1    1 
ATOM   4229  C CE2    . PHE A 1 274 ? 6.293   -18.764 -6.623  1.00 16.04  ?  274  PHE A CE2    1 
ATOM   4230  C CZ     . PHE A 1 274 ? 6.243   -18.703 -7.991  1.00 16.54  ?  274  PHE A CZ     1 
ATOM   4231  H H      . PHE A 1 274 ? 2.145   -19.312 -3.893  1.00 16.77  ?  274  PHE A H      1 
ATOM   4232  H HA     . PHE A 1 274 ? 1.763   -19.744 -6.537  1.00 16.35  ?  274  PHE A HA     1 
ATOM   4233  H HB2    . PHE A 1 274 ? 3.656   -21.154 -4.997  1.00 15.68  ?  274  PHE A HB2    1 
ATOM   4234  H HB3    . PHE A 1 274 ? 3.094   -21.718 -6.372  1.00 15.68  ?  274  PHE A HB3    1 
ATOM   4235  H HD1    . PHE A 1 274 ? 3.621   -20.495 -8.450  1.00 16.85  ?  274  PHE A HD1    1 
ATOM   4236  H HD2    . PHE A 1 274 ? 5.395   -19.531 -5.005  1.00 17.10  ?  274  PHE A HD2    1 
ATOM   4237  H HE1    . PHE A 1 274 ? 5.202   -19.284 -9.595  1.00 18.28  ?  274  PHE A HE1    1 
ATOM   4238  H HE2    . PHE A 1 274 ? 6.963   -18.312 -6.162  1.00 19.25  ?  274  PHE A HE2    1 
ATOM   4239  H HZ     . PHE A 1 274 ? 6.890   -18.227 -8.459  1.00 19.85  ?  274  PHE A HZ     1 
ATOM   4240  N N      . GLY A 1 275 ? 0.188   -21.637 -6.140  1.00 13.60  ?  275  GLY A N      1 
ATOM   4241  C CA     . GLY A 1 275 ? -0.842  -22.576 -5.744  1.00 14.48  ?  275  GLY A CA     1 
ATOM   4242  C C      . GLY A 1 275 ? -0.262  -23.743 -4.970  1.00 13.66  ?  275  GLY A C      1 
ATOM   4243  O O      . GLY A 1 275 ? -0.919  -24.291 -4.084  1.00 13.81  ?  275  GLY A O      1 
ATOM   4244  H H      . GLY A 1 275 ? 0.287   -21.539 -6.988  1.00 16.31  ?  275  GLY A H      1 
ATOM   4245  H HA2    . GLY A 1 275 ? -1.493  -22.126 -5.183  1.00 17.38  ?  275  GLY A HA2    1 
ATOM   4246  H HA3    . GLY A 1 275 ? -1.289  -22.919 -6.533  1.00 17.38  ?  275  GLY A HA3    1 
ATOM   4247  N N      . SER A 1 276 ? 0.976   -24.125 -5.289  1.00 13.98  ?  276  SER A N      1 
ATOM   4248  C CA     . SER A 1 276 ? 1.650   -25.187 -4.551  1.00 13.97  ?  276  SER A CA     1 
ATOM   4249  C C      . SER A 1 276 ? 1.760   -24.860 -3.071  1.00 15.53  ?  276  SER A C      1 
ATOM   4250  O O      . SER A 1 276 ? 1.690   -25.758 -2.227  1.00 14.41  ?  276  SER A O      1 
ATOM   4251  C CB     . SER A 1 276 ? 3.032   -25.429 -5.140  1.00 14.56  ?  276  SER A CB     1 
ATOM   4252  O OG     . SER A 1 276 ? 2.964   -26.016 -6.425  1.00 15.17  ?  276  SER A OG     1 
ATOM   4253  H H      . SER A 1 276 ? 1.446   -23.787 -5.925  1.00 16.77  ?  276  SER A H      1 
ATOM   4254  H HA     . SER A 1 276 ? 1.129   -26.001 -4.639  1.00 16.76  ?  276  SER A HA     1 
ATOM   4255  H HB2    . SER A 1 276 ? 3.494   -24.579 -5.211  1.00 17.47  ?  276  SER A HB2    1 
ATOM   4256  H HB3    . SER A 1 276 ? 3.522   -26.024 -4.552  1.00 17.47  ?  276  SER A HB3    1 
ATOM   4257  H HG     . SER A 1 276 ? 2.499   -25.537 -6.935  1.00 18.20  ?  276  SER A HG     1 
ATOM   4258  N N      . HIS A 1 277 ? 1.981   -23.592 -2.726  1.00 16.52  ?  277  HIS A N      1 
ATOM   4259  C CA     . HIS A 1 277 ? 2.072   -23.229 -1.316  1.00 14.01  ?  277  HIS A CA     1 
ATOM   4260  C C      . HIS A 1 277 ? 0.732   -23.436 -0.627  1.00 15.33  ?  277  HIS A C      1 
ATOM   4261  O O      . HIS A 1 277 ? 0.663   -23.962 0.492   1.00 18.24  ?  277  HIS A O      1 
ATOM   4262  C CB     . HIS A 1 277 ? 2.475   -21.771 -1.183  1.00 15.26  ?  277  HIS A CB     1 
ATOM   4263  C CG     . HIS A 1 277 ? 3.842   -21.464 -1.695  1.00 16.75  ?  277  HIS A CG     1 
ATOM   4264  N ND1    . HIS A 1 277 ? 4.363   -20.188 -1.686  1.00 18.46  ?  277  HIS A ND1    1 
ATOM   4265  C CD2    . HIS A 1 277 ? 4.799   -22.258 -2.230  1.00 16.58  ?  277  HIS A CD2    1 
ATOM   4266  C CE1    . HIS A 1 277 ? 5.589   -20.213 -2.183  1.00 19.94  ?  277  HIS A CE1    1 
ATOM   4267  N NE2    . HIS A 1 277 ? 5.870   -21.454 -2.536  1.00 18.65  ?  277  HIS A NE2    1 
ATOM   4268  H H      . HIS A 1 277 ? 2.080   -22.937 -3.275  1.00 19.83  ?  277  HIS A H      1 
ATOM   4269  H HA     . HIS A 1 277 ? 2.745   -23.784 -0.891  1.00 16.80  ?  277  HIS A HA     1 
ATOM   4270  H HB2    . HIS A 1 277 ? 1.845   -21.228 -1.682  1.00 18.31  ?  277  HIS A HB2    1 
ATOM   4271  H HB3    . HIS A 1 277 ? 2.452   -21.527 -0.244  1.00 18.31  ?  277  HIS A HB3    1 
ATOM   4272  H HD2    . HIS A 1 277 ? 4.742   -23.176 -2.365  1.00 19.89  ?  277  HIS A HD2    1 
ATOM   4273  H HE1    . HIS A 1 277 ? 6.156   -19.481 -2.269  1.00 23.93  ?  277  HIS A HE1    1 
ATOM   4274  H HE2    . HIS A 1 277 ? 6.605   -21.716 -2.899  1.00 22.37  ?  277  HIS A HE2    1 
ATOM   4275  N N      . HIS A 1 278 ? -0.342  -23.050 -1.305  1.00 14.57  ?  278  HIS A N      1 
ATOM   4276  C CA     . HIS A 1 278 ? -1.674  -23.142 -0.727  1.00 15.96  ?  278  HIS A CA     1 
ATOM   4277  C C      . HIS A 1 278 ? -2.094  -24.584 -0.470  1.00 16.02  ?  278  HIS A C      1 
ATOM   4278  O O      . HIS A 1 278 ? -2.717  -24.876 0.560   1.00 17.86  ?  278  HIS A O      1 
ATOM   4279  C CB     . HIS A 1 278 ? -2.667  -22.490 -1.688  1.00 16.72  ?  278  HIS A CB     1 
ATOM   4280  C CG     . HIS A 1 278 ? -4.039  -22.368 -1.130  1.00 17.74  ?  278  HIS A CG     1 
ATOM   4281  N ND1    . HIS A 1 278 ? -4.361  -21.445 -0.159  1.00 21.80  ?  278  HIS A ND1    1 
ATOM   4282  C CD2    . HIS A 1 278 ? -5.171  -23.064 -1.388  1.00 20.03  ?  278  HIS A CD2    1 
ATOM   4283  C CE1    . HIS A 1 278 ? -5.639  -21.574 0.151   1.00 23.41  ?  278  HIS A CE1    1 
ATOM   4284  N NE2    . HIS A 1 278 ? -6.154  -22.544 -0.585  1.00 22.04  ?  278  HIS A NE2    1 
ATOM   4285  H H      . HIS A 1 278 ? -0.329  -22.730 -2.103  1.00 17.48  ?  278  HIS A H      1 
ATOM   4286  H HA     . HIS A 1 278 ? -1.676  -22.678 0.124   1.00 19.15  ?  278  HIS A HA     1 
ATOM   4287  H HB2    . HIS A 1 278 ? -2.354  -21.598 -1.904  1.00 20.06  ?  278  HIS A HB2    1 
ATOM   4288  H HB3    . HIS A 1 278 ? -2.721  -23.027 -2.494  1.00 20.06  ?  278  HIS A HB3    1 
ATOM   4289  H HD2    . HIS A 1 278 ? -5.265  -23.762 -1.996  1.00 24.04  ?  278  HIS A HD2    1 
ATOM   4290  H HE1    . HIS A 1 278 ? -6.099  -21.067 0.780   1.00 28.09  ?  278  HIS A HE1    1 
ATOM   4291  H HE2    . HIS A 1 278 ? -6.972  -22.806 -0.563  1.00 26.45  ?  278  HIS A HE2    1 
ATOM   4292  N N      . TYR A 1 279 ? -1.760  -25.500 -1.388  1.00 15.02  ?  279  TYR A N      1 
ATOM   4293  C CA     . TYR A 1 279 ? -2.179  -26.894 -1.340  1.00 14.94  ?  279  TYR A CA     1 
ATOM   4294  C C      . TYR A 1 279 ? -1.100  -27.842 -0.821  1.00 14.94  ?  279  TYR A C      1 
ATOM   4295  O O      . TYR A 1 279 ? -1.294  -29.057 -0.856  1.00 14.73  ?  279  TYR A O      1 
ATOM   4296  C CB     . TYR A 1 279 ? -2.705  -27.346 -2.718  1.00 14.59  ?  279  TYR A CB     1 
ATOM   4297  C CG     . TYR A 1 279 ? -4.000  -26.671 -3.100  1.00 14.45  ?  279  TYR A CG     1 
ATOM   4298  C CD1    . TYR A 1 279 ? -5.173  -26.953 -2.416  1.00 14.71  ?  279  TYR A CD1    1 
ATOM   4299  C CD2    . TYR A 1 279 ? -4.051  -25.750 -4.130  1.00 15.64  ?  279  TYR A CD2    1 
ATOM   4300  C CE1    . TYR A 1 279 ? -6.347  -26.327 -2.749  1.00 15.65  ?  279  TYR A CE1    1 
ATOM   4301  C CE2    . TYR A 1 279 ? -5.230  -25.132 -4.470  1.00 14.92  ?  279  TYR A CE2    1 
ATOM   4302  C CZ     . TYR A 1 279 ? -6.369  -25.426 -3.763  1.00 16.19  ?  279  TYR A CZ     1 
ATOM   4303  O OH     . TYR A 1 279 ? -7.560  -24.809 -4.093  1.00 16.89  ?  279  TYR A OH     1 
ATOM   4304  H H      . TYR A 1 279 ? -1.272  -25.323 -2.074  1.00 18.02  ?  279  TYR A H      1 
ATOM   4305  H HA     . TYR A 1 279 ? -2.919  -26.961 -0.717  1.00 17.93  ?  279  TYR A HA     1 
ATOM   4306  H HB2    . TYR A 1 279 ? -2.043  -27.131 -3.394  1.00 17.50  ?  279  TYR A HB2    1 
ATOM   4307  H HB3    . TYR A 1 279 ? -2.860  -28.303 -2.698  1.00 17.50  ?  279  TYR A HB3    1 
ATOM   4308  H HD1    . TYR A 1 279 ? -5.163  -27.574 -1.724  1.00 17.65  ?  279  TYR A HD1    1 
ATOM   4309  H HD2    . TYR A 1 279 ? -3.275  -25.545 -4.600  1.00 18.76  ?  279  TYR A HD2    1 
ATOM   4310  H HE1    . TYR A 1 279 ? -7.127  -26.520 -2.281  1.00 18.77  ?  279  TYR A HE1    1 
ATOM   4311  H HE2    . TYR A 1 279 ? -5.256  -24.521 -5.171  1.00 17.90  ?  279  TYR A HE2    1 
ATOM   4312  H HH     . TYR A 1 279 ? -7.434  -24.255 -4.711  1.00 20.27  ?  279  TYR A HH     1 
ATOM   4313  N N      . ALA A 1 280 ? 0.011   -27.318 -0.307  1.00 13.81  ?  280  ALA A N      1 
ATOM   4314  C CA     . ALA A 1 280 ? 1.088   -28.142 0.246   1.00 14.33  ?  280  ALA A CA     1 
ATOM   4315  C C      . ALA A 1 280 ? 1.639   -29.113 -0.792  1.00 14.98  ?  280  ALA A C      1 
ATOM   4316  O O      . ALA A 1 280 ? 1.880   -30.296 -0.510  1.00 15.80  ?  280  ALA A O      1 
ATOM   4317  C CB     . ALA A 1 280 ? 0.671   -28.858 1.536   1.00 15.52  ?  280  ALA A CB     1 
ATOM   4318  H H      . ALA A 1 280 ? 0.169   -26.473 -0.267  1.00 16.57  ?  280  ALA A H      1 
ATOM   4319  H HA     . ALA A 1 280 ? 1.816   -27.549 0.488   1.00 17.19  ?  280  ALA A HA     1 
ATOM   4320  H HB1    . ALA A 1 280 ? 1.443   -29.310 1.910   1.00 18.62  ?  280  ALA A HB1    1 
ATOM   4321  H HB2    . ALA A 1 280 ? 0.334   -28.202 2.166   1.00 18.62  ?  280  ALA A HB2    1 
ATOM   4322  H HB3    . ALA A 1 280 ? -0.023  -29.504 1.329   1.00 18.62  ?  280  ALA A HB3    1 
ATOM   4323  N N      . ILE A 1 281 ? 1.861   -28.608 -1.984  1.00 12.98  ?  281  ILE A N      1 
ATOM   4324  C CA     . ILE A 1 281 ? 2.500   -29.360 -3.054  1.00 13.44  ?  281  ILE A CA     1 
ATOM   4325  C C      . ILE A 1 281 ? 3.986   -29.053 -3.008  1.00 12.92  ?  281  ILE A C      1 
ATOM   4326  O O      . ILE A 1 281 ? 4.378   -27.890 -2.882  1.00 14.90  ?  281  ILE A O      1 
ATOM   4327  C CB     . ILE A 1 281 ? 1.921   -28.967 -4.427  1.00 13.34  ?  281  ILE A CB     1 
ATOM   4328  C CG1    . ILE A 1 281 ? 0.391   -29.062 -4.433  1.00 13.00  ?  281  ILE A CG1    1 
ATOM   4329  C CG2    . ILE A 1 281 ? 2.494   -29.886 -5.496  1.00 15.26  ?  281  ILE A CG2    1 
ATOM   4330  C CD1    . ILE A 1 281 ? -0.255  -28.524 -5.707  1.00 13.01  ?  281  ILE A CD1    1 
ATOM   4331  H H      . ILE A 1 281 ? 1.645   -27.806 -2.210  1.00 15.57  ?  281  ILE A H      1 
ATOM   4332  H HA     . ILE A 1 281 ? 2.351   -30.309 -2.918  1.00 16.13  ?  281  ILE A HA     1 
ATOM   4333  H HB     . ILE A 1 281 ? 2.168   -28.046 -4.608  1.00 16.00  ?  281  ILE A HB     1 
ATOM   4334  H HG12   . ILE A 1 281 ? 0.136   -29.994 -4.343  1.00 15.60  ?  281  ILE A HG12   1 
ATOM   4335  H HG13   . ILE A 1 281 ? 0.044   -28.550 -3.686  1.00 15.60  ?  281  ILE A HG13   1 
ATOM   4336  H HG21   . ILE A 1 281 ? 2.206   -29.574 -6.368  1.00 18.30  ?  281  ILE A HG21   1 
ATOM   4337  H HG22   . ILE A 1 281 ? 3.462   -29.869 -5.442  1.00 18.30  ?  281  ILE A HG22   1 
ATOM   4338  H HG23   . ILE A 1 281 ? 2.170   -30.788 -5.344  1.00 18.30  ?  281  ILE A HG23   1 
ATOM   4339  H HD11   . ILE A 1 281 ? -1.214  -28.469 -5.575  1.00 15.61  ?  281  ILE A HD11   1 
ATOM   4340  H HD12   . ILE A 1 281 ? 0.105   -27.643 -5.895  1.00 15.61  ?  281  ILE A HD12   1 
ATOM   4341  H HD13   . ILE A 1 281 ? -0.055  -29.126 -6.440  1.00 15.61  ?  281  ILE A HD13   1 
ATOM   4342  N N      . LYS A 1 282 ? 4.820   -30.092 -3.116  1.00 14.08  ?  282  LYS A N      1 
ATOM   4343  C CA     . LYS A 1 282 ? 6.278   -29.958 -3.079  1.00 14.53  ?  282  LYS A CA     1 
ATOM   4344  C C      . LYS A 1 282 ? 6.840   -30.425 -4.421  1.00 13.23  ?  282  LYS A C      1 
ATOM   4345  O O      . LYS A 1 282 ? 7.333   -31.553 -4.548  1.00 15.07  ?  282  LYS A O      1 
ATOM   4346  C CB     . LYS A 1 282 ? 6.871   -30.774 -1.935  1.00 18.66  ?  282  LYS A CB     1 
ATOM   4347  C CG     . LYS A 1 282 ? 6.347   -30.369 -0.578  1.00 25.28  ?  282  LYS A CG     1 
ATOM   4348  C CD     . LYS A 1 282 ? 6.635   -28.916 -0.248  1.00 34.33  ?  282  LYS A CD     1 
ATOM   4349  C CE     . LYS A 1 282 ? 6.106   -28.559 1.134   1.00 41.16  ?  282  LYS A CE     1 
ATOM   4350  N NZ     . LYS A 1 282 ? 6.041   -27.083 1.347   1.00 45.94  ?  282  LYS A NZ     1 
ATOM   4351  H H      . LYS A 1 282 ? 4.554   -30.904 -3.215  1.00 16.90  ?  282  LYS A H      1 
ATOM   4352  H HA     . LYS A 1 282 ? 6.511   -29.025 -2.957  1.00 17.43  ?  282  LYS A HA     1 
ATOM   4353  H HB2    . LYS A 1 282 ? 6.653   -31.710 -2.071  1.00 22.39  ?  282  LYS A HB2    1 
ATOM   4354  H HB3    . LYS A 1 282 ? 7.833   -30.655 -1.930  1.00 22.39  ?  282  LYS A HB3    1 
ATOM   4355  H HG2    . LYS A 1 282 ? 5.385   -30.496 -0.560  1.00 30.33  ?  282  LYS A HG2    1 
ATOM   4356  H HG3    . LYS A 1 282 ? 6.767   -30.920 0.101   1.00 30.33  ?  282  LYS A HG3    1 
ATOM   4357  H HD2    . LYS A 1 282 ? 7.593   -28.765 -0.259  1.00 41.19  ?  282  LYS A HD2    1 
ATOM   4358  H HD3    . LYS A 1 282 ? 6.201   -28.343 -0.900  1.00 41.19  ?  282  LYS A HD3    1 
ATOM   4359  H HE2    . LYS A 1 282 ? 5.212   -28.920 1.236   1.00 49.39  ?  282  LYS A HE2    1 
ATOM   4360  H HE3    . LYS A 1 282 ? 6.694   -28.936 1.807   1.00 49.39  ?  282  LYS A HE3    1 
ATOM   4361  H HZ1    . LYS A 1 282 ? 5.781   -26.907 2.180   1.00 55.12  ?  282  LYS A HZ1    1 
ATOM   4362  H HZ2    . LYS A 1 282 ? 6.842   -26.720 1.212   1.00 55.12  ?  282  LYS A HZ2    1 
ATOM   4363  H HZ3    . LYS A 1 282 ? 5.460   -26.720 0.780   1.00 55.12  ?  282  LYS A HZ3    1 
ATOM   4364  N N      . PRO A 1 283 ? 6.783   -29.583 -5.440  1.00 13.28  ?  283  PRO A N      1 
ATOM   4365  C CA     . PRO A 1 283 ? 7.234   -29.997 -6.768  1.00 13.21  ?  283  PRO A CA     1 
ATOM   4366  C C      . PRO A 1 283 ? 8.749   -30.025 -6.902  1.00 12.05  ?  283  PRO A C      1 
ATOM   4367  O O      . PRO A 1 283 ? 9.487   -29.345 -6.190  1.00 13.31  ?  283  PRO A O      1 
ATOM   4368  C CB     . PRO A 1 283 ? 6.643   -28.915 -7.688  1.00 14.42  ?  283  PRO A CB     1 
ATOM   4369  C CG     . PRO A 1 283 ? 6.587   -27.695 -6.788  1.00 14.90  ?  283  PRO A CG     1 
ATOM   4370  C CD     . PRO A 1 283 ? 6.276   -28.194 -5.432  1.00 14.58  ?  283  PRO A CD     1 
ATOM   4371  H HA     . PRO A 1 283 ? 6.875   -30.872 -6.984  1.00 15.85  ?  283  PRO A HA     1 
ATOM   4372  H HB2    . PRO A 1 283 ? 7.224   -28.766 -8.450  1.00 17.30  ?  283  PRO A HB2    1 
ATOM   4373  H HB3    . PRO A 1 283 ? 5.759   -29.174 -7.990  1.00 17.30  ?  283  PRO A HB3    1 
ATOM   4374  H HG2    . PRO A 1 283 ? 7.445   -27.243 -6.798  1.00 17.87  ?  283  PRO A HG2    1 
ATOM   4375  H HG3    . PRO A 1 283 ? 5.892   -27.093 -7.099  1.00 17.87  ?  283  PRO A HG3    1 
ATOM   4376  H HD2    . PRO A 1 283 ? 6.733   -27.666 -4.759  1.00 17.49  ?  283  PRO A HD2    1 
ATOM   4377  H HD3    . PRO A 1 283 ? 5.319   -28.179 -5.272  1.00 17.49  ?  283  PRO A HD3    1 
ATOM   4378  N N      . ASP A 1 284 ? 9.200   -30.818 -7.879  1.00 13.09  ?  284  ASP A N      1 
ATOM   4379  C CA     . ASP A 1 284 ? 10.591  -30.836 -8.299  1.00 12.15  ?  284  ASP A CA     1 
ATOM   4380  C C      . ASP A 1 284 ? 10.910  -29.776 -9.341  1.00 11.27  ?  284  ASP A C      1 
ATOM   4381  O O      . ASP A 1 284 ? 12.070  -29.359 -9.444  1.00 13.32  ?  284  ASP A O      1 
ATOM   4382  C CB     . ASP A 1 284 ? 10.939  -32.202 -8.887  1.00 13.97  ?  284  ASP A CB     1 
ATOM   4383  C CG     . ASP A 1 284 ? 10.754  -33.330 -7.890  1.00 15.90  ?  284  ASP A CG     1 
ATOM   4384  O OD1    . ASP A 1 284 ? 11.554  -33.449 -6.943  1.00 21.14  ?  284  ASP A OD1    1 
ATOM   4385  O OD2    . ASP A 1 284 ? 9.776   -34.098 -8.041  1.00 15.69  -1 284  ASP A OD2    1 
ATOM   4386  H H      . ASP A 1 284 ? 8.705   -31.364 -8.321  1.00 15.70  ?  284  ASP A H      1 
ATOM   4387  H HA     . ASP A 1 284 ? 11.145  -30.677 -7.518  1.00 14.57  ?  284  ASP A HA     1 
ATOM   4388  H HB2    . ASP A 1 284 ? 10.363  -32.375 -9.648  1.00 16.76  ?  284  ASP A HB2    1 
ATOM   4389  H HB3    . ASP A 1 284 ? 11.868  -32.198 -9.167  1.00 16.76  ?  284  ASP A HB3    1 
ATOM   4390  N N      . LEU A 1 285 ? 9.902   -29.359 -10.110 1.00 12.87  ?  285  LEU A N      1 
ATOM   4391  C CA     . LEU A 1 285 ? 10.010  -28.448 -11.240 1.00 12.16  ?  285  LEU A CA     1 
ATOM   4392  C C      . LEU A 1 285 ? 8.732   -27.618 -11.250 1.00 11.48  ?  285  LEU A C      1 
ATOM   4393  O O      . LEU A 1 285 ? 7.653   -28.139 -10.946 1.00 11.92  ?  285  LEU A O      1 
ATOM   4394  C CB     . LEU A 1 285 ? 10.100  -29.255 -12.541 1.00 12.05  ?  285  LEU A CB     1 
ATOM   4395  C CG     . LEU A 1 285 ? 11.386  -30.058 -12.730 1.00 13.01  ?  285  LEU A CG     1 
ATOM   4396  C CD1    . LEU A 1 285 ? 11.253  -31.097 -13.821 1.00 14.40  ?  285  LEU A CD1    1 
ATOM   4397  C CD2    . LEU A 1 285 ? 12.508  -29.114 -13.099 1.00 13.48  ?  285  LEU A CD2    1 
ATOM   4398  H H      . LEU A 1 285 ? 9.089   -29.610 -9.985  1.00 15.44  ?  285  LEU A H      1 
ATOM   4399  H HA     . LEU A 1 285 ? 10.784  -27.866 -11.167 1.00 14.59  ?  285  LEU A HA     1 
ATOM   4400  H HB2    . LEU A 1 285 ? 9.362   -29.884 -12.561 1.00 14.46  ?  285  LEU A HB2    1 
ATOM   4401  H HB3    . LEU A 1 285 ? 10.032  -28.639 -13.287 1.00 14.46  ?  285  LEU A HB3    1 
ATOM   4402  H HG     . LEU A 1 285 ? 11.580  -30.521 -11.900 1.00 15.60  ?  285  LEU A HG     1 
ATOM   4403  H HD11   . LEU A 1 285 ? 12.108  -31.540 -13.942 1.00 17.27  ?  285  LEU A HD11   1 
ATOM   4404  H HD12   . LEU A 1 285 ? 10.580  -31.745 -13.560 1.00 17.27  ?  285  LEU A HD12   1 
ATOM   4405  H HD13   . LEU A 1 285 ? 10.989  -30.658 -14.645 1.00 17.27  ?  285  LEU A HD13   1 
ATOM   4406  H HD21   . LEU A 1 285 ? 13.337  -29.614 -13.150 1.00 16.18  ?  285  LEU A HD21   1 
ATOM   4407  H HD22   . LEU A 1 285 ? 12.311  -28.711 -13.959 1.00 16.18  ?  285  LEU A HD22   1 
ATOM   4408  H HD23   . LEU A 1 285 ? 12.578  -28.426 -12.419 1.00 16.18  ?  285  LEU A HD23   1 
ATOM   4409  N N      . ILE A 1 286 ? 8.841   -26.346 -11.618 1.00 11.48  ?  286  ILE A N      1 
ATOM   4410  C CA     . ILE A 1 286 ? 7.690   -25.435 -11.663 1.00 11.57  ?  286  ILE A CA     1 
ATOM   4411  C C      . ILE A 1 286 ? 7.676   -24.692 -12.996 1.00 10.93  ?  286  ILE A C      1 
ATOM   4412  O O      . ILE A 1 286 ? 8.700   -24.143 -13.406 1.00 11.82  ?  286  ILE A O      1 
ATOM   4413  C CB     . ILE A 1 286 ? 7.723   -24.426 -10.495 1.00 11.84  ?  286  ILE A CB     1 
ATOM   4414  C CG1    . ILE A 1 286 ? 7.730   -25.151 -9.158  1.00 12.28  ?  286  ILE A CG1    1 
ATOM   4415  C CG2    . ILE A 1 286 ? 6.540   -23.486 -10.596 1.00 13.53  ?  286  ILE A CG2    1 
ATOM   4416  C CD1    . ILE A 1 286 ? 7.942   -24.226 -7.960  1.00 12.95  ?  286  ILE A CD1    1 
ATOM   4417  H H      . ILE A 1 286 ? 9.583   -25.979 -11.851 1.00 13.77  ?  286  ILE A H      1 
ATOM   4418  H HA     . ILE A 1 286 ? 6.877   -25.962 -11.611 1.00 13.89  ?  286  ILE A HA     1 
ATOM   4419  H HB     . ILE A 1 286 ? 8.541   -23.907 -10.554 1.00 14.21  ?  286  ILE A HB     1 
ATOM   4420  H HG12   . ILE A 1 286 ? 6.876   -25.597 -9.040  1.00 14.74  ?  286  ILE A HG12   1 
ATOM   4421  H HG13   . ILE A 1 286 ? 8.447   -25.803 -9.160  1.00 14.74  ?  286  ILE A HG13   1 
ATOM   4422  H HG21   . ILE A 1 286 ? 6.516   -22.923 -9.806  1.00 16.23  ?  286  ILE A HG21   1 
ATOM   4423  H HG22   . ILE A 1 286 ? 6.639   -22.938 -11.390 1.00 16.23  ?  286  ILE A HG22   1 
ATOM   4424  H HG23   . ILE A 1 286 ? 5.726   -24.009 -10.654 1.00 16.23  ?  286  ILE A HG23   1 
ATOM   4425  H HD11   . ILE A 1 286 ? 8.083   -24.764 -7.166  1.00 15.54  ?  286  ILE A HD11   1 
ATOM   4426  H HD12   . ILE A 1 286 ? 8.720   -23.670 -8.125  1.00 15.54  ?  286  ILE A HD12   1 
ATOM   4427  H HD13   . ILE A 1 286 ? 7.156   -23.669 -7.847  1.00 15.54  ?  286  ILE A HD13   1 
ATOM   4428  N N      . THR A 1 287 ? 6.505   -24.634 -13.635 1.00 11.85  ?  287  THR A N      1 
ATOM   4429  C CA     . THR A 1 287 ? 6.282   -23.834 -14.838 1.00 10.17  ?  287  THR A CA     1 
ATOM   4430  C C      . THR A 1 287 ? 5.594   -22.525 -14.465 1.00 11.24  ?  287  THR A C      1 
ATOM   4431  O O      . THR A 1 287 ? 4.579   -22.545 -13.760 1.00 11.59  ?  287  THR A O      1 
ATOM   4432  C CB     . THR A 1 287 ? 5.374   -24.595 -15.818 1.00 10.25  ?  287  THR A CB     1 
ATOM   4433  O OG1    . THR A 1 287 ? 5.852   -25.944 -15.913 1.00 13.04  ?  287  THR A OG1    1 
ATOM   4434  C CG2    . THR A 1 287 ? 5.368   -23.938 -17.185 1.00 12.42  ?  287  THR A CG2    1 
ATOM   4435  H H      . THR A 1 287 ? 5.805   -25.065 -13.381 1.00 14.22  ?  287  THR A H      1 
ATOM   4436  H HA     . THR A 1 287 ? 7.136   -23.640 -15.255 1.00 12.20  ?  287  THR A HA     1 
ATOM   4437  H HB     . THR A 1 287 ? 4.457   -24.589 -15.502 1.00 12.30  ?  287  THR A HB     1 
ATOM   4438  H HG1    . THR A 1 287 ? 5.405   -26.368 -16.484 1.00 15.64  ?  287  THR A HG1    1 
ATOM   4439  H HG21   . THR A 1 287 ? 4.734   -24.388 -17.766 1.00 14.90  ?  287  THR A HG21   1 
ATOM   4440  H HG22   . THR A 1 287 ? 5.113   -23.006 -17.104 1.00 14.90  ?  287  THR A HG22   1 
ATOM   4441  H HG23   . THR A 1 287 ? 6.251   -23.990 -17.582 1.00 14.90  ?  287  THR A HG23   1 
ATOM   4442  N N      . ILE A 1 288 ? 6.100   -21.404 -14.990 1.00 11.97  ?  288  ILE A N      1 
ATOM   4443  C CA     . ILE A 1 288 ? 5.527   -20.084 -14.762 1.00 11.50  ?  288  ILE A CA     1 
ATOM   4444  C C      . ILE A 1 288 ? 5.426   -19.301 -16.070 1.00 13.36  ?  288  ILE A C      1 
ATOM   4445  O O      . ILE A 1 288 ? 6.233   -19.470 -16.991 1.00 12.66  ?  288  ILE A O      1 
ATOM   4446  C CB     . ILE A 1 288 ? 6.284   -19.248 -13.707 1.00 11.73  ?  288  ILE A CB     1 
ATOM   4447  C CG1    . ILE A 1 288 ? 7.751   -19.088 -14.087 1.00 12.74  ?  288  ILE A CG1    1 
ATOM   4448  C CG2    . ILE A 1 288 ? 6.147   -19.849 -12.342 1.00 13.47  ?  288  ILE A CG2    1 
ATOM   4449  C CD1    . ILE A 1 288 ? 8.559   -18.247 -13.113 1.00 14.01  ?  288  ILE A CD1    1 
ATOM   4450  H H      . ILE A 1 288 ? 6.796   -21.389 -15.495 1.00 14.37  ?  288  ILE A H      1 
ATOM   4451  H HA     . ILE A 1 288 ? 4.627   -20.236 -14.435 1.00 13.80  ?  288  ILE A HA     1 
ATOM   4452  H HB     . ILE A 1 288 ? 5.880   -18.366 -13.688 1.00 14.08  ?  288  ILE A HB     1 
ATOM   4453  H HG12   . ILE A 1 288 ? 8.159   -19.968 -14.125 1.00 15.29  ?  288  ILE A HG12   1 
ATOM   4454  H HG13   . ILE A 1 288 ? 7.801   -18.662 -14.956 1.00 15.29  ?  288  ILE A HG13   1 
ATOM   4455  H HG21   . ILE A 1 288 ? 6.465   -19.212 -11.683 1.00 16.17  ?  288  ILE A HG21   1 
ATOM   4456  H HG22   . ILE A 1 288 ? 5.213   -20.054 -12.179 1.00 16.17  ?  288  ILE A HG22   1 
ATOM   4457  H HG23   . ILE A 1 288 ? 6.676   -20.661 -12.300 1.00 16.17  ?  288  ILE A HG23   1 
ATOM   4458  H HD11   . ILE A 1 288 ? 9.436   -18.079 -13.493 1.00 16.81  ?  288  ILE A HD11   1 
ATOM   4459  H HD12   . ILE A 1 288 ? 8.098   -17.407 -12.962 1.00 16.81  ?  288  ILE A HD12   1 
ATOM   4460  H HD13   . ILE A 1 288 ? 8.649   -18.730 -12.277 1.00 16.81  ?  288  ILE A HD13   1 
ATOM   4461  N N      . ALA A 1 289 ? 4.428   -18.405 -16.122 1.00 12.70  ?  289  ALA A N      1 
ATOM   4462  C CA     . ALA A 1 289 ? 4.265   -17.396 -17.158 1.00 13.00  ?  289  ALA A CA     1 
ATOM   4463  C C      . ALA A 1 289 ? 3.166   -16.438 -16.681 1.00 13.92  ?  289  ALA A C      1 
ATOM   4464  O O      . ALA A 1 289 ? 3.098   -16.124 -15.489 1.00 15.10  ?  289  ALA A O      1 
ATOM   4465  C CB     . ALA A 1 289 ? 3.977   -18.036 -18.514 1.00 14.55  ?  289  ALA A CB     1 
ATOM   4466  H H      . ALA A 1 289 ? 3.802   -18.366 -15.533 1.00 15.24  ?  289  ALA A H      1 
ATOM   4467  H HA     . ALA A 1 289 ? 5.078   -16.888 -17.309 1.00 15.60  ?  289  ALA A HA     1 
ATOM   4468  H HB1    . ALA A 1 289 ? 3.944   -17.342 -19.191 1.00 17.46  ?  289  ALA A HB1    1 
ATOM   4469  H HB2    . ALA A 1 289 ? 4.684   -18.667 -18.722 1.00 17.46  ?  289  ALA A HB2    1 
ATOM   4470  H HB3    . ALA A 1 289 ? 3.124   -18.497 -18.471 1.00 17.46  ?  289  ALA A HB3    1 
HETATM 4471  N N1     . LLP A 1 290 ? -0.064  -23.999 -18.623 1.00 16.14  ?  290  LLP A N1     1 
HETATM 4472  C C2     . LLP A 1 290 ? -1.122  -23.483 -18.068 1.00 16.91  ?  290  LLP A C2     1 
HETATM 4473  C "C2'"  . LLP A 1 290 ? -1.601  -24.025 -16.777 1.00 21.59  ?  290  LLP A "C2'"  1 
HETATM 4474  C C3     . LLP A 1 290 ? -1.773  -22.413 -18.683 1.00 28.68  ?  290  LLP A C3     1 
HETATM 4475  O O3     . LLP A 1 290 ? -2.878  -21.841 -18.200 1.00 24.83  ?  290  LLP A O3     1 
HETATM 4476  C C4     . LLP A 1 290 ? -1.282  -21.923 -19.869 1.00 15.21  ?  290  LLP A C4     1 
HETATM 4477  C "C4'"  . LLP A 1 290 ? -1.987  -20.781 -20.489 1.00 41.70  ?  290  LLP A "C4'"  1 
HETATM 4478  C C5     . LLP A 1 290 ? -0.159  -22.478 -20.441 1.00 15.37  ?  290  LLP A C5     1 
HETATM 4479  C C6     . LLP A 1 290 ? 0.428   -23.546 -19.789 1.00 17.70  ?  290  LLP A C6     1 
HETATM 4480  C "C5'"  . LLP A 1 290 ? 0.379   -21.999 -21.774 1.00 21.35  ?  290  LLP A "C5'"  1 
HETATM 4481  O OP4    . LLP A 1 290 ? 0.976   -20.803 -21.648 1.00 17.45  ?  290  LLP A OP4    1 
HETATM 4482  P P      . LLP A 1 290 ? 0.854   -20.015 -23.152 1.00 21.06  ?  290  LLP A P      1 
HETATM 4483  O OP1    . LLP A 1 290 ? 1.757   -18.860 -22.839 1.00 20.02  ?  290  LLP A OP1    1 
HETATM 4484  O OP2    . LLP A 1 290 ? 1.689   -20.789 -24.291 1.00 15.46  ?  290  LLP A OP2    1 
HETATM 4485  O OP3    . LLP A 1 290 ? -0.351  -19.565 -24.119 1.00 68.70  ?  290  LLP A OP3    1 
HETATM 4486  N N      . LLP A 1 290 ? 2.322   -15.943 -17.591 1.00 13.36  ?  290  LLP A N      1 
HETATM 4487  C CA     . LLP A 1 290 ? 1.160   -15.108 -17.257 1.00 15.20  ?  290  LLP A CA     1 
HETATM 4488  C CB     . LLP A 1 290 ? -0.072  -15.971 -16.965 1.00 17.49  ?  290  LLP A CB     1 
HETATM 4489  C CG     . LLP A 1 290 ? -0.560  -16.816 -18.194 1.00 18.49  ?  290  LLP A CG     1 
HETATM 4490  C CD     . LLP A 1 290 ? -1.892  -17.524 -17.970 1.00 23.58  ?  290  LLP A CD     1 
HETATM 4491  C CE     . LLP A 1 290 ? -2.521  -18.088 -19.282 1.00 33.79  ?  290  LLP A CE     1 
HETATM 4492  N NZ     . LLP A 1 290 ? -2.258  -19.560 -19.605 1.00 48.13  ?  290  LLP A NZ     1 
HETATM 4493  C C      . LLP A 1 290 ? 1.408   -14.047 -16.182 1.00 15.97  ?  290  LLP A C      1 
HETATM 4494  O O      . LLP A 1 290 ? 1.933   -12.966 -16.486 1.00 16.73  ?  290  LLP A O      1 
HETATM 4495  H "H2'1" . LLP A 1 290 ? -0.879  -24.398 -16.307 1.00 25.91  ?  290  LLP A "H2'1" 1 
HETATM 4496  H "H2'2" . LLP A 1 290 ? -2.246  -24.689 -16.936 1.00 25.91  ?  290  LLP A "H2'2" 1 
HETATM 4497  H "H2'3" . LLP A 1 290 ? -1.982  -23.333 -16.269 1.00 25.91  ?  290  LLP A "H2'3" 1 
HETATM 4498  H HO3    . LLP A 1 290 ? -3.624  -22.064 -18.492 1.00 29.79  ?  290  LLP A HO3    1 
HETATM 4499  H "H4'1" . LLP A 1 290 ? -2.097  -20.779 -21.338 1.00 50.03  ?  290  LLP A "H4'1" 1 
HETATM 4500  H H6     . LLP A 1 290 ? 1.186   -23.944 -20.151 1.00 21.24  ?  290  LLP A H6     1 
HETATM 4501  H "H5'1" . LLP A 1 290 ? -0.329  -21.928 -22.386 1.00 25.62  ?  290  LLP A "H5'1" 1 
HETATM 4502  H "H5'2" . LLP A 1 290 ? 0.981   -22.628 -22.126 1.00 25.62  ?  290  LLP A "H5'2" 1 
HETATM 4503  H H      . LLP A 1 290 ? 2.401   -16.079 -18.437 1.00 16.03  ?  290  LLP A H      1 
HETATM 4504  H HA     . LLP A 1 290 ? 0.967   -14.580 -18.048 1.00 18.24  ?  290  LLP A HA     1 
HETATM 4505  H HB2    . LLP A 1 290 ? 0.143   -16.588 -16.249 1.00 20.99  ?  290  LLP A HB2    1 
HETATM 4506  H HB3    . LLP A 1 290 ? -0.802  -15.391 -16.696 1.00 20.99  ?  290  LLP A HB3    1 
HETATM 4507  H HG2    . LLP A 1 290 ? -0.665  -16.225 -18.956 1.00 22.18  ?  290  LLP A HG2    1 
HETATM 4508  H HG3    . LLP A 1 290 ? 0.105   -17.495 -18.389 1.00 22.18  ?  290  LLP A HG3    1 
HETATM 4509  H HD2    . LLP A 1 290 ? -1.754  -18.268 -17.363 1.00 28.29  ?  290  LLP A HD2    1 
HETATM 4510  H HD3    . LLP A 1 290 ? -2.522  -16.894 -17.585 1.00 28.29  ?  290  LLP A HD3    1 
HETATM 4511  H HE2    . LLP A 1 290 ? -3.483  -17.980 -19.223 1.00 40.54  ?  290  LLP A HE2    1 
HETATM 4512  H HE3    . LLP A 1 290 ? -2.174  -17.571 -20.026 1.00 40.54  ?  290  LLP A HE3    1 
HETATM 4513  H HZ3    . LLP A 1 290 ? -2.527  -20.072 -18.929 1.00 57.75  ?  290  LLP A HZ3    1 
ATOM   4514  N N      . GLY A 1 291 ? 1.012   -14.321 -14.939 1.00 15.59  ?  291  GLY A N      1 
ATOM   4515  C CA     . GLY A 1 291 ? 1.159   -13.364 -13.846 1.00 14.95  ?  291  GLY A CA     1 
ATOM   4516  C C      . GLY A 1 291 ? 2.588   -13.008 -13.508 1.00 15.56  ?  291  GLY A C      1 
ATOM   4517  O O      . GLY A 1 291 ? 2.804   -12.085 -12.709 1.00 15.89  ?  291  GLY A O      1 
ATOM   4518  H H      . GLY A 1 291 ? 0.649   -15.063 -14.700 1.00 18.70  ?  291  GLY A H      1 
ATOM   4519  H HA2    . GLY A 1 291 ? 0.699   -12.544 -14.085 1.00 17.93  ?  291  GLY A HA2    1 
ATOM   4520  H HA3    . GLY A 1 291 ? 0.750   -13.735 -13.049 1.00 17.93  ?  291  GLY A HA3    1 
ATOM   4521  N N      . LEU A 1 292 ? 3.573   -13.689 -14.116 1.00 14.33  ?  292  LEU A N      1 
ATOM   4522  C CA     . LEU A 1 292 ? 4.971   -13.293 -13.946 1.00 14.24  ?  292  LEU A CA     1 
ATOM   4523  C C      . LEU A 1 292 ? 5.229   -11.873 -14.439 1.00 14.95  ?  292  LEU A C      1 
ATOM   4524  O O      . LEU A 1 292 ? 6.025   -11.143 -13.838 1.00 15.26  ?  292  LEU A O      1 
ATOM   4525  C CB     . LEU A 1 292 ? 5.860   -14.294 -14.694 1.00 13.43  ?  292  LEU A CB     1 
ATOM   4526  C CG     . LEU A 1 292 ? 7.347   -13.982 -14.785 1.00 15.22  ?  292  LEU A CG     1 
ATOM   4527  C CD1    . LEU A 1 292 ? 7.986   -13.844 -13.395 1.00 15.11  ?  292  LEU A CD1    1 
ATOM   4528  C CD2    . LEU A 1 292 ? 8.038   -15.060 -15.602 1.00 16.49  ?  292  LEU A CD2    1 
ATOM   4529  H H      . LEU A 1 292 ? 3.458   -14.373 -14.625 1.00 17.19  ?  292  LEU A H      1 
ATOM   4530  H HA     . LEU A 1 292 ? 5.195   -13.310 -13.002 1.00 17.09  ?  292  LEU A HA     1 
ATOM   4531  H HB2    . LEU A 1 292 ? 5.780   -15.153 -14.249 1.00 16.11  ?  292  LEU A HB2    1 
ATOM   4532  H HB3    . LEU A 1 292 ? 5.530   -14.360 -15.604 1.00 16.11  ?  292  LEU A HB3    1 
ATOM   4533  H HG     . LEU A 1 292 ? 7.467   -13.127 -15.227 1.00 18.26  ?  292  LEU A HG     1 
ATOM   4534  H HD11   . LEU A 1 292 ? 8.936   -13.679 -13.499 1.00 18.13  ?  292  LEU A HD11   1 
ATOM   4535  H HD12   . LEU A 1 292 ? 7.570   -13.103 -12.928 1.00 18.13  ?  292  LEU A HD12   1 
ATOM   4536  H HD13   . LEU A 1 292 ? 7.846   -14.667 -12.901 1.00 18.13  ?  292  LEU A HD13   1 
ATOM   4537  H HD21   . LEU A 1 292 ? 8.991   -14.880 -15.620 1.00 19.79  ?  292  LEU A HD21   1 
ATOM   4538  H HD22   . LEU A 1 292 ? 7.872   -15.923 -15.191 1.00 19.79  ?  292  LEU A HD22   1 
ATOM   4539  H HD23   . LEU A 1 292 ? 7.683   -15.050 -16.504 1.00 19.79  ?  292  LEU A HD23   1 
ATOM   4540  N N      . THR A 1 293 ? 4.597   -11.469 -15.551 1.00 14.38  ?  293  THR A N      1 
ATOM   4541  C CA     . THR A 1 293 ? 4.732   -10.114 -16.068 1.00 12.63  ?  293  THR A CA     1 
ATOM   4542  C C      . THR A 1 293 ? 3.395   -9.399  -16.203 1.00 12.67  ?  293  THR A C      1 
ATOM   4543  O O      . THR A 1 293 ? 3.359   -8.296  -16.758 1.00 13.78  ?  293  THR A O      1 
ATOM   4544  C CB     . THR A 1 293 ? 5.351   -10.112 -17.463 1.00 12.89  ?  293  THR A CB     1 
ATOM   4545  O OG1    . THR A 1 293 ? 4.519   -10.911 -18.322 1.00 14.97  ?  293  THR A OG1    1 
ATOM   4546  C CG2    . THR A 1 293 ? 6.758   -10.630 -17.456 1.00 13.23  ?  293  THR A CG2    1 
ATOM   4547  H H      . THR A 1 293 ? 4.082   -11.972 -16.022 1.00 17.25  ?  293  THR A H      1 
ATOM   4548  H HA     . THR A 1 293 ? 5.315   -9.637  -15.457 1.00 15.16  ?  293  THR A HA     1 
ATOM   4549  H HB     . THR A 1 293 ? 5.403   -9.204  -17.800 1.00 15.46  ?  293  THR A HB     1 
ATOM   4550  H HG1    . THR A 1 293 ? 4.731   -10.784 -19.125 1.00 17.96  ?  293  THR A HG1    1 
ATOM   4551  H HG21   . THR A 1 293 ? 7.110   -10.645 -18.359 1.00 15.87  ?  293  THR A HG21   1 
ATOM   4552  H HG22   . THR A 1 293 ? 7.319   -10.058 -16.909 1.00 15.87  ?  293  THR A HG22   1 
ATOM   4553  H HG23   . THR A 1 293 ? 6.779   -11.530 -17.094 1.00 15.87  ?  293  THR A HG23   1 
ATOM   4554  N N      . SER A 1 294 ? 2.290   -10.030 -15.800 1.00 13.76  ?  294  SER A N      1 
ATOM   4555  C CA     . SER A 1 294 ? 0.945   -9.505  -16.058 1.00 13.60  ?  294  SER A CA     1 
ATOM   4556  C C      . SER A 1 294 ? 0.724   -9.226  -17.536 1.00 13.41  ?  294  SER A C      1 
ATOM   4557  O O      . SER A 1 294 ? -0.051  -8.345  -17.901 1.00 14.75  ?  294  SER A O      1 
ATOM   4558  C CB     . SER A 1 294 ? 0.610   -8.294  -15.187 1.00 13.42  ?  294  SER A CB     1 
ATOM   4559  O OG     . SER A 1 294 ? 0.335   -8.715  -13.856 1.00 14.32  ?  294  SER A OG     1 
ATOM   4560  H H      . SER A 1 294 ? 2.292   -10.774 -15.369 1.00 16.51  ?  294  SER A H      1 
ATOM   4561  H HA     . SER A 1 294 ? 0.310   -10.195 -15.807 1.00 16.31  ?  294  SER A HA     1 
ATOM   4562  H HB2    . SER A 1 294 ? 1.366   -7.686  -15.181 1.00 16.10  ?  294  SER A HB2    1 
ATOM   4563  H HB3    . SER A 1 294 ? -0.172  -7.847  -15.549 1.00 16.10  ?  294  SER A HB3    1 
ATOM   4564  H HG     . SER A 1 294 ? 1.004   -9.109  -13.535 1.00 17.18  ?  294  SER A HG     1 
ATOM   4565  N N      . ALA A 1 295 ? 1.403   -9.998  -18.379 1.00 13.41  ?  295  ALA A N      1 
ATOM   4566  C CA     . ALA A 1 295 ? 1.298   -9.939  -19.836 1.00 13.93  ?  295  ALA A CA     1 
ATOM   4567  C C      . ALA A 1 295 ? 1.894   -8.679  -20.449 1.00 12.92  ?  295  ALA A C      1 
ATOM   4568  O O      . ALA A 1 295 ? 1.781   -8.487  -21.679 1.00 13.75  ?  295  ALA A O      1 
ATOM   4569  C CB     . ALA A 1 295 ? -0.140  -10.143 -20.333 1.00 14.22  ?  295  ALA A CB     1 
ATOM   4570  H H      . ALA A 1 295 ? 1.960   -10.596 -18.111 1.00 16.09  ?  295  ALA A H      1 
ATOM   4571  H HA     . ALA A 1 295 ? 1.826   -10.677 -20.179 1.00 16.72  ?  295  ALA A HA     1 
ATOM   4572  H HB1    . ALA A 1 295 ? -0.143  -10.131 -21.303 1.00 17.06  ?  295  ALA A HB1    1 
ATOM   4573  H HB2    . ALA A 1 295 ? -0.467  -10.998 -20.012 1.00 17.06  ?  295  ALA A HB2    1 
ATOM   4574  H HB3    . ALA A 1 295 ? -0.697  -9.426  -19.992 1.00 17.06  ?  295  ALA A HB3    1 
ATOM   4575  N N      . TYR A 1 296 ? 2.567   -7.827  -19.665 1.00 13.50  ?  296  TYR A N      1 
ATOM   4576  C CA     . TYR A 1 296 ? 3.137   -6.609  -20.248 1.00 14.00  ?  296  TYR A CA     1 
ATOM   4577  C C      . TYR A 1 296 ? 4.258   -6.941  -21.220 1.00 15.39  ?  296  TYR A C      1 
ATOM   4578  O O      . TYR A 1 296 ? 4.499   -6.174  -22.153 1.00 14.12  ?  296  TYR A O      1 
ATOM   4579  C CB     . TYR A 1 296 ? 3.556   -5.613  -19.157 1.00 13.12  ?  296  TYR A CB     1 
ATOM   4580  C CG     . TYR A 1 296 ? 2.380   -4.854  -18.598 1.00 13.03  ?  296  TYR A CG     1 
ATOM   4581  C CD1    . TYR A 1 296 ? 1.939   -3.696  -19.203 1.00 14.84  ?  296  TYR A CD1    1 
ATOM   4582  C CD2    . TYR A 1 296 ? 1.653   -5.328  -17.531 1.00 13.60  ?  296  TYR A CD2    1 
ATOM   4583  C CE1    . TYR A 1 296 ? 0.868   -3.014  -18.736 1.00 15.21  ?  296  TYR A CE1    1 
ATOM   4584  C CE2    . TYR A 1 296 ? 0.541   -4.638  -17.064 1.00 13.53  ?  296  TYR A CE2    1 
ATOM   4585  C CZ     . TYR A 1 296 ? 0.150   -3.496  -17.682 1.00 13.60  ?  296  TYR A CZ     1 
ATOM   4586  O OH     . TYR A 1 296 ? -0.953  -2.785  -17.270 1.00 14.94  ?  296  TYR A OH     1 
ATOM   4587  H H      . TYR A 1 296 ? 2.704   -7.927  -18.822 1.00 16.20  ?  296  TYR A H      1 
ATOM   4588  H HA     . TYR A 1 296 ? 2.454   -6.144  -20.757 1.00 16.80  ?  296  TYR A HA     1 
ATOM   4589  H HB2    . TYR A 1 296 ? 3.977   -6.097  -18.430 1.00 15.74  ?  296  TYR A HB2    1 
ATOM   4590  H HB3    . TYR A 1 296 ? 4.179   -4.972  -19.534 1.00 15.74  ?  296  TYR A HB3    1 
ATOM   4591  H HD1    . TYR A 1 296 ? 2.389   -3.376  -19.951 1.00 17.80  ?  296  TYR A HD1    1 
ATOM   4592  H HD2    . TYR A 1 296 ? 1.909   -6.120  -17.117 1.00 16.32  ?  296  TYR A HD2    1 
ATOM   4593  H HE1    . TYR A 1 296 ? 0.620   -2.212  -19.136 1.00 18.25  ?  296  TYR A HE1    1 
ATOM   4594  H HE2    . TYR A 1 296 ? 0.066   -4.958  -16.330 1.00 16.24  ?  296  TYR A HE2    1 
ATOM   4595  H HH     . TYR A 1 296 ? -1.348  -3.199  -16.655 1.00 17.93  ?  296  TYR A HH     1 
ATOM   4596  N N      . GLN A 1 297 ? 4.952   -8.057  -21.005 1.00 14.63  ?  297  GLN A N      1 
ATOM   4597  C CA     . GLN A 1 297 ? 5.900   -8.621  -21.953 1.00 13.46  ?  297  GLN A CA     1 
ATOM   4598  C C      . GLN A 1 297 ? 5.724   -10.132 -21.944 1.00 13.31  ?  297  GLN A C      1 
ATOM   4599  O O      . GLN A 1 297 ? 5.398   -10.705 -20.906 1.00 12.80  ?  297  GLN A O      1 
ATOM   4600  C CB     . GLN A 1 297 ? 7.347   -8.312  -21.535 1.00 14.29  ?  297  GLN A CB     1 
ATOM   4601  C CG     . GLN A 1 297 ? 7.757   -6.837  -21.643 1.00 12.73  ?  297  GLN A CG     1 
ATOM   4602  C CD     . GLN A 1 297 ? 8.012   -6.442  -23.059 1.00 13.64  ?  297  GLN A CD     1 
ATOM   4603  O OE1    . GLN A 1 297 ? 9.130   -6.583  -23.556 1.00 15.28  ?  297  GLN A OE1    1 
ATOM   4604  N NE2    . GLN A 1 297 ? 6.980   -5.952  -23.736 1.00 13.60  ?  297  GLN A NE2    1 
ATOM   4605  H H      . GLN A 1 297 ? 4.883   -8.522  -20.285 1.00 17.55  ?  297  GLN A H      1 
ATOM   4606  H HA     . GLN A 1 297 ? 5.740   -8.269  -22.842 1.00 16.15  ?  297  GLN A HA     1 
ATOM   4607  H HB2    . GLN A 1 297 ? 7.462   -8.578  -20.610 1.00 17.15  ?  297  GLN A HB2    1 
ATOM   4608  H HB3    . GLN A 1 297 ? 7.945   -8.821  -22.104 1.00 17.15  ?  297  GLN A HB3    1 
ATOM   4609  H HG2    . GLN A 1 297 ? 7.044   -6.279  -21.295 1.00 15.28  ?  297  GLN A HG2    1 
ATOM   4610  H HG3    . GLN A 1 297 ? 8.571   -6.692  -21.135 1.00 15.28  ?  297  GLN A HG3    1 
ATOM   4611  H HE21   . GLN A 1 297 ? 6.213   -5.876  -23.355 1.00 16.32  ?  297  GLN A HE21   1 
ATOM   4612  H HE22   . GLN A 1 297 ? 7.079   -5.711  -24.556 1.00 16.32  ?  297  GLN A HE22   1 
ATOM   4613  N N      . PRO A 1 298 ? 5.986   -10.808 -23.059 1.00 13.52  ?  298  PRO A N      1 
ATOM   4614  C CA     . PRO A 1 298 ? 5.958   -12.279 -23.047 1.00 13.96  ?  298  PRO A CA     1 
ATOM   4615  C C      . PRO A 1 298 ? 7.182   -12.815 -22.317 1.00 17.76  ?  298  PRO A C      1 
ATOM   4616  O O      . PRO A 1 298 ? 8.311   -12.554 -22.712 1.00 25.44  ?  298  PRO A O      1 
ATOM   4617  C CB     . PRO A 1 298 ? 5.985   -12.656 -24.536 1.00 16.10  ?  298  PRO A CB     1 
ATOM   4618  C CG     . PRO A 1 298 ? 5.985   -11.398 -25.295 1.00 18.77  ?  298  PRO A CG     1 
ATOM   4619  C CD     . PRO A 1 298 ? 6.268   -10.263 -24.405 1.00 16.05  ?  298  PRO A CD     1 
ATOM   4620  H HA     . PRO A 1 298 ? 5.143   -12.612 -22.639 1.00 16.75  ?  298  PRO A HA     1 
ATOM   4621  H HB2    . PRO A 1 298 ? 6.788   -13.167 -24.725 1.00 19.32  ?  298  PRO A HB2    1 
ATOM   4622  H HB3    . PRO A 1 298 ? 5.199   -13.182 -24.750 1.00 19.32  ?  298  PRO A HB3    1 
ATOM   4623  H HG2    . PRO A 1 298 ? 6.668   -11.453 -25.982 1.00 22.52  ?  298  PRO A HG2    1 
ATOM   4624  H HG3    . PRO A 1 298 ? 5.113   -11.284 -25.703 1.00 22.52  ?  298  PRO A HG3    1 
ATOM   4625  H HD2    . PRO A 1 298 ? 7.196   -9.989  -24.479 1.00 19.25  ?  298  PRO A HD2    1 
ATOM   4626  H HD3    . PRO A 1 298 ? 5.684   -9.515  -24.604 1.00 19.25  ?  298  PRO A HD3    1 
ATOM   4627  N N      . LEU A 1 299 ? 6.957   -13.573 -21.259 1.00 13.12  ?  299  LEU A N      1 
ATOM   4628  C CA     . LEU A 1 299 ? 8.037   -14.164 -20.488 1.00 12.52  ?  299  LEU A CA     1 
ATOM   4629  C C      . LEU A 1 299 ? 7.508   -15.430 -19.821 1.00 12.35  ?  299  LEU A C      1 
ATOM   4630  O O      . LEU A 1 299 ? 6.393   -15.450 -19.292 1.00 15.33  ?  299  LEU A O      1 
ATOM   4631  C CB     . LEU A 1 299 ? 8.563   -13.191 -19.414 1.00 12.29  ?  299  LEU A CB     1 
ATOM   4632  C CG     . LEU A 1 299 ? 9.948   -13.506 -18.821 1.00 12.93  ?  299  LEU A CG     1 
ATOM   4633  C CD1    . LEU A 1 299 ? 11.015  -13.244 -19.874 1.00 15.60  ?  299  LEU A CD1    1 
ATOM   4634  C CD2    . LEU A 1 299 ? 10.223  -12.699 -17.577 1.00 14.56  ?  299  LEU A CD2    1 
ATOM   4635  H H      . LEU A 1 299 ? 6.173   -13.765 -20.961 1.00 15.74  ?  299  LEU A H      1 
ATOM   4636  H HA     . LEU A 1 299 ? 8.774   -14.395 -21.075 1.00 15.01  ?  299  LEU A HA     1 
ATOM   4637  H HB2    . LEU A 1 299 ? 8.617   -12.307 -19.810 1.00 14.75  ?  299  LEU A HB2    1 
ATOM   4638  H HB3    . LEU A 1 299 ? 7.932   -13.186 -18.677 1.00 14.75  ?  299  LEU A HB3    1 
ATOM   4639  H HG     . LEU A 1 299 ? 9.974   -14.439 -18.559 1.00 15.51  ?  299  LEU A HG     1 
ATOM   4640  H HD11   . LEU A 1 299 ? 11.890  -13.371 -19.475 1.00 18.71  ?  299  LEU A HD11   1 
ATOM   4641  H HD12   . LEU A 1 299 ? 10.893  -13.865 -20.609 1.00 18.71  ?  299  LEU A HD12   1 
ATOM   4642  H HD13   . LEU A 1 299 ? 10.927  -12.332 -20.193 1.00 18.71  ?  299  LEU A HD13   1 
ATOM   4643  H HD21   . LEU A 1 299 ? 11.080  -12.965 -17.210 1.00 17.47  ?  299  LEU A HD21   1 
ATOM   4644  H HD22   . LEU A 1 299 ? 10.240  -11.757 -17.809 1.00 17.47  ?  299  LEU A HD22   1 
ATOM   4645  H HD23   . LEU A 1 299 ? 9.520   -12.867 -16.930 1.00 17.47  ?  299  LEU A HD23   1 
ATOM   4646  N N      . SER A 1 300 ? 8.326   -16.473 -19.813 1.00 12.59  ?  300  SER A N      1 
ATOM   4647  C CA     . SER A 1 300 ? 8.019   -17.703 -19.090 1.00 11.25  ?  300  SER A CA     1 
ATOM   4648  C C      . SER A 1 300 ? 9.250   -18.131 -18.317 1.00 11.34  ?  300  SER A C      1 
ATOM   4649  O O      . SER A 1 300 ? 10.369  -17.668 -18.569 1.00 12.52  ?  300  SER A O      1 
ATOM   4650  C CB     . SER A 1 300 ? 7.611   -18.835 -20.038 1.00 10.37  ?  300  SER A CB     1 
ATOM   4651  O OG     . SER A 1 300 ? 8.750   -19.337 -20.689 1.00 11.91  ?  300  SER A OG     1 
ATOM   4652  H H      . SER A 1 300 ? 9.079   -16.493 -20.227 1.00 15.11  ?  300  SER A H      1 
ATOM   4653  H HA     . SER A 1 300 ? 7.288   -17.533 -18.476 1.00 13.49  ?  300  SER A HA     1 
ATOM   4654  H HB2    . SER A 1 300 ? 7.194   -19.546 -19.527 1.00 12.44  ?  300  SER A HB2    1 
ATOM   4655  H HB3    . SER A 1 300 ? 6.989   -18.491 -20.698 1.00 12.44  ?  300  SER A HB3    1 
ATOM   4656  H HG     . SER A 1 300 ? 8.529   -19.934 -21.236 1.00 14.29  ?  300  SER A HG     1 
ATOM   4657  N N      . GLY A 1 301 ? 9.036   -19.043 -17.391 1.00 11.67  ?  301  GLY A N      1 
ATOM   4658  C CA     . GLY A 1 301 ? 10.127  -19.589 -16.610 1.00 11.90  ?  301  GLY A CA     1 
ATOM   4659  C C      . GLY A 1 301 ? 9.914   -21.051 -16.298 1.00 11.63  ?  301  GLY A C      1 
ATOM   4660  O O      . GLY A 1 301 ? 8.777   -21.534 -16.219 1.00 12.90  ?  301  GLY A O      1 
ATOM   4661  H H      . GLY A 1 301 ? 8.264   -19.365 -17.193 1.00 14.01  ?  301  GLY A H      1 
ATOM   4662  H HA2    . GLY A 1 301 ? 10.957  -19.496 -17.103 1.00 14.28  ?  301  GLY A HA2    1 
ATOM   4663  H HA3    . GLY A 1 301 ? 10.201  -19.103 -15.773 1.00 14.28  ?  301  GLY A HA3    1 
ATOM   4664  N N      . VAL A 1 302 ? 11.021  -21.770 -16.172 1.00 11.08  ?  302  VAL A N      1 
ATOM   4665  C CA     . VAL A 1 302 ? 11.096  -23.060 -15.502 1.00 9.68   ?  302  VAL A CA     1 
ATOM   4666  C C      . VAL A 1 302 ? 11.899  -22.819 -14.234 1.00 10.77  ?  302  VAL A C      1 
ATOM   4667  O O      . VAL A 1 302 ? 13.005  -22.279 -14.288 1.00 12.64  ?  302  VAL A O      1 
ATOM   4668  C CB     . VAL A 1 302 ? 11.740  -24.133 -16.384 1.00 10.93  ?  302  VAL A CB     1 
ATOM   4669  C CG1    . VAL A 1 302 ? 11.985  -25.396 -15.557 1.00 12.62  ?  302  VAL A CG1    1 
ATOM   4670  C CG2    . VAL A 1 302 ? 10.828  -24.437 -17.576 1.00 12.30  ?  302  VAL A CG2    1 
ATOM   4671  H H      . VAL A 1 302 ? 11.782  -21.516 -16.483 1.00 13.29  ?  302  VAL A H      1 
ATOM   4672  H HA     . VAL A 1 302 ? 10.209  -23.380 -15.274 1.00 11.61  ?  302  VAL A HA     1 
ATOM   4673  H HB     . VAL A 1 302 ? 12.592  -23.817 -16.723 1.00 13.11  ?  302  VAL A HB     1 
ATOM   4674  H HG11   . VAL A 1 302 ? 12.189  -26.131 -16.156 1.00 15.14  ?  302  VAL A HG11   1 
ATOM   4675  H HG12   . VAL A 1 302 ? 12.731  -25.241 -14.957 1.00 15.14  ?  302  VAL A HG12   1 
ATOM   4676  H HG13   . VAL A 1 302 ? 11.186  -25.598 -15.045 1.00 15.14  ?  302  VAL A HG13   1 
ATOM   4677  H HG21   . VAL A 1 302 ? 11.241  -25.125 -18.121 1.00 14.76  ?  302  VAL A HG21   1 
ATOM   4678  H HG22   . VAL A 1 302 ? 9.970   -24.746 -17.247 1.00 14.76  ?  302  VAL A HG22   1 
ATOM   4679  H HG23   . VAL A 1 302 ? 10.711  -23.628 -18.098 1.00 14.76  ?  302  VAL A HG23   1 
ATOM   4680  N N      . ILE A 1 303 ? 11.330  -23.178 -13.088 1.00 12.01  ?  303  ILE A N      1 
ATOM   4681  C CA     . ILE A 1 303 ? 12.060  -23.137 -11.832 1.00 11.27  ?  303  ILE A CA     1 
ATOM   4682  C C      . ILE A 1 303 ? 12.492  -24.569 -11.535 1.00 12.01  ?  303  ILE A C      1 
ATOM   4683  O O      . ILE A 1 303 ? 11.652  -25.474 -11.450 1.00 12.03  ?  303  ILE A O      1 
ATOM   4684  C CB     . ILE A 1 303 ? 11.208  -22.562 -10.692 1.00 12.42  ?  303  ILE A CB     1 
ATOM   4685  C CG1    . ILE A 1 303 ? 10.376  -21.375 -11.152 1.00 12.48  ?  303  ILE A CG1    1 
ATOM   4686  C CG2    . ILE A 1 303 ? 12.116  -22.105 -9.542  1.00 13.92  ?  303  ILE A CG2    1 
ATOM   4687  C CD1    . ILE A 1 303 ? 9.479   -20.815 -10.049 1.00 12.70  ?  303  ILE A CD1    1 
ATOM   4688  H H      . ILE A 1 303 ? 10.517  -23.449 -13.017 1.00 14.41  ?  303  ILE A H      1 
ATOM   4689  H HA     . ILE A 1 303 ? 12.845  -22.574 -11.920 1.00 13.52  ?  303  ILE A HA     1 
ATOM   4690  H HB     . ILE A 1 303 ? 10.610  -23.267 -10.399 1.00 14.90  ?  303  ILE A HB     1 
ATOM   4691  H HG12   . ILE A 1 303 ? 10.971  -20.667 -11.444 1.00 14.98  ?  303  ILE A HG12   1 
ATOM   4692  H HG13   . ILE A 1 303 ? 9.807   -21.654 -11.887 1.00 14.98  ?  303  ILE A HG13   1 
ATOM   4693  H HG21   . ILE A 1 303 ? 11.564  -21.860 -8.783  1.00 16.70  ?  303  ILE A HG21   1 
ATOM   4694  H HG22   . ILE A 1 303 ? 12.708  -22.834 -9.299  1.00 16.70  ?  303  ILE A HG22   1 
ATOM   4695  H HG23   . ILE A 1 303 ? 12.635  -21.340 -9.834  1.00 16.70  ?  303  ILE A HG23   1 
ATOM   4696  H HD11   . ILE A 1 303 ? 8.873   -20.164 -10.436 1.00 15.23  ?  303  ILE A HD11   1 
ATOM   4697  H HD12   . ILE A 1 303 ? 8.975   -21.542 -9.652  1.00 15.23  ?  303  ILE A HD12   1 
ATOM   4698  H HD13   . ILE A 1 303 ? 10.035  -20.390 -9.376  1.00 15.23  ?  303  ILE A HD13   1 
ATOM   4699  N N      . ILE A 1 304 ? 13.802  -24.764 -11.392 1.00 12.20  ?  304  ILE A N      1 
ATOM   4700  C CA     . ILE A 1 304 ? 14.405  -26.088 -11.232 1.00 11.32  ?  304  ILE A CA     1 
ATOM   4701  C C      . ILE A 1 304 ? 14.729  -26.269 -9.758  1.00 12.75  ?  304  ILE A C      1 
ATOM   4702  O O      . ILE A 1 304 ? 15.470  -25.471 -9.176  1.00 13.13  ?  304  ILE A O      1 
ATOM   4703  C CB     . ILE A 1 304 ? 15.676  -26.249 -12.083 1.00 12.44  ?  304  ILE A CB     1 
ATOM   4704  C CG1    . ILE A 1 304 ? 15.399  -26.028 -13.570 1.00 14.70  ?  304  ILE A CG1    1 
ATOM   4705  C CG2    . ILE A 1 304 ? 16.247  -27.627 -11.869 1.00 14.54  ?  304  ILE A CG2    1 
ATOM   4706  C CD1    . ILE A 1 304 ? 15.484  -24.576 -14.020 1.00 15.96  ?  304  ILE A CD1    1 
ATOM   4707  H H      . ILE A 1 304 ? 14.378  -24.126 -11.385 1.00 14.64  ?  304  ILE A H      1 
ATOM   4708  H HA     . ILE A 1 304 ? 13.766  -26.762 -11.510 1.00 13.58  ?  304  ILE A HA     1 
ATOM   4709  H HB     . ILE A 1 304 ? 16.311  -25.573 -11.800 1.00 14.93  ?  304  ILE A HB     1 
ATOM   4710  H HG12   . ILE A 1 304 ? 16.050  -26.532 -14.083 1.00 17.63  ?  304  ILE A HG12   1 
ATOM   4711  H HG13   . ILE A 1 304 ? 14.504  -26.344 -13.768 1.00 17.63  ?  304  ILE A HG13   1 
ATOM   4712  H HG21   . ILE A 1 304 ? 16.976  -27.767 -12.493 1.00 17.44  ?  304  ILE A HG21   1 
ATOM   4713  H HG22   . ILE A 1 304 ? 16.573  -27.695 -10.958 1.00 17.44  ?  304  ILE A HG22   1 
ATOM   4714  H HG23   . ILE A 1 304 ? 15.551  -28.285 -12.021 1.00 17.44  ?  304  ILE A HG23   1 
ATOM   4715  H HD11   . ILE A 1 304 ? 15.497  -24.546 -14.989 1.00 19.14  ?  304  ILE A HD11   1 
ATOM   4716  H HD12   . ILE A 1 304 ? 14.710  -24.096 -13.685 1.00 19.14  ?  304  ILE A HD12   1 
ATOM   4717  H HD13   . ILE A 1 304 ? 16.296  -24.182 -13.665 1.00 19.14  ?  304  ILE A HD13   1 
ATOM   4718  N N      . GLY A 1 305 ? 14.189  -27.333 -9.164  1.00 12.87  ?  305  GLY A N      1 
ATOM   4719  C CA     . GLY A 1 305 ? 14.478  -27.639 -7.778  1.00 13.29  ?  305  GLY A CA     1 
ATOM   4720  C C      . GLY A 1 305 ? 15.890  -28.164 -7.555  1.00 13.23  ?  305  GLY A C      1 
ATOM   4721  O O      . GLY A 1 305 ? 16.619  -28.516 -8.487  1.00 13.84  ?  305  GLY A O      1 
ATOM   4722  H H      . GLY A 1 305 ? 13.655  -27.889 -9.545  1.00 15.44  ?  305  GLY A H      1 
ATOM   4723  H HA2    . GLY A 1 305 ? 14.369  -26.834 -7.246  1.00 15.95  ?  305  GLY A HA2    1 
ATOM   4724  H HA3    . GLY A 1 305 ? 13.854  -28.312 -7.464  1.00 15.95  ?  305  GLY A HA3    1 
ATOM   4725  N N      . ASP A 1 306 ? 16.248  -28.259 -6.269  1.00 15.52  ?  306  ASP A N      1 
ATOM   4726  C CA     . ASP A 1 306 ? 17.602  -28.663 -5.898  1.00 15.71  ?  306  ASP A CA     1 
ATOM   4727  C C      . ASP A 1 306 ? 17.950  -30.043 -6.449  1.00 15.74  ?  306  ASP A C      1 
ATOM   4728  O O      . ASP A 1 306 ? 19.066  -30.254 -6.959  1.00 16.42  ?  306  ASP A O      1 
ATOM   4729  C CB     . ASP A 1 306 ? 17.747  -28.662 -4.381  1.00 16.20  ?  306  ASP A CB     1 
ATOM   4730  C CG     . ASP A 1 306 ? 17.843  -27.267 -3.798  1.00 18.78  ?  306  ASP A CG     1 
ATOM   4731  O OD1    . ASP A 1 306 ? 18.279  -26.334 -4.510  1.00 21.43  ?  306  ASP A OD1    1 
ATOM   4732  O OD2    . ASP A 1 306 ? 17.510  -27.111 -2.605  1.00 22.36  -1 306  ASP A OD2    1 
ATOM   4733  H H      . ASP A 1 306 ? 15.732  -28.097 -5.601  1.00 18.62  ?  306  ASP A H      1 
ATOM   4734  H HA     . ASP A 1 306 ? 18.225  -28.021 -6.274  1.00 18.85  ?  306  ASP A HA     1 
ATOM   4735  H HB2    . ASP A 1 306 ? 16.973  -29.096 -3.989  1.00 19.43  ?  306  ASP A HB2    1 
ATOM   4736  H HB3    . ASP A 1 306 ? 18.554  -29.143 -4.140  1.00 19.43  ?  306  ASP A HB3    1 
ATOM   4737  N N      . ARG A 1 307 ? 17.033  -31.008 -6.316  1.00 16.06  ?  307  ARG A N      1 
ATOM   4738  C CA     . ARG A 1 307 ? 17.334  -32.388 -6.711  1.00 16.33  ?  307  ARG A CA     1 
ATOM   4739  C C      . ARG A 1 307 ? 17.628  -32.491 -8.206  1.00 15.50  ?  307  ARG A C      1 
ATOM   4740  O O      . ARG A 1 307 ? 18.614  -33.109 -8.625  1.00 15.92  ?  307  ARG A O      1 
ATOM   4741  C CB     . ARG A 1 307 ? 16.148  -33.286 -6.343  1.00 20.75  ?  307  ARG A CB     1 
ATOM   4742  C CG     . ARG A 1 307 ? 16.339  -34.747 -6.703  1.00 29.86  ?  307  ARG A CG     1 
ATOM   4743  C CD     . ARG A 1 307 ? 15.054  -35.549 -6.479  1.00 38.66  ?  307  ARG A CD     1 
ATOM   4744  N NE     . ARG A 1 307 ? 14.464  -35.303 -5.169  1.00 47.41  ?  307  ARG A NE     1 
ATOM   4745  C CZ     . ARG A 1 307 ? 14.722  -36.022 -4.080  1.00 53.05  ?  307  ARG A CZ     1 
ATOM   4746  N NH1    . ARG A 1 307 ? 15.573  -37.037 -4.136  1.00 55.15  ?  307  ARG A NH1    1 
ATOM   4747  N NH2    . ARG A 1 307 ? 14.132  -35.721 -2.932  1.00 54.95  ?  307  ARG A NH2    1 
ATOM   4748  H H      . ARG A 1 307 ? 16.240  -30.893 -6.005  1.00 19.27  ?  307  ARG A H      1 
ATOM   4749  H HA     . ARG A 1 307 ? 18.123  -32.687 -6.231  1.00 19.60  ?  307  ARG A HA     1 
ATOM   4750  H HB2    . ARG A 1 307 ? 16.006  -33.235 -5.385  1.00 24.90  ?  307  ARG A HB2    1 
ATOM   4751  H HB3    . ARG A 1 307 ? 15.361  -32.968 -6.812  1.00 24.90  ?  307  ARG A HB3    1 
ATOM   4752  H HG2    . ARG A 1 307 ? 16.584  -34.819 -7.639  1.00 35.83  ?  307  ARG A HG2    1 
ATOM   4753  H HG3    . ARG A 1 307 ? 17.037  -35.127 -6.147  1.00 35.83  ?  307  ARG A HG3    1 
ATOM   4754  H HD2    . ARG A 1 307 ? 14.403  -35.300 -7.153  1.00 46.39  ?  307  ARG A HD2    1 
ATOM   4755  H HD3    . ARG A 1 307 ? 15.255  -36.496 -6.545  1.00 46.39  ?  307  ARG A HD3    1 
ATOM   4756  H HE     . ARG A 1 307 ? 13.912  -34.648 -5.095  1.00 56.89  ?  307  ARG A HE     1 
ATOM   4757  H HH11   . ARG A 1 307 ? 15.960  -37.232 -4.879  1.00 66.18  ?  307  ARG A HH11   1 
ATOM   4758  H HH12   . ARG A 1 307 ? 15.737  -37.500 -3.430  1.00 66.18  ?  307  ARG A HH12   1 
ATOM   4759  H HH21   . ARG A 1 307 ? 13.583  -35.060 -2.890  1.00 65.94  ?  307  ARG A HH21   1 
ATOM   4760  H HH22   . ARG A 1 307 ? 14.299  -36.186 -2.228  1.00 65.94  ?  307  ARG A HH22   1 
ATOM   4761  N N      . VAL A 1 308 ? 16.766  -31.910 -9.033  1.00 13.68  ?  308  VAL A N      1 
ATOM   4762  C CA     . VAL A 1 308 ? 17.001  -31.966 -10.473 1.00 13.20  ?  308  VAL A CA     1 
ATOM   4763  C C      . VAL A 1 308 ? 18.247  -31.178 -10.846 1.00 14.48  ?  308  VAL A C      1 
ATOM   4764  O O      . VAL A 1 308 ? 19.023  -31.590 -11.730 1.00 14.81  ?  308  VAL A O      1 
ATOM   4765  C CB     . VAL A 1 308 ? 15.740  -31.495 -11.219 1.00 13.63  ?  308  VAL A CB     1 
ATOM   4766  C CG1    . VAL A 1 308 ? 16.027  -31.342 -12.705 1.00 14.81  ?  308  VAL A CG1    1 
ATOM   4767  C CG2    . VAL A 1 308 ? 14.594  -32.484 -10.976 1.00 14.83  ?  308  VAL A CG2    1 
ATOM   4768  H H      . VAL A 1 308 ? 16.055  -31.487 -8.797  1.00 16.42  ?  308  VAL A H      1 
ATOM   4769  H HA     . VAL A 1 308 ? 17.171  -32.883 -10.738 1.00 15.84  ?  308  VAL A HA     1 
ATOM   4770  H HB     . VAL A 1 308 ? 15.468  -30.627 -10.882 1.00 16.35  ?  308  VAL A HB     1 
ATOM   4771  H HG11   . VAL A 1 308 ? 15.191  -31.204 -13.176 1.00 17.77  ?  308  VAL A HG11   1 
ATOM   4772  H HG12   . VAL A 1 308 ? 16.611  -30.578 -12.837 1.00 17.77  ?  308  VAL A HG12   1 
ATOM   4773  H HG13   . VAL A 1 308 ? 16.460  -32.148 -13.028 1.00 17.77  ?  308  VAL A HG13   1 
ATOM   4774  H HG21   . VAL A 1 308 ? 13.820  -32.204 -11.490 1.00 17.79  ?  308  VAL A HG21   1 
ATOM   4775  H HG22   . VAL A 1 308 ? 14.875  -33.369 -11.257 1.00 17.79  ?  308  VAL A HG22   1 
ATOM   4776  H HG23   . VAL A 1 308 ? 14.378  -32.491 -10.030 1.00 17.79  ?  308  VAL A HG23   1 
ATOM   4777  N N      . TRP A 1 309 ? 18.447  -30.013 -10.210 1.00 14.43  ?  309  TRP A N      1 
ATOM   4778  C CA     . TRP A 1 309 ? 19.603  -29.186 -10.553 1.00 13.73  ?  309  TRP A CA     1 
ATOM   4779  C C      . TRP A 1 309 ? 20.905  -29.957 -10.353 1.00 14.18  ?  309  TRP A C      1 
ATOM   4780  O O      . TRP A 1 309 ? 21.830  -29.853 -11.166 1.00 13.99  ?  309  TRP A O      1 
ATOM   4781  C CB     . TRP A 1 309 ? 19.621  -27.900 -9.727  1.00 13.90  ?  309  TRP A CB     1 
ATOM   4782  C CG     . TRP A 1 309 ? 20.770  -27.065 -10.150 1.00 13.65  ?  309  TRP A CG     1 
ATOM   4783  C CD1    . TRP A 1 309 ? 21.916  -26.813 -9.447  1.00 14.17  ?  309  TRP A CD1    1 
ATOM   4784  C CD2    . TRP A 1 309 ? 20.916  -26.407 -11.408 1.00 13.34  ?  309  TRP A CD2    1 
ATOM   4785  N NE1    . TRP A 1 309 ? 22.769  -26.039 -10.196 1.00 14.42  ?  309  TRP A NE1    1 
ATOM   4786  C CE2    . TRP A 1 309 ? 22.182  -25.787 -11.410 1.00 14.06  ?  309  TRP A CE2    1 
ATOM   4787  C CE3    . TRP A 1 309 ? 20.110  -26.299 -12.544 1.00 14.19  ?  309  TRP A CE3    1 
ATOM   4788  C CZ2    . TRP A 1 309 ? 22.642  -25.049 -12.488 1.00 14.29  ?  309  TRP A CZ2    1 
ATOM   4789  C CZ3    . TRP A 1 309 ? 20.575  -25.584 -13.625 1.00 14.43  ?  309  TRP A CZ3    1 
ATOM   4790  C CH2    . TRP A 1 309 ? 21.832  -24.955 -13.587 1.00 15.29  ?  309  TRP A CH2    1 
ATOM   4791  H H      . TRP A 1 309 ? 17.942  -29.689 -9.595  1.00 17.31  ?  309  TRP A H      1 
ATOM   4792  H HA     . TRP A 1 309 ? 19.529  -28.934 -11.487 1.00 16.47  ?  309  TRP A HA     1 
ATOM   4793  H HB2    . TRP A 1 309 ? 18.800  -27.404 -9.873  1.00 16.68  ?  309  TRP A HB2    1 
ATOM   4794  H HB3    . TRP A 1 309 ? 19.716  -28.114 -8.786  1.00 16.68  ?  309  TRP A HB3    1 
ATOM   4795  H HD1    . TRP A 1 309 ? 22.092  -27.120 -8.587  1.00 17.00  ?  309  TRP A HD1    1 
ATOM   4796  H HE1    . TRP A 1 309 ? 23.543  -25.759 -9.945  1.00 17.30  ?  309  TRP A HE1    1 
ATOM   4797  H HE3    . TRP A 1 309 ? 19.274  -26.704 -12.570 1.00 17.02  ?  309  TRP A HE3    1 
ATOM   4798  H HZ2    . TRP A 1 309 ? 23.473  -24.632 -12.466 1.00 17.15  ?  309  TRP A HZ2    1 
ATOM   4799  H HZ3    . TRP A 1 309 ? 20.050  -25.515 -14.390 1.00 17.32  ?  309  TRP A HZ3    1 
ATOM   4800  H HH2    . TRP A 1 309 ? 22.119  -24.466 -14.323 1.00 18.34  ?  309  TRP A HH2    1 
ATOM   4801  N N      . GLN A 1 310 ? 20.991  -30.715 -9.292  1.00 15.26  ?  310  GLN A N      1 
ATOM   4802  C CA     . GLN A 1 310 ? 22.193  -31.489 -9.037  1.00 17.35  ?  310  GLN A CA     1 
ATOM   4803  C C      . GLN A 1 310 ? 22.514  -32.433 -10.181 1.00 15.94  ?  310  GLN A C      1 
ATOM   4804  O O      . GLN A 1 310 ? 23.619  -32.585 -10.549 1.00 16.72  ?  310  GLN A O      1 
ATOM   4805  C CB     . GLN A 1 310 ? 22.088  -32.246 -7.722  1.00 23.85  ?  310  GLN A CB     1 
ATOM   4806  C CG     . GLN A 1 310 ? 23.367  -32.949 -7.342  1.00 39.58  ?  310  GLN A CG     1 
ATOM   4807  C CD     . GLN A 1 310 ? 23.277  -33.558 -5.929  1.00 51.72  ?  310  GLN A CD     1 
ATOM   4808  O OE1    . GLN A 1 310 ? 22.296  -33.364 -5.227  1.00 56.37  ?  310  GLN A OE1    1 
ATOM   4809  N NE2    . GLN A 1 310 ? 24.334  -34.271 -5.503  1.00 55.02  ?  310  GLN A NE2    1 
ATOM   4810  H H      . GLN A 1 310 ? 20.374  -30.806 -8.700  1.00 18.31  ?  310  GLN A H      1 
ATOM   4811  H HA     . GLN A 1 310 ? 22.946  -30.867 -8.954  1.00 20.82  ?  310  GLN A HA     1 
ATOM   4812  H HB2    . GLN A 1 310 ? 21.869  -31.619 -7.014  1.00 28.62  ?  310  GLN A HB2    1 
ATOM   4813  H HB3    . GLN A 1 310 ? 21.390  -32.915 -7.799  1.00 28.62  ?  310  GLN A HB3    1 
ATOM   4814  H HG2    . GLN A 1 310 ? 23.536  -33.668 -7.972  1.00 47.49  ?  310  GLN A HG2    1 
ATOM   4815  H HG3    . GLN A 1 310 ? 24.099  -32.313 -7.354  1.00 47.49  ?  310  GLN A HG3    1 
ATOM   4816  H HE21   . GLN A 1 310 ? 25.050  -34.305 -5.979  1.00 66.02  ?  310  GLN A HE21   1 
ATOM   4817  H HE22   . GLN A 1 310 ? 24.295  -34.694 -4.756  1.00 66.02  ?  310  GLN A HE22   1 
ATOM   4818  N N      . VAL A 1 311 ? 21.502  -33.042 -10.747 1.00 15.38  ?  311  VAL A N      1 
ATOM   4819  C CA     . VAL A 1 311 ? 21.699  -33.957 -11.864 1.00 14.67  ?  311  VAL A CA     1 
ATOM   4820  C C      . VAL A 1 311 ? 22.000  -33.192 -13.153 1.00 15.74  ?  311  VAL A C      1 
ATOM   4821  O O      . VAL A 1 311 ? 22.758  -33.685 -13.987 1.00 15.39  ?  311  VAL A O      1 
ATOM   4822  C CB     . VAL A 1 311 ? 20.473  -34.876 -11.996 1.00 16.46  ?  311  VAL A CB     1 
ATOM   4823  C CG1    . VAL A 1 311 ? 20.567  -35.745 -13.247 1.00 15.34  ?  311  VAL A CG1    1 
ATOM   4824  C CG2    . VAL A 1 311 ? 20.355  -35.763 -10.759 1.00 16.60  ?  311  VAL A CG2    1 
ATOM   4825  H H      . VAL A 1 311 ? 20.680  -32.944 -10.517 1.00 18.46  ?  311  VAL A H      1 
ATOM   4826  H HA     . VAL A 1 311 ? 22.471  -34.519 -11.689 1.00 17.60  ?  311  VAL A HA     1 
ATOM   4827  H HB     . VAL A 1 311 ? 19.679  -34.323 -12.073 1.00 19.75  ?  311  VAL A HB     1 
ATOM   4828  H HG11   . VAL A 1 311 ? 19.848  -36.396 -13.235 1.00 18.41  ?  311  VAL A HG11   1 
ATOM   4829  H HG12   . VAL A 1 311 ? 20.488  -35.179 -14.031 1.00 18.41  ?  311  VAL A HG12   1 
ATOM   4830  H HG13   . VAL A 1 311 ? 21.425  -36.198 -13.252 1.00 18.41  ?  311  VAL A HG13   1 
ATOM   4831  H HG21   . VAL A 1 311 ? 19.582  -36.340 -10.857 1.00 19.91  ?  311  VAL A HG21   1 
ATOM   4832  H HG22   . VAL A 1 311 ? 21.160  -36.299 -10.678 1.00 19.91  ?  311  VAL A HG22   1 
ATOM   4833  H HG23   . VAL A 1 311 ? 20.252  -35.201 -9.976  1.00 19.91  ?  311  VAL A HG23   1 
ATOM   4834  N N      . LEU A 1 312 ? 21.443  -31.987 -13.329 1.00 15.05  ?  312  LEU A N      1 
ATOM   4835  C CA     . LEU A 1 312 ? 21.840  -31.152 -14.459 1.00 15.11  ?  312  LEU A CA     1 
ATOM   4836  C C      . LEU A 1 312 ? 23.318  -30.776 -14.365 1.00 14.98  ?  312  LEU A C      1 
ATOM   4837  O O      . LEU A 1 312 ? 24.015  -30.742 -15.382 1.00 15.86  ?  312  LEU A O      1 
ATOM   4838  C CB     . LEU A 1 312 ? 20.956  -29.920 -14.551 1.00 14.69  ?  312  LEU A CB     1 
ATOM   4839  C CG     . LEU A 1 312 ? 19.478  -30.206 -14.828 1.00 15.80  ?  312  LEU A CG     1 
ATOM   4840  C CD1    . LEU A 1 312 ? 18.739  -28.886 -15.049 1.00 16.90  ?  312  LEU A CD1    1 
ATOM   4841  C CD2    . LEU A 1 312 ? 19.280  -31.144 -15.980 1.00 20.66  ?  312  LEU A CD2    1 
ATOM   4842  H H      . LEU A 1 312 ? 20.846  -31.638 -12.818 1.00 18.06  ?  312  LEU A H      1 
ATOM   4843  H HA     . LEU A 1 312 ? 21.713  -31.651 -15.281 1.00 18.13  ?  312  LEU A HA     1 
ATOM   4844  H HB2    . LEU A 1 312 ? 21.008  -29.442 -13.709 1.00 17.63  ?  312  LEU A HB2    1 
ATOM   4845  H HB3    . LEU A 1 312 ? 21.285  -29.360 -15.272 1.00 17.63  ?  312  LEU A HB3    1 
ATOM   4846  H HG     . LEU A 1 312 ? 19.097  -30.655 -14.057 1.00 18.96  ?  312  LEU A HG     1 
ATOM   4847  H HD11   . LEU A 1 312 ? 17.823  -29.075 -15.304 1.00 20.28  ?  312  LEU A HD11   1 
ATOM   4848  H HD12   . LEU A 1 312 ? 18.754  -28.374 -14.225 1.00 20.28  ?  312  LEU A HD12   1 
ATOM   4849  H HD13   . LEU A 1 312 ? 19.183  -28.389 -15.754 1.00 20.28  ?  312  LEU A HD13   1 
ATOM   4850  H HD21   . LEU A 1 312 ? 18.336  -31.180 -16.199 1.00 24.78  ?  312  LEU A HD21   1 
ATOM   4851  H HD22   . LEU A 1 312 ? 19.785  -30.818 -16.742 1.00 24.78  ?  312  LEU A HD22   1 
ATOM   4852  H HD23   . LEU A 1 312 ? 19.596  -32.025 -15.727 1.00 24.78  ?  312  LEU A HD23   1 
ATOM   4853  N N      . GLU A 1 313 ? 23.819  -30.528 -13.149 1.00 16.24  ?  313  GLU A N      1 
ATOM   4854  C CA     . GLU A 1 313 ? 25.246  -30.290 -12.978 1.00 15.02  ?  313  GLU A CA     1 
ATOM   4855  C C      . GLU A 1 313 ? 26.043  -31.545 -13.331 1.00 15.87  ?  313  GLU A C      1 
ATOM   4856  O O      . GLU A 1 313 ? 27.073  -31.471 -14.010 1.00 17.36  ?  313  GLU A O      1 
ATOM   4857  C CB     . GLU A 1 313 ? 25.545  -29.856 -11.546 1.00 16.34  ?  313  GLU A CB     1 
ATOM   4858  C CG     . GLU A 1 313 ? 25.077  -28.447 -11.218 1.00 17.25  ?  313  GLU A CG     1 
ATOM   4859  C CD     . GLU A 1 313 ? 25.685  -27.878 -9.946  1.00 18.00  ?  313  GLU A CD     1 
ATOM   4860  O OE1    . GLU A 1 313 ? 26.354  -28.626 -9.183  1.00 20.83  ?  313  GLU A OE1    1 
ATOM   4861  O OE2    . GLU A 1 313 ? 25.500  -26.672 -9.694  1.00 19.23  -1 313  GLU A OE2    1 
ATOM   4862  H H      . GLU A 1 313 ? 23.360  -30.493 -12.423 1.00 19.48  ?  313  GLU A H      1 
ATOM   4863  H HA     . GLU A 1 313 ? 25.519  -29.569 -13.568 1.00 18.02  ?  313  GLU A HA     1 
ATOM   4864  H HB2    . GLU A 1 313 ? 25.099  -30.465 -10.937 1.00 19.60  ?  313  GLU A HB2    1 
ATOM   4865  H HB3    . GLU A 1 313 ? 26.504  -29.889 -11.404 1.00 19.60  ?  313  GLU A HB3    1 
ATOM   4866  H HG2    . GLU A 1 313 ? 25.320  -27.859 -11.950 1.00 20.70  ?  313  GLU A HG2    1 
ATOM   4867  H HG3    . GLU A 1 313 ? 24.113  -28.456 -11.106 1.00 20.70  ?  313  GLU A HG3    1 
ATOM   4868  N N      . GLN A 1 314 ? 25.594  -32.705 -12.853 1.00 16.23  ?  314  GLN A N      1 
ATOM   4869  C CA     . GLN A 1 314 ? 26.297  -33.944 -13.164 1.00 17.06  ?  314  GLN A CA     1 
ATOM   4870  C C      . GLN A 1 314 ? 26.346  -34.190 -14.662 1.00 16.51  ?  314  GLN A C      1 
ATOM   4871  O O      . GLN A 1 314 ? 27.385  -34.594 -15.202 1.00 18.09  ?  314  GLN A O      1 
ATOM   4872  C CB     . GLN A 1 314 ? 25.611  -35.116 -12.452 1.00 18.54  ?  314  GLN A CB     1 
ATOM   4873  C CG     . GLN A 1 314 ? 26.192  -36.477 -12.784 1.00 24.81  ?  314  GLN A CG     1 
ATOM   4874  C CD     . GLN A 1 314 ? 25.396  -37.628 -12.178 1.00 31.43  ?  314  GLN A CD     1 
ATOM   4875  O OE1    . GLN A 1 314 ? 24.700  -37.464 -11.160 1.00 32.20  ?  314  GLN A OE1    1 
ATOM   4876  N NE2    . GLN A 1 314 ? 25.496  -38.804 -12.797 1.00 33.45  ?  314  GLN A NE2    1 
ATOM   4877  H H      . GLN A 1 314 ? 24.899  -32.801 -12.357 1.00 19.47  ?  314  GLN A H      1 
ATOM   4878  H HA     . GLN A 1 314 ? 27.210  -33.879 -12.842 1.00 20.47  ?  314  GLN A HA     1 
ATOM   4879  H HB2    . GLN A 1 314 ? 25.694  -34.987 -11.494 1.00 22.24  ?  314  GLN A HB2    1 
ATOM   4880  H HB3    . GLN A 1 314 ? 24.675  -35.126 -12.705 1.00 22.24  ?  314  GLN A HB3    1 
ATOM   4881  H HG2    . GLN A 1 314 ? 26.197  -36.591 -13.747 1.00 29.77  ?  314  GLN A HG2    1 
ATOM   4882  H HG3    . GLN A 1 314 ? 27.098  -36.526 -12.440 1.00 29.77  ?  314  GLN A HG3    1 
ATOM   4883  H HE21   . GLN A 1 314 ? 25.989  -38.881 -13.497 1.00 40.14  ?  314  GLN A HE21   1 
ATOM   4884  H HE22   . GLN A 1 314 ? 25.067  -39.486 -12.496 1.00 40.14  ?  314  GLN A HE22   1 
ATOM   4885  N N      . GLY A 1 315 ? 25.218  -33.996 -15.343 1.00 15.94  ?  315  GLY A N      1 
ATOM   4886  C CA     . GLY A 1 315 ? 25.156  -34.249 -16.774 1.00 17.50  ?  315  GLY A CA     1 
ATOM   4887  C C      . GLY A 1 315 ? 26.056  -33.321 -17.569 1.00 16.43  ?  315  GLY A C      1 
ATOM   4888  O O      . GLY A 1 315 ? 26.761  -33.760 -18.482 1.00 17.10  ?  315  GLY A O      1 
ATOM   4889  H H      . GLY A 1 315 ? 24.478  -33.721 -15.002 1.00 19.13  ?  315  GLY A H      1 
ATOM   4890  H HA2    . GLY A 1 315 ? 25.430  -35.163 -16.949 1.00 21.00  ?  315  GLY A HA2    1 
ATOM   4891  H HA3    . GLY A 1 315 ? 24.245  -34.128 -17.081 1.00 21.00  ?  315  GLY A HA3    1 
ATOM   4892  N N      . THR A 1 316 ? 26.043  -32.023 -17.242 1.00 15.82  ?  316  THR A N      1 
ATOM   4893  C CA     . THR A 1 316 ? 26.902  -31.096 -17.983 1.00 15.29  ?  316  THR A CA     1 
ATOM   4894  C C      . THR A 1 316 ? 28.372  -31.343 -17.660 1.00 15.25  ?  316  THR A C      1 
ATOM   4895  O O      . THR A 1 316 ? 29.230  -31.157 -18.521 1.00 17.18  ?  316  THR A O      1 
ATOM   4896  C CB     . THR A 1 316 ? 26.502  -29.639 -17.761 1.00 15.87  ?  316  THR A CB     1 
ATOM   4897  O OG1    . THR A 1 316 ? 26.462  -29.323 -16.363 1.00 16.88  ?  316  THR A OG1    1 
ATOM   4898  C CG2    . THR A 1 316 ? 25.140  -29.355 -18.411 1.00 15.68  ?  316  THR A CG2    1 
ATOM   4899  H H      . THR A 1 316 ? 25.566  -31.667 -16.622 1.00 18.99  ?  316  THR A H      1 
ATOM   4900  H HA     . THR A 1 316 ? 26.773  -31.249 -18.932 1.00 18.35  ?  316  THR A HA     1 
ATOM   4901  H HB     . THR A 1 316 ? 27.164  -29.064 -18.176 1.00 19.04  ?  316  THR A HB     1 
ATOM   4902  H HG1    . THR A 1 316 ? 25.794  -29.686 -16.005 1.00 20.26  ?  316  THR A HG1    1 
ATOM   4903  H HG21   . THR A 1 316 ? 24.892  -28.428 -18.269 1.00 18.81  ?  316  THR A HG21   1 
ATOM   4904  H HG22   . THR A 1 316 ? 25.184  -29.528 -19.364 1.00 18.81  ?  316  THR A HG22   1 
ATOM   4905  H HG23   . THR A 1 316 ? 24.460  -29.926 -18.019 1.00 18.81  ?  316  THR A HG23   1 
ATOM   4906  N N      . GLY A 1 317 ? 28.671  -31.788 -16.437 1.00 16.64  ?  317  GLY A N      1 
ATOM   4907  C CA     . GLY A 1 317 ? 30.022  -32.215 -16.139 1.00 18.43  ?  317  GLY A CA     1 
ATOM   4908  C C      . GLY A 1 317 ? 30.485  -33.342 -17.039 1.00 17.82  ?  317  GLY A C      1 
ATOM   4909  O O      . GLY A 1 317 ? 31.635  -33.363 -17.463 1.00 19.85  ?  317  GLY A O      1 
ATOM   4910  H H      . GLY A 1 317 ? 28.120  -31.850 -15.780 1.00 19.97  ?  317  GLY A H      1 
ATOM   4911  H HA2    . GLY A 1 317 ? 30.628  -31.466 -16.251 1.00 22.11  ?  317  GLY A HA2    1 
ATOM   4912  H HA3    . GLY A 1 317 ? 30.066  -32.522 -15.219 1.00 22.11  ?  317  GLY A HA3    1 
ATOM   4913  N N      . GLU A 1 318 ? 29.591  -34.289 -17.345 1.00 18.36  ?  318  GLU A N      1 
ATOM   4914  C CA     . GLU A 1 318 ? 29.946  -35.430 -18.183 1.00 18.45  ?  318  GLU A CA     1 
ATOM   4915  C C      . GLU A 1 318 ? 29.912  -35.081 -19.671 1.00 18.59  ?  318  GLU A C      1 
ATOM   4916  O O      . GLU A 1 318 ? 30.747  -35.565 -20.436 1.00 21.86  ?  318  GLU A O      1 
ATOM   4917  C CB     . GLU A 1 318 ? 28.984  -36.601 -17.947 1.00 23.33  ?  318  GLU A CB     1 
ATOM   4918  C CG     . GLU A 1 318 ? 29.073  -37.241 -16.576 1.00 29.18  ?  318  GLU A CG     1 
ATOM   4919  C CD     . GLU A 1 318 ? 28.024  -38.325 -16.343 1.00 32.72  ?  318  GLU A CD     1 
ATOM   4920  O OE1    . GLU A 1 318 ? 27.610  -38.978 -17.323 1.00 29.84  ?  318  GLU A OE1    1 
ATOM   4921  O OE2    . GLU A 1 318 ? 27.651  -38.531 -15.157 1.00 36.60  -1 318  GLU A OE2    1 
ATOM   4922  H H      . GLU A 1 318 ? 28.773  -34.292 -17.079 1.00 22.03  ?  318  GLU A H      1 
ATOM   4923  H HA     . GLU A 1 318 ? 30.843  -35.699 -17.934 1.00 22.13  ?  318  GLU A HA     1 
ATOM   4924  H HB2    . GLU A 1 318 ? 28.076  -36.279 -18.059 1.00 27.99  ?  318  GLU A HB2    1 
ATOM   4925  H HB3    . GLU A 1 318 ? 29.174  -37.291 -18.602 1.00 27.99  ?  318  GLU A HB3    1 
ATOM   4926  H HG2    . GLU A 1 318 ? 29.948  -37.648 -16.476 1.00 35.01  ?  318  GLU A HG2    1 
ATOM   4927  H HG3    . GLU A 1 318 ? 28.947  -36.555 -15.901 1.00 35.01  ?  318  GLU A HG3    1 
ATOM   4928  N N      . PHE A 1 319 ? 28.945  -34.265 -20.112 1.00 18.94  ?  319  PHE A N      1 
ATOM   4929  C CA     . PHE A 1 319 ? 28.649  -34.133 -21.535 1.00 18.84  ?  319  PHE A CA     1 
ATOM   4930  C C      . PHE A 1 319 ? 28.852  -32.735 -22.103 1.00 19.94  ?  319  PHE A C      1 
ATOM   4931  O O      . PHE A 1 319 ? 28.773  -32.571 -23.325 1.00 21.63  ?  319  PHE A O      1 
ATOM   4932  C CB     . PHE A 1 319 ? 27.207  -34.585 -21.820 1.00 19.85  ?  319  PHE A CB     1 
ATOM   4933  C CG     . PHE A 1 319 ? 26.933  -36.018 -21.447 1.00 20.51  ?  319  PHE A CG     1 
ATOM   4934  C CD1    . PHE A 1 319 ? 27.672  -37.051 -21.991 1.00 22.06  ?  319  PHE A CD1    1 
ATOM   4935  C CD2    . PHE A 1 319 ? 25.917  -36.333 -20.568 1.00 21.02  ?  319  PHE A CD2    1 
ATOM   4936  C CE1    . PHE A 1 319 ? 27.403  -38.369 -21.662 1.00 22.79  ?  319  PHE A CE1    1 
ATOM   4937  C CE2    . PHE A 1 319 ? 25.654  -37.653 -20.229 1.00 22.39  ?  319  PHE A CE2    1 
ATOM   4938  C CZ     . PHE A 1 319 ? 26.404  -38.668 -20.771 1.00 23.81  ?  319  PHE A CZ     1 
ATOM   4939  H H      . PHE A 1 319 ? 28.451  -33.780 -19.602 1.00 22.73  ?  319  PHE A H      1 
ATOM   4940  H HA     . PHE A 1 319 ? 29.252  -34.719 -22.019 1.00 22.60  ?  319  PHE A HA     1 
ATOM   4941  H HB2    . PHE A 1 319 ? 26.599  -34.025 -21.311 1.00 23.82  ?  319  PHE A HB2    1 
ATOM   4942  H HB3    . PHE A 1 319 ? 27.031  -34.487 -22.769 1.00 23.82  ?  319  PHE A HB3    1 
ATOM   4943  H HD1    . PHE A 1 319 ? 28.359  -36.859 -22.587 1.00 26.47  ?  319  PHE A HD1    1 
ATOM   4944  H HD2    . PHE A 1 319 ? 25.403  -35.653 -20.198 1.00 25.22  ?  319  PHE A HD2    1 
ATOM   4945  H HE1    . PHE A 1 319 ? 27.901  -39.054 -22.046 1.00 27.34  ?  319  PHE A HE1    1 
ATOM   4946  H HE2    . PHE A 1 319 ? 24.968  -37.851 -19.633 1.00 26.86  ?  319  PHE A HE2    1 
ATOM   4947  H HZ     . PHE A 1 319 ? 26.235  -39.552 -20.536 1.00 28.56  ?  319  PHE A HZ     1 
ATOM   4948  N N      . GLY A 1 320 ? 29.087  -31.732 -21.264 1.00 18.58  ?  320  GLY A N      1 
ATOM   4949  C CA     . GLY A 1 320 ? 29.353  -30.399 -21.738 1.00 17.78  ?  320  GLY A CA     1 
ATOM   4950  C C      . GLY A 1 320 ? 28.118  -29.519 -21.723 1.00 16.33  ?  320  GLY A C      1 
ATOM   4951  O O      . GLY A 1 320 ? 27.087  -29.875 -21.162 1.00 16.34  ?  320  GLY A O      1 
ATOM   4952  H H      . GLY A 1 320 ? 29.095  -31.809 -20.407 1.00 22.29  ?  320  GLY A H      1 
ATOM   4953  H HA2    . GLY A 1 320 ? 30.028  -29.987 -21.175 1.00 21.34  ?  320  GLY A HA2    1 
ATOM   4954  H HA3    . GLY A 1 320 ? 29.686  -30.443 -22.648 1.00 21.34  ?  320  GLY A HA3    1 
ATOM   4955  N N      . PRO A 1 321 ? 28.210  -28.348 -22.359 1.00 17.03  ?  321  PRO A N      1 
ATOM   4956  C CA     . PRO A 1 321 ? 27.101  -27.390 -22.318 1.00 16.21  ?  321  PRO A CA     1 
ATOM   4957  C C      . PRO A 1 321 ? 25.783  -28.012 -22.760 1.00 15.26  ?  321  PRO A C      1 
ATOM   4958  O O      . PRO A 1 321 ? 25.729  -28.817 -23.694 1.00 17.39  ?  321  PRO A O      1 
ATOM   4959  C CB     . PRO A 1 321 ? 27.562  -26.289 -23.277 1.00 17.33  ?  321  PRO A CB     1 
ATOM   4960  C CG     . PRO A 1 321 ? 29.062  -26.365 -23.232 1.00 17.14  ?  321  PRO A CG     1 
ATOM   4961  C CD     . PRO A 1 321 ? 29.377  -27.825 -23.098 1.00 18.80  ?  321  PRO A CD     1 
ATOM   4962  H HA     . PRO A 1 321 ? 26.995  -27.033 -21.422 1.00 19.45  ?  321  PRO A HA     1 
ATOM   4963  H HB2    . PRO A 1 321 ? 27.230  -26.465 -24.171 1.00 20.79  ?  321  PRO A HB2    1 
ATOM   4964  H HB3    . PRO A 1 321 ? 27.246  -25.425 -22.970 1.00 20.79  ?  321  PRO A HB3    1 
ATOM   4965  H HG2    . PRO A 1 321 ? 29.435  -26.004 -24.051 1.00 20.56  ?  321  PRO A HG2    1 
ATOM   4966  H HG3    . PRO A 1 321 ? 29.394  -25.867 -22.468 1.00 20.56  ?  321  PRO A HG3    1 
ATOM   4967  H HD2    . PRO A 1 321 ? 29.452  -28.245 -23.969 1.00 22.56  ?  321  PRO A HD2    1 
ATOM   4968  H HD3    . PRO A 1 321 ? 30.194  -27.958 -22.594 1.00 22.56  ?  321  PRO A HD3    1 
ATOM   4969  N N      . ILE A 1 322 ? 24.708  -27.626 -22.079 1.00 14.86  ?  322  ILE A N      1 
ATOM   4970  C CA     . ILE A 1 322 ? 23.394  -28.204 -22.329 1.00 15.82  ?  322  ILE A CA     1 
ATOM   4971  C C      . ILE A 1 322 ? 22.843  -27.713 -23.666 1.00 13.58  ?  322  ILE A C      1 
ATOM   4972  O O      . ILE A 1 322 ? 22.893  -26.515 -23.989 1.00 13.51  ?  322  ILE A O      1 
ATOM   4973  C CB     . ILE A 1 322 ? 22.452  -27.924 -21.146 1.00 17.75  ?  322  ILE A CB     1 
ATOM   4974  C CG1    . ILE A 1 322 ? 21.161  -28.732 -21.326 1.00 21.63  ?  322  ILE A CG1    1 
ATOM   4975  C CG2    . ILE A 1 322 ? 22.159  -26.456 -21.024 1.00 18.49  ?  322  ILE A CG2    1 
ATOM   4976  C CD1    . ILE A 1 322 ? 20.765  -29.555 -20.197 1.00 25.78  ?  322  ILE A CD1    1 
ATOM   4977  H H      . ILE A 1 322 ? 24.712  -27.027 -21.463 1.00 17.82  ?  322  ILE A H      1 
ATOM   4978  H HA     . ILE A 1 322 ? 23.479  -29.167 -22.408 1.00 18.98  ?  322  ILE A HA     1 
ATOM   4979  H HB     . ILE A 1 322 ? 22.887  -28.201 -20.324 1.00 21.30  ?  322  ILE A HB     1 
ATOM   4980  H HG12   . ILE A 1 322 ? 20.436  -28.111 -21.497 1.00 25.95  ?  322  ILE A HG12   1 
ATOM   4981  H HG13   . ILE A 1 322 ? 21.277  -29.323 -22.086 1.00 25.95  ?  322  ILE A HG13   1 
ATOM   4982  H HG21   . ILE A 1 322 ? 21.724  -26.290 -20.173 1.00 22.18  ?  322  ILE A HG21   1 
ATOM   4983  H HG22   . ILE A 1 322 ? 22.993  -25.963 -21.072 1.00 22.18  ?  322  ILE A HG22   1 
ATOM   4984  H HG23   . ILE A 1 322 ? 21.575  -26.190 -21.752 1.00 22.18  ?  322  ILE A HG23   1 
ATOM   4985  H HD11   . ILE A 1 322 ? 19.982  -30.072 -20.442 1.00 30.94  ?  322  ILE A HD11   1 
ATOM   4986  H HD12   . ILE A 1 322 ? 21.496  -30.151 -19.969 1.00 30.94  ?  322  ILE A HD12   1 
ATOM   4987  H HD13   . ILE A 1 322 ? 20.560  -28.980 -19.443 1.00 30.94  ?  322  ILE A HD13   1 
ATOM   4988  N N      . GLY A 1 323 ? 22.356  -28.653 -24.478 1.00 14.47  ?  323  GLY A N      1 
ATOM   4989  C CA     . GLY A 1 323 ? 21.849  -28.365 -25.810 1.00 12.36  ?  323  GLY A CA     1 
ATOM   4990  C C      . GLY A 1 323 ? 20.417  -27.852 -25.806 1.00 12.34  ?  323  GLY A C      1 
ATOM   4991  O O      . GLY A 1 323 ? 19.478  -28.557 -26.206 1.00 12.58  ?  323  GLY A O      1 
ATOM   4992  H H      . GLY A 1 323 ? 22.308  -29.486 -24.272 1.00 17.36  ?  323  GLY A H      1 
ATOM   4993  H HA2    . GLY A 1 323 ? 22.411  -27.693 -26.225 1.00 14.83  ?  323  GLY A HA2    1 
ATOM   4994  H HA3    . GLY A 1 323 ? 21.879  -29.175 -26.343 1.00 14.83  ?  323  GLY A HA3    1 
ATOM   4995  N N      . HIS A 1 324 ? 20.256  -26.611 -25.340 1.00 12.34  ?  324  HIS A N      1 
ATOM   4996  C CA     . HIS A 1 324 ? 18.938  -26.001 -25.214 1.00 12.28  ?  324  HIS A CA     1 
ATOM   4997  C C      . HIS A 1 324 ? 19.094  -24.488 -25.233 1.00 11.48  ?  324  HIS A C      1 
ATOM   4998  O O      . HIS A 1 324 ? 19.990  -23.934 -24.578 1.00 14.47  ?  324  HIS A O      1 
ATOM   4999  C CB     . HIS A 1 324 ? 18.265  -26.421 -23.918 1.00 14.07  ?  324  HIS A CB     1 
ATOM   5000  C CG     . HIS A 1 324 ? 16.831  -26.034 -23.854 1.00 12.82  ?  324  HIS A CG     1 
ATOM   5001  N ND1    . HIS A 1 324 ? 15.929  -26.423 -24.819 1.00 11.64  ?  324  HIS A ND1    1 
ATOM   5002  C CD2    . HIS A 1 324 ? 16.148  -25.263 -22.976 1.00 12.82  ?  324  HIS A CD2    1 
ATOM   5003  C CE1    . HIS A 1 324 ? 14.738  -25.925 -24.519 1.00 12.46  ?  324  HIS A CE1    1 
ATOM   5004  N NE2    . HIS A 1 324 ? 14.843  -25.227 -23.399 1.00 12.39  ?  324  HIS A NE2    1 
ATOM   5005  H H      . HIS A 1 324 ? 20.901  -26.101 -25.088 1.00 14.80  ?  324  HIS A H      1 
ATOM   5006  H HA     . HIS A 1 324 ? 18.385  -26.270 -25.964 1.00 14.74  ?  324  HIS A HA     1 
ATOM   5007  H HB2    . HIS A 1 324 ? 18.318  -27.386 -23.835 1.00 16.88  ?  324  HIS A HB2    1 
ATOM   5008  H HB3    . HIS A 1 324 ? 18.722  -25.999 -23.175 1.00 16.88  ?  324  HIS A HB3    1 
ATOM   5009  H HD2    . HIS A 1 324 ? 16.498  -24.837 -22.226 1.00 15.38  ?  324  HIS A HD2    1 
ATOM   5010  H HE1    . HIS A 1 324 ? 13.959  -26.045 -25.013 1.00 14.95  ?  324  HIS A HE1    1 
ATOM   5011  H HE2    . HIS A 1 324 ? 14.199  -24.817 -23.002 1.00 14.86  ?  324  HIS A HE2    1 
ATOM   5012  N N      . GLY A 1 325 ? 18.214  -23.825 -25.963 1.00 11.55  ?  325  GLY A N      1 
ATOM   5013  C CA     . GLY A 1 325 ? 18.201  -22.379 -25.975 1.00 11.52  ?  325  GLY A CA     1 
ATOM   5014  C C      . GLY A 1 325 ? 17.133  -21.838 -26.895 1.00 12.00  ?  325  GLY A C      1 
ATOM   5015  O O      . GLY A 1 325 ? 16.819  -22.455 -27.923 1.00 14.42  ?  325  GLY A O      1 
ATOM   5016  H H      . GLY A 1 325 ? 17.615  -24.191 -26.460 1.00 13.85  ?  325  GLY A H      1 
ATOM   5017  H HA2    . GLY A 1 325 ? 18.032  -22.049 -25.078 1.00 13.82  ?  325  GLY A HA2    1 
ATOM   5018  H HA3    . GLY A 1 325 ? 19.063  -22.050 -26.275 1.00 13.82  ?  325  GLY A HA3    1 
ATOM   5019  N N      . TRP A 1 326 ? 16.536  -20.711 -26.502 1.00 12.37  ?  326  TRP A N      1 
ATOM   5020  C CA     . TRP A 1 326 ? 15.707  -19.907 -27.385 1.00 11.84  ?  326  TRP A CA     1 
ATOM   5021  C C      . TRP A 1 326 ? 16.415  -18.571 -27.617 1.00 12.92  ?  326  TRP A C      1 
ATOM   5022  O O      . TRP A 1 326 ? 16.946  -17.981 -26.670 1.00 13.02  ?  326  TRP A O      1 
ATOM   5023  C CB     . TRP A 1 326 ? 14.344  -19.579 -26.759 1.00 13.99  ?  326  TRP A CB     1 
ATOM   5024  C CG     . TRP A 1 326 ? 13.639  -20.639 -25.973 1.00 13.01  ?  326  TRP A CG     1 
ATOM   5025  C CD1    . TRP A 1 326 ? 13.343  -20.576 -24.649 1.00 13.08  ?  326  TRP A CD1    1 
ATOM   5026  C CD2    . TRP A 1 326 ? 13.095  -21.884 -26.450 1.00 11.56  ?  326  TRP A CD2    1 
ATOM   5027  N NE1    . TRP A 1 326 ? 12.675  -21.709 -24.249 1.00 12.01  ?  326  TRP A NE1    1 
ATOM   5028  C CE2    . TRP A 1 326 ? 12.489  -22.518 -25.343 1.00 11.66  ?  326  TRP A CE2    1 
ATOM   5029  C CE3    . TRP A 1 326 ? 13.041  -22.521 -27.699 1.00 11.35  ?  326  TRP A CE3    1 
ATOM   5030  C CZ2    . TRP A 1 326 ? 11.864  -23.762 -25.445 1.00 11.28  ?  326  TRP A CZ2    1 
ATOM   5031  C CZ3    . TRP A 1 326 ? 12.405  -23.753 -27.800 1.00 12.12  ?  326  TRP A CZ3    1 
ATOM   5032  C CH2    . TRP A 1 326 ? 11.820  -24.358 -26.679 1.00 12.80  ?  326  TRP A CH2    1 
ATOM   5033  H H      . TRP A 1 326 ? 16.603  -20.390 -25.707 1.00 14.84  ?  326  TRP A H      1 
ATOM   5034  H HA     . TRP A 1 326 ? 15.567  -20.394 -28.212 1.00 14.20  ?  326  TRP A HA     1 
ATOM   5035  H HB2    . TRP A 1 326 ? 14.472  -18.830 -26.156 1.00 16.78  ?  326  TRP A HB2    1 
ATOM   5036  H HB3    . TRP A 1 326 ? 13.745  -19.327 -27.479 1.00 16.78  ?  326  TRP A HB3    1 
ATOM   5037  H HD1    . TRP A 1 326 ? 13.562  -19.865 -24.090 1.00 15.70  ?  326  TRP A HD1    1 
ATOM   5038  H HE1    . TRP A 1 326 ? 12.417  -21.882 -23.447 1.00 14.41  ?  326  TRP A HE1    1 
ATOM   5039  H HE3    . TRP A 1 326 ? 13.425  -22.125 -28.448 1.00 13.61  ?  326  TRP A HE3    1 
ATOM   5040  H HZ2    . TRP A 1 326 ? 11.490  -24.173 -24.700 1.00 13.54  ?  326  TRP A HZ2    1 
ATOM   5041  H HZ3    . TRP A 1 326 ? 12.367  -24.182 -28.624 1.00 14.54  ?  326  TRP A HZ3    1 
ATOM   5042  H HH2    . TRP A 1 326 ? 11.393  -25.179 -26.774 1.00 15.36  ?  326  TRP A HH2    1 
ATOM   5043  N N      . THR A 1 327 ? 16.374  -18.066 -28.860 1.00 12.33  ?  327  THR A N      1 
ATOM   5044  C CA     . THR A 1 327 ? 17.068  -16.822 -29.184 1.00 12.67  ?  327  THR A CA     1 
ATOM   5045  C C      . THR A 1 327 ? 16.760  -15.721 -28.183 1.00 13.15  ?  327  THR A C      1 
ATOM   5046  O O      . THR A 1 327 ? 17.666  -14.994 -27.755 1.00 14.13  ?  327  THR A O      1 
ATOM   5047  C CB     . THR A 1 327 ? 16.665  -16.359 -30.585 1.00 13.35  ?  327  THR A CB     1 
ATOM   5048  O OG1    . THR A 1 327 ? 16.979  -17.387 -31.528 1.00 17.66  ?  327  THR A OG1    1 
ATOM   5049  C CG2    . THR A 1 327 ? 17.378  -15.060 -30.988 1.00 14.74  ?  327  THR A CG2    1 
ATOM   5050  H H      . THR A 1 327 ? 15.957  -18.422 -29.522 1.00 14.80  ?  327  THR A H      1 
ATOM   5051  H HA     . THR A 1 327 ? 18.023  -16.994 -29.164 1.00 15.20  ?  327  THR A HA     1 
ATOM   5052  H HB     . THR A 1 327 ? 15.712  -16.177 -30.593 1.00 16.02  ?  327  THR A HB     1 
ATOM   5053  H HG1    . THR A 1 327 ? 16.526  -18.075 -31.364 1.00 21.18  ?  327  THR A HG1    1 
ATOM   5054  H HG21   . THR A 1 327 ? 17.178  -14.845 -31.912 1.00 17.68  ?  327  THR A HG21   1 
ATOM   5055  H HG22   . THR A 1 327 ? 17.080  -14.330 -30.423 1.00 17.68  ?  327  THR A HG22   1 
ATOM   5056  H HG23   . THR A 1 327 ? 18.337  -15.164 -30.889 1.00 17.68  ?  327  THR A HG23   1 
ATOM   5057  N N      . TYR A 1 328 ? 15.484  -15.582 -27.799 1.00 12.53  ?  328  TYR A N      1 
ATOM   5058  C CA     . TYR A 1 328 ? 15.036  -14.498 -26.935 1.00 13.26  ?  328  TYR A CA     1 
ATOM   5059  C C      . TYR A 1 328 ? 14.996  -14.868 -25.452 1.00 13.95  ?  328  TYR A C      1 
ATOM   5060  O O      . TYR A 1 328 ? 14.461  -14.078 -24.654 1.00 12.71  ?  328  TYR A O      1 
ATOM   5061  C CB     . TYR A 1 328 ? 13.673  -13.981 -27.397 1.00 12.94  ?  328  TYR A CB     1 
ATOM   5062  C CG     . TYR A 1 328 ? 13.644  -13.451 -28.830 1.00 12.38  ?  328  TYR A CG     1 
ATOM   5063  C CD1    . TYR A 1 328 ? 14.710  -12.704 -29.324 1.00 14.42  ?  328  TYR A CD1    1 
ATOM   5064  C CD2    . TYR A 1 328 ? 12.575  -13.687 -29.675 1.00 13.97  ?  328  TYR A CD2    1 
ATOM   5065  C CE1    . TYR A 1 328 ? 14.715  -12.215 -30.594 1.00 15.21  ?  328  TYR A CE1    1 
ATOM   5066  C CE2    . TYR A 1 328 ? 12.572  -13.196 -30.989 1.00 14.49  ?  328  TYR A CE2    1 
ATOM   5067  C CZ     . TYR A 1 328 ? 13.656  -12.442 -31.427 1.00 15.38  ?  328  TYR A CZ     1 
ATOM   5068  O OH     . TYR A 1 328 ? 13.697  -11.886 -32.699 1.00 17.47  ?  328  TYR A OH     1 
ATOM   5069  H H      . TYR A 1 328 ? 14.854  -16.117 -28.035 1.00 15.04  ?  328  TYR A H      1 
ATOM   5070  H HA     . TYR A 1 328 ? 15.669  -13.768 -27.020 1.00 15.90  ?  328  TYR A HA     1 
ATOM   5071  H HB2    . TYR A 1 328 ? 13.033  -14.708 -27.342 1.00 15.52  ?  328  TYR A HB2    1 
ATOM   5072  H HB3    . TYR A 1 328 ? 13.403  -13.256 -26.812 1.00 15.52  ?  328  TYR A HB3    1 
ATOM   5073  H HD1    . TYR A 1 328 ? 15.438  -12.534 -28.771 1.00 17.30  ?  328  TYR A HD1    1 
ATOM   5074  H HD2    . TYR A 1 328 ? 11.848  -14.179 -29.368 1.00 16.76  ?  328  TYR A HD2    1 
ATOM   5075  H HE1    . TYR A 1 328 ? 15.444  -11.723 -30.897 1.00 18.25  ?  328  TYR A HE1    1 
ATOM   5076  H HE2    . TYR A 1 328 ? 11.857  -13.371 -31.557 1.00 17.39  ?  328  TYR A HE2    1 
ATOM   5077  H HH     . TYR A 1 328 ? 14.401  -11.439 -32.795 1.00 20.96  ?  328  TYR A HH     1 
ATOM   5078  N N      . SER A 1 329 ? 15.585  -16.000 -25.063 1.00 13.52  ?  329  SER A N      1 
ATOM   5079  C CA     . SER A 1 329 ? 15.646  -16.377 -23.655 1.00 12.03  ?  329  SER A CA     1 
ATOM   5080  C C      . SER A 1 329 ? 16.301  -15.276 -22.831 1.00 11.52  ?  329  SER A C      1 
ATOM   5081  O O      . SER A 1 329 ? 17.387  -14.788 -23.169 1.00 13.62  ?  329  SER A O      1 
ATOM   5082  C CB     . SER A 1 329 ? 16.450  -17.665 -23.498 1.00 11.95  ?  329  SER A CB     1 
ATOM   5083  O OG     . SER A 1 329 ? 16.606  -18.036 -22.144 1.00 12.85  ?  329  SER A OG     1 
ATOM   5084  H H      . SER A 1 329 ? 15.955  -16.565 -25.594 1.00 16.22  ?  329  SER A H      1 
ATOM   5085  H HA     . SER A 1 329 ? 14.745  -16.523 -23.328 1.00 14.44  ?  329  SER A HA     1 
ATOM   5086  H HB2    . SER A 1 329 ? 15.986  -18.379 -23.964 1.00 14.34  ?  329  SER A HB2    1 
ATOM   5087  H HB3    . SER A 1 329 ? 17.329  -17.532 -23.886 1.00 14.34  ?  329  SER A HB3    1 
ATOM   5088  H HG     . SER A 1 329 ? 15.853  -18.120 -21.781 1.00 15.42  ?  329  SER A HG     1 
ATOM   5089  N N      . GLY A 1 330 ? 15.636  -14.884 -21.749 1.00 12.20  ?  330  GLY A N      1 
ATOM   5090  C CA     . GLY A 1 330 ? 16.191  -13.861 -20.882 1.00 12.64  ?  330  GLY A CA     1 
ATOM   5091  C C      . GLY A 1 330 ? 16.067  -12.430 -21.363 1.00 12.83  ?  330  GLY A C      1 
ATOM   5092  O O      . GLY A 1 330 ? 16.764  -11.556 -20.836 1.00 13.99  ?  330  GLY A O      1 
ATOM   5093  H H      . GLY A 1 330 ? 14.873  -15.192 -21.500 1.00 14.64  ?  330  GLY A H      1 
ATOM   5094  H HA2    . GLY A 1 330 ? 15.746  -13.917 -20.022 1.00 15.17  ?  330  GLY A HA2    1 
ATOM   5095  H HA3    . GLY A 1 330 ? 17.136  -14.044 -20.761 1.00 15.17  ?  330  GLY A HA3    1 
ATOM   5096  N N      . HIS A 1 331 ? 15.208  -12.170 -22.344 1.00 13.65  ?  331  HIS A N      1 
ATOM   5097  C CA     . HIS A 1 331 ? 15.087  -10.851 -22.958 1.00 14.03  ?  331  HIS A CA     1 
ATOM   5098  C C      . HIS A 1 331 ? 15.010  -9.765  -21.898 1.00 12.90  ?  331  HIS A C      1 
ATOM   5099  O O      . HIS A 1 331 ? 14.163  -9.813  -21.004 1.00 13.97  ?  331  HIS A O      1 
ATOM   5100  C CB     . HIS A 1 331 ? 13.819  -10.840 -23.818 1.00 12.81  ?  331  HIS A CB     1 
ATOM   5101  C CG     . HIS A 1 331 ? 13.764  -9.721  -24.805 1.00 11.78  ?  331  HIS A CG     1 
ATOM   5102  N ND1    . HIS A 1 331 ? 13.423  -8.429  -24.453 1.00 13.30  ?  331  HIS A ND1    1 
ATOM   5103  C CD2    . HIS A 1 331 ? 14.036  -9.695  -26.129 1.00 13.87  ?  331  HIS A CD2    1 
ATOM   5104  C CE1    . HIS A 1 331 ? 13.483  -7.664  -25.530 1.00 15.62  ?  331  HIS A CE1    1 
ATOM   5105  N NE2    . HIS A 1 331 ? 13.828  -8.414  -26.560 1.00 13.49  ?  331  HIS A NE2    1 
ATOM   5106  H H      . HIS A 1 331 ? 14.672  -12.752 -22.681 1.00 16.37  ?  331  HIS A H      1 
ATOM   5107  H HA     . HIS A 1 331 ? 15.860  -10.666 -23.513 1.00 16.83  ?  331  HIS A HA     1 
ATOM   5108  H HB2    . HIS A 1 331 ? 13.773  -11.673 -24.314 1.00 15.37  ?  331  HIS A HB2    1 
ATOM   5109  H HB3    . HIS A 1 331 ? 13.049  -10.757 -23.235 1.00 15.37  ?  331  HIS A HB3    1 
ATOM   5110  H HD2    . HIS A 1 331 ? 14.312  -10.415 -26.650 1.00 16.64  ?  331  HIS A HD2    1 
ATOM   5111  H HE1    . HIS A 1 331 ? 13.311  -6.751  -25.558 1.00 18.74  ?  331  HIS A HE1    1 
ATOM   5112  H HE2    . HIS A 1 331 ? 13.909  -8.141  -27.372 1.00 16.18  ?  331  HIS A HE2    1 
ATOM   5113  N N      . ALA A 1 332 ? 15.882  -8.759  -22.030 1.00 13.36  ?  332  ALA A N      1 
ATOM   5114  C CA     . ALA A 1 332 ? 16.041  -7.761  -20.976 1.00 13.43  ?  332  ALA A CA     1 
ATOM   5115  C C      . ALA A 1 332 ? 14.755  -6.980  -20.727 1.00 13.20  ?  332  ALA A C      1 
ATOM   5116  O O      . ALA A 1 332 ? 14.466  -6.614  -19.583 1.00 14.57  ?  332  ALA A O      1 
ATOM   5117  C CB     . ALA A 1 332 ? 17.176  -6.794  -21.342 1.00 14.21  ?  332  ALA A CB     1 
ATOM   5118  H H      . ALA A 1 332 ? 16.389  -8.634  -22.713 1.00 16.03  ?  332  ALA A H      1 
ATOM   5119  H HA     . ALA A 1 332 ? 16.271  -8.223  -20.155 1.00 16.12  ?  332  ALA A HA     1 
ATOM   5120  H HB1    . ALA A 1 332 ? 17.306  -6.169  -20.612 1.00 17.05  ?  332  ALA A HB1    1 
ATOM   5121  H HB2    . ALA A 1 332 ? 17.989  -7.302  -21.490 1.00 17.05  ?  332  ALA A HB2    1 
ATOM   5122  H HB3    . ALA A 1 332 ? 16.935  -6.314  -22.149 1.00 17.05  ?  332  ALA A HB3    1 
ATOM   5123  N N      . LEU A 1 333 ? 14.008  -6.656  -21.786 1.00 13.31  ?  333  LEU A N      1 
ATOM   5124  C CA     . LEU A 1 333 ? 12.756  -5.927  -21.604 1.00 11.92  ?  333  LEU A CA     1 
ATOM   5125  C C      . LEU A 1 333 ? 11.705  -6.798  -20.928 1.00 13.25  ?  333  LEU A C      1 
ATOM   5126  O O      . LEU A 1 333 ? 10.920  -6.304  -20.110 1.00 13.54  ?  333  LEU A O      1 
ATOM   5127  C CB     . LEU A 1 333 ? 12.252  -5.383  -22.942 1.00 11.96  ?  333  LEU A CB     1 
ATOM   5128  C CG     . LEU A 1 333 ? 13.220  -4.457  -23.682 1.00 14.36  ?  333  LEU A CG     1 
ATOM   5129  C CD1    . LEU A 1 333 ? 12.568  -3.779  -24.874 1.00 14.57  ?  333  LEU A CD1    1 
ATOM   5130  C CD2    . LEU A 1 333 ? 13.822  -3.418  -22.720 1.00 15.36  ?  333  LEU A CD2    1 
ATOM   5131  H H      . LEU A 1 333 ? 14.200  -6.842  -22.603 1.00 15.97  ?  333  LEU A H      1 
ATOM   5132  H HA     . LEU A 1 333 ? 12.920  -5.163  -21.030 1.00 14.30  ?  333  LEU A HA     1 
ATOM   5133  H HB2    . LEU A 1 333 ? 12.067  -6.134  -23.526 1.00 14.35  ?  333  LEU A HB2    1 
ATOM   5134  H HB3    . LEU A 1 333 ? 11.439  -4.880  -22.779 1.00 14.35  ?  333  LEU A HB3    1 
ATOM   5135  H HG     . LEU A 1 333 ? 13.943  -5.001  -24.033 1.00 17.23  ?  333  LEU A HG     1 
ATOM   5136  H HD11   . LEU A 1 333 ? 13.212  -3.186  -25.293 1.00 17.49  ?  333  LEU A HD11   1 
ATOM   5137  H HD12   . LEU A 1 333 ? 12.283  -4.457  -25.507 1.00 17.49  ?  333  LEU A HD12   1 
ATOM   5138  H HD13   . LEU A 1 333 ? 11.801  -3.270  -24.568 1.00 17.49  ?  333  LEU A HD13   1 
ATOM   5139  H HD21   . LEU A 1 333 ? 14.309  -2.756  -23.235 1.00 18.43  ?  333  LEU A HD21   1 
ATOM   5140  H HD22   . LEU A 1 333 ? 13.105  -2.992  -22.226 1.00 18.43  ?  333  LEU A HD22   1 
ATOM   5141  H HD23   . LEU A 1 333 ? 14.424  -3.868  -22.106 1.00 18.43  ?  333  LEU A HD23   1 
ATOM   5142  N N      . GLY A 1 334 ? 11.676  -8.087  -21.244 1.00 12.86  ?  334  GLY A N      1 
ATOM   5143  C CA     . GLY A 1 334 ? 10.792  -8.995  -20.527 1.00 13.37  ?  334  GLY A CA     1 
ATOM   5144  C C      . GLY A 1 334 ? 11.117  -9.070  -19.051 1.00 13.48  ?  334  GLY A C      1 
ATOM   5145  O O      . GLY A 1 334 ? 10.221  -9.006  -18.191 1.00 14.11  ?  334  GLY A O      1 
ATOM   5146  H H      . GLY A 1 334 ? 12.149  -8.459  -21.859 1.00 15.42  ?  334  GLY A H      1 
ATOM   5147  H HA2    . GLY A 1 334 ? 9.875   -8.692  -20.623 1.00 16.04  ?  334  GLY A HA2    1 
ATOM   5148  H HA3    . GLY A 1 334 ? 10.871  -9.885  -20.904 1.00 16.04  ?  334  GLY A HA3    1 
ATOM   5149  N N      . CYS A 1 335 ? 12.402  -9.165  -18.729 1.00 13.72  ?  335  CYS A N      1 
ATOM   5150  C CA     . CYS A 1 335 ? 12.802  -9.245  -17.331 1.00 14.97  ?  335  CYS A CA     1 
ATOM   5151  C C      . CYS A 1 335 ? 12.575  -7.929  -16.599 1.00 13.28  ?  335  CYS A C      1 
ATOM   5152  O O      . CYS A 1 335 ? 12.160  -7.927  -15.432 1.00 14.95  ?  335  CYS A O      1 
ATOM   5153  C CB     . CYS A 1 335 ? 14.250  -9.702  -17.239 1.00 14.29  ?  335  CYS A CB     1 
ATOM   5154  S SG     . CYS A 1 335 ? 14.502  -11.410 -17.807 1.00 14.57  ?  335  CYS A SG     1 
ATOM   5155  H H      . CYS A 1 335 ? 13.053  -9.186  -19.290 1.00 16.46  ?  335  CYS A H      1 
ATOM   5156  H HA     . CYS A 1 335 ? 12.256  -9.908  -16.882 1.00 17.96  ?  335  CYS A HA     1 
ATOM   5157  H HB2    . CYS A 1 335 ? 14.798  -9.120  -17.789 1.00 17.14  ?  335  CYS A HB2    1 
ATOM   5158  H HB3    . CYS A 1 335 ? 14.537  -9.650  -16.313 1.00 17.14  ?  335  CYS A HB3    1 
ATOM   5159  H HG     . CYS A 1 335 ? 14.183  -11.489 -18.961 1.00 17.48  ?  335  CYS A HG     1 
ATOM   5160  N N      . ALA A 1 336 ? 12.789  -6.799  -17.278 1.00 13.49  ?  336  ALA A N      1 
ATOM   5161  C CA     . ALA A 1 336 ? 12.477  -5.514  -16.674 1.00 13.55  ?  336  ALA A CA     1 
ATOM   5162  C C      . ALA A 1 336 ? 10.996  -5.391  -16.352 1.00 15.04  ?  336  ALA A C      1 
ATOM   5163  O O      . ALA A 1 336 ? 10.626  -4.901  -15.281 1.00 16.20  ?  336  ALA A O      1 
ATOM   5164  C CB     . ALA A 1 336 ? 12.946  -4.382  -17.579 1.00 14.32  ?  336  ALA A CB     1 
ATOM   5165  H H      . ALA A 1 336 ? 13.108  -6.753  -18.076 1.00 16.19  ?  336  ALA A H      1 
ATOM   5166  H HA     . ALA A 1 336 ? 12.958  -5.436  -15.836 1.00 16.26  ?  336  ALA A HA     1 
ATOM   5167  H HB1    . ALA A 1 336 ? 12.697  -3.534  -17.180 1.00 17.17  ?  336  ALA A HB1    1 
ATOM   5168  H HB2    . ALA A 1 336 ? 13.910  -4.433  -17.674 1.00 17.17  ?  336  ALA A HB2    1 
ATOM   5169  H HB3    . ALA A 1 336 ? 12.523  -4.476  -18.447 1.00 17.17  ?  336  ALA A HB3    1 
ATOM   5170  N N      . ALA A 1 337 ? 10.129  -5.899  -17.235 1.00 15.12  ?  337  ALA A N      1 
ATOM   5171  C CA     . ALA A 1 337 ? 8.696   -5.881  -16.944 1.00 13.42  ?  337  ALA A CA     1 
ATOM   5172  C C      . ALA A 1 337 ? 8.358   -6.823  -15.800 1.00 13.42  ?  337  ALA A C      1 
ATOM   5173  O O      . ALA A 1 337 ? 7.492   -6.521  -14.979 1.00 14.15  ?  337  ALA A O      1 
ATOM   5174  C CB     . ALA A 1 337 ? 7.912   -6.284  -18.190 1.00 15.36  ?  337  ALA A CB     1 
ATOM   5175  H H      . ALA A 1 337 ? 10.338  -6.251  -17.991 1.00 18.14  ?  337  ALA A H      1 
ATOM   5176  H HA     . ALA A 1 337 ? 8.439   -4.980  -16.690 1.00 16.10  ?  337  ALA A HA     1 
ATOM   5177  H HB1    . ALA A 1 337 ? 6.966   -6.297  -17.978 1.00 18.42  ?  337  ALA A HB1    1 
ATOM   5178  H HB2    . ALA A 1 337 ? 8.085   -5.640  -18.894 1.00 18.42  ?  337  ALA A HB2    1 
ATOM   5179  H HB3    . ALA A 1 337 ? 8.200   -7.167  -18.472 1.00 18.42  ?  337  ALA A HB3    1 
ATOM   5180  N N      . GLY A 1 338 ? 8.974   -8.003  -15.771 1.00 13.24  ?  338  GLY A N      1 
ATOM   5181  C CA     . GLY A 1 338 ? 8.768   -8.905  -14.654 1.00 13.35  ?  338  GLY A CA     1 
ATOM   5182  C C      . GLY A 1 338 ? 9.111   -8.271  -13.319 1.00 13.56  ?  338  GLY A C      1 
ATOM   5183  O O      . GLY A 1 338 ? 8.350   -8.381  -12.354 1.00 14.69  ?  338  GLY A O      1 
ATOM   5184  H H      . GLY A 1 338 ? 9.508   -8.300  -16.377 1.00 15.89  ?  338  GLY A H      1 
ATOM   5185  H HA2    . GLY A 1 338 ? 7.838   -9.179  -14.631 1.00 16.01  ?  338  GLY A HA2    1 
ATOM   5186  H HA3    . GLY A 1 338 ? 9.326   -9.690  -14.770 1.00 16.01  ?  338  GLY A HA3    1 
ATOM   5187  N N      . LEU A 1 339 ? 10.256  -7.595  -13.246 1.00 14.05  ?  339  LEU A N      1 
ATOM   5188  C CA     . LEU A 1 339 ? 10.643  -6.945  -11.998 1.00 14.90  ?  339  LEU A CA     1 
ATOM   5189  C C      . LEU A 1 339 ? 9.615   -5.900  -11.587 1.00 14.59  ?  339  LEU A C      1 
ATOM   5190  O O      . LEU A 1 339 ? 9.213   -5.833  -10.419 1.00 17.26  ?  339  LEU A O      1 
ATOM   5191  C CB     . LEU A 1 339 ? 12.012  -6.285  -12.143 1.00 16.54  ?  339  LEU A CB     1 
ATOM   5192  C CG     . LEU A 1 339 ? 13.203  -7.244  -12.153 1.00 17.21  ?  339  LEU A CG     1 
ATOM   5193  C CD1    . LEU A 1 339 ? 14.436  -6.506  -12.613 1.00 16.57  ?  339  LEU A CD1    1 
ATOM   5194  C CD2    . LEU A 1 339 ? 13.433  -7.898  -10.787 1.00 17.22  ?  339  LEU A CD2    1 
ATOM   5195  H H      . LEU A 1 339 ? 10.817  -7.498  -13.891 1.00 16.85  ?  339  LEU A H      1 
ATOM   5196  H HA     . LEU A 1 339 ? 10.698  -7.624  -11.307 1.00 17.88  ?  339  LEU A HA     1 
ATOM   5197  H HB2    . LEU A 1 339 ? 12.027  -5.795  -12.980 1.00 19.85  ?  339  LEU A HB2    1 
ATOM   5198  H HB3    . LEU A 1 339 ? 12.138  -5.675  -11.400 1.00 19.85  ?  339  LEU A HB3    1 
ATOM   5199  H HG     . LEU A 1 339 ? 13.016  -7.968  -12.771 1.00 20.65  ?  339  LEU A HG     1 
ATOM   5200  H HD11   . LEU A 1 339 ? 15.175  -7.130  -12.669 1.00 19.89  ?  339  LEU A HD11   1 
ATOM   5201  H HD12   . LEU A 1 339 ? 14.264  -6.117  -13.485 1.00 19.89  ?  339  LEU A HD12   1 
ATOM   5202  H HD13   . LEU A 1 339 ? 14.641  -5.806  -11.973 1.00 19.89  ?  339  LEU A HD13   1 
ATOM   5203  H HD21   . LEU A 1 339 ? 14.280  -8.371  -10.801 1.00 20.66  ?  339  LEU A HD21   1 
ATOM   5204  H HD22   . LEU A 1 339 ? 13.452  -7.208  -10.105 1.00 20.66  ?  339  LEU A HD22   1 
ATOM   5205  H HD23   . LEU A 1 339 ? 12.710  -8.520  -10.608 1.00 20.66  ?  339  LEU A HD23   1 
ATOM   5206  N N      . ALA A 1 340 ? 9.208   -5.035  -12.523 1.00 15.46  ?  340  ALA A N      1 
ATOM   5207  C CA     . ALA A 1 340 ? 8.237   -3.997  -12.180 1.00 15.17  ?  340  ALA A CA     1 
ATOM   5208  C C      . ALA A 1 340 ? 6.914   -4.604  -11.724 1.00 15.48  ?  340  ALA A C      1 
ATOM   5209  O O      . ALA A 1 340 ? 6.312   -4.147  -10.740 1.00 15.69  ?  340  ALA A O      1 
ATOM   5210  C CB     . ALA A 1 340 ? 8.047   -3.074  -13.380 1.00 14.27  ?  340  ALA A CB     1 
ATOM   5211  H H      . ALA A 1 340 ? 9.472   -5.028  -13.342 1.00 18.55  ?  340  ALA A H      1 
ATOM   5212  H HA     . ALA A 1 340 ? 8.574   -3.464  -11.443 1.00 18.20  ?  340  ALA A HA     1 
ATOM   5213  H HB1    . ALA A 1 340 ? 7.437   -2.360  -13.135 1.00 17.12  ?  340  ALA A HB1    1 
ATOM   5214  H HB2    . ALA A 1 340 ? 8.907   -2.702  -13.632 1.00 17.12  ?  340  ALA A HB2    1 
ATOM   5215  H HB3    . ALA A 1 340 ? 7.679   -3.585  -14.117 1.00 17.12  ?  340  ALA A HB3    1 
ATOM   5216  N N      . ASN A 1 341 ? 6.447   -5.635  -12.437 1.00 13.91  ?  341  ASN A N      1 
ATOM   5217  C CA     . ASN A 1 341 ? 5.222   -6.331  -12.084 1.00 13.95  ?  341  ASN A CA     1 
ATOM   5218  C C      . ASN A 1 341 ? 5.297   -6.906  -10.675 1.00 13.83  ?  341  ASN A C      1 
ATOM   5219  O O      . ASN A 1 341 ? 4.382   -6.706  -9.870  1.00 14.27  ?  341  ASN A O      1 
ATOM   5220  C CB     . ASN A 1 341 ? 4.984   -7.439  -13.131 1.00 14.72  ?  341  ASN A CB     1 
ATOM   5221  C CG     . ASN A 1 341 ? 3.771   -8.273  -12.824 1.00 14.17  ?  341  ASN A CG     1 
ATOM   5222  O OD1    . ASN A 1 341 ? 2.634   -7.788  -12.849 1.00 14.43  ?  341  ASN A OD1    1 
ATOM   5223  N ND2    . ASN A 1 341 ? 3.998   -9.546  -12.540 1.00 16.06  ?  341  ASN A ND2    1 
ATOM   5224  H H      . ASN A 1 341 ? 6.828   -5.951  -13.140 1.00 16.69  ?  341  ASN A H      1 
ATOM   5225  H HA     . ASN A 1 341 ? 4.472   -5.717  -12.095 1.00 16.73  ?  341  ASN A HA     1 
ATOM   5226  H HB2    . ASN A 1 341 ? 4.856   -7.031  -14.002 1.00 17.65  ?  341  ASN A HB2    1 
ATOM   5227  H HB3    . ASN A 1 341 ? 5.756   -8.027  -13.151 1.00 17.65  ?  341  ASN A HB3    1 
ATOM   5228  H HD21   . ASN A 1 341 ? 3.341   -10.070 -12.356 1.00 19.27  ?  341  ASN A HD21   1 
ATOM   5229  H HD22   . ASN A 1 341 ? 4.803   -9.849  -12.538 1.00 19.27  ?  341  ASN A HD22   1 
ATOM   5230  N N      . LEU A 1 342 ? 6.372   -7.641  -10.359 1.00 14.18  ?  342  LEU A N      1 
ATOM   5231  C CA     . LEU A 1 342 ? 6.476   -8.250  -9.031  1.00 14.44  ?  342  LEU A CA     1 
ATOM   5232  C C      . LEU A 1 342 ? 6.557   -7.179  -7.946  1.00 13.81  ?  342  LEU A C      1 
ATOM   5233  O O      . LEU A 1 342 ? 5.995   -7.341  -6.856  1.00 15.67  ?  342  LEU A O      1 
ATOM   5234  C CB     . LEU A 1 342 ? 7.662   -9.200  -8.952  1.00 16.88  ?  342  LEU A CB     1 
ATOM   5235  C CG     . LEU A 1 342 ? 7.586   -10.436 -9.848  1.00 17.33  ?  342  LEU A CG     1 
ATOM   5236  C CD1    . LEU A 1 342 ? 8.802   -11.331 -9.594  1.00 18.24  ?  342  LEU A CD1    1 
ATOM   5237  C CD2    . LEU A 1 342 ? 6.314   -11.245 -9.677  1.00 20.22  ?  342  LEU A CD2    1 
ATOM   5238  H H      . LEU A 1 342 ? 7.038   -7.798  -10.881 1.00 17.01  ?  342  LEU A H      1 
ATOM   5239  H HA     . LEU A 1 342 ? 5.680   -8.783  -8.875  1.00 17.32  ?  342  LEU A HA     1 
ATOM   5240  H HB2    . LEU A 1 342 ? 8.460   -8.710  -9.205  1.00 20.25  ?  342  LEU A HB2    1 
ATOM   5241  H HB3    . LEU A 1 342 ? 7.740   -9.512  -8.037  1.00 20.25  ?  342  LEU A HB3    1 
ATOM   5242  H HG     . LEU A 1 342 ? 7.579   -10.120 -10.764 1.00 20.79  ?  342  LEU A HG     1 
ATOM   5243  H HD11   . LEU A 1 342 ? 8.712   -12.142 -10.118 1.00 21.89  ?  342  LEU A HD11   1 
ATOM   5244  H HD12   . LEU A 1 342 ? 9.605   -10.854 -9.855  1.00 21.89  ?  342  LEU A HD12   1 
ATOM   5245  H HD13   . LEU A 1 342 ? 8.840   -11.551 -8.650  1.00 21.89  ?  342  LEU A HD13   1 
ATOM   5246  H HD21   . LEU A 1 342 ? 6.371   -12.042 -10.227 1.00 24.26  ?  342  LEU A HD21   1 
ATOM   5247  H HD22   . LEU A 1 342 ? 6.221   -11.494 -8.744  1.00 24.26  ?  342  LEU A HD22   1 
ATOM   5248  H HD23   . LEU A 1 342 ? 5.557   -10.706 -9.953  1.00 24.26  ?  342  LEU A HD23   1 
ATOM   5249  N N      . ALA A 1 343 ? 7.247   -6.071  -8.225  1.00 15.88  ?  343  ALA A N      1 
ATOM   5250  C CA     . ALA A 1 343 ? 7.353   -5.005  -7.230  1.00 17.09  ?  343  ALA A CA     1 
ATOM   5251  C C      . ALA A 1 343 ? 5.994   -4.398  -6.936  1.00 16.51  ?  343  ALA A C      1 
ATOM   5252  O O      . ALA A 1 343 ? 5.694   -4.047  -5.786  1.00 16.21  ?  343  ALA A O      1 
ATOM   5253  C CB     . ALA A 1 343 ? 8.317   -3.930  -7.716  1.00 16.77  ?  343  ALA A CB     1 
ATOM   5254  H H      . ALA A 1 343 ? 7.655   -5.913  -8.966  1.00 19.05  ?  343  ALA A H      1 
ATOM   5255  H HA     . ALA A 1 343 ? 7.706   -5.378  -6.407  1.00 20.50  ?  343  ALA A HA     1 
ATOM   5256  H HB1    . ALA A 1 343 ? 8.358   -3.220  -7.056  1.00 20.11  ?  343  ALA A HB1    1 
ATOM   5257  H HB2    . ALA A 1 343 ? 9.196   -4.323  -7.834  1.00 20.11  ?  343  ALA A HB2    1 
ATOM   5258  H HB3    . ALA A 1 343 ? 7.997   -3.577  -8.561  1.00 20.11  ?  343  ALA A HB3    1 
ATOM   5259  N N      . ILE A 1 344 ? 5.153   -4.257  -7.971  1.00 16.41  ?  344  ILE A N      1 
ATOM   5260  C CA     . ILE A 1 344 ? 3.796   -3.747  -7.779  1.00 15.37  ?  344  ILE A CA     1 
ATOM   5261  C C      . ILE A 1 344 ? 2.954   -4.717  -6.956  1.00 14.65  ?  344  ILE A C      1 
ATOM   5262  O O      . ILE A 1 344 ? 2.203   -4.310  -6.067  1.00 15.66  ?  344  ILE A O      1 
ATOM   5263  C CB     . ILE A 1 344 ? 3.162   -3.426  -9.147  1.00 15.26  ?  344  ILE A CB     1 
ATOM   5264  C CG1    . ILE A 1 344 ? 3.865   -2.199  -9.751  1.00 17.65  ?  344  ILE A CG1    1 
ATOM   5265  C CG2    . ILE A 1 344 ? 1.654   -3.234  -9.018  1.00 15.69  ?  344  ILE A CG2    1 
ATOM   5266  C CD1    . ILE A 1 344 ? 3.598   -2.006  -11.241 1.00 18.13  ?  344  ILE A CD1    1 
ATOM   5267  H H      . ILE A 1 344 ? 5.343   -4.449  -8.788  1.00 19.68  ?  344  ILE A H      1 
ATOM   5268  H HA     . ILE A 1 344 ? 3.843   -2.922  -7.270  1.00 18.44  ?  344  ILE A HA     1 
ATOM   5269  H HB     . ILE A 1 344 ? 3.289   -4.175  -9.750  1.00 18.31  ?  344  ILE A HB     1 
ATOM   5270  H HG12   . ILE A 1 344 ? 3.555   -1.404  -9.290  1.00 21.18  ?  344  ILE A HG12   1 
ATOM   5271  H HG13   . ILE A 1 344 ? 4.822   -2.299  -9.633  1.00 21.18  ?  344  ILE A HG13   1 
ATOM   5272  H HG21   . ILE A 1 344 ? 1.331   -2.739  -9.787  1.00 18.83  ?  344  ILE A HG21   1 
ATOM   5273  H HG22   . ILE A 1 344 ? 1.226   -4.104  -8.981  1.00 18.83  ?  344  ILE A HG22   1 
ATOM   5274  H HG23   . ILE A 1 344 ? 1.467   -2.739  -8.204  1.00 18.83  ?  344  ILE A HG23   1 
ATOM   5275  H HD11   . ILE A 1 344 ? 4.098   -1.236  -11.554 1.00 21.75  ?  344  ILE A HD11   1 
ATOM   5276  H HD12   . ILE A 1 344 ? 3.881   -2.801  -11.718 1.00 21.75  ?  344  ILE A HD12   1 
ATOM   5277  H HD13   . ILE A 1 344 ? 2.648   -1.860  -11.375 1.00 21.75  ?  344  ILE A HD13   1 
ATOM   5278  N N      . ILE A 1 345 ? 3.041   -6.008  -7.252  1.00 15.14  ?  345  ILE A N      1 
ATOM   5279  C CA     . ILE A 1 345 ? 2.277   -6.993  -6.493  1.00 15.39  ?  345  ILE A CA     1 
ATOM   5280  C C      . ILE A 1 345 ? 2.647   -6.911  -5.030  1.00 17.18  ?  345  ILE A C      1 
ATOM   5281  O O      . ILE A 1 345 ? 1.781   -6.934  -4.150  1.00 17.76  ?  345  ILE A O      1 
ATOM   5282  C CB     . ILE A 1 345 ? 2.519   -8.398  -7.074  1.00 14.08  ?  345  ILE A CB     1 
ATOM   5283  C CG1    . ILE A 1 345 ? 1.859   -8.510  -8.449  1.00 15.01  ?  345  ILE A CG1    1 
ATOM   5284  C CG2    . ILE A 1 345 ? 2.030   -9.480  -6.122  1.00 15.84  ?  345  ILE A CG2    1 
ATOM   5285  C CD1    . ILE A 1 345 ? 2.376   -9.656  -9.249  1.00 16.04  ?  345  ILE A CD1    1 
ATOM   5286  H H      . ILE A 1 345 ? 3.527   -6.339  -7.880  1.00 18.17  ?  345  ILE A H      1 
ATOM   5287  H HA     . ILE A 1 345 ? 1.330   -6.799  -6.570  1.00 18.46  ?  345  ILE A HA     1 
ATOM   5288  H HB     . ILE A 1 345 ? 3.474   -8.530  -7.183  1.00 16.89  ?  345  ILE A HB     1 
ATOM   5289  H HG12   . ILE A 1 345 ? 0.904   -8.633  -8.331  1.00 18.01  ?  345  ILE A HG12   1 
ATOM   5290  H HG13   . ILE A 1 345 ? 2.030   -7.696  -8.948  1.00 18.01  ?  345  ILE A HG13   1 
ATOM   5291  H HG21   . ILE A 1 345 ? 1.994   -10.326 -6.596  1.00 19.00  ?  345  ILE A HG21   1 
ATOM   5292  H HG22   . ILE A 1 345 ? 2.647   -9.546  -5.376  1.00 19.00  ?  345  ILE A HG22   1 
ATOM   5293  H HG23   . ILE A 1 345 ? 1.146   -9.243  -5.801  1.00 19.00  ?  345  ILE A HG23   1 
ATOM   5294  H HD11   . ILE A 1 345 ? 2.012   -9.604  -10.147 1.00 19.25  ?  345  ILE A HD11   1 
ATOM   5295  H HD12   . ILE A 1 345 ? 3.344   -9.608  -9.281  1.00 19.25  ?  345  ILE A HD12   1 
ATOM   5296  H HD13   . ILE A 1 345 ? 2.099   -10.485 -8.828  1.00 19.25  ?  345  ILE A HD13   1 
ATOM   5297  N N      . GLU A 1 346 ? 3.943   -6.790  -4.747  1.00 19.49  ?  346  GLU A N      1 
ATOM   5298  C CA     . GLU A 1 346 ? 4.401   -6.736  -3.366  1.00 21.34  ?  346  GLU A CA     1 
ATOM   5299  C C      . GLU A 1 346 ? 3.966   -5.437  -2.709  1.00 19.94  ?  346  GLU A C      1 
ATOM   5300  O O      . GLU A 1 346 ? 3.451   -5.441  -1.588  1.00 22.46  ?  346  GLU A O      1 
ATOM   5301  C CB     . GLU A 1 346 ? 5.926   -6.873  -3.316  1.00 27.39  ?  346  GLU A CB     1 
ATOM   5302  C CG     . GLU A 1 346 ? 6.535   -6.775  -1.910  1.00 37.00  ?  346  GLU A CG     1 
ATOM   5303  C CD     . GLU A 1 346 ? 6.067   -7.873  -0.970  1.00 48.98  ?  346  GLU A CD     1 
ATOM   5304  O OE1    . GLU A 1 346 ? 5.566   -8.903  -1.470  1.00 54.00  ?  346  GLU A OE1    1 
ATOM   5305  O OE2    . GLU A 1 346 ? 6.199   -7.703  0.263   1.00 54.68  -1 346  GLU A OE2    1 
ATOM   5306  H H      . GLU A 1 346 ? 4.572   -6.738  -5.331  1.00 23.38  ?  346  GLU A H      1 
ATOM   5307  H HA     . GLU A 1 346 ? 4.014   -7.476  -2.874  1.00 25.61  ?  346  GLU A HA     1 
ATOM   5308  H HB2    . GLU A 1 346 ? 6.170   -7.739  -3.679  1.00 32.87  ?  346  GLU A HB2    1 
ATOM   5309  H HB3    . GLU A 1 346 ? 6.317   -6.166  -3.853  1.00 32.87  ?  346  GLU A HB3    1 
ATOM   5310  H HG2    . GLU A 1 346 ? 7.500   -6.837  -1.982  1.00 44.39  ?  346  GLU A HG2    1 
ATOM   5311  H HG3    . GLU A 1 346 ? 6.285   -5.923  -1.520  1.00 44.39  ?  346  GLU A HG3    1 
ATOM   5312  N N      . ARG A 1 347 ? 4.158   -4.311  -3.403  1.00 18.70  ?  347  ARG A N      1 
ATOM   5313  C CA     . ARG A 1 347 ? 3.919   -3.011  -2.785  1.00 19.83  ?  347  ARG A CA     1 
ATOM   5314  C C      . ARG A 1 347 ? 2.449   -2.800  -2.454  1.00 19.25  ?  347  ARG A C      1 
ATOM   5315  O O      . ARG A 1 347 ? 2.113   -2.237  -1.397  1.00 22.38  ?  347  ARG A O      1 
ATOM   5316  C CB     . ARG A 1 347 ? 4.369   -1.919  -3.749  1.00 22.29  ?  347  ARG A CB     1 
ATOM   5317  C CG     . ARG A 1 347 ? 4.239   -0.524  -3.204  1.00 25.80  ?  347  ARG A CG     1 
ATOM   5318  C CD     . ARG A 1 347 ? 4.857   0.492   -4.148  1.00 28.32  ?  347  ARG A CD     1 
ATOM   5319  N NE     . ARG A 1 347 ? 4.038   0.729   -5.331  1.00 32.05  ?  347  ARG A NE     1 
ATOM   5320  C CZ     . ARG A 1 347 ? 4.448   0.612   -6.601  1.00 34.75  ?  347  ARG A CZ     1 
ATOM   5321  N NH1    . ARG A 1 347 ? 5.692   0.254   -6.905  1.00 35.28  ?  347  ARG A NH1    1 
ATOM   5322  N NH2    . ARG A 1 347 ? 3.597   0.871   -7.575  1.00 37.23  ?  347  ARG A NH2    1 
ATOM   5323  H H      . ARG A 1 347 ? 4.423   -4.274  -4.220  1.00 22.44  ?  347  ARG A H      1 
ATOM   5324  H HA     . ARG A 1 347 ? 4.428   -2.962  -1.961  1.00 23.79  ?  347  ARG A HA     1 
ATOM   5325  H HB2    . ARG A 1 347 ? 5.303   -2.063  -3.967  1.00 26.75  ?  347  ARG A HB2    1 
ATOM   5326  H HB3    . ARG A 1 347 ? 3.829   -1.972  -4.553  1.00 26.75  ?  347  ARG A HB3    1 
ATOM   5327  H HG2    . ARG A 1 347 ? 3.300   -0.307  -3.093  1.00 30.96  ?  347  ARG A HG2    1 
ATOM   5328  H HG3    . ARG A 1 347 ? 4.696   -0.467  -2.351  1.00 30.96  ?  347  ARG A HG3    1 
ATOM   5329  H HD2    . ARG A 1 347 ? 4.962   1.336   -3.680  1.00 33.98  ?  347  ARG A HD2    1 
ATOM   5330  H HD3    . ARG A 1 347 ? 5.722   0.166   -4.442  1.00 33.98  ?  347  ARG A HD3    1 
ATOM   5331  H HE     . ARG A 1 347 ? 3.221   0.965   -5.202  1.00 38.46  ?  347  ARG A HE     1 
ATOM   5332  H HH11   . ARG A 1 347 ? 6.258   0.090   -6.279  1.00 42.33  ?  347  ARG A HH11   1 
ATOM   5333  H HH12   . ARG A 1 347 ? 5.931   0.185   -7.729  1.00 42.33  ?  347  ARG A HH12   1 
ATOM   5334  H HH21   . ARG A 1 347 ? 2.792   1.112   -7.390  1.00 44.67  ?  347  ARG A HH21   1 
ATOM   5335  H HH22   . ARG A 1 347 ? 3.846   0.800   -8.395  1.00 44.67  ?  347  ARG A HH22   1 
ATOM   5336  N N      . GLU A 1 348 ? 1.562   -3.239  -3.351  1.00 19.33  ?  348  GLU A N      1 
ATOM   5337  C CA     . GLU A 1 348 ? 0.125   -3.066  -3.224  1.00 18.64  ?  348  GLU A CA     1 
ATOM   5338  C C      . GLU A 1 348 ? -0.552  -4.210  -2.490  1.00 18.92  ?  348  GLU A C      1 
ATOM   5339  O O      . GLU A 1 348 ? -1.770  -4.177  -2.317  1.00 20.83  ?  348  GLU A O      1 
ATOM   5340  C CB     . GLU A 1 348 ? -0.496  -2.890  -4.620  1.00 18.94  ?  348  GLU A CB     1 
ATOM   5341  C CG     . GLU A 1 348 ? -0.010  -1.641  -5.328  1.00 18.96  ?  348  GLU A CG     1 
ATOM   5342  C CD     . GLU A 1 348 ? -0.704  -1.339  -6.648  1.00 20.79  ?  348  GLU A CD     1 
ATOM   5343  O OE1    . GLU A 1 348 ? -1.604  -2.114  -7.076  1.00 19.91  ?  348  GLU A OE1    1 
ATOM   5344  O OE2    . GLU A 1 348 ? -0.324  -0.316  -7.271  1.00 22.06  -1 348  GLU A OE2    1 
ATOM   5345  H H      . GLU A 1 348 ? 1.784   -3.657  -4.069  1.00 23.20  ?  348  GLU A H      1 
ATOM   5346  H HA     . GLU A 1 348 ? -0.053  -2.260  -2.715  1.00 22.37  ?  348  GLU A HA     1 
ATOM   5347  H HB2    . GLU A 1 348 ? -0.263  -3.655  -5.168  1.00 22.73  ?  348  GLU A HB2    1 
ATOM   5348  H HB3    . GLU A 1 348 ? -1.460  -2.828  -4.530  1.00 22.73  ?  348  GLU A HB3    1 
ATOM   5349  H HG2    . GLU A 1 348 ? -0.155  -0.880  -4.743  1.00 22.74  ?  348  GLU A HG2    1 
ATOM   5350  H HG3    . GLU A 1 348 ? 0.937   -1.742  -5.513  1.00 22.74  ?  348  GLU A HG3    1 
ATOM   5351  N N      . GLY A 1 349 ? 0.202   -5.207  -2.039  1.00 19.06  ?  349  GLY A N      1 
ATOM   5352  C CA     . GLY A 1 349 ? -0.389  -6.333  -1.325  1.00 19.59  ?  349  GLY A CA     1 
ATOM   5353  C C      . GLY A 1 349 ? -1.429  -7.080  -2.131  1.00 17.19  ?  349  GLY A C      1 
ATOM   5354  O O      . GLY A 1 349 ? -2.485  -7.447  -1.600  1.00 16.00  ?  349  GLY A O      1 
ATOM   5355  H H      . GLY A 1 349 ? 1.056   -5.258  -2.131  1.00 22.87  ?  349  GLY A H      1 
ATOM   5356  H HA2    . GLY A 1 349 ? 0.312   -6.958  -1.085  1.00 23.50  ?  349  GLY A HA2    1 
ATOM   5357  H HA3    . GLY A 1 349 ? -0.813  -6.006  -0.516  1.00 23.50  ?  349  GLY A HA3    1 
ATOM   5358  N N      . LEU A 1 350 ? -1.152  -7.331  -3.408  1.00 17.88  ?  350  LEU A N      1 
ATOM   5359  C CA     . LEU A 1 350 ? -2.177  -7.914  -4.263  1.00 17.31  ?  350  LEU A CA     1 
ATOM   5360  C C      . LEU A 1 350 ? -2.422  -9.390  -3.960  1.00 15.99  ?  350  LEU A C      1 
ATOM   5361  O O      . LEU A 1 350 ? -3.519  -9.900  -4.239  1.00 14.91  ?  350  LEU A O      1 
ATOM   5362  C CB     . LEU A 1 350 ? -1.797  -7.707  -5.732  1.00 17.04  ?  350  LEU A CB     1 
ATOM   5363  C CG     . LEU A 1 350 ? -1.700  -6.241  -6.163  1.00 17.11  ?  350  LEU A CG     1 
ATOM   5364  C CD1    . LEU A 1 350 ? -1.506  -6.161  -7.654  1.00 19.19  ?  350  LEU A CD1    1 
ATOM   5365  C CD2    . LEU A 1 350 ? -2.941  -5.464  -5.771  1.00 17.64  ?  350  LEU A CD2    1 
ATOM   5366  H H      . LEU A 1 350 ? -0.399  -7.179  -3.794  1.00 21.45  ?  350  LEU A H      1 
ATOM   5367  H HA     . LEU A 1 350 ? -3.017  -7.456  -4.100  1.00 20.77  ?  350  LEU A HA     1 
ATOM   5368  H HB2    . LEU A 1 350 ? -0.932  -8.117  -5.887  1.00 20.44  ?  350  LEU A HB2    1 
ATOM   5369  H HB3    . LEU A 1 350 ? -2.470  -8.132  -6.287  1.00 20.44  ?  350  LEU A HB3    1 
ATOM   5370  H HG     . LEU A 1 350 ? -0.942  -5.837  -5.713  1.00 20.53  ?  350  LEU A HG     1 
ATOM   5371  H HD11   . LEU A 1 350 ? -1.467  -5.228  -7.918  1.00 23.03  ?  350  LEU A HD11   1 
ATOM   5372  H HD12   . LEU A 1 350 ? -0.677  -6.606  -7.889  1.00 23.03  ?  350  LEU A HD12   1 
ATOM   5373  H HD13   . LEU A 1 350 ? -2.252  -6.598  -8.093  1.00 23.03  ?  350  LEU A HD13   1 
ATOM   5374  H HD21   . LEU A 1 350 ? -2.925  -4.600  -6.212  1.00 21.17  ?  350  LEU A HD21   1 
ATOM   5375  H HD22   . LEU A 1 350 ? -3.726  -5.962  -6.047  1.00 21.17  ?  350  LEU A HD22   1 
ATOM   5376  H HD23   . LEU A 1 350 ? -2.947  -5.343  -4.809  1.00 21.17  ?  350  LEU A HD23   1 
ATOM   5377  N N      . THR A 1 351 ? -1.431  -10.102 -3.412  1.00 15.93  ?  351  THR A N      1 
ATOM   5378  C CA     . THR A 1 351 ? -1.677  -11.490 -3.029  1.00 15.60  ?  351  THR A CA     1 
ATOM   5379  C C      . THR A 1 351 ? -2.690  -11.559 -1.896  1.00 15.56  ?  351  THR A C      1 
ATOM   5380  O O      . THR A 1 351 ? -3.596  -12.403 -1.904  1.00 16.27  ?  351  THR A O      1 
ATOM   5381  C CB     . THR A 1 351 ? -0.357  -12.145 -2.627  1.00 17.76  ?  351  THR A CB     1 
ATOM   5382  O OG1    . THR A 1 351 ? 0.572   -12.018 -3.713  1.00 20.87  ?  351  THR A OG1    1 
ATOM   5383  C CG2    . THR A 1 351 ? -0.524  -13.611 -2.322  1.00 18.64  ?  351  THR A CG2    1 
ATOM   5384  H H      . THR A 1 351 ? -0.635  -9.814  -3.257  1.00 19.11  ?  351  THR A H      1 
ATOM   5385  H HA     . THR A 1 351 ? -2.038  -11.984 -3.783  1.00 18.72  ?  351  THR A HA     1 
ATOM   5386  H HB     . THR A 1 351 ? -0.026  -11.708 -1.827  1.00 21.31  ?  351  THR A HB     1 
ATOM   5387  H HG1    . THR A 1 351 ? 1.280   -12.432 -3.535  1.00 25.05  ?  351  THR A HG1    1 
ATOM   5388  H HG21   . THR A 1 351 ? 0.346   -14.028 -2.216  1.00 22.37  ?  351  THR A HG21   1 
ATOM   5389  H HG22   . THR A 1 351 ? -1.029  -13.723 -1.502  1.00 22.37  ?  351  THR A HG22   1 
ATOM   5390  H HG23   . THR A 1 351 ? -0.997  -14.049 -3.046  1.00 22.37  ?  351  THR A HG23   1 
ATOM   5391  N N      . ALA A 1 352 ? -2.550  -10.674 -0.911  1.00 16.75  ?  352  ALA A N      1 
ATOM   5392  C CA     . ALA A 1 352 ? -3.548  -10.591 0.152   1.00 16.55  ?  352  ALA A CA     1 
ATOM   5393  C C      . ALA A 1 352 ? -4.893  -10.111 -0.381  1.00 17.89  ?  352  ALA A C      1 
ATOM   5394  O O      . ALA A 1 352 ? -5.941  -10.570 0.077   1.00 18.33  ?  352  ALA A O      1 
ATOM   5395  C CB     . ALA A 1 352 ? -3.048  -9.642  1.234   1.00 18.47  ?  352  ALA A CB     1 
ATOM   5396  H H      . ALA A 1 352 ? -1.898  -10.118 -0.834  1.00 20.10  ?  352  ALA A H      1 
ATOM   5397  H HA     . ALA A 1 352 ? -3.674  -11.472 0.536   1.00 19.85  ?  352  ALA A HA     1 
ATOM   5398  H HB1    . ALA A 1 352 ? -3.703  -9.606  1.949   1.00 22.16  ?  352  ALA A HB1    1 
ATOM   5399  H HB2    . ALA A 1 352 ? -2.202  -9.971  1.577   1.00 22.16  ?  352  ALA A HB2    1 
ATOM   5400  H HB3    . ALA A 1 352 ? -2.929  -8.759  0.850   1.00 22.16  ?  352  ALA A HB3    1 
ATOM   5401  N N      . ASN A 1 353 ? -4.897  -9.192  -1.349  1.00 16.55  ?  353  ASN A N      1 
ATOM   5402  C CA     . ASN A 1 353 ? -6.183  -8.808  -1.929  1.00 16.49  ?  353  ASN A CA     1 
ATOM   5403  C C      . ASN A 1 353 ? -6.836  -9.988  -2.637  1.00 17.15  ?  353  ASN A C      1 
ATOM   5404  O O      . ASN A 1 353 ? -8.054  -10.179 -2.553  1.00 18.04  ?  353  ASN A O      1 
ATOM   5405  C CB     . ASN A 1 353 ? -6.073  -7.615  -2.873  1.00 17.61  ?  353  ASN A CB     1 
ATOM   5406  C CG     . ASN A 1 353 ? -7.438  -7.091  -3.253  1.00 17.95  ?  353  ASN A CG     1 
ATOM   5407  O OD1    . ASN A 1 353 ? -8.235  -6.734  -2.369  1.00 19.83  ?  353  ASN A OD1    1 
ATOM   5408  N ND2    . ASN A 1 353 ? -7.741  -7.061  -4.549  1.00 18.62  ?  353  ASN A ND2    1 
ATOM   5409  H H      . ASN A 1 353 ? -4.206  -8.796  -1.674  1.00 19.86  ?  353  ASN A H      1 
ATOM   5410  H HA     . ASN A 1 353 ? -6.750  -8.519  -1.197  1.00 19.79  ?  353  ASN A HA     1 
ATOM   5411  H HB2    . ASN A 1 353 ? -5.582  -6.903  -2.435  1.00 21.13  ?  353  ASN A HB2    1 
ATOM   5412  H HB3    . ASN A 1 353 ? -5.612  -7.887  -3.682  1.00 21.13  ?  353  ASN A HB3    1 
ATOM   5413  H HD21   . ASN A 1 353 ? -8.509  -6.769  -4.805  1.00 22.34  ?  353  ASN A HD21   1 
ATOM   5414  H HD22   . ASN A 1 353 ? -7.170  -7.333  -5.131  1.00 22.34  ?  353  ASN A HD22   1 
ATOM   5415  N N      . ALA A 1 354 ? -6.037  -10.798 -3.345  1.00 16.12  ?  354  ALA A N      1 
ATOM   5416  C CA     . ALA A 1 354 ? -6.581  -11.981 -4.006  1.00 15.95  ?  354  ALA A CA     1 
ATOM   5417  C C      . ALA A 1 354 ? -7.158  -12.947 -2.987  1.00 16.51  ?  354  ALA A C      1 
ATOM   5418  O O      . ALA A 1 354 ? -8.198  -13.564 -3.231  1.00 16.29  ?  354  ALA A O      1 
ATOM   5419  C CB     . ALA A 1 354 ? -5.489  -12.643 -4.847  1.00 16.69  ?  354  ALA A CB     1 
ATOM   5420  H H      . ALA A 1 354 ? -5.191  -10.687 -3.454  1.00 19.34  ?  354  ALA A H      1 
ATOM   5421  H HA     . ALA A 1 354 ? -7.298  -11.722 -4.605  1.00 19.14  ?  354  ALA A HA     1 
ATOM   5422  H HB1    . ALA A 1 354 ? -5.862  -13.418 -5.295  1.00 20.03  ?  354  ALA A HB1    1 
ATOM   5423  H HB2    . ALA A 1 354 ? -5.164  -12.005 -5.502  1.00 20.03  ?  354  ALA A HB2    1 
ATOM   5424  H HB3    . ALA A 1 354 ? -4.763  -12.916 -4.264  1.00 20.03  ?  354  ALA A HB3    1 
ATOM   5425  N N      . ALA A 1 355 ? -6.504  -13.082 -1.831  1.00 16.30  ?  355  ALA A N      1 
ATOM   5426  C CA     . ALA A 1 355 ? -7.045  -13.954 -0.790  1.00 16.68  ?  355  ALA A CA     1 
ATOM   5427  C C      . ALA A 1 355 ? -8.339  -13.387 -0.215  1.00 16.98  ?  355  ALA A C      1 
ATOM   5428  O O      . ALA A 1 355 ? -9.334  -14.108 -0.078  1.00 16.99  ?  355  ALA A O      1 
ATOM   5429  C CB     . ALA A 1 355 ? -6.013  -14.144 0.321   1.00 16.84  ?  355  ALA A CB     1 
ATOM   5430  H H      . ALA A 1 355 ? -5.765  -12.692 -1.629  1.00 19.56  ?  355  ALA A H      1 
ATOM   5431  H HA     . ALA A 1 355 ? -7.238  -14.821 -1.181  1.00 20.01  ?  355  ALA A HA     1 
ATOM   5432  H HB1    . ALA A 1 355 ? -6.383  -14.731 0.999   1.00 20.21  ?  355  ALA A HB1    1 
ATOM   5433  H HB2    . ALA A 1 355 ? -5.212  -14.540 -0.056  1.00 20.21  ?  355  ALA A HB2    1 
ATOM   5434  H HB3    . ALA A 1 355 ? -5.803  -13.280 0.709   1.00 20.21  ?  355  ALA A HB3    1 
ATOM   5435  N N      . GLU A 1 356 ? -8.345  -12.092 0.127   1.00 17.01  ?  356  GLU A N      1 
ATOM   5436  C CA     . GLU A 1 356 ? -9.462  -11.528 0.878   1.00 18.65  ?  356  GLU A CA     1 
ATOM   5437  C C      . GLU A 1 356 ? -10.639 -11.188 -0.028  1.00 16.22  ?  356  GLU A C      1 
ATOM   5438  O O      . GLU A 1 356 ? -11.781 -11.600 0.229   1.00 17.81  ?  356  GLU A O      1 
ATOM   5439  C CB     . GLU A 1 356 ? -8.982  -10.285 1.643   1.00 24.89  ?  356  GLU A CB     1 
ATOM   5440  C CG     . GLU A 1 356 ? -7.917  -10.600 2.684   1.00 31.23  ?  356  GLU A CG     1 
ATOM   5441  C CD     . GLU A 1 356 ? -7.197  -9.366  3.222   1.00 40.34  ?  356  GLU A CD     1 
ATOM   5442  O OE1    . GLU A 1 356 ? -7.661  -8.230  2.965   1.00 43.96  ?  356  GLU A OE1    1 
ATOM   5443  O OE2    . GLU A 1 356 ? -6.160  -9.534  3.907   1.00 42.53  -1 356  GLU A OE2    1 
ATOM   5444  H H      . GLU A 1 356 ? -7.723  -11.529 -0.062  1.00 20.40  ?  356  GLU A H      1 
ATOM   5445  H HA     . GLU A 1 356 ? -9.776  -12.183 1.521   1.00 22.37  ?  356  GLU A HA     1 
ATOM   5446  H HB2    . GLU A 1 356 ? -8.604  -9.654  1.011   1.00 29.86  ?  356  GLU A HB2    1 
ATOM   5447  H HB3    . GLU A 1 356 ? -9.738  -9.885  2.100   1.00 29.86  ?  356  GLU A HB3    1 
ATOM   5448  H HG2    . GLU A 1 356 ? -8.338  -11.047 3.436   1.00 37.48  ?  356  GLU A HG2    1 
ATOM   5449  H HG3    . GLU A 1 356 ? -7.251  -11.181 2.284   1.00 37.48  ?  356  GLU A HG3    1 
ATOM   5450  N N      . THR A 1 357 ? -10.390 -10.422 -1.089  1.00 16.19  ?  357  THR A N      1 
ATOM   5451  C CA     . THR A 1 357 ? -11.449 -10.133 -2.048  1.00 16.42  ?  357  THR A CA     1 
ATOM   5452  C C      . THR A 1 357 ? -11.828 -11.369 -2.849  1.00 16.79  ?  357  THR A C      1 
ATOM   5453  O O      . THR A 1 357 ? -12.990 -11.511 -3.253  1.00 17.50  ?  357  THR A O      1 
ATOM   5454  C CB     . THR A 1 357 ? -11.014 -8.943  -2.907  1.00 17.06  ?  357  THR A CB     1 
ATOM   5455  O OG1    . THR A 1 357 ? -10.756 -7.824  -2.027  1.00 19.69  ?  357  THR A OG1    1 
ATOM   5456  C CG2    . THR A 1 357 ? -12.096 -8.573  -3.912  1.00 17.94  ?  357  THR A CG2    1 
ATOM   5457  H H      . THR A 1 357 ? -9.630  -10.064 -1.274  1.00 19.43  ?  357  THR A H      1 
ATOM   5458  H HA     . THR A 1 357 ? -12.266 -9.864  -1.600  1.00 19.70  ?  357  THR A HA     1 
ATOM   5459  H HB     . THR A 1 357 ? -10.216 -9.165  -3.412  1.00 20.47  ?  357  THR A HB     1 
ATOM   5460  H HG1    . THR A 1 357 ? -10.543 -7.148  -2.478  1.00 23.63  ?  357  THR A HG1    1 
ATOM   5461  H HG21   . THR A 1 357 ? -11.886 -7.721  -4.327  1.00 21.52  ?  357  THR A HG21   1 
ATOM   5462  H HG22   . THR A 1 357 ? -12.155 -9.252  -4.602  1.00 21.52  ?  357  THR A HG22   1 
ATOM   5463  H HG23   . THR A 1 357 ? -12.954 -8.502  -3.466  1.00 21.52  ?  357  THR A HG23   1 
ATOM   5464  N N      . GLY A 1 358 ? -10.881 -12.288 -3.061  1.00 15.44  ?  358  GLY A N      1 
ATOM   5465  C CA     . GLY A 1 358 ? -11.241 -13.552 -3.672  1.00 15.30  ?  358  GLY A CA     1 
ATOM   5466  C C      . GLY A 1 358 ? -12.214 -14.344 -2.828  1.00 16.01  ?  358  GLY A C      1 
ATOM   5467  O O      . GLY A 1 358 ? -13.172 -14.919 -3.345  1.00 15.89  ?  358  GLY A O      1 
ATOM   5468  H H      . GLY A 1 358 ? -10.048 -12.202 -2.864  1.00 18.53  ?  358  GLY A H      1 
ATOM   5469  H HA2    . GLY A 1 358 ? -11.650 -13.386 -4.536  1.00 18.35  ?  358  GLY A HA2    1 
ATOM   5470  H HA3    . GLY A 1 358 ? -10.441 -14.086 -3.799  1.00 18.35  ?  358  GLY A HA3    1 
ATOM   5471  N N      . ALA A 1 359 ? -11.978 -14.399 -1.514  1.00 16.41  ?  359  ALA A N      1 
ATOM   5472  C CA     . ALA A 1 359 ? -12.960 -15.033 -0.637  1.00 14.95  ?  359  ALA A CA     1 
ATOM   5473  C C      . ALA A 1 359 ? -14.322 -14.369 -0.763  1.00 16.73  ?  359  ALA A C      1 
ATOM   5474  O O      . ALA A 1 359 ? -15.352 -15.051 -0.743  1.00 17.40  ?  359  ALA A O      1 
ATOM   5475  C CB     . ALA A 1 359 ? -12.481 -14.990 0.813   1.00 16.81  ?  359  ALA A CB     1 
ATOM   5476  H H      . ALA A 1 359 ? -11.281 -14.088 -1.118  1.00 19.68  ?  359  ALA A H      1 
ATOM   5477  H HA     . ALA A 1 359 ? -13.051 -15.963 -0.896  1.00 17.93  ?  359  ALA A HA     1 
ATOM   5478  H HB1    . ALA A 1 359 ? -13.154 -15.398 1.381   1.00 20.17  ?  359  ALA A HB1    1 
ATOM   5479  H HB2    . ALA A 1 359 ? -11.647 -15.480 0.885   1.00 20.17  ?  359  ALA A HB2    1 
ATOM   5480  H HB3    . ALA A 1 359 ? -12.345 -14.066 1.074   1.00 20.17  ?  359  ALA A HB3    1 
ATOM   5481  N N      . TYR A 1 360 ? -14.343 -13.029 -0.841  1.00 15.40  ?  360  TYR A N      1 
ATOM   5482  C CA     . TYR A 1 360 ? -15.589 -12.296 -1.056  1.00 17.28  ?  360  TYR A CA     1 
ATOM   5483  C C      . TYR A 1 360 ? -16.230 -12.664 -2.392  1.00 15.68  ?  360  TYR A C      1 
ATOM   5484  O O      . TYR A 1 360 ? -17.458 -12.850 -2.473  1.00 16.39  ?  360  TYR A O      1 
ATOM   5485  C CB     . TYR A 1 360 ? -15.311 -10.792 -0.969  1.00 17.83  ?  360  TYR A CB     1 
ATOM   5486  C CG     . TYR A 1 360 ? -16.556 -9.971  -1.105  1.00 15.63  ?  360  TYR A CG     1 
ATOM   5487  C CD1    . TYR A 1 360 ? -17.513 -9.974  -0.110  1.00 16.43  ?  360  TYR A CD1    1 
ATOM   5488  C CD2    . TYR A 1 360 ? -16.797 -9.196  -2.243  1.00 14.70  ?  360  TYR A CD2    1 
ATOM   5489  C CE1    . TYR A 1 360 ? -18.649 -9.233  -0.227  1.00 17.68  ?  360  TYR A CE1    1 
ATOM   5490  C CE2    . TYR A 1 360 ? -17.938 -8.466  -2.374  1.00 16.88  ?  360  TYR A CE2    1 
ATOM   5491  C CZ     . TYR A 1 360 ? -18.871 -8.478  -1.351  1.00 18.72  ?  360  TYR A CZ     1 
ATOM   5492  O OH     . TYR A 1 360 ? -20.039 -7.752  -1.449  1.00 20.37  ?  360  TYR A OH     1 
ATOM   5493  H H      . TYR A 1 360 ? -13.650 -12.524 -0.773  1.00 18.47  ?  360  TYR A H      1 
ATOM   5494  H HA     . TYR A 1 360 ? -16.225 -12.527 -0.361  1.00 20.73  ?  360  TYR A HA     1 
ATOM   5495  H HB2    . TYR A 1 360 ? -14.911 -10.593 -0.108  1.00 21.39  ?  360  TYR A HB2    1 
ATOM   5496  H HB3    . TYR A 1 360 ? -14.704 -10.541 -1.683  1.00 21.39  ?  360  TYR A HB3    1 
ATOM   5497  H HD1    . TYR A 1 360 ? -17.380 -10.491 0.652   1.00 19.72  ?  360  TYR A HD1    1 
ATOM   5498  H HD2    . TYR A 1 360 ? -16.165 -9.179  -2.925  1.00 17.64  ?  360  TYR A HD2    1 
ATOM   5499  H HE1    . TYR A 1 360 ? -19.277 -9.239  0.458   1.00 21.21  ?  360  TYR A HE1    1 
ATOM   5500  H HE2    . TYR A 1 360 ? -18.089 -7.964  -3.142  1.00 20.25  ?  360  TYR A HE2    1 
ATOM   5501  H HH     . TYR A 1 360 ? -20.073 -7.361  -2.192  1.00 24.44  ?  360  TYR A HH     1 
ATOM   5502  N N      . LEU A 1 361 ? -15.417 -12.806 -3.439  1.00 14.57  ?  361  LEU A N      1 
ATOM   5503  C CA     . LEU A 1 361 ? -15.921 -13.297 -4.718  1.00 14.06  ?  361  LEU A CA     1 
ATOM   5504  C C      . LEU A 1 361 ? -16.608 -14.648 -4.555  1.00 13.60  ?  361  LEU A C      1 
ATOM   5505  O O      . LEU A 1 361 ? -17.722 -14.853 -5.048  1.00 15.00  ?  361  LEU A O      1 
ATOM   5506  C CB     . LEU A 1 361 ? -14.776 -13.380 -5.721  1.00 15.04  ?  361  LEU A CB     1 
ATOM   5507  C CG     . LEU A 1 361 ? -15.080 -14.024 -7.073  1.00 14.53  ?  361  LEU A CG     1 
ATOM   5508  C CD1    . LEU A 1 361 ? -16.067 -13.182 -7.862  1.00 16.96  ?  361  LEU A CD1    1 
ATOM   5509  C CD2    . LEU A 1 361 ? -13.795 -14.190 -7.868  1.00 16.00  ?  361  LEU A CD2    1 
ATOM   5510  H H      . LEU A 1 361 ? -14.576 -12.626 -3.437  1.00 17.49  ?  361  LEU A H      1 
ATOM   5511  H HA     . LEU A 1 361 ? -16.578 -12.673 -5.063  1.00 16.87  ?  361  LEU A HA     1 
ATOM   5512  H HB2    . LEU A 1 361 ? -14.471 -12.477 -5.900  1.00 18.04  ?  361  LEU A HB2    1 
ATOM   5513  H HB3    . LEU A 1 361 ? -14.062 -13.897 -5.316  1.00 18.04  ?  361  LEU A HB3    1 
ATOM   5514  H HG     . LEU A 1 361 ? -15.477 -14.896 -6.925  1.00 17.43  ?  361  LEU A HG     1 
ATOM   5515  H HD11   . LEU A 1 361 ? -16.228 -13.604 -8.720  1.00 20.35  ?  361  LEU A HD11   1 
ATOM   5516  H HD12   . LEU A 1 361 ? -16.897 -13.118 -7.364  1.00 20.35  ?  361  LEU A HD12   1 
ATOM   5517  H HD13   . LEU A 1 361 ? -15.692 -12.297 -7.994  1.00 20.35  ?  361  LEU A HD13   1 
ATOM   5518  H HD21   . LEU A 1 361 ? -13.999 -14.620 -8.713  1.00 19.20  ?  361  LEU A HD21   1 
ATOM   5519  H HD22   . LEU A 1 361 ? -13.406 -13.316 -8.027  1.00 19.20  ?  361  LEU A HD22   1 
ATOM   5520  H HD23   . LEU A 1 361 ? -13.178 -14.739 -7.358  1.00 19.20  ?  361  LEU A HD23   1 
ATOM   5521  N N      . GLN A 1 362 ? -15.969 -15.585 -3.853  1.00 15.41  ?  362  GLN A N      1 
ATOM   5522  C CA     . GLN A 1 362 ? -16.602 -16.880 -3.651  1.00 14.76  ?  362  GLN A CA     1 
ATOM   5523  C C      . GLN A 1 362 ? -17.925 -16.734 -2.897  1.00 15.57  ?  362  GLN A C      1 
ATOM   5524  O O      . GLN A 1 362 ? -18.920 -17.378 -3.243  1.00 15.91  ?  362  GLN A O      1 
ATOM   5525  C CB     . GLN A 1 362 ? -15.678 -17.829 -2.881  1.00 13.98  ?  362  GLN A CB     1 
ATOM   5526  C CG     . GLN A 1 362 ? -14.295 -18.008 -3.421  1.00 14.99  ?  362  GLN A CG     1 
ATOM   5527  C CD     . GLN A 1 362 ? -14.245 -18.362 -4.889  1.00 15.38  ?  362  GLN A CD     1 
ATOM   5528  O OE1    . GLN A 1 362 ? -15.014 -19.199 -5.387  1.00 16.73  ?  362  GLN A OE1    1 
ATOM   5529  N NE2    . GLN A 1 362 ? -13.358 -17.693 -5.598  1.00 16.42  ?  362  GLN A NE2    1 
ATOM   5530  H H      . GLN A 1 362 ? -15.192 -15.498 -3.494  1.00 18.48  ?  362  GLN A H      1 
ATOM   5531  H HA     . GLN A 1 362 ? -16.773 -17.268 -4.524  1.00 17.71  ?  362  GLN A HA     1 
ATOM   5532  H HB2    . GLN A 1 362 ? -15.587 -17.491 -1.976  1.00 16.77  ?  362  GLN A HB2    1 
ATOM   5533  H HB3    . GLN A 1 362 ? -16.092 -18.706 -2.867  1.00 16.77  ?  362  GLN A HB3    1 
ATOM   5534  H HG2    . GLN A 1 362 ? -13.805 -17.179 -3.302  1.00 17.98  ?  362  GLN A HG2    1 
ATOM   5535  H HG3    . GLN A 1 362 ? -13.860 -18.724 -2.931  1.00 17.98  ?  362  GLN A HG3    1 
ATOM   5536  H HE21   . GLN A 1 362 ? -12.860 -17.103 -5.218  1.00 19.70  ?  362  GLN A HE21   1 
ATOM   5537  H HE22   . GLN A 1 362 ? -13.278 -17.846 -6.440  1.00 19.70  ?  362  GLN A HE22   1 
ATOM   5538  N N      . GLN A 1 363 ? -17.943 -15.899 -1.853  1.00 14.70  ?  363  GLN A N      1 
ATOM   5539  C CA     . GLN A 1 363 ? -19.152 -15.701 -1.062  1.00 15.50  ?  363  GLN A CA     1 
ATOM   5540  C C      . GLN A 1 363 ? -20.277 -15.137 -1.914  1.00 17.04  ?  363  GLN A C      1 
ATOM   5541  O O      . GLN A 1 363 ? -21.427 -15.594 -1.824  1.00 17.07  ?  363  GLN A O      1 
ATOM   5542  C CB     . GLN A 1 363 ? -18.842 -14.795 0.129   1.00 20.76  ?  363  GLN A CB     1 
ATOM   5543  C CG     . GLN A 1 363 ? -17.933 -15.476 1.154   1.00 27.89  ?  363  GLN A CG     1 
ATOM   5544  C CD     . GLN A 1 363 ? -17.263 -14.507 2.108   1.00 33.74  ?  363  GLN A CD     1 
ATOM   5545  O OE1    . GLN A 1 363 ? -17.551 -13.303 2.115   1.00 34.77  ?  363  GLN A OE1    1 
ATOM   5546  N NE2    . GLN A 1 363 ? -16.356 -15.033 2.932   1.00 36.66  ?  363  GLN A NE2    1 
ATOM   5547  H H      . GLN A 1 363 ? -17.269 -15.437 -1.583  1.00 17.64  ?  363  GLN A H      1 
ATOM   5548  H HA     . GLN A 1 363 ? -19.456 -16.553 -0.712  1.00 18.59  ?  363  GLN A HA     1 
ATOM   5549  H HB2    . GLN A 1 363 ? -18.394 -13.996 -0.188  1.00 24.91  ?  363  GLN A HB2    1 
ATOM   5550  H HB3    . GLN A 1 363 ? -19.671 -14.557 0.572   1.00 24.91  ?  363  GLN A HB3    1 
ATOM   5551  H HG2    . GLN A 1 363 ? -18.464 -16.093 1.682   1.00 33.46  ?  363  GLN A HG2    1 
ATOM   5552  H HG3    . GLN A 1 363 ? -17.236 -15.958 0.682   1.00 33.46  ?  363  GLN A HG3    1 
ATOM   5553  H HE21   . GLN A 1 363 ? -16.183 -15.875 2.901   1.00 43.99  ?  363  GLN A HE21   1 
ATOM   5554  H HE22   . GLN A 1 363 ? -15.944 -14.531 3.496   1.00 43.99  ?  363  GLN A HE22   1 
ATOM   5555  N N      . CYS A 1 364 ? -19.974 -14.142 -2.744  1.00 17.67  ?  364  CYS A N      1 
ATOM   5556  C CA     . CYS A 1 364 ? -21.010 -13.543 -3.578  1.00 16.39  ?  364  CYS A CA     1 
ATOM   5557  C C      . CYS A 1 364 ? -21.520 -14.514 -4.637  1.00 14.58  ?  364  CYS A C      1 
ATOM   5558  O O      . CYS A 1 364 ? -22.728 -14.559 -4.910  1.00 15.50  ?  364  CYS A O      1 
ATOM   5559  C CB     . CYS A 1 364 ? -20.476 -12.272 -4.239  1.00 17.84  ?  364  CYS A CB     1 
ATOM   5560  S SG     . CYS A 1 364 ? -20.158 -10.915 -3.103  1.00 19.83  ?  364  CYS A SG     1 
ATOM   5561  H H      . CYS A 1 364 ? -19.191 -13.800 -2.843  1.00 21.20  ?  364  CYS A H      1 
ATOM   5562  H HA     . CYS A 1 364 ? -21.759 -13.305 -3.010  1.00 19.67  ?  364  CYS A HA     1 
ATOM   5563  H HB2    . CYS A 1 364 ? -19.640 -12.484 -4.684  1.00 21.40  ?  364  CYS A HB2    1 
ATOM   5564  H HB3    . CYS A 1 364 ? -21.128 -11.964 -4.888  1.00 21.40  ?  364  CYS A HB3    1 
ATOM   5565  H HG     . CYS A 1 364 ? -19.830 -9.948  -3.733  1.00 23.79  ?  364  CYS A HG     1 
ATOM   5566  N N      A MET A 1 365 ? -20.623 -15.296 -5.248  0.62 15.14  ?  365  MET A N      1 
ATOM   5567  N N      B MET A 1 365 ? -20.624 -15.300 -5.243  0.38 15.33  ?  365  MET A N      1 
ATOM   5568  C CA     A MET A 1 365 ? -21.053 -16.282 -6.236  0.62 15.38  ?  365  MET A CA     1 
ATOM   5569  C CA     B MET A 1 365 ? -21.055 -16.281 -6.235  0.38 15.72  ?  365  MET A CA     1 
ATOM   5570  C C      A MET A 1 365 ? -21.931 -17.358 -5.598  0.62 15.37  ?  365  MET A C      1 
ATOM   5571  C C      B MET A 1 365 ? -21.930 -17.359 -5.600  0.38 15.72  ?  365  MET A C      1 
ATOM   5572  O O      A MET A 1 365 ? -22.943 -17.763 -6.175  0.62 15.61  ?  365  MET A O      1 
ATOM   5573  O O      B MET A 1 365 ? -22.943 -17.764 -6.177  0.38 15.77  ?  365  MET A O      1 
ATOM   5574  C CB     A MET A 1 365 ? -19.829 -16.925 -6.903  0.62 15.26  ?  365  MET A CB     1 
ATOM   5575  C CB     B MET A 1 365 ? -19.833 -16.912 -6.912  0.38 15.79  ?  365  MET A CB     1 
ATOM   5576  C CG     A MET A 1 365 ? -19.070 -15.994 -7.827  0.62 14.55  ?  365  MET A CG     1 
ATOM   5577  C CG     B MET A 1 365 ? -19.022 -15.934 -7.745  0.38 15.18  ?  365  MET A CG     1 
ATOM   5578  S SD     A MET A 1 365 ? -20.018 -15.595 -9.313  0.62 17.16  ?  365  MET A SD     1 
ATOM   5579  S SD     B MET A 1 365 ? -19.820 -15.507 -9.308  0.38 16.89  ?  365  MET A SD     1 
ATOM   5580  C CE     A MET A 1 365 ? -18.868 -14.550 -10.192 0.62 16.54  ?  365  MET A CE     1 
ATOM   5581  C CE     B MET A 1 365 ? -19.434 -16.961 -10.279 0.38 16.59  ?  365  MET A CE     1 
ATOM   5582  H H      A MET A 1 365 ? -19.774 -15.276 -5.110  0.62 18.17  ?  365  MET A H      1 
ATOM   5583  H H      B MET A 1 365 ? -19.776 -15.285 -5.100  0.38 18.39  ?  365  MET A H      1 
ATOM   5584  H HA     A MET A 1 365 ? -21.564 -15.824 -6.922  0.62 18.45  ?  365  MET A HA     1 
ATOM   5585  H HA     B MET A 1 365 ? -21.570 -15.823 -6.918  0.38 18.86  ?  365  MET A HA     1 
ATOM   5586  H HB2    A MET A 1 365 ? -19.216 -17.218 -6.210  0.62 18.30  ?  365  MET A HB2    1 
ATOM   5587  H HB2    B MET A 1 365 ? -19.249 -17.273 -6.227  0.38 18.95  ?  365  MET A HB2    1 
ATOM   5588  H HB3    A MET A 1 365 ? -20.125 -17.685 -7.427  0.62 18.30  ?  365  MET A HB3    1 
ATOM   5589  H HB3    B MET A 1 365 ? -20.134 -17.623 -7.499  0.38 18.95  ?  365  MET A HB3    1 
ATOM   5590  H HG2    A MET A 1 365 ? -18.878 -15.167 -7.359  0.62 17.45  ?  365  MET A HG2    1 
ATOM   5591  H HG2    B MET A 1 365 ? -18.898 -15.116 -7.239  0.38 18.21  ?  365  MET A HG2    1 
ATOM   5592  H HG3    A MET A 1 365 ? -18.243 -16.421 -8.101  0.62 17.45  ?  365  MET A HG3    1 
ATOM   5593  H HG3    B MET A 1 365 ? -18.161 -16.332 -7.949  0.38 18.21  ?  365  MET A HG3    1 
ATOM   5594  H HE1    A MET A 1 365 ? -19.278 -14.256 -11.020 0.62 19.85  ?  365  MET A HE1    1 
ATOM   5595  H HE1    B MET A 1 365 ? -19.894 -16.903 -11.131 0.38 19.90  ?  365  MET A HE1    1 
ATOM   5596  H HE2    A MET A 1 365 ? -18.651 -13.783 -9.639  0.62 19.85  ?  365  MET A HE2    1 
ATOM   5597  H HE2    B MET A 1 365 ? -18.475 -16.999 -10.423 0.38 19.90  ?  365  MET A HE2    1 
ATOM   5598  H HE3    A MET A 1 365 ? -18.063 -15.057 -10.384 0.62 19.85  ?  365  MET A HE3    1 
ATOM   5599  H HE3    B MET A 1 365 ? -19.728 -17.750 -9.797  0.38 19.90  ?  365  MET A HE3    1 
ATOM   5600  N N      . GLN A 1 366 ? -21.555 -17.836 -4.411  1.00 16.31  ?  366  GLN A N      1 
ATOM   5601  C CA     . GLN A 1 366 ? -22.372 -18.832 -3.724  1.00 17.89  ?  366  GLN A CA     1 
ATOM   5602  C C      . GLN A 1 366 ? -23.732 -18.257 -3.351  1.00 16.98  ?  366  GLN A C      1 
ATOM   5603  O O      . GLN A 1 366 ? -24.760 -18.911 -3.540  1.00 18.95  ?  366  GLN A O      1 
ATOM   5604  C CB     . GLN A 1 366 ? -21.652 -19.330 -2.467  1.00 19.04  ?  366  GLN A CB     1 
ATOM   5605  C CG     . GLN A 1 366 ? -20.377 -20.118 -2.755  1.00 21.13  ?  366  GLN A CG     1 
ATOM   5606  C CD     . GLN A 1 366 ? -20.656 -21.485 -3.373  1.00 25.90  ?  366  GLN A CD     1 
ATOM   5607  O OE1    . GLN A 1 366 ? -21.773 -22.012 -3.291  1.00 26.85  ?  366  GLN A OE1    1 
ATOM   5608  N NE2    . GLN A 1 366 ? -19.629 -22.070 -3.987  1.00 26.56  ?  366  GLN A NE2    1 
ATOM   5609  H H      . GLN A 1 366 ? -20.843 -17.605 -3.987  1.00 19.57  ?  366  GLN A H      1 
ATOM   5610  H HA     . GLN A 1 366 ? -22.507 -19.588 -4.317  1.00 21.46  ?  366  GLN A HA     1 
ATOM   5611  H HB2    . GLN A 1 366 ? -21.409 -18.564 -1.924  1.00 22.85  ?  366  GLN A HB2    1 
ATOM   5612  H HB3    . GLN A 1 366 ? -22.253 -19.910 -1.974  1.00 22.85  ?  366  GLN A HB3    1 
ATOM   5613  H HG2    . GLN A 1 366 ? -19.828 -19.614 -3.376  1.00 25.36  ?  366  GLN A HG2    1 
ATOM   5614  H HG3    . GLN A 1 366 ? -19.897 -20.256 -1.924  1.00 25.36  ?  366  GLN A HG3    1 
ATOM   5615  H HE21   . GLN A 1 366 ? -18.865 -21.677 -4.018  1.00 31.86  ?  366  GLN A HE21   1 
ATOM   5616  H HE22   . GLN A 1 366 ? -19.730 -22.842 -4.353  1.00 31.86  ?  366  GLN A HE22   1 
ATOM   5617  N N      . GLN A 1 367 ? -23.762 -17.018 -2.845  1.00 16.41  ?  367  GLN A N      1 
ATOM   5618  C CA     . GLN A 1 367 ? -25.030 -16.392 -2.488  1.00 20.52  ?  367  GLN A CA     1 
ATOM   5619  C C      . GLN A 1 367 ? -25.926 -16.212 -3.706  1.00 18.66  ?  367  GLN A C      1 
ATOM   5620  O O      . GLN A 1 367 ? -27.131 -16.498 -3.670  1.00 21.45  ?  367  GLN A O      1 
ATOM   5621  C CB     . GLN A 1 367 ? -24.745 -15.038 -1.847  1.00 26.37  ?  367  GLN A CB     1 
ATOM   5622  C CG     . GLN A 1 367 ? -25.967 -14.199 -1.607  1.00 36.38  ?  367  GLN A CG     1 
ATOM   5623  C CD     . GLN A 1 367 ? -26.496 -14.393 -0.230  1.00 46.85  ?  367  GLN A CD     1 
ATOM   5624  O OE1    . GLN A 1 367 ? -27.369 -15.228 -0.001  1.00 51.59  ?  367  GLN A OE1    1 
ATOM   5625  N NE2    . GLN A 1 367 ? -25.959 -13.634 0.723   1.00 50.83  ?  367  GLN A NE2    1 
ATOM   5626  H H      . GLN A 1 367 ? -23.071 -16.527 -2.702  1.00 19.69  ?  367  GLN A H      1 
ATOM   5627  H HA     . GLN A 1 367 ? -25.498 -16.960 -1.856  1.00 24.62  ?  367  GLN A HA     1 
ATOM   5628  H HB2    . GLN A 1 367 ? -24.316 -15.186 -0.990  1.00 31.64  ?  367  GLN A HB2    1 
ATOM   5629  H HB3    . GLN A 1 367 ? -24.154 -14.537 -2.431  1.00 31.64  ?  367  GLN A HB3    1 
ATOM   5630  H HG2    . GLN A 1 367 ? -25.741 -13.262 -1.720  1.00 43.65  ?  367  GLN A HG2    1 
ATOM   5631  H HG3    . GLN A 1 367 ? -26.659 -14.451 -2.239  1.00 43.65  ?  367  GLN A HG3    1 
ATOM   5632  H HE21   . GLN A 1 367 ? -25.341 -13.070 0.526   1.00 60.99  ?  367  GLN A HE21   1 
ATOM   5633  H HE22   . GLN A 1 367 ? -26.231 -13.709 1.535   1.00 60.99  ?  367  GLN A HE22   1 
ATOM   5634  N N      . THR A 1 368 ? -25.367 -15.687 -4.781  1.00 17.86  ?  368  THR A N      1 
ATOM   5635  C CA     . THR A 1 368 ? -26.175 -15.337 -5.940  1.00 17.27  ?  368  THR A CA     1 
ATOM   5636  C C      . THR A 1 368 ? -26.572 -16.563 -6.744  1.00 18.05  ?  368  THR A C      1 
ATOM   5637  O O      . THR A 1 368 ? -27.677 -16.610 -7.287  1.00 20.13  ?  368  THR A O      1 
ATOM   5638  C CB     . THR A 1 368 ? -25.391 -14.339 -6.794  1.00 18.04  ?  368  THR A CB     1 
ATOM   5639  O OG1    . THR A 1 368 ? -25.204 -13.133 -6.031  1.00 19.53  ?  368  THR A OG1    1 
ATOM   5640  C CG2    . THR A 1 368 ? -26.131 -14.002 -8.089  1.00 17.66  ?  368  THR A CG2    1 
ATOM   5641  H H      . THR A 1 368 ? -24.527 -15.523 -4.869  1.00 21.43  ?  368  THR A H      1 
ATOM   5642  H HA     . THR A 1 368 ? -27.000 -14.916 -5.652  1.00 20.72  ?  368  THR A HA     1 
ATOM   5643  H HB     . THR A 1 368 ? -24.537 -14.727 -7.039  1.00 21.65  ?  368  THR A HB     1 
ATOM   5644  H HG1    . THR A 1 368 ? -24.766 -13.298 -5.333  1.00 23.43  ?  368  THR A HG1    1 
ATOM   5645  H HG21   . THR A 1 368 ? -25.701 -13.253 -8.531  1.00 21.18  ?  368  THR A HG21   1 
ATOM   5646  H HG22   . THR A 1 368 ? -26.122 -14.767 -8.685  1.00 21.18  ?  368  THR A HG22   1 
ATOM   5647  H HG23   . THR A 1 368 ? -27.051 -13.766 -7.893  1.00 21.18  ?  368  THR A HG23   1 
ATOM   5648  N N      . PHE A 1 369 ? -25.696 -17.572 -6.838  1.00 15.38  ?  369  PHE A N      1 
ATOM   5649  C CA     . PHE A 1 369 ? -25.926 -18.686 -7.744  1.00 16.67  ?  369  PHE A CA     1 
ATOM   5650  C C      . PHE A 1 369 ? -26.076 -20.051 -7.089  1.00 17.35  ?  369  PHE A C      1 
ATOM   5651  O O      . PHE A 1 369 ? -26.345 -21.029 -7.800  1.00 18.07  ?  369  PHE A O      1 
ATOM   5652  C CB     . PHE A 1 369 ? -24.789 -18.727 -8.775  1.00 16.67  ?  369  PHE A CB     1 
ATOM   5653  C CG     . PHE A 1 369 ? -24.756 -17.540 -9.686  1.00 15.69  ?  369  PHE A CG     1 
ATOM   5654  C CD1    . PHE A 1 369 ? -25.744 -17.357 -10.650 1.00 15.41  ?  369  PHE A CD1    1 
ATOM   5655  C CD2    . PHE A 1 369 ? -23.750 -16.595 -9.584  1.00 15.62  ?  369  PHE A CD2    1 
ATOM   5656  C CE1    . PHE A 1 369 ? -25.713 -16.263 -11.508 1.00 16.82  ?  369  PHE A CE1    1 
ATOM   5657  C CE2    . PHE A 1 369 ? -23.725 -15.499 -10.435 1.00 15.44  ?  369  PHE A CE2    1 
ATOM   5658  C CZ     . PHE A 1 369 ? -24.695 -15.334 -11.387 1.00 17.24  ?  369  PHE A CZ     1 
ATOM   5659  H H      . PHE A 1 369 ? -24.966 -17.625 -6.386  1.00 18.45  ?  369  PHE A H      1 
ATOM   5660  H HA     . PHE A 1 369 ? -26.770 -18.531 -8.197  1.00 20.00  ?  369  PHE A HA     1 
ATOM   5661  H HB2    . PHE A 1 369 ? -23.942 -18.760 -8.303  1.00 20.00  ?  369  PHE A HB2    1 
ATOM   5662  H HB3    . PHE A 1 369 ? -24.894 -19.519 -9.324  1.00 20.00  ?  369  PHE A HB3    1 
ATOM   5663  H HD1    . PHE A 1 369 ? -26.434 -17.976 -10.720 1.00 18.49  ?  369  PHE A HD1    1 
ATOM   5664  H HD2    . PHE A 1 369 ? -23.086 -16.695 -8.940  1.00 18.74  ?  369  PHE A HD2    1 
ATOM   5665  H HE1    . PHE A 1 369 ? -26.371 -16.158 -12.157 1.00 20.18  ?  369  PHE A HE1    1 
ATOM   5666  H HE2    . PHE A 1 369 ? -23.043 -14.871 -10.358 1.00 18.53  ?  369  PHE A HE2    1 
ATOM   5667  H HZ     . PHE A 1 369 ? -24.670 -14.597 -11.954 1.00 20.68  ?  369  PHE A HZ     1 
ATOM   5668  N N      . GLY A 1 370 ? -25.951 -20.149 -5.767  1.00 18.51  ?  370  GLY A N      1 
ATOM   5669  C CA     . GLY A 1 370 ? -25.982 -21.441 -5.101  1.00 20.02  ?  370  GLY A CA     1 
ATOM   5670  C C      . GLY A 1 370 ? -27.304 -22.182 -5.186  1.00 21.85  ?  370  GLY A C      1 
ATOM   5671  O O      . GLY A 1 370 ? -27.334 -23.397 -4.951  1.00 22.85  ?  370  GLY A O      1 
ATOM   5672  H H      . GLY A 1 370 ? -25.846 -19.481 -5.235  1.00 22.21  ?  370  GLY A H      1 
ATOM   5673  H HA2    . GLY A 1 370 ? -25.301 -22.009 -5.495  1.00 24.02  ?  370  GLY A HA2    1 
ATOM   5674  H HA3    . GLY A 1 370 ? -25.778 -21.310 -4.162  1.00 24.02  ?  370  GLY A HA3    1 
ATOM   5675  N N      . GLU A 1 371 ? -28.379 -21.497 -5.533  1.00 21.64  ?  371  GLU A N      1 
ATOM   5676  C CA     . GLU A 1 371 ? -29.678 -22.110 -5.723  1.00 24.98  ?  371  GLU A CA     1 
ATOM   5677  C C      . GLU A 1 371 ? -30.299 -21.671 -7.030  1.00 23.09  ?  371  GLU A C      1 
ATOM   5678  O O      . GLU A 1 371 ? -31.461 -21.616 -7.147  1.00 25.90  ?  371  GLU A O      1 
ATOM   5679  C CB     . GLU A 1 371 ? -30.621 -21.678 -4.631  1.00 32.03  ?  371  GLU A CB     1 
ATOM   5680  C CG     . GLU A 1 371 ? -30.532 -22.516 -3.417  1.00 42.24  ?  371  GLU A CG     1 
ATOM   5681  C CD     . GLU A 1 371 ? -31.126 -21.854 -2.175  1.00 51.62  ?  371  GLU A CD     1 
ATOM   5682  O OE1    . GLU A 1 371 ? -31.973 -20.915 -2.260  1.00 54.07  ?  371  GLU A OE1    1 
ATOM   5683  O OE2    . GLU A 1 371 ? -30.682 -22.267 -1.112  1.00 56.45  -1 371  GLU A OE2    1 
ATOM   5684  H H      . GLU A 1 371 ? -28.380 -20.648 -5.668  1.00 25.97  ?  371  GLU A H      1 
ATOM   5685  H HA     . GLU A 1 371 ? -29.598 -23.087 -5.714  1.00 29.98  ?  371  GLU A HA     1 
ATOM   5686  H HB2    . GLU A 1 371 ? -30.413 -20.765 -4.379  1.00 38.43  ?  371  GLU A HB2    1 
ATOM   5687  H HB3    . GLU A 1 371 ? -31.531 -21.729 -4.963  1.00 38.43  ?  371  GLU A HB3    1 
ATOM   5688  H HG2    . GLU A 1 371 ? -31.013 -23.345 -3.571  1.00 50.68  ?  371  GLU A HG2    1 
ATOM   5689  H HG3    . GLU A 1 371 ? -29.598 -22.706 -3.234  1.00 50.68  ?  371  GLU A HG3    1 
ATOM   5690  N N      . HIS A 1 372 ? -29.492 -21.298 -7.994  1.00 22.08  ?  372  HIS A N      1 
ATOM   5691  C CA     . HIS A 1 372 ? -30.023 -20.869 -9.275  1.00 20.90  ?  372  HIS A CA     1 
ATOM   5692  C C      . HIS A 1 372 ? -30.412 -22.093 -10.107 1.00 20.73  ?  372  HIS A C      1 
ATOM   5693  O O      . HIS A 1 372 ? -29.658 -23.073 -10.153 1.00 20.74  ?  372  HIS A O      1 
ATOM   5694  C CB     . HIS A 1 372 ? -28.969 -20.050 -10.005 1.00 20.96  ?  372  HIS A CB     1 
ATOM   5695  C CG     . HIS A 1 372 ? -29.513 -19.332 -11.188 1.00 17.91  ?  372  HIS A CG     1 
ATOM   5696  N ND1    . HIS A 1 372 ? -29.888 -19.987 -12.340 1.00 17.24  ?  372  HIS A ND1    1 
ATOM   5697  C CD2    . HIS A 1 372 ? -29.775 -18.023 -11.395 1.00 19.08  ?  372  HIS A CD2    1 
ATOM   5698  C CE1    . HIS A 1 372 ? -30.388 -19.113 -13.194 1.00 17.33  ?  372  HIS A CE1    1 
ATOM   5699  N NE2    . HIS A 1 372 ? -30.304 -17.914 -12.655 1.00 18.76  ?  372  HIS A NE2    1 
ATOM   5700  H H      . HIS A 1 372 ? -28.634 -21.282 -7.932  1.00 26.49  ?  372  HIS A H      1 
ATOM   5701  H HA     . HIS A 1 372 ? -30.815 -20.321 -9.156  1.00 25.07  ?  372  HIS A HA     1 
ATOM   5702  H HB2    . HIS A 1 372 ? -28.604 -19.390 -9.395  1.00 25.15  ?  372  HIS A HB2    1 
ATOM   5703  H HB3    . HIS A 1 372 ? -28.266 -20.643 -10.312 1.00 25.15  ?  372  HIS A HB3    1 
ATOM   5704  H HD2    . HIS A 1 372 ? -29.626 -17.327 -10.796 1.00 22.90  ?  372  HIS A HD2    1 
ATOM   5705  H HE1    . HIS A 1 372 ? -30.740 -19.311 -14.032 1.00 20.79  ?  372  HIS A HE1    1 
ATOM   5706  H HE2    . HIS A 1 372 ? -30.542 -17.180 -13.034 1.00 22.50  ?  372  HIS A HE2    1 
ATOM   5707  N N      . PRO A 1 373 ? -31.581 -22.066 -10.760 1.00 21.28  ?  373  PRO A N      1 
ATOM   5708  C CA     . PRO A 1 373 ? -32.060 -23.261 -11.468 1.00 22.27  ?  373  PRO A CA     1 
ATOM   5709  C C      . PRO A 1 373 ? -31.236 -23.672 -12.673 1.00 21.64  ?  373  PRO A C      1 
ATOM   5710  O O      . PRO A 1 373 ? -31.463 -24.778 -13.197 1.00 22.48  ?  373  PRO A O      1 
ATOM   5711  C CB     . PRO A 1 373 ? -33.498 -22.882 -11.882 1.00 23.09  ?  373  PRO A CB     1 
ATOM   5712  C CG     . PRO A 1 373 ? -33.519 -21.395 -11.868 1.00 24.40  ?  373  PRO A CG     1 
ATOM   5713  C CD     . PRO A 1 373 ? -32.582 -20.978 -10.774 1.00 21.86  ?  373  PRO A CD     1 
ATOM   5714  H HA     . PRO A 1 373 ? -32.086 -24.005 -10.847 1.00 26.72  ?  373  PRO A HA     1 
ATOM   5715  H HB2    . PRO A 1 373 ? -33.687 -23.224 -12.770 1.00 27.70  ?  373  PRO A HB2    1 
ATOM   5716  H HB3    . PRO A 1 373 ? -34.132 -23.245 -11.245 1.00 27.70  ?  373  PRO A HB3    1 
ATOM   5717  H HG2    . PRO A 1 373 ? -33.218 -21.056 -12.725 1.00 29.28  ?  373  PRO A HG2    1 
ATOM   5718  H HG3    . PRO A 1 373 ? -34.419 -21.084 -11.685 1.00 29.28  ?  373  PRO A HG3    1 
ATOM   5719  H HD2    . PRO A 1 373 ? -32.165 -20.127 -10.981 1.00 26.23  ?  373  PRO A HD2    1 
ATOM   5720  H HD3    . PRO A 1 373 ? -33.045 -20.923 -9.924  1.00 26.23  ?  373  PRO A HD3    1 
ATOM   5721  N N      . LEU A 1 374 ? -30.324 -22.823 -13.152 1.00 19.47  ?  374  LEU A N      1 
ATOM   5722  C CA     . LEU A 1 374 ? -29.468 -23.185 -14.269 1.00 19.25  ?  374  LEU A CA     1 
ATOM   5723  C C      . LEU A 1 374 ? -28.078 -23.627 -13.827 1.00 16.44  ?  374  LEU A C      1 
ATOM   5724  O O      . LEU A 1 374 ? -27.281 -24.018 -14.677 1.00 17.15  ?  374  LEU A O      1 
ATOM   5725  C CB     . LEU A 1 374 ? -29.316 -22.002 -15.239 1.00 20.80  ?  374  LEU A CB     1 
ATOM   5726  C CG     . LEU A 1 374 ? -28.891 -22.372 -16.663 1.00 22.33  ?  374  LEU A CG     1 
ATOM   5727  C CD1    . LEU A 1 374 ? -30.017 -23.096 -17.409 1.00 25.42  ?  374  LEU A CD1    1 
ATOM   5728  C CD2    . LEU A 1 374 ? -28.470 -21.154 -17.462 1.00 20.52  ?  374  LEU A CD2    1 
ATOM   5729  H H      . LEU A 1 374 ? -30.186 -22.032 -12.842 1.00 23.37  ?  374  LEU A H      1 
ATOM   5730  H HA     . LEU A 1 374 ? -29.889 -23.915 -14.749 1.00 23.09  ?  374  LEU A HA     1 
ATOM   5731  H HB2    . LEU A 1 374 ? -30.170 -21.546 -15.300 1.00 24.95  ?  374  LEU A HB2    1 
ATOM   5732  H HB3    . LEU A 1 374 ? -28.643 -21.401 -14.882 1.00 24.95  ?  374  LEU A HB3    1 
ATOM   5733  H HG     . LEU A 1 374 ? -28.128 -22.966 -16.586 1.00 26.80  ?  374  LEU A HG     1 
ATOM   5734  H HD11   . LEU A 1 374 ? -29.733 -23.267 -18.321 1.00 30.50  ?  374  LEU A HD11   1 
ATOM   5735  H HD12   . LEU A 1 374 ? -30.206 -23.934 -16.959 1.00 30.50  ?  374  LEU A HD12   1 
ATOM   5736  H HD13   . LEU A 1 374 ? -30.808 -22.535 -17.409 1.00 30.50  ?  374  LEU A HD13   1 
ATOM   5737  H HD21   . LEU A 1 374 ? -28.176 -21.440 -18.342 1.00 24.62  ?  374  LEU A HD21   1 
ATOM   5738  H HD22   . LEU A 1 374 ? -29.227 -20.554 -17.545 1.00 24.62  ?  374  LEU A HD22   1 
ATOM   5739  H HD23   . LEU A 1 374 ? -27.743 -20.708 -16.999 1.00 24.62  ?  374  LEU A HD23   1 
ATOM   5740  N N      . VAL A 1 375 ? -27.757 -23.555 -12.537 1.00 17.83  ?  375  VAL A N      1 
ATOM   5741  C CA     . VAL A 1 375 ? -26.374 -23.699 -12.084 1.00 16.38  ?  375  VAL A CA     1 
ATOM   5742  C C      . VAL A 1 375 ? -26.222 -25.012 -11.331 1.00 16.41  ?  375  VAL A C      1 
ATOM   5743  O O      . VAL A 1 375 ? -26.762 -25.179 -10.231 1.00 17.75  ?  375  VAL A O      1 
ATOM   5744  C CB     . VAL A 1 375 ? -25.914 -22.484 -11.254 1.00 17.51  ?  375  VAL A CB     1 
ATOM   5745  C CG1    . VAL A 1 375 ? -24.480 -22.695 -10.732 1.00 17.13  ?  375  VAL A CG1    1 
ATOM   5746  C CG2    . VAL A 1 375 ? -26.012 -21.208 -12.075 1.00 18.17  ?  375  VAL A CG2    1 
ATOM   5747  H H      . VAL A 1 375 ? -28.325 -23.423 -11.905 1.00 21.39  ?  375  VAL A H      1 
ATOM   5748  H HA     . VAL A 1 375 ? -25.801 -23.769 -12.864 1.00 19.65  ?  375  VAL A HA     1 
ATOM   5749  H HB     . VAL A 1 375 ? -26.498 -22.391 -10.486 1.00 21.01  ?  375  VAL A HB     1 
ATOM   5750  H HG11   . VAL A 1 375 ? -24.176 -21.878 -10.307 1.00 20.55  ?  375  VAL A HG11   1 
ATOM   5751  H HG12   . VAL A 1 375 ? -24.482 -23.421 -10.089 1.00 20.55  ?  375  VAL A HG12   1 
ATOM   5752  H HG13   . VAL A 1 375 ? -23.901 -22.915 -11.479 1.00 20.55  ?  375  VAL A HG13   1 
ATOM   5753  H HG21   . VAL A 1 375 ? -25.728 -20.458 -11.528 1.00 21.80  ?  375  VAL A HG21   1 
ATOM   5754  H HG22   . VAL A 1 375 ? -25.437 -21.287 -12.852 1.00 21.80  ?  375  VAL A HG22   1 
ATOM   5755  H HG23   . VAL A 1 375 ? -26.932 -21.082 -12.355 1.00 21.80  ?  375  VAL A HG23   1 
ATOM   5756  N N      . GLY A 1 376 ? -25.464 -25.941 -11.924 1.00 16.98  ?  376  GLY A N      1 
ATOM   5757  C CA     . GLY A 1 376 ? -25.161 -27.199 -11.263 1.00 18.10  ?  376  GLY A CA     1 
ATOM   5758  C C      . GLY A 1 376 ? -24.057 -27.109 -10.234 1.00 17.11  ?  376  GLY A C      1 
ATOM   5759  O O      . GLY A 1 376 ? -24.090 -27.821 -9.225  1.00 18.99  ?  376  GLY A O      1 
ATOM   5760  H H      . GLY A 1 376 ? -25.115 -25.863 -12.706 1.00 20.37  ?  376  GLY A H      1 
ATOM   5761  H HA2    . GLY A 1 376 ? -25.960 -27.518 -10.816 1.00 21.71  ?  376  GLY A HA2    1 
ATOM   5762  H HA3    . GLY A 1 376 ? -24.893 -27.848 -11.932 1.00 21.71  ?  376  GLY A HA3    1 
ATOM   5763  N N      . GLU A 1 377 ? -23.055 -26.259 -10.467 1.00 16.55  ?  377  GLU A N      1 
ATOM   5764  C CA     . GLU A 1 377 ? -21.987 -26.089 -9.498  1.00 15.43  ?  377  GLU A CA     1 
ATOM   5765  C C      . GLU A 1 377 ? -21.461 -24.657 -9.523  1.00 15.13  ?  377  GLU A C      1 
ATOM   5766  O O      . GLU A 1 377 ? -21.235 -24.076 -10.591 1.00 16.05  ?  377  GLU A O      1 
ATOM   5767  C CB     . GLU A 1 377 ? -20.832 -27.084 -9.727  1.00 15.37  ?  377  GLU A CB     1 
ATOM   5768  C CG     . GLU A 1 377 ? -19.705 -26.859 -8.732  1.00 16.88  ?  377  GLU A CG     1 
ATOM   5769  C CD     . GLU A 1 377 ? -18.750 -28.028 -8.603  1.00 17.89  ?  377  GLU A CD     1 
ATOM   5770  O OE1    . GLU A 1 377 ? -17.849 -28.175 -9.444  1.00 16.88  ?  377  GLU A OE1    1 
ATOM   5771  O OE2    . GLU A 1 377 ? -18.889 -28.798 -7.638  1.00 22.08  -1 377  GLU A OE2    1 
ATOM   5772  H H      . GLU A 1 377 ? -22.977 -25.777 -11.175 1.00 19.86  ?  377  GLU A H      1 
ATOM   5773  H HA     . GLU A 1 377 ? -22.356 -26.246 -8.615  1.00 18.51  ?  377  GLU A HA     1 
ATOM   5774  H HB2    . GLU A 1 377 ? -21.161 -27.989 -9.618  1.00 18.44  ?  377  GLU A HB2    1 
ATOM   5775  H HB3    . GLU A 1 377 ? -20.478 -26.965 -10.623 1.00 18.44  ?  377  GLU A HB3    1 
ATOM   5776  H HG2    . GLU A 1 377 ? -19.189 -26.088 -9.015  1.00 20.25  ?  377  GLU A HG2    1 
ATOM   5777  H HG3    . GLU A 1 377 ? -20.091 -26.697 -7.857  1.00 20.25  ?  377  GLU A HG3    1 
ATOM   5778  N N      . VAL A 1 378 ? -21.275 -24.095 -8.329  1.00 16.03  ?  378  VAL A N      1 
ATOM   5779  C CA     . VAL A 1 378 ? -20.542 -22.854 -8.121  1.00 15.75  ?  378  VAL A CA     1 
ATOM   5780  C C      . VAL A 1 378 ? -19.240 -23.266 -7.443  1.00 14.77  ?  378  VAL A C      1 
ATOM   5781  O O      . VAL A 1 378 ? -19.266 -23.971 -6.423  1.00 16.35  ?  378  VAL A O      1 
ATOM   5782  C CB     . VAL A 1 378 ? -21.292 -21.897 -7.180  1.00 18.51  ?  378  VAL A CB     1 
ATOM   5783  C CG1    . VAL A 1 378 ? -20.531 -20.574 -7.050  1.00 18.57  ?  378  VAL A CG1    1 
ATOM   5784  C CG2    . VAL A 1 378 ? -22.710 -21.626 -7.637  1.00 19.31  ?  378  VAL A CG2    1 
ATOM   5785  H H      . VAL A 1 378 ? -21.579 -24.433 -7.598  1.00 19.23  ?  378  VAL A H      1 
ATOM   5786  H HA     . VAL A 1 378 ? -20.391 -22.408 -8.970  1.00 18.90  ?  378  VAL A HA     1 
ATOM   5787  H HB     . VAL A 1 378 ? -21.347 -22.331 -6.314  1.00 22.21  ?  378  VAL A HB     1 
ATOM   5788  H HG11   . VAL A 1 378 ? -21.062 -19.954 -6.526  1.00 22.28  ?  378  VAL A HG11   1 
ATOM   5789  H HG12   . VAL A 1 378 ? -19.683 -20.739 -6.609  1.00 22.28  ?  378  VAL A HG12   1 
ATOM   5790  H HG13   . VAL A 1 378 ? -20.377 -20.210 -7.936  1.00 22.28  ?  378  VAL A HG13   1 
ATOM   5791  H HG21   . VAL A 1 378 ? -23.137 -21.029 -7.002  1.00 23.17  ?  378  VAL A HG21   1 
ATOM   5792  H HG22   . VAL A 1 378 ? -22.685 -21.213 -8.514  1.00 23.17  ?  378  VAL A HG22   1 
ATOM   5793  H HG23   . VAL A 1 378 ? -23.194 -22.465 -7.679  1.00 23.17  ?  378  VAL A HG23   1 
ATOM   5794  N N      . ARG A 1 379 ? -18.106 -22.832 -7.981  1.00 14.08  ?  379  ARG A N      1 
ATOM   5795  C CA     . ARG A 1 379 ? -16.824 -23.250 -7.430  1.00 13.06  ?  379  ARG A CA     1 
ATOM   5796  C C      . ARG A 1 379 ? -15.775 -22.168 -7.625  1.00 13.44  ?  379  ARG A C      1 
ATOM   5797  O O      . ARG A 1 379 ? -15.941 -21.239 -8.418  1.00 14.92  ?  379  ARG A O      1 
ATOM   5798  C CB     . ARG A 1 379 ? -16.360 -24.589 -8.049  1.00 14.58  ?  379  ARG A CB     1 
ATOM   5799  C CG     . ARG A 1 379 ? -16.167 -24.540 -9.555  1.00 15.14  ?  379  ARG A CG     1 
ATOM   5800  C CD     . ARG A 1 379 ? -15.691 -25.860 -10.158 1.00 15.17  ?  379  ARG A CD     1 
ATOM   5801  N NE     . ARG A 1 379 ? -15.633 -25.759 -11.612 1.00 13.79  ?  379  ARG A NE     1 
ATOM   5802  C CZ     . ARG A 1 379 ? -16.478 -26.341 -12.461 1.00 15.36  ?  379  ARG A CZ     1 
ATOM   5803  N NH1    . ARG A 1 379 ? -17.481 -27.110 -12.035 1.00 14.42  ?  379  ARG A NH1    1 
ATOM   5804  N NH2    . ARG A 1 379 ? -16.345 -26.110 -13.772 1.00 15.22  ?  379  ARG A NH2    1 
ATOM   5805  H H      . ARG A 1 379 ? -18.054 -22.301 -8.656  1.00 16.89  ?  379  ARG A H      1 
ATOM   5806  H HA     . ARG A 1 379 ? -16.924 -23.367 -6.472  1.00 15.67  ?  379  ARG A HA     1 
ATOM   5807  H HB2    . ARG A 1 379 ? -15.512 -24.838 -7.651  1.00 17.49  ?  379  ARG A HB2    1 
ATOM   5808  H HB3    . ARG A 1 379 ? -17.028 -25.267 -7.860  1.00 17.49  ?  379  ARG A HB3    1 
ATOM   5809  H HG2    . ARG A 1 379 ? -17.013 -24.313 -9.971  1.00 18.17  ?  379  ARG A HG2    1 
ATOM   5810  H HG3    . ARG A 1 379 ? -15.504 -23.864 -9.763  1.00 18.17  ?  379  ARG A HG3    1 
ATOM   5811  H HD2    . ARG A 1 379 ? -14.804 -26.069 -9.826  1.00 18.20  ?  379  ARG A HD2    1 
ATOM   5812  H HD3    . ARG A 1 379 ? -16.309 -26.569 -9.921  1.00 18.20  ?  379  ARG A HD3    1 
ATOM   5813  H HE     . ARG A 1 379 ? -15.000 -25.285 -11.950 1.00 16.55  ?  379  ARG A HE     1 
ATOM   5814  H HH11   . ARG A 1 379 ? -17.594 -27.241 -11.193 1.00 17.30  ?  379  ARG A HH11   1 
ATOM   5815  H HH12   . ARG A 1 379 ? -18.014 -27.475 -12.603 1.00 17.30  ?  379  ARG A HH12   1 
ATOM   5816  H HH21   . ARG A 1 379 ? -15.720 -25.593 -14.057 1.00 18.26  ?  379  ARG A HH21   1 
ATOM   5817  H HH22   . ARG A 1 379 ? -16.885 -26.480 -14.331 1.00 18.26  ?  379  ARG A HH22   1 
ATOM   5818  N N      . GLY A 1 380 ? -14.680 -22.311 -6.893  1.00 13.31  ?  380  GLY A N      1 
ATOM   5819  C CA     . GLY A 1 380 ? -13.564 -21.403 -7.047  1.00 14.27  ?  380  GLY A CA     1 
ATOM   5820  C C      . GLY A 1 380 ? -12.682 -21.365 -5.815  1.00 13.11  ?  380  GLY A C      1 
ATOM   5821  O O      . GLY A 1 380 ? -12.939 -22.023 -4.802  1.00 14.37  ?  380  GLY A O      1 
ATOM   5822  H H      . GLY A 1 380 ? -14.561 -22.926 -6.303  1.00 15.97  ?  380  GLY A H      1 
ATOM   5823  H HA2    . GLY A 1 380 ? -13.023 -21.682 -7.802  1.00 17.12  ?  380  GLY A HA2    1 
ATOM   5824  H HA3    . GLY A 1 380 ? -13.898 -20.507 -7.212  1.00 17.12  ?  380  GLY A HA3    1 
ATOM   5825  N N      . VAL A 1 381 ? -11.611 -20.588 -5.948  1.00 14.41  ?  381  VAL A N      1 
ATOM   5826  C CA     . VAL A 1 381 ? -10.666 -20.329 -4.871  1.00 14.40  ?  381  VAL A CA     1 
ATOM   5827  C C      . VAL A 1 381 ? -9.932  -19.042 -5.214  1.00 13.59  ?  381  VAL A C      1 
ATOM   5828  O O      . VAL A 1 381 ? -9.534  -18.826 -6.367  1.00 13.56  ?  381  VAL A O      1 
ATOM   5829  C CB     . VAL A 1 381 ? -9.699  -21.517 -4.665  1.00 14.60  ?  381  VAL A CB     1 
ATOM   5830  C CG1    . VAL A 1 381 ? -8.891  -21.797 -5.888  1.00 13.76  ?  381  VAL A CG1    1 
ATOM   5831  C CG2    . VAL A 1 381 ? -8.779  -21.243 -3.482  1.00 16.27  ?  381  VAL A CG2    1 
ATOM   5832  H H      . VAL A 1 381 ? -11.403 -20.186 -6.680  1.00 17.29  ?  381  VAL A H      1 
ATOM   5833  H HA     . VAL A 1 381 ? -11.148 -20.200 -4.039  1.00 17.27  ?  381  VAL A HA     1 
ATOM   5834  H HB     . VAL A 1 381 ? -10.230 -22.307 -4.482  1.00 17.52  ?  381  VAL A HB     1 
ATOM   5835  H HG11   . VAL A 1 381 ? -8.351  -22.588 -5.735  1.00 16.51  ?  381  VAL A HG11   1 
ATOM   5836  H HG12   . VAL A 1 381 ? -9.492  -21.947 -6.635  1.00 16.51  ?  381  VAL A HG12   1 
ATOM   5837  H HG13   . VAL A 1 381 ? -8.319  -21.035 -6.070  1.00 16.51  ?  381  VAL A HG13   1 
ATOM   5838  H HG21   . VAL A 1 381 ? -8.249  -22.035 -3.305  1.00 19.52  ?  381  VAL A HG21   1 
ATOM   5839  H HG22   . VAL A 1 381 ? -8.198  -20.498 -3.701  1.00 19.52  ?  381  VAL A HG22   1 
ATOM   5840  H HG23   . VAL A 1 381 ? -9.319  -21.025 -2.706  1.00 19.52  ?  381  VAL A HG23   1 
ATOM   5841  N N      . GLY A 1 382 ? -9.776  -18.173 -4.227  1.00 14.80  ?  382  GLY A N      1 
ATOM   5842  C CA     . GLY A 1 382 ? -9.054  -16.934 -4.501  1.00 14.44  ?  382  GLY A CA     1 
ATOM   5843  C C      . GLY A 1 382 ? -9.748  -16.154 -5.597  1.00 13.75  ?  382  GLY A C      1 
ATOM   5844  O O      . GLY A 1 382 ? -10.968 -16.061 -5.624  1.00 15.19  ?  382  GLY A O      1 
ATOM   5845  H H      . GLY A 1 382 ? -10.065 -18.267 -3.422  1.00 17.76  ?  382  GLY A H      1 
ATOM   5846  H HA2    . GLY A 1 382 ? -9.020  -16.389 -3.699  1.00 17.33  ?  382  GLY A HA2    1 
ATOM   5847  H HA3    . GLY A 1 382 ? -8.148  -17.137 -4.784  1.00 17.33  ?  382  GLY A HA3    1 
ATOM   5848  N N      . MET A 1 383 ? -8.962  -15.613 -6.542  1.00 13.54  ?  383  MET A N      1 
ATOM   5849  C CA     . MET A 1 383 ? -9.521  -14.871 -7.671  1.00 13.32  ?  383  MET A CA     1 
ATOM   5850  C C      . MET A 1 383 ? -9.807  -15.731 -8.892  1.00 13.43  ?  383  MET A C      1 
ATOM   5851  O O      . MET A 1 383 ? -9.671  -15.258 -10.029 1.00 13.57  ?  383  MET A O      1 
ATOM   5852  C CB     . MET A 1 383 ? -8.605  -13.704 -8.014  1.00 16.55  ?  383  MET A CB     1 
ATOM   5853  C CG     . MET A 1 383 ? -8.645  -12.603 -6.984  1.00 19.82  ?  383  MET A CG     1 
ATOM   5854  S SD     . MET A 1 383 ? -10.229 -11.716 -6.927  1.00 20.27  ?  383  MET A SD     1 
ATOM   5855  C CE     . MET A 1 383 ? -9.653  -10.208 -6.127  1.00 23.30  ?  383  MET A CE     1 
ATOM   5856  H H      . MET A 1 383 ? -8.104  -15.667 -6.545  1.00 16.25  ?  383  MET A H      1 
ATOM   5857  H HA     . MET A 1 383 ? -10.372 -14.504 -7.387  1.00 15.98  ?  383  MET A HA     1 
ATOM   5858  H HB2    . MET A 1 383 ? -7.692  -14.026 -8.073  1.00 19.85  ?  383  MET A HB2    1 
ATOM   5859  H HB3    . MET A 1 383 ? -8.880  -13.328 -8.865  1.00 19.85  ?  383  MET A HB3    1 
ATOM   5860  H HG2    . MET A 1 383 ? -8.491  -12.990 -6.108  1.00 23.78  ?  383  MET A HG2    1 
ATOM   5861  H HG3    . MET A 1 383 ? -7.951  -11.958 -7.189  1.00 23.78  ?  383  MET A HG3    1 
ATOM   5862  H HE1    . MET A 1 383 ? -10.389 -9.579  -6.073  1.00 27.96  ?  383  MET A HE1    1 
ATOM   5863  H HE2    . MET A 1 383 ? -9.336  -10.424 -5.236  1.00 27.96  ?  383  MET A HE2    1 
ATOM   5864  H HE3    . MET A 1 383 ? -8.931  -9.828  -6.652  1.00 27.96  ?  383  MET A HE3    1 
ATOM   5865  N N      . LEU A 1 384 ? -10.242 -16.977 -8.676  1.00 13.59  ?  384  LEU A N      1 
ATOM   5866  C CA     . LEU A 1 384 ? -10.741 -17.862 -9.723  1.00 13.19  ?  384  LEU A CA     1 
ATOM   5867  C C      . LEU A 1 384 ? -12.136 -18.314 -9.301  1.00 12.67  ?  384  LEU A C      1 
ATOM   5868  O O      . LEU A 1 384 ? -12.319 -18.720 -8.151  1.00 13.94  ?  384  LEU A O      1 
ATOM   5869  C CB     . LEU A 1 384 ? -9.854  -19.103 -9.881  1.00 13.64  ?  384  LEU A CB     1 
ATOM   5870  C CG     . LEU A 1 384 ? -8.447  -18.883 -10.414 1.00 12.37  ?  384  LEU A CG     1 
ATOM   5871  C CD1    . LEU A 1 384 ? -7.656  -20.185 -10.354 1.00 14.83  ?  384  LEU A CD1    1 
ATOM   5872  C CD2    . LEU A 1 384 ? -8.479  -18.364 -11.830 1.00 14.65  ?  384  LEU A CD2    1 
ATOM   5873  H H      . LEU A 1 384 ? -10.257 -17.342 -7.897  1.00 16.30  ?  384  LEU A H      1 
ATOM   5874  H HA     . LEU A 1 384 ? -10.768 -17.390 -10.570 1.00 15.82  ?  384  LEU A HA     1 
ATOM   5875  H HB2    . LEU A 1 384 ? -9.765  -19.519 -9.009  1.00 16.36  ?  384  LEU A HB2    1 
ATOM   5876  H HB3    . LEU A 1 384 ? -10.297 -19.710 -10.494 1.00 16.36  ?  384  LEU A HB3    1 
ATOM   5877  H HG     . LEU A 1 384 ? -8.004  -18.219 -9.862  1.00 14.84  ?  384  LEU A HG     1 
ATOM   5878  H HD11   . LEU A 1 384 ? -6.765  -20.030 -10.706 1.00 17.79  ?  384  LEU A HD11   1 
ATOM   5879  H HD12   . LEU A 1 384 ? -7.601  -20.479 -9.432  1.00 17.79  ?  384  LEU A HD12   1 
ATOM   5880  H HD13   . LEU A 1 384 ? -8.110  -20.855 -10.889 1.00 17.79  ?  384  LEU A HD13   1 
ATOM   5881  H HD21   . LEU A 1 384 ? -7.570  -18.287 -12.159 1.00 17.58  ?  384  LEU A HD21   1 
ATOM   5882  H HD22   . LEU A 1 384 ? -8.980  -18.984 -12.383 1.00 17.58  ?  384  LEU A HD22   1 
ATOM   5883  H HD23   . LEU A 1 384 ? -8.908  -17.494 -11.838 1.00 17.58  ?  384  LEU A HD23   1 
ATOM   5884  N N      . ALA A 1 385 ? -13.109 -18.248 -10.214 1.00 13.90  ?  385  ALA A N      1 
ATOM   5885  C CA     . ALA A 1 385 ? -14.434 -18.758 -9.929  1.00 13.16  ?  385  ALA A CA     1 
ATOM   5886  C C      . ALA A 1 385 ? -15.087 -19.235 -11.215 1.00 13.01  ?  385  ALA A C      1 
ATOM   5887  O O      . ALA A 1 385 ? -14.721 -18.817 -12.315 1.00 14.42  ?  385  ALA A O      1 
ATOM   5888  C CB     . ALA A 1 385 ? -15.307 -17.683 -9.261  1.00 14.37  ?  385  ALA A CB     1 
ATOM   5889  H H      . ALA A 1 385 ? -13.018 -17.912 -11.001 1.00 16.68  ?  385  ALA A H      1 
ATOM   5890  H HA     . ALA A 1 385 ? -14.358 -19.520 -9.334  1.00 15.79  ?  385  ALA A HA     1 
ATOM   5891  H HB1    . ALA A 1 385 ? -16.159 -18.077 -9.014  1.00 17.24  ?  385  ALA A HB1    1 
ATOM   5892  H HB2    . ALA A 1 385 ? -14.853 -17.354 -8.469  1.00 17.24  ?  385  ALA A HB2    1 
ATOM   5893  H HB3    . ALA A 1 385 ? -15.448 -16.956 -9.887  1.00 17.24  ?  385  ALA A HB3    1 
ATOM   5894  N N      . ALA A 1 386 ? -16.074 -20.114 -11.063 1.00 13.88  ?  386  ALA A N      1 
ATOM   5895  C CA     . ALA A 1 386 ? -16.789 -20.624 -12.217 1.00 14.13  ?  386  ALA A CA     1 
ATOM   5896  C C      . ALA A 1 386 ? -18.194 -21.067 -11.852 1.00 14.92  ?  386  ALA A C      1 
ATOM   5897  O O      . ALA A 1 386 ? -18.467 -21.475 -10.720 1.00 14.68  ?  386  ALA A O      1 
ATOM   5898  C CB     . ALA A 1 386 ? -16.058 -21.798 -12.864 1.00 15.42  ?  386  ALA A CB     1 
ATOM   5899  H H      . ALA A 1 386 ? -16.343 -20.425 -10.308 1.00 16.65  ?  386  ALA A H      1 
ATOM   5900  H HA     . ALA A 1 386 ? -16.866 -19.890 -12.847 1.00 16.96  ?  386  ALA A HA     1 
ATOM   5901  H HB1    . ALA A 1 386 ? -16.588 -22.131 -13.605 1.00 18.50  ?  386  ALA A HB1    1 
ATOM   5902  H HB2    . ALA A 1 386 ? -15.195 -21.494 -13.186 1.00 18.50  ?  386  ALA A HB2    1 
ATOM   5903  H HB3    . ALA A 1 386 ? -15.937 -22.498 -12.204 1.00 18.50  ?  386  ALA A HB3    1 
ATOM   5904  N N      . LEU A 1 387 ? -19.064 -21.011 -12.853 1.00 14.01  ?  387  LEU A N      1 
ATOM   5905  C CA     . LEU A 1 387 ? -20.433 -21.491 -12.786 1.00 14.43  ?  387  LEU A CA     1 
ATOM   5906  C C      . LEU A 1 387 ? -20.574 -22.554 -13.865 1.00 14.39  ?  387  LEU A C      1 
ATOM   5907  O O      . LEU A 1 387 ? -20.356 -22.266 -15.052 1.00 16.21  ?  387  LEU A O      1 
ATOM   5908  C CB     . LEU A 1 387 ? -21.412 -20.362 -13.069 1.00 14.76  ?  387  LEU A CB     1 
ATOM   5909  C CG     . LEU A 1 387 ? -21.336 -19.107 -12.211 1.00 16.17  ?  387  LEU A CG     1 
ATOM   5910  C CD1    . LEU A 1 387 ? -22.308 -18.069 -12.756 1.00 17.98  ?  387  LEU A CD1    1 
ATOM   5911  C CD2    . LEU A 1 387 ? -21.667 -19.426 -10.760 1.00 17.70  ?  387  LEU A CD2    1 
ATOM   5912  H H      . LEU A 1 387 ? -18.869 -20.679 -13.622 1.00 16.81  ?  387  LEU A H      1 
ATOM   5913  H HA     . LEU A 1 387 ? -20.623 -21.862 -11.910 1.00 17.31  ?  387  LEU A HA     1 
ATOM   5914  H HB2    . LEU A 1 387 ? -21.276 -20.079 -13.986 1.00 17.71  ?  387  LEU A HB2    1 
ATOM   5915  H HB3    . LEU A 1 387 ? -22.308 -20.717 -12.960 1.00 17.71  ?  387  LEU A HB3    1 
ATOM   5916  H HG     . LEU A 1 387 ? -20.436 -18.748 -12.237 1.00 19.40  ?  387  LEU A HG     1 
ATOM   5917  H HD11   . LEU A 1 387 ? -22.260 -17.272 -12.205 1.00 21.57  ?  387  LEU A HD11   1 
ATOM   5918  H HD12   . LEU A 1 387 ? -22.061 -17.854 -13.669 1.00 21.57  ?  387  LEU A HD12   1 
ATOM   5919  H HD13   . LEU A 1 387 ? -23.206 -18.434 -12.733 1.00 21.57  ?  387  LEU A HD13   1 
ATOM   5920  H HD21   . LEU A 1 387 ? -21.640 -18.607 -10.242 1.00 21.24  ?  387  LEU A HD21   1 
ATOM   5921  H HD22   . LEU A 1 387 ? -22.555 -19.815 -10.717 1.00 21.24  ?  387  LEU A HD22   1 
ATOM   5922  H HD23   . LEU A 1 387 ? -21.013 -20.056 -10.419 1.00 21.24  ?  387  LEU A HD23   1 
ATOM   5923  N N      . GLU A 1 388 ? -20.931 -23.772 -13.472 1.00 15.63  ?  388  GLU A N      1 
ATOM   5924  C CA     . GLU A 1 388 ? -21.182 -24.838 -14.439 1.00 15.22  ?  388  GLU A CA     1 
ATOM   5925  C C      . GLU A 1 388 ? -22.691 -25.052 -14.533 1.00 16.83  ?  388  GLU A C      1 
ATOM   5926  O O      . GLU A 1 388 ? -23.354 -25.290 -13.520 1.00 16.98  ?  388  GLU A O      1 
ATOM   5927  C CB     . GLU A 1 388 ? -20.447 -26.133 -14.085 1.00 14.65  ?  388  GLU A CB     1 
ATOM   5928  C CG     . GLU A 1 388 ? -20.661 -27.183 -15.160 1.00 15.92  ?  388  GLU A CG     1 
ATOM   5929  C CD     . GLU A 1 388 ? -19.610 -28.280 -15.182 1.00 16.10  ?  388  GLU A CD     1 
ATOM   5930  O OE1    . GLU A 1 388 ? -18.680 -28.249 -14.352 1.00 15.90  ?  388  GLU A OE1    1 
ATOM   5931  O OE2    . GLU A 1 388 ? -19.739 -29.171 -16.040 1.00 16.85  -1 388  GLU A OE2    1 
ATOM   5932  H H      . GLU A 1 388 ? -21.033 -24.004 -12.650 1.00 18.75  ?  388  GLU A H      1 
ATOM   5933  H HA     . GLU A 1 388 ? -20.853 -24.565 -15.310 1.00 18.26  ?  388  GLU A HA     1 
ATOM   5934  H HB2    . GLU A 1 388 ? -19.497 -25.956 -14.011 1.00 17.57  ?  388  GLU A HB2    1 
ATOM   5935  H HB3    . GLU A 1 388 ? -20.787 -26.479 -13.244 1.00 17.57  ?  388  GLU A HB3    1 
ATOM   5936  H HG2    . GLU A 1 388 ? -21.522 -27.605 -15.015 1.00 19.10  ?  388  GLU A HG2    1 
ATOM   5937  H HG3    . GLU A 1 388 ? -20.647 -26.747 -16.026 1.00 19.10  ?  388  GLU A HG3    1 
ATOM   5938  N N      . PHE A 1 389 ? -23.229 -24.932 -15.745 1.00 16.89  ?  389  PHE A N      1 
ATOM   5939  C CA     . PHE A 1 389 ? -24.673 -24.946 -15.963 1.00 18.18  ?  389  PHE A CA     1 
ATOM   5940  C C      . PHE A 1 389 ? -25.210 -26.363 -16.129 1.00 19.38  ?  389  PHE A C      1 
ATOM   5941  O O      . PHE A 1 389 ? -24.499 -27.274 -16.542 1.00 19.49  ?  389  PHE A O      1 
ATOM   5942  C CB     . PHE A 1 389 ? -25.004 -24.054 -17.159 1.00 16.46  ?  389  PHE A CB     1 
ATOM   5943  C CG     . PHE A 1 389 ? -24.445 -22.671 -16.998 1.00 14.78  ?  389  PHE A CG     1 
ATOM   5944  C CD1    . PHE A 1 389 ? -24.912 -21.869 -15.974 1.00 15.19  ?  389  PHE A CD1    1 
ATOM   5945  C CD2    . PHE A 1 389 ? -23.411 -22.219 -17.790 1.00 16.62  ?  389  PHE A CD2    1 
ATOM   5946  C CE1    . PHE A 1 389 ? -24.395 -20.607 -15.753 1.00 15.21  ?  389  PHE A CE1    1 
ATOM   5947  C CE2    . PHE A 1 389 ? -22.860 -20.962 -17.578 1.00 15.38  ?  389  PHE A CE2    1 
ATOM   5948  C CZ     . PHE A 1 389 ? -23.346 -20.149 -16.548 1.00 15.35  ?  389  PHE A CZ     1 
ATOM   5949  H H      . PHE A 1 389 ? -22.772 -24.839 -16.468 1.00 20.26  ?  389  PHE A H      1 
ATOM   5950  H HA     . PHE A 1 389 ? -25.137 -24.595 -15.186 1.00 21.82  ?  389  PHE A HA     1 
ATOM   5951  H HB2    . PHE A 1 389 ? -24.625 -24.443 -17.962 1.00 19.75  ?  389  PHE A HB2    1 
ATOM   5952  H HB3    . PHE A 1 389 ? -25.968 -23.983 -17.247 1.00 19.75  ?  389  PHE A HB3    1 
ATOM   5953  H HD1    . PHE A 1 389 ? -25.589 -22.187 -15.421 1.00 18.23  ?  389  PHE A HD1    1 
ATOM   5954  H HD2    . PHE A 1 389 ? -23.080 -22.760 -18.470 1.00 19.94  ?  389  PHE A HD2    1 
ATOM   5955  H HE1    . PHE A 1 389 ? -24.744 -20.068 -15.080 1.00 18.25  ?  389  PHE A HE1    1 
ATOM   5956  H HE2    . PHE A 1 389 ? -22.168 -20.661 -18.121 1.00 18.45  ?  389  PHE A HE2    1 
ATOM   5957  H HZ     . PHE A 1 389 ? -22.972 -19.311 -16.395 1.00 18.41  ?  389  PHE A HZ     1 
ATOM   5958  N N      . SER A 1 390 ? -26.486 -26.536 -15.781 1.00 17.91  ?  390  SER A N      1 
ATOM   5959  C CA     . SER A 1 390 ? -27.139 -27.839 -15.797 1.00 18.03  ?  390  SER A CA     1 
ATOM   5960  C C      . SER A 1 390 ? -28.626 -27.645 -16.016 1.00 19.89  ?  390  SER A C      1 
ATOM   5961  O O      . SER A 1 390 ? -29.198 -26.678 -15.496 1.00 21.60  ?  390  SER A O      1 
ATOM   5962  C CB     . SER A 1 390 ? -26.913 -28.556 -14.457 1.00 20.50  ?  390  SER A CB     1 
ATOM   5963  O OG     . SER A 1 390 ? -27.741 -29.697 -14.320 1.00 23.85  ?  390  SER A OG     1 
ATOM   5964  H H      . SER A 1 390 ? -27.003 -25.898 -15.526 1.00 21.49  ?  390  SER A H      1 
ATOM   5965  H HA     . SER A 1 390 ? -26.797 -28.374 -16.530 1.00 21.63  ?  390  SER A HA     1 
ATOM   5966  H HB2    . SER A 1 390 ? -25.986 -28.836 -14.407 1.00 24.59  ?  390  SER A HB2    1 
ATOM   5967  H HB3    . SER A 1 390 ? -27.112 -27.938 -13.736 1.00 24.59  ?  390  SER A HB3    1 
ATOM   5968  H HG     . SER A 1 390 ? -27.498 -30.295 -14.858 1.00 28.62  ?  390  SER A HG     1 
ATOM   5969  N N      . PRO A 1 391 ? -29.273 -28.529 -16.778 1.00 23.24  ?  391  PRO A N      1 
ATOM   5970  C CA     . PRO A 1 391 ? -30.740 -28.490 -16.868 1.00 23.97  ?  391  PRO A CA     1 
ATOM   5971  C C      . PRO A 1 391 ? -31.421 -29.057 -15.636 1.00 26.42  ?  391  PRO A C      1 
ATOM   5972  O O      . PRO A 1 391 ? -32.640 -28.902 -15.485 1.00 28.93  ?  391  PRO A O      1 
ATOM   5973  C CB     . PRO A 1 391 ? -31.028 -29.375 -18.087 1.00 24.99  ?  391  PRO A CB     1 
ATOM   5974  C CG     . PRO A 1 391 ? -29.870 -30.352 -18.096 1.00 25.46  ?  391  PRO A CG     1 
ATOM   5975  C CD     . PRO A 1 391 ? -28.685 -29.572 -17.639 1.00 25.47  ?  391  PRO A CD     1 
ATOM   5976  H HA     . PRO A 1 391 ? -31.053 -27.588 -17.042 1.00 28.76  ?  391  PRO A HA     1 
ATOM   5977  H HB2    . PRO A 1 391 ? -31.876 -29.833 -17.977 1.00 29.98  ?  391  PRO A HB2    1 
ATOM   5978  H HB3    . PRO A 1 391 ? -31.044 -28.839 -18.896 1.00 29.98  ?  391  PRO A HB3    1 
ATOM   5979  H HG2    . PRO A 1 391 ? -30.055 -31.086 -17.488 1.00 30.55  ?  391  PRO A HG2    1 
ATOM   5980  H HG3    . PRO A 1 391 ? -29.734 -30.692 -18.994 1.00 30.55  ?  391  PRO A HG3    1 
ATOM   5981  H HD2    . PRO A 1 391 ? -28.076 -30.133 -17.133 1.00 30.56  ?  391  PRO A HD2    1 
ATOM   5982  H HD3    . PRO A 1 391 ? -28.221 -29.175 -18.393 1.00 30.56  ?  391  PRO A HD3    1 
ATOM   5983  N N      . ALA A 1 392 ? -30.667 -29.707 -14.760 1.00 26.13  ?  392  ALA A N      1 
ATOM   5984  C CA     . ALA A 1 392 ? -31.219 -30.322 -13.551 1.00 27.36  ?  392  ALA A CA     1 
ATOM   5985  C C      . ALA A 1 392 ? -30.096 -30.384 -12.536 1.00 26.19  ?  392  ALA A C      1 
ATOM   5986  O O      . ALA A 1 392 ? -29.439 -31.417 -12.370 1.00 25.67  ?  392  ALA A O      1 
ATOM   5987  C CB     . ALA A 1 392 ? -31.781 -31.714 -13.840 1.00 29.72  ?  392  ALA A CB     1 
ATOM   5988  H H      . ALA A 1 392 ? -29.817 -29.810 -14.841 1.00 31.35  ?  392  ALA A H      1 
ATOM   5989  H HA     . ALA A 1 392 ? -31.945 -29.785 -13.198 1.00 32.83  ?  392  ALA A HA     1 
ATOM   5990  H HB1    . ALA A 1 392 ? -32.179 -32.068 -13.029 1.00 35.67  ?  392  ALA A HB1    1 
ATOM   5991  H HB2    . ALA A 1 392 ? -32.453 -31.646 -14.536 1.00 35.67  ?  392  ALA A HB2    1 
ATOM   5992  H HB3    . ALA A 1 392 ? -31.059 -32.291 -14.134 1.00 35.67  ?  392  ALA A HB3    1 
ATOM   5993  N N      . PRO A 1 393 ? -29.810 -29.265 -11.867 1.00 25.02  ?  393  PRO A N      1 
ATOM   5994  C CA     . PRO A 1 393 ? -28.686 -29.237 -10.917 1.00 25.40  ?  393  PRO A CA     1 
ATOM   5995  C C      . PRO A 1 393 ? -28.644 -30.393 -9.934  1.00 28.36  ?  393  PRO A C      1 
ATOM   5996  O O      . PRO A 1 393 ? -27.567 -30.951 -9.681  1.00 28.36  ?  393  PRO A O      1 
ATOM   5997  C CB     . PRO A 1 393 ? -28.887 -27.890 -10.210 1.00 24.55  ?  393  PRO A CB     1 
ATOM   5998  C CG     . PRO A 1 393 ? -29.498 -27.021 -11.266 1.00 25.61  ?  393  PRO A CG     1 
ATOM   5999  C CD     . PRO A 1 393 ? -30.420 -27.928 -12.052 1.00 25.13  ?  393  PRO A CD     1 
ATOM   6000  H HA     . PRO A 1 393 ? -27.852 -29.237 -11.413 1.00 30.48  ?  393  PRO A HA     1 
ATOM   6001  H HB2    . PRO A 1 393 ? -29.484 -27.995 -9.452  1.00 29.45  ?  393  PRO A HB2    1 
ATOM   6002  H HB3    . PRO A 1 393 ? -28.034 -27.537 -9.914  1.00 29.45  ?  393  PRO A HB3    1 
ATOM   6003  H HG2    . PRO A 1 393 ? -29.996 -26.299 -10.850 1.00 30.72  ?  393  PRO A HG2    1 
ATOM   6004  H HG3    . PRO A 1 393 ? -28.802 -26.658 -11.836 1.00 30.72  ?  393  PRO A HG3    1 
ATOM   6005  H HD2    . PRO A 1 393 ? -31.320 -27.905 -11.690 1.00 30.15  ?  393  PRO A HD2    1 
ATOM   6006  H HD3    . PRO A 1 393 ? -30.434 -27.680 -12.990 1.00 30.15  ?  393  PRO A HD3    1 
ATOM   6007  N N      . ALA A 1 394 ? -29.784 -30.783 -9.370  1.00 30.40  ?  394  ALA A N      1 
ATOM   6008  C CA     . ALA A 1 394 ? -29.760 -31.812 -8.336  1.00 33.41  ?  394  ALA A CA     1 
ATOM   6009  C C      . ALA A 1 394 ? -29.285 -33.157 -8.871  1.00 35.02  ?  394  ALA A C      1 
ATOM   6010  O O      . ALA A 1 394 ? -28.926 -34.036 -8.080  1.00 36.33  ?  394  ALA A O      1 
ATOM   6011  C CB     . ALA A 1 394 ? -31.141 -31.943 -7.694  1.00 32.55  ?  394  ALA A CB     1 
ATOM   6012  H H      . ALA A 1 394 ? -30.564 -30.477 -9.561  1.00 36.48  ?  394  ALA A H      1 
ATOM   6013  H HA     . ALA A 1 394 ? -29.140 -31.543 -7.640  1.00 40.09  ?  394  ALA A HA     1 
ATOM   6014  H HB1    . ALA A 1 394 ? -31.119 -32.658 -7.039  1.00 39.06  ?  394  ALA A HB1    1 
ATOM   6015  H HB2    . ALA A 1 394 ? -31.370 -31.105 -7.262  1.00 39.06  ?  394  ALA A HB2    1 
ATOM   6016  H HB3    . ALA A 1 394 ? -31.792 -32.147 -8.384  1.00 39.06  ?  394  ALA A HB3    1 
ATOM   6017  N N      . ARG A 1 395 ? -29.275 -33.345 -10.187 1.00 36.19  ?  395  ARG A N      1 
ATOM   6018  C CA     . ARG A 1 395 ? -28.796 -34.583 -10.785 1.00 37.68  ?  395  ARG A CA     1 
ATOM   6019  C C      . ARG A 1 395 ? -27.429 -34.445 -11.439 1.00 35.95  ?  395  ARG A C      1 
ATOM   6020  O O      . ARG A 1 395 ? -26.940 -35.415 -12.040 1.00 36.96  ?  395  ARG A O      1 
ATOM   6021  C CB     . ARG A 1 395 ? -29.807 -35.087 -11.817 1.00 44.06  ?  395  ARG A CB     1 
ATOM   6022  C CG     . ARG A 1 395 ? -31.152 -35.463 -11.230 1.00 50.48  ?  395  ARG A CG     1 
ATOM   6023  C CD     . ARG A 1 395 ? -32.085 -35.997 -12.308 1.00 57.72  ?  395  ARG A CD     1 
ATOM   6024  N NE     . ARG A 1 395 ? -33.376 -36.384 -11.753 1.00 64.91  ?  395  ARG A NE     1 
ATOM   6025  C CZ     . ARG A 1 395 ? -34.387 -36.872 -12.465 1.00 70.11  ?  395  ARG A CZ     1 
ATOM   6026  N NH1    . ARG A 1 395 ? -35.524 -37.194 -11.861 1.00 72.07  ?  395  ARG A NH1    1 
ATOM   6027  N NH2    . ARG A 1 395 ? -34.266 -37.039 -13.778 1.00 72.11  ?  395  ARG A NH2    1 
ATOM   6028  H H      . ARG A 1 395 ? -29.544 -32.762 -10.759 1.00 43.42  ?  395  ARG A H      1 
ATOM   6029  H HA     . ARG A 1 395 ? -28.718 -35.250 -10.085 1.00 45.22  ?  395  ARG A HA     1 
ATOM   6030  H HB2    . ARG A 1 395 ? -29.956 -34.388 -12.473 1.00 52.86  ?  395  ARG A HB2    1 
ATOM   6031  H HB3    . ARG A 1 395 ? -29.443 -35.876 -12.249 1.00 52.86  ?  395  ARG A HB3    1 
ATOM   6032  H HG2    . ARG A 1 395 ? -31.031 -36.152 -10.558 1.00 60.57  ?  395  ARG A HG2    1 
ATOM   6033  H HG3    . ARG A 1 395 ? -31.561 -34.679 -10.830 1.00 60.57  ?  395  ARG A HG3    1 
ATOM   6034  H HD2    . ARG A 1 395 ? -32.234 -35.308 -12.975 1.00 69.26  ?  395  ARG A HD2    1 
ATOM   6035  H HD3    . ARG A 1 395 ? -31.684 -36.778 -12.722 1.00 69.26  ?  395  ARG A HD3    1 
ATOM   6036  H HE     . ARG A 1 395 ? -33.491 -36.291 -10.906 1.00 77.89  ?  395  ARG A HE     1 
ATOM   6037  H HH11   . ARG A 1 395 ? -35.605 -37.087 -11.011 1.00 86.48  ?  395  ARG A HH11   1 
ATOM   6038  H HH12   . ARG A 1 395 ? -36.180 -37.510 -12.318 1.00 86.48  ?  395  ARG A HH12   1 
ATOM   6039  H HH21   . ARG A 1 395 ? -33.530 -36.831 -14.172 1.00 86.53  ?  395  ARG A HH21   1 
ATOM   6040  H HH22   . ARG A 1 395 ? -34.923 -37.355 -14.234 1.00 86.53  ?  395  ARG A HH22   1 
ATOM   6041  N N      . ARG A 1 396 ? -26.793 -33.281 -11.338 1.00 30.56  ?  396  ARG A N      1 
ATOM   6042  C CA     . ARG A 1 396 ? -25.518 -33.034 -12.011 1.00 28.55  ?  396  ARG A CA     1 
ATOM   6043  C C      . ARG A 1 396 ? -25.624 -33.318 -13.504 1.00 31.24  ?  396  ARG A C      1 
ATOM   6044  O O      . ARG A 1 396 ? -24.656 -33.758 -14.136 1.00 33.25  ?  396  ARG A O      1 
ATOM   6045  C CB     . ARG A 1 396 ? -24.376 -33.836 -11.385 1.00 26.61  ?  396  ARG A CB     1 
ATOM   6046  C CG     . ARG A 1 396 ? -24.180 -33.548 -9.935  1.00 24.93  ?  396  ARG A CG     1 
ATOM   6047  C CD     . ARG A 1 396 ? -22.887 -34.140 -9.428  1.00 22.69  ?  396  ARG A CD     1 
ATOM   6048  N NE     . ARG A 1 396 ? -22.950 -35.592 -9.337  1.00 20.69  ?  396  ARG A NE     1 
ATOM   6049  C CZ     . ARG A 1 396 ? -22.195 -36.437 -10.031 1.00 20.76  ?  396  ARG A CZ     1 
ATOM   6050  N NH1    . ARG A 1 396 ? -21.288 -36.000 -10.891 1.00 22.73  ?  396  ARG A NH1    1 
ATOM   6051  N NH2    . ARG A 1 396 ? -22.345 -37.742 -9.839  1.00 22.74  ?  396  ARG A NH2    1 
ATOM   6052  H H      . ARG A 1 396 ? -27.082 -32.612 -10.881 1.00 36.67  ?  396  ARG A H      1 
ATOM   6053  H HA     . ARG A 1 396 ? -25.299 -32.095 -11.902 1.00 34.25  ?  396  ARG A HA     1 
ATOM   6054  H HB2    . ARG A 1 396 ? -24.570 -34.782 -11.477 1.00 31.93  ?  396  ARG A HB2    1 
ATOM   6055  H HB3    . ARG A 1 396 ? -23.550 -33.620 -11.846 1.00 31.93  ?  396  ARG A HB3    1 
ATOM   6056  H HG2    . ARG A 1 396 ? -24.151 -32.588 -9.799  1.00 29.91  ?  396  ARG A HG2    1 
ATOM   6057  H HG3    . ARG A 1 396 ? -24.912 -33.933 -9.429  1.00 29.91  ?  396  ARG A HG3    1 
ATOM   6058  H HD2    . ARG A 1 396 ? -22.169 -33.904 -10.035 1.00 27.22  ?  396  ARG A HD2    1 
ATOM   6059  H HD3    . ARG A 1 396 ? -22.702 -33.789 -8.543  1.00 27.22  ?  396  ARG A HD3    1 
ATOM   6060  H HE     . ARG A 1 396 ? -23.521 -35.930 -8.791  1.00 24.83  ?  396  ARG A HE     1 
ATOM   6061  H HH11   . ARG A 1 396 ? -21.179 -35.155 -11.009 1.00 27.27  ?  396  ARG A HH11   1 
ATOM   6062  H HH12   . ARG A 1 396 ? -20.808 -36.561 -11.331 1.00 27.27  ?  396  ARG A HH12   1 
ATOM   6063  H HH21   . ARG A 1 396 ? -22.924 -38.029 -9.272  1.00 27.29  ?  396  ARG A HH21   1 
ATOM   6064  H HH22   . ARG A 1 396 ? -21.862 -38.300 -10.281 1.00 27.29  ?  396  ARG A HH22   1 
ATOM   6065  N N      . ALA A 1 397 ? -26.794 -33.030 -14.078 1.00 30.00  ?  397  ALA A N      1 
ATOM   6066  C CA     . ALA A 1 397 ? -27.030 -33.308 -15.481 1.00 29.37  ?  397  ALA A CA     1 
ATOM   6067  C C      . ALA A 1 397 ? -26.270 -32.314 -16.344 1.00 26.08  ?  397  ALA A C      1 
ATOM   6068  O O      . ALA A 1 397 ? -26.000 -31.175 -15.936 1.00 25.56  ?  397  ALA A O      1 
ATOM   6069  C CB     . ALA A 1 397 ? -28.523 -33.207 -15.793 1.00 28.78  ?  397  ALA A CB     1 
ATOM   6070  H H      . ALA A 1 397 ? -27.464 -32.674 -13.672 1.00 35.99  ?  397  ALA A H      1 
ATOM   6071  H HA     . ALA A 1 397 ? -26.730 -34.206 -15.693 1.00 35.24  ?  397  ALA A HA     1 
ATOM   6072  H HB1    . ALA A 1 397 ? -28.659 -33.367 -16.740 1.00 34.54  ?  397  ALA A HB1    1 
ATOM   6073  H HB2    . ALA A 1 397 ? -29.000 -33.873 -15.274 1.00 34.54  ?  397  ALA A HB2    1 
ATOM   6074  H HB3    . ALA A 1 397 ? -28.835 -32.319 -15.560 1.00 34.54  ?  397  ALA A HB3    1 
ATOM   6075  N N      . PHE A 1 398 ? -25.911 -32.757 -17.544 1.00 27.88  ?  398  PHE A N      1 
ATOM   6076  C CA     . PHE A 1 398 ? -25.247 -31.913 -18.527 1.00 29.99  ?  398  PHE A CA     1 
ATOM   6077  C C      . PHE A 1 398 ? -26.234 -31.565 -19.636 1.00 29.00  ?  398  PHE A C      1 
ATOM   6078  O O      . PHE A 1 398 ? -27.091 -32.378 -20.003 1.00 28.12  ?  398  PHE A O      1 
ATOM   6079  C CB     . PHE A 1 398 ? -24.086 -32.648 -19.219 1.00 32.83  ?  398  PHE A CB     1 
ATOM   6080  C CG     . PHE A 1 398 ? -22.957 -33.021 -18.314 1.00 37.26  ?  398  PHE A CG     1 
ATOM   6081  C CD1    . PHE A 1 398 ? -22.509 -32.152 -17.321 1.00 37.22  ?  398  PHE A CD1    1 
ATOM   6082  C CD2    . PHE A 1 398 ? -22.314 -34.239 -18.473 1.00 40.34  ?  398  PHE A CD2    1 
ATOM   6083  C CE1    . PHE A 1 398 ? -21.464 -32.506 -16.506 1.00 37.75  ?  398  PHE A CE1    1 
ATOM   6084  C CE2    . PHE A 1 398 ? -21.261 -34.598 -17.656 1.00 41.04  ?  398  PHE A CE2    1 
ATOM   6085  C CZ     . PHE A 1 398 ? -20.833 -33.733 -16.677 1.00 39.28  ?  398  PHE A CZ     1 
ATOM   6086  H H      . PHE A 1 398 ? -26.045 -33.562 -17.815 1.00 33.45  ?  398  PHE A H      1 
ATOM   6087  H HA     . PHE A 1 398 ? -24.919 -31.121 -18.075 1.00 35.98  ?  398  PHE A HA     1 
ATOM   6088  H HB2    . PHE A 1 398 ? -24.428 -33.466 -19.611 1.00 39.39  ?  398  PHE A HB2    1 
ATOM   6089  H HB3    . PHE A 1 398 ? -23.727 -32.072 -19.912 1.00 39.39  ?  398  PHE A HB3    1 
ATOM   6090  H HD1    . PHE A 1 398 ? -22.922 -31.326 -17.210 1.00 44.66  ?  398  PHE A HD1    1 
ATOM   6091  H HD2    . PHE A 1 398 ? -22.597 -34.822 -19.140 1.00 48.41  ?  398  PHE A HD2    1 
ATOM   6092  H HE1    . PHE A 1 398 ? -21.178 -31.925 -15.838 1.00 45.29  ?  398  PHE A HE1    1 
ATOM   6093  H HE2    . PHE A 1 398 ? -20.842 -35.421 -17.768 1.00 49.24  ?  398  PHE A HE2    1 
ATOM   6094  H HZ     . PHE A 1 398 ? -20.120 -33.969 -16.128 1.00 47.13  ?  398  PHE A HZ     1 
ATOM   6095  N N      . PHE A 1 399 ? -26.083 -30.371 -20.200 1.00 28.01  ?  399  PHE A N      1 
ATOM   6096  C CA     . PHE A 1 399 ? -26.878 -30.004 -21.358 1.00 24.84  ?  399  PHE A CA     1 
ATOM   6097  C C      . PHE A 1 399 ? -26.355 -30.716 -22.607 1.00 25.30  ?  399  PHE A C      1 
ATOM   6098  O O      . PHE A 1 399 ? -25.187 -31.097 -22.693 1.00 27.54  ?  399  PHE A O      1 
ATOM   6099  C CB     . PHE A 1 399 ? -26.784 -28.500 -21.626 1.00 24.48  ?  399  PHE A CB     1 
ATOM   6100  C CG     . PHE A 1 399 ? -27.693 -27.659 -20.784 1.00 22.06  ?  399  PHE A CG     1 
ATOM   6101  C CD1    . PHE A 1 399 ? -29.046 -27.596 -21.049 1.00 22.25  ?  399  PHE A CD1    1 
ATOM   6102  C CD2    . PHE A 1 399 ? -27.180 -26.882 -19.752 1.00 21.27  ?  399  PHE A CD2    1 
ATOM   6103  C CE1    . PHE A 1 399 ? -29.875 -26.798 -20.276 1.00 20.96  ?  399  PHE A CE1    1 
ATOM   6104  C CE2    . PHE A 1 399 ? -28.009 -26.090 -18.989 1.00 20.70  ?  399  PHE A CE2    1 
ATOM   6105  C CZ     . PHE A 1 399 ? -29.350 -26.056 -19.248 1.00 20.11  ?  399  PHE A CZ     1 
ATOM   6106  H H      . PHE A 1 399 ? -25.534 -29.766 -19.933 1.00 33.61  ?  399  PHE A H      1 
ATOM   6107  H HA     . PHE A 1 399 ? -27.800 -30.251 -21.187 1.00 29.81  ?  399  PHE A HA     1 
ATOM   6108  H HB2    . PHE A 1 399 ? -25.875 -28.212 -21.452 1.00 29.38  ?  399  PHE A HB2    1 
ATOM   6109  H HB3    . PHE A 1 399 ? -27.013 -28.338 -22.555 1.00 29.38  ?  399  PHE A HB3    1 
ATOM   6110  H HD1    . PHE A 1 399 ? -29.404 -28.092 -21.749 1.00 26.70  ?  399  PHE A HD1    1 
ATOM   6111  H HD2    . PHE A 1 399 ? -26.268 -26.898 -19.574 1.00 25.52  ?  399  PHE A HD2    1 
ATOM   6112  H HE1    . PHE A 1 399 ? -30.787 -26.765 -20.455 1.00 25.14  ?  399  PHE A HE1    1 
ATOM   6113  H HE2    . PHE A 1 399 ? -27.655 -25.577 -18.298 1.00 24.83  ?  399  PHE A HE2    1 
ATOM   6114  H HZ     . PHE A 1 399 ? -29.910 -25.528 -18.725 1.00 24.13  ?  399  PHE A HZ     1 
ATOM   6115  N N      . ASP A 1 400 ? -27.228 -30.880 -23.586 1.00 27.31  ?  400  ASP A N      1 
ATOM   6116  C CA     . ASP A 1 400 ? -26.791 -31.225 -24.934 1.00 28.78  ?  400  ASP A CA     1 
ATOM   6117  C C      . ASP A 1 400 ? -25.776 -30.174 -25.369 1.00 27.97  ?  400  ASP A C      1 
ATOM   6118  O O      . ASP A 1 400 ? -26.112 -28.989 -25.390 1.00 27.14  ?  400  ASP A O      1 
ATOM   6119  C CB     . ASP A 1 400 ? -28.013 -31.202 -25.852 1.00 31.46  ?  400  ASP A CB     1 
ATOM   6120  C CG     . ASP A 1 400 ? -27.678 -31.529 -27.302 1.00 34.49  ?  400  ASP A CG     1 
ATOM   6121  O OD1    . ASP A 1 400 ? -26.492 -31.643 -27.661 1.00 34.95  ?  400  ASP A OD1    1 
ATOM   6122  O OD2    . ASP A 1 400 ? -28.617 -31.666 -28.103 1.00 40.09  -1 400  ASP A OD2    1 
ATOM   6123  H H      . ASP A 1 400 ? -28.080 -30.798 -23.501 1.00 32.76  ?  400  ASP A H      1 
ATOM   6124  H HA     . ASP A 1 400 ? -26.385 -32.105 -24.980 1.00 34.53  ?  400  ASP A HA     1 
ATOM   6125  H HB2    . ASP A 1 400 ? -28.655 -31.858 -25.538 1.00 37.75  ?  400  ASP A HB2    1 
ATOM   6126  H HB3    . ASP A 1 400 ? -28.407 -30.316 -25.829 1.00 37.75  ?  400  ASP A HB3    1 
ATOM   6127  N N      . PRO A 1 401 ? -24.533 -30.551 -25.693 1.00 27.91  ?  401  PRO A N      1 
ATOM   6128  C CA     . PRO A 1 401 ? -23.546 -29.524 -26.077 1.00 27.78  ?  401  PRO A CA     1 
ATOM   6129  C C      . PRO A 1 401 ? -23.983 -28.653 -27.237 1.00 27.34  ?  401  PRO A C      1 
ATOM   6130  O O      . PRO A 1 401 ? -23.530 -27.504 -27.339 1.00 25.96  ?  401  PRO A O      1 
ATOM   6131  C CB     . PRO A 1 401 ? -22.293 -30.343 -26.425 1.00 28.16  ?  401  PRO A CB     1 
ATOM   6132  C CG     . PRO A 1 401 ? -22.457 -31.629 -25.657 1.00 29.43  ?  401  PRO A CG     1 
ATOM   6133  C CD     . PRO A 1 401 ? -23.944 -31.907 -25.670 1.00 27.73  ?  401  PRO A CD     1 
ATOM   6134  H HA     . PRO A 1 401 ? -23.358 -28.959 -25.312 1.00 33.33  ?  401  PRO A HA     1 
ATOM   6135  H HB2    . PRO A 1 401 ? -22.259 -30.509 -27.380 1.00 33.79  ?  401  PRO A HB2    1 
ATOM   6136  H HB3    . PRO A 1 401 ? -21.496 -29.867 -26.143 1.00 33.79  ?  401  PRO A HB3    1 
ATOM   6137  H HG2    . PRO A 1 401 ? -21.968 -32.342 -26.096 1.00 35.31  ?  401  PRO A HG2    1 
ATOM   6138  H HG3    . PRO A 1 401 ? -22.134 -31.515 -24.749 1.00 35.31  ?  401  PRO A HG3    1 
ATOM   6139  H HD2    . PRO A 1 401 ? -24.196 -32.408 -26.461 1.00 33.27  ?  401  PRO A HD2    1 
ATOM   6140  H HD3    . PRO A 1 401 ? -24.214 -32.388 -24.872 1.00 33.27  ?  401  PRO A HD3    1 
ATOM   6141  N N      . ALA A 1 402 ? -24.867 -29.154 -28.099 1.00 27.78  ?  402  ALA A N      1 
ATOM   6142  C CA     . ALA A 1 402 ? -25.299 -28.392 -29.261 1.00 27.96  ?  402  ALA A CA     1 
ATOM   6143  C C      . ALA A 1 402 ? -26.069 -27.142 -28.881 1.00 26.71  ?  402  ALA A C      1 
ATOM   6144  O O      . ALA A 1 402 ? -26.151 -26.211 -29.692 1.00 28.05  ?  402  ALA A O      1 
ATOM   6145  C CB     . ALA A 1 402 ? -26.175 -29.258 -30.167 1.00 28.88  ?  402  ALA A CB     1 
ATOM   6146  H H      . ALA A 1 402 ? -25.230 -29.931 -28.033 1.00 33.33  ?  402  ALA A H      1 
ATOM   6147  H HA     . ALA A 1 402 ? -24.508 -28.128 -29.756 1.00 33.55  ?  402  ALA A HA     1 
ATOM   6148  H HB1    . ALA A 1 402 ? -26.452 -28.733 -30.934 1.00 34.66  ?  402  ALA A HB1    1 
ATOM   6149  H HB2    . ALA A 1 402 ? -25.663 -30.027 -30.460 1.00 34.66  ?  402  ALA A HB2    1 
ATOM   6150  H HB3    . ALA A 1 402 ? -26.954 -29.550 -29.668 1.00 34.66  ?  402  ALA A HB3    1 
ATOM   6151  N N      . LEU A 1 403 ? -26.640 -27.101 -27.675 1.00 25.04  ?  403  LEU A N      1 
ATOM   6152  C CA     . LEU A 1 403 ? -27.360 -25.915 -27.231 1.00 23.47  ?  403  LEU A CA     1 
ATOM   6153  C C      . LEU A 1 403 ? -26.433 -24.741 -26.937 1.00 22.84  ?  403  LEU A C      1 
ATOM   6154  O O      . LEU A 1 403 ? -26.909 -23.612 -26.821 1.00 21.01  ?  403  LEU A O      1 
ATOM   6155  C CB     . LEU A 1 403 ? -28.207 -26.224 -25.990 1.00 24.47  ?  403  LEU A CB     1 
ATOM   6156  C CG     . LEU A 1 403 ? -29.362 -27.212 -26.221 1.00 26.42  ?  403  LEU A CG     1 
ATOM   6157  C CD1    . LEU A 1 403 ? -30.067 -27.518 -24.921 1.00 28.21  ?  403  LEU A CD1    1 
ATOM   6158  C CD2    . LEU A 1 403 ? -30.358 -26.683 -27.245 1.00 29.00  ?  403  LEU A CD2    1 
ATOM   6159  H H      . LEU A 1 403 ? -26.625 -27.742 -27.102 1.00 30.04  ?  403  LEU A H      1 
ATOM   6160  H HA     . LEU A 1 403 ? -27.964 -25.651 -27.943 1.00 28.16  ?  403  LEU A HA     1 
ATOM   6161  H HB2    . LEU A 1 403 ? -27.628 -26.605 -25.311 1.00 29.36  ?  403  LEU A HB2    1 
ATOM   6162  H HB3    . LEU A 1 403 ? -28.593 -25.394 -25.668 1.00 29.36  ?  403  LEU A HB3    1 
ATOM   6163  H HG     . LEU A 1 403 ? -28.987 -28.034 -26.574 1.00 31.70  ?  403  LEU A HG     1 
ATOM   6164  H HD11   . LEU A 1 403 ? -30.762 -28.174 -25.085 1.00 33.85  ?  403  LEU A HD11   1 
ATOM   6165  H HD12   . LEU A 1 403 ? -29.422 -27.870 -24.287 1.00 33.85  ?  403  LEU A HD12   1 
ATOM   6166  H HD13   . LEU A 1 403 ? -30.458 -26.701 -24.574 1.00 33.85  ?  403  LEU A HD13   1 
ATOM   6167  H HD21   . LEU A 1 403 ? -31.172 -27.208 -27.194 1.00 34.79  ?  403  LEU A HD21   1 
ATOM   6168  H HD22   . LEU A 1 403 ? -30.550 -25.753 -27.048 1.00 34.79  ?  403  LEU A HD22   1 
ATOM   6169  H HD23   . LEU A 1 403 ? -29.971 -26.760 -28.131 1.00 34.79  ?  403  LEU A HD23   1 
ATOM   6170  N N      . LYS A 1 404 ? -25.133 -24.984 -26.786 1.00 21.40  ?  404  LYS A N      1 
ATOM   6171  C CA     . LYS A 1 404 ? -24.149 -23.918 -26.583 1.00 19.48  ?  404  LYS A CA     1 
ATOM   6172  C C      . LYS A 1 404 ? -24.492 -23.037 -25.381 1.00 18.29  ?  404  LYS A C      1 
ATOM   6173  O O      . LYS A 1 404 ? -24.332 -21.821 -25.421 1.00 18.32  ?  404  LYS A O      1 
ATOM   6174  C CB     . LYS A 1 404 ? -23.989 -23.063 -27.851 1.00 24.99  ?  404  LYS A CB     1 
ATOM   6175  C CG     . LYS A 1 404 ? -23.611 -23.853 -29.129 1.00 30.92  ?  404  LYS A CG     1 
ATOM   6176  C CD     . LYS A 1 404 ? -22.216 -24.428 -29.051 1.00 35.49  ?  404  LYS A CD     1 
ATOM   6177  C CE     . LYS A 1 404 ? -21.840 -25.210 -30.315 1.00 39.55  ?  404  LYS A CE     1 
ATOM   6178  N NZ     . LYS A 1 404 ? -20.611 -26.044 -30.102 1.00 43.55  ?  404  LYS A NZ     1 
ATOM   6179  H H      . LYS A 1 404 ? -24.789 -25.773 -26.798 1.00 25.67  ?  404  LYS A H      1 
ATOM   6180  H HA     . LYS A 1 404 ? -23.297 -24.339 -26.389 1.00 23.37  ?  404  LYS A HA     1 
ATOM   6181  H HB2    . LYS A 1 404 ? -24.830 -22.612 -28.026 1.00 29.99  ?  404  LYS A HB2    1 
ATOM   6182  H HB3    . LYS A 1 404 ? -23.289 -22.409 -27.695 1.00 29.99  ?  404  LYS A HB3    1 
ATOM   6183  H HG2    . LYS A 1 404 ? -24.234 -24.587 -29.246 1.00 37.10  ?  404  LYS A HG2    1 
ATOM   6184  H HG3    . LYS A 1 404 ? -23.651 -23.258 -29.894 1.00 37.10  ?  404  LYS A HG3    1 
ATOM   6185  H HD2    . LYS A 1 404 ? -21.579 -23.704 -28.943 1.00 42.59  ?  404  LYS A HD2    1 
ATOM   6186  H HD3    . LYS A 1 404 ? -22.163 -25.033 -28.295 1.00 42.59  ?  404  LYS A HD3    1 
ATOM   6187  H HE2    . LYS A 1 404 ? -22.571 -25.800 -30.557 1.00 47.46  ?  404  LYS A HE2    1 
ATOM   6188  H HE3    . LYS A 1 404 ? -21.664 -24.587 -31.038 1.00 47.46  ?  404  LYS A HE3    1 
ATOM   6189  H HZ1    . LYS A 1 404 ? -20.412 -26.490 -30.846 1.00 52.26  ?  404  LYS A HZ1    1 
ATOM   6190  H HZ2    . LYS A 1 404 ? -19.923 -25.523 -29.885 1.00 52.26  ?  404  LYS A HZ2    1 
ATOM   6191  H HZ3    . LYS A 1 404 ? -20.749 -26.628 -29.444 1.00 52.26  ?  404  LYS A HZ3    1 
ATOM   6192  N N      . VAL A 1 405 ? -24.934 -23.649 -24.282 1.00 16.36  ?  405  VAL A N      1 
ATOM   6193  C CA     . VAL A 1 405 ? -25.364 -22.860 -23.127 1.00 18.45  ?  405  VAL A CA     1 
ATOM   6194  C C      . VAL A 1 405 ? -24.233 -21.983 -22.599 1.00 16.13  ?  405  VAL A C      1 
ATOM   6195  O O      . VAL A 1 405 ? -24.426 -20.788 -22.342 1.00 16.26  ?  405  VAL A O      1 
ATOM   6196  C CB     . VAL A 1 405 ? -25.960 -23.764 -22.030 1.00 16.77  ?  405  VAL A CB     1 
ATOM   6197  C CG1    . VAL A 1 405 ? -26.277 -22.970 -20.787 1.00 19.15  ?  405  VAL A CG1    1 
ATOM   6198  C CG2    . VAL A 1 405 ? -27.216 -24.446 -22.547 1.00 18.14  ?  405  VAL A CG2    1 
ATOM   6199  H H      . VAL A 1 405 ? -24.993 -24.500 -24.179 1.00 19.62  ?  405  VAL A H      1 
ATOM   6200  H HA     . VAL A 1 405 ? -26.069 -22.264 -23.426 1.00 22.14  ?  405  VAL A HA     1 
ATOM   6201  H HB     . VAL A 1 405 ? -25.305 -24.440 -21.795 1.00 20.13  ?  405  VAL A HB     1 
ATOM   6202  H HG11   . VAL A 1 405 ? -26.826 -23.510 -20.198 1.00 22.97  ?  405  VAL A HG11   1 
ATOM   6203  H HG12   . VAL A 1 405 ? -25.448 -22.735 -20.342 1.00 22.97  ?  405  VAL A HG12   1 
ATOM   6204  H HG13   . VAL A 1 405 ? -26.756 -22.165 -21.040 1.00 22.97  ?  405  VAL A HG13   1 
ATOM   6205  H HG21   . VAL A 1 405 ? -27.651 -24.905 -21.811 1.00 21.77  ?  405  VAL A HG21   1 
ATOM   6206  H HG22   . VAL A 1 405 ? -27.811 -23.775 -22.916 1.00 21.77  ?  405  VAL A HG22   1 
ATOM   6207  H HG23   . VAL A 1 405 ? -26.969 -25.084 -23.234 1.00 21.77  ?  405  VAL A HG23   1 
ATOM   6208  N N      . GLY A 1 406 ? -23.055 -22.560 -22.389 1.00 17.73  ?  406  GLY A N      1 
ATOM   6209  C CA     . GLY A 1 406 ? -21.941 -21.796 -21.887 1.00 17.55  ?  406  GLY A CA     1 
ATOM   6210  C C      . GLY A 1 406 ? -21.576 -20.617 -22.776 1.00 16.86  ?  406  GLY A C      1 
ATOM   6211  O O      . GLY A 1 406 ? -21.507 -19.461 -22.336 1.00 15.64  ?  406  GLY A O      1 
ATOM   6212  H H      . GLY A 1 406 ? -22.885 -23.391 -22.532 1.00 21.27  ?  406  GLY A H      1 
ATOM   6213  H HA2    . GLY A 1 406 ? -22.161 -21.454 -21.006 1.00 21.05  ?  406  GLY A HA2    1 
ATOM   6214  H HA3    . GLY A 1 406 ? -21.165 -22.373 -21.816 1.00 21.05  ?  406  GLY A HA3    1 
ATOM   6215  N N      . PRO A 1 407 ? -21.311 -20.885 -24.055 1.00 17.44  ?  407  PRO A N      1 
ATOM   6216  C CA     . PRO A 1 407 ? -21.062 -19.768 -24.985 1.00 16.98  ?  407  PRO A CA     1 
ATOM   6217  C C      . PRO A 1 407 ? -22.173 -18.727 -24.988 1.00 16.23  ?  407  PRO A C      1 
ATOM   6218  O O      . PRO A 1 407 ? -21.898 -17.521 -25.068 1.00 16.86  ?  407  PRO A O      1 
ATOM   6219  C CB     . PRO A 1 407 ? -20.887 -20.480 -26.341 1.00 19.51  ?  407  PRO A CB     1 
ATOM   6220  C CG     . PRO A 1 407 ? -20.320 -21.847 -25.943 1.00 19.04  ?  407  PRO A CG     1 
ATOM   6221  C CD     . PRO A 1 407 ? -21.059 -22.200 -24.667 1.00 18.88  ?  407  PRO A CD     1 
ATOM   6222  H HA     . PRO A 1 407 ? -20.228 -19.325 -24.766 1.00 20.37  ?  407  PRO A HA     1 
ATOM   6223  H HB2    . PRO A 1 407 ? -21.743 -20.568 -26.790 1.00 23.41  ?  407  PRO A HB2    1 
ATOM   6224  H HB3    . PRO A 1 407 ? -20.267 -19.990 -26.903 1.00 23.41  ?  407  PRO A HB3    1 
ATOM   6225  H HG2    . PRO A 1 407 ? -20.497 -22.498 -26.640 1.00 22.84  ?  407  PRO A HG2    1 
ATOM   6226  H HG3    . PRO A 1 407 ? -19.365 -21.780 -25.786 1.00 22.84  ?  407  PRO A HG3    1 
ATOM   6227  H HD2    . PRO A 1 407 ? -21.893 -22.655 -24.864 1.00 22.65  ?  407  PRO A HD2    1 
ATOM   6228  H HD3    . PRO A 1 407 ? -20.509 -22.750 -24.089 1.00 22.65  ?  407  PRO A HD3    1 
ATOM   6229  N N      . ARG A 1 408 ? -23.430 -19.154 -24.895 1.00 15.76  ?  408  ARG A N      1 
ATOM   6230  C CA     . ARG A 1 408 ? -24.534 -18.206 -24.901 1.00 16.99  ?  408  ARG A CA     1 
ATOM   6231  C C      . ARG A 1 408 ? -24.546 -17.339 -23.650 1.00 16.58  ?  408  ARG A C      1 
ATOM   6232  O O      . ARG A 1 408 ? -24.865 -16.143 -23.725 1.00 16.18  ?  408  ARG A O      1 
ATOM   6233  C CB     . ARG A 1 408 ? -25.838 -18.964 -25.074 1.00 18.29  ?  408  ARG A CB     1 
ATOM   6234  C CG     . ARG A 1 408 ? -26.002 -19.507 -26.507 1.00 17.91  ?  408  ARG A CG     1 
ATOM   6235  C CD     . ARG A 1 408 ? -27.098 -20.550 -26.579 1.00 17.59  ?  408  ARG A CD     1 
ATOM   6236  N NE     . ARG A 1 408 ? -28.398 -20.015 -26.218 1.00 18.88  ?  408  ARG A NE     1 
ATOM   6237  C CZ     . ARG A 1 408 ? -29.498 -20.756 -26.115 1.00 21.40  ?  408  ARG A CZ     1 
ATOM   6238  N NH1    . ARG A 1 408 ? -29.431 -22.052 -26.364 1.00 21.16  ?  408  ARG A NH1    1 
ATOM   6239  N NH2    . ARG A 1 408 ? -30.651 -20.202 -25.778 1.00 23.60  ?  408  ARG A NH2    1 
ATOM   6240  H H      . ARG A 1 408 ? -23.668 -19.978 -24.827 1.00 18.90  ?  408  ARG A H      1 
ATOM   6241  H HA     . ARG A 1 408 ? -24.436 -17.601 -25.653 1.00 20.39  ?  408  ARG A HA     1 
ATOM   6242  H HB2    . ARG A 1 408 ? -25.854 -19.714 -24.460 1.00 21.95  ?  408  ARG A HB2    1 
ATOM   6243  H HB3    . ARG A 1 408 ? -26.580 -18.367 -24.888 1.00 21.95  ?  408  ARG A HB3    1 
ATOM   6244  H HG2    . ARG A 1 408 ? -26.234 -18.778 -27.103 1.00 21.48  ?  408  ARG A HG2    1 
ATOM   6245  H HG3    . ARG A 1 408 ? -25.171 -19.918 -26.792 1.00 21.48  ?  408  ARG A HG3    1 
ATOM   6246  H HD2    . ARG A 1 408 ? -27.154 -20.888 -27.487 1.00 21.10  ?  408  ARG A HD2    1 
ATOM   6247  H HD3    . ARG A 1 408 ? -26.889 -21.273 -25.968 1.00 21.10  ?  408  ARG A HD3    1 
ATOM   6248  H HE     . ARG A 1 408 ? -28.461 -19.172 -26.061 1.00 22.66  ?  408  ARG A HE     1 
ATOM   6249  H HH11   . ARG A 1 408 ? -28.682 -22.408 -26.590 1.00 25.39  ?  408  ARG A HH11   1 
ATOM   6250  H HH12   . ARG A 1 408 ? -30.137 -22.538 -26.300 1.00 25.39  ?  408  ARG A HH12   1 
ATOM   6251  H HH21   . ARG A 1 408 ? -30.693 -19.357 -25.623 1.00 28.32  ?  408  ARG A HH21   1 
ATOM   6252  H HH22   . ARG A 1 408 ? -31.359 -20.686 -25.713 1.00 28.32  ?  408  ARG A HH22   1 
ATOM   6253  N N      . VAL A 1 409 ? -24.206 -17.913 -22.492 1.00 16.24  ?  409  VAL A N      1 
ATOM   6254  C CA     . VAL A 1 409 ? -24.138 -17.102 -21.284 1.00 15.55  ?  409  VAL A CA     1 
ATOM   6255  C C      . VAL A 1 409 ? -22.994 -16.095 -21.381 1.00 14.93  ?  409  VAL A C      1 
ATOM   6256  O O      . VAL A 1 409 ? -23.153 -14.926 -20.995 1.00 16.14  ?  409  VAL A O      1 
ATOM   6257  C CB     . VAL A 1 409 ? -24.026 -17.974 -20.021 1.00 14.87  ?  409  VAL A CB     1 
ATOM   6258  C CG1    . VAL A 1 409 ? -23.856 -17.076 -18.795 1.00 16.61  ?  409  VAL A CG1    1 
ATOM   6259  C CG2    . VAL A 1 409 ? -25.257 -18.843 -19.853 1.00 17.29  ?  409  VAL A CG2    1 
ATOM   6260  H H      . VAL A 1 409 ? -24.016 -18.745 -22.383 1.00 19.48  ?  409  VAL A H      1 
ATOM   6261  H HA     . VAL A 1 409 ? -24.972 -16.610 -21.215 1.00 18.65  ?  409  VAL A HA     1 
ATOM   6262  H HB     . VAL A 1 409 ? -23.255 -18.556 -20.108 1.00 17.85  ?  409  VAL A HB     1 
ATOM   6263  H HG11   . VAL A 1 409 ? -23.956 -17.613 -17.994 1.00 19.93  ?  409  VAL A HG11   1 
ATOM   6264  H HG12   . VAL A 1 409 ? -22.972 -16.676 -18.817 1.00 19.93  ?  409  VAL A HG12   1 
ATOM   6265  H HG13   . VAL A 1 409 ? -24.534 -16.382 -18.815 1.00 19.93  ?  409  VAL A HG13   1 
ATOM   6266  H HG21   . VAL A 1 409 ? -25.149 -19.394 -19.062 1.00 20.74  ?  409  VAL A HG21   1 
ATOM   6267  H HG22   . VAL A 1 409 ? -26.036 -18.273 -19.756 1.00 20.74  ?  409  VAL A HG22   1 
ATOM   6268  H HG23   . VAL A 1 409 ? -25.355 -19.406 -20.637 1.00 20.74  ?  409  VAL A HG23   1 
ATOM   6269  N N      . SER A 1 410 ? -21.840 -16.522 -21.904 1.00 17.24  ?  410  SER A N      1 
ATOM   6270  C CA     . SER A 1 410 ? -20.729 -15.600 -22.107 1.00 16.71  ?  410  SER A CA     1 
ATOM   6271  C C      . SER A 1 410 ? -21.125 -14.459 -23.041 1.00 15.11  ?  410  SER A C      1 
ATOM   6272  O O      . SER A 1 410 ? -20.813 -13.297 -22.774 1.00 15.30  ?  410  SER A O      1 
ATOM   6273  C CB     . SER A 1 410 ? -19.518 -16.373 -22.643 1.00 17.04  ?  410  SER A CB     1 
ATOM   6274  O OG     . SER A 1 410 ? -18.443 -15.505 -22.937 1.00 18.00  ?  410  SER A OG     1 
ATOM   6275  H H      . SER A 1 410 ? -21.678 -17.331 -22.146 1.00 20.69  ?  410  SER A H      1 
ATOM   6276  H HA     . SER A 1 410 ? -20.475 -15.202 -21.259 1.00 20.05  ?  410  SER A HA     1 
ATOM   6277  H HB2    . SER A 1 410 ? -19.231 -17.011 -21.972 1.00 20.44  ?  410  SER A HB2    1 
ATOM   6278  H HB3    . SER A 1 410 ? -19.777 -16.837 -23.454 1.00 20.44  ?  410  SER A HB3    1 
ATOM   6279  H HG     . SER A 1 410 ? -18.201 -15.101 -22.242 1.00 21.59  ?  410  SER A HG     1 
ATOM   6280  N N      . ALA A 1 411 ? -21.814 -14.769 -24.142 1.00 14.24  ?  411  ALA A N      1 
ATOM   6281  C CA     . ALA A 1 411 ? -22.253 -13.711 -25.059 1.00 14.60  ?  411  ALA A CA     1 
ATOM   6282  C C      . ALA A 1 411 ? -23.248 -12.768 -24.390 1.00 15.66  ?  411  ALA A C      1 
ATOM   6283  O O      . ALA A 1 411 ? -23.208 -11.548 -24.604 1.00 16.77  ?  411  ALA A O      1 
ATOM   6284  C CB     . ALA A 1 411 ? -22.866 -14.338 -26.304 1.00 16.81  ?  411  ALA A CB     1 
ATOM   6285  H H      . ALA A 1 411 ? -22.038 -15.565 -24.379 1.00 17.08  ?  411  ALA A H      1 
ATOM   6286  H HA     . ALA A 1 411 ? -21.482 -13.185 -25.324 1.00 17.52  ?  411  ALA A HA     1 
ATOM   6287  H HB1    . ALA A 1 411 ? -23.164 -13.632 -26.899 1.00 20.17  ?  411  ALA A HB1    1 
ATOM   6288  H HB2    . ALA A 1 411 ? -22.196 -14.882 -26.746 1.00 20.17  ?  411  ALA A HB2    1 
ATOM   6289  H HB3    . ALA A 1 411 ? -23.619 -14.890 -26.041 1.00 20.17  ?  411  ALA A HB3    1 
ATOM   6290  N N      . ALA A 1 412 ? -24.159 -13.315 -23.587 1.00 15.87  ?  412  ALA A N      1 
ATOM   6291  C CA     . ALA A 1 412 ? -25.091 -12.472 -22.856 1.00 14.58  ?  412  ALA A CA     1 
ATOM   6292  C C      . ALA A 1 412 ? -24.355 -11.581 -21.864 1.00 15.60  ?  412  ALA A C      1 
ATOM   6293  O O      . ALA A 1 412 ? -24.730 -10.419 -21.662 1.00 16.63  ?  412  ALA A O      1 
ATOM   6294  C CB     . ALA A 1 412 ? -26.139 -13.332 -22.148 1.00 15.08  ?  412  ALA A CB     1 
ATOM   6295  H H      . ALA A 1 412 ? -24.257 -14.158 -23.449 1.00 19.05  ?  412  ALA A H      1 
ATOM   6296  H HA     . ALA A 1 412 ? -25.560 -11.900 -23.483 1.00 17.49  ?  412  ALA A HA     1 
ATOM   6297  H HB1    . ALA A 1 412 ? -26.742 -12.754 -21.656 1.00 18.10  ?  412  ALA A HB1    1 
ATOM   6298  H HB2    . ALA A 1 412 ? -26.633 -13.837 -22.813 1.00 18.10  ?  412  ALA A HB2    1 
ATOM   6299  H HB3    . ALA A 1 412 ? -25.690 -13.938 -21.538 1.00 18.10  ?  412  ALA A HB3    1 
ATOM   6300  N N      . ALA A 1 413 ? -23.282 -12.093 -21.255 1.00 15.25  ?  413  ALA A N      1 
ATOM   6301  C CA     . ALA A 1 413 ? -22.497 -11.258 -20.357 1.00 13.33  ?  413  ALA A CA     1 
ATOM   6302  C C      . ALA A 1 413 ? -21.845 -10.122 -21.121 1.00 15.52  ?  413  ALA A C      1 
ATOM   6303  O O      . ALA A 1 413 ? -21.792 -8.989  -20.631 1.00 15.82  ?  413  ALA A O      1 
ATOM   6304  C CB     . ALA A 1 413 ? -21.464 -12.116 -19.625 1.00 14.99  ?  413  ALA A CB     1 
ATOM   6305  H H      . ALA A 1 413 ? -22.995 -12.899 -21.343 1.00 18.30  ?  413  ALA A H      1 
ATOM   6306  H HA     . ALA A 1 413 ? -23.072 -10.865 -19.682 1.00 15.99  ?  413  ALA A HA     1 
ATOM   6307  H HB1    . ALA A 1 413 ? -20.948 -11.550 -19.030 1.00 17.98  ?  413  ALA A HB1    1 
ATOM   6308  H HB2    . ALA A 1 413 ? -21.926 -12.799 -19.115 1.00 17.98  ?  413  ALA A HB2    1 
ATOM   6309  H HB3    . ALA A 1 413 ? -20.878 -12.530 -20.278 1.00 17.98  ?  413  ALA A HB3    1 
ATOM   6310  N N      . MET A 1 414 ? -21.364 -10.402 -22.338 1.00 15.99  ?  414  MET A N      1 
ATOM   6311  C CA     . MET A 1 414 ? -20.762 -9.355  -23.150 1.00 17.35  ?  414  MET A CA     1 
ATOM   6312  C C      . MET A 1 414 ? -21.763 -8.240  -23.417 1.00 17.78  ?  414  MET A C      1 
ATOM   6313  O O      . MET A 1 414 ? -21.393 -7.058  -23.456 1.00 17.57  ?  414  MET A O      1 
ATOM   6314  C CB     . MET A 1 414 ? -20.271 -9.963  -24.463 1.00 20.25  ?  414  MET A CB     1 
ATOM   6315  C CG     . MET A 1 414 ? -19.170 -9.170  -25.116 1.00 23.14  ?  414  MET A CG     1 
ATOM   6316  S SD     . MET A 1 414 ? -17.662 -9.187  -24.115 1.00 22.54  ?  414  MET A SD     1 
ATOM   6317  C CE     . MET A 1 414 ? -16.538 -8.463  -25.295 1.00 24.50  ?  414  MET A CE     1 
ATOM   6318  H H      . MET A 1 414 ? -21.376 -11.179 -22.707 1.00 19.18  ?  414  MET A H      1 
ATOM   6319  H HA     . MET A 1 414 ? -19.995 -8.981  -22.689 1.00 20.81  ?  414  MET A HA     1 
ATOM   6320  H HB2    . MET A 1 414 ? -19.931 -10.855 -24.288 1.00 24.30  ?  414  MET A HB2    1 
ATOM   6321  H HB3    . MET A 1 414 ? -21.014 -10.008 -25.085 1.00 24.30  ?  414  MET A HB3    1 
ATOM   6322  H HG2    . MET A 1 414 ? -18.966 -9.555  -25.983 1.00 27.77  ?  414  MET A HG2    1 
ATOM   6323  H HG3    . MET A 1 414 ? -19.456 -8.249  -25.222 1.00 27.77  ?  414  MET A HG3    1 
ATOM   6324  H HE1    . MET A 1 414 ? -15.711 -8.234  -24.844 1.00 29.40  ?  414  MET A HE1    1 
ATOM   6325  H HE2    . MET A 1 414 ? -16.363 -9.106  -26.000 1.00 29.40  ?  414  MET A HE2    1 
ATOM   6326  H HE3    . MET A 1 414 ? -16.944 -7.665  -25.669 1.00 29.40  ?  414  MET A HE3    1 
ATOM   6327  N N      . SER A 1 415 ? -23.045 -8.580  -23.564 1.00 19.04  ?  415  SER A N      1 
ATOM   6328  C CA     . SER A 1 415 ? -24.074 -7.557  -23.740 1.00 20.11  ?  415  SER A CA     1 
ATOM   6329  C C      . SER A 1 415 ? -24.305 -6.734  -22.479 1.00 20.14  ?  415  SER A C      1 
ATOM   6330  O O      . SER A 1 415 ? -24.855 -5.636  -22.570 1.00 21.95  ?  415  SER A O      1 
ATOM   6331  C CB     . SER A 1 415 ? -25.391 -8.222  -24.162 1.00 23.36  ?  415  SER A CB     1 
ATOM   6332  O OG     . SER A 1 415 ? -25.289 -8.720  -25.474 1.00 29.41  ?  415  SER A OG     1 
ATOM   6333  H H      . SER A 1 415 ? -23.342 -9.387  -23.565 1.00 22.84  ?  415  SER A H      1 
ATOM   6334  H HA     . SER A 1 415 ? -23.790 -6.950  -24.441 1.00 24.12  ?  415  SER A HA     1 
ATOM   6335  H HB2    . SER A 1 415 ? -25.585 -8.955  -23.557 1.00 28.03  ?  415  SER A HB2    1 
ATOM   6336  H HB3    . SER A 1 415 ? -26.104 -7.565  -24.126 1.00 28.03  ?  415  SER A HB3    1 
ATOM   6337  H HG     . SER A 1 415 ? -25.981 -9.154  -25.671 1.00 35.29  ?  415  SER A HG     1 
ATOM   6338  N N      . GLU A 1 416 ? -23.915 -7.244  -21.311 1.00 18.28  ?  416  GLU A N      1 
ATOM   6339  C CA     . GLU A 1 416 ? -23.881 -6.465  -20.078 1.00 18.78  ?  416  GLU A CA     1 
ATOM   6340  C C      . GLU A 1 416 ? -22.536 -5.763  -19.899 1.00 18.74  ?  416  GLU A C      1 
ATOM   6341  O O      . GLU A 1 416 ? -22.249 -5.269  -18.810 1.00 19.21  ?  416  GLU A O      1 
ATOM   6342  C CB     . GLU A 1 416 ? -24.128 -7.370  -18.867 1.00 19.41  ?  416  GLU A CB     1 
ATOM   6343  C CG     . GLU A 1 416 ? -25.318 -8.333  -18.990 1.00 19.22  ?  416  GLU A CG     1 
ATOM   6344  C CD     . GLU A 1 416 ? -26.661 -7.642  -18.907 1.00 20.87  ?  416  GLU A CD     1 
ATOM   6345  O OE1    . GLU A 1 416 ? -26.741 -6.542  -18.314 1.00 20.29  ?  416  GLU A OE1    1 
ATOM   6346  O OE2    . GLU A 1 416 ? -27.658 -8.192  -19.440 1.00 22.22  -1 416  GLU A OE2    1 
ATOM   6347  H H      . GLU A 1 416 ? -23.661 -8.059  -21.208 1.00 21.93  ?  416  GLU A H      1 
ATOM   6348  H HA     . GLU A 1 416 ? -24.591 -5.804  -20.108 1.00 22.53  ?  416  GLU A HA     1 
ATOM   6349  H HB2    . GLU A 1 416 ? -23.334 -7.909  -18.723 1.00 23.29  ?  416  GLU A HB2    1 
ATOM   6350  H HB3    . GLU A 1 416 ? -24.291 -6.807  -18.094 1.00 23.29  ?  416  GLU A HB3    1 
ATOM   6351  H HG2    . GLU A 1 416 ? -25.269 -8.785  -19.847 1.00 23.06  ?  416  GLU A HG2    1 
ATOM   6352  H HG3    . GLU A 1 416 ? -25.273 -8.981  -18.270 1.00 23.06  ?  416  GLU A HG3    1 
ATOM   6353  N N      . ASN A 1 417 ? -21.696 -5.759  -20.937 1.00 17.89  ?  417  ASN A N      1 
ATOM   6354  C CA     . ASN A 1 417 ? -20.349 -5.173  -20.909 1.00 18.00  ?  417  ASN A CA     1 
ATOM   6355  C C      . ASN A 1 417 ? -19.462 -5.862  -19.870 1.00 17.75  ?  417  ASN A C      1 
ATOM   6356  O O      . ASN A 1 417 ? -18.638 -5.237  -19.204 1.00 18.49  ?  417  ASN A O      1 
ATOM   6357  C CB     . ASN A 1 417 ? -20.370 -3.652  -20.733 1.00 20.44  ?  417  ASN A CB     1 
ATOM   6358  C CG     . ASN A 1 417 ? -20.752 -2.923  -22.015 1.00 24.93  ?  417  ASN A CG     1 
ATOM   6359  O OD1    . ASN A 1 417 ? -21.382 -3.497  -22.896 1.00 30.77  ?  417  ASN A OD1    1 
ATOM   6360  N ND2    . ASN A 1 417 ? -20.359 -1.671  -22.130 1.00 25.79  ?  417  ASN A ND2    1 
ATOM   6361  H H      . ASN A 1 417 ? -21.890 -6.103  -21.701 1.00 21.46  ?  417  ASN A H      1 
ATOM   6362  H HA     . ASN A 1 417 ? -19.943 -5.333  -21.775 1.00 21.60  ?  417  ASN A HA     1 
ATOM   6363  H HB2    . ASN A 1 417 ? -21.019 -3.420  -20.050 1.00 24.52  ?  417  ASN A HB2    1 
ATOM   6364  H HB3    . ASN A 1 417 ? -19.487 -3.351  -20.467 1.00 24.52  ?  417  ASN A HB3    1 
ATOM   6365  H HD21   . ASN A 1 417 ? -20.553 -1.223  -22.838 1.00 30.95  ?  417  ASN A HD21   1 
ATOM   6366  H HD22   . ASN A 1 417 ? -19.908 -1.302  -21.497 1.00 30.95  ?  417  ASN A HD22   1 
ATOM   6367  N N      . LEU A 1 418 ? -19.622 -7.171  -19.753 1.00 16.72  ?  418  LEU A N      1 
ATOM   6368  C CA     . LEU A 1 418 ? -18.787 -8.000  -18.893 1.00 14.90  ?  418  LEU A CA     1 
ATOM   6369  C C      . LEU A 1 418 ? -18.148 -9.100  -19.723 1.00 14.64  ?  418  LEU A C      1 
ATOM   6370  O O      . LEU A 1 418 ? -18.852 -9.864  -20.389 1.00 14.77  ?  418  LEU A O      1 
ATOM   6371  C CB     . LEU A 1 418 ? -19.636 -8.642  -17.790 1.00 15.65  ?  418  LEU A CB     1 
ATOM   6372  C CG     . LEU A 1 418 ? -18.931 -9.745  -16.992 1.00 16.43  ?  418  LEU A CG     1 
ATOM   6373  C CD1    . LEU A 1 418 ? -17.726 -9.178  -16.225 1.00 17.13  ?  418  LEU A CD1    1 
ATOM   6374  C CD2    . LEU A 1 418 ? -19.866 -10.458 -16.028 1.00 17.12  ?  418  LEU A CD2    1 
ATOM   6375  H H      . LEU A 1 418 ? -20.226 -7.614  -20.174 1.00 20.06  ?  418  LEU A H      1 
ATOM   6376  H HA     . LEU A 1 418 ? -18.087 -7.457  -18.498 1.00 17.88  ?  418  LEU A HA     1 
ATOM   6377  H HB2    . LEU A 1 418 ? -19.898 -7.950  -17.163 1.00 18.77  ?  418  LEU A HB2    1 
ATOM   6378  H HB3    . LEU A 1 418 ? -20.423 -9.035  -18.199 1.00 18.77  ?  418  LEU A HB3    1 
ATOM   6379  H HG     . LEU A 1 418 ? -18.619 -10.405 -17.631 1.00 19.72  ?  418  LEU A HG     1 
ATOM   6380  H HD11   . LEU A 1 418 ? -17.281 -9.901  -15.757 1.00 20.55  ?  418  LEU A HD11   1 
ATOM   6381  H HD12   . LEU A 1 418 ? -17.115 -8.766  -16.856 1.00 20.55  ?  418  LEU A HD12   1 
ATOM   6382  H HD13   . LEU A 1 418 ? -18.040 -8.516  -15.589 1.00 20.55  ?  418  LEU A HD13   1 
ATOM   6383  H HD21   . LEU A 1 418 ? -19.383 -11.179 -15.594 1.00 20.54  ?  418  LEU A HD21   1 
ATOM   6384  H HD22   . LEU A 1 418 ? -20.180 -9.824  -15.365 1.00 20.54  ?  418  LEU A HD22   1 
ATOM   6385  H HD23   . LEU A 1 418 ? -20.618 -10.816 -16.525 1.00 20.54  ?  418  LEU A HD23   1 
ATOM   6386  N N      . ILE A 1 419 ? -16.827 -9.204  -19.649 1.00 14.37  ?  419  ILE A N      1 
ATOM   6387  C CA     . ILE A 1 419 ? -16.100 -10.326 -20.244 1.00 14.37  ?  419  ILE A CA     1 
ATOM   6388  C C      . ILE A 1 419 ? -15.942 -11.415 -19.198 1.00 14.26  ?  419  ILE A C      1 
ATOM   6389  O O      . ILE A 1 419 ? -15.307 -11.195 -18.161 1.00 14.50  ?  419  ILE A O      1 
ATOM   6390  C CB     . ILE A 1 419 ? -14.722 -9.881  -20.771 1.00 13.66  ?  419  ILE A CB     1 
ATOM   6391  C CG1    . ILE A 1 419 ? -14.856 -8.763  -21.801 1.00 15.82  ?  419  ILE A CG1    1 
ATOM   6392  C CG2    . ILE A 1 419 ? -14.006 -11.079 -21.367 1.00 14.47  ?  419  ILE A CG2    1 
ATOM   6393  C CD1    . ILE A 1 419 ? -13.558 -7.992  -22.073 1.00 15.70  ?  419  ILE A CD1    1 
ATOM   6394  H H      . ILE A 1 419 ? -16.321 -8.631  -19.256 1.00 17.24  ?  419  ILE A H      1 
ATOM   6395  H HA     . ILE A 1 419 ? -16.620 -10.679 -20.983 1.00 17.24  ?  419  ILE A HA     1 
ATOM   6396  H HB     . ILE A 1 419 ? -14.205 -9.529  -20.029 1.00 16.39  ?  419  ILE A HB     1 
ATOM   6397  H HG12   . ILE A 1 419 ? -15.149 -9.151  -22.641 1.00 18.98  ?  419  ILE A HG12   1 
ATOM   6398  H HG13   . ILE A 1 419 ? -15.515 -8.126  -21.483 1.00 18.98  ?  419  ILE A HG13   1 
ATOM   6399  H HG21   . ILE A 1 419 ? -13.249 -10.768 -21.888 1.00 17.36  ?  419  ILE A HG21   1 
ATOM   6400  H HG22   . ILE A 1 419 ? -13.699 -11.654 -20.648 1.00 17.36  ?  419  ILE A HG22   1 
ATOM   6401  H HG23   . ILE A 1 419 ? -14.623 -11.564 -21.938 1.00 17.36  ?  419  ILE A HG23   1 
ATOM   6402  H HD11   . ILE A 1 419 ? -13.747 -7.261  -22.682 1.00 18.84  ?  419  ILE A HD11   1 
ATOM   6403  H HD12   . ILE A 1 419 ? -13.215 -7.644  -21.235 1.00 18.84  ?  419  ILE A HD12   1 
ATOM   6404  H HD13   . ILE A 1 419 ? -12.910 -8.594  -22.471 1.00 18.84  ?  419  ILE A HD13   1 
ATOM   6405  N N      . ALA A 1 420 ? -16.556 -12.574 -19.448 1.00 12.97  ?  420  ALA A N      1 
ATOM   6406  C CA     . ALA A 1 420 ? -16.358 -13.792 -18.674 1.00 14.11  ?  420  ALA A CA     1 
ATOM   6407  C C      . ALA A 1 420 ? -16.399 -14.938 -19.677 1.00 15.48  ?  420  ALA A C      1 
ATOM   6408  O O      . ALA A 1 420 ? -17.248 -14.973 -20.566 1.00 17.51  ?  420  ALA A O      1 
ATOM   6409  C CB     . ALA A 1 420 ? -17.436 -13.960 -17.609 1.00 16.58  ?  420  ALA A CB     1 
ATOM   6410  H H      . ALA A 1 420 ? -17.116 -12.680 -20.092 1.00 15.56  ?  420  ALA A H      1 
ATOM   6411  H HA     . ALA A 1 420 ? -15.508 -13.792 -18.206 1.00 16.93  ?  420  ALA A HA     1 
ATOM   6412  H HB1    . ALA A 1 420 ? -17.236 -14.746 -17.078 1.00 19.89  ?  420  ALA A HB1    1 
ATOM   6413  H HB2    . ALA A 1 420 ? -17.447 -13.172 -17.044 1.00 19.89  ?  420  ALA A HB2    1 
ATOM   6414  H HB3    . ALA A 1 420 ? -18.297 -14.065 -18.045 1.00 19.89  ?  420  ALA A HB3    1 
ATOM   6415  N N      A ARG A 1 421 ? -15.483 -15.883 -19.521 0.46 14.97  ?  421  ARG A N      1 
ATOM   6416  N N      B ARG A 1 421 ? -15.467 -15.864 -19.540 0.54 15.33  ?  421  ARG A N      1 
ATOM   6417  C CA     A ARG A 1 421 ? -15.167 -16.822 -20.590 0.46 17.12  ?  421  ARG A CA     1 
ATOM   6418  C CA     B ARG A 1 421 ? -15.173 -16.806 -20.609 0.54 17.70  ?  421  ARG A CA     1 
ATOM   6419  C C      A ARG A 1 421 ? -16.044 -18.063 -20.556 0.46 16.30  ?  421  ARG A C      1 
ATOM   6420  C C      B ARG A 1 421 ? -16.057 -18.041 -20.559 0.54 16.89  ?  421  ARG A C      1 
ATOM   6421  O O      A ARG A 1 421 ? -16.255 -18.662 -19.503 0.46 15.60  ?  421  ARG A O      1 
ATOM   6422  O O      B ARG A 1 421 ? -16.289 -18.609 -19.495 0.54 16.97  ?  421  ARG A O      1 
ATOM   6423  C CB     A ARG A 1 421 ? -13.706 -17.241 -20.438 0.46 20.11  ?  421  ARG A CB     1 
ATOM   6424  C CB     B ARG A 1 421 ? -13.714 -17.231 -20.473 0.54 20.93  ?  421  ARG A CB     1 
ATOM   6425  C CG     A ARG A 1 421 ? -13.220 -18.311 -21.391 0.46 25.18  ?  421  ARG A CG     1 
ATOM   6426  C CG     B ARG A 1 421 ? -13.204 -18.066 -21.597 0.54 25.82  ?  421  ARG A CG     1 
ATOM   6427  C CD     A ARG A 1 421 ? -11.736 -18.072 -21.714 0.46 29.80  ?  421  ARG A CD     1 
ATOM   6428  C CD     B ARG A 1 421 ? -11.733 -18.391 -21.385 0.54 30.28  ?  421  ARG A CD     1 
ATOM   6429  N NE     A ARG A 1 421 ? -11.617 -16.859 -22.511 0.46 31.96  ?  421  ARG A NE     1 
ATOM   6430  N NE     B ARG A 1 421 ? -11.252 -19.228 -22.467 0.54 33.82  ?  421  ARG A NE     1 
ATOM   6431  C CZ     A ARG A 1 421 ? -11.477 -16.846 -23.831 0.46 34.16  ?  421  ARG A CZ     1 
ATOM   6432  C CZ     B ARG A 1 421 ? -10.234 -20.077 -22.376 0.54 33.97  ?  421  ARG A CZ     1 
ATOM   6433  N NH1    A ARG A 1 421 ? -11.408 -15.694 -24.472 0.46 34.40  ?  421  ARG A NH1    1 
ATOM   6434  N NH1    B ARG A 1 421 ? -9.894  -20.784 -23.442 0.54 35.26  ?  421  ARG A NH1    1 
ATOM   6435  N NH2    A ARG A 1 421 ? -11.392 -17.981 -24.513 0.46 36.23  ?  421  ARG A NH2    1 
ATOM   6436  N NH2    B ARG A 1 421 ? -9.571  -20.231 -21.225 0.54 28.47  ?  421  ARG A NH2    1 
ATOM   6437  H H      A ARG A 1 421 ? -15.028 -16.003 -18.801 0.46 17.96  ?  421  ARG A H      1 
ATOM   6438  H H      B ARG A 1 421 ? -14.988 -15.970 -18.834 0.54 18.39  ?  421  ARG A H      1 
ATOM   6439  H HA     A ARG A 1 421 ? -15.326 -16.395 -21.447 0.46 20.55  ?  421  ARG A HA     1 
ATOM   6440  H HA     B ARG A 1 421 ? -15.342 -16.382 -21.465 0.54 21.23  ?  421  ARG A HA     1 
ATOM   6441  H HB2    A ARG A 1 421 ? -13.150 -16.458 -20.579 0.46 24.13  ?  421  ARG A HB2    1 
ATOM   6442  H HB2    B ARG A 1 421 ? -13.163 -16.434 -20.428 0.54 25.11  ?  421  ARG A HB2    1 
ATOM   6443  H HB3    A ARG A 1 421 ? -13.579 -17.579 -19.538 0.46 24.13  ?  421  ARG A HB3    1 
ATOM   6444  H HB3    B ARG A 1 421 ? -13.617 -17.748 -19.658 0.54 25.11  ?  421  ARG A HB3    1 
ATOM   6445  H HG2    A ARG A 1 421 ? -13.314 -19.185 -20.980 0.46 30.21  ?  421  ARG A HG2    1 
ATOM   6446  H HG2    B ARG A 1 421 ? -13.702 -18.898 -21.638 0.54 30.98  ?  421  ARG A HG2    1 
ATOM   6447  H HG3    A ARG A 1 421 ? -13.730 -18.275 -22.215 0.46 30.21  ?  421  ARG A HG3    1 
ATOM   6448  H HG3    B ARG A 1 421 ? -13.298 -17.582 -22.433 0.54 30.98  ?  421  ARG A HG3    1 
ATOM   6449  H HD2    A ARG A 1 421 ? -11.232 -17.961 -20.893 0.46 35.76  ?  421  ARG A HD2    1 
ATOM   6450  H HD2    B ARG A 1 421 ? -11.215 -17.570 -21.372 0.54 36.33  ?  421  ARG A HD2    1 
ATOM   6451  H HD3    A ARG A 1 421 ? -11.384 -18.819 -22.222 0.46 35.76  ?  421  ARG A HD3    1 
ATOM   6452  H HD3    B ARG A 1 421 ? -11.620 -18.868 -20.548 0.54 36.33  ?  421  ARG A HD3    1 
ATOM   6453  H HE     A ARG A 1 421 ? -11.638 -16.103 -22.100 0.46 38.34  ?  421  ARG A HE     1 
ATOM   6454  H HE     B ARG A 1 421 ? -11.656 -19.170 -23.225 0.54 40.58  ?  421  ARG A HE     1 
ATOM   6455  H HH11   A ARG A 1 421 ? -11.454 -14.955 -24.035 0.46 41.28  ?  421  ARG A HH11   1 
ATOM   6456  H HH11   B ARG A 1 421 ? -10.329 -20.689 -24.178 0.54 42.31  ?  421  ARG A HH11   1 
ATOM   6457  H HH12   A ARG A 1 421 ? -11.317 -15.682 -25.328 0.46 41.28  ?  421  ARG A HH12   1 
ATOM   6458  H HH12   B ARG A 1 421 ? -9.237  -21.338 -23.400 0.54 42.31  ?  421  ARG A HH12   1 
ATOM   6459  H HH21   A ARG A 1 421 ? -11.428 -18.735 -24.099 0.46 43.47  ?  421  ARG A HH21   1 
ATOM   6460  H HH21   B ARG A 1 421 ? -9.803  -19.777 -20.531 0.54 34.16  ?  421  ARG A HH21   1 
ATOM   6461  H HH22   A ARG A 1 421 ? -11.302 -17.964 -25.368 0.46 43.47  ?  421  ARG A HH22   1 
ATOM   6462  H HH22   B ARG A 1 421 ? -8.914  -20.783 -21.177 0.54 34.16  ?  421  ARG A HH22   1 
ATOM   6463  N N      . ALA A 1 422 ? -16.521 -18.476 -21.729 1.00 16.29  ?  422  ALA A N      1 
ATOM   6464  C CA     . ALA A 1 422 ? -17.156 -19.780 -21.867 1.00 15.23  ?  422  ALA A CA     1 
ATOM   6465  C C      . ALA A 1 422 ? -16.010 -20.788 -21.962 1.00 16.93  ?  422  ALA A C      1 
ATOM   6466  O O      . ALA A 1 422 ? -15.216 -20.753 -22.914 1.00 18.78  ?  422  ALA A O      1 
ATOM   6467  C CB     . ALA A 1 422 ? -18.045 -19.826 -23.099 1.00 17.06  ?  422  ALA A CB     1 
ATOM   6468  H H      . ALA A 1 422 ? -16.478 -18.028 -22.462 1.00 19.55  ?  422  ALA A H      1 
ATOM   6469  H HA     . ALA A 1 422 ? -17.725 -19.980 -21.107 1.00 18.27  ?  422  ALA A HA     1 
ATOM   6470  H HB1    . ALA A 1 422 ? -18.399 -20.723 -23.200 1.00 20.47  ?  422  ALA A HB1    1 
ATOM   6471  H HB2    . ALA A 1 422 ? -18.772 -19.194 -22.987 1.00 20.47  ?  422  ALA A HB2    1 
ATOM   6472  H HB3    . ALA A 1 422 ? -17.517 -19.588 -23.877 1.00 20.47  ?  422  ALA A HB3    1 
ATOM   6473  N N      . MET A 1 423 ? -15.897 -21.662 -20.975 1.00 16.64  ?  423  MET A N      1 
ATOM   6474  C CA     . MET A 1 423 ? -14.785 -22.587 -20.927 1.00 16.51  ?  423  MET A CA     1 
ATOM   6475  C C      . MET A 1 423 ? -15.018 -23.737 -21.901 1.00 16.76  ?  423  MET A C      1 
ATOM   6476  O O      . MET A 1 423 ? -16.162 -24.101 -22.203 1.00 18.64  ?  423  MET A O      1 
ATOM   6477  C CB     . MET A 1 423 ? -14.597 -23.125 -19.520 1.00 17.73  ?  423  MET A CB     1 
ATOM   6478  C CG     . MET A 1 423 ? -14.650 -22.060 -18.448 1.00 18.34  ?  423  MET A CG     1 
ATOM   6479  S SD     . MET A 1 423 ? -13.267 -20.910 -18.531 1.00 18.69  ?  423  MET A SD     1 
ATOM   6480  C CE     . MET A 1 423 ? -11.895 -21.967 -18.106 1.00 19.82  ?  423  MET A CE     1 
ATOM   6481  H H      . MET A 1 423 ? -16.450 -21.739 -20.321 1.00 19.96  ?  423  MET A H      1 
ATOM   6482  H HA     . MET A 1 423 ? -13.968 -22.124 -21.172 1.00 19.81  ?  423  MET A HA     1 
ATOM   6483  H HB2    . MET A 1 423 ? -15.300 -23.767 -19.335 1.00 21.27  ?  423  MET A HB2    1 
ATOM   6484  H HB3    . MET A 1 423 ? -13.730 -23.558 -19.465 1.00 21.27  ?  423  MET A HB3    1 
ATOM   6485  H HG2    . MET A 1 423 ? -15.470 -21.551 -18.551 1.00 22.01  ?  423  MET A HG2    1 
ATOM   6486  H HG3    . MET A 1 423 ? -14.632 -22.488 -17.578 1.00 22.01  ?  423  MET A HG3    1 
ATOM   6487  H HE1    . MET A 1 423 ? -11.306 -22.044 -18.873 1.00 23.78  ?  423  MET A HE1    1 
ATOM   6488  H HE2    . MET A 1 423 ? -11.415 -21.576 -17.359 1.00 23.78  ?  423  MET A HE2    1 
ATOM   6489  H HE3    . MET A 1 423 ? -12.234 -22.842 -17.860 1.00 23.78  ?  423  MET A HE3    1 
ATOM   6490  N N      . PRO A 1 424 ? -13.943 -24.332 -22.403 1.00 17.90  ?  424  PRO A N      1 
ATOM   6491  C CA     . PRO A 1 424 ? -14.094 -25.410 -23.389 1.00 19.11  ?  424  PRO A CA     1 
ATOM   6492  C C      . PRO A 1 424 ? -14.683 -26.673 -22.790 1.00 21.42  ?  424  PRO A C      1 
ATOM   6493  O O      . PRO A 1 424 ? -14.597 -26.938 -21.588 1.00 20.94  ?  424  PRO A O      1 
ATOM   6494  C CB     . PRO A 1 424 ? -12.654 -25.666 -23.857 1.00 22.59  ?  424  PRO A CB     1 
ATOM   6495  C CG     . PRO A 1 424 ? -11.819 -25.161 -22.741 1.00 22.20  ?  424  PRO A CG     1 
ATOM   6496  C CD     . PRO A 1 424 ? -12.537 -23.979 -22.180 1.00 21.15  ?  424  PRO A CD     1 
ATOM   6497  H HA     . PRO A 1 424 ? -14.649 -25.109 -24.126 1.00 22.93  ?  424  PRO A HA     1 
ATOM   6498  H HB2    . PRO A 1 424 ? -12.512 -26.615 -24.000 1.00 27.10  ?  424  PRO A HB2    1 
ATOM   6499  H HB3    . PRO A 1 424 ? -12.477 -25.178 -24.677 1.00 27.10  ?  424  PRO A HB3    1 
ATOM   6500  H HG2    . PRO A 1 424 ? -11.723 -25.853 -22.068 1.00 26.64  ?  424  PRO A HG2    1 
ATOM   6501  H HG3    . PRO A 1 424 ? -10.947 -24.902 -23.078 1.00 26.64  ?  424  PRO A HG3    1 
ATOM   6502  H HD2    . PRO A 1 424 ? -12.350 -23.874 -21.234 1.00 25.37  ?  424  PRO A HD2    1 
ATOM   6503  H HD3    . PRO A 1 424 ? -12.301 -23.169 -22.657 1.00 25.37  ?  424  PRO A HD3    1 
ATOM   6504  N N      . GLN A 1 425 ? -15.281 -27.472 -23.680 1.00 21.34  ?  425  GLN A N      1 
ATOM   6505  C CA     . GLN A 1 425 ? -15.667 -28.843 -23.377 1.00 22.02  ?  425  GLN A CA     1 
ATOM   6506  C C      . GLN A 1 425 ? -16.643 -28.891 -22.204 1.00 20.93  ?  425  GLN A C      1 
ATOM   6507  O O      . GLN A 1 425 ? -16.478 -29.643 -21.245 1.00 22.96  ?  425  GLN A O      1 
ATOM   6508  C CB     . GLN A 1 425 ? -14.417 -29.686 -23.108 1.00 23.25  ?  425  GLN A CB     1 
ATOM   6509  C CG     . GLN A 1 425 ? -14.277 -30.892 -23.956 1.00 21.00  ?  425  GLN A CG     1 
ATOM   6510  C CD     . GLN A 1 425 ? -12.977 -31.645 -23.699 1.00 18.34  ?  425  GLN A CD     1 
ATOM   6511  O OE1    . GLN A 1 425 ? -11.912 -31.263 -24.179 1.00 16.03  ?  425  GLN A OE1    1 
ATOM   6512  N NE2    . GLN A 1 425 ? -13.059 -32.719 -22.938 1.00 21.24  ?  425  GLN A NE2    1 
ATOM   6513  H H      . GLN A 1 425 ? -15.475 -27.232 -24.483 1.00 25.60  ?  425  GLN A H      1 
ATOM   6514  H HA     . GLN A 1 425 ? -16.132 -29.223 -24.138 1.00 26.42  ?  425  GLN A HA     1 
ATOM   6515  H HB2    . GLN A 1 425 ? -13.635 -29.133 -23.260 1.00 27.90  ?  425  GLN A HB2    1 
ATOM   6516  H HB3    . GLN A 1 425 ? -14.440 -29.982 -22.185 1.00 27.90  ?  425  GLN A HB3    1 
ATOM   6517  H HG2    . GLN A 1 425 ? -15.014 -31.496 -23.772 1.00 25.19  ?  425  GLN A HG2    1 
ATOM   6518  H HG3    . GLN A 1 425 ? -14.291 -30.627 -24.889 1.00 25.19  ?  425  GLN A HG3    1 
ATOM   6519  H HE21   . GLN A 1 425 ? -13.819 -32.961 -22.616 1.00 25.48  ?  425  GLN A HE21   1 
ATOM   6520  H HE22   . GLN A 1 425 ? -12.352 -33.178 -22.764 1.00 25.48  ?  425  GLN A HE22   1 
ATOM   6521  N N      . GLY A 1 426 ? -17.685 -28.081 -22.296 1.00 20.99  ?  426  GLY A N      1 
ATOM   6522  C CA     . GLY A 1 426 ? -18.688 -28.028 -21.256 1.00 21.85  ?  426  GLY A CA     1 
ATOM   6523  C C      . GLY A 1 426 ? -19.453 -26.731 -21.353 1.00 19.90  ?  426  GLY A C      1 
ATOM   6524  O O      . GLY A 1 426 ? -19.244 -25.931 -22.259 1.00 19.89  ?  426  GLY A O      1 
ATOM   6525  H H      . GLY A 1 426 ? -17.833 -27.549 -22.955 1.00 25.18  ?  426  GLY A H      1 
ATOM   6526  H HA2    . GLY A 1 426 ? -19.307 -28.768 -21.354 1.00 26.22  ?  426  GLY A HA2    1 
ATOM   6527  H HA3    . GLY A 1 426 ? -18.266 -28.082 -20.384 1.00 26.22  ?  426  GLY A HA3    1 
ATOM   6528  N N      . ASP A 1 427 ? -20.340 -26.537 -20.382 1.00 18.88  ?  427  ASP A N      1 
ATOM   6529  C CA     . ASP A 1 427 ? -21.108 -25.298 -20.255 1.00 17.03  ?  427  ASP A CA     1 
ATOM   6530  C C      . ASP A 1 427 ? -20.713 -24.659 -18.937 1.00 15.50  ?  427  ASP A C      1 
ATOM   6531  O O      . ASP A 1 427 ? -21.322 -24.929 -17.896 1.00 16.66  ?  427  ASP A O      1 
ATOM   6532  C CB     . ASP A 1 427 ? -22.566 -25.590 -20.336 1.00 18.57  ?  427  ASP A CB     1 
ATOM   6533  C CG     . ASP A 1 427 ? -22.960 -26.101 -21.690 1.00 20.95  ?  427  ASP A CG     1 
ATOM   6534  O OD1    . ASP A 1 427 ? -22.693 -25.383 -22.675 1.00 21.24  ?  427  ASP A OD1    1 
ATOM   6535  O OD2    . ASP A 1 427 ? -23.505 -27.230 -21.768 1.00 22.87  -1 427  ASP A OD2    1 
ATOM   6536  H H      . ASP A 1 427 ? -20.517 -27.119 -19.774 1.00 22.65  ?  427  ASP A H      1 
ATOM   6537  H HA     . ASP A 1 427 ? -20.882 -24.680 -20.967 1.00 20.43  ?  427  ASP A HA     1 
ATOM   6538  H HB2    . ASP A 1 427 ? -22.794 -26.266 -19.679 1.00 22.28  ?  427  ASP A HB2    1 
ATOM   6539  H HB3    . ASP A 1 427 ? -23.065 -24.777 -20.162 1.00 22.28  ?  427  ASP A HB3    1 
ATOM   6540  N N      . ILE A 1 428 ? -19.701 -23.799 -18.998 1.00 15.03  ?  428  ILE A N      1 
ATOM   6541  C CA     . ILE A 1 428 ? -19.044 -23.272 -17.814 1.00 14.10  ?  428  ILE A CA     1 
ATOM   6542  C C      . ILE A 1 428 ? -18.691 -21.819 -18.087 1.00 14.86  ?  428  ILE A C      1 
ATOM   6543  O O      . ILE A 1 428 ? -18.035 -21.518 -19.096 1.00 16.09  ?  428  ILE A O      1 
ATOM   6544  C CB     . ILE A 1 428 ? -17.750 -24.046 -17.505 1.00 15.52  ?  428  ILE A CB     1 
ATOM   6545  C CG1    . ILE A 1 428 ? -17.992 -25.541 -17.340 1.00 17.18  ?  428  ILE A CG1    1 
ATOM   6546  C CG2    . ILE A 1 428 ? -17.106 -23.494 -16.238 1.00 14.46  ?  428  ILE A CG2    1 
ATOM   6547  C CD1    . ILE A 1 428 ? -16.736 -26.356 -17.525 1.00 15.22  ?  428  ILE A CD1    1 
ATOM   6548  H H      . ILE A 1 428 ? -19.371 -23.502 -19.734 1.00 18.04  ?  428  ILE A H      1 
ATOM   6549  H HA     . ILE A 1 428 ? -19.647 -23.327 -17.056 1.00 16.91  ?  428  ILE A HA     1 
ATOM   6550  H HB     . ILE A 1 428 ? -17.159 -23.925 -18.265 1.00 18.63  ?  428  ILE A HB     1 
ATOM   6551  H HG12   . ILE A 1 428 ? -18.331 -25.710 -16.448 1.00 20.61  ?  428  ILE A HG12   1 
ATOM   6552  H HG13   . ILE A 1 428 ? -18.639 -25.831 -18.002 1.00 20.61  ?  428  ILE A HG13   1 
ATOM   6553  H HG21   . ILE A 1 428 ? -16.351 -24.054 -15.998 1.00 17.35  ?  428  ILE A HG21   1 
ATOM   6554  H HG22   . ILE A 1 428 ? -16.806 -22.587 -16.406 1.00 17.35  ?  428  ILE A HG22   1 
ATOM   6555  H HG23   . ILE A 1 428 ? -17.762 -23.498 -15.523 1.00 17.35  ?  428  ILE A HG23   1 
ATOM   6556  H HD11   . ILE A 1 428 ? -16.959 -27.298 -17.464 1.00 18.26  ?  428  ILE A HD11   1 
ATOM   6557  H HD12   . ILE A 1 428 ? -16.359 -26.161 -18.398 1.00 18.26  ?  428  ILE A HD12   1 
ATOM   6558  H HD13   . ILE A 1 428 ? -16.102 -26.120 -16.831 1.00 18.26  ?  428  ILE A HD13   1 
ATOM   6559  N N      . LEU A 1 429 ? -19.102 -20.923 -17.181 1.00 14.78  ?  429  LEU A N      1 
ATOM   6560  C CA     . LEU A 1 429 ? -18.722 -19.517 -17.253 1.00 14.78  ?  429  LEU A CA     1 
ATOM   6561  C C      . LEU A 1 429 ? -17.605 -19.292 -16.246 1.00 15.28  ?  429  LEU A C      1 
ATOM   6562  O O      . LEU A 1 429 ? -17.800 -19.499 -15.050 1.00 15.26  ?  429  LEU A O      1 
ATOM   6563  C CB     . LEU A 1 429 ? -19.898 -18.604 -16.930 1.00 16.13  ?  429  LEU A CB     1 
ATOM   6564  C CG     . LEU A 1 429 ? -19.670 -17.122 -17.213 1.00 16.39  ?  429  LEU A CG     1 
ATOM   6565  C CD1    . LEU A 1 429 ? -19.558 -16.842 -18.696 1.00 15.84  ?  429  LEU A CD1    1 
ATOM   6566  C CD2    . LEU A 1 429 ? -20.801 -16.319 -16.617 1.00 15.68  ?  429  LEU A CD2    1 
ATOM   6567  H H      . LEU A 1 429 ? -19.606 -21.115 -16.511 1.00 17.74  ?  429  LEU A H      1 
ATOM   6568  H HA     . LEU A 1 429 ? -18.416 -19.306 -18.149 1.00 17.74  ?  429  LEU A HA     1 
ATOM   6569  H HB2    . LEU A 1 429 ? -20.660 -18.887 -17.460 1.00 19.36  ?  429  LEU A HB2    1 
ATOM   6570  H HB3    . LEU A 1 429 ? -20.102 -18.691 -15.985 1.00 19.36  ?  429  LEU A HB3    1 
ATOM   6571  H HG     . LEU A 1 429 ? -18.830 -16.853 -16.810 1.00 19.66  ?  429  LEU A HG     1 
ATOM   6572  H HD11   . LEU A 1 429 ? -19.501 -15.884 -18.833 1.00 19.01  ?  429  LEU A HD11   1 
ATOM   6573  H HD12   . LEU A 1 429 ? -18.761 -17.274 -19.040 1.00 19.01  ?  429  LEU A HD12   1 
ATOM   6574  H HD13   . LEU A 1 429 ? -20.344 -17.194 -19.144 1.00 19.01  ?  429  LEU A HD13   1 
ATOM   6575  H HD21   . LEU A 1 429 ? -20.695 -15.388 -16.868 1.00 18.82  ?  429  LEU A HD21   1 
ATOM   6576  H HD22   . LEU A 1 429 ? -21.643 -16.659 -16.959 1.00 18.82  ?  429  LEU A HD22   1 
ATOM   6577  H HD23   . LEU A 1 429 ? -20.776 -16.407 -15.652 1.00 18.82  ?  429  LEU A HD23   1 
ATOM   6578  N N      . GLY A 1 430 ? -16.444 -18.866 -16.734 1.00 15.24  ?  430  GLY A N      1 
ATOM   6579  C CA     . GLY A 1 430 ? -15.255 -18.727 -15.916 1.00 14.80  ?  430  GLY A CA     1 
ATOM   6580  C C      . GLY A 1 430 ? -14.912 -17.281 -15.614 1.00 13.15  ?  430  GLY A C      1 
ATOM   6581  O O      . GLY A 1 430 ? -15.124 -16.383 -16.438 1.00 14.40  ?  430  GLY A O      1 
ATOM   6582  H H      . GLY A 1 430 ? -16.324 -18.648 -17.557 1.00 18.28  ?  430  GLY A H      1 
ATOM   6583  H HA2    . GLY A 1 430 ? -15.390 -19.188 -15.073 1.00 17.76  ?  430  GLY A HA2    1 
ATOM   6584  H HA3    . GLY A 1 430 ? -14.501 -19.127 -16.377 1.00 17.76  ?  430  GLY A HA3    1 
ATOM   6585  N N      . PHE A 1 431 ? -14.343 -17.070 -14.423 1.00 13.33  ?  431  PHE A N      1 
ATOM   6586  C CA     . PHE A 1 431 ? -13.944 -15.756 -13.935 1.00 12.67  ?  431  PHE A CA     1 
ATOM   6587  C C      . PHE A 1 431 ? -12.507 -15.825 -13.440 1.00 12.98  ?  431  PHE A C      1 
ATOM   6588  O O      . PHE A 1 431 ? -12.150 -16.725 -12.660 1.00 13.09  ?  431  PHE A O      1 
ATOM   6589  C CB     . PHE A 1 431 ? -14.836 -15.308 -12.764 1.00 14.80  ?  431  PHE A CB     1 
ATOM   6590  C CG     . PHE A 1 431 ? -16.276 -15.185 -13.131 1.00 13.42  ?  431  PHE A CG     1 
ATOM   6591  C CD1    . PHE A 1 431 ? -17.101 -16.287 -13.178 1.00 12.82  ?  431  PHE A CD1    1 
ATOM   6592  C CD2    . PHE A 1 431 ? -16.801 -13.946 -13.460 1.00 15.54  ?  431  PHE A CD2    1 
ATOM   6593  C CE1    . PHE A 1 431 ? -18.428 -16.161 -13.542 1.00 14.11  ?  431  PHE A CE1    1 
ATOM   6594  C CE2    . PHE A 1 431 ? -18.113 -13.823 -13.836 1.00 15.12  ?  431  PHE A CE2    1 
ATOM   6595  C CZ     . PHE A 1 431 ? -18.938 -14.930 -13.859 1.00 15.57  ?  431  PHE A CZ     1 
ATOM   6596  H H      . PHE A 1 431 ? -14.174 -17.700 -13.862 1.00 15.99  ?  431  PHE A H      1 
ATOM   6597  H HA     . PHE A 1 431 ? -14.010 -15.116 -14.661 1.00 15.20  ?  431  PHE A HA     1 
ATOM   6598  H HB2    . PHE A 1 431 ? -14.766 -15.959 -12.049 1.00 17.75  ?  431  PHE A HB2    1 
ATOM   6599  H HB3    . PHE A 1 431 ? -14.533 -14.440 -12.454 1.00 17.75  ?  431  PHE A HB3    1 
ATOM   6600  H HD1    . PHE A 1 431 ? -16.761 -17.125 -12.962 1.00 15.38  ?  431  PHE A HD1    1 
ATOM   6601  H HD2    . PHE A 1 431 ? -16.258 -13.191 -13.426 1.00 18.65  ?  431  PHE A HD2    1 
ATOM   6602  H HE1    . PHE A 1 431 ? -18.975 -16.912 -13.571 1.00 16.93  ?  431  PHE A HE1    1 
ATOM   6603  H HE2    . PHE A 1 431 ? -18.450 -12.990 -14.077 1.00 18.14  ?  431  PHE A HE2    1 
ATOM   6604  H HZ     . PHE A 1 431 ? -19.835 -14.841 -14.089 1.00 18.68  ?  431  PHE A HZ     1 
ATOM   6605  N N      . ALA A 1 432 ? -11.687 -14.869 -13.877 1.00 13.15  ?  432  ALA A N      1 
ATOM   6606  C CA     . ALA A 1 432 ? -10.303 -14.742 -13.406 1.00 12.83  ?  432  ALA A CA     1 
ATOM   6607  C C      . ALA A 1 432 ? -9.945  -13.264 -13.438 1.00 13.51  ?  432  ALA A C      1 
ATOM   6608  O O      . ALA A 1 432 ? -9.114  -12.829 -14.232 1.00 14.17  ?  432  ALA A O      1 
ATOM   6609  C CB     . ALA A 1 432 ? -9.346  -15.561 -14.276 1.00 12.98  ?  432  ALA A CB     1 
ATOM   6610  H H      . ALA A 1 432 ? -11.911 -14.273 -14.454 1.00 15.78  ?  432  ALA A H      1 
ATOM   6611  H HA     . ALA A 1 432 ? -10.231 -15.072 -12.497 1.00 15.40  ?  432  ALA A HA     1 
ATOM   6612  H HB1    . ALA A 1 432 ? -8.452  -15.504 -13.903 1.00 15.57  ?  432  ALA A HB1    1 
ATOM   6613  H HB2    . ALA A 1 432 ? -9.641  -16.484 -14.288 1.00 15.57  ?  432  ALA A HB2    1 
ATOM   6614  H HB3    . ALA A 1 432 ? -9.351  -15.200 -15.177 1.00 15.57  ?  432  ALA A HB3    1 
ATOM   6615  N N      . PRO A 1 433 ? -10.583 -12.458 -12.602 1.00 14.96  ?  433  PRO A N      1 
ATOM   6616  C CA     . PRO A 1 433 ? -10.444 -10.997 -12.739 1.00 14.65  ?  433  PRO A CA     1 
ATOM   6617  C C      . PRO A 1 433 ? -9.083  -10.536 -12.260 1.00 14.41  ?  433  PRO A C      1 
ATOM   6618  O O      . PRO A 1 433 ? -8.361  -11.279 -11.579 1.00 15.25  ?  433  PRO A O      1 
ATOM   6619  C CB     . PRO A 1 433 ? -11.568 -10.435 -11.857 1.00 16.96  ?  433  PRO A CB     1 
ATOM   6620  C CG     . PRO A 1 433 ? -11.905 -11.535 -10.906 1.00 18.94  ?  433  PRO A CG     1 
ATOM   6621  C CD     . PRO A 1 433 ? -11.575 -12.847 -11.577 1.00 15.35  ?  433  PRO A CD     1 
ATOM   6622  H HA     . PRO A 1 433 ? -10.586 -10.721 -13.658 1.00 17.58  ?  433  PRO A HA     1 
ATOM   6623  H HB2    . PRO A 1 433 ? -11.253 -9.651  -11.381 1.00 20.35  ?  433  PRO A HB2    1 
ATOM   6624  H HB3    . PRO A 1 433 ? -12.334 -10.204 -12.405 1.00 20.35  ?  433  PRO A HB3    1 
ATOM   6625  H HG2    . PRO A 1 433 ? -11.380 -11.430 -10.098 1.00 22.72  ?  433  PRO A HG2    1 
ATOM   6626  H HG3    . PRO A 1 433 ? -12.851 -11.495 -10.695 1.00 22.72  ?  433  PRO A HG3    1 
ATOM   6627  H HD2    . PRO A 1 433 ? -11.191 -13.472 -10.943 1.00 18.42  ?  433  PRO A HD2    1 
ATOM   6628  H HD3    . PRO A 1 433 ? -12.364 -13.234 -11.987 1.00 18.42  ?  433  PRO A HD3    1 
ATOM   6629  N N      . PRO A 1 434 ? -8.675  -9.330  -12.622 1.00 14.08  ?  434  PRO A N      1 
ATOM   6630  C CA     . PRO A 1 434 ? -7.380  -8.840  -12.139 1.00 14.04  ?  434  PRO A CA     1 
ATOM   6631  C C      . PRO A 1 434 ? -7.308  -8.857  -10.622 1.00 14.54  ?  434  PRO A C      1 
ATOM   6632  O O      . PRO A 1 434 ? -8.314  -8.720  -9.912  1.00 15.05  ?  434  PRO A O      1 
ATOM   6633  C CB     . PRO A 1 434 ? -7.303  -7.416  -12.697 1.00 13.19  ?  434  PRO A CB     1 
ATOM   6634  C CG     . PRO A 1 434 ? -8.186  -7.464  -13.937 1.00 15.30  ?  434  PRO A CG     1 
ATOM   6635  C CD     . PRO A 1 434 ? -9.346  -8.356  -13.506 1.00 15.02  ?  434  PRO A CD     1 
ATOM   6636  H HA     . PRO A 1 434 ? -6.653  -9.369  -12.503 1.00 16.85  ?  434  PRO A HA     1 
ATOM   6637  H HB2    . PRO A 1 434 ? -7.645  -6.782  -12.047 1.00 15.83  ?  434  PRO A HB2    1 
ATOM   6638  H HB3    . PRO A 1 434 ? -6.387  -7.194  -12.926 1.00 15.83  ?  434  PRO A HB3    1 
ATOM   6639  H HG2    . PRO A 1 434 ? -8.492  -6.573  -14.169 1.00 18.36  ?  434  PRO A HG2    1 
ATOM   6640  H HG3    . PRO A 1 434 ? -7.700  -7.852  -14.682 1.00 18.36  ?  434  PRO A HG3    1 
ATOM   6641  H HD2    . PRO A 1 434 ? -10.017 -7.848  -13.023 1.00 18.02  ?  434  PRO A HD2    1 
ATOM   6642  H HD3    . PRO A 1 434 ? -9.751  -8.797  -14.270 1.00 18.02  ?  434  PRO A HD3    1 
ATOM   6643  N N      . LEU A 1 435 ? -6.081  -9.007  -10.109 1.00 13.72  ?  435  LEU A N      1 
ATOM   6644  C CA     . LEU A 1 435 ? -5.893  -9.103  -8.660  1.00 13.77  ?  435  LEU A CA     1 
ATOM   6645  C C      . LEU A 1 435 ? -6.077  -7.785  -7.932  1.00 15.17  ?  435  LEU A C      1 
ATOM   6646  O O      . LEU A 1 435 ? -6.070  -7.793  -6.698  1.00 17.26  ?  435  LEU A O      1 
ATOM   6647  C CB     . LEU A 1 435 ? -4.528  -9.705  -8.347  1.00 15.62  ?  435  LEU A CB     1 
ATOM   6648  C CG     . LEU A 1 435 ? -4.216  -11.007 -9.083  1.00 14.04  ?  435  LEU A CG     1 
ATOM   6649  C CD1    . LEU A 1 435 ? -2.890  -11.584 -8.577  1.00 14.82  ?  435  LEU A CD1    1 
ATOM   6650  C CD2    . LEU A 1 435 ? -5.299  -12.094 -9.016  1.00 15.63  ?  435  LEU A CD2    1 
ATOM   6651  H H      . LEU A 1 435 ? -5.357  -9.056  -10.570 1.00 16.46  ?  435  LEU A H      1 
ATOM   6652  H HA     . LEU A 1 435 ? -6.565  -9.706  -8.308  1.00 16.52  ?  435  LEU A HA     1 
ATOM   6653  H HB2    . LEU A 1 435 ? -3.845  -9.060  -8.591  1.00 18.74  ?  435  LEU A HB2    1 
ATOM   6654  H HB3    . LEU A 1 435 ? -4.484  -9.889  -7.396  1.00 18.74  ?  435  LEU A HB3    1 
ATOM   6655  H HG     . LEU A 1 435 ? -4.165  -10.764 -10.021 1.00 16.84  ?  435  LEU A HG     1 
ATOM   6656  H HD11   . LEU A 1 435 ? -2.699  -12.405 -9.056  1.00 17.78  ?  435  LEU A HD11   1 
ATOM   6657  H HD12   . LEU A 1 435 ? -2.184  -10.937 -8.734  1.00 17.78  ?  435  LEU A HD12   1 
ATOM   6658  H HD13   . LEU A 1 435 ? -2.966  -11.765 -7.627  1.00 17.78  ?  435  LEU A HD13   1 
ATOM   6659  H HD21   . LEU A 1 435 ? -5.014  -12.857 -9.543  1.00 18.75  ?  435  LEU A HD21   1 
ATOM   6660  H HD22   . LEU A 1 435 ? -5.425  -12.358 -8.091  1.00 18.75  ?  435  LEU A HD22   1 
ATOM   6661  H HD23   . LEU A 1 435 ? -6.127  -11.736 -9.373  1.00 18.75  ?  435  LEU A HD23   1 
ATOM   6662  N N      . VAL A 1 436 ? -6.241  -6.676  -8.661  1.00 14.62  ?  436  VAL A N      1 
ATOM   6663  C CA     . VAL A 1 436 ? -6.587  -5.379  -8.074  1.00 14.98  ?  436  VAL A CA     1 
ATOM   6664  C C      . VAL A 1 436 ? -8.083  -5.205  -7.865  1.00 15.88  ?  436  VAL A C      1 
ATOM   6665  O O      . VAL A 1 436 ? -8.505  -4.175  -7.329  1.00 17.97  ?  436  VAL A O      1 
ATOM   6666  C CB     . VAL A 1 436 ? -6.062  -4.227  -8.956  1.00 16.07  ?  436  VAL A CB     1 
ATOM   6667  C CG1    . VAL A 1 436 ? -4.530  -4.220  -9.026  1.00 17.47  ?  436  VAL A CG1    1 
ATOM   6668  C CG2    . VAL A 1 436 ? -6.652  -4.302  -10.372 1.00 15.32  ?  436  VAL A CG2    1 
ATOM   6669  H H      . VAL A 1 436 ? -6.155  -6.648  -9.516  1.00 17.54  ?  436  VAL A H      1 
ATOM   6670  H HA     . VAL A 1 436 ? -6.163  -5.324  -7.203  1.00 17.97  ?  436  VAL A HA     1 
ATOM   6671  H HB     . VAL A 1 436 ? -6.347  -3.396  -8.545  1.00 19.28  ?  436  VAL A HB     1 
ATOM   6672  H HG11   . VAL A 1 436 ? -4.242  -3.461  -9.558  1.00 20.96  ?  436  VAL A HG11   1 
ATOM   6673  H HG12   . VAL A 1 436 ? -4.173  -4.148  -8.127  1.00 20.96  ?  436  VAL A HG12   1 
ATOM   6674  H HG13   . VAL A 1 436 ? -4.229  -5.045  -9.437  1.00 20.96  ?  436  VAL A HG13   1 
ATOM   6675  H HG21   . VAL A 1 436 ? -6.397  -3.505  -10.863 1.00 18.38  ?  436  VAL A HG21   1 
ATOM   6676  H HG22   . VAL A 1 436 ? -6.303  -5.090  -10.818 1.00 18.38  ?  436  VAL A HG22   1 
ATOM   6677  H HG23   . VAL A 1 436 ? -7.618  -4.358  -10.310 1.00 18.38  ?  436  VAL A HG23   1 
ATOM   6678  N N      . THR A 1 437 ? -8.906  -6.161  -8.294  1.00 15.24  ?  437  THR A N      1 
ATOM   6679  C CA     . THR A 1 437 ? -10.354 -6.002  -8.217  1.00 14.21  ?  437  THR A CA     1 
ATOM   6680  C C      . THR A 1 437 ? -10.786 -5.739  -6.775  1.00 15.73  ?  437  THR A C      1 
ATOM   6681  O O      . THR A 1 437 ? -10.310 -6.393  -5.844  1.00 16.42  ?  437  THR A O      1 
ATOM   6682  C CB     . THR A 1 437 ? -11.035 -7.279  -8.736  1.00 15.97  ?  437  THR A CB     1 
ATOM   6683  O OG1    . THR A 1 437 ? -10.651 -7.511  -10.098 1.00 15.54  ?  437  THR A OG1    1 
ATOM   6684  C CG2    . THR A 1 437 ? -12.537 -7.161  -8.669  1.00 18.02  ?  437  THR A CG2    1 
ATOM   6685  H H      . THR A 1 437 ? -8.653  -6.910  -8.633  1.00 18.28  ?  437  THR A H      1 
ATOM   6686  H HA     . THR A 1 437 ? -10.631 -5.249  -8.762  1.00 17.05  ?  437  THR A HA     1 
ATOM   6687  H HB     . THR A 1 437 ? -10.763 -8.027  -8.182  1.00 19.16  ?  437  THR A HB     1 
ATOM   6688  H HG1    . THR A 1 437 ? -9.828  -7.676  -10.140 1.00 18.65  ?  437  THR A HG1    1 
ATOM   6689  H HG21   . THR A 1 437 ? -12.950 -7.920  -9.111  1.00 21.62  ?  437  THR A HG21   1 
ATOM   6690  H HG22   . THR A 1 437 ? -12.828 -7.139  -7.744  1.00 21.62  ?  437  THR A HG22   1 
ATOM   6691  H HG23   . THR A 1 437 ? -12.826 -6.346  -9.110  1.00 21.62  ?  437  THR A HG23   1 
ATOM   6692  N N      . THR A 1 438 ? -11.720 -4.802  -6.598  1.00 16.23  ?  438  THR A N      1 
ATOM   6693  C CA     . THR A 1 438 ? -12.227 -4.445  -5.285  1.00 17.51  ?  438  THR A CA     1 
ATOM   6694  C C      . THR A 1 438 ? -13.541 -5.182  -4.993  1.00 17.60  ?  438  THR A C      1 
ATOM   6695  O O      . THR A 1 438 ? -14.139 -5.804  -5.868  1.00 17.40  ?  438  THR A O      1 
ATOM   6696  C CB     . THR A 1 438 ? -12.520 -2.941  -5.186  1.00 18.89  ?  438  THR A CB     1 
ATOM   6697  O OG1    . THR A 1 438 ? -13.613 -2.640  -6.073  1.00 18.46  ?  438  THR A OG1    1 
ATOM   6698  C CG2    . THR A 1 438 ? -11.313 -2.074  -5.534  1.00 20.74  ?  438  THR A CG2    1 
ATOM   6699  H H      . THR A 1 438 ? -12.077 -4.356  -7.241  1.00 19.47  ?  438  THR A H      1 
ATOM   6700  H HA     . THR A 1 438 ? -11.547 -4.690  -4.638  1.00 21.01  ?  438  THR A HA     1 
ATOM   6701  H HB     . THR A 1 438 ? -12.745 -2.722  -4.268  1.00 22.67  ?  438  THR A HB     1 
ATOM   6702  H HG1    . THR A 1 438 ? -13.817 -1.828  -6.012  1.00 22.15  ?  438  THR A HG1    1 
ATOM   6703  H HG21   . THR A 1 438 ? -11.520 -1.139  -5.374  1.00 24.88  ?  438  THR A HG21   1 
ATOM   6704  H HG22   . THR A 1 438 ? -10.554 -2.326  -4.985  1.00 24.88  ?  438  THR A HG22   1 
ATOM   6705  H HG23   . THR A 1 438 ? -11.080 -2.190  -6.468  1.00 24.88  ?  438  THR A HG23   1 
ATOM   6706  N N      . ARG A 1 439 ? -14.009 -5.072  -3.748  1.00 18.04  ?  439  ARG A N      1 
ATOM   6707  C CA     . ARG A 1 439 ? -15.284 -5.700  -3.406  1.00 18.18  ?  439  ARG A CA     1 
ATOM   6708  C C      . ARG A 1 439 ? -16.433 -5.095  -4.198  1.00 17.16  ?  439  ARG A C      1 
ATOM   6709  O O      . ARG A 1 439 ? -17.338 -5.814  -4.656  1.00 16.94  ?  439  ARG A O      1 
ATOM   6710  C CB     . ARG A 1 439 ? -15.553 -5.574  -1.910  1.00 20.28  ?  439  ARG A CB     1 
ATOM   6711  C CG     . ARG A 1 439 ? -14.641 -6.434  -1.074  1.00 23.06  ?  439  ARG A CG     1 
ATOM   6712  C CD     . ARG A 1 439 ? -14.983 -6.394  0.415   1.00 28.68  ?  439  ARG A CD     1 
ATOM   6713  N NE     . ARG A 1 439 ? -14.160 -7.399  1.078   1.00 34.88  ?  439  ARG A NE     1 
ATOM   6714  C CZ     . ARG A 1 439 ? -14.602 -8.308  1.938   1.00 38.80  ?  439  ARG A CZ     1 
ATOM   6715  N NH1    . ARG A 1 439 ? -15.876 -8.332  2.323   1.00 37.94  ?  439  ARG A NH1    1 
ATOM   6716  N NH2    . ARG A 1 439 ? -13.741 -9.178  2.450   1.00 41.79  ?  439  ARG A NH2    1 
ATOM   6717  H H      . ARG A 1 439 ? -13.623 -4.655  -3.103  1.00 21.64  ?  439  ARG A H      1 
ATOM   6718  H HA     . ARG A 1 439 ? -15.227 -6.643  -3.624  1.00 21.82  ?  439  ARG A HA     1 
ATOM   6719  H HB2    . ARG A 1 439 ? -15.422 -4.651  -1.644  1.00 24.34  ?  439  ARG A HB2    1 
ATOM   6720  H HB3    . ARG A 1 439 ? -16.467 -5.844  -1.731  1.00 24.34  ?  439  ARG A HB3    1 
ATOM   6721  H HG2    . ARG A 1 439 ? -14.713 -7.354  -1.372  1.00 27.67  ?  439  ARG A HG2    1 
ATOM   6722  H HG3    . ARG A 1 439 ? -13.728 -6.122  -1.179  1.00 27.67  ?  439  ARG A HG3    1 
ATOM   6723  H HD2    . ARG A 1 439 ? -14.782 -5.519  0.783   1.00 34.41  ?  439  ARG A HD2    1 
ATOM   6724  H HD3    . ARG A 1 439 ? -15.920 -6.604  0.550   1.00 34.41  ?  439  ARG A HD3    1 
ATOM   6725  H HE     . ARG A 1 439 ? -13.320 -7.402  0.898   1.00 41.86  ?  439  ARG A HE     1 
ATOM   6726  H HH11   . ARG A 1 439 ? -16.430 -7.751  2.013   1.00 45.53  ?  439  ARG A HH11   1 
ATOM   6727  H HH12   . ARG A 1 439 ? -16.145 -8.928  2.881   1.00 45.53  ?  439  ARG A HH12   1 
ATOM   6728  H HH21   . ARG A 1 439 ? -12.912 -9.146  2.224   1.00 50.15  ?  439  ARG A HH21   1 
ATOM   6729  H HH22   . ARG A 1 439 ? -14.012 -9.773  3.009   1.00 50.15  ?  439  ARG A HH22   1 
ATOM   6730  N N      . ALA A 1 440 ? -16.415 -3.770  -4.372  1.00 18.20  ?  440  ALA A N      1 
ATOM   6731  C CA     . ALA A 1 440 ? -17.461 -3.119  -5.146  1.00 18.43  ?  440  ALA A CA     1 
ATOM   6732  C C      . ALA A 1 440 ? -17.454 -3.611  -6.583  1.00 17.75  ?  440  ALA A C      1 
ATOM   6733  O O      . ALA A 1 440 ? -18.515 -3.815  -7.179  1.00 17.98  ?  440  ALA A O      1 
ATOM   6734  C CB     . ALA A 1 440 ? -17.263 -1.611  -5.099  1.00 17.90  ?  440  ALA A CB     1 
ATOM   6735  H H      . ALA A 1 440 ? -15.817 -3.237  -4.058  1.00 21.83  ?  440  ALA A H      1 
ATOM   6736  H HA     . ALA A 1 440 ? -18.325 -3.327  -4.758  1.00 22.11  ?  440  ALA A HA     1 
ATOM   6737  H HB1    . ALA A 1 440 ? -17.983 -1.183  -5.589  1.00 21.47  ?  440  ALA A HB1    1 
ATOM   6738  H HB2    . ALA A 1 440 ? -17.274 -1.319  -4.174  1.00 21.47  ?  440  ALA A HB2    1 
ATOM   6739  H HB3    . ALA A 1 440 ? -16.410 -1.391  -5.505  1.00 21.47  ?  440  ALA A HB3    1 
ATOM   6740  N N      . GLU A 1 441 ? -16.264 -3.828  -7.151  1.00 17.30  ?  441  GLU A N      1 
ATOM   6741  C CA     . GLU A 1 441 ? -16.179 -4.364  -8.506  1.00 16.91  ?  441  GLU A CA     1 
ATOM   6742  C C      . GLU A 1 441 ? -16.659 -5.816  -8.558  1.00 14.73  ?  441  GLU A C      1 
ATOM   6743  O O      . GLU A 1 441 ? -17.327 -6.218  -9.520  1.00 16.32  ?  441  GLU A O      1 
ATOM   6744  C CB     . GLU A 1 441 ? -14.756 -4.208  -9.046  1.00 16.60  ?  441  GLU A CB     1 
ATOM   6745  C CG     . GLU A 1 441 ? -14.414 -2.734  -9.330  1.00 18.46  ?  441  GLU A CG     1 
ATOM   6746  C CD     . GLU A 1 441 ? -12.934 -2.452  -9.536  1.00 21.12  ?  441  GLU A CD     1 
ATOM   6747  O OE1    . GLU A 1 441 ? -12.088 -3.245  -9.054  1.00 18.86  ?  441  GLU A OE1    1 
ATOM   6748  O OE2    . GLU A 1 441 ? -12.626 -1.414  -10.176 1.00 22.09  -1 441  GLU A OE2    1 
ATOM   6749  H H      . GLU A 1 441 ? -15.504 -3.676  -6.780  1.00 20.75  ?  441  GLU A H      1 
ATOM   6750  H HA     . GLU A 1 441 ? -16.759 -3.853  -9.092  1.00 20.29  ?  441  GLU A HA     1 
ATOM   6751  H HB2    . GLU A 1 441 ? -14.126 -4.546  -8.391  1.00 19.91  ?  441  GLU A HB2    1 
ATOM   6752  H HB3    . GLU A 1 441 ? -14.672 -4.705  -9.875  1.00 19.91  ?  441  GLU A HB3    1 
ATOM   6753  H HG2    . GLU A 1 441 ? -14.878 -2.459  -10.136 1.00 22.15  ?  441  GLU A HG2    1 
ATOM   6754  H HG3    . GLU A 1 441 ? -14.711 -2.198  -8.578  1.00 22.15  ?  441  GLU A HG3    1 
ATOM   6755  N N      . VAL A 1 442 ? -16.347 -6.622  -7.533  1.00 15.31  ?  442  VAL A N      1 
ATOM   6756  C CA     . VAL A 1 442 ? -16.935 -7.961  -7.449  1.00 14.99  ?  442  VAL A CA     1 
ATOM   6757  C C      . VAL A 1 442 ? -18.456 -7.875  -7.509  1.00 16.52  ?  442  VAL A C      1 
ATOM   6758  O O      . VAL A 1 442 ? -19.116 -8.633  -8.227  1.00 16.36  ?  442  VAL A O      1 
ATOM   6759  C CB     . VAL A 1 442 ? -16.464 -8.681  -6.175  1.00 15.27  ?  442  VAL A CB     1 
ATOM   6760  C CG1    . VAL A 1 442 ? -17.358 -9.876  -5.907  1.00 15.92  ?  442  VAL A CG1    1 
ATOM   6761  C CG2    . VAL A 1 442 ? -15.000 -9.112  -6.310  1.00 16.98  ?  442  VAL A CG2    1 
ATOM   6762  H H      . VAL A 1 442 ? -15.811 -6.422  -6.891  1.00 18.37  ?  442  VAL A H      1 
ATOM   6763  H HA     . VAL A 1 442 ? -16.632 -8.477  -8.213  1.00 17.98  ?  442  VAL A HA     1 
ATOM   6764  H HB     . VAL A 1 442 ? -16.522 -8.076  -5.419  1.00 18.33  ?  442  VAL A HB     1 
ATOM   6765  H HG11   . VAL A 1 442 ? -16.917 -10.464 -5.273  1.00 19.10  ?  442  VAL A HG11   1 
ATOM   6766  H HG12   . VAL A 1 442 ? -18.199 -9.565  -5.539  1.00 19.10  ?  442  VAL A HG12   1 
ATOM   6767  H HG13   . VAL A 1 442 ? -17.514 -10.346 -6.741  1.00 19.10  ?  442  VAL A HG13   1 
ATOM   6768  H HG21   . VAL A 1 442 ? -14.704 -9.496  -5.470  1.00 20.37  ?  442  VAL A HG21   1 
ATOM   6769  H HG22   . VAL A 1 442 ? -14.929 -9.772  -7.018  1.00 20.37  ?  442  VAL A HG22   1 
ATOM   6770  H HG23   . VAL A 1 442 ? -14.461 -8.336  -6.527  1.00 20.37  ?  442  VAL A HG23   1 
ATOM   6771  N N      . ASP A 1 443 ? -19.037 -6.946  -6.750  1.00 16.30  ?  443  ASP A N      1 
ATOM   6772  C CA     . ASP A 1 443 ? -20.493 -6.841  -6.743  1.00 16.71  ?  443  ASP A CA     1 
ATOM   6773  C C      . ASP A 1 443 ? -21.022 -6.565  -8.145  1.00 16.74  ?  443  ASP A C      1 
ATOM   6774  O O      . ASP A 1 443 ? -22.048 -7.123  -8.553  1.00 17.16  ?  443  ASP A O      1 
ATOM   6775  C CB     . ASP A 1 443 ? -20.953 -5.716  -5.811  1.00 18.11  ?  443  ASP A CB     1 
ATOM   6776  C CG     . ASP A 1 443 ? -20.748 -6.026  -4.348  1.00 19.74  ?  443  ASP A CG     1 
ATOM   6777  O OD1    . ASP A 1 443 ? -20.589 -7.207  -3.982  1.00 20.14  ?  443  ASP A OD1    1 
ATOM   6778  O OD2    . ASP A 1 443 ? -20.786 -5.059  -3.554  1.00 21.87  -1 443  ASP A OD2    1 
ATOM   6779  H H      . ASP A 1 443 ? -18.627 -6.383  -6.247  1.00 19.55  ?  443  ASP A H      1 
ATOM   6780  H HA     . ASP A 1 443 ? -20.852 -7.680  -6.415  1.00 20.04  ?  443  ASP A HA     1 
ATOM   6781  H HB2    . ASP A 1 443 ? -20.451 -4.913  -6.017  1.00 21.73  ?  443  ASP A HB2    1 
ATOM   6782  H HB3    . ASP A 1 443 ? -21.900 -5.561  -5.951  1.00 21.73  ?  443  ASP A HB3    1 
ATOM   6783  N N      . GLU A 1 444 ? -20.331 -5.707  -8.900  1.00 17.11  ?  444  GLU A N      1 
ATOM   6784  C CA     . GLU A 1 444 ? -20.782 -5.363  -10.244 1.00 18.19  ?  444  GLU A CA     1 
ATOM   6785  C C      . GLU A 1 444 ? -20.608 -6.534  -11.211 1.00 16.76  ?  444  GLU A C      1 
ATOM   6786  O O      . GLU A 1 444 ? -21.477 -6.781  -12.060 1.00 17.87  ?  444  GLU A O      1 
ATOM   6787  C CB     . GLU A 1 444 ? -20.043 -4.117  -10.716 1.00 21.09  ?  444  GLU A CB     1 
ATOM   6788  C CG     . GLU A 1 444 ? -20.488 -3.603  -12.050 1.00 24.72  ?  444  GLU A CG     1 
ATOM   6789  C CD     . GLU A 1 444 ? -21.948 -3.159  -12.065 1.00 26.57  ?  444  GLU A CD     1 
ATOM   6790  O OE1    . GLU A 1 444 ? -22.487 -2.817  -10.981 1.00 30.51  ?  444  GLU A OE1    1 
ATOM   6791  O OE2    . GLU A 1 444 ? -22.547 -3.139  -13.162 1.00 27.46  -1 444  GLU A OE2    1 
ATOM   6792  H H      . GLU A 1 444 ? -19.605 -5.314  -8.659  1.00 20.52  ?  444  GLU A H      1 
ATOM   6793  H HA     . GLU A 1 444 ? -21.729 -5.156  -10.229 1.00 21.83  ?  444  GLU A HA     1 
ATOM   6794  H HB2    . GLU A 1 444 ? -20.183 -3.409  -10.067 1.00 25.30  ?  444  GLU A HB2    1 
ATOM   6795  H HB3    . GLU A 1 444 ? -19.097 -4.324  -10.782 1.00 25.30  ?  444  GLU A HB3    1 
ATOM   6796  H HG2    . GLU A 1 444 ? -19.941 -2.839  -12.292 1.00 29.65  ?  444  GLU A HG2    1 
ATOM   6797  H HG3    . GLU A 1 444 ? -20.384 -4.307  -12.709 1.00 29.65  ?  444  GLU A HG3    1 
ATOM   6798  N N      . ILE A 1 445 ? -19.495 -7.265  -11.099 1.00 16.74  ?  445  ILE A N      1 
ATOM   6799  C CA     . ILE A 1 445 ? -19.291 -8.447  -11.925 1.00 15.53  ?  445  ILE A CA     1 
ATOM   6800  C C      . ILE A 1 445 ? -20.410 -9.443  -11.677 1.00 16.08  ?  445  ILE A C      1 
ATOM   6801  O O      . ILE A 1 445 ? -21.008 -9.988  -12.615 1.00 16.02  ?  445  ILE A O      1 
ATOM   6802  C CB     . ILE A 1 445 ? -17.915 -9.065  -11.619 1.00 15.76  ?  445  ILE A CB     1 
ATOM   6803  C CG1    . ILE A 1 445 ? -16.799 -8.172  -12.201 1.00 17.00  ?  445  ILE A CG1    1 
ATOM   6804  C CG2    . ILE A 1 445 ? -17.790 -10.506 -12.140 1.00 17.46  ?  445  ILE A CG2    1 
ATOM   6805  C CD1    . ILE A 1 445 ? -15.399 -8.510  -11.652 1.00 18.36  ?  445  ILE A CD1    1 
ATOM   6806  H H      . ILE A 1 445 ? -18.849 -7.097  -10.557 1.00 20.08  ?  445  ILE A H      1 
ATOM   6807  H HA     . ILE A 1 445 ? -19.311 -8.193  -12.861 1.00 18.63  ?  445  ILE A HA     1 
ATOM   6808  H HB     . ILE A 1 445 ? -17.823 -9.108  -10.654 1.00 18.90  ?  445  ILE A HB     1 
ATOM   6809  H HG12   . ILE A 1 445 ? -16.777 -8.285  -13.164 1.00 20.40  ?  445  ILE A HG12   1 
ATOM   6810  H HG13   . ILE A 1 445 ? -16.990 -7.247  -11.979 1.00 20.40  ?  445  ILE A HG13   1 
ATOM   6811  H HG21   . ILE A 1 445 ? -16.851 -10.744 -12.188 1.00 20.95  ?  445  ILE A HG21   1 
ATOM   6812  H HG22   . ILE A 1 445 ? -18.252 -11.103 -11.531 1.00 20.95  ?  445  ILE A HG22   1 
ATOM   6813  H HG23   . ILE A 1 445 ? -18.190 -10.558 -13.022 1.00 20.95  ?  445  ILE A HG23   1 
ATOM   6814  H HD11   . ILE A 1 445 ? -14.789 -7.791  -11.879 1.00 22.03  ?  445  ILE A HD11   1 
ATOM   6815  H HD12   . ILE A 1 445 ? -15.453 -8.607  -10.688 1.00 22.03  ?  445  ILE A HD12   1 
ATOM   6816  H HD13   . ILE A 1 445 ? -15.096 -9.340  -12.052 1.00 22.03  ?  445  ILE A HD13   1 
ATOM   6817  N N      . VAL A 1 446 ? -20.708 -9.694  -10.403 1.00 15.75  ?  446  VAL A N      1 
ATOM   6818  C CA     . VAL A 1 446 ? -21.730 -10.670 -10.045 1.00 15.28  ?  446  VAL A CA     1 
ATOM   6819  C C      . VAL A 1 446 ? -23.099 -10.239 -10.554 1.00 15.40  ?  446  VAL A C      1 
ATOM   6820  O O      . VAL A 1 446 ? -23.864 -11.064 -11.069 1.00 16.42  ?  446  VAL A O      1 
ATOM   6821  C CB     . VAL A 1 446 ? -21.714 -10.924 -8.527  1.00 17.80  ?  446  VAL A CB     1 
ATOM   6822  C CG1    . VAL A 1 446 ? -22.916 -11.741 -8.087  1.00 19.59  ?  446  VAL A CG1    1 
ATOM   6823  C CG2    . VAL A 1 446 ? -20.413 -11.631 -8.144  1.00 18.71  ?  446  VAL A CG2    1 
ATOM   6824  H H      . VAL A 1 446 ? -20.334 -9.314  -9.728  1.00 18.90  ?  446  VAL A H      1 
ATOM   6825  H HA     . VAL A 1 446 ? -21.523 -11.510 -10.483 1.00 18.33  ?  446  VAL A HA     1 
ATOM   6826  H HB     . VAL A 1 446 ? -21.763 -10.072 -8.066  1.00 21.35  ?  446  VAL A HB     1 
ATOM   6827  H HG11   . VAL A 1 446 ? -22.753 -12.086 -7.195  1.00 23.50  ?  446  VAL A HG11   1 
ATOM   6828  H HG12   . VAL A 1 446 ? -23.701 -11.172 -8.084  1.00 23.50  ?  446  VAL A HG12   1 
ATOM   6829  H HG13   . VAL A 1 446 ? -23.042 -12.476 -8.708  1.00 23.50  ?  446  VAL A HG13   1 
ATOM   6830  H HG21   . VAL A 1 446 ? -20.403 -11.776 -7.185  1.00 22.45  ?  446  VAL A HG21   1 
ATOM   6831  H HG22   . VAL A 1 446 ? -20.368 -12.483 -8.607  1.00 22.45  ?  446  VAL A HG22   1 
ATOM   6832  H HG23   . VAL A 1 446 ? -19.663 -11.074 -8.403  1.00 22.45  ?  446  VAL A HG23   1 
ATOM   6833  N N      . ALA A 1 447 ? -23.429 -8.948  -10.420 1.00 15.93  ?  447  ALA A N      1 
ATOM   6834  C CA     . ALA A 1 447 ? -24.720 -8.449  -10.874 1.00 16.03  ?  447  ALA A CA     1 
ATOM   6835  C C      . ALA A 1 447 ? -24.870 -8.599  -12.384 1.00 16.48  ?  447  ALA A C      1 
ATOM   6836  O O      . ALA A 1 447 ? -25.938 -8.974  -12.870 1.00 16.48  ?  447  ALA A O      1 
ATOM   6837  C CB     . ALA A 1 447 ? -24.889 -6.975  -10.476 1.00 17.88  ?  447  ALA A CB     1 
ATOM   6838  H H      . ALA A 1 447 ? -22.924 -8.346  -10.071 1.00 19.11  ?  447  ALA A H      1 
ATOM   6839  H HA     . ALA A 1 447 ? -25.418 -8.966  -10.441 1.00 19.23  ?  447  ALA A HA     1 
ATOM   6840  H HB1    . ALA A 1 447 ? -25.770 -6.674  -10.748 1.00 21.46  ?  447  ALA A HB1    1 
ATOM   6841  H HB2    . ALA A 1 447 ? -24.794 -6.895  -9.514  1.00 21.46  ?  447  ALA A HB2    1 
ATOM   6842  H HB3    . ALA A 1 447 ? -24.207 -6.448  -10.921 1.00 21.46  ?  447  ALA A HB3    1 
ATOM   6843  N N      . ARG A 1 448 ? -23.821 -8.286  -13.142 1.00 16.77  ?  448  ARG A N      1 
ATOM   6844  C CA     . ARG A 1 448 ? -23.885 -8.450  -14.594 1.00 15.71  ?  448  ARG A CA     1 
ATOM   6845  C C      . ARG A 1 448 ? -23.978 -9.917  -14.974 1.00 16.51  ?  448  ARG A C      1 
ATOM   6846  O O      . ARG A 1 448 ? -24.737 -10.282 -15.873 1.00 16.78  ?  448  ARG A O      1 
ATOM   6847  C CB     . ARG A 1 448 ? -22.668 -7.795  -15.253 1.00 17.44  ?  448  ARG A CB     1 
ATOM   6848  C CG     . ARG A 1 448 ? -22.637 -6.292  -15.045 1.00 18.22  ?  448  ARG A CG     1 
ATOM   6849  C CD     . ARG A 1 448 ? -21.463 -5.602  -15.731 1.00 21.17  ?  448  ARG A CD     1 
ATOM   6850  N NE     . ARG A 1 448 ? -21.500 -4.174  -15.440 1.00 22.56  ?  448  ARG A NE     1 
ATOM   6851  C CZ     . ARG A 1 448 ? -20.812 -3.238  -16.088 1.00 24.61  ?  448  ARG A CZ     1 
ATOM   6852  N NH1    . ARG A 1 448 ? -20.002 -3.560  -17.094 1.00 27.07  ?  448  ARG A NH1    1 
ATOM   6853  N NH2    . ARG A 1 448 ? -20.929 -1.971  -15.720 1.00 28.46  ?  448  ARG A NH2    1 
ATOM   6854  H H      . ARG A 1 448 ? -23.071 -7.983  -12.849 1.00 20.13  ?  448  ARG A H      1 
ATOM   6855  H HA     . ARG A 1 448 ? -24.679 -8.002  -14.927 1.00 18.84  ?  448  ARG A HA     1 
ATOM   6856  H HB2    . ARG A 1 448 ? -21.860 -8.170  -14.869 1.00 20.92  ?  448  ARG A HB2    1 
ATOM   6857  H HB3    . ARG A 1 448 ? -22.693 -7.967  -16.207 1.00 20.92  ?  448  ARG A HB3    1 
ATOM   6858  H HG2    . ARG A 1 448 ? -23.454 -5.910  -15.402 1.00 21.86  ?  448  ARG A HG2    1 
ATOM   6859  H HG3    . ARG A 1 448 ? -22.572 -6.109  -14.095 1.00 21.86  ?  448  ARG A HG3    1 
ATOM   6860  H HD2    . ARG A 1 448 ? -20.627 -5.967  -15.399 1.00 25.40  ?  448  ARG A HD2    1 
ATOM   6861  H HD3    . ARG A 1 448 ? -21.522 -5.728  -16.691 1.00 25.40  ?  448  ARG A HD3    1 
ATOM   6862  H HE     . ARG A 1 448 ? -22.009 -3.915  -14.797 1.00 27.07  ?  448  ARG A HE     1 
ATOM   6863  H HH11   . ARG A 1 448 ? -19.919 -4.382  -17.333 1.00 32.48  ?  448  ARG A HH11   1 
ATOM   6864  H HH12   . ARG A 1 448 ? -19.563 -2.946  -17.505 1.00 32.48  ?  448  ARG A HH12   1 
ATOM   6865  H HH21   . ARG A 1 448 ? -21.447 -1.759  -15.067 1.00 34.15  ?  448  ARG A HH21   1 
ATOM   6866  H HH22   . ARG A 1 448 ? -20.487 -1.360  -16.134 1.00 34.15  ?  448  ARG A HH22   1 
ATOM   6867  N N      . ALA A 1 449 ? -23.214 -10.778 -14.298 1.00 16.44  ?  449  ALA A N      1 
ATOM   6868  C CA     . ALA A 1 449 ? -23.297 -12.208 -14.564 1.00 15.53  ?  449  ALA A CA     1 
ATOM   6869  C C      . ALA A 1 449 ? -24.701 -12.730 -14.279 1.00 14.97  ?  449  ALA A C      1 
ATOM   6870  O O      . ALA A 1 449 ? -25.237 -13.548 -15.043 1.00 14.86  ?  449  ALA A O      1 
ATOM   6871  C CB     . ALA A 1 449 ? -22.259 -12.966 -13.727 1.00 16.07  ?  449  ALA A CB     1 
ATOM   6872  H H      . ALA A 1 449 ? -22.647 -10.563 -13.689 1.00 19.72  ?  449  ALA A H      1 
ATOM   6873  H HA     . ALA A 1 449 ? -23.095 -12.368 -15.499 1.00 18.64  ?  449  ALA A HA     1 
ATOM   6874  H HB1    . ALA A 1 449 ? -22.305 -13.910 -13.945 1.00 19.28  ?  449  ALA A HB1    1 
ATOM   6875  H HB2    . ALA A 1 449 ? -21.376 -12.621 -13.932 1.00 19.28  ?  449  ALA A HB2    1 
ATOM   6876  H HB3    . ALA A 1 449 ? -22.455 -12.834 -12.786 1.00 19.28  ?  449  ALA A HB3    1 
ATOM   6877  N N      . LYS A 1 450 ? -25.327 -12.242 -13.205 1.00 14.36  ?  450  LYS A N      1 
ATOM   6878  C CA     . LYS A 1 450 ? -26.672 -12.686 -12.862 1.00 15.78  ?  450  LYS A CA     1 
ATOM   6879  C C      . LYS A 1 450 ? -27.654 -12.345 -13.977 1.00 15.42  ?  450  LYS A C      1 
ATOM   6880  O O      . LYS A 1 450 ? -28.488 -13.181 -14.364 1.00 15.54  ?  450  LYS A O      1 
ATOM   6881  C CB     . LYS A 1 450 ? -27.113 -12.074 -11.538 1.00 15.97  ?  450  LYS A CB     1 
ATOM   6882  C CG     . LYS A 1 450 ? -28.544 -12.384 -11.113 1.00 20.47  ?  450  LYS A CG     1 
ATOM   6883  C CD     . LYS A 1 450 ? -28.812 -13.856 -11.063 1.00 27.94  ?  450  LYS A CD     1 
ATOM   6884  C CE     . LYS A 1 450 ? -29.862 -14.174 -10.002 1.00 32.12  ?  450  LYS A CE     1 
ATOM   6885  N NZ     . LYS A 1 450 ? -31.087 -13.369 -10.184 1.00 32.85  ?  450  LYS A NZ     1 
ATOM   6886  H H      . LYS A 1 450 ? -24.998 -11.658 -12.665 1.00 17.22  ?  450  LYS A H      1 
ATOM   6887  H HA     . LYS A 1 450 ? -26.667 -13.649 -12.746 1.00 18.94  ?  450  LYS A HA     1 
ATOM   6888  H HB2    . LYS A 1 450 ? -26.527 -12.404 -10.839 1.00 19.16  ?  450  LYS A HB2    1 
ATOM   6889  H HB3    . LYS A 1 450 ? -27.036 -11.109 -11.608 1.00 19.16  ?  450  LYS A HB3    1 
ATOM   6890  H HG2    . LYS A 1 450 ? -28.700 -12.018 -10.229 1.00 24.56  ?  450  LYS A HG2    1 
ATOM   6891  H HG3    . LYS A 1 450 ? -29.159 -11.986 -11.750 1.00 24.56  ?  450  LYS A HG3    1 
ATOM   6892  H HD2    . LYS A 1 450 ? -29.143 -14.156 -11.925 1.00 33.53  ?  450  LYS A HD2    1 
ATOM   6893  H HD3    . LYS A 1 450 ? -27.995 -14.328 -10.840 1.00 33.53  ?  450  LYS A HD3    1 
ATOM   6894  H HE2    . LYS A 1 450 ? -30.104 -15.112 -10.062 1.00 38.54  ?  450  LYS A HE2    1 
ATOM   6895  H HE3    . LYS A 1 450 ? -29.499 -13.980 -9.124  1.00 38.54  ?  450  LYS A HE3    1 
ATOM   6896  H HZ1    . LYS A 1 450 ? -31.712 -13.631 -9.607  1.00 39.41  ?  450  LYS A HZ1    1 
ATOM   6897  H HZ2    . LYS A 1 450 ? -30.909 -12.508 -10.045 1.00 39.41  ?  450  LYS A HZ2    1 
ATOM   6898  H HZ3    . LYS A 1 450 ? -31.398 -13.470 -11.012 1.00 39.41  ?  450  LYS A HZ3    1 
ATOM   6899  N N      . ARG A 1 451 ? -27.566 -11.125 -14.519 1.00 14.43  ?  451  ARG A N      1 
ATOM   6900  C CA     . ARG A 1 451 ? -28.486 -10.745 -15.588 1.00 15.29  ?  451  ARG A CA     1 
ATOM   6901  C C      . ARG A 1 451 ? -28.289 -11.631 -16.810 1.00 15.13  ?  451  ARG A C      1 
ATOM   6902  O O      . ARG A 1 451 ? -29.256 -12.025 -17.467 1.00 16.20  ?  451  ARG A O      1 
ATOM   6903  C CB     . ARG A 1 451 ? -28.355 -9.255  -15.914 1.00 17.17  ?  451  ARG A CB     1 
ATOM   6904  C CG     . ARG A 1 451 ? -28.865 -8.336  -14.795 1.00 17.16  ?  451  ARG A CG     1 
ATOM   6905  C CD     . ARG A 1 451 ? -29.137 -6.908  -15.285 1.00 19.31  ?  451  ARG A CD     1 
ATOM   6906  N NE     . ARG A 1 451 ? -27.941 -6.247  -15.799 1.00 21.42  ?  451  ARG A NE     1 
ATOM   6907  C CZ     . ARG A 1 451 ? -27.094 -5.533  -15.058 1.00 22.97  ?  451  ARG A CZ     1 
ATOM   6908  N NH1    . ARG A 1 451 ? -27.289 -5.372  -13.755 1.00 23.04  ?  451  ARG A NH1    1 
ATOM   6909  N NH2    . ARG A 1 451 ? -26.041 -4.979  -15.640 1.00 24.06  ?  451  ARG A NH2    1 
ATOM   6910  H H      . ARG A 1 451 ? -27.000 -10.518 -14.292 1.00 17.31  ?  451  ARG A H      1 
ATOM   6911  H HA     . ARG A 1 451 ? -29.399 -10.872 -15.286 1.00 18.35  ?  451  ARG A HA     1 
ATOM   6912  H HB2    . ARG A 1 451 ? -27.419 -9.049  -16.064 1.00 20.60  ?  451  ARG A HB2    1 
ATOM   6913  H HB3    . ARG A 1 451 ? -28.869 -9.063  -16.713 1.00 20.60  ?  451  ARG A HB3    1 
ATOM   6914  H HG2    . ARG A 1 451 ? -29.694 -8.696  -14.443 1.00 20.59  ?  451  ARG A HG2    1 
ATOM   6915  H HG3    . ARG A 1 451 ? -28.197 -8.291  -14.093 1.00 20.59  ?  451  ARG A HG3    1 
ATOM   6916  H HD2    . ARG A 1 451 ? -29.792 -6.939  -16.000 1.00 23.16  ?  451  ARG A HD2    1 
ATOM   6917  H HD3    . ARG A 1 451 ? -29.477 -6.380  -14.546 1.00 23.16  ?  451  ARG A HD3    1 
ATOM   6918  H HE     . ARG A 1 451 ? -27.771 -6.324  -16.638 1.00 25.70  ?  451  ARG A HE     1 
ATOM   6919  H HH11   . ARG A 1 451 ? -27.972 -5.731  -13.375 1.00 27.64  ?  451  ARG A HH11   1 
ATOM   6920  H HH12   . ARG A 1 451 ? -26.734 -4.908  -13.291 1.00 27.64  ?  451  ARG A HH12   1 
ATOM   6921  H HH21   . ARG A 1 451 ? -25.912 -5.083  -16.484 1.00 28.87  ?  451  ARG A HH21   1 
ATOM   6922  H HH22   . ARG A 1 451 ? -25.486 -4.516  -15.174 1.00 28.87  ?  451  ARG A HH22   1 
ATOM   6923  N N      . ALA A 1 452 ? -27.032 -11.963 -17.120 1.00 14.69  ?  452  ALA A N      1 
ATOM   6924  C CA     . ALA A 1 452 ? -26.731 -12.805 -18.272 1.00 16.10  ?  452  ALA A CA     1 
ATOM   6925  C C      . ALA A 1 452 ? -27.237 -14.229 -18.072 1.00 15.69  ?  452  ALA A C      1 
ATOM   6926  O O      . ALA A 1 452 ? -27.846 -14.813 -18.977 1.00 16.51  ?  452  ALA A O      1 
ATOM   6927  C CB     . ALA A 1 452 ? -25.221 -12.785 -18.495 1.00 16.00  ?  452  ALA A CB     1 
ATOM   6928  H H      . ALA A 1 452 ? -26.337 -11.714 -16.680 1.00 17.62  ?  452  ALA A H      1 
ATOM   6929  H HA     . ALA A 1 452 ? -27.175 -12.456 -19.061 1.00 19.32  ?  452  ALA A HA     1 
ATOM   6930  H HB1    . ALA A 1 452 ? -25.003 -13.377 -19.232 1.00 19.19  ?  452  ALA A HB1    1 
ATOM   6931  H HB2    . ALA A 1 452 ? -24.944 -11.880 -18.704 1.00 19.19  ?  452  ALA A HB2    1 
ATOM   6932  H HB3    . ALA A 1 452 ? -24.779 -13.088 -17.686 1.00 19.19  ?  452  ALA A HB3    1 
ATOM   6933  N N      . VAL A 1 453 ? -26.991 -14.809 -16.893 1.00 16.97  ?  453  VAL A N      1 
ATOM   6934  C CA     . VAL A 1 453 ? -27.458 -16.170 -16.621 1.00 15.84  ?  453  VAL A CA     1 
ATOM   6935  C C      . VAL A 1 453 ? -28.974 -16.224 -16.655 1.00 16.79  ?  453  VAL A C      1 
ATOM   6936  O O      . VAL A 1 453 ? -29.559 -17.145 -17.238 1.00 16.96  ?  453  VAL A O      1 
ATOM   6937  C CB     . VAL A 1 453 ? -26.899 -16.669 -15.274 1.00 16.28  ?  453  VAL A CB     1 
ATOM   6938  C CG1    . VAL A 1 453 ? -27.536 -17.994 -14.866 1.00 16.15  ?  453  VAL A CG1    1 
ATOM   6939  C CG2    . VAL A 1 453 ? -25.386 -16.821 -15.341 1.00 17.14  ?  453  VAL A CG2    1 
ATOM   6940  H H      . VAL A 1 453 ? -26.563 -14.444 -16.244 1.00 20.36  ?  453  VAL A H      1 
ATOM   6941  H HA     . VAL A 1 453 ? -27.122 -16.757 -17.316 1.00 19.00  ?  453  VAL A HA     1 
ATOM   6942  H HB     . VAL A 1 453 ? -27.116 -16.009 -14.598 1.00 19.53  ?  453  VAL A HB     1 
ATOM   6943  H HG11   . VAL A 1 453 ? -27.037 -18.370 -14.125 1.00 19.38  ?  453  VAL A HG11   1 
ATOM   6944  H HG12   . VAL A 1 453 ? -28.455 -17.834 -14.599 1.00 19.38  ?  453  VAL A HG12   1 
ATOM   6945  H HG13   . VAL A 1 453 ? -27.513 -18.602 -15.622 1.00 19.38  ?  453  VAL A HG13   1 
ATOM   6946  H HG21   . VAL A 1 453 ? -25.052 -17.050 -14.460 1.00 20.56  ?  453  VAL A HG21   1 
ATOM   6947  H HG22   . VAL A 1 453 ? -25.166 -17.525 -15.971 1.00 20.56  ?  453  VAL A HG22   1 
ATOM   6948  H HG23   . VAL A 1 453 ? -24.997 -15.982 -15.635 1.00 20.56  ?  453  VAL A HG23   1 
ATOM   6949  N N      . ASP A 1 454 ? -29.628 -15.224 -16.054 1.00 16.70  ?  454  ASP A N      1 
ATOM   6950  C CA     . ASP A 1 454 ? -31.089 -15.166 -16.052 1.00 16.48  ?  454  ASP A CA     1 
ATOM   6951  C C      . ASP A 1 454 ? -31.635 -15.061 -17.472 1.00 17.63  ?  454  ASP A C      1 
ATOM   6952  O O      . ASP A 1 454 ? -32.653 -15.682 -17.792 1.00 17.56  ?  454  ASP A O      1 
ATOM   6953  C CB     . ASP A 1 454 ? -31.553 -13.944 -15.246 1.00 17.78  ?  454  ASP A CB     1 
ATOM   6954  C CG     . ASP A 1 454 ? -31.473 -14.157 -13.744 1.00 19.84  ?  454  ASP A CG     1 
ATOM   6955  O OD1    . ASP A 1 454 ? -31.220 -15.288 -13.300 1.00 20.89  ?  454  ASP A OD1    1 
ATOM   6956  O OD2    . ASP A 1 454 ? -31.658 -13.176 -13.004 1.00 20.10  -1 454  ASP A OD2    1 
ATOM   6957  H H      . ASP A 1 454 ? -29.252 -14.569 -15.642 1.00 20.03  ?  454  ASP A H      1 
ATOM   6958  H HA     . ASP A 1 454 ? -31.432 -15.975 -15.641 1.00 19.77  ?  454  ASP A HA     1 
ATOM   6959  H HB2    . ASP A 1 454 ? -30.990 -13.186 -15.471 1.00 21.33  ?  454  ASP A HB2    1 
ATOM   6960  H HB3    . ASP A 1 454 ? -32.476 -13.750 -15.471 1.00 21.33  ?  454  ASP A HB3    1 
ATOM   6961  N N      . LYS A 1 455 ? -30.986 -14.263 -18.330 1.00 17.29  ?  455  LYS A N      1 
ATOM   6962  C CA     . LYS A 1 455 ? -31.468 -14.109 -19.696 1.00 17.13  ?  455  LYS A CA     1 
ATOM   6963  C C      . LYS A 1 455 ? -31.463 -15.445 -20.434 1.00 18.05  ?  455  LYS A C      1 
ATOM   6964  O O      . LYS A 1 455 ? -32.436 -15.792 -21.115 1.00 19.73  ?  455  LYS A O      1 
ATOM   6965  C CB     . LYS A 1 455 ? -30.621 -13.081 -20.448 1.00 18.66  ?  455  LYS A CB     1 
ATOM   6966  C CG     . LYS A 1 455 ? -31.043 -12.920 -21.886 1.00 24.34  ?  455  LYS A CG     1 
ATOM   6967  C CD     . LYS A 1 455 ? -30.043 -12.104 -22.676 1.00 30.49  ?  455  LYS A CD     1 
ATOM   6968  C CE     . LYS A 1 455 ? -30.264 -10.613 -22.517 1.00 35.58  ?  455  LYS A CE     1 
ATOM   6969  N NZ     . LYS A 1 455 ? -29.287 -9.828  -23.336 1.00 36.93  ?  455  LYS A NZ     1 
ATOM   6970  H H      . LYS A 1 455 ? -30.279 -13.809 -18.146 1.00 20.75  ?  455  LYS A H      1 
ATOM   6971  H HA     . LYS A 1 455 ? -32.381 -13.781 -19.665 1.00 20.55  ?  455  LYS A HA     1 
ATOM   6972  H HB2    . LYS A 1 455 ? -30.708 -12.219 -20.011 1.00 22.39  ?  455  LYS A HB2    1 
ATOM   6973  H HB3    . LYS A 1 455 ? -29.694 -13.366 -20.437 1.00 22.39  ?  455  LYS A HB3    1 
ATOM   6974  H HG2    . LYS A 1 455 ? -31.115 -13.795 -22.298 1.00 29.20  ?  455  LYS A HG2    1 
ATOM   6975  H HG3    . LYS A 1 455 ? -31.900 -12.466 -21.919 1.00 29.20  ?  455  LYS A HG3    1 
ATOM   6976  H HD2    . LYS A 1 455 ? -29.147 -12.311 -22.366 1.00 36.58  ?  455  LYS A HD2    1 
ATOM   6977  H HD3    . LYS A 1 455 ? -30.126 -12.322 -23.617 1.00 36.58  ?  455  LYS A HD3    1 
ATOM   6978  H HE2    . LYS A 1 455 ? -31.161 -10.387 -22.811 1.00 42.70  ?  455  LYS A HE2    1 
ATOM   6979  H HE3    . LYS A 1 455 ? -30.149 -10.368 -21.585 1.00 42.70  ?  455  LYS A HE3    1 
ATOM   6980  H HZ1    . LYS A 1 455 ? -29.472 -8.960  -23.282 1.00 44.31  ?  455  LYS A HZ1    1 
ATOM   6981  H HZ2    . LYS A 1 455 ? -28.460 -9.966  -23.037 1.00 44.31  ?  455  LYS A HZ2    1 
ATOM   6982  H HZ3    . LYS A 1 455 ? -29.332 -10.081 -24.188 1.00 44.31  ?  455  LYS A HZ3    1 
ATOM   6983  N N      . VAL A 1 456 ? -30.361 -16.196 -20.339 1.00 16.15  ?  456  VAL A N      1 
ATOM   6984  C CA     . VAL A 1 456 ? -30.288 -17.471 -21.041 1.00 17.02  ?  456  VAL A CA     1 
ATOM   6985  C C      . VAL A 1 456 ? -31.217 -18.491 -20.395 1.00 17.76  ?  456  VAL A C      1 
ATOM   6986  O O      . VAL A 1 456 ? -31.829 -19.326 -21.082 1.00 18.01  ?  456  VAL A O      1 
ATOM   6987  C CB     . VAL A 1 456 ? -28.834 -17.968 -21.120 1.00 16.04  ?  456  VAL A CB     1 
ATOM   6988  C CG1    . VAL A 1 456 ? -28.793 -19.337 -21.763 1.00 17.77  ?  456  VAL A CG1    1 
ATOM   6989  C CG2    . VAL A 1 456 ? -27.980 -16.989 -21.924 1.00 18.13  ?  456  VAL A CG2    1 
ATOM   6990  H H      . VAL A 1 456 ? -29.659 -15.994 -19.884 1.00 19.37  ?  456  VAL A H      1 
ATOM   6991  H HA     . VAL A 1 456 ? -30.592 -17.337 -21.952 1.00 20.42  ?  456  VAL A HA     1 
ATOM   6992  H HB     . VAL A 1 456 ? -28.470 -18.030 -20.224 1.00 19.24  ?  456  VAL A HB     1 
ATOM   6993  H HG11   . VAL A 1 456 ? -27.870 -19.569 -21.952 1.00 21.32  ?  456  VAL A HG11   1 
ATOM   6994  H HG12   . VAL A 1 456 ? -29.179 -19.984 -21.153 1.00 21.32  ?  456  VAL A HG12   1 
ATOM   6995  H HG13   . VAL A 1 456 ? -29.304 -19.314 -22.588 1.00 21.32  ?  456  VAL A HG13   1 
ATOM   6996  H HG21   . VAL A 1 456 ? -27.057 -17.287 -21.907 1.00 21.75  ?  456  VAL A HG21   1 
ATOM   6997  H HG22   . VAL A 1 456 ? -28.303 -16.964 -22.838 1.00 21.75  ?  456  VAL A HG22   1 
ATOM   6998  H HG23   . VAL A 1 456 ? -28.050 -16.108 -21.524 1.00 21.75  ?  456  VAL A HG23   1 
ATOM   6999  N N      . THR A 1 457 ? -31.357 -18.432 -19.071 1.00 17.91  ?  457  THR A N      1 
ATOM   7000  C CA     . THR A 1 457 ? -32.343 -19.281 -18.398 1.00 17.76  ?  457  THR A CA     1 
ATOM   7001  C C      . THR A 1 457 ? -33.731 -19.076 -18.991 1.00 18.12  ?  457  THR A C      1 
ATOM   7002  O O      . THR A 1 457 ? -34.435 -20.044 -19.300 1.00 18.86  ?  457  THR A O      1 
ATOM   7003  C CB     . THR A 1 457 ? -32.343 -18.972 -16.901 1.00 18.14  ?  457  THR A CB     1 
ATOM   7004  O OG1    . THR A 1 457 ? -31.058 -19.274 -16.340 1.00 18.20  ?  457  THR A OG1    1 
ATOM   7005  C CG2    . THR A 1 457 ? -33.399 -19.788 -16.163 1.00 18.54  ?  457  THR A CG2    1 
ATOM   7006  H H      . THR A 1 457 ? -30.905 -17.922 -18.547 1.00 21.49  ?  457  THR A H      1 
ATOM   7007  H HA     . THR A 1 457 ? -32.101 -20.212 -18.519 1.00 21.31  ?  457  THR A HA     1 
ATOM   7008  H HB     . THR A 1 457 ? -32.545 -18.031 -16.783 1.00 21.77  ?  457  THR A HB     1 
ATOM   7009  H HG1    . THR A 1 457 ? -30.480 -18.746 -16.645 1.00 21.84  ?  457  THR A HG1    1 
ATOM   7010  H HG21   . THR A 1 457 ? -33.286 -19.688 -15.205 1.00 22.25  ?  457  THR A HG21   1 
ATOM   7011  H HG22   . THR A 1 457 ? -34.286 -19.483 -16.409 1.00 22.25  ?  457  THR A HG22   1 
ATOM   7012  H HG23   . THR A 1 457 ? -33.314 -20.726 -16.393 1.00 22.25  ?  457  THR A HG23   1 
ATOM   7013  N N      . ASP A 1 458 ? -34.133 -17.822 -19.174 1.00 18.62  ?  458  ASP A N      1 
ATOM   7014  C CA     . ASP A 1 458 ? -35.449 -17.541 -19.736 1.00 21.57  ?  458  ASP A CA     1 
ATOM   7015  C C      . ASP A 1 458 ? -35.570 -18.051 -21.169 1.00 19.91  ?  458  ASP A C      1 
ATOM   7016  O O      . ASP A 1 458 ? -36.609 -18.602 -21.556 1.00 19.17  ?  458  ASP A O      1 
ATOM   7017  C CB     . ASP A 1 458 ? -35.727 -16.039 -19.670 1.00 26.71  ?  458  ASP A CB     1 
ATOM   7018  C CG     . ASP A 1 458 ? -35.975 -15.551 -18.257 1.00 32.18  ?  458  ASP A CG     1 
ATOM   7019  O OD1    . ASP A 1 458 ? -36.243 -16.384 -17.357 1.00 35.80  ?  458  ASP A OD1    1 
ATOM   7020  O OD2    . ASP A 1 458 ? -35.918 -14.321 -18.038 1.00 33.79  -1 458  ASP A OD2    1 
ATOM   7021  H H      . ASP A 1 458 ? -33.670 -17.122 -18.985 1.00 22.34  ?  458  ASP A H      1 
ATOM   7022  H HA     . ASP A 1 458 ? -36.120 -17.998 -19.207 1.00 25.88  ?  458  ASP A HA     1 
ATOM   7023  H HB2    . ASP A 1 458 ? -34.960 -15.560 -20.022 1.00 32.05  ?  458  ASP A HB2    1 
ATOM   7024  H HB3    . ASP A 1 458 ? -36.514 -15.839 -20.200 1.00 32.05  ?  458  ASP A HB3    1 
ATOM   7025  N N      . GLU A 1 459 ? -34.526 -17.871 -21.975 1.00 18.73  ?  459  GLU A N      1 
ATOM   7026  C CA     . GLU A 1 459 ? -34.559 -18.366 -23.344 1.00 19.00  ?  459  GLU A CA     1 
ATOM   7027  C C      . GLU A 1 459 ? -34.757 -19.876 -23.364 1.00 18.98  ?  459  GLU A C      1 
ATOM   7028  O O      . GLU A 1 459 ? -35.594 -20.402 -24.113 1.00 20.52  ?  459  GLU A O      1 
ATOM   7029  C CB     . GLU A 1 459 ? -33.254 -18.017 -24.063 1.00 19.07  ?  459  GLU A CB     1 
ATOM   7030  C CG     . GLU A 1 459 ? -33.042 -16.559 -24.332 1.00 21.37  ?  459  GLU A CG     1 
ATOM   7031  C CD     . GLU A 1 459 ? -31.674 -16.275 -24.943 1.00 24.63  ?  459  GLU A CD     1 
ATOM   7032  O OE1    . GLU A 1 459 ? -30.872 -17.222 -25.138 1.00 27.15  ?  459  GLU A OE1    1 
ATOM   7033  O OE2    . GLU A 1 459 ? -31.403 -15.101 -25.222 1.00 24.84  -1 459  GLU A OE2    1 
ATOM   7034  H H      . GLU A 1 459 ? -33.797 -17.471 -21.757 1.00 22.47  ?  459  GLU A H      1 
ATOM   7035  H HA     . GLU A 1 459 ? -35.296 -17.939 -23.809 1.00 22.80  ?  459  GLU A HA     1 
ATOM   7036  H HB2    . GLU A 1 459 ? -32.513 -18.320 -23.515 1.00 22.87  ?  459  GLU A HB2    1 
ATOM   7037  H HB3    . GLU A 1 459 ? -33.244 -18.474 -24.918 1.00 22.87  ?  459  GLU A HB3    1 
ATOM   7038  H HG2    . GLU A 1 459 ? -33.719 -16.249 -24.953 1.00 25.64  ?  459  GLU A HG2    1 
ATOM   7039  H HG3    . GLU A 1 459 ? -33.107 -16.068 -23.498 1.00 25.64  ?  459  GLU A HG3    1 
ATOM   7040  N N      . LEU A 1 460 ? -33.983 -20.593 -22.545 1.00 18.99  ?  460  LEU A N      1 
ATOM   7041  C CA     . LEU A 1 460 ? -34.084 -22.050 -22.513 1.00 19.27  ?  460  LEU A CA     1 
ATOM   7042  C C      . LEU A 1 460 ? -35.428 -22.514 -21.968 1.00 20.95  ?  460  LEU A C      1 
ATOM   7043  O O      . LEU A 1 460 ? -35.943 -23.559 -22.387 1.00 22.72  ?  460  LEU A O      1 
ATOM   7044  C CB     . LEU A 1 460 ? -32.946 -22.601 -21.661 1.00 18.81  ?  460  LEU A CB     1 
ATOM   7045  C CG     . LEU A 1 460 ? -31.540 -22.401 -22.201 1.00 19.07  ?  460  LEU A CG     1 
ATOM   7046  C CD1    . LEU A 1 460 ? -30.503 -22.747 -21.129 1.00 19.70  ?  460  LEU A CD1    1 
ATOM   7047  C CD2    . LEU A 1 460 ? -31.318 -23.262 -23.433 1.00 20.77  ?  460  LEU A CD2    1 
ATOM   7048  H H      . LEU A 1 460 ? -33.399 -20.265 -22.006 1.00 22.79  ?  460  LEU A H      1 
ATOM   7049  H HA     . LEU A 1 460 ? -34.003 -22.400 -23.414 1.00 23.12  ?  460  LEU A HA     1 
ATOM   7050  H HB2    . LEU A 1 460 ? -32.983 -22.169 -20.794 1.00 22.57  ?  460  LEU A HB2    1 
ATOM   7051  H HB3    . LEU A 1 460 ? -33.080 -23.556 -21.562 1.00 22.57  ?  460  LEU A HB3    1 
ATOM   7052  H HG     . LEU A 1 460 ? -31.427 -21.470 -22.450 1.00 22.88  ?  460  LEU A HG     1 
ATOM   7053  H HD11   . LEU A 1 460 ? -29.615 -22.649 -21.506 1.00 23.63  ?  460  LEU A HD11   1 
ATOM   7054  H HD12   . LEU A 1 460 ? -30.612 -22.143 -20.378 1.00 23.63  ?  460  LEU A HD12   1 
ATOM   7055  H HD13   . LEU A 1 460 ? -30.641 -23.663 -20.840 1.00 23.63  ?  460  LEU A HD13   1 
ATOM   7056  H HD21   . LEU A 1 460 ? -30.390 -23.192 -23.704 1.00 24.92  ?  460  LEU A HD21   1 
ATOM   7057  H HD22   . LEU A 1 460 ? -31.531 -24.184 -23.216 1.00 24.92  ?  460  LEU A HD22   1 
ATOM   7058  H HD23   . LEU A 1 460 ? -31.896 -22.948 -24.146 1.00 24.92  ?  460  LEU A HD23   1 
ATOM   7059  N N      . THR A 1 461 ? -36.017 -21.763 -21.044 1.00 21.12  ?  461  THR A N      1 
ATOM   7060  C CA     . THR A 1 461 ? -37.362 -22.096 -20.592 1.00 22.42  ?  461  THR A CA     1 
ATOM   7061  C C      . THR A 1 461 ? -38.359 -21.977 -21.745 1.00 23.66  ?  461  THR A C      1 
ATOM   7062  O O      . THR A 1 461 ? -39.146 -22.899 -22.016 1.00 24.85  ?  461  THR A O      1 
ATOM   7063  C CB     . THR A 1 461 ? -37.739 -21.180 -19.428 1.00 24.32  ?  461  THR A CB     1 
ATOM   7064  O OG1    . THR A 1 461 ? -36.800 -21.357 -18.352 1.00 24.84  ?  461  THR A OG1    1 
ATOM   7065  C CG2    . THR A 1 461 ? -39.143 -21.494 -18.935 1.00 27.27  ?  461  THR A CG2    1 
ATOM   7066  H H      . THR A 1 461 ? -35.670 -21.070 -20.670 1.00 25.34  ?  461  THR A H      1 
ATOM   7067  H HA     . THR A 1 461 ? -37.390 -23.012 -20.274 1.00 26.90  ?  461  THR A HA     1 
ATOM   7068  H HB     . THR A 1 461 ? -37.720 -20.256 -19.722 1.00 29.19  ?  461  THR A HB     1 
ATOM   7069  H HG1    . THR A 1 461 ? -36.026 -21.162 -18.611 1.00 29.81  ?  461  THR A HG1    1 
ATOM   7070  H HG21   . THR A 1 461 ? -39.314 -21.030 -18.101 1.00 32.72  ?  461  THR A HG21   1 
ATOM   7071  H HG22   . THR A 1 461 ? -39.797 -21.209 -19.593 1.00 32.72  ?  461  THR A HG22   1 
ATOM   7072  H HG23   . THR A 1 461 ? -39.239 -22.448 -18.790 1.00 32.72  ?  461  THR A HG23   1 
ATOM   7073  N N      . ARG A 1 462 ? -38.310 -20.858 -22.466 1.00 24.98  ?  462  ARG A N      1 
ATOM   7074  C CA     . ARG A 1 462 ? -39.268 -20.614 -23.530 1.00 25.78  ?  462  ARG A CA     1 
ATOM   7075  C C      . ARG A 1 462 ? -39.114 -21.585 -24.687 1.00 26.13  ?  462  ARG A C      1 
ATOM   7076  O O      . ARG A 1 462 ? -40.101 -21.895 -25.364 1.00 28.11  ?  462  ARG A O      1 
ATOM   7077  C CB     . ARG A 1 462 ? -39.120 -19.184 -24.033 1.00 29.13  ?  462  ARG A CB     1 
ATOM   7078  C CG     . ARG A 1 462 ? -39.529 -18.152 -23.019 1.00 36.18  ?  462  ARG A CG     1 
ATOM   7079  C CD     . ARG A 1 462 ? -39.660 -16.787 -23.654 1.00 44.65  ?  462  ARG A CD     1 
ATOM   7080  N NE     . ARG A 1 462 ? -38.371 -16.240 -24.045 1.00 52.93  ?  462  ARG A NE     1 
ATOM   7081  C CZ     . ARG A 1 462 ? -37.636 -15.428 -23.285 1.00 58.44  ?  462  ARG A CZ     1 
ATOM   7082  N NH1    . ARG A 1 462 ? -38.067 -15.062 -22.080 1.00 60.92  ?  462  ARG A NH1    1 
ATOM   7083  N NH2    . ARG A 1 462 ? -36.470 -14.980 -23.732 1.00 59.12  ?  462  ARG A NH2    1 
ATOM   7084  H H      . ARG A 1 462 ? -37.735 -20.228 -22.358 1.00 29.98  ?  462  ARG A H      1 
ATOM   7085  H HA     . ARG A 1 462 ? -40.160 -20.731 -23.167 1.00 30.93  ?  462  ARG A HA     1 
ATOM   7086  H HB2    . ARG A 1 462 ? -38.190 -19.027 -24.260 1.00 34.95  ?  462  ARG A HB2    1 
ATOM   7087  H HB3    . ARG A 1 462 ? -39.677 -19.069 -24.818 1.00 34.95  ?  462  ARG A HB3    1 
ATOM   7088  H HG2    . ARG A 1 462 ? -40.386 -18.397 -22.637 1.00 43.42  ?  462  ARG A HG2    1 
ATOM   7089  H HG3    . ARG A 1 462 ? -38.857 -18.102 -22.321 1.00 43.42  ?  462  ARG A HG3    1 
ATOM   7090  H HD2    . ARG A 1 462 ? -40.213 -16.857 -24.448 1.00 53.58  ?  462  ARG A HD2    1 
ATOM   7091  H HD3    . ARG A 1 462 ? -40.068 -16.178 -23.019 1.00 53.58  ?  462  ARG A HD3    1 
ATOM   7092  H HE     . ARG A 1 462 ? -38.062 -16.454 -24.819 1.00 63.52  ?  462  ARG A HE     1 
ATOM   7093  H HH11   . ARG A 1 462 ? -38.823 -15.350 -21.787 1.00 73.10  ?  462  ARG A HH11   1 
ATOM   7094  H HH12   . ARG A 1 462 ? -37.588 -14.539 -21.593 1.00 73.10  ?  462  ARG A HH12   1 
ATOM   7095  H HH21   . ARG A 1 462 ? -36.190 -15.213 -24.511 1.00 70.94  ?  462  ARG A HH21   1 
ATOM   7096  H HH22   . ARG A 1 462 ? -35.995 -14.456 -23.242 1.00 70.94  ?  462  ARG A HH22   1 
ATOM   7097  N N      . SER A 1 463 ? -37.906 -22.050 -24.958 1.00 24.35  ?  463  SER A N      1 
ATOM   7098  C CA     . SER A 1 463 ? -37.702 -22.977 -26.058 1.00 25.92  ?  463  SER A CA     1 
ATOM   7099  C C      . SER A 1 463 ? -37.944 -24.436 -25.669 1.00 27.61  ?  463  SER A C      1 
ATOM   7100  O O      . SER A 1 463 ? -37.873 -25.315 -26.537 1.00 28.49  ?  463  SER A O      1 
ATOM   7101  C CB     . SER A 1 463 ? -36.293 -22.810 -26.639 1.00 24.98  ?  463  SER A CB     1 
ATOM   7102  O OG     . SER A 1 463 ? -35.287 -23.152 -25.697 1.00 26.21  ?  463  SER A OG     1 
ATOM   7103  H H      . SER A 1 463 ? -37.194 -21.845 -24.522 1.00 29.22  ?  463  SER A H      1 
ATOM   7104  H HA     . SER A 1 463 ? -38.333 -22.761 -26.762 1.00 31.10  ?  463  SER A HA     1 
ATOM   7105  H HB2    . SER A 1 463 ? -36.205 -23.388 -27.413 1.00 29.98  ?  463  SER A HB2    1 
ATOM   7106  H HB3    . SER A 1 463 ? -36.172 -21.884 -26.901 1.00 29.98  ?  463  SER A HB3    1 
ATOM   7107  H HG     . SER A 1 463 ? -35.348 -23.965 -25.495 1.00 31.45  ?  463  SER A HG     1 
ATOM   7108  N N      . GLY A 1 464 ? -38.226 -24.716 -24.400 1.00 26.47  ?  464  GLY A N      1 
ATOM   7109  C CA     . GLY A 1 464 ? -38.494 -26.067 -23.950 1.00 27.64  ?  464  GLY A CA     1 
ATOM   7110  C C      . GLY A 1 464 ? -37.270 -26.883 -23.589 1.00 28.73  ?  464  GLY A C      1 
ATOM   7111  O O      . GLY A 1 464 ? -37.382 -28.105 -23.435 1.00 29.80  ?  464  GLY A O      1 
ATOM   7112  H H      . GLY A 1 464 ? -38.268 -24.128 -23.774 1.00 31.76  ?  464  GLY A H      1 
ATOM   7113  H HA2    . GLY A 1 464 ? -39.061 -26.024 -23.165 1.00 33.16  ?  464  GLY A HA2    1 
ATOM   7114  H HA3    . GLY A 1 464 ? -38.965 -26.540 -24.655 1.00 33.16  ?  464  GLY A HA3    1 
ATOM   7115  N N      . ASP A 1 465 ? -36.106 -26.253 -23.460 1.00 29.53  ?  465  ASP A N      1 
ATOM   7116  C CA     . ASP A 1 465 ? -34.857 -26.937 -23.144 1.00 29.05  ?  465  ASP A CA     1 
ATOM   7117  C C      . ASP A 1 465 ? -34.528 -26.926 -21.658 1.00 31.77  ?  465  ASP A C      1 
ATOM   7118  O O      . ASP A 1 465 ? -33.452 -27.401 -21.270 1.00 33.45  ?  465  ASP A O      1 
ATOM   7119  C CB     . ASP A 1 465 ? -33.718 -26.291 -23.940 1.00 29.78  ?  465  ASP A CB     1 
ATOM   7120  C CG     . ASP A 1 465 ? -33.886 -26.464 -25.440 1.00 30.57  ?  465  ASP A CG     1 
ATOM   7121  O OD1    . ASP A 1 465 ? -34.047 -27.615 -25.891 1.00 32.20  ?  465  ASP A OD1    1 
ATOM   7122  O OD2    . ASP A 1 465 ? -33.872 -25.451 -26.164 1.00 30.97  -1 465  ASP A OD2    1 
ATOM   7123  H H      . ASP A 1 465 ? -36.014 -25.404 -23.553 1.00 35.43  ?  465  ASP A H      1 
ATOM   7124  H HA     . ASP A 1 465 ? -34.926 -27.867 -23.411 1.00 34.86  ?  465  ASP A HA     1 
ATOM   7125  H HB2    . ASP A 1 465 ? -33.695 -25.341 -23.747 1.00 35.73  ?  465  ASP A HB2    1 
ATOM   7126  H HB3    . ASP A 1 465 ? -32.878 -26.702 -23.682 1.00 35.73  ?  465  ASP A HB3    1 
ATOM   7127  N N      . LEU A 1 466 ? -35.415 -26.409 -20.819 1.00 32.77  ?  466  LEU A N      1 
ATOM   7128  C CA     . LEU A 1 466 ? -35.175 -26.406 -19.380 1.00 36.30  ?  466  LEU A CA     1 
ATOM   7129  C C      . LEU A 1 466 ? -36.478 -26.594 -18.619 1.00 39.66  ?  466  LEU A C      1 
ATOM   7130  O O      . LEU A 1 466 ? -37.472 -25.914 -18.907 1.00 43.55  ?  466  LEU A O      1 
ATOM   7131  C CB     . LEU A 1 466 ? -34.515 -25.098 -18.954 1.00 37.17  ?  466  LEU A CB     1 
ATOM   7132  C CG     . LEU A 1 466 ? -34.234 -24.953 -17.466 1.00 38.64  ?  466  LEU A CG     1 
ATOM   7133  C CD1    . LEU A 1 466 ? -33.022 -25.768 -17.078 1.00 38.63  ?  466  LEU A CD1    1 
ATOM   7134  C CD2    . LEU A 1 466 ? -34.046 -23.492 -17.093 1.00 39.62  ?  466  LEU A CD2    1 
ATOM   7135  H H      . LEU A 1 466 ? -36.162 -26.055 -21.056 1.00 39.31  ?  466  LEU A H      1 
ATOM   7136  H HA     . LEU A 1 466 ? -34.578 -27.136 -19.155 1.00 43.55  ?  466  LEU A HA     1 
ATOM   7137  H HB2    . LEU A 1 466 ? -33.665 -25.022 -19.416 1.00 44.60  ?  466  LEU A HB2    1 
ATOM   7138  H HB3    . LEU A 1 466 ? -35.098 -24.366 -19.209 1.00 44.60  ?  466  LEU A HB3    1 
ATOM   7139  H HG     . LEU A 1 466 ? -34.994 -25.289 -16.966 1.00 46.36  ?  466  LEU A HG     1 
ATOM   7140  H HD11   . LEU A 1 466 ? -32.830 -25.621 -16.138 1.00 46.36  ?  466  LEU A HD11   1 
ATOM   7141  H HD12   . LEU A 1 466 ? -33.209 -26.707 -17.234 1.00 46.36  ?  466  LEU A HD12   1 
ATOM   7142  H HD13   . LEU A 1 466 ? -32.266 -25.488 -17.618 1.00 46.36  ?  466  LEU A HD13   1 
ATOM   7143  H HD21   . LEU A 1 466 ? -33.983 -23.418 -16.127 1.00 47.54  ?  466  LEU A HD21   1 
ATOM   7144  H HD22   . LEU A 1 466 ? -33.232 -23.163 -17.504 1.00 47.54  ?  466  LEU A HD22   1 
ATOM   7145  H HD23   . LEU A 1 466 ? -34.807 -22.984 -17.414 1.00 47.54  ?  466  LEU A HD23   1 
ATOM   7146  N N      . SER B 2 2   ? 35.526  -7.163  -9.268  1.00 21.55  ?  2    SER B N      1 
ATOM   7147  C CA     . SER B 2 2   ? 34.813  -6.016  -9.797  1.00 18.16  ?  2    SER B CA     1 
ATOM   7148  C C      . SER B 2 2   ? 33.301  -6.144  -9.609  1.00 16.39  ?  2    SER B C      1 
ATOM   7149  O O      . SER B 2 2   ? 32.792  -7.231  -9.328  1.00 17.75  ?  2    SER B O      1 
ATOM   7150  C CB     . SER B 2 2   ? 35.088  -5.875  -11.296 1.00 22.33  ?  2    SER B CB     1 
ATOM   7151  O OG     . SER B 2 2   ? 34.526  -6.986  -11.988 1.00 17.95  ?  2    SER B OG     1 
ATOM   7152  H HA     . SER B 2 2   ? 35.121  -5.228  -9.322  1.00 21.79  ?  2    SER B HA     1 
ATOM   7153  H HB2    . SER B 2 2   ? 34.684  -5.056  -11.622 1.00 26.79  ?  2    SER B HB2    1 
ATOM   7154  H HB3    . SER B 2 2   ? 36.046  -5.855  -11.446 1.00 26.79  ?  2    SER B HB3    1 
ATOM   7155  H HG     . SER B 2 2   ? 34.773  -7.703  -11.627 1.00 21.53  ?  2    SER B HG     1 
ATOM   7156  N N      . GLN B 2 3   ? 32.592  -5.024  -9.791  1.00 16.15  ?  3    GLN B N      1 
ATOM   7157  C CA     . GLN B 2 3   ? 31.137  -5.059  -9.765  1.00 17.00  ?  3    GLN B CA     1 
ATOM   7158  C C      . GLN B 2 3   ? 30.602  -6.038  -10.798 1.00 17.10  ?  3    GLN B C      1 
ATOM   7159  O O      . GLN B 2 3   ? 29.634  -6.766  -10.537 1.00 16.34  ?  3    GLN B O      1 
ATOM   7160  C CB     . GLN B 2 3   ? 30.608  -3.654  -10.018 1.00 19.41  ?  3    GLN B CB     1 
ATOM   7161  C CG     . GLN B 2 3   ? 30.998  -2.663  -8.933  1.00 25.63  ?  3    GLN B CG     1 
ATOM   7162  C CD     . GLN B 2 3   ? 30.558  -1.237  -9.250  1.00 30.06  ?  3    GLN B CD     1 
ATOM   7163  O OE1    . GLN B 2 3   ? 29.998  -0.965  -10.314 1.00 31.41  ?  3    GLN B OE1    1 
ATOM   7164  N NE2    . GLN B 2 3   ? 30.818  -0.321  -8.326  1.00 33.90  ?  3    GLN B NE2    1 
ATOM   7165  H H      . GLN B 2 3   ? 32.926  -4.244  -9.928  1.00 19.38  ?  3    GLN B H      1 
ATOM   7166  H HA     . GLN B 2 3   ? 30.826  -5.352  -8.895  1.00 20.39  ?  3    GLN B HA     1 
ATOM   7167  H HB2    . GLN B 2 3   ? 30.965  -3.330  -10.860 1.00 23.29  ?  3    GLN B HB2    1 
ATOM   7168  H HB3    . GLN B 2 3   ? 29.639  -3.686  -10.059 1.00 23.29  ?  3    GLN B HB3    1 
ATOM   7169  H HG2    . GLN B 2 3   ? 30.580  -2.927  -8.099  1.00 30.75  ?  3    GLN B HG2    1 
ATOM   7170  H HG3    . GLN B 2 3   ? 31.963  -2.665  -8.836  1.00 30.75  ?  3    GLN B HG3    1 
ATOM   7171  H HE21   . GLN B 2 3   ? 31.214  -0.547  -7.597  1.00 40.67  ?  3    GLN B HE21   1 
ATOM   7172  H HE22   . GLN B 2 3   ? 30.591  0.498   -8.456  1.00 40.67  ?  3    GLN B HE22   1 
ATOM   7173  N N      . HIS B 2 4   ? 31.233  -6.076  -11.973 1.00 18.19  ?  4    HIS B N      1 
ATOM   7174  C CA     . HIS B 2 4   ? 30.839  -6.999  -13.033 1.00 16.06  ?  4    HIS B CA     1 
ATOM   7175  C C      . HIS B 2 4   ? 30.934  -8.449  -12.572 1.00 14.38  ?  4    HIS B C      1 
ATOM   7176  O O      . HIS B 2 4   ? 29.990  -9.233  -12.747 1.00 16.22  ?  4    HIS B O      1 
ATOM   7177  C CB     . HIS B 2 4   ? 31.748  -6.741  -14.236 1.00 16.38  ?  4    HIS B CB     1 
ATOM   7178  C CG     . HIS B 2 4   ? 31.341  -7.445  -15.490 1.00 17.56  ?  4    HIS B CG     1 
ATOM   7179  N ND1    . HIS B 2 4   ? 32.052  -7.325  -16.666 1.00 19.04  ?  4    HIS B ND1    1 
ATOM   7180  C CD2    . HIS B 2 4   ? 30.291  -8.248  -15.766 1.00 16.99  ?  4    HIS B CD2    1 
ATOM   7181  C CE1    . HIS B 2 4   ? 31.463  -8.040  -17.611 1.00 19.03  ?  4    HIS B CE1    1 
ATOM   7182  N NE2    . HIS B 2 4   ? 30.384  -8.600  -17.094 1.00 17.25  ?  4    HIS B NE2    1 
ATOM   7183  H H      . HIS B 2 4   ? 31.897  -5.573  -12.185 1.00 21.82  ?  4    HIS B H      1 
ATOM   7184  H HA     . HIS B 2 4   ? 29.915  -6.847  -13.287 1.00 19.27  ?  4    HIS B HA     1 
ATOM   7185  H HB2    . HIS B 2 4   ? 31.750  -5.790  -14.422 1.00 19.65  ?  4    HIS B HB2    1 
ATOM   7186  H HB3    . HIS B 2 4   ? 32.645  -7.037  -14.013 1.00 19.65  ?  4    HIS B HB3    1 
ATOM   7187  H HD1    . HIS B 2 4   ? 32.767  -6.858  -16.770 1.00 22.84  ?  4    HIS B HD1    1 
ATOM   7188  H HD2    . HIS B 2 4   ? 29.628  -8.514  -15.170 1.00 20.38  ?  4    HIS B HD2    1 
ATOM   7189  H HE1    . HIS B 2 4   ? 31.759  -8.133  -18.488 1.00 22.83  ?  4    HIS B HE1    1 
ATOM   7190  N N      . GLN B 2 5   ? 32.076  -8.839  -12.007 1.00 14.70  ?  5    GLN B N      1 
ATOM   7191  C CA     . GLN B 2 5   ? 32.194  -10.224 -11.562 1.00 16.85  ?  5    GLN B CA     1 
ATOM   7192  C C      . GLN B 2 5   ? 31.261  -10.510 -10.393 1.00 15.27  ?  5    GLN B C      1 
ATOM   7193  O O      . GLN B 2 5   ? 30.753  -11.624 -10.273 1.00 15.98  ?  5    GLN B O      1 
ATOM   7194  C CB     . GLN B 2 5   ? 33.643  -10.556 -11.232 1.00 18.35  ?  5    GLN B CB     1 
ATOM   7195  C CG     . GLN B 2 5   ? 34.571  -10.453 -12.412 1.00 19.34  ?  5    GLN B CG     1 
ATOM   7196  C CD     . GLN B 2 5   ? 34.118  -11.262 -13.614 1.00 21.84  ?  5    GLN B CD     1 
ATOM   7197  O OE1    . GLN B 2 5   ? 33.712  -12.428 -13.497 1.00 21.84  ?  5    GLN B OE1    1 
ATOM   7198  N NE2    . GLN B 2 5   ? 34.158  -10.631 -14.789 1.00 23.85  ?  5    GLN B NE2    1 
ATOM   7199  H H      . GLN B 2 5   ? 32.767  -8.345  -11.874 1.00 17.64  ?  5    GLN B H      1 
ATOM   7200  H HA     . GLN B 2 5   ? 31.936  -10.816 -12.285 1.00 20.22  ?  5    GLN B HA     1 
ATOM   7201  H HB2    . GLN B 2 5   ? 33.957  -9.938  -10.553 1.00 22.01  ?  5    GLN B HB2    1 
ATOM   7202  H HB3    . GLN B 2 5   ? 33.686  -11.466 -10.899 1.00 22.01  ?  5    GLN B HB3    1 
ATOM   7203  H HG2    . GLN B 2 5   ? 34.629  -9.524  -12.685 1.00 23.20  ?  5    GLN B HG2    1 
ATOM   7204  H HG3    . GLN B 2 5   ? 35.447  -10.777 -12.150 1.00 23.20  ?  5    GLN B HG3    1 
ATOM   7205  H HE21   . GLN B 2 5   ? 34.428  -9.816  -14.831 1.00 28.62  ?  5    GLN B HE21   1 
ATOM   7206  H HE22   . GLN B 2 5   ? 33.912  -11.040 -15.505 1.00 28.62  ?  5    GLN B HE22   1 
ATOM   7207  N N      . ASN B 2 6   ? 31.012  -9.528  -9.520  1.00 15.98  ?  6    ASN B N      1 
ATOM   7208  C CA     . ASN B 2 6   ? 30.053  -9.749  -8.438  1.00 16.69  ?  6    ASN B CA     1 
ATOM   7209  C C      . ASN B 2 6   ? 28.652  -10.009 -8.992  1.00 14.85  ?  6    ASN B C      1 
ATOM   7210  O O      . ASN B 2 6   ? 27.897  -10.821 -8.443  1.00 14.57  ?  6    ASN B O      1 
ATOM   7211  C CB     . ASN B 2 6   ? 30.031  -8.553  -7.491  1.00 16.31  ?  6    ASN B CB     1 
ATOM   7212  C CG     . ASN B 2 6   ? 31.338  -8.339  -6.763  1.00 17.03  ?  6    ASN B CG     1 
ATOM   7213  O OD1    . ASN B 2 6   ? 32.209  -9.211  -6.719  1.00 18.21  ?  6    ASN B OD1    1 
ATOM   7214  N ND2    . ASN B 2 6   ? 31.479  -7.160  -6.155  1.00 21.06  ?  6    ASN B ND2    1 
ATOM   7215  H H      . ASN B 2 6   ? 31.373  -8.748  -9.532  1.00 19.18  ?  6    ASN B H      1 
ATOM   7216  H HA     . ASN B 2 6   ? 30.335  -10.527 -7.931  1.00 20.02  ?  6    ASN B HA     1 
ATOM   7217  H HB2    . ASN B 2 6   ? 29.841  -7.751  -8.003  1.00 19.57  ?  6    ASN B HB2    1 
ATOM   7218  H HB3    . ASN B 2 6   ? 29.339  -8.693  -6.825  1.00 19.57  ?  6    ASN B HB3    1 
ATOM   7219  H HD21   . ASN B 2 6   ? 32.202  -6.983  -5.725  1.00 25.27  ?  6    ASN B HD21   1 
ATOM   7220  H HD22   . ASN B 2 6   ? 30.847  -6.578  -6.193  1.00 25.27  ?  6    ASN B HD22   1 
ATOM   7221  N N      . LEU B 2 7   ? 28.284  -9.308  -10.076 1.00 15.38  ?  7    LEU B N      1 
ATOM   7222  C CA     . LEU B 2 7   ? 26.995  -9.553  -10.720 1.00 15.49  ?  7    LEU B CA     1 
ATOM   7223  C C      . LEU B 2 7   ? 26.940  -10.938 -11.341 1.00 16.27  ?  7    LEU B C      1 
ATOM   7224  O O      . LEU B 2 7   ? 25.937  -11.651 -11.208 1.00 15.87  ?  7    LEU B O      1 
ATOM   7225  C CB     . LEU B 2 7   ? 26.755  -8.510  -11.792 1.00 19.18  ?  7    LEU B CB     1 
ATOM   7226  C CG     . LEU B 2 7   ? 25.848  -7.355  -11.429 1.00 25.68  ?  7    LEU B CG     1 
ATOM   7227  C CD1    . LEU B 2 7   ? 25.790  -6.374  -12.605 1.00 28.21  ?  7    LEU B CD1    1 
ATOM   7228  C CD2    . LEU B 2 7   ? 24.427  -7.846  -11.030 1.00 25.03  ?  7    LEU B CD2    1 
ATOM   7229  H H      . LEU B 2 7   ? 28.757  -8.696  -10.451 1.00 18.45  ?  7    LEU B H      1 
ATOM   7230  H HA     . LEU B 2 7   ? 26.298  -9.486  -10.049 1.00 18.59  ?  7    LEU B HA     1 
ATOM   7231  H HB2    . LEU B 2 7   ? 27.613  -8.131  -12.039 1.00 23.02  ?  7    LEU B HB2    1 
ATOM   7232  H HB3    . LEU B 2 7   ? 26.356  -8.954  -12.557 1.00 23.02  ?  7    LEU B HB3    1 
ATOM   7233  H HG     . LEU B 2 7   ? 26.204  -6.894  -10.653 1.00 30.81  ?  7    LEU B HG     1 
ATOM   7234  H HD11   . LEU B 2 7   ? 25.248  -5.610  -12.353 1.00 33.85  ?  7    LEU B HD11   1 
ATOM   7235  H HD12   . LEU B 2 7   ? 26.690  -6.085  -12.820 1.00 33.85  ?  7    LEU B HD12   1 
ATOM   7236  H HD13   . LEU B 2 7   ? 25.396  -6.822  -13.370 1.00 33.85  ?  7    LEU B HD13   1 
ATOM   7237  H HD21   . LEU B 2 7   ? 23.822  -7.088  -11.021 1.00 30.03  ?  7    LEU B HD21   1 
ATOM   7238  H HD22   . LEU B 2 7   ? 24.126  -8.502  -11.678 1.00 30.03  ?  7    LEU B HD22   1 
ATOM   7239  H HD23   . LEU B 2 7   ? 24.467  -8.247  -10.147 1.00 30.03  ?  7    LEU B HD23   1 
ATOM   7240  N N      . ILE B 2 8   ? 28.014  -11.336 -12.023 1.00 15.59  ?  8    ILE B N      1 
ATOM   7241  C CA     . ILE B 2 8   ? 28.086  -12.684 -12.577 1.00 15.48  ?  8    ILE B CA     1 
ATOM   7242  C C      . ILE B 2 8   ? 27.935  -13.715 -11.467 1.00 15.74  ?  8    ILE B C      1 
ATOM   7243  O O      . ILE B 2 8   ? 27.204  -14.699 -11.611 1.00 15.46  ?  8    ILE B O      1 
ATOM   7244  C CB     . ILE B 2 8   ? 29.399  -12.861 -13.366 1.00 14.64  ?  8    ILE B CB     1 
ATOM   7245  C CG1    . ILE B 2 8   ? 29.360  -12.012 -14.622 1.00 16.21  ?  8    ILE B CG1    1 
ATOM   7246  C CG2    . ILE B 2 8   ? 29.628  -14.337 -13.687 1.00 15.62  ?  8    ILE B CG2    1 
ATOM   7247  C CD1    . ILE B 2 8   ? 30.693  -11.852 -15.282 1.00 17.19  ?  8    ILE B CD1    1 
ATOM   7248  H H      . ILE B 2 8   ? 28.707  -10.852 -12.177 1.00 18.71  ?  8    ILE B H      1 
ATOM   7249  H HA     . ILE B 2 8   ? 27.353  -12.813 -13.198 1.00 18.58  ?  8    ILE B HA     1 
ATOM   7250  H HB     . ILE B 2 8   ? 30.144  -12.561 -12.823 1.00 17.56  ?  8    ILE B HB     1 
ATOM   7251  H HG12   . ILE B 2 8   ? 28.761  -12.427 -15.262 1.00 19.45  ?  8    ILE B HG12   1 
ATOM   7252  H HG13   . ILE B 2 8   ? 29.036  -11.127 -14.391 1.00 19.45  ?  8    ILE B HG13   1 
ATOM   7253  H HG21   . ILE B 2 8   ? 30.294  -14.408 -14.388 1.00 18.74  ?  8    ILE B HG21   1 
ATOM   7254  H HG22   . ILE B 2 8   ? 29.939  -14.790 -12.888 1.00 18.74  ?  8    ILE B HG22   1 
ATOM   7255  H HG23   . ILE B 2 8   ? 28.792  -14.729 -13.985 1.00 18.74  ?  8    ILE B HG23   1 
ATOM   7256  H HD11   . ILE B 2 8   ? 30.624  -11.176 -15.975 1.00 20.63  ?  8    ILE B HD11   1 
ATOM   7257  H HD12   . ILE B 2 8   ? 31.344  -11.578 -14.617 1.00 20.63  ?  8    ILE B HD12   1 
ATOM   7258  H HD13   . ILE B 2 8   ? 30.956  -12.700 -15.673 1.00 20.63  ?  8    ILE B HD13   1 
ATOM   7259  N N      . ASP B 2 9   ? 28.624  -13.503 -10.340 1.00 15.38  ?  9    ASP B N      1 
ATOM   7260  C CA     . ASP B 2 9   ? 28.574  -14.472 -9.252  1.00 15.30  ?  9    ASP B CA     1 
ATOM   7261  C C      . ASP B 2 9   ? 27.178  -14.569 -8.648  1.00 15.16  ?  9    ASP B C      1 
ATOM   7262  O O      . ASP B 2 9   ? 26.787  -15.645 -8.176  1.00 15.64  ?  9    ASP B O      1 
ATOM   7263  C CB     . ASP B 2 9   ? 29.636  -14.155 -8.200  1.00 16.94  ?  9    ASP B CB     1 
ATOM   7264  C CG     . ASP B 2 9   ? 31.059  -14.432 -8.676  1.00 19.21  ?  9    ASP B CG     1 
ATOM   7265  O OD1    . ASP B 2 9   ? 31.253  -14.990 -9.780  1.00 19.94  ?  9    ASP B OD1    1 
ATOM   7266  O OD2    . ASP B 2 9   ? 32.008  -14.075 -7.934  1.00 20.11  -1 9    ASP B OD2    1 
ATOM   7267  H H      . ASP B 2 9   ? 29.118  -12.817 -10.184 1.00 18.45  ?  9    ASP B H      1 
ATOM   7268  H HA     . ASP B 2 9   ? 28.792  -15.350 -9.602  1.00 18.35  ?  9    ASP B HA     1 
ATOM   7269  H HB2    . ASP B 2 9   ? 29.578  -13.214 -7.969  1.00 20.33  ?  9    ASP B HB2    1 
ATOM   7270  H HB3    . ASP B 2 9   ? 29.473  -14.700 -7.415  1.00 20.33  ?  9    ASP B HB3    1 
ATOM   7271  N N      . ARG B 2 10  ? 26.415  -13.470 -8.648  1.00 14.48  ?  10   ARG B N      1 
ATOM   7272  C CA     . ARG B 2 10  ? 25.009  -13.558 -8.264  1.00 14.36  ?  10   ARG B CA     1 
ATOM   7273  C C      . ARG B 2 10  ? 24.257  -14.440 -9.243  1.00 14.19  ?  10   ARG B C      1 
ATOM   7274  O O      . ARG B 2 10  ? 23.485  -15.323 -8.841  1.00 13.57  ?  10   ARG B O      1 
ATOM   7275  C CB     . ARG B 2 10  ? 24.371  -12.164 -8.223  1.00 14.66  ?  10   ARG B CB     1 
ATOM   7276  C CG     . ARG B 2 10  ? 24.713  -11.379 -6.960  1.00 15.88  ?  10   ARG B CG     1 
ATOM   7277  C CD     . ARG B 2 10  ? 24.372  -9.910  -7.116  1.00 16.23  ?  10   ARG B CD     1 
ATOM   7278  N NE     . ARG B 2 10  ? 22.944  -9.696  -7.318  1.00 15.06  ?  10   ARG B NE     1 
ATOM   7279  C CZ     . ARG B 2 10  ? 22.399  -8.525  -7.628  1.00 15.81  ?  10   ARG B CZ     1 
ATOM   7280  N NH1    . ARG B 2 10  ? 23.161  -7.448  -7.755  1.00 17.20  ?  10   ARG B NH1    1 
ATOM   7281  N NH2    . ARG B 2 10  ? 21.089  -8.420  -7.802  1.00 18.02  ?  10   ARG B NH2    1 
ATOM   7282  H H      . ARG B 2 10  ? 26.682  -12.681 -8.862  1.00 17.37  ?  10   ARG B H      1 
ATOM   7283  H HA     . ARG B 2 10  ? 24.949  -13.937 -7.373  1.00 17.22  ?  10   ARG B HA     1 
ATOM   7284  H HB2    . ARG B 2 10  ? 24.685  -11.653 -8.985  1.00 17.59  ?  10   ARG B HB2    1 
ATOM   7285  H HB3    . ARG B 2 10  ? 23.406  -12.259 -8.262  1.00 17.59  ?  10   ARG B HB3    1 
ATOM   7286  H HG2    . ARG B 2 10  ? 24.205  -11.734 -6.213  1.00 19.05  ?  10   ARG B HG2    1 
ATOM   7287  H HG3    . ARG B 2 10  ? 25.663  -11.456 -6.781  1.00 19.05  ?  10   ARG B HG3    1 
ATOM   7288  H HD2    . ARG B 2 10  ? 24.639  -9.434  -6.313  1.00 19.47  ?  10   ARG B HD2    1 
ATOM   7289  H HD3    . ARG B 2 10  ? 24.844  -9.553  -7.885  1.00 19.47  ?  10   ARG B HD3    1 
ATOM   7290  H HE     . ARG B 2 10  ? 22.420  -10.372 -7.232  1.00 18.06  ?  10   ARG B HE     1 
ATOM   7291  H HH11   . ARG B 2 10  ? 24.011  -7.506  -7.638  1.00 20.64  ?  10   ARG B HH11   1 
ATOM   7292  H HH12   . ARG B 2 10  ? 22.806  -6.691  -7.956  1.00 20.64  ?  10   ARG B HH12   1 
ATOM   7293  H HH21   . ARG B 2 10  ? 20.587  -9.113  -7.715  1.00 21.62  ?  10   ARG B HH21   1 
ATOM   7294  H HH22   . ARG B 2 10  ? 20.741  -7.660  -8.002  1.00 21.62  ?  10   ARG B HH22   1 
ATOM   7295  N N      . ASP B 2 11  ? 24.513  -14.238 -10.540 1.00 13.46  ?  11   ASP B N      1 
ATOM   7296  C CA     . ASP B 2 11  ? 23.825  -14.981 -11.589 1.00 13.88  ?  11   ASP B CA     1 
ATOM   7297  C C      . ASP B 2 11  ? 24.142  -16.466 -11.522 1.00 14.25  ?  11   ASP B C      1 
ATOM   7298  O O      . ASP B 2 11  ? 23.260  -17.301 -11.755 1.00 14.19  ?  11   ASP B O      1 
ATOM   7299  C CB     . ASP B 2 11  ? 24.250  -14.381 -12.930 1.00 13.40  ?  11   ASP B CB     1 
ATOM   7300  C CG     . ASP B 2 11  ? 23.419  -14.869 -14.086 1.00 14.48  ?  11   ASP B CG     1 
ATOM   7301  O OD1    . ASP B 2 11  ? 22.177  -14.948 -13.932 1.00 14.06  ?  11   ASP B OD1    1 
ATOM   7302  O OD2    . ASP B 2 11  ? 23.987  -15.172 -15.140 1.00 15.59  -1 11   ASP B OD2    1 
ATOM   7303  H H      . ASP B 2 11  ? 25.086  -13.672 -10.841 1.00 16.15  ?  11   ASP B H      1 
ATOM   7304  H HA     . ASP B 2 11  ? 22.863  -14.901 -11.489 1.00 16.65  ?  11   ASP B HA     1 
ATOM   7305  H HB2    . ASP B 2 11  ? 24.160  -13.416 -12.885 1.00 16.07  ?  11   ASP B HB2    1 
ATOM   7306  H HB3    . ASP B 2 11  ? 25.173  -14.621 -13.104 1.00 16.07  ?  11   ASP B HB3    1 
ATOM   7307  N N      . ARG B 2 12  ? 25.386  -16.816 -11.171 1.00 15.24  ?  12   ARG B N      1 
ATOM   7308  C CA     . ARG B 2 12  ? 25.769  -18.227 -11.054 1.00 15.32  ?  12   ARG B CA     1 
ATOM   7309  C C      . ARG B 2 12  ? 24.870  -18.979 -10.084 1.00 14.17  ?  12   ARG B C      1 
ATOM   7310  O O      . ARG B 2 12  ? 24.666  -20.188 -10.240 1.00 14.83  ?  12   ARG B O      1 
ATOM   7311  C CB     . ARG B 2 12  ? 27.205  -18.357 -10.556 1.00 15.31  ?  12   ARG B CB     1 
ATOM   7312  C CG     . ARG B 2 12  ? 28.268  -17.826 -11.512 1.00 15.20  ?  12   ARG B CG     1 
ATOM   7313  C CD     . ARG B 2 12  ? 29.632  -17.987 -10.874 1.00 14.14  ?  12   ARG B CD     1 
ATOM   7314  N NE     . ARG B 2 12  ? 30.673  -17.242 -11.558 1.00 15.99  ?  12   ARG B NE     1 
ATOM   7315  C CZ     . ARG B 2 12  ? 31.244  -17.622 -12.695 1.00 17.60  ?  12   ARG B CZ     1 
ATOM   7316  N NH1    . ARG B 2 12  ? 30.858  -18.725 -13.290 1.00 17.63  ?  12   ARG B NH1    1 
ATOM   7317  N NH2    . ARG B 2 12  ? 32.194  -16.879 -13.256 1.00 18.38  ?  12   ARG B NH2    1 
ATOM   7318  H H      . ARG B 2 12  ? 26.021  -16.264 -10.995 1.00 18.29  ?  12   ARG B H      1 
ATOM   7319  H HA     . ARG B 2 12  ? 25.698  -18.619 -11.939 1.00 18.38  ?  12   ARG B HA     1 
ATOM   7320  H HB2    . ARG B 2 12  ? 27.288  -17.863 -9.726  1.00 18.37  ?  12   ARG B HB2    1 
ATOM   7321  H HB3    . ARG B 2 12  ? 27.394  -19.296 -10.404 1.00 18.37  ?  12   ARG B HB3    1 
ATOM   7322  H HG2    . ARG B 2 12  ? 28.247  -18.329 -12.341 1.00 18.24  ?  12   ARG B HG2    1 
ATOM   7323  H HG3    . ARG B 2 12  ? 28.112  -16.886 -11.690 1.00 18.24  ?  12   ARG B HG3    1 
ATOM   7324  H HD2    . ARG B 2 12  ? 29.590  -17.669 -9.959  1.00 16.96  ?  12   ARG B HD2    1 
ATOM   7325  H HD3    . ARG B 2 12  ? 29.878  -18.925 -10.889 1.00 16.96  ?  12   ARG B HD3    1 
ATOM   7326  H HE     . ARG B 2 12  ? 30.938  -16.504 -11.203 1.00 19.18  ?  12   ARG B HE     1 
ATOM   7327  H HH11   . ARG B 2 12  ? 30.233  -19.204 -12.944 1.00 21.15  ?  12   ARG B HH11   1 
ATOM   7328  H HH12   . ARG B 2 12  ? 31.230  -18.969 -14.026 1.00 21.15  ?  12   ARG B HH12   1 
ATOM   7329  H HH21   . ARG B 2 12  ? 32.443  -16.145 -12.882 1.00 22.05  ?  12   ARG B HH21   1 
ATOM   7330  H HH22   . ARG B 2 12  ? 32.559  -17.131 -13.992 1.00 22.05  ?  12   ARG B HH22   1 
ATOM   7331  N N      . LYS B 2 13  ? 24.344  -18.293 -9.067  1.00 13.51  ?  13   LYS B N      1 
ATOM   7332  C CA     . LYS B 2 13  ? 23.539  -18.962 -8.059  1.00 14.92  ?  13   LYS B CA     1 
ATOM   7333  C C      . LYS B 2 13  ? 22.069  -19.122 -8.464  1.00 12.47  ?  13   LYS B C      1 
ATOM   7334  O O      . LYS B 2 13  ? 21.354  -19.870 -7.794  1.00 13.58  ?  13   LYS B O      1 
ATOM   7335  C CB     . LYS B 2 13  ? 23.598  -18.186 -6.738  1.00 14.45  ?  13   LYS B CB     1 
ATOM   7336  C CG     . LYS B 2 13  ? 25.013  -18.041 -6.159  1.00 15.14  ?  13   LYS B CG     1 
ATOM   7337  C CD     . LYS B 2 13  ? 25.080  -17.061 -4.998  1.00 18.54  ?  13   LYS B CD     1 
ATOM   7338  C CE     . LYS B 2 13  ? 26.512  -16.915 -4.439  1.00 22.11  ?  13   LYS B CE     1 
ATOM   7339  N NZ     . LYS B 2 13  ? 27.517  -16.366 -5.448  1.00 23.64  ?  13   LYS B NZ     1 
ATOM   7340  H H      . LYS B 2 13  ? 24.442  -17.447 -8.943  1.00 16.21  ?  13   LYS B H      1 
ATOM   7341  H HA     . LYS B 2 13  ? 23.911  -19.847 -7.919  1.00 17.90  ?  13   LYS B HA     1 
ATOM   7342  H HB2    . LYS B 2 13  ? 23.247  -17.293 -6.886  1.00 17.34  ?  13   LYS B HB2    1 
ATOM   7343  H HB3    . LYS B 2 13  ? 23.057  -18.650 -6.080  1.00 17.34  ?  13   LYS B HB3    1 
ATOM   7344  H HG2    . LYS B 2 13  ? 25.314  -18.905 -5.838  1.00 18.16  ?  13   LYS B HG2    1 
ATOM   7345  H HG3    . LYS B 2 13  ? 25.608  -17.720 -6.855  1.00 18.16  ?  13   LYS B HG3    1 
ATOM   7346  H HD2    . LYS B 2 13  ? 24.783  -16.189 -5.300  1.00 22.24  ?  13   LYS B HD2    1 
ATOM   7347  H HD3    . LYS B 2 13  ? 24.507  -17.377 -4.282  1.00 22.24  ?  13   LYS B HD3    1 
ATOM   7348  H HE2    . LYS B 2 13  ? 26.491  -16.307 -3.683  1.00 26.53  ?  13   LYS B HE2    1 
ATOM   7349  H HE3    . LYS B 2 13  ? 26.826  -17.787 -4.155  1.00 26.53  ?  13   LYS B HE3    1 
ATOM   7350  H HZ1    . LYS B 2 13  ? 28.316  -16.280 -5.065  1.00 28.36  ?  13   LYS B HZ1    1 
ATOM   7351  H HZ2    . LYS B 2 13  ? 27.587  -16.920 -6.141  1.00 28.36  ?  13   LYS B HZ2    1 
ATOM   7352  H HZ3    . LYS B 2 13  ? 27.250  -15.569 -5.741  1.00 28.36  ?  13   LYS B HZ3    1 
ATOM   7353  N N      . VAL B 2 14  ? 21.600  -18.434 -9.510  1.00 13.31  ?  14   VAL B N      1 
ATOM   7354  C CA     . VAL B 2 14  ? 20.158  -18.320 -9.720  1.00 12.90  ?  14   VAL B CA     1 
ATOM   7355  C C      . VAL B 2 14  ? 19.690  -18.590 -11.142 1.00 12.34  ?  14   VAL B C      1 
ATOM   7356  O O      . VAL B 2 14  ? 18.488  -18.856 -11.325 1.00 14.58  ?  14   VAL B O      1 
ATOM   7357  C CB     . VAL B 2 14  ? 19.611  -16.962 -9.241  1.00 13.77  ?  14   VAL B CB     1 
ATOM   7358  C CG1    . VAL B 2 14  ? 19.845  -16.774 -7.755  1.00 14.78  ?  14   VAL B CG1    1 
ATOM   7359  C CG2    . VAL B 2 14  ? 20.241  -15.811 -10.042 1.00 15.30  ?  14   VAL B CG2    1 
ATOM   7360  H H      . VAL B 2 14  ? 22.086  -18.034 -10.096 1.00 15.97  ?  14   VAL B H      1 
ATOM   7361  H HA     . VAL B 2 14  ? 19.757  -19.008 -9.166  1.00 15.48  ?  14   VAL B HA     1 
ATOM   7362  H HB     . VAL B 2 14  ? 18.653  -16.946 -9.392  1.00 16.52  ?  14   VAL B HB     1 
ATOM   7363  H HG11   . VAL B 2 14  ? 19.423  -15.949 -7.471  1.00 17.74  ?  14   VAL B HG11   1 
ATOM   7364  H HG12   . VAL B 2 14  ? 19.459  -17.525 -7.277  1.00 17.74  ?  14   VAL B HG12   1 
ATOM   7365  H HG13   . VAL B 2 14  ? 20.800  -16.732 -7.589  1.00 17.74  ?  14   VAL B HG13   1 
ATOM   7366  H HG21   . VAL B 2 14  ? 19.915  -14.967 -9.694  1.00 18.36  ?  14   VAL B HG21   1 
ATOM   7367  H HG22   . VAL B 2 14  ? 21.206  -15.855 -9.952  1.00 18.36  ?  14   VAL B HG22   1 
ATOM   7368  H HG23   . VAL B 2 14  ? 19.992  -15.903 -10.975 1.00 18.36  ?  14   VAL B HG23   1 
ATOM   7369  N N      . THR B 2 15  ? 20.522  -18.514 -12.190 1.00 12.82  ?  15   THR B N      1 
ATOM   7370  C CA     . THR B 2 15  ? 20.028  -18.640 -13.559 1.00 11.38  ?  15   THR B CA     1 
ATOM   7371  C C      . THR B 2 15  ? 20.622  -19.850 -14.283 1.00 13.93  ?  15   THR B C      1 
ATOM   7372  O O      . THR B 2 15  ? 21.838  -20.071 -14.253 1.00 14.49  ?  15   THR B O      1 
ATOM   7373  C CB     . THR B 2 15  ? 20.307  -17.362 -14.371 1.00 13.05  ?  15   THR B CB     1 
ATOM   7374  O OG1    . THR B 2 15  ? 19.800  -16.215 -13.682 1.00 14.29  ?  15   THR B OG1    1 
ATOM   7375  C CG2    . THR B 2 15  ? 19.679  -17.426 -15.737 1.00 13.69  ?  15   THR B CG2    1 
ATOM   7376  H H      . THR B 2 15  ? 21.371  -18.392 -12.126 1.00 15.38  ?  15   THR B H      1 
ATOM   7377  H HA     . THR B 2 15  ? 19.071  -18.792 -13.506 1.00 13.66  ?  15   THR B HA     1 
ATOM   7378  H HB     . THR B 2 15  ? 21.267  -17.278 -14.482 1.00 15.66  ?  15   THR B HB     1 
ATOM   7379  H HG1    . THR B 2 15  ? 19.941  -15.522 -14.135 1.00 17.14  ?  15   THR B HG1    1 
ATOM   7380  H HG21   . THR B 2 15  ? 19.783  -16.575 -16.190 1.00 16.42  ?  15   THR B HG21   1 
ATOM   7381  H HG22   . THR B 2 15  ? 20.106  -18.119 -16.266 1.00 16.42  ?  15   THR B HG22   1 
ATOM   7382  H HG23   . THR B 2 15  ? 18.734  -17.628 -15.658 1.00 16.42  ?  15   THR B HG23   1 
ATOM   7383  N N      . PHE B 2 16  ? 19.741  -20.622 -14.934 1.00 13.32  ?  16   PHE B N      1 
ATOM   7384  C CA     . PHE B 2 16  ? 20.077  -21.660 -15.919 1.00 11.91  ?  16   PHE B CA     1 
ATOM   7385  C C      . PHE B 2 16  ? 20.076  -20.957 -17.265 1.00 13.12  ?  16   PHE B C      1 
ATOM   7386  O O      . PHE B 2 16  ? 19.027  -20.484 -17.717 1.00 13.92  ?  16   PHE B O      1 
ATOM   7387  C CB     . PHE B 2 16  ? 19.010  -22.744 -15.756 1.00 11.83  ?  16   PHE B CB     1 
ATOM   7388  C CG     . PHE B 2 16  ? 18.941  -23.832 -16.813 1.00 12.52  ?  16   PHE B CG     1 
ATOM   7389  C CD1    . PHE B 2 16  ? 19.531  -23.744 -18.049 1.00 14.11  ?  16   PHE B CD1    1 
ATOM   7390  C CD2    . PHE B 2 16  ? 18.150  -24.946 -16.537 1.00 13.58  ?  16   PHE B CD2    1 
ATOM   7391  C CE1    . PHE B 2 16  ? 19.371  -24.774 -18.994 1.00 15.03  ?  16   PHE B CE1    1 
ATOM   7392  C CE2    . PHE B 2 16  ? 17.976  -25.974 -17.469 1.00 14.52  ?  16   PHE B CE2    1 
ATOM   7393  C CZ     . PHE B 2 16  ? 18.580  -25.886 -18.694 1.00 14.61  ?  16   PHE B CZ     1 
ATOM   7394  H H      . PHE B 2 16  ? 18.892  -20.558 -14.815 1.00 15.98  ?  16   PHE B H      1 
ATOM   7395  H HA     . PHE B 2 16  ? 20.949  -22.074 -15.823 1.00 14.29  ?  16   PHE B HA     1 
ATOM   7396  H HB2    . PHE B 2 16  ? 19.166  -23.189 -14.908 1.00 14.19  ?  16   PHE B HB2    1 
ATOM   7397  H HB3    . PHE B 2 16  ? 18.143  -22.308 -15.748 1.00 14.19  ?  16   PHE B HB3    1 
ATOM   7398  H HD1    . PHE B 2 16  ? 20.041  -22.996 -18.264 1.00 16.92  ?  16   PHE B HD1    1 
ATOM   7399  H HD2    . PHE B 2 16  ? 17.728  -25.008 -15.711 1.00 16.30  ?  16   PHE B HD2    1 
ATOM   7400  H HE1    . PHE B 2 16  ? 19.794  -24.715 -19.820 1.00 18.03  ?  16   PHE B HE1    1 
ATOM   7401  H HE2    . PHE B 2 16  ? 17.452  -26.713 -17.257 1.00 17.42  ?  16   PHE B HE2    1 
ATOM   7402  H HZ     . PHE B 2 16  ? 18.464  -26.562 -19.323 1.00 17.52  ?  16   PHE B HZ     1 
ATOM   7403  N N      . HIS B 2 17  ? 21.262  -20.837 -17.875 1.00 13.20  ?  17   HIS B N      1 
ATOM   7404  C CA     . HIS B 2 17  ? 21.423  -20.212 -19.181 1.00 12.63  ?  17   HIS B CA     1 
ATOM   7405  C C      . HIS B 2 17  ? 21.403  -21.215 -20.332 1.00 11.66  ?  17   HIS B C      1 
ATOM   7406  O O      . HIS B 2 17  ? 21.920  -22.324 -20.231 1.00 13.94  ?  17   HIS B O      1 
ATOM   7407  C CB     . HIS B 2 17  ? 22.748  -19.444 -19.264 1.00 15.06  ?  17   HIS B CB     1 
ATOM   7408  C CG     . HIS B 2 17  ? 22.738  -18.158 -18.501 1.00 13.49  ?  17   HIS B CG     1 
ATOM   7409  N ND1    . HIS B 2 17  ? 22.168  -17.015 -19.003 1.00 15.13  ?  17   HIS B ND1    1 
ATOM   7410  C CD2    . HIS B 2 17  ? 23.190  -17.839 -17.262 1.00 13.60  ?  17   HIS B CD2    1 
ATOM   7411  C CE1    . HIS B 2 17  ? 22.280  -16.041 -18.115 1.00 14.08  ?  17   HIS B CE1    1 
ATOM   7412  N NE2    . HIS B 2 17  ? 22.899  -16.512 -17.049 1.00 13.51  ?  17   HIS B NE2    1 
ATOM   7413  H H      . HIS B 2 17  ? 22.001  -21.120 -17.537 1.00 15.84  ?  17   HIS B H      1 
ATOM   7414  H HA     . HIS B 2 17  ? 20.671  -19.611 -19.293 1.00 15.15  ?  17   HIS B HA     1 
ATOM   7415  H HB2    . HIS B 2 17  ? 23.456  -19.999 -18.901 1.00 18.07  ?  17   HIS B HB2    1 
ATOM   7416  H HB3    . HIS B 2 17  ? 22.933  -19.237 -20.194 1.00 18.07  ?  17   HIS B HB3    1 
ATOM   7417  H HD1    . HIS B 2 17  ? 21.796  -16.943 -19.775 1.00 18.15  ?  17   HIS B HD1    1 
ATOM   7418  H HD2    . HIS B 2 17  ? 23.618  -18.412 -16.667 1.00 16.32  ?  17   HIS B HD2    1 
ATOM   7419  H HE1    . HIS B 2 17  ? 21.973  -15.169 -18.224 1.00 16.90  ?  17   HIS B HE1    1 
ATOM   7420  H HE2    . HIS B 2 17  ? 23.089  -16.064 -16.340 1.00 16.21  ?  17   HIS B HE2    1 
ATOM   7421  N N      . ALA B 2 18  ? 20.843  -20.773 -21.449 1.00 13.69  ?  18   ALA B N      1 
ATOM   7422  C CA     . ALA B 2 18  ? 20.937  -21.511 -22.701 1.00 12.69  ?  18   ALA B CA     1 
ATOM   7423  C C      . ALA B 2 18  ? 22.388  -21.858 -23.016 1.00 13.22  ?  18   ALA B C      1 
ATOM   7424  O O      . ALA B 2 18  ? 23.303  -21.064 -22.791 1.00 14.06  ?  18   ALA B O      1 
ATOM   7425  C CB     . ALA B 2 18  ? 20.399  -20.628 -23.832 1.00 14.03  ?  18   ALA B CB     1 
ATOM   7426  H H      . ALA B 2 18  ? 20.397  -20.040 -21.512 1.00 16.42  ?  18   ALA B H      1 
ATOM   7427  H HA     . ALA B 2 18  ? 20.423  -22.331 -22.635 1.00 15.22  ?  18   ALA B HA     1 
ATOM   7428  H HB1    . ALA B 2 18  ? 20.489  -21.103 -24.673 1.00 16.83  ?  18   ALA B HB1    1 
ATOM   7429  H HB2    . ALA B 2 18  ? 19.464  -20.432 -23.662 1.00 16.83  ?  18   ALA B HB2    1 
ATOM   7430  H HB3    . ALA B 2 18  ? 20.910  -19.804 -23.860 1.00 16.83  ?  18   ALA B HB3    1 
ATOM   7431  N N      A SER B 2 19  ? 22.580  -23.057 -23.556 0.51 13.30  ?  19   SER B N      1 
ATOM   7432  N N      B SER B 2 19  ? 22.581  -23.056 -23.559 0.49 12.70  ?  19   SER B N      1 
ATOM   7433  C CA     A SER B 2 19  ? 23.861  -23.466 -24.136 0.51 15.26  ?  19   SER B CA     1 
ATOM   7434  C CA     B SER B 2 19  ? 23.865  -23.472 -24.131 0.49 14.15  ?  19   SER B CA     1 
ATOM   7435  C C      A SER B 2 19  ? 25.034  -23.175 -23.205 0.51 15.76  ?  19   SER B C      1 
ATOM   7436  C C      B SER B 2 19  ? 25.041  -23.190 -23.203 0.49 15.21  ?  19   SER B C      1 
ATOM   7437  O O      A SER B 2 19  ? 26.093  -22.708 -23.628 0.51 18.12  ?  19   SER B O      1 
ATOM   7438  O O      B SER B 2 19  ? 26.112  -22.753 -23.631 0.49 17.08  ?  19   SER B O      1 
ATOM   7439  C CB     A SER B 2 19  ? 24.059  -22.808 -25.505 0.51 17.55  ?  19   SER B CB     1 
ATOM   7440  C CB     B SER B 2 19  ? 24.080  -22.827 -25.502 0.49 14.95  ?  19   SER B CB     1 
ATOM   7441  O OG     A SER B 2 19  ? 25.063  -23.465 -26.259 0.51 19.68  ?  19   SER B OG     1 
ATOM   7442  O OG     B SER B 2 19  ? 23.162  -23.344 -26.440 0.49 16.27  ?  19   SER B OG     1 
ATOM   7443  H H      A SER B 2 19  ? 21.974  -23.665 -23.600 0.51 15.96  ?  19   SER B H      1 
ATOM   7444  H H      B SER B 2 19  ? 21.973  -23.661 -23.611 0.49 15.24  ?  19   SER B H      1 
ATOM   7445  H HA     A SER B 2 19  ? 23.844  -24.428 -24.257 0.51 18.31  ?  19   SER B HA     1 
ATOM   7446  H HA     B SER B 2 19  ? 23.834  -24.435 -24.243 0.49 16.98  ?  19   SER B HA     1 
ATOM   7447  H HB2    A SER B 2 19  ? 23.224  -22.849 -25.995 0.51 21.06  ?  19   SER B HB2    1 
ATOM   7448  H HB2    B SER B 2 19  ? 23.951  -21.869 -25.426 0.49 17.94  ?  19   SER B HB2    1 
ATOM   7449  H HB3    A SER B 2 19  ? 24.322  -21.884 -25.372 0.51 21.06  ?  19   SER B HB3    1 
ATOM   7450  H HB3    B SER B 2 19  ? 24.983  -23.017 -25.803 0.49 17.94  ?  19   SER B HB3    1 
ATOM   7451  H HG     A SER B 2 19  ? 24.819  -24.247 -26.444 0.51 23.61  ?  19   SER B HG     1 
ATOM   7452  H HG     B SER B 2 19  ? 23.191  -22.893 -27.149 0.49 19.52  ?  19   SER B HG     1 
ATOM   7453  N N      . THR B 2 20  ? 24.863  -23.493 -21.927 1.00 14.75  ?  20   THR B N      1 
ATOM   7454  C CA     . THR B 2 20  ? 25.869  -23.217 -20.907 1.00 13.12  ?  20   THR B CA     1 
ATOM   7455  C C      . THR B 2 20  ? 26.309  -24.510 -20.237 1.00 13.86  ?  20   THR B C      1 
ATOM   7456  O O      . THR B 2 20  ? 25.517  -25.434 -20.061 1.00 13.86  ?  20   THR B O      1 
ATOM   7457  C CB     . THR B 2 20  ? 25.321  -22.202 -19.913 1.00 13.25  ?  20   THR B CB     1 
ATOM   7458  O OG1    . THR B 2 20  ? 25.129  -20.967 -20.603 1.00 13.58  ?  20   THR B OG1    1 
ATOM   7459  C CG2    . THR B 2 20  ? 26.268  -21.967 -18.760 1.00 15.19  ?  20   THR B CG2    1 
ATOM   7460  H H      A THR B 2 20  ? 24.156  -23.877 -21.622 0.51 17.69  ?  20   THR B H      1 
ATOM   7461  H H      B THR B 2 20  ? 24.152  -23.866 -21.620 0.49 17.69  ?  20   THR B H      1 
ATOM   7462  H HA     . THR B 2 20  ? 26.674  -22.844 -21.299 1.00 15.74  ?  20   THR B HA     1 
ATOM   7463  H HB     . THR B 2 20  ? 24.490  -22.535 -19.541 1.00 15.89  ?  20   THR B HB     1 
ATOM   7464  H HG1    . THR B 2 20  ? 24.656  -21.090 -21.287 1.00 16.29  ?  20   THR B HG1    1 
ATOM   7465  H HG21   . THR B 2 20  ? 25.949  -21.234 -18.213 1.00 18.22  ?  20   THR B HG21   1 
ATOM   7466  H HG22   . THR B 2 20  ? 26.328  -22.766 -18.213 1.00 18.22  ?  20   THR B HG22   1 
ATOM   7467  H HG23   . THR B 2 20  ? 27.152  -21.749 -19.096 1.00 18.22  ?  20   THR B HG23   1 
ATOM   7468  N N      . HIS B 2 21  ? 27.591  -24.562 -19.884 1.00 14.74  ?  21   HIS B N      1 
ATOM   7469  C CA     . HIS B 2 21  ? 28.120  -25.634 -19.052 1.00 14.32  ?  21   HIS B CA     1 
ATOM   7470  C C      . HIS B 2 21  ? 27.590  -25.398 -17.641 1.00 14.99  ?  21   HIS B C      1 
ATOM   7471  O O      . HIS B 2 21  ? 28.181  -24.653 -16.854 1.00 13.96  ?  21   HIS B O      1 
ATOM   7472  C CB     . HIS B 2 21  ? 29.638  -25.656 -19.079 1.00 13.79  ?  21   HIS B CB     1 
ATOM   7473  C CG     . HIS B 2 21  ? 30.209  -26.929 -18.562 1.00 15.13  ?  21   HIS B CG     1 
ATOM   7474  N ND1    . HIS B 2 21  ? 29.927  -27.397 -17.297 1.00 15.74  ?  21   HIS B ND1    1 
ATOM   7475  C CD2    . HIS B 2 21  ? 31.024  -27.845 -19.138 1.00 16.77  ?  21   HIS B CD2    1 
ATOM   7476  C CE1    . HIS B 2 21  ? 30.566  -28.540 -17.113 1.00 18.81  ?  21   HIS B CE1    1 
ATOM   7477  N NE2    . HIS B 2 21  ? 31.234  -28.834 -18.216 1.00 16.89  ?  21   HIS B NE2    1 
ATOM   7478  H H      . HIS B 2 21  ? 28.181  -23.981 -20.117 1.00 17.68  ?  21   HIS B H      1 
ATOM   7479  H HA     . HIS B 2 21  ? 27.844  -26.506 -19.376 1.00 17.18  ?  21   HIS B HA     1 
ATOM   7480  H HB2    . HIS B 2 21  ? 29.939  -25.543 -19.994 1.00 16.55  ?  21   HIS B HB2    1 
ATOM   7481  H HB3    . HIS B 2 21  ? 29.973  -24.932 -18.527 1.00 16.55  ?  21   HIS B HB3    1 
ATOM   7482  H HD2    . HIS B 2 21  ? 31.375  -27.809 -19.999 1.00 20.12  ?  21   HIS B HD2    1 
ATOM   7483  H HE1    . HIS B 2 21  ? 30.549  -29.052 -16.337 1.00 22.57  ?  21   HIS B HE1    1 
ATOM   7484  H HE2    . HIS B 2 21  ? 31.722  -29.533 -18.334 1.00 20.27  ?  21   HIS B HE2    1 
ATOM   7485  N N      . LEU B 2 22  ? 26.441  -25.994 -17.331 1.00 13.27  ?  22   LEU B N      1 
ATOM   7486  C CA     . LEU B 2 22  ? 25.699  -25.605 -16.134 1.00 13.33  ?  22   LEU B CA     1 
ATOM   7487  C C      . LEU B 2 22  ? 26.518  -25.825 -14.869 1.00 14.33  ?  22   LEU B C      1 
ATOM   7488  O O      . LEU B 2 22  ? 26.520  -24.977 -13.969 1.00 15.51  ?  22   LEU B O      1 
ATOM   7489  C CB     . LEU B 2 22  ? 24.367  -26.355 -16.092 1.00 14.85  ?  22   LEU B CB     1 
ATOM   7490  C CG     . LEU B 2 22  ? 23.435  -26.095 -17.267 1.00 14.87  ?  22   LEU B CG     1 
ATOM   7491  C CD1    . LEU B 2 22  ? 22.135  -26.853 -17.066 1.00 14.87  ?  22   LEU B CD1    1 
ATOM   7492  C CD2    . LEU B 2 22  ? 23.139  -24.601 -17.439 1.00 14.69  ?  22   LEU B CD2    1 
ATOM   7493  H H      . LEU B 2 22  ? 26.069  -26.619 -17.790 1.00 15.92  ?  22   LEU B H      1 
ATOM   7494  H HA     . LEU B 2 22  ? 25.500  -24.656 -16.172 1.00 15.99  ?  22   LEU B HA     1 
ATOM   7495  H HB2    . LEU B 2 22  ? 24.554  -27.306 -16.075 1.00 17.81  ?  22   LEU B HB2    1 
ATOM   7496  H HB3    . LEU B 2 22  ? 23.896  -26.095 -15.285 1.00 17.81  ?  22   LEU B HB3    1 
ATOM   7497  H HG     . LEU B 2 22  ? 23.872  -26.401 -18.076 1.00 17.84  ?  22   LEU B HG     1 
ATOM   7498  H HD11   . LEU B 2 22  ? 21.683  -26.936 -17.920 1.00 17.84  ?  22   LEU B HD11   1 
ATOM   7499  H HD12   . LEU B 2 22  ? 22.334  -27.733 -16.710 1.00 17.84  ?  22   LEU B HD12   1 
ATOM   7500  H HD13   . LEU B 2 22  ? 21.576  -26.362 -16.442 1.00 17.84  ?  22   LEU B HD13   1 
ATOM   7501  H HD21   . LEU B 2 22  ? 22.492  -24.488 -18.153 1.00 17.62  ?  22   LEU B HD21   1 
ATOM   7502  H HD22   . LEU B 2 22  ? 22.779  -24.253 -16.608 1.00 17.62  ?  22   LEU B HD22   1 
ATOM   7503  H HD23   . LEU B 2 22  ? 23.962  -24.140 -17.663 1.00 17.62  ?  22   LEU B HD23   1 
ATOM   7504  N N      . ARG B 2 23  ? 27.236  -26.951 -14.779 1.00 14.21  ?  23   ARG B N      1 
ATOM   7505  C CA     . ARG B 2 23  ? 28.055  -27.204 -13.595 1.00 15.11  ?  23   ARG B CA     1 
ATOM   7506  C C      . ARG B 2 23  ? 29.160  -26.162 -13.463 1.00 15.72  ?  23   ARG B C      1 
ATOM   7507  O O      . ARG B 2 23  ? 29.342  -25.555 -12.399 1.00 15.80  ?  23   ARG B O      1 
ATOM   7508  C CB     . ARG B 2 23  ? 28.684  -28.595 -13.679 1.00 16.31  ?  23   ARG B CB     1 
ATOM   7509  C CG     . ARG B 2 23  ? 29.457  -28.951 -12.423 1.00 17.51  ?  23   ARG B CG     1 
ATOM   7510  C CD     . ARG B 2 23  ? 30.439  -30.083 -12.647 1.00 22.56  ?  23   ARG B CD     1 
ATOM   7511  N NE     . ARG B 2 23  ? 31.472  -29.736 -13.623 1.00 24.02  ?  23   ARG B NE     1 
ATOM   7512  C CZ     . ARG B 2 23  ? 32.394  -30.585 -14.060 1.00 26.09  ?  23   ARG B CZ     1 
ATOM   7513  N NH1    . ARG B 2 23  ? 32.408  -31.834 -13.599 1.00 27.31  ?  23   ARG B NH1    1 
ATOM   7514  N NH2    . ARG B 2 23  ? 33.297  -30.197 -14.962 1.00 25.68  ?  23   ARG B NH2    1 
ATOM   7515  H H      . ARG B 2 23  ? 27.266  -27.569 -15.377 1.00 17.05  ?  23   ARG B H      1 
ATOM   7516  H HA     . ARG B 2 23  ? 27.482  -27.163 -12.814 1.00 18.13  ?  23   ARG B HA     1 
ATOM   7517  H HB2    . ARG B 2 23  ? 27.983  -29.254 -13.800 1.00 19.57  ?  23   ARG B HB2    1 
ATOM   7518  H HB3    . ARG B 2 23  ? 29.298  -28.621 -14.429 1.00 19.57  ?  23   ARG B HB3    1 
ATOM   7519  H HG2    . ARG B 2 23  ? 29.956  -28.174 -12.126 1.00 21.00  ?  23   ARG B HG2    1 
ATOM   7520  H HG3    . ARG B 2 23  ? 28.832  -29.227 -11.733 1.00 21.00  ?  23   ARG B HG3    1 
ATOM   7521  H HD2    . ARG B 2 23  ? 30.876  -30.296 -11.807 1.00 27.07  ?  23   ARG B HD2    1 
ATOM   7522  H HD3    . ARG B 2 23  ? 29.960  -30.859 -12.977 1.00 27.07  ?  23   ARG B HD3    1 
ATOM   7523  H HE     . ARG B 2 23  ? 31.482  -28.933 -13.932 1.00 28.81  ?  23   ARG B HE     1 
ATOM   7524  H HH11   . ARG B 2 23  ? 31.823  -32.085 -13.021 1.00 32.77  ?  23   ARG B HH11   1 
ATOM   7525  H HH12   . ARG B 2 23  ? 33.003  -32.389 -13.878 1.00 32.77  ?  23   ARG B HH12   1 
ATOM   7526  H HH21   . ARG B 2 23  ? 33.284  -29.392 -15.265 1.00 30.82  ?  23   ARG B HH21   1 
ATOM   7527  H HH22   . ARG B 2 23  ? 33.892  -30.752 -15.242 1.00 30.82  ?  23   ARG B HH22   1 
ATOM   7528  N N      . ASP B 2 24  ? 29.955  -25.983 -14.527 1.00 15.70  ?  24   ASP B N      1 
ATOM   7529  C CA     . ASP B 2 24  ? 31.100  -25.084 -14.426 1.00 16.49  ?  24   ASP B CA     1 
ATOM   7530  C C      . ASP B 2 24  ? 30.652  -23.647 -14.182 1.00 16.10  ?  24   ASP B C      1 
ATOM   7531  O O      . ASP B 2 24  ? 31.285  -22.913 -13.417 1.00 17.13  ?  24   ASP B O      1 
ATOM   7532  C CB     . ASP B 2 24  ? 31.957  -25.178 -15.684 1.00 17.68  ?  24   ASP B CB     1 
ATOM   7533  C CG     . ASP B 2 24  ? 32.782  -26.454 -15.749 1.00 18.80  ?  24   ASP B CG     1 
ATOM   7534  O OD1    . ASP B 2 24  ? 32.770  -27.251 -14.780 1.00 20.97  ?  24   ASP B OD1    1 
ATOM   7535  O OD2    . ASP B 2 24  ? 33.446  -26.655 -16.786 1.00 20.63  -1 24   ASP B OD2    1 
ATOM   7536  H H      . ASP B 2 24  ? 29.854  -26.359 -15.294 1.00 18.84  ?  24   ASP B H      1 
ATOM   7537  H HA     . ASP B 2 24  ? 31.647  -25.359 -13.674 1.00 19.78  ?  24   ASP B HA     1 
ATOM   7538  H HB2    . ASP B 2 24  ? 31.378  -25.156 -16.462 1.00 21.22  ?  24   ASP B HB2    1 
ATOM   7539  H HB3    . ASP B 2 24  ? 32.569  -24.425 -15.705 1.00 21.22  ?  24   ASP B HB3    1 
ATOM   7540  N N      . PHE B 2 25  ? 29.543  -23.234 -14.783 1.00 15.59  ?  25   PHE B N      1 
ATOM   7541  C CA     . PHE B 2 25  ? 29.078  -21.873 -14.538 1.00 14.98  ?  25   PHE B CA     1 
ATOM   7542  C C      . PHE B 2 25  ? 28.624  -21.703 -13.095 1.00 14.29  ?  25   PHE B C      1 
ATOM   7543  O O      . PHE B 2 25  ? 28.967  -20.709 -12.445 1.00 15.19  ?  25   PHE B O      1 
ATOM   7544  C CB     . PHE B 2 25  ? 27.964  -21.486 -15.516 1.00 14.41  ?  25   PHE B CB     1 
ATOM   7545  C CG     . PHE B 2 25  ? 27.578  -20.039 -15.414 1.00 13.45  ?  25   PHE B CG     1 
ATOM   7546  C CD1    . PHE B 2 25  ? 28.432  -19.044 -15.865 1.00 15.08  ?  25   PHE B CD1    1 
ATOM   7547  C CD2    . PHE B 2 25  ? 26.367  -19.664 -14.846 1.00 15.01  ?  25   PHE B CD2    1 
ATOM   7548  C CE1    . PHE B 2 25  ? 28.084  -17.706 -15.749 1.00 16.54  ?  25   PHE B CE1    1 
ATOM   7549  C CE2    . PHE B 2 25  ? 26.020  -18.343 -14.727 1.00 13.42  ?  25   PHE B CE2    1 
ATOM   7550  C CZ     . PHE B 2 25  ? 26.877  -17.349 -15.169 1.00 15.33  ?  25   PHE B CZ     1 
ATOM   7551  H H      . PHE B 2 25  ? 29.056  -23.701 -15.317 1.00 18.70  ?  25   PHE B H      1 
ATOM   7552  H HA     . PHE B 2 25  ? 29.815  -21.264 -14.698 1.00 17.98  ?  25   PHE B HA     1 
ATOM   7553  H HB2    . PHE B 2 25  ? 28.267  -21.652 -16.422 1.00 17.29  ?  25   PHE B HB2    1 
ATOM   7554  H HB3    . PHE B 2 25  ? 27.177  -22.020 -15.326 1.00 17.29  ?  25   PHE B HB3    1 
ATOM   7555  H HD1    . PHE B 2 25  ? 29.246  -19.275 -16.249 1.00 18.09  ?  25   PHE B HD1    1 
ATOM   7556  H HD2    . PHE B 2 25  ? 25.782  -20.320 -14.540 1.00 18.00  ?  25   PHE B HD2    1 
ATOM   7557  H HE1    . PHE B 2 25  ? 28.661  -17.048 -16.062 1.00 19.84  ?  25   PHE B HE1    1 
ATOM   7558  H HE2    . PHE B 2 25  ? 25.203  -18.113 -14.348 1.00 16.09  ?  25   PHE B HE2    1 
ATOM   7559  H HZ     . PHE B 2 25  ? 26.646  -16.453 -15.077 1.00 18.40  ?  25   PHE B HZ     1 
ATOM   7560  N N      . ALA B 2 26  ? 27.858  -22.661 -12.572 1.00 15.22  ?  26   ALA B N      1 
ATOM   7561  C CA     . ALA B 2 26  ? 27.369  -22.535 -11.202 1.00 15.68  ?  26   ALA B CA     1 
ATOM   7562  C C      . ALA B 2 26  ? 28.506  -22.563 -10.199 1.00 16.22  ?  26   ALA B C      1 
ATOM   7563  O O      . ALA B 2 26  ? 28.404  -21.948 -9.137  1.00 18.60  ?  26   ALA B O      1 
ATOM   7564  C CB     . ALA B 2 26  ? 26.380  -23.640 -10.881 1.00 16.24  ?  26   ALA B CB     1 
ATOM   7565  H H      . ALA B 2 26  ? 27.611  -23.378 -12.979 1.00 18.26  ?  26   ALA B H      1 
ATOM   7566  H HA     . ALA B 2 26  ? 26.907  -21.686 -11.124 1.00 18.81  ?  26   ALA B HA     1 
ATOM   7567  H HB1    . ALA B 2 26  ? 26.099  -23.554 -9.957  1.00 19.48  ?  26   ALA B HB1    1 
ATOM   7568  H HB2    . ALA B 2 26  ? 25.612  -23.558 -11.469 1.00 19.48  ?  26   ALA B HB2    1 
ATOM   7569  H HB3    . ALA B 2 26  ? 26.810  -24.499 -11.018 1.00 19.48  ?  26   ALA B HB3    1 
ATOM   7570  N N      . HIS B 2 27  ? 29.593  -23.248 -10.520 1.00 15.96  ?  27   HIS B N      1 
ATOM   7571  C CA     . HIS B 2 27  ? 30.697  -23.429 -9.582  1.00 17.63  ?  27   HIS B CA     1 
ATOM   7572  C C      . HIS B 2 27  ? 31.837  -22.454 -9.789  1.00 19.07  ?  27   HIS B C      1 
ATOM   7573  O O      . HIS B 2 27  ? 32.847  -22.550 -9.084  1.00 20.61  ?  27   HIS B O      1 
ATOM   7574  C CB     . HIS B 2 27  ? 31.221  -24.859 -9.624  1.00 21.24  ?  27   HIS B CB     1 
ATOM   7575  C CG     . HIS B 2 27  ? 30.290  -25.856 -9.009  1.00 24.16  ?  27   HIS B CG     1 
ATOM   7576  N ND1    . HIS B 2 27  ? 30.439  -26.311 -7.718  1.00 28.89  ?  27   HIS B ND1    1 
ATOM   7577  C CD2    . HIS B 2 27  ? 29.192  -26.472 -9.501  1.00 24.35  ?  27   HIS B CD2    1 
ATOM   7578  C CE1    . HIS B 2 27  ? 29.477  -27.179 -7.448  1.00 28.04  ?  27   HIS B CE1    1 
ATOM   7579  N NE2    . HIS B 2 27  ? 28.715  -27.300 -8.518  1.00 25.74  ?  27   HIS B NE2    1 
ATOM   7580  H H      . HIS B 2 27  ? 29.718  -23.623 -11.284 1.00 19.15  ?  27   HIS B H      1 
ATOM   7581  H HA     . HIS B 2 27  ? 30.350  -23.277 -8.689  1.00 21.15  ?  27   HIS B HA     1 
ATOM   7582  H HB2    . HIS B 2 27  ? 31.359  -25.114 -10.550 1.00 25.49  ?  27   HIS B HB2    1 
ATOM   7583  H HB3    . HIS B 2 27  ? 32.060  -24.899 -9.140  1.00 25.49  ?  27   HIS B HB3    1 
ATOM   7584  H HD2    . HIS B 2 27  ? 28.827  -26.355 -10.349 1.00 29.21  ?  27   HIS B HD2    1 
ATOM   7585  H HE1    . HIS B 2 27  ? 29.359  -27.626 -6.641  1.00 33.65  ?  27   HIS B HE1    1 
ATOM   7586  H HE2    . HIS B 2 27  ? 28.030  -27.816 -8.588  1.00 30.88  ?  27   HIS B HE2    1 
ATOM   7587  N N      . GLY B 2 28  ? 31.707  -21.509 -10.712 1.00 19.24  ?  28   GLY B N      1 
ATOM   7588  C CA     . GLY B 2 28  ? 32.686  -20.452 -10.860 1.00 21.55  ?  28   GLY B CA     1 
ATOM   7589  C C      . GLY B 2 28  ? 33.804  -20.731 -11.827 1.00 22.26  ?  28   GLY B C      1 
ATOM   7590  O O      . GLY B 2 28  ? 34.735  -19.922 -11.914 1.00 26.60  ?  28   GLY B O      1 
ATOM   7591  H H      . GLY B 2 28  ? 31.052  -21.461 -11.268 1.00 23.09  ?  28   GLY B H      1 
ATOM   7592  H HA2    . GLY B 2 28  ? 32.230  -19.651 -11.162 1.00 25.86  ?  28   GLY B HA2    1 
ATOM   7593  H HA3    . GLY B 2 28  ? 33.085  -20.279 -9.993  1.00 25.86  ?  28   GLY B HA3    1 
ATOM   7594  N N      . GLU B 2 29  ? 33.746  -21.849 -12.552 1.00 22.38  ?  29   GLU B N      1 
ATOM   7595  C CA     . GLU B 2 29  ? 34.839  -22.294 -13.402 1.00 26.74  ?  29   GLU B CA     1 
ATOM   7596  C C      . GLU B 2 29  ? 34.643  -21.935 -14.868 1.00 27.02  ?  29   GLU B C      1 
ATOM   7597  O O      . GLU B 2 29  ? 35.570  -22.110 -15.661 1.00 34.95  ?  29   GLU B O      1 
ATOM   7598  C CB     . GLU B 2 29  ? 35.002  -23.820 -13.300 1.00 34.49  ?  29   GLU B CB     1 
ATOM   7599  C CG     . GLU B 2 29  ? 35.392  -24.351 -11.935 1.00 43.14  ?  29   GLU B CG     1 
ATOM   7600  C CD     . GLU B 2 29  ? 36.848  -24.106 -11.619 1.00 51.36  ?  29   GLU B CD     1 
ATOM   7601  O OE1    . GLU B 2 29  ? 37.190  -24.023 -10.420 1.00 54.55  ?  29   GLU B OE1    1 
ATOM   7602  O OE2    . GLU B 2 29  ? 37.654  -23.992 -12.576 1.00 55.12  -1 29   GLU B OE2    1 
ATOM   7603  H H      . GLU B 2 29  ? 33.066  -22.376 -12.564 1.00 26.85  ?  29   GLU B H      1 
ATOM   7604  H HA     . GLU B 2 29  ? 35.654  -21.872 -13.089 1.00 32.08  ?  29   GLU B HA     1 
ATOM   7605  H HB2    . GLU B 2 29  ? 34.157  -24.232 -13.538 1.00 41.39  ?  29   GLU B HB2    1 
ATOM   7606  H HB3    . GLU B 2 29  ? 35.692  -24.094 -13.923 1.00 41.39  ?  29   GLU B HB3    1 
ATOM   7607  H HG2    . GLU B 2 29  ? 34.858  -23.909 -11.257 1.00 51.76  ?  29   GLU B HG2    1 
ATOM   7608  H HG3    . GLU B 2 29  ? 35.235  -25.308 -11.910 1.00 51.76  ?  29   GLU B HG3    1 
ATOM   7609  N N      . ALA B 2 30  ? 33.462  -21.479 -15.252 1.00 21.56  ?  30   ALA B N      1 
ATOM   7610  C CA     . ALA B 2 30  ? 33.206  -21.023 -16.608 1.00 19.88  ?  30   ALA B CA     1 
ATOM   7611  C C      . ALA B 2 30  ? 32.896  -19.531 -16.575 1.00 17.60  ?  30   ALA B C      1 
ATOM   7612  O O      . ALA B 2 30  ? 32.284  -19.043 -15.621 1.00 19.61  ?  30   ALA B O      1 
ATOM   7613  C CB     . ALA B 2 30  ? 32.013  -21.755 -17.246 1.00 20.27  ?  30   ALA B CB     1 
ATOM   7614  H H      . ALA B 2 30  ? 32.778  -21.423 -14.734 1.00 25.87  ?  30   ALA B H      1 
ATOM   7615  H HA     . ALA B 2 30  ? 33.985  -21.192 -17.160 1.00 23.85  ?  30   ALA B HA     1 
ATOM   7616  H HB1    . ALA B 2 30  ? 31.904  -21.446 -18.159 1.00 24.32  ?  30   ALA B HB1    1 
ATOM   7617  H HB2    . ALA B 2 30  ? 32.187  -22.709 -17.238 1.00 24.32  ?  30   ALA B HB2    1 
ATOM   7618  H HB3    . ALA B 2 30  ? 31.213  -21.561 -16.733 1.00 24.32  ?  30   ALA B HB3    1 
ATOM   7619  N N      . PRO B 2 31  ? 33.288  -18.790 -17.599 1.00 17.38  ?  31   PRO B N      1 
ATOM   7620  C CA     . PRO B 2 31  ? 33.089  -17.342 -17.575 1.00 17.49  ?  31   PRO B CA     1 
ATOM   7621  C C      . PRO B 2 31  ? 31.645  -16.938 -17.805 1.00 17.29  ?  31   PRO B C      1 
ATOM   7622  O O      . PRO B 2 31  ? 30.859  -17.638 -18.443 1.00 19.43  ?  31   PRO B O      1 
ATOM   7623  C CB     . PRO B 2 31  ? 33.955  -16.853 -18.736 1.00 20.03  ?  31   PRO B CB     1 
ATOM   7624  C CG     . PRO B 2 31  ? 33.947  -17.979 -19.687 1.00 20.12  ?  31   PRO B CG     1 
ATOM   7625  C CD     . PRO B 2 31  ? 33.934  -19.236 -18.850 1.00 19.70  ?  31   PRO B CD     1 
ATOM   7626  H HA     . PRO B 2 31  ? 33.397  -16.984 -16.727 1.00 20.99  ?  31   PRO B HA     1 
ATOM   7627  H HB2    . PRO B 2 31  ? 33.566  -16.058 -19.131 1.00 24.03  ?  31   PRO B HB2    1 
ATOM   7628  H HB3    . PRO B 2 31  ? 34.854  -16.663 -18.426 1.00 24.03  ?  31   PRO B HB3    1 
ATOM   7629  H HG2    . PRO B 2 31  ? 33.153  -17.930 -20.243 1.00 24.14  ?  31   PRO B HG2    1 
ATOM   7630  H HG3    . PRO B 2 31  ? 34.742  -17.944 -20.240 1.00 24.14  ?  31   PRO B HG3    1 
ATOM   7631  H HD2    . PRO B 2 31  ? 33.415  -19.934 -19.280 1.00 23.64  ?  31   PRO B HD2    1 
ATOM   7632  H HD3    . PRO B 2 31  ? 34.837  -19.550 -18.682 1.00 23.64  ?  31   PRO B HD3    1 
ATOM   7633  N N      . GLY B 2 32  ? 31.326  -15.739 -17.307 1.00 17.12  ?  32   GLY B N      1 
ATOM   7634  C CA     . GLY B 2 32  ? 30.111  -15.047 -17.656 1.00 17.53  ?  32   GLY B CA     1 
ATOM   7635  C C      . GLY B 2 32  ? 30.419  -13.692 -18.271 1.00 16.52  ?  32   GLY B C      1 
ATOM   7636  O O      . GLY B 2 32  ? 31.573  -13.242 -18.317 1.00 17.13  ?  32   GLY B O      1 
ATOM   7637  H H      . GLY B 2 32  ? 31.820  -15.306 -16.751 1.00 20.54  ?  32   GLY B H      1 
ATOM   7638  H HA2    . GLY B 2 32  ? 29.606  -15.573 -18.296 1.00 21.03  ?  32   GLY B HA2    1 
ATOM   7639  H HA3    . GLY B 2 32  ? 29.570  -14.913 -16.862 1.00 21.03  ?  32   GLY B HA3    1 
ATOM   7640  N N      . ARG B 2 33  ? 29.358  -13.034 -18.751 1.00 14.39  ?  33   ARG B N      1 
ATOM   7641  C CA     . ARG B 2 33  ? 29.501  -11.645 -19.172 1.00 14.93  ?  33   ARG B CA     1 
ATOM   7642  C C      . ARG B 2 33  ? 28.143  -10.960 -19.106 1.00 14.95  ?  33   ARG B C      1 
ATOM   7643  O O      . ARG B 2 33  ? 27.160  -11.471 -19.646 1.00 15.45  ?  33   ARG B O      1 
ATOM   7644  C CB     . ARG B 2 33  ? 30.073  -11.547 -20.586 1.00 16.63  ?  33   ARG B CB     1 
ATOM   7645  C CG     . ARG B 2 33  ? 30.460  -10.121 -20.987 1.00 17.25  ?  33   ARG B CG     1 
ATOM   7646  C CD     . ARG B 2 33  ? 31.127  -10.003 -22.355 1.00 18.55  ?  33   ARG B CD     1 
ATOM   7647  N NE     . ARG B 2 33  ? 32.318  -10.844 -22.480 1.00 18.87  ?  33   ARG B NE     1 
ATOM   7648  C CZ     . ARG B 2 33  ? 33.527  -10.523 -22.032 1.00 22.33  ?  33   ARG B CZ     1 
ATOM   7649  N NH1    . ARG B 2 33  ? 33.764  -9.336  -21.434 1.00 23.21  ?  33   ARG B NH1    1 
ATOM   7650  N NH2    . ARG B 2 33  ? 34.520  -11.388 -22.204 1.00 23.69  ?  33   ARG B NH2    1 
ATOM   7651  H H      . ARG B 2 33  ? 28.569  -13.364 -18.837 1.00 17.27  ?  33   ARG B H      1 
ATOM   7652  H HA     . ARG B 2 33  ? 30.105  -11.191 -18.564 1.00 17.91  ?  33   ARG B HA     1 
ATOM   7653  H HB2    . ARG B 2 33  ? 30.869  -12.098 -20.640 1.00 19.95  ?  33   ARG B HB2    1 
ATOM   7654  H HB3    . ARG B 2 33  ? 29.407  -11.864 -21.216 1.00 19.95  ?  33   ARG B HB3    1 
ATOM   7655  H HG2    . ARG B 2 33  ? 29.657  -9.577  -21.007 1.00 20.70  ?  33   ARG B HG2    1 
ATOM   7656  H HG3    . ARG B 2 33  ? 31.080  -9.772  -20.328 1.00 20.70  ?  33   ARG B HG3    1 
ATOM   7657  H HD2    . ARG B 2 33  ? 30.496  -10.274 -23.039 1.00 22.26  ?  33   ARG B HD2    1 
ATOM   7658  H HD3    . ARG B 2 33  ? 31.396  -9.082  -22.497 1.00 22.26  ?  33   ARG B HD3    1 
ATOM   7659  H HE     . ARG B 2 33  ? 32.228  -11.603 -22.873 1.00 22.64  ?  33   ARG B HE     1 
ATOM   7660  H HH11   . ARG B 2 33  ? 33.125  -8.769  -21.337 1.00 27.84  ?  33   ARG B HH11   1 
ATOM   7661  H HH12   . ARG B 2 33  ? 34.553  -9.147  -21.151 1.00 27.84  ?  33   ARG B HH12   1 
ATOM   7662  H HH21   . ARG B 2 33  ? 34.374  -12.137 -22.599 1.00 28.42  ?  33   ARG B HH21   1 
ATOM   7663  H HH22   . ARG B 2 33  ? 35.309  -11.197 -21.920 1.00 28.42  ?  33   ARG B HH22   1 
ATOM   7664  N N      . VAL B 2 34  ? 28.089  -9.814  -18.442 1.00 15.05  ?  34   VAL B N      1 
ATOM   7665  C CA     . VAL B 2 34  ? 26.866  -9.026  -18.338 1.00 15.14  ?  34   VAL B CA     1 
ATOM   7666  C C      . VAL B 2 34  ? 26.915  -7.945  -19.404 1.00 15.42  ?  34   VAL B C      1 
ATOM   7667  O O      . VAL B 2 34  ? 27.780  -7.059  -19.356 1.00 16.40  ?  34   VAL B O      1 
ATOM   7668  C CB     . VAL B 2 34  ? 26.744  -8.375  -16.953 1.00 16.44  ?  34   VAL B CB     1 
ATOM   7669  C CG1    . VAL B 2 34  ? 25.456  -7.538  -16.879 1.00 18.36  ?  34   VAL B CG1    1 
ATOM   7670  C CG2    . VAL B 2 34  ? 26.788  -9.405  -15.863 1.00 16.15  ?  34   VAL B CG2    1 
ATOM   7671  H H      . VAL B 2 34  ? 28.762  -9.466  -18.034 1.00 18.05  ?  34   VAL B H      1 
ATOM   7672  H HA     . VAL B 2 34  ? 26.102  -9.602  -18.497 1.00 18.17  ?  34   VAL B HA     1 
ATOM   7673  H HB     . VAL B 2 34  ? 27.500  -7.784  -16.813 1.00 19.72  ?  34   VAL B HB     1 
ATOM   7674  H HG11   . VAL B 2 34  ? 25.261  -7.341  -15.949 1.00 22.02  ?  34   VAL B HG11   1 
ATOM   7675  H HG12   . VAL B 2 34  ? 25.587  -6.713  -17.372 1.00 22.02  ?  34   VAL B HG12   1 
ATOM   7676  H HG13   . VAL B 2 34  ? 24.727  -8.045  -17.270 1.00 22.02  ?  34   VAL B HG13   1 
ATOM   7677  H HG21   . VAL B 2 34  ? 26.660  -8.966  -15.008 1.00 19.37  ?  34   VAL B HG21   1 
ATOM   7678  H HG22   . VAL B 2 34  ? 26.080  -10.052 -16.011 1.00 19.37  ?  34   VAL B HG22   1 
ATOM   7679  H HG23   . VAL B 2 34  ? 27.650  -9.848  -15.882 1.00 19.37  ?  34   VAL B HG23   1 
ATOM   7680  N N      A MET B 2 35  ? 26.011  -8.017  -20.381 0.65 17.05  ?  35   MET B N      1 
ATOM   7681  N N      B MET B 2 35  ? 25.998  -8.009  -20.368 0.35 16.30  ?  35   MET B N      1 
ATOM   7682  C CA     A MET B 2 35  ? 25.921  -6.974  -21.395 0.65 17.26  ?  35   MET B CA     1 
ATOM   7683  C CA     B MET B 2 35  ? 25.905  -6.982  -21.399 0.35 16.10  ?  35   MET B CA     1 
ATOM   7684  C C      A MET B 2 35  ? 25.006  -5.860  -20.905 0.65 16.05  ?  35   MET B C      1 
ATOM   7685  C C      B MET B 2 35  ? 24.995  -5.860  -20.916 0.35 16.03  ?  35   MET B C      1 
ATOM   7686  O O      A MET B 2 35  ? 23.987  -6.113  -20.256 0.65 17.78  ?  35   MET B O      1 
ATOM   7687  O O      B MET B 2 35  ? 23.955  -6.110  -20.300 0.35 17.05  ?  35   MET B O      1 
ATOM   7688  C CB     A MET B 2 35  ? 25.415  -7.556  -22.710 0.65 18.21  ?  35   MET B CB     1 
ATOM   7689  C CB     B MET B 2 35  ? 25.361  -7.586  -22.690 0.35 15.72  ?  35   MET B CB     1 
ATOM   7690  C CG     A MET B 2 35  ? 26.413  -8.493  -23.349 0.65 19.82  ?  35   MET B CG     1 
ATOM   7691  C CG     B MET B 2 35  ? 26.100  -8.839  -23.118 0.35 15.90  ?  35   MET B CG     1 
ATOM   7692  S SD     A MET B 2 35  ? 27.974  -7.688  -23.760 0.65 22.18  ?  35   MET B SD     1 
ATOM   7693  S SD     B MET B 2 35  ? 27.882  -8.601  -23.248 0.35 16.01  ?  35   MET B SD     1 
ATOM   7694  C CE     A MET B 2 35  ? 28.499  -8.747  -25.086 0.65 20.40  ?  35   MET B CE     1 
ATOM   7695  C CE     B MET B 2 35  ? 27.969  -7.228  -24.402 0.35 16.89  ?  35   MET B CE     1 
ATOM   7696  H H      A MET B 2 35  ? 25.444  -8.657  -20.475 0.65 20.46  ?  35   MET B H      1 
ATOM   7697  H H      B MET B 2 35  ? 25.419  -8.640  -20.445 0.35 19.55  ?  35   MET B H      1 
ATOM   7698  H HA     A MET B 2 35  ? 26.799  -6.600  -21.566 0.65 20.71  ?  35   MET B HA     1 
ATOM   7699  H HA     B MET B 2 35  ? 26.784  -6.618  -21.588 0.35 19.31  ?  35   MET B HA     1 
ATOM   7700  H HB2    A MET B 2 35  ? 24.599  -8.054  -22.543 0.65 21.85  ?  35   MET B HB2    1 
ATOM   7701  H HB2    B MET B 2 35  ? 24.428  -7.819  -22.559 0.35 18.86  ?  35   MET B HB2    1 
ATOM   7702  H HB3    A MET B 2 35  ? 25.240  -6.832  -23.331 0.65 21.85  ?  35   MET B HB3    1 
ATOM   7703  H HB3    B MET B 2 35  ? 25.443  -6.932  -23.402 0.35 18.86  ?  35   MET B HB3    1 
ATOM   7704  H HG2    A MET B 2 35  ? 26.604  -9.218  -22.734 0.65 23.78  ?  35   MET B HG2    1 
ATOM   7705  H HG2    B MET B 2 35  ? 25.940  -9.538  -22.465 0.35 19.08  ?  35   MET B HG2    1 
ATOM   7706  H HG3    A MET B 2 35  ? 26.034  -8.845  -24.170 0.65 23.78  ?  35   MET B HG3    1 
ATOM   7707  H HG3    B MET B 2 35  ? 25.772  -9.116  -23.988 0.35 19.08  ?  35   MET B HG3    1 
ATOM   7708  H HE1    A MET B 2 35  ? 29.314  -8.391  -25.471 0.65 24.47  ?  35   MET B HE1    1 
ATOM   7709  H HE1    B MET B 2 35  ? 28.899  -7.053  -24.615 0.35 20.27  ?  35   MET B HE1    1 
ATOM   7710  H HE2    A MET B 2 35  ? 28.660  -9.637  -24.734 0.65 24.47  ?  35   MET B HE2    1 
ATOM   7711  H HE2    B MET B 2 35  ? 27.484  -7.462  -25.209 0.35 20.27  ?  35   MET B HE2    1 
ATOM   7712  H HE3    A MET B 2 35  ? 27.801  -8.780  -25.759 0.65 24.47  ?  35   MET B HE3    1 
ATOM   7713  H HE3    B MET B 2 35  ? 27.571  -6.445  -23.992 0.35 20.27  ?  35   MET B HE3    1 
ATOM   7714  N N      . ALA B 2 36  ? 25.402  -4.620  -21.185 1.00 16.91  ?  36   ALA B N      1 
ATOM   7715  C CA     . ALA B 2 36  ? 24.752  -3.460  -20.582 1.00 18.11  ?  36   ALA B CA     1 
ATOM   7716  C C      . ALA B 2 36  ? 24.367  -2.343  -21.535 1.00 18.73  ?  36   ALA B C      1 
ATOM   7717  O O      . ALA B 2 36  ? 23.511  -1.516  -21.178 1.00 19.96  ?  36   ALA B O      1 
ATOM   7718  C CB     . ALA B 2 36  ? 25.657  -2.878  -19.492 1.00 20.82  ?  36   ALA B CB     1 
ATOM   7719  H H      A ALA B 2 36  ? 26.045  -4.425  -21.723 0.65 20.29  ?  36   ALA B H      1 
ATOM   7720  H H      B ALA B 2 36  ? 26.052  -4.426  -21.714 0.35 20.29  ?  36   ALA B H      1 
ATOM   7721  H HA     . ALA B 2 36  ? 23.923  -3.762  -20.180 1.00 21.73  ?  36   ALA B HA     1 
ATOM   7722  H HB1    . ALA B 2 36  ? 25.232  -2.093  -19.113 1.00 24.98  ?  36   ALA B HB1    1 
ATOM   7723  H HB2    . ALA B 2 36  ? 25.791  -3.547  -18.802 1.00 24.98  ?  36   ALA B HB2    1 
ATOM   7724  H HB3    . ALA B 2 36  ? 26.510  -2.634  -19.886 1.00 24.98  ?  36   ALA B HB3    1 
ATOM   7725  N N      . GLY B 2 37  ? 24.941  -2.291  -22.725 1.00 17.01  ?  37   GLY B N      1 
ATOM   7726  C CA     . GLY B 2 37  ? 24.609  -1.202  -23.626 1.00 16.42  ?  37   GLY B CA     1 
ATOM   7727  C C      . GLY B 2 37  ? 25.009  -1.572  -25.035 1.00 16.96  ?  37   GLY B C      1 
ATOM   7728  O O      . GLY B 2 37  ? 25.475  -2.685  -25.312 1.00 17.11  ?  37   GLY B O      1 
ATOM   7729  H H      . GLY B 2 37  ? 25.511  -2.859  -23.028 1.00 20.41  ?  37   GLY B H      1 
ATOM   7730  H HA2    . GLY B 2 37  ? 23.655  -1.029  -23.602 1.00 19.70  ?  37   GLY B HA2    1 
ATOM   7731  H HA3    . GLY B 2 37  ? 25.083  -0.397  -23.363 1.00 19.70  ?  37   GLY B HA3    1 
ATOM   7732  N N      . GLY B 2 38  ? 24.824  -0.610  -25.931 1.00 16.50  ?  38   GLY B N      1 
ATOM   7733  C CA     . GLY B 2 38  ? 25.201  -0.814  -27.315 1.00 16.95  ?  38   GLY B CA     1 
ATOM   7734  C C      . GLY B 2 38  ? 24.574  0.196   -28.251 1.00 18.05  ?  38   GLY B C      1 
ATOM   7735  O O      . GLY B 2 38  ? 23.494  0.723   -27.973 1.00 18.16  ?  38   GLY B O      1 
ATOM   7736  H H      . GLY B 2 38  ? 24.484  0.161   -25.761 1.00 19.80  ?  38   GLY B H      1 
ATOM   7737  H HA2    . GLY B 2 38  ? 26.166  -0.745  -27.396 1.00 20.34  ?  38   GLY B HA2    1 
ATOM   7738  H HA3    . GLY B 2 38  ? 24.924  -1.700  -27.594 1.00 20.34  ?  38   GLY B HA3    1 
ATOM   7739  N N      . GLU B 2 39  ? 25.251  0.459   -29.362 1.00 18.27  ?  39   GLU B N      1 
ATOM   7740  C CA     . GLU B 2 39  ? 24.747  1.360   -30.388 1.00 19.79  ?  39   GLU B CA     1 
ATOM   7741  C C      . GLU B 2 39  ? 25.310  0.904   -31.722 1.00 18.30  ?  39   GLU B C      1 
ATOM   7742  O O      . GLU B 2 39  ? 26.492  0.572   -31.821 1.00 19.15  ?  39   GLU B O      1 
ATOM   7743  C CB     . GLU B 2 39  ? 25.175  2.807   -30.096 1.00 25.07  ?  39   GLU B CB     1 
ATOM   7744  C CG     . GLU B 2 39  ? 24.539  3.831   -31.006 1.00 32.87  ?  39   GLU B CG     1 
ATOM   7745  C CD     . GLU B 2 39  ? 25.224  3.926   -32.365 1.00 41.24  ?  39   GLU B CD     1 
ATOM   7746  O OE1    . GLU B 2 39  ? 24.561  4.330   -33.357 1.00 44.44  ?  39   GLU B OE1    1 
ATOM   7747  O OE2    . GLU B 2 39  ? 26.433  3.584   -32.448 1.00 42.19  -1 39   GLU B OE2    1 
ATOM   7748  H H      . GLU B 2 39  ? 26.020  0.121   -29.548 1.00 21.92  ?  39   GLU B H      1 
ATOM   7749  H HA     . GLU B 2 39  ? 23.778  1.330   -30.429 1.00 23.74  ?  39   GLU B HA     1 
ATOM   7750  H HB2    . GLU B 2 39  ? 24.926  3.027   -29.185 1.00 30.08  ?  39   GLU B HB2    1 
ATOM   7751  H HB3    . GLU B 2 39  ? 26.137  2.874   -30.203 1.00 30.08  ?  39   GLU B HB3    1 
ATOM   7752  H HG2    . GLU B 2 39  ? 23.612  3.588   -31.155 1.00 39.44  ?  39   GLU B HG2    1 
ATOM   7753  H HG3    . GLU B 2 39  ? 24.590  4.703   -30.584 1.00 39.44  ?  39   GLU B HG3    1 
ATOM   7754  N N      . GLY B 2 40  ? 24.464  0.885   -32.747 1.00 19.10  ?  40   GLY B N      1 
ATOM   7755  C CA     . GLY B 2 40  ? 24.938  0.528   -34.068 1.00 17.13  ?  40   GLY B CA     1 
ATOM   7756  C C      . GLY B 2 40  ? 25.382  -0.914  -34.118 1.00 16.21  ?  40   GLY B C      1 
ATOM   7757  O O      . GLY B 2 40  ? 24.600  -1.815  -33.790 1.00 16.57  ?  40   GLY B O      1 
ATOM   7758  H H      . GLY B 2 40  ? 23.626  1.073   -32.699 1.00 22.92  ?  40   GLY B H      1 
ATOM   7759  H HA2    . GLY B 2 40  ? 24.227  0.657   -34.715 1.00 20.55  ?  40   GLY B HA2    1 
ATOM   7760  H HA3    . GLY B 2 40  ? 25.689  1.093   -34.308 1.00 20.55  ?  40   GLY B HA3    1 
ATOM   7761  N N      . ILE B 2 41  ? 26.642  -1.153  -34.516 1.00 17.83  ?  41   ILE B N      1 
ATOM   7762  C CA     . ILE B 2 41  ? 27.165  -2.519  -34.560 1.00 17.89  ?  41   ILE B CA     1 
ATOM   7763  C C      . ILE B 2 41  ? 27.900  -2.896  -33.286 1.00 17.53  ?  41   ILE B C      1 
ATOM   7764  O O      . ILE B 2 41  ? 28.472  -3.996  -33.210 1.00 17.40  ?  41   ILE B O      1 
ATOM   7765  C CB     . ILE B 2 41  ? 28.048  -2.766  -35.808 1.00 18.89  ?  41   ILE B CB     1 
ATOM   7766  C CG1    . ILE B 2 41  ? 29.367  -1.993  -35.732 1.00 20.08  ?  41   ILE B CG1    1 
ATOM   7767  C CG2    . ILE B 2 41  ? 27.249  -2.446  -37.071 1.00 19.55  ?  41   ILE B CG2    1 
ATOM   7768  C CD1    . ILE B 2 41  ? 30.334  -2.337  -36.869 1.00 23.22  ?  41   ILE B CD1    1 
ATOM   7769  H H      . ILE B 2 41  ? 27.202  -0.548  -34.761 1.00 21.39  ?  41   ILE B H      1 
ATOM   7770  H HA     . ILE B 2 41  ? 26.406  -3.117  -34.641 1.00 21.47  ?  41   ILE B HA     1 
ATOM   7771  H HB     . ILE B 2 41  ? 28.295  -3.704  -35.836 1.00 22.67  ?  41   ILE B HB     1 
ATOM   7772  H HG12   . ILE B 2 41  ? 29.178  -1.043  -35.779 1.00 24.09  ?  41   ILE B HG12   1 
ATOM   7773  H HG13   . ILE B 2 41  ? 29.806  -2.203  -34.893 1.00 24.09  ?  41   ILE B HG13   1 
ATOM   7774  H HG21   . ILE B 2 41  ? 27.741  -2.763  -37.845 1.00 23.46  ?  41   ILE B HG21   1 
ATOM   7775  H HG22   . ILE B 2 41  ? 26.388  -2.890  -37.021 1.00 23.46  ?  41   ILE B HG22   1 
ATOM   7776  H HG23   . ILE B 2 41  ? 27.123  -1.486  -37.130 1.00 23.46  ?  41   ILE B HG23   1 
ATOM   7777  H HD11   . ILE B 2 41  ? 31.149  -1.824  -36.756 1.00 27.86  ?  41   ILE B HD11   1 
ATOM   7778  H HD12   . ILE B 2 41  ? 30.534  -3.286  -36.837 1.00 27.86  ?  41   ILE B HD12   1 
ATOM   7779  H HD13   . ILE B 2 41  ? 29.917  -2.115  -37.716 1.00 27.86  ?  41   ILE B HD13   1 
ATOM   7780  N N      . HIS B 2 42  ? 27.911  -2.024  -32.282 1.00 17.95  ?  42   HIS B N      1 
ATOM   7781  C CA     . HIS B 2 42  ? 28.687  -2.256  -31.074 1.00 18.34  ?  42   HIS B CA     1 
ATOM   7782  C C      . HIS B 2 42  ? 27.798  -2.654  -29.898 1.00 17.48  ?  42   HIS B C      1 
ATOM   7783  O O      . HIS B 2 42  ? 26.682  -2.148  -29.746 1.00 18.29  ?  42   HIS B O      1 
ATOM   7784  C CB     . HIS B 2 42  ? 29.485  -1.006  -30.681 1.00 20.03  ?  42   HIS B CB     1 
ATOM   7785  C CG     . HIS B 2 42  ? 30.434  -0.535  -31.736 1.00 22.86  ?  42   HIS B CG     1 
ATOM   7786  N ND1    . HIS B 2 42  ? 31.731  -0.988  -31.828 1.00 27.22  ?  42   HIS B ND1    1 
ATOM   7787  C CD2    . HIS B 2 42  ? 30.272  0.343   -32.753 1.00 24.23  ?  42   HIS B CD2    1 
ATOM   7788  C CE1    . HIS B 2 42  ? 32.330  -0.405  -32.851 1.00 25.82  ?  42   HIS B CE1    1 
ATOM   7789  N NE2    . HIS B 2 42  ? 31.461  0.393   -33.441 1.00 26.92  ?  42   HIS B NE2    1 
ATOM   7790  H H      . HIS B 2 42  ? 27.471  -1.285  -32.281 1.00 21.54  ?  42   HIS B H      1 
ATOM   7791  H HA     . HIS B 2 42  ? 29.296  -2.991  -31.250 1.00 22.00  ?  42   HIS B HA     1 
ATOM   7792  H HB2    . HIS B 2 42  ? 28.862  -0.284  -30.500 1.00 24.03  ?  42   HIS B HB2    1 
ATOM   7793  H HB3    . HIS B 2 42  ? 30.003  -1.204  -29.885 1.00 24.03  ?  42   HIS B HB3    1 
ATOM   7794  H HD1    . HIS B 2 42  ? 32.094  -1.562  -31.301 1.00 32.66  ?  42   HIS B HD1    1 
ATOM   7795  H HD2    . HIS B 2 42  ? 29.500  0.824   -32.949 1.00 29.08  ?  42   HIS B HD2    1 
ATOM   7796  H HE1    . HIS B 2 42  ? 33.214  -0.536  -33.111 1.00 30.98  ?  42   HIS B HE1    1 
ATOM   7797  N N      A VAL B 2 43  ? 28.301  -3.581  -29.090 0.36 17.84  ?  43   VAL B N      1 
ATOM   7798  N N      B VAL B 2 43  ? 28.314  -3.555  -29.060 0.64 18.18  ?  43   VAL B N      1 
ATOM   7799  C CA     A VAL B 2 43  ? 27.718  -3.906  -27.797 0.36 17.82  ?  43   VAL B CA     1 
ATOM   7800  C CA     B VAL B 2 43  ? 27.680  -3.937  -27.799 0.64 18.13  ?  43   VAL B CA     1 
ATOM   7801  C C      A VAL B 2 43  ? 28.731  -3.535  -26.725 0.36 18.01  ?  43   VAL B C      1 
ATOM   7802  C C      B VAL B 2 43  ? 28.708  -3.810  -26.677 0.64 17.14  ?  43   VAL B C      1 
ATOM   7803  O O      A VAL B 2 43  ? 29.925  -3.369  -26.992 0.36 17.38  ?  43   VAL B O      1 
ATOM   7804  O O      B VAL B 2 43  ? 29.898  -4.084  -26.882 0.64 16.73  ?  43   VAL B O      1 
ATOM   7805  C CB     A VAL B 2 43  ? 27.310  -5.386  -27.683 0.36 18.30  ?  43   VAL B CB     1 
ATOM   7806  C CB     B VAL B 2 43  ? 27.068  -5.355  -27.874 0.64 20.50  ?  43   VAL B CB     1 
ATOM   7807  C CG1    A VAL B 2 43  ? 26.175  -5.675  -28.635 0.36 17.87  ?  43   VAL B CG1    1 
ATOM   7808  C CG1    B VAL B 2 43  ? 28.143  -6.440  -27.922 0.64 20.49  ?  43   VAL B CG1    1 
ATOM   7809  C CG2    A VAL B 2 43  ? 28.490  -6.302  -27.963 0.36 19.26  ?  43   VAL B CG2    1 
ATOM   7810  C CG2    B VAL B 2 43  ? 26.103  -5.601  -26.703 0.64 22.63  ?  43   VAL B CG2    1 
ATOM   7811  H H      A VAL B 2 43  ? 28.999  -4.047  -29.277 0.36 21.41  ?  43   VAL B H      1 
ATOM   7812  H H      B VAL B 2 43  ? 29.053  -3.969  -29.208 0.64 21.82  ?  43   VAL B H      1 
ATOM   7813  H HA     A VAL B 2 43  ? 26.916  -3.377  -27.664 0.36 21.38  ?  43   VAL B HA     1 
ATOM   7814  H HA     B VAL B 2 43  ? 26.957  -3.324  -27.595 0.64 21.76  ?  43   VAL B HA     1 
ATOM   7815  H HB     A VAL B 2 43  ? 27.014  -5.563  -26.776 0.36 21.96  ?  43   VAL B HB     1 
ATOM   7816  H HB     B VAL B 2 43  ? 26.565  -5.411  -28.701 0.64 24.60  ?  43   VAL B HB     1 
ATOM   7817  H HG11   A VAL B 2 43  ? 25.921  -6.608  -28.549 0.36 21.45  ?  43   VAL B HG11   1 
ATOM   7818  H HG11   B VAL B 2 43  ? 27.730  -7.282  -28.170 0.64 24.59  ?  43   VAL B HG11   1 
ATOM   7819  H HG12   A VAL B 2 43  ? 25.423  -5.105  -28.412 0.36 21.45  ?  43   VAL B HG12   1 
ATOM   7820  H HG12   B VAL B 2 43  ? 28.812  -6.193  -28.579 0.64 24.59  ?  43   VAL B HG12   1 
ATOM   7821  H HG13   A VAL B 2 43  ? 26.469  -5.495  -29.541 0.36 21.45  ?  43   VAL B HG13   1 
ATOM   7822  H HG13   B VAL B 2 43  ? 28.552  -6.517  -27.046 0.64 24.59  ?  43   VAL B HG13   1 
ATOM   7823  H HG21   A VAL B 2 43  ? 28.193  -7.224  -27.909 0.36 23.10  ?  43   VAL B HG21   1 
ATOM   7824  H HG21   B VAL B 2 43  ? 25.848  -6.537  -26.696 0.64 27.16  ?  43   VAL B HG21   1 
ATOM   7825  H HG22   A VAL B 2 43  ? 28.830  -6.115  -28.851 0.36 23.10  ?  43   VAL B HG22   1 
ATOM   7826  H HG22   B VAL B 2 43  ? 26.550  -5.374  -25.873 0.64 27.16  ?  43   VAL B HG22   1 
ATOM   7827  H HG23   A VAL B 2 43  ? 29.181  -6.138  -27.302 0.36 23.10  ?  43   VAL B HG23   1 
ATOM   7828  H HG23   B VAL B 2 43  ? 25.317  -5.044  -26.819 0.64 27.16  ?  43   VAL B HG23   1 
ATOM   7829  N N      . VAL B 2 44  ? 28.242  -3.397  -25.495 1.00 19.03  ?  44   VAL B N      1 
ATOM   7830  C CA     . VAL B 2 44  ? 29.092  -2.968  -24.388 1.00 17.13  ?  44   VAL B CA     1 
ATOM   7831  C C      . VAL B 2 44  ? 28.737  -3.758  -23.141 1.00 16.98  ?  44   VAL B C      1 
ATOM   7832  O O      . VAL B 2 44  ? 27.558  -3.881  -22.802 1.00 16.42  ?  44   VAL B O      1 
ATOM   7833  C CB     . VAL B 2 44  ? 28.925  -1.461  -24.117 1.00 20.66  ?  44   VAL B CB     1 
ATOM   7834  C CG1    . VAL B 2 44  ? 29.920  -1.005  -23.080 1.00 21.22  ?  44   VAL B CG1    1 
ATOM   7835  C CG2    . VAL B 2 44  ? 29.067  -0.662  -25.428 1.00 22.16  ?  44   VAL B CG2    1 
ATOM   7836  H H      A VAL B 2 44  ? 27.423  -3.546  -25.279 0.36 22.83  ?  44   VAL B H      1 
ATOM   7837  H H      B VAL B 2 44  ? 27.404  -3.356  -25.308 0.64 22.83  ?  44   VAL B H      1 
ATOM   7838  H HA     . VAL B 2 44  ? 30.017  -3.162  -24.607 1.00 20.55  ?  44   VAL B HA     1 
ATOM   7839  H HB     . VAL B 2 44  ? 28.036  -1.291  -23.767 1.00 24.78  ?  44   VAL B HB     1 
ATOM   7840  H HG11   . VAL B 2 44  ? 29.896  -0.037  -23.024 1.00 25.46  ?  44   VAL B HG11   1 
ATOM   7841  H HG12   . VAL B 2 44  ? 29.683  -1.393  -22.223 1.00 25.46  ?  44   VAL B HG12   1 
ATOM   7842  H HG13   . VAL B 2 44  ? 30.807  -1.299  -23.342 1.00 25.46  ?  44   VAL B HG13   1 
ATOM   7843  H HG21   . VAL B 2 44  ? 29.029  0.286   -25.226 1.00 26.59  ?  44   VAL B HG21   1 
ATOM   7844  H HG22   . VAL B 2 44  ? 29.918  -0.878  -25.840 1.00 26.59  ?  44   VAL B HG22   1 
ATOM   7845  H HG23   . VAL B 2 44  ? 28.341  -0.902  -26.025 1.00 26.59  ?  44   VAL B HG23   1 
ATOM   7846  N N      . ASP B 2 45  ? 29.761  -4.262  -22.439 1.00 16.60  ?  45   ASP B N      1 
ATOM   7847  C CA     . ASP B 2 45  ? 29.548  -5.006  -21.205 1.00 16.62  ?  45   ASP B CA     1 
ATOM   7848  C C      . ASP B 2 45  ? 29.530  -4.070  -19.989 1.00 17.34  ?  45   ASP B C      1 
ATOM   7849  O O      . ASP B 2 45  ? 29.660  -2.845  -20.101 1.00 17.97  ?  45   ASP B O      1 
ATOM   7850  C CB     . ASP B 2 45  ? 30.514  -6.193  -21.081 1.00 15.92  ?  45   ASP B CB     1 
ATOM   7851  C CG     . ASP B 2 45  ? 31.916  -5.804  -20.660 1.00 18.23  ?  45   ASP B CG     1 
ATOM   7852  O OD1    . ASP B 2 45  ? 32.150  -4.639  -20.283 1.00 20.19  ?  45   ASP B OD1    1 
ATOM   7853  O OD2    . ASP B 2 45  ? 32.811  -6.692  -20.720 1.00 18.14  -1 45   ASP B OD2    1 
ATOM   7854  H H      . ASP B 2 45  ? 30.587  -4.182  -22.664 1.00 19.91  ?  45   ASP B H      1 
ATOM   7855  H HA     . ASP B 2 45  ? 28.664  -5.404  -21.239 1.00 19.94  ?  45   ASP B HA     1 
ATOM   7856  H HB2    . ASP B 2 45  ? 30.167  -6.810  -20.417 1.00 19.10  ?  45   ASP B HB2    1 
ATOM   7857  H HB3    . ASP B 2 45  ? 30.577  -6.635  -21.943 1.00 19.10  ?  45   ASP B HB3    1 
ATOM   7858  N N      . LYS B 2 46  ? 29.330  -4.667  -18.812 1.00 17.32  ?  46   LYS B N      1 
ATOM   7859  C CA     . LYS B 2 46  ? 29.167  -3.907  -17.582 1.00 20.37  ?  46   LYS B CA     1 
ATOM   7860  C C      . LYS B 2 46  ? 30.416  -3.130  -17.192 1.00 20.18  ?  46   LYS B C      1 
ATOM   7861  O O      . LYS B 2 46  ? 30.314  -2.167  -16.420 1.00 21.07  ?  46   LYS B O      1 
ATOM   7862  C CB     . LYS B 2 46  ? 28.777  -4.882  -16.459 1.00 21.12  ?  46   LYS B CB     1 
ATOM   7863  C CG     . LYS B 2 46  ? 28.557  -4.246  -15.107 1.00 26.00  ?  46   LYS B CG     1 
ATOM   7864  C CD     . LYS B 2 46  ? 27.298  -3.407  -15.064 1.00 29.93  ?  46   LYS B CD     1 
ATOM   7865  C CE     . LYS B 2 46  ? 27.063  -2.892  -13.656 1.00 33.78  ?  46   LYS B CE     1 
ATOM   7866  N NZ     . LYS B 2 46  ? 25.781  -2.153  -13.504 1.00 35.98  ?  46   LYS B NZ     1 
ATOM   7867  H H      . LYS B 2 46  ? 29.285  -5.518  -18.700 1.00 20.78  ?  46   LYS B H      1 
ATOM   7868  H HA     . LYS B 2 46  ? 28.460  -3.253  -17.699 1.00 24.44  ?  46   LYS B HA     1 
ATOM   7869  H HB2    . LYS B 2 46  ? 27.950  -5.323  -16.710 1.00 25.34  ?  46   LYS B HB2    1 
ATOM   7870  H HB3    . LYS B 2 46  ? 29.486  -5.536  -16.361 1.00 25.34  ?  46   LYS B HB3    1 
ATOM   7871  H HG2    . LYS B 2 46  ? 28.478  -4.943  -14.437 1.00 31.20  ?  46   LYS B HG2    1 
ATOM   7872  H HG3    . LYS B 2 46  ? 29.310  -3.671  -14.900 1.00 31.20  ?  46   LYS B HG3    1 
ATOM   7873  H HD2    . LYS B 2 46  ? 27.391  -2.649  -15.662 1.00 35.91  ?  46   LYS B HD2    1 
ATOM   7874  H HD3    . LYS B 2 46  ? 26.537  -3.947  -15.329 1.00 35.91  ?  46   LYS B HD3    1 
ATOM   7875  H HE2    . LYS B 2 46  ? 27.046  -3.645  -13.045 1.00 40.53  ?  46   LYS B HE2    1 
ATOM   7876  H HE3    . LYS B 2 46  ? 27.784  -2.288  -13.419 1.00 40.53  ?  46   LYS B HE3    1 
ATOM   7877  H HZ1    . LYS B 2 46  ? 25.676  -1.895  -12.659 1.00 43.18  ?  46   LYS B HZ1    1 
ATOM   7878  H HZ2    . LYS B 2 46  ? 25.780  -1.433  -14.028 1.00 43.18  ?  46   LYS B HZ2    1 
ATOM   7879  H HZ3    . LYS B 2 46  ? 25.098  -2.677  -13.732 1.00 43.18  ?  46   LYS B HZ3    1 
ATOM   7880  N N      . ASP B 2 47  ? 31.588  -3.527  -17.672 1.00 21.03  ?  47   ASP B N      1 
ATOM   7881  C CA     . ASP B 2 47  ? 32.810  -2.777  -17.414 1.00 20.88  ?  47   ASP B CA     1 
ATOM   7882  C C      . ASP B 2 47  ? 33.015  -1.635  -18.401 1.00 22.05  ?  47   ASP B C      1 
ATOM   7883  O O      . ASP B 2 47  ? 33.988  -0.886  -18.275 1.00 24.50  ?  47   ASP B O      1 
ATOM   7884  C CB     . ASP B 2 47  ? 34.025  -3.693  -17.510 1.00 21.78  ?  47   ASP B CB     1 
ATOM   7885  C CG     . ASP B 2 47  ? 34.136  -4.656  -16.350 1.00 21.88  ?  47   ASP B CG     1 
ATOM   7886  O OD1    . ASP B 2 47  ? 33.997  -4.219  -15.189 1.00 23.82  ?  47   ASP B OD1    1 
ATOM   7887  O OD2    . ASP B 2 47  ? 34.388  -5.863  -16.620 1.00 21.38  -1 47   ASP B OD2    1 
ATOM   7888  H H      . ASP B 2 47  ? 31.700  -4.231  -18.153 1.00 25.23  ?  47   ASP B H      1 
ATOM   7889  H HA     . ASP B 2 47  ? 32.756  -2.420  -16.514 1.00 25.05  ?  47   ASP B HA     1 
ATOM   7890  H HB2    . ASP B 2 47  ? 33.963  -4.215  -18.326 1.00 26.14  ?  47   ASP B HB2    1 
ATOM   7891  H HB3    . ASP B 2 47  ? 34.829  -3.150  -17.525 1.00 26.14  ?  47   ASP B HB3    1 
ATOM   7892  N N      . GLY B 2 48  ? 32.155  -1.519  -19.413 1.00 21.44  ?  48   GLY B N      1 
ATOM   7893  C CA     . GLY B 2 48  ? 32.359  -0.560  -20.475 1.00 21.72  ?  48   GLY B CA     1 
ATOM   7894  C C      . GLY B 2 48  ? 33.216  -1.057  -21.619 1.00 20.29  ?  48   GLY B C      1 
ATOM   7895  O O      . GLY B 2 48  ? 33.592  -0.261  -22.490 1.00 22.48  ?  48   GLY B O      1 
ATOM   7896  H H      . GLY B 2 48  ? 31.443  -1.993  -19.501 1.00 25.72  ?  48   GLY B H      1 
ATOM   7897  H HA2    . GLY B 2 48  ? 31.495  -0.310  -20.838 1.00 26.06  ?  48   GLY B HA2    1 
ATOM   7898  H HA3    . GLY B 2 48  ? 32.786  0.228   -20.104 1.00 26.06  ?  48   GLY B HA3    1 
ATOM   7899  N N      . ARG B 2 49  ? 33.555  -2.339  -21.634 1.00 20.35  ?  49   ARG B N      1 
ATOM   7900  C CA     . ARG B 2 49  ? 34.318  -2.893  -22.743 1.00 18.87  ?  49   ARG B CA     1 
ATOM   7901  C C      . ARG B 2 49  ? 33.405  -3.037  -23.958 1.00 19.25  ?  49   ARG B C      1 
ATOM   7902  O O      . ARG B 2 49  ? 32.310  -3.608  -23.866 1.00 19.91  ?  49   ARG B O      1 
ATOM   7903  C CB     . ARG B 2 49  ? 34.904  -4.251  -22.349 1.00 20.47  ?  49   ARG B CB     1 
ATOM   7904  C CG     . ARG B 2 49  ? 35.818  -4.847  -23.400 1.00 21.29  ?  49   ARG B CG     1 
ATOM   7905  C CD     . ARG B 2 49  ? 36.484  -6.134  -22.907 1.00 22.56  ?  49   ARG B CD     1 
ATOM   7906  N NE     . ARG B 2 49  ? 37.145  -6.855  -23.992 1.00 22.27  ?  49   ARG B NE     1 
ATOM   7907  C CZ     . ARG B 2 49  ? 37.558  -8.117  -23.933 1.00 25.16  ?  49   ARG B CZ     1 
ATOM   7908  N NH1    . ARG B 2 49  ? 37.390  -8.822  -22.823 1.00 24.81  ?  49   ARG B NH1    1 
ATOM   7909  N NH2    . ARG B 2 49  ? 38.132  -8.676  -24.990 1.00 27.48  ?  49   ARG B NH2    1 
ATOM   7910  H H      . ARG B 2 49  ? 33.357  -2.907  -21.020 1.00 24.42  ?  49   ARG B H      1 
ATOM   7911  H HA     . ARG B 2 49  ? 35.055  -2.305  -22.971 1.00 22.64  ?  49   ARG B HA     1 
ATOM   7912  H HB2    . ARG B 2 49  ? 35.419  -4.144  -21.535 1.00 24.56  ?  49   ARG B HB2    1 
ATOM   7913  H HB3    . ARG B 2 49  ? 34.176  -4.874  -22.202 1.00 24.56  ?  49   ARG B HB3    1 
ATOM   7914  H HG2    . ARG B 2 49  ? 35.300  -5.057  -24.193 1.00 25.55  ?  49   ARG B HG2    1 
ATOM   7915  H HG3    . ARG B 2 49  ? 36.515  -4.208  -23.618 1.00 25.55  ?  49   ARG B HG3    1 
ATOM   7916  H HD2    . ARG B 2 49  ? 37.151  -5.913  -22.238 1.00 27.07  ?  49   ARG B HD2    1 
ATOM   7917  H HD3    . ARG B 2 49  ? 35.809  -6.716  -22.522 1.00 27.07  ?  49   ARG B HD3    1 
ATOM   7918  H HE     . ARG B 2 49  ? 37.277  -6.430  -24.728 1.00 26.72  ?  49   ARG B HE     1 
ATOM   7919  H HH11   . ARG B 2 49  ? 37.012  -8.464  -22.139 1.00 29.77  ?  49   ARG B HH11   1 
ATOM   7920  H HH12   . ARG B 2 49  ? 37.659  -9.639  -22.788 1.00 29.77  ?  49   ARG B HH12   1 
ATOM   7921  H HH21   . ARG B 2 49  ? 38.235  -8.222  -25.713 1.00 32.98  ?  49   ARG B HH21   1 
ATOM   7922  H HH22   . ARG B 2 49  ? 38.400  -9.492  -24.953 1.00 32.98  ?  49   ARG B HH22   1 
ATOM   7923  N N      . GLU B 2 50  ? 33.861  -2.509  -25.090 1.00 20.90  ?  50   GLU B N      1 
ATOM   7924  C CA     . GLU B 2 50  ? 33.039  -2.353  -26.283 1.00 20.75  ?  50   GLU B CA     1 
ATOM   7925  C C      . GLU B 2 50  ? 33.499  -3.329  -27.354 1.00 18.88  ?  50   GLU B C      1 
ATOM   7926  O O      . GLU B 2 50  ? 34.691  -3.389  -27.680 1.00 21.29  ?  50   GLU B O      1 
ATOM   7927  C CB     . GLU B 2 50  ? 33.152  -0.926  -26.809 1.00 23.44  ?  50   GLU B CB     1 
ATOM   7928  C CG     . GLU B 2 50  ? 32.331  -0.657  -28.040 1.00 31.06  ?  50   GLU B CG     1 
ATOM   7929  C CD     . GLU B 2 50  ? 32.385  0.798   -28.458 1.00 36.95  ?  50   GLU B CD     1 
ATOM   7930  O OE1    . GLU B 2 50  ? 33.422  1.229   -28.993 1.00 37.32  ?  50   GLU B OE1    1 
ATOM   7931  O OE2    . GLU B 2 50  ? 31.385  1.513   -28.227 1.00 41.38  -1 50   GLU B OE2    1 
ATOM   7932  H H      . GLU B 2 50  ? 34.667  -2.227  -25.192 1.00 25.08  ?  50   GLU B H      1 
ATOM   7933  H HA     . GLU B 2 50  ? 32.113  -2.549  -26.071 1.00 24.90  ?  50   GLU B HA     1 
ATOM   7934  H HB2    . GLU B 2 50  ? 32.853  -0.316  -26.117 1.00 28.13  ?  50   GLU B HB2    1 
ATOM   7935  H HB3    . GLU B 2 50  ? 34.080  -0.750  -27.030 1.00 28.13  ?  50   GLU B HB3    1 
ATOM   7936  H HG2    . GLU B 2 50  ? 32.670  -1.194  -28.773 1.00 37.27  ?  50   GLU B HG2    1 
ATOM   7937  H HG3    . GLU B 2 50  ? 31.406  -0.886  -27.861 1.00 37.27  ?  50   GLU B HG3    1 
ATOM   7938  N N      . PHE B 2 51  ? 32.545  -4.069  -27.920 1.00 16.71  ?  51   PHE B N      1 
ATOM   7939  C CA     . PHE B 2 51  ? 32.820  -5.084  -28.926 1.00 17.41  ?  51   PHE B CA     1 
ATOM   7940  C C      . PHE B 2 51  ? 32.110  -4.726  -30.219 1.00 17.08  ?  51   PHE B C      1 
ATOM   7941  O O      . PHE B 2 51  ? 30.993  -4.208  -30.197 1.00 18.35  ?  51   PHE B O      1 
ATOM   7942  C CB     . PHE B 2 51  ? 32.256  -6.440  -28.467 1.00 18.56  ?  51   PHE B CB     1 
ATOM   7943  C CG     . PHE B 2 51  ? 32.862  -6.951  -27.214 1.00 18.05  ?  51   PHE B CG     1 
ATOM   7944  C CD1    . PHE B 2 51  ? 32.352  -6.584  -25.982 1.00 17.09  ?  51   PHE B CD1    1 
ATOM   7945  C CD2    . PHE B 2 51  ? 33.965  -7.782  -27.258 1.00 19.62  ?  51   PHE B CD2    1 
ATOM   7946  C CE1    . PHE B 2 51  ? 32.933  -7.043  -24.814 1.00 18.74  ?  51   PHE B CE1    1 
ATOM   7947  C CE2    . PHE B 2 51  ? 34.538  -8.240  -26.096 1.00 20.28  ?  51   PHE B CE2    1 
ATOM   7948  C CZ     . PHE B 2 51  ? 34.030  -7.862  -24.881 1.00 19.49  ?  51   PHE B CZ     1 
ATOM   7949  H H      . PHE B 2 51  ? 31.710  -3.995  -27.728 1.00 20.05  ?  51   PHE B H      1 
ATOM   7950  H HA     . PHE B 2 51  ? 33.777  -5.136  -29.078 1.00 20.89  ?  51   PHE B HA     1 
ATOM   7951  H HB2    . PHE B 2 51  ? 31.302  -6.345  -28.317 1.00 22.27  ?  51   PHE B HB2    1 
ATOM   7952  H HB3    . PHE B 2 51  ? 32.418  -7.096  -29.163 1.00 22.27  ?  51   PHE B HB3    1 
ATOM   7953  H HD1    . PHE B 2 51  ? 31.611  -6.024  -25.939 1.00 20.51  ?  51   PHE B HD1    1 
ATOM   7954  H HD2    . PHE B 2 51  ? 34.322  -8.034  -28.079 1.00 23.55  ?  51   PHE B HD2    1 
ATOM   7955  H HE1    . PHE B 2 51  ? 32.582  -6.798  -23.988 1.00 22.48  ?  51   PHE B HE1    1 
ATOM   7956  H HE2    . PHE B 2 51  ? 35.273  -8.808  -26.135 1.00 24.34  ?  51   PHE B HE2    1 
ATOM   7957  H HZ     . PHE B 2 51  ? 34.432  -8.163  -24.098 1.00 23.38  ?  51   PHE B HZ     1 
ATOM   7958  N N      . ILE B 2 52  ? 32.738  -5.022  -31.352 1.00 16.84  ?  52   ILE B N      1 
ATOM   7959  C CA     . ILE B 2 52  ? 31.990  -5.116  -32.601 1.00 17.18  ?  52   ILE B CA     1 
ATOM   7960  C C      . ILE B 2 52  ? 31.261  -6.451  -32.575 1.00 15.44  ?  52   ILE B C      1 
ATOM   7961  O O      . ILE B 2 52  ? 31.890  -7.506  -32.420 1.00 17.08  ?  52   ILE B O      1 
ATOM   7962  C CB     . ILE B 2 52  ? 32.912  -5.024  -33.819 1.00 17.29  ?  52   ILE B CB     1 
ATOM   7963  C CG1    . ILE B 2 52  ? 33.511  -3.632  -33.896 1.00 19.45  ?  52   ILE B CG1    1 
ATOM   7964  C CG2    . ILE B 2 52  ? 32.136  -5.300  -35.074 1.00 18.35  ?  52   ILE B CG2    1 
ATOM   7965  C CD1    . ILE B 2 52  ? 34.498  -3.452  -35.059 1.00 21.52  ?  52   ILE B CD1    1 
ATOM   7966  H H      . ILE B 2 52  ? 33.583  -5.169  -31.423 1.00 20.20  ?  52   ILE B H      1 
ATOM   7967  H HA     . ILE B 2 52  ? 31.351  -4.389  -32.662 1.00 20.61  ?  52   ILE B HA     1 
ATOM   7968  H HB     . ILE B 2 52  ? 33.619  -5.681  -33.728 1.00 20.75  ?  52   ILE B HB     1 
ATOM   7969  H HG12   . ILE B 2 52  ? 32.795  -2.988  -34.012 1.00 23.33  ?  52   ILE B HG12   1 
ATOM   7970  H HG13   . ILE B 2 52  ? 33.989  -3.451  -33.071 1.00 23.33  ?  52   ILE B HG13   1 
ATOM   7971  H HG21   . ILE B 2 52  ? 32.707  -5.139  -35.841 1.00 22.02  ?  52   ILE B HG21   1 
ATOM   7972  H HG22   . ILE B 2 52  ? 31.844  -6.225  -35.067 1.00 22.02  ?  52   ILE B HG22   1 
ATOM   7973  H HG23   . ILE B 2 52  ? 31.366  -4.710  -35.105 1.00 22.02  ?  52   ILE B HG23   1 
ATOM   7974  H HD11   . ILE B 2 52  ? 35.106  -2.726  -34.848 1.00 25.82  ?  52   ILE B HD11   1 
ATOM   7975  H HD12   . ILE B 2 52  ? 34.996  -4.275  -35.181 1.00 25.82  ?  52   ILE B HD12   1 
ATOM   7976  H HD13   . ILE B 2 52  ? 34.001  -3.243  -35.865 1.00 25.82  ?  52   ILE B HD13   1 
ATOM   7977  N N      . ASP B 2 53  ? 29.931  -6.409  -32.697 1.00 15.93  ?  53   ASP B N      1 
ATOM   7978  C CA     . ASP B 2 53  ? 29.143  -7.641  -32.720 1.00 14.78  ?  53   ASP B CA     1 
ATOM   7979  C C      . ASP B 2 53  ? 28.993  -8.095  -34.165 1.00 17.00  ?  53   ASP B C      1 
ATOM   7980  O O      . ASP B 2 53  ? 28.050  -7.727  -34.870 1.00 16.51  ?  53   ASP B O      1 
ATOM   7981  C CB     . ASP B 2 53  ? 27.781  -7.460  -32.078 1.00 14.91  ?  53   ASP B CB     1 
ATOM   7982  C CG     . ASP B 2 53  ? 27.052  -8.773  -31.919 1.00 15.98  ?  53   ASP B CG     1 
ATOM   7983  O OD1    . ASP B 2 53  ? 27.642  -9.799  -32.298 1.00 16.19  ?  53   ASP B OD1    1 
ATOM   7984  O OD2    . ASP B 2 53  ? 25.892  -8.767  -31.447 1.00 15.68  -1 53   ASP B OD2    1 
ATOM   7985  H H      . ASP B 2 53  ? 29.470  -5.686  -32.766 1.00 19.11  ?  53   ASP B H      1 
ATOM   7986  H HA     . ASP B 2 53  ? 29.634  -8.311  -32.220 1.00 17.74  ?  53   ASP B HA     1 
ATOM   7987  H HB2    . ASP B 2 53  ? 27.893  -7.067  -31.198 1.00 17.89  ?  53   ASP B HB2    1 
ATOM   7988  H HB3    . ASP B 2 53  ? 27.240  -6.878  -32.634 1.00 17.89  ?  53   ASP B HB3    1 
ATOM   7989  N N      . GLY B 2 54  ? 29.920  -8.946  -34.591 1.00 15.64  ?  54   GLY B N      1 
ATOM   7990  C CA     . GLY B 2 54  ? 29.851  -9.521  -35.906 1.00 15.24  ?  54   GLY B CA     1 
ATOM   7991  C C      . GLY B 2 54  ? 28.785  -10.577 -36.088 1.00 16.13  ?  54   GLY B C      1 
ATOM   7992  O O      . GLY B 2 54  ? 28.672  -11.100 -37.194 1.00 16.50  ?  54   GLY B O      1 
ATOM   7993  H H      . GLY B 2 54  ? 30.599  -9.200  -34.128 1.00 18.76  ?  54   GLY B H      1 
ATOM   7994  H HA2    . GLY B 2 54  ? 29.677  -8.813  -36.545 1.00 18.28  ?  54   GLY B HA2    1 
ATOM   7995  H HA3    . GLY B 2 54  ? 30.707  -9.928  -36.111 1.00 18.28  ?  54   GLY B HA3    1 
ATOM   7996  N N      . PHE B 2 55  ? 27.988  -10.871 -35.053 1.00 15.45  ?  55   PHE B N      1 
ATOM   7997  C CA     . PHE B 2 55  ? 26.916  -11.853 -35.160 1.00 15.40  ?  55   PHE B CA     1 
ATOM   7998  C C      . PHE B 2 55  ? 25.540  -11.260 -34.888 1.00 14.89  ?  55   PHE B C      1 
ATOM   7999  O O      . PHE B 2 55  ? 24.561  -12.007 -34.880 1.00 15.01  ?  55   PHE B O      1 
ATOM   8000  C CB     . PHE B 2 55  ? 27.171  -13.035 -34.206 1.00 16.31  ?  55   PHE B CB     1 
ATOM   8001  C CG     . PHE B 2 55  ? 26.827  -14.379 -34.807 1.00 16.46  ?  55   PHE B CG     1 
ATOM   8002  C CD1    . PHE B 2 55  ? 27.569  -14.898 -35.854 1.00 17.24  ?  55   PHE B CD1    1 
ATOM   8003  C CD2    . PHE B 2 55  ? 25.756  -15.116 -34.319 1.00 18.35  ?  55   PHE B CD2    1 
ATOM   8004  C CE1    . PHE B 2 55  ? 27.243  -16.120 -36.428 1.00 16.64  ?  55   PHE B CE1    1 
ATOM   8005  C CE2    . PHE B 2 55  ? 25.438  -16.353 -34.866 1.00 16.97  ?  55   PHE B CE2    1 
ATOM   8006  C CZ     . PHE B 2 55  ? 26.180  -16.857 -35.913 1.00 15.49  ?  55   PHE B CZ     1 
ATOM   8007  H H      . PHE B 2 55  ? 28.054  -10.508 -34.275 1.00 18.54  ?  55   PHE B H      1 
ATOM   8008  H HA     . PHE B 2 55  ? 26.911  -12.208 -36.063 1.00 18.47  ?  55   PHE B HA     1 
ATOM   8009  H HB2    . PHE B 2 55  ? 28.111  -13.047 -33.968 1.00 19.57  ?  55   PHE B HB2    1 
ATOM   8010  H HB3    . PHE B 2 55  ? 26.628  -12.917 -33.411 1.00 19.57  ?  55   PHE B HB3    1 
ATOM   8011  H HD1    . PHE B 2 55  ? 28.297  -14.419 -36.179 1.00 20.68  ?  55   PHE B HD1    1 
ATOM   8012  H HD2    . PHE B 2 55  ? 25.245  -14.778 -33.620 1.00 22.02  ?  55   PHE B HD2    1 
ATOM   8013  H HE1    . PHE B 2 55  ? 27.731  -16.444 -37.151 1.00 19.97  ?  55   PHE B HE1    1 
ATOM   8014  H HE2    . PHE B 2 55  ? 24.724  -16.842 -34.525 1.00 20.36  ?  55   PHE B HE2    1 
ATOM   8015  H HZ     . PHE B 2 55  ? 25.971  -17.688 -36.274 1.00 18.59  ?  55   PHE B HZ     1 
ATOM   8016  N N      . ALA B 2 56  ? 25.439  -9.949  -34.656 1.00 14.91  ?  56   ALA B N      1 
ATOM   8017  C CA     . ALA B 2 56  ? 24.154  -9.278  -34.442 1.00 14.43  ?  56   ALA B CA     1 
ATOM   8018  C C      . ALA B 2 56  ? 23.294  -10.039 -33.434 1.00 14.72  ?  56   ALA B C      1 
ATOM   8019  O O      . ALA B 2 56  ? 22.133  -10.361 -33.683 1.00 14.16  ?  56   ALA B O      1 
ATOM   8020  C CB     . ALA B 2 56  ? 23.398  -9.095  -35.758 1.00 15.31  ?  56   ALA B CB     1 
ATOM   8021  H H      . ALA B 2 56  ? 26.113  -9.417  -34.618 1.00 17.89  ?  56   ALA B H      1 
ATOM   8022  H HA     . ALA B 2 56  ? 24.338  -8.399  -34.074 1.00 17.32  ?  56   ALA B HA     1 
ATOM   8023  H HB1    . ALA B 2 56  ? 22.582  -8.598  -35.587 1.00 18.36  ?  56   ALA B HB1    1 
ATOM   8024  H HB2    . ALA B 2 56  ? 23.959  -8.605  -36.379 1.00 18.36  ?  56   ALA B HB2    1 
ATOM   8025  H HB3    . ALA B 2 56  ? 23.184  -9.967  -36.123 1.00 18.36  ?  56   ALA B HB3    1 
ATOM   8026  N N      . GLY B 2 57  ? 23.860  -10.297 -32.267 1.00 14.95  ?  57   GLY B N      1 
ATOM   8027  C CA     . GLY B 2 57  ? 23.175  -11.086 -31.265 1.00 14.84  ?  57   GLY B CA     1 
ATOM   8028  C C      . GLY B 2 57  ? 23.270  -12.542 -31.659 1.00 14.93  ?  57   GLY B C      1 
ATOM   8029  O O      . GLY B 2 57  ? 24.311  -13.183 -31.499 1.00 15.49  ?  57   GLY B O      1 
ATOM   8030  H H      . GLY B 2 57  ? 24.641  -10.025 -32.032 1.00 17.93  ?  57   GLY B H      1 
ATOM   8031  H HA2    . GLY B 2 57  ? 23.588  -10.959 -30.396 1.00 17.80  ?  57   GLY B HA2    1 
ATOM   8032  H HA3    . GLY B 2 57  ? 22.242  -10.827 -31.212 1.00 17.80  ?  57   GLY B HA3    1 
ATOM   8033  N N      . LEU B 2 58  ? 22.162  -13.067 -32.197 1.00 14.83  ?  58   LEU B N      1 
ATOM   8034  C CA     . LEU B 2 58  ? 22.111  -14.375 -32.866 1.00 14.11  ?  58   LEU B CA     1 
ATOM   8035  C C      . LEU B 2 58  ? 21.384  -14.154 -34.197 1.00 14.73  ?  58   LEU B C      1 
ATOM   8036  O O      . LEU B 2 58  ? 20.195  -14.452 -34.331 1.00 14.97  ?  58   LEU B O      1 
ATOM   8037  C CB     . LEU B 2 58  ? 21.392  -15.408 -32.009 1.00 15.36  ?  58   LEU B CB     1 
ATOM   8038  C CG     . LEU B 2 58  ? 22.113  -15.768 -30.699 1.00 16.16  ?  58   LEU B CG     1 
ATOM   8039  C CD1    . LEU B 2 58  ? 21.192  -16.569 -29.800 1.00 15.19  ?  58   LEU B CD1    1 
ATOM   8040  C CD2    . LEU B 2 58  ? 23.387  -16.573 -30.970 1.00 18.81  ?  58   LEU B CD2    1 
ATOM   8041  H H      . LEU B 2 58  ? 21.400  -12.668 -32.186 1.00 17.79  ?  58   LEU B H      1 
ATOM   8042  H HA     . LEU B 2 58  ? 23.013  -14.692 -33.030 1.00 16.93  ?  58   LEU B HA     1 
ATOM   8043  H HB2    . LEU B 2 58  ? 20.517  -15.059 -31.775 1.00 18.43  ?  58   LEU B HB2    1 
ATOM   8044  H HB3    . LEU B 2 58  ? 21.297  -16.224 -32.525 1.00 18.43  ?  58   LEU B HB3    1 
ATOM   8045  H HG     . LEU B 2 58  ? 22.363  -14.944 -30.253 1.00 19.39  ?  58   LEU B HG     1 
ATOM   8046  H HD11   . LEU B 2 58  ? 21.654  -16.765 -28.970 1.00 18.22  ?  58   LEU B HD11   1 
ATOM   8047  H HD12   . LEU B 2 58  ? 20.395  -16.047 -29.619 1.00 18.22  ?  58   LEU B HD12   1 
ATOM   8048  H HD13   . LEU B 2 58  ? 20.952  -17.394 -30.249 1.00 18.22  ?  58   LEU B HD13   1 
ATOM   8049  H HD21   . LEU B 2 58  ? 23.815  -16.780 -30.124 1.00 22.57  ?  58   LEU B HD21   1 
ATOM   8050  H HD22   . LEU B 2 58  ? 23.150  -17.393 -31.431 1.00 22.57  ?  58   LEU B HD22   1 
ATOM   8051  H HD23   . LEU B 2 58  ? 23.983  -16.043 -31.522 1.00 22.57  ?  58   LEU B HD23   1 
ATOM   8052  N N      . TYR B 2 59  ? 22.099  -13.600 -35.172 1.00 14.35  ?  59   TYR B N      1 
ATOM   8053  C CA     . TYR B 2 59  ? 21.541  -13.298 -36.490 1.00 15.23  ?  59   TYR B CA     1 
ATOM   8054  C C      . TYR B 2 59  ? 20.263  -12.451 -36.392 1.00 15.02  ?  59   TYR B C      1 
ATOM   8055  O O      . TYR B 2 59  ? 19.329  -12.629 -37.182 1.00 16.41  ?  59   TYR B O      1 
ATOM   8056  C CB     . TYR B 2 59  ? 21.167  -14.540 -37.337 1.00 16.75  ?  59   TYR B CB     1 
ATOM   8057  C CG     . TYR B 2 59  ? 21.954  -15.817 -37.202 1.00 16.08  ?  59   TYR B CG     1 
ATOM   8058  C CD1    . TYR B 2 59  ? 21.692  -16.703 -36.168 1.00 17.17  ?  59   TYR B CD1    1 
ATOM   8059  C CD2    . TYR B 2 59  ? 22.897  -16.188 -38.161 1.00 18.08  ?  59   TYR B CD2    1 
ATOM   8060  C CE1    . TYR B 2 59  ? 22.383  -17.887 -36.054 1.00 19.51  ?  59   TYR B CE1    1 
ATOM   8061  C CE2    . TYR B 2 59  ? 23.577  -17.382 -38.058 1.00 18.17  ?  59   TYR B CE2    1 
ATOM   8062  C CZ     . TYR B 2 59  ? 23.330  -18.220 -36.996 1.00 19.68  ?  59   TYR B CZ     1 
ATOM   8063  O OH     . TYR B 2 59  ? 24.003  -19.407 -36.860 1.00 24.28  ?  59   TYR B OH     1 
ATOM   8064  H H      . TYR B 2 59  ? 22.927  -13.384 -35.094 1.00 17.22  ?  59   TYR B H      1 
ATOM   8065  H HA     . TYR B 2 59  ? 22.257  -12.819 -36.937 1.00 18.28  ?  59   TYR B HA     1 
ATOM   8066  H HB2    . TYR B 2 59  ? 20.249  -14.767 -37.121 1.00 20.10  ?  59   TYR B HB2    1 
ATOM   8067  H HB3    . TYR B 2 59  ? 21.234  -14.281 -38.269 1.00 20.10  ?  59   TYR B HB3    1 
ATOM   8068  H HD1    . TYR B 2 59  ? 21.039  -16.492 -35.540 1.00 20.60  ?  59   TYR B HD1    1 
ATOM   8069  H HD2    . TYR B 2 59  ? 23.068  -15.622 -38.878 1.00 21.69  ?  59   TYR B HD2    1 
ATOM   8070  H HE1    . TYR B 2 59  ? 22.211  -18.461 -35.343 1.00 23.41  ?  59   TYR B HE1    1 
ATOM   8071  H HE2    . TYR B 2 59  ? 24.201  -17.620 -38.705 1.00 21.80  ?  59   TYR B HE2    1 
ATOM   8072  H HH     . TYR B 2 59  ? 24.325  -19.641 -37.600 1.00 29.13  ?  59   TYR B HH     1 
ATOM   8073  N N      . CYS B 2 60  ? 20.167  -11.539 -35.425 1.00 14.36  ?  60   CYS B N      1 
ATOM   8074  C CA     . CYS B 2 60  ? 18.858  -10.949 -35.193 1.00 14.97  ?  60   CYS B CA     1 
ATOM   8075  C C      . CYS B 2 60  ? 18.822  -9.459  -34.926 1.00 15.05  ?  60   CYS B C      1 
ATOM   8076  O O      . CYS B 2 60  ? 17.777  -8.862  -35.189 1.00 16.37  ?  60   CYS B O      1 
ATOM   8077  C CB     . CYS B 2 60  ? 18.099  -11.669 -34.064 1.00 14.43  ?  60   CYS B CB     1 
ATOM   8078  S SG     . CYS B 2 60  ? 18.928  -11.772 -32.463 1.00 14.78  ?  60   CYS B SG     1 
ATOM   8079  H H      . CYS B 2 60  ? 20.808  -11.265 -34.921 1.00 17.23  ?  60   CYS B H      1 
ATOM   8080  H HA     . CYS B 2 60  ? 18.360  -11.085 -36.014 1.00 17.96  ?  60   CYS B HA     1 
ATOM   8081  H HB2    . CYS B 2 60  ? 17.262  -11.201 -33.920 1.00 17.31  ?  60   CYS B HB2    1 
ATOM   8082  H HB3    . CYS B 2 60  ? 17.926  -12.579 -34.352 1.00 17.31  ?  60   CYS B HB3    1 
ATOM   8083  H HG     . CYS B 2 60  ? 18.185  -12.282 -31.671 1.00 17.73  ?  60   CYS B HG     1 
ATOM   8084  N N      . VAL B 2 61  ? 19.884  -8.816  -34.458 1.00 13.31  ?  61   VAL B N      1 
ATOM   8085  C CA     . VAL B 2 61  ? 19.823  -7.380  -34.201 1.00 14.42  ?  61   VAL B CA     1 
ATOM   8086  C C      . VAL B 2 61  ? 20.109  -6.666  -35.516 1.00 15.44  ?  61   VAL B C      1 
ATOM   8087  O O      . VAL B 2 61  ? 21.144  -6.021  -35.688 1.00 15.88  ?  61   VAL B O      1 
ATOM   8088  C CB     . VAL B 2 61  ? 20.750  -6.956  -33.060 1.00 14.80  ?  61   VAL B CB     1 
ATOM   8089  C CG1    . VAL B 2 61  ? 20.528  -5.488  -32.742 1.00 17.29  ?  61   VAL B CG1    1 
ATOM   8090  C CG2    . VAL B 2 61  ? 20.496  -7.836  -31.847 1.00 16.35  ?  61   VAL B CG2    1 
ATOM   8091  H H      . VAL B 2 61  ? 20.642  -9.184  -34.284 1.00 15.97  ?  61   VAL B H      1 
ATOM   8092  H HA     . VAL B 2 61  ? 18.933  -7.127  -33.910 1.00 17.30  ?  61   VAL B HA     1 
ATOM   8093  H HB     . VAL B 2 61  ? 21.678  -7.066  -33.318 1.00 17.76  ?  61   VAL B HB     1 
ATOM   8094  H HG11   . VAL B 2 61  ? 21.021  -5.261  -31.938 1.00 20.74  ?  61   VAL B HG11   1 
ATOM   8095  H HG12   . VAL B 2 61  ? 20.845  -4.952  -33.486 1.00 20.74  ?  61   VAL B HG12   1 
ATOM   8096  H HG13   . VAL B 2 61  ? 19.580  -5.335  -32.604 1.00 20.74  ?  61   VAL B HG13   1 
ATOM   8097  H HG21   . VAL B 2 61  ? 20.948  -7.453  -31.080 1.00 19.62  ?  61   VAL B HG21   1 
ATOM   8098  H HG22   . VAL B 2 61  ? 19.541  -7.877  -31.682 1.00 19.62  ?  61   VAL B HG22   1 
ATOM   8099  H HG23   . VAL B 2 61  ? 20.839  -8.725  -32.025 1.00 19.62  ?  61   VAL B HG23   1 
ATOM   8100  N N      . ASN B 2 62  ? 19.171  -6.777  -36.450 1.00 15.34  ?  62   ASN B N      1 
ATOM   8101  C CA     . ASN B 2 62  ? 19.466  -6.493  -37.849 1.00 15.22  ?  62   ASN B CA     1 
ATOM   8102  C C      . ASN B 2 62  ? 19.551  -5.003  -38.149 1.00 15.48  ?  62   ASN B C      1 
ATOM   8103  O O      . ASN B 2 62  ? 20.364  -4.619  -38.987 1.00 16.18  ?  62   ASN B O      1 
ATOM   8104  C CB     . ASN B 2 62  ? 18.476  -7.229  -38.757 1.00 14.48  ?  62   ASN B CB     1 
ATOM   8105  C CG     . ASN B 2 62  ? 18.776  -8.717  -38.834 1.00 14.69  ?  62   ASN B CG     1 
ATOM   8106  O OD1    . ASN B 2 62  ? 19.713  -9.202  -38.190 1.00 15.62  ?  62   ASN B OD1    1 
ATOM   8107  N ND2    . ASN B 2 62  ? 18.025  -9.430  -39.630 1.00 14.53  ?  62   ASN B ND2    1 
ATOM   8108  H H      . ASN B 2 62  ? 18.357  -7.014  -36.303 1.00 18.40  ?  62   ASN B H      1 
ATOM   8109  H HA     . ASN B 2 62  ? 20.343  -6.846  -38.066 1.00 18.26  ?  62   ASN B HA     1 
ATOM   8110  H HB2    . ASN B 2 62  ? 17.579  -7.118  -38.407 1.00 17.37  ?  62   ASN B HB2    1 
ATOM   8111  H HB3    . ASN B 2 62  ? 18.531  -6.861  -39.653 1.00 17.37  ?  62   ASN B HB3    1 
ATOM   8112  H HD21   . ASN B 2 62  ? 18.160  -10.276 -39.704 1.00 17.43  ?  62   ASN B HD21   1 
ATOM   8113  H HD22   . ASN B 2 62  ? 17.396  -9.053  -40.079 1.00 17.43  ?  62   ASN B HD22   1 
ATOM   8114  N N      . ILE B 2 63  ? 18.758  -4.164  -37.482 1.00 16.17  ?  63   ILE B N      1 
ATOM   8115  C CA     . ILE B 2 63  ? 18.843  -2.720  -37.674 1.00 16.13  ?  63   ILE B CA     1 
ATOM   8116  C C      . ILE B 2 63  ? 19.874  -2.069  -36.754 1.00 17.29  ?  63   ILE B C      1 
ATOM   8117  O O      . ILE B 2 63  ? 20.007  -0.847  -36.725 1.00 17.65  ?  63   ILE B O      1 
ATOM   8118  C CB     . ILE B 2 63  ? 17.473  -2.031  -37.502 1.00 16.53  ?  63   ILE B CB     1 
ATOM   8119  C CG1    . ILE B 2 63  ? 16.913  -2.253  -36.097 1.00 15.99  ?  63   ILE B CG1    1 
ATOM   8120  C CG2    . ILE B 2 63  ? 16.491  -2.497  -38.594 1.00 17.21  ?  63   ILE B CG2    1 
ATOM   8121  C CD1    . ILE B 2 63  ? 15.634  -1.441  -35.841 1.00 17.45  ?  63   ILE B CD1    1 
ATOM   8122  H H      . ILE B 2 63  ? 18.162  -4.409  -36.912 1.00 19.40  ?  63   ILE B H      1 
ATOM   8123  H HA     . ILE B 2 63  ? 19.156  -2.595  -38.583 1.00 19.36  ?  63   ILE B HA     1 
ATOM   8124  H HB     . ILE B 2 63  ? 17.600  -1.075  -37.608 1.00 19.83  ?  63   ILE B HB     1 
ATOM   8125  H HG12   . ILE B 2 63  ? 16.701  -3.193  -35.985 1.00 19.18  ?  63   ILE B HG12   1 
ATOM   8126  H HG13   . ILE B 2 63  ? 17.577  -1.983  -35.444 1.00 19.18  ?  63   ILE B HG13   1 
ATOM   8127  H HG21   . ILE B 2 63  ? 15.678  -1.970  -38.534 1.00 20.64  ?  63   ILE B HG21   1 
ATOM   8128  H HG22   . ILE B 2 63  ? 16.902  -2.372  -39.464 1.00 20.64  ?  63   ILE B HG22   1 
ATOM   8129  H HG23   . ILE B 2 63  ? 16.287  -3.435  -38.456 1.00 20.64  ?  63   ILE B HG23   1 
ATOM   8130  H HD11   . ILE B 2 63  ? 15.392  -1.520  -34.905 1.00 20.93  ?  63   ILE B HD11   1 
ATOM   8131  H HD12   . ILE B 2 63  ? 15.801  -0.511  -36.062 1.00 20.93  ?  63   ILE B HD12   1 
ATOM   8132  H HD13   . ILE B 2 63  ? 14.921  -1.790  -36.398 1.00 20.93  ?  63   ILE B HD13   1 
ATOM   8133  N N      . GLY B 2 64  ? 20.613  -2.872  -36.007 1.00 17.40  ?  64   GLY B N      1 
ATOM   8134  C CA     . GLY B 2 64  ? 21.590  -2.348  -35.071 1.00 16.82  ?  64   GLY B CA     1 
ATOM   8135  C C      . GLY B 2 64  ? 21.020  -2.097  -33.681 1.00 17.05  ?  64   GLY B C      1 
ATOM   8136  O O      . GLY B 2 64  ? 19.802  -2.087  -33.445 1.00 16.82  ?  64   GLY B O      1 
ATOM   8137  H H      . GLY B 2 64  ? 20.566  -3.730  -36.024 1.00 20.88  ?  64   GLY B H      1 
ATOM   8138  H HA2    . GLY B 2 64  ? 22.320  -2.981  -34.987 1.00 20.18  ?  64   GLY B HA2    1 
ATOM   8139  H HA3    . GLY B 2 64  ? 21.936  -1.508  -35.411 1.00 20.18  ?  64   GLY B HA3    1 
ATOM   8140  N N      . TYR B 2 65  ? 21.948  -1.902  -32.750 1.00 16.45  ?  65   TYR B N      1 
ATOM   8141  C CA     . TYR B 2 65  ? 21.647  -1.646  -31.351 1.00 16.96  ?  65   TYR B CA     1 
ATOM   8142  C C      . TYR B 2 65  ? 21.277  -0.187  -31.093 1.00 16.86  ?  65   TYR B C      1 
ATOM   8143  O O      . TYR B 2 65  ? 21.683  0.733   -31.824 1.00 17.71  ?  65   TYR B O      1 
ATOM   8144  C CB     . TYR B 2 65  ? 22.878  -1.999  -30.508 1.00 16.90  ?  65   TYR B CB     1 
ATOM   8145  C CG     . TYR B 2 65  ? 23.168  -3.478  -30.453 1.00 16.89  ?  65   TYR B CG     1 
ATOM   8146  C CD1    . TYR B 2 65  ? 22.528  -4.294  -29.527 1.00 17.41  ?  65   TYR B CD1    1 
ATOM   8147  C CD2    . TYR B 2 65  ? 24.052  -4.068  -31.343 1.00 19.37  ?  65   TYR B CD2    1 
ATOM   8148  C CE1    . TYR B 2 65  ? 22.777  -5.656  -29.474 1.00 15.71  ?  65   TYR B CE1    1 
ATOM   8149  C CE2    . TYR B 2 65  ? 24.294  -5.433  -31.307 1.00 18.33  ?  65   TYR B CE2    1 
ATOM   8150  C CZ     . TYR B 2 65  ? 23.653  -6.223  -30.374 1.00 15.29  ?  65   TYR B CZ     1 
ATOM   8151  O OH     . TYR B 2 65  ? 23.873  -7.574  -30.308 1.00 16.81  ?  65   TYR B OH     1 
ATOM   8152  H H      . TYR B 2 65  ? 22.793  -1.914  -32.911 1.00 19.73  ?  65   TYR B H      1 
ATOM   8153  H HA     . TYR B 2 65  ? 20.885  -2.185  -31.088 1.00 20.35  ?  65   TYR B HA     1 
ATOM   8154  H HB2    . TYR B 2 65  ? 23.654  -1.559  -30.888 1.00 20.27  ?  65   TYR B HB2    1 
ATOM   8155  H HB3    . TYR B 2 65  ? 22.734  -1.691  -29.599 1.00 20.27  ?  65   TYR B HB3    1 
ATOM   8156  H HD1    . TYR B 2 65  ? 21.921  -3.918  -28.931 1.00 20.89  ?  65   TYR B HD1    1 
ATOM   8157  H HD2    . TYR B 2 65  ? 24.488  -3.541  -31.973 1.00 23.24  ?  65   TYR B HD2    1 
ATOM   8158  H HE1    . TYR B 2 65  ? 22.355  -6.184  -28.835 1.00 18.85  ?  65   TYR B HE1    1 
ATOM   8159  H HE2    . TYR B 2 65  ? 24.889  -5.816  -31.911 1.00 21.99  ?  65   TYR B HE2    1 
ATOM   8160  H HH     . TYR B 2 65  ? 24.413  -7.807  -30.908 1.00 20.17  ?  65   TYR B HH     1 
ATOM   8161  N N      . GLY B 2 66  ? 20.509  0.032   -30.028 1.00 18.47  ?  66   GLY B N      1 
ATOM   8162  C CA     . GLY B 2 66  ? 20.316  1.379   -29.525 1.00 18.37  ?  66   GLY B CA     1 
ATOM   8163  C C      . GLY B 2 66  ? 19.293  2.200   -30.280 1.00 17.21  ?  66   GLY B C      1 
ATOM   8164  O O      . GLY B 2 66  ? 19.378  3.434   -30.275 1.00 20.14  ?  66   GLY B O      1 
ATOM   8165  H H      . GLY B 2 66  ? 20.095  -0.578  -29.585 1.00 22.16  ?  66   GLY B H      1 
ATOM   8166  H HA2    . GLY B 2 66  ? 20.029  1.327   -28.600 1.00 22.04  ?  66   GLY B HA2    1 
ATOM   8167  H HA3    . GLY B 2 66  ? 21.163  1.850   -29.566 1.00 22.04  ?  66   GLY B HA3    1 
ATOM   8168  N N      . ARG B 2 67  ? 18.315  1.547   -30.908 1.00 17.79  ?  67   ARG B N      1 
ATOM   8169  C CA     . ARG B 2 67  ? 17.309  2.238   -31.716 1.00 19.29  ?  67   ARG B CA     1 
ATOM   8170  C C      . ARG B 2 67  ? 16.241  2.825   -30.809 1.00 19.81  ?  67   ARG B C      1 
ATOM   8171  O O      . ARG B 2 67  ? 15.224  2.189   -30.510 1.00 19.86  ?  67   ARG B O      1 
ATOM   8172  C CB     . ARG B 2 67  ? 16.701  1.279   -32.719 1.00 18.89  ?  67   ARG B CB     1 
ATOM   8173  C CG     . ARG B 2 67  ? 17.661  0.912   -33.831 1.00 18.40  ?  67   ARG B CG     1 
ATOM   8174  C CD     . ARG B 2 67  ? 17.676  1.965   -34.924 1.00 19.72  ?  67   ARG B CD     1 
ATOM   8175  N NE     . ARG B 2 67  ? 18.397  1.479   -36.105 1.00 19.59  ?  67   ARG B NE     1 
ATOM   8176  C CZ     . ARG B 2 67  ? 18.471  2.119   -37.267 1.00 18.76  ?  67   ARG B CZ     1 
ATOM   8177  N NH1    . ARG B 2 67  ? 17.873  3.294   -37.441 1.00 18.87  ?  67   ARG B NH1    1 
ATOM   8178  N NH2    . ARG B 2 67  ? 19.147  1.580   -38.263 1.00 21.87  ?  67   ARG B NH2    1 
ATOM   8179  H H      . ARG B 2 67  ? 18.213  0.693   -30.882 1.00 21.34  ?  67   ARG B H      1 
ATOM   8180  H HA     . ARG B 2 67  ? 17.735  2.973   -32.183 1.00 23.14  ?  67   ARG B HA     1 
ATOM   8181  H HB2    . ARG B 2 67  ? 16.445  0.463   -32.261 1.00 22.66  ?  67   ARG B HB2    1 
ATOM   8182  H HB3    . ARG B 2 67  ? 15.921  1.694   -33.120 1.00 22.66  ?  67   ARG B HB3    1 
ATOM   8183  H HG2    . ARG B 2 67  ? 18.558  0.835   -33.469 1.00 22.08  ?  67   ARG B HG2    1 
ATOM   8184  H HG3    . ARG B 2 67  ? 17.389  0.068   -34.224 1.00 22.08  ?  67   ARG B HG3    1 
ATOM   8185  H HD2    . ARG B 2 67  ? 16.766  2.175   -35.184 1.00 23.66  ?  67   ARG B HD2    1 
ATOM   8186  H HD3    . ARG B 2 67  ? 18.121  2.763   -34.598 1.00 23.66  ?  67   ARG B HD3    1 
ATOM   8187  H HE     . ARG B 2 67  ? 18.802  0.724   -36.040 1.00 23.50  ?  67   ARG B HE     1 
ATOM   8188  H HH11   . ARG B 2 67  ? 17.431  3.651   -36.796 1.00 22.64  ?  67   ARG B HH11   1 
ATOM   8189  H HH12   . ARG B 2 67  ? 17.929  3.697   -38.199 1.00 22.64  ?  67   ARG B HH12   1 
ATOM   8190  H HH21   . ARG B 2 67  ? 19.536  0.820   -38.158 1.00 26.24  ?  67   ARG B HH21   1 
ATOM   8191  H HH22   . ARG B 2 67  ? 19.198  1.988   -39.018 1.00 26.24  ?  67   ARG B HH22   1 
ATOM   8192  N N      . THR B 2 68  ? 16.453  4.076   -30.389 1.00 21.09  ?  68   THR B N      1 
ATOM   8193  C CA     . THR B 2 68  ? 15.451  4.743   -29.572 1.00 22.52  ?  68   THR B CA     1 
ATOM   8194  C C      . THR B 2 68  ? 14.133  4.860   -30.317 1.00 19.62  ?  68   THR B C      1 
ATOM   8195  O O      . THR B 2 68  ? 13.068  4.900   -29.697 1.00 19.33  ?  68   THR B O      1 
ATOM   8196  C CB     . THR B 2 68  ? 15.960  6.115   -29.133 1.00 27.14  ?  68   THR B CB     1 
ATOM   8197  O OG1    . THR B 2 68  ? 16.106  6.962   -30.275 1.00 32.45  ?  68   THR B OG1    1 
ATOM   8198  C CG2    . THR B 2 68  ? 17.298  5.985   -28.459 1.00 25.98  ?  68   THR B CG2    1 
ATOM   8199  H H      . THR B 2 68  ? 17.152  4.547   -30.560 1.00 25.30  ?  68   THR B H      1 
ATOM   8200  H HA     . THR B 2 68  ? 15.293  4.225   -28.768 1.00 27.02  ?  68   THR B HA     1 
ATOM   8201  H HB     . THR B 2 68  ? 15.328  6.507   -28.510 1.00 32.56  ?  68   THR B HB     1 
ATOM   8202  H HG1    . THR B 2 68  ? 16.619  6.603   -30.835 1.00 38.93  ?  68   THR B HG1    1 
ATOM   8203  H HG21   . THR B 2 68  ? 17.523  6.813   -28.006 1.00 31.17  ?  68   THR B HG21   1 
ATOM   8204  H HG22   . THR B 2 68  ? 17.274  5.266   -27.809 1.00 31.17  ?  68   THR B HG22   1 
ATOM   8205  H HG23   . THR B 2 68  ? 17.984  5.791   -29.118 1.00 31.17  ?  68   THR B HG23   1 
ATOM   8206  N N      . GLU B 2 69  ? 14.183  4.909   -31.648 1.00 18.49  ?  69   GLU B N      1 
ATOM   8207  C CA     . GLU B 2 69  ? 12.959  4.970   -32.427 1.00 20.06  ?  69   GLU B CA     1 
ATOM   8208  C C      . GLU B 2 69  ? 12.061  3.771   -32.130 1.00 19.68  ?  69   GLU B C      1 
ATOM   8209  O O      . GLU B 2 69  ? 10.835  3.911   -32.016 1.00 19.00  ?  69   GLU B O      1 
ATOM   8210  C CB     . GLU B 2 69  ? 13.321  5.025   -33.910 1.00 20.61  ?  69   GLU B CB     1 
ATOM   8211  C CG     . GLU B 2 69  ? 12.135  5.158   -34.809 1.00 23.97  ?  69   GLU B CG     1 
ATOM   8212  C CD     . GLU B 2 69  ? 12.531  5.267   -36.274 1.00 26.75  ?  69   GLU B CD     1 
ATOM   8213  O OE1    . GLU B 2 69  ? 13.737  5.381   -36.573 1.00 28.79  ?  69   GLU B OE1    1 
ATOM   8214  O OE2    . GLU B 2 69  ? 11.620  5.236   -37.119 1.00 27.23  -1 69   GLU B OE2    1 
ATOM   8215  H H      . GLU B 2 69  ? 14.904  4.907   -32.116 1.00 22.19  ?  69   GLU B H      1 
ATOM   8216  H HA     . GLU B 2 69  ? 12.462  5.771   -32.199 1.00 24.07  ?  69   GLU B HA     1 
ATOM   8217  H HB2    . GLU B 2 69  ? 13.897  5.791   -34.063 1.00 24.72  ?  69   GLU B HB2    1 
ATOM   8218  H HB3    . GLU B 2 69  ? 13.785  4.208   -34.150 1.00 24.72  ?  69   GLU B HB3    1 
ATOM   8219  H HG2    . GLU B 2 69  ? 11.569  4.377   -34.707 1.00 28.76  ?  69   GLU B HG2    1 
ATOM   8220  H HG3    . GLU B 2 69  ? 11.642  5.959   -34.570 1.00 28.76  ?  69   GLU B HG3    1 
ATOM   8221  N N      . VAL B 2 70  ? 12.649  2.580   -31.998 1.00 17.58  ?  70   VAL B N      1 
ATOM   8222  C CA     . VAL B 2 70  ? 11.850  1.391   -31.692 1.00 16.39  ?  70   VAL B CA     1 
ATOM   8223  C C      . VAL B 2 70  ? 11.367  1.421   -30.246 1.00 16.10  ?  70   VAL B C      1 
ATOM   8224  O O      . VAL B 2 70  ? 10.215  1.065   -29.949 1.00 16.17  ?  70   VAL B O      1 
ATOM   8225  C CB     . VAL B 2 70  ? 12.636  0.112   -32.020 1.00 15.73  ?  70   VAL B CB     1 
ATOM   8226  C CG1    . VAL B 2 70  ? 11.808  -1.099  -31.660 1.00 15.81  ?  70   VAL B CG1    1 
ATOM   8227  C CG2    . VAL B 2 70  ? 13.022  0.086   -33.490 1.00 17.82  ?  70   VAL B CG2    1 
ATOM   8228  H H      . VAL B 2 70  ? 13.492  2.433   -32.078 1.00 21.09  ?  70   VAL B H      1 
ATOM   8229  H HA     . VAL B 2 70  ? 11.063  1.399   -32.259 1.00 19.66  ?  70   VAL B HA     1 
ATOM   8230  H HB     . VAL B 2 70  ? 13.454  0.092   -31.499 1.00 18.88  ?  70   VAL B HB     1 
ATOM   8231  H HG11   . VAL B 2 70  ? 12.196  -1.883  -32.080 1.00 18.97  ?  70   VAL B HG11   1 
ATOM   8232  H HG12   . VAL B 2 70  ? 11.806  -1.207  -30.696 1.00 18.97  ?  70   VAL B HG12   1 
ATOM   8233  H HG13   . VAL B 2 70  ? 10.901  -0.968  -31.980 1.00 18.97  ?  70   VAL B HG13   1 
ATOM   8234  H HG21   . VAL B 2 70  ? 13.436  -0.768  -33.693 1.00 21.38  ?  70   VAL B HG21   1 
ATOM   8235  H HG22   . VAL B 2 70  ? 12.223  0.202   -34.028 1.00 21.38  ?  70   VAL B HG22   1 
ATOM   8236  H HG23   . VAL B 2 70  ? 13.647  0.807   -33.665 1.00 21.38  ?  70   VAL B HG23   1 
ATOM   8237  N N      . ALA B 2 71  ? 12.227  1.854   -29.321 1.00 18.46  ?  71   ALA B N      1 
ATOM   8238  C CA     . ALA B 2 71  ? 11.795  2.010   -27.934 1.00 19.18  ?  71   ALA B CA     1 
ATOM   8239  C C      . ALA B 2 71  ? 10.595  2.948   -27.842 1.00 19.44  ?  71   ALA B C      1 
ATOM   8240  O O      . ALA B 2 71  ? 9.650   2.683   -27.088 1.00 19.43  ?  71   ALA B O      1 
ATOM   8241  C CB     . ALA B 2 71  ? 12.953  2.559   -27.084 1.00 18.42  ?  71   ALA B CB     1 
ATOM   8242  H H      . ALA B 2 71  ? 13.049  2.060   -29.466 1.00 22.14  ?  71   ALA B H      1 
ATOM   8243  H HA     . ALA B 2 71  ? 11.540  1.142   -27.584 1.00 23.02  ?  71   ALA B HA     1 
ATOM   8244  H HB1    . ALA B 2 71  ? 12.658  2.643   -26.164 1.00 22.10  ?  71   ALA B HB1    1 
ATOM   8245  H HB2    . ALA B 2 71  ? 13.702  1.945   -27.136 1.00 22.10  ?  71   ALA B HB2    1 
ATOM   8246  H HB3    . ALA B 2 71  ? 13.213  3.428   -27.428 1.00 22.10  ?  71   ALA B HB3    1 
ATOM   8247  N N      . GLU B 2 72  ? 10.616  4.046   -28.607 1.00 18.05  ?  72   GLU B N      1 
ATOM   8248  C CA     . GLU B 2 72  ? 9.519   5.002   -28.556 1.00 19.26  ?  72   GLU B CA     1 
ATOM   8249  C C      . GLU B 2 72  ? 8.236   4.415   -29.132 1.00 17.77  ?  72   GLU B C      1 
ATOM   8250  O O      . GLU B 2 72  ? 7.145   4.693   -28.615 1.00 17.97  ?  72   GLU B O      1 
ATOM   8251  C CB     . GLU B 2 72  ? 9.910   6.283   -29.292 1.00 21.59  ?  72   GLU B CB     1 
ATOM   8252  C CG     . GLU B 2 72  ? 10.923  7.074   -28.524 1.00 29.66  ?  72   GLU B CG     1 
ATOM   8253  C CD     . GLU B 2 72  ? 11.402  8.314   -29.260 1.00 39.85  ?  72   GLU B CD     1 
ATOM   8254  O OE1    . GLU B 2 72  ? 11.262  8.383   -30.502 1.00 44.05  ?  72   GLU B OE1    1 
ATOM   8255  O OE2    . GLU B 2 72  ? 11.921  9.219   -28.575 1.00 44.28  -1 72   GLU B OE2    1 
ATOM   8256  H H      . GLU B 2 72  ? 11.246  4.255   -29.154 1.00 21.66  ?  72   GLU B H      1 
ATOM   8257  H HA     . GLU B 2 72  ? 9.346   5.229   -27.629 1.00 23.11  ?  72   GLU B HA     1 
ATOM   8258  H HB2    . GLU B 2 72  ? 10.291  6.053   -30.154 1.00 25.90  ?  72   GLU B HB2    1 
ATOM   8259  H HB3    . GLU B 2 72  ? 9.121   6.835   -29.415 1.00 25.90  ?  72   GLU B HB3    1 
ATOM   8260  H HG2    . GLU B 2 72  ? 10.529  7.359   -27.685 1.00 35.58  ?  72   GLU B HG2    1 
ATOM   8261  H HG3    . GLU B 2 72  ? 11.696  6.512   -28.354 1.00 35.58  ?  72   GLU B HG3    1 
ATOM   8262  N N      . ALA B 2 73  ? 8.339   3.622   -30.209 1.00 18.20  ?  73   ALA B N      1 
ATOM   8263  C CA     . ALA B 2 73  ? 7.145   2.984   -30.756 1.00 18.85  ?  73   ALA B CA     1 
ATOM   8264  C C      . ALA B 2 73  ? 6.542   2.004   -29.752 1.00 18.32  ?  73   ALA B C      1 
ATOM   8265  O O      . ALA B 2 73  ? 5.317   1.910   -29.620 1.00 18.90  ?  73   ALA B O      1 
ATOM   8266  C CB     . ALA B 2 73  ? 7.489   2.258   -32.056 1.00 19.02  ?  73   ALA B CB     1 
ATOM   8267  H H      . ALA B 2 73  ? 9.068   3.443   -30.627 1.00 21.84  ?  73   ALA B H      1 
ATOM   8268  H HA     . ALA B 2 73  ? 6.486   3.668   -30.954 1.00 22.62  ?  73   ALA B HA     1 
ATOM   8269  H HB1    . ALA B 2 73  ? 6.680   1.867   -32.423 1.00 22.82  ?  73   ALA B HB1    1 
ATOM   8270  H HB2    . ALA B 2 73  ? 7.863   2.895   -32.684 1.00 22.82  ?  73   ALA B HB2    1 
ATOM   8271  H HB3    . ALA B 2 73  ? 8.137   1.561   -31.867 1.00 22.82  ?  73   ALA B HB3    1 
ATOM   8272  N N      . ILE B 2 74  ? 7.389   1.249   -29.059 1.00 15.57  ?  74   ILE B N      1 
ATOM   8273  C CA     . ILE B 2 74  ? 6.905   0.340   -28.028 1.00 15.66  ?  74   ILE B CA     1 
ATOM   8274  C C      . ILE B 2 74  ? 6.208   1.139   -26.940 1.00 16.20  ?  74   ILE B C      1 
ATOM   8275  O O      . ILE B 2 74  ? 5.110   0.789   -26.489 1.00 16.48  ?  74   ILE B O      1 
ATOM   8276  C CB     . ILE B 2 74  ? 8.073   -0.488  -27.465 1.00 17.24  ?  74   ILE B CB     1 
ATOM   8277  C CG1    . ILE B 2 74  ? 8.573   -1.485  -28.508 1.00 15.96  ?  74   ILE B CG1    1 
ATOM   8278  C CG2    . ILE B 2 74  ? 7.634   -1.196  -26.197 1.00 18.08  ?  74   ILE B CG2    1 
ATOM   8279  C CD1    . ILE B 2 74  ? 9.929   -2.071  -28.220 1.00 17.02  ?  74   ILE B CD1    1 
ATOM   8280  H H      . ILE B 2 74  ? 8.242   1.243   -29.164 1.00 18.68  ?  74   ILE B H      1 
ATOM   8281  H HA     . ILE B 2 74  ? 6.262   -0.276  -28.413 1.00 18.79  ?  74   ILE B HA     1 
ATOM   8282  H HB     . ILE B 2 74  ? 8.807   0.108   -27.250 1.00 20.68  ?  74   ILE B HB     1 
ATOM   8283  H HG12   . ILE B 2 74  ? 7.942   -2.220  -28.559 1.00 19.15  ?  74   ILE B HG12   1 
ATOM   8284  H HG13   . ILE B 2 74  ? 8.626   -1.033  -29.365 1.00 19.15  ?  74   ILE B HG13   1 
ATOM   8285  H HG21   . ILE B 2 74  ? 8.241   -1.931  -26.020 1.00 21.69  ?  74   ILE B HG21   1 
ATOM   8286  H HG22   . ILE B 2 74  ? 7.653   -0.566  -25.460 1.00 21.69  ?  74   ILE B HG22   1 
ATOM   8287  H HG23   . ILE B 2 74  ? 6.733   -1.534  -26.320 1.00 21.69  ?  74   ILE B HG23   1 
ATOM   8288  H HD11   . ILE B 2 74  ? 10.191  -2.640  -28.961 1.00 20.42  ?  74   ILE B HD11   1 
ATOM   8289  H HD12   . ILE B 2 74  ? 10.569  -1.349  -28.116 1.00 20.42  ?  74   ILE B HD12   1 
ATOM   8290  H HD13   . ILE B 2 74  ? 9.881   -2.591  -27.403 1.00 20.42  ?  74   ILE B HD13   1 
ATOM   8291  N N      . HIS B 2 75  ? 6.837   2.233   -26.516 1.00 17.19  ?  75   HIS B N      1 
ATOM   8292  C CA     . HIS B 2 75  ? 6.295   3.030   -25.426 1.00 17.67  ?  75   HIS B CA     1 
ATOM   8293  C C      . HIS B 2 75  ? 4.964   3.673   -25.798 1.00 17.63  ?  75   HIS B C      1 
ATOM   8294  O O      . HIS B 2 75  ? 4.024   3.659   -24.990 1.00 17.74  ?  75   HIS B O      1 
ATOM   8295  C CB     . HIS B 2 75  ? 7.311   4.096   -25.013 1.00 19.41  ?  75   HIS B CB     1 
ATOM   8296  C CG     . HIS B 2 75  ? 6.995   4.744   -23.709 1.00 21.44  ?  75   HIS B CG     1 
ATOM   8297  N ND1    . HIS B 2 75  ? 7.012   4.052   -22.516 1.00 23.05  ?  75   HIS B ND1    1 
ATOM   8298  C CD2    . HIS B 2 75  ? 6.649   6.014   -23.404 1.00 25.57  ?  75   HIS B CD2    1 
ATOM   8299  C CE1    . HIS B 2 75  ? 6.696   4.874   -21.531 1.00 25.43  ?  75   HIS B CE1    1 
ATOM   8300  N NE2    . HIS B 2 75  ? 6.469   6.069   -22.043 1.00 25.53  ?  75   HIS B NE2    1 
ATOM   8301  H H      . HIS B 2 75  ? 7.574   2.534   -26.840 1.00 20.63  ?  75   HIS B H      1 
ATOM   8302  H HA     . HIS B 2 75  ? 6.134   2.448   -24.667 1.00 21.20  ?  75   HIS B HA     1 
ATOM   8303  H HB2    . HIS B 2 75  ? 8.185   3.682   -24.935 1.00 23.29  ?  75   HIS B HB2    1 
ATOM   8304  H HB3    . HIS B 2 75  ? 7.332   4.788   -25.692 1.00 23.29  ?  75   HIS B HB3    1 
ATOM   8305  H HD2    . HIS B 2 75  ? 6.550   6.719   -24.003 1.00 30.69  ?  75   HIS B HD2    1 
ATOM   8306  H HE1    . HIS B 2 75  ? 6.643   4.648   -20.630 1.00 30.52  ?  75   HIS B HE1    1 
ATOM   8307  H HE2    . HIS B 2 75  ? 6.245   6.769   -21.597 1.00 30.63  ?  75   HIS B HE2    1 
ATOM   8308  N N      . ARG B 2 76  ? 4.861   4.238   -27.003 1.00 18.81  ?  76   ARG B N      1 
ATOM   8309  C CA     . ARG B 2 76  ? 3.597   4.814   -27.451 1.00 19.25  ?  76   ARG B CA     1 
ATOM   8310  C C      . ARG B 2 76  ? 2.471   3.786   -27.380 1.00 18.12  ?  76   ARG B C      1 
ATOM   8311  O O      . ARG B 2 76  ? 1.362   4.082   -26.906 1.00 19.18  ?  76   ARG B O      1 
ATOM   8312  C CB     . ARG B 2 76  ? 3.738   5.342   -28.886 1.00 25.05  ?  76   ARG B CB     1 
ATOM   8313  C CG     . ARG B 2 76  ? 4.315   6.726   -28.995 1.00 35.46  ?  76   ARG B CG     1 
ATOM   8314  C CD     . ARG B 2 76  ? 4.233   7.265   -30.439 1.00 42.49  ?  76   ARG B CD     1 
ATOM   8315  N NE     . ARG B 2 76  ? 5.470   7.021   -31.189 1.00 48.99  ?  76   ARG B NE     1 
ATOM   8316  C CZ     . ARG B 2 76  ? 5.621   6.105   -32.143 1.00 52.47  ?  76   ARG B CZ     1 
ATOM   8317  N NH1    . ARG B 2 76  ? 4.613   5.321   -32.520 1.00 54.30  ?  76   ARG B NH1    1 
ATOM   8318  N NH2    . ARG B 2 76  ? 6.794   5.978   -32.731 1.00 53.67  ?  76   ARG B NH2    1 
ATOM   8319  H H      . ARG B 2 76  ? 5.501   4.300   -27.574 1.00 22.57  ?  76   ARG B H      1 
ATOM   8320  H HA     . ARG B 2 76  ? 3.373   5.560   -26.872 1.00 23.10  ?  76   ARG B HA     1 
ATOM   8321  H HB2    . ARG B 2 76  ? 4.320   4.743   -29.379 1.00 30.06  ?  76   ARG B HB2    1 
ATOM   8322  H HB3    . ARG B 2 76  ? 2.858   5.360   -29.295 1.00 30.06  ?  76   ARG B HB3    1 
ATOM   8323  H HG2    . ARG B 2 76  ? 3.819   7.328   -28.417 1.00 42.54  ?  76   ARG B HG2    1 
ATOM   8324  H HG3    . ARG B 2 76  ? 5.248   6.706   -28.730 1.00 42.54  ?  76   ARG B HG3    1 
ATOM   8325  H HD2    . ARG B 2 76  ? 3.506   6.822   -30.903 1.00 50.98  ?  76   ARG B HD2    1 
ATOM   8326  H HD3    . ARG B 2 76  ? 4.078   8.222   -30.414 1.00 50.98  ?  76   ARG B HD3    1 
ATOM   8327  H HE     . ARG B 2 76  ? 6.152   7.510   -30.997 1.00 58.78  ?  76   ARG B HE     1 
ATOM   8328  H HH11   . ARG B 2 76  ? 3.843   5.401   -32.146 1.00 65.16  ?  76   ARG B HH11   1 
ATOM   8329  H HH12   . ARG B 2 76  ? 4.732   4.735   -33.138 1.00 65.16  ?  76   ARG B HH12   1 
ATOM   8330  H HH21   . ARG B 2 76  ? 7.449   6.484   -32.498 1.00 64.40  ?  76   ARG B HH21   1 
ATOM   8331  H HH22   . ARG B 2 76  ? 6.904   5.390   -33.348 1.00 64.40  ?  76   ARG B HH22   1 
ATOM   8332  N N      . GLN B 2 77  ? 2.731   2.562   -27.843 1.00 16.33  ?  77   GLN B N      1 
ATOM   8333  C CA     . GLN B 2 77  ? 1.685   1.552   -27.800 1.00 16.04  ?  77   GLN B CA     1 
ATOM   8334  C C      . GLN B 2 77  ? 1.408   1.112   -26.376 1.00 17.08  ?  77   GLN B C      1 
ATOM   8335  O O      . GLN B 2 77  ? 0.263   0.804   -26.050 1.00 17.98  ?  77   GLN B O      1 
ATOM   8336  C CB     . GLN B 2 77  ? 2.054   0.331   -28.660 1.00 15.59  ?  77   GLN B CB     1 
ATOM   8337  C CG     . GLN B 2 77  ? 0.953   -0.714  -28.708 1.00 15.45  ?  77   GLN B CG     1 
ATOM   8338  C CD     . GLN B 2 77  ? -0.360  -0.187  -29.224 1.00 17.45  ?  77   GLN B CD     1 
ATOM   8339  O OE1    . GLN B 2 77  ? -0.421  0.630   -30.148 1.00 18.96  ?  77   GLN B OE1    1 
ATOM   8340  N NE2    . GLN B 2 77  ? -1.451  -0.677  -28.626 1.00 18.61  ?  77   GLN B NE2    1 
ATOM   8341  H H      . GLN B 2 77  ? 3.481   2.301   -28.175 1.00 19.59  ?  77   GLN B H      1 
ATOM   8342  H HA     . GLN B 2 77  ? 0.878   1.937   -28.176 1.00 19.25  ?  77   GLN B HA     1 
ATOM   8343  H HB2    . GLN B 2 77  ? 2.227   0.626   -29.568 1.00 18.70  ?  77   GLN B HB2    1 
ATOM   8344  H HB3    . GLN B 2 77  ? 2.847   -0.086  -28.290 1.00 18.70  ?  77   GLN B HB3    1 
ATOM   8345  H HG2    . GLN B 2 77  ? 1.233   -1.435  -29.293 1.00 18.54  ?  77   GLN B HG2    1 
ATOM   8346  H HG3    . GLN B 2 77  ? 0.805   -1.052  -27.812 1.00 18.54  ?  77   GLN B HG3    1 
ATOM   8347  H HE21   . GLN B 2 77  ? -1.372  -1.253  -27.992 1.00 22.33  ?  77   GLN B HE21   1 
ATOM   8348  H HE22   . GLN B 2 77  ? -2.231  -0.416  -28.875 1.00 22.33  ?  77   GLN B HE22   1 
ATOM   8349  N N      . ALA B 2 78  ? 2.429   1.083   -25.512 1.00 16.61  ?  78   ALA B N      1 
ATOM   8350  C CA     . ALA B 2 78  ? 2.206   0.662   -24.134 1.00 18.61  ?  78   ALA B CA     1 
ATOM   8351  C C      . ALA B 2 78  ? 1.311   1.650   -23.397 1.00 19.98  ?  78   ALA B C      1 
ATOM   8352  O O      . ALA B 2 78  ? 0.600   1.257   -22.466 1.00 22.49  ?  78   ALA B O      1 
ATOM   8353  C CB     . ALA B 2 78  ? 3.543   0.503   -23.400 1.00 19.52  ?  78   ALA B CB     1 
ATOM   8354  H H      . ALA B 2 78  ? 3.242   1.296   -25.696 1.00 19.93  ?  78   ALA B H      1 
ATOM   8355  H HA     . ALA B 2 78  ? 1.769   -0.204  -24.137 1.00 22.32  ?  78   ALA B HA     1 
ATOM   8356  H HB1    . ALA B 2 78  ? 3.376   0.154   -22.510 1.00 23.42  ?  78   ALA B HB1    1 
ATOM   8357  H HB2    . ALA B 2 78  ? 4.106   -0.112  -23.896 1.00 23.42  ?  78   ALA B HB2    1 
ATOM   8358  H HB3    . ALA B 2 78  ? 3.975   1.370   -23.338 1.00 23.42  ?  78   ALA B HB3    1 
ATOM   8359  N N      . LEU B 2 79  ? 1.326   2.926   -23.794 1.00 20.31  ?  79   LEU B N      1 
ATOM   8360  C CA     . LEU B 2 79  ? 0.455   3.903   -23.156 1.00 22.49  ?  79   LEU B CA     1 
ATOM   8361  C C      . LEU B 2 79  ? -0.986  3.803   -23.646 1.00 21.43  ?  79   LEU B C      1 
ATOM   8362  O O      . LEU B 2 79  ? -1.881  4.368   -23.004 1.00 23.65  ?  79   LEU B O      1 
ATOM   8363  C CB     . LEU B 2 79  ? 0.995   5.317   -23.368 1.00 23.31  ?  79   LEU B CB     1 
ATOM   8364  C CG     . LEU B 2 79  ? 2.370   5.603   -22.760 1.00 27.18  ?  79   LEU B CG     1 
ATOM   8365  C CD1    . LEU B 2 79  ? 2.817   7.044   -23.024 1.00 29.09  ?  79   LEU B CD1    1 
ATOM   8366  C CD2    . LEU B 2 79  ? 2.399   5.344   -21.262 1.00 28.56  ?  79   LEU B CD2    1 
ATOM   8367  H H      . LEU B 2 79  ? 1.825   3.240   -24.420 1.00 24.36  ?  79   LEU B H      1 
ATOM   8368  H HA     . LEU B 2 79  ? 0.450   3.748   -22.198 1.00 26.98  ?  79   LEU B HA     1 
ATOM   8369  H HB2    . LEU B 2 79  ? 1.064   5.476   -24.323 1.00 27.97  ?  79   LEU B HB2    1 
ATOM   8370  H HB3    . LEU B 2 79  ? 0.369   5.944   -22.972 1.00 27.97  ?  79   LEU B HB3    1 
ATOM   8371  H HG     . LEU B 2 79  ? 2.993   4.996   -23.190 1.00 32.61  ?  79   LEU B HG     1 
ATOM   8372  H HD11   . LEU B 2 79  ? 3.703   7.173   -22.651 1.00 34.90  ?  79   LEU B HD11   1 
ATOM   8373  H HD12   . LEU B 2 79  ? 2.835   7.199   -23.981 1.00 34.90  ?  79   LEU B HD12   1 
ATOM   8374  H HD13   . LEU B 2 79  ? 2.189   7.651   -22.602 1.00 34.90  ?  79   LEU B HD13   1 
ATOM   8375  H HD21   . LEU B 2 79  ? 3.228   5.691   -20.897 1.00 34.26  ?  79   LEU B HD21   1 
ATOM   8376  H HD22   . LEU B 2 79  ? 1.643   5.792   -20.850 1.00 34.26  ?  79   LEU B HD22   1 
ATOM   8377  H HD23   . LEU B 2 79  ? 2.343   4.389   -21.105 1.00 34.26  ?  79   LEU B HD23   1 
ATOM   8378  N N      . GLU B 2 80  ? -1.228  3.075   -24.738 1.00 21.43  ?  80   GLU B N      1 
ATOM   8379  C CA     . GLU B 2 80  ? -2.576  2.800   -25.222 1.00 20.88  ?  80   GLU B CA     1 
ATOM   8380  C C      . GLU B 2 80  ? -3.058  1.447   -24.699 1.00 20.63  ?  80   GLU B C      1 
ATOM   8381  O O      . GLU B 2 80  ? -4.026  1.373   -23.927 1.00 19.68  ?  80   GLU B O      1 
ATOM   8382  C CB     . GLU B 2 80  ? -2.592  2.803   -26.752 1.00 23.97  ?  80   GLU B CB     1 
ATOM   8383  C CG     . GLU B 2 80  ? -2.089  4.091   -27.401 1.00 28.18  ?  80   GLU B CG     1 
ATOM   8384  C CD     . GLU B 2 80  ? -2.928  5.299   -27.040 1.00 35.69  ?  80   GLU B CD     1 
ATOM   8385  O OE1    . GLU B 2 80  ? -4.124  5.130   -26.718 1.00 36.80  ?  80   GLU B OE1    1 
ATOM   8386  O OE2    . GLU B 2 80  ? -2.390  6.430   -27.064 1.00 39.06  -1 80   GLU B OE2    1 
ATOM   8387  H H      . GLU B 2 80  ? -0.613  2.722   -25.224 1.00 25.71  ?  80   GLU B H      1 
ATOM   8388  H HA     . GLU B 2 80  ? -3.175  3.497   -24.913 1.00 25.06  ?  80   GLU B HA     1 
ATOM   8389  H HB2    . GLU B 2 80  ? -2.026  2.079   -27.067 1.00 28.76  ?  80   GLU B HB2    1 
ATOM   8390  H HB3    . GLU B 2 80  ? -3.504  2.664   -27.050 1.00 28.76  ?  80   GLU B HB3    1 
ATOM   8391  H HG2    . GLU B 2 80  ? -1.180  4.259   -27.107 1.00 33.81  ?  80   GLU B HG2    1 
ATOM   8392  H HG3    . GLU B 2 80  ? -2.112  3.989   -28.366 1.00 33.81  ?  80   GLU B HG3    1 
ATOM   8393  N N      . LEU B 2 81  ? -2.389  0.375   -25.124 1.00 19.16  ?  81   LEU B N      1 
ATOM   8394  C CA     . LEU B 2 81  ? -2.717  -0.983  -24.692 1.00 17.06  ?  81   LEU B CA     1 
ATOM   8395  C C      . LEU B 2 81  ? -1.508  -1.870  -24.943 1.00 17.22  ?  81   LEU B C      1 
ATOM   8396  O O      . LEU B 2 81  ? -1.148  -2.119  -26.100 1.00 17.65  ?  81   LEU B O      1 
ATOM   8397  C CB     . LEU B 2 81  ? -3.930  -1.510  -25.455 1.00 17.74  ?  81   LEU B CB     1 
ATOM   8398  C CG     . LEU B 2 81  ? -4.414  -2.917  -25.093 1.00 17.92  ?  81   LEU B CG     1 
ATOM   8399  C CD1    . LEU B 2 81  ? -4.959  -2.959  -23.678 1.00 18.87  ?  81   LEU B CD1    1 
ATOM   8400  C CD2    . LEU B 2 81  ? -5.467  -3.376  -26.088 1.00 20.44  ?  81   LEU B CD2    1 
ATOM   8401  H H      . LEU B 2 81  ? -1.729  0.408   -25.674 1.00 22.99  ?  81   LEU B H      1 
ATOM   8402  H HA     . LEU B 2 81  ? -2.915  -0.984  -23.742 1.00 20.46  ?  81   LEU B HA     1 
ATOM   8403  H HB2    . LEU B 2 81  ? -4.670  -0.905  -25.295 1.00 21.28  ?  81   LEU B HB2    1 
ATOM   8404  H HB3    . LEU B 2 81  ? -3.707  -1.521  -26.399 1.00 21.28  ?  81   LEU B HB3    1 
ATOM   8405  H HG     . LEU B 2 81  ? -3.664  -3.530  -25.133 1.00 21.51  ?  81   LEU B HG     1 
ATOM   8406  H HD11   . LEU B 2 81  ? -5.250  -3.862  -23.479 1.00 22.64  ?  81   LEU B HD11   1 
ATOM   8407  H HD12   . LEU B 2 81  ? -4.258  -2.694  -23.062 1.00 22.64  ?  81   LEU B HD12   1 
ATOM   8408  H HD13   . LEU B 2 81  ? -5.708  -2.346  -23.610 1.00 22.64  ?  81   LEU B HD13   1 
ATOM   8409  H HD21   . LEU B 2 81  ? -5.773  -4.262  -25.838 1.00 24.52  ?  81   LEU B HD21   1 
ATOM   8410  H HD22   . LEU B 2 81  ? -6.210  -2.752  -26.072 1.00 24.52  ?  81   LEU B HD22   1 
ATOM   8411  H HD23   . LEU B 2 81  ? -5.075  -3.399  -26.974 1.00 24.52  ?  81   LEU B HD23   1 
ATOM   8412  N N      . ALA B 2 82  ? -0.923  -2.388  -23.867 1.00 15.84  ?  82   ALA B N      1 
ATOM   8413  C CA     . ALA B 2 82  ? 0.204   -3.305  -23.996 1.00 16.58  ?  82   ALA B CA     1 
ATOM   8414  C C      . ALA B 2 82  ? -0.241  -4.671  -24.491 1.00 15.93  ?  82   ALA B C      1 
ATOM   8415  O O      . ALA B 2 82  ? 0.454   -5.285  -25.316 1.00 15.77  ?  82   ALA B O      1 
ATOM   8416  C CB     . ALA B 2 82  ? 0.931   -3.410  -22.659 1.00 16.89  ?  82   ALA B CB     1 
ATOM   8417  H H      . ALA B 2 82  ? -1.155  -2.227  -23.055 1.00 19.01  ?  82   ALA B H      1 
ATOM   8418  H HA     . ALA B 2 82  ? 0.828   -2.955  -24.651 1.00 19.89  ?  82   ALA B HA     1 
ATOM   8419  H HB1    . ALA B 2 82  ? 1.700   -3.993  -22.762 1.00 20.26  ?  82   ALA B HB1    1 
ATOM   8420  H HB2    . ALA B 2 82  ? 1.222   -2.525  -22.387 1.00 20.26  ?  82   ALA B HB2    1 
ATOM   8421  H HB3    . ALA B 2 82  ? 0.324   -3.776  -21.997 1.00 20.26  ?  82   ALA B HB3    1 
ATOM   8422  N N      . TYR B 2 83  ? -1.396  -5.149  -24.013 1.00 14.65  ?  83   TYR B N      1 
ATOM   8423  C CA     . TYR B 2 83  ? -1.838  -6.504  -24.306 1.00 12.72  ?  83   TYR B CA     1 
ATOM   8424  C C      . TYR B 2 83  ? -3.335  -6.681  -24.100 1.00 12.28  ?  83   TYR B C      1 
ATOM   8425  O O      . TYR B 2 83  ? -3.889  -6.262  -23.085 1.00 13.70  ?  83   TYR B O      1 
ATOM   8426  C CB     . TYR B 2 83  ? -1.128  -7.540  -23.413 1.00 14.50  ?  83   TYR B CB     1 
ATOM   8427  C CG     . TYR B 2 83  ? -1.762  -8.924  -23.478 1.00 14.62  ?  83   TYR B CG     1 
ATOM   8428  C CD1    . TYR B 2 83  ? -1.407  -9.836  -24.459 1.00 13.81  ?  83   TYR B CD1    1 
ATOM   8429  C CD2    . TYR B 2 83  ? -2.730  -9.315  -22.552 1.00 14.27  ?  83   TYR B CD2    1 
ATOM   8430  C CE1    . TYR B 2 83  ? -1.993  -11.091 -24.524 1.00 13.35  ?  83   TYR B CE1    1 
ATOM   8431  C CE2    . TYR B 2 83  ? -3.321  -10.557 -22.618 1.00 15.35  ?  83   TYR B CE2    1 
ATOM   8432  C CZ     . TYR B 2 83  ? -2.954  -11.451 -23.613 1.00 13.13  ?  83   TYR B CZ     1 
ATOM   8433  O OH     . TYR B 2 83  ? -3.543  -12.688 -23.652 1.00 14.58  ?  83   TYR B OH     1 
ATOM   8434  H H      . TYR B 2 83  ? -1.938  -4.703  -23.517 1.00 17.57  ?  83   TYR B H      1 
ATOM   8435  H HA     . TYR B 2 83  ? -1.641  -6.650  -25.245 1.00 15.26  ?  83   TYR B HA     1 
ATOM   8436  H HB2    . TYR B 2 83  ? -0.205  -7.621  -23.700 1.00 17.40  ?  83   TYR B HB2    1 
ATOM   8437  H HB3    . TYR B 2 83  ? -1.164  -7.238  -22.492 1.00 17.40  ?  83   TYR B HB3    1 
ATOM   8438  H HD1    . TYR B 2 83  ? -0.762  -9.602  -25.086 1.00 16.57  ?  83   TYR B HD1    1 
ATOM   8439  H HD2    . TYR B 2 83  ? -2.980  -8.725  -21.877 1.00 17.12  ?  83   TYR B HD2    1 
ATOM   8440  H HE1    . TYR B 2 83  ? -1.734  -11.689 -25.187 1.00 16.01  ?  83   TYR B HE1    1 
ATOM   8441  H HE2    . TYR B 2 83  ? -3.967  -10.797 -21.994 1.00 18.41  ?  83   TYR B HE2    1 
ATOM   8442  H HH     . TYR B 2 83  ? -3.191  -13.156 -24.254 1.00 17.49  ?  83   TYR B HH     1 
ATOM   8443  N N      . TYR B 2 84  ? -3.960  -7.361  -25.052 1.00 13.96  ?  84   TYR B N      1 
ATOM   8444  C CA     . TYR B 2 84  ? -5.183  -8.122  -24.853 1.00 12.20  ?  84   TYR B CA     1 
ATOM   8445  C C      . TYR B 2 84  ? -5.000  -9.359  -25.729 1.00 12.41  ?  84   TYR B C      1 
ATOM   8446  O O      . TYR B 2 84  ? -4.159  -9.366  -26.633 1.00 13.57  ?  84   TYR B O      1 
ATOM   8447  C CB     . TYR B 2 84  ? -6.441  -7.318  -25.204 1.00 13.58  ?  84   TYR B CB     1 
ATOM   8448  C CG     . TYR B 2 84  ? -7.691  -8.064  -24.794 1.00 13.77  ?  84   TYR B CG     1 
ATOM   8449  C CD1    . TYR B 2 84  ? -8.042  -8.177  -23.463 1.00 13.90  ?  84   TYR B CD1    1 
ATOM   8450  C CD2    . TYR B 2 84  ? -8.488  -8.696  -25.734 1.00 13.74  ?  84   TYR B CD2    1 
ATOM   8451  C CE1    . TYR B 2 84  ? -9.166  -8.895  -23.071 1.00 15.22  ?  84   TYR B CE1    1 
ATOM   8452  C CE2    . TYR B 2 84  ? -9.610  -9.413  -25.348 1.00 13.57  ?  84   TYR B CE2    1 
ATOM   8453  C CZ     . TYR B 2 84  ? -9.948  -9.497  -24.018 1.00 13.80  ?  84   TYR B CZ     1 
ATOM   8454  O OH     . TYR B 2 84  ? -11.043 -10.229 -23.603 1.00 14.85  ?  84   TYR B OH     1 
ATOM   8455  H H      . TYR B 2 84  ? -3.679  -7.399  -25.864 1.00 16.75  ?  84   TYR B H      1 
ATOM   8456  H HA     . TYR B 2 84  ? -5.322  -8.385  -23.930 1.00 14.63  ?  84   TYR B HA     1 
ATOM   8457  H HB2    . TYR B 2 84  ? -6.422  -6.469  -24.736 1.00 16.29  ?  84   TYR B HB2    1 
ATOM   8458  H HB3    . TYR B 2 84  ? -6.472  -7.169  -26.162 1.00 16.29  ?  84   TYR B HB3    1 
ATOM   8459  H HD1    . TYR B 2 84  ? -7.515  -7.766  -22.816 1.00 16.67  ?  84   TYR B HD1    1 
ATOM   8460  H HD2    . TYR B 2 84  ? -8.267  -8.639  -26.635 1.00 16.48  ?  84   TYR B HD2    1 
ATOM   8461  H HE1    . TYR B 2 84  ? -9.386  -8.965  -22.170 1.00 18.25  ?  84   TYR B HE1    1 
ATOM   8462  H HE2    . TYR B 2 84  ? -10.134 -9.836  -25.989 1.00 16.28  ?  84   TYR B HE2    1 
ATOM   8463  H HH     . TYR B 2 84  ? -10.949 -10.457 -22.800 1.00 17.82  ?  84   TYR B HH     1 
ATOM   8464  N N      . HIS B 2 85  ? -5.744  -10.420 -25.452 1.00 13.05  ?  85   HIS B N      1 
ATOM   8465  C CA     . HIS B 2 85  ? -5.601  -11.617 -26.281 1.00 12.29  ?  85   HIS B CA     1 
ATOM   8466  C C      . HIS B 2 85  ? -6.068  -11.337 -27.705 1.00 13.44  ?  85   HIS B C      1 
ATOM   8467  O O      . HIS B 2 85  ? -6.801  -10.368 -27.974 1.00 15.03  ?  85   HIS B O      1 
ATOM   8468  C CB     . HIS B 2 85  ? -6.281  -12.825 -25.641 1.00 12.22  ?  85   HIS B CB     1 
ATOM   8469  C CG     . HIS B 2 85  ? -7.771  -12.811 -25.673 1.00 12.70  ?  85   HIS B CG     1 
ATOM   8470  N ND1    . HIS B 2 85  ? -8.487  -12.904 -26.841 1.00 13.67  ?  85   HIS B ND1    1 
ATOM   8471  C CD2    . HIS B 2 85  ? -8.683  -12.757 -24.672 1.00 14.75  ?  85   HIS B CD2    1 
ATOM   8472  C CE1    . HIS B 2 85  ? -9.780  -12.878 -26.564 1.00 15.19  ?  85   HIS B CE1    1 
ATOM   8473  N NE2    . HIS B 2 85  ? -9.922  -12.798 -25.252 1.00 15.43  ?  85   HIS B NE2    1 
ATOM   8474  H H      . HIS B 2 85  ? -6.318  -10.476 -24.815 1.00 15.66  ?  85   HIS B H      1 
ATOM   8475  H HA     . HIS B 2 85  ? -4.666  -11.868 -26.349 1.00 14.74  ?  85   HIS B HA     1 
ATOM   8476  H HB2    . HIS B 2 85  ? -5.989  -13.623 -26.109 1.00 14.67  ?  85   HIS B HB2    1 
ATOM   8477  H HB3    . HIS B 2 85  ? -6.013  -12.869 -24.710 1.00 14.67  ?  85   HIS B HB3    1 
ATOM   8478  H HD2    . HIS B 2 85  ? -8.501  -12.701 -23.762 1.00 17.69  ?  85   HIS B HD2    1 
ATOM   8479  H HE1    . HIS B 2 85  ? -10.470 -12.910 -27.186 1.00 18.23  ?  85   HIS B HE1    1 
ATOM   8480  H HE2    . HIS B 2 85  ? -10.672 -12.775 -24.831 1.00 18.52  ?  85   HIS B HE2    1 
ATOM   8481  N N      . THR B 2 86  ? -5.599  -12.173 -28.644 1.00 13.43  ?  86   THR B N      1 
ATOM   8482  C CA     . THR B 2 86  ? -6.072  -12.112 -30.032 1.00 14.53  ?  86   THR B CA     1 
ATOM   8483  C C      . THR B 2 86  ? -6.734  -13.426 -30.451 1.00 13.56  ?  86   THR B C      1 
ATOM   8484  O O      . THR B 2 86  ? -6.612  -13.884 -31.607 1.00 14.52  ?  86   THR B O      1 
ATOM   8485  C CB     . THR B 2 86  ? -4.987  -11.692 -31.024 1.00 13.26  ?  86   THR B CB     1 
ATOM   8486  O OG1    . THR B 2 86  ? -3.962  -12.685 -31.115 1.00 15.60  ?  86   THR B OG1    1 
ATOM   8487  C CG2    . THR B 2 86  ? -4.362  -10.371 -30.614 1.00 13.79  ?  86   THR B CG2    1 
ATOM   8488  H H      . THR B 2 86  ? -5.008  -12.781 -28.496 1.00 16.11  ?  86   THR B H      1 
ATOM   8489  H HA     . THR B 2 86  ? -6.745  -11.414 -30.067 1.00 17.44  ?  86   THR B HA     1 
ATOM   8490  H HB     . THR B 2 86  ? -5.399  -11.587 -31.896 1.00 15.90  ?  86   THR B HB     1 
ATOM   8491  H HG1    . THR B 2 86  ? -3.594  -12.788 -30.366 1.00 18.71  ?  86   THR B HG1    1 
ATOM   8492  H HG21   . THR B 2 86  ? -3.658  -10.130 -31.237 1.00 16.54  ?  86   THR B HG21   1 
ATOM   8493  H HG22   . THR B 2 86  ? -5.034  -9.672  -30.612 1.00 16.54  ?  86   THR B HG22   1 
ATOM   8494  H HG23   . THR B 2 86  ? -3.983  -10.445 -29.724 1.00 16.54  ?  86   THR B HG23   1 
ATOM   8495  N N      . TYR B 2 87  ? -7.449  -14.031 -29.517 1.00 13.19  ?  87   TYR B N      1 
ATOM   8496  C CA     . TYR B 2 87  ? -8.261  -15.213 -29.751 1.00 12.10  ?  87   TYR B CA     1 
ATOM   8497  C C      . TYR B 2 87  ? -9.651  -14.821 -30.250 1.00 14.75  ?  87   TYR B C      1 
ATOM   8498  O O      . TYR B 2 87  ? -10.115 -13.701 -30.046 1.00 14.54  ?  87   TYR B O      1 
ATOM   8499  C CB     . TYR B 2 87  ? -8.426  -15.991 -28.443 1.00 12.96  ?  87   TYR B CB     1 
ATOM   8500  C CG     . TYR B 2 87  ? -7.245  -16.766 -27.932 1.00 13.38  ?  87   TYR B CG     1 
ATOM   8501  C CD1    . TYR B 2 87  ? -5.976  -16.230 -27.914 1.00 14.77  ?  87   TYR B CD1    1 
ATOM   8502  C CD2    . TYR B 2 87  ? -7.416  -18.042 -27.411 1.00 14.35  ?  87   TYR B CD2    1 
ATOM   8503  C CE1    . TYR B 2 87  ? -4.903  -16.947 -27.398 1.00 15.29  ?  87   TYR B CE1    1 
ATOM   8504  C CE2    . TYR B 2 87  ? -6.359  -18.764 -26.914 1.00 14.17  ?  87   TYR B CE2    1 
ATOM   8505  C CZ     . TYR B 2 87  ? -5.102  -18.217 -26.915 1.00 13.13  ?  87   TYR B CZ     1 
ATOM   8506  O OH     . TYR B 2 87  ? -4.060  -18.968 -26.408 1.00 14.97  ?  87   TYR B OH     1 
ATOM   8507  H H      . TYR B 2 87  ? -7.482  -13.763 -28.700 1.00 15.83  ?  87   TYR B H      1 
ATOM   8508  H HA     . TYR B 2 87  ? -7.829  -15.770 -30.418 1.00 14.51  ?  87   TYR B HA     1 
ATOM   8509  H HB2    . TYR B 2 87  ? -8.664  -15.357 -27.750 1.00 15.55  ?  87   TYR B HB2    1 
ATOM   8510  H HB3    . TYR B 2 87  ? -9.145  -16.631 -28.569 1.00 15.55  ?  87   TYR B HB3    1 
ATOM   8511  H HD1    . TYR B 2 87  ? -5.835  -15.375 -28.252 1.00 17.72  ?  87   TYR B HD1    1 
ATOM   8512  H HD2    . TYR B 2 87  ? -8.267  -18.416 -27.399 1.00 17.22  ?  87   TYR B HD2    1 
ATOM   8513  H HE1    . TYR B 2 87  ? -4.054  -16.569 -27.381 1.00 18.34  ?  87   TYR B HE1    1 
ATOM   8514  H HE2    . TYR B 2 87  ? -6.496  -19.620 -26.577 1.00 16.99  ?  87   TYR B HE2    1 
ATOM   8515  H HH     . TYR B 2 87  ? -4.338  -19.727 -26.179 1.00 17.96  ?  87   TYR B HH     1 
ATOM   8516  N N      . VAL B 2 88  ? -10.314 -15.769 -30.906 1.00 14.75  ?  88   VAL B N      1 
ATOM   8517  C CA     . VAL B 2 88  ? -11.710 -15.627 -31.325 1.00 16.40  ?  88   VAL B CA     1 
ATOM   8518  C C      . VAL B 2 88  ? -11.965 -14.276 -32.000 1.00 15.12  ?  88   VAL B C      1 
ATOM   8519  O O      . VAL B 2 88  ? -12.867 -13.518 -31.604 1.00 15.51  ?  88   VAL B O      1 
ATOM   8520  C CB     . VAL B 2 88  ? -12.679 -15.856 -30.147 1.00 15.46  ?  88   VAL B CB     1 
ATOM   8521  C CG1    . VAL B 2 88  ? -14.091 -16.110 -30.635 1.00 17.17  ?  88   VAL B CG1    1 
ATOM   8522  C CG2    . VAL B 2 88  ? -12.205 -17.026 -29.293 1.00 16.67  ?  88   VAL B CG2    1 
ATOM   8523  H H      . VAL B 2 88  ? -9.969  -16.525 -31.128 1.00 17.70  ?  88   VAL B H      1 
ATOM   8524  H HA     . VAL B 2 88  ? -11.875 -16.304 -32.000 1.00 19.68  ?  88   VAL B HA     1 
ATOM   8525  H HB     . VAL B 2 88  ? -12.692 -15.053 -29.604 1.00 18.55  ?  88   VAL B HB     1 
ATOM   8526  H HG11   . VAL B 2 88  ? -14.671 -16.242 -29.869 1.00 20.60  ?  88   VAL B HG11   1 
ATOM   8527  H HG12   . VAL B 2 88  ? -14.390 -15.344 -31.149 1.00 20.60  ?  88   VAL B HG12   1 
ATOM   8528  H HG13   . VAL B 2 88  ? -14.094 -16.904 -31.193 1.00 20.60  ?  88   VAL B HG13   1 
ATOM   8529  H HG21   . VAL B 2 88  ? -12.911 -17.274 -28.676 1.00 20.00  ?  88   VAL B HG21   1 
ATOM   8530  H HG22   . VAL B 2 88  ? -11.992 -17.774 -29.872 1.00 20.00  ?  88   VAL B HG22   1 
ATOM   8531  H HG23   . VAL B 2 88  ? -11.415 -16.756 -28.799 1.00 20.00  ?  88   VAL B HG23   1 
ATOM   8532  N N      . GLY B 2 89  ? -11.173 -13.977 -33.035 1.00 14.45  ?  89   GLY B N      1 
ATOM   8533  C CA     . GLY B 2 89  ? -11.375 -12.783 -33.840 1.00 14.84  ?  89   GLY B CA     1 
ATOM   8534  C C      . GLY B 2 89  ? -11.010 -11.469 -33.185 1.00 14.12  ?  89   GLY B C      1 
ATOM   8535  O O      . GLY B 2 89  ? -11.297 -10.412 -33.757 1.00 15.48  ?  89   GLY B O      1 
ATOM   8536  H H      . GLY B 2 89  ? -10.507 -14.457 -33.291 1.00 17.33  ?  89   GLY B H      1 
ATOM   8537  H HA2    . GLY B 2 89  ? -10.842 -12.864 -34.646 1.00 17.80  ?  89   GLY B HA2    1 
ATOM   8538  H HA3    . GLY B 2 89  ? -12.313 -12.735 -34.084 1.00 17.80  ?  89   GLY B HA3    1 
ATOM   8539  N N      . HIS B 2 90  ? -10.411 -11.491 -32.001 1.00 15.28  ?  90   HIS B N      1 
ATOM   8540  C CA     . HIS B 2 90  ? -9.967  -10.255 -31.360 1.00 14.29  ?  90   HIS B CA     1 
ATOM   8541  C C      . HIS B 2 90  ? -8.600  -9.862  -31.919 1.00 13.88  ?  90   HIS B C      1 
ATOM   8542  O O      . HIS B 2 90  ? -7.758  -10.720 -32.219 1.00 14.13  ?  90   HIS B O      1 
ATOM   8543  C CB     . HIS B 2 90  ? -9.852  -10.444 -29.847 1.00 14.06  ?  90   HIS B CB     1 
ATOM   8544  C CG     . HIS B 2 90  ? -11.167 -10.523 -29.127 1.00 14.97  ?  90   HIS B CG     1 
ATOM   8545  N ND1    . HIS B 2 90  ? -11.970 -11.642 -29.146 1.00 17.23  ?  90   HIS B ND1    1 
ATOM   8546  C CD2    . HIS B 2 90  ? -11.805 -9.620  -28.346 1.00 15.80  ?  90   HIS B CD2    1 
ATOM   8547  C CE1    . HIS B 2 90  ? -13.046 -11.426 -28.410 1.00 18.04  ?  90   HIS B CE1    1 
ATOM   8548  N NE2    . HIS B 2 90  ? -12.968 -10.207 -27.901 1.00 16.52  ?  90   HIS B NE2    1 
ATOM   8549  H H      . HIS B 2 90  ? -10.249 -12.204 -31.548 1.00 18.34  ?  90   HIS B H      1 
ATOM   8550  H HA     . HIS B 2 90  ? -10.609 -9.548  -31.529 1.00 17.14  ?  90   HIS B HA     1 
ATOM   8551  H HB2    . HIS B 2 90  ? -9.373  -11.270 -29.675 1.00 16.86  ?  90   HIS B HB2    1 
ATOM   8552  H HB3    . HIS B 2 90  ? -9.361  -9.693  -29.479 1.00 16.86  ?  90   HIS B HB3    1 
ATOM   8553  H HD1    . HIS B 2 90  ? -11.798 -12.369 -29.572 1.00 20.67  ?  90   HIS B HD1    1 
ATOM   8554  H HD2    . HIS B 2 90  ? -11.511 -8.761  -28.146 1.00 18.96  ?  90   HIS B HD2    1 
ATOM   8555  H HE1    . HIS B 2 90  ? -13.741 -12.029 -28.272 1.00 21.65  ?  90   HIS B HE1    1 
ATOM   8556  N N      . SER B 2 91  ? -8.379  -8.559  -32.040 1.00 14.43  ?  91   SER B N      1 
ATOM   8557  C CA     . SER B 2 91  ? -7.167  -8.045  -32.660 1.00 14.74  ?  91   SER B CA     1 
ATOM   8558  C C      . SER B 2 91  ? -6.764  -6.735  -31.981 1.00 14.68  ?  91   SER B C      1 
ATOM   8559  O O      . SER B 2 91  ? -7.462  -6.220  -31.112 1.00 16.07  ?  91   SER B O      1 
ATOM   8560  C CB     . SER B 2 91  ? -7.387  -7.798  -34.163 1.00 17.16  ?  91   SER B CB     1 
ATOM   8561  O OG     . SER B 2 91  ? -8.448  -6.876  -34.330 1.00 17.58  ?  91   SER B OG     1 
ATOM   8562  H H      . SER B 2 91  ? -8.921  -7.949  -31.769 1.00 17.31  ?  91   SER B H      1 
ATOM   8563  H HA     . SER B 2 91  ? -6.455  -8.690  -32.533 1.00 17.69  ?  91   SER B HA     1 
ATOM   8564  H HB2    . SER B 2 91  ? -6.577  -7.432  -34.552 1.00 20.59  ?  91   SER B HB2    1 
ATOM   8565  H HB3    . SER B 2 91  ? -7.616  -8.635  -34.598 1.00 20.59  ?  91   SER B HB3    1 
ATOM   8566  H HG     . SER B 2 91  ? -9.120  -7.130  -33.895 1.00 21.09  ?  91   SER B HG     1 
ATOM   8567  N N      . ASN B 2 92  ? -5.610  -6.218  -32.379 1.00 15.53  ?  92   ASN B N      1 
ATOM   8568  C CA     . ASN B 2 92  ? -5.190  -4.861  -32.034 1.00 14.82  ?  92   ASN B CA     1 
ATOM   8569  C C      . ASN B 2 92  ? -4.668  -4.214  -33.309 1.00 15.57  ?  92   ASN B C      1 
ATOM   8570  O O      . ASN B 2 92  ? -4.318  -4.896  -34.276 1.00 15.26  ?  92   ASN B O      1 
ATOM   8571  C CB     . ASN B 2 92  ? -4.152  -4.827  -30.903 1.00 14.84  ?  92   ASN B CB     1 
ATOM   8572  C CG     . ASN B 2 92  ? -2.890  -5.603  -31.227 1.00 16.13  ?  92   ASN B CG     1 
ATOM   8573  O OD1    . ASN B 2 92  ? -1.999  -5.110  -31.934 1.00 17.17  ?  92   ASN B OD1    1 
ATOM   8574  N ND2    . ASN B 2 92  ? -2.813  -6.821  -30.723 1.00 16.47  ?  92   ASN B ND2    1 
ATOM   8575  H H      . ASN B 2 92  ? -5.039  -6.642  -32.861 1.00 18.63  ?  92   ASN B H      1 
ATOM   8576  H HA     . ASN B 2 92  ? -5.939  -4.341  -31.703 1.00 17.78  ?  92   ASN B HA     1 
ATOM   8577  H HB2    . ASN B 2 92  ? -3.901  -3.906  -30.734 1.00 17.80  ?  92   ASN B HB2    1 
ATOM   8578  H HB3    . ASN B 2 92  ? -4.544  -5.216  -30.105 1.00 17.80  ?  92   ASN B HB3    1 
ATOM   8579  H HD21   . ASN B 2 92  ? -2.119  -7.306  -30.876 1.00 19.76  ?  92   ASN B HD21   1 
ATOM   8580  H HD22   . ASN B 2 92  ? -3.456  -7.130  -30.243 1.00 19.76  ?  92   ASN B HD22   1 
ATOM   8581  N N      . GLU B 2 93  ? -4.664  -2.896  -33.334 1.00 16.37  ?  93   GLU B N      1 
ATOM   8582  C CA     . GLU B 2 93  ? -4.343  -2.188  -34.569 1.00 17.46  ?  93   GLU B CA     1 
ATOM   8583  C C      . GLU B 2 93  ? -2.922  -2.462  -35.052 1.00 17.99  ?  93   GLU B C      1 
ATOM   8584  O O      . GLU B 2 93  ? -2.747  -2.723  -36.258 1.00 18.57  ?  93   GLU B O      1 
ATOM   8585  C CB     . GLU B 2 93  ? -4.673  -0.698  -34.414 1.00 21.61  ?  93   GLU B CB     1 
ATOM   8586  C CG     . GLU B 2 93  ? -4.622  0.055   -35.708 1.00 26.85  ?  93   GLU B CG     1 
ATOM   8587  C CD     . GLU B 2 93  ? -5.423  1.349   -35.698 1.00 31.30  ?  93   GLU B CD     1 
ATOM   8588  O OE1    . GLU B 2 93  ? -6.004  1.706   -34.642 1.00 32.55  ?  93   GLU B OE1    1 
ATOM   8589  O OE2    . GLU B 2 93  ? -5.468  1.997   -36.771 1.00 32.18  -1 93   GLU B OE2    1 
ATOM   8590  H H      . GLU B 2 93  ? -4.840  -2.385  -32.665 1.00 19.64  ?  93   GLU B H      1 
ATOM   8591  H HA     . GLU B 2 93  ? -4.921  -2.509  -35.279 1.00 20.95  ?  93   GLU B HA     1 
ATOM   8592  H HB2    . GLU B 2 93  ? -5.569  -0.611  -34.053 1.00 25.93  ?  93   GLU B HB2    1 
ATOM   8593  H HB3    . GLU B 2 93  ? -4.031  -0.296  -33.809 1.00 25.93  ?  93   GLU B HB3    1 
ATOM   8594  H HG2    . GLU B 2 93  ? -3.698  0.281   -35.902 1.00 32.22  ?  93   GLU B HG2    1 
ATOM   8595  H HG3    . GLU B 2 93  ? -4.980  -0.509  -36.412 1.00 32.22  ?  93   GLU B HG3    1 
ATOM   8596  N N      . PRO B 2 94  ? -1.888  -2.433  -34.208 1.00 16.65  ?  94   PRO B N      1 
ATOM   8597  C CA     . PRO B 2 94  ? -0.556  -2.782  -34.723 1.00 15.21  ?  94   PRO B CA     1 
ATOM   8598  C C      . PRO B 2 94  ? -0.498  -4.170  -35.340 1.00 14.93  ?  94   PRO B C      1 
ATOM   8599  O O      . PRO B 2 94  ? 0.181   -4.364  -36.362 1.00 16.18  ?  94   PRO B O      1 
ATOM   8600  C CB     . PRO B 2 94  ? 0.354   -2.653  -33.490 1.00 16.74  ?  94   PRO B CB     1 
ATOM   8601  C CG     . PRO B 2 94  ? -0.380  -1.718  -32.560 1.00 18.89  ?  94   PRO B CG     1 
ATOM   8602  C CD     . PRO B 2 94  ? -1.850  -1.943  -32.813 1.00 16.80  ?  94   PRO B CD     1 
ATOM   8603  H HA     . PRO B 2 94  ? -0.279  -2.127  -35.382 1.00 18.25  ?  94   PRO B HA     1 
ATOM   8604  H HB2    . PRO B 2 94  ? 0.480   -3.523  -33.080 1.00 20.09  ?  94   PRO B HB2    1 
ATOM   8605  H HB3    . PRO B 2 94  ? 1.212   -2.282  -33.750 1.00 20.09  ?  94   PRO B HB3    1 
ATOM   8606  H HG2    . PRO B 2 94  ? -0.155  -1.928  -31.641 1.00 22.66  ?  94   PRO B HG2    1 
ATOM   8607  H HG3    . PRO B 2 94  ? -0.135  -0.801  -32.760 1.00 22.66  ?  94   PRO B HG3    1 
ATOM   8608  H HD2    . PRO B 2 94  ? -2.206  -2.609  -32.204 1.00 20.15  ?  94   PRO B HD2    1 
ATOM   8609  H HD3    . PRO B 2 94  ? -2.346  -1.114  -32.725 1.00 20.15  ?  94   PRO B HD3    1 
ATOM   8610  N N      A GLN B 2 95  ? -1.218  -5.137  -34.767 0.46 15.21  ?  95   GLN B N      1 
ATOM   8611  N N      B GLN B 2 95  ? -1.196  -5.152  -34.744 0.54 15.54  ?  95   GLN B N      1 
ATOM   8612  C CA     A GLN B 2 95  ? -1.187  -6.501  -35.285 0.46 15.49  ?  95   GLN B CA     1 
ATOM   8613  C CA     B GLN B 2 95  ? -1.196  -6.509  -35.289 0.54 16.42  ?  95   GLN B CA     1 
ATOM   8614  C C      A GLN B 2 95  ? -1.825  -6.589  -36.667 0.46 16.00  ?  95   GLN B C      1 
ATOM   8615  C C      B GLN B 2 95  ? -1.776  -6.528  -36.698 0.54 16.83  ?  95   GLN B C      1 
ATOM   8616  O O      A GLN B 2 95  ? -1.355  -7.347  -37.525 0.46 15.55  ?  95   GLN B O      1 
ATOM   8617  O O      B GLN B 2 95  ? -1.239  -7.192  -37.594 0.54 16.89  ?  95   GLN B O      1 
ATOM   8618  C CB     A GLN B 2 95  ? -1.876  -7.414  -34.276 0.46 13.80  ?  95   GLN B CB     1 
ATOM   8619  C CB     B GLN B 2 95  ? -2.010  -7.442  -34.385 0.54 16.59  ?  95   GLN B CB     1 
ATOM   8620  C CG     A GLN B 2 95  ? -2.202  -8.783  -34.779 0.46 13.15  ?  95   GLN B CG     1 
ATOM   8621  C CG     B GLN B 2 95  ? -2.018  -8.916  -34.827 0.54 17.38  ?  95   GLN B CG     1 
ATOM   8622  C CD     A GLN B 2 95  ? -3.649  -8.904  -35.167 0.46 14.92  ?  95   GLN B CD     1 
ATOM   8623  C CD     B GLN B 2 95  ? -3.115  -9.760  -34.165 0.54 17.01  ?  95   GLN B CD     1 
ATOM   8624  O OE1    A GLN B 2 95  ? -4.544  -8.801  -34.323 0.46 15.42  ?  95   GLN B OE1    1 
ATOM   8625  O OE1    B GLN B 2 95  ? -4.203  -9.265  -33.871 0.54 18.47  ?  95   GLN B OE1    1 
ATOM   8626  N NE2    A GLN B 2 95  ? -3.895  -9.089  -36.452 0.46 15.43  ?  95   GLN B NE2    1 
ATOM   8627  N NE2    B GLN B 2 95  ? -2.820  -11.048 -33.928 0.54 17.12  ?  95   GLN B NE2    1 
ATOM   8628  H H      A GLN B 2 95  ? -1.729  -5.032  -34.083 0.46 18.25  ?  95   GLN B H      1 
ATOM   8629  H H      B GLN B 2 95  ? -1.670  -5.058  -34.032 0.54 18.64  ?  95   GLN B H      1 
ATOM   8630  H HA     A GLN B 2 95  ? -0.271  -6.800  -35.390 0.46 18.58  ?  95   GLN B HA     1 
ATOM   8631  H HA     B GLN B 2 95  ? -0.281  -6.830  -35.321 0.54 19.70  ?  95   GLN B HA     1 
ATOM   8632  H HB2    A GLN B 2 95  ? -1.293  -7.518  -33.508 0.46 16.55  ?  95   GLN B HB2    1 
ATOM   8633  H HB2    B GLN B 2 95  ? -1.637  -7.407  -33.490 0.54 19.90  ?  95   GLN B HB2    1 
ATOM   8634  H HB3    A GLN B 2 95  ? -2.710  -6.999  -34.005 0.46 16.55  ?  95   GLN B HB3    1 
ATOM   8635  H HB3    B GLN B 2 95  ? -2.930  -7.135  -34.373 0.54 19.90  ?  95   GLN B HB3    1 
ATOM   8636  H HG2    A GLN B 2 95  ? -1.660  -8.974  -35.560 0.46 15.78  ?  95   GLN B HG2    1 
ATOM   8637  H HG2    B GLN B 2 95  ? -2.156  -8.952  -35.786 0.54 20.85  ?  95   GLN B HG2    1 
ATOM   8638  H HG3    A GLN B 2 95  ? -2.018  -9.432  -34.081 0.46 15.78  ?  95   GLN B HG3    1 
ATOM   8639  H HG3    B GLN B 2 95  ? -1.163  -9.313  -34.600 0.54 20.85  ?  95   GLN B HG3    1 
ATOM   8640  H HE21   A GLN B 2 95  ? -3.245  -9.133  -37.013 0.46 18.51  ?  95   GLN B HE21   1 
ATOM   8641  H HE21   B GLN B 2 95  ? -2.049  -11.360 -34.145 0.54 20.54  ?  95   GLN B HE21   1 
ATOM   8642  H HE22   A GLN B 2 95  ? -4.707  -9.164  -36.728 0.46 18.51  ?  95   GLN B HE22   1 
ATOM   8643  H HE22   B GLN B 2 95  ? -3.403  -11.561 -33.558 0.54 20.54  ?  95   GLN B HE22   1 
ATOM   8644  N N      . ILE B 2 96  ? -2.881  -5.811  -36.907 1.00 16.40  ?  96   ILE B N      1 
ATOM   8645  C CA     . ILE B 2 96  ? -3.518  -5.782  -38.219 1.00 15.42  ?  96   ILE B CA     1 
ATOM   8646  C C      . ILE B 2 96  ? -2.567  -5.184  -39.243 1.00 15.85  ?  96   ILE B C      1 
ATOM   8647  O O      . ILE B 2 96  ? -2.344  -5.748  -40.325 1.00 16.34  ?  96   ILE B O      1 
ATOM   8648  C CB     . ILE B 2 96  ? -4.838  -4.996  -38.143 1.00 15.43  ?  96   ILE B CB     1 
ATOM   8649  C CG1    . ILE B 2 96  ? -5.798  -5.641  -37.169 1.00 15.50  ?  96   ILE B CG1    1 
ATOM   8650  C CG2    . ILE B 2 96  ? -5.461  -4.893  -39.541 1.00 16.58  ?  96   ILE B CG2    1 
ATOM   8651  C CD1    . ILE B 2 96  ? -7.030  -4.793  -36.862 1.00 15.41  ?  96   ILE B CD1    1 
ATOM   8652  H H      A ILE B 2 96  ? -3.247  -5.290  -36.328 0.46 19.67  ?  96   ILE B H      1 
ATOM   8653  H H      B ILE B 2 96  ? -3.278  -5.335  -36.310 0.54 19.67  ?  96   ILE B H      1 
ATOM   8654  H HA     . ILE B 2 96  ? -3.724  -6.689  -38.494 1.00 18.50  ?  96   ILE B HA     1 
ATOM   8655  H HB     . ILE B 2 96  ? -4.646  -4.102  -37.817 1.00 18.52  ?  96   ILE B HB     1 
ATOM   8656  H HG12   . ILE B 2 96  ? -6.105  -6.481  -37.545 1.00 18.60  ?  96   ILE B HG12   1 
ATOM   8657  H HG13   . ILE B 2 96  ? -5.333  -5.801  -36.333 1.00 18.60  ?  96   ILE B HG13   1 
ATOM   8658  H HG21   . ILE B 2 96  ? -6.373  -4.574  -39.457 1.00 19.89  ?  96   ILE B HG21   1 
ATOM   8659  H HG22   . ILE B 2 96  ? -4.941  -4.272  -40.074 1.00 19.89  ?  96   ILE B HG22   1 
ATOM   8660  H HG23   . ILE B 2 96  ? -5.455  -5.770  -39.954 1.00 19.89  ?  96   ILE B HG23   1 
ATOM   8661  H HD11   . ILE B 2 96  ? -7.479  -5.159  -36.084 1.00 18.48  ?  96   ILE B HD11   1 
ATOM   8662  H HD12   . ILE B 2 96  ? -6.749  -3.882  -36.683 1.00 18.48  ?  96   ILE B HD12   1 
ATOM   8663  H HD13   . ILE B 2 96  ? -7.625  -4.812  -37.627 1.00 18.48  ?  96   ILE B HD13   1 
ATOM   8664  N N      . GLN B 2 97  ? -1.980  -4.033  -38.899 1.00 16.16  ?  97   GLN B N      1 
ATOM   8665  C CA     . GLN B 2 97  ? -1.047  -3.357  -39.791 1.00 16.49  ?  97   GLN B CA     1 
ATOM   8666  C C      . GLN B 2 97  ? 0.153   -4.243  -40.090 1.00 16.43  ?  97   GLN B C      1 
ATOM   8667  O O      . GLN B 2 97  ? 0.626   -4.283  -41.234 1.00 16.94  ?  97   GLN B O      1 
ATOM   8668  C CB     . GLN B 2 97  ? -0.592  -2.034  -39.179 1.00 17.81  ?  97   GLN B CB     1 
ATOM   8669  C CG     . GLN B 2 97  ? -1.699  -1.007  -39.069 1.00 20.55  ?  97   GLN B CG     1 
ATOM   8670  C CD     . GLN B 2 97  ? -1.336  0.184   -38.200 1.00 26.00  ?  97   GLN B CD     1 
ATOM   8671  O OE1    . GLN B 2 97  ? -0.489  0.092   -37.318 1.00 30.29  ?  97   GLN B OE1    1 
ATOM   8672  N NE2    . GLN B 2 97  ? -1.999  1.306   -38.436 1.00 29.85  ?  97   GLN B NE2    1 
ATOM   8673  H H      . GLN B 2 97  ? -2.105  -3.623  -38.154 1.00 19.39  ?  97   GLN B H      1 
ATOM   8674  H HA     . GLN B 2 97  ? -1.500  -3.159  -40.626 1.00 19.79  ?  97   GLN B HA     1 
ATOM   8675  H HB2    . GLN B 2 97  ? -0.253  -2.203  -38.286 1.00 21.37  ?  97   GLN B HB2    1 
ATOM   8676  H HB3    . GLN B 2 97  ? 0.109   -1.657  -39.734 1.00 21.37  ?  97   GLN B HB3    1 
ATOM   8677  H HG2    . GLN B 2 97  ? -1.907  -0.674  -39.956 1.00 24.66  ?  97   GLN B HG2    1 
ATOM   8678  H HG3    . GLN B 2 97  ? -2.481  -1.430  -38.682 1.00 24.66  ?  97   GLN B HG3    1 
ATOM   8679  H HE21   . GLN B 2 97  ? -2.596  1.330   -39.054 1.00 35.82  ?  97   GLN B HE21   1 
ATOM   8680  H HE22   . GLN B 2 97  ? -1.831  2.010   -37.972 1.00 35.82  ?  97   GLN B HE22   1 
ATOM   8681  N N      . LEU B 2 98  ? 0.649   -4.971  -39.084 1.00 15.25  ?  98   LEU B N      1 
ATOM   8682  C CA     . LEU B 2 98  ? 1.854   -5.772  -39.306 1.00 14.91  ?  98   LEU B CA     1 
ATOM   8683  C C      . LEU B 2 98  ? 1.561   -6.975  -40.197 1.00 15.73  ?  98   LEU B C      1 
ATOM   8684  O O      . LEU B 2 98  ? 2.402   -7.364  -41.016 1.00 15.68  ?  98   LEU B O      1 
ATOM   8685  C CB     . LEU B 2 98  ? 2.466   -6.199  -37.965 1.00 15.30  ?  98   LEU B CB     1 
ATOM   8686  C CG     . LEU B 2 98  ? 3.779   -6.964  -38.068 1.00 15.89  ?  98   LEU B CG     1 
ATOM   8687  C CD1    . LEU B 2 98  ? 4.870   -6.155  -38.757 1.00 16.19  ?  98   LEU B CD1    1 
ATOM   8688  C CD2    . LEU B 2 98  ? 4.221   -7.421  -36.674 1.00 16.00  ?  98   LEU B CD2    1 
ATOM   8689  H H      . LEU B 2 98  ? 0.319   -5.018  -38.291 1.00 18.30  ?  98   LEU B H      1 
ATOM   8690  H HA     . LEU B 2 98  ? 2.516   -5.227  -39.759 1.00 17.89  ?  98   LEU B HA     1 
ATOM   8691  H HB2    . LEU B 2 98  ? 2.634   -5.402  -37.438 1.00 18.35  ?  98   LEU B HB2    1 
ATOM   8692  H HB3    . LEU B 2 98  ? 1.831   -6.772  -37.507 1.00 18.35  ?  98   LEU B HB3    1 
ATOM   8693  H HG     . LEU B 2 98  ? 3.638   -7.746  -38.625 1.00 19.06  ?  98   LEU B HG     1 
ATOM   8694  H HD11   . LEU B 2 98  ? 5.709   -6.637  -38.692 1.00 19.42  ?  98   LEU B HD11   1 
ATOM   8695  H HD12   . LEU B 2 98  ? 4.630   -6.031  -39.688 1.00 19.42  ?  98   LEU B HD12   1 
ATOM   8696  H HD13   . LEU B 2 98  ? 4.949   -5.294  -38.318 1.00 19.42  ?  98   LEU B HD13   1 
ATOM   8697  H HD21   . LEU B 2 98  ? 4.988   -8.008  -36.762 1.00 19.19  ?  98   LEU B HD21   1 
ATOM   8698  H HD22   . LEU B 2 98  ? 4.460   -6.642  -36.147 1.00 19.19  ?  98   LEU B HD22   1 
ATOM   8699  H HD23   . LEU B 2 98  ? 3.488   -7.894  -36.250 1.00 19.19  ?  98   LEU B HD23   1 
ATOM   8700  N N      . SER B 2 99  ? 0.381   -7.578  -40.061 1.00 14.54  ?  99   SER B N      1 
ATOM   8701  C CA     . SER B 2 99  ? 0.026   -8.667  -40.963 1.00 13.41  ?  99   SER B CA     1 
ATOM   8702  C C      . SER B 2 99  ? 0.068   -8.196  -42.414 1.00 15.85  ?  99   SER B C      1 
ATOM   8703  O O      . SER B 2 99  ? 0.630   -8.880  -43.283 1.00 15.59  ?  99   SER B O      1 
ATOM   8704  C CB     . SER B 2 99  ? -1.348  -9.212  -40.598 1.00 14.94  ?  99   SER B CB     1 
ATOM   8705  O OG     . SER B 2 99  ? -1.262  -9.909  -39.369 1.00 15.13  ?  99   SER B OG     1 
ATOM   8706  H H      . SER B 2 99  ? -0.215  -7.382  -39.473 1.00 17.45  ?  99   SER B H      1 
ATOM   8707  H HA     . SER B 2 99  ? 0.662   -9.392  -40.866 1.00 16.09  ?  99   SER B HA     1 
ATOM   8708  H HB2    . SER B 2 99  ? -1.973  -8.476  -40.507 1.00 17.93  ?  99   SER B HB2    1 
ATOM   8709  H HB3    . SER B 2 99  ? -1.649  -9.819  -41.292 1.00 17.93  ?  99   SER B HB3    1 
ATOM   8710  H HG     . SER B 2 99  ? -2.015  -10.215 -39.159 1.00 18.15  ?  99   SER B HG     1 
ATOM   8711  N N      . GLU B 2 100 ? -0.505  -7.024  -42.680 1.00 15.96  ?  100  GLU B N      1 
ATOM   8712  C CA     . GLU B 2 100 ? -0.462  -6.454  -44.019 1.00 15.41  ?  100  GLU B CA     1 
ATOM   8713  C C      . GLU B 2 100 ? 0.980   -6.258  -44.487 1.00 17.04  ?  100  GLU B C      1 
ATOM   8714  O O      . GLU B 2 100 ? 1.329   -6.621  -45.618 1.00 17.11  ?  100  GLU B O      1 
ATOM   8715  C CB     . GLU B 2 100 ? -1.231  -5.128  -44.030 1.00 15.57  ?  100  GLU B CB     1 
ATOM   8716  C CG     . GLU B 2 100 ? -2.712  -5.302  -43.786 1.00 16.56  ?  100  GLU B CG     1 
ATOM   8717  C CD     . GLU B 2 100 ? -3.465  -3.985  -43.688 1.00 19.01  ?  100  GLU B CD     1 
ATOM   8718  O OE1    . GLU B 2 100 ? -2.836  -2.946  -43.401 1.00 20.85  ?  100  GLU B OE1    1 
ATOM   8719  O OE2    . GLU B 2 100 ? -4.701  -4.007  -43.889 1.00 19.08  -1 100  GLU B OE2    1 
ATOM   8720  H H      . GLU B 2 100 ? -0.924  -6.540  -42.105 1.00 19.15  ?  100  GLU B H      1 
ATOM   8721  H HA     . GLU B 2 100 ? -0.891  -7.061  -44.642 1.00 18.49  ?  100  GLU B HA     1 
ATOM   8722  H HB2    . GLU B 2 100 ? -0.879  -4.554  -43.332 1.00 18.69  ?  100  GLU B HB2    1 
ATOM   8723  H HB3    . GLU B 2 100 ? -1.118  -4.706  -44.896 1.00 18.69  ?  100  GLU B HB3    1 
ATOM   8724  H HG2    . GLU B 2 100 ? -3.094  -5.808  -44.520 1.00 19.87  ?  100  GLU B HG2    1 
ATOM   8725  H HG3    . GLU B 2 100 ? -2.839  -5.780  -42.952 1.00 19.87  ?  100  GLU B HG3    1 
ATOM   8726  N N      . LYS B 2 101 ? 1.829   -5.680  -43.639 1.00 16.71  ?  101  LYS B N      1 
ATOM   8727  C CA     . LYS B 2 101 ? 3.204   -5.401  -44.049 1.00 17.00  ?  101  LYS B CA     1 
ATOM   8728  C C      . LYS B 2 101 ? 3.976   -6.696  -44.305 1.00 16.01  ?  101  LYS B C      1 
ATOM   8729  O O      . LYS B 2 101 ? 4.769   -6.782  -45.258 1.00 17.11  ?  101  LYS B O      1 
ATOM   8730  C CB     . LYS B 2 101 ? 3.923   -4.582  -42.970 1.00 17.62  ?  101  LYS B CB     1 
ATOM   8731  C CG     . LYS B 2 101 ? 3.416   -3.180  -42.733 1.00 22.65  ?  101  LYS B CG     1 
ATOM   8732  C CD     . LYS B 2 101 ? 3.699   -2.295  -43.929 1.00 26.29  ?  101  LYS B CD     1 
ATOM   8733  C CE     . LYS B 2 101 ? 3.432   -0.838  -43.590 1.00 29.45  ?  101  LYS B CE     1 
ATOM   8734  N NZ     . LYS B 2 101 ? 3.612   -0.023  -44.801 1.00 33.15  ?  101  LYS B NZ     1 
ATOM   8735  H H      . LYS B 2 101 ? 1.641   -5.443  -42.834 1.00 20.05  ?  101  LYS B H      1 
ATOM   8736  H HA     . LYS B 2 101 ? 3.179   -4.882  -44.868 1.00 20.40  ?  101  LYS B HA     1 
ATOM   8737  H HB2    . LYS B 2 101 ? 3.844   -5.058  -42.129 1.00 21.15  ?  101  LYS B HB2    1 
ATOM   8738  H HB3    . LYS B 2 101 ? 4.857   -4.507  -43.222 1.00 21.15  ?  101  LYS B HB3    1 
ATOM   8739  H HG2    . LYS B 2 101 ? 2.457   -3.202  -42.588 1.00 27.18  ?  101  LYS B HG2    1 
ATOM   8740  H HG3    . LYS B 2 101 ? 3.860   -2.801  -41.958 1.00 27.18  ?  101  LYS B HG3    1 
ATOM   8741  H HD2    . LYS B 2 101 ? 4.630   -2.387  -44.188 1.00 31.54  ?  101  LYS B HD2    1 
ATOM   8742  H HD3    . LYS B 2 101 ? 3.124   -2.551  -44.666 1.00 31.54  ?  101  LYS B HD3    1 
ATOM   8743  H HE2    . LYS B 2 101 ? 2.522   -0.734  -43.272 1.00 35.34  ?  101  LYS B HE2    1 
ATOM   8744  H HE3    . LYS B 2 101 ? 4.057   -0.537  -42.912 1.00 35.34  ?  101  LYS B HE3    1 
ATOM   8745  H HZ1    . LYS B 2 101 ? 3.462   0.834   -44.616 1.00 39.78  ?  101  LYS B HZ1    1 
ATOM   8746  H HZ2    . LYS B 2 101 ? 4.443   -0.111  -45.107 1.00 39.78  ?  101  LYS B HZ2    1 
ATOM   8747  H HZ3    . LYS B 2 101 ? 3.043   -0.287  -45.432 1.00 39.78  ?  101  LYS B HZ3    1 
ATOM   8748  N N      . ILE B 2 102 ? 3.797   -7.696  -43.436 1.00 15.55  ?  102  ILE B N      1 
ATOM   8749  C CA     . ILE B 2 102 ? 4.477   -8.972  -43.620 1.00 15.12  ?  102  ILE B CA     1 
ATOM   8750  C C      . ILE B 2 102 ? 4.089   -9.601  -44.946 1.00 14.51  ?  102  ILE B C      1 
ATOM   8751  O O      . ILE B 2 102 ? 4.941   -10.076 -45.693 1.00 16.71  ?  102  ILE B O      1 
ATOM   8752  C CB     . ILE B 2 102 ? 4.173   -9.927  -42.452 1.00 14.67  ?  102  ILE B CB     1 
ATOM   8753  C CG1    . ILE B 2 102 ? 4.847   -9.448  -41.183 1.00 14.88  ?  102  ILE B CG1    1 
ATOM   8754  C CG2    . ILE B 2 102 ? 4.634   -11.355 -42.801 1.00 16.47  ?  102  ILE B CG2    1 
ATOM   8755  C CD1    . ILE B 2 102 ? 4.406   -10.175 -39.920 1.00 14.79  ?  102  ILE B CD1    1 
ATOM   8756  H H      . ILE B 2 102 ? 3.293   -7.659  -42.740 1.00 18.66  ?  102  ILE B H      1 
ATOM   8757  H HA     . ILE B 2 102 ? 5.431   -8.800  -43.632 1.00 18.14  ?  102  ILE B HA     1 
ATOM   8758  H HB     . ILE B 2 102 ? 3.214   -9.934  -42.304 1.00 17.60  ?  102  ILE B HB     1 
ATOM   8759  H HG12   . ILE B 2 102 ? 5.805   -9.575  -41.275 1.00 17.86  ?  102  ILE B HG12   1 
ATOM   8760  H HG13   . ILE B 2 102 ? 4.648   -8.506  -41.064 1.00 17.86  ?  102  ILE B HG13   1 
ATOM   8761  H HG21   . ILE B 2 102 ? 4.603   -11.901 -42.000 1.00 19.77  ?  102  ILE B HG21   1 
ATOM   8762  H HG22   . ILE B 2 102 ? 4.041   -11.723 -43.474 1.00 19.77  ?  102  ILE B HG22   1 
ATOM   8763  H HG23   . ILE B 2 102 ? 5.541   -11.320 -43.143 1.00 19.77  ?  102  ILE B HG23   1 
ATOM   8764  H HD11   . ILE B 2 102 ? 4.771   -9.717  -39.147 1.00 17.74  ?  102  ILE B HD11   1 
ATOM   8765  H HD12   . ILE B 2 102 ? 3.437   -10.175 -39.878 1.00 17.74  ?  102  ILE B HD12   1 
ATOM   8766  H HD13   . ILE B 2 102 ? 4.735   -11.087 -39.950 1.00 17.74  ?  102  ILE B HD13   1 
ATOM   8767  N N      . LEU B 2 103 ? 2.794   -9.639  -45.247 1.00 14.55  ?  103  LEU B N      1 
ATOM   8768  C CA     . LEU B 2 103 ? 2.355   -10.268 -46.484 1.00 16.22  ?  103  LEU B CA     1 
ATOM   8769  C C      . LEU B 2 103 ? 2.839   -9.502  -47.706 1.00 18.00  ?  103  LEU B C      1 
ATOM   8770  O O      . LEU B 2 103 ? 3.161   -10.118 -48.734 1.00 19.97  ?  103  LEU B O      1 
ATOM   8771  C CB     . LEU B 2 103 ? 0.836   -10.420 -46.467 1.00 15.91  ?  103  LEU B CB     1 
ATOM   8772  C CG     . LEU B 2 103 ? 0.349   -11.479 -45.485 1.00 16.62  ?  103  LEU B CG     1 
ATOM   8773  C CD1    . LEU B 2 103 ? -1.131  -11.243 -45.221 1.00 17.55  ?  103  LEU B CD1    1 
ATOM   8774  C CD2    . LEU B 2 103 ? 0.621   -12.908 -45.964 1.00 17.63  ?  103  LEU B CD2    1 
ATOM   8775  H H      . LEU B 2 103 ? 2.162   -9.315  -44.763 1.00 17.45  ?  103  LEU B H      1 
ATOM   8776  H HA     . LEU B 2 103 ? 2.732   -11.159 -46.550 1.00 19.47  ?  103  LEU B HA     1 
ATOM   8777  H HB2    . LEU B 2 103 ? 0.439   -9.572  -46.213 1.00 19.08  ?  103  LEU B HB2    1 
ATOM   8778  H HB3    . LEU B 2 103 ? 0.537   -10.675 -47.354 1.00 19.08  ?  103  LEU B HB3    1 
ATOM   8779  H HG     . LEU B 2 103 ? 0.844   -11.400 -44.655 1.00 19.94  ?  103  LEU B HG     1 
ATOM   8780  H HD11   . LEU B 2 103 ? -1.464  -11.945 -44.640 1.00 21.05  ?  103  LEU B HD11   1 
ATOM   8781  H HD12   . LEU B 2 103 ? -1.242  -10.380 -44.794 1.00 21.05  ?  103  LEU B HD12   1 
ATOM   8782  H HD13   . LEU B 2 103 ? -1.609  -11.259 -46.065 1.00 21.05  ?  103  LEU B HD13   1 
ATOM   8783  H HD21   . LEU B 2 103 ? 0.214   -13.532 -45.343 1.00 21.16  ?  103  LEU B HD21   1 
ATOM   8784  H HD22   . LEU B 2 103 ? 0.238   -13.023 -46.848 1.00 21.16  ?  103  LEU B HD22   1 
ATOM   8785  H HD23   . LEU B 2 103 ? 1.580   -13.052 -45.997 1.00 21.16  ?  103  LEU B HD23   1 
ATOM   8786  N N      . GLU B 2 104 ? 2.903   -8.175  -47.612 1.00 17.63  ?  104  GLU B N      1 
ATOM   8787  C CA     . GLU B 2 104 ? 3.423   -7.371  -48.707 1.00 18.24  ?  104  GLU B CA     1 
ATOM   8788  C C      . GLU B 2 104 ? 4.857   -7.758  -49.025 1.00 18.56  ?  104  GLU B C      1 
ATOM   8789  O O      . GLU B 2 104 ? 5.249   -7.823  -50.201 1.00 19.82  ?  104  GLU B O      1 
ATOM   8790  C CB     . GLU B 2 104 ? 3.344   -5.885  -48.341 1.00 21.65  ?  104  GLU B CB     1 
ATOM   8791  C CG     . GLU B 2 104 ? 3.992   -4.974  -49.354 1.00 31.53  ?  104  GLU B CG     1 
ATOM   8792  C CD     . GLU B 2 104 ? 3.786   -3.507  -49.046 1.00 36.98  ?  104  GLU B CD     1 
ATOM   8793  O OE1    . GLU B 2 104 ? 3.714   -3.141  -47.853 1.00 38.50  ?  104  GLU B OE1    1 
ATOM   8794  O OE2    . GLU B 2 104 ? 3.690   -2.719  -50.017 1.00 41.57  -1 104  GLU B OE2    1 
ATOM   8795  H H      . GLU B 2 104 ? 2.653   -7.717  -46.929 1.00 21.15  ?  104  GLU B H      1 
ATOM   8796  H HA     . GLU B 2 104 ? 2.881   -7.521  -49.497 1.00 21.89  ?  104  GLU B HA     1 
ATOM   8797  H HB2    . GLU B 2 104 ? 2.410   -5.631  -48.269 1.00 25.98  ?  104  GLU B HB2    1 
ATOM   8798  H HB3    . GLU B 2 104 ? 3.791   -5.749  -47.492 1.00 25.98  ?  104  GLU B HB3    1 
ATOM   8799  H HG2    . GLU B 2 104 ? 4.946   -5.146  -49.367 1.00 37.83  ?  104  GLU B HG2    1 
ATOM   8800  H HG3    . GLU B 2 104 ? 3.611   -5.153  -50.228 1.00 37.83  ?  104  GLU B HG3    1 
ATOM   8801  N N      . LEU B 2 105 ? 5.661   -8.000  -47.987 1.00 16.60  ?  105  LEU B N      1 
ATOM   8802  C CA     . LEU B 2 105 ? 7.052   -8.386  -48.195 1.00 15.98  ?  105  LEU B CA     1 
ATOM   8803  C C      . LEU B 2 105 ? 7.171   -9.820  -48.701 1.00 17.30  ?  105  LEU B C      1 
ATOM   8804  O O      . LEU B 2 105 ? 8.001   -10.102 -49.568 1.00 18.26  ?  105  LEU B O      1 
ATOM   8805  C CB     . LEU B 2 105 ? 7.826   -8.204  -46.890 1.00 16.60  ?  105  LEU B CB     1 
ATOM   8806  C CG     . LEU B 2 105 ? 8.111   -6.747  -46.534 1.00 19.42  ?  105  LEU B CG     1 
ATOM   8807  C CD1    . LEU B 2 105 ? 8.390   -6.596  -45.067 1.00 20.79  ?  105  LEU B CD1    1 
ATOM   8808  C CD2    . LEU B 2 105 ? 9.282   -6.208  -47.367 1.00 21.83  ?  105  LEU B CD2    1 
ATOM   8809  H H      . LEU B 2 105 ? 5.429   -7.948  -47.160 1.00 19.92  ?  105  LEU B H      1 
ATOM   8810  H HA     . LEU B 2 105 ? 7.443   -7.810  -48.871 1.00 19.17  ?  105  LEU B HA     1 
ATOM   8811  H HB2    . LEU B 2 105 ? 7.308   -8.590  -46.166 1.00 19.92  ?  105  LEU B HB2    1 
ATOM   8812  H HB3    . LEU B 2 105 ? 8.678   -8.662  -46.969 1.00 19.92  ?  105  LEU B HB3    1 
ATOM   8813  H HG     . LEU B 2 105 ? 7.325   -6.217  -46.740 1.00 23.30  ?  105  LEU B HG     1 
ATOM   8814  H HD11   . LEU B 2 105 ? 8.561   -5.661  -44.873 1.00 24.94  ?  105  LEU B HD11   1 
ATOM   8815  H HD12   . LEU B 2 105 ? 7.618   -6.902  -44.566 1.00 24.94  ?  105  LEU B HD12   1 
ATOM   8816  H HD13   . LEU B 2 105 ? 9.167   -7.129  -44.837 1.00 24.94  ?  105  LEU B HD13   1 
ATOM   8817  H HD21   . LEU B 2 105 ? 9.455   -5.289  -47.111 1.00 26.19  ?  105  LEU B HD21   1 
ATOM   8818  H HD22   . LEU B 2 105 ? 10.067  -6.752  -47.196 1.00 26.19  ?  105  LEU B HD22   1 
ATOM   8819  H HD23   . LEU B 2 105 ? 9.048   -6.252  -48.307 1.00 26.19  ?  105  LEU B HD23   1 
ATOM   8820  N N      . ALA B 2 106 ? 6.376   -10.741 -48.152 1.00 17.63  ?  106  ALA B N      1 
ATOM   8821  C CA     . ALA B 2 106 ? 6.519   -12.153 -48.508 1.00 17.47  ?  106  ALA B CA     1 
ATOM   8822  C C      . ALA B 2 106 ? 6.127   -12.391 -49.953 1.00 19.63  ?  106  ALA B C      1 
ATOM   8823  O O      . ALA B 2 106 ? 6.738   -13.215 -50.638 1.00 21.33  ?  106  ALA B O      1 
ATOM   8824  C CB     . ALA B 2 106 ? 5.649   -13.020 -47.594 1.00 18.95  ?  106  ALA B CB     1 
ATOM   8825  H H      . ALA B 2 106 ? 5.755   -10.580 -47.580 1.00 21.16  ?  106  ALA B H      1 
ATOM   8826  H HA     . ALA B 2 106 ? 7.446   -12.409 -48.386 1.00 20.96  ?  106  ALA B HA     1 
ATOM   8827  H HB1    . ALA B 2 106 ? 5.789   -13.953 -47.817 1.00 22.73  ?  106  ALA B HB1    1 
ATOM   8828  H HB2    . ALA B 2 106 ? 5.901   -12.859 -46.672 1.00 22.73  ?  106  ALA B HB2    1 
ATOM   8829  H HB3    . ALA B 2 106 ? 4.717   -12.784 -47.728 1.00 22.73  ?  106  ALA B HB3    1 
ATOM   8830  N N      . GLY B 2 107 ? 5.104   -11.684 -50.427 1.00 19.75  ?  107  GLY B N      1 
ATOM   8831  C CA     . GLY B 2 107 ? 4.779   -11.684 -51.828 1.00 22.65  ?  107  GLY B CA     1 
ATOM   8832  C C      . GLY B 2 107 ? 3.518   -12.447 -52.150 1.00 24.90  ?  107  GLY B C      1 
ATOM   8833  O O      . GLY B 2 107 ? 2.908   -13.106 -51.312 1.00 22.89  ?  107  GLY B O      1 
ATOM   8834  H H      . GLY B 2 107 ? 4.586   -11.195 -49.944 1.00 23.69  ?  107  GLY B H      1 
ATOM   8835  H HA2    . GLY B 2 107 ? 4.662   -10.768 -52.126 1.00 27.18  ?  107  GLY B HA2    1 
ATOM   8836  H HA3    . GLY B 2 107 ? 5.509   -12.087 -52.323 1.00 27.18  ?  107  GLY B HA3    1 
ATOM   8837  N N      . PRO B 2 108 ? 3.094   -12.349 -53.401 1.00 28.82  ?  108  PRO B N      1 
ATOM   8838  C CA     . PRO B 2 108 ? 1.856   -13.020 -53.804 1.00 32.81  ?  108  PRO B CA     1 
ATOM   8839  C C      . PRO B 2 108 ? 1.955   -14.523 -53.584 1.00 32.42  ?  108  PRO B C      1 
ATOM   8840  O O      . PRO B 2 108 ? 3.030   -15.127 -53.683 1.00 32.95  ?  108  PRO B O      1 
ATOM   8841  C CB     . PRO B 2 108 ? 1.717   -12.667 -55.287 1.00 36.29  ?  108  PRO B CB     1 
ATOM   8842  C CG     . PRO B 2 108 ? 3.082   -12.195 -55.720 1.00 37.50  ?  108  PRO B CG     1 
ATOM   8843  C CD     . PRO B 2 108 ? 3.753   -11.628 -54.506 1.00 34.05  ?  108  PRO B CD     1 
ATOM   8844  H HA     . PRO B 2 108 ? 1.093   -12.667 -53.321 1.00 39.37  ?  108  PRO B HA     1 
ATOM   8845  H HB2    . PRO B 2 108 ? 1.449   -13.453 -55.788 1.00 43.54  ?  108  PRO B HB2    1 
ATOM   8846  H HB3    . PRO B 2 108 ? 1.058   -11.964 -55.396 1.00 43.54  ?  108  PRO B HB3    1 
ATOM   8847  H HG2    . PRO B 2 108 ? 3.588   -12.946 -56.068 1.00 45.00  ?  108  PRO B HG2    1 
ATOM   8848  H HG3    . PRO B 2 108 ? 2.986   -11.514 -56.404 1.00 45.00  ?  108  PRO B HG3    1 
ATOM   8849  H HD2    . PRO B 2 108 ? 4.706   -11.811 -54.520 1.00 40.85  ?  108  PRO B HD2    1 
ATOM   8850  H HD3    . PRO B 2 108 ? 3.599   -10.673 -54.439 1.00 40.85  ?  108  PRO B HD3    1 
ATOM   8851  N N      . GLY B 2 109 ? 0.819   -15.121 -53.245 1.00 29.51  ?  109  GLY B N      1 
ATOM   8852  C CA     . GLY B 2 109 ? 0.757   -16.517 -52.900 1.00 26.70  ?  109  GLY B CA     1 
ATOM   8853  C C      . GLY B 2 109 ? 0.669   -16.764 -51.413 1.00 20.50  ?  109  GLY B C      1 
ATOM   8854  O O      . GLY B 2 109 ? 0.202   -17.828 -51.001 1.00 20.32  ?  109  GLY B O      1 
ATOM   8855  H H      . GLY B 2 109 ? 0.059   -14.720 -53.210 1.00 35.41  ?  109  GLY B H      1 
ATOM   8856  H HA2    . GLY B 2 109 ? -0.024  -16.912 -53.318 1.00 32.03  ?  109  GLY B HA2    1 
ATOM   8857  H HA3    . GLY B 2 109 ? 1.553   -16.961 -53.233 1.00 32.03  ?  109  GLY B HA3    1 
ATOM   8858  N N      . MET B 2 110 ? 1.085   -15.800 -50.607 1.00 18.04  ?  110  MET B N      1 
ATOM   8859  C CA     . MET B 2 110 ? 0.959   -15.872 -49.167 1.00 15.65  ?  110  MET B CA     1 
ATOM   8860  C C      . MET B 2 110 ? -0.326  -15.184 -48.750 1.00 16.29  ?  110  MET B C      1 
ATOM   8861  O O      . MET B 2 110 ? -0.697  -14.137 -49.300 1.00 18.38  ?  110  MET B O      1 
ATOM   8862  C CB     . MET B 2 110 ? 2.174   -15.226 -48.506 1.00 15.64  ?  110  MET B CB     1 
ATOM   8863  C CG     . MET B 2 110 ? 3.422   -16.089 -48.628 1.00 16.74  ?  110  MET B CG     1 
ATOM   8864  S SD     . MET B 2 110 ? 3.273   -17.666 -47.711 1.00 17.02  ?  110  MET B SD     1 
ATOM   8865  C CE     . MET B 2 110 ? 3.706   -18.851 -48.990 1.00 19.78  ?  110  MET B CE     1 
ATOM   8866  H H      . MET B 2 110 ? 1.456   -15.074 -50.882 1.00 21.64  ?  110  MET B H      1 
ATOM   8867  H HA     . MET B 2 110 ? 0.928   -16.795 -48.868 1.00 18.78  ?  110  MET B HA     1 
ATOM   8868  H HB2    . MET B 2 110 ? 2.353   -14.374 -48.934 1.00 18.76  ?  110  MET B HB2    1 
ATOM   8869  H HB3    . MET B 2 110 ? 1.990   -15.091 -47.564 1.00 18.76  ?  110  MET B HB3    1 
ATOM   8870  H HG2    . MET B 2 110 ? 3.575   -16.297 -49.563 1.00 20.08  ?  110  MET B HG2    1 
ATOM   8871  H HG3    . MET B 2 110 ? 4.181   -15.603 -48.268 1.00 20.08  ?  110  MET B HG3    1 
ATOM   8872  H HE1    . MET B 2 110 ? 3.578   -19.749 -48.645 1.00 23.73  ?  110  MET B HE1    1 
ATOM   8873  H HE2    . MET B 2 110 ? 3.134   -18.708 -49.760 1.00 23.73  ?  110  MET B HE2    1 
ATOM   8874  H HE3    . MET B 2 110 ? 4.635   -18.722 -49.239 1.00 23.73  ?  110  MET B HE3    1 
ATOM   8875  N N      . SER B 2 111 ? -1.034  -15.812 -47.811 1.00 16.42  ?  111  SER B N      1 
ATOM   8876  C CA     . SER B 2 111 ? -2.406  -15.438 -47.501 1.00 15.54  ?  111  SER B CA     1 
ATOM   8877  C C      . SER B 2 111 ? -2.611  -14.862 -46.103 1.00 14.40  ?  111  SER B C      1 
ATOM   8878  O O      . SER B 2 111 ? -3.332  -13.859 -45.953 1.00 14.02  ?  111  SER B O      1 
ATOM   8879  C CB     . SER B 2 111 ? -3.316  -16.646 -47.683 1.00 15.99  ?  111  SER B CB     1 
ATOM   8880  O OG     . SER B 2 111 ? -4.647  -16.248 -47.487 1.00 16.79  ?  111  SER B OG     1 
ATOM   8881  H H      . SER B 2 111 ? -0.733  -16.464 -47.337 1.00 19.69  ?  111  SER B H      1 
ATOM   8882  H HA     . SER B 2 111 ? -2.678  -14.747 -48.125 1.00 18.65  ?  111  SER B HA     1 
ATOM   8883  H HB2    . SER B 2 111 ? -3.213  -16.997 -48.582 1.00 19.18  ?  111  SER B HB2    1 
ATOM   8884  H HB3    . SER B 2 111 ? -3.084  -17.327 -47.033 1.00 19.18  ?  111  SER B HB3    1 
ATOM   8885  H HG     . SER B 2 111 ? -5.161  -16.903 -47.593 1.00 20.15  ?  111  SER B HG     1 
ATOM   8886  N N      . LYS B 2 112 ? -2.016  -15.477 -45.072 1.00 13.44  ?  112  LYS B N      1 
ATOM   8887  C CA     . LYS B 2 112 ? -2.335  -15.103 -43.697 1.00 12.29  ?  112  LYS B CA     1 
ATOM   8888  C C      . LYS B 2 112 ? -1.096  -15.255 -42.829 1.00 12.64  ?  112  LYS B C      1 
ATOM   8889  O O      . LYS B 2 112 ? -0.168  -15.983 -43.178 1.00 13.15  ?  112  LYS B O      1 
ATOM   8890  C CB     . LYS B 2 112 ? -3.429  -16.007 -43.099 1.00 13.08  ?  112  LYS B CB     1 
ATOM   8891  C CG     . LYS B 2 112 ? -4.737  -16.047 -43.887 1.00 13.59  ?  112  LYS B CG     1 
ATOM   8892  C CD     . LYS B 2 112 ? -5.539  -14.779 -43.704 1.00 13.39  ?  112  LYS B CD     1 
ATOM   8893  C CE     . LYS B 2 112 ? -6.767  -14.765 -44.602 1.00 13.87  ?  112  LYS B CE     1 
ATOM   8894  N NZ     . LYS B 2 112 ? -6.441  -14.518 -46.035 1.00 15.84  ?  112  LYS B NZ     1 
ATOM   8895  H H      . LYS B 2 112 ? -1.432  -16.104 -45.146 1.00 16.13  ?  112  LYS B H      1 
ATOM   8896  H HA     . LYS B 2 112 ? -2.627  -14.178 -43.701 1.00 14.74  ?  112  LYS B HA     1 
ATOM   8897  H HB2    . LYS B 2 112 ? -3.088  -16.914 -43.057 1.00 15.69  ?  112  LYS B HB2    1 
ATOM   8898  H HB3    . LYS B 2 112 ? -3.636  -15.689 -42.207 1.00 15.69  ?  112  LYS B HB3    1 
ATOM   8899  H HG2    . LYS B 2 112 ? -4.540  -16.148 -44.831 1.00 16.31  ?  112  LYS B HG2    1 
ATOM   8900  H HG3    . LYS B 2 112 ? -5.275  -16.793 -43.578 1.00 16.31  ?  112  LYS B HG3    1 
ATOM   8901  H HD2    . LYS B 2 112 ? -5.835  -14.715 -42.782 1.00 16.06  ?  112  LYS B HD2    1 
ATOM   8902  H HD3    . LYS B 2 112 ? -4.987  -14.014 -43.929 1.00 16.06  ?  112  LYS B HD3    1 
ATOM   8903  H HE2    . LYS B 2 112 ? -7.212  -15.624 -44.541 1.00 16.64  ?  112  LYS B HE2    1 
ATOM   8904  H HE3    . LYS B 2 112 ? -7.365  -14.060 -44.306 1.00 16.64  ?  112  LYS B HE3    1 
ATOM   8905  H HZ1    . LYS B 2 112 ? -7.182  -14.556 -46.527 1.00 19.01  ?  112  LYS B HZ1    1 
ATOM   8906  H HZ2    . LYS B 2 112 ? -6.073  -13.713 -46.130 1.00 19.01  ?  112  LYS B HZ2    1 
ATOM   8907  H HZ3    . LYS B 2 112 ? -5.869  -15.133 -46.328 1.00 19.01  ?  112  LYS B HZ3    1 
ATOM   8908  N N      . VAL B 2 113 ? -1.103  -14.569 -41.679 1.00 13.26  ?  113  VAL B N      1 
ATOM   8909  C CA     . VAL B 2 113 ? -0.034  -14.645 -40.687 1.00 13.11  ?  113  VAL B CA     1 
ATOM   8910  C C      . VAL B 2 113 ? -0.624  -15.092 -39.346 1.00 12.91  ?  113  VAL B C      1 
ATOM   8911  O O      . VAL B 2 113 ? -1.665  -14.575 -38.919 1.00 14.77  ?  113  VAL B O      1 
ATOM   8912  C CB     . VAL B 2 113 ? 0.668   -13.287 -40.511 1.00 14.23  ?  113  VAL B CB     1 
ATOM   8913  C CG1    . VAL B 2 113 ? 1.753   -13.387 -39.475 1.00 13.99  ?  113  VAL B CG1    1 
ATOM   8914  C CG2    . VAL B 2 113 ? 1.255   -12.782 -41.819 1.00 16.77  ?  113  VAL B CG2    1 
ATOM   8915  H H      . VAL B 2 113 ? -1.740  -14.038 -41.450 1.00 15.91  ?  113  VAL B H      1 
ATOM   8916  H HA     . VAL B 2 113 ? 0.610   -15.309 -40.980 1.00 15.73  ?  113  VAL B HA     1 
ATOM   8917  H HB     . VAL B 2 113 ? 0.001   -12.647 -40.216 1.00 17.07  ?  113  VAL B HB     1 
ATOM   8918  H HG11   . VAL B 2 113 ? 2.275   -12.570 -39.485 1.00 16.78  ?  113  VAL B HG11   1 
ATOM   8919  H HG12   . VAL B 2 113 ? 1.346   -13.510 -38.603 1.00 16.78  ?  113  VAL B HG12   1 
ATOM   8920  H HG13   . VAL B 2 113 ? 2.321   -14.145 -39.685 1.00 16.78  ?  113  VAL B HG13   1 
ATOM   8921  H HG21   . VAL B 2 113 ? 1.764   -11.974 -41.646 1.00 20.13  ?  113  VAL B HG21   1 
ATOM   8922  H HG22   . VAL B 2 113 ? 1.836   -13.465 -42.189 1.00 20.13  ?  113  VAL B HG22   1 
ATOM   8923  H HG23   . VAL B 2 113 ? 0.532   -12.591 -42.437 1.00 20.13  ?  113  VAL B HG23   1 
ATOM   8924  N N      . TYR B 2 114 ? 0.043   -16.046 -38.689 1.00 12.59  ?  114  TYR B N      1 
ATOM   8925  C CA     . TYR B 2 114 ? -0.244  -16.441 -37.303 1.00 13.79  ?  114  TYR B CA     1 
ATOM   8926  C C      . TYR B 2 114 ? 0.950   -16.075 -36.424 1.00 11.93  ?  114  TYR B C      1 
ATOM   8927  O O      . TYR B 2 114 ? 2.087   -16.403 -36.764 1.00 12.37  ?  114  TYR B O      1 
ATOM   8928  C CB     . TYR B 2 114 ? -0.529  -17.942 -37.171 1.00 13.18  ?  114  TYR B CB     1 
ATOM   8929  C CG     . TYR B 2 114 ? -0.693  -18.346 -35.719 1.00 12.41  ?  114  TYR B CG     1 
ATOM   8930  C CD1    . TYR B 2 114 ? -1.883  -18.072 -35.046 1.00 13.53  ?  114  TYR B CD1    1 
ATOM   8931  C CD2    . TYR B 2 114 ? 0.350   -18.898 -35.001 1.00 13.81  ?  114  TYR B CD2    1 
ATOM   8932  C CE1    . TYR B 2 114 ? -2.042  -18.372 -33.710 1.00 13.90  ?  114  TYR B CE1    1 
ATOM   8933  C CE2    . TYR B 2 114 ? 0.191   -19.195 -33.639 1.00 12.27  ?  114  TYR B CE2    1 
ATOM   8934  C CZ     . TYR B 2 114 ? -1.000  -18.929 -33.022 1.00 12.87  ?  114  TYR B CZ     1 
ATOM   8935  O OH     . TYR B 2 114 ? -1.175  -19.218 -31.655 1.00 15.48  ?  114  TYR B OH     1 
ATOM   8936  H H      . TYR B 2 114 ? 0.688   -16.494 -39.038 1.00 15.10  ?  114  TYR B H      1 
ATOM   8937  H HA     . TYR B 2 114 ? -1.032  -15.961 -37.004 1.00 16.55  ?  114  TYR B HA     1 
ATOM   8938  H HB2    . TYR B 2 114 ? -1.348  -18.157 -37.643 1.00 15.81  ?  114  TYR B HB2    1 
ATOM   8939  H HB3    . TYR B 2 114 ? 0.212   -18.444 -37.546 1.00 15.81  ?  114  TYR B HB3    1 
ATOM   8940  H HD1    . TYR B 2 114 ? -2.586  -17.678 -35.510 1.00 16.24  ?  114  TYR B HD1    1 
ATOM   8941  H HD2    . TYR B 2 114 ? 1.160   -19.074 -35.422 1.00 16.57  ?  114  TYR B HD2    1 
ATOM   8942  H HE1    . TYR B 2 114 ? -2.849  -18.197 -33.282 1.00 16.68  ?  114  TYR B HE1    1 
ATOM   8943  H HE2    . TYR B 2 114 ? 0.892   -19.571 -33.159 1.00 14.73  ?  114  TYR B HE2    1 
ATOM   8944  H HH     . TYR B 2 114 ? -0.473  -19.557 -31.341 1.00 18.57  ?  114  TYR B HH     1 
ATOM   8945  N N      . TYR B 2 115 ? 0.698   -15.418 -35.285 1.00 11.77  ?  115  TYR B N      1 
ATOM   8946  C CA     . TYR B 2 115 ? 1.781   -14.876 -34.460 1.00 12.44  ?  115  TYR B CA     1 
ATOM   8947  C C      . TYR B 2 115 ? 2.133   -15.724 -33.238 1.00 11.51  ?  115  TYR B C      1 
ATOM   8948  O O      . TYR B 2 115 ? 1.265   -16.209 -32.504 1.00 12.24  ?  115  TYR B O      1 
ATOM   8949  C CB     . TYR B 2 115 ? 1.435   -13.462 -33.960 1.00 13.63  ?  115  TYR B CB     1 
ATOM   8950  C CG     . TYR B 2 115 ? 1.377   -12.447 -35.066 1.00 12.68  ?  115  TYR B CG     1 
ATOM   8951  C CD1    . TYR B 2 115 ? 2.524   -11.793 -35.507 1.00 13.78  ?  115  TYR B CD1    1 
ATOM   8952  C CD2    . TYR B 2 115 ? 0.171   -12.117 -35.658 1.00 13.14  ?  115  TYR B CD2    1 
ATOM   8953  C CE1    . TYR B 2 115 ? 2.470   -10.851 -36.513 1.00 14.31  ?  115  TYR B CE1    1 
ATOM   8954  C CE2    . TYR B 2 115 ? 0.111   -11.209 -36.675 1.00 14.74  ?  115  TYR B CE2    1 
ATOM   8955  C CZ     . TYR B 2 115 ? 1.268   -10.565 -37.087 1.00 14.66  ?  115  TYR B CZ     1 
ATOM   8956  O OH     . TYR B 2 115 ? 1.194   -9.640  -38.107 1.00 14.97  ?  115  TYR B OH     1 
ATOM   8957  H H      . TYR B 2 115 ? -0.091  -15.276 -34.973 1.00 14.12  ?  115  TYR B H      1 
ATOM   8958  H HA     . TYR B 2 115 ? 2.565   -14.869 -35.031 1.00 14.93  ?  115  TYR B HA     1 
ATOM   8959  H HB2    . TYR B 2 115 ? 0.566   -13.485 -33.529 1.00 16.35  ?  115  TYR B HB2    1 
ATOM   8960  H HB3    . TYR B 2 115 ? 2.112   -13.177 -33.327 1.00 16.35  ?  115  TYR B HB3    1 
ATOM   8961  H HD1    . TYR B 2 115 ? 3.343   -11.996 -35.115 1.00 16.53  ?  115  TYR B HD1    1 
ATOM   8962  H HD2    . TYR B 2 115 ? -0.611  -12.521 -35.358 1.00 15.76  ?  115  TYR B HD2    1 
ATOM   8963  H HE1    . TYR B 2 115 ? 3.243   -10.418 -36.795 1.00 17.17  ?  115  TYR B HE1    1 
ATOM   8964  H HE2    . TYR B 2 115 ? -0.701  -11.022 -37.088 1.00 17.69  ?  115  TYR B HE2    1 
ATOM   8965  H HH     . TYR B 2 115 ? 0.405   -9.589  -38.391 1.00 17.96  ?  115  TYR B HH     1 
ATOM   8966  N N      . GLY B 2 116 ? 3.439   -15.829 -32.989 1.00 11.77  ?  116  GLY B N      1 
ATOM   8967  C CA     . GLY B 2 116 ? 3.991   -16.445 -31.797 1.00 11.57  ?  116  GLY B CA     1 
ATOM   8968  C C      . GLY B 2 116 ? 5.141   -15.587 -31.280 1.00 12.32  ?  116  GLY B C      1 
ATOM   8969  O O      . GLY B 2 116 ? 5.196   -14.377 -31.560 1.00 13.61  ?  116  GLY B O      1 
ATOM   8970  H H      . GLY B 2 116 ? 4.048   -15.537 -33.521 1.00 14.13  ?  116  GLY B H      1 
ATOM   8971  H HA2    . GLY B 2 116 ? 3.310   -16.514 -31.110 1.00 13.88  ?  116  GLY B HA2    1 
ATOM   8972  H HA3    . GLY B 2 116 ? 4.323   -17.333 -32.003 1.00 13.88  ?  116  GLY B HA3    1 
ATOM   8973  N N      A MET B 2 117 ? 6.069   -16.198 -30.514 0.56 11.53  ?  117  MET B N      1 
ATOM   8974  N N      B MET B 2 117 ? 6.049   -16.183 -30.509 0.44 11.65  ?  117  MET B N      1 
ATOM   8975  C CA     A MET B 2 117 ? 7.126   -15.455 -29.835 0.56 13.53  ?  117  MET B CA     1 
ATOM   8976  C CA     B MET B 2 117 ? 7.137   -15.433 -29.898 0.44 13.05  ?  117  MET B CA     1 
ATOM   8977  C C      A MET B 2 117 ? 8.535   -15.932 -30.169 0.56 13.38  ?  117  MET B C      1 
ATOM   8978  C C      B MET B 2 117 ? 8.503   -15.831 -30.424 0.44 12.61  ?  117  MET B C      1 
ATOM   8979  O O      A MET B 2 117 ? 9.497   -15.212 -29.876 0.56 17.02  ?  117  MET B O      1 
ATOM   8980  O O      B MET B 2 117 ? 9.369   -14.961 -30.574 0.44 12.78  ?  117  MET B O      1 
ATOM   8981  C CB     A MET B 2 117 ? 6.937   -15.528 -28.308 0.56 14.99  ?  117  MET B CB     1 
ATOM   8982  C CB     B MET B 2 117 ? 7.096   -15.608 -28.372 0.44 13.93  ?  117  MET B CB     1 
ATOM   8983  C CG     A MET B 2 117 ? 5.775   -14.711 -27.760 0.56 14.88  ?  117  MET B CG     1 
ATOM   8984  C CG     B MET B 2 117 ? 5.939   -14.860 -27.706 0.44 13.13  ?  117  MET B CG     1 
ATOM   8985  S SD     A MET B 2 117 ? 4.132   -15.352 -28.127 0.56 16.47  ?  117  MET B SD     1 
ATOM   8986  S SD     B MET B 2 117 ? 4.934   -15.828 -26.551 0.44 15.51  ?  117  MET B SD     1 
ATOM   8987  C CE     A MET B 2 117 ? 4.228   -16.971 -27.370 0.56 16.91  ?  117  MET B CE     1 
ATOM   8988  C CE     B MET B 2 117 ? 3.956   -16.829 -27.672 0.44 15.88  ?  117  MET B CE     1 
ATOM   8989  H H      A MET B 2 117 ? 6.098   -17.046 -30.379 0.56 13.83  ?  117  MET B H      1 
ATOM   8990  H H      B MET B 2 117 ? 6.053   -17.024 -30.326 0.44 13.98  ?  117  MET B H      1 
ATOM   8991  H HA     A MET B 2 117 ? 7.050   -14.525 -30.100 0.56 16.23  ?  117  MET B HA     1 
ATOM   8992  H HA     B MET B 2 117 ? 7.015   -14.487 -30.076 0.44 15.66  ?  117  MET B HA     1 
ATOM   8993  H HB2    A MET B 2 117 ? 6.782   -16.454 -28.062 0.56 17.99  ?  117  MET B HB2    1 
ATOM   8994  H HB2    B MET B 2 117 ? 6.998   -16.551 -28.167 0.44 16.71  ?  117  MET B HB2    1 
ATOM   8995  H HB3    A MET B 2 117 ? 7.746   -15.203 -27.883 0.56 17.99  ?  117  MET B HB3    1 
ATOM   8996  H HB3    B MET B 2 117 ? 7.924   -15.271 -27.995 0.44 16.71  ?  117  MET B HB3    1 
ATOM   8997  H HG2    A MET B 2 117 ? 5.858   -14.671 -26.794 0.56 17.86  ?  117  MET B HG2    1 
ATOM   8998  H HG2    B MET B 2 117 ? 6.306   -14.112 -27.210 0.44 15.76  ?  117  MET B HG2    1 
ATOM   8999  H HG3    A MET B 2 117 ? 5.826   -13.818 -28.135 0.56 17.86  ?  117  MET B HG3    1 
ATOM   9000  H HG3    B MET B 2 117 ? 5.345   -14.538 -28.402 0.44 15.76  ?  117  MET B HG3    1 
ATOM   9001  H HE1    A MET B 2 117 ? 3.392   -17.156 -26.914 0.56 20.29  ?  117  MET B HE1    1 
ATOM   9002  H HE1    B MET B 2 117 ? 3.374   -17.407 -27.154 0.44 19.06  ?  117  MET B HE1    1 
ATOM   9003  H HE2    A MET B 2 117 ? 4.382   -17.634 -28.060 0.56 20.29  ?  117  MET B HE2    1 
ATOM   9004  H HE2    B MET B 2 117 ? 3.426   -16.245 -28.236 0.44 19.06  ?  117  MET B HE2    1 
ATOM   9005  H HE3    A MET B 2 117 ? 4.960   -16.979 -26.733 0.56 20.29  ?  117  MET B HE3    1 
ATOM   9006  H HE3    B MET B 2 117 ? 4.552   -17.365 -28.219 0.44 19.06  ?  117  MET B HE3    1 
ATOM   9007  N N      . SER B 2 118 ? 8.686   -17.103 -30.778 1.00 12.71  ?  118  SER B N      1 
ATOM   9008  C CA     . SER B 2 118 ? 9.995   -17.646 -31.115 1.00 12.90  ?  118  SER B CA     1 
ATOM   9009  C C      . SER B 2 118 ? 9.898   -18.408 -32.426 1.00 11.45  ?  118  SER B C      1 
ATOM   9010  O O      . SER B 2 118 ? 8.834   -18.883 -32.817 1.00 12.54  ?  118  SER B O      1 
ATOM   9011  C CB     . SER B 2 118 ? 10.470  -18.611 -30.022 1.00 14.01  ?  118  SER B CB     1 
ATOM   9012  O OG     . SER B 2 118 ? 9.614   -19.728 -29.921 1.00 13.82  ?  118  SER B OG     1 
ATOM   9013  H H      A SER B 2 118 ? 8.032   -17.611 -31.012 0.56 15.25  ?  118  SER B H      1 
ATOM   9014  H H      B SER B 2 118 ? 8.050   -17.680 -30.831 0.44 15.25  ?  118  SER B H      1 
ATOM   9015  H HA     . SER B 2 118 ? 10.633  -16.923 -31.219 1.00 15.48  ?  118  SER B HA     1 
ATOM   9016  H HB2    . SER B 2 118 ? 11.364  -18.918 -30.240 1.00 16.81  ?  118  SER B HB2    1 
ATOM   9017  H HB3    . SER B 2 118 ? 10.478  -18.144 -29.172 1.00 16.81  ?  118  SER B HB3    1 
ATOM   9018  H HG     . SER B 2 118 ? 9.911   -20.268 -29.351 1.00 16.58  ?  118  SER B HG     1 
ATOM   9019  N N      . GLY B 2 119 ? 11.031  -18.528 -33.112 1.00 13.36  ?  119  GLY B N      1 
ATOM   9020  C CA     . GLY B 2 119 ? 11.078  -19.397 -34.269 1.00 11.99  ?  119  GLY B CA     1 
ATOM   9021  C C      . GLY B 2 119 ? 10.681  -20.819 -33.939 1.00 13.03  ?  119  GLY B C      1 
ATOM   9022  O O      . GLY B 2 119 ? 10.022  -21.490 -34.748 1.00 12.65  ?  119  GLY B O      1 
ATOM   9023  H H      . GLY B 2 119 ? 11.769  -18.126 -32.932 1.00 16.02  ?  119  GLY B H      1 
ATOM   9024  H HA2    . GLY B 2 119 ? 10.472  -19.060 -34.948 1.00 14.38  ?  119  GLY B HA2    1 
ATOM   9025  H HA3    . GLY B 2 119 ? 11.979  -19.406 -34.627 1.00 14.38  ?  119  GLY B HA3    1 
ATOM   9026  N N      . SER B 2 120 ? 11.084  -21.301 -32.745 1.00 11.39  ?  120  SER B N      1 
ATOM   9027  C CA     . SER B 2 120 ? 10.737  -22.650 -32.320 1.00 11.70  ?  120  SER B CA     1 
ATOM   9028  C C      . SER B 2 120 ? 9.228   -22.832 -32.232 1.00 11.74  ?  120  SER B C      1 
ATOM   9029  O O      . SER B 2 120 ? 8.694   -23.841 -32.717 1.00 12.45  ?  120  SER B O      1 
ATOM   9030  C CB     . SER B 2 120 ? 11.378  -22.985 -30.956 1.00 11.85  ?  120  SER B CB     1 
ATOM   9031  O OG     . SER B 2 120 ? 12.781  -23.014 -31.014 1.00 12.34  ?  120  SER B OG     1 
ATOM   9032  H H      . SER B 2 120 ? 11.555  -20.864 -32.173 1.00 13.67  ?  120  SER B H      1 
ATOM   9033  H HA     . SER B 2 120 ? 11.092  -23.265 -32.982 1.00 14.04  ?  120  SER B HA     1 
ATOM   9034  H HB2    . SER B 2 120 ? 11.109  -22.310 -30.314 1.00 14.21  ?  120  SER B HB2    1 
ATOM   9035  H HB3    . SER B 2 120 ? 11.062  -23.857 -30.672 1.00 14.21  ?  120  SER B HB3    1 
ATOM   9036  H HG     . SER B 2 120 ? 13.083  -22.231 -31.057 1.00 14.81  ?  120  SER B HG     1 
ATOM   9037  N N      . ASP B 2 121 ? 8.514   -21.874 -31.608 1.00 11.62  ?  121  ASP B N      1 
ATOM   9038  C CA     . ASP B 2 121 ? 7.053   -22.032 -31.503 1.00 12.07  ?  121  ASP B CA     1 
ATOM   9039  C C      . ASP B 2 121 ? 6.387   -21.893 -32.866 1.00 11.92  ?  121  ASP B C      1 
ATOM   9040  O O      . ASP B 2 121 ? 5.363   -22.534 -33.131 1.00 12.13  ?  121  ASP B O      1 
ATOM   9041  C CB     . ASP B 2 121 ? 6.418   -21.176 -30.390 1.00 13.13  ?  121  ASP B CB     1 
ATOM   9042  C CG     . ASP B 2 121 ? 6.259   -19.693 -30.707 1.00 12.54  ?  121  ASP B CG     1 
ATOM   9043  O OD1    . ASP B 2 121 ? 5.951   -19.282 -31.837 1.00 13.61  ?  121  ASP B OD1    1 
ATOM   9044  O OD2    . ASP B 2 121 ? 6.360   -18.899 -29.732 1.00 16.14  -1 121  ASP B OD2    1 
ATOM   9045  H H      . ASP B 2 121 ? 8.835   -21.159 -31.255 1.00 13.94  ?  121  ASP B H      1 
ATOM   9046  H HA     . ASP B 2 121 ? 6.864   -22.931 -31.192 1.00 14.48  ?  121  ASP B HA     1 
ATOM   9047  H HB2    . ASP B 2 121 ? 5.533   -21.527 -30.202 1.00 15.75  ?  121  ASP B HB2    1 
ATOM   9048  H HB3    . ASP B 2 121 ? 6.976   -21.243 -29.599 1.00 15.75  ?  121  ASP B HB3    1 
ATOM   9049  N N      . ALA B 2 122 ? 7.004   -21.153 -33.782 1.00 11.50  ?  122  ALA B N      1 
ATOM   9050  C CA     . ALA B 2 122 ? 6.434   -21.053 -35.116 1.00 11.19  ?  122  ALA B CA     1 
ATOM   9051  C C      . ALA B 2 122 ? 6.523   -22.394 -35.822 1.00 12.34  ?  122  ALA B C      1 
ATOM   9052  O O      . ALA B 2 122 ? 5.585   -22.798 -36.516 1.00 12.10  ?  122  ALA B O      1 
ATOM   9053  C CB     . ALA B 2 122 ? 7.128   -19.938 -35.899 1.00 10.85  ?  122  ALA B CB     1 
ATOM   9054  H H      . ALA B 2 122 ? 7.732   -20.711 -33.661 1.00 13.79  ?  122  ALA B H      1 
ATOM   9055  H HA     . ALA B 2 122 ? 5.497   -20.809 -35.063 1.00 13.43  ?  122  ALA B HA     1 
ATOM   9056  H HB1    . ALA B 2 122 ? 6.710   -19.857 -36.771 1.00 13.02  ?  122  ALA B HB1    1 
ATOM   9057  H HB2    . ALA B 2 122 ? 7.038   -19.105 -35.410 1.00 13.02  ?  122  ALA B HB2    1 
ATOM   9058  H HB3    . ALA B 2 122 ? 8.066   -20.161 -36.003 1.00 13.02  ?  122  ALA B HB3    1 
ATOM   9059  N N      . ASN B 2 123 ? 7.619   -23.131 -35.612 1.00 10.90  ?  123  ASN B N      1 
ATOM   9060  C CA     . ASN B 2 123 ? 7.719   -24.455 -36.217 1.00 11.73  ?  123  ASN B CA     1 
ATOM   9061  C C      . ASN B 2 123 ? 6.836   -25.478 -35.525 1.00 12.56  ?  123  ASN B C      1 
ATOM   9062  O O      . ASN B 2 123 ? 6.377   -26.424 -36.185 1.00 12.19  ?  123  ASN B O      1 
ATOM   9063  C CB     . ASN B 2 123 ? 9.174   -24.880 -36.340 1.00 12.00  ?  123  ASN B CB     1 
ATOM   9064  C CG     . ASN B 2 123 ? 9.869   -24.173 -37.513 1.00 11.67  ?  123  ASN B CG     1 
ATOM   9065  O OD1    . ASN B 2 123 ? 9.222   -23.894 -38.525 1.00 12.06  ?  123  ASN B OD1    1 
ATOM   9066  N ND2    . ASN B 2 123 ? 11.173  -23.876 -37.375 1.00 12.40  ?  123  ASN B ND2    1 
ATOM   9067  H H      . ASN B 2 123 ? 8.297   -22.895 -35.139 1.00 13.08  ?  123  ASN B H      1 
ATOM   9068  H HA     . ASN B 2 123 ? 7.388   -24.415 -37.128 1.00 14.07  ?  123  ASN B HA     1 
ATOM   9069  H HB2    . ASN B 2 123 ? 9.646   -24.652 -35.524 1.00 14.40  ?  123  ASN B HB2    1 
ATOM   9070  H HB3    . ASN B 2 123 ? 9.218   -25.837 -36.492 1.00 14.40  ?  123  ASN B HB3    1 
ATOM   9071  H HD21   . ASN B 2 123 ? 11.593  -23.480 -38.013 1.00 14.88  ?  123  ASN B HD21   1 
ATOM   9072  H HD22   . ASN B 2 123 ? 11.587  -24.083 -36.651 1.00 14.88  ?  123  ASN B HD22   1 
ATOM   9073  N N      . GLU B 2 124 ? 6.540   -25.307 -34.231 1.00 12.64  ?  124  GLU B N      1 
ATOM   9074  C CA     . GLU B 2 124 ? 5.490   -26.120 -33.614 1.00 11.40  ?  124  GLU B CA     1 
ATOM   9075  C C      . GLU B 2 124 ? 4.170   -25.902 -34.360 1.00 13.41  ?  124  GLU B C      1 
ATOM   9076  O O      . GLU B 2 124 ? 3.466   -26.859 -34.691 1.00 12.20  ?  124  GLU B O      1 
ATOM   9077  C CB     . GLU B 2 124 ? 5.291   -25.752 -32.141 1.00 11.86  ?  124  GLU B CB     1 
ATOM   9078  C CG     . GLU B 2 124 ? 6.481   -25.952 -31.197 1.00 12.92  ?  124  GLU B CG     1 
ATOM   9079  C CD     . GLU B 2 124 ? 6.823   -27.409 -30.951 1.00 14.03  ?  124  GLU B CD     1 
ATOM   9080  O OE1    . GLU B 2 124 ? 8.040   -27.697 -30.831 1.00 14.14  ?  124  GLU B OE1    1 
ATOM   9081  O OE2    . GLU B 2 124 ? 5.903   -28.268 -30.848 1.00 14.20  -1 124  GLU B OE2    1 
ATOM   9082  H H      . GLU B 2 124 ? 6.920   -24.744 -33.704 1.00 15.16  ?  124  GLU B H      1 
ATOM   9083  H HA     . GLU B 2 124 ? 5.761   -27.051 -33.654 1.00 13.67  ?  124  GLU B HA     1 
ATOM   9084  H HB2    . GLU B 2 124 ? 5.055   -24.812 -32.098 1.00 14.22  ?  124  GLU B HB2    1 
ATOM   9085  H HB3    . GLU B 2 124 ? 4.565   -26.293 -31.794 1.00 14.22  ?  124  GLU B HB3    1 
ATOM   9086  H HG2    . GLU B 2 124 ? 7.262   -25.526 -31.584 1.00 15.50  ?  124  GLU B HG2    1 
ATOM   9087  H HG3    . GLU B 2 124 ? 6.272   -25.548 -30.341 1.00 15.50  ?  124  GLU B HG3    1 
ATOM   9088  N N      . THR B 2 125 ? 3.833   -24.634 -34.633 1.00 12.52  ?  125  THR B N      1 
ATOM   9089  C CA     . THR B 2 125 ? 2.613   -24.320 -35.364 1.00 12.17  ?  125  THR B CA     1 
ATOM   9090  C C      . THR B 2 125 ? 2.637   -24.943 -36.753 1.00 12.62  ?  125  THR B C      1 
ATOM   9091  O O      . THR B 2 125 ? 1.624   -25.502 -37.203 1.00 11.89  ?  125  THR B O      1 
ATOM   9092  C CB     . THR B 2 125 ? 2.436   -22.803 -35.439 1.00 11.27  ?  125  THR B CB     1 
ATOM   9093  O OG1    . THR B 2 125 ? 2.347   -22.274 -34.106 1.00 12.10  ?  125  THR B OG1    1 
ATOM   9094  C CG2    . THR B 2 125 ? 1.195   -22.420 -36.211 1.00 12.63  ?  125  THR B CG2    1 
ATOM   9095  H H      . THR B 2 125 ? 4.293   -23.944 -34.405 1.00 15.02  ?  125  THR B H      1 
ATOM   9096  H HA     . THR B 2 125 ? 1.848   -24.683 -34.891 1.00 14.61  ?  125  THR B HA     1 
ATOM   9097  H HB     . THR B 2 125 ? 3.197   -22.419 -35.903 1.00 13.51  ?  125  THR B HB     1 
ATOM   9098  H HG1    . THR B 2 125 ? 3.062   -22.418 -33.691 1.00 14.51  ?  125  THR B HG1    1 
ATOM   9099  H HG21   . THR B 2 125 ? 1.078   -21.457 -36.195 1.00 15.15  ?  125  THR B HG21   1 
ATOM   9100  H HG22   . THR B 2 125 ? 1.274   -22.712 -37.133 1.00 15.15  ?  125  THR B HG22   1 
ATOM   9101  H HG23   . THR B 2 125 ? 0.415   -22.839 -35.814 1.00 15.15  ?  125  THR B HG23   1 
ATOM   9102  N N      . GLN B 2 126 ? 3.773   -24.841 -37.451 1.00 12.53  ?  126  GLN B N      1 
ATOM   9103  C CA     . GLN B 2 126 ? 3.878   -25.432 -38.779 1.00 11.66  ?  126  GLN B CA     1 
ATOM   9104  C C      . GLN B 2 126 ? 3.517   -26.915 -38.725 1.00 12.43  ?  126  GLN B C      1 
ATOM   9105  O O      . GLN B 2 126 ? 2.785   -27.428 -39.575 1.00 12.55  ?  126  GLN B O      1 
ATOM   9106  C CB     . GLN B 2 126 ? 5.295   -25.273 -39.337 1.00 12.27  ?  126  GLN B CB     1 
ATOM   9107  C CG     . GLN B 2 126 ? 5.816   -23.859 -39.569 1.00 13.43  ?  126  GLN B CG     1 
ATOM   9108  C CD     . GLN B 2 126 ? 5.194   -23.174 -40.758 1.00 13.96  ?  126  GLN B CD     1 
ATOM   9109  O OE1    . GLN B 2 126 ? 4.103   -23.527 -41.210 1.00 13.45  ?  126  GLN B OE1    1 
ATOM   9110  N NE2    . GLN B 2 126 ? 5.900   -22.188 -41.288 1.00 13.19  ?  126  GLN B NE2    1 
ATOM   9111  H H      . GLN B 2 126 ? 4.485   -24.440 -37.182 1.00 15.03  ?  126  GLN B H      1 
ATOM   9112  H HA     . GLN B 2 126 ? 3.268   -24.965 -39.370 1.00 13.99  ?  126  GLN B HA     1 
ATOM   9113  H HB2    . GLN B 2 126 ? 5.907   -25.697 -38.715 1.00 14.72  ?  126  GLN B HB2    1 
ATOM   9114  H HB3    . GLN B 2 126 ? 5.327   -25.725 -40.195 1.00 14.72  ?  126  GLN B HB3    1 
ATOM   9115  H HG2    . GLN B 2 126 ? 5.625   -23.322 -38.784 1.00 16.12  ?  126  GLN B HG2    1 
ATOM   9116  H HG3    . GLN B 2 126 ? 6.774   -23.900 -39.718 1.00 16.12  ?  126  GLN B HG3    1 
ATOM   9117  H HE21   . GLN B 2 126 ? 6.662   -21.976 -40.951 1.00 15.82  ?  126  GLN B HE21   1 
ATOM   9118  H HE22   . GLN B 2 126 ? 5.595   -21.759 -41.968 1.00 15.82  ?  126  GLN B HE22   1 
ATOM   9119  N N      . LEU B 2 127 ? 4.069   -27.635 -37.754 1.00 11.95  ?  127  LEU B N      1 
ATOM   9120  C CA     . LEU B 2 127 ? 3.810   -29.078 -37.662 1.00 11.67  ?  127  LEU B CA     1 
ATOM   9121  C C      . LEU B 2 127 ? 2.332   -29.366 -37.411 1.00 11.72  ?  127  LEU B C      1 
ATOM   9122  O O      . LEU B 2 127 ? 1.763   -30.286 -38.013 1.00 11.81  ?  127  LEU B O      1 
ATOM   9123  C CB     . LEU B 2 127 ? 4.708   -29.723 -36.609 1.00 10.86  ?  127  LEU B CB     1 
ATOM   9124  C CG     . LEU B 2 127 ? 6.196   -29.689 -36.921 1.00 12.53  ?  127  LEU B CG     1 
ATOM   9125  C CD1    . LEU B 2 127 ? 7.000   -30.261 -35.763 1.00 15.77  ?  127  LEU B CD1    1 
ATOM   9126  C CD2    . LEU B 2 127 ? 6.536   -30.475 -38.209 1.00 17.30  ?  127  LEU B CD2    1 
ATOM   9127  H H      . LEU B 2 127 ? 4.590   -27.326 -37.143 1.00 14.34  ?  127  LEU B H      1 
ATOM   9128  H HA     . LEU B 2 127 ? 4.038   -29.490 -38.509 1.00 14.01  ?  127  LEU B HA     1 
ATOM   9129  H HB2    . LEU B 2 127 ? 4.577   -29.257 -35.768 1.00 13.03  ?  127  LEU B HB2    1 
ATOM   9130  H HB3    . LEU B 2 127 ? 4.451   -30.653 -36.516 1.00 13.03  ?  127  LEU B HB3    1 
ATOM   9131  H HG     . LEU B 2 127 ? 6.442   -28.762 -37.060 1.00 15.04  ?  127  LEU B HG     1 
ATOM   9132  H HD11   . LEU B 2 127 ? 7.943   -30.229 -35.986 1.00 18.92  ?  127  LEU B HD11   1 
ATOM   9133  H HD12   . LEU B 2 127 ? 6.829   -29.732 -34.968 1.00 18.92  ?  127  LEU B HD12   1 
ATOM   9134  H HD13   . LEU B 2 127 ? 6.727   -31.180 -35.612 1.00 18.92  ?  127  LEU B HD13   1 
ATOM   9135  H HD21   . LEU B 2 127 ? 7.497   -30.595 -38.261 1.00 20.76  ?  127  LEU B HD21   1 
ATOM   9136  H HD22   . LEU B 2 127 ? 6.096   -31.339 -38.177 1.00 20.76  ?  127  LEU B HD22   1 
ATOM   9137  H HD23   . LEU B 2 127 ? 6.223   -29.973 -38.977 1.00 20.76  ?  127  LEU B HD23   1 
ATOM   9138  N N      . LYS B 2 128 ? 1.687   -28.586 -36.535 1.00 11.57  ?  128  LYS B N      1 
ATOM   9139  C CA     . LYS B 2 128 ? 0.247   -28.756 -36.330 1.00 10.49  ?  128  LYS B CA     1 
ATOM   9140  C C      . LYS B 2 128 ? -0.525  -28.503 -37.619 1.00 12.59  ?  128  LYS B C      1 
ATOM   9141  O O      . LYS B 2 128 ? -1.474  -29.235 -37.944 1.00 13.55  ?  128  LYS B O      1 
ATOM   9142  C CB     . LYS B 2 128 ? -0.247  -27.863 -35.185 1.00 12.32  ?  128  LYS B CB     1 
ATOM   9143  C CG     . LYS B 2 128 ? 0.139   -28.379 -33.814 1.00 11.41  ?  128  LYS B CG     1 
ATOM   9144  C CD     . LYS B 2 128 ? -0.416  -27.554 -32.654 1.00 10.93  ?  128  LYS B CD     1 
ATOM   9145  C CE     . LYS B 2 128 ? -1.914  -27.540 -32.625 1.00 11.44  ?  128  LYS B CE     1 
ATOM   9146  N NZ     . LYS B 2 128 ? -2.428  -26.832 -31.410 1.00 11.72  ?  128  LYS B NZ     1 
ATOM   9147  H H      . LYS B 2 128 ? 2.049   -27.968 -36.059 1.00 13.88  ?  128  LYS B H      1 
ATOM   9148  H HA     . LYS B 2 128 ? 0.073   -29.673 -36.063 1.00 12.58  ?  128  LYS B HA     1 
ATOM   9149  H HB2    . LYS B 2 128 ? 0.136   -26.978 -35.290 1.00 14.78  ?  128  LYS B HB2    1 
ATOM   9150  H HB3    . LYS B 2 128 ? -1.215  -27.811 -35.222 1.00 14.78  ?  128  LYS B HB3    1 
ATOM   9151  H HG2    . LYS B 2 128 ? -0.195  -29.284 -33.717 1.00 13.68  ?  128  LYS B HG2    1 
ATOM   9152  H HG3    . LYS B 2 128 ? 1.107   -28.373 -33.741 1.00 13.68  ?  128  LYS B HG3    1 
ATOM   9153  H HD2    . LYS B 2 128 ? -0.103  -27.932 -31.817 1.00 13.11  ?  128  LYS B HD2    1 
ATOM   9154  H HD3    . LYS B 2 128 ? -0.109  -26.638 -32.739 1.00 13.11  ?  128  LYS B HD3    1 
ATOM   9155  H HE2    . LYS B 2 128 ? -2.247  -27.079 -33.411 1.00 13.72  ?  128  LYS B HE2    1 
ATOM   9156  H HE3    . LYS B 2 128 ? -2.245  -28.452 -32.611 1.00 13.72  ?  128  LYS B HE3    1 
ATOM   9157  H HZ1    . LYS B 2 128 ? -3.155  -26.362 -31.616 1.00 14.07  ?  128  LYS B HZ1    1 
ATOM   9158  H HZ2    . LYS B 2 128 ? -2.636  -27.424 -30.778 1.00 14.07  ?  128  LYS B HZ2    1 
ATOM   9159  H HZ3    . LYS B 2 128 ? -1.806  -26.279 -31.094 1.00 14.07  ?  128  LYS B HZ3    1 
ATOM   9160  N N      . ILE B 2 129 ? -0.130  -27.471 -38.377 1.00 12.23  ?  129  ILE B N      1 
ATOM   9161  C CA     . ILE B 2 129 ? -0.811  -27.179 -39.636 1.00 12.30  ?  129  ILE B CA     1 
ATOM   9162  C C      . ILE B 2 129 ? -0.692  -28.339 -40.609 1.00 12.37  ?  129  ILE B C      1 
ATOM   9163  O O      . ILE B 2 129 ? -1.659  -28.698 -41.278 1.00 12.18  ?  129  ILE B O      1 
ATOM   9164  C CB     . ILE B 2 129 ? -0.303  -25.857 -40.234 1.00 11.67  ?  129  ILE B CB     1 
ATOM   9165  C CG1    . ILE B 2 129 ? -0.761  -24.697 -39.374 1.00 13.23  ?  129  ILE B CG1    1 
ATOM   9166  C CG2    . ILE B 2 129 ? -0.735  -25.705 -41.725 1.00 12.20  ?  129  ILE B CG2    1 
ATOM   9167  C CD1    . ILE B 2 129 ? -0.115  -23.395 -39.768 1.00 13.79  ?  129  ILE B CD1    1 
ATOM   9168  H H      . ILE B 2 129 ? 0.516   -26.936 -38.187 1.00 14.68  ?  129  ILE B H      1 
ATOM   9169  H HA     . ILE B 2 129 ? -1.756  -27.067 -39.445 1.00 14.76  ?  129  ILE B HA     1 
ATOM   9170  H HB     . ILE B 2 129 ? 0.667   -25.863 -40.233 1.00 14.00  ?  129  ILE B HB     1 
ATOM   9171  H HG12   . ILE B 2 129 ? -1.721  -24.597 -39.463 1.00 15.87  ?  129  ILE B HG12   1 
ATOM   9172  H HG13   . ILE B 2 129 ? -0.531  -24.879 -38.449 1.00 15.87  ?  129  ILE B HG13   1 
ATOM   9173  H HG21   . ILE B 2 129 ? -0.575  -24.791 -42.009 1.00 14.63  ?  129  ILE B HG21   1 
ATOM   9174  H HG22   . ILE B 2 129 ? -0.214  -26.316 -42.269 1.00 14.63  ?  129  ILE B HG22   1 
ATOM   9175  H HG23   . ILE B 2 129 ? -1.679  -25.915 -41.804 1.00 14.63  ?  129  ILE B HG23   1 
ATOM   9176  H HD11   . ILE B 2 129 ? -0.277  -22.739 -39.073 1.00 16.54  ?  129  ILE B HD11   1 
ATOM   9177  H HD12   . ILE B 2 129 ? 0.839   -23.535 -39.876 1.00 16.54  ?  129  ILE B HD12   1 
ATOM   9178  H HD13   . ILE B 2 129 ? -0.501  -23.092 -40.605 1.00 16.54  ?  129  ILE B HD13   1 
ATOM   9179  N N      . VAL B 2 130 ? 0.498   -28.925 -40.721 1.00 12.38  ?  130  VAL B N      1 
ATOM   9180  C CA     . VAL B 2 130 ? 0.702   -30.018 -41.668 1.00 11.92  ?  130  VAL B CA     1 
ATOM   9181  C C      . VAL B 2 130 ? -0.174  -31.211 -41.311 1.00 12.26  ?  130  VAL B C      1 
ATOM   9182  O O      . VAL B 2 130 ? -0.758  -31.854 -42.183 1.00 13.29  ?  130  VAL B O      1 
ATOM   9183  C CB     . VAL B 2 130 ? 2.197   -30.391 -41.712 1.00 13.90  ?  130  VAL B CB     1 
ATOM   9184  C CG1    . VAL B 2 130 ? 2.389   -31.717 -42.453 1.00 16.73  ?  130  VAL B CG1    1 
ATOM   9185  C CG2    . VAL B 2 130 ? 3.012   -29.295 -42.376 1.00 16.15  ?  130  VAL B CG2    1 
ATOM   9186  H H      . VAL B 2 130 ? 1.197   -28.714 -40.267 1.00 14.85  ?  130  VAL B H      1 
ATOM   9187  H HA     . VAL B 2 130 ? 0.436   -29.723 -42.552 1.00 14.31  ?  130  VAL B HA     1 
ATOM   9188  H HB     . VAL B 2 130 ? 2.517   -30.492 -40.802 1.00 16.68  ?  130  VAL B HB     1 
ATOM   9189  H HG11   . VAL B 2 130 ? 3.332   -31.836 -42.648 1.00 20.07  ?  130  VAL B HG11   1 
ATOM   9190  H HG12   . VAL B 2 130 ? 2.074   -32.441 -41.891 1.00 20.07  ?  130  VAL B HG12   1 
ATOM   9191  H HG13   . VAL B 2 130 ? 1.881   -31.693 -43.279 1.00 20.07  ?  130  VAL B HG13   1 
ATOM   9192  H HG21   . VAL B 2 130 ? 3.954   -29.513 -42.301 1.00 19.37  ?  130  VAL B HG21   1 
ATOM   9193  H HG22   . VAL B 2 130 ? 2.759   -29.236 -43.311 1.00 19.37  ?  130  VAL B HG22   1 
ATOM   9194  H HG23   . VAL B 2 130 ? 2.830   -28.453 -41.930 1.00 19.37  ?  130  VAL B HG23   1 
ATOM   9195  N N      . ARG B 2 131 ? -0.251  -31.542 -40.027 1.00 13.11  ?  131  ARG B N      1 
ATOM   9196  C CA     . ARG B 2 131 ? -1.089  -32.646 -39.579 1.00 13.67  ?  131  ARG B CA     1 
ATOM   9197  C C      . ARG B 2 131 ? -2.560  -32.369 -39.861 1.00 13.07  ?  131  ARG B C      1 
ATOM   9198  O O      . ARG B 2 131 ? -3.276  -33.240 -40.378 1.00 12.47  ?  131  ARG B O      1 
ATOM   9199  C CB     . ARG B 2 131 ? -0.865  -32.846 -38.074 1.00 14.02  ?  131  ARG B CB     1 
ATOM   9200  C CG     . ARG B 2 131 ? 0.486   -33.437 -37.727 1.00 14.40  ?  131  ARG B CG     1 
ATOM   9201  C CD     . ARG B 2 131 ? 0.960   -33.057 -36.307 1.00 16.70  ?  131  ARG B CD     1 
ATOM   9202  N NE     . ARG B 2 131 ? 2.249   -33.704 -36.058 1.00 19.40  ?  131  ARG B NE     1 
ATOM   9203  C CZ     . ARG B 2 131 ? 2.486   -34.637 -35.138 1.00 17.00  ?  131  ARG B CZ     1 
ATOM   9204  N NH1    . ARG B 2 131 ? 1.537   -35.036 -34.307 1.00 15.85  ?  131  ARG B NH1    1 
ATOM   9205  N NH2    . ARG B 2 131 ? 3.696   -35.159 -35.044 1.00 19.88  ?  131  ARG B NH2    1 
ATOM   9206  H H      . ARG B 2 131 ? 0.172   -31.143 -39.393 1.00 15.73  ?  131  ARG B H      1 
ATOM   9207  H HA     . ARG B 2 131 ? -0.843  -33.456 -40.053 1.00 16.40  ?  131  ARG B HA     1 
ATOM   9208  H HB2    . ARG B 2 131 ? -0.934  -31.986 -37.633 1.00 16.82  ?  131  ARG B HB2    1 
ATOM   9209  H HB3    . ARG B 2 131 ? -1.547  -33.448 -37.736 1.00 16.82  ?  131  ARG B HB3    1 
ATOM   9210  H HG2    . ARG B 2 131 ? 0.430   -34.404 -37.774 1.00 17.27  ?  131  ARG B HG2    1 
ATOM   9211  H HG3    . ARG B 2 131 ? 1.145   -33.111 -38.359 1.00 17.27  ?  131  ARG B HG3    1 
ATOM   9212  H HD2    . ARG B 2 131 ? 1.070   -32.096 -36.239 1.00 20.04  ?  131  ARG B HD2    1 
ATOM   9213  H HD3    . ARG B 2 131 ? 0.318   -33.365 -35.648 1.00 20.04  ?  131  ARG B HD3    1 
ATOM   9214  H HE     . ARG B 2 131 ? 2.911   -33.461 -36.550 1.00 23.28  ?  131  ARG B HE     1 
ATOM   9215  H HH11   . ARG B 2 131 ? 0.750   -34.692 -34.356 1.00 19.01  ?  131  ARG B HH11   1 
ATOM   9216  H HH12   . ARG B 2 131 ? 1.706   -35.639 -33.718 1.00 19.01  ?  131  ARG B HH12   1 
ATOM   9217  H HH21   . ARG B 2 131 ? 4.320   -34.895 -35.574 1.00 23.85  ?  131  ARG B HH21   1 
ATOM   9218  H HH22   . ARG B 2 131 ? 3.860   -35.762 -34.453 1.00 23.85  ?  131  ARG B HH22   1 
ATOM   9219  N N      . TYR B 2 132 ? -3.017  -31.163 -39.510 1.00 13.42  ?  132  TYR B N      1 
ATOM   9220  C CA     . TYR B 2 132 ? -4.408  -30.768 -39.702 1.00 12.80  ?  132  TYR B CA     1 
ATOM   9221  C C      . TYR B 2 132 ? -4.771  -30.818 -41.181 1.00 11.69  ?  132  TYR B C      1 
ATOM   9222  O O      . TYR B 2 132 ? -5.799  -31.385 -41.559 1.00 12.83  ?  132  TYR B O      1 
ATOM   9223  C CB     . TYR B 2 132 ? -4.584  -29.352 -39.126 1.00 14.17  ?  132  TYR B CB     1 
ATOM   9224  C CG     . TYR B 2 132 ? -6.005  -28.825 -39.057 1.00 13.45  ?  132  TYR B CG     1 
ATOM   9225  C CD1    . TYR B 2 132 ? -6.550  -28.127 -40.128 1.00 13.99  ?  132  TYR B CD1    1 
ATOM   9226  C CD2    . TYR B 2 132 ? -6.787  -29.000 -37.934 1.00 13.96  ?  132  TYR B CD2    1 
ATOM   9227  C CE1    . TYR B 2 132 ? -7.849  -27.623 -40.075 1.00 14.02  ?  132  TYR B CE1    1 
ATOM   9228  C CE2    . TYR B 2 132 ? -8.084  -28.521 -37.874 1.00 15.53  ?  132  TYR B CE2    1 
ATOM   9229  C CZ     . TYR B 2 132 ? -8.618  -27.824 -38.952 1.00 14.02  ?  132  TYR B CZ     1 
ATOM   9230  O OH     . TYR B 2 132 ? -9.912  -27.347 -38.911 1.00 16.40  ?  132  TYR B OH     1 
ATOM   9231  H H      . TYR B 2 132 ? -2.535  -30.547 -39.154 1.00 16.10  ?  132  TYR B H      1 
ATOM   9232  H HA     . TYR B 2 132 ? -5.008  -31.370 -39.234 1.00 15.36  ?  132  TYR B HA     1 
ATOM   9233  H HB2    . TYR B 2 132 ? -4.234  -29.349 -38.221 1.00 17.00  ?  132  TYR B HB2    1 
ATOM   9234  H HB3    . TYR B 2 132 ? -4.078  -28.737 -39.679 1.00 17.00  ?  132  TYR B HB3    1 
ATOM   9235  H HD1    . TYR B 2 132 ? -6.040  -27.994 -40.894 1.00 16.79  ?  132  TYR B HD1    1 
ATOM   9236  H HD2    . TYR B 2 132 ? -6.435  -29.451 -37.201 1.00 16.75  ?  132  TYR B HD2    1 
ATOM   9237  H HE1    . TYR B 2 132 ? -8.196  -27.152 -40.798 1.00 16.81  ?  132  TYR B HE1    1 
ATOM   9238  H HE2    . TYR B 2 132 ? -8.598  -28.665 -37.112 1.00 18.63  ?  132  TYR B HE2    1 
ATOM   9239  H HH     . TYR B 2 132 ? -10.052 -26.839 -39.566 1.00 19.67  ?  132  TYR B HH     1 
ATOM   9240  N N      . TYR B 2 133 ? -3.901  -30.269 -42.025 1.00 11.75  ?  133  TYR B N      1 
ATOM   9241  C CA     . TYR B 2 133 ? -4.104  -30.267 -43.475 1.00 11.38  ?  133  TYR B CA     1 
ATOM   9242  C C      . TYR B 2 133 ? -4.374  -31.666 -44.013 1.00 11.74  ?  133  TYR B C      1 
ATOM   9243  O O      . TYR B 2 133 ? -5.363  -31.897 -44.715 1.00 12.80  ?  133  TYR B O      1 
ATOM   9244  C CB     . TYR B 2 133 ? -2.846  -29.648 -44.106 1.00 12.14  ?  133  TYR B CB     1 
ATOM   9245  C CG     . TYR B 2 133 ? -2.791  -29.651 -45.628 1.00 12.69  ?  133  TYR B CG     1 
ATOM   9246  C CD1    . TYR B 2 133 ? -2.233  -30.725 -46.308 1.00 15.58  ?  133  TYR B CD1    1 
ATOM   9247  C CD2    . TYR B 2 133 ? -3.223  -28.577 -46.363 1.00 14.07  ?  133  TYR B CD2    1 
ATOM   9248  C CE1    . TYR B 2 133 ? -2.152  -30.737 -47.667 1.00 19.92  ?  133  TYR B CE1    1 
ATOM   9249  C CE2    . TYR B 2 133 ? -3.143  -28.574 -47.737 1.00 16.87  ?  133  TYR B CE2    1 
ATOM   9250  C CZ     . TYR B 2 133 ? -2.603  -29.657 -48.382 1.00 21.31  ?  133  TYR B CZ     1 
ATOM   9251  O OH     . TYR B 2 133 ? -2.520  -29.673 -49.751 1.00 25.37  ?  133  TYR B OH     1 
ATOM   9252  H H      . TYR B 2 133 ? -3.171  -29.884 -41.784 1.00 14.09  ?  133  TYR B H      1 
ATOM   9253  H HA     . TYR B 2 133 ? -4.882  -29.738 -43.710 1.00 13.66  ?  133  TYR B HA     1 
ATOM   9254  H HB2    . TYR B 2 133 ? -2.788  -28.723 -43.819 1.00 14.57  ?  133  TYR B HB2    1 
ATOM   9255  H HB3    . TYR B 2 133 ? -2.074  -30.142 -43.790 1.00 14.57  ?  133  TYR B HB3    1 
ATOM   9256  H HD1    . TYR B 2 133 ? -1.908  -31.450 -45.825 1.00 18.69  ?  133  TYR B HD1    1 
ATOM   9257  H HD2    . TYR B 2 133 ? -3.576  -27.836 -45.925 1.00 16.89  ?  133  TYR B HD2    1 
ATOM   9258  H HE1    . TYR B 2 133 ? -1.794  -31.473 -48.107 1.00 23.89  ?  133  TYR B HE1    1 
ATOM   9259  H HE2    . TYR B 2 133 ? -3.453  -27.845 -48.224 1.00 20.24  ?  133  TYR B HE2    1 
ATOM   9260  H HH     . TYR B 2 133 ? -2.097  -30.353 -50.005 1.00 30.44  ?  133  TYR B HH     1 
ATOM   9261  N N      . ASN B 2 134 ? -3.520  -32.624 -43.673 1.00 11.56  ?  134  ASN B N      1 
ATOM   9262  C CA     . ASN B 2 134 ? -3.706  -33.976 -44.200 1.00 12.15  ?  134  ASN B CA     1 
ATOM   9263  C C      . ASN B 2 134 ? -4.891  -34.698 -43.560 1.00 12.18  ?  134  ASN B C      1 
ATOM   9264  O O      . ASN B 2 134 ? -5.590  -35.451 -44.236 1.00 13.31  ?  134  ASN B O      1 
ATOM   9265  C CB     . ASN B 2 134 ? -2.410  -34.760 -44.123 1.00 12.25  ?  134  ASN B CB     1 
ATOM   9266  C CG     . ASN B 2 134 ? -1.519  -34.407 -45.275 1.00 12.85  ?  134  ASN B CG     1 
ATOM   9267  O OD1    . ASN B 2 134 ? -1.798  -34.775 -46.411 1.00 14.81  ?  134  ASN B OD1    1 
ATOM   9268  N ND2    . ASN B 2 134 ? -0.502  -33.586 -45.015 1.00 14.10  ?  134  ASN B ND2    1 
ATOM   9269  H H      . ASN B 2 134 ? -2.842  -32.526 -43.153 1.00 13.87  ?  134  ASN B H      1 
ATOM   9270  H HA     . ASN B 2 134 ? -3.926  -33.914 -45.142 1.00 14.58  ?  134  ASN B HA     1 
ATOM   9271  H HB2    . ASN B 2 134 ? -1.949  -34.546 -43.297 1.00 14.69  ?  134  ASN B HB2    1 
ATOM   9272  H HB3    . ASN B 2 134 ? -2.602  -35.711 -44.159 1.00 14.69  ?  134  ASN B HB3    1 
ATOM   9273  H HD21   . ASN B 2 134 ? 0.036   -33.355 -45.645 1.00 16.91  ?  134  ASN B HD21   1 
ATOM   9274  H HD22   . ASN B 2 134 ? -0.384  -33.287 -44.218 1.00 16.91  ?  134  ASN B HD22   1 
ATOM   9275  N N      . ASN B 2 135 ? -5.156  -34.471 -42.273 1.00 13.08  ?  135  ASN B N      1 
ATOM   9276  C CA     . ASN B 2 135 ? -6.342  -35.075 -41.670 1.00 13.20  ?  135  ASN B CA     1 
ATOM   9277  C C      . ASN B 2 135 ? -7.622  -34.557 -42.327 1.00 13.50  ?  135  ASN B C      1 
ATOM   9278  O O      . ASN B 2 135 ? -8.543  -35.335 -42.619 1.00 13.83  ?  135  ASN B O      1 
ATOM   9279  C CB     . ASN B 2 135 ? -6.305  -34.829 -40.170 1.00 12.35  ?  135  ASN B CB     1 
ATOM   9280  C CG     . ASN B 2 135 ? -5.416  -35.820 -39.456 1.00 12.16  ?  135  ASN B CG     1 
ATOM   9281  O OD1    . ASN B 2 135 ? -5.319  -36.982 -39.873 1.00 13.75  ?  135  ASN B OD1    1 
ATOM   9282  N ND2    . ASN B 2 135 ? -4.736  -35.374 -38.406 1.00 13.71  ?  135  ASN B ND2    1 
ATOM   9283  H H      . ASN B 2 135 ? -4.682  -33.987 -41.743 1.00 15.69  ?  135  ASN B H      1 
ATOM   9284  H HA     . ASN B 2 135 ? -6.343  -36.036 -41.805 1.00 15.83  ?  135  ASN B HA     1 
ATOM   9285  H HB2    . ASN B 2 135 ? -5.962  -33.937 -40.001 1.00 14.81  ?  135  ASN B HB2    1 
ATOM   9286  H HB3    . ASN B 2 135 ? -7.202  -34.912 -39.810 1.00 14.81  ?  135  ASN B HB3    1 
ATOM   9287  H HD21   . ASN B 2 135 ? -4.218  -35.906 -37.972 1.00 16.45  ?  135  ASN B HD21   1 
ATOM   9288  H HD22   . ASN B 2 135 ? -4.813  -34.554 -38.160 1.00 16.45  ?  135  ASN B HD22   1 
ATOM   9289  N N      . VAL B 2 136 ? -7.690  -33.245 -42.595 1.00 14.86  ?  136  VAL B N      1 
ATOM   9290  C CA     . VAL B 2 136 ? -8.887  -32.666 -43.217 1.00 13.32  ?  136  VAL B CA     1 
ATOM   9291  C C      . VAL B 2 136 ? -9.098  -33.231 -44.615 1.00 12.42  ?  136  VAL B C      1 
ATOM   9292  O O      . VAL B 2 136 ? -10.233 -33.453 -45.057 1.00 14.22  ?  136  VAL B O      1 
ATOM   9293  C CB     . VAL B 2 136 ? -8.795  -31.128 -43.223 1.00 16.11  ?  136  VAL B CB     1 
ATOM   9294  C CG1    . VAL B 2 136 ? -9.854  -30.534 -44.141 1.00 17.12  ?  136  VAL B CG1    1 
ATOM   9295  C CG2    . VAL B 2 136 ? -8.957  -30.608 -41.813 1.00 18.33  ?  136  VAL B CG2    1 
ATOM   9296  H H      . VAL B 2 136 ? -7.066  -32.676 -42.429 1.00 17.83  ?  136  VAL B H      1 
ATOM   9297  H HA     . VAL B 2 136 ? -9.659  -32.915 -42.685 1.00 15.98  ?  136  VAL B HA     1 
ATOM   9298  H HB     . VAL B 2 136 ? -7.927  -30.855 -43.560 1.00 19.33  ?  136  VAL B HB     1 
ATOM   9299  H HG11   . VAL B 2 136 ? -9.958  -29.592 -43.935 1.00 20.54  ?  136  VAL B HG11   1 
ATOM   9300  H HG12   . VAL B 2 136 ? -9.570  -30.643 -45.062 1.00 20.54  ?  136  VAL B HG12   1 
ATOM   9301  H HG13   . VAL B 2 136 ? -10.693 -30.999 -43.996 1.00 20.54  ?  136  VAL B HG13   1 
ATOM   9302  H HG21   . VAL B 2 136 ? -8.829  -29.647 -41.814 1.00 21.99  ?  136  VAL B HG21   1 
ATOM   9303  H HG22   . VAL B 2 136 ? -9.848  -30.823 -41.497 1.00 21.99  ?  136  VAL B HG22   1 
ATOM   9304  H HG23   . VAL B 2 136 ? -8.294  -31.030 -41.243 1.00 21.99  ?  136  VAL B HG23   1 
ATOM   9305  N N      . LEU B 2 137 ? -8.018  -33.462 -45.335 1.00 13.93  ?  137  LEU B N      1 
ATOM   9306  C CA     . LEU B 2 137 ? -8.114  -34.018 -46.677 1.00 13.80  ?  137  LEU B CA     1 
ATOM   9307  C C      . LEU B 2 137 ? -8.351  -35.518 -46.677 1.00 14.43  ?  137  LEU B C      1 
ATOM   9308  O O      . LEU B 2 137 ? -8.396  -36.114 -47.763 1.00 15.57  ?  137  LEU B O      1 
ATOM   9309  C CB     . LEU B 2 137 ? -6.852  -33.703 -47.477 1.00 14.69  ?  137  LEU B CB     1 
ATOM   9310  C CG     . LEU B 2 137 ? -6.575  -32.268 -47.877 1.00 14.43  ?  137  LEU B CG     1 
ATOM   9311  C CD1    . LEU B 2 137 ? -5.280  -32.208 -48.692 1.00 16.43  ?  137  LEU B CD1    1 
ATOM   9312  C CD2    . LEU B 2 137 ? -7.722  -31.714 -48.667 1.00 15.25  ?  137  LEU B CD2    1 
ATOM   9313  H H      . LEU B 2 137 ? -7.214  -33.306 -45.072 1.00 16.72  ?  137  LEU B H      1 
ATOM   9314  H HA     . LEU B 2 137 ? -8.862  -33.596 -47.129 1.00 16.56  ?  137  LEU B HA     1 
ATOM   9315  H HB2    . LEU B 2 137 ? -6.093  -33.991 -46.946 1.00 17.63  ?  137  LEU B HB2    1 
ATOM   9316  H HB3    . LEU B 2 137 ? -6.894  -34.214 -48.300 1.00 17.63  ?  137  LEU B HB3    1 
ATOM   9317  H HG     . LEU B 2 137 ? -6.470  -31.720 -47.084 1.00 17.31  ?  137  LEU B HG     1 
ATOM   9318  H HD11   . LEU B 2 137 ? -5.116  -31.290 -48.957 1.00 19.71  ?  137  LEU B HD11   1 
ATOM   9319  H HD12   . LEU B 2 137 ? -4.547  -32.530 -48.144 1.00 19.71  ?  137  LEU B HD12   1 
ATOM   9320  H HD13   . LEU B 2 137 ? -5.376  -32.768 -49.478 1.00 19.71  ?  137  LEU B HD13   1 
ATOM   9321  H HD21   . LEU B 2 137 ? -7.463  -30.858 -49.043 1.00 18.29  ?  137  LEU B HD21   1 
ATOM   9322  H HD22   . LEU B 2 137 ? -7.944  -32.334 -49.380 1.00 18.29  ?  137  LEU B HD22   1 
ATOM   9323  H HD23   . LEU B 2 137 ? -8.485  -31.600 -48.079 1.00 18.29  ?  137  LEU B HD23   1 
ATOM   9324  N N      . GLY B 2 138 ? -8.482  -36.147 -45.515 1.00 13.64  ?  138  GLY B N      1 
ATOM   9325  C CA     . GLY B 2 138 ? -8.717  -37.578 -45.485 1.00 13.54  ?  138  GLY B CA     1 
ATOM   9326  C C      . GLY B 2 138 ? -7.512  -38.414 -45.843 1.00 13.14  ?  138  GLY B C      1 
ATOM   9327  O O      . GLY B 2 138 ? -7.651  -39.497 -46.432 1.00 14.02  ?  138  GLY B O      1 
ATOM   9328  H H      . GLY B 2 138 ? -8.439  -35.772 -44.742 1.00 16.36  ?  138  GLY B H      1 
ATOM   9329  H HA2    . GLY B 2 138 ? -8.999  -37.830 -44.592 1.00 16.24  ?  138  GLY B HA2    1 
ATOM   9330  H HA3    . GLY B 2 138 ? -9.425  -37.791 -46.112 1.00 16.24  ?  138  GLY B HA3    1 
ATOM   9331  N N      . ARG B 2 139 ? -6.324  -37.926 -45.503 1.00 13.15  ?  139  ARG B N      1 
ATOM   9332  C CA     . ARG B 2 139 ? -5.055  -38.593 -45.769 1.00 12.45  ?  139  ARG B CA     1 
ATOM   9333  C C      . ARG B 2 139 ? -4.345  -38.814 -44.443 1.00 11.86  ?  139  ARG B C      1 
ATOM   9334  O O      . ARG B 2 139 ? -3.286  -38.231 -44.177 1.00 14.06  ?  139  ARG B O      1 
ATOM   9335  C CB     . ARG B 2 139 ? -4.194  -37.775 -46.725 1.00 13.12  ?  139  ARG B CB     1 
ATOM   9336  C CG     . ARG B 2 139 ? -4.928  -37.423 -48.025 1.00 13.37  ?  139  ARG B CG     1 
ATOM   9337  C CD     . ARG B 2 139 ? -4.053  -36.905 -49.125 1.00 13.00  ?  139  ARG B CD     1 
ATOM   9338  N NE     . ARG B 2 139 ? -3.269  -35.732 -48.750 1.00 11.75  ?  139  ARG B NE     1 
ATOM   9339  C CZ     . ARG B 2 139 ? -2.583  -34.981 -49.591 1.00 12.22  ?  139  ARG B CZ     1 
ATOM   9340  N NH1    . ARG B 2 139 ? -2.698  -35.184 -50.902 1.00 13.31  ?  139  ARG B NH1    1 
ATOM   9341  N NH2    . ARG B 2 139 ? -1.800  -34.029 -49.140 1.00 13.70  ?  139  ARG B NH2    1 
ATOM   9342  H H      . ARG B 2 139 ? -6.226  -37.174 -45.097 1.00 15.78  ?  139  ARG B H      1 
ATOM   9343  H HA     . ARG B 2 139 ? -5.213  -39.451 -46.192 1.00 14.94  ?  139  ARG B HA     1 
ATOM   9344  H HB2    . ARG B 2 139 ? -3.938  -36.947 -46.289 1.00 15.74  ?  139  ARG B HB2    1 
ATOM   9345  H HB3    . ARG B 2 139 ? -3.402  -38.287 -46.955 1.00 15.74  ?  139  ARG B HB3    1 
ATOM   9346  H HG2    . ARG B 2 139 ? -5.368  -38.221 -48.356 1.00 16.05  ?  139  ARG B HG2    1 
ATOM   9347  H HG3    . ARG B 2 139 ? -5.586  -36.737 -47.831 1.00 16.05  ?  139  ARG B HG3    1 
ATOM   9348  H HD2    . ARG B 2 139 ? -3.434  -37.603 -49.387 1.00 15.60  ?  139  ARG B HD2    1 
ATOM   9349  H HD3    . ARG B 2 139 ? -4.612  -36.657 -49.878 1.00 15.60  ?  139  ARG B HD3    1 
ATOM   9350  H HE     . ARG B 2 139 ? -3.252  -35.515 -47.918 1.00 14.10  ?  139  ARG B HE     1 
ATOM   9351  H HH11   . ARG B 2 139 ? -3.217  -35.803 -51.198 1.00 15.97  ?  139  ARG B HH11   1 
ATOM   9352  H HH12   . ARG B 2 139 ? -2.253  -34.696 -51.453 1.00 15.97  ?  139  ARG B HH12   1 
ATOM   9353  H HH21   . ARG B 2 139 ? -1.731  -33.893 -48.294 1.00 16.44  ?  139  ARG B HH21   1 
ATOM   9354  H HH22   . ARG B 2 139 ? -1.355  -33.541 -49.691 1.00 16.44  ?  139  ARG B HH22   1 
ATOM   9355  N N      . PRO B 2 140 ? -4.921  -39.639 -43.565 1.00 11.79  ?  140  PRO B N      1 
ATOM   9356  C CA     . PRO B 2 140 ? -4.338  -39.784 -42.223 1.00 12.66  ?  140  PRO B CA     1 
ATOM   9357  C C      . PRO B 2 140 ? -2.940  -40.346 -42.212 1.00 12.60  ?  140  PRO B C      1 
ATOM   9358  O O      . PRO B 2 140 ? -2.241  -40.168 -41.215 1.00 14.06  ?  140  PRO B O      1 
ATOM   9359  C CB     . PRO B 2 140 ? -5.319  -40.722 -41.498 1.00 15.10  ?  140  PRO B CB     1 
ATOM   9360  C CG     . PRO B 2 140 ? -6.004  -41.482 -42.603 1.00 16.47  ?  140  PRO B CG     1 
ATOM   9361  C CD     . PRO B 2 140 ? -6.132  -40.461 -43.728 1.00 12.99  ?  140  PRO B CD     1 
ATOM   9362  H HA     . PRO B 2 140 ? -4.335  -38.919 -41.783 1.00 15.19  ?  140  PRO B HA     1 
ATOM   9363  H HB2    . PRO B 2 140 ? -4.832  -41.323 -40.912 1.00 18.12  ?  140  PRO B HB2    1 
ATOM   9364  H HB3    . PRO B 2 140 ? -5.957  -40.203 -40.984 1.00 18.12  ?  140  PRO B HB3    1 
ATOM   9365  H HG2    . PRO B 2 140 ? -5.461  -42.238 -42.876 1.00 19.75  ?  140  PRO B HG2    1 
ATOM   9366  H HG3    . PRO B 2 140 ? -6.875  -41.789 -42.308 1.00 19.75  ?  140  PRO B HG3    1 
ATOM   9367  H HD2    . PRO B 2 140 ? -6.141  -40.898 -44.594 1.00 15.59  ?  140  PRO B HD2    1 
ATOM   9368  H HD3    . PRO B 2 140 ? -6.933  -39.924 -43.620 1.00 15.59  ?  140  PRO B HD3    1 
ATOM   9369  N N      . GLN B 2 141 ? -2.519  -41.047 -43.261 1.00 12.96  ?  141  GLN B N      1 
ATOM   9370  C CA     . GLN B 2 141 ? -1.173  -41.590 -43.303 1.00 12.92  ?  141  GLN B CA     1 
ATOM   9371  C C      . GLN B 2 141 ? -0.130  -40.598 -43.801 1.00 12.86  ?  141  GLN B C      1 
ATOM   9372  O O      . GLN B 2 141 ? 1.071   -40.833 -43.606 1.00 14.23  ?  141  GLN B O      1 
ATOM   9373  C CB     . GLN B 2 141 ? -1.111  -42.828 -44.203 1.00 15.71  ?  141  GLN B CB     1 
ATOM   9374  C CG     . GLN B 2 141 ? -1.975  -43.940 -43.748 1.00 18.11  ?  141  GLN B CG     1 
ATOM   9375  C CD     . GLN B 2 141 ? -2.050  -45.076 -44.733 1.00 22.29  ?  141  GLN B CD     1 
ATOM   9376  O OE1    . GLN B 2 141 ? -1.612  -44.969 -45.901 1.00 24.37  ?  141  GLN B OE1    1 
ATOM   9377  N NE2    . GLN B 2 141 ? -2.569  -46.193 -44.268 1.00 22.60  ?  141  GLN B NE2    1 
ATOM   9378  H H      . GLN B 2 141 ? -2.995  -41.219 -43.957 1.00 15.55  ?  141  GLN B H      1 
ATOM   9379  H HA     . GLN B 2 141 ? -0.942  -41.855 -42.399 1.00 15.50  ?  141  GLN B HA     1 
ATOM   9380  H HB2    . GLN B 2 141 ? -1.395  -42.579 -45.096 1.00 18.84  ?  141  GLN B HB2    1 
ATOM   9381  H HB3    . GLN B 2 141 ? -0.197  -43.153 -44.225 1.00 18.84  ?  141  GLN B HB3    1 
ATOM   9382  H HG2    . GLN B 2 141 ? -1.623  -44.291 -42.915 1.00 21.73  ?  141  GLN B HG2    1 
ATOM   9383  H HG3    . GLN B 2 141 ? -2.875  -43.604 -43.612 1.00 21.73  ?  141  GLN B HG3    1 
ATOM   9384  H HE21   . GLN B 2 141 ? -2.837  -46.235 -43.452 1.00 27.12  ?  141  GLN B HE21   1 
ATOM   9385  H HE22   . GLN B 2 141 ? -2.641  -46.880 -44.781 1.00 27.12  ?  141  GLN B HE22   1 
ATOM   9386  N N      . LYS B 2 142 ? -0.548  -39.508 -44.438 1.00 12.17  ?  142  LYS B N      1 
ATOM   9387  C CA     . LYS B 2 142 ? 0.394   -38.610 -45.106 1.00 12.30  ?  142  LYS B CA     1 
ATOM   9388  C C      . LYS B 2 142 ? 0.820   -37.582 -44.065 1.00 13.23  ?  142  LYS B C      1 
ATOM   9389  O O      . LYS B 2 142 ? 0.236   -36.505 -43.938 1.00 13.03  ?  142  LYS B O      1 
ATOM   9390  C CB     . LYS B 2 142 ? -0.244  -37.997 -46.341 1.00 12.71  ?  142  LYS B CB     1 
ATOM   9391  C CG     . LYS B 2 142 ? 0.729   -37.275 -47.244 1.00 13.63  ?  142  LYS B CG     1 
ATOM   9392  C CD     . LYS B 2 142 ? 0.112   -37.019 -48.602 1.00 14.12  ?  142  LYS B CD     1 
ATOM   9393  C CE     . LYS B 2 142 ? 0.967   -36.162 -49.519 1.00 14.47  ?  142  LYS B CE     1 
ATOM   9394  N NZ     . LYS B 2 142 ? 2.156   -36.840 -50.101 1.00 14.48  ?  142  LYS B NZ     1 
ATOM   9395  H H      . LYS B 2 142 ? -1.372  -39.268 -44.498 1.00 14.60  ?  142  LYS B H      1 
ATOM   9396  H HA     . LYS B 2 142 ? 1.185   -39.085 -45.406 1.00 14.76  ?  142  LYS B HA     1 
ATOM   9397  H HB2    . LYS B 2 142 ? -0.659  -38.705 -46.860 1.00 15.25  ?  142  LYS B HB2    1 
ATOM   9398  H HB3    . LYS B 2 142 ? -0.916  -37.357 -46.058 1.00 15.25  ?  142  LYS B HB3    1 
ATOM   9399  H HG2    . LYS B 2 142 ? 0.966   -36.422 -46.848 1.00 16.35  ?  142  LYS B HG2    1 
ATOM   9400  H HG3    . LYS B 2 142 ? 1.524   -37.818 -47.363 1.00 16.35  ?  142  LYS B HG3    1 
ATOM   9401  H HD2    . LYS B 2 142 ? -0.030  -37.871 -49.045 1.00 16.94  ?  142  LYS B HD2    1 
ATOM   9402  H HD3    . LYS B 2 142 ? -0.735  -36.564 -48.479 1.00 16.94  ?  142  LYS B HD3    1 
ATOM   9403  H HE2    . LYS B 2 142 ? 0.416   -35.861 -50.259 1.00 17.36  ?  142  LYS B HE2    1 
ATOM   9404  H HE3    . LYS B 2 142 ? 1.288   -35.399 -49.013 1.00 17.36  ?  142  LYS B HE3    1 
ATOM   9405  H HZ1    . LYS B 2 142 ? 2.600   -36.278 -50.629 1.00 17.37  ?  142  LYS B HZ1    1 
ATOM   9406  H HZ2    . LYS B 2 142 ? 2.698   -37.115 -49.451 1.00 17.37  ?  142  LYS B HZ2    1 
ATOM   9407  H HZ3    . LYS B 2 142 ? 1.900   -37.545 -50.580 1.00 17.37  ?  142  LYS B HZ3    1 
ATOM   9408  N N      . LYS B 2 143 ? 1.867   -37.932 -43.301 1.00 13.05  ?  143  LYS B N      1 
ATOM   9409  C CA     . LYS B 2 143 ? 2.228   -37.167 -42.111 1.00 14.08  ?  143  LYS B CA     1 
ATOM   9410  C C      . LYS B 2 143 ? 3.719   -36.982 -41.882 1.00 13.55  ?  143  LYS B C      1 
ATOM   9411  O O      . LYS B 2 143 ? 4.095   -36.123 -41.066 1.00 13.81  ?  143  LYS B O      1 
ATOM   9412  C CB     . LYS B 2 143 ? 1.647   -37.856 -40.863 1.00 14.30  ?  143  LYS B CB     1 
ATOM   9413  C CG     . LYS B 2 143 ? 0.113   -37.989 -40.873 1.00 13.14  ?  143  LYS B CG     1 
ATOM   9414  C CD     . LYS B 2 143 ? -0.553  -36.614 -40.758 1.00 12.01  ?  143  LYS B CD     1 
ATOM   9415  C CE     . LYS B 2 143 ? -2.038  -36.742 -40.924 1.00 13.55  ?  143  LYS B CE     1 
ATOM   9416  N NZ     . LYS B 2 143 ? -2.606  -37.668 -39.913 1.00 14.43  ?  143  LYS B NZ     1 
ATOM   9417  H H      . LYS B 2 143 ? 2.377   -38.606 -43.455 1.00 15.66  ?  143  LYS B H      1 
ATOM   9418  H HA     . LYS B 2 143 ? 1.845   -36.280 -42.200 1.00 16.89  ?  143  LYS B HA     1 
ATOM   9419  H HB2    . LYS B 2 143 ? 2.020   -38.749 -40.800 1.00 17.16  ?  143  LYS B HB2    1 
ATOM   9420  H HB3    . LYS B 2 143 ? 1.893   -37.338 -40.080 1.00 17.16  ?  143  LYS B HB3    1 
ATOM   9421  H HG2    . LYS B 2 143 ? -0.171  -38.401 -41.704 1.00 15.76  ?  143  LYS B HG2    1 
ATOM   9422  H HG3    . LYS B 2 143 ? -0.170  -38.532 -40.120 1.00 15.76  ?  143  LYS B HG3    1 
ATOM   9423  H HD2    . LYS B 2 143 ? -0.370  -36.234 -39.884 1.00 14.41  ?  143  LYS B HD2    1 
ATOM   9424  H HD3    . LYS B 2 143 ? -0.213  -36.027 -41.452 1.00 14.41  ?  143  LYS B HD3    1 
ATOM   9425  H HE2    . LYS B 2 143 ? -2.452  -35.872 -40.811 1.00 16.25  ?  143  LYS B HE2    1 
ATOM   9426  H HE3    . LYS B 2 143 ? -2.235  -37.092 -41.807 1.00 16.25  ?  143  LYS B HE3    1 
ATOM   9427  H HZ1    . LYS B 2 143 ? -3.493  -37.595 -39.898 1.00 17.31  ?  143  LYS B HZ1    1 
ATOM   9428  H HZ2    . LYS B 2 143 ? -2.389  -38.508 -40.113 1.00 17.31  ?  143  LYS B HZ2    1 
ATOM   9429  H HZ3    . LYS B 2 143 ? -2.286  -37.471 -39.106 1.00 17.31  ?  143  LYS B HZ3    1 
ATOM   9430  N N      . LYS B 2 144 ? 4.592   -37.752 -42.515 1.00 13.74  ?  144  LYS B N      1 
ATOM   9431  C CA     . LYS B 2 144 ? 6.006   -37.642 -42.205 1.00 12.92  ?  144  LYS B CA     1 
ATOM   9432  C C      . LYS B 2 144 ? 6.549   -36.299 -42.676 1.00 12.38  ?  144  LYS B C      1 
ATOM   9433  O O      . LYS B 2 144 ? 6.115   -35.733 -43.697 1.00 13.08  ?  144  LYS B O      1 
ATOM   9434  C CB     . LYS B 2 144 ? 6.802   -38.792 -42.818 1.00 12.79  ?  144  LYS B CB     1 
ATOM   9435  C CG     . LYS B 2 144 ? 6.366   -40.152 -42.305 1.00 13.68  ?  144  LYS B CG     1 
ATOM   9436  C CD     . LYS B 2 144 ? 6.924   -41.288 -43.157 1.00 13.81  ?  144  LYS B CD     1 
ATOM   9437  C CE     . LYS B 2 144 ? 6.406   -42.645 -42.665 1.00 13.88  ?  144  LYS B CE     1 
ATOM   9438  N NZ     . LYS B 2 144 ? 6.702   -43.764 -43.613 1.00 16.65  ?  144  LYS B NZ     1 
ATOM   9439  H H      . LYS B 2 144 ? 4.396   -38.335 -43.116 1.00 16.48  ?  144  LYS B H      1 
ATOM   9440  H HA     . LYS B 2 144 ? 6.127   -37.698 -41.244 1.00 15.50  ?  144  LYS B HA     1 
ATOM   9441  H HB2    . LYS B 2 144 ? 6.681   -38.781 -43.780 1.00 15.35  ?  144  LYS B HB2    1 
ATOM   9442  H HB3    . LYS B 2 144 ? 7.741   -38.676 -42.601 1.00 15.35  ?  144  LYS B HB3    1 
ATOM   9443  H HG2    . LYS B 2 144 ? 6.687   -40.270 -41.397 1.00 16.41  ?  144  LYS B HG2    1 
ATOM   9444  H HG3    . LYS B 2 144 ? 5.398   -40.206 -42.325 1.00 16.41  ?  144  LYS B HG3    1 
ATOM   9445  H HD2    . LYS B 2 144 ? 6.645   -41.168 -44.079 1.00 16.57  ?  144  LYS B HD2    1 
ATOM   9446  H HD3    . LYS B 2 144 ? 7.892   -41.290 -43.101 1.00 16.57  ?  144  LYS B HD3    1 
ATOM   9447  H HE2    . LYS B 2 144 ? 6.826   -42.853 -41.816 1.00 16.66  ?  144  LYS B HE2    1 
ATOM   9448  H HE3    . LYS B 2 144 ? 5.443   -42.594 -42.555 1.00 16.66  ?  144  LYS B HE3    1 
ATOM   9449  H HZ1    . LYS B 2 144 ? 6.355   -44.523 -43.305 1.00 19.98  ?  144  LYS B HZ1    1 
ATOM   9450  H HZ2    . LYS B 2 144 ? 6.350   -43.588 -44.411 1.00 19.98  ?  144  LYS B HZ2    1 
ATOM   9451  H HZ3    . LYS B 2 144 ? 7.582   -43.863 -43.701 1.00 19.98  ?  144  LYS B HZ3    1 
ATOM   9452  N N      . VAL B 2 145 ? 7.506   -35.785 -41.925 1.00 12.81  ?  145  VAL B N      1 
ATOM   9453  C CA     . VAL B 2 145 ? 8.142   -34.509 -42.223 1.00 13.54  ?  145  VAL B CA     1 
ATOM   9454  C C      . VAL B 2 145 ? 9.636   -34.739 -42.385 1.00 12.61  ?  145  VAL B C      1 
ATOM   9455  O O      . VAL B 2 145 ? 10.285  -35.315 -41.496 1.00 14.02  ?  145  VAL B O      1 
ATOM   9456  C CB     . VAL B 2 145 ? 7.841   -33.439 -41.160 1.00 13.38  ?  145  VAL B CB     1 
ATOM   9457  C CG1    . VAL B 2 145 ? 8.616   -32.182 -41.488 1.00 15.33  ?  145  VAL B CG1    1 
ATOM   9458  C CG2    . VAL B 2 145 ? 6.345   -33.174 -41.081 1.00 13.59  ?  145  VAL B CG2    1 
ATOM   9459  H H      . VAL B 2 145 ? 7.812   -36.166 -41.218 1.00 15.37  ?  145  VAL B H      1 
ATOM   9460  H HA     . VAL B 2 145 ? 7.801   -34.178 -43.068 1.00 16.24  ?  145  VAL B HA     1 
ATOM   9461  H HB     . VAL B 2 145 ? 8.119   -33.749 -40.283 1.00 16.05  ?  145  VAL B HB     1 
ATOM   9462  H HG11   . VAL B 2 145 ? 8.253   -31.444 -40.974 1.00 18.40  ?  145  VAL B HG11   1 
ATOM   9463  H HG12   . VAL B 2 145 ? 9.549   -32.317 -41.259 1.00 18.40  ?  145  VAL B HG12   1 
ATOM   9464  H HG13   . VAL B 2 145 ? 8.532   -31.998 -42.437 1.00 18.40  ?  145  VAL B HG13   1 
ATOM   9465  H HG21   . VAL B 2 145 ? 6.183   -32.463 -40.442 1.00 16.30  ?  145  VAL B HG21   1 
ATOM   9466  H HG22   . VAL B 2 145 ? 6.024   -32.911 -41.958 1.00 16.30  ?  145  VAL B HG22   1 
ATOM   9467  H HG23   . VAL B 2 145 ? 5.895   -33.985 -40.795 1.00 16.30  ?  145  VAL B HG23   1 
ATOM   9468  N N      . ILE B 2 146 ? 10.167  -34.304 -43.527 1.00 12.89  ?  146  ILE B N      1 
ATOM   9469  C CA     . ILE B 2 146 ? 11.578  -34.466 -43.869 1.00 12.75  ?  146  ILE B CA     1 
ATOM   9470  C C      . ILE B 2 146 ? 12.277  -33.131 -43.638 1.00 13.18  ?  146  ILE B C      1 
ATOM   9471  O O      . ILE B 2 146 ? 11.928  -32.122 -44.260 1.00 14.09  ?  146  ILE B O      1 
ATOM   9472  C CB     . ILE B 2 146 ? 11.744  -34.932 -45.322 1.00 12.55  ?  146  ILE B CB     1 
ATOM   9473  C CG1    . ILE B 2 146 ? 11.084  -36.297 -45.518 1.00 12.22  ?  146  ILE B CG1    1 
ATOM   9474  C CG2    . ILE B 2 146 ? 13.232  -35.017 -45.710 1.00 15.43  ?  146  ILE B CG2    1 
ATOM   9475  C CD1    . ILE B 2 146 ? 11.128  -36.793 -46.939 1.00 14.59  ?  146  ILE B CD1    1 
ATOM   9476  H H      . ILE B 2 146 ? 9.714   -33.899 -44.136 1.00 15.47  ?  146  ILE B H      1 
ATOM   9477  H HA     . ILE B 2 146 ? 11.980  -35.127 -43.284 1.00 15.29  ?  146  ILE B HA     1 
ATOM   9478  H HB     . ILE B 2 146 ? 11.312  -34.278 -45.894 1.00 15.05  ?  146  ILE B HB     1 
ATOM   9479  H HG12   . ILE B 2 146 ? 11.542  -36.947 -44.963 1.00 14.66  ?  146  ILE B HG12   1 
ATOM   9480  H HG13   . ILE B 2 146 ? 10.152  -36.233 -45.255 1.00 14.66  ?  146  ILE B HG13   1 
ATOM   9481  H HG21   . ILE B 2 146 ? 13.303  -35.337 -46.623 1.00 18.52  ?  146  ILE B HG21   1 
ATOM   9482  H HG22   . ILE B 2 146 ? 13.629  -34.135 -45.636 1.00 18.52  ?  146  ILE B HG22   1 
ATOM   9483  H HG23   . ILE B 2 146 ? 13.680  -35.633 -45.109 1.00 18.52  ?  146  ILE B HG23   1 
ATOM   9484  H HD11   . ILE B 2 146 ? 10.577  -37.588 -47.014 1.00 17.51  ?  146  ILE B HD11   1 
ATOM   9485  H HD12   . ILE B 2 146 ? 10.788  -36.099 -47.527 1.00 17.51  ?  146  ILE B HD12   1 
ATOM   9486  H HD13   . ILE B 2 146 ? 12.046  -37.003 -47.172 1.00 17.51  ?  146  ILE B HD13   1 
ATOM   9487  N N      . ALA B 2 147 ? 13.254  -33.132 -42.736 1.00 13.45  ?  147  ALA B N      1 
ATOM   9488  C CA     . ALA B 2 147 ? 14.206  -32.053 -42.561 1.00 13.06  ?  147  ALA B CA     1 
ATOM   9489  C C      . ALA B 2 147 ? 15.550  -32.547 -43.100 1.00 14.67  ?  147  ALA B C      1 
ATOM   9490  O O      . ALA B 2 147 ? 15.642  -33.583 -43.766 1.00 14.61  ?  147  ALA B O      1 
ATOM   9491  C CB     . ALA B 2 147 ? 14.259  -31.622 -41.095 1.00 11.98  ?  147  ALA B CB     1 
ATOM   9492  H H      . ALA B 2 147 ? 13.385  -33.784 -42.190 1.00 16.14  ?  147  ALA B H      1 
ATOM   9493  H HA     . ALA B 2 147 ? 13.933  -31.268 -43.060 1.00 15.66  ?  147  ALA B HA     1 
ATOM   9494  H HB1    . ALA B 2 147 ? 14.899  -30.899 -41.001 1.00 14.37  ?  147  ALA B HB1    1 
ATOM   9495  H HB2    . ALA B 2 147 ? 13.378  -31.321 -40.822 1.00 14.37  ?  147  ALA B HB2    1 
ATOM   9496  H HB3    . ALA B 2 147 ? 14.533  -32.378 -40.553 1.00 14.37  ?  147  ALA B HB3    1 
ATOM   9497  N N      . ARG B 2 148 ? 16.615  -31.805 -42.803 1.00 15.58  ?  148  ARG B N      1 
ATOM   9498  C CA     . ARG B 2 148 ? 17.937  -32.113 -43.328 1.00 14.87  ?  148  ARG B CA     1 
ATOM   9499  C C      . ARG B 2 148 ? 18.957  -32.176 -42.208 1.00 14.61  ?  148  ARG B C      1 
ATOM   9500  O O      . ARG B 2 148 ? 18.880  -31.436 -41.225 1.00 14.55  ?  148  ARG B O      1 
ATOM   9501  C CB     . ARG B 2 148 ? 18.371  -31.069 -44.345 1.00 15.91  ?  148  ARG B CB     1 
ATOM   9502  C CG     . ARG B 2 148 ? 17.370  -30.960 -45.464 1.00 17.54  ?  148  ARG B CG     1 
ATOM   9503  C CD     . ARG B 2 148 ? 17.594  -29.837 -46.376 1.00 18.07  ?  148  ARG B CD     1 
ATOM   9504  N NE     . ARG B 2 148 ? 17.687  -28.556 -45.672 1.00 15.56  ?  148  ARG B NE     1 
ATOM   9505  C CZ     . ARG B 2 148 ? 17.997  -27.418 -46.282 1.00 14.73  ?  148  ARG B CZ     1 
ATOM   9506  N NH1    . ARG B 2 148 ? 18.230  -27.423 -47.585 1.00 15.22  ?  148  ARG B NH1    1 
ATOM   9507  N NH2    . ARG B 2 148 ? 18.127  -26.296 -45.584 1.00 15.16  ?  148  ARG B NH2    1 
ATOM   9508  H H      . ARG B 2 148 ? 16.593  -31.112 -42.294 1.00 18.69  ?  148  ARG B H      1 
ATOM   9509  H HA     . ARG B 2 148 ? 17.914  -32.986 -43.751 1.00 17.84  ?  148  ARG B HA     1 
ATOM   9510  H HB2    . ARG B 2 148 ? 18.442  -30.205 -43.911 1.00 19.09  ?  148  ARG B HB2    1 
ATOM   9511  H HB3    . ARG B 2 148 ? 19.228  -31.323 -44.723 1.00 19.09  ?  148  ARG B HB3    1 
ATOM   9512  H HG2    . ARG B 2 148 ? 17.404  -31.774 -45.990 1.00 21.04  ?  148  ARG B HG2    1 
ATOM   9513  H HG3    . ARG B 2 148 ? 16.486  -30.851 -45.079 1.00 21.04  ?  148  ARG B HG3    1 
ATOM   9514  H HD2    . ARG B 2 148 ? 18.426  -29.979 -46.855 1.00 21.68  ?  148  ARG B HD2    1 
ATOM   9515  H HD3    . ARG B 2 148 ? 16.855  -29.784 -47.002 1.00 21.68  ?  148  ARG B HD3    1 
ATOM   9516  H HE     . ARG B 2 148 ? 17.534  -28.540 -44.826 1.00 18.67  ?  148  ARG B HE     1 
ATOM   9517  H HH11   . ARG B 2 148 ? 18.180  -28.159 -48.028 1.00 18.26  ?  148  ARG B HH11   1 
ATOM   9518  H HH12   . ARG B 2 148 ? 18.432  -26.691 -47.988 1.00 18.26  ?  148  ARG B HH12   1 
ATOM   9519  H HH21   . ARG B 2 148 ? 18.010  -26.303 -44.732 1.00 18.19  ?  148  ARG B HH21   1 
ATOM   9520  H HH22   . ARG B 2 148 ? 18.328  -25.561 -45.984 1.00 18.19  ?  148  ARG B HH22   1 
ATOM   9521  N N      . GLN B 2 149 ? 19.932  -33.066 -42.375 1.00 14.64  ?  149  GLN B N      1 
ATOM   9522  C CA     . GLN B 2 149 ? 21.092  -33.026 -41.502 1.00 14.70  ?  149  GLN B CA     1 
ATOM   9523  C C      . GLN B 2 149 ? 21.663  -31.618 -41.519 1.00 14.49  ?  149  GLN B C      1 
ATOM   9524  O O      . GLN B 2 149 ? 21.732  -30.971 -42.565 1.00 15.32  ?  149  GLN B O      1 
ATOM   9525  C CB     . GLN B 2 149 ? 22.127  -34.047 -41.958 1.00 15.63  ?  149  GLN B CB     1 
ATOM   9526  C CG     . GLN B 2 149 ? 21.681  -35.503 -41.848 1.00 17.03  ?  149  GLN B CG     1 
ATOM   9527  C CD     . GLN B 2 149 ? 21.478  -35.982 -40.404 1.00 26.27  ?  149  GLN B CD     1 
ATOM   9528  O OE1    . GLN B 2 149 ? 21.596  -35.214 -39.455 1.00 32.52  ?  149  GLN B OE1    1 
ATOM   9529  N NE2    . GLN B 2 149 ? 21.159  -37.257 -40.246 1.00 30.65  ?  149  GLN B NE2    1 
ATOM   9530  H H      . GLN B 2 149 ? 19.943  -33.685 -42.972 1.00 17.57  ?  149  GLN B H      1 
ATOM   9531  H HA     . GLN B 2 149 ? 20.850  -33.259 -40.592 1.00 17.64  ?  149  GLN B HA     1 
ATOM   9532  H HB2    . GLN B 2 149 ? 22.339  -33.877 -42.889 1.00 18.75  ?  149  GLN B HB2    1 
ATOM   9533  H HB3    . GLN B 2 149 ? 22.922  -33.944 -41.412 1.00 18.75  ?  149  GLN B HB3    1 
ATOM   9534  H HG2    . GLN B 2 149 ? 20.836  -35.607 -42.314 1.00 20.44  ?  149  GLN B HG2    1 
ATOM   9535  H HG3    . GLN B 2 149 ? 22.356  -36.068 -42.255 1.00 20.44  ?  149  GLN B HG3    1 
ATOM   9536  H HE21   . GLN B 2 149 ? 21.076  -37.768 -40.933 1.00 36.78  ?  149  GLN B HE21   1 
ATOM   9537  H HE22   . GLN B 2 149 ? 21.035  -37.575 -39.456 1.00 36.78  ?  149  GLN B HE22   1 
ATOM   9538  N N      . ARG B 2 150 ? 22.013  -31.140 -40.332 1.00 13.96  ?  150  ARG B N      1 
ATOM   9539  C CA     . ARG B 2 150 ? 22.576  -29.821 -40.069 1.00 14.45  ?  150  ARG B CA     1 
ATOM   9540  C C      . ARG B 2 150 ? 21.595  -28.668 -40.237 1.00 15.40  ?  150  ARG B C      1 
ATOM   9541  O O      . ARG B 2 150 ? 21.985  -27.518 -40.084 1.00 16.18  ?  150  ARG B O      1 
ATOM   9542  C CB     . ARG B 2 150 ? 23.864  -29.573 -40.868 1.00 16.98  ?  150  ARG B CB     1 
ATOM   9543  C CG     . ARG B 2 150 ? 24.960  -30.603 -40.523 1.00 18.82  ?  150  ARG B CG     1 
ATOM   9544  C CD     . ARG B 2 150 ? 26.322  -30.176 -40.946 1.00 19.98  ?  150  ARG B CD     1 
ATOM   9545  N NE     . ARG B 2 150 ? 26.822  -29.049 -40.167 1.00 19.35  ?  150  ARG B NE     1 
ATOM   9546  C CZ     . ARG B 2 150 ? 27.803  -29.135 -39.267 1.00 20.86  ?  150  ARG B CZ     1 
ATOM   9547  N NH1    . ARG B 2 150 ? 28.377  -30.301 -38.986 1.00 22.02  ?  150  ARG B NH1    1 
ATOM   9548  N NH2    . ARG B 2 150 ? 28.193  -28.045 -38.640 1.00 19.61  ?  150  ARG B NH2    1 
ATOM   9549  H H      . ARG B 2 150 ? 21.924  -31.600 -39.611 1.00 16.75  ?  150  ARG B H      1 
ATOM   9550  H HA     . ARG B 2 150 ? 22.816  -29.804 -39.129 1.00 17.34  ?  150  ARG B HA     1 
ATOM   9551  H HB2    . ARG B 2 150 ? 23.671  -29.640 -41.816 1.00 20.37  ?  150  ARG B HB2    1 
ATOM   9552  H HB3    . ARG B 2 150 ? 24.203  -28.687 -40.661 1.00 20.37  ?  150  ARG B HB3    1 
ATOM   9553  H HG2    . ARG B 2 150 ? 24.974  -30.737 -39.562 1.00 22.58  ?  150  ARG B HG2    1 
ATOM   9554  H HG3    . ARG B 2 150 ? 24.757  -31.439 -40.971 1.00 22.58  ?  150  ARG B HG3    1 
ATOM   9555  H HD2    . ARG B 2 150 ? 26.937  -30.918 -40.831 1.00 23.98  ?  150  ARG B HD2    1 
ATOM   9556  H HD3    . ARG B 2 150 ? 26.296  -29.909 -41.878 1.00 23.98  ?  150  ARG B HD3    1 
ATOM   9557  H HE     . ARG B 2 150 ? 26.462  -28.279 -40.296 1.00 23.22  ?  150  ARG B HE     1 
ATOM   9558  H HH11   . ARG B 2 150 ? 28.118  -31.016 -39.387 1.00 26.41  ?  150  ARG B HH11   1 
ATOM   9559  H HH12   . ARG B 2 150 ? 29.009  -30.340 -38.403 1.00 26.41  ?  150  ARG B HH12   1 
ATOM   9560  H HH21   . ARG B 2 150 ? 27.817  -27.291 -38.813 1.00 23.53  ?  150  ARG B HH21   1 
ATOM   9561  H HH22   . ARG B 2 150 ? 28.825  -28.086 -38.057 1.00 23.53  ?  150  ARG B HH22   1 
ATOM   9562  N N      . GLY B 2 151 ? 20.323  -28.932 -40.496 1.00 14.79  ?  151  GLY B N      1 
ATOM   9563  C CA     . GLY B 2 151 ? 19.344  -27.877 -40.396 1.00 14.79  ?  151  GLY B CA     1 
ATOM   9564  C C      . GLY B 2 151 ? 19.157  -27.448 -38.953 1.00 13.13  ?  151  GLY B C      1 
ATOM   9565  O O      . GLY B 2 151 ? 19.430  -28.193 -38.008 1.00 14.15  ?  151  GLY B O      1 
ATOM   9566  H H      . GLY B 2 151 ? 20.010  -29.699 -40.727 1.00 17.74  ?  151  GLY B H      1 
ATOM   9567  H HA2    . GLY B 2 151 ? 19.635  -27.111 -40.914 1.00 17.74  ?  151  GLY B HA2    1 
ATOM   9568  H HA3    . GLY B 2 151 ? 18.493  -28.187 -40.742 1.00 17.74  ?  151  GLY B HA3    1 
ATOM   9569  N N      . TYR B 2 152 ? 18.683  -26.216 -38.773 1.00 12.41  ?  152  TYR B N      1 
ATOM   9570  C CA     . TYR B 2 152 ? 18.317  -25.724 -37.445 1.00 12.68  ?  152  TYR B CA     1 
ATOM   9571  C C      . TYR B 2 152 ? 16.929  -25.111 -37.508 1.00 12.77  ?  152  TYR B C      1 
ATOM   9572  O O      . TYR B 2 152 ? 16.698  -24.181 -38.290 1.00 13.18  ?  152  TYR B O      1 
ATOM   9573  C CB     . TYR B 2 152 ? 19.321  -24.728 -36.869 1.00 13.13  ?  152  TYR B CB     1 
ATOM   9574  C CG     . TYR B 2 152 ? 18.955  -24.410 -35.455 1.00 12.83  ?  152  TYR B CG     1 
ATOM   9575  C CD1    . TYR B 2 152 ? 19.254  -25.310 -34.437 1.00 14.35  ?  152  TYR B CD1    1 
ATOM   9576  C CD2    . TYR B 2 152 ? 18.252  -23.248 -35.128 1.00 14.25  ?  152  TYR B CD2    1 
ATOM   9577  C CE1    . TYR B 2 152 ? 18.879  -25.048 -33.122 1.00 15.47  ?  152  TYR B CE1    1 
ATOM   9578  C CE2    . TYR B 2 152 ? 17.873  -22.985 -33.813 1.00 15.37  ?  152  TYR B CE2    1 
ATOM   9579  C CZ     . TYR B 2 152 ? 18.188  -23.895 -32.807 1.00 15.09  ?  152  TYR B CZ     1 
ATOM   9580  O OH     . TYR B 2 152 ? 17.831  -23.697 -31.488 1.00 15.58  ?  152  TYR B OH     1 
ATOM   9581  H H      . TYR B 2 152 ? 18.564  -25.647 -39.407 1.00 14.89  ?  152  TYR B H      1 
ATOM   9582  H HA     . TYR B 2 152 ? 18.297  -26.484 -36.843 1.00 15.22  ?  152  TYR B HA     1 
ATOM   9583  H HB2    . TYR B 2 152 ? 20.211  -25.114 -36.884 1.00 15.76  ?  152  TYR B HB2    1 
ATOM   9584  H HB3    . TYR B 2 152 ? 19.306  -23.909 -37.389 1.00 15.76  ?  152  TYR B HB3    1 
ATOM   9585  H HD1    . TYR B 2 152 ? 19.710  -26.095 -34.637 1.00 17.22  ?  152  TYR B HD1    1 
ATOM   9586  H HD2    . TYR B 2 152 ? 18.035  -22.641 -35.798 1.00 17.09  ?  152  TYR B HD2    1 
ATOM   9587  H HE1    . TYR B 2 152 ? 19.095  -25.655 -32.450 1.00 18.56  ?  152  TYR B HE1    1 
ATOM   9588  H HE2    . TYR B 2 152 ? 17.411  -22.204 -33.608 1.00 18.44  ?  152  TYR B HE2    1 
ATOM   9589  H HH     . TYR B 2 152 ? 17.406  -22.977 -31.411 1.00 18.69  ?  152  TYR B HH     1 
ATOM   9590  N N      . HIS B 2 153 ? 16.018  -25.630 -36.672 1.00 12.70  ?  153  HIS B N      1 
ATOM   9591  C CA     . HIS B 2 153 ? 14.610  -25.252 -36.701 1.00 12.41  ?  153  HIS B CA     1 
ATOM   9592  C C      . HIS B 2 153 ? 14.071  -25.007 -35.306 1.00 12.22  ?  153  HIS B C      1 
ATOM   9593  O O      . HIS B 2 153 ? 12.851  -24.830 -35.157 1.00 12.89  ?  153  HIS B O      1 
ATOM   9594  C CB     . HIS B 2 153 ? 13.807  -26.348 -37.433 1.00 11.88  ?  153  HIS B CB     1 
ATOM   9595  C CG     . HIS B 2 153 ? 14.275  -26.530 -38.843 1.00 12.84  ?  153  HIS B CG     1 
ATOM   9596  N ND1    . HIS B 2 153 ? 14.131  -25.554 -39.806 1.00 12.37  ?  153  HIS B ND1    1 
ATOM   9597  C CD2    . HIS B 2 153 ? 14.948  -27.544 -39.435 1.00 14.41  ?  153  HIS B CD2    1 
ATOM   9598  C CE1    . HIS B 2 153 ? 14.692  -25.962 -40.931 1.00 13.32  ?  153  HIS B CE1    1 
ATOM   9599  N NE2    . HIS B 2 153 ? 15.201  -27.164 -40.727 1.00 13.30  ?  153  HIS B NE2    1 
ATOM   9600  H H      . HIS B 2 153 ? 16.199  -26.215 -36.068 1.00 15.24  ?  153  HIS B H      1 
ATOM   9601  H HA     . HIS B 2 153 ? 14.483  -24.427 -37.195 1.00 14.89  ?  153  HIS B HA     1 
ATOM   9602  H HB2    . HIS B 2 153 ? 13.916  -27.191 -36.965 1.00 14.26  ?  153  HIS B HB2    1 
ATOM   9603  H HB3    . HIS B 2 153 ? 12.870  -26.099 -37.453 1.00 14.26  ?  153  HIS B HB3    1 
ATOM   9604  H HD1    . HIS B 2 153 ? 13.737  -24.798 -39.692 1.00 14.84  ?  153  HIS B HD1    1 
ATOM   9605  H HD2    . HIS B 2 153 ? 15.193  -28.349 -39.038 1.00 17.29  ?  153  HIS B HD2    1 
ATOM   9606  H HE1    . HIS B 2 153 ? 14.723  -25.485 -41.728 1.00 15.98  ?  153  HIS B HE1    1 
ATOM   9607  N N      . GLY B 2 154 ? 14.938  -24.978 -34.279 1.00 12.74  ?  154  GLY B N      1 
ATOM   9608  C CA     . GLY B 2 154 ? 14.505  -24.670 -32.934 1.00 13.91  ?  154  GLY B CA     1 
ATOM   9609  C C      . GLY B 2 154 ? 14.958  -25.731 -31.960 1.00 12.41  ?  154  GLY B C      1 
ATOM   9610  O O      . GLY B 2 154 ? 15.687  -26.671 -32.312 1.00 13.40  ?  154  GLY B O      1 
ATOM   9611  H H      . GLY B 2 154 ? 15.780  -25.137 -34.355 1.00 15.28  ?  154  GLY B H      1 
ATOM   9612  H HA2    . GLY B 2 154 ? 14.875  -23.816 -32.659 1.00 16.69  ?  154  GLY B HA2    1 
ATOM   9613  H HA3    . GLY B 2 154 ? 13.536  -24.617 -32.907 1.00 16.69  ?  154  GLY B HA3    1 
ATOM   9614  N N      . SER B 2 155 ? 14.509  -25.561 -30.707 1.00 12.67  ?  155  SER B N      1 
ATOM   9615  C CA     . SER B 2 155 ? 15.111  -26.202 -29.542 1.00 12.42  ?  155  SER B CA     1 
ATOM   9616  C C      . SER B 2 155 ? 14.078  -26.835 -28.608 1.00 12.15  ?  155  SER B C      1 
ATOM   9617  O O      . SER B 2 155 ? 14.404  -27.151 -27.453 1.00 12.60  ?  155  SER B O      1 
ATOM   9618  C CB     . SER B 2 155 ? 15.947  -25.161 -28.793 1.00 12.54  ?  155  SER B CB     1 
ATOM   9619  O OG     . SER B 2 155 ? 16.694  -25.723 -27.726 1.00 13.31  ?  155  SER B OG     1 
ATOM   9620  H H      . SER B 2 155 ? 13.837  -25.063 -30.507 1.00 15.20  ?  155  SER B H      1 
ATOM   9621  H HA     . SER B 2 155 ? 15.682  -26.930 -29.834 1.00 14.90  ?  155  SER B HA     1 
ATOM   9622  H HB2    . SER B 2 155 ? 16.564  -24.752 -29.420 1.00 15.05  ?  155  SER B HB2    1 
ATOM   9623  H HB3    . SER B 2 155 ? 15.349  -24.489 -28.430 1.00 15.05  ?  155  SER B HB3    1 
ATOM   9624  H HG     . SER B 2 155 ? 16.186  -26.155 -27.216 1.00 15.97  ?  155  SER B HG     1 
ATOM   9625  N N      . GLY B 2 156 ? 12.857  -27.043 -29.065 1.00 12.58  ?  156  GLY B N      1 
ATOM   9626  C CA     . GLY B 2 156 ? 11.846  -27.755 -28.303 1.00 13.03  ?  156  GLY B CA     1 
ATOM   9627  C C      . GLY B 2 156 ? 11.884  -29.248 -28.552 1.00 12.49  ?  156  GLY B C      1 
ATOM   9628  O O      . GLY B 2 156 ? 12.866  -29.800 -29.055 1.00 14.02  ?  156  GLY B O      1 
ATOM   9629  H H      . GLY B 2 156 ? 12.582  -26.774 -29.835 1.00 15.09  ?  156  GLY B H      1 
ATOM   9630  H HA2    . GLY B 2 156 ? 11.988  -27.599 -27.356 1.00 15.63  ?  156  GLY B HA2    1 
ATOM   9631  H HA3    . GLY B 2 156 ? 10.967  -27.426 -28.549 1.00 15.63  ?  156  GLY B HA3    1 
ATOM   9632  N N      . ILE B 2 157 ? 10.792  -29.912 -28.183 1.00 12.30  ?  157  ILE B N      1 
ATOM   9633  C CA     . ILE B 2 157 ? 10.679  -31.344 -28.460 1.00 11.23  ?  157  ILE B CA     1 
ATOM   9634  C C      . ILE B 2 157 ? 10.479  -31.584 -29.955 1.00 11.23  ?  157  ILE B C      1 
ATOM   9635  O O      . ILE B 2 157 ? 11.313  -32.221 -30.614 1.00 12.34  ?  157  ILE B O      1 
ATOM   9636  C CB     . ILE B 2 157 ? 9.561   -31.976 -27.612 1.00 10.60  ?  157  ILE B CB     1 
ATOM   9637  C CG1    . ILE B 2 157 ? 9.934   -31.934 -26.132 1.00 11.70  ?  157  ILE B CG1    1 
ATOM   9638  C CG2    . ILE B 2 157 ? 9.283   -33.414 -28.037 1.00 11.33  ?  157  ILE B CG2    1 
ATOM   9639  C CD1    . ILE B 2 157 ? 11.100  -32.829 -25.706 1.00 13.16  ?  157  ILE B CD1    1 
ATOM   9640  H H      . ILE B 2 157 ? 10.115  -29.568 -27.779 1.00 14.76  ?  157  ILE B H      1 
ATOM   9641  H HA     . ILE B 2 157 ? 11.510  -31.776 -28.208 1.00 13.47  ?  157  ILE B HA     1 
ATOM   9642  H HB     . ILE B 2 157 ? 8.754   -31.456 -27.755 1.00 12.71  ?  157  ILE B HB     1 
ATOM   9643  H HG12   . ILE B 2 157 ? 10.177  -31.022 -25.906 1.00 14.03  ?  157  ILE B HG12   1 
ATOM   9644  H HG13   . ILE B 2 157 ? 9.160   -32.208 -25.616 1.00 14.03  ?  157  ILE B HG13   1 
ATOM   9645  H HG21   . ILE B 2 157 ? 8.722   -33.839 -27.369 1.00 13.59  ?  157  ILE B HG21   1 
ATOM   9646  H HG22   . ILE B 2 157 ? 8.828   -33.408 -28.894 1.00 13.59  ?  157  ILE B HG22   1 
ATOM   9647  H HG23   . ILE B 2 157 ? 10.125  -33.889 -28.113 1.00 13.59  ?  157  ILE B HG23   1 
ATOM   9648  H HD11   . ILE B 2 157 ? 11.224  -32.751 -24.747 1.00 15.79  ?  157  ILE B HD11   1 
ATOM   9649  H HD12   . ILE B 2 157 ? 10.893  -33.748 -25.939 1.00 15.79  ?  157  ILE B HD12   1 
ATOM   9650  H HD13   . ILE B 2 157 ? 11.903  -32.543 -26.168 1.00 15.79  ?  157  ILE B HD13   1 
ATOM   9651  N N      . ALA B 2 158 ? 9.384   -31.060 -30.525 1.00 10.99  ?  158  ALA B N      1 
ATOM   9652  C CA     . ALA B 2 158 ? 9.147   -31.274 -31.957 1.00 12.86  ?  158  ALA B CA     1 
ATOM   9653  C C      . ALA B 2 158 ? 10.040  -30.373 -32.815 1.00 11.83  ?  158  ALA B C      1 
ATOM   9654  O O      . ALA B 2 158 ? 10.665  -30.837 -33.782 1.00 11.55  ?  158  ALA B O      1 
ATOM   9655  C CB     . ALA B 2 158 ? 7.672   -31.042 -32.306 1.00 13.29  ?  158  ALA B CB     1 
ATOM   9656  H H      . ALA B 2 158 ? 8.785   -30.594 -30.119 1.00 13.18  ?  158  ALA B H      1 
ATOM   9657  H HA     . ALA B 2 158 ? 9.358   -32.198 -32.160 1.00 15.43  ?  158  ALA B HA     1 
ATOM   9658  H HB1    . ALA B 2 158 ? 7.533   -31.248 -33.243 1.00 15.95  ?  158  ALA B HB1    1 
ATOM   9659  H HB2    . ALA B 2 158 ? 7.122   -31.620 -31.754 1.00 15.95  ?  158  ALA B HB2    1 
ATOM   9660  H HB3    . ALA B 2 158 ? 7.450   -30.113 -32.135 1.00 15.95  ?  158  ALA B HB3    1 
ATOM   9661  N N      . SER B 2 159 ? 10.143  -29.084 -32.459 1.00 11.68  ?  159  SER B N      1 
ATOM   9662  C CA     . SER B 2 159 ? 10.981  -28.194 -33.245 1.00 11.59  ?  159  SER B CA     1 
ATOM   9663  C C      . SER B 2 159 ? 12.434  -28.650 -33.201 1.00 13.47  ?  159  SER B C      1 
ATOM   9664  O O      . SER B 2 159 ? 13.132  -28.617 -34.219 1.00 13.18  ?  159  SER B O      1 
ATOM   9665  C CB     . SER B 2 159 ? 10.827  -26.747 -32.774 1.00 11.72  ?  159  SER B CB     1 
ATOM   9666  O OG     . SER B 2 159 ? 11.332  -26.570 -31.486 1.00 14.35  ?  159  SER B OG     1 
ATOM   9667  H H      . SER B 2 159 ? 9.749   -28.717 -31.788 1.00 14.02  ?  159  SER B H      1 
ATOM   9668  H HA     . SER B 2 159 ? 10.689  -28.215 -34.169 1.00 13.91  ?  159  SER B HA     1 
ATOM   9669  H HB2    . SER B 2 159 ? 11.312  -26.167 -33.382 1.00 14.06  ?  159  SER B HB2    1 
ATOM   9670  H HB3    . SER B 2 159 ? 9.885   -26.515 -32.776 1.00 14.06  ?  159  SER B HB3    1 
ATOM   9671  H HG     . SER B 2 159 ? 10.894  -27.034 -30.939 1.00 17.21  ?  159  SER B HG     1 
ATOM   9672  N N      . GLY B 2 160 ? 12.882  -29.166 -32.053 1.00 12.04  ?  160  GLY B N      1 
ATOM   9673  C CA     . GLY B 2 160 ? 14.231  -29.694 -31.957 1.00 12.35  ?  160  GLY B CA     1 
ATOM   9674  C C      . GLY B 2 160 ? 14.420  -31.004 -32.676 1.00 11.89  ?  160  GLY B C      1 
ATOM   9675  O O      . GLY B 2 160 ? 15.558  -31.344 -33.035 1.00 12.97  ?  160  GLY B O      1 
ATOM   9676  H H      . GLY B 2 160 ? 12.426  -29.220 -31.326 1.00 14.45  ?  160  GLY B H      1 
ATOM   9677  H HA2    . GLY B 2 160 ? 14.849  -29.050 -32.337 1.00 14.81  ?  160  GLY B HA2    1 
ATOM   9678  H HA3    . GLY B 2 160 ? 14.451  -29.829 -31.022 1.00 14.81  ?  160  GLY B HA3    1 
ATOM   9679  N N      . SER B 2 161 ? 13.341  -31.764 -32.847 1.00 13.27  ?  161  SER B N      1 
ATOM   9680  C CA     . SER B 2 161 ? 13.400  -32.965 -33.669 1.00 10.70  ?  161  SER B CA     1 
ATOM   9681  C C      . SER B 2 161 ? 13.670  -32.605 -35.121 1.00 10.96  ?  161  SER B C      1 
ATOM   9682  O O      . SER B 2 161 ? 14.387  -33.329 -35.816 1.00 13.47  ?  161  SER B O      1 
ATOM   9683  C CB     . SER B 2 161 ? 12.091  -33.751 -33.525 1.00 12.39  ?  161  SER B CB     1 
ATOM   9684  O OG     . SER B 2 161 ? 11.947  -34.303 -32.229 1.00 14.19  ?  161  SER B OG     1 
ATOM   9685  H H      . SER B 2 161 ? 12.569  -31.610 -32.502 1.00 15.92  ?  161  SER B H      1 
ATOM   9686  H HA     . SER B 2 161 ? 14.122  -33.537 -33.366 1.00 12.84  ?  161  SER B HA     1 
ATOM   9687  H HB2    . SER B 2 161 ? 11.348  -33.151 -33.692 1.00 14.86  ?  161  SER B HB2    1 
ATOM   9688  H HB3    . SER B 2 161 ? 12.088  -34.472 -34.173 1.00 14.86  ?  161  SER B HB3    1 
ATOM   9689  H HG     . SER B 2 161 ? 11.978  -33.694 -31.652 1.00 17.03  ?  161  SER B HG     1 
ATOM   9690  N N      . LEU B 2 162 ? 13.066  -31.506 -35.600 1.00 11.28  ?  162  LEU B N      1 
ATOM   9691  C CA     . LEU B 2 162 ? 13.319  -31.028 -36.960 1.00 12.44  ?  162  LEU B CA     1 
ATOM   9692  C C      . LEU B 2 162 ? 14.786  -30.636 -37.136 1.00 13.15  ?  162  LEU B C      1 
ATOM   9693  O O      . LEU B 2 162 ? 15.409  -30.951 -38.148 1.00 13.32  ?  162  LEU B O      1 
ATOM   9694  C CB     . LEU B 2 162 ? 12.431  -29.821 -37.278 1.00 12.46  ?  162  LEU B CB     1 
ATOM   9695  C CG     . LEU B 2 162 ? 10.933  -30.112 -37.302 1.00 13.47  ?  162  LEU B CG     1 
ATOM   9696  C CD1    . LEU B 2 162 ? 10.169  -28.800 -37.453 1.00 14.39  ?  162  LEU B CD1    1 
ATOM   9697  C CD2    . LEU B 2 162 ? 10.578  -31.096 -38.445 1.00 12.52  ?  162  LEU B CD2    1 
ATOM   9698  H H      . LEU B 2 162 ? 12.508  -31.023 -35.159 1.00 13.53  ?  162  LEU B H      1 
ATOM   9699  H HA     . LEU B 2 162 ? 13.103  -31.743 -37.580 1.00 14.93  ?  162  LEU B HA     1 
ATOM   9700  H HB2    . LEU B 2 162 ? 12.586  -29.141 -36.604 1.00 14.95  ?  162  LEU B HB2    1 
ATOM   9701  H HB3    . LEU B 2 162 ? 12.676  -29.482 -38.153 1.00 14.95  ?  162  LEU B HB3    1 
ATOM   9702  H HG     . LEU B 2 162 ? 10.667  -30.535 -36.470 1.00 16.16  ?  162  LEU B HG     1 
ATOM   9703  H HD11   . LEU B 2 162 ? 9.218   -28.989 -37.481 1.00 17.26  ?  162  LEU B HD11   1 
ATOM   9704  H HD12   . LEU B 2 162 ? 10.370  -28.228 -36.696 1.00 17.26  ?  162  LEU B HD12   1 
ATOM   9705  H HD13   . LEU B 2 162 ? 10.444  -28.367 -38.277 1.00 17.26  ?  162  LEU B HD13   1 
ATOM   9706  H HD21   . LEU B 2 162 ? 9.615   -31.210 -38.477 1.00 15.02  ?  162  LEU B HD21   1 
ATOM   9707  H HD22   . LEU B 2 162 ? 10.896  -30.731 -39.286 1.00 15.02  ?  162  LEU B HD22   1 
ATOM   9708  H HD23   . LEU B 2 162 ? 11.006  -31.949 -38.272 1.00 15.02  ?  162  LEU B HD23   1 
ATOM   9709  N N      . THR B 2 163 ? 15.340  -29.924 -36.168 1.00 12.63  ?  163  THR B N      1 
ATOM   9710  C CA     . THR B 2 163 ? 16.765  -29.620 -36.159 1.00 11.44  ?  163  THR B CA     1 
ATOM   9711  C C      . THR B 2 163 ? 17.575  -30.876 -36.399 1.00 11.68  ?  163  THR B C      1 
ATOM   9712  O O      . THR B 2 163 ? 17.199  -31.975 -35.967 1.00 12.96  ?  163  THR B O      1 
ATOM   9713  C CB     . THR B 2 163 ? 17.075  -28.982 -34.808 1.00 13.03  ?  163  THR B CB     1 
ATOM   9714  O OG1    . THR B 2 163 ? 16.441  -27.695 -34.786 1.00 13.73  ?  163  THR B OG1    1 
ATOM   9715  C CG2    . THR B 2 163 ? 18.567  -28.830 -34.552 1.00 13.35  ?  163  THR B CG2    1 
ATOM   9716  H H      . THR B 2 163 ? 14.913  -29.600 -35.496 1.00 15.16  ?  163  THR B H      1 
ATOM   9717  H HA     . THR B 2 163 ? 17.014  -29.003 -36.865 1.00 13.72  ?  163  THR B HA     1 
ATOM   9718  H HB     . THR B 2 163 ? 16.745  -29.551 -34.095 1.00 15.63  ?  163  THR B HB     1 
ATOM   9719  H HG1    . THR B 2 163 ? 16.529  -27.344 -34.028 1.00 16.47  ?  163  THR B HG1    1 
ATOM   9720  H HG21   . THR B 2 163 ? 18.715  -28.277 -33.769 1.00 16.02  ?  163  THR B HG21   1 
ATOM   9721  H HG22   . THR B 2 163 ? 18.969  -29.701 -34.403 1.00 16.02  ?  163  THR B HG22   1 
ATOM   9722  H HG23   . THR B 2 163 ? 18.995  -28.413 -35.317 1.00 16.02  ?  163  THR B HG23   1 
ATOM   9723  N N      . GLY B 2 164 ? 18.673  -30.712 -37.134 1.00 12.50  ?  164  GLY B N      1 
ATOM   9724  C CA     . GLY B 2 164 ? 19.512  -31.834 -37.535 1.00 12.49  ?  164  GLY B CA     1 
ATOM   9725  C C      . GLY B 2 164 ? 20.936  -31.732 -37.009 1.00 12.54  ?  164  GLY B C      1 
ATOM   9726  O O      . GLY B 2 164 ? 21.894  -32.074 -37.702 1.00 14.27  ?  164  GLY B O      1 
ATOM   9727  H H      . GLY B 2 164 ? 18.956  -29.951 -37.417 1.00 15.00  ?  164  GLY B H      1 
ATOM   9728  H HA2    . GLY B 2 164 ? 19.124  -32.657 -37.201 1.00 14.99  ?  164  GLY B HA2    1 
ATOM   9729  H HA3    . GLY B 2 164 ? 19.550  -31.873 -38.504 1.00 14.99  ?  164  GLY B HA3    1 
ATOM   9730  N N      . LEU B 2 165 ? 21.068  -31.248 -35.781 1.00 13.65  ?  165  LEU B N      1 
ATOM   9731  C CA     . LEU B 2 165 ? 22.329  -31.090 -35.081 1.00 13.25  ?  165  LEU B CA     1 
ATOM   9732  C C      . LEU B 2 165 ? 22.262  -31.856 -33.770 1.00 13.95  ?  165  LEU B C      1 
ATOM   9733  O O      . LEU B 2 165 ? 21.258  -31.772 -33.038 1.00 15.31  ?  165  LEU B O      1 
ATOM   9734  C CB     . LEU B 2 165 ? 22.563  -29.614 -34.789 1.00 14.66  ?  165  LEU B CB     1 
ATOM   9735  C CG     . LEU B 2 165 ? 22.813  -28.763 -36.029 1.00 14.92  ?  165  LEU B CG     1 
ATOM   9736  C CD1    . LEU B 2 165 ? 22.790  -27.284 -35.674 1.00 18.48  ?  165  LEU B CD1    1 
ATOM   9737  C CD2    . LEU B 2 165 ? 24.156  -29.103 -36.662 1.00 15.43  ?  165  LEU B CD2    1 
ATOM   9738  H H      . LEU B 2 165 ? 20.398  -30.990 -35.308 1.00 16.38  ?  165  LEU B H      1 
ATOM   9739  H HA     . LEU B 2 165 ? 23.064  -31.438 -35.609 1.00 15.89  ?  165  LEU B HA     1 
ATOM   9740  H HB2    . LEU B 2 165 ? 21.780  -29.259 -34.340 1.00 17.59  ?  165  LEU B HB2    1 
ATOM   9741  H HB3    . LEU B 2 165 ? 23.340  -29.533 -34.214 1.00 17.59  ?  165  LEU B HB3    1 
ATOM   9742  H HG     . LEU B 2 165 ? 22.109  -28.949 -36.671 1.00 17.90  ?  165  LEU B HG     1 
ATOM   9743  H HD11   . LEU B 2 165 ? 22.914  -26.763 -36.483 1.00 22.17  ?  165  LEU B HD11   1 
ATOM   9744  H HD12   . LEU B 2 165 ? 21.935  -27.070 -35.270 1.00 22.17  ?  165  LEU B HD12   1 
ATOM   9745  H HD13   . LEU B 2 165 ? 23.508  -27.099 -35.048 1.00 22.17  ?  165  LEU B HD13   1 
ATOM   9746  H HD21   . LEU B 2 165 ? 24.318  -28.498 -37.403 1.00 18.51  ?  165  LEU B HD21   1 
ATOM   9747  H HD22   . LEU B 2 165 ? 24.853  -29.003 -35.995 1.00 18.51  ?  165  LEU B HD22   1 
ATOM   9748  H HD23   . LEU B 2 165 ? 24.132  -30.019 -36.981 1.00 18.51  ?  165  LEU B HD23   1 
ATOM   9749  N N      . LYS B 2 166 ? 23.351  -32.582 -33.480 1.00 15.04  ?  166  LYS B N      1 
ATOM   9750  C CA     . LYS B 2 166 ? 23.388  -33.547 -32.382 1.00 15.96  ?  166  LYS B CA     1 
ATOM   9751  C C      . LYS B 2 166 ? 23.065  -32.917 -31.030 1.00 14.16  ?  166  LYS B C      1 
ATOM   9752  O O      . LYS B 2 166 ? 22.439  -33.563 -30.175 1.00 14.20  ?  166  LYS B O      1 
ATOM   9753  C CB     . LYS B 2 166 ? 24.782  -34.183 -32.322 1.00 20.30  ?  166  LYS B CB     1 
ATOM   9754  C CG     . LYS B 2 166 ? 25.146  -35.058 -33.502 1.00 29.88  ?  166  LYS B CG     1 
ATOM   9755  C CD     . LYS B 2 166 ? 26.550  -35.634 -33.338 1.00 37.86  ?  166  LYS B CD     1 
ATOM   9756  C CE     . LYS B 2 166 ? 26.966  -36.440 -34.558 1.00 46.47  ?  166  LYS B CE     1 
ATOM   9757  N NZ     . LYS B 2 166 ? 26.078  -37.624 -34.803 1.00 50.99  ?  166  LYS B NZ     1 
ATOM   9758  H H      . LYS B 2 166 ? 24.093  -32.534 -33.912 1.00 18.04  ?  166  LYS B H      1 
ATOM   9759  H HA     . LYS B 2 166 ? 22.717  -34.225 -32.556 1.00 19.15  ?  166  LYS B HA     1 
ATOM   9760  H HB2    . LYS B 2 166 ? 25.441  -33.473 -32.274 1.00 24.36  ?  166  LYS B HB2    1 
ATOM   9761  H HB3    . LYS B 2 166 ? 24.832  -34.736 -31.526 1.00 24.36  ?  166  LYS B HB3    1 
ATOM   9762  H HG2    . LYS B 2 166 ? 24.517  -35.793 -33.566 1.00 35.85  ?  166  LYS B HG2    1 
ATOM   9763  H HG3    . LYS B 2 166 ? 25.123  -34.530 -34.315 1.00 35.85  ?  166  LYS B HG3    1 
ATOM   9764  H HD2    . LYS B 2 166 ? 27.184  -34.909 -33.221 1.00 45.43  ?  166  LYS B HD2    1 
ATOM   9765  H HD3    . LYS B 2 166 ? 26.569  -36.220 -32.564 1.00 45.43  ?  166  LYS B HD3    1 
ATOM   9766  H HE2    . LYS B 2 166 ? 26.928  -35.870 -35.341 1.00 55.76  ?  166  LYS B HE2    1 
ATOM   9767  H HE3    . LYS B 2 166 ? 27.870  -36.766 -34.428 1.00 55.76  ?  166  LYS B HE3    1 
ATOM   9768  H HZ1    . LYS B 2 166 ? 26.349  -38.061 -35.530 1.00 61.19  ?  166  LYS B HZ1    1 
ATOM   9769  H HZ2    . LYS B 2 166 ? 26.108  -38.177 -34.106 1.00 61.19  ?  166  LYS B HZ2    1 
ATOM   9770  H HZ3    . LYS B 2 166 ? 25.239  -37.355 -34.924 1.00 61.19  ?  166  LYS B HZ3    1 
ATOM   9771  N N      . ALA B 2 167 ? 23.509  -31.677 -30.803 1.00 15.10  ?  167  ALA B N      1 
ATOM   9772  C CA     . ALA B 2 167 ? 23.362  -31.087 -29.474 1.00 15.75  ?  167  ALA B CA     1 
ATOM   9773  C C      . ALA B 2 167 ? 21.906  -30.989 -29.051 1.00 15.46  ?  167  ALA B C      1 
ATOM   9774  O O      . ALA B 2 167 ? 21.604  -31.010 -27.855 1.00 15.49  ?  167  ALA B O      1 
ATOM   9775  C CB     . ALA B 2 167 ? 24.005  -29.701 -29.433 1.00 16.68  ?  167  ALA B CB     1 
ATOM   9776  H H      . ALA B 2 167 ? 23.888  -31.170 -31.384 1.00 18.11  ?  167  ALA B H      1 
ATOM   9777  H HA     . ALA B 2 167 ? 23.824  -31.657 -28.839 1.00 18.90  ?  167  ALA B HA     1 
ATOM   9778  H HB1    . ALA B 2 167 ? 23.892  -29.326 -28.546 1.00 20.01  ?  167  ALA B HB1    1 
ATOM   9779  H HB2    . ALA B 2 167 ? 24.949  -29.785 -29.639 1.00 20.01  ?  167  ALA B HB2    1 
ATOM   9780  H HB3    . ALA B 2 167 ? 23.573  -29.133 -30.090 1.00 20.01  ?  167  ALA B HB3    1 
ATOM   9781  N N      . PHE B 2 168 ? 20.992  -30.895 -30.007 1.00 13.50  ?  168  PHE B N      1 
ATOM   9782  C CA     . PHE B 2 168 ? 19.575  -30.722 -29.718 1.00 13.73  ?  168  PHE B CA     1 
ATOM   9783  C C      . PHE B 2 168 ? 18.827  -32.029 -29.682 1.00 12.69  ?  168  PHE B C      1 
ATOM   9784  O O      . PHE B 2 168 ? 17.616  -32.023 -29.412 1.00 14.08  ?  168  PHE B O      1 
ATOM   9785  C CB     . PHE B 2 168 ? 18.990  -29.743 -30.728 1.00 14.01  ?  168  PHE B CB     1 
ATOM   9786  C CG     . PHE B 2 168 ? 19.596  -28.389 -30.595 1.00 14.58  ?  168  PHE B CG     1 
ATOM   9787  C CD1    . PHE B 2 168 ? 19.107  -27.488 -29.665 1.00 16.15  ?  168  PHE B CD1    1 
ATOM   9788  C CD2    . PHE B 2 168 ? 20.725  -28.039 -31.328 1.00 16.45  ?  168  PHE B CD2    1 
ATOM   9789  C CE1    . PHE B 2 168 ? 19.701  -26.247 -29.511 1.00 15.90  ?  168  PHE B CE1    1 
ATOM   9790  C CE2    . PHE B 2 168 ? 21.327  -26.797 -31.163 1.00 17.15  ?  168  PHE B CE2    1 
ATOM   9791  C CZ     . PHE B 2 168 ? 20.826  -25.909 -30.245 1.00 16.73  ?  168  PHE B CZ     1 
ATOM   9792  H H      . PHE B 2 168 ? 21.172  -30.929 -30.847 1.00 16.19  ?  168  PHE B H      1 
ATOM   9793  H HA     . PHE B 2 168 ? 19.447  -30.328 -28.840 1.00 16.47  ?  168  PHE B HA     1 
ATOM   9794  H HB2    . PHE B 2 168 ? 19.163  -30.068 -31.626 1.00 16.81  ?  168  PHE B HB2    1 
ATOM   9795  H HB3    . PHE B 2 168 ? 18.034  -29.665 -30.582 1.00 16.81  ?  168  PHE B HB3    1 
ATOM   9796  H HD1    . PHE B 2 168 ? 18.374  -27.718 -29.141 1.00 19.38  ?  168  PHE B HD1    1 
ATOM   9797  H HD2    . PHE B 2 168 ? 21.082  -28.644 -31.937 1.00 19.74  ?  168  PHE B HD2    1 
ATOM   9798  H HE1    . PHE B 2 168 ? 19.342  -25.635 -28.910 1.00 19.08  ?  168  PHE B HE1    1 
ATOM   9799  H HE2    . PHE B 2 168 ? 22.069  -26.569 -31.674 1.00 20.58  ?  168  PHE B HE2    1 
ATOM   9800  H HZ     . PHE B 2 168 ? 21.239  -25.086 -30.116 1.00 20.07  ?  168  PHE B HZ     1 
ATOM   9801  N N      . HIS B 2 169 ? 19.533  -33.150 -29.886 1.00 13.75  ?  169  HIS B N      1 
ATOM   9802  C CA     . HIS B 2 169 ? 18.946  -34.480 -29.813 1.00 14.26  ?  169  HIS B CA     1 
ATOM   9803  C C      . HIS B 2 169 ? 19.543  -35.338 -28.704 1.00 15.60  ?  169  HIS B C      1 
ATOM   9804  O O      . HIS B 2 169 ? 18.807  -36.015 -27.980 1.00 15.52  ?  169  HIS B O      1 
ATOM   9805  C CB     . HIS B 2 169 ? 19.178  -35.234 -31.125 1.00 13.88  ?  169  HIS B CB     1 
ATOM   9806  C CG     . HIS B 2 169 ? 18.462  -34.662 -32.300 1.00 14.31  ?  169  HIS B CG     1 
ATOM   9807  N ND1    . HIS B 2 169 ? 18.691  -35.097 -33.587 1.00 16.07  ?  169  HIS B ND1    1 
ATOM   9808  C CD2    . HIS B 2 169 ? 17.517  -33.696 -32.387 1.00 13.31  ?  169  HIS B CD2    1 
ATOM   9809  C CE1    . HIS B 2 169 ? 17.927  -34.409 -34.421 1.00 17.21  ?  169  HIS B CE1    1 
ATOM   9810  N NE2    . HIS B 2 169 ? 17.207  -33.551 -33.716 1.00 15.89  ?  169  HIS B NE2    1 
ATOM   9811  H H      . HIS B 2 169 ? 20.373  -33.157 -30.072 1.00 16.49  ?  169  HIS B H      1 
ATOM   9812  H HA     . HIS B 2 169 ? 17.996  -34.362 -29.656 1.00 17.11  ?  169  HIS B HA     1 
ATOM   9813  H HB2    . HIS B 2 169 ? 20.127  -35.222 -31.326 1.00 16.65  ?  169  HIS B HB2    1 
ATOM   9814  H HB3    . HIS B 2 169 ? 18.874  -36.149 -31.014 1.00 16.65  ?  169  HIS B HB3    1 
ATOM   9815  H HD1    . HIS B 2 169 ? 19.242  -35.718 -33.813 1.00 19.28  ?  169  HIS B HD1    1 
ATOM   9816  H HD2    . HIS B 2 169 ? 17.147  -33.219 -31.679 1.00 15.97  ?  169  HIS B HD2    1 
ATOM   9817  H HE1    . HIS B 2 169 ? 17.902  -34.511 -35.345 1.00 20.65  ?  169  HIS B HE1    1 
ATOM   9818  H HE2    . HIS B 2 169 ? 16.637  -32.994 -34.039 1.00 19.06  ?  169  HIS B HE2    1 
ATOM   9819  N N      . ASP B 2 170 ? 20.865  -35.392 -28.610 1.00 15.86  ?  170  ASP B N      1 
ATOM   9820  C CA     . ASP B 2 170 ? 21.516  -36.327 -27.702 1.00 15.45  ?  170  ASP B CA     1 
ATOM   9821  C C      . ASP B 2 170 ? 21.071  -36.047 -26.268 1.00 15.74  ?  170  ASP B C      1 
ATOM   9822  O O      . ASP B 2 170 ? 21.004  -34.898 -25.820 1.00 16.65  ?  170  ASP B O      1 
ATOM   9823  C CB     . ASP B 2 170 ? 23.037  -36.185 -27.816 1.00 17.65  ?  170  ASP B CB     1 
ATOM   9824  C CG     . ASP B 2 170 ? 23.591  -36.635 -29.165 1.00 19.49  ?  170  ASP B CG     1 
ATOM   9825  O OD1    . ASP B 2 170 ? 22.851  -37.242 -29.982 1.00 21.30  ?  170  ASP B OD1    1 
ATOM   9826  O OD2    . ASP B 2 170 ? 24.793  -36.369 -29.413 1.00 22.58  -1 170  ASP B OD2    1 
ATOM   9827  H H      . ASP B 2 170 ? 21.409  -34.901 -29.058 1.00 19.03  ?  170  ASP B H      1 
ATOM   9828  H HA     . ASP B 2 170 ? 21.276  -37.238 -27.932 1.00 18.54  ?  170  ASP B HA     1 
ATOM   9829  H HB2    . ASP B 2 170 ? 23.275  -35.252 -27.694 1.00 21.18  ?  170  ASP B HB2    1 
ATOM   9830  H HB3    . ASP B 2 170 ? 23.455  -36.727 -27.128 1.00 21.18  ?  170  ASP B HB3    1 
ATOM   9831  N N      . HIS B 2 171 ? 20.766  -37.109 -25.541 1.00 15.20  ?  171  HIS B N      1 
ATOM   9832  C CA     . HIS B 2 171 ? 20.339  -37.060 -24.146 1.00 14.50  ?  171  HIS B CA     1 
ATOM   9833  C C      . HIS B 2 171 ? 18.901  -36.592 -24.013 1.00 14.65  ?  171  HIS B C      1 
ATOM   9834  O O      . HIS B 2 171 ? 18.389  -36.590 -22.894 1.00 15.83  ?  171  HIS B O      1 
ATOM   9835  C CB     . HIS B 2 171 ? 21.250  -36.183 -23.278 1.00 16.03  ?  171  HIS B CB     1 
ATOM   9836  C CG     . HIS B 2 171 ? 22.697  -36.434 -23.534 1.00 19.75  ?  171  HIS B CG     1 
ATOM   9837  N ND1    . HIS B 2 171 ? 23.276  -37.666 -23.331 1.00 20.86  ?  171  HIS B ND1    1 
ATOM   9838  C CD2    . HIS B 2 171 ? 23.671  -35.634 -24.037 1.00 20.04  ?  171  HIS B CD2    1 
ATOM   9839  C CE1    . HIS B 2 171 ? 24.557  -37.606 -23.659 1.00 23.09  ?  171  HIS B CE1    1 
ATOM   9840  N NE2    . HIS B 2 171 ? 24.821  -36.385 -24.094 1.00 21.09  ?  171  HIS B NE2    1 
ATOM   9841  H H      . HIS B 2 171 ? 20.803  -37.907 -25.848 1.00 18.24  ?  171  HIS B H      1 
ATOM   9842  H HA     . HIS B 2 171 ? 20.378  -37.957 -23.780 1.00 17.40  ?  171  HIS B HA     1 
ATOM   9843  H HB2    . HIS B 2 171 ? 21.068  -35.250 -23.469 1.00 19.24  ?  171  HIS B HB2    1 
ATOM   9844  H HB3    . HIS B 2 171 ? 21.073  -36.371 -22.343 1.00 19.24  ?  171  HIS B HB3    1 
ATOM   9845  H HD2    . HIS B 2 171 ? 23.578  -34.745 -24.294 1.00 24.05  ?  171  HIS B HD2    1 
ATOM   9846  H HE1    . HIS B 2 171 ? 25.168  -38.304 -23.594 1.00 27.71  ?  171  HIS B HE1    1 
ATOM   9847  H HE2    . HIS B 2 171 ? 25.587  -36.106 -24.369 1.00 25.31  ?  171  HIS B HE2    1 
ATOM   9848  N N      . PHE B 2 172 ? 18.241  -36.203 -25.106 1.00 14.54  ?  172  PHE B N      1 
ATOM   9849  C CA     . PHE B 2 172 ? 16.840  -35.807 -25.069 1.00 14.32  ?  172  PHE B CA     1 
ATOM   9850  C C      . PHE B 2 172 ? 15.914  -36.795 -25.765 1.00 14.50  ?  172  PHE B C      1 
ATOM   9851  O O      . PHE B 2 172 ? 14.710  -36.545 -25.851 1.00 15.19  ?  172  PHE B O      1 
ATOM   9852  C CB     . PHE B 2 172 ? 16.656  -34.428 -25.691 1.00 12.78  ?  172  PHE B CB     1 
ATOM   9853  C CG     . PHE B 2 172 ? 17.500  -33.361 -25.067 1.00 13.59  ?  172  PHE B CG     1 
ATOM   9854  C CD1    . PHE B 2 172 ? 17.296  -32.992 -23.739 1.00 14.57  ?  172  PHE B CD1    1 
ATOM   9855  C CD2    . PHE B 2 172 ? 18.470  -32.694 -25.807 1.00 13.56  ?  172  PHE B CD2    1 
ATOM   9856  C CE1    . PHE B 2 172 ? 18.070  -31.975 -23.160 1.00 13.94  ?  172  PHE B CE1    1 
ATOM   9857  C CE2    . PHE B 2 172 ? 19.238  -31.707 -25.238 1.00 13.00  ?  172  PHE B CE2    1 
ATOM   9858  C CZ     . PHE B 2 172 ? 19.035  -31.351 -23.906 1.00 13.17  ?  172  PHE B CZ     1 
ATOM   9859  H H      . PHE B 2 172 ? 18.593  -36.162 -25.889 1.00 17.44  ?  172  PHE B H      1 
ATOM   9860  H HA     . PHE B 2 172 ? 16.573  -35.754 -24.138 1.00 17.18  ?  172  PHE B HA     1 
ATOM   9861  H HB2    . PHE B 2 172 ? 16.891  -34.477 -26.631 1.00 15.33  ?  172  PHE B HB2    1 
ATOM   9862  H HB3    . PHE B 2 172 ? 15.727  -34.164 -25.594 1.00 15.33  ?  172  PHE B HB3    1 
ATOM   9863  H HD1    . PHE B 2 172 ? 16.644  -33.422 -23.235 1.00 17.49  ?  172  PHE B HD1    1 
ATOM   9864  H HD2    . PHE B 2 172 ? 18.601  -32.918 -26.700 1.00 16.26  ?  172  PHE B HD2    1 
ATOM   9865  H HE1    . PHE B 2 172 ? 17.928  -31.726 -22.275 1.00 16.73  ?  172  PHE B HE1    1 
ATOM   9866  H HE2    . PHE B 2 172 ? 19.893  -31.278 -25.740 1.00 15.59  ?  172  PHE B HE2    1 
ATOM   9867  H HZ     . PHE B 2 172 ? 19.558  -30.686 -23.521 1.00 15.81  ?  172  PHE B HZ     1 
ATOM   9868  N N      . ASP B 2 173 ? 16.433  -37.895 -26.281 1.00 14.69  ?  173  ASP B N      1 
ATOM   9869  C CA     . ASP B 2 173 ? 15.619  -38.919 -26.939 1.00 15.36  ?  173  ASP B CA     1 
ATOM   9870  C C      . ASP B 2 173 ? 14.907  -38.382 -28.180 1.00 15.27  ?  173  ASP B C      1 
ATOM   9871  O O      . ASP B 2 173 ? 13.803  -38.807 -28.512 1.00 19.80  ?  173  ASP B O      1 
ATOM   9872  C CB     . ASP B 2 173 ? 14.593  -39.541 -25.989 1.00 15.74  ?  173  ASP B CB     1 
ATOM   9873  C CG     . ASP B 2 173 ? 15.206  -40.168 -24.757 1.00 17.64  ?  173  ASP B CG     1 
ATOM   9874  O OD1    . ASP B 2 173 ? 16.434  -40.395 -24.701 1.00 18.14  ?  173  ASP B OD1    1 
ATOM   9875  O OD2    . ASP B 2 173 ? 14.415  -40.441 -23.830 1.00 19.39  -1 173  ASP B OD2    1 
ATOM   9876  H H      . ASP B 2 173 ? 17.273  -38.081 -26.265 1.00 17.63  ?  173  ASP B H      1 
ATOM   9877  H HA     . ASP B 2 173 ? 16.227  -39.620 -27.223 1.00 18.42  ?  173  ASP B HA     1 
ATOM   9878  H HB2    . ASP B 2 173 ? 13.980  -38.850 -25.695 1.00 18.88  ?  173  ASP B HB2    1 
ATOM   9879  H HB3    . ASP B 2 173 ? 14.108  -40.235 -26.464 1.00 18.88  ?  173  ASP B HB3    1 
ATOM   9880  N N      . LEU B 2 174 ? 15.535  -37.468 -28.896 1.00 15.06  ?  174  LEU B N      1 
ATOM   9881  C CA     . LEU B 2 174 ? 14.964  -36.910 -30.106 1.00 14.32  ?  174  LEU B CA     1 
ATOM   9882  C C      . LEU B 2 174 ? 15.744  -37.428 -31.307 1.00 14.35  ?  174  LEU B C      1 
ATOM   9883  O O      . LEU B 2 174 ? 16.904  -37.833 -31.169 1.00 16.39  ?  174  LEU B O      1 
ATOM   9884  C CB     . LEU B 2 174 ? 15.029  -35.376 -30.057 1.00 14.42  ?  174  LEU B CB     1 
ATOM   9885  C CG     . LEU B 2 174 ? 14.334  -34.741 -28.847 1.00 13.97  ?  174  LEU B CG     1 
ATOM   9886  C CD1    . LEU B 2 174 ? 14.541  -33.238 -28.818 1.00 14.44  ?  174  LEU B CD1    1 
ATOM   9887  C CD2    . LEU B 2 174 ? 12.847  -35.040 -28.823 1.00 14.77  ?  174  LEU B CD2    1 
ATOM   9888  H H      . LEU B 2 174 ? 16.309  -37.151 -28.694 1.00 18.07  ?  174  LEU B H      1 
ATOM   9889  H HA     . LEU B 2 174 ? 14.032  -37.162 -30.203 1.00 17.19  ?  174  LEU B HA     1 
ATOM   9890  H HB2    . LEU B 2 174 ? 15.961  -35.109 -30.032 1.00 17.30  ?  174  LEU B HB2    1 
ATOM   9891  H HB3    . LEU B 2 174 ? 14.605  -35.025 -30.856 1.00 17.30  ?  174  LEU B HB3    1 
ATOM   9892  H HG     . LEU B 2 174 ? 14.734  -35.131 -28.054 1.00 16.77  ?  174  LEU B HG     1 
ATOM   9893  H HD11   . LEU B 2 174 ? 14.146  -32.880 -28.008 1.00 17.32  ?  174  LEU B HD11   1 
ATOM   9894  H HD12   . LEU B 2 174 ? 15.493  -33.050 -28.833 1.00 17.32  ?  174  LEU B HD12   1 
ATOM   9895  H HD13   . LEU B 2 174 ? 14.114  -32.845 -29.596 1.00 17.32  ?  174  LEU B HD13   1 
ATOM   9896  H HD21   . LEU B 2 174 ? 12.459  -34.650 -28.024 1.00 17.72  ?  174  LEU B HD21   1 
ATOM   9897  H HD22   . LEU B 2 174 ? 12.435  -34.655 -29.613 1.00 17.72  ?  174  LEU B HD22   1 
ATOM   9898  H HD23   . LEU B 2 174 ? 12.718  -36.001 -28.818 1.00 17.72  ?  174  LEU B HD23   1 
ATOM   9899  N N      . PRO B 2 175 ? 15.139  -37.440 -32.510 1.00 15.05  ?  175  PRO B N      1 
ATOM   9900  C CA     . PRO B 2 175 ? 13.815  -36.889 -32.811 1.00 15.29  ?  175  PRO B CA     1 
ATOM   9901  C C      . PRO B 2 175 ? 12.634  -37.773 -32.420 1.00 15.75  ?  175  PRO B C      1 
ATOM   9902  O O      . PRO B 2 175 ? 12.769  -39.004 -32.306 1.00 15.89  ?  175  PRO B O      1 
ATOM   9903  C CB     . PRO B 2 175 ? 13.831  -36.763 -34.334 1.00 16.64  ?  175  PRO B CB     1 
ATOM   9904  C CG     . PRO B 2 175 ? 14.748  -37.871 -34.781 1.00 16.18  ?  175  PRO B CG     1 
ATOM   9905  C CD     . PRO B 2 175 ? 15.828  -37.915 -33.727 1.00 15.65  ?  175  PRO B CD     1 
ATOM   9906  H HA     . PRO B 2 175 ? 13.733  -36.030 -32.367 1.00 18.34  ?  175  PRO B HA     1 
ATOM   9907  H HB2    . PRO B 2 175 ? 12.936  -36.883 -34.689 1.00 19.96  ?  175  PRO B HB2    1 
ATOM   9908  H HB3    . PRO B 2 175 ? 14.177  -35.895 -34.594 1.00 19.96  ?  175  PRO B HB3    1 
ATOM   9909  H HG2    . PRO B 2 175 ? 14.263  -38.710 -34.818 1.00 19.41  ?  175  PRO B HG2    1 
ATOM   9910  H HG3    . PRO B 2 175 ? 15.120  -37.664 -35.653 1.00 19.41  ?  175  PRO B HG3    1 
ATOM   9911  H HD2    . PRO B 2 175 ? 16.155  -38.820 -33.607 1.00 18.77  ?  175  PRO B HD2    1 
ATOM   9912  H HD3    . PRO B 2 175 ? 16.562  -37.325 -33.961 1.00 18.77  ?  175  PRO B HD3    1 
ATOM   9913  N N      . ILE B 2 176 ? 11.475  -37.148 -32.250 1.00 14.59  ?  176  ILE B N      1 
ATOM   9914  C CA     . ILE B 2 176 ? 10.226  -37.870 -32.069 1.00 14.24  ?  176  ILE B CA     1 
ATOM   9915  C C      . ILE B 2 176 ? 9.869   -38.604 -33.360 1.00 14.14  ?  176  ILE B C      1 
ATOM   9916  O O      . ILE B 2 176 ? 10.449  -38.359 -34.422 1.00 15.17  ?  176  ILE B O      1 
ATOM   9917  C CB     . ILE B 2 176 ? 9.082   -36.936 -31.634 1.00 13.36  ?  176  ILE B CB     1 
ATOM   9918  C CG1    . ILE B 2 176 ? 8.775   -35.886 -32.710 1.00 16.19  ?  176  ILE B CG1    1 
ATOM   9919  C CG2    . ILE B 2 176 ? 9.394   -36.269 -30.274 1.00 15.18  ?  176  ILE B CG2    1 
ATOM   9920  C CD1    . ILE B 2 176 ? 7.548   -35.055 -32.412 1.00 17.36  ?  176  ILE B CD1    1 
ATOM   9921  H H      . ILE B 2 176 ? 11.386  -36.292 -32.236 1.00 17.50  ?  176  ILE B H      1 
ATOM   9922  H HA     . ILE B 2 176 ? 10.356  -38.530 -31.370 1.00 17.08  ?  176  ILE B HA     1 
ATOM   9923  H HB     . ILE B 2 176 ? 8.288   -37.482 -31.525 1.00 16.03  ?  176  ILE B HB     1 
ATOM   9924  H HG12   . ILE B 2 176 ? 9.531   -35.284 -32.784 1.00 19.42  ?  176  ILE B HG12   1 
ATOM   9925  H HG13   . ILE B 2 176 ? 8.628   -36.339 -33.556 1.00 19.42  ?  176  ILE B HG13   1 
ATOM   9926  H HG21   . ILE B 2 176 ? 8.604   -35.801 -29.964 1.00 18.21  ?  176  ILE B HG21   1 
ATOM   9927  H HG22   . ILE B 2 176 ? 9.644   -36.956 -29.636 1.00 18.21  ?  176  ILE B HG22   1 
ATOM   9928  H HG23   . ILE B 2 176 ? 10.126  -35.644 -30.390 1.00 18.21  ?  176  ILE B HG23   1 
ATOM   9929  H HD11   . ILE B 2 176 ? 7.383   -34.457 -33.158 1.00 20.83  ?  176  ILE B HD11   1 
ATOM   9930  H HD12   . ILE B 2 176 ? 6.789   -35.645 -32.287 1.00 20.83  ?  176  ILE B HD12   1 
ATOM   9931  H HD13   . ILE B 2 176 ? 7.703   -34.541 -31.605 1.00 20.83  ?  176  ILE B HD13   1 
ATOM   9932  N N      . GLU B 2 177 ? 8.874   -39.484 -33.274 1.00 15.94  ?  177  GLU B N      1 
ATOM   9933  C CA     . GLU B 2 177 ? 8.452   -40.273 -34.416 1.00 16.87  ?  177  GLU B CA     1 
ATOM   9934  C C      . GLU B 2 177 ? 7.893   -39.385 -35.515 1.00 16.52  ?  177  GLU B C      1 
ATOM   9935  O O      . GLU B 2 177 ? 7.278   -38.342 -35.251 1.00 16.77  ?  177  GLU B O      1 
ATOM   9936  C CB     . GLU B 2 177 ? 7.368   -41.258 -33.993 1.00 21.40  ?  177  GLU B CB     1 
ATOM   9937  C CG     . GLU B 2 177 ? 7.885   -42.411 -33.167 1.00 31.73  ?  177  GLU B CG     1 
ATOM   9938  C CD     . GLU B 2 177 ? 8.717   -43.378 -34.003 1.00 42.89  ?  177  GLU B CD     1 
ATOM   9939  O OE1    . GLU B 2 177 ? 8.477   -43.486 -35.226 1.00 46.42  ?  177  GLU B OE1    1 
ATOM   9940  O OE2    . GLU B 2 177 ? 9.617   -44.018 -33.422 1.00 48.30  -1 177  GLU B OE2    1 
ATOM   9941  H H      . GLU B 2 177 ? 8.424   -39.642 -32.558 1.00 19.12  ?  177  GLU B H      1 
ATOM   9942  H HA     . GLU B 2 177 ? 9.218   -40.757 -34.762 1.00 20.25  ?  177  GLU B HA     1 
ATOM   9943  H HB2    . GLU B 2 177 ? 6.707   -40.787 -33.463 1.00 25.67  ?  177  GLU B HB2    1 
ATOM   9944  H HB3    . GLU B 2 177 ? 6.953   -41.626 -34.789 1.00 25.67  ?  177  GLU B HB3    1 
ATOM   9945  H HG2    . GLU B 2 177 ? 8.444   -42.068 -32.453 1.00 38.08  ?  177  GLU B HG2    1 
ATOM   9946  H HG3    . GLU B 2 177 ? 7.134   -42.900 -32.795 1.00 38.08  ?  177  GLU B HG3    1 
ATOM   9947  N N      . GLY B 2 178 ? 8.111   -39.818 -36.756 1.00 14.37  ?  178  GLY B N      1 
ATOM   9948  C CA     . GLY B 2 178 ? 7.538   -39.167 -37.912 1.00 16.17  ?  178  GLY B CA     1 
ATOM   9949  C C      . GLY B 2 178 ? 8.386   -38.080 -38.521 1.00 13.53  ?  178  GLY B C      1 
ATOM   9950  O O      . GLY B 2 178 ? 7.949   -37.447 -39.489 1.00 16.20  ?  178  GLY B O      1 
ATOM   9951  H H      . GLY B 2 178 ? 8.598   -40.500 -36.949 1.00 17.24  ?  178  GLY B H      1 
ATOM   9952  H HA2    . GLY B 2 178 ? 7.380   -39.836 -38.597 1.00 19.40  ?  178  GLY B HA2    1 
ATOM   9953  H HA3    . GLY B 2 178 ? 6.690   -38.771 -37.656 1.00 19.40  ?  178  GLY B HA3    1 
ATOM   9954  N N      . ILE B 2 179 ? 9.579   -37.824 -37.987 1.00 12.31  ?  179  ILE B N      1 
ATOM   9955  C CA     . ILE B 2 179 ? 10.465  -36.786 -38.510 1.00 13.24  ?  179  ILE B CA     1 
ATOM   9956  C C      . ILE B 2 179 ? 11.752  -37.441 -39.002 1.00 13.85  ?  179  ILE B C      1 
ATOM   9957  O O      . ILE B 2 179 ? 12.395  -38.207 -38.265 1.00 16.66  ?  179  ILE B O      1 
ATOM   9958  C CB     . ILE B 2 179 ? 10.718  -35.703 -37.441 1.00 14.48  ?  179  ILE B CB     1 
ATOM   9959  C CG1    . ILE B 2 179 ? 9.409   -34.896 -37.223 1.00 15.31  ?  179  ILE B CG1    1 
ATOM   9960  C CG2    . ILE B 2 179 ? 11.904  -34.825 -37.817 1.00 14.10  ?  179  ILE B CG2    1 
ATOM   9961  C CD1    . ILE B 2 179 ? 9.419   -33.935 -36.055 1.00 17.45  ?  179  ILE B CD1    1 
ATOM   9962  H H      . ILE B 2 179 ? 9.899   -38.246 -37.310 1.00 14.77  ?  179  ILE B H      1 
ATOM   9963  H HA     . ILE B 2 179 ? 10.067  -36.357 -39.283 1.00 15.89  ?  179  ILE B HA     1 
ATOM   9964  H HB     . ILE B 2 179 ? 10.957  -36.122 -36.600 1.00 17.38  ?  179  ILE B HB     1 
ATOM   9965  H HG12   . ILE B 2 179 ? 9.236   -34.375 -38.023 1.00 18.36  ?  179  ILE B HG12   1 
ATOM   9966  H HG13   . ILE B 2 179 ? 8.685   -35.524 -37.073 1.00 18.36  ?  179  ILE B HG13   1 
ATOM   9967  H HG21   . ILE B 2 179 ? 11.937  -34.064 -37.216 1.00 16.92  ?  179  ILE B HG21   1 
ATOM   9968  H HG22   . ILE B 2 179 ? 12.719  -35.344 -37.739 1.00 16.92  ?  179  ILE B HG22   1 
ATOM   9969  H HG23   . ILE B 2 179 ? 11.793  -34.518 -38.731 1.00 16.92  ?  179  ILE B HG23   1 
ATOM   9970  H HD11   . ILE B 2 179 ? 8.516   -33.615 -35.902 1.00 20.93  ?  179  ILE B HD11   1 
ATOM   9971  H HD12   . ILE B 2 179 ? 9.743   -34.399 -35.267 1.00 20.93  ?  179  ILE B HD12   1 
ATOM   9972  H HD13   . ILE B 2 179 ? 10.003  -33.190 -36.264 1.00 20.93  ?  179  ILE B HD13   1 
ATOM   9973  N N      . LEU B 2 180 ? 12.114  -37.144 -40.245 1.00 14.04  ?  180  LEU B N      1 
ATOM   9974  C CA     . LEU B 2 180 ? 13.237  -37.774 -40.921 1.00 14.48  ?  180  LEU B CA     1 
ATOM   9975  C C      . LEU B 2 180 ? 14.248  -36.705 -41.308 1.00 12.75  ?  180  LEU B C      1 
ATOM   9976  O O      . LEU B 2 180 ? 13.914  -35.520 -41.379 1.00 13.68  ?  180  LEU B O      1 
ATOM   9977  C CB     . LEU B 2 180 ? 12.781  -38.473 -42.217 1.00 16.83  ?  180  LEU B CB     1 
ATOM   9978  C CG     . LEU B 2 180 ? 11.594  -39.406 -42.043 1.00 20.47  ?  180  LEU B CG     1 
ATOM   9979  C CD1    . LEU B 2 180 ? 11.088  -39.954 -43.343 1.00 23.07  ?  180  LEU B CD1    1 
ATOM   9980  C CD2    . LEU B 2 180 ? 11.962  -40.534 -41.088 1.00 22.45  ?  180  LEU B CD2    1 
ATOM   9981  H H      . LEU B 2 180 ? 11.709  -36.561 -40.730 1.00 16.85  ?  180  LEU B H      1 
ATOM   9982  H HA     . LEU B 2 180 ? 13.644  -38.423 -40.326 1.00 17.37  ?  180  LEU B HA     1 
ATOM   9983  H HB2    . LEU B 2 180 ? 12.529  -37.793 -42.861 1.00 20.19  ?  180  LEU B HB2    1 
ATOM   9984  H HB3    . LEU B 2 180 ? 13.520  -38.998 -42.560 1.00 20.19  ?  180  LEU B HB3    1 
ATOM   9985  H HG     . LEU B 2 180 ? 10.862  -38.892 -41.668 1.00 24.56  ?  180  LEU B HG     1 
ATOM   9986  H HD11   . LEU B 2 180 ? 10.369  -40.580 -43.163 1.00 27.68  ?  180  LEU B HD11   1 
ATOM   9987  H HD12   . LEU B 2 180 ? 10.760  -39.222 -43.888 1.00 27.68  ?  180  LEU B HD12   1 
ATOM   9988  H HD13   . LEU B 2 180 ? 11.815  -40.406 -43.799 1.00 27.68  ?  180  LEU B HD13   1 
ATOM   9989  H HD21   . LEU B 2 180 ? 11.235  -41.176 -41.063 1.00 26.93  ?  180  LEU B HD21   1 
ATOM   9990  H HD22   . LEU B 2 180 ? 12.772  -40.964 -41.404 1.00 26.93  ?  180  LEU B HD22   1 
ATOM   9991  H HD23   . LEU B 2 180 ? 12.108  -40.164 -40.203 1.00 26.93  ?  180  LEU B HD23   1 
ATOM   9992  N N      . HIS B 2 181 ? 15.481  -37.128 -41.579 1.00 13.75  ?  181  HIS B N      1 
ATOM   9993  C CA     . HIS B 2 181 ? 16.542  -36.213 -41.991 1.00 12.58  ?  181  HIS B CA     1 
ATOM   9994  C C      . HIS B 2 181 ? 17.243  -36.723 -43.241 1.00 14.01  ?  181  HIS B C      1 
ATOM   9995  O O      . HIS B 2 181 ? 17.870  -37.789 -43.214 1.00 15.12  ?  181  HIS B O      1 
ATOM   9996  C CB     . HIS B 2 181 ? 17.539  -36.008 -40.846 1.00 13.27  ?  181  HIS B CB     1 
ATOM   9997  C CG     . HIS B 2 181 ? 16.943  -35.334 -39.653 1.00 12.84  ?  181  HIS B CG     1 
ATOM   9998  N ND1    . HIS B 2 181 ? 16.303  -36.034 -38.657 1.00 14.01  ?  181  HIS B ND1    1 
ATOM   9999  C CD2    . HIS B 2 181 ? 16.844  -34.024 -39.318 1.00 12.82  ?  181  HIS B CD2    1 
ATOM   10000 C CE1    . HIS B 2 181 ? 15.839  -35.185 -37.760 1.00 14.59  ?  181  HIS B CE1    1 
ATOM   10001 N NE2    . HIS B 2 181 ? 16.159  -33.960 -38.133 1.00 13.95  ?  181  HIS B NE2    1 
ATOM   10002 H H      . HIS B 2 181 ? 15.728  -37.951 -41.530 1.00 16.49  ?  181  HIS B H      1 
ATOM   10003 H HA     . HIS B 2 181 ? 16.146  -35.361 -42.231 1.00 15.10  ?  181  HIS B HA     1 
ATOM   10004 H HB2    . HIS B 2 181 ? 17.873  -36.873 -40.563 1.00 15.92  ?  181  HIS B HB2    1 
ATOM   10005 H HB3    . HIS B 2 181 ? 18.271  -35.457 -41.164 1.00 15.92  ?  181  HIS B HB3    1 
ATOM   10006 H HD2    . HIS B 2 181 ? 17.178  -33.303 -39.803 1.00 15.38  ?  181  HIS B HD2    1 
ATOM   10007 H HE1    . HIS B 2 181 ? 15.364  -35.412 -36.993 1.00 17.51  ?  181  HIS B HE1    1 
ATOM   10008 H HE2    . HIS B 2 181 ? 15.970  -33.240 -37.702 1.00 16.73  ?  181  HIS B HE2    1 
ATOM   10009 N N      . THR B 2 182 ? 17.150  -35.951 -44.319 1.00 15.13  ?  182  THR B N      1 
ATOM   10010 C CA     . THR B 2 182 ? 17.844  -36.245 -45.564 1.00 13.94  ?  182  THR B CA     1 
ATOM   10011 C C      . THR B 2 182 ? 19.197  -35.518 -45.575 1.00 13.78  ?  182  THR B C      1 
ATOM   10012 O O      . THR B 2 182 ? 19.661  -35.030 -44.541 1.00 14.46  ?  182  THR B O      1 
ATOM   10013 C CB     . THR B 2 182 ? 16.929  -35.937 -46.766 1.00 14.91  ?  182  THR B CB     1 
ATOM   10014 O OG1    . THR B 2 182 ? 17.516  -36.473 -47.967 1.00 15.62  ?  182  THR B OG1    1 
ATOM   10015 C CG2    . THR B 2 182 ? 16.715  -34.443 -46.959 1.00 15.37  ?  182  THR B CG2    1 
ATOM   10016 H H      . THR B 2 182 ? 16.679  -35.232 -44.352 1.00 18.15  ?  182  THR B H      1 
ATOM   10017 H HA     . THR B 2 182 ? 18.035  -37.196 -45.594 1.00 16.73  ?  182  THR B HA     1 
ATOM   10018 H HB     . THR B 2 182 ? 16.064  -36.341 -46.597 1.00 17.89  ?  182  THR B HB     1 
ATOM   10019 H HG1    . THR B 2 182 ? 17.553  -37.311 -47.919 1.00 18.74  ?  182  THR B HG1    1 
ATOM   10020 H HG21   . THR B 2 182 ? 16.095  -34.289 -47.688 1.00 18.44  ?  182  THR B HG21   1 
ATOM   10021 H HG22   . THR B 2 182 ? 16.352  -34.053 -46.148 1.00 18.44  ?  182  THR B HG22   1 
ATOM   10022 H HG23   . THR B 2 182 ? 17.559  -34.011 -47.166 1.00 18.44  ?  182  THR B HG23   1 
ATOM   10023 N N      . GLU B 2 183 ? 19.835  -35.420 -46.744 1.00 14.68  ?  183  GLU B N      1 
ATOM   10024 C CA     . GLU B 2 183 ? 21.235  -35.028 -46.822 1.00 15.30  ?  183  GLU B CA     1 
ATOM   10025 C C      . GLU B 2 183 ? 21.434  -33.581 -46.412 1.00 14.87  ?  183  GLU B C      1 
ATOM   10026 O O      . GLU B 2 183 ? 20.622  -32.710 -46.725 1.00 15.23  ?  183  GLU B O      1 
ATOM   10027 C CB     . GLU B 2 183 ? 21.724  -35.189 -48.265 1.00 18.82  ?  183  GLU B CB     1 
ATOM   10028 C CG     . GLU B 2 183 ? 21.456  -36.545 -48.856 1.00 25.10  ?  183  GLU B CG     1 
ATOM   10029 C CD     . GLU B 2 183 ? 22.147  -37.636 -48.092 1.00 30.54  ?  183  GLU B CD     1 
ATOM   10030 O OE1    . GLU B 2 183 ? 23.376  -37.544 -47.973 1.00 29.73  ?  183  GLU B OE1    1 
ATOM   10031 O OE2    . GLU B 2 183 ? 21.457  -38.567 -47.592 1.00 33.30  -1 183  GLU B OE2    1 
ATOM   10032 H H      . GLU B 2 183 ? 19.475  -35.577 -47.509 1.00 17.62  ?  183  GLU B H      1 
ATOM   10033 H HA     . GLU B 2 183 ? 21.751  -35.590 -46.223 1.00 18.36  ?  183  GLU B HA     1 
ATOM   10034 H HB2    . GLU B 2 183 ? 21.275  -34.532 -48.820 1.00 22.59  ?  183  GLU B HB2    1 
ATOM   10035 H HB3    . GLU B 2 183 ? 22.682  -35.042 -48.287 1.00 22.59  ?  183  GLU B HB3    1 
ATOM   10036 H HG2    . GLU B 2 183 ? 20.502  -36.719 -48.836 1.00 30.12  ?  183  GLU B HG2    1 
ATOM   10037 H HG3    . GLU B 2 183 ? 21.777  -36.564 -49.770 1.00 30.12  ?  183  GLU B HG3    1 
ATOM   10038 N N      . ALA B 2 184 ? 22.548  -33.310 -45.733 1.00 15.62  ?  184  ALA B N      1 
ATOM   10039 C CA     . ALA B 2 184 ? 22.923  -31.936 -45.450 1.00 15.65  ?  184  ALA B CA     1 
ATOM   10040 C C      . ALA B 2 184 ? 23.227  -31.224 -46.762 1.00 15.33  ?  184  ALA B C      1 
ATOM   10041 O O      . ALA B 2 184 ? 23.924  -31.786 -47.618 1.00 16.31  ?  184  ALA B O      1 
ATOM   10042 C CB     . ALA B 2 184 ? 24.161  -31.929 -44.569 1.00 16.48  ?  184  ALA B CB     1 
ATOM   10043 H H      . ALA B 2 184 ? 23.097  -33.900 -45.430 1.00 18.74  ?  184  ALA B H      1 
ATOM   10044 H HA     . ALA B 2 184 ? 22.203  -31.472 -44.995 1.00 18.78  ?  184  ALA B HA     1 
ATOM   10045 H HB1    . ALA B 2 184 ? 24.404  -31.011 -44.374 1.00 19.77  ?  184  ALA B HB1    1 
ATOM   10046 H HB2    . ALA B 2 184 ? 23.965  -32.402 -43.745 1.00 19.77  ?  184  ALA B HB2    1 
ATOM   10047 H HB3    . ALA B 2 184 ? 24.885  -32.371 -45.039 1.00 19.77  ?  184  ALA B HB3    1 
ATOM   10048 N N      . PRO B 2 185 ? 22.698  -30.025 -46.978 1.00 16.17  ?  185  PRO B N      1 
ATOM   10049 C CA     . PRO B 2 185 ? 22.932  -29.296 -48.240 1.00 16.36  ?  185  PRO B CA     1 
ATOM   10050 C C      . PRO B 2 185 ? 24.266  -28.562 -48.192 1.00 15.38  ?  185  PRO B C      1 
ATOM   10051 O O      . PRO B 2 185 ? 24.336  -27.335 -48.188 1.00 16.04  ?  185  PRO B O      1 
ATOM   10052 C CB     . PRO B 2 185 ? 21.733  -28.346 -48.285 1.00 16.69  ?  185  PRO B CB     1 
ATOM   10053 C CG     . PRO B 2 185 ? 21.529  -28.000 -46.811 1.00 15.96  ?  185  PRO B CG     1 
ATOM   10054 C CD     . PRO B 2 185 ? 21.742  -29.307 -46.105 1.00 15.70  ?  185  PRO B CD     1 
ATOM   10055 H HA     . PRO B 2 185 ? 22.898  -29.888 -49.008 1.00 19.63  ?  185  PRO B HA     1 
ATOM   10056 H HB2    . PRO B 2 185 ? 21.943  -27.557 -48.810 1.00 20.02  ?  185  PRO B HB2    1 
ATOM   10057 H HB3    . PRO B 2 185 ? 20.957  -28.794 -48.657 1.00 20.02  ?  185  PRO B HB3    1 
ATOM   10058 H HG2    . PRO B 2 185 ? 22.179  -27.338 -46.529 1.00 19.14  ?  185  PRO B HG2    1 
ATOM   10059 H HG3    . PRO B 2 185 ? 20.630  -27.665 -46.666 1.00 19.14  ?  185  PRO B HG3    1 
ATOM   10060 H HD2    . PRO B 2 185 ? 22.122  -29.164 -45.224 1.00 18.83  ?  185  PRO B HD2    1 
ATOM   10061 H HD3    . PRO B 2 185 ? 20.909  -29.798 -46.031 1.00 18.83  ?  185  PRO B HD3    1 
ATOM   10062 N N      . TYR B 2 186 ? 25.356  -29.330 -48.122 1.00 17.01  ?  186  TYR B N      1 
ATOM   10063 C CA     . TYR B 2 186 ? 26.641  -28.855 -47.569 1.00 17.03  ?  186  TYR B CA     1 
ATOM   10064 C C      . TYR B 2 186 ? 27.748  -29.482 -48.413 1.00 17.64  ?  186  TYR B C      1 
ATOM   10065 O O      . TYR B 2 186 ? 28.327  -30.517 -48.078 1.00 18.32  ?  186  TYR B O      1 
ATOM   10066 C CB     . TYR B 2 186 ? 26.714  -29.235 -46.087 1.00 17.38  ?  186  TYR B CB     1 
ATOM   10067 C CG     . TYR B 2 186 ? 27.714  -28.536 -45.197 1.00 18.53  ?  186  TYR B CG     1 
ATOM   10068 C CD1    . TYR B 2 186 ? 28.948  -28.090 -45.655 1.00 19.49  ?  186  TYR B CD1    1 
ATOM   10069 C CD2    . TYR B 2 186 ? 27.408  -28.343 -43.855 1.00 17.84  ?  186  TYR B CD2    1 
ATOM   10070 C CE1    . TYR B 2 186 ? 29.847  -27.478 -44.777 1.00 19.90  ?  186  TYR B CE1    1 
ATOM   10071 C CE2    . TYR B 2 186 ? 28.286  -27.765 -42.995 1.00 19.34  ?  186  TYR B CE2    1 
ATOM   10072 C CZ     . TYR B 2 186 ? 29.503  -27.321 -43.454 1.00 18.02  ?  186  TYR B CZ     1 
ATOM   10073 O OH     . TYR B 2 186 ? 30.370  -26.748 -42.540 1.00 19.48  ?  186  TYR B OH     1 
ATOM   10074 H H      . TYR B 2 186 ? 25.380  -30.146 -48.393 1.00 20.41  ?  186  TYR B H      1 
ATOM   10075 H HA     . TYR B 2 186 ? 26.738  -27.894 -47.650 1.00 20.43  ?  186  TYR B HA     1 
ATOM   10076 H HB2    . TYR B 2 186 ? 25.841  -29.066 -45.700 1.00 20.86  ?  186  TYR B HB2    1 
ATOM   10077 H HB3    . TYR B 2 186 ? 26.921  -30.181 -46.039 1.00 20.86  ?  186  TYR B HB3    1 
ATOM   10078 H HD1    . TYR B 2 186 ? 29.177  -28.200 -46.550 1.00 23.39  ?  186  TYR B HD1    1 
ATOM   10079 H HD2    . TYR B 2 186 ? 26.579  -28.618 -43.536 1.00 21.40  ?  186  TYR B HD2    1 
ATOM   10080 H HE1    . TYR B 2 186 ? 30.671  -27.179 -45.085 1.00 23.87  ?  186  TYR B HE1    1 
ATOM   10081 H HE2    . TYR B 2 186 ? 28.064  -27.670 -42.097 1.00 23.21  ?  186  TYR B HE2    1 
ATOM   10082 H HH     . TYR B 2 186 ? 31.135  -26.673 -42.878 1.00 23.37  ?  186  TYR B HH     1 
ATOM   10083 N N      . TYR B 2 187 ? 28.031  -28.818 -49.531 1.00 16.38  ?  187  TYR B N      1 
ATOM   10084 C CA     . TYR B 2 187 ? 28.956  -29.336 -50.532 1.00 17.23  ?  187  TYR B CA     1 
ATOM   10085 C C      . TYR B 2 187 ? 30.323  -29.647 -49.938 1.00 18.49  ?  187  TYR B C      1 
ATOM   10086 O O      . TYR B 2 187 ? 30.928  -30.682 -50.254 1.00 18.51  ?  187  TYR B O      1 
ATOM   10087 C CB     . TYR B 2 187 ? 29.065  -28.292 -51.648 1.00 18.50  ?  187  TYR B CB     1 
ATOM   10088 C CG     . TYR B 2 187 ? 29.969  -28.638 -52.797 1.00 18.85  ?  187  TYR B CG     1 
ATOM   10089 C CD1    . TYR B 2 187 ? 29.737  -29.759 -53.577 1.00 19.08  ?  187  TYR B CD1    1 
ATOM   10090 C CD2    . TYR B 2 187 ? 31.061  -27.838 -53.104 1.00 19.69  ?  187  TYR B CD2    1 
ATOM   10091 C CE1    . TYR B 2 187 ? 30.586  -30.076 -54.638 1.00 22.21  ?  187  TYR B CE1    1 
ATOM   10092 C CE2    . TYR B 2 187 ? 31.891  -28.137 -54.156 1.00 22.04  ?  187  TYR B CE2    1 
ATOM   10093 C CZ     . TYR B 2 187 ? 31.654  -29.257 -54.920 1.00 22.52  ?  187  TYR B CZ     1 
ATOM   10094 O OH     . TYR B 2 187 ? 32.509  -29.520 -55.957 1.00 24.16  ?  187  TYR B OH     1 
ATOM   10095 H H      . TYR B 2 187 ? 27.697  -28.054 -49.740 1.00 19.65  ?  187  TYR B H      1 
ATOM   10096 H HA     . TYR B 2 187 ? 28.621  -30.170 -50.896 1.00 20.68  ?  187  TYR B HA     1 
ATOM   10097 H HB2    . TYR B 2 187 ? 28.179  -28.150 -52.016 1.00 22.19  ?  187  TYR B HB2    1 
ATOM   10098 H HB3    . TYR B 2 187 ? 29.399  -27.468 -51.260 1.00 22.19  ?  187  TYR B HB3    1 
ATOM   10099 H HD1    . TYR B 2 187 ? 29.008  -30.306 -53.392 1.00 22.90  ?  187  TYR B HD1    1 
ATOM   10100 H HD2    . TYR B 2 187 ? 31.233  -27.084 -52.587 1.00 23.63  ?  187  TYR B HD2    1 
ATOM   10101 H HE1    . TYR B 2 187 ? 30.431  -30.836 -55.150 1.00 26.65  ?  187  TYR B HE1    1 
ATOM   10102 H HE2    . TYR B 2 187 ? 32.613  -27.584 -54.352 1.00 26.45  ?  187  TYR B HE2    1 
ATOM   10103 H HH     . TYR B 2 187 ? 32.207  -30.148 -56.426 1.00 28.99  ?  187  TYR B HH     1 
ATOM   10104 N N      . TYR B 2 188 ? 30.840  -28.764 -49.087 1.00 18.83  ?  188  TYR B N      1 
ATOM   10105 C CA     . TYR B 2 188 ? 32.197  -28.955 -48.574 1.00 18.53  ?  188  TYR B CA     1 
ATOM   10106 C C      . TYR B 2 188 ? 32.317  -30.174 -47.660 1.00 19.25  ?  188  TYR B C      1 
ATOM   10107 O O      . TYR B 2 188 ? 33.430  -30.660 -47.440 1.00 20.15  ?  188  TYR B O      1 
ATOM   10108 C CB     . TYR B 2 188 ? 32.637  -27.677 -47.864 1.00 18.45  ?  188  TYR B CB     1 
ATOM   10109 C CG     . TYR B 2 188 ? 34.016  -27.712 -47.237 1.00 19.99  ?  188  TYR B CG     1 
ATOM   10110 C CD1    . TYR B 2 188 ? 35.164  -27.660 -48.024 1.00 21.91  ?  188  TYR B CD1    1 
ATOM   10111 C CD2    . TYR B 2 188 ? 34.174  -27.768 -45.856 1.00 22.18  ?  188  TYR B CD2    1 
ATOM   10112 C CE1    . TYR B 2 188 ? 36.417  -27.670 -47.452 1.00 23.39  ?  188  TYR B CE1    1 
ATOM   10113 C CE2    . TYR B 2 188 ? 35.431  -27.780 -45.281 1.00 23.36  ?  188  TYR B CE2    1 
ATOM   10114 C CZ     . TYR B 2 188 ? 36.547  -27.746 -46.091 1.00 24.13  ?  188  TYR B CZ     1 
ATOM   10115 O OH     . TYR B 2 188 ? 37.803  -27.766 -45.534 1.00 27.24  ?  188  TYR B OH     1 
ATOM   10116 H H      . TYR B 2 188 ? 30.438  -28.062 -48.796 1.00 22.59  ?  188  TYR B H      1 
ATOM   10117 H HA     . TYR B 2 188 ? 32.809  -29.113 -49.310 1.00 22.24  ?  188  TYR B HA     1 
ATOM   10118 H HB2    . TYR B 2 188 ? 32.633  -26.954 -48.510 1.00 22.13  ?  188  TYR B HB2    1 
ATOM   10119 H HB3    . TYR B 2 188 ? 32.003  -27.490 -47.154 1.00 22.13  ?  188  TYR B HB3    1 
ATOM   10120 H HD1    . TYR B 2 188 ? 35.084  -27.619 -48.950 1.00 26.28  ?  188  TYR B HD1    1 
ATOM   10121 H HD2    . TYR B 2 188 ? 33.422  -27.797 -45.311 1.00 26.61  ?  188  TYR B HD2    1 
ATOM   10122 H HE1    . TYR B 2 188 ? 37.174  -27.626 -47.990 1.00 28.07  ?  188  TYR B HE1    1 
ATOM   10123 H HE2    . TYR B 2 188 ? 35.523  -27.812 -44.356 1.00 28.03  ?  188  TYR B HE2    1 
ATOM   10124 H HH     . TYR B 2 188 ? 37.745  -27.812 -44.697 1.00 32.69  ?  188  TYR B HH     1 
ATOM   10125 N N      . HIS B 2 189 ? 31.207  -30.707 -47.169 1.00 18.74  ?  189  HIS B N      1 
ATOM   10126 C CA     . HIS B 2 189 ? 31.234  -31.890 -46.324 1.00 19.51  ?  189  HIS B CA     1 
ATOM   10127 C C      . HIS B 2 189 ? 30.915  -33.176 -47.081 1.00 19.15  ?  189  HIS B C      1 
ATOM   10128 O O      . HIS B 2 189 ? 30.723  -34.225 -46.452 1.00 21.25  ?  189  HIS B O      1 
ATOM   10129 C CB     . HIS B 2 189 ? 30.263  -31.734 -45.148 1.00 19.41  ?  189  HIS B CB     1 
ATOM   10130 C CG     . HIS B 2 189 ? 30.800  -30.895 -44.033 1.00 19.84  ?  189  HIS B CG     1 
ATOM   10131 N ND1    . HIS B 2 189 ? 30.170  -30.786 -42.811 1.00 21.38  ?  189  HIS B ND1    1 
ATOM   10132 C CD2    . HIS B 2 189 ? 31.895  -30.098 -43.969 1.00 21.47  ?  189  HIS B CD2    1 
ATOM   10133 C CE1    . HIS B 2 189 ? 30.869  -29.970 -42.037 1.00 23.56  ?  189  HIS B CE1    1 
ATOM   10134 N NE2    . HIS B 2 189 ? 31.916  -29.539 -42.719 1.00 23.08  ?  189  HIS B NE2    1 
ATOM   10135 H H      . HIS B 2 189 ? 30.418  -30.397 -47.314 1.00 22.49  ?  189  HIS B H      1 
ATOM   10136 H HA     . HIS B 2 189 ? 32.131  -31.972 -45.964 1.00 23.41  ?  189  HIS B HA     1 
ATOM   10137 H HB2    . HIS B 2 189 ? 29.449  -31.316 -45.468 1.00 23.29  ?  189  HIS B HB2    1 
ATOM   10138 H HB3    . HIS B 2 189 ? 30.065  -32.613 -44.788 1.00 23.29  ?  189  HIS B HB3    1 
ATOM   10139 H HD2    . HIS B 2 189 ? 32.516  -29.957 -44.647 1.00 25.77  ?  189  HIS B HD2    1 
ATOM   10140 H HE1    . HIS B 2 189 ? 30.658  -29.739 -41.161 1.00 28.27  ?  189  HIS B HE1    1 
ATOM   10141 H HE2    . HIS B 2 189 ? 32.514  -28.996 -42.425 1.00 27.69  ?  189  HIS B HE2    1 
ATOM   10142 N N      . ARG B 2 190 ? 30.823  -33.129 -48.408 1.00 21.17  ?  190  ARG B N      1 
ATOM   10143 C CA     . ARG B 2 190 ? 30.467  -34.334 -49.139 1.00 22.98  ?  190  ARG B CA     1 
ATOM   10144 C C      . ARG B 2 190 ? 31.534  -35.402 -48.916 1.00 24.50  ?  190  ARG B C      1 
ATOM   10145 O O      . ARG B 2 190 ? 32.685  -35.109 -48.586 1.00 23.80  ?  190  ARG B O      1 
ATOM   10146 C CB     . ARG B 2 190 ? 30.305  -34.029 -50.631 1.00 23.20  ?  190  ARG B CB     1 
ATOM   10147 C CG     . ARG B 2 190 ? 31.597  -33.698 -51.353 1.00 23.72  ?  190  ARG B CG     1 
ATOM   10148 C CD     . ARG B 2 190 ? 31.335  -32.980 -52.675 1.00 22.73  ?  190  ARG B CD     1 
ATOM   10149 N NE     . ARG B 2 190 ? 32.591  -32.737 -53.381 1.00 23.26  ?  190  ARG B NE     1 
ATOM   10150 C CZ     . ARG B 2 190 ? 33.414  -31.727 -53.135 1.00 24.73  ?  190  ARG B CZ     1 
ATOM   10151 N NH1    . ARG B 2 190 ? 33.127  -30.832 -52.192 1.00 23.11  ?  190  ARG B NH1    1 
ATOM   10152 N NH2    . ARG B 2 190 ? 34.535  -31.622 -53.834 1.00 27.04  ?  190  ARG B NH2    1 
ATOM   10153 H H      . ARG B 2 190 ? 30.959  -32.433 -48.893 1.00 25.40  ?  190  ARG B H      1 
ATOM   10154 H HA     . ARG B 2 190 ? 29.617  -34.679 -48.823 1.00 27.58  ?  190  ARG B HA     1 
ATOM   10155 H HB2    . ARG B 2 190 ? 29.920  -34.806 -51.065 1.00 27.84  ?  190  ARG B HB2    1 
ATOM   10156 H HB3    . ARG B 2 190 ? 29.713  -33.267 -50.728 1.00 27.84  ?  190  ARG B HB3    1 
ATOM   10157 H HG2    . ARG B 2 190 ? 32.138  -33.118 -50.793 1.00 28.46  ?  190  ARG B HG2    1 
ATOM   10158 H HG3    . ARG B 2 190 ? 32.078  -34.518 -51.542 1.00 28.46  ?  190  ARG B HG3    1 
ATOM   10159 H HD2    . ARG B 2 190 ? 30.765  -33.529 -53.236 1.00 27.27  ?  190  ARG B HD2    1 
ATOM   10160 H HD3    . ARG B 2 190 ? 30.907  -32.127 -52.502 1.00 27.27  ?  190  ARG B HD3    1 
ATOM   10161 H HE     . ARG B 2 190 ? 32.813  -33.290 -54.001 1.00 27.91  ?  190  ARG B HE     1 
ATOM   10162 H HH11   . ARG B 2 190 ? 32.402  -30.906 -51.736 1.00 27.72  ?  190  ARG B HH11   1 
ATOM   10163 H HH12   . ARG B 2 190 ? 33.667  -30.180 -52.040 1.00 27.72  ?  190  ARG B HH12   1 
ATOM   10164 H HH21   . ARG B 2 190 ? 34.721  -32.204 -54.439 1.00 32.44  ?  190  ARG B HH21   1 
ATOM   10165 H HH22   . ARG B 2 190 ? 35.076  -30.971 -53.683 1.00 32.44  ?  190  ARG B HH22   1 
ATOM   10166 N N      . GLY B 2 191 ? 31.134  -36.658 -49.068 1.00 25.99  ?  191  GLY B N      1 
ATOM   10167 C CA     . GLY B 2 191 ? 32.062  -37.742 -48.820 1.00 28.95  ?  191  GLY B CA     1 
ATOM   10168 C C      . GLY B 2 191 ? 33.255  -37.691 -49.755 1.00 31.08  ?  191  GLY B C      1 
ATOM   10169 O O      . GLY B 2 191 ? 33.183  -37.174 -50.872 1.00 29.77  ?  191  GLY B O      1 
ATOM   10170 H H      . GLY B 2 191 ? 30.346  -36.904 -49.309 1.00 31.18  ?  191  GLY B H      1 
ATOM   10171 H HA2    . GLY B 2 191 ? 32.384  -37.689 -47.907 1.00 34.74  ?  191  GLY B HA2    1 
ATOM   10172 H HA3    . GLY B 2 191 ? 31.608  -38.590 -48.946 1.00 34.74  ?  191  GLY B HA3    1 
ATOM   10173 N N      . ALA B 2 192 ? 34.375  -38.246 -49.281 1.00 34.05  ?  192  ALA B N      1 
ATOM   10174 C CA     . ALA B 2 192 ? 35.547  -38.393 -50.135 1.00 36.13  ?  192  ALA B CA     1 
ATOM   10175 C C      . ALA B 2 192 ? 35.203  -39.132 -51.414 1.00 37.56  ?  192  ALA B C      1 
ATOM   10176 O O      . ALA B 2 192 ? 35.776  -38.843 -52.472 1.00 37.94  ?  192  ALA B O      1 
ATOM   10177 C CB     . ALA B 2 192 ? 36.637  -39.153 -49.376 1.00 37.15  ?  192  ALA B CB     1 
ATOM   10178 H H      . ALA B 2 192 ? 34.479  -38.541 -48.480 1.00 40.85  ?  192  ALA B H      1 
ATOM   10179 H HA     . ALA B 2 192 ? 35.886  -37.515 -50.368 1.00 43.36  ?  192  ALA B HA     1 
ATOM   10180 H HB1    . ALA B 2 192 ? 37.398  -39.283 -49.964 1.00 44.57  ?  192  ALA B HB1    1 
ATOM   10181 H HB2    . ALA B 2 192 ? 36.903  -38.634 -48.602 1.00 44.57  ?  192  ALA B HB2    1 
ATOM   10182 H HB3    . ALA B 2 192 ? 36.286  -40.012 -49.094 1.00 44.57  ?  192  ALA B HB3    1 
ATOM   10183 N N      . GLU B 2 193 ? 34.270  -40.081 -51.342 1.00 38.89  ?  193  GLU B N      1 
ATOM   10184 C CA     . GLU B 2 193 ? 33.831  -40.804 -52.528 1.00 42.53  ?  193  GLU B CA     1 
ATOM   10185 C C      . GLU B 2 193 ? 33.132  -39.902 -53.533 1.00 40.56  ?  193  GLU B C      1 
ATOM   10186 O O      . GLU B 2 193 ? 32.925  -40.319 -54.679 1.00 41.61  ?  193  GLU B O      1 
ATOM   10187 C CB     . GLU B 2 193 ? 32.911  -41.955 -52.104 1.00 47.72  ?  193  GLU B CB     1 
ATOM   10188 C CG     . GLU B 2 193 ? 31.645  -41.538 -51.336 1.00 52.80  ?  193  GLU B CG     1 
ATOM   10189 C CD     . GLU B 2 193 ? 31.859  -41.367 -49.837 1.00 56.46  ?  193  GLU B CD     1 
ATOM   10190 O OE1    . GLU B 2 193 ? 33.028  -41.311 -49.395 1.00 57.45  ?  193  GLU B OE1    1 
ATOM   10191 O OE2    . GLU B 2 193 ? 30.852  -41.285 -49.097 1.00 58.58  -1 193  GLU B OE2    1 
ATOM   10192 H H      . GLU B 2 193 ? 33.875  -40.324 -50.617 1.00 46.67  ?  193  GLU B H      1 
ATOM   10193 H HA     . GLU B 2 193 ? 34.601  -41.189 -52.976 1.00 51.03  ?  193  GLU B HA     1 
ATOM   10194 H HB2    . GLU B 2 193 ? 32.623  -42.426 -52.902 1.00 57.26  ?  193  GLU B HB2    1 
ATOM   10195 H HB3    . GLU B 2 193 ? 33.414  -42.554 -51.530 1.00 57.26  ?  193  GLU B HB3    1 
ATOM   10196 H HG2    . GLU B 2 193 ? 31.332  -40.690 -51.688 1.00 63.35  ?  193  GLU B HG2    1 
ATOM   10197 H HG3    . GLU B 2 193 ? 30.966  -42.219 -51.461 1.00 63.35  ?  193  GLU B HG3    1 
ATOM   10198 N N      . ARG B 2 194 ? 32.778  -38.676 -53.137 1.00 37.23  ?  194  ARG B N      1 
ATOM   10199 C CA     . ARG B 2 194 ? 32.122  -37.718 -54.016 1.00 34.34  ?  194  ARG B CA     1 
ATOM   10200 C C      . ARG B 2 194 ? 32.972  -36.483 -54.266 1.00 30.14  ?  194  ARG B C      1 
ATOM   10201 O O      . ARG B 2 194 ? 32.443  -35.436 -54.646 1.00 27.41  ?  194  ARG B O      1 
ATOM   10202 C CB     . ARG B 2 194 ? 30.756  -37.335 -53.452 1.00 36.64  ?  194  ARG B CB     1 
ATOM   10203 C CG     . ARG B 2 194 ? 29.731  -38.404 -53.716 1.00 41.22  ?  194  ARG B CG     1 
ATOM   10204 C CD     . ARG B 2 194 ? 28.516  -38.280 -52.825 1.00 44.76  ?  194  ARG B CD     1 
ATOM   10205 N NE     . ARG B 2 194 ? 27.748  -39.514 -52.919 1.00 48.93  ?  194  ARG B NE     1 
ATOM   10206 C CZ     . ARG B 2 194 ? 27.622  -40.408 -51.942 1.00 51.94  ?  194  ARG B CZ     1 
ATOM   10207 N NH1    . ARG B 2 194 ? 26.904  -41.503 -52.159 1.00 53.52  ?  194  ARG B NH1    1 
ATOM   10208 N NH2    . ARG B 2 194 ? 28.178  -40.207 -50.751 1.00 52.28  ?  194  ARG B NH2    1 
ATOM   10209 H H      . ARG B 2 194 ? 32.914  -38.374 -52.344 1.00 44.68  ?  194  ARG B H      1 
ATOM   10210 H HA     . ARG B 2 194 ? 31.979  -38.138 -54.879 1.00 41.20  ?  194  ARG B HA     1 
ATOM   10211 H HB2    . ARG B 2 194 ? 30.828  -37.211 -52.492 1.00 43.96  ?  194  ARG B HB2    1 
ATOM   10212 H HB3    . ARG B 2 194 ? 30.455  -36.513 -53.870 1.00 43.96  ?  194  ARG B HB3    1 
ATOM   10213 H HG2    . ARG B 2 194 ? 29.434  -38.338 -54.637 1.00 49.46  ?  194  ARG B HG2    1 
ATOM   10214 H HG3    . ARG B 2 194 ? 30.131  -39.273 -53.558 1.00 49.46  ?  194  ARG B HG3    1 
ATOM   10215 H HD2    . ARG B 2 194 ? 28.791  -38.146 -51.905 1.00 53.71  ?  194  ARG B HD2    1 
ATOM   10216 H HD3    . ARG B 2 194 ? 27.963  -37.539 -53.118 1.00 53.71  ?  194  ARG B HD3    1 
ATOM   10217 H HE     . ARG B 2 194 ? 27.347  -39.677 -53.662 1.00 58.71  ?  194  ARG B HE     1 
ATOM   10218 H HH11   . ARG B 2 194 ? 26.529  -41.627 -52.922 1.00 64.22  ?  194  ARG B HH11   1 
ATOM   10219 H HH12   . ARG B 2 194 ? 26.815  -42.089 -51.535 1.00 64.22  ?  194  ARG B HH12   1 
ATOM   10220 H HH21   . ARG B 2 194 ? 28.628  -39.489 -50.602 1.00 62.73  ?  194  ARG B HH21   1 
ATOM   10221 H HH22   . ARG B 2 194 ? 28.087  -40.794 -50.129 1.00 62.73  ?  194  ARG B HH22   1 
ATOM   10222 N N      . GLU B 2 195 ? 34.284  -36.593 -54.076 1.00 30.42  ?  195  GLU B N      1 
ATOM   10223 C CA     . GLU B 2 195 ? 35.167  -35.450 -54.277 1.00 31.86  ?  195  GLU B CA     1 
ATOM   10224 C C      . GLU B 2 195 ? 34.997  -34.847 -55.661 1.00 30.89  ?  195  GLU B C      1 
ATOM   10225 O O      . GLU B 2 195 ? 35.057  -33.623 -55.824 1.00 30.89  ?  195  GLU B O      1 
ATOM   10226 C CB     . GLU B 2 195 ? 36.625  -35.883 -54.088 1.00 34.10  ?  195  GLU B CB     1 
ATOM   10227 C CG     . GLU B 2 195 ? 37.647  -34.795 -54.387 1.00 35.49  ?  195  GLU B CG     1 
ATOM   10228 C CD     . GLU B 2 195 ? 37.725  -33.738 -53.302 1.00 35.49  ?  195  GLU B CD     1 
ATOM   10229 O OE1    . GLU B 2 195 ? 37.318  -34.023 -52.156 1.00 33.85  ?  195  GLU B OE1    1 
ATOM   10230 O OE2    . GLU B 2 195 ? 38.188  -32.618 -53.594 1.00 37.40  -1 195  GLU B OE2    1 
ATOM   10231 H H      . GLU B 2 195 ? 34.688  -37.312 -53.833 1.00 36.51  ?  195  GLU B H      1 
ATOM   10232 H HA     . GLU B 2 195 ? 34.946  -34.774 -53.617 1.00 38.22  ?  195  GLU B HA     1 
ATOM   10233 H HB2    . GLU B 2 195 ? 36.749  -36.158 -53.165 1.00 40.91  ?  195  GLU B HB2    1 
ATOM   10234 H HB3    . GLU B 2 195 ? 36.806  -36.628 -54.682 1.00 40.91  ?  195  GLU B HB3    1 
ATOM   10235 H HG2    . GLU B 2 195 ? 38.524  -35.201 -54.472 1.00 42.59  ?  195  GLU B HG2    1 
ATOM   10236 H HG3    . GLU B 2 195 ? 37.403  -34.354 -55.216 1.00 42.59  ?  195  GLU B HG3    1 
ATOM   10237 N N      . GLY B 2 196 ? 34.822  -35.692 -56.675 1.00 31.10  ?  196  GLY B N      1 
ATOM   10238 C CA     . GLY B 2 196 ? 34.790  -35.222 -58.040 1.00 31.04  ?  196  GLY B CA     1 
ATOM   10239 C C      . GLY B 2 196 ? 33.515  -34.545 -58.476 1.00 30.58  ?  196  GLY B C      1 
ATOM   10240 O O      . GLY B 2 196 ? 33.466  -34.010 -59.585 1.00 32.25  ?  196  GLY B O      1 
ATOM   10241 H H      . GLY B 2 196 ? 34.719  -36.542 -56.590 1.00 37.32  ?  196  GLY B H      1 
ATOM   10242 H HA2    . GLY B 2 196 ? 35.513  -34.587 -58.162 1.00 37.25  ?  196  GLY B HA2    1 
ATOM   10243 H HA3    . GLY B 2 196 ? 34.933  -35.980 -58.629 1.00 37.25  ?  196  GLY B HA3    1 
ATOM   10244 N N      . MET B 2 197 ? 32.485  -34.555 -57.634 1.00 29.28  ?  197  MET B N      1 
ATOM   10245 C CA     . MET B 2 197 ? 31.241  -33.889 -57.973 1.00 27.04  ?  197  MET B CA     1 
ATOM   10246 C C      . MET B 2 197 ? 31.427  -32.378 -58.012 1.00 26.05  ?  197  MET B C      1 
ATOM   10247 O O      . MET B 2 197 ? 32.024  -31.789 -57.102 1.00 26.94  ?  197  MET B O      1 
ATOM   10248 C CB     . MET B 2 197 ? 30.161  -34.196 -56.929 1.00 27.85  ?  197  MET B CB     1 
ATOM   10249 C CG     . MET B 2 197 ? 29.539  -35.563 -57.060 1.00 29.40  ?  197  MET B CG     1 
ATOM   10250 S SD     . MET B 2 197 ? 28.122  -35.840 -55.991 1.00 30.84  ?  197  MET B SD     1 
ATOM   10251 C CE     . MET B 2 197 ? 27.566  -37.407 -56.676 1.00 31.93  ?  197  MET B CE     1 
ATOM   10252 H H      . MET B 2 197 ? 32.484  -34.940 -56.865 1.00 35.13  ?  197  MET B H      1 
ATOM   10253 H HA     . MET B 2 197 ? 30.961  -34.220 -58.841 1.00 32.44  ?  197  MET B HA     1 
ATOM   10254 H HB2    . MET B 2 197 ? 30.560  -34.139 -56.046 1.00 33.41  ?  197  MET B HB2    1 
ATOM   10255 H HB3    . MET B 2 197 ? 29.451  -33.541 -57.016 1.00 33.41  ?  197  MET B HB3    1 
ATOM   10256 H HG2    . MET B 2 197 ? 29.243  -35.682 -57.976 1.00 35.27  ?  197  MET B HG2    1 
ATOM   10257 H HG3    . MET B 2 197 ? 30.208  -36.230 -56.839 1.00 35.27  ?  197  MET B HG3    1 
ATOM   10258 H HE1    . MET B 2 197 ? 26.865  -37.767 -56.111 1.00 38.31  ?  197  MET B HE1    1 
ATOM   10259 H HE2    . MET B 2 197 ? 27.225  -37.257 -57.572 1.00 38.31  ?  197  MET B HE2    1 
ATOM   10260 H HE3    . MET B 2 197 ? 28.315  -38.022 -56.706 1.00 38.31  ?  197  MET B HE3    1 
ATOM   10261 N N      . SER B 2 198 ? 30.881  -31.754 -59.058 1.00 22.99  ?  198  SER B N      1 
ATOM   10262 C CA     . SER B 2 198 ? 30.639  -30.328 -59.047 1.00 24.21  ?  198  SER B CA     1 
ATOM   10263 C C      . SER B 2 198 ? 29.475  -30.023 -58.110 1.00 22.26  ?  198  SER B C      1 
ATOM   10264 O O      . SER B 2 198 ? 28.756  -30.917 -57.650 1.00 21.77  ?  198  SER B O      1 
ATOM   10265 C CB     . SER B 2 198 ? 30.228  -29.853 -60.434 1.00 25.32  ?  198  SER B CB     1 
ATOM   10266 O OG     . SER B 2 198 ? 28.990  -30.440 -60.790 1.00 26.34  ?  198  SER B OG     1 
ATOM   10267 H H      . SER B 2 198 ? 30.644  -32.143 -59.787 1.00 27.58  ?  198  SER B H      1 
ATOM   10268 H HA     . SER B 2 198 ? 31.446  -29.872 -58.762 1.00 29.05  ?  198  SER B HA     1 
ATOM   10269 H HB2    . SER B 2 198 ? 30.136  -28.887 -60.428 1.00 30.38  ?  198  SER B HB2    1 
ATOM   10270 H HB3    . SER B 2 198 ? 30.905  -30.117 -61.077 1.00 30.38  ?  198  SER B HB3    1 
ATOM   10271 H HG     . SER B 2 198 ? 28.756  -30.176 -61.553 1.00 31.60  ?  198  SER B HG     1 
ATOM   10272 N N      . GLU B 2 199 ? 29.266  -28.732 -57.846 1.00 21.26  ?  199  GLU B N      1 
ATOM   10273 C CA     . GLU B 2 199 ? 28.116  -28.351 -57.031 1.00 21.36  ?  199  GLU B CA     1 
ATOM   10274 C C      . GLU B 2 199 ? 26.810  -28.834 -57.654 1.00 20.61  ?  199  GLU B C      1 
ATOM   10275 O O      . GLU B 2 199 ? 25.944  -29.366 -56.955 1.00 20.00  ?  199  GLU B O      1 
ATOM   10276 C CB     . GLU B 2 199 ? 28.064  -26.838 -56.836 1.00 21.57  ?  199  GLU B CB     1 
ATOM   10277 C CG     . GLU B 2 199 ? 29.087  -26.285 -55.893 1.00 23.00  ?  199  GLU B CG     1 
ATOM   10278 C CD     . GLU B 2 199 ? 28.849  -24.817 -55.578 1.00 24.27  ?  199  GLU B CD     1 
ATOM   10279 O OE1    . GLU B 2 199 ? 29.823  -24.113 -55.269 1.00 26.31  ?  199  GLU B OE1    1 
ATOM   10280 O OE2    . GLU B 2 199 ? 27.692  -24.360 -55.646 1.00 23.96  -1 199  GLU B OE2    1 
ATOM   10281 H H      . GLU B 2 199 ? 29.758  -28.080 -58.117 1.00 25.51  ?  199  GLU B H      1 
ATOM   10282 H HA     . GLU B 2 199 ? 28.222  -28.766 -56.161 1.00 25.63  ?  199  GLU B HA     1 
ATOM   10283 H HB2    . GLU B 2 199 ? 28.202  -26.413 -57.697 1.00 25.88  ?  199  GLU B HB2    1 
ATOM   10284 H HB3    . GLU B 2 199 ? 27.190  -26.604 -56.487 1.00 25.88  ?  199  GLU B HB3    1 
ATOM   10285 H HG2    . GLU B 2 199 ? 29.053  -26.781 -55.060 1.00 27.60  ?  199  GLU B HG2    1 
ATOM   10286 H HG3    . GLU B 2 199 ? 29.967  -26.369 -56.293 1.00 27.60  ?  199  GLU B HG3    1 
ATOM   10287 N N      . ARG B 2 200 ? 26.634  -28.618 -58.969 1.00 22.24  ?  200  ARG B N      1 
ATOM   10288 C CA     . ARG B 2 200 ? 25.401  -29.060 -59.623 1.00 23.62  ?  200  ARG B CA     1 
ATOM   10289 C C      . ARG B 2 200 ? 25.225  -30.572 -59.503 1.00 20.92  ?  200  ARG B C      1 
ATOM   10290 O O      . ARG B 2 200 ? 24.107  -31.062 -59.296 1.00 21.57  ?  200  ARG B O      1 
ATOM   10291 C CB     . ARG B 2 200 ? 25.377  -28.650 -61.095 1.00 29.87  ?  200  ARG B CB     1 
ATOM   10292 C CG     . ARG B 2 200 ? 25.237  -27.169 -61.316 1.00 39.09  ?  200  ARG B CG     1 
ATOM   10293 C CD     . ARG B 2 200 ? 25.149  -26.810 -62.812 1.00 48.08  ?  200  ARG B CD     1 
ATOM   10294 N NE     . ARG B 2 200 ? 25.178  -25.358 -62.997 1.00 56.98  ?  200  ARG B NE     1 
ATOM   10295 C CZ     . ARG B 2 200 ? 25.337  -24.737 -64.168 1.00 63.61  ?  200  ARG B CZ     1 
ATOM   10296 N NH1    . ARG B 2 200 ? 25.352  -23.408 -64.208 1.00 66.14  ?  200  ARG B NH1    1 
ATOM   10297 N NH2    . ARG B 2 200 ? 25.482  -25.425 -65.297 1.00 65.98  ?  200  ARG B NH2    1 
ATOM   10298 H H      . ARG B 2 200 ? 27.199  -28.229 -59.488 1.00 26.69  ?  200  ARG B H      1 
ATOM   10299 H HA     . ARG B 2 200 ? 24.658  -28.619 -59.183 1.00 28.34  ?  200  ARG B HA     1 
ATOM   10300 H HB2    . ARG B 2 200 ? 26.206  -28.934 -61.511 1.00 35.83  ?  200  ARG B HB2    1 
ATOM   10301 H HB3    . ARG B 2 200 ? 24.624  -29.085 -61.526 1.00 35.83  ?  200  ARG B HB3    1 
ATOM   10302 H HG2    . ARG B 2 200 ? 24.428  -26.857 -60.882 1.00 46.91  ?  200  ARG B HG2    1 
ATOM   10303 H HG3    . ARG B 2 200 ? 26.010  -26.717 -60.942 1.00 46.91  ?  200  ARG B HG3    1 
ATOM   10304 H HD2    . ARG B 2 200 ? 25.903  -27.197 -63.283 1.00 57.69  ?  200  ARG B HD2    1 
ATOM   10305 H HD3    . ARG B 2 200 ? 24.318  -27.151 -63.178 1.00 57.69  ?  200  ARG B HD3    1 
ATOM   10306 H HE     . ARG B 2 200 ? 25.086  -24.867 -62.297 1.00 68.37  ?  200  ARG B HE     1 
ATOM   10307 H HH11   . ARG B 2 200 ? 25.259  -22.955 -63.483 1.00 79.36  ?  200  ARG B HH11   1 
ATOM   10308 H HH12   . ARG B 2 200 ? 25.454  -23.002 -64.959 1.00 79.36  ?  200  ARG B HH12   1 
ATOM   10309 H HH21   . ARG B 2 200 ? 25.474  -26.285 -65.280 1.00 79.18  ?  200  ARG B HH21   1 
ATOM   10310 H HH22   . ARG B 2 200 ? 25.583  -25.010 -66.043 1.00 79.18  ?  200  ARG B HH22   1 
ATOM   10311 N N      . GLU B 2 201 ? 26.312  -31.327 -59.651 1.00 22.16  ?  201  GLU B N      1 
ATOM   10312 C CA     . GLU B 2 201 ? 26.232  -32.773 -59.475 1.00 21.55  ?  201  GLU B CA     1 
ATOM   10313 C C      . GLU B 2 201 ? 25.857  -33.132 -58.043 1.00 20.68  ?  201  GLU B C      1 
ATOM   10314 O O      . GLU B 2 201 ? 25.059  -34.052 -57.808 1.00 22.54  ?  201  GLU B O      1 
ATOM   10315 C CB     . GLU B 2 201 ? 27.556  -33.405 -59.885 1.00 22.35  ?  201  GLU B CB     1 
ATOM   10316 C CG     . GLU B 2 201 ? 27.732  -33.455 -61.399 1.00 24.82  ?  201  GLU B CG     1 
ATOM   10317 C CD     . GLU B 2 201 ? 29.113  -33.897 -61.841 1.00 29.26  ?  201  GLU B CD     1 
ATOM   10318 O OE1    . GLU B 2 201 ? 30.075  -33.720 -61.075 1.00 29.26  ?  201  GLU B OE1    1 
ATOM   10319 O OE2    . GLU B 2 201 ? 29.235  -34.419 -62.970 1.00 34.12  -1 201  GLU B OE2    1 
ATOM   10320 H H      . GLU B 2 201 ? 27.095  -31.033 -59.851 1.00 26.59  ?  201  GLU B H      1 
ATOM   10321 H HA     . GLU B 2 201 ? 25.540  -33.135 -60.051 1.00 25.85  ?  201  GLU B HA     1 
ATOM   10322 H HB2    . GLU B 2 201 ? 28.285  -32.883 -59.513 1.00 26.82  ?  201  GLU B HB2    1 
ATOM   10323 H HB3    . GLU B 2 201 ? 27.592  -34.313 -59.546 1.00 26.82  ?  201  GLU B HB3    1 
ATOM   10324 H HG2    . GLU B 2 201 ? 27.090  -34.081 -61.767 1.00 29.78  ?  201  GLU B HG2    1 
ATOM   10325 H HG3    . GLU B 2 201 ? 27.576  -32.568 -61.761 1.00 29.78  ?  201  GLU B HG3    1 
ATOM   10326 N N      . PHE B 2 202 ? 26.403  -32.400 -57.069 1.00 18.97  ?  202  PHE B N      1 
ATOM   10327 C CA     . PHE B 2 202 ? 26.052  -32.651 -55.678 1.00 17.15  ?  202  PHE B CA     1 
ATOM   10328 C C      . PHE B 2 202 ? 24.593  -32.312 -55.421 1.00 18.09  ?  202  PHE B C      1 
ATOM   10329 O O      . PHE B 2 202 ? 23.908  -33.035 -54.703 1.00 17.94  ?  202  PHE B O      1 
ATOM   10330 C CB     . PHE B 2 202 ? 26.996  -31.880 -54.767 1.00 18.14  ?  202  PHE B CB     1 
ATOM   10331 C CG     . PHE B 2 202 ? 26.681  -32.022 -53.312 1.00 16.61  ?  202  PHE B CG     1 
ATOM   10332 C CD1    . PHE B 2 202 ? 26.954  -33.191 -52.642 1.00 19.64  ?  202  PHE B CD1    1 
ATOM   10333 C CD2    . PHE B 2 202 ? 26.077  -30.989 -52.629 1.00 18.22  ?  202  PHE B CD2    1 
ATOM   10334 C CE1    . PHE B 2 202 ? 26.642  -33.317 -51.287 1.00 19.82  ?  202  PHE B CE1    1 
ATOM   10335 C CE2    . PHE B 2 202 ? 25.771  -31.101 -51.285 1.00 19.05  ?  202  PHE B CE2    1 
ATOM   10336 C CZ     . PHE B 2 202 ? 26.035  -32.268 -50.622 1.00 19.24  ?  202  PHE B CZ     1 
ATOM   10337 H H      . PHE B 2 202 ? 26.970  -31.764 -57.186 1.00 22.76  ?  202  PHE B H      1 
ATOM   10338 H HA     . PHE B 2 202 ? 26.164  -33.592 -55.470 1.00 20.57  ?  202  PHE B HA     1 
ATOM   10339 H HB2    . PHE B 2 202 ? 27.899  -32.206 -54.907 1.00 21.76  ?  202  PHE B HB2    1 
ATOM   10340 H HB3    . PHE B 2 202 ? 26.945  -30.938 -54.991 1.00 21.76  ?  202  PHE B HB3    1 
ATOM   10341 H HD1    . PHE B 2 202 ? 27.348  -33.902 -53.094 1.00 23.57  ?  202  PHE B HD1    1 
ATOM   10342 H HD2    . PHE B 2 202 ? 25.872  -30.202 -53.080 1.00 21.86  ?  202  PHE B HD2    1 
ATOM   10343 H HE1    . PHE B 2 202 ? 26.841  -34.104 -50.834 1.00 23.78  ?  202  PHE B HE1    1 
ATOM   10344 H HE2    . PHE B 2 202 ? 25.387  -30.385 -50.833 1.00 22.86  ?  202  PHE B HE2    1 
ATOM   10345 H HZ     . PHE B 2 202 ? 25.807  -32.356 -49.725 1.00 23.08  ?  202  PHE B HZ     1 
ATOM   10346 N N      . SER B 2 203 ? 24.089  -31.236 -56.026 1.00 18.81  ?  203  SER B N      1 
ATOM   10347 C CA     . SER B 2 203 ? 22.667  -30.935 -55.905 1.00 16.85  ?  203  SER B CA     1 
ATOM   10348 C C      . SER B 2 203 ? 21.807  -32.045 -56.479 1.00 17.76  ?  203  SER B C      1 
ATOM   10349 O O      . SER B 2 203 ? 20.797  -32.424 -55.875 1.00 17.07  ?  203  SER B O      1 
ATOM   10350 C CB     . SER B 2 203 ? 22.341  -29.610 -56.595 1.00 16.51  ?  203  SER B CB     1 
ATOM   10351 O OG     . SER B 2 203 ? 22.926  -28.554 -55.879 1.00 17.70  ?  203  SER B OG     1 
ATOM   10352 H H      . SER B 2 203 ? 24.537  -30.677 -56.502 1.00 22.57  ?  203  SER B H      1 
ATOM   10353 H HA     . SER B 2 203 ? 22.459  -30.846 -54.962 1.00 20.21  ?  203  SER B HA     1 
ATOM   10354 H HB2    . SER B 2 203 ? 22.696  -29.622 -57.498 1.00 19.80  ?  203  SER B HB2    1 
ATOM   10355 H HB3    . SER B 2 203 ? 21.379  -29.489 -56.619 1.00 19.80  ?  203  SER B HB3    1 
ATOM   10356 H HG     . SER B 2 203 ? 22.819  -27.832 -56.295 1.00 21.24  ?  203  SER B HG     1 
ATOM   10357 N N      . ALA B 2 204 ? 22.171  -32.562 -57.654 1.00 17.16  ?  204  ALA B N      1 
ATOM   10358 C CA     . ALA B 2 204 ? 21.416  -33.677 -58.219 1.00 18.49  ?  204  ALA B CA     1 
ATOM   10359 C C      . ALA B 2 204 ? 21.457  -34.875 -57.281 1.00 17.40  ?  204  ALA B C      1 
ATOM   10360 O O      . ALA B 2 204 ? 20.451  -35.578 -57.116 1.00 19.88  ?  204  ALA B O      1 
ATOM   10361 C CB     . ALA B 2 204 ? 21.965  -34.063 -59.596 1.00 20.71  ?  204  ALA B CB     1 
ATOM   10362 H H      . ALA B 2 204 ? 22.833  -32.293 -58.133 1.00 20.58  ?  204  ALA B H      1 
ATOM   10363 H HA     . ALA B 2 204 ? 20.494  -33.400 -58.341 1.00 22.18  ?  204  ALA B HA     1 
ATOM   10364 H HB1    . ALA B 2 204 ? 21.415  -34.770 -59.968 1.00 24.85  ?  204  ALA B HB1    1 
ATOM   10365 H HB2    . ALA B 2 204 ? 21.940  -33.285 -60.175 1.00 24.85  ?  204  ALA B HB2    1 
ATOM   10366 H HB3    . ALA B 2 204 ? 22.879  -34.372 -59.496 1.00 24.85  ?  204  ALA B HB3    1 
ATOM   10367 N N      . HIS B 2 205 ? 22.614  -35.126 -56.663 1.00 19.18  ?  205  HIS B N      1 
ATOM   10368 C CA     . HIS B 2 205 ? 22.723  -36.202 -55.675 1.00 17.01  ?  205  HIS B CA     1 
ATOM   10369 C C      . HIS B 2 205 ? 21.772  -35.977 -54.502 1.00 18.47  ?  205  HIS B C      1 
ATOM   10370 O O      . HIS B 2 205 ? 21.080  -36.905 -54.070 1.00 17.52  ?  205  HIS B O      1 
ATOM   10371 C CB     . HIS B 2 205 ? 24.176  -36.294 -55.221 1.00 17.44  ?  205  HIS B CB     1 
ATOM   10372 C CG     . HIS B 2 205 ? 24.385  -37.130 -54.001 1.00 22.04  ?  205  HIS B CG     1 
ATOM   10373 N ND1    . HIS B 2 205 ? 24.379  -38.507 -54.036 1.00 25.49  ?  205  HIS B ND1    1 
ATOM   10374 C CD2    . HIS B 2 205 ? 24.597  -36.784 -52.708 1.00 23.97  ?  205  HIS B CD2    1 
ATOM   10375 C CE1    . HIS B 2 205 ? 24.589  -38.971 -52.819 1.00 26.19  ?  205  HIS B CE1    1 
ATOM   10376 N NE2    . HIS B 2 205 ? 24.717  -37.950 -51.994 1.00 26.22  ?  205  HIS B NE2    1 
ATOM   10377 H H      . HIS B 2 205 ? 23.346  -34.695 -56.795 1.00 23.01  ?  205  HIS B H      1 
ATOM   10378 H HA     . HIS B 2 205 ? 22.473  -37.051 -56.072 1.00 20.41  ?  205  HIS B HA     1 
ATOM   10379 H HB2    . HIS B 2 205 ? 24.700  -36.684 -55.937 1.00 20.93  ?  205  HIS B HB2    1 
ATOM   10380 H HB3    . HIS B 2 205 ? 24.497  -35.401 -55.023 1.00 20.93  ?  205  HIS B HB3    1 
ATOM   10381 H HD1    . HIS B 2 205 ? 24.257  -38.988 -54.739 1.00 30.59  ?  205  HIS B HD1    1 
ATOM   10382 H HD2    . HIS B 2 205 ? 24.651  -35.920 -52.368 1.00 28.76  ?  205  HIS B HD2    1 
ATOM   10383 H HE1    . HIS B 2 205 ? 24.639  -39.869 -52.581 1.00 31.42  ?  205  HIS B HE1    1 
ATOM   10384 N N      . CYS B 2 206 ? 21.706  -34.752 -53.987 1.00 16.72  ?  206  CYS B N      1 
ATOM   10385 C CA     . CYS B 2 206 ? 20.794  -34.462 -52.883 1.00 15.55  ?  206  CYS B CA     1 
ATOM   10386 C C      . CYS B 2 206 ? 19.352  -34.696 -53.296 1.00 16.06  ?  206  CYS B C      1 
ATOM   10387 O O      . CYS B 2 206 ? 18.568  -35.276 -52.535 1.00 16.73  ?  206  CYS B O      1 
ATOM   10388 C CB     . CYS B 2 206 ? 20.975  -33.021 -52.407 1.00 16.96  ?  206  CYS B CB     1 
ATOM   10389 S SG     . CYS B 2 206 ? 22.474  -32.706 -51.471 1.00 17.90  ?  206  CYS B SG     1 
ATOM   10390 H H      . CYS B 2 206 ? 22.170  -34.079 -54.252 1.00 20.06  ?  206  CYS B H      1 
ATOM   10391 H HA     . CYS B 2 206 ? 21.005  -35.051 -52.142 1.00 18.66  ?  206  CYS B HA     1 
ATOM   10392 H HB2    . CYS B 2 206 ? 20.993  -32.442 -53.185 1.00 20.35  ?  206  CYS B HB2    1 
ATOM   10393 H HB3    . CYS B 2 206 ? 20.224  -32.790 -51.838 1.00 20.35  ?  206  CYS B HB3    1 
ATOM   10394 H HG     . CYS B 2 206 ? 22.473  -31.564 -51.103 1.00 21.47  ?  206  CYS B HG     1 
ATOM   10395 N N      . ALA B 2 207 ? 18.994  -34.288 -54.523 1.00 15.87  ?  207  ALA B N      1 
ATOM   10396 C CA     . ALA B 2 207 ? 17.624  -34.496 -54.981 1.00 16.16  ?  207  ALA B CA     1 
ATOM   10397 C C      . ALA B 2 207 ? 17.337  -35.977 -55.164 1.00 15.70  ?  207  ALA B C      1 
ATOM   10398 O O      . ALA B 2 207 ? 16.240  -36.449 -54.832 1.00 16.34  ?  207  ALA B O      1 
ATOM   10399 C CB     . ALA B 2 207 ? 17.369  -33.728 -56.266 1.00 17.24  ?  207  ALA B CB     1 
ATOM   10400 H H      . ALA B 2 207 ? 19.511  -33.900 -55.090 1.00 19.04  ?  207  ALA B H      1 
ATOM   10401 H HA     . ALA B 2 207 ? 17.013  -34.149 -54.313 1.00 19.38  ?  207  ALA B HA     1 
ATOM   10402 H HB1    . ALA B 2 207 ? 16.456  -33.885 -56.552 1.00 20.68  ?  207  ALA B HB1    1 
ATOM   10403 H HB2    . ALA B 2 207 ? 17.506  -32.782 -56.101 1.00 20.68  ?  207  ALA B HB2    1 
ATOM   10404 H HB3    . ALA B 2 207 ? 17.987  -34.038 -56.947 1.00 20.68  ?  207  ALA B HB3    1 
ATOM   10405 N N      . ALA B 2 208 ? 18.332  -36.734 -55.643 1.00 15.78  ?  208  ALA B N      1 
ATOM   10406 C CA     . ALA B 2 208 ? 18.157  -38.178 -55.790 1.00 16.77  ?  208  ALA B CA     1 
ATOM   10407 C C      . ALA B 2 208 ? 17.976  -38.872 -54.443 1.00 17.36  ?  208  ALA B C      1 
ATOM   10408 O O      . ALA B 2 208 ? 17.165  -39.800 -54.322 1.00 17.78  ?  208  ALA B O      1 
ATOM   10409 C CB     . ALA B 2 208 ? 19.345  -38.782 -56.539 1.00 18.38  ?  208  ALA B CB     1 
ATOM   10410 H H      . ALA B 2 208 ? 19.103  -36.441 -55.886 1.00 18.94  ?  208  ALA B H      1 
ATOM   10411 H HA     . ALA B 2 208 ? 17.355  -38.330 -56.313 1.00 20.12  ?  208  ALA B HA     1 
ATOM   10412 H HB1    . ALA B 2 208 ? 19.248  -39.747 -56.560 1.00 22.05  ?  208  ALA B HB1    1 
ATOM   10413 H HB2    . ALA B 2 208 ? 19.359  -38.432 -57.444 1.00 22.05  ?  208  ALA B HB2    1 
ATOM   10414 H HB3    . ALA B 2 208 ? 20.164  -38.542 -56.079 1.00 22.05  ?  208  ALA B HB3    1 
ATOM   10415 N N      . LYS B 2 209 ? 18.750  -38.468 -53.430 1.00 17.15  ?  209  LYS B N      1 
ATOM   10416 C CA     . LYS B 2 209 ? 18.607  -39.069 -52.102 1.00 16.88  ?  209  LYS B CA     1 
ATOM   10417 C C      . LYS B 2 209 ? 17.255  -38.729 -51.479 1.00 15.40  ?  209  LYS B C      1 
ATOM   10418 O O      . LYS B 2 209 ? 16.660  -39.561 -50.772 1.00 16.28  ?  209  LYS B O      1 
ATOM   10419 C CB     . LYS B 2 209 ? 19.740  -38.603 -51.187 1.00 17.61  ?  209  LYS B CB     1 
ATOM   10420 C CG     . LYS B 2 209 ? 21.131  -39.048 -51.611 1.00 19.89  ?  209  LYS B CG     1 
ATOM   10421 C CD     . LYS B 2 209 ? 21.266  -40.569 -51.504 1.00 25.35  ?  209  LYS B CD     1 
ATOM   10422 C CE     . LYS B 2 209 ? 21.372  -41.011 -50.067 1.00 30.70  ?  209  LYS B CE     1 
ATOM   10423 N NZ     . LYS B 2 209 ? 21.521  -42.495 -49.983 1.00 34.03  ?  209  LYS B NZ     1 
ATOM   10424 H H      . LYS B 2 209 ? 19.356  -37.860 -53.482 1.00 20.58  ?  209  LYS B H      1 
ATOM   10425 H HA     . LYS B 2 209 ? 18.665  -40.033 -52.193 1.00 20.26  ?  209  LYS B HA     1 
ATOM   10426 H HB2    . LYS B 2 209 ? 19.739  -37.633 -51.167 1.00 21.13  ?  209  LYS B HB2    1 
ATOM   10427 H HB3    . LYS B 2 209 ? 19.581  -38.954 -50.297 1.00 21.13  ?  209  LYS B HB3    1 
ATOM   10428 H HG2    . LYS B 2 209 ? 21.289  -38.788 -52.532 1.00 23.87  ?  209  LYS B HG2    1 
ATOM   10429 H HG3    . LYS B 2 209 ? 21.794  -38.637 -51.033 1.00 23.87  ?  209  LYS B HG3    1 
ATOM   10430 H HD2    . LYS B 2 209 ? 20.486  -40.990 -51.896 1.00 30.42  ?  209  LYS B HD2    1 
ATOM   10431 H HD3    . LYS B 2 209 ? 22.067  -40.855 -51.970 1.00 30.42  ?  209  LYS B HD3    1 
ATOM   10432 H HE2    . LYS B 2 209 ? 22.148  -40.599 -49.656 1.00 36.84  ?  209  LYS B HE2    1 
ATOM   10433 H HE3    . LYS B 2 209 ? 20.568  -40.755 -49.589 1.00 36.84  ?  209  LYS B HE3    1 
ATOM   10434 H HZ1    . LYS B 2 209 ? 21.625  -42.743 -49.134 1.00 40.83  ?  209  LYS B HZ1    1 
ATOM   10435 H HZ2    . LYS B 2 209 ? 20.798  -42.893 -50.314 1.00 40.83  ?  209  LYS B HZ2    1 
ATOM   10436 H HZ3    . LYS B 2 209 ? 22.233  -42.756 -50.449 1.00 40.83  ?  209  LYS B HZ3    1 
ATOM   10437 N N      . LEU B 2 210 ? 16.750  -37.514 -51.727 1.00 15.00  ?  210  LEU B N      1 
ATOM   10438 C CA     . LEU B 2 210 ? 15.406  -37.168 -51.257 1.00 14.32  ?  210  LEU B CA     1 
ATOM   10439 C C      . LEU B 2 210 ? 14.354  -38.057 -51.907 1.00 13.42  ?  210  LEU B C      1 
ATOM   10440 O O      . LEU B 2 210 ? 13.458  -38.571 -51.232 1.00 13.54  ?  210  LEU B O      1 
ATOM   10441 C CB     . LEU B 2 210 ? 15.101  -35.701 -51.531 1.00 15.05  ?  210  LEU B CB     1 
ATOM   10442 C CG     . LEU B 2 210 ? 13.683  -35.240 -51.211 1.00 13.32  ?  210  LEU B CG     1 
ATOM   10443 C CD1    . LEU B 2 210 ? 13.394  -35.368 -49.727 1.00 14.96  ?  210  LEU B CD1    1 
ATOM   10444 C CD2    . LEU B 2 210 ? 13.520  -33.805 -51.674 1.00 14.20  ?  210  LEU B CD2    1 
ATOM   10445 H H      . LEU B 2 210 ? 17.154  -36.887 -52.155 1.00 18.00  ?  210  LEU B H      1 
ATOM   10446 H HA     . LEU B 2 210 ? 15.375  -37.304 -50.297 1.00 17.18  ?  210  LEU B HA     1 
ATOM   10447 H HB2    . LEU B 2 210 ? 15.706  -35.162 -50.997 1.00 18.06  ?  210  LEU B HB2    1 
ATOM   10448 H HB3    . LEU B 2 210 ? 15.252  -35.532 -52.474 1.00 18.06  ?  210  LEU B HB3    1 
ATOM   10449 H HG     . LEU B 2 210 ? 13.040  -35.799 -51.674 1.00 15.98  ?  210  LEU B HG     1 
ATOM   10450 H HD11   . LEU B 2 210 ? 12.482  -35.083 -49.557 1.00 17.95  ?  210  LEU B HD11   1 
ATOM   10451 H HD12   . LEU B 2 210 ? 13.507  -36.294 -49.462 1.00 17.95  ?  210  LEU B HD12   1 
ATOM   10452 H HD13   . LEU B 2 210 ? 14.013  -34.805 -49.235 1.00 17.95  ?  210  LEU B HD13   1 
ATOM   10453 H HD21   . LEU B 2 210 ? 12.602  -33.528 -51.527 1.00 17.04  ?  210  LEU B HD21   1 
ATOM   10454 H HD22   . LEU B 2 210 ? 14.122  -33.239 -51.166 1.00 17.04  ?  210  LEU B HD22   1 
ATOM   10455 H HD23   . LEU B 2 210 ? 13.735  -33.751 -52.619 1.00 17.04  ?  210  LEU B HD23   1 
ATOM   10456 N N      . GLU B 2 211 ? 14.428  -38.220 -53.232 1.00 14.91  ?  211  GLU B N      1 
ATOM   10457 C CA     . GLU B 2 211 ? 13.495  -39.097 -53.926 1.00 14.57  ?  211  GLU B CA     1 
ATOM   10458 C C      . GLU B 2 211 ? 13.595  -40.527 -53.402 1.00 16.27  ?  211  GLU B C      1 
ATOM   10459 O O      . GLU B 2 211 ? 12.575  -41.190 -53.172 1.00 15.79  ?  211  GLU B O      1 
ATOM   10460 C CB     . GLU B 2 211 ? 13.745  -39.055 -55.437 1.00 15.87  ?  211  GLU B CB     1 
ATOM   10461 C CG     . GLU B 2 211 ? 12.847  -40.031 -56.183 1.00 16.57  ?  211  GLU B CG     1 
ATOM   10462 C CD     . GLU B 2 211 ? 12.701  -39.710 -57.658 1.00 19.93  ?  211  GLU B CD     1 
ATOM   10463 O OE1    . GLU B 2 211 ? 11.606  -39.921 -58.211 1.00 19.65  ?  211  GLU B OE1    1 
ATOM   10464 O OE2    . GLU B 2 211 ? 13.686  -39.244 -58.272 1.00 27.45  -1 211  GLU B OE2    1 
ATOM   10465 H H      . GLU B 2 211 ? 15.003  -37.838 -53.745 1.00 17.88  ?  211  GLU B H      1 
ATOM   10466 H HA     . GLU B 2 211 ? 12.593  -38.778 -53.769 1.00 17.48  ?  211  GLU B HA     1 
ATOM   10467 H HB2    . GLU B 2 211 ? 13.563  -38.161 -55.766 1.00 19.05  ?  211  GLU B HB2    1 
ATOM   10468 H HB3    . GLU B 2 211 ? 14.668  -39.293 -55.615 1.00 19.05  ?  211  GLU B HB3    1 
ATOM   10469 H HG2    . GLU B 2 211 ? 13.223  -40.922 -56.109 1.00 19.89  ?  211  GLU B HG2    1 
ATOM   10470 H HG3    . GLU B 2 211 ? 11.963  -40.010 -55.786 1.00 19.89  ?  211  GLU B HG3    1 
ATOM   10471 N N      . GLU B 2 212 ? 14.824  -41.009 -53.193 1.00 17.29  ?  212  GLU B N      1 
ATOM   10472 C CA     . GLU B 2 212 ? 15.024  -42.341 -52.630 1.00 18.06  ?  212  GLU B CA     1 
ATOM   10473 C C      . GLU B 2 212 ? 14.348  -42.486 -51.273 1.00 18.71  ?  212  GLU B C      1 
ATOM   10474 O O      . GLU B 2 212 ? 13.702  -43.512 -50.989 1.00 17.64  ?  212  GLU B O      1 
ATOM   10475 C CB     . GLU B 2 212 ? 16.521  -42.586 -52.522 1.00 22.46  ?  212  GLU B CB     1 
ATOM   10476 C CG     . GLU B 2 212 ? 16.924  -43.849 -51.817 1.00 28.91  ?  212  GLU B CG     1 
ATOM   10477 C CD     . GLU B 2 212 ? 18.424  -43.902 -51.672 1.00 35.63  ?  212  GLU B CD     1 
ATOM   10478 O OE1    . GLU B 2 212 ? 18.917  -43.896 -50.543 1.00 39.61  ?  212  GLU B OE1    1 
ATOM   10479 O OE2    . GLU B 2 212 ? 19.102  -43.882 -52.707 1.00 39.48  -1 212  GLU B OE2    1 
ATOM   10480 H H      . GLU B 2 212 ? 15.553  -40.588 -53.367 1.00 20.75  ?  212  GLU B H      1 
ATOM   10481 H HA     . GLU B 2 212 ? 14.629  -43.009 -53.212 1.00 21.67  ?  212  GLU B HA     1 
ATOM   10482 H HB2    . GLU B 2 212 ? 16.888  -42.627 -53.419 1.00 26.95  ?  212  GLU B HB2    1 
ATOM   10483 H HB3    . GLU B 2 212 ? 16.916  -41.846 -52.035 1.00 26.95  ?  212  GLU B HB3    1 
ATOM   10484 H HG2    . GLU B 2 212 ? 16.525  -43.872 -50.933 1.00 34.69  ?  212  GLU B HG2    1 
ATOM   10485 H HG3    . GLU B 2 212 ? 16.633  -44.618 -52.332 1.00 34.69  ?  212  GLU B HG3    1 
ATOM   10486 N N      . MET B 2 213 ? 14.496  -41.483 -50.411 1.00 17.36  ?  213  MET B N      1 
ATOM   10487 C CA     . MET B 2 213 ? 13.845  -41.517 -49.105 1.00 16.51  ?  213  MET B CA     1 
ATOM   10488 C C      . MET B 2 213 ? 12.333  -41.546 -49.248 1.00 15.60  ?  213  MET B C      1 
ATOM   10489 O O      . MET B 2 213 ? 11.652  -42.313 -48.555 1.00 15.71  ?  213  MET B O      1 
ATOM   10490 C CB     . MET B 2 213 ? 14.272  -40.301 -48.280 1.00 15.69  ?  213  MET B CB     1 
ATOM   10491 C CG     . MET B 2 213 ? 13.531  -40.147 -46.954 1.00 15.63  ?  213  MET B CG     1 
ATOM   10492 S SD     . MET B 2 213 ? 14.169  -38.815 -45.925 1.00 16.75  ?  213  MET B SD     1 
ATOM   10493 C CE     . MET B 2 213 ? 15.627  -39.615 -45.267 1.00 18.70  ?  213  MET B CE     1 
ATOM   10494 H H      . MET B 2 213 ? 14.964  -40.776 -50.554 1.00 20.82  ?  213  MET B H      1 
ATOM   10495 H HA     . MET B 2 213 ? 14.134  -42.317 -48.639 1.00 19.80  ?  213  MET B HA     1 
ATOM   10496 H HB2    . MET B 2 213 ? 15.218  -40.380 -48.080 1.00 18.82  ?  213  MET B HB2    1 
ATOM   10497 H HB3    . MET B 2 213 ? 14.109  -39.500 -48.802 1.00 18.82  ?  213  MET B HB3    1 
ATOM   10498 H HG2    . MET B 2 213 ? 12.597  -39.959 -47.137 1.00 18.76  ?  213  MET B HG2    1 
ATOM   10499 H HG3    . MET B 2 213 ? 13.611  -40.974 -46.452 1.00 18.76  ?  213  MET B HG3    1 
ATOM   10500 H HE1    . MET B 2 213 ? 16.040  -39.030 -44.612 1.00 22.44  ?  213  MET B HE1    1 
ATOM   10501 H HE2    . MET B 2 213 ? 15.367  -40.450 -44.848 1.00 22.44  ?  213  MET B HE2    1 
ATOM   10502 H HE3    . MET B 2 213 ? 16.247  -39.788 -45.993 1.00 22.44  ?  213  MET B HE3    1 
ATOM   10503 N N      . ILE B 2 214 ? 11.785  -40.686 -50.115 1.00 15.49  ?  214  ILE B N      1 
ATOM   10504 C CA     . ILE B 2 214 ? 10.334  -40.604 -50.275 1.00 14.53  ?  214  ILE B CA     1 
ATOM   10505 C C      . ILE B 2 214 ? 9.787   -41.929 -50.783 1.00 14.94  ?  214  ILE B C      1 
ATOM   10506 O O      . ILE B 2 214 ? 8.765   -42.424 -50.298 1.00 16.09  ?  214  ILE B O      1 
ATOM   10507 C CB     . ILE B 2 214 ? 9.972   -39.432 -51.208 1.00 14.19  ?  214  ILE B CB     1 
ATOM   10508 C CG1    . ILE B 2 214 ? 10.273  -38.099 -50.519 1.00 13.64  ?  214  ILE B CG1    1 
ATOM   10509 C CG2    . ILE B 2 214 ? 8.504   -39.484 -51.596 1.00 15.02  ?  214  ILE B CG2    1 
ATOM   10510 C CD1    . ILE B 2 214 ? 10.183  -36.875 -51.430 1.00 14.76  ?  214  ILE B CD1    1 
ATOM   10511 H H      . ILE B 2 214 ? 12.227  -40.145 -50.617 1.00 18.58  ?  214  ILE B H      1 
ATOM   10512 H HA     . ILE B 2 214 ? 9.930   -40.431 -49.410 1.00 17.43  ?  214  ILE B HA     1 
ATOM   10513 H HB     . ILE B 2 214 ? 10.511  -39.512 -52.010 1.00 17.03  ?  214  ILE B HB     1 
ATOM   10514 H HG12   . ILE B 2 214 ? 9.637   -37.974 -49.798 1.00 16.37  ?  214  ILE B HG12   1 
ATOM   10515 H HG13   . ILE B 2 214 ? 11.175  -38.133 -50.164 1.00 16.37  ?  214  ILE B HG13   1 
ATOM   10516 H HG21   . ILE B 2 214 ? 8.268   -38.659 -52.048 1.00 18.02  ?  214  ILE B HG21   1 
ATOM   10517 H HG22   . ILE B 2 214 ? 8.361   -40.238 -52.189 1.00 18.02  ?  214  ILE B HG22   1 
ATOM   10518 H HG23   . ILE B 2 214 ? 7.968   -39.587 -50.794 1.00 18.02  ?  214  ILE B HG23   1 
ATOM   10519 H HD11   . ILE B 2 214 ? 10.574  -36.113 -50.975 1.00 17.71  ?  214  ILE B HD11   1 
ATOM   10520 H HD12   . ILE B 2 214 ? 10.669  -37.055 -52.250 1.00 17.71  ?  214  ILE B HD12   1 
ATOM   10521 H HD13   . ILE B 2 214 ? 9.250   -36.698 -51.630 1.00 17.71  ?  214  ILE B HD13   1 
ATOM   10522 N N      . LEU B 2 215 ? 10.462  -42.525 -51.764 1.00 15.32  ?  215  LEU B N      1 
ATOM   10523 C CA     . LEU B 2 215 ? 10.021  -43.815 -52.287 1.00 15.96  ?  215  LEU B CA     1 
ATOM   10524 C C      . LEU B 2 215 ? 10.131  -44.926 -51.244 1.00 16.80  ?  215  LEU B C      1 
ATOM   10525 O O      . LEU B 2 215 ? 9.251   -45.783 -51.166 1.00 18.12  ?  215  LEU B O      1 
ATOM   10526 C CB     . LEU B 2 215 ? 10.830  -44.162 -53.537 1.00 18.01  ?  215  LEU B CB     1 
ATOM   10527 C CG     . LEU B 2 215 ? 10.439  -43.329 -54.753 1.00 19.16  ?  215  LEU B CG     1 
ATOM   10528 C CD1    . LEU B 2 215 ? 11.424  -43.591 -55.877 1.00 21.52  ?  215  LEU B CD1    1 
ATOM   10529 C CD2    . LEU B 2 215 ? 9.027   -43.639 -55.203 1.00 21.54  ?  215  LEU B CD2    1 
ATOM   10530 H H      . LEU B 2 215 ? 11.168  -42.211 -52.141 1.00 18.38  ?  215  LEU B H      1 
ATOM   10531 H HA     . LEU B 2 215 ? 9.085   -43.747 -52.533 1.00 19.15  ?  215  LEU B HA     1 
ATOM   10532 H HB2    . LEU B 2 215 ? 11.770  -44.005 -53.356 1.00 21.61  ?  215  LEU B HB2    1 
ATOM   10533 H HB3    . LEU B 2 215 ? 10.685  -45.096 -53.755 1.00 21.61  ?  215  LEU B HB3    1 
ATOM   10534 H HG     . LEU B 2 215 ? 10.464  -42.388 -54.517 1.00 22.99  ?  215  LEU B HG     1 
ATOM   10535 H HD11   . LEU B 2 215 ? 11.201  -43.023 -56.631 1.00 25.83  ?  215  LEU B HD11   1 
ATOM   10536 H HD12   . LEU B 2 215 ? 12.320  -43.389 -55.565 1.00 25.83  ?  215  LEU B HD12   1 
ATOM   10537 H HD13   . LEU B 2 215 ? 11.366  -44.524 -56.136 1.00 25.83  ?  215  LEU B HD13   1 
ATOM   10538 H HD21   . LEU B 2 215 ? 8.889   -43.268 -56.089 1.00 25.85  ?  215  LEU B HD21   1 
ATOM   10539 H HD22   . LEU B 2 215 ? 8.906   -44.601 -55.224 1.00 25.85  ?  215  LEU B HD22   1 
ATOM   10540 H HD23   . LEU B 2 215 ? 8.401   -43.241 -54.577 1.00 25.85  ?  215  LEU B HD23   1 
ATOM   10541 N N      . ALA B 2 216 ? 11.209  -44.942 -50.451 1.00 15.94  ?  216  ALA B N      1 
ATOM   10542 C CA     . ALA B 2 216 ? 11.363  -45.979 -49.431 1.00 18.18  ?  216  ALA B CA     1 
ATOM   10543 C C      . ALA B 2 216 ? 10.322  -45.844 -48.327 1.00 16.43  ?  216  ALA B C      1 
ATOM   10544 O O      . ALA B 2 216 ? 9.847   -46.855 -47.786 1.00 17.98  ?  216  ALA B O      1 
ATOM   10545 C CB     . ALA B 2 216 ? 12.765  -45.894 -48.824 1.00 19.14  ?  216  ALA B CB     1 
ATOM   10546 H H      . ALA B 2 216 ? 11.854  -44.374 -50.481 1.00 19.13  ?  216  ALA B H      1 
ATOM   10547 H HA     . ALA B 2 216 ? 11.248  -46.845 -49.853 1.00 21.81  ?  216  ALA B HA     1 
ATOM   10548 H HB1    . ALA B 2 216 ? 12.861  -46.588 -48.153 1.00 22.96  ?  216  ALA B HB1    1 
ATOM   10549 H HB2    . ALA B 2 216 ? 13.421  -46.019 -49.527 1.00 22.96  ?  216  ALA B HB2    1 
ATOM   10550 H HB3    . ALA B 2 216 ? 12.880  -45.021 -48.416 1.00 22.96  ?  216  ALA B HB3    1 
ATOM   10551 N N      . GLU B 2 217 ? 9.980   -44.612 -47.958 1.00 15.84  ?  217  GLU B N      1 
ATOM   10552 C CA     . GLU B 2 217 ? 8.958   -44.393 -46.940 1.00 15.06  ?  217  GLU B CA     1 
ATOM   10553 C C      . GLU B 2 217 ? 7.556   -44.624 -47.471 1.00 15.43  ?  217  GLU B C      1 
ATOM   10554 O O      . GLU B 2 217 ? 6.651   -44.934 -46.684 1.00 16.28  ?  217  GLU B O      1 
ATOM   10555 C CB     . GLU B 2 217 ? 9.051   -42.955 -46.409 1.00 15.06  ?  217  GLU B CB     1 
ATOM   10556 C CG     . GLU B 2 217 ? 10.302  -42.665 -45.598 1.00 15.89  ?  217  GLU B CG     1 
ATOM   10557 C CD     . GLU B 2 217 ? 10.419  -43.530 -44.339 1.00 16.25  ?  217  GLU B CD     1 
ATOM   10558 O OE1    . GLU B 2 217 ? 9.382   -43.897 -43.734 1.00 17.76  ?  217  GLU B OE1    1 
ATOM   10559 O OE2    . GLU B 2 217 ? 11.553  -43.818 -43.944 1.00 20.87  -1 217  GLU B OE2    1 
ATOM   10560 H H      . GLU B 2 217 ? 10.321  -43.891 -48.279 1.00 19.01  ?  217  GLU B H      1 
ATOM   10561 H HA     . GLU B 2 217 ? 9.120   -45.012 -46.211 1.00 18.07  ?  217  GLU B HA     1 
ATOM   10562 H HB2    . GLU B 2 217 ? 9.042   -42.345 -47.163 1.00 18.07  ?  217  GLU B HB2    1 
ATOM   10563 H HB3    . GLU B 2 217 ? 8.285   -42.786 -45.837 1.00 18.07  ?  217  GLU B HB3    1 
ATOM   10564 H HG2    . GLU B 2 217 ? 11.081  -42.835 -46.151 1.00 19.06  ?  217  GLU B HG2    1 
ATOM   10565 H HG3    . GLU B 2 217 ? 10.288  -41.735 -45.321 1.00 19.06  ?  217  GLU B HG3    1 
ATOM   10566 N N      . GLY B 2 218 ? 7.366   -44.464 -48.786 1.00 16.51  ?  218  GLY B N      1 
ATOM   10567 C CA     . GLY B 2 218 ? 6.063   -44.427 -49.413 1.00 16.17  ?  218  GLY B CA     1 
ATOM   10568 C C      . GLY B 2 218 ? 5.566   -43.001 -49.540 1.00 15.53  ?  218  GLY B C      1 
ATOM   10569 O O      . GLY B 2 218 ? 5.346   -42.322 -48.532 1.00 15.00  ?  218  GLY B O      1 
ATOM   10570 H H      . GLY B 2 218 ? 8.009   -44.372 -49.349 1.00 19.81  ?  218  GLY B H      1 
ATOM   10571 H HA2    . GLY B 2 218 ? 6.115   -44.819 -50.299 1.00 19.40  ?  218  GLY B HA2    1 
ATOM   10572 H HA3    . GLY B 2 218 ? 5.429   -44.932 -48.881 1.00 19.40  ?  218  GLY B HA3    1 
ATOM   10573 N N      . PRO B 2 219 ? 5.442   -42.488 -50.774 1.00 16.82  ?  219  PRO B N      1 
ATOM   10574 C CA     . PRO B 2 219 ? 5.067   -41.070 -50.930 1.00 17.28  ?  219  PRO B CA     1 
ATOM   10575 C C      . PRO B 2 219 ? 3.758   -40.729 -50.262 1.00 16.15  ?  219  PRO B C      1 
ATOM   10576 O O      . PRO B 2 219 ? 3.599   -39.597 -49.781 1.00 15.88  ?  219  PRO B O      1 
ATOM   10577 C CB     . PRO B 2 219 ? 4.982   -40.867 -52.452 1.00 20.94  ?  219  PRO B CB     1 
ATOM   10578 C CG     . PRO B 2 219 ? 5.643   -42.012 -53.062 1.00 22.85  ?  219  PRO B CG     1 
ATOM   10579 C CD     . PRO B 2 219 ? 5.716   -43.143 -52.066 1.00 18.83  ?  219  PRO B CD     1 
ATOM   10580 H HA     . PRO B 2 219 ? 5.777   -40.510 -50.580 1.00 20.73  ?  219  PRO B HA     1 
ATOM   10581 H HB2    . PRO B 2 219 ? 4.051   -40.827 -52.721 1.00 25.12  ?  219  PRO B HB2    1 
ATOM   10582 H HB3    . PRO B 2 219 ? 5.433   -40.043 -52.694 1.00 25.12  ?  219  PRO B HB3    1 
ATOM   10583 H HG2    . PRO B 2 219 ? 5.132   -42.289 -53.839 1.00 27.42  ?  219  PRO B HG2    1 
ATOM   10584 H HG3    . PRO B 2 219 ? 6.537   -41.749 -53.329 1.00 27.42  ?  219  PRO B HG3    1 
ATOM   10585 H HD2    . PRO B 2 219 ? 5.044   -43.815 -52.260 1.00 22.59  ?  219  PRO B HD2    1 
ATOM   10586 H HD3    . PRO B 2 219 ? 6.598   -43.545 -52.068 1.00 22.59  ?  219  PRO B HD3    1 
ATOM   10587 N N      . GLU B 2 220 ? 2.824   -41.682 -50.207 1.00 16.37  ?  220  GLU B N      1 
ATOM   10588 C CA     . GLU B 2 220 ? 1.545   -41.477 -49.551 1.00 15.55  ?  220  GLU B CA     1 
ATOM   10589 C C      . GLU B 2 220 ? 1.682   -41.257 -48.051 1.00 14.31  ?  220  GLU B C      1 
ATOM   10590 O O      . GLU B 2 220 ? 0.685   -40.872 -47.405 1.00 15.42  ?  220  GLU B O      1 
ATOM   10591 C CB     . GLU B 2 220 ? 0.626   -42.658 -49.861 1.00 16.53  ?  220  GLU B CB     1 
ATOM   10592 C CG     . GLU B 2 220 ? 0.851   -43.931 -49.056 1.00 20.38  ?  220  GLU B CG     1 
ATOM   10593 C CD     . GLU B 2 220 ? 2.096   -44.740 -49.446 1.00 23.35  ?  220  GLU B CD     1 
ATOM   10594 O OE1    . GLU B 2 220 ? 2.798   -44.420 -50.442 1.00 21.85  ?  220  GLU B OE1    1 
ATOM   10595 O OE2    . GLU B 2 220 ? 2.358   -45.749 -48.724 1.00 24.17  -1 220  GLU B OE2    1 
ATOM   10596 H H      . GLU B 2 220 ? 2.913   -42.466 -50.549 1.00 19.64  ?  220  GLU B H      1 
ATOM   10597 H HA     . GLU B 2 220 ? 1.118   -40.681 -49.905 1.00 18.66  ?  220  GLU B HA     1 
ATOM   10598 H HB2    . GLU B 2 220 ? -0.288  -42.377 -49.698 1.00 19.83  ?  220  GLU B HB2    1 
ATOM   10599 H HB3    . GLU B 2 220 ? 0.741   -42.890 -50.796 1.00 19.83  ?  220  GLU B HB3    1 
ATOM   10600 H HG2    . GLU B 2 220 ? 0.943   -43.691 -48.121 1.00 24.46  ?  220  GLU B HG2    1 
ATOM   10601 H HG3    . GLU B 2 220 ? 0.081   -44.509 -49.175 1.00 24.46  ?  220  GLU B HG3    1 
ATOM   10602 N N      . THR B 2 221 ? 2.873   -41.481 -47.487 1.00 13.75  ?  221  THR B N      1 
ATOM   10603 C CA     . THR B 2 221 ? 3.105   -41.239 -46.062 1.00 13.37  ?  221  THR B CA     1 
ATOM   10604 C C      . THR B 2 221 ? 3.920   -39.981 -45.785 1.00 12.72  ?  221  THR B C      1 
ATOM   10605 O O      . THR B 2 221 ? 4.145   -39.669 -44.611 1.00 13.10  ?  221  THR B O      1 
ATOM   10606 C CB     . THR B 2 221 ? 3.832   -42.424 -45.384 1.00 15.55  ?  221  THR B CB     1 
ATOM   10607 O OG1    . THR B 2 221 ? 5.206   -42.470 -45.787 1.00 14.98  ?  221  THR B OG1    1 
ATOM   10608 C CG2    . THR B 2 221 ? 3.142   -43.755 -45.730 1.00 18.17  ?  221  THR B CG2    1 
ATOM   10609 H H      . THR B 2 221 ? 3.561   -41.775 -47.911 1.00 16.50  ?  221  THR B H      1 
ATOM   10610 H HA     . THR B 2 221 ? 2.227   -41.149 -45.658 1.00 16.04  ?  221  THR B HA     1 
ATOM   10611 H HB     . THR B 2 221 ? 3.797   -42.304 -44.422 1.00 18.65  ?  221  THR B HB     1 
ATOM   10612 H HG1    . THR B 2 221 ? 5.259   -42.624 -46.611 1.00 17.98  ?  221  THR B HG1    1 
ATOM   10613 H HG21   . THR B 2 221 ? 3.522   -44.474 -45.201 1.00 21.80  ?  221  THR B HG21   1 
ATOM   10614 H HG22   . THR B 2 221 ? 2.192   -43.696 -45.542 1.00 21.80  ?  221  THR B HG22   1 
ATOM   10615 H HG23   . THR B 2 221 ? 3.265   -43.958 -46.670 1.00 21.80  ?  221  THR B HG23   1 
ATOM   10616 N N      . VAL B 2 222 ? 4.355   -39.256 -46.816 1.00 12.91  ?  222  VAL B N      1 
ATOM   10617 C CA     . VAL B 2 222 ? 5.219   -38.089 -46.648 1.00 13.00  ?  222  VAL B CA     1 
ATOM   10618 C C      . VAL B 2 222 ? 4.420   -36.819 -46.883 1.00 12.25  ?  222  VAL B C      1 
ATOM   10619 O O      . VAL B 2 222 ? 3.941   -36.569 -47.999 1.00 13.77  ?  222  VAL B O      1 
ATOM   10620 C CB     . VAL B 2 222 ? 6.443   -38.147 -47.570 1.00 12.32  ?  222  VAL B CB     1 
ATOM   10621 C CG1    . VAL B 2 222 ? 7.326   -36.929 -47.361 1.00 15.63  ?  222  VAL B CG1    1 
ATOM   10622 C CG2    . VAL B 2 222 ? 7.227   -39.433 -47.325 1.00 13.08  ?  222  VAL B CG2    1 
ATOM   10623 H H      . VAL B 2 222 ? 4.159   -39.427 -47.636 1.00 15.49  ?  222  VAL B H      1 
ATOM   10624 H HA     . VAL B 2 222 ? 5.519   -38.071 -45.726 1.00 15.60  ?  222  VAL B HA     1 
ATOM   10625 H HB     . VAL B 2 222 ? 6.144   -38.145 -48.493 1.00 14.78  ?  222  VAL B HB     1 
ATOM   10626 H HG11   . VAL B 2 222 ? 8.194   -37.095 -47.763 1.00 18.75  ?  222  VAL B HG11   1 
ATOM   10627 H HG12   . VAL B 2 222 ? 6.909   -36.160 -47.781 1.00 18.75  ?  222  VAL B HG12   1 
ATOM   10628 H HG13   . VAL B 2 222 ? 7.427   -36.771 -46.409 1.00 18.75  ?  222  VAL B HG13   1 
ATOM   10629 H HG21   . VAL B 2 222 ? 8.029   -39.422 -47.871 1.00 15.70  ?  222  VAL B HG21   1 
ATOM   10630 H HG22   . VAL B 2 222 ? 7.467   -39.483 -46.386 1.00 15.70  ?  222  VAL B HG22   1 
ATOM   10631 H HG23   . VAL B 2 222 ? 6.673   -40.192 -47.566 1.00 15.70  ?  222  VAL B HG23   1 
ATOM   10632 N N      . ALA B 2 223 ? 4.358   -35.965 -45.852 1.00 13.11  ?  223  ALA B N      1 
ATOM   10633 C CA     . ALA B 2 223 ? 3.533   -34.763 -45.883 1.00 13.32  ?  223  ALA B CA     1 
ATOM   10634 C C      . ALA B 2 223 ? 4.295   -33.490 -46.228 1.00 11.79  ?  223  ALA B C      1 
ATOM   10635 O O      . ALA B 2 223 ? 3.745   -32.614 -46.915 1.00 12.25  ?  223  ALA B O      1 
ATOM   10636 C CB     . ALA B 2 223 ? 2.873   -34.560 -44.514 1.00 14.19  ?  223  ALA B CB     1 
ATOM   10637 H H      . ALA B 2 223 ? 4.792   -36.069 -45.117 1.00 15.73  ?  223  ALA B H      1 
ATOM   10638 H HA     . ALA B 2 223 ? 2.852   -34.889 -46.563 1.00 15.98  ?  223  ALA B HA     1 
ATOM   10639 H HB1    . ALA B 2 223 ? 2.357   -33.738 -44.531 1.00 17.03  ?  223  ALA B HB1    1 
ATOM   10640 H HB2    . ALA B 2 223 ? 2.289   -35.313 -44.330 1.00 17.03  ?  223  ALA B HB2    1 
ATOM   10641 H HB3    . ALA B 2 223 ? 3.563   -34.503 -43.836 1.00 17.03  ?  223  ALA B HB3    1 
ATOM   10642 N N      . ALA B 2 224 ? 5.516   -33.328 -45.726 1.00 11.85  ?  224  ALA B N      1 
ATOM   10643 C CA     . ALA B 2 224 ? 6.163   -32.026 -45.856 1.00 12.19  ?  224  ALA B CA     1 
ATOM   10644 C C      . ALA B 2 224 ? 7.677   -32.157 -45.787 1.00 12.11  ?  224  ALA B C      1 
ATOM   10645 O O      . ALA B 2 224 ? 8.222   -33.139 -45.266 1.00 12.36  ?  224  ALA B O      1 
ATOM   10646 C CB     . ALA B 2 224 ? 5.682   -31.029 -44.777 1.00 12.68  ?  224  ALA B CB     1 
ATOM   10647 H H      . ALA B 2 224 ? 5.973   -33.934 -45.321 1.00 14.21  ?  224  ALA B H      1 
ATOM   10648 H HA     . ALA B 2 224 ? 5.938   -31.685 -46.735 1.00 14.63  ?  224  ALA B HA     1 
ATOM   10649 H HB1    . ALA B 2 224 ? 6.044   -30.151 -44.975 1.00 15.22  ?  224  ALA B HB1    1 
ATOM   10650 H HB2    . ALA B 2 224 ? 4.713   -30.998 -44.785 1.00 15.22  ?  224  ALA B HB2    1 
ATOM   10651 H HB3    . ALA B 2 224 ? 5.996   -31.327 -43.909 1.00 15.22  ?  224  ALA B HB3    1 
ATOM   10652 N N      . PHE B 2 225 ? 8.338   -31.104 -46.280 1.00 12.15  ?  225  PHE B N      1 
ATOM   10653 C CA     . PHE B 2 225 ? 9.782   -30.915 -46.267 1.00 12.37  ?  225  PHE B CA     1 
ATOM   10654 C C      . PHE B 2 225 ? 10.039  -29.517 -45.732 1.00 12.87  ?  225  PHE B C      1 
ATOM   10655 O O      . PHE B 2 225 ? 9.397   -28.562 -46.180 1.00 14.39  ?  225  PHE B O      1 
ATOM   10656 C CB     . PHE B 2 225 ? 10.300  -31.018 -47.710 1.00 12.00  ?  225  PHE B CB     1 
ATOM   10657 C CG     . PHE B 2 225 ? 11.776  -30.747 -47.891 1.00 13.46  ?  225  PHE B CG     1 
ATOM   10658 C CD1    . PHE B 2 225 ? 12.245  -29.459 -48.043 1.00 14.74  ?  225  PHE B CD1    1 
ATOM   10659 C CD2    . PHE B 2 225 ? 12.676  -31.790 -47.982 1.00 16.20  ?  225  PHE B CD2    1 
ATOM   10660 C CE1    . PHE B 2 225 ? 13.588  -29.211 -48.265 1.00 16.32  ?  225  PHE B CE1    1 
ATOM   10661 C CE2    . PHE B 2 225 ? 14.032  -31.554 -48.213 1.00 17.75  ?  225  PHE B CE2    1 
ATOM   10662 C CZ     . PHE B 2 225 ? 14.480  -30.267 -48.351 1.00 16.26  ?  225  PHE B CZ     1 
ATOM   10663 H H      . PHE B 2 225 ? 7.936   -30.442 -46.653 1.00 14.58  ?  225  PHE B H      1 
ATOM   10664 H HA     . PHE B 2 225 ? 10.236  -31.564 -45.706 1.00 14.84  ?  225  PHE B HA     1 
ATOM   10665 H HB2    . PHE B 2 225 ? 10.130  -31.917 -48.032 1.00 14.39  ?  225  PHE B HB2    1 
ATOM   10666 H HB3    . PHE B 2 225 ? 9.819   -30.375 -48.253 1.00 14.39  ?  225  PHE B HB3    1 
ATOM   10667 H HD1    . PHE B 2 225 ? 11.649  -28.746 -47.996 1.00 17.69  ?  225  PHE B HD1    1 
ATOM   10668 H HD2    . PHE B 2 225 ? 12.373  -32.665 -47.888 1.00 19.44  ?  225  PHE B HD2    1 
ATOM   10669 H HE1    . PHE B 2 225 ? 13.892  -28.337 -48.356 1.00 19.58  ?  225  PHE B HE1    1 
ATOM   10670 H HE2    . PHE B 2 225 ? 14.627  -32.266 -48.273 1.00 21.29  ?  225  PHE B HE2    1 
ATOM   10671 H HZ     . PHE B 2 225 ? 15.383  -30.102 -48.502 1.00 19.51  ?  225  PHE B HZ     1 
ATOM   10672 N N      . ILE B 2 226 ? 10.966  -29.393 -44.784 1.00 11.97  ?  226  ILE B N      1 
ATOM   10673 C CA     . ILE B 2 226 ? 11.339  -28.100 -44.222 1.00 12.51  ?  226  ILE B CA     1 
ATOM   10674 C C      . ILE B 2 226 ? 12.816  -27.836 -44.466 1.00 12.32  ?  226  ILE B C      1 
ATOM   10675 O O      . ILE B 2 226 ? 13.657  -28.725 -44.280 1.00 13.26  ?  226  ILE B O      1 
ATOM   10676 C CB     . ILE B 2 226 ? 10.993  -27.982 -42.713 1.00 12.84  ?  226  ILE B CB     1 
ATOM   10677 C CG1    . ILE B 2 226 ? 11.293  -26.570 -42.208 1.00 14.22  ?  226  ILE B CG1    1 
ATOM   10678 C CG2    . ILE B 2 226 ? 11.735  -29.008 -41.876 1.00 13.09  ?  226  ILE B CG2    1 
ATOM   10679 C CD1    . ILE B 2 226 ? 10.773  -26.344 -40.794 1.00 16.46  ?  226  ILE B CD1    1 
ATOM   10680 H H      . ILE B 2 226 ? 11.398  -30.057 -44.448 1.00 14.36  ?  226  ILE B H      1 
ATOM   10681 H HA     . ILE B 2 226 ? 10.837  -27.417 -44.695 1.00 15.00  ?  226  ILE B HA     1 
ATOM   10682 H HB     . ILE B 2 226 ? 10.044  -28.160 -42.621 1.00 15.41  ?  226  ILE B HB     1 
ATOM   10683 H HG12   . ILE B 2 226 ? 12.253  -26.431 -42.204 1.00 17.06  ?  226  ILE B HG12   1 
ATOM   10684 H HG13   . ILE B 2 226 ? 10.868  -25.925 -42.794 1.00 17.06  ?  226  ILE B HG13   1 
ATOM   10685 H HG21   . ILE B 2 226 ? 11.372  -29.005 -40.977 1.00 15.71  ?  226  ILE B HG21   1 
ATOM   10686 H HG22   . ILE B 2 226 ? 11.621  -29.884 -42.276 1.00 15.71  ?  226  ILE B HG22   1 
ATOM   10687 H HG23   . ILE B 2 226 ? 12.677  -28.775 -41.853 1.00 15.71  ?  226  ILE B HG23   1 
ATOM   10688 H HD11   . ILE B 2 226 ? 10.865  -25.405 -40.569 1.00 19.75  ?  226  ILE B HD11   1 
ATOM   10689 H HD12   . ILE B 2 226 ? 9.838   -26.602 -40.756 1.00 19.75  ?  226  ILE B HD12   1 
ATOM   10690 H HD13   . ILE B 2 226 ? 11.291  -26.884 -40.176 1.00 19.75  ?  226  ILE B HD13   1 
ATOM   10691 N N      . GLY B 2 227 ? 13.125  -26.605 -44.872 1.00 13.01  ?  227  GLY B N      1 
ATOM   10692 C CA     . GLY B 2 227 ? 14.498  -26.181 -45.050 1.00 13.60  ?  227  GLY B CA     1 
ATOM   10693 C C      . GLY B 2 227 ? 14.693  -24.680 -44.946 1.00 12.56  ?  227  GLY B C      1 
ATOM   10694 O O      . GLY B 2 227 ? 13.849  -23.882 -45.374 1.00 13.30  ?  227  GLY B O      1 
ATOM   10695 H H      . GLY B 2 227 ? 12.547  -25.994 -45.052 1.00 15.61  ?  227  GLY B H      1 
ATOM   10696 H HA2    . GLY B 2 227 ? 15.049  -26.603 -44.373 1.00 16.32  ?  227  GLY B HA2    1 
ATOM   10697 H HA3    . GLY B 2 227 ? 14.804  -26.463 -45.926 1.00 16.32  ?  227  GLY B HA3    1 
ATOM   10698 N N      . GLU B 2 228 ? 15.800  -24.285 -44.334 1.00 13.47  ?  228  GLU B N      1 
ATOM   10699 C CA     . GLU B 2 228 ? 16.302  -22.927 -44.444 1.00 14.68  ?  228  GLU B CA     1 
ATOM   10700 C C      . GLU B 2 228 ? 16.882  -22.717 -45.842 1.00 13.29  ?  228  GLU B C      1 
ATOM   10701 O O      . GLU B 2 228 ? 17.555  -23.605 -46.369 1.00 14.02  ?  228  GLU B O      1 
ATOM   10702 C CB     . GLU B 2 228 ? 17.466  -22.772 -43.471 1.00 14.63  ?  228  GLU B CB     1 
ATOM   10703 C CG     . GLU B 2 228 ? 17.140  -22.958 -41.985 1.00 12.67  ?  228  GLU B CG     1 
ATOM   10704 C CD     . GLU B 2 228 ? 18.393  -23.309 -41.218 1.00 13.61  ?  228  GLU B CD     1 
ATOM   10705 O OE1    . GLU B 2 228 ? 19.054  -22.361 -40.705 1.00 15.63  ?  228  GLU B OE1    1 
ATOM   10706 O OE2    . GLU B 2 228 ? 18.731  -24.525 -41.135 1.00 15.15  -1 228  GLU B OE2    1 
ATOM   10707 H H      . GLU B 2 228 ? 16.289  -24.792 -43.840 1.00 16.16  ?  228  GLU B H      1 
ATOM   10708 H HA     . GLU B 2 228 ? 15.594  -22.288 -44.267 1.00 17.62  ?  228  GLU B HA     1 
ATOM   10709 H HB2    . GLU B 2 228 ? 18.140  -23.430 -43.699 1.00 17.55  ?  228  GLU B HB2    1 
ATOM   10710 H HB3    . GLU B 2 228 ? 17.827  -21.877 -43.573 1.00 17.55  ?  228  GLU B HB3    1 
ATOM   10711 H HG2    . GLU B 2 228 ? 16.776  -22.134 -41.625 1.00 15.21  ?  228  GLU B HG2    1 
ATOM   10712 H HG3    . GLU B 2 228 ? 16.499  -23.678 -41.880 1.00 15.21  ?  228  GLU B HG3    1 
ATOM   10713 N N      . PRO B 2 229 ? 16.636  -21.575 -46.474 1.00 14.25  ?  229  PRO B N      1 
ATOM   10714 C CA     . PRO B 2 229 ? 17.277  -21.337 -47.784 1.00 14.79  ?  229  PRO B CA     1 
ATOM   10715 C C      . PRO B 2 229 ? 18.783  -21.489 -47.730 1.00 13.74  ?  229  PRO B C      1 
ATOM   10716 O O      . PRO B 2 229 ? 19.376  -22.092 -48.629 1.00 14.65  ?  229  PRO B O      1 
ATOM   10717 C CB     . PRO B 2 229 ? 16.846  -19.903 -48.123 1.00 15.67  ?  229  PRO B CB     1 
ATOM   10718 C CG     . PRO B 2 229 ? 15.531  -19.752 -47.433 1.00 15.76  ?  229  PRO B CG     1 
ATOM   10719 C CD     . PRO B 2 229 ? 15.718  -20.486 -46.113 1.00 14.82  ?  229  PRO B CD     1 
ATOM   10720 H HA     . PRO B 2 229 ? 16.915  -21.937 -48.455 1.00 17.74  ?  229  PRO B HA     1 
ATOM   10721 H HB2    . PRO B 2 229 ? 17.496  -19.269 -47.783 1.00 18.81  ?  229  PRO B HB2    1 
ATOM   10722 H HB3    . PRO B 2 229 ? 16.752  -19.800 -49.083 1.00 18.81  ?  229  PRO B HB3    1 
ATOM   10723 H HG2    . PRO B 2 229 ? 15.337  -18.813 -47.286 1.00 18.91  ?  229  PRO B HG2    1 
ATOM   10724 H HG3    . PRO B 2 229 ? 14.827  -20.157 -47.963 1.00 18.91  ?  229  PRO B HG3    1 
ATOM   10725 H HD2    . PRO B 2 229 ? 16.114  -19.905 -45.445 1.00 17.78  ?  229  PRO B HD2    1 
ATOM   10726 H HD3    . PRO B 2 229 ? 14.874  -20.837 -45.789 1.00 17.78  ?  229  PRO B HD3    1 
ATOM   10727 N N      . VAL B 2 230 ? 19.399  -20.947 -46.677 1.00 14.19  ?  230  VAL B N      1 
ATOM   10728 C CA     . VAL B 2 230 ? 20.820  -21.026 -46.375 1.00 13.09  ?  230  VAL B CA     1 
ATOM   10729 C C      . VAL B 2 230 ? 20.914  -21.589 -44.964 1.00 13.80  ?  230  VAL B C      1 
ATOM   10730 O O      . VAL B 2 230 ? 20.181  -21.141 -44.081 1.00 14.93  ?  230  VAL B O      1 
ATOM   10731 C CB     . VAL B 2 230 ? 21.418  -19.604 -46.404 1.00 14.46  ?  230  VAL B CB     1 
ATOM   10732 C CG1    . VAL B 2 230 ? 22.868  -19.608 -45.944 1.00 16.22  ?  230  VAL B CG1    1 
ATOM   10733 C CG2    . VAL B 2 230 ? 21.263  -18.959 -47.789 1.00 14.74  ?  230  VAL B CG2    1 
ATOM   10734 H H      . VAL B 2 230 ? 18.975  -20.495 -46.081 1.00 17.03  ?  230  VAL B H      1 
ATOM   10735 H HA     . VAL B 2 230 ? 21.298  -21.601 -46.993 1.00 15.70  ?  230  VAL B HA     1 
ATOM   10736 H HB     . VAL B 2 230 ? 20.921  -19.054 -45.778 1.00 17.35  ?  230  VAL B HB     1 
ATOM   10737 H HG11   . VAL B 2 230 ? 23.248  -18.727 -46.091 1.00 19.46  ?  230  VAL B HG11   1 
ATOM   10738 H HG12   . VAL B 2 230 ? 22.899  -19.829 -45.000 1.00 19.46  ?  230  VAL B HG12   1 
ATOM   10739 H HG13   . VAL B 2 230 ? 23.359  -20.270 -46.456 1.00 19.46  ?  230  VAL B HG13   1 
ATOM   10740 H HG21   . VAL B 2 230 ? 21.715  -18.100 -47.790 1.00 17.68  ?  230  VAL B HG21   1 
ATOM   10741 H HG22   . VAL B 2 230 ? 21.660  -19.542 -48.455 1.00 17.68  ?  230  VAL B HG22   1 
ATOM   10742 H HG23   . VAL B 2 230 ? 20.320  -18.836 -47.977 1.00 17.68  ?  230  VAL B HG23   1 
ATOM   10743 N N      . LEU B 2 231 ? 21.787  -22.576 -44.738 1.00 14.21  ?  231  LEU B N      1 
ATOM   10744 C CA     . LEU B 2 231 ? 21.927  -23.082 -43.370 1.00 15.22  ?  231  LEU B CA     1 
ATOM   10745 C C      . LEU B 2 231 ? 22.522  -21.993 -42.485 1.00 15.18  ?  231  LEU B C      1 
ATOM   10746 O O      . LEU B 2 231 ? 23.562  -21.400 -42.826 1.00 16.44  ?  231  LEU B O      1 
ATOM   10747 C CB     . LEU B 2 231 ? 22.852  -24.287 -43.276 1.00 16.60  ?  231  LEU B CB     1 
ATOM   10748 C CG     . LEU B 2 231 ? 22.492  -25.578 -44.010 1.00 14.79  ?  231  LEU B CG     1 
ATOM   10749 C CD1    . LEU B 2 231 ? 23.530  -26.622 -43.695 1.00 13.86  ?  231  LEU B CD1    1 
ATOM   10750 C CD2    . LEU B 2 231 ? 21.116  -26.045 -43.593 1.00 15.81  ?  231  LEU B CD2    1 
ATOM   10751 H H      . LEU B 2 231 ? 22.285  -22.951 -45.330 1.00 17.05  ?  231  LEU B H      1 
ATOM   10752 H HA     . LEU B 2 231 ? 21.043  -23.351 -43.074 1.00 18.26  ?  231  LEU B HA     1 
ATOM   10753 H HB2    . LEU B 2 231 ? 23.717  -24.013 -43.619 1.00 19.91  ?  231  LEU B HB2    1 
ATOM   10754 H HB3    . LEU B 2 231 ? 22.925  -24.520 -42.337 1.00 19.91  ?  231  LEU B HB3    1 
ATOM   10755 H HG     . LEU B 2 231 ? 22.474  -25.430 -44.968 1.00 17.74  ?  231  LEU B HG     1 
ATOM   10756 H HD11   . LEU B 2 231 ? 23.318  -27.434 -44.181 1.00 16.63  ?  231  LEU B HD11   1 
ATOM   10757 H HD12   . LEU B 2 231 ? 24.401  -26.292 -43.966 1.00 16.63  ?  231  LEU B HD12   1 
ATOM   10758 H HD13   . LEU B 2 231 ? 23.524  -26.795 -42.741 1.00 16.63  ?  231  LEU B HD13   1 
ATOM   10759 H HD21   . LEU B 2 231 ? 20.960  -26.931 -43.956 1.00 18.97  ?  231  LEU B HD21   1 
ATOM   10760 H HD22   . LEU B 2 231 ? 21.072  -26.071 -42.624 1.00 18.97  ?  231  LEU B HD22   1 
ATOM   10761 H HD23   . LEU B 2 231 ? 20.454  -25.425 -43.938 1.00 18.97  ?  231  LEU B HD23   1 
ATOM   10762 N N      . GLY B 2 232 ? 21.881  -21.734 -41.350 1.00 15.40  ?  232  GLY B N      1 
ATOM   10763 C CA     . GLY B 2 232 ? 22.407  -20.805 -40.375 1.00 14.94  ?  232  GLY B CA     1 
ATOM   10764 C C      . GLY B 2 232 ? 23.263  -21.492 -39.330 1.00 14.49  ?  232  GLY B C      1 
ATOM   10765 O O      . GLY B 2 232 ? 24.457  -21.696 -39.531 1.00 15.12  ?  232  GLY B O      1 
ATOM   10766 H H      . GLY B 2 232 ? 21.131  -22.089 -41.124 1.00 18.47  ?  232  GLY B H      1 
ATOM   10767 H HA2    . GLY B 2 232 ? 22.950  -20.139 -40.826 1.00 17.93  ?  232  GLY B HA2    1 
ATOM   10768 H HA3    . GLY B 2 232 ? 21.672  -20.360 -39.925 1.00 17.93  ?  232  GLY B HA3    1 
ATOM   10769 N N      . THR B 2 233 ? 22.640  -21.900 -38.223 1.00 14.17  ?  233  THR B N      1 
ATOM   10770 C CA     . THR B 2 233 ? 23.396  -22.497 -37.129 1.00 15.27  ?  233  THR B CA     1 
ATOM   10771 C C      . THR B 2 233 ? 24.148  -23.759 -37.544 1.00 15.03  ?  233  THR B C      1 
ATOM   10772 O O      . THR B 2 233 ? 25.180  -24.092 -36.932 1.00 16.19  ?  233  THR B O      1 
ATOM   10773 C CB     . THR B 2 233 ? 22.445  -22.714 -35.966 1.00 16.65  ?  233  THR B CB     1 
ATOM   10774 O OG1    . THR B 2 233 ? 22.042  -21.419 -35.503 1.00 18.43  ?  233  THR B OG1    1 
ATOM   10775 C CG2    . THR B 2 233 ? 23.092  -23.517 -34.822 1.00 17.34  ?  233  THR B CG2    1 
ATOM   10776 H H      . THR B 2 233 ? 21.793  -21.843 -38.082 1.00 17.00  ?  233  THR B H      1 
ATOM   10777 H HA     . THR B 2 233 ? 24.095  -21.895 -36.831 1.00 18.32  ?  233  THR B HA     1 
ATOM   10778 H HB     . THR B 2 233 ? 21.679  -23.237 -36.251 1.00 19.98  ?  233  THR B HB     1 
ATOM   10779 H HG1    . THR B 2 233 ? 21.594  -21.493 -34.796 1.00 22.11  ?  233  THR B HG1    1 
ATOM   10780 H HG21   . THR B 2 233 ? 22.557  -23.437 -34.016 1.00 20.81  ?  233  THR B HG21   1 
ATOM   10781 H HG22   . THR B 2 233 ? 23.153  -24.454 -35.067 1.00 20.81  ?  233  THR B HG22   1 
ATOM   10782 H HG23   . THR B 2 233 ? 23.984  -23.180 -34.643 1.00 20.81  ?  233  THR B HG23   1 
ATOM   10783 N N      . GLY B 2 234 ? 23.679  -24.468 -38.567 1.00 15.37  ?  234  GLY B N      1 
ATOM   10784 C CA     . GLY B 2 234 ? 24.388  -25.619 -39.091 1.00 16.28  ?  234  GLY B CA     1 
ATOM   10785 C C      . GLY B 2 234 ? 25.630  -25.322 -39.907 1.00 16.91  ?  234  GLY B C      1 
ATOM   10786 O O      . GLY B 2 234 ? 26.230  -26.262 -40.439 1.00 17.07  ?  234  GLY B O      1 
ATOM   10787 H H      . GLY B 2 234 ? 22.942  -24.297 -38.977 1.00 18.44  ?  234  GLY B H      1 
ATOM   10788 H HA2    . GLY B 2 234 ? 24.657  -26.178 -38.345 1.00 19.53  ?  234  GLY B HA2    1 
ATOM   10789 H HA3    . GLY B 2 234 ? 23.781  -26.121 -39.658 1.00 19.53  ?  234  GLY B HA3    1 
ATOM   10790 N N      . GLY B 2 235 ? 26.034  -24.057 -40.031 1.00 15.73  ?  235  GLY B N      1 
ATOM   10791 C CA     . GLY B 2 235 ? 27.348  -23.748 -40.563 1.00 16.14  ?  235  GLY B CA     1 
ATOM   10792 C C      . GLY B 2 235 ? 27.476  -22.540 -41.471 1.00 14.93  ?  235  GLY B C      1 
ATOM   10793 O O      . GLY B 2 235 ? 28.563  -22.304 -41.991 1.00 16.16  ?  235  GLY B O      1 
ATOM   10794 H H      . GLY B 2 235 ? 25.565  -23.369 -39.814 1.00 18.87  ?  235  GLY B H      1 
ATOM   10795 H HA2    . GLY B 2 235 ? 27.949  -23.605 -39.815 1.00 19.36  ?  235  GLY B HA2    1 
ATOM   10796 H HA3    . GLY B 2 235 ? 27.654  -24.516 -41.071 1.00 19.36  ?  235  GLY B HA3    1 
ATOM   10797 N N      . ILE B 2 236 ? 26.397  -21.775 -41.679 1.00 15.23  ?  236  ILE B N      1 
ATOM   10798 C CA     . ILE B 2 236 ? 26.391  -20.646 -42.609 1.00 16.48  ?  236  ILE B CA     1 
ATOM   10799 C C      . ILE B 2 236 ? 26.765  -21.145 -44.001 1.00 15.48  ?  236  ILE B C      1 
ATOM   10800 O O      . ILE B 2 236 ? 27.853  -20.861 -44.522 1.00 16.40  ?  236  ILE B O      1 
ATOM   10801 C CB     . ILE B 2 236 ? 27.224  -19.455 -42.087 1.00 18.12  ?  236  ILE B CB     1 
ATOM   10802 C CG1    . ILE B 2 236 ? 26.543  -18.923 -40.809 1.00 21.94  ?  236  ILE B CG1    1 
ATOM   10803 C CG2    . ILE B 2 236 ? 27.290  -18.350 -43.120 1.00 16.06  ?  236  ILE B CG2    1 
ATOM   10804 C CD1    . ILE B 2 236 ? 27.256  -17.834 -40.068 1.00 21.32  ?  236  ILE B CD1    1 
ATOM   10805 H H      . ILE B 2 236 ? 25.642  -21.896 -41.285 1.00 18.27  ?  236  ILE B H      1 
ATOM   10806 H HA     . ILE B 2 236 ? 25.493  -20.289 -42.692 1.00 19.77  ?  236  ILE B HA     1 
ATOM   10807 H HB     . ILE B 2 236 ? 28.129  -19.752 -41.903 1.00 21.74  ?  236  ILE B HB     1 
ATOM   10808 H HG12   . ILE B 2 236 ? 25.672  -18.574 -41.056 1.00 26.32  ?  236  ILE B HG12   1 
ATOM   10809 H HG13   . ILE B 2 236 ? 26.441  -19.665 -40.192 1.00 26.32  ?  236  ILE B HG13   1 
ATOM   10810 H HG21   . ILE B 2 236 ? 27.724  -17.576 -42.727 1.00 19.27  ?  236  ILE B HG21   1 
ATOM   10811 H HG22   . ILE B 2 236 ? 27.798  -18.661 -43.885 1.00 19.27  ?  236  ILE B HG22   1 
ATOM   10812 H HG23   . ILE B 2 236 ? 26.388  -18.119 -43.393 1.00 19.27  ?  236  ILE B HG23   1 
ATOM   10813 H HD11   . ILE B 2 236 ? 26.861  -17.740 -39.187 1.00 25.58  ?  236  ILE B HD11   1 
ATOM   10814 H HD12   . ILE B 2 236 ? 28.194  -18.068 -39.988 1.00 25.58  ?  236  ILE B HD12   1 
ATOM   10815 H HD13   . ILE B 2 236 ? 27.163  -17.003 -40.562 1.00 25.58  ?  236  ILE B HD13   1 
ATOM   10816 N N      . VAL B 2 237 ? 25.835  -21.874 -44.614 1.00 15.36  ?  237  VAL B N      1 
ATOM   10817 C CA     . VAL B 2 237 ? 26.101  -22.661 -45.814 1.00 15.16  ?  237  VAL B CA     1 
ATOM   10818 C C      . VAL B 2 237 ? 25.098  -22.289 -46.896 1.00 14.99  ?  237  VAL B C      1 
ATOM   10819 O O      . VAL B 2 237 ? 23.952  -22.745 -46.871 1.00 15.00  ?  237  VAL B O      1 
ATOM   10820 C CB     . VAL B 2 237 ? 26.054  -24.178 -45.529 1.00 15.21  ?  237  VAL B CB     1 
ATOM   10821 C CG1    . VAL B 2 237 ? 26.540  -24.946 -46.724 1.00 16.02  ?  237  VAL B CG1    1 
ATOM   10822 C CG2    . VAL B 2 237 ? 26.885  -24.531 -44.287 1.00 17.75  ?  237  VAL B CG2    1 
ATOM   10823 H H      . VAL B 2 237 ? 25.020  -21.931 -44.346 1.00 18.43  ?  237  VAL B H      1 
ATOM   10824 H HA     . VAL B 2 237 ? 26.990  -22.436 -46.129 1.00 18.19  ?  237  VAL B HA     1 
ATOM   10825 H HB     . VAL B 2 237 ? 25.135  -24.431 -45.352 1.00 18.25  ?  237  VAL B HB     1 
ATOM   10826 H HG11   . VAL B 2 237 ? 26.518  -25.894 -46.520 1.00 19.22  ?  237  VAL B HG11   1 
ATOM   10827 H HG12   . VAL B 2 237 ? 25.960  -24.756 -47.478 1.00 19.22  ?  237  VAL B HG12   1 
ATOM   10828 H HG13   . VAL B 2 237 ? 27.448  -24.672 -46.927 1.00 19.22  ?  237  VAL B HG13   1 
ATOM   10829 H HG21   . VAL B 2 237 ? 26.953  -25.496 -44.216 1.00 21.29  ?  237  VAL B HG21   1 
ATOM   10830 H HG22   . VAL B 2 237 ? 27.770  -24.143 -44.377 1.00 21.29  ?  237  VAL B HG22   1 
ATOM   10831 H HG23   . VAL B 2 237 ? 26.446  -24.172 -43.500 1.00 21.29  ?  237  VAL B HG23   1 
ATOM   10832 N N      . PRO B 2 238 ? 25.489  -21.461 -47.858 1.00 15.49  ?  238  PRO B N      1 
ATOM   10833 C CA     . PRO B 2 238 ? 24.621  -21.227 -49.003 1.00 14.52  ?  238  PRO B CA     1 
ATOM   10834 C C      . PRO B 2 238 ? 24.370  -22.525 -49.736 1.00 15.85  ?  238  PRO B C      1 
ATOM   10835 O O      . PRO B 2 238 ? 25.215  -23.444 -49.728 1.00 16.35  ?  238  PRO B O      1 
ATOM   10836 C CB     . PRO B 2 238 ? 25.418  -20.228 -49.855 1.00 15.71  ?  238  PRO B CB     1 
ATOM   10837 C CG     . PRO B 2 238 ? 26.406  -19.610 -48.888 1.00 15.93  ?  238  PRO B CG     1 
ATOM   10838 C CD     . PRO B 2 238 ? 26.752  -20.708 -47.934 1.00 15.98  ?  238  PRO B CD     1 
ATOM   10839 H HA     . PRO B 2 238 ? 23.778  -20.826 -48.737 1.00 17.42  ?  238  PRO B HA     1 
ATOM   10840 H HB2    . PRO B 2 238 ? 25.876  -20.694 -50.571 1.00 18.85  ?  238  PRO B HB2    1 
ATOM   10841 H HB3    . PRO B 2 238 ? 24.824  -19.556 -50.223 1.00 18.85  ?  238  PRO B HB3    1 
ATOM   10842 H HG2    . PRO B 2 238 ? 27.193  -19.307 -49.368 1.00 19.11  ?  238  PRO B HG2    1 
ATOM   10843 H HG3    . PRO B 2 238 ? 25.993  -18.865 -48.424 1.00 19.11  ?  238  PRO B HG3    1 
ATOM   10844 H HD2    . PRO B 2 238 ? 27.468  -21.262 -48.283 1.00 19.17  ?  238  PRO B HD2    1 
ATOM   10845 H HD3    . PRO B 2 238 ? 27.000  -20.353 -47.066 1.00 19.17  ?  238  PRO B HD3    1 
ATOM   10846 N N      . PRO B 2 239 ? 23.211  -22.662 -50.374 1.00 16.02  ?  239  PRO B N      1 
ATOM   10847 C CA     . PRO B 2 239 ? 22.908  -23.907 -51.060 1.00 16.06  ?  239  PRO B CA     1 
ATOM   10848 C C      . PRO B 2 239 ? 23.818  -24.074 -52.268 1.00 16.72  ?  239  PRO B C      1 
ATOM   10849 O O      . PRO B 2 239 ? 24.199  -23.083 -52.913 1.00 17.85  ?  239  PRO B O      1 
ATOM   10850 C CB     . PRO B 2 239 ? 21.441  -23.732 -51.487 1.00 17.67  ?  239  PRO B CB     1 
ATOM   10851 C CG     . PRO B 2 239 ? 21.278  -22.277 -51.623 1.00 16.31  ?  239  PRO B CG     1 
ATOM   10852 C CD     . PRO B 2 239 ? 22.109  -21.686 -50.501 1.00 16.58  ?  239  PRO B CD     1 
ATOM   10853 H HA     . PRO B 2 239 ? 22.990  -24.669 -50.466 1.00 19.26  ?  239  PRO B HA     1 
ATOM   10854 H HB2    . PRO B 2 239 ? 21.282  -24.182 -52.331 1.00 21.20  ?  239  PRO B HB2    1 
ATOM   10855 H HB3    . PRO B 2 239 ? 20.850  -24.088 -50.804 1.00 21.20  ?  239  PRO B HB3    1 
ATOM   10856 H HG2    . PRO B 2 239 ? 21.607  -21.987 -52.488 1.00 19.57  ?  239  PRO B HG2    1 
ATOM   10857 H HG3    . PRO B 2 239 ? 20.344  -22.038 -51.525 1.00 19.57  ?  239  PRO B HG3    1 
ATOM   10858 H HD2    . PRO B 2 239 ? 22.447  -20.809 -50.743 1.00 19.89  ?  239  PRO B HD2    1 
ATOM   10859 H HD3    . PRO B 2 239 ? 21.597  -21.630 -49.680 1.00 19.89  ?  239  PRO B HD3    1 
ATOM   10860 N N      . PRO B 2 240 ? 24.159  -25.309 -52.620 1.00 16.45  ?  240  PRO B N      1 
ATOM   10861 C CA     . PRO B 2 240 ? 24.953  -25.536 -53.836 1.00 17.49  ?  240  PRO B CA     1 
ATOM   10862 C C      . PRO B 2 240 ? 24.147  -25.239 -55.100 1.00 17.98  ?  240  PRO B C      1 
ATOM   10863 O O      . PRO B 2 240 ? 22.918  -25.309 -55.127 1.00 17.92  ?  240  PRO B O      1 
ATOM   10864 C CB     . PRO B 2 240 ? 25.315  -27.024 -53.737 1.00 19.19  ?  240  PRO B CB     1 
ATOM   10865 C CG     . PRO B 2 240 ? 24.172  -27.636 -52.934 1.00 17.59  ?  240  PRO B CG     1 
ATOM   10866 C CD     . PRO B 2 240 ? 23.725  -26.565 -51.975 1.00 18.48  ?  240  PRO B CD     1 
ATOM   10867 H HA     . PRO B 2 240 ? 25.760  -24.998 -53.836 1.00 20.98  ?  240  PRO B HA     1 
ATOM   10868 H HB2    . PRO B 2 240 ? 25.367  -27.414 -54.624 1.00 23.02  ?  240  PRO B HB2    1 
ATOM   10869 H HB3    . PRO B 2 240 ? 26.162  -27.131 -53.277 1.00 23.02  ?  240  PRO B HB3    1 
ATOM   10870 H HG2    . PRO B 2 240 ? 23.450  -27.886 -53.532 1.00 21.10  ?  240  PRO B HG2    1 
ATOM   10871 H HG3    . PRO B 2 240 ? 24.491  -28.416 -52.454 1.00 21.10  ?  240  PRO B HG3    1 
ATOM   10872 H HD2    . PRO B 2 240 ? 22.761  -26.580 -51.869 1.00 22.18  ?  240  PRO B HD2    1 
ATOM   10873 H HD3    . PRO B 2 240 ? 24.156  -26.675 -51.113 1.00 22.18  ?  240  PRO B HD3    1 
ATOM   10874 N N      . GLU B 2 241 ? 24.867  -24.865 -56.151 1.00 20.19  ?  241  GLU B N      1 
ATOM   10875 C CA     . GLU B 2 241 ? 24.244  -24.484 -57.411 1.00 21.19  ?  241  GLU B CA     1 
ATOM   10876 C C      . GLU B 2 241 ? 23.276  -25.565 -57.870 1.00 18.37  ?  241  GLU B C      1 
ATOM   10877 O O      . GLU B 2 241 ? 23.620  -26.750 -57.883 1.00 18.78  ?  241  GLU B O      1 
ATOM   10878 C CB     . GLU B 2 241 ? 25.345  -24.283 -58.452 1.00 27.23  ?  241  GLU B CB     1 
ATOM   10879 C CG     . GLU B 2 241 ? 24.891  -23.694 -59.754 1.00 35.58  ?  241  GLU B CG     1 
ATOM   10880 C CD     . GLU B 2 241 ? 26.056  -23.487 -60.716 1.00 46.38  ?  241  GLU B CD     1 
ATOM   10881 O OE1    . GLU B 2 241 ? 27.224  -23.606 -60.274 1.00 49.40  ?  241  GLU B OE1    1 
ATOM   10882 O OE2    . GLU B 2 241 ? 25.806  -23.224 -61.917 1.00 51.51  -1 241  GLU B OE2    1 
ATOM   10883 H H      . GLU B 2 241 ? 25.725  -24.823 -56.161 1.00 24.22  ?  241  GLU B H      1 
ATOM   10884 H HA     . GLU B 2 241 ? 23.747  -23.658 -57.308 1.00 25.43  ?  241  GLU B HA     1 
ATOM   10885 H HB2    . GLU B 2 241 ? 26.012  -23.685 -58.080 1.00 32.67  ?  241  GLU B HB2    1 
ATOM   10886 H HB3    . GLU B 2 241 ? 25.744  -25.145 -58.647 1.00 32.67  ?  241  GLU B HB3    1 
ATOM   10887 H HG2    . GLU B 2 241 ? 24.254  -24.294 -60.172 1.00 42.69  ?  241  GLU B HG2    1 
ATOM   10888 H HG3    . GLU B 2 241 ? 24.477  -22.833 -59.588 1.00 42.69  ?  241  GLU B HG3    1 
ATOM   10889 N N      . GLY B 2 242 ? 22.050  -25.151 -58.196 1.00 20.09  ?  242  GLY B N      1 
ATOM   10890 C CA     . GLY B 2 242 ? 21.022  -26.064 -58.668 1.00 18.99  ?  242  GLY B CA     1 
ATOM   10891 C C      . GLY B 2 242 ? 20.177  -26.727 -57.609 1.00 18.07  ?  242  GLY B C      1 
ATOM   10892 O O      . GLY B 2 242 ? 19.217  -27.430 -57.960 1.00 18.33  ?  242  GLY B O      1 
ATOM   10893 H H      . GLY B 2 242 ? 21.791  -24.332 -58.150 1.00 24.11  ?  242  GLY B H      1 
ATOM   10894 H HA2    . GLY B 2 242 ? 20.422  -25.573 -59.251 1.00 22.79  ?  242  GLY B HA2    1 
ATOM   10895 H HA3    . GLY B 2 242 ? 21.451  -26.769 -59.179 1.00 22.79  ?  242  GLY B HA3    1 
ATOM   10896 N N      . TYR B 2 243 ? 20.482  -26.507 -56.328 1.00 15.95  ?  243  TYR B N      1 
ATOM   10897 C CA     . TYR B 2 243 ? 19.859  -27.272 -55.254 1.00 14.84  ?  243  TYR B CA     1 
ATOM   10898 C C      . TYR B 2 243 ? 18.353  -27.035 -55.189 1.00 14.82  ?  243  TYR B C      1 
ATOM   10899 O O      . TYR B 2 243 ? 17.549  -27.984 -55.213 1.00 15.31  ?  243  TYR B O      1 
ATOM   10900 C CB     . TYR B 2 243 ? 20.506  -26.877 -53.918 1.00 13.90  ?  243  TYR B CB     1 
ATOM   10901 C CG     . TYR B 2 243 ? 19.918  -27.610 -52.730 1.00 14.63  ?  243  TYR B CG     1 
ATOM   10902 C CD1    . TYR B 2 243 ? 20.367  -28.878 -52.395 1.00 14.85  ?  243  TYR B CD1    1 
ATOM   10903 C CD2    . TYR B 2 243 ? 18.899  -27.041 -51.967 1.00 13.58  ?  243  TYR B CD2    1 
ATOM   10904 C CE1    . TYR B 2 243 ? 19.825  -29.564 -51.305 1.00 13.64  ?  243  TYR B CE1    1 
ATOM   10905 C CE2    . TYR B 2 243 ? 18.351  -27.714 -50.889 1.00 13.27  ?  243  TYR B CE2    1 
ATOM   10906 C CZ     . TYR B 2 243 ? 18.803  -28.967 -50.570 1.00 13.56  ?  243  TYR B CZ     1 
ATOM   10907 O OH     . TYR B 2 243 ? 18.263  -29.634 -49.494 1.00 14.60  ?  243  TYR B OH     1 
ATOM   10908 H H      . TYR B 2 243 ? 21.048  -25.920 -56.055 1.00 19.14  ?  243  TYR B H      1 
ATOM   10909 H HA     . TYR B 2 243 ? 20.005  -28.216 -55.421 1.00 17.80  ?  243  TYR B HA     1 
ATOM   10910 H HB2    . TYR B 2 243 ? 21.453  -27.081 -53.955 1.00 16.67  ?  243  TYR B HB2    1 
ATOM   10911 H HB3    . TYR B 2 243 ? 20.377  -25.926 -53.776 1.00 16.67  ?  243  TYR B HB3    1 
ATOM   10912 H HD1    . TYR B 2 243 ? 21.037  -29.277 -52.902 1.00 17.82  ?  243  TYR B HD1    1 
ATOM   10913 H HD2    . TYR B 2 243 ? 18.583  -26.195 -52.187 1.00 16.29  ?  243  TYR B HD2    1 
ATOM   10914 H HE1    . TYR B 2 243 ? 20.142  -30.407 -51.073 1.00 16.36  ?  243  TYR B HE1    1 
ATOM   10915 H HE2    . TYR B 2 243 ? 17.679  -27.316 -50.383 1.00 15.92  ?  243  TYR B HE2    1 
ATOM   10916 H HH     . TYR B 2 243 ? 17.503  -29.324 -49.316 1.00 17.51  ?  243  TYR B HH     1 
ATOM   10917 N N      . TRP B 2 244 ? 17.943  -25.782 -55.056 1.00 14.19  ?  244  TRP B N      1 
ATOM   10918 C CA     . TRP B 2 244 ? 16.525  -25.523 -54.810 1.00 15.22  ?  244  TRP B CA     1 
ATOM   10919 C C      . TRP B 2 244 ? 15.672  -25.859 -56.028 1.00 15.99  ?  244  TRP B C      1 
ATOM   10920 O O      . TRP B 2 244 ? 14.504  -26.237 -55.880 1.00 16.45  ?  244  TRP B O      1 
ATOM   10921 C CB     . TRP B 2 244 ? 16.307  -24.100 -54.294 1.00 15.13  ?  244  TRP B CB     1 
ATOM   10922 C CG     . TRP B 2 244 ? 16.670  -23.996 -52.847 1.00 14.68  ?  244  TRP B CG     1 
ATOM   10923 C CD1    . TRP B 2 244 ? 17.721  -23.324 -52.313 1.00 15.93  ?  244  TRP B CD1    1 
ATOM   10924 C CD2    . TRP B 2 244 ? 15.989  -24.616 -51.753 1.00 13.30  ?  244  TRP B CD2    1 
ATOM   10925 N NE1    . TRP B 2 244 ? 17.746  -23.492 -50.953 1.00 14.95  ?  244  TRP B NE1    1 
ATOM   10926 C CE2    . TRP B 2 244 ? 16.688  -24.292 -50.588 1.00 13.97  ?  244  TRP B CE2    1 
ATOM   10927 C CE3    . TRP B 2 244 ? 14.862  -25.437 -51.657 1.00 15.25  ?  244  TRP B CE3    1 
ATOM   10928 C CZ2    . TRP B 2 244 ? 16.271  -24.730 -49.321 1.00 15.73  ?  244  TRP B CZ2    1 
ATOM   10929 C CZ3    . TRP B 2 244 ? 14.462  -25.878 -50.426 1.00 15.03  ?  244  TRP B CZ3    1 
ATOM   10930 C CH2    . TRP B 2 244 ? 15.154  -25.522 -49.272 1.00 14.27  ?  244  TRP B CH2    1 
ATOM   10931 H H      . TRP B 2 244 ? 18.442  -25.083 -55.101 1.00 17.02  ?  244  TRP B H      1 
ATOM   10932 H HA     . TRP B 2 244 ? 16.215  -26.100 -54.095 1.00 18.26  ?  244  TRP B HA     1 
ATOM   10933 H HB2    . TRP B 2 244 ? 16.864  -23.485 -54.796 1.00 18.16  ?  244  TRP B HB2    1 
ATOM   10934 H HB3    . TRP B 2 244 ? 15.373  -23.860 -54.395 1.00 18.16  ?  244  TRP B HB3    1 
ATOM   10935 H HD1    . TRP B 2 244 ? 18.334  -22.822 -52.799 1.00 19.11  ?  244  TRP B HD1    1 
ATOM   10936 H HE1    . TRP B 2 244 ? 18.327  -23.154 -50.416 1.00 17.94  ?  244  TRP B HE1    1 
ATOM   10937 H HE3    . TRP B 2 244 ? 14.390  -25.681 -52.421 1.00 18.30  ?  244  TRP B HE3    1 
ATOM   10938 H HZ2    . TRP B 2 244 ? 16.732  -24.492 -48.549 1.00 18.87  ?  244  TRP B HZ2    1 
ATOM   10939 H HZ3    . TRP B 2 244 ? 13.714  -26.426 -50.358 1.00 18.03  ?  244  TRP B HZ3    1 
ATOM   10940 H HH2    . TRP B 2 244 ? 14.851  -25.829 -48.448 1.00 17.13  ?  244  TRP B HH2    1 
ATOM   10941 N N      A GLU B 2 245 ? 16.220  -25.732 -57.237 0.50 15.99  ?  245  GLU B N      1 
ATOM   10942 N N      B GLU B 2 245 ? 16.238  -25.732 -57.222 0.50 16.13  ?  245  GLU B N      1 
ATOM   10943 C CA     A GLU B 2 245 ? 15.472  -26.135 -58.429 0.50 16.24  ?  245  GLU B CA     1 
ATOM   10944 C CA     B GLU B 2 245 ? 15.526  -26.122 -58.432 0.50 16.60  ?  245  GLU B CA     1 
ATOM   10945 C C      A GLU B 2 245 ? 15.210  -27.637 -58.408 0.50 15.78  ?  245  GLU B C      1 
ATOM   10946 C C      B GLU B 2 245 ? 15.231  -27.619 -58.419 0.50 16.13  ?  245  GLU B C      1 
ATOM   10947 O O      A GLU B 2 245 ? 14.084  -28.094 -58.633 0.50 15.76  ?  245  GLU B O      1 
ATOM   10948 O O      B GLU B 2 245 ? 14.098  -28.050 -58.660 0.50 16.72  ?  245  GLU B O      1 
ATOM   10949 C CB     A GLU B 2 245 ? 16.229  -25.716 -59.696 0.50 16.83  ?  245  GLU B CB     1 
ATOM   10950 C CB     B GLU B 2 245 ? 16.374  -25.729 -59.645 0.50 17.65  ?  245  GLU B CB     1 
ATOM   10951 C CG     A GLU B 2 245 ? 15.596  -26.145 -61.030 0.50 19.18  ?  245  GLU B CG     1 
ATOM   10952 C CG     B GLU B 2 245 ? 16.558  -24.223 -59.870 0.50 19.06  ?  245  GLU B CG     1 
ATOM   10953 C CD     A GLU B 2 245 ? 16.482  -25.808 -62.235 0.50 21.73  ?  245  GLU B CD     1 
ATOM   10954 C CD     B GLU B 2 245 ? 17.510  -23.495 -58.895 0.50 18.20  ?  245  GLU B CD     1 
ATOM   10955 O OE1    A GLU B 2 245 ? 17.716  -26.020 -62.134 0.50 25.95  ?  245  GLU B OE1    1 
ATOM   10956 O OE1    B GLU B 2 245 ? 18.367  -24.110 -58.216 0.50 14.33  ?  245  GLU B OE1    1 
ATOM   10957 O OE2    A GLU B 2 245 ? 15.963  -25.332 -63.267 0.50 21.30  -1 245  GLU B OE2    1 
ATOM   10958 O OE2    B GLU B 2 245 ? 17.393  -22.247 -58.828 0.50 20.76  -1 245  GLU B OE2    1 
ATOM   10959 H H      A GLU B 2 245 ? 17.006  -25.422 -57.394 0.50 19.18  ?  245  GLU B H      1 
ATOM   10960 H H      B GLU B 2 245 ? 17.029  -25.424 -57.361 0.50 19.35  ?  245  GLU B H      1 
ATOM   10961 H HA     A GLU B 2 245 ? 14.615  -25.680 -58.442 0.50 19.48  ?  245  GLU B HA     1 
ATOM   10962 H HA     B GLU B 2 245 ? 14.676  -25.659 -58.490 0.50 19.92  ?  245  GLU B HA     1 
ATOM   10963 H HB2    A GLU B 2 245 ? 16.291  -24.748 -59.706 0.50 20.20  ?  245  GLU B HB2    1 
ATOM   10964 H HB2    B GLU B 2 245 ? 17.257  -26.113 -59.535 0.50 21.18  ?  245  GLU B HB2    1 
ATOM   10965 H HB3    A GLU B 2 245 ? 17.117  -26.104 -59.662 0.50 20.20  ?  245  GLU B HB3    1 
ATOM   10966 H HB3    B GLU B 2 245 ? 15.951  -26.089 -60.440 0.50 21.18  ?  245  GLU B HB3    1 
ATOM   10967 H HG2    A GLU B 2 245 ? 15.454  -27.105 -61.019 0.50 23.01  ?  245  GLU B HG2    1 
ATOM   10968 H HG2    B GLU B 2 245 ? 16.911  -24.092 -60.764 0.50 22.87  ?  245  GLU B HG2    1 
ATOM   10969 H HG3    A GLU B 2 245 ? 14.748  -25.686 -61.141 0.50 23.01  ?  245  GLU B HG3    1 
ATOM   10970 H HG3    B GLU B 2 245 ? 15.690  -23.797 -59.791 0.50 22.87  ?  245  GLU B HG3    1 
ATOM   10971 N N      . ALA B 2 246 ? 16.240  -28.427 -58.110 1.00 14.49  ?  246  ALA B N      1 
ATOM   10972 C CA     . ALA B 2 246 ? 16.072  -29.878 -58.135 1.00 15.27  ?  246  ALA B CA     1 
ATOM   10973 C C      . ALA B 2 246 ? 15.175  -30.365 -57.009 1.00 16.41  ?  246  ALA B C      1 
ATOM   10974 O O      . ALA B 2 246 ? 14.342  -31.254 -57.220 1.00 16.46  ?  246  ALA B O      1 
ATOM   10975 C CB     . ALA B 2 246 ? 17.447  -30.541 -58.050 1.00 17.44  ?  246  ALA B CB     1 
ATOM   10976 H H      . ALA B 2 246 ? 17.027  -28.158 -57.894 1.00 17.39  ?  246  ALA B H      1 
ATOM   10977 H HA     . ALA B 2 246 ? 15.651  -30.133 -58.971 1.00 18.32  ?  246  ALA B HA     1 
ATOM   10978 H HB1    . ALA B 2 246 ? 17.337  -31.504 -58.100 1.00 20.93  ?  246  ALA B HB1    1 
ATOM   10979 H HB2    . ALA B 2 246 ? 17.993  -30.232 -58.790 1.00 20.93  ?  246  ALA B HB2    1 
ATOM   10980 H HB3    . ALA B 2 246 ? 17.863  -30.299 -57.208 1.00 20.93  ?  246  ALA B HB3    1 
ATOM   10981 N N      . ILE B 2 247 ? 15.346  -29.821 -55.803 1.00 14.85  ?  247  ILE B N      1 
ATOM   10982 C CA     . ILE B 2 247 ? 14.533  -30.258 -54.664 1.00 14.69  ?  247  ILE B CA     1 
ATOM   10983 C C      . ILE B 2 247 ? 13.064  -29.949 -54.911 1.00 14.17  ?  247  ILE B C      1 
ATOM   10984 O O      . ILE B 2 247 ? 12.176  -30.776 -54.641 1.00 14.28  ?  247  ILE B O      1 
ATOM   10985 C CB     . ILE B 2 247 ? 15.049  -29.584 -53.370 1.00 15.33  ?  247  ILE B CB     1 
ATOM   10986 C CG1    . ILE B 2 247 ? 16.455  -30.092 -53.008 1.00 16.86  ?  247  ILE B CG1    1 
ATOM   10987 C CG2    . ILE B 2 247 ? 14.054  -29.764 -52.225 1.00 16.14  ?  247  ILE B CG2    1 
ATOM   10988 C CD1    . ILE B 2 247 ? 16.538  -31.516 -52.512 1.00 18.33  ?  247  ILE B CD1    1 
ATOM   10989 H H      . ILE B 2 247 ? 15.918  -29.206 -55.615 1.00 17.82  ?  247  ILE B H      1 
ATOM   10990 H HA     . ILE B 2 247 ? 14.617  -31.219 -54.564 1.00 17.63  ?  247  ILE B HA     1 
ATOM   10991 H HB     . ILE B 2 247 ? 15.126  -28.631 -53.534 1.00 18.39  ?  247  ILE B HB     1 
ATOM   10992 H HG12   . ILE B 2 247 ? 17.012  -30.031 -53.800 1.00 20.23  ?  247  ILE B HG12   1 
ATOM   10993 H HG13   . ILE B 2 247 ? 16.811  -29.523 -52.307 1.00 20.23  ?  247  ILE B HG13   1 
ATOM   10994 H HG21   . ILE B 2 247 ? 14.489  -29.535 -51.390 1.00 19.37  ?  247  ILE B HG21   1 
ATOM   10995 H HG22   . ILE B 2 247 ? 13.294  -29.180 -52.373 1.00 19.37  ?  247  ILE B HG22   1 
ATOM   10996 H HG23   . ILE B 2 247 ? 13.762  -30.688 -52.204 1.00 19.37  ?  247  ILE B HG23   1 
ATOM   10997 H HD11   . ILE B 2 247 ? 17.471  -31.775 -52.450 1.00 21.99  ?  247  ILE B HD11   1 
ATOM   10998 H HD12   . ILE B 2 247 ? 16.121  -31.571 -51.637 1.00 21.99  ?  247  ILE B HD12   1 
ATOM   10999 H HD13   . ILE B 2 247 ? 16.074  -32.096 -53.136 1.00 21.99  ?  247  ILE B HD13   1 
ATOM   11000 N N      . GLN B 2 248 ? 12.771  -28.752 -55.419 1.00 13.84  ?  248  GLN B N      1 
ATOM   11001 C CA     . GLN B 2 248 ? 11.363  -28.397 -55.623 1.00 13.87  ?  248  GLN B CA     1 
ATOM   11002 C C      . GLN B 2 248 ? 10.685  -29.288 -56.664 1.00 14.59  ?  248  GLN B C      1 
ATOM   11003 O O      . GLN B 2 248 ? 9.497   -29.570 -56.552 1.00 16.27  ?  248  GLN B O      1 
ATOM   11004 C CB     . GLN B 2 248 ? 11.266  -26.915 -55.962 1.00 16.52  ?  248  GLN B CB     1 
ATOM   11005 C CG     . GLN B 2 248 ? 11.555  -26.024 -54.758 1.00 15.55  ?  248  GLN B CG     1 
ATOM   11006 C CD     . GLN B 2 248 ? 11.408  -24.560 -55.057 1.00 15.88  ?  248  GLN B CD     1 
ATOM   11007 O OE1    . GLN B 2 248 ? 10.412  -23.935 -54.692 1.00 16.48  ?  248  GLN B OE1    1 
ATOM   11008 N NE2    . GLN B 2 248 ? 12.411  -23.999 -55.713 1.00 17.01  ?  248  GLN B NE2    1 
ATOM   11009 H H      . GLN B 2 248 ? 13.340  -28.149 -55.646 1.00 16.61  ?  248  GLN B H      1 
ATOM   11010 H HA     . GLN B 2 248 ? 10.865  -28.536 -54.803 1.00 16.64  ?  248  GLN B HA     1 
ATOM   11011 H HB2    . GLN B 2 248 ? 11.912  -26.705 -56.655 1.00 19.82  ?  248  GLN B HB2    1 
ATOM   11012 H HB3    . GLN B 2 248 ? 10.369  -26.719 -56.274 1.00 19.82  ?  248  GLN B HB3    1 
ATOM   11013 H HG2    . GLN B 2 248 ? 10.936  -26.247 -54.046 1.00 18.66  ?  248  GLN B HG2    1 
ATOM   11014 H HG3    . GLN B 2 248 ? 12.467  -26.178 -54.465 1.00 18.66  ?  248  GLN B HG3    1 
ATOM   11015 H HE21   . GLN B 2 248 ? 13.093  -24.470 -55.941 1.00 20.41  ?  248  GLN B HE21   1 
ATOM   11016 H HE22   . GLN B 2 248 ? 12.381  -23.163 -55.912 1.00 20.41  ?  248  GLN B HE22   1 
ATOM   11017 N N      . GLY B 2 249 ? 11.412  -29.757 -57.668 1.00 15.08  ?  249  GLY B N      1 
ATOM   11018 C CA     . GLY B 2 249 ? 10.822  -30.691 -58.616 1.00 15.05  ?  249  GLY B CA     1 
ATOM   11019 C C      . GLY B 2 249 ? 10.440  -32.007 -57.962 1.00 14.19  ?  249  GLY B C      1 
ATOM   11020 O O      . GLY B 2 249 ? 9.375   -32.566 -58.245 1.00 14.81  ?  249  GLY B O      1 
ATOM   11021 H H      . GLY B 2 249 ? 12.234  -29.557 -57.824 1.00 18.09  ?  249  GLY B H      1 
ATOM   11022 H HA2    . GLY B 2 249 ? 10.024  -30.296 -59.001 1.00 18.06  ?  249  GLY B HA2    1 
ATOM   11023 H HA3    . GLY B 2 249 ? 11.457  -30.874 -59.325 1.00 18.06  ?  249  GLY B HA3    1 
ATOM   11024 N N      . VAL B 2 250 ? 11.297  -32.513 -57.073 1.00 13.93  ?  250  VAL B N      1 
ATOM   11025 C CA     . VAL B 2 250 ? 10.991  -33.755 -56.369 1.00 13.92  ?  250  VAL B CA     1 
ATOM   11026 C C      . VAL B 2 250 ? 9.782   -33.578 -55.463 1.00 13.37  ?  250  VAL B C      1 
ATOM   11027 O O      . VAL B 2 250 ? 8.919   -34.461 -55.385 1.00 13.97  ?  250  VAL B O      1 
ATOM   11028 C CB     . VAL B 2 250 ? 12.220  -34.245 -55.589 1.00 15.22  ?  250  VAL B CB     1 
ATOM   11029 C CG1    . VAL B 2 250 ? 11.880  -35.450 -54.714 1.00 15.50  ?  250  VAL B CG1    1 
ATOM   11030 C CG2    . VAL B 2 250 ? 13.352  -34.606 -56.555 1.00 16.14  ?  250  VAL B CG2    1 
ATOM   11031 H H      . VAL B 2 250 ? 12.053  -32.162 -56.861 1.00 16.72  ?  250  VAL B H      1 
ATOM   11032 H HA     . VAL B 2 250 ? 10.766  -34.431 -57.028 1.00 16.71  ?  250  VAL B HA     1 
ATOM   11033 H HB     . VAL B 2 250 ? 12.516  -33.526 -55.009 1.00 18.26  ?  250  VAL B HB     1 
ATOM   11034 H HG11   . VAL B 2 250 ? 12.703  -35.850 -54.393 1.00 18.60  ?  250  VAL B HG11   1 
ATOM   11035 H HG12   . VAL B 2 250 ? 11.341  -35.154 -53.964 1.00 18.60  ?  250  VAL B HG12   1 
ATOM   11036 H HG13   . VAL B 2 250 ? 11.383  -36.095 -55.243 1.00 18.60  ?  250  VAL B HG13   1 
ATOM   11037 H HG21   . VAL B 2 250 ? 14.099  -34.960 -56.047 1.00 19.36  ?  250  VAL B HG21   1 
ATOM   11038 H HG22   . VAL B 2 250 ? 13.032  -35.273 -57.181 1.00 19.36  ?  250  VAL B HG22   1 
ATOM   11039 H HG23   . VAL B 2 250 ? 13.626  -33.808 -57.033 1.00 19.36  ?  250  VAL B HG23   1 
ATOM   11040 N N      . LEU B 2 251 ? 9.694   -32.444 -54.763 1.00 13.93  ?  251  LEU B N      1 
ATOM   11041 C CA     . LEU B 2 251 ? 8.567   -32.239 -53.865 1.00 13.19  ?  251  LEU B CA     1 
ATOM   11042 C C      . LEU B 2 251 ? 7.256   -32.139 -54.634 1.00 13.75  ?  251  LEU B C      1 
ATOM   11043 O O      . LEU B 2 251 ? 6.228   -32.656 -54.195 1.00 14.85  ?  251  LEU B O      1 
ATOM   11044 C CB     . LEU B 2 251 ? 8.785   -30.992 -53.011 1.00 12.90  ?  251  LEU B CB     1 
ATOM   11045 C CG     . LEU B 2 251 ? 10.009  -30.979 -52.121 1.00 13.02  ?  251  LEU B CG     1 
ATOM   11046 C CD1    . LEU B 2 251 ? 10.117  -29.633 -51.401 1.00 15.72  ?  251  LEU B CD1    1 
ATOM   11047 C CD2    . LEU B 2 251 ? 9.979   -32.105 -51.106 1.00 14.45  ?  251  LEU B CD2    1 
ATOM   11048 H H      . LEU B 2 251 ? 10.259  -31.796 -54.790 1.00 16.71  ?  251  LEU B H      1 
ATOM   11049 H HA     . LEU B 2 251 ? 8.509   -33.001 -53.267 1.00 15.82  ?  251  LEU B HA     1 
ATOM   11050 H HB2    . LEU B 2 251 ? 8.860   -30.230 -53.608 1.00 15.47  ?  251  LEU B HB2    1 
ATOM   11051 H HB3    . LEU B 2 251 ? 8.013   -30.886 -52.434 1.00 15.47  ?  251  LEU B HB3    1 
ATOM   11052 H HG     . LEU B 2 251 ? 10.792  -31.111 -52.679 1.00 15.62  ?  251  LEU B HG     1 
ATOM   11053 H HD11   . LEU B 2 251 ? 10.905  -29.640 -50.835 1.00 18.86  ?  251  LEU B HD11   1 
ATOM   11054 H HD12   . LEU B 2 251 ? 10.192  -28.927 -52.062 1.00 18.86  ?  251  LEU B HD12   1 
ATOM   11055 H HD13   . LEU B 2 251 ? 9.323   -29.499 -50.862 1.00 18.86  ?  251  LEU B HD13   1 
ATOM   11056 H HD21   . LEU B 2 251 ? 10.710  -31.986 -50.480 1.00 17.33  ?  251  LEU B HD21   1 
ATOM   11057 H HD22   . LEU B 2 251 ? 9.132   -32.082 -50.634 1.00 17.33  ?  251  LEU B HD22   1 
ATOM   11058 H HD23   . LEU B 2 251 ? 10.076  -32.952 -51.570 1.00 17.33  ?  251  LEU B HD23   1 
ATOM   11059 N N      . ALA B 2 252 ? 7.260   -31.454 -55.771 1.00 13.84  ?  252  ALA B N      1 
ATOM   11060 C CA     . ALA B 2 252 ? 6.048   -31.396 -56.577 1.00 13.24  ?  252  ALA B CA     1 
ATOM   11061 C C      . ALA B 2 252 ? 5.691   -32.774 -57.120 1.00 14.45  ?  252  ALA B C      1 
ATOM   11062 O O      . ALA B 2 252 ? 4.514   -33.152 -57.164 1.00 15.33  ?  252  ALA B O      1 
ATOM   11063 C CB     . ALA B 2 252 ? 6.211   -30.410 -57.726 1.00 13.52  ?  252  ALA B CB     1 
ATOM   11064 H H      . ALA B 2 252 ? 7.931   -31.023 -56.092 1.00 16.60  ?  252  ALA B H      1 
ATOM   11065 H HA     . ALA B 2 252 ? 5.323   -31.082 -56.015 1.00 15.89  ?  252  ALA B HA     1 
ATOM   11066 H HB1    . ALA B 2 252 ? 5.414   -30.435 -58.279 1.00 16.22  ?  252  ALA B HB1    1 
ATOM   11067 H HB2    . ALA B 2 252 ? 6.333   -29.519 -57.363 1.00 16.22  ?  252  ALA B HB2    1 
ATOM   11068 H HB3    . ALA B 2 252 ? 6.986   -30.662 -58.252 1.00 16.22  ?  252  ALA B HB3    1 
ATOM   11069 N N      . LYS B 2 253 ? 6.694   -33.533 -57.537 1.00 13.99  ?  253  LYS B N      1 
ATOM   11070 C CA     . LYS B 2 253 ? 6.446   -34.857 -58.094 1.00 13.69  ?  253  LYS B CA     1 
ATOM   11071 C C      . LYS B 2 253 ? 5.672   -35.741 -57.118 1.00 12.30  ?  253  LYS B C      1 
ATOM   11072 O O      . LYS B 2 253 ? 4.825   -36.536 -57.534 1.00 13.78  ?  253  LYS B O      1 
ATOM   11073 C CB     . LYS B 2 253 ? 7.787   -35.498 -58.451 1.00 13.28  ?  253  LYS B CB     1 
ATOM   11074 C CG     . LYS B 2 253 ? 7.728   -36.873 -59.098 1.00 13.83  ?  253  LYS B CG     1 
ATOM   11075 C CD     . LYS B 2 253 ? 9.119   -37.355 -59.440 1.00 14.57  ?  253  LYS B CD     1 
ATOM   11076 C CE     . LYS B 2 253 ? 9.097   -38.662 -60.211 1.00 16.81  ?  253  LYS B CE     1 
ATOM   11077 N NZ     . LYS B 2 253 ? 10.467  -39.106 -60.591 1.00 20.61  ?  253  LYS B NZ     1 
ATOM   11078 H H      . LYS B 2 253 ? 7.524   -33.311 -57.511 1.00 16.78  ?  253  LYS B H      1 
ATOM   11079 H HA     . LYS B 2 253 ? 5.909   -34.775 -58.898 1.00 16.43  ?  253  LYS B HA     1 
ATOM   11080 H HB2    . LYS B 2 253 ? 8.247   -34.911 -59.072 1.00 15.93  ?  253  LYS B HB2    1 
ATOM   11081 H HB3    . LYS B 2 253 ? 8.305   -35.589 -57.636 1.00 15.93  ?  253  LYS B HB3    1 
ATOM   11082 H HG2    . LYS B 2 253 ? 7.325   -37.505 -58.482 1.00 16.59  ?  253  LYS B HG2    1 
ATOM   11083 H HG3    . LYS B 2 253 ? 7.207   -36.827 -59.914 1.00 16.59  ?  253  LYS B HG3    1 
ATOM   11084 H HD2    . LYS B 2 253 ? 9.562   -36.689 -59.989 1.00 17.49  ?  253  LYS B HD2    1 
ATOM   11085 H HD3    . LYS B 2 253 ? 9.619   -37.496 -58.621 1.00 17.49  ?  253  LYS B HD3    1 
ATOM   11086 H HE2    . LYS B 2 253 ? 8.696   -39.352 -59.659 1.00 20.17  ?  253  LYS B HE2    1 
ATOM   11087 H HE3    . LYS B 2 253 ? 8.579   -38.545 -61.023 1.00 20.17  ?  253  LYS B HE3    1 
ATOM   11088 H HZ1    . LYS B 2 253 ? 10.427  -39.886 -61.018 1.00 24.73  ?  253  LYS B HZ1    1 
ATOM   11089 H HZ2    . LYS B 2 253 ? 10.845  -38.503 -61.125 1.00 24.73  ?  253  LYS B HZ2    1 
ATOM   11090 H HZ3    . LYS B 2 253 ? 10.969  -39.202 -59.862 1.00 24.73  ?  253  LYS B HZ3    1 
ATOM   11091 N N      . TYR B 2 254 ? 5.962   -35.626 -55.812 1.00 13.51  ?  254  TYR B N      1 
ATOM   11092 C CA     . TYR B 2 254 ? 5.373   -36.498 -54.802 1.00 12.94  ?  254  TYR B CA     1 
ATOM   11093 C C      . TYR B 2 254 ? 4.338   -35.801 -53.926 1.00 13.48  ?  254  TYR B C      1 
ATOM   11094 O O      . TYR B 2 254 ? 3.932   -36.364 -52.907 1.00 14.35  ?  254  TYR B O      1 
ATOM   11095 C CB     . TYR B 2 254 ? 6.482   -37.157 -53.980 1.00 13.91  ?  254  TYR B CB     1 
ATOM   11096 C CG     . TYR B 2 254 ? 7.313   -38.106 -54.823 1.00 14.58  ?  254  TYR B CG     1 
ATOM   11097 C CD1    . TYR B 2 254 ? 6.774   -39.303 -55.265 1.00 16.19  ?  254  TYR B CD1    1 
ATOM   11098 C CD2    . TYR B 2 254 ? 8.599   -37.792 -55.201 1.00 13.75  ?  254  TYR B CD2    1 
ATOM   11099 C CE1    . TYR B 2 254 ? 7.493   -40.163 -56.055 1.00 13.48  ?  254  TYR B CE1    1 
ATOM   11100 C CE2    . TYR B 2 254 ? 9.346   -38.655 -55.984 1.00 15.21  ?  254  TYR B CE2    1 
ATOM   11101 C CZ     . TYR B 2 254 ? 8.775   -39.834 -56.416 1.00 14.05  ?  254  TYR B CZ     1 
ATOM   11102 O OH     . TYR B 2 254 ? 9.470   -40.721 -57.209 1.00 17.75  ?  254  TYR B OH     1 
ATOM   11103 H H      . TYR B 2 254 ? 6.504   -35.041 -55.491 1.00 16.21  ?  254  TYR B H      1 
ATOM   11104 H HA     . TYR B 2 254 ? 4.889   -37.212 -55.245 1.00 15.53  ?  254  TYR B HA     1 
ATOM   11105 H HB2    . TYR B 2 254 ? 7.069   -36.471 -53.625 1.00 16.69  ?  254  TYR B HB2    1 
ATOM   11106 H HB3    . TYR B 2 254 ? 6.085   -37.663 -53.254 1.00 16.69  ?  254  TYR B HB3    1 
ATOM   11107 H HD1    . TYR B 2 254 ? 5.906   -39.528 -55.022 1.00 19.42  ?  254  TYR B HD1    1 
ATOM   11108 H HD2    . TYR B 2 254 ? 8.972   -36.986 -54.926 1.00 16.50  ?  254  TYR B HD2    1 
ATOM   11109 H HE1    . TYR B 2 254 ? 7.115   -40.963 -56.343 1.00 16.18  ?  254  TYR B HE1    1 
ATOM   11110 H HE2    . TYR B 2 254 ? 10.222  -38.443 -56.216 1.00 18.25  ?  254  TYR B HE2    1 
ATOM   11111 H HH     . TYR B 2 254 ? 10.229  -40.410 -57.391 1.00 21.30  ?  254  TYR B HH     1 
ATOM   11112 N N      . ASP B 2 255 ? 3.922   -34.582 -54.282 1.00 13.06  ?  255  ASP B N      1 
ATOM   11113 C CA     . ASP B 2 255 ? 2.865   -33.875 -53.559 1.00 13.57  ?  255  ASP B CA     1 
ATOM   11114 C C      . ASP B 2 255 ? 3.245   -33.704 -52.093 1.00 12.73  ?  255  ASP B C      1 
ATOM   11115 O O      . ASP B 2 255 ? 2.482   -34.053 -51.187 1.00 14.78  ?  255  ASP B O      1 
ATOM   11116 C CB     . ASP B 2 255 ? 1.534   -34.611 -53.715 1.00 14.70  ?  255  ASP B CB     1 
ATOM   11117 C CG     . ASP B 2 255 ? 0.356   -33.870 -53.142 1.00 15.41  ?  255  ASP B CG     1 
ATOM   11118 O OD1    . ASP B 2 255 ? 0.392   -32.620 -53.024 1.00 17.50  ?  255  ASP B OD1    1 
ATOM   11119 O OD2    . ASP B 2 255 ? -0.644  -34.563 -52.812 1.00 16.27  -1 255  ASP B OD2    1 
ATOM   11120 H H      . ASP B 2 255 ? 4.243   -34.141 -54.947 1.00 15.67  ?  255  ASP B H      1 
ATOM   11121 H HA     . ASP B 2 255 ? 2.757   -32.986 -53.933 1.00 16.27  ?  255  ASP B HA     1 
ATOM   11122 H HB2    . ASP B 2 255 ? 1.364   -34.752 -54.659 1.00 17.63  ?  255  ASP B HB2    1 
ATOM   11123 H HB3    . ASP B 2 255 ? 1.596   -35.465 -53.258 1.00 17.63  ?  255  ASP B HB3    1 
ATOM   11124 N N      . VAL B 2 256 ? 4.427   -33.132 -51.870 1.00 12.19  ?  256  VAL B N      1 
ATOM   11125 C CA     . VAL B 2 256 ? 4.959   -32.847 -50.536 1.00 11.61  ?  256  VAL B CA     1 
ATOM   11126 C C      . VAL B 2 256 ? 4.994   -31.334 -50.333 1.00 13.16  ?  256  VAL B C      1 
ATOM   11127 O O      . VAL B 2 256 ? 5.522   -30.602 -51.177 1.00 15.23  ?  256  VAL B O      1 
ATOM   11128 C CB     . VAL B 2 256 ? 6.368   -33.454 -50.395 1.00 13.28  ?  256  VAL B CB     1 
ATOM   11129 C CG1    . VAL B 2 256 ? 6.959   -33.120 -49.042 1.00 13.42  ?  256  VAL B CG1    1 
ATOM   11130 C CG2    . VAL B 2 256 ? 6.315   -34.970 -50.585 1.00 15.94  ?  256  VAL B CG2    1 
ATOM   11131 H H      . VAL B 2 256 ? 4.959   -32.892 -52.501 1.00 14.63  ?  256  VAL B H      1 
ATOM   11132 H HA     . VAL B 2 256 ? 4.374   -33.219 -49.857 1.00 13.93  ?  256  VAL B HA     1 
ATOM   11133 H HB     . VAL B 2 256 ? 6.939   -33.074 -51.081 1.00 15.93  ?  256  VAL B HB     1 
ATOM   11134 H HG11   . VAL B 2 256 ? 7.767   -33.642 -48.913 1.00 16.10  ?  256  VAL B HG11   1 
ATOM   11135 H HG12   . VAL B 2 256 ? 7.170   -32.173 -49.014 1.00 16.10  ?  256  VAL B HG12   1 
ATOM   11136 H HG13   . VAL B 2 256 ? 6.312   -33.336 -48.352 1.00 16.10  ?  256  VAL B HG13   1 
ATOM   11137 H HG21   . VAL B 2 256 ? 7.213   -35.329 -50.509 1.00 19.12  ?  256  VAL B HG21   1 
ATOM   11138 H HG22   . VAL B 2 256 ? 5.746   -35.354 -49.900 1.00 19.12  ?  256  VAL B HG22   1 
ATOM   11139 H HG23   . VAL B 2 256 ? 5.954   -35.166 -51.464 1.00 19.12  ?  256  VAL B HG23   1 
ATOM   11140 N N      . LEU B 2 257 ? 4.427   -30.869 -49.224 1.00 13.19  ?  257  LEU B N      1 
ATOM   11141 C CA     . LEU B 2 257 ? 4.423   -29.452 -48.925 1.00 13.11  ?  257  LEU B CA     1 
ATOM   11142 C C      . LEU B 2 257 ? 5.828   -28.962 -48.602 1.00 13.17  ?  257  LEU B C      1 
ATOM   11143 O O      . LEU B 2 257 ? 6.667   -29.698 -48.079 1.00 13.40  ?  257  LEU B O      1 
ATOM   11144 C CB     . LEU B 2 257 ? 3.530   -29.154 -47.721 1.00 12.88  ?  257  LEU B CB     1 
ATOM   11145 C CG     . LEU B 2 257 ? 2.035   -29.458 -47.868 1.00 14.00  ?  257  LEU B CG     1 
ATOM   11146 C CD1    . LEU B 2 257 ? 1.357   -29.389 -46.494 1.00 15.55  ?  257  LEU B CD1    1 
ATOM   11147 C CD2    . LEU B 2 257 ? 1.361   -28.527 -48.873 1.00 15.86  ?  257  LEU B CD2    1 
ATOM   11148 H H      . LEU B 2 257 ? 4.040   -31.356 -48.631 1.00 15.83  ?  257  LEU B H      1 
ATOM   11149 H HA     . LEU B 2 257 ? 4.083   -28.977 -49.699 1.00 15.72  ?  257  LEU B HA     1 
ATOM   11150 H HB2    . LEU B 2 257 ? 3.853   -29.681 -46.973 1.00 15.45  ?  257  LEU B HB2    1 
ATOM   11151 H HB3    . LEU B 2 257 ? 3.608   -28.209 -47.520 1.00 15.45  ?  257  LEU B HB3    1 
ATOM   11152 H HG     . LEU B 2 257 ? 1.929   -30.356 -48.220 1.00 16.79  ?  257  LEU B HG     1 
ATOM   11153 H HD11   . LEU B 2 257 ? 0.403   -29.521 -46.606 1.00 18.66  ?  257  LEU B HD11   1 
ATOM   11154 H HD12   . LEU B 2 257 ? 1.724   -30.084 -45.926 1.00 18.66  ?  257  LEU B HD12   1 
ATOM   11155 H HD13   . LEU B 2 257 ? 1.527   -28.518 -46.102 1.00 18.66  ?  257  LEU B HD13   1 
ATOM   11156 H HD21   . LEU B 2 257 ? 0.421   -28.760 -48.939 1.00 19.03  ?  257  LEU B HD21   1 
ATOM   11157 H HD22   . LEU B 2 257 ? 1.454   -27.611 -48.567 1.00 19.03  ?  257  LEU B HD22   1 
ATOM   11158 H HD23   . LEU B 2 257 ? 1.788   -28.632 -49.738 1.00 19.03  ?  257  LEU B HD23   1 
ATOM   11159 N N      . LEU B 2 258 ? 6.078   -27.698 -48.909 1.00 12.72  ?  258  LEU B N      1 
ATOM   11160 C CA     . LEU B 2 258 ? 7.385   -27.087 -48.670 1.00 12.70  ?  258  LEU B CA     1 
ATOM   11161 C C      . LEU B 2 258 ? 7.248   -25.998 -47.612 1.00 13.22  ?  258  LEU B C      1 
ATOM   11162 O O      . LEU B 2 258 ? 6.501   -25.031 -47.793 1.00 13.42  ?  258  LEU B O      1 
ATOM   11163 C CB     . LEU B 2 258 ? 7.958   -26.525 -49.965 1.00 15.10  ?  258  LEU B CB     1 
ATOM   11164 C CG     . LEU B 2 258 ? 9.225   -25.673 -49.855 1.00 16.17  ?  258  LEU B CG     1 
ATOM   11165 C CD1    . LEU B 2 258 ? 10.358  -26.450 -49.196 1.00 16.32  ?  258  LEU B CD1    1 
ATOM   11166 C CD2    . LEU B 2 258 ? 9.648   -25.165 -51.213 1.00 18.01  ?  258  LEU B CD2    1 
ATOM   11167 H H      . LEU B 2 258 ? 5.501   -27.166 -49.260 1.00 15.26  ?  258  LEU B H      1 
ATOM   11168 H HA     . LEU B 2 258 ? 7.999   -27.755 -48.326 1.00 15.23  ?  258  LEU B HA     1 
ATOM   11169 H HB2    . LEU B 2 258 ? 8.170   -27.272 -50.546 1.00 18.11  ?  258  LEU B HB2    1 
ATOM   11170 H HB3    . LEU B 2 258 ? 7.278   -25.968 -50.375 1.00 18.11  ?  258  LEU B HB3    1 
ATOM   11171 H HG     . LEU B 2 258 ? 9.030   -24.906 -49.293 1.00 19.40  ?  258  LEU B HG     1 
ATOM   11172 H HD11   . LEU B 2 258 ? 11.167  -25.916 -49.226 1.00 19.58  ?  258  LEU B HD11   1 
ATOM   11173 H HD12   . LEU B 2 258 ? 10.119  -26.636 -48.274 1.00 19.58  ?  258  LEU B HD12   1 
ATOM   11174 H HD13   . LEU B 2 258 ? 10.492  -27.282 -49.677 1.00 19.58  ?  258  LEU B HD13   1 
ATOM   11175 H HD21   . LEU B 2 258 ? 10.480  -24.676 -51.123 1.00 21.61  ?  258  LEU B HD21   1 
ATOM   11176 H HD22   . LEU B 2 258 ? 9.771   -25.920 -51.809 1.00 21.61  ?  258  LEU B HD22   1 
ATOM   11177 H HD23   . LEU B 2 258 ? 8.956   -24.579 -51.561 1.00 21.61  ?  258  LEU B HD23   1 
ATOM   11178 N N      . ILE B 2 259 ? 7.980   -26.160 -46.520 1.00 12.67  ?  259  ILE B N      1 
ATOM   11179 C CA     . ILE B 2 259 ? 8.114   -25.145 -45.492 1.00 12.70  ?  259  ILE B CA     1 
ATOM   11180 C C      . ILE B 2 259 ? 9.479   -24.490 -45.650 1.00 12.36  ?  259  ILE B C      1 
ATOM   11181 O O      . ILE B 2 259 ? 10.516  -25.149 -45.506 1.00 14.33  ?  259  ILE B O      1 
ATOM   11182 C CB     . ILE B 2 259 ? 8.004   -25.771 -44.092 1.00 12.23  ?  259  ILE B CB     1 
ATOM   11183 C CG1    . ILE B 2 259 ? 6.688   -26.529 -43.908 1.00 13.08  ?  259  ILE B CG1    1 
ATOM   11184 C CG2    . ILE B 2 259 ? 8.141   -24.694 -43.042 1.00 14.74  ?  259  ILE B CG2    1 
ATOM   11185 C CD1    . ILE B 2 259 ? 6.744   -27.474 -42.710 1.00 16.05  ?  259  ILE B CD1    1 
ATOM   11186 H H      . ILE B 2 259 ? 8.424   -26.877 -46.350 1.00 15.20  ?  259  ILE B H      1 
ATOM   11187 H HA     . ILE B 2 259 ? 7.422   -24.476 -45.609 1.00 15.23  ?  259  ILE B HA     1 
ATOM   11188 H HB     . ILE B 2 259 ? 8.723   -26.415 -43.997 1.00 14.68  ?  259  ILE B HB     1 
ATOM   11189 H HG12   . ILE B 2 259 ? 5.970   -25.894 -43.761 1.00 15.69  ?  259  ILE B HG12   1 
ATOM   11190 H HG13   . ILE B 2 259 ? 6.508   -27.055 -44.703 1.00 15.69  ?  259  ILE B HG13   1 
ATOM   11191 H HG21   . ILE B 2 259 ? 7.970   -25.080 -42.169 1.00 17.68  ?  259  ILE B HG21   1 
ATOM   11192 H HG22   . ILE B 2 259 ? 9.042   -24.334 -43.074 1.00 17.68  ?  259  ILE B HG22   1 
ATOM   11193 H HG23   . ILE B 2 259 ? 7.498   -23.991 -43.224 1.00 17.68  ?  259  ILE B HG23   1 
ATOM   11194 H HD11   . ILE B 2 259 ? 5.962   -28.048 -42.723 1.00 19.26  ?  259  ILE B HD11   1 
ATOM   11195 H HD12   . ILE B 2 259 ? 7.550   -28.012 -42.770 1.00 19.26  ?  259  ILE B HD12   1 
ATOM   11196 H HD13   . ILE B 2 259 ? 6.756   -26.950 -41.894 1.00 19.26  ?  259  ILE B HD13   1 
ATOM   11197 N N      . ALA B 2 260 ? 9.502   -23.182 -45.931 1.00 12.61  ?  260  ALA B N      1 
ATOM   11198 C CA     . ALA B 2 260 ? 10.746  -22.427 -45.936 1.00 13.13  ?  260  ALA B CA     1 
ATOM   11199 C C      . ALA B 2 260 ? 10.935  -21.791 -44.572 1.00 11.36  ?  260  ALA B C      1 
ATOM   11200 O O      . ALA B 2 260 ? 10.104  -20.971 -44.131 1.00 13.05  ?  260  ALA B O      1 
ATOM   11201 C CB     . ALA B 2 260 ? 10.731  -21.358 -47.024 1.00 13.66  ?  260  ALA B CB     1 
ATOM   11202 H H      . ALA B 2 260 ? 8.805   -22.716 -46.121 1.00 15.13  ?  260  ALA B H      1 
ATOM   11203 H HA     . ALA B 2 260 ? 11.488  -23.027 -46.114 1.00 15.75  ?  260  ALA B HA     1 
ATOM   11204 H HB1    . ALA B 2 260 ? 11.549  -20.839 -46.968 1.00 16.38  ?  260  ALA B HB1    1 
ATOM   11205 H HB2    . ALA B 2 260 ? 10.671  -21.789 -47.890 1.00 16.38  ?  260  ALA B HB2    1 
ATOM   11206 H HB3    . ALA B 2 260 ? 9.964   -20.780 -46.888 1.00 16.38  ?  260  ALA B HB3    1 
ATOM   11207 N N      . ASP B 2 261 ? 12.029  -22.159 -43.897 1.00 11.42  ?  261  ASP B N      1 
ATOM   11208 C CA     . ASP B 2 261 ? 12.330  -21.602 -42.580 1.00 10.87  ?  261  ASP B CA     1 
ATOM   11209 C C      . ASP B 2 261 ? 13.196  -20.369 -42.810 1.00 13.08  ?  261  ASP B C      1 
ATOM   11210 O O      . ASP B 2 261 ? 14.404  -20.477 -43.069 1.00 13.11  ?  261  ASP B O      1 
ATOM   11211 C CB     . ASP B 2 261 ? 13.013  -22.623 -41.678 1.00 11.73  ?  261  ASP B CB     1 
ATOM   11212 C CG     . ASP B 2 261 ? 13.160  -22.100 -40.255 1.00 13.96  ?  261  ASP B CG     1 
ATOM   11213 O OD1    . ASP B 2 261 ? 13.166  -20.851 -40.100 1.00 13.98  ?  261  ASP B OD1    1 
ATOM   11214 O OD2    . ASP B 2 261 ? 13.264  -22.925 -39.310 1.00 14.39  -1 261  ASP B OD2    1 
ATOM   11215 H H      . ASP B 2 261 ? 12.607  -22.728 -44.183 1.00 13.70  ?  261  ASP B H      1 
ATOM   11216 H HA     . ASP B 2 261 ? 11.508  -21.340 -42.137 1.00 13.04  ?  261  ASP B HA     1 
ATOM   11217 H HB2    . ASP B 2 261 ? 12.481  -23.434 -41.651 1.00 14.07  ?  261  ASP B HB2    1 
ATOM   11218 H HB3    . ASP B 2 261 ? 13.897  -22.818 -42.025 1.00 14.07  ?  261  ASP B HB3    1 
ATOM   11219 N N      . GLU B 2 262 ? 12.554  -19.197 -42.753 1.00 13.03  ?  262  GLU B N      1 
ATOM   11220 C CA     . GLU B 2 262 ? 13.176  -17.911 -42.996 1.00 12.55  ?  262  GLU B CA     1 
ATOM   11221 C C      . GLU B 2 262 ? 13.546  -17.181 -41.718 1.00 13.75  ?  262  GLU B C      1 
ATOM   11222 O O      . GLU B 2 262 ? 13.713  -15.959 -41.726 1.00 13.31  ?  262  GLU B O      1 
ATOM   11223 C CB     . GLU B 2 262 ? 12.233  -17.038 -43.816 1.00 13.69  ?  262  GLU B CB     1 
ATOM   11224 C CG     . GLU B 2 262 ? 11.993  -17.532 -45.215 1.00 13.94  ?  262  GLU B CG     1 
ATOM   11225 C CD     . GLU B 2 262 ? 13.008  -17.005 -46.232 1.00 15.05  ?  262  GLU B CD     1 
ATOM   11226 O OE1    . GLU B 2 262 ? 13.923  -16.221 -45.855 1.00 14.32  ?  262  GLU B OE1    1 
ATOM   11227 O OE2    . GLU B 2 262 ? 12.872  -17.385 -47.411 1.00 15.21  -1 262  GLU B OE2    1 
ATOM   11228 H H      . GLU B 2 262 ? 11.717  -19.129 -42.565 1.00 15.64  ?  262  GLU B H      1 
ATOM   11229 H HA     . GLU B 2 262 ? 13.993  -18.062 -43.498 1.00 15.06  ?  262  GLU B HA     1 
ATOM   11230 H HB2    . GLU B 2 262 ? 11.374  -17.002 -43.366 1.00 16.43  ?  262  GLU B HB2    1 
ATOM   11231 H HB3    . GLU B 2 262 ? 12.612  -16.147 -43.879 1.00 16.43  ?  262  GLU B HB3    1 
ATOM   11232 H HG2    . GLU B 2 262 ? 12.045  -18.500 -45.219 1.00 16.72  ?  262  GLU B HG2    1 
ATOM   11233 H HG3    . GLU B 2 262 ? 11.111  -17.246 -45.501 1.00 16.72  ?  262  GLU B HG3    1 
ATOM   11234 N N      . VAL B 2 263 ? 13.679  -17.892 -40.612 1.00 12.43  ?  263  VAL B N      1 
ATOM   11235 C CA     . VAL B 2 263 ? 13.963  -17.191 -39.366 1.00 12.55  ?  263  VAL B CA     1 
ATOM   11236 C C      . VAL B 2 263 ? 15.268  -16.404 -39.465 1.00 13.09  ?  263  VAL B C      1 
ATOM   11237 O O      . VAL B 2 263 ? 15.358  -15.274 -38.972 1.00 13.31  ?  263  VAL B O      1 
ATOM   11238 C CB     . VAL B 2 263 ? 13.938  -18.172 -38.188 1.00 13.74  ?  263  VAL B CB     1 
ATOM   11239 C CG1    . VAL B 2 263 ? 14.523  -17.537 -36.947 1.00 16.17  ?  263  VAL B CG1    1 
ATOM   11240 C CG2    . VAL B 2 263 ? 12.520  -18.630 -37.909 1.00 14.75  ?  263  VAL B CG2    1 
ATOM   11241 H H      . VAL B 2 263 ? 13.615  -18.747 -40.553 1.00 14.91  ?  263  VAL B H      1 
ATOM   11242 H HA     . VAL B 2 263 ? 13.262  -16.539 -39.210 1.00 15.05  ?  263  VAL B HA     1 
ATOM   11243 H HB     . VAL B 2 263 ? 14.477  -18.944 -38.422 1.00 16.49  ?  263  VAL B HB     1 
ATOM   11244 H HG11   . VAL B 2 263 ? 14.358  -18.118 -36.187 1.00 19.40  ?  263  VAL B HG11   1 
ATOM   11245 H HG12   . VAL B 2 263 ? 15.478  -17.421 -37.072 1.00 19.40  ?  263  VAL B HG12   1 
ATOM   11246 H HG13   . VAL B 2 263 ? 14.101  -16.676 -36.803 1.00 19.40  ?  263  VAL B HG13   1 
ATOM   11247 H HG21   . VAL B 2 263 ? 12.535  -19.293 -37.201 1.00 17.70  ?  263  VAL B HG21   1 
ATOM   11248 H HG22   . VAL B 2 263 ? 11.990  -17.865 -37.635 1.00 17.70  ?  263  VAL B HG22   1 
ATOM   11249 H HG23   . VAL B 2 263 ? 12.149  -19.017 -38.717 1.00 17.70  ?  263  VAL B HG23   1 
ATOM   11250 N N      . VAL B 2 264 ? 16.295  -16.969 -40.085 1.00 14.57  ?  264  VAL B N      1 
ATOM   11251 C CA     . VAL B 2 264 ? 17.536  -16.192 -40.271 1.00 15.13  ?  264  VAL B CA     1 
ATOM   11252 C C      . VAL B 2 264 ? 17.489  -15.338 -41.540 1.00 14.84  ?  264  VAL B C      1 
ATOM   11253 O O      . VAL B 2 264 ? 17.841  -14.157 -41.520 1.00 15.57  ?  264  VAL B O      1 
ATOM   11254 C CB     . VAL B 2 264 ? 18.786  -17.097 -40.259 1.00 15.71  ?  264  VAL B CB     1 
ATOM   11255 C CG1    . VAL B 2 264 ? 19.997  -16.340 -40.795 1.00 17.64  ?  264  VAL B CG1    1 
ATOM   11256 C CG2    . VAL B 2 264 ? 19.049  -17.604 -38.853 1.00 16.89  ?  264  VAL B CG2    1 
ATOM   11257 H H      . VAL B 2 264 ? 16.308  -17.770 -40.400 1.00 17.49  ?  264  VAL B H      1 
ATOM   11258 H HA     . VAL B 2 264 ? 17.606  -15.598 -39.507 1.00 18.16  ?  264  VAL B HA     1 
ATOM   11259 H HB     . VAL B 2 264 ? 18.632  -17.862 -40.835 1.00 18.85  ?  264  VAL B HB     1 
ATOM   11260 H HG11   . VAL B 2 264 ? 20.804  -16.818 -40.546 1.00 21.17  ?  264  VAL B HG11   1 
ATOM   11261 H HG12   . VAL B 2 264 ? 19.931  -16.283 -41.761 1.00 21.17  ?  264  VAL B HG12   1 
ATOM   11262 H HG13   . VAL B 2 264 ? 20.009  -15.449 -40.411 1.00 21.17  ?  264  VAL B HG13   1 
ATOM   11263 H HG21   . VAL B 2 264 ? 19.642  -18.370 -38.900 1.00 20.26  ?  264  VAL B HG21   1 
ATOM   11264 H HG22   . VAL B 2 264 ? 19.463  -16.897 -38.335 1.00 20.26  ?  264  VAL B HG22   1 
ATOM   11265 H HG23   . VAL B 2 264 ? 18.207  -17.862 -38.448 1.00 20.26  ?  264  VAL B HG23   1 
ATOM   11266 N N      . CYS B 2 265 ? 17.067  -15.905 -42.668 1.00 13.42  ?  265  CYS B N      1 
ATOM   11267 C CA     . CYS B 2 265 ? 17.202  -15.175 -43.927 1.00 14.96  ?  265  CYS B CA     1 
ATOM   11268 C C      . CYS B 2 265 ? 16.162  -14.085 -44.110 1.00 14.85  ?  265  CYS B C      1 
ATOM   11269 O O      . CYS B 2 265 ? 16.338  -13.218 -44.976 1.00 16.48  ?  265  CYS B O      1 
ATOM   11270 C CB     . CYS B 2 265 ? 17.105  -16.147 -45.111 1.00 15.28  ?  265  CYS B CB     1 
ATOM   11271 S SG     . CYS B 2 265 ? 18.512  -17.262 -45.193 1.00 17.21  ?  265  CYS B SG     1 
ATOM   11272 H H      . CYS B 2 265 ? 16.710  -16.685 -42.730 1.00 16.10  ?  265  CYS B H      1 
ATOM   11273 H HA     . CYS B 2 265 ? 18.077  -14.756 -43.933 1.00 17.94  ?  265  CYS B HA     1 
ATOM   11274 H HB2    . CYS B 2 265 ? 16.300  -16.682 -45.019 1.00 18.34  ?  265  CYS B HB2    1 
ATOM   11275 H HB3    . CYS B 2 265 ? 17.073  -15.640 -45.937 1.00 18.34  ?  265  CYS B HB3    1 
ATOM   11276 H HG     . CYS B 2 265 ? 18.495  -17.983 -44.234 1.00 20.65  ?  265  CYS B HG     1 
ATOM   11277 N N      . GLY B 2 266 ? 15.086  -14.088 -43.325 1.00 16.58  ?  266  GLY B N      1 
ATOM   11278 C CA     . GLY B 2 266 ? 14.003  -13.151 -43.577 1.00 14.43  ?  266  GLY B CA     1 
ATOM   11279 C C      . GLY B 2 266 ? 14.372  -11.705 -43.292 1.00 15.49  ?  266  GLY B C      1 
ATOM   11280 O O      . GLY B 2 266 ? 15.219  -11.393 -42.449 1.00 16.27  ?  266  GLY B O      1 
ATOM   11281 H H      . GLY B 2 266 ? 14.962  -14.611 -42.653 1.00 19.89  ?  266  GLY B H      1 
ATOM   11282 H HA2    . GLY B 2 266 ? 13.739  -13.216 -44.508 1.00 17.31  ?  266  GLY B HA2    1 
ATOM   11283 H HA3    . GLY B 2 266 ? 13.246  -13.384 -43.017 1.00 17.31  ?  266  GLY B HA3    1 
ATOM   11284 N N      . PHE B 2 267 ? 13.696  -10.813 -44.013 1.00 15.15  ?  267  PHE B N      1 
ATOM   11285 C CA     . PHE B 2 267 ? 13.755  -9.373  -43.769 1.00 15.51  ?  267  PHE B CA     1 
ATOM   11286 C C      . PHE B 2 267 ? 15.130  -8.768  -44.030 1.00 16.93  ?  267  PHE B C      1 
ATOM   11287 O O      . PHE B 2 267 ? 15.602  -7.939  -43.261 1.00 17.27  ?  267  PHE B O      1 
ATOM   11288 C CB     . PHE B 2 267 ? 13.203  -9.028  -42.384 1.00 15.61  ?  267  PHE B CB     1 
ATOM   11289 C CG     . PHE B 2 267 ? 11.812  -9.576  -42.186 1.00 15.09  ?  267  PHE B CG     1 
ATOM   11290 C CD1    . PHE B 2 267 ? 10.718  -8.943  -42.773 1.00 16.24  ?  267  PHE B CD1    1 
ATOM   11291 C CD2    . PHE B 2 267 ? 11.597  -10.750 -41.487 1.00 14.20  ?  267  PHE B CD2    1 
ATOM   11292 C CE1    . PHE B 2 267 ? 9.446   -9.476  -42.650 1.00 17.26  ?  267  PHE B CE1    1 
ATOM   11293 C CE2    . PHE B 2 267 ? 10.322  -11.276 -41.351 1.00 15.09  ?  267  PHE B CE2    1 
ATOM   11294 C CZ     . PHE B 2 267 ? 9.251   -10.636 -41.928 1.00 16.20  ?  267  PHE B CZ     1 
ATOM   11295 H H      . PHE B 2 267 ? 13.181  -11.024 -44.669 1.00 18.18  ?  267  PHE B H      1 
ATOM   11296 H HA     . PHE B 2 267 ? 13.185  -8.937  -44.422 1.00 18.61  ?  267  PHE B HA     1 
ATOM   11297 H HB2    . PHE B 2 267 ? 13.781  -9.410  -41.705 1.00 18.73  ?  267  PHE B HB2    1 
ATOM   11298 H HB3    . PHE B 2 267 ? 13.168  -8.064  -42.285 1.00 18.73  ?  267  PHE B HB3    1 
ATOM   11299 H HD1    . PHE B 2 267 ? 10.843  -8.155  -43.251 1.00 19.48  ?  267  PHE B HD1    1 
ATOM   11300 H HD2    . PHE B 2 267 ? 12.319  -11.193 -41.102 1.00 17.04  ?  267  PHE B HD2    1 
ATOM   11301 H HE1    . PHE B 2 267 ? 8.724   -9.053  -43.054 1.00 20.71  ?  267  PHE B HE1    1 
ATOM   11302 H HE2    . PHE B 2 267 ? 10.191  -12.061 -40.870 1.00 18.10  ?  267  PHE B HE2    1 
ATOM   11303 H HZ     . PHE B 2 267 ? 8.395   -10.985 -41.831 1.00 19.44  ?  267  PHE B HZ     1 
ATOM   11304 N N      . GLY B 2 268 ? 15.750  -9.163  -45.143 1.00 14.97  ?  268  GLY B N      1 
ATOM   11305 C CA     . GLY B 2 268 ? 16.892  -8.468  -45.697 1.00 15.83  ?  268  GLY B CA     1 
ATOM   11306 C C      . GLY B 2 268 ? 18.240  -9.113  -45.495 1.00 15.37  ?  268  GLY B C      1 
ATOM   11307 O O      . GLY B 2 268 ? 19.204  -8.669  -46.110 1.00 16.95  ?  268  GLY B O      1 
ATOM   11308 H H      . GLY B 2 268 ? 15.513  -9.852  -45.601 1.00 17.96  ?  268  GLY B H      1 
ATOM   11309 H HA2    . GLY B 2 268 ? 16.757  -8.375  -46.653 1.00 18.99  ?  268  GLY B HA2    1 
ATOM   11310 H HA3    . GLY B 2 268 ? 16.932  -7.585  -45.297 1.00 18.99  ?  268  GLY B HA3    1 
ATOM   11311 N N      . ARG B 2 269 ? 18.330  -10.185 -44.711 1.00 15.60  ?  269  ARG B N      1 
ATOM   11312 C CA     . ARG B 2 269 ? 19.632  -10.676 -44.258 1.00 15.50  ?  269  ARG B CA     1 
ATOM   11313 C C      . ARG B 2 269 ? 20.564  -11.031 -45.413 1.00 15.92  ?  269  ARG B C      1 
ATOM   11314 O O      . ARG B 2 269 ? 21.773  -10.776 -45.331 1.00 16.87  ?  269  ARG B O      1 
ATOM   11315 C CB     . ARG B 2 269 ? 19.405  -11.858 -43.312 1.00 15.89  ?  269  ARG B CB     1 
ATOM   11316 C CG     . ARG B 2 269 ? 20.608  -12.736 -43.010 1.00 15.90  ?  269  ARG B CG     1 
ATOM   11317 C CD     . ARG B 2 269 ? 21.752  -11.986 -42.353 1.00 15.20  ?  269  ARG B CD     1 
ATOM   11318 N NE     . ARG B 2 269 ? 21.482  -11.526 -40.990 1.00 15.09  ?  269  ARG B NE     1 
ATOM   11319 C CZ     . ARG B 2 269 ? 22.362  -10.839 -40.268 1.00 15.78  ?  269  ARG B CZ     1 
ATOM   11320 N NH1    . ARG B 2 269 ? 23.571  -10.574 -40.766 1.00 16.65  ?  269  ARG B NH1    1 
ATOM   11321 N NH2    . ARG B 2 269 ? 22.063  -10.433 -39.040 1.00 16.11  ?  269  ARG B NH2    1 
ATOM   11322 H H      . ARG B 2 269 ? 17.661  -10.645 -44.428 1.00 18.72  ?  269  ARG B H      1 
ATOM   11323 H HA     . ARG B 2 269 ? 20.088  -9.974  -43.768 1.00 18.60  ?  269  ARG B HA     1 
ATOM   11324 H HB2    . ARG B 2 269 ? 19.091  -11.507 -42.464 1.00 19.07  ?  269  ARG B HB2    1 
ATOM   11325 H HB3    . ARG B 2 269 ? 18.728  -12.430 -43.705 1.00 19.07  ?  269  ARG B HB3    1 
ATOM   11326 H HG2    . ARG B 2 269 ? 20.335  -13.447 -42.408 1.00 19.07  ?  269  ARG B HG2    1 
ATOM   11327 H HG3    . ARG B 2 269 ? 20.939  -13.113 -43.840 1.00 19.07  ?  269  ARG B HG3    1 
ATOM   11328 H HD2    . ARG B 2 269 ? 22.524  -12.573 -42.314 1.00 18.23  ?  269  ARG B HD2    1 
ATOM   11329 H HD3    . ARG B 2 269 ? 21.956  -11.204 -42.889 1.00 18.23  ?  269  ARG B HD3    1 
ATOM   11330 H HE     . ARG B 2 269 ? 20.718  -11.708 -40.640 1.00 18.10  ?  269  ARG B HE     1 
ATOM   11331 H HH11   . ARG B 2 269 ? 23.780  -10.846 -41.554 1.00 19.98  ?  269  ARG B HH11   1 
ATOM   11332 H HH12   . ARG B 2 269 ? 24.140  -10.130 -40.299 1.00 19.98  ?  269  ARG B HH12   1 
ATOM   11333 H HH21   . ARG B 2 269 ? 21.293  -10.613 -38.703 1.00 19.33  ?  269  ARG B HH21   1 
ATOM   11334 H HH22   . ARG B 2 269 ? 22.640  -9.989  -38.582 1.00 19.33  ?  269  ARG B HH22   1 
ATOM   11335 N N      . ILE B 2 270 ? 20.052  -11.646 -46.481 1.00 17.48  ?  270  ILE B N      1 
ATOM   11336 C CA     . ILE B 2 270 ? 20.938  -12.029 -47.575 1.00 16.86  ?  270  ILE B CA     1 
ATOM   11337 C C      . ILE B 2 270 ? 20.802  -11.120 -48.792 1.00 15.36  ?  270  ILE B C      1 
ATOM   11338 O O      . ILE B 2 270 ? 21.242  -11.478 -49.864 1.00 17.70  ?  270  ILE B O      1 
ATOM   11339 C CB     . ILE B 2 270 ? 20.876  -13.521 -47.938 1.00 15.91  ?  270  ILE B CB     1 
ATOM   11340 C CG1    . ILE B 2 270 ? 19.602  -13.893 -48.668 1.00 17.01  ?  270  ILE B CG1    1 
ATOM   11341 C CG2    . ILE B 2 270 ? 21.081  -14.378 -46.686 1.00 18.89  ?  270  ILE B CG2    1 
ATOM   11342 C CD1    . ILE B 2 270 ? 19.670  -15.313 -49.243 1.00 18.10  ?  270  ILE B CD1    1 
ATOM   11343 H H      . ILE B 2 270 ? 19.222  -11.844 -46.588 1.00 20.97  ?  270  ILE B H      1 
ATOM   11344 H HA     . ILE B 2 270 ? 21.836  -11.888 -47.235 1.00 20.23  ?  270  ILE B HA     1 
ATOM   11345 H HB     . ILE B 2 270 ? 21.599  -13.697 -48.560 1.00 19.09  ?  270  ILE B HB     1 
ATOM   11346 H HG12   . ILE B 2 270 ? 18.856  -13.851 -48.050 1.00 20.41  ?  270  ILE B HG12   1 
ATOM   11347 H HG13   . ILE B 2 270 ? 19.461  -13.274 -49.401 1.00 20.41  ?  270  ILE B HG13   1 
ATOM   11348 H HG21   . ILE B 2 270 ? 21.103  -15.313 -46.943 1.00 22.67  ?  270  ILE B HG21   1 
ATOM   11349 H HG22   . ILE B 2 270 ? 21.921  -14.130 -46.268 1.00 22.67  ?  270  ILE B HG22   1 
ATOM   11350 H HG23   . ILE B 2 270 ? 20.347  -14.221 -46.072 1.00 22.67  ?  270  ILE B HG23   1 
ATOM   11351 H HD11   . ILE B 2 270 ? 18.915  -15.450 -49.837 1.00 21.72  ?  270  ILE B HD11   1 
ATOM   11352 H HD12   . ILE B 2 270 ? 20.500  -15.415 -49.736 1.00 21.72  ?  270  ILE B HD12   1 
ATOM   11353 H HD13   . ILE B 2 270 ? 19.638  -15.951 -48.514 1.00 21.72  ?  270  ILE B HD13   1 
ATOM   11354 N N      . GLY B 2 271 ? 20.230  -9.922  -48.625 1.00 16.52  ?  271  GLY B N      1 
ATOM   11355 C CA     . GLY B 2 271 ? 20.154  -8.962  -49.703 1.00 18.03  ?  271  GLY B CA     1 
ATOM   11356 C C      . GLY B 2 271 ? 18.857  -9.006  -50.487 1.00 18.17  ?  271  GLY B C      1 
ATOM   11357 O O      . GLY B 2 271 ? 18.725  -8.282  -51.483 1.00 20.11  ?  271  GLY B O      1 
ATOM   11358 H H      . GLY B 2 271 ? 19.878  -9.652  -47.888 1.00 19.83  ?  271  GLY B H      1 
ATOM   11359 H HA2    . GLY B 2 271 ? 20.251  -8.070  -49.335 1.00 21.64  ?  271  GLY B HA2    1 
ATOM   11360 H HA3    . GLY B 2 271 ? 20.883  -9.128  -50.322 1.00 21.64  ?  271  GLY B HA3    1 
ATOM   11361 N N      . ALA B 2 272 ? 17.902  -9.820  -50.053 1.00 18.51  ?  272  ALA B N      1 
ATOM   11362 C CA     . ALA B 2 272 ? 16.563  -9.876  -50.612 1.00 18.04  ?  272  ALA B CA     1 
ATOM   11363 C C      . ALA B 2 272 ? 15.583  -9.814  -49.451 1.00 18.08  ?  272  ALA B C      1 
ATOM   11364 O O      . ALA B 2 272 ? 15.955  -10.008 -48.298 1.00 18.84  ?  272  ALA B O      1 
ATOM   11365 C CB     . ALA B 2 272 ? 16.339  -11.164 -51.412 1.00 17.50  ?  272  ALA B CB     1 
ATOM   11366 H H      . ALA B 2 272 ? 18.015  -10.375 -49.405 1.00 22.21  ?  272  ALA B H      1 
ATOM   11367 H HA     . ALA B 2 272 ? 16.412  -9.127  -51.210 1.00 21.65  ?  272  ALA B HA     1 
ATOM   11368 H HB1    . ALA B 2 272 ? 15.447  -11.147 -51.795 1.00 21.00  ?  272  ALA B HB1    1 
ATOM   11369 H HB2    . ALA B 2 272 ? 17.001  -11.216 -52.119 1.00 21.00  ?  272  ALA B HB2    1 
ATOM   11370 H HB3    . ALA B 2 272 ? 16.429  -11.925 -50.818 1.00 21.00  ?  272  ALA B HB3    1 
ATOM   11371 N N      . ASP B 2 273 ? 14.317  -9.537  -49.751 1.00 18.83  ?  273  ASP B N      1 
ATOM   11372 C CA     . ASP B 2 273 ? 13.320  -9.507  -48.679 1.00 18.84  ?  273  ASP B CA     1 
ATOM   11373 C C      . ASP B 2 273 ? 13.261  -10.836 -47.939 1.00 17.76  ?  273  ASP B C      1 
ATOM   11374 O O      . ASP B 2 273 ? 13.113  -10.858 -46.712 1.00 17.08  ?  273  ASP B O      1 
ATOM   11375 C CB     . ASP B 2 273 ? 11.949  -9.118  -49.243 1.00 21.58  ?  273  ASP B CB     1 
ATOM   11376 C CG     . ASP B 2 273 ? 11.910  -7.675  -49.733 1.00 25.79  ?  273  ASP B CG     1 
ATOM   11377 O OD1    . ASP B 2 273 ? 12.746  -6.866  -49.273 1.00 28.37  ?  273  ASP B OD1    1 
ATOM   11378 O OD2    . ASP B 2 273 ? 11.044  -7.329  -50.567 1.00 28.18  -1 273  ASP B OD2    1 
ATOM   11379 H H      . ASP B 2 273 ? 14.015  -9.368  -50.538 1.00 22.59  ?  273  ASP B H      1 
ATOM   11380 H HA     . ASP B 2 273 ? 13.572  -8.828  -48.034 1.00 22.61  ?  273  ASP B HA     1 
ATOM   11381 H HB2    . ASP B 2 273 ? 11.738  -9.697  -49.992 1.00 25.89  ?  273  ASP B HB2    1 
ATOM   11382 H HB3    . ASP B 2 273 ? 11.280  -9.219  -48.547 1.00 25.89  ?  273  ASP B HB3    1 
ATOM   11383 N N      . PHE B 2 274 ? 13.345  -11.948 -48.674 1.00 16.40  ?  274  PHE B N      1 
ATOM   11384 C CA     . PHE B 2 274 ? 13.429  -13.284 -48.111 1.00 15.13  ?  274  PHE B CA     1 
ATOM   11385 C C      . PHE B 2 274 ? 14.435  -14.108 -48.901 1.00 16.85  ?  274  PHE B C      1 
ATOM   11386 O O      . PHE B 2 274 ? 14.654  -13.878 -50.086 1.00 18.16  ?  274  PHE B O      1 
ATOM   11387 C CB     . PHE B 2 274 ? 12.071  -13.994 -48.135 1.00 14.14  ?  274  PHE B CB     1 
ATOM   11388 C CG     . PHE B 2 274 ? 11.126  -13.436 -47.142 1.00 15.48  ?  274  PHE B CG     1 
ATOM   11389 C CD1    . PHE B 2 274 ? 11.158  -13.873 -45.828 1.00 16.26  ?  274  PHE B CD1    1 
ATOM   11390 C CD2    . PHE B 2 274 ? 10.257  -12.425 -47.483 1.00 16.68  ?  274  PHE B CD2    1 
ATOM   11391 C CE1    . PHE B 2 274 ? 10.317  -13.332 -44.890 1.00 17.93  ?  274  PHE B CE1    1 
ATOM   11392 C CE2    . PHE B 2 274 ? 9.405   -11.879 -46.549 1.00 16.73  ?  274  PHE B CE2    1 
ATOM   11393 C CZ     . PHE B 2 274 ? 9.424   -12.336 -45.254 1.00 18.24  ?  274  PHE B CZ     1 
ATOM   11394 H H      . PHE B 2 274 ? 13.354  -11.947 -49.534 1.00 19.67  ?  274  PHE B H      1 
ATOM   11395 H HA     . PHE B 2 274 ? 13.734  -13.222 -47.192 1.00 18.16  ?  274  PHE B HA     1 
ATOM   11396 H HB2    . PHE B 2 274 ? 11.677  -13.895 -49.016 1.00 16.96  ?  274  PHE B HB2    1 
ATOM   11397 H HB3    . PHE B 2 274 ? 12.200  -14.934 -47.934 1.00 16.96  ?  274  PHE B HB3    1 
ATOM   11398 H HD1    . PHE B 2 274 ? 11.756  -14.540 -45.580 1.00 19.51  ?  274  PHE B HD1    1 
ATOM   11399 H HD2    . PHE B 2 274 ? 10.245  -12.107 -48.356 1.00 20.02  ?  274  PHE B HD2    1 
ATOM   11400 H HE1    . PHE B 2 274 ? 10.346  -13.633 -44.010 1.00 21.51  ?  274  PHE B HE1    1 
ATOM   11401 H HE2    . PHE B 2 274 ? 8.818   -11.201 -46.795 1.00 20.07  ?  274  PHE B HE2    1 
ATOM   11402 H HZ     . PHE B 2 274 ? 8.840   -11.978 -44.624 1.00 21.89  ?  274  PHE B HZ     1 
ATOM   11403 N N      . GLY B 2 275 ? 15.067  -15.062 -48.217 1.00 14.82  ?  275  GLY B N      1 
ATOM   11404 C CA     . GLY B 2 275 ? 15.966  -15.969 -48.908 1.00 16.99  ?  275  GLY B CA     1 
ATOM   11405 C C      . GLY B 2 275 ? 15.272  -16.694 -50.039 1.00 14.58  ?  275  GLY B C      1 
ATOM   11406 O O      . GLY B 2 275 ? 15.883  -16.967 -51.077 1.00 15.45  ?  275  GLY B O      1 
ATOM   11407 H H      . GLY B 2 275 ? 14.993  -15.200 -47.371 1.00 17.78  ?  275  GLY B H      1 
ATOM   11408 H HA2    . GLY B 2 275 ? 16.712  -15.469 -49.273 1.00 20.38  ?  275  GLY B HA2    1 
ATOM   11409 H HA3    . GLY B 2 275 ? 16.304  -16.628 -48.281 1.00 20.38  ?  275  GLY B HA3    1 
ATOM   11410 N N      . SER B 2 276 ? 13.988  -17.025 -49.845 1.00 15.51  ?  276  SER B N      1 
ATOM   11411 C CA     . SER B 2 276 ? 13.227  -17.694 -50.888 1.00 15.94  ?  276  SER B CA     1 
ATOM   11412 C C      . SER B 2 276 ? 13.186  -16.860 -52.158 1.00 17.29  ?  276  SER B C      1 
ATOM   11413 O O      . SER B 2 276 ? 13.182  -17.413 -53.257 1.00 17.41  ?  276  SER B O      1 
ATOM   11414 C CB     . SER B 2 276 ? 11.802  -17.969 -50.395 1.00 17.63  ?  276  SER B CB     1 
ATOM   11415 O OG     . SER B 2 276 ? 11.785  -18.961 -49.368 1.00 17.19  ?  276  SER B OG     1 
ATOM   11416 H H      . SER B 2 276 ? 13.544  -16.873 -49.124 1.00 18.61  ?  276  SER B H      1 
ATOM   11417 H HA     . SER B 2 276 ? 13.653  -18.541 -51.091 1.00 19.13  ?  276  SER B HA     1 
ATOM   11418 H HB2    . SER B 2 276 ? 11.428  -17.146 -50.042 1.00 21.15  ?  276  SER B HB2    1 
ATOM   11419 H HB3    . SER B 2 276 ? 11.267  -18.282 -51.142 1.00 21.15  ?  276  SER B HB3    1 
ATOM   11420 H HG     . SER B 2 276 ? 12.168  -18.669 -48.680 1.00 20.62  ?  276  SER B HG     1 
ATOM   11421 N N      . HIS B 2 277 ? 13.122  -15.531 -52.031 1.00 17.19  ?  277  HIS B N      1 
ATOM   11422 C CA     . HIS B 2 277 ? 13.120  -14.683 -53.224 1.00 18.00  ?  277  HIS B CA     1 
ATOM   11423 C C      . HIS B 2 277 ? 14.434  -14.814 -53.980 1.00 18.79  ?  277  HIS B C      1 
ATOM   11424 O O      . HIS B 2 277 ? 14.455  -14.904 -55.214 1.00 20.20  ?  277  HIS B O      1 
ATOM   11425 C CB     . HIS B 2 277 ? 12.887  -13.220 -52.846 1.00 19.59  ?  277  HIS B CB     1 
ATOM   11426 C CG     . HIS B 2 277 ? 11.554  -12.960 -52.224 1.00 18.50  ?  277  HIS B CG     1 
ATOM   11427 N ND1    . HIS B 2 277 ? 11.169  -11.712 -51.784 1.00 18.29  ?  277  HIS B ND1    1 
ATOM   11428 C CD2    . HIS B 2 277 ? 10.528  -13.797 -51.934 1.00 17.32  ?  277  HIS B CD2    1 
ATOM   11429 C CE1    . HIS B 2 277 ? 9.945   -11.783 -51.283 1.00 18.33  ?  277  HIS B CE1    1 
ATOM   11430 N NE2    . HIS B 2 277 ? 9.533   -13.038 -51.364 1.00 18.35  ?  277  HIS B NE2    1 
ATOM   11431 H H      . HIS B 2 277 ? 13.081  -15.104 -51.286 1.00 20.62  ?  277  HIS B H      1 
ATOM   11432 H HA     . HIS B 2 277 ? 12.392  -14.965 -53.799 1.00 21.60  ?  277  HIS B HA     1 
ATOM   11433 H HB2    . HIS B 2 277 ? 13.567  -12.951 -52.209 1.00 23.50  ?  277  HIS B HB2    1 
ATOM   11434 H HB3    . HIS B 2 277 ? 12.949  -12.678 -53.648 1.00 23.50  ?  277  HIS B HB3    1 
ATOM   11435 H HD2    . HIS B 2 277 ? 10.501  -14.713 -52.091 1.00 20.78  ?  277  HIS B HD2    1 
ATOM   11436 H HE1    . HIS B 2 277 ? 9.458   -11.072 -50.934 1.00 21.99  ?  277  HIS B HE1    1 
ATOM   11437 H HE2    . HIS B 2 277 ? 8.768   -13.331 -51.102 1.00 22.01  ?  277  HIS B HE2    1 
ATOM   11438 N N      . HIS B 2 278 ? 15.541  -14.825 -53.248 1.00 17.91  ?  278  HIS B N      1 
ATOM   11439 C CA     . HIS B 2 278 ? 16.855  -14.877 -53.862 1.00 15.43  ?  278  HIS B CA     1 
ATOM   11440 C C      . HIS B 2 278 ? 17.089  -16.194 -54.597 1.00 17.49  ?  278  HIS B C      1 
ATOM   11441 O O      . HIS B 2 278 ? 17.705  -16.212 -55.673 1.00 18.81  ?  278  HIS B O      1 
ATOM   11442 C CB     . HIS B 2 278 ? 17.894  -14.697 -52.758 1.00 18.45  ?  278  HIS B CB     1 
ATOM   11443 C CG     . HIS B 2 278 ? 19.285  -14.580 -53.269 1.00 20.46  ?  278  HIS B CG     1 
ATOM   11444 N ND1    . HIS B 2 278 ? 19.752  -13.439 -53.881 1.00 22.79  ?  278  HIS B ND1    1 
ATOM   11445 C CD2    . HIS B 2 278 ? 20.308  -15.464 -53.279 1.00 22.43  ?  278  HIS B CD2    1 
ATOM   11446 C CE1    . HIS B 2 278 ? 21.009  -13.620 -54.240 1.00 25.50  ?  278  HIS B CE1    1 
ATOM   11447 N NE2    . HIS B 2 278 ? 21.372  -14.839 -53.886 1.00 24.89  ?  278  HIS B NE2    1 
ATOM   11448 H H      . HIS B 2 278 ? 15.560  -14.802 -52.388 1.00 21.49  ?  278  HIS B H      1 
ATOM   11449 H HA     . HIS B 2 278 ? 16.938  -14.166 -54.517 1.00 18.52  ?  278  HIS B HA     1 
ATOM   11450 H HB2    . HIS B 2 278 ? 17.690  -13.888 -52.263 1.00 22.14  ?  278  HIS B HB2    1 
ATOM   11451 H HB3    . HIS B 2 278 ? 17.859  -15.465 -52.166 1.00 22.14  ?  278  HIS B HB3    1 
ATOM   11452 H HD1    . HIS B 2 278 ? 19.297  -12.721 -54.010 1.00 27.35  ?  278  HIS B HD1    1 
ATOM   11453 H HD2    . HIS B 2 278 ? 20.295  -16.330 -52.940 1.00 26.91  ?  278  HIS B HD2    1 
ATOM   11454 H HE1    . HIS B 2 278 ? 21.548  -12.995 -54.670 1.00 30.60  ?  278  HIS B HE1    1 
ATOM   11455 N N      . TYR B 2 279 ? 16.604  -17.304 -54.036 1.00 17.00  ?  279  TYR B N      1 
ATOM   11456 C CA     . TYR B 2 279 ? 16.869  -18.629 -54.574 1.00 14.85  ?  279  TYR B CA     1 
ATOM   11457 C C      . TYR B 2 279 ? 15.690  -19.205 -55.348 1.00 16.46  ?  279  TYR B C      1 
ATOM   11458 O O      . TYR B 2 279 ? 15.717  -20.382 -55.691 1.00 17.25  ?  279  TYR B O      1 
ATOM   11459 C CB     . TYR B 2 279 ? 17.284  -19.583 -53.442 1.00 15.55  ?  279  TYR B CB     1 
ATOM   11460 C CG     . TYR B 2 279 ? 18.649  -19.264 -52.888 1.00 16.30  ?  279  TYR B CG     1 
ATOM   11461 C CD1    . TYR B 2 279 ? 19.799  -19.466 -53.649 1.00 17.52  ?  279  TYR B CD1    1 
ATOM   11462 C CD2    . TYR B 2 279 ? 18.803  -18.741 -51.617 1.00 17.42  ?  279  TYR B CD2    1 
ATOM   11463 C CE1    . TYR B 2 279 ? 21.049  -19.150 -53.147 1.00 18.23  ?  279  TYR B CE1    1 
ATOM   11464 C CE2    . TYR B 2 279 ? 20.038  -18.447 -51.108 1.00 18.51  ?  279  TYR B CE2    1 
ATOM   11465 C CZ     . TYR B 2 279 ? 21.168  -18.645 -51.877 1.00 18.64  ?  279  TYR B CZ     1 
ATOM   11466 O OH     . TYR B 2 279 ? 22.420  -18.340 -51.373 1.00 20.39  ?  279  TYR B OH     1 
ATOM   11467 H H      . TYR B 2 279 ? 16.112  -17.308 -53.331 1.00 20.40  ?  279  TYR B H      1 
ATOM   11468 H HA     . TYR B 2 279 ? 17.612  -18.563 -55.194 1.00 17.82  ?  279  TYR B HA     1 
ATOM   11469 H HB2    . TYR B 2 279 ? 16.642  -19.515 -52.718 1.00 18.65  ?  279  TYR B HB2    1 
ATOM   11470 H HB3    . TYR B 2 279 ? 17.303  -20.491 -53.784 1.00 18.65  ?  279  TYR B HB3    1 
ATOM   11471 H HD1    . TYR B 2 279 ? 19.724  -19.818 -54.506 1.00 21.02  ?  279  TYR B HD1    1 
ATOM   11472 H HD2    . TYR B 2 279 ? 18.048  -18.586 -51.095 1.00 20.90  ?  279  TYR B HD2    1 
ATOM   11473 H HE1    . TYR B 2 279 ? 21.808  -19.281 -53.670 1.00 21.88  ?  279  TYR B HE1    1 
ATOM   11474 H HE2    . TYR B 2 279 ? 20.117  -18.114 -50.243 1.00 22.21  ?  279  TYR B HE2    1 
ATOM   11475 H HH     . TYR B 2 279 ? 22.349  -18.031 -50.595 1.00 24.47  ?  279  TYR B HH     1 
ATOM   11476 N N      . ALA B 2 280 ? 14.667  -18.402 -55.634 1.00 17.16  ?  280  ALA B N      1 
ATOM   11477 C CA     . ALA B 2 280 ? 13.496  -18.842 -56.402 1.00 17.31  ?  280  ALA B CA     1 
ATOM   11478 C C      . ALA B 2 280 ? 12.810  -20.051 -55.751 1.00 16.77  ?  280  ALA B C      1 
ATOM   11479 O O      . ALA B 2 280 ? 12.441  -21.034 -56.419 1.00 17.30  ?  280  ALA B O      1 
ATOM   11480 C CB     . ALA B 2 280 ? 13.842  -19.110 -57.867 1.00 19.93  ?  280  ALA B CB     1 
ATOM   11481 H H      . ALA B 2 280 ? 14.624  -17.579 -55.390 1.00 20.59  ?  280  ALA B H      1 
ATOM   11482 H HA     . ALA B 2 280 ? 12.852  -18.116 -56.391 1.00 20.77  ?  280  ALA B HA     1 
ATOM   11483 H HB1    . ALA B 2 280 ? 13.039  -19.384 -58.336 1.00 23.91  ?  280  ALA B HB1    1 
ATOM   11484 H HB2    . ALA B 2 280 ? 14.194  -18.297 -58.262 1.00 23.91  ?  280  ALA B HB2    1 
ATOM   11485 H HB3    . ALA B 2 280 ? 14.508  -19.814 -57.911 1.00 23.91  ?  280  ALA B HB3    1 
ATOM   11486 N N      . ILE B 2 281 ? 12.630  -19.963 -54.438 1.00 15.49  ?  281  ILE B N      1 
ATOM   11487 C CA     . ILE B 2 281 ? 11.876  -20.952 -53.670 1.00 16.18  ?  281  ILE B CA     1 
ATOM   11488 C C      . ILE B 2 281 ? 10.434  -20.462 -53.582 1.00 15.34  ?  281  ILE B C      1 
ATOM   11489 O O      . ILE B 2 281 ? 10.181  -19.289 -53.280 1.00 16.69  ?  281  ILE B O      1 
ATOM   11490 C CB     . ILE B 2 281 ? 12.466  -21.136 -52.265 1.00 15.02  ?  281  ILE B CB     1 
ATOM   11491 C CG1    . ILE B 2 281 ? 13.985  -21.351 -52.326 1.00 16.97  ?  281  ILE B CG1    1 
ATOM   11492 C CG2    . ILE B 2 281 ? 11.806  -22.326 -51.568 1.00 14.88  ?  281  ILE B CG2    1 
ATOM   11493 C CD1    . ILE B 2 281 ? 14.673  -21.482 -50.938 1.00 16.44  ?  281  ILE B CD1    1 
ATOM   11494 H H      . ILE B 2 281 ? 12.944  -19.323 -53.956 1.00 18.59  ?  281  ILE B H      1 
ATOM   11495 H HA     . ILE B 2 281 ? 11.904  -21.809 -54.123 1.00 19.41  ?  281  ILE B HA     1 
ATOM   11496 H HB     . ILE B 2 281 ? 12.291  -20.326 -51.762 1.00 18.02  ?  281  ILE B HB     1 
ATOM   11497 H HG12   . ILE B 2 281 ? 14.162  -22.168 -52.818 1.00 20.36  ?  281  ILE B HG12   1 
ATOM   11498 H HG13   . ILE B 2 281 ? 14.386  -20.595 -52.782 1.00 20.36  ?  281  ILE B HG13   1 
ATOM   11499 H HG21   . ILE B 2 281 ? 12.158  -22.399 -50.667 1.00 17.85  ?  281  ILE B HG21   1 
ATOM   11500 H HG22   . ILE B 2 281 ? 10.847  -22.181 -51.538 1.00 17.85  ?  281  ILE B HG22   1 
ATOM   11501 H HG23   . ILE B 2 281 ? 12.003  -23.134 -52.067 1.00 17.85  ?  281  ILE B HG23   1 
ATOM   11502 H HD11   . ILE B 2 281 ? 15.634  -21.443 -51.057 1.00 19.72  ?  281  ILE B HD11   1 
ATOM   11503 H HD12   . ILE B 2 281 ? 14.380  -20.752 -50.370 1.00 19.72  ?  281  ILE B HD12   1 
ATOM   11504 H HD13   . ILE B 2 281 ? 14.423  -22.330 -50.540 1.00 19.72  ?  281  ILE B HD13   1 
ATOM   11505 N N      . LYS B 2 282 ? 9.487   -21.361 -53.842 1.00 14.51  ?  282  LYS B N      1 
ATOM   11506 C CA     . LYS B 2 282 ? 8.056   -21.056 -53.786 1.00 16.24  ?  282  LYS B CA     1 
ATOM   11507 C C      . LYS B 2 282 ? 7.427   -21.923 -52.702 1.00 15.08  ?  282  LYS B C      1 
ATOM   11508 O O      . LYS B 2 282 ? 6.832   -22.972 -52.991 1.00 16.65  ?  282  LYS B O      1 
ATOM   11509 C CB     . LYS B 2 282 ? 7.404   -21.294 -55.149 1.00 17.58  ?  282  LYS B CB     1 
ATOM   11510 C CG     . LYS B 2 282 ? 7.814   -20.275 -56.211 1.00 22.73  ?  282  LYS B CG     1 
ATOM   11511 C CD     . LYS B 2 282 ? 7.336   -18.872 -55.825 1.00 29.41  ?  282  LYS B CD     1 
ATOM   11512 C CE     . LYS B 2 282 ? 7.394   -17.868 -56.937 1.00 34.29  ?  282  LYS B CE     1 
ATOM   11513 N NZ     . LYS B 2 282 ? 6.912   -16.549 -56.439 1.00 36.25  ?  282  LYS B NZ     1 
ATOM   11514 H H      . LYS B 2 282 ? 9.655   -22.176 -54.058 1.00 17.41  ?  282  LYS B H      1 
ATOM   11515 H HA     . LYS B 2 282 ? 7.922   -20.128 -53.538 1.00 19.49  ?  282  LYS B HA     1 
ATOM   11516 H HB2    . LYS B 2 282 ? 7.659   -22.174 -55.468 1.00 21.09  ?  282  LYS B HB2    1 
ATOM   11517 H HB3    . LYS B 2 282 ? 6.441   -21.245 -55.047 1.00 21.09  ?  282  LYS B HB3    1 
ATOM   11518 H HG2    . LYS B 2 282 ? 8.780   -20.260 -56.292 1.00 27.27  ?  282  LYS B HG2    1 
ATOM   11519 H HG3    . LYS B 2 282 ? 7.414   -20.514 -57.062 1.00 27.27  ?  282  LYS B HG3    1 
ATOM   11520 H HD2    . LYS B 2 282 ? 6.413   -18.929 -55.531 1.00 35.29  ?  282  LYS B HD2    1 
ATOM   11521 H HD3    . LYS B 2 282 ? 7.894   -18.542 -55.104 1.00 35.29  ?  282  LYS B HD3    1 
ATOM   11522 H HE2    . LYS B 2 282 ? 8.308   -17.772 -57.246 1.00 41.15  ?  282  LYS B HE2    1 
ATOM   11523 H HE3    . LYS B 2 282 ? 6.825   -18.154 -57.669 1.00 41.15  ?  282  LYS B HE3    1 
ATOM   11524 H HZ1    . LYS B 2 282 ? 6.835   -15.978 -57.117 1.00 43.49  ?  282  LYS B HZ1    1 
ATOM   11525 H HZ2    . LYS B 2 282 ? 6.118   -16.643 -56.048 1.00 43.49  ?  282  LYS B HZ2    1 
ATOM   11526 H HZ3    . LYS B 2 282 ? 7.489   -16.219 -55.847 1.00 43.49  ?  282  LYS B HZ3    1 
ATOM   11527 N N      . PRO B 2 283 ? 7.514   -21.506 -51.447 1.00 13.68  ?  283  PRO B N      1 
ATOM   11528 C CA     . PRO B 2 283 ? 7.048   -22.357 -50.353 1.00 14.18  ?  283  PRO B CA     1 
ATOM   11529 C C      . PRO B 2 283 ? 5.545   -22.283 -50.180 1.00 13.88  ?  283  PRO B C      1 
ATOM   11530 O O      . PRO B 2 283 ? 4.878   -21.356 -50.631 1.00 16.11  ?  283  PRO B O      1 
ATOM   11531 C CB     . PRO B 2 283 ? 7.758   -21.764 -49.131 1.00 14.73  ?  283  PRO B CB     1 
ATOM   11532 C CG     . PRO B 2 283 ? 7.924   -20.298 -49.473 1.00 14.34  ?  283  PRO B CG     1 
ATOM   11533 C CD     . PRO B 2 283 ? 8.180   -20.275 -50.964 1.00 14.31  ?  283  PRO B CD     1 
ATOM   11534 H HA     . PRO B 2 283 ? 7.320   -23.278 -50.489 1.00 17.01  ?  283  PRO B HA     1 
ATOM   11535 H HB2    . PRO B 2 283 ? 7.209   -21.879 -48.339 1.00 17.68  ?  283  PRO B HB2    1 
ATOM   11536 H HB3    . PRO B 2 283 ? 8.618   -22.194 -49.004 1.00 17.68  ?  283  PRO B HB3    1 
ATOM   11537 H HG2    . PRO B 2 283 ? 7.113   -19.813 -49.253 1.00 17.21  ?  283  PRO B HG2    1 
ATOM   11538 H HG3    . PRO B 2 283 ? 8.676   -19.928 -48.986 1.00 17.21  ?  283  PRO B HG3    1 
ATOM   11539 H HD2    . PRO B 2 283 ? 7.785   -19.487 -51.369 1.00 17.17  ?  283  PRO B HD2    1 
ATOM   11540 H HD3    . PRO B 2 283 ? 9.132   -20.302 -51.150 1.00 17.17  ?  283  PRO B HD3    1 
ATOM   11541 N N      . ASP B 2 284 ? 5.022   -23.289 -49.480 1.00 12.79  ?  284  ASP B N      1 
ATOM   11542 C CA     . ASP B 2 284 ? 3.631   -23.319 -49.064 1.00 13.30  ?  284  ASP B CA     1 
ATOM   11543 C C      . ASP B 2 284 ? 3.403   -22.672 -47.713 1.00 12.53  ?  284  ASP B C      1 
ATOM   11544 O O      . ASP B 2 284 ? 2.289   -22.184 -47.451 1.00 13.09  ?  284  ASP B O      1 
ATOM   11545 C CB     . ASP B 2 284 ? 3.152   -24.767 -49.038 1.00 15.55  ?  284  ASP B CB     1 
ATOM   11546 C CG     . ASP B 2 284 ? 3.290   -25.438 -50.395 1.00 17.24  ?  284  ASP B CG     1 
ATOM   11547 O OD1    . ASP B 2 284 ? 2.657   -24.965 -51.361 1.00 21.25  ?  284  ASP B OD1    1 
ATOM   11548 O OD2    . ASP B 2 284 ? 4.051   -26.428 -50.512 1.00 16.16  -1 284  ASP B OD2    1 
ATOM   11549 H H      . ASP B 2 284 ? 5.466   -23.982 -49.230 1.00 15.34  ?  284  ASP B H      1 
ATOM   11550 H HA     . ASP B 2 284 ? 3.091   -22.829 -49.703 1.00 15.96  ?  284  ASP B HA     1 
ATOM   11551 H HB2    . ASP B 2 284 ? 3.683   -25.267 -48.398 1.00 18.65  ?  284  ASP B HB2    1 
ATOM   11552 H HB3    . ASP B 2 284 ? 2.217   -24.789 -48.782 1.00 18.65  ?  284  ASP B HB3    1 
ATOM   11553 N N      . LEU B 2 285 ? 4.441   -22.667 -46.873 1.00 12.56  ?  285  LEU B N      1 
ATOM   11554 C CA     . LEU B 2 285 ? 4.428   -22.177 -45.493 1.00 11.82  ?  285  LEU B CA     1 
ATOM   11555 C C      . LEU B 2 285 ? 5.787   -21.541 -45.233 1.00 12.32  ?  285  LEU B C      1 
ATOM   11556 O O      . LEU B 2 285 ? 6.799   -22.043 -45.725 1.00 13.39  ?  285  LEU B O      1 
ATOM   11557 C CB     . LEU B 2 285 ? 4.230   -23.354 -44.543 1.00 12.55  ?  285  LEU B CB     1 
ATOM   11558 C CG     . LEU B 2 285 ? 2.851   -24.014 -44.577 1.00 12.87  ?  285  LEU B CG     1 
ATOM   11559 C CD1    . LEU B 2 285 ? 2.894   -25.383 -43.899 1.00 12.66  ?  285  LEU B CD1    1 
ATOM   11560 C CD2    . LEU B 2 285 ? 1.836   -23.120 -43.915 1.00 14.41  ?  285  LEU B CD2    1 
ATOM   11561 H H      . LEU B 2 285 ? 5.217   -22.964 -47.095 1.00 15.06  ?  285  LEU B H      1 
ATOM   11562 H HA     . LEU B 2 285 ? 3.729   -21.519 -45.348 1.00 14.18  ?  285  LEU B HA     1 
ATOM   11563 H HB2    . LEU B 2 285 ? 4.881   -24.037 -44.767 1.00 15.06  ?  285  LEU B HB2    1 
ATOM   11564 H HB3    . LEU B 2 285 ? 4.376   -23.040 -43.637 1.00 15.06  ?  285  LEU B HB3    1 
ATOM   11565 H HG     . LEU B 2 285 ? 2.581   -24.151 -45.498 1.00 15.44  ?  285  LEU B HG     1 
ATOM   11566 H HD11   . LEU B 2 285 ? 2.002   -25.764 -43.901 1.00 15.19  ?  285  LEU B HD11   1 
ATOM   11567 H HD12   . LEU B 2 285 ? 3.502   -25.959 -44.389 1.00 15.19  ?  285  LEU B HD12   1 
ATOM   11568 H HD13   . LEU B 2 285 ? 3.205   -25.273 -42.987 1.00 15.19  ?  285  LEU B HD13   1 
ATOM   11569 H HD21   . LEU B 2 285 ? 0.946   -23.432 -44.140 1.00 17.29  ?  285  LEU B HD21   1 
ATOM   11570 H HD22   . LEU B 2 285 ? 1.966   -23.153 -42.954 1.00 17.29  ?  285  LEU B HD22   1 
ATOM   11571 H HD23   . LEU B 2 285 ? 1.959   -22.212 -44.234 1.00 17.29  ?  285  LEU B HD23   1 
ATOM   11572 N N      . ILE B 2 286 ? 5.817   -20.451 -44.465 1.00 13.96  ?  286  ILE B N      1 
ATOM   11573 C CA     . ILE B 2 286 ? 7.058   -19.740 -44.149 1.00 12.79  ?  286  ILE B CA     1 
ATOM   11574 C C      . ILE B 2 286 ? 7.141   -19.510 -42.643 1.00 11.47  ?  286  ILE B C      1 
ATOM   11575 O O      . ILE B 2 286 ? 6.182   -19.016 -42.037 1.00 13.72  ?  286  ILE B O      1 
ATOM   11576 C CB     . ILE B 2 286 ? 7.138   -18.395 -44.896 1.00 12.39  ?  286  ILE B CB     1 
ATOM   11577 C CG1    . ILE B 2 286 ? 7.083   -18.620 -46.399 1.00 14.25  ?  286  ILE B CG1    1 
ATOM   11578 C CG2    . ILE B 2 286 ? 8.430   -17.672 -44.500 1.00 13.39  ?  286  ILE B CG2    1 
ATOM   11579 C CD1    . ILE B 2 286 ? 7.092   -17.358 -47.211 1.00 14.97  ?  286  ILE B CD1    1 
ATOM   11580 H H      . ILE B 2 286 ? 5.117   -20.099 -44.110 1.00 16.75  ?  286  ILE B H      1 
ATOM   11581 H HA     . ILE B 2 286 ? 7.811   -20.295 -44.406 1.00 15.34  ?  286  ILE B HA     1 
ATOM   11582 H HB     . ILE B 2 286 ? 6.378   -17.846 -44.648 1.00 14.87  ?  286  ILE B HB     1 
ATOM   11583 H HG12   . ILE B 2 286 ? 7.854   -19.145 -46.663 1.00 17.09  ?  286  ILE B HG12   1 
ATOM   11584 H HG13   . ILE B 2 286 ? 6.267   -19.100 -46.611 1.00 17.09  ?  286  ILE B HG13   1 
ATOM   11585 H HG21   . ILE B 2 286 ? 8.517   -16.866 -45.033 1.00 16.06  ?  286  ILE B HG21   1 
ATOM   11586 H HG22   . ILE B 2 286 ? 8.388   -17.443 -43.558 1.00 16.06  ?  286  ILE B HG22   1 
ATOM   11587 H HG23   . ILE B 2 286 ? 9.184   -18.259 -44.664 1.00 16.06  ?  286  ILE B HG23   1 
ATOM   11588 H HD11   . ILE B 2 286 ? 6.779   -17.557 -48.108 1.00 17.96  ?  286  ILE B HD11   1 
ATOM   11589 H HD12   . ILE B 2 286 ? 6.505   -16.709 -46.793 1.00 17.96  ?  286  ILE B HD12   1 
ATOM   11590 H HD13   . ILE B 2 286 ? 7.997   -17.011 -47.246 1.00 17.96  ?  286  ILE B HD13   1 
ATOM   11591 N N      . THR B 2 287 ? 8.310   -19.806 -42.051 1.00 11.38  ?  287  THR B N      1 
ATOM   11592 C CA     . THR B 2 287 ? 8.554   -19.523 -40.628 1.00 11.55  ?  287  THR B CA     1 
ATOM   11593 C C      . THR B 2 287 ? 9.385   -18.251 -40.533 1.00 13.41  ?  287  THR B C      1 
ATOM   11594 O O      . THR B 2 287 ? 10.383  -18.122 -41.252 1.00 13.46  ?  287  THR B O      1 
ATOM   11595 C CB     . THR B 2 287 ? 9.358   -20.655 -39.991 1.00 11.80  ?  287  THR B CB     1 
ATOM   11596 O OG1    . THR B 2 287 ? 8.783   -21.904 -40.357 1.00 14.24  ?  287  THR B OG1    1 
ATOM   11597 C CG2    . THR B 2 287 ? 9.442   -20.522 -38.477 1.00 12.56  ?  287  THR B CG2    1 
ATOM   11598 H H      . THR B 2 287 ? 8.975   -20.171 -42.455 1.00 13.66  ?  287  THR B H      1 
ATOM   11599 H HA     . THR B 2 287 ? 7.709   -19.419 -40.163 1.00 13.86  ?  287  THR B HA     1 
ATOM   11600 H HB     . THR B 2 287 ? 10.272  -20.614 -40.315 1.00 14.16  ?  287  THR B HB     1 
ATOM   11601 H HG1    . THR B 2 287 ? 9.243   -22.534 -40.047 1.00 17.08  ?  287  THR B HG1    1 
ATOM   11602 H HG21   . THR B 2 287 ? 10.104  -21.137 -38.126 1.00 15.06  ?  287  THR B HG21   1 
ATOM   11603 H HG22   . THR B 2 287 ? 9.694   -19.617 -38.236 1.00 15.06  ?  287  THR B HG22   1 
ATOM   11604 H HG23   . THR B 2 287 ? 8.581   -20.726 -38.078 1.00 15.06  ?  287  THR B HG23   1 
ATOM   11605 N N      . ILE B 2 288 ? 8.989   -17.320 -39.648 1.00 12.43  ?  288  ILE B N      1 
ATOM   11606 C CA     . ILE B 2 288 ? 9.714   -16.062 -39.472 1.00 12.94  ?  288  ILE B CA     1 
ATOM   11607 C C      . ILE B 2 288 ? 9.892   -15.748 -37.987 1.00 13.94  ?  288  ILE B C      1 
ATOM   11608 O O      . ILE B 2 288 ? 9.070   -16.133 -37.139 1.00 13.05  ?  288  ILE B O      1 
ATOM   11609 C CB     . ILE B 2 288 ? 9.074   -14.849 -40.200 1.00 11.50  ?  288  ILE B CB     1 
ATOM   11610 C CG1    . ILE B 2 288 ? 7.631   -14.605 -39.747 1.00 11.78  ?  288  ILE B CG1    1 
ATOM   11611 C CG2    . ILE B 2 288 ? 9.179   -15.027 -41.720 1.00 13.99  ?  288  ILE B CG2    1 
ATOM   11612 C CD1    . ILE B 2 288 ? 6.978   -13.338 -40.307 1.00 13.30  ?  288  ILE B CD1    1 
ATOM   11613 H H      . ILE B 2 288 ? 8.300   -17.402 -39.139 1.00 14.91  ?  288  ILE B H      1 
ATOM   11614 H HA     . ILE B 2 288 ? 10.592  -16.205 -39.858 1.00 15.53  ?  288  ILE B HA     1 
ATOM   11615 H HB     . ILE B 2 288 ? 9.574   -14.054 -39.954 1.00 13.80  ?  288  ILE B HB     1 
ATOM   11616 H HG12   . ILE B 2 288 ? 7.090   -15.359 -40.028 1.00 14.13  ?  288  ILE B HG12   1 
ATOM   11617 H HG13   . ILE B 2 288 ? 7.621   -14.533 -38.779 1.00 14.13  ?  288  ILE B HG13   1 
ATOM   11618 H HG21   . ILE B 2 288 ? 8.895   -14.208 -42.154 1.00 16.78  ?  288  ILE B HG21   1 
ATOM   11619 H HG22   . ILE B 2 288 ? 10.100  -15.223 -41.952 1.00 16.78  ?  288  ILE B HG22   1 
ATOM   11620 H HG23   . ILE B 2 288 ? 8.606   -15.762 -41.992 1.00 16.78  ?  288  ILE B HG23   1 
ATOM   11621 H HD11   . ILE B 2 288 ? 6.113   -13.215 -39.884 1.00 15.96  ?  288  ILE B HD11   1 
ATOM   11622 H HD12   . ILE B 2 288 ? 7.549   -12.578 -40.118 1.00 15.96  ?  288  ILE B HD12   1 
ATOM   11623 H HD13   . ILE B 2 288 ? 6.866   -13.437 -41.265 1.00 15.96  ?  288  ILE B HD13   1 
ATOM   11624 N N      . ALA B 2 289 ? 11.004  -15.072 -37.672 1.00 12.50  ?  289  ALA B N      1 
ATOM   11625 C CA     . ALA B 2 289 ? 11.265  -14.508 -36.336 1.00 12.83  ?  289  ALA B CA     1 
ATOM   11626 C C      . ALA B 2 289 ? 12.448  -13.534 -36.462 1.00 14.57  ?  289  ALA B C      1 
ATOM   11627 O O      . ALA B 2 289 ? 12.571  -12.845 -37.476 1.00 16.78  ?  289  ALA B O      1 
ATOM   11628 C CB     . ALA B 2 289 ? 11.532  -15.612 -35.325 1.00 15.25  ?  289  ALA B CB     1 
ATOM   11629 H H      . ALA B 2 289 ? 11.643  -14.921 -38.229 1.00 14.99  ?  289  ALA B H      1 
ATOM   11630 H HA     . ALA B 2 289 ? 10.493  -14.028 -35.996 1.00 15.39  ?  289  ALA B HA     1 
ATOM   11631 H HB1    . ALA B 2 289 ? 11.624  -15.217 -34.444 1.00 18.30  ?  289  ALA B HB1    1 
ATOM   11632 H HB2    . ALA B 2 289 ? 10.788  -16.234 -35.333 1.00 18.30  ?  289  ALA B HB2    1 
ATOM   11633 H HB3    . ALA B 2 289 ? 12.351  -16.072 -35.569 1.00 18.30  ?  289  ALA B HB3    1 
ATOM   11634 N N      . LYS B 2 290 ? 13.322  -13.536 -35.487 1.00 15.80  ?  290  LYS B N      1 
ATOM   11635 C CA     . LYS B 2 290 ? 14.534  -12.697 -35.504 1.00 16.33  ?  290  LYS B CA     1 
ATOM   11636 C C      . LYS B 2 290 ? 14.460  -11.291 -36.173 1.00 15.93  ?  290  LYS B C      1 
ATOM   11637 O O      . LYS B 2 290 ? 14.067  -10.327 -35.539 1.00 15.76  ?  290  LYS B O      1 
ATOM   11638 C CB     . LYS B 2 290 ? 15.675  -13.513 -36.117 1.00 18.27  ?  290  LYS B CB     1 
ATOM   11639 C CG     . LYS B 2 290 ? 16.086  -14.712 -35.292 1.00 22.30  ?  290  LYS B CG     1 
ATOM   11640 C CD     . LYS B 2 290 ? 17.314  -15.415 -35.793 1.00 32.01  ?  290  LYS B CD     1 
ATOM   11641 C CE     . LYS B 2 290 ? 17.806  -16.432 -34.777 1.00 43.35  ?  290  LYS B CE     1 
ATOM   11642 N NZ     . LYS B 2 290 ? 17.683  -17.843 -35.147 1.00 58.04  ?  290  LYS B NZ     1 
ATOM   11643 H H      . LYS B 2 290 ? 13.249  -14.021 -34.780 1.00 18.95  ?  290  LYS B H      1 
ATOM   11644 H HA     . LYS B 2 290 ? 14.783  -12.537 -34.570 1.00 19.59  ?  290  LYS B HA     1 
ATOM   11645 H HB2    . LYS B 2 290 ? 15.396  -13.834 -36.988 1.00 21.92  ?  290  LYS B HB2    1 
ATOM   11646 H HB3    . LYS B 2 290 ? 16.452  -12.939 -36.212 1.00 21.92  ?  290  LYS B HB3    1 
ATOM   11647 H HG2    . LYS B 2 290 ? 16.264  -14.418 -34.385 1.00 26.76  ?  290  LYS B HG2    1 
ATOM   11648 H HG3    . LYS B 2 290 ? 15.358  -15.353 -35.291 1.00 26.76  ?  290  LYS B HG3    1 
ATOM   11649 H HD2    . LYS B 2 290 ? 17.104  -15.882 -36.617 1.00 38.41  ?  290  LYS B HD2    1 
ATOM   11650 H HD3    . LYS B 2 290 ? 18.018  -14.765 -35.943 1.00 38.41  ?  290  LYS B HD3    1 
ATOM   11651 H HE2    . LYS B 2 290 ? 18.745  -16.260 -34.608 1.00 52.01  ?  290  LYS B HE2    1 
ATOM   11652 H HE3    . LYS B 2 290 ? 17.305  -16.306 -33.956 1.00 52.01  ?  290  LYS B HE3    1 
ATOM   11653 H HZ3    . LYS B 2 290 ? 17.662  -17.931 -36.103 1.00 69.65  ?  290  LYS B HZ3    1 
ATOM   11654 N N      . GLY B 2 291 ? 14.830  -11.207 -37.442 1.00 16.40  ?  291  GLY B N      1 
ATOM   11655 C CA     . GLY B 2 291 ? 14.829  -9.922  -38.140 1.00 16.43  ?  291  GLY B CA     1 
ATOM   11656 C C      . GLY B 2 291 ? 13.463  -9.299  -38.334 1.00 15.99  ?  291  GLY B C      1 
ATOM   11657 O O      . GLY B 2 291 ? 13.388  -8.152  -38.804 1.00 17.13  ?  291  GLY B O      1 
ATOM   11658 H H      . GLY B 2 291 ? 15.079  -11.870 -37.929 1.00 19.68  ?  291  GLY B H      1 
ATOM   11659 H HA2    . GLY B 2 291 ? 15.370  -9.295  -37.635 1.00 19.72  ?  291  GLY B HA2    1 
ATOM   11660 H HA3    . GLY B 2 291 ? 15.224  -10.046 -39.017 1.00 19.72  ?  291  GLY B HA3    1 
ATOM   11661 N N      . LEU B 2 292 ? 12.397  -10.023 -37.981 1.00 15.70  ?  292  LEU B N      1 
ATOM   11662 C CA     . LEU B 2 292 ? 11.055  -9.454  -37.969 1.00 14.63  ?  292  LEU B CA     1 
ATOM   11663 C C      . LEU B 2 292 ? 10.975  -8.261  -37.021 1.00 14.00  ?  292  LEU B C      1 
ATOM   11664 O O      . LEU B 2 292 ? 10.308  -7.264  -37.327 1.00 15.01  ?  292  LEU B O      1 
ATOM   11665 C CB     . LEU B 2 292 ? 10.074  -10.547 -37.551 1.00 16.42  ?  292  LEU B CB     1 
ATOM   11666 C CG     . LEU B 2 292 ? 8.649   -10.106 -37.288 1.00 16.12  ?  292  LEU B CG     1 
ATOM   11667 C CD1    . LEU B 2 292 ? 8.047   -9.484  -38.515 1.00 17.22  ?  292  LEU B CD1    1 
ATOM   11668 C CD2    . LEU B 2 292 ? 7.833   -11.291 -36.862 1.00 17.55  ?  292  LEU B CD2    1 
ATOM   11669 H H      . LEU B 2 292 ? 12.424  -10.849 -37.744 1.00 18.84  ?  292  LEU B H      1 
ATOM   11670 H HA     . LEU B 2 292 ? 10.817  -9.138  -38.855 1.00 17.55  ?  292  LEU B HA     1 
ATOM   11671 H HB2    . LEU B 2 292 ? 10.042  -11.210 -38.259 1.00 19.70  ?  292  LEU B HB2    1 
ATOM   11672 H HB3    . LEU B 2 292 ? 10.404  -10.951 -36.733 1.00 19.70  ?  292  LEU B HB3    1 
ATOM   11673 H HG     . LEU B 2 292 ? 8.643   -9.440  -36.582 1.00 19.34  ?  292  LEU B HG     1 
ATOM   11674 H HD11   . LEU B 2 292 ? 7.104   -9.324  -38.357 1.00 20.66  ?  292  LEU B HD11   1 
ATOM   11675 H HD12   . LEU B 2 292 ? 8.499   -8.645  -38.697 1.00 20.66  ?  292  LEU B HD12   1 
ATOM   11676 H HD13   . LEU B 2 292 ? 8.159   -10.090 -39.264 1.00 20.66  ?  292  LEU B HD13   1 
ATOM   11677 H HD21   . LEU B 2 292 ? 6.914   -11.010 -36.726 1.00 21.06  ?  292  LEU B HD21   1 
ATOM   11678 H HD22   . LEU B 2 292 ? 7.872   -11.968 -37.556 1.00 21.06  ?  292  LEU B HD22   1 
ATOM   11679 H HD23   . LEU B 2 292 ? 8.197   -11.644 -36.035 1.00 21.06  ?  292  LEU B HD23   1 
ATOM   11680 N N      . THR B 2 293 ? 11.623  -8.350  -35.855 1.00 14.31  ?  293  THR B N      1 
ATOM   11681 C CA     . THR B 2 293 ? 11.642  -7.232  -34.912 1.00 12.91  ?  293  THR B CA     1 
ATOM   11682 C C      . THR B 2 293 ? 13.055  -6.757  -34.582 1.00 14.10  ?  293  THR B C      1 
ATOM   11683 O O      . THR B 2 293 ? 13.218  -5.894  -33.710 1.00 14.48  ?  293  THR B O      1 
ATOM   11684 C CB     . THR B 2 293 ? 10.970  -7.620  -33.583 1.00 14.53  ?  293  THR B CB     1 
ATOM   11685 O OG1    . THR B 2 293 ? 11.663  -8.729  -33.027 1.00 15.18  ?  293  THR B OG1    1 
ATOM   11686 C CG2    . THR B 2 293 ? 9.508   -7.968  -33.791 1.00 16.10  ?  293  THR B CG2    1 
ATOM   11687 H H      . THR B 2 293 ? 12.056  -9.045  -35.592 1.00 17.17  ?  293  THR B H      1 
ATOM   11688 H HA     . THR B 2 293 ? 11.140  -6.506  -35.314 1.00 15.49  ?  293  THR B HA     1 
ATOM   11689 H HB     . THR B 2 293 ? 11.001  -6.872  -32.966 1.00 17.43  ?  293  THR B HB     1 
ATOM   11690 H HG1    . THR B 2 293 ? 11.363  -8.901  -32.262 1.00 18.22  ?  293  THR B HG1    1 
ATOM   11691 H HG21   . THR B 2 293 ? 9.094   -8.187  -32.941 1.00 19.32  ?  293  THR B HG21   1 
ATOM   11692 H HG22   . THR B 2 293 ? 9.040   -7.215  -34.185 1.00 19.32  ?  293  THR B HG22   1 
ATOM   11693 H HG23   . THR B 2 293 ? 9.430   -8.732  -34.384 1.00 19.32  ?  293  THR B HG23   1 
ATOM   11694 N N      . SER B 2 294 ? 14.082  -7.329  -35.221 1.00 15.05  ?  294  SER B N      1 
ATOM   11695 C CA     . SER B 2 294 ? 15.475  -7.101  -34.834 1.00 14.46  ?  294  SER B CA     1 
ATOM   11696 C C      . SER B 2 294 ? 15.694  -7.350  -33.346 1.00 13.74  ?  294  SER B C      1 
ATOM   11697 O O      . SER B 2 294 ? 16.539  -6.714  -32.721 1.00 15.16  ?  294  SER B O      1 
ATOM   11698 C CB     . SER B 2 294 ? 15.962  -5.714  -35.256 1.00 15.46  ?  294  SER B CB     1 
ATOM   11699 O OG     . SER B 2 294 ? 16.171  -5.663  -36.662 1.00 14.89  ?  294  SER B OG     1 
ATOM   11700 H H      . SER B 2 294 ? 13.994  -7.861  -35.891 1.00 18.06  ?  294  SER B H      1 
ATOM   11701 H HA     . SER B 2 294 ? 16.025  -7.745  -35.306 1.00 17.35  ?  294  SER B HA     1 
ATOM   11702 H HB2    . SER B 2 294 ? 15.293  -5.056  -35.012 1.00 18.55  ?  294  SER B HB2    1 
ATOM   11703 H HB3    . SER B 2 294 ? 16.798  -5.521  -34.804 1.00 18.55  ?  294  SER B HB3    1 
ATOM   11704 H HG     . SER B 2 294 ? 15.440  -5.755  -37.065 1.00 17.86  ?  294  SER B HG     1 
ATOM   11705 N N      . ALA B 2 295 ? 14.923  -8.282  -32.779 1.00 13.86  ?  295  ALA B N      1 
ATOM   11706 C CA     . ALA B 2 295 ? 15.020  -8.725  -31.389 1.00 14.27  ?  295  ALA B CA     1 
ATOM   11707 C C      . ALA B 2 295 ? 14.536  -7.692  -30.385 1.00 14.65  ?  295  ALA B C      1 
ATOM   11708 O O      . ALA B 2 295 ? 14.656  -7.935  -29.170 1.00 15.16  ?  295  ALA B O      1 
ATOM   11709 C CB     . ALA B 2 295 ? 16.433  -9.211  -31.022 1.00 14.50  ?  295  ALA B CB     1 
ATOM   11710 H H      . ALA B 2 295 ? 14.306  -8.700  -33.205 1.00 16.63  ?  295  ALA B H      1 
ATOM   11711 H HA     . ALA B 2 295 ? 14.427  -9.486  -31.286 1.00 17.12  ?  295  ALA B HA     1 
ATOM   11712 H HB1    . ALA B 2 295 ? 16.436  -9.503  -30.097 1.00 17.40  ?  295  ALA B HB1    1 
ATOM   11713 H HB2    . ALA B 2 295 ? 16.673  -9.949  -31.603 1.00 17.40  ?  295  ALA B HB2    1 
ATOM   11714 H HB3    . ALA B 2 295 ? 17.059  -8.479  -31.141 1.00 17.40  ?  295  ALA B HB3    1 
ATOM   11715 N N      . TYR B 2 296 ? 13.998  -6.549  -30.829 1.00 13.38  ?  296  TYR B N      1 
ATOM   11716 C CA     . TYR B 2 296 ? 13.551  -5.533  -29.876 1.00 14.15  ?  296  TYR B CA     1 
ATOM   11717 C C      . TYR B 2 296 ? 12.381  -6.026  -29.035 1.00 14.25  ?  296  TYR B C      1 
ATOM   11718 O O      . TYR B 2 296 ? 12.211  -5.582  -27.886 1.00 15.01  ?  296  TYR B O      1 
ATOM   11719 C CB     . TYR B 2 296 ? 13.261  -4.223  -30.595 1.00 14.53  ?  296  TYR B CB     1 
ATOM   11720 C CG     . TYR B 2 296 ? 14.549  -3.456  -30.863 1.00 13.94  ?  296  TYR B CG     1 
ATOM   11721 C CD1    . TYR B 2 296 ? 15.107  -2.637  -29.897 1.00 13.69  ?  296  TYR B CD1    1 
ATOM   11722 C CD2    . TYR B 2 296 ? 15.235  -3.597  -32.066 1.00 13.81  ?  296  TYR B CD2    1 
ATOM   11723 C CE1    . TYR B 2 296 ? 16.281  -1.946  -30.125 1.00 14.12  ?  296  TYR B CE1    1 
ATOM   11724 C CE2    . TYR B 2 296 ? 16.434  -2.908  -32.301 1.00 15.74  ?  296  TYR B CE2    1 
ATOM   11725 C CZ     . TYR B 2 296 ? 16.956  -2.105  -31.312 1.00 14.30  ?  296  TYR B CZ     1 
ATOM   11726 O OH     . TYR B 2 296 ? 18.122  -1.420  -31.499 1.00 16.87  ?  296  TYR B OH     1 
ATOM   11727 H H      . TYR B 2 296 ? 13.883  -6.341  -31.656 1.00 16.05  ?  296  TYR B H      1 
ATOM   11728 H HA     . TYR B 2 296 ? 14.267  -5.338  -29.251 1.00 16.98  ?  296  TYR B HA     1 
ATOM   11729 H HB2    . TYR B 2 296 ? 12.829  -4.408  -31.443 1.00 17.43  ?  296  TYR B HB2    1 
ATOM   11730 H HB3    . TYR B 2 296 ? 12.683  -3.672  -30.042 1.00 17.43  ?  296  TYR B HB3    1 
ATOM   11731 H HD1    . TYR B 2 296 ? 14.682  -2.550  -29.075 1.00 16.43  ?  296  TYR B HD1    1 
ATOM   11732 H HD2    . TYR B 2 296 ? 14.893  -4.158  -32.725 1.00 16.57  ?  296  TYR B HD2    1 
ATOM   11733 H HE1    . TYR B 2 296 ? 16.615  -1.372  -29.474 1.00 16.94  ?  296  TYR B HE1    1 
ATOM   11734 H HE2    . TYR B 2 296 ? 16.873  -2.993  -33.117 1.00 18.89  ?  296  TYR B HE2    1 
ATOM   11735 H HH     . TYR B 2 296 ? 18.396  -1.530  -32.285 1.00 20.24  ?  296  TYR B HH     1 
ATOM   11736 N N      . GLN B 2 297 ? 11.584  -6.939  -29.580 1.00 12.98  ?  297  GLN B N      1 
ATOM   11737 C CA     . GLN B 2 297 ? 10.529  -7.651  -28.874 1.00 13.65  ?  297  GLN B CA     1 
ATOM   11738 C C      . GLN B 2 297 ? 10.533  -9.077  -29.400 1.00 14.81  ?  297  GLN B C      1 
ATOM   11739 O O      . GLN B 2 297 ? 10.859  -9.302  -30.574 1.00 15.09  ?  297  GLN B O      1 
ATOM   11740 C CB     . GLN B 2 297 ? 9.142   -7.047  -29.149 1.00 13.04  ?  297  GLN B CB     1 
ATOM   11741 C CG     . GLN B 2 297 ? 8.897   -5.695  -28.534 1.00 13.53  ?  297  GLN B CG     1 
ATOM   11742 C CD     . GLN B 2 297 ? 8.633   -5.781  -27.041 1.00 13.41  ?  297  GLN B CD     1 
ATOM   11743 O OE1    . GLN B 2 297 ? 7.497   -5.940  -26.612 1.00 15.04  ?  297  GLN B OE1    1 
ATOM   11744 N NE2    . GLN B 2 297 ? 9.696   -5.666  -26.240 1.00 14.10  ?  297  GLN B NE2    1 
ATOM   11745 H H      . GLN B 2 297 ? 11.641  -7.175  -30.405 1.00 15.58  ?  297  GLN B H      1 
ATOM   11746 H HA     . GLN B 2 297 ? 10.688  -7.628  -27.917 1.00 16.38  ?  297  GLN B HA     1 
ATOM   11747 H HB2    . GLN B 2 297 ? 9.034   -6.953  -30.108 1.00 15.65  ?  297  GLN B HB2    1 
ATOM   11748 H HB3    . GLN B 2 297 ? 8.470   -7.652  -28.797 1.00 15.65  ?  297  GLN B HB3    1 
ATOM   11749 H HG2    . GLN B 2 297 ? 9.679   -5.137  -28.670 1.00 16.23  ?  297  GLN B HG2    1 
ATOM   11750 H HG3    . GLN B 2 297 ? 8.123   -5.289  -28.954 1.00 16.23  ?  297  GLN B HG3    1 
ATOM   11751 H HE21   . GLN B 2 297 ? 10.479  -5.549  -26.578 1.00 16.91  ?  297  GLN B HE21   1 
ATOM   11752 H HE22   . GLN B 2 297 ? 9.598   -5.708  -25.387 1.00 16.91  ?  297  GLN B HE22   1 
ATOM   11753 N N      . PRO B 2 298 ? 10.201  -10.059 -28.557 1.00 13.31  ?  298  PRO B N      1 
ATOM   11754 C CA     . PRO B 2 298 ? 10.046  -11.437 -29.053 1.00 13.30  ?  298  PRO B CA     1 
ATOM   11755 C C      . PRO B 2 298 ? 8.805   -11.528 -29.921 1.00 17.31  ?  298  PRO B C      1 
ATOM   11756 O O      . PRO B 2 298 ? 7.720   -11.157 -29.498 1.00 26.64  ?  298  PRO B O      1 
ATOM   11757 C CB     . PRO B 2 298 ? 9.878   -12.269 -27.777 1.00 15.92  ?  298  PRO B CB     1 
ATOM   11758 C CG     . PRO B 2 298 ? 10.060  -11.371 -26.656 1.00 18.36  ?  298  PRO B CG     1 
ATOM   11759 C CD     . PRO B 2 298 ? 9.938   -9.959  -27.107 1.00 15.30  ?  298  PRO B CD     1 
ATOM   11760 H HA     . PRO B 2 298 ? 10.835  -11.731 -29.535 1.00 15.95  ?  298  PRO B HA     1 
ATOM   11761 H HB2    . PRO B 2 298 ? 8.989   -12.656 -27.760 1.00 19.10  ?  298  PRO B HB2    1 
ATOM   11762 H HB3    . PRO B 2 298 ? 10.546  -12.971 -27.761 1.00 19.10  ?  298  PRO B HB3    1 
ATOM   11763 H HG2    . PRO B 2 298 ? 9.380   -11.563 -25.992 1.00 22.03  ?  298  PRO B HG2    1 
ATOM   11764 H HG3    . PRO B 2 298 ? 10.942  -11.520 -26.281 1.00 22.03  ?  298  PRO B HG3    1 
ATOM   11765 H HD2    . PRO B 2 298 ? 9.047   -9.616  -26.938 1.00 18.36  ?  298  PRO B HD2    1 
ATOM   11766 H HD3    . PRO B 2 298 ? 10.598  -9.396  -26.672 1.00 18.36  ?  298  PRO B HD3    1 
ATOM   11767 N N      . LEU B 2 299 ? 8.969   -12.003 -31.139 1.00 13.07  ?  299  LEU B N      1 
ATOM   11768 C CA     . LEU B 2 299 ? 7.835   -12.167 -32.031 1.00 11.83  ?  299  LEU B CA     1 
ATOM   11769 C C      . LEU B 2 299 ? 8.217   -13.148 -33.127 1.00 12.82  ?  299  LEU B C      1 
ATOM   11770 O O      . LEU B 2 299 ? 9.338   -13.086 -33.656 1.00 16.01  ?  299  LEU B O      1 
ATOM   11771 C CB     . LEU B 2 299 ? 7.412   -10.836 -32.652 1.00 13.03  ?  299  LEU B CB     1 
ATOM   11772 C CG     . LEU B 2 299 ? 6.044   -10.780 -33.338 1.00 13.20  ?  299  LEU B CG     1 
ATOM   11773 C CD1    . LEU B 2 299 ? 4.931   -10.847 -32.317 1.00 16.02  ?  299  LEU B CD1    1 
ATOM   11774 C CD2    . LEU B 2 299 ? 5.871   -9.534  -34.180 1.00 14.86  ?  299  LEU B CD2    1 
ATOM   11775 H H      . LEU B 2 299 ? 9.725   -12.238 -31.474 1.00 15.68  ?  299  LEU B H      1 
ATOM   11776 H HA     . LEU B 2 299 ? 7.084   -12.526 -31.532 1.00 14.19  ?  299  LEU B HA     1 
ATOM   11777 H HB2    . LEU B 2 299 ? 7.401   -10.170 -31.948 1.00 15.63  ?  299  LEU B HB2    1 
ATOM   11778 H HB3    . LEU B 2 299 ? 8.072   -10.599 -33.323 1.00 15.63  ?  299  LEU B HB3    1 
ATOM   11779 H HG     . LEU B 2 299 ? 5.990   -11.547 -33.929 1.00 15.84  ?  299  LEU B HG     1 
ATOM   11780 H HD11   . LEU B 2 299 ? 4.079   -10.766 -32.774 1.00 19.22  ?  299  LEU B HD11   1 
ATOM   11781 H HD12   . LEU B 2 299 ? 4.978   -11.698 -31.854 1.00 19.22  ?  299  LEU B HD12   1 
ATOM   11782 H HD13   . LEU B 2 299 ? 5.038   -10.119 -31.685 1.00 19.22  ?  299  LEU B HD13   1 
ATOM   11783 H HD21   . LEU B 2 299 ? 4.980   -9.534  -34.564 1.00 17.83  ?  299  LEU B HD21   1 
ATOM   11784 H HD22   . LEU B 2 299 ? 5.989   -8.754  -33.617 1.00 17.83  ?  299  LEU B HD22   1 
ATOM   11785 H HD23   . LEU B 2 299 ? 6.535   -9.536  -34.886 1.00 17.83  ?  299  LEU B HD23   1 
ATOM   11786 N N      . SER B 2 300 ? 7.275   -14.024 -33.468 1.00 12.45  ?  300  SER B N      1 
ATOM   11787 C CA     . SER B 2 300 ? 7.455   -14.964 -34.555 1.00 11.49  ?  300  SER B CA     1 
ATOM   11788 C C      . SER B 2 300 ? 6.202   -14.974 -35.396 1.00 10.95  ?  300  SER B C      1 
ATOM   11789 O O      . SER B 2 300 ? 5.138   -14.521 -34.968 1.00 13.24  ?  300  SER B O      1 
ATOM   11790 C CB     . SER B 2 300 ? 7.702   -16.388 -34.055 1.00 13.24  ?  300  SER B CB     1 
ATOM   11791 O OG     . SER B 2 300 ? 6.497   -16.937 -33.540 1.00 13.60  ?  300  SER B OG     1 
ATOM   11792 H H      . SER B 2 300 ? 6.513   -14.089 -33.075 1.00 14.93  ?  300  SER B H      1 
ATOM   11793 H HA     . SER B 2 300 ? 8.216   -14.673 -35.082 1.00 13.78  ?  300  SER B HA     1 
ATOM   11794 H HB2    . SER B 2 300 ? 8.014   -16.936 -34.792 1.00 15.88  ?  300  SER B HB2    1 
ATOM   11795 H HB3    . SER B 2 300 ? 8.370   -16.367 -33.352 1.00 15.88  ?  300  SER B HB3    1 
ATOM   11796 H HG     . SER B 2 300 ? 6.607   -17.749 -33.354 1.00 16.32  ?  300  SER B HG     1 
ATOM   11797 N N      . GLY B 2 301 ? 6.329   -15.557 -36.579 1.00 11.81  ?  301  GLY B N      1 
ATOM   11798 C CA     . GLY B 2 301 ? 5.199   -15.689 -37.477 1.00 12.43  ?  301  GLY B CA     1 
ATOM   11799 C C      . GLY B 2 301 ? 5.251   -16.974 -38.267 1.00 12.52  ?  301  GLY B C      1 
ATOM   11800 O O      . GLY B 2 301 ? 6.324   -17.527 -38.551 1.00 13.02  ?  301  GLY B O      1 
ATOM   11801 H H      . GLY B 2 301 ? 7.063   -15.885 -36.885 1.00 14.16  ?  301  GLY B H      1 
ATOM   11802 H HA2    . GLY B 2 301 ? 4.376   -15.678 -36.964 1.00 14.91  ?  301  GLY B HA2    1 
ATOM   11803 H HA3    . GLY B 2 301 ? 5.193   -14.946 -38.101 1.00 14.91  ?  301  GLY B HA3    1 
ATOM   11804 N N      . VAL B 2 302 ? 4.062   -17.465 -38.585 1.00 12.22  ?  302  VAL B N      1 
ATOM   11805 C CA     . VAL B 2 302 ? 3.864   -18.436 -39.646 1.00 11.19  ?  302  VAL B CA     1 
ATOM   11806 C C      . VAL B 2 302 ? 3.106   -17.713 -40.736 1.00 11.49  ?  302  VAL B C      1 
ATOM   11807 O O      . VAL B 2 302 ? 2.058   -17.113 -40.463 1.00 13.55  ?  302  VAL B O      1 
ATOM   11808 C CB     . VAL B 2 302 ? 3.067   -19.647 -39.150 1.00 11.51  ?  302  VAL B CB     1 
ATOM   11809 C CG1    . VAL B 2 302 ? 2.618   -20.516 -40.334 1.00 13.50  ?  302  VAL B CG1    1 
ATOM   11810 C CG2    . VAL B 2 302 ? 3.896   -20.457 -38.177 1.00 13.92  ?  302  VAL B CG2    1 
ATOM   11811 H H      . VAL B 2 302 ? 3.334   -17.242 -38.185 1.00 14.67  ?  302  VAL B H      1 
ATOM   11812 H HA     . VAL B 2 302 ? 4.716   -18.756 -39.985 1.00 13.43  ?  302  VAL B HA     1 
ATOM   11813 H HB     . VAL B 2 302 ? 2.273   -19.335 -38.689 1.00 13.81  ?  302  VAL B HB     1 
ATOM   11814 H HG11   . VAL B 2 302 ? 2.389   -21.400 -40.007 1.00 16.20  ?  302  VAL B HG11   1 
ATOM   11815 H HG12   . VAL B 2 302 ? 1.843   -20.107 -40.750 1.00 16.20  ?  302  VAL B HG12   1 
ATOM   11816 H HG13   . VAL B 2 302 ? 3.344   -20.578 -40.974 1.00 16.20  ?  302  VAL B HG13   1 
ATOM   11817 H HG21   . VAL B 2 302 ? 3.379   -21.223 -37.884 1.00 16.70  ?  302  VAL B HG21   1 
ATOM   11818 H HG22   . VAL B 2 302 ? 4.705   -20.754 -38.622 1.00 16.70  ?  302  VAL B HG22   1 
ATOM   11819 H HG23   . VAL B 2 302 ? 4.123   -19.900 -37.416 1.00 16.70  ?  302  VAL B HG23   1 
ATOM   11820 N N      . ILE B 2 303 ? 3.650   -17.731 -41.951 1.00 12.19  ?  303  ILE B N      1 
ATOM   11821 C CA     . ILE B 2 303 ? 2.955   -17.218 -43.123 1.00 11.68  ?  303  ILE B CA     1 
ATOM   11822 C C      . ILE B 2 303 ? 2.387   -18.423 -43.877 1.00 12.17  ?  303  ILE B C      1 
ATOM   11823 O O      . ILE B 2 303 ? 3.121   -19.337 -44.266 1.00 13.23  ?  303  ILE B O      1 
ATOM   11824 C CB     . ILE B 2 303 ? 3.882   -16.390 -44.021 1.00 12.00  ?  303  ILE B CB     1 
ATOM   11825 C CG1    . ILE B 2 303 ? 4.840   -15.515 -43.206 1.00 13.23  ?  303  ILE B CG1    1 
ATOM   11826 C CG2    . ILE B 2 303 ? 3.038   -15.490 -44.928 1.00 14.28  ?  303  ILE B CG2    1 
ATOM   11827 C CD1    . ILE B 2 303 ? 5.792   -14.671 -44.066 1.00 14.09  ?  303  ILE B CD1    1 
ATOM   11828 H H      . ILE B 2 303 ? 4.434   -18.042 -42.120 1.00 14.63  ?  303  ILE B H      1 
ATOM   11829 H HA     . ILE B 2 303 ? 2.225   -16.644 -42.843 1.00 14.01  ?  303  ILE B HA     1 
ATOM   11830 H HB     . ILE B 2 303 ? 4.411   -17.011 -44.544 1.00 14.40  ?  303  ILE B HB     1 
ATOM   11831 H HG12   . ILE B 2 303 ? 4.318   -14.907 -42.659 1.00 15.87  ?  303  ILE B HG12   1 
ATOM   11832 H HG13   . ILE B 2 303 ? 5.381   -16.088 -42.641 1.00 15.87  ?  303  ILE B HG13   1 
ATOM   11833 H HG21   . ILE B 2 303 ? 3.619   -15.060 -45.575 1.00 17.13  ?  303  ILE B HG21   1 
ATOM   11834 H HG22   . ILE B 2 303 ? 2.378   -16.033 -45.386 1.00 17.13  ?  303  ILE B HG22   1 
ATOM   11835 H HG23   . ILE B 2 303 ? 2.595   -14.820 -44.384 1.00 17.13  ?  303  ILE B HG23   1 
ATOM   11836 H HD11   . ILE B 2 303 ? 6.461   -14.267 -43.492 1.00 16.90  ?  303  ILE B HD11   1 
ATOM   11837 H HD12   . ILE B 2 303 ? 6.220   -15.246 -44.720 1.00 16.90  ?  303  ILE B HD12   1 
ATOM   11838 H HD13   . ILE B 2 303 ? 5.282   -13.980 -44.517 1.00 16.90  ?  303  ILE B HD13   1 
ATOM   11839 N N      . ILE B 2 304 ? 1.072   -18.436 -44.061 1.00 13.24  ?  304  ILE B N      1 
ATOM   11840 C CA     . ILE B 2 304 ? 0.364   -19.557 -44.662 1.00 14.10  ?  304  ILE B CA     1 
ATOM   11841 C C      . ILE B 2 304 ? 0.016   -19.199 -46.102 1.00 14.18  ?  304  ILE B C      1 
ATOM   11842 O O      . ILE B 2 304 ? -0.650  -18.183 -46.361 1.00 13.38  ?  304  ILE B O      1 
ATOM   11843 C CB     . ILE B 2 304 ? -0.912  -19.866 -43.861 1.00 13.92  ?  304  ILE B CB     1 
ATOM   11844 C CG1    . ILE B 2 304 ? -0.625  -20.187 -42.393 1.00 13.92  ?  304  ILE B CG1    1 
ATOM   11845 C CG2    . ILE B 2 304 ? -1.643  -21.031 -44.496 1.00 15.17  ?  304  ILE B CG2    1 
ATOM   11846 C CD1    . ILE B 2 304 ? -0.624  -18.958 -41.473 1.00 15.44  ?  304  ILE B CD1    1 
ATOM   11847 H H      . ILE B 2 304 ? 0.555   -17.786 -43.838 1.00 15.88  ?  304  ILE B H      1 
ATOM   11848 H HA     . ILE B 2 304 ? 0.937   -20.340 -44.672 1.00 16.92  ?  304  ILE B HA     1 
ATOM   11849 H HB     . ILE B 2 304 ? -1.458  -19.065 -43.883 1.00 16.70  ?  304  ILE B HB     1 
ATOM   11850 H HG12   . ILE B 2 304 ? -1.307  -20.797 -42.069 1.00 16.70  ?  304  ILE B HG12   1 
ATOM   11851 H HG13   . ILE B 2 304 ? 0.249   -20.603 -42.330 1.00 16.70  ?  304  ILE B HG13   1 
ATOM   11852 H HG21   . ILE B 2 304 ? -2.363  -21.309 -43.909 1.00 18.20  ?  304  ILE B HG21   1 
ATOM   11853 H HG22   . ILE B 2 304 ? -2.003  -20.749 -45.351 1.00 18.20  ?  304  ILE B HG22   1 
ATOM   11854 H HG23   . ILE B 2 304 ? -1.019  -21.763 -44.625 1.00 18.20  ?  304  ILE B HG23   1 
ATOM   11855 H HD11   . ILE B 2 304 ? -0.524  -19.251 -40.554 1.00 18.52  ?  304  ILE B HD11   1 
ATOM   11856 H HD12   . ILE B 2 304 ? 0.116   -18.380 -41.719 1.00 18.52  ?  304  ILE B HD12   1 
ATOM   11857 H HD13   . ILE B 2 304 ? -1.463  -18.483 -41.580 1.00 18.52  ?  304  ILE B HD13   1 
ATOM   11858 N N      . GLY B 2 305 ? 0.407   -20.061 -47.029 1.00 13.15  ?  305  GLY B N      1 
ATOM   11859 C CA     . GLY B 2 305 ? 0.099   -19.847 -48.433 1.00 14.47  ?  305  GLY B CA     1 
ATOM   11860 C C      . GLY B 2 305 ? -1.332  -20.189 -48.794 1.00 14.82  ?  305  GLY B C      1 
ATOM   11861 O O      . GLY B 2 305 ? -2.073  -20.775 -48.001 1.00 14.28  ?  305  GLY B O      1 
ATOM   11862 H H      . GLY B 2 305 ? 0.853   -20.779 -46.872 1.00 15.77  ?  305  GLY B H      1 
ATOM   11863 H HA2    . GLY B 2 305 ? 0.251   -18.914 -48.652 1.00 17.36  ?  305  GLY B HA2    1 
ATOM   11864 H HA3    . GLY B 2 305 ? 0.686   -20.398 -48.974 1.00 17.36  ?  305  GLY B HA3    1 
ATOM   11865 N N      . ASP B 2 306 ? -1.719  -19.805 -50.017 1.00 15.73  ?  306  ASP B N      1 
ATOM   11866 C CA     . ASP B 2 306 ? -3.109  -19.940 -50.426 1.00 15.28  ?  306  ASP B CA     1 
ATOM   11867 C C      . ASP B 2 306 ? -3.589  -21.384 -50.350 1.00 13.13  ?  306  ASP B C      1 
ATOM   11868 O O      . ASP B 2 306 ? -4.723  -21.642 -49.931 1.00 15.63  ?  306  ASP B O      1 
ATOM   11869 C CB     . ASP B 2 306 ? -3.305  -19.449 -51.865 1.00 17.95  ?  306  ASP B CB     1 
ATOM   11870 C CG     . ASP B 2 306 ? -3.200  -17.949 -52.015 1.00 21.75  ?  306  ASP B CG     1 
ATOM   11871 O OD1    . ASP B 2 306 ? -3.587  -17.210 -51.087 1.00 22.85  ?  306  ASP B OD1    1 
ATOM   11872 O OD2    . ASP B 2 306 ? -2.769  -17.506 -53.115 1.00 26.29  -1 306  ASP B OD2    1 
ATOM   11873 H H      . ASP B 2 306 ? -1.202  -19.469 -50.616 1.00 18.87  ?  306  ASP B H      1 
ATOM   11874 H HA     . ASP B 2 306 ? -3.634  -19.392 -49.822 1.00 18.33  ?  306  ASP B HA     1 
ATOM   11875 H HB2    . ASP B 2 306 ? -2.624  -19.850 -52.428 1.00 21.54  ?  306  ASP B HB2    1 
ATOM   11876 H HB3    . ASP B 2 306 ? -4.186  -19.716 -52.169 1.00 21.54  ?  306  ASP B HB3    1 
ATOM   11877 N N      . ARG B 2 307 ? -2.778  -22.350 -50.791 1.00 13.76  ?  307  ARG B N      1 
ATOM   11878 C CA     . ARG B 2 307 ? -3.329  -23.704 -50.895 1.00 16.96  ?  307  ARG B CA     1 
ATOM   11879 C C      . ARG B 2 307 ? -3.514  -24.355 -49.535 1.00 13.65  ?  307  ARG B C      1 
ATOM   11880 O O      . ARG B 2 307 ? -4.511  -25.063 -49.321 1.00 16.01  ?  307  ARG B O      1 
ATOM   11881 C CB     . ARG B 2 307 ? -2.575  -24.582 -51.878 1.00 23.92  ?  307  ARG B CB     1 
ATOM   11882 C CG     . ARG B 2 307 ? -1.231  -25.093 -51.518 1.00 30.24  ?  307  ARG B CG     1 
ATOM   11883 C CD     . ARG B 2 307 ? -0.778  -26.067 -52.640 1.00 33.99  ?  307  ARG B CD     1 
ATOM   11884 N NE     . ARG B 2 307 ? 0.600   -26.519 -52.478 1.00 36.03  ?  307  ARG B NE     1 
ATOM   11885 C CZ     . ARG B 2 307 ? 1.068   -27.677 -52.931 1.00 36.99  ?  307  ARG B CZ     1 
ATOM   11886 N NH1    . ARG B 2 307 ? 0.269   -28.521 -53.565 1.00 35.73  ?  307  ARG B NH1    1 
ATOM   11887 N NH2    . ARG B 2 307 ? 2.339   -27.993 -52.729 1.00 37.71  ?  307  ARG B NH2    1 
ATOM   11888 H H      . ARG B 2 307 ? -1.956  -22.256 -51.023 1.00 16.50  ?  307  ARG B H      1 
ATOM   11889 H HA     . ARG B 2 307 ? -4.212  -23.618 -51.286 1.00 20.35  ?  307  ARG B HA     1 
ATOM   11890 H HB2    . ARG B 2 307 ? -3.125  -25.362 -52.049 1.00 28.70  ?  307  ARG B HB2    1 
ATOM   11891 H HB3    . ARG B 2 307 ? -2.461  -24.070 -52.694 1.00 28.70  ?  307  ARG B HB3    1 
ATOM   11892 H HG2    . ARG B 2 307 ? -0.599  -24.360 -51.456 1.00 36.28  ?  307  ARG B HG2    1 
ATOM   11893 H HG3    . ARG B 2 307 ? -1.268  -25.571 -50.675 1.00 36.28  ?  307  ARG B HG3    1 
ATOM   11894 H HD2    . ARG B 2 307 ? -1.352  -26.848 -52.631 1.00 40.79  ?  307  ARG B HD2    1 
ATOM   11895 H HD3    . ARG B 2 307 ? -0.846  -25.616 -53.496 1.00 40.79  ?  307  ARG B HD3    1 
ATOM   11896 H HE     . ARG B 2 307 ? 1.145   -26.001 -52.062 1.00 43.23  ?  307  ARG B HE     1 
ATOM   11897 H HH11   . ARG B 2 307 ? -0.559  -28.321 -53.687 1.00 42.87  ?  307  ARG B HH11   1 
ATOM   11898 H HH12   . ARG B 2 307 ? 0.577   -29.269 -53.856 1.00 42.87  ?  307  ARG B HH12   1 
ATOM   11899 H HH21   . ARG B 2 307 ? 2.856   -27.450 -52.307 1.00 45.25  ?  307  ARG B HH21   1 
ATOM   11900 H HH22   . ARG B 2 307 ? 2.648   -28.741 -53.020 1.00 45.25  ?  307  ARG B HH22   1 
ATOM   11901 N N      . VAL B 2 308 ? -2.600  -24.102 -48.585 1.00 12.97  ?  308  VAL B N      1 
ATOM   11902 C CA     . VAL B 2 308 ? -2.821  -24.596 -47.234 1.00 14.43  ?  308  VAL B CA     1 
ATOM   11903 C C      . VAL B 2 308 ? -3.978  -23.847 -46.584 1.00 13.85  ?  308  VAL B C      1 
ATOM   11904 O O      . VAL B 2 308 ? -4.805  -24.446 -45.892 1.00 14.21  ?  308  VAL B O      1 
ATOM   11905 C CB     . VAL B 2 308 ? -1.531  -24.523 -46.391 1.00 14.38  ?  308  VAL B CB     1 
ATOM   11906 C CG1    . VAL B 2 308 ? -1.790  -24.905 -44.958 1.00 15.30  ?  308  VAL B CG1    1 
ATOM   11907 C CG2    . VAL B 2 308 ? -0.510  -25.474 -46.950 1.00 15.45  ?  308  VAL B CG2    1 
ATOM   11908 H H      . VAL B 2 308 ? -1.870  -23.661 -48.699 1.00 15.56  ?  308  VAL B H      1 
ATOM   11909 H HA     . VAL B 2 308 ? -3.063  -25.534 -47.290 1.00 17.31  ?  308  VAL B HA     1 
ATOM   11910 H HB     . VAL B 2 308 ? -1.204  -23.610 -46.420 1.00 17.25  ?  308  VAL B HB     1 
ATOM   11911 H HG11   . VAL B 2 308 ? -0.941  -25.006 -44.499 1.00 18.36  ?  308  VAL B HG11   1 
ATOM   11912 H HG12   . VAL B 2 308 ? -2.313  -24.206 -44.534 1.00 18.36  ?  308  VAL B HG12   1 
ATOM   11913 H HG13   . VAL B 2 308 ? -2.279  -25.742 -44.937 1.00 18.36  ?  308  VAL B HG13   1 
ATOM   11914 H HG21   . VAL B 2 308 ? 0.283   -25.452 -46.391 1.00 18.54  ?  308  VAL B HG21   1 
ATOM   11915 H HG22   . VAL B 2 308 ? -0.883  -26.369 -46.959 1.00 18.54  ?  308  VAL B HG22   1 
ATOM   11916 H HG23   . VAL B 2 308 ? -0.285  -25.200 -47.853 1.00 18.54  ?  308  VAL B HG23   1 
ATOM   11917 N N      . TRP B 2 309 ? -4.070  -22.532 -46.798 1.00 14.32  ?  309  TRP B N      1 
ATOM   11918 C CA     . TRP B 2 309 ? -5.148  -21.769 -46.186 1.00 14.42  ?  309  TRP B CA     1 
ATOM   11919 C C      . TRP B 2 309 ? -6.511  -22.306 -46.612 1.00 14.78  ?  309  TRP B C      1 
ATOM   11920 O O      . TRP B 2 309 ? -7.451  -22.349 -45.810 1.00 14.85  ?  309  TRP B O      1 
ATOM   11921 C CB     . TRP B 2 309 ? -5.034  -20.277 -46.533 1.00 15.01  ?  309  TRP B CB     1 
ATOM   11922 C CG     . TRP B 2 309 ? -6.092  -19.509 -45.838 1.00 14.82  ?  309  TRP B CG     1 
ATOM   11923 C CD1    . TRP B 2 309 ? -7.201  -18.960 -46.393 1.00 15.06  ?  309  TRP B CD1    1 
ATOM   11924 C CD2    . TRP B 2 309 ? -6.172  -19.253 -44.436 1.00 14.82  ?  309  TRP B CD2    1 
ATOM   11925 N NE1    . TRP B 2 309 ? -7.971  -18.349 -45.417 1.00 14.35  ?  309  TRP B NE1    1 
ATOM   11926 C CE2    . TRP B 2 309 ? -7.352  -18.522 -44.208 1.00 13.46  ?  309  TRP B CE2    1 
ATOM   11927 C CE3    . TRP B 2 309 ? -5.358  -19.567 -43.345 1.00 12.83  ?  309  TRP B CE3    1 
ATOM   11928 C CZ2    . TRP B 2 309 ? -7.728  -18.093 -42.931 1.00 13.79  ?  309  TRP B CZ2    1 
ATOM   11929 C CZ3    . TRP B 2 309 ? -5.740  -19.157 -42.090 1.00 14.19  ?  309  TRP B CZ3    1 
ATOM   11930 C CH2    . TRP B 2 309 ? -6.908  -18.415 -41.896 1.00 14.97  ?  309  TRP B CH2    1 
ATOM   11931 H H      . TRP B 2 309 ? -3.532  -22.069 -47.282 1.00 17.19  ?  309  TRP B H      1 
ATOM   11932 H HA     . TRP B 2 309 ? -5.067  -21.852 -45.223 1.00 17.30  ?  309  TRP B HA     1 
ATOM   11933 H HB2    . TRP B 2 309 ? -4.169  -19.942 -46.249 1.00 18.01  ?  309  TRP B HB2    1 
ATOM   11934 H HB3    . TRP B 2 309 ? -5.139  -20.156 -47.490 1.00 18.01  ?  309  TRP B HB3    1 
ATOM   11935 H HD1    . TRP B 2 309 ? -7.413  -18.989 -47.298 1.00 18.07  ?  309  TRP B HD1    1 
ATOM   11936 H HE1    . TRP B 2 309 ? -8.712  -17.932 -45.548 1.00 17.22  ?  309  TRP B HE1    1 
ATOM   11937 H HE3    . TRP B 2 309 ? -4.570  -20.046 -43.466 1.00 15.39  ?  309  TRP B HE3    1 
ATOM   11938 H HZ2    . TRP B 2 309 ? -8.508  -17.605 -42.796 1.00 16.54  ?  309  TRP B HZ2    1 
ATOM   11939 H HZ3    . TRP B 2 309 ? -5.212  -19.377 -41.358 1.00 17.02  ?  309  TRP B HZ3    1 
ATOM   11940 H HH2    . TRP B 2 309 ? -7.130  -18.136 -41.037 1.00 17.96  ?  309  TRP B HH2    1 
ATOM   11941 N N      . GLN B 2 310 ? -6.643  -22.707 -47.878 1.00 14.76  ?  310  GLN B N      1 
ATOM   11942 C CA     . GLN B 2 310 ? -7.922  -23.220 -48.356 1.00 15.55  ?  310  GLN B CA     1 
ATOM   11943 C C      . GLN B 2 310 ? -8.372  -24.430 -47.545 1.00 14.43  ?  310  GLN B C      1 
ATOM   11944 O O      . GLN B 2 310 ? -9.561  -24.557 -47.221 1.00 14.55  ?  310  GLN B O      1 
ATOM   11945 C CB     . GLN B 2 310 ? -7.790  -23.580 -49.830 1.00 15.54  ?  310  GLN B CB     1 
ATOM   11946 C CG     . GLN B 2 310 ? -9.026  -24.204 -50.407 1.00 19.79  ?  310  GLN B CG     1 
ATOM   11947 C CD     . GLN B 2 310 ? -8.984  -24.283 -51.899 1.00 26.23  ?  310  GLN B CD     1 
ATOM   11948 O OE1    . GLN B 2 310 ? -8.447  -25.220 -52.477 1.00 30.74  ?  310  GLN B OE1    1 
ATOM   11949 N NE2    . GLN B 2 310 ? -9.549  -23.268 -52.539 1.00 27.34  ?  310  GLN B NE2    1 
ATOM   11950 H H      . GLN B 2 310 ? -6.019  -22.694 -48.470 1.00 17.71  ?  310  GLN B H      1 
ATOM   11951 H HA     . GLN B 2 310 ? -8.602  -22.535 -48.261 1.00 18.66  ?  310  GLN B HA     1 
ATOM   11952 H HB2    . GLN B 2 310 ? -7.603  -22.772 -50.333 1.00 18.65  ?  310  GLN B HB2    1 
ATOM   11953 H HB3    . GLN B 2 310 ? -7.062  -24.212 -49.933 1.00 18.65  ?  310  GLN B HB3    1 
ATOM   11954 H HG2    . GLN B 2 310 ? -9.118  -25.106 -50.060 1.00 23.74  ?  310  GLN B HG2    1 
ATOM   11955 H HG3    . GLN B 2 310 ? -9.797  -23.673 -50.155 1.00 23.74  ?  310  GLN B HG3    1 
ATOM   11956 H HE21   . GLN B 2 310 ? -9.905  -22.623 -52.095 1.00 32.81  ?  310  GLN B HE21   1 
ATOM   11957 H HE22   . GLN B 2 310 ? -9.558  -23.253 -53.399 1.00 32.81  ?  310  GLN B HE22   1 
ATOM   11958 N N      . VAL B 2 311 ? -7.428  -25.302 -47.168 1.00 14.77  ?  311  VAL B N      1 
ATOM   11959 C CA     . VAL B 2 311 ? -7.771  -26.483 -46.378 1.00 14.78  ?  311  VAL B CA     1 
ATOM   11960 C C      . VAL B 2 311 ? -8.027  -26.109 -44.919 1.00 14.65  ?  311  VAL B C      1 
ATOM   11961 O O      . VAL B 2 311 ? -8.878  -26.722 -44.272 1.00 15.15  ?  311  VAL B O      1 
ATOM   11962 C CB     . VAL B 2 311 ? -6.680  -27.547 -46.546 1.00 13.76  ?  311  VAL B CB     1 
ATOM   11963 C CG1    . VAL B 2 311 ? -6.941  -28.796 -45.693 1.00 15.18  ?  311  VAL B CG1    1 
ATOM   11964 C CG2    . VAL B 2 311 ? -6.629  -27.967 -48.026 1.00 13.96  ?  311  VAL B CG2    1 
ATOM   11965 H H      . VAL B 2 311 ? -6.591  -25.233 -47.354 1.00 17.72  ?  311  VAL B H      1 
ATOM   11966 H HA     . VAL B 2 311 ? -8.598  -26.869 -46.707 1.00 17.74  ?  311  VAL B HA     1 
ATOM   11967 H HB     . VAL B 2 311 ? -5.838  -27.164 -46.255 1.00 16.50  ?  311  VAL B HB     1 
ATOM   11968 H HG11   . VAL B 2 311 ? -6.247  -29.450 -45.871 1.00 18.22  ?  311  VAL B HG11   1 
ATOM   11969 H HG12   . VAL B 2 311 ? -6.928  -28.546 -44.756 1.00 18.22  ?  311  VAL B HG12   1 
ATOM   11970 H HG13   . VAL B 2 311 ? -7.808  -29.162 -45.926 1.00 18.22  ?  311  VAL B HG13   1 
ATOM   11971 H HG21   . VAL B 2 311 ? -5.947  -28.647 -48.137 1.00 16.75  ?  311  VAL B HG21   1 
ATOM   11972 H HG22   . VAL B 2 311 ? -7.494  -28.321 -48.284 1.00 16.75  ?  311  VAL B HG22   1 
ATOM   11973 H HG23   . VAL B 2 311 ? -6.414  -27.191 -48.567 1.00 16.75  ?  311  VAL B HG23   1 
ATOM   11974 N N      . LEU B 2 312 ? -7.331  -25.092 -44.384 1.00 13.55  ?  312  LEU B N      1 
ATOM   11975 C CA     . LEU B 2 312 ? -7.687  -24.595 -43.055 1.00 13.54  ?  312  LEU B CA     1 
ATOM   11976 C C      . LEU B 2 312 ? -9.118  -24.071 -43.037 1.00 13.02  ?  312  LEU B C      1 
ATOM   11977 O O      . LEU B 2 312 ? -9.837  -24.250 -42.053 1.00 14.89  ?  312  LEU B O      1 
ATOM   11978 C CB     . LEU B 2 312 ? -6.689  -23.535 -42.580 1.00 13.83  ?  312  LEU B CB     1 
ATOM   11979 C CG     . LEU B 2 312 ? -5.248  -24.002 -42.384 1.00 15.48  ?  312  LEU B CG     1 
ATOM   11980 C CD1    . LEU B 2 312 ? -4.304  -22.866 -41.927 1.00 17.96  ?  312  LEU B CD1    1 
ATOM   11981 C CD2    . LEU B 2 312 ? -5.133  -25.160 -41.400 1.00 21.65  ?  312  LEU B CD2    1 
ATOM   11982 H H      . LEU B 2 312 ? -6.671  -24.688 -44.759 1.00 16.26  ?  312  LEU B H      1 
ATOM   11983 H HA     . LEU B 2 312 ? -7.631  -25.328 -42.421 1.00 16.25  ?  312  LEU B HA     1 
ATOM   11984 H HB2    . LEU B 2 312 ? -6.672  -22.822 -43.238 1.00 16.59  ?  312  LEU B HB2    1 
ATOM   11985 H HB3    . LEU B 2 312 ? -6.997  -23.192 -41.727 1.00 16.59  ?  312  LEU B HB3    1 
ATOM   11986 H HG     . LEU B 2 312 ? -4.961  -24.307 -43.259 1.00 18.57  ?  312  LEU B HG     1 
ATOM   11987 H HD11   . LEU B 2 312 ? -3.480  -23.255 -41.595 1.00 21.54  ?  312  LEU B HD11   1 
ATOM   11988 H HD12   . LEU B 2 312 ? -4.116  -22.289 -42.684 1.00 21.54  ?  312  LEU B HD12   1 
ATOM   11989 H HD13   . LEU B 2 312 ? -4.738  -22.358 -41.224 1.00 21.54  ?  312  LEU B HD13   1 
ATOM   11990 H HD21   . LEU B 2 312 ? -4.195  -25.336 -41.228 1.00 25.97  ?  312  LEU B HD21   1 
ATOM   11991 H HD22   . LEU B 2 312 ? -5.581  -24.918 -40.574 1.00 25.97  ?  312  LEU B HD22   1 
ATOM   11992 H HD23   . LEU B 2 312 ? -5.552  -25.945 -41.786 1.00 25.97  ?  312  LEU B HD23   1 
ATOM   11993 N N      . GLU B 2 313 ? -9.549  -23.398 -44.112 1.00 13.89  ?  313  GLU B N      1 
ATOM   11994 C CA     . GLU B 2 313 ? -10.948 -22.978 -44.198 1.00 13.69  ?  313  GLU B CA     1 
ATOM   11995 C C      . GLU B 2 313 ? -11.876 -24.189 -44.271 1.00 13.76  ?  313  GLU B C      1 
ATOM   11996 O O      . GLU B 2 313 ? -12.887 -24.257 -43.568 1.00 15.55  ?  313  GLU B O      1 
ATOM   11997 C CB     . GLU B 2 313 ? -11.168 -22.057 -45.393 1.00 15.91  ?  313  GLU B CB     1 
ATOM   11998 C CG     . GLU B 2 313 ? -10.523 -20.667 -45.230 1.00 16.92  ?  313  GLU B CG     1 
ATOM   11999 C CD     . GLU B 2 313 ? -11.010 -19.636 -46.244 1.00 17.60  ?  313  GLU B CD     1 
ATOM   12000 O OE1    . GLU B 2 313 ? -11.656 -20.016 -47.248 1.00 21.75  ?  313  GLU B OE1    1 
ATOM   12001 O OE2    . GLU B 2 313 ? -10.729 -18.431 -46.049 1.00 16.21  -1 313  GLU B OE2    1 
ATOM   12002 H H      . GLU B 2 313 ? -9.065  -23.179 -44.788 1.00 16.67  ?  313  GLU B H      1 
ATOM   12003 H HA     . GLU B 2 313 ? -11.164 -22.472 -43.399 1.00 16.43  ?  313  GLU B HA     1 
ATOM   12004 H HB2    . GLU B 2 313 ? -10.784 -22.471 -46.182 1.00 19.09  ?  313  GLU B HB2    1 
ATOM   12005 H HB3    . GLU B 2 313 ? -12.121 -21.929 -45.517 1.00 19.09  ?  313  GLU B HB3    1 
ATOM   12006 H HG2    . GLU B 2 313 ? -10.729 -20.329 -44.344 1.00 20.30  ?  313  GLU B HG2    1 
ATOM   12007 H HG3    . GLU B 2 313 ? -9.562  -20.754 -45.336 1.00 20.30  ?  313  GLU B HG3    1 
ATOM   12008 N N      . GLN B 2 314 ? -11.538 -25.173 -45.097 1.00 15.46  ?  314  GLN B N      1 
ATOM   12009 C CA     . GLN B 2 314 ? -12.426 -26.323 -45.211 1.00 16.34  ?  314  GLN B CA     1 
ATOM   12010 C C      . GLN B 2 314 ? -12.557 -27.026 -43.866 1.00 14.52  ?  314  GLN B C      1 
ATOM   12011 O O      . GLN B 2 314 ? -13.656 -27.403 -43.451 1.00 16.16  ?  314  GLN B O      1 
ATOM   12012 C CB     . GLN B 2 314 ? -11.922 -27.300 -46.272 1.00 18.11  ?  314  GLN B CB     1 
ATOM   12013 C CG     . GLN B 2 314 ? -12.904 -28.424 -46.485 1.00 21.27  ?  314  GLN B CG     1 
ATOM   12014 C CD     . GLN B 2 314 ? -12.487 -29.431 -47.534 1.00 25.43  ?  314  GLN B CD     1 
ATOM   12015 O OE1    . GLN B 2 314 ? -11.308 -29.709 -47.725 1.00 24.74  ?  314  GLN B OE1    1 
ATOM   12016 N NE2    . GLN B 2 314 ? -13.485 -29.991 -48.236 1.00 30.39  ?  314  GLN B NE2    1 
ATOM   12017 H H      . GLN B 2 314 ? -10.829 -25.201 -45.583 1.00 18.54  ?  314  GLN B H      1 
ATOM   12018 H HA     . GLN B 2 314 ? -13.300 -26.013 -45.496 1.00 19.61  ?  314  GLN B HA     1 
ATOM   12019 H HB2    . GLN B 2 314 ? -11.806 -26.830 -47.113 1.00 21.73  ?  314  GLN B HB2    1 
ATOM   12020 H HB3    . GLN B 2 314 ? -11.077 -27.680 -45.985 1.00 21.73  ?  314  GLN B HB3    1 
ATOM   12021 H HG2    . GLN B 2 314 ? -13.013 -28.902 -45.648 1.00 25.53  ?  314  GLN B HG2    1 
ATOM   12022 H HG3    . GLN B 2 314 ? -13.752 -28.045 -46.763 1.00 25.53  ?  314  GLN B HG3    1 
ATOM   12023 H HE21   . GLN B 2 314 ? -14.301 -29.769 -48.076 1.00 36.47  ?  314  GLN B HE21   1 
ATOM   12024 H HE22   . GLN B 2 314 ? -13.309 -30.570 -48.847 1.00 36.47  ?  314  GLN B HE22   1 
ATOM   12025 N N      . GLY B 2 315 ? -11.443 -27.172 -43.155 1.00 14.99  ?  315  GLY B N      1 
ATOM   12026 C CA     . GLY B 2 315 ? -11.461 -27.898 -41.896 1.00 16.50  ?  315  GLY B CA     1 
ATOM   12027 C C      . GLY B 2 315 ? -12.232 -27.175 -40.814 1.00 15.10  ?  315  GLY B C      1 
ATOM   12028 O O      . GLY B 2 315 ? -12.999 -27.795 -40.068 1.00 15.65  ?  315  GLY B O      1 
ATOM   12029 H H      . GLY B 2 315 ? -10.671 -26.865 -43.376 1.00 17.99  ?  315  GLY B H      1 
ATOM   12030 H HA2    . GLY B 2 315 ? -11.871 -28.766 -42.034 1.00 19.80  ?  315  GLY B HA2    1 
ATOM   12031 H HA3    . GLY B 2 315 ? -10.550 -28.025 -41.587 1.00 19.80  ?  315  GLY B HA3    1 
ATOM   12032 N N      . THR B 2 316 ? -12.047 -25.858 -40.708 1.00 13.98  ?  316  THR B N      1 
ATOM   12033 C CA     . THR B 2 316 ? -12.806 -25.101 -39.711 1.00 14.87  ?  316  THR B CA     1 
ATOM   12034 C C      . THR B 2 316 ? -14.276 -25.049 -40.076 1.00 15.89  ?  316  THR B C      1 
ATOM   12035 O O      . THR B 2 316 ? -15.131 -25.074 -39.185 1.00 16.92  ?  316  THR B O      1 
ATOM   12036 C CB     . THR B 2 316 ? -12.194 -23.721 -39.451 1.00 14.64  ?  316  THR B CB     1 
ATOM   12037 O OG1    . THR B 2 316 ? -12.095 -22.950 -40.653 1.00 15.07  ?  316  THR B OG1    1 
ATOM   12038 C CG2    . THR B 2 316 ? -10.817 -23.870 -38.805 1.00 15.35  ?  316  THR B CG2    1 
ATOM   12039 H H      . THR B 2 316 ? -11.505 -25.390 -41.185 1.00 16.78  ?  316  THR B H      1 
ATOM   12040 H HA     . THR B 2 316 ? -12.743 -25.550 -38.854 1.00 17.85  ?  316  THR B HA     1 
ATOM   12041 H HB     . THR B 2 316 ? -12.773 -23.235 -38.844 1.00 17.56  ?  316  THR B HB     1 
ATOM   12042 H HG1    . THR B 2 316 ? -11.524 -23.289 -41.166 1.00 18.09  ?  316  THR B HG1    1 
ATOM   12043 H HG21   . THR B 2 316 ? -10.411 -22.997 -38.685 1.00 18.42  ?  316  THR B HG21   1 
ATOM   12044 H HG22   . THR B 2 316 ? -10.901 -24.299 -37.939 1.00 18.42  ?  316  THR B HG22   1 
ATOM   12045 H HG23   . THR B 2 316 ? -10.242 -24.409 -39.369 1.00 18.42  ?  316  THR B HG23   1 
ATOM   12046 N N      . GLY B 2 317 ? -14.591 -25.053 -41.368 1.00 17.35  ?  317  GLY B N      1 
ATOM   12047 C CA     . GLY B 2 317 ? -15.984 -25.159 -41.769 1.00 17.90  ?  317  GLY B CA     1 
ATOM   12048 C C      . GLY B 2 317 ? -16.611 -26.448 -41.283 1.00 16.89  ?  317  GLY B C      1 
ATOM   12049 O O      . GLY B 2 317 ? -17.784 -26.477 -40.905 1.00 19.37  ?  317  GLY B O      1 
ATOM   12050 H H      . GLY B 2 317 ? -14.031 -24.996 -42.018 1.00 20.82  ?  317  GLY B H      1 
ATOM   12051 H HA2    . GLY B 2 317 ? -16.484 -24.414 -41.401 1.00 21.48  ?  317  GLY B HA2    1 
ATOM   12052 H HA3    . GLY B 2 317 ? -16.045 -25.132 -42.737 1.00 21.48  ?  317  GLY B HA3    1 
ATOM   12053 N N      . GLU B 2 318 ? -15.827 -27.534 -41.269 1.00 18.65  ?  318  GLU B N      1 
ATOM   12054 C CA     . GLU B 2 318 ? -16.343 -28.829 -40.838 1.00 21.10  ?  318  GLU B CA     1 
ATOM   12055 C C      . GLU B 2 318 ? -16.312 -28.983 -39.318 1.00 17.80  ?  318  GLU B C      1 
ATOM   12056 O O      . GLU B 2 318 ? -17.254 -29.538 -38.732 1.00 20.43  ?  318  GLU B O      1 
ATOM   12057 C CB     . GLU B 2 318 ? -15.542 -29.942 -41.525 1.00 24.87  ?  318  GLU B CB     1 
ATOM   12058 C CG     . GLU B 2 318 ? -16.047 -31.330 -41.236 1.00 31.11  ?  318  GLU B CG     1 
ATOM   12059 C CD     . GLU B 2 318 ? -15.393 -32.386 -42.112 1.00 36.51  ?  318  GLU B CD     1 
ATOM   12060 O OE1    . GLU B 2 318 ? -14.522 -32.043 -42.952 1.00 35.22  ?  318  GLU B OE1    1 
ATOM   12061 O OE2    . GLU B 2 318 ? -15.769 -33.572 -41.954 1.00 39.37  -1 318  GLU B OE2    1 
ATOM   12062 H H      . GLU B 2 318 ? -15.000 -27.545 -41.503 1.00 22.37  ?  318  GLU B H      1 
ATOM   12063 H HA     . GLU B 2 318 ? -17.272 -28.910 -41.107 1.00 25.32  ?  318  GLU B HA     1 
ATOM   12064 H HB2    . GLU B 2 318 ? -15.584 -29.808 -42.485 1.00 29.84  ?  318  GLU B HB2    1 
ATOM   12065 H HB3    . GLU B 2 318 ? -14.622 -29.895 -41.223 1.00 29.84  ?  318  GLU B HB3    1 
ATOM   12066 H HG2    . GLU B 2 318 ? -15.859 -31.549 -40.310 1.00 37.32  ?  318  GLU B HG2    1 
ATOM   12067 H HG3    . GLU B 2 318 ? -17.004 -31.358 -41.395 1.00 37.32  ?  318  GLU B HG3    1 
ATOM   12068 N N      . PHE B 2 319 ? -15.262 -28.498 -38.663 1.00 17.50  ?  319  PHE B N      1 
ATOM   12069 C CA     . PHE B 2 319 ? -14.989 -28.858 -37.280 1.00 17.93  ?  319  PHE B CA     1 
ATOM   12070 C C      . PHE B 2 319 ? -15.045 -27.691 -36.301 1.00 18.93  ?  319  PHE B C      1 
ATOM   12071 O O      . PHE B 2 319 ? -14.993 -27.932 -35.082 1.00 21.66  ?  319  PHE B O      1 
ATOM   12072 C CB     . PHE B 2 319 ? -13.607 -29.531 -37.182 1.00 17.79  ?  319  PHE B CB     1 
ATOM   12073 C CG     . PHE B 2 319 ? -13.498 -30.790 -37.984 1.00 19.19  ?  319  PHE B CG     1 
ATOM   12074 C CD1    . PHE B 2 319 ? -14.354 -31.854 -37.743 1.00 20.53  ?  319  PHE B CD1    1 
ATOM   12075 C CD2    . PHE B 2 319 ? -12.543 -30.929 -38.966 1.00 22.34  ?  319  PHE B CD2    1 
ATOM   12076 C CE1    . PHE B 2 319 ? -14.258 -33.013 -38.477 1.00 21.02  ?  319  PHE B CE1    1 
ATOM   12077 C CE2    . PHE B 2 319 ? -12.451 -32.096 -39.706 1.00 21.57  ?  319  PHE B CE2    1 
ATOM   12078 C CZ     . PHE B 2 319 ? -13.304 -33.132 -39.459 1.00 20.53  ?  319  PHE B CZ     1 
ATOM   12079 H H      . PHE B 2 319 ? -14.690 -27.954 -39.003 1.00 20.99  ?  319  PHE B H      1 
ATOM   12080 H HA     . PHE B 2 319 ? -15.660 -29.495 -36.991 1.00 21.51  ?  319  PHE B HA     1 
ATOM   12081 H HB2    . PHE B 2 319 ? -12.934 -28.913 -37.506 1.00 21.35  ?  319  PHE B HB2    1 
ATOM   12082 H HB3    . PHE B 2 319 ? -13.433 -29.755 -36.254 1.00 21.35  ?  319  PHE B HB3    1 
ATOM   12083 H HD1    . PHE B 2 319 ? -15.000 -31.784 -37.077 1.00 24.63  ?  319  PHE B HD1    1 
ATOM   12084 H HD2    . PHE B 2 319 ? -11.953 -30.230 -39.135 1.00 26.80  ?  319  PHE B HD2    1 
ATOM   12085 H HE1    . PHE B 2 319 ? -14.840 -33.718 -38.308 1.00 25.22  ?  319  PHE B HE1    1 
ATOM   12086 H HE2    . PHE B 2 319 ? -11.806 -32.174 -40.372 1.00 25.88  ?  319  PHE B HE2    1 
ATOM   12087 H HZ     . PHE B 2 319 ? -13.241 -33.916 -39.954 1.00 24.63  ?  319  PHE B HZ     1 
ATOM   12088 N N      . GLY B 2 320 ? -15.141 -26.456 -36.787 1.00 16.94  ?  320  GLY B N      1 
ATOM   12089 C CA     . GLY B 2 320 ? -15.222 -25.292 -35.924 1.00 14.90  ?  320  GLY B CA     1 
ATOM   12090 C C      . GLY B 2 320 ? -13.877 -24.650 -35.637 1.00 15.30  ?  320  GLY B C      1 
ATOM   12091 O O      . GLY B 2 320 ? -12.863 -24.919 -36.297 1.00 15.36  ?  320  GLY B O      1 
ATOM   12092 H H      . GLY B 2 320 ? -15.162 -26.269 -37.626 1.00 20.32  ?  320  GLY B H      1 
ATOM   12093 H HA2    . GLY B 2 320 ? -15.788 -24.626 -36.345 1.00 17.88  ?  320  GLY B HA2    1 
ATOM   12094 H HA3    . GLY B 2 320 ? -15.617 -25.554 -35.078 1.00 17.88  ?  320  GLY B HA3    1 
ATOM   12095 N N      . PRO B 2 321 ? -13.855 -23.758 -34.664 1.00 14.88  ?  321  PRO B N      1 
ATOM   12096 C CA     . PRO B 2 321 ? -12.631 -22.996 -34.393 1.00 14.19  ?  321  PRO B CA     1 
ATOM   12097 C C      . PRO B 2 321 ? -11.410 -23.881 -34.186 1.00 14.10  ?  321  PRO B C      1 
ATOM   12098 O O      . PRO B 2 321 ? -11.472 -24.941 -33.552 1.00 16.26  ?  321  PRO B O      1 
ATOM   12099 C CB     . PRO B 2 321 ? -12.981 -22.220 -33.121 1.00 15.76  ?  321  PRO B CB     1 
ATOM   12100 C CG     . PRO B 2 321 ? -14.485 -22.077 -33.166 1.00 17.17  ?  321  PRO B CG     1 
ATOM   12101 C CD     . PRO B 2 321 ? -14.976 -23.361 -33.786 1.00 17.21  ?  321  PRO B CD     1 
ATOM   12102 H HA     . PRO B 2 321 ? -12.455 -22.388 -35.128 1.00 17.02  ?  321  PRO B HA     1 
ATOM   12103 H HB2    . PRO B 2 321 ? -12.701 -22.721 -32.338 1.00 18.91  ?  321  PRO B HB2    1 
ATOM   12104 H HB3    . PRO B 2 321 ? -12.547 -21.352 -33.131 1.00 18.91  ?  321  PRO B HB3    1 
ATOM   12105 H HG2    . PRO B 2 321 ? -14.835 -21.969 -32.268 1.00 20.60  ?  321  PRO B HG2    1 
ATOM   12106 H HG3    . PRO B 2 321 ? -14.729 -21.313 -33.711 1.00 20.60  ?  321  PRO B HG3    1 
ATOM   12107 H HD2    . PRO B 2 321 ? -15.138 -24.034 -33.106 1.00 20.65  ?  321  PRO B HD2    1 
ATOM   12108 H HD3    . PRO B 2 321 ? -15.784 -23.210 -34.302 1.00 20.65  ?  321  PRO B HD3    1 
ATOM   12109 N N      . ILE B 2 322 ? -10.276 -23.416 -34.689 1.00 13.55  ?  322  ILE B N      1 
ATOM   12110 C CA     . ILE B 2 322 ? -9.064  -24.225 -34.689 1.00 13.34  ?  322  ILE B CA     1 
ATOM   12111 C C      . ILE B 2 322 ? -8.476  -24.281 -33.278 1.00 11.41  ?  322  ILE B C      1 
ATOM   12112 O O      . ILE B 2 322 ? -8.366  -23.258 -32.580 1.00 13.08  ?  322  ILE B O      1 
ATOM   12113 C CB     . ILE B 2 322 ? -8.058  -23.713 -35.740 1.00 16.26  ?  322  ILE B CB     1 
ATOM   12114 C CG1    . ILE B 2 322 ? -6.926  -24.725 -35.888 1.00 19.67  ?  322  ILE B CG1    1 
ATOM   12115 C CG2    . ILE B 2 322 ? -7.558  -22.314 -35.375 1.00 17.51  ?  322  ILE B CG2    1 
ATOM   12116 C CD1    . ILE B 2 322 ? -6.478  -24.981 -37.249 1.00 23.46  ?  322  ILE B CD1    1 
ATOM   12117 H H      . ILE B 2 322 ? -10.181 -22.635 -35.037 1.00 16.25  ?  322  ILE B H      1 
ATOM   12118 H HA     . ILE B 2 322 ? -9.292  -25.137 -34.930 1.00 16.00  ?  322  ILE B HA     1 
ATOM   12119 H HB     . ILE B 2 322 ? -8.497  -23.629 -36.601 1.00 19.51  ?  322  ILE B HB     1 
ATOM   12120 H HG12   . ILE B 2 322 ? -6.160  -24.399 -35.390 1.00 23.60  ?  322  ILE B HG12   1 
ATOM   12121 H HG13   . ILE B 2 322 ? -7.226  -25.571 -35.520 1.00 23.60  ?  322  ILE B HG13   1 
ATOM   12122 H HG21   . ILE B 2 322 ? -7.006  -21.978 -36.098 1.00 21.01  ?  322  ILE B HG21   1 
ATOM   12123 H HG22   . ILE B 2 322 ? -8.322  -21.731 -35.243 1.00 21.01  ?  322  ILE B HG22   1 
ATOM   12124 H HG23   . ILE B 2 322 ? -7.037  -22.368 -34.559 1.00 21.01  ?  322  ILE B HG23   1 
ATOM   12125 H HD11   . ILE B 2 322 ? -5.772  -25.645 -37.229 1.00 28.15  ?  322  ILE B HD11   1 
ATOM   12126 H HD12   . ILE B 2 322 ? -7.226  -25.309 -37.771 1.00 28.15  ?  322  ILE B HD12   1 
ATOM   12127 H HD13   . ILE B 2 322 ? -6.144  -24.155 -37.632 1.00 28.15  ?  322  ILE B HD13   1 
ATOM   12128 N N      . GLY B 2 323 ? -8.128  -25.484 -32.848 1.00 12.99  ?  323  GLY B N      1 
ATOM   12129 C CA     . GLY B 2 323 ? -7.577  -25.730 -31.521 1.00 13.77  ?  323  GLY B CA     1 
ATOM   12130 C C      . GLY B 2 323 ? -6.110  -25.383 -31.412 1.00 12.00  ?  323  GLY B C      1 
ATOM   12131 O O      . GLY B 2 323 ? -5.266  -26.279 -31.295 1.00 11.46  ?  323  GLY B O      1 
ATOM   12132 H H      . GLY B 2 323 ? -8.202  -26.200 -33.319 1.00 15.58  ?  323  GLY B H      1 
ATOM   12133 H HA2    . GLY B 2 323 ? -8.063  -25.197 -30.872 1.00 16.53  ?  323  GLY B HA2    1 
ATOM   12134 H HA3    . GLY B 2 323 ? -7.684  -26.669 -31.301 1.00 16.53  ?  323  GLY B HA3    1 
ATOM   12135 N N      . HIS B 2 324 ? -5.812  -24.086 -31.462 1.00 12.85  ?  324  HIS B N      1 
ATOM   12136 C CA     . HIS B 2 324 ? -4.440  -23.605 -31.415 1.00 11.36  ?  324  HIS B CA     1 
ATOM   12137 C C      . HIS B 2 324 ? -4.409  -22.185 -30.879 1.00 12.25  ?  324  HIS B C      1 
ATOM   12138 O O      . HIS B 2 324 ? -5.201  -21.337 -31.293 1.00 13.58  ?  324  HIS B O      1 
ATOM   12139 C CB     . HIS B 2 324 ? -3.776  -23.648 -32.790 1.00 12.18  ?  324  HIS B CB     1 
ATOM   12140 C CG     . HIS B 2 324 ? -2.306  -23.405 -32.734 1.00 11.80  ?  324  HIS B CG     1 
ATOM   12141 N ND1    . HIS B 2 324 ? -1.469  -24.173 -31.949 1.00 12.48  ?  324  HIS B ND1    1 
ATOM   12142 C CD2    . HIS B 2 324 ? -1.523  -22.474 -33.329 1.00 10.95  ?  324  HIS B CD2    1 
ATOM   12143 C CE1    . HIS B 2 324 ? -0.230  -23.721 -32.077 1.00 12.16  ?  324  HIS B CE1    1 
ATOM   12144 N NE2    . HIS B 2 324 ? -0.238  -22.697 -32.913 1.00 12.38  ?  324  HIS B NE2    1 
ATOM   12145 H H      . HIS B 2 324 ? -6.397  -23.459 -31.524 1.00 15.41  ?  324  HIS B H      1 
ATOM   12146 H HA     . HIS B 2 324 ? -3.940  -24.173 -30.809 1.00 13.63  ?  324  HIS B HA     1 
ATOM   12147 H HB2    . HIS B 2 324 ? -3.921  -24.523 -33.183 1.00 14.62  ?  324  HIS B HB2    1 
ATOM   12148 H HB3    . HIS B 2 324 ? -4.172  -22.963 -33.352 1.00 14.62  ?  324  HIS B HB3    1 
ATOM   12149 H HD2    . HIS B 2 324 ? -1.806  -21.806 -33.912 1.00 13.13  ?  324  HIS B HD2    1 
ATOM   12150 H HE1    . HIS B 2 324 ? 0.520   -24.067 -31.650 1.00 14.58  ?  324  HIS B HE1    1 
ATOM   12151 H HE2    . HIS B 2 324 ? 0.452   -22.244 -33.155 1.00 14.85  ?  324  HIS B HE2    1 
ATOM   12152 N N      . GLY B 2 325 ? -3.497  -21.934 -29.938 1.00 12.40  ?  325  GLY B N      1 
ATOM   12153 C CA     . GLY B 2 325 ? -3.301  -20.569 -29.489 1.00 12.32  ?  325  GLY B CA     1 
ATOM   12154 C C      . GLY B 2 325 ? -2.192  -20.473 -28.462 1.00 11.82  ?  325  GLY B C      1 
ATOM   12155 O O      . GLY B 2 325 ? -1.954  -21.423 -27.700 1.00 13.86  ?  325  GLY B O      1 
ATOM   12156 H H      . GLY B 2 325 ? -2.998  -22.522 -29.559 1.00 14.87  ?  325  GLY B H      1 
ATOM   12157 H HA2    . GLY B 2 325 ? -3.069  -20.009 -30.247 1.00 14.78  ?  325  GLY B HA2    1 
ATOM   12158 H HA3    . GLY B 2 325 ? -4.121  -20.237 -29.091 1.00 14.78  ?  325  GLY B HA3    1 
ATOM   12159 N N      . TRP B 2 326 ? -1.469  -19.355 -28.472 1.00 12.59  ?  326  TRP B N      1 
ATOM   12160 C CA     . TRP B 2 326 ? -0.601  -18.989 -27.374 1.00 12.02  ?  326  TRP B CA     1 
ATOM   12161 C C      . TRP B 2 326 ? -1.158  -17.736 -26.700 1.00 12.36  ?  326  TRP B C      1 
ATOM   12162 O O      . TRP B 2 326 ? -1.607  -16.812 -27.381 1.00 13.83  ?  326  TRP B O      1 
ATOM   12163 C CB     . TRP B 2 326 ? 0.804   -18.620 -27.837 1.00 12.84  ?  326  TRP B CB     1 
ATOM   12164 C CG     . TRP B 2 326 ? 1.425   -19.417 -28.958 1.00 11.26  ?  326  TRP B CG     1 
ATOM   12165 C CD1    . TRP B 2 326 ? 1.796   -18.927 -30.173 1.00 12.31  ?  326  TRP B CD1    1 
ATOM   12166 C CD2    . TRP B 2 326 ? 1.821   -20.798 -28.946 1.00 10.94  ?  326  TRP B CD2    1 
ATOM   12167 N NE1    . TRP B 2 326 ? 2.367   -19.914 -30.930 1.00 11.85  ?  326  TRP B NE1    1 
ATOM   12168 C CE2    . TRP B 2 326 ? 2.397   -21.077 -30.207 1.00 11.91  ?  326  TRP B CE2    1 
ATOM   12169 C CE3    . TRP B 2 326 ? 1.742   -21.827 -28.001 1.00 12.03  ?  326  TRP B CE3    1 
ATOM   12170 C CZ2    . TRP B 2 326 ? 2.888   -22.336 -30.539 1.00 12.26  ?  326  TRP B CZ2    1 
ATOM   12171 C CZ3    . TRP B 2 326 ? 2.221   -23.081 -28.328 1.00 12.21  ?  326  TRP B CZ3    1 
ATOM   12172 C CH2    . TRP B 2 326 ? 2.822   -23.309 -29.592 1.00 12.02  ?  326  TRP B CH2    1 
ATOM   12173 H H      . TRP B 2 326 ? -1.472  -18.789 -29.119 1.00 15.11  ?  326  TRP B H      1 
ATOM   12174 H HA     . TRP B 2 326 ? -0.556  -19.744 -26.767 1.00 14.42  ?  326  TRP B HA     1 
ATOM   12175 H HB2    . TRP B 2 326 ? 0.782   -17.697 -28.134 1.00 15.40  ?  326  TRP B HB2    1 
ATOM   12176 H HB3    . TRP B 2 326 ? 1.397   -18.709 -27.074 1.00 15.40  ?  326  TRP B HB3    1 
ATOM   12177 H HD1    . TRP B 2 326 ? 1.678   -18.047 -30.450 1.00 14.76  ?  326  TRP B HD1    1 
ATOM   12178 H HE1    . TRP B 2 326 ? 2.660   -19.819 -31.733 1.00 14.21  ?  326  TRP B HE1    1 
ATOM   12179 H HE3    . TRP B 2 326 ? 1.372   -21.669 -27.163 1.00 14.43  ?  326  TRP B HE3    1 
ATOM   12180 H HZ2    . TRP B 2 326 ? 3.249   -22.506 -31.380 1.00 14.71  ?  326  TRP B HZ2    1 
ATOM   12181 H HZ3    . TRP B 2 326 ? 2.150   -23.778 -27.717 1.00 14.65  ?  326  TRP B HZ3    1 
ATOM   12182 H HH2    . TRP B 2 326 ? 3.180   -24.147 -29.778 1.00 14.42  ?  326  TRP B HH2    1 
ATOM   12183 N N      . THR B 2 327 ? -1.072  -17.681 -25.372 1.00 11.27  ?  327  THR B N      1 
ATOM   12184 C CA     . THR B 2 327 ? -1.643  -16.551 -24.633 1.00 11.21  ?  327  THR B CA     1 
ATOM   12185 C C      . THR B 2 327 ? -1.181  -15.215 -25.192 1.00 11.44  ?  327  THR B C      1 
ATOM   12186 O O      . THR B 2 327 ? -1.979  -14.280 -25.331 1.00 12.62  ?  327  THR B O      1 
ATOM   12187 C CB     . THR B 2 327 ? -1.206  -16.633 -23.175 1.00 12.95  ?  327  THR B CB     1 
ATOM   12188 O OG1    . THR B 2 327 ? -1.662  -17.850 -22.616 1.00 16.86  ?  327  THR B OG1    1 
ATOM   12189 C CG2    . THR B 2 327 ? -1.741  -15.489 -22.343 1.00 14.00  ?  327  THR B CG2    1 
ATOM   12190 H H      . THR B 2 327 ? -0.694  -18.274 -24.877 1.00 13.52  ?  327  THR B H      1 
ATOM   12191 H HA     . THR B 2 327 ? -2.609  -16.603 -24.700 1.00 13.45  ?  327  THR B HA     1 
ATOM   12192 H HB     . THR B 2 327 ? -0.238  -16.582 -23.149 1.00 15.54  ?  327  THR B HB     1 
ATOM   12193 H HG1    . THR B 2 327 ? -1.306  -18.500 -23.012 1.00 20.23  ?  327  THR B HG1    1 
ATOM   12194 H HG21   . THR B 2 327 ? -1.616  -15.678 -21.399 1.00 16.79  ?  327  THR B HG21   1 
ATOM   12195 H HG22   . THR B 2 327 ? -1.273  -14.670 -22.565 1.00 16.79  ?  327  THR B HG22   1 
ATOM   12196 H HG23   . THR B 2 327 ? -2.688  -15.367 -22.516 1.00 16.79  ?  327  THR B HG23   1 
ATOM   12197 N N      . TYR B 2 328 ? 0.106   -15.116 -25.543 1.00 11.85  ?  328  TYR B N      1 
ATOM   12198 C CA     . TYR B 2 328 ? 0.694   -13.853 -25.984 1.00 11.48  ?  328  TYR B CA     1 
ATOM   12199 C C      . TYR B 2 328 ? 0.709   -13.676 -27.494 1.00 14.11  ?  328  TYR B C      1 
ATOM   12200 O O      . TYR B 2 328 ? 1.311   -12.718 -27.999 1.00 13.40  ?  328  TYR B O      1 
ATOM   12201 C CB     . TYR B 2 328 ? 2.092   -13.700 -25.385 1.00 13.72  ?  328  TYR B CB     1 
ATOM   12202 C CG     . TYR B 2 328 ? 2.118   -13.657 -23.866 1.00 11.51  ?  328  TYR B CG     1 
ATOM   12203 C CD1    . TYR B 2 328 ? 1.151   -12.987 -23.156 1.00 13.77  ?  328  TYR B CD1    1 
ATOM   12204 C CD2    . TYR B 2 328 ? 3.121   -14.301 -23.157 1.00 13.56  ?  328  TYR B CD2    1 
ATOM   12205 C CE1    . TYR B 2 328 ? 1.174   -12.945 -21.779 1.00 15.44  ?  328  TYR B CE1    1 
ATOM   12206 C CE2    . TYR B 2 328 ? 3.161   -14.276 -21.759 1.00 13.45  ?  328  TYR B CE2    1 
ATOM   12207 C CZ     . TYR B 2 328 ? 2.178   -13.578 -21.086 1.00 14.10  ?  328  TYR B CZ     1 
ATOM   12208 O OH     . TYR B 2 328 ? 2.184   -13.489 -19.717 1.00 16.29  ?  328  TYR B OH     1 
ATOM   12209 H H      . TYR B 2 328 ? 0.659   -15.774 -25.533 1.00 14.22  ?  328  TYR B H      1 
ATOM   12210 H HA     . TYR B 2 328 ? 0.154   -13.124 -25.642 1.00 13.77  ?  328  TYR B HA     1 
ATOM   12211 H HB2    . TYR B 2 328 ? 2.634   -14.453 -25.668 1.00 16.46  ?  328  TYR B HB2    1 
ATOM   12212 H HB3    . TYR B 2 328 ? 2.479   -12.872 -25.710 1.00 16.46  ?  328  TYR B HB3    1 
ATOM   12213 H HD1    . TYR B 2 328 ? 0.466   -12.555 -23.613 1.00 16.52  ?  328  TYR B HD1    1 
ATOM   12214 H HD2    . TYR B 2 328 ? 3.783   -14.760 -23.622 1.00 16.27  ?  328  TYR B HD2    1 
ATOM   12215 H HE1    . TYR B 2 328 ? 0.509   -12.487 -21.317 1.00 18.52  ?  328  TYR B HE1    1 
ATOM   12216 H HE2    . TYR B 2 328 ? 3.832   -14.720 -21.294 1.00 16.13  ?  328  TYR B HE2    1 
ATOM   12217 H HH     . TYR B 2 328 ? 1.586   -12.957 -19.461 1.00 19.54  ?  328  TYR B HH     1 
ATOM   12218 N N      . SER B 2 329 ? 0.055   -14.567 -28.235 1.00 13.48  ?  329  SER B N      1 
ATOM   12219 C CA     . SER B 2 329 ? -0.033  -14.420 -29.683 1.00 13.37  ?  329  SER B CA     1 
ATOM   12220 C C      . SER B 2 329 ? -0.556  -13.038 -30.062 1.00 14.00  ?  329  SER B C      1 
ATOM   12221 O O      . SER B 2 329 ? -1.608  -12.602 -29.595 1.00 13.36  ?  329  SER B O      1 
ATOM   12222 C CB     . SER B 2 329 ? -0.967  -15.493 -30.239 1.00 11.85  ?  329  SER B CB     1 
ATOM   12223 O OG     . SER B 2 329 ? -1.144  -15.335 -31.640 1.00 13.20  ?  329  SER B OG     1 
ATOM   12224 H H      . SER B 2 329 ? -0.345  -15.262 -27.925 1.00 16.17  ?  329  SER B H      1 
ATOM   12225 H HA     . SER B 2 329 ? 0.849   -14.528 -30.073 1.00 16.04  ?  329  SER B HA     1 
ATOM   12226 H HB2    . SER B 2 329 ? -0.582  -16.366 -30.067 1.00 14.21  ?  329  SER B HB2    1 
ATOM   12227 H HB3    . SER B 2 329 ? -1.829  -15.418 -29.802 1.00 14.21  ?  329  SER B HB3    1 
ATOM   12228 H HG     . SER B 2 329 ? -0.407  -15.417 -32.034 1.00 15.83  ?  329  SER B HG     1 
ATOM   12229 N N      . GLY B 2 330 ? 0.188   -12.352 -30.923 1.00 12.04  ?  330  GLY B N      1 
ATOM   12230 C CA     . GLY B 2 330 ? -0.238  -11.073 -31.425 1.00 12.73  ?  330  GLY B CA     1 
ATOM   12231 C C      . GLY B 2 330 ? 0.005   -9.910  -30.499 1.00 13.26  ?  330  GLY B C      1 
ATOM   12232 O O      . GLY B 2 330 ? -0.560  -8.843  -30.733 1.00 13.33  ?  330  GLY B O      1 
ATOM   12233 H H      . GLY B 2 330 ? 0.947   -12.615 -31.230 1.00 14.44  ?  330  GLY B H      1 
ATOM   12234 H HA2    . GLY B 2 330 ? 0.233   -10.893 -32.254 1.00 15.28  ?  330  GLY B HA2    1 
ATOM   12235 H HA3    . GLY B 2 330 ? -1.190  -11.112 -31.605 1.00 15.28  ?  330  GLY B HA3    1 
ATOM   12236 N N      . HIS B 2 331 ? 0.836   -10.083 -29.476 1.00 14.06  ?  331  HIS B N      1 
ATOM   12237 C CA     . HIS B 2 331 ? 1.107   -9.046  -28.480 1.00 15.00  ?  331  HIS B CA     1 
ATOM   12238 C C      . HIS B 2 331 ? 1.350   -7.682  -29.106 1.00 13.71  ?  331  HIS B C      1 
ATOM   12239 O O      . HIS B 2 331 ? 2.204   -7.526  -29.975 1.00 14.15  ?  331  HIS B O      1 
ATOM   12240 C CB     . HIS B 2 331 ? 2.339   -9.484  -27.684 1.00 14.22  ?  331  HIS B CB     1 
ATOM   12241 C CG     . HIS B 2 331 ? 2.519   -8.771  -26.388 1.00 12.99  ?  331  HIS B CG     1 
ATOM   12242 N ND1    . HIS B 2 331 ? 3.062   -7.508  -26.301 1.00 13.06  ?  331  HIS B ND1    1 
ATOM   12243 C CD2    . HIS B 2 331 ? 2.237   -9.152  -25.121 1.00 14.57  ?  331  HIS B CD2    1 
ATOM   12244 C CE1    . HIS B 2 331 ? 3.074   -7.124  -25.037 1.00 14.66  ?  331  HIS B CE1    1 
ATOM   12245 N NE2    . HIS B 2 331 ? 2.593   -8.111  -24.296 1.00 14.82  ?  331  HIS B NE2    1 
ATOM   12246 H H      . HIS B 2 331 ? 1.269   -10.811 -29.330 1.00 16.87  ?  331  HIS B H      1 
ATOM   12247 H HA     . HIS B 2 331 ? 0.339   -8.948  -27.896 1.00 18.00  ?  331  HIS B HA     1 
ATOM   12248 H HB2    . HIS B 2 331 ? 2.262   -10.431 -27.490 1.00 17.06  ?  331  HIS B HB2    1 
ATOM   12249 H HB3    . HIS B 2 331 ? 3.130   -9.319  -28.222 1.00 17.06  ?  331  HIS B HB3    1 
ATOM   12250 H HD2    . HIS B 2 331 ? 1.870   -9.965  -24.858 1.00 17.48  ?  331  HIS B HD2    1 
ATOM   12251 H HE1    . HIS B 2 331 ? 3.371   -6.301  -24.721 1.00 17.59  ?  331  HIS B HE1    1 
ATOM   12252 H HE2    . HIS B 2 331 ? 2.516   -8.102  -23.440 1.00 17.78  ?  331  HIS B HE2    1 
ATOM   12253 N N      . ALA B 2 332 ? 0.606   -6.678  -28.628 1.00 12.59  ?  332  ALA B N      1 
ATOM   12254 C CA     . ALA B 2 332 ? 0.596   -5.391  -29.313 1.00 11.65  ?  332  ALA B CA     1 
ATOM   12255 C C      . ALA B 2 332 ? 1.956   -4.697  -29.270 1.00 14.46  ?  332  ALA B C      1 
ATOM   12256 O O      . ALA B 2 332 ? 2.315   -3.980  -30.207 1.00 14.30  ?  332  ALA B O      1 
ATOM   12257 C CB     . ALA B 2 332 ? -0.490  -4.481  -28.733 1.00 15.19  ?  332  ALA B CB     1 
ATOM   12258 H H      . ALA B 2 332 ? 0.111   -6.717  -27.926 1.00 15.10  ?  332  ALA B H      1 
ATOM   12259 H HA     . ALA B 2 332 ? 0.382   -5.552  -30.245 1.00 13.97  ?  332  ALA B HA     1 
ATOM   12260 H HB1    . ALA B 2 332 ? -0.531  -3.665  -29.256 1.00 18.22  ?  332  ALA B HB1    1 
ATOM   12261 H HB2    . ALA B 2 332 ? -1.343  -4.942  -28.772 1.00 18.22  ?  332  ALA B HB2    1 
ATOM   12262 H HB3    . ALA B 2 332 ? -0.269  -4.272  -27.812 1.00 18.22  ?  332  ALA B HB3    1 
ATOM   12263 N N      . LEU B 2 333 ? 2.714   -4.871  -28.188 1.00 14.10  ?  333  LEU B N      1 
ATOM   12264 C CA     . LEU B 2 333 ? 4.037   -4.246  -28.139 1.00 14.17  ?  333  LEU B CA     1 
ATOM   12265 C C      . LEU B 2 333 ? 4.995   -4.953  -29.086 1.00 15.07  ?  333  LEU B C      1 
ATOM   12266 O O      . LEU B 2 333 ? 5.853   -4.319  -29.711 1.00 15.14  ?  333  LEU B O      1 
ATOM   12267 C CB     . LEU B 2 333 ? 4.571   -4.268  -26.715 1.00 13.16  ?  333  LEU B CB     1 
ATOM   12268 C CG     . LEU B 2 333 ? 3.709   -3.523  -25.693 1.00 14.49  ?  333  LEU B CG     1 
ATOM   12269 C CD1    . LEU B 2 333 ? 4.459   -3.385  -24.365 1.00 16.68  ?  333  LEU B CD1    1 
ATOM   12270 C CD2    . LEU B 2 333 ? 3.255   -2.164  -26.187 1.00 15.40  ?  333  LEU B CD2    1 
ATOM   12271 H H      . LEU B 2 333 ? 2.498   -5.329  -27.493 1.00 16.92  ?  333  LEU B H      1 
ATOM   12272 H HA     . LEU B 2 333 ? 3.965   -3.317  -28.411 1.00 17.00  ?  333  LEU B HA     1 
ATOM   12273 H HB2    . LEU B 2 333 ? 4.635   -5.192  -26.426 1.00 15.79  ?  333  LEU B HB2    1 
ATOM   12274 H HB3    . LEU B 2 333 ? 5.450   -3.858  -26.710 1.00 15.79  ?  333  LEU B HB3    1 
ATOM   12275 H HG     . LEU B 2 333 ? 2.904   -4.047  -25.551 1.00 17.39  ?  333  LEU B HG     1 
ATOM   12276 H HD11   . LEU B 2 333 ? 3.929   -2.848  -23.756 1.00 20.01  ?  333  LEU B HD11   1 
ATOM   12277 H HD12   . LEU B 2 333 ? 4.601   -4.268  -23.990 1.00 20.01  ?  333  LEU B HD12   1 
ATOM   12278 H HD13   . LEU B 2 333 ? 5.313   -2.954  -24.528 1.00 20.01  ?  333  LEU B HD13   1 
ATOM   12279 H HD21   . LEU B 2 333 ? 2.875   -1.669  -25.445 1.00 18.48  ?  333  LEU B HD21   1 
ATOM   12280 H HD22   . LEU B 2 333 ? 4.020   -1.687  -26.545 1.00 18.48  ?  333  LEU B HD22   1 
ATOM   12281 H HD23   . LEU B 2 333 ? 2.588   -2.287  -26.880 1.00 18.48  ?  333  LEU B HD23   1 
ATOM   12282 N N      . GLY B 2 334 ? 4.844   -6.266  -29.233 1.00 15.41  ?  334  GLY B N      1 
ATOM   12283 C CA     . GLY B 2 334 ? 5.667   -6.969  -30.203 1.00 15.85  ?  334  GLY B CA     1 
ATOM   12284 C C      . GLY B 2 334 ? 5.368   -6.511  -31.612 1.00 15.63  ?  334  GLY B C      1 
ATOM   12285 O O      . GLY B 2 334 ? 6.278   -6.273  -32.411 1.00 15.54  ?  334  GLY B O      1 
ATOM   12286 H H      . GLY B 2 334 ? 4.289   -6.759  -28.798 1.00 18.49  ?  334  GLY B H      1 
ATOM   12287 H HA2    . GLY B 2 334 ? 6.604   -6.804  -30.015 1.00 19.01  ?  334  GLY B HA2    1 
ATOM   12288 H HA3    . GLY B 2 334 ? 5.496   -7.922  -30.144 1.00 19.01  ?  334  GLY B HA3    1 
ATOM   12289 N N      . CYS B 2 335 ? 4.085   -6.338  -31.922 1.00 14.14  ?  335  CYS B N      1 
ATOM   12290 C CA     . CYS B 2 335 ? 3.708   -5.903  -33.265 1.00 13.43  ?  335  CYS B CA     1 
ATOM   12291 C C      . CYS B 2 335 ? 4.104   -4.459  -33.510 1.00 15.04  ?  335  CYS B C      1 
ATOM   12292 O O      . CYS B 2 335 ? 4.502   -4.112  -34.624 1.00 16.12  ?  335  CYS B O      1 
ATOM   12293 C CB     . CYS B 2 335 ? 2.212   -6.122  -33.463 1.00 14.06  ?  335  CYS B CB     1 
ATOM   12294 S SG     . CYS B 2 335 ? 1.754   -7.901  -33.537 1.00 15.23  ?  335  CYS B SG     1 
ATOM   12295 H H      . CYS B 2 335 ? 3.424   -6.463  -31.387 1.00 16.96  ?  335  CYS B H      1 
ATOM   12296 H HA     . CYS B 2 335 ? 4.176   -6.438  -33.926 1.00 16.11  ?  335  CYS B HA     1 
ATOM   12297 H HB2    . CYS B 2 335 ? 1.733   -5.720  -32.721 1.00 16.86  ?  335  CYS B HB2    1 
ATOM   12298 H HB3    . CYS B 2 335 ? 1.940   -5.707  -34.297 1.00 16.86  ?  335  CYS B HB3    1 
ATOM   12299 H HG     . CYS B 2 335 ? 0.593   -8.018  -33.256 1.00 18.28  ?  335  CYS B HG     1 
ATOM   12300 N N      . ALA B 2 336 ? 4.007   -3.608  -32.489 1.00 15.67  ?  336  ALA B N      1 
ATOM   12301 C CA     . ALA B 2 336 ? 4.487   -2.241  -32.645 1.00 14.07  ?  336  ALA B CA     1 
ATOM   12302 C C      . ALA B 2 336 ? 5.980   -2.207  -32.966 1.00 15.84  ?  336  ALA B C      1 
ATOM   12303 O O      . ALA B 2 336 ? 6.419   -1.429  -33.824 1.00 16.42  ?  336  ALA B O      1 
ATOM   12304 C CB     . ALA B 2 336 ? 4.169   -1.415  -31.400 1.00 14.95  ?  336  ALA B CB     1 
ATOM   12305 H H      . ALA B 2 336 ? 3.677   -3.791  -31.717 1.00 18.80  ?  336  ALA B H      1 
ATOM   12306 H HA     . ALA B 2 336 ? 4.018   -1.831  -33.389 1.00 16.88  ?  336  ALA B HA     1 
ATOM   12307 H HB1    . ALA B 2 336 ? 4.421   -0.492  -31.560 1.00 17.93  ?  336  ALA B HB1    1 
ATOM   12308 H HB2    . ALA B 2 336 ? 3.218   -1.471  -31.219 1.00 17.93  ?  336  ALA B HB2    1 
ATOM   12309 H HB3    . ALA B 2 336 ? 4.670   -1.770  -30.650 1.00 17.93  ?  336  ALA B HB3    1 
ATOM   12310 N N      . ALA B 2 337 ? 6.782   -3.023  -32.270 1.00 15.57  ?  337  ALA B N      1 
ATOM   12311 C CA     . ALA B 2 337 ? 8.210   -3.079  -32.585 1.00 13.66  ?  337  ALA B CA     1 
ATOM   12312 C C      . ALA B 2 337 ? 8.436   -3.602  -33.997 1.00 13.62  ?  337  ALA B C      1 
ATOM   12313 O O      . ALA B 2 337 ? 9.337   -3.136  -34.701 1.00 15.92  ?  337  ALA B O      1 
ATOM   12314 C CB     . ALA B 2 337 ? 8.912   -3.976  -31.578 1.00 15.26  ?  337  ALA B CB     1 
ATOM   12315 H H      . ALA B 2 337 ? 6.532   -3.539  -31.629 1.00 18.68  ?  337  ALA B H      1 
ATOM   12316 H HA     . ALA B 2 337 ? 8.588   -2.188  -32.527 1.00 16.38  ?  337  ALA B HA     1 
ATOM   12317 H HB1    . ALA B 2 337 ? 9.859   -4.003  -31.785 1.00 18.31  ?  337  ALA B HB1    1 
ATOM   12318 H HB2    . ALA B 2 337 ? 8.778   -3.615  -30.687 1.00 18.31  ?  337  ALA B HB2    1 
ATOM   12319 H HB3    . ALA B 2 337 ? 8.535   -4.868  -31.633 1.00 18.31  ?  337  ALA B HB3    1 
ATOM   12320 N N      . GLY B 2 338 ? 7.643   -4.595  -34.411 1.00 13.29  ?  338  GLY B N      1 
ATOM   12321 C CA     . GLY B 2 338 ? 7.757   -5.115  -35.764 1.00 14.72  ?  338  GLY B CA     1 
ATOM   12322 C C      . GLY B 2 338 ? 7.537   -4.034  -36.802 1.00 16.46  ?  338  GLY B C      1 
ATOM   12323 O O      . GLY B 2 338 ? 8.316   -3.893  -37.747 1.00 16.19  ?  338  GLY B O      1 
ATOM   12324 H H      . GLY B 2 338 ? 7.039   -4.979  -33.933 1.00 15.94  ?  338  GLY B H      1 
ATOM   12325 H HA2    . GLY B 2 338 ? 8.642   -5.491  -35.892 1.00 17.66  ?  338  GLY B HA2    1 
ATOM   12326 H HA3    . GLY B 2 338 ? 7.096   -5.812  -35.899 1.00 17.66  ?  338  GLY B HA3    1 
ATOM   12327 N N      . LEU B 2 339 ? 6.493   -3.227  -36.612 1.00 15.99  ?  339  LEU B N      1 
ATOM   12328 C CA     . LEU B 2 339 ? 6.198   -2.157  -37.560 1.00 16.53  ?  339  LEU B CA     1 
ATOM   12329 C C      . LEU B 2 339 ? 7.340   -1.145  -37.619 1.00 16.37  ?  339  LEU B C      1 
ATOM   12330 O O      . LEU B 2 339 ? 7.752   -0.707  -38.695 1.00 17.71  ?  339  LEU B O      1 
ATOM   12331 C CB     . LEU B 2 339 ? 4.894   -1.460  -37.173 1.00 16.38  ?  339  LEU B CB     1 
ATOM   12332 C CG     . LEU B 2 339 ? 3.637   -2.269  -37.455 1.00 18.19  ?  339  LEU B CG     1 
ATOM   12333 C CD1    . LEU B 2 339 ? 2.464   -1.626  -36.763 1.00 19.69  ?  339  LEU B CD1    1 
ATOM   12334 C CD2    . LEU B 2 339 ? 3.386   -2.388  -38.954 1.00 17.49  ?  339  LEU B CD2    1 
ATOM   12335 H H      . LEU B 2 339 ? 5.946   -3.276  -35.951 1.00 19.19  ?  339  LEU B H      1 
ATOM   12336 H HA     . LEU B 2 339 ? 6.086   -2.545  -38.442 1.00 19.83  ?  339  LEU B HA     1 
ATOM   12337 H HB2    . LEU B 2 339 ? 4.915   -1.273  -36.222 1.00 19.66  ?  339  LEU B HB2    1 
ATOM   12338 H HB3    . LEU B 2 339 ? 4.827   -0.631  -37.673 1.00 19.66  ?  339  LEU B HB3    1 
ATOM   12339 H HG     . LEU B 2 339 ? 3.747   -3.169  -37.113 1.00 21.83  ?  339  LEU B HG     1 
ATOM   12340 H HD11   . LEU B 2 339 ? 1.668   -2.151  -36.938 1.00 23.63  ?  339  LEU B HD11   1 
ATOM   12341 H HD12   . LEU B 2 339 ? 2.638   -1.595  -35.809 1.00 23.63  ?  339  LEU B HD12   1 
ATOM   12342 H HD13   . LEU B 2 339 ? 2.349   -0.726  -37.107 1.00 23.63  ?  339  LEU B HD13   1 
ATOM   12343 H HD21   . LEU B 2 339 ? 2.513   -2.786  -39.098 1.00 20.99  ?  339  LEU B HD21   1 
ATOM   12344 H HD22   . LEU B 2 339 ? 3.415   -1.503  -39.351 1.00 20.99  ?  339  LEU B HD22   1 
ATOM   12345 H HD23   . LEU B 2 339 ? 4.074   -2.948  -39.346 1.00 20.99  ?  339  LEU B HD23   1 
ATOM   12346 N N      . ALA B 2 340 ? 7.854   -0.740  -36.461 1.00 14.95  ?  340  ALA B N      1 
ATOM   12347 C CA     . ALA B 2 340 ? 8.940   0.236   -36.445 1.00 15.91  ?  340  ALA B CA     1 
ATOM   12348 C C      . ALA B 2 340 ? 10.187  -0.346  -37.096 1.00 16.70  ?  340  ALA B C      1 
ATOM   12349 O O      . ALA B 2 340 ? 10.875  0.326   -37.868 1.00 16.30  ?  340  ALA B O      1 
ATOM   12350 C CB     . ALA B 2 340 ? 9.220   0.663   -35.006 1.00 16.86  ?  340  ALA B CB     1 
ATOM   12351 H H      . ALA B 2 340 ? 7.599   -1.007  -35.684 1.00 17.93  ?  340  ALA B H      1 
ATOM   12352 H HA     . ALA B 2 340 ? 8.682   1.026   -36.945 1.00 19.08  ?  340  ALA B HA     1 
ATOM   12353 H HB1    . ALA B 2 340 ? 9.910   1.345   -35.008 1.00 20.22  ?  340  ALA B HB1    1 
ATOM   12354 H HB2    . ALA B 2 340 ? 8.405   1.018   -34.618 1.00 20.22  ?  340  ALA B HB2    1 
ATOM   12355 H HB3    . ALA B 2 340 ? 9.519   -0.108  -34.500 1.00 20.22  ?  340  ALA B HB3    1 
ATOM   12356 N N      . ASN B 2 341 ? 10.474  -1.613  -36.817 1.00 17.16  ?  341  ASN B N      1 
ATOM   12357 C CA     . ASN B 2 341 ? 11.627  -2.279  -37.415 1.00 17.00  ?  341  ASN B CA     1 
ATOM   12358 C C      . ASN B 2 341 ? 11.513  -2.332  -38.935 1.00 17.38  ?  341  ASN B C      1 
ATOM   12359 O O      . ASN B 2 341 ? 12.449  -1.968  -39.651 1.00 17.25  ?  341  ASN B O      1 
ATOM   12360 C CB     . ASN B 2 341 ? 11.725  -3.671  -36.794 1.00 15.75  ?  341  ASN B CB     1 
ATOM   12361 C CG     . ASN B 2 341 ? 12.838  -4.508  -37.376 1.00 15.49  ?  341  ASN B CG     1 
ATOM   12362 O OD1    . ASN B 2 341 ? 14.030  -4.217  -37.198 1.00 16.18  ?  341  ASN B OD1    1 
ATOM   12363 N ND2    . ASN B 2 341 ? 12.455  -5.560  -38.058 1.00 16.37  ?  341  ASN B ND2    1 
ATOM   12364 H H      . ASN B 2 341 ? 10.019  -2.113  -36.286 1.00 20.59  ?  341  ASN B H      1 
ATOM   12365 H HA     . ASN B 2 341 ? 12.444  -1.792  -37.226 1.00 20.40  ?  341  ASN B HA     1 
ATOM   12366 H HB2    . ASN B 2 341 ? 11.888  -3.580  -35.843 1.00 18.89  ?  341  ASN B HB2    1 
ATOM   12367 H HB3    . ASN B 2 341 ? 10.890  -4.141  -36.944 1.00 18.89  ?  341  ASN B HB3    1 
ATOM   12368 H HD21   . ASN B 2 341 ? 13.041  -6.078  -38.415 1.00 19.64  ?  341  ASN B HD21   1 
ATOM   12369 H HD22   . ASN B 2 341 ? 11.617  -5.732  -38.148 1.00 19.64  ?  341  ASN B HD22   1 
ATOM   12370 N N      . LEU B 2 342 ? 10.372  -2.786  -39.450 1.00 17.76  ?  342  LEU B N      1 
ATOM   12371 C CA     . LEU B 2 342 ? 10.207  -2.894  -40.897 1.00 16.61  ?  342  LEU B CA     1 
ATOM   12372 C C      . LEU B 2 342 ? 10.268  -1.529  -41.565 1.00 17.98  ?  342  LEU B C      1 
ATOM   12373 O O      . LEU B 2 342 ? 10.817  -1.394  -42.669 1.00 17.96  ?  342  LEU B O      1 
ATOM   12374 C CB     . LEU B 2 342 ? 8.895   -3.598  -41.226 1.00 17.27  ?  342  LEU B CB     1 
ATOM   12375 C CG     . LEU B 2 342 ? 8.796   -5.061  -40.800 1.00 20.17  ?  342  LEU B CG     1 
ATOM   12376 C CD1    . LEU B 2 342 ? 7.525   -5.681  -41.352 1.00 20.13  ?  342  LEU B CD1    1 
ATOM   12377 C CD2    . LEU B 2 342 ? 10.000  -5.852  -41.266 1.00 20.96  ?  342  LEU B CD2    1 
ATOM   12378 H H      . LEU B 2 342 ? 9.687   -3.036  -38.994 1.00 21.31  ?  342  LEU B H      1 
ATOM   12379 H HA     . LEU B 2 342 ? 10.932  -3.432  -41.252 1.00 19.93  ?  342  LEU B HA     1 
ATOM   12380 H HB2    . LEU B 2 342 ? 8.176   -3.121  -40.783 1.00 20.72  ?  342  LEU B HB2    1 
ATOM   12381 H HB3    . LEU B 2 342 ? 8.770   -3.570  -42.187 1.00 20.72  ?  342  LEU B HB3    1 
ATOM   12382 H HG     . LEU B 2 342 ? 8.771   -5.099  -39.831 1.00 24.20  ?  342  LEU B HG     1 
ATOM   12383 H HD11   . LEU B 2 342 ? 7.467   -6.602  -41.053 1.00 24.15  ?  342  LEU B HD11   1 
ATOM   12384 H HD12   . LEU B 2 342 ? 6.761   -5.179  -41.025 1.00 24.15  ?  342  LEU B HD12   1 
ATOM   12385 H HD13   . LEU B 2 342 ? 7.552   -5.648  -42.321 1.00 24.15  ?  342  LEU B HD13   1 
ATOM   12386 H HD21   . LEU B 2 342 ? 9.800   -6.799  -41.200 1.00 25.15  ?  342  LEU B HD21   1 
ATOM   12387 H HD22   . LEU B 2 342 ? 10.194  -5.619  -42.187 1.00 25.15  ?  342  LEU B HD22   1 
ATOM   12388 H HD23   . LEU B 2 342 ? 10.758  -5.634  -40.702 1.00 25.15  ?  342  LEU B HD23   1 
ATOM   12389 N N      . ALA B 2 343 ? 9.726   -0.494  -40.905 1.00 17.39  ?  343  ALA B N      1 
ATOM   12390 C CA     . ALA B 2 343 ? 9.773   0.850   -41.474 1.00 18.58  ?  343  ALA B CA     1 
ATOM   12391 C C      . ALA B 2 343 ? 11.201  1.365   -41.557 1.00 17.78  ?  343  ALA B C      1 
ATOM   12392 O O      . ALA B 2 343 ? 11.568  2.019   -42.532 1.00 21.05  ?  343  ALA B O      1 
ATOM   12393 C CB     . ALA B 2 343 ? 8.921   1.803   -40.632 1.00 20.49  ?  343  ALA B CB     1 
ATOM   12394 H H      . ALA B 2 343 ? 9.334   -0.545  -40.142 1.00 20.87  ?  343  ALA B H      1 
ATOM   12395 H HA     . ALA B 2 343 ? 9.405   0.819   -42.371 1.00 22.29  ?  343  ALA B HA     1 
ATOM   12396 H HB1    . ALA B 2 343 ? 8.988   2.697   -41.003 1.00 24.58  ?  343  ALA B HB1    1 
ATOM   12397 H HB2    . ALA B 2 343 ? 7.998   1.505   -40.654 1.00 24.58  ?  343  ALA B HB2    1 
ATOM   12398 H HB3    . ALA B 2 343 ? 9.249   1.798   -39.719 1.00 24.58  ?  343  ALA B HB3    1 
ATOM   12399 N N      . ILE B 2 344 ? 12.029  1.060   -40.559 1.00 17.95  ?  344  ILE B N      1 
ATOM   12400 C CA     . ILE B 2 344 ? 13.435  1.450   -40.597 1.00 17.21  ?  344  ILE B CA     1 
ATOM   12401 C C      . ILE B 2 344 ? 14.170  0.732   -41.724 1.00 17.10  ?  344  ILE B C      1 
ATOM   12402 O O      . ILE B 2 344 ? 14.918  1.354   -42.490 1.00 19.49  ?  344  ILE B O      1 
ATOM   12403 C CB     . ILE B 2 344 ? 14.089  1.194   -39.229 1.00 18.80  ?  344  ILE B CB     1 
ATOM   12404 C CG1    . ILE B 2 344 ? 13.575  2.223   -38.211 1.00 18.46  ?  344  ILE B CG1    1 
ATOM   12405 C CG2    . ILE B 2 344 ? 15.614  1.255   -39.358 1.00 19.80  ?  344  ILE B CG2    1 
ATOM   12406 C CD1    . ILE B 2 344 ? 13.875  1.857   -36.768 1.00 20.29  ?  344  ILE B CD1    1 
ATOM   12407 H H      . ILE B 2 344 ? 11.803  0.630   -39.849 1.00 21.53  ?  344  ILE B H      1 
ATOM   12408 H HA     . ILE B 2 344 ? 13.485  2.401   -40.781 1.00 20.65  ?  344  ILE B HA     1 
ATOM   12409 H HB     . ILE B 2 344 ? 13.848  0.308   -38.916 1.00 22.55  ?  344  ILE B HB     1 
ATOM   12410 H HG12   . ILE B 2 344 ? 13.994  3.079   -38.393 1.00 22.15  ?  344  ILE B HG12   1 
ATOM   12411 H HG13   . ILE B 2 344 ? 12.612  2.299   -38.303 1.00 22.15  ?  344  ILE B HG13   1 
ATOM   12412 H HG21   . ILE B 2 344 ? 16.000  1.398   -38.480 1.00 23.75  ?  344  ILE B HG21   1 
ATOM   12413 H HG22   . ILE B 2 344 ? 15.933  0.417   -39.727 1.00 23.75  ?  344  ILE B HG22   1 
ATOM   12414 H HG23   . ILE B 2 344 ? 15.852  1.988   -39.947 1.00 23.75  ?  344  ILE B HG23   1 
ATOM   12415 H HD11   . ILE B 2 344 ? 13.396  2.463   -36.182 1.00 24.34  ?  344  ILE B HD11   1 
ATOM   12416 H HD12   . ILE B 2 344 ? 13.587  0.944   -36.608 1.00 24.34  ?  344  ILE B HD12   1 
ATOM   12417 H HD13   . ILE B 2 344 ? 14.830  1.934   -36.615 1.00 24.34  ?  344  ILE B HD13   1 
ATOM   12418 N N      . ILE B 2 345 ? 13.934  -0.577  -41.875 1.00 18.56  ?  345  ILE B N      1 
ATOM   12419 C CA     . ILE B 2 345 ? 14.565  -1.339  -42.955 1.00 17.14  ?  345  ILE B CA     1 
ATOM   12420 C C      . ILE B 2 345 ? 14.224  -0.728  -44.310 1.00 17.06  ?  345  ILE B C      1 
ATOM   12421 O O      . ILE B 2 345 ? 15.090  -0.563  -45.184 1.00 18.57  ?  345  ILE B O      1 
ATOM   12422 C CB     . ILE B 2 345 ? 14.135  -2.821  -42.857 1.00 17.03  ?  345  ILE B CB     1 
ATOM   12423 C CG1    . ILE B 2 345 ? 14.759  -3.470  -41.634 1.00 15.29  ?  345  ILE B CG1    1 
ATOM   12424 C CG2    . ILE B 2 345 ? 14.485  -3.548  -44.155 1.00 16.72  ?  345  ILE B CG2    1 
ATOM   12425 C CD1    . ILE B 2 345 ? 14.166  -4.799  -41.275 1.00 15.43  ?  345  ILE B CD1    1 
ATOM   12426 H H      . ILE B 2 345 ? 13.417  -1.045  -41.371 1.00 22.27  ?  345  ILE B H      1 
ATOM   12427 H HA     . ILE B 2 345 ? 15.529  -1.295  -42.856 1.00 20.56  ?  345  ILE B HA     1 
ATOM   12428 H HB     . ILE B 2 345 ? 13.173  -2.877  -42.743 1.00 20.43  ?  345  ILE B HB     1 
ATOM   12429 H HG12   . ILE B 2 345 ? 15.704  -3.606  -41.804 1.00 18.35  ?  345  ILE B HG12   1 
ATOM   12430 H HG13   . ILE B 2 345 ? 14.639  -2.879  -40.874 1.00 18.35  ?  345  ILE B HG13   1 
ATOM   12431 H HG21   . ILE B 2 345 ? 14.437  -4.505  -44.004 1.00 20.06  ?  345  ILE B HG21   1 
ATOM   12432 H HG22   . ILE B 2 345 ? 13.852  -3.289  -44.843 1.00 20.06  ?  345  ILE B HG22   1 
ATOM   12433 H HG23   . ILE B 2 345 ? 15.384  -3.300  -44.423 1.00 20.06  ?  345  ILE B HG23   1 
ATOM   12434 H HD11   . ILE B 2 345 ? 14.512  -5.077  -40.412 1.00 18.51  ?  345  ILE B HD11   1 
ATOM   12435 H HD12   . ILE B 2 345 ? 13.200  -4.713  -41.231 1.00 18.51  ?  345  ILE B HD12   1 
ATOM   12436 H HD13   . ILE B 2 345 ? 14.409  -5.448  -41.954 1.00 18.51  ?  345  ILE B HD13   1 
ATOM   12437 N N      A GLU B 2 346 ? 12.963  -0.344  -44.493 0.42 16.76  ?  346  GLU B N      1 
ATOM   12438 N N      B GLU B 2 346 ? 12.961  -0.367  -44.494 0.58 17.76  ?  346  GLU B N      1 
ATOM   12439 C CA     A GLU B 2 346 ? 12.529  0.238   -45.759 0.42 19.02  ?  346  GLU B CA     1 
ATOM   12440 C CA     B GLU B 2 346 ? 12.520  0.247   -45.739 0.58 21.49  ?  346  GLU B CA     1 
ATOM   12441 C C      A GLU B 2 346 ? 13.108  1.639   -45.956 0.42 19.77  ?  346  GLU B C      1 
ATOM   12442 C C      B GLU B 2 346 ? 13.150  1.623   -45.930 0.58 21.14  ?  346  GLU B C      1 
ATOM   12443 O O      A GLU B 2 346 ? 13.637  1.956   -47.028 0.42 20.27  ?  346  GLU B O      1 
ATOM   12444 O O      B GLU B 2 346 ? 13.759  1.899   -46.972 0.58 22.43  ?  346  GLU B O      1 
ATOM   12445 C CB     A GLU B 2 346 ? 10.997  0.269   -45.800 0.42 20.95  ?  346  GLU B CB     1 
ATOM   12446 C CB     B GLU B 2 346 ? 10.994  0.365   -45.705 0.58 25.71  ?  346  GLU B CB     1 
ATOM   12447 C CG     A GLU B 2 346 ? 10.399  1.129   -46.914 0.42 24.12  ?  346  GLU B CG     1 
ATOM   12448 C CG     B GLU B 2 346 ? 10.400  1.142   -46.865 0.58 31.75  ?  346  GLU B CG     1 
ATOM   12449 C CD     A GLU B 2 346 ? 10.688  0.597   -48.292 0.42 26.47  ?  346  GLU B CD     1 
ATOM   12450 C CD     B GLU B 2 346 ? 9.413   0.318   -47.639 0.58 37.01  ?  346  GLU B CD     1 
ATOM   12451 O OE1    A GLU B 2 346 ? 11.151  -0.561  -48.391 0.42 26.72  ?  346  GLU B OE1    1 
ATOM   12452 O OE1    B GLU B 2 346 ? 8.284   0.122   -47.145 0.58 38.62  ?  346  GLU B OE1    1 
ATOM   12453 O OE2    A GLU B 2 346 ? 10.446  1.333   -49.273 0.42 27.38  -1 346  GLU B OE2    1 
ATOM   12454 O OE2    B GLU B 2 346 ? 9.781   -0.161  -48.731 0.58 40.44  -1 346  GLU B OE2    1 
ATOM   12455 H H      A GLU B 2 346 ? 12.340  -0.408  -43.904 0.42 20.11  ?  346  GLU B H      1 
ATOM   12456 H H      B GLU B 2 346 ? 12.334  -0.466  -43.913 0.58 21.30  ?  346  GLU B H      1 
ATOM   12457 H HA     A GLU B 2 346 ? 12.848  -0.313  -46.491 0.42 22.83  ?  346  GLU B HA     1 
ATOM   12458 H HA     B GLU B 2 346 ? 12.787  -0.307  -46.489 0.58 25.78  ?  346  GLU B HA     1 
ATOM   12459 H HB2    A GLU B 2 346 ? 10.675  -0.638  -45.928 0.42 25.13  ?  346  GLU B HB2    1 
ATOM   12460 H HB2    B GLU B 2 346 ? 10.614  -0.527  -45.724 0.58 30.85  ?  346  GLU B HB2    1 
ATOM   12461 H HB3    A GLU B 2 346 ? 10.674  0.620   -44.956 0.42 25.13  ?  346  GLU B HB3    1 
ATOM   12462 H HB3    B GLU B 2 346 ? 10.737  0.818   -44.886 0.58 30.85  ?  346  GLU B HB3    1 
ATOM   12463 H HG2    A GLU B 2 346 ? 9.436   1.163   -46.803 0.42 28.94  ?  346  GLU B HG2    1 
ATOM   12464 H HG2    B GLU B 2 346 ? 9.940   1.925   -46.524 0.58 38.10  ?  346  GLU B HG2    1 
ATOM   12465 H HG3    A GLU B 2 346 ? 10.772  2.023   -46.855 0.42 28.94  ?  346  GLU B HG3    1 
ATOM   12466 H HG3    B GLU B 2 346 ? 11.111  1.410   -47.468 0.58 38.10  ?  346  GLU B HG3    1 
ATOM   12467 N N      . ARG B 2 347 ? 13.009  2.496   -44.932 1.00 20.39  ?  347  ARG B N      1 
ATOM   12468 C CA     . ARG B 2 347 ? 13.470  3.871   -45.063 1.00 20.58  ?  347  ARG B CA     1 
ATOM   12469 C C      . ARG B 2 347 ? 14.963  3.949   -45.338 1.00 19.58  ?  347  ARG B C      1 
ATOM   12470 O O      . ARG B 2 347 ? 15.409  4.757   -46.164 1.00 22.82  ?  347  ARG B O      1 
ATOM   12471 C CB     . ARG B 2 347 ? 13.159  4.603   -43.764 1.00 25.64  ?  347  ARG B CB     1 
ATOM   12472 C CG     . ARG B 2 347 ? 13.387  6.088   -43.821 1.00 29.80  ?  347  ARG B CG     1 
ATOM   12473 C CD     . ARG B 2 347 ? 12.939  6.743   -42.517 1.00 32.66  ?  347  ARG B CD     1 
ATOM   12474 N NE     . ARG B 2 347 ? 13.837  6.413   -41.426 1.00 32.78  ?  347  ARG B NE     1 
ATOM   12475 C CZ     . ARG B 2 347 ? 13.466  5.932   -40.235 1.00 33.54  ?  347  ARG B CZ     1 
ATOM   12476 N NH1    . ARG B 2 347 ? 12.195  5.699   -39.938 1.00 33.94  ?  347  ARG B NH1    1 
ATOM   12477 N NH2    . ARG B 2 347 ? 14.394  5.689   -39.336 1.00 35.90  ?  347  ARG B NH2    1 
ATOM   12478 H H      A ARG B 2 347 ? 12.682  2.306   -44.159 0.42 24.46  ?  347  ARG B H      1 
ATOM   12479 H H      B ARG B 2 347 ? 12.651  2.319   -44.170 0.58 24.46  ?  347  ARG B H      1 
ATOM   12480 H HA     . ARG B 2 347 ? 13.011  4.290   -45.807 1.00 24.70  ?  347  ARG B HA     1 
ATOM   12481 H HB2    . ARG B 2 347 ? 12.225  4.458   -43.542 1.00 30.77  ?  347  ARG B HB2    1 
ATOM   12482 H HB3    . ARG B 2 347 ? 13.726  4.246   -43.063 1.00 30.77  ?  347  ARG B HB3    1 
ATOM   12483 H HG2    . ARG B 2 347 ? 14.331  6.268   -43.949 1.00 35.76  ?  347  ARG B HG2    1 
ATOM   12484 H HG3    . ARG B 2 347 ? 12.874  6.469   -44.551 1.00 35.76  ?  347  ARG B HG3    1 
ATOM   12485 H HD2    . ARG B 2 347 ? 12.932  7.707   -42.626 1.00 39.19  ?  347  ARG B HD2    1 
ATOM   12486 H HD3    . ARG B 2 347 ? 12.051  6.429   -42.287 1.00 39.19  ?  347  ARG B HD3    1 
ATOM   12487 H HE     . ARG B 2 347 ? 14.678  6.538   -41.557 1.00 39.33  ?  347  ARG B HE     1 
ATOM   12488 H HH11   . ARG B 2 347 ? 11.582  5.857   -40.519 1.00 40.73  ?  347  ARG B HH11   1 
ATOM   12489 H HH12   . ARG B 2 347 ? 11.985  5.389   -39.163 1.00 40.73  ?  347  ARG B HH12   1 
ATOM   12490 H HH21   . ARG B 2 347 ? 15.221  5.839   -39.520 1.00 43.08  ?  347  ARG B HH21   1 
ATOM   12491 H HH22   . ARG B 2 347 ? 14.175  5.379   -38.564 1.00 43.08  ?  347  ARG B HH22   1 
ATOM   12492 N N      . GLU B 2 348 ? 15.755  3.155   -44.628 1.00 20.56  ?  348  GLU B N      1 
ATOM   12493 C CA     . GLU B 2 348 ? 17.206  3.209   -44.749 1.00 20.80  ?  348  GLU B CA     1 
ATOM   12494 C C      . GLU B 2 348 ? 17.749  2.303   -45.845 1.00 20.22  ?  348  GLU B C      1 
ATOM   12495 O O      . GLU B 2 348 ? 18.966  2.223   -46.015 1.00 22.14  ?  348  GLU B O      1 
ATOM   12496 C CB     . GLU B 2 348 ? 17.859  2.878   -43.404 1.00 21.28  ?  348  GLU B CB     1 
ATOM   12497 C CG     . GLU B 2 348 ? 17.499  3.870   -42.330 1.00 21.93  ?  348  GLU B CG     1 
ATOM   12498 C CD     . GLU B 2 348 ? 18.191  3.616   -40.994 1.00 21.66  ?  348  GLU B CD     1 
ATOM   12499 O OE1    . GLU B 2 348 ? 18.986  2.670   -40.858 1.00 22.77  ?  348  GLU B OE1    1 
ATOM   12500 O OE2    . GLU B 2 348 ? 17.927  4.380   -40.064 1.00 23.53  -1 348  GLU B OE2    1 
ATOM   12501 H H      . GLU B 2 348 ? 15.471  2.571   -44.064 1.00 24.67  ?  348  GLU B H      1 
ATOM   12502 H HA     . GLU B 2 348 ? 17.466  4.115   -44.977 1.00 24.96  ?  348  GLU B HA     1 
ATOM   12503 H HB2    . GLU B 2 348 ? 17.563  2.001   -43.116 1.00 25.53  ?  348  GLU B HB2    1 
ATOM   12504 H HB3    . GLU B 2 348 ? 18.823  2.885   -43.510 1.00 25.53  ?  348  GLU B HB3    1 
ATOM   12505 H HG2    . GLU B 2 348 ? 17.752  4.757   -42.629 1.00 26.31  ?  348  GLU B HG2    1 
ATOM   12506 H HG3    . GLU B 2 348 ? 16.542  3.831   -42.179 1.00 26.31  ?  348  GLU B HG3    1 
ATOM   12507 N N      . GLY B 2 349 ? 16.883  1.625   -46.586 1.00 20.53  ?  349  GLY B N      1 
ATOM   12508 C CA     . GLY B 2 349 ? 17.333  0.756   -47.652 1.00 19.59  ?  349  GLY B CA     1 
ATOM   12509 C C      . GLY B 2 349 ? 18.258  -0.338  -47.174 1.00 19.78  ?  349  GLY B C      1 
ATOM   12510 O O      . GLY B 2 349 ? 19.282  -0.605  -47.812 1.00 20.61  ?  349  GLY B O      1 
ATOM   12511 H H      . GLY B 2 349 ? 16.029  1.653   -46.490 1.00 24.64  ?  349  GLY B H      1 
ATOM   12512 H HA2    . GLY B 2 349 ? 16.562  0.340   -48.069 1.00 23.51  ?  349  GLY B HA2    1 
ATOM   12513 H HA3    . GLY B 2 349 ? 17.804  1.284   -48.316 1.00 23.51  ?  349  GLY B HA3    1 
ATOM   12514 N N      . LEU B 2 350 ? 17.919  -0.988  -46.063 1.00 18.67  ?  350  LEU B N      1 
ATOM   12515 C CA     . LEU B 2 350 ? 18.861  -1.934  -45.480 1.00 17.84  ?  350  LEU B CA     1 
ATOM   12516 C C      . LEU B 2 350 ? 18.945  -3.238  -46.270 1.00 19.47  ?  350  LEU B C      1 
ATOM   12517 O O      . LEU B 2 350 ? 19.969  -3.922  -46.211 1.00 18.26  ?  350  LEU B O      1 
ATOM   12518 C CB     . LEU B 2 350 ? 18.510  -2.200  -44.014 1.00 18.18  ?  350  LEU B CB     1 
ATOM   12519 C CG     . LEU B 2 350 ? 18.608  -0.960  -43.132 1.00 19.00  ?  350  LEU B CG     1 
ATOM   12520 C CD1    . LEU B 2 350 ? 18.412  -1.411  -41.677 1.00 19.87  ?  350  LEU B CD1    1 
ATOM   12521 C CD2    . LEU B 2 350 ? 19.917  -0.233  -43.317 1.00 21.79  ?  350  LEU B CD2    1 
ATOM   12522 H H      . LEU B 2 350 ? 17.175  -0.902  -45.640 1.00 22.40  ?  350  LEU B H      1 
ATOM   12523 H HA     . LEU B 2 350 ? 19.744  -1.534  -45.502 1.00 21.41  ?  350  LEU B HA     1 
ATOM   12524 H HB2    . LEU B 2 350 ? 17.599  -2.529  -43.965 1.00 21.82  ?  350  LEU B HB2    1 
ATOM   12525 H HB3    . LEU B 2 350 ? 19.123  -2.865  -43.662 1.00 21.82  ?  350  LEU B HB3    1 
ATOM   12526 H HG     . LEU B 2 350 ? 17.922  -0.319  -43.376 1.00 22.80  ?  350  LEU B HG     1 
ATOM   12527 H HD11   . LEU B 2 350 ? 18.445  -0.633  -41.098 1.00 23.84  ?  350  LEU B HD11   1 
ATOM   12528 H HD12   . LEU B 2 350 ? 17.550  -1.848  -41.594 1.00 23.84  ?  350  LEU B HD12   1 
ATOM   12529 H HD13   . LEU B 2 350 ? 19.121  -2.029  -41.440 1.00 23.84  ?  350  LEU B HD13   1 
ATOM   12530 H HD21   . LEU B 2 350 ? 20.048  0.377   -42.574 1.00 26.14  ?  350  LEU B HD21   1 
ATOM   12531 H HD22   . LEU B 2 350 ? 20.638  -0.882  -43.343 1.00 26.14  ?  350  LEU B HD22   1 
ATOM   12532 H HD23   . LEU B 2 350 ? 19.889  0.262   -44.150 1.00 26.14  ?  350  LEU B HD23   1 
ATOM   12533 N N      . THR B 2 351 ? 17.890  -3.630  -46.981 1.00 18.64  ?  351  THR B N      1 
ATOM   12534 C CA     . THR B 2 351 ? 17.994  -4.839  -47.799 1.00 20.15  ?  351  THR B CA     1 
ATOM   12535 C C      . THR B 2 351 ? 19.020  -4.638  -48.905 1.00 19.14  ?  351  THR B C      1 
ATOM   12536 O O      . THR B 2 351 ? 19.839  -5.519  -49.175 1.00 17.89  ?  351  THR B O      1 
ATOM   12537 C CB     . THR B 2 351 ? 16.614  -5.214  -48.330 1.00 21.10  ?  351  THR B CB     1 
ATOM   12538 O OG1    . THR B 2 351 ? 15.752  -5.463  -47.212 1.00 22.69  ?  351  THR B OG1    1 
ATOM   12539 C CG2    . THR B 2 351 ? 16.674  -6.468  -49.194 1.00 19.06  ?  351  THR B CG2    1 
ATOM   12540 H H      . THR B 2 351 ? 17.128  -3.231  -47.009 1.00 22.36  ?  351  THR B H      1 
ATOM   12541 H HA     . THR B 2 351 ? 18.296  -5.591  -47.266 1.00 24.18  ?  351  THR B HA     1 
ATOM   12542 H HB     . THR B 2 351 ? 16.269  -4.492  -48.878 1.00 25.32  ?  351  THR B HB     1 
ATOM   12543 H HG1    . THR B 2 351 ? 14.983  -5.667  -47.482 1.00 27.22  ?  351  THR B HG1    1 
ATOM   12544 H HG21   . THR B 2 351 ? 15.778  -6.732  -49.458 1.00 22.87  ?  351  THR B HG21   1 
ATOM   12545 H HG22   . THR B 2 351 ? 17.199  -6.297  -49.991 1.00 22.87  ?  351  THR B HG22   1 
ATOM   12546 H HG23   . THR B 2 351 ? 17.082  -7.194  -48.697 1.00 22.87  ?  351  THR B HG23   1 
ATOM   12547 N N      . ALA B 2 352 ? 19.002  -3.468  -49.544 1.00 18.14  ?  352  ALA B N      1 
ATOM   12548 C CA     . ALA B 2 352 ? 20.017  -3.149  -50.537 1.00 19.21  ?  352  ALA B CA     1 
ATOM   12549 C C      . ALA B 2 352 ? 21.405  -3.050  -49.916 1.00 19.21  ?  352  ALA B C      1 
ATOM   12550 O O      . ALA B 2 352 ? 22.390  -3.475  -50.533 1.00 20.45  ?  352  ALA B O      1 
ATOM   12551 C CB     . ALA B 2 352 ? 19.667  -1.852  -51.253 1.00 19.72  ?  352  ALA B CB     1 
ATOM   12552 H H      . ALA B 2 352 ? 18.419  -2.848  -49.423 1.00 21.77  ?  352  ALA B H      1 
ATOM   12553 H HA     . ALA B 2 352 ? 20.032  -3.864  -51.192 1.00 23.04  ?  352  ALA B HA     1 
ATOM   12554 H HB1    . ALA B 2 352 ? 20.371  -1.642  -51.887 1.00 23.66  ?  352  ALA B HB1    1 
ATOM   12555 H HB2    . ALA B 2 352 ? 18.825  -1.966  -51.720 1.00 23.66  ?  352  ALA B HB2    1 
ATOM   12556 H HB3    . ALA B 2 352 ? 19.589  -1.141  -50.598 1.00 23.66  ?  352  ALA B HB3    1 
ATOM   12557 N N      . ASN B 2 353 ? 21.525  -2.477  -48.714 1.00 19.30  ?  353  ASN B N      1 
ATOM   12558 C CA     . ASN B 2 353 ? 22.843  -2.449  -48.098 1.00 18.23  ?  353  ASN B CA     1 
ATOM   12559 C C      . ASN B 2 353 ? 23.339  -3.864  -47.841 1.00 19.37  ?  353  ASN B C      1 
ATOM   12560 O O      . ASN B 2 353 ? 24.527  -4.159  -48.024 1.00 20.12  ?  353  ASN B O      1 
ATOM   12561 C CB     . ASN B 2 353 ? 22.861  -1.656  -46.801 1.00 18.66  ?  353  ASN B CB     1 
ATOM   12562 C CG     . ASN B 2 353 ? 24.274  -1.441  -46.306 1.00 18.75  ?  353  ASN B CG     1 
ATOM   12563 O OD1    . ASN B 2 353 ? 25.107  -0.889  -47.027 1.00 20.68  ?  353  ASN B OD1    1 
ATOM   12564 N ND2    . ASN B 2 353 ? 24.567  -1.891  -45.091 1.00 19.71  ?  353  ASN B ND2    1 
ATOM   12565 H H      . ASN B 2 353 ? 20.890  -2.116  -48.259 1.00 23.16  ?  353  ASN B H      1 
ATOM   12566 H HA     . ASN B 2 353 ? 23.440  -1.994  -48.712 1.00 21.88  ?  353  ASN B HA     1 
ATOM   12567 H HB2    . ASN B 2 353 ? 22.454  -0.788  -46.949 1.00 22.39  ?  353  ASN B HB2    1 
ATOM   12568 H HB3    . ASN B 2 353 ? 22.369  -2.141  -46.120 1.00 22.39  ?  353  ASN B HB3    1 
ATOM   12569 H HD21   . ASN B 2 353 ? 25.360  -1.788  -44.774 1.00 23.64  ?  353  ASN B HD21   1 
ATOM   12570 H HD22   . ASN B 2 353 ? 23.964  -2.284  -44.622 1.00 23.64  ?  353  ASN B HD22   1 
ATOM   12571 N N      . ALA B 2 354 ? 22.443  -4.751  -47.400 1.00 17.51  ?  354  ALA B N      1 
ATOM   12572 C CA     . ALA B 2 354 ? 22.834  -6.133  -47.161 1.00 18.09  ?  354  ALA B CA     1 
ATOM   12573 C C      . ALA B 2 354 ? 23.313  -6.786  -48.453 1.00 19.30  ?  354  ALA B C      1 
ATOM   12574 O O      . ALA B 2 354 ? 24.263  -7.584  -48.447 1.00 18.22  ?  354  ALA B O      1 
ATOM   12575 C CB     . ALA B 2 354 ? 21.680  -6.905  -46.533 1.00 18.08  ?  354  ALA B CB     1 
ATOM   12576 H H      . ALA B 2 354 ? 21.616  -4.580  -47.234 1.00 21.01  ?  354  ALA B H      1 
ATOM   12577 H HA     . ALA B 2 354 ? 23.568  -6.159  -46.528 1.00 21.71  ?  354  ALA B HA     1 
ATOM   12578 H HB1    . ALA B 2 354 ? 21.939  -7.834  -46.432 1.00 21.69  ?  354  ALA B HB1    1 
ATOM   12579 H HB2    . ALA B 2 354 ? 21.479  -6.522  -45.665 1.00 21.69  ?  354  ALA B HB2    1 
ATOM   12580 H HB3    . ALA B 2 354 ? 20.904  -6.839  -47.112 1.00 21.69  ?  354  ALA B HB3    1 
ATOM   12581 N N      . ALA B 2 355 ? 22.686  -6.447  -49.576 1.00 20.05  ?  355  ALA B N      1 
ATOM   12582 C CA     . ALA B 2 355 ? 23.131  -6.990  -50.858 1.00 20.39  ?  355  ALA B CA     1 
ATOM   12583 C C      . ALA B 2 355 ? 24.471  -6.397  -51.273 1.00 21.15  ?  355  ALA B C      1 
ATOM   12584 O O      . ALA B 2 355 ? 25.376  -7.119  -51.703 1.00 18.95  ?  355  ALA B O      1 
ATOM   12585 C CB     . ALA B 2 355 ? 22.081  -6.708  -51.940 1.00 18.89  ?  355  ALA B CB     1 
ATOM   12586 H H      . ALA B 2 355 ? 22.012  -5.915  -49.626 1.00 24.06  ?  355  ALA B H      1 
ATOM   12587 H HA     . ALA B 2 355 ? 23.234  -7.950  -50.766 1.00 24.47  ?  355  ALA B HA     1 
ATOM   12588 H HB1    . ALA B 2 355 ? 22.389  -7.077  -52.782 1.00 22.66  ?  355  ALA B HB1    1 
ATOM   12589 H HB2    . ALA B 2 355 ? 21.244  -7.125  -51.683 1.00 22.66  ?  355  ALA B HB2    1 
ATOM   12590 H HB3    . ALA B 2 355 ? 21.962  -5.749  -52.022 1.00 22.66  ?  355  ALA B HB3    1 
ATOM   12591 N N      . GLU B 2 356 ? 24.607  -5.077  -51.166 1.00 21.60  ?  356  GLU B N      1 
ATOM   12592 C CA     . GLU B 2 356 ? 25.781  -4.393  -51.689 1.00 22.30  ?  356  GLU B CA     1 
ATOM   12593 C C      . GLU B 2 356 ? 26.980  -4.525  -50.758 1.00 21.30  ?  356  GLU B C      1 
ATOM   12594 O O      . GLU B 2 356 ? 28.073  -4.916  -51.187 1.00 20.30  ?  356  GLU B O      1 
ATOM   12595 C CB     . GLU B 2 356 ? 25.444  -2.914  -51.926 1.00 26.19  ?  356  GLU B CB     1 
ATOM   12596 C CG     . GLU B 2 356 ? 24.388  -2.680  -52.985 1.00 33.79  ?  356  GLU B CG     1 
ATOM   12597 C CD     . GLU B 2 356 ? 23.745  -1.298  -52.910 1.00 41.94  ?  356  GLU B CD     1 
ATOM   12598 O OE1    . GLU B 2 356 ? 24.100  -0.505  -52.014 1.00 45.57  ?  356  GLU B OE1    1 
ATOM   12599 O OE2    . GLU B 2 356 ? 22.870  -1.005  -53.747 1.00 45.80  -1 356  GLU B OE2    1 
ATOM   12600 H H      . GLU B 2 356 ? 24.033  -4.555  -50.795 1.00 25.92  ?  356  GLU B H      1 
ATOM   12601 H HA     . GLU B 2 356 ? 26.028  -4.797  -52.536 1.00 26.76  ?  356  GLU B HA     1 
ATOM   12602 H HB2    . GLU B 2 356 ? 25.118  -2.534  -51.096 1.00 31.42  ?  356  GLU B HB2    1 
ATOM   12603 H HB3    . GLU B 2 356 ? 26.250  -2.454  -52.208 1.00 31.42  ?  356  GLU B HB3    1 
ATOM   12604 H HG2    . GLU B 2 356 ? 24.796  -2.771  -53.860 1.00 40.54  ?  356  GLU B HG2    1 
ATOM   12605 H HG3    . GLU B 2 356 ? 23.685  -3.340  -52.877 1.00 40.54  ?  356  GLU B HG3    1 
ATOM   12606 N N      . THR B 2 357 ? 26.814  -4.147  -49.494 1.00 21.87  ?  357  THR B N      1 
ATOM   12607 C CA     . THR B 2 357 ? 27.891  -4.316  -48.521 1.00 21.70  ?  357  THR B CA     1 
ATOM   12608 C C      . THR B 2 357 ? 28.114  -5.793  -48.221 1.00 19.84  ?  357  THR B C      1 
ATOM   12609 O O      . THR B 2 357 ? 29.244  -6.197  -47.919 1.00 19.81  ?  357  THR B O      1 
ATOM   12610 C CB     . THR B 2 357 ? 27.588  -3.475  -47.282 1.00 21.14  ?  357  THR B CB     1 
ATOM   12611 O OG1    . THR B 2 357 ? 27.485  -2.090  -47.667 1.00 22.30  ?  357  THR B OG1    1 
ATOM   12612 C CG2    . THR B 2 357 ? 28.696  -3.608  -46.247 1.00 21.84  ?  357  THR B CG2    1 
ATOM   12613 H H      . THR B 2 357 ? 26.097  -3.794  -49.175 1.00 26.24  ?  357  THR B H      1 
ATOM   12614 H HA     . THR B 2 357 ? 28.734  -3.982  -48.867 1.00 26.04  ?  357  THR B HA     1 
ATOM   12615 H HB     . THR B 2 357 ? 26.758  -3.781  -46.884 1.00 25.36  ?  357  THR B HB     1 
ATOM   12616 H HG1    . THR B 2 357 ? 27.266  -1.623  -47.004 1.00 26.76  ?  357  THR B HG1    1 
ATOM   12617 H HG21   . THR B 2 357 ? 28.527  -3.012  -45.501 1.00 26.21  ?  357  THR B HG21   1 
ATOM   12618 H HG22   . THR B 2 357 ? 28.736  -4.520  -45.918 1.00 26.21  ?  357  THR B HG22   1 
ATOM   12619 H HG23   . THR B 2 357 ? 29.551  -3.380  -46.645 1.00 26.21  ?  357  THR B HG23   1 
ATOM   12620 N N      . GLY B 2 358 ? 27.067  -6.619  -48.336 1.00 17.96  ?  358  GLY B N      1 
ATOM   12621 C CA     . GLY B 2 358 ? 27.248  -8.049  -48.198 1.00 17.00  ?  358  GLY B CA     1 
ATOM   12622 C C      . GLY B 2 358 ? 28.142  -8.618  -49.279 1.00 17.76  ?  358  GLY B C      1 
ATOM   12623 O O      . GLY B 2 358 ? 29.043  -9.416  -49.001 1.00 17.30  ?  358  GLY B O      1 
ATOM   12624 H H      . GLY B 2 358 ? 26.257  -6.375  -48.492 1.00 21.55  ?  358  GLY B H      1 
ATOM   12625 H HA2    . GLY B 2 358 ? 27.650  -8.241  -47.336 1.00 20.40  ?  358  GLY B HA2    1 
ATOM   12626 H HA3    . GLY B 2 358 ? 26.386  -8.490  -48.249 1.00 20.40  ?  358  GLY B HA3    1 
ATOM   12627 N N      . ALA B 2 359 ? 27.930  -8.199  -50.529 1.00 19.52  ?  359  ALA B N      1 
ATOM   12628 C CA     . ALA B 2 359 ? 28.828  -8.639  -51.588 1.00 19.79  ?  359  ALA B CA     1 
ATOM   12629 C C      . ALA B 2 359 ? 30.257  -8.197  -51.307 1.00 20.51  ?  359  ALA B C      1 
ATOM   12630 O O      . ALA B 2 359 ? 31.214  -8.930  -51.591 1.00 20.78  ?  359  ALA B O      1 
ATOM   12631 C CB     . ALA B 2 359 ? 28.366  -8.066  -52.927 1.00 19.60  ?  359  ALA B CB     1 
ATOM   12632 H H      . ALA B 2 359 ? 27.295  -7.677  -50.781 1.00 23.42  ?  359  ALA B H      1 
ATOM   12633 H HA     . ALA B 2 359 ? 28.805  -9.607  -51.637 1.00 23.74  ?  359  ALA B HA     1 
ATOM   12634 H HB1    . ALA B 2 359 ? 28.956  -8.385  -53.627 1.00 23.51  ?  359  ALA B HB1    1 
ATOM   12635 H HB2    . ALA B 2 359 ? 27.458  -8.361  -53.100 1.00 23.51  ?  359  ALA B HB2    1 
ATOM   12636 H HB3    . ALA B 2 359 ? 28.396  -7.098  -52.883 1.00 23.51  ?  359  ALA B HB3    1 
ATOM   12637 N N      . TYR B 2 360 ? 30.420  -7.003  -50.739 1.00 19.98  ?  360  TYR B N      1 
ATOM   12638 C CA     . TYR B 2 360 ? 31.752  -6.530  -50.381 1.00 20.40  ?  360  TYR B CA     1 
ATOM   12639 C C      . TYR B 2 360 ? 32.357  -7.386  -49.269 1.00 19.02  ?  360  TYR B C      1 
ATOM   12640 O O      . TYR B 2 360 ? 33.549  -7.724  -49.312 1.00 19.84  ?  360  TYR B O      1 
ATOM   12641 C CB     . TYR B 2 360 ? 31.672  -5.065  -49.952 1.00 20.59  ?  360  TYR B CB     1 
ATOM   12642 C CG     . TYR B 2 360 ? 33.009  -4.478  -49.559 1.00 21.39  ?  360  TYR B CG     1 
ATOM   12643 C CD1    . TYR B 2 360 ? 33.966  -4.202  -50.520 1.00 24.78  ?  360  TYR B CD1    1 
ATOM   12644 C CD2    . TYR B 2 360 ? 33.306  -4.218  -48.235 1.00 21.89  ?  360  TYR B CD2    1 
ATOM   12645 C CE1    . TYR B 2 360 ? 35.184  -3.686  -50.174 1.00 26.45  ?  360  TYR B CE1    1 
ATOM   12646 C CE2    . TYR B 2 360 ? 34.527  -3.691  -47.875 1.00 22.63  ?  360  TYR B CE2    1 
ATOM   12647 C CZ     . TYR B 2 360 ? 35.458  -3.437  -48.851 1.00 24.81  ?  360  TYR B CZ     1 
ATOM   12648 O OH     . TYR B 2 360 ? 36.681  -2.907  -48.515 1.00 25.74  ?  360  TYR B OH     1 
ATOM   12649 H H      . TYR B 2 360 ? 29.785  -6.454  -50.552 1.00 23.97  ?  360  TYR B H      1 
ATOM   12650 H HA     . TYR B 2 360 ? 32.335  -6.590  -51.153 1.00 24.48  ?  360  TYR B HA     1 
ATOM   12651 H HB2    . TYR B 2 360 ? 31.323  -4.542  -50.691 1.00 24.71  ?  360  TYR B HB2    1 
ATOM   12652 H HB3    . TYR B 2 360 ? 31.080  -4.995  -49.187 1.00 24.71  ?  360  TYR B HB3    1 
ATOM   12653 H HD1    . TYR B 2 360 ? 33.778  -4.371  -51.415 1.00 29.74  ?  360  TYR B HD1    1 
ATOM   12654 H HD2    . TYR B 2 360 ? 32.674  -4.401  -47.579 1.00 26.26  ?  360  TYR B HD2    1 
ATOM   12655 H HE1    . TYR B 2 360 ? 35.820  -3.505  -50.827 1.00 31.74  ?  360  TYR B HE1    1 
ATOM   12656 H HE2    . TYR B 2 360 ? 34.717  -3.509  -46.983 1.00 27.15  ?  360  TYR B HE2    1 
ATOM   12657 H HH     . TYR B 2 360 ? 36.728  -2.797  -47.684 1.00 30.89  ?  360  TYR B HH     1 
ATOM   12658 N N      . LEU B 2 361 ? 31.549  -7.759  -48.276 1.00 19.15  ?  361  LEU B N      1 
ATOM   12659 C CA     . LEU B 2 361 ? 31.992  -8.705  -47.252 1.00 19.89  ?  361  LEU B CA     1 
ATOM   12660 C C      . LEU B 2 361 ? 32.497  -10.002 -47.874 1.00 20.26  ?  361  LEU B C      1 
ATOM   12661 O O      . LEU B 2 361 ? 33.549  -10.517 -47.481 1.00 21.57  ?  361  LEU B O      1 
ATOM   12662 C CB     . LEU B 2 361 ? 30.834  -9.002  -46.291 1.00 18.65  ?  361  LEU B CB     1 
ATOM   12663 C CG     . LEU B 2 361 ? 31.043  -10.102 -45.242 1.00 18.04  ?  361  LEU B CG     1 
ATOM   12664 C CD1    . LEU B 2 361 ? 32.145  -9.712  -44.250 1.00 19.92  ?  361  LEU B CD1    1 
ATOM   12665 C CD2    . LEU B 2 361 ? 29.735  -10.388 -44.515 1.00 18.86  ?  361  LEU B CD2    1 
ATOM   12666 H H      . LEU B 2 361 ? 30.742  -7.481  -48.170 1.00 22.98  ?  361  LEU B H      1 
ATOM   12667 H HA     . LEU B 2 361 ? 32.720  -8.303  -46.753 1.00 23.87  ?  361  LEU B HA     1 
ATOM   12668 H HB2    . LEU B 2 361 ? 30.636  -8.186  -45.805 1.00 22.37  ?  361  LEU B HB2    1 
ATOM   12669 H HB3    . LEU B 2 361 ? 30.067  -9.266  -46.823 1.00 22.37  ?  361  LEU B HB3    1 
ATOM   12670 H HG     . LEU B 2 361 ? 31.329  -10.915 -45.687 1.00 21.65  ?  361  LEU B HG     1 
ATOM   12671 H HD11   . LEU B 2 361 ? 32.301  -10.453 -43.644 1.00 23.90  ?  361  LEU B HD11   1 
ATOM   12672 H HD12   . LEU B 2 361 ? 32.956  -9.511  -44.743 1.00 23.90  ?  361  LEU B HD12   1 
ATOM   12673 H HD13   . LEU B 2 361 ? 31.859  -8.931  -43.752 1.00 23.90  ?  361  LEU B HD13   1 
ATOM   12674 H HD21   . LEU B 2 361 ? 29.882  -11.093 -43.865 1.00 22.62  ?  361  LEU B HD21   1 
ATOM   12675 H HD22   . LEU B 2 361 ? 29.440  -9.581  -44.065 1.00 22.62  ?  361  LEU B HD22   1 
ATOM   12676 H HD23   . LEU B 2 361 ? 29.069  -10.669 -45.162 1.00 22.62  ?  361  LEU B HD23   1 
ATOM   12677 N N      . GLN B 2 362 ? 31.750  -10.564 -48.830 1.00 19.56  ?  362  GLN B N      1 
ATOM   12678 C CA     . GLN B 2 362 ? 32.189  -11.806 -49.465 1.00 19.86  ?  362  GLN B CA     1 
ATOM   12679 C C      . GLN B 2 362 ? 33.529  -11.613 -50.159 1.00 20.78  ?  362  GLN B C      1 
ATOM   12680 O O      . GLN B 2 362 ? 34.423  -12.470 -50.068 1.00 21.22  ?  362  GLN B O      1 
ATOM   12681 C CB     . GLN B 2 362 ? 31.152  -12.291 -50.476 1.00 20.04  ?  362  GLN B CB     1 
ATOM   12682 C CG     . GLN B 2 362 ? 29.731  -12.480 -49.936 1.00 19.86  ?  362  GLN B CG     1 
ATOM   12683 C CD     . GLN B 2 362 ? 29.672  -13.283 -48.659 1.00 19.99  ?  362  GLN B CD     1 
ATOM   12684 O OE1    . GLN B 2 362 ? 30.334  -14.314 -48.520 1.00 21.32  ?  362  GLN B OE1    1 
ATOM   12685 N NE2    . GLN B 2 362 ? 28.885  -12.806 -47.712 1.00 19.54  ?  362  GLN B NE2    1 
ATOM   12686 H H      . GLN B 2 362 ? 31.003  -10.254 -49.123 1.00 23.47  ?  362  GLN B H      1 
ATOM   12687 H HA     . GLN B 2 362 ? 32.280  -12.484 -48.778 1.00 23.83  ?  362  GLN B HA     1 
ATOM   12688 H HB2    . GLN B 2 362 ? 31.101  -11.641 -51.195 1.00 24.04  ?  362  GLN B HB2    1 
ATOM   12689 H HB3    . GLN B 2 362 ? 31.444  -13.148 -50.824 1.00 24.04  ?  362  GLN B HB3    1 
ATOM   12690 H HG2    . GLN B 2 362 ? 29.346  -11.608 -49.757 1.00 23.83  ?  362  GLN B HG2    1 
ATOM   12691 H HG3    . GLN B 2 362 ? 29.202  -12.946 -50.603 1.00 23.83  ?  362  GLN B HG3    1 
ATOM   12692 H HE21   . GLN B 2 362 ? 28.445  -12.079 -47.844 1.00 23.45  ?  362  GLN B HE21   1 
ATOM   12693 H HE22   . GLN B 2 362 ? 28.813  -13.222 -46.963 1.00 23.45  ?  362  GLN B HE22   1 
ATOM   12694 N N      . GLN B 2 363 ? 33.682  -10.499 -50.882 1.00 21.43  ?  363  GLN B N      1 
ATOM   12695 C CA     . GLN B 2 363 ? 34.930  -10.228 -51.587 1.00 22.99  ?  363  GLN B CA     1 
ATOM   12696 C C      . GLN B 2 363 ? 36.088  -10.109 -50.609 1.00 22.19  ?  363  GLN B C      1 
ATOM   12697 O O      . GLN B 2 363 ? 37.157  -10.686 -50.829 1.00 23.07  ?  363  GLN B O      1 
ATOM   12698 C CB     . GLN B 2 363 ? 34.782  -8.950  -52.415 1.00 27.10  ?  363  GLN B CB     1 
ATOM   12699 C CG     . GLN B 2 363 ? 36.071  -8.452  -53.052 1.00 33.60  ?  363  GLN B CG     1 
ATOM   12700 C CD     . GLN B 2 363 ? 35.915  -7.069  -53.674 1.00 39.97  ?  363  GLN B CD     1 
ATOM   12701 O OE1    . GLN B 2 363 ? 36.453  -6.077  -53.174 1.00 41.77  ?  363  GLN B OE1    1 
ATOM   12702 N NE2    . GLN B 2 363 ? 35.171  -7.000  -54.757 1.00 43.15  ?  363  GLN B NE2    1 
ATOM   12703 H H      . GLN B 2 363 ? 33.083  -9.889  -50.979 1.00 25.72  ?  363  GLN B H      1 
ATOM   12704 H HA     . GLN B 2 363 ? 35.124  -10.961 -52.192 1.00 27.59  ?  363  GLN B HA     1 
ATOM   12705 H HB2    . GLN B 2 363 ? 34.149  -9.119  -53.131 1.00 32.52  ?  363  GLN B HB2    1 
ATOM   12706 H HB3    . GLN B 2 363 ? 34.450  -8.246  -51.838 1.00 32.52  ?  363  GLN B HB3    1 
ATOM   12707 H HG2    . GLN B 2 363 ? 36.762  -8.401  -52.373 1.00 40.32  ?  363  GLN B HG2    1 
ATOM   12708 H HG3    . GLN B 2 363 ? 36.338  -9.068  -53.752 1.00 40.32  ?  363  GLN B HG3    1 
ATOM   12709 H HE21   . GLN B 2 363 ? 34.806  -7.711  -55.074 1.00 51.78  ?  363  GLN B HE21   1 
ATOM   12710 H HE22   . GLN B 2 363 ? 35.050  -6.244  -55.148 1.00 51.78  ?  363  GLN B HE22   1 
ATOM   12711 N N      . CYS B 2 364 ? 35.893  -9.361  -49.515 1.00 21.24  ?  364  CYS B N      1 
ATOM   12712 C CA     . CYS B 2 364 ? 36.971  -9.199  -48.543 1.00 21.60  ?  364  CYS B CA     1 
ATOM   12713 C C      . CYS B 2 364 ? 37.329  -10.532 -47.897 1.00 20.78  ?  364  CYS B C      1 
ATOM   12714 O O      . CYS B 2 364 ? 38.510  -10.828 -47.667 1.00 22.25  ?  364  CYS B O      1 
ATOM   12715 C CB     . CYS B 2 364 ? 36.542  -8.218  -47.465 1.00 23.86  ?  364  CYS B CB     1 
ATOM   12716 S SG     . CYS B 2 364 ? 36.408  -6.543  -48.044 1.00 24.90  ?  364  CYS B SG     1 
ATOM   12717 H H      . CYS B 2 364 ? 35.165  -8.948  -49.318 1.00 25.49  ?  364  CYS B H      1 
ATOM   12718 H HA     . CYS B 2 364 ? 37.754  -8.850  -48.997 1.00 25.92  ?  364  CYS B HA     1 
ATOM   12719 H HB2    . CYS B 2 364 ? 35.674  -8.486  -47.126 1.00 28.63  ?  364  CYS B HB2    1 
ATOM   12720 H HB3    . CYS B 2 364 ? 37.197  -8.234  -46.749 1.00 28.63  ?  364  CYS B HB3    1 
ATOM   12721 H HG     . CYS B 2 364 ? 36.114  -5.834  -47.122 1.00 29.88  ?  364  CYS B HG     1 
ATOM   12722 N N      . MET B 2 365 ? 36.319  -11.349 -47.586 1.00 20.57  ?  365  MET B N      1 
ATOM   12723 C CA     . MET B 2 365 ? 36.604  -12.644 -46.982 1.00 21.39  ?  365  MET B CA     1 
ATOM   12724 C C      . MET B 2 365 ? 37.363  -13.534 -47.954 1.00 22.16  ?  365  MET B C      1 
ATOM   12725 O O      . MET B 2 365 ? 38.327  -14.205 -47.566 1.00 23.08  ?  365  MET B O      1 
ATOM   12726 C CB     . MET B 2 365 ? 35.311  -13.289 -46.513 1.00 21.82  ?  365  MET B CB     1 
ATOM   12727 C CG     . MET B 2 365 ? 34.688  -12.578 -45.316 1.00 21.65  ?  365  MET B CG     1 
ATOM   12728 S SD     . MET B 2 365 ? 35.612  -12.813 -43.781 1.00 22.91  ?  365  MET B SD     1 
ATOM   12729 C CE     . MET B 2 365 ? 34.601  -11.977 -42.606 1.00 25.23  ?  365  MET B CE     1 
ATOM   12730 H H      . MET B 2 365 ? 35.485  -11.181 -47.711 1.00 24.68  ?  365  MET B H      1 
ATOM   12731 H HA     . MET B 2 365 ? 37.156  -12.519 -46.194 1.00 25.66  ?  365  MET B HA     1 
ATOM   12732 H HB2    . MET B 2 365 ? 34.668  -13.271 -47.240 1.00 26.18  ?  365  MET B HB2    1 
ATOM   12733 H HB3    . MET B 2 365 ? 35.493  -14.206 -46.255 1.00 26.18  ?  365  MET B HB3    1 
ATOM   12734 H HG2    . MET B 2 365 ? 34.655  -11.626 -45.499 1.00 25.98  ?  365  MET B HG2    1 
ATOM   12735 H HG3    . MET B 2 365 ? 33.792  -12.921 -45.178 1.00 25.98  ?  365  MET B HG3    1 
ATOM   12736 H HE1    . MET B 2 365 ? 35.043  -11.991 -41.742 1.00 30.27  ?  365  MET B HE1    1 
ATOM   12737 H HE2    . MET B 2 365 ? 34.472  -11.060 -42.896 1.00 30.27  ?  365  MET B HE2    1 
ATOM   12738 H HE3    . MET B 2 365 ? 33.745  -12.429 -42.547 1.00 30.27  ?  365  MET B HE3    1 
ATOM   12739 N N      . GLN B 2 366 ? 36.968  -13.531 -49.230 1.00 22.78  ?  366  GLN B N      1 
ATOM   12740 C CA     . GLN B 2 366 ? 37.679  -14.344 -50.214 1.00 24.35  ?  366  GLN B CA     1 
ATOM   12741 C C      . GLN B 2 366 ? 39.117  -13.876 -50.379 1.00 26.00  ?  366  GLN B C      1 
ATOM   12742 O O      . GLN B 2 366 ? 40.039  -14.701 -50.468 1.00 25.58  ?  366  GLN B O      1 
ATOM   12743 C CB     . GLN B 2 366 ? 36.960  -14.308 -51.561 1.00 28.34  ?  366  GLN B CB     1 
ATOM   12744 C CG     . GLN B 2 366 ? 35.581  -14.987 -51.544 1.00 33.12  ?  366  GLN B CG     1 
ATOM   12745 C CD     . GLN B 2 366 ? 35.660  -16.510 -51.463 1.00 38.22  ?  366  GLN B CD     1 
ATOM   12746 O OE1    . GLN B 2 366 ? 36.712  -17.116 -51.729 1.00 39.17  ?  366  GLN B OE1    1 
ATOM   12747 N NE2    . GLN B 2 366 ? 34.538  -17.139 -51.107 1.00 38.91  ?  366  GLN B NE2    1 
ATOM   12748 H H      . GLN B 2 366 ? 36.308  -13.078 -49.545 1.00 27.34  ?  366  GLN B H      1 
ATOM   12749 H HA     . GLN B 2 366 ? 37.686  -15.261 -49.900 1.00 29.21  ?  366  GLN B HA     1 
ATOM   12750 H HB2    . GLN B 2 366 ? 36.832  -13.383 -51.822 1.00 34.01  ?  366  GLN B HB2    1 
ATOM   12751 H HB3    . GLN B 2 366 ? 37.507  -14.766 -52.219 1.00 34.01  ?  366  GLN B HB3    1 
ATOM   12752 H HG2    . GLN B 2 366 ? 35.086  -14.672 -50.772 1.00 39.74  ?  366  GLN B HG2    1 
ATOM   12753 H HG3    . GLN B 2 366 ? 35.108  -14.756 -52.359 1.00 39.74  ?  366  GLN B HG3    1 
ATOM   12754 H HE21   . GLN B 2 366 ? 33.826  -16.686 -50.940 1.00 46.69  ?  366  GLN B HE21   1 
ATOM   12755 H HE22   . GLN B 2 366 ? 34.527  -17.996 -51.046 1.00 46.69  ?  366  GLN B HE22   1 
ATOM   12756 N N      . GLN B 2 367 ? 39.325  -12.555 -50.436 1.00 25.37  ?  367  GLN B N      1 
ATOM   12757 C CA     . GLN B 2 367 ? 40.654  -12.017 -50.687 1.00 27.75  ?  367  GLN B CA     1 
ATOM   12758 C C      . GLN B 2 367 ? 41.573  -12.247 -49.503 1.00 26.50  ?  367  GLN B C      1 
ATOM   12759 O O      . GLN B 2 367 ? 42.765  -12.522 -49.683 1.00 29.18  ?  367  GLN B O      1 
ATOM   12760 C CB     . GLN B 2 367 ? 40.560  -10.523 -50.984 1.00 31.64  ?  367  GLN B CB     1 
ATOM   12761 C CG     . GLN B 2 367 ? 40.004  -10.228 -52.354 1.00 38.02  ?  367  GLN B CG     1 
ATOM   12762 C CD     . GLN B 2 367 ? 39.848  -8.752  -52.628 1.00 44.83  ?  367  GLN B CD     1 
ATOM   12763 O OE1    . GLN B 2 367 ? 39.811  -7.933  -51.706 1.00 47.58  ?  367  GLN B OE1    1 
ATOM   12764 N NE2    . GLN B 2 367 ? 39.745  -8.402  -53.907 1.00 46.80  ?  367  GLN B NE2    1 
ATOM   12765 H H      . GLN B 2 367 ? 38.717  -11.956 -50.332 1.00 30.44  ?  367  GLN B H      1 
ATOM   12766 H HA     . GLN B 2 367 ? 41.029  -12.466 -51.461 1.00 33.30  ?  367  GLN B HA     1 
ATOM   12767 H HB2    . GLN B 2 367 ? 39.978  -10.107 -50.329 1.00 37.96  ?  367  GLN B HB2    1 
ATOM   12768 H HB3    . GLN B 2 367 ? 41.448  -10.135 -50.932 1.00 37.96  ?  367  GLN B HB3    1 
ATOM   12769 H HG2    . GLN B 2 367 ? 40.605  -10.593 -53.022 1.00 45.62  ?  367  GLN B HG2    1 
ATOM   12770 H HG3    . GLN B 2 367 ? 39.129  -10.640 -52.433 1.00 45.62  ?  367  GLN B HG3    1 
ATOM   12771 H HE21   . GLN B 2 367 ? 39.770  -9.004  -54.521 1.00 56.15  ?  367  GLN B HE21   1 
ATOM   12772 H HE22   . GLN B 2 367 ? 39.654  -7.574  -54.120 1.00 56.15  ?  367  GLN B HE22   1 
ATOM   12773 N N      . THR B 2 368 ? 41.036  -12.141 -48.290 1.00 24.57  ?  368  THR B N      1 
ATOM   12774 C CA     . THR B 2 368 ? 41.856  -12.239 -47.094 1.00 25.04  ?  368  THR B CA     1 
ATOM   12775 C C      . THR B 2 368 ? 42.117  -13.692 -46.718 1.00 24.36  ?  368  THR B C      1 
ATOM   12776 O O      . THR B 2 368 ? 43.207  -14.030 -46.244 1.00 26.04  ?  368  THR B O      1 
ATOM   12777 C CB     . THR B 2 368 ? 41.158  -11.510 -45.946 1.00 26.43  ?  368  THR B CB     1 
ATOM   12778 O OG1    . THR B 2 368 ? 41.004  -10.128 -46.277 1.00 26.86  ?  368  THR B OG1    1 
ATOM   12779 C CG2    . THR B 2 368 ? 41.947  -11.637 -44.643 1.00 26.41  ?  368  THR B CG2    1 
ATOM   12780 H H      . THR B 2 368 ? 40.200  -12.013 -48.134 1.00 29.48  ?  368  THR B H      1 
ATOM   12781 H HA     . THR B 2 368 ? 42.714  -11.814 -47.254 1.00 30.05  ?  368  THR B HA     1 
ATOM   12782 H HB     . THR B 2 368 ? 40.286  -11.911 -45.804 1.00 31.71  ?  368  THR B HB     1 
ATOM   12783 H HG1    . THR B 2 368 ? 40.510  -10.048 -46.951 1.00 32.23  ?  368  THR B HG1    1 
ATOM   12784 H HG21   . THR B 2 368 ? 41.639  -10.976 -44.003 1.00 31.69  ?  368  THR B HG21   1 
ATOM   12785 H HG22   . THR B 2 368 ? 41.825  -12.522 -44.265 1.00 31.69  ?  368  THR B HG22   1 
ATOM   12786 H HG23   . THR B 2 368 ? 42.892  -11.494 -44.811 1.00 31.69  ?  368  THR B HG23   1 
ATOM   12787 N N      . PHE B 2 369 ? 41.135  -14.570 -46.940 1.00 23.51  ?  369  PHE B N      1 
ATOM   12788 C CA     . PHE B 2 369 ? 41.185  -15.924 -46.413 1.00 24.47  ?  369  PHE B CA     1 
ATOM   12789 C C      . PHE B 2 369 ? 41.154  -17.011 -47.470 1.00 25.90  ?  369  PHE B C      1 
ATOM   12790 O O      . PHE B 2 369 ? 41.328  -18.189 -47.120 1.00 25.50  ?  369  PHE B O      1 
ATOM   12791 C CB     . PHE B 2 369 ? 40.018  -16.142 -45.429 1.00 24.17  ?  369  PHE B CB     1 
ATOM   12792 C CG     . PHE B 2 369 ? 40.120  -15.287 -44.184 1.00 22.85  ?  369  PHE B CG     1 
ATOM   12793 C CD1    . PHE B 2 369 ? 41.115  -15.529 -43.249 1.00 22.23  ?  369  PHE B CD1    1 
ATOM   12794 C CD2    . PHE B 2 369 ? 39.243  -14.243 -43.962 1.00 22.64  ?  369  PHE B CD2    1 
ATOM   12795 C CE1    . PHE B 2 369 ? 41.224  -14.753 -42.118 1.00 22.93  ?  369  PHE B CE1    1 
ATOM   12796 C CE2    . PHE B 2 369 ? 39.349  -13.453 -42.825 1.00 23.96  ?  369  PHE B CE2    1 
ATOM   12797 C CZ     . PHE B 2 369 ? 40.336  -13.709 -41.906 1.00 23.30  ?  369  PHE B CZ     1 
ATOM   12798 H H      . PHE B 2 369 ? 40.427  -14.397 -47.397 1.00 28.21  ?  369  PHE B H      1 
ATOM   12799 H HA     . PHE B 2 369 ? 42.017  -16.035 -45.926 1.00 29.36  ?  369  PHE B HA     1 
ATOM   12800 H HB2    . PHE B 2 369 ? 39.186  -15.920 -45.876 1.00 29.01  ?  369  PHE B HB2    1 
ATOM   12801 H HB3    . PHE B 2 369 ? 40.009  -17.071 -45.153 1.00 29.01  ?  369  PHE B HB3    1 
ATOM   12802 H HD1    . PHE B 2 369 ? 41.717  -16.225 -43.388 1.00 26.67  ?  369  PHE B HD1    1 
ATOM   12803 H HD2    . PHE B 2 369 ? 38.573  -14.067 -44.582 1.00 27.17  ?  369  PHE B HD2    1 
ATOM   12804 H HE1    . PHE B 2 369 ? 41.892  -14.928 -41.496 1.00 27.52  ?  369  PHE B HE1    1 
ATOM   12805 H HE2    . PHE B 2 369 ? 38.753  -12.753 -42.686 1.00 28.75  ?  369  PHE B HE2    1 
ATOM   12806 H HZ     . PHE B 2 369 ? 40.409  -13.183 -41.143 1.00 27.96  ?  369  PHE B HZ     1 
ATOM   12807 N N      . GLY B 2 370 ? 40.965  -16.659 -48.749 1.00 26.51  ?  370  GLY B N      1 
ATOM   12808 C CA     . GLY B 2 370 ? 40.816  -17.670 -49.782 1.00 27.82  ?  370  GLY B CA     1 
ATOM   12809 C C      . GLY B 2 370 ? 42.025  -18.574 -49.947 1.00 30.27  ?  370  GLY B C      1 
ATOM   12810 O O      . GLY B 2 370 ? 41.896  -19.698 -50.441 1.00 32.76  ?  370  GLY B O      1 
ATOM   12811 H H      . GLY B 2 370 ? 40.921  -15.850 -49.038 1.00 31.81  ?  370  GLY B H      1 
ATOM   12812 H HA2    . GLY B 2 370 ? 40.053  -18.229 -49.566 1.00 33.38  ?  370  GLY B HA2    1 
ATOM   12813 H HA3    . GLY B 2 370 ? 40.655  -17.230 -50.631 1.00 33.38  ?  370  GLY B HA3    1 
ATOM   12814 N N      . GLU B 2 371 ? 43.209  -18.099 -49.571 1.00 30.96  ?  371  GLU B N      1 
ATOM   12815 C CA     . GLU B 2 371 ? 44.426  -18.898 -49.641 1.00 34.11  ?  371  GLU B CA     1 
ATOM   12816 C C      . GLU B 2 371 ? 45.130  -18.950 -48.291 1.00 32.96  ?  371  GLU B C      1 
ATOM   12817 O O      . GLU B 2 371 ? 46.348  -19.161 -48.244 1.00 33.52  ?  371  GLU B O      1 
ATOM   12818 C CB     . GLU B 2 371 ? 45.362  -18.355 -50.724 1.00 38.14  ?  371  GLU B CB     1 
ATOM   12819 C CG     . GLU B 2 371 ? 44.675  -18.251 -52.081 1.00 43.55  ?  371  GLU B CG     1 
ATOM   12820 C CD     . GLU B 2 371 ? 45.622  -18.430 -53.230 1.00 49.57  ?  371  GLU B CD     1 
ATOM   12821 O OE1    . GLU B 2 371 ? 46.537  -17.595 -53.381 1.00 51.61  ?  371  GLU B OE1    1 
ATOM   12822 O OE2    . GLU B 2 371 ? 45.456  -19.409 -53.988 1.00 52.64  -1 371  GLU B OE2    1 
ATOM   12823 H H      . GLU B 2 371 ? 43.333  -17.304 -49.267 1.00 37.14  ?  371  GLU B H      1 
ATOM   12824 H HA     . GLU B 2 371 ? 44.200  -19.809 -49.884 1.00 40.92  ?  371  GLU B HA     1 
ATOM   12825 H HB2    . GLU B 2 371 ? 45.663  -17.469 -50.469 1.00 45.77  ?  371  GLU B HB2    1 
ATOM   12826 H HB3    . GLU B 2 371 ? 46.122  -18.951 -50.815 1.00 45.77  ?  371  GLU B HB3    1 
ATOM   12827 H HG2    . GLU B 2 371 ? 43.995  -18.940 -52.143 1.00 52.26  ?  371  GLU B HG2    1 
ATOM   12828 H HG3    . GLU B 2 371 ? 44.268  -17.375 -52.162 1.00 52.26  ?  371  GLU B HG3    1 
ATOM   12829 N N      . HIS B 2 372 ? 44.402  -18.765 -47.218 1.00 30.05  ?  372  HIS B N      1 
ATOM   12830 C CA     . HIS B 2 372 ? 44.994  -18.794 -45.889 1.00 29.03  ?  372  HIS B CA     1 
ATOM   12831 C C      . HIS B 2 372 ? 45.279  -20.242 -45.483 1.00 30.76  ?  372  HIS B C      1 
ATOM   12832 O O      . HIS B 2 372 ? 44.442  -21.127 -45.698 1.00 31.02  ?  372  HIS B O      1 
ATOM   12833 C CB     . HIS B 2 372 ? 44.037  -18.152 -44.890 1.00 27.44  ?  372  HIS B CB     1 
ATOM   12834 C CG     . HIS B 2 372 ? 44.649  -17.935 -43.548 1.00 26.46  ?  372  HIS B CG     1 
ATOM   12835 N ND1    . HIS B 2 372 ? 44.932  -18.974 -42.690 1.00 25.24  ?  372  HIS B ND1    1 
ATOM   12836 C CD2    . HIS B 2 372 ? 45.048  -16.805 -42.921 1.00 25.65  ?  372  HIS B CD2    1 
ATOM   12837 C CE1    . HIS B 2 372 ? 45.496  -18.495 -41.596 1.00 26.03  ?  372  HIS B CE1    1 
ATOM   12838 N NE2    . HIS B 2 372 ? 45.570  -17.180 -41.708 1.00 25.20  ?  372  HIS B NE2    1 
ATOM   12839 H H      . HIS B 2 372 ? 43.554  -18.617 -47.220 1.00 36.05  ?  372  HIS B H      1 
ATOM   12840 H HA     . HIS B 2 372 ? 45.831  -18.305 -45.876 1.00 34.83  ?  372  HIS B HA     1 
ATOM   12841 H HB2    . HIS B 2 372 ? 43.757  -17.289 -45.234 1.00 32.92  ?  372  HIS B HB2    1 
ATOM   12842 H HB3    . HIS B 2 372 ? 43.266  -18.730 -44.778 1.00 32.92  ?  372  HIS B HB3    1 
ATOM   12843 H HD2    . HIS B 2 372 ? 44.982  -15.938 -43.249 1.00 30.78  ?  372  HIS B HD2    1 
ATOM   12844 H HE1    . HIS B 2 372 ? 45.790  -18.997 -40.871 1.00 31.24  ?  372  HIS B HE1    1 
ATOM   12845 H HE2    . HIS B 2 372 ? 45.893  -16.646 -41.116 1.00 30.24  ?  372  HIS B HE2    1 
ATOM   12846 N N      . PRO B 2 373 ? 46.455  -20.516 -44.915 1.00 30.25  ?  373  PRO B N      1 
ATOM   12847 C CA     . PRO B 2 373 ? 46.815  -21.914 -44.624 1.00 31.40  ?  373  PRO B CA     1 
ATOM   12848 C C      . PRO B 2 373 ? 45.869  -22.649 -43.675 1.00 29.30  ?  373  PRO B C      1 
ATOM   12849 O O      . PRO B 2 373 ? 45.896  -23.889 -43.640 1.00 31.02  ?  373  PRO B O      1 
ATOM   12850 C CB     . PRO B 2 373 ? 48.233  -21.810 -44.041 1.00 31.23  ?  373  PRO B CB     1 
ATOM   12851 C CG     . PRO B 2 373 ? 48.425  -20.376 -43.692 1.00 31.68  ?  373  PRO B CG     1 
ATOM   12852 C CD     . PRO B 2 373 ? 47.563  -19.588 -44.627 1.00 29.34  ?  373  PRO B CD     1 
ATOM   12853 H HA     . PRO B 2 373 ? 46.845  -22.405 -45.460 1.00 37.67  ?  373  PRO B HA     1 
ATOM   12854 H HB2    . PRO B 2 373 ? 48.304  -22.368 -43.252 1.00 37.47  ?  373  PRO B HB2    1 
ATOM   12855 H HB3    . PRO B 2 373 ? 48.881  -22.091 -44.706 1.00 37.47  ?  373  PRO B HB3    1 
ATOM   12856 H HG2    . PRO B 2 373 ? 48.154  -20.228 -42.773 1.00 38.02  ?  373  PRO B HG2    1 
ATOM   12857 H HG3    . PRO B 2 373 ? 49.358  -20.137 -43.806 1.00 38.02  ?  373  PRO B HG3    1 
ATOM   12858 H HD2    . PRO B 2 373 ? 47.237  -18.780 -44.200 1.00 35.21  ?  373  PRO B HD2    1 
ATOM   12859 H HD3    . PRO B 2 373 ? 48.046  -19.363 -45.437 1.00 35.21  ?  373  PRO B HD3    1 
ATOM   12860 N N      . LEU B 2 374 ? 45.042  -21.949 -42.907 1.00 28.19  ?  374  LEU B N      1 
ATOM   12861 C CA     . LEU B 2 374 ? 44.150  -22.606 -41.964 1.00 26.83  ?  374  LEU B CA     1 
ATOM   12862 C C      . LEU B 2 374 ? 42.735  -22.796 -42.504 1.00 26.43  ?  374  LEU B C      1 
ATOM   12863 O O      . LEU B 2 374 ? 41.934  -23.493 -41.866 1.00 26.64  ?  374  LEU B O      1 
ATOM   12864 C CB     . LEU B 2 374 ? 44.077  -21.788 -40.664 1.00 26.20  ?  374  LEU B CB     1 
ATOM   12865 C CG     . LEU B 2 374 ? 43.436  -22.437 -39.440 1.00 27.37  ?  374  LEU B CG     1 
ATOM   12866 C CD1    . LEU B 2 374 ? 44.197  -23.688 -39.048 1.00 30.81  ?  374  LEU B CD1    1 
ATOM   12867 C CD2    . LEU B 2 374 ? 43.378  -21.494 -38.266 1.00 28.31  ?  374  LEU B CD2    1 
ATOM   12868 H H      . LEU B 2 374 ? 44.980  -21.091 -42.916 1.00 33.83  ?  374  LEU B H      1 
ATOM   12869 H HA     . LEU B 2 374 ? 44.510  -23.483 -41.757 1.00 32.20  ?  374  LEU B HA     1 
ATOM   12870 H HB2    . LEU B 2 374 ? 44.984  -21.554 -40.412 1.00 31.44  ?  374  LEU B HB2    1 
ATOM   12871 H HB3    . LEU B 2 374 ? 43.567  -20.985 -40.851 1.00 31.44  ?  374  LEU B HB3    1 
ATOM   12872 H HG     . LEU B 2 374 ? 42.525  -22.674 -39.674 1.00 32.84  ?  374  LEU B HG     1 
ATOM   12873 H HD11   . LEU B 2 374 ? 43.852  -24.015 -38.202 1.00 36.96  ?  374  LEU B HD11   1 
ATOM   12874 H HD12   . LEU B 2 374 ? 44.077  -24.360 -39.737 1.00 36.96  ?  374  LEU B HD12   1 
ATOM   12875 H HD13   . LEU B 2 374 ? 45.138  -23.470 -38.959 1.00 36.96  ?  374  LEU B HD13   1 
ATOM   12876 H HD21   . LEU B 2 374 ? 42.959  -21.947 -37.518 1.00 33.97  ?  374  LEU B HD21   1 
ATOM   12877 H HD22   . LEU B 2 374 ? 44.280  -21.228 -38.030 1.00 33.97  ?  374  LEU B HD22   1 
ATOM   12878 H HD23   . LEU B 2 374 ? 42.857  -20.714 -38.514 1.00 33.97  ?  374  LEU B HD23   1 
ATOM   12879 N N      . VAL B 2 375 ? 42.412  -22.217 -43.654 1.00 25.25  ?  375  VAL B N      1 
ATOM   12880 C CA     . VAL B 2 375 ? 41.027  -22.072 -44.094 1.00 24.20  ?  375  VAL B CA     1 
ATOM   12881 C C      . VAL B 2 375 ? 40.744  -23.074 -45.201 1.00 23.66  ?  375  VAL B C      1 
ATOM   12882 O O      . VAL B 2 375 ? 41.297  -22.983 -46.303 1.00 26.47  ?  375  VAL B O      1 
ATOM   12883 C CB     . VAL B 2 375 ? 40.725  -20.628 -44.519 1.00 22.65  ?  375  VAL B CB     1 
ATOM   12884 C CG1    . VAL B 2 375 ? 39.303  -20.491 -45.042 1.00 23.90  ?  375  VAL B CG1    1 
ATOM   12885 C CG2    . VAL B 2 375 ? 40.940  -19.698 -43.337 1.00 22.53  ?  375  VAL B CG2    1 
ATOM   12886 H H      . VAL B 2 375 ? 42.989  -21.896 -44.205 1.00 30.30  ?  375  VAL B H      1 
ATOM   12887 H HA     . VAL B 2 375 ? 40.438  -22.308 -43.361 1.00 29.03  ?  375  VAL B HA     1 
ATOM   12888 H HB     . VAL B 2 375 ? 41.325  -20.380 -45.240 1.00 27.17  ?  375  VAL B HB     1 
ATOM   12889 H HG11   . VAL B 2 375 ? 39.085  -19.549 -45.123 1.00 28.68  ?  375  VAL B HG11   1 
ATOM   12890 H HG12   . VAL B 2 375 ? 39.243  -20.920 -45.910 1.00 28.68  ?  375  VAL B HG12   1 
ATOM   12891 H HG13   . VAL B 2 375 ? 38.695  -20.919 -44.420 1.00 28.68  ?  375  VAL B HG13   1 
ATOM   12892 H HG21   . VAL B 2 375 ? 40.678  -18.799 -43.591 1.00 27.03  ?  375  VAL B HG21   1 
ATOM   12893 H HG22   . VAL B 2 375 ? 40.399  -20.003 -42.593 1.00 27.03  ?  375  VAL B HG22   1 
ATOM   12894 H HG23   . VAL B 2 375 ? 41.879  -19.712 -43.092 1.00 27.03  ?  375  VAL B HG23   1 
ATOM   12895 N N      . GLY B 2 376 ? 39.871  -24.034 -44.904 1.00 22.47  ?  376  GLY B N      1 
ATOM   12896 C CA     . GLY B 2 376 ? 39.427  -24.975 -45.924 1.00 23.74  ?  376  GLY B CA     1 
ATOM   12897 C C      . GLY B 2 376 ? 38.356  -24.431 -46.844 1.00 23.04  ?  376  GLY B C      1 
ATOM   12898 O O      . GLY B 2 376 ? 38.319  -24.786 -48.030 1.00 23.51  ?  376  GLY B O      1 
ATOM   12899 H H      . GLY B 2 376 ? 39.523  -24.162 -44.128 1.00 26.96  ?  376  GLY B H      1 
ATOM   12900 H HA2    . GLY B 2 376 ? 40.188  -25.228 -46.469 1.00 28.48  ?  376  GLY B HA2    1 
ATOM   12901 H HA3    . GLY B 2 376 ? 39.073  -25.766 -45.489 1.00 28.48  ?  376  GLY B HA3    1 
ATOM   12902 N N      . GLU B 2 377 ? 37.462  -23.581 -46.329 1.00 23.49  ?  377  GLU B N      1 
ATOM   12903 C CA     . GLU B 2 377 ? 36.448  -22.967 -47.170 1.00 21.79  ?  377  GLU B CA     1 
ATOM   12904 C C      . GLU B 2 377 ? 36.060  -21.596 -46.634 1.00 20.54  ?  377  GLU B C      1 
ATOM   12905 O O      . GLU B 2 377 ? 35.847  -21.432 -45.433 1.00 20.51  ?  377  GLU B O      1 
ATOM   12906 C CB     . GLU B 2 377 ? 35.202  -23.851 -47.276 1.00 20.17  ?  377  GLU B CB     1 
ATOM   12907 C CG     . GLU B 2 377 ? 34.091  -23.195 -48.080 1.00 19.69  ?  377  GLU B CG     1 
ATOM   12908 C CD     . GLU B 2 377 ? 33.015  -24.144 -48.534 1.00 21.00  ?  377  GLU B CD     1 
ATOM   12909 O OE1    . GLU B 2 377 ? 32.148  -24.492 -47.727 1.00 18.81  ?  377  GLU B OE1    1 
ATOM   12910 O OE2    . GLU B 2 377 ? 33.020  -24.531 -49.720 1.00 26.27  -1 377  GLU B OE2    1 
ATOM   12911 H H      . GLU B 2 377 ? 37.428  -23.350 -45.501 1.00 28.18  ?  377  GLU B H      1 
ATOM   12912 H HA     . GLU B 2 377 ? 36.829  -22.839 -48.053 1.00 26.14  ?  377  GLU B HA     1 
ATOM   12913 H HB2    . GLU B 2 377 ? 35.440  -24.683 -47.714 1.00 24.21  ?  377  GLU B HB2    1 
ATOM   12914 H HB3    . GLU B 2 377 ? 34.864  -24.031 -46.385 1.00 24.21  ?  377  GLU B HB3    1 
ATOM   12915 H HG2    . GLU B 2 377 ? 33.670  -22.515 -47.532 1.00 23.62  ?  377  GLU B HG2    1 
ATOM   12916 H HG3    . GLU B 2 377 ? 34.478  -22.790 -48.872 1.00 23.62  ?  377  GLU B HG3    1 
ATOM   12917 N N      . VAL B 2 378 ? 35.992  -20.627 -47.540 1.00 19.32  ?  378  VAL B N      1 
ATOM   12918 C CA     . VAL B 2 378 ? 35.375  -19.326 -47.318 1.00 18.58  ?  378  VAL B CA     1 
ATOM   12919 C C      . VAL B 2 378 ? 34.049  -19.340 -48.064 1.00 17.48  ?  378  VAL B C      1 
ATOM   12920 O O      . VAL B 2 378 ? 34.005  -19.683 -49.254 1.00 20.19  ?  378  VAL B O      1 
ATOM   12921 C CB     . VAL B 2 378 ? 36.247  -18.190 -47.875 1.00 20.77  ?  378  VAL B CB     1 
ATOM   12922 C CG1    . VAL B 2 378 ? 35.642  -16.839 -47.520 1.00 22.64  ?  378  VAL B CG1    1 
ATOM   12923 C CG2    . VAL B 2 378 ? 37.689  -18.294 -47.395 1.00 23.17  ?  378  VAL B CG2    1 
ATOM   12924 H H      . VAL B 2 378 ? 36.315  -20.707 -48.333 1.00 23.18  ?  378  VAL B H      1 
ATOM   12925 H HA     . VAL B 2 378 ? 35.237  -19.186 -46.369 1.00 22.30  ?  378  VAL B HA     1 
ATOM   12926 H HB     . VAL B 2 378 ? 36.271  -18.269 -48.841 1.00 24.92  ?  378  VAL B HB     1 
ATOM   12927 H HG11   . VAL B 2 378 ? 36.248  -16.137 -47.804 1.00 27.16  ?  378  VAL B HG11   1 
ATOM   12928 H HG12   . VAL B 2 378 ? 34.791  -16.745 -47.974 1.00 27.16  ?  378  VAL B HG12   1 
ATOM   12929 H HG13   . VAL B 2 378 ? 35.512  -16.794 -46.560 1.00 27.16  ?  378  VAL B HG13   1 
ATOM   12930 H HG21   . VAL B 2 378 ? 38.190  -17.536 -47.734 1.00 27.80  ?  378  VAL B HG21   1 
ATOM   12931 H HG22   . VAL B 2 378 ? 37.700  -18.291 -46.425 1.00 27.80  ?  378  VAL B HG22   1 
ATOM   12932 H HG23   . VAL B 2 378 ? 38.073  -19.121 -47.728 1.00 27.80  ?  378  VAL B HG23   1 
ATOM   12933 N N      . ARG B 2 379 ? 32.971  -18.987 -47.377 1.00 18.97  ?  379  ARG B N      1 
ATOM   12934 C CA     . ARG B 2 379 ? 31.660  -19.056 -48.006 1.00 17.13  ?  379  ARG B CA     1 
ATOM   12935 C C      . ARG B 2 379 ? 30.745  -17.986 -47.418 1.00 16.96  ?  379  ARG B C      1 
ATOM   12936 O O      . ARG B 2 379 ? 31.016  -17.406 -46.359 1.00 17.89  ?  379  ARG B O      1 
ATOM   12937 C CB     . ARG B 2 379 ? 31.062  -20.452 -47.838 1.00 17.46  ?  379  ARG B CB     1 
ATOM   12938 C CG     . ARG B 2 379 ? 30.878  -20.859 -46.388 1.00 18.42  ?  379  ARG B CG     1 
ATOM   12939 C CD     . ARG B 2 379 ? 30.202  -22.229 -46.250 1.00 17.01  ?  379  ARG B CD     1 
ATOM   12940 N NE     . ARG B 2 379 ? 30.139  -22.603 -44.832 1.00 17.69  ?  379  ARG B NE     1 
ATOM   12941 C CZ     . ARG B 2 379 ? 30.912  -23.520 -44.249 1.00 17.51  ?  379  ARG B CZ     1 
ATOM   12942 N NH1    . ARG B 2 379 ? 31.810  -24.203 -44.940 1.00 16.95  ?  379  ARG B NH1    1 
ATOM   12943 N NH2    . ARG B 2 379 ? 30.766  -23.765 -42.955 1.00 18.13  ?  379  ARG B NH2    1 
ATOM   12944 H H      . ARG B 2 379 ? 32.972  -18.709 -46.563 1.00 22.77  ?  379  ARG B H      1 
ATOM   12945 H HA     . ARG B 2 379 ? 31.739  -18.863 -48.953 1.00 20.55  ?  379  ARG B HA     1 
ATOM   12946 H HB2    . ARG B 2 379 ? 30.192  -20.473 -48.265 1.00 20.95  ?  379  ARG B HB2    1 
ATOM   12947 H HB3    . ARG B 2 379 ? 31.653  -21.098 -48.255 1.00 20.95  ?  379  ARG B HB3    1 
ATOM   12948 H HG2    . ARG B 2 379 ? 31.746  -20.906 -45.958 1.00 22.10  ?  379  ARG B HG2    1 
ATOM   12949 H HG3    . ARG B 2 379 ? 30.322  -20.202 -45.941 1.00 22.10  ?  379  ARG B HG3    1 
ATOM   12950 H HD2    . ARG B 2 379 ? 29.300  -22.187 -46.603 1.00 20.41  ?  379  ARG B HD2    1 
ATOM   12951 H HD3    . ARG B 2 379 ? 30.715  -22.898 -46.728 1.00 20.41  ?  379  ARG B HD3    1 
ATOM   12952 H HE     . ARG B 2 379 ? 29.560  -22.201 -44.340 1.00 21.23  ?  379  ARG B HE     1 
ATOM   12953 H HH11   . ARG B 2 379 ? 31.904  -24.059 -45.783 1.00 20.34  ?  379  ARG B HH11   1 
ATOM   12954 H HH12   . ARG B 2 379 ? 32.300  -24.790 -44.547 1.00 20.34  ?  379  ARG B HH12   1 
ATOM   12955 H HH21   . ARG B 2 379 ? 30.177  -23.335 -42.500 1.00 21.75  ?  379  ARG B HH21   1 
ATOM   12956 H HH22   . ARG B 2 379 ? 31.260  -24.355 -42.571 1.00 21.75  ?  379  ARG B HH22   1 
ATOM   12957 N N      . GLY B 2 380 ? 29.649  -17.745 -48.115 1.00 17.93  ?  380  GLY B N      1 
ATOM   12958 C CA     . GLY B 2 380 ? 28.631  -16.846 -47.620 1.00 17.83  ?  380  GLY B CA     1 
ATOM   12959 C C      . GLY B 2 380 ? 27.797  -16.273 -48.744 1.00 16.46  ?  380  GLY B C      1 
ATOM   12960 O O      . GLY B 2 380 ? 28.026  -16.544 -49.930 1.00 18.01  ?  380  GLY B O      1 
ATOM   12961 H H      . GLY B 2 380 ? 29.472  -18.091 -48.882 1.00 21.51  ?  380  GLY B H      1 
ATOM   12962 H HA2    . GLY B 2 380 ? 28.044  -17.324 -47.014 1.00 21.39  ?  380  GLY B HA2    1 
ATOM   12963 H HA3    . GLY B 2 380 ? 29.049  -16.113 -47.143 1.00 21.39  ?  380  GLY B HA3    1 
ATOM   12964 N N      . VAL B 2 381 ? 26.839  -15.442 -48.330 1.00 17.41  ?  381  VAL B N      1 
ATOM   12965 C CA     . VAL B 2 381 ? 25.964  -14.702 -49.236 1.00 17.02  ?  381  VAL B CA     1 
ATOM   12966 C C      . VAL B 2 381 ? 25.364  -13.543 -48.449 1.00 17.18  ?  381  VAL B C      1 
ATOM   12967 O O      . VAL B 2 381 ? 25.017  -13.689 -47.275 1.00 16.58  ?  381  VAL B O      1 
ATOM   12968 C CB     . VAL B 2 381 ? 24.885  -15.632 -49.834 1.00 17.63  ?  381  VAL B CB     1 
ATOM   12969 C CG1    . VAL B 2 381 ? 23.982  -16.214 -48.741 1.00 17.79  ?  381  VAL B CG1    1 
ATOM   12970 C CG2    . VAL B 2 381 ? 24.044  -14.891 -50.855 1.00 19.03  ?  381  VAL B CG2    1 
ATOM   12971 H H      . VAL B 2 381 ? 26.672  -15.285 -47.501 1.00 20.89  ?  381  VAL B H      1 
ATOM   12972 H HA     . VAL B 2 381 ? 26.479  -14.332 -49.970 1.00 20.42  ?  381  VAL B HA     1 
ATOM   12973 H HB     . VAL B 2 381 ? 25.338  -16.368 -50.276 1.00 21.15  ?  381  VAL B HB     1 
ATOM   12974 H HG11   . VAL B 2 381 ? 23.347  -16.824 -49.147 1.00 21.35  ?  381  VAL B HG11   1 
ATOM   12975 H HG12   . VAL B 2 381 ? 24.531  -16.688 -48.096 1.00 21.35  ?  381  VAL B HG12   1 
ATOM   12976 H HG13   . VAL B 2 381 ? 23.510  -15.488 -48.302 1.00 21.35  ?  381  VAL B HG13   1 
ATOM   12977 H HG21   . VAL B 2 381 ? 23.454  -15.522 -51.296 1.00 22.84  ?  381  VAL B HG21   1 
ATOM   12978 H HG22   . VAL B 2 381 ? 23.522  -14.212 -50.401 1.00 22.84  ?  381  VAL B HG22   1 
ATOM   12979 H HG23   . VAL B 2 381 ? 24.631  -14.477 -51.507 1.00 22.84  ?  381  VAL B HG23   1 
ATOM   12980 N N      . GLY B 2 382 ? 25.241  -12.390 -49.091 1.00 17.06  ?  382  GLY B N      1 
ATOM   12981 C CA     . GLY B 2 382 ? 24.670  -11.259 -48.390 1.00 16.91  ?  382  GLY B CA     1 
ATOM   12982 C C      . GLY B 2 382 ? 25.457  -10.964 -47.131 1.00 16.98  ?  382  GLY B C      1 
ATOM   12983 O O      . GLY B 2 382 ? 26.692  -10.923 -47.135 1.00 18.17  ?  382  GLY B O      1 
ATOM   12984 H H      . GLY B 2 382 ? 25.473  -12.241 -49.906 1.00 20.46  ?  382  GLY B H      1 
ATOM   12985 H HA2    . GLY B 2 382 ? 24.688  -10.475 -48.961 1.00 20.28  ?  382  GLY B HA2    1 
ATOM   12986 H HA3    . GLY B 2 382 ? 23.751  -11.452 -48.147 1.00 20.28  ?  382  GLY B HA3    1 
ATOM   12987 N N      A MET B 2 383 ? 24.744  -10.750 -46.025 0.64 16.47  ?  383  MET B N      1 
ATOM   12988 N N      B MET B 2 383 ? 24.742  -10.762 -46.024 0.36 16.78  ?  383  MET B N      1 
ATOM   12989 C CA     A MET B 2 383 ? 25.388  -10.447 -44.739 0.64 15.87  ?  383  MET B CA     1 
ATOM   12990 C CA     B MET B 2 383 ? 25.370  -10.454 -44.743 0.36 16.69  ?  383  MET B CA     1 
ATOM   12991 C C      A MET B 2 383 ? 25.542  -11.688 -43.872 0.64 15.89  ?  383  MET B C      1 
ATOM   12992 C C      B MET B 2 383 ? 25.540  -11.693 -43.874 0.36 16.45  ?  383  MET B C      1 
ATOM   12993 O O      A MET B 2 383 ? 25.430  -11.624 -42.641 0.64 16.45  ?  383  MET B O      1 
ATOM   12994 O O      B MET B 2 383 ? 25.431  -11.615 -42.644 0.36 16.75  ?  383  MET B O      1 
ATOM   12995 C CB     A MET B 2 383 ? 24.629  -9.364  -43.986 0.64 18.12  ?  383  MET B CB     1 
ATOM   12996 C CB     B MET B 2 383 ? 24.585  -9.364  -44.018 0.36 18.19  ?  383  MET B CB     1 
ATOM   12997 C CG     A MET B 2 383 ? 24.851  -7.974  -44.540 0.64 18.78  ?  383  MET B CG     1 
ATOM   12998 C CG     B MET B 2 383 ? 24.594  -8.050  -44.782 0.36 18.55  ?  383  MET B CG     1 
ATOM   12999 S SD     A MET B 2 383 ? 26.507  -7.322  -44.252 0.64 19.36  ?  383  MET B SD     1 
ATOM   13000 S SD     B MET B 2 383 ? 26.264  -7.355  -44.897 0.36 19.20  ?  383  MET B SD     1 
ATOM   13001 C CE     A MET B 2 383 ? 26.159  -5.593  -44.601 0.64 21.37  ?  383  MET B CE     1 
ATOM   13002 C CE     B MET B 2 383 ? 26.458  -6.711  -43.239 0.36 19.41  ?  383  MET B CE     1 
ATOM   13003 H H      A MET B 2 383 ? 23.885  -10.775 -45.993 0.64 19.75  ?  383  MET B H      1 
ATOM   13004 H H      B MET B 2 383 ? 23.884  -10.798 -45.993 0.36 20.13  ?  383  MET B H      1 
ATOM   13005 H HA     A MET B 2 383 ? 26.271  -10.093 -44.932 0.64 19.04  ?  383  MET B HA     1 
ATOM   13006 H HA     B MET B 2 383 ? 26.256  -10.096 -44.912 0.36 20.03  ?  383  MET B HA     1 
ATOM   13007 H HB2    A MET B 2 383 ? 23.680  -9.556  -44.036 0.64 21.74  ?  383  MET B HB2    1 
ATOM   13008 H HB2    B MET B 2 383 ? 23.664  -9.649  -43.917 0.36 21.82  ?  383  MET B HB2    1 
ATOM   13009 H HB3    A MET B 2 383 ? 24.919  -9.365  -43.060 0.64 21.74  ?  383  MET B HB3    1 
ATOM   13010 H HB3    B MET B 2 383 ? 24.983  -9.211  -43.147 0.36 21.82  ?  383  MET B HB3    1 
ATOM   13011 H HG2    A MET B 2 383 ? 24.706  -7.995  -45.499 0.64 22.53  ?  383  MET B HG2    1 
ATOM   13012 H HG2    B MET B 2 383 ? 24.263  -8.200  -45.681 0.36 22.26  ?  383  MET B HG2    1 
ATOM   13013 H HG3    A MET B 2 383 ? 24.219  -7.368  -44.123 0.64 22.53  ?  383  MET B HG3    1 
ATOM   13014 H HG3    B MET B 2 383 ? 24.028  -7.409  -44.323 0.36 22.26  ?  383  MET B HG3    1 
ATOM   13015 H HE1    A MET B 2 383 ? 26.974  -5.078  -44.494 0.64 25.64  ?  383  MET B HE1    1 
ATOM   13016 H HE1    B MET B 2 383 ? 27.401  -6.709  -43.010 0.36 23.29  ?  383  MET B HE1    1 
ATOM   13017 H HE2    A MET B 2 383 ? 25.834  -5.513  -45.511 0.64 25.64  ?  383  MET B HE2    1 
ATOM   13018 H HE2    B MET B 2 383 ? 26.108  -5.807  -43.209 0.36 23.29  ?  383  MET B HE2    1 
ATOM   13019 H HE3    A MET B 2 383 ? 25.484  -5.275  -43.980 0.64 25.64  ?  383  MET B HE3    1 
ATOM   13020 H HE3    B MET B 2 383 ? 25.970  -7.277  -42.621 0.36 23.29  ?  383  MET B HE3    1 
ATOM   13021 N N      . LEU B 2 384 ? 25.797  -12.837 -44.502 1.00 16.12  ?  384  LEU B N      1 
ATOM   13022 C CA     . LEU B 2 384 ? 26.211  -14.057 -43.820 1.00 15.18  ?  384  LEU B CA     1 
ATOM   13023 C C      . LEU B 2 384 ? 27.548  -14.489 -44.410 1.00 15.43  ?  384  LEU B C      1 
ATOM   13024 O O      . LEU B 2 384 ? 27.711  -14.508 -45.635 1.00 18.38  ?  384  LEU B O      1 
ATOM   13025 C CB     . LEU B 2 384 ? 25.213  -15.191 -44.055 1.00 15.20  ?  384  LEU B CB     1 
ATOM   13026 C CG     . LEU B 2 384 ? 23.836  -15.004 -43.443 1.00 15.91  ?  384  LEU B CG     1 
ATOM   13027 C CD1    . LEU B 2 384 ? 22.925  -16.092 -43.935 1.00 16.19  ?  384  LEU B CD1    1 
ATOM   13028 C CD2    . LEU B 2 384 ? 23.902  -15.027 -41.941 1.00 18.05  ?  384  LEU B CD2    1 
ATOM   13029 H H      A LEU B 2 384 ? 25.733  -12.932 -45.355 0.64 19.34  ?  384  LEU B H      1 
ATOM   13030 H H      B LEU B 2 384 ? 25.735  -12.931 -45.355 0.36 19.34  ?  384  LEU B H      1 
ATOM   13031 H HA     . LEU B 2 384 ? 26.286  -13.885 -42.868 1.00 18.21  ?  384  LEU B HA     1 
ATOM   13032 H HB2    . LEU B 2 384 ? 25.091  -15.292 -45.012 1.00 18.24  ?  384  LEU B HB2    1 
ATOM   13033 H HB3    . LEU B 2 384 ? 25.586  -16.004 -43.680 1.00 18.24  ?  384  LEU B HB3    1 
ATOM   13034 H HG     . LEU B 2 384 ? 23.482  -14.140 -43.707 1.00 19.09  ?  384  LEU B HG     1 
ATOM   13035 H HD11   . LEU B 2 384 ? 22.057  -15.993 -43.513 1.00 19.42  ?  384  LEU B HD11   1 
ATOM   13036 H HD12   . LEU B 2 384 ? 22.835  -16.016 -44.898 1.00 19.42  ?  384  LEU B HD12   1 
ATOM   13037 H HD13   . LEU B 2 384 ? 23.308  -16.953 -43.706 1.00 19.42  ?  384  LEU B HD13   1 
ATOM   13038 H HD21   . LEU B 2 384 ? 23.002  -15.105 -41.586 1.00 21.66  ?  384  LEU B HD21   1 
ATOM   13039 H HD22   . LEU B 2 384 ? 24.436  -15.786 -41.660 1.00 21.66  ?  384  LEU B HD22   1 
ATOM   13040 H HD23   . LEU B 2 384 ? 24.309  -14.203 -41.630 1.00 21.66  ?  384  LEU B HD23   1 
ATOM   13041 N N      . ALA B 2 385 ? 28.499  -14.844 -43.553 1.00 14.71  ?  385  ALA B N      1 
ATOM   13042 C CA     . ALA B 2 385 ? 29.772  -15.346 -44.043 1.00 14.51  ?  385  ALA B CA     1 
ATOM   13043 C C      . ALA B 2 385 ? 30.355  -16.317 -43.025 1.00 16.33  ?  385  ALA B C      1 
ATOM   13044 O O      . ALA B 2 385 ? 30.038  -16.254 -41.831 1.00 16.80  ?  385  ALA B O      1 
ATOM   13045 C CB     . ALA B 2 385 ? 30.762  -14.203 -44.335 1.00 16.91  ?  385  ALA B CB     1 
ATOM   13046 H H      . ALA B 2 385 ? 28.431  -14.803 -42.697 1.00 17.65  ?  385  ALA B H      1 
ATOM   13047 H HA     . ALA B 2 385 ? 29.625  -15.834 -44.869 1.00 17.41  ?  385  ALA B HA     1 
ATOM   13048 H HB1    . ALA B 2 385 ? 31.573  -14.576 -44.713 1.00 20.29  ?  385  ALA B HB1    1 
ATOM   13049 H HB2    . ALA B 2 385 ? 30.356  -13.587 -44.966 1.00 20.29  ?  385  ALA B HB2    1 
ATOM   13050 H HB3    . ALA B 2 385 ? 30.964  -13.741 -43.507 1.00 20.29  ?  385  ALA B HB3    1 
ATOM   13051 N N      . ALA B 2 386 ? 31.227  -17.206 -43.502 1.00 16.99  ?  386  ALA B N      1 
ATOM   13052 C CA     . ALA B 2 386 ? 31.874  -18.153 -42.603 1.00 16.51  ?  386  ALA B CA     1 
ATOM   13053 C C      . ALA B 2 386 ? 33.225  -18.609 -43.145 1.00 18.16  ?  386  ALA B C      1 
ATOM   13054 O O      . ALA B 2 386 ? 33.457  -18.650 -44.362 1.00 18.38  ?  386  ALA B O      1 
ATOM   13055 C CB     . ALA B 2 386 ? 30.995  -19.383 -42.362 1.00 16.89  ?  386  ALA B CB     1 
ATOM   13056 H H      . ALA B 2 386 ? 31.455  -17.277 -44.328 1.00 20.39  ?  386  ALA B H      1 
ATOM   13057 H HA     . ALA B 2 386 ? 32.040  -17.691 -41.766 1.00 19.80  ?  386  ALA B HA     1 
ATOM   13058 H HB1    . ALA B 2 386 ? 31.485  -20.020 -41.820 1.00 20.26  ?  386  ALA B HB1    1 
ATOM   13059 H HB2    . ALA B 2 386 ? 30.187  -19.109 -41.901 1.00 20.26  ?  386  ALA B HB2    1 
ATOM   13060 H HB3    . ALA B 2 386 ? 30.769  -19.782 -43.217 1.00 20.26  ?  386  ALA B HB3    1 
ATOM   13061 N N      . LEU B 2 387 ? 34.105  -18.971 -42.207 1.00 17.74  ?  387  LEU B N      1 
ATOM   13062 C CA     . LEU B 2 387 ? 35.402  -19.571 -42.484 1.00 18.67  ?  387  LEU B CA     1 
ATOM   13063 C C      . LEU B 2 387 ? 35.397  -20.948 -41.842 1.00 19.46  ?  387  LEU B C      1 
ATOM   13064 O O      . LEU B 2 387 ? 35.178  -21.063 -40.633 1.00 21.23  ?  387  LEU B O      1 
ATOM   13065 C CB     . LEU B 2 387 ? 36.525  -18.753 -41.838 1.00 19.45  ?  387  LEU B CB     1 
ATOM   13066 C CG     . LEU B 2 387 ? 36.584  -17.280 -42.199 1.00 19.11  ?  387  LEU B CG     1 
ATOM   13067 C CD1    . LEU B 2 387 ? 37.701  -16.577 -41.459 1.00 21.04  ?  387  LEU B CD1    1 
ATOM   13068 C CD2    . LEU B 2 387 ? 36.761  -17.134 -43.710 1.00 20.86  ?  387  LEU B CD2    1 
ATOM   13069 H H      . LEU B 2 387 ? 33.959  -18.871 -41.365 1.00 21.29  ?  387  LEU B H      1 
ATOM   13070 H HA     . LEU B 2 387 ? 35.545  -19.628 -43.442 1.00 22.40  ?  387  LEU B HA     1 
ATOM   13071 H HB2    . LEU B 2 387 ? 36.420  -18.807 -40.875 1.00 23.34  ?  387  LEU B HB2    1 
ATOM   13072 H HB3    . LEU B 2 387 ? 37.372  -19.145 -42.102 1.00 23.34  ?  387  LEU B HB3    1 
ATOM   13073 H HG     . LEU B 2 387 ? 35.754  -16.853 -41.934 1.00 22.93  ?  387  LEU B HG     1 
ATOM   13074 H HD11   . LEU B 2 387 ? 37.730  -15.649 -41.739 1.00 25.25  ?  387  LEU B HD11   1 
ATOM   13075 H HD12   . LEU B 2 387 ? 37.530  -16.629 -40.506 1.00 25.25  ?  387  LEU B HD12   1 
ATOM   13076 H HD13   . LEU B 2 387 ? 38.542  -17.013 -41.669 1.00 25.25  ?  387  LEU B HD13   1 
ATOM   13077 H HD21   . LEU B 2 387 ? 36.895  -16.197 -43.923 1.00 25.03  ?  387  LEU B HD21   1 
ATOM   13078 H HD22   . LEU B 2 387 ? 37.534  -17.650 -43.989 1.00 25.03  ?  387  LEU B HD22   1 
ATOM   13079 H HD23   . LEU B 2 387 ? 35.965  -17.464 -44.155 1.00 25.03  ?  387  LEU B HD23   1 
ATOM   13080 N N      . GLU B 2 388 ? 35.632  -21.990 -42.631 1.00 18.95  ?  388  GLU B N      1 
ATOM   13081 C CA     . GLU B 2 388 ? 35.754  -23.339 -42.082 1.00 21.12  ?  388  GLU B CA     1 
ATOM   13082 C C      . GLU B 2 388 ? 37.223  -23.732 -42.118 1.00 20.93  ?  388  GLU B C      1 
ATOM   13083 O O      . GLU B 2 388 ? 37.848  -23.691 -43.184 1.00 22.75  ?  388  GLU B O      1 
ATOM   13084 C CB     . GLU B 2 388 ? 34.883  -24.374 -42.791 1.00 20.08  ?  388  GLU B CB     1 
ATOM   13085 C CG     . GLU B 2 388 ? 34.925  -25.714 -42.081 1.00 21.05  ?  388  GLU B CG     1 
ATOM   13086 C CD     . GLU B 2 388 ? 33.762  -26.617 -42.392 1.00 19.61  ?  388  GLU B CD     1 
ATOM   13087 O OE1    . GLU B 2 388 ? 32.829  -26.209 -43.136 1.00 20.19  ?  388  GLU B OE1    1 
ATOM   13088 O OE2    . GLU B 2 388 ? 33.777  -27.747 -41.864 1.00 20.98  -1 388  GLU B OE2    1 
ATOM   13089 H H      . GLU B 2 388 ? 35.725  -21.941 -43.484 1.00 22.73  ?  388  GLU B H      1 
ATOM   13090 H HA     . GLU B 2 388 ? 35.445  -23.324 -41.163 1.00 25.34  ?  388  GLU B HA     1 
ATOM   13091 H HB2    . GLU B 2 388 ? 33.964  -24.064 -42.805 1.00 24.09  ?  388  GLU B HB2    1 
ATOM   13092 H HB3    . GLU B 2 388 ? 35.206  -24.498 -43.697 1.00 24.09  ?  388  GLU B HB3    1 
ATOM   13093 H HG2    . GLU B 2 388 ? 35.735  -26.179 -42.342 1.00 25.25  ?  388  GLU B HG2    1 
ATOM   13094 H HG3    . GLU B 2 388 ? 34.926  -25.558 -41.123 1.00 25.25  ?  388  GLU B HG3    1 
ATOM   13095 N N      . PHE B 2 389 ? 37.767  -24.095 -40.954 1.00 22.72  ?  389  PHE B N      1 
ATOM   13096 C CA     . PHE B 2 389 ? 39.194  -24.333 -40.807 1.00 20.99  ?  389  PHE B CA     1 
ATOM   13097 C C      . PHE B 2 389 ? 39.546  -25.786 -41.073 1.00 25.01  ?  389  PHE B C      1 
ATOM   13098 O O      . PHE B 2 389 ? 38.716  -26.686 -40.931 1.00 26.23  ?  389  PHE B O      1 
ATOM   13099 C CB     . PHE B 2 389 ? 39.647  -23.900 -39.407 1.00 22.20  ?  389  PHE B CB     1 
ATOM   13100 C CG     . PHE B 2 389 ? 39.236  -22.509 -39.078 1.00 20.05  ?  389  PHE B CG     1 
ATOM   13101 C CD1    . PHE B 2 389 ? 39.757  -21.441 -39.789 1.00 20.92  ?  389  PHE B CD1    1 
ATOM   13102 C CD2    . PHE B 2 389 ? 38.286  -22.253 -38.101 1.00 20.35  ?  389  PHE B CD2    1 
ATOM   13103 C CE1    . PHE B 2 389 ? 39.357  -20.149 -39.501 1.00 20.79  ?  389  PHE B CE1    1 
ATOM   13104 C CE2    . PHE B 2 389 ? 37.891  -20.966 -37.834 1.00 20.24  ?  389  PHE B CE2    1 
ATOM   13105 C CZ     . PHE B 2 389 ? 38.425  -19.925 -38.533 1.00 19.48  ?  389  PHE B CZ     1 
ATOM   13106 H H      . PHE B 2 389 ? 37.319  -24.210 -40.229 1.00 27.26  ?  389  PHE B H      1 
ATOM   13107 H HA     . PHE B 2 389 ? 39.685  -23.811 -41.461 1.00 25.18  ?  389  PHE B HA     1 
ATOM   13108 H HB2    . PHE B 2 389 ? 39.252  -24.494 -38.749 1.00 26.64  ?  389  PHE B HB2    1 
ATOM   13109 H HB3    . PHE B 2 389 ? 40.615  -23.947 -39.358 1.00 26.64  ?  389  PHE B HB3    1 
ATOM   13110 H HD1    . PHE B 2 389 ? 40.379  -21.594 -40.464 1.00 25.10  ?  389  PHE B HD1    1 
ATOM   13111 H HD2    . PHE B 2 389 ? 37.914  -22.959 -37.623 1.00 24.41  ?  389  PHE B HD2    1 
ATOM   13112 H HE1    . PHE B 2 389 ? 39.723  -19.433 -39.969 1.00 24.94  ?  389  PHE B HE1    1 
ATOM   13113 H HE2    . PHE B 2 389 ? 37.256  -20.804 -37.173 1.00 24.29  ?  389  PHE B HE2    1 
ATOM   13114 H HZ     . PHE B 2 389 ? 38.151  -19.056 -38.347 1.00 23.37  ?  389  PHE B HZ     1 
ATOM   13115 N N      . SER B 2 390 ? 40.793  -26.005 -41.488 1.00 27.18  ?  390  SER B N      1 
ATOM   13116 C CA     . SER B 2 390 ? 41.240  -27.326 -41.880 1.00 27.25  ?  390  SER B CA     1 
ATOM   13117 C C      . SER B 2 390 ? 42.719  -27.458 -41.595 1.00 30.66  ?  390  SER B C      1 
ATOM   13118 O O      . SER B 2 390 ? 43.455  -26.475 -41.738 1.00 32.04  ?  390  SER B O      1 
ATOM   13119 C CB     . SER B 2 390 ? 40.994  -27.526 -43.383 1.00 29.70  ?  390  SER B CB     1 
ATOM   13120 O OG     . SER B 2 390 ? 41.597  -28.715 -43.864 1.00 30.87  ?  390  SER B OG     1 
ATOM   13121 H H      . SER B 2 390 ? 41.397  -25.395 -41.548 1.00 32.61  ?  390  SER B H      1 
ATOM   13122 H HA     . SER B 2 390 ? 40.780  -28.004 -41.362 1.00 32.69  ?  390  SER B HA     1 
ATOM   13123 H HB2    . SER B 2 390 ? 40.037  -27.577 -43.537 1.00 35.64  ?  390  SER B HB2    1 
ATOM   13124 H HB3    . SER B 2 390 ? 41.368  -26.771 -43.863 1.00 35.64  ?  390  SER B HB3    1 
ATOM   13125 H HG     . SER B 2 390 ? 41.299  -29.378 -43.443 1.00 37.05  ?  390  SER B HG     1 
ATOM   13126 N N      . PRO B 2 391 ? 43.175  -28.647 -41.181 1.00 32.72  ?  391  PRO B N      1 
ATOM   13127 C CA     . PRO B 2 391 ? 44.623  -28.885 -41.082 1.00 35.12  ?  391  PRO B CA     1 
ATOM   13128 C C      . PRO B 2 391 ? 45.295  -29.064 -42.428 1.00 37.75  ?  391  PRO B C      1 
ATOM   13129 O O      . PRO B 2 391 ? 46.529  -29.073 -42.486 1.00 39.63  ?  391  PRO B O      1 
ATOM   13130 C CB     . PRO B 2 391 ? 44.710  -30.179 -40.257 1.00 35.07  ?  391  PRO B CB     1 
ATOM   13131 C CG     . PRO B 2 391 ? 43.460  -30.906 -40.620 1.00 34.48  ?  391  PRO B CG     1 
ATOM   13132 C CD     . PRO B 2 391 ? 42.401  -29.830 -40.753 1.00 33.68  ?  391  PRO B CD     1 
ATOM   13133 H HA     . PRO B 2 391 ? 45.051  -28.162 -40.595 1.00 42.14  ?  391  PRO B HA     1 
ATOM   13134 H HB2    . PRO B 2 391 ? 45.498  -30.686 -40.508 1.00 42.09  ?  391  PRO B HB2    1 
ATOM   13135 H HB3    . PRO B 2 391 ? 44.735  -29.973 -39.309 1.00 42.09  ?  391  PRO B HB3    1 
ATOM   13136 H HG2    . PRO B 2 391 ? 43.583  -31.375 -41.460 1.00 41.37  ?  391  PRO B HG2    1 
ATOM   13137 H HG3    . PRO B 2 391 ? 43.228  -31.535 -39.919 1.00 41.37  ?  391  PRO B HG3    1 
ATOM   13138 H HD2    . PRO B 2 391 ? 41.742  -30.073 -41.422 1.00 40.41  ?  391  PRO B HD2    1 
ATOM   13139 H HD3    . PRO B 2 391 ? 41.964  -29.668 -39.902 1.00 40.41  ?  391  PRO B HD3    1 
ATOM   13140 N N      . ALA B 2 392 ? 44.531  -29.208 -43.498 1.00 40.27  ?  392  ALA B N      1 
ATOM   13141 C CA     . ALA B 2 392 ? 45.063  -29.362 -44.844 1.00 41.48  ?  392  ALA B CA     1 
ATOM   13142 C C      . ALA B 2 392 ? 43.968  -28.964 -45.826 1.00 41.56  ?  392  ALA B C      1 
ATOM   13143 O O      . ALA B 2 392 ? 43.239  -29.826 -46.334 1.00 42.62  ?  392  ALA B O      1 
ATOM   13144 C CB     . ALA B 2 392 ? 45.510  -30.802 -45.070 1.00 43.39  ?  392  ALA B CB     1 
ATOM   13145 H H      . ALA B 2 392 ? 43.672  -29.220 -43.472 1.00 48.32  ?  392  ALA B H      1 
ATOM   13146 H HA     . ALA B 2 392 ? 45.837  -28.794 -44.984 1.00 49.77  ?  392  ALA B HA     1 
ATOM   13147 H HB1    . ALA B 2 392 ? 45.849  -30.890 -45.975 1.00 52.07  ?  392  ALA B HB1    1 
ATOM   13148 H HB2    . ALA B 2 392 ? 46.209  -31.020 -44.433 1.00 52.07  ?  392  ALA B HB2    1 
ATOM   13149 H HB3    . ALA B 2 392 ? 44.751  -31.392 -44.944 1.00 52.07  ?  392  ALA B HB3    1 
ATOM   13150 N N      . PRO B 2 393 ? 43.822  -27.668 -46.108 1.00 39.72  ?  393  PRO B N      1 
ATOM   13151 C CA     . PRO B 2 393 ? 42.682  -27.217 -46.926 1.00 39.47  ?  393  PRO B CA     1 
ATOM   13152 C C      . PRO B 2 393 ? 42.483  -27.995 -48.216 1.00 42.66  ?  393  PRO B C      1 
ATOM   13153 O O      . PRO B 2 393 ? 41.341  -28.207 -48.637 1.00 42.27  ?  393  PRO B O      1 
ATOM   13154 C CB     . PRO B 2 393 ? 43.020  -25.745 -47.196 1.00 38.87  ?  393  PRO B CB     1 
ATOM   13155 C CG     . PRO B 2 393 ? 43.841  -25.329 -45.994 1.00 39.27  ?  393  PRO B CG     1 
ATOM   13156 C CD     . PRO B 2 393 ? 44.625  -26.543 -45.584 1.00 38.55  ?  393  PRO B CD     1 
ATOM   13157 H HA     . PRO B 2 393 ? 41.869  -27.278 -46.401 1.00 47.36  ?  393  PRO B HA     1 
ATOM   13158 H HB2    . PRO B 2 393 ? 43.533  -25.665 -48.016 1.00 46.64  ?  393  PRO B HB2    1 
ATOM   13159 H HB3    . PRO B 2 393 ? 42.206  -25.222 -47.262 1.00 46.64  ?  393  PRO B HB3    1 
ATOM   13160 H HG2    . PRO B 2 393 ? 44.437  -24.604 -46.240 1.00 47.12  ?  393  PRO B HG2    1 
ATOM   13161 H HG3    . PRO B 2 393 ? 43.251  -25.045 -45.278 1.00 47.12  ?  393  PRO B HG3    1 
ATOM   13162 H HD2    . PRO B 2 393 ? 45.508  -26.534 -45.985 1.00 46.26  ?  393  PRO B HD2    1 
ATOM   13163 H HD3    . PRO B 2 393 ? 44.701  -26.594 -44.618 1.00 46.26  ?  393  PRO B HD3    1 
ATOM   13164 N N      . ALA B 2 394 ? 43.571  -28.430 -48.856 1.00 45.18  ?  394  ALA B N      1 
ATOM   13165 C CA     . ALA B 2 394 ? 43.446  -29.082 -50.155 1.00 47.69  ?  394  ALA B CA     1 
ATOM   13166 C C      . ALA B 2 394 ? 42.818  -30.467 -50.065 1.00 50.55  ?  394  ALA B C      1 
ATOM   13167 O O      . ALA B 2 394 ? 42.285  -30.956 -51.069 1.00 51.66  ?  394  ALA B O      1 
ATOM   13168 C CB     . ALA B 2 394 ? 44.817  -29.179 -50.820 1.00 48.64  ?  394  ALA B CB     1 
ATOM   13169 H H      . ALA B 2 394 ? 44.377  -28.361 -48.565 1.00 54.21  ?  394  ALA B H      1 
ATOM   13170 H HA     . ALA B 2 394 ? 42.871  -28.538 -50.715 1.00 57.22  ?  394  ALA B HA     1 
ATOM   13171 H HB1    . ALA B 2 394 ? 44.718  -29.601 -51.687 1.00 58.36  ?  394  ALA B HB1    1 
ATOM   13172 H HB2    . ALA B 2 394 ? 45.180  -28.286 -50.927 1.00 58.36  ?  394  ALA B HB2    1 
ATOM   13173 H HB3    . ALA B 2 394 ? 45.404  -29.709 -50.259 1.00 58.36  ?  394  ALA B HB3    1 
ATOM   13174 N N      . ARG B 2 395 ? 42.878  -31.114 -48.907 1.00 52.27  ?  395  ARG B N      1 
ATOM   13175 C CA     . ARG B 2 395 ? 42.254  -32.418 -48.727 1.00 53.20  ?  395  ARG B CA     1 
ATOM   13176 C C      . ARG B 2 395 ? 40.838  -32.318 -48.174 1.00 49.14  ?  395  ARG B C      1 
ATOM   13177 O O      . ARG B 2 395 ? 40.211  -33.351 -47.925 1.00 49.94  ?  395  ARG B O      1 
ATOM   13178 C CB     . ARG B 2 395 ? 43.089  -33.293 -47.775 1.00 57.96  ?  395  ARG B CB     1 
ATOM   13179 C CG     . ARG B 2 395 ? 44.570  -33.415 -48.129 1.00 61.84  ?  395  ARG B CG     1 
ATOM   13180 C CD     . ARG B 2 395 ? 45.219  -34.666 -47.503 1.00 65.12  ?  395  ARG B CD     1 
ATOM   13181 N NE     . ARG B 2 395 ? 45.484  -34.563 -46.063 1.00 67.87  ?  395  ARG B NE     1 
ATOM   13182 C CZ     . ARG B 2 395 ? 44.815  -35.220 -45.109 1.00 69.18  ?  395  ARG B CZ     1 
ATOM   13183 N NH1    . ARG B 2 395 ? 43.816  -36.038 -45.420 1.00 69.48  ?  395  ARG B NH1    1 
ATOM   13184 N NH2    . ARG B 2 395 ? 45.151  -35.056 -43.834 1.00 68.98  ?  395  ARG B NH2    1 
ATOM   13185 H H      . ARG B 2 395 ? 43.278  -30.816 -48.206 1.00 62.72  ?  395  ARG B H      1 
ATOM   13186 H HA     . ARG B 2 395 ? 42.224  -32.857 -49.592 1.00 63.83  ?  395  ARG B HA     1 
ATOM   13187 H HB2    . ARG B 2 395 ? 43.035  -32.913 -46.884 1.00 69.55  ?  395  ARG B HB2    1 
ATOM   13188 H HB3    . ARG B 2 395 ? 42.716  -34.188 -47.777 1.00 69.55  ?  395  ARG B HB3    1 
ATOM   13189 H HG2    . ARG B 2 395 ? 44.663  -33.476 -49.092 1.00 74.21  ?  395  ARG B HG2    1 
ATOM   13190 H HG3    . ARG B 2 395 ? 45.042  -32.634 -47.799 1.00 74.21  ?  395  ARG B HG3    1 
ATOM   13191 H HD2    . ARG B 2 395 ? 44.625  -35.422 -47.637 1.00 78.14  ?  395  ARG B HD2    1 
ATOM   13192 H HD3    . ARG B 2 395 ? 46.067  -34.828 -47.945 1.00 78.14  ?  395  ARG B HD3    1 
ATOM   13193 H HE     . ARG B 2 395 ? 46.119  -34.040 -45.813 1.00 81.44  ?  395  ARG B HE     1 
ATOM   13194 H HH11   . ARG B 2 395 ? 43.592  -36.151 -46.242 1.00 83.38  ?  395  ARG B HH11   1 
ATOM   13195 H HH12   . ARG B 2 395 ? 43.392  -36.455 -44.798 1.00 83.38  ?  395  ARG B HH12   1 
ATOM   13196 H HH21   . ARG B 2 395 ? 45.797  -34.528 -43.624 1.00 82.77  ?  395  ARG B HH21   1 
ATOM   13197 H HH22   . ARG B 2 395 ? 44.722  -35.477 -43.219 1.00 82.77  ?  395  ARG B HH22   1 
ATOM   13198 N N      . ARG B 2 396 ? 40.321  -31.106 -47.972 1.00 44.96  ?  396  ARG B N      1 
ATOM   13199 C CA     . ARG B 2 396 ? 39.085  -30.921 -47.218 1.00 41.87  ?  396  ARG B CA     1 
ATOM   13200 C C      . ARG B 2 396 ? 39.168  -31.672 -45.897 1.00 42.86  ?  396  ARG B C      1 
ATOM   13201 O O      . ARG B 2 396 ? 38.190  -32.263 -45.424 1.00 46.48  ?  396  ARG B O      1 
ATOM   13202 C CB     . ARG B 2 396 ? 37.848  -31.360 -48.001 1.00 37.52  ?  396  ARG B CB     1 
ATOM   13203 C CG     . ARG B 2 396 ? 37.612  -30.578 -49.249 1.00 34.67  ?  396  ARG B CG     1 
ATOM   13204 C CD     . ARG B 2 396 ? 36.237  -30.858 -49.806 1.00 31.37  ?  396  ARG B CD     1 
ATOM   13205 N NE     . ARG B 2 396 ? 36.084  -32.216 -50.321 1.00 29.75  ?  396  ARG B NE     1 
ATOM   13206 C CZ     . ARG B 2 396 ? 35.187  -33.106 -49.884 1.00 28.40  ?  396  ARG B CZ     1 
ATOM   13207 N NH1    . ARG B 2 396 ? 34.353  -32.807 -48.897 1.00 26.92  ?  396  ARG B NH1    1 
ATOM   13208 N NH2    . ARG B 2 396 ? 35.123  -34.310 -50.446 1.00 29.13  ?  396  ARG B NH2    1 
ATOM   13209 H H      . ARG B 2 396 ? 40.669  -30.376 -48.262 1.00 53.95  ?  396  ARG B H      1 
ATOM   13210 H HA     . ARG B 2 396 ? 38.984  -29.972 -47.043 1.00 50.24  ?  396  ARG B HA     1 
ATOM   13211 H HB2    . ARG B 2 396 ? 37.953  -32.291 -48.252 1.00 45.03  ?  396  ARG B HB2    1 
ATOM   13212 H HB3    . ARG B 2 396 ? 37.068  -31.254 -47.435 1.00 45.03  ?  396  ARG B HB3    1 
ATOM   13213 H HG2    . ARG B 2 396 ? 37.678  -29.630 -49.055 1.00 41.60  ?  396  ARG B HG2    1 
ATOM   13214 H HG3    . ARG B 2 396 ? 38.271  -30.826 -49.917 1.00 41.60  ?  396  ARG B HG3    1 
ATOM   13215 H HD2    . ARG B 2 396 ? 35.582  -30.732 -49.102 1.00 37.64  ?  396  ARG B HD2    1 
ATOM   13216 H HD3    . ARG B 2 396 ? 36.063  -30.243 -50.535 1.00 37.64  ?  396  ARG B HD3    1 
ATOM   13217 H HE     . ARG B 2 396 ? 36.611  -32.463 -50.954 1.00 35.69  ?  396  ARG B HE     1 
ATOM   13218 H HH11   . ARG B 2 396 ? 34.384  -32.030 -48.529 1.00 32.30  ?  396  ARG B HH11   1 
ATOM   13219 H HH12   . ARG B 2 396 ? 33.781  -33.389 -48.626 1.00 32.30  ?  396  ARG B HH12   1 
ATOM   13220 H HH21   . ARG B 2 396 ? 35.658  -34.514 -51.089 1.00 34.95  ?  396  ARG B HH21   1 
ATOM   13221 H HH22   . ARG B 2 396 ? 34.548  -34.885 -50.168 1.00 34.95  ?  396  ARG B HH22   1 
ATOM   13222 N N      . ALA B 2 397 ? 40.356  -31.677 -45.309 1.00 38.58  ?  397  ALA B N      1 
ATOM   13223 C CA     . ALA B 2 397 ? 40.556  -32.402 -44.075 1.00 36.47  ?  397  ALA B CA     1 
ATOM   13224 C C      . ALA B 2 397 ? 39.915  -31.641 -42.924 1.00 35.66  ?  397  ALA B C      1 
ATOM   13225 O O      . ALA B 2 397 ? 39.763  -30.413 -42.955 1.00 34.81  ?  397  ALA B O      1 
ATOM   13226 C CB     . ALA B 2 397 ? 42.048  -32.575 -43.799 1.00 36.88  ?  397  ALA B CB     1 
ATOM   13227 H H      . ALA B 2 397 ? 41.054  -31.271 -45.605 1.00 46.30  ?  397  ALA B H      1 
ATOM   13228 H HA     . ALA B 2 397 ? 40.155  -33.283 -44.140 1.00 43.77  ?  397  ALA B HA     1 
ATOM   13229 H HB1    . ALA B 2 397 ? 42.161  -33.070 -42.972 1.00 44.26  ?  397  ALA B HB1    1 
ATOM   13230 H HB2    . ALA B 2 397 ? 42.451  -33.063 -44.534 1.00 44.26  ?  397  ALA B HB2    1 
ATOM   13231 H HB3    . ALA B 2 397 ? 42.458  -31.700 -43.719 1.00 44.26  ?  397  ALA B HB3    1 
ATOM   13232 N N      . PHE B 2 398 ? 39.555  -32.385 -41.893 1.00 35.84  ?  398  PHE B N      1 
ATOM   13233 C CA     . PHE B 2 398 ? 38.936  -31.825 -40.708 1.00 37.14  ?  398  PHE B CA     1 
ATOM   13234 C C      . PHE B 2 398 ? 39.832  -32.061 -39.509 1.00 36.30  ?  398  PHE B C      1 
ATOM   13235 O O      . PHE B 2 398 ? 40.547  -33.062 -39.434 1.00 36.66  ?  398  PHE B O      1 
ATOM   13236 C CB     . PHE B 2 398 ? 37.567  -32.444 -40.507 1.00 39.56  ?  398  PHE B CB     1 
ATOM   13237 C CG     . PHE B 2 398 ? 36.678  -32.282 -41.697 1.00 42.73  ?  398  PHE B CG     1 
ATOM   13238 C CD1    . PHE B 2 398 ? 35.978  -31.114 -41.889 1.00 42.24  ?  398  PHE B CD1    1 
ATOM   13239 C CD2    . PHE B 2 398 ? 36.578  -33.281 -42.648 1.00 45.48  ?  398  PHE B CD2    1 
ATOM   13240 C CE1    . PHE B 2 398 ? 35.172  -30.951 -42.991 1.00 43.67  ?  398  PHE B CE1    1 
ATOM   13241 C CE2    . PHE B 2 398 ? 35.773  -33.125 -43.754 1.00 45.79  ?  398  PHE B CE2    1 
ATOM   13242 C CZ     . PHE B 2 398 ? 35.073  -31.962 -43.926 1.00 44.46  ?  398  PHE B CZ     1 
ATOM   13243 H H      . PHE B 2 398 ? 39.663  -33.238 -41.858 1.00 43.00  ?  398  PHE B H      1 
ATOM   13244 H HA     . PHE B 2 398 ? 38.823  -30.865 -40.789 1.00 44.56  ?  398  PHE B HA     1 
ATOM   13245 H HB2    . PHE B 2 398 ? 37.671  -33.393 -40.338 1.00 47.47  ?  398  PHE B HB2    1 
ATOM   13246 H HB3    . PHE B 2 398 ? 37.136  -32.017 -39.750 1.00 47.47  ?  398  PHE B HB3    1 
ATOM   13247 H HD1    . PHE B 2 398 ? 36.051  -30.426 -41.266 1.00 50.69  ?  398  PHE B HD1    1 
ATOM   13248 H HD2    . PHE B 2 398 ? 37.062  -34.068 -42.539 1.00 54.57  ?  398  PHE B HD2    1 
ATOM   13249 H HE1    . PHE B 2 398 ? 34.694  -30.162 -43.106 1.00 52.40  ?  398  PHE B HE1    1 
ATOM   13250 H HE2    . PHE B 2 398 ? 35.705  -33.808 -44.381 1.00 54.94  ?  398  PHE B HE2    1 
ATOM   13251 H HZ     . PHE B 2 398 ? 34.530  -31.852 -44.673 1.00 53.35  ?  398  PHE B HZ     1 
ATOM   13252 N N      . PHE B 2 399 ? 39.810  -31.098 -38.595 1.00 35.63  ?  399  PHE B N      1 
ATOM   13253 C CA     . PHE B 2 399 ? 40.585  -31.195 -37.372 1.00 36.02  ?  399  PHE B CA     1 
ATOM   13254 C C      . PHE B 2 399 ? 39.964  -32.218 -36.432 1.00 35.68  ?  399  PHE B C      1 
ATOM   13255 O O      . PHE B 2 399 ? 38.755  -32.455 -36.445 1.00 36.62  ?  399  PHE B O      1 
ATOM   13256 C CB     . PHE B 2 399 ? 40.599  -29.842 -36.650 1.00 35.24  ?  399  PHE B CB     1 
ATOM   13257 C CG     . PHE B 2 399 ? 41.619  -28.881 -37.182 1.00 34.58  ?  399  PHE B CG     1 
ATOM   13258 C CD1    . PHE B 2 399 ? 42.968  -29.107 -36.968 1.00 34.33  ?  399  PHE B CD1    1 
ATOM   13259 C CD2    . PHE B 2 399 ? 41.239  -27.754 -37.885 1.00 32.62  ?  399  PHE B CD2    1 
ATOM   13260 C CE1    . PHE B 2 399 ? 43.922  -28.228 -37.458 1.00 34.24  ?  399  PHE B CE1    1 
ATOM   13261 C CE2    . PHE B 2 399 ? 42.187  -26.870 -38.375 1.00 33.01  ?  399  PHE B CE2    1 
ATOM   13262 C CZ     . PHE B 2 399 ? 43.526  -27.110 -38.165 1.00 33.73  ?  399  PHE B CZ     1 
ATOM   13263 H H      . PHE B 2 399 ? 39.352  -30.374 -38.661 1.00 42.75  ?  399  PHE B H      1 
ATOM   13264 H HA     . PHE B 2 399 ? 41.493  -31.459 -37.591 1.00 43.22  ?  399  PHE B HA     1 
ATOM   13265 H HB2    . PHE B 2 399 ? 39.726  -29.429 -36.746 1.00 42.29  ?  399  PHE B HB2    1 
ATOM   13266 H HB3    . PHE B 2 399 ? 40.794  -29.992 -35.712 1.00 42.29  ?  399  PHE B HB3    1 
ATOM   13267 H HD1    . PHE B 2 399 ? 43.238  -29.857 -36.490 1.00 41.19  ?  399  PHE B HD1    1 
ATOM   13268 H HD2    . PHE B 2 399 ? 40.336  -27.587 -38.032 1.00 39.13  ?  399  PHE B HD2    1 
ATOM   13269 H HE1    . PHE B 2 399 ? 44.825  -28.391 -37.311 1.00 41.08  ?  399  PHE B HE1    1 
ATOM   13270 H HE2    . PHE B 2 399 ? 41.918  -26.115 -38.846 1.00 39.60  ?  399  PHE B HE2    1 
ATOM   13271 H HZ     . PHE B 2 399 ? 44.163  -26.520 -38.499 1.00 40.47  ?  399  PHE B HZ     1 
ATOM   13272 N N      . ASP B 2 400 ? 40.798  -32.817 -35.604 1.00 36.72  ?  400  ASP B N      1 
ATOM   13273 C CA     . ASP B 2 400 ? 40.313  -33.525 -34.427 1.00 37.41  ?  400  ASP B CA     1 
ATOM   13274 C C      . ASP B 2 400 ? 39.493  -32.540 -33.599 1.00 34.24  ?  400  ASP B C      1 
ATOM   13275 O O      . ASP B 2 400 ? 40.011  -31.474 -33.227 1.00 33.89  ?  400  ASP B O      1 
ATOM   13276 C CB     . ASP B 2 400 ? 41.520  -34.023 -33.638 1.00 40.64  ?  400  ASP B CB     1 
ATOM   13277 C CG     . ASP B 2 400 ? 41.135  -34.768 -32.370 1.00 43.52  ?  400  ASP B CG     1 
ATOM   13278 O OD1    . ASP B 2 400 ? 39.939  -34.830 -32.022 1.00 44.39  ?  400  ASP B OD1    1 
ATOM   13279 O OD2    . ASP B 2 400 ? 42.047  -35.293 -31.707 1.00 46.82  -1 400  ASP B OD2    1 
ATOM   13280 H H      . ASP B 2 400 ? 41.653  -32.830 -35.696 1.00 44.06  ?  400  ASP B H      1 
ATOM   13281 H HA     . ASP B 2 400 ? 39.758  -34.287 -34.657 1.00 44.89  ?  400  ASP B HA     1 
ATOM   13282 H HB2    . ASP B 2 400 ? 42.033  -34.629 -34.196 1.00 48.76  ?  400  ASP B HB2    1 
ATOM   13283 H HB3    . ASP B 2 400 ? 42.066  -33.263 -33.384 1.00 48.76  ?  400  ASP B HB3    1 
ATOM   13284 N N      . PRO B 2 401 ? 38.225  -32.833 -33.305 1.00 34.25  ?  401  PRO B N      1 
ATOM   13285 C CA     . PRO B 2 401 ? 37.420  -31.868 -32.538 1.00 34.97  ?  401  PRO B CA     1 
ATOM   13286 C C      . PRO B 2 401 ? 38.029  -31.518 -31.196 1.00 35.43  ?  401  PRO B C      1 
ATOM   13287 O O      . PRO B 2 401 ? 37.749  -30.435 -30.668 1.00 35.26  ?  401  PRO B O      1 
ATOM   13288 C CB     . PRO B 2 401 ? 36.063  -32.570 -32.375 1.00 35.69  ?  401  PRO B CB     1 
ATOM   13289 C CG     . PRO B 2 401 ? 36.028  -33.601 -33.450 1.00 37.24  ?  401  PRO B CG     1 
ATOM   13290 C CD     . PRO B 2 401 ? 37.452  -34.041 -33.660 1.00 36.64  ?  401  PRO B CD     1 
ATOM   13291 H HA     . PRO B 2 401 ? 37.290  -31.059 -33.057 1.00 41.97  ?  401  PRO B HA     1 
ATOM   13292 H HB2    . PRO B 2 401 ? 36.008  -32.981 -31.498 1.00 42.83  ?  401  PRO B HB2    1 
ATOM   13293 H HB3    . PRO B 2 401 ? 35.345  -31.928 -32.487 1.00 42.83  ?  401  PRO B HB3    1 
ATOM   13294 H HG2    . PRO B 2 401 ? 35.477  -34.348 -33.166 1.00 44.68  ?  401  PRO B HG2    1 
ATOM   13295 H HG3    . PRO B 2 401 ? 35.666  -33.213 -34.262 1.00 44.68  ?  401  PRO B HG3    1 
ATOM   13296 H HD2    . PRO B 2 401 ? 37.677  -34.781 -33.074 1.00 43.96  ?  401  PRO B HD2    1 
ATOM   13297 H HD3    . PRO B 2 401 ? 37.605  -34.291 -34.584 1.00 43.96  ?  401  PRO B HD3    1 
ATOM   13298 N N      . ALA B 2 402 ? 38.856  -32.401 -30.631 1.00 35.69  ?  402  ALA B N      1 
ATOM   13299 C CA     . ALA B 2 402 ? 39.458  -32.168 -29.324 1.00 34.84  ?  402  ALA B CA     1 
ATOM   13300 C C      . ALA B 2 402 ? 40.406  -30.981 -29.315 1.00 32.60  ?  402  ALA B C      1 
ATOM   13301 O O      . ALA B 2 402 ? 40.685  -30.432 -28.235 1.00 32.90  ?  402  ALA B O      1 
ATOM   13302 C CB     . ALA B 2 402 ? 40.224  -33.422 -28.883 1.00 35.44  ?  402  ALA B CB     1 
ATOM   13303 H H      . ALA B 2 402 ? 39.087  -33.149 -30.988 1.00 42.82  ?  402  ALA B H      1 
ATOM   13304 H HA     . ALA B 2 402 ? 38.748  -31.987 -28.689 1.00 41.80  ?  402  ALA B HA     1 
ATOM   13305 H HB1    . ALA B 2 402 ? 40.653  -33.246 -28.031 1.00 42.53  ?  402  ALA B HB1    1 
ATOM   13306 H HB2    . ALA B 2 402 ? 39.599  -34.158 -28.793 1.00 42.53  ?  402  ALA B HB2    1 
ATOM   13307 H HB3    . ALA B 2 402 ? 40.893  -33.635 -29.553 1.00 42.53  ?  402  ALA B HB3    1 
ATOM   13308 N N      . LEU B 2 403 ? 40.919  -30.589 -30.481 1.00 30.60  ?  403  LEU B N      1 
ATOM   13309 C CA     . LEU B 2 403 ? 41.779  -29.413 -30.574 1.00 28.69  ?  403  LEU B CA     1 
ATOM   13310 C C      . LEU B 2 403 ? 40.996  -28.121 -30.387 1.00 27.01  ?  403  LEU B C      1 
ATOM   13311 O O      . LEU B 2 403 ? 41.594  -27.080 -30.073 1.00 27.58  ?  403  LEU B O      1 
ATOM   13312 C CB     . LEU B 2 403 ? 42.493  -29.387 -31.930 1.00 30.63  ?  403  LEU B CB     1 
ATOM   13313 C CG     . LEU B 2 403 ? 43.501  -30.497 -32.236 1.00 32.86  ?  403  LEU B CG     1 
ATOM   13314 C CD1    . LEU B 2 403 ? 44.055  -30.349 -33.643 1.00 34.23  ?  403  LEU B CD1    1 
ATOM   13315 C CD2    . LEU B 2 403 ? 44.638  -30.504 -31.212 1.00 33.86  ?  403  LEU B CD2    1 
ATOM   13316 H H      . LEU B 2 403 ? 40.786  -30.985 -31.233 1.00 36.72  ?  403  LEU B H      1 
ATOM   13317 H HA     . LEU B 2 403 ? 42.454  -29.465 -29.879 1.00 34.42  ?  403  LEU B HA     1 
ATOM   13318 H HB2    . LEU B 2 403 ? 41.813  -29.431 -32.620 1.00 36.75  ?  403  LEU B HB2    1 
ATOM   13319 H HB3    . LEU B 2 403 ? 42.975  -28.548 -31.992 1.00 36.75  ?  403  LEU B HB3    1 
ATOM   13320 H HG     . LEU B 2 403 ? 43.044  -31.351 -32.179 1.00 39.43  ?  403  LEU B HG     1 
ATOM   13321 H HD11   . LEU B 2 403 ? 44.704  -31.052 -33.802 1.00 41.07  ?  403  LEU B HD11   1 
ATOM   13322 H HD12   . LEU B 2 403 ? 43.326  -30.421 -34.278 1.00 41.07  ?  403  LEU B HD12   1 
ATOM   13323 H HD13   . LEU B 2 403 ? 44.481  -29.481 -33.725 1.00 41.07  ?  403  LEU B HD13   1 
ATOM   13324 H HD21   . LEU B 2 403 ? 45.353  -31.074 -31.538 1.00 40.62  ?  403  LEU B HD21   1 
ATOM   13325 H HD22   . LEU B 2 403 ? 44.965  -29.598 -31.097 1.00 40.62  ?  403  LEU B HD22   1 
ATOM   13326 H HD23   . LEU B 2 403 ? 44.302  -30.845 -30.369 1.00 40.62  ?  403  LEU B HD23   1 
ATOM   13327 N N      . LYS B 2 404 ? 39.680  -28.155 -30.579 1.00 26.69  ?  404  LYS B N      1 
ATOM   13328 C CA     . LYS B 2 404 ? 38.830  -26.985 -30.343 1.00 26.94  ?  404  LYS B CA     1 
ATOM   13329 C C      . LYS B 2 404 ? 39.269  -25.787 -31.183 1.00 24.12  ?  404  LYS B C      1 
ATOM   13330 O O      . LYS B 2 404 ? 39.288  -24.655 -30.710 1.00 22.28  ?  404  LYS B O      1 
ATOM   13331 C CB     . LYS B 2 404 ? 38.786  -26.618 -28.858 1.00 31.62  ?  404  LYS B CB     1 
ATOM   13332 C CG     . LYS B 2 404 ? 38.386  -27.761 -27.939 1.00 38.97  ?  404  LYS B CG     1 
ATOM   13333 C CD     . LYS B 2 404 ? 36.922  -27.700 -27.578 1.00 46.33  ?  404  LYS B CD     1 
ATOM   13334 C CE     . LYS B 2 404 ? 36.705  -26.909 -26.290 1.00 52.03  ?  404  LYS B CE     1 
ATOM   13335 N NZ     . LYS B 2 404 ? 36.865  -27.767 -25.084 1.00 54.69  ?  404  LYS B NZ     1 
ATOM   13336 H H      . LYS B 2 404 ? 39.250  -28.850 -30.847 1.00 32.02  ?  404  LYS B H      1 
ATOM   13337 H HA     . LYS B 2 404 ? 37.930  -27.213 -30.623 1.00 32.32  ?  404  LYS B HA     1 
ATOM   13338 H HB2    . LYS B 2 404 ? 39.668  -26.319 -28.586 1.00 37.94  ?  404  LYS B HB2    1 
ATOM   13339 H HB3    . LYS B 2 404 ? 38.141  -25.904 -28.734 1.00 37.94  ?  404  LYS B HB3    1 
ATOM   13340 H HG2    . LYS B 2 404 ? 38.554  -28.605 -28.386 1.00 46.76  ?  404  LYS B HG2    1 
ATOM   13341 H HG3    . LYS B 2 404 ? 38.904  -27.710 -27.120 1.00 46.76  ?  404  LYS B HG3    1 
ATOM   13342 H HD2    . LYS B 2 404 ? 36.432  -27.264 -28.292 1.00 55.59  ?  404  LYS B HD2    1 
ATOM   13343 H HD3    . LYS B 2 404 ? 36.585  -28.600 -27.445 1.00 55.59  ?  404  LYS B HD3    1 
ATOM   13344 H HE2    . LYS B 2 404 ? 37.355  -26.191 -26.241 1.00 62.44  ?  404  LYS B HE2    1 
ATOM   13345 H HE3    . LYS B 2 404 ? 35.806  -26.543 -26.287 1.00 62.44  ?  404  LYS B HE3    1 
ATOM   13346 H HZ1    . LYS B 2 404 ? 36.741  -27.284 -24.348 1.00 65.62  ?  404  LYS B HZ1    1 
ATOM   13347 H HZ2    . LYS B 2 404 ? 36.269  -28.428 -25.100 1.00 65.62  ?  404  LYS B HZ2    1 
ATOM   13348 H HZ3    . LYS B 2 404 ? 37.683  -28.117 -25.066 1.00 65.62  ?  404  LYS B HZ3    1 
ATOM   13349 N N      . VAL B 2 405 ? 39.576  -26.017 -32.461 1.00 23.16  ?  405  VAL B N      1 
ATOM   13350 C CA     . VAL B 2 405 ? 40.103  -24.929 -33.287 1.00 21.47  ?  405  VAL B CA     1 
ATOM   13351 C C      . VAL B 2 405 ? 39.075  -23.808 -33.433 1.00 19.98  ?  405  VAL B C      1 
ATOM   13352 O O      . VAL B 2 405 ? 39.396  -22.628 -33.268 1.00 19.39  ?  405  VAL B O      1 
ATOM   13353 C CB     . VAL B 2 405 ? 40.588  -25.461 -34.649 1.00 20.94  ?  405  VAL B CB     1 
ATOM   13354 C CG1    . VAL B 2 405 ? 41.008  -24.305 -35.536 1.00 22.00  ?  405  VAL B CG1    1 
ATOM   13355 C CG2    . VAL B 2 405 ? 41.737  -26.450 -34.439 1.00 21.56  ?  405  VAL B CG2    1 
ATOM   13356 H H      . VAL B 2 405 ? 39.492  -26.772 -32.864 1.00 27.79  ?  405  VAL B H      1 
ATOM   13357 H HA     . VAL B 2 405 ? 40.873  -24.551 -32.834 1.00 25.75  ?  405  VAL B HA     1 
ATOM   13358 H HB     . VAL B 2 405 ? 39.867  -25.932 -35.096 1.00 25.13  ?  405  VAL B HB     1 
ATOM   13359 H HG11   . VAL B 2 405 ? 41.519  -24.651 -36.285 1.00 26.40  ?  405  VAL B HG11   1 
ATOM   13360 H HG12   . VAL B 2 405 ? 40.214  -23.850 -35.859 1.00 26.40  ?  405  VAL B HG12   1 
ATOM   13361 H HG13   . VAL B 2 405 ? 41.553  -23.692 -35.019 1.00 26.40  ?  405  VAL B HG13   1 
ATOM   13362 H HG21   . VAL B 2 405 ? 42.052  -26.758 -35.303 1.00 25.86  ?  405  VAL B HG21   1 
ATOM   13363 H HG22   . VAL B 2 405 ? 42.456  -26.003 -33.966 1.00 25.86  ?  405  VAL B HG22   1 
ATOM   13364 H HG23   . VAL B 2 405 ? 41.416  -27.202 -33.917 1.00 25.86  ?  405  VAL B HG23   1 
ATOM   13365 N N      . GLY B 2 406 ? 37.837  -24.153 -33.765 1.00 19.94  ?  406  GLY B N      1 
ATOM   13366 C CA     . GLY B 2 406 ? 36.805  -23.156 -33.951 1.00 19.64  ?  406  GLY B CA     1 
ATOM   13367 C C      . GLY B 2 406 ? 36.616  -22.302 -32.717 1.00 20.99  ?  406  GLY B C      1 
ATOM   13368 O O      . GLY B 2 406 ? 36.684  -21.074 -32.764 1.00 19.67  ?  406  GLY B O      1 
ATOM   13369 H H      . GLY B 2 406 ? 37.574  -24.963 -33.888 1.00 23.92  ?  406  GLY B H      1 
ATOM   13370 H HA2    . GLY B 2 406 ? 37.045  -22.577 -34.692 1.00 23.56  ?  406  GLY B HA2    1 
ATOM   13371 H HA3    . GLY B 2 406 ? 35.965  -23.596 -34.153 1.00 23.56  ?  406  GLY B HA3    1 
ATOM   13372 N N      . PRO B 2 407 ? 36.358  -22.943 -31.576 1.00 19.55  ?  407  PRO B N      1 
ATOM   13373 C CA     . PRO B 2 407 ? 36.204  -22.157 -30.335 1.00 19.27  ?  407  PRO B CA     1 
ATOM   13374 C C      . PRO B 2 407 ? 37.418  -21.304 -30.031 1.00 20.37  ?  407  PRO B C      1 
ATOM   13375 O O      . PRO B 2 407 ? 37.274  -20.171 -29.550 1.00 21.63  ?  407  PRO B O      1 
ATOM   13376 C CB     . PRO B 2 407 ? 35.950  -23.237 -29.273 1.00 19.81  ?  407  PRO B CB     1 
ATOM   13377 C CG     . PRO B 2 407 ? 35.258  -24.323 -30.039 1.00 19.40  ?  407  PRO B CG     1 
ATOM   13378 C CD     . PRO B 2 407 ? 35.941  -24.344 -31.397 1.00 20.42  ?  407  PRO B CD     1 
ATOM   13379 H HA     . PRO B 2 407 ? 35.422  -21.586 -30.386 1.00 23.13  ?  407  PRO B HA     1 
ATOM   13380 H HB2    . PRO B 2 407 ? 36.791  -23.548 -28.902 1.00 23.77  ?  407  PRO B HB2    1 
ATOM   13381 H HB3    . PRO B 2 407 ? 35.384  -22.888 -28.567 1.00 23.77  ?  407  PRO B HB3    1 
ATOM   13382 H HG2    . PRO B 2 407 ? 35.368  -25.172 -29.583 1.00 23.28  ?  407  PRO B HG2    1 
ATOM   13383 H HG3    . PRO B 2 407 ? 34.315  -24.115 -30.129 1.00 23.28  ?  407  PRO B HG3    1 
ATOM   13384 H HD2    . PRO B 2 407 ? 36.710  -24.936 -31.389 1.00 24.50  ?  407  PRO B HD2    1 
ATOM   13385 H HD3    . PRO B 2 407 ? 35.322  -24.613 -32.093 1.00 24.50  ?  407  PRO B HD3    1 
ATOM   13386 N N      . ARG B 2 408 ? 38.617  -21.806 -30.327 1.00 20.54  ?  408  ARG B N      1 
ATOM   13387 C CA     . ARG B 2 408 ? 39.824  -21.034 -30.064 1.00 20.66  ?  408  ARG B CA     1 
ATOM   13388 C C      . ARG B 2 408 ? 39.900  -19.792 -30.949 1.00 18.14  ?  408  ARG B C      1 
ATOM   13389 O O      . ARG B 2 408 ? 40.294  -18.710 -30.484 1.00 19.93  ?  408  ARG B O      1 
ATOM   13390 C CB     . ARG B 2 408 ? 41.056  -21.928 -30.240 1.00 21.58  ?  408  ARG B CB     1 
ATOM   13391 C CG     . ARG B 2 408 ? 41.272  -22.901 -29.072 1.00 22.60  ?  408  ARG B CG     1 
ATOM   13392 C CD     . ARG B 2 408 ? 42.260  -24.005 -29.386 1.00 23.58  ?  408  ARG B CD     1 
ATOM   13393 N NE     . ARG B 2 408 ? 43.603  -23.502 -29.657 1.00 24.07  ?  408  ARG B NE     1 
ATOM   13394 C CZ     . ARG B 2 408 ? 44.610  -24.266 -30.062 1.00 25.02  ?  408  ARG B CZ     1 
ATOM   13395 N NH1    . ARG B 2 408 ? 44.408  -25.566 -30.242 1.00 26.36  ?  408  ARG B NH1    1 
ATOM   13396 N NH2    . ARG B 2 408 ? 45.808  -23.743 -30.275 1.00 25.33  ?  408  ARG B NH2    1 
ATOM   13397 H H      . ARG B 2 408 ? 38.757  -22.580 -30.676 1.00 24.64  ?  408  ARG B H      1 
ATOM   13398 H HA     . ARG B 2 408 ? 39.812  -20.726 -29.145 1.00 24.79  ?  408  ARG B HA     1 
ATOM   13399 H HB2    . ARG B 2 408 ? 40.950  -22.453 -31.049 1.00 25.89  ?  408  ARG B HB2    1 
ATOM   13400 H HB3    . ARG B 2 408 ? 41.844  -21.366 -30.309 1.00 25.89  ?  408  ARG B HB3    1 
ATOM   13401 H HG2    . ARG B 2 408 ? 41.611  -22.407 -28.310 1.00 27.12  ?  408  ARG B HG2    1 
ATOM   13402 H HG3    . ARG B 2 408 ? 40.424  -23.316 -28.848 1.00 27.12  ?  408  ARG B HG3    1 
ATOM   13403 H HD2    . ARG B 2 408 ? 42.313  -24.607 -28.628 1.00 28.29  ?  408  ARG B HD2    1 
ATOM   13404 H HD3    . ARG B 2 408 ? 41.957  -24.487 -30.172 1.00 28.29  ?  408  ARG B HD3    1 
ATOM   13405 H HE     . ARG B 2 408 ? 43.751  -22.662 -29.547 1.00 28.88  ?  408  ARG B HE     1 
ATOM   13406 H HH11   . ARG B 2 408 ? 43.631  -25.904 -30.096 1.00 31.63  ?  408  ARG B HH11   1 
ATOM   13407 H HH12   . ARG B 2 408 ? 45.054  -26.069 -30.505 1.00 31.63  ?  408  ARG B HH12   1 
ATOM   13408 H HH21   . ARG B 2 408 ? 45.939  -22.902 -30.150 1.00 30.40  ?  408  ARG B HH21   1 
ATOM   13409 H HH22   . ARG B 2 408 ? 46.456  -24.244 -30.537 1.00 30.40  ?  408  ARG B HH22   1 
ATOM   13410 N N      . VAL B 2 409 ? 39.573  -19.924 -32.234 1.00 19.06  ?  409  VAL B N      1 
ATOM   13411 C CA     . VAL B 2 409 ? 39.579  -18.751 -33.097 1.00 20.01  ?  409  VAL B CA     1 
ATOM   13412 C C      . VAL B 2 409 ? 38.551  -17.730 -32.622 1.00 19.50  ?  409  VAL B C      1 
ATOM   13413 O O      . VAL B 2 409 ? 38.816  -16.525 -32.616 1.00 18.33  ?  409  VAL B O      1 
ATOM   13414 C CB     . VAL B 2 409 ? 39.351  -19.154 -34.563 1.00 21.14  ?  409  VAL B CB     1 
ATOM   13415 C CG1    . VAL B 2 409 ? 39.227  -17.906 -35.402 1.00 20.66  ?  409  VAL B CG1    1 
ATOM   13416 C CG2    . VAL B 2 409 ? 40.496  -20.025 -35.049 1.00 21.80  ?  409  VAL B CG2    1 
ATOM   13417 H H      . VAL B 2 409 ? 39.350  -20.660 -32.620 1.00 22.87  ?  409  VAL B H      1 
ATOM   13418 H HA     . VAL B 2 409 ? 40.454  -18.337 -33.040 1.00 24.01  ?  409  VAL B HA     1 
ATOM   13419 H HB     . VAL B 2 409 ? 38.534  -19.669 -34.647 1.00 25.36  ?  409  VAL B HB     1 
ATOM   13420 H HG11   . VAL B 2 409 ? 39.289  -18.147 -36.339 1.00 24.79  ?  409  VAL B HG11   1 
ATOM   13421 H HG12   . VAL B 2 409 ? 38.369  -17.490 -35.224 1.00 24.79  ?  409  VAL B HG12   1 
ATOM   13422 H HG13   . VAL B 2 409 ? 39.945  -17.296 -35.169 1.00 24.79  ?  409  VAL B HG13   1 
ATOM   13423 H HG21   . VAL B 2 409 ? 40.338  -20.267 -35.975 1.00 26.16  ?  409  VAL B HG21   1 
ATOM   13424 H HG22   . VAL B 2 409 ? 41.325  -19.527 -34.975 1.00 26.16  ?  409  VAL B HG22   1 
ATOM   13425 H HG23   . VAL B 2 409 ? 40.540  -20.824 -34.501 1.00 26.16  ?  409  VAL B HG23   1 
ATOM   13426 N N      . SER B 2 410 ? 37.350  -18.189 -32.243 1.00 19.45  ?  410  SER B N      1 
ATOM   13427 C CA     . SER B 2 410 ? 36.334  -17.268 -31.739 1.00 18.44  ?  410  SER B CA     1 
ATOM   13428 C C      . SER B 2 410 ? 36.814  -16.551 -30.484 1.00 16.78  ?  410  SER B C      1 
ATOM   13429 O O      . SER B 2 410 ? 36.578  -15.346 -30.314 1.00 17.43  ?  410  SER B O      1 
ATOM   13430 C CB     . SER B 2 410 ? 35.039  -18.040 -31.477 1.00 17.17  ?  410  SER B CB     1 
ATOM   13431 O OG     . SER B 2 410 ? 34.065  -17.222 -30.852 1.00 18.08  ?  410  SER B OG     1 
ATOM   13432 H H      . SER B 2 410 ? 37.104  -19.013 -32.267 1.00 23.34  ?  410  SER B H      1 
ATOM   13433 H HA     . SER B 2 410 ? 36.151  -16.589 -32.407 1.00 22.12  ?  410  SER B HA     1 
ATOM   13434 H HB2    . SER B 2 410 ? 34.686  -18.356 -32.323 1.00 20.60  ?  410  SER B HB2    1 
ATOM   13435 H HB3    . SER B 2 410 ? 35.235  -18.792 -30.897 1.00 20.60  ?  410  SER B HB3    1 
ATOM   13436 H HG     . SER B 2 410 ? 33.881  -16.567 -31.344 1.00 21.70  ?  410  SER B HG     1 
ATOM   13437 N N      . ALA B 2 411 ? 37.498  -17.267 -29.591 1.00 18.31  ?  411  ALA B N      1 
ATOM   13438 C CA     . ALA B 2 411 ? 38.025  -16.617 -28.391 1.00 18.33  ?  411  ALA B CA     1 
ATOM   13439 C C      . ALA B 2 411 ? 39.114  -15.615 -28.741 1.00 17.28  ?  411  ALA B C      1 
ATOM   13440 O O      . ALA B 2 411 ? 39.185  -14.530 -28.141 1.00 18.67  ?  411  ALA B O      1 
ATOM   13441 C CB     . ALA B 2 411 ? 38.552  -17.662 -27.423 1.00 19.80  ?  411  ALA B CB     1 
ATOM   13442 H H      . ALA B 2 411 ? 37.668  -18.108 -29.651 1.00 21.97  ?  411  ALA B H      1 
ATOM   13443 H HA     . ALA B 2 411 ? 37.304  -16.138 -27.953 1.00 21.99  ?  411  ALA B HA     1 
ATOM   13444 H HB1    . ALA B 2 411 ? 38.909  -17.215 -26.639 1.00 23.76  ?  411  ALA B HB1    1 
ATOM   13445 H HB2    . ALA B 2 411 ? 37.825  -18.250 -27.166 1.00 23.76  ?  411  ALA B HB2    1 
ATOM   13446 H HB3    . ALA B 2 411 ? 39.252  -18.173 -27.860 1.00 23.76  ?  411  ALA B HB3    1 
ATOM   13447 N N      . ALA B 2 412 ? 39.980  -15.959 -29.702 1.00 18.83  ?  412  ALA B N      1 
ATOM   13448 C CA     . ALA B 2 412 ? 41.000  -15.011 -30.144 1.00 18.60  ?  412  ALA B CA     1 
ATOM   13449 C C      . ALA B 2 412 ? 40.364  -13.765 -30.743 1.00 20.19  ?  412  ALA B C      1 
ATOM   13450 O O      . ALA B 2 412 ? 40.864  -12.656 -30.556 1.00 19.63  ?  412  ALA B O      1 
ATOM   13451 C CB     . ALA B 2 412 ? 41.923  -15.680 -31.157 1.00 18.63  ?  412  ALA B CB     1 
ATOM   13452 H H      . ALA B 2 412 ? 39.998  -16.719 -30.105 1.00 22.60  ?  412  ALA B H      1 
ATOM   13453 H HA     . ALA B 2 412 ? 41.534  -14.739 -29.381 1.00 22.32  ?  412  ALA B HA     1 
ATOM   13454 H HB1    . ALA B 2 412 ? 42.609  -15.048 -31.425 1.00 22.36  ?  412  ALA B HB1    1 
ATOM   13455 H HB2    . ALA B 2 412 ? 42.332  -16.458 -30.746 1.00 22.36  ?  412  ALA B HB2    1 
ATOM   13456 H HB3    . ALA B 2 412 ? 41.402  -15.950 -31.930 1.00 22.36  ?  412  ALA B HB3    1 
ATOM   13457 N N      . ALA B 2 413 ? 39.249  -13.927 -31.461 1.00 19.26  ?  413  ALA B N      1 
ATOM   13458 C CA     . ALA B 2 413 ? 38.541  -12.769 -31.988 1.00 18.04  ?  413  ALA B CA     1 
ATOM   13459 C C      . ALA B 2 413 ? 37.986  -11.908 -30.864 1.00 17.51  ?  413  ALA B C      1 
ATOM   13460 O O      . ALA B 2 413 ? 38.043  -10.677 -30.934 1.00 18.05  ?  413  ALA B O      1 
ATOM   13461 C CB     . ALA B 2 413 ? 37.419  -13.236 -32.918 1.00 16.28  ?  413  ALA B CB     1 
ATOM   13462 H H      . ALA B 2 413 ? 38.888  -14.684 -31.651 1.00 23.11  ?  413  ALA B H      1 
ATOM   13463 H HA     . ALA B 2 413 ? 39.157  -12.224 -32.504 1.00 21.64  ?  413  ALA B HA     1 
ATOM   13464 H HB1    . ALA B 2 413 ? 36.981  -12.459 -33.299 1.00 19.53  ?  413  ALA B HB1    1 
ATOM   13465 H HB2    . ALA B 2 413 ? 37.801  -13.780 -33.625 1.00 19.53  ?  413  ALA B HB2    1 
ATOM   13466 H HB3    . ALA B 2 413 ? 36.782  -13.758 -32.406 1.00 19.53  ?  413  ALA B HB3    1 
ATOM   13467 N N      . MET B 2 414 ? 37.475  -12.538 -29.808 1.00 18.64  ?  414  MET B N      1 
ATOM   13468 C CA     . MET B 2 414 ? 36.988  -11.785 -28.663 1.00 18.64  ?  414  MET B CA     1 
ATOM   13469 C C      . MET B 2 414 ? 38.098  -10.927 -28.078 1.00 19.17  ?  414  MET B C      1 
ATOM   13470 O O      . MET B 2 414 ? 37.856  -9.805  -27.620 1.00 20.87  ?  414  MET B O      1 
ATOM   13471 C CB     . MET B 2 414 ? 36.454  -12.758 -27.618 1.00 22.55  ?  414  MET B CB     1 
ATOM   13472 C CG     . MET B 2 414 ? 35.426  -12.158 -26.696 1.00 23.83  ?  414  MET B CG     1 
ATOM   13473 S SD     . MET B 2 414 ? 33.894  -11.674 -27.531 1.00 24.04  ?  414  MET B SD     1 
ATOM   13474 C CE     . MET B 2 414 ? 32.912  -11.297 -26.090 1.00 25.66  ?  414  MET B CE     1 
ATOM   13475 H H      . MET B 2 414 ? 37.399  -13.391 -29.730 1.00 22.37  ?  414  MET B H      1 
ATOM   13476 H HA     . MET B 2 414 ? 36.259  -11.206 -28.938 1.00 22.37  ?  414  MET B HA     1 
ATOM   13477 H HB2    . MET B 2 414 ? 36.041  -13.508 -28.074 1.00 27.06  ?  414  MET B HB2    1 
ATOM   13478 H HB3    . MET B 2 414 ? 37.195  -13.067 -27.074 1.00 27.06  ?  414  MET B HB3    1 
ATOM   13479 H HG2    . MET B 2 414 ? 35.199  -12.810 -26.015 1.00 28.59  ?  414  MET B HG2    1 
ATOM   13480 H HG3    . MET B 2 414 ? 35.802  -11.364 -26.283 1.00 28.59  ?  414  MET B HG3    1 
ATOM   13481 H HE1    . MET B 2 414 ? 32.072  -10.905 -26.375 1.00 30.79  ?  414  MET B HE1    1 
ATOM   13482 H HE2    . MET B 2 414 ? 32.745  -12.117 -25.599 1.00 30.79  ?  414  MET B HE2    1 
ATOM   13483 H HE3    . MET B 2 414 ? 33.398  -10.670 -25.532 1.00 30.79  ?  414  MET B HE3    1 
ATOM   13484 N N      . SER B 2 415 ? 39.335  -11.451 -28.071 1.00 20.76  ?  415  SER B N      1 
ATOM   13485 C CA     . SER B 2 415 ? 40.482  -10.697 -27.590 1.00 23.75  ?  415  SER B CA     1 
ATOM   13486 C C      . SER B 2 415 ? 40.777  -9.479  -28.447 1.00 21.61  ?  415  SER B C      1 
ATOM   13487 O O      . SER B 2 415 ? 41.401  -8.539  -27.958 1.00 24.28  ?  415  SER B O      1 
ATOM   13488 C CB     . SER B 2 415 ? 41.725  -11.589 -27.594 1.00 29.10  ?  415  SER B CB     1 
ATOM   13489 O OG     . SER B 2 415 ? 41.630  -12.571 -26.590 1.00 35.68  ?  415  SER B OG     1 
ATOM   13490 H H      . SER B 2 415 ? 39.530  -12.243 -28.341 1.00 24.90  ?  415  SER B H      1 
ATOM   13491 H HA     . SER B 2 415 ? 40.291  -10.407 -26.684 1.00 28.49  ?  415  SER B HA     1 
ATOM   13492 H HB2    . SER B 2 415 ? 41.800  -12.025 -28.458 1.00 34.92  ?  415  SER B HB2    1 
ATOM   13493 H HB3    . SER B 2 415 ? 42.509  -11.042 -27.430 1.00 34.92  ?  415  SER B HB3    1 
ATOM   13494 H HG     . SER B 2 415 ? 41.006  -13.105 -26.768 1.00 42.81  ?  415  SER B HG     1 
ATOM   13495 N N      . GLU B 2 416 ? 40.372  -9.495  -29.715 1.00 20.76  ?  416  GLU B N      1 
ATOM   13496 C CA     . GLU B 2 416 ? 40.423  -8.330  -30.585 1.00 21.13  ?  416  GLU B CA     1 
ATOM   13497 C C      . GLU B 2 416 ? 39.156  -7.487  -30.487 1.00 18.76  ?  416  GLU B C      1 
ATOM   13498 O O      . GLU B 2 416 ? 38.959  -6.587  -31.314 1.00 19.25  ?  416  GLU B O      1 
ATOM   13499 C CB     . GLU B 2 416 ? 40.619  -8.773  -32.045 1.00 23.24  ?  416  GLU B CB     1 
ATOM   13500 C CG     . GLU B 2 416 ? 41.801  -9.681  -32.282 1.00 25.32  ?  416  GLU B CG     1 
ATOM   13501 C CD     . GLU B 2 416 ? 43.120  -8.969  -32.094 1.00 27.78  ?  416  GLU B CD     1 
ATOM   13502 O OE1    . GLU B 2 416 ? 43.178  -7.726  -32.291 1.00 28.72  ?  416  GLU B OE1    1 
ATOM   13503 O OE2    . GLU B 2 416 ? 44.108  -9.640  -31.747 1.00 29.98  -1 416  GLU B OE2    1 
ATOM   13504 H H      . GLU B 2 416 ? 40.054  -10.194 -30.103 1.00 24.91  ?  416  GLU B H      1 
ATOM   13505 H HA     . GLU B 2 416 ? 41.182  -7.783  -30.328 1.00 25.35  ?  416  GLU B HA     1 
ATOM   13506 H HB2    . GLU B 2 416 ? 39.824  -9.249  -32.330 1.00 27.88  ?  416  GLU B HB2    1 
ATOM   13507 H HB3    . GLU B 2 416 ? 40.746  -7.981  -32.591 1.00 27.88  ?  416  GLU B HB3    1 
ATOM   13508 H HG2    . GLU B 2 416 ? 41.765  -10.419 -31.655 1.00 30.38  ?  416  GLU B HG2    1 
ATOM   13509 H HG3    . GLU B 2 416 ? 41.767  -10.016 -33.192 1.00 30.38  ?  416  GLU B HG3    1 
ATOM   13510 N N      . ASN B 2 417 ? 38.296  -7.775  -29.511 1.00 17.78  ?  417  ASN B N      1 
ATOM   13511 C CA     . ASN B 2 417 ? 37.017  -7.082  -29.325 1.00 17.76  ?  417  ASN B CA     1 
ATOM   13512 C C      . ASN B 2 417 ? 36.093  -7.272  -30.526 1.00 16.31  ?  417  ASN B C      1 
ATOM   13513 O O      . ASN B 2 417 ? 35.343  -6.372  -30.900 1.00 17.42  ?  417  ASN B O      1 
ATOM   13514 C CB     . ASN B 2 417 ? 37.208  -5.612  -28.948 1.00 21.12  ?  417  ASN B CB     1 
ATOM   13515 C CG     . ASN B 2 417 ? 37.817  -5.454  -27.567 1.00 23.68  ?  417  ASN B CG     1 
ATOM   13516 O OD1    . ASN B 2 417 ? 37.760  -6.348  -26.727 1.00 24.52  ?  417  ASN B OD1    1 
ATOM   13517 N ND2    . ASN B 2 417 ? 38.418  -4.316  -27.336 1.00 27.74  ?  417  ASN B ND2    1 
ATOM   13518 H H      . ASN B 2 417 ? 38.433  -8.388  -28.924 1.00 21.33  ?  417  ASN B H      1 
ATOM   13519 H HA     . ASN B 2 417 ? 36.562  -7.491  -28.573 1.00 21.31  ?  417  ASN B HA     1 
ATOM   13520 H HB2    . ASN B 2 417 ? 37.800  -5.191  -29.591 1.00 25.34  ?  417  ASN B HB2    1 
ATOM   13521 H HB3    . ASN B 2 417 ? 36.345  -5.167  -28.951 1.00 25.34  ?  417  ASN B HB3    1 
ATOM   13522 H HD21   . ASN B 2 417 ? 38.782  -4.170  -26.571 1.00 33.29  ?  417  ASN B HD21   1 
ATOM   13523 H HD22   . ASN B 2 417 ? 38.448  -3.714  -27.949 1.00 33.29  ?  417  ASN B HD22   1 
ATOM   13524 N N      . LEU B 2 418 ? 36.130  -8.469  -31.100 1.00 15.64  ?  418  LEU B N      1 
ATOM   13525 C CA     . LEU B 2 418 ? 35.211  -8.886  -32.154 1.00 16.28  ?  418  LEU B CA     1 
ATOM   13526 C C      . LEU B 2 418 ? 34.430  -10.110 -31.696 1.00 16.24  ?  418  LEU B C      1 
ATOM   13527 O O      . LEU B 2 418 ? 35.027  -11.113 -31.300 1.00 16.84  ?  418  LEU B O      1 
ATOM   13528 C CB     . LEU B 2 418 ? 35.978  -9.231  -33.431 1.00 17.34  ?  418  LEU B CB     1 
ATOM   13529 C CG     . LEU B 2 418 ? 35.147  -9.866  -34.544 1.00 16.87  ?  418  LEU B CG     1 
ATOM   13530 C CD1    . LEU B 2 418 ? 34.084  -8.923  -35.083 1.00 17.76  ?  418  LEU B CD1    1 
ATOM   13531 C CD2    . LEU B 2 418 ? 36.013  -10.332 -35.684 1.00 17.90  ?  418  LEU B CD2    1 
ATOM   13532 H H      . LEU B 2 418 ? 36.699  -9.077  -30.887 1.00 18.77  ?  418  LEU B H      1 
ATOM   13533 H HA     . LEU B 2 418 ? 34.586  -8.166  -32.336 1.00 19.53  ?  418  LEU B HA     1 
ATOM   13534 H HB2    . LEU B 2 418 ? 36.362  -8.414  -33.787 1.00 20.81  ?  418  LEU B HB2    1 
ATOM   13535 H HB3    . LEU B 2 418 ? 36.683  -9.857  -33.203 1.00 20.81  ?  418  LEU B HB3    1 
ATOM   13536 H HG     . LEU B 2 418 ? 34.700  -10.631 -34.150 1.00 20.24  ?  418  LEU B HG     1 
ATOM   13537 H HD11   . LEU B 2 418 ? 33.580  -9.379  -35.776 1.00 21.31  ?  418  LEU B HD11   1 
ATOM   13538 H HD12   . LEU B 2 418 ? 33.493  -8.667  -34.359 1.00 21.31  ?  418  LEU B HD12   1 
ATOM   13539 H HD13   . LEU B 2 418 ? 34.516  -8.137  -35.452 1.00 21.31  ?  418  LEU B HD13   1 
ATOM   13540 H HD21   . LEU B 2 418 ? 35.448  -10.701 -36.380 1.00 21.48  ?  418  LEU B HD21   1 
ATOM   13541 H HD22   . LEU B 2 418 ? 36.513  -9.576  -36.030 1.00 21.48  ?  418  LEU B HD22   1 
ATOM   13542 H HD23   . LEU B 2 418 ? 36.624  -11.011 -35.358 1.00 21.48  ?  418  LEU B HD23   1 
ATOM   13543 N N      . ILE B 2 419 ? 33.104  -10.033 -31.764 1.00 16.42  ?  419  ILE B N      1 
ATOM   13544 C CA     . ILE B 2 419 ? 32.245  -11.188 -31.532 1.00 14.92  ?  419  ILE B CA     1 
ATOM   13545 C C      . ILE B 2 419 ? 31.975  -11.847 -32.883 1.00 16.24  ?  419  ILE B C      1 
ATOM   13546 O O      . ILE B 2 419 ? 31.381  -11.233 -33.780 1.00 17.03  ?  419  ILE B O      1 
ATOM   13547 C CB     . ILE B 2 419 ? 30.929  -10.787 -30.850 1.00 16.15  ?  419  ILE B CB     1 
ATOM   13548 C CG1    . ILE B 2 419 ? 31.191  -10.129 -29.507 1.00 18.24  ?  419  ILE B CG1    1 
ATOM   13549 C CG2    . ILE B 2 419 ? 30.042  -12.015 -30.674 1.00 18.32  ?  419  ILE B CG2    1 
ATOM   13550 C CD1    . ILE B 2 419 ? 30.019  -9.362  -28.985 1.00 18.09  ?  419  ILE B CD1    1 
ATOM   13551 H H      . ILE B 2 419 ? 32.674  -9.311  -31.946 1.00 19.70  ?  419  ILE B H      1 
ATOM   13552 H HA     . ILE B 2 419 ? 32.704  -11.819 -30.955 1.00 17.90  ?  419  ILE B HA     1 
ATOM   13553 H HB     . ILE B 2 419 ? 30.476  -10.143 -31.416 1.00 19.37  ?  419  ILE B HB     1 
ATOM   13554 H HG12   . ILE B 2 419 ? 31.411  -10.815 -28.858 1.00 21.88  ?  419  ILE B HG12   1 
ATOM   13555 H HG13   . ILE B 2 419 ? 31.933  -9.511  -29.600 1.00 21.88  ?  419  ILE B HG13   1 
ATOM   13556 H HG21   . ILE B 2 419 ? 29.297  -11.787 -30.097 1.00 21.98  ?  419  ILE B HG21   1 
ATOM   13557 H HG22   . ILE B 2 419 ? 29.714  -12.294 -31.543 1.00 21.98  ?  419  ILE B HG22   1 
ATOM   13558 H HG23   . ILE B 2 419 ? 30.565  -12.728 -30.274 1.00 21.98  ?  419  ILE B HG23   1 
ATOM   13559 H HD11   . ILE B 2 419 ? 30.287  -8.879  -28.188 1.00 21.70  ?  419  ILE B HD11   1 
ATOM   13560 H HD12   . ILE B 2 419 ? 29.721  -8.739  -29.666 1.00 21.70  ?  419  ILE B HD12   1 
ATOM   13561 H HD13   . ILE B 2 419 ? 29.306  -9.984  -28.771 1.00 21.70  ?  419  ILE B HD13   1 
ATOM   13562 N N      . ALA B 2 420 ? 32.441  -13.086 -33.039 1.00 17.10  ?  420  ALA B N      1 
ATOM   13563 C CA     . ALA B 2 420 ? 32.173  -13.921 -34.203 1.00 18.28  ?  420  ALA B CA     1 
ATOM   13564 C C      . ALA B 2 420 ? 32.054  -15.326 -33.636 1.00 17.96  ?  420  ALA B C      1 
ATOM   13565 O O      . ALA B 2 420 ? 32.888  -15.736 -32.823 1.00 18.90  ?  420  ALA B O      1 
ATOM   13566 C CB     . ALA B 2 420 ? 33.305  -13.843 -35.222 1.00 18.17  ?  420  ALA B CB     1 
ATOM   13567 H H      . ALA B 2 420 ? 32.936  -13.480 -32.456 1.00 20.52  ?  420  ALA B H      1 
ATOM   13568 H HA     . ALA B 2 420 ? 31.366  -13.659 -34.673 1.00 21.94  ?  420  ALA B HA     1 
ATOM   13569 H HB1    . ALA B 2 420 ? 33.061  -14.360 -36.006 1.00 21.80  ?  420  ALA B HB1    1 
ATOM   13570 H HB2    . ALA B 2 420 ? 33.446  -12.915 -35.468 1.00 21.80  ?  420  ALA B HB2    1 
ATOM   13571 H HB3    . ALA B 2 420 ? 34.113  -14.205 -34.825 1.00 21.80  ?  420  ALA B HB3    1 
ATOM   13572 N N      A ARG B 2 421 ? 31.038  -16.060 -34.064 0.48 19.18  ?  421  ARG B N      1 
ATOM   13573 N N      B ARG B 2 421 ? 31.021  -16.054 -34.044 0.52 18.91  ?  421  ARG B N      1 
ATOM   13574 C CA     A ARG B 2 421 ? 30.628  -17.269 -33.375 0.48 19.39  ?  421  ARG B CA     1 
ATOM   13575 C CA     B ARG B 2 421 ? 30.614  -17.274 -33.364 0.52 18.86  ?  421  ARG B CA     1 
ATOM   13576 C C      A ARG B 2 421 ? 31.394  -18.493 -33.854 0.48 17.90  ?  421  ARG B C      1 
ATOM   13577 C C      B ARG B 2 421 ? 31.384  -18.495 -33.850 0.52 17.67  ?  421  ARG B C      1 
ATOM   13578 O O      A ARG B 2 421 ? 31.600  -18.687 -35.053 0.48 18.27  ?  421  ARG B O      1 
ATOM   13579 O O      B ARG B 2 421 ? 31.585  -18.684 -35.050 0.52 18.11  ?  421  ARG B O      1 
ATOM   13580 C CB     A ARG B 2 421 ? 29.135  -17.480 -33.623 0.48 22.69  ?  421  ARG B CB     1 
ATOM   13581 C CB     B ARG B 2 421 ? 29.113  -17.495 -33.594 0.52 21.54  ?  421  ARG B CB     1 
ATOM   13582 C CG     A ARG B 2 421 ? 28.537  -18.602 -32.847 0.48 28.09  ?  421  ARG B CG     1 
ATOM   13583 C CG     B ARG B 2 421 ? 28.479  -18.517 -32.684 0.52 26.85  ?  421  ARG B CG     1 
ATOM   13584 C CD     A ARG B 2 421 ? 27.260  -19.070 -33.509 0.48 31.77  ?  421  ARG B CD     1 
ATOM   13585 C CD     B ARG B 2 421 ? 27.127  -18.022 -32.126 0.52 29.39  ?  421  ARG B CD     1 
ATOM   13586 N NE     A ARG B 2 421 ? 26.628  -20.103 -32.711 0.48 34.33  ?  421  ARG B NE     1 
ATOM   13587 N NE     B ARG B 2 421 ? 26.815  -18.712 -30.876 0.52 32.87  ?  421  ARG B NE     1 
ATOM   13588 C CZ     A ARG B 2 421 ? 25.404  -20.567 -32.914 0.48 36.95  ?  421  ARG B CZ     1 
ATOM   13589 C CZ     B ARG B 2 421 ? 26.960  -18.185 -29.666 0.52 36.28  ?  421  ARG B CZ     1 
ATOM   13590 N NH1    A ARG B 2 421 ? 24.661  -20.096 -33.914 0.48 35.17  ?  421  ARG B NH1    1 
ATOM   13591 N NH1    B ARG B 2 421 ? 27.376  -16.935 -29.524 0.52 37.33  ?  421  ARG B NH1    1 
ATOM   13592 N NH2    A ARG B 2 421 ? 24.931  -21.508 -32.114 0.48 37.75  ?  421  ARG B NH2    1 
ATOM   13593 N NH2    B ARG B 2 421 ? 26.671  -18.905 -28.594 0.52 37.10  ?  421  ARG B NH2    1 
ATOM   13594 H H      A ARG B 2 421 ? 30.568  -15.875 -34.760 0.48 23.01  ?  421  ARG B H      1 
ATOM   13595 H H      B ARG B 2 421 ? 30.534  -15.858 -34.725 0.52 22.69  ?  421  ARG B H      1 
ATOM   13596 H HA     A ARG B 2 421 ? 30.813  -17.177 -32.427 0.48 23.26  ?  421  ARG B HA     1 
ATOM   13597 H HA     B ARG B 2 421 ? 30.803  -17.182 -32.417 0.52 22.63  ?  421  ARG B HA     1 
ATOM   13598 H HB2    A ARG B 2 421 ? 28.662  -16.669 -33.379 0.48 27.22  ?  421  ARG B HB2    1 
ATOM   13599 H HB2    B ARG B 2 421 ? 28.652  -16.653 -33.453 0.52 25.85  ?  421  ARG B HB2    1 
ATOM   13600 H HB3    A ARG B 2 421 ? 29.001  -17.670 -34.565 0.48 27.22  ?  421  ARG B HB3    1 
ATOM   13601 H HB3    B ARG B 2 421 ? 28.983  -17.796 -34.506 0.52 25.85  ?  421  ARG B HB3    1 
ATOM   13602 H HG2    A ARG B 2 421 ? 29.160  -19.345 -32.814 0.48 33.70  ?  421  ARG B HG2    1 
ATOM   13603 H HG2    B ARG B 2 421 ? 28.322  -19.335 -33.181 0.52 32.22  ?  421  ARG B HG2    1 
ATOM   13604 H HG3    A ARG B 2 421 ? 28.329  -18.303 -31.948 0.48 33.70  ?  421  ARG B HG3    1 
ATOM   13605 H HG3    B ARG B 2 421 ? 29.071  -18.692 -31.936 0.52 32.22  ?  421  ARG B HG3    1 
ATOM   13606 H HD2    A ARG B 2 421 ? 26.645  -18.324 -33.594 0.48 38.12  ?  421  ARG B HD2    1 
ATOM   13607 H HD2    B ARG B 2 421 ? 27.176  -17.069 -31.951 0.52 35.26  ?  421  ARG B HD2    1 
ATOM   13608 H HD3    A ARG B 2 421 ? 27.462  -19.434 -34.385 0.48 38.12  ?  421  ARG B HD3    1 
ATOM   13609 H HD3    B ARG B 2 421 ? 26.423  -18.206 -32.767 0.52 35.26  ?  421  ARG B HD3    1 
ATOM   13610 H HE     A ARG B 2 421 ? 27.080  -20.439 -32.061 0.48 41.20  ?  421  ARG B HE     1 
ATOM   13611 H HE     B ARG B 2 421 ? 26.517  -19.517 -30.928 0.52 39.44  ?  421  ARG B HE     1 
ATOM   13612 H HH11   A ARG B 2 421 ? 24.976  -19.487 -34.433 0.48 42.20  ?  421  ARG B HH11   1 
ATOM   13613 H HH11   B ARG B 2 421 ? 27.554  -16.460 -30.218 0.52 44.80  ?  421  ARG B HH11   1 
ATOM   13614 H HH12   A ARG B 2 421 ? 23.867  -20.401 -34.041 0.48 42.20  ?  421  ARG B HH12   1 
ATOM   13615 H HH12   B ARG B 2 421 ? 27.468  -16.600 -28.737 0.52 44.80  ?  421  ARG B HH12   1 
ATOM   13616 H HH21   A ARG B 2 421 ? 25.417  -21.811 -31.473 0.48 45.30  ?  421  ARG B HH21   1 
ATOM   13617 H HH21   B ARG B 2 421 ? 26.390  -19.713 -28.682 0.52 44.51  ?  421  ARG B HH21   1 
ATOM   13618 H HH22   A ARG B 2 421 ? 24.138  -21.817 -32.235 0.48 45.30  ?  421  ARG B HH22   1 
ATOM   13619 H HH22   B ARG B 2 421 ? 26.765  -18.565 -27.810 0.52 44.51  ?  421  ARG B HH22   1 
ATOM   13620 N N      . ALA B 2 422 ? 31.801  -19.330 -32.901 1.00 17.03  ?  422  ALA B N      1 
ATOM   13621 C CA     . ALA B 2 422 ? 32.277  -20.668 -33.219 1.00 17.26  ?  422  ALA B CA     1 
ATOM   13622 C C      . ALA B 2 422 ? 31.030  -21.513 -33.439 1.00 17.24  ?  422  ALA B C      1 
ATOM   13623 O O      . ALA B 2 422 ? 30.247  -21.722 -32.509 1.00 19.45  ?  422  ALA B O      1 
ATOM   13624 C CB     . ALA B 2 422 ? 33.086  -21.237 -32.074 1.00 18.93  ?  422  ALA B CB     1 
ATOM   13625 H H      . ALA B 2 422 ? 31.817  -19.142 -32.061 1.00 20.43  ?  422  ALA B H      1 
ATOM   13626 H HA     . ALA B 2 422 ? 32.845  -20.660 -34.006 1.00 20.71  ?  422  ALA B HA     1 
ATOM   13627 H HB1    . ALA B 2 422 ? 33.389  -22.127 -32.311 1.00 22.72  ?  422  ALA B HB1    1 
ATOM   13628 H HB2    . ALA B 2 422 ? 33.850  -20.661 -31.910 1.00 22.72  ?  422  ALA B HB2    1 
ATOM   13629 H HB3    . ALA B 2 422 ? 32.527  -21.278 -31.282 1.00 22.72  ?  422  ALA B HB3    1 
ATOM   13630 N N      A MET B 2 423 ? 30.827  -21.985 -34.657 0.87 16.95  ?  423  MET B N      1 
ATOM   13631 N N      B MET B 2 423 ? 30.850  -22.010 -34.649 0.13 18.55  ?  423  MET B N      1 
ATOM   13632 C CA     A MET B 2 423 ? 29.607  -22.709 -34.970 0.87 18.12  ?  423  MET B CA     1 
ATOM   13633 C CA     B MET B 2 423 ? 29.619  -22.712 -34.969 0.13 19.67  ?  423  MET B CA     1 
ATOM   13634 C C      A MET B 2 423 ? 29.696  -24.145 -34.471 0.87 19.60  ?  423  MET B C      1 
ATOM   13635 C C      B MET B 2 423 ? 29.695  -24.168 -34.519 0.13 20.16  ?  423  MET B C      1 
ATOM   13636 O O      A MET B 2 423 ? 30.794  -24.688 -34.323 0.87 19.72  ?  423  MET B O      1 
ATOM   13637 O O      B MET B 2 423 ? 30.780  -24.752 -34.459 0.13 20.64  ?  423  MET B O      1 
ATOM   13638 C CB     A MET B 2 423 ? 29.381  -22.712 -36.482 0.87 17.81  ?  423  MET B CB     1 
ATOM   13639 C CB     B MET B 2 423 ? 29.365  -22.648 -36.470 0.13 20.19  ?  423  MET B CB     1 
ATOM   13640 C CG     A MET B 2 423 ? 29.573  -21.336 -37.143 0.87 18.85  ?  423  MET B CG     1 
ATOM   13641 C CG     B MET B 2 423 ? 29.556  -21.248 -37.036 0.13 20.50  ?  423  MET B CG     1 
ATOM   13642 S SD     A MET B 2 423 ? 28.303  -20.153 -36.670 0.87 18.96  ?  423  MET B SD     1 
ATOM   13643 S SD     B MET B 2 423 ? 28.399  -20.828 -38.348 0.13 20.38  ?  423  MET B SD     1 
ATOM   13644 C CE     A MET B 2 423 ? 26.876  -20.934 -37.417 0.87 20.47  ?  423  MET B CE     1 
ATOM   13645 C CE     B MET B 2 423 ? 26.834  -21.055 -37.501 0.13 20.99  ?  423  MET B CE     1 
ATOM   13646 H H      A MET B 2 423 ? 31.374  -21.902 -35.315 0.87 20.34  ?  423  MET B H      1 
ATOM   13647 H H      B MET B 2 423 ? 31.415  -21.957 -35.295 0.13 22.26  ?  423  MET B H      1 
ATOM   13648 H HA     A MET B 2 423 ? 28.853  -22.271 -34.545 0.87 21.74  ?  423  MET B HA     1 
ATOM   13649 H HA     B MET B 2 423 ? 28.874  -22.287 -34.515 0.13 23.60  ?  423  MET B HA     1 
ATOM   13650 H HB2    A MET B 2 423 ? 30.011  -23.327 -36.890 0.87 21.37  ?  423  MET B HB2    1 
ATOM   13651 H HB2    B MET B 2 423 ? 29.984  -23.242 -36.922 0.13 24.23  ?  423  MET B HB2    1 
ATOM   13652 H HB3    A MET B 2 423 ? 28.472  -23.001 -36.660 0.87 21.37  ?  423  MET B HB3    1 
ATOM   13653 H HB3    B MET B 2 423 ? 28.452  -22.923 -36.649 0.13 24.23  ?  423  MET B HB3    1 
ATOM   13654 H HG2    A MET B 2 423 ? 30.433  -20.975 -36.877 0.87 22.61  ?  423  MET B HG2    1 
ATOM   13655 H HG2    B MET B 2 423 ? 29.437  -20.604 -36.321 0.13 24.60  ?  423  MET B HG2    1 
ATOM   13656 H HG3    A MET B 2 423 ? 29.541  -21.442 -38.107 0.87 22.61  ?  423  MET B HG3    1 
ATOM   13657 H HG3    B MET B 2 423 ? 30.452  -21.178 -37.400 0.13 24.60  ?  423  MET B HG3    1 
ATOM   13658 H HE1    A MET B 2 423 ? 26.342  -20.256 -37.859 0.87 24.56  ?  423  MET B HE1    1 
ATOM   13659 H HE1    B MET B 2 423 ? 26.143  -20.569 -37.978 0.13 25.18  ?  423  MET B HE1    1 
ATOM   13660 H HE2    A MET B 2 423 ? 27.178  -21.591 -38.063 0.87 24.56  ?  423  MET B HE2    1 
ATOM   13661 H HE2    B MET B 2 423 ? 26.619  -22.001 -37.482 0.13 25.18  ?  423  MET B HE2    1 
ATOM   13662 H HE3    A MET B 2 423 ? 26.354  -21.367 -36.723 0.87 24.56  ?  423  MET B HE3    1 
ATOM   13663 H HE3    B MET B 2 423 ? 26.912  -20.715 -36.596 0.13 25.18  ?  423  MET B HE3    1 
ATOM   13664 N N      . PRO B 2 424 ? 28.553  -24.773 -34.200 1.00 20.10  ?  424  PRO B N      1 
ATOM   13665 C CA     . PRO B 2 424 ? 28.572  -26.126 -33.640 1.00 23.43  ?  424  PRO B CA     1 
ATOM   13666 C C      . PRO B 2 424 ? 29.003  -27.166 -34.659 1.00 22.27  ?  424  PRO B C      1 
ATOM   13667 O O      . PRO B 2 424 ? 28.888  -26.982 -35.875 1.00 21.03  ?  424  PRO B O      1 
ATOM   13668 C CB     . PRO B 2 424 ? 27.123  -26.359 -33.195 1.00 23.77  ?  424  PRO B CB     1 
ATOM   13669 C CG     . PRO B 2 424 ? 26.317  -25.437 -34.020 1.00 23.57  ?  424  PRO B CG     1 
ATOM   13670 C CD     . PRO B 2 424 ? 27.187  -24.227 -34.275 1.00 20.43  ?  424  PRO B CD     1 
ATOM   13671 H HA     . PRO B 2 424 ? 29.163  -26.162 -32.871 1.00 28.12  ?  424  PRO B HA     1 
ATOM   13672 H HB2    . PRO B 2 424 ? 26.872  -27.282 -33.359 1.00 28.52  ?  424  PRO B HB2    1 
ATOM   13673 H HB3    . PRO B 2 424 ? 27.030  -26.153 -32.252 1.00 28.52  ?  424  PRO B HB3    1 
ATOM   13674 H HG2    . PRO B 2 424 ? 26.080  -25.870 -34.855 1.00 28.28  ?  424  PRO B HG2    1 
ATOM   13675 H HG3    . PRO B 2 424 ? 25.514  -25.185 -33.537 1.00 28.28  ?  424  PRO B HG3    1 
ATOM   13676 H HD2    . PRO B 2 424 ? 27.012  -23.854 -35.153 1.00 24.51  ?  424  PRO B HD2    1 
ATOM   13677 H HD3    . PRO B 2 424 ? 27.048  -23.551 -33.593 1.00 24.51  ?  424  PRO B HD3    1 
ATOM   13678 N N      . GLN B 2 425 ? 29.520  -28.279 -34.125 1.00 23.77  ?  425  GLN B N      1 
ATOM   13679 C CA     . GLN B 2 425 ? 29.709  -29.501 -34.900 1.00 23.81  ?  425  GLN B CA     1 
ATOM   13680 C C      . GLN B 2 425 ? 30.696  -29.270 -36.041 1.00 24.30  ?  425  GLN B C      1 
ATOM   13681 O O      . GLN B 2 425 ? 30.447  -29.606 -37.193 1.00 25.31  ?  425  GLN B O      1 
ATOM   13682 C CB     . GLN B 2 425 ? 28.367  -30.049 -35.393 1.00 24.18  ?  425  GLN B CB     1 
ATOM   13683 C CG     . GLN B 2 425 ? 28.075  -31.423 -34.918 1.00 22.37  ?  425  GLN B CG     1 
ATOM   13684 C CD     . GLN B 2 425 ? 26.699  -31.912 -35.333 1.00 19.76  ?  425  GLN B CD     1 
ATOM   13685 O OE1    . GLN B 2 425 ? 25.713  -31.612 -34.686 1.00 19.09  ?  425  GLN B OE1    1 
ATOM   13686 N NE2    . GLN B 2 425 ? 26.635  -32.657 -36.428 1.00 24.18  ?  425  GLN B NE2    1 
ATOM   13687 H H      . GLN B 2 425 ? 29.769  -28.346 -33.305 1.00 28.52  ?  425  GLN B H      1 
ATOM   13688 H HA     . GLN B 2 425 ? 30.099  -30.182 -34.330 1.00 28.57  ?  425  GLN B HA     1 
ATOM   13689 H HB2    . GLN B 2 425 ? 27.658  -29.469 -35.076 1.00 29.02  ?  425  GLN B HB2    1 
ATOM   13690 H HB3    . GLN B 2 425 ? 28.374  -30.066 -36.363 1.00 29.02  ?  425  GLN B HB3    1 
ATOM   13691 H HG2    . GLN B 2 425 ? 28.733  -32.032 -35.289 1.00 26.84  ?  425  GLN B HG2    1 
ATOM   13692 H HG3    . GLN B 2 425 ? 28.118  -31.438 -33.949 1.00 26.84  ?  425  GLN B HG3    1 
ATOM   13693 H HE21   . GLN B 2 425 ? 27.352  -32.841 -36.865 1.00 29.01  ?  425  GLN B HE21   1 
ATOM   13694 H HE22   . GLN B 2 425 ? 25.876  -32.956 -36.700 1.00 29.01  ?  425  GLN B HE22   1 
ATOM   13695 N N      . GLY B 2 426 ? 31.844  -28.708 -35.693 1.00 25.02  ?  426  GLY B N      1 
ATOM   13696 C CA     . GLY B 2 426 ? 32.844  -28.358 -36.677 1.00 25.86  ?  426  GLY B CA     1 
ATOM   13697 C C      . GLY B 2 426 ? 33.723  -27.251 -36.141 1.00 23.58  ?  426  GLY B C      1 
ATOM   13698 O O      . GLY B 2 426 ? 33.582  -26.804 -35.000 1.00 23.38  ?  426  GLY B O      1 
ATOM   13699 H H      . GLY B 2 426 ? 32.067  -28.517 -34.885 1.00 30.02  ?  426  GLY B H      1 
ATOM   13700 H HA2    . GLY B 2 426 ? 33.395  -29.131 -36.878 1.00 31.03  ?  426  GLY B HA2    1 
ATOM   13701 H HA3    . GLY B 2 426 ? 32.415  -28.055 -37.492 1.00 31.03  ?  426  GLY B HA3    1 
ATOM   13702 N N      . ASP B 2 427 ? 34.644  -26.819 -36.998 1.00 22.59  ?  427  ASP B N      1 
ATOM   13703 C CA     . ASP B 2 427 ? 35.571  -25.721 -36.698 1.00 21.06  ?  427  ASP B CA     1 
ATOM   13704 C C      . ASP B 2 427 ? 35.277  -24.634 -37.726 1.00 19.94  ?  427  ASP B C      1 
ATOM   13705 O O      . ASP B 2 427 ? 35.855  -24.617 -38.821 1.00 20.69  ?  427  ASP B O      1 
ATOM   13706 C CB     . ASP B 2 427 ? 36.998  -26.196 -36.749 1.00 22.60  ?  427  ASP B CB     1 
ATOM   13707 C CG     . ASP B 2 427 ? 37.310  -27.189 -35.647 1.00 25.38  ?  427  ASP B CG     1 
ATOM   13708 O OD1    . ASP B 2 427 ? 37.147  -26.824 -34.460 1.00 25.39  ?  427  ASP B OD1    1 
ATOM   13709 O OD2    . ASP B 2 427 ? 37.680  -28.331 -35.974 1.00 29.51  -1 427  ASP B OD2    1 
ATOM   13710 H H      . ASP B 2 427 ? 34.756  -27.156 -37.782 1.00 27.10  ?  427  ASP B H      1 
ATOM   13711 H HA     . ASP B 2 427 ? 35.415  -25.367 -35.808 1.00 25.27  ?  427  ASP B HA     1 
ATOM   13712 H HB2    . ASP B 2 427 ? 37.159  -26.630 -37.601 1.00 27.12  ?  427  ASP B HB2    1 
ATOM   13713 H HB3    . ASP B 2 427 ? 37.591  -25.435 -36.647 1.00 27.12  ?  427  ASP B HB3    1 
ATOM   13714 N N      . ILE B 2 428 ? 34.365  -23.728 -37.362 1.00 18.22  ?  428  ILE B N      1 
ATOM   13715 C CA     . ILE B 2 428 ? 33.810  -22.756 -38.295 1.00 17.76  ?  428  ILE B CA     1 
ATOM   13716 C C      . ILE B 2 428 ? 33.639  -21.457 -37.529 1.00 17.79  ?  428  ILE B C      1 
ATOM   13717 O O      . ILE B 2 428 ? 33.034  -21.445 -36.449 1.00 18.46  ?  428  ILE B O      1 
ATOM   13718 C CB     . ILE B 2 428 ? 32.428  -23.198 -38.822 1.00 16.22  ?  428  ILE B CB     1 
ATOM   13719 C CG1    . ILE B 2 428 ? 32.457  -24.563 -39.502 1.00 16.08  ?  428  ILE B CG1    1 
ATOM   13720 C CG2    . ILE B 2 428 ? 31.873  -22.141 -39.781 1.00 18.69  ?  428  ILE B CG2    1 
ATOM   13721 C CD1    . ILE B 2 428 ? 31.110  -25.267 -39.487 1.00 17.74  ?  428  ILE B CD1    1 
ATOM   13722 H H      . ILE B 2 428 ? 34.050  -23.661 -36.565 1.00 21.87  ?  428  ILE B H      1 
ATOM   13723 H HA     . ILE B 2 428 ? 34.416  -22.637 -39.043 1.00 21.31  ?  428  ILE B HA     1 
ATOM   13724 H HB     . ILE B 2 428 ? 31.848  -23.283 -38.049 1.00 19.46  ?  428  ILE B HB     1 
ATOM   13725 H HG12   . ILE B 2 428 ? 32.723  -24.447 -40.428 1.00 19.29  ?  428  ILE B HG12   1 
ATOM   13726 H HG13   . ILE B 2 428 ? 33.095  -25.130 -39.042 1.00 19.29  ?  428  ILE B HG13   1 
ATOM   13727 H HG21   . ILE B 2 428 ? 31.079  -22.493 -40.213 1.00 22.42  ?  428  ILE B HG21   1 
ATOM   13728 H HG22   . ILE B 2 428 ? 31.650  -21.343 -39.276 1.00 22.42  ?  428  ILE B HG22   1 
ATOM   13729 H HG23   . ILE B 2 428 ? 32.547  -21.934 -40.446 1.00 22.42  ?  428  ILE B HG23   1 
ATOM   13730 H HD11   . ILE B 2 428 ? 31.178  -26.090 -39.996 1.00 21.29  ?  428  ILE B HD11   1 
ATOM   13731 H HD12   . ILE B 2 428 ? 30.867  -25.464 -38.569 1.00 21.29  ?  428  ILE B HD12   1 
ATOM   13732 H HD13   . ILE B 2 428 ? 30.445  -24.685 -39.887 1.00 21.29  ?  428  ILE B HD13   1 
ATOM   13733 N N      . LEU B 2 429 ? 34.131  -20.353 -38.094 1.00 17.16  ?  429  LEU B N      1 
ATOM   13734 C CA     . LEU B 2 429 ? 33.913  -19.025 -37.537 1.00 17.21  ?  429  LEU B CA     1 
ATOM   13735 C C      . LEU B 2 429 ? 32.836  -18.356 -38.378 1.00 16.58  ?  429  LEU B C      1 
ATOM   13736 O O      . LEU B 2 429 ? 33.005  -18.176 -39.598 1.00 16.52  ?  429  LEU B O      1 
ATOM   13737 C CB     . LEU B 2 429 ? 35.192  -18.197 -37.572 1.00 17.86  ?  429  LEU B CB     1 
ATOM   13738 C CG     . LEU B 2 429 ? 35.115  -16.860 -36.825 1.00 18.24  ?  429  LEU B CG     1 
ATOM   13739 C CD1    . LEU B 2 429 ? 35.030  -17.135 -35.332 1.00 18.42  ?  429  LEU B CD1    1 
ATOM   13740 C CD2    . LEU B 2 429 ? 36.331  -16.014 -37.170 1.00 18.20  ?  429  LEU B CD2    1 
ATOM   13741 H H      . LEU B 2 429 ? 34.602  -20.354 -38.813 1.00 20.59  ?  429  LEU B H      1 
ATOM   13742 H HA     . LEU B 2 429 ? 33.625  -19.091 -36.613 1.00 20.65  ?  429  LEU B HA     1 
ATOM   13743 H HB2    . LEU B 2 429 ? 35.905  -18.717 -37.169 1.00 21.43  ?  429  LEU B HB2    1 
ATOM   13744 H HB3    . LEU B 2 429 ? 35.406  -18.002 -38.498 1.00 21.43  ?  429  LEU B HB3    1 
ATOM   13745 H HG     . LEU B 2 429 ? 34.327  -16.359 -37.086 1.00 21.89  ?  429  LEU B HG     1 
ATOM   13746 H HD11   . LEU B 2 429 ? 35.152  -16.302 -34.850 1.00 22.10  ?  429  LEU B HD11   1 
ATOM   13747 H HD12   . LEU B 2 429 ? 34.158  -17.509 -35.129 1.00 22.10  ?  429  LEU B HD12   1 
ATOM   13748 H HD13   . LEU B 2 429 ? 35.726  -17.764 -35.086 1.00 22.10  ?  429  LEU B HD13   1 
ATOM   13749 H HD21   . LEU B 2 429 ? 36.293  -15.186 -36.666 1.00 21.84  ?  429  LEU B HD21   1 
ATOM   13750 H HD22   . LEU B 2 429 ? 37.135  -16.505 -36.939 1.00 21.84  ?  429  LEU B HD22   1 
ATOM   13751 H HD23   . LEU B 2 429 ? 36.323  -15.822 -38.121 1.00 21.84  ?  429  LEU B HD23   1 
ATOM   13752 N N      . GLY B 2 430 ? 31.726  -17.998 -37.737 1.00 17.10  ?  430  GLY B N      1 
ATOM   13753 C CA     . GLY B 2 430 ? 30.575  -17.448 -38.428 1.00 15.04  ?  430  GLY B CA     1 
ATOM   13754 C C      . GLY B 2 430 ? 30.371  -15.962 -38.201 1.00 15.67  ?  430  GLY B C      1 
ATOM   13755 O O      . GLY B 2 430 ? 30.693  -15.418 -37.135 1.00 16.54  ?  430  GLY B O      1 
ATOM   13756 H H      . GLY B 2 430 ? 31.620  -18.068 -36.886 1.00 20.51  ?  430  GLY B H      1 
ATOM   13757 H HA2    . GLY B 2 430 ? 30.680  -17.593 -39.381 1.00 18.04  ?  430  GLY B HA2    1 
ATOM   13758 H HA3    . GLY B 2 430 ? 29.776  -17.908 -38.126 1.00 18.04  ?  430  GLY B HA3    1 
ATOM   13759 N N      . PHE B 2 431 ? 29.826  -15.310 -39.230 1.00 15.79  ?  431  PHE B N      1 
ATOM   13760 C CA     . PHE B 2 431 ? 29.575  -13.880 -39.240 1.00 15.00  ?  431  PHE B CA     1 
ATOM   13761 C C      . PHE B 2 431 ? 28.148  -13.611 -39.707 1.00 15.11  ?  431  PHE B C      1 
ATOM   13762 O O      . PHE B 2 431 ? 27.704  -14.156 -40.724 1.00 15.12  ?  431  PHE B O      1 
ATOM   13763 C CB     . PHE B 2 431 ? 30.530  -13.165 -40.194 1.00 16.81  ?  431  PHE B CB     1 
ATOM   13764 C CG     . PHE B 2 431 ? 31.981  -13.333 -39.860 1.00 16.85  ?  431  PHE B CG     1 
ATOM   13765 C CD1    . PHE B 2 431 ? 32.674  -14.477 -40.243 1.00 17.52  ?  431  PHE B CD1    1 
ATOM   13766 C CD2    . PHE B 2 431 ? 32.663  -12.345 -39.162 1.00 17.21  ?  431  PHE B CD2    1 
ATOM   13767 C CE1    . PHE B 2 431 ? 34.007  -14.620 -39.941 1.00 17.74  ?  431  PHE B CE1    1 
ATOM   13768 C CE2    . PHE B 2 431 ? 33.988  -12.486 -38.864 1.00 18.42  ?  431  PHE B CE2    1 
ATOM   13769 C CZ     . PHE B 2 431 ? 34.663  -13.633 -39.258 1.00 17.53  ?  431  PHE B CZ     1 
ATOM   13770 H H      . PHE B 2 431 ? 29.586  -15.698 -39.960 1.00 18.94  ?  431  PHE B H      1 
ATOM   13771 H HA     . PHE B 2 431 ? 29.687  -13.540 -38.339 1.00 17.99  ?  431  PHE B HA     1 
ATOM   13772 H HB2    . PHE B 2 431 ? 30.392  -13.514 -41.088 1.00 20.17  ?  431  PHE B HB2    1 
ATOM   13773 H HB3    . PHE B 2 431 ? 30.332  -12.216 -40.175 1.00 20.17  ?  431  PHE B HB3    1 
ATOM   13774 H HD1    . PHE B 2 431 ? 32.232  -15.151 -40.707 1.00 21.02  ?  431  PHE B HD1    1 
ATOM   13775 H HD2    . PHE B 2 431 ? 32.212  -11.577 -38.894 1.00 20.65  ?  431  PHE B HD2    1 
ATOM   13776 H HE1    . PHE B 2 431 ? 34.463  -15.388 -40.202 1.00 21.28  ?  431  PHE B HE1    1 
ATOM   13777 H HE2    . PHE B 2 431 ? 34.436  -11.817 -38.399 1.00 22.10  ?  431  PHE B HE2    1 
ATOM   13778 H HZ     . PHE B 2 431 ? 35.566  -13.732 -39.056 1.00 21.03  ?  431  PHE B HZ     1 
ATOM   13779 N N      . ALA B 2 432 ? 27.441  -12.768 -38.960 1.00 15.36  ?  432  ALA B N      1 
ATOM   13780 C CA     . ALA B 2 432 ? 26.096  -12.320 -39.329 1.00 15.28  ?  432  ALA B CA     1 
ATOM   13781 C C      . ALA B 2 432 ? 25.926  -10.903 -38.785 1.00 14.83  ?  432  ALA B C      1 
ATOM   13782 O O      . ALA B 2 432 ? 25.125  -10.652 -37.883 1.00 15.87  ?  432  ALA B O      1 
ATOM   13783 C CB     . ALA B 2 432 ? 25.039  -13.271 -38.766 1.00 16.07  ?  432  ALA B CB     1 
ATOM   13784 H H      . ALA B 2 432 ? 27.723  -12.433 -38.220 1.00 18.43  ?  432  ALA B H      1 
ATOM   13785 H HA     . ALA B 2 432 ? 25.994  -12.304 -40.294 1.00 18.33  ?  432  ALA B HA     1 
ATOM   13786 H HB1    . ALA B 2 432 ? 24.158  -12.945 -39.012 1.00 19.28  ?  432  ALA B HB1    1 
ATOM   13787 H HB2    . ALA B 2 432 ? 25.180  -14.156 -39.138 1.00 19.28  ?  432  ALA B HB2    1 
ATOM   13788 H HB3    . ALA B 2 432 ? 25.122  -13.300 -37.800 1.00 19.28  ?  432  ALA B HB3    1 
ATOM   13789 N N      . PRO B 2 433 ? 26.671  -9.947  -39.315 1.00 17.09  ?  433  PRO B N      1 
ATOM   13790 C CA     . PRO B 2 433 ? 26.686  -8.625  -38.695 1.00 17.37  ?  433  PRO B CA     1 
ATOM   13791 C C      . PRO B 2 433 ? 25.386  -7.883  -38.947 1.00 16.60  ?  433  PRO B C      1 
ATOM   13792 O O      . PRO B 2 433 ? 24.588  -8.276  -39.815 1.00 16.92  ?  433  PRO B O      1 
ATOM   13793 C CB     . PRO B 2 433 ? 27.886  -7.933  -39.360 1.00 18.68  ?  433  PRO B CB     1 
ATOM   13794 C CG     . PRO B 2 433 ? 28.066  -8.646  -40.655 1.00 20.33  ?  433  PRO B CG     1 
ATOM   13795 C CD     . PRO B 2 433 ? 27.627  -10.060 -40.442 1.00 17.34  ?  433  PRO B CD     1 
ATOM   13796 H HA     . PRO B 2 433 ? 26.839  -8.687  -37.739 1.00 20.84  ?  433  PRO B HA     1 
ATOM   13797 H HB2    . PRO B 2 433 ? 27.690  -6.994  -39.504 1.00 22.42  ?  433  PRO B HB2    1 
ATOM   13798 H HB3    . PRO B 2 433 ? 28.673  -8.025  -38.800 1.00 22.42  ?  433  PRO B HB3    1 
ATOM   13799 H HG2    . PRO B 2 433 ? 27.521  -8.220  -41.335 1.00 24.39  ?  433  PRO B HG2    1 
ATOM   13800 H HG3    . PRO B 2 433 ? 29.001  -8.616  -40.912 1.00 24.39  ?  433  PRO B HG3    1 
ATOM   13801 H HD2    . PRO B 2 433 ? 27.189  -10.409 -41.234 1.00 20.81  ?  433  PRO B HD2    1 
ATOM   13802 H HD3    . PRO B 2 433 ? 28.379  -10.624 -40.203 1.00 20.81  ?  433  PRO B HD3    1 
ATOM   13803 N N      . PRO B 2 434 ? 25.128  -6.805  -38.209 1.00 15.75  ?  434  PRO B N      1 
ATOM   13804 C CA     . PRO B 2 434 ? 23.919  -6.011  -38.468 1.00 15.65  ?  434  PRO B CA     1 
ATOM   13805 C C      . PRO B 2 434 ? 23.854  -5.535  -39.917 1.00 15.57  ?  434  PRO B C      1 
ATOM   13806 O O      . PRO B 2 434 ? 24.873  -5.338  -40.586 1.00 17.26  ?  434  PRO B O      1 
ATOM   13807 C CB     . PRO B 2 434 ? 24.041  -4.839  -37.476 1.00 16.99  ?  434  PRO B CB     1 
ATOM   13808 C CG     . PRO B 2 434 ? 24.861  -5.438  -36.321 1.00 17.94  ?  434  PRO B CG     1 
ATOM   13809 C CD     . PRO B 2 434 ? 25.889  -6.285  -37.058 1.00 15.44  ?  434  PRO B CD     1 
ATOM   13810 H HA     . PRO B 2 434 ? 23.122  -6.525  -38.266 1.00 18.78  ?  434  PRO B HA     1 
ATOM   13811 H HB2    . PRO B 2 434 ? 24.504  -4.094  -37.890 1.00 20.38  ?  434  PRO B HB2    1 
ATOM   13812 H HB3    . PRO B 2 434 ? 23.162  -4.557  -37.177 1.00 20.38  ?  434  PRO B HB3    1 
ATOM   13813 H HG2    . PRO B 2 434 ? 25.284  -4.735  -35.802 1.00 21.53  ?  434  PRO B HG2    1 
ATOM   13814 H HG3    . PRO B 2 434 ? 24.297  -5.980  -35.747 1.00 21.53  ?  434  PRO B HG3    1 
ATOM   13815 H HD2    . PRO B 2 434 ? 26.637  -5.743  -37.354 1.00 18.52  ?  434  PRO B HD2    1 
ATOM   13816 H HD3    . PRO B 2 434 ? 26.206  -7.010  -36.497 1.00 18.52  ?  434  PRO B HD3    1 
ATOM   13817 N N      . LEU B 2 435 ? 22.625  -5.373  -40.415 1.00 15.39  ?  435  LEU B N      1 
ATOM   13818 C CA     . LEU B 2 435 ? 22.450  -4.994  -41.813 1.00 16.02  ?  435  LEU B CA     1 
ATOM   13819 C C      . LEU B 2 435 ? 22.807  -3.540  -42.075 1.00 16.99  ?  435  LEU B C      1 
ATOM   13820 O O      . LEU B 2 435 ? 22.852  -3.133  -43.244 1.00 18.99  ?  435  LEU B O      1 
ATOM   13821 C CB     . LEU B 2 435 ? 21.027  -5.289  -42.277 1.00 16.24  ?  435  LEU B CB     1 
ATOM   13822 C CG     . LEU B 2 435 ? 20.496  -6.696  -41.979 1.00 17.05  ?  435  LEU B CG     1 
ATOM   13823 C CD1    . LEU B 2 435 ? 19.141  -6.925  -42.660 1.00 17.23  ?  435  LEU B CD1    1 
ATOM   13824 C CD2    . LEU B 2 435 ? 21.482  -7.773  -42.418 1.00 17.77  ?  435  LEU B CD2    1 
ATOM   13825 H H      . LEU B 2 435 ? 21.895  -5.475  -39.973 1.00 18.46  ?  435  LEU B H      1 
ATOM   13826 H HA     . LEU B 2 435 ? 23.040  -5.540  -42.356 1.00 19.22  ?  435  LEU B HA     1 
ATOM   13827 H HB2    . LEU B 2 435 ? 20.431  -4.660  -41.841 1.00 19.49  ?  435  LEU B HB2    1 
ATOM   13828 H HB3    . LEU B 2 435 ? 20.992  -5.168  -43.239 1.00 19.49  ?  435  LEU B HB3    1 
ATOM   13829 H HG     . LEU B 2 435 ? 20.379  -6.770  -41.019 1.00 20.46  ?  435  LEU B HG     1 
ATOM   13830 H HD11   . LEU B 2 435 ? 18.796  -7.792  -42.394 1.00 20.67  ?  435  LEU B HD11   1 
ATOM   13831 H HD12   . LEU B 2 435 ? 18.527  -6.226  -42.385 1.00 20.67  ?  435  LEU B HD12   1 
ATOM   13832 H HD13   . LEU B 2 435 ? 19.263  -6.898  -43.622 1.00 20.67  ?  435  LEU B HD13   1 
ATOM   13833 H HD21   . LEU B 2 435 ? 21.120  -8.644  -42.190 1.00 21.32  ?  435  LEU B HD21   1 
ATOM   13834 H HD22   . LEU B 2 435 ? 21.613  -7.709  -43.377 1.00 21.32  ?  435  LEU B HD22   1 
ATOM   13835 H HD23   . LEU B 2 435 ? 22.325  -7.635  -41.959 1.00 21.32  ?  435  LEU B HD23   1 
ATOM   13836 N N      . VAL B 2 436 ? 23.059  -2.760  -41.019 1.00 17.48  ?  436  VAL B N      1 
ATOM   13837 C CA     . VAL B 2 436 ? 23.543  -1.388  -41.171 1.00 18.36  ?  436  VAL B CA     1 
ATOM   13838 C C      . VAL B 2 436 ? 25.052  -1.303  -41.343 1.00 17.96  ?  436  VAL B C      1 
ATOM   13839 O O      . VAL B 2 436 ? 25.581  -0.205  -41.547 1.00 18.10  ?  436  VAL B O      1 
ATOM   13840 C CB     . VAL B 2 436 ? 23.135  -0.546  -39.942 1.00 18.66  ?  436  VAL B CB     1 
ATOM   13841 C CG1    . VAL B 2 436 ? 21.636  -0.396  -39.870 1.00 20.02  ?  436  VAL B CG1    1 
ATOM   13842 C CG2    . VAL B 2 436 ? 23.659  -1.167  -38.652 1.00 20.50  ?  436  VAL B CG2    1 
ATOM   13843 H H      . VAL B 2 436 ? 22.956  -3.003  -40.201 1.00 20.97  ?  436  VAL B H      1 
ATOM   13844 H HA     . VAL B 2 436 ? 23.139  -1.014  -41.970 1.00 22.03  ?  436  VAL B HA     1 
ATOM   13845 H HB     . VAL B 2 436 ? 23.530  0.334   -40.038 1.00 22.39  ?  436  VAL B HB     1 
ATOM   13846 H HG11   . VAL B 2 436 ? 21.408  0.121   -39.081 1.00 24.02  ?  436  VAL B HG11   1 
ATOM   13847 H HG12   . VAL B 2 436 ? 21.325  0.062   -40.666 1.00 24.02  ?  436  VAL B HG12   1 
ATOM   13848 H HG13   . VAL B 2 436 ? 21.232  -1.276  -39.816 1.00 24.02  ?  436  VAL B HG13   1 
ATOM   13849 H HG21   . VAL B 2 436 ? 23.514  -0.545  -37.922 1.00 24.59  ?  436  VAL B HG21   1 
ATOM   13850 H HG22   . VAL B 2 436 ? 23.180  -1.993  -38.483 1.00 24.59  ?  436  VAL B HG22   1 
ATOM   13851 H HG23   . VAL B 2 436 ? 24.607  -1.347  -38.751 1.00 24.59  ?  436  VAL B HG23   1 
ATOM   13852 N N      . THR B 2 437 ? 25.765  -2.426  -41.267 1.00 15.76  ?  437  THR B N      1 
ATOM   13853 C CA     . THR B 2 437 ? 27.221  -2.401  -41.311 1.00 16.27  ?  437  THR B CA     1 
ATOM   13854 C C      . THR B 2 437 ? 27.703  -1.741  -42.601 1.00 17.06  ?  437  THR B C      1 
ATOM   13855 O O      . THR B 2 437 ? 27.172  -2.009  -43.695 1.00 18.09  ?  437  THR B O      1 
ATOM   13856 C CB     . THR B 2 437 ? 27.737  -3.840  -41.254 1.00 17.87  ?  437  THR B CB     1 
ATOM   13857 O OG1    . THR B 2 437 ? 27.340  -4.458  -40.032 1.00 18.25  ?  437  THR B OG1    1 
ATOM   13858 C CG2    . THR B 2 437 ? 29.236  -3.879  -41.346 1.00 18.43  ?  437  THR B CG2    1 
ATOM   13859 H H      . THR B 2 437 ? 25.431  -3.214  -41.188 1.00 18.90  ?  437  THR B H      1 
ATOM   13860 H HA     . THR B 2 437 ? 27.571  -1.897  -40.560 1.00 19.52  ?  437  THR B HA     1 
ATOM   13861 H HB     . THR B 2 437 ? 27.365  -4.331  -42.003 1.00 21.44  ?  437  THR B HB     1 
ATOM   13862 H HG1    . THR B 2 437 ? 26.504  -4.534  -40.007 1.00 21.89  ?  437  THR B HG1    1 
ATOM   13863 H HG21   . THR B 2 437 ? 29.561  -4.759  -41.101 1.00 22.12  ?  437  THR B HG21   1 
ATOM   13864 H HG22   . THR B 2 437 ? 29.517  -3.680  -42.253 1.00 22.12  ?  437  THR B HG22   1 
ATOM   13865 H HG23   . THR B 2 437 ? 29.622  -3.222  -40.746 1.00 22.12  ?  437  THR B HG23   1 
ATOM   13866 N N      . THR B 2 438 ? 28.715  -0.875  -42.468 1.00 18.00  ?  438  THR B N      1 
ATOM   13867 C CA     . THR B 2 438 ? 29.284  -0.171  -43.610 1.00 17.83  ?  438  THR B CA     1 
ATOM   13868 C C      . THR B 2 438 ? 30.479  -0.939  -44.183 1.00 19.01  ?  438  THR B C      1 
ATOM   13869 O O      . THR B 2 438 ? 30.980  -1.901  -43.586 1.00 19.65  ?  438  THR B O      1 
ATOM   13870 C CB     . THR B 2 438 ? 29.794  1.202   -43.168 1.00 19.14  ?  438  THR B CB     1 
ATOM   13871 O OG1    . THR B 2 438 ? 30.956  1.013   -42.335 1.00 19.72  ?  438  THR B OG1    1 
ATOM   13872 C CG2    . THR B 2 438 ? 28.737  1.975   -42.416 1.00 19.79  ?  438  THR B CG2    1 
ATOM   13873 H H      . THR B 2 438 ? 29.089  -0.682  -41.718 1.00 21.59  ?  438  THR B H      1 
ATOM   13874 H HA     . THR B 2 438 ? 28.595  -0.080  -44.286 1.00 21.40  ?  438  THR B HA     1 
ATOM   13875 H HB     . THR B 2 438 ? 30.025  1.731   -43.947 1.00 22.96  ?  438  THR B HB     1 
ATOM   13876 H HG1    . THR B 2 438 ? 31.245  1.757   -42.073 1.00 23.66  ?  438  THR B HG1    1 
ATOM   13877 H HG21   . THR B 2 438 ? 29.054  2.871   -42.224 1.00 23.74  ?  438  THR B HG21   1 
ATOM   13878 H HG22   . THR B 2 438 ? 27.928  2.034   -42.949 1.00 23.74  ?  438  THR B HG22   1 
ATOM   13879 H HG23   . THR B 2 438 ? 28.531  1.528   -41.580 1.00 23.74  ?  438  THR B HG23   1 
ATOM   13880 N N      . ARG B 2 439 ? 30.972  -0.479  -45.337 1.00 18.97  ?  439  ARG B N      1 
ATOM   13881 C CA     . ARG B 2 439 ? 32.164  -1.099  -45.917 1.00 19.86  ?  439  ARG B CA     1 
ATOM   13882 C C      . ARG B 2 439 ? 33.375  -0.936  -45.001 1.00 20.58  ?  439  ARG B C      1 
ATOM   13883 O O      . ARG B 2 439 ? 34.175  -1.867  -44.850 1.00 19.55  ?  439  ARG B O      1 
ATOM   13884 C CB     . ARG B 2 439 ? 32.460  -0.510  -47.300 1.00 21.88  ?  439  ARG B CB     1 
ATOM   13885 C CG     . ARG B 2 439 ? 31.418  -0.902  -48.352 1.00 25.61  ?  439  ARG B CG     1 
ATOM   13886 C CD     . ARG B 2 439 ? 31.957  -0.620  -49.745 1.00 30.87  ?  439  ARG B CD     1 
ATOM   13887 N NE     . ARG B 2 439 ? 30.939  -0.776  -50.778 1.00 36.65  ?  439  ARG B NE     1 
ATOM   13888 C CZ     . ARG B 2 439 ? 31.215  -0.894  -52.074 1.00 42.15  ?  439  ARG B CZ     1 
ATOM   13889 N NH1    . ARG B 2 439 ? 32.475  -0.904  -52.484 1.00 43.92  ?  439  ARG B NH1    1 
ATOM   13890 N NH2    . ARG B 2 439 ? 30.235  -1.015  -52.962 1.00 44.76  ?  439  ARG B NH2    1 
ATOM   13891 H H      . ARG B 2 439 ? 30.645  0.172   -45.794 1.00 22.77  ?  439  ARG B H      1 
ATOM   13892 H HA     . ARG B 2 439 ? 31.990  -2.047  -46.028 1.00 23.83  ?  439  ARG B HA     1 
ATOM   13893 H HB2    . ARG B 2 439 ? 32.470  0.457   -47.234 1.00 26.25  ?  439  ARG B HB2    1 
ATOM   13894 H HB3    . ARG B 2 439 ? 33.324  -0.832  -47.600 1.00 26.25  ?  439  ARG B HB3    1 
ATOM   13895 H HG2    . ARG B 2 439 ? 31.220  -1.849  -48.281 1.00 30.73  ?  439  ARG B HG2    1 
ATOM   13896 H HG3    . ARG B 2 439 ? 30.609  -0.383  -48.221 1.00 30.73  ?  439  ARG B HG3    1 
ATOM   13897 H HD2    . ARG B 2 439 ? 32.284  0.293   -49.781 1.00 37.04  ?  439  ARG B HD2    1 
ATOM   13898 H HD3    . ARG B 2 439 ? 32.679  -1.239  -49.938 1.00 37.04  ?  439  ARG B HD3    1 
ATOM   13899 H HE     . ARG B 2 439 ? 30.114  -0.793  -50.536 1.00 43.98  ?  439  ARG B HE     1 
ATOM   13900 H HH11   . ARG B 2 439 ? 33.114  -0.833  -51.912 1.00 52.70  ?  439  ARG B HH11   1 
ATOM   13901 H HH12   . ARG B 2 439 ? 32.655  -0.980  -53.321 1.00 52.70  ?  439  ARG B HH12   1 
ATOM   13902 H HH21   . ARG B 2 439 ? 29.415  -1.018  -52.701 1.00 53.70  ?  439  ARG B HH21   1 
ATOM   13903 H HH22   . ARG B 2 439 ? 30.419  -1.091  -53.799 1.00 53.70  ?  439  ARG B HH22   1 
ATOM   13904 N N      . ALA B 2 440 ? 33.541  0.248   -44.396 1.00 19.40  ?  440  ALA B N      1 
ATOM   13905 C CA     . ALA B 2 440 ? 34.660  0.460   -43.481 1.00 19.54  ?  440  ALA B CA     1 
ATOM   13906 C C      . ALA B 2 440 ? 34.551  -0.452  -42.269 1.00 18.82  ?  440  ALA B C      1 
ATOM   13907 O O      . ALA B 2 440 ? 35.567  -0.937  -41.752 1.00 21.01  ?  440  ALA B O      1 
ATOM   13908 C CB     . ALA B 2 440 ? 34.715  1.930   -43.051 1.00 20.95  ?  440  ALA B CB     1 
ATOM   13909 H H      . ALA B 2 440 ? 33.029  0.931   -44.497 1.00 23.27  ?  440  ALA B H      1 
ATOM   13910 H HA     . ALA B 2 440 ? 35.489  0.253   -43.941 1.00 23.44  ?  440  ALA B HA     1 
ATOM   13911 H HB1    . ALA B 2 440 ? 35.492  2.065   -42.488 1.00 25.14  ?  440  ALA B HB1    1 
ATOM   13912 H HB2    . ALA B 2 440 ? 34.778  2.488   -43.842 1.00 25.14  ?  440  ALA B HB2    1 
ATOM   13913 H HB3    . ALA B 2 440 ? 33.907  2.145   -42.558 1.00 25.14  ?  440  ALA B HB3    1 
ATOM   13914 N N      . GLU B 2 441 ? 33.325  -0.692  -41.792 1.00 18.03  ?  441  GLU B N      1 
ATOM   13915 C CA     . GLU B 2 441 ? 33.147  -1.628  -40.682 1.00 18.05  ?  441  GLU B CA     1 
ATOM   13916 C C      . GLU B 2 441 ? 33.462  -3.060  -41.099 1.00 18.24  ?  441  GLU B C      1 
ATOM   13917 O O      . GLU B 2 441 ? 34.049  -3.816  -40.319 1.00 18.63  ?  441  GLU B O      1 
ATOM   13918 C CB     . GLU B 2 441 ? 31.731  -1.487  -40.113 1.00 18.13  ?  441  GLU B CB     1 
ATOM   13919 C CG     . GLU B 2 441 ? 31.560  -0.163  -39.392 1.00 19.50  ?  441  GLU B CG     1 
ATOM   13920 C CD     . GLU B 2 441 ? 30.131  0.195   -39.013 1.00 21.27  ?  441  GLU B CD     1 
ATOM   13921 O OE1    . GLU B 2 441 ? 29.190  -0.288  -39.643 1.00 19.88  ?  441  GLU B OE1    1 
ATOM   13922 O OE2    . GLU B 2 441 ? 29.991  1.022   -38.063 1.00 21.56  -1 441  GLU B OE2    1 
ATOM   13923 H H      . GLU B 2 441 ? 32.599  -0.335  -42.084 1.00 21.63  ?  441  GLU B H      1 
ATOM   13924 H HA     . GLU B 2 441 ? 33.767  -1.408  -39.970 1.00 21.66  ?  441  GLU B HA     1 
ATOM   13925 H HB2    . GLU B 2 441 ? 31.087  -1.527  -40.837 1.00 21.75  ?  441  GLU B HB2    1 
ATOM   13926 H HB3    . GLU B 2 441 ? 31.565  -2.204  -39.481 1.00 21.75  ?  441  GLU B HB3    1 
ATOM   13927 H HG2    . GLU B 2 441 ? 32.077  -0.193  -38.572 1.00 23.40  ?  441  GLU B HG2    1 
ATOM   13928 H HG3    . GLU B 2 441 ? 31.892  0.544   -39.968 1.00 23.40  ?  441  GLU B HG3    1 
ATOM   13929 N N      . VAL B 2 442 ? 33.081  -3.454  -42.321 1.00 18.67  ?  442  VAL B N      1 
ATOM   13930 C CA     . VAL B 2 442 ? 33.500  -4.751  -42.857 1.00 18.97  ?  442  VAL B CA     1 
ATOM   13931 C C      . VAL B 2 442 ? 35.016  -4.879  -42.814 1.00 17.34  ?  442  VAL B C      1 
ATOM   13932 O O      . VAL B 2 442 ? 35.560  -5.905  -42.384 1.00 18.66  ?  442  VAL B O      1 
ATOM   13933 C CB     . VAL B 2 442 ? 32.944  -4.961  -44.277 1.00 17.97  ?  442  VAL B CB     1 
ATOM   13934 C CG1    . VAL B 2 442 ? 33.674  -6.089  -44.983 1.00 21.53  ?  442  VAL B CG1    1 
ATOM   13935 C CG2    . VAL B 2 442 ? 31.443  -5.234  -44.218 1.00 19.22  ?  442  VAL B CG2    1 
ATOM   13936 H H      . VAL B 2 442 ? 32.586  -2.995  -42.853 1.00 22.40  ?  442  VAL B H      1 
ATOM   13937 H HA     . VAL B 2 442 ? 33.131  -5.449  -42.294 1.00 22.75  ?  442  VAL B HA     1 
ATOM   13938 H HB     . VAL B 2 442 ? 33.087  -4.152  -44.793 1.00 21.56  ?  442  VAL B HB     1 
ATOM   13939 H HG11   . VAL B 2 442 ? 33.176  -6.340  -45.776 1.00 25.83  ?  442  VAL B HG11   1 
ATOM   13940 H HG12   . VAL B 2 442 ? 34.561  -5.783  -45.232 1.00 25.83  ?  442  VAL B HG12   1 
ATOM   13941 H HG13   . VAL B 2 442 ? 33.743  -6.846  -44.381 1.00 25.83  ?  442  VAL B HG13   1 
ATOM   13942 H HG21   . VAL B 2 442 ? 31.129  -5.466  -45.106 1.00 23.06  ?  442  VAL B HG21   1 
ATOM   13943 H HG22   . VAL B 2 442 ? 31.279  -5.969  -43.607 1.00 23.06  ?  442  VAL B HG22   1 
ATOM   13944 H HG23   . VAL B 2 442 ? 30.989  -4.436  -43.904 1.00 23.06  ?  442  VAL B HG23   1 
ATOM   13945 N N      . ASP B 2 443 ? 35.725  -3.839  -43.265 1.00 18.42  ?  443  ASP B N      1 
ATOM   13946 C CA     . ASP B 2 443 ? 37.179  -3.911  -43.278 1.00 18.36  ?  443  ASP B CA     1 
ATOM   13947 C C      . ASP B 2 443 ? 37.733  -4.139  -41.874 1.00 18.96  ?  443  ASP B C      1 
ATOM   13948 O O      . ASP B 2 443 ? 38.693  -4.903  -41.683 1.00 20.26  ?  443  ASP B O      1 
ATOM   13949 C CB     . ASP B 2 443 ? 37.768  -2.624  -43.848 1.00 19.80  ?  443  ASP B CB     1 
ATOM   13950 C CG     . ASP B 2 443 ? 37.626  -2.523  -45.351 1.00 20.09  ?  443  ASP B CG     1 
ATOM   13951 O OD1    . ASP B 2 443 ? 37.307  -3.534  -46.035 1.00 20.65  ?  443  ASP B OD1    1 
ATOM   13952 O OD2    . ASP B 2 443 ? 37.842  -1.404  -45.858 1.00 22.87  -1 443  ASP B OD2    1 
ATOM   13953 H H      . ASP B 2 443 ? 35.396  -3.101  -43.560 1.00 22.10  ?  443  ASP B H      1 
ATOM   13954 H HA     . ASP B 2 443 ? 37.440  -4.652  -43.847 1.00 22.03  ?  443  ASP B HA     1 
ATOM   13955 H HB2    . ASP B 2 443 ? 37.310  -1.866  -43.453 1.00 23.76  ?  443  ASP B HB2    1 
ATOM   13956 H HB3    . ASP B 2 443 ? 38.714  -2.589  -43.635 1.00 23.76  ?  443  ASP B HB3    1 
ATOM   13957 N N      . GLU B 2 444 ? 37.135  -3.499  -40.872 1.00 19.07  ?  444  GLU B N      1 
ATOM   13958 C CA     . GLU B 2 444 ? 37.635  -3.659  -39.508 1.00 20.21  ?  444  GLU B CA     1 
ATOM   13959 C C      . GLU B 2 444 ? 37.284  -5.037  -38.952 1.00 18.92  ?  444  GLU B C      1 
ATOM   13960 O O      . GLU B 2 444 ? 38.100  -5.655  -38.261 1.00 21.98  ?  444  GLU B O      1 
ATOM   13961 C CB     . GLU B 2 444 ? 37.105  -2.536  -38.620 1.00 22.66  ?  444  GLU B CB     1 
ATOM   13962 C CG     . GLU B 2 444 ? 37.552  -2.617  -37.164 1.00 24.61  ?  444  GLU B CG     1 
ATOM   13963 C CD     . GLU B 2 444 ? 39.045  -2.405  -36.986 1.00 26.50  ?  444  GLU B CD     1 
ATOM   13964 O OE1    . GLU B 2 444 ? 39.671  -1.813  -37.885 1.00 27.67  ?  444  GLU B OE1    1 
ATOM   13965 O OE2    . GLU B 2 444 ? 39.595  -2.842  -35.949 1.00 27.51  -1 444  GLU B OE2    1 
ATOM   13966 H H      . GLU B 2 444 ? 36.456  -2.977  -40.950 1.00 22.88  ?  444  GLU B H      1 
ATOM   13967 H HA     . GLU B 2 444 ? 38.602  -3.588  -39.509 1.00 24.25  ?  444  GLU B HA     1 
ATOM   13968 H HB2    . GLU B 2 444 ? 37.416  -1.689  -38.976 1.00 27.19  ?  444  GLU B HB2    1 
ATOM   13969 H HB3    . GLU B 2 444 ? 36.136  -2.565  -38.631 1.00 27.19  ?  444  GLU B HB3    1 
ATOM   13970 H HG2    . GLU B 2 444 ? 37.091  -1.932  -36.655 1.00 29.53  ?  444  GLU B HG2    1 
ATOM   13971 H HG3    . GLU B 2 444 ? 37.331  -3.495  -36.815 1.00 29.53  ?  444  GLU B HG3    1 
ATOM   13972 N N      . ILE B 2 445 ? 36.082  -5.541  -39.243 1.00 19.00  ?  445  ILE B N      1 
ATOM   13973 C CA     . ILE B 2 445 ? 35.733  -6.902  -38.854 1.00 19.36  ?  445  ILE B CA     1 
ATOM   13974 C C      . ILE B 2 445 ? 36.726  -7.895  -39.430 1.00 20.01  ?  445  ILE B C      1 
ATOM   13975 O O      . ILE B 2 445 ? 37.217  -8.789  -38.729 1.00 19.41  ?  445  ILE B O      1 
ATOM   13976 C CB     . ILE B 2 445 ? 34.298  -7.227  -39.299 1.00 18.47  ?  445  ILE B CB     1 
ATOM   13977 C CG1    . ILE B 2 445 ? 33.305  -6.441  -38.451 1.00 19.55  ?  445  ILE B CG1    1 
ATOM   13978 C CG2    . ILE B 2 445 ? 34.044  -8.739  -39.216 1.00 18.07  ?  445  ILE B CG2    1 
ATOM   13979 C CD1    . ILE B 2 445 ? 31.914  -6.401  -39.031 1.00 20.84  ?  445  ILE B CD1    1 
ATOM   13980 H H      . ILE B 2 445 ? 35.459  -5.120  -39.660 1.00 22.79  ?  445  ILE B H      1 
ATOM   13981 H HA     . ILE B 2 445 ? 35.778  -6.964  -37.887 1.00 23.23  ?  445  ILE B HA     1 
ATOM   13982 H HB     . ILE B 2 445 ? 34.180  -6.961  -40.224 1.00 22.16  ?  445  ILE B HB     1 
ATOM   13983 H HG12   . ILE B 2 445 ? 33.249  -6.851  -37.574 1.00 23.45  ?  445  ILE B HG12   1 
ATOM   13984 H HG13   . ILE B 2 445 ? 33.619  -5.526  -38.370 1.00 23.45  ?  445  ILE B HG13   1 
ATOM   13985 H HG21   . ILE B 2 445 ? 33.087  -8.900  -39.221 1.00 21.68  ?  445  ILE B HG21   1 
ATOM   13986 H HG22   . ILE B 2 445 ? 34.455  -9.171  -39.981 1.00 21.68  ?  445  ILE B HG22   1 
ATOM   13987 H HG23   . ILE B 2 445 ? 34.432  -9.080  -38.396 1.00 21.68  ?  445  ILE B HG23   1 
ATOM   13988 H HD11   . ILE B 2 445 ? 31.373  -5.785  -38.513 1.00 25.00  ?  445  ILE B HD11   1 
ATOM   13989 H HD12   . ILE B 2 445 ? 31.964  -6.101  -39.953 1.00 25.00  ?  445  ILE B HD12   1 
ATOM   13990 H HD13   . ILE B 2 445 ? 31.530  -7.291  -38.994 1.00 25.00  ?  445  ILE B HD13   1 
ATOM   13991 N N      . VAL B 2 446 ? 37.005  -7.773  -40.732 1.00 19.27  ?  446  VAL B N      1 
ATOM   13992 C CA     . VAL B 2 446 ? 37.907  -8.703  -41.401 1.00 17.65  ?  446  VAL B CA     1 
ATOM   13993 C C      . VAL B 2 446 ? 39.301  -8.610  -40.806 1.00 19.78  ?  446  VAL B C      1 
ATOM   13994 O O      . VAL B 2 446 ? 39.983  -9.629  -40.620 1.00 20.81  ?  446  VAL B O      1 
ATOM   13995 C CB     . VAL B 2 446 ? 37.906  -8.427  -42.915 1.00 19.78  ?  446  VAL B CB     1 
ATOM   13996 C CG1    . VAL B 2 446 ? 39.036  -9.196  -43.580 1.00 22.90  ?  446  VAL B CG1    1 
ATOM   13997 C CG2    . VAL B 2 446 ? 36.561  -8.817  -43.532 1.00 20.90  ?  446  VAL B CG2    1 
ATOM   13998 H H      . VAL B 2 446 ? 36.685  -7.163  -41.247 1.00 23.12  ?  446  VAL B H      1 
ATOM   13999 H HA     . VAL B 2 446 ? 37.590  -9.609  -41.260 1.00 21.18  ?  446  VAL B HA     1 
ATOM   14000 H HB     . VAL B 2 446 ? 38.042  -7.479  -43.067 1.00 23.74  ?  446  VAL B HB     1 
ATOM   14001 H HG11   . VAL B 2 446 ? 38.860  -9.257  -44.532 1.00 27.48  ?  446  VAL B HG11   1 
ATOM   14002 H HG12   . VAL B 2 446 ? 39.871  -8.726  -43.427 1.00 27.48  ?  446  VAL B HG12   1 
ATOM   14003 H HG13   . VAL B 2 446 ? 39.082  -10.086 -43.195 1.00 27.48  ?  446  VAL B HG13   1 
ATOM   14004 H HG21   . VAL B 2 446 ? 36.569  -8.592  -44.475 1.00 25.08  ?  446  VAL B HG21   1 
ATOM   14005 H HG22   . VAL B 2 446 ? 36.428  -9.771  -43.421 1.00 25.08  ?  446  VAL B HG22   1 
ATOM   14006 H HG23   . VAL B 2 446 ? 35.854  -8.330  -43.081 1.00 25.08  ?  446  VAL B HG23   1 
ATOM   14007 N N      . ALA B 2 447 ? 39.761  -7.387  -40.524 1.00 21.45  ?  447  ALA B N      1 
ATOM   14008 C CA     . ALA B 2 447 ? 41.099  -7.217  -39.977 1.00 21.50  ?  447  ALA B CA     1 
ATOM   14009 C C      . ALA B 2 447 ? 41.219  -7.851  -38.595 1.00 22.08  ?  447  ALA B C      1 
ATOM   14010 O O      . ALA B 2 447 ? 42.234  -8.490  -38.282 1.00 22.83  ?  447  ALA B O      1 
ATOM   14011 C CB     . ALA B 2 447 ? 41.457  -5.735  -39.922 1.00 21.17  ?  447  ALA B CB     1 
ATOM   14012 H H      . ALA B 2 447 ? 39.325  -6.655  -40.638 1.00 25.73  ?  447  ALA B H      1 
ATOM   14013 H HA     . ALA B 2 447 ? 41.733  -7.658  -40.563 1.00 25.79  ?  447  ALA B HA     1 
ATOM   14014 H HB1    . ALA B 2 447 ? 42.362  -5.642  -39.585 1.00 25.40  ?  447  ALA B HB1    1 
ATOM   14015 H HB2    . ALA B 2 447 ? 41.396  -5.362  -40.815 1.00 25.40  ?  447  ALA B HB2    1 
ATOM   14016 H HB3    . ALA B 2 447 ? 40.836  -5.282  -39.331 1.00 25.40  ?  447  ALA B HB3    1 
ATOM   14017 N N      . ARG B 2 448 ? 40.188  -7.697  -37.749 1.00 21.19  ?  448  ARG B N      1 
ATOM   14018 C CA     . ARG B 2 448 ? 40.214  -8.324  -36.429 1.00 19.88  ?  448  ARG B CA     1 
ATOM   14019 C C      . ARG B 2 448 ? 40.148  -9.842  -36.548 1.00 21.45  ?  448  ARG B C      1 
ATOM   14020 O O      . ARG B 2 448 ? 40.853  -10.560 -35.826 1.00 19.62  ?  448  ARG B O      1 
ATOM   14021 C CB     . ARG B 2 448 ? 39.072  -7.777  -35.571 1.00 19.92  ?  448  ARG B CB     1 
ATOM   14022 C CG     . ARG B 2 448 ? 39.234  -6.314  -35.181 1.00 20.14  ?  448  ARG B CG     1 
ATOM   14023 C CD     . ARG B 2 448 ? 38.090  -5.810  -34.296 1.00 21.48  ?  448  ARG B CD     1 
ATOM   14024 N NE     . ARG B 2 448 ? 38.158  -4.345  -34.175 1.00 21.34  ?  448  ARG B NE     1 
ATOM   14025 C CZ     . ARG B 2 448 ? 37.502  -3.613  -33.288 1.00 21.81  ?  448  ARG B CZ     1 
ATOM   14026 N NH1    . ARG B 2 448 ? 36.725  -4.187  -32.370 1.00 23.07  ?  448  ARG B NH1    1 
ATOM   14027 N NH2    . ARG B 2 448 ? 37.637  -2.284  -33.318 1.00 22.82  ?  448  ARG B NH2    1 
ATOM   14028 H H      . ARG B 2 448 ? 39.477  -7.242  -37.914 1.00 25.43  ?  448  ARG B H      1 
ATOM   14029 H HA     . ARG B 2 448 ? 41.045  -8.102  -35.981 1.00 23.85  ?  448  ARG B HA     1 
ATOM   14030 H HB2    . ARG B 2 448 ? 38.243  -7.859  -36.068 1.00 23.90  ?  448  ARG B HB2    1 
ATOM   14031 H HB3    . ARG B 2 448 ? 39.022  -8.296  -34.754 1.00 23.90  ?  448  ARG B HB3    1 
ATOM   14032 H HG2    . ARG B 2 448 ? 40.063  -6.207  -34.689 1.00 24.17  ?  448  ARG B HG2    1 
ATOM   14033 H HG3    . ARG B 2 448 ? 39.253  -5.772  -35.985 1.00 24.17  ?  448  ARG B HG3    1 
ATOM   14034 H HD2    . ARG B 2 448 ? 37.239  -6.051  -34.694 1.00 25.78  ?  448  ARG B HD2    1 
ATOM   14035 H HD3    . ARG B 2 448 ? 38.165  -6.200  -33.411 1.00 25.78  ?  448  ARG B HD3    1 
ATOM   14036 H HE     . ARG B 2 448 ? 38.669  -3.928  -34.727 1.00 25.61  ?  448  ARG B HE     1 
ATOM   14037 H HH11   . ARG B 2 448 ? 36.645  -5.043  -32.348 1.00 27.68  ?  448  ARG B HH11   1 
ATOM   14038 H HH12   . ARG B 2 448 ? 36.303  -3.701  -31.799 1.00 27.68  ?  448  ARG B HH12   1 
ATOM   14039 H HH21   . ARG B 2 448 ? 38.145  -1.917  -33.907 1.00 27.38  ?  448  ARG B HH21   1 
ATOM   14040 H HH22   . ARG B 2 448 ? 37.216  -1.797  -32.748 1.00 27.38  ?  448  ARG B HH22   1 
ATOM   14041 N N      . ALA B 2 449 ? 39.329  -10.344 -37.472 1.00 21.99  ?  449  ALA B N      1 
ATOM   14042 C CA     . ALA B 2 449 ? 39.257  -11.788 -37.688 1.00 20.96  ?  449  ALA B CA     1 
ATOM   14043 C C      . ALA B 2 449 ? 40.598  -12.341 -38.160 1.00 21.06  ?  449  ALA B C      1 
ATOM   14044 O O      . ALA B 2 449 ? 41.020  -13.418 -37.722 1.00 22.57  ?  449  ALA B O      1 
ATOM   14045 C CB     . ALA B 2 449 ? 38.149  -12.142 -38.685 1.00 20.30  ?  449  ALA B CB     1 
ATOM   14046 H H      . ALA B 2 449 ? 38.813  -9.880  -37.981 1.00 26.39  ?  449  ALA B H      1 
ATOM   14047 H HA     . ALA B 2 449 ? 39.030  -12.208 -36.843 1.00 25.15  ?  449  ALA B HA     1 
ATOM   14048 H HB1    . ALA B 2 449 ? 38.112  -13.106 -38.787 1.00 24.35  ?  449  ALA B HB1    1 
ATOM   14049 H HB2    . ALA B 2 449 ? 37.302  -11.812 -38.346 1.00 24.35  ?  449  ALA B HB2    1 
ATOM   14050 H HB3    . ALA B 2 449 ? 38.348  -11.727 -39.539 1.00 24.35  ?  449  ALA B HB3    1 
ATOM   14051 N N      . LYS B 2 450 ? 41.289  -11.610 -39.050 1.00 21.96  ?  450  LYS B N      1 
ATOM   14052 C CA     . LYS B 2 450 ? 42.580  -12.077 -39.550 1.00 23.19  ?  450  LYS B CA     1 
ATOM   14053 C C      . LYS B 2 450 ? 43.578  -12.219 -38.412 1.00 21.99  ?  450  LYS B C      1 
ATOM   14054 O O      . LYS B 2 450 ? 44.307  -13.218 -38.334 1.00 22.38  ?  450  LYS B O      1 
ATOM   14055 C CB     . LYS B 2 450 ? 43.123  -11.123 -40.614 1.00 25.58  ?  450  LYS B CB     1 
ATOM   14056 C CG     . LYS B 2 450 ? 44.468  -11.566 -41.188 1.00 26.60  ?  450  LYS B CG     1 
ATOM   14057 C CD     . LYS B 2 450 ? 44.946  -10.666 -42.324 1.00 29.99  ?  450  LYS B CD     1 
ATOM   14058 C CE     . LYS B 2 450 ? 46.414  -10.911 -42.713 1.00 33.65  ?  450  LYS B CE     1 
ATOM   14059 N NZ     . LYS B 2 450 ? 46.875  -12.325 -42.566 1.00 35.57  ?  450  LYS B NZ     1 
ATOM   14060 H H      . LYS B 2 450 ? 41.034  -10.855 -39.374 1.00 26.35  ?  450  LYS B H      1 
ATOM   14061 H HA     . LYS B 2 450 ? 42.456  -12.944 -39.967 1.00 27.83  ?  450  LYS B HA     1 
ATOM   14062 H HB2    . LYS B 2 450 ? 42.488  -11.075 -41.346 1.00 30.70  ?  450  LYS B HB2    1 
ATOM   14063 H HB3    . LYS B 2 450 ? 43.241  -10.246 -40.218 1.00 30.70  ?  450  LYS B HB3    1 
ATOM   14064 H HG2    . LYS B 2 450 ? 45.136  -11.542 -40.485 1.00 31.91  ?  450  LYS B HG2    1 
ATOM   14065 H HG3    . LYS B 2 450 ? 44.384  -12.468 -41.534 1.00 31.91  ?  450  LYS B HG3    1 
ATOM   14066 H HD2    . LYS B 2 450 ? 44.399  -10.831 -43.108 1.00 35.99  ?  450  LYS B HD2    1 
ATOM   14067 H HD3    . LYS B 2 450 ? 44.861  -9.739  -42.050 1.00 35.99  ?  450  LYS B HD3    1 
ATOM   14068 H HE2    . LYS B 2 450 ? 46.532  -10.661 -43.643 1.00 40.37  ?  450  LYS B HE2    1 
ATOM   14069 H HE3    . LYS B 2 450 ? 46.978  -10.361 -42.147 1.00 40.37  ?  450  LYS B HE3    1 
ATOM   14070 H HZ1    . LYS B 2 450 ? 47.672  -12.427 -42.948 1.00 42.68  ?  450  LYS B HZ1    1 
ATOM   14071 H HZ2    . LYS B 2 450 ? 46.939  -12.536 -41.703 1.00 42.68  ?  450  LYS B HZ2    1 
ATOM   14072 H HZ3    . LYS B 2 450 ? 46.295  -12.876 -42.956 1.00 42.68  ?  450  LYS B HZ3    1 
ATOM   14073 N N      . ARG B 2 451 ? 43.611  -11.240 -37.502 1.00 22.07  ?  451  ARG B N      1 
ATOM   14074 C CA     . ARG B 2 451 ? 44.545  -11.319 -36.385 1.00 24.23  ?  451  ARG B CA     1 
ATOM   14075 C C      . ARG B 2 451 ? 44.240  -12.539 -35.531 1.00 23.43  ?  451  ARG B C      1 
ATOM   14076 O O      . ARG B 2 451 ? 45.155  -13.239 -35.080 1.00 24.61  ?  451  ARG B O      1 
ATOM   14077 C CB     . ARG B 2 451 ? 44.472  -10.054 -35.536 1.00 26.26  ?  451  ARG B CB     1 
ATOM   14078 C CG     . ARG B 2 451 ? 45.054  -8.824  -36.229 1.00 29.55  ?  451  ARG B CG     1 
ATOM   14079 C CD     . ARG B 2 451 ? 45.396  -7.696  -35.273 1.00 33.16  ?  451  ARG B CD     1 
ATOM   14080 N NE     . ARG B 2 451 ? 44.229  -7.010  -34.717 1.00 35.83  ?  451  ARG B NE     1 
ATOM   14081 C CZ     . ARG B 2 451 ? 43.590  -6.000  -35.308 1.00 38.67  ?  451  ARG B CZ     1 
ATOM   14082 N NH1    . ARG B 2 451 ? 43.980  -5.557  -36.494 1.00 39.23  ?  451  ARG B NH1    1 
ATOM   14083 N NH2    . ARG B 2 451 ? 42.549  -5.440  -34.708 1.00 38.94  ?  451  ARG B NH2    1 
ATOM   14084 H H      . ARG B 2 451 ? 43.115  -10.537 -37.509 1.00 26.48  ?  451  ARG B H      1 
ATOM   14085 H HA     . ARG B 2 451 ? 45.448  -11.390 -36.732 1.00 29.07  ?  451  ARG B HA     1 
ATOM   14086 H HB2    . ARG B 2 451 ? 43.543  -9.868  -35.331 1.00 31.50  ?  451  ARG B HB2    1 
ATOM   14087 H HB3    . ARG B 2 451 ? 44.971  -10.197 -34.717 1.00 31.50  ?  451  ARG B HB3    1 
ATOM   14088 H HG2    . ARG B 2 451 ? 45.868  -9.080  -36.690 1.00 35.45  ?  451  ARG B HG2    1 
ATOM   14089 H HG3    . ARG B 2 451 ? 44.404  -8.487  -36.866 1.00 35.45  ?  451  ARG B HG3    1 
ATOM   14090 H HD2    . ARG B 2 451 ? 45.904  -8.060  -34.531 1.00 39.79  ?  451  ARG B HD2    1 
ATOM   14091 H HD3    . ARG B 2 451 ? 45.927  -7.037  -35.747 1.00 39.79  ?  451  ARG B HD3    1 
ATOM   14092 H HE     . ARG B 2 451 ? 43.935  -7.278  -33.955 1.00 43.00  ?  451  ARG B HE     1 
ATOM   14093 H HH11   . ARG B 2 451 ? 44.651  -5.921  -36.890 1.00 47.07  ?  451  ARG B HH11   1 
ATOM   14094 H HH12   . ARG B 2 451 ? 43.562  -4.905  -36.868 1.00 47.07  ?  451  ARG B HH12   1 
ATOM   14095 H HH21   . ARG B 2 451 ? 42.289  -5.728  -33.940 1.00 46.73  ?  451  ARG B HH21   1 
ATOM   14096 H HH22   . ARG B 2 451 ? 42.134  -4.788  -35.085 1.00 46.73  ?  451  ARG B HH22   1 
ATOM   14097 N N      . ALA B 2 452 ? 42.952  -12.826 -35.324 1.00 21.90  ?  452  ALA B N      1 
ATOM   14098 C CA     . ALA B 2 452 ? 42.563  -13.990 -34.542 1.00 20.87  ?  452  ALA B CA     1 
ATOM   14099 C C      . ALA B 2 452 ? 42.929  -15.286 -35.251 1.00 21.38  ?  452  ALA B C      1 
ATOM   14100 O O      . ALA B 2 452 ? 43.446  -16.219 -34.622 1.00 23.47  ?  452  ALA B O      1 
ATOM   14101 C CB     . ALA B 2 452 ? 41.063  -13.949 -34.278 1.00 20.85  ?  452  ALA B CB     1 
ATOM   14102 H H      . ALA B 2 452 ? 42.290  -12.364 -35.623 1.00 26.28  ?  452  ALA B H      1 
ATOM   14103 H HA     . ALA B 2 452 ? 43.036  -13.966 -33.695 1.00 25.04  ?  452  ALA B HA     1 
ATOM   14104 H HB1    . ALA B 2 452 ? 40.811  -14.732 -33.764 1.00 25.01  ?  452  ALA B HB1    1 
ATOM   14105 H HB2    . ALA B 2 452 ? 40.853  -13.144 -33.778 1.00 25.01  ?  452  ALA B HB2    1 
ATOM   14106 H HB3    . ALA B 2 452 ? 40.593  -13.944 -35.126 1.00 25.01  ?  452  ALA B HB3    1 
ATOM   14107 N N      . VAL B 2 453 ? 42.606  -15.386 -36.543 1.00 22.10  ?  453  VAL B N      1 
ATOM   14108 C CA     . VAL B 2 453 ? 42.927  -16.585 -37.310 1.00 22.09  ?  453  VAL B CA     1 
ATOM   14109 C C      . VAL B 2 453 ? 44.436  -16.813 -37.331 1.00 23.19  ?  453  VAL B C      1 
ATOM   14110 O O      . VAL B 2 453 ? 44.916  -17.932 -37.104 1.00 23.77  ?  453  VAL B O      1 
ATOM   14111 C CB     . VAL B 2 453 ? 42.323  -16.492 -38.725 1.00 19.66  ?  453  VAL B CB     1 
ATOM   14112 C CG1    . VAL B 2 453 ? 42.784  -17.643 -39.599 1.00 21.91  ?  453  VAL B CG1    1 
ATOM   14113 C CG2    . VAL B 2 453 ? 40.797  -16.492 -38.659 1.00 19.82  ?  453  VAL B CG2    1 
ATOM   14114 H H      . VAL B 2 453 ? 42.202  -14.776 -36.996 1.00 26.51  ?  453  VAL B H      1 
ATOM   14115 H HA     . VAL B 2 453 ? 42.527  -17.355 -36.876 1.00 26.50  ?  453  VAL B HA     1 
ATOM   14116 H HB     . VAL B 2 453 ? 42.627  -15.660 -39.122 1.00 23.59  ?  453  VAL B HB     1 
ATOM   14117 H HG11   . VAL B 2 453 ? 42.274  -17.637 -40.424 1.00 26.29  ?  453  VAL B HG11   1 
ATOM   14118 H HG12   . VAL B 2 453 ? 43.728  -17.534 -39.792 1.00 26.29  ?  453  VAL B HG12   1 
ATOM   14119 H HG13   . VAL B 2 453 ? 42.637  -18.477 -39.125 1.00 26.29  ?  453  VAL B HG13   1 
ATOM   14120 H HG21   . VAL B 2 453 ? 40.443  -16.385 -39.556 1.00 23.78  ?  453  VAL B HG21   1 
ATOM   14121 H HG22   . VAL B 2 453 ? 40.498  -17.335 -38.283 1.00 23.78  ?  453  VAL B HG22   1 
ATOM   14122 H HG23   . VAL B 2 453 ? 40.505  -15.757 -38.098 1.00 23.78  ?  453  VAL B HG23   1 
ATOM   14123 N N      . ASP B 2 454 ? 45.210  -15.748 -37.579 1.00 23.72  ?  454  ASP B N      1 
ATOM   14124 C CA     . ASP B 2 454 ? 46.665  -15.872 -37.620 1.00 23.75  ?  454  ASP B CA     1 
ATOM   14125 C C      . ASP B 2 454 ? 47.229  -16.337 -36.282 1.00 24.26  ?  454  ASP B C      1 
ATOM   14126 O O      . ASP B 2 454 ? 48.167  -17.137 -36.242 1.00 24.88  ?  454  ASP B O      1 
ATOM   14127 C CB     . ASP B 2 454 ? 47.282  -14.517 -37.983 1.00 26.85  ?  454  ASP B CB     1 
ATOM   14128 C CG     . ASP B 2 454 ? 47.113  -14.159 -39.450 1.00 29.76  ?  454  ASP B CG     1 
ATOM   14129 O OD1    . ASP B 2 454 ? 46.742  -15.039 -40.253 1.00 29.86  ?  454  ASP B OD1    1 
ATOM   14130 O OD2    . ASP B 2 454 ? 47.367  -12.982 -39.801 1.00 31.24  -1 454  ASP B OD2    1 
ATOM   14131 H H      . ASP B 2 454 ? 44.920  -14.952 -37.725 1.00 28.46  ?  454  ASP B H      1 
ATOM   14132 H HA     . ASP B 2 454 ? 46.898  -16.527 -38.296 1.00 28.50  ?  454  ASP B HA     1 
ATOM   14133 H HB2    . ASP B 2 454 ? 46.855  -13.824 -37.455 1.00 32.21  ?  454  ASP B HB2    1 
ATOM   14134 H HB3    . ASP B 2 454 ? 48.233  -14.542 -37.790 1.00 32.21  ?  454  ASP B HB3    1 
ATOM   14135 N N      . LYS B 2 455 ? 46.677  -15.836 -35.177 1.00 22.99  ?  455  LYS B N      1 
ATOM   14136 C CA     . LYS B 2 455 ? 47.156  -16.230 -33.855 1.00 25.17  ?  455  LYS B CA     1 
ATOM   14137 C C      . LYS B 2 455 ? 47.001  -17.730 -33.641 1.00 24.12  ?  455  LYS B C      1 
ATOM   14138 O O      . LYS B 2 455 ? 47.952  -18.417 -33.252 1.00 25.35  ?  455  LYS B O      1 
ATOM   14139 C CB     . LYS B 2 455 ? 46.386  -15.450 -32.793 1.00 30.36  ?  455  LYS B CB     1 
ATOM   14140 C CG     . LYS B 2 455 ? 46.807  -15.748 -31.372 1.00 35.40  ?  455  LYS B CG     1 
ATOM   14141 C CD     . LYS B 2 455 ? 46.006  -14.927 -30.353 1.00 40.64  ?  455  LYS B CD     1 
ATOM   14142 C CE     . LYS B 2 455 ? 46.258  -15.399 -28.929 1.00 45.18  ?  455  LYS B CE     1 
ATOM   14143 N NZ     . LYS B 2 455 ? 45.248  -14.867 -27.960 1.00 47.71  ?  455  LYS B NZ     1 
ATOM   14144 H H      . LYS B 2 455 ? 46.030  -15.271 -35.163 1.00 27.59  ?  455  LYS B H      1 
ATOM   14145 H HA     . LYS B 2 455 ? 48.099  -16.017 -33.776 1.00 30.20  ?  455  LYS B HA     1 
ATOM   14146 H HB2    . LYS B 2 455 ? 46.521  -14.502 -32.947 1.00 36.43  ?  455  LYS B HB2    1 
ATOM   14147 H HB3    . LYS B 2 455 ? 45.444  -15.668 -32.871 1.00 36.43  ?  455  LYS B HB3    1 
ATOM   14148 H HG2    . LYS B 2 455 ? 46.661  -16.689 -31.185 1.00 42.48  ?  455  LYS B HG2    1 
ATOM   14149 H HG3    . LYS B 2 455 ? 47.747  -15.530 -31.265 1.00 42.48  ?  455  LYS B HG3    1 
ATOM   14150 H HD2    . LYS B 2 455 ? 46.267  -13.995 -30.415 1.00 48.76  ?  455  LYS B HD2    1 
ATOM   14151 H HD3    . LYS B 2 455 ? 45.059  -15.019 -30.540 1.00 48.76  ?  455  LYS B HD3    1 
ATOM   14152 H HE2    . LYS B 2 455 ? 46.218  -16.367 -28.904 1.00 54.21  ?  455  LYS B HE2    1 
ATOM   14153 H HE3    . LYS B 2 455 ? 47.135  -15.096 -28.645 1.00 54.21  ?  455  LYS B HE3    1 
ATOM   14154 H HZ1    . LYS B 2 455 ? 45.431  -15.157 -27.139 1.00 57.25  ?  455  LYS B HZ1    1 
ATOM   14155 H HZ2    . LYS B 2 455 ? 45.263  -13.977 -27.962 1.00 57.25  ?  455  LYS B HZ2    1 
ATOM   14156 H HZ3    . LYS B 2 455 ? 44.433  -15.143 -28.189 1.00 57.25  ?  455  LYS B HZ3    1 
ATOM   14157 N N      . VAL B 2 456 ? 45.806  -18.262 -33.889 1.00 22.82  ?  456  VAL B N      1 
ATOM   14158 C CA     . VAL B 2 456 ? 45.609  -19.698 -33.727 1.00 23.83  ?  456  VAL B CA     1 
ATOM   14159 C C      . VAL B 2 456 ? 46.433  -20.479 -34.746 1.00 24.65  ?  456  VAL B C      1 
ATOM   14160 O O      . VAL B 2 456 ? 46.951  -21.562 -34.442 1.00 24.74  ?  456  VAL B O      1 
ATOM   14161 C CB     . VAL B 2 456 ? 44.110  -20.030 -33.790 1.00 21.86  ?  456  VAL B CB     1 
ATOM   14162 C CG1    . VAL B 2 456 ? 43.874  -21.521 -33.673 1.00 25.26  ?  456  VAL B CG1    1 
ATOM   14163 C CG2    . VAL B 2 456 ? 43.360  -19.289 -32.677 1.00 21.46  ?  456  VAL B CG2    1 
ATOM   14164 H H      . VAL B 2 456 ? 45.111  -17.826 -34.146 1.00 27.38  ?  456  VAL B H      1 
ATOM   14165 H HA     . VAL B 2 456 ? 45.930  -19.963 -32.850 1.00 28.59  ?  456  VAL B HA     1 
ATOM   14166 H HB     . VAL B 2 456 ? 43.767  -19.741 -34.650 1.00 26.23  ?  456  VAL B HB     1 
ATOM   14167 H HG11   . VAL B 2 456 ? 42.921  -21.685 -33.604 1.00 30.30  ?  456  VAL B HG11   1 
ATOM   14168 H HG12   . VAL B 2 456 ? 44.230  -21.960 -34.461 1.00 30.30  ?  456  VAL B HG12   1 
ATOM   14169 H HG13   . VAL B 2 456 ? 44.325  -21.850 -32.879 1.00 30.30  ?  456  VAL B HG13   1 
ATOM   14170 H HG21   . VAL B 2 456 ? 42.429  -19.561 -32.688 1.00 25.75  ?  456  VAL B HG21   1 
ATOM   14171 H HG22   . VAL B 2 456 ? 43.760  -19.514 -31.822 1.00 25.75  ?  456  VAL B HG22   1 
ATOM   14172 H HG23   . VAL B 2 456 ? 43.427  -18.334 -32.832 1.00 25.75  ?  456  VAL B HG23   1 
ATOM   14173 N N      . THR B 2 457 ? 46.580  -19.955 -35.966 1.00 24.67  ?  457  THR B N      1 
ATOM   14174 C CA     . THR B 2 457 ? 47.429  -20.634 -36.943 1.00 24.70  ?  457  THR B CA     1 
ATOM   14175 C C      . THR B 2 457 ? 48.847  -20.792 -36.410 1.00 26.35  ?  457  THR B C      1 
ATOM   14176 O O      . THR B 2 457 ? 49.448  -21.867 -36.519 1.00 26.07  ?  457  THR B O      1 
ATOM   14177 C CB     . THR B 2 457 ? 47.443  -19.876 -38.271 1.00 23.80  ?  457  THR B CB     1 
ATOM   14178 O OG1    . THR B 2 457 ? 46.125  -19.826 -38.798 1.00 25.31  ?  457  THR B OG1    1 
ATOM   14179 C CG2    . THR B 2 457 ? 48.347  -20.565 -39.283 1.00 26.29  ?  457  THR B CG2    1 
ATOM   14180 H H      . THR B 2 457 ? 46.212  -19.230 -36.245 1.00 29.61  ?  457  THR B H      1 
ATOM   14181 H HA     . THR B 2 457 ? 47.059  -21.514 -37.113 1.00 29.64  ?  457  THR B HA     1 
ATOM   14182 H HB     . THR B 2 457 ? 47.779  -18.978 -38.121 1.00 28.56  ?  457  THR B HB     1 
ATOM   14183 H HG1    . THR B 2 457 ? 45.633  -19.362 -38.299 1.00 30.36  ?  457  THR B HG1    1 
ATOM   14184 H HG21   . THR B 2 457 ? 48.216  -20.177 -40.162 1.00 31.55  ?  457  THR B HG21   1 
ATOM   14185 H HG22   . THR B 2 457 ? 49.276  -20.456 -39.026 1.00 31.55  ?  457  THR B HG22   1 
ATOM   14186 H HG23   . THR B 2 457 ? 48.139  -21.511 -39.322 1.00 31.55  ?  457  THR B HG23   1 
ATOM   14187 N N      . ASP B 2 458 ? 49.390  -19.737 -35.802 1.00 26.94  ?  458  ASP B N      1 
ATOM   14188 C CA     . ASP B 2 458 ? 50.743  -19.814 -35.265 1.00 27.95  ?  458  ASP B CA     1 
ATOM   14189 C C      . ASP B 2 458 ? 50.839  -20.836 -34.137 1.00 27.75  ?  458  ASP B C      1 
ATOM   14190 O O      . ASP B 2 458 ? 51.845  -21.546 -34.019 1.00 29.26  ?  458  ASP B O      1 
ATOM   14191 C CB     . ASP B 2 458 ? 51.191  -18.432 -34.783 1.00 30.85  ?  458  ASP B CB     1 
ATOM   14192 C CG     . ASP B 2 458 ? 51.412  -17.457 -35.930 1.00 34.50  ?  458  ASP B CG     1 
ATOM   14193 O OD1    . ASP B 2 458 ? 51.581  -17.907 -37.078 1.00 34.54  ?  458  ASP B OD1    1 
ATOM   14194 O OD2    . ASP B 2 458 ? 51.411  -16.237 -35.686 1.00 37.75  -1 458  ASP B OD2    1 
ATOM   14195 H H      . ASP B 2 458 ? 49.003  -18.977 -35.690 1.00 32.32  ?  458  ASP B H      1 
ATOM   14196 H HA     . ASP B 2 458 ? 51.344  -20.098 -35.971 1.00 33.53  ?  458  ASP B HA     1 
ATOM   14197 H HB2    . ASP B 2 458 ? 50.508  -18.063 -34.202 1.00 37.02  ?  458  ASP B HB2    1 
ATOM   14198 H HB3    . ASP B 2 458 ? 52.026  -18.521 -34.298 1.00 37.02  ?  458  ASP B HB3    1 
ATOM   14199 N N      . GLU B 2 459 ? 49.802  -20.924 -33.298 1.00 26.54  ?  459  GLU B N      1 
ATOM   14200 C CA     . GLU B 2 459 ? 49.796  -21.916 -32.231 1.00 26.62  ?  459  GLU B CA     1 
ATOM   14201 C C      . GLU B 2 459 ? 49.814  -23.324 -32.801 1.00 28.74  ?  459  GLU B C      1 
ATOM   14202 O O      . GLU B 2 459 ? 50.558  -24.193 -32.324 1.00 29.82  ?  459  GLU B O      1 
ATOM   14203 C CB     . GLU B 2 459 ? 48.554  -21.732 -31.358 1.00 25.43  ?  459  GLU B CB     1 
ATOM   14204 C CG     . GLU B 2 459 ? 48.564  -20.437 -30.558 1.00 25.70  ?  459  GLU B CG     1 
ATOM   14205 C CD     . GLU B 2 459 ? 47.302  -20.249 -29.741 1.00 29.25  ?  459  GLU B CD     1 
ATOM   14206 O OE1    . GLU B 2 459 ? 46.302  -20.955 -29.999 1.00 26.74  ?  459  GLU B OE1    1 
ATOM   14207 O OE2    . GLU B 2 459 ? 47.323  -19.386 -28.843 1.00 33.71  -1 459  GLU B OE2    1 
ATOM   14208 H H      . GLU B 2 459 ? 49.101  -20.427 -33.325 1.00 31.84  ?  459  GLU B H      1 
ATOM   14209 H HA     . GLU B 2 459 ? 50.586  -21.788 -31.684 1.00 31.94  ?  459  GLU B HA     1 
ATOM   14210 H HB2    . GLU B 2 459 ? 47.769  -21.724 -31.928 1.00 30.51  ?  459  GLU B HB2    1 
ATOM   14211 H HB3    . GLU B 2 459 ? 48.501  -22.469 -30.731 1.00 30.51  ?  459  GLU B HB3    1 
ATOM   14212 H HG2    . GLU B 2 459 ? 49.318  -20.447 -29.948 1.00 30.83  ?  459  GLU B HG2    1 
ATOM   14213 H HG3    . GLU B 2 459 ? 48.641  -19.688 -31.169 1.00 30.83  ?  459  GLU B HG3    1 
ATOM   14214 N N      . LEU B 2 460 ? 48.980  -23.573 -33.815 1.00 27.55  ?  460  LEU B N      1 
ATOM   14215 C CA     . LEU B 2 460 ? 48.869  -24.914 -34.372 1.00 28.10  ?  460  LEU B CA     1 
ATOM   14216 C C      . LEU B 2 460 ? 50.086  -25.269 -35.205 1.00 30.28  ?  460  LEU B C      1 
ATOM   14217 O O      . LEU B 2 460 ? 50.462  -26.446 -35.285 1.00 30.24  ?  460  LEU B O      1 
ATOM   14218 C CB     . LEU B 2 460 ? 47.607  -25.000 -35.218 1.00 27.26  ?  460  LEU B CB     1 
ATOM   14219 C CG     . LEU B 2 460 ? 46.272  -24.799 -34.498 1.00 26.82  ?  460  LEU B CG     1 
ATOM   14220 C CD1    . LEU B 2 460 ? 45.173  -24.601 -35.529 1.00 26.73  ?  460  LEU B CD1    1 
ATOM   14221 C CD2    . LEU B 2 460 ? 45.952  -25.997 -33.633 1.00 30.15  ?  460  LEU B CD2    1 
ATOM   14222 H H      . LEU B 2 460 ? 48.474  -22.989 -34.193 1.00 33.06  ?  460  LEU B H      1 
ATOM   14223 H HA     . LEU B 2 460 ? 48.803  -25.560 -33.652 1.00 33.72  ?  460  LEU B HA     1 
ATOM   14224 H HB2    . LEU B 2 460 ? 47.663  -24.318 -35.906 1.00 32.71  ?  460  LEU B HB2    1 
ATOM   14225 H HB3    . LEU B 2 460 ? 47.580  -25.880 -35.624 1.00 32.71  ?  460  LEU B HB3    1 
ATOM   14226 H HG     . LEU B 2 460 ? 46.324  -24.017 -33.925 1.00 32.19  ?  460  LEU B HG     1 
ATOM   14227 H HD11   . LEU B 2 460 ? 44.322  -24.516 -35.071 1.00 32.08  ?  460  LEU B HD11   1 
ATOM   14228 H HD12   . LEU B 2 460 ? 45.357  -23.795 -36.036 1.00 32.08  ?  460  LEU B HD12   1 
ATOM   14229 H HD13   . LEU B 2 460 ? 45.154  -25.369 -36.122 1.00 32.08  ?  460  LEU B HD13   1 
ATOM   14230 H HD21   . LEU B 2 460 ? 45.105  -25.846 -33.186 1.00 36.17  ?  460  LEU B HD21   1 
ATOM   14231 H HD22   . LEU B 2 460 ? 45.894  -26.785 -34.195 1.00 36.17  ?  460  LEU B HD22   1 
ATOM   14232 H HD23   . LEU B 2 460 ? 46.657  -26.110 -32.977 1.00 36.17  ?  460  LEU B HD23   1 
ATOM   14233 N N      . THR B 2 461 ? 50.698  -24.281 -35.855 1.00 31.68  ?  461  THR B N      1 
ATOM   14234 C CA     . THR B 2 461 ? 51.951  -24.542 -36.556 1.00 32.31  ?  461  THR B CA     1 
ATOM   14235 C C      . THR B 2 461 ? 53.025  -24.967 -35.567 1.00 33.84  ?  461  THR B C      1 
ATOM   14236 O O      . THR B 2 461 ? 53.754  -25.942 -35.792 1.00 34.69  ?  461  THR B O      1 
ATOM   14237 C CB     . THR B 2 461 ? 52.383  -23.299 -37.336 1.00 32.82  ?  461  THR B CB     1 
ATOM   14238 O OG1    . THR B 2 461 ? 51.416  -23.026 -38.363 1.00 33.98  ?  461  THR B OG1    1 
ATOM   14239 C CG2    . THR B 2 461 ? 53.759  -23.506 -37.956 1.00 34.04  ?  461  THR B CG2    1 
ATOM   14240 H H      . THR B 2 461 ? 50.417  -23.470 -35.906 1.00 38.02  ?  461  THR B H      1 
ATOM   14241 H HA     . THR B 2 461 ? 51.823  -25.259 -37.197 1.00 38.76  ?  461  THR B HA     1 
ATOM   14242 H HB     . THR B 2 461 ? 52.439  -22.538 -36.738 1.00 39.39  ?  461  THR B HB     1 
ATOM   14243 H HG1    . THR B 2 461 ? 50.664  -22.879 -38.019 1.00 40.78  ?  461  THR B HG1    1 
ATOM   14244 H HG21   . THR B 2 461 ? 53.914  -22.844 -38.649 1.00 40.85  ?  461  THR B HG21   1 
ATOM   14245 H HG22   . THR B 2 461 ? 54.446  -23.416 -37.277 1.00 40.85  ?  461  THR B HG22   1 
ATOM   14246 H HG23   . THR B 2 461 ? 53.818  -24.391 -38.348 1.00 40.85  ?  461  THR B HG23   1 
ATOM   14247 N N      . ARG B 2 462 ? 53.121  -24.250 -34.443 1.00 32.87  ?  462  ARG B N      1 
ATOM   14248 C CA     . ARG B 2 462 ? 54.135  -24.568 -33.446 1.00 34.12  ?  462  ARG B CA     1 
ATOM   14249 C C      . ARG B 2 462 ? 53.892  -25.938 -32.831 1.00 36.42  ?  462  ARG B C      1 
ATOM   14250 O O      . ARG B 2 462 ? 54.841  -26.709 -32.624 1.00 38.70  ?  462  ARG B O      1 
ATOM   14251 C CB     . ARG B 2 462 ? 54.145  -23.480 -32.367 1.00 34.06  ?  462  ARG B CB     1 
ATOM   14252 C CG     . ARG B 2 462 ? 55.110  -23.725 -31.232 1.00 34.02  ?  462  ARG B CG     1 
ATOM   14253 C CD     . ARG B 2 462 ? 55.221  -22.474 -30.348 1.00 35.13  ?  462  ARG B CD     1 
ATOM   14254 N NE     . ARG B 2 462 ? 53.896  -21.978 -30.017 1.00 38.34  ?  462  ARG B NE     1 
ATOM   14255 C CZ     . ARG B 2 462 ? 53.578  -20.697 -29.871 1.00 38.27  ?  462  ARG B CZ     1 
ATOM   14256 N NH1    . ARG B 2 462 ? 54.495  -19.748 -30.011 1.00 37.96  ?  462  ARG B NH1    1 
ATOM   14257 N NH2    . ARG B 2 462 ? 52.326  -20.373 -29.581 1.00 38.65  ?  462  ARG B NH2    1 
ATOM   14258 H H      . ARG B 2 462 ? 52.618  -23.583 -34.238 1.00 39.44  ?  462  ARG B H      1 
ATOM   14259 H HA     . ARG B 2 462 ? 55.008  -24.587 -33.869 1.00 40.94  ?  462  ARG B HA     1 
ATOM   14260 H HB2    . ARG B 2 462 ? 54.390  -22.638 -32.782 1.00 40.87  ?  462  ARG B HB2    1 
ATOM   14261 H HB3    . ARG B 2 462 ? 53.256  -23.416 -31.986 1.00 40.87  ?  462  ARG B HB3    1 
ATOM   14262 H HG2    . ARG B 2 462 ? 54.793  -24.463 -30.688 1.00 40.82  ?  462  ARG B HG2    1 
ATOM   14263 H HG3    . ARG B 2 462 ? 55.988  -23.931 -31.590 1.00 40.82  ?  462  ARG B HG3    1 
ATOM   14264 H HD2    . ARG B 2 462 ? 55.685  -22.696 -29.525 1.00 42.15  ?  462  ARG B HD2    1 
ATOM   14265 H HD3    . ARG B 2 462 ? 55.704  -21.780 -30.824 1.00 42.15  ?  462  ARG B HD3    1 
ATOM   14266 H HE     . ARG B 2 462 ? 53.270  -22.558 -29.908 1.00 46.01  ?  462  ARG B HE     1 
ATOM   14267 H HH11   . ARG B 2 462 ? 55.307  -19.959 -30.199 1.00 45.55  ?  462  ARG B HH11   1 
ATOM   14268 H HH12   . ARG B 2 462 ? 54.277  -18.922 -29.914 1.00 45.55  ?  462  ARG B HH12   1 
ATOM   14269 H HH21   . ARG B 2 462 ? 51.733  -20.988 -29.490 1.00 46.37  ?  462  ARG B HH21   1 
ATOM   14270 H HH22   . ARG B 2 462 ? 52.108  -19.547 -29.483 1.00 46.37  ?  462  ARG B HH22   1 
ATOM   14271 N N      . SER B 2 463 ? 52.635  -26.264 -32.534 1.00 37.07  ?  463  SER B N      1 
ATOM   14272 C CA     . SER B 2 463 ? 52.329  -27.528 -31.878 1.00 38.16  ?  463  SER B CA     1 
ATOM   14273 C C      . SER B 2 463 ? 52.329  -28.707 -32.842 1.00 39.86  ?  463  SER B C      1 
ATOM   14274 O O      . SER B 2 463 ? 52.221  -29.851 -32.386 1.00 40.88  ?  463  SER B O      1 
ATOM   14275 C CB     . SER B 2 463 ? 50.989  -27.458 -31.139 1.00 37.50  ?  463  SER B CB     1 
ATOM   14276 O OG     . SER B 2 463 ? 49.886  -27.326 -32.033 1.00 38.83  ?  463  SER B OG     1 
ATOM   14277 H H      . SER B 2 463 ? 51.949  -25.774 -32.702 1.00 44.48  ?  463  SER B H      1 
ATOM   14278 H HA     . SER B 2 463 ? 53.009  -27.690 -31.205 1.00 45.78  ?  463  SER B HA     1 
ATOM   14279 H HB2    . SER B 2 463 ? 50.875  -28.272 -30.624 1.00 45.00  ?  463  SER B HB2    1 
ATOM   14280 H HB3    . SER B 2 463 ? 51.001  -26.690 -30.547 1.00 45.00  ?  463  SER B HB3    1 
ATOM   14281 H HG     . SER B 2 463 ? 49.810  -28.021 -32.499 1.00 46.60  ?  463  SER B HG     1 
ATOM   14282 N N      . GLY B 2 464 ? 52.463  -28.460 -34.145 1.00 39.35  ?  464  GLY B N      1 
ATOM   14283 C CA     . GLY B 2 464 ? 52.500  -29.529 -35.122 1.00 39.43  ?  464  GLY B CA     1 
ATOM   14284 C C      . GLY B 2 464 ? 51.150  -30.087 -35.503 1.00 42.73  ?  464  GLY B C      1 
ATOM   14285 O O      . GLY B 2 464 ? 51.084  -31.190 -36.059 1.00 43.44  ?  464  GLY B O      1 
ATOM   14286 H H      . GLY B 2 464 ? 52.535  -27.674 -34.487 1.00 47.22  ?  464  GLY B H      1 
ATOM   14287 H HA2    . GLY B 2 464 ? 52.922  -29.197 -35.929 1.00 47.32  ?  464  GLY B HA2    1 
ATOM   14288 H HA3    . GLY B 2 464 ? 53.031  -30.258 -34.764 1.00 47.32  ?  464  GLY B HA3    1 
ATOM   14289 N N      . ASP B 2 465 ? 50.068  -29.366 -35.214 1.00 42.11  ?  465  ASP B N      1 
ATOM   14290 C CA     . ASP B 2 465 ? 48.721  -29.804 -35.546 1.00 42.90  ?  465  ASP B CA     1 
ATOM   14291 C C      . ASP B 2 465 ? 48.278  -29.352 -36.932 1.00 44.49  ?  465  ASP B C      1 
ATOM   14292 O O      . ASP B 2 465 ? 47.157  -29.671 -37.336 1.00 44.46  ?  465  ASP B O      1 
ATOM   14293 C CB     . ASP B 2 465 ? 47.736  -29.306 -34.488 1.00 42.29  ?  465  ASP B CB     1 
ATOM   14294 C CG     . ASP B 2 465 ? 47.934  -29.981 -33.143 1.00 42.68  ?  465  ASP B CG     1 
ATOM   14295 O OD1    . ASP B 2 465 ? 47.955  -31.228 -33.100 1.00 43.61  ?  465  ASP B OD1    1 
ATOM   14296 O OD2    . ASP B 2 465 ? 48.069  -29.273 -32.123 1.00 42.86  -1 465  ASP B OD2    1 
ATOM   14297 H H      . ASP B 2 465 ? 50.094  -28.603 -34.817 1.00 50.53  ?  465  ASP B H      1 
ATOM   14298 H HA     . ASP B 2 465 ? 48.695  -30.774 -35.537 1.00 51.48  ?  465  ASP B HA     1 
ATOM   14299 H HB2    . ASP B 2 465 ? 47.857  -28.352 -34.366 1.00 50.75  ?  465  ASP B HB2    1 
ATOM   14300 H HB3    . ASP B 2 465 ? 46.831  -29.490 -34.786 1.00 50.75  ?  465  ASP B HB3    1 
ATOM   14301 N N      . LEU B 2 466 ? 49.121  -28.626 -37.664 1.00 46.95  ?  466  LEU B N      1 
ATOM   14302 C CA     . LEU B 2 466 ? 48.843  -28.320 -39.062 1.00 49.31  ?  466  LEU B CA     1 
ATOM   14303 C C      . LEU B 2 466 ? 49.572  -29.303 -39.983 1.00 52.09  ?  466  LEU B C      1 
ATOM   14304 O O      . LEU B 2 466 ? 49.412  -29.258 -41.203 1.00 53.15  ?  466  LEU B O      1 
ATOM   14305 C CB     . LEU B 2 466 ? 49.261  -26.898 -39.415 1.00 49.62  ?  466  LEU B CB     1 
ATOM   14306 C CG     . LEU B 2 466 ? 48.397  -25.767 -38.865 1.00 49.02  ?  466  LEU B CG     1 
ATOM   14307 C CD1    . LEU B 2 466 ? 48.653  -24.470 -39.631 1.00 49.39  ?  466  LEU B CD1    1 
ATOM   14308 C CD2    . LEU B 2 466 ? 46.917  -26.111 -38.907 1.00 49.83  ?  466  LEU B CD2    1 
ATOM   14309 H H      . LEU B 2 466 ? 49.862  -28.300 -37.372 1.00 56.33  ?  466  LEU B H      1 
ATOM   14310 H HA     . LEU B 2 466 ? 47.887  -28.394 -39.207 1.00 59.17  ?  466  LEU B HA     1 
ATOM   14311 H HB2    . LEU B 2 466 ? 50.159  -26.758 -39.077 1.00 59.54  ?  466  LEU B HB2    1 
ATOM   14312 H HB3    . LEU B 2 466 ? 49.254  -26.815 -40.381 1.00 59.54  ?  466  LEU B HB3    1 
ATOM   14313 H HG     . LEU B 2 466 ? 48.640  -25.635 -37.935 1.00 58.82  ?  466  LEU B HG     1 
ATOM   14314 H HD11   . LEU B 2 466 ? 48.083  -23.773 -39.271 1.00 59.27  ?  466  LEU B HD11   1 
ATOM   14315 H HD12   . LEU B 2 466 ? 49.585  -24.221 -39.529 1.00 59.27  ?  466  LEU B HD12   1 
ATOM   14316 H HD13   . LEU B 2 466 ? 48.449  -24.613 -40.569 1.00 59.27  ?  466  LEU B HD13   1 
ATOM   14317 H HD21   . LEU B 2 466 ? 46.400  -25.303 -38.765 1.00 59.80  ?  466  LEU B HD21   1 
ATOM   14318 H HD22   . LEU B 2 466 ? 46.706  -26.490 -39.775 1.00 59.80  ?  466  LEU B HD22   1 
ATOM   14319 H HD23   . LEU B 2 466 ? 46.722  -26.756 -38.209 1.00 59.80  ?  466  LEU B HD23   1 
HETATM 14320 C C1     . GOL C 3 .   ? -13.891 -29.248 -6.838  1.00 39.59  ?  501  GOL A C1     1 
HETATM 14321 O O1     . GOL C 3 .   ? -13.966 -30.119 -5.727  1.00 40.57  ?  501  GOL A O1     1 
HETATM 14322 C C2     . GOL C 3 .   ? -14.506 -27.892 -6.412  1.00 41.28  ?  501  GOL A C2     1 
HETATM 14323 O O2     . GOL C 3 .   ? -13.822 -27.311 -5.334  1.00 40.71  ?  501  GOL A O2     1 
HETATM 14324 C C3     . GOL C 3 .   ? -15.990 -28.115 -6.061  1.00 42.46  ?  501  GOL A C3     1 
HETATM 14325 O O3     . GOL C 3 .   ? -16.328 -29.445 -6.363  1.00 41.92  ?  501  GOL A O3     1 
HETATM 14326 H H11    . GOL C 3 .   ? -14.372 -29.587 -7.609  1.00 47.50  ?  501  GOL A H11    1 
HETATM 14327 H H12    . GOL C 3 .   ? -12.979 -29.104 -7.136  1.00 47.50  ?  501  GOL A H12    1 
HETATM 14328 H HO1    . GOL C 3 .   ? -14.741 -30.466 -5.745  1.00 48.69  ?  501  GOL A HO1    1 
HETATM 14329 H H2     . GOL C 3 .   ? -14.436 -27.291 -7.170  1.00 49.54  ?  501  GOL A H2     1 
HETATM 14330 H HO2    . GOL C 3 .   ? -13.411 -27.930 -4.922  1.00 48.85  ?  501  GOL A HO2    1 
HETATM 14331 H H31    . GOL C 3 .   ? -16.520 -27.468 -6.552  1.00 50.95  ?  501  GOL A H31    1 
HETATM 14332 H H32    . GOL C 3 .   ? -16.119 -27.894 -5.125  1.00 50.95  ?  501  GOL A H32    1 
HETATM 14333 H HO3    . GOL C 3 .   ? -17.082 -29.422 -6.756  1.00 50.30  ?  501  GOL A HO3    1 
HETATM 14334 C C1     . GOL D 3 .   ? 12.835  -29.743 -3.980  1.00 56.12  ?  502  GOL A C1     1 
HETATM 14335 O O1     . GOL D 3 .   ? 12.073  -30.892 -3.698  1.00 59.16  ?  502  GOL A O1     1 
HETATM 14336 C C2     . GOL D 3 .   ? 13.960  -30.183 -4.895  1.00 52.53  ?  502  GOL A C2     1 
HETATM 14337 O O2     . GOL D 3 .   ? 15.032  -30.698 -4.221  1.00 51.19  ?  502  GOL A O2     1 
HETATM 14338 C C3     . GOL D 3 .   ? 13.338  -31.233 -5.805  1.00 50.34  ?  502  GOL A C3     1 
HETATM 14339 O O3     . GOL D 3 .   ? 12.684  -32.134 -5.004  1.00 50.60  ?  502  GOL A O3     1 
HETATM 14340 H H11    . GOL D 3 .   ? 13.209  -29.336 -3.183  1.00 67.34  ?  502  GOL A H11    1 
HETATM 14341 H H12    . GOL D 3 .   ? 12.318  -29.049 -4.416  1.00 67.34  ?  502  GOL A H12    1 
HETATM 14342 H HO1    . GOL D 3 .   ? 12.543  -31.371 -3.176  1.00 70.99  ?  502  GOL A HO1    1 
HETATM 14343 H H2     . GOL D 3 .   ? 14.292  -29.416 -5.387  1.00 63.03  ?  502  GOL A H2     1 
HETATM 14344 H HO2    . GOL D 3 .   ? 15.044  -31.538 -4.351  1.00 61.43  ?  502  GOL A HO2    1 
HETATM 14345 H H31    . GOL D 3 .   ? 14.038  -31.635 -6.341  1.00 60.41  ?  502  GOL A H31    1 
HETATM 14346 H H32    . GOL D 3 .   ? 12.753  -30.789 -6.438  1.00 60.41  ?  502  GOL A H32    1 
HETATM 14347 C C1     . GOL E 3 .   ? 31.057  -15.260 -21.809 1.00 42.59  ?  503  GOL A C1     1 
HETATM 14348 O O1     . GOL E 3 .   ? 30.919  -16.654 -22.079 1.00 38.87  ?  503  GOL A O1     1 
HETATM 14349 C C2     . GOL E 3 .   ? 32.116  -14.688 -22.791 1.00 44.24  ?  503  GOL A C2     1 
HETATM 14350 O O2     . GOL E 3 .   ? 31.871  -13.374 -23.225 1.00 41.33  ?  503  GOL A O2     1 
HETATM 14351 C C3     . GOL E 3 .   ? 33.396  -14.767 -21.972 1.00 47.20  ?  503  GOL A C3     1 
HETATM 14352 O O3     . GOL E 3 .   ? 34.452  -14.456 -22.838 1.00 48.10  ?  503  GOL A O3     1 
HETATM 14353 H H11    . GOL E 3 .   ? 31.341  -15.085 -20.899 1.00 51.11  ?  503  GOL A H11    1 
HETATM 14354 H H12    . GOL E 3 .   ? 30.224  -14.776 -21.925 1.00 51.11  ?  503  GOL A H12    1 
HETATM 14355 H HO1    . GOL E 3 .   ? 30.104  -16.850 -21.934 1.00 46.64  ?  503  GOL A HO1    1 
HETATM 14356 H H2     . GOL E 3 .   ? 32.129  -15.211 -23.608 1.00 53.09  ?  503  GOL A H2     1 
HETATM 14357 H HO2    . GOL E 3 .   ? 31.092  -13.154 -22.965 1.00 49.60  ?  503  GOL A HO2    1 
HETATM 14358 H H31    . GOL E 3 .   ? 33.466  -15.653 -21.583 1.00 56.63  ?  503  GOL A H31    1 
HETATM 14359 H H32    . GOL E 3 .   ? 33.325  -14.161 -21.218 1.00 56.63  ?  503  GOL A H32    1 
HETATM 14360 H HO3    . GOL E 3 .   ? 34.518  -15.102 -23.386 1.00 57.71  ?  503  GOL A HO3    1 
HETATM 14361 C C1     . GOL F 3 .   ? 8.064   -53.876 -16.529 1.00 38.96  ?  504  GOL A C1     1 
HETATM 14362 O O1     . GOL F 3 .   ? 6.939   -53.338 -17.140 1.00 111.25 ?  504  GOL A O1     1 
HETATM 14363 C C2     . GOL F 3 .   ? 7.675   -54.529 -15.175 1.00 72.00  ?  504  GOL A C2     1 
HETATM 14364 O O2     . GOL F 3 .   ? 7.722   -53.632 -14.105 1.00 45.56  ?  504  GOL A O2     1 
HETATM 14365 C C3     . GOL F 3 .   ? 6.280   -55.138 -15.413 1.00 97.52  ?  504  GOL A C3     1 
HETATM 14366 O O3     . GOL F 3 .   ? 5.351   -54.092 -15.379 1.00 50.75  ?  504  GOL A O3     1 
HETATM 14367 H H11    . GOL F 3 .   ? 8.490   -54.548 -17.082 1.00 46.74  ?  504  GOL A H11    1 
HETATM 14368 H H12    . GOL F 3 .   ? 8.741   -53.202 -16.360 1.00 46.74  ?  504  GOL A H12    1 
HETATM 14369 H HO1    . GOL F 3 .   ? 6.975   -53.568 -17.957 1.00 133.49 ?  504  GOL A HO1    1 
HETATM 14370 H H2     . GOL F 3 .   ? 8.310   -55.223 -14.937 1.00 86.40  ?  504  GOL A H2     1 
HETATM 14371 H HO2    . GOL F 3 .   ? 8.083   -52.913 -14.382 1.00 54.67  ?  504  GOL A HO2    1 
HETATM 14372 H H31    . GOL F 3 .   ? 6.289   -55.614 -16.258 1.00 117.03 ?  504  GOL A H31    1 
HETATM 14373 H H32    . GOL F 3 .   ? 6.118   -55.816 -14.738 1.00 117.03 ?  504  GOL A H32    1 
HETATM 14374 H HO3    . GOL F 3 .   ? 4.955   -54.091 -16.131 1.00 60.90  ?  504  GOL A HO3    1 
HETATM 14375 C C1     A GOL G 3 .   ? 30.080  -23.367 -50.643 0.50 50.86  ?  501  GOL B C1     1 
HETATM 14376 C C1     B GOL G 3 .   ? 30.252  -23.295 -50.891 0.50 51.12  ?  501  GOL B C1     1 
HETATM 14377 O O1     A GOL G 3 .   ? 30.541  -24.553 -51.238 0.50 43.63  ?  501  GOL B O1     1 
HETATM 14378 O O1     B GOL G 3 .   ? 30.667  -24.605 -51.247 0.50 40.95  ?  501  GOL B O1     1 
HETATM 14379 C C2     A GOL G 3 .   ? 28.948  -22.809 -51.517 0.50 52.09  ?  501  GOL B C2     1 
HETATM 14380 C C2     B GOL G 3 .   ? 28.986  -22.979 -51.643 0.50 53.02  ?  501  GOL B C2     1 
HETATM 14381 O O2     A GOL G 3 .   ? 28.438  -21.621 -50.969 0.50 65.07  ?  501  GOL B O2     1 
HETATM 14382 O O2     B GOL G 3 .   ? 28.388  -21.883 -50.972 0.50 65.14  ?  501  GOL B O2     1 
HETATM 14383 C C3     A GOL G 3 .   ? 27.837  -23.879 -51.597 0.50 37.82  ?  501  GOL B C3     1 
HETATM 14384 C C3     B GOL G 3 .   ? 28.076  -24.187 -51.674 0.50 32.17  ?  501  GOL B C3     1 
HETATM 14385 O O3     A GOL G 3 .   ? 28.407  -25.033 -52.116 0.50 41.54  ?  501  GOL B O3     1 
HETATM 14386 O O3     B GOL G 3 .   ? 27.700  -24.364 -50.312 0.50 41.36  ?  501  GOL B O3     1 
HETATM 14387 H H11    A GOL G 3 .   ? 30.777  -22.698 -50.562 0.50 61.03  ?  501  GOL B H11    1 
HETATM 14388 H H11    B GOL G 3 .   ? 31.030  -22.573 -51.149 0.50 61.34  ?  501  GOL B H11    1 
HETATM 14389 H H12    A GOL G 3 .   ? 29.744  -23.511 -49.744 0.50 61.03  ?  501  GOL B H12    1 
HETATM 14390 H H12    B GOL G 3 .   ? 30.072  -23.239 -49.815 0.50 61.34  ?  501  GOL B H12    1 
HETATM 14391 H HO1    A GOL G 3 .   ? 31.228  -24.793 -50.799 0.50 52.36  ?  501  GOL B HO1    1 
HETATM 14392 H HO1    B GOL G 3 .   ? 31.296  -24.933 -50.590 0.50 49.14  ?  501  GOL B HO1    1 
HETATM 14393 H H2     A GOL G 3 .   ? 29.297  -22.627 -52.403 0.50 62.51  ?  501  GOL B H2     1 
HETATM 14394 H H2     B GOL G 3 .   ? 29.243  -22.697 -52.674 0.50 63.62  ?  501  GOL B H2     1 
HETATM 14395 H HO2    A GOL G 3 .   ? 27.790  -21.826 -50.458 0.50 78.08  ?  501  GOL B HO2    1 
HETATM 14396 H HO2    B GOL G 3 .   ? 28.252  -22.110 -50.042 0.50 78.16  ?  501  GOL B HO2    1 
HETATM 14397 H H31    A GOL G 3 .   ? 27.460  -24.002 -50.712 0.50 45.38  ?  501  GOL B H31    1 
HETATM 14398 H H31    B GOL G 3 .   ? 27.200  -23.997 -52.298 0.50 38.60  ?  501  GOL B H31    1 
HETATM 14399 H H32    A GOL G 3 .   ? 27.111  -23.533 -52.140 0.50 45.38  ?  501  GOL B H32    1 
HETATM 14400 H H32    B GOL G 3 .   ? 28.606  -25.064 -52.050 0.50 38.60  ?  501  GOL B H32    1 
HETATM 14401 H HO3    A GOL G 3 .   ? 27.897  -25.296 -52.743 0.50 49.84  ?  501  GOL B HO3    1 
HETATM 14402 H HO3    B GOL G 3 .   ? 28.466  -24.662 -49.803 0.50 49.62  ?  501  GOL B HO3    1 
HETATM 14403 N N1     . PLP H 4 .   ? 14.812  -21.628 -37.345 1.00 16.73  ?  502  PLP B N1     1 
HETATM 14404 C C2     . PLP H 4 .   ? 15.946  -21.085 -37.674 1.00 21.39  ?  502  PLP B C2     1 
HETATM 14405 C C2A    . PLP H 4 .   ? 16.452  -21.194 -39.053 1.00 24.94  ?  502  PLP B C2A    1 
HETATM 14406 C C3     . PLP H 4 .   ? 16.678  -20.387 -36.730 1.00 20.02  ?  502  PLP B C3     1 
HETATM 14407 O O3     . PLP H 4 .   ? 17.828  -19.842 -37.040 1.00 23.03  ?  502  PLP B O3     1 
HETATM 14408 C C4     . PLP H 4 .   ? 16.201  -20.277 -35.449 1.00 17.72  ?  502  PLP B C4     1 
HETATM 14409 C C4A    . PLP H 4 .   ? 16.971  -19.485 -34.482 1.00 50.74  ?  502  PLP B C4A    1 
HETATM 14410 C C5     . PLP H 4 .   ? 15.004  -20.839 -35.084 1.00 20.05  ?  502  PLP B C5     1 
HETATM 14411 C C6     . PLP H 4 .   ? 14.325  -21.550 -36.077 1.00 22.48  ?  502  PLP B C6     1 
HETATM 14412 C C5A    . PLP H 4 .   ? 14.468  -20.720 -33.677 1.00 21.93  ?  502  PLP B C5A    1 
HETATM 14413 O O4P    . PLP H 4 .   ? 14.341  -19.408 -33.368 1.00 17.47  ?  502  PLP B O4P    1 
HETATM 14414 P P      . PLP H 4 .   ? 14.013  -19.434 -31.705 1.00 22.11  ?  502  PLP B P      1 
HETATM 14415 O O1P    . PLP H 4 .   ? 15.416  -19.421 -31.185 1.00 21.30  ?  502  PLP B O1P    1 
HETATM 14416 O O2P    . PLP H 4 .   ? 13.483  -17.860 -31.511 1.00 21.32  ?  502  PLP B O2P    1 
HETATM 14417 O O3P    . PLP H 4 .   ? 13.506  -20.175 -30.429 1.00 24.45  ?  502  PLP B O3P    1 
HETATM 14418 H H2A1   . PLP H 4 .   ? 15.873  -21.735 -39.556 1.00 29.93  ?  502  PLP B H2A1   1 
HETATM 14419 H H2A2   . PLP H 4 .   ? 17.309  -21.578 -39.042 1.00 29.93  ?  502  PLP B H2A2   1 
HETATM 14420 H H2A3   . PLP H 4 .   ? 16.496  -20.339 -39.439 1.00 29.93  ?  502  PLP B H2A3   1 
HETATM 14421 H HO3    . PLP H 4 .   ? 18.057  -19.779 -37.838 1.00 27.63  ?  502  PLP B HO3    1 
HETATM 14422 H H4A    . PLP H 4 .   ? 17.810  -19.636 -34.404 1.00 60.89  ?  502  PLP B H4A    1 
HETATM 14423 H H6     . PLP H 4 .   ? 13.507  -21.943 -35.879 1.00 26.97  ?  502  PLP B H6     1 
HETATM 14424 H H5A1   . PLP H 4 .   ? 15.061  -21.131 -33.076 1.00 26.32  ?  502  PLP B H5A1   1 
HETATM 14425 H H5A2   . PLP H 4 .   ? 13.642  -21.160 -33.598 1.00 26.32  ?  502  PLP B H5A2   1 
HETATM 14426 O O      . HOH I 5 .   ? 6.575   -52.428 -18.963 1.00 47.66  ?  601  HOH A O      1 
HETATM 14427 O O      . HOH I 5 .   ? -5.438  -35.196 3.675   1.00 49.47  ?  602  HOH A O      1 
HETATM 14428 O O      . HOH I 5 .   ? 28.892  -40.006 -18.710 1.00 33.27  ?  603  HOH A O      1 
HETATM 14429 O O      . HOH I 5 .   ? 11.153  7.940   -24.778 1.00 42.90  ?  604  HOH A O      1 
HETATM 14430 O O      . HOH I 5 .   ? 7.374   -38.860 -28.133 1.00 30.40  ?  605  HOH A O      1 
HETATM 14431 O O      . HOH I 5 .   ? -11.372 -16.820 -26.472 1.00 63.61  ?  606  HOH A O      1 
HETATM 14432 O O      . HOH I 5 .   ? -38.276 -17.404 -17.150 1.00 62.15  ?  607  HOH A O      1 
HETATM 14433 O O      . HOH I 5 .   ? -12.265 -40.692 -12.284 1.00 38.98  ?  608  HOH A O      1 
HETATM 14434 O O      . HOH I 5 .   ? -15.472 4.448   -17.645 1.00 41.52  ?  609  HOH A O      1 
HETATM 14435 O O      . HOH I 5 .   ? 16.340  -24.096 -1.622  1.00 44.32  ?  610  HOH A O      1 
HETATM 14436 O O      . HOH I 5 .   ? 9.505   -38.864 -27.316 1.00 30.00  ?  611  HOH A O      1 
HETATM 14437 O O      . HOH I 5 .   ? 4.737   -25.463 0.214   1.00 51.28  ?  612  HOH A O      1 
HETATM 14438 O O      . HOH I 5 .   ? 1.730   -17.375 -20.977 1.00 17.29  ?  613  HOH A O      1 
HETATM 14439 O O      . HOH I 5 .   ? -24.547 -2.278  -14.169 1.00 56.19  ?  614  HOH A O      1 
HETATM 14440 O O      . HOH I 5 .   ? -17.748 -20.610 -4.320  1.00 45.08  ?  615  HOH A O      1 
HETATM 14441 O O      . HOH I 5 .   ? -19.655 -12.120 2.005   1.00 35.32  ?  616  HOH A O      1 
HETATM 14442 O O      . HOH I 5 .   ? 20.184  -34.503 -4.888  1.00 30.00  ?  617  HOH A O      1 
HETATM 14443 O O      . HOH I 5 .   ? -23.813 -34.528 -6.132  1.00 45.04  ?  618  HOH A O      1 
HETATM 14444 O O      . HOH I 5 .   ? 7.592   -1.288  -10.499 1.00 38.55  ?  619  HOH A O      1 
HETATM 14445 O O      . HOH I 5 .   ? -23.944 -22.220 -2.174  1.00 37.85  ?  620  HOH A O      1 
HETATM 14446 O O      . HOH I 5 .   ? 24.207  -35.921 -9.314  1.00 38.92  ?  621  HOH A O      1 
HETATM 14447 O O      . HOH I 5 .   ? 10.583  -38.216 -21.129 1.00 32.20  ?  622  HOH A O      1 
HETATM 14448 O O      . HOH I 5 .   ? -25.667 -32.982 -29.560 1.00 55.95  ?  623  HOH A O      1 
HETATM 14449 O O      . HOH I 5 .   ? 8.159   4.786   -13.329 1.00 51.18  ?  624  HOH A O      1 
HETATM 14450 O O      . HOH I 5 .   ? -38.989 -25.351 -20.778 1.00 40.49  ?  625  HOH A O      1 
HETATM 14451 O O      . HOH I 5 .   ? -22.203 -34.046 -14.283 1.00 48.68  ?  626  HOH A O      1 
HETATM 14452 O O      . HOH I 5 .   ? -19.401 -30.715 -6.153  1.00 45.61  ?  627  HOH A O      1 
HETATM 14453 O O      . HOH I 5 .   ? 10.472  -11.363 -22.992 1.00 19.46  ?  628  HOH A O      1 
HETATM 14454 O O      . HOH I 5 .   ? 13.303  0.266   -13.623 1.00 40.44  ?  629  HOH A O      1 
HETATM 14455 O O      . HOH I 5 .   ? -6.383  -50.094 -7.213  1.00 26.52  ?  630  HOH A O      1 
HETATM 14456 O O      . HOH I 5 .   ? 3.322   -12.117 -1.895  1.00 30.00  ?  631  HOH A O      1 
HETATM 14457 O O      . HOH I 5 .   ? 4.478   -10.309 -3.247  1.00 25.28  ?  632  HOH A O      1 
HETATM 14458 O O      . HOH I 5 .   ? 2.880   -12.950 -4.303  1.00 32.94  ?  633  HOH A O      1 
HETATM 14459 O O      . HOH I 5 .   ? -1.329  -21.962 -25.029 1.00 16.34  ?  634  HOH A O      1 
HETATM 14460 O O      . HOH I 5 .   ? 16.918  -3.468  -13.161 1.00 30.89  ?  635  HOH A O      1 
HETATM 14461 O O      . HOH I 5 .   ? -12.902 -28.981 -1.348  1.00 34.56  ?  636  HOH A O      1 
HETATM 14462 O O      . HOH I 5 .   ? -12.738 -32.108 -31.282 1.00 35.16  ?  637  HOH A O      1 
HETATM 14463 O O      . HOH I 5 .   ? -16.916 -6.907  -40.184 1.00 32.00  ?  638  HOH A O      1 
HETATM 14464 O O      . HOH I 5 .   ? -17.204 -19.433 -6.701  1.00 40.97  ?  639  HOH A O      1 
HETATM 14465 O O      . HOH I 5 .   ? -31.758 -10.730 -13.773 1.00 27.87  ?  640  HOH A O      1 
HETATM 14466 O O      . HOH I 5 .   ? 2.086   -17.076 -24.658 1.00 14.33  ?  641  HOH A O      1 
HETATM 14467 O O      . HOH I 5 .   ? 16.736  -28.689 -0.731  1.00 25.85  ?  642  HOH A O      1 
HETATM 14468 O O      . HOH I 5 .   ? -27.419 -10.027 -21.236 1.00 24.87  ?  643  HOH A O      1 
HETATM 14469 O O      . HOH I 5 .   ? -14.583 -43.610 3.136   1.00 42.92  ?  644  HOH A O      1 
HETATM 14470 O O      . HOH I 5 .   ? -21.194 -2.597  -4.225  1.00 32.43  ?  645  HOH A O      1 
HETATM 14471 O O      . HOH I 5 .   ? 10.089  -52.135 -12.041 1.00 40.04  ?  646  HOH A O      1 
HETATM 14472 O O      . HOH I 5 .   ? -30.175 -7.666  -19.125 1.00 26.41  ?  647  HOH A O      1 
HETATM 14473 O O      . HOH I 5 .   ? -17.874 -30.301 -3.556  1.00 32.60  ?  648  HOH A O      1 
HETATM 14474 O O      . HOH I 5 .   ? -28.589 -17.044 -26.350 1.00 26.79  ?  649  HOH A O      1 
HETATM 14475 O O      . HOH I 5 .   ? -25.736 -38.381 -10.156 1.00 47.16  ?  650  HOH A O      1 
HETATM 14476 O O      . HOH I 5 .   ? -25.289 -24.485 -3.780  1.00 35.29  ?  651  HOH A O      1 
HETATM 14477 O O      . HOH I 5 .   ? 1.310   1.482   -6.338  1.00 43.04  ?  652  HOH A O      1 
HETATM 14478 O O      . HOH I 5 .   ? -33.330 -13.380 -24.904 1.00 38.55  ?  653  HOH A O      1 
HETATM 14479 O O      . HOH I 5 .   ? 29.451  -37.782 -13.432 1.00 44.75  ?  654  HOH A O      1 
HETATM 14480 O O      . HOH I 5 .   ? -17.446 0.818   -17.751 1.00 50.58  ?  655  HOH A O      1 
HETATM 14481 O O      . HOH I 5 .   ? 9.971   -46.130 -21.389 1.00 26.46  ?  656  HOH A O      1 
HETATM 14482 O O      . HOH I 5 .   ? -14.432 0.114   -11.279 1.00 37.64  ?  657  HOH A O      1 
HETATM 14483 O O      . HOH I 5 .   ? 4.501   -53.192 -12.695 1.00 32.03  ?  658  HOH A O      1 
HETATM 14484 O O      . HOH I 5 .   ? 10.511  -52.009 -18.832 1.00 26.05  ?  659  HOH A O      1 
HETATM 14485 O O      . HOH I 5 .   ? -41.906 -20.161 -26.135 1.00 28.08  ?  660  HOH A O      1 
HETATM 14486 O O      . HOH I 5 .   ? -17.969 -25.544 -4.770  1.00 35.03  ?  661  HOH A O      1 
HETATM 14487 O O      . HOH I 5 .   ? -5.821  -43.196 -14.786 1.00 24.58  ?  662  HOH A O      1 
HETATM 14488 O O      . HOH I 5 .   ? -3.371  -29.781 -14.945 1.00 12.99  ?  663  HOH A O      1 
HETATM 14489 O O      . HOH I 5 .   ? 24.861  -42.034 -14.242 1.00 74.59  ?  664  HOH A O      1 
HETATM 14490 O O      . HOH I 5 .   ? 25.645  -40.698 -17.007 1.00 31.44  ?  665  HOH A O      1 
HETATM 14491 O O      . HOH I 5 .   ? 7.036   -17.157 -0.793  1.00 27.49  ?  666  HOH A O      1 
HETATM 14492 O O      . HOH I 5 .   ? -27.040 -11.265 -5.751  1.00 45.06  ?  667  HOH A O      1 
HETATM 14493 O O      . HOH I 5 .   ? -9.688  -25.132 -2.574  1.00 21.53  ?  668  HOH A O      1 
HETATM 14494 O O      . HOH I 5 .   ? 18.016  -0.872  -26.901 1.00 41.26  ?  669  HOH A O      1 
HETATM 14495 O O      . HOH I 5 .   ? -3.274  -32.443 -18.774 1.00 20.57  ?  670  HOH A O      1 
HETATM 14496 O O      . HOH I 5 .   ? -33.513 -26.400 -13.564 1.00 37.11  ?  671  HOH A O      1 
HETATM 14497 O O      . HOH I 5 .   ? 25.722  -25.569 -7.305  1.00 30.16  ?  672  HOH A O      1 
HETATM 14498 O O      . HOH I 5 .   ? 20.410  -42.705 -22.588 1.00 49.37  ?  673  HOH A O      1 
HETATM 14499 O O      . HOH I 5 .   ? -24.769 -26.098 -31.947 1.00 30.92  ?  674  HOH A O      1 
HETATM 14500 O O      . HOH I 5 .   ? 4.559   -13.741 -18.441 1.00 17.26  ?  675  HOH A O      1 
HETATM 14501 O O      . HOH I 5 .   ? -31.728 -11.095 -17.267 1.00 31.47  ?  676  HOH A O      1 
HETATM 14502 O O      . HOH I 5 .   ? 5.331   -25.523 -2.168  1.00 30.74  ?  677  HOH A O      1 
HETATM 14503 O O      . HOH I 5 .   ? -4.219  -0.094  -21.473 1.00 26.05  ?  678  HOH A O      1 
HETATM 14504 O O      . HOH I 5 .   ? 0.943   -41.219 -25.819 1.00 20.97  ?  679  HOH A O      1 
HETATM 14505 O O      . HOH I 5 .   ? -29.418 -24.903 -8.248  1.00 36.05  ?  680  HOH A O      1 
HETATM 14506 O O      . HOH I 5 .   ? -15.791 -9.573  -28.698 1.00 26.16  ?  681  HOH A O      1 
HETATM 14507 O O      . HOH I 5 .   ? -15.146 3.046   -34.995 1.00 34.47  ?  682  HOH A O      1 
HETATM 14508 O O      . HOH I 5 .   ? -15.690 -11.772 3.241   1.00 49.02  ?  683  HOH A O      1 
HETATM 14509 O O      . HOH I 5 .   ? -10.707 2.105   -19.036 1.00 32.42  ?  684  HOH A O      1 
HETATM 14510 O O      . HOH I 5 .   ? 26.729  -12.026 -30.813 1.00 15.37  ?  685  HOH A O      1 
HETATM 14511 O O      . HOH I 5 .   ? -33.420 -24.949 -28.744 1.00 51.42  ?  686  HOH A O      1 
HETATM 14512 O O      . HOH I 5 .   ? 8.650   -47.434 -2.835  1.00 30.00  ?  687  HOH A O      1 
HETATM 14513 O O      . HOH I 5 .   ? -25.344 -30.072 -8.492  1.00 26.85  ?  688  HOH A O      1 
HETATM 14514 O O      . HOH I 5 .   ? -18.775 -23.348 -21.765 1.00 16.23  ?  689  HOH A O      1 
HETATM 14515 O O      . HOH I 5 .   ? 7.477   -19.356 -27.320 1.00 28.77  ?  690  HOH A O      1 
HETATM 14516 O O      . HOH I 5 .   ? 9.491   -24.252 -2.063  1.00 59.32  ?  691  HOH A O      1 
HETATM 14517 O O      . HOH I 5 .   ? 3.689   -1.272  0.537   1.00 34.35  ?  692  HOH A O      1 
HETATM 14518 O O      . HOH I 5 .   ? -11.388 -29.285 -25.902 1.00 16.69  ?  693  HOH A O      1 
HETATM 14519 O O      . HOH I 5 .   ? 4.877   -25.963 -27.446 1.00 17.01  ?  694  HOH A O      1 
HETATM 14520 O O      . HOH I 5 .   ? 4.824   -20.836 -27.593 1.00 22.71  ?  695  HOH A O      1 
HETATM 14521 O O      . HOH I 5 .   ? 18.453  -25.231 -0.943  1.00 40.46  ?  696  HOH A O      1 
HETATM 14522 O O      . HOH I 5 .   ? 7.643   -37.470 -6.165  1.00 31.12  ?  697  HOH A O      1 
HETATM 14523 O O      . HOH I 5 .   ? -9.442  -30.406 4.635   1.00 42.37  ?  698  HOH A O      1 
HETATM 14524 O O      . HOH I 5 .   ? -19.723 -3.523  -29.946 1.00 28.72  ?  699  HOH A O      1 
HETATM 14525 O O      . HOH I 5 .   ? -7.403  -36.587 -26.628 1.00 43.95  ?  700  HOH A O      1 
HETATM 14526 O O      . HOH I 5 .   ? 10.436  -8.851  -24.168 1.00 15.65  ?  701  HOH A O      1 
HETATM 14527 O O      . HOH I 5 .   ? -1.764  -18.210 -6.017  1.00 14.52  ?  702  HOH A O      1 
HETATM 14528 O O      . HOH I 5 .   ? 32.877  -31.254 -18.579 1.00 24.67  ?  703  HOH A O      1 
HETATM 14529 O O      . HOH I 5 .   ? -18.578 -18.812 -36.825 1.00 34.66  ?  704  HOH A O      1 
HETATM 14530 O O      . HOH I 5 .   ? -8.880  -29.933 -32.701 1.00 16.41  ?  705  HOH A O      1 
HETATM 14531 O O      . HOH I 5 .   ? -22.966 -3.229  -8.364  1.00 38.04  ?  706  HOH A O      1 
HETATM 14532 O O      . HOH I 5 .   ? 22.209  -14.354 -6.455  1.00 16.54  ?  707  HOH A O      1 
HETATM 14533 O O      . HOH I 5 .   ? -13.527 -31.903 -34.218 1.00 31.24  ?  708  HOH A O      1 
HETATM 14534 O O      . HOH I 5 .   ? -22.794 -29.753 -22.431 1.00 32.25  ?  709  HOH A O      1 
HETATM 14535 O O      . HOH I 5 .   ? -34.829 -29.281 -17.027 1.00 42.78  ?  710  HOH A O      1 
HETATM 14536 O O      . HOH I 5 .   ? -14.094 -0.005  -6.453  1.00 27.42  ?  711  HOH A O      1 
HETATM 14537 O O      . HOH I 5 .   ? 4.628   -42.614 -0.345  1.00 24.67  ?  712  HOH A O      1 
HETATM 14538 O O      . HOH I 5 .   ? 25.011  -31.640 -21.696 1.00 19.07  ?  713  HOH A O      1 
HETATM 14539 O O      . HOH I 5 .   ? -4.374  -39.769 -23.550 1.00 55.19  ?  714  HOH A O      1 
HETATM 14540 O O      . HOH I 5 .   ? -18.106 -1.322  -30.090 1.00 24.18  ?  715  HOH A O      1 
HETATM 14541 O O      . HOH I 5 .   ? -23.931 -8.006  -6.811  1.00 22.32  ?  716  HOH A O      1 
HETATM 14542 O O      . HOH I 5 .   ? -26.195 -17.113 1.560   1.00 42.82  ?  717  HOH A O      1 
HETATM 14543 O O      . HOH I 5 .   ? -9.598  -2.169  -8.948  1.00 20.32  ?  718  HOH A O      1 
HETATM 14544 O O      . HOH I 5 .   ? 19.176  -18.364 -21.331 1.00 13.47  ?  719  HOH A O      1 
HETATM 14545 O O      . HOH I 5 .   ? -10.796 -12.346 -46.284 1.00 45.52  ?  720  HOH A O      1 
HETATM 14546 O O      . HOH I 5 .   ? 13.725  -37.999 -8.510  1.00 30.30  ?  721  HOH A O      1 
HETATM 14547 O O      . HOH I 5 .   ? 18.254  -23.858 -3.388  1.00 27.05  ?  722  HOH A O      1 
HETATM 14548 O O      . HOH I 5 .   ? -26.402 -23.921 -7.848  1.00 36.39  ?  723  HOH A O      1 
HETATM 14549 O O      . HOH I 5 .   ? -15.045 5.124   -23.437 1.00 33.72  ?  724  HOH A O      1 
HETATM 14550 O O      . HOH I 5 .   ? 17.026  -9.236  -7.039  1.00 25.78  ?  725  HOH A O      1 
HETATM 14551 O O      . HOH I 5 .   ? -29.078 -6.304  -11.929 1.00 36.01  ?  726  HOH A O      1 
HETATM 14552 O O      . HOH I 5 .   ? 20.820  -26.315 -5.816  1.00 24.49  ?  727  HOH A O      1 
HETATM 14553 O O      . HOH I 5 .   ? -5.831  -37.257 -11.164 1.00 12.95  ?  728  HOH A O      1 
HETATM 14554 O O      . HOH I 5 .   ? -32.130 -29.695 -21.904 1.00 41.04  ?  729  HOH A O      1 
HETATM 14555 O O      . HOH I 5 .   ? 12.028  -17.744 0.271   1.00 38.39  ?  730  HOH A O      1 
HETATM 14556 O O      . HOH I 5 .   ? -3.210  -15.686 -12.978 1.00 12.73  ?  731  HOH A O      1 
HETATM 14557 O O      . HOH I 5 .   ? -4.106  -23.582 -13.566 1.00 14.15  ?  732  HOH A O      1 
HETATM 14558 O O      . HOH I 5 .   ? 1.599   1.594   -10.887 1.00 22.43  ?  733  HOH A O      1 
HETATM 14559 O O      . HOH I 5 .   ? 24.102  -3.636  -16.227 1.00 34.18  ?  734  HOH A O      1 
HETATM 14560 O O      . HOH I 5 .   ? -1.415  -41.916 -1.521  1.00 22.47  ?  735  HOH A O      1 
HETATM 14561 O O      . HOH I 5 .   ? -18.419 -12.184 -21.766 1.00 16.25  ?  736  HOH A O      1 
HETATM 14562 O O      . HOH I 5 .   ? -12.908 -11.758 2.795   1.00 34.74  ?  737  HOH A O      1 
HETATM 14563 O O      . HOH I 5 .   ? -1.747  -46.367 -19.231 1.00 28.02  ?  738  HOH A O      1 
HETATM 14564 O O      . HOH I 5 .   ? -11.860 -13.291 -23.249 1.00 32.25  ?  739  HOH A O      1 
HETATM 14565 O O      . HOH I 5 .   ? 29.631  -35.276 -13.797 1.00 30.86  ?  740  HOH A O      1 
HETATM 14566 O O      . HOH I 5 .   ? -9.712  2.024   -12.118 1.00 69.79  ?  741  HOH A O      1 
HETATM 14567 O O      . HOH I 5 .   ? 12.123  -39.307 -13.185 1.00 14.86  ?  742  HOH A O      1 
HETATM 14568 O O      . HOH I 5 .   ? -4.146  -1.848  -6.098  1.00 30.33  ?  743  HOH A O      1 
HETATM 14569 O O      . HOH I 5 .   ? 3.792   -51.558 -5.628  1.00 35.29  ?  744  HOH A O      1 
HETATM 14570 O O      . HOH I 5 .   ? 2.721   -46.955 -22.989 1.00 36.73  ?  745  HOH A O      1 
HETATM 14571 O O      . HOH I 5 .   ? -23.736 -29.612 -15.298 1.00 22.40  ?  746  HOH A O      1 
HETATM 14572 O O      . HOH I 5 .   ? 2.065   -37.507 -32.763 1.00 31.56  ?  747  HOH A O      1 
HETATM 14573 O O      . HOH I 5 .   ? -14.505 -33.279 5.063   1.00 19.59  ?  748  HOH A O      1 
HETATM 14574 O O      . HOH I 5 .   ? 12.842  -15.244 -22.098 1.00 15.01  ?  749  HOH A O      1 
HETATM 14575 O O      . HOH I 5 .   ? -9.178  -35.589 -38.407 1.00 28.78  ?  750  HOH A O      1 
HETATM 14576 O O      . HOH I 5 .   ? 5.893   -34.363 -3.150  1.00 28.62  ?  751  HOH A O      1 
HETATM 14577 O O      . HOH I 5 .   ? -20.680 -2.141  -6.999  1.00 25.86  ?  752  HOH A O      1 
HETATM 14578 O O      . HOH I 5 .   ? 7.348   -38.537 -24.508 1.00 43.63  ?  753  HOH A O      1 
HETATM 14579 O O      . HOH I 5 .   ? -11.959 -14.233 -21.793 1.00 32.63  ?  754  HOH A O      1 
HETATM 14580 O O      . HOH I 5 .   ? -10.939 2.524   -16.348 1.00 33.59  ?  755  HOH A O      1 
HETATM 14581 O O      . HOH I 5 .   ? -12.265 -38.001 -12.982 1.00 22.85  ?  756  HOH A O      1 
HETATM 14582 O O      . HOH I 5 .   ? 27.929  -30.876 -9.121  1.00 40.25  ?  757  HOH A O      1 
HETATM 14583 O O      . HOH I 5 .   ? -5.508  -1.389  -31.037 1.00 20.15  ?  758  HOH A O      1 
HETATM 14584 O O      . HOH I 5 .   ? 0.641   -16.517 -13.106 1.00 14.14  ?  759  HOH A O      1 
HETATM 14585 O O      . HOH I 5 .   ? -8.516  -14.377 -41.565 1.00 14.97  ?  760  HOH A O      1 
HETATM 14586 O O      . HOH I 5 .   ? -2.230  -32.488 -15.726 1.00 12.91  ?  761  HOH A O      1 
HETATM 14587 O O      . HOH I 5 .   ? 1.705   -37.115 0.611   1.00 28.91  ?  762  HOH A O      1 
HETATM 14588 O O      . HOH I 5 .   ? -7.549  -37.205 -30.807 1.00 35.83  ?  763  HOH A O      1 
HETATM 14589 O O      . HOH I 5 .   ? -2.067  -40.137 -30.057 1.00 29.87  ?  764  HOH A O      1 
HETATM 14590 O O      . HOH I 5 .   ? -5.384  -39.949 -11.218 1.00 16.03  ?  765  HOH A O      1 
HETATM 14591 O O      . HOH I 5 .   ? -3.183  -45.645 -4.404  1.00 32.44  ?  766  HOH A O      1 
HETATM 14592 O O      . HOH I 5 .   ? 23.726  -39.321 -9.377  1.00 49.09  ?  767  HOH A O      1 
HETATM 14593 O O      . HOH I 5 .   ? -21.828 -26.317 -25.117 1.00 27.99  ?  768  HOH A O      1 
HETATM 14594 O O      . HOH I 5 .   ? 10.610  -11.786 -4.481  1.00 23.13  ?  769  HOH A O      1 
HETATM 14595 O O      . HOH I 5 .   ? 11.864  -13.521 -23.923 1.00 21.06  ?  770  HOH A O      1 
HETATM 14596 O O      . HOH I 5 .   ? -10.766 -48.737 -13.052 1.00 36.80  ?  771  HOH A O      1 
HETATM 14597 O O      . HOH I 5 .   ? -17.931 -6.506  2.139   1.00 47.07  ?  772  HOH A O      1 
HETATM 14598 O O      . HOH I 5 .   ? 8.775   2.299   -13.421 1.00 31.01  ?  773  HOH A O      1 
HETATM 14599 O O      . HOH I 5 .   ? -1.615  -22.984 -12.668 1.00 14.94  ?  774  HOH A O      1 
HETATM 14600 O O      . HOH I 5 .   ? -3.261  0.522   -13.803 1.00 32.98  ?  775  HOH A O      1 
HETATM 14601 O O      . HOH I 5 .   ? 16.724  -0.403  -16.734 1.00 34.55  ?  776  HOH A O      1 
HETATM 14602 O O      . HOH I 5 .   ? 17.883  -12.143 -24.187 1.00 16.79  ?  777  HOH A O      1 
HETATM 14603 O O      . HOH I 5 .   ? -37.107 -18.812 -16.372 1.00 45.46  ?  778  HOH A O      1 
HETATM 14604 O O      . HOH I 5 .   ? 29.443  -34.586 -25.089 1.00 33.64  ?  779  HOH A O      1 
HETATM 14605 O O      . HOH I 5 .   ? 2.877   -7.206  0.457   1.00 43.94  ?  780  HOH A O      1 
HETATM 14606 O O      . HOH I 5 .   ? 13.968  -0.719  -16.038 1.00 24.59  ?  781  HOH A O      1 
HETATM 14607 O O      . HOH I 5 .   ? -3.943  -29.553 -0.245  1.00 35.45  ?  782  HOH A O      1 
HETATM 14608 O O      . HOH I 5 .   ? -12.502 -44.136 -2.676  1.00 29.52  ?  783  HOH A O      1 
HETATM 14609 O O      . HOH I 5 .   ? -7.573  -38.151 2.354   1.00 22.69  ?  784  HOH A O      1 
HETATM 14610 O O      . HOH I 5 .   ? -10.627 -34.317 -22.495 1.00 23.11  ?  785  HOH A O      1 
HETATM 14611 O O      . HOH I 5 .   ? -4.197  -7.826  4.844   1.00 56.66  ?  786  HOH A O      1 
HETATM 14612 O O      . HOH I 5 .   ? 0.420   -12.049 -10.901 1.00 14.83  ?  787  HOH A O      1 
HETATM 14613 O O      . HOH I 5 .   ? -13.225 -26.202 -19.299 1.00 13.71  ?  788  HOH A O      1 
HETATM 14614 O O      . HOH I 5 .   ? 21.918  -5.132  -9.116  1.00 31.43  ?  789  HOH A O      1 
HETATM 14615 O O      . HOH I 5 .   ? 23.460  -10.649 -22.417 1.00 19.37  ?  790  HOH A O      1 
HETATM 14616 O O      . HOH I 5 .   ? -26.645 -15.300 -25.677 1.00 27.64  ?  791  HOH A O      1 
HETATM 14617 O O      . HOH I 5 .   ? -12.692 -8.411  -45.417 1.00 26.59  ?  792  HOH A O      1 
HETATM 14618 O O      . HOH I 5 .   ? -34.356 -13.930 -22.275 1.00 30.49  ?  793  HOH A O      1 
HETATM 14619 O O      . HOH I 5 .   ? -22.726 -10.533 -27.142 1.00 33.64  ?  794  HOH A O      1 
HETATM 14620 O O      . HOH I 5 .   ? -12.124 -23.860 -2.882  1.00 31.93  ?  795  HOH A O      1 
HETATM 14621 O O      . HOH I 5 .   ? 14.326  -46.953 -15.030 1.00 22.80  ?  796  HOH A O      1 
HETATM 14622 O O      . HOH I 5 .   ? -3.672  -5.899  0.382   1.00 33.33  ?  797  HOH A O      1 
HETATM 14623 O O      . HOH I 5 .   ? -15.038 -31.957 1.230   1.00 42.00  ?  798  HOH A O      1 
HETATM 14624 O O      . HOH I 5 .   ? -5.270  -37.386 1.293   1.00 20.69  ?  799  HOH A O      1 
HETATM 14625 O O      . HOH I 5 .   ? 19.719  -35.205 -7.158  1.00 24.56  ?  800  HOH A O      1 
HETATM 14626 O O      . HOH I 5 .   ? -20.944 -28.815 -18.529 1.00 25.19  ?  801  HOH A O      1 
HETATM 14627 O O      . HOH I 5 .   ? -2.125  -14.505 -34.817 1.00 13.43  ?  802  HOH A O      1 
HETATM 14628 O O      . HOH I 5 .   ? -7.020  -27.185 -16.943 1.00 12.54  ?  803  HOH A O      1 
HETATM 14629 O O      . HOH I 5 .   ? 7.814   -3.387  -4.097  1.00 30.58  ?  804  HOH A O      1 
HETATM 14630 O O      . HOH I 5 .   ? -8.265  -39.506 -0.107  1.00 28.03  ?  805  HOH A O      1 
HETATM 14631 O O      . HOH I 5 .   ? -14.405 -35.220 1.747   1.00 18.77  ?  806  HOH A O      1 
HETATM 14632 O O      . HOH I 5 .   ? 17.488  4.437   -19.285 1.00 26.33  ?  807  HOH A O      1 
HETATM 14633 O O      . HOH I 5 .   ? -6.671  -48.164 -14.304 1.00 26.78  ?  808  HOH A O      1 
HETATM 14634 O O      . HOH I 5 .   ? -6.697  -17.885 -0.628  1.00 25.71  ?  809  HOH A O      1 
HETATM 14635 O O      . HOH I 5 .   ? -13.060 -20.611 -29.864 1.00 24.03  ?  810  HOH A O      1 
HETATM 14636 O O      . HOH I 5 .   ? -2.647  -19.837 1.351   1.00 26.54  ?  811  HOH A O      1 
HETATM 14637 O O      . HOH I 5 .   ? 9.350   -28.338 -3.586  1.00 25.30  ?  812  HOH A O      1 
HETATM 14638 O O      . HOH I 5 .   ? 27.357  -30.675 -25.005 1.00 39.52  ?  813  HOH A O      1 
HETATM 14639 O O      . HOH I 5 .   ? -18.465 -0.534  -34.927 1.00 35.56  ?  814  HOH A O      1 
HETATM 14640 O O      . HOH I 5 .   ? -11.385 -7.481  0.677   1.00 29.47  ?  815  HOH A O      1 
HETATM 14641 O O      . HOH I 5 .   ? 19.895  -2.510  -16.412 1.00 32.56  ?  816  HOH A O      1 
HETATM 14642 O O      . HOH I 5 .   ? 1.488   -36.814 -37.528 1.00 22.58  ?  817  HOH A O      1 
HETATM 14643 O O      . HOH I 5 .   ? 20.907  -43.764 -10.932 1.00 49.55  ?  818  HOH A O      1 
HETATM 14644 O O      . HOH I 5 .   ? -11.739 3.593   -41.501 1.00 44.68  ?  819  HOH A O      1 
HETATM 14645 O O      . HOH I 5 .   ? -11.024 -19.740 -26.664 1.00 46.00  ?  820  HOH A O      1 
HETATM 14646 O O      . HOH I 5 .   ? -5.071  -23.496 -17.640 1.00 14.96  ?  821  HOH A O      1 
HETATM 14647 O O      . HOH I 5 .   ? 8.908   -35.410 -5.717  1.00 37.41  ?  822  HOH A O      1 
HETATM 14648 O O      . HOH I 5 .   ? -9.510  -16.552 -40.383 1.00 15.47  ?  823  HOH A O      1 
HETATM 14649 O O      . HOH I 5 .   ? -10.665 -0.790  -12.085 1.00 27.84  ?  824  HOH A O      1 
HETATM 14650 O O      . HOH I 5 .   ? -18.761 -1.411  -18.406 1.00 33.42  ?  825  HOH A O      1 
HETATM 14651 O O      . HOH I 5 .   ? 11.199  -22.289 -21.901 1.00 12.03  ?  826  HOH A O      1 
HETATM 14652 O O      . HOH I 5 .   ? 26.311  -13.999 -16.279 1.00 16.29  ?  827  HOH A O      1 
HETATM 14653 O O      . HOH I 5 .   ? -19.678 -16.659 -26.556 1.00 24.65  ?  828  HOH A O      1 
HETATM 14654 O O      . HOH I 5 .   ? 2.884   -25.311 1.558   1.00 36.26  ?  829  HOH A O      1 
HETATM 14655 O O      . HOH I 5 .   ? -17.432 -5.559  -33.700 1.00 40.65  ?  830  HOH A O      1 
HETATM 14656 O O      . HOH I 5 .   ? 19.037  -15.513 -25.324 1.00 13.97  ?  831  HOH A O      1 
HETATM 14657 O O      . HOH I 5 .   ? -7.925  -3.142  -4.780  1.00 28.32  ?  832  HOH A O      1 
HETATM 14658 O O      . HOH I 5 .   ? 24.161  -42.098 -19.008 1.00 35.27  ?  833  HOH A O      1 
HETATM 14659 O O      . HOH I 5 .   ? -23.198 -43.578 -5.421  1.00 48.07  ?  834  HOH A O      1 
HETATM 14660 O O      . HOH I 5 .   ? -29.133 -18.812 -5.905  1.00 33.85  ?  835  HOH A O      1 
HETATM 14661 O O      . HOH I 5 .   ? 3.204   -31.797 1.469   1.00 38.49  ?  836  HOH A O      1 
HETATM 14662 O O      . HOH I 5 .   ? -6.049  -38.152 -28.726 1.00 38.06  ?  837  HOH A O      1 
HETATM 14663 O O      . HOH I 5 .   ? -33.327 -21.219 -26.291 1.00 23.99  ?  838  HOH A O      1 
HETATM 14664 O O      . HOH I 5 .   ? -18.185 -31.282 -19.716 1.00 44.85  ?  839  HOH A O      1 
HETATM 14665 O O      . HOH I 5 .   ? -24.970 -26.701 -24.207 1.00 21.39  ?  840  HOH A O      1 
HETATM 14666 O O      . HOH I 5 .   ? 12.204  -3.052  -13.855 1.00 23.24  ?  841  HOH A O      1 
HETATM 14667 O O      . HOH I 5 .   ? -22.158 -17.010 0.502   1.00 24.27  ?  842  HOH A O      1 
HETATM 14668 O O      . HOH I 5 .   ? 32.621  -18.420 -23.471 1.00 33.02  ?  843  HOH A O      1 
HETATM 14669 O O      . HOH I 5 .   ? 16.638  -15.335 -4.019  1.00 30.14  ?  844  HOH A O      1 
HETATM 14670 O O      . HOH I 5 .   ? -34.235 -12.202 -17.242 1.00 45.11  ?  845  HOH A O      1 
HETATM 14671 O O      . HOH I 5 .   ? -20.937 -6.645  -29.719 1.00 37.09  ?  846  HOH A O      1 
HETATM 14672 O O      . HOH I 5 .   ? -9.151  -16.903 -0.443  1.00 30.32  ?  847  HOH A O      1 
HETATM 14673 O O      . HOH I 5 .   ? -15.119 -14.897 -34.137 1.00 19.49  ?  848  HOH A O      1 
HETATM 14674 O O      . HOH I 5 .   ? -8.331  -15.580 -38.075 1.00 14.90  ?  849  HOH A O      1 
HETATM 14675 O O      . HOH I 5 .   ? 24.101  -23.451 -7.216  1.00 29.78  ?  850  HOH A O      1 
HETATM 14676 O O      . HOH I 5 .   ? 3.111   -18.172 -13.430 1.00 13.17  ?  851  HOH A O      1 
HETATM 14677 O O      . HOH I 5 .   ? 10.872  -41.104 -3.999  1.00 48.37  ?  852  HOH A O      1 
HETATM 14678 O O      . HOH I 5 .   ? -0.280  -47.546 -22.660 1.00 46.01  ?  853  HOH A O      1 
HETATM 14679 O O      . HOH I 5 .   ? -24.200 -3.412  -17.934 1.00 42.22  ?  854  HOH A O      1 
HETATM 14680 O O      . HOH I 5 .   ? 2.675   -18.241 -0.508  1.00 26.31  ?  855  HOH A O      1 
HETATM 14681 O O      . HOH I 5 .   ? -12.604 -31.632 -7.993  1.00 16.64  ?  856  HOH A O      1 
HETATM 14682 O O      . HOH I 5 .   ? 19.364  -20.780 -5.603  1.00 23.08  ?  857  HOH A O      1 
HETATM 14683 O O      . HOH I 5 .   ? -2.307  -51.769 -12.627 1.00 21.84  ?  858  HOH A O      1 
HETATM 14684 O O      . HOH I 5 .   ? -5.434  -37.316 -31.953 1.00 29.84  ?  859  HOH A O      1 
HETATM 14685 O O      . HOH I 5 .   ? -8.537  -29.950 -9.652  1.00 13.26  ?  860  HOH A O      1 
HETATM 14686 O O      . HOH I 5 .   ? 9.836   -35.636 -21.382 1.00 25.50  ?  861  HOH A O      1 
HETATM 14687 O O      . HOH I 5 .   ? -17.464 -24.463 -24.709 1.00 31.46  ?  862  HOH A O      1 
HETATM 14688 O O      . HOH I 5 .   ? 12.702  -39.591 -10.479 1.00 16.74  ?  863  HOH A O      1 
HETATM 14689 O O      . HOH I 5 .   ? 19.277  -4.755  -28.472 1.00 14.75  ?  864  HOH A O      1 
HETATM 14690 O O      . HOH I 5 .   ? -9.356  -36.671 -28.116 1.00 35.44  ?  865  HOH A O      1 
HETATM 14691 O O      . HOH I 5 .   ? 29.570  -12.280 -26.854 1.00 19.79  ?  866  HOH A O      1 
HETATM 14692 O O      . HOH I 5 .   ? 1.559   -9.314  -2.591  1.00 19.33  ?  867  HOH A O      1 
HETATM 14693 O O      . HOH I 5 .   ? 10.747  -6.865  -8.245  1.00 19.13  ?  868  HOH A O      1 
HETATM 14694 O O      . HOH I 5 .   ? -6.039  -44.234 -2.714  1.00 42.49  ?  869  HOH A O      1 
HETATM 14695 O O      . HOH I 5 .   ? -24.015 -28.763 -19.066 1.00 25.45  ?  870  HOH A O      1 
HETATM 14696 O O      . HOH I 5 .   ? 15.777  -29.922 -28.756 1.00 13.20  ?  871  HOH A O      1 
HETATM 14697 O O      . HOH I 5 .   ? -14.297 -36.560 -13.155 1.00 27.91  ?  872  HOH A O      1 
HETATM 14698 O O      . HOH I 5 .   ? -8.678  -23.856 -0.320  1.00 29.86  ?  873  HOH A O      1 
HETATM 14699 O O      . HOH I 5 .   ? 18.249  -37.648 -8.007  1.00 40.17  ?  874  HOH A O      1 
HETATM 14700 O O      . HOH I 5 .   ? -22.244 -40.981 -15.353 1.00 37.20  ?  875  HOH A O      1 
HETATM 14701 O O      . HOH I 5 .   ? 24.264  -41.195 -11.821 1.00 57.85  ?  876  HOH A O      1 
HETATM 14702 O O      . HOH I 5 .   ? 15.431  -11.722 -3.283  1.00 48.99  ?  877  HOH A O      1 
HETATM 14703 O O      . HOH I 5 .   ? -24.315 -3.047  -21.471 1.00 42.21  ?  878  HOH A O      1 
HETATM 14704 O O      . HOH I 5 .   ? -14.195 -17.488 -34.353 1.00 16.53  ?  879  HOH A O      1 
HETATM 14705 O O      . HOH I 5 .   ? -18.346 -31.552 -1.608  1.00 48.84  ?  880  HOH A O      1 
HETATM 14706 O O      . HOH I 5 .   ? -11.661 -2.433  -44.629 1.00 29.76  ?  881  HOH A O      1 
HETATM 14707 O O      . HOH I 5 .   ? -20.933 -32.808 -6.856  1.00 26.34  ?  882  HOH A O      1 
HETATM 14708 O O      . HOH I 5 .   ? -34.931 -16.017 -14.829 1.00 44.45  ?  883  HOH A O      1 
HETATM 14709 O O      . HOH I 5 .   ? 19.082  -19.108 -32.463 1.00 38.50  ?  884  HOH A O      1 
HETATM 14710 O O      . HOH I 5 .   ? -9.451  -21.282 -26.238 1.00 52.16  ?  885  HOH A O      1 
HETATM 14711 O O      . HOH I 5 .   ? -0.543  -6.257  -19.815 1.00 15.07  ?  886  HOH A O      1 
HETATM 14712 O O      . HOH I 5 .   ? -6.760  -36.307 -23.448 1.00 32.02  ?  887  HOH A O      1 
HETATM 14713 O O      . HOH I 5 .   ? -4.991  -21.711 -25.926 1.00 22.42  ?  888  HOH A O      1 
HETATM 14714 O O      . HOH I 5 .   ? -21.364 -24.789 -3.923  1.00 40.99  ?  889  HOH A O      1 
HETATM 14715 O O      . HOH I 5 .   ? 2.032   -48.342 -0.166  1.00 27.46  ?  890  HOH A O      1 
HETATM 14716 O O      . HOH I 5 .   ? -22.489 -9.235  -4.734  1.00 30.28  ?  891  HOH A O      1 
HETATM 14717 O O      . HOH I 5 .   ? 14.200  -30.809 -8.158  1.00 15.28  ?  892  HOH A O      1 
HETATM 14718 O O      . HOH I 5 .   ? 15.341  -20.473 -3.429  1.00 36.53  ?  893  HOH A O      1 
HETATM 14719 O O      . HOH I 5 .   ? 9.111   -37.668 -22.057 1.00 30.00  ?  894  HOH A O      1 
HETATM 14720 O O      . HOH I 5 .   ? -19.379 -41.058 1.522   1.00 50.96  ?  895  HOH A O      1 
HETATM 14721 O O      . HOH I 5 .   ? -15.830 -30.226 -9.240  1.00 16.59  ?  896  HOH A O      1 
HETATM 14722 O O      . HOH I 5 .   ? 21.047  -9.827  -22.440 1.00 21.40  ?  897  HOH A O      1 
HETATM 14723 O O      . HOH I 5 .   ? -28.264 -8.566  -11.207 1.00 23.34  ?  898  HOH A O      1 
HETATM 14724 O O      . HOH I 5 .   ? 5.840   -9.971  -5.668  1.00 20.75  ?  899  HOH A O      1 
HETATM 14725 O O      . HOH I 5 .   ? -15.291 -26.748 -26.478 1.00 43.87  ?  900  HOH A O      1 
HETATM 14726 O O      . HOH I 5 .   ? -18.801 1.911   -22.705 1.00 29.82  ?  901  HOH A O      1 
HETATM 14727 O O      . HOH I 5 .   ? 19.442  -20.734 -31.166 1.00 63.64  ?  902  HOH A O      1 
HETATM 14728 O O      . HOH I 5 .   ? 17.491  2.427   -27.474 1.00 38.82  ?  903  HOH A O      1 
HETATM 14729 O O      . HOH I 5 .   ? -2.291  -13.730 1.120   1.00 30.12  ?  904  HOH A O      1 
HETATM 14730 O O      . HOH I 5 .   ? -2.585  -40.332 -23.411 1.00 30.72  ?  905  HOH A O      1 
HETATM 14731 O O      . HOH I 5 .   ? -14.227 -34.452 -16.507 1.00 26.74  ?  906  HOH A O      1 
HETATM 14732 O O      . HOH I 5 .   ? 7.540   -38.989 -22.585 1.00 31.93  ?  907  HOH A O      1 
HETATM 14733 O O      . HOH I 5 .   ? 10.469  -48.985 -21.982 1.00 36.01  ?  908  HOH A O      1 
HETATM 14734 O O      . HOH I 5 .   ? -22.342 -25.715 -6.159  1.00 22.29  ?  909  HOH A O      1 
HETATM 14735 O O      . HOH I 5 .   ? -18.311 -18.856 -44.169 1.00 46.62  ?  910  HOH A O      1 
HETATM 14736 O O      . HOH I 5 .   ? -14.350 -34.127 -20.026 1.00 23.68  ?  911  HOH A O      1 
HETATM 14737 O O      . HOH I 5 .   ? -40.457 -15.967 -20.683 1.00 52.23  ?  912  HOH A O      1 
HETATM 14738 O O      . HOH I 5 .   ? -19.635 -37.021 -16.066 1.00 55.82  ?  913  HOH A O      1 
HETATM 14739 O O      . HOH I 5 .   ? 21.312  -28.584 -6.152  1.00 31.96  ?  914  HOH A O      1 
HETATM 14740 O O      . HOH I 5 .   ? -16.224 3.578   -15.935 1.00 38.67  ?  915  HOH A O      1 
HETATM 14741 O O      . HOH I 5 .   ? 15.926  -2.069  -15.916 1.00 53.12  ?  916  HOH A O      1 
HETATM 14742 O O      . HOH I 5 .   ? 7.549   1.181   -22.980 1.00 18.87  ?  917  HOH A O      1 
HETATM 14743 O O      . HOH I 5 .   ? 23.527  1.876   -24.650 1.00 29.63  ?  918  HOH A O      1 
HETATM 14744 O O      . HOH I 5 .   ? 2.431   -43.457 -25.505 1.00 24.94  ?  919  HOH A O      1 
HETATM 14745 O O      . HOH I 5 .   ? -5.172  -20.775 -21.443 1.00 58.39  ?  920  HOH A O      1 
HETATM 14746 O O      . HOH I 5 .   ? -9.497  -4.115  -2.673  1.00 28.21  ?  921  HOH A O      1 
HETATM 14747 O O      . HOH I 5 .   ? -7.161  -31.089 0.948   1.00 29.20  ?  922  HOH A O      1 
HETATM 14748 O O      . HOH I 5 .   ? 1.256   2.602   -13.331 1.00 23.82  ?  923  HOH A O      1 
HETATM 14749 O O      . HOH I 5 .   ? -15.873 -16.917 -24.125 1.00 25.24  ?  924  HOH A O      1 
HETATM 14750 O O      . HOH I 5 .   ? -7.783  -41.609 -18.439 1.00 49.97  ?  925  HOH A O      1 
HETATM 14751 O O      . HOH I 5 .   ? 8.294   -8.614  -2.507  1.00 30.00  ?  926  HOH A O      1 
HETATM 14752 O O      . HOH I 5 .   ? -5.210  -46.047 -14.609 1.00 32.19  ?  927  HOH A O      1 
HETATM 14753 O O      . HOH I 5 .   ? -30.655 -7.454  -22.281 1.00 61.91  ?  928  HOH A O      1 
HETATM 14754 O O      . HOH I 5 .   ? -3.339  -42.164 -21.483 1.00 21.62  ?  929  HOH A O      1 
HETATM 14755 O O      . HOH I 5 .   ? -18.652 -9.999  -29.212 1.00 45.09  ?  930  HOH A O      1 
HETATM 14756 O O      . HOH I 5 .   ? -0.886  -31.886 -0.158  1.00 23.19  ?  931  HOH A O      1 
HETATM 14757 O O      . HOH I 5 .   ? -17.252 -34.344 0.341   1.00 25.31  ?  932  HOH A O      1 
HETATM 14758 O O      . HOH I 5 .   ? -5.858  -36.552 -34.433 1.00 25.85  ?  933  HOH A O      1 
HETATM 14759 O O      . HOH I 5 .   ? 18.318  -9.527  -23.496 1.00 14.61  ?  934  HOH A O      1 
HETATM 14760 O O      . HOH I 5 .   ? -4.208  -39.812 -37.876 1.00 30.27  ?  935  HOH A O      1 
HETATM 14761 O O      . HOH I 5 .   ? 35.718  -15.900 -25.076 1.00 42.35  ?  936  HOH A O      1 
HETATM 14762 O O      . HOH I 5 .   ? 23.280  -31.412 -23.989 1.00 24.46  ?  937  HOH A O      1 
HETATM 14763 O O      . HOH I 5 .   ? -5.710  -30.250 -9.584  1.00 13.70  ?  938  HOH A O      1 
HETATM 14764 O O      . HOH I 5 .   ? -11.279 -38.482 -16.103 1.00 26.35  ?  939  HOH A O      1 
HETATM 14765 O O      . HOH I 5 .   ? 2.939   -51.931 -2.339  1.00 45.41  ?  940  HOH A O      1 
HETATM 14766 O O      . HOH I 5 .   ? -15.106 -34.412 -18.132 1.00 52.27  ?  941  HOH A O      1 
HETATM 14767 O O      . HOH I 5 .   ? 5.244   7.615   -19.471 1.00 42.00  ?  942  HOH A O      1 
HETATM 14768 O O      . HOH I 5 .   ? 25.415  -27.809 -26.469 1.00 29.32  ?  943  HOH A O      1 
HETATM 14769 O O      . HOH I 5 .   ? -16.270 -21.426 -3.875  1.00 30.92  ?  944  HOH A O      1 
HETATM 14770 O O      . HOH I 5 .   ? -12.577 -36.941 -30.233 1.00 54.20  ?  945  HOH A O      1 
HETATM 14771 O O      . HOH I 5 .   ? -3.310  4.534   -17.702 1.00 49.98  ?  946  HOH A O      1 
HETATM 14772 O O      . HOH I 5 .   ? 21.452  -2.976  -19.261 1.00 22.77  ?  947  HOH A O      1 
HETATM 14773 O O      . HOH I 5 .   ? -20.664 -38.398 0.471   1.00 42.29  ?  948  HOH A O      1 
HETATM 14774 O O      . HOH I 5 .   ? -25.399 -3.411  -12.340 1.00 38.64  ?  949  HOH A O      1 
HETATM 14775 O O      . HOH I 5 .   ? -9.597  -23.686 -29.138 1.00 34.10  ?  950  HOH A O      1 
HETATM 14776 O O      . HOH I 5 .   ? -15.338 -41.000 -12.415 1.00 27.50  ?  951  HOH A O      1 
HETATM 14777 O O      . HOH I 5 .   ? 7.117   -49.470 -22.070 1.00 33.81  ?  952  HOH A O      1 
HETATM 14778 O O      . HOH I 5 .   ? 5.486   -36.541 -4.653  1.00 27.56  ?  953  HOH A O      1 
HETATM 14779 O O      . HOH I 5 .   ? -2.500  -2.077  -20.688 1.00 19.99  ?  954  HOH A O      1 
HETATM 14780 O O      . HOH I 5 .   ? 2.813   -13.003 0.089   1.00 54.24  ?  955  HOH A O      1 
HETATM 14781 O O      . HOH I 5 .   ? -15.019 -24.602 -4.898  1.00 20.62  ?  956  HOH A O      1 
HETATM 14782 O O      . HOH I 5 .   ? -4.746  -4.505  -2.325  1.00 37.17  ?  957  HOH A O      1 
HETATM 14783 O O      . HOH I 5 .   ? -26.511 -35.604 -18.251 1.00 35.66  ?  958  HOH A O      1 
HETATM 14784 O O      . HOH I 5 .   ? 10.901  -21.081 -19.468 1.00 11.96  ?  959  HOH A O      1 
HETATM 14785 O O      . HOH I 5 .   ? -7.588  -22.051 -24.878 1.00 26.17  ?  960  HOH A O      1 
HETATM 14786 O O      . HOH I 5 .   ? 12.013  -36.414 -6.780  1.00 32.28  ?  961  HOH A O      1 
HETATM 14787 O O      . HOH I 5 .   ? -15.930 -41.045 -11.087 1.00 36.48  ?  962  HOH A O      1 
HETATM 14788 O O      . HOH I 5 .   ? -31.961 -23.385 -27.298 1.00 34.38  ?  963  HOH A O      1 
HETATM 14789 O O      . HOH I 5 .   ? 11.905  -46.353 -10.988 1.00 20.49  ?  964  HOH A O      1 
HETATM 14790 O O      . HOH I 5 .   ? -14.114 5.192   -19.360 1.00 51.87  ?  965  HOH A O      1 
HETATM 14791 O O      . HOH I 5 .   ? -10.879 3.593   -28.011 1.00 35.83  ?  966  HOH A O      1 
HETATM 14792 O O      . HOH I 5 .   ? -30.144 -30.688 -22.832 1.00 33.93  ?  967  HOH A O      1 
HETATM 14793 O O      . HOH I 5 .   ? 1.206   -41.000 -31.023 1.00 49.02  ?  968  HOH A O      1 
HETATM 14794 O O      . HOH I 5 .   ? 8.173   -36.626 -22.986 1.00 40.14  ?  969  HOH A O      1 
HETATM 14795 O O      . HOH I 5 .   ? -17.576 -5.809  -31.948 1.00 48.13  ?  970  HOH A O      1 
HETATM 14796 O O      . HOH I 5 .   ? -4.247  -32.693 0.111   1.00 19.35  ?  971  HOH A O      1 
HETATM 14797 O O      . HOH I 5 .   ? -33.136 -30.148 -24.486 1.00 50.97  ?  972  HOH A O      1 
HETATM 14798 O O      . HOH I 5 .   ? -6.847  -20.640 -22.510 1.00 38.70  ?  973  HOH A O      1 
HETATM 14799 O O      . HOH I 5 .   ? -19.875 -33.703 -1.118  1.00 53.61  ?  974  HOH A O      1 
HETATM 14800 O O      . HOH I 5 .   ? 16.432  -45.639 -9.548  1.00 40.34  ?  975  HOH A O      1 
HETATM 14801 O O      . HOH I 5 .   ? -8.614  -36.725 -34.813 1.00 33.26  ?  976  HOH A O      1 
HETATM 14802 O O      . HOH I 5 .   ? -32.850 -16.186 -10.890 1.00 57.86  ?  977  HOH A O      1 
HETATM 14803 O O      . HOH I 5 .   ? -14.732 -39.689 3.453   1.00 34.50  ?  978  HOH A O      1 
HETATM 14804 O O      . HOH I 5 .   ? -25.558 -20.423 -1.019  1.00 29.15  ?  979  HOH A O      1 
HETATM 14805 O O      . HOH I 5 .   ? -13.770 3.986   -16.474 1.00 43.71  ?  980  HOH A O      1 
HETATM 14806 O O      . HOH I 5 .   ? -15.461 -17.547 1.010   1.00 40.07  ?  981  HOH A O      1 
HETATM 14807 O O      . HOH I 5 .   ? -18.392 -8.791  -42.288 1.00 59.46  ?  982  HOH A O      1 
HETATM 14808 O O      . HOH I 5 .   ? -18.210 -14.124 -25.656 1.00 37.36  ?  983  HOH A O      1 
HETATM 14809 O O      . HOH I 5 .   ? 8.883   -15.480 0.209   1.00 42.92  ?  984  HOH A O      1 
HETATM 14810 O O      . HOH I 5 .   ? -23.807 -11.404 -3.926  1.00 29.38  ?  985  HOH A O      1 
HETATM 14811 O O      . HOH I 5 .   ? -32.652 -30.239 -10.294 1.00 38.39  ?  986  HOH A O      1 
HETATM 14812 O O      . HOH I 5 .   ? 6.034   -13.190 -0.068  1.00 40.91  ?  987  HOH A O      1 
HETATM 14813 O O      . HOH I 5 .   ? -14.818 -1.883  -2.538  1.00 21.98  ?  988  HOH A O      1 
HETATM 14814 O O      . HOH I 5 .   ? -4.501  -1.289  -12.561 1.00 35.68  ?  989  HOH A O      1 
HETATM 14815 O O      . HOH I 5 .   ? -0.713  4.181   -14.051 1.00 51.62  ?  990  HOH A O      1 
HETATM 14816 O O      . HOH I 5 .   ? -21.895 -0.236  -24.397 1.00 25.84  ?  991  HOH A O      1 
HETATM 14817 O O      . HOH I 5 .   ? -18.477 -7.292  -33.053 1.00 47.12  ?  992  HOH A O      1 
HETATM 14818 O O      . HOH I 5 .   ? -12.340 -44.201 -13.352 1.00 51.48  ?  993  HOH A O      1 
HETATM 14819 O O      . HOH I 5 .   ? -12.195 -3.686  -1.659  1.00 25.33  ?  994  HOH A O      1 
HETATM 14820 O O      . HOH I 5 .   ? -22.421 -7.515  -27.123 1.00 25.46  ?  995  HOH A O      1 
HETATM 14821 O O      . HOH I 5 .   ? 15.614  -39.907 -8.319  1.00 48.59  ?  996  HOH A O      1 
HETATM 14822 O O      . HOH I 5 .   ? -0.828  -48.612 -2.173  1.00 57.53  ?  997  HOH A O      1 
HETATM 14823 O O      . HOH I 5 .   ? -3.843  -23.112 2.846   1.00 66.11  ?  998  HOH A O      1 
HETATM 14824 O O      . HOH I 5 .   ? -11.187 -18.536 -1.490  1.00 16.76  ?  999  HOH A O      1 
HETATM 14825 O O      . HOH I 5 .   ? -36.449 -27.831 -27.843 1.00 53.97  ?  1000 HOH A O      1 
HETATM 14826 O O      . HOH I 5 .   ? 20.343  -47.043 -13.065 1.00 50.50  ?  1001 HOH A O      1 
HETATM 14827 O O      . HOH I 5 .   ? -15.888 5.287   -36.733 1.00 46.58  ?  1002 HOH A O      1 
HETATM 14828 O O      . HOH I 5 .   ? 0.181   -9.450  -0.059  1.00 20.52  ?  1003 HOH A O      1 
HETATM 14829 O O      . HOH I 5 .   ? 10.275  -25.981 -3.562  1.00 47.31  ?  1004 HOH A O      1 
HETATM 14830 O O      . HOH I 5 .   ? -19.014 -4.244  -1.122  1.00 48.62  ?  1005 HOH A O      1 
HETATM 14831 O O      . HOH I 5 .   ? 18.647  -1.748  -10.551 1.00 47.80  ?  1006 HOH A O      1 
HETATM 14832 O O      . HOH I 5 .   ? 19.687  -32.293 -3.879  1.00 50.54  ?  1007 HOH A O      1 
HETATM 14833 O O      . HOH I 5 .   ? -21.018 -8.097  -27.965 1.00 70.34  ?  1008 HOH A O      1 
HETATM 14834 O O      . HOH I 5 .   ? -18.369 -27.138 -25.215 1.00 54.67  ?  1009 HOH A O      1 
HETATM 14835 O O      . HOH I 5 .   ? -9.754  -36.837 -23.863 1.00 63.94  ?  1010 HOH A O      1 
HETATM 14836 O O      . HOH I 5 .   ? 26.256  -33.081 -8.908  1.00 48.93  ?  1011 HOH A O      1 
HETATM 14837 O O      . HOH I 5 .   ? -15.972 -33.787 -22.402 1.00 37.27  ?  1012 HOH A O      1 
HETATM 14838 O O      . HOH I 5 .   ? 1.968   -51.023 -0.431  1.00 47.90  ?  1013 HOH A O      1 
HETATM 14839 O O      . HOH I 5 .   ? -9.283  1.066   -41.707 1.00 33.91  ?  1014 HOH A O      1 
HETATM 14840 O O      . HOH I 5 .   ? -4.982  3.996   -19.826 1.00 45.94  ?  1015 HOH A O      1 
HETATM 14841 O O      . HOH I 5 .   ? -5.232  -37.817 5.315   1.00 49.78  ?  1016 HOH A O      1 
HETATM 14842 O O      . HOH I 5 .   ? -17.650 -8.006  -36.456 1.00 20.68  ?  1017 HOH A O      1 
HETATM 14843 O O      . HOH I 5 .   ? -8.033  -29.846 -1.722  1.00 36.65  ?  1018 HOH A O      1 
HETATM 14844 O O      . HOH I 5 .   ? -13.248 -14.554 -26.788 1.00 27.30  ?  1019 HOH A O      1 
HETATM 14845 O O      . HOH I 5 .   ? -2.594  1.630   -41.660 1.00 32.77  ?  1020 HOH A O      1 
HETATM 14846 O O      . HOH I 5 .   ? 21.138  -43.434 -20.442 1.00 48.71  ?  1021 HOH A O      1 
HETATM 14847 O O      . HOH I 5 .   ? 8.178   -0.676  -5.152  1.00 43.88  ?  1022 HOH A O      1 
HETATM 14848 O O      . HOH I 5 .   ? 10.441  -46.785 -10.084 1.00 57.40  ?  1023 HOH A O      1 
HETATM 14849 O O      . HOH I 5 .   ? -41.771 -24.564 -25.833 1.00 41.19  ?  1024 HOH A O      1 
HETATM 14850 O O      . HOH I 5 .   ? -20.160 -11.773 -45.459 1.00 53.01  ?  1025 HOH A O      1 
HETATM 14851 O O      . HOH I 5 .   ? 13.573  -45.536 -8.886  1.00 39.93  ?  1026 HOH A O      1 
HETATM 14852 O O      . HOH I 5 .   ? -24.297 -36.894 -13.063 1.00 30.00  ?  1027 HOH A O      1 
HETATM 14853 O O      . HOH I 5 .   ? 0.224   -3.224  0.986   1.00 51.33  ?  1028 HOH A O      1 
HETATM 14854 O O      . HOH I 5 .   ? 14.510  -46.545 -23.744 1.00 55.27  ?  1029 HOH A O      1 
HETATM 14855 O O      . HOH I 5 .   ? -21.541 -37.182 -1.589  1.00 51.37  ?  1030 HOH A O      1 
HETATM 14856 O O      . HOH I 5 .   ? -5.639  -31.029 -2.109  1.00 13.89  ?  1031 HOH A O      1 
HETATM 14857 O O      . HOH I 5 .   ? -34.552 -12.272 -20.160 1.00 54.60  ?  1032 HOH A O      1 
HETATM 14858 O O      . HOH I 5 .   ? -4.122  -48.853 -6.699  1.00 36.12  ?  1033 HOH A O      1 
HETATM 14859 O O      . HOH I 5 .   ? -16.589 -33.355 -25.606 1.00 58.29  ?  1034 HOH A O      1 
HETATM 14860 O O      . HOH I 5 .   ? 16.132  -47.788 -17.159 1.00 14.63  ?  1035 HOH A O      1 
HETATM 14861 O O      . HOH I 5 .   ? 5.713   -39.886 -31.204 1.00 27.06  ?  1036 HOH A O      1 
HETATM 14862 O O      . HOH I 5 .   ? 21.761  -10.790 -3.815  1.00 44.37  ?  1037 HOH A O      1 
HETATM 14863 O O      . HOH I 5 .   ? 22.306  -36.218 -7.290  1.00 39.95  ?  1038 HOH A O      1 
HETATM 14864 O O      . HOH I 5 .   ? -6.523  -37.666 -35.782 1.00 61.94  ?  1039 HOH A O      1 
HETATM 14865 O O      . HOH I 5 .   ? -0.912  -51.307 -5.101  1.00 58.16  ?  1040 HOH A O      1 
HETATM 14866 O O      . HOH I 5 .   ? -16.654 -12.782 -23.834 1.00 29.70  ?  1041 HOH A O      1 
HETATM 14867 O O      . HOH I 5 .   ? -20.701 -28.787 -23.691 1.00 37.29  ?  1042 HOH A O      1 
HETATM 14868 O O      . HOH I 5 .   ? 14.606  -19.073 -1.342  1.00 48.18  ?  1043 HOH A O      1 
HETATM 14869 O O      . HOH I 5 .   ? 10.015  -37.775 -6.210  1.00 61.79  ?  1044 HOH A O      1 
HETATM 14870 O O      . HOH I 5 .   ? -25.160 -25.555 -6.454  1.00 39.89  ?  1045 HOH A O      1 
HETATM 14871 O O      . HOH I 5 .   ? -22.146 -28.859 -6.611  1.00 48.25  ?  1046 HOH A O      1 
HETATM 14872 O O      . HOH I 5 .   ? 1.352   1.938   -3.579  1.00 48.86  ?  1047 HOH A O      1 
HETATM 14873 O O      . HOH I 5 .   ? -13.671 4.478   -34.283 1.00 54.53  ?  1048 HOH A O      1 
HETATM 14874 O O      . HOH I 5 .   ? -28.613 -6.537  -22.294 1.00 55.21  ?  1049 HOH A O      1 
HETATM 14875 O O      . HOH I 5 .   ? 10.888  5.966   -18.725 1.00 44.40  ?  1050 HOH A O      1 
HETATM 14876 O O      . HOH I 5 .   ? -8.995  3.313   -25.893 1.00 47.44  ?  1051 HOH A O      1 
HETATM 14877 O O      . HOH I 5 .   ? -8.177  -35.601 -24.774 1.00 53.18  ?  1052 HOH A O      1 
HETATM 14878 O O      . HOH I 5 .   ? -2.522  -47.874 -18.777 1.00 57.59  ?  1053 HOH A O      1 
HETATM 14879 O O      . HOH I 5 .   ? -5.015  -32.981 2.547   1.00 42.65  ?  1054 HOH A O      1 
HETATM 14880 O O      . HOH I 5 .   ? 0.853   -32.944 1.517   1.00 41.51  ?  1055 HOH A O      1 
HETATM 14881 O O      . HOH I 5 .   ? 6.037   -23.456 -27.637 1.00 17.13  ?  1056 HOH A O      1 
HETATM 14882 O O      . HOH I 5 .   ? 17.604  -19.841 -3.959  1.00 44.44  ?  1057 HOH A O      1 
HETATM 14883 O O      . HOH I 5 .   ? 0.244   -46.439 -1.769  1.00 40.50  ?  1058 HOH A O      1 
HETATM 14884 O O      . HOH I 5 .   ? -4.358  -17.881 1.703   1.00 57.50  ?  1059 HOH A O      1 
HETATM 14885 O O      . HOH I 5 .   ? 15.860  -9.766  -3.963  1.00 53.30  ?  1060 HOH A O      1 
HETATM 14886 O O      . HOH I 5 .   ? -4.181  -48.941 -15.461 1.00 37.88  ?  1061 HOH A O      1 
HETATM 14887 O O      . HOH I 5 .   ? 8.085   -24.918 -3.939  1.00 48.72  ?  1062 HOH A O      1 
HETATM 14888 O O      . HOH I 5 .   ? -34.227 -17.110 -12.928 1.00 52.38  ?  1063 HOH A O      1 
HETATM 14889 O O      . HOH I 5 .   ? 4.297   -37.734 -0.048  1.00 35.00  ?  1064 HOH A O      1 
HETATM 14890 O O      . HOH I 5 .   ? 17.335  -21.377 -2.036  1.00 57.39  ?  1065 HOH A O      1 
HETATM 14891 O O      . HOH I 5 .   ? -19.872 -8.545  -31.820 1.00 51.38  ?  1066 HOH A O      1 
HETATM 14892 O O      . HOH I 5 .   ? 7.746   -22.656 0.245   1.00 45.28  ?  1067 HOH A O      1 
HETATM 14893 O O      . HOH I 5 .   ? -17.869 -18.911 0.066   1.00 32.87  ?  1068 HOH A O      1 
HETATM 14894 O O      . HOH I 5 .   ? -22.791 -37.589 -14.183 1.00 58.08  ?  1069 HOH A O      1 
HETATM 14895 O O      . HOH I 5 .   ? -20.129 -16.863 -36.235 1.00 46.21  ?  1070 HOH A O      1 
HETATM 14896 O O      . HOH I 5 .   ? 26.182  -30.909 -26.598 1.00 47.16  ?  1071 HOH A O      1 
HETATM 14897 O O      . HOH I 5 .   ? 9.449   0.079   -11.414 1.00 47.53  ?  1072 HOH A O      1 
HETATM 14898 O O      . HOH I 5 .   ? 21.164  -3.818  -7.462  1.00 63.63  ?  1073 HOH A O      1 
HETATM 14899 O O      . HOH I 5 .   ? 9.623   -7.367  -5.805  1.00 23.85  ?  1074 HOH A O      1 
HETATM 14900 O O      . HOH I 5 .   ? 9.849   -47.554 -8.349  1.00 40.96  ?  1075 HOH A O      1 
HETATM 14901 O O      . HOH I 5 .   ? 9.252   7.816   -25.886 1.00 66.48  ?  1076 HOH A O      1 
HETATM 14902 O O      . HOH I 5 .   ? 31.955  -36.229 -15.221 1.00 44.16  ?  1077 HOH A O      1 
HETATM 14903 O O      . HOH I 5 .   ? -15.097 -36.851 3.840   1.00 36.68  ?  1078 HOH A O      1 
HETATM 14904 O O      . HOH I 5 .   ? 24.796  -44.280 -13.668 1.00 47.89  ?  1079 HOH A O      1 
HETATM 14905 O O      . HOH I 5 .   ? -16.745 -8.845  -44.596 1.00 51.37  ?  1080 HOH A O      1 
HETATM 14906 O O      . HOH I 5 .   ? -8.929  3.503   -20.492 1.00 39.59  ?  1081 HOH A O      1 
HETATM 14907 O O      . HOH I 5 .   ? -27.271 -12.174 -25.321 1.00 52.94  ?  1082 HOH A O      1 
HETATM 14908 O O      . HOH I 5 .   ? 3.927   -44.684 -23.597 1.00 31.34  ?  1083 HOH A O      1 
HETATM 14909 O O      . HOH I 5 .   ? -20.669 1.489   -23.996 1.00 53.86  ?  1084 HOH A O      1 
HETATM 14910 O O      . HOH I 5 .   ? -14.666 -14.241 -23.444 1.00 36.19  ?  1085 HOH A O      1 
HETATM 14911 O O      . HOH I 5 .   ? -18.922 -9.923  3.733   1.00 49.91  ?  1086 HOH A O      1 
HETATM 14912 O O      . HOH I 5 .   ? -6.887  3.598   -30.840 1.00 45.57  ?  1087 HOH A O      1 
HETATM 14913 O O      . HOH I 5 .   ? 6.753   -53.562 -10.516 1.00 54.51  ?  1088 HOH A O      1 
HETATM 14914 O O      . HOH I 5 .   ? -9.711  -23.792 -25.624 1.00 37.04  ?  1089 HOH A O      1 
HETATM 14915 O O      . HOH I 5 .   ? 0.231   -12.123 1.094   1.00 35.87  ?  1090 HOH A O      1 
HETATM 14916 O O      . HOH I 5 .   ? -13.895 -38.465 5.083   1.00 28.25  ?  1091 HOH A O      1 
HETATM 14917 O O      . HOH I 5 .   ? -31.569 -9.207  -18.263 1.00 78.01  ?  1092 HOH A O      1 
HETATM 14918 O O      . HOH I 5 .   ? -10.777 -45.883 -4.129  1.00 44.04  ?  1093 HOH A O      1 
HETATM 14919 O O      . HOH I 5 .   ? -23.150 -24.262 -0.642  1.00 44.11  ?  1094 HOH A O      1 
HETATM 14920 O O      . HOH I 5 .   ? -10.649 -4.329  -46.187 1.00 35.23  ?  1095 HOH A O      1 
HETATM 14921 O O      . HOH I 5 .   ? -6.057  -43.847 -20.386 1.00 50.54  ?  1096 HOH A O      1 
HETATM 14922 O O      . HOH I 5 .   ? -4.999  -9.391  -48.515 1.00 42.96  ?  1097 HOH A O      1 
HETATM 14923 O O      . HOH I 5 .   ? -10.916 -41.782 1.721   1.00 33.99  ?  1098 HOH A O      1 
HETATM 14924 O O      . HOH I 5 .   ? 28.622  -32.440 -10.645 1.00 44.47  ?  1099 HOH A O      1 
HETATM 14925 O O      . HOH I 5 .   ? 3.887   -39.692 -32.200 1.00 46.44  ?  1100 HOH A O      1 
HETATM 14926 O O      . HOH I 5 .   ? -19.148 1.541   -19.782 1.00 35.84  ?  1101 HOH A O      1 
HETATM 14927 O O      . HOH I 5 .   ? -19.937 -44.461 -4.346  1.00 45.59  ?  1102 HOH A O      1 
HETATM 14928 O O      . HOH I 5 .   ? -31.810 -9.956  -15.596 1.00 74.04  ?  1103 HOH A O      1 
HETATM 14929 O O      . HOH I 5 .   ? 0.030   -20.373 1.530   1.00 49.15  ?  1104 HOH A O      1 
HETATM 14930 O O      . HOH I 5 .   ? -19.901 -25.544 -26.403 1.00 55.23  ?  1105 HOH A O      1 
HETATM 14931 O O      . HOH I 5 .   ? -13.441 -19.998 -27.000 1.00 46.41  ?  1106 HOH A O      1 
HETATM 14932 O O      . HOH I 5 .   ? -25.891 -9.501  -7.569  1.00 40.65  ?  1107 HOH A O      1 
HETATM 14933 O O      . HOH I 5 .   ? -23.422 -17.751 -28.554 1.00 40.89  ?  1108 HOH A O      1 
HETATM 14934 O O      . HOH I 5 .   ? 11.023  -46.792 -6.974  1.00 56.84  ?  1109 HOH A O      1 
HETATM 14935 O O      . HOH I 5 .   ? -18.250 -19.051 -46.450 1.00 52.82  ?  1110 HOH A O      1 
HETATM 14936 O O      . HOH I 5 .   ? -14.222 -36.741 -15.523 1.00 33.84  ?  1111 HOH A O      1 
HETATM 14937 O O      . HOH I 5 .   ? -11.916 -35.619 -20.243 1.00 33.37  ?  1112 HOH A O      1 
HETATM 14938 O O      . HOH I 5 .   ? 21.017  -28.227 -1.398  1.00 30.39  ?  1113 HOH A O      1 
HETATM 14939 O O      . HOH I 5 .   ? 9.196   -41.088 -23.915 1.00 35.28  ?  1114 HOH A O      1 
HETATM 14940 O O      . HOH I 5 .   ? 6.314   -44.905 -24.424 1.00 31.62  ?  1115 HOH A O      1 
HETATM 14941 O O      . HOH I 5 .   ? -31.632 -31.404 -25.680 1.00 59.30  ?  1116 HOH A O      1 
HETATM 14942 O O      . HOH I 5 .   ? -9.121  3.842   -23.339 1.00 40.12  ?  1117 HOH A O      1 
HETATM 14943 O O      . HOH I 5 .   ? -18.564 -4.955  0.825   1.00 30.00  ?  1118 HOH A O      1 
HETATM 14944 O O      . HOH I 5 .   ? 35.305  -18.169 -23.652 1.00 48.94  ?  1119 HOH A O      1 
HETATM 14945 O O      . HOH I 5 .   ? -19.755 0.730   -29.476 1.00 47.05  ?  1120 HOH A O      1 
HETATM 14946 O O      . HOH I 5 .   ? 7.751   -25.983 -2.381  1.00 53.72  ?  1121 HOH A O      1 
HETATM 14947 O O      . HOH I 5 .   ? 9.001   8.840   -23.811 1.00 56.25  ?  1122 HOH A O      1 
HETATM 14948 O O      . HOH I 5 .   ? 7.869   -20.528 0.713   1.00 53.31  ?  1123 HOH A O      1 
HETATM 14949 O O      . HOH I 5 .   ? -4.937  -28.054 1.196   1.00 57.30  ?  1124 HOH A O      1 
HETATM 14950 O O      . HOH I 5 .   ? -14.441 0.569   -3.958  1.00 47.02  ?  1125 HOH A O      1 
HETATM 14951 O O      . HOH I 5 .   ? -4.029  -39.842 1.280   1.00 33.57  ?  1126 HOH A O      1 
HETATM 14952 O O      . HOH I 5 .   ? -24.567 -1.193  -23.276 1.00 36.35  ?  1127 HOH A O      1 
HETATM 14953 O O      . HOH I 5 .   ? -16.861 -21.147 -1.325  1.00 39.35  ?  1128 HOH A O      1 
HETATM 14954 O O      . HOH I 5 .   ? -13.097 -23.466 -29.589 1.00 36.35  ?  1129 HOH A O      1 
HETATM 14955 O O      . HOH I 5 .   ? -21.111 -16.633 -28.843 1.00 51.04  ?  1130 HOH A O      1 
HETATM 14956 O O      . HOH I 5 .   ? 0.814   -44.522 -1.126  1.00 50.48  ?  1131 HOH A O      1 
HETATM 14957 O O      . HOH I 5 .   ? -16.754 -10.470 -30.454 1.00 47.14  ?  1132 HOH A O      1 
HETATM 14958 O O      . HOH I 5 .   ? 17.421  -12.859 -3.192  1.00 41.72  ?  1133 HOH A O      1 
HETATM 14959 O O      . HOH I 5 .   ? 15.411  -5.129  -8.405  1.00 55.45  ?  1134 HOH A O      1 
HETATM 14960 O O      . HOH I 5 .   ? 7.073   -2.677  -1.216  1.00 44.81  ?  1135 HOH A O      1 
HETATM 14961 O O      . HOH I 5 .   ? 8.145   -51.877 -20.658 1.00 40.72  ?  1136 HOH A O      1 
HETATM 14962 O O      . HOH I 5 .   ? 0.817   3.414   -8.922  1.00 44.29  ?  1137 HOH A O      1 
HETATM 14963 O O      . HOH I 5 .   ? -5.470  -0.786  -10.766 1.00 42.80  ?  1138 HOH A O      1 
HETATM 14964 O O      . HOH I 5 .   ? 15.992  -16.331 -1.698  1.00 50.58  ?  1139 HOH A O      1 
HETATM 14965 O O      . HOH I 5 .   ? 11.390  -1.784  -11.624 1.00 42.24  ?  1140 HOH A O      1 
HETATM 14966 O O      . HOH I 5 .   ? 8.542   -13.622 -0.408  1.00 49.07  ?  1141 HOH A O      1 
HETATM 14967 O O      . HOH I 5 .   ? -11.590 -30.150 -32.343 1.00 30.29  ?  1142 HOH A O      1 
HETATM 14968 O O      . HOH I 5 .   ? 18.118  -23.386 -1.174  1.00 34.39  ?  1143 HOH A O      1 
HETATM 14969 O O      . HOH I 5 .   ? 23.619  -42.449 -21.605 1.00 56.99  ?  1144 HOH A O      1 
HETATM 14970 O O      . HOH I 5 .   ? -0.727  -54.163 -13.217 1.00 47.40  ?  1145 HOH A O      1 
HETATM 14971 O O      . HOH I 5 .   ? -17.030 -1.619  -0.972  1.00 48.12  ?  1146 HOH A O      1 
HETATM 14972 O O      . HOH I 5 .   ? 7.089   -47.810 -24.134 1.00 50.39  ?  1147 HOH A O      1 
HETATM 14973 O O      . HOH I 5 .   ? 21.496  -29.645 -3.729  1.00 37.83  ?  1148 HOH A O      1 
HETATM 14974 O O      . HOH I 5 .   ? 10.013  -4.986  -4.282  1.00 37.86  ?  1149 HOH A O      1 
HETATM 14975 O O      . HOH I 5 .   ? 22.954  4.746   -16.342 1.00 63.36  ?  1150 HOH A O      1 
HETATM 14976 O O      . HOH I 5 .   ? 13.253  6.531   -19.425 1.00 46.21  ?  1151 HOH A O      1 
HETATM 14977 O O      . HOH I 5 .   ? -14.871 -16.828 -26.350 1.00 62.85  ?  1152 HOH A O      1 
HETATM 14978 O O      . HOH I 5 .   ? 0.670   -40.591 1.515   1.00 48.69  ?  1153 HOH A O      1 
HETATM 14979 O O      . HOH I 5 .   ? 8.581   -9.857  -4.896  1.00 24.35  ?  1154 HOH A O      1 
HETATM 14980 O O      . HOH I 5 .   ? 4.215   -12.307 -6.787  1.00 19.87  ?  1155 HOH A O      1 
HETATM 14981 O O      . HOH I 5 .   ? -8.159  -0.940  -10.692 1.00 29.64  ?  1156 HOH A O      1 
HETATM 14982 O O      . HOH I 5 .   ? -5.484  -3.591  -4.461  1.00 42.61  ?  1157 HOH A O      1 
HETATM 14983 O O      . HOH I 5 .   ? -43.897 -23.195 -26.390 1.00 45.37  ?  1158 HOH A O      1 
HETATM 14984 O O      . HOH I 5 .   ? -20.519 2.579   -31.469 1.00 47.46  ?  1159 HOH A O      1 
HETATM 14985 O O      . HOH I 5 .   ? -42.515 -16.125 -23.939 1.00 52.54  ?  1160 HOH A O      1 
HETATM 14986 O O      . HOH I 5 .   ? -15.354 -45.369 -1.866  1.00 49.49  ?  1161 HOH A O      1 
HETATM 14987 O O      . HOH I 5 .   ? -3.808  -0.660  -3.253  1.00 65.58  ?  1162 HOH A O      1 
HETATM 14988 O O      . HOH I 5 .   ? 30.306  -40.449 -20.183 1.00 50.30  ?  1163 HOH A O      1 
HETATM 14989 O O      . HOH I 5 .   ? 23.923  -13.698 -4.294  1.00 21.28  ?  1164 HOH A O      1 
HETATM 14990 O O      . HOH I 5 .   ? -30.813 -9.275  -11.606 1.00 31.79  ?  1165 HOH A O      1 
HETATM 14991 O O      . HOH I 5 .   ? -13.694 -28.494 -27.468 1.00 36.04  ?  1166 HOH A O      1 
HETATM 14992 O O      . HOH I 5 .   ? -24.581 -37.292 -16.489 1.00 51.69  ?  1167 HOH A O      1 
HETATM 14993 O O      . HOH I 5 .   ? 12.682  -4.914  -8.125  1.00 33.16  ?  1168 HOH A O      1 
HETATM 14994 O O      . HOH I 5 .   ? -10.260 0.519   -44.557 1.00 50.67  ?  1169 HOH A O      1 
HETATM 14995 O O      . HOH I 5 .   ? -1.483  -41.209 1.027   1.00 54.86  ?  1170 HOH A O      1 
HETATM 14996 O O      . HOH I 5 .   ? -6.274  -41.450 -0.217  1.00 29.44  ?  1171 HOH A O      1 
HETATM 14997 O O      . HOH I 5 .   ? -13.073 -36.369 -36.890 1.00 62.19  ?  1172 HOH A O      1 
HETATM 14998 O O      . HOH I 5 .   ? -3.076  -41.530 -28.262 1.00 49.12  ?  1173 HOH A O      1 
HETATM 14999 O O      . HOH I 5 .   ? -17.557 -18.226 -26.175 1.00 41.86  ?  1174 HOH A O      1 
HETATM 15000 O O      . HOH I 5 .   ? -8.027  -2.957  -0.259  1.00 59.00  ?  1175 HOH A O      1 
HETATM 15001 O O      . HOH I 5 .   ? 16.806  -17.825 -2.854  1.00 68.83  ?  1176 HOH A O      1 
HETATM 15002 O O      . HOH I 5 .   ? 16.938  -6.427  -6.881  1.00 38.71  ?  1177 HOH A O      1 
HETATM 15003 O O      . HOH I 5 .   ? 19.878  -12.425 -2.751  1.00 55.35  ?  1178 HOH A O      1 
HETATM 15004 O O      . HOH I 5 .   ? -11.291 -36.794 -34.586 1.00 48.03  ?  1179 HOH A O      1 
HETATM 15005 O O      . HOH I 5 .   ? 8.670   -44.092 -23.133 1.00 33.98  ?  1180 HOH A O      1 
HETATM 15006 O O      . HOH I 5 .   ? -13.380 -18.851 0.195   1.00 44.46  ?  1181 HOH A O      1 
HETATM 15007 O O      . HOH I 5 .   ? 31.555  -18.188 -26.136 1.00 45.95  ?  1182 HOH A O      1 
HETATM 15008 O O      . HOH I 5 .   ? 32.571  -20.726 -21.883 1.00 24.66  ?  1183 HOH A O      1 
HETATM 15009 O O      . HOH I 5 .   ? 14.725  -3.383  -14.747 1.00 26.45  ?  1184 HOH A O      1 
HETATM 15010 O O      . HOH I 5 .   ? -20.761 -30.921 -20.440 1.00 41.26  ?  1185 HOH A O      1 
HETATM 15011 O O      . HOH I 5 .   ? -19.289 -32.784 -19.948 1.00 63.18  ?  1186 HOH A O      1 
HETATM 15012 O O      . HOH I 5 .   ? -17.279 -35.503 3.289   1.00 40.22  ?  1187 HOH A O      1 
HETATM 15013 O O      . HOH I 5 .   ? -4.946  -42.901 -1.349  1.00 44.10  ?  1188 HOH A O      1 
HETATM 15014 O O      . HOH I 5 .   ? -2.784  -50.643 -7.301  1.00 34.89  ?  1189 HOH A O      1 
HETATM 15015 O O      . HOH I 5 .   ? -9.359  0.183   -7.562  1.00 39.82  ?  1190 HOH A O      1 
HETATM 15016 O O      . HOH I 5 .   ? 4.845   -47.051 0.000   0.50 38.19  ?  1191 HOH A O      1 
HETATM 15017 O O      . HOH I 5 .   ? -36.649 -20.106 -14.052 1.00 51.14  ?  1192 HOH A O      1 
HETATM 15018 O O      . HOH I 5 .   ? 18.796  -14.508 -3.815  1.00 56.13  ?  1193 HOH A O      1 
HETATM 15019 O O      . HOH I 5 .   ? 14.281  -47.493 -12.320 1.00 30.31  ?  1194 HOH A O      1 
HETATM 15020 O O      . HOH I 5 .   ? 0.198   -7.680  2.012   1.00 35.39  ?  1195 HOH A O      1 
HETATM 15021 O O      . HOH I 5 .   ? -10.984 -38.095 -27.014 1.00 66.82  ?  1196 HOH A O      1 
HETATM 15022 O O      . HOH I 5 .   ? 5.846   -45.199 0.056   1.00 45.34  ?  1197 HOH A O      1 
HETATM 15023 O O      . HOH I 5 .   ? -19.929 -12.004 -27.732 1.00 44.17  ?  1198 HOH A O      1 
HETATM 15024 O O      . HOH I 5 .   ? -18.408 -23.155 -34.477 1.00 41.61  ?  1199 HOH A O      1 
HETATM 15025 O O      . HOH I 5 .   ? -15.625 -19.720 -30.394 1.00 26.96  ?  1200 HOH A O      1 
HETATM 15026 O O      . HOH I 5 .   ? -3.248  -44.105 -2.470  1.00 33.18  ?  1201 HOH A O      1 
HETATM 15027 O O      . HOH I 5 .   ? -16.255 0.638   -8.185  1.00 41.50  ?  1202 HOH A O      1 
HETATM 15028 O O      . HOH I 5 .   ? -7.763  -0.280  -4.943  1.00 48.19  ?  1203 HOH A O      1 
HETATM 15029 O O      . HOH I 5 .   ? 32.179  -35.658 -24.838 1.00 64.88  ?  1204 HOH A O      1 
HETATM 15030 O O      . HOH I 5 .   ? 18.240  -17.007 -4.388  1.00 51.56  ?  1205 HOH A O      1 
HETATM 15031 O O      . HOH I 5 .   ? -3.547  -13.698 3.291   1.00 44.57  ?  1206 HOH A O      1 
HETATM 15032 O O      . HOH I 5 .   ? 15.973  6.510   -18.984 1.00 44.67  ?  1207 HOH A O      1 
HETATM 15033 O O      . HOH I 5 .   ? 20.938  -15.980 -4.558  1.00 22.85  ?  1208 HOH A O      1 
HETATM 15034 O O      . HOH I 5 .   ? -17.211 -15.897 -32.474 1.00 24.71  ?  1209 HOH A O      1 
HETATM 15035 O O      . HOH I 5 .   ? -27.971 -8.139  -8.707  1.00 37.54  ?  1210 HOH A O      1 
HETATM 15036 O O      . HOH I 5 .   ? -16.194 -18.709 -32.650 1.00 27.17  ?  1211 HOH A O      1 
HETATM 15037 O O      . HOH I 5 .   ? -11.528 -44.333 0.221   1.00 35.98  ?  1212 HOH A O      1 
HETATM 15038 O O      . HOH I 5 .   ? -3.241  -44.945 -21.093 1.00 46.67  ?  1213 HOH A O      1 
HETATM 15039 O O      . HOH I 5 .   ? -33.243 -31.752 -19.407 1.00 50.28  ?  1214 HOH A O      1 
HETATM 15040 O O      . HOH I 5 .   ? -25.282 -15.760 -28.432 1.00 43.24  ?  1215 HOH A O      1 
HETATM 15041 O O      . HOH I 5 .   ? -19.633 -35.554 1.423   1.00 45.14  ?  1216 HOH A O      1 
HETATM 15042 O O      . HOH I 5 .   ? 5.231   -39.965 1.209   1.00 50.30  ?  1217 HOH A O      1 
HETATM 15043 O O      . HOH I 5 .   ? -12.511 -36.426 -18.103 1.00 43.09  ?  1218 HOH A O      1 
HETATM 15044 O O      . HOH I 5 .   ? 32.948  -38.086 -16.936 1.00 48.56  ?  1219 HOH A O      1 
HETATM 15045 O O      . HOH I 5 .   ? -19.830 -16.397 -33.470 1.00 42.78  ?  1220 HOH A O      1 
HETATM 15046 O O      . HOH I 5 .   ? -17.719 -20.482 -34.315 1.00 25.59  ?  1221 HOH A O      1 
HETATM 15047 O O      . HOH I 5 .   ? -19.456 -0.673  -1.657  1.00 60.31  ?  1222 HOH A O      1 
HETATM 15048 O O      . HOH I 5 .   ? -32.090 -33.263 -18.110 1.00 51.47  ?  1223 HOH A O      1 
HETATM 15049 O O      . HOH I 5 .   ? -16.081 -15.199 -27.678 1.00 41.42  ?  1224 HOH A O      1 
HETATM 15050 O O      . HOH I 5 .   ? -18.880 1.383   -3.614  1.00 51.66  ?  1225 HOH A O      1 
HETATM 15051 O O      . HOH I 5 .   ? -19.823 -13.786 -29.725 1.00 46.74  ?  1226 HOH A O      1 
HETATM 15052 O O      . HOH I 5 .   ? -16.386 -18.053 -28.240 1.00 47.12  ?  1227 HOH A O      1 
HETATM 15053 O O      . HOH J 5 .   ? 28.851  -0.596  -11.942 1.00 59.77  ?  601  HOH B O      1 
HETATM 15054 O O      . HOH J 5 .   ? -3.130  -13.061 -33.965 1.00 136.85 ?  602  HOH B O      1 
HETATM 15055 O O      . HOH J 5 .   ? -0.961  -30.192 -51.262 1.00 38.34  ?  603  HOH B O      1 
HETATM 15056 O O      . HOH J 5 .   ? 13.718  -16.052 -32.805 1.00 17.91  ?  604  HOH B O      1 
HETATM 15057 O O      . HOH J 5 .   ? -14.371 -31.319 -45.064 1.00 45.17  ?  605  HOH B O      1 
HETATM 15058 O O      . HOH J 5 .   ? 45.334  -34.018 -41.815 1.00 52.71  ?  606  HOH B O      1 
HETATM 15059 O O      . HOH J 5 .   ? 20.490  -14.396 -15.397 1.00 75.97  ?  607  HOH B O      1 
HETATM 15060 O O      . HOH J 5 .   ? -3.313  -28.395 -51.502 1.00 30.54  ?  608  HOH B O      1 
HETATM 15061 O O      . HOH J 5 .   ? 9.082   5.739   -33.075 1.00 29.22  ?  609  HOH B O      1 
HETATM 15062 O O      . HOH J 5 .   ? 16.905  6.471   -40.155 1.00 43.66  ?  610  HOH B O      1 
HETATM 15063 O O      . HOH J 5 .   ? 38.795  -17.080 -52.837 1.00 56.97  ?  611  HOH B O      1 
HETATM 15064 O O      . HOH J 5 .   ? 4.182   -16.828 -52.487 1.00 48.66  ?  612  HOH B O      1 
HETATM 15065 O O      . HOH J 5 .   ? 12.134  -45.353 -42.166 1.00 56.17  ?  613  HOH B O      1 
HETATM 15066 O O      . HOH J 5 .   ? 22.013  0.656   -51.571 1.00 58.06  ?  614  HOH B O      1 
HETATM 15067 O O      . HOH J 5 .   ? -0.425  -0.604  -21.239 1.00 58.71  ?  615  HOH B O      1 
HETATM 15068 O O      . HOH J 5 .   ? 26.547  -26.524 -50.148 1.00 18.92  ?  616  HOH B O      1 
HETATM 15069 O O      . HOH J 5 .   ? 32.986  -15.551 -50.047 1.00 60.53  ?  617  HOH B O      1 
HETATM 15070 O O      . HOH J 5 .   ? 14.155  -23.708 -62.876 1.00 39.30  ?  618  HOH B O      1 
HETATM 15071 O O      . HOH J 5 .   ? -3.750  -14.744 -51.181 1.00 33.97  ?  619  HOH B O      1 
HETATM 15072 O O      . HOH J 5 .   ? 31.113  -1.041  -55.290 1.00 48.68  ?  620  HOH B O      1 
HETATM 15073 O O      . HOH J 5 .   ? 32.765  -7.395  -54.256 1.00 58.40  ?  621  HOH B O      1 
HETATM 15074 O O      . HOH J 5 .   ? 5.602   -10.093 -28.710 1.00 17.68  ?  622  HOH B O      1 
HETATM 15075 O O      . HOH J 5 .   ? 13.311  -16.912 -29.204 1.00 15.70  ?  623  HOH B O      1 
HETATM 15076 O O      . HOH J 5 .   ? 37.853  -28.285 -43.075 1.00 32.35  ?  624  HOH B O      1 
HETATM 15077 O O      . HOH J 5 .   ? 28.630  -18.058 -6.957  1.00 42.97  ?  625  HOH B O      1 
HETATM 15078 O O      . HOH J 5 .   ? 18.105  -21.368 -56.568 1.00 29.48  ?  626  HOH B O      1 
HETATM 15079 O O      . HOH J 5 .   ? 4.496   -15.705 -55.660 1.00 46.46  ?  627  HOH B O      1 
HETATM 15080 O O      . HOH J 5 .   ? 27.788  -14.439 -29.562 1.00 35.36  ?  628  HOH B O      1 
HETATM 15081 O O      . HOH J 5 .   ? 1.773   -30.531 -53.896 1.00 45.75  ?  629  HOH B O      1 
HETATM 15082 O O      . HOH J 5 .   ? 26.076  -34.479 -28.319 1.00 47.80  ?  630  HOH B O      1 
HETATM 15083 O O      . HOH J 5 .   ? 11.265  -38.886 -28.591 1.00 35.26  ?  631  HOH B O      1 
HETATM 15084 O O      . HOH J 5 .   ? 13.292  -6.179  -46.888 1.00 32.53  ?  632  HOH B O      1 
HETATM 15085 O O      . HOH J 5 .   ? 38.088  -6.229  -50.931 1.00 44.80  ?  633  HOH B O      1 
HETATM 15086 O O      . HOH J 5 .   ? 25.153  -36.313 -49.333 1.00 35.01  ?  634  HOH B O      1 
HETATM 15087 O O      . HOH J 5 .   ? 16.215  5.107   -36.005 1.00 25.02  ?  635  HOH B O      1 
HETATM 15088 O O      . HOH J 5 .   ? 9.973   3.266   -37.216 1.00 40.42  ?  636  HOH B O      1 
HETATM 15089 O O      . HOH J 5 .   ? 44.052  -20.740 -28.761 1.00 23.60  ?  637  HOH B O      1 
HETATM 15090 O O      . HOH J 5 .   ? 26.195  -21.435 -28.412 1.00 41.85  ?  638  HOH B O      1 
HETATM 15091 O O      . HOH J 5 .   ? 16.154  -21.958 -30.574 1.00 16.19  ?  639  HOH B O      1 
HETATM 15092 O O      . HOH J 5 .   ? 36.237  -19.633 -52.110 1.00 30.00  ?  640  HOH B O      1 
HETATM 15093 O O      . HOH J 5 .   ? 39.432  -26.702 -49.532 1.00 47.80  ?  641  HOH B O      1 
HETATM 15094 O O      . HOH J 5 .   ? 23.912  1.033   -20.939 1.00 38.44  ?  642  HOH B O      1 
HETATM 15095 O O      . HOH J 5 .   ? -2.434  -44.001 -48.161 1.00 42.42  ?  643  HOH B O      1 
HETATM 15096 O O      . HOH J 5 .   ? -6.287  3.753   -26.314 1.00 35.90  ?  644  HOH B O      1 
HETATM 15097 O O      . HOH J 5 .   ? 2.548   -34.626 -39.608 1.00 24.55  ?  645  HOH B O      1 
HETATM 15098 O O      . HOH J 5 .   ? -11.518 -32.292 -47.484 1.00 33.56  ?  646  HOH B O      1 
HETATM 15099 O O      . HOH J 5 .   ? 8.845   -8.419  -51.435 1.00 28.57  ?  647  HOH B O      1 
HETATM 15100 O O      . HOH J 5 .   ? 21.590  -0.549  -26.706 1.00 32.47  ?  648  HOH B O      1 
HETATM 15101 O O      . HOH J 5 .   ? 46.689  -9.605  -32.184 1.00 47.50  ?  649  HOH B O      1 
HETATM 15102 O O      . HOH J 5 .   ? 46.174  -16.534 -26.160 1.00 50.25  ?  650  HOH B O      1 
HETATM 15103 O O      . HOH J 5 .   ? 11.355  -11.414 -33.833 1.00 16.88  ?  651  HOH B O      1 
HETATM 15104 O O      . HOH J 5 .   ? -1.163  -13.307 -51.748 1.00 37.95  ?  652  HOH B O      1 
HETATM 15105 O O      . HOH J 5 .   ? -10.597 -16.562 -47.897 1.00 26.83  ?  653  HOH B O      1 
HETATM 15106 O O      . HOH J 5 .   ? 27.834  -15.025 -31.276 1.00 46.59  ?  654  HOH B O      1 
HETATM 15107 O O      . HOH J 5 .   ? 32.628  -3.707  -13.000 1.00 21.05  ?  655  HOH B O      1 
HETATM 15108 O O      . HOH J 5 .   ? 43.724  -22.177 -48.003 1.00 42.06  ?  656  HOH B O      1 
HETATM 15109 O O      . HOH J 5 .   ? 23.727  0.554   -55.688 1.00 50.49  ?  657  HOH B O      1 
HETATM 15110 O O      . HOH J 5 .   ? 26.899  0.997   -39.457 1.00 22.63  ?  658  HOH B O      1 
HETATM 15111 O O      . HOH J 5 .   ? -6.722  0.995   -32.210 1.00 33.37  ?  659  HOH B O      1 
HETATM 15112 O O      . HOH J 5 .   ? -0.663  -37.060 -53.656 1.00 19.13  ?  660  HOH B O      1 
HETATM 15113 O O      . HOH J 5 .   ? 36.101  -28.280 -32.527 1.00 35.50  ?  661  HOH B O      1 
HETATM 15114 O O      . HOH J 5 .   ? 34.888  -28.779 -17.388 1.00 40.59  ?  662  HOH B O      1 
HETATM 15115 O O      . HOH J 5 .   ? 47.710  -10.989 -38.100 1.00 36.22  ?  663  HOH B O      1 
HETATM 15116 O O      . HOH J 5 .   ? 49.293  -17.845 -27.990 1.00 52.83  ?  664  HOH B O      1 
HETATM 15117 O O      . HOH J 5 .   ? 17.258  -12.132 -47.210 1.00 16.88  ?  665  HOH B O      1 
HETATM 15118 O O      . HOH J 5 .   ? 17.460  -26.119 -42.827 1.00 14.92  ?  666  HOH B O      1 
HETATM 15119 O O      . HOH J 5 .   ? 31.940  1.824   -36.445 1.00 33.20  ?  667  HOH B O      1 
HETATM 15120 O O      . HOH J 5 .   ? 2.452   -42.302 -41.873 1.00 24.18  ?  668  HOH B O      1 
HETATM 15121 O O      . HOH J 5 .   ? 52.093  -19.873 -38.799 1.00 50.64  ?  669  HOH B O      1 
HETATM 15122 O O      . HOH J 5 .   ? 22.626  -32.734 -26.101 1.00 16.70  ?  670  HOH B O      1 
HETATM 15123 O O      . HOH J 5 .   ? 17.047  -29.919 -40.027 1.00 21.94  ?  671  HOH B O      1 
HETATM 15124 O O      . HOH J 5 .   ? 19.148  -32.105 -49.006 1.00 15.72  ?  672  HOH B O      1 
HETATM 15125 O O      . HOH J 5 .   ? -10.937 -21.584 -50.996 1.00 49.35  ?  673  HOH B O      1 
HETATM 15126 O O      . HOH J 5 .   ? 33.005  -14.398 -11.834 1.00 28.17  ?  674  HOH B O      1 
HETATM 15127 O O      . HOH J 5 .   ? 1.284   -3.049  -46.739 1.00 49.43  ?  675  HOH B O      1 
HETATM 15128 O O      . HOH J 5 .   ? 1.253   1.413   -32.082 1.00 53.00  ?  676  HOH B O      1 
HETATM 15129 O O      . HOH J 5 .   ? -6.075  -5.980  -45.066 1.00 18.00  ?  677  HOH B O      1 
HETATM 15130 O O      . HOH J 5 .   ? -10.683 -11.494 -21.269 1.00 14.00  ?  678  HOH B O      1 
HETATM 15131 O O      . HOH J 5 .   ? -18.764 -24.683 -39.172 1.00 28.34  ?  679  HOH B O      1 
HETATM 15132 O O      . HOH J 5 .   ? 33.428  -24.168 -34.539 1.00 18.59  ?  680  HOH B O      1 
HETATM 15133 O O      . HOH J 5 .   ? 9.506   -25.835 -29.577 1.00 17.13  ?  681  HOH B O      1 
HETATM 15134 O O      . HOH J 5 .   ? 27.865  -19.976 -53.008 1.00 51.78  ?  682  HOH B O      1 
HETATM 15135 O O      . HOH J 5 .   ? 3.919   -8.202  -52.505 1.00 34.11  ?  683  HOH B O      1 
HETATM 15136 O O      . HOH J 5 .   ? 10.121  -21.139 -27.681 1.00 21.75  ?  684  HOH B O      1 
HETATM 15137 O O      . HOH J 5 .   ? 9.605   -43.989 -41.049 1.00 31.09  ?  685  HOH B O      1 
HETATM 15138 O O      . HOH J 5 .   ? -13.387 -21.727 -48.409 1.00 38.84  ?  686  HOH B O      1 
HETATM 15139 O O      . HOH J 5 .   ? 35.296  -19.580 -27.813 1.00 30.84  ?  687  HOH B O      1 
HETATM 15140 O O      . HOH J 5 .   ? 6.966   -30.159 -29.242 1.00 12.77  ?  688  HOH B O      1 
HETATM 15141 O O      . HOH J 5 .   ? 34.768  -8.373  -6.905  1.00 30.01  ?  689  HOH B O      1 
HETATM 15142 O O      . HOH J 5 .   ? 21.179  -22.612 -57.912 1.00 43.90  ?  690  HOH B O      1 
HETATM 15143 O O      . HOH J 5 .   ? 28.318  -1.092  -50.212 1.00 29.81  ?  691  HOH B O      1 
HETATM 15144 O O      . HOH J 5 .   ? 14.744  -40.707 -31.605 1.00 36.41  ?  692  HOH B O      1 
HETATM 15145 O O      . HOH J 5 .   ? 24.557  -18.419 -53.023 1.00 22.93  ?  693  HOH B O      1 
HETATM 15146 O O      . HOH J 5 .   ? 40.466  -5.493  -43.636 1.00 26.19  ?  694  HOH B O      1 
HETATM 15147 O O      . HOH J 5 .   ? 30.478  -19.881 -19.904 1.00 20.53  ?  695  HOH B O      1 
HETATM 15148 O O      . HOH J 5 .   ? 33.222  -11.530 -7.674  1.00 24.66  ?  696  HOH B O      1 
HETATM 15149 O O      . HOH J 5 .   ? 13.919  -32.285 -59.687 1.00 21.55  ?  697  HOH B O      1 
HETATM 15150 O O      . HOH J 5 .   ? 20.141  -20.158 -34.041 1.00 45.74  ?  698  HOH B O      1 
HETATM 15151 O O      . HOH J 5 .   ? 25.313  -30.180 -32.419 1.00 17.38  ?  699  HOH B O      1 
HETATM 15152 O O      . HOH J 5 .   ? 46.101  -19.052 -26.446 1.00 32.91  ?  700  HOH B O      1 
HETATM 15153 O O      . HOH J 5 .   ? 35.347  -7.454  -14.644 1.00 24.10  ?  701  HOH B O      1 
HETATM 15154 O O      . HOH J 5 .   ? 27.075  -17.218 -52.379 1.00 38.05  ?  702  HOH B O      1 
HETATM 15155 O O      . HOH J 5 .   ? -11.042 -27.144 -36.450 1.00 18.20  ?  703  HOH B O      1 
HETATM 15156 O O      . HOH J 5 .   ? -2.459  1.504   -31.717 1.00 35.95  ?  704  HOH B O      1 
HETATM 15157 O O      . HOH J 5 .   ? 23.786  -21.233 -12.592 1.00 14.59  ?  705  HOH B O      1 
HETATM 15158 O O      . HOH J 5 .   ? -12.489 -33.801 -43.371 1.00 33.34  ?  706  HOH B O      1 
HETATM 15159 O O      . HOH J 5 .   ? 44.101  -15.664 -48.746 1.00 40.79  ?  707  HOH B O      1 
HETATM 15160 O O      . HOH J 5 .   ? 4.235   -47.660 -49.209 1.00 48.07  ?  708  HOH B O      1 
HETATM 15161 O O      . HOH J 5 .   ? 7.233   -46.385 -52.892 1.00 31.14  ?  709  HOH B O      1 
HETATM 15162 O O      . HOH J 5 .   ? 10.399  -4.716  -50.988 1.00 47.71  ?  710  HOH B O      1 
HETATM 15163 O O      . HOH J 5 .   ? 12.112  -26.460 -59.635 1.00 23.68  ?  711  HOH B O      1 
HETATM 15164 O O      . HOH J 5 .   ? 11.318  -49.150 -47.796 1.00 47.66  ?  712  HOH B O      1 
HETATM 15165 O O      . HOH J 5 .   ? 35.091  -6.346  -19.265 1.00 20.18  ?  713  HOH B O      1 
HETATM 15166 O O      . HOH J 5 .   ? 26.431  -20.918 -7.561  1.00 30.43  ?  714  HOH B O      1 
HETATM 15167 O O      . HOH J 5 .   ? -16.050 -27.290 -44.753 1.00 22.83  ?  715  HOH B O      1 
HETATM 15168 O O      . HOH J 5 .   ? 18.945  -12.199 -39.851 1.00 15.38  ?  716  HOH B O      1 
HETATM 15169 O O      . HOH J 5 .   ? 5.923   -8.165  -26.784 1.00 18.00  ?  717  HOH B O      1 
HETATM 15170 O O      . HOH J 5 .   ? 20.312  -35.301 -37.046 1.00 34.48  ?  718  HOH B O      1 
HETATM 15171 O O      . HOH J 5 .   ? 34.407  -13.722 -30.778 1.00 19.34  ?  719  HOH B O      1 
HETATM 15172 O O      . HOH J 5 .   ? 14.080  -43.181 -44.768 1.00 35.93  ?  720  HOH B O      1 
HETATM 15173 O O      . HOH J 5 .   ? 39.245  -28.860 -33.455 1.00 26.62  ?  721  HOH B O      1 
HETATM 15174 O O      . HOH J 5 .   ? -2.165  -31.720 -53.380 1.00 24.88  ?  722  HOH B O      1 
HETATM 15175 O O      . HOH J 5 .   ? 4.915   -47.046 -46.729 1.00 40.91  ?  723  HOH B O      1 
HETATM 15176 O O      . HOH J 5 .   ? 34.501  -14.921 -8.674  1.00 36.32  ?  724  HOH B O      1 
HETATM 15177 O O      . HOH J 5 .   ? 37.858  0.527   -41.436 1.00 22.84  ?  725  HOH B O      1 
HETATM 15178 O O      . HOH J 5 .   ? -5.962  -17.296 -49.647 1.00 20.66  ?  726  HOH B O      1 
HETATM 15179 O O      . HOH J 5 .   ? 28.285  -11.671 -5.869  1.00 16.42  ?  727  HOH B O      1 
HETATM 15180 O O      . HOH J 5 .   ? 1.903   -44.109 -53.012 1.00 47.37  ?  728  HOH B O      1 
HETATM 15181 O O      . HOH J 5 .   ? 16.022  -28.874 -42.903 1.00 14.36  ?  729  HOH B O      1 
HETATM 15182 O O      . HOH J 5 .   ? 20.819  -36.767 -34.036 1.00 44.57  ?  730  HOH B O      1 
HETATM 15183 O O      . HOH J 5 .   ? 3.975   -12.342 -28.531 1.00 21.71  ?  731  HOH B O      1 
HETATM 15184 O O      . HOH J 5 .   ? 0.532   -46.510 -46.644 1.00 33.11  ?  732  HOH B O      1 
HETATM 15185 O O      . HOH J 5 .   ? 29.290  -4.297  -53.566 1.00 46.23  ?  733  HOH B O      1 
HETATM 15186 O O      . HOH J 5 .   ? -1.998  -40.945 -47.972 1.00 19.93  ?  734  HOH B O      1 
HETATM 15187 O O      . HOH J 5 .   ? 18.907  -19.923 -41.978 1.00 17.12  ?  735  HOH B O      1 
HETATM 15188 O O      . HOH J 5 .   ? 5.139   -19.491 -52.627 1.00 19.55  ?  736  HOH B O      1 
HETATM 15189 O O      . HOH J 5 .   ? 25.192  1.642   -43.541 1.00 31.58  ?  737  HOH B O      1 
HETATM 15190 O O      . HOH J 5 .   ? 18.480  -39.018 -47.603 1.00 22.71  ?  738  HOH B O      1 
HETATM 15191 O O      . HOH J 5 .   ? -5.304  -26.892 -51.212 1.00 25.11  ?  739  HOH B O      1 
HETATM 15192 O O      . HOH J 5 .   ? -5.967  -7.901  -28.853 1.00 40.48  ?  740  HOH B O      1 
HETATM 15193 O O      . HOH J 5 .   ? 27.935  1.242   -34.130 1.00 48.35  ?  741  HOH B O      1 
HETATM 15194 O O      . HOH J 5 .   ? 18.952  -28.150 -60.600 1.00 27.05  ?  742  HOH B O      1 
HETATM 15195 O O      . HOH J 5 .   ? 24.907  -9.807  -52.045 1.00 36.46  ?  743  HOH B O      1 
HETATM 15196 O O      . HOH J 5 .   ? 11.826  -39.992 -36.251 1.00 22.23  ?  744  HOH B O      1 
HETATM 15197 O O      . HOH J 5 .   ? 24.101  -33.694 -37.423 1.00 27.57  ?  745  HOH B O      1 
HETATM 15198 O O      . HOH J 5 .   ? 32.666  -15.136 -47.307 1.00 36.44  ?  746  HOH B O      1 
HETATM 15199 O O      . HOH J 5 .   ? 3.572   2.507   -31.669 1.00 25.42  ?  747  HOH B O      1 
HETATM 15200 O O      . HOH J 5 .   ? 32.505  2.127   -23.337 1.00 43.90  ?  748  HOH B O      1 
HETATM 15201 O O      . HOH J 5 .   ? 2.861   -13.121 -30.799 1.00 14.95  ?  749  HOH B O      1 
HETATM 15202 O O      . HOH J 5 .   ? -1.861  -10.404 -27.757 1.00 16.39  ?  750  HOH B O      1 
HETATM 15203 O O      . HOH J 5 .   ? 9.399   -16.648 -53.089 1.00 36.68  ?  751  HOH B O      1 
HETATM 15204 O O      . HOH J 5 .   ? 19.832  -21.384 -38.149 1.00 15.86  ?  752  HOH B O      1 
HETATM 15205 O O      . HOH J 5 .   ? 5.236   -37.728 -33.495 1.00 34.23  ?  753  HOH B O      1 
HETATM 15206 O O      . HOH J 5 .   ? 25.306  -34.179 -47.612 1.00 26.26  ?  754  HOH B O      1 
HETATM 15207 O O      . HOH J 5 .   ? 22.166  -40.109 -22.665 1.00 27.77  ?  755  HOH B O      1 
HETATM 15208 O O      . HOH J 5 .   ? 1.046   -32.951 -47.414 1.00 13.98  ?  756  HOH B O      1 
HETATM 15209 O O      . HOH J 5 .   ? -8.028  -27.673 -51.270 1.00 23.00  ?  757  HOH B O      1 
HETATM 15210 O O      . HOH J 5 .   ? 0.372   6.663   -26.788 1.00 28.44  ?  758  HOH B O      1 
HETATM 15211 O O      . HOH J 5 .   ? 16.545  -18.804 -42.541 1.00 16.85  ?  759  HOH B O      1 
HETATM 15212 O O      . HOH J 5 .   ? -6.264  -41.397 -47.891 1.00 35.49  ?  760  HOH B O      1 
HETATM 15213 O O      . HOH J 5 .   ? -8.812  -14.607 -47.462 1.00 28.17  ?  761  HOH B O      1 
HETATM 15214 O O      . HOH J 5 .   ? -3.919  -19.430 -22.340 1.00 40.25  ?  762  HOH B O      1 
HETATM 15215 O O      . HOH J 5 .   ? 22.527  -5.293  -18.050 1.00 18.69  ?  763  HOH B O      1 
HETATM 15216 O O      . HOH J 5 .   ? 35.982  0.956   -23.181 1.00 42.52  ?  764  HOH B O      1 
HETATM 15217 O O      . HOH J 5 .   ? 15.141  -38.567 -38.240 1.00 27.89  ?  765  HOH B O      1 
HETATM 15218 O O      . HOH J 5 .   ? 18.373  -34.572 -49.863 1.00 17.26  ?  766  HOH B O      1 
HETATM 15219 O O      . HOH J 5 .   ? 5.675   -14.842 -52.911 1.00 53.42  ?  767  HOH B O      1 
HETATM 15220 O O      . HOH J 5 .   ? -4.866  1.584   -39.445 1.00 29.79  ?  768  HOH B O      1 
HETATM 15221 O O      . HOH J 5 .   ? 43.621  -12.438 -30.769 1.00 36.65  ?  769  HOH B O      1 
HETATM 15222 O O      . HOH J 5 .   ? 27.568  -25.333 -37.673 1.00 17.81  ?  770  HOH B O      1 
HETATM 15223 O O      . HOH J 5 .   ? 0.153   1.360   -34.933 1.00 34.20  ?  771  HOH B O      1 
HETATM 15224 O O      . HOH J 5 .   ? -3.783  -15.106 -32.475 1.00 14.89  ?  772  HOH B O      1 
HETATM 15225 O O      . HOH J 5 .   ? 24.665  -22.974 -14.480 1.00 13.63  ?  773  HOH B O      1 
HETATM 15226 O O      . HOH J 5 .   ? 15.037  -12.701 -39.971 1.00 14.71  ?  774  HOH B O      1 
HETATM 15227 O O      . HOH J 5 .   ? 44.634  -7.734  -39.462 1.00 34.72  ?  775  HOH B O      1 
HETATM 15228 O O      . HOH J 5 .   ? 32.435  -20.216 -51.485 1.00 66.26  ?  776  HOH B O      1 
HETATM 15229 O O      . HOH J 5 .   ? 21.348  -24.768 -40.055 1.00 13.81  ?  777  HOH B O      1 
HETATM 15230 O O      . HOH J 5 .   ? 34.658  -28.531 -51.876 1.00 29.64  ?  778  HOH B O      1 
HETATM 15231 O O      . HOH J 5 .   ? -10.237 -8.571  -35.622 1.00 16.42  ?  779  HOH B O      1 
HETATM 15232 O O      . HOH J 5 .   ? 35.390  -30.775 -16.703 1.00 69.44  ?  780  HOH B O      1 
HETATM 15233 O O      . HOH J 5 .   ? 22.333  -10.614 -52.277 1.00 26.71  ?  781  HOH B O      1 
HETATM 15234 O O      . HOH J 5 .   ? 17.583  -18.396 -18.871 1.00 12.95  ?  782  HOH B O      1 
HETATM 15235 O O      . HOH J 5 .   ? 23.536  -21.200 -16.296 1.00 13.86  ?  783  HOH B O      1 
HETATM 15236 O O      . HOH J 5 .   ? -13.716 -26.468 -32.897 1.00 33.83  ?  784  HOH B O      1 
HETATM 15237 O O      . HOH J 5 .   ? 36.505  -8.494  -20.194 1.00 25.38  ?  785  HOH B O      1 
HETATM 15238 O O      . HOH J 5 .   ? 30.592  -33.395 -12.160 1.00 34.50  ?  786  HOH B O      1 
HETATM 15239 O O      . HOH J 5 .   ? -7.462  -7.748  -28.773 1.00 20.83  ?  787  HOH B O      1 
HETATM 15240 O O      . HOH J 5 .   ? 29.895  3.519   -39.315 1.00 47.51  ?  788  HOH B O      1 
HETATM 15241 O O      . HOH J 5 .   ? 25.036  -36.370 -59.373 1.00 28.10  ?  789  HOH B O      1 
HETATM 15242 O O      . HOH J 5 .   ? 41.963  -7.861  -25.303 1.00 43.00  ?  790  HOH B O      1 
HETATM 15243 O O      . HOH J 5 .   ? -15.320 -12.350 -30.936 1.00 31.49  ?  791  HOH B O      1 
HETATM 15244 O O      . HOH J 5 .   ? 9.690   3.485   -43.999 1.00 32.92  ?  792  HOH B O      1 
HETATM 15245 O O      . HOH J 5 .   ? 27.158  -35.899 -25.554 1.00 36.93  ?  793  HOH B O      1 
HETATM 15246 O O      . HOH J 5 .   ? 15.779  -7.714  -40.475 1.00 16.11  ?  794  HOH B O      1 
HETATM 15247 O O      . HOH J 5 .   ? 5.089   0.973   -34.378 1.00 24.71  ?  795  HOH B O      1 
HETATM 15248 O O      . HOH J 5 .   ? 29.789  -19.167 -50.936 1.00 26.54  ?  796  HOH B O      1 
HETATM 15249 O O      . HOH J 5 .   ? 5.542   -36.312 -38.611 1.00 25.08  ?  797  HOH B O      1 
HETATM 15250 O O      . HOH J 5 .   ? 11.939  -41.489 -24.626 1.00 46.42  ?  798  HOH B O      1 
HETATM 15251 O O      . HOH J 5 .   ? -3.414  -13.752 -27.783 1.00 13.97  ?  799  HOH B O      1 
HETATM 15252 O O      . HOH J 5 .   ? -10.091 -40.699 -47.117 1.00 27.42  ?  800  HOH B O      1 
HETATM 15253 O O      . HOH J 5 .   ? 28.583  1.381   -28.207 1.00 31.23  ?  801  HOH B O      1 
HETATM 15254 O O      . HOH J 5 .   ? 40.939  -15.151 -25.725 1.00 41.71  ?  802  HOH B O      1 
HETATM 15255 O O      . HOH J 5 .   ? 22.677  -25.089 -47.882 1.00 15.32  ?  803  HOH B O      1 
HETATM 15256 O O      . HOH J 5 .   ? 8.102   -42.443 -58.957 1.00 37.28  ?  804  HOH B O      1 
HETATM 15257 O O      . HOH J 5 .   ? -4.552  -7.356  -28.556 1.00 20.30  ?  805  HOH B O      1 
HETATM 15258 O O      . HOH J 5 .   ? 28.244  3.534   -34.596 1.00 50.98  ?  806  HOH B O      1 
HETATM 15259 O O      . HOH J 5 .   ? 12.365  -14.042 -40.175 1.00 13.85  ?  807  HOH B O      1 
HETATM 15260 O O      . HOH J 5 .   ? 38.020  -28.838 -39.255 1.00 28.38  ?  808  HOH B O      1 
HETATM 15261 O O      . HOH J 5 .   ? 1.014   -22.681 -51.454 1.00 31.65  ?  809  HOH B O      1 
HETATM 15262 O O      . HOH J 5 .   ? 35.474  -2.576  -30.262 1.00 24.30  ?  810  HOH B O      1 
HETATM 15263 O O      . HOH J 5 .   ? 13.996  -45.979 -52.321 1.00 24.50  ?  811  HOH B O      1 
HETATM 15264 O O      . HOH J 5 .   ? 3.713   -19.878 -33.448 1.00 12.39  ?  812  HOH B O      1 
HETATM 15265 O O      . HOH J 5 .   ? 31.832  3.396   -41.100 1.00 23.05  ?  813  HOH B O      1 
HETATM 15266 O O      . HOH J 5 .   ? 42.194  -15.368 -52.166 1.00 46.30  ?  814  HOH B O      1 
HETATM 15267 O O      . HOH J 5 .   ? 13.470  -39.982 -60.989 1.00 46.40  ?  815  HOH B O      1 
HETATM 15268 O O      . HOH J 5 .   ? 28.542  -0.353  -19.381 1.00 34.25  ?  816  HOH B O      1 
HETATM 15269 O O      . HOH J 5 .   ? -2.417  -4.743  -21.211 1.00 15.19  ?  817  HOH B O      1 
HETATM 15270 O O      . HOH J 5 .   ? 48.024  -25.462 -30.622 1.00 41.65  ?  818  HOH B O      1 
HETATM 15271 O O      . HOH J 5 .   ? -6.856  -19.791 -50.055 1.00 20.97  ?  819  HOH B O      1 
HETATM 15272 O O      . HOH J 5 .   ? 23.994  -25.869 -27.406 1.00 29.96  ?  820  HOH B O      1 
HETATM 15273 O O      . HOH J 5 .   ? 37.109  -9.013  -10.710 1.00 39.67  ?  821  HOH B O      1 
HETATM 15274 O O      . HOH J 5 .   ? -15.693 -30.454 -34.006 1.00 27.14  ?  822  HOH B O      1 
HETATM 15275 O O      . HOH J 5 .   ? 38.945  -5.842  -46.031 1.00 29.77  ?  823  HOH B O      1 
HETATM 15276 O O      . HOH J 5 .   ? 20.633  -38.979 -30.254 1.00 36.73  ?  824  HOH B O      1 
HETATM 15277 O O      . HOH J 5 .   ? 20.832  1.318   -49.197 1.00 35.51  ?  825  HOH B O      1 
HETATM 15278 O O      . HOH J 5 .   ? 39.910  -0.929  -40.566 1.00 29.25  ?  826  HOH B O      1 
HETATM 15279 O O      . HOH J 5 .   ? -1.143  -19.302 -54.584 1.00 48.44  ?  827  HOH B O      1 
HETATM 15280 O O      . HOH J 5 .   ? 33.399  -24.864 -18.982 1.00 33.99  ?  828  HOH B O      1 
HETATM 15281 O O      . HOH J 5 .   ? 17.792  -41.387 -48.920 1.00 25.87  ?  829  HOH B O      1 
HETATM 15282 O O      . HOH J 5 .   ? -5.858  3.094   -22.609 1.00 27.58  ?  830  HOH B O      1 
HETATM 15283 O O      . HOH J 5 .   ? 21.267  4.840   -28.689 1.00 45.07  ?  831  HOH B O      1 
HETATM 15284 O O      . HOH J 5 .   ? 21.715  1.673   -46.465 1.00 41.95  ?  832  HOH B O      1 
HETATM 15285 O O      . HOH J 5 .   ? 39.819  -1.542  -47.892 1.00 43.75  ?  833  HOH B O      1 
HETATM 15286 O O      . HOH J 5 .   ? 6.087   -0.824  -40.993 1.00 22.47  ?  834  HOH B O      1 
HETATM 15287 O O      . HOH J 5 .   ? -7.594  -38.582 -39.295 1.00 39.81  ?  835  HOH B O      1 
HETATM 15288 O O      . HOH J 5 .   ? 31.179  -10.549 -53.925 1.00 34.85  ?  836  HOH B O      1 
HETATM 15289 O O      . HOH J 5 .   ? 18.438  -5.698  -52.629 1.00 31.77  ?  837  HOH B O      1 
HETATM 15290 O O      . HOH J 5 .   ? -7.841  3.458   -37.337 1.00 50.71  ?  838  HOH B O      1 
HETATM 15291 O O      . HOH J 5 .   ? 51.523  -23.719 -29.687 1.00 32.79  ?  839  HOH B O      1 
HETATM 15292 O O      . HOH J 5 .   ? 27.857  -23.705 -25.763 1.00 23.58  ?  840  HOH B O      1 
HETATM 15293 O O      . HOH J 5 .   ? 3.590   -32.404 -38.556 1.00 21.28  ?  841  HOH B O      1 
HETATM 15294 O O      . HOH J 5 .   ? 35.019  -28.468 -39.400 1.00 28.71  ?  842  HOH B O      1 
HETATM 15295 O O      . HOH J 5 .   ? 31.966  -26.047 -32.104 1.00 38.70  ?  843  HOH B O      1 
HETATM 15296 O O      . HOH J 5 .   ? 17.246  -5.495  -30.239 1.00 16.47  ?  844  HOH B O      1 
HETATM 15297 O O      . HOH J 5 .   ? -1.754  -28.775 -29.430 1.00 12.51  ?  845  HOH B O      1 
HETATM 15298 O O      . HOH J 5 .   ? 14.066  0.603   -49.506 1.00 39.18  ?  846  HOH B O      1 
HETATM 15299 O O      . HOH J 5 .   ? 10.680  -3.458  -44.638 1.00 21.84  ?  847  HOH B O      1 
HETATM 15300 O O      . HOH J 5 .   ? 5.777   -4.284  -46.207 1.00 23.19  ?  848  HOH B O      1 
HETATM 15301 O O      . HOH J 5 .   ? 19.756  -22.498 -29.751 1.00 24.74  ?  849  HOH B O      1 
HETATM 15302 O O      . HOH J 5 .   ? -0.191  -1.947  -42.993 1.00 31.14  ?  850  HOH B O      1 
HETATM 15303 O O      . HOH J 5 .   ? -3.915  -12.038 -48.076 1.00 27.17  ?  851  HOH B O      1 
HETATM 15304 O O      . HOH J 5 .   ? 39.331  -30.765 -25.741 1.00 48.29  ?  852  HOH B O      1 
HETATM 15305 O O      . HOH J 5 .   ? 33.550  -14.486 -15.476 1.00 21.80  ?  853  HOH B O      1 
HETATM 15306 O O      . HOH J 5 .   ? 18.194  -11.203 -54.749 1.00 33.79  ?  854  HOH B O      1 
HETATM 15307 O O      . HOH J 5 .   ? 19.185  -38.792 -32.604 1.00 39.20  ?  855  HOH B O      1 
HETATM 15308 O O      . HOH J 5 .   ? 20.209  5.668   -38.912 1.00 45.61  ?  856  HOH B O      1 
HETATM 15309 O O      . HOH J 5 .   ? -13.504 -10.034 -25.055 1.00 18.85  ?  857  HOH B O      1 
HETATM 15310 O O      . HOH J 5 .   ? 28.002  1.101   -36.002 1.00 28.81  ?  858  HOH B O      1 
HETATM 15311 O O      . HOH J 5 .   ? -8.402  -38.080 -41.802 1.00 32.52  ?  859  HOH B O      1 
HETATM 15312 O O      . HOH J 5 .   ? 21.685  2.880   -41.809 1.00 32.10  ?  860  HOH B O      1 
HETATM 15313 O O      . HOH J 5 .   ? 9.945   1.304   -24.589 1.00 18.34  ?  861  HOH B O      1 
HETATM 15314 O O      . HOH J 5 .   ? 5.319   -46.120 -42.735 1.00 39.19  ?  862  HOH B O      1 
HETATM 15315 O O      . HOH J 5 .   ? 27.360  -21.524 -55.357 1.00 43.38  ?  863  HOH B O      1 
HETATM 15316 O O      . HOH J 5 .   ? 16.953  -38.763 -38.051 1.00 68.15  ?  864  HOH B O      1 
HETATM 15317 O O      . HOH J 5 .   ? 11.627  -39.761 -23.765 1.00 28.49  ?  865  HOH B O      1 
HETATM 15318 O O      . HOH J 5 .   ? 15.132  -2.329  -47.448 1.00 24.11  ?  866  HOH B O      1 
HETATM 15319 O O      . HOH J 5 .   ? -9.947  -27.716 -49.283 1.00 21.40  ?  867  HOH B O      1 
HETATM 15320 O O      . HOH J 5 .   ? 43.613  -32.844 -36.185 1.00 37.26  ?  868  HOH B O      1 
HETATM 15321 O O      . HOH J 5 .   ? 5.120   -29.224 -53.673 1.00 48.66  ?  869  HOH B O      1 
HETATM 15322 O O      . HOH J 5 .   ? 29.286  -22.341 -20.591 1.00 16.84  ?  870  HOH B O      1 
HETATM 15323 O O      . HOH J 5 .   ? 2.304   -38.745 -52.725 1.00 58.12  ?  871  HOH B O      1 
HETATM 15324 O O      . HOH J 5 .   ? -1.894  -7.607  -27.507 1.00 15.27  ?  872  HOH B O      1 
HETATM 15325 O O      . HOH J 5 .   ? 32.475  -32.679 -62.325 1.00 41.52  ?  873  HOH B O      1 
HETATM 15326 O O      . HOH J 5 .   ? 16.088  -39.865 -40.836 1.00 23.96  ?  874  HOH B O      1 
HETATM 15327 O O      . HOH J 5 .   ? 9.935   -42.009 -37.298 1.00 28.09  ?  875  HOH B O      1 
HETATM 15328 O O      . HOH J 5 .   ? 28.675  2.895   -30.738 1.00 41.85  ?  876  HOH B O      1 
HETATM 15329 O O      . HOH J 5 .   ? 0.916   3.148   -30.702 1.00 39.79  ?  877  HOH B O      1 
HETATM 15330 O O      . HOH J 5 .   ? 47.686  -11.864 -34.706 1.00 44.70  ?  878  HOH B O      1 
HETATM 15331 O O      . HOH J 5 .   ? 27.770  -32.426 -42.714 1.00 33.38  ?  879  HOH B O      1 
HETATM 15332 O O      . HOH J 5 .   ? 20.871  2.755   -33.751 1.00 42.63  ?  880  HOH B O      1 
HETATM 15333 O O      . HOH J 5 .   ? 29.825  -26.081 -48.595 1.00 19.25  ?  881  HOH B O      1 
HETATM 15334 O O      . HOH J 5 .   ? 46.572  -27.515 -30.196 1.00 39.74  ?  882  HOH B O      1 
HETATM 15335 O O      . HOH J 5 .   ? 48.302  -30.796 -29.651 1.00 59.58  ?  883  HOH B O      1 
HETATM 15336 O O      . HOH J 5 .   ? 13.152  -9.563  -52.421 1.00 32.57  ?  884  HOH B O      1 
HETATM 15337 O O      . HOH J 5 .   ? 19.677  -2.095  -28.215 1.00 22.34  ?  885  HOH B O      1 
HETATM 15338 O O      . HOH J 5 .   ? -7.710  -25.320 -55.298 1.00 28.84  ?  886  HOH B O      1 
HETATM 15339 O O      . HOH J 5 .   ? 22.780  -37.641 -32.872 1.00 37.46  ?  887  HOH B O      1 
HETATM 15340 O O      . HOH J 5 .   ? -9.370  -27.743 -34.216 1.00 20.34  ?  888  HOH B O      1 
HETATM 15341 O O      . HOH J 5 .   ? 26.721  1.282   -45.932 1.00 29.67  ?  889  HOH B O      1 
HETATM 15342 O O      . HOH J 5 .   ? 12.726  -3.948  -49.194 1.00 68.19  ?  890  HOH B O      1 
HETATM 15343 O O      . HOH J 5 .   ? 43.010  -16.615 -27.282 1.00 36.65  ?  891  HOH B O      1 
HETATM 15344 O O      . HOH J 5 .   ? -11.167 -25.102 -30.652 1.00 33.34  ?  892  HOH B O      1 
HETATM 15345 O O      . HOH J 5 .   ? 0.259   -32.165 -50.044 1.00 15.55  ?  893  HOH B O      1 
HETATM 15346 O O      . HOH J 5 .   ? 24.379  -35.420 -44.879 1.00 26.29  ?  894  HOH B O      1 
HETATM 15347 O O      . HOH J 5 .   ? 36.344  0.440   -47.559 1.00 43.89  ?  895  HOH B O      1 
HETATM 15348 O O      . HOH J 5 .   ? 2.460   -38.091 -56.786 1.00 58.38  ?  896  HOH B O      1 
HETATM 15349 O O      . HOH J 5 .   ? 27.673  -33.186 -47.067 1.00 31.50  ?  897  HOH B O      1 
HETATM 15350 O O      . HOH J 5 .   ? 32.806  -35.411 -44.765 1.00 56.91  ?  898  HOH B O      1 
HETATM 15351 O O      . HOH J 5 .   ? -12.174 -24.356 -48.536 1.00 32.23  ?  899  HOH B O      1 
HETATM 15352 O O      . HOH J 5 .   ? 51.018  -17.810 -29.015 1.00 43.55  ?  900  HOH B O      1 
HETATM 15353 O O      . HOH J 5 .   ? 7.883   -15.785 -59.099 1.00 47.07  ?  901  HOH B O      1 
HETATM 15354 O O      . HOH J 5 .   ? 33.822  -11.395 -17.951 1.00 39.72  ?  902  HOH B O      1 
HETATM 15355 O O      . HOH J 5 .   ? 41.017  -4.678  -32.165 1.00 49.47  ?  903  HOH B O      1 
HETATM 15356 O O      . HOH J 5 .   ? 54.476  -20.654 -34.963 1.00 41.47  ?  904  HOH B O      1 
HETATM 15357 O O      . HOH J 5 .   ? 34.499  -1.025  -30.853 1.00 53.50  ?  905  HOH B O      1 
HETATM 15358 O O      . HOH J 5 .   ? 39.903  -35.250 -42.431 1.00 45.27  ?  906  HOH B O      1 
HETATM 15359 O O      . HOH J 5 .   ? 34.297  -39.227 -46.514 1.00 45.16  ?  907  HOH B O      1 
HETATM 15360 O O      . HOH J 5 .   ? 37.367  -11.691 -21.531 1.00 36.84  ?  908  HOH B O      1 
HETATM 15361 O O      . HOH J 5 .   ? 21.906  1.151   -35.699 1.00 31.99  ?  909  HOH B O      1 
HETATM 15362 O O      . HOH J 5 .   ? 7.762   -40.056 -30.604 1.00 27.21  ?  910  HOH B O      1 
HETATM 15363 O O      . HOH J 5 .   ? 36.252  -30.899 -36.319 1.00 42.58  ?  911  HOH B O      1 
HETATM 15364 O O      . HOH J 5 .   ? 4.079   -46.587 -51.980 1.00 48.68  ?  912  HOH B O      1 
HETATM 15365 O O      . HOH J 5 .   ? 4.341   -39.363 -58.238 1.00 31.62  ?  913  HOH B O      1 
HETATM 15366 O O      . HOH J 5 .   ? 29.657  -21.173 -54.996 1.00 30.00  ?  914  HOH B O      1 
HETATM 15367 O O      . HOH J 5 .   ? 19.839  -24.977 -48.013 1.00 14.32  ?  915  HOH B O      1 
HETATM 15368 O O      . HOH J 5 .   ? 18.906  -39.552 -26.094 1.00 26.26  ?  916  HOH B O      1 
HETATM 15369 O O      . HOH J 5 .   ? 35.760  -0.163  -32.457 1.00 47.48  ?  917  HOH B O      1 
HETATM 15370 O O      . HOH J 5 .   ? 16.645  5.171   -33.275 1.00 25.90  ?  918  HOH B O      1 
HETATM 15371 O O      . HOH J 5 .   ? 24.235  -22.801 -29.148 1.00 50.46  ?  919  HOH B O      1 
HETATM 15372 O O      . HOH J 5 .   ? 29.559  -28.442 -31.166 1.00 40.67  ?  920  HOH B O      1 
HETATM 15373 O O      . HOH J 5 .   ? 30.810  4.306   -29.035 1.00 64.17  ?  921  HOH B O      1 
HETATM 15374 O O      . HOH J 5 .   ? 5.489   -33.949 -37.076 1.00 25.72  ?  922  HOH B O      1 
HETATM 15375 O O      . HOH J 5 .   ? 35.109  -31.480 -57.880 1.00 38.86  ?  923  HOH B O      1 
HETATM 15376 O O      . HOH J 5 .   ? -0.568  -21.493 -52.583 1.00 32.42  ?  924  HOH B O      1 
HETATM 15377 O O      . HOH J 5 .   ? 14.409  -37.652 -60.678 1.00 30.00  ?  925  HOH B O      1 
HETATM 15378 O O      . HOH J 5 .   ? 28.271  -30.091 -63.658 1.00 40.41  ?  926  HOH B O      1 
HETATM 15379 O O      . HOH J 5 .   ? 33.921  -34.169 -14.663 1.00 63.18  ?  927  HOH B O      1 
HETATM 15380 O O      . HOH J 5 .   ? 31.380  -18.631 -30.033 1.00 29.31  ?  928  HOH B O      1 
HETATM 15381 O O      . HOH J 5 .   ? 19.271  -9.278  -54.241 1.00 52.20  ?  929  HOH B O      1 
HETATM 15382 O O      . HOH J 5 .   ? 17.780  4.947   -47.965 1.00 62.35  ?  930  HOH B O      1 
HETATM 15383 O O      . HOH J 5 .   ? 36.534  -1.189  -24.963 1.00 30.16  ?  931  HOH B O      1 
HETATM 15384 O O      . HOH J 5 .   ? 27.697  -5.497  -8.655  1.00 33.92  ?  932  HOH B O      1 
HETATM 15385 O O      . HOH J 5 .   ? 0.741   -38.750 -51.905 1.00 20.80  ?  933  HOH B O      1 
HETATM 15386 O O      . HOH J 5 .   ? 36.810  -21.478 -50.281 1.00 32.41  ?  934  HOH B O      1 
HETATM 15387 O O      . HOH J 5 .   ? 18.582  -35.838 -59.430 1.00 34.70  ?  935  HOH B O      1 
HETATM 15388 O O      . HOH J 5 .   ? 0.077   -23.004 -49.325 1.00 16.69  ?  936  HOH B O      1 
HETATM 15389 O O      . HOH J 5 .   ? 23.767  -16.445 -54.665 1.00 32.67  ?  937  HOH B O      1 
HETATM 15390 O O      . HOH J 5 .   ? -3.760  -41.614 -45.919 1.00 15.36  ?  938  HOH B O      1 
HETATM 15391 O O      . HOH J 5 .   ? 42.238  -18.913 -28.216 1.00 35.49  ?  939  HOH B O      1 
HETATM 15392 O O      . HOH J 5 .   ? 42.119  -27.286 -27.131 1.00 42.77  ?  940  HOH B O      1 
HETATM 15393 O O      . HOH J 5 .   ? 23.601  -39.958 -56.547 1.00 52.93  ?  941  HOH B O      1 
HETATM 15394 O O      . HOH J 5 .   ? 29.407  1.624   -46.811 1.00 23.72  ?  942  HOH B O      1 
HETATM 15395 O O      . HOH J 5 .   ? 4.199   -17.925 -35.257 1.00 13.97  ?  943  HOH B O      1 
HETATM 15396 O O      . HOH J 5 .   ? -4.222  0.330   -29.254 1.00 24.55  ?  944  HOH B O      1 
HETATM 15397 O O      . HOH J 5 .   ? 30.250  -16.145 -29.989 1.00 47.15  ?  945  HOH B O      1 
HETATM 15398 O O      . HOH J 5 .   ? 11.775  -37.271 -62.602 1.00 48.36  ?  946  HOH B O      1 
HETATM 15399 O O      . HOH J 5 .   ? 31.236  -26.659 -58.826 1.00 29.35  ?  947  HOH B O      1 
HETATM 15400 O O      . HOH J 5 .   ? 55.917  -29.149 -34.055 1.00 48.18  ?  948  HOH B O      1 
HETATM 15401 O O      . HOH J 5 .   ? 22.898  3.460   -26.823 1.00 47.13  ?  949  HOH B O      1 
HETATM 15402 O O      . HOH J 5 .   ? 29.257  -5.110  -6.350  1.00 28.65  ?  950  HOH B O      1 
HETATM 15403 O O      . HOH J 5 .   ? 34.562  -38.699 -56.937 1.00 44.93  ?  951  HOH B O      1 
HETATM 15404 O O      . HOH J 5 .   ? 27.798  -33.195 -39.679 1.00 27.43  ?  952  HOH B O      1 
HETATM 15405 O O      . HOH J 5 .   ? 14.752  -22.765 -57.428 1.00 25.17  ?  953  HOH B O      1 
HETATM 15406 O O      . HOH J 5 .   ? 32.300  2.816   -45.431 1.00 23.57  ?  954  HOH B O      1 
HETATM 15407 O O      . HOH J 5 .   ? 12.051  -3.077  -46.949 1.00 26.61  ?  955  HOH B O      1 
HETATM 15408 O O      . HOH J 5 .   ? -11.457 -35.552 -41.786 1.00 45.17  ?  956  HOH B O      1 
HETATM 15409 O O      . HOH J 5 .   ? -4.728  -20.631 -23.952 1.00 72.70  ?  957  HOH B O      1 
HETATM 15410 O O      . HOH J 5 .   ? 17.038  -43.361 -24.340 1.00 42.14  ?  958  HOH B O      1 
HETATM 15411 O O      . HOH J 5 .   ? -12.027 -35.236 -46.762 1.00 49.72  ?  959  HOH B O      1 
HETATM 15412 O O      . HOH J 5 .   ? 33.162  -27.174 -11.751 1.00 43.12  ?  960  HOH B O      1 
HETATM 15413 O O      . HOH J 5 .   ? 33.729  -6.649  -4.147  1.00 33.10  ?  961  HOH B O      1 
HETATM 15414 O O      . HOH J 5 .   ? 57.531  -20.026 -30.346 1.00 44.84  ?  962  HOH B O      1 
HETATM 15415 O O      . HOH J 5 .   ? 28.509  -26.760 -60.545 1.00 29.01  ?  963  HOH B O      1 
HETATM 15416 O O      . HOH J 5 .   ? 32.723  -29.119 -32.774 1.00 44.35  ?  964  HOH B O      1 
HETATM 15417 O O      . HOH J 5 .   ? 38.683  -11.616 -24.266 1.00 26.05  ?  965  HOH B O      1 
HETATM 15418 O O      . HOH J 5 .   ? 16.607  -40.113 -58.757 1.00 45.84  ?  966  HOH B O      1 
HETATM 15419 O O      . HOH J 5 .   ? 42.648  -2.626  -37.952 1.00 41.03  ?  967  HOH B O      1 
HETATM 15420 O O      . HOH J 5 .   ? 19.705  -5.719  -7.198  1.00 31.70  ?  968  HOH B O      1 
HETATM 15421 O O      . HOH J 5 .   ? -1.099  -7.010  -47.500 1.00 39.86  ?  969  HOH B O      1 
HETATM 15422 O O      . HOH J 5 .   ? 16.801  -41.787 -56.682 1.00 46.60  ?  970  HOH B O      1 
HETATM 15423 O O      . HOH J 5 .   ? 19.671  -23.196 -55.181 1.00 20.02  ?  971  HOH B O      1 
HETATM 15424 O O      . HOH J 5 .   ? -0.555  -41.813 -39.175 1.00 46.82  ?  972  HOH B O      1 
HETATM 15425 O O      . HOH J 5 .   ? 37.000  -4.571  -14.392 1.00 36.44  ?  973  HOH B O      1 
HETATM 15426 O O      . HOH J 5 .   ? 28.778  -17.002 -26.728 1.00 30.12  ?  974  HOH B O      1 
HETATM 15427 O O      . HOH J 5 .   ? 21.765  -20.440 -32.541 1.00 41.09  ?  975  HOH B O      1 
HETATM 15428 O O      . HOH J 5 .   ? 31.020  -16.173 -50.950 1.00 35.45  ?  976  HOH B O      1 
HETATM 15429 O O      . HOH J 5 .   ? 26.270  -7.071  -7.472  1.00 20.01  ?  977  HOH B O      1 
HETATM 15430 O O      . HOH J 5 .   ? 13.100  -4.450  -51.260 1.00 57.21  ?  978  HOH B O      1 
HETATM 15431 O O      . HOH J 5 .   ? 18.612  -39.210 -28.909 1.00 32.22  ?  979  HOH B O      1 
HETATM 15432 O O      . HOH J 5 .   ? 26.663  -11.941 -51.868 1.00 20.51  ?  980  HOH B O      1 
HETATM 15433 O O      . HOH J 5 .   ? 22.249  -22.630 -30.889 1.00 26.35  ?  981  HOH B O      1 
HETATM 15434 O O      . HOH J 5 .   ? 22.039  -39.713 -26.805 1.00 35.54  ?  982  HOH B O      1 
HETATM 15435 O O      . HOH J 5 .   ? 16.378  -1.734  -49.882 1.00 21.37  ?  983  HOH B O      1 
HETATM 15436 O O      . HOH J 5 .   ? 28.042  -37.096 -49.592 1.00 23.62  ?  984  HOH B O      1 
HETATM 15437 O O      . HOH J 5 .   ? 39.321  -3.834  -24.332 1.00 44.24  ?  985  HOH B O      1 
HETATM 15438 O O      . HOH J 5 .   ? -3.357  -19.421 -55.585 1.00 44.70  ?  986  HOH B O      1 
HETATM 15439 O O      . HOH J 5 .   ? 32.398  -31.230 -39.110 1.00 46.71  ?  987  HOH B O      1 
HETATM 15440 O O      . HOH J 5 .   ? 44.362  -17.872 -28.514 1.00 47.25  ?  988  HOH B O      1 
HETATM 15441 O O      . HOH J 5 .   ? 35.087  0.065   -50.943 1.00 53.40  ?  989  HOH B O      1 
HETATM 15442 O O      . HOH J 5 .   ? 34.539  -17.121 -10.413 1.00 58.20  ?  990  HOH B O      1 
HETATM 15443 O O      . HOH J 5 .   ? -2.815  -29.192 -54.022 1.00 33.18  ?  991  HOH B O      1 
HETATM 15444 O O      . HOH J 5 .   ? -16.627 -29.426 -48.308 1.00 31.64  ?  992  HOH B O      1 
HETATM 15445 O O      . HOH J 5 .   ? 9.658   5.772   -41.879 1.00 46.48  ?  993  HOH B O      1 
HETATM 15446 O O      . HOH J 5 .   ? 34.077  -16.866 -27.676 1.00 53.00  ?  994  HOH B O      1 
HETATM 15447 O O      . HOH J 5 .   ? 35.099  -16.806 -14.587 1.00 42.04  ?  995  HOH B O      1 
HETATM 15448 O O      . HOH J 5 .   ? 34.053  -31.030 -60.585 1.00 39.89  ?  996  HOH B O      1 
HETATM 15449 O O      . HOH J 5 .   ? 7.923   -48.597 -49.656 1.00 56.02  ?  997  HOH B O      1 
HETATM 15450 O O      . HOH J 5 .   ? 11.763  -15.637 -56.805 1.00 47.26  ?  998  HOH B O      1 
HETATM 15451 O O      . HOH J 5 .   ? 51.656  -21.560 -41.223 1.00 53.21  ?  999  HOH B O      1 
HETATM 15452 O O      . HOH J 5 .   ? 9.810   -16.012 -55.135 1.00 48.42  ?  1000 HOH B O      1 
HETATM 15453 O O      . HOH J 5 .   ? 7.423   1.726   -44.482 1.00 44.46  ?  1001 HOH B O      1 
HETATM 15454 O O      . HOH J 5 .   ? 7.821   -27.606 -54.611 1.00 42.64  ?  1002 HOH B O      1 
HETATM 15455 O O      . HOH J 5 .   ? 16.336  -37.475 -58.831 1.00 55.57  ?  1003 HOH B O      1 
HETATM 15456 O O      . HOH J 5 .   ? 7.499   -5.807  -51.360 1.00 47.79  ?  1004 HOH B O      1 
HETATM 15457 O O      . HOH J 5 .   ? 33.156  -17.394 -8.734  1.00 50.88  ?  1005 HOH B O      1 
HETATM 15458 O O      . HOH J 5 .   ? -11.837 -27.863 -32.200 1.00 53.03  ?  1006 HOH B O      1 
HETATM 15459 O O      . HOH J 5 .   ? 35.301  -22.990 -18.771 1.00 47.03  ?  1007 HOH B O      1 
HETATM 15460 O O      . HOH J 5 .   ? -4.278  -1.293  -45.794 1.00 46.50  ?  1008 HOH B O      1 
HETATM 15461 O O      . HOH J 5 .   ? 18.795  6.010   -32.167 1.00 51.83  ?  1009 HOH B O      1 
HETATM 15462 O O      . HOH J 5 .   ? 40.069  -7.441  -47.886 1.00 38.56  ?  1010 HOH B O      1 
HETATM 15463 O O      . HOH J 5 .   ? 5.754   -26.765 -53.283 1.00 43.79  ?  1011 HOH B O      1 
HETATM 15464 O O      . HOH J 5 .   ? 21.361  -30.194 -60.860 1.00 54.19  ?  1012 HOH B O      1 
HETATM 15465 O O      . HOH J 5 .   ? 22.280  -22.103 -55.430 1.00 42.00  ?  1013 HOH B O      1 
HETATM 15466 O O      . HOH J 5 .   ? 34.520  -30.064 -34.343 1.00 44.33  ?  1014 HOH B O      1 
HETATM 15467 O O      . HOH J 5 .   ? 29.500  -33.708 -37.673 1.00 48.67  ?  1015 HOH B O      1 
HETATM 15468 O O      . HOH J 5 .   ? 27.729  -1.947  -54.933 1.00 50.43  ?  1016 HOH B O      1 
HETATM 15469 O O      . HOH J 5 .   ? 32.613  -14.858 -29.011 1.00 28.47  ?  1017 HOH B O      1 
HETATM 15470 O O      . HOH J 5 .   ? 34.883  -13.058 -17.923 1.00 56.25  ?  1018 HOH B O      1 
HETATM 15471 O O      . HOH J 5 .   ? 24.499  -24.598 -30.878 1.00 42.96  ?  1019 HOH B O      1 
HETATM 15472 O O      . HOH J 5 .   ? 38.342  -5.371  -9.677  1.00 26.08  ?  1020 HOH B O      1 
HETATM 15473 O O      . HOH J 5 .   ? 38.359  -14.297 -24.878 1.00 47.08  ?  1021 HOH B O      1 
HETATM 15474 O O      . HOH J 5 .   ? 37.158  -34.914 -47.282 1.00 55.52  ?  1022 HOH B O      1 
HETATM 15475 O O      . HOH J 5 .   ? 12.261  -36.266 -61.106 1.00 39.72  ?  1023 HOH B O      1 
HETATM 15476 O O      . HOH J 5 .   ? 6.596   -16.552 -51.294 1.00 46.61  ?  1024 HOH B O      1 
HETATM 15477 O O      . HOH J 5 .   ? 23.495  -36.267 -36.581 1.00 55.17  ?  1025 HOH B O      1 
HETATM 15478 O O      . HOH J 5 .   ? 2.597   -38.842 -54.861 1.00 35.29  ?  1026 HOH B O      1 
HETATM 15479 O O      . HOH J 5 .   ? 35.593  -11.003 -18.968 1.00 61.65  ?  1027 HOH B O      1 
HETATM 15480 O O      . HOH J 5 .   ? -5.562  -13.524 -49.403 1.00 53.72  ?  1028 HOH B O      1 
HETATM 15481 O O      . HOH J 5 .   ? 8.665   -23.397 -28.501 1.00 17.95  ?  1029 HOH B O      1 
HETATM 15482 O O      . HOH J 5 .   ? 36.795  -0.783  -20.352 1.00 43.60  ?  1030 HOH B O      1 
HETATM 15483 O O      . HOH J 5 .   ? 8.032   -2.811  -45.243 1.00 25.28  ?  1031 HOH B O      1 
HETATM 15484 O O      . HOH J 5 .   ? 11.699  -33.935 -60.484 1.00 32.64  ?  1032 HOH B O      1 
HETATM 15485 O O      . HOH J 5 .   ? 53.030  -16.809 -28.755 1.00 50.76  ?  1033 HOH B O      1 
HETATM 15486 O O      . HOH J 5 .   ? -16.292 -32.094 -48.779 1.00 37.69  ?  1034 HOH B O      1 
HETATM 15487 O O      . HOH J 5 .   ? -9.503  -20.220 -50.063 1.00 38.88  ?  1035 HOH B O      1 
HETATM 15488 O O      . HOH J 5 .   ? 26.731  2.366   -26.289 1.00 37.91  ?  1036 HOH B O      1 
HETATM 15489 O O      . HOH J 5 .   ? 36.227  -18.271 -15.669 1.00 57.70  ?  1037 HOH B O      1 
HETATM 15490 O O      . HOH J 5 .   ? 16.820  7.863   -42.706 1.00 49.79  ?  1038 HOH B O      1 
HETATM 15491 O O      . HOH J 5 .   ? 30.934  -24.527 -30.428 1.00 45.81  ?  1039 HOH B O      1 
HETATM 15492 O O      . HOH J 5 .   ? 7.014   -17.414 -52.949 1.00 80.26  ?  1040 HOH B O      1 
HETATM 15493 O O      . HOH J 5 .   ? 24.382  -0.985  -16.610 1.00 34.70  ?  1041 HOH B O      1 
HETATM 15494 O O      . HOH J 5 .   ? 1.680   1.110   -40.034 1.00 52.47  ?  1042 HOH B O      1 
HETATM 15495 O O      . HOH J 5 .   ? -13.524 -12.760 -24.806 1.00 39.62  ?  1043 HOH B O      1 
HETATM 15496 O O      . HOH J 5 .   ? 23.068  -38.215 -58.523 1.00 43.49  ?  1044 HOH B O      1 
HETATM 15497 O O      . HOH J 5 .   ? 16.072  -3.625  -51.740 1.00 32.68  ?  1045 HOH B O      1 
HETATM 15498 O O      . HOH J 5 .   ? 0.317   -1.438  -45.565 1.00 50.68  ?  1046 HOH B O      1 
HETATM 15499 O O      . HOH J 5 .   ? -16.369 -29.640 -45.967 1.00 45.66  ?  1047 HOH B O      1 
HETATM 15500 O O      . HOH J 5 .   ? 17.040  -41.285 -29.860 1.00 41.68  ?  1048 HOH B O      1 
HETATM 15501 O O      . HOH J 5 .   ? 17.689  6.987   -37.169 1.00 49.78  ?  1049 HOH B O      1 
HETATM 15502 O O      . HOH J 5 .   ? 26.432  -3.208  -10.009 1.00 53.02  ?  1050 HOH B O      1 
HETATM 15503 O O      . HOH J 5 .   ? 8.279   4.040   -35.997 1.00 50.38  ?  1051 HOH B O      1 
HETATM 15504 O O      . HOH J 5 .   ? 55.622  -31.155 -33.181 1.00 48.50  ?  1052 HOH B O      1 
HETATM 15505 O O      . HOH J 5 .   ? 7.168   -0.664  -43.612 1.00 23.98  ?  1053 HOH B O      1 
HETATM 15506 O O      . HOH J 5 .   ? 27.371  -34.088 -44.821 1.00 47.43  ?  1054 HOH B O      1 
HETATM 15507 O O      . HOH J 5 .   ? 5.979   2.476   -36.223 1.00 45.37  ?  1055 HOH B O      1 
HETATM 15508 O O      . HOH J 5 .   ? 33.234  -12.667 -53.896 1.00 46.97  ?  1056 HOH B O      1 
HETATM 15509 O O      . HOH J 5 .   ? 37.496  -2.208  -18.300 1.00 39.74  ?  1057 HOH B O      1 
HETATM 15510 O O      . HOH J 5 .   ? 3.659   -38.164 -37.292 1.00 40.40  ?  1058 HOH B O      1 
HETATM 15511 O O      . HOH J 5 .   ? 8.996   6.894   -19.385 1.00 77.05  ?  1059 HOH B O      1 
HETATM 15512 O O      . HOH J 5 .   ? 21.174  -10.037 -54.616 1.00 41.83  ?  1060 HOH B O      1 
HETATM 15513 O O      . HOH J 5 .   ? 27.656  -26.115 -26.910 1.00 35.79  ?  1061 HOH B O      1 
HETATM 15514 O O      . HOH J 5 .   ? 12.911  -23.222 -59.454 1.00 37.67  ?  1062 HOH B O      1 
HETATM 15515 O O      . HOH J 5 .   ? 21.942  -35.325 -35.674 1.00 56.05  ?  1063 HOH B O      1 
HETATM 15516 O O      . HOH J 5 .   ? -7.882  -37.027 -37.086 1.00 43.08  ?  1064 HOH B O      1 
HETATM 15517 O O      . HOH J 5 .   ? 30.565  -17.731 -7.234  1.00 50.62  ?  1065 HOH B O      1 
HETATM 15518 O O      . HOH J 5 .   ? 25.319  -34.575 -39.908 1.00 41.43  ?  1066 HOH B O      1 
HETATM 15519 O O      . HOH J 5 .   ? 37.513  -0.328  -16.947 1.00 53.61  ?  1067 HOH B O      1 
HETATM 15520 O O      . HOH J 5 .   ? 0.977   -40.706 -53.391 1.00 50.91  ?  1068 HOH B O      1 
HETATM 15521 O O      . HOH J 5 .   ? 32.836  -28.880 -10.170 1.00 49.80  ?  1069 HOH B O      1 
HETATM 15522 O O      . HOH J 5 .   ? 35.784  -15.758 -12.631 1.00 48.98  ?  1070 HOH B O      1 
HETATM 15523 O O      . HOH J 5 .   ? 42.484  -7.371  -43.193 1.00 37.22  ?  1071 HOH B O      1 
HETATM 15524 O O      . HOH J 5 .   ? 12.018  -47.866 -52.779 1.00 43.88  ?  1072 HOH B O      1 
HETATM 15525 O O      . HOH J 5 .   ? 10.459  4.976   -46.336 1.00 44.60  ?  1073 HOH B O      1 
HETATM 15526 O O      . HOH J 5 .   ? 8.622   -42.257 -39.666 1.00 27.60  ?  1074 HOH B O      1 
HETATM 15527 O O      . HOH J 5 .   ? 33.853  -28.016 -31.370 1.00 62.90  ?  1075 HOH B O      1 
HETATM 15528 O O      . HOH J 5 .   ? 22.398  3.458   -39.250 1.00 50.88  ?  1076 HOH B O      1 
HETATM 15529 O O      . HOH J 5 .   ? 15.855  -11.310 -55.134 1.00 49.37  ?  1077 HOH B O      1 
HETATM 15530 O O      . HOH J 5 .   ? 9.205   8.385   -20.589 1.00 53.24  ?  1078 HOH B O      1 
HETATM 15531 O O      . HOH J 5 .   ? 30.404  -19.658 -27.845 1.00 54.51  ?  1079 HOH B O      1 
HETATM 15532 O O      . HOH J 5 .   ? 20.057  -18.572 -4.359  1.00 64.71  ?  1080 HOH B O      1 
HETATM 15533 O O      . HOH J 5 .   ? 1.292   -46.458 -43.678 1.00 44.77  ?  1081 HOH B O      1 
HETATM 15534 O O      . HOH J 5 .   ? 29.316  -27.463 -63.325 1.00 55.02  ?  1082 HOH B O      1 
HETATM 15535 O O      . HOH J 5 .   ? 40.745  -28.340 -24.886 1.00 49.45  ?  1083 HOH B O      1 
HETATM 15536 O O      . HOH J 5 .   ? 14.885  -43.343 -56.352 1.00 39.91  ?  1084 HOH B O      1 
HETATM 15537 O O      . HOH J 5 .   ? 31.568  -5.385  -54.134 1.00 50.31  ?  1085 HOH B O      1 
HETATM 15538 O O      . HOH J 5 .   ? 16.214  -43.620 -47.585 1.00 42.24  ?  1086 HOH B O      1 
HETATM 15539 O O      . HOH J 5 .   ? 33.862  3.041   -18.583 1.00 52.80  ?  1087 HOH B O      1 
HETATM 15540 O O      . HOH J 5 .   ? 31.659  4.697   -43.627 1.00 35.40  ?  1088 HOH B O      1 
HETATM 15541 O O      . HOH J 5 .   ? 26.626  1.049   -21.367 1.00 45.75  ?  1089 HOH B O      1 
HETATM 15542 O O      . HOH J 5 .   ? 6.034   -42.493 -38.865 1.00 29.71  ?  1090 HOH B O      1 
HETATM 15543 O O      . HOH J 5 .   ? 27.561  -29.529 -30.881 1.00 37.04  ?  1091 HOH B O      1 
HETATM 15544 O O      . HOH J 5 .   ? 25.601  1.762   -37.099 1.00 29.85  ?  1092 HOH B O      1 
HETATM 15545 O O      . HOH J 5 .   ? 5.871   -47.977 -50.904 1.00 49.90  ?  1093 HOH B O      1 
HETATM 15546 O O      . HOH J 5 .   ? 35.517  3.278   -46.253 1.00 33.45  ?  1094 HOH B O      1 
HETATM 15547 O O      . HOH J 5 .   ? 47.176  -8.943  -39.363 1.00 38.51  ?  1095 HOH B O      1 
HETATM 15548 O O      . HOH J 5 .   ? 6.011   -48.621 -48.279 1.00 60.98  ?  1096 HOH B O      1 
HETATM 15549 O O      . HOH J 5 .   ? 21.024  -41.125 -24.912 1.00 39.12  ?  1097 HOH B O      1 
HETATM 15550 O O      . HOH J 5 .   ? 25.383  -33.159 -26.540 1.00 33.91  ?  1098 HOH B O      1 
HETATM 15551 O O      . HOH J 5 .   ? 32.877  -20.284 -28.390 1.00 62.28  ?  1099 HOH B O      1 
HETATM 15552 O O      . HOH J 5 .   ? 37.394  -4.788  -19.229 1.00 27.20  ?  1100 HOH B O      1 
HETATM 15553 O O      . HOH J 5 .   ? 22.663  1.593   -43.916 1.00 40.65  ?  1101 HOH B O      1 
HETATM 15554 O O      . HOH J 5 .   ? 35.273  -15.175 -10.782 1.00 45.29  ?  1102 HOH B O      1 
HETATM 15555 O O      . HOH J 5 .   ? 26.184  1.439   -55.038 1.00 37.89  ?  1103 HOH B O      1 
HETATM 15556 O O      . HOH J 5 .   ? -2.360  -45.314 -49.985 1.00 77.93  ?  1104 HOH B O      1 
HETATM 15557 O O      . HOH J 5 .   ? 41.430  -1.811  -42.279 1.00 45.43  ?  1105 HOH B O      1 
HETATM 15558 O O      . HOH J 5 .   ? 13.920  -43.315 -59.174 1.00 64.72  ?  1106 HOH B O      1 
HETATM 15559 O O      . HOH J 5 .   ? 34.362  0.304   -36.444 1.00 44.86  ?  1107 HOH B O      1 
HETATM 15560 O O      . HOH J 5 .   ? 12.030  -6.099  -44.440 1.00 25.30  ?  1108 HOH B O      1 
HETATM 15561 O O      . HOH J 5 .   ? -3.772  -43.983 -40.342 1.00 31.40  ?  1109 HOH B O      1 
HETATM 15562 O O      . HOH J 5 .   ? 23.065  2.759   -37.267 1.00 45.75  ?  1110 HOH B O      1 
HETATM 15563 O O      . HOH J 5 .   ? -1.919  -39.850 -50.556 1.00 26.59  ?  1111 HOH B O      1 
HETATM 15564 O O      . HOH J 5 .   ? -10.348 -17.394 -50.328 1.00 46.19  ?  1112 HOH B O      1 
HETATM 15565 O O      . HOH J 5 .   ? 35.969  -11.356 -8.666  1.00 42.48  ?  1113 HOH B O      1 
HETATM 15566 O O      . HOH J 5 .   ? 3.925   -40.859 -39.660 1.00 30.14  ?  1114 HOH B O      1 
HETATM 15567 O O      . HOH J 5 .   ? 19.743  -31.428 -60.985 1.00 52.61  ?  1115 HOH B O      1 
HETATM 15568 O O      . HOH J 5 .   ? 4.431   1.346   -40.443 1.00 33.25  ?  1116 HOH B O      1 
HETATM 15569 O O      . HOH J 5 .   ? 27.055  2.296   -23.722 1.00 50.64  ?  1117 HOH B O      1 
HETATM 15570 O O      . HOH J 5 .   ? 28.383  -5.707  -3.577  1.00 32.06  ?  1118 HOH B O      1 
HETATM 15571 O O      . HOH J 5 .   ? 25.562  -26.208 -29.539 1.00 58.57  ?  1119 HOH B O      1 
HETATM 15572 O O      . HOH J 5 .   ? 2.804   -44.614 -41.993 1.00 47.54  ?  1120 HOH B O      1 
HETATM 15573 O O      . HOH J 5 .   ? -10.036 -39.842 -42.851 1.00 49.45  ?  1121 HOH B O      1 
HETATM 15574 O O      . HOH J 5 .   ? 0.242   0.599   -42.058 1.00 36.04  ?  1122 HOH B O      1 
HETATM 15575 O O      . HOH J 5 .   ? 18.543  -33.521 -60.432 1.00 40.17  ?  1123 HOH B O      1 
HETATM 15576 O O      . HOH J 5 .   ? 35.923  -20.584 -25.438 1.00 51.68  ?  1124 HOH B O      1 
HETATM 15577 O O      . HOH J 5 .   ? -10.428 -42.864 -45.792 1.00 57.59  ?  1125 HOH B O      1 
HETATM 15578 O O      . HOH J 5 .   ? 16.834  0.466   -51.326 1.00 38.70  ?  1126 HOH B O      1 
HETATM 15579 O O      . HOH J 5 .   ? 3.838   -47.512 -44.425 1.00 47.48  ?  1127 HOH B O      1 
HETATM 15580 O O      . HOH J 5 .   ? -7.828  -4.495  -47.000 1.00 32.39  ?  1128 HOH B O      1 
HETATM 15581 O O      . HOH J 5 .   ? 28.789  -11.886 -53.858 1.00 47.31  ?  1129 HOH B O      1 
HETATM 15582 O O      . HOH J 5 .   ? 34.501  -31.034 -38.500 1.00 48.22  ?  1130 HOH B O      1 
HETATM 15583 O O      . HOH J 5 .   ? 2.454   0.683   -33.736 1.00 32.42  ?  1131 HOH B O      1 
HETATM 15584 O O      . HOH J 5 .   ? -0.609  5.457   -31.073 1.00 46.33  ?  1132 HOH B O      1 
HETATM 15585 O O      . HOH J 5 .   ? 2.548   -21.776 -54.549 1.00 39.00  ?  1133 HOH B O      1 
HETATM 15586 O O      . HOH J 5 .   ? -5.533  -41.004 -50.141 1.00 45.48  ?  1134 HOH B O      1 
HETATM 15587 O O      . HOH J 5 .   ? 19.996  -4.454  -54.395 1.00 51.26  ?  1135 HOH B O      1 
HETATM 15588 O O      . HOH J 5 .   ? 44.490  -6.787  -41.850 1.00 38.82  ?  1136 HOH B O      1 
HETATM 15589 O O      . HOH J 5 .   ? 14.136  -41.673 -35.847 1.00 48.83  ?  1137 HOH B O      1 
HETATM 15590 O O      . HOH J 5 .   ? 32.992  -21.070 -53.963 1.00 51.49  ?  1138 HOH B O      1 
HETATM 15591 O O      . HOH J 5 .   ? 33.986  -24.724 -26.949 1.00 56.12  ?  1139 HOH B O      1 
HETATM 15592 O O      . HOH J 5 .   ? 12.673  -49.352 -50.396 1.00 41.99  ?  1140 HOH B O      1 
HETATM 15593 O O      . HOH J 5 .   ? -4.883  -6.924  -47.427 1.00 27.79  ?  1141 HOH B O      1 
HETATM 15594 O O      . HOH J 5 .   ? 35.411  -12.376 -54.731 1.00 48.20  ?  1142 HOH B O      1 
HETATM 15595 O O      . HOH J 5 .   ? 30.456  -23.312 -25.068 1.00 27.79  ?  1143 HOH B O      1 
HETATM 15596 O O      . HOH J 5 .   ? -17.148 -14.419 -30.149 1.00 30.11  ?  1144 HOH B O      1 
HETATM 15597 O O      . HOH J 5 .   ? 31.174  -23.151 -22.431 1.00 24.63  ?  1145 HOH B O      1 
HETATM 15598 O O      . HOH J 5 .   ? -13.053 -27.831 -30.305 1.00 48.34  ?  1146 HOH B O      1 
HETATM 15599 O O      . HOH J 5 .   ? 35.521  1.183   -55.271 1.00 47.59  ?  1147 HOH B O      1 
HETATM 15600 O O      . HOH J 5 .   ? 15.767  -42.358 -42.646 1.00 35.16  ?  1148 HOH B O      1 
HETATM 15601 O O      . HOH J 5 .   ? 30.921  -14.908 -53.179 1.00 50.14  ?  1149 HOH B O      1 
HETATM 15602 O O      . HOH J 5 .   ? 25.550  4.338   -42.726 1.00 56.77  ?  1150 HOH B O      1 
HETATM 15603 O O      . HOH J 5 .   ? 24.331  -35.363 -62.267 1.00 40.86  ?  1151 HOH B O      1 
HETATM 15604 O O      . HOH J 5 .   ? 32.263  -26.396 -25.325 1.00 58.10  ?  1152 HOH B O      1 
HETATM 15605 O O      . HOH J 5 .   ? 34.184  3.512   -39.615 1.00 33.58  ?  1153 HOH B O      1 
HETATM 15606 O O      . HOH J 5 .   ? 35.058  -21.425 -21.352 1.00 40.28  ?  1154 HOH B O      1 
HETATM 15607 O O      . HOH J 5 .   ? 32.428  -25.427 -21.553 1.00 27.81  ?  1155 HOH B O      1 
HETATM 15608 O O      . HOH J 5 .   ? 24.866  4.103   -44.996 1.00 74.57  ?  1156 HOH B O      1 
HETATM 15609 O O      . HOH J 5 .   ? 31.691  -21.221 -26.380 1.00 49.35  ?  1157 HOH B O      1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N N   . SER A 2   ? 0.6019 0.4615 0.4339 0.2155  0.0422  0.0139  2   SER A N   
2     C CA  . SER A 2   ? 0.5866 0.4165 0.4370 0.2295  0.0349  0.0474  2   SER A CA  
3     C C   . SER A 2   ? 0.5433 0.3463 0.4260 0.2004  0.0422  0.0583  2   SER A C   
4     O O   . SER A 2   ? 0.5258 0.3260 0.4229 0.2110  0.0270  0.0610  2   SER A O   
5     C CB  . SER A 2   ? 0.5763 0.4502 0.4486 0.2363  0.0341  0.0495  2   SER A CB  
6     O OG  . SER A 2   ? 0.5299 0.4470 0.4523 0.2841  0.0176  0.0625  2   SER A OG  
11    N N   . GLN A 3   ? 0.5869 0.2946 0.4175 0.1711  0.0450  0.0713  3   GLN A N   
12    C CA  . GLN A 3   ? 0.6220 0.2820 0.4116 0.0610  0.0432  0.0777  3   GLN A CA  
13    C C   . GLN A 3   ? 0.4734 0.2034 0.3661 0.0554  0.0684  0.0607  3   GLN A C   
14    O O   . GLN A 3   ? 0.4419 0.1698 0.3676 0.0457  0.0814  0.0250  3   GLN A O   
15    C CB  . GLN A 3   ? 0.7720 0.2923 0.4432 -0.0125 0.0177  0.1236  3   GLN A CB  
16    C CG  . GLN A 3   ? 0.8940 0.3802 0.4738 -0.0653 0.0029  0.1204  3   GLN A CG  
17    C CD  . GLN A 3   ? 0.9843 0.4924 0.4951 -0.0732 -0.0187 0.1082  3   GLN A CD  
18    O OE1 . GLN A 3   ? 1.0038 0.5430 0.4993 -0.0938 -0.0284 0.1100  3   GLN A OE1 
19    N NE2 . GLN A 3   ? 1.0274 0.5389 0.5085 -0.0588 -0.0243 0.0848  3   GLN A NE2 
28    N N   . HIS A 4   ? 0.4038 0.2212 0.3329 0.0806  0.0603  0.0468  4   HIS A N   
29    C CA  . HIS A 4   ? 0.3298 0.2468 0.2980 0.1024  0.0473  0.0341  4   HIS A CA  
30    C C   . HIS A 4   ? 0.3072 0.2428 0.3008 0.0384  0.0301  0.0243  4   HIS A C   
31    O O   . HIS A 4   ? 0.2891 0.2277 0.2795 0.0386  0.0390  0.0292  4   HIS A O   
32    C CB  . HIS A 4   ? 0.3396 0.2662 0.2864 0.1082  0.0261  0.0545  4   HIS A CB  
33    C CG  . HIS A 4   ? 0.3045 0.2188 0.2698 0.0683  0.0144  0.0433  4   HIS A CG  
34    N ND1 . HIS A 4   ? 0.3004 0.2026 0.2590 0.0841  0.0147  0.0284  4   HIS A ND1 
35    C CD2 . HIS A 4   ? 0.2967 0.2038 0.2664 0.0239  0.0097  0.0128  4   HIS A CD2 
36    C CE1 . HIS A 4   ? 0.2673 0.1712 0.2566 0.0310  -0.0067 0.0210  4   HIS A CE1 
37    N NE2 . HIS A 4   ? 0.2637 0.1818 0.2619 0.0001  0.0062  -0.0210 4   HIS A NE2 
45    N N   . GLN A 5   ? 0.3067 0.3042 0.3124 0.0904  0.0197  -0.0015 5   GLN A N   
46    C CA  . GLN A 5   ? 0.3117 0.3606 0.3164 0.0886  -0.0092 0.0173  5   GLN A CA  
47    C C   . GLN A 5   ? 0.2959 0.3236 0.2980 0.0870  -0.0145 0.0365  5   GLN A C   
48    O O   . GLN A 5   ? 0.2874 0.3180 0.2852 0.1140  -0.0340 0.0255  5   GLN A O   
49    C CB  . GLN A 5   ? 0.3053 0.4825 0.3434 0.1004  0.0234  0.0121  5   GLN A CB  
50    C CG  . GLN A 5   ? 0.3669 0.5647 0.3716 0.0943  0.0188  0.0246  5   GLN A CG  
51    C CD  . GLN A 5   ? 0.4098 0.6382 0.3880 0.0813  0.0290  0.0255  5   GLN A CD  
52    O OE1 . GLN A 5   ? 0.3828 0.6439 0.3942 0.0903  0.0263  0.0248  5   GLN A OE1 
53    N NE2 . GLN A 5   ? 0.4284 0.6623 0.4001 0.0649  0.0099  0.0352  5   GLN A NE2 
62    N N   . ASN A 6   ? 0.3530 0.3226 0.2888 0.1034  -0.0153 0.0707  6   ASN A N   
63    C CA  . ASN A 6   ? 0.3356 0.2608 0.2898 0.1187  0.0083  0.0656  6   ASN A CA  
64    C C   . ASN A 6   ? 0.3336 0.1985 0.2620 0.0668  0.0078  0.0401  6   ASN A C   
65    O O   . ASN A 6   ? 0.3388 0.2065 0.2557 0.0448  0.0051  0.0306  6   ASN A O   
66    C CB  . ASN A 6   ? 0.4252 0.2878 0.3273 0.0694  0.0043  0.0825  6   ASN A CB  
67    C CG  . ASN A 6   ? 0.5201 0.3597 0.3766 0.0836  -0.0065 0.0837  6   ASN A CG  
68    O OD1 . ASN A 6   ? 0.5437 0.3993 0.3958 0.1340  -0.0357 0.0877  6   ASN A OD1 
69    N ND2 . ASN A 6   ? 0.5652 0.3920 0.3896 0.1009  0.0005  0.0972  6   ASN A ND2 
76    N N   . LEU A 7   ? 0.3266 0.1799 0.2399 0.0207  0.0031  0.0311  7   LEU A N   
77    C CA  . LEU A 7   ? 0.2892 0.1831 0.2288 0.0338  0.0047  0.0205  7   LEU A CA  
78    C C   . LEU A 7   ? 0.2768 0.2079 0.2228 0.0215  -0.0128 0.0114  7   LEU A C   
79    O O   . LEU A 7   ? 0.2538 0.1897 0.2120 -0.0010 -0.0357 0.0141  7   LEU A O   
80    C CB  . LEU A 7   ? 0.3557 0.1354 0.2434 0.0013  0.0357  0.0071  7   LEU A CB  
81    C CG  . LEU A 7   ? 0.4328 0.2304 0.2510 -0.0423 0.0658  0.0018  7   LEU A CG  
82    C CD1 . LEU A 7   ? 0.4574 0.3009 0.2491 -0.0367 0.0876  0.0103  7   LEU A CD1 
83    C CD2 . LEU A 7   ? 0.4504 0.3237 0.2564 -0.0553 0.0804  0.0262  7   LEU A CD2 
95    N N   . ILE A 8   ? 0.2693 0.1441 0.2245 0.0083  0.0233  0.0059  8   ILE A N   
96    C CA  . ILE A 8   ? 0.2412 0.1562 0.2179 0.0131  0.0076  0.0034  8   ILE A CA  
97    C C   . ILE A 8   ? 0.2662 0.1947 0.2148 0.0022  0.0066  0.0191  8   ILE A C   
98    O O   . ILE A 8   ? 0.2731 0.2087 0.2019 0.0074  0.0045  0.0149  8   ILE A O   
99    C CB  . ILE A 8   ? 0.2400 0.1740 0.2162 0.0300  0.0102  0.0202  8   ILE A CB  
100   C CG1 . ILE A 8   ? 0.2658 0.1946 0.2090 -0.0002 0.0348  0.0247  8   ILE A CG1 
101   C CG2 . ILE A 8   ? 0.3050 0.2424 0.2265 0.0142  -0.0060 0.0361  8   ILE A CG2 
102   C CD1 . ILE A 8   ? 0.3603 0.2348 0.2110 -0.0139 0.0141  0.0488  8   ILE A CD1 
114   N N   . ASP A 9   ? 0.2375 0.2107 0.2123 0.0740  0.0003  0.0125  9   ASP A N   
115   C CA  . ASP A 9   ? 0.2461 0.2525 0.2170 0.0574  -0.0070 0.0359  9   ASP A CA  
116   C C   . ASP A 9   ? 0.2328 0.2222 0.2121 0.0328  -0.0255 0.0416  9   ASP A C   
117   O O   . ASP A 9   ? 0.2736 0.2331 0.2231 0.0136  -0.0255 0.0509  9   ASP A O   
118   C CB  . ASP A 9   ? 0.2969 0.2655 0.2309 0.0460  -0.0343 0.0581  9   ASP A CB  
119   C CG  . ASP A 9   ? 0.3554 0.3009 0.2605 0.0633  -0.0450 0.0752  9   ASP A CG  
120   O OD1 . ASP A 9   ? 0.3482 0.2582 0.2875 0.0424  -0.0179 0.0515  9   ASP A OD1 
121   O OD2 . ASP A 9   ? 0.3700 0.3484 0.2903 0.1015  -0.0155 0.0766  9   ASP A OD2 
126   N N   . ARG A 10  ? 0.2451 0.1714 0.1950 -0.0043 -0.0190 0.0459  10  ARG A N   
127   C CA  . ARG A 10  ? 0.2869 0.1622 0.1792 0.0085  -0.0231 0.0433  10  ARG A CA  
128   C C   . ARG A 10  ? 0.2877 0.1773 0.1796 0.0142  -0.0122 0.0283  10  ARG A C   
129   O O   . ARG A 10  ? 0.2656 0.1550 0.2005 -0.0165 -0.0145 0.0157  10  ARG A O   
130   C CB  . ARG A 10  ? 0.3088 0.1321 0.1962 0.0064  -0.0087 0.0607  10  ARG A CB  
131   C CG  . ARG A 10  ? 0.3035 0.1461 0.2112 0.0002  -0.0036 0.0425  10  ARG A CG  
132   C CD  . ARG A 10  ? 0.3035 0.1803 0.2265 0.0534  0.0312  0.0048  10  ARG A CD  
133   N NE  . ARG A 10  ? 0.3082 0.2084 0.2456 0.0760  0.0289  0.0317  10  ARG A NE  
134   C CZ  . ARG A 10  ? 0.2931 0.2421 0.2754 0.0326  0.0201  0.0318  10  ARG A CZ  
135   N NH1 . ARG A 10  ? 0.3101 0.2420 0.2919 0.0376  0.0198  0.0344  10  ARG A NH1 
136   N NH2 . ARG A 10  ? 0.2977 0.2665 0.2820 0.0240  -0.0080 0.0407  10  ARG A NH2 
150   N N   . ASP A 11  ? 0.2384 0.2052 0.1741 -0.0052 -0.0107 0.0208  11  ASP A N   
151   C CA  . ASP A 11  ? 0.1890 0.1646 0.1767 -0.0118 -0.0303 0.0188  11  ASP A CA  
152   C C   . ASP A 11  ? 0.2023 0.1509 0.1775 0.0403  -0.0151 0.0133  11  ASP A C   
153   O O   . ASP A 11  ? 0.2171 0.1823 0.1849 0.0090  -0.0022 0.0018  11  ASP A O   
154   C CB  . ASP A 11  ? 0.2431 0.1960 0.1917 0.0191  -0.0124 0.0267  11  ASP A CB  
155   C CG  . ASP A 11  ? 0.2766 0.1718 0.1970 -0.0011 -0.0159 0.0297  11  ASP A CG  
156   O OD1 . ASP A 11  ? 0.2739 0.1664 0.2074 -0.0057 -0.0379 0.0033  11  ASP A OD1 
157   O OD2 . ASP A 11  ? 0.2757 0.1766 0.2028 0.0206  -0.0058 0.0564  11  ASP A OD2 
162   N N   . ARG A 12  ? 0.2318 0.1691 0.1735 0.0698  -0.0265 0.0011  12  ARG A N   
163   C CA  . ARG A 12  ? 0.2468 0.1728 0.1820 0.0317  -0.0368 -0.0041 12  ARG A CA  
164   C C   . ARG A 12  ? 0.2264 0.1985 0.1909 0.0102  -0.0277 0.0241  12  ARG A C   
165   O O   . ARG A 12  ? 0.2043 0.2057 0.2071 0.0262  0.0003  0.0451  12  ARG A O   
166   C CB  . ARG A 12  ? 0.2293 0.1552 0.1999 0.0355  -0.0283 0.0121  12  ARG A CB  
167   C CG  . ARG A 12  ? 0.2577 0.1894 0.2103 0.0332  0.0011  0.0073  12  ARG A CG  
168   C CD  . ARG A 12  ? 0.2792 0.1737 0.2287 0.0411  -0.0063 -0.0320 12  ARG A CD  
169   N NE  . ARG A 12  ? 0.2285 0.2174 0.2559 0.0247  -0.0277 -0.0171 12  ARG A NE  
170   C CZ  . ARG A 12  ? 0.2121 0.2235 0.2563 0.0390  -0.0031 -0.0115 12  ARG A CZ  
171   N NH1 . ARG A 12  ? 0.2100 0.2062 0.2657 0.0223  0.0029  -0.0334 12  ARG A NH1 
172   N NH2 . ARG A 12  ? 0.2566 0.2434 0.2635 0.0096  0.0092  -0.0097 12  ARG A NH2 
186   N N   . LYS A 13  ? 0.2457 0.2109 0.1886 0.0394  -0.0177 0.0188  13  LYS A N   
187   C CA  . LYS A 13  ? 0.2549 0.1697 0.1903 0.0022  -0.0322 0.0144  13  LYS A CA  
188   C C   . LYS A 13  ? 0.2485 0.1794 0.1806 -0.0286 -0.0186 0.0232  13  LYS A C   
189   O O   . LYS A 13  ? 0.2496 0.2089 0.1575 -0.0006 0.0044  0.0188  13  LYS A O   
190   C CB  . LYS A 13  ? 0.2739 0.2236 0.1970 0.0518  -0.0320 0.0233  13  LYS A CB  
191   C CG  . LYS A 13  ? 0.3111 0.2926 0.2286 0.1004  -0.0091 0.0855  13  LYS A CG  
192   C CD  . LYS A 13  ? 0.4046 0.3894 0.2650 0.1097  -0.0283 0.0798  13  LYS A CD  
193   C CE  . LYS A 13  ? 0.5367 0.4894 0.2980 0.1036  -0.0514 0.0895  13  LYS A CE  
194   N NZ  . LYS A 13  ? 0.6497 0.5891 0.3367 0.0901  -0.0333 0.0622  13  LYS A NZ  
208   N N   . VAL A 14  ? 0.2220 0.1934 0.1634 -0.0215 -0.0360 0.0367  14  VAL A N   
209   C CA  . VAL A 14  ? 0.2097 0.1717 0.1687 -0.0046 -0.0208 0.0495  14  VAL A CA  
210   C C   . VAL A 14  ? 0.2058 0.1724 0.1695 -0.0128 -0.0128 0.0418  14  VAL A C   
211   O O   . VAL A 14  ? 0.2308 0.1569 0.1729 0.0004  -0.0160 0.0265  14  VAL A O   
212   C CB  . VAL A 14  ? 0.2171 0.1727 0.1736 0.0205  0.0138  0.0312  14  VAL A CB  
213   C CG1 . VAL A 14  ? 0.2279 0.2145 0.1772 0.0286  0.0347  0.0337  14  VAL A CG1 
214   C CG2 . VAL A 14  ? 0.2272 0.1229 0.1792 -0.0157 0.0088  0.0213  14  VAL A CG2 
224   N N   . THR A 15  ? 0.1750 0.1404 0.1837 -0.0074 -0.0374 0.0496  15  THR A N   
225   C CA  . THR A 15  ? 0.1797 0.1493 0.1772 0.0267  -0.0519 0.0185  15  THR A CA  
226   C C   . THR A 15  ? 0.2134 0.1714 0.1866 -0.0017 -0.0368 0.0072  15  THR A C   
227   O O   . THR A 15  ? 0.2201 0.1735 0.2076 -0.0121 -0.0423 0.0242  15  THR A O   
228   C CB  . THR A 15  ? 0.2105 0.1451 0.1930 -0.0019 -0.0502 0.0361  15  THR A CB  
229   O OG1 . THR A 15  ? 0.2257 0.1303 0.2118 -0.0132 -0.0168 0.0090  15  THR A OG1 
230   C CG2 . THR A 15  ? 0.2075 0.2362 0.2024 0.0359  -0.0482 0.0325  15  THR A CG2 
238   N N   . PHE A 16  ? 0.2045 0.1369 0.1746 -0.0154 -0.0304 0.0277  16  PHE A N   
239   C CA  . PHE A 16  ? 0.1853 0.1409 0.1609 -0.0049 -0.0091 0.0111  16  PHE A CA  
240   C C   . PHE A 16  ? 0.1787 0.1840 0.1649 -0.0040 -0.0193 0.0068  16  PHE A C   
241   O O   . PHE A 16  ? 0.1438 0.1984 0.1756 -0.0139 -0.0086 0.0001  16  PHE A O   
242   C CB  . PHE A 16  ? 0.1746 0.1290 0.1570 -0.0213 -0.0105 0.0021  16  PHE A CB  
243   C CG  . PHE A 16  ? 0.1636 0.1496 0.1582 -0.0060 -0.0087 0.0185  16  PHE A CG  
244   C CD1 . PHE A 16  ? 0.2122 0.1222 0.1820 -0.0438 -0.0053 0.0255  16  PHE A CD1 
245   C CD2 . PHE A 16  ? 0.2249 0.1492 0.1753 -0.0555 -0.0190 0.0200  16  PHE A CD2 
246   C CE1 . PHE A 16  ? 0.2622 0.1609 0.1892 -0.0465 -0.0162 0.0086  16  PHE A CE1 
247   C CE2 . PHE A 16  ? 0.2285 0.1688 0.1850 -0.0618 0.0040  0.0054  16  PHE A CE2 
248   C CZ  . PHE A 16  ? 0.2626 0.1300 0.1985 -0.0585 -0.0364 0.0287  16  PHE A CZ  
258   N N   . HIS A 17  ? 0.2071 0.1720 0.1760 -0.0205 -0.0294 -0.0088 17  HIS A N   
259   C CA  . HIS A 17  ? 0.1554 0.1367 0.1735 -0.0307 -0.0347 -0.0166 17  HIS A CA  
260   C C   . HIS A 17  ? 0.2027 0.1223 0.1600 0.0037  -0.0376 -0.0277 17  HIS A C   
261   O O   . HIS A 17  ? 0.1979 0.1384 0.1620 0.0066  -0.0329 -0.0183 17  HIS A O   
262   C CB  . HIS A 17  ? 0.1781 0.1325 0.1813 -0.0359 -0.0023 -0.0040 17  HIS A CB  
263   C CG  . HIS A 17  ? 0.1830 0.1230 0.1763 -0.0149 -0.0042 0.0173  17  HIS A CG  
264   N ND1 . HIS A 17  ? 0.2260 0.1286 0.1879 -0.0301 -0.0467 0.0123  17  HIS A ND1 
265   C CD2 . HIS A 17  ? 0.2028 0.1273 0.1767 0.0206  0.0014  0.0105  17  HIS A CD2 
266   C CE1 . HIS A 17  ? 0.2227 0.1300 0.1729 -0.0132 -0.0331 0.0048  17  HIS A CE1 
267   N NE2 . HIS A 17  ? 0.2464 0.1465 0.1668 0.0214  -0.0298 0.0022  17  HIS A NE2 
276   N N   . ALA A 18  ? 0.1868 0.1547 0.1613 -0.0143 -0.0261 0.0022  18  ALA A N   
277   C CA  . ALA A 18  ? 0.1865 0.1553 0.1633 0.0129  -0.0285 0.0161  18  ALA A CA  
278   C C   . ALA A 18  ? 0.1475 0.1111 0.1761 0.0044  -0.0370 0.0046  18  ALA A C   
279   O O   . ALA A 18  ? 0.1699 0.1484 0.1853 0.0288  -0.0219 -0.0099 18  ALA A O   
280   C CB  . ALA A 18  ? 0.1731 0.1807 0.1662 0.0115  -0.0121 -0.0021 18  ALA A CB  
286   N N   A SER A 19  ? 0.1557 0.1270 0.1809 -0.0115 -0.0045 0.0052  19  SER A N   
287   N N   B SER A 19  ? 0.1561 0.1323 0.1777 -0.0296 -0.0159 0.0017  19  SER A N   
288   C CA  A SER A 19  ? 0.1862 0.1641 0.1815 -0.0076 0.0208  0.0170  19  SER A CA  
289   C CA  B SER A 19  ? 0.1927 0.1768 0.1771 -0.0343 -0.0104 0.0115  19  SER A CA  
290   C C   A SER A 19  ? 0.1982 0.1713 0.1736 -0.0039 0.0086  0.0026  19  SER A C   
291   C C   B SER A 19  ? 0.2185 0.1754 0.1708 0.0034  -0.0089 0.0124  19  SER A C   
292   O O   A SER A 19  ? 0.1773 0.2385 0.1641 -0.0166 0.0254  0.0027  19  SER A O   
293   O O   B SER A 19  ? 0.2615 0.2144 0.1606 0.0375  0.0008  0.0287  19  SER A O   
294   C CB  A SER A 19  ? 0.2268 0.1866 0.1838 -0.0163 0.0318  0.0425  19  SER A CB  
295   C CB  B SER A 19  ? 0.2221 0.2143 0.1768 -0.0715 -0.0358 0.0169  19  SER A CB  
296   O OG  A SER A 19  ? 0.2473 0.1543 0.1905 0.0091  0.0531  0.0780  19  SER A OG  
297   O OG  B SER A 19  ? 0.2298 0.2382 0.1806 -0.0429 -0.0336 0.0355  19  SER A OG  
308   N N   . THR A 20  ? 0.2037 0.1227 0.1733 -0.0026 -0.0155 -0.0011 20  THR A N   
309   C CA  . THR A 20  ? 0.1537 0.1631 0.1769 -0.0018 -0.0191 -0.0055 20  THR A CA  
310   C C   . THR A 20  ? 0.1558 0.1890 0.1835 0.0034  -0.0024 0.0109  20  THR A C   
311   O O   . THR A 20  ? 0.1700 0.1744 0.1789 0.0185  -0.0057 0.0028  20  THR A O   
312   C CB  . THR A 20  ? 0.1959 0.1626 0.1682 -0.0324 -0.0440 0.0213  20  THR A CB  
313   O OG1 . THR A 20  ? 0.1883 0.1645 0.1743 0.0032  -0.0434 -0.0187 20  THR A OG1 
314   C CG2 . THR A 20  ? 0.2206 0.2117 0.1783 0.0002  -0.0362 0.0341  20  THR A CG2 
323   N N   . HIS A 21  ? 0.1569 0.1755 0.1828 0.0247  -0.0081 -0.0070 21  HIS A N   
324   C CA  . HIS A 21  ? 0.1641 0.1807 0.1861 -0.0053 -0.0358 0.0021  21  HIS A CA  
325   C C   . HIS A 21  ? 0.1530 0.1647 0.1910 0.0172  -0.0440 0.0060  21  HIS A C   
326   O O   . HIS A 21  ? 0.1994 0.1820 0.1934 -0.0030 -0.0292 0.0178  21  HIS A O   
327   C CB  . HIS A 21  ? 0.1762 0.2535 0.1878 0.0127  -0.0143 0.0139  21  HIS A CB  
328   C CG  . HIS A 21  ? 0.1859 0.2372 0.1903 -0.0038 -0.0109 -0.0082 21  HIS A CG  
329   N ND1 . HIS A 21  ? 0.1630 0.2590 0.1978 -0.0174 -0.0220 -0.0194 21  HIS A ND1 
330   C CD2 . HIS A 21  ? 0.1975 0.2753 0.1933 -0.0147 -0.0134 -0.0144 21  HIS A CD2 
331   C CE1 . HIS A 21  ? 0.1832 0.2475 0.1917 -0.0412 -0.0181 -0.0363 21  HIS A CE1 
332   N NE2 . HIS A 21  ? 0.2060 0.2466 0.2054 -0.0364 -0.0309 -0.0116 21  HIS A NE2 
340   N N   . LEU A 22  ? 0.1835 0.1289 0.1941 0.0357  -0.0355 -0.0046 22  LEU A N   
341   C CA  . LEU A 22  ? 0.1958 0.1615 0.1971 -0.0063 -0.0355 0.0067  22  LEU A CA  
342   C C   . LEU A 22  ? 0.1750 0.1796 0.1928 -0.0059 -0.0343 0.0261  22  LEU A C   
343   O O   . LEU A 22  ? 0.2276 0.1872 0.1842 -0.0081 -0.0385 0.0354  22  LEU A O   
344   C CB  . LEU A 22  ? 0.1910 0.1328 0.1969 -0.0108 -0.0356 -0.0220 22  LEU A CB  
345   C CG  . LEU A 22  ? 0.1886 0.1375 0.1993 -0.0103 -0.0286 0.0027  22  LEU A CG  
346   C CD1 . LEU A 22  ? 0.1969 0.1787 0.1993 -0.0123 -0.0046 -0.0037 22  LEU A CD1 
347   C CD2 . LEU A 22  ? 0.1552 0.1599 0.1959 -0.0647 -0.0236 0.0046  22  LEU A CD2 
359   N N   . ARG A 23  ? 0.1865 0.2056 0.1931 -0.0093 -0.0620 0.0085  23  ARG A N   
360   C CA  . ARG A 23  ? 0.1653 0.2231 0.2113 -0.0210 -0.0389 -0.0062 23  ARG A CA  
361   C C   . ARG A 23  ? 0.2051 0.1967 0.2072 0.0297  -0.0266 0.0130  23  ARG A C   
362   O O   . ARG A 23  ? 0.2250 0.2159 0.2033 0.0287  -0.0530 -0.0066 23  ARG A O   
363   C CB  . ARG A 23  ? 0.1627 0.2624 0.2425 -0.0012 -0.0429 -0.0037 23  ARG A CB  
364   C CG  . ARG A 23  ? 0.2099 0.3110 0.2670 -0.0051 -0.0601 -0.0061 23  ARG A CG  
365   C CD  . ARG A 23  ? 0.2769 0.3547 0.3004 0.0132  -0.0621 0.0245  23  ARG A CD  
366   N NE  . ARG A 23  ? 0.2649 0.4097 0.3372 -0.0098 -0.0913 0.0254  23  ARG A NE  
367   C CZ  . ARG A 23  ? 0.3251 0.4500 0.3672 -0.0391 -0.1032 0.0227  23  ARG A CZ  
368   N NH1 . ARG A 23  ? 0.3634 0.4684 0.3729 -0.0664 -0.1505 0.0240  23  ARG A NH1 
369   N NH2 . ARG A 23  ? 0.3075 0.4386 0.3779 -0.0497 -0.0847 0.0206  23  ARG A NH2 
383   N N   . ASP A 24  ? 0.1569 0.1858 0.2132 0.0054  -0.0302 0.0170  24  ASP A N   
384   C CA  . ASP A 24  ? 0.1776 0.1987 0.2304 0.0188  -0.0334 0.0060  24  ASP A CA  
385   C C   . ASP A 24  ? 0.1709 0.2180 0.2274 0.0301  -0.0291 0.0210  24  ASP A C   
386   O O   . ASP A 24  ? 0.2178 0.2151 0.2387 0.0510  -0.0385 0.0204  24  ASP A O   
387   C CB  . ASP A 24  ? 0.1849 0.2371 0.2700 -0.0074 -0.0281 0.0074  24  ASP A CB  
388   C CG  . ASP A 24  ? 0.2258 0.2442 0.2967 0.0173  -0.0341 0.0306  24  ASP A CG  
389   O OD1 . ASP A 24  ? 0.2508 0.2587 0.3019 -0.0281 -0.0766 0.0101  24  ASP A OD1 
390   O OD2 . ASP A 24  ? 0.2735 0.2691 0.3208 -0.0422 -0.0237 0.0464  24  ASP A OD2 
395   N N   . PHE A 25  ? 0.1450 0.1811 0.2058 0.0463  -0.0461 0.0102  25  PHE A N   
396   C CA  . PHE A 25  ? 0.2351 0.1799 0.2003 0.0146  -0.0321 -0.0031 25  PHE A CA  
397   C C   . PHE A 25  ? 0.2197 0.1786 0.2070 -0.0074 -0.0152 -0.0128 25  PHE A C   
398   O O   . PHE A 25  ? 0.2278 0.2100 0.1962 0.0187  -0.0248 0.0060  25  PHE A O   
399   C CB  . PHE A 25  ? 0.2416 0.1849 0.2046 0.0320  -0.0564 -0.0142 25  PHE A CB  
400   C CG  . PHE A 25  ? 0.1890 0.2128 0.1892 0.0512  -0.0369 -0.0323 25  PHE A CG  
401   C CD1 . PHE A 25  ? 0.2395 0.1956 0.1937 0.0498  -0.0231 -0.0524 25  PHE A CD1 
402   C CD2 . PHE A 25  ? 0.1649 0.2216 0.1923 0.0202  -0.0340 -0.0122 25  PHE A CD2 
403   C CE1 . PHE A 25  ? 0.2186 0.2223 0.2012 0.0142  -0.0230 -0.0487 25  PHE A CE1 
404   C CE2 . PHE A 25  ? 0.1970 0.2289 0.1873 0.0318  -0.0299 -0.0107 25  PHE A CE2 
405   C CZ  . PHE A 25  ? 0.1966 0.2166 0.2009 0.0250  -0.0175 -0.0102 25  PHE A CZ  
415   N N   . ALA A 26  ? 0.2193 0.1969 0.2156 0.0220  -0.0234 -0.0191 26  ALA A N   
416   C CA  . ALA A 26  ? 0.2042 0.1660 0.2270 0.0211  -0.0188 -0.0104 26  ALA A CA  
417   C C   . ALA A 26  ? 0.2324 0.1636 0.2331 0.0272  -0.0366 0.0284  26  ALA A C   
418   O O   . ALA A 26  ? 0.2294 0.2127 0.2358 0.0064  -0.0421 0.0476  26  ALA A O   
419   C CB  . ALA A 26  ? 0.2028 0.1344 0.2378 0.0446  -0.0164 -0.0234 26  ALA A CB  
425   N N   . HIS A 27  ? 0.2270 0.2179 0.2445 0.0226  -0.0520 0.0245  27  HIS A N   
426   C CA  . HIS A 27  ? 0.2528 0.2060 0.2486 0.0190  -0.0790 0.0137  27  HIS A CA  
427   C C   . HIS A 27  ? 0.2522 0.2607 0.2692 0.0072  -0.0593 0.0119  27  HIS A C   
428   O O   . HIS A 27  ? 0.2916 0.3096 0.2742 0.0418  -0.0748 -0.0253 27  HIS A O   
429   C CB  . HIS A 27  ? 0.2977 0.2480 0.2350 0.0690  -0.0723 -0.0263 27  HIS A CB  
430   C CG  . HIS A 27  ? 0.3307 0.3179 0.2350 0.0805  -0.0977 -0.0530 27  HIS A CG  
431   N ND1 . HIS A 27  ? 0.4112 0.4210 0.2499 0.1281  -0.0681 -0.0782 27  HIS A ND1 
432   C CD2 . HIS A 27  ? 0.3131 0.2961 0.2379 0.0943  -0.0939 -0.0533 27  HIS A CD2 
433   C CE1 . HIS A 27  ? 0.4045 0.4297 0.2478 0.1458  -0.0809 -0.0697 27  HIS A CE1 
434   N NE2 . HIS A 27  ? 0.3351 0.3620 0.2450 0.1328  -0.0984 -0.0392 27  HIS A NE2 
442   N N   . GLY A 28  ? 0.2180 0.2417 0.2765 0.0418  -0.0698 0.0163  28  GLY A N   
443   C CA  . GLY A 28  ? 0.2528 0.2711 0.2970 0.0745  -0.0308 0.0009  28  GLY A CA  
444   C C   . GLY A 28  ? 0.2225 0.2824 0.3264 0.0948  -0.0233 -0.0085 28  GLY A C   
445   O O   . GLY A 28  ? 0.2897 0.2798 0.3542 0.1516  0.0216  0.0103  28  GLY A O   
449   N N   . GLU A 29  ? 0.2134 0.3459 0.3188 0.0779  -0.0879 0.0001  29  GLU A N   
450   C CA  . GLU A 29  ? 0.2503 0.4354 0.3250 0.0588  -0.0749 0.0004  29  GLU A CA  
451   C C   . GLU A 29  ? 0.2133 0.4491 0.2914 0.0388  -0.0299 0.0154  29  GLU A C   
452   O O   . GLU A 29  ? 0.3331 0.5788 0.3132 0.0253  -0.0319 0.0321  29  GLU A O   
453   C CB  . GLU A 29  ? 0.3696 0.5186 0.3767 0.0621  -0.1105 -0.0120 29  GLU A CB  
454   C CG  . GLU A 29  ? 0.5782 0.6445 0.4305 -0.0325 -0.1256 -0.0377 29  GLU A CG  
455   C CD  . GLU A 29  ? 0.6962 0.7524 0.4824 -0.0981 -0.1431 -0.0711 29  GLU A CD  
456   O OE1 . GLU A 29  ? 0.7546 0.7815 0.5090 -0.1057 -0.1486 -0.0789 29  GLU A OE1 
457   O OE2 . GLU A 29  ? 0.7236 0.7918 0.4928 -0.1426 -0.1728 -0.1041 29  GLU A OE2 
464   N N   . ALA A 30  ? 0.2107 0.3149 0.2584 0.0282  -0.0099 0.0029  30  ALA A N   
465   C CA  . ALA A 30  ? 0.2192 0.2569 0.2587 -0.0076 -0.0113 -0.0017 30  ALA A CA  
466   C C   . ALA A 30  ? 0.2517 0.2225 0.2623 0.0278  -0.0048 -0.0267 30  ALA A C   
467   O O   . ALA A 30  ? 0.2744 0.1742 0.2665 0.0233  -0.0122 -0.0194 30  ALA A O   
468   C CB  . ALA A 30  ? 0.2798 0.2215 0.2621 0.0439  -0.0133 0.0220  30  ALA A CB  
474   N N   . PRO A 31  ? 0.2092 0.2458 0.2550 0.0142  -0.0012 -0.0142 31  PRO A N   
475   C CA  . PRO A 31  ? 0.2182 0.2216 0.2577 0.0604  -0.0074 -0.0098 31  PRO A CA  
476   C C   . PRO A 31  ? 0.1963 0.1637 0.2501 0.0119  -0.0286 -0.0011 31  PRO A C   
477   O O   . PRO A 31  ? 0.2378 0.1824 0.2632 0.0465  -0.0457 0.0042  31  PRO A O   
478   C CB  . PRO A 31  ? 0.2820 0.2580 0.2677 0.0406  0.0078  -0.0227 31  PRO A CB  
479   C CG  . PRO A 31  ? 0.2683 0.2852 0.2700 0.0466  0.0144  -0.0319 31  PRO A CG  
480   C CD  . PRO A 31  ? 0.2245 0.2844 0.2608 0.0240  0.0112  -0.0290 31  PRO A CD  
488   N N   . GLY A 32  ? 0.2095 0.1364 0.2437 -0.0101 -0.0226 -0.0016 32  GLY A N   
489   C CA  . GLY A 32  ? 0.2304 0.1633 0.2447 0.0151  -0.0125 -0.0243 32  GLY A CA  
490   C C   . GLY A 32  ? 0.2024 0.1421 0.2339 0.0064  -0.0149 -0.0110 32  GLY A C   
491   O O   . GLY A 32  ? 0.2055 0.2067 0.2346 0.0286  0.0083  0.0146  32  GLY A O   
495   N N   . ARG A 33  ? 0.2265 0.1604 0.2455 0.0084  -0.0154 0.0064  33  ARG A N   
496   C CA  . ARG A 33  ? 0.2372 0.1470 0.2366 0.0467  0.0084  0.0249  33  ARG A CA  
497   C C   . ARG A 33  ? 0.2549 0.1785 0.2373 0.0388  0.0145  0.0205  33  ARG A C   
498   O O   . ARG A 33  ? 0.2128 0.1721 0.2588 0.0280  0.0164  0.0198  33  ARG A O   
499   C CB  . ARG A 33  ? 0.2210 0.1852 0.2379 0.0114  0.0032  -0.0047 33  ARG A CB  
500   C CG  . ARG A 33  ? 0.2806 0.2223 0.2346 -0.0251 0.0151  0.0105  33  ARG A CG  
501   C CD  . ARG A 33  ? 0.2967 0.2513 0.2338 -0.0514 0.0016  0.0028  33  ARG A CD  
502   N NE  . ARG A 33  ? 0.2639 0.2498 0.2390 -0.0019 -0.0301 0.0335  33  ARG A NE  
503   C CZ  . ARG A 33  ? 0.3076 0.2984 0.2790 -0.0229 0.0165  0.0120  33  ARG A CZ  
504   N NH1 . ARG A 33  ? 0.2711 0.2880 0.3004 -0.0163 0.0027  -0.0045 33  ARG A NH1 
505   N NH2 . ARG A 33  ? 0.3248 0.3682 0.2901 -0.0266 0.0209  0.0090  33  ARG A NH2 
519   N N   . VAL A 34  ? 0.2366 0.1605 0.2195 -0.0005 0.0151  0.0261  34  VAL A N   
520   C CA  . VAL A 34  ? 0.2332 0.1270 0.2121 -0.0160 0.0137  0.0312  34  VAL A CA  
521   C C   . VAL A 34  ? 0.2527 0.1313 0.2075 0.0335  -0.0085 0.0336  34  VAL A C   
522   O O   . VAL A 34  ? 0.2896 0.1631 0.2100 0.0338  0.0000  0.0120  34  VAL A O   
523   C CB  . VAL A 34  ? 0.2003 0.1466 0.2187 0.0373  0.0063  0.0118  34  VAL A CB  
524   C CG1 . VAL A 34  ? 0.2591 0.2478 0.2260 0.0047  0.0130  0.0469  34  VAL A CG1 
525   C CG2 . VAL A 34  ? 0.1945 0.1881 0.2234 0.0083  0.0076  0.0045  34  VAL A CG2 
535   N N   A MET A 35  ? 0.2404 0.1493 0.2067 0.0322  -0.0139 0.0200  35  MET A N   
536   N N   B MET A 35  ? 0.2522 0.1361 0.2105 0.0520  -0.0097 0.0135  35  MET A N   
537   C CA  A MET A 35  ? 0.2270 0.1557 0.2087 0.0239  -0.0096 0.0312  35  MET A CA  
538   C CA  B MET A 35  ? 0.2511 0.1333 0.2184 0.0611  0.0002  0.0264  35  MET A CA  
539   C C   A MET A 35  ? 0.2508 0.1648 0.2181 0.0076  0.0079  0.0040  35  MET A C   
540   C C   B MET A 35  ? 0.2547 0.1628 0.2242 0.0237  0.0138  -0.0058 35  MET A C   
541   O O   A MET A 35  ? 0.2574 0.1922 0.2277 0.0106  0.0199  0.0020  35  MET A O   
542   O O   B MET A 35  ? 0.2481 0.2101 0.2380 0.0284  0.0303  -0.0071 35  MET A O   
543   C CB  A MET A 35  ? 0.2396 0.1911 0.2066 -0.0075 -0.0173 0.0523  35  MET A CB  
544   C CB  B MET A 35  ? 0.3115 0.1801 0.2294 0.0392  0.0058  0.0382  35  MET A CB  
545   C CG  A MET A 35  ? 0.2255 0.2168 0.2036 0.0014  -0.0094 0.0717  35  MET A CG  
546   C CG  B MET A 35  ? 0.3137 0.2023 0.2406 0.0783  0.0326  0.0353  35  MET A CG  
547   S SD  A MET A 35  ? 0.2293 0.2698 0.2116 -0.0174 -0.0135 0.0716  35  MET A SD  
548   S SD  B MET A 35  ? 0.3313 0.2397 0.2605 0.0550  0.0369  0.0280  35  MET A SD  
549   C CE  A MET A 35  ? 0.1634 0.2955 0.2038 -0.0032 0.0230  0.0699  35  MET A CE  
550   C CE  B MET A 35  ? 0.3723 0.2220 0.2509 0.0372  0.0403  0.0344  35  MET A CE  
569   N N   . ALA A 36  ? 0.2781 0.1422 0.2203 -0.0107 0.0216  0.0002  36  ALA A N   
570   C CA  . ALA A 36  ? 0.3036 0.1800 0.2251 -0.0476 0.0174  -0.0056 36  ALA A CA  
571   C C   . ALA A 36  ? 0.3068 0.1604 0.2262 -0.0879 0.0031  0.0001  36  ALA A C   
572   O O   . ALA A 36  ? 0.3436 0.1915 0.2383 -0.0568 -0.0022 0.0052  36  ALA A O   
573   C CB  . ALA A 36  ? 0.3758 0.2503 0.2339 -0.0403 -0.0131 -0.0289 36  ALA A CB  
580   N N   . GLY A 37  ? 0.2939 0.1542 0.2164 -0.0234 -0.0028 0.0181  37  GLY A N   
581   C CA  . GLY A 37  ? 0.3087 0.1466 0.2222 0.0276  0.0000  0.0163  37  GLY A CA  
582   C C   . GLY A 37  ? 0.2822 0.1364 0.2221 -0.0311 -0.0041 0.0144  37  GLY A C   
583   O O   . GLY A 37  ? 0.2625 0.1436 0.2254 -0.0221 0.0100  0.0208  37  GLY A O   
587   N N   . GLY A 38  ? 0.2252 0.1741 0.2249 -0.0391 0.0222  -0.0030 38  GLY A N   
588   C CA  . GLY A 38  ? 0.2569 0.1693 0.2306 -0.0244 0.0127  0.0100  38  GLY A CA  
589   C C   . GLY A 38  ? 0.2488 0.1173 0.2308 -0.0292 0.0356  -0.0181 38  GLY A C   
590   O O   . GLY A 38  ? 0.2536 0.1777 0.2258 0.0102  0.0181  -0.0041 38  GLY A O   
594   N N   . GLU A 39  ? 0.2635 0.1867 0.2427 0.0000  0.0243  -0.0260 39  GLU A N   
595   C CA  . GLU A 39  ? 0.2807 0.1580 0.2481 0.0382  0.0238  -0.0368 39  GLU A CA  
596   C C   . GLU A 39  ? 0.2415 0.1747 0.2386 -0.0075 0.0223  -0.0209 39  GLU A C   
597   O O   . GLU A 39  ? 0.2498 0.1696 0.2491 0.0147  0.0134  -0.0097 39  GLU A O   
598   C CB  . GLU A 39  ? 0.4358 0.1957 0.2655 -0.0118 0.0170  -0.0426 39  GLU A CB  
599   C CG  . GLU A 39  ? 0.5983 0.3144 0.2830 -0.0150 0.0217  -0.0424 39  GLU A CG  
600   C CD  . GLU A 39  ? 0.7682 0.4754 0.3193 0.0157  0.0046  -0.0436 39  GLU A CD  
601   O OE1 . GLU A 39  ? 0.8289 0.5278 0.3180 0.0555  0.0048  -0.0513 39  GLU A OE1 
602   O OE2 . GLU A 39  ? 0.8161 0.5163 0.3444 -0.0234 0.0073  -0.0449 39  GLU A OE2 
609   N N   . GLY A 40  ? 0.2586 0.1752 0.2295 -0.0251 0.0296  -0.0143 40  GLY A N   
610   C CA  . GLY A 40  ? 0.2394 0.1847 0.2107 0.0065  -0.0065 0.0167  40  GLY A CA  
611   C C   . GLY A 40  ? 0.1947 0.1603 0.2089 0.0262  -0.0010 -0.0225 40  GLY A C   
612   O O   . GLY A 40  ? 0.2555 0.1397 0.2258 0.0347  0.0122  -0.0114 40  GLY A O   
616   N N   . ILE A 41  ? 0.2157 0.1638 0.2097 -0.0184 0.0123  -0.0124 41  ILE A N   
617   C CA  . ILE A 41  ? 0.2111 0.1589 0.2123 -0.0092 0.0037  -0.0182 41  ILE A CA  
618   C C   . ILE A 41  ? 0.2192 0.1610 0.2146 -0.0019 0.0036  -0.0152 41  ILE A C   
619   O O   . ILE A 41  ? 0.2766 0.1993 0.2088 -0.0201 -0.0054 -0.0291 41  ILE A O   
620   C CB  . ILE A 41  ? 0.2233 0.1973 0.2111 0.0199  0.0299  -0.0082 41  ILE A CB  
621   C CG1 . ILE A 41  ? 0.2784 0.2144 0.2158 0.0137  0.0464  0.0034  41  ILE A CG1 
622   C CG2 . ILE A 41  ? 0.2308 0.1764 0.2098 -0.0198 0.0129  -0.0127 41  ILE A CG2 
623   C CD1 . ILE A 41  ? 0.3004 0.2663 0.2227 -0.0129 0.0157  0.0013  41  ILE A CD1 
635   N N   . HIS A 42  ? 0.2290 0.1665 0.2259 -0.0097 0.0210  -0.0133 42  HIS A N   
636   C CA  . HIS A 42  ? 0.2689 0.1906 0.2333 -0.0325 0.0267  0.0000  42  HIS A CA  
637   C C   . HIS A 42  ? 0.2724 0.1883 0.2316 -0.0330 0.0299  0.0070  42  HIS A C   
638   O O   . HIS A 42  ? 0.2536 0.1740 0.2273 -0.0428 0.0070  -0.0069 42  HIS A O   
639   C CB  . HIS A 42  ? 0.3010 0.1956 0.2498 -0.0003 0.0210  -0.0051 42  HIS A CB  
640   C CG  . HIS A 42  ? 0.3287 0.2580 0.2768 0.0350  0.0319  -0.0557 42  HIS A CG  
641   N ND1 . HIS A 42  ? 0.3740 0.3712 0.2963 0.0243  0.0487  -0.0627 42  HIS A ND1 
642   C CD2 . HIS A 42  ? 0.3657 0.2868 0.2856 -0.0643 0.0706  -0.0545 42  HIS A CD2 
643   C CE1 . HIS A 42  ? 0.3717 0.3387 0.2998 -0.0133 0.0578  -0.0757 42  HIS A CE1 
644   N NE2 . HIS A 42  ? 0.3762 0.2807 0.2967 -0.0735 0.0703  -0.0663 42  HIS A NE2 
652   N N   A VAL A 43  ? 0.2547 0.1790 0.2235 -0.0411 0.0149  0.0241  43  VAL A N   
653   N N   B VAL A 43  ? 0.2544 0.1695 0.2225 -0.0260 0.0278  0.0142  43  VAL A N   
654   C CA  A VAL A 43  ? 0.2575 0.1832 0.2228 -0.0365 0.0149  0.0228  43  VAL A CA  
655   C CA  B VAL A 43  ? 0.2459 0.1539 0.2147 -0.0191 0.0333  0.0137  43  VAL A CA  
656   C C   A VAL A 43  ? 0.2751 0.2104 0.2220 -0.0530 -0.0079 0.0237  43  VAL A C   
657   C C   B VAL A 43  ? 0.2619 0.1766 0.2188 -0.0462 0.0126  0.0179  43  VAL A C   
658   O O   A VAL A 43  ? 0.2718 0.2496 0.2207 -0.0593 -0.0234 0.0418  43  VAL A O   
659   O O   B VAL A 43  ? 0.2617 0.1925 0.2218 -0.0590 0.0073  0.0282  43  VAL A O   
660   C CB  A VAL A 43  ? 0.3057 0.1913 0.2281 -0.0670 0.0405  0.0275  43  VAL A CB  
661   C CB  B VAL A 43  ? 0.2543 0.1301 0.2115 -0.0150 0.0560  0.0131  43  VAL A CB  
662   C CG1 A VAL A 43  ? 0.3044 0.2303 0.2353 -0.1286 0.0487  0.0465  43  VAL A CG1 
663   C CG1 B VAL A 43  ? 0.1646 0.0799 0.1795 -0.0390 0.0430  0.0206  43  VAL A CG1 
664   C CG2 A VAL A 43  ? 0.2648 0.1430 0.2102 -0.0650 0.0708  0.0300  43  VAL A CG2 
665   C CG2 B VAL A 43  ? 0.2679 0.1664 0.2175 0.0145  0.0765  0.0035  43  VAL A CG2 
684   N N   . VAL A 44  ? 0.2555 0.1579 0.2166 -0.0622 0.0117  0.0174  44  VAL A N   
685   C CA  . VAL A 44  ? 0.3098 0.1555 0.2193 0.0151  0.0151  0.0289  44  VAL A CA  
686   C C   . VAL A 44  ? 0.2863 0.1588 0.2309 0.0186  0.0165  0.0211  44  VAL A C   
687   O O   . VAL A 44  ? 0.2690 0.1964 0.2248 0.0075  0.0141  0.0064  44  VAL A O   
688   C CB  . VAL A 44  ? 0.3385 0.2213 0.2278 0.0279  0.0392  0.0159  44  VAL A CB  
689   C CG1 . VAL A 44  ? 0.3486 0.2057 0.2379 -0.0123 0.0310  0.0253  44  VAL A CG1 
690   C CG2 . VAL A 44  ? 0.3424 0.2800 0.2331 0.0014  0.0712  -0.0086 44  VAL A CG2 
701   N N   . ASP A 45  ? 0.2782 0.1909 0.2298 -0.0055 0.0262  0.0216  45  ASP A N   
702   C CA  . ASP A 45  ? 0.2665 0.1626 0.2300 0.0163  0.0576  0.0029  45  ASP A CA  
703   C C   . ASP A 45  ? 0.3134 0.1460 0.2372 0.0568  0.0537  0.0090  45  ASP A C   
704   O O   . ASP A 45  ? 0.3446 0.1689 0.2221 0.0715  0.0518  0.0070  45  ASP A O   
705   C CB  . ASP A 45  ? 0.2925 0.1427 0.2341 0.0123  0.0346  0.0079  45  ASP A CB  
706   C CG  . ASP A 45  ? 0.3276 0.1869 0.2350 0.0191  0.0356  0.0259  45  ASP A CG  
707   O OD1 . ASP A 45  ? 0.3085 0.1842 0.2372 0.0728  0.0529  0.0127  45  ASP A OD1 
708   O OD2 . ASP A 45  ? 0.3464 0.1947 0.2303 0.0486  0.0246  0.0330  45  ASP A OD2 
713   N N   . LYS A 46  ? 0.3077 0.1442 0.2395 0.0514  0.0281  0.0280  46  LYS A N   
714   C CA  . LYS A 46  ? 0.3513 0.1409 0.2580 0.0501  0.0577  0.0287  46  LYS A CA  
715   C C   . LYS A 46  ? 0.4261 0.1914 0.2689 0.0738  0.0635  0.0421  46  LYS A C   
716   O O   . LYS A 46  ? 0.4557 0.2274 0.2879 0.0764  0.0617  0.0503  46  LYS A O   
717   C CB  . LYS A 46  ? 0.3841 0.1774 0.2733 0.0132  0.0759  0.0156  46  LYS A CB  
718   C CG  . LYS A 46  ? 0.4150 0.2028 0.2962 -0.0520 0.0899  0.0201  46  LYS A CG  
719   C CD  . LYS A 46  ? 0.4818 0.1834 0.3315 -0.0909 0.0838  0.0178  46  LYS A CD  
720   C CE  . LYS A 46  ? 0.5059 0.2237 0.3701 -0.1514 0.0767  0.0172  46  LYS A CE  
721   N NZ  . LYS A 46  ? 0.5802 0.2686 0.4030 -0.1601 0.0709  0.0352  46  LYS A NZ  
735   N N   . ASP A 47  ? 0.4007 0.1869 0.2644 0.1116  0.0579  0.0363  47  ASP A N   
736   C CA  . ASP A 47  ? 0.4145 0.2097 0.2757 0.1121  0.0705  0.0146  47  ASP A CA  
737   C C   . ASP A 47  ? 0.4277 0.2087 0.3003 0.1211  0.0542  0.0099  47  ASP A C   
738   O O   . ASP A 47  ? 0.4851 0.2255 0.3136 0.0898  0.0338  0.0165  47  ASP A O   
739   C CB  . ASP A 47  ? 0.4522 0.2343 0.2786 0.1157  0.0472  0.0411  47  ASP A CB  
740   C CG  . ASP A 47  ? 0.4621 0.2444 0.2805 0.1448  0.0319  0.0569  47  ASP A CG  
741   O OD1 . ASP A 47  ? 0.4964 0.2915 0.2893 0.1364  0.0395  0.0915  47  ASP A OD1 
742   O OD2 . ASP A 47  ? 0.4202 0.2814 0.2787 0.1721  0.0113  0.0226  47  ASP A OD2 
747   N N   . GLY A 48  ? 0.4098 0.1785 0.2961 0.1032  0.0459  0.0082  48  GLY A N   
748   C CA  . GLY A 48  ? 0.4010 0.1936 0.2930 0.0945  0.0617  0.0221  48  GLY A CA  
749   C C   . GLY A 48  ? 0.3885 0.1850 0.2875 0.0727  0.0691  0.0174  48  GLY A C   
750   O O   . GLY A 48  ? 0.4099 0.2197 0.2943 0.0282  0.0449  0.0167  48  GLY A O   
754   N N   . ARG A 49  ? 0.3415 0.1640 0.2703 0.0617  0.0811  0.0123  49  ARG A N   
755   C CA  . ARG A 49  ? 0.3106 0.1670 0.2654 0.0748  0.0505  0.0053  49  ARG A CA  
756   C C   . ARG A 49  ? 0.3009 0.1409 0.2576 0.0699  0.0431  0.0031  49  ARG A C   
757   O O   . ARG A 49  ? 0.3209 0.1988 0.2520 0.0590  0.0460  0.0044  49  ARG A O   
758   C CB  . ARG A 49  ? 0.3050 0.2154 0.2695 0.0138  0.0497  0.0193  49  ARG A CB  
759   C CG  . ARG A 49  ? 0.3192 0.2651 0.2638 0.0317  0.0390  0.0470  49  ARG A CG  
760   C CD  . ARG A 49  ? 0.3451 0.2923 0.2700 0.0120  -0.0023 0.0645  49  ARG A CD  
761   N NE  . ARG A 49  ? 0.3627 0.3731 0.2781 -0.0275 0.0028  0.0627  49  ARG A NE  
762   C CZ  . ARG A 49  ? 0.3591 0.4300 0.2907 -0.0392 -0.0001 0.0756  49  ARG A CZ  
763   N NH1 . ARG A 49  ? 0.3867 0.4450 0.2882 0.0149  -0.0033 0.0609  49  ARG A NH1 
764   N NH2 . ARG A 49  ? 0.3883 0.4298 0.2982 -0.0419 0.0017  0.1019  49  ARG A NH2 
778   N N   . GLU A 50  ? 0.3371 0.2166 0.2593 0.0350  0.0298  0.0008  50  GLU A N   
779   C CA  . GLU A 50  ? 0.2992 0.2003 0.2622 0.0497  0.0167  -0.0145 50  GLU A CA  
780   C C   . GLU A 50  ? 0.2961 0.2155 0.2618 0.0523  0.0254  -0.0197 50  GLU A C   
781   O O   . GLU A 50  ? 0.3011 0.1892 0.2800 0.0800  0.0273  -0.0048 50  GLU A O   
782   C CB  . GLU A 50  ? 0.3355 0.1692 0.2788 0.0703  0.0105  -0.0329 50  GLU A CB  
783   C CG  . GLU A 50  ? 0.4192 0.1970 0.3113 -0.0178 0.0065  -0.0258 50  GLU A CG  
784   C CD  . GLU A 50  ? 0.4926 0.2611 0.3489 -0.0055 0.0195  -0.0591 50  GLU A CD  
785   O OE1 . GLU A 50  ? 0.4409 0.2882 0.3534 0.0571  0.0450  -0.0857 50  GLU A OE1 
786   O OE2 . GLU A 50  ? 0.5795 0.2867 0.3808 -0.0341 0.0162  -0.0341 50  GLU A OE2 
793   N N   . PHE A 51  ? 0.2720 0.1958 0.2283 0.0124  0.0252  -0.0213 51  PHE A N   
794   C CA  . PHE A 51  ? 0.2593 0.1532 0.2214 0.0117  0.0306  -0.0090 51  PHE A CA  
795   C C   . PHE A 51  ? 0.2042 0.1573 0.2272 -0.0040 0.0220  -0.0108 51  PHE A C   
796   O O   . PHE A 51  ? 0.2139 0.2125 0.2320 -0.0147 0.0152  0.0154  51  PHE A O   
797   C CB  . PHE A 51  ? 0.2482 0.1436 0.2110 0.0275  0.0141  0.0193  51  PHE A CB  
798   C CG  . PHE A 51  ? 0.2683 0.2050 0.2179 0.0197  -0.0043 0.0406  51  PHE A CG  
799   C CD1 . PHE A 51  ? 0.3189 0.1714 0.2236 0.0489  0.0035  0.0485  51  PHE A CD1 
800   C CD2 . PHE A 51  ? 0.3011 0.2023 0.2140 0.0236  -0.0456 0.0213  51  PHE A CD2 
801   C CE1 . PHE A 51  ? 0.3454 0.1586 0.2218 0.0176  -0.0020 0.0576  51  PHE A CE1 
802   C CE2 . PHE A 51  ? 0.3246 0.2303 0.2099 -0.0259 -0.0427 0.0405  51  PHE A CE2 
803   C CZ  . PHE A 51  ? 0.3324 0.1919 0.2241 -0.0243 -0.0445 0.0364  51  PHE A CZ  
813   N N   . ILE A 52  ? 0.2263 0.1555 0.2298 0.0364  0.0349  -0.0112 52  ILE A N   
814   C CA  . ILE A 52  ? 0.2378 0.1984 0.2180 0.0331  0.0258  0.0027  52  ILE A CA  
815   C C   . ILE A 52  ? 0.2156 0.1880 0.2158 -0.0009 0.0118  0.0001  52  ILE A C   
816   O O   . ILE A 52  ? 0.2166 0.1601 0.2228 0.0295  0.0272  -0.0186 52  ILE A O   
817   C CB  . ILE A 52  ? 0.2800 0.1903 0.2232 0.0641  0.0616  -0.0026 52  ILE A CB  
818   C CG1 . ILE A 52  ? 0.3035 0.1942 0.2323 0.0496  0.0848  -0.0245 52  ILE A CG1 
819   C CG2 . ILE A 52  ? 0.3146 0.1789 0.2346 0.0217  0.0587  0.0100  52  ILE A CG2 
820   C CD1 . ILE A 52  ? 0.3080 0.2353 0.2430 0.0760  0.0962  -0.0100 52  ILE A CD1 
832   N N   . ASP A 53  ? 0.1826 0.1911 0.2107 0.0145  -0.0086 0.0026  53  ASP A N   
833   C CA  . ASP A 53  ? 0.1958 0.1841 0.1963 0.0083  -0.0181 -0.0088 53  ASP A CA  
834   C C   . ASP A 53  ? 0.2147 0.1506 0.2055 0.0174  -0.0173 -0.0128 53  ASP A C   
835   O O   . ASP A 53  ? 0.2215 0.1482 0.1998 0.0015  -0.0091 -0.0145 53  ASP A O   
836   C CB  . ASP A 53  ? 0.1781 0.1808 0.1935 -0.0060 0.0040  -0.0073 53  ASP A CB  
837   C CG  . ASP A 53  ? 0.1490 0.1592 0.1972 -0.0385 -0.0074 -0.0173 53  ASP A CG  
838   O OD1 . ASP A 53  ? 0.1759 0.1936 0.1847 -0.0170 0.0002  -0.0047 53  ASP A OD1 
839   O OD2 . ASP A 53  ? 0.1521 0.1587 0.2116 -0.0034 -0.0037 0.0059  53  ASP A OD2 
844   N N   . GLY A 54  ? 0.1703 0.1664 0.2095 0.0113  -0.0073 0.0006  54  GLY A N   
845   C CA  . GLY A 54  ? 0.1776 0.1682 0.2087 0.0192  -0.0007 0.0230  54  GLY A CA  
846   C C   . GLY A 54  ? 0.1883 0.1678 0.2067 0.0131  0.0050  0.0029  54  GLY A C   
847   O O   . GLY A 54  ? 0.1910 0.1749 0.2074 -0.0054 0.0121  0.0067  54  GLY A O   
851   N N   . PHE A 55  ? 0.1729 0.1451 0.1964 0.0174  0.0120  0.0141  55  PHE A N   
852   C CA  . PHE A 55  ? 0.1424 0.1414 0.1803 0.0056  -0.0122 -0.0167 55  PHE A CA  
853   C C   . PHE A 55  ? 0.1401 0.1247 0.1905 0.0299  -0.0263 0.0031  55  PHE A C   
854   O O   . PHE A 55  ? 0.1626 0.1576 0.2011 -0.0061 0.0043  -0.0006 55  PHE A O   
855   C CB  . PHE A 55  ? 0.1589 0.1647 0.1864 -0.0396 -0.0208 0.0012  55  PHE A CB  
856   C CG  . PHE A 55  ? 0.1853 0.1264 0.2069 -0.0236 -0.0014 0.0209  55  PHE A CG  
857   C CD1 . PHE A 55  ? 0.1633 0.1231 0.2312 0.0263  -0.0003 0.0187  55  PHE A CD1 
858   C CD2 . PHE A 55  ? 0.2027 0.1526 0.2151 0.0197  0.0081  0.0022  55  PHE A CD2 
859   C CE1 . PHE A 55  ? 0.1888 0.1326 0.2426 0.0631  0.0208  -0.0047 55  PHE A CE1 
860   C CE2 . PHE A 55  ? 0.1792 0.1568 0.2282 -0.0037 0.0234  -0.0009 55  PHE A CE2 
861   C CZ  . PHE A 55  ? 0.1906 0.1088 0.2400 0.0313  0.0335  0.0112  55  PHE A CZ  
871   N N   . ALA A 56  ? 0.1994 0.1373 0.1940 0.0038  0.0047  -0.0002 56  ALA A N   
872   C CA  . ALA A 56  ? 0.1799 0.1800 0.1919 0.0178  0.0110  -0.0022 56  ALA A CA  
873   C C   . ALA A 56  ? 0.2116 0.1591 0.1667 0.0532  -0.0024 -0.0065 56  ALA A C   
874   O O   . ALA A 56  ? 0.2059 0.1379 0.1619 0.0549  -0.0037 0.0162  56  ALA A O   
875   C CB  . ALA A 56  ? 0.1530 0.2047 0.2123 0.0094  0.0148  -0.0264 56  ALA A CB  
881   N N   . GLY A 57  ? 0.1753 0.1737 0.1448 -0.0011 -0.0040 -0.0132 57  GLY A N   
882   C CA  . GLY A 57  ? 0.2131 0.1444 0.1577 0.0326  -0.0160 0.0012  57  GLY A CA  
883   C C   . GLY A 57  ? 0.1715 0.1326 0.1703 -0.0052 -0.0219 -0.0047 57  GLY A C   
884   O O   . GLY A 57  ? 0.1713 0.1266 0.1787 0.0052  -0.0176 -0.0269 57  GLY A O   
888   N N   . LEU A 58  ? 0.1686 0.1199 0.1733 0.0105  0.0012  -0.0016 58  LEU A N   
889   C CA  . LEU A 58  ? 0.1949 0.1028 0.1624 -0.0055 -0.0082 0.0071  58  LEU A CA  
890   C C   . LEU A 58  ? 0.1866 0.1645 0.1537 -0.0324 -0.0073 -0.0033 58  LEU A C   
891   O O   . LEU A 58  ? 0.1824 0.2329 0.1478 -0.0124 -0.0136 -0.0203 58  LEU A O   
892   C CB  . LEU A 58  ? 0.1688 0.1572 0.1638 -0.0015 -0.0197 0.0000  58  LEU A CB  
893   C CG  . LEU A 58  ? 0.1535 0.2087 0.1734 0.0040  -0.0071 -0.0209 58  LEU A CG  
894   C CD1 . LEU A 58  ? 0.2179 0.2224 0.1699 0.0768  -0.0028 -0.0294 58  LEU A CD1 
895   C CD2 . LEU A 58  ? 0.1703 0.2212 0.1780 -0.0150 -0.0123 -0.0532 58  LEU A CD2 
907   N N   . TYR A 59  ? 0.1928 0.1516 0.1606 -0.0084 -0.0091 0.0162  59  TYR A N   
908   C CA  . TYR A 59  ? 0.1908 0.1195 0.1872 -0.0131 -0.0040 -0.0049 59  TYR A CA  
909   C C   . TYR A 59  ? 0.1927 0.1309 0.1740 -0.0161 0.0054  -0.0017 59  TYR A C   
910   O O   . TYR A 59  ? 0.2238 0.1436 0.1750 0.0109  0.0033  0.0044  59  TYR A O   
911   C CB  . TYR A 59  ? 0.2402 0.1110 0.2256 0.0195  0.0181  0.0087  59  TYR A CB  
912   C CG  . TYR A 59  ? 0.1754 0.1527 0.2487 -0.0250 0.0139  0.0279  59  TYR A CG  
913   C CD1 . TYR A 59  ? 0.1965 0.1928 0.2584 -0.0539 -0.0158 0.0214  59  TYR A CD1 
914   C CD2 . TYR A 59  ? 0.1641 0.1621 0.2676 -0.0020 0.0234  -0.0024 59  TYR A CD2 
915   C CE1 . TYR A 59  ? 0.2022 0.2179 0.2722 -0.0311 -0.0484 -0.0129 59  TYR A CE1 
916   C CE2 . TYR A 59  ? 0.1923 0.1894 0.2815 -0.0062 -0.0049 0.0267  59  TYR A CE2 
917   C CZ  . TYR A 59  ? 0.2029 0.1450 0.3020 -0.0033 -0.0459 -0.0126 59  TYR A CZ  
918   O OH  . TYR A 59  ? 0.3074 0.1346 0.3508 -0.0168 -0.0869 0.0025  59  TYR A OH  
928   N N   . CYS A 60  ? 0.1546 0.1503 0.1723 0.0071  0.0031  0.0014  60  CYS A N   
929   C CA  . CYS A 60  ? 0.1358 0.1480 0.1785 0.0096  0.0149  -0.0023 60  CYS A CA  
930   C C   . CYS A 60  ? 0.1490 0.1342 0.1910 -0.0224 0.0074  -0.0010 60  CYS A C   
931   O O   . CYS A 60  ? 0.1559 0.1962 0.1969 0.0102  0.0083  -0.0263 60  CYS A O   
932   C CB  . CYS A 60  ? 0.2015 0.1742 0.1708 -0.0261 0.0416  0.0141  60  CYS A CB  
933   S SG  . CYS A 60  ? 0.1852 0.1772 0.1774 -0.0098 0.0037  -0.0112 60  CYS A SG  
939   N N   . VAL A 61  ? 0.1880 0.1208 0.1859 -0.0138 0.0176  -0.0142 61  VAL A N   
940   C CA  . VAL A 61  ? 0.1993 0.1253 0.1711 -0.0419 0.0117  -0.0001 61  VAL A CA  
941   C C   . VAL A 61  ? 0.1988 0.1753 0.1733 0.0008  0.0109  -0.0159 61  VAL A C   
942   O O   . VAL A 61  ? 0.2082 0.1609 0.1728 -0.0011 -0.0052 -0.0064 61  VAL A O   
943   C CB  . VAL A 61  ? 0.2255 0.1188 0.1823 -0.0044 0.0009  -0.0471 61  VAL A CB  
944   C CG1 . VAL A 61  ? 0.2892 0.1488 0.1953 0.0120  -0.0207 -0.0100 61  VAL A CG1 
945   C CG2 . VAL A 61  ? 0.2478 0.1421 0.1823 -0.0037 0.0097  -0.0330 61  VAL A CG2 
955   N N   . ASN A 62  ? 0.1983 0.1946 0.1572 -0.0083 0.0111  0.0119  62  ASN A N   
956   C CA  . ASN A 62  ? 0.1738 0.1577 0.1666 -0.0238 0.0245  0.0052  62  ASN A CA  
957   C C   . ASN A 62  ? 0.1828 0.1462 0.1852 -0.0122 0.0157  -0.0142 62  ASN A C   
958   O O   . ASN A 62  ? 0.1985 0.1463 0.1947 -0.0059 0.0131  0.0043  62  ASN A O   
959   C CB  . ASN A 62  ? 0.1841 0.1378 0.1821 -0.0242 0.0014  -0.0152 62  ASN A CB  
960   C CG  . ASN A 62  ? 0.1809 0.1520 0.1856 -0.0047 0.0053  -0.0313 62  ASN A CG  
961   O OD1 . ASN A 62  ? 0.1711 0.1721 0.1981 -0.0039 0.0067  -0.0455 62  ASN A OD1 
962   N ND2 . ASN A 62  ? 0.1961 0.1298 0.1872 -0.0064 -0.0072 -0.0155 62  ASN A ND2 
969   N N   . ILE A 63  ? 0.2104 0.1314 0.1920 -0.0106 0.0282  -0.0310 63  ILE A N   
970   C CA  . ILE A 63  ? 0.2094 0.1245 0.1882 0.0142  0.0280  -0.0325 63  ILE A CA  
971   C C   . ILE A 63  ? 0.2187 0.1715 0.2032 0.0100  0.0168  -0.0350 63  ILE A C   
972   O O   . ILE A 63  ? 0.2168 0.2098 0.2073 -0.0037 0.0047  -0.0526 63  ILE A O   
973   C CB  . ILE A 63  ? 0.2328 0.1518 0.1875 0.0010  0.0275  -0.0248 63  ILE A CB  
974   C CG1 . ILE A 63  ? 0.1828 0.2016 0.1842 -0.0150 0.0217  -0.0231 63  ILE A CG1 
975   C CG2 . ILE A 63  ? 0.2408 0.1567 0.1951 -0.0055 0.0270  -0.0192 63  ILE A CG2 
976   C CD1 . ILE A 63  ? 0.2034 0.1932 0.1781 -0.0358 -0.0141 -0.0092 63  ILE A CD1 
988   N N   . GLY A 64  ? 0.2218 0.1570 0.2062 -0.0120 0.0068  0.0085  64  GLY A N   
989   C CA  . GLY A 64  ? 0.2417 0.1503 0.2090 -0.0374 0.0185  -0.0115 64  GLY A CA  
990   C C   . GLY A 64  ? 0.2045 0.1326 0.2061 0.0023  0.0260  -0.0361 64  GLY A C   
991   O O   . GLY A 64  ? 0.1760 0.1463 0.2162 -0.0054 0.0004  -0.0267 64  GLY A O   
995   N N   . TYR A 65  ? 0.2378 0.1164 0.2075 0.0214  0.0283  -0.0245 65  TYR A N   
996   C CA  . TYR A 65  ? 0.2112 0.1394 0.2057 0.0224  0.0167  -0.0113 65  TYR A CA  
997   C C   . TYR A 65  ? 0.2378 0.1654 0.2204 -0.0069 0.0185  -0.0100 65  TYR A C   
998   O O   . TYR A 65  ? 0.2447 0.1757 0.2246 -0.0197 0.0329  -0.0250 65  TYR A O   
999   C CB  . TYR A 65  ? 0.2343 0.1538 0.1971 0.0413  0.0294  0.0199  65  TYR A CB  
1000  C CG  . TYR A 65  ? 0.2120 0.1385 0.1977 -0.0363 0.0429  0.0150  65  TYR A CG  
1001  C CD1 . TYR A 65  ? 0.2285 0.2072 0.1922 -0.0246 0.0495  -0.0059 65  TYR A CD1 
1002  C CD2 . TYR A 65  ? 0.1870 0.1414 0.1974 -0.0117 0.0032  -0.0153 65  TYR A CD2 
1003  C CE1 . TYR A 65  ? 0.2100 0.2082 0.1971 0.0098  0.0304  -0.0235 65  TYR A CE1 
1004  C CE2 . TYR A 65  ? 0.1920 0.1564 0.1968 -0.0459 0.0155  -0.0279 65  TYR A CE2 
1005  C CZ  . TYR A 65  ? 0.1468 0.1485 0.1921 -0.0279 0.0199  -0.0336 65  TYR A CZ  
1006  O OH  . TYR A 65  ? 0.1972 0.1656 0.1978 -0.0293 0.0142  -0.0197 65  TYR A OH  
1016  N N   . GLY A 66  ? 0.2685 0.1185 0.2319 0.0356  -0.0100 0.0050  66  GLY A N   
1017  C CA  . GLY A 66  ? 0.2942 0.1035 0.2552 0.0083  -0.0152 -0.0036 66  GLY A CA  
1018  C C   . GLY A 66  ? 0.2799 0.1411 0.2615 0.0143  0.0072  0.0062  66  GLY A C   
1019  O O   . GLY A 66  ? 0.3179 0.1551 0.2704 0.0417  0.0072  -0.0001 66  GLY A O   
1023  N N   . ARG A 67  ? 0.2407 0.1680 0.2567 -0.0192 0.0047  0.0030  67  ARG A N   
1024  C CA  . ARG A 67  ? 0.2723 0.1698 0.2586 -0.0270 0.0164  -0.0215 67  ARG A CA  
1025  C C   . ARG A 67  ? 0.2504 0.1637 0.2797 -0.0248 0.0175  -0.0405 67  ARG A C   
1026  O O   . ARG A 67  ? 0.2092 0.1662 0.2740 -0.0352 0.0372  -0.0508 67  ARG A O   
1027  C CB  . ARG A 67  ? 0.2806 0.1754 0.2466 -0.0228 -0.0041 -0.0120 67  ARG A CB  
1028  C CG  . ARG A 67  ? 0.2935 0.1793 0.2240 -0.0026 0.0312  -0.0068 67  ARG A CG  
1029  C CD  . ARG A 67  ? 0.3079 0.2046 0.2384 -0.0254 0.0113  -0.0283 67  ARG A CD  
1030  N NE  . ARG A 67  ? 0.2783 0.2051 0.2378 -0.0205 0.0231  -0.0477 67  ARG A NE  
1031  C CZ  . ARG A 67  ? 0.2621 0.1875 0.2484 -0.0212 0.0236  -0.0570 67  ARG A CZ  
1032  N NH1 . ARG A 67  ? 0.2838 0.1692 0.2612 -0.0217 0.0093  -0.0488 67  ARG A NH1 
1033  N NH2 . ARG A 67  ? 0.2638 0.1550 0.2533 -0.0415 0.0193  -0.0244 67  ARG A NH2 
1047  N N   A THR A 68  ? 0.2425 0.1667 0.2888 -0.0171 0.0319  -0.0394 68  THR A N   
1048  N N   B THR A 68  ? 0.2578 0.1539 0.2944 -0.0377 0.0274  -0.0240 68  THR A N   
1049  C CA  A THR A 68  ? 0.2311 0.1788 0.2881 -0.0053 0.0408  -0.0442 68  THR A CA  
1050  C CA  B THR A 68  ? 0.2611 0.1619 0.2955 -0.0295 0.0256  -0.0105 68  THR A CA  
1051  C C   A THR A 68  ? 0.2438 0.1841 0.2842 -0.0101 0.0336  -0.0430 68  THR A C   
1052  C C   B THR A 68  ? 0.2558 0.1693 0.2889 -0.0192 0.0313  -0.0143 68  THR A C   
1053  O O   A THR A 68  ? 0.2432 0.1893 0.2870 -0.0064 0.0189  -0.0548 68  THR A O   
1054  O O   B THR A 68  ? 0.2388 0.1537 0.2941 -0.0041 0.0268  0.0029  68  THR A O   
1055  C CB  A THR A 68  ? 0.2212 0.1865 0.2963 0.0336  0.0399  -0.0405 68  THR A CB  
1056  C CB  B THR A 68  ? 0.2987 0.1713 0.3108 -0.0029 0.0070  0.0139  68  THR A CB  
1057  O OG1 A THR A 68  ? 0.2748 0.1789 0.3029 0.0610  0.0435  -0.0446 68  THR A OG1 
1058  O OG1 B THR A 68  ? 0.3625 0.1877 0.3167 -0.0203 -0.0115 0.0400  68  THR A OG1 
1059  C CG2 A THR A 68  ? 0.2291 0.1939 0.2955 0.0453  0.0521  -0.0299 68  THR A CG2 
1060  C CG2 B THR A 68  ? 0.3327 0.1398 0.3201 0.0150  0.0173  0.0343  68  THR A CG2 
1075  N N   . GLU A 69  ? 0.2552 0.1629 0.2817 -0.0227 0.0306  -0.0399 69  GLU A N   
1076  C CA  . GLU A 69  ? 0.2903 0.1643 0.2699 -0.0225 0.0051  -0.0528 69  GLU A CA  
1077  C C   . GLU A 69  ? 0.2280 0.1639 0.2497 -0.0447 0.0235  -0.0384 69  GLU A C   
1078  O O   . GLU A 69  ? 0.2508 0.1732 0.2408 -0.0464 0.0328  -0.0332 69  GLU A O   
1079  C CB  . GLU A 69  ? 0.3410 0.1871 0.2732 -0.0006 0.0079  -0.0387 69  GLU A CB  
1080  C CG  . GLU A 69  ? 0.4052 0.2335 0.2665 -0.0126 -0.0091 -0.0320 69  GLU A CG  
1081  C CD  . GLU A 69  ? 0.4378 0.2731 0.2640 -0.0014 -0.0220 -0.0399 69  GLU A CD  
1082  O OE1 . GLU A 69  ? 0.4486 0.3141 0.2569 -0.0075 0.0064  -0.0430 69  GLU A OE1 
1083  O OE2 . GLU A 69  ? 0.4764 0.3035 0.2825 -0.0334 -0.0384 -0.0395 69  GLU A OE2 
1091  N N   . VAL A 70  ? 0.2465 0.1407 0.2344 -0.0795 0.0352  -0.0420 70  VAL A N   
1092  C CA  . VAL A 70  ? 0.2436 0.1146 0.2203 -0.0543 0.0179  -0.0453 70  VAL A CA  
1093  C C   . VAL A 70  ? 0.2507 0.1458 0.2235 -0.0194 -0.0007 -0.0326 70  VAL A C   
1094  O O   . VAL A 70  ? 0.2386 0.2013 0.2303 -0.0263 0.0070  -0.0420 70  VAL A O   
1095  C CB  . VAL A 70  ? 0.1979 0.1454 0.2220 -0.0205 0.0219  -0.0349 70  VAL A CB  
1096  C CG1 . VAL A 70  ? 0.1929 0.1889 0.2300 -0.0280 0.0286  -0.0327 70  VAL A CG1 
1097  C CG2 . VAL A 70  ? 0.2179 0.1590 0.2410 -0.0210 0.0076  -0.0607 70  VAL A CG2 
1107  N N   . ALA A 71  ? 0.2473 0.1535 0.2200 -0.0367 0.0115  -0.0229 71  ALA A N   
1108  C CA  . ALA A 71  ? 0.2381 0.2201 0.2046 -0.0254 0.0167  -0.0287 71  ALA A CA  
1109  C C   . ALA A 71  ? 0.2067 0.2278 0.2136 -0.0275 0.0338  -0.0376 71  ALA A C   
1110  O O   . ALA A 71  ? 0.2131 0.2502 0.2190 0.0076  0.0447  -0.0244 71  ALA A O   
1111  C CB  . ALA A 71  ? 0.2932 0.2386 0.1905 -0.0508 0.0165  0.0041  71  ALA A CB  
1117  N N   . GLU A 72  ? 0.2492 0.2036 0.2302 -0.0363 0.0237  -0.0237 72  GLU A N   
1118  C CA  . GLU A 72  ? 0.2827 0.2142 0.2494 -0.0391 -0.0079 -0.0263 72  GLU A CA  
1119  C C   . GLU A 72  ? 0.2621 0.2097 0.2261 -0.0420 -0.0053 -0.0382 72  GLU A C   
1120  O O   . GLU A 72  ? 0.2584 0.2266 0.2107 -0.0433 0.0272  -0.0165 72  GLU A O   
1121  C CB  . GLU A 72  ? 0.3582 0.2132 0.2950 -0.0812 -0.0189 -0.0279 72  GLU A CB  
1122  C CG  . GLU A 72  ? 0.4684 0.2980 0.3461 -0.0604 -0.0230 -0.0472 72  GLU A CG  
1123  C CD  . GLU A 72  ? 0.6215 0.3888 0.4052 -0.0244 -0.0350 -0.0244 72  GLU A CD  
1124  O OE1 . GLU A 72  ? 0.6711 0.3966 0.4155 -0.0296 -0.0567 -0.0636 72  GLU A OE1 
1125  O OE2 . GLU A 72  ? 0.6780 0.4313 0.4433 -0.0199 -0.0321 -0.0023 72  GLU A OE2 
1132  N N   . ALA A 73  ? 0.2452 0.1790 0.2101 -0.0077 0.0117  -0.0265 73  ALA A N   
1133  C CA  . ALA A 73  ? 0.2526 0.1496 0.2170 -0.0481 -0.0006 -0.0282 73  ALA A CA  
1134  C C   . ALA A 73  ? 0.2474 0.1707 0.2215 -0.0625 0.0049  -0.0165 73  ALA A C   
1135  O O   . ALA A 73  ? 0.2726 0.2331 0.2270 -0.0376 0.0329  -0.0152 73  ALA A O   
1136  C CB  . ALA A 73  ? 0.2200 0.1925 0.2105 -0.0727 -0.0063 -0.0350 73  ALA A CB  
1142  N N   . ILE A 74  ? 0.2275 0.1490 0.2205 -0.0726 -0.0050 -0.0180 74  ILE A N   
1143  C CA  . ILE A 74  ? 0.2292 0.1686 0.2195 -0.0367 0.0106  -0.0058 74  ILE A CA  
1144  C C   . ILE A 74  ? 0.2157 0.1675 0.2312 -0.0233 0.0069  0.0050  74  ILE A C   
1145  O O   . ILE A 74  ? 0.2287 0.1572 0.2432 -0.0329 -0.0041 0.0057  74  ILE A O   
1146  C CB  . ILE A 74  ? 0.2299 0.1500 0.2170 -0.0323 -0.0074 -0.0270 74  ILE A CB  
1147  C CG1 . ILE A 74  ? 0.2121 0.1419 0.2272 -0.0547 -0.0265 -0.0186 74  ILE A CG1 
1148  C CG2 . ILE A 74  ? 0.2426 0.1524 0.2101 -0.0290 -0.0212 -0.0290 74  ILE A CG2 
1149  C CD1 . ILE A 74  ? 0.2503 0.1145 0.2448 -0.0299 -0.0155 -0.0342 74  ILE A CD1 
1161  N N   . HIS A 75  ? 0.2070 0.2101 0.2369 0.0157  0.0285  0.0140  75  HIS A N   
1162  C CA  . HIS A 75  ? 0.2511 0.1945 0.2486 0.0103  0.0272  0.0048  75  HIS A CA  
1163  C C   . HIS A 75  ? 0.2528 0.1457 0.2331 -0.0231 0.0296  -0.0080 75  HIS A C   
1164  O O   . HIS A 75  ? 0.2615 0.1545 0.2477 -0.0048 0.0364  -0.0110 75  HIS A O   
1165  C CB  . HIS A 75  ? 0.2868 0.1660 0.2605 0.0312  0.0123  0.0316  75  HIS A CB  
1166  C CG  . HIS A 75  ? 0.3377 0.1923 0.2686 0.0047  -0.0014 0.0273  75  HIS A CG  
1167  N ND1 . HIS A 75  ? 0.3911 0.2792 0.2753 -0.0256 -0.0051 0.0471  75  HIS A ND1 
1168  C CD2 . HIS A 75  ? 0.4452 0.2604 0.2869 -0.0297 -0.0049 0.0324  75  HIS A CD2 
1169  C CE1 . HIS A 75  ? 0.4310 0.2720 0.2841 -0.0442 -0.0123 0.0522  75  HIS A CE1 
1170  N NE2 . HIS A 75  ? 0.4865 0.2013 0.2871 -0.0026 -0.0187 0.0469  75  HIS A NE2 
1178  N N   . ARG A 76  ? 0.2708 0.1416 0.2081 -0.0452 0.0396  -0.0104 76  ARG A N   
1179  C CA  . ARG A 76  ? 0.3212 0.1833 0.2271 -0.0998 0.0287  -0.0048 76  ARG A CA  
1180  C C   . ARG A 76  ? 0.3108 0.2005 0.2192 -0.0489 0.0054  -0.0026 76  ARG A C   
1181  O O   . ARG A 76  ? 0.3096 0.1781 0.2356 -0.0482 0.0041  -0.0056 76  ARG A O   
1182  C CB  . ARG A 76  ? 0.4327 0.3020 0.2460 -0.0761 0.0593  -0.0212 76  ARG A CB  
1183  C CG  . ARG A 76  ? 0.5205 0.4100 0.2667 -0.1234 0.0315  -0.0143 76  ARG A CG  
1184  C CD  . ARG A 76  ? 0.5526 0.5031 0.2720 -0.2223 0.0196  -0.0143 76  ARG A CD  
1185  N NE  . ARG A 76  ? 0.6948 0.6348 0.2898 -0.1496 -0.0202 -0.0093 76  ARG A NE  
1186  C CZ  . ARG A 76  ? 0.7429 0.7123 0.2966 -0.1517 -0.0194 0.0040  76  ARG A CZ  
1187  N NH1 . ARG A 76  ? 0.7404 0.7572 0.3010 -0.1020 -0.0177 0.0096  76  ARG A NH1 
1188  N NH2 . ARG A 76  ? 0.7766 0.7223 0.3030 -0.1985 -0.0424 0.0043  76  ARG A NH2 
1202  N N   . GLN A 77  ? 0.2466 0.2086 0.2015 -0.0559 0.0036  0.0033  77  GLN A N   
1203  C CA  . GLN A 77  ? 0.2263 0.1096 0.1978 -0.0397 0.0153  -0.0092 77  GLN A CA  
1204  C C   . GLN A 77  ? 0.2707 0.1921 0.2186 -0.0102 0.0317  -0.0112 77  GLN A C   
1205  O O   . GLN A 77  ? 0.2557 0.1881 0.2286 -0.0179 0.0260  0.0158  77  GLN A O   
1206  C CB  . GLN A 77  ? 0.2237 0.1332 0.2034 -0.0157 -0.0019 -0.0063 77  GLN A CB  
1207  C CG  . GLN A 77  ? 0.2251 0.1717 0.2032 -0.0296 0.0048  0.0033  77  GLN A CG  
1208  C CD  . GLN A 77  ? 0.2545 0.1686 0.2126 -0.0419 0.0121  -0.0178 77  GLN A CD  
1209  O OE1 . GLN A 77  ? 0.2658 0.2122 0.2196 -0.0379 -0.0282 -0.0349 77  GLN A OE1 
1210  N NE2 . GLN A 77  ? 0.2304 0.1550 0.2165 -0.0219 0.0210  0.0089  77  GLN A NE2 
1219  N N   . ALA A 78  ? 0.2442 0.1585 0.2331 -0.0042 0.0517  -0.0179 78  ALA A N   
1220  C CA  . ALA A 78  ? 0.2186 0.1696 0.2320 -0.0162 0.0557  -0.0086 78  ALA A CA  
1221  C C   . ALA A 78  ? 0.2865 0.1616 0.2450 -0.0188 0.0887  -0.0011 78  ALA A C   
1222  O O   . ALA A 78  ? 0.3232 0.2390 0.2572 -0.0386 0.1043  0.0113  78  ALA A O   
1223  C CB  . ALA A 78  ? 0.2591 0.1671 0.2218 0.0282  0.0297  0.0109  78  ALA A CB  
1229  N N   . LEU A 79  ? 0.2780 0.1545 0.2643 -0.0258 0.0780  -0.0174 79  LEU A N   
1230  C CA  . LEU A 79  ? 0.2828 0.1634 0.3023 -0.0498 0.0789  -0.0013 79  LEU A CA  
1231  C C   . LEU A 79  ? 0.2836 0.1820 0.3338 -0.0743 0.0823  0.0170  79  LEU A C   
1232  O O   . LEU A 79  ? 0.3403 0.1987 0.3700 -0.0853 0.0684  0.0483  79  LEU A O   
1233  C CB  . LEU A 79  ? 0.3088 0.1617 0.3198 -0.0771 0.0547  -0.0181 79  LEU A CB  
1234  C CG  . LEU A 79  ? 0.4151 0.2572 0.3379 -0.0274 0.0478  -0.0147 79  LEU A CG  
1235  C CD1 . LEU A 79  ? 0.4546 0.2965 0.3510 -0.0356 0.0238  0.0100  79  LEU A CD1 
1236  C CD2 . LEU A 79  ? 0.4504 0.2574 0.3415 -0.0545 0.0725  -0.0319 79  LEU A CD2 
1248  N N   . GLU A 80  ? 0.2800 0.1870 0.3323 -0.0924 0.0416  -0.0383 80  GLU A N   
1249  C CA  . GLU A 80  ? 0.2875 0.2286 0.3412 -0.0671 0.0451  -0.0683 80  GLU A CA  
1250  C C   . GLU A 80  ? 0.2558 0.1992 0.3014 -0.0291 0.0309  -0.0515 80  GLU A C   
1251  O O   . GLU A 80  ? 0.2608 0.2164 0.2990 -0.0563 0.0122  -0.0307 80  GLU A O   
1252  C CB  . GLU A 80  ? 0.3027 0.2675 0.3879 -0.0903 0.0579  -0.1218 80  GLU A CB  
1253  C CG  . GLU A 80  ? 0.3694 0.3094 0.4425 -0.0831 0.0885  -0.1503 80  GLU A CG  
1254  C CD  . GLU A 80  ? 0.4284 0.4172 0.4925 -0.0762 0.0908  -0.1705 80  GLU A CD  
1255  O OE1 . GLU A 80  ? 0.4517 0.4528 0.5146 -0.0990 0.0794  -0.1559 80  GLU A OE1 
1256  O OE2 . GLU A 80  ? 0.5110 0.4716 0.5207 -0.0886 0.0709  -0.1631 80  GLU A OE2 
1263  N N   . LEU A 81  ? 0.2526 0.1839 0.2645 -0.0771 0.0328  -0.0308 81  LEU A N   
1264  C CA  . LEU A 81  ? 0.2269 0.1668 0.2299 -0.0404 0.0402  -0.0230 81  LEU A CA  
1265  C C   . LEU A 81  ? 0.2469 0.1796 0.2096 -0.0535 0.0103  -0.0088 81  LEU A C   
1266  O O   . LEU A 81  ? 0.2620 0.1806 0.2020 -0.0601 0.0243  -0.0226 81  LEU A O   
1267  C CB  . LEU A 81  ? 0.2784 0.1898 0.2324 -0.0492 0.0027  -0.0353 81  LEU A CB  
1268  C CG  . LEU A 81  ? 0.3014 0.2153 0.2281 -0.0249 -0.0352 -0.0470 81  LEU A CG  
1269  C CD1 . LEU A 81  ? 0.2414 0.2698 0.2299 -0.0342 -0.0220 -0.0483 81  LEU A CD1 
1270  C CD2 . LEU A 81  ? 0.3731 0.2267 0.2450 -0.0268 -0.0564 -0.0657 81  LEU A CD2 
1282  N N   . ALA A 82  ? 0.2473 0.1795 0.2183 -0.0424 0.0103  0.0014  82  ALA A N   
1283  C CA  . ALA A 82  ? 0.2105 0.1689 0.2097 -0.0091 -0.0070 0.0039  82  ALA A CA  
1284  C C   . ALA A 82  ? 0.2141 0.1691 0.2004 -0.0678 0.0042  0.0135  82  ALA A C   
1285  O O   . ALA A 82  ? 0.2069 0.1660 0.2058 -0.0218 0.0226  -0.0066 82  ALA A O   
1286  C CB  . ALA A 82  ? 0.2251 0.1896 0.2297 0.0275  -0.0282 0.0134  82  ALA A CB  
1292  N N   . TYR A 83  ? 0.2050 0.1837 0.2009 -0.0482 0.0012  -0.0122 83  TYR A N   
1293  C CA  . TYR A 83  ? 0.1708 0.1549 0.1817 -0.0673 0.0116  -0.0392 83  TYR A CA  
1294  C C   . TYR A 83  ? 0.1606 0.1618 0.1699 -0.0705 -0.0075 -0.0146 83  TYR A C   
1295  O O   . TYR A 83  ? 0.2066 0.1903 0.1619 -0.0760 -0.0015 0.0176  83  TYR A O   
1296  C CB  . TYR A 83  ? 0.1758 0.1862 0.1797 -0.0712 0.0137  -0.0060 83  TYR A CB  
1297  C CG  . TYR A 83  ? 0.1800 0.1602 0.1681 -0.0373 0.0008  -0.0048 83  TYR A CG  
1298  C CD1 . TYR A 83  ? 0.1719 0.1544 0.1605 -0.0625 0.0023  -0.0150 83  TYR A CD1 
1299  C CD2 . TYR A 83  ? 0.1953 0.1583 0.1605 -0.0056 -0.0152 0.0097  83  TYR A CD2 
1300  C CE1 . TYR A 83  ? 0.1890 0.1295 0.1582 -0.0581 0.0088  -0.0412 83  TYR A CE1 
1301  C CE2 . TYR A 83  ? 0.1688 0.1512 0.1464 -0.0446 -0.0049 0.0167  83  TYR A CE2 
1302  C CZ  . TYR A 83  ? 0.1807 0.1524 0.1595 -0.0672 0.0007  -0.0101 83  TYR A CZ  
1303  O OH  . TYR A 83  ? 0.1713 0.2410 0.1730 -0.0294 0.0100  -0.0184 83  TYR A OH  
1313  N N   . TYR A 84  ? 0.1779 0.1647 0.1676 0.0127  -0.0001 -0.0179 84  TYR A N   
1314  C CA  . TYR A 84  ? 0.1497 0.1496 0.1598 -0.0430 -0.0018 -0.0086 84  TYR A CA  
1315  C C   . TYR A 84  ? 0.1808 0.1765 0.1748 -0.0463 0.0038  -0.0115 84  TYR A C   
1316  O O   . TYR A 84  ? 0.1951 0.1740 0.1739 -0.0193 0.0189  0.0202  84  TYR A O   
1317  C CB  . TYR A 84  ? 0.1743 0.1916 0.1686 -0.0479 -0.0051 -0.0020 84  TYR A CB  
1318  C CG  . TYR A 84  ? 0.2040 0.1923 0.1813 -0.0632 0.0124  0.0000  84  TYR A CG  
1319  C CD1 . TYR A 84  ? 0.1985 0.1827 0.1891 -0.0312 0.0129  -0.0015 84  TYR A CD1 
1320  C CD2 . TYR A 84  ? 0.1809 0.2045 0.1869 -0.0688 -0.0028 -0.0073 84  TYR A CD2 
1321  C CE1 . TYR A 84  ? 0.1940 0.1865 0.1830 -0.0101 0.0006  0.0006  84  TYR A CE1 
1322  C CE2 . TYR A 84  ? 0.1857 0.1951 0.1982 -0.0410 -0.0122 0.0061  84  TYR A CE2 
1323  C CZ  . TYR A 84  ? 0.1793 0.1788 0.1935 -0.0221 0.0091  -0.0072 84  TYR A CZ  
1324  O OH  . TYR A 84  ? 0.2004 0.1975 0.2071 -0.0392 0.0143  0.0088  84  TYR A OH  
1334  N N   . HIS A 85  ? 0.1876 0.1776 0.1667 -0.0373 -0.0053 -0.0083 85  HIS A N   
1335  C CA  . HIS A 85  ? 0.1980 0.1465 0.1770 -0.0557 0.0067  -0.0009 85  HIS A CA  
1336  C C   . HIS A 85  ? 0.1774 0.1406 0.1783 -0.0371 0.0021  -0.0142 85  HIS A C   
1337  O O   . HIS A 85  ? 0.1839 0.1797 0.1847 -0.0538 0.0006  0.0018  85  HIS A O   
1338  C CB  . HIS A 85  ? 0.2050 0.1721 0.1862 -0.0223 0.0120  -0.0031 85  HIS A CB  
1339  C CG  . HIS A 85  ? 0.1781 0.2056 0.1943 -0.0225 0.0139  0.0107  85  HIS A CG  
1340  N ND1 . HIS A 85  ? 0.1614 0.2111 0.2120 -0.0774 -0.0014 0.0084  85  HIS A ND1 
1341  C CD2 . HIS A 85  ? 0.1702 0.2137 0.2019 -0.0344 0.0211  0.0079  85  HIS A CD2 
1342  C CE1 . HIS A 85  ? 0.1631 0.1838 0.2085 -0.0577 -0.0231 0.0114  85  HIS A CE1 
1343  N NE2 . HIS A 85  ? 0.2133 0.2215 0.2114 -0.0373 -0.0001 -0.0185 85  HIS A NE2 
1351  N N   . THR A 86  ? 0.1534 0.1384 0.1642 -0.0583 -0.0081 0.0149  86  THR A N   
1352  C CA  . THR A 86  ? 0.1550 0.1463 0.1688 -0.0344 -0.0212 0.0102  86  THR A CA  
1353  C C   . THR A 86  ? 0.1477 0.1853 0.1686 -0.0242 -0.0073 -0.0097 86  THR A C   
1354  O O   . THR A 86  ? 0.1702 0.2126 0.1605 -0.0456 0.0037  -0.0255 86  THR A O   
1355  C CB  . THR A 86  ? 0.1685 0.1779 0.1838 -0.0284 -0.0083 -0.0084 86  THR A CB  
1356  O OG1 . THR A 86  ? 0.1733 0.2139 0.1742 -0.0192 -0.0097 0.0111  86  THR A OG1 
1357  C CG2 . THR A 86  ? 0.1802 0.1928 0.1844 -0.0345 -0.0188 -0.0216 86  THR A CG2 
1365  N N   . TYR A 87  ? 0.1344 0.1769 0.1768 -0.0349 0.0034  0.0132  87  TYR A N   
1366  C CA  . TYR A 87  ? 0.1759 0.1635 0.1872 -0.0212 -0.0049 -0.0026 87  TYR A CA  
1367  C C   . TYR A 87  ? 0.1653 0.1949 0.2054 -0.0219 0.0064  -0.0204 87  TYR A C   
1368  O O   . TYR A 87  ? 0.1462 0.1710 0.2023 -0.0581 -0.0011 -0.0063 87  TYR A O   
1369  C CB  . TYR A 87  ? 0.1609 0.1362 0.1761 -0.0136 -0.0159 -0.0101 87  TYR A CB  
1370  C CG  . TYR A 87  ? 0.1462 0.1594 0.1721 -0.0217 -0.0051 -0.0100 87  TYR A CG  
1371  C CD1 . TYR A 87  ? 0.1483 0.1814 0.1763 -0.0250 -0.0091 0.0088  87  TYR A CD1 
1372  C CD2 . TYR A 87  ? 0.1803 0.2230 0.1713 -0.0128 -0.0211 -0.0259 87  TYR A CD2 
1373  C CE1 . TYR A 87  ? 0.1658 0.1803 0.1740 -0.0450 -0.0193 -0.0122 87  TYR A CE1 
1374  C CE2 . TYR A 87  ? 0.2102 0.2202 0.1786 -0.0453 -0.0416 -0.0281 87  TYR A CE2 
1375  C CZ  . TYR A 87  ? 0.1519 0.1922 0.1799 -0.0520 -0.0371 0.0035  87  TYR A CZ  
1376  O OH  . TYR A 87  ? 0.1750 0.2442 0.1918 -0.0557 -0.0121 0.0176  87  TYR A OH  
1386  N N   . VAL A 88  ? 0.1505 0.2081 0.2112 -0.0820 0.0102  -0.0034 88  VAL A N   
1387  C CA  . VAL A 88  ? 0.1213 0.2339 0.2216 -0.0683 -0.0017 -0.0109 88  VAL A CA  
1388  C C   . VAL A 88  ? 0.1428 0.1823 0.2223 -0.0678 0.0019  -0.0220 88  VAL A C   
1389  O O   . VAL A 88  ? 0.1528 0.2441 0.2304 -0.0622 -0.0026 -0.0157 88  VAL A O   
1390  C CB  . VAL A 88  ? 0.1283 0.2726 0.2259 -0.0518 -0.0133 0.0060  88  VAL A CB  
1391  C CG1 . VAL A 88  ? 0.1435 0.2328 0.2336 -0.0380 0.0050  0.0202  88  VAL A CG1 
1392  C CG2 . VAL A 88  ? 0.1765 0.3405 0.2376 -0.0003 0.0202  0.0089  88  VAL A CG2 
1402  N N   . GLY A 89  ? 0.1652 0.2235 0.2091 -0.0356 0.0205  -0.0143 89  GLY A N   
1403  C CA  . GLY A 89  ? 0.1894 0.2386 0.2017 -0.0710 -0.0029 -0.0252 89  GLY A CA  
1404  C C   . GLY A 89  ? 0.1783 0.2352 0.1986 -0.0445 -0.0124 -0.0056 89  GLY A C   
1405  O O   . GLY A 89  ? 0.1658 0.2618 0.1986 -0.0555 0.0080  0.0217  89  GLY A O   
1409  N N   . HIS A 90  ? 0.1587 0.2167 0.1888 -0.0148 -0.0124 0.0235  90  HIS A N   
1410  C CA  . HIS A 90  ? 0.1407 0.1749 0.1812 -0.0116 -0.0250 0.0029  90  HIS A CA  
1411  C C   . HIS A 90  ? 0.1677 0.1869 0.1884 -0.0658 -0.0205 -0.0273 90  HIS A C   
1412  O O   . HIS A 90  ? 0.1521 0.1969 0.2018 -0.0559 0.0008  -0.0283 90  HIS A O   
1413  C CB  . HIS A 90  ? 0.1691 0.2260 0.1929 -0.0690 -0.0092 0.0047  90  HIS A CB  
1414  C CG  . HIS A 90  ? 0.1764 0.2166 0.1946 -0.0705 0.0052  -0.0070 90  HIS A CG  
1415  N ND1 . HIS A 90  ? 0.1867 0.2719 0.1964 -0.0705 0.0167  0.0170  90  HIS A ND1 
1416  C CD2 . HIS A 90  ? 0.2189 0.2209 0.2017 -0.1003 0.0339  -0.0034 90  HIS A CD2 
1417  C CE1 . HIS A 90  ? 0.1800 0.2868 0.2185 -0.0511 0.0123  0.0256  90  HIS A CE1 
1418  N NE2 . HIS A 90  ? 0.2119 0.2534 0.2236 -0.1106 0.0094  0.0319  90  HIS A NE2 
1426  N N   . SER A 91  ? 0.1659 0.1599 0.1915 -0.0612 -0.0085 -0.0268 91  SER A N   
1427  C CA  . SER A 91  ? 0.1474 0.2007 0.1875 -0.0452 -0.0133 -0.0081 91  SER A CA  
1428  C C   . SER A 91  ? 0.1451 0.1714 0.1897 -0.0637 0.0020  -0.0352 91  SER A C   
1429  O O   . SER A 91  ? 0.1736 0.2150 0.1968 -0.0602 0.0063  -0.0072 91  SER A O   
1430  C CB  . SER A 91  ? 0.1462 0.2339 0.1973 -0.0752 -0.0123 -0.0010 91  SER A CB  
1431  O OG  . SER A 91  ? 0.1784 0.2505 0.2007 -0.0761 0.0036  -0.0104 91  SER A OG  
1437  N N   . ASN A 92  ? 0.1746 0.2044 0.1984 -0.0452 -0.0128 -0.0228 92  ASN A N   
1438  C CA  . ASN A 92  ? 0.2036 0.1934 0.1993 -0.0433 -0.0078 -0.0241 92  ASN A CA  
1439  C C   . ASN A 92  ? 0.1726 0.1635 0.1904 -0.0634 -0.0028 -0.0122 92  ASN A C   
1440  O O   . ASN A 92  ? 0.1679 0.2363 0.1809 -0.0487 -0.0056 0.0001  92  ASN A O   
1441  C CB  . ASN A 92  ? 0.2122 0.1669 0.1933 -0.0397 -0.0088 -0.0152 92  ASN A CB  
1442  C CG  . ASN A 92  ? 0.2147 0.1846 0.1894 -0.0475 -0.0078 -0.0222 92  ASN A CG  
1443  O OD1 . ASN A 92  ? 0.2102 0.2085 0.1936 -0.0663 -0.0041 0.0066  92  ASN A OD1 
1444  N ND2 . ASN A 92  ? 0.2238 0.1884 0.2058 -0.0679 -0.0057 -0.0446 92  ASN A ND2 
1451  N N   . GLU A 93  ? 0.2036 0.1469 0.2020 -0.0951 -0.0250 -0.0193 93  GLU A N   
1452  C CA  . GLU A 93  ? 0.2231 0.2087 0.2033 -0.0511 -0.0541 -0.0448 93  GLU A CA  
1453  C C   . GLU A 93  ? 0.2266 0.1935 0.1947 -0.0688 -0.0031 -0.0384 93  GLU A C   
1454  O O   . GLU A 93  ? 0.2209 0.1701 0.2176 -0.0370 -0.0138 -0.0272 93  GLU A O   
1455  C CB  . GLU A 93  ? 0.2709 0.2116 0.2363 -0.0538 -0.0709 -0.0501 93  GLU A CB  
1456  C CG  . GLU A 93  ? 0.3756 0.2343 0.2835 -0.0718 -0.0791 -0.0496 93  GLU A CG  
1457  C CD  . GLU A 93  ? 0.4560 0.2421 0.3167 -0.1152 -0.0926 -0.0484 93  GLU A CD  
1458  O OE1 . GLU A 93  ? 0.5010 0.1748 0.3398 -0.0975 -0.1159 0.0136  93  GLU A OE1 
1459  O OE2 . GLU A 93  ? 0.5132 0.2654 0.3421 -0.0680 -0.0368 -0.0807 93  GLU A OE2 
1466  N N   . PRO A 94  ? 0.2017 0.1937 0.1703 -0.0612 0.0123  -0.0062 94  PRO A N   
1467  C CA  . PRO A 94  ? 0.2118 0.2122 0.1705 -0.0711 0.0090  -0.0045 94  PRO A CA  
1468  C C   . PRO A 94  ? 0.1964 0.2137 0.1678 -0.0491 0.0131  -0.0048 94  PRO A C   
1469  O O   . PRO A 94  ? 0.2119 0.1812 0.1787 -0.0210 -0.0002 0.0106  94  PRO A O   
1470  C CB  . PRO A 94  ? 0.2391 0.1909 0.1857 -0.0712 0.0228  0.0143  94  PRO A CB  
1471  C CG  . PRO A 94  ? 0.2705 0.2302 0.2050 -0.0677 0.0151  0.0207  94  PRO A CG  
1472  C CD  . PRO A 94  ? 0.2144 0.2137 0.1876 -0.0648 0.0113  0.0099  94  PRO A CD  
1480  N N   . GLN A 95  ? 0.1737 0.1657 0.1774 -0.0914 0.0056  -0.0220 95  GLN A N   
1481  C CA  . GLN A 95  ? 0.1879 0.1785 0.1812 -0.0730 0.0200  -0.0062 95  GLN A CA  
1482  C C   . GLN A 95  ? 0.1593 0.2285 0.1820 -0.0456 0.0078  -0.0005 95  GLN A C   
1483  O O   . GLN A 95  ? 0.1541 0.2222 0.1897 -0.0383 -0.0056 0.0035  95  GLN A O   
1484  C CB  . GLN A 95  ? 0.1525 0.1745 0.2019 -0.0743 0.0238  -0.0019 95  GLN A CB  
1485  C CG  . GLN A 95  ? 0.2667 0.1929 0.2254 -0.0483 -0.0069 -0.0076 95  GLN A CG  
1486  C CD  . GLN A 95  ? 0.2768 0.2568 0.2697 -0.0484 0.0091  0.0422  95  GLN A CD  
1487  O OE1 . GLN A 95  ? 0.2255 0.2578 0.2987 -0.0064 0.0354  0.0532  95  GLN A OE1 
1488  N NE2 . GLN A 95  ? 0.2787 0.3273 0.2733 -0.0599 -0.0054 0.0777  95  GLN A NE2 
1497  N N   . ILE A 96  ? 0.1676 0.2203 0.1779 -0.0315 0.0026  -0.0002 96  ILE A N   
1498  C CA  . ILE A 96  ? 0.1453 0.1655 0.1838 -0.0441 0.0038  -0.0016 96  ILE A CA  
1499  C C   . ILE A 96  ? 0.1751 0.1622 0.1969 -0.0470 -0.0069 0.0019  96  ILE A C   
1500  O O   . ILE A 96  ? 0.1861 0.1622 0.1990 -0.0199 -0.0131 -0.0115 96  ILE A O   
1501  C CB  . ILE A 96  ? 0.1404 0.2186 0.1838 -0.0313 -0.0209 0.0035  96  ILE A CB  
1502  C CG1 . ILE A 96  ? 0.1447 0.2288 0.1977 -0.0440 -0.0089 -0.0096 96  ILE A CG1 
1503  C CG2 . ILE A 96  ? 0.1628 0.2414 0.1973 -0.0068 -0.0323 0.0141  96  ILE A CG2 
1504  C CD1 . ILE A 96  ? 0.1888 0.1984 0.2115 0.0026  0.0051  -0.0120 96  ILE A CD1 
1517  N N   . GLN A 97  ? 0.1653 0.1524 0.2070 -0.0476 -0.0106 0.0087  97  GLN A N   
1518  C CA  . GLN A 97  ? 0.1803 0.1601 0.1959 -0.0497 -0.0030 -0.0079 97  GLN A CA  
1519  C C   . GLN A 97  ? 0.1864 0.1670 0.1699 -0.0661 -0.0225 -0.0062 97  GLN A C   
1520  O O   . GLN A 97  ? 0.1992 0.1743 0.1863 -0.0505 -0.0012 0.0044  97  GLN A O   
1521  C CB  . GLN A 97  ? 0.2214 0.1266 0.2300 -0.0672 0.0039  0.0027  97  GLN A CB  
1522  C CG  . GLN A 97  ? 0.2818 0.1305 0.2637 -0.0721 -0.0415 -0.0091 97  GLN A CG  
1523  C CD  . GLN A 97  ? 0.3835 0.2176 0.3046 -0.0923 -0.1032 0.0144  97  GLN A CD  
1524  O OE1 . GLN A 97  ? 0.4095 0.2683 0.3464 -0.0744 -0.1261 0.0043  97  GLN A OE1 
1525  N NE2 . GLN A 97  ? 0.4195 0.2328 0.2990 -0.0954 -0.0653 -0.0038 97  GLN A NE2 
1534  N N   . LEU A 98  ? 0.1547 0.1466 0.1680 -0.0174 -0.0285 -0.0173 98  LEU A N   
1535  C CA  . LEU A 98  ? 0.1763 0.1751 0.1673 -0.0328 -0.0061 -0.0029 98  LEU A CA  
1536  C C   . LEU A 98  ? 0.1534 0.1862 0.1640 -0.0226 -0.0086 -0.0028 98  LEU A C   
1537  O O   . LEU A 98  ? 0.1593 0.1776 0.1623 -0.0422 0.0006  -0.0078 98  LEU A O   
1538  C CB  . LEU A 98  ? 0.2281 0.1532 0.1678 -0.0435 0.0095  -0.0077 98  LEU A CB  
1539  C CG  . LEU A 98  ? 0.1969 0.1705 0.1646 -0.0292 -0.0024 0.0034  98  LEU A CG  
1540  C CD1 . LEU A 98  ? 0.1888 0.1740 0.1653 -0.0395 -0.0267 0.0162  98  LEU A CD1 
1541  C CD2 . LEU A 98  ? 0.1699 0.1634 0.1619 -0.0189 0.0124  0.0021  98  LEU A CD2 
1553  N N   . SER A 99  ? 0.1533 0.1735 0.1646 -0.0085 -0.0149 0.0118  99  SER A N   
1554  C CA  . SER A 99  ? 0.1449 0.1751 0.1686 0.0015  -0.0342 0.0020  99  SER A CA  
1555  C C   . SER A 99  ? 0.1924 0.2037 0.1713 -0.0274 -0.0321 0.0062  99  SER A C   
1556  O O   . SER A 99  ? 0.1445 0.2165 0.1776 -0.0011 -0.0059 -0.0068 99  SER A O   
1557  C CB  . SER A 99  ? 0.1659 0.2050 0.1544 0.0070  0.0049  -0.0158 99  SER A CB  
1558  O OG  . SER A 99  ? 0.1527 0.2362 0.1432 -0.0160 -0.0008 -0.0368 99  SER A OG  
1564  N N   . GLU A 100 ? 0.1612 0.2074 0.1666 -0.0306 -0.0322 -0.0280 100 GLU A N   
1565  C CA  . GLU A 100 ? 0.1654 0.2155 0.1613 -0.0166 -0.0359 -0.0217 100 GLU A CA  
1566  C C   . GLU A 100 ? 0.1690 0.1866 0.1657 -0.0405 -0.0143 -0.0112 100 GLU A C   
1567  O O   . GLU A 100 ? 0.1865 0.1847 0.1715 -0.0233 0.0195  -0.0268 100 GLU A O   
1568  C CB  . GLU A 100 ? 0.1850 0.1967 0.1578 -0.0405 0.0022  -0.0251 100 GLU A CB  
1569  C CG  . GLU A 100 ? 0.1959 0.1973 0.1884 -0.0513 0.0123  -0.0376 100 GLU A CG  
1570  C CD  . GLU A 100 ? 0.1615 0.1820 0.2225 0.0065  -0.0079 -0.0489 100 GLU A CD  
1571  O OE1 . GLU A 100 ? 0.1580 0.1686 0.2258 -0.0089 -0.0308 -0.0096 100 GLU A OE1 
1572  O OE2 . GLU A 100 ? 0.1956 0.1886 0.2690 -0.0113 -0.0082 -0.0584 100 GLU A OE2 
1579  N N   . LYS A 101 ? 0.1906 0.1867 0.1800 -0.0127 -0.0212 -0.0194 101 LYS A N   
1580  C CA  . LYS A 101 ? 0.1538 0.1869 0.1811 -0.0184 -0.0240 -0.0120 101 LYS A CA  
1581  C C   . LYS A 101 ? 0.1745 0.1986 0.1768 -0.0402 -0.0090 -0.0031 101 LYS A C   
1582  O O   . LYS A 101 ? 0.1734 0.2334 0.1830 -0.0272 -0.0002 0.0016  101 LYS A O   
1583  C CB  . LYS A 101 ? 0.2108 0.1777 0.1925 -0.0636 -0.0480 -0.0087 101 LYS A CB  
1584  C CG  . LYS A 101 ? 0.2452 0.2334 0.2315 -0.0546 -0.0193 -0.0112 101 LYS A CG  
1585  C CD  . LYS A 101 ? 0.3645 0.2773 0.2622 -0.0745 -0.0168 -0.0271 101 LYS A CD  
1586  C CE  . LYS A 101 ? 0.4290 0.3756 0.2823 -0.0725 0.0042  -0.0478 101 LYS A CE  
1587  N NZ  . LYS A 101 ? 0.5266 0.4387 0.3060 -0.0686 0.0288  -0.0512 101 LYS A NZ  
1601  N N   . ILE A 102 ? 0.1652 0.2152 0.1656 -0.0306 -0.0137 0.0048  102 ILE A N   
1602  C CA  . ILE A 102 ? 0.1566 0.2194 0.1710 -0.0342 -0.0135 -0.0125 102 ILE A CA  
1603  C C   . ILE A 102 ? 0.1499 0.1963 0.1648 -0.0437 -0.0194 -0.0040 102 ILE A C   
1604  O O   . ILE A 102 ? 0.1666 0.2139 0.1776 -0.0388 -0.0009 0.0198  102 ILE A O   
1605  C CB  . ILE A 102 ? 0.1379 0.1781 0.1717 -0.0203 -0.0462 -0.0270 102 ILE A CB  
1606  C CG1 . ILE A 102 ? 0.1607 0.1526 0.1816 -0.0289 -0.0455 0.0048  102 ILE A CG1 
1607  C CG2 . ILE A 102 ? 0.1454 0.2087 0.1915 -0.0079 -0.0453 -0.0259 102 ILE A CG2 
1608  C CD1 . ILE A 102 ? 0.2030 0.1846 0.1833 -0.0496 -0.0581 0.0060  102 ILE A CD1 
1620  N N   . LEU A 103 ? 0.1315 0.1827 0.1744 -0.0416 -0.0059 0.0033  103 LEU A N   
1621  C CA  . LEU A 103 ? 0.1726 0.2036 0.1778 -0.0264 -0.0003 0.0273  103 LEU A CA  
1622  C C   . LEU A 103 ? 0.1680 0.1778 0.1762 -0.0262 -0.0017 0.0081  103 LEU A C   
1623  O O   . LEU A 103 ? 0.2298 0.1915 0.1763 -0.0498 -0.0077 0.0278  103 LEU A O   
1624  C CB  . LEU A 103 ? 0.1449 0.1802 0.1940 0.0022  0.0160  0.0241  103 LEU A CB  
1625  C CG  . LEU A 103 ? 0.1206 0.2125 0.1962 -0.0259 0.0222  0.0069  103 LEU A CG  
1626  C CD1 . LEU A 103 ? 0.1517 0.2294 0.1926 0.0034  0.0142  0.0119  103 LEU A CD1 
1627  C CD2 . LEU A 103 ? 0.1570 0.2260 0.2100 0.0029  -0.0016 -0.0026 103 LEU A CD2 
1639  N N   . GLU A 104 ? 0.1666 0.2263 0.1787 -0.0272 0.0077  0.0086  104 GLU A N   
1640  C CA  . GLU A 104 ? 0.2363 0.2283 0.1624 -0.0188 -0.0083 0.0149  104 GLU A CA  
1641  C C   . GLU A 104 ? 0.2125 0.2201 0.1490 -0.0316 0.0155  0.0152  104 GLU A C   
1642  O O   . GLU A 104 ? 0.2337 0.2586 0.1575 -0.0386 0.0009  0.0492  104 GLU A O   
1643  C CB  . GLU A 104 ? 0.2923 0.2248 0.1907 -0.0417 -0.0417 0.0168  104 GLU A CB  
1644  C CG  . GLU A 104 ? 0.5216 0.3126 0.2336 -0.0355 -0.0800 0.0286  104 GLU A CG  
1645  C CD  . GLU A 104 ? 0.7314 0.4145 0.2690 -0.0030 -0.1092 0.0029  104 GLU A CD  
1646  O OE1 . GLU A 104 ? 0.7865 0.4072 0.2765 -0.0368 -0.1440 -0.0225 104 GLU A OE1 
1647  O OE2 . GLU A 104 ? 0.7937 0.5244 0.3036 0.0354  -0.1146 0.0168  104 GLU A OE2 
1654  N N   . LEU A 105 ? 0.1816 0.2024 0.1376 -0.0378 0.0166  -0.0087 105 LEU A N   
1655  C CA  . LEU A 105 ? 0.1834 0.2074 0.1597 -0.0797 0.0187  -0.0160 105 LEU A CA  
1656  C C   . LEU A 105 ? 0.1795 0.2422 0.1788 -0.0629 0.0169  -0.0284 105 LEU A C   
1657  O O   . LEU A 105 ? 0.2014 0.2232 0.2085 -0.0424 0.0264  -0.0277 105 LEU A O   
1658  C CB  . LEU A 105 ? 0.1989 0.2208 0.1832 -0.0390 0.0112  -0.0218 105 LEU A CB  
1659  C CG  . LEU A 105 ? 0.2561 0.2219 0.2015 -0.0176 0.0242  -0.0312 105 LEU A CG  
1660  C CD1 . LEU A 105 ? 0.2954 0.2254 0.2138 0.0114  0.0032  -0.0288 105 LEU A CD1 
1661  C CD2 . LEU A 105 ? 0.3098 0.2679 0.2310 -0.0276 0.0280  -0.0357 105 LEU A CD2 
1673  N N   . ALA A 106 ? 0.1869 0.2640 0.1846 -0.0470 0.0188  -0.0243 106 ALA A N   
1674  C CA  . ALA A 106 ? 0.2353 0.2128 0.1897 -0.0604 0.0108  -0.0030 106 ALA A CA  
1675  C C   . ALA A 106 ? 0.2478 0.2292 0.2039 -0.0438 0.0295  0.0224  106 ALA A C   
1676  O O   . ALA A 106 ? 0.2755 0.2416 0.2249 -0.0102 0.0105  0.0417  106 ALA A O   
1677  C CB  . ALA A 106 ? 0.2415 0.2331 0.2009 -0.0367 0.0257  -0.0050 106 ALA A CB  
1683  N N   . GLY A 107 ? 0.2051 0.2482 0.1964 0.0007  0.0223  0.0522  107 GLY A N   
1684  C CA  . GLY A 107 ? 0.2707 0.2701 0.2057 -0.0110 0.0025  0.0236  107 GLY A CA  
1685  C C   . GLY A 107 ? 0.3397 0.2705 0.2064 0.0296  -0.0349 0.0128  107 GLY A C   
1686  O O   . GLY A 107 ? 0.3076 0.2662 0.2183 0.0737  -0.0266 0.0107  107 GLY A O   
1690  N N   . PRO A 108 ? 0.4465 0.2936 0.2103 0.0739  -0.0785 0.0033  108 PRO A N   
1691  C CA  . PRO A 108 ? 0.5079 0.3552 0.2156 0.0689  -0.0763 -0.0087 108 PRO A CA  
1692  C C   . PRO A 108 ? 0.4918 0.3050 0.2300 0.0339  -0.0367 0.0164  108 PRO A C   
1693  O O   . PRO A 108 ? 0.6202 0.2239 0.2487 -0.0380 -0.0100 0.0033  108 PRO A O   
1694  C CB  . PRO A 108 ? 0.5464 0.3648 0.2139 0.0807  -0.0834 -0.0131 108 PRO A CB  
1695  C CG  . PRO A 108 ? 0.5102 0.3262 0.2217 0.0603  -0.0728 -0.0067 108 PRO A CG  
1696  C CD  . PRO A 108 ? 0.4735 0.2860 0.2112 0.0679  -0.0729 0.0128  108 PRO A CD  
1704  N N   . GLY A 109 ? 0.3513 0.3016 0.1978 0.0635  0.0194  0.0618  109 GLY A N   
1705  C CA  . GLY A 109 ? 0.2804 0.2366 0.1908 0.0206  -0.0054 0.0429  109 GLY A CA  
1706  C C   . GLY A 109 ? 0.2040 0.1921 0.1836 -0.0003 -0.0057 0.0323  109 GLY A C   
1707  O O   . GLY A 109 ? 0.2641 0.2139 0.1953 0.0018  0.0066  0.0088  109 GLY A O   
1711  N N   . MET A 110 ? 0.2383 0.1671 0.1683 -0.0288 -0.0085 0.0204  110 MET A N   
1712  C CA  . MET A 110 ? 0.1741 0.1654 0.1639 -0.0053 -0.0021 -0.0101 110 MET A CA  
1713  C C   . MET A 110 ? 0.1608 0.1676 0.1663 -0.0384 -0.0237 -0.0138 110 MET A C   
1714  O O   . MET A 110 ? 0.1658 0.2483 0.1851 -0.0255 -0.0294 -0.0411 110 MET A O   
1715  C CB  . MET A 110 ? 0.1664 0.1916 0.1850 -0.0181 -0.0414 -0.0144 110 MET A CB  
1716  C CG  . MET A 110 ? 0.1616 0.1844 0.2102 -0.0004 -0.0100 0.0032  110 MET A CG  
1717  S SD  . MET A 110 ? 0.1985 0.1730 0.2380 -0.0204 -0.0191 -0.0078 110 MET A SD  
1718  C CE  . MET A 110 ? 0.2543 0.2133 0.2579 -0.0515 0.0177  0.0056  110 MET A CE  
1728  N N   . SER A 111 ? 0.1503 0.1873 0.1785 -0.0249 -0.0131 0.0055  111 SER A N   
1729  C CA  . SER A 111 ? 0.1154 0.1713 0.1940 -0.0133 -0.0106 -0.0028 111 SER A CA  
1730  C C   . SER A 111 ? 0.1521 0.1857 0.1904 -0.0420 -0.0167 -0.0027 111 SER A C   
1731  O O   . SER A 111 ? 0.1717 0.1453 0.1945 -0.0116 -0.0192 0.0016  111 SER A O   
1732  C CB  . SER A 111 ? 0.1734 0.1756 0.2040 0.0038  -0.0125 0.0325  111 SER A CB  
1733  O OG  . SER A 111 ? 0.1699 0.2149 0.2004 0.0112  -0.0167 0.0285  111 SER A OG  
1739  N N   . LYS A 112 ? 0.1472 0.1941 0.1732 -0.0742 -0.0199 0.0029  112 LYS A N   
1740  C CA  . LYS A 112 ? 0.1220 0.1870 0.1746 -0.0187 -0.0029 -0.0056 112 LYS A CA  
1741  C C   . LYS A 112 ? 0.1177 0.1906 0.1671 -0.0132 -0.0114 0.0109  112 LYS A C   
1742  O O   . LYS A 112 ? 0.1484 0.1801 0.1763 -0.0128 -0.0273 0.0083  112 LYS A O   
1743  C CB  . LYS A 112 ? 0.1515 0.1878 0.1664 0.0004  0.0018  -0.0020 112 LYS A CB  
1744  C CG  . LYS A 112 ? 0.1134 0.2017 0.1710 -0.0066 0.0015  0.0107  112 LYS A CG  
1745  C CD  . LYS A 112 ? 0.1665 0.1741 0.1686 -0.0377 -0.0412 0.0395  112 LYS A CD  
1746  C CE  . LYS A 112 ? 0.2004 0.1546 0.1710 -0.0005 -0.0301 0.0143  112 LYS A CE  
1747  N NZ  . LYS A 112 ? 0.2321 0.1712 0.1795 -0.0494 -0.0447 0.0188  112 LYS A NZ  
1761  N N   . VAL A 113 ? 0.1217 0.2067 0.1481 -0.0324 -0.0102 0.0383  113 VAL A N   
1762  C CA  . VAL A 113 ? 0.1305 0.1724 0.1534 -0.0305 -0.0160 -0.0001 113 VAL A CA  
1763  C C   . VAL A 113 ? 0.1638 0.1546 0.1580 -0.0363 0.0178  -0.0028 113 VAL A C   
1764  O O   . VAL A 113 ? 0.1480 0.1800 0.1599 -0.0390 -0.0007 -0.0017 113 VAL A O   
1765  C CB  . VAL A 113 ? 0.1337 0.1710 0.1446 -0.0229 -0.0180 -0.0063 113 VAL A CB  
1766  C CG1 . VAL A 113 ? 0.1666 0.1677 0.1505 0.0033  0.0084  -0.0100 113 VAL A CG1 
1767  C CG2 . VAL A 113 ? 0.1949 0.1999 0.1243 0.0113  -0.0243 0.0123  113 VAL A CG2 
1777  N N   . TYR A 114 ? 0.1582 0.1766 0.1419 -0.0331 0.0012  -0.0042 114 TYR A N   
1778  C CA  . TYR A 114 ? 0.1430 0.1919 0.1488 -0.0374 0.0070  -0.0126 114 TYR A CA  
1779  C C   . TYR A 114 ? 0.1254 0.1639 0.1476 -0.0291 0.0016  0.0090  114 TYR A C   
1780  O O   . TYR A 114 ? 0.1289 0.1945 0.1511 -0.0118 -0.0067 -0.0040 114 TYR A O   
1781  C CB  . TYR A 114 ? 0.1583 0.2085 0.1608 -0.0197 0.0072  0.0028  114 TYR A CB  
1782  C CG  . TYR A 114 ? 0.1327 0.1603 0.1507 -0.0540 -0.0115 0.0195  114 TYR A CG  
1783  C CD1 . TYR A 114 ? 0.1566 0.1785 0.1593 -0.0316 -0.0243 0.0137  114 TYR A CD1 
1784  C CD2 . TYR A 114 ? 0.1368 0.1468 0.1462 -0.0482 0.0122  -0.0166 114 TYR A CD2 
1785  C CE1 . TYR A 114 ? 0.1527 0.1931 0.1599 -0.0402 -0.0250 0.0078  114 TYR A CE1 
1786  C CE2 . TYR A 114 ? 0.1726 0.1651 0.1418 -0.0554 0.0195  -0.0235 114 TYR A CE2 
1787  C CZ  . TYR A 114 ? 0.1595 0.1844 0.1492 -0.0270 -0.0115 -0.0162 114 TYR A CZ  
1788  O OH  . TYR A 114 ? 0.2023 0.2161 0.1617 -0.0082 -0.0232 -0.0127 114 TYR A OH  
1798  N N   . TYR A 115 ? 0.1628 0.1138 0.1568 -0.0326 -0.0067 0.0090  115 TYR A N   
1799  C CA  . TYR A 115 ? 0.1697 0.1280 0.1480 -0.0285 -0.0111 0.0005  115 TYR A CA  
1800  C C   . TYR A 115 ? 0.1565 0.1589 0.1525 -0.0221 0.0092  0.0234  115 TYR A C   
1801  O O   . TYR A 115 ? 0.1578 0.1558 0.1473 -0.0033 -0.0040 0.0084  115 TYR A O   
1802  C CB  . TYR A 115 ? 0.1615 0.1535 0.1623 -0.0071 -0.0095 -0.0121 115 TYR A CB  
1803  C CG  . TYR A 115 ? 0.1522 0.1458 0.1523 -0.0287 -0.0171 -0.0146 115 TYR A CG  
1804  C CD1 . TYR A 115 ? 0.1459 0.1639 0.1414 0.0020  -0.0275 -0.0271 115 TYR A CD1 
1805  C CD2 . TYR A 115 ? 0.1638 0.1331 0.1538 -0.0166 -0.0177 -0.0064 115 TYR A CD2 
1806  C CE1 . TYR A 115 ? 0.1947 0.1713 0.1520 0.0143  -0.0425 -0.0161 115 TYR A CE1 
1807  C CE2 . TYR A 115 ? 0.1807 0.1634 0.1571 -0.0502 0.0091  -0.0214 115 TYR A CE2 
1808  C CZ  . TYR A 115 ? 0.1764 0.1850 0.1538 -0.0303 -0.0055 -0.0016 115 TYR A CZ  
1809  O OH  . TYR A 115 ? 0.2060 0.2221 0.1485 -0.0223 -0.0044 -0.0162 115 TYR A OH  
1819  N N   . GLY A 116 ? 0.1215 0.1759 0.1489 -0.0202 -0.0137 0.0342  116 GLY A N   
1820  C CA  . GLY A 116 ? 0.1932 0.1363 0.1523 0.0024  -0.0163 0.0455  116 GLY A CA  
1821  C C   . GLY A 116 ? 0.1590 0.1247 0.1705 -0.0241 0.0028  0.0358  116 GLY A C   
1822  O O   . GLY A 116 ? 0.1683 0.1662 0.1690 -0.0169 -0.0023 0.0026  116 GLY A O   
1826  N N   A MET A 117 ? 0.1440 0.1540 0.1829 -0.0142 0.0055  0.0247  117 MET A N   
1827  N N   B MET A 117 ? 0.1429 0.1437 0.1748 -0.0127 0.0110  0.0077  117 MET A N   
1828  C CA  A MET A 117 ? 0.1652 0.1640 0.1901 -0.0486 -0.0123 0.0237  117 MET A CA  
1829  C CA  B MET A 117 ? 0.1511 0.1447 0.1754 -0.0414 -0.0016 -0.0070 117 MET A CA  
1830  C C   A MET A 117 ? 0.1832 0.1567 0.2034 -0.0275 0.0033  0.0266  117 MET A C   
1831  C C   B MET A 117 ? 0.1778 0.1331 0.1810 -0.0155 -0.0061 -0.0102 117 MET A C   
1832  O O   A MET A 117 ? 0.2076 0.1431 0.2252 -0.0309 -0.0330 0.0572  117 MET A O   
1833  O O   B MET A 117 ? 0.1930 0.1439 0.1801 -0.0070 -0.0160 -0.0087 117 MET A O   
1834  C CB  A MET A 117 ? 0.2010 0.1992 0.1867 -0.0428 -0.0106 0.0331  117 MET A CB  
1835  C CB  B MET A 117 ? 0.1511 0.1678 0.1709 -0.0453 0.0154  -0.0073 117 MET A CB  
1836  C CG  A MET A 117 ? 0.1558 0.2380 0.1867 -0.0461 -0.0087 0.0377  117 MET A CG  
1837  C CG  B MET A 117 ? 0.1655 0.2020 0.1694 -0.0231 0.0272  -0.0057 117 MET A CG  
1838  S SD  A MET A 117 ? 0.1510 0.2436 0.1938 -0.0687 -0.0037 0.0467  117 MET A SD  
1839  S SD  B MET A 117 ? 0.2170 0.2020 0.1719 -0.0214 0.0059  -0.0043 117 MET A SD  
1840  C CE  A MET A 117 ? 0.1736 0.2631 0.2013 -0.0432 -0.0241 0.0456  117 MET A CE  
1841  C CE  B MET A 117 ? 0.2391 0.2369 0.1763 -0.0202 0.0076  -0.0053 117 MET A CE  
1860  N N   . SER A 118 ? 0.1707 0.1197 0.1986 -0.0485 0.0014  0.0021  118 SER A N   
1861  C CA  . SER A 118 ? 0.1622 0.1357 0.1689 -0.0689 -0.0065 0.0019  118 SER A CA  
1862  C C   . SER A 118 ? 0.1820 0.1496 0.1484 -0.0541 0.0022  0.0041  118 SER A C   
1863  O O   . SER A 118 ? 0.1920 0.1683 0.1423 -0.0269 0.0063  0.0099  118 SER A O   
1864  C CB  . SER A 118 ? 0.1655 0.1621 0.1641 -0.0210 -0.0028 -0.0006 118 SER A CB  
1865  O OG  . SER A 118 ? 0.2284 0.1573 0.1678 -0.0234 -0.0080 -0.0138 118 SER A OG  
1872  N N   . GLY A 119 ? 0.1687 0.1570 0.1464 -0.0405 0.0220  -0.0104 119 GLY A N   
1873  C CA  . GLY A 119 ? 0.1288 0.1804 0.1386 -0.0254 0.0082  0.0056  119 GLY A CA  
1874  C C   . GLY A 119 ? 0.1356 0.1788 0.1419 -0.0340 -0.0010 0.0106  119 GLY A C   
1875  O O   . GLY A 119 ? 0.1974 0.2012 0.1406 -0.0154 0.0029  0.0033  119 GLY A O   
1879  N N   . SER A 120 ? 0.1495 0.1694 0.1258 0.0114  -0.0125 0.0003  120 SER A N   
1880  C CA  . SER A 120 ? 0.1804 0.1331 0.1428 -0.0365 0.0119  -0.0012 120 SER A CA  
1881  C C   . SER A 120 ? 0.1622 0.1303 0.1522 -0.0151 -0.0245 0.0094  120 SER A C   
1882  O O   . SER A 120 ? 0.1715 0.1306 0.1548 -0.0314 0.0114  -0.0017 120 SER A O   
1883  C CB  . SER A 120 ? 0.1652 0.1536 0.1491 -0.0317 -0.0042 -0.0038 120 SER A CB  
1884  O OG  . SER A 120 ? 0.1672 0.1546 0.1399 -0.0322 0.0015  -0.0058 120 SER A OG  
1890  N N   . ASP A 121 ? 0.1932 0.1265 0.1515 -0.0090 -0.0108 -0.0107 121 ASP A N   
1891  C CA  . ASP A 121 ? 0.1328 0.1247 0.1395 0.0067  -0.0232 0.0023  121 ASP A CA  
1892  C C   . ASP A 121 ? 0.1399 0.1320 0.1429 0.0080  0.0126  -0.0035 121 ASP A C   
1893  O O   . ASP A 121 ? 0.1580 0.1201 0.1370 -0.0330 0.0171  0.0031  121 ASP A O   
1894  C CB  . ASP A 121 ? 0.1388 0.1333 0.1605 -0.0238 -0.0213 0.0156  121 ASP A CB  
1895  C CG  . ASP A 121 ? 0.1571 0.1424 0.1762 -0.0188 -0.0309 0.0597  121 ASP A CG  
1896  O OD1 . ASP A 121 ? 0.1835 0.1578 0.1653 -0.0224 -0.0139 0.0188  121 ASP A OD1 
1897  O OD2 . ASP A 121 ? 0.2114 0.1340 0.2153 -0.0574 -0.0481 0.0252  121 ASP A OD2 
1902  N N   . ALA A 122 ? 0.1393 0.1600 0.1488 -0.0216 0.0007  0.0013  122 ALA A N   
1903  C CA  . ALA A 122 ? 0.1326 0.1497 0.1449 -0.0296 -0.0062 -0.0136 122 ALA A CA  
1904  C C   . ALA A 122 ? 0.1422 0.1315 0.1383 -0.0308 -0.0120 0.0061  122 ALA A C   
1905  O O   . ALA A 122 ? 0.1505 0.1762 0.1603 -0.0170 0.0008  0.0123  122 ALA A O   
1906  C CB  . ALA A 122 ? 0.1631 0.1569 0.1515 -0.0241 0.0098  0.0207  122 ALA A CB  
1912  N N   . ASN A 123 ? 0.1612 0.1198 0.1470 0.0157  -0.0124 0.0226  123 ASN A N   
1913  C CA  . ASN A 123 ? 0.1182 0.1369 0.1513 0.0044  -0.0092 0.0243  123 ASN A CA  
1914  C C   . ASN A 123 ? 0.1467 0.1429 0.1517 -0.0136 -0.0159 0.0176  123 ASN A C   
1915  O O   . ASN A 123 ? 0.1527 0.1427 0.1526 -0.0169 -0.0189 0.0247  123 ASN A O   
1916  C CB  . ASN A 123 ? 0.1151 0.1604 0.1560 0.0048  -0.0009 0.0189  123 ASN A CB  
1917  C CG  . ASN A 123 ? 0.1425 0.1318 0.1531 0.0056  0.0145  0.0251  123 ASN A CG  
1918  O OD1 . ASN A 123 ? 0.1392 0.1540 0.1426 -0.0072 -0.0110 0.0286  123 ASN A OD1 
1919  N ND2 . ASN A 123 ? 0.1510 0.1232 0.1490 -0.0075 0.0330  0.0096  123 ASN A ND2 
1926  N N   . GLU A 124 ? 0.1258 0.1379 0.1576 0.0035  -0.0026 -0.0016 124 GLU A N   
1927  C CA  . GLU A 124 ? 0.1180 0.1422 0.1524 -0.0351 0.0155  -0.0005 124 GLU A CA  
1928  C C   . GLU A 124 ? 0.1236 0.1623 0.1562 -0.0388 0.0018  -0.0167 124 GLU A C   
1929  O O   . GLU A 124 ? 0.1348 0.1935 0.1554 -0.0027 0.0124  -0.0227 124 GLU A O   
1930  C CB  . GLU A 124 ? 0.1419 0.1253 0.1574 -0.0092 0.0084  0.0305  124 GLU A CB  
1931  C CG  . GLU A 124 ? 0.1717 0.1276 0.1582 -0.0052 -0.0293 0.0030  124 GLU A CG  
1932  C CD  . GLU A 124 ? 0.1846 0.1635 0.1683 -0.0093 0.0051  0.0187  124 GLU A CD  
1933  O OE1 . GLU A 124 ? 0.1867 0.1494 0.1650 -0.0315 -0.0095 0.0258  124 GLU A OE1 
1934  O OE2 . GLU A 124 ? 0.1626 0.1740 0.1689 -0.0171 -0.0169 -0.0016 124 GLU A OE2 
1941  N N   . THR A 125 ? 0.1182 0.1624 0.1531 -0.0160 -0.0069 0.0009  125 THR A N   
1942  C CA  . THR A 125 ? 0.1353 0.1665 0.1530 -0.0222 -0.0150 0.0170  125 THR A CA  
1943  C C   . THR A 125 ? 0.1513 0.1733 0.1534 -0.0325 -0.0134 0.0118  125 THR A C   
1944  O O   . THR A 125 ? 0.1363 0.1938 0.1465 -0.0287 0.0086  0.0229  125 THR A O   
1945  C CB  . THR A 125 ? 0.1675 0.1526 0.1410 -0.0452 0.0018  0.0130  125 THR A CB  
1946  O OG1 . THR A 125 ? 0.1526 0.1394 0.1374 -0.0246 -0.0165 0.0153  125 THR A OG1 
1947  C CG2 . THR A 125 ? 0.2145 0.1904 0.1574 -0.0274 -0.0219 -0.0184 125 THR A CG2 
1955  N N   . GLN A 126 ? 0.1439 0.1362 0.1639 -0.0126 -0.0028 -0.0052 126 GLN A N   
1956  C CA  . GLN A 126 ? 0.1314 0.1150 0.1638 -0.0617 0.0123  0.0136  126 GLN A CA  
1957  C C   . GLN A 126 ? 0.1552 0.1150 0.1544 -0.0181 0.0074  0.0175  126 GLN A C   
1958  O O   . GLN A 126 ? 0.1370 0.1200 0.1577 0.0041  -0.0080 -0.0004 126 GLN A O   
1959  C CB  . GLN A 126 ? 0.1635 0.1084 0.1577 -0.0117 -0.0030 0.0092  126 GLN A CB  
1960  C CG  . GLN A 126 ? 0.1350 0.1106 0.1540 -0.0019 -0.0004 -0.0312 126 GLN A CG  
1961  C CD  . GLN A 126 ? 0.1449 0.1635 0.1566 -0.0078 0.0062  -0.0209 126 GLN A CD  
1962  O OE1 . GLN A 126 ? 0.1717 0.1982 0.1625 -0.0121 -0.0163 0.0006  126 GLN A OE1 
1963  N NE2 . GLN A 126 ? 0.1579 0.1537 0.1412 0.0052  -0.0122 -0.0199 126 GLN A NE2 
1972  N N   . LEU A 127 ? 0.1808 0.1277 0.1432 0.0085  0.0116  0.0279  127 LEU A N   
1973  C CA  . LEU A 127 ? 0.1543 0.1370 0.1461 -0.0417 0.0116  0.0126  127 LEU A CA  
1974  C C   . LEU A 127 ? 0.1345 0.1381 0.1534 -0.0279 0.0207  -0.0075 127 LEU A C   
1975  O O   . LEU A 127 ? 0.1553 0.1758 0.1578 0.0130  0.0177  0.0143  127 LEU A O   
1976  C CB  . LEU A 127 ? 0.1609 0.1735 0.1406 -0.0482 0.0215  0.0202  127 LEU A CB  
1977  C CG  . LEU A 127 ? 0.1539 0.1594 0.1579 -0.0276 0.0142  0.0290  127 LEU A CG  
1978  C CD1 . LEU A 127 ? 0.1932 0.2221 0.1680 -0.0407 0.0121  -0.0046 127 LEU A CD1 
1979  C CD2 . LEU A 127 ? 0.1943 0.1718 0.1706 -0.0500 0.0169  0.0374  127 LEU A CD2 
1991  N N   . LYS A 128 ? 0.1332 0.1530 0.1513 -0.0025 0.0155  -0.0030 128 LYS A N   
1992  C CA  . LYS A 128 ? 0.1138 0.1446 0.1643 0.0012  -0.0007 0.0063  128 LYS A CA  
1993  C C   . LYS A 128 ? 0.1648 0.1709 0.1718 -0.0016 0.0066  0.0241  128 LYS A C   
1994  O O   . LYS A 128 ? 0.1539 0.1680 0.1785 0.0012  0.0021  0.0171  128 LYS A O   
1995  C CB  . LYS A 128 ? 0.1561 0.1983 0.1627 -0.0258 -0.0015 0.0238  128 LYS A CB  
1996  C CG  . LYS A 128 ? 0.1704 0.1846 0.1682 -0.0338 0.0061  0.0234  128 LYS A CG  
1997  C CD  . LYS A 128 ? 0.1363 0.1287 0.1837 -0.0412 -0.0255 0.0083  128 LYS A CD  
1998  C CE  . LYS A 128 ? 0.1610 0.1136 0.1672 -0.0489 0.0063  0.0208  128 LYS A CE  
1999  N NZ  . LYS A 128 ? 0.1617 0.1167 0.1599 -0.0197 -0.0030 -0.0031 128 LYS A NZ  
2013  N N   . ILE A 129 ? 0.1482 0.1753 0.1596 0.0129  0.0071  0.0287  129 ILE A N   
2014  C CA  . ILE A 129 ? 0.1278 0.1606 0.1569 -0.0074 -0.0146 0.0337  129 ILE A CA  
2015  C C   . ILE A 129 ? 0.1419 0.1523 0.1631 -0.0196 0.0126  0.0302  129 ILE A C   
2016  O O   . ILE A 129 ? 0.1802 0.1617 0.1612 -0.0163 0.0142  0.0204  129 ILE A O   
2017  C CB  . ILE A 129 ? 0.1170 0.1992 0.1557 0.0047  -0.0171 0.0148  129 ILE A CB  
2018  C CG1 . ILE A 129 ? 0.1461 0.1734 0.1538 0.0118  -0.0023 -0.0014 129 ILE A CG1 
2019  C CG2 . ILE A 129 ? 0.1342 0.2049 0.1541 -0.0052 -0.0048 -0.0104 129 ILE A CG2 
2020  C CD1 . ILE A 129 ? 0.1381 0.1933 0.1761 0.0167  -0.0233 -0.0213 129 ILE A CD1 
2032  N N   . VAL A 130 ? 0.1354 0.1300 0.1820 0.0200  0.0064  0.0114  130 VAL A N   
2033  C CA  . VAL A 130 ? 0.1547 0.1656 0.2104 -0.0175 0.0042  0.0038  130 VAL A CA  
2034  C C   . VAL A 130 ? 0.1607 0.1917 0.2031 0.0059  0.0001  0.0106  130 VAL A C   
2035  O O   . VAL A 130 ? 0.1646 0.1714 0.1960 0.0191  0.0137  -0.0096 130 VAL A O   
2036  C CB  . VAL A 130 ? 0.1687 0.1482 0.2295 0.0015  0.0313  0.0068  130 VAL A CB  
2037  C CG1 . VAL A 130 ? 0.2336 0.1642 0.2487 0.0249  0.0562  0.0304  130 VAL A CG1 
2038  C CG2 . VAL A 130 ? 0.1934 0.1773 0.2292 0.0006  0.0018  0.0436  130 VAL A CG2 
2048  N N   . ARG A 131 ? 0.1533 0.1969 0.1939 0.0059  -0.0147 0.0075  131 ARG A N   
2049  C CA  . ARG A 131 ? 0.1782 0.2061 0.1838 0.0185  -0.0217 -0.0052 131 ARG A CA  
2050  C C   . ARG A 131 ? 0.1616 0.1559 0.1712 -0.0160 0.0021  -0.0072 131 ARG A C   
2051  O O   . ARG A 131 ? 0.1834 0.1086 0.1970 -0.0050 -0.0060 0.0108  131 ARG A O   
2052  C CB  . ARG A 131 ? 0.1893 0.1989 0.1846 0.0231  -0.0554 -0.0362 131 ARG A CB  
2053  C CG  . ARG A 131 ? 0.1926 0.2431 0.1984 0.0708  -0.0598 -0.0554 131 ARG A CG  
2054  C CD  . ARG A 131 ? 0.1601 0.4310 0.2035 0.0309  -0.0393 -0.0552 131 ARG A CD  
2055  N NE  . ARG A 131 ? 0.1571 0.4799 0.2128 0.0170  -0.0262 -0.0276 131 ARG A NE  
2056  C CZ  . ARG A 131 ? 0.1423 0.3901 0.1984 -0.0098 -0.0325 0.0113  131 ARG A CZ  
2057  N NH1 . ARG A 131 ? 0.1963 0.3096 0.1911 -0.0246 0.0108  0.0234  131 ARG A NH1 
2058  N NH2 . ARG A 131 ? 0.1964 0.3764 0.2115 -0.0127 -0.0526 0.0383  131 ARG A NH2 
2072  N N   . TYR A 132 ? 0.1243 0.2045 0.1592 -0.0508 -0.0112 0.0088  132 TYR A N   
2073  C CA  . TYR A 132 ? 0.1541 0.1690 0.1765 -0.0162 -0.0224 -0.0099 132 TYR A CA  
2074  C C   . TYR A 132 ? 0.1477 0.1589 0.1895 -0.0203 -0.0168 0.0000  132 TYR A C   
2075  O O   . TYR A 132 ? 0.1542 0.1908 0.2021 -0.0125 0.0018  -0.0026 132 TYR A O   
2076  C CB  . TYR A 132 ? 0.1705 0.1527 0.1617 -0.0159 -0.0196 -0.0050 132 TYR A CB  
2077  C CG  . TYR A 132 ? 0.1325 0.1767 0.1702 -0.0068 -0.0217 0.0059  132 TYR A CG  
2078  C CD1 . TYR A 132 ? 0.1696 0.1941 0.1801 -0.0101 -0.0195 0.0043  132 TYR A CD1 
2079  C CD2 . TYR A 132 ? 0.1610 0.1960 0.1832 -0.0655 -0.0096 -0.0105 132 TYR A CD2 
2080  C CE1 . TYR A 132 ? 0.1330 0.2318 0.1857 -0.0299 -0.0099 0.0014  132 TYR A CE1 
2081  C CE2 . TYR A 132 ? 0.1739 0.1829 0.1910 -0.0798 0.0248  -0.0059 132 TYR A CE2 
2082  C CZ  . TYR A 132 ? 0.1211 0.1933 0.2003 -0.0689 0.0079  0.0050  132 TYR A CZ  
2083  O OH  . TYR A 132 ? 0.1538 0.2170 0.2150 -0.0405 -0.0308 -0.0048 132 TYR A OH  
2093  N N   . TYR A 133 ? 0.1309 0.1965 0.1781 0.0221  -0.0055 0.0015  133 TYR A N   
2094  C CA  . TYR A 133 ? 0.1241 0.1953 0.1726 0.0098  -0.0157 0.0090  133 TYR A CA  
2095  C C   . TYR A 133 ? 0.1903 0.2262 0.1771 0.0011  -0.0137 0.0270  133 TYR A C   
2096  O O   . TYR A 133 ? 0.1956 0.1921 0.1699 -0.0119 -0.0032 0.0148  133 TYR A O   
2097  C CB  . TYR A 133 ? 0.1244 0.1767 0.1868 -0.0043 -0.0020 0.0248  133 TYR A CB  
2098  C CG  . TYR A 133 ? 0.1581 0.1577 0.1877 -0.0124 -0.0126 0.0376  133 TYR A CG  
2099  C CD1 . TYR A 133 ? 0.1891 0.1992 0.1857 0.0153  -0.0272 0.0477  133 TYR A CD1 
2100  C CD2 . TYR A 133 ? 0.1521 0.1904 0.1946 0.0009  0.0330  0.0502  133 TYR A CD2 
2101  C CE1 . TYR A 133 ? 0.2236 0.1868 0.1881 0.0063  0.0008  0.0427  133 TYR A CE1 
2102  C CE2 . TYR A 133 ? 0.2113 0.1596 0.2049 -0.0406 0.0264  0.0481  133 TYR A CE2 
2103  C CZ  . TYR A 133 ? 0.2095 0.1900 0.1813 0.0289  0.0328  0.0276  133 TYR A CZ  
2104  O OH  . TYR A 133 ? 0.2586 0.2607 0.1831 0.0061  0.0333  0.0223  133 TYR A OH  
2114  N N   . ASN A 134 ? 0.1711 0.1814 0.1752 -0.0020 0.0011  0.0173  134 ASN A N   
2115  C CA  . ASN A 134 ? 0.1619 0.1782 0.1906 -0.0379 0.0210  0.0030  134 ASN A CA  
2116  C C   . ASN A 134 ? 0.1580 0.1914 0.2000 -0.0324 0.0242  0.0257  134 ASN A C   
2117  O O   . ASN A 134 ? 0.1942 0.1669 0.1988 0.0143  0.0190  -0.0004 134 ASN A O   
2118  C CB  . ASN A 134 ? 0.1855 0.1160 0.1988 -0.0278 0.0241  0.0193  134 ASN A CB  
2119  C CG  . ASN A 134 ? 0.1832 0.1671 0.2049 0.0102  0.0388  0.0100  134 ASN A CG  
2120  O OD1 . ASN A 134 ? 0.2339 0.1866 0.2259 0.0075  0.0879  0.0315  134 ASN A OD1 
2121  N ND2 . ASN A 134 ? 0.1905 0.2067 0.2103 0.0000  0.0114  -0.0168 134 ASN A ND2 
2128  N N   . ASN A 135 ? 0.1310 0.1749 0.2107 -0.0427 0.0120  0.0276  135 ASN A N   
2129  C CA  . ASN A 135 ? 0.1415 0.1480 0.2143 0.0146  0.0290  -0.0097 135 ASN A CA  
2130  C C   . ASN A 135 ? 0.1562 0.1844 0.2265 0.0338  0.0124  -0.0102 135 ASN A C   
2131  O O   . ASN A 135 ? 0.2028 0.1594 0.2360 0.0034  0.0108  0.0072  135 ASN A O   
2132  C CB  . ASN A 135 ? 0.1903 0.2007 0.2064 0.0119  0.0358  -0.0214 135 ASN A CB  
2133  C CG  . ASN A 135 ? 0.2073 0.1825 0.1931 -0.0152 0.0140  -0.0263 135 ASN A CG  
2134  O OD1 . ASN A 135 ? 0.2199 0.2156 0.1969 -0.0391 0.0036  -0.0027 135 ASN A OD1 
2135  N ND2 . ASN A 135 ? 0.2386 0.2085 0.2051 -0.0366 0.0193  -0.0072 135 ASN A ND2 
2142  N N   . VAL A 136 ? 0.1262 0.1851 0.2357 0.0035  0.0110  -0.0025 136 VAL A N   
2143  C CA  . VAL A 136 ? 0.1497 0.1572 0.2742 -0.0179 -0.0015 0.0091  136 VAL A CA  
2144  C C   . VAL A 136 ? 0.1407 0.1978 0.2705 -0.0254 -0.0054 0.0168  136 VAL A C   
2145  O O   . VAL A 136 ? 0.1552 0.2311 0.2756 -0.0103 -0.0287 0.0042  136 VAL A O   
2146  C CB  . VAL A 136 ? 0.1713 0.2508 0.3047 -0.0232 -0.0253 -0.0133 136 VAL A CB  
2147  C CG1 . VAL A 136 ? 0.1947 0.2366 0.2991 0.0218  -0.0120 -0.0084 136 VAL A CG1 
2148  C CG2 . VAL A 136 ? 0.1814 0.2757 0.3244 -0.0380 -0.0277 0.0061  136 VAL A CG2 
2158  N N   . LEU A 137 ? 0.1775 0.2247 0.2645 0.0008  0.0048  0.0174  137 LEU A N   
2159  C CA  . LEU A 137 ? 0.1570 0.1943 0.2573 0.0176  -0.0184 0.0089  137 LEU A CA  
2160  C C   . LEU A 137 ? 0.2129 0.1743 0.2675 0.0212  0.0079  0.0134  137 LEU A C   
2161  O O   . LEU A 137 ? 0.2845 0.1996 0.2724 0.0552  0.0155  0.0287  137 LEU A O   
2162  C CB  . LEU A 137 ? 0.1876 0.2134 0.2504 0.0226  -0.0052 0.0169  137 LEU A CB  
2163  C CG  . LEU A 137 ? 0.1831 0.2122 0.2413 0.0095  -0.0107 -0.0019 137 LEU A CG  
2164  C CD1 . LEU A 137 ? 0.2298 0.2512 0.2387 0.0539  0.0166  -0.0070 137 LEU A CD1 
2165  C CD2 . LEU A 137 ? 0.2788 0.2094 0.2329 0.0068  -0.0169 0.0069  137 LEU A CD2 
2177  N N   . GLY A 138 ? 0.1890 0.1710 0.2741 0.0144  0.0168  0.0106  138 GLY A N   
2178  C CA  . GLY A 138 ? 0.2198 0.1886 0.2826 0.0296  0.0478  0.0086  138 GLY A CA  
2179  C C   . GLY A 138 ? 0.2055 0.1931 0.2907 0.0063  0.0353  0.0231  138 GLY A C   
2180  O O   . GLY A 138 ? 0.1749 0.2214 0.3104 -0.0145 0.0075  0.0247  138 GLY A O   
2184  N N   . ARG A 139 ? 0.1885 0.1699 0.2822 0.0196  0.0214  0.0252  139 ARG A N   
2185  C CA  . ARG A 139 ? 0.1808 0.1715 0.2697 0.0204  0.0302  -0.0129 139 ARG A CA  
2186  C C   . ARG A 139 ? 0.1817 0.1830 0.2517 0.0263  0.0479  -0.0182 139 ARG A C   
2187  O O   . ARG A 139 ? 0.1936 0.1674 0.2341 -0.0170 0.0158  -0.0058 139 ARG A O   
2188  C CB  . ARG A 139 ? 0.1698 0.2089 0.2671 0.0335  0.0205  -0.0200 139 ARG A CB  
2189  C CG  . ARG A 139 ? 0.1999 0.2305 0.2613 0.0367  0.0442  -0.0061 139 ARG A CG  
2190  C CD  . ARG A 139 ? 0.1875 0.1909 0.2680 0.0375  0.0239  0.0013  139 ARG A CD  
2191  N NE  . ARG A 139 ? 0.1955 0.1897 0.2570 0.0222  0.0169  0.0143  139 ARG A NE  
2192  C CZ  . ARG A 139 ? 0.2149 0.1589 0.2477 0.0077  0.0135  0.0232  139 ARG A CZ  
2193  N NH1 . ARG A 139 ? 0.2682 0.2704 0.2583 0.0574  0.0107  0.0050  139 ARG A NH1 
2194  N NH2 . ARG A 139 ? 0.2412 0.1504 0.2442 0.0061  0.0551  0.0195  139 ARG A NH2 
2208  N N   . PRO A 140 ? 0.1749 0.2242 0.2605 0.0200  0.0461  -0.0235 140 PRO A N   
2209  C CA  . PRO A 140 ? 0.1780 0.2561 0.2533 -0.0164 0.0516  -0.0399 140 PRO A CA  
2210  C C   . PRO A 140 ? 0.1792 0.2189 0.2404 -0.0351 0.0632  -0.0178 140 PRO A C   
2211  O O   . PRO A 140 ? 0.2323 0.2207 0.2351 -0.0090 0.0601  0.0099  140 PRO A O   
2212  C CB  . PRO A 140 ? 0.2080 0.3101 0.2702 -0.0588 0.0557  -0.0489 140 PRO A CB  
2213  C CG  . PRO A 140 ? 0.2104 0.2827 0.2736 0.0132  0.0470  -0.0839 140 PRO A CG  
2214  C CD  . PRO A 140 ? 0.2078 0.2737 0.2718 0.0415  0.0521  -0.0553 140 PRO A CD  
2222  N N   . GLN A 141 ? 0.1622 0.1841 0.2211 -0.0241 0.0681  -0.0031 141 GLN A N   
2223  C CA  . GLN A 141 ? 0.1668 0.1190 0.2442 -0.0435 0.0636  -0.0272 141 GLN A CA  
2224  C C   . GLN A 141 ? 0.2006 0.1225 0.2294 -0.0152 0.0548  -0.0005 141 GLN A C   
2225  O O   . GLN A 141 ? 0.2272 0.1603 0.2223 0.0196  0.0378  0.0254  141 GLN A O   
2226  C CB  . GLN A 141 ? 0.2229 0.1780 0.2842 -0.0260 0.0567  -0.0548 141 GLN A CB  
2227  C CG  . GLN A 141 ? 0.2522 0.2246 0.3270 -0.0177 0.0359  -0.0556 141 GLN A CG  
2228  C CD  . GLN A 141 ? 0.2870 0.2514 0.3588 -0.0037 -0.0101 -0.0311 141 GLN A CD  
2229  O OE1 . GLN A 141 ? 0.3320 0.2890 0.3676 0.0119  -0.0228 -0.0270 141 GLN A OE1 
2230  N NE2 . GLN A 141 ? 0.2996 0.2297 0.3750 0.0166  -0.0140 -0.0066 141 GLN A NE2 
2239  N N   . LYS A 142 ? 0.1831 0.1380 0.2325 0.0151  0.0466  -0.0239 142 LYS A N   
2240  C CA  . LYS A 142 ? 0.2115 0.1057 0.2075 0.0452  0.0326  -0.0026 142 LYS A CA  
2241  C C   . LYS A 142 ? 0.1819 0.1435 0.1882 -0.0086 0.0313  0.0098  142 LYS A C   
2242  O O   . LYS A 142 ? 0.1885 0.1422 0.1839 0.0125  0.0333  0.0226  142 LYS A O   
2243  C CB  . LYS A 142 ? 0.2134 0.1160 0.2109 -0.0022 0.0123  0.0095  142 LYS A CB  
2244  C CG  . LYS A 142 ? 0.2087 0.1638 0.2041 0.0417  0.0325  0.0271  142 LYS A CG  
2245  C CD  . LYS A 142 ? 0.2054 0.1730 0.2143 0.0476  0.0183  -0.0010 142 LYS A CD  
2246  C CE  . LYS A 142 ? 0.1736 0.1839 0.2127 0.0374  0.0208  -0.0042 142 LYS A CE  
2247  N NZ  . LYS A 142 ? 0.1497 0.1802 0.2207 0.0129  0.0041  0.0067  142 LYS A NZ  
2261  N N   . LYS A 143 ? 0.1609 0.1559 0.1754 0.0195  0.0062  0.0106  143 LYS A N   
2262  C CA  . LYS A 143 ? 0.1852 0.1749 0.1722 0.0443  0.0082  0.0251  143 LYS A CA  
2263  C C   . LYS A 143 ? 0.1968 0.1991 0.1726 0.0089  0.0307  0.0379  143 LYS A C   
2264  O O   . LYS A 143 ? 0.2131 0.1928 0.1882 0.0329  0.0305  0.0397  143 LYS A O   
2265  C CB  . LYS A 143 ? 0.1845 0.2112 0.1724 0.0018  0.0248  0.0144  143 LYS A CB  
2266  C CG  . LYS A 143 ? 0.1860 0.1573 0.1728 0.0175  0.0232  -0.0104 143 LYS A CG  
2267  C CD  . LYS A 143 ? 0.2517 0.1498 0.1913 0.0237  0.0120  0.0018  143 LYS A CD  
2268  C CE  . LYS A 143 ? 0.2279 0.1115 0.1984 -0.0221 0.0475  -0.0443 143 LYS A CE  
2269  N NZ  . LYS A 143 ? 0.2342 0.1589 0.2133 0.0191  0.0261  -0.0175 143 LYS A NZ  
2283  N N   . LYS A 144 ? 0.1434 0.1694 0.1767 -0.0008 0.0076  0.0128  144 LYS A N   
2284  C CA  . LYS A 144 ? 0.1437 0.1795 0.1631 -0.0165 0.0240  0.0185  144 LYS A CA  
2285  C C   . LYS A 144 ? 0.1671 0.1529 0.1576 0.0232  0.0046  0.0032  144 LYS A C   
2286  O O   . LYS A 144 ? 0.1908 0.1671 0.1681 0.0341  -0.0094 0.0015  144 LYS A O   
2287  C CB  . LYS A 144 ? 0.1632 0.2157 0.1731 0.0391  0.0107  0.0020  144 LYS A CB  
2288  C CG  . LYS A 144 ? 0.1952 0.1739 0.1727 0.0211  0.0200  -0.0107 144 LYS A CG  
2289  C CD  . LYS A 144 ? 0.2169 0.1506 0.1845 0.0060  -0.0115 -0.0123 144 LYS A CD  
2290  C CE  . LYS A 144 ? 0.1768 0.1818 0.1941 -0.0424 -0.0061 -0.0112 144 LYS A CE  
2291  N NZ  . LYS A 144 ? 0.1909 0.2198 0.2183 -0.0502 0.0186  0.0004  144 LYS A NZ  
2305  N N   . VAL A 145 ? 0.1795 0.1312 0.1459 0.0151  0.0154  0.0084  145 VAL A N   
2306  C CA  . VAL A 145 ? 0.1385 0.1697 0.1679 -0.0080 0.0186  0.0029  145 VAL A CA  
2307  C C   . VAL A 145 ? 0.1433 0.1520 0.1641 -0.0019 0.0019  -0.0081 145 VAL A C   
2308  O O   . VAL A 145 ? 0.1636 0.1591 0.1636 -0.0048 -0.0052 0.0021  145 VAL A O   
2309  C CB  . VAL A 145 ? 0.1708 0.1641 0.1760 0.0179  0.0093  0.0089  145 VAL A CB  
2310  C CG1 . VAL A 145 ? 0.1598 0.1212 0.1955 0.0207  -0.0234 0.0351  145 VAL A CG1 
2311  C CG2 . VAL A 145 ? 0.2025 0.1890 0.1852 -0.0207 0.0047  0.0194  145 VAL A CG2 
2321  N N   . ILE A 146 ? 0.1353 0.1363 0.1577 0.0098  0.0091  -0.0003 146 ILE A N   
2322  C CA  . ILE A 146 ? 0.1370 0.0975 0.1626 -0.0145 0.0065  0.0076  146 ILE A CA  
2323  C C   . ILE A 146 ? 0.1358 0.1206 0.1548 -0.0159 -0.0070 0.0029  146 ILE A C   
2324  O O   . ILE A 146 ? 0.1676 0.1310 0.1551 0.0015  -0.0313 -0.0019 146 ILE A O   
2325  C CB  . ILE A 146 ? 0.1126 0.1309 0.1797 -0.0148 0.0201  0.0162  146 ILE A CB  
2326  C CG1 . ILE A 146 ? 0.1810 0.1869 0.1830 -0.0303 0.0164  0.0162  146 ILE A CG1 
2327  C CG2 . ILE A 146 ? 0.1372 0.1441 0.2045 -0.0018 0.0301  0.0176  146 ILE A CG2 
2328  C CD1 . ILE A 146 ? 0.1679 0.1707 0.1776 -0.0148 0.0388  0.0434  146 ILE A CD1 
2340  N N   . ALA A 147 ? 0.1640 0.1473 0.1544 0.0076  0.0080  0.0097  147 ALA A N   
2341  C CA  . ALA A 147 ? 0.1746 0.1155 0.1691 -0.0409 0.0005  0.0112  147 ALA A CA  
2342  C C   . ALA A 147 ? 0.1750 0.0763 0.1700 -0.0150 0.0169  0.0144  147 ALA A C   
2343  O O   . ALA A 147 ? 0.1597 0.1416 0.1575 0.0045  0.0058  0.0063  147 ALA A O   
2344  C CB  . ALA A 147 ? 0.1852 0.1502 0.1765 -0.0441 0.0071  0.0263  147 ALA A CB  
2350  N N   . ARG A 148 ? 0.1379 0.1231 0.1979 -0.0239 0.0365  0.0277  148 ARG A N   
2351  C CA  . ARG A 148 ? 0.1584 0.1608 0.1726 -0.0040 0.0223  0.0420  148 ARG A CA  
2352  C C   . ARG A 148 ? 0.1717 0.1134 0.1712 0.0070  0.0246  0.0199  148 ARG A C   
2353  O O   . ARG A 148 ? 0.1687 0.1354 0.1566 -0.0072 0.0343  0.0112  148 ARG A O   
2354  C CB  . ARG A 148 ? 0.1713 0.1603 0.1702 -0.0188 -0.0093 0.0512  148 ARG A CB  
2355  C CG  . ARG A 148 ? 0.1901 0.1520 0.1745 0.0221  -0.0236 0.0604  148 ARG A CG  
2356  C CD  . ARG A 148 ? 0.2224 0.1963 0.1649 0.0809  -0.0153 0.0332  148 ARG A CD  
2357  N NE  . ARG A 148 ? 0.2048 0.1655 0.1513 0.0074  -0.0307 0.0191  148 ARG A NE  
2358  C CZ  . ARG A 148 ? 0.1746 0.1586 0.1562 -0.0237 -0.0441 0.0157  148 ARG A CZ  
2359  N NH1 . ARG A 148 ? 0.1540 0.1686 0.1541 0.0037  -0.0088 0.0051  148 ARG A NH1 
2360  N NH2 . ARG A 148 ? 0.2150 0.1831 0.1618 -0.0487 -0.0095 0.0625  148 ARG A NH2 
2374  N N   . GLN A 149 ? 0.1658 0.0920 0.1836 -0.0018 0.0020  0.0030  149 GLN A N   
2375  C CA  . GLN A 149 ? 0.1319 0.1647 0.1996 -0.0072 0.0198  0.0281  149 GLN A CA  
2376  C C   . GLN A 149 ? 0.1624 0.0944 0.1735 -0.0088 0.0032  0.0069  149 GLN A C   
2377  O O   . GLN A 149 ? 0.1534 0.1620 0.1647 -0.0023 0.0136  0.0059  149 GLN A O   
2378  C CB  . GLN A 149 ? 0.1612 0.1493 0.2284 -0.0340 -0.0165 0.0694  149 GLN A CB  
2379  C CG  . GLN A 149 ? 0.2507 0.1652 0.2581 -0.0036 0.0146  0.0301  149 GLN A CG  
2380  C CD  . GLN A 149 ? 0.4413 0.2514 0.3205 -0.0193 0.0021  -0.0050 149 GLN A CD  
2381  O OE1 . GLN A 149 ? 0.5442 0.3511 0.3270 -0.0836 -0.0030 -0.0026 149 GLN A OE1 
2382  N NE2 . GLN A 149 ? 0.4861 0.2752 0.3597 -0.0346 0.0240  -0.0150 149 GLN A NE2 
2391  N N   . ARG A 150 ? 0.1736 0.1383 0.1786 0.0088  -0.0020 0.0084  150 ARG A N   
2392  C CA  . ARG A 150 ? 0.1651 0.1319 0.1974 0.0091  -0.0068 -0.0069 150 ARG A CA  
2393  C C   . ARG A 150 ? 0.1536 0.1140 0.1964 0.0176  -0.0190 0.0223  150 ARG A C   
2394  O O   . ARG A 150 ? 0.1472 0.1572 0.2063 0.0075  -0.0200 0.0409  150 ARG A O   
2395  C CB  . ARG A 150 ? 0.1692 0.1462 0.2460 0.0150  0.0073  -0.0151 150 ARG A CB  
2396  C CG  . ARG A 150 ? 0.1741 0.1340 0.2733 -0.0388 0.0273  -0.0170 150 ARG A CG  
2397  C CD  . ARG A 150 ? 0.2371 0.1204 0.2907 -0.0295 -0.0210 -0.0161 150 ARG A CD  
2398  N NE  . ARG A 150 ? 0.2044 0.1392 0.2940 -0.0039 -0.0308 -0.0090 150 ARG A NE  
2399  C CZ  . ARG A 150 ? 0.1860 0.1694 0.3195 0.0086  -0.0647 -0.0436 150 ARG A CZ  
2400  N NH1 . ARG A 150 ? 0.2103 0.2283 0.3417 0.0276  -0.0996 -0.0524 150 ARG A NH1 
2401  N NH2 . ARG A 150 ? 0.2096 0.1637 0.3247 0.0354  -0.0871 -0.0514 150 ARG A NH2 
2415  N N   . GLY A 151 ? 0.1663 0.0976 0.1698 -0.0124 -0.0145 -0.0123 151 GLY A N   
2416  C CA  . GLY A 151 ? 0.1935 0.0810 0.1606 0.0020  -0.0295 -0.0056 151 GLY A CA  
2417  C C   . GLY A 151 ? 0.1665 0.1123 0.1545 0.0136  -0.0279 0.0025  151 GLY A C   
2418  O O   . GLY A 151 ? 0.1637 0.1405 0.1529 -0.0008 -0.0016 0.0154  151 GLY A O   
2422  N N   . TYR A 152 ? 0.1464 0.0988 0.1508 -0.0041 0.0122  -0.0006 152 TYR A N   
2423  C CA  . TYR A 152 ? 0.1054 0.1267 0.1508 -0.0228 0.0097  0.0123  152 TYR A CA  
2424  C C   . TYR A 152 ? 0.1245 0.1625 0.1471 -0.0222 0.0067  -0.0004 152 TYR A C   
2425  O O   . TYR A 152 ? 0.1504 0.1558 0.1615 0.0014  0.0032  0.0125  152 TYR A O   
2426  C CB  . TYR A 152 ? 0.1474 0.1457 0.1608 -0.0280 -0.0157 0.0130  152 TYR A CB  
2427  C CG  . TYR A 152 ? 0.1425 0.1605 0.1594 -0.0187 -0.0156 0.0199  152 TYR A CG  
2428  C CD1 . TYR A 152 ? 0.1640 0.1482 0.1472 -0.0586 -0.0229 0.0375  152 TYR A CD1 
2429  C CD2 . TYR A 152 ? 0.1805 0.1634 0.1671 -0.0421 -0.0047 0.0265  152 TYR A CD2 
2430  C CE1 . TYR A 152 ? 0.2418 0.1124 0.1633 -0.0351 0.0030  0.0218  152 TYR A CE1 
2431  C CE2 . TYR A 152 ? 0.2136 0.1465 0.1709 -0.0324 0.0072  0.0284  152 TYR A CE2 
2432  C CZ  . TYR A 152 ? 0.2096 0.1422 0.1736 -0.0104 -0.0017 0.0255  152 TYR A CZ  
2433  O OH  . TYR A 152 ? 0.2027 0.1658 0.1957 -0.0151 0.0079  0.0184  152 TYR A OH  
2443  N N   . HIS A 153 ? 0.1305 0.1450 0.1437 -0.0309 0.0043  0.0262  153 HIS A N   
2444  C CA  . HIS A 153 ? 0.1446 0.1127 0.1443 -0.0326 -0.0073 0.0167  153 HIS A CA  
2445  C C   . HIS A 153 ? 0.1508 0.1468 0.1465 0.0056  -0.0137 0.0237  153 HIS A C   
2446  O O   . HIS A 153 ? 0.1790 0.1494 0.1504 0.0038  -0.0082 -0.0009 153 HIS A O   
2447  C CB  . HIS A 153 ? 0.1346 0.1486 0.1369 0.0059  0.0037  0.0215  153 HIS A CB  
2448  C CG  . HIS A 153 ? 0.1611 0.1288 0.1277 -0.0076 0.0053  0.0170  153 HIS A CG  
2449  N ND1 . HIS A 153 ? 0.1548 0.1447 0.1305 -0.0240 0.0064  0.0107  153 HIS A ND1 
2450  C CD2 . HIS A 153 ? 0.1695 0.1334 0.1263 -0.0130 0.0086  0.0172  153 HIS A CD2 
2451  C CE1 . HIS A 153 ? 0.1625 0.1736 0.1509 -0.0191 0.0005  0.0101  153 HIS A CE1 
2452  N NE2 . HIS A 153 ? 0.1334 0.1618 0.1387 0.0142  -0.0098 0.0271  153 HIS A NE2 
2460  N N   . GLY A 154 ? 0.1260 0.1542 0.1531 -0.0289 -0.0299 0.0319  154 GLY A N   
2461  C CA  . GLY A 154 ? 0.1627 0.1434 0.1508 -0.0306 -0.0241 0.0256  154 GLY A CA  
2462  C C   . GLY A 154 ? 0.1190 0.1500 0.1559 -0.0379 0.0033  0.0071  154 GLY A C   
2463  O O   . GLY A 154 ? 0.1210 0.1234 0.1713 -0.0197 -0.0155 0.0328  154 GLY A O   
2467  N N   . SER A 155 ? 0.1596 0.1586 0.1366 -0.0033 0.0095  -0.0018 155 SER A N   
2468  C CA  . SER A 155 ? 0.1276 0.1356 0.1259 -0.0281 0.0030  0.0148  155 SER A CA  
2469  C C   . SER A 155 ? 0.1576 0.1532 0.1412 -0.0214 -0.0035 -0.0063 155 SER A C   
2470  O O   . SER A 155 ? 0.1869 0.1268 0.1424 -0.0361 0.0020  -0.0115 155 SER A O   
2471  C CB  . SER A 155 ? 0.1443 0.1325 0.1392 0.0308  -0.0038 0.0187  155 SER A CB  
2472  O OG  . SER A 155 ? 0.1537 0.1637 0.1380 0.0001  0.0042  0.0210  155 SER A OG  
2478  N N   . GLY A 156 ? 0.1766 0.1210 0.1391 0.0059  0.0003  -0.0115 156 GLY A N   
2479  C CA  . GLY A 156 ? 0.1942 0.1140 0.1483 -0.0024 0.0261  -0.0136 156 GLY A CA  
2480  C C   . GLY A 156 ? 0.1609 0.1362 0.1442 -0.0169 -0.0090 -0.0222 156 GLY A C   
2481  O O   . GLY A 156 ? 0.1466 0.1656 0.1569 -0.0299 0.0106  -0.0109 156 GLY A O   
2485  N N   . ILE A 157 ? 0.1811 0.1900 0.1449 -0.0300 0.0085  0.0228  157 ILE A N   
2486  C CA  . ILE A 157 ? 0.1484 0.1657 0.1506 -0.0194 0.0027  0.0035  157 ILE A CA  
2487  C C   . ILE A 157 ? 0.1595 0.1127 0.1556 -0.0299 0.0004  -0.0087 157 ILE A C   
2488  O O   . ILE A 157 ? 0.1586 0.1263 0.1696 -0.0097 -0.0072 -0.0027 157 ILE A O   
2489  C CB  . ILE A 157 ? 0.1608 0.0889 0.1509 -0.0018 0.0044  0.0059  157 ILE A CB  
2490  C CG1 . ILE A 157 ? 0.1248 0.1671 0.1543 0.0024  -0.0025 -0.0076 157 ILE A CG1 
2491  C CG2 . ILE A 157 ? 0.1802 0.0951 0.1654 0.0396  0.0041  0.0068  157 ILE A CG2 
2492  C CD1 . ILE A 157 ? 0.1355 0.1871 0.1518 0.0184  -0.0170 0.0141  157 ILE A CD1 
2504  N N   . ALA A 158 ? 0.1491 0.1328 0.1563 -0.0306 0.0043  -0.0038 158 ALA A N   
2505  C CA  . ALA A 158 ? 0.1236 0.1372 0.1593 -0.0026 -0.0053 0.0197  158 ALA A CA  
2506  C C   . ALA A 158 ? 0.1418 0.1159 0.1540 -0.0046 -0.0128 0.0098  158 ALA A C   
2507  O O   . ALA A 158 ? 0.1672 0.1670 0.1589 -0.0185 -0.0082 0.0260  158 ALA A O   
2508  C CB  . ALA A 158 ? 0.1601 0.1305 0.1605 0.0483  0.0020  0.0086  158 ALA A CB  
2514  N N   . SER A 159 ? 0.1499 0.1447 0.1483 0.0155  -0.0034 0.0263  159 SER A N   
2515  C CA  . SER A 159 ? 0.1227 0.1540 0.1547 0.0072  -0.0026 0.0090  159 SER A CA  
2516  C C   . SER A 159 ? 0.1568 0.1412 0.1555 -0.0033 -0.0057 0.0246  159 SER A C   
2517  O O   . SER A 159 ? 0.1576 0.1453 0.1592 -0.0026 -0.0138 0.0143  159 SER A O   
2518  C CB  . SER A 159 ? 0.1605 0.1730 0.1563 -0.0126 -0.0042 -0.0030 159 SER A CB  
2519  O OG  . SER A 159 ? 0.1974 0.1586 0.1541 -0.0441 -0.0178 0.0128  159 SER A OG  
2525  N N   . GLY A 160 ? 0.1586 0.1458 0.1529 -0.0243 0.0019  0.0213  160 GLY A N   
2526  C CA  . GLY A 160 ? 0.1052 0.1522 0.1519 -0.0143 -0.0015 0.0068  160 GLY A CA  
2527  C C   . GLY A 160 ? 0.1265 0.1339 0.1570 0.0002  -0.0165 -0.0099 160 GLY A C   
2528  O O   . GLY A 160 ? 0.1462 0.1737 0.1644 -0.0308 -0.0034 -0.0051 160 GLY A O   
2532  N N   . SER A 161 ? 0.1205 0.1379 0.1464 0.0124  -0.0153 -0.0027 161 SER A N   
2533  C CA  . SER A 161 ? 0.1725 0.1234 0.1353 -0.0085 0.0203  -0.0278 161 SER A CA  
2534  C C   . SER A 161 ? 0.1593 0.1371 0.1335 -0.0174 0.0090  -0.0117 161 SER A C   
2535  O O   . SER A 161 ? 0.1637 0.1159 0.1486 -0.0352 -0.0083 0.0063  161 SER A O   
2536  C CB  . SER A 161 ? 0.1783 0.1203 0.1451 -0.0123 0.0184  -0.0120 161 SER A CB  
2537  O OG  . SER A 161 ? 0.1657 0.1281 0.1565 -0.0299 0.0348  -0.0001 161 SER A OG  
2543  N N   . LEU A 162 ? 0.1644 0.1502 0.1415 -0.0107 -0.0138 -0.0290 162 LEU A N   
2544  C CA  . LEU A 162 ? 0.1553 0.1661 0.1340 -0.0089 -0.0226 -0.0193 162 LEU A CA  
2545  C C   . LEU A 162 ? 0.1578 0.1302 0.1441 -0.0164 -0.0148 0.0122  162 LEU A C   
2546  O O   . LEU A 162 ? 0.1509 0.1173 0.1634 0.0087  0.0100  0.0344  162 LEU A O   
2547  C CB  . LEU A 162 ? 0.1647 0.1631 0.1356 0.0028  0.0077  -0.0141 162 LEU A CB  
2548  C CG  . LEU A 162 ? 0.1460 0.1422 0.1383 0.0011  0.0106  0.0030  162 LEU A CG  
2549  C CD1 . LEU A 162 ? 0.1833 0.1624 0.1451 -0.0088 -0.0175 -0.0049 162 LEU A CD1 
2550  C CD2 . LEU A 162 ? 0.1558 0.1859 0.1466 0.0085  -0.0069 0.0232  162 LEU A CD2 
2562  N N   . THR A 163 ? 0.1239 0.1224 0.1489 -0.0203 0.0142  0.0264  163 THR A N   
2563  C CA  . THR A 163 ? 0.1438 0.1305 0.1503 -0.0077 -0.0264 0.0077  163 THR A CA  
2564  C C   . THR A 163 ? 0.1479 0.1251 0.1541 0.0099  -0.0165 0.0025  163 THR A C   
2565  O O   . THR A 163 ? 0.1790 0.1139 0.1610 0.0010  0.0205  -0.0015 163 THR A O   
2566  C CB  . THR A 163 ? 0.1709 0.1325 0.1518 -0.0080 -0.0173 0.0121  163 THR A CB  
2567  O OG1 . THR A 163 ? 0.2009 0.1380 0.1454 -0.0142 -0.0107 0.0168  163 THR A OG1 
2568  C CG2 . THR A 163 ? 0.1641 0.1839 0.1460 0.0091  -0.0201 0.0002  163 THR A CG2 
2576  N N   . GLY A 164 ? 0.1672 0.1441 0.1597 -0.0039 0.0060  -0.0156 164 GLY A N   
2577  C CA  . GLY A 164 ? 0.1538 0.1297 0.1547 -0.0098 0.0102  -0.0219 164 GLY A CA  
2578  C C   . GLY A 164 ? 0.1630 0.1973 0.1627 -0.0270 0.0188  -0.0065 164 GLY A C   
2579  O O   . GLY A 164 ? 0.1663 0.1964 0.1862 -0.0130 0.0187  0.0299  164 GLY A O   
2583  N N   . LEU A 165 ? 0.1336 0.2205 0.1755 -0.0382 0.0151  0.0026  165 LEU A N   
2584  C CA  . LEU A 165 ? 0.1552 0.2125 0.1775 -0.0351 -0.0053 0.0129  165 LEU A CA  
2585  C C   . LEU A 165 ? 0.1288 0.1622 0.1713 -0.0136 0.0123  0.0142  165 LEU A C   
2586  O O   . LEU A 165 ? 0.1329 0.1836 0.1700 -0.0066 -0.0012 0.0166  165 LEU A O   
2587  C CB  . LEU A 165 ? 0.1500 0.1932 0.1787 0.0111  -0.0037 0.0101  165 LEU A CB  
2588  C CG  . LEU A 165 ? 0.1343 0.1890 0.1851 -0.0174 -0.0101 -0.0098 165 LEU A CG  
2589  C CD1 . LEU A 165 ? 0.1655 0.2110 0.1952 -0.0420 0.0195  -0.0049 165 LEU A CD1 
2590  C CD2 . LEU A 165 ? 0.1420 0.1682 0.1900 0.0321  -0.0024 -0.0001 165 LEU A CD2 
2602  N N   . LYS A 166 ? 0.1591 0.1626 0.1848 -0.0414 0.0016  -0.0004 166 LYS A N   
2603  C CA  . LYS A 166 ? 0.1903 0.1872 0.1876 -0.0418 -0.0028 -0.0074 166 LYS A CA  
2604  C C   . LYS A 166 ? 0.1746 0.1941 0.1769 -0.0305 0.0032  0.0010  166 LYS A C   
2605  O O   . LYS A 166 ? 0.2069 0.2118 0.1675 -0.0550 0.0049  0.0102  166 LYS A O   
2606  C CB  . LYS A 166 ? 0.2993 0.2154 0.2312 -0.1331 -0.0098 -0.0102 166 LYS A CB  
2607  C CG  . LYS A 166 ? 0.3923 0.3328 0.2875 -0.1592 -0.0613 -0.0155 166 LYS A CG  
2608  C CD  . LYS A 166 ? 0.5043 0.4646 0.3519 -0.2050 -0.0804 -0.0229 166 LYS A CD  
2609  C CE  . LYS A 166 ? 0.6240 0.5870 0.4083 -0.1841 -0.0713 -0.0099 166 LYS A CE  
2610  N NZ  . LYS A 166 ? 0.6951 0.6529 0.4397 -0.1772 -0.0601 -0.0026 166 LYS A NZ  
2624  N N   . ALA A 167 ? 0.1636 0.1635 0.1711 -0.0046 -0.0107 0.0275  167 ALA A N   
2625  C CA  . ALA A 167 ? 0.1668 0.1823 0.1799 -0.0260 0.0075  0.0247  167 ALA A CA  
2626  C C   . ALA A 167 ? 0.1757 0.2068 0.1703 -0.0165 -0.0157 0.0168  167 ALA A C   
2627  O O   . ALA A 167 ? 0.1923 0.2060 0.1734 -0.0143 -0.0433 0.0238  167 ALA A O   
2628  C CB  . ALA A 167 ? 0.1975 0.2275 0.2033 0.0330  0.0139  0.0265  167 ALA A CB  
2634  N N   . PHE A 168 ? 0.1602 0.1598 0.1471 -0.0053 -0.0099 0.0204  168 PHE A N   
2635  C CA  . PHE A 168 ? 0.1367 0.1354 0.1517 0.0050  -0.0244 0.0424  168 PHE A CA  
2636  C C   . PHE A 168 ? 0.1497 0.1634 0.1610 -0.0106 -0.0206 -0.0020 168 PHE A C   
2637  O O   . PHE A 168 ? 0.1689 0.2228 0.1716 -0.0413 -0.0166 0.0045  168 PHE A O   
2638  C CB  . PHE A 168 ? 0.1591 0.1668 0.1568 -0.0264 -0.0273 0.0556  168 PHE A CB  
2639  C CG  . PHE A 168 ? 0.1585 0.1624 0.1641 -0.0472 -0.0164 0.0265  168 PHE A CG  
2640  C CD1 . PHE A 168 ? 0.1619 0.1748 0.1719 -0.0138 -0.0121 0.0308  168 PHE A CD1 
2641  C CD2 . PHE A 168 ? 0.1764 0.1921 0.1569 -0.0662 0.0196  0.0227  168 PHE A CD2 
2642  C CE1 . PHE A 168 ? 0.1761 0.1905 0.1882 -0.0577 0.0134  0.0036  168 PHE A CE1 
2643  C CE2 . PHE A 168 ? 0.2102 0.2395 0.1663 -0.0831 0.0084  -0.0004 168 PHE A CE2 
2644  C CZ  . PHE A 168 ? 0.2058 0.2390 0.1873 -0.0714 0.0271  0.0038  168 PHE A CZ  
2654  N N   . HIS A 169 ? 0.1301 0.1658 0.1538 -0.0272 -0.0079 0.0006  169 HIS A N   
2655  C CA  . HIS A 169 ? 0.1668 0.1337 0.1635 -0.0307 0.0062  0.0066  169 HIS A CA  
2656  C C   . HIS A 169 ? 0.1647 0.1677 0.1717 -0.0173 -0.0060 0.0162  169 HIS A C   
2657  O O   . HIS A 169 ? 0.1756 0.1961 0.1778 -0.0227 -0.0127 0.0099  169 HIS A O   
2658  C CB  . HIS A 169 ? 0.1891 0.1244 0.1614 -0.0133 -0.0157 -0.0044 169 HIS A CB  
2659  C CG  . HIS A 169 ? 0.1544 0.1538 0.1460 -0.0298 0.0069  0.0169  169 HIS A CG  
2660  N ND1 . HIS A 169 ? 0.1985 0.1834 0.1669 -0.0311 0.0061  0.0258  169 HIS A ND1 
2661  C CD2 . HIS A 169 ? 0.1610 0.1463 0.1354 -0.0272 0.0162  -0.0050 169 HIS A CD2 
2662  C CE1 . HIS A 169 ? 0.2361 0.1535 0.1594 -0.0500 -0.0077 0.0114  169 HIS A CE1 
2663  N NE2 . HIS A 169 ? 0.1887 0.1678 0.1505 -0.0436 0.0016  0.0137  169 HIS A NE2 
2671  N N   . ASP A 170 ? 0.1463 0.1928 0.1789 -0.0111 -0.0107 0.0127  170 ASP A N   
2672  C CA  . ASP A 170 ? 0.1612 0.2487 0.1879 -0.0024 -0.0335 0.0160  170 ASP A CA  
2673  C C   . ASP A 170 ? 0.1496 0.2122 0.1928 -0.0194 -0.0341 0.0115  170 ASP A C   
2674  O O   . ASP A 170 ? 0.1647 0.2279 0.2088 -0.0263 -0.0085 0.0184  170 ASP A O   
2675  C CB  . ASP A 170 ? 0.1730 0.2947 0.1975 -0.0801 -0.0113 0.0079  170 ASP A CB  
2676  C CG  . ASP A 170 ? 0.2150 0.3356 0.2325 -0.1099 -0.0176 0.0233  170 ASP A CG  
2677  O OD1 . ASP A 170 ? 0.2472 0.3464 0.2453 -0.0945 -0.0066 0.0508  170 ASP A OD1 
2678  O OD2 . ASP A 170 ? 0.2696 0.3906 0.2430 -0.0723 0.0037  0.0233  170 ASP A OD2 
2683  N N   . HIS A 171 ? 0.1984 0.1737 0.1678 -0.0183 -0.0301 -0.0071 171 HIS A N   
2684  C CA  . HIS A 171 ? 0.2024 0.1736 0.1661 -0.0056 -0.0317 0.0172  171 HIS A CA  
2685  C C   . HIS A 171 ? 0.1899 0.1641 0.1605 -0.0150 -0.0081 0.0190  171 HIS A C   
2686  O O   . HIS A 171 ? 0.2002 0.1753 0.1615 -0.0279 -0.0103 0.0272  171 HIS A O   
2687  C CB  . HIS A 171 ? 0.1945 0.1813 0.1910 0.0026  0.0040  0.0063  171 HIS A CB  
2688  C CG  . HIS A 171 ? 0.1999 0.2262 0.2042 -0.0163 -0.0326 0.0001  171 HIS A CG  
2689  N ND1 . HIS A 171 ? 0.2455 0.2525 0.2243 -0.0137 -0.0110 -0.0010 171 HIS A ND1 
2690  C CD2 . HIS A 171 ? 0.2651 0.2455 0.2109 -0.0215 -0.0196 -0.0024 171 HIS A CD2 
2691  C CE1 . HIS A 171 ? 0.2662 0.3012 0.2301 -0.0186 -0.0237 -0.0098 171 HIS A CE1 
2692  N NE2 . HIS A 171 ? 0.2548 0.3111 0.2188 -0.0145 -0.0189 -0.0052 171 HIS A NE2 
2700  N N   . PHE A 172 ? 0.1741 0.1696 0.1547 -0.0470 -0.0146 0.0285  172 PHE A N   
2701  C CA  . PHE A 172 ? 0.1896 0.1898 0.1651 -0.0506 -0.0079 0.0014  172 PHE A CA  
2702  C C   . PHE A 172 ? 0.2121 0.1610 0.1715 -0.0278 0.0100  -0.0108 172 PHE A C   
2703  O O   . PHE A 172 ? 0.1654 0.1534 0.1766 -0.0004 0.0079  -0.0170 172 PHE A O   
2704  C CB  . PHE A 172 ? 0.1841 0.1725 0.1738 -0.0214 -0.0271 0.0032  172 PHE A CB  
2705  C CG  . PHE A 172 ? 0.1627 0.1043 0.1755 -0.0396 -0.0038 0.0027  172 PHE A CG  
2706  C CD1 . PHE A 172 ? 0.1798 0.1053 0.1784 -0.0571 -0.0055 0.0082  172 PHE A CD1 
2707  C CD2 . PHE A 172 ? 0.1998 0.1114 0.1872 -0.0439 -0.0020 -0.0035 172 PHE A CD2 
2708  C CE1 . PHE A 172 ? 0.2036 0.0855 0.1798 -0.0142 -0.0065 0.0099  172 PHE A CE1 
2709  C CE2 . PHE A 172 ? 0.2068 0.1233 0.1873 0.0094  -0.0168 0.0165  172 PHE A CE2 
2710  C CZ  . PHE A 172 ? 0.1794 0.1094 0.1842 -0.0142 -0.0322 0.0235  172 PHE A CZ  
2720  N N   . ASP A 173 ? 0.2196 0.1189 0.1708 -0.0406 0.0092  0.0107  173 ASP A N   
2721  C CA  . ASP A 173 ? 0.2138 0.1356 0.1744 -0.0313 0.0001  -0.0109 173 ASP A CA  
2722  C C   . ASP A 173 ? 0.2141 0.1688 0.1834 -0.0029 -0.0238 -0.0259 173 ASP A C   
2723  O O   . ASP A 173 ? 0.2587 0.2490 0.1999 0.0606  -0.0373 -0.0389 173 ASP A O   
2724  C CB  . ASP A 173 ? 0.2222 0.1284 0.1689 0.0095  -0.0017 -0.0040 173 ASP A CB  
2725  C CG  . ASP A 173 ? 0.2266 0.1866 0.1770 -0.0177 0.0107  -0.0027 173 ASP A CG  
2726  O OD1 . ASP A 173 ? 0.2409 0.1897 0.1733 -0.0299 0.0014  0.0097  173 ASP A OD1 
2727  O OD2 . ASP A 173 ? 0.2326 0.2924 0.1830 -0.0350 0.0057  -0.0089 173 ASP A OD2 
2732  N N   . LEU A 174 ? 0.1711 0.1675 0.1601 -0.0175 -0.0323 -0.0228 174 LEU A N   
2733  C CA  . LEU A 174 ? 0.1686 0.1504 0.1605 -0.0360 -0.0078 -0.0142 174 LEU A CA  
2734  C C   . LEU A 174 ? 0.1494 0.1654 0.1620 -0.0376 0.0178  -0.0051 174 LEU A C   
2735  O O   . LEU A 174 ? 0.1719 0.2049 0.1893 -0.0210 0.0155  -0.0115 174 LEU A O   
2736  C CB  . LEU A 174 ? 0.1504 0.1530 0.1685 -0.0647 -0.0159 0.0147  174 LEU A CB  
2737  C CG  . LEU A 174 ? 0.1549 0.1917 0.1705 -0.0191 -0.0140 -0.0137 174 LEU A CG  
2738  C CD1 . LEU A 174 ? 0.1572 0.2086 0.1777 -0.0393 -0.0070 -0.0272 174 LEU A CD1 
2739  C CD2 . LEU A 174 ? 0.2108 0.2080 0.1556 0.0014  0.0154  0.0150  174 LEU A CD2 
2751  N N   . PRO A 175 ? 0.1722 0.1710 0.1566 -0.0220 0.0050  -0.0022 175 PRO A N   
2752  C CA  . PRO A 175 ? 0.1542 0.1725 0.1493 -0.0187 0.0163  0.0024  175 PRO A CA  
2753  C C   . PRO A 175 ? 0.1673 0.1754 0.1592 -0.0350 0.0058  -0.0084 175 PRO A C   
2754  O O   . PRO A 175 ? 0.2199 0.2068 0.1498 -0.0373 -0.0146 -0.0014 175 PRO A O   
2755  C CB  . PRO A 175 ? 0.2351 0.1508 0.1574 -0.0644 0.0205  0.0244  175 PRO A CB  
2756  C CG  . PRO A 175 ? 0.2451 0.1535 0.1567 -0.0618 0.0090  0.0130  175 PRO A CG  
2757  C CD  . PRO A 175 ? 0.1954 0.1856 0.1608 -0.0718 -0.0130 0.0245  175 PRO A CD  
2765  N N   . ILE A 176 ? 0.1571 0.1845 0.1753 -0.0334 0.0028  0.0159  176 ILE A N   
2766  C CA  . ILE A 176 ? 0.1834 0.1568 0.1826 -0.0055 0.0038  0.0174  176 ILE A CA  
2767  C C   . ILE A 176 ? 0.1809 0.1779 0.1686 -0.0055 0.0089  0.0205  176 ILE A C   
2768  O O   . ILE A 176 ? 0.1918 0.1370 0.1671 -0.0208 0.0291  -0.0064 176 ILE A O   
2769  C CB  . ILE A 176 ? 0.1824 0.1106 0.1950 0.0369  -0.0007 -0.0060 176 ILE A CB  
2770  C CG1 . ILE A 176 ? 0.1991 0.1267 0.2102 -0.0131 -0.0032 -0.0018 176 ILE A CG1 
2771  C CG2 . ILE A 176 ? 0.2218 0.1513 0.2086 0.0445  0.0028  0.0223  176 ILE A CG2 
2772  C CD1 . ILE A 176 ? 0.2264 0.1555 0.2222 0.0242  0.0217  0.0039  176 ILE A CD1 
2784  N N   . GLU A 177 ? 0.2028 0.1742 0.1860 -0.0120 0.0377  0.0180  177 GLU A N   
2785  C CA  . GLU A 177 ? 0.2126 0.2000 0.2212 0.0643  0.0460  0.0567  177 GLU A CA  
2786  C C   . GLU A 177 ? 0.1995 0.1592 0.2104 0.0157  0.0626  0.0157  177 GLU A C   
2787  O O   . GLU A 177 ? 0.1940 0.1876 0.2378 0.0259  0.0258  0.0139  177 GLU A O   
2788  C CB  . GLU A 177 ? 0.3611 0.2860 0.2882 0.1380  0.0856  0.0921  177 GLU A CB  
2789  C CG  . GLU A 177 ? 0.6161 0.4850 0.3515 0.1845  0.0944  0.0478  177 GLU A CG  
2790  C CD  . GLU A 177 ? 0.8426 0.6104 0.4074 0.2164  0.0911  0.0279  177 GLU A CD  
2791  O OE1 . GLU A 177 ? 0.9243 0.6663 0.4276 0.2065  0.1096  0.0029  177 GLU A OE1 
2792  O OE2 . GLU A 177 ? 0.9289 0.6596 0.4397 0.2224  0.0698  0.0293  177 GLU A OE2 
2799  N N   . GLY A 178 ? 0.2246 0.1573 0.1980 0.0083  0.0481  0.0294  178 GLY A N   
2800  C CA  . GLY A 178 ? 0.2188 0.1717 0.1968 0.0104  0.0410  -0.0027 178 GLY A CA  
2801  C C   . GLY A 178 ? 0.1811 0.1785 0.1911 -0.0113 0.0150  -0.0299 178 GLY A C   
2802  O O   . GLY A 178 ? 0.2103 0.1859 0.1939 0.0610  -0.0137 -0.0406 178 GLY A O   
2806  N N   . ILE A 179 ? 0.1861 0.1781 0.1825 -0.0130 -0.0108 -0.0399 179 ILE A N   
2807  C CA  . ILE A 179 ? 0.1932 0.1650 0.1802 0.0163  0.0044  -0.0217 179 ILE A CA  
2808  C C   . ILE A 179 ? 0.1894 0.1605 0.1609 0.0112  0.0174  -0.0299 179 ILE A C   
2809  O O   . ILE A 179 ? 0.2253 0.1897 0.1701 -0.0085 0.0225  -0.0320 179 ILE A O   
2810  C CB  . ILE A 179 ? 0.1806 0.1302 0.1896 0.0458  0.0144  -0.0125 179 ILE A CB  
2811  C CG1 . ILE A 179 ? 0.2454 0.1342 0.1921 0.0099  0.0298  0.0188  179 ILE A CG1 
2812  C CG2 . ILE A 179 ? 0.1872 0.2111 0.1910 0.0601  -0.0058 -0.0128 179 ILE A CG2 
2813  C CD1 . ILE A 179 ? 0.2334 0.1814 0.2056 -0.0203 0.0224  0.0185  179 ILE A CD1 
2825  N N   . LEU A 180 ? 0.1791 0.1674 0.1523 0.0023  -0.0059 -0.0137 180 LEU A N   
2826  C CA  . LEU A 180 ? 0.1510 0.1466 0.1620 -0.0417 -0.0023 0.0000  180 LEU A CA  
2827  C C   . LEU A 180 ? 0.1458 0.1879 0.1629 -0.0305 0.0198  -0.0124 180 LEU A C   
2828  O O   . LEU A 180 ? 0.1381 0.1817 0.1812 -0.0196 0.0140  -0.0118 180 LEU A O   
2829  C CB  . LEU A 180 ? 0.2076 0.1496 0.1996 -0.0076 0.0261  0.0236  180 LEU A CB  
2830  C CG  . LEU A 180 ? 0.3393 0.1814 0.2473 0.0230  0.0166  0.0106  180 LEU A CG  
2831  C CD1 . LEU A 180 ? 0.3609 0.2420 0.2781 0.0142  0.0224  0.0021  180 LEU A CD1 
2832  C CD2 . LEU A 180 ? 0.3896 0.2861 0.2814 0.0384  0.0291  -0.0086 180 LEU A CD2 
2844  N N   . HIS A 181 ? 0.1702 0.1827 0.1613 -0.0543 0.0233  0.0172  181 HIS A N   
2845  C CA  . HIS A 181 ? 0.1417 0.1568 0.1518 -0.0309 -0.0063 0.0390  181 HIS A CA  
2846  C C   . HIS A 181 ? 0.1544 0.1723 0.1664 -0.0081 -0.0073 0.0194  181 HIS A C   
2847  O O   . HIS A 181 ? 0.1906 0.1864 0.1790 -0.0271 0.0081  -0.0038 181 HIS A O   
2848  C CB  . HIS A 181 ? 0.1458 0.1166 0.1477 0.0130  0.0154  0.0189  181 HIS A CB  
2849  C CG  . HIS A 181 ? 0.1578 0.1293 0.1557 -0.0506 0.0147  0.0188  181 HIS A CG  
2850  N ND1 . HIS A 181 ? 0.1973 0.1990 0.1514 -0.0322 0.0394  0.0386  181 HIS A ND1 
2851  C CD2 . HIS A 181 ? 0.1835 0.1386 0.1574 -0.0302 -0.0004 0.0186  181 HIS A CD2 
2852  C CE1 . HIS A 181 ? 0.1944 0.1758 0.1559 -0.0340 0.0163  0.0141  181 HIS A CE1 
2853  N NE2 . HIS A 181 ? 0.1551 0.1617 0.1681 0.0020  0.0041  0.0061  181 HIS A NE2 
2861  N N   . THR A 182 ? 0.1842 0.1536 0.1707 -0.0083 0.0138  0.0254  182 THR A N   
2862  C CA  . THR A 182 ? 0.1624 0.1384 0.1679 -0.0280 0.0244  0.0498  182 THR A CA  
2863  C C   . THR A 182 ? 0.1841 0.1057 0.1752 -0.0208 0.0149  0.0356  182 THR A C   
2864  O O   . THR A 182 ? 0.1766 0.1389 0.1840 0.0034  0.0264  0.0477  182 THR A O   
2865  C CB  . THR A 182 ? 0.1636 0.1109 0.1736 -0.0003 0.0298  0.0641  182 THR A CB  
2866  O OG1 . THR A 182 ? 0.2074 0.1556 0.1697 0.0278  0.0537  0.0423  182 THR A OG1 
2867  C CG2 . THR A 182 ? 0.1895 0.1149 0.1839 -0.0096 0.0179  0.0525  182 THR A CG2 
2875  N N   . GLU A 183 ? 0.1642 0.1500 0.1827 0.0049  0.0232  0.0281  183 GLU A N   
2876  C CA  . GLU A 183 ? 0.1791 0.1695 0.2064 -0.0164 0.0049  0.0271  183 GLU A CA  
2877  C C   . GLU A 183 ? 0.1374 0.1704 0.2071 0.0115  0.0061  0.0396  183 GLU A C   
2878  O O   . GLU A 183 ? 0.1558 0.1973 0.2139 0.0286  0.0199  0.0218  183 GLU A O   
2879  C CB  . GLU A 183 ? 0.1885 0.1668 0.2435 -0.0174 0.0247  0.0592  183 GLU A CB  
2880  C CG  . GLU A 183 ? 0.1985 0.1907 0.3025 -0.0515 0.0303  0.0430  183 GLU A CG  
2881  C CD  . GLU A 183 ? 0.3561 0.2694 0.3760 -0.0906 -0.0004 0.0194  183 GLU A CD  
2882  O OE1 . GLU A 183 ? 0.3249 0.3304 0.4181 -0.0849 -0.0629 0.0104  183 GLU A OE1 
2883  O OE2 . GLU A 183 ? 0.5298 0.3362 0.4088 -0.1193 -0.0290 -0.0010 183 GLU A OE2 
2890  N N   . ALA A 184 ? 0.1330 0.1185 0.1879 0.0055  -0.0017 0.0392  184 ALA A N   
2891  C CA  . ALA A 184 ? 0.1263 0.1405 0.1887 0.0367  0.0247  0.0406  184 ALA A CA  
2892  C C   . ALA A 184 ? 0.1456 0.1352 0.1880 0.0238  0.0438  0.0292  184 ALA A C   
2893  O O   . ALA A 184 ? 0.1800 0.1587 0.1969 0.0066  0.0586  0.0126  184 ALA A O   
2894  C CB  . ALA A 184 ? 0.1557 0.1930 0.2016 0.0286  0.0075  0.0160  184 ALA A CB  
2900  N N   . PRO A 185 ? 0.1522 0.1585 0.1874 -0.0027 0.0399  0.0223  185 PRO A N   
2901  C CA  . PRO A 185 ? 0.1236 0.1631 0.1968 -0.0041 0.0427  0.0255  185 PRO A CA  
2902  C C   . PRO A 185 ? 0.1825 0.1646 0.2036 0.0062  0.0321  0.0133  185 PRO A C   
2903  O O   . PRO A 185 ? 0.1645 0.1861 0.2012 -0.0001 -0.0001 0.0022  185 PRO A O   
2904  C CB  . PRO A 185 ? 0.1464 0.2007 0.2046 0.0100  0.0304  0.0299  185 PRO A CB  
2905  C CG  . PRO A 185 ? 0.1688 0.1420 0.1973 0.0108  0.0427  -0.0088 185 PRO A CG  
2906  C CD  . PRO A 185 ? 0.1398 0.1388 0.1962 0.0162  0.0259  0.0098  185 PRO A CD  
2914  N N   . TYR A 186 ? 0.1401 0.1551 0.2092 -0.0247 0.0388  0.0193  186 TYR A N   
2915  C CA  . TYR A 186 ? 0.1448 0.1420 0.2036 0.0095  0.0023  0.0075  186 TYR A CA  
2916  C C   . TYR A 186 ? 0.1300 0.1531 0.2021 -0.0021 -0.0135 -0.0088 186 TYR A C   
2917  O O   . TYR A 186 ? 0.1667 0.1765 0.1954 0.0088  -0.0154 0.0204  186 TYR A O   
2918  C CB  . TYR A 186 ? 0.1614 0.1470 0.2014 0.0326  0.0280  -0.0017 186 TYR A CB  
2919  C CG  . TYR A 186 ? 0.1823 0.1681 0.2006 0.0167  -0.0010 -0.0039 186 TYR A CG  
2920  C CD1 . TYR A 186 ? 0.1719 0.1865 0.2158 0.0551  0.0055  0.0170  186 TYR A CD1 
2921  C CD2 . TYR A 186 ? 0.1927 0.1555 0.1897 0.0332  -0.0034 -0.0099 186 TYR A CD2 
2922  C CE1 . TYR A 186 ? 0.1749 0.1560 0.2228 0.0306  -0.0019 0.0087  186 TYR A CE1 
2923  C CE2 . TYR A 186 ? 0.2332 0.1288 0.1961 0.0742  -0.0028 -0.0119 186 TYR A CE2 
2924  C CZ  . TYR A 186 ? 0.2176 0.1381 0.2098 0.0418  -0.0193 -0.0007 186 TYR A CZ  
2925  O OH  . TYR A 186 ? 0.2348 0.1948 0.2161 0.0322  -0.0337 -0.0010 186 TYR A OH  
2935  N N   . TYR A 187 ? 0.1393 0.1780 0.2027 -0.0211 0.0079  0.0193  187 TYR A N   
2936  C CA  . TYR A 187 ? 0.1538 0.2250 0.2059 -0.0485 0.0201  0.0257  187 TYR A CA  
2937  C C   . TYR A 187 ? 0.1452 0.1967 0.2130 -0.0218 0.0169  0.0077  187 TYR A C   
2938  O O   . TYR A 187 ? 0.1745 0.1945 0.1949 -0.0202 0.0242  -0.0007 187 TYR A O   
2939  C CB  . TYR A 187 ? 0.1526 0.1995 0.2054 -0.0417 -0.0034 0.0219  187 TYR A CB  
2940  C CG  . TYR A 187 ? 0.1456 0.2057 0.2011 -0.0176 0.0322  0.0143  187 TYR A CG  
2941  C CD1 . TYR A 187 ? 0.1900 0.2245 0.2054 0.0219  0.0283  0.0109  187 TYR A CD1 
2942  C CD2 . TYR A 187 ? 0.1757 0.1725 0.2101 -0.0401 0.0187  -0.0006 187 TYR A CD2 
2943  C CE1 . TYR A 187 ? 0.1727 0.2444 0.2135 -0.0260 0.0360  -0.0017 187 TYR A CE1 
2944  C CE2 . TYR A 187 ? 0.1995 0.1928 0.2058 -0.0578 0.0314  0.0034  187 TYR A CE2 
2945  C CZ  . TYR A 187 ? 0.1604 0.2236 0.2136 -0.0297 0.0379  0.0037  187 TYR A CZ  
2946  O OH  . TYR A 187 ? 0.1882 0.3005 0.2257 -0.0363 0.0490  -0.0007 187 TYR A OH  
2956  N N   . TYR A 188 ? 0.1512 0.1472 0.2156 -0.0110 0.0280  0.0092  188 TYR A N   
2957  C CA  . TYR A 188 ? 0.1313 0.1620 0.2253 0.0072  0.0027  -0.0084 188 TYR A CA  
2958  C C   . TYR A 188 ? 0.1415 0.1093 0.2385 0.0325  -0.0089 -0.0130 188 TYR A C   
2959  O O   . TYR A 188 ? 0.1655 0.1633 0.2464 -0.0242 -0.0012 -0.0171 188 TYR A O   
2960  C CB  . TYR A 188 ? 0.1542 0.1757 0.2450 0.0180  -0.0153 0.0035  188 TYR A CB  
2961  C CG  . TYR A 188 ? 0.1919 0.1857 0.2885 -0.0089 0.0021  -0.0010 188 TYR A CG  
2962  C CD1 . TYR A 188 ? 0.1773 0.1853 0.3106 -0.0288 0.0016  0.0068  188 TYR A CD1 
2963  C CD2 . TYR A 188 ? 0.1769 0.1704 0.2995 0.0068  -0.0200 0.0350  188 TYR A CD2 
2964  C CE1 . TYR A 188 ? 0.2039 0.1793 0.3269 0.0152  -0.0399 0.0052  188 TYR A CE1 
2965  C CE2 . TYR A 188 ? 0.1768 0.1762 0.3173 -0.0540 -0.0396 0.0428  188 TYR A CE2 
2966  C CZ  . TYR A 188 ? 0.1914 0.1797 0.3392 0.0321  -0.0597 0.0199  188 TYR A CZ  
2967  O OH  . TYR A 188 ? 0.2165 0.1863 0.3752 -0.0121 -0.0772 0.0088  188 TYR A OH  
2977  N N   . HIS A 189 ? 0.1587 0.1641 0.2266 0.0404  0.0157  -0.0127 189 HIS A N   
2978  C CA  . HIS A 189 ? 0.1715 0.1447 0.2319 0.0398  0.0076  -0.0316 189 HIS A CA  
2979  C C   . HIS A 189 ? 0.2014 0.1870 0.2431 0.0467  0.0142  -0.0157 189 HIS A C   
2980  O O   . HIS A 189 ? 0.3072 0.2414 0.2381 0.0571  0.0127  -0.0285 189 HIS A O   
2981  C CB  . HIS A 189 ? 0.1530 0.1708 0.2217 0.0217  0.0129  -0.0166 189 HIS A CB  
2982  C CG  . HIS A 189 ? 0.2129 0.1772 0.2097 -0.0036 0.0186  -0.0025 189 HIS A CG  
2983  N ND1 . HIS A 189 ? 0.2437 0.1991 0.2225 -0.0094 0.0383  -0.0207 189 HIS A ND1 
2984  C CD2 . HIS A 189 ? 0.1720 0.1926 0.1935 -0.0134 0.0245  -0.0265 189 HIS A CD2 
2985  C CE1 . HIS A 189 ? 0.2355 0.2480 0.2274 0.0467  0.0350  -0.0015 189 HIS A CE1 
2986  N NE2 . HIS A 189 ? 0.1744 0.2246 0.2038 0.0121  0.0036  -0.0213 189 HIS A NE2 
2994  N N   . ARG A 190 ? 0.2125 0.1437 0.2522 0.0134  -0.0052 -0.0111 190 ARG A N   
2995  C CA  . ARG A 190 ? 0.2778 0.1211 0.2721 -0.0194 -0.0239 0.0078  190 ARG A CA  
2996  C C   . ARG A 190 ? 0.3447 0.1606 0.2777 -0.0160 -0.0553 0.0045  190 ARG A C   
2997  O O   . ARG A 190 ? 0.3571 0.1828 0.2614 -0.0159 -0.0365 -0.0174 190 ARG A O   
2998  C CB  . ARG A 190 ? 0.2625 0.1859 0.2741 0.0104  -0.0360 -0.0076 190 ARG A CB  
2999  C CG  . ARG A 190 ? 0.2299 0.2114 0.2745 -0.0066 -0.0485 -0.0135 190 ARG A CG  
3000  C CD  . ARG A 190 ? 0.2204 0.2232 0.2728 -0.0371 -0.0305 0.0034  190 ARG A CD  
3001  N NE  . ARG A 190 ? 0.2286 0.2415 0.2749 -0.0431 -0.0106 0.0147  190 ARG A NE  
3002  C CZ  . ARG A 190 ? 0.2163 0.1752 0.2731 -0.0391 0.0218  0.0086  190 ARG A CZ  
3003  N NH1 . ARG A 190 ? 0.1696 0.1622 0.2731 -0.0369 0.0332  0.0065  190 ARG A NH1 
3004  N NH2 . ARG A 190 ? 0.2331 0.2302 0.2869 -0.0706 0.0330  0.0027  190 ARG A NH2 
3018  N N   . GLY A 191 ? 0.4115 0.2276 0.3135 -0.0524 -0.0718 -0.0352 191 GLY A N   
3019  C CA  . GLY A 191 ? 0.4381 0.2545 0.3401 -0.1308 -0.1192 -0.0421 191 GLY A CA  
3020  C C   . GLY A 191 ? 0.4530 0.2693 0.3640 -0.1507 -0.1285 -0.0258 191 GLY A C   
3021  O O   . GLY A 191 ? 0.4831 0.2603 0.3614 -0.1564 -0.1162 0.0031  191 GLY A O   
3025  N N   . ALA A 192 ? 0.4671 0.2826 0.4003 -0.1555 -0.1405 -0.0268 192 ALA A N   
3026  C CA  . ALA A 192 ? 0.5342 0.3400 0.4239 -0.1673 -0.1436 -0.0078 192 ALA A CA  
3027  C C   . ALA A 192 ? 0.5896 0.3539 0.4448 -0.1919 -0.1447 0.0103  192 ALA A C   
3028  O O   . ALA A 192 ? 0.6063 0.3887 0.4554 -0.2377 -0.1194 0.0348  192 ALA A O   
3029  C CB  . ALA A 192 ? 0.5584 0.3562 0.4286 -0.1937 -0.1302 -0.0210 192 ALA A CB  
3035  N N   . GLU A 193 ? 0.6471 0.3153 0.4609 -0.1597 -0.1599 0.0124  193 GLU A N   
3036  C CA  . GLU A 193 ? 0.7005 0.3619 0.4844 -0.1354 -0.1507 0.0144  193 GLU A CA  
3037  C C   . GLU A 193 ? 0.6954 0.3457 0.4788 -0.1632 -0.1537 0.0492  193 GLU A C   
3038  O O   . GLU A 193 ? 0.7355 0.3234 0.4842 -0.1504 -0.1619 0.0679  193 GLU A O   
3039  C CB  . GLU A 193 ? 0.7342 0.4106 0.5118 -0.0664 -0.1319 -0.0134 193 GLU A CB  
3040  C CG  . GLU A 193 ? 0.7578 0.4628 0.5376 -0.0409 -0.1242 -0.0262 193 GLU A CG  
3041  C CD  . GLU A 193 ? 0.7689 0.5216 0.5584 -0.0291 -0.1222 -0.0277 193 GLU A CD  
3042  O OE1 . GLU A 193 ? 0.7717 0.5051 0.5652 -0.0105 -0.1356 -0.0218 193 GLU A OE1 
3043  O OE2 . GLU A 193 ? 0.7594 0.5628 0.5671 -0.0360 -0.1141 -0.0359 193 GLU A OE2 
3050  N N   . ARG A 194 ? 0.6263 0.3106 0.4643 -0.1958 -0.1649 0.0594  194 ARG A N   
3051  C CA  . ARG A 194 ? 0.5602 0.2927 0.4515 -0.1876 -0.1799 0.0650  194 ARG A CA  
3052  C C   . ARG A 194 ? 0.4856 0.3250 0.4313 -0.1872 -0.1523 0.1205  194 ARG A C   
3053  O O   . ARG A 194 ? 0.4480 0.2642 0.4200 -0.1510 -0.1705 0.1257  194 ARG A O   
3054  C CB  . ARG A 194 ? 0.6285 0.3458 0.4713 -0.1339 -0.1930 0.0431  194 ARG A CB  
3055  C CG  . ARG A 194 ? 0.6723 0.4482 0.5054 -0.1099 -0.1790 0.0311  194 ARG A CG  
3056  C CD  . ARG A 194 ? 0.7178 0.5229 0.5383 -0.1062 -0.1632 0.0289  194 ARG A CD  
3057  N NE  . ARG A 194 ? 0.7378 0.6126 0.5630 -0.1002 -0.1575 0.0264  194 ARG A NE  
3058  C CZ  . ARG A 194 ? 0.7769 0.6802 0.5816 -0.1050 -0.1523 0.0401  194 ARG A CZ  
3059  N NH1 . ARG A 194 ? 0.8225 0.6973 0.5908 -0.1045 -0.1292 0.0429  194 ARG A NH1 
3060  N NH2 . ARG A 194 ? 0.7880 0.7159 0.5908 -0.1270 -0.1549 0.0458  194 ARG A NH2 
3074  N N   . GLU A 195 ? 0.4282 0.3549 0.4228 -0.1735 -0.1215 0.1333  195 GLU A N   
3075  C CA  . GLU A 195 ? 0.3779 0.3853 0.4175 -0.1941 -0.0790 0.1223  195 GLU A CA  
3076  C C   . GLU A 195 ? 0.3499 0.3915 0.4112 -0.1824 -0.0492 0.1101  195 GLU A C   
3077  O O   . GLU A 195 ? 0.3385 0.3997 0.4038 -0.1565 -0.0312 0.1085  195 GLU A O   
3078  C CB  . GLU A 195 ? 0.3764 0.4196 0.4298 -0.1937 -0.0470 0.1135  195 GLU A CB  
3079  C CG  . GLU A 195 ? 0.3147 0.4492 0.4418 -0.1467 -0.0392 0.0833  195 GLU A CG  
3080  C CD  . GLU A 195 ? 0.3608 0.4885 0.4634 -0.1162 -0.0266 0.0637  195 GLU A CD  
3081  O OE1 . GLU A 195 ? 0.3579 0.4941 0.4632 -0.1166 -0.0200 0.0991  195 GLU A OE1 
3082  O OE2 . GLU A 195 ? 0.4019 0.5317 0.4847 -0.0844 -0.0117 0.0375  195 GLU A OE2 
3089  N N   . GLY A 196 ? 0.3503 0.3912 0.3982 -0.1771 -0.0568 0.1150  196 GLY A N   
3090  C CA  . GLY A 196 ? 0.3057 0.3713 0.3655 -0.1570 -0.0499 0.1108  196 GLY A CA  
3091  C C   . GLY A 196 ? 0.2561 0.3559 0.3480 -0.1265 -0.0188 0.0836  196 GLY A C   
3092  O O   . GLY A 196 ? 0.2627 0.3877 0.3468 -0.0645 -0.0059 0.0625  196 GLY A O   
3096  N N   . MET A 197 ? 0.3380 0.3047 0.3282 -0.0884 0.0240  0.0847  197 MET A N   
3097  C CA  . MET A 197 ? 0.3007 0.2988 0.3102 -0.0585 0.0496  0.0458  197 MET A CA  
3098  C C   . MET A 197 ? 0.2227 0.3030 0.2849 -0.0698 0.0451  0.0289  197 MET A C   
3099  O O   . MET A 197 ? 0.2360 0.3304 0.2888 -0.0671 0.0192  0.0517  197 MET A O   
3100  C CB  . MET A 197 ? 0.3993 0.3524 0.3167 -0.0069 0.0718  0.0213  197 MET A CB  
3101  C CG  . MET A 197 ? 0.3700 0.4123 0.3295 -0.0090 0.0826  -0.0133 197 MET A CG  
3102  S SD  . MET A 197 ? 0.3236 0.4463 0.3492 -0.1100 0.0808  -0.0906 197 MET A SD  
3103  C CE  . MET A 197 ? 0.3636 0.4991 0.3712 -0.0779 0.0529  -0.0609 197 MET A CE  
3113  N N   . SER A 198 ? 0.1847 0.2926 0.2517 -0.0498 0.0434  0.0245  198 SER A N   
3114  C CA  . SER A 198 ? 0.1490 0.3038 0.2319 -0.0577 0.0372  0.0299  198 SER A CA  
3115  C C   . SER A 198 ? 0.1792 0.2908 0.2291 -0.0034 0.0347  0.0089  198 SER A C   
3116  O O   . SER A 198 ? 0.1786 0.2475 0.2324 -0.0178 0.0253  -0.0283 198 SER A O   
3117  C CB  . SER A 198 ? 0.1932 0.3690 0.2143 -0.0591 0.0563  0.0177  198 SER A CB  
3118  O OG  . SER A 198 ? 0.2247 0.3390 0.2067 -0.0367 0.0460  0.0082  198 SER A OG  
3124  N N   . GLU A 199 ? 0.1957 0.2861 0.2281 -0.0050 0.0415  0.0060  199 GLU A N   
3125  C CA  . GLU A 199 ? 0.1814 0.2353 0.2043 0.0101  0.0460  0.0194  199 GLU A CA  
3126  C C   . GLU A 199 ? 0.2090 0.2047 0.2045 0.0136  0.0482  0.0340  199 GLU A C   
3127  O O   . GLU A 199 ? 0.1917 0.2117 0.2223 0.0108  0.0370  0.0334  199 GLU A O   
3128  C CB  . GLU A 199 ? 0.2039 0.1956 0.2070 -0.0001 0.0759  -0.0012 199 GLU A CB  
3129  C CG  . GLU A 199 ? 0.2267 0.1680 0.2420 0.0224  0.0327  -0.0169 199 GLU A CG  
3130  C CD  . GLU A 199 ? 0.1968 0.1859 0.2760 0.0591  0.0076  0.0094  199 GLU A CD  
3131  O OE1 . GLU A 199 ? 0.2178 0.2289 0.3131 0.0437  0.0299  0.0174  199 GLU A OE1 
3132  O OE2 . GLU A 199 ? 0.1815 0.2114 0.2771 0.0416  -0.0073 0.0471  199 GLU A OE2 
3139  N N   . ARG A 200 ? 0.1997 0.2041 0.2031 -0.0027 0.0486  0.0539  200 ARG A N   
3140  C CA  . ARG A 200 ? 0.2222 0.2596 0.2014 -0.0186 0.0681  0.0574  200 ARG A CA  
3141  C C   . ARG A 200 ? 0.2077 0.2389 0.2080 -0.0170 0.0725  0.0630  200 ARG A C   
3142  O O   . ARG A 200 ? 0.2268 0.2064 0.1983 -0.0412 0.0286  0.0486  200 ARG A O   
3143  C CB  . ARG A 200 ? 0.2786 0.3866 0.2103 -0.0033 0.0796  0.0866  200 ARG A CB  
3144  C CG  . ARG A 200 ? 0.3396 0.4858 0.2288 0.0520  0.0696  0.0603  200 ARG A CG  
3145  C CD  . ARG A 200 ? 0.2970 0.5029 0.2453 0.0988  0.0766  0.0505  200 ARG A CD  
3146  N NE  . ARG A 200 ? 0.2858 0.4601 0.2587 0.1630  0.0553  0.0301  200 ARG A NE  
3147  C CZ  . ARG A 200 ? 0.3490 0.4300 0.2665 0.1648  0.0519  0.0371  200 ARG A CZ  
3148  N NH1 . ARG A 200 ? 0.3522 0.4102 0.2608 0.1166  0.0188  0.0378  200 ARG A NH1 
3149  N NH2 . ARG A 200 ? 0.4287 0.4219 0.2776 0.2084  0.0437  0.0505  200 ARG A NH2 
3163  N N   . GLU A 201 ? 0.1836 0.2312 0.2244 0.0051  0.0765  0.0490  201 GLU A N   
3164  C CA  . GLU A 201 ? 0.1566 0.2215 0.2259 0.0068  0.0828  0.0346  201 GLU A CA  
3165  C C   . GLU A 201 ? 0.1793 0.1978 0.2130 -0.0089 0.0588  0.0269  201 GLU A C   
3166  O O   . GLU A 201 ? 0.1734 0.2142 0.2167 -0.0048 0.0496  0.0233  201 GLU A O   
3167  C CB  . GLU A 201 ? 0.1683 0.2649 0.2459 -0.0124 0.0829  0.0781  201 GLU A CB  
3168  C CG  . GLU A 201 ? 0.2264 0.3183 0.2680 -0.0547 0.0730  0.1044  201 GLU A CG  
3169  C CD  . GLU A 201 ? 0.2499 0.3605 0.2796 -0.0827 0.0606  0.1083  201 GLU A CD  
3170  O OE1 . GLU A 201 ? 0.2624 0.3588 0.2887 -0.0645 0.0579  0.1063  201 GLU A OE1 
3171  O OE2 . GLU A 201 ? 0.2663 0.4161 0.2903 -0.0482 0.0292  0.1220  201 GLU A OE2 
3178  N N   . PHE A 202 ? 0.1677 0.2142 0.1890 0.0063  0.0301  0.0235  202 PHE A N   
3179  C CA  . PHE A 202 ? 0.1637 0.2070 0.1836 -0.0081 0.0255  0.0269  202 PHE A CA  
3180  C C   . PHE A 202 ? 0.1548 0.2134 0.1828 -0.0048 0.0125  0.0241  202 PHE A C   
3181  O O   . PHE A 202 ? 0.1995 0.2158 0.1801 -0.0139 0.0196  0.0360  202 PHE A O   
3182  C CB  . PHE A 202 ? 0.1482 0.2084 0.1859 -0.0093 0.0072  0.0209  202 PHE A CB  
3183  C CG  . PHE A 202 ? 0.1652 0.1933 0.1851 0.0065  0.0306  0.0122  202 PHE A CG  
3184  C CD1 . PHE A 202 ? 0.1728 0.2232 0.1892 0.0060  0.0135  0.0333  202 PHE A CD1 
3185  C CD2 . PHE A 202 ? 0.1739 0.2153 0.1952 -0.0229 0.0083  0.0059  202 PHE A CD2 
3186  C CE1 . PHE A 202 ? 0.2155 0.2101 0.1995 -0.0355 0.0155  0.0356  202 PHE A CE1 
3187  C CE2 . PHE A 202 ? 0.1978 0.2077 0.2010 0.0399  0.0115  0.0152  202 PHE A CE2 
3188  C CZ  . PHE A 202 ? 0.1729 0.2013 0.2054 -0.0051 0.0264  0.0267  202 PHE A CZ  
3198  N N   . SER A 203 ? 0.1548 0.1759 0.1909 -0.0256 0.0018  0.0529  203 SER A N   
3199  C CA  . SER A 203 ? 0.1471 0.1926 0.1922 0.0115  0.0252  0.0282  203 SER A CA  
3200  C C   . SER A 203 ? 0.1316 0.1911 0.1991 -0.0100 0.0358  0.0364  203 SER A C   
3201  O O   . SER A 203 ? 0.1692 0.2022 0.2031 0.0037  0.0197  0.0417  203 SER A O   
3202  C CB  . SER A 203 ? 0.1510 0.2049 0.1794 -0.0161 0.0164  0.0212  203 SER A CB  
3203  O OG  . SER A 203 ? 0.2020 0.1998 0.1818 -0.0138 0.0196  0.0067  203 SER A OG  
3209  N N   . ALA A 204 ? 0.1769 0.2037 0.2136 -0.0018 0.0516  0.0563  204 ALA A N   
3210  C CA  . ALA A 204 ? 0.1938 0.1972 0.2217 -0.0419 0.0374  0.0488  204 ALA A CA  
3211  C C   . ALA A 204 ? 0.1914 0.1774 0.2310 -0.0296 0.0367  0.0424  204 ALA A C   
3212  O O   . ALA A 204 ? 0.2249 0.2296 0.2259 0.0015  0.0447  0.0542  204 ALA A O   
3213  C CB  . ALA A 204 ? 0.2383 0.2071 0.2140 -0.0449 0.0431  0.0711  204 ALA A CB  
3219  N N   . HIS A 205 ? 0.1703 0.1637 0.2449 -0.0098 0.0302  0.0248  205 HIS A N   
3220  C CA  . HIS A 205 ? 0.2023 0.1594 0.2469 0.0294  0.0200  -0.0001 205 HIS A CA  
3221  C C   . HIS A 205 ? 0.2006 0.1398 0.2174 -0.0232 0.0190  -0.0015 205 HIS A C   
3222  O O   . HIS A 205 ? 0.1966 0.1496 0.2152 -0.0259 0.0318  0.0170  205 HIS A O   
3223  C CB  . HIS A 205 ? 0.1911 0.2186 0.2836 0.0077  0.0154  0.0070  205 HIS A CB  
3224  C CG  . HIS A 205 ? 0.1596 0.2433 0.3156 -0.0115 0.0001  -0.0044 205 HIS A CG  
3225  N ND1 . HIS A 205 ? 0.2244 0.3204 0.3351 -0.0356 -0.0007 0.0056  205 HIS A ND1 
3226  C CD2 . HIS A 205 ? 0.1700 0.3341 0.3257 -0.0574 -0.0360 -0.0086 205 HIS A CD2 
3227  C CE1 . HIS A 205 ? 0.2259 0.3419 0.3392 -0.0673 -0.0201 -0.0172 205 HIS A CE1 
3228  N NE2 . HIS A 205 ? 0.2416 0.3356 0.3414 -0.0523 -0.0310 -0.0238 205 HIS A NE2 
3236  N N   . CYS A 206 ? 0.1851 0.1612 0.2067 -0.0190 0.0264  0.0182  206 CYS A N   
3237  C CA  . CYS A 206 ? 0.1497 0.1544 0.1937 0.0286  0.0375  0.0178  206 CYS A CA  
3238  C C   . CYS A 206 ? 0.1527 0.1699 0.1884 0.0058  0.0221  0.0214  206 CYS A C   
3239  O O   . CYS A 206 ? 0.1645 0.1509 0.1923 0.0048  0.0359  0.0348  206 CYS A O   
3240  C CB  . CYS A 206 ? 0.1577 0.1849 0.2031 0.0361  0.0492  -0.0042 206 CYS A CB  
3241  S SG  . CYS A 206 ? 0.1780 0.1849 0.2132 0.0201  0.0198  0.0212  206 CYS A SG  
3247  N N   . ALA A 207 ? 0.1458 0.1538 0.1900 -0.0104 0.0073  0.0084  207 ALA A N   
3248  C CA  . ALA A 207 ? 0.1695 0.1491 0.1867 0.0388  0.0109  0.0030  207 ALA A CA  
3249  C C   . ALA A 207 ? 0.1579 0.1750 0.1875 0.0307  -0.0045 0.0171  207 ALA A C   
3250  O O   . ALA A 207 ? 0.1725 0.2182 0.1916 -0.0141 -0.0021 0.0249  207 ALA A O   
3251  C CB  . ALA A 207 ? 0.1924 0.2059 0.2043 0.0356  0.0083  -0.0098 207 ALA A CB  
3257  N N   . ALA A 208 ? 0.1766 0.1642 0.2169 -0.0167 0.0128  0.0388  208 ALA A N   
3258  C CA  . ALA A 208 ? 0.1663 0.1902 0.2336 -0.0143 0.0566  0.0542  208 ALA A CA  
3259  C C   . ALA A 208 ? 0.1643 0.1704 0.2338 -0.0072 0.0307  0.0174  208 ALA A C   
3260  O O   . ALA A 208 ? 0.2018 0.1341 0.2520 0.0046  0.0318  0.0199  208 ALA A O   
3261  C CB  . ALA A 208 ? 0.2256 0.1828 0.2319 -0.0033 0.0433  0.0628  208 ALA A CB  
3267  N N   . LYS A 209 ? 0.1717 0.1426 0.2205 -0.0259 0.0346  0.0195  209 LYS A N   
3268  C CA  . LYS A 209 ? 0.1472 0.1796 0.2196 -0.0183 0.0082  0.0000  209 LYS A CA  
3269  C C   . LYS A 209 ? 0.1819 0.1767 0.2164 -0.0314 0.0015  -0.0001 209 LYS A C   
3270  O O   . LYS A 209 ? 0.1863 0.1731 0.2005 0.0003  -0.0056 0.0308  209 LYS A O   
3271  C CB  . LYS A 209 ? 0.1316 0.1481 0.2271 -0.0108 0.0123  0.0082  209 LYS A CB  
3272  C CG  . LYS A 209 ? 0.2066 0.2392 0.2656 -0.0111 0.0021  -0.0096 209 LYS A CG  
3273  C CD  . LYS A 209 ? 0.2523 0.2489 0.3003 0.0099  0.0159  -0.0261 209 LYS A CD  
3274  C CE  . LYS A 209 ? 0.3590 0.2867 0.3252 -0.0192 0.0153  -0.0349 209 LYS A CE  
3275  N NZ  . LYS A 209 ? 0.4379 0.3971 0.3410 -0.0085 0.0200  -0.0223 209 LYS A NZ  
3289  N N   . LEU A 210 ? 0.1475 0.1197 0.2209 0.0151  0.0022  -0.0156 210 LEU A N   
3290  C CA  . LEU A 210 ? 0.1330 0.1102 0.2121 0.0178  -0.0102 0.0033  210 LEU A CA  
3291  C C   . LEU A 210 ? 0.1637 0.1497 0.2096 -0.0119 -0.0118 0.0409  210 LEU A C   
3292  O O   . LEU A 210 ? 0.1669 0.1824 0.2158 -0.0198 0.0184  0.0344  210 LEU A O   
3293  C CB  . LEU A 210 ? 0.1813 0.1180 0.1996 -0.0143 -0.0094 0.0259  210 LEU A CB  
3294  C CG  . LEU A 210 ? 0.1654 0.1763 0.1904 0.0084  0.0033  0.0206  210 LEU A CG  
3295  C CD1 . LEU A 210 ? 0.1594 0.1714 0.1864 -0.0107 0.0223  0.0403  210 LEU A CD1 
3296  C CD2 . LEU A 210 ? 0.1851 0.1773 0.1965 -0.0197 0.0137  0.0086  210 LEU A CD2 
3308  N N   . GLU A 211 ? 0.1745 0.1379 0.1965 0.0068  0.0095  0.0244  211 GLU A N   
3309  C CA  . GLU A 211 ? 0.1870 0.1261 0.1875 0.0137  0.0257  0.0211  211 GLU A CA  
3310  C C   . GLU A 211 ? 0.2004 0.1310 0.1925 0.0044  0.0161  0.0208  211 GLU A C   
3311  O O   . GLU A 211 ? 0.1970 0.1413 0.1932 -0.0106 0.0075  0.0430  211 GLU A O   
3312  C CB  . GLU A 211 ? 0.1745 0.1781 0.1821 0.0325  -0.0187 0.0401  211 GLU A CB  
3313  C CG  . GLU A 211 ? 0.1865 0.1674 0.1909 0.0097  -0.0238 0.0890  211 GLU A CG  
3314  C CD  . GLU A 211 ? 0.2627 0.3079 0.2119 0.0194  0.0015  0.0968  211 GLU A CD  
3315  O OE1 . GLU A 211 ? 0.2080 0.3173 0.2214 0.0239  -0.0051 0.0871  211 GLU A OE1 
3316  O OE2 . GLU A 211 ? 0.3372 0.3558 0.2232 0.0359  0.0117  0.0864  211 GLU A OE2 
3323  N N   . GLU A 212 ? 0.1623 0.1544 0.1970 0.0016  0.0130  0.0074  212 GLU A N   
3324  C CA  . GLU A 212 ? 0.1748 0.1450 0.2093 0.0035  -0.0042 0.0047  212 GLU A CA  
3325  C C   . GLU A 212 ? 0.1878 0.1280 0.1961 -0.0211 -0.0015 -0.0073 212 GLU A C   
3326  O O   . GLU A 212 ? 0.2131 0.1567 0.1940 -0.0170 0.0277  -0.0109 212 GLU A O   
3327  C CB  . GLU A 212 ? 0.1619 0.1960 0.2254 -0.0326 0.0248  0.0015  212 GLU A CB  
3328  C CG  . GLU A 212 ? 0.1838 0.2094 0.2533 -0.0535 0.0216  -0.0122 212 GLU A CG  
3329  C CD  . GLU A 212 ? 0.2284 0.2637 0.2689 -0.0873 0.0065  -0.0197 212 GLU A CD  
3330  O OE1 . GLU A 212 ? 0.1957 0.2997 0.2789 -0.0725 -0.0167 -0.0217 212 GLU A OE1 
3331  O OE2 . GLU A 212 ? 0.2781 0.2219 0.2785 -0.0937 0.0317  -0.0313 212 GLU A OE2 
3338  N N   . MET A 213 ? 0.1800 0.1342 0.2001 -0.0067 -0.0050 0.0042  213 MET A N   
3339  C CA  . MET A 213 ? 0.1808 0.1360 0.1821 -0.0088 0.0000  0.0086  213 MET A CA  
3340  C C   . MET A 213 ? 0.1896 0.1565 0.1879 0.0113  -0.0010 0.0040  213 MET A C   
3341  O O   . MET A 213 ? 0.2008 0.1430 0.1870 0.0144  -0.0049 0.0056  213 MET A O   
3342  C CB  . MET A 213 ? 0.1959 0.1337 0.1821 0.0043  0.0197  0.0021  213 MET A CB  
3343  C CG  . MET A 213 ? 0.2169 0.1509 0.2058 0.0236  0.0199  0.0167  213 MET A CG  
3344  S SD  . MET A 213 ? 0.2030 0.1423 0.2278 0.0004  0.0143  0.0277  213 MET A SD  
3345  C CE  . MET A 213 ? 0.1936 0.1765 0.2245 -0.0315 -0.0075 0.0368  213 MET A CE  
3355  N N   . ILE A 214 ? 0.1221 0.1934 0.1826 0.0209  0.0076  0.0267  214 ILE A N   
3356  C CA  . ILE A 214 ? 0.1467 0.1735 0.1957 0.0162  0.0303  0.0315  214 ILE A CA  
3357  C C   . ILE A 214 ? 0.1742 0.1706 0.2103 0.0234  0.0290  0.0516  214 ILE A C   
3358  O O   . ILE A 214 ? 0.1597 0.1820 0.2258 0.0118  0.0174  0.0399  214 ILE A O   
3359  C CB  . ILE A 214 ? 0.1849 0.1515 0.1835 0.0152  0.0241  0.0132  214 ILE A CB  
3360  C CG1 . ILE A 214 ? 0.1760 0.1795 0.1965 0.0021  0.0277  0.0097  214 ILE A CG1 
3361  C CG2 . ILE A 214 ? 0.1877 0.1292 0.1831 0.0300  0.0241  0.0080  214 ILE A CG2 
3362  C CD1 . ILE A 214 ? 0.1864 0.1550 0.2213 0.0145  0.0206  0.0123  214 ILE A CD1 
3374  N N   . LEU A 215 ? 0.1856 0.1358 0.2315 0.0006  0.0372  0.0460  215 LEU A N   
3375  C CA  . LEU A 215 ? 0.2049 0.1385 0.2193 0.0102  0.0358  0.0465  215 LEU A CA  
3376  C C   . LEU A 215 ? 0.2274 0.1607 0.2265 0.0291  0.0330  0.0165  215 LEU A C   
3377  O O   . LEU A 215 ? 0.2581 0.1903 0.2381 0.0477  0.0156  0.0151  215 LEU A O   
3378  C CB  . LEU A 215 ? 0.1934 0.1687 0.2231 -0.0006 0.0376  0.0433  215 LEU A CB  
3379  C CG  . LEU A 215 ? 0.2072 0.1848 0.2358 0.0193  0.0386  0.0341  215 LEU A CG  
3380  C CD1 . LEU A 215 ? 0.2426 0.1636 0.2312 0.0110  0.0496  0.0539  215 LEU A CD1 
3381  C CD2 . LEU A 215 ? 0.1989 0.2616 0.2528 0.0217  0.0603  0.0203  215 LEU A CD2 
3393  N N   . ALA A 216 ? 0.2402 0.1447 0.2182 0.0247  0.0098  0.0132  216 ALA A N   
3394  C CA  . ALA A 216 ? 0.2474 0.1837 0.2267 0.0107  0.0147  0.0177  216 ALA A CA  
3395  C C   . ALA A 216 ? 0.2482 0.1679 0.2253 0.0289  0.0208  0.0014  216 ALA A C   
3396  O O   . ALA A 216 ? 0.2821 0.1573 0.2446 -0.0054 0.0449  -0.0165 216 ALA A O   
3397  C CB  . ALA A 216 ? 0.2181 0.1502 0.2317 -0.0286 0.0195  0.0329  216 ALA A CB  
3403  N N   . GLU A 217 ? 0.2227 0.1730 0.2137 0.0287  0.0077  -0.0006 217 GLU A N   
3404  C CA  . GLU A 217 ? 0.2288 0.1391 0.2213 0.0045  0.0040  -0.0064 217 GLU A CA  
3405  C C   . GLU A 217 ? 0.1902 0.1153 0.2315 0.0195  0.0044  -0.0009 217 GLU A C   
3406  O O   . GLU A 217 ? 0.2221 0.1761 0.2437 -0.0019 0.0348  -0.0177 217 GLU A O   
3407  C CB  . GLU A 217 ? 0.2288 0.1236 0.2261 0.0118  0.0280  0.0153  217 GLU A CB  
3408  C CG  . GLU A 217 ? 0.2388 0.1332 0.2358 0.0060  0.0149  0.0163  217 GLU A CG  
3409  C CD  . GLU A 217 ? 0.2277 0.2012 0.2595 0.0035  0.0032  0.0028  217 GLU A CD  
3410  O OE1 . GLU A 217 ? 0.2417 0.2417 0.2445 0.0130  -0.0092 0.0286  217 GLU A OE1 
3411  O OE2 . GLU A 217 ? 0.2053 0.2307 0.2846 -0.0240 0.0407  -0.0023 217 GLU A OE2 
3418  N N   . GLY A 218 ? 0.1926 0.1630 0.2343 -0.0076 0.0169  0.0443  218 GLY A N   
3419  C CA  . GLY A 218 ? 0.1910 0.1813 0.2313 -0.0043 0.0043  0.0331  218 GLY A CA  
3420  C C   . GLY A 218 ? 0.1567 0.1927 0.2213 0.0098  0.0045  0.0366  218 GLY A C   
3421  O O   . GLY A 218 ? 0.1654 0.1907 0.2246 0.0063  0.0174  0.0414  218 GLY A O   
3425  N N   . PRO A 219 ? 0.1685 0.2285 0.2136 0.0085  0.0209  0.0339  219 PRO A N   
3426  C CA  . PRO A 219 ? 0.2370 0.2202 0.2106 -0.0063 0.0221  0.0461  219 PRO A CA  
3427  C C   . PRO A 219 ? 0.2096 0.2134 0.2088 0.0366  -0.0071 0.0391  219 PRO A C   
3428  O O   . PRO A 219 ? 0.2057 0.2384 0.2050 0.0395  0.0077  0.0174  219 PRO A O   
3429  C CB  . PRO A 219 ? 0.2423 0.2889 0.2106 -0.0351 0.0271  0.0504  219 PRO A CB  
3430  C CG  . PRO A 219 ? 0.3277 0.3018 0.2195 -0.0181 0.0238  0.0644  219 PRO A CG  
3431  C CD  . PRO A 219 ? 0.2415 0.2717 0.2170 0.0198  -0.0020 0.0631  219 PRO A CD  
3439  N N   . GLU A 220 ? 0.1450 0.1775 0.2183 0.0304  -0.0040 0.0455  220 GLU A N   
3440  C CA  . GLU A 220 ? 0.1502 0.1710 0.2199 0.0294  -0.0186 0.0450  220 GLU A CA  
3441  C C   . GLU A 220 ? 0.1562 0.1562 0.2198 0.0393  -0.0103 0.0319  220 GLU A C   
3442  O O   . GLU A 220 ? 0.1754 0.1646 0.2217 -0.0134 0.0117  0.0235  220 GLU A O   
3443  C CB  . GLU A 220 ? 0.2334 0.1987 0.2535 0.0305  -0.0081 0.0243  220 GLU A CB  
3444  C CG  . GLU A 220 ? 0.2336 0.2300 0.2866 0.0725  0.0098  0.0244  220 GLU A CG  
3445  C CD  . GLU A 220 ? 0.2204 0.2245 0.3043 0.0821  0.0073  0.0140  220 GLU A CD  
3446  O OE1 . GLU A 220 ? 0.2282 0.1882 0.3004 0.0192  0.0336  0.0118  220 GLU A OE1 
3447  O OE2 . GLU A 220 ? 0.2415 0.2094 0.3326 0.0166  0.0198  -0.0078 220 GLU A OE2 
3454  N N   . THR A 221 ? 0.1505 0.1676 0.2218 0.0166  -0.0028 0.0119  221 THR A N   
3455  C CA  . THR A 221 ? 0.1572 0.1636 0.2068 0.0119  0.0077  0.0142  221 THR A CA  
3456  C C   . THR A 221 ? 0.1697 0.1419 0.1899 0.0496  0.0063  0.0271  221 THR A C   
3457  O O   . THR A 221 ? 0.1719 0.1676 0.1723 0.0154  0.0094  0.0284  221 THR A O   
3458  C CB  . THR A 221 ? 0.1400 0.1603 0.2146 0.0488  0.0037  0.0192  221 THR A CB  
3459  O OG1 . THR A 221 ? 0.1484 0.1607 0.2039 0.0332  -0.0074 0.0126  221 THR A OG1 
3460  C CG2 . THR A 221 ? 0.1860 0.1880 0.2307 0.0299  -0.0040 0.0004  221 THR A CG2 
3468  N N   . VAL A 222 ? 0.1811 0.1786 0.1920 0.0239  0.0222  0.0423  222 VAL A N   
3469  C CA  . VAL A 222 ? 0.1698 0.1577 0.1928 0.0241  0.0254  0.0165  222 VAL A CA  
3470  C C   . VAL A 222 ? 0.1705 0.1529 0.1888 0.0218  0.0055  0.0314  222 VAL A C   
3471  O O   . VAL A 222 ? 0.1586 0.1759 0.1984 0.0019  -0.0051 0.0204  222 VAL A O   
3472  C CB  . VAL A 222 ? 0.1532 0.1636 0.2079 0.0351  0.0251  -0.0087 222 VAL A CB  
3473  C CG1 . VAL A 222 ? 0.1551 0.1715 0.2081 0.0314  0.0475  0.0176  222 VAL A CG1 
3474  C CG2 . VAL A 222 ? 0.2047 0.1733 0.2224 -0.0107 0.0206  -0.0159 222 VAL A CG2 
3484  N N   . ALA A 223 ? 0.1501 0.1495 0.1802 0.0168  0.0043  0.0309  223 ALA A N   
3485  C CA  . ALA A 223 ? 0.1376 0.1742 0.1817 0.0195  0.0152  0.0169  223 ALA A CA  
3486  C C   . ALA A 223 ? 0.1380 0.1312 0.1580 -0.0042 0.0061  0.0099  223 ALA A C   
3487  O O   . ALA A 223 ? 0.1877 0.1634 0.1493 0.0086  -0.0087 -0.0110 223 ALA A O   
3488  C CB  . ALA A 223 ? 0.1640 0.2136 0.1907 -0.0120 -0.0034 0.0161  223 ALA A CB  
3494  N N   . ALA A 224 ? 0.1616 0.1587 0.1641 -0.0062 -0.0090 0.0100  224 ALA A N   
3495  C CA  . ALA A 224 ? 0.1614 0.1340 0.1695 -0.0180 -0.0154 0.0314  224 ALA A CA  
3496  C C   . ALA A 224 ? 0.1291 0.1065 0.1679 0.0011  -0.0138 -0.0077 224 ALA A C   
3497  O O   . ALA A 224 ? 0.1498 0.1340 0.1727 -0.0083 0.0106  0.0170  224 ALA A O   
3498  C CB  . ALA A 224 ? 0.1685 0.1134 0.1785 -0.0114 -0.0051 0.0348  224 ALA A CB  
3504  N N   . PHE A 225 ? 0.1216 0.1390 0.1583 0.0038  0.0153  0.0130  225 PHE A N   
3505  C CA  . PHE A 225 ? 0.1190 0.1392 0.1744 -0.0385 0.0062  0.0245  225 PHE A CA  
3506  C C   . PHE A 225 ? 0.1388 0.1084 0.1751 -0.0103 -0.0013 0.0030  225 PHE A C   
3507  O O   . PHE A 225 ? 0.1502 0.1700 0.1877 -0.0059 -0.0281 0.0174  225 PHE A O   
3508  C CB  . PHE A 225 ? 0.1343 0.1495 0.1837 -0.0279 -0.0006 0.0236  225 PHE A CB  
3509  C CG  . PHE A 225 ? 0.1446 0.1783 0.1827 -0.0086 -0.0151 0.0263  225 PHE A CG  
3510  C CD1 . PHE A 225 ? 0.1510 0.2039 0.1858 0.0344  -0.0337 0.0230  225 PHE A CD1 
3511  C CD2 . PHE A 225 ? 0.1613 0.2602 0.2014 0.0535  0.0064  -0.0020 225 PHE A CD2 
3512  C CE1 . PHE A 225 ? 0.1664 0.2295 0.1893 0.0327  -0.0152 0.0115  225 PHE A CE1 
3513  C CE2 . PHE A 225 ? 0.1601 0.2752 0.1971 0.0496  -0.0085 0.0157  225 PHE A CE2 
3514  C CZ  . PHE A 225 ? 0.1778 0.2720 0.1939 0.0591  -0.0083 0.0053  225 PHE A CZ  
3524  N N   . ILE A 226 ? 0.1507 0.1307 0.1686 -0.0240 0.0182  0.0004  226 ILE A N   
3525  C CA  . ILE A 226 ? 0.1396 0.1097 0.1620 -0.0509 0.0079  0.0125  226 ILE A CA  
3526  C C   . ILE A 226 ? 0.1481 0.0792 0.1630 -0.0499 0.0103  -0.0197 226 ILE A C   
3527  O O   . ILE A 226 ? 0.1654 0.1215 0.1642 -0.0429 0.0063  -0.0112 226 ILE A O   
3528  C CB  . ILE A 226 ? 0.1583 0.1286 0.1480 -0.0130 0.0132  0.0029  226 ILE A CB  
3529  C CG1 . ILE A 226 ? 0.1477 0.1602 0.1410 -0.0128 0.0125  0.0084  226 ILE A CG1 
3530  C CG2 . ILE A 226 ? 0.1745 0.0851 0.1583 -0.0087 -0.0204 0.0163  226 ILE A CG2 
3531  C CD1 . ILE A 226 ? 0.1567 0.1694 0.1421 -0.0306 -0.0018 0.0030  226 ILE A CD1 
3543  N N   . GLY A 227 ? 0.1316 0.1095 0.1669 0.0068  0.0151  0.0063  227 GLY A N   
3544  C CA  . GLY A 227 ? 0.1270 0.1206 0.1614 0.0046  0.0178  0.0047  227 GLY A CA  
3545  C C   . GLY A 227 ? 0.1277 0.1448 0.1617 -0.0324 0.0141  -0.0008 227 GLY A C   
3546  O O   . GLY A 227 ? 0.1423 0.1292 0.1620 0.0042  0.0011  0.0159  227 GLY A O   
3550  N N   . GLU A 228 ? 0.1092 0.1474 0.1621 -0.0043 0.0109  0.0032  228 GLU A N   
3551  C CA  . GLU A 228 ? 0.0992 0.1813 0.1547 0.0138  0.0079  0.0038  228 GLU A CA  
3552  C C   . GLU A 228 ? 0.1705 0.1301 0.1552 -0.0042 0.0107  0.0146  228 GLU A C   
3553  O O   . GLU A 228 ? 0.1649 0.1660 0.1590 0.0030  -0.0078 0.0066  228 GLU A O   
3554  C CB  . GLU A 228 ? 0.1230 0.1600 0.1591 -0.0207 -0.0035 0.0382  228 GLU A CB  
3555  C CG  . GLU A 228 ? 0.1413 0.1404 0.1544 -0.0306 -0.0187 0.0139  228 GLU A CG  
3556  C CD  . GLU A 228 ? 0.1596 0.1487 0.1472 -0.0098 0.0000  0.0114  228 GLU A CD  
3557  O OE1 . GLU A 228 ? 0.1945 0.1838 0.1508 -0.0021 -0.0021 0.0155  228 GLU A OE1 
3558  O OE2 . GLU A 228 ? 0.1830 0.1431 0.1489 -0.0473 -0.0093 -0.0059 228 GLU A OE2 
3565  N N   . PRO A 229 ? 0.1619 0.1233 0.1477 -0.0472 0.0177  0.0045  229 PRO A N   
3566  C CA  . PRO A 229 ? 0.1293 0.1347 0.1501 0.0045  0.0286  0.0000  229 PRO A CA  
3567  C C   . PRO A 229 ? 0.1278 0.1348 0.1577 -0.0214 0.0218  0.0043  229 PRO A C   
3568  O O   . PRO A 229 ? 0.1408 0.1483 0.1692 -0.0287 -0.0093 -0.0028 229 PRO A O   
3569  C CB  . PRO A 229 ? 0.1208 0.1625 0.1562 -0.0153 0.0256  0.0182  229 PRO A CB  
3570  C CG  . PRO A 229 ? 0.1385 0.1473 0.1616 -0.0339 0.0178  0.0201  229 PRO A CG  
3571  C CD  . PRO A 229 ? 0.1623 0.1199 0.1622 -0.0484 0.0211  0.0067  229 PRO A CD  
3579  N N   . VAL A 230 ? 0.1559 0.1390 0.1584 -0.0106 -0.0141 0.0227  230 VAL A N   
3580  C CA  . VAL A 230 ? 0.1445 0.1715 0.1638 -0.0123 -0.0033 0.0090  230 VAL A CA  
3581  C C   . VAL A 230 ? 0.1250 0.1541 0.1702 -0.0026 -0.0114 0.0093  230 VAL A C   
3582  O O   . VAL A 230 ? 0.1364 0.1583 0.1872 -0.0077 -0.0060 0.0289  230 VAL A O   
3583  C CB  . VAL A 230 ? 0.1208 0.1738 0.1620 0.0027  0.0065  -0.0008 230 VAL A CB  
3584  C CG1 . VAL A 230 ? 0.1519 0.1990 0.1763 0.0016  0.0256  0.0116  230 VAL A CG1 
3585  C CG2 . VAL A 230 ? 0.1790 0.1320 0.1720 0.0020  -0.0146 0.0021  230 VAL A CG2 
3595  N N   . LEU A 231 ? 0.1441 0.1797 0.1715 0.0113  -0.0097 -0.0040 231 LEU A N   
3596  C CA  . LEU A 231 ? 0.1383 0.1339 0.1895 0.0324  -0.0146 -0.0178 231 LEU A CA  
3597  C C   . LEU A 231 ? 0.1588 0.1322 0.1805 0.0642  0.0122  -0.0062 231 LEU A C   
3598  O O   . LEU A 231 ? 0.1548 0.1765 0.1842 0.0374  0.0128  -0.0047 231 LEU A O   
3599  C CB  . LEU A 231 ? 0.1712 0.1560 0.1953 -0.0033 0.0067  0.0131  231 LEU A CB  
3600  C CG  . LEU A 231 ? 0.1677 0.1535 0.1955 0.0341  0.0209  0.0245  231 LEU A CG  
3601  C CD1 . LEU A 231 ? 0.1546 0.1696 0.1905 -0.0043 0.0242  0.0059  231 LEU A CD1 
3602  C CD2 . LEU A 231 ? 0.1963 0.1623 0.1751 0.0339  0.0272  0.0147  231 LEU A CD2 
3614  N N   . GLY A 232 ? 0.1389 0.1463 0.1915 0.0185  0.0151  0.0101  232 GLY A N   
3615  C CA  . GLY A 232 ? 0.1436 0.1642 0.1777 0.0175  0.0233  0.0252  232 GLY A CA  
3616  C C   . GLY A 232 ? 0.1427 0.1756 0.1779 0.0381  0.0200  0.0138  232 GLY A C   
3617  O O   . GLY A 232 ? 0.1443 0.1566 0.1761 0.0181  0.0217  -0.0262 232 GLY A O   
3621  N N   . THR A 233 ? 0.1344 0.1500 0.1760 0.0062  0.0223  0.0031  233 THR A N   
3622  C CA  . THR A 233 ? 0.1679 0.1761 0.1601 0.0150  -0.0060 -0.0040 233 THR A CA  
3623  C C   . THR A 233 ? 0.1479 0.2055 0.1618 -0.0293 0.0195  0.0167  233 THR A C   
3624  O O   . THR A 233 ? 0.1919 0.2305 0.1719 0.0003  -0.0147 0.0208  233 THR A O   
3625  C CB  . THR A 233 ? 0.2199 0.1579 0.1755 -0.0090 0.0103  0.0036  233 THR A CB  
3626  O OG1 . THR A 233 ? 0.2522 0.2002 0.1841 -0.0548 0.0091  0.0121  233 THR A OG1 
3627  C CG2 . THR A 233 ? 0.2515 0.1281 0.1827 0.0316  -0.0103 0.0003  233 THR A CG2 
3635  N N   . GLY A 234 ? 0.1651 0.1622 0.1829 -0.0125 0.0181  0.0017  234 GLY A N   
3636  C CA  . GLY A 234 ? 0.1652 0.1530 0.1823 -0.0264 0.0001  0.0148  234 GLY A CA  
3637  C C   . GLY A 234 ? 0.1444 0.1512 0.1888 -0.0504 0.0089  0.0355  234 GLY A C   
3638  O O   . GLY A 234 ? 0.1438 0.1476 0.2069 -0.0173 0.0103  0.0160  234 GLY A O   
3642  N N   . GLY A 235 ? 0.1141 0.1760 0.1850 -0.0193 -0.0048 -0.0114 235 GLY A N   
3643  C CA  . GLY A 235 ? 0.1411 0.1438 0.1658 -0.0236 0.0153  -0.0083 235 GLY A CA  
3644  C C   . GLY A 235 ? 0.1642 0.1886 0.1757 0.0327  0.0175  -0.0122 235 GLY A C   
3645  O O   . GLY A 235 ? 0.1563 0.2077 0.1750 0.0155  -0.0041 -0.0014 235 GLY A O   
3649  N N   . ILE A 236 ? 0.1613 0.1863 0.1996 -0.0164 0.0280  -0.0050 236 ILE A N   
3650  C CA  . ILE A 236 ? 0.1605 0.1532 0.2099 -0.0066 0.0271  -0.0051 236 ILE A CA  
3651  C C   . ILE A 236 ? 0.1409 0.1327 0.1994 0.0124  0.0248  -0.0035 236 ILE A C   
3652  O O   . ILE A 236 ? 0.1803 0.1168 0.1884 0.0210  -0.0377 0.0120  236 ILE A O   
3653  C CB  . ILE A 236 ? 0.1890 0.1219 0.2230 -0.0341 0.0189  -0.0202 236 ILE A CB  
3654  C CG1 . ILE A 236 ? 0.2473 0.1641 0.2698 0.0062  0.0249  -0.0153 236 ILE A CG1 
3655  C CG2 . ILE A 236 ? 0.2323 0.1123 0.2326 0.0183  0.0107  -0.0531 236 ILE A CG2 
3656  C CD1 . ILE A 236 ? 0.2396 0.2340 0.2878 0.0057  0.0231  0.0144  236 ILE A CD1 
3668  N N   . VAL A 237 ? 0.1357 0.1558 0.1956 0.0059  0.0246  0.0196  237 VAL A N   
3669  C CA  . VAL A 237 ? 0.1370 0.1062 0.1944 0.0269  0.0060  0.0196  237 VAL A CA  
3670  C C   . VAL A 237 ? 0.1161 0.1463 0.1782 -0.0007 -0.0108 -0.0086 237 VAL A C   
3671  O O   . VAL A 237 ? 0.1456 0.1734 0.1708 0.0201  -0.0117 0.0141  237 VAL A O   
3672  C CB  . VAL A 237 ? 0.1492 0.1501 0.1902 0.0250  0.0029  0.0370  237 VAL A CB  
3673  C CG1 . VAL A 237 ? 0.1934 0.1353 0.2171 0.0267  -0.0041 0.0401  237 VAL A CG1 
3674  C CG2 . VAL A 237 ? 0.1820 0.1670 0.1952 0.0046  -0.0238 0.0228  237 VAL A CG2 
3684  N N   . PRO A 238 ? 0.1471 0.1695 0.1940 -0.0018 -0.0010 -0.0258 238 PRO A N   
3685  C CA  . PRO A 238 ? 0.1690 0.1936 0.1921 0.0303  0.0027  0.0038  238 PRO A CA  
3686  C C   . PRO A 238 ? 0.1636 0.1856 0.1819 -0.0162 0.0075  0.0211  238 PRO A C   
3687  O O   . PRO A 238 ? 0.1829 0.1736 0.1722 -0.0127 0.0198  0.0274  238 PRO A O   
3688  C CB  . PRO A 238 ? 0.1813 0.1481 0.1884 0.0390  0.0135  0.0130  238 PRO A CB  
3689  C CG  . PRO A 238 ? 0.1597 0.1616 0.1808 0.0152  0.0105  0.0068  238 PRO A CG  
3690  C CD  . PRO A 238 ? 0.1640 0.1638 0.1931 -0.0084 0.0304  -0.0057 238 PRO A CD  
3698  N N   . PRO A 239 ? 0.1643 0.1565 0.1768 0.0180  0.0041  0.0190  239 PRO A N   
3699  C CA  . PRO A 239 ? 0.1773 0.1916 0.1805 0.0375  0.0413  0.0189  239 PRO A CA  
3700  C C   . PRO A 239 ? 0.1808 0.1642 0.1763 0.0331  0.0224  0.0085  239 PRO A C   
3701  O O   . PRO A 239 ? 0.2214 0.2064 0.1932 -0.0090 0.0368  0.0134  239 PRO A O   
3702  C CB  . PRO A 239 ? 0.1922 0.1867 0.1797 0.0358  0.0342  0.0151  239 PRO A CB  
3703  C CG  . PRO A 239 ? 0.1863 0.1823 0.1801 0.0599  0.0121  0.0233  239 PRO A CG  
3704  C CD  . PRO A 239 ? 0.1809 0.1806 0.1690 0.0116  -0.0027 0.0357  239 PRO A CD  
3712  N N   . PRO A 240 ? 0.1474 0.1797 0.1739 0.0147  0.0239  0.0067  240 PRO A N   
3713  C CA  . PRO A 240 ? 0.1299 0.2275 0.1765 0.0080  0.0051  0.0069  240 PRO A CA  
3714  C C   . PRO A 240 ? 0.0730 0.2239 0.1692 -0.0062 0.0377  0.0253  240 PRO A C   
3715  O O   . PRO A 240 ? 0.1424 0.2349 0.1781 0.0314  0.0386  0.0245  240 PRO A O   
3716  C CB  . PRO A 240 ? 0.1699 0.2273 0.1834 0.0239  0.0218  0.0127  240 PRO A CB  
3717  C CG  . PRO A 240 ? 0.1697 0.1565 0.1871 -0.0051 0.0043  0.0095  240 PRO A CG  
3718  C CD  . PRO A 240 ? 0.1849 0.1582 0.1813 -0.0132 0.0221  0.0143  240 PRO A CD  
3726  N N   . GLU A 241 ? 0.1305 0.2579 0.1746 0.0040  0.0230  0.0099  241 GLU A N   
3727  C CA  . GLU A 241 ? 0.1453 0.2425 0.1811 -0.0032 0.0251  0.0340  241 GLU A CA  
3728  C C   . GLU A 241 ? 0.1691 0.2376 0.1750 0.0079  0.0209  0.0111  241 GLU A C   
3729  O O   . GLU A 241 ? 0.1801 0.2289 0.1652 0.0023  0.0302  0.0096  241 GLU A O   
3730  C CB  . GLU A 241 ? 0.1881 0.2160 0.2048 -0.0012 0.0124  0.0305  241 GLU A CB  
3731  C CG  . GLU A 241 ? 0.2159 0.2380 0.2245 0.0129  0.0505  0.0162  241 GLU A CG  
3732  C CD  . GLU A 241 ? 0.2290 0.2774 0.2466 0.0624  0.0439  -0.0204 241 GLU A CD  
3733  O OE1 . GLU A 241 ? 0.2590 0.2953 0.2699 0.0703  0.0232  -0.0270 241 GLU A OE1 
3734  O OE2 . GLU A 241 ? 0.2425 0.3138 0.2521 0.0554  0.0594  -0.0143 241 GLU A OE2 
3741  N N   . GLY A 242 ? 0.1726 0.2265 0.1744 0.0229  0.0190  0.0255  242 GLY A N   
3742  C CA  . GLY A 242 ? 0.1873 0.2231 0.1665 0.0357  0.0051  0.0170  242 GLY A CA  
3743  C C   . GLY A 242 ? 0.1694 0.2099 0.1809 0.0315  0.0216  0.0125  242 GLY A C   
3744  O O   . GLY A 242 ? 0.1489 0.1921 0.2056 0.0175  0.0159  0.0246  242 GLY A O   
3748  N N   . TYR A 243 ? 0.1770 0.1777 0.1714 0.0106  0.0228  0.0222  243 TYR A N   
3749  C CA  . TYR A 243 ? 0.1482 0.1782 0.1625 -0.0090 0.0080  -0.0022 243 TYR A CA  
3750  C C   . TYR A 243 ? 0.1442 0.1596 0.1552 -0.0379 0.0064  0.0200  243 TYR A C   
3751  O O   . TYR A 243 ? 0.1772 0.1836 0.1648 0.0069  0.0118  0.0080  243 TYR A O   
3752  C CB  . TYR A 243 ? 0.1611 0.1891 0.1790 -0.0041 -0.0049 -0.0084 243 TYR A CB  
3753  C CG  . TYR A 243 ? 0.1291 0.2041 0.1728 0.0163  0.0072  0.0229  243 TYR A CG  
3754  C CD1 . TYR A 243 ? 0.1636 0.1977 0.1691 0.0309  0.0242  0.0033  243 TYR A CD1 
3755  C CD2 . TYR A 243 ? 0.1364 0.1753 0.1733 -0.0061 0.0253  0.0163  243 TYR A CD2 
3756  C CE1 . TYR A 243 ? 0.1632 0.1815 0.1706 0.0186  0.0298  -0.0051 243 TYR A CE1 
3757  C CE2 . TYR A 243 ? 0.1409 0.1871 0.1737 -0.0076 0.0272  0.0161  243 TYR A CE2 
3758  C CZ  . TYR A 243 ? 0.1579 0.1825 0.1698 0.0002  0.0339  0.0212  243 TYR A CZ  
3759  O OH  . TYR A 243 ? 0.1585 0.1567 0.1672 -0.0199 0.0246  -0.0069 243 TYR A OH  
3769  N N   . TRP A 244 ? 0.1437 0.1585 0.1672 -0.0338 -0.0067 0.0153  244 TRP A N   
3770  C CA  . TRP A 244 ? 0.1321 0.1736 0.1658 -0.0155 -0.0068 0.0130  244 TRP A CA  
3771  C C   . TRP A 244 ? 0.1308 0.1782 0.1706 0.0053  0.0037  0.0343  244 TRP A C   
3772  O O   . TRP A 244 ? 0.1280 0.1683 0.1784 0.0100  0.0204  0.0166  244 TRP A O   
3773  C CB  . TRP A 244 ? 0.1486 0.1872 0.1691 -0.0036 -0.0059 -0.0126 244 TRP A CB  
3774  C CG  . TRP A 244 ? 0.1581 0.1915 0.1682 -0.0334 0.0022  -0.0094 244 TRP A CG  
3775  C CD1 . TRP A 244 ? 0.1567 0.2018 0.1648 -0.0194 -0.0055 -0.0112 244 TRP A CD1 
3776  C CD2 . TRP A 244 ? 0.1417 0.1587 0.1629 0.0102  0.0007  -0.0007 244 TRP A CD2 
3777  N NE1 . TRP A 244 ? 0.1381 0.1542 0.1702 0.0133  -0.0059 0.0061  244 TRP A NE1 
3778  C CE2 . TRP A 244 ? 0.1516 0.1289 0.1682 0.0164  -0.0042 0.0139  244 TRP A CE2 
3779  C CE3 . TRP A 244 ? 0.1921 0.1793 0.1617 0.0169  0.0252  0.0124  244 TRP A CE3 
3780  C CZ2 . TRP A 244 ? 0.1691 0.1433 0.1689 0.0225  0.0015  0.0196  244 TRP A CZ2 
3781  C CZ3 . TRP A 244 ? 0.1898 0.1673 0.1694 0.0261  0.0123  0.0159  244 TRP A CZ3 
3782  C CH2 . TRP A 244 ? 0.1807 0.1122 0.1610 0.0166  -0.0126 0.0216  244 TRP A CH2 
3793  N N   . GLU A 245 ? 0.1366 0.2015 0.1755 -0.0183 0.0057  0.0520  245 GLU A N   
3794  C CA  . GLU A 245 ? 0.1629 0.1869 0.1844 -0.0208 0.0272  0.0475  245 GLU A CA  
3795  C C   . GLU A 245 ? 0.1768 0.1901 0.1897 0.0006  0.0252  0.0299  245 GLU A C   
3796  O O   . GLU A 245 ? 0.1932 0.2183 0.1675 0.0102  0.0382  0.0259  245 GLU A O   
3797  C CB  . GLU A 245 ? 0.1879 0.2444 0.1900 -0.0206 0.0196  0.0564  245 GLU A CB  
3798  C CG  . GLU A 245 ? 0.2804 0.3195 0.2044 0.0129  0.0168  0.0575  245 GLU A CG  
3799  C CD  . GLU A 245 ? 0.4565 0.5054 0.2445 0.0314  -0.0090 0.0599  245 GLU A CD  
3800  O OE1 . GLU A 245 ? 0.5285 0.5918 0.2573 0.1293  0.0271  0.0632  245 GLU A OE1 
3801  O OE2 . GLU A 245 ? 0.5722 0.5946 0.2705 -0.0113 -0.0273 0.0229  245 GLU A OE2 
3808  N N   . ALA A 246 ? 0.1251 0.1586 0.1885 0.0229  0.0392  0.0335  246 ALA A N   
3809  C CA  . ALA A 246 ? 0.1605 0.1632 0.1875 0.0382  0.0198  0.0250  246 ALA A CA  
3810  C C   . ALA A 246 ? 0.1567 0.1268 0.1769 0.0104  0.0067  0.0350  246 ALA A C   
3811  O O   . ALA A 246 ? 0.1770 0.1839 0.1889 0.0161  0.0086  0.0121  246 ALA A O   
3812  C CB  . ALA A 246 ? 0.1906 0.1689 0.1983 -0.0083 0.0324  -0.0034 246 ALA A CB  
3818  N N   . ILE A 247 ? 0.1660 0.1243 0.1898 -0.0071 0.0133  0.0268  247 ILE A N   
3819  C CA  . ILE A 247 ? 0.1599 0.1289 0.1728 0.0158  -0.0028 0.0134  247 ILE A CA  
3820  C C   . ILE A 247 ? 0.1335 0.1506 0.1705 0.0260  0.0137  0.0052  247 ILE A C   
3821  O O   . ILE A 247 ? 0.1473 0.1664 0.1706 0.0407  0.0029  0.0270  247 ILE A O   
3822  C CB  . ILE A 247 ? 0.1677 0.1737 0.1943 0.0434  0.0099  0.0229  247 ILE A CB  
3823  C CG1 . ILE A 247 ? 0.2006 0.2320 0.2039 0.0157  -0.0100 0.0398  247 ILE A CG1 
3824  C CG2 . ILE A 247 ? 0.1626 0.1715 0.1811 0.0276  0.0091  0.0413  247 ILE A CG2 
3825  C CD1 . ILE A 247 ? 0.1882 0.2833 0.2074 0.0279  -0.0141 0.0190  247 ILE A CD1 
3837  N N   . GLN A 248 ? 0.1606 0.1615 0.1616 -0.0045 0.0118  0.0019  248 GLN A N   
3838  C CA  . GLN A 248 ? 0.1290 0.1630 0.1735 0.0168  -0.0073 0.0058  248 GLN A CA  
3839  C C   . GLN A 248 ? 0.1500 0.1799 0.1760 0.0035  -0.0082 0.0080  248 GLN A C   
3840  O O   . GLN A 248 ? 0.1576 0.1757 0.1976 0.0053  0.0025  -0.0123 248 GLN A O   
3841  C CB  . GLN A 248 ? 0.1569 0.1306 0.1853 0.0202  -0.0116 -0.0155 248 GLN A CB  
3842  C CG  . GLN A 248 ? 0.1333 0.1553 0.1908 0.0078  0.0039  0.0035  248 GLN A CG  
3843  C CD  . GLN A 248 ? 0.1538 0.1631 0.2084 0.0239  -0.0111 0.0161  248 GLN A CD  
3844  O OE1 . GLN A 248 ? 0.1556 0.2123 0.2372 -0.0140 0.0008  -0.0004 248 GLN A OE1 
3845  N NE2 . GLN A 248 ? 0.1580 0.1457 0.2060 -0.0012 -0.0056 0.0179  248 GLN A NE2 
3854  N N   . GLY A 249 ? 0.1643 0.1968 0.1665 0.0313  -0.0080 0.0480  249 GLY A N   
3855  C CA  . GLY A 249 ? 0.1575 0.1576 0.1617 0.0154  -0.0086 0.0354  249 GLY A CA  
3856  C C   . GLY A 249 ? 0.1905 0.1463 0.1814 0.0432  0.0094  0.0421  249 GLY A C   
3857  O O   . GLY A 249 ? 0.2071 0.1584 0.1904 0.0056  -0.0067 0.0171  249 GLY A O   
3861  N N   . VAL A 250 ? 0.1518 0.1590 0.1876 0.0344  0.0346  0.0460  250 VAL A N   
3862  C CA  . VAL A 250 ? 0.1605 0.1742 0.1898 0.0563  0.0221  0.0217  250 VAL A CA  
3863  C C   . VAL A 250 ? 0.1515 0.1378 0.1891 0.0089  0.0026  0.0263  250 VAL A C   
3864  O O   . VAL A 250 ? 0.1787 0.1615 0.1919 0.0189  -0.0005 0.0159  250 VAL A O   
3865  C CB  . VAL A 250 ? 0.1487 0.1827 0.1814 0.0384  0.0118  0.0486  250 VAL A CB  
3866  C CG1 . VAL A 250 ? 0.1676 0.2049 0.1868 -0.0066 -0.0104 0.0546  250 VAL A CG1 
3867  C CG2 . VAL A 250 ? 0.1817 0.1835 0.2010 -0.0122 0.0088  -0.0214 250 VAL A CG2 
3877  N N   . LEU A 251 ? 0.1386 0.1483 0.1791 -0.0160 0.0157  0.0241  251 LEU A N   
3878  C CA  . LEU A 251 ? 0.1404 0.1816 0.1740 -0.0077 -0.0018 0.0492  251 LEU A CA  
3879  C C   . LEU A 251 ? 0.1601 0.1967 0.1818 -0.0102 0.0196  0.0499  251 LEU A C   
3880  O O   . LEU A 251 ? 0.1798 0.2133 0.1910 0.0057  0.0345  0.0289  251 LEU A O   
3881  C CB  . LEU A 251 ? 0.1433 0.1822 0.1670 0.0111  0.0185  0.0291  251 LEU A CB  
3882  C CG  . LEU A 251 ? 0.1556 0.1665 0.1724 0.0093  0.0186  0.0421  251 LEU A CG  
3883  C CD1 . LEU A 251 ? 0.2042 0.1620 0.1744 -0.0409 0.0112  0.0585  251 LEU A CD1 
3884  C CD2 . LEU A 251 ? 0.1719 0.1236 0.1954 0.0000  0.0102  0.0308  251 LEU A CD2 
3896  N N   . ALA A 252 ? 0.1613 0.1863 0.1731 0.0093  0.0083  0.0281  252 ALA A N   
3897  C CA  . ALA A 252 ? 0.1790 0.2083 0.1713 -0.0193 -0.0030 0.0255  252 ALA A CA  
3898  C C   . ALA A 252 ? 0.1827 0.1941 0.1903 0.0123  0.0087  0.0115  252 ALA A C   
3899  O O   . ALA A 252 ? 0.1606 0.1925 0.2286 0.0233  0.0155  0.0147  252 ALA A O   
3900  C CB  . ALA A 252 ? 0.1451 0.2352 0.1771 0.0151  -0.0081 0.0044  252 ALA A CB  
3906  N N   . LYS A 253 ? 0.2054 0.1795 0.1906 -0.0037 0.0204  0.0192  253 LYS A N   
3907  C CA  . LYS A 253 ? 0.1729 0.1840 0.1985 0.0002  -0.0009 0.0092  253 LYS A CA  
3908  C C   . LYS A 253 ? 0.1733 0.2073 0.2054 0.0602  -0.0124 0.0383  253 LYS A C   
3909  O O   . LYS A 253 ? 0.1902 0.1831 0.2178 0.0699  0.0183  0.0216  253 LYS A O   
3910  C CB  . LYS A 253 ? 0.2081 0.2093 0.1964 -0.0031 0.0153  0.0290  253 LYS A CB  
3911  C CG  . LYS A 253 ? 0.2308 0.2269 0.1915 0.0135  0.0188  0.0228  253 LYS A CG  
3912  C CD  . LYS A 253 ? 0.2531 0.2048 0.1855 0.0000  0.0009  0.0405  253 LYS A CD  
3913  C CE  . LYS A 253 ? 0.2826 0.2338 0.1981 -0.0177 -0.0212 0.0452  253 LYS A CE  
3914  N NZ  . LYS A 253 ? 0.3184 0.2287 0.2168 -0.0328 -0.0079 0.0471  253 LYS A NZ  
3928  N N   . TYR A 254 ? 0.2255 0.1739 0.1933 0.0186  -0.0062 0.0365  254 TYR A N   
3929  C CA  . TYR A 254 ? 0.2425 0.1737 0.1939 -0.0049 0.0061  0.0442  254 TYR A CA  
3930  C C   . TYR A 254 ? 0.1831 0.1747 0.1874 0.0068  0.0265  0.0411  254 TYR A C   
3931  O O   . TYR A 254 ? 0.1761 0.1817 0.1743 0.0186  0.0109  0.0310  254 TYR A O   
3932  C CB  . TYR A 254 ? 0.2477 0.2165 0.2048 0.0009  -0.0220 0.0413  254 TYR A CB  
3933  C CG  . TYR A 254 ? 0.2027 0.1734 0.2023 0.0059  -0.0006 0.0462  254 TYR A CG  
3934  C CD1 . TYR A 254 ? 0.2205 0.1826 0.2148 -0.0037 0.0102  0.0390  254 TYR A CD1 
3935  C CD2 . TYR A 254 ? 0.2085 0.1533 0.2107 0.0095  -0.0131 0.0257  254 TYR A CD2 
3936  C CE1 . TYR A 254 ? 0.2345 0.1751 0.2220 0.0092  0.0430  0.0278  254 TYR A CE1 
3937  C CE2 . TYR A 254 ? 0.2177 0.1141 0.2145 -0.0383 -0.0128 0.0051  254 TYR A CE2 
3938  C CZ  . TYR A 254 ? 0.2232 0.1686 0.2258 -0.0386 0.0031  0.0175  254 TYR A CZ  
3939  O OH  . TYR A 254 ? 0.2303 0.2071 0.2423 -0.0276 0.0118  0.0155  254 TYR A OH  
3949  N N   . ASP A 255 ? 0.1722 0.1652 0.1884 -0.0028 0.0112  0.0265  255 ASP A N   
3950  C CA  . ASP A 255 ? 0.1814 0.2051 0.2048 0.0375  0.0225  0.0436  255 ASP A CA  
3951  C C   . ASP A 255 ? 0.1787 0.1676 0.1859 0.0218  0.0342  0.0365  255 ASP A C   
3952  O O   . ASP A 255 ? 0.1647 0.2386 0.1933 0.0075  0.0212  0.0692  255 ASP A O   
3953  C CB  . ASP A 255 ? 0.1804 0.2592 0.2292 0.0330  0.0127  0.0609  255 ASP A CB  
3954  C CG  . ASP A 255 ? 0.2539 0.3819 0.2600 0.0340  0.0015  0.0479  255 ASP A CG  
3955  O OD1 . ASP A 255 ? 0.2221 0.3566 0.2803 0.0218  -0.0234 0.0555  255 ASP A OD1 
3956  O OD2 . ASP A 255 ? 0.2920 0.4549 0.2595 0.0264  0.0179  0.0439  255 ASP A OD2 
3961  N N   . VAL A 256 ? 0.1641 0.1481 0.1762 0.0277  0.0173  0.0076  256 VAL A N   
3962  C CA  . VAL A 256 ? 0.1680 0.1634 0.1702 0.0163  0.0194  -0.0073 256 VAL A CA  
3963  C C   . VAL A 256 ? 0.1492 0.1811 0.1747 0.0226  0.0269  0.0177  256 VAL A C   
3964  O O   . VAL A 256 ? 0.1708 0.1947 0.1746 0.0170  0.0437  -0.0063 256 VAL A O   
3965  C CB  . VAL A 256 ? 0.1308 0.1317 0.1786 0.0259  0.0080  -0.0141 256 VAL A CB  
3966  C CG1 . VAL A 256 ? 0.1737 0.1742 0.1831 -0.0132 -0.0034 -0.0199 256 VAL A CG1 
3967  C CG2 . VAL A 256 ? 0.1782 0.1739 0.1899 0.0227  -0.0273 0.0141  256 VAL A CG2 
3977  N N   . LEU A 257 ? 0.1338 0.1659 0.1691 0.0092  0.0173  0.0258  257 LEU A N   
3978  C CA  . LEU A 257 ? 0.1526 0.1399 0.1763 0.0078  0.0152  0.0146  257 LEU A CA  
3979  C C   . LEU A 257 ? 0.1557 0.1517 0.1766 0.0070  0.0022  0.0067  257 LEU A C   
3980  O O   . LEU A 257 ? 0.1306 0.1547 0.1953 -0.0014 -0.0063 -0.0011 257 LEU A O   
3981  C CB  . LEU A 257 ? 0.1398 0.1450 0.1974 0.0023  0.0120  0.0111  257 LEU A CB  
3982  C CG  . LEU A 257 ? 0.1467 0.1704 0.2059 0.0251  0.0241  0.0192  257 LEU A CG  
3983  C CD1 . LEU A 257 ? 0.1889 0.2352 0.2226 -0.0278 0.0267  0.0391  257 LEU A CD1 
3984  C CD2 . LEU A 257 ? 0.1824 0.1384 0.2208 0.0228  0.0307  0.0024  257 LEU A CD2 
3996  N N   . LEU A 258 ? 0.1747 0.1599 0.1734 0.0166  0.0052  0.0157  258 LEU A N   
3997  C CA  . LEU A 258 ? 0.1738 0.1563 0.1670 0.0038  -0.0055 -0.0079 258 LEU A CA  
3998  C C   . LEU A 258 ? 0.1485 0.1161 0.1701 -0.0076 0.0173  -0.0098 258 LEU A C   
3999  O O   . LEU A 258 ? 0.1690 0.1454 0.1881 0.0048  -0.0128 -0.0083 258 LEU A O   
4000  C CB  . LEU A 258 ? 0.1649 0.1424 0.1629 0.0002  0.0081  -0.0269 258 LEU A CB  
4001  C CG  . LEU A 258 ? 0.1952 0.2467 0.1747 0.0151  0.0437  -0.0343 258 LEU A CG  
4002  C CD1 . LEU A 258 ? 0.1842 0.2462 0.2032 -0.0011 0.0291  -0.0242 258 LEU A CD1 
4003  C CD2 . LEU A 258 ? 0.2041 0.3070 0.1675 0.0207  0.0578  -0.0235 258 LEU A CD2 
4015  N N   . ILE A 259 ? 0.1459 0.1470 0.1705 0.0070  -0.0018 -0.0067 259 ILE A N   
4016  C CA  . ILE A 259 ? 0.1454 0.1326 0.1581 -0.0268 -0.0099 -0.0115 259 ILE A CA  
4017  C C   . ILE A 259 ? 0.1817 0.1374 0.1608 -0.0213 -0.0108 0.0065  259 ILE A C   
4018  O O   . ILE A 259 ? 0.1454 0.1341 0.1800 -0.0001 0.0054  -0.0163 259 ILE A O   
4019  C CB  . ILE A 259 ? 0.1561 0.1756 0.1541 -0.0432 0.0304  0.0031  259 ILE A CB  
4020  C CG1 . ILE A 259 ? 0.1422 0.2062 0.1640 -0.0151 -0.0048 -0.0258 259 ILE A CG1 
4021  C CG2 . ILE A 259 ? 0.1833 0.1730 0.1637 -0.0843 0.0117  -0.0221 259 ILE A CG2 
4022  C CD1 . ILE A 259 ? 0.1498 0.2347 0.1748 -0.0083 -0.0142 0.0025  259 ILE A CD1 
4034  N N   . ALA A 260 ? 0.1276 0.1397 0.1476 -0.0050 -0.0073 0.0065  260 ALA A N   
4035  C CA  . ALA A 260 ? 0.1353 0.1060 0.1478 0.0082  -0.0063 0.0059  260 ALA A CA  
4036  C C   . ALA A 260 ? 0.2008 0.1154 0.1523 0.0024  -0.0100 -0.0153 260 ALA A C   
4037  O O   . ALA A 260 ? 0.1620 0.1228 0.1605 -0.0085 -0.0103 0.0005  260 ALA A O   
4038  C CB  . ALA A 260 ? 0.1816 0.1601 0.1277 -0.0039 0.0078  0.0259  260 ALA A CB  
4044  N N   . ASP A 261 ? 0.1686 0.1061 0.1547 -0.0106 -0.0066 0.0063  261 ASP A N   
4045  C CA  . ASP A 261 ? 0.1212 0.1569 0.1531 -0.0187 -0.0028 0.0083  261 ASP A CA  
4046  C C   . ASP A 261 ? 0.1356 0.1738 0.1538 -0.0236 -0.0146 0.0057  261 ASP A C   
4047  O O   . ASP A 261 ? 0.1457 0.1478 0.1539 -0.0035 -0.0008 0.0185  261 ASP A O   
4048  C CB  . ASP A 261 ? 0.1264 0.1735 0.1481 -0.0026 -0.0027 0.0045  261 ASP A CB  
4049  C CG  . ASP A 261 ? 0.1495 0.1513 0.1551 0.0083  -0.0028 -0.0103 261 ASP A CG  
4050  O OD1 . ASP A 261 ? 0.1755 0.1856 0.1500 0.0124  0.0207  -0.0050 261 ASP A OD1 
4051  O OD2 . ASP A 261 ? 0.1618 0.1641 0.1577 0.0249  0.0157  -0.0260 261 ASP A OD2 
4056  N N   . GLU A 262 ? 0.1186 0.1081 0.1510 -0.0126 -0.0165 -0.0080 262 GLU A N   
4057  C CA  . GLU A 262 ? 0.1375 0.1340 0.1496 -0.0155 -0.0168 -0.0250 262 GLU A CA  
4058  C C   . GLU A 262 ? 0.1318 0.1391 0.1537 -0.0186 -0.0174 -0.0247 262 GLU A C   
4059  O O   . GLU A 262 ? 0.1874 0.1160 0.1658 -0.0300 -0.0059 -0.0213 262 GLU A O   
4060  C CB  . GLU A 262 ? 0.1607 0.1840 0.1555 -0.0032 -0.0142 -0.0227 262 GLU A CB  
4061  C CG  . GLU A 262 ? 0.1785 0.1887 0.1494 -0.0026 -0.0133 -0.0108 262 GLU A CG  
4062  C CD  . GLU A 262 ? 0.2007 0.1569 0.1598 0.0067  -0.0027 -0.0011 262 GLU A CD  
4063  O OE1 . GLU A 262 ? 0.1943 0.1671 0.1621 0.0179  -0.0190 -0.0134 262 GLU A OE1 
4064  O OE2 . GLU A 262 ? 0.1722 0.1801 0.1637 -0.0015 -0.0005 0.0091  262 GLU A OE2 
4071  N N   . VAL A 263 ? 0.1415 0.1746 0.1562 0.0059  -0.0047 -0.0128 263 VAL A N   
4072  C CA  . VAL A 263 ? 0.1481 0.1230 0.1565 -0.0406 0.0120  0.0007  263 VAL A CA  
4073  C C   . VAL A 263 ? 0.1576 0.1551 0.1576 -0.0192 0.0034  -0.0181 263 VAL A C   
4074  O O   . VAL A 263 ? 0.1721 0.1612 0.1749 0.0053  -0.0075 -0.0116 263 VAL A O   
4075  C CB  . VAL A 263 ? 0.1646 0.0983 0.1547 -0.0096 0.0232  -0.0053 263 VAL A CB  
4076  C CG1 . VAL A 263 ? 0.1978 0.1441 0.1584 -0.0302 0.0296  0.0336  263 VAL A CG1 
4077  C CG2 . VAL A 263 ? 0.1609 0.1384 0.1270 -0.0253 0.0289  -0.0054 263 VAL A CG2 
4087  N N   . VAL A 264 ? 0.1797 0.1316 0.1543 0.0102  0.0025  -0.0094 264 VAL A N   
4088  C CA  . VAL A 264 ? 0.1750 0.1024 0.1660 0.0010  -0.0008 -0.0012 264 VAL A CA  
4089  C C   . VAL A 264 ? 0.1782 0.1415 0.1767 -0.0128 0.0155  0.0039  264 VAL A C   
4090  O O   . VAL A 264 ? 0.2149 0.1244 0.1858 0.0028  0.0096  0.0071  264 VAL A O   
4091  C CB  . VAL A 264 ? 0.2062 0.1522 0.1728 -0.0118 0.0302  -0.0086 264 VAL A CB  
4092  C CG1 . VAL A 264 ? 0.2199 0.1395 0.1670 -0.0793 0.0174  0.0128  264 VAL A CG1 
4093  C CG2 . VAL A 264 ? 0.1786 0.1762 0.1802 -0.0050 0.0108  -0.0212 264 VAL A CG2 
4103  N N   . CYS A 265 ? 0.1459 0.1744 0.1707 0.0038  0.0278  0.0063  265 CYS A N   
4104  C CA  . CYS A 265 ? 0.1745 0.2097 0.1736 -0.0213 0.0419  -0.0030 265 CYS A CA  
4105  C C   . CYS A 265 ? 0.2147 0.1747 0.1661 -0.0256 0.0208  -0.0129 265 CYS A C   
4106  O O   . CYS A 265 ? 0.2267 0.1970 0.1783 -0.0225 0.0177  -0.0319 265 CYS A O   
4107  C CB  . CYS A 265 ? 0.1655 0.1763 0.1964 -0.0639 0.0432  0.0068  265 CYS A CB  
4108  S SG  . CYS A 265 ? 0.1964 0.1941 0.2223 -0.0219 0.0114  0.0172  265 CYS A SG  
4114  N N   . GLY A 266 ? 0.1966 0.1602 0.1712 -0.0180 0.0017  0.0072  266 GLY A N   
4115  C CA  . GLY A 266 ? 0.2026 0.1931 0.1630 -0.0019 0.0029  0.0044  266 GLY A CA  
4116  C C   . GLY A 266 ? 0.1600 0.2117 0.1648 0.0116  -0.0192 -0.0150 266 GLY A C   
4117  O O   . GLY A 266 ? 0.1912 0.1650 0.1651 0.0097  -0.0210 -0.0141 266 GLY A O   
4121  N N   . PHE A 267 ? 0.1522 0.2117 0.1596 0.0185  -0.0187 -0.0079 267 PHE A N   
4122  C CA  . PHE A 267 ? 0.1715 0.1787 0.1725 -0.0216 -0.0169 -0.0115 267 PHE A CA  
4123  C C   . PHE A 267 ? 0.1754 0.1714 0.1728 -0.0387 0.0223  0.0028  267 PHE A C   
4124  O O   . PHE A 267 ? 0.2348 0.1557 0.1748 -0.0197 0.0135  -0.0007 267 PHE A O   
4125  C CB  . PHE A 267 ? 0.2200 0.2028 0.1830 -0.0110 -0.0228 0.0010  267 PHE A CB  
4126  C CG  . PHE A 267 ? 0.1824 0.1738 0.1654 -0.0259 0.0024  -0.0120 267 PHE A CG  
4127  C CD1 . PHE A 267 ? 0.1836 0.1894 0.1705 -0.0627 0.0296  -0.0453 267 PHE A CD1 
4128  C CD2 . PHE A 267 ? 0.2197 0.1425 0.1578 0.0042  0.0076  -0.0117 267 PHE A CD2 
4129  C CE1 . PHE A 267 ? 0.1868 0.2166 0.1738 -0.0266 0.0020  -0.0381 267 PHE A CE1 
4130  C CE2 . PHE A 267 ? 0.2176 0.1712 0.1528 -0.0295 0.0015  0.0051  267 PHE A CE2 
4131  C CZ  . PHE A 267 ? 0.1930 0.2179 0.1636 -0.0120 -0.0086 -0.0077 267 PHE A CZ  
4141  N N   . GLY A 268 ? 0.1788 0.1298 0.1694 -0.0173 0.0334  -0.0085 268 GLY A N   
4142  C CA  . GLY A 268 ? 0.1987 0.1754 0.1668 -0.0119 0.0401  -0.0161 268 GLY A CA  
4143  C C   . GLY A 268 ? 0.1787 0.1801 0.1683 -0.0088 0.0189  -0.0114 268 GLY A C   
4144  O O   . GLY A 268 ? 0.1973 0.2346 0.1610 -0.0128 0.0316  0.0036  268 GLY A O   
4148  N N   . ARG A 269 ? 0.1796 0.1687 0.1723 -0.0187 -0.0017 -0.0235 269 ARG A N   
4149  C CA  . ARG A 269 ? 0.1939 0.1556 0.1723 -0.0120 0.0219  0.0256  269 ARG A CA  
4150  C C   . ARG A 269 ? 0.1916 0.1715 0.1820 0.0033  0.0288  -0.0043 269 ARG A C   
4151  O O   . ARG A 269 ? 0.1901 0.2018 0.1959 -0.0264 0.0327  -0.0156 269 ARG A O   
4152  C CB  . ARG A 269 ? 0.1928 0.1706 0.1860 0.0129  0.0268  0.0066  269 ARG A CB  
4153  C CG  . ARG A 269 ? 0.1326 0.1643 0.1845 0.0049  0.0147  0.0115  269 ARG A CG  
4154  C CD  . ARG A 269 ? 0.1830 0.1411 0.1942 -0.0085 0.0126  0.0055  269 ARG A CD  
4155  N NE  . ARG A 269 ? 0.1647 0.1348 0.1938 -0.0115 -0.0006 0.0005  269 ARG A NE  
4156  C CZ  . ARG A 269 ? 0.1955 0.1356 0.1892 0.0053  0.0165  -0.0035 269 ARG A CZ  
4157  N NH1 . ARG A 269 ? 0.1792 0.1616 0.1657 0.0134  0.0492  0.0085  269 ARG A NH1 
4158  N NH2 . ARG A 269 ? 0.2208 0.1490 0.2049 -0.0069 0.0212  -0.0277 269 ARG A NH2 
4172  N N   . ILE A 270 ? 0.1716 0.1812 0.1546 0.0088  0.0112  0.0150  270 ILE A N   
4173  C CA  . ILE A 270 ? 0.1901 0.1902 0.1660 0.0101  0.0168  -0.0095 270 ILE A CA  
4174  C C   . ILE A 270 ? 0.2440 0.2138 0.1736 0.0214  0.0005  -0.0078 270 ILE A C   
4175  O O   . ILE A 270 ? 0.2766 0.1574 0.1660 0.0125  0.0013  0.0048  270 ILE A O   
4176  C CB  . ILE A 270 ? 0.1557 0.1958 0.1794 0.0146  0.0436  -0.0006 270 ILE A CB  
4177  C CG1 . ILE A 270 ? 0.2208 0.1596 0.1972 -0.0308 0.0238  0.0131  270 ILE A CG1 
4178  C CG2 . ILE A 270 ? 0.1893 0.1758 0.1800 -0.0272 0.0211  -0.0183 270 ILE A CG2 
4179  C CD1 . ILE A 270 ? 0.1492 0.2086 0.1987 -0.0215 0.0201  0.0308  270 ILE A CD1 
4191  N N   . GLY A 271 ? 0.2182 0.1984 0.1881 0.0252  0.0189  -0.0321 271 GLY A N   
4192  C CA  . GLY A 271 ? 0.1766 0.1769 0.1872 -0.0036 0.0339  -0.0452 271 GLY A CA  
4193  C C   . GLY A 271 ? 0.2307 0.1801 0.1932 -0.0140 0.0373  -0.0450 271 GLY A C   
4194  O O   . GLY A 271 ? 0.2844 0.1956 0.2016 0.0103  0.0254  -0.0464 271 GLY A O   
4198  N N   . ALA A 272 ? 0.2047 0.2177 0.2101 0.0244  0.0294  -0.0390 272 ALA A N   
4199  C CA  . ALA A 272 ? 0.1771 0.2145 0.2110 0.0180  0.0369  -0.0056 272 ALA A CA  
4200  C C   . ALA A 272 ? 0.1901 0.1870 0.1889 -0.0476 0.0148  -0.0032 272 ALA A C   
4201  O O   . ALA A 272 ? 0.2160 0.2382 0.1890 -0.0003 -0.0032 -0.0067 272 ALA A O   
4202  C CB  . ALA A 272 ? 0.2649 0.2705 0.2221 0.0483  0.0312  0.0183  272 ALA A CB  
4208  N N   . ASP A 273 ? 0.2343 0.1855 0.1891 -0.0108 0.0024  -0.0156 273 ASP A N   
4209  C CA  . ASP A 273 ? 0.2449 0.1972 0.1983 -0.0360 -0.0053 -0.0207 273 ASP A CA  
4210  C C   . ASP A 273 ? 0.2061 0.1601 0.1797 -0.0105 -0.0019 -0.0200 273 ASP A C   
4211  O O   . ASP A 273 ? 0.2349 0.1640 0.1679 -0.0136 -0.0183 0.0063  273 ASP A O   
4212  C CB  . ASP A 273 ? 0.2183 0.2429 0.2269 -0.0441 -0.0354 -0.0568 273 ASP A CB  
4213  C CG  . ASP A 273 ? 0.2766 0.2303 0.2603 -0.0112 -0.0430 -0.0667 273 ASP A CG  
4214  O OD1 . ASP A 273 ? 0.3475 0.2285 0.2962 -0.0126 -0.0274 -0.0630 273 ASP A OD1 
4215  O OD2 . ASP A 273 ? 0.3159 0.2849 0.2562 0.0304  -0.0490 -0.0676 273 ASP A OD2 
4220  N N   . PHE A 274 ? 0.2014 0.1626 0.1671 -0.0191 -0.0091 0.0007  274 PHE A N   
4221  C CA  . PHE A 274 ? 0.1790 0.1619 0.1770 -0.0006 0.0000  0.0163  274 PHE A CA  
4222  C C   . PHE A 274 ? 0.1627 0.1869 0.1757 -0.0097 0.0014  -0.0011 274 PHE A C   
4223  O O   . PHE A 274 ? 0.2010 0.1649 0.1700 0.0153  0.0176  0.0091  274 PHE A O   
4224  C CB  . PHE A 274 ? 0.1842 0.1448 0.1676 -0.0115 -0.0030 0.0130  274 PHE A CB  
4225  C CG  . PHE A 274 ? 0.1446 0.1783 0.1815 -0.0380 0.0119  0.0018  274 PHE A CG  
4226  C CD1 . PHE A 274 ? 0.1431 0.2139 0.1765 -0.0160 0.0273  0.0008  274 PHE A CD1 
4227  C CD2 . PHE A 274 ? 0.1694 0.1861 0.1860 -0.0173 0.0030  0.0028  274 PHE A CD2 
4228  C CE1 . PHE A 274 ? 0.1266 0.2660 0.1864 -0.0292 -0.0033 0.0072  274 PHE A CE1 
4229  C CE2 . PHE A 274 ? 0.1999 0.2144 0.1952 -0.0197 -0.0060 -0.0053 274 PHE A CE2 
4230  C CZ  . PHE A 274 ? 0.1823 0.2483 0.1979 -0.0309 -0.0018 0.0111  274 PHE A CZ  
4240  N N   . GLY A 275 ? 0.1663 0.1799 0.1704 -0.0271 0.0013  -0.0142 275 GLY A N   
4241  C CA  . GLY A 275 ? 0.1829 0.1893 0.1782 -0.0037 -0.0176 0.0058  275 GLY A CA  
4242  C C   . GLY A 275 ? 0.1719 0.1739 0.1733 -0.0535 -0.0011 0.0093  275 GLY A C   
4243  O O   . GLY A 275 ? 0.1492 0.2039 0.1716 -0.0338 0.0157  0.0111  275 GLY A O   
4247  N N   . SER A 276 ? 0.2005 0.1590 0.1717 -0.0346 0.0043  -0.0122 276 SER A N   
4248  C CA  . SER A 276 ? 0.1723 0.1996 0.1588 -0.0275 0.0143  -0.0123 276 SER A CA  
4249  C C   . SER A 276 ? 0.2067 0.2190 0.1644 -0.0380 0.0189  -0.0031 276 SER A C   
4250  O O   . SER A 276 ? 0.2171 0.1574 0.1729 -0.0111 0.0077  0.0204  276 SER A O   
4251  C CB  . SER A 276 ? 0.1826 0.2054 0.1651 -0.0349 0.0113  0.0104  276 SER A CB  
4252  O OG  . SER A 276 ? 0.1971 0.2137 0.1656 -0.0254 0.0143  0.0063  276 SER A OG  
4258  N N   . HIS A 277 ? 0.2221 0.2419 0.1639 -0.0036 0.0141  -0.0109 277 HIS A N   
4259  C CA  . HIS A 277 ? 0.2108 0.1569 0.1644 -0.0067 -0.0009 -0.0281 277 HIS A CA  
4260  C C   . HIS A 277 ? 0.2256 0.1913 0.1655 -0.0200 0.0259  -0.0072 277 HIS A C   
4261  O O   . HIS A 277 ? 0.2606 0.2577 0.1746 -0.0782 0.0232  -0.0167 277 HIS A O   
4262  C CB  . HIS A 277 ? 0.2416 0.1636 0.1748 -0.0164 0.0039  -0.0242 277 HIS A CB  
4263  C CG  . HIS A 277 ? 0.2147 0.2390 0.1827 -0.0478 -0.0007 -0.0165 277 HIS A CG  
4264  N ND1 . HIS A 277 ? 0.2496 0.2622 0.1897 -0.0568 -0.0036 -0.0120 277 HIS A ND1 
4265  C CD2 . HIS A 277 ? 0.1984 0.2455 0.1862 -0.0521 0.0033  0.0077  277 HIS A CD2 
4266  C CE1 . HIS A 277 ? 0.2493 0.3180 0.1904 -0.0554 -0.0082 -0.0080 277 HIS A CE1 
4267  N NE2 . HIS A 277 ? 0.2208 0.2930 0.1948 -0.0298 0.0020  0.0096  277 HIS A NE2 
4275  N N   . HIS A 278 ? 0.1973 0.1877 0.1685 -0.0068 0.0223  -0.0007 278 HIS A N   
4276  C CA  . HIS A 278 ? 0.2316 0.2092 0.1654 -0.0056 0.0242  0.0039  278 HIS A CA  
4277  C C   . HIS A 278 ? 0.2365 0.2184 0.1539 -0.0111 0.0240  -0.0081 278 HIS A C   
4278  O O   . HIS A 278 ? 0.2386 0.2608 0.1790 0.0320  0.0283  0.0020  278 HIS A O   
4279  C CB  . HIS A 278 ? 0.2242 0.2169 0.1941 0.0082  0.0132  0.0143  278 HIS A CB  
4280  C CG  . HIS A 278 ? 0.2168 0.2329 0.2243 0.0147  0.0127  -0.0235 278 HIS A CG  
4281  N ND1 . HIS A 278 ? 0.2653 0.3050 0.2579 0.0353  0.0358  -0.0580 278 HIS A ND1 
4282  C CD2 . HIS A 278 ? 0.2407 0.2839 0.2366 0.0257  0.0196  -0.0512 278 HIS A CD2 
4283  C CE1 . HIS A 278 ? 0.2916 0.3324 0.2655 0.0156  0.0326  -0.0823 278 HIS A CE1 
4284  N NE2 . HIS A 278 ? 0.2562 0.3372 0.2440 0.0397  0.0097  -0.0896 278 HIS A NE2 
4292  N N   . TYR A 279 ? 0.2029 0.2283 0.1393 -0.0182 0.0085  -0.0228 279 TYR A N   
4293  C CA  . TYR A 279 ? 0.1833 0.2365 0.1480 -0.0134 -0.0029 0.0019  279 TYR A CA  
4294  C C   . TYR A 279 ? 0.2139 0.2028 0.1510 -0.0237 -0.0092 0.0061  279 TYR A C   
4295  O O   . TYR A 279 ? 0.1948 0.1970 0.1681 -0.0089 0.0010  0.0059  279 TYR A O   
4296  C CB  . TYR A 279 ? 0.1730 0.2136 0.1677 -0.0057 0.0019  -0.0222 279 TYR A CB  
4297  C CG  . TYR A 279 ? 0.1447 0.2383 0.1661 -0.0185 -0.0020 -0.0026 279 TYR A CG  
4298  C CD1 . TYR A 279 ? 0.1326 0.2525 0.1739 0.0002  0.0111  0.0109  279 TYR A CD1 
4299  C CD2 . TYR A 279 ? 0.1907 0.2367 0.1667 -0.0201 -0.0189 -0.0278 279 TYR A CD2 
4300  C CE1 . TYR A 279 ? 0.1658 0.2421 0.1866 -0.0464 0.0042  0.0139  279 TYR A CE1 
4301  C CE2 . TYR A 279 ? 0.1753 0.2129 0.1785 -0.0080 0.0135  -0.0182 279 TYR A CE2 
4302  C CZ  . TYR A 279 ? 0.2069 0.2140 0.1940 0.0040  0.0018  0.0021  279 TYR A CZ  
4303  O OH  . TYR A 279 ? 0.2522 0.1772 0.2123 0.0419  -0.0338 -0.0167 279 TYR A OH  
4313  N N   . ALA A 280 ? 0.2035 0.1843 0.1371 0.0074  -0.0028 -0.0008 280 ALA A N   
4314  C CA  . ALA A 280 ? 0.2147 0.1929 0.1368 0.0020  -0.0117 -0.0002 280 ALA A CA  
4315  C C   . ALA A 280 ? 0.2159 0.2011 0.1524 0.0014  -0.0087 0.0089  280 ALA A C   
4316  O O   . ALA A 280 ? 0.2434 0.2001 0.1567 -0.0009 0.0116  0.0210  280 ALA A O   
4317  C CB  . ALA A 280 ? 0.2230 0.2219 0.1448 -0.0021 -0.0204 -0.0010 280 ALA A CB  
4323  N N   . ILE A 281 ? 0.1650 0.1798 0.1485 -0.0071 -0.0034 -0.0061 281 ILE A N   
4324  C CA  . ILE A 281 ? 0.1711 0.1757 0.1639 -0.0089 0.0110  -0.0125 281 ILE A CA  
4325  C C   . ILE A 281 ? 0.1456 0.1792 0.1661 -0.0021 0.0203  -0.0049 281 ILE A C   
4326  O O   . ILE A 281 ? 0.1870 0.2088 0.1705 -0.0252 0.0149  0.0351  281 ILE A O   
4327  C CB  . ILE A 281 ? 0.1784 0.1649 0.1634 -0.0116 0.0056  -0.0166 281 ILE A CB  
4328  C CG1 . ILE A 281 ? 0.1828 0.1448 0.1665 -0.0290 -0.0023 -0.0043 281 ILE A CG1 
4329  C CG2 . ILE A 281 ? 0.2078 0.1997 0.1722 0.0209  0.0286  -0.0028 281 ILE A CG2 
4330  C CD1 . ILE A 281 ? 0.1822 0.1421 0.1701 0.0045  0.0198  0.0006  281 ILE A CD1 
4342  N N   . LYS A 282 ? 0.1647 0.1935 0.1769 -0.0284 0.0122  0.0161  282 LYS A N   
4343  C CA  . LYS A 282 ? 0.1469 0.2345 0.1704 -0.0081 0.0081  0.0208  282 LYS A CA  
4344  C C   . LYS A 282 ? 0.1558 0.1831 0.1637 0.0164  0.0076  0.0148  282 LYS A C   
4345  O O   . LYS A 282 ? 0.1825 0.2179 0.1722 -0.0077 0.0014  0.0309  282 LYS A O   
4346  C CB  . LYS A 282 ? 0.2323 0.2927 0.1841 0.0069  -0.0044 0.0260  282 LYS A CB  
4347  C CG  . LYS A 282 ? 0.3640 0.3710 0.2256 0.0328  -0.0033 -0.0039 282 LYS A CG  
4348  C CD  . LYS A 282 ? 0.5775 0.4513 0.2754 0.0793  -0.0019 0.0029  282 LYS A CD  
4349  C CE  . LYS A 282 ? 0.7374 0.4918 0.3347 0.0804  -0.0043 -0.0298 282 LYS A CE  
4350  N NZ  . LYS A 282 ? 0.8314 0.5443 0.3697 0.0402  -0.0064 -0.0433 282 LYS A NZ  
4364  N N   . PRO A 283 ? 0.1795 0.1669 0.1582 -0.0426 0.0401  0.0224  283 PRO A N   
4365  C CA  . PRO A 283 ? 0.1603 0.1946 0.1470 -0.0199 0.0169  0.0204  283 PRO A CA  
4366  C C   . PRO A 283 ? 0.1527 0.1595 0.1457 -0.0424 -0.0008 0.0122  283 PRO A C   
4367  O O   . PRO A 283 ? 0.1784 0.1610 0.1664 -0.0253 -0.0120 0.0026  283 PRO A O   
4368  C CB  . PRO A 283 ? 0.1789 0.1979 0.1712 -0.0111 -0.0023 0.0221  283 PRO A CB  
4369  C CG  . PRO A 283 ? 0.2320 0.1703 0.1637 -0.0215 0.0138  0.0332  283 PRO A CG  
4370  C CD  . PRO A 283 ? 0.2244 0.1696 0.1599 -0.0066 0.0098  0.0170  283 PRO A CD  
4378  N N   . ASP A 284 ? 0.1835 0.1736 0.1402 0.0064  -0.0111 -0.0112 284 ASP A N   
4379  C CA  . ASP A 284 ? 0.1331 0.1763 0.1521 -0.0209 -0.0131 -0.0021 284 ASP A CA  
4380  C C   . ASP A 284 ? 0.1203 0.1375 0.1701 -0.0062 -0.0086 0.0026  284 ASP A C   
4381  O O   . ASP A 284 ? 0.1244 0.2004 0.1813 -0.0219 -0.0262 -0.0111 284 ASP A O   
4382  C CB  . ASP A 284 ? 0.1867 0.1701 0.1741 -0.0090 -0.0174 0.0231  284 ASP A CB  
4383  C CG  . ASP A 284 ? 0.2410 0.1702 0.1931 -0.0082 -0.0531 0.0349  284 ASP A CG  
4384  O OD1 . ASP A 284 ? 0.2829 0.2669 0.2535 -0.0402 -0.1104 0.0504  284 ASP A OD1 
4385  O OD2 . ASP A 284 ? 0.2261 0.1800 0.1902 0.0013  -0.0354 0.0215  284 ASP A OD2 
4390  N N   . LEU A 285 ? 0.1259 0.1922 0.1709 -0.0030 0.0199  0.0201  285 LEU A N   
4391  C CA  . LEU A 285 ? 0.1279 0.1653 0.1688 -0.0149 0.0152  -0.0012 285 LEU A CA  
4392  C C   . LEU A 285 ? 0.1351 0.1393 0.1619 -0.0385 -0.0092 -0.0009 285 LEU A C   
4393  O O   . LEU A 285 ? 0.1368 0.1576 0.1586 -0.0424 -0.0133 0.0130  285 LEU A O   
4394  C CB  . LEU A 285 ? 0.1552 0.1264 0.1762 -0.0070 0.0053  -0.0231 285 LEU A CB  
4395  C CG  . LEU A 285 ? 0.1624 0.1532 0.1786 -0.0154 0.0026  -0.0385 285 LEU A CG  
4396  C CD1 . LEU A 285 ? 0.2078 0.1530 0.1862 0.0161  -0.0137 -0.0452 285 LEU A CD1 
4397  C CD2 . LEU A 285 ? 0.1133 0.2092 0.1898 -0.0338 0.0014  -0.0223 285 LEU A CD2 
4409  N N   . ILE A 286 ? 0.1462 0.1192 0.1707 -0.0144 0.0047  0.0046  286 ILE A N   
4410  C CA  . ILE A 286 ? 0.1325 0.1539 0.1534 -0.0175 -0.0024 0.0106  286 ILE A CA  
4411  C C   . ILE A 286 ? 0.1173 0.1519 0.1461 0.0275  0.0076  0.0095  286 ILE A C   
4412  O O   . ILE A 286 ? 0.1412 0.1753 0.1328 -0.0142 0.0253  0.0009  286 ILE A O   
4413  C CB  . ILE A 286 ? 0.1340 0.1682 0.1479 0.0149  -0.0080 0.0129  286 ILE A CB  
4414  C CG1 . ILE A 286 ? 0.1596 0.1766 0.1306 -0.0346 -0.0327 0.0006  286 ILE A CG1 
4415  C CG2 . ILE A 286 ? 0.1258 0.2267 0.1616 -0.0015 0.0248  -0.0153 286 ILE A CG2 
4416  C CD1 . ILE A 286 ? 0.1772 0.1959 0.1189 -0.0086 -0.0284 -0.0213 286 ILE A CD1 
4428  N N   . THR A 287 ? 0.1536 0.1455 0.1512 -0.0171 0.0030  0.0008  287 THR A N   
4429  C CA  . THR A 287 ? 0.1475 0.0994 0.1396 -0.0167 -0.0076 -0.0032 287 THR A CA  
4430  C C   . THR A 287 ? 0.1554 0.1326 0.1391 -0.0014 0.0168  -0.0055 287 THR A C   
4431  O O   . THR A 287 ? 0.1246 0.1743 0.1416 -0.0277 0.0072  0.0026  287 THR A O   
4432  C CB  . THR A 287 ? 0.1116 0.1310 0.1470 0.0095  -0.0004 0.0170  287 THR A CB  
4433  O OG1 . THR A 287 ? 0.1670 0.1726 0.1558 -0.0112 -0.0266 -0.0096 287 THR A OG1 
4434  C CG2 . THR A 287 ? 0.1414 0.1757 0.1547 -0.0019 -0.0017 0.0079  287 THR A CG2 
4442  N N   . ILE A 288 ? 0.1716 0.1407 0.1426 -0.0032 -0.0044 0.0110  288 ILE A N   
4443  C CA  . ILE A 288 ? 0.1806 0.1159 0.1406 -0.0528 -0.0051 -0.0135 288 ILE A CA  
4444  C C   . ILE A 288 ? 0.2135 0.1434 0.1506 -0.0392 -0.0112 -0.0178 288 ILE A C   
4445  O O   . ILE A 288 ? 0.1627 0.1581 0.1600 -0.0102 0.0067  0.0181  288 ILE A O   
4446  C CB  . ILE A 288 ? 0.1753 0.1149 0.1557 -0.0459 0.0235  -0.0076 288 ILE A CB  
4447  C CG1 . ILE A 288 ? 0.1705 0.1441 0.1695 -0.0685 0.0072  -0.0012 288 ILE A CG1 
4448  C CG2 . ILE A 288 ? 0.2400 0.1156 0.1563 -0.0753 0.0119  -0.0313 288 ILE A CG2 
4449  C CD1 . ILE A 288 ? 0.1806 0.1797 0.1721 -0.0471 0.0051  -0.0010 288 ILE A CD1 
4461  N N   . ALA A 289 ? 0.1909 0.1344 0.1574 -0.0324 -0.0106 -0.0115 289 ALA A N   
4462  C CA  . ALA A 289 ? 0.1839 0.1376 0.1724 -0.0061 0.0077  0.0125  289 ALA A CA  
4463  C C   . ALA A 289 ? 0.1759 0.1586 0.1946 0.0291  0.0223  0.0399  289 ALA A C   
4464  O O   . ALA A 289 ? 0.2058 0.1769 0.1911 0.0085  0.0144  0.0353  289 ALA A O   
4465  C CB  . ALA A 289 ? 0.2092 0.1626 0.1810 0.0059  0.0071  0.0579  289 ALA A CB  
4486  N N   . LLP A 290 ? 0.1460 0.1465 0.2151 0.0216  0.0189  0.0561  290 LLP A N   
4487  C CA  . LLP A 290 ? 0.1742 0.1615 0.2419 -0.0118 0.0243  0.0443  290 LLP A CA  
4488  C CB  . LLP A 290 ? 0.1892 0.1890 0.2864 -0.0077 0.0513  0.0564  290 LLP A CB  
4489  C CG  . LLP A 290 ? 0.1556 0.1930 0.3539 0.0305  0.0535  0.0738  290 LLP A CG  
4490  C CD  . LLP A 290 ? 0.1976 0.2550 0.4433 0.0711  0.1243  0.1056  290 LLP A CD  
4491  C CE  . LLP A 290 ? 0.3313 0.3844 0.5680 0.1158  0.1856  0.0996  290 LLP A CE  
4492  N NZ  . LLP A 290 ? 0.5446 0.5694 0.7145 0.0452  0.1597  0.1338  290 LLP A NZ  
4493  C C   . LLP A 290 ? 0.1876 0.1870 0.2323 -0.0047 0.0251  0.0327  290 LLP A C   
4494  O O   . LLP A 290 ? 0.2060 0.1902 0.2396 -0.0056 0.0379  0.0201  290 LLP A O   
4514  N N   . GLY A 291 ? 0.1860 0.1745 0.2318 0.0033  0.0314  0.0017  291 GLY A N   
4515  C CA  . GLY A 291 ? 0.1755 0.1640 0.2285 0.0176  0.0456  0.0049  291 GLY A CA  
4516  C C   . GLY A 291 ? 0.1990 0.1769 0.2152 -0.0084 0.0489  0.0093  291 GLY A C   
4517  O O   . GLY A 291 ? 0.2001 0.1801 0.2237 -0.0233 0.0272  0.0174  291 GLY A O   
4521  N N   . LEU A 292 ? 0.2018 0.1348 0.2078 -0.0087 0.0504  0.0217  292 LEU A N   
4522  C CA  . LEU A 292 ? 0.2110 0.1261 0.2040 -0.0076 0.0574  0.0025  292 LEU A CA  
4523  C C   . LEU A 292 ? 0.2151 0.1589 0.1943 -0.0155 0.0143  0.0004  292 LEU A C   
4524  O O   . LEU A 292 ? 0.1802 0.1938 0.2060 0.0165  0.0129  -0.0110 292 LEU A O   
4525  C CB  . LEU A 292 ? 0.1640 0.1404 0.2059 -0.0064 0.0533  -0.0026 292 LEU A CB  
4526  C CG  . LEU A 292 ? 0.1873 0.1794 0.2117 -0.0309 0.0459  0.0073  292 LEU A CG  
4527  C CD1 . LEU A 292 ? 0.1609 0.1993 0.2138 -0.0254 -0.0107 -0.0071 292 LEU A CD1 
4528  C CD2 . LEU A 292 ? 0.2064 0.2022 0.2180 -0.0087 0.0464  0.0350  292 LEU A CD2 
4540  N N   . THR A 293 ? 0.1885 0.1665 0.1913 0.0097  -0.0145 0.0009  293 THR A N   
4541  C CA  . THR A 293 ? 0.1510 0.1601 0.1689 -0.0144 -0.0126 -0.0067 293 THR A CA  
4542  C C   . THR A 293 ? 0.1366 0.1761 0.1687 -0.0164 -0.0085 0.0049  293 THR A C   
4543  O O   . THR A 293 ? 0.1921 0.1521 0.1795 -0.0187 -0.0078 0.0168  293 THR A O   
4544  C CB  . THR A 293 ? 0.1717 0.1571 0.1608 0.0020  -0.0210 0.0013  293 THR A CB  
4545  O OG1 . THR A 293 ? 0.1824 0.2216 0.1647 -0.0025 -0.0201 -0.0180 293 THR A OG1 
4546  C CG2 . THR A 293 ? 0.1839 0.1603 0.1584 -0.0169 0.0179  0.0182  293 THR A CG2 
4554  N N   . SER A 294 ? 0.1577 0.2009 0.1644 0.0205  0.0165  -0.0053 294 SER A N   
4555  C CA  . SER A 294 ? 0.1650 0.1893 0.1624 0.0118  0.0183  0.0040  294 SER A CA  
4556  C C   . SER A 294 ? 0.1582 0.1800 0.1712 0.0083  0.0234  -0.0064 294 SER A C   
4557  O O   . SER A 294 ? 0.1844 0.1999 0.1762 0.0095  0.0120  -0.0054 294 SER A O   
4558  C CB  . SER A 294 ? 0.1619 0.1823 0.1655 -0.0078 0.0256  -0.0210 294 SER A CB  
4559  O OG  . SER A 294 ? 0.1919 0.1894 0.1628 0.0051  0.0198  -0.0224 294 SER A OG  
4565  N N   . ALA A 295 ? 0.1755 0.1585 0.1756 -0.0240 0.0239  -0.0052 295 ALA A N   
4566  C CA  . ALA A 295 ? 0.1999 0.1574 0.1722 -0.0546 -0.0017 -0.0113 295 ALA A CA  
4567  C C   . ALA A 295 ? 0.1844 0.1347 0.1719 -0.0304 -0.0111 -0.0221 295 ALA A C   
4568  O O   . ALA A 295 ? 0.1753 0.1760 0.1712 -0.0164 -0.0199 -0.0071 295 ALA A O   
4569  C CB  . ALA A 295 ? 0.2136 0.1494 0.1773 -0.0666 -0.0173 -0.0201 295 ALA A CB  
4575  N N   . TYR A 296 ? 0.1817 0.1615 0.1698 -0.0314 0.0065  -0.0117 296 TYR A N   
4576  C CA  . TYR A 296 ? 0.1870 0.1752 0.1698 0.0006  0.0010  -0.0118 296 TYR A CA  
4577  C C   . TYR A 296 ? 0.2119 0.1978 0.1752 -0.0311 0.0120  -0.0048 296 TYR A C   
4578  O O   . TYR A 296 ? 0.2088 0.1527 0.1749 -0.0374 0.0192  -0.0141 296 TYR A O   
4579  C CB  . TYR A 296 ? 0.1692 0.1412 0.1881 0.0004  -0.0083 -0.0231 296 TYR A CB  
4580  C CG  . TYR A 296 ? 0.1679 0.1384 0.1886 -0.0248 0.0086  -0.0013 296 TYR A CG  
4581  C CD1 . TYR A 296 ? 0.2144 0.1450 0.2043 -0.0413 0.0115  -0.0084 296 TYR A CD1 
4582  C CD2 . TYR A 296 ? 0.1827 0.1631 0.1710 -0.0305 0.0099  -0.0103 296 TYR A CD2 
4583  C CE1 . TYR A 296 ? 0.2338 0.1428 0.2013 -0.0259 0.0294  -0.0151 296 TYR A CE1 
4584  C CE2 . TYR A 296 ? 0.2078 0.1313 0.1751 -0.0211 0.0010  -0.0152 296 TYR A CE2 
4585  C CZ  . TYR A 296 ? 0.2090 0.1118 0.1960 0.0219  0.0213  -0.0230 296 TYR A CZ  
4586  O OH  . TYR A 296 ? 0.2142 0.1428 0.2107 0.0176  0.0174  -0.0156 296 TYR A OH  
4596  N N   . GLN A 297 ? 0.1995 0.1925 0.1639 -0.0260 0.0220  -0.0103 297 GLN A N   
4597  C CA  . GLN A 297 ? 0.1758 0.1628 0.1728 -0.0396 0.0210  -0.0163 297 GLN A CA  
4598  C C   . GLN A 297 ? 0.1680 0.1702 0.1676 -0.0757 0.0015  0.0038  297 GLN A C   
4599  O O   . GLN A 297 ? 0.1870 0.1424 0.1568 -0.0454 0.0190  0.0042  297 GLN A O   
4600  C CB  . GLN A 297 ? 0.1777 0.1777 0.1875 -0.0548 0.0076  0.0007  297 GLN A CB  
4601  C CG  . GLN A 297 ? 0.1568 0.1358 0.1912 -0.0179 0.0152  0.0479  297 GLN A CG  
4602  C CD  . GLN A 297 ? 0.1602 0.1489 0.2090 -0.0176 0.0120  0.0390  297 GLN A CD  
4603  O OE1 . GLN A 297 ? 0.1774 0.1846 0.2187 -0.0497 0.0242  -0.0002 297 GLN A OE1 
4604  N NE2 . GLN A 297 ? 0.1769 0.1356 0.2043 -0.0318 0.0182  0.0469  297 GLN A NE2 
4613  N N   . PRO A 298 ? 0.2098 0.1361 0.1676 -0.0298 -0.0147 0.0183  298 PRO A N   
4614  C CA  . PRO A 298 ? 0.1851 0.1674 0.1780 -0.0221 -0.0083 0.0235  298 PRO A CA  
4615  C C   . PRO A 298 ? 0.2177 0.2294 0.2277 -0.0437 -0.0062 0.0701  298 PRO A C   
4616  O O   . PRO A 298 ? 0.2565 0.4083 0.3019 -0.0302 0.0006  0.1806  298 PRO A O   
4617  C CB  . PRO A 298 ? 0.2753 0.1802 0.1564 -0.0040 -0.0298 0.0055  298 PRO A CB  
4618  C CG  . PRO A 298 ? 0.3599 0.2028 0.1502 0.0035  -0.0301 -0.0032 298 PRO A CG  
4619  C CD  . PRO A 298 ? 0.2894 0.1709 0.1495 -0.0160 -0.0127 -0.0179 298 PRO A CD  
4627  N N   . LEU A 299 ? 0.1596 0.1453 0.1937 -0.0359 -0.0054 0.0316  299 LEU A N   
4628  C CA  . LEU A 299 ? 0.1587 0.1335 0.1833 -0.0051 -0.0181 0.0045  299 LEU A CA  
4629  C C   . LEU A 299 ? 0.1352 0.1411 0.1930 -0.0441 -0.0022 0.0058  299 LEU A C   
4630  O O   . LEU A 299 ? 0.1468 0.1949 0.2408 -0.0106 0.0046  0.0411  299 LEU A O   
4631  C CB  . LEU A 299 ? 0.1330 0.1624 0.1716 -0.0282 0.0037  0.0048  299 LEU A CB  
4632  C CG  . LEU A 299 ? 0.1547 0.1729 0.1638 -0.0161 -0.0188 -0.0098 299 LEU A CG  
4633  C CD1 . LEU A 299 ? 0.1746 0.2375 0.1804 -0.0314 -0.0175 -0.0496 299 LEU A CD1 
4634  C CD2 . LEU A 299 ? 0.1834 0.1795 0.1902 -0.0709 -0.0340 -0.0117 299 LEU A CD2 
4646  N N   . SER A 300 ? 0.1582 0.1547 0.1655 0.0057  -0.0023 0.0189  300 SER A N   
4647  C CA  . SER A 300 ? 0.1635 0.1102 0.1537 -0.0118 -0.0182 -0.0116 300 SER A CA  
4648  C C   . SER A 300 ? 0.1576 0.1273 0.1462 -0.0401 -0.0093 -0.0174 300 SER A C   
4649  O O   . SER A 300 ? 0.1632 0.1555 0.1570 -0.0322 -0.0196 0.0014  300 SER A O   
4650  C CB  . SER A 300 ? 0.1415 0.1134 0.1390 -0.0045 -0.0020 0.0029  300 SER A CB  
4651  O OG  . SER A 300 ? 0.1378 0.1758 0.1390 -0.0200 0.0105  -0.0133 300 SER A OG  
4657  N N   . GLY A 301 ? 0.1408 0.1585 0.1442 -0.0279 -0.0122 0.0111  301 GLY A N   
4658  C CA  . GLY A 301 ? 0.1361 0.1805 0.1355 -0.0379 0.0002  0.0021  301 GLY A CA  
4659  C C   . GLY A 301 ? 0.1278 0.1627 0.1512 -0.0239 0.0018  -0.0083 301 GLY A C   
4660  O O   . GLY A 301 ? 0.1581 0.1795 0.1526 -0.0413 -0.0112 0.0026  301 GLY A O   
4664  N N   . VAL A 302 ? 0.1331 0.1347 0.1531 0.0150  0.0126  0.0006  302 VAL A N   
4665  C CA  . VAL A 302 ? 0.1040 0.1148 0.1489 -0.0361 -0.0022 -0.0167 302 VAL A CA  
4666  C C   . VAL A 302 ? 0.1034 0.1467 0.1591 -0.0496 -0.0161 0.0175  302 VAL A C   
4667  O O   . VAL A 302 ? 0.1316 0.1828 0.1659 -0.0576 -0.0154 0.0003  302 VAL A O   
4668  C CB  . VAL A 302 ? 0.1265 0.1318 0.1570 -0.0317 -0.0085 0.0133  302 VAL A CB  
4669  C CG1 . VAL A 302 ? 0.1616 0.1450 0.1728 -0.0073 0.0006  -0.0096 302 VAL A CG1 
4670  C CG2 . VAL A 302 ? 0.1637 0.1422 0.1613 -0.0511 -0.0181 -0.0238 302 VAL A CG2 
4680  N N   . ILE A 303 ? 0.1278 0.1671 0.1615 -0.0408 -0.0120 0.0090  303 ILE A N   
4681  C CA  . ILE A 303 ? 0.1246 0.1487 0.1549 -0.0060 -0.0267 -0.0069 303 ILE A CA  
4682  C C   . ILE A 303 ? 0.1345 0.1616 0.1604 -0.0209 0.0042  0.0091  303 ILE A C   
4683  O O   . ILE A 303 ? 0.1308 0.1649 0.1613 -0.0256 -0.0112 0.0216  303 ILE A O   
4684  C CB  . ILE A 303 ? 0.1686 0.1431 0.1602 -0.0098 -0.0161 -0.0016 303 ILE A CB  
4685  C CG1 . ILE A 303 ? 0.1744 0.1403 0.1596 0.0254  0.0027  -0.0151 303 ILE A CG1 
4686  C CG2 . ILE A 303 ? 0.1622 0.2079 0.1587 -0.0211 -0.0152 0.0197  303 ILE A CG2 
4687  C CD1 . ILE A 303 ? 0.1681 0.1584 0.1560 0.0091  -0.0145 -0.0168 303 ILE A CD1 
4699  N N   . ILE A 304 ? 0.1283 0.1603 0.1751 -0.0264 0.0011  -0.0078 304 ILE A N   
4700  C CA  . ILE A 304 ? 0.1189 0.1461 0.1652 -0.0158 0.0169  -0.0183 304 ILE A CA  
4701  C C   . ILE A 304 ? 0.1570 0.1626 0.1648 -0.0200 -0.0097 -0.0166 304 ILE A C   
4702  O O   . ILE A 304 ? 0.1632 0.1666 0.1692 -0.0168 0.0009  -0.0110 304 ILE A O   
4703  C CB  . ILE A 304 ? 0.1426 0.1720 0.1582 -0.0061 -0.0216 -0.0077 304 ILE A CB  
4704  C CG1 . ILE A 304 ? 0.2046 0.1827 0.1711 -0.0236 -0.0019 -0.0112 304 ILE A CG1 
4705  C CG2 . ILE A 304 ? 0.2057 0.2100 0.1367 -0.0004 -0.0098 0.0260  304 ILE A CG2 
4706  C CD1 . ILE A 304 ? 0.1658 0.2634 0.1771 -0.0388 -0.0135 0.0275  304 ILE A CD1 
4718  N N   . GLY A 305 ? 0.1584 0.1678 0.1629 0.0045  0.0083  -0.0323 305 GLY A N   
4719  C CA  . GLY A 305 ? 0.1483 0.1985 0.1583 -0.0199 -0.0106 -0.0165 305 GLY A CA  
4720  C C   . GLY A 305 ? 0.1525 0.1851 0.1652 -0.0024 -0.0056 0.0168  305 GLY A C   
4721  O O   . GLY A 305 ? 0.1569 0.1913 0.1777 0.0177  -0.0093 0.0258  305 GLY A O   
4725  N N   . ASP A 306 ? 0.1912 0.2163 0.1822 0.0210  -0.0095 0.0510  306 ASP A N   
4726  C CA  . ASP A 306 ? 0.1944 0.2295 0.1731 0.0154  -0.0127 0.0402  306 ASP A CA  
4727  C C   . ASP A 306 ? 0.2023 0.2226 0.1733 0.0117  -0.0045 0.0118  306 ASP A C   
4728  O O   . ASP A 306 ? 0.1824 0.2602 0.1812 0.0575  -0.0019 0.0202  306 ASP A O   
4729  C CB  . ASP A 306 ? 0.2249 0.2134 0.1771 -0.0046 0.0062  0.0244  306 ASP A CB  
4730  C CG  . ASP A 306 ? 0.2985 0.2271 0.1880 0.0045  0.0017  0.0386  306 ASP A CG  
4731  O OD1 . ASP A 306 ? 0.3735 0.2345 0.2063 -0.0351 -0.0144 0.0394  306 ASP A OD1 
4732  O OD2 . ASP A 306 ? 0.3096 0.3306 0.2093 -0.0251 0.0150  0.0021  306 ASP A OD2 
4737  N N   . ARG A 307 ? 0.2055 0.2231 0.1818 -0.0070 -0.0037 0.0129  307 ARG A N   
4738  C CA  . ARG A 307 ? 0.1944 0.2185 0.2076 -0.0094 0.0011  0.0079  307 ARG A CA  
4739  C C   . ARG A 307 ? 0.1886 0.1926 0.2077 0.0226  -0.0063 0.0151  307 ARG A C   
4740  O O   . ARG A 307 ? 0.1738 0.2113 0.2196 0.0045  -0.0080 0.0100  307 ARG A O   
4741  C CB  . ARG A 307 ? 0.2933 0.2626 0.2325 -0.0403 0.0406  -0.0020 307 ARG A CB  
4742  C CG  . ARG A 307 ? 0.4799 0.3821 0.2725 -0.0007 0.0497  0.0246  307 ARG A CG  
4743  C CD  . ARG A 307 ? 0.6351 0.5224 0.3115 0.0209  0.0696  0.0506  307 ARG A CD  
4744  N NE  . ARG A 307 ? 0.8107 0.6360 0.3548 0.0194  0.0619  0.0591  307 ARG A NE  
4745  C CZ  . ARG A 307 ? 0.9168 0.7201 0.3786 0.0668  0.0631  0.0573  307 ARG A CZ  
4746  N NH1 . ARG A 307 ? 0.9624 0.7416 0.3914 0.0728  0.0538  0.0472  307 ARG A NH1 
4747  N NH2 . ARG A 307 ? 0.9394 0.7558 0.3926 0.0705  0.0793  0.0608  307 ARG A NH2 
4761  N N   . VAL A 308 ? 0.1724 0.1568 0.1907 -0.0077 0.0036  0.0460  308 VAL A N   
4762  C CA  . VAL A 308 ? 0.1689 0.1567 0.1761 0.0120  -0.0056 0.0260  308 VAL A CA  
4763  C C   . VAL A 308 ? 0.1983 0.1715 0.1803 0.0045  0.0006  0.0207  308 VAL A C   
4764  O O   . VAL A 308 ? 0.1760 0.1954 0.1911 -0.0200 -0.0078 0.0084  308 VAL A O   
4765  C CB  . VAL A 308 ? 0.1843 0.1514 0.1821 -0.0120 -0.0091 0.0051  308 VAL A CB  
4766  C CG1 . VAL A 308 ? 0.1850 0.1918 0.1859 -0.0193 -0.0033 -0.0067 308 VAL A CG1 
4767  C CG2 . VAL A 308 ? 0.2142 0.1707 0.1784 -0.0160 0.0018  0.0101  308 VAL A CG2 
4777  N N   . TRP A 309 ? 0.1721 0.2055 0.1707 -0.0222 0.0150  0.0142  309 TRP A N   
4778  C CA  . TRP A 309 ? 0.1684 0.1635 0.1898 -0.0334 -0.0058 0.0084  309 TRP A CA  
4779  C C   . TRP A 309 ? 0.1852 0.1504 0.2031 0.0004  -0.0038 -0.0029 309 TRP A C   
4780  O O   . TRP A 309 ? 0.1666 0.1596 0.2054 0.0037  0.0175  0.0112  309 TRP A O   
4781  C CB  . TRP A 309 ? 0.1782 0.1683 0.1818 -0.0329 0.0272  0.0281  309 TRP A CB  
4782  C CG  . TRP A 309 ? 0.1838 0.1438 0.1913 -0.0277 -0.0035 0.0125  309 TRP A CG  
4783  C CD1 . TRP A 309 ? 0.1975 0.1343 0.2067 0.0020  -0.0260 0.0375  309 TRP A CD1 
4784  C CD2 . TRP A 309 ? 0.1818 0.1384 0.1867 -0.0116 -0.0060 -0.0069 309 TRP A CD2 
4785  N NE1 . TRP A 309 ? 0.1902 0.1392 0.2186 -0.0420 -0.0471 0.0465  309 TRP A NE1 
4786  C CE2 . TRP A 309 ? 0.1824 0.1536 0.1982 -0.0096 -0.0175 0.0114  309 TRP A CE2 
4787  C CE3 . TRP A 309 ? 0.1863 0.1753 0.1776 0.0079  -0.0029 -0.0002 309 TRP A CE3 
4788  C CZ2 . TRP A 309 ? 0.1630 0.1748 0.2052 -0.0255 0.0048  0.0280  309 TRP A CZ2 
4789  C CZ3 . TRP A 309 ? 0.1632 0.1986 0.1867 -0.0085 0.0016  0.0450  309 TRP A CZ3 
4790  C CH2 . TRP A 309 ? 0.2044 0.1841 0.1924 0.0061  0.0114  0.0174  309 TRP A CH2 
4801  N N   . GLN A 310 ? 0.1650 0.1999 0.2150 0.0231  0.0057  -0.0023 310 GLN A N   
4802  C CA  . GLN A 310 ? 0.1782 0.2380 0.2432 0.0269  0.0180  0.0045  310 GLN A CA  
4803  C C   . GLN A 310 ? 0.1751 0.1899 0.2405 -0.0156 0.0011  0.0108  310 GLN A C   
4804  O O   . GLN A 310 ? 0.1972 0.1983 0.2398 -0.0164 0.0029  0.0213  310 GLN A O   
4805  C CB  . GLN A 310 ? 0.2261 0.3943 0.2858 0.0119  -0.0213 0.0515  310 GLN A CB  
4806  C CG  . GLN A 310 ? 0.5049 0.6683 0.3308 -0.0345 -0.0589 0.0787  310 GLN A CG  
4807  C CD  . GLN A 310 ? 0.7191 0.8700 0.3758 -0.0141 -0.0871 0.1084  310 GLN A CD  
4808  O OE1 . GLN A 310 ? 0.8023 0.9462 0.3934 -0.0105 -0.1095 0.1174  310 GLN A OE1 
4809  N NE2 . GLN A 310 ? 0.7639 0.9297 0.3969 -0.0010 -0.1006 0.1029  310 GLN A NE2 
4818  N N   . VAL A 311 ? 0.1594 0.1817 0.2434 -0.0318 -0.0181 0.0078  311 VAL A N   
4819  C CA  . VAL A 311 ? 0.1401 0.1732 0.2441 -0.0268 0.0004  0.0051  311 VAL A CA  
4820  C C   . VAL A 311 ? 0.1727 0.1884 0.2368 0.0227  -0.0077 0.0005  311 VAL A C   
4821  O O   . VAL A 311 ? 0.1799 0.1664 0.2387 0.0116  -0.0126 0.0001  311 VAL A O   
4822  C CB  . VAL A 311 ? 0.1985 0.1691 0.2578 -0.0261 -0.0064 -0.0021 311 VAL A CB  
4823  C CG1 . VAL A 311 ? 0.2049 0.1241 0.2540 0.0005  0.0004  -0.0128 311 VAL A CG1 
4824  C CG2 . VAL A 311 ? 0.2227 0.1421 0.2658 0.0196  -0.0016 0.0031  311 VAL A CG2 
4834  N N   . LEU A 312 ? 0.1697 0.1805 0.2217 0.0181  0.0145  0.0217  312 LEU A N   
4835  C CA  . LEU A 312 ? 0.1401 0.2130 0.2210 0.0131  -0.0075 0.0200  312 LEU A CA  
4836  C C   . LEU A 312 ? 0.1581 0.1998 0.2111 -0.0247 -0.0005 0.0215  312 LEU A C   
4837  O O   . LEU A 312 ? 0.1961 0.2052 0.2013 0.0124  0.0098  0.0177  312 LEU A O   
4838  C CB  . LEU A 312 ? 0.1265 0.2012 0.2306 0.0205  0.0242  -0.0002 312 LEU A CB  
4839  C CG  . LEU A 312 ? 0.1558 0.2030 0.2417 0.0376  0.0066  -0.0659 312 LEU A CG  
4840  C CD1 . LEU A 312 ? 0.1387 0.2507 0.2527 0.0070  -0.0062 -0.0281 312 LEU A CD1 
4841  C CD2 . LEU A 312 ? 0.1906 0.3299 0.2644 0.0717  0.0021  -0.0924 312 LEU A CD2 
4853  N N   . GLU A 313 ? 0.1620 0.2401 0.2149 -0.0085 0.0007  -0.0065 313 GLU A N   
4854  C CA  . GLU A 313 ? 0.1199 0.2221 0.2287 -0.0075 -0.0162 -0.0271 313 GLU A CA  
4855  C C   . GLU A 313 ? 0.1319 0.2273 0.2441 -0.0028 -0.0111 -0.0303 313 GLU A C   
4856  O O   . GLU A 313 ? 0.1405 0.2526 0.2666 -0.0280 0.0019  -0.0450 313 GLU A O   
4857  C CB  . GLU A 313 ? 0.1427 0.2356 0.2425 0.0134  -0.0187 -0.0418 313 GLU A CB  
4858  C CG  . GLU A 313 ? 0.1495 0.2439 0.2623 0.0056  -0.0098 -0.0537 313 GLU A CG  
4859  C CD  . GLU A 313 ? 0.1637 0.2496 0.2708 0.0152  -0.0566 -0.0285 313 GLU A CD  
4860  O OE1 . GLU A 313 ? 0.2547 0.2653 0.2716 0.0190  -0.0848 -0.0104 313 GLU A OE1 
4861  O OE2 . GLU A 313 ? 0.2050 0.2397 0.2859 -0.0266 -0.0494 -0.0379 313 GLU A OE2 
4868  N N   . GLN A 314 ? 0.1688 0.1962 0.2515 -0.0039 -0.0146 -0.0179 314 GLN A N   
4869  C CA  . GLN A 314 ? 0.2002 0.1797 0.2685 0.0278  -0.0151 -0.0177 314 GLN A CA  
4870  C C   . GLN A 314 ? 0.1625 0.2039 0.2609 0.0216  -0.0215 -0.0141 314 GLN A C   
4871  O O   . GLN A 314 ? 0.1998 0.2239 0.2638 0.0426  -0.0083 -0.0363 314 GLN A O   
4872  C CB  . GLN A 314 ? 0.2310 0.1812 0.2922 0.0566  -0.0521 0.0047  314 GLN A CB  
4873  C CG  . GLN A 314 ? 0.3580 0.2542 0.3304 0.0162  -0.0428 0.0202  314 GLN A CG  
4874  C CD  . GLN A 314 ? 0.4829 0.3413 0.3699 0.0198  -0.0541 0.0149  314 GLN A CD  
4875  O OE1 . GLN A 314 ? 0.5036 0.3338 0.3862 0.0376  -0.0750 0.0283  314 GLN A OE1 
4876  N NE2 . GLN A 314 ? 0.5297 0.3618 0.3795 0.0384  -0.0743 -0.0104 314 GLN A NE2 
4885  N N   . GLY A 315 ? 0.1513 0.1916 0.2628 0.0201  -0.0198 -0.0174 315 GLY A N   
4886  C CA  . GLY A 315 ? 0.2005 0.2070 0.2575 -0.0065 -0.0089 -0.0217 315 GLY A CA  
4887  C C   . GLY A 315 ? 0.1774 0.1974 0.2493 -0.0360 -0.0134 -0.0093 315 GLY A C   
4888  O O   . GLY A 315 ? 0.2098 0.1884 0.2515 -0.0112 0.0075  -0.0231 315 GLY A O   
4892  N N   . THR A 316 ? 0.1578 0.1989 0.2445 -0.0293 -0.0209 -0.0052 316 THR A N   
4893  C CA  . THR A 316 ? 0.1435 0.1999 0.2377 -0.0369 0.0011  -0.0099 316 THR A CA  
4894  C C   . THR A 316 ? 0.1352 0.1990 0.2450 -0.0787 0.0062  -0.0005 316 THR A C   
4895  O O   . THR A 316 ? 0.1288 0.2633 0.2608 -0.0112 -0.0086 0.0138  316 THR A O   
4896  C CB  . THR A 316 ? 0.1560 0.2130 0.2340 0.0239  0.0127  0.0072  316 THR A CB  
4897  O OG1 . THR A 316 ? 0.1659 0.2432 0.2324 -0.0178 0.0001  0.0323  316 THR A OG1 
4898  C CG2 . THR A 316 ? 0.1488 0.2067 0.2402 0.0345  0.0199  -0.0026 316 THR A CG2 
4906  N N   . GLY A 317 ? 0.1726 0.2047 0.2551 0.0236  -0.0117 -0.0048 317 GLY A N   
4907  C CA  . GLY A 317 ? 0.2056 0.2274 0.2671 0.0045  -0.0083 -0.0243 317 GLY A CA  
4908  C C   . GLY A 317 ? 0.1895 0.2070 0.2807 0.0265  -0.0047 0.0009  317 GLY A C   
4909  O O   . GLY A 317 ? 0.1862 0.2594 0.3085 0.0274  -0.0096 -0.0156 317 GLY A O   
4913  N N   . GLU A 318 ? 0.1682 0.2355 0.2941 0.0561  -0.0208 -0.0031 318 GLU A N   
4914  C CA  . GLU A 318 ? 0.1807 0.2320 0.2881 0.0372  -0.0129 -0.0113 318 GLU A CA  
4915  C C   . GLU A 318 ? 0.1769 0.2577 0.2716 0.0153  0.0173  -0.0078 318 GLU A C   
4916  O O   . GLU A 318 ? 0.2374 0.3091 0.2841 0.0668  0.0307  -0.0146 318 GLU A O   
4917  C CB  . GLU A 318 ? 0.2453 0.3244 0.3167 -0.0110 -0.0017 -0.0105 318 GLU A CB  
4918  C CG  . GLU A 318 ? 0.3677 0.3841 0.3569 -0.0947 0.0081  -0.0116 318 GLU A CG  
4919  C CD  . GLU A 318 ? 0.4752 0.3830 0.3850 -0.1182 -0.0042 -0.0505 318 GLU A CD  
4920  O OE1 . GLU A 318 ? 0.4410 0.3083 0.3847 -0.1674 -0.0601 -0.0629 318 GLU A OE1 
4921  O OE2 . GLU A 318 ? 0.5644 0.4179 0.4082 -0.0874 0.0343  -0.0629 318 GLU A OE2 
4928  N N   . PHE A 319 ? 0.1896 0.2727 0.2574 0.0006  -0.0070 -0.0273 319 PHE A N   
4929  C CA  . PHE A 319 ? 0.2094 0.2491 0.2573 0.0296  -0.0004 -0.0173 319 PHE A CA  
4930  C C   . PHE A 319 ? 0.2428 0.2666 0.2481 0.0280  0.0005  -0.0027 319 PHE A C   
4931  O O   . PHE A 319 ? 0.2940 0.2700 0.2577 -0.0079 -0.0018 -0.0007 319 PHE A O   
4932  C CB  . PHE A 319 ? 0.2272 0.2661 0.2610 0.0259  -0.0323 -0.0220 319 PHE A CB  
4933  C CG  . PHE A 319 ? 0.2333 0.2681 0.2778 -0.0250 -0.0144 -0.0188 319 PHE A CG  
4934  C CD1 . PHE A 319 ? 0.2525 0.2811 0.3047 -0.0216 -0.0162 0.0118  319 PHE A CD1 
4935  C CD2 . PHE A 319 ? 0.2776 0.2412 0.2800 -0.1067 -0.0080 -0.0057 319 PHE A CD2 
4936  C CE1 . PHE A 319 ? 0.2557 0.3000 0.3101 -0.0098 0.0096  0.0047  319 PHE A CE1 
4937  C CE2 . PHE A 319 ? 0.3077 0.2572 0.2857 -0.0319 0.0129  -0.0306 319 PHE A CE2 
4938  C CZ  . PHE A 319 ? 0.3138 0.2858 0.3049 -0.0166 -0.0258 -0.0106 319 PHE A CZ  
4948  N N   . GLY A 320 ? 0.2106 0.2548 0.2406 0.0385  -0.0015 -0.0062 320 GLY A N   
4949  C CA  . GLY A 320 ? 0.1979 0.2404 0.2375 -0.0121 0.0012  0.0244  320 GLY A CA  
4950  C C   . GLY A 320 ? 0.1732 0.2246 0.2225 -0.0200 0.0200  0.0048  320 GLY A C   
4951  O O   . GLY A 320 ? 0.1530 0.2536 0.2142 0.0033  0.0237  -0.0049 320 GLY A O   
4955  N N   . PRO A 321 ? 0.2018 0.2222 0.2233 -0.0224 0.0167  -0.0036 321 PRO A N   
4956  C CA  . PRO A 321 ? 0.1761 0.2266 0.2134 -0.0060 0.0114  -0.0263 321 PRO A CA  
4957  C C   . PRO A 321 ? 0.1743 0.1979 0.2078 0.0081  0.0108  -0.0391 321 PRO A C   
4958  O O   . PRO A 321 ? 0.1986 0.2313 0.2307 0.0249  0.0003  -0.0413 321 PRO A O   
4959  C CB  . PRO A 321 ? 0.1524 0.2813 0.2247 -0.0366 -0.0058 -0.0321 321 PRO A CB  
4960  C CG  . PRO A 321 ? 0.1834 0.2264 0.2413 -0.0391 0.0237  -0.0142 321 PRO A CG  
4961  C CD  . PRO A 321 ? 0.2245 0.2487 0.2412 -0.0132 0.0117  0.0120  321 PRO A CD  
4969  N N   . ILE A 322 ? 0.1767 0.1973 0.1905 0.0008  -0.0045 -0.0345 322 ILE A N   
4970  C CA  . ILE A 322 ? 0.1660 0.2431 0.1919 -0.0410 0.0018  0.0201  322 ILE A CA  
4971  C C   . ILE A 322 ? 0.1649 0.1589 0.1920 -0.0237 -0.0005 0.0311  322 ILE A C   
4972  O O   . ILE A 322 ? 0.1697 0.1514 0.1922 -0.0404 -0.0025 0.0055  322 ILE A O   
4973  C CB  . ILE A 322 ? 0.1519 0.3148 0.2077 -0.0556 -0.0016 0.0274  322 ILE A CB  
4974  C CG1 . ILE A 322 ? 0.1772 0.4276 0.2170 -0.0903 -0.0194 0.0467  322 ILE A CG1 
4975  C CG2 . ILE A 322 ? 0.1528 0.3314 0.2182 -0.0587 0.0062  0.0483  322 ILE A CG2 
4976  C CD1 . ILE A 322 ? 0.2725 0.4566 0.2505 -0.1427 -0.0298 0.0651  322 ILE A CD1 
4988  N N   . GLY A 323 ? 0.1699 0.2085 0.1713 -0.0037 -0.0126 0.0076  323 GLY A N   
4989  C CA  . GLY A 323 ? 0.1191 0.1785 0.1720 0.0160  0.0182  0.0001  323 GLY A CA  
4990  C C   . GLY A 323 ? 0.1502 0.1402 0.1785 -0.0524 -0.0111 -0.0045 323 GLY A C   
4991  O O   . GLY A 323 ? 0.1661 0.1471 0.1647 -0.0199 -0.0084 0.0076  323 GLY A O   
4995  N N   . HIS A 324 ? 0.1705 0.1166 0.1818 -0.0265 -0.0033 0.0107  324 HIS A N   
4996  C CA  . HIS A 324 ? 0.1446 0.1487 0.1735 -0.0372 0.0068  0.0109  324 HIS A CA  
4997  C C   . HIS A 324 ? 0.1064 0.1566 0.1732 -0.0162 -0.0203 0.0059  324 HIS A C   
4998  O O   . HIS A 324 ? 0.1635 0.2177 0.1684 -0.0330 -0.0344 0.0068  324 HIS A O   
4999  C CB  . HIS A 324 ? 0.1677 0.1863 0.1806 -0.0274 0.0115  0.0085  324 HIS A CB  
5000  C CG  . HIS A 324 ? 0.1402 0.1768 0.1701 -0.0221 0.0215  -0.0096 324 HIS A CG  
5001  N ND1 . HIS A 324 ? 0.1433 0.1283 0.1707 -0.0139 -0.0008 -0.0247 324 HIS A ND1 
5002  C CD2 . HIS A 324 ? 0.1777 0.1360 0.1734 -0.0185 -0.0047 -0.0084 324 HIS A CD2 
5003  C CE1 . HIS A 324 ? 0.1617 0.1440 0.1678 -0.0269 -0.0069 -0.0285 324 HIS A CE1 
5004  N NE2 . HIS A 324 ? 0.1758 0.1283 0.1665 -0.0020 -0.0041 -0.0302 324 HIS A NE2 
5012  N N   . GLY A 325 ? 0.1369 0.1312 0.1706 -0.0166 -0.0057 -0.0100 325 GLY A N   
5013  C CA  . GLY A 325 ? 0.1364 0.1261 0.1751 -0.0023 0.0075  -0.0117 325 GLY A CA  
5014  C C   . GLY A 325 ? 0.1321 0.1425 0.1813 -0.0547 -0.0063 -0.0169 325 GLY A C   
5015  O O   . GLY A 325 ? 0.1960 0.1576 0.1942 -0.0235 -0.0334 -0.0279 325 GLY A O   
5019  N N   . TRP A 326 ? 0.1596 0.1344 0.1761 -0.0349 0.0261  0.0041  326 TRP A N   
5020  C CA  . TRP A 326 ? 0.1514 0.1241 0.1743 -0.0147 0.0068  0.0042  326 TRP A CA  
5021  C C   . TRP A 326 ? 0.1640 0.1589 0.1681 0.0042  0.0072  0.0033  326 TRP A C   
5022  O O   . TRP A 326 ? 0.1572 0.1658 0.1716 -0.0271 0.0003  -0.0082 326 TRP A O   
5023  C CB  . TRP A 326 ? 0.1878 0.1826 0.1611 -0.0265 0.0368  0.0112  326 TRP A CB  
5024  C CG  . TRP A 326 ? 0.1832 0.1635 0.1477 -0.0429 0.0060  0.0085  326 TRP A CG  
5025  C CD1 . TRP A 326 ? 0.2018 0.1491 0.1463 -0.0064 0.0037  0.0139  326 TRP A CD1 
5026  C CD2 . TRP A 326 ? 0.1394 0.1620 0.1377 -0.0059 0.0006  -0.0165 326 TRP A CD2 
5027  N NE1 . TRP A 326 ? 0.1907 0.1274 0.1384 -0.0199 0.0147  0.0223  326 TRP A NE1 
5028  C CE2 . TRP A 326 ? 0.1752 0.1368 0.1312 -0.0105 0.0227  -0.0212 326 TRP A CE2 
5029  C CE3 . TRP A 326 ? 0.1725 0.1096 0.1491 -0.0359 -0.0023 -0.0054 326 TRP A CE3 
5030  C CZ2 . TRP A 326 ? 0.1601 0.1466 0.1220 -0.0009 0.0002  0.0036  326 TRP A CZ2 
5031  C CZ3 . TRP A 326 ? 0.1828 0.1369 0.1406 -0.0221 0.0067  0.0009  326 TRP A CZ3 
5032  C CH2 . TRP A 326 ? 0.1763 0.1737 0.1364 -0.0189 0.0151  0.0144  326 TRP A CH2 
5043  N N   . THR A 327 ? 0.1445 0.1601 0.1640 -0.0288 -0.0130 0.0009  327 THR A N   
5044  C CA  . THR A 327 ? 0.1462 0.1708 0.1643 -0.0284 -0.0128 -0.0191 327 THR A CA  
5045  C C   . THR A 327 ? 0.1598 0.1907 0.1490 -0.0597 -0.0378 -0.0102 327 THR A C   
5046  O O   . THR A 327 ? 0.1967 0.1792 0.1610 -0.0379 -0.0365 -0.0040 327 THR A O   
5047  C CB  . THR A 327 ? 0.1650 0.1792 0.1631 -0.0737 -0.0201 -0.0358 327 THR A CB  
5048  O OG1 . THR A 327 ? 0.3038 0.2040 0.1630 -0.0575 0.0121  -0.0415 327 THR A OG1 
5049  C CG2 . THR A 327 ? 0.1938 0.2033 0.1627 -0.0948 -0.0114 -0.0130 327 THR A CG2 
5057  N N   . TYR A 328 ? 0.1811 0.1574 0.1377 -0.0830 -0.0070 0.0071  328 TYR A N   
5058  C CA  . TYR A 328 ? 0.1878 0.1602 0.1556 -0.0538 0.0058  -0.0143 328 TYR A CA  
5059  C C   . TYR A 328 ? 0.1850 0.1810 0.1642 -0.0200 -0.0042 -0.0015 328 TYR A C   
5060  O O   . TYR A 328 ? 0.1743 0.1483 0.1603 -0.0148 -0.0068 0.0152  328 TYR A O   
5061  C CB  . TYR A 328 ? 0.1792 0.1501 0.1623 -0.0208 0.0287  0.0048  328 TYR A CB  
5062  C CG  . TYR A 328 ? 0.1638 0.1454 0.1612 -0.0376 0.0091  -0.0143 328 TYR A CG  
5063  C CD1 . TYR A 328 ? 0.1947 0.1810 0.1723 -0.0249 -0.0198 0.0095  328 TYR A CD1 
5064  C CD2 . TYR A 328 ? 0.1727 0.1943 0.1638 -0.0362 0.0093  0.0325  328 TYR A CD2 
5065  C CE1 . TYR A 328 ? 0.2017 0.1950 0.1812 -0.0133 -0.0407 0.0173  328 TYR A CE1 
5066  C CE2 . TYR A 328 ? 0.2023 0.1907 0.1576 -0.0405 0.0180  0.0298  328 TYR A CE2 
5067  C CZ  . TYR A 328 ? 0.1855 0.2321 0.1668 -0.0404 -0.0160 0.0182  328 TYR A CZ  
5068  O OH  . TYR A 328 ? 0.2478 0.2195 0.1966 -0.0400 0.0117  0.0185  328 TYR A OH  
5078  N N   . SER A 329 ? 0.1784 0.1827 0.1526 -0.0220 -0.0118 0.0001  329 SER A N   
5079  C CA  . SER A 329 ? 0.1609 0.1522 0.1442 -0.0194 -0.0011 0.0067  329 SER A CA  
5080  C C   . SER A 329 ? 0.1478 0.1412 0.1487 -0.0121 0.0092  -0.0050 329 SER A C   
5081  O O   . SER A 329 ? 0.1892 0.1673 0.1610 -0.0344 0.0145  -0.0069 329 SER A O   
5082  C CB  . SER A 329 ? 0.1486 0.1710 0.1346 0.0178  0.0075  0.0061  329 SER A CB  
5083  O OG  . SER A 329 ? 0.1716 0.1833 0.1335 -0.0295 0.0028  0.0140  329 SER A OG  
5089  N N   . GLY A 330 ? 0.1635 0.1368 0.1634 -0.0256 0.0310  0.0105  330 GLY A N   
5090  C CA  . GLY A 330 ? 0.1708 0.1306 0.1789 -0.0540 0.0073  -0.0176 330 GLY A CA  
5091  C C   . GLY A 330 ? 0.1357 0.1613 0.1904 -0.0680 0.0021  -0.0021 330 GLY A C   
5092  O O   . GLY A 330 ? 0.1620 0.1713 0.1980 -0.0402 -0.0085 0.0044  330 GLY A O   
5096  N N   . HIS A 331 ? 0.1628 0.1739 0.1818 -0.0194 -0.0030 -0.0019 331 HIS A N   
5097  C CA  . HIS A 331 ? 0.1860 0.1640 0.1830 -0.0181 -0.0242 -0.0033 331 HIS A CA  
5098  C C   . HIS A 331 ? 0.1577 0.1615 0.1708 -0.0755 -0.0080 -0.0102 331 HIS A C   
5099  O O   . HIS A 331 ? 0.1817 0.1667 0.1823 -0.0231 0.0338  0.0101  331 HIS A O   
5100  C CB  . HIS A 331 ? 0.1704 0.1350 0.1814 -0.0386 -0.0151 0.0164  331 HIS A CB  
5101  C CG  . HIS A 331 ? 0.1855 0.0816 0.1805 -0.0332 -0.0060 -0.0091 331 HIS A CG  
5102  N ND1 . HIS A 331 ? 0.1896 0.1229 0.1927 -0.0448 0.0145  -0.0008 331 HIS A ND1 
5103  C CD2 . HIS A 331 ? 0.2244 0.1294 0.1730 -0.0314 0.0040  -0.0088 331 HIS A CD2 
5104  C CE1 . HIS A 331 ? 0.2239 0.1798 0.1896 -0.0632 -0.0004 0.0041  331 HIS A CE1 
5105  N NE2 . HIS A 331 ? 0.2098 0.1358 0.1667 -0.0721 0.0004  0.0025  331 HIS A NE2 
5113  N N   . ALA A 332 ? 0.1818 0.1679 0.1579 -0.0429 -0.0165 -0.0105 332 ALA A N   
5114  C CA  . ALA A 332 ? 0.1744 0.1742 0.1618 -0.0323 -0.0135 0.0150  332 ALA A CA  
5115  C C   . ALA A 332 ? 0.1538 0.1859 0.1617 -0.0478 0.0001  0.0046  332 ALA A C   
5116  O O   . ALA A 332 ? 0.1890 0.1989 0.1658 -0.0352 0.0024  -0.0097 332 ALA A O   
5117  C CB  . ALA A 332 ? 0.1774 0.1857 0.1770 -0.0751 0.0024  0.0197  332 ALA A CB  
5123  N N   . LEU A 333 ? 0.1636 0.1803 0.1619 -0.0647 0.0137  -0.0216 333 LEU A N   
5124  C CA  . LEU A 333 ? 0.1369 0.1531 0.1629 -0.0301 0.0142  0.0012  333 LEU A CA  
5125  C C   . LEU A 333 ? 0.1773 0.1526 0.1734 -0.0143 0.0066  0.0040  333 LEU A C   
5126  O O   . LEU A 333 ? 0.1966 0.1480 0.1698 -0.0254 0.0123  -0.0157 333 LEU A O   
5127  C CB  . LEU A 333 ? 0.1631 0.1271 0.1643 0.0038  0.0065  0.0082  333 LEU A CB  
5128  C CG  . LEU A 333 ? 0.2479 0.1269 0.1707 -0.0551 0.0392  0.0063  333 LEU A CG  
5129  C CD1 . LEU A 333 ? 0.2586 0.1156 0.1795 -0.0452 0.0277  0.0125  333 LEU A CD1 
5130  C CD2 . LEU A 333 ? 0.2691 0.1248 0.1898 -0.0455 0.0332  0.0146  333 LEU A CD2 
5142  N N   . GLY A 334 ? 0.1912 0.1291 0.1682 -0.0473 -0.0047 0.0275  334 GLY A N   
5143  C CA  . GLY A 334 ? 0.2002 0.1233 0.1846 -0.0366 -0.0071 0.0163  334 GLY A CA  
5144  C C   . GLY A 334 ? 0.1666 0.1725 0.1732 -0.0193 0.0013  -0.0124 334 GLY A C   
5145  O O   . GLY A 334 ? 0.1873 0.1903 0.1587 -0.0130 -0.0022 -0.0087 334 GLY A O   
5149  N N   . CYS A 335 ? 0.1468 0.1973 0.1771 -0.0316 0.0008  -0.0139 335 CYS A N   
5150  C CA  . CYS A 335 ? 0.1857 0.2041 0.1789 -0.0623 -0.0107 -0.0005 335 CYS A CA  
5151  C C   . CYS A 335 ? 0.1621 0.1724 0.1702 -0.0346 -0.0057 0.0093  335 CYS A C   
5152  O O   . CYS A 335 ? 0.2025 0.1911 0.1744 -0.0383 -0.0197 -0.0049 335 CYS A O   
5153  C CB  . CYS A 335 ? 0.1806 0.1659 0.1963 -0.0459 -0.0144 0.0149  335 CYS A CB  
5154  S SG  . CYS A 335 ? 0.1945 0.1696 0.1895 -0.0105 -0.0061 -0.0018 335 CYS A SG  
5160  N N   . ALA A 336 ? 0.2062 0.1294 0.1770 -0.0338 0.0152  -0.0239 336 ALA A N   
5161  C CA  . ALA A 336 ? 0.1918 0.1526 0.1706 -0.0300 0.0099  -0.0088 336 ALA A CA  
5162  C C   . ALA A 336 ? 0.2067 0.1909 0.1740 -0.0141 0.0054  0.0038  336 ALA A C   
5163  O O   . ALA A 336 ? 0.2113 0.2164 0.1879 -0.0255 0.0065  -0.0044 336 ALA A O   
5164  C CB  . ALA A 336 ? 0.2292 0.1555 0.1592 -0.0258 -0.0056 0.0067  336 ALA A CB  
5170  N N   . ALA A 337 ? 0.1912 0.2155 0.1677 0.0001  0.0064  -0.0135 337 ALA A N   
5171  C CA  . ALA A 337 ? 0.1541 0.1955 0.1603 -0.0171 0.0015  -0.0139 337 ALA A CA  
5172  C C   . ALA A 337 ? 0.1826 0.1626 0.1647 0.0273  0.0010  -0.0183 337 ALA A C   
5173  O O   . ALA A 337 ? 0.2063 0.1633 0.1682 -0.0109 0.0119  -0.0195 337 ALA A O   
5174  C CB  . ALA A 337 ? 0.1651 0.2431 0.1752 0.0029  -0.0330 0.0028  337 ALA A CB  
5180  N N   . GLY A 338 ? 0.1785 0.1551 0.1695 0.0098  0.0083  0.0039  338 GLY A N   
5181  C CA  . GLY A 338 ? 0.1829 0.1640 0.1603 -0.0240 -0.0033 0.0185  338 GLY A CA  
5182  C C   . GLY A 338 ? 0.1738 0.1670 0.1742 -0.0088 -0.0057 0.0109  338 GLY A C   
5183  O O   . GLY A 338 ? 0.2083 0.1805 0.1696 -0.0495 0.0146  0.0115  338 GLY A O   
5187  N N   . LEU A 339 ? 0.1940 0.1563 0.1835 0.0095  -0.0046 0.0134  339 LEU A N   
5188  C CA  . LEU A 339 ? 0.1827 0.2079 0.1757 -0.0463 -0.0200 0.0001  339 LEU A CA  
5189  C C   . LEU A 339 ? 0.2212 0.1603 0.1729 -0.0618 -0.0032 0.0131  339 LEU A C   
5190  O O   . LEU A 339 ? 0.2617 0.2284 0.1657 -0.0448 -0.0143 0.0062  339 LEU A O   
5191  C CB  . LEU A 339 ? 0.2276 0.2132 0.1878 -0.0735 0.0046  -0.0100 339 LEU A CB  
5192  C CG  . LEU A 339 ? 0.2310 0.2096 0.2134 -0.0762 0.0163  -0.0059 339 LEU A CG  
5193  C CD1 . LEU A 339 ? 0.2233 0.1908 0.2156 -0.0829 0.0183  0.0111  339 LEU A CD1 
5194  C CD2 . LEU A 339 ? 0.2125 0.2190 0.2226 -0.0728 0.0007  -0.0048 339 LEU A CD2 
5206  N N   . ALA A 340 ? 0.2398 0.1674 0.1803 -0.0764 -0.0136 -0.0051 340 ALA A N   
5207  C CA  . ALA A 340 ? 0.2370 0.1628 0.1767 -0.0364 0.0116  -0.0090 340 ALA A CA  
5208  C C   . ALA A 340 ? 0.2310 0.1785 0.1785 -0.0273 0.0034  -0.0342 340 ALA A C   
5209  O O   . ALA A 340 ? 0.2458 0.1751 0.1751 -0.0200 0.0027  -0.0469 340 ALA A O   
5210  C CB  . ALA A 340 ? 0.2319 0.1438 0.1666 -0.0204 -0.0047 -0.0079 340 ALA A CB  
5216  N N   . ASN A 341 ? 0.1960 0.1377 0.1949 -0.0155 0.0049  -0.0416 341 ASN A N   
5217  C CA  . ASN A 341 ? 0.1606 0.1749 0.1945 -0.0294 0.0024  -0.0434 341 ASN A CA  
5218  C C   . ASN A 341 ? 0.1432 0.1869 0.1956 -0.0004 0.0148  -0.0171 341 ASN A C   
5219  O O   . ASN A 341 ? 0.1737 0.1630 0.2057 -0.0090 0.0054  -0.0109 341 ASN A O   
5220  C CB  . ASN A 341 ? 0.1809 0.1820 0.1963 -0.0260 -0.0097 -0.0499 341 ASN A CB  
5221  C CG  . ASN A 341 ? 0.1936 0.1521 0.1926 -0.0396 0.0030  -0.0284 341 ASN A CG  
5222  O OD1 . ASN A 341 ? 0.1897 0.1545 0.2039 -0.0239 -0.0041 -0.0162 341 ASN A OD1 
5223  N ND2 . ASN A 341 ? 0.2474 0.1781 0.1848 -0.0297 0.0128  -0.0116 341 ASN A ND2 
5230  N N   . LEU A 342 ? 0.1770 0.1819 0.1797 -0.0053 0.0049  -0.0003 342 LEU A N   
5231  C CA  . LEU A 342 ? 0.1987 0.1652 0.1847 -0.0137 0.0159  -0.0237 342 LEU A CA  
5232  C C   . LEU A 342 ? 0.1765 0.1727 0.1755 -0.0446 0.0214  -0.0218 342 LEU A C   
5233  O O   . LEU A 342 ? 0.2117 0.2155 0.1682 -0.0293 0.0184  -0.0251 342 LEU A O   
5234  C CB  . LEU A 342 ? 0.2376 0.2071 0.1966 -0.0122 0.0104  -0.0322 342 LEU A CB  
5235  C CG  . LEU A 342 ? 0.2663 0.1619 0.2301 -0.0039 0.0187  -0.0048 342 LEU A CG  
5236  C CD1 . LEU A 342 ? 0.2745 0.1810 0.2377 0.0298  0.0234  0.0048  342 LEU A CD1 
5237  C CD2 . LEU A 342 ? 0.3149 0.2127 0.2405 0.0425  0.0416  -0.0268 342 LEU A CD2 
5249  N N   . ALA A 343 ? 0.2301 0.1981 0.1752 -0.0661 0.0139  -0.0173 343 ALA A N   
5250  C CA  . ALA A 343 ? 0.2659 0.2055 0.1779 -0.0802 -0.0229 -0.0328 343 ALA A CA  
5251  C C   . ALA A 343 ? 0.2403 0.2145 0.1725 -0.0750 0.0126  -0.0443 343 ALA A C   
5252  O O   . ALA A 343 ? 0.2317 0.2263 0.1580 -0.0176 0.0183  -0.0351 343 ALA A O   
5253  C CB  . ALA A 343 ? 0.2248 0.2228 0.1894 -0.0732 -0.0164 -0.0239 343 ALA A CB  
5259  N N   . ILE A 344 ? 0.2406 0.2091 0.1736 -0.0532 0.0368  -0.0430 344 ILE A N   
5260  C CA  . ILE A 344 ? 0.2238 0.1794 0.1806 -0.0224 0.0316  -0.0324 344 ILE A CA  
5261  C C   . ILE A 344 ? 0.2201 0.1499 0.1865 0.0445  0.0218  -0.0413 344 ILE A C   
5262  O O   . ILE A 344 ? 0.1994 0.2031 0.1923 -0.0039 0.0307  -0.0456 344 ILE A O   
5263  C CB  . ILE A 344 ? 0.2347 0.1614 0.1838 -0.0200 0.0121  -0.0148 344 ILE A CB  
5264  C CG1 . ILE A 344 ? 0.2601 0.2102 0.2003 -0.0370 0.0162  -0.0263 344 ILE A CG1 
5265  C CG2 . ILE A 344 ? 0.2689 0.1476 0.1797 -0.0188 0.0032  -0.0009 344 ILE A CG2 
5266  C CD1 . ILE A 344 ? 0.2578 0.2154 0.2156 -0.0611 0.0060  -0.0033 344 ILE A CD1 
5278  N N   . ILE A 345 ? 0.2126 0.1808 0.1821 -0.0082 0.0136  -0.0319 345 ILE A N   
5279  C CA  . ILE A 345 ? 0.2161 0.1925 0.1761 -0.0241 0.0047  -0.0132 345 ILE A CA  
5280  C C   . ILE A 345 ? 0.2415 0.2381 0.1731 -0.0326 0.0268  -0.0393 345 ILE A C   
5281  O O   . ILE A 345 ? 0.2629 0.2307 0.1811 -0.0507 0.0389  -0.0353 345 ILE A O   
5282  C CB  . ILE A 345 ? 0.1757 0.1872 0.1721 -0.0242 0.0112  -0.0039 345 ILE A CB  
5283  C CG1 . ILE A 345 ? 0.1905 0.1921 0.1878 -0.0138 0.0182  -0.0143 345 ILE A CG1 
5284  C CG2 . ILE A 345 ? 0.1920 0.2337 0.1760 -0.0287 0.0256  -0.0162 345 ILE A CG2 
5285  C CD1 . ILE A 345 ? 0.2099 0.2007 0.1990 -0.0586 0.0345  -0.0094 345 ILE A CD1 
5297  N N   . GLU A 346 ? 0.2723 0.2934 0.1746 -0.0258 0.0163  -0.0600 346 GLU A N   
5298  C CA  . GLU A 346 ? 0.3039 0.3193 0.1877 -0.0401 -0.0072 -0.0784 346 GLU A CA  
5299  C C   . GLU A 346 ? 0.2729 0.2957 0.1891 -0.0578 0.0264  -0.0802 346 GLU A C   
5300  O O   . GLU A 346 ? 0.3312 0.3360 0.1861 -0.0688 0.0274  -0.0698 346 GLU A O   
5301  C CB  . GLU A 346 ? 0.3865 0.4474 0.2068 -0.0255 -0.0593 -0.0966 346 GLU A CB  
5302  C CG  . GLU A 346 ? 0.5674 0.6016 0.2367 0.0085  -0.0564 -0.1306 346 GLU A CG  
5303  C CD  . GLU A 346 ? 0.7649 0.8049 0.2910 0.0616  -0.0649 -0.1290 346 GLU A CD  
5304  O OE1 . GLU A 346 ? 0.8276 0.9034 0.3209 0.0843  -0.0598 -0.1100 346 GLU A OE1 
5305  O OE2 . GLU A 346 ? 0.8602 0.8964 0.3210 0.0495  -0.0566 -0.1122 346 GLU A OE2 
5312  N N   . ARG A 347 ? 0.2368 0.2771 0.1967 -0.0640 0.0484  -0.0698 347 ARG A N   
5313  C CA  . ARG A 347 ? 0.2555 0.2875 0.2106 -0.0757 0.0341  -0.0845 347 ARG A CA  
5314  C C   . ARG A 347 ? 0.2514 0.2780 0.2021 -0.0703 0.0349  -0.0891 347 ARG A C   
5315  O O   . ARG A 347 ? 0.3184 0.2929 0.2391 -0.0216 0.0268  -0.0887 347 ARG A O   
5316  C CB  . ARG A 347 ? 0.3182 0.2854 0.2434 -0.1247 0.0394  -0.0772 347 ARG A CB  
5317  C CG  . ARG A 347 ? 0.3839 0.3281 0.2683 -0.1114 0.0269  -0.0888 347 ARG A CG  
5318  C CD  . ARG A 347 ? 0.4695 0.3242 0.2822 -0.1228 0.0248  -0.0592 347 ARG A CD  
5319  N NE  . ARG A 347 ? 0.5999 0.3268 0.2911 -0.0896 0.0142  -0.0629 347 ARG A NE  
5320  C CZ  . ARG A 347 ? 0.6870 0.3297 0.3036 -0.1020 0.0009  -0.0678 347 ARG A CZ  
5321  N NH1 . ARG A 347 ? 0.6990 0.3332 0.3083 -0.1458 -0.0105 -0.0494 347 ARG A NH1 
5322  N NH2 . ARG A 347 ? 0.7466 0.3526 0.3154 -0.0809 -0.0004 -0.0570 347 ARG A NH2 
5336  N N   . GLU A 348 ? 0.2908 0.2490 0.1949 -0.0456 0.0245  -0.0594 348 GLU A N   
5337  C CA  . GLU A 348 ? 0.2503 0.2533 0.2047 -0.0282 0.0234  -0.0476 348 GLU A CA  
5338  C C   . GLU A 348 ? 0.2320 0.2595 0.2274 -0.0352 0.0224  -0.0415 348 GLU A C   
5339  O O   . GLU A 348 ? 0.2234 0.3164 0.2517 -0.0091 0.0209  -0.0315 348 GLU A O   
5340  C CB  . GLU A 348 ? 0.2605 0.2397 0.2196 -0.0316 0.0313  -0.0632 348 GLU A CB  
5341  C CG  . GLU A 348 ? 0.3227 0.1633 0.2342 -0.0257 0.0414  -0.0549 348 GLU A CG  
5342  C CD  . GLU A 348 ? 0.3583 0.1852 0.2465 -0.0277 0.0533  -0.0391 348 GLU A CD  
5343  O OE1 . GLU A 348 ? 0.3043 0.2090 0.2431 -0.0439 0.0299  -0.0479 348 GLU A OE1 
5344  O OE2 . GLU A 348 ? 0.4018 0.1778 0.2585 -0.0154 0.0386  -0.0161 348 GLU A OE2 
5351  N N   . GLY A 349 ? 0.2589 0.2431 0.2223 -0.0407 0.0218  -0.0571 349 GLY A N   
5352  C CA  . GLY A 349 ? 0.2903 0.2381 0.2158 -0.0648 0.0392  -0.0219 349 GLY A CA  
5353  C C   . GLY A 349 ? 0.2263 0.2260 0.2008 -0.0345 0.0120  -0.0215 349 GLY A C   
5354  O O   . GLY A 349 ? 0.2040 0.1985 0.2055 -0.0262 0.0046  -0.0227 349 GLY A O   
5358  N N   . LEU A 350 ? 0.2035 0.2831 0.1926 -0.0174 0.0158  -0.0220 350 LEU A N   
5359  C CA  . LEU A 350 ? 0.2160 0.2628 0.1789 -0.0067 0.0086  -0.0294 350 LEU A CA  
5360  C C   . LEU A 350 ? 0.2053 0.2206 0.1818 0.0001  -0.0012 -0.0142 350 LEU A C   
5361  O O   . LEU A 350 ? 0.2166 0.1596 0.1902 -0.0253 -0.0043 0.0090  350 LEU A O   
5362  C CB  . LEU A 350 ? 0.2260 0.2466 0.1747 0.0253  0.0058  -0.0602 350 LEU A CB  
5363  C CG  . LEU A 350 ? 0.2469 0.2189 0.1842 0.0266  -0.0196 -0.0373 350 LEU A CG  
5364  C CD1 . LEU A 350 ? 0.2912 0.2486 0.1894 -0.0279 0.0118  -0.0414 350 LEU A CD1 
5365  C CD2 . LEU A 350 ? 0.2875 0.1951 0.1877 -0.0181 0.0033  -0.0329 350 LEU A CD2 
5377  N N   . THR A 351 ? 0.1980 0.2234 0.1838 -0.0207 0.0096  -0.0165 351 THR A N   
5378  C CA  . THR A 351 ? 0.1810 0.2212 0.1905 0.0062  0.0193  -0.0061 351 THR A CA  
5379  C C   . THR A 351 ? 0.1903 0.2115 0.1893 0.0180  0.0179  -0.0282 351 THR A C   
5380  O O   . THR A 351 ? 0.2139 0.2159 0.1882 -0.0149 0.0102  -0.0389 351 THR A O   
5381  C CB  . THR A 351 ? 0.1972 0.2710 0.2067 -0.0189 0.0269  -0.0100 351 THR A CB  
5382  O OG1 . THR A 351 ? 0.2297 0.3191 0.2443 0.0117  0.0379  0.0103  351 THR A OG1 
5383  C CG2 . THR A 351 ? 0.2187 0.2864 0.2033 -0.0255 0.0179  -0.0092 351 THR A CG2 
5391  N N   . ALA A 352 ? 0.2473 0.1964 0.1929 -0.0071 0.0151  -0.0428 352 ALA A N   
5392  C CA  . ALA A 352 ? 0.2276 0.2149 0.1862 -0.0018 0.0070  -0.0363 352 ALA A CA  
5393  C C   . ALA A 352 ? 0.2459 0.2429 0.1911 0.0094  0.0249  -0.0437 352 ALA A C   
5394  O O   . ALA A 352 ? 0.2365 0.2685 0.1916 0.0005  0.0112  -0.0479 352 ALA A O   
5395  C CB  . ALA A 352 ? 0.2222 0.2885 0.1912 -0.0518 0.0030  -0.0435 352 ALA A CB  
5401  N N   . ASN A 353 ? 0.2348 0.1962 0.1981 0.0481  0.0380  -0.0285 353 ASN A N   
5402  C CA  . ASN A 353 ? 0.2459 0.1831 0.1977 0.0169  0.0333  -0.0029 353 ASN A CA  
5403  C C   . ASN A 353 ? 0.2392 0.2106 0.2020 0.0315  0.0365  -0.0244 353 ASN A C   
5404  O O   . ASN A 353 ? 0.2436 0.2211 0.2207 0.0179  0.0349  -0.0463 353 ASN A O   
5405  C CB  . ASN A 353 ? 0.2858 0.1806 0.2029 -0.0048 0.0304  -0.0021 353 ASN A CB  
5406  C CG  . ASN A 353 ? 0.2645 0.2020 0.2155 -0.0027 0.0368  -0.0129 353 ASN A CG  
5407  O OD1 . ASN A 353 ? 0.2948 0.2264 0.2322 0.0245  0.0381  -0.0303 353 ASN A OD1 
5408  N ND2 . ASN A 353 ? 0.2446 0.2285 0.2345 0.0074  0.0068  0.0159  353 ASN A ND2 
5415  N N   . ALA A 354 ? 0.2104 0.2179 0.1843 0.0201  0.0080  -0.0493 354 ALA A N   
5416  C CA  . ALA A 354 ? 0.1842 0.2435 0.1784 -0.0127 0.0221  -0.0527 354 ALA A CA  
5417  C C   . ALA A 354 ? 0.2044 0.2429 0.1800 -0.0421 -0.0076 -0.0607 354 ALA A C   
5418  O O   . ALA A 354 ? 0.1861 0.2421 0.1908 -0.0055 -0.0225 -0.0576 354 ALA A O   
5419  C CB  . ALA A 354 ? 0.1970 0.2504 0.1869 -0.0086 0.0408  -0.0367 354 ALA A CB  
5425  N N   . ALA A 355 ? 0.2037 0.2321 0.1836 -0.0037 0.0064  -0.0484 355 ALA A N   
5426  C CA  . ALA A 355 ? 0.2030 0.2306 0.2002 -0.0072 0.0043  -0.0484 355 ALA A CA  
5427  C C   . ALA A 355 ? 0.1852 0.2563 0.2039 -0.0108 0.0075  -0.0604 355 ALA A C   
5428  O O   . ALA A 355 ? 0.1905 0.2527 0.2024 0.0024  0.0179  -0.0476 355 ALA A O   
5429  C CB  . ALA A 355 ? 0.1966 0.2386 0.2047 -0.0308 0.0059  -0.0404 355 ALA A CB  
5435  N N   . GLU A 356 ? 0.2041 0.2296 0.2124 -0.0209 0.0197  -0.0700 356 GLU A N   
5436  C CA  . GLU A 356 ? 0.2317 0.2384 0.2385 0.0211  0.0062  -0.0813 356 GLU A CA  
5437  C C   . GLU A 356 ? 0.1620 0.2268 0.2276 -0.0381 0.0278  -0.0491 356 GLU A C   
5438  O O   . GLU A 356 ? 0.2044 0.2441 0.2282 -0.0354 0.0408  -0.0295 356 GLU A O   
5439  C CB  . GLU A 356 ? 0.3568 0.3096 0.2792 0.0249  -0.0134 -0.1136 356 GLU A CB  
5440  C CG  . GLU A 356 ? 0.4973 0.3792 0.3102 -0.0068 -0.0411 -0.1185 356 GLU A CG  
5441  C CD  . GLU A 356 ? 0.6599 0.5222 0.3505 -0.0265 -0.0891 -0.0894 356 GLU A CD  
5442  O OE1 . GLU A 356 ? 0.7554 0.5425 0.3723 -0.0465 -0.1175 -0.0765 356 GLU A OE1 
5443  O OE2 . GLU A 356 ? 0.6656 0.5919 0.3585 -0.0279 -0.0903 -0.0832 356 GLU A OE2 
5450  N N   . THR A 357 ? 0.1757 0.2006 0.2389 -0.0314 0.0519  -0.0392 357 THR A N   
5451  C CA  . THR A 357 ? 0.2169 0.1801 0.2268 0.0161  0.0349  -0.0300 357 THR A CA  
5452  C C   . THR A 357 ? 0.2262 0.1933 0.2184 0.0312  0.0309  -0.0173 357 THR A C   
5453  O O   . THR A 357 ? 0.2139 0.2280 0.2229 0.0298  0.0487  -0.0042 357 THR A O   
5454  C CB  . THR A 357 ? 0.2160 0.1891 0.2433 0.0255  0.0172  -0.0253 357 THR A CB  
5455  O OG1 . THR A 357 ? 0.2435 0.2471 0.2577 0.0246  0.0205  -0.0382 357 THR A OG1 
5456  C CG2 . THR A 357 ? 0.2243 0.2099 0.2474 -0.0159 0.0165  -0.0144 357 THR A CG2 
5464  N N   . GLY A 358 ? 0.2026 0.1781 0.2061 0.0204  0.0105  -0.0536 358 GLY A N   
5465  C CA  . GLY A 358 ? 0.1993 0.1864 0.1956 -0.0063 0.0114  -0.0156 358 GLY A CA  
5466  C C   . GLY A 358 ? 0.1900 0.2232 0.1949 0.0040  0.0236  -0.0152 358 GLY A C   
5467  O O   . GLY A 358 ? 0.1764 0.2309 0.1963 0.0280  0.0230  0.0005  358 GLY A O   
5471  N N   . ALA A 359 ? 0.1955 0.2202 0.2076 -0.0091 0.0179  -0.0036 359 ALA A N   
5472  C CA  . ALA A 359 ? 0.1544 0.2046 0.2090 -0.0008 0.0237  0.0023  359 ALA A CA  
5473  C C   . ALA A 359 ? 0.1958 0.2245 0.2155 0.0003  0.0273  -0.0240 359 ALA A C   
5474  O O   . ALA A 359 ? 0.1959 0.2350 0.2303 -0.0131 0.0025  -0.0021 359 ALA A O   
5475  C CB  . ALA A 359 ? 0.1618 0.2656 0.2113 -0.0284 0.0366  0.0064  359 ALA A CB  
5481  N N   . TYR A 360 ? 0.1807 0.1924 0.2119 0.0055  0.0286  -0.0378 360 TYR A N   
5482  C CA  . TYR A 360 ? 0.2226 0.2222 0.2118 -0.0198 0.0249  -0.0430 360 TYR A CA  
5483  C C   . TYR A 360 ? 0.1670 0.2194 0.2093 -0.0005 0.0275  -0.0293 360 TYR A C   
5484  O O   . TYR A 360 ? 0.1810 0.2328 0.2091 0.0117  0.0088  -0.0332 360 TYR A O   
5485  C CB  . TYR A 360 ? 0.2627 0.2141 0.2007 -0.0289 0.0197  -0.0553 360 TYR A CB  
5486  C CG  . TYR A 360 ? 0.2400 0.1732 0.1808 0.0321  0.0256  -0.0339 360 TYR A CG  
5487  C CD1 . TYR A 360 ? 0.2130 0.2277 0.1836 0.0285  0.0338  -0.0241 360 TYR A CD1 
5488  C CD2 . TYR A 360 ? 0.1804 0.1960 0.1821 0.0142  0.0067  0.0049  360 TYR A CD2 
5489  C CE1 . TYR A 360 ? 0.2272 0.2568 0.1876 0.0477  0.0496  -0.0219 360 TYR A CE1 
5490  C CE2 . TYR A 360 ? 0.2188 0.2341 0.1885 0.0063  0.0128  0.0054  360 TYR A CE2 
5491  C CZ  . TYR A 360 ? 0.2474 0.2634 0.2007 0.0145  0.0308  -0.0153 360 TYR A CZ  
5492  O OH  . TYR A 360 ? 0.2803 0.2751 0.2186 0.0067  0.0412  -0.0168 360 TYR A OH  
5502  N N   . LEU A 361 ? 0.2029 0.1604 0.1904 0.0050  0.0247  -0.0048 361 LEU A N   
5503  C CA  . LEU A 361 ? 0.2099 0.1386 0.1858 -0.0184 0.0320  0.0032  361 LEU A CA  
5504  C C   . LEU A 361 ? 0.1766 0.1575 0.1828 -0.0029 0.0244  -0.0142 361 LEU A C   
5505  O O   . LEU A 361 ? 0.1749 0.2023 0.1928 0.0004  0.0032  0.0108  361 LEU A O   
5506  C CB  . LEU A 361 ? 0.2290 0.1699 0.1725 0.0058  0.0412  -0.0130 361 LEU A CB  
5507  C CG  . LEU A 361 ? 0.2025 0.1939 0.1555 0.0125  0.0135  -0.0218 361 LEU A CG  
5508  C CD1 . LEU A 361 ? 0.2404 0.2604 0.1436 0.0122  0.0080  -0.0168 361 LEU A CD1 
5509  C CD2 . LEU A 361 ? 0.2492 0.1891 0.1696 -0.0008 0.0175  -0.0233 361 LEU A CD2 
5521  N N   . GLN A 362 ? 0.1938 0.1982 0.1934 -0.0036 0.0118  -0.0029 362 GLN A N   
5522  C CA  . GLN A 362 ? 0.1684 0.1896 0.2029 0.0138  0.0109  -0.0027 362 GLN A CA  
5523  C C   . GLN A 362 ? 0.1605 0.2183 0.2128 0.0061  0.0189  0.0028  362 GLN A C   
5524  O O   . GLN A 362 ? 0.1600 0.2266 0.2181 0.0303  0.0224  0.0028  362 GLN A O   
5525  C CB  . GLN A 362 ? 0.1619 0.1751 0.1942 0.0167  0.0009  -0.0042 362 GLN A CB  
5526  C CG  . GLN A 362 ? 0.1810 0.1937 0.1948 0.0063  0.0148  -0.0308 362 GLN A CG  
5527  C CD  . GLN A 362 ? 0.1756 0.2093 0.1994 0.0099  0.0034  -0.0323 362 GLN A CD  
5528  O OE1 . GLN A 362 ? 0.1808 0.2471 0.2079 -0.0283 0.0108  -0.0470 362 GLN A OE1 
5529  N NE2 . GLN A 362 ? 0.2027 0.2224 0.1987 0.0177  0.0132  -0.0045 362 GLN A NE2 
5538  N N   . GLN A 363 ? 0.1604 0.1918 0.2064 -0.0214 0.0138  -0.0026 363 GLN A N   
5539  C CA  . GLN A 363 ? 0.1819 0.1885 0.2184 0.0082  0.0225  0.0053  363 GLN A CA  
5540  C C   . GLN A 363 ? 0.2249 0.1933 0.2294 0.0137  0.0501  0.0224  363 GLN A C   
5541  O O   . GLN A 363 ? 0.2103 0.1938 0.2443 0.0301  0.0536  0.0018  363 GLN A O   
5542  C CB  . GLN A 363 ? 0.2826 0.2869 0.2193 0.0004  -0.0161 0.0170  363 GLN A CB  
5543  C CG  . GLN A 363 ? 0.4350 0.3797 0.2448 -0.0168 -0.0146 -0.0025 363 GLN A CG  
5544  C CD  . GLN A 363 ? 0.5848 0.4295 0.2676 -0.0269 -0.0542 -0.0208 363 GLN A CD  
5545  O OE1 . GLN A 363 ? 0.6727 0.3742 0.2741 -0.0246 -0.0487 -0.0414 363 GLN A OE1 
5546  N NE2 . GLN A 363 ? 0.6437 0.4670 0.2822 -0.0482 -0.0594 -0.0299 363 GLN A NE2 
5555  N N   . CYS A 364 ? 0.2318 0.2189 0.2208 0.0183  0.0525  0.0167  364 CYS A N   
5556  C CA  . CYS A 364 ? 0.1921 0.2116 0.2191 0.0308  0.0377  0.0132  364 CYS A CA  
5557  C C   . CYS A 364 ? 0.1653 0.1786 0.2102 -0.0051 0.0169  -0.0027 364 CYS A C   
5558  O O   . CYS A 364 ? 0.1931 0.1945 0.2015 0.0198  0.0088  -0.0256 364 CYS A O   
5559  C CB  . CYS A 364 ? 0.2128 0.2316 0.2333 -0.0303 0.0493  0.0034  364 CYS A CB  
5560  S SG  . CYS A 364 ? 0.2568 0.2361 0.2603 0.0004  0.0241  -0.0037 364 CYS A SG  
5566  N N   A MET A 365 ? 0.1729 0.1854 0.2170 0.0049  0.0074  0.0038  365 MET A N   
5567  N N   B MET A 365 ? 0.1787 0.1861 0.2175 0.0101  0.0116  -0.0021 365 MET A N   
5568  C CA  A MET A 365 ? 0.1850 0.1968 0.2025 0.0144  0.0141  -0.0021 365 MET A CA  
5569  C CA  B MET A 365 ? 0.1900 0.1948 0.2124 0.0218  0.0157  -0.0101 365 MET A CA  
5570  C C   A MET A 365 ? 0.1877 0.1896 0.2067 0.0047  0.0171  -0.0179 365 MET A C   
5571  C C   B MET A 365 ? 0.1903 0.1935 0.2135 0.0083  0.0167  -0.0118 365 MET A C   
5572  O O   A MET A 365 ? 0.1932 0.1957 0.2043 -0.0013 0.0206  -0.0109 365 MET A O   
5573  O O   B MET A 365 ? 0.1933 0.1941 0.2118 0.0073  0.0201  -0.0067 365 MET A O   
5574  C CB  A MET A 365 ? 0.1688 0.2171 0.1938 -0.0423 0.0093  0.0103  365 MET A CB  
5575  C CB  B MET A 365 ? 0.1829 0.2045 0.2127 -0.0010 0.0127  -0.0133 365 MET A CB  
5576  C CG  A MET A 365 ? 0.1824 0.1684 0.2019 -0.0323 -0.0042 0.0269  365 MET A CG  
5577  C CG  B MET A 365 ? 0.1928 0.1615 0.2224 0.0125  0.0010  -0.0118 365 MET A CG  
5578  S SD  A MET A 365 ? 0.2292 0.2210 0.2019 -0.0234 0.0097  0.0231  365 MET A SD  
5579  S SD  B MET A 365 ? 0.2254 0.1868 0.2296 0.0259  0.0065  -0.0168 365 MET A SD  
5580  C CE  A MET A 365 ? 0.1876 0.2342 0.2067 -0.0784 0.0394  0.0272  365 MET A CE  
5581  C CE  B MET A 365 ? 0.2040 0.1904 0.2359 -0.0021 0.0044  -0.0140 365 MET A CE  
5600  N N   . GLN A 366 ? 0.1920 0.2103 0.2175 -0.0109 0.0083  0.0125  366 GLN A N   
5601  C CA  . GLN A 366 ? 0.2233 0.2280 0.2283 -0.0172 -0.0119 0.0259  366 GLN A CA  
5602  C C   . GLN A 366 ? 0.2066 0.2084 0.2303 0.0141  0.0037  0.0359  366 GLN A C   
5603  O O   . GLN A 366 ? 0.2142 0.2589 0.2470 -0.0097 0.0004  -0.0020 366 GLN A O   
5604  C CB  . GLN A 366 ? 0.2394 0.2371 0.2469 0.0086  -0.0154 0.0225  366 GLN A CB  
5605  C CG  . GLN A 366 ? 0.2710 0.2534 0.2786 -0.0157 -0.0518 -0.0080 366 GLN A CG  
5606  C CD  . GLN A 366 ? 0.3342 0.3257 0.3243 -0.0225 -0.0452 -0.0135 366 GLN A CD  
5607  O OE1 . GLN A 366 ? 0.3652 0.2958 0.3593 -0.0642 -0.0619 0.0100  366 GLN A OE1 
5608  N NE2 . GLN A 366 ? 0.3289 0.3515 0.3287 -0.0033 -0.0205 -0.0201 366 GLN A NE2 
5617  N N   . GLN A 367 ? 0.1803 0.2164 0.2268 0.0408  0.0321  0.0142  367 GLN A N   
5618  C CA  . GLN A 367 ? 0.1914 0.3163 0.2718 0.0454  0.0310  0.0106  367 GLN A CA  
5619  C C   . GLN A 367 ? 0.1683 0.2770 0.2636 0.0159  0.0576  0.0028  367 GLN A C   
5620  O O   . GLN A 367 ? 0.2165 0.3244 0.2742 0.0138  0.0596  0.0153  367 GLN A O   
5621  C CB  . GLN A 367 ? 0.2311 0.4457 0.3250 0.0877  0.0407  0.0156  367 GLN A CB  
5622  C CG  . GLN A 367 ? 0.3984 0.6166 0.3671 0.0338  0.0346  0.0061  367 GLN A CG  
5623  C CD  . GLN A 367 ? 0.5859 0.7783 0.4159 -0.0216 0.0142  0.0004  367 GLN A CD  
5624  O OE1 . GLN A 367 ? 0.6806 0.8400 0.4395 -0.0511 0.0099  -0.0082 367 GLN A OE1 
5625  N NE2 . GLN A 367 ? 0.6560 0.8445 0.4307 -0.0393 0.0032  0.0040  367 GLN A NE2 
5634  N N   . THR A 368 ? 0.1884 0.2358 0.2543 0.0212  0.0460  0.0117  368 THR A N   
5635  C CA  . THR A 368 ? 0.1866 0.2155 0.2541 0.0556  0.0225  0.0156  368 THR A CA  
5636  C C   . THR A 368 ? 0.2116 0.2071 0.2669 0.0258  0.0139  0.0557  368 THR A C   
5637  O O   . THR A 368 ? 0.1976 0.2712 0.2960 0.0418  -0.0010 0.0172  368 THR A O   
5638  C CB  . THR A 368 ? 0.2266 0.2176 0.2413 0.0324  0.0183  0.0267  368 THR A CB  
5639  O OG1 . THR A 368 ? 0.2519 0.2361 0.2540 -0.0018 0.0364  0.0277  368 THR A OG1 
5640  C CG2 . THR A 368 ? 0.2069 0.2196 0.2444 0.0339  0.0097  0.0436  368 THR A CG2 
5648  N N   . PHE A 369 ? 0.1888 0.1497 0.2456 0.0190  0.0169  0.0564  369 PHE A N   
5649  C CA  . PHE A 369 ? 0.1980 0.2017 0.2337 0.0386  0.0291  0.0272  369 PHE A CA  
5650  C C   . PHE A 369 ? 0.2063 0.2104 0.2425 0.0239  -0.0075 0.0401  369 PHE A C   
5651  O O   . PHE A 369 ? 0.2377 0.1986 0.2502 -0.0100 -0.0158 0.0443  369 PHE A O   
5652  C CB  . PHE A 369 ? 0.1723 0.2301 0.2309 0.0238  0.0255  0.0268  369 PHE A CB  
5653  C CG  . PHE A 369 ? 0.1807 0.1895 0.2261 0.0064  0.0257  0.0507  369 PHE A CG  
5654  C CD1 . PHE A 369 ? 0.1618 0.2013 0.2225 0.0156  0.0126  0.0642  369 PHE A CD1 
5655  C CD2 . PHE A 369 ? 0.1962 0.1819 0.2153 0.0248  0.0246  0.0359  369 PHE A CD2 
5656  C CE1 . PHE A 369 ? 0.1843 0.2256 0.2291 -0.0155 0.0394  0.0588  369 PHE A CE1 
5657  C CE2 . PHE A 369 ? 0.2180 0.1542 0.2145 0.0232  0.0113  0.0408  369 PHE A CE2 
5658  C CZ  . PHE A 369 ? 0.2120 0.2224 0.2204 0.0285  0.0305  0.0501  369 PHE A CZ  
5668  N N   . GLY A 370 ? 0.2548 0.2044 0.2443 -0.0020 -0.0121 0.0630  370 GLY A N   
5669  C CA  . GLY A 370 ? 0.2953 0.2150 0.2505 0.0026  -0.0158 0.0731  370 GLY A CA  
5670  C C   . GLY A 370 ? 0.3075 0.2527 0.2698 -0.0327 0.0005  0.0806  370 GLY A C   
5671  O O   . GLY A 370 ? 0.3345 0.2630 0.2705 -0.0230 0.0058  0.0742  370 GLY A O   
5675  N N   . GLU A 371 ? 0.2481 0.2829 0.2913 -0.0294 0.0208  0.0794  371 GLU A N   
5676  C CA  . GLU A 371 ? 0.2716 0.3648 0.3129 -0.0566 0.0134  0.0923  371 GLU A CA  
5677  C C   . GLU A 371 ? 0.1737 0.4036 0.3000 -0.0591 0.0045  0.0882  371 GLU A C   
5678  O O   . GLU A 371 ? 0.2270 0.4504 0.3069 -0.0354 0.0204  0.1041  371 GLU A O   
5679  C CB  . GLU A 371 ? 0.3439 0.5248 0.3482 -0.0922 0.0387  0.1011  371 GLU A CB  
5680  C CG  . GLU A 371 ? 0.5220 0.6937 0.3892 -0.0273 0.0779  0.0810  371 GLU A CG  
5681  C CD  . GLU A 371 ? 0.7125 0.8270 0.4219 0.0490  0.0955  0.0736  371 GLU A CD  
5682  O OE1 . GLU A 371 ? 0.7221 0.8956 0.4365 0.0812  0.1115  0.0520  371 GLU A OE1 
5683  O OE2 . GLU A 371 ? 0.8306 0.8679 0.4462 0.0481  0.0749  0.0675  371 GLU A OE2 
5690  N N   . HIS A 372 ? 0.1729 0.3765 0.2894 -0.0023 -0.0038 0.0785  372 HIS A N   
5691  C CA  . HIS A 372 ? 0.2127 0.2936 0.2877 0.0085  -0.0084 0.0811  372 HIS A CA  
5692  C C   . HIS A 372 ? 0.1978 0.2904 0.2993 0.0158  -0.0133 0.0577  372 HIS A C   
5693  O O   . HIS A 372 ? 0.2008 0.2904 0.2969 -0.0232 -0.0221 0.0391  372 HIS A O   
5694  C CB  . HIS A 372 ? 0.2112 0.3048 0.2804 0.0363  -0.0082 0.0482  372 HIS A CB  
5695  C CG  . HIS A 372 ? 0.1787 0.2289 0.2729 0.0303  -0.0276 0.0394  372 HIS A CG  
5696  N ND1 . HIS A 372 ? 0.1803 0.2069 0.2678 0.0067  0.0041  0.0169  372 HIS A ND1 
5697  C CD2 . HIS A 372 ? 0.2501 0.2054 0.2696 0.0625  0.0085  0.0427  372 HIS A CD2 
5698  C CE1 . HIS A 372 ? 0.2201 0.1743 0.2640 0.0511  -0.0040 0.0392  372 HIS A CE1 
5699  N NE2 . HIS A 372 ? 0.2530 0.1898 0.2698 0.0293  -0.0080 0.0418  372 HIS A NE2 
5707  N N   . PRO A 373 ? 0.1987 0.2953 0.3143 0.0333  0.0101  0.0488  373 PRO A N   
5708  C CA  . PRO A 373 ? 0.1905 0.3326 0.3231 -0.0009 -0.0272 0.0310  373 PRO A CA  
5709  C C   . PRO A 373 ? 0.2133 0.2883 0.3204 -0.0335 -0.0379 0.0151  373 PRO A C   
5710  O O   . PRO A 373 ? 0.2408 0.2883 0.3251 -0.0443 -0.0321 0.0125  373 PRO A O   
5711  C CB  . PRO A 373 ? 0.1967 0.3453 0.3352 -0.0216 -0.0329 0.0228  373 PRO A CB  
5712  C CG  . PRO A 373 ? 0.2299 0.3587 0.3386 -0.0083 -0.0226 0.0312  373 PRO A CG  
5713  C CD  . PRO A 373 ? 0.2256 0.2921 0.3130 0.0312  -0.0181 0.0603  373 PRO A CD  
5721  N N   . LEU A 374 ? 0.1768 0.2616 0.3015 -0.0083 -0.0273 0.0004  374 LEU A N   
5722  C CA  . LEU A 374 ? 0.1993 0.2508 0.2813 -0.0052 -0.0374 0.0099  374 LEU A CA  
5723  C C   . LEU A 374 ? 0.1589 0.2081 0.2577 0.0240  -0.0349 0.0154  374 LEU A C   
5724  O O   . LEU A 374 ? 0.1685 0.2391 0.2442 0.0450  0.0055  0.0217  374 LEU A O   
5725  C CB  . LEU A 374 ? 0.2329 0.2742 0.2830 0.0004  -0.0537 -0.0066 374 LEU A CB  
5726  C CG  . LEU A 374 ? 0.2598 0.2987 0.2900 0.0231  -0.0576 -0.0023 374 LEU A CG  
5727  C CD1 . LEU A 374 ? 0.4014 0.2727 0.2917 0.0021  -0.0833 -0.0098 374 LEU A CD1 
5728  C CD2 . LEU A 374 ? 0.2139 0.2761 0.2898 0.0125  -0.0523 -0.0152 374 LEU A CD2 
5740  N N   . VAL A 375 ? 0.1879 0.2337 0.2558 0.0014  -0.0258 0.0214  375 VAL A N   
5741  C CA  . VAL A 375 ? 0.1457 0.2301 0.2466 -0.0048 -0.0144 0.0279  375 VAL A CA  
5742  C C   . VAL A 375 ? 0.1576 0.2196 0.2463 -0.0196 0.0079  0.0163  375 VAL A C   
5743  O O   . VAL A 375 ? 0.1944 0.2411 0.2388 0.0134  0.0215  0.0284  375 VAL A O   
5744  C CB  . VAL A 375 ? 0.1739 0.2316 0.2600 0.0016  -0.0066 0.0374  375 VAL A CB  
5745  C CG1 . VAL A 375 ? 0.1893 0.2028 0.2587 -0.0010 -0.0182 0.0227  375 VAL A CG1 
5746  C CG2 . VAL A 375 ? 0.1745 0.2289 0.2870 -0.0003 -0.0108 0.0463  375 VAL A CG2 
5756  N N   . GLY A 376 ? 0.1484 0.2371 0.2596 0.0163  -0.0155 0.0272  376 GLY A N   
5757  C CA  . GLY A 376 ? 0.1748 0.2385 0.2743 -0.0017 -0.0179 0.0362  376 GLY A CA  
5758  C C   . GLY A 376 ? 0.1952 0.1814 0.2735 -0.0132 -0.0198 0.0396  376 GLY A C   
5759  O O   . GLY A 376 ? 0.1831 0.2631 0.2754 -0.0265 -0.0182 0.0231  376 GLY A O   
5763  N N   . GLU A 377 ? 0.1666 0.1985 0.2639 -0.0245 -0.0210 0.0331  377 GLU A N   
5764  C CA  . GLU A 377 ? 0.1631 0.1653 0.2580 0.0223  -0.0186 0.0409  377 GLU A CA  
5765  C C   . GLU A 377 ? 0.1678 0.1501 0.2572 0.0201  -0.0146 0.0321  377 GLU A C   
5766  O O   . GLU A 377 ? 0.2023 0.1431 0.2643 0.0339  -0.0181 0.0257  377 GLU A O   
5767  C CB  . GLU A 377 ? 0.1615 0.1712 0.2512 -0.0009 -0.0249 0.0337  377 GLU A CB  
5768  C CG  . GLU A 377 ? 0.1894 0.1910 0.2609 -0.0111 -0.0188 -0.0011 377 GLU A CG  
5769  C CD  . GLU A 377 ? 0.2556 0.1716 0.2526 0.0017  -0.0118 0.0220  377 GLU A CD  
5770  O OE1 . GLU A 377 ? 0.1783 0.2094 0.2536 -0.0060 -0.0265 0.0133  377 GLU A OE1 
5771  O OE2 . GLU A 377 ? 0.3533 0.2382 0.2473 0.0386  0.0178  0.0279  377 GLU A OE2 
5778  N N   . VAL A 378 ? 0.1738 0.1742 0.2611 0.0012  -0.0135 0.0123  378 VAL A N   
5779  C CA  . VAL A 378 ? 0.1901 0.1551 0.2533 0.0053  -0.0090 -0.0051 378 VAL A CA  
5780  C C   . VAL A 378 ? 0.1610 0.1727 0.2274 -0.0003 -0.0076 0.0127  378 VAL A C   
5781  O O   . VAL A 378 ? 0.1912 0.2111 0.2188 -0.0274 0.0183  0.0353  378 VAL A O   
5782  C CB  . VAL A 378 ? 0.2226 0.1973 0.2835 0.0020  -0.0035 -0.0427 378 VAL A CB  
5783  C CG1 . VAL A 378 ? 0.2044 0.2009 0.3003 0.0113  0.0241  -0.0457 378 VAL A CG1 
5784  C CG2 . VAL A 378 ? 0.2329 0.2122 0.2886 -0.0080 -0.0305 -0.0466 378 VAL A CG2 
5794  N N   . ARG A 379 ? 0.1759 0.1467 0.2124 -0.0245 0.0234  0.0053  379 ARG A N   
5795  C CA  . ARG A 379 ? 0.1298 0.1739 0.1925 -0.0020 0.0157  0.0195  379 ARG A CA  
5796  C C   . ARG A 379 ? 0.1503 0.1837 0.1767 0.0119  -0.0002 0.0025  379 ARG A C   
5797  O O   . ARG A 379 ? 0.1736 0.2013 0.1919 0.0104  -0.0088 0.0093  379 ARG A O   
5798  C CB  . ARG A 379 ? 0.1565 0.1903 0.2071 -0.0296 -0.0024 -0.0039 379 ARG A CB  
5799  C CG  . ARG A 379 ? 0.1803 0.1821 0.2130 -0.0427 -0.0098 -0.0043 379 ARG A CG  
5800  C CD  . ARG A 379 ? 0.1842 0.1664 0.2258 -0.0204 0.0103  -0.0051 379 ARG A CD  
5801  N NE  . ARG A 379 ? 0.1437 0.1509 0.2293 -0.0074 0.0146  0.0006  379 ARG A NE  
5802  C CZ  . ARG A 379 ? 0.1774 0.1707 0.2355 -0.0390 0.0075  0.0092  379 ARG A CZ  
5803  N NH1 . ARG A 379 ? 0.1517 0.1431 0.2530 0.0177  -0.0038 0.0280  379 ARG A NH1 
5804  N NH2 . ARG A 379 ? 0.1792 0.1678 0.2311 -0.0151 0.0025  0.0033  379 ARG A NH2 
5818  N N   . GLY A 380 ? 0.1532 0.1869 0.1656 -0.0212 0.0008  0.0224  380 GLY A N   
5819  C CA  . GLY A 380 ? 0.1730 0.2021 0.1671 -0.0146 0.0154  -0.0091 380 GLY A CA  
5820  C C   . GLY A 380 ? 0.1453 0.1932 0.1596 0.0014  0.0177  0.0008  380 GLY A C   
5821  O O   . GLY A 380 ? 0.1868 0.1950 0.1640 -0.0234 0.0145  0.0268  380 GLY A O   
5825  N N   . VAL A 381 ? 0.1786 0.2074 0.1615 -0.0488 0.0296  -0.0095 381 VAL A N   
5826  C CA  . VAL A 381 ? 0.1969 0.1894 0.1607 -0.0105 0.0284  -0.0027 381 VAL A CA  
5827  C C   . VAL A 381 ? 0.1881 0.1620 0.1663 0.0004  0.0260  -0.0061 381 VAL A C   
5828  O O   . VAL A 381 ? 0.1741 0.1792 0.1620 -0.0082 0.0195  -0.0078 381 VAL A O   
5829  C CB  . VAL A 381 ? 0.2039 0.1857 0.1652 0.0065  0.0137  0.0031  381 VAL A CB  
5830  C CG1 . VAL A 381 ? 0.1925 0.1529 0.1774 -0.0125 -0.0013 -0.0058 381 VAL A CG1 
5831  C CG2 . VAL A 381 ? 0.2540 0.2146 0.1494 0.0187  0.0113  0.0036  381 VAL A CG2 
5841  N N   . GLY A 382 ? 0.2145 0.1765 0.1714 0.0134  0.0335  -0.0215 382 GLY A N   
5842  C CA  . GLY A 382 ? 0.2149 0.1483 0.1856 0.0106  0.0182  -0.0245 382 GLY A CA  
5843  C C   . GLY A 382 ? 0.1704 0.1607 0.1915 -0.0095 0.0226  -0.0154 382 GLY A C   
5844  O O   . GLY A 382 ? 0.1683 0.2023 0.2065 0.0268  0.0491  -0.0158 382 GLY A O   
5848  N N   . MET A 383 ? 0.1806 0.1430 0.1909 0.0028  0.0133  0.0184  383 MET A N   
5849  C CA  . MET A 383 ? 0.1724 0.1264 0.2074 0.0003  0.0079  -0.0024 383 MET A CA  
5850  C C   . MET A 383 ? 0.1613 0.1529 0.1959 -0.0174 0.0108  0.0148  383 MET A C   
5851  O O   . MET A 383 ? 0.1889 0.1422 0.1845 0.0025  -0.0023 -0.0276 383 MET A O   
5852  C CB  . MET A 383 ? 0.1533 0.2277 0.2478 -0.0432 -0.0128 -0.0125 383 MET A CB  
5853  C CG  . MET A 383 ? 0.1930 0.2592 0.3008 -0.0091 0.0180  -0.0156 383 MET A CG  
5854  S SD  . MET A 383 ? 0.2227 0.2013 0.3461 0.0157  0.0394  -0.0667 383 MET A SD  
5855  C CE  . MET A 383 ? 0.2545 0.2880 0.3429 -0.0415 0.0099  -0.0590 383 MET A CE  
5865  N N   . LEU A 384 ? 0.1762 0.1504 0.1897 -0.0229 0.0183  0.0307  384 LEU A N   
5866  C CA  . LEU A 384 ? 0.1552 0.1634 0.1825 0.0135  0.0133  -0.0146 384 LEU A CA  
5867  C C   . LEU A 384 ? 0.1539 0.1550 0.1724 0.0074  -0.0096 0.0051  384 LEU A C   
5868  O O   . LEU A 384 ? 0.1763 0.1827 0.1706 0.0071  -0.0008 0.0019  384 LEU A O   
5869  C CB  . LEU A 384 ? 0.1666 0.1756 0.1759 0.0123  0.0126  -0.0224 384 LEU A CB  
5870  C CG  . LEU A 384 ? 0.1579 0.1454 0.1668 0.0171  0.0173  -0.0230 384 LEU A CG  
5871  C CD1 . LEU A 384 ? 0.1937 0.1923 0.1774 -0.0087 0.0052  -0.0175 384 LEU A CD1 
5872  C CD2 . LEU A 384 ? 0.2019 0.1847 0.1701 -0.0182 0.0097  -0.0013 384 LEU A CD2 
5884  N N   . ALA A 385 ? 0.1453 0.1914 0.1914 0.0226  -0.0085 0.0028  385 ALA A N   
5885  C CA  . ALA A 385 ? 0.1463 0.1610 0.1926 0.0177  0.0037  0.0105  385 ALA A CA  
5886  C C   . ALA A 385 ? 0.1425 0.1585 0.1932 0.0162  0.0075  0.0014  385 ALA A C   
5887  O O   . ALA A 385 ? 0.1564 0.1911 0.2003 0.0081  0.0078  -0.0013 385 ALA A O   
5888  C CB  . ALA A 385 ? 0.1464 0.2002 0.1995 0.0165  0.0111  -0.0210 385 ALA A CB  
5894  N N   . ALA A 386 ? 0.1675 0.1777 0.1822 -0.0223 -0.0009 -0.0127 386 ALA A N   
5895  C CA  . ALA A 386 ? 0.1734 0.1751 0.1884 -0.0256 0.0165  -0.0402 386 ALA A CA  
5896  C C   . ALA A 386 ? 0.2035 0.1665 0.1968 -0.0060 0.0273  -0.0294 386 ALA A C   
5897  O O   . ALA A 386 ? 0.1756 0.1706 0.2114 -0.0057 0.0167  -0.0032 386 ALA A O   
5898  C CB  . ALA A 386 ? 0.2220 0.1597 0.2043 -0.0509 0.0106  -0.0387 386 ALA A CB  
5904  N N   . LEU A 387 ? 0.1847 0.1485 0.1991 -0.0050 0.0116  0.0078  387 LEU A N   
5905  C CA  . LEU A 387 ? 0.1531 0.1652 0.2299 0.0310  0.0002  0.0189  387 LEU A CA  
5906  C C   . LEU A 387 ? 0.1466 0.1768 0.2234 -0.0120 0.0039  0.0124  387 LEU A C   
5907  O O   . LEU A 387 ? 0.2118 0.1962 0.2081 -0.0075 0.0130  -0.0037 387 LEU A O   
5908  C CB  . LEU A 387 ? 0.1264 0.1748 0.2597 0.0276  0.0025  0.0117  387 LEU A CB  
5909  C CG  . LEU A 387 ? 0.1555 0.1970 0.2620 0.0219  -0.0124 0.0219  387 LEU A CG  
5910  C CD1 . LEU A 387 ? 0.1852 0.2260 0.2720 0.0140  -0.0042 0.0264  387 LEU A CD1 
5911  C CD2 . LEU A 387 ? 0.2059 0.1994 0.2673 0.0192  0.0204  0.0234  387 LEU A CD2 
5923  N N   . GLU A 388 ? 0.1765 0.1853 0.2321 0.0023  -0.0024 0.0318  388 GLU A N   
5924  C CA  . GLU A 388 ? 0.1391 0.1959 0.2433 0.0083  -0.0288 0.0098  388 GLU A CA  
5925  C C   . GLU A 388 ? 0.1594 0.2165 0.2637 0.0056  -0.0244 0.0067  388 GLU A C   
5926  O O   . GLU A 388 ? 0.1651 0.2140 0.2661 0.0109  -0.0247 0.0073  388 GLU A O   
5927  C CB  . GLU A 388 ? 0.1314 0.1837 0.2414 -0.0159 -0.0400 0.0100  388 GLU A CB  
5928  C CG  . GLU A 388 ? 0.1747 0.1818 0.2484 -0.0212 -0.0295 0.0049  388 GLU A CG  
5929  C CD  . GLU A 388 ? 0.1969 0.1695 0.2453 -0.0053 -0.0468 0.0176  388 GLU A CD  
5930  O OE1 . GLU A 388 ? 0.1676 0.1858 0.2508 0.0251  -0.0429 0.0181  388 GLU A OE1 
5931  O OE2 . GLU A 388 ? 0.2010 0.1958 0.2435 -0.0095 -0.0476 -0.0062 388 GLU A OE2 
5938  N N   . PHE A 389 ? 0.1547 0.2112 0.2758 0.0159  -0.0470 0.0200  389 PHE A N   
5939  C CA  . PHE A 389 ? 0.1788 0.2149 0.2971 -0.0030 -0.0391 0.0268  389 PHE A CA  
5940  C C   . PHE A 389 ? 0.2014 0.2058 0.3291 -0.0174 -0.0516 0.0011  389 PHE A C   
5941  O O   . PHE A 389 ? 0.1959 0.1945 0.3503 0.0110  -0.0364 -0.0168 389 PHE A O   
5942  C CB  . PHE A 389 ? 0.1701 0.1680 0.2874 0.0127  -0.0407 0.0397  389 PHE A CB  
5943  C CG  . PHE A 389 ? 0.1456 0.1363 0.2798 0.0084  -0.0031 0.0194  389 PHE A CG  
5944  C CD1 . PHE A 389 ? 0.1619 0.1343 0.2811 0.0314  0.0034  0.0036  389 PHE A CD1 
5945  C CD2 . PHE A 389 ? 0.2099 0.1552 0.2664 0.0502  -0.0172 0.0249  389 PHE A CD2 
5946  C CE1 . PHE A 389 ? 0.1660 0.1383 0.2736 -0.0020 0.0091  -0.0080 389 PHE A CE1 
5947  C CE2 . PHE A 389 ? 0.1632 0.1606 0.2605 0.0701  0.0031  0.0391  389 PHE A CE2 
5948  C CZ  . PHE A 389 ? 0.1478 0.1686 0.2668 0.0553  -0.0112 0.0115  389 PHE A CZ  
5958  N N   . SER A 390 ? 0.1570 0.1779 0.3455 -0.0330 -0.0641 0.0191  390 SER A N   
5959  C CA  . SER A 390 ? 0.1611 0.1532 0.3709 -0.0436 -0.0875 0.0736  390 SER A CA  
5960  C C   . SER A 390 ? 0.1857 0.1736 0.3966 -0.0449 -0.0804 0.0649  390 SER A C   
5961  O O   . SER A 390 ? 0.1843 0.2285 0.4078 0.0222  -0.0856 0.0418  390 SER A O   
5962  C CB  . SER A 390 ? 0.2065 0.2014 0.3709 -0.0370 -0.0850 0.0813  390 SER A CB  
5963  O OG  . SER A 390 ? 0.2557 0.2784 0.3722 -0.0369 -0.1069 0.0738  390 SER A OG  
5969  N N   . PRO A 391 ? 0.2105 0.2538 0.4188 -0.0653 -0.1012 0.0795  391 PRO A N   
5970  C CA  . PRO A 391 ? 0.2012 0.2797 0.4300 -0.0867 -0.1078 0.0843  391 PRO A CA  
5971  C C   . PRO A 391 ? 0.2218 0.3364 0.4457 -0.0709 -0.0879 0.0882  391 PRO A C   
5972  O O   . PRO A 391 ? 0.2038 0.4353 0.4601 -0.0397 -0.0761 0.1156  391 PRO A O   
5973  C CB  . PRO A 391 ? 0.2409 0.2750 0.4336 -0.0922 -0.1310 0.0632  391 PRO A CB  
5974  C CG  . PRO A 391 ? 0.2528 0.2814 0.4330 -0.1013 -0.1439 0.0405  391 PRO A CG  
5975  C CD  . PRO A 391 ? 0.2779 0.2573 0.4327 -0.0753 -0.1098 0.0768  391 PRO A CD  
5983  N N   . ALA A 392 ? 0.2651 0.2862 0.4413 -0.0629 -0.0902 0.0844  392 ALA A N   
5984  C CA  . ALA A 392 ? 0.3046 0.2947 0.4404 -0.0820 -0.0926 0.0682  392 ALA A CA  
5985  C C   . ALA A 392 ? 0.3030 0.2671 0.4249 -0.0817 -0.0953 0.0675  392 ALA A C   
5986  O O   . ALA A 392 ? 0.2987 0.2581 0.4185 -0.1023 -0.1025 0.0697  392 ALA A O   
5987  C CB  . ALA A 392 ? 0.3599 0.3177 0.4518 -0.0900 -0.1135 0.0439  392 ALA A CB  
5993  N N   . PRO A 393 ? 0.2758 0.2544 0.4206 -0.0785 -0.0910 0.0632  393 PRO A N   
5994  C CA  . PRO A 393 ? 0.2775 0.2682 0.4195 -0.0788 -0.0865 0.0669  393 PRO A CA  
5995  C C   . PRO A 393 ? 0.3244 0.3302 0.4229 -0.0761 -0.0912 0.0760  393 PRO A C   
5996  O O   . PRO A 393 ? 0.3243 0.3325 0.4208 -0.0505 -0.0939 0.0732  393 PRO A O   
5997  C CB  . PRO A 393 ? 0.2791 0.2342 0.4194 -0.0305 -0.0743 0.0774  393 PRO A CB  
5998  C CG  . PRO A 393 ? 0.3011 0.2534 0.4184 -0.0621 -0.0672 0.0793  393 PRO A CG  
5999  C CD  . PRO A 393 ? 0.2584 0.2757 0.4206 -0.0580 -0.0970 0.0685  393 PRO A CD  
6007  N N   . ALA A 394 ? 0.4001 0.3236 0.4315 -0.0665 -0.0769 0.1200  394 ALA A N   
6008  C CA  . ALA A 394 ? 0.4643 0.3645 0.4407 -0.0720 -0.0864 0.1308  394 ALA A CA  
6009  C C   . ALA A 394 ? 0.5388 0.3452 0.4464 -0.0573 -0.1234 0.1330  394 ALA A C   
6010  O O   . ALA A 394 ? 0.5840 0.3558 0.4405 -0.0023 -0.1265 0.1409  394 ALA A O   
6011  C CB  . ALA A 394 ? 0.4192 0.3757 0.4419 -0.0942 -0.0629 0.1379  394 ALA A CB  
6017  N N   . ARG A 395 ? 0.5363 0.3736 0.4650 -0.1070 -0.1378 0.1096  395 ARG A N   
6018  C CA  . ARG A 395 ? 0.5430 0.4078 0.4811 -0.0962 -0.1742 0.0638  395 ARG A CA  
6019  C C   . ARG A 395 ? 0.5480 0.3443 0.4735 -0.0123 -0.2079 0.0358  395 ARG A C   
6020  O O   . ARG A 395 ? 0.6106 0.3223 0.4715 0.0055  -0.2232 0.0121  395 ARG A O   
6021  C CB  . ARG A 395 ? 0.6272 0.5373 0.5094 -0.1281 -0.1706 0.0379  395 ARG A CB  
6022  C CG  . ARG A 395 ? 0.6888 0.6875 0.5416 -0.1641 -0.1601 0.0248  395 ARG A CG  
6023  C CD  . ARG A 395 ? 0.7817 0.8337 0.5777 -0.2134 -0.1371 0.0203  395 ARG A CD  
6024  N NE  . ARG A 395 ? 0.8973 0.9652 0.6039 -0.2287 -0.1289 0.0206  395 ARG A NE  
6025  C CZ  . ARG A 395 ? 0.9878 1.0538 0.6224 -0.2530 -0.1221 0.0267  395 ARG A CZ  
6026  N NH1 . ARG A 395 ? 1.0265 1.0806 0.6311 -0.2535 -0.1142 0.0305  395 ARG A NH1 
6027  N NH2 . ARG A 395 ? 1.0283 1.0840 0.6274 -0.2636 -0.1194 0.0256  395 ARG A NH2 
6041  N N   . ARG A 396 ? 0.4215 0.2780 0.4617 -0.0304 -0.2091 0.0350  396 ARG A N   
6042  C CA  . ARG A 396 ? 0.4009 0.2381 0.4457 0.0286  -0.1996 0.0232  396 ARG A CA  
6043  C C   . ARG A 396 ? 0.4359 0.2881 0.4630 0.0391  -0.2082 0.0048  396 ARG A C   
6044  O O   . ARG A 396 ? 0.4729 0.3235 0.4669 0.0534  -0.2165 -0.0120 396 ARG A O   
6045  C CB  . ARG A 396 ? 0.3701 0.2177 0.4232 0.0086  -0.1412 -0.0089 396 ARG A CB  
6046  C CG  . ARG A 396 ? 0.3239 0.2199 0.4035 -0.0426 -0.0895 -0.0314 396 ARG A CG  
6047  C CD  . ARG A 396 ? 0.2434 0.2410 0.3775 -0.0253 -0.0509 -0.0264 396 ARG A CD  
6048  N NE  . ARG A 396 ? 0.1833 0.2341 0.3689 -0.0338 -0.0182 0.0031  396 ARG A NE  
6049  C CZ  . ARG A 396 ? 0.2115 0.2106 0.3669 -0.0571 -0.0613 0.0092  396 ARG A CZ  
6050  N NH1 . ARG A 396 ? 0.2572 0.2369 0.3693 -0.0252 -0.0628 0.0021  396 ARG A NH1 
6051  N NH2 . ARG A 396 ? 0.2592 0.2293 0.3757 -0.0430 -0.0760 0.0241  396 ARG A NH2 
6065  N N   . ALA A 397 ? 0.3735 0.2960 0.4702 -0.0421 -0.2084 0.0235  397 ALA A N   
6066  C CA  . ALA A 397 ? 0.3417 0.2946 0.4796 -0.0508 -0.1777 0.0445  397 ALA A CA  
6067  C C   . ALA A 397 ? 0.3033 0.1994 0.4883 -0.0483 -0.1720 0.0642  397 ALA A C   
6068  O O   . ALA A 397 ? 0.2823 0.1942 0.4945 -0.0536 -0.1894 0.0468  397 ALA A O   
6069  C CB  . ALA A 397 ? 0.3244 0.3041 0.4651 -0.1401 -0.1526 0.0403  397 ALA A CB  
6075  N N   . PHE A 398 ? 0.3497 0.2133 0.4963 -0.0457 -0.1646 0.0559  398 PHE A N   
6076  C CA  . PHE A 398 ? 0.3767 0.2614 0.5014 -0.0425 -0.1455 0.0323  398 PHE A CA  
6077  C C   . PHE A 398 ? 0.3709 0.2527 0.4783 -0.0098 -0.1111 0.0059  398 PHE A C   
6078  O O   . PHE A 398 ? 0.3637 0.2310 0.4736 -0.0195 -0.1150 -0.0181 398 PHE A O   
6079  C CB  . PHE A 398 ? 0.3910 0.3197 0.5366 -0.0222 -0.1541 0.0195  398 PHE A CB  
6080  C CG  . PHE A 398 ? 0.4752 0.3699 0.5705 -0.0134 -0.1784 0.0015  398 PHE A CG  
6081  C CD1 . PHE A 398 ? 0.4503 0.3789 0.5850 -0.0427 -0.2049 0.0003  398 PHE A CD1 
6082  C CD2 . PHE A 398 ? 0.5372 0.4097 0.5860 -0.0279 -0.1868 -0.0173 398 PHE A CD2 
6083  C CE1 . PHE A 398 ? 0.4554 0.3812 0.5975 -0.1009 -0.2287 -0.0055 398 PHE A CE1 
6084  C CE2 . PHE A 398 ? 0.5365 0.4324 0.5904 -0.0130 -0.2096 -0.0029 398 PHE A CE2 
6085  C CZ  . PHE A 398 ? 0.4894 0.4046 0.5983 -0.0704 -0.2262 -0.0217 398 PHE A CZ  
6095  N N   . PHE A 399 ? 0.3537 0.2631 0.4475 -0.0043 -0.0983 0.0001  399 PHE A N   
6096  C CA  . PHE A 399 ? 0.2943 0.2261 0.4236 0.0174  -0.1067 -0.0148 399 PHE A CA  
6097  C C   . PHE A 399 ? 0.2887 0.2538 0.4186 -0.0014 -0.1291 -0.0548 399 PHE A C   
6098  O O   . PHE A 399 ? 0.3589 0.2635 0.4241 0.0093  -0.0971 -0.0869 399 PHE A O   
6099  C CB  . PHE A 399 ? 0.2850 0.2390 0.4062 -0.0018 -0.0741 0.0079  399 PHE A CB  
6100  C CG  . PHE A 399 ? 0.2203 0.2321 0.3858 0.0212  -0.0711 0.0189  399 PHE A CG  
6101  C CD1 . PHE A 399 ? 0.2283 0.2408 0.3765 0.0125  -0.0719 0.0221  399 PHE A CD1 
6102  C CD2 . PHE A 399 ? 0.2111 0.2180 0.3790 -0.0141 -0.0653 0.0192  399 PHE A CD2 
6103  C CE1 . PHE A 399 ? 0.2233 0.1994 0.3735 0.0216  -0.0552 0.0260  399 PHE A CE1 
6104  C CE2 . PHE A 399 ? 0.2290 0.1914 0.3660 -0.0013 -0.0668 0.0227  399 PHE A CE2 
6105  C CZ  . PHE A 399 ? 0.2363 0.1619 0.3658 0.0121  -0.0566 0.0192  399 PHE A CZ  
6115  N N   . ASP A 400 ? 0.3006 0.3134 0.4236 -0.0162 -0.1295 -0.0556 400 ASP A N   
6116  C CA  . ASP A 400 ? 0.3572 0.3101 0.4262 -0.0252 -0.1484 -0.0602 400 ASP A CA  
6117  C C   . ASP A 400 ? 0.3679 0.2899 0.4050 -0.0110 -0.1479 -0.0551 400 ASP A C   
6118  O O   . ASP A 400 ? 0.3638 0.2764 0.3910 0.0018  -0.1716 -0.0435 400 ASP A O   
6119  C CB  . ASP A 400 ? 0.3902 0.3632 0.4420 -0.0138 -0.1657 -0.0542 400 ASP A CB  
6120  C CG  . ASP A 400 ? 0.4333 0.4202 0.4568 -0.0345 -0.1783 -0.0755 400 ASP A CG  
6121  O OD1 . ASP A 400 ? 0.4600 0.4121 0.4559 -0.0285 -0.1656 -0.0849 400 ASP A OD1 
6122  O OD2 . ASP A 400 ? 0.5095 0.5345 0.4792 -0.0556 -0.1608 -0.0739 400 ASP A OD2 
6127  N N   . PRO A 401 ? 0.3964 0.2616 0.4023 0.0731  -0.1284 -0.0641 401 PRO A N   
6128  C CA  . PRO A 401 ? 0.3764 0.2846 0.3944 0.1094  -0.1107 -0.0638 401 PRO A CA  
6129  C C   . PRO A 401 ? 0.3601 0.3020 0.3766 0.1087  -0.0815 -0.0866 401 PRO A C   
6130  O O   . PRO A 401 ? 0.3252 0.2941 0.3668 0.1134  -0.0610 -0.1016 401 PRO A O   
6131  C CB  . PRO A 401 ? 0.4204 0.2471 0.4025 0.1302  -0.1032 -0.0586 401 PRO A CB  
6132  C CG  . PRO A 401 ? 0.4240 0.2794 0.4147 0.1183  -0.1049 -0.0564 401 PRO A CG  
6133  C CD  . PRO A 401 ? 0.3963 0.2406 0.4167 0.0735  -0.1208 -0.0556 401 PRO A CD  
6141  N N   . ALA A 402 ? 0.3980 0.2970 0.3605 0.1154  -0.0886 -0.1038 402 ALA A N   
6142  C CA  . ALA A 402 ? 0.4022 0.3183 0.3419 0.0571  -0.1152 -0.1156 402 ALA A CA  
6143  C C   . ALA A 402 ? 0.3430 0.3419 0.3299 0.0836  -0.1063 -0.0825 402 ALA A C   
6144  O O   . ALA A 402 ? 0.3795 0.3584 0.3278 0.1193  -0.0859 -0.0755 402 ALA A O   
6145  C CB  . ALA A 402 ? 0.4433 0.3098 0.3443 0.0103  -0.1255 -0.1503 402 ALA A CB  
6151  N N   . LEU A 403 ? 0.3093 0.3252 0.3169 0.0380  -0.0944 -0.0731 403 LEU A N   
6152  C CA  . LEU A 403 ? 0.2929 0.2748 0.3242 0.0436  -0.1007 -0.0390 403 LEU A CA  
6153  C C   . LEU A 403 ? 0.2659 0.2958 0.3063 0.0250  -0.0795 -0.0253 403 LEU A C   
6154  O O   . LEU A 403 ? 0.2562 0.2427 0.2994 -0.0030 -0.1014 -0.0069 403 LEU A O   
6155  C CB  . LEU A 403 ? 0.2875 0.3003 0.3419 0.0337  -0.1259 -0.0213 403 LEU A CB  
6156  C CG  . LEU A 403 ? 0.2946 0.3552 0.3542 0.0051  -0.1259 0.0109  403 LEU A CG  
6157  C CD1 . LEU A 403 ? 0.3533 0.3540 0.3645 -0.0140 -0.1047 -0.0070 403 LEU A CD1 
6158  C CD2 . LEU A 403 ? 0.3376 0.3944 0.3698 -0.0343 -0.1198 0.0259  403 LEU A CD2 
6170  N N   . LYS A 404 ? 0.2601 0.2584 0.2944 0.0324  -0.0775 -0.0525 404 LYS A N   
6171  C CA  . LYS A 404 ? 0.2367 0.2090 0.2945 0.0321  -0.0520 -0.0399 404 LYS A CA  
6172  C C   . LYS A 404 ? 0.2215 0.1992 0.2744 0.0583  -0.0546 -0.0278 404 LYS A C   
6173  O O   . LYS A 404 ? 0.2305 0.2046 0.2611 0.0593  -0.0688 -0.0207 404 LYS A O   
6174  C CB  . LYS A 404 ? 0.2974 0.3351 0.3171 0.0846  -0.0186 -0.0678 404 LYS A CB  
6175  C CG  . LYS A 404 ? 0.4238 0.4023 0.3488 0.1060  -0.0180 -0.0843 404 LYS A CG  
6176  C CD  . LYS A 404 ? 0.4834 0.4873 0.3779 0.1238  0.0020  -0.0853 404 LYS A CD  
6177  C CE  . LYS A 404 ? 0.5151 0.5740 0.4138 0.2093  0.0253  -0.0756 404 LYS A CE  
6178  N NZ  . LYS A 404 ? 0.5712 0.6506 0.4330 0.2119  0.0191  -0.0531 404 LYS A NZ  
6192  N N   . VAL A 405 ? 0.1987 0.1476 0.2751 0.0190  -0.0378 -0.0227 405 VAL A N   
6193  C CA  . VAL A 405 ? 0.2162 0.2018 0.2832 0.0469  -0.0674 -0.0015 405 VAL A CA  
6194  C C   . VAL A 405 ? 0.1623 0.1783 0.2724 0.0604  -0.0648 0.0112  405 VAL A C   
6195  O O   . VAL A 405 ? 0.2113 0.1370 0.2694 0.0281  -0.0609 0.0435  405 VAL A O   
6196  C CB  . VAL A 405 ? 0.1716 0.1708 0.2949 0.0449  -0.0755 -0.0004 405 VAL A CB  
6197  C CG1 . VAL A 405 ? 0.1959 0.2231 0.3085 0.0245  -0.0615 -0.0138 405 VAL A CG1 
6198  C CG2 . VAL A 405 ? 0.1861 0.1989 0.3044 0.0456  -0.0805 0.0102  405 VAL A CG2 
6208  N N   . GLY A 406 ? 0.1690 0.2526 0.2520 0.0637  -0.0601 -0.0268 406 GLY A N   
6209  C CA  . GLY A 406 ? 0.1702 0.2436 0.2529 0.0829  -0.0356 -0.0067 406 GLY A CA  
6210  C C   . GLY A 406 ? 0.1915 0.1964 0.2527 0.0580  -0.0190 -0.0279 406 GLY A C   
6211  O O   . GLY A 406 ? 0.1790 0.1612 0.2541 0.0656  -0.0395 -0.0143 406 GLY A O   
6215  N N   . PRO A 407 ? 0.1712 0.2376 0.2536 0.0355  0.0010  -0.0223 407 PRO A N   
6216  C CA  . PRO A 407 ? 0.1500 0.2524 0.2428 0.0292  0.0121  -0.0239 407 PRO A CA  
6217  C C   . PRO A 407 ? 0.1571 0.2356 0.2239 0.0056  0.0081  -0.0142 407 PRO A C   
6218  O O   . PRO A 407 ? 0.1917 0.2350 0.2138 0.0171  -0.0099 -0.0139 407 PRO A O   
6219  C CB  . PRO A 407 ? 0.1902 0.2941 0.2570 0.0316  0.0197  -0.0317 407 PRO A CB  
6220  C CG  . PRO A 407 ? 0.1885 0.2795 0.2554 0.0522  0.0247  -0.0346 407 PRO A CG  
6221  C CD  . PRO A 407 ? 0.2064 0.2603 0.2506 0.0730  0.0058  -0.0320 407 PRO A CD  
6229  N N   . ARG A 408 ? 0.1565 0.2091 0.2330 0.0525  0.0210  -0.0161 408 ARG A N   
6230  C CA  . ARG A 408 ? 0.1910 0.2186 0.2361 0.0260  -0.0120 -0.0101 408 ARG A CA  
6231  C C   . ARG A 408 ? 0.1779 0.2171 0.2350 0.0258  -0.0132 0.0075  408 ARG A C   
6232  O O   . ARG A 408 ? 0.1793 0.1982 0.2372 0.0126  0.0052  0.0040  408 ARG A O   
6233  C CB  . ARG A 408 ? 0.2203 0.2229 0.2519 0.0137  -0.0257 -0.0270 408 ARG A CB  
6234  C CG  . ARG A 408 ? 0.1993 0.2316 0.2495 0.0071  -0.0408 -0.0062 408 ARG A CG  
6235  C CD  . ARG A 408 ? 0.1386 0.2572 0.2725 0.0243  -0.0507 -0.0098 408 ARG A CD  
6236  N NE  . ARG A 408 ? 0.1423 0.2764 0.2988 0.0294  -0.0490 -0.0074 408 ARG A NE  
6237  C CZ  . ARG A 408 ? 0.2115 0.3015 0.3002 0.0318  -0.0324 0.0004  408 ARG A CZ  
6238  N NH1 . ARG A 408 ? 0.2236 0.2851 0.2954 0.0495  -0.0287 0.0026  408 ARG A NH1 
6239  N NH2 . ARG A 408 ? 0.2629 0.3353 0.2985 0.0169  -0.0278 0.0145  408 ARG A NH2 
6253  N N   . VAL A 409 ? 0.1681 0.2312 0.2177 0.0555  -0.0242 0.0037  409 VAL A N   
6254  C CA  . VAL A 409 ? 0.1582 0.2126 0.2199 0.0177  -0.0165 -0.0182 409 VAL A CA  
6255  C C   . VAL A 409 ? 0.1592 0.1917 0.2164 0.0536  -0.0123 -0.0154 409 VAL A C   
6256  O O   . VAL A 409 ? 0.2138 0.1837 0.2158 0.0558  0.0223  0.0024  409 VAL A O   
6257  C CB  . VAL A 409 ? 0.1470 0.1838 0.2343 0.0382  0.0117  -0.0090 409 VAL A CB  
6258  C CG1 . VAL A 409 ? 0.1404 0.2542 0.2365 0.0695  0.0001  0.0108  409 VAL A CG1 
6259  C CG2 . VAL A 409 ? 0.1481 0.2758 0.2330 0.0237  0.0415  0.0010  409 VAL A CG2 
6269  N N   . SER A 410 ? 0.2028 0.2295 0.2228 0.0463  -0.0079 -0.0169 410 SER A N   
6270  C CA  . SER A 410 ? 0.1730 0.2370 0.2249 0.0341  0.0020  -0.0264 410 SER A CA  
6271  C C   . SER A 410 ? 0.1737 0.1822 0.2181 0.0090  0.0070  -0.0179 410 SER A C   
6272  O O   . SER A 410 ? 0.1964 0.1566 0.2281 0.0030  -0.0075 -0.0185 410 SER A O   
6273  C CB  . SER A 410 ? 0.1893 0.2245 0.2335 0.0598  0.0038  -0.0167 410 SER A CB  
6274  O OG  . SER A 410 ? 0.1986 0.2487 0.2366 -0.0064 0.0158  -0.0268 410 SER A OG  
6280  N N   . ALA A 411 ? 0.1850 0.1492 0.2067 0.0167  -0.0045 -0.0068 411 ALA A N   
6281  C CA  . ALA A 411 ? 0.1942 0.1509 0.2096 0.0128  -0.0057 -0.0115 411 ALA A CA  
6282  C C   . ALA A 411 ? 0.2336 0.1383 0.2233 0.0140  -0.0106 0.0078  411 ALA A C   
6283  O O   . ALA A 411 ? 0.2473 0.1659 0.2239 0.0344  0.0049  0.0141  411 ALA A O   
6284  C CB  . ALA A 411 ? 0.1973 0.2213 0.2201 -0.0158 -0.0311 -0.0238 411 ALA A CB  
6290  N N   . ALA A 412 ? 0.2015 0.1803 0.2213 0.0580  -0.0092 0.0041  412 ALA A N   
6291  C CA  . ALA A 412 ? 0.1655 0.1639 0.2245 0.0369  0.0039  -0.0212 412 ALA A CA  
6292  C C   . ALA A 412 ? 0.1599 0.2098 0.2230 0.0676  0.0350  -0.0177 412 ALA A C   
6293  O O   . ALA A 412 ? 0.1886 0.1929 0.2505 0.0374  0.0138  -0.0066 412 ALA A O   
6294  C CB  . ALA A 412 ? 0.1797 0.1684 0.2250 0.0152  -0.0290 0.0006  412 ALA A CB  
6300  N N   . ALA A 413 ? 0.1685 0.2038 0.2071 0.0021  0.0312  -0.0014 413 ALA A N   
6301  C CA  . ALA A 413 ? 0.1612 0.1392 0.2059 0.0181  0.0296  0.0186  413 ALA A CA  
6302  C C   . ALA A 413 ? 0.2118 0.1739 0.2039 0.0212  0.0090  0.0096  413 ALA A C   
6303  O O   . ALA A 413 ? 0.2296 0.1673 0.2043 -0.0002 0.0059  0.0190  413 ALA A O   
6304  C CB  . ALA A 413 ? 0.2093 0.1465 0.2136 0.0467  0.0031  -0.0077 413 ALA A CB  
6310  N N   . MET A 414 ? 0.1909 0.2002 0.2165 0.0299  -0.0009 0.0033  414 MET A N   
6311  C CA  . MET A 414 ? 0.2293 0.2078 0.2221 0.0259  -0.0058 -0.0043 414 MET A CA  
6312  C C   . MET A 414 ? 0.2555 0.1865 0.2336 0.0395  -0.0064 0.0012  414 MET A C   
6313  O O   . MET A 414 ? 0.2713 0.1524 0.2439 0.0128  -0.0011 -0.0245 414 MET A O   
6314  C CB  . MET A 414 ? 0.2613 0.2703 0.2379 -0.0512 0.0118  0.0196  414 MET A CB  
6315  C CG  . MET A 414 ? 0.2859 0.3293 0.2641 -0.0382 0.0036  -0.0092 414 MET A CG  
6316  S SD  . MET A 414 ? 0.2518 0.3444 0.2600 -0.0090 -0.0073 0.0086  414 MET A SD  
6317  C CE  . MET A 414 ? 0.3121 0.3573 0.2616 0.0379  0.0090  0.0423  414 MET A CE  
6327  N N   . SER A 415 ? 0.2604 0.2211 0.2419 0.0429  -0.0096 0.0195  415 SER A N   
6328  C CA  . SER A 415 ? 0.2768 0.2292 0.2579 0.0453  -0.0371 -0.0128 415 SER A CA  
6329  C C   . SER A 415 ? 0.2734 0.2193 0.2724 0.0924  -0.0091 0.0019  415 SER A C   
6330  O O   . SER A 415 ? 0.3404 0.2058 0.2877 0.0872  -0.0230 0.0197  415 SER A O   
6331  C CB  . SER A 415 ? 0.3368 0.2704 0.2802 0.0261  -0.0521 -0.0551 415 SER A CB  
6332  O OG  . SER A 415 ? 0.4090 0.3871 0.3214 0.0045  -0.0658 -0.0236 415 SER A OG  
6338  N N   . GLU A 416 ? 0.2405 0.1967 0.2572 0.0640  -0.0085 -0.0100 416 GLU A N   
6339  C CA  . GLU A 416 ? 0.2575 0.1999 0.2562 0.0497  0.0040  -0.0170 416 GLU A CA  
6340  C C   . GLU A 416 ? 0.2713 0.1798 0.2608 0.0332  0.0115  -0.0117 416 GLU A C   
6341  O O   . GLU A 416 ? 0.2591 0.1948 0.2758 0.0244  0.0196  -0.0092 416 GLU A O   
6342  C CB  . GLU A 416 ? 0.2957 0.1866 0.2551 0.0658  -0.0107 -0.0047 416 GLU A CB  
6343  C CG  . GLU A 416 ? 0.2910 0.1866 0.2526 0.0860  -0.0089 -0.0013 416 GLU A CG  
6344  C CD  . GLU A 416 ? 0.3078 0.2209 0.2640 0.0663  -0.0158 -0.0122 416 GLU A CD  
6345  O OE1 . GLU A 416 ? 0.3083 0.2044 0.2580 0.0644  -0.0275 -0.0056 416 GLU A OE1 
6346  O OE2 . GLU A 416 ? 0.2881 0.2681 0.2881 0.0598  0.0062  -0.0292 416 GLU A OE2 
6353  N N   . ASN A 417 ? 0.2109 0.2251 0.2436 0.0631  0.0241  -0.0008 417 ASN A N   
6354  C CA  . ASN A 417 ? 0.2155 0.2185 0.2501 0.0511  0.0165  -0.0159 417 ASN A CA  
6355  C C   . ASN A 417 ? 0.2354 0.1916 0.2474 0.0387  -0.0020 -0.0116 417 ASN A C   
6356  O O   . ASN A 417 ? 0.2213 0.2142 0.2669 0.0246  -0.0054 0.0343  417 ASN A O   
6357  C CB  . ASN A 417 ? 0.2606 0.2470 0.2688 0.0322  0.0061  0.0067  417 ASN A CB  
6358  C CG  . ASN A 417 ? 0.3706 0.2952 0.2813 0.0046  -0.0537 -0.0095 417 ASN A CG  
6359  O OD1 . ASN A 417 ? 0.5230 0.3431 0.3029 0.0098  -0.0664 0.0083  417 ASN A OD1 
6360  N ND2 . ASN A 417 ? 0.3633 0.3378 0.2789 0.0500  -0.0197 -0.0193 417 ASN A ND2 
6367  N N   . LEU A 418 ? 0.2347 0.1648 0.2357 0.0626  0.0094  0.0044  418 LEU A N   
6368  C CA  . LEU A 418 ? 0.1804 0.1582 0.2275 0.0633  0.0173  0.0180  418 LEU A CA  
6369  C C   . LEU A 418 ? 0.1858 0.1603 0.2102 0.0215  0.0078  0.0209  418 LEU A C   
6370  O O   . LEU A 418 ? 0.2115 0.1422 0.2073 -0.0010 0.0052  0.0003  418 LEU A O   
6371  C CB  . LEU A 418 ? 0.2017 0.1642 0.2286 0.0237  0.0120  0.0229  418 LEU A CB  
6372  C CG  . LEU A 418 ? 0.2166 0.1765 0.2314 0.0440  0.0196  -0.0286 418 LEU A CG  
6373  C CD1 . LEU A 418 ? 0.2285 0.1812 0.2410 0.0544  0.0086  -0.0093 418 LEU A CD1 
6374  C CD2 . LEU A 418 ? 0.1805 0.2359 0.2340 0.0301  0.0106  -0.0452 418 LEU A CD2 
6386  N N   . ILE A 419 ? 0.1966 0.1473 0.2021 0.0124  0.0122  0.0297  419 ILE A N   
6387  C CA  . ILE A 419 ? 0.1795 0.1564 0.2101 -0.0143 -0.0034 0.0006  419 ILE A CA  
6388  C C   . ILE A 419 ? 0.1566 0.1758 0.2094 -0.0326 -0.0031 -0.0067 419 ILE A C   
6389  O O   . ILE A 419 ? 0.1813 0.1448 0.2246 0.0024  0.0047  0.0079  419 ILE A O   
6390  C CB  . ILE A 419 ? 0.1717 0.1415 0.2059 0.0032  0.0208  0.0135  419 ILE A CB  
6391  C CG1 . ILE A 419 ? 0.2099 0.1788 0.2123 -0.0041 0.0420  0.0232  419 ILE A CG1 
6392  C CG2 . ILE A 419 ? 0.1959 0.1458 0.2080 -0.0148 0.0006  0.0104  419 ILE A CG2 
6393  C CD1 . ILE A 419 ? 0.2164 0.1665 0.2137 -0.0059 0.0561  -0.0084 419 ILE A CD1 
6405  N N   . ALA A 420 ? 0.1360 0.1643 0.1925 -0.0007 -0.0076 0.0019  420 ALA A N   
6406  C CA  . ALA A 420 ? 0.2084 0.1189 0.2087 0.0067  -0.0087 0.0005  420 ALA A CA  
6407  C C   . ALA A 420 ? 0.1962 0.1757 0.2165 -0.0074 -0.0033 -0.0102 420 ALA A C   
6408  O O   . ALA A 420 ? 0.2356 0.2061 0.2236 0.0060  -0.0347 -0.0193 420 ALA A O   
6409  C CB  . ALA A 420 ? 0.2425 0.1912 0.1963 -0.0174 -0.0525 -0.0017 420 ALA A CB  
6415  N N   A ARG A 421 ? 0.1708 0.1813 0.2168 -0.0106 -0.0060 -0.0074 421 ARG A N   
6416  N N   B ARG A 421 ? 0.1763 0.1929 0.2133 0.0057  -0.0204 -0.0079 421 ARG A N   
6417  C CA  A ARG A 421 ? 0.1769 0.2521 0.2217 -0.0342 0.0111  -0.0334 421 ARG A CA  
6418  C CA  B ARG A 421 ? 0.1898 0.2683 0.2143 -0.0155 -0.0139 -0.0410 421 ARG A CA  
6419  C C   A ARG A 421 ? 0.1775 0.2285 0.2132 -0.0013 0.0008  -0.0455 421 ARG A C   
6420  C C   B ARG A 421 ? 0.1844 0.2461 0.2113 0.0001  -0.0138 -0.0428 421 ARG A C   
6421  O O   A ARG A 421 ? 0.1916 0.1934 0.2078 0.0157  0.0265  -0.0495 421 ARG A O   
6422  O O   B ARG A 421 ? 0.2026 0.2327 0.2097 0.0050  0.0089  -0.0311 421 ARG A O   
6423  C CB  A ARG A 421 ? 0.1835 0.3362 0.2444 -0.0360 0.0486  -0.0450 421 ARG A CB  
6424  C CB  B ARG A 421 ? 0.2105 0.3560 0.2286 0.0126  0.0001  -0.0660 421 ARG A CB  
6425  C CG  A ARG A 421 ? 0.2356 0.4524 0.2686 -0.1065 0.0516  -0.0628 421 ARG A CG  
6426  C CG  B ARG A 421 ? 0.2729 0.4692 0.2389 -0.0248 -0.0227 -0.0941 421 ARG A CG  
6427  C CD  A ARG A 421 ? 0.2991 0.5462 0.2871 -0.1419 0.0657  -0.0732 421 ARG A CD  
6428  C CD  B ARG A 421 ? 0.3570 0.5481 0.2454 -0.0322 -0.0335 -0.1161 421 ARG A CD  
6429  N NE  A ARG A 421 ? 0.3218 0.5858 0.3066 -0.1928 0.0835  -0.0709 421 ARG A NE  
6430  N NE  B ARG A 421 ? 0.4473 0.5832 0.2546 -0.0167 -0.0224 -0.1323 421 ARG A NE  
6431  C CZ  A ARG A 421 ? 0.3782 0.6043 0.3153 -0.2459 0.0938  -0.0831 421 ARG A CZ  
6432  C CZ  B ARG A 421 ? 0.5023 0.5488 0.2398 -0.0532 -0.0363 -0.1448 421 ARG A CZ  
6433  N NH1 A ARG A 421 ? 0.4039 0.5841 0.3190 -0.2617 0.0864  -0.0829 421 ARG A NH1 
6434  N NH1 B ARG A 421 ? 0.5353 0.5613 0.2432 -0.0681 -0.0467 -0.1561 421 ARG A NH1 
6435  N NH2 A ARG A 421 ? 0.4297 0.6147 0.3322 -0.2404 0.1114  -0.0756 421 ARG A NH2 
6436  N NH2 B ARG A 421 ? 0.4080 0.4297 0.2439 -0.0631 -0.0683 -0.1510 421 ARG A NH2 
6463  N N   . ALA A 422 ? 0.1889 0.2087 0.2214 -0.0056 -0.0243 -0.0328 422 ALA A N   
6464  C CA  . ALA A 422 ? 0.1603 0.1879 0.2305 0.0129  -0.0275 -0.0281 422 ALA A CA  
6465  C C   . ALA A 422 ? 0.1921 0.2191 0.2320 0.0440  -0.0191 -0.0200 422 ALA A C   
6466  O O   . ALA A 422 ? 0.2182 0.2396 0.2558 0.0749  -0.0045 -0.0321 422 ALA A O   
6467  C CB  . ALA A 422 ? 0.2051 0.1962 0.2470 0.0146  -0.0342 -0.0320 422 ALA A CB  
6473  N N   . MET A 423 ? 0.1866 0.2132 0.2323 0.0580  -0.0194 -0.0148 423 MET A N   
6474  C CA  . MET A 423 ? 0.1649 0.2302 0.2323 0.0368  -0.0193 -0.0436 423 MET A CA  
6475  C C   . MET A 423 ? 0.1598 0.2302 0.2468 0.0461  -0.0356 -0.0459 423 MET A C   
6476  O O   . MET A 423 ? 0.2017 0.2494 0.2570 0.0542  -0.0517 -0.0738 423 MET A O   
6477  C CB  . MET A 423 ? 0.2101 0.2102 0.2533 0.0244  -0.0343 -0.0545 423 MET A CB  
6478  C CG  . MET A 423 ? 0.2054 0.2140 0.2776 0.0089  -0.0222 -0.0554 423 MET A CG  
6479  S SD  . MET A 423 ? 0.2156 0.2102 0.2844 0.0439  -0.0158 -0.0391 423 MET A SD  
6480  C CE  . MET A 423 ? 0.2405 0.2079 0.3046 0.0842  -0.0480 -0.0816 423 MET A CE  
6490  N N   . PRO A 424 ? 0.1623 0.2748 0.2428 0.0710  -0.0266 -0.0643 424 PRO A N   
6491  C CA  . PRO A 424 ? 0.1808 0.2853 0.2602 0.0757  -0.0487 -0.0904 424 PRO A CA  
6492  C C   . PRO A 424 ? 0.2406 0.2907 0.2826 0.0737  -0.0844 -0.1168 424 PRO A C   
6493  O O   . PRO A 424 ? 0.2329 0.2756 0.2873 0.0966  -0.0907 -0.0989 424 PRO A O   
6494  C CB  . PRO A 424 ? 0.2547 0.3372 0.2664 0.0888  -0.0534 -0.0778 424 PRO A CB  
6495  C CG  . PRO A 424 ? 0.2468 0.3327 0.2641 0.0876  -0.0537 -0.0958 424 PRO A CG  
6496  C CD  . PRO A 424 ? 0.2209 0.3343 0.2483 0.1157  -0.0393 -0.0718 424 PRO A CD  
6504  N N   . GLN A 425 ? 0.2173 0.2877 0.3059 0.0959  -0.0956 -0.1084 425 GLN A N   
6505  C CA  . GLN A 425 ? 0.2398 0.2708 0.3261 0.1214  -0.0912 -0.0941 425 GLN A CA  
6506  C C   . GLN A 425 ? 0.2058 0.2517 0.3377 0.0882  -0.1152 -0.0772 425 GLN A C   
6507  O O   . GLN A 425 ? 0.2542 0.2492 0.3688 0.0541  -0.1406 -0.0730 425 GLN A O   
6508  C CB  . GLN A 425 ? 0.2273 0.3388 0.3173 0.1050  -0.0628 -0.0758 425 GLN A CB  
6509  C CG  . GLN A 425 ? 0.2515 0.2692 0.2771 0.0796  -0.0057 -0.0438 425 GLN A CG  
6510  C CD  . GLN A 425 ? 0.1936 0.2504 0.2527 0.0444  -0.0032 -0.0048 425 GLN A CD  
6511  O OE1 . GLN A 425 ? 0.1934 0.1787 0.2370 -0.0109 0.0111  -0.0254 425 GLN A OE1 
6512  N NE2 . GLN A 425 ? 0.2361 0.2949 0.2758 0.0310  0.0316  -0.0048 425 GLN A NE2 
6521  N N   . GLY A 426 ? 0.2098 0.2656 0.3219 0.0962  -0.0899 -0.0784 426 GLY A N   
6522  C CA  . GLY A 426 ? 0.2603 0.2617 0.3082 0.0814  -0.0600 -0.0770 426 GLY A CA  
6523  C C   . GLY A 426 ? 0.2214 0.2396 0.2950 0.0711  -0.0659 -0.0471 426 GLY A C   
6524  O O   . GLY A 426 ? 0.2237 0.2343 0.2978 0.0138  -0.0496 -0.0617 426 GLY A O   
6528  N N   . ASP A 427 ? 0.1936 0.2354 0.2881 0.0537  -0.0684 -0.0380 427 ASP A N   
6529  C CA  . ASP A 427 ? 0.1568 0.2115 0.2786 0.0339  -0.0311 -0.0166 427 ASP A CA  
6530  C C   . ASP A 427 ? 0.1495 0.1872 0.2522 -0.0089 -0.0218 -0.0093 427 ASP A C   
6531  O O   . ASP A 427 ? 0.1733 0.2208 0.2390 0.0145  -0.0203 0.0146  427 ASP A O   
6532  C CB  . ASP A 427 ? 0.1975 0.1996 0.3083 0.0509  -0.0500 -0.0131 427 ASP A CB  
6533  C CG  . ASP A 427 ? 0.2191 0.2306 0.3462 0.0126  -0.0773 -0.0409 427 ASP A CG  
6534  O OD1 . ASP A 427 ? 0.2211 0.2427 0.3433 0.0467  -0.0993 -0.0490 427 ASP A OD1 
6535  O OD2 . ASP A 427 ? 0.2484 0.2387 0.3818 0.0009  -0.0960 -0.0393 427 ASP A OD2 
6540  N N   . ILE A 428 ? 0.1553 0.1798 0.2361 0.0083  -0.0178 -0.0153 428 ILE A N   
6541  C CA  . ILE A 428 ? 0.1589 0.1486 0.2280 -0.0195 -0.0336 0.0071  428 ILE A CA  
6542  C C   . ILE A 428 ? 0.2020 0.1454 0.2171 -0.0073 -0.0182 0.0154  428 ILE A C   
6543  O O   . ILE A 428 ? 0.2170 0.1682 0.2260 0.0177  -0.0246 0.0110  428 ILE A O   
6544  C CB  . ILE A 428 ? 0.1554 0.1903 0.2441 0.0135  -0.0239 0.0237  428 ILE A CB  
6545  C CG1 . ILE A 428 ? 0.1681 0.2335 0.2510 0.0390  -0.0088 0.0234  428 ILE A CG1 
6546  C CG2 . ILE A 428 ? 0.1561 0.1464 0.2470 0.0077  -0.0493 0.0325  428 ILE A CG2 
6547  C CD1 . ILE A 428 ? 0.1625 0.1730 0.2427 0.0218  -0.0092 -0.0043 428 ILE A CD1 
6559  N N   . LEU A 429 ? 0.1690 0.1897 0.2030 0.0208  0.0109  0.0074  429 LEU A N   
6560  C CA  . LEU A 429 ? 0.1498 0.2009 0.2110 0.0502  -0.0192 0.0030  429 LEU A CA  
6561  C C   . LEU A 429 ? 0.1839 0.1928 0.2038 0.0341  -0.0290 0.0044  429 LEU A C   
6562  O O   . LEU A 429 ? 0.2014 0.1777 0.2007 0.0104  -0.0176 0.0141  429 LEU A O   
6563  C CB  . LEU A 429 ? 0.1741 0.2162 0.2227 0.0218  -0.0125 -0.0141 429 LEU A CB  
6564  C CG  . LEU A 429 ? 0.1772 0.2146 0.2309 0.0074  -0.0047 -0.0132 429 LEU A CG  
6565  C CD1 . LEU A 429 ? 0.1732 0.2025 0.2263 0.0822  -0.0120 0.0083  429 LEU A CD1 
6566  C CD2 . LEU A 429 ? 0.2185 0.1225 0.2549 -0.0260 -0.0018 -0.0096 429 LEU A CD2 
6578  N N   . GLY A 430 ? 0.1669 0.2108 0.2013 0.0255  -0.0255 0.0073  430 GLY A N   
6579  C CA  . GLY A 430 ? 0.2053 0.1792 0.1778 0.0534  -0.0351 -0.0073 430 GLY A CA  
6580  C C   . GLY A 430 ? 0.1773 0.1406 0.1819 0.0560  -0.0171 0.0204  430 GLY A C   
6581  O O   . GLY A 430 ? 0.1992 0.1640 0.1840 0.0362  -0.0134 0.0146  430 GLY A O   
6585  N N   . PHE A 431 ? 0.1701 0.1506 0.1858 -0.0101 -0.0015 0.0014  431 PHE A N   
6586  C CA  . PHE A 431 ? 0.1400 0.1461 0.1952 -0.0028 0.0069  0.0054  431 PHE A CA  
6587  C C   . PHE A 431 ? 0.1607 0.1461 0.1862 -0.0005 -0.0232 -0.0039 431 PHE A C   
6588  O O   . PHE A 431 ? 0.1673 0.1512 0.1790 0.0097  0.0054  0.0083  431 PHE A O   
6589  C CB  . PHE A 431 ? 0.1605 0.1997 0.2020 0.0294  0.0109  0.0167  431 PHE A CB  
6590  C CG  . PHE A 431 ? 0.1395 0.1648 0.2056 -0.0029 0.0063  0.0156  431 PHE A CG  
6591  C CD1 . PHE A 431 ? 0.1522 0.1323 0.2026 -0.0198 0.0127  0.0294  431 PHE A CD1 
6592  C CD2 . PHE A 431 ? 0.1887 0.1956 0.2063 0.0515  -0.0041 0.0277  431 PHE A CD2 
6593  C CE1 . PHE A 431 ? 0.1772 0.1453 0.2136 0.0189  0.0068  0.0356  431 PHE A CE1 
6594  C CE2 . PHE A 431 ? 0.1736 0.1844 0.2163 0.0285  -0.0002 0.0116  431 PHE A CE2 
6595  C CZ  . PHE A 431 ? 0.1797 0.1963 0.2157 0.0161  0.0105  0.0303  431 PHE A CZ  
6605  N N   . ALA A 432 ? 0.1668 0.1429 0.1901 -0.0109 -0.0402 0.0177  432 ALA A N   
6606  C CA  . ALA A 432 ? 0.1899 0.1207 0.1770 -0.0064 -0.0210 -0.0079 432 ALA A CA  
6607  C C   . ALA A 432 ? 0.1872 0.1459 0.1802 -0.0175 -0.0176 0.0092  432 ALA A C   
6608  O O   . ALA A 432 ? 0.2055 0.1605 0.1724 -0.0193 0.0141  0.0045  432 ALA A O   
6609  C CB  . ALA A 432 ? 0.1669 0.1461 0.1801 0.0146  0.0049  -0.0432 432 ALA A CB  
6615  N N   . PRO A 433 ? 0.1890 0.1870 0.1923 -0.0078 0.0075  0.0108  433 PRO A N   
6616  C CA  . PRO A 433 ? 0.1794 0.1819 0.1954 0.0170  0.0236  -0.0138 433 PRO A CA  
6617  C C   . PRO A 433 ? 0.1875 0.1693 0.1905 0.0099  0.0112  -0.0071 433 PRO A C   
6618  O O   . PRO A 433 ? 0.1720 0.2072 0.2003 0.0005  -0.0041 -0.0106 433 PRO A O   
6619  C CB  . PRO A 433 ? 0.2132 0.2269 0.2046 -0.0006 0.0368  -0.0130 433 PRO A CB  
6620  C CG  . PRO A 433 ? 0.2713 0.2422 0.2061 -0.0182 0.0513  -0.0089 433 PRO A CG  
6621  C CD  . PRO A 433 ? 0.2132 0.1668 0.2034 -0.0332 0.0190  0.0153  433 PRO A CD  
6629  N N   . PRO A 434 ? 0.1902 0.1537 0.1912 0.0279  -0.0058 0.0045  434 PRO A N   
6630  C CA  . PRO A 434 ? 0.1938 0.1386 0.2013 0.0011  -0.0133 0.0027  434 PRO A CA  
6631  C C   . PRO A 434 ? 0.1881 0.1755 0.1890 0.0302  -0.0006 -0.0159 434 PRO A C   
6632  O O   . PRO A 434 ? 0.1829 0.1992 0.1897 -0.0160 -0.0007 -0.0387 434 PRO A O   
6633  C CB  . PRO A 434 ? 0.2002 0.1049 0.1961 -0.0156 0.0129  -0.0136 434 PRO A CB  
6634  C CG  . PRO A 434 ? 0.2492 0.1429 0.1893 -0.0418 -0.0128 -0.0055 434 PRO A CG  
6635  C CD  . PRO A 434 ? 0.2168 0.1686 0.1854 -0.0204 -0.0003 0.0144  434 PRO A CD  
6643  N N   . LEU A 435 ? 0.1657 0.1793 0.1763 0.0324  -0.0149 -0.0050 435 LEU A N   
6644  C CA  . LEU A 435 ? 0.1981 0.1581 0.1671 0.0153  -0.0106 -0.0053 435 LEU A CA  
6645  C C   . LEU A 435 ? 0.2102 0.1904 0.1759 0.0229  -0.0116 -0.0127 435 LEU A C   
6646  O O   . LEU A 435 ? 0.2642 0.2090 0.1825 0.0377  0.0178  -0.0156 435 LEU A O   
6647  C CB  . LEU A 435 ? 0.2301 0.1875 0.1760 -0.0207 -0.0259 0.0038  435 LEU A CB  
6648  C CG  . LEU A 435 ? 0.1963 0.1593 0.1777 -0.0125 -0.0079 0.0108  435 LEU A CG  
6649  C CD1 . LEU A 435 ? 0.1921 0.2027 0.1681 0.0020  0.0100  0.0065  435 LEU A CD1 
6650  C CD2 . LEU A 435 ? 0.2325 0.1687 0.1926 -0.0095 0.0006  0.0204  435 LEU A CD2 
6662  N N   . VAL A 436 ? 0.1733 0.1918 0.1904 0.0188  0.0135  -0.0069 436 VAL A N   
6663  C CA  . VAL A 436 ? 0.1735 0.1871 0.2085 0.0044  0.0244  0.0025  436 VAL A CA  
6664  C C   . VAL A 436 ? 0.2255 0.1634 0.2146 0.0312  0.0023  -0.0021 436 VAL A C   
6665  O O   . VAL A 436 ? 0.2581 0.2013 0.2235 -0.0117 0.0057  -0.0477 436 VAL A O   
6666  C CB  . VAL A 436 ? 0.2265 0.1791 0.2048 0.0032  -0.0039 -0.0140 436 VAL A CB  
6667  C CG1 . VAL A 436 ? 0.2504 0.1983 0.2149 -0.0125 -0.0330 -0.0158 436 VAL A CG1 
6668  C CG2 . VAL A 436 ? 0.2499 0.1298 0.2025 -0.0108 0.0208  -0.0067 436 VAL A CG2 
6678  N N   . THR A 437 ? 0.2359 0.1300 0.2130 -0.0071 0.0272  0.0035  437 THR A N   
6679  C CA  . THR A 437 ? 0.1992 0.1366 0.2042 -0.0171 0.0387  -0.0203 437 THR A CA  
6680  C C   . THR A 437 ? 0.2054 0.1762 0.2161 0.0148  0.0196  -0.0245 437 THR A C   
6681  O O   . THR A 437 ? 0.2065 0.1970 0.2205 0.0221  0.0032  -0.0388 437 THR A O   
6682  C CB  . THR A 437 ? 0.2265 0.1659 0.2145 -0.0200 0.0460  -0.0103 437 THR A CB  
6683  O OG1 . THR A 437 ? 0.2190 0.1675 0.2040 -0.0081 0.0111  -0.0065 437 THR A OG1 
6684  C CG2 . THR A 437 ? 0.2433 0.2110 0.2302 -0.0468 0.0281  -0.0069 437 THR A CG2 
6692  N N   . THR A 438 ? 0.2268 0.1658 0.2240 0.0391  0.0173  -0.0146 438 THR A N   
6693  C CA  . THR A 438 ? 0.2437 0.1923 0.2294 0.0245  0.0247  -0.0306 438 THR A CA  
6694  C C   . THR A 438 ? 0.2322 0.2124 0.2240 0.0050  0.0265  -0.0465 438 THR A C   
6695  O O   . THR A 438 ? 0.2575 0.1643 0.2393 0.0318  0.0339  -0.0215 438 THR A O   
6696  C CB  . THR A 438 ? 0.2586 0.2073 0.2520 -0.0194 0.0237  -0.0275 438 THR A CB  
6697  O OG1 . THR A 438 ? 0.2544 0.1824 0.2647 -0.0135 -0.0054 -0.0480 438 THR A OG1 
6698  C CG2 . THR A 438 ? 0.2958 0.2346 0.2575 -0.0271 0.0517  -0.0474 438 THR A CG2 
6706  N N   . ARG A 439 ? 0.2629 0.2058 0.2166 0.0002  0.0286  -0.0663 439 ARG A N   
6707  C CA  . ARG A 439 ? 0.2579 0.2211 0.2120 -0.0218 0.0067  -0.0590 439 ARG A CA  
6708  C C   . ARG A 439 ? 0.2554 0.1732 0.2232 -0.0212 0.0298  -0.0528 439 ARG A C   
6709  O O   . ARG A 439 ? 0.2388 0.1891 0.2158 0.0206  0.0266  -0.0424 439 ARG A O   
6710  C CB  . ARG A 439 ? 0.2827 0.2736 0.2144 -0.0180 0.0021  -0.0706 439 ARG A CB  
6711  C CG  . ARG A 439 ? 0.3173 0.3345 0.2244 0.0146  -0.0041 -0.0691 439 ARG A CG  
6712  C CD  . ARG A 439 ? 0.4225 0.4138 0.2535 0.0353  -0.0366 -0.0447 439 ARG A CD  
6713  N NE  . ARG A 439 ? 0.5044 0.5380 0.2830 0.0074  -0.0252 -0.0439 439 ARG A NE  
6714  C CZ  . ARG A 439 ? 0.5472 0.6109 0.3162 -0.0157 -0.0386 -0.0323 439 ARG A CZ  
6715  N NH1 . ARG A 439 ? 0.5002 0.6172 0.3242 -0.0665 -0.0326 -0.0474 439 ARG A NH1 
6716  N NH2 . ARG A 439 ? 0.5917 0.6627 0.3335 0.0144  -0.0312 -0.0219 439 ARG A NH2 
6730  N N   . ALA A 440 ? 0.2473 0.2038 0.2403 -0.0189 0.0442  -0.0456 440 ALA A N   
6731  C CA  . ALA A 440 ? 0.2699 0.1822 0.2482 -0.0115 0.0461  -0.0425 440 ALA A CA  
6732  C C   . ALA A 440 ? 0.2628 0.1662 0.2456 0.0026  0.0299  -0.0398 440 ALA A C   
6733  O O   . ALA A 440 ? 0.2438 0.1927 0.2466 -0.0053 0.0205  -0.0530 440 ALA A O   
6734  C CB  . ALA A 440 ? 0.2846 0.1401 0.2553 0.0082  0.0362  -0.0716 440 ALA A CB  
6740  N N   . GLU A 441 ? 0.2559 0.1540 0.2473 0.0154  0.0161  -0.0459 441 GLU A N   
6741  C CA  . GLU A 441 ? 0.2492 0.1532 0.2401 -0.0080 0.0069  -0.0455 441 GLU A CA  
6742  C C   . GLU A 441 ? 0.2054 0.1305 0.2239 -0.0037 0.0191  -0.0289 441 GLU A C   
6743  O O   . GLU A 441 ? 0.2346 0.1631 0.2223 -0.0106 0.0446  -0.0261 441 GLU A O   
6744  C CB  . GLU A 441 ? 0.2420 0.1370 0.2516 -0.0429 0.0036  -0.0335 441 GLU A CB  
6745  C CG  . GLU A 441 ? 0.2591 0.1757 0.2668 -0.0419 0.0080  -0.0105 441 GLU A CG  
6746  C CD  . GLU A 441 ? 0.2970 0.2244 0.2812 -0.0218 0.0357  0.0105  441 GLU A CD  
6747  O OE1 . GLU A 441 ? 0.2449 0.2025 0.2693 -0.0012 0.0453  -0.0022 441 GLU A OE1 
6748  O OE2 . GLU A 441 ? 0.3000 0.2377 0.3015 0.0089  0.0196  0.0252  441 GLU A OE2 
6755  N N   . VAL A 442 ? 0.2181 0.1486 0.2150 0.0045  -0.0006 -0.0194 442 VAL A N   
6756  C CA  . VAL A 442 ? 0.2057 0.1391 0.2248 0.0310  0.0158  -0.0232 442 VAL A CA  
6757  C C   . VAL A 442 ? 0.2353 0.1643 0.2283 0.0236  0.0296  -0.0183 442 VAL A C   
6758  O O   . VAL A 442 ? 0.2413 0.1694 0.2107 0.0098  0.0412  -0.0148 442 VAL A O   
6759  C CB  . VAL A 442 ? 0.2023 0.1470 0.2311 -0.0143 -0.0050 -0.0252 442 VAL A CB  
6760  C CG1 . VAL A 442 ? 0.2212 0.1559 0.2278 -0.0117 -0.0135 -0.0293 442 VAL A CG1 
6761  C CG2 . VAL A 442 ? 0.2144 0.1978 0.2329 0.0255  0.0417  -0.0436 442 VAL A CG2 
6771  N N   . ASP A 443 ? 0.2161 0.1772 0.2259 0.0215  0.0400  -0.0399 443 ASP A N   
6772  C CA  . ASP A 443 ? 0.1964 0.1984 0.2399 0.0440  0.0359  -0.0211 443 ASP A CA  
6773  C C   . ASP A 443 ? 0.2012 0.1902 0.2444 0.0127  0.0162  -0.0216 443 ASP A C   
6774  O O   . ASP A 443 ? 0.2210 0.1910 0.2401 0.0192  0.0063  -0.0402 443 ASP A O   
6775  C CB  . ASP A 443 ? 0.2159 0.2310 0.2413 0.0179  0.0429  -0.0471 443 ASP A CB  
6776  C CG  . ASP A 443 ? 0.2330 0.2666 0.2504 0.0416  0.0292  -0.0513 443 ASP A CG  
6777  O OD1 . ASP A 443 ? 0.2766 0.2519 0.2366 0.0679  0.0459  -0.0244 443 ASP A OD1 
6778  O OD2 . ASP A 443 ? 0.2887 0.2755 0.2668 0.0676  0.0383  -0.0536 443 ASP A OD2 
6783  N N   . GLU A 444 ? 0.2127 0.1903 0.2469 0.0171  0.0271  0.0032  444 GLU A N   
6784  C CA  . GLU A 444 ? 0.2154 0.2200 0.2558 -0.0089 0.0361  0.0162  444 GLU A CA  
6785  C C   . GLU A 444 ? 0.1810 0.2086 0.2470 0.0345  0.0203  0.0224  444 GLU A C   
6786  O O   . GLU A 444 ? 0.2012 0.2234 0.2545 0.0107  0.0064  0.0164  444 GLU A O   
6787  C CB  . GLU A 444 ? 0.2828 0.2448 0.2738 -0.0121 0.0197  0.0094  444 GLU A CB  
6788  C CG  . GLU A 444 ? 0.3587 0.3055 0.2749 0.0210  0.0444  -0.0101 444 GLU A CG  
6789  C CD  . GLU A 444 ? 0.3947 0.3347 0.2801 0.1126  0.0392  -0.0213 444 GLU A CD  
6790  O OE1 . GLU A 444 ? 0.4911 0.3683 0.2997 0.1900  0.0380  -0.0297 444 GLU A OE1 
6791  O OE2 . GLU A 444 ? 0.4049 0.3597 0.2790 0.0977  0.0149  -0.0450 444 GLU A OE2 
6798  N N   . ILE A 445 ? 0.2100 0.1922 0.2336 0.0501  0.0268  0.0280  445 ILE A N   
6799  C CA  . ILE A 445 ? 0.1713 0.1971 0.2215 0.0250  0.0450  0.0086  445 ILE A CA  
6800  C C   . ILE A 445 ? 0.2033 0.1791 0.2286 0.0615  0.0197  0.0068  445 ILE A C   
6801  O O   . ILE A 445 ? 0.2029 0.1669 0.2388 0.0257  0.0275  0.0184  445 ILE A O   
6802  C CB  . ILE A 445 ? 0.1850 0.1935 0.2201 0.0183  0.0665  -0.0087 445 ILE A CB  
6803  C CG1 . ILE A 445 ? 0.1874 0.2284 0.2301 -0.0487 0.0355  -0.0067 445 ILE A CG1 
6804  C CG2 . ILE A 445 ? 0.2278 0.2200 0.2157 0.0544  0.0512  -0.0132 445 ILE A CG2 
6805  C CD1 . ILE A 445 ? 0.1797 0.2786 0.2394 -0.0395 0.0187  -0.0334 445 ILE A CD1 
6817  N N   . VAL A 446 ? 0.1900 0.1910 0.2175 0.0345  0.0208  0.0094  446 VAL A N   
6818  C CA  . VAL A 446 ? 0.1568 0.2042 0.2196 -0.0180 0.0140  0.0210  446 VAL A CA  
6819  C C   . VAL A 446 ? 0.1719 0.1941 0.2192 0.0154  0.0043  -0.0007 446 VAL A C   
6820  O O   . VAL A 446 ? 0.1884 0.2042 0.2313 0.0213  0.0114  0.0012  446 VAL A O   
6821  C CB  . VAL A 446 ? 0.1934 0.2617 0.2212 -0.0123 0.0133  0.0104  446 VAL A CB  
6822  C CG1 . VAL A 446 ? 0.2280 0.2867 0.2295 -0.0090 0.0084  0.0353  446 VAL A CG1 
6823  C CG2 . VAL A 446 ? 0.2466 0.2431 0.2213 0.0023  -0.0280 0.0264  446 VAL A CG2 
6833  N N   . ALA A 447 ? 0.1645 0.2114 0.2295 0.0459  0.0103  0.0158  447 ALA A N   
6834  C CA  . ALA A 447 ? 0.1758 0.1872 0.2460 0.0207  0.0109  -0.0032 447 ALA A CA  
6835  C C   . ALA A 447 ? 0.1849 0.1910 0.2501 0.0250  0.0260  0.0055  447 ALA A C   
6836  O O   . ALA A 447 ? 0.1914 0.1730 0.2617 0.0534  -0.0014 0.0104  447 ALA A O   
6837  C CB  . ALA A 447 ? 0.2399 0.1915 0.2480 0.0509  0.0316  -0.0085 447 ALA A CB  
6843  N N   . ARG A 448 ? 0.2122 0.1749 0.2502 0.0174  0.0368  0.0131  448 ARG A N   
6844  C CA  . ARG A 448 ? 0.2093 0.1364 0.2510 -0.0014 0.0106  0.0304  448 ARG A CA  
6845  C C   . ARG A 448 ? 0.2051 0.1707 0.2517 0.0061  0.0016  0.0401  448 ARG A C   
6846  O O   . ARG A 448 ? 0.1839 0.1905 0.2632 0.0311  0.0148  0.0647  448 ARG A O   
6847  C CB  . ARG A 448 ? 0.2512 0.1471 0.2643 0.0309  0.0085  0.0182  448 ARG A CB  
6848  C CG  . ARG A 448 ? 0.2614 0.1461 0.2847 0.0468  0.0491  0.0063  448 ARG A CG  
6849  C CD  . ARG A 448 ? 0.3403 0.1662 0.2978 -0.0364 0.0649  0.0149  448 ARG A CD  
6850  N NE  . ARG A 448 ? 0.3708 0.1772 0.3092 -0.0599 0.1035  0.0007  448 ARG A NE  
6851  C CZ  . ARG A 448 ? 0.4391 0.1765 0.3196 -0.0697 0.1102  0.0056  448 ARG A CZ  
6852  N NH1 . ARG A 448 ? 0.4760 0.2292 0.3232 -0.0906 0.1153  0.0287  448 ARG A NH1 
6853  N NH2 . ARG A 448 ? 0.5044 0.2362 0.3407 -0.0575 0.0939  -0.0098 448 ARG A NH2 
6867  N N   . ALA A 449 ? 0.1957 0.1813 0.2476 0.0250  0.0146  0.0211  449 ALA A N   
6868  C CA  . ALA A 449 ? 0.1867 0.1491 0.2544 0.0447  -0.0015 0.0246  449 ALA A CA  
6869  C C   . ALA A 449 ? 0.1654 0.1436 0.2598 0.0324  -0.0066 0.0122  449 ALA A C   
6870  O O   . ALA A 449 ? 0.1535 0.1434 0.2676 0.0058  -0.0101 0.0214  449 ALA A O   
6871  C CB  . ALA A 449 ? 0.2209 0.1362 0.2536 0.0486  -0.0385 0.0105  449 ALA A CB  
6877  N N   . LYS A 450 ? 0.1861 0.1114 0.2479 0.0224  0.0047  -0.0107 450 LYS A N   
6878  C CA  . LYS A 450 ? 0.1810 0.1647 0.2541 0.0053  0.0123  -0.0204 450 LYS A CA  
6879  C C   . LYS A 450 ? 0.1820 0.1612 0.2428 0.0120  0.0022  0.0200  450 LYS A C   
6880  O O   . LYS A 450 ? 0.1863 0.1645 0.2394 0.0173  0.0054  0.0520  450 LYS A O   
6881  C CB  . LYS A 450 ? 0.1798 0.1616 0.2653 0.0340  0.0044  -0.0067 450 LYS A CB  
6882  C CG  . LYS A 450 ? 0.2437 0.2422 0.2920 0.0002  -0.0186 0.0080  450 LYS A CG  
6883  C CD  . LYS A 450 ? 0.3188 0.4256 0.3173 0.0353  0.0191  0.0184  450 LYS A CD  
6884  C CE  . LYS A 450 ? 0.3504 0.5404 0.3297 0.0662  0.0565  0.0257  450 LYS A CE  
6885  N NZ  . LYS A 450 ? 0.3024 0.6069 0.3387 0.0806  0.0720  0.0427  450 LYS A NZ  
6899  N N   . ARG A 451 ? 0.1699 0.1433 0.2351 0.0540  -0.0214 0.0068  451 ARG A N   
6900  C CA  . ARG A 451 ? 0.1729 0.1623 0.2459 0.0609  -0.0236 0.0050  451 ARG A CA  
6901  C C   . ARG A 451 ? 0.1664 0.1747 0.2340 0.0309  -0.0262 0.0100  451 ARG A C   
6902  O O   . ARG A 451 ? 0.1869 0.1900 0.2388 0.0369  -0.0224 -0.0050 451 ARG A O   
6903  C CB  . ARG A 451 ? 0.2153 0.1735 0.2635 0.0571  -0.0090 -0.0021 451 ARG A CB  
6904  C CG  . ARG A 451 ? 0.2351 0.1317 0.2853 0.0957  -0.0075 -0.0041 451 ARG A CG  
6905  C CD  . ARG A 451 ? 0.2486 0.1686 0.3163 0.1167  0.0117  0.0079  451 ARG A CD  
6906  N NE  . ARG A 451 ? 0.2665 0.2047 0.3425 0.1084  0.0076  -0.0025 451 ARG A NE  
6907  C CZ  . ARG A 451 ? 0.2703 0.2419 0.3605 0.0867  -0.0054 -0.0182 451 ARG A CZ  
6908  N NH1 . ARG A 451 ? 0.2902 0.2452 0.3400 0.1347  -0.0462 -0.0215 451 ARG A NH1 
6909  N NH2 . ARG A 451 ? 0.2470 0.2794 0.3877 0.0536  -0.0153 -0.0232 451 ARG A NH2 
6923  N N   . ALA A 452 ? 0.1655 0.1767 0.2159 0.0437  -0.0178 0.0022  452 ALA A N   
6924  C CA  . ALA A 452 ? 0.1772 0.2043 0.2302 0.0260  0.0109  0.0040  452 ALA A CA  
6925  C C   . ALA A 452 ? 0.1600 0.2033 0.2327 0.0274  -0.0049 -0.0142 452 ALA A C   
6926  O O   . ALA A 452 ? 0.1816 0.2147 0.2312 -0.0108 -0.0283 -0.0094 452 ALA A O   
6927  C CB  . ALA A 452 ? 0.1496 0.2198 0.2385 -0.0233 -0.0284 0.0195  452 ALA A CB  
6933  N N   . VAL A 453 ? 0.1860 0.2134 0.2454 -0.0026 -0.0072 -0.0222 453 VAL A N   
6934  C CA  . VAL A 453 ? 0.1489 0.2009 0.2520 0.0005  0.0013  -0.0141 453 VAL A CA  
6935  C C   . VAL A 453 ? 0.1698 0.2112 0.2569 0.0304  -0.0121 0.0142  453 VAL A C   
6936  O O   . VAL A 453 ? 0.1946 0.2069 0.2428 0.0187  -0.0355 0.0301  453 VAL A O   
6937  C CB  . VAL A 453 ? 0.1723 0.1826 0.2636 0.0028  -0.0099 -0.0005 453 VAL A CB  
6938  C CG1 . VAL A 453 ? 0.1726 0.1774 0.2638 -0.0168 -0.0328 -0.0328 453 VAL A CG1 
6939  C CG2 . VAL A 453 ? 0.1907 0.1878 0.2728 0.0287  -0.0119 0.0050  453 VAL A CG2 
6949  N N   . ASP A 454 ? 0.1437 0.2285 0.2622 0.0366  -0.0031 0.0174  454 ASP A N   
6950  C CA  . ASP A 454 ? 0.1480 0.2151 0.2631 0.0280  0.0021  0.0156  454 ASP A CA  
6951  C C   . ASP A 454 ? 0.1687 0.2356 0.2654 -0.0017 0.0018  0.0080  454 ASP A C   
6952  O O   . ASP A 454 ? 0.1786 0.2282 0.2606 0.0241  0.0065  0.0170  454 ASP A O   
6953  C CB  . ASP A 454 ? 0.1822 0.2164 0.2768 0.0486  -0.0006 0.0062  454 ASP A CB  
6954  C CG  . ASP A 454 ? 0.2121 0.2468 0.2947 0.0468  0.0135  0.0150  454 ASP A CG  
6955  O OD1 . ASP A 454 ? 0.2448 0.2408 0.3081 0.0499  -0.0041 0.0503  454 ASP A OD1 
6956  O OD2 . ASP A 454 ? 0.1900 0.2846 0.2892 0.0274  0.0032  -0.0218 454 ASP A OD2 
6961  N N   . LYS A 455 ? 0.1597 0.2345 0.2627 0.0189  0.0103  -0.0053 455 LYS A N   
6962  C CA  . LYS A 455 ? 0.1471 0.2389 0.2648 -0.0087 -0.0009 0.0129  455 LYS A CA  
6963  C C   . LYS A 455 ? 0.1617 0.2691 0.2550 0.0027  -0.0143 0.0005  455 LYS A C   
6964  O O   . LYS A 455 ? 0.1803 0.3159 0.2534 0.0391  -0.0019 0.0195  455 LYS A O   
6965  C CB  . LYS A 455 ? 0.1676 0.2582 0.2831 0.0300  -0.0390 0.0500  455 LYS A CB  
6966  C CG  . LYS A 455 ? 0.2548 0.3578 0.3121 0.0755  -0.0520 0.0794  455 LYS A CG  
6967  C CD  . LYS A 455 ? 0.3703 0.4417 0.3463 0.0385  -0.0465 0.0886  455 LYS A CD  
6968  C CE  . LYS A 455 ? 0.4574 0.5164 0.3782 0.0178  -0.0358 0.0849  455 LYS A CE  
6969  N NZ  . LYS A 455 ? 0.4540 0.5532 0.3961 -0.0203 -0.0463 0.1034  455 LYS A NZ  
6983  N N   . VAL A 456 ? 0.1634 0.2055 0.2445 0.0146  -0.0474 -0.0107 456 VAL A N   
6984  C CA  . VAL A 456 ? 0.1705 0.2278 0.2484 0.0203  -0.0052 0.0094  456 VAL A CA  
6985  C C   . VAL A 456 ? 0.1908 0.2377 0.2463 0.0408  -0.0208 0.0233  456 VAL A C   
6986  O O   . VAL A 456 ? 0.1672 0.2709 0.2460 0.0062  -0.0211 0.0222  456 VAL A O   
6987  C CB  . VAL A 456 ? 0.1414 0.2220 0.2459 0.0373  0.0107  0.0076  456 VAL A CB  
6988  C CG1 . VAL A 456 ? 0.2077 0.2202 0.2474 0.0705  -0.0083 0.0030  456 VAL A CG1 
6989  C CG2 . VAL A 456 ? 0.1572 0.2833 0.2484 0.0053  -0.0041 0.0128  456 VAL A CG2 
6999  N N   . THR A 457 ? 0.1930 0.2411 0.2464 0.0365  -0.0136 0.0196  457 THR A N   
7000  C CA  . THR A 457 ? 0.1613 0.2671 0.2465 0.0136  -0.0169 0.0317  457 THR A CA  
7001  C C   . THR A 457 ? 0.1858 0.2580 0.2446 0.0039  -0.0315 0.0235  457 THR A C   
7002  O O   . THR A 457 ? 0.1976 0.2774 0.2417 0.0231  -0.0269 0.0249  457 THR A O   
7003  C CB  . THR A 457 ? 0.1761 0.2611 0.2522 -0.0251 -0.0131 0.0101  457 THR A CB  
7004  O OG1 . THR A 457 ? 0.1759 0.2682 0.2476 -0.0105 -0.0256 0.0302  457 THR A OG1 
7005  C CG2 . THR A 457 ? 0.2068 0.2395 0.2583 0.0414  -0.0037 0.0356  457 THR A CG2 
7013  N N   . ASP A 458 ? 0.1926 0.2669 0.2481 0.0310  -0.0378 0.0353  458 ASP A N   
7014  C CA  . ASP A 458 ? 0.2313 0.3108 0.2773 0.0496  -0.0157 0.0000  458 ASP A CA  
7015  C C   . ASP A 458 ? 0.1960 0.2910 0.2694 0.0168  -0.0304 0.0195  458 ASP A C   
7016  O O   . ASP A 458 ? 0.2123 0.2608 0.2552 0.0252  -0.0207 0.0099  458 ASP A O   
7017  C CB  . ASP A 458 ? 0.3546 0.3423 0.3181 0.0695  -0.0001 -0.0069 458 ASP A CB  
7018  C CG  . ASP A 458 ? 0.4585 0.3976 0.3667 0.1166  0.0036  -0.0217 458 ASP A CG  
7019  O OD1 . ASP A 458 ? 0.5178 0.4597 0.3829 0.1182  0.0328  -0.0278 458 ASP A OD1 
7020  O OD2 . ASP A 458 ? 0.4526 0.4398 0.3914 0.1078  -0.0026 -0.0461 458 ASP A OD2 
7025  N N   . GLU A 459 ? 0.1537 0.2717 0.2862 0.0323  -0.0458 0.0255  459 GLU A N   
7026  C CA  . GLU A 459 ? 0.1433 0.2901 0.2885 0.0455  -0.0422 0.0262  459 GLU A CA  
7027  C C   . GLU A 459 ? 0.1476 0.2832 0.2902 0.0438  -0.0506 0.0312  459 GLU A C   
7028  O O   . GLU A 459 ? 0.1914 0.2918 0.2965 -0.0213 -0.0433 0.0213  459 GLU A O   
7029  C CB  . GLU A 459 ? 0.1566 0.2741 0.2938 0.0257  -0.0131 0.0277  459 GLU A CB  
7030  C CG  . GLU A 459 ? 0.2039 0.3027 0.3053 -0.0041 0.0109  0.0093  459 GLU A CG  
7031  C CD  . GLU A 459 ? 0.3147 0.2891 0.3321 0.0263  0.0352  0.0375  459 GLU A CD  
7032  O OE1 . GLU A 459 ? 0.4077 0.2812 0.3428 0.0651  0.0295  0.0482  459 GLU A OE1 
7033  O OE2 . GLU A 459 ? 0.2950 0.3012 0.3477 0.0310  0.0311  0.0559  459 GLU A OE2 
7040  N N   . LEU A 460 ? 0.1649 0.2720 0.2848 0.0261  -0.0408 0.0321  460 LEU A N   
7041  C CA  . LEU A 460 ? 0.1891 0.2603 0.2828 0.0148  -0.0493 0.0162  460 LEU A CA  
7042  C C   . LEU A 460 ? 0.1875 0.3214 0.2871 0.0158  -0.0412 0.0219  460 LEU A C   
7043  O O   . LEU A 460 ? 0.2112 0.3539 0.2983 -0.0132 -0.0354 0.0314  460 LEU A O   
7044  C CB  . LEU A 460 ? 0.1962 0.2351 0.2834 0.0480  -0.0687 -0.0024 460 LEU A CB  
7045  C CG  . LEU A 460 ? 0.2130 0.2180 0.2937 0.0217  -0.0680 0.0037  460 LEU A CG  
7046  C CD1 . LEU A 460 ? 0.2037 0.2347 0.3101 0.0367  -0.0613 -0.0002 460 LEU A CD1 
7047  C CD2 . LEU A 460 ? 0.2325 0.2597 0.2969 0.0364  -0.0536 -0.0111 460 LEU A CD2 
7059  N N   . THR A 461 ? 0.1753 0.3466 0.2807 -0.0024 -0.0044 0.0281  461 THR A N   
7060  C CA  . THR A 461 ? 0.1570 0.3972 0.2976 -0.0096 -0.0357 0.0158  461 THR A CA  
7061  C C   . THR A 461 ? 0.1731 0.4095 0.3166 -0.0418 -0.0469 0.0196  461 THR A C   
7062  O O   . THR A 461 ? 0.2118 0.4158 0.3165 -0.0814 -0.0561 0.0314  461 THR A O   
7063  C CB  . THR A 461 ? 0.1918 0.4333 0.2991 -0.0399 -0.0444 0.0129  461 THR A CB  
7064  O OG1 . THR A 461 ? 0.2190 0.4377 0.2872 0.0044  -0.0400 0.0345  461 THR A OG1 
7065  C CG2 . THR A 461 ? 0.2595 0.4669 0.3098 0.0157  -0.0163 0.0161  461 THR A CG2 
7073  N N   . ARG A 462 ? 0.1955 0.4300 0.3237 -0.0141 -0.0546 0.0368  462 ARG A N   
7074  C CA  . ARG A 462 ? 0.1877 0.4495 0.3421 -0.0083 -0.0839 0.0243  462 ARG A CA  
7075  C C   . ARG A 462 ? 0.2084 0.4480 0.3364 -0.0085 -0.0825 0.0160  462 ARG A C   
7076  O O   . ARG A 462 ? 0.2289 0.4844 0.3548 -0.0232 -0.0835 0.0037  462 ARG A O   
7077  C CB  . ARG A 462 ? 0.2425 0.4948 0.3694 -0.0267 -0.1014 0.0280  462 ARG A CB  
7078  C CG  . ARG A 462 ? 0.3685 0.5856 0.4207 -0.0102 -0.0460 0.0283  462 ARG A CG  
7079  C CD  . ARG A 462 ? 0.5662 0.6582 0.4722 -0.0342 -0.0173 0.0013  462 ARG A CD  
7080  N NE  . ARG A 462 ? 0.7724 0.7318 0.5070 -0.0223 -0.0169 -0.0061 462 ARG A NE  
7081  C CZ  . ARG A 462 ? 0.9328 0.7633 0.5245 -0.0045 -0.0247 -0.0141 462 ARG A CZ  
7082  N NH1 . ARG A 462 ? 0.9965 0.7838 0.5342 0.0223  -0.0246 -0.0099 462 ARG A NH1 
7083  N NH2 . ARG A 462 ? 0.9564 0.7606 0.5294 -0.0161 -0.0231 -0.0143 462 ARG A NH2 
7097  N N   . SER A 463 ? 0.1972 0.4043 0.3239 0.0202  -0.0647 -0.0281 463 SER A N   
7098  C CA  . SER A 463 ? 0.2478 0.4071 0.3298 -0.0047 -0.0513 -0.0413 463 SER A CA  
7099  C C   . SER A 463 ? 0.2660 0.4240 0.3591 -0.0412 -0.0420 -0.0532 463 SER A C   
7100  O O   . SER A 463 ? 0.2589 0.4577 0.3658 -0.0569 -0.0366 -0.0684 463 SER A O   
7101  C CB  . SER A 463 ? 0.2331 0.4039 0.3123 -0.0433 -0.0733 -0.0502 463 SER A CB  
7102  O OG  . SER A 463 ? 0.2718 0.4138 0.3103 -0.0401 -0.0629 -0.0383 463 SER A OG  
7108  N N   . GLY A 464 ? 0.2716 0.3605 0.3738 -0.0390 -0.0411 -0.0280 464 GLY A N   
7109  C CA  . GLY A 464 ? 0.3077 0.3383 0.4042 -0.0952 -0.0445 -0.0455 464 GLY A CA  
7110  C C   . GLY A 464 ? 0.3331 0.3228 0.4357 -0.0715 -0.0451 -0.0338 464 GLY A C   
7111  O O   . GLY A 464 ? 0.3559 0.3282 0.4482 -0.0892 -0.0475 -0.0227 464 GLY A O   
7115  N N   . ASP A 465 ? 0.3115 0.3625 0.4480 -0.0394 -0.0675 -0.0396 465 ASP A N   
7116  C CA  . ASP A 465 ? 0.3028 0.3400 0.4611 -0.0349 -0.0537 -0.0538 465 ASP A CA  
7117  C C   . ASP A 465 ? 0.3115 0.3997 0.4959 0.0001  -0.0761 -0.0341 465 ASP A C   
7118  O O   . ASP A 465 ? 0.3540 0.4211 0.4957 -0.0145 -0.0967 -0.0310 465 ASP A O   
7119  C CB  . ASP A 465 ? 0.3406 0.3420 0.4489 -0.0356 -0.0334 -0.0552 465 ASP A CB  
7120  C CG  . ASP A 465 ? 0.3743 0.3451 0.4420 -0.0206 -0.0014 -0.0476 465 ASP A CG  
7121  O OD1 . ASP A 465 ? 0.4170 0.3613 0.4454 0.0243  -0.0100 -0.0440 465 ASP A OD1 
7122  O OD2 . ASP A 465 ? 0.3799 0.3647 0.4321 -0.0104 0.0336  -0.0355 465 ASP A OD2 
7127  N N   . LEU A 466 ? 0.3095 0.4159 0.5195 0.0253  -0.0878 -0.0500 466 LEU A N   
7128  C CA  . LEU A 466 ? 0.3560 0.4748 0.5482 0.0938  -0.0862 -0.0462 466 LEU A CA  
7129  C C   . LEU A 466 ? 0.3751 0.5600 0.5717 0.1202  -0.0976 -0.0653 466 LEU A C   
7130  O O   . LEU A 466 ? 0.4594 0.6058 0.5896 0.0763  -0.0831 -0.0778 466 LEU A O   
7131  C CB  . LEU A 466 ? 0.3986 0.4598 0.5538 0.1155  -0.0592 -0.0496 466 LEU A CB  
7132  C CG  . LEU A 466 ? 0.4281 0.4694 0.5706 0.1358  -0.0137 -0.0614 466 LEU A CG  
7133  C CD1 . LEU A 466 ? 0.3814 0.5098 0.5767 0.1207  -0.0066 -0.0707 466 LEU A CD1 
7134  C CD2 . LEU A 466 ? 0.4676 0.4638 0.5740 0.1758  0.0064  -0.0650 466 LEU A CD2 
7146  N N   . SER B 2   ? 0.2227 0.2867 0.3094 0.0077  -0.0276 0.0237  2   SER B N   
7147  C CA  . SER B 2   ? 0.1842 0.2386 0.2673 -0.0549 -0.0162 0.0286  2   SER B CA  
7148  C C   . SER B 2   ? 0.1927 0.1918 0.2382 -0.0640 -0.0211 0.0027  2   SER B C   
7149  O O   . SER B 2   ? 0.2269 0.2218 0.2256 -0.0647 -0.0408 0.0046  2   SER B O   
7150  C CB  . SER B 2   ? 0.2665 0.2989 0.2831 -0.0548 0.0063  0.0058  2   SER B CB  
7151  O OG  . SER B 2   ? 0.2212 0.1964 0.2644 -0.0200 0.0006  -0.0307 2   SER B OG  
7156  N N   . GLN B 3   ? 0.1708 0.2063 0.2366 -0.0759 -0.0155 -0.0046 3   GLN B N   
7157  C CA  . GLN B 3   ? 0.1909 0.2146 0.2402 -0.0606 -0.0083 -0.0060 3   GLN B CA  
7158  C C   . GLN B 3   ? 0.1942 0.2195 0.2361 -0.0657 -0.0051 0.0019  3   GLN B C   
7159  O O   . GLN B 3   ? 0.1783 0.2113 0.2311 -0.0623 -0.0184 0.0170  3   GLN B O   
7160  C CB  . GLN B 3   ? 0.2536 0.2160 0.2679 -0.0857 0.0161  -0.0484 3   GLN B CB  
7161  C CG  . GLN B 3   ? 0.3982 0.2703 0.3053 -0.0532 0.0174  -0.0191 3   GLN B CG  
7162  C CD  . GLN B 3   ? 0.5036 0.3060 0.3324 0.0193  0.0225  -0.0039 3   GLN B CD  
7163  O OE1 . GLN B 3   ? 0.5225 0.3236 0.3475 0.0465  0.0169  0.0146  3   GLN B OE1 
7164  N NE2 . GLN B 3   ? 0.5409 0.3953 0.3517 0.0045  0.0244  0.0157  3   GLN B NE2 
7173  N N   . HIS B 4   ? 0.1798 0.2764 0.2348 -0.0265 -0.0011 -0.0214 4   HIS B N   
7174  C CA  . HIS B 4   ? 0.1654 0.2277 0.2172 -0.0189 -0.0029 0.0072  4   HIS B CA  
7175  C C   . HIS B 4   ? 0.1384 0.2005 0.2073 -0.0539 -0.0289 -0.0185 4   HIS B C   
7176  O O   . HIS B 4   ? 0.1970 0.2201 0.1993 -0.0999 -0.0026 -0.0055 4   HIS B O   
7177  C CB  . HIS B 4   ? 0.1679 0.2431 0.2114 -0.0335 0.0060  0.0448  4   HIS B CB  
7178  C CG  . HIS B 4   ? 0.2077 0.2614 0.1980 -0.0614 0.0109  0.0204  4   HIS B CG  
7179  N ND1 . HIS B 4   ? 0.2303 0.2907 0.2023 -0.1115 -0.0101 0.0115  4   HIS B ND1 
7180  C CD2 . HIS B 4   ? 0.2148 0.2487 0.1819 -0.0545 0.0104  0.0179  4   HIS B CD2 
7181  C CE1 . HIS B 4   ? 0.2462 0.2833 0.1936 -0.0951 0.0038  0.0361  4   HIS B CE1 
7182  N NE2 . HIS B 4   ? 0.2188 0.2480 0.1888 -0.0541 -0.0035 0.0385  4   HIS B NE2 
7190  N N   . GLN B 5   ? 0.1413 0.2104 0.2070 -0.0534 -0.0247 -0.0287 5   GLN B N   
7191  C CA  . GLN B 5   ? 0.1828 0.2435 0.2139 -0.0403 -0.0318 -0.0247 5   GLN B CA  
7192  C C   . GLN B 5   ? 0.1515 0.2192 0.2096 -0.0628 -0.0424 -0.0011 5   GLN B C   
7193  O O   . GLN B 5   ? 0.1848 0.2094 0.2129 -0.0663 -0.0199 -0.0038 5   GLN B O   
7194  C CB  . GLN B 5   ? 0.2034 0.2696 0.2240 -0.0826 0.0086  -0.0317 5   GLN B CB  
7195  C CG  . GLN B 5   ? 0.2022 0.2972 0.2354 -0.0569 0.0238  -0.0385 5   GLN B CG  
7196  C CD  . GLN B 5   ? 0.2625 0.3169 0.2502 -0.0665 0.0389  -0.0392 5   GLN B CD  
7197  O OE1 . GLN B 5   ? 0.2672 0.2996 0.2629 -0.0568 0.0187  -0.0093 5   GLN B OE1 
7198  N NE2 . GLN B 5   ? 0.2887 0.3553 0.2623 -0.0833 0.0367  -0.0471 5   GLN B NE2 
7207  N N   . ASN B 6   ? 0.1720 0.2262 0.2091 -0.0737 -0.0212 0.0121  6   ASN B N   
7208  C CA  . ASN B 6   ? 0.1795 0.2385 0.2162 -0.0731 -0.0170 0.0325  6   ASN B CA  
7209  C C   . ASN B 6   ? 0.1392 0.2167 0.2083 -0.0829 -0.0213 0.0413  6   ASN B C   
7210  O O   . ASN B 6   ? 0.1699 0.1866 0.1972 -0.0695 -0.0123 0.0028  6   ASN B O   
7211  C CB  . ASN B 6   ? 0.1779 0.2261 0.2159 -0.0904 -0.0288 -0.0009 6   ASN B CB  
7212  C CG  . ASN B 6   ? 0.2007 0.2232 0.2230 -0.0487 -0.0249 -0.0053 6   ASN B CG  
7213  O OD1 . ASN B 6   ? 0.2280 0.2452 0.2187 -0.0379 -0.0516 -0.0016 6   ASN B OD1 
7214  N ND2 . ASN B 6   ? 0.2767 0.2888 0.2347 -0.0107 -0.0119 -0.0294 6   ASN B ND2 
7221  N N   . LEU B 7   ? 0.1529 0.2333 0.1980 -0.0474 -0.0218 0.0401  7   LEU B N   
7222  C CA  . LEU B 7   ? 0.1546 0.2214 0.2126 -0.0327 -0.0006 0.0430  7   LEU B CA  
7223  C C   . LEU B 7   ? 0.1799 0.2361 0.2022 -0.0465 -0.0102 0.0350  7   LEU B C   
7224  O O   . LEU B 7   ? 0.1697 0.2356 0.1977 -0.0307 -0.0122 0.0363  7   LEU B O   
7225  C CB  . LEU B 7   ? 0.2490 0.2360 0.2438 0.0020  0.0073  0.0665  7   LEU B CB  
7226  C CG  . LEU B 7   ? 0.3263 0.3742 0.2751 0.0858  0.0438  0.0931  7   LEU B CG  
7227  C CD1 . LEU B 7   ? 0.4150 0.3596 0.2973 0.1085  0.0602  0.1029  7   LEU B CD1 
7228  C CD2 . LEU B 7   ? 0.2495 0.4247 0.2767 0.1193  0.0646  0.0806  7   LEU B CD2 
7240  N N   . ILE B 8   ? 0.1872 0.2043 0.2010 -0.0381 -0.0063 0.0304  8   ILE B N   
7241  C CA  . ILE B 8   ? 0.1813 0.2055 0.2014 -0.0377 -0.0159 0.0131  8   ILE B CA  
7242  C C   . ILE B 8   ? 0.1522 0.2465 0.1992 -0.0439 -0.0065 0.0005  8   ILE B C   
7243  O O   . ILE B 8   ? 0.1629 0.2289 0.1957 -0.0385 -0.0207 -0.0077 8   ILE B O   
7244  C CB  . ILE B 8   ? 0.1813 0.1748 0.2001 -0.0482 -0.0051 0.0099  8   ILE B CB  
7245  C CG1 . ILE B 8   ? 0.2043 0.2218 0.1900 -0.0694 -0.0070 -0.0089 8   ILE B CG1 
7246  C CG2 . ILE B 8   ? 0.1915 0.1952 0.2066 -0.0595 0.0008  0.0067  8   ILE B CG2 
7247  C CD1 . ILE B 8   ? 0.2340 0.2215 0.1977 -0.0540 -0.0038 -0.0006 8   ILE B CD1 
7259  N N   . ASP B 9   ? 0.1578 0.2451 0.1812 -0.0509 -0.0127 -0.0134 9   ASP B N   
7260  C CA  . ASP B 9   ? 0.1499 0.2410 0.1904 -0.0342 -0.0297 -0.0090 9   ASP B CA  
7261  C C   . ASP B 9   ? 0.1653 0.2280 0.1829 -0.0336 -0.0199 -0.0104 9   ASP B C   
7262  O O   . ASP B 9   ? 0.1755 0.2277 0.1912 -0.0617 -0.0168 0.0047  9   ASP B O   
7263  C CB  . ASP B 9   ? 0.1755 0.2507 0.2176 -0.0094 -0.0475 0.0189  9   ASP B CB  
7264  C CG  . ASP B 9   ? 0.1715 0.3103 0.2480 -0.0149 -0.0594 -0.0189 9   ASP B CG  
7265  O OD1 . ASP B 9   ? 0.1607 0.3328 0.2641 -0.0657 -0.0212 -0.0277 9   ASP B OD1 
7266  O OD2 . ASP B 9   ? 0.1749 0.3180 0.2713 -0.0168 -0.0804 -0.0324 9   ASP B OD2 
7271  N N   . ARG B 10  ? 0.1692 0.2018 0.1792 -0.0542 -0.0189 -0.0263 10  ARG B N   
7272  C CA  . ARG B 10  ? 0.1631 0.1957 0.1867 -0.0158 -0.0161 -0.0429 10  ARG B CA  
7273  C C   . ARG B 10  ? 0.1718 0.1859 0.1816 -0.0540 -0.0054 -0.0276 10  ARG B C   
7274  O O   . ARG B 10  ? 0.1575 0.1775 0.1806 -0.0521 -0.0474 -0.0009 10  ARG B O   
7275  C CB  . ARG B 10  ? 0.1636 0.1995 0.1940 -0.0517 -0.0082 -0.0392 10  ARG B CB  
7276  C CG  . ARG B 10  ? 0.1822 0.2135 0.2077 -0.0461 -0.0330 -0.0297 10  ARG B CG  
7277  C CD  . ARG B 10  ? 0.2020 0.1972 0.2175 -0.0348 -0.0231 -0.0271 10  ARG B CD  
7278  N NE  . ARG B 10  ? 0.1754 0.1711 0.2256 -0.0091 -0.0165 -0.0111 10  ARG B NE  
7279  C CZ  . ARG B 10  ? 0.1703 0.1833 0.2470 -0.0390 -0.0310 -0.0236 10  ARG B CZ  
7280  N NH1 . ARG B 10  ? 0.1903 0.2075 0.2557 -0.0519 -0.0242 -0.0202 10  ARG B NH1 
7281  N NH2 . ARG B 10  ? 0.2008 0.2229 0.2611 -0.0593 -0.0321 -0.0037 10  ARG B NH2 
7295  N N   . ASP B 11  ? 0.1369 0.2078 0.1667 -0.0713 -0.0026 -0.0162 11  ASP B N   
7296  C CA  . ASP B 11  ? 0.1524 0.2002 0.1749 -0.0616 -0.0192 -0.0320 11  ASP B CA  
7297  C C   . ASP B 11  ? 0.1603 0.1963 0.1847 -0.0693 -0.0092 -0.0348 11  ASP B C   
7298  O O   . ASP B 11  ? 0.1708 0.1810 0.1875 -0.0654 -0.0031 -0.0155 11  ASP B O   
7299  C CB  . ASP B 11  ? 0.1693 0.1718 0.1679 -0.0325 0.0005  0.0009  11  ASP B CB  
7300  C CG  . ASP B 11  ? 0.2182 0.1605 0.1717 -0.0584 0.0155  0.0023  11  ASP B CG  
7301  O OD1 . ASP B 11  ? 0.1877 0.1580 0.1887 -0.0219 0.0084  -0.0023 11  ASP B OD1 
7302  O OD2 . ASP B 11  ? 0.2069 0.2370 0.1487 -0.0588 0.0028  0.0084  11  ASP B OD2 
7307  N N   . ARG B 12  ? 0.1490 0.2156 0.2145 -0.0186 -0.0251 -0.0291 12  ARG B N   
7308  C CA  . ARG B 12  ? 0.1419 0.2276 0.2126 -0.0284 -0.0207 -0.0151 12  ARG B CA  
7309  C C   . ARG B 12  ? 0.1510 0.1927 0.1948 -0.0520 -0.0147 0.0087  12  ARG B C   
7310  O O   . ARG B 12  ? 0.1444 0.2242 0.1951 -0.0595 -0.0126 0.0113  12  ARG B O   
7311  C CB  . ARG B 12  ? 0.1553 0.2004 0.2260 -0.0281 -0.0198 -0.0179 12  ARG B CB  
7312  C CG  . ARG B 12  ? 0.1474 0.2023 0.2280 -0.0663 -0.0088 -0.0046 12  ARG B CG  
7313  C CD  . ARG B 12  ? 0.1535 0.1564 0.2274 -0.0613 0.0048  -0.0227 12  ARG B CD  
7314  N NE  . ARG B 12  ? 0.1625 0.1976 0.2475 -0.0666 0.0055  -0.0022 12  ARG B NE  
7315  C CZ  . ARG B 12  ? 0.1664 0.2212 0.2811 -0.0320 0.0147  0.0024  12  ARG B CZ  
7316  N NH1 . ARG B 12  ? 0.1362 0.2371 0.2967 -0.0342 0.0406  0.0089  12  ARG B NH1 
7317  N NH2 . ARG B 12  ? 0.1754 0.2324 0.2906 -0.0598 0.0059  0.0037  12  ARG B NH2 
7331  N N   . LYS B 13  ? 0.1839 0.1542 0.1752 -0.0336 -0.0001 0.0037  13  LYS B N   
7332  C CA  . LYS B 13  ? 0.1835 0.2112 0.1721 -0.0384 0.0057  -0.0128 13  LYS B CA  
7333  C C   . LYS B 13  ? 0.1233 0.1854 0.1649 -0.0814 0.0162  -0.0122 13  LYS B C   
7334  O O   . LYS B 13  ? 0.1539 0.1928 0.1693 -0.0464 0.0008  -0.0076 13  LYS B O   
7335  C CB  . LYS B 13  ? 0.1570 0.2118 0.1803 -0.0395 -0.0054 -0.0220 13  LYS B CB  
7336  C CG  . LYS B 13  ? 0.1678 0.2250 0.1825 -0.0696 -0.0280 -0.0153 13  LYS B CG  
7337  C CD  . LYS B 13  ? 0.2296 0.2603 0.2145 -0.0846 -0.0559 0.0017  13  LYS B CD  
7338  C CE  . LYS B 13  ? 0.2619 0.3418 0.2365 -0.0508 -0.0687 0.0261  13  LYS B CE  
7339  N NZ  . LYS B 13  ? 0.2798 0.3538 0.2644 -0.0740 -0.0621 0.0112  13  LYS B NZ  
7353  N N   . VAL B 14  ? 0.1658 0.1700 0.1701 -0.0169 0.0038  0.0184  14  VAL B N   
7354  C CA  . VAL B 14  ? 0.1519 0.1637 0.1746 -0.0481 -0.0303 0.0166  14  VAL B CA  
7355  C C   . VAL B 14  ? 0.1363 0.1696 0.1631 -0.0442 -0.0214 -0.0003 14  VAL B C   
7356  O O   . VAL B 14  ? 0.1590 0.2233 0.1718 -0.0283 -0.0133 -0.0273 14  VAL B O   
7357  C CB  . VAL B 14  ? 0.1949 0.1612 0.1672 -0.0160 -0.0326 -0.0074 14  VAL B CB  
7358  C CG1 . VAL B 14  ? 0.2338 0.1602 0.1677 -0.0264 -0.0344 -0.0145 14  VAL B CG1 
7359  C CG2 . VAL B 14  ? 0.2261 0.1628 0.1924 -0.0291 -0.0121 -0.0126 14  VAL B CG2 
7369  N N   . THR B 15  ? 0.1488 0.1715 0.1669 -0.0380 -0.0272 -0.0034 15  THR B N   
7370  C CA  . THR B 15  ? 0.1506 0.1283 0.1535 -0.0416 -0.0323 -0.0142 15  THR B CA  
7371  C C   . THR B 15  ? 0.1670 0.1958 0.1663 -0.0141 -0.0294 0.0099  15  THR B C   
7372  O O   . THR B 15  ? 0.1581 0.2304 0.1621 -0.0263 -0.0162 0.0079  15  THR B O   
7373  C CB  . THR B 15  ? 0.1667 0.1668 0.1626 -0.0343 -0.0075 -0.0054 15  THR B CB  
7374  O OG1 . THR B 15  ? 0.1976 0.1667 0.1785 -0.0199 0.0160  0.0057  15  THR B OG1 
7375  C CG2 . THR B 15  ? 0.1722 0.1881 0.1597 -0.0254 -0.0131 0.0284  15  THR B CG2 
7383  N N   . PHE B 16  ? 0.1553 0.1871 0.1638 -0.0169 -0.0207 0.0022  16  PHE B N   
7384  C CA  . PHE B 16  ? 0.1413 0.1462 0.1651 -0.0026 0.0043  0.0001  16  PHE B CA  
7385  C C   . PHE B 16  ? 0.1212 0.1993 0.1779 -0.0227 -0.0093 0.0070  16  PHE B C   
7386  O O   . PHE B 16  ? 0.1352 0.1934 0.2003 -0.0148 0.0039  0.0112  16  PHE B O   
7387  C CB  . PHE B 16  ? 0.1450 0.1253 0.1791 -0.0397 -0.0039 -0.0247 16  PHE B CB  
7388  C CG  . PHE B 16  ? 0.1319 0.1582 0.1857 -0.0428 -0.0103 0.0045  16  PHE B CG  
7389  C CD1 . PHE B 16  ? 0.1560 0.1794 0.2005 -0.0326 -0.0007 -0.0007 16  PHE B CD1 
7390  C CD2 . PHE B 16  ? 0.1590 0.1569 0.2002 -0.0580 0.0055  -0.0195 16  PHE B CD2 
7391  C CE1 . PHE B 16  ? 0.2103 0.1554 0.2052 -0.0234 0.0096  0.0079  16  PHE B CE1 
7392  C CE2 . PHE B 16  ? 0.1673 0.1695 0.2149 -0.0195 0.0002  -0.0081 16  PHE B CE2 
7393  C CZ  . PHE B 16  ? 0.1925 0.1523 0.2102 0.0131  -0.0087 -0.0298 16  PHE B CZ  
7403  N N   . HIS B 17  ? 0.1206 0.2105 0.1704 -0.0418 0.0134  -0.0114 17  HIS B N   
7404  C CA  . HIS B 17  ? 0.1339 0.1710 0.1749 -0.0565 -0.0028 -0.0108 17  HIS B CA  
7405  C C   . HIS B 17  ? 0.1319 0.1342 0.1771 -0.0281 -0.0212 -0.0020 17  HIS B C   
7406  O O   . HIS B 17  ? 0.1902 0.1620 0.1776 0.0121  -0.0302 0.0104  17  HIS B O   
7407  C CB  . HIS B 17  ? 0.1758 0.2123 0.1841 -0.0278 0.0027  0.0130  17  HIS B CB  
7408  C CG  . HIS B 17  ? 0.1644 0.1829 0.1652 -0.0247 0.0088  -0.0037 17  HIS B CG  
7409  N ND1 . HIS B 17  ? 0.2041 0.2052 0.1656 -0.0168 0.0005  0.0047  17  HIS B ND1 
7410  C CD2 . HIS B 17  ? 0.1605 0.1899 0.1664 -0.0197 -0.0080 -0.0029 17  HIS B CD2 
7411  C CE1 . HIS B 17  ? 0.1994 0.1826 0.1531 -0.0299 -0.0250 0.0151  17  HIS B CE1 
7412  N NE2 . HIS B 17  ? 0.1826 0.1816 0.1492 -0.0422 -0.0193 -0.0110 17  HIS B NE2 
7421  N N   . ALA B 18  ? 0.1697 0.1763 0.1741 -0.0128 -0.0126 0.0030  18  ALA B N   
7422  C CA  . ALA B 18  ? 0.1513 0.1448 0.1859 -0.0248 -0.0153 0.0251  18  ALA B CA  
7423  C C   . ALA B 18  ? 0.1564 0.1700 0.1760 -0.0276 -0.0078 0.0152  18  ALA B C   
7424  O O   . ALA B 18  ? 0.1624 0.1874 0.1843 -0.0618 -0.0083 0.0127  18  ALA B O   
7425  C CB  . ALA B 18  ? 0.1743 0.1584 0.2004 -0.0328 -0.0295 0.0488  18  ALA B CB  
7431  N N   A SER B 19  ? 0.1614 0.1624 0.1817 -0.0226 0.0036  0.0009  19  SER B N   
7432  N N   B SER B 19  ? 0.1467 0.1589 0.1769 -0.0125 -0.0127 0.0053  19  SER B N   
7433  C CA  A SER B 19  ? 0.1631 0.2205 0.1964 -0.0306 0.0315  -0.0168 19  SER B CA  
7434  C CA  B SER B 19  ? 0.1362 0.2145 0.1871 -0.0151 -0.0017 -0.0091 19  SER B CA  
7435  C C   A SER B 19  ? 0.1601 0.2344 0.2042 -0.0532 0.0298  -0.0057 19  SER B C   
7436  C C   B SER B 19  ? 0.1469 0.2321 0.1990 -0.0444 0.0133  -0.0019 19  SER B C   
7437  O O   A SER B 19  ? 0.1856 0.2895 0.2133 -0.0674 0.0151  0.0100  19  SER B O   
7438  O O   B SER B 19  ? 0.1581 0.2846 0.2062 -0.0556 -0.0001 0.0143  19  SER B O   
7439  C CB  A SER B 19  ? 0.2077 0.2543 0.2049 0.0016  0.0280  -0.0224 19  SER B CB  
7440  C CB  B SER B 19  ? 0.1401 0.2422 0.1857 0.0262  -0.0409 -0.0044 19  SER B CB  
7441  O OG  A SER B 19  ? 0.2520 0.2854 0.2104 -0.0029 0.0379  -0.0360 19  SER B OG  
7442  O OG  B SER B 19  ? 0.1577 0.2793 0.1812 0.0193  -0.0687 -0.0018 19  SER B OG  
7453  N N   . THR B 20  ? 0.1507 0.2046 0.2051 -0.0054 -0.0053 -0.0210 20  THR B N   
7454  C CA  . THR B 20  ? 0.1466 0.1496 0.2023 -0.0198 -0.0171 -0.0093 20  THR B CA  
7455  C C   . THR B 20  ? 0.1389 0.1827 0.2052 -0.0347 0.0081  0.0091  20  THR B C   
7456  O O   . THR B 20  ? 0.1395 0.1889 0.1982 -0.0139 -0.0014 -0.0051 20  THR B O   
7457  C CB  . THR B 20  ? 0.1447 0.1641 0.1946 -0.0055 -0.0223 -0.0268 20  THR B CB  
7458  O OG1 . THR B 20  ? 0.1790 0.1558 0.1811 -0.0385 -0.0026 0.0026  20  THR B OG1 
7459  C CG2 . THR B 20  ? 0.1716 0.2086 0.1968 0.0065  -0.0222 -0.0551 20  THR B CG2 
7468  N N   . HIS B 21  ? 0.1487 0.2011 0.2101 -0.0105 0.0022  0.0181  21  HIS B N   
7469  C CA  . HIS B 21  ? 0.1389 0.1938 0.2115 -0.0025 0.0045  -0.0005 21  HIS B CA  
7470  C C   . HIS B 21  ? 0.1598 0.2087 0.2009 -0.0313 -0.0161 -0.0130 21  HIS B C   
7471  O O   . HIS B 21  ? 0.1685 0.1670 0.1950 -0.0133 -0.0209 -0.0098 21  HIS B O   
7472  C CB  . HIS B 21  ? 0.1323 0.1898 0.2019 0.0153  0.0085  -0.0113 21  HIS B CB  
7473  C CG  . HIS B 21  ? 0.1698 0.2049 0.2004 -0.0053 0.0053  -0.0001 21  HIS B CG  
7474  N ND1 . HIS B 21  ? 0.1826 0.2065 0.2090 -0.0297 -0.0157 -0.0045 21  HIS B ND1 
7475  C CD2 . HIS B 21  ? 0.2066 0.2283 0.2023 -0.0195 0.0031  0.0039  21  HIS B CD2 
7476  C CE1 . HIS B 21  ? 0.2328 0.2598 0.2221 0.0015  -0.0395 -0.0054 21  HIS B CE1 
7477  N NE2 . HIS B 21  ? 0.2084 0.2148 0.2187 -0.0025 -0.0107 -0.0060 21  HIS B NE2 
7485  N N   . LEU B 22  ? 0.1022 0.2027 0.1991 -0.0467 0.0078  -0.0174 22  LEU B N   
7486  C CA  . LEU B 22  ? 0.1340 0.1791 0.1934 0.0276  0.0166  0.0161  22  LEU B CA  
7487  C C   . LEU B 22  ? 0.1534 0.1840 0.2071 -0.0010 -0.0033 0.0011  22  LEU B C   
7488  O O   . LEU B 22  ? 0.1779 0.2025 0.2089 -0.0290 -0.0231 -0.0081 22  LEU B O   
7489  C CB  . LEU B 22  ? 0.1644 0.2064 0.1933 0.0093  -0.0080 0.0005  22  LEU B CB  
7490  C CG  . LEU B 22  ? 0.1789 0.1866 0.1993 -0.0145 -0.0016 -0.0095 22  LEU B CG  
7491  C CD1 . LEU B 22  ? 0.1501 0.2189 0.1960 -0.0260 -0.0023 -0.0162 22  LEU B CD1 
7492  C CD2 . LEU B 22  ? 0.1589 0.1920 0.2072 -0.0351 0.0097  -0.0142 22  LEU B CD2 
7504  N N   . ARG B 23  ? 0.1636 0.1539 0.2225 0.0033  -0.0004 0.0007  23  ARG B N   
7505  C CA  . ARG B 23  ? 0.1471 0.1979 0.2290 -0.0086 0.0041  0.0171  23  ARG B CA  
7506  C C   . ARG B 23  ? 0.1639 0.2103 0.2232 -0.0053 -0.0184 -0.0083 23  ARG B C   
7507  O O   . ARG B 23  ? 0.1760 0.1999 0.2244 -0.0534 -0.0319 -0.0015 23  ARG B O   
7508  C CB  . ARG B 23  ? 0.1777 0.1954 0.2468 -0.0315 -0.0234 0.0070  23  ARG B CB  
7509  C CG  . ARG B 23  ? 0.1839 0.2146 0.2666 0.0500  -0.0485 -0.0203 23  ARG B CG  
7510  C CD  . ARG B 23  ? 0.2385 0.3173 0.3015 0.0514  -0.0241 -0.0171 23  ARG B CD  
7511  N NE  . ARG B 23  ? 0.2326 0.3496 0.3303 0.0069  -0.0184 -0.0032 23  ARG B NE  
7512  C CZ  . ARG B 23  ? 0.2453 0.3951 0.3509 -0.0164 -0.0164 -0.0123 23  ARG B CZ  
7513  N NH1 . ARG B 23  ? 0.2728 0.4116 0.3534 0.0161  -0.0503 0.0105  23  ARG B NH1 
7514  N NH2 . ARG B 23  ? 0.2392 0.3687 0.3679 -0.0191 0.0122  -0.0133 23  ARG B NH2 
7528  N N   . ASP B 24  ? 0.1544 0.2263 0.2159 -0.0207 -0.0213 0.0129  24  ASP B N   
7529  C CA  . ASP B 24  ? 0.1546 0.2403 0.2315 -0.0333 -0.0405 -0.0093 24  ASP B CA  
7530  C C   . ASP B 24  ? 0.1435 0.2369 0.2314 -0.0355 -0.0412 -0.0178 24  ASP B C   
7531  O O   . ASP B 24  ? 0.1346 0.2658 0.2506 -0.0136 -0.0590 -0.0145 24  ASP B O   
7532  C CB  . ASP B 24  ? 0.1557 0.2519 0.2642 -0.0037 -0.0067 -0.0436 24  ASP B CB  
7533  C CG  . ASP B 24  ? 0.1567 0.2741 0.2836 0.0266  0.0023  -0.0344 24  ASP B CG  
7534  O OD1 . ASP B 24  ? 0.1780 0.3142 0.3048 0.0484  -0.0122 -0.0376 24  ASP B OD1 
7535  O OD2 . ASP B 24  ? 0.2128 0.2816 0.2894 0.0425  0.0450  -0.0040 24  ASP B OD2 
7540  N N   . PHE B 25  ? 0.1609 0.2039 0.2276 -0.0219 -0.0263 -0.0315 25  PHE B N   
7541  C CA  . PHE B 25  ? 0.1625 0.1880 0.2188 -0.0329 -0.0493 -0.0206 25  PHE B CA  
7542  C C   . PHE B 25  ? 0.1676 0.1575 0.2181 -0.0415 -0.0220 -0.0158 25  PHE B C   
7543  O O   . PHE B 25  ? 0.1947 0.1686 0.2138 -0.0547 -0.0258 -0.0055 25  PHE B O   
7544  C CB  . PHE B 25  ? 0.1497 0.1929 0.2051 -0.0282 -0.0466 0.0069  25  PHE B CB  
7545  C CG  . PHE B 25  ? 0.1590 0.1561 0.1959 -0.0423 -0.0120 0.0089  25  PHE B CG  
7546  C CD1 . PHE B 25  ? 0.1790 0.1885 0.2054 -0.0356 -0.0287 -0.0002 25  PHE B CD1 
7547  C CD2 . PHE B 25  ? 0.1714 0.2094 0.1894 0.0028  -0.0139 -0.0158 25  PHE B CD2 
7548  C CE1 . PHE B 25  ? 0.1868 0.2330 0.2085 -0.0185 -0.0350 0.0180  25  PHE B CE1 
7549  C CE2 . PHE B 25  ? 0.1354 0.1746 0.1997 -0.0565 -0.0092 0.0107  25  PHE B CE2 
7550  C CZ  . PHE B 25  ? 0.1673 0.2019 0.2135 -0.0633 -0.0194 0.0090  25  PHE B CZ  
7560  N N   . ALA B 26  ? 0.1424 0.2188 0.2173 -0.0345 0.0029  -0.0354 26  ALA B N   
7561  C CA  . ALA B 26  ? 0.1508 0.2223 0.2227 -0.0259 -0.0145 -0.0237 26  ALA B CA  
7562  C C   . ALA B 26  ? 0.1681 0.2181 0.2302 -0.0001 -0.0248 -0.0314 26  ALA B C   
7563  O O   . ALA B 26  ? 0.2321 0.2330 0.2417 -0.0424 -0.0374 -0.0512 26  ALA B O   
7564  C CB  . ALA B 26  ? 0.1849 0.2019 0.2302 -0.0545 -0.0298 0.0130  26  ALA B CB  
7570  N N   . HIS B 27  ? 0.1714 0.1882 0.2469 -0.0041 -0.0266 0.0004  27  HIS B N   
7571  C CA  . HIS B 27  ? 0.1697 0.2335 0.2665 -0.0244 -0.0492 0.0243  27  HIS B CA  
7572  C C   . HIS B 27  ? 0.1752 0.2688 0.2805 -0.0177 -0.0491 0.0148  27  HIS B C   
7573  O O   . HIS B 27  ? 0.2212 0.2598 0.3019 -0.0260 -0.0712 0.0462  27  HIS B O   
7574  C CB  . HIS B 27  ? 0.2332 0.2976 0.2764 -0.0667 -0.0620 0.0585  27  HIS B CB  
7575  C CG  . HIS B 27  ? 0.2770 0.3497 0.2914 -0.1209 -0.0817 0.0951  27  HIS B CG  
7576  N ND1 . HIS B 27  ? 0.3428 0.4318 0.3229 -0.1597 -0.0721 0.1087  27  HIS B ND1 
7577  C CD2 . HIS B 27  ? 0.2647 0.3645 0.2958 -0.1067 -0.0802 0.1110  27  HIS B CD2 
7578  C CE1 . HIS B 27  ? 0.3024 0.4413 0.3218 -0.1617 -0.0812 0.1287  27  HIS B CE1 
7579  N NE2 . HIS B 27  ? 0.2606 0.4199 0.2974 -0.0988 -0.0999 0.1106  27  HIS B NE2 
7587  N N   . GLY B 28  ? 0.1666 0.2824 0.2821 -0.0567 -0.0586 -0.0121 28  GLY B N   
7588  C CA  . GLY B 28  ? 0.1864 0.3433 0.2892 -0.0616 -0.0634 -0.0037 28  GLY B CA  
7589  C C   . GLY B 28  ? 0.1641 0.3875 0.2941 -0.0961 -0.0426 -0.0055 28  GLY B C   
7590  O O   . GLY B 28  ? 0.2812 0.4120 0.3175 -0.1412 -0.0273 -0.0429 28  GLY B O   
7594  N N   . GLU B 29  ? 0.1717 0.4114 0.2673 -0.0385 -0.0507 -0.0286 29  GLU B N   
7595  C CA  . GLU B 29  ? 0.1990 0.5282 0.2886 -0.0044 -0.0286 -0.0231 29  GLU B CA  
7596  C C   . GLU B 29  ? 0.2033 0.5378 0.2853 0.0109  0.0251  -0.0091 29  GLU B C   
7597  O O   . GLU B 29  ? 0.3052 0.7042 0.3185 0.0743  0.0281  -0.0194 29  GLU B O   
7598  C CB  . GLU B 29  ? 0.3484 0.6330 0.3293 0.0122  -0.0369 -0.0476 29  GLU B CB  
7599  C CG  . GLU B 29  ? 0.5006 0.7625 0.3760 0.0350  -0.0457 -0.0615 29  GLU B CG  
7600  C CD  . GLU B 29  ? 0.6696 0.8720 0.4100 0.1001  -0.0640 -0.0633 29  GLU B CD  
7601  O OE1 . GLU B 29  ? 0.7400 0.9108 0.4218 0.1189  -0.0572 -0.0683 29  GLU B OE1 
7602  O OE2 . GLU B 29  ? 0.7380 0.9196 0.4367 0.1244  -0.0763 -0.0563 29  GLU B OE2 
7609  N N   . ALA B 30  ? 0.2000 0.3626 0.2566 -0.0073 0.0224  -0.0054 30  ALA B N   
7610  C CA  . ALA B 30  ? 0.2164 0.2935 0.2454 -0.0333 -0.0153 -0.0127 30  ALA B CA  
7611  C C   . ALA B 30  ? 0.1939 0.2472 0.2277 -0.0204 0.0119  -0.0176 30  ALA B C   
7612  O O   . ALA B 30  ? 0.2161 0.2990 0.2299 -0.0361 0.0144  -0.0157 30  ALA B O   
7613  C CB  . ALA B 30  ? 0.2488 0.2615 0.2598 -0.0352 -0.0594 -0.0238 30  ALA B CB  
7619  N N   . PRO B 31  ? 0.1933 0.2331 0.2340 -0.0280 0.0361  0.0037  31  PRO B N   
7620  C CA  . PRO B 31  ? 0.1935 0.2410 0.2302 -0.0296 -0.0026 -0.0044 31  PRO B CA  
7621  C C   . PRO B 31  ? 0.1906 0.2399 0.2263 -0.0479 0.0077  -0.0100 31  PRO B C   
7622  O O   . PRO B 31  ? 0.2241 0.2897 0.2246 -0.0385 0.0042  -0.0223 31  PRO B O   
7623  C CB  . PRO B 31  ? 0.2277 0.2924 0.2409 -0.0387 0.0272  -0.0118 31  PRO B CB  
7624  C CG  . PRO B 31  ? 0.2498 0.2734 0.2411 -0.0211 0.0464  -0.0075 31  PRO B CG  
7625  C CD  . PRO B 31  ? 0.2269 0.2799 0.2416 -0.0282 0.0419  0.0065  31  PRO B CD  
7633  N N   . GLY B 32  ? 0.2060 0.2260 0.2185 -0.0323 -0.0057 -0.0114 32  GLY B N   
7634  C CA  . GLY B 32  ? 0.2398 0.2183 0.2079 -0.0280 -0.0043 0.0025  32  GLY B CA  
7635  C C   . GLY B 32  ? 0.2031 0.2270 0.1976 -0.0528 -0.0106 -0.0098 32  GLY B C   
7636  O O   . GLY B 32  ? 0.1914 0.2559 0.2037 -0.0639 0.0033  -0.0096 32  GLY B O   
7640  N N   . ARG B 33  ? 0.1379 0.2276 0.1813 -0.0559 -0.0068 -0.0107 33  ARG B N   
7641  C CA  . ARG B 33  ? 0.1746 0.2111 0.1816 -0.0623 0.0031  -0.0099 33  ARG B CA  
7642  C C   . ARG B 33  ? 0.1938 0.1880 0.1863 -0.0194 -0.0132 -0.0092 33  ARG B C   
7643  O O   . ARG B 33  ? 0.1913 0.2020 0.1938 -0.0329 -0.0227 -0.0287 33  ARG B O   
7644  C CB  . ARG B 33  ? 0.1841 0.2615 0.1861 -0.0717 0.0256  0.0083  33  ARG B CB  
7645  C CG  . ARG B 33  ? 0.2014 0.2591 0.1950 -0.0480 0.0277  0.0155  33  ARG B CG  
7646  C CD  . ARG B 33  ? 0.1990 0.2934 0.2125 -0.0613 0.0284  0.0125  33  ARG B CD  
7647  N NE  . ARG B 33  ? 0.1817 0.2969 0.2383 -0.0685 0.0323  0.0170  33  ARG B NE  
7648  C CZ  . ARG B 33  ? 0.2556 0.3085 0.2844 -0.0341 0.0707  -0.0258 33  ARG B CZ  
7649  N NH1 . ARG B 33  ? 0.2716 0.3153 0.2948 -0.1053 0.0806  -0.0251 33  ARG B NH1 
7650  N NH2 . ARG B 33  ? 0.2734 0.3085 0.3181 0.0424  0.0683  -0.0386 33  ARG B NH2 
7664  N N   . VAL B 34  ? 0.2074 0.1763 0.1880 -0.0408 0.0008  -0.0010 34  VAL B N   
7665  C CA  . VAL B 34  ? 0.1943 0.1905 0.1905 -0.0426 -0.0117 -0.0179 34  VAL B CA  
7666  C C   . VAL B 34  ? 0.1779 0.2137 0.1944 -0.0577 -0.0267 -0.0083 34  VAL B C   
7667  O O   . VAL B 34  ? 0.1970 0.2204 0.2056 -0.0872 -0.0061 -0.0026 34  VAL B O   
7668  C CB  . VAL B 34  ? 0.1952 0.2325 0.1968 -0.0413 -0.0285 -0.0217 34  VAL B CB  
7669  C CG1 . VAL B 34  ? 0.1885 0.2916 0.2173 -0.0395 -0.0131 -0.0123 34  VAL B CG1 
7670  C CG2 . VAL B 34  ? 0.1937 0.2290 0.1909 -0.0783 -0.0197 -0.0007 34  VAL B CG2 
7680  N N   A MET B 35  ? 0.2225 0.2181 0.2074 -0.0895 -0.0194 0.0008  35  MET B N   
7681  N N   B MET B 35  ? 0.2096 0.2066 0.2029 -0.0636 -0.0176 0.0069  35  MET B N   
7682  C CA  A MET B 35  ? 0.2237 0.2222 0.2100 -0.0970 0.0054  -0.0066 35  MET B CA  
7683  C CA  B MET B 35  ? 0.2089 0.1977 0.2050 -0.0605 0.0021  0.0114  35  MET B CA  
7684  C C   A MET B 35  ? 0.1959 0.1953 0.2186 -0.1077 0.0122  -0.0116 35  MET B C   
7685  C C   B MET B 35  ? 0.1983 0.1942 0.2164 -0.0810 0.0102  -0.0015 35  MET B C   
7686  O O   A MET B 35  ? 0.2136 0.2381 0.2237 -0.0738 0.0042  -0.0181 35  MET B O   
7687  O O   B MET B 35  ? 0.2075 0.2209 0.2196 -0.0621 0.0077  -0.0085 35  MET B O   
7688  C CB  A MET B 35  ? 0.2231 0.2559 0.2130 -0.0956 0.0163  -0.0155 35  MET B CB  
7689  C CB  B MET B 35  ? 0.2003 0.1982 0.1988 -0.0323 0.0063  0.0244  35  MET B CB  
7690  C CG  A MET B 35  ? 0.2417 0.2812 0.2301 -0.1213 0.0028  -0.0298 35  MET B CG  
7691  C CG  B MET B 35  ? 0.2075 0.1958 0.2008 -0.0149 -0.0075 0.0278  35  MET B CG  
7692  S SD  A MET B 35  ? 0.2851 0.3036 0.2539 -0.1297 0.0259  -0.0239 35  MET B SD  
7693  S SD  B MET B 35  ? 0.1986 0.1958 0.2139 -0.0071 0.0193  0.0168  35  MET B SD  
7694  C CE  A MET B 35  ? 0.2745 0.2491 0.2514 -0.1222 0.0498  -0.0364 35  MET B CE  
7695  C CE  B MET B 35  ? 0.2033 0.2255 0.2130 -0.0246 0.0450  0.0294  35  MET B CE  
7714  N N   . ALA B 36  ? 0.2115 0.2036 0.2277 -0.0881 0.0171  -0.0031 36  ALA B N   
7715  C CA  . ALA B 36  ? 0.2534 0.2008 0.2340 -0.0427 -0.0140 -0.0140 36  ALA B CA  
7716  C C   . ALA B 36  ? 0.3024 0.1745 0.2348 -0.0341 -0.0095 -0.0052 36  ALA B C   
7717  O O   . ALA B 36  ? 0.3231 0.1938 0.2416 -0.0671 -0.0347 -0.0067 36  ALA B O   
7718  C CB  . ALA B 36  ? 0.3029 0.2451 0.2429 -0.0587 -0.0343 -0.0255 36  ALA B CB  
7725  N N   . GLY B 37  ? 0.2314 0.1898 0.2253 -0.0357 0.0181  0.0112  37  GLY B N   
7726  C CA  . GLY B 37  ? 0.2197 0.1819 0.2224 -0.0596 0.0031  -0.0042 37  GLY B CA  
7727  C C   . GLY B 37  ? 0.2565 0.1751 0.2125 -0.0733 0.0158  -0.0131 37  GLY B C   
7728  O O   . GLY B 37  ? 0.2482 0.1836 0.2183 -0.0479 -0.0016 0.0064  37  GLY B O   
7732  N N   . GLY B 38  ? 0.2397 0.1813 0.2061 -0.0403 0.0289  -0.0130 38  GLY B N   
7733  C CA  . GLY B 38  ? 0.2516 0.1777 0.2149 -0.0597 0.0315  -0.0110 38  GLY B CA  
7734  C C   . GLY B 38  ? 0.2585 0.2042 0.2230 -0.0624 0.0113  0.0026  38  GLY B C   
7735  O O   . GLY B 38  ? 0.2425 0.2170 0.2306 -0.0828 -0.0097 0.0013  38  GLY B O   
7739  N N   . GLU B 39  ? 0.2563 0.2026 0.2354 -0.0858 0.0179  -0.0008 39  GLU B N   
7740  C CA  . GLU B 39  ? 0.2972 0.2170 0.2376 -0.0925 -0.0025 -0.0200 39  GLU B CA  
7741  C C   . GLU B 39  ? 0.2648 0.2077 0.2229 -0.0634 -0.0088 -0.0106 39  GLU B C   
7742  O O   . GLU B 39  ? 0.3004 0.2050 0.2221 -0.0436 -0.0002 0.0057  39  GLU B O   
7743  C CB  . GLU B 39  ? 0.4442 0.2407 0.2675 -0.0844 0.0201  -0.0177 39  GLU B CB  
7744  C CG  . GLU B 39  ? 0.5963 0.3381 0.3146 -0.0299 0.0310  -0.0021 39  GLU B CG  
7745  C CD  . GLU B 39  ? 0.7439 0.4552 0.3680 -0.0483 -0.0019 0.0158  39  GLU B CD  
7746  O OE1 . GLU B 39  ? 0.8014 0.4990 0.3883 -0.0183 -0.0251 0.0430  39  GLU B OE1 
7747  O OE2 . GLU B 39  ? 0.7643 0.4529 0.3858 -0.0403 0.0114  0.0042  39  GLU B OE2 
7754  N N   . GLY B 40  ? 0.2923 0.2154 0.2180 -0.0646 0.0047  -0.0006 40  GLY B N   
7755  C CA  . GLY B 40  ? 0.2677 0.1588 0.2243 -0.0938 0.0132  -0.0198 40  GLY B CA  
7756  C C   . GLY B 40  ? 0.2260 0.1718 0.2183 -0.0783 0.0181  -0.0086 40  GLY B C   
7757  O O   . GLY B 40  ? 0.2035 0.2054 0.2206 -0.0846 0.0302  0.0027  40  GLY B O   
7761  N N   . ILE B 41  ? 0.2391 0.2192 0.2192 -0.0636 0.0440  0.0084  41  ILE B N   
7762  C CA  . ILE B 41  ? 0.2433 0.2227 0.2137 -0.0896 0.0329  0.0046  41  ILE B CA  
7763  C C   . ILE B 41  ? 0.2225 0.2352 0.2083 -0.0561 0.0228  0.0013  41  ILE B C   
7764  O O   . ILE B 41  ? 0.2154 0.2378 0.2081 -0.0570 0.0138  -0.0038 41  ILE B O   
7765  C CB  . ILE B 41  ? 0.2637 0.2316 0.2225 -0.0640 0.0325  0.0075  41  ILE B CB  
7766  C CG1 . ILE B 41  ? 0.2864 0.2661 0.2104 -0.0375 0.0455  -0.0091 41  ILE B CG1 
7767  C CG2 . ILE B 41  ? 0.2814 0.2365 0.2249 -0.0487 0.0159  -0.0088 41  ILE B CG2 
7768  C CD1 . ILE B 41  ? 0.3633 0.3070 0.2119 -0.0122 0.0364  -0.0223 41  ILE B CD1 
7780  N N   . HIS B 42  ? 0.2268 0.2422 0.2130 -0.0702 0.0181  0.0015  42  HIS B N   
7781  C CA  . HIS B 42  ? 0.1961 0.2651 0.2355 -0.0754 0.0120  -0.0004 42  HIS B CA  
7782  C C   . HIS B 42  ? 0.1899 0.2518 0.2224 -0.0401 0.0225  -0.0061 42  HIS B C   
7783  O O   . HIS B 42  ? 0.2231 0.2595 0.2122 -0.0563 0.0436  -0.0073 42  HIS B O   
7784  C CB  . HIS B 42  ? 0.2249 0.2639 0.2723 -0.0842 0.0155  0.0234  42  HIS B CB  
7785  C CG  . HIS B 42  ? 0.2609 0.2998 0.3078 -0.0936 0.0214  0.0049  42  HIS B CG  
7786  N ND1 . HIS B 42  ? 0.3851 0.3158 0.3334 -0.0740 0.0447  0.0107  42  HIS B ND1 
7787  C CD2 . HIS B 42  ? 0.3003 0.3026 0.3179 -0.1550 0.0217  0.0149  42  HIS B CD2 
7788  C CE1 . HIS B 42  ? 0.3695 0.2790 0.3325 -0.0909 0.0475  0.0198  42  HIS B CE1 
7789  N NE2 . HIS B 42  ? 0.3460 0.3401 0.3366 -0.1358 0.0284  0.0088  42  HIS B NE2 
7797  N N   A VAL B 43  ? 0.1963 0.2563 0.2254 -0.0082 0.0230  -0.0029 43  VAL B N   
7798  N N   B VAL B 43  ? 0.2218 0.2406 0.2285 -0.0098 0.0305  -0.0030 43  VAL B N   
7799  C CA  A VAL B 43  ? 0.1878 0.2609 0.2284 -0.0242 0.0279  0.0029  43  VAL B CA  
7800  C CA  B VAL B 43  ? 0.2191 0.2351 0.2348 -0.0755 0.0375  0.0028  43  VAL B CA  
7801  C C   A VAL B 43  ? 0.2044 0.2502 0.2299 -0.0185 0.0342  0.0162  43  VAL B C   
7802  C C   B VAL B 43  ? 0.2138 0.2110 0.2263 -0.0877 0.0408  0.0053  43  VAL B C   
7803  O O   A VAL B 43  ? 0.1843 0.2472 0.2289 0.0107  0.0227  0.0378  43  VAL B O   
7804  O O   B VAL B 43  ? 0.2202 0.2053 0.2100 -0.0766 0.0360  0.0233  43  VAL B O   
7805  C CB  A VAL B 43  ? 0.1824 0.2844 0.2286 -0.0231 0.0340  -0.0086 43  VAL B CB  
7806  C CB  B VAL B 43  ? 0.2639 0.2667 0.2483 -0.0970 0.0562  -0.0032 43  VAL B CB  
7807  C CG1 A VAL B 43  ? 0.1692 0.2924 0.2175 -0.0357 0.0415  -0.0161 43  VAL B CG1 
7808  C CG1 B VAL B 43  ? 0.2598 0.2631 0.2557 -0.1227 0.0513  -0.0188 43  VAL B CG1 
7809  C CG2 A VAL B 43  ? 0.1948 0.3024 0.2345 -0.0103 0.0316  -0.0115 43  VAL B CG2 
7810  C CG2 B VAL B 43  ? 0.2919 0.3223 0.2459 -0.0894 0.0516  -0.0039 43  VAL B CG2 
7829  N N   . VAL B 44  ? 0.2469 0.2463 0.2296 -0.0473 0.0403  0.0085  44  VAL B N   
7830  C CA  . VAL B 44  ? 0.2251 0.1922 0.2335 -0.0759 0.0393  0.0028  44  VAL B CA  
7831  C C   . VAL B 44  ? 0.1983 0.2233 0.2235 -0.0847 0.0297  -0.0267 44  VAL B C   
7832  O O   . VAL B 44  ? 0.2004 0.2101 0.2132 -0.0678 0.0344  -0.0332 44  VAL B O   
7833  C CB  . VAL B 44  ? 0.3041 0.2302 0.2506 -0.0998 0.0400  0.0004  44  VAL B CB  
7834  C CG1 . VAL B 44  ? 0.3204 0.2232 0.2628 -0.1404 0.0553  -0.0111 44  VAL B CG1 
7835  C CG2 . VAL B 44  ? 0.3333 0.2510 0.2579 -0.0768 0.0213  -0.0159 44  VAL B CG2 
7846  N N   . ASP B 45  ? 0.2159 0.1907 0.2240 -0.0721 0.0156  -0.0101 45  ASP B N   
7847  C CA  . ASP B 45  ? 0.2185 0.1789 0.2340 -0.0690 -0.0063 -0.0137 45  ASP B CA  
7848  C C   . ASP B 45  ? 0.2396 0.1779 0.2412 -0.0849 0.0074  -0.0266 45  ASP B C   
7849  O O   . ASP B 45  ? 0.2484 0.1922 0.2421 -0.0525 0.0311  -0.0050 45  ASP B O   
7850  C CB  . ASP B 45  ? 0.1662 0.2016 0.2372 -0.0520 0.0138  -0.0352 45  ASP B CB  
7851  C CG  . ASP B 45  ? 0.2120 0.2370 0.2437 -0.0471 0.0107  -0.0156 45  ASP B CG  
7852  O OD1 . ASP B 45  ? 0.2331 0.2885 0.2456 -0.1069 0.0322  -0.0336 45  ASP B OD1 
7853  O OD2 . ASP B 45  ? 0.2232 0.2154 0.2506 -0.0396 -0.0030 -0.0395 45  ASP B OD2 
7858  N N   . LYS B 46  ? 0.2203 0.1890 0.2489 -0.0979 -0.0066 -0.0311 46  LYS B N   
7859  C CA  . LYS B 46  ? 0.2526 0.2526 0.2687 -0.0648 0.0010  -0.0551 46  LYS B CA  
7860  C C   . LYS B 46  ? 0.2491 0.2465 0.2712 -0.0742 0.0056  -0.0644 46  LYS B C   
7861  O O   . LYS B 46  ? 0.2794 0.2382 0.2830 -0.1177 0.0149  -0.0846 46  LYS B O   
7862  C CB  . LYS B 46  ? 0.2418 0.2777 0.2829 -0.1209 0.0269  -0.0855 46  LYS B CB  
7863  C CG  . LYS B 46  ? 0.3117 0.3645 0.3116 -0.0621 0.0470  -0.1010 46  LYS B CG  
7864  C CD  . LYS B 46  ? 0.3809 0.4061 0.3501 -0.0300 0.0767  -0.1101 46  LYS B CD  
7865  C CE  . LYS B 46  ? 0.4323 0.4538 0.3973 -0.0310 0.0898  -0.1279 46  LYS B CE  
7866  N NZ  . LYS B 46  ? 0.4783 0.4677 0.4212 0.0467  0.0874  -0.1437 46  LYS B NZ  
7880  N N   . ASP B 47  ? 0.2567 0.2754 0.2669 -0.1097 0.0060  -0.0757 47  ASP B N   
7881  C CA  . ASP B 47  ? 0.2465 0.2732 0.2737 -0.1091 0.0157  -0.0627 47  ASP B CA  
7882  C C   . ASP B 47  ? 0.2699 0.2688 0.2992 -0.1454 0.0114  -0.0588 47  ASP B C   
7883  O O   . ASP B 47  ? 0.2985 0.3112 0.3211 -0.1287 -0.0033 -0.0754 47  ASP B O   
7884  C CB  . ASP B 47  ? 0.2453 0.3197 0.2626 -0.1279 0.0180  -0.0302 47  ASP B CB  
7885  C CG  . ASP B 47  ? 0.2596 0.3150 0.2566 -0.1334 0.0153  -0.0253 47  ASP B CG  
7886  O OD1 . ASP B 47  ? 0.3039 0.3633 0.2379 -0.1028 0.0161  -0.0396 47  ASP B OD1 
7887  O OD2 . ASP B 47  ? 0.2210 0.3248 0.2665 -0.1418 -0.0023 -0.0006 47  ASP B OD2 
7892  N N   . GLY B 48  ? 0.2668 0.2525 0.2952 -0.1063 0.0177  -0.0564 48  GLY B N   
7893  C CA  . GLY B 48  ? 0.2963 0.2316 0.2974 -0.1166 0.0480  -0.0391 48  GLY B CA  
7894  C C   . GLY B 48  ? 0.2818 0.2035 0.2857 -0.1065 0.0401  -0.0446 48  GLY B C   
7895  O O   . GLY B 48  ? 0.3360 0.2325 0.2856 -0.1049 0.0376  -0.0252 48  GLY B O   
7899  N N   . ARG B 49  ? 0.2543 0.2383 0.2807 -0.0828 0.0216  -0.0506 49  ARG B N   
7900  C CA  . ARG B 49  ? 0.1966 0.2422 0.2780 -0.0687 0.0466  -0.0512 49  ARG B CA  
7901  C C   . ARG B 49  ? 0.1899 0.2611 0.2802 -0.0952 0.0511  -0.0267 49  ARG B C   
7902  O O   . ARG B 49  ? 0.2168 0.2600 0.2795 -0.0919 0.0359  -0.0199 49  ARG B O   
7903  C CB  . ARG B 49  ? 0.2082 0.2834 0.2863 -0.0685 0.0218  -0.0630 49  ARG B CB  
7904  C CG  . ARG B 49  ? 0.2268 0.3025 0.2797 -0.0689 0.0339  -0.0534 49  ARG B CG  
7905  C CD  . ARG B 49  ? 0.2257 0.3445 0.2871 -0.0686 0.0172  -0.0536 49  ARG B CD  
7906  N NE  . ARG B 49  ? 0.2128 0.3511 0.2822 -0.0865 0.0182  -0.0641 49  ARG B NE  
7907  C CZ  . ARG B 49  ? 0.2610 0.4015 0.2936 0.0108  0.0313  -0.0515 49  ARG B CZ  
7908  N NH1 . ARG B 49  ? 0.2871 0.3595 0.2962 -0.0054 0.0330  -0.0424 49  ARG B NH1 
7909  N NH2 . ARG B 49  ? 0.3170 0.4294 0.2978 0.0611  0.0306  -0.0662 49  ARG B NH2 
7923  N N   . GLU B 50  ? 0.2375 0.2719 0.2848 -0.0728 0.0688  -0.0217 50  GLU B N   
7924  C CA  . GLU B 50  ? 0.2325 0.2645 0.2913 -0.0927 0.0769  -0.0025 50  GLU B CA  
7925  C C   . GLU B 50  ? 0.2096 0.2422 0.2656 -0.1015 0.0605  -0.0127 50  GLU B C   
7926  O O   . GLU B 50  ? 0.2411 0.2997 0.2681 -0.1010 0.0358  -0.0253 50  GLU B O   
7927  C CB  . GLU B 50  ? 0.2727 0.2835 0.3346 -0.1105 0.0881  0.0113  50  GLU B CB  
7928  C CG  . GLU B 50  ? 0.4299 0.3568 0.3935 -0.1156 0.0966  0.0116  50  GLU B CG  
7929  C CD  . GLU B 50  ? 0.5458 0.4175 0.4404 -0.0693 0.1034  0.0271  50  GLU B CD  
7930  O OE1 . GLU B 50  ? 0.5383 0.4207 0.4588 -0.0715 0.1250  0.0369  50  GLU B OE1 
7931  O OE2 . GLU B 50  ? 0.6347 0.4756 0.4619 -0.0557 0.0791  0.0101  50  GLU B OE2 
7938  N N   . PHE B 51  ? 0.2141 0.1751 0.2458 -0.0866 0.0570  -0.0239 51  PHE B N   
7939  C CA  . PHE B 51  ? 0.2037 0.2254 0.2323 -0.0553 0.0350  -0.0276 51  PHE B CA  
7940  C C   . PHE B 51  ? 0.2023 0.2171 0.2296 -0.0503 0.0542  -0.0066 51  PHE B C   
7941  O O   . PHE B 51  ? 0.2583 0.2095 0.2294 0.0108  0.0537  -0.0042 51  PHE B O   
7942  C CB  . PHE B 51  ? 0.1933 0.2836 0.2284 -0.0965 0.0058  -0.0152 51  PHE B CB  
7943  C CG  . PHE B 51  ? 0.1964 0.2689 0.2206 -0.0694 -0.0092 -0.0183 51  PHE B CG  
7944  C CD1 . PHE B 51  ? 0.2130 0.2187 0.2178 -0.0881 -0.0152 -0.0196 51  PHE B CD1 
7945  C CD2 . PHE B 51  ? 0.2400 0.2832 0.2224 -0.0509 -0.0183 0.0015  51  PHE B CD2 
7946  C CE1 . PHE B 51  ? 0.2546 0.2353 0.2220 -0.0408 -0.0363 -0.0162 51  PHE B CE1 
7947  C CE2 . PHE B 51  ? 0.2569 0.2897 0.2241 -0.0347 -0.0306 0.0119  51  PHE B CE2 
7948  C CZ  . PHE B 51  ? 0.2642 0.2553 0.2209 0.0001  -0.0312 0.0045  51  PHE B CZ  
7958  N N   . ILE B 52  ? 0.1929 0.2144 0.2324 -0.0870 0.0282  0.0218  52  ILE B N   
7959  C CA  . ILE B 52  ? 0.2056 0.2134 0.2336 -0.0736 0.0126  0.0172  52  ILE B CA  
7960  C C   . ILE B 52  ? 0.1854 0.1651 0.2362 -0.0389 0.0168  0.0119  52  ILE B C   
7961  O O   . ILE B 52  ? 0.2209 0.1818 0.2464 -0.0500 0.0014  -0.0005 52  ILE B O   
7962  C CB  . ILE B 52  ? 0.2155 0.2164 0.2251 -0.0824 0.0366  0.0090  52  ILE B CB  
7963  C CG1 . ILE B 52  ? 0.2593 0.2520 0.2275 -0.1023 0.0794  0.0120  52  ILE B CG1 
7964  C CG2 . ILE B 52  ? 0.2577 0.2091 0.2306 -0.0950 0.0337  0.0120  52  ILE B CG2 
7965  C CD1 . ILE B 52  ? 0.3019 0.2827 0.2330 -0.1365 0.0791  0.0272  52  ILE B CD1 
7977  N N   . ASP B 53  ? 0.1980 0.1816 0.2255 -0.0324 0.0211  -0.0034 53  ASP B N   
7978  C CA  . ASP B 53  ? 0.1860 0.1598 0.2158 -0.0463 0.0229  -0.0124 53  ASP B CA  
7979  C C   . ASP B 53  ? 0.2286 0.1949 0.2223 -0.0518 0.0116  -0.0077 53  ASP B C   
7980  O O   . ASP B 53  ? 0.2416 0.1662 0.2195 -0.0750 0.0129  -0.0140 53  ASP B O   
7981  C CB  . ASP B 53  ? 0.2150 0.1461 0.2054 -0.0619 0.0426  -0.0277 53  ASP B CB  
7982  C CG  . ASP B 53  ? 0.2194 0.1831 0.2046 -0.0525 0.0199  -0.0151 53  ASP B CG  
7983  O OD1 . ASP B 53  ? 0.2203 0.1944 0.2003 -0.0491 0.0211  -0.0043 53  ASP B OD1 
7984  O OD2 . ASP B 53  ? 0.1869 0.2098 0.1989 -0.0337 0.0090  -0.0161 53  ASP B OD2 
7989  N N   . GLY B 54  ? 0.1703 0.2059 0.2179 -0.0582 0.0043  -0.0134 54  GLY B N   
7990  C CA  . GLY B 54  ? 0.1971 0.1732 0.2087 -0.0866 0.0111  -0.0075 54  GLY B CA  
7991  C C   . GLY B 54  ? 0.2319 0.1695 0.2116 -0.0733 0.0091  0.0084  54  GLY B C   
7992  O O   . GLY B 54  ? 0.2126 0.1968 0.2174 -0.0664 0.0091  0.0045  54  GLY B O   
7996  N N   . PHE B 55  ? 0.2325 0.1546 0.2000 -0.0706 -0.0079 0.0122  55  PHE B N   
7997  C CA  . PHE B 55  ? 0.2037 0.1875 0.1939 -0.0623 0.0100  -0.0011 55  PHE B CA  
7998  C C   . PHE B 55  ? 0.1821 0.2006 0.1829 -0.0543 0.0254  -0.0280 55  PHE B C   
7999  O O   . PHE B 55  ? 0.1796 0.2079 0.1830 -0.0830 0.0204  -0.0253 55  PHE B O   
8000  C CB  . PHE B 55  ? 0.2173 0.2095 0.1929 -0.0898 -0.0040 -0.0289 55  PHE B CB  
8001  C CG  . PHE B 55  ? 0.2289 0.1990 0.1977 -0.0947 0.0208  -0.0374 55  PHE B CG  
8002  C CD1 . PHE B 55  ? 0.2314 0.2284 0.1951 -0.0735 0.0228  -0.0301 55  PHE B CD1 
8003  C CD2 . PHE B 55  ? 0.2603 0.2275 0.2095 -0.0669 0.0430  -0.0182 55  PHE B CD2 
8004  C CE1 . PHE B 55  ? 0.2396 0.1881 0.2047 -0.0634 0.0577  -0.0247 55  PHE B CE1 
8005  C CE2 . PHE B 55  ? 0.2544 0.1841 0.2061 -0.0420 0.0395  -0.0307 55  PHE B CE2 
8006  C CZ  . PHE B 55  ? 0.2509 0.1328 0.2050 -0.0450 0.0408  -0.0161 55  PHE B CZ  
8016  N N   . ALA B 56  ? 0.1903 0.1996 0.1765 -0.0587 0.0230  -0.0191 56  ALA B N   
8017  C CA  . ALA B 56  ? 0.1758 0.1858 0.1868 -0.0457 0.0068  0.0150  56  ALA B CA  
8018  C C   . ALA B 56  ? 0.1790 0.1893 0.1909 -0.0678 0.0027  0.0198  56  ALA B C   
8019  O O   . ALA B 56  ? 0.1894 0.1670 0.1815 -0.0681 0.0154  0.0099  56  ALA B O   
8020  C CB  . ALA B 56  ? 0.2086 0.1778 0.1952 -0.0411 0.0192  0.0339  56  ALA B CB  
8026  N N   . GLY B 57  ? 0.2004 0.1778 0.1898 -0.0540 -0.0002 0.0139  57  GLY B N   
8027  C CA  . GLY B 57  ? 0.1924 0.1874 0.1839 -0.0509 0.0084  0.0048  57  GLY B CA  
8028  C C   . GLY B 57  ? 0.2260 0.1557 0.1858 -0.0392 0.0175  -0.0223 57  GLY B C   
8029  O O   . GLY B 57  ? 0.2042 0.2043 0.1802 -0.0451 0.0215  -0.0150 57  GLY B O   
8033  N N   . LEU B 58  ? 0.2154 0.1525 0.1953 -0.0338 0.0205  -0.0090 58  LEU B N   
8034  C CA  . LEU B 58  ? 0.1810 0.1721 0.1829 -0.0484 0.0290  -0.0155 58  LEU B CA  
8035  C C   . LEU B 58  ? 0.1782 0.2019 0.1795 -0.0304 0.0002  -0.0171 58  LEU B C   
8036  O O   . LEU B 58  ? 0.1846 0.2049 0.1791 -0.0548 0.0021  -0.0035 58  LEU B O   
8037  C CB  . LEU B 58  ? 0.2048 0.1958 0.1831 -0.0641 0.0175  -0.0027 58  LEU B CB  
8038  C CG  . LEU B 58  ? 0.2149 0.2065 0.1928 -0.0475 0.0109  -0.0011 58  LEU B CG  
8039  C CD1 . LEU B 58  ? 0.2244 0.1628 0.1899 -0.0863 -0.0123 0.0182  58  LEU B CD1 
8040  C CD2 . LEU B 58  ? 0.2277 0.2716 0.2154 -0.0309 0.0151  0.0364  58  LEU B CD2 
8052  N N   . TYR B 59  ? 0.1736 0.1845 0.1872 -0.0498 -0.0165 -0.0091 59  TYR B N   
8053  C CA  . TYR B 59  ? 0.2135 0.1720 0.1932 -0.0617 -0.0124 0.0042  59  TYR B CA  
8054  C C   . TYR B 59  ? 0.2168 0.1685 0.1856 -0.0585 0.0098  -0.0065 59  TYR B C   
8055  O O   . TYR B 59  ? 0.2593 0.1887 0.1755 -0.0575 0.0063  -0.0164 59  TYR B O   
8056  C CB  . TYR B 59  ? 0.2591 0.1679 0.2095 -0.0706 0.0088  -0.0083 59  TYR B CB  
8057  C CG  . TYR B 59  ? 0.2293 0.1616 0.2202 -0.0682 0.0402  -0.0213 59  TYR B CG  
8058  C CD1 . TYR B 59  ? 0.2524 0.1587 0.2411 -0.0671 0.0444  0.0058  59  TYR B CD1 
8059  C CD2 . TYR B 59  ? 0.2140 0.2330 0.2398 -0.0043 0.0109  -0.0236 59  TYR B CD2 
8060  C CE1 . TYR B 59  ? 0.3015 0.1789 0.2611 -0.0476 0.0291  -0.0065 59  TYR B CE1 
8061  C CE2 . TYR B 59  ? 0.2296 0.2057 0.2549 -0.0449 0.0311  -0.0486 59  TYR B CE2 
8062  C CZ  . TYR B 59  ? 0.2739 0.1942 0.2795 -0.0296 0.0000  -0.0348 59  TYR B CZ  
8063  O OH  . TYR B 59  ? 0.3547 0.2479 0.3199 -0.0129 -0.0378 -0.0646 59  TYR B OH  
8073  N N   . CYS B 60  ? 0.1861 0.1827 0.1769 -0.0443 -0.0031 0.0178  60  CYS B N   
8074  C CA  . CYS B 60  ? 0.1999 0.1876 0.1811 -0.0575 -0.0219 0.0088  60  CYS B CA  
8075  C C   . CYS B 60  ? 0.1948 0.1882 0.1888 -0.0452 -0.0177 0.0024  60  CYS B C   
8076  O O   . CYS B 60  ? 0.2144 0.2148 0.1928 -0.0301 -0.0090 0.0029  60  CYS B O   
8077  C CB  . CYS B 60  ? 0.2245 0.1449 0.1787 -0.0696 -0.0121 0.0085  60  CYS B CB  
8078  S SG  . CYS B 60  ? 0.1826 0.2039 0.1750 -0.0456 0.0060  -0.0027 60  CYS B SG  
8084  N N   . VAL B 61  ? 0.1886 0.1359 0.1811 -0.0657 -0.0243 0.0084  61  VAL B N   
8085  C CA  . VAL B 61  ? 0.1841 0.1649 0.1990 -0.0620 -0.0034 0.0124  61  VAL B CA  
8086  C C   . VAL B 61  ? 0.1897 0.1988 0.1980 -0.0593 0.0048  -0.0016 61  VAL B C   
8087  O O   . VAL B 61  ? 0.2351 0.1703 0.1978 -0.0929 -0.0027 0.0091  61  VAL B O   
8088  C CB  . VAL B 61  ? 0.1901 0.1726 0.1998 -0.0647 0.0083  0.0219  61  VAL B CB  
8089  C CG1 . VAL B 61  ? 0.2303 0.2219 0.2047 -0.0601 -0.0044 0.0012  61  VAL B CG1 
8090  C CG2 . VAL B 61  ? 0.2370 0.1868 0.1976 -0.0292 0.0217  -0.0089 61  VAL B CG2 
8100  N N   . ASN B 62  ? 0.1622 0.2299 0.1906 -0.0247 0.0028  -0.0087 62  ASN B N   
8101  C CA  . ASN B 62  ? 0.1863 0.2041 0.1877 -0.0570 0.0333  0.0172  62  ASN B CA  
8102  C C   . ASN B 62  ? 0.2170 0.1736 0.1974 -0.0349 0.0180  0.0066  62  ASN B C   
8103  O O   . ASN B 62  ? 0.2181 0.1884 0.2084 -0.0599 0.0207  0.0120  62  ASN B O   
8104  C CB  . ASN B 62  ? 0.2053 0.1699 0.1749 -0.0481 0.0290  0.0340  62  ASN B CB  
8105  C CG  . ASN B 62  ? 0.2101 0.1652 0.1830 -0.0503 0.0132  0.0068  62  ASN B CG  
8106  O OD1 . ASN B 62  ? 0.2321 0.1634 0.1980 -0.0299 0.0031  0.0013  62  ASN B OD1 
8107  N ND2 . ASN B 62  ? 0.2406 0.1305 0.1809 -0.0201 0.0006  -0.0019 62  ASN B ND2 
8114  N N   . ILE B 63  ? 0.2386 0.1635 0.2124 -0.0691 0.0243  0.0033  63  ILE B N   
8115  C CA  . ILE B 63  ? 0.2274 0.1693 0.2163 -0.0694 -0.0067 0.0001  63  ILE B CA  
8116  C C   . ILE B 63  ? 0.2418 0.1846 0.2304 -0.0741 0.0099  -0.0004 63  ILE B C   
8117  O O   . ILE B 63  ? 0.2369 0.1929 0.2407 -0.0691 0.0311  -0.0324 63  ILE B O   
8118  C CB  . ILE B 63  ? 0.2383 0.1826 0.2070 -0.0682 0.0056  -0.0136 63  ILE B CB  
8119  C CG1 . ILE B 63  ? 0.2405 0.1640 0.2030 -0.0519 -0.0118 -0.0353 63  ILE B CG1 
8120  C CG2 . ILE B 63  ? 0.2554 0.1820 0.2164 -0.0840 -0.0179 0.0158  63  ILE B CG2 
8121  C CD1 . ILE B 63  ? 0.2781 0.1808 0.2040 -0.0176 -0.0232 -0.0211 63  ILE B CD1 
8133  N N   . GLY B 64  ? 0.2215 0.2176 0.2220 -0.0629 0.0026  -0.0063 64  GLY B N   
8134  C CA  . GLY B 64  ? 0.2134 0.2097 0.2159 -0.0612 0.0170  -0.0207 64  GLY B CA  
8135  C C   . GLY B 64  ? 0.2212 0.2080 0.2187 -0.0706 0.0331  -0.0053 64  GLY B C   
8136  O O   . GLY B 64  ? 0.2457 0.1585 0.2349 -0.0522 0.0249  0.0149  64  GLY B O   
8140  N N   . TYR B 65  ? 0.2298 0.1928 0.2024 -0.0439 0.0553  -0.0352 65  TYR B N   
8141  C CA  . TYR B 65  ? 0.2208 0.2292 0.1945 -0.0485 0.0400  -0.0310 65  TYR B CA  
8142  C C   . TYR B 65  ? 0.2335 0.2038 0.2035 -0.0468 0.0225  -0.0128 65  TYR B C   
8143  O O   . TYR B 65  ? 0.3111 0.1624 0.1992 -0.1072 0.0164  -0.0076 65  TYR B O   
8144  C CB  . TYR B 65  ? 0.2179 0.2293 0.1948 -0.0780 0.0273  -0.0415 65  TYR B CB  
8145  C CG  . TYR B 65  ? 0.2139 0.2241 0.2038 -0.0671 0.0288  -0.0199 65  TYR B CG  
8146  C CD1 . TYR B 65  ? 0.2308 0.2220 0.2087 -0.0452 0.0387  -0.0010 65  TYR B CD1 
8147  C CD2 . TYR B 65  ? 0.2453 0.2780 0.2125 -0.0540 0.0321  -0.0312 65  TYR B CD2 
8148  C CE1 . TYR B 65  ? 0.2098 0.1786 0.2085 -0.0015 0.0346  0.0037  65  TYR B CE1 
8149  C CE2 . TYR B 65  ? 0.2267 0.2576 0.2121 -0.0571 0.0483  -0.0071 65  TYR B CE2 
8150  C CZ  . TYR B 65  ? 0.1997 0.1807 0.2007 -0.0293 0.0362  0.0115  65  TYR B CZ  
8151  O OH  . TYR B 65  ? 0.2100 0.2237 0.2050 -0.0390 0.0216  0.0099  65  TYR B OH  
8161  N N   . GLY B 66  ? 0.2599 0.2121 0.2297 -0.0818 -0.0032 -0.0249 66  GLY B N   
8162  C CA  . GLY B 66  ? 0.2554 0.1983 0.2441 -0.0662 -0.0007 -0.0266 66  GLY B CA  
8163  C C   . GLY B 66  ? 0.2415 0.1479 0.2647 -0.0711 0.0001  0.0020  66  GLY B C   
8164  O O   . GLY B 66  ? 0.2900 0.1771 0.2980 -0.0693 -0.0178 -0.0043 66  GLY B O   
8168  N N   . ARG B 67  ? 0.2466 0.1733 0.2559 -0.0869 0.0036  0.0079  67  ARG B N   
8169  C CA  . ARG B 67  ? 0.2914 0.1817 0.2597 -0.0213 -0.0027 0.0095  67  ARG B CA  
8170  C C   . ARG B 67  ? 0.3109 0.1668 0.2749 -0.0219 0.0175  -0.0134 67  ARG B C   
8171  O O   . ARG B 67  ? 0.2791 0.1950 0.2807 -0.0522 0.0200  -0.0337 67  ARG B O   
8172  C CB  . ARG B 67  ? 0.2846 0.1787 0.2544 -0.0223 -0.0208 0.0383  67  ARG B CB  
8173  C CG  . ARG B 67  ? 0.2972 0.1641 0.2379 -0.0631 0.0039  0.0511  67  ARG B CG  
8174  C CD  . ARG B 67  ? 0.3081 0.2084 0.2326 -0.0740 -0.0049 0.0403  67  ARG B CD  
8175  N NE  . ARG B 67  ? 0.2999 0.2211 0.2232 -0.0416 0.0277  0.0179  67  ARG B NE  
8176  C CZ  . ARG B 67  ? 0.3142 0.1687 0.2298 -0.0700 0.0240  0.0158  67  ARG B CZ  
8177  N NH1 . ARG B 67  ? 0.3073 0.1899 0.2197 -0.0116 -0.0018 0.0445  67  ARG B NH1 
8178  N NH2 . ARG B 67  ? 0.3451 0.2365 0.2493 -0.0550 0.0356  -0.0039 67  ARG B NH2 
8192  N N   . THR B 68  ? 0.3272 0.1885 0.2856 -0.0476 0.0197  -0.0312 68  THR B N   
8193  C CA  . THR B 68  ? 0.3338 0.2283 0.2935 -0.0469 0.0124  -0.0230 68  THR B CA  
8194  C C   . THR B 68  ? 0.2877 0.1897 0.2681 -0.0646 0.0310  -0.0029 68  THR B C   
8195  O O   . THR B 68  ? 0.2756 0.1897 0.2692 -0.0277 0.0520  0.0046  68  THR B O   
8196  C CB  . THR B 68  ? 0.4116 0.2896 0.3300 -0.0633 0.0099  -0.0387 68  THR B CB  
8197  O OG1 . THR B 68  ? 0.4990 0.3639 0.3699 -0.0926 0.0388  -0.0589 68  THR B OG1 
8198  C CG2 . THR B 68  ? 0.3838 0.2665 0.3367 -0.0366 0.0055  -0.0821 68  THR B CG2 
8206  N N   . GLU B 69  ? 0.2781 0.1620 0.2625 -0.0647 0.0333  0.0112  69  GLU B N   
8207  C CA  . GLU B 69  ? 0.3138 0.1983 0.2500 -0.0504 0.0125  0.0298  69  GLU B CA  
8208  C C   . GLU B 69  ? 0.3230 0.1783 0.2464 -0.0292 0.0014  0.0261  69  GLU B C   
8209  O O   . GLU B 69  ? 0.3086 0.1573 0.2561 -0.0641 -0.0012 0.0420  69  GLU B O   
8210  C CB  . GLU B 69  ? 0.3537 0.1764 0.2528 -0.0173 -0.0032 0.0530  69  GLU B CB  
8211  C CG  . GLU B 69  ? 0.4057 0.2394 0.2656 -0.0102 -0.0001 0.0541  69  GLU B CG  
8212  C CD  . GLU B 69  ? 0.4734 0.2687 0.2741 -0.0165 0.0006  0.0496  69  GLU B CD  
8213  O OE1 . GLU B 69  ? 0.5119 0.2997 0.2823 0.0099  0.0130  0.0335  69  GLU B OE1 
8214  O OE2 . GLU B 69  ? 0.4869 0.2654 0.2824 -0.0213 -0.0181 0.0474  69  GLU B OE2 
8221  N N   . VAL B 70  ? 0.2723 0.1620 0.2337 0.0052  0.0090  0.0329  70  VAL B N   
8222  C CA  . VAL B 70  ? 0.2433 0.1559 0.2234 -0.0070 0.0207  0.0357  70  VAL B CA  
8223  C C   . VAL B 70  ? 0.2348 0.1594 0.2176 -0.0413 0.0100  0.0160  70  VAL B C   
8224  O O   . VAL B 70  ? 0.2320 0.1686 0.2137 -0.0442 0.0267  0.0090  70  VAL B O   
8225  C CB  . VAL B 70  ? 0.2128 0.1601 0.2249 -0.0408 0.0348  0.0286  70  VAL B CB  
8226  C CG1 . VAL B 70  ? 0.2085 0.1618 0.2305 0.0129  0.0482  0.0247  70  VAL B CG1 
8227  C CG2 . VAL B 70  ? 0.2327 0.2061 0.2383 -0.0320 0.0203  0.0210  70  VAL B CG2 
8237  N N   . ALA B 71  ? 0.2894 0.1878 0.2241 -0.0480 -0.0048 -0.0011 71  ALA B N   
8238  C CA  . ALA B 71  ? 0.2839 0.2151 0.2299 -0.0779 -0.0048 0.0205  71  ALA B CA  
8239  C C   . ALA B 71  ? 0.2906 0.2046 0.2435 -0.0442 -0.0040 0.0258  71  ALA B C   
8240  O O   . ALA B 71  ? 0.2843 0.2116 0.2422 -0.0456 0.0163  0.0209  71  ALA B O   
8241  C CB  . ALA B 71  ? 0.2691 0.1964 0.2343 0.0005  -0.0195 0.0342  71  ALA B CB  
8247  N N   . GLU B 72  ? 0.2795 0.1510 0.2553 -0.0471 -0.0109 -0.0074 72  GLU B N   
8248  C CA  . GLU B 72  ? 0.2997 0.1587 0.2734 -0.0485 0.0162  0.0176  72  GLU B CA  
8249  C C   . GLU B 72  ? 0.2651 0.1526 0.2575 -0.0202 0.0147  -0.0013 72  GLU B C   
8250  O O   . GLU B 72  ? 0.2748 0.1527 0.2551 -0.0026 0.0048  0.0236  72  GLU B O   
8251  C CB  . GLU B 72  ? 0.3366 0.1730 0.3108 -0.0726 0.0275  0.0360  72  GLU B CB  
8252  C CG  . GLU B 72  ? 0.4920 0.2592 0.3756 -0.1012 0.0208  0.0556  72  GLU B CG  
8253  C CD  . GLU B 72  ? 0.6813 0.3969 0.4359 -0.0803 0.0008  0.0043  72  GLU B CD  
8254  O OE1 . GLU B 72  ? 0.7650 0.4521 0.4567 -0.0373 -0.0002 0.0209  72  GLU B OE1 
8255  O OE2 . GLU B 72  ? 0.7384 0.4740 0.4700 -0.0836 -0.0134 -0.0391 72  GLU B OE2 
8262  N N   . ALA B 73  ? 0.2646 0.1675 0.2594 -0.0365 0.0394  0.0142  73  ALA B N   
8263  C CA  . ALA B 73  ? 0.2977 0.1746 0.2440 -0.0134 0.0302  0.0087  73  ALA B CA  
8264  C C   . ALA B 73  ? 0.2885 0.1661 0.2414 -0.0166 0.0306  0.0158  73  ALA B C   
8265  O O   . ALA B 73  ? 0.2717 0.1886 0.2580 -0.0330 0.0148  0.0098  73  ALA B O   
8266  C CB  . ALA B 73  ? 0.2995 0.1960 0.2272 0.0083  0.0339  0.0419  73  ALA B CB  
8272  N N   . ILE B 74  ? 0.2552 0.1310 0.2052 -0.0567 0.0323  0.0129  74  ILE B N   
8273  C CA  . ILE B 74  ? 0.2214 0.1669 0.2068 -0.0359 0.0143  0.0207  74  ILE B CA  
8274  C C   . ILE B 74  ? 0.2282 0.1856 0.2019 -0.0071 0.0069  0.0208  74  ILE B C   
8275  O O   . ILE B 74  ? 0.2288 0.1818 0.2154 -0.0436 0.0288  -0.0195 74  ILE B O   
8276  C CB  . ILE B 74  ? 0.2234 0.2156 0.2160 -0.0149 0.0263  -0.0033 74  ILE B CB  
8277  C CG1 . ILE B 74  ? 0.1758 0.2102 0.2204 -0.0277 0.0084  -0.0121 74  ILE B CG1 
8278  C CG2 . ILE B 74  ? 0.2764 0.1921 0.2183 -0.0207 0.0217  -0.0048 74  ILE B CG2 
8279  C CD1 . ILE B 74  ? 0.2061 0.2109 0.2298 -0.0444 0.0130  -0.0234 74  ILE B CD1 
8291  N N   . HIS B 75  ? 0.2299 0.2109 0.2124 -0.0260 0.0181  -0.0166 75  HIS B N   
8292  C CA  . HIS B 75  ? 0.2762 0.1817 0.2133 -0.0640 -0.0078 -0.0360 75  HIS B CA  
8293  C C   . HIS B 75  ? 0.2672 0.1822 0.2204 -0.0441 0.0245  -0.0174 75  HIS B C   
8294  O O   . HIS B 75  ? 0.2563 0.1922 0.2256 -0.0567 0.0296  -0.0207 75  HIS B O   
8295  C CB  . HIS B 75  ? 0.3159 0.2048 0.2169 -0.0739 -0.0072 -0.0583 75  HIS B CB  
8296  C CG  . HIS B 75  ? 0.3785 0.2101 0.2261 -0.0567 0.0185  -0.0535 75  HIS B CG  
8297  N ND1 . HIS B 75  ? 0.4045 0.2392 0.2322 -0.0358 -0.0049 -0.0446 75  HIS B ND1 
8298  C CD2 . HIS B 75  ? 0.4763 0.2512 0.2442 -0.0274 0.0024  -0.0417 75  HIS B CD2 
8299  C CE1 . HIS B 75  ? 0.4651 0.2643 0.2369 -0.0476 -0.0270 -0.0594 75  HIS B CE1 
8300  N NE2 . HIS B 75  ? 0.5030 0.2292 0.2377 -0.0160 -0.0164 -0.0649 75  HIS B NE2 
8308  N N   . ARG B 76  ? 0.3021 0.1841 0.2285 -0.0246 0.0328  -0.0020 76  ARG B N   
8309  C CA  . ARG B 76  ? 0.2984 0.1900 0.2430 -0.0048 0.0580  -0.0029 76  ARG B CA  
8310  C C   . ARG B 76  ? 0.2589 0.1845 0.2449 -0.0016 0.0464  -0.0072 76  ARG B C   
8311  O O   . ARG B 76  ? 0.2501 0.2129 0.2659 0.0075  0.0367  -0.0286 76  ARG B O   
8312  C CB  . ARG B 76  ? 0.4135 0.2523 0.2862 -0.1119 0.0926  0.0488  76  ARG B CB  
8313  C CG  . ARG B 76  ? 0.5915 0.4287 0.3270 -0.0236 0.1025  0.0658  76  ARG B CG  
8314  C CD  . ARG B 76  ? 0.7143 0.5484 0.3516 0.0295  0.1275  0.1036  76  ARG B CD  
8315  N NE  . ARG B 76  ? 0.8517 0.6315 0.3782 0.0635  0.1120  0.1366  76  ARG B NE  
8316  C CZ  . ARG B 76  ? 0.8989 0.6866 0.4082 0.0768  0.1322  0.1492  76  ARG B CZ  
8317  N NH1 . ARG B 76  ? 0.9193 0.7185 0.4253 0.0927  0.1283  0.1603  76  ARG B NH1 
8318  N NH2 . ARG B 76  ? 0.9183 0.6965 0.4244 0.0730  0.1290  0.1502  76  ARG B NH2 
8332  N N   . GLN B 77  ? 0.2533 0.1261 0.2410 -0.0349 0.0225  0.0102  77  GLN B N   
8333  C CA  . GLN B 77  ? 0.2698 0.1021 0.2377 0.0026  0.0161  -0.0082 77  GLN B CA  
8334  C C   . GLN B 77  ? 0.2796 0.1344 0.2350 -0.0305 0.0031  -0.0044 77  GLN B C   
8335  O O   . GLN B 77  ? 0.2482 0.1977 0.2371 0.0084  0.0163  -0.0016 77  GLN B O   
8336  C CB  . GLN B 77  ? 0.2753 0.0889 0.2280 -0.0158 0.0086  0.0071  77  GLN B CB  
8337  C CG  . GLN B 77  ? 0.2329 0.1208 0.2334 0.0010  0.0122  0.0030  77  GLN B CG  
8338  C CD  . GLN B 77  ? 0.2796 0.1448 0.2386 -0.0052 -0.0170 -0.0001 77  GLN B CD  
8339  O OE1 . GLN B 77  ? 0.3477 0.1479 0.2248 -0.0126 -0.0253 -0.0272 77  GLN B OE1 
8340  N NE2 . GLN B 77  ? 0.2851 0.1711 0.2509 0.0290  -0.0507 -0.0085 77  GLN B NE2 
8349  N N   . ALA B 78  ? 0.2967 0.1164 0.2180 -0.0237 -0.0018 0.0005  78  ALA B N   
8350  C CA  . ALA B 78  ? 0.3226 0.1503 0.2341 -0.0617 0.0206  -0.0066 78  ALA B CA  
8351  C C   . ALA B 78  ? 0.3377 0.1724 0.2491 -0.0518 0.0541  -0.0147 78  ALA B C   
8352  O O   . ALA B 78  ? 0.3627 0.2317 0.2602 -0.0564 0.1000  -0.0147 78  ALA B O   
8353  C CB  . ALA B 78  ? 0.3523 0.1705 0.2189 -0.0373 -0.0092 0.0113  78  ALA B CB  
8359  N N   . LEU B 79  ? 0.3305 0.1733 0.2677 -0.0299 0.0637  -0.0043 79  LEU B N   
8360  C CA  . LEU B 79  ? 0.3684 0.1808 0.3052 -0.0373 0.0627  -0.0138 79  LEU B CA  
8361  C C   . LEU B 79  ? 0.3338 0.1617 0.3186 -0.0305 0.0828  -0.0109 79  LEU B C   
8362  O O   . LEU B 79  ? 0.3341 0.2184 0.3462 -0.0044 0.0794  -0.0656 79  LEU B O   
8363  C CB  . LEU B 79  ? 0.3848 0.1774 0.3236 -0.0508 0.0616  -0.0358 79  LEU B CB  
8364  C CG  . LEU B 79  ? 0.4400 0.2536 0.3391 -0.0988 0.0262  -0.0531 79  LEU B CG  
8365  C CD1 . LEU B 79  ? 0.4668 0.2998 0.3386 -0.1037 -0.0023 -0.0662 79  LEU B CD1 
8366  C CD2 . LEU B 79  ? 0.4580 0.2826 0.3444 -0.0996 0.0357  -0.0551 79  LEU B CD2 
8378  N N   . GLU B 80  ? 0.3402 0.1625 0.3114 -0.0320 0.0441  0.0069  80  GLU B N   
8379  C CA  . GLU B 80  ? 0.3060 0.1650 0.3224 -0.0261 0.0328  0.0118  80  GLU B CA  
8380  C C   . GLU B 80  ? 0.3085 0.1840 0.2914 0.0177  0.0072  0.0192  80  GLU B C   
8381  O O   . GLU B 80  ? 0.3095 0.1579 0.2804 0.0187  0.0056  -0.0058 80  GLU B O   
8382  C CB  . GLU B 80  ? 0.3356 0.2066 0.3685 -0.0127 0.0034  0.0323  80  GLU B CB  
8383  C CG  . GLU B 80  ? 0.3927 0.2551 0.4229 0.0077  0.0108  0.0401  80  GLU B CG  
8384  C CD  . GLU B 80  ? 0.4941 0.3787 0.4835 -0.0331 0.0154  0.0579  80  GLU B CD  
8385  O OE1 . GLU B 80  ? 0.5052 0.3867 0.5064 -0.0663 0.0159  0.0561  80  GLU B OE1 
8386  O OE2 . GLU B 80  ? 0.5566 0.4228 0.5047 0.0192  0.0122  0.0626  80  GLU B OE2 
8393  N N   . LEU B 81  ? 0.2731 0.1802 0.2747 -0.0147 0.0169  0.0295  81  LEU B N   
8394  C CA  . LEU B 81  ? 0.2447 0.1496 0.2538 -0.0073 -0.0043 0.0128  81  LEU B CA  
8395  C C   . LEU B 81  ? 0.2670 0.1533 0.2340 0.0095  0.0071  0.0032  81  LEU B C   
8396  O O   . LEU B 81  ? 0.2844 0.1588 0.2275 0.0482  0.0100  -0.0038 81  LEU B O   
8397  C CB  . LEU B 81  ? 0.2314 0.1805 0.2621 -0.0088 0.0034  0.0015  81  LEU B CB  
8398  C CG  . LEU B 81  ? 0.2472 0.1610 0.2729 -0.0005 -0.0310 0.0076  81  LEU B CG  
8399  C CD1 . LEU B 81  ? 0.2379 0.1974 0.2816 -0.0220 0.0119  0.0376  81  LEU B CD1 
8400  C CD2 . LEU B 81  ? 0.3174 0.1659 0.2933 0.0090  -0.0680 0.0218  81  LEU B CD2 
8412  N N   . ALA B 82  ? 0.2345 0.1373 0.2302 0.0081  0.0031  0.0191  82  ALA B N   
8413  C CA  . ALA B 82  ? 0.2283 0.1686 0.2330 -0.0190 -0.0106 0.0138  82  ALA B CA  
8414  C C   . ALA B 82  ? 0.2156 0.1712 0.2185 0.0132  -0.0006 0.0041  82  ALA B C   
8415  O O   . ALA B 82  ? 0.2093 0.1744 0.2154 -0.0169 -0.0054 0.0201  82  ALA B O   
8416  C CB  . ALA B 82  ? 0.2017 0.1916 0.2483 0.0291  -0.0357 0.0097  82  ALA B CB  
8422  N N   . TYR B 83  ? 0.2144 0.1316 0.2106 -0.0255 0.0097  -0.0063 83  TYR B N   
8423  C CA  . TYR B 83  ? 0.1882 0.1060 0.1889 -0.0314 0.0034  0.0110  83  TYR B CA  
8424  C C   . TYR B 83  ? 0.1852 0.1012 0.1801 -0.0104 -0.0309 -0.0281 83  TYR B C   
8425  O O   . TYR B 83  ? 0.2037 0.1227 0.1940 0.0055  -0.0137 -0.0205 83  TYR B O   
8426  C CB  . TYR B 83  ? 0.2038 0.1534 0.1936 -0.0007 -0.0038 0.0093  83  TYR B CB  
8427  C CG  . TYR B 83  ? 0.1819 0.1819 0.1916 -0.0267 -0.0067 0.0129  83  TYR B CG  
8428  C CD1 . TYR B 83  ? 0.1944 0.1337 0.1968 0.0161  -0.0010 0.0113  83  TYR B CD1 
8429  C CD2 . TYR B 83  ? 0.1849 0.1778 0.1793 -0.0007 -0.0156 0.0015  83  TYR B CD2 
8430  C CE1 . TYR B 83  ? 0.2010 0.1168 0.1893 0.0146  0.0034  0.0122  83  TYR B CE1 
8431  C CE2 . TYR B 83  ? 0.2190 0.1834 0.1806 0.0374  -0.0199 0.0081  83  TYR B CE2 
8432  C CZ  . TYR B 83  ? 0.2098 0.1113 0.1777 -0.0013 0.0032  0.0056  83  TYR B CZ  
8433  O OH  . TYR B 83  ? 0.2176 0.1565 0.1800 0.0066  0.0038  -0.0109 83  TYR B OH  
8443  N N   . TYR B 84  ? 0.2001 0.1704 0.1601 -0.0185 -0.0260 -0.0054 84  TYR B N   
8444  C CA  . TYR B 84  ? 0.1675 0.1390 0.1569 -0.0019 0.0044  -0.0009 84  TYR B CA  
8445  C C   . TYR B 84  ? 0.1856 0.1123 0.1736 -0.0216 -0.0070 -0.0015 84  TYR B C   
8446  O O   . TYR B 84  ? 0.2053 0.1284 0.1818 0.0011  -0.0065 -0.0218 84  TYR B O   
8447  C CB  . TYR B 84  ? 0.2091 0.1536 0.1532 0.0225  0.0240  -0.0115 84  TYR B CB  
8448  C CG  . TYR B 84  ? 0.1868 0.1656 0.1706 0.0215  0.0213  -0.0202 84  TYR B CG  
8449  C CD1 . TYR B 84  ? 0.1972 0.1571 0.1737 0.0175  0.0333  0.0300  84  TYR B CD1 
8450  C CD2 . TYR B 84  ? 0.1902 0.1571 0.1745 -0.0076 -0.0141 0.0025  84  TYR B CD2 
8451  C CE1 . TYR B 84  ? 0.2192 0.1755 0.1834 -0.0023 0.0360  0.0077  84  TYR B CE1 
8452  C CE2 . TYR B 84  ? 0.1507 0.1847 0.1803 0.0332  0.0042  0.0110  84  TYR B CE2 
8453  C CZ  . TYR B 84  ? 0.1875 0.1568 0.1799 -0.0396 0.0016  0.0236  84  TYR B CZ  
8454  O OH  . TYR B 84  ? 0.2234 0.1499 0.1909 -0.0024 -0.0044 0.0024  84  TYR B OH  
8464  N N   . HIS B 85  ? 0.1648 0.1483 0.1829 -0.0081 -0.0080 -0.0075 85  HIS B N   
8465  C CA  . HIS B 85  ? 0.1743 0.1193 0.1734 -0.0051 -0.0135 -0.0068 85  HIS B CA  
8466  C C   . HIS B 85  ? 0.1936 0.1459 0.1712 -0.0105 -0.0261 0.0109  85  HIS B C   
8467  O O   . HIS B 85  ? 0.2125 0.1871 0.1715 0.0139  -0.0126 0.0139  85  HIS B O   
8468  C CB  . HIS B 85  ? 0.1863 0.1048 0.1733 0.0471  -0.0091 -0.0077 85  HIS B CB  
8469  C CG  . HIS B 85  ? 0.1742 0.1386 0.1696 0.0123  -0.0013 0.0054  85  HIS B CG  
8470  N ND1 . HIS B 85  ? 0.1911 0.1442 0.1841 0.0255  -0.0111 0.0247  85  HIS B ND1 
8471  C CD2 . HIS B 85  ? 0.1895 0.1836 0.1873 0.0030  -0.0135 0.0227  85  HIS B CD2 
8472  C CE1 . HIS B 85  ? 0.2139 0.1752 0.1882 -0.0027 -0.0050 0.0066  85  HIS B CE1 
8473  N NE2 . HIS B 85  ? 0.2073 0.1954 0.1837 0.0161  -0.0197 0.0043  85  HIS B NE2 
8481  N N   . THR B 86  ? 0.2010 0.1507 0.1586 0.0201  -0.0324 0.0254  86  THR B N   
8482  C CA  . THR B 86  ? 0.2125 0.1770 0.1627 -0.0149 -0.0167 0.0257  86  THR B CA  
8483  C C   . THR B 86  ? 0.1896 0.1658 0.1596 -0.0284 -0.0269 0.0214  86  THR B C   
8484  O O   . THR B 86  ? 0.2051 0.1755 0.1710 0.0113  -0.0398 0.0386  86  THR B O   
8485  C CB  . THR B 86  ? 0.1835 0.1496 0.1706 -0.0296 0.0046  0.0214  86  THR B CB  
8486  O OG1 . THR B 86  ? 0.1885 0.2260 0.1781 -0.0086 0.0117  -0.0169 86  THR B OG1 
8487  C CG2 . THR B 86  ? 0.1527 0.1972 0.1739 -0.0200 -0.0135 0.0190  86  THR B CG2 
8495  N N   . TYR B 87  ? 0.2102 0.1341 0.1569 0.0128  -0.0093 0.0034  87  TYR B N   
8496  C CA  . TYR B 87  ? 0.1765 0.1113 0.1719 -0.0065 -0.0246 -0.0014 87  TYR B CA  
8497  C C   . TYR B 87  ? 0.1989 0.1678 0.1939 0.0022  -0.0246 0.0073  87  TYR B C   
8498  O O   . TYR B 87  ? 0.1774 0.1766 0.1986 0.0090  -0.0146 0.0410  87  TYR B O   
8499  C CB  . TYR B 87  ? 0.2022 0.1247 0.1655 0.0007  -0.0205 0.0150  87  TYR B CB  
8500  C CG  . TYR B 87  ? 0.1941 0.1468 0.1676 -0.0350 -0.0046 0.0355  87  TYR B CG  
8501  C CD1 . TYR B 87  ? 0.2267 0.1614 0.1730 -0.0351 -0.0165 0.0308  87  TYR B CD1 
8502  C CD2 . TYR B 87  ? 0.1794 0.1801 0.1859 -0.0651 -0.0244 0.0213  87  TYR B CD2 
8503  C CE1 . TYR B 87  ? 0.2175 0.1766 0.1867 -0.0184 -0.0006 0.0060  87  TYR B CE1 
8504  C CE2 . TYR B 87  ? 0.1849 0.1661 0.1872 0.0273  -0.0443 0.0284  87  TYR B CE2 
8505  C CZ  . TYR B 87  ? 0.1539 0.1576 0.1875 0.0010  -0.0384 0.0175  87  TYR B CZ  
8506  O OH  . TYR B 87  ? 0.1868 0.1865 0.1956 0.0033  -0.0399 0.0440  87  TYR B OH  
8516  N N   . VAL B 88  ? 0.2003 0.1602 0.2000 0.0213  -0.0399 0.0049  88  VAL B N   
8517  C CA  . VAL B 88  ? 0.2213 0.1816 0.2202 0.0196  -0.0328 -0.0211 88  VAL B CA  
8518  C C   . VAL B 88  ? 0.1995 0.1557 0.2193 0.0242  -0.0170 -0.0022 88  VAL B C   
8519  O O   . VAL B 88  ? 0.2175 0.1448 0.2270 0.0338  -0.0079 -0.0094 88  VAL B O   
8520  C CB  . VAL B 88  ? 0.1852 0.1721 0.2300 -0.0032 -0.0221 -0.0096 88  VAL B CB  
8521  C CG1 . VAL B 88  ? 0.2095 0.1982 0.2445 -0.0078 -0.0019 0.0046  88  VAL B CG1 
8522  C CG2 . VAL B 88  ? 0.1893 0.2126 0.2316 -0.0146 0.0065  0.0096  88  VAL B CG2 
8532  N N   . GLY B 89  ? 0.1942 0.1524 0.2023 0.0337  0.0046  0.0153  89  GLY B N   
8533  C CA  . GLY B 89  ? 0.2026 0.1642 0.1970 0.0489  0.0181  0.0284  89  GLY B CA  
8534  C C   . GLY B 89  ? 0.1810 0.1601 0.1952 0.0140  -0.0001 0.0105  89  GLY B C   
8535  O O   . GLY B 89  ? 0.2276 0.1593 0.2014 0.0269  -0.0274 0.0022  89  GLY B O   
8539  N N   . HIS B 90  ? 0.2058 0.1761 0.1988 0.0109  -0.0228 0.0032  90  HIS B N   
8540  C CA  . HIS B 90  ? 0.2057 0.1468 0.1905 0.0408  -0.0089 -0.0030 90  HIS B CA  
8541  C C   . HIS B 90  ? 0.1857 0.1515 0.1900 0.0059  -0.0193 -0.0206 90  HIS B C   
8542  O O   . HIS B 90  ? 0.1836 0.1606 0.1925 -0.0170 -0.0130 -0.0061 90  HIS B O   
8543  C CB  . HIS B 90  ? 0.1773 0.1767 0.1801 0.0331  -0.0052 0.0166  90  HIS B CB  
8544  C CG  . HIS B 90  ? 0.2015 0.1719 0.1952 0.0200  0.0075  -0.0036 90  HIS B CG  
8545  N ND1 . HIS B 90  ? 0.2025 0.2403 0.2119 0.0363  0.0177  -0.0117 90  HIS B ND1 
8546  C CD2 . HIS B 90  ? 0.2030 0.1887 0.2087 0.0305  0.0176  0.0137  90  HIS B CD2 
8547  C CE1 . HIS B 90  ? 0.2488 0.2226 0.2140 -0.0218 0.0233  -0.0106 90  HIS B CE1 
8548  N NE2 . HIS B 90  ? 0.2359 0.1835 0.2083 0.0046  0.0232  0.0073  90  HIS B NE2 
8556  N N   . SER B 91  ? 0.2235 0.1250 0.1998 0.0009  -0.0027 0.0020  91  SER B N   
8557  C CA  . SER B 91  ? 0.2050 0.1555 0.1997 -0.0050 -0.0100 0.0412  91  SER B CA  
8558  C C   . SER B 91  ? 0.1978 0.1641 0.1960 0.0287  0.0034  -0.0086 91  SER B C   
8559  O O   . SER B 91  ? 0.2165 0.1884 0.2055 0.0504  0.0286  -0.0192 91  SER B O   
8560  C CB  . SER B 91  ? 0.2466 0.2006 0.2049 -0.0071 -0.0183 0.0477  91  SER B CB  
8561  O OG  . SER B 91  ? 0.2555 0.2109 0.2016 0.0129  -0.0056 0.0350  91  SER B OG  
8567  N N   . ASN B 92  ? 0.2571 0.1381 0.1949 0.0108  -0.0046 -0.0011 92  ASN B N   
8568  C CA  . ASN B 92  ? 0.2176 0.1471 0.1985 0.0331  -0.0082 0.0126  92  ASN B CA  
8569  C C   . ASN B 92  ? 0.2105 0.1774 0.2039 0.0061  -0.0118 0.0022  92  ASN B C   
8570  O O   . ASN B 92  ? 0.2209 0.1661 0.1928 -0.0047 -0.0175 -0.0036 92  ASN B O   
8571  C CB  . ASN B 92  ? 0.2208 0.1329 0.2101 -0.0061 0.0066  -0.0024 92  ASN B CB  
8572  C CG  . ASN B 92  ? 0.2176 0.1789 0.2165 0.0022  0.0074  0.0148  92  ASN B CG  
8573  O OD1 . ASN B 92  ? 0.2472 0.1755 0.2296 0.0035  0.0091  0.0316  92  ASN B OD1 
8574  N ND2 . ASN B 92  ? 0.2134 0.2012 0.2112 0.0215  -0.0085 0.0135  92  ASN B ND2 
8581  N N   . GLU B 93  ? 0.2693 0.1514 0.2014 -0.0181 0.0012  0.0111  93  GLU B N   
8582  C CA  . GLU B 93  ? 0.2918 0.1645 0.2072 -0.0188 0.0075  0.0255  93  GLU B CA  
8583  C C   . GLU B 93  ? 0.3097 0.1647 0.2093 -0.0393 0.0083  0.0333  93  GLU B C   
8584  O O   . GLU B 93  ? 0.3174 0.1721 0.2159 -0.0149 -0.0030 0.0182  93  GLU B O   
8585  C CB  . GLU B 93  ? 0.3853 0.1976 0.2381 -0.0086 0.0073  0.0351  93  GLU B CB  
8586  C CG  . GLU B 93  ? 0.5137 0.2281 0.2786 0.0366  -0.0045 0.0321  93  GLU B CG  
8587  C CD  . GLU B 93  ? 0.6212 0.2610 0.3068 0.0920  -0.0144 0.0332  93  GLU B CD  
8588  O OE1 . GLU B 93  ? 0.6502 0.2619 0.3246 0.1046  -0.0389 0.0216  93  GLU B OE1 
8589  O OE2 . GLU B 93  ? 0.6548 0.2488 0.3193 0.0449  0.0011  0.0381  93  GLU B OE2 
8596  N N   . PRO B 94  ? 0.2725 0.1559 0.2043 -0.0113 0.0177  0.0209  94  PRO B N   
8597  C CA  . PRO B 94  ? 0.2361 0.1341 0.2079 0.0196  0.0118  0.0009  94  PRO B CA  
8598  C C   . PRO B 94  ? 0.2289 0.1404 0.1981 -0.0127 0.0163  0.0141  94  PRO B C   
8599  O O   . PRO B 94  ? 0.2429 0.1751 0.1968 0.0013  0.0157  0.0032  94  PRO B O   
8600  C CB  . PRO B 94  ? 0.2843 0.1506 0.2012 0.0357  0.0022  -0.0437 94  PRO B CB  
8601  C CG  . PRO B 94  ? 0.2976 0.2066 0.2135 -0.0195 0.0196  -0.0233 94  PRO B CG  
8602  C CD  . PRO B 94  ? 0.2604 0.1703 0.2075 0.0177  0.0079  0.0183  94  PRO B CD  
8610  N N   A GLN B 95  ? 0.2112 0.1684 0.1984 -0.0192 0.0153  0.0340  95  GLN B N   
8611  N N   B GLN B 95  ? 0.2062 0.1929 0.1913 -0.0063 0.0060  0.0427  95  GLN B N   
8612  C CA  A GLN B 95  ? 0.2349 0.1553 0.1983 -0.0016 0.0039  0.0246  95  GLN B CA  
8613  C CA  B GLN B 95  ? 0.2252 0.2129 0.1858 0.0187  -0.0065 0.0362  95  GLN B CA  
8614  C C   A GLN B 95  ? 0.2561 0.1612 0.1907 -0.0161 -0.0039 0.0028  95  GLN B C   
8615  C C   B GLN B 95  ? 0.2549 0.2032 0.1812 -0.0084 -0.0089 0.0027  95  GLN B C   
8616  O O   A GLN B 95  ? 0.2679 0.1360 0.1871 -0.0080 -0.0022 0.0228  95  GLN B O   
8617  O O   B GLN B 95  ? 0.2682 0.2028 0.1705 -0.0018 -0.0059 0.0133  95  GLN B O   
8618  C CB  A GLN B 95  ? 0.2282 0.0807 0.2152 -0.0234 0.0013  0.0140  95  GLN B CB  
8619  C CB  B GLN B 95  ? 0.2161 0.2155 0.1986 0.0290  -0.0124 0.0407  95  GLN B CB  
8620  C CG  A GLN B 95  ? 0.2073 0.0816 0.2108 -0.0569 0.0103  0.0145  95  GLN B CG  
8621  C CG  B GLN B 95  ? 0.2274 0.2378 0.1951 0.0211  -0.0200 0.0613  95  GLN B CG  
8622  C CD  A GLN B 95  ? 0.2278 0.1345 0.2046 -0.0361 0.0116  -0.0012 95  GLN B CD  
8623  C CD  B GLN B 95  ? 0.1911 0.2750 0.1802 0.0543  -0.0203 0.0685  95  GLN B CD  
8624  O OE1 A GLN B 95  ? 0.2188 0.1660 0.2012 -0.0090 0.0022  -0.0107 95  GLN B OE1 
8625  O OE1 B GLN B 95  ? 0.1722 0.3374 0.1920 -0.0036 -0.0150 0.0717  95  GLN B OE1 
8626  N NE2 A GLN B 95  ? 0.2640 0.1267 0.1955 0.0202  0.0066  -0.0202 95  GLN B NE2 
8627  N NE2 B GLN B 95  ? 0.1740 0.3117 0.1648 0.0793  -0.0377 0.0583  95  GLN B NE2 
8644  N N   . ILE B 96  ? 0.2566 0.1811 0.1853 0.0117  -0.0195 0.0058  96  ILE B N   
8645  C CA  . ILE B 96  ? 0.2323 0.1609 0.1927 0.0006  -0.0066 0.0346  96  ILE B CA  
8646  C C   . ILE B 96  ? 0.2458 0.1593 0.1972 -0.0014 -0.0243 0.0213  96  ILE B C   
8647  O O   . ILE B 96  ? 0.2414 0.1828 0.1968 0.0013  -0.0097 0.0090  96  ILE B O   
8648  C CB  . ILE B 96  ? 0.2135 0.1690 0.2039 -0.0058 0.0012  0.0442  96  ILE B CB  
8649  C CG1 . ILE B 96  ? 0.2054 0.1687 0.2150 -0.0091 -0.0027 0.0261  96  ILE B CG1 
8650  C CG2 . ILE B 96  ? 0.2359 0.1935 0.2006 -0.0116 0.0055  0.0239  96  ILE B CG2 
8651  C CD1 . ILE B 96  ? 0.2051 0.1587 0.2215 -0.0282 0.0121  0.0072  96  ILE B CD1 
8664  N N   . GLN B 97  ? 0.2549 0.1430 0.2161 -0.0342 -0.0204 0.0114  97  GLN B N   
8665  C CA  . GLN B 97  ? 0.2491 0.1395 0.2380 -0.0349 -0.0142 0.0263  97  GLN B CA  
8666  C C   . GLN B 97  ? 0.2296 0.1686 0.2260 0.0231  -0.0314 0.0349  97  GLN B C   
8667  O O   . GLN B 97  ? 0.2449 0.1755 0.2232 -0.0125 -0.0107 0.0265  97  GLN B O   
8668  C CB  . GLN B 97  ? 0.2543 0.1466 0.2758 -0.0069 -0.0394 0.0489  97  GLN B CB  
8669  C CG  . GLN B 97  ? 0.3035 0.1582 0.3192 -0.0012 -0.0531 0.0371  97  GLN B CG  
8670  C CD  . GLN B 97  ? 0.4242 0.1924 0.3712 0.0443  -0.1141 0.0181  97  GLN B CD  
8671  O OE1 . GLN B 97  ? 0.4994 0.2470 0.4044 0.0193  -0.1011 -0.0379 97  GLN B OE1 
8672  N NE2 . GLN B 97  ? 0.5231 0.2142 0.3968 0.0246  -0.0995 0.0359  97  GLN B NE2 
8681  N N   . LEU B 98  ? 0.1981 0.1582 0.2233 -0.0058 0.0021  0.0513  98  LEU B N   
8682  C CA  . LEU B 98  ? 0.1772 0.1802 0.2093 -0.0214 0.0046  0.0215  98  LEU B CA  
8683  C C   . LEU B 98  ? 0.2181 0.1701 0.2093 -0.0091 0.0139  0.0272  98  LEU B C   
8684  O O   . LEU B 98  ? 0.2404 0.1609 0.1944 0.0161  0.0053  0.0322  98  LEU B O   
8685  C CB  . LEU B 98  ? 0.1877 0.1860 0.2075 -0.0101 -0.0196 0.0283  98  LEU B CB  
8686  C CG  . LEU B 98  ? 0.2239 0.1903 0.1894 -0.0285 -0.0242 0.0362  98  LEU B CG  
8687  C CD1 . LEU B 98  ? 0.2522 0.1772 0.1857 -0.0567 -0.0538 0.0359  98  LEU B CD1 
8688  C CD2 . LEU B 98  ? 0.2520 0.1644 0.1914 -0.0629 0.0020  0.0572  98  LEU B CD2 
8700  N N   . SER B 99  ? 0.2248 0.1311 0.1968 -0.0175 -0.0143 0.0439  99  SER B N   
8701  C CA  . SER B 99  ? 0.2154 0.1128 0.1815 -0.0676 -0.0123 0.0485  99  SER B CA  
8702  C C   . SER B 99  ? 0.2497 0.1496 0.2029 -0.0171 -0.0099 0.0404  99  SER B C   
8703  O O   . SER B 99  ? 0.2136 0.1552 0.2234 0.0187  0.0038  0.0284  99  SER B O   
8704  C CB  . SER B 99  ? 0.2468 0.1494 0.1716 -0.0624 -0.0206 0.0602  99  SER B CB  
8705  O OG  . SER B 99  ? 0.2597 0.1432 0.1719 -0.0052 -0.0130 0.0274  99  SER B OG  
8711  N N   . GLU B 100 ? 0.2525 0.1426 0.2114 -0.0312 -0.0017 0.0488  100 GLU B N   
8712  C CA  . GLU B 100 ? 0.2594 0.1275 0.1988 -0.0168 -0.0028 0.0268  100 GLU B CA  
8713  C C   . GLU B 100 ? 0.2675 0.1815 0.1985 -0.0166 0.0063  0.0260  100 GLU B C   
8714  O O   . GLU B 100 ? 0.2575 0.1922 0.2002 0.0247  0.0204  0.0265  100 GLU B O   
8715  C CB  . GLU B 100 ? 0.2575 0.1211 0.2132 -0.0157 -0.0121 0.0353  100 GLU B CB  
8716  C CG  . GLU B 100 ? 0.2421 0.1597 0.2273 -0.0167 0.0057  0.0219  100 GLU B CG  
8717  C CD  . GLU B 100 ? 0.2578 0.2050 0.2596 -0.0193 0.0039  0.0307  100 GLU B CD  
8718  O OE1 . GLU B 100 ? 0.2689 0.2289 0.2942 0.0005  0.0117  0.0269  100 GLU B OE1 
8719  O OE2 . GLU B 100 ? 0.2624 0.2054 0.2571 -0.0311 -0.0040 0.0229  100 GLU B OE2 
8726  N N   . LYS B 101 ? 0.2594 0.1696 0.2059 -0.0462 0.0047  0.0226  101 LYS B N   
8727  C CA  . LYS B 101 ? 0.2699 0.1640 0.2120 -0.0060 -0.0009 0.0365  101 LYS B CA  
8728  C C   . LYS B 101 ? 0.2580 0.1515 0.1990 -0.0129 0.0168  0.0151  101 LYS B C   
8729  O O   . LYS B 101 ? 0.2318 0.2081 0.2104 0.0375  0.0052  0.0208  101 LYS B O   
8730  C CB  . LYS B 101 ? 0.3341 0.0942 0.2413 0.0008  0.0063  0.0337  101 LYS B CB  
8731  C CG  . LYS B 101 ? 0.4369 0.1407 0.2831 -0.0350 0.0137  0.0660  101 LYS B CG  
8732  C CD  . LYS B 101 ? 0.5288 0.1618 0.3082 -0.0156 0.0037  0.0595  101 LYS B CD  
8733  C CE  . LYS B 101 ? 0.5892 0.2016 0.3283 0.0191  -0.0047 0.0592  101 LYS B CE  
8734  N NZ  . LYS B 101 ? 0.6342 0.2742 0.3512 0.0175  -0.0076 0.0569  101 LYS B NZ  
8748  N N   . ILE B 102 ? 0.2616 0.1414 0.1879 -0.0203 -0.0003 0.0374  102 ILE B N   
8749  C CA  . ILE B 102 ? 0.2117 0.1835 0.1792 -0.0345 -0.0110 0.0274  102 ILE B CA  
8750  C C   . ILE B 102 ? 0.1852 0.1823 0.1839 0.0085  -0.0022 0.0248  102 ILE B C   
8751  O O   . ILE B 102 ? 0.2377 0.2026 0.1944 -0.0134 0.0190  0.0211  102 ILE B O   
8752  C CB  . ILE B 102 ? 0.2095 0.1687 0.1791 -0.0503 0.0063  0.0180  102 ILE B CB  
8753  C CG1 . ILE B 102 ? 0.2110 0.1816 0.1729 -0.0422 -0.0021 -0.0098 102 ILE B CG1 
8754  C CG2 . ILE B 102 ? 0.2540 0.1952 0.1767 -0.0186 0.0089  0.0124  102 ILE B CG2 
8755  C CD1 . ILE B 102 ? 0.2028 0.1717 0.1873 -0.0246 -0.0061 0.0136  102 ILE B CD1 
8767  N N   . LEU B 103 ? 0.1865 0.1764 0.1898 -0.0036 0.0006  0.0133  103 LEU B N   
8768  C CA  . LEU B 103 ? 0.2351 0.1986 0.1827 -0.0147 -0.0178 0.0283  103 LEU B CA  
8769  C C   . LEU B 103 ? 0.2682 0.2364 0.1793 -0.0334 -0.0221 0.0119  103 LEU B C   
8770  O O   . LEU B 103 ? 0.3072 0.2643 0.1871 -0.0269 -0.0255 -0.0075 103 LEU B O   
8771  C CB  . LEU B 103 ? 0.2349 0.1754 0.1940 -0.0117 -0.0117 0.0384  103 LEU B CB  
8772  C CG  . LEU B 103 ? 0.2288 0.1880 0.2145 0.0028  0.0035  0.0142  103 LEU B CG  
8773  C CD1 . LEU B 103 ? 0.2437 0.2044 0.2185 -0.0875 0.0269  0.0135  103 LEU B CD1 
8774  C CD2 . LEU B 103 ? 0.2246 0.2246 0.2207 -0.0086 0.0106  0.0187  103 LEU B CD2 
8786  N N   . GLU B 104 ? 0.2706 0.2181 0.1812 -0.0007 0.0020  0.0242  104 GLU B N   
8787  C CA  . GLU B 104 ? 0.3016 0.1931 0.1984 -0.0163 0.0012  0.0605  104 GLU B CA  
8788  C C   . GLU B 104 ? 0.3013 0.2126 0.1913 -0.0324 0.0131  0.0641  104 GLU B C   
8789  O O   . GLU B 104 ? 0.2958 0.2589 0.1983 -0.0340 0.0217  0.0473  104 GLU B O   
8790  C CB  . GLU B 104 ? 0.3836 0.2063 0.2327 0.0462  0.0085  0.0710  104 GLU B CB  
8791  C CG  . GLU B 104 ? 0.5943 0.3247 0.2791 0.0621  -0.0250 0.0544  104 GLU B CG  
8792  C CD  . GLU B 104 ? 0.7513 0.3442 0.3096 0.0373  -0.0513 0.0780  104 GLU B CD  
8793  O OE1 . GLU B 104 ? 0.8251 0.3179 0.3200 0.0201  -0.0700 0.0667  104 GLU B OE1 
8794  O OE2 . GLU B 104 ? 0.8242 0.4177 0.3376 0.0320  -0.0620 0.0712  104 GLU B OE2 
8801  N N   . LEU B 105 ? 0.2744 0.1813 0.1749 -0.0211 -0.0037 0.0322  105 LEU B N   
8802  C CA  . LEU B 105 ? 0.2362 0.1935 0.1775 -0.0537 0.0092  0.0151  105 LEU B CA  
8803  C C   . LEU B 105 ? 0.2720 0.2066 0.1787 -0.0313 0.0131  -0.0149 105 LEU B C   
8804  O O   . LEU B 105 ? 0.2841 0.2203 0.1894 -0.0216 0.0374  -0.0044 105 LEU B O   
8805  C CB  . LEU B 105 ? 0.2279 0.2184 0.1844 -0.0310 0.0269  0.0167  105 LEU B CB  
8806  C CG  . LEU B 105 ? 0.3273 0.2171 0.1936 -0.0508 0.0236  0.0308  105 LEU B CG  
8807  C CD1 . LEU B 105 ? 0.3618 0.2315 0.1966 -0.0262 -0.0183 0.0168  105 LEU B CD1 
8808  C CD2 . LEU B 105 ? 0.3863 0.2196 0.2234 -0.0840 0.0327  0.0156  105 LEU B CD2 
8820  N N   . ALA B 106 ? 0.2663 0.2028 0.2009 -0.0208 0.0036  -0.0191 106 ALA B N   
8821  C CA  . ALA B 106 ? 0.2866 0.1690 0.2081 -0.0387 0.0240  0.0065  106 ALA B CA  
8822  C C   . ALA B 106 ? 0.2871 0.2415 0.2172 -0.0132 0.0325  -0.0045 106 ALA B C   
8823  O O   . ALA B 106 ? 0.2759 0.3014 0.2333 -0.0441 0.0362  -0.0225 106 ALA B O   
8824  C CB  . ALA B 106 ? 0.3318 0.1708 0.2173 -0.0017 0.0205  -0.0058 106 ALA B CB  
8830  N N   . GLY B 107 ? 0.2713 0.2678 0.2112 -0.0167 0.0273  0.0032  107 GLY B N   
8831  C CA  . GLY B 107 ? 0.3281 0.3247 0.2078 -0.0866 -0.0034 0.0687  107 GLY B CA  
8832  C C   . GLY B 107 ? 0.4053 0.3274 0.2132 -0.1163 -0.0438 0.0879  107 GLY B C   
8833  O O   . GLY B 107 ? 0.3824 0.2658 0.2214 -0.1019 -0.0480 0.0816  107 GLY B O   
8837  N N   . PRO B 108 ? 0.4742 0.4014 0.2196 -0.1749 -0.0531 0.1129  108 PRO B N   
8838  C CA  . PRO B 108 ? 0.5414 0.4659 0.2394 -0.1901 -0.0605 0.0913  108 PRO B CA  
8839  C C   . PRO B 108 ? 0.5443 0.4461 0.2415 -0.1808 -0.0577 0.0317  108 PRO B C   
8840  O O   . PRO B 108 ? 0.5612 0.4424 0.2483 -0.1031 -0.0669 -0.0371 108 PRO B O   
8841  C CB  . PRO B 108 ? 0.5882 0.5442 0.2464 -0.2323 -0.0305 0.1077  108 PRO B CB  
8842  C CG  . PRO B 108 ? 0.6062 0.5780 0.2406 -0.2123 -0.0364 0.0941  108 PRO B CG  
8843  C CD  . PRO B 108 ? 0.5535 0.5074 0.2328 -0.1873 -0.0372 0.1181  108 PRO B CD  
8851  N N   . GLY B 109 ? 0.4663 0.4302 0.2249 -0.2081 -0.0468 0.0674  109 GLY B N   
8852  C CA  . GLY B 109 ? 0.4255 0.3725 0.2164 -0.1509 -0.0360 0.0338  109 GLY B CA  
8853  C C   . GLY B 109 ? 0.3023 0.2815 0.1950 -0.1030 -0.0246 0.0309  109 GLY B C   
8854  O O   . GLY B 109 ? 0.3607 0.2431 0.1682 -0.0709 -0.0058 0.0312  109 GLY B O   
8858  N N   . MET B 110 ? 0.2979 0.1929 0.1944 -0.0524 -0.0306 0.0126  110 MET B N   
8859  C CA  . MET B 110 ? 0.2002 0.2099 0.1847 -0.0107 -0.0278 -0.0059 110 MET B CA  
8860  C C   . MET B 110 ? 0.2399 0.1855 0.1936 0.0208  -0.0313 0.0378  110 MET B C   
8861  O O   . MET B 110 ? 0.2480 0.2180 0.2325 0.0416  0.0226  0.0528  110 MET B O   
8862  C CB  . MET B 110 ? 0.1827 0.2237 0.1878 -0.0002 -0.0321 -0.0383 110 MET B CB  
8863  C CG  . MET B 110 ? 0.1836 0.2515 0.2009 -0.0327 -0.0235 0.0011  110 MET B CG  
8864  S SD  . MET B 110 ? 0.2474 0.1831 0.2164 -0.0193 -0.0096 0.0023  110 MET B SD  
8865  C CE  . MET B 110 ? 0.2985 0.2111 0.2418 -0.0523 0.0050  -0.0303 110 MET B CE  
8875  N N   . SER B 111 ? 0.2660 0.1763 0.1815 0.0361  -0.0358 0.0344  111 SER B N   
8876  C CA  . SER B 111 ? 0.2219 0.1867 0.1819 -0.0217 -0.0297 0.0195  111 SER B CA  
8877  C C   . SER B 111 ? 0.2514 0.1266 0.1692 0.0376  -0.0128 0.0165  111 SER B C   
8878  O O   . SER B 111 ? 0.2294 0.1259 0.1772 0.0123  -0.0174 0.0243  111 SER B O   
8879  C CB  . SER B 111 ? 0.2165 0.1979 0.1931 0.0196  -0.0256 -0.0005 111 SER B CB  
8880  O OG  . SER B 111 ? 0.2059 0.2151 0.2171 0.0106  -0.0069 -0.0103 111 SER B OG  
8886  N N   . LYS B 112 ? 0.1934 0.1500 0.1672 0.0355  0.0125  0.0253  112 LYS B N   
8887  C CA  . LYS B 112 ? 0.1782 0.1227 0.1660 0.0135  0.0094  0.0045  112 LYS B CA  
8888  C C   . LYS B 112 ? 0.1806 0.1269 0.1728 0.0113  0.0079  0.0191  112 LYS B C   
8889  O O   . LYS B 112 ? 0.1798 0.1393 0.1806 0.0036  -0.0188 0.0087  112 LYS B O   
8890  C CB  . LYS B 112 ? 0.2270 0.0887 0.1813 0.0183  0.0053  0.0017  112 LYS B CB  
8891  C CG  . LYS B 112 ? 0.1896 0.1214 0.2054 0.0407  -0.0065 0.0102  112 LYS B CG  
8892  C CD  . LYS B 112 ? 0.1932 0.1089 0.2064 0.0356  -0.0282 0.0152  112 LYS B CD  
8893  C CE  . LYS B 112 ? 0.1923 0.1217 0.2130 0.0007  -0.0355 0.0321  112 LYS B CE  
8894  N NZ  . LYS B 112 ? 0.2170 0.1793 0.2056 -0.0318 -0.0491 0.0136  112 LYS B NZ  
8908  N N   . VAL B 113 ? 0.1873 0.1529 0.1637 0.0232  -0.0177 0.0103  113 VAL B N   
8909  C CA  . VAL B 113 ? 0.1933 0.1361 0.1688 0.0223  -0.0073 0.0036  113 VAL B CA  
8910  C C   . VAL B 113 ? 0.1675 0.1541 0.1690 -0.0125 0.0160  0.0094  113 VAL B C   
8911  O O   . VAL B 113 ? 0.1886 0.2047 0.1678 -0.0129 0.0128  0.0096  113 VAL B O   
8912  C CB  . VAL B 113 ? 0.2315 0.1378 0.1713 0.0006  -0.0045 0.0045  113 VAL B CB  
8913  C CG1 . VAL B 113 ? 0.2260 0.1312 0.1743 -0.0394 0.0009  -0.0075 113 VAL B CG1 
8914  C CG2 . VAL B 113 ? 0.2937 0.1729 0.1708 -0.0319 -0.0044 -0.0004 113 VAL B CG2 
8924  N N   . TYR B 114 ? 0.1821 0.1389 0.1572 -0.0016 -0.0126 0.0153  114 TYR B N   
8925  C CA  . TYR B 114 ? 0.1874 0.1838 0.1529 0.0040  -0.0134 0.0074  114 TYR B CA  
8926  C C   . TYR B 114 ? 0.1695 0.1287 0.1552 0.0037  -0.0044 0.0069  114 TYR B C   
8927  O O   . TYR B 114 ? 0.1494 0.1506 0.1700 -0.0115 -0.0019 -0.0117 114 TYR B O   
8928  C CB  . TYR B 114 ? 0.1787 0.1631 0.1590 -0.0209 -0.0142 0.0130  114 TYR B CB  
8929  C CG  . TYR B 114 ? 0.1968 0.1092 0.1656 -0.0326 -0.0342 0.0038  114 TYR B CG  
8930  C CD1 . TYR B 114 ? 0.1869 0.1528 0.1745 0.0113  -0.0227 0.0206  114 TYR B CD1 
8931  C CD2 . TYR B 114 ? 0.1976 0.1492 0.1778 -0.0417 -0.0164 -0.0110 114 TYR B CD2 
8932  C CE1 . TYR B 114 ? 0.1733 0.1761 0.1786 0.0094  0.0043  0.0276  114 TYR B CE1 
8933  C CE2 . TYR B 114 ? 0.1606 0.1315 0.1743 -0.0325 -0.0206 -0.0022 114 TYR B CE2 
8934  C CZ  . TYR B 114 ? 0.1689 0.1463 0.1738 -0.0284 0.0087  0.0355  114 TYR B CZ  
8935  O OH  . TYR B 114 ? 0.2110 0.1812 0.1960 -0.0458 0.0028  0.0369  114 TYR B OH  
8945  N N   . TYR B 115 ? 0.1642 0.1193 0.1638 -0.0219 0.0068  -0.0128 115 TYR B N   
8946  C CA  . TYR B 115 ? 0.1782 0.1305 0.1641 -0.0325 0.0085  0.0168  115 TYR B CA  
8947  C C   . TYR B 115 ? 0.1715 0.1009 0.1648 -0.0288 0.0114  0.0362  115 TYR B C   
8948  O O   . TYR B 115 ? 0.1968 0.0964 0.1719 -0.0368 -0.0133 0.0147  115 TYR B O   
8949  C CB  . TYR B 115 ? 0.1904 0.1574 0.1701 -0.0032 0.0213  0.0295  115 TYR B CB  
8950  C CG  . TYR B 115 ? 0.2147 0.0940 0.1730 -0.0237 -0.0022 0.0042  115 TYR B CG  
8951  C CD1 . TYR B 115 ? 0.2098 0.1406 0.1732 -0.0324 0.0063  0.0295  115 TYR B CD1 
8952  C CD2 . TYR B 115 ? 0.2049 0.1148 0.1796 -0.0631 -0.0073 -0.0073 115 TYR B CD2 
8953  C CE1 . TYR B 115 ? 0.1965 0.1616 0.1855 -0.0364 0.0015  0.0317  115 TYR B CE1 
8954  C CE2 . TYR B 115 ? 0.2403 0.1329 0.1869 -0.0120 -0.0072 0.0435  115 TYR B CE2 
8955  C CZ  . TYR B 115 ? 0.2046 0.1655 0.1867 0.0003  -0.0192 0.0271  115 TYR B CZ  
8956  O OH  . TYR B 115 ? 0.1851 0.1887 0.1949 -0.0030 -0.0163 0.0494  115 TYR B OH  
8966  N N   . GLY B 116 ? 0.1578 0.1339 0.1557 -0.0265 -0.0219 0.0295  116 GLY B N   
8967  C CA  . GLY B 116 ? 0.1506 0.1239 0.1652 -0.0356 -0.0126 0.0302  116 GLY B CA  
8968  C C   . GLY B 116 ? 0.1342 0.1646 0.1692 -0.0115 -0.0037 0.0100  116 GLY B C   
8969  O O   . GLY B 116 ? 0.1854 0.1638 0.1680 -0.0330 -0.0074 -0.0116 116 GLY B O   
8973  N N   A MET B 117 ? 0.1333 0.1390 0.1658 -0.0278 -0.0393 -0.0025 117 MET B N   
8974  N N   B MET B 117 ? 0.1283 0.1457 0.1687 -0.0175 -0.0259 0.0052  117 MET B N   
8975  C CA  A MET B 117 ? 0.1641 0.1785 0.1715 -0.0391 -0.0177 -0.0219 117 MET B CA  
8976  C CA  B MET B 117 ? 0.1479 0.1731 0.1749 -0.0237 -0.0092 -0.0027 117 MET B CA  
8977  C C   A MET B 117 ? 0.1499 0.1777 0.1809 -0.0634 -0.0204 -0.0406 117 MET B C   
8978  C C   B MET B 117 ? 0.1439 0.1598 0.1753 -0.0338 -0.0131 -0.0206 117 MET B C   
8979  O O   A MET B 117 ? 0.2080 0.2494 0.1893 -0.0430 -0.0279 -0.0862 117 MET B O   
8980  O O   B MET B 117 ? 0.1731 0.1537 0.1587 -0.0306 -0.0031 -0.0286 117 MET B O   
8981  C CB  A MET B 117 ? 0.2007 0.1977 0.1712 -0.0116 0.0019  0.0028  117 MET B CB  
8982  C CB  B MET B 117 ? 0.1676 0.1817 0.1799 0.0055  0.0024  0.0286  117 MET B CB  
8983  C CG  A MET B 117 ? 0.2255 0.1713 0.1688 -0.0104 0.0007  0.0070  117 MET B CG  
8984  C CG  B MET B 117 ? 0.1789 0.1388 0.1813 0.0046  -0.0120 0.0468  117 MET B CG  
8985  S SD  A MET B 117 ? 0.2111 0.2414 0.1732 0.0028  0.0038  -0.0058 117 MET B SD  
8986  S SD  B MET B 117 ? 0.1891 0.2115 0.1889 -0.0290 -0.0123 0.0322  117 MET B SD  
8987  C CE  A MET B 117 ? 0.2147 0.2505 0.1774 -0.0299 -0.0244 0.0147  117 MET B CE  
8988  C CE  B MET B 117 ? 0.1775 0.2350 0.1910 -0.0530 -0.0413 0.0361  117 MET B CE  
9007  N N   . SER B 118 ? 0.1466 0.1525 0.1837 -0.0231 -0.0201 -0.0197 118 SER B N   
9008  C CA  . SER B 118 ? 0.1678 0.1520 0.1704 -0.0350 -0.0007 0.0153  118 SER B CA  
9009  C C   . SER B 118 ? 0.1160 0.1465 0.1726 -0.0228 -0.0091 0.0178  118 SER B C   
9010  O O   . SER B 118 ? 0.1322 0.1644 0.1799 -0.0406 0.0082  0.0024  118 SER B O   
9011  C CB  . SER B 118 ? 0.1931 0.1634 0.1759 -0.0611 -0.0083 -0.0001 118 SER B CB  
9012  O OG  . SER B 118 ? 0.1848 0.1648 0.1754 -0.0284 -0.0196 -0.0002 118 SER B OG  
9019  N N   . GLY B 119 ? 0.1639 0.1688 0.1747 -0.0097 0.0104  0.0005  119 GLY B N   
9020  C CA  . GLY B 119 ? 0.1577 0.1389 0.1589 0.0101  -0.0040 0.0022  119 GLY B CA  
9021  C C   . GLY B 119 ? 0.2011 0.1512 0.1429 -0.0032 -0.0095 0.0054  119 GLY B C   
9022  O O   . GLY B 119 ? 0.1882 0.1491 0.1432 -0.0213 -0.0149 0.0057  119 GLY B O   
9026  N N   . SER B 120 ? 0.1530 0.1480 0.1319 -0.0346 0.0039  0.0045  120 SER B N   
9027  C CA  . SER B 120 ? 0.1645 0.1437 0.1363 -0.0191 -0.0027 0.0051  120 SER B CA  
9028  C C   . SER B 120 ? 0.1611 0.1433 0.1415 0.0243  -0.0026 0.0031  120 SER B C   
9029  O O   . SER B 120 ? 0.1861 0.1352 0.1518 -0.0104 -0.0034 -0.0132 120 SER B O   
9030  C CB  . SER B 120 ? 0.1450 0.1654 0.1398 -0.0031 0.0120  -0.0003 120 SER B CB  
9031  O OG  . SER B 120 ? 0.1551 0.1663 0.1475 -0.0363 0.0031  -0.0149 120 SER B OG  
9037  N N   . ASP B 121 ? 0.1579 0.1426 0.1411 -0.0128 -0.0088 0.0208  121 ASP B N   
9038  C CA  . ASP B 121 ? 0.1497 0.1697 0.1392 -0.0118 -0.0070 0.0133  121 ASP B CA  
9039  C C   . ASP B 121 ? 0.1409 0.1717 0.1402 -0.0101 0.0066  -0.0021 121 ASP B C   
9040  O O   . ASP B 121 ? 0.1630 0.1483 0.1497 -0.0116 -0.0107 -0.0026 121 ASP B O   
9041  C CB  . ASP B 121 ? 0.1594 0.1834 0.1561 -0.0384 0.0075  -0.0183 121 ASP B CB  
9042  C CG  . ASP B 121 ? 0.1734 0.1587 0.1444 -0.0243 0.0061  -0.0347 121 ASP B CG  
9043  O OD1 . ASP B 121 ? 0.1657 0.1887 0.1626 -0.0245 -0.0014 0.0122  121 ASP B OD1 
9044  O OD2 . ASP B 121 ? 0.2457 0.1851 0.1824 0.0165  -0.0059 -0.0733 121 ASP B OD2 
9049  N N   . ALA B 122 ? 0.1439 0.1431 0.1497 -0.0425 0.0017  0.0049  122 ALA B N   
9050  C CA  . ALA B 122 ? 0.1441 0.1365 0.1446 0.0023  -0.0051 0.0201  122 ALA B CA  
9051  C C   . ALA B 122 ? 0.1643 0.1535 0.1510 0.0143  -0.0195 0.0234  122 ALA B C   
9052  O O   . ALA B 122 ? 0.1602 0.1439 0.1558 -0.0108 -0.0158 0.0159  122 ALA B O   
9053  C CB  . ALA B 122 ? 0.1480 0.1228 0.1415 0.0081  0.0009  0.0125  122 ALA B CB  
9059  N N   . ASN B 123 ? 0.1328 0.1352 0.1461 -0.0021 -0.0221 -0.0004 123 ASN B N   
9060  C CA  . ASN B 123 ? 0.1631 0.1301 0.1524 0.0215  0.0091  0.0054  123 ASN B CA  
9061  C C   . ASN B 123 ? 0.1768 0.1433 0.1570 -0.0006 -0.0040 0.0042  123 ASN B C   
9062  O O   . ASN B 123 ? 0.1672 0.1338 0.1622 -0.0016 0.0022  -0.0088 123 ASN B O   
9063  C CB  . ASN B 123 ? 0.1764 0.1378 0.1418 -0.0258 0.0028  0.0074  123 ASN B CB  
9064  C CG  . ASN B 123 ? 0.1680 0.1327 0.1427 -0.0615 0.0053  0.0132  123 ASN B CG  
9065  O OD1 . ASN B 123 ? 0.1689 0.1538 0.1357 -0.0244 0.0058  0.0002  123 ASN B OD1 
9066  N ND2 . ASN B 123 ? 0.1690 0.1604 0.1419 -0.0370 0.0154  0.0115  123 ASN B ND2 
9073  N N   . GLU B 124 ? 0.1869 0.1469 0.1463 -0.0369 -0.0079 -0.0148 124 GLU B N   
9074  C CA  . GLU B 124 ? 0.1607 0.1380 0.1344 0.0087  -0.0207 0.0026  124 GLU B CA  
9075  C C   . GLU B 124 ? 0.1900 0.1744 0.1453 -0.0345 -0.0166 -0.0082 124 GLU B C   
9076  O O   . GLU B 124 ? 0.1758 0.1412 0.1468 -0.0426 -0.0057 0.0041  124 GLU B O   
9077  C CB  . GLU B 124 ? 0.1630 0.1579 0.1296 -0.0146 -0.0257 0.0055  124 GLU B CB  
9078  C CG  . GLU B 124 ? 0.1637 0.1902 0.1370 -0.0417 -0.0252 0.0176  124 GLU B CG  
9079  C CD  . GLU B 124 ? 0.1870 0.1801 0.1660 -0.0863 -0.0029 0.0075  124 GLU B CD  
9080  O OE1 . GLU B 124 ? 0.1760 0.1851 0.1762 -0.0274 0.0110  -0.0026 124 GLU B OE1 
9081  O OE2 . GLU B 124 ? 0.1915 0.1729 0.1752 -0.0458 -0.0197 0.0147  124 GLU B OE2 
9088  N N   . THR B 125 ? 0.1579 0.1752 0.1425 -0.0259 -0.0115 -0.0021 125 THR B N   
9089  C CA  . THR B 125 ? 0.1496 0.1672 0.1457 -0.0267 -0.0171 0.0240  125 THR B CA  
9090  C C   . THR B 125 ? 0.1712 0.1635 0.1448 -0.0257 -0.0016 0.0131  125 THR B C   
9091  O O   . THR B 125 ? 0.1746 0.1284 0.1489 -0.0134 0.0035  0.0048  125 THR B O   
9092  C CB  . THR B 125 ? 0.1519 0.1400 0.1361 0.0014  -0.0305 0.0154  125 THR B CB  
9093  O OG1 . THR B 125 ? 0.1686 0.1536 0.1374 -0.0051 -0.0126 -0.0028 125 THR B OG1 
9094  C CG2 . THR B 125 ? 0.1960 0.1457 0.1382 -0.0060 -0.0128 0.0166  125 THR B CG2 
9102  N N   . GLN B 126 ? 0.1701 0.1563 0.1496 -0.0065 0.0029  -0.0042 126 GLN B N   
9103  C CA  . GLN B 126 ? 0.1476 0.1511 0.1444 0.0077  -0.0160 -0.0174 126 GLN B CA  
9104  C C   . GLN B 126 ? 0.1747 0.1591 0.1385 0.0236  -0.0065 0.0025  126 GLN B C   
9105  O O   . GLN B 126 ? 0.1851 0.1706 0.1211 -0.0312 -0.0083 0.0228  126 GLN B O   
9106  C CB  . GLN B 126 ? 0.1587 0.1603 0.1470 -0.0370 -0.0080 0.0018  126 GLN B CB  
9107  C CG  . GLN B 126 ? 0.1890 0.1566 0.1648 -0.0430 -0.0144 0.0216  126 GLN B CG  
9108  C CD  . GLN B 126 ? 0.2180 0.1498 0.1625 -0.0815 -0.0094 0.0208  126 GLN B CD  
9109  O OE1 . GLN B 126 ? 0.2088 0.1392 0.1629 -0.0503 -0.0041 0.0019  126 GLN B OE1 
9110  N NE2 . GLN B 126 ? 0.1924 0.1405 0.1681 -0.0390 0.0133  0.0336  126 GLN B NE2 
9119  N N   . LEU B 127 ? 0.1274 0.1833 0.1434 -0.0180 -0.0047 0.0282  127 LEU B N   
9120  C CA  . LEU B 127 ? 0.1356 0.1658 0.1422 -0.0223 -0.0178 0.0101  127 LEU B CA  
9121  C C   . LEU B 127 ? 0.1630 0.1498 0.1327 -0.0432 -0.0224 0.0039  127 LEU B C   
9122  O O   . LEU B 127 ? 0.1822 0.1370 0.1295 -0.0397 -0.0076 -0.0154 127 LEU B O   
9123  C CB  . LEU B 127 ? 0.1211 0.1432 0.1483 -0.0339 -0.0110 -0.0152 127 LEU B CB  
9124  C CG  . LEU B 127 ? 0.1603 0.1505 0.1654 -0.0269 -0.0071 0.0025  127 LEU B CG  
9125  C CD1 . LEU B 127 ? 0.2262 0.1761 0.1968 0.0104  0.0099  0.0319  127 LEU B CD1 
9126  C CD2 . LEU B 127 ? 0.2402 0.2354 0.1816 -0.0298 -0.0005 -0.0332 127 LEU B CD2 
9138  N N   . LYS B 128 ? 0.1559 0.1418 0.1420 -0.0118 -0.0167 0.0019  128 LYS B N   
9139  C CA  . LYS B 128 ? 0.1289 0.1110 0.1587 -0.0007 0.0023  -0.0037 128 LYS B CA  
9140  C C   . LYS B 128 ? 0.1565 0.1568 0.1650 -0.0289 -0.0023 0.0051  128 LYS B C   
9141  O O   . LYS B 128 ? 0.1748 0.1696 0.1703 -0.0412 -0.0075 0.0069  128 LYS B O   
9142  C CB  . LYS B 128 ? 0.1915 0.1081 0.1685 -0.0050 0.0009  0.0188  128 LYS B CB  
9143  C CG  . LYS B 128 ? 0.1582 0.1113 0.1639 0.0150  -0.0029 0.0325  128 LYS B CG  
9144  C CD  . LYS B 128 ? 0.1297 0.1153 0.1703 -0.0011 -0.0080 0.0270  128 LYS B CD  
9145  C CE  . LYS B 128 ? 0.1404 0.1252 0.1690 -0.0028 0.0075  -0.0064 128 LYS B CE  
9146  N NZ  . LYS B 128 ? 0.1550 0.1326 0.1579 0.0272  -0.0068 -0.0081 128 LYS B NZ  
9160  N N   . ILE B 129 ? 0.1613 0.1534 0.1502 -0.0263 -0.0182 0.0092  129 ILE B N   
9161  C CA  . ILE B 129 ? 0.1665 0.1661 0.1348 -0.0135 -0.0355 0.0050  129 ILE B CA  
9162  C C   . ILE B 129 ? 0.1862 0.1437 0.1402 -0.0312 -0.0355 0.0073  129 ILE B C   
9163  O O   . ILE B 129 ? 0.1837 0.1420 0.1370 -0.0145 -0.0418 0.0003  129 ILE B O   
9164  C CB  . ILE B 129 ? 0.1628 0.1430 0.1378 -0.0251 -0.0296 0.0286  129 ILE B CB  
9165  C CG1 . ILE B 129 ? 0.1784 0.1561 0.1681 -0.0101 -0.0291 0.0480  129 ILE B CG1 
9166  C CG2 . ILE B 129 ? 0.1935 0.1308 0.1391 -0.0085 -0.0008 0.0157  129 ILE B CG2 
9167  C CD1 . ILE B 129 ? 0.1952 0.1522 0.1765 -0.0084 -0.0349 0.0365  129 ILE B CD1 
9179  N N   . VAL B 130 ? 0.1732 0.1479 0.1492 -0.0331 -0.0418 -0.0003 130 VAL B N   
9180  C CA  . VAL B 130 ? 0.1595 0.1267 0.1668 -0.0613 -0.0109 -0.0187 130 VAL B CA  
9181  C C   . VAL B 130 ? 0.1794 0.1234 0.1630 -0.0394 -0.0340 -0.0166 130 VAL B C   
9182  O O   . VAL B 130 ? 0.2061 0.1316 0.1671 -0.0174 -0.0462 -0.0045 130 VAL B O   
9183  C CB  . VAL B 130 ? 0.1654 0.1787 0.1842 -0.0669 0.0073  -0.0458 130 VAL B CB  
9184  C CG1 . VAL B 130 ? 0.2082 0.2321 0.1952 -0.0571 -0.0196 -0.0446 130 VAL B CG1 
9185  C CG2 . VAL B 130 ? 0.2183 0.1926 0.2027 -0.0130 -0.0067 -0.0615 130 VAL B CG2 
9195  N N   . ARG B 131 ? 0.1748 0.1752 0.1482 -0.0275 -0.0275 -0.0266 131 ARG B N   
9196  C CA  . ARG B 131 ? 0.1803 0.1787 0.1605 -0.0347 -0.0373 -0.0220 131 ARG B CA  
9197  C C   . ARG B 131 ? 0.1712 0.1612 0.1642 -0.0483 -0.0286 -0.0119 131 ARG B C   
9198  O O   . ARG B 131 ? 0.1693 0.1391 0.1655 -0.0499 -0.0300 0.0046  131 ARG B O   
9199  C CB  . ARG B 131 ? 0.1839 0.1801 0.1686 -0.0998 -0.0441 0.0029  131 ARG B CB  
9200  C CG  . ARG B 131 ? 0.1877 0.1718 0.1875 -0.0552 -0.0608 0.0087  131 ARG B CG  
9201  C CD  . ARG B 131 ? 0.1649 0.2754 0.1944 -0.0151 -0.0336 0.0358  131 ARG B CD  
9202  N NE  . ARG B 131 ? 0.1801 0.3521 0.2049 0.0148  -0.0286 0.0414  131 ARG B NE  
9203  C CZ  . ARG B 131 ? 0.1684 0.2879 0.1897 -0.0305 -0.0203 -0.0122 131 ARG B CZ  
9204  N NH1 . ARG B 131 ? 0.1921 0.2197 0.1904 0.0134  0.0145  -0.0394 131 ARG B NH1 
9205  N NH2 . ARG B 131 ? 0.2054 0.3593 0.1906 -0.0150 0.0007  -0.0469 131 ARG B NH2 
9219  N N   . TYR B 132 ? 0.1613 0.1860 0.1627 -0.0650 0.0170  -0.0236 132 TYR B N   
9220  C CA  . TYR B 132 ? 0.1625 0.1583 0.1656 -0.0153 -0.0012 0.0010  132 TYR B CA  
9221  C C   . TYR B 132 ? 0.1366 0.1494 0.1582 -0.0011 0.0059  -0.0005 132 TYR B C   
9222  O O   . TYR B 132 ? 0.1545 0.1570 0.1758 -0.0394 -0.0134 0.0002  132 TYR B O   
9223  C CB  . TYR B 132 ? 0.1966 0.1759 0.1658 0.0048  0.0119  -0.0255 132 TYR B CB  
9224  C CG  . TYR B 132 ? 0.1926 0.1512 0.1672 -0.0207 -0.0076 -0.0230 132 TYR B CG  
9225  C CD1 . TYR B 132 ? 0.2256 0.1314 0.1747 0.0091  -0.0233 -0.0283 132 TYR B CD1 
9226  C CD2 . TYR B 132 ? 0.2046 0.1652 0.1607 -0.0264 -0.0235 -0.0158 132 TYR B CD2 
9227  C CE1 . TYR B 132 ? 0.2115 0.1410 0.1800 0.0057  -0.0115 0.0031  132 TYR B CE1 
9228  C CE2 . TYR B 132 ? 0.2342 0.1835 0.1723 0.0019  -0.0347 -0.0038 132 TYR B CE2 
9229  C CZ  . TYR B 132 ? 0.1936 0.1496 0.1895 0.0198  -0.0392 -0.0021 132 TYR B CZ  
9230  O OH  . TYR B 132 ? 0.2025 0.2158 0.2047 0.0316  -0.0533 0.0011  132 TYR B OH  
9240  N N   . TYR B 133 ? 0.1807 0.1132 0.1526 -0.0053 -0.0026 0.0132  133 TYR B N   
9241  C CA  . TYR B 133 ? 0.1583 0.1347 0.1396 -0.0076 -0.0250 0.0094  133 TYR B CA  
9242  C C   . TYR B 133 ? 0.1676 0.1436 0.1349 -0.0241 -0.0359 0.0213  133 TYR B C   
9243  O O   . TYR B 133 ? 0.1657 0.1730 0.1476 -0.0202 -0.0352 0.0051  133 TYR B O   
9244  C CB  . TYR B 133 ? 0.1707 0.1448 0.1458 -0.0256 -0.0275 -0.0003 133 TYR B CB  
9245  C CG  . TYR B 133 ? 0.2141 0.1182 0.1498 -0.0389 -0.0199 0.0111  133 TYR B CG  
9246  C CD1 . TYR B 133 ? 0.2835 0.1494 0.1588 -0.0309 -0.0112 -0.0024 133 TYR B CD1 
9247  C CD2 . TYR B 133 ? 0.2231 0.1619 0.1498 -0.0499 -0.0361 0.0279  133 TYR B CD2 
9248  C CE1 . TYR B 133 ? 0.3797 0.2131 0.1639 -0.0443 0.0164  0.0054  133 TYR B CE1 
9249  C CE2 . TYR B 133 ? 0.2728 0.2152 0.1531 -0.0916 -0.0423 0.0353  133 TYR B CE2 
9250  C CZ  . TYR B 133 ? 0.3966 0.2667 0.1466 -0.0969 -0.0206 0.0124  133 TYR B CZ  
9251  O OH  . TYR B 133 ? 0.5020 0.3088 0.1532 -0.1665 0.0314  -0.0112 133 TYR B OH  
9261  N N   . ASN B 134 ? 0.1567 0.1368 0.1458 -0.0112 -0.0011 0.0070  134 ASN B N   
9262  C CA  . ASN B 134 ? 0.1577 0.1405 0.1635 0.0076  -0.0114 0.0185  134 ASN B CA  
9263  C C   . ASN B 134 ? 0.1583 0.1424 0.1623 -0.0246 -0.0041 -0.0042 134 ASN B C   
9264  O O   . ASN B 134 ? 0.1557 0.1722 0.1780 -0.0283 -0.0042 -0.0383 134 ASN B O   
9265  C CB  . ASN B 134 ? 0.1913 0.1150 0.1591 -0.0321 0.0042  0.0130  134 ASN B CB  
9266  C CG  . ASN B 134 ? 0.1771 0.1576 0.1537 0.0119  0.0275  0.0083  134 ASN B CG  
9267  O OD1 . ASN B 134 ? 0.2139 0.2044 0.1443 -0.0248 0.0258  -0.0083 134 ASN B OD1 
9268  N ND2 . ASN B 134 ? 0.1975 0.1912 0.1469 -0.0156 -0.0066 0.0233  134 ASN B ND2 
9275  N N   . ASN B 135 ? 0.1764 0.1632 0.1575 -0.0256 -0.0250 -0.0086 135 ASN B N   
9276  C CA  . ASN B 135 ? 0.1626 0.1878 0.1511 -0.0203 -0.0049 -0.0066 135 ASN B CA  
9277  C C   . ASN B 135 ? 0.1342 0.2109 0.1680 -0.0337 -0.0015 -0.0010 135 ASN B C   
9278  O O   . ASN B 135 ? 0.1561 0.1966 0.1725 -0.0386 -0.0031 -0.0059 135 ASN B O   
9279  C CB  . ASN B 135 ? 0.1308 0.1869 0.1514 -0.0466 -0.0119 0.0239  135 ASN B CB  
9280  C CG  . ASN B 135 ? 0.1558 0.1450 0.1613 -0.0339 -0.0173 0.0039  135 ASN B CG  
9281  O OD1 . ASN B 135 ? 0.2238 0.1346 0.1641 -0.0175 -0.0031 -0.0192 135 ASN B OD1 
9282  N ND2 . ASN B 135 ? 0.1709 0.1776 0.1724 0.0015  -0.0369 0.0133  135 ASN B ND2 
9289  N N   . VAL B 136 ? 0.1724 0.2189 0.1734 -0.0146 -0.0152 -0.0012 136 VAL B N   
9290  C CA  . VAL B 136 ? 0.1432 0.1775 0.1852 -0.0222 -0.0176 0.0056  136 VAL B CA  
9291  C C   . VAL B 136 ? 0.1237 0.1714 0.1769 -0.0281 -0.0240 -0.0044 136 VAL B C   
9292  O O   . VAL B 136 ? 0.1414 0.2153 0.1834 0.0042  -0.0260 -0.0243 136 VAL B O   
9293  C CB  . VAL B 136 ? 0.1763 0.2318 0.2041 -0.0014 -0.0336 -0.0179 136 VAL B CB  
9294  C CG1 . VAL B 136 ? 0.2268 0.1988 0.2251 -0.0332 0.0065  -0.0289 136 VAL B CG1 
9295  C CG2 . VAL B 136 ? 0.2128 0.2734 0.2102 0.0244  -0.0492 -0.0628 136 VAL B CG2 
9305  N N   . LEU B 137 ? 0.1836 0.1681 0.1777 0.0238  -0.0271 -0.0033 137 LEU B N   
9306  C CA  . LEU B 137 ? 0.1781 0.1736 0.1728 0.0036  -0.0046 -0.0169 137 LEU B CA  
9307  C C   . LEU B 137 ? 0.1854 0.1941 0.1688 -0.0296 0.0062  0.0135  137 LEU B C   
9308  O O   . LEU B 137 ? 0.2090 0.1946 0.1881 -0.0556 -0.0184 0.0048  137 LEU B O   
9309  C CB  . LEU B 137 ? 0.1867 0.1854 0.1862 -0.0188 -0.0018 -0.0009 137 LEU B CB  
9310  C CG  . LEU B 137 ? 0.1801 0.1774 0.1907 0.0087  -0.0223 0.0003  137 LEU B CG  
9311  C CD1 . LEU B 137 ? 0.2126 0.2162 0.1953 -0.0017 -0.0160 0.0238  137 LEU B CD1 
9312  C CD2 . LEU B 137 ? 0.2073 0.1682 0.2038 -0.0233 -0.0493 -0.0054 137 LEU B CD2 
9324  N N   . GLY B 138 ? 0.1810 0.1857 0.1516 -0.0251 -0.0082 0.0167  138 GLY B N   
9325  C CA  . GLY B 138 ? 0.1739 0.1728 0.1676 -0.0293 -0.0041 0.0128  138 GLY B CA  
9326  C C   . GLY B 138 ? 0.2153 0.1148 0.1691 -0.0275 -0.0005 0.0056  138 GLY B C   
9327  O O   . GLY B 138 ? 0.2296 0.1294 0.1738 -0.0394 -0.0264 -0.0123 138 GLY B O   
9331  N N   . ARG B 139 ? 0.1995 0.1402 0.1602 -0.0193 0.0094  -0.0019 139 ARG B N   
9332  C CA  . ARG B 139 ? 0.1575 0.1601 0.1557 0.0025  0.0076  0.0006  139 ARG B CA  
9333  C C   . ARG B 139 ? 0.1476 0.1428 0.1603 -0.0323 0.0067  -0.0120 139 ARG B C   
9334  O O   . ARG B 139 ? 0.1574 0.1913 0.1856 -0.0289 -0.0215 -0.0039 139 ARG B O   
9335  C CB  . ARG B 139 ? 0.1876 0.1587 0.1521 -0.0435 -0.0176 0.0195  139 ARG B CB  
9336  C CG  . ARG B 139 ? 0.2099 0.1455 0.1529 -0.0312 -0.0149 0.0116  139 ARG B CG  
9337  C CD  . ARG B 139 ? 0.1861 0.1526 0.1552 0.0041  -0.0055 -0.0055 139 ARG B CD  
9338  N NE  . ARG B 139 ? 0.1946 0.0977 0.1542 -0.0206 -0.0109 0.0485  139 ARG B NE  
9339  C CZ  . ARG B 139 ? 0.2241 0.0842 0.1559 -0.0402 0.0031  0.0231  139 ARG B CZ  
9340  N NH1 . ARG B 139 ? 0.1983 0.1381 0.1694 -0.0178 0.0123  0.0247  139 ARG B NH1 
9341  N NH2 . ARG B 139 ? 0.2242 0.1358 0.1605 -0.0412 0.0017  -0.0001 139 ARG B NH2 
9355  N N   . PRO B 140 ? 0.1432 0.1462 0.1585 -0.0207 0.0091  0.0089  140 PRO B N   
9356  C CA  . PRO B 140 ? 0.1746 0.1627 0.1438 -0.0090 0.0300  0.0245  140 PRO B CA  
9357  C C   . PRO B 140 ? 0.1734 0.1502 0.1552 -0.0259 -0.0014 0.0259  140 PRO B C   
9358  O O   . PRO B 140 ? 0.1905 0.1822 0.1617 -0.0077 -0.0216 0.0108  140 PRO B O   
9359  C CB  . PRO B 140 ? 0.1978 0.2177 0.1584 -0.0354 0.0155  0.0440  140 PRO B CB  
9360  C CG  . PRO B 140 ? 0.2230 0.2315 0.1711 -0.0390 -0.0062 0.0341  140 PRO B CG  
9361  C CD  . PRO B 140 ? 0.1705 0.1631 0.1602 -0.0297 -0.0219 0.0041  140 PRO B CD  
9369  N N   . GLN B 141 ? 0.1859 0.1413 0.1653 -0.0180 -0.0187 0.0252  141 GLN B N   
9370  C CA  . GLN B 141 ? 0.1725 0.1352 0.1832 -0.0332 -0.0132 0.0361  141 GLN B CA  
9371  C C   . GLN B 141 ? 0.1551 0.1540 0.1796 0.0082  0.0022  0.0464  141 GLN B C   
9372  O O   . GLN B 141 ? 0.1777 0.1581 0.2047 0.0055  0.0130  -0.0019 141 GLN B O   
9373  C CB  . GLN B 141 ? 0.2538 0.1360 0.2070 -0.0544 -0.0020 0.0381  141 GLN B CB  
9374  C CG  . GLN B 141 ? 0.2917 0.1694 0.2271 -0.0205 0.0147  0.0228  141 GLN B CG  
9375  C CD  . GLN B 141 ? 0.3851 0.2200 0.2420 -0.0483 0.0243  0.0237  141 GLN B CD  
9376  O OE1 . GLN B 141 ? 0.4045 0.2567 0.2648 -0.0281 0.0200  0.0109  141 GLN B OE1 
9377  N NE2 . GLN B 141 ? 0.3690 0.2432 0.2467 -0.1119 0.0657  0.0117  141 GLN B NE2 
9386  N N   . LYS B 142 ? 0.1392 0.1331 0.1901 0.0225  -0.0105 0.0021  142 LYS B N   
9387  C CA  . LYS B 142 ? 0.1548 0.1402 0.1724 -0.0108 -0.0016 0.0120  142 LYS B CA  
9388  C C   . LYS B 142 ? 0.1591 0.1791 0.1645 -0.0021 0.0006  0.0038  142 LYS B C   
9389  O O   . LYS B 142 ? 0.1719 0.1744 0.1489 -0.0395 -0.0122 0.0190  142 LYS B O   
9390  C CB  . LYS B 142 ? 0.1357 0.1798 0.1673 -0.0550 -0.0176 -0.0084 142 LYS B CB  
9391  C CG  . LYS B 142 ? 0.1773 0.1695 0.1710 -0.0531 -0.0045 0.0066  142 LYS B CG  
9392  C CD  . LYS B 142 ? 0.1756 0.1754 0.1855 0.0084  0.0064  0.0129  142 LYS B CD  
9393  C CE  . LYS B 142 ? 0.1836 0.1693 0.1970 0.0232  0.0092  0.0146  142 LYS B CE  
9394  N NZ  . LYS B 142 ? 0.1684 0.1981 0.1836 0.0003  -0.0177 0.0229  142 LYS B NZ  
9408  N N   . LYS B 143 ? 0.1574 0.1708 0.1676 0.0200  -0.0065 0.0173  143 LYS B N   
9409  C CA  . LYS B 143 ? 0.1821 0.1913 0.1616 -0.0351 -0.0207 0.0180  143 LYS B CA  
9410  C C   . LYS B 143 ? 0.1764 0.1648 0.1737 -0.0131 -0.0175 -0.0064 143 LYS B C   
9411  O O   . LYS B 143 ? 0.1768 0.1687 0.1794 -0.0298 -0.0332 -0.0179 143 LYS B O   
9412  C CB  . LYS B 143 ? 0.1980 0.1806 0.1648 -0.0380 -0.0124 0.0329  143 LYS B CB  
9413  C CG  . LYS B 143 ? 0.1914 0.1371 0.1706 -0.0511 -0.0181 0.0149  143 LYS B CG  
9414  C CD  . LYS B 143 ? 0.1968 0.0936 0.1659 -0.0424 -0.0161 0.0114  143 LYS B CD  
9415  C CE  . LYS B 143 ? 0.1973 0.1666 0.1508 -0.0055 -0.0111 -0.0177 143 LYS B CE  
9416  N NZ  . LYS B 143 ? 0.2154 0.1882 0.1446 -0.0229 -0.0059 -0.0091 143 LYS B NZ  
9430  N N   . LYS B 144 ? 0.1905 0.1694 0.1620 -0.0085 -0.0272 0.0069  144 LYS B N   
9431  C CA  . LYS B 144 ? 0.1704 0.1576 0.1627 -0.0128 -0.0300 0.0005  144 LYS B CA  
9432  C C   . LYS B 144 ? 0.1328 0.1783 0.1591 -0.0444 -0.0164 0.0010  144 LYS B C   
9433  O O   . LYS B 144 ? 0.1792 0.1641 0.1537 -0.0156 -0.0307 0.0046  144 LYS B O   
9434  C CB  . LYS B 144 ? 0.1598 0.1612 0.1651 -0.0135 -0.0001 0.0010  144 LYS B CB  
9435  C CG  . LYS B 144 ? 0.1841 0.1683 0.1674 -0.0130 -0.0131 0.0188  144 LYS B CG  
9436  C CD  . LYS B 144 ? 0.2076 0.1296 0.1877 -0.0284 -0.0189 0.0007  144 LYS B CD  
9437  C CE  . LYS B 144 ? 0.2128 0.1298 0.1850 0.0027  -0.0157 -0.0160 144 LYS B CE  
9438  N NZ  . LYS B 144 ? 0.2480 0.1947 0.1900 0.0360  -0.0136 -0.0025 144 LYS B NZ  
9452  N N   . VAL B 145 ? 0.1544 0.1709 0.1616 -0.0262 -0.0280 -0.0067 145 VAL B N   
9453  C CA  . VAL B 145 ? 0.1617 0.1878 0.1647 -0.0272 0.0016  -0.0135 145 VAL B CA  
9454  C C   . VAL B 145 ? 0.1590 0.1566 0.1637 -0.0110 -0.0197 0.0153  145 VAL B C   
9455  O O   . VAL B 145 ? 0.1961 0.1850 0.1517 -0.0183 -0.0213 0.0111  145 VAL B O   
9456  C CB  . VAL B 145 ? 0.1400 0.1938 0.1747 -0.0296 -0.0212 -0.0299 145 VAL B CB  
9457  C CG1 . VAL B 145 ? 0.1613 0.2239 0.1974 -0.0275 -0.0213 -0.0333 145 VAL B CG1 
9458  C CG2 . VAL B 145 ? 0.1666 0.1762 0.1734 0.0150  -0.0114 -0.0139 145 VAL B CG2 
9468  N N   . ILE B 146 ? 0.1657 0.1623 0.1618 -0.0031 0.0013  -0.0120 146 ILE B N   
9469  C CA  . ILE B 146 ? 0.1526 0.1638 0.1680 -0.0182 0.0009  0.0049  146 ILE B CA  
9470  C C   . ILE B 146 ? 0.1738 0.1627 0.1643 -0.0040 -0.0325 0.0011  146 ILE B C   
9471  O O   . ILE B 146 ? 0.1680 0.1881 0.1793 -0.0189 -0.0337 0.0087  146 ILE B O   
9472  C CB  . ILE B 146 ? 0.1651 0.1336 0.1779 -0.0006 -0.0040 0.0186  146 ILE B CB  
9473  C CG1 . ILE B 146 ? 0.1556 0.1392 0.1694 -0.0117 -0.0144 -0.0127 146 ILE B CG1 
9474  C CG2 . ILE B 146 ? 0.2083 0.1970 0.1810 0.0190  -0.0101 0.0140  146 ILE B CG2 
9475  C CD1 . ILE B 146 ? 0.1917 0.1868 0.1760 0.0011  -0.0297 -0.0417 146 ILE B CD1 
9487  N N   . ALA B 147 ? 0.1603 0.1936 0.1574 -0.0109 -0.0015 0.0087  147 ALA B N   
9488  C CA  . ALA B 147 ? 0.1424 0.1939 0.1598 -0.0049 0.0252  -0.0159 147 ALA B CA  
9489  C C   . ALA B 147 ? 0.1688 0.1906 0.1981 -0.0048 0.0110  -0.0166 147 ALA B C   
9490  O O   . ALA B 147 ? 0.1861 0.1544 0.2145 -0.0241 0.0135  0.0236  147 ALA B O   
9491  C CB  . ALA B 147 ? 0.1482 0.1592 0.1476 -0.0308 0.0356  -0.0155 147 ALA B CB  
9497  N N   . ARG B 148 ? 0.1751 0.2025 0.2142 -0.0252 -0.0013 -0.0442 148 ARG B N   
9498  C CA  . ARG B 148 ? 0.1715 0.2000 0.1934 -0.0036 0.0086  -0.0221 148 ARG B CA  
9499  C C   . ARG B 148 ? 0.1758 0.1895 0.1898 0.0084  0.0231  -0.0145 148 ARG B C   
9500  O O   . ARG B 148 ? 0.1695 0.2090 0.1742 -0.0200 0.0180  -0.0290 148 ARG B O   
9501  C CB  . ARG B 148 ? 0.2293 0.1964 0.1790 -0.0225 -0.0129 -0.0449 148 ARG B CB  
9502  C CG  . ARG B 148 ? 0.2715 0.2151 0.1798 -0.0661 -0.0120 -0.0391 148 ARG B CG  
9503  C CD  . ARG B 148 ? 0.3130 0.2056 0.1680 -0.0983 -0.0193 -0.0003 148 ARG B CD  
9504  N NE  . ARG B 148 ? 0.2378 0.1882 0.1650 -0.0462 -0.0449 -0.0046 148 ARG B NE  
9505  C CZ  . ARG B 148 ? 0.2139 0.1826 0.1632 -0.0181 -0.0421 0.0023  148 ARG B CZ  
9506  N NH1 . ARG B 148 ? 0.2187 0.2054 0.1543 0.0075  -0.0019 -0.0237 148 ARG B NH1 
9507  N NH2 . ARG B 148 ? 0.2266 0.1802 0.1693 -0.0266 -0.0103 -0.0019 148 ARG B NH2 
9521  N N   . GLN B 149 ? 0.1731 0.1927 0.1905 -0.0024 0.0214  -0.0026 149 GLN B N   
9522  C CA  . GLN B 149 ? 0.1924 0.1817 0.1845 -0.0369 0.0190  -0.0245 149 GLN B CA  
9523  C C   . GLN B 149 ? 0.1982 0.1731 0.1794 -0.0097 0.0049  -0.0052 149 GLN B C   
9524  O O   . GLN B 149 ? 0.1691 0.2336 0.1796 -0.0301 -0.0004 -0.0472 149 GLN B O   
9525  C CB  . GLN B 149 ? 0.1750 0.2174 0.2015 -0.0229 0.0129  -0.0362 149 GLN B CB  
9526  C CG  . GLN B 149 ? 0.2413 0.1864 0.2195 -0.0672 0.0140  -0.0729 149 GLN B CG  
9527  C CD  . GLN B 149 ? 0.4624 0.2595 0.2762 -0.0538 0.0144  -0.0638 149 GLN B CD  
9528  O OE1 . GLN B 149 ? 0.5889 0.3395 0.3073 -0.0322 0.0175  -0.0391 149 GLN B OE1 
9529  N NE2 . GLN B 149 ? 0.5330 0.3273 0.3044 0.0254  0.0357  -0.0577 149 GLN B NE2 
9538  N N   . ARG B 150 ? 0.2043 0.1406 0.1857 -0.0133 -0.0222 -0.0094 150 ARG B N   
9539  C CA  . ARG B 150 ? 0.1980 0.1563 0.1949 -0.0344 0.0003  0.0094  150 ARG B CA  
9540  C C   . ARG B 150 ? 0.1731 0.2434 0.1686 -0.0566 0.0154  -0.0015 150 ARG B C   
9541  O O   . ARG B 150 ? 0.1673 0.2781 0.1693 -0.0660 -0.0044 -0.0246 150 ARG B O   
9542  C CB  . ARG B 150 ? 0.1782 0.2191 0.2478 -0.0237 0.0062  0.0004  150 ARG B CB  
9543  C CG  . ARG B 150 ? 0.1808 0.2317 0.3026 -0.0214 0.0371  -0.0126 150 ARG B CG  
9544  C CD  . ARG B 150 ? 0.2046 0.2356 0.3192 -0.0323 -0.0239 -0.0336 150 ARG B CD  
9545  N NE  . ARG B 150 ? 0.2055 0.2060 0.3237 -0.0289 -0.0657 -0.0351 150 ARG B NE  
9546  C CZ  . ARG B 150 ? 0.2476 0.2043 0.3407 0.0126  -0.0783 -0.0198 150 ARG B CZ  
9547  N NH1 . ARG B 150 ? 0.2666 0.2025 0.3673 -0.0383 -0.0928 0.0088  150 ARG B NH1 
9548  N NH2 . ARG B 150 ? 0.2348 0.1780 0.3322 0.0058  -0.0773 -0.0338 150 ARG B NH2 
9562  N N   . GLY B 151 ? 0.1893 0.2101 0.1625 -0.0358 0.0179  -0.0294 151 GLY B N   
9563  C CA  . GLY B 151 ? 0.1851 0.2089 0.1679 -0.0461 0.0141  -0.0218 151 GLY B CA  
9564  C C   . GLY B 151 ? 0.1916 0.1452 0.1620 -0.0149 0.0111  -0.0078 151 GLY B C   
9565  O O   . GLY B 151 ? 0.1905 0.1852 0.1619 -0.0428 -0.0058 0.0152  151 GLY B O   
9569  N N   . TYR B 152 ? 0.1590 0.1511 0.1613 -0.0176 0.0122  -0.0021 152 TYR B N   
9570  C CA  . TYR B 152 ? 0.1371 0.1787 0.1662 -0.0252 0.0211  0.0059  152 TYR B CA  
9571  C C   . TYR B 152 ? 0.1595 0.1672 0.1586 -0.0455 0.0220  0.0052  152 TYR B C   
9572  O O   . TYR B 152 ? 0.1721 0.1758 0.1530 -0.0245 0.0148  -0.0082 152 TYR B O   
9573  C CB  . TYR B 152 ? 0.1570 0.1620 0.1800 -0.0044 0.0299  -0.0029 152 TYR B CB  
9574  C CG  . TYR B 152 ? 0.1310 0.1841 0.1723 0.0032  0.0087  -0.0266 152 TYR B CG  
9575  C CD1 . TYR B 152 ? 0.1529 0.2219 0.1705 -0.0131 0.0085  -0.0386 152 TYR B CD1 
9576  C CD2 . TYR B 152 ? 0.1506 0.2072 0.1835 0.0029  0.0048  -0.0311 152 TYR B CD2 
9577  C CE1 . TYR B 152 ? 0.1999 0.2290 0.1588 -0.0014 0.0131  0.0003  152 TYR B CE1 
9578  C CE2 . TYR B 152 ? 0.2005 0.2129 0.1707 0.0063  0.0101  -0.0352 152 TYR B CE2 
9579  C CZ  . TYR B 152 ? 0.1846 0.2276 0.1612 -0.0034 0.0029  -0.0032 152 TYR B CZ  
9580  O OH  . TYR B 152 ? 0.2236 0.2096 0.1588 0.0036  0.0277  -0.0001 152 TYR B OH  
9590  N N   . HIS B 153 ? 0.1683 0.1570 0.1573 -0.0232 0.0123  0.0200  153 HIS B N   
9591  C CA  . HIS B 153 ? 0.1851 0.1258 0.1606 -0.0188 0.0022  -0.0052 153 HIS B CA  
9592  C C   . HIS B 153 ? 0.1521 0.1552 0.1569 -0.0400 0.0013  -0.0032 153 HIS B C   
9593  O O   . HIS B 153 ? 0.1510 0.1783 0.1607 -0.0287 -0.0028 -0.0106 153 HIS B O   
9594  C CB  . HIS B 153 ? 0.1789 0.1148 0.1578 -0.0098 0.0303  0.0124  153 HIS B CB  
9595  C CG  . HIS B 153 ? 0.1789 0.1672 0.1419 -0.0300 0.0154  0.0108  153 HIS B CG  
9596  N ND1 . HIS B 153 ? 0.1620 0.1587 0.1491 -0.0537 0.0313  0.0106  153 HIS B ND1 
9597  C CD2 . HIS B 153 ? 0.1765 0.2175 0.1536 -0.0261 -0.0184 0.0247  153 HIS B CD2 
9598  C CE1 . HIS B 153 ? 0.1674 0.1946 0.1440 -0.0028 0.0302  0.0102  153 HIS B CE1 
9599  N NE2 . HIS B 153 ? 0.1504 0.2114 0.1433 -0.0357 -0.0059 0.0109  153 HIS B NE2 
9607  N N   . GLY B 154 ? 0.1513 0.1755 0.1571 0.0173  0.0033  -0.0033 154 GLY B N   
9608  C CA  . GLY B 154 ? 0.1658 0.2092 0.1535 0.0159  -0.0002 -0.0078 154 GLY B CA  
9609  C C   . GLY B 154 ? 0.1262 0.1941 0.1513 -0.0076 0.0107  -0.0258 154 GLY B C   
9610  O O   . GLY B 154 ? 0.1507 0.2037 0.1549 -0.0217 -0.0003 -0.0084 154 GLY B O   
9614  N N   . SER B 155 ? 0.1389 0.2025 0.1399 -0.0193 0.0229  -0.0017 155 SER B N   
9615  C CA  . SER B 155 ? 0.1723 0.1553 0.1444 -0.0277 -0.0100 -0.0002 155 SER B CA  
9616  C C   . SER B 155 ? 0.1588 0.1526 0.1502 -0.0521 -0.0233 -0.0139 155 SER B C   
9617  O O   . SER B 155 ? 0.1893 0.1332 0.1561 -0.0110 -0.0236 -0.0043 155 SER B O   
9618  C CB  . SER B 155 ? 0.1561 0.1657 0.1547 -0.0612 -0.0063 0.0039  155 SER B CB  
9619  O OG  . SER B 155 ? 0.1560 0.1900 0.1597 -0.0328 -0.0307 0.0018  155 SER B OG  
9625  N N   . GLY B 156 ? 0.1715 0.1592 0.1472 -0.0434 -0.0166 -0.0015 156 GLY B N   
9626  C CA  . GLY B 156 ? 0.1821 0.1672 0.1456 -0.0469 0.0041  -0.0136 156 GLY B CA  
9627  C C   . GLY B 156 ? 0.1488 0.1817 0.1443 -0.0333 0.0049  -0.0221 156 GLY B C   
9628  O O   . GLY B 156 ? 0.1590 0.2147 0.1589 -0.0086 0.0011  -0.0286 156 GLY B O   
9632  N N   . ILE B 157 ? 0.1597 0.1614 0.1464 -0.0176 -0.0104 -0.0173 157 ILE B N   
9633  C CA  . ILE B 157 ? 0.1392 0.1378 0.1496 -0.0130 0.0000  -0.0229 157 ILE B CA  
9634  C C   . ILE B 157 ? 0.1270 0.1540 0.1458 -0.0154 -0.0057 -0.0127 157 ILE B C   
9635  O O   . ILE B 157 ? 0.1569 0.1636 0.1484 -0.0002 -0.0058 -0.0105 157 ILE B O   
9636  C CB  . ILE B 157 ? 0.1222 0.1288 0.1516 -0.0308 0.0079  0.0081  157 ILE B CB  
9637  C CG1 . ILE B 157 ? 0.1426 0.1408 0.1610 -0.0378 -0.0003 -0.0023 157 ILE B CG1 
9638  C CG2 . ILE B 157 ? 0.1064 0.1696 0.1543 -0.0139 0.0129  0.0108  157 ILE B CG2 
9639  C CD1 . ILE B 157 ? 0.1662 0.1721 0.1616 -0.0778 -0.0137 -0.0149 157 ILE B CD1 
9651  N N   . ALA B 158 ? 0.1369 0.1418 0.1387 -0.0143 -0.0141 -0.0020 158 ALA B N   
9652  C CA  . ALA B 158 ? 0.1612 0.1856 0.1420 0.0064  -0.0087 0.0075  158 ALA B CA  
9653  C C   . ALA B 158 ? 0.1606 0.1498 0.1390 -0.0055 -0.0045 -0.0075 158 ALA B C   
9654  O O   . ALA B 158 ? 0.1671 0.1329 0.1389 -0.0286 0.0079  -0.0005 158 ALA B O   
9655  C CB  . ALA B 158 ? 0.1666 0.2077 0.1307 -0.0373 -0.0119 -0.0073 158 ALA B CB  
9661  N N   . SER B 159 ? 0.1881 0.1271 0.1287 -0.0269 0.0049  0.0068  159 SER B N   
9662  C CA  . SER B 159 ? 0.1913 0.1154 0.1337 -0.0363 -0.0040 0.0052  159 SER B CA  
9663  C C   . SER B 159 ? 0.1964 0.1681 0.1474 -0.0159 -0.0084 0.0184  159 SER B C   
9664  O O   . SER B 159 ? 0.1775 0.1741 0.1490 -0.0244 -0.0023 0.0026  159 SER B O   
9665  C CB  . SER B 159 ? 0.1591 0.1465 0.1398 -0.0287 0.0097  0.0201  159 SER B CB  
9666  O OG  . SER B 159 ? 0.1983 0.1977 0.1491 -0.0558 -0.0030 0.0177  159 SER B OG  
9672  N N   . GLY B 160 ? 0.1716 0.1373 0.1487 -0.0036 -0.0074 0.0058  160 GLY B N   
9673  C CA  . GLY B 160 ? 0.1470 0.1688 0.1534 -0.0251 -0.0259 -0.0136 160 GLY B CA  
9674  C C   . GLY B 160 ? 0.1454 0.1600 0.1464 -0.0009 0.0036  0.0079  160 GLY B C   
9675  O O   . GLY B 160 ? 0.1496 0.1762 0.1671 -0.0197 0.0077  -0.0140 160 GLY B O   
9679  N N   . SER B 161 ? 0.1530 0.2081 0.1429 0.0100  0.0177  0.0011  161 SER B N   
9680  C CA  . SER B 161 ? 0.1356 0.1250 0.1461 0.0096  0.0010  0.0093  161 SER B CA  
9681  C C   . SER B 161 ? 0.1276 0.1359 0.1531 -0.0147 0.0149  -0.0105 161 SER B C   
9682  O O   . SER B 161 ? 0.1769 0.1797 0.1550 -0.0226 0.0154  -0.0171 161 SER B O   
9683  C CB  . SER B 161 ? 0.1856 0.1405 0.1446 -0.0601 -0.0049 -0.0020 161 SER B CB  
9684  O OG  . SER B 161 ? 0.1982 0.1801 0.1610 -0.0224 0.0119  0.0210  161 SER B OG  
9690  N N   . LEU B 162 ? 0.1472 0.1295 0.1517 -0.0148 0.0164  0.0196  162 LEU B N   
9691  C CA  . LEU B 162 ? 0.1550 0.1734 0.1443 -0.0067 0.0112  0.0307  162 LEU B CA  
9692  C C   . LEU B 162 ? 0.1457 0.2001 0.1541 -0.0242 -0.0115 0.0099  162 LEU B C   
9693  O O   . LEU B 162 ? 0.1781 0.1595 0.1685 -0.0106 -0.0002 -0.0333 162 LEU B O   
9694  C CB  . LEU B 162 ? 0.1747 0.1518 0.1469 -0.0503 0.0086  -0.0032 162 LEU B CB  
9695  C CG  . LEU B 162 ? 0.1755 0.1827 0.1536 -0.0128 0.0073  -0.0023 162 LEU B CG  
9696  C CD1 . LEU B 162 ? 0.1641 0.2230 0.1595 -0.0300 -0.0054 0.0026  162 LEU B CD1 
9697  C CD2 . LEU B 162 ? 0.1556 0.1766 0.1435 -0.0336 0.0193  -0.0020 162 LEU B CD2 
9709  N N   . THR B 163 ? 0.1448 0.1862 0.1490 -0.0501 0.0098  0.0029  163 THR B N   
9710  C CA  . THR B 163 ? 0.1397 0.1443 0.1506 -0.0506 -0.0003 -0.0065 163 THR B CA  
9711  C C   . THR B 163 ? 0.1544 0.1439 0.1456 -0.0328 0.0025  -0.0247 163 THR B C   
9712  O O   . THR B 163 ? 0.1691 0.1776 0.1456 -0.0475 0.0137  -0.0159 163 THR B O   
9713  C CB  . THR B 163 ? 0.1570 0.1787 0.1595 -0.0544 -0.0010 -0.0086 163 THR B CB  
9714  O OG1 . THR B 163 ? 0.1873 0.1657 0.1686 -0.0406 -0.0018 -0.0085 163 THR B OG1 
9715  C CG2 . THR B 163 ? 0.1471 0.1958 0.1643 -0.0626 -0.0045 -0.0221 163 THR B CG2 
9723  N N   . GLY B 164 ? 0.1594 0.1626 0.1530 0.0154  0.0184  -0.0204 164 GLY B N   
9724  C CA  . GLY B 164 ? 0.1572 0.1507 0.1668 0.0206  0.0210  -0.0253 164 GLY B CA  
9725  C C   . GLY B 164 ? 0.1409 0.1705 0.1650 0.0275  0.0242  -0.0152 164 GLY B C   
9726  O O   . GLY B 164 ? 0.1508 0.2345 0.1568 0.0142  0.0127  -0.0285 164 GLY B O   
9730  N N   . LEU B 165 ? 0.1617 0.1915 0.1655 -0.0384 0.0189  -0.0145 165 LEU B N   
9731  C CA  . LEU B 165 ? 0.1657 0.1691 0.1685 -0.0123 0.0169  -0.0055 165 LEU B CA  
9732  C C   . LEU B 165 ? 0.1690 0.1861 0.1747 -0.0178 0.0047  -0.0206 165 LEU B C   
9733  O O   . LEU B 165 ? 0.1659 0.2319 0.1840 -0.0046 -0.0024 -0.0199 165 LEU B O   
9734  C CB  . LEU B 165 ? 0.1722 0.2153 0.1696 -0.0101 0.0106  -0.0299 165 LEU B CB  
9735  C CG  . LEU B 165 ? 0.1773 0.2150 0.1746 -0.0258 0.0232  -0.0211 165 LEU B CG  
9736  C CD1 . LEU B 165 ? 0.2435 0.2595 0.1991 0.0065  0.0316  -0.0203 165 LEU B CD1 
9737  C CD2 . LEU B 165 ? 0.2394 0.1840 0.1627 -0.0063 -0.0005 -0.0067 165 LEU B CD2 
9749  N N   . LYS B 166 ? 0.1860 0.1917 0.1937 -0.0019 0.0307  0.0070  166 LYS B N   
9750  C CA  . LYS B 166 ? 0.2004 0.2011 0.2051 0.0302  0.0479  0.0135  166 LYS B CA  
9751  C C   . LYS B 166 ? 0.1538 0.1942 0.1901 -0.0104 0.0309  0.0121  166 LYS B C   
9752  O O   . LYS B 166 ? 0.1542 0.1996 0.1857 -0.0317 0.0296  0.0006  166 LYS B O   
9753  C CB  . LYS B 166 ? 0.2943 0.2415 0.2354 0.1288  0.0827  0.0232  166 LYS B CB  
9754  C CG  . LYS B 166 ? 0.4374 0.3955 0.3023 0.1498  0.0673  0.0019  166 LYS B CG  
9755  C CD  . LYS B 166 ? 0.5575 0.5286 0.3524 0.1855  0.0790  -0.0124 166 LYS B CD  
9756  C CE  . LYS B 166 ? 0.7266 0.6351 0.4041 0.1535  0.0431  -0.0205 166 LYS B CE  
9757  N NZ  . LYS B 166 ? 0.8152 0.6882 0.4340 0.1477  0.0325  -0.0380 166 LYS B NZ  
9771  N N   . ALA B 167 ? 0.1691 0.2181 0.1865 0.0014  0.0089  0.0033  167 ALA B N   
9772  C CA  . ALA B 167 ? 0.1731 0.2353 0.1899 -0.0126 -0.0007 0.0003  167 ALA B CA  
9773  C C   . ALA B 167 ? 0.1720 0.2363 0.1792 -0.0155 0.0037  -0.0033 167 ALA B C   
9774  O O   . ALA B 167 ? 0.1853 0.2180 0.1852 -0.0182 -0.0009 -0.0211 167 ALA B O   
9775  C CB  . ALA B 167 ? 0.1676 0.2591 0.2069 -0.0373 -0.0073 -0.0356 167 ALA B CB  
9781  N N   . PHE B 168 ? 0.1464 0.2067 0.1597 -0.0200 0.0036  -0.0155 168 PHE B N   
9782  C CA  . PHE B 168 ? 0.1690 0.1949 0.1578 -0.0090 -0.0016 -0.0170 168 PHE B CA  
9783  C C   . PHE B 168 ? 0.1423 0.1796 0.1602 -0.0292 -0.0045 0.0074  168 PHE B C   
9784  O O   . PHE B 168 ? 0.1523 0.2056 0.1772 -0.0131 0.0024  0.0065  168 PHE B O   
9785  C CB  . PHE B 168 ? 0.1642 0.1959 0.1723 -0.0154 0.0049  -0.0021 168 PHE B CB  
9786  C CG  . PHE B 168 ? 0.1818 0.1871 0.1849 -0.0403 0.0016  0.0177  168 PHE B CG  
9787  C CD1 . PHE B 168 ? 0.2281 0.2003 0.1852 -0.0091 0.0209  0.0053  168 PHE B CD1 
9788  C CD2 . PHE B 168 ? 0.1808 0.2455 0.1988 -0.0243 0.0068  0.0101  168 PHE B CD2 
9789  C CE1 . PHE B 168 ? 0.2191 0.1978 0.1873 -0.0468 0.0205  0.0205  168 PHE B CE1 
9790  C CE2 . PHE B 168 ? 0.2242 0.2241 0.2034 -0.0356 0.0103  0.0269  168 PHE B CE2 
9791  C CZ  . PHE B 168 ? 0.2212 0.2157 0.1988 -0.0528 0.0043  0.0226  168 PHE B CZ  
9801  N N   . HIS B 169 ? 0.1471 0.2017 0.1735 0.0047  0.0136  -0.0209 169 HIS B N   
9802  C CA  . HIS B 169 ? 0.1590 0.2091 0.1737 0.0011  0.0269  0.0153  169 HIS B CA  
9803  C C   . HIS B 169 ? 0.1732 0.2430 0.1763 -0.0036 0.0126  0.0163  169 HIS B C   
9804  O O   . HIS B 169 ? 0.1849 0.2151 0.1896 -0.0017 0.0299  -0.0019 169 HIS B O   
9805  C CB  . HIS B 169 ? 0.1502 0.2064 0.1707 -0.0024 0.0301  -0.0058 169 HIS B CB  
9806  C CG  . HIS B 169 ? 0.2039 0.1751 0.1648 0.0173  0.0149  0.0010  169 HIS B CG  
9807  N ND1 . HIS B 169 ? 0.2362 0.2016 0.1729 0.0077  0.0028  -0.0084 169 HIS B ND1 
9808  C CD2 . HIS B 169 ? 0.1382 0.1981 0.1695 -0.0165 0.0050  -0.0122 169 HIS B CD2 
9809  C CE1 . HIS B 169 ? 0.2487 0.2245 0.1807 0.0272  -0.0173 -0.0045 169 HIS B CE1 
9810  N NE2 . HIS B 169 ? 0.2190 0.2097 0.1750 -0.0017 0.0106  -0.0100 169 HIS B NE2 
9819  N N   . ASP B 170 ? 0.1628 0.2597 0.1802 -0.0184 -0.0105 0.0042  170 ASP B N   
9820  C CA  . ASP B 170 ? 0.1593 0.2391 0.1887 -0.0064 -0.0063 0.0048  170 ASP B CA  
9821  C C   . ASP B 170 ? 0.1757 0.2321 0.1902 0.0103  0.0054  0.0205  170 ASP B C   
9822  O O   . ASP B 170 ? 0.1969 0.2379 0.1978 0.0159  0.0136  0.0324  170 ASP B O   
9823  C CB  . ASP B 170 ? 0.2039 0.2619 0.2048 0.0421  0.0121  0.0076  170 ASP B CB  
9824  C CG  . ASP B 170 ? 0.2159 0.3055 0.2190 0.0549  0.0083  0.0117  170 ASP B CG  
9825  O OD1 . ASP B 170 ? 0.2834 0.3046 0.2213 0.0447  0.0060  0.0118  170 ASP B OD1 
9826  O OD2 . ASP B 170 ? 0.2533 0.3782 0.2264 0.0578  0.0371  0.0048  170 ASP B OD2 
9831  N N   . HIS B 171 ? 0.2084 0.1749 0.1942 -0.0160 -0.0064 0.0062  171 HIS B N   
9832  C CA  . HIS B 171 ? 0.1743 0.1875 0.1891 -0.0332 -0.0066 -0.0050 171 HIS B CA  
9833  C C   . HIS B 171 ? 0.2120 0.1665 0.1781 -0.0084 -0.0060 -0.0097 171 HIS B C   
9834  O O   . HIS B 171 ? 0.2172 0.2203 0.1640 -0.0047 -0.0033 -0.0132 171 HIS B O   
9835  C CB  . HIS B 171 ? 0.1617 0.2326 0.2150 -0.0136 -0.0198 -0.0200 171 HIS B CB  
9836  C CG  . HIS B 171 ? 0.1957 0.3043 0.2504 0.0091  -0.0317 -0.0070 171 HIS B CG  
9837  N ND1 . HIS B 171 ? 0.2054 0.3285 0.2588 0.0139  -0.0312 -0.0174 171 HIS B ND1 
9838  C CD2 . HIS B 171 ? 0.1837 0.3075 0.2704 0.0131  -0.0243 -0.0015 171 HIS B CD2 
9839  C CE1 . HIS B 171 ? 0.2530 0.3564 0.2679 -0.0220 -0.0323 -0.0122 171 HIS B CE1 
9840  N NE2 . HIS B 171 ? 0.2131 0.3222 0.2662 -0.0204 -0.0410 0.0148  171 HIS B NE2 
9848  N N   . PHE B 172 ? 0.2077 0.1650 0.1797 -0.0174 0.0138  -0.0123 172 PHE B N   
9849  C CA  . PHE B 172 ? 0.1873 0.1746 0.1822 -0.0094 0.0263  0.0236  172 PHE B CA  
9850  C C   . PHE B 172 ? 0.1855 0.1699 0.1957 -0.0234 0.0238  0.0197  172 PHE B C   
9851  O O   . PHE B 172 ? 0.1626 0.2087 0.2057 -0.0151 0.0064  0.0096  172 PHE B O   
9852  C CB  . PHE B 172 ? 0.1928 0.1155 0.1771 0.0035  0.0356  0.0053  172 PHE B CB  
9853  C CG  . PHE B 172 ? 0.1949 0.1489 0.1726 -0.0480 0.0188  0.0020  172 PHE B CG  
9854  C CD1 . PHE B 172 ? 0.1973 0.1872 0.1692 -0.0293 -0.0071 -0.0146 172 PHE B CD1 
9855  C CD2 . PHE B 172 ? 0.1772 0.1628 0.1750 -0.0554 0.0060  0.0131  172 PHE B CD2 
9856  C CE1 . PHE B 172 ? 0.2078 0.1452 0.1768 -0.0524 -0.0024 -0.0029 172 PHE B CE1 
9857  C CE2 . PHE B 172 ? 0.1396 0.1789 0.1754 -0.0476 -0.0154 -0.0033 172 PHE B CE2 
9858  C CZ  . PHE B 172 ? 0.2010 0.1249 0.1747 -0.0223 -0.0123 0.0061  172 PHE B CZ  
9868  N N   . ASP B 173 ? 0.1951 0.1542 0.2090 -0.0316 0.0194  0.0036  173 ASP B N   
9869  C CA  . ASP B 173 ? 0.1982 0.1793 0.2060 -0.0311 0.0020  0.0079  173 ASP B CA  
9870  C C   . ASP B 173 ? 0.1721 0.1935 0.2145 -0.0057 0.0061  0.0125  173 ASP B C   
9871  O O   . ASP B 173 ? 0.2522 0.2676 0.2325 -0.0775 -0.0293 0.0569  173 ASP B O   
9872  C CB  . ASP B 173 ? 0.2260 0.1607 0.2112 -0.0433 0.0008  0.0087  173 ASP B CB  
9873  C CG  . ASP B 173 ? 0.1974 0.2597 0.2131 -0.0379 0.0231  0.0426  173 ASP B CG  
9874  O OD1 . ASP B 173 ? 0.2036 0.2671 0.2183 -0.0123 0.0031  0.0503  173 ASP B OD1 
9875  O OD2 . ASP B 173 ? 0.2352 0.2840 0.2175 -0.0005 0.0335  0.0563  173 ASP B OD2 
9880  N N   . LEU B 174 ? 0.1998 0.1815 0.1908 -0.0091 0.0207  0.0018  174 LEU B N   
9881  C CA  . LEU B 174 ? 0.1728 0.1827 0.1888 -0.0139 0.0178  -0.0062 174 LEU B CA  
9882  C C   . LEU B 174 ? 0.1673 0.1897 0.1883 -0.0084 0.0263  -0.0104 174 LEU B C   
9883  O O   . LEU B 174 ? 0.2007 0.2248 0.1972 -0.0142 0.0090  -0.0011 174 LEU B O   
9884  C CB  . LEU B 174 ? 0.1664 0.1906 0.1910 -0.0212 0.0000  -0.0042 174 LEU B CB  
9885  C CG  . LEU B 174 ? 0.1870 0.1605 0.1835 -0.0315 0.0148  -0.0003 174 LEU B CG  
9886  C CD1 . LEU B 174 ? 0.1873 0.1657 0.1955 0.0050  0.0420  -0.0429 174 LEU B CD1 
9887  C CD2 . LEU B 174 ? 0.1921 0.1926 0.1765 -0.0098 0.0181  -0.0136 174 LEU B CD2 
9899  N N   . PRO B 175 ? 0.1815 0.2087 0.1817 0.0107  0.0331  0.0141  175 PRO B N   
9900  C CA  . PRO B 175 ? 0.1884 0.2149 0.1775 -0.0148 0.0070  0.0101  175 PRO B CA  
9901  C C   . PRO B 175 ? 0.2067 0.2075 0.1842 0.0138  -0.0038 0.0132  175 PRO B C   
9902  O O   . PRO B 175 ? 0.2278 0.1907 0.1853 0.0004  0.0280  0.0302  175 PRO B O   
9903  C CB  . PRO B 175 ? 0.2308 0.2151 0.1862 -0.0059 0.0063  0.0186  175 PRO B CB  
9904  C CG  . PRO B 175 ? 0.2149 0.2078 0.1920 -0.0110 0.0028  0.0114  175 PRO B CG  
9905  C CD  . PRO B 175 ? 0.2179 0.2009 0.1756 0.0158  0.0084  0.0295  175 PRO B CD  
9913  N N   . ILE B 176 ? 0.1932 0.1816 0.1796 -0.0227 -0.0136 -0.0020 176 ILE B N   
9914  C CA  . ILE B 176 ? 0.1791 0.1728 0.1891 -0.0115 0.0049  -0.0090 176 ILE B CA  
9915  C C   . ILE B 176 ? 0.1789 0.1816 0.1765 0.0046  0.0334  -0.0148 176 ILE B C   
9916  O O   . ILE B 176 ? 0.2031 0.2039 0.1691 -0.0245 0.0514  -0.0093 176 ILE B O   
9917  C CB  . ILE B 176 ? 0.1785 0.1311 0.1981 -0.0355 0.0178  -0.0103 176 ILE B CB  
9918  C CG1 . ILE B 176 ? 0.1906 0.2043 0.2201 -0.0786 0.0626  0.0012  176 ILE B CG1 
9919  C CG2 . ILE B 176 ? 0.2331 0.1559 0.1878 -0.0412 0.0007  -0.0308 176 ILE B CG2 
9920  C CD1 . ILE B 176 ? 0.1918 0.2283 0.2394 -0.0573 0.0245  0.0019  176 ILE B CD1 
9932  N N   . GLU B 177 ? 0.2356 0.1849 0.1851 -0.0573 0.0050  -0.0185 177 GLU B N   
9933  C CA  . GLU B 177 ? 0.2684 0.1732 0.1994 -0.0726 -0.0210 -0.0229 177 GLU B CA  
9934  C C   . GLU B 177 ? 0.2381 0.1834 0.2064 -0.0553 -0.0052 -0.0033 177 GLU B C   
9935  O O   . GLU B 177 ? 0.2450 0.1658 0.2265 -0.0709 0.0098  0.0019  177 GLU B O   
9936  C CB  . GLU B 177 ? 0.3801 0.2073 0.2256 -0.1003 -0.0384 -0.0311 177 GLU B CB  
9937  C CG  . GLU B 177 ? 0.5882 0.3397 0.2778 -0.0662 -0.0509 -0.0369 177 GLU B CG  
9938  C CD  . GLU B 177 ? 0.7842 0.5075 0.3381 -0.0346 -0.0703 -0.0148 177 GLU B CD  
9939  O OE1 . GLU B 177 ? 0.8748 0.5294 0.3596 -0.1023 -0.0679 -0.0259 177 GLU B OE1 
9940  O OE2 . GLU B 177 ? 0.8493 0.6121 0.3740 0.0139  -0.0719 -0.0082 177 GLU B OE2 
9947  N N   . GLY B 178 ? 0.1860 0.1780 0.1821 -0.0293 -0.0161 0.0020  178 GLY B N   
9948  C CA  . GLY B 178 ? 0.1908 0.2417 0.1817 -0.0141 -0.0199 0.0189  178 GLY B CA  
9949  C C   . GLY B 178 ? 0.1674 0.1771 0.1694 -0.0057 -0.0182 0.0013  178 GLY B C   
9950  O O   . GLY B 178 ? 0.2238 0.2165 0.1753 -0.0461 -0.0453 0.0298  178 GLY B O   
9954  N N   . ILE B 179 ? 0.1397 0.1668 0.1612 -0.0013 -0.0174 0.0337  179 ILE B N   
9955  C CA  . ILE B 179 ? 0.1466 0.1865 0.1701 -0.0420 -0.0140 0.0339  179 ILE B CA  
9956  C C   . ILE B 179 ? 0.1583 0.1917 0.1761 -0.0052 -0.0122 0.0436  179 ILE B C   
9957  O O   . ILE B 179 ? 0.1889 0.2464 0.1978 0.0030  -0.0017 0.0364  179 ILE B O   
9958  C CB  . ILE B 179 ? 0.1637 0.2028 0.1838 -0.0226 -0.0250 -0.0044 179 ILE B CB  
9959  C CG1 . ILE B 179 ? 0.2037 0.1794 0.1985 -0.0232 -0.0089 -0.0376 179 ILE B CG1 
9960  C CG2 . ILE B 179 ? 0.1716 0.1919 0.1724 -0.0188 -0.0189 0.0093  179 ILE B CG2 
9961  C CD1 . ILE B 179 ? 0.2630 0.1977 0.2022 -0.0361 -0.0264 0.0178  179 ILE B CD1 
9973  N N   . LEU B 180 ? 0.1721 0.1885 0.1730 0.0196  0.0166  0.0472  180 LEU B N   
9974  C CA  . LEU B 180 ? 0.1849 0.1872 0.1780 -0.0049 0.0230  -0.0008 180 LEU B CA  
9975  C C   . LEU B 180 ? 0.1703 0.1432 0.1711 0.0069  0.0313  0.0033  180 LEU B C   
9976  O O   . LEU B 180 ? 0.1890 0.1527 0.1780 0.0104  0.0191  0.0185  180 LEU B O   
9977  C CB  . LEU B 180 ? 0.2509 0.1931 0.1954 -0.0526 0.0087  -0.0329 180 LEU B CB  
9978  C CG  . LEU B 180 ? 0.2998 0.2450 0.2331 -0.1018 0.0063  -0.0293 180 LEU B CG  
9979  C CD1 . LEU B 180 ? 0.3582 0.2697 0.2488 -0.0961 0.0125  -0.0488 180 LEU B CD1 
9980  C CD2 . LEU B 180 ? 0.3199 0.2547 0.2784 -0.1318 0.0088  -0.0220 180 LEU B CD2 
9992  N N   . HIS B 181 ? 0.2010 0.1752 0.1461 -0.0208 0.0215  -0.0108 181 HIS B N   
9993  C CA  . HIS B 181 ? 0.1918 0.1463 0.1400 0.0026  0.0022  -0.0170 181 HIS B CA  
9994  C C   . HIS B 181 ? 0.1949 0.1756 0.1621 -0.0124 0.0012  -0.0074 181 HIS B C   
9995  O O   . HIS B 181 ? 0.1943 0.2163 0.1637 -0.0142 -0.0119 0.0082  181 HIS B O   
9996  C CB  . HIS B 181 ? 0.1817 0.1725 0.1501 -0.0205 -0.0033 -0.0186 181 HIS B CB  
9997  C CG  . HIS B 181 ? 0.1629 0.1618 0.1630 -0.0083 0.0140  -0.0185 181 HIS B CG  
9998  N ND1 . HIS B 181 ? 0.1937 0.1815 0.1569 -0.0242 0.0300  -0.0125 181 HIS B ND1 
9999  C CD2 . HIS B 181 ? 0.1610 0.1601 0.1660 0.0014  0.0138  -0.0260 181 HIS B CD2 
10000 C CE1 . HIS B 181 ? 0.1915 0.1808 0.1822 -0.0117 0.0034  -0.0123 181 HIS B CE1 
10001 N NE2 . HIS B 181 ? 0.1659 0.1852 0.1788 0.0051  0.0209  -0.0294 181 HIS B NE2 
10009 N N   . THR B 182 ? 0.1866 0.2265 0.1617 -0.0241 -0.0184 -0.0132 182 THR B N   
10010 C CA  . THR B 182 ? 0.1826 0.1950 0.1522 -0.0240 0.0091  -0.0298 182 THR B CA  
10011 C C   . THR B 182 ? 0.1558 0.2066 0.1612 0.0225  -0.0009 -0.0330 182 THR B C   
10012 O O   . THR B 182 ? 0.1559 0.2296 0.1638 -0.0093 -0.0154 -0.0185 182 THR B O   
10013 C CB  . THR B 182 ? 0.1980 0.1983 0.1702 -0.0140 0.0142  -0.0489 182 THR B CB  
10014 O OG1 . THR B 182 ? 0.1775 0.2496 0.1662 -0.0248 0.0197  -0.0407 182 THR B OG1 
10015 C CG2 . THR B 182 ? 0.2056 0.2021 0.1763 0.0213  -0.0144 -0.0364 182 THR B CG2 
10023 N N   . GLU B 183 ? 0.1695 0.2236 0.1649 0.0231  0.0062  -0.0320 183 GLU B N   
10024 C CA  . GLU B 183 ? 0.1631 0.2385 0.1798 -0.0072 0.0216  -0.0422 183 GLU B CA  
10025 C C   . GLU B 183 ? 0.1257 0.2636 0.1755 -0.0321 -0.0028 -0.0290 183 GLU B C   
10026 O O   . GLU B 183 ? 0.1636 0.2381 0.1771 -0.0313 -0.0024 -0.0239 183 GLU B O   
10027 C CB  . GLU B 183 ? 0.2603 0.2396 0.2153 -0.0046 0.0371  -0.0480 183 GLU B CB  
10028 C CG  . GLU B 183 ? 0.3640 0.3378 0.2519 0.0173  0.0343  -0.0454 183 GLU B CG  
10029 C CD  . GLU B 183 ? 0.4451 0.4187 0.2965 0.0778  0.0125  -0.0338 183 GLU B CD  
10030 O OE1 . GLU B 183 ? 0.3550 0.4602 0.3143 0.1246  0.0036  -0.0301 183 GLU B OE1 
10031 O OE2 . GLU B 183 ? 0.5363 0.4076 0.3212 0.0944  -0.0061 -0.0267 183 GLU B OE2 
10038 N N   . ALA B 184 ? 0.1610 0.2641 0.1682 -0.0338 0.0041  -0.0211 184 ALA B N   
10039 C CA  . ALA B 184 ? 0.1669 0.2479 0.1799 -0.0548 0.0083  -0.0242 184 ALA B CA  
10040 C C   . ALA B 184 ? 0.1705 0.2362 0.1759 -0.0198 -0.0101 -0.0540 184 ALA B C   
10041 O O   . ALA B 184 ? 0.2175 0.2231 0.1791 0.0058  0.0156  -0.0375 184 ALA B O   
10042 C CB  . ALA B 184 ? 0.1942 0.2436 0.1884 -0.0515 0.0194  -0.0132 184 ALA B CB  
10048 N N   . PRO B 185 ? 0.1972 0.2434 0.1737 -0.0056 -0.0028 -0.0519 185 PRO B N   
10049 C CA  . PRO B 185 ? 0.2091 0.2282 0.1845 -0.0279 0.0082  -0.0263 185 PRO B CA  
10050 C C   . PRO B 185 ? 0.1888 0.2104 0.1854 -0.0460 0.0214  -0.0183 185 PRO B C   
10051 O O   . PRO B 185 ? 0.2007 0.2036 0.2052 -0.0354 0.0397  -0.0009 185 PRO B O   
10052 C CB  . PRO B 185 ? 0.1972 0.2480 0.1889 -0.0330 0.0022  -0.0377 185 PRO B CB  
10053 C CG  . PRO B 185 ? 0.1870 0.2338 0.1854 -0.0045 -0.0026 -0.0248 185 PRO B CG  
10054 C CD  . PRO B 185 ? 0.1793 0.2452 0.1719 0.0300  0.0114  -0.0338 185 PRO B CD  
10062 N N   . TYR B 186 ? 0.2098 0.2501 0.1864 0.0055  0.0212  -0.0361 186 TYR B N   
10063 C CA  . TYR B 186 ? 0.1839 0.2699 0.1930 -0.0274 0.0273  -0.0134 186 TYR B CA  
10064 C C   . TYR B 186 ? 0.2012 0.2690 0.2003 -0.0392 0.0270  0.0079  186 TYR B C   
10065 O O   . TYR B 186 ? 0.1917 0.2961 0.2085 -0.0534 0.0250  -0.0156 186 TYR B O   
10066 C CB  . TYR B 186 ? 0.1783 0.2786 0.2035 -0.0328 0.0195  -0.0268 186 TYR B CB  
10067 C CG  . TYR B 186 ? 0.2219 0.2706 0.2115 -0.0564 0.0211  -0.0150 186 TYR B CG  
10068 C CD1 . TYR B 186 ? 0.2311 0.2968 0.2128 -0.0408 0.0270  -0.0445 186 TYR B CD1 
10069 C CD2 . TYR B 186 ? 0.2157 0.2484 0.2136 -0.0149 0.0202  -0.0153 186 TYR B CD2 
10070 C CE1 . TYR B 186 ? 0.2585 0.2862 0.2112 -0.0344 0.0291  -0.0296 186 TYR B CE1 
10071 C CE2 . TYR B 186 ? 0.2758 0.2418 0.2172 -0.0511 -0.0007 -0.0030 186 TYR B CE2 
10072 C CZ  . TYR B 186 ? 0.2362 0.2340 0.2144 -0.0326 0.0037  -0.0228 186 TYR B CZ  
10073 O OH  . TYR B 186 ? 0.3009 0.2306 0.2088 -0.0154 -0.0281 -0.0325 186 TYR B OH  
10083 N N   . TYR B 187 ? 0.1771 0.2571 0.1882 -0.0672 0.0303  0.0048  187 TYR B N   
10084 C CA  . TYR B 187 ? 0.1662 0.2889 0.1997 -0.0373 0.0398  -0.0224 187 TYR B CA  
10085 C C   . TYR B 187 ? 0.1675 0.3123 0.2228 -0.0294 0.0550  -0.0349 187 TYR B C   
10086 O O   . TYR B 187 ? 0.1667 0.3057 0.2309 -0.0142 0.0565  -0.0288 187 TYR B O   
10087 C CB  . TYR B 187 ? 0.1864 0.3146 0.2018 -0.0253 0.0266  -0.0174 187 TYR B CB  
10088 C CG  . TYR B 187 ? 0.2045 0.3170 0.1947 -0.0461 0.0363  -0.0389 187 TYR B CG  
10089 C CD1 . TYR B 187 ? 0.2107 0.3206 0.1938 -0.0373 0.0359  -0.0481 187 TYR B CD1 
10090 C CD2 . TYR B 187 ? 0.2004 0.3461 0.2017 -0.0350 0.0563  -0.0357 187 TYR B CD2 
10091 C CE1 . TYR B 187 ? 0.2527 0.3805 0.2107 -0.0679 0.0453  -0.0625 187 TYR B CE1 
10092 C CE2 . TYR B 187 ? 0.2535 0.3738 0.2103 -0.0478 0.0619  -0.0486 187 TYR B CE2 
10093 C CZ  . TYR B 187 ? 0.2435 0.3980 0.2144 -0.0711 0.0620  -0.0454 187 TYR B CZ  
10094 O OH  . TYR B 187 ? 0.2705 0.4235 0.2239 -0.0581 0.0583  -0.0382 187 TYR B OH  
10104 N N   . TYR B 188 ? 0.1743 0.3056 0.2354 -0.0274 0.0354  -0.0358 188 TYR B N   
10105 C CA  . TYR B 188 ? 0.1618 0.2948 0.2476 -0.0207 0.0261  -0.0408 188 TYR B CA  
10106 C C   . TYR B 188 ? 0.1929 0.2943 0.2442 -0.0475 0.0061  -0.0386 188 TYR B C   
10107 O O   . TYR B 188 ? 0.2168 0.2904 0.2584 0.0058  0.0081  -0.0400 188 TYR B O   
10108 C CB  . TYR B 188 ? 0.1811 0.2577 0.2621 -0.0323 0.0246  -0.0439 188 TYR B CB  
10109 C CG  . TYR B 188 ? 0.1660 0.2938 0.2999 -0.0457 0.0181  -0.0604 188 TYR B CG  
10110 C CD1 . TYR B 188 ? 0.1952 0.3144 0.3227 -0.0313 -0.0225 -0.0584 188 TYR B CD1 
10111 C CD2 . TYR B 188 ? 0.2010 0.3246 0.3172 -0.0489 0.0176  -0.0821 188 TYR B CD2 
10112 C CE1 . TYR B 188 ? 0.2282 0.3211 0.3395 -0.0412 -0.0244 -0.0747 188 TYR B CE1 
10113 C CE2 . TYR B 188 ? 0.2209 0.3322 0.3346 -0.0233 -0.0074 -0.0884 188 TYR B CE2 
10114 C CZ  . TYR B 188 ? 0.2472 0.3227 0.3469 -0.0488 -0.0275 -0.0986 188 TYR B CZ  
10115 O OH  . TYR B 188 ? 0.2736 0.3898 0.3717 -0.0108 -0.0495 -0.0867 188 TYR B OH  
10125 N N   . HIS B 189 ? 0.1839 0.2856 0.2427 -0.0492 0.0077  -0.0071 189 HIS B N   
10126 C CA  . HIS B 189 ? 0.2326 0.2664 0.2424 -0.0494 0.0003  0.0057  189 HIS B CA  
10127 C C   . HIS B 189 ? 0.2531 0.2152 0.2594 -0.0752 -0.0058 0.0069  189 HIS B C   
10128 O O   . HIS B 189 ? 0.3265 0.2233 0.2575 -0.0430 -0.0080 0.0154  189 HIS B O   
10129 C CB  . HIS B 189 ? 0.2541 0.2407 0.2428 -0.0461 0.0199  -0.0004 189 HIS B CB  
10130 C CG  . HIS B 189 ? 0.3098 0.2087 0.2353 -0.0778 0.0232  -0.0085 189 HIS B CG  
10131 N ND1 . HIS B 189 ? 0.3585 0.2085 0.2454 -0.0526 0.0228  -0.0175 189 HIS B ND1 
10132 C CD2 . HIS B 189 ? 0.3451 0.2275 0.2433 -0.0587 0.0068  -0.0130 189 HIS B CD2 
10133 C CE1 . HIS B 189 ? 0.3953 0.2494 0.2506 -0.0316 0.0005  -0.0276 189 HIS B CE1 
10134 N NE2 . HIS B 189 ? 0.3825 0.2479 0.2466 -0.0422 0.0041  -0.0127 189 HIS B NE2 
10142 N N   . ARG B 190 ? 0.2635 0.2526 0.2881 -0.0214 -0.0056 -0.0309 190 ARG B N   
10143 C CA  . ARG B 190 ? 0.2902 0.2789 0.3043 -0.0516 0.0073  -0.0358 190 ARG B CA  
10144 C C   . ARG B 190 ? 0.3081 0.2893 0.3334 -0.0301 0.0109  -0.0335 190 ARG B C   
10145 O O   . ARG B 190 ? 0.2771 0.2868 0.3403 -0.0120 0.0145  -0.0274 190 ARG B O   
10146 C CB  . ARG B 190 ? 0.2929 0.3098 0.2790 -0.0278 0.0168  -0.0551 190 ARG B CB  
10147 C CG  . ARG B 190 ? 0.2993 0.3342 0.2678 -0.0024 0.0243  -0.0521 190 ARG B CG  
10148 C CD  . ARG B 190 ? 0.2467 0.3634 0.2536 -0.0135 0.0232  -0.0704 190 ARG B CD  
10149 N NE  . ARG B 190 ? 0.2548 0.3770 0.2520 -0.0342 0.0447  -0.0537 190 ARG B NE  
10150 C CZ  . ARG B 190 ? 0.2699 0.4149 0.2549 -0.0108 0.0686  -0.0442 190 ARG B CZ  
10151 N NH1 . ARG B 190 ? 0.2168 0.4127 0.2485 0.0204  0.0614  -0.0264 190 ARG B NH1 
10152 N NH2 . ARG B 190 ? 0.3311 0.4269 0.2694 -0.0188 0.0740  -0.0368 190 ARG B NH2 
10166 N N   . GLY B 191 ? 0.3269 0.3006 0.3599 -0.0002 -0.0094 -0.0543 191 GLY B N   
10167 C CA  . GLY B 191 ? 0.3669 0.3464 0.3868 0.0170  -0.0019 -0.0396 191 GLY B CA  
10168 C C   . GLY B 191 ? 0.3921 0.3751 0.4137 0.0644  0.0066  -0.0396 191 GLY B C   
10169 O O   . GLY B 191 ? 0.4014 0.3193 0.4106 0.0645  0.0498  -0.0237 191 GLY B O   
10173 N N   . ALA B 192 ? 0.4160 0.4403 0.4373 0.0893  -0.0068 -0.0358 192 ALA B N   
10174 C CA  . ALA B 192 ? 0.4457 0.4688 0.4583 0.0947  0.0118  -0.0352 192 ALA B CA  
10175 C C   . ALA B 192 ? 0.4780 0.4761 0.4729 0.1018  0.0399  -0.0532 192 ALA B C   
10176 O O   . ALA B 192 ? 0.4752 0.4896 0.4767 0.1279  0.0622  -0.0587 192 ALA B O   
10177 C CB  . ALA B 192 ? 0.4583 0.4857 0.4674 0.0948  0.0103  -0.0217 192 ALA B CB  
10183 N N   . GLU B 193 ? 0.5134 0.4785 0.4859 0.0897  0.0494  -0.0718 193 GLU B N   
10184 C CA  . GLU B 193 ? 0.5790 0.5245 0.5124 0.0740  0.0446  -0.0824 193 GLU B CA  
10185 C C   . GLU B 193 ? 0.5447 0.4928 0.5037 0.0458  0.0326  -0.1129 193 GLU B C   
10186 O O   . GLU B 193 ? 0.5766 0.4855 0.5190 0.0397  0.0266  -0.1177 193 GLU B O   
10187 C CB  . GLU B 193 ? 0.6631 0.6067 0.5433 0.0690  0.0621  -0.0825 193 GLU B CB  
10188 C CG  . GLU B 193 ? 0.7551 0.6810 0.5700 0.0955  0.0724  -0.0749 193 GLU B CG  
10189 C CD  . GLU B 193 ? 0.8274 0.7256 0.5921 0.1101  0.0857  -0.0716 193 GLU B CD  
10190 O OE1 . GLU B 193 ? 0.8551 0.7261 0.6015 0.1070  0.0913  -0.0625 193 GLU B OE1 
10191 O OE2 . GLU B 193 ? 0.8668 0.7559 0.6032 0.1135  0.0793  -0.0778 193 GLU B OE2 
10198 N N   . ARG B 194 ? 0.4594 0.4645 0.4909 0.0339  0.0324  -0.1074 194 ARG B N   
10199 C CA  . ARG B 194 ? 0.3947 0.4323 0.4777 0.0231  0.0352  -0.1195 194 ARG B CA  
10200 C C   . ARG B 194 ? 0.3190 0.4040 0.4221 0.0452  0.0441  -0.1497 194 ARG B C   
10201 O O   . ARG B 194 ? 0.2700 0.3670 0.4044 0.0721  0.0353  -0.1472 194 ARG B O   
10202 C CB  . ARG B 194 ? 0.4241 0.4517 0.5163 -0.0254 0.0241  -0.0998 194 ARG B CB  
10203 C CG  . ARG B 194 ? 0.4876 0.5246 0.5539 -0.0151 0.0202  -0.0723 194 ARG B CG  
10204 C CD  . ARG B 194 ? 0.5269 0.5874 0.5866 -0.0167 0.0001  -0.0578 194 ARG B CD  
10205 N NE  . ARG B 194 ? 0.5841 0.6626 0.6124 -0.0222 -0.0268 -0.0494 194 ARG B NE  
10206 C CZ  . ARG B 194 ? 0.6386 0.7047 0.6302 -0.0197 -0.0567 -0.0505 194 ARG B CZ  
10207 N NH1 . ARG B 194 ? 0.6760 0.7200 0.6373 -0.0157 -0.0641 -0.0630 194 ARG B NH1 
10208 N NH2 . ARG B 194 ? 0.6388 0.7133 0.6342 -0.0316 -0.0786 -0.0573 194 ARG B NH2 
10222 N N   . GLU B 195 ? 0.3260 0.4272 0.4028 0.0590  0.0603  -0.1367 195 GLU B N   
10223 C CA  . GLU B 195 ? 0.3619 0.4491 0.3994 0.0208  0.0846  -0.0942 195 GLU B CA  
10224 C C   . GLU B 195 ? 0.3456 0.4532 0.3749 0.0376  0.1023  -0.0817 195 GLU B C   
10225 O O   . GLU B 195 ? 0.3797 0.4298 0.3642 0.0217  0.1390  -0.0674 195 GLU B O   
10226 C CB  . GLU B 195 ? 0.3977 0.4806 0.4172 0.0223  0.0713  -0.0866 195 GLU B CB  
10227 C CG  . GLU B 195 ? 0.4086 0.5024 0.4375 0.0013  0.0983  -0.0872 195 GLU B CG  
10228 C CD  . GLU B 195 ? 0.4092 0.4811 0.4583 -0.0630 0.0879  -0.0835 195 GLU B CD  
10229 O OE1 . GLU B 195 ? 0.3942 0.4413 0.4505 -0.1092 0.0939  -0.0769 195 GLU B OE1 
10230 O OE2 . GLU B 195 ? 0.4315 0.5089 0.4805 -0.0786 0.0792  -0.0911 195 GLU B OE2 
10237 N N   . GLY B 196 ? 0.3493 0.4681 0.3643 0.0577  0.0815  -0.0747 196 GLY B N   
10238 C CA  . GLY B 196 ? 0.3467 0.4833 0.3494 0.0583  0.0912  -0.0711 196 GLY B CA  
10239 C C   . GLY B 196 ? 0.3268 0.5008 0.3343 0.0528  0.0970  -0.0580 196 GLY B C   
10240 O O   . GLY B 196 ? 0.3538 0.5390 0.3323 0.0351  0.1104  -0.0295 196 GLY B O   
10244 N N   . MET B 197 ? 0.3102 0.4810 0.3211 0.0719  0.1164  -0.0726 197 MET B N   
10245 C CA  . MET B 197 ? 0.2534 0.4630 0.3108 0.0378  0.0868  -0.0592 197 MET B CA  
10246 C C   . MET B 197 ? 0.2518 0.4519 0.2861 -0.0025 0.0591  -0.0552 197 MET B C   
10247 O O   . MET B 197 ? 0.2633 0.4790 0.2814 0.0150  0.0273  -0.0653 197 MET B O   
10248 C CB  . MET B 197 ? 0.2779 0.4470 0.3331 0.0287  0.1004  -0.0516 197 MET B CB  
10249 C CG  . MET B 197 ? 0.2897 0.4549 0.3723 0.0461  0.1001  -0.0328 197 MET B CG  
10250 S SD  . MET B 197 ? 0.3303 0.4233 0.4182 0.0632  0.0894  -0.0300 197 MET B SD  
10251 C CE  . MET B 197 ? 0.3702 0.4263 0.4168 0.0645  0.0990  -0.0352 197 MET B CE  
10261 N N   . SER B 198 ? 0.2131 0.3946 0.2658 -0.0349 0.0519  -0.0444 198 SER B N   
10262 C CA  . SER B 198 ? 0.2728 0.3942 0.2529 -0.0133 0.0542  -0.0327 198 SER B CA  
10263 C C   . SER B 198 ? 0.2603 0.3461 0.2393 -0.0196 0.0580  -0.0144 198 SER B C   
10264 O O   . SER B 198 ? 0.2675 0.3121 0.2475 -0.0410 0.0499  -0.0026 198 SER B O   
10265 C CB  . SER B 198 ? 0.2671 0.4367 0.2581 -0.0108 0.0581  -0.0114 198 SER B CB  
10266 O OG  . SER B 198 ? 0.2947 0.4481 0.2579 0.0185  0.0601  -0.0050 198 SER B OG  
10272 N N   . GLU B 199 ? 0.2693 0.3050 0.2336 -0.0265 0.0526  -0.0228 199 GLU B N   
10273 C CA  . GLU B 199 ? 0.2561 0.3256 0.2300 -0.0137 0.0476  -0.0295 199 GLU B CA  
10274 C C   . GLU B 199 ? 0.2603 0.3059 0.2170 -0.0317 0.0429  -0.0341 199 GLU B C   
10275 O O   . GLU B 199 ? 0.2213 0.3228 0.2159 -0.0345 0.0571  -0.0382 199 GLU B O   
10276 C CB  . GLU B 199 ? 0.2308 0.3409 0.2478 -0.0241 0.0167  -0.0226 199 GLU B CB  
10277 C CG  . GLU B 199 ? 0.2117 0.3948 0.2674 -0.0739 0.0019  -0.0449 199 GLU B CG  
10278 C CD  . GLU B 199 ? 0.2292 0.4158 0.2774 -0.0856 -0.0085 -0.0388 199 GLU B CD  
10279 O OE1 . GLU B 199 ? 0.2298 0.4615 0.3082 -0.0563 -0.0103 -0.0429 199 GLU B OE1 
10280 O OE2 . GLU B 199 ? 0.2436 0.4115 0.2552 -0.0806 -0.0062 -0.0158 199 GLU B OE2 
10287 N N   . ARG B 200 ? 0.2881 0.3533 0.2038 -0.0195 0.0385  -0.0156 200 ARG B N   
10288 C CA  . ARG B 200 ? 0.3233 0.3671 0.2068 -0.0345 0.0344  0.0107  200 ARG B CA  
10289 C C   . ARG B 200 ? 0.2609 0.3407 0.1932 -0.0213 0.0333  -0.0019 200 ARG B C   
10290 O O   . ARG B 200 ? 0.2679 0.3622 0.1893 -0.0585 0.0363  -0.0217 200 ARG B O   
10291 C CB  . ARG B 200 ? 0.4629 0.4502 0.2216 -0.0415 0.0155  0.0371  200 ARG B CB  
10292 C CG  . ARG B 200 ? 0.6775 0.5499 0.2580 -0.0338 -0.0069 0.0406  200 ARG B CG  
10293 C CD  . ARG B 200 ? 0.8845 0.6494 0.2929 -0.0308 -0.0236 0.0592  200 ARG B CD  
10294 N NE  . ARG B 200 ? 1.0664 0.7657 0.3328 -0.0040 -0.0552 0.0514  200 ARG B NE  
10295 C CZ  . ARG B 200 ? 1.1956 0.8488 0.3724 0.0078  -0.0639 0.0317  200 ARG B CZ  
10296 N NH1 . ARG B 200 ? 1.2352 0.8843 0.3934 -0.0020 -0.0698 0.0242  200 ARG B NH1 
10297 N NH2 . ARG B 200 ? 1.2411 0.8786 0.3873 0.0230  -0.0617 0.0258  200 ARG B NH2 
10311 N N   . GLU B 201 ? 0.2765 0.3725 0.1931 -0.0304 0.0300  -0.0109 201 GLU B N   
10312 C CA  . GLU B 201 ? 0.2253 0.3818 0.2116 -0.0161 0.0585  -0.0162 201 GLU B CA  
10313 C C   . GLU B 201 ? 0.2100 0.3670 0.2088 0.0140  0.0524  -0.0354 201 GLU B C   
10314 O O   . GLU B 201 ? 0.2518 0.3947 0.2100 0.0368  0.0322  -0.0350 201 GLU B O   
10315 C CB  . GLU B 201 ? 0.2441 0.3844 0.2208 -0.0234 0.0724  -0.0363 201 GLU B CB  
10316 C CG  . GLU B 201 ? 0.2994 0.4273 0.2164 -0.0437 0.0804  -0.0674 201 GLU B CG  
10317 C CD  . GLU B 201 ? 0.3949 0.4850 0.2318 -0.0015 0.0866  -0.0835 201 GLU B CD  
10318 O OE1 . GLU B 201 ? 0.4119 0.4590 0.2408 0.1110  0.0908  -0.0716 201 GLU B OE1 
10319 O OE2 . GLU B 201 ? 0.4587 0.5853 0.2525 -0.0163 0.0833  -0.0875 201 GLU B OE2 
10326 N N   . PHE B 202 ? 0.2133 0.3138 0.1937 -0.0139 0.0391  -0.0376 202 PHE B N   
10327 C CA  . PHE B 202 ? 0.2308 0.2261 0.1947 0.0118  0.0279  -0.0366 202 PHE B CA  
10328 C C   . PHE B 202 ? 0.2441 0.2627 0.1805 -0.0192 0.0319  -0.0262 202 PHE B C   
10329 O O   . PHE B 202 ? 0.2508 0.2661 0.1647 -0.0276 0.0208  -0.0011 202 PHE B O   
10330 C CB  . PHE B 202 ? 0.2226 0.2654 0.2012 -0.0229 0.0151  0.0033  202 PHE B CB  
10331 C CG  . PHE B 202 ? 0.1981 0.2288 0.2042 -0.0540 0.0204  0.0093  202 PHE B CG  
10332 C CD1 . PHE B 202 ? 0.2406 0.2859 0.2199 -0.0197 0.0119  -0.0190 202 PHE B CD1 
10333 C CD2 . PHE B 202 ? 0.2529 0.2257 0.2136 -0.0532 0.0180  0.0026  202 PHE B CD2 
10334 C CE1 . PHE B 202 ? 0.2570 0.2714 0.2248 -0.0359 0.0171  -0.0198 202 PHE B CE1 
10335 C CE2 . PHE B 202 ? 0.2465 0.2555 0.2220 -0.0533 0.0198  -0.0271 202 PHE B CE2 
10336 C CZ  . PHE B 202 ? 0.2104 0.2934 0.2270 -0.0102 0.0082  -0.0249 202 PHE B CZ  
10346 N N   . SER B 203 ? 0.2431 0.2908 0.1810 -0.0217 0.0340  -0.0002 203 SER B N   
10347 C CA  . SER B 203 ? 0.2301 0.2282 0.1817 -0.0147 0.0410  -0.0203 203 SER B CA  
10348 C C   . SER B 203 ? 0.2266 0.2707 0.1775 -0.0123 0.0325  -0.0190 203 SER B C   
10349 O O   . SER B 203 ? 0.2066 0.2674 0.1744 -0.0251 0.0259  -0.0221 203 SER B O   
10350 C CB  . SER B 203 ? 0.2403 0.2040 0.1829 -0.0221 0.0383  -0.0175 203 SER B CB  
10351 O OG  . SER B 203 ? 0.2610 0.2119 0.1998 -0.0377 0.0148  -0.0250 203 SER B OG  
10357 N N   . ALA B 204 ? 0.2321 0.2404 0.1794 0.0128  0.0276  -0.0563 204 ALA B N   
10358 C CA  . ALA B 204 ? 0.2448 0.2722 0.1854 0.0074  0.0374  -0.0441 204 ALA B CA  
10359 C C   . ALA B 204 ? 0.2294 0.2395 0.1920 -0.0122 0.0389  -0.0387 204 ALA B C   
10360 O O   . ALA B 204 ? 0.2770 0.2785 0.1997 -0.0247 0.0367  -0.0165 204 ALA B O   
10361 C CB  . ALA B 204 ? 0.2904 0.3108 0.1859 -0.0179 0.0408  -0.0278 204 ALA B CB  
10367 N N   . HIS B 205 ? 0.2597 0.2682 0.2007 0.0116  0.0306  -0.0391 205 HIS B N   
10368 C CA  . HIS B 205 ? 0.1917 0.2319 0.2225 -0.0188 0.0401  -0.0238 205 HIS B CA  
10369 C C   . HIS B 205 ? 0.2444 0.2495 0.2079 -0.0497 0.0191  0.0013  205 HIS B C   
10370 O O   . HIS B 205 ? 0.2259 0.2225 0.2173 0.0142  -0.0047 -0.0303 205 HIS B O   
10371 C CB  . HIS B 205 ? 0.1599 0.2440 0.2588 0.0154  0.0436  0.0074  205 HIS B CB  
10372 C CG  . HIS B 205 ? 0.2143 0.3161 0.3071 -0.0010 0.0488  0.0421  205 HIS B CG  
10373 N ND1 . HIS B 205 ? 0.2818 0.3629 0.3240 -0.0192 0.0651  0.0561  205 HIS B ND1 
10374 C CD2 . HIS B 205 ? 0.2372 0.3492 0.3243 -0.0114 0.0364  0.0655  205 HIS B CD2 
10375 C CE1 . HIS B 205 ? 0.2753 0.3883 0.3314 -0.0213 0.0436  0.0696  205 HIS B CE1 
10376 N NE2 . HIS B 205 ? 0.2513 0.4119 0.3328 -0.0127 0.0341  0.0647  205 HIS B NE2 
10384 N N   . CYS B 206 ? 0.2090 0.2351 0.1911 -0.0242 0.0353  -0.0108 206 CYS B N   
10385 C CA  . CYS B 206 ? 0.1838 0.2220 0.1851 -0.0402 0.0141  -0.0212 206 CYS B CA  
10386 C C   . CYS B 206 ? 0.1912 0.2321 0.1868 0.0103  0.0266  -0.0076 206 CYS B C   
10387 O O   . CYS B 206 ? 0.2324 0.2304 0.1731 0.0125  0.0068  0.0027  206 CYS B O   
10388 C CB  . CYS B 206 ? 0.2007 0.2472 0.1965 -0.0143 0.0136  -0.0195 206 CYS B CB  
10389 S SG  . CYS B 206 ? 0.2280 0.2566 0.1954 -0.0401 0.0091  -0.0271 206 CYS B SG  
10395 N N   . ALA B 207 ? 0.1718 0.2406 0.1906 0.0070  0.0300  0.0017  207 ALA B N   
10396 C CA  . ALA B 207 ? 0.1901 0.2264 0.1974 0.0012  0.0049  -0.0219 207 ALA B CA  
10397 C C   . ALA B 207 ? 0.1960 0.1917 0.2087 -0.0339 -0.0022 -0.0238 207 ALA B C   
10398 O O   . ALA B 207 ? 0.2451 0.1585 0.2172 -0.0481 0.0175  -0.0071 207 ALA B O   
10399 C CB  . ALA B 207 ? 0.2226 0.2316 0.2008 -0.0284 0.0278  -0.0198 207 ALA B CB  
10405 N N   . ALA B 208 ? 0.1985 0.2031 0.1981 -0.0519 0.0035  -0.0253 208 ALA B N   
10406 C CA  . ALA B 208 ? 0.1949 0.2340 0.2084 -0.0238 0.0370  -0.0416 208 ALA B CA  
10407 C C   . ALA B 208 ? 0.2189 0.2161 0.2246 -0.0061 0.0151  -0.0051 208 ALA B C   
10408 O O   . ALA B 208 ? 0.2005 0.2345 0.2405 0.0102  0.0264  0.0134  208 ALA B O   
10409 C CB  . ALA B 208 ? 0.1970 0.2801 0.2213 0.0022  0.0449  -0.0237 208 ALA B CB  
10415 N N   . LYS B 209 ? 0.2241 0.2115 0.2162 0.0014  -0.0026 -0.0186 209 LYS B N   
10416 C CA  . LYS B 209 ? 0.1845 0.2426 0.2143 -0.0359 0.0142  -0.0054 209 LYS B CA  
10417 C C   . LYS B 209 ? 0.1843 0.2031 0.1978 -0.0040 0.0357  0.0067  209 LYS B C   
10418 O O   . LYS B 209 ? 0.2082 0.2072 0.2030 0.0026  0.0497  0.0071  209 LYS B O   
10419 C CB  . LYS B 209 ? 0.1716 0.2511 0.2463 -0.0325 0.0401  -0.0002 209 LYS B CB  
10420 C CG  . LYS B 209 ? 0.1958 0.2832 0.2769 -0.0315 0.0488  -0.0111 209 LYS B CG  
10421 C CD  . LYS B 209 ? 0.2678 0.3797 0.3157 -0.0122 0.0305  -0.0007 209 LYS B CD  
10422 C CE  . LYS B 209 ? 0.3624 0.4413 0.3629 0.0044  0.0481  0.0114  209 LYS B CE  
10423 N NZ  . LYS B 209 ? 0.4347 0.4674 0.3908 -0.0062 0.0360  0.0291  209 LYS B NZ  
10437 N N   . LEU B 210 ? 0.1780 0.2038 0.1883 0.0186  0.0106  -0.0022 210 LEU B N   
10438 C CA  . LEU B 210 ? 0.1675 0.2041 0.1723 -0.0216 -0.0037 0.0009  210 LEU B CA  
10439 C C   . LEU B 210 ? 0.1494 0.1912 0.1692 -0.0322 -0.0018 -0.0037 210 LEU B C   
10440 O O   . LEU B 210 ? 0.1855 0.1523 0.1768 0.0068  0.0147  -0.0144 210 LEU B O   
10441 C CB  . LEU B 210 ? 0.1917 0.2227 0.1576 -0.0078 0.0031  0.0022  210 LEU B CB  
10442 C CG  . LEU B 210 ? 0.1539 0.1928 0.1594 0.0114  -0.0115 -0.0013 210 LEU B CG  
10443 C CD1 . LEU B 210 ? 0.1751 0.2093 0.1841 0.0051  -0.0062 -0.0120 210 LEU B CD1 
10444 C CD2 . LEU B 210 ? 0.1644 0.2154 0.1598 0.0146  -0.0101 -0.0202 210 LEU B CD2 
10456 N N   . GLU B 211 ? 0.1825 0.2072 0.1766 0.0233  0.0114  -0.0061 211 GLU B N   
10457 C CA  . GLU B 211 ? 0.2176 0.1704 0.1657 -0.0134 -0.0081 0.0108  211 GLU B CA  
10458 C C   . GLU B 211 ? 0.2195 0.2159 0.1828 -0.0039 -0.0032 -0.0096 211 GLU B C   
10459 O O   . GLU B 211 ? 0.1939 0.2266 0.1795 0.0173  0.0211  0.0003  211 GLU B O   
10460 C CB  . GLU B 211 ? 0.2567 0.1791 0.1673 -0.0060 0.0055  0.0179  211 GLU B CB  
10461 C CG  . GLU B 211 ? 0.2354 0.2256 0.1687 -0.0010 0.0028  0.0034  211 GLU B CG  
10462 C CD  . GLU B 211 ? 0.2561 0.3163 0.1847 -0.0770 0.0183  0.0258  211 GLU B CD  
10463 O OE1 . GLU B 211 ? 0.2747 0.2750 0.1971 -0.0293 0.0132  -0.0048 211 GLU B OE1 
10464 O OE2 . GLU B 211 ? 0.3745 0.4710 0.1974 -0.0813 0.0253  0.0302  211 GLU B OE2 
10471 N N   . GLU B 212 ? 0.2290 0.2407 0.1875 -0.0019 -0.0021 -0.0086 212 GLU B N   
10472 C CA  . GLU B 212 ? 0.2293 0.2421 0.2149 0.0258  -0.0013 -0.0041 212 GLU B CA  
10473 C C   . GLU B 212 ? 0.2512 0.2485 0.2110 -0.0203 -0.0108 0.0093  212 GLU B C   
10474 O O   . GLU B 212 ? 0.2359 0.2202 0.2141 -0.0169 -0.0018 -0.0028 212 GLU B O   
10475 C CB  . GLU B 212 ? 0.2488 0.3492 0.2553 0.0951  -0.0083 0.0019  212 GLU B CB  
10476 C CG  . GLU B 212 ? 0.2665 0.5216 0.3104 0.1111  0.0005  -0.0058 212 GLU B CG  
10477 C CD  . GLU B 212 ? 0.2952 0.6896 0.3690 0.1366  -0.0040 -0.0015 212 GLU B CD  
10478 O OE1 . GLU B 212 ? 0.3270 0.7733 0.4047 0.1358  -0.0415 0.0226  212 GLU B OE1 
10479 O OE2 . GLU B 212 ? 0.3249 0.7670 0.4082 0.1196  0.0154  -0.0239 212 GLU B OE2 
10486 N N   . MET B 213 ? 0.2081 0.2484 0.2030 -0.0045 -0.0059 0.0304  213 MET B N   
10487 C CA  . MET B 213 ? 0.2003 0.2301 0.1968 -0.0522 0.0261  0.0235  213 MET B CA  
10488 C C   . MET B 213 ? 0.1925 0.2099 0.1903 -0.0497 0.0096  0.0103  213 MET B C   
10489 O O   . MET B 213 ? 0.1986 0.2012 0.1970 -0.0217 0.0035  0.0142  213 MET B O   
10490 C CB  . MET B 213 ? 0.1948 0.2010 0.2002 0.0145  0.0237  0.0114  213 MET B CB  
10491 C CG  . MET B 213 ? 0.2358 0.1631 0.1951 0.0190  0.0119  -0.0060 213 MET B CG  
10492 S SD  . MET B 213 ? 0.2171 0.2023 0.2172 -0.0001 0.0038  -0.0236 213 MET B SD  
10493 C CE  . MET B 213 ? 0.2610 0.2370 0.2125 -0.0358 -0.0199 -0.0042 213 MET B CE  
10503 N N   . ILE B 214 ? 0.1707 0.2171 0.2008 -0.0073 0.0214  0.0249  214 ILE B N   
10504 C CA  . ILE B 214 ? 0.1742 0.1774 0.2004 -0.0191 0.0061  0.0113  214 ILE B CA  
10505 C C   . ILE B 214 ? 0.1748 0.1834 0.2096 0.0052  0.0018  0.0032  214 ILE B C   
10506 O O   . ILE B 214 ? 0.2141 0.1925 0.2047 0.0049  -0.0034 -0.0025 214 ILE B O   
10507 C CB  . ILE B 214 ? 0.1577 0.1754 0.2061 -0.0047 0.0144  0.0227  214 ILE B CB  
10508 C CG1 . ILE B 214 ? 0.1669 0.1408 0.2107 -0.0130 0.0226  0.0371  214 ILE B CG1 
10509 C CG2 . ILE B 214 ? 0.1905 0.1706 0.2095 -0.0070 -0.0039 0.0426  214 ILE B CG2 
10510 C CD1 . ILE B 214 ? 0.1890 0.1470 0.2249 -0.0661 -0.0018 0.0265  214 ILE B CD1 
10522 N N   . LEU B 215 ? 0.1887 0.1813 0.2121 0.0154  0.0154  -0.0091 215 LEU B N   
10523 C CA  . LEU B 215 ? 0.2129 0.1706 0.2230 0.0523  0.0167  -0.0266 215 LEU B CA  
10524 C C   . LEU B 215 ? 0.2176 0.1879 0.2326 -0.0085 0.0094  -0.0071 215 LEU B C   
10525 O O   . LEU B 215 ? 0.2795 0.1614 0.2477 -0.0281 -0.0153 -0.0013 215 LEU B O   
10526 C CB  . LEU B 215 ? 0.1988 0.2548 0.2306 0.0481  0.0180  -0.0034 215 LEU B CB  
10527 C CG  . LEU B 215 ? 0.2382 0.2644 0.2255 0.0465  0.0078  -0.0025 215 LEU B CG  
10528 C CD1 . LEU B 215 ? 0.3107 0.2715 0.2357 0.0745  0.0143  -0.0064 215 LEU B CD1 
10529 C CD2 . LEU B 215 ? 0.3032 0.2806 0.2346 0.0409  0.0131  -0.0057 215 LEU B CD2 
10541 N N   . ALA B 216 ? 0.2295 0.1473 0.2288 0.0165  0.0039  0.0148  216 ALA B N   
10542 C CA  . ALA B 216 ? 0.2570 0.1955 0.2382 0.0243  0.0055  0.0107  216 ALA B CA  
10543 C C   . ALA B 216 ? 0.2475 0.1433 0.2335 0.0236  0.0045  0.0273  216 ALA B C   
10544 O O   . ALA B 216 ? 0.3023 0.1344 0.2464 0.0186  -0.0037 0.0383  216 ALA B O   
10545 C CB  . ALA B 216 ? 0.2755 0.2060 0.2456 0.0515  -0.0269 0.0109  216 ALA B CB  
10551 N N   . GLU B 217 ? 0.2137 0.1698 0.2185 0.0208  -0.0266 -0.0151 217 GLU B N   
10552 C CA  . GLU B 217 ? 0.1992 0.1569 0.2161 0.0423  0.0094  -0.0059 217 GLU B CA  
10553 C C   . GLU B 217 ? 0.1832 0.1825 0.2206 0.0160  0.0274  0.0033  217 GLU B C   
10554 O O   . GLU B 217 ? 0.1874 0.2104 0.2208 -0.0083 0.0302  0.0023  217 GLU B O   
10555 C CB  . GLU B 217 ? 0.1990 0.1653 0.2080 0.0200  -0.0036 -0.0115 217 GLU B CB  
10556 C CG  . GLU B 217 ? 0.1948 0.2004 0.2084 0.0332  -0.0161 0.0076  217 GLU B CG  
10557 C CD  . GLU B 217 ? 0.1847 0.2122 0.2204 -0.0046 -0.0395 0.0374  217 GLU B CD  
10558 O OE1 . GLU B 217 ? 0.2027 0.2678 0.2042 -0.0210 -0.0008 0.0342  217 GLU B OE1 
10559 O OE2 . GLU B 217 ? 0.2375 0.3052 0.2502 0.0175  -0.0457 0.0363  217 GLU B OE2 
10566 N N   . GLY B 218 ? 0.1674 0.2458 0.2140 0.0134  0.0118  -0.0273 218 GLY B N   
10567 C CA  . GLY B 218 ? 0.1792 0.2263 0.2088 -0.0199 0.0207  -0.0271 218 GLY B CA  
10568 C C   . GLY B 218 ? 0.1972 0.2049 0.1878 -0.0117 0.0159  -0.0038 218 GLY B C   
10569 O O   . GLY B 218 ? 0.1997 0.1921 0.1779 -0.0097 0.0146  -0.0203 218 GLY B O   
10573 N N   . PRO B 219 ? 0.2361 0.2349 0.1682 -0.0047 -0.0132 0.0030  219 PRO B N   
10574 C CA  . PRO B 219 ? 0.2215 0.2661 0.1689 0.0029  -0.0141 0.0215  219 PRO B CA  
10575 C C   . PRO B 219 ? 0.2210 0.2030 0.1898 -0.0016 -0.0569 0.0068  219 PRO B C   
10576 O O   . PRO B 219 ? 0.2182 0.1816 0.2035 -0.0226 -0.0554 0.0406  219 PRO B O   
10577 C CB  . PRO B 219 ? 0.2824 0.3422 0.1709 0.0213  0.0132  0.0309  219 PRO B CB  
10578 C CG  . PRO B 219 ? 0.3595 0.3210 0.1878 -0.0069 -0.0130 -0.0051 219 PRO B CG  
10579 C CD  . PRO B 219 ? 0.2729 0.2734 0.1692 -0.0058 -0.0198 -0.0106 219 PRO B CD  
10587 N N   . GLU B 220 ? 0.2160 0.2061 0.1998 -0.0054 -0.0555 -0.0211 220 GLU B N   
10588 C CA  . GLU B 220 ? 0.1828 0.2038 0.2042 -0.0400 -0.0313 -0.0341 220 GLU B CA  
10589 C C   . GLU B 220 ? 0.1656 0.1886 0.1895 -0.0061 -0.0176 -0.0017 220 GLU B C   
10590 O O   . GLU B 220 ? 0.1772 0.2097 0.1989 0.0092  -0.0222 -0.0015 220 GLU B O   
10591 C CB  . GLU B 220 ? 0.2145 0.1895 0.2242 -0.0684 -0.0182 -0.0267 220 GLU B CB  
10592 C CG  . GLU B 220 ? 0.2857 0.2325 0.2562 -0.0640 -0.0112 -0.0131 220 GLU B CG  
10593 C CD  . GLU B 220 ? 0.3449 0.2603 0.2822 -0.0343 0.0016  0.0014  220 GLU B CD  
10594 O OE1 . GLU B 220 ? 0.2804 0.2740 0.2759 -0.0461 0.0367  -0.0113 220 GLU B OE1 
10595 O OE2 . GLU B 220 ? 0.3799 0.2256 0.3128 -0.0202 0.0031  -0.0272 220 GLU B OE2 
10602 N N   . THR B 221 ? 0.1894 0.1537 0.1793 -0.0052 -0.0071 -0.0172 221 THR B N   
10603 C CA  . THR B 221 ? 0.1785 0.1532 0.1763 -0.0347 -0.0117 -0.0123 221 THR B CA  
10604 C C   . THR B 221 ? 0.1664 0.1386 0.1783 -0.0003 -0.0128 0.0065  221 THR B C   
10605 O O   . THR B 221 ? 0.1689 0.1557 0.1731 -0.0105 -0.0266 -0.0182 221 THR B O   
10606 C CB  . THR B 221 ? 0.1934 0.1980 0.1993 -0.0388 -0.0170 0.0056  221 THR B CB  
10607 O OG1 . THR B 221 ? 0.2052 0.1762 0.1879 -0.0194 -0.0291 -0.0074 221 THR B OG1 
10608 C CG2 . THR B 221 ? 0.2289 0.2424 0.2191 -0.0653 -0.0156 -0.0033 221 THR B CG2 
10616 N N   . VAL B 222 ? 0.1878 0.1273 0.1754 -0.0106 0.0187  -0.0021 222 VAL B N   
10617 C CA  . VAL B 222 ? 0.1807 0.1402 0.1731 -0.0474 -0.0026 -0.0143 222 VAL B CA  
10618 C C   . VAL B 222 ? 0.1977 0.1132 0.1546 -0.0235 -0.0043 0.0046  222 VAL B C   
10619 O O   . VAL B 222 ? 0.1874 0.1792 0.1567 0.0205  0.0185  0.0330  222 VAL B O   
10620 C CB  . VAL B 222 ? 0.1746 0.1049 0.1885 -0.0371 0.0065  0.0101  222 VAL B CB  
10621 C CG1 . VAL B 222 ? 0.2116 0.1817 0.2006 -0.0363 0.0172  0.0193  222 VAL B CG1 
10622 C CG2 . VAL B 222 ? 0.1990 0.1011 0.1970 -0.0316 -0.0047 0.0110  222 VAL B CG2 
10632 N N   . ALA B 223 ? 0.1788 0.1570 0.1623 0.0204  -0.0230 -0.0015 223 ALA B N   
10633 C CA  . ALA B 223 ? 0.1913 0.1411 0.1737 0.0079  -0.0128 0.0000  223 ALA B CA  
10634 C C   . ALA B 223 ? 0.1547 0.1318 0.1613 0.0028  -0.0159 0.0124  223 ALA B C   
10635 O O   . ALA B 223 ? 0.1662 0.1552 0.1439 -0.0083 -0.0060 0.0197  223 ALA B O   
10636 C CB  . ALA B 223 ? 0.1493 0.1937 0.1963 -0.0330 0.0034  0.0075  223 ALA B CB  
10642 N N   . ALA B 224 ? 0.1341 0.1400 0.1761 -0.0101 -0.0088 0.0105  224 ALA B N   
10643 C CA  . ALA B 224 ? 0.1614 0.1477 0.1543 -0.0096 0.0084  0.0048  224 ALA B CA  
10644 C C   . ALA B 224 ? 0.1742 0.1294 0.1564 0.0128  -0.0095 -0.0003 224 ALA B C   
10645 O O   . ALA B 224 ? 0.1500 0.1583 0.1613 -0.0319 -0.0191 0.0071  224 ALA B O   
10646 C CB  . ALA B 224 ? 0.1485 0.1740 0.1594 -0.0168 0.0153  0.0115  224 ALA B CB  
10652 N N   . PHE B 225 ? 0.1833 0.1275 0.1508 -0.0363 -0.0173 0.0029  225 PHE B N   
10653 C CA  . PHE B 225 ? 0.1759 0.1438 0.1504 -0.0632 -0.0287 -0.0016 225 PHE B CA  
10654 C C   . PHE B 225 ? 0.1837 0.1428 0.1627 -0.0503 -0.0292 0.0026  225 PHE B C   
10655 O O   . PHE B 225 ? 0.2127 0.1638 0.1704 -0.0395 -0.0059 -0.0070 225 PHE B O   
10656 C CB  . PHE B 225 ? 0.1343 0.1766 0.1449 -0.0502 -0.0251 0.0137  225 PHE B CB  
10657 C CG  . PHE B 225 ? 0.1817 0.1734 0.1562 -0.0578 -0.0252 -0.0046 225 PHE B CG  
10658 C CD1 . PHE B 225 ? 0.2092 0.1876 0.1634 -0.0589 -0.0322 0.0071  225 PHE B CD1 
10659 C CD2 . PHE B 225 ? 0.1986 0.2503 0.1668 -0.0483 -0.0192 -0.0009 225 PHE B CD2 
10660 C CE1 . PHE B 225 ? 0.2335 0.2181 0.1685 -0.0432 -0.0279 0.0043  225 PHE B CE1 
10661 C CE2 . PHE B 225 ? 0.2456 0.2578 0.1708 -0.0404 -0.0376 -0.0053 225 PHE B CE2 
10662 C CZ  . PHE B 225 ? 0.2143 0.2340 0.1695 -0.0827 -0.0255 0.0178  225 PHE B CZ  
10672 N N   . ILE B 226 ? 0.1618 0.1264 0.1665 -0.0257 -0.0139 0.0249  226 ILE B N   
10673 C CA  . ILE B 226 ? 0.1688 0.1400 0.1664 -0.0492 0.0060  0.0060  226 ILE B CA  
10674 C C   . ILE B 226 ? 0.1788 0.1110 0.1783 0.0009  -0.0007 0.0047  226 ILE B C   
10675 O O   . ILE B 226 ? 0.1461 0.1683 0.1895 -0.0007 0.0111  0.0054  226 ILE B O   
10676 C CB  . ILE B 226 ? 0.1796 0.1584 0.1501 -0.0385 0.0121  0.0116  226 ILE B CB  
10677 C CG1 . ILE B 226 ? 0.1641 0.2371 0.1389 -0.0132 0.0005  0.0084  226 ILE B CG1 
10678 C CG2 . ILE B 226 ? 0.1960 0.1520 0.1494 -0.0358 -0.0192 0.0175  226 ILE B CG2 
10679 C CD1 . ILE B 226 ? 0.1894 0.2799 0.1562 -0.0144 0.0064  0.0162  226 ILE B CD1 
10691 N N   . GLY B 227 ? 0.1775 0.1496 0.1674 -0.0085 -0.0055 0.0229  227 GLY B N   
10692 C CA  . GLY B 227 ? 0.1744 0.1838 0.1587 -0.0238 0.0025  0.0351  227 GLY B CA  
10693 C C   . GLY B 227 ? 0.1559 0.1744 0.1469 0.0009  -0.0221 0.0218  227 GLY B C   
10694 O O   . GLY B 227 ? 0.1422 0.2043 0.1590 -0.0275 -0.0210 0.0224  227 GLY B O   
10698 N N   . GLU B 228 ? 0.2058 0.1519 0.1540 0.0063  -0.0352 0.0055  228 GLU B N   
10699 C CA  . GLU B 228 ? 0.2320 0.1683 0.1576 -0.0111 -0.0190 -0.0020 228 GLU B CA  
10700 C C   . GLU B 228 ? 0.2191 0.1359 0.1501 -0.0305 -0.0081 -0.0007 228 GLU B C   
10701 O O   . GLU B 228 ? 0.2046 0.1564 0.1715 -0.0327 0.0123  -0.0008 228 GLU B O   
10702 C CB  . GLU B 228 ? 0.2071 0.2005 0.1481 -0.0336 -0.0187 0.0014  228 GLU B CB  
10703 C CG  . GLU B 228 ? 0.1853 0.1468 0.1495 -0.0064 -0.0069 -0.0101 228 GLU B CG  
10704 C CD  . GLU B 228 ? 0.1896 0.1710 0.1566 -0.0336 -0.0044 -0.0021 228 GLU B CD  
10705 O OE1 . GLU B 228 ? 0.1935 0.2362 0.1643 -0.0396 0.0047  0.0179  228 GLU B OE1 
10706 O OE2 . GLU B 228 ? 0.2171 0.1893 0.1691 -0.0339 0.0150  0.0187  228 GLU B OE2 
10713 N N   . PRO B 229 ? 0.2307 0.1675 0.1433 -0.0229 0.0111  0.0005  229 PRO B N   
10714 C CA  . PRO B 229 ? 0.2010 0.2161 0.1446 -0.0193 0.0229  -0.0042 229 PRO B CA  
10715 C C   . PRO B 229 ? 0.2034 0.1703 0.1482 -0.0302 0.0118  -0.0160 229 PRO B C   
10716 O O   . PRO B 229 ? 0.2167 0.1910 0.1490 -0.0374 0.0240  -0.0288 229 PRO B O   
10717 C CB  . PRO B 229 ? 0.2190 0.2301 0.1464 -0.0539 0.0432  -0.0142 229 PRO B CB  
10718 C CG  . PRO B 229 ? 0.2562 0.2035 0.1392 -0.0512 0.0308  -0.0082 229 PRO B CG  
10719 C CD  . PRO B 229 ? 0.2471 0.1770 0.1390 -0.0448 0.0304  -0.0023 229 PRO B CD  
10727 N N   . VAL B 230 ? 0.2261 0.1440 0.1691 -0.0734 0.0063  -0.0035 230 VAL B N   
10728 C CA  . VAL B 230 ? 0.1498 0.1707 0.1768 -0.0335 0.0059  0.0015  230 VAL B CA  
10729 C C   . VAL B 230 ? 0.1496 0.1990 0.1757 -0.0593 0.0223  0.0201  230 VAL B C   
10730 O O   . VAL B 230 ? 0.1716 0.2297 0.1662 -0.0660 0.0228  0.0008  230 VAL B O   
10731 C CB  . VAL B 230 ? 0.1576 0.2027 0.1891 -0.0448 0.0040  0.0241  230 VAL B CB  
10732 C CG1 . VAL B 230 ? 0.1651 0.2487 0.2026 -0.0685 0.0019  0.0103  230 VAL B CG1 
10733 C CG2 . VAL B 230 ? 0.1662 0.1919 0.2019 -0.0685 -0.0050 0.0542  230 VAL B CG2 
10743 N N   . LEU B 231 ? 0.1647 0.2055 0.1698 -0.0239 -0.0036 0.0356  231 LEU B N   
10744 C CA  . LEU B 231 ? 0.1897 0.2015 0.1872 -0.0416 -0.0005 0.0101  231 LEU B CA  
10745 C C   . LEU B 231 ? 0.1882 0.2007 0.1877 -0.0379 0.0174  0.0119  231 LEU B C   
10746 O O   . LEU B 231 ? 0.1899 0.2519 0.1829 -0.0492 0.0154  0.0095  231 LEU B O   
10747 C CB  . LEU B 231 ? 0.2118 0.2233 0.1955 -0.0657 0.0163  -0.0118 231 LEU B CB  
10748 C CG  . LEU B 231 ? 0.1760 0.1952 0.1907 -0.0570 0.0170  -0.0305 231 LEU B CG  
10749 C CD1 . LEU B 231 ? 0.1737 0.1730 0.1799 -0.0370 0.0116  -0.0039 231 LEU B CD1 
10750 C CD2 . LEU B 231 ? 0.1786 0.2224 0.1997 -0.0830 0.0333  -0.0430 231 LEU B CD2 
10762 N N   . GLY B 232 ? 0.1871 0.2183 0.1796 -0.0421 0.0230  -0.0203 232 GLY B N   
10763 C CA  . GLY B 232 ? 0.1955 0.1964 0.1758 -0.0392 -0.0095 -0.0070 232 GLY B CA  
10764 C C   . GLY B 232 ? 0.1883 0.1883 0.1742 -0.0770 -0.0023 -0.0036 232 GLY B C   
10765 O O   . GLY B 232 ? 0.1728 0.2224 0.1791 -0.0168 0.0126  -0.0024 232 GLY B O   
10769 N N   . THR B 233 ? 0.1732 0.2034 0.1618 -0.0517 -0.0215 0.0102  233 THR B N   
10770 C CA  . THR B 233 ? 0.2048 0.2026 0.1728 -0.0371 -0.0258 0.0226  233 THR B CA  
10771 C C   . THR B 233 ? 0.2044 0.1948 0.1719 -0.0596 -0.0204 -0.0105 233 THR B C   
10772 O O   . THR B 233 ? 0.2086 0.2351 0.1715 -0.0554 -0.0203 -0.0136 233 THR B O   
10773 C CB  . THR B 233 ? 0.2451 0.2227 0.1650 -0.0491 -0.0140 -0.0228 233 THR B CB  
10774 O OG1 . THR B 233 ? 0.2576 0.2722 0.1704 -0.0140 0.0337  -0.0136 233 THR B OG1 
10775 C CG2 . THR B 233 ? 0.2407 0.2456 0.1726 -0.1082 -0.0072 -0.0116 233 THR B CG2 
10783 N N   . GLY B 234 ? 0.2140 0.1982 0.1719 -0.0532 0.0032  -0.0023 234 GLY B N   
10784 C CA  . GLY B 234 ? 0.2175 0.2208 0.1802 -0.0624 -0.0095 0.0054  234 GLY B CA  
10785 C C   . GLY B 234 ? 0.2057 0.2501 0.1867 -0.0206 0.0031  -0.0180 234 GLY B C   
10786 O O   . GLY B 234 ? 0.1892 0.2861 0.1731 -0.0624 0.0068  -0.0269 234 GLY B O   
10790 N N   . GLY B 235 ? 0.1707 0.2302 0.1967 0.0028  0.0179  -0.0083 235 GLY B N   
10791 C CA  . GLY B 235 ? 0.1773 0.2317 0.2042 -0.0414 0.0244  -0.0183 235 GLY B CA  
10792 C C   . GLY B 235 ? 0.1499 0.2118 0.2054 -0.0366 0.0213  -0.0125 235 GLY B C   
10793 O O   . GLY B 235 ? 0.1721 0.2288 0.2132 -0.0277 -0.0001 -0.0421 235 GLY B O   
10797 N N   . ILE B 236 ? 0.1522 0.2219 0.2047 -0.0582 0.0262  -0.0194 236 ILE B N   
10798 C CA  . ILE B 236 ? 0.1912 0.2286 0.2063 -0.0609 0.0348  -0.0157 236 ILE B CA  
10799 C C   . ILE B 236 ? 0.1824 0.2067 0.1992 -0.0488 0.0305  -0.0019 236 ILE B C   
10800 O O   . ILE B 236 ? 0.2124 0.2087 0.2020 -0.0357 0.0234  -0.0134 236 ILE B O   
10801 C CB  . ILE B 236 ? 0.2217 0.2497 0.2170 -0.0455 0.0283  -0.0058 236 ILE B CB  
10802 C CG1 . ILE B 236 ? 0.3245 0.2852 0.2238 -0.0808 0.0241  -0.0249 236 ILE B CG1 
10803 C CG2 . ILE B 236 ? 0.1991 0.1842 0.2269 -0.0319 0.0034  -0.0155 236 ILE B CG2 
10804 C CD1 . ILE B 236 ? 0.3148 0.2681 0.2272 -0.0323 0.0409  -0.0730 236 ILE B CD1 
10816 N N   . VAL B 237 ? 0.1739 0.2199 0.1900 -0.0297 0.0132  -0.0077 237 VAL B N   
10817 C CA  . VAL B 237 ? 0.1787 0.2223 0.1751 -0.0445 0.0159  0.0048  237 VAL B CA  
10818 C C   . VAL B 237 ? 0.1420 0.2341 0.1934 -0.0600 0.0084  0.0000  237 VAL B C   
10819 O O   . VAL B 237 ? 0.1472 0.2176 0.2053 -0.0352 0.0100  -0.0063 237 VAL B O   
10820 C CB  . VAL B 237 ? 0.1708 0.2228 0.1843 -0.0267 0.0279  -0.0048 237 VAL B CB  
10821 C CG1 . VAL B 237 ? 0.1820 0.2289 0.1978 -0.0054 0.0331  -0.0108 237 VAL B CG1 
10822 C CG2 . VAL B 237 ? 0.2249 0.2436 0.2058 -0.0489 0.0160  0.0104  237 VAL B CG2 
10832 N N   . PRO B 238 ? 0.1760 0.2217 0.1911 -0.0556 -0.0012 -0.0051 238 PRO B N   
10833 C CA  . PRO B 238 ? 0.1798 0.1791 0.1928 -0.0081 0.0107  -0.0075 238 PRO B CA  
10834 C C   . PRO B 238 ? 0.1942 0.2120 0.1960 -0.0385 0.0169  0.0014  238 PRO B C   
10835 O O   . PRO B 238 ? 0.2035 0.2196 0.1981 -0.0698 0.0396  -0.0110 238 PRO B O   
10836 C CB  . PRO B 238 ? 0.2198 0.1859 0.1913 -0.0471 0.0097  -0.0150 238 PRO B CB  
10837 C CG  . PRO B 238 ? 0.2371 0.1749 0.1932 -0.0272 -0.0068 0.0109  238 PRO B CG  
10838 C CD  . PRO B 238 ? 0.1916 0.2197 0.1957 -0.0529 0.0107  -0.0043 238 PRO B CD  
10846 N N   . PRO B 239 ? 0.1896 0.2192 0.1997 -0.0954 0.0095  0.0094  239 PRO B N   
10847 C CA  . PRO B 239 ? 0.2020 0.2100 0.1981 -0.0532 -0.0039 0.0135  239 PRO B CA  
10848 C C   . PRO B 239 ? 0.2237 0.2260 0.1856 -0.0595 -0.0004 0.0151  239 PRO B C   
10849 O O   . PRO B 239 ? 0.2605 0.2246 0.1932 -0.0849 0.0338  0.0013  239 PRO B O   
10850 C CB  . PRO B 239 ? 0.2105 0.2618 0.1991 -0.0414 0.0010  0.0020  239 PRO B CB  
10851 C CG  . PRO B 239 ? 0.1650 0.2553 0.1993 -0.0557 0.0156  -0.0195 239 PRO B CG  
10852 C CD  . PRO B 239 ? 0.2011 0.2259 0.2030 -0.0483 0.0106  -0.0087 239 PRO B CD  
10860 N N   . PRO B 240 ? 0.1795 0.2707 0.1750 -0.0509 0.0218  -0.0131 240 PRO B N   
10861 C CA  . PRO B 240 ? 0.2043 0.2952 0.1650 -0.0372 0.0295  0.0035  240 PRO B CA  
10862 C C   . PRO B 240 ? 0.2122 0.3016 0.1694 -0.0468 0.0296  -0.0042 240 PRO B C   
10863 O O   . PRO B 240 ? 0.2291 0.2914 0.1604 -0.0823 0.0324  -0.0134 240 PRO B O   
10864 C CB  . PRO B 240 ? 0.2215 0.3320 0.1755 -0.0379 0.0327  -0.0016 240 PRO B CB  
10865 C CG  . PRO B 240 ? 0.1864 0.3080 0.1738 -0.0211 0.0392  -0.0168 240 PRO B CG  
10866 C CD  . PRO B 240 ? 0.2045 0.3188 0.1790 -0.0299 0.0373  -0.0124 240 PRO B CD  
10874 N N   . GLU B 241 ? 0.2565 0.3331 0.1775 -0.0415 0.0224  0.0202  241 GLU B N   
10875 C CA  . GLU B 241 ? 0.2556 0.3613 0.1884 -0.0538 0.0343  0.0316  241 GLU B CA  
10876 C C   . GLU B 241 ? 0.2194 0.3036 0.1748 -0.0447 0.0345  0.0177  241 GLU B C   
10877 O O   . GLU B 241 ? 0.2433 0.2845 0.1856 -0.0708 0.0267  -0.0157 241 GLU B O   
10878 C CB  . GLU B 241 ? 0.3559 0.4544 0.2241 -0.0701 0.0600  0.0412  241 GLU B CB  
10879 C CG  . GLU B 241 ? 0.4913 0.5971 0.2633 -0.0782 0.1091  0.0661  241 GLU B CG  
10880 C CD  . GLU B 241 ? 0.7132 0.7358 0.3132 -0.0611 0.0955  0.0826  241 GLU B CD  
10881 O OE1 . GLU B 241 ? 0.7529 0.7798 0.3445 -0.0561 0.1083  0.0953  241 GLU B OE1 
10882 O OE2 . GLU B 241 ? 0.8242 0.7989 0.3341 -0.0196 0.0950  0.0695  241 GLU B OE2 
10889 N N   . GLY B 242 ? 0.2615 0.3266 0.1754 -0.0265 0.0212  0.0232  242 GLY B N   
10890 C CA  . GLY B 242 ? 0.2486 0.3058 0.1672 -0.0011 0.0350  0.0197  242 GLY B CA  
10891 C C   . GLY B 242 ? 0.2483 0.2659 0.1723 -0.0340 0.0215  0.0042  242 GLY B C   
10892 O O   . GLY B 242 ? 0.2878 0.2259 0.1829 -0.0215 0.0398  -0.0152 242 GLY B O   
10896 N N   . TYR B 243 ? 0.2423 0.2017 0.1621 -0.0117 0.0175  -0.0080 243 TYR B N   
10897 C CA  . TYR B 243 ? 0.1981 0.2056 0.1600 -0.0363 0.0120  -0.0077 243 TYR B CA  
10898 C C   . TYR B 243 ? 0.2084 0.1921 0.1624 -0.0719 0.0289  0.0112  243 TYR B C   
10899 O O   . TYR B 243 ? 0.2449 0.1753 0.1618 -0.0675 0.0194  -0.0021 243 TYR B O   
10900 C CB  . TYR B 243 ? 0.1633 0.2001 0.1646 0.0093  0.0170  -0.0063 243 TYR B CB  
10901 C CG  . TYR B 243 ? 0.1964 0.1935 0.1658 0.0094  0.0296  0.0034  243 TYR B CG  
10902 C CD1 . TYR B 243 ? 0.2161 0.1859 0.1623 0.0106  0.0160  -0.0133 243 TYR B CD1 
10903 C CD2 . TYR B 243 ? 0.1972 0.1537 0.1650 0.0055  0.0209  -0.0024 243 TYR B CD2 
10904 C CE1 . TYR B 243 ? 0.1854 0.1798 0.1528 -0.0016 0.0057  -0.0342 243 TYR B CE1 
10905 C CE2 . TYR B 243 ? 0.1573 0.1816 0.1652 0.0065  0.0172  -0.0030 243 TYR B CE2 
10906 C CZ  . TYR B 243 ? 0.1661 0.1857 0.1635 0.0129  0.0141  -0.0199 243 TYR B CZ  
10907 O OH  . TYR B 243 ? 0.1800 0.1964 0.1782 -0.0232 0.0307  -0.0197 243 TYR B OH  
10917 N N   . TRP B 244 ? 0.1644 0.1929 0.1817 -0.0210 0.0257  0.0132  244 TRP B N   
10918 C CA  . TRP B 244 ? 0.1824 0.2136 0.1822 -0.0725 0.0193  0.0116  244 TRP B CA  
10919 C C   . TRP B 244 ? 0.2098 0.2213 0.1763 -0.0699 0.0099  0.0050  244 TRP B C   
10920 O O   . TRP B 244 ? 0.2067 0.2495 0.1688 -0.0494 0.0137  0.0095  244 TRP B O   
10921 C CB  . TRP B 244 ? 0.2087 0.1966 0.1698 -0.0492 -0.0210 0.0003  244 TRP B CB  
10922 C CG  . TRP B 244 ? 0.2083 0.1837 0.1660 -0.0386 -0.0094 -0.0089 244 TRP B CG  
10923 C CD1 . TRP B 244 ? 0.2048 0.2342 0.1662 -0.0224 -0.0037 0.0016  244 TRP B CD1 
10924 C CD2 . TRP B 244 ? 0.1882 0.1644 0.1529 -0.0618 -0.0141 0.0018  244 TRP B CD2 
10925 N NE1 . TRP B 244 ? 0.2008 0.2172 0.1500 -0.0415 0.0133  -0.0092 244 TRP B NE1 
10926 C CE2 . TRP B 244 ? 0.1948 0.1856 0.1506 -0.0406 0.0002  0.0050  244 TRP B CE2 
10927 C CE3 . TRP B 244 ? 0.2200 0.2020 0.1576 -0.0503 0.0025  -0.0141 244 TRP B CE3 
10928 C CZ2 . TRP B 244 ? 0.2507 0.1917 0.1553 -0.0571 -0.0159 0.0283  244 TRP B CZ2 
10929 C CZ3 . TRP B 244 ? 0.2123 0.2069 0.1518 -0.0226 -0.0016 -0.0074 244 TRP B CZ3 
10930 C CH2 . TRP B 244 ? 0.2213 0.1962 0.1249 -0.0459 -0.0012 -0.0029 244 TRP B CH2 
10941 N N   A GLU B 245 ? 0.2048 0.2304 0.1721 -0.0717 0.0018  -0.0171 245 GLU B N   
10942 N N   B GLU B 245 ? 0.2135 0.2195 0.1798 -0.0786 0.0128  -0.0192 245 GLU B N   
10943 C CA  A GLU B 245 ? 0.2060 0.2405 0.1704 -0.0661 -0.0071 -0.0088 245 GLU B CA  
10944 C CA  B GLU B 245 ? 0.2240 0.2215 0.1853 -0.0883 0.0140  -0.0142 245 GLU B CA  
10945 C C   A GLU B 245 ? 0.1976 0.2233 0.1786 -0.0391 0.0011  -0.0155 245 GLU B C   
10946 C C   B GLU B 245 ? 0.2097 0.2148 0.1882 -0.0487 0.0111  -0.0195 245 GLU B C   
10947 O O   A GLU B 245 ? 0.1725 0.2393 0.1871 -0.0272 -0.0076 -0.0243 245 GLU B O   
10948 O O   B GLU B 245 ? 0.1983 0.2365 0.2005 -0.0325 0.0003  -0.0303 245 GLU B O   
10949 C CB  A GLU B 245 ? 0.2187 0.2541 0.1668 -0.0407 -0.0292 0.0011  245 GLU B CB  
10950 C CB  B GLU B 245 ? 0.2564 0.2211 0.1933 -0.0846 0.0128  -0.0084 245 GLU B CB  
10951 C CG  A GLU B 245 ? 0.2733 0.2749 0.1804 -0.0197 -0.0535 0.0138  245 GLU B CG  
10952 C CG  B GLU B 245 ? 0.3028 0.2050 0.2163 -0.0778 0.0101  0.0028  245 GLU B CG  
10953 C CD  A GLU B 245 ? 0.3091 0.3323 0.1842 0.0138  -0.0560 0.0145  245 GLU B CD  
10954 C CD  B GLU B 245 ? 0.3139 0.1501 0.2274 -0.0506 -0.0005 0.0060  245 GLU B CD  
10955 O OE1 A GLU B 245 ? 0.4311 0.3696 0.1854 0.0179  -0.0487 0.0137  245 GLU B OE1 
10956 O OE1 B GLU B 245 ? 0.1701 0.1508 0.2236 -0.0522 0.0204  0.0438  245 GLU B OE1 
10957 O OE2 A GLU B 245 ? 0.2938 0.3248 0.1907 0.0146  -0.0794 -0.0025 245 GLU B OE2 
10958 O OE2 B GLU B 245 ? 0.3875 0.1606 0.2406 -0.0909 -0.0236 -0.0275 245 GLU B OE2 
10971 N N   . ALA B 246 ? 0.1889 0.1813 0.1805 -0.0425 0.0152  -0.0040 246 ALA B N   
10972 C CA  . ALA B 246 ? 0.2081 0.1886 0.1836 -0.0884 0.0290  -0.0069 246 ALA B CA  
10973 C C   . ALA B 246 ? 0.2276 0.2229 0.1732 -0.0312 0.0189  -0.0093 246 ALA B C   
10974 O O   . ALA B 246 ? 0.2276 0.2202 0.1778 -0.0252 0.0153  -0.0248 246 ALA B O   
10975 C CB  . ALA B 246 ? 0.2179 0.2448 0.2000 -0.0877 0.0280  -0.0229 246 ALA B CB  
10981 N N   . ILE B 247 ? 0.1844 0.2200 0.1600 -0.0168 0.0090  -0.0138 247 ILE B N   
10982 C CA  . ILE B 247 ? 0.1883 0.2211 0.1488 -0.0979 0.0138  -0.0035 247 ILE B CA  
10983 C C   . ILE B 247 ? 0.2074 0.1927 0.1383 -0.0735 0.0028  0.0129  247 ILE B C   
10984 O O   . ILE B 247 ? 0.1917 0.2002 0.1505 -0.0401 -0.0044 -0.0049 247 ILE B O   
10985 C CB  . ILE B 247 ? 0.1927 0.2233 0.1665 -0.0662 -0.0040 -0.0204 247 ILE B CB  
10986 C CG1 . ILE B 247 ? 0.2330 0.2168 0.1910 -0.0957 -0.0312 -0.0072 247 ILE B CG1 
10987 C CG2 . ILE B 247 ? 0.2336 0.2286 0.1510 -0.0438 0.0190  -0.0339 247 ILE B CG2 
10988 C CD1 . ILE B 247 ? 0.2287 0.2621 0.2055 -0.0828 -0.0551 0.0349  247 ILE B CD1 
11000 N N   . GLN B 248 ? 0.1734 0.2138 0.1388 -0.0532 -0.0202 0.0185  248 GLN B N   
11001 C CA  . GLN B 248 ? 0.1723 0.2041 0.1504 -0.0054 0.0003  0.0213  248 GLN B CA  
11002 C C   . GLN B 248 ? 0.1709 0.2228 0.1607 -0.0340 -0.0080 0.0178  248 GLN B C   
11003 O O   . GLN B 248 ? 0.1879 0.2470 0.1831 -0.0546 0.0014  -0.0048 248 GLN B O   
11004 C CB  . GLN B 248 ? 0.2766 0.1966 0.1543 -0.0336 0.0156  0.0051  248 GLN B CB  
11005 C CG  . GLN B 248 ? 0.2562 0.1735 0.1611 -0.0231 0.0086  0.0004  248 GLN B CG  
11006 C CD  . GLN B 248 ? 0.2442 0.1770 0.1823 -0.0124 -0.0102 -0.0112 248 GLN B CD  
11007 O OE1 . GLN B 248 ? 0.2331 0.1824 0.2108 -0.0191 -0.0038 -0.0005 248 GLN B OE1 
11008 N NE2 . GLN B 248 ? 0.2767 0.1771 0.1924 -0.0151 -0.0015 -0.0168 248 GLN B NE2 
11017 N N   . GLY B 249 ? 0.2117 0.2056 0.1557 -0.0646 -0.0300 0.0307  249 GLY B N   
11018 C CA  . GLY B 249 ? 0.2066 0.1938 0.1715 -0.0662 -0.0562 0.0224  249 GLY B CA  
11019 C C   . GLY B 249 ? 0.1963 0.1820 0.1608 -0.0459 -0.0412 0.0267  249 GLY B C   
11020 O O   . GLY B 249 ? 0.2140 0.1808 0.1678 -0.0274 -0.0473 0.0256  249 GLY B O   
11024 N N   . VAL B 250 ? 0.2216 0.1548 0.1530 -0.0248 -0.0291 0.0010  250 VAL B N   
11025 C CA  . VAL B 250 ? 0.1999 0.1737 0.1555 -0.0182 -0.0035 -0.0047 250 VAL B CA  
11026 C C   . VAL B 250 ? 0.1889 0.1627 0.1565 -0.0197 -0.0112 -0.0080 250 VAL B C   
11027 O O   . VAL B 250 ? 0.2109 0.1552 0.1648 -0.0386 -0.0130 -0.0014 250 VAL B O   
11028 C CB  . VAL B 250 ? 0.2131 0.1939 0.1711 -0.0205 0.0033  0.0283  250 VAL B CB  
11029 C CG1 . VAL B 250 ? 0.2155 0.1894 0.1841 -0.0302 0.0049  0.0224  250 VAL B CG1 
11030 C CG2 . VAL B 250 ? 0.1976 0.2322 0.1832 -0.0137 0.0269  0.0375  250 VAL B CG2 
11040 N N   . LEU B 251 ? 0.1837 0.1901 0.1553 -0.0312 -0.0045 0.0097  251 LEU B N   
11041 C CA  . LEU B 251 ? 0.1908 0.1698 0.1404 -0.0188 0.0155  0.0007  251 LEU B CA  
11042 C C   . LEU B 251 ? 0.1802 0.2035 0.1387 -0.0569 0.0283  0.0034  251 LEU B C   
11043 O O   . LEU B 251 ? 0.1940 0.2204 0.1499 -0.0139 0.0115  -0.0095 251 LEU B O   
11044 C CB  . LEU B 251 ? 0.1811 0.1558 0.1532 -0.0287 -0.0049 -0.0008 251 LEU B CB  
11045 C CG  . LEU B 251 ? 0.1932 0.1410 0.1604 -0.0491 -0.0210 -0.0057 251 LEU B CG  
11046 C CD1 . LEU B 251 ? 0.2266 0.2118 0.1587 -0.0852 0.0041  -0.0251 251 LEU B CD1 
11047 C CD2 . LEU B 251 ? 0.2185 0.1563 0.1741 -0.0369 -0.0054 -0.0001 251 LEU B CD2 
11059 N N   . ALA B 252 ? 0.1778 0.2045 0.1435 -0.0387 0.0103  0.0103  252 ALA B N   
11060 C CA  . ALA B 252 ? 0.1573 0.1909 0.1549 -0.0163 -0.0151 0.0134  252 ALA B CA  
11061 C C   . ALA B 252 ? 0.1991 0.1850 0.1647 0.0031  -0.0091 0.0146  252 ALA B C   
11062 O O   . ALA B 252 ? 0.2227 0.1859 0.1737 0.0184  -0.0194 0.0236  252 ALA B O   
11063 C CB  . ALA B 252 ? 0.1871 0.1725 0.1543 -0.0256 -0.0075 0.0106  252 ALA B CB  
11069 N N   . LYS B 253 ? 0.1943 0.1810 0.1561 0.0282  -0.0184 0.0065  253 LYS B N   
11070 C CA  . LYS B 253 ? 0.2087 0.1508 0.1608 0.0012  -0.0065 0.0145  253 LYS B CA  
11071 C C   . LYS B 253 ? 0.1785 0.1278 0.1609 -0.0123 -0.0252 0.0141  253 LYS B C   
11072 O O   . LYS B 253 ? 0.1974 0.1669 0.1593 -0.0017 -0.0181 -0.0006 253 LYS B O   
11073 C CB  . LYS B 253 ? 0.1771 0.1565 0.1709 0.0085  -0.0241 0.0096  253 LYS B CB  
11074 C CG  . LYS B 253 ? 0.2043 0.1349 0.1862 0.0436  -0.0245 0.0079  253 LYS B CG  
11075 C CD  . LYS B 253 ? 0.2111 0.1504 0.1922 0.0448  -0.0389 -0.0009 253 LYS B CD  
11076 C CE  . LYS B 253 ? 0.2310 0.1948 0.2131 0.0823  -0.0355 -0.0169 253 LYS B CE  
11077 N NZ  . LYS B 253 ? 0.2915 0.2818 0.2098 0.0740  -0.0250 -0.0143 253 LYS B NZ  
11091 N N   . TYR B 254 ? 0.2020 0.1429 0.1685 -0.0362 -0.0348 0.0101  254 TYR B N   
11092 C CA  . TYR B 254 ? 0.1780 0.1478 0.1660 -0.0009 -0.0292 0.0225  254 TYR B CA  
11093 C C   . TYR B 254 ? 0.1919 0.1593 0.1611 -0.0255 0.0010  0.0290  254 TYR B C   
11094 O O   . TYR B 254 ? 0.1805 0.1877 0.1769 0.0030  -0.0062 0.0603  254 TYR B O   
11095 C CB  . TYR B 254 ? 0.1961 0.1624 0.1700 0.0168  -0.0134 0.0331  254 TYR B CB  
11096 C CG  . TYR B 254 ? 0.1764 0.2045 0.1730 0.0058  -0.0045 0.0191  254 TYR B CG  
11097 C CD1 . TYR B 254 ? 0.2097 0.2301 0.1752 0.0085  0.0043  0.0166  254 TYR B CD1 
11098 C CD2 . TYR B 254 ? 0.1402 0.2023 0.1799 0.0377  0.0028  0.0074  254 TYR B CD2 
11099 C CE1 . TYR B 254 ? 0.1469 0.1870 0.1784 -0.0204 0.0026  0.0092  254 TYR B CE1 
11100 C CE2 . TYR B 254 ? 0.1955 0.2033 0.1793 0.0400  -0.0070 0.0242  254 TYR B CE2 
11101 C CZ  . TYR B 254 ? 0.1656 0.1852 0.1830 0.0058  0.0152  -0.0035 254 TYR B CZ  
11102 O OH  . TYR B 254 ? 0.2436 0.2272 0.2036 0.0564  0.0163  0.0154  254 TYR B OH  
11112 N N   . ASP B 255 ? 0.2015 0.1448 0.1500 -0.0127 -0.0061 0.0152  255 ASP B N   
11113 C CA  . ASP B 255 ? 0.2098 0.1453 0.1603 -0.0135 -0.0056 0.0002  255 ASP B CA  
11114 C C   . ASP B 255 ? 0.1710 0.1590 0.1537 0.0231  -0.0117 0.0025  255 ASP B C   
11115 O O   . ASP B 255 ? 0.2218 0.1818 0.1579 -0.0197 -0.0021 -0.0063 255 ASP B O   
11116 C CB  . ASP B 255 ? 0.1938 0.1944 0.1702 -0.0156 -0.0095 -0.0493 255 ASP B CB  
11117 C CG  . ASP B 255 ? 0.2052 0.2063 0.1739 -0.0412 -0.0223 -0.0098 255 ASP B CG  
11118 O OD1 . ASP B 255 ? 0.2412 0.2513 0.1726 -0.0473 -0.0033 -0.0239 255 ASP B OD1 
11119 O OD2 . ASP B 255 ? 0.2090 0.2383 0.1709 -0.0241 -0.0323 -0.0091 255 ASP B OD2 
11124 N N   . VAL B 256 ? 0.1669 0.1490 0.1474 -0.0107 -0.0165 -0.0015 256 VAL B N   
11125 C CA  . VAL B 256 ? 0.1471 0.1475 0.1465 -0.0184 -0.0156 0.0260  256 VAL B CA  
11126 C C   . VAL B 256 ? 0.1919 0.1581 0.1503 -0.0288 0.0149  0.0131  256 VAL B C   
11127 O O   . VAL B 256 ? 0.2512 0.1437 0.1837 -0.0451 0.0189  0.0000  256 VAL B O   
11128 C CB  . VAL B 256 ? 0.1928 0.1574 0.1543 -0.0330 -0.0195 0.0331  256 VAL B CB  
11129 C CG1 . VAL B 256 ? 0.1971 0.1538 0.1591 -0.0595 -0.0025 0.0140  256 VAL B CG1 
11130 C CG2 . VAL B 256 ? 0.2175 0.2386 0.1495 -0.0257 -0.0313 0.0078  256 VAL B CG2 
11140 N N   . LEU B 257 ? 0.1735 0.1705 0.1573 -0.0636 0.0005  0.0230  257 LEU B N   
11141 C CA  . LEU B 257 ? 0.1707 0.1543 0.1730 -0.0387 -0.0327 0.0312  257 LEU B CA  
11142 C C   . LEU B 257 ? 0.1781 0.1549 0.1673 0.0078  -0.0144 0.0216  257 LEU B C   
11143 O O   . LEU B 257 ? 0.2075 0.1378 0.1640 -0.0081 -0.0069 0.0324  257 LEU B O   
11144 C CB  . LEU B 257 ? 0.1736 0.1274 0.1884 -0.0186 -0.0231 -0.0149 257 LEU B CB  
11145 C CG  . LEU B 257 ? 0.1744 0.1462 0.2112 -0.0221 -0.0378 -0.0050 257 LEU B CG  
11146 C CD1 . LEU B 257 ? 0.1843 0.1837 0.2228 -0.0489 -0.0264 -0.0245 257 LEU B CD1 
11147 C CD2 . LEU B 257 ? 0.2309 0.1286 0.2432 0.0117  -0.0184 0.0157  257 LEU B CD2 
11159 N N   . LEU B 258 ? 0.1603 0.1537 0.1693 -0.0264 -0.0115 0.0158  258 LEU B N   
11160 C CA  . LEU B 258 ? 0.1550 0.1642 0.1632 -0.0324 -0.0110 -0.0069 258 LEU B CA  
11161 C C   . LEU B 258 ? 0.1962 0.1462 0.1599 -0.0327 -0.0253 0.0089  258 LEU B C   
11162 O O   . LEU B 258 ? 0.1970 0.1645 0.1485 -0.0257 -0.0180 -0.0043 258 LEU B O   
11163 C CB  . LEU B 258 ? 0.2001 0.2178 0.1558 -0.0264 -0.0134 -0.0187 258 LEU B CB  
11164 C CG  . LEU B 258 ? 0.2348 0.2100 0.1697 -0.0487 -0.0022 -0.0089 258 LEU B CG  
11165 C CD1 . LEU B 258 ? 0.1916 0.2339 0.1945 -0.0870 -0.0117 -0.0051 258 LEU B CD1 
11166 C CD2 . LEU B 258 ? 0.2891 0.2191 0.1762 -0.0750 0.0154  0.0129  258 LEU B CD2 
11178 N N   . ILE B 259 ? 0.1964 0.1258 0.1591 -0.0299 -0.0316 0.0132  259 ILE B N   
11179 C CA  . ILE B 259 ? 0.1530 0.1625 0.1669 -0.0442 -0.0136 0.0032  259 ILE B CA  
11180 C C   . ILE B 259 ? 0.1550 0.1542 0.1603 -0.0781 -0.0022 0.0231  259 ILE B C   
11181 O O   . ILE B 259 ? 0.1871 0.1855 0.1721 -0.0137 0.0036  0.0205  259 ILE B O   
11182 C CB  . ILE B 259 ? 0.1471 0.1435 0.1742 -0.0352 -0.0328 0.0277  259 ILE B CB  
11183 C CG1 . ILE B 259 ? 0.1791 0.1488 0.1691 0.0243  -0.0155 0.0106  259 ILE B CG1 
11184 C CG2 . ILE B 259 ? 0.1822 0.1854 0.1923 -0.0503 -0.0117 0.0242  259 ILE B CG2 
11185 C CD1 . ILE B 259 ? 0.2435 0.1834 0.1831 -0.0347 -0.0316 0.0027  259 ILE B CD1 
11197 N N   . ALA B 260 ? 0.1854 0.1400 0.1539 -0.0728 0.0039  0.0205  260 ALA B N   
11198 C CA  . ALA B 260 ? 0.1798 0.1663 0.1527 -0.0522 -0.0072 0.0045  260 ALA B CA  
11199 C C   . ALA B 260 ? 0.1583 0.1211 0.1521 -0.0298 -0.0031 -0.0085 260 ALA B C   
11200 O O   . ALA B 260 ? 0.1844 0.1562 0.1553 -0.0241 0.0198  -0.0262 260 ALA B O   
11201 C CB  . ALA B 260 ? 0.2141 0.1383 0.1665 -0.0497 -0.0330 -0.0188 260 ALA B CB  
11207 N N   . ASP B 261 ? 0.1315 0.1555 0.1469 -0.0167 0.0029  -0.0315 261 ASP B N   
11208 C CA  . ASP B 261 ? 0.1364 0.1349 0.1416 -0.0400 -0.0207 -0.0229 261 ASP B CA  
11209 C C   . ASP B 261 ? 0.1639 0.1906 0.1424 -0.0719 0.0043  0.0011  261 ASP B C   
11210 O O   . ASP B 261 ? 0.1850 0.1832 0.1298 -0.0628 0.0120  0.0141  261 ASP B O   
11211 C CB  . ASP B 261 ? 0.1689 0.1346 0.1422 -0.0349 -0.0009 0.0150  261 ASP B CB  
11212 C CG  . ASP B 261 ? 0.2008 0.1672 0.1625 -0.0317 -0.0180 -0.0003 261 ASP B CG  
11213 O OD1 . ASP B 261 ? 0.2042 0.1636 0.1635 -0.0274 0.0077  0.0052  261 ASP B OD1 
11214 O OD2 . ASP B 261 ? 0.1992 0.1850 0.1627 -0.0229 -0.0131 -0.0097 261 ASP B OD2 
11219 N N   . GLU B 262 ? 0.1787 0.1617 0.1548 -0.0440 0.0122  0.0080  262 GLU B N   
11220 C CA  . GLU B 262 ? 0.1802 0.1440 0.1527 -0.0493 0.0190  -0.0097 262 GLU B CA  
11221 C C   . GLU B 262 ? 0.2045 0.1623 0.1558 -0.0174 0.0125  0.0130  262 GLU B C   
11222 O O   . GLU B 262 ? 0.1962 0.1385 0.1710 -0.0481 0.0138  0.0324  262 GLU B O   
11223 C CB  . GLU B 262 ? 0.2018 0.1635 0.1550 -0.0059 0.0247  0.0037  262 GLU B CB  
11224 C CG  . GLU B 262 ? 0.1978 0.1847 0.1470 -0.0113 0.0344  0.0088  262 GLU B CG  
11225 C CD  . GLU B 262 ? 0.2347 0.1830 0.1541 -0.0339 0.0231  0.0154  262 GLU B CD  
11226 O OE1 . GLU B 262 ? 0.2190 0.1546 0.1706 -0.0350 0.0113  0.0151  262 GLU B OE1 
11227 O OE2 . GLU B 262 ? 0.2314 0.1993 0.1472 -0.0552 0.0174  0.0106  262 GLU B OE2 
11234 N N   . VAL B 263 ? 0.1731 0.1423 0.1568 -0.0368 0.0169  0.0003  263 VAL B N   
11235 C CA  . VAL B 263 ? 0.1698 0.1599 0.1469 -0.0395 0.0231  -0.0423 263 VAL B CA  
11236 C C   . VAL B 263 ? 0.1711 0.1746 0.1518 -0.0268 -0.0023 -0.0156 263 VAL B C   
11237 O O   . VAL B 263 ? 0.1992 0.1506 0.1557 -0.0195 -0.0193 -0.0080 263 VAL B O   
11238 C CB  . VAL B 263 ? 0.2069 0.1667 0.1485 -0.0270 0.0208  -0.0046 263 VAL B CB  
11239 C CG1 . VAL B 263 ? 0.2303 0.2472 0.1369 -0.0476 0.0209  -0.0010 263 VAL B CG1 
11240 C CG2 . VAL B 263 ? 0.2047 0.2034 0.1523 0.0059  0.0346  -0.0176 263 VAL B CG2 
11250 N N   . VAL B 264 ? 0.2268 0.1606 0.1664 -0.0611 -0.0133 0.0185  264 VAL B N   
11251 C CA  . VAL B 264 ? 0.2249 0.1718 0.1784 -0.0670 -0.0089 -0.0019 264 VAL B CA  
11252 C C   . VAL B 264 ? 0.2113 0.1726 0.1801 -0.0601 -0.0117 0.0053  264 VAL B C   
11253 O O   . VAL B 264 ? 0.2361 0.1748 0.1805 -0.0597 0.0129  -0.0203 264 VAL B O   
11254 C CB  . VAL B 264 ? 0.2203 0.1822 0.1944 -0.1056 0.0076  0.0223  264 VAL B CB  
11255 C CG1 . VAL B 264 ? 0.2885 0.1762 0.2056 -0.1011 0.0016  0.0189  264 VAL B CG1 
11256 C CG2 . VAL B 264 ? 0.2424 0.2048 0.1944 -0.0666 0.0036  0.0461  264 VAL B CG2 
11266 N N   . CYS B 265 ? 0.1759 0.1551 0.1788 -0.0639 -0.0237 0.0237  265 CYS B N   
11267 C CA  . CYS B 265 ? 0.2170 0.1641 0.1872 -0.0529 0.0202  0.0253  265 CYS B CA  
11268 C C   . CYS B 265 ? 0.2271 0.1373 0.2000 -0.0557 0.0259  0.0235  265 CYS B C   
11269 O O   . CYS B 265 ? 0.2446 0.1636 0.2179 -0.0315 0.0414  0.0440  265 CYS B O   
11270 C CB  . CYS B 265 ? 0.2434 0.1427 0.1946 -0.0239 0.0382  -0.0059 265 CYS B CB  
11271 S SG  . CYS B 265 ? 0.2512 0.1994 0.2033 -0.0357 0.0227  -0.0211 265 CYS B SG  
11277 N N   . GLY B 266 ? 0.2561 0.1734 0.2005 -0.0557 0.0221  0.0198  266 GLY B N   
11278 C CA  . GLY B 266 ? 0.2345 0.1216 0.1923 -0.0586 0.0103  0.0051  266 GLY B CA  
11279 C C   . GLY B 266 ? 0.2396 0.1615 0.1873 -0.0665 0.0071  0.0189  266 GLY B C   
11280 O O   . GLY B 266 ? 0.2356 0.1862 0.1963 -0.0567 -0.0023 -0.0001 266 GLY B O   
11284 N N   . PHE B 267 ? 0.2307 0.1645 0.1806 -0.0571 0.0031  0.0220  267 PHE B N   
11285 C CA  . PHE B 267 ? 0.2186 0.1881 0.1827 -0.0401 0.0140  0.0027  267 PHE B CA  
11286 C C   . PHE B 267 ? 0.2396 0.2250 0.1787 -0.0471 0.0359  0.0221  267 PHE B C   
11287 O O   . PHE B 267 ? 0.2757 0.1991 0.1813 -0.0139 0.0128  0.0197  267 PHE B O   
11288 C CB  . PHE B 267 ? 0.1995 0.1992 0.1943 -0.0505 0.0153  -0.0062 267 PHE B CB  
11289 C CG  . PHE B 267 ? 0.1947 0.1763 0.2022 -0.0784 0.0086  0.0177  267 PHE B CG  
11290 C CD1 . PHE B 267 ? 0.2090 0.1812 0.2268 -0.0569 0.0202  0.0083  267 PHE B CD1 
11291 C CD2 . PHE B 267 ? 0.1937 0.1567 0.1893 -0.0550 0.0094  0.0367  267 PHE B CD2 
11292 C CE1 . PHE B 267 ? 0.2281 0.1932 0.2346 -0.0802 0.0237  0.0255  267 PHE B CE1 
11293 C CE2 . PHE B 267 ? 0.2192 0.1579 0.1961 -0.0541 0.0242  0.0027  267 PHE B CE2 
11294 C CZ  . PHE B 267 ? 0.2131 0.1869 0.2156 -0.0813 0.0303  0.0217  267 PHE B CZ  
11304 N N   . GLY B 268 ? 0.2155 0.1872 0.1662 -0.0350 0.0475  0.0223  268 GLY B N   
11305 C CA  . GLY B 268 ? 0.2220 0.1918 0.1877 -0.0857 0.0393  0.0343  268 GLY B CA  
11306 C C   . GLY B 268 ? 0.2336 0.1628 0.1877 -0.0912 0.0191  0.0389  268 GLY B C   
11307 O O   . GLY B 268 ? 0.2414 0.2054 0.1972 -0.0764 0.0141  0.0454  268 GLY B O   
11311 N N   . ARG B 269 ? 0.2261 0.1717 0.1951 -0.0747 0.0093  0.0360  269 ARG B N   
11312 C CA  . ARG B 269 ? 0.2114 0.1885 0.1890 -0.0938 0.0296  0.0098  269 ARG B CA  
11313 C C   . ARG B 269 ? 0.2254 0.1882 0.1913 -0.1048 0.0281  -0.0011 269 ARG B C   
11314 O O   . ARG B 269 ? 0.2286 0.2121 0.2002 -0.0890 0.0548  0.0215  269 ARG B O   
11315 C CB  . ARG B 269 ? 0.2568 0.1591 0.1880 -0.0900 0.0436  0.0046  269 ARG B CB  
11316 C CG  . ARG B 269 ? 0.2179 0.1955 0.1907 -0.0760 0.0174  -0.0260 269 ARG B CG  
11317 C CD  . ARG B 269 ? 0.2254 0.1668 0.1853 -0.0931 -0.0137 -0.0202 269 ARG B CD  
11318 N NE  . ARG B 269 ? 0.2352 0.1660 0.1721 -0.0672 -0.0175 -0.0151 269 ARG B NE  
11319 C CZ  . ARG B 269 ? 0.2085 0.2164 0.1748 -0.1138 0.0148  -0.0318 269 ARG B CZ  
11320 N NH1 . ARG B 269 ? 0.2210 0.2299 0.1818 -0.0400 0.0155  -0.0227 269 ARG B NH1 
11321 N NH2 . ARG B 269 ? 0.2255 0.2178 0.1688 -0.0653 0.0161  -0.0165 269 ARG B NH2 
11335 N N   . ILE B 270 ? 0.2481 0.2349 0.1812 -0.0755 0.0261  -0.0035 270 ILE B N   
11336 C CA  . ILE B 270 ? 0.2432 0.2113 0.1862 -0.0686 0.0166  0.0099  270 ILE B CA  
11337 C C   . ILE B 270 ? 0.2561 0.1374 0.1903 -0.0303 0.0235  0.0011  270 ILE B C   
11338 O O   . ILE B 270 ? 0.2867 0.2058 0.1801 -0.0063 0.0295  -0.0081 270 ILE B O   
11339 C CB  . ILE B 270 ? 0.2131 0.2120 0.1795 -0.0798 -0.0146 0.0048  270 ILE B CB  
11340 C CG1 . ILE B 270 ? 0.2403 0.2024 0.2037 -0.0468 -0.0047 -0.0056 270 ILE B CG1 
11341 C CG2 . ILE B 270 ? 0.2541 0.2820 0.1818 -0.0822 -0.0171 0.0072  270 ILE B CG2 
11342 C CD1 . ILE B 270 ? 0.2510 0.2343 0.2024 -0.0580 0.0353  0.0173  270 ILE B CD1 
11354 N N   . GLY B 271 ? 0.2783 0.1394 0.2102 -0.0553 0.0416  0.0203  271 GLY B N   
11355 C CA  . GLY B 271 ? 0.3019 0.1726 0.2108 -0.0611 0.0290  0.0341  271 GLY B CA  
11356 C C   . GLY B 271 ? 0.3034 0.1702 0.2169 -0.0660 0.0110  0.0285  271 GLY B C   
11357 O O   . GLY B 271 ? 0.3062 0.2308 0.2270 -0.0804 -0.0223 0.0213  271 GLY B O   
11361 N N   . ALA B 272 ? 0.3073 0.1768 0.2193 -0.0726 0.0275  0.0264  272 ALA B N   
11362 C CA  . ALA B 272 ? 0.2968 0.1646 0.2241 -0.0465 0.0242  0.0175  272 ALA B CA  
11363 C C   . ALA B 272 ? 0.2935 0.1872 0.2064 -0.0573 0.0219  0.0154  272 ALA B C   
11364 O O   . ALA B 272 ? 0.3343 0.1886 0.1927 -0.0861 0.0107  0.0205  272 ALA B O   
11365 C CB  . ALA B 272 ? 0.2476 0.1824 0.2351 -0.0634 0.0460  0.0012  272 ALA B CB  
11371 N N   . ASP B 273 ? 0.2817 0.2300 0.2036 -0.0761 0.0264  0.0223  273 ASP B N   
11372 C CA  . ASP B 273 ? 0.3224 0.1897 0.2039 -0.0532 0.0016  0.0209  273 ASP B CA  
11373 C C   . ASP B 273 ? 0.2911 0.1963 0.1876 -0.0520 0.0034  0.0089  273 ASP B C   
11374 O O   . ASP B 273 ? 0.2838 0.1742 0.1910 -0.0426 -0.0030 -0.0229 273 ASP B O   
11375 C CB  . ASP B 273 ? 0.3489 0.2270 0.2440 -0.0695 -0.0076 0.0191  273 ASP B CB  
11376 C CG  . ASP B 273 ? 0.4611 0.2472 0.2714 -0.0502 -0.0169 0.0533  273 ASP B CG  
11377 O OD1 . ASP B 273 ? 0.5372 0.2320 0.3085 -0.0479 -0.0093 0.0491  273 ASP B OD1 
11378 O OD2 . ASP B 273 ? 0.5116 0.2853 0.2740 -0.0222 -0.0223 0.0974  273 ASP B OD2 
11383 N N   . PHE B 274 ? 0.2697 0.1727 0.1805 -0.0694 0.0111  0.0198  274 PHE B N   
11384 C CA  . PHE B 274 ? 0.1993 0.1930 0.1827 -0.0487 0.0145  0.0283  274 PHE B CA  
11385 C C   . PHE B 274 ? 0.2392 0.2270 0.1740 -0.0562 0.0120  0.0089  274 PHE B C   
11386 O O   . PHE B 274 ? 0.2564 0.2651 0.1684 -0.0869 0.0153  0.0057  274 PHE B O   
11387 C CB  . PHE B 274 ? 0.1988 0.1547 0.1838 -0.0599 0.0046  0.0156  274 PHE B CB  
11388 C CG  . PHE B 274 ? 0.2094 0.1850 0.1938 -0.0277 0.0074  0.0199  274 PHE B CG  
11389 C CD1 . PHE B 274 ? 0.2228 0.1971 0.1981 0.0002  0.0297  0.0336  274 PHE B CD1 
11390 C CD2 . PHE B 274 ? 0.2298 0.2077 0.1964 -0.0219 0.0176  0.0198  274 PHE B CD2 
11391 C CE1 . PHE B 274 ? 0.2434 0.2231 0.2148 0.0230  0.0461  0.0402  274 PHE B CE1 
11392 C CE2 . PHE B 274 ? 0.2290 0.2000 0.2065 0.0083  0.0221  0.0233  274 PHE B CE2 
11393 C CZ  . PHE B 274 ? 0.2357 0.2409 0.2165 0.0290  0.0394  0.0262  274 PHE B CZ  
11403 N N   . GLY B 275 ? 0.2340 0.1656 0.1635 -0.0519 0.0121  0.0418  275 GLY B N   
11404 C CA  . GLY B 275 ? 0.2474 0.2324 0.1655 -0.0319 0.0061  0.0049  275 GLY B CA  
11405 C C   . GLY B 275 ? 0.2091 0.1759 0.1690 -0.0060 0.0161  -0.0027 275 GLY B C   
11406 O O   . GLY B 275 ? 0.2304 0.1789 0.1777 0.0042  0.0324  -0.0222 275 GLY B O   
11410 N N   . SER B 276 ? 0.2205 0.1952 0.1736 -0.0183 0.0168  0.0170  276 SER B N   
11411 C CA  . SER B 276 ? 0.2481 0.1836 0.1741 -0.0373 0.0200  0.0258  276 SER B CA  
11412 C C   . SER B 276 ? 0.2749 0.2187 0.1635 -0.0088 0.0156  0.0245  276 SER B C   
11413 O O   . SER B 276 ? 0.2827 0.2351 0.1438 -0.0476 0.0129  -0.0007 276 SER B O   
11414 C CB  . SER B 276 ? 0.2645 0.2019 0.2036 -0.0456 0.0158  0.0094  276 SER B CB  
11415 O OG  . SER B 276 ? 0.2204 0.2088 0.2240 -0.0403 0.0110  -0.0144 276 SER B OG  
11421 N N   . HIS B 277 ? 0.2752 0.2109 0.1669 -0.0296 0.0009  0.0122  277 HIS B N   
11422 C CA  . HIS B 277 ? 0.2798 0.2262 0.1779 -0.0709 0.0075  0.0170  277 HIS B CA  
11423 C C   . HIS B 277 ? 0.2580 0.2696 0.1863 -0.0590 0.0081  0.0270  277 HIS B C   
11424 O O   . HIS B 277 ? 0.2772 0.2906 0.1996 -0.0169 -0.0137 0.0022  277 HIS B O   
11425 C CB  . HIS B 277 ? 0.3314 0.2293 0.1834 -0.0382 -0.0052 0.0199  277 HIS B CB  
11426 C CG  . HIS B 277 ? 0.2749 0.2340 0.1941 -0.0079 0.0023  0.0079  277 HIS B CG  
11427 N ND1 . HIS B 277 ? 0.2435 0.2424 0.2092 -0.0264 0.0008  0.0206  277 HIS B ND1 
11428 C CD2 . HIS B 277 ? 0.2458 0.2185 0.1939 -0.0023 -0.0112 -0.0125 277 HIS B CD2 
11429 C CE1 . HIS B 277 ? 0.2396 0.2505 0.2064 -0.0380 0.0199  -0.0178 277 HIS B CE1 
11430 N NE2 . HIS B 277 ? 0.2717 0.2230 0.2025 -0.0169 0.0018  -0.0122 277 HIS B NE2 
11438 N N   . HIS B 278 ? 0.2454 0.2408 0.1944 -0.0642 0.0203  0.0266  278 HIS B N   
11439 C CA  . HIS B 278 ? 0.1776 0.2014 0.2074 -0.0678 0.0121  0.0157  278 HIS B CA  
11440 C C   . HIS B 278 ? 0.2554 0.2084 0.2009 -0.0533 0.0236  0.0158  278 HIS B C   
11441 O O   . HIS B 278 ? 0.2716 0.2343 0.2088 -0.0494 0.0063  0.0060  278 HIS B O   
11442 C CB  . HIS B 278 ? 0.2097 0.2536 0.2379 -0.0993 0.0121  -0.0011 278 HIS B CB  
11443 C CG  . HIS B 278 ? 0.2399 0.2788 0.2585 -0.1017 0.0462  0.0460  278 HIS B CG  
11444 N ND1 . HIS B 278 ? 0.2845 0.2926 0.2888 -0.0873 0.0472  0.0628  278 HIS B ND1 
11445 C CD2 . HIS B 278 ? 0.2677 0.3090 0.2756 -0.0737 0.0595  0.0537  278 HIS B CD2 
11446 C CE1 . HIS B 278 ? 0.3312 0.3390 0.2987 -0.0552 0.0614  0.0769  278 HIS B CE1 
11447 N NE2 . HIS B 278 ? 0.3062 0.3472 0.2925 -0.0443 0.0623  0.0908  278 HIS B NE2 
11455 N N   . TYR B 279 ? 0.2419 0.2205 0.1836 -0.0576 0.0181  0.0204  279 TYR B N   
11456 C CA  . TYR B 279 ? 0.2036 0.1843 0.1764 -0.0530 -0.0140 0.0239  279 TYR B CA  
11457 C C   . TYR B 279 ? 0.2204 0.2120 0.1929 -0.0839 -0.0015 0.0058  279 TYR B C   
11458 O O   . TYR B 279 ? 0.2795 0.1705 0.2053 -0.0740 -0.0073 -0.0071 279 TYR B O   
11459 C CB  . TYR B 279 ? 0.2118 0.2032 0.1757 -0.0551 0.0229  0.0392  279 TYR B CB  
11460 C CG  . TYR B 279 ? 0.2364 0.1985 0.1845 -0.0724 0.0180  0.0117  279 TYR B CG  
11461 C CD1 . TYR B 279 ? 0.2688 0.2041 0.1927 -0.1038 0.0238  0.0039  279 TYR B CD1 
11462 C CD2 . TYR B 279 ? 0.2493 0.2243 0.1882 -0.0358 0.0138  0.0087  279 TYR B CD2 
11463 C CE1 . TYR B 279 ? 0.2467 0.2563 0.1897 -0.0999 0.0104  0.0180  279 TYR B CE1 
11464 C CE2 . TYR B 279 ? 0.2711 0.2336 0.1986 -0.0618 -0.0013 0.0096  279 TYR B CE2 
11465 C CZ  . TYR B 279 ? 0.2643 0.2355 0.2084 -0.0718 -0.0089 0.0060  279 TYR B CZ  
11466 O OH  . TYR B 279 ? 0.2943 0.2597 0.2209 -0.0700 -0.0325 0.0237  279 TYR B OH  
11476 N N   . ALA B 280 ? 0.2575 0.1999 0.1948 -0.0223 0.0263  0.0084  280 ALA B N   
11477 C CA  . ALA B 280 ? 0.2338 0.2363 0.1876 -0.0028 0.0107  0.0104  280 ALA B CA  
11478 C C   . ALA B 280 ? 0.2383 0.2110 0.1877 -0.0608 -0.0186 -0.0053 280 ALA B C   
11479 O O   . ALA B 280 ? 0.2892 0.2045 0.1635 -0.0846 -0.0169 0.0093  280 ALA B O   
11480 C CB  . ALA B 280 ? 0.2584 0.3087 0.1901 -0.0157 0.0005  0.0062  280 ALA B CB  
11486 N N   . ILE B 281 ? 0.2410 0.1654 0.1822 -0.0397 0.0010  0.0112  281 ILE B N   
11487 C CA  . ILE B 281 ? 0.2309 0.2152 0.1686 -0.0305 0.0024  0.0147  281 ILE B CA  
11488 C C   . ILE B 281 ? 0.2308 0.1845 0.1676 -0.0420 0.0171  0.0009  281 ILE B C   
11489 O O   . ILE B 281 ? 0.2376 0.2085 0.1880 -0.0391 0.0050  -0.0113 281 ILE B O   
11490 C CB  . ILE B 281 ? 0.2113 0.1914 0.1679 -0.0277 -0.0185 0.0439  281 ILE B CB  
11491 C CG1 . ILE B 281 ? 0.2065 0.2671 0.1712 -0.0563 -0.0162 0.0063  281 ILE B CG1 
11492 C CG2 . ILE B 281 ? 0.2155 0.1694 0.1804 -0.0308 -0.0006 0.0476  281 ILE B CG2 
11493 C CD1 . ILE B 281 ? 0.2121 0.2393 0.1731 0.0098  -0.0113 -0.0081 281 ILE B CD1 
11505 N N   . LYS B 282 ? 0.2304 0.1508 0.1701 -0.0298 -0.0152 0.0079  282 LYS B N   
11506 C CA  . LYS B 282 ? 0.2555 0.1888 0.1728 -0.0188 -0.0229 0.0146  282 LYS B CA  
11507 C C   . LYS B 282 ? 0.2007 0.2090 0.1633 -0.0271 -0.0228 -0.0050 282 LYS B C   
11508 O O   . LYS B 282 ? 0.2552 0.2070 0.1705 -0.0465 -0.0153 -0.0068 282 LYS B O   
11509 C CB  . LYS B 282 ? 0.3343 0.1709 0.1627 -0.0531 -0.0159 0.0197  282 LYS B CB  
11510 C CG  . LYS B 282 ? 0.4480 0.2346 0.1809 -0.0369 -0.0476 -0.0085 282 LYS B CG  
11511 C CD  . LYS B 282 ? 0.6010 0.2866 0.2298 -0.0849 -0.0649 -0.0318 282 LYS B CD  
11512 C CE  . LYS B 282 ? 0.6971 0.3325 0.2734 -0.0385 -0.0890 -0.0675 282 LYS B CE  
11513 N NZ  . LYS B 282 ? 0.7277 0.3535 0.2960 0.0262  -0.0920 -0.0905 282 LYS B NZ  
11527 N N   . PRO B 283 ? 0.2105 0.1569 0.1525 -0.0450 -0.0106 -0.0016 283 PRO B N   
11528 C CA  . PRO B 283 ? 0.2057 0.1877 0.1453 -0.0015 0.0030  -0.0003 283 PRO B CA  
11529 C C   . PRO B 283 ? 0.1941 0.1835 0.1496 -0.0259 -0.0146 0.0132  283 PRO B C   
11530 O O   . PRO B 283 ? 0.2289 0.1969 0.1863 -0.0307 -0.0254 0.0101  283 PRO B O   
11531 C CB  . PRO B 283 ? 0.1951 0.2126 0.1521 -0.0359 -0.0068 0.0313  283 PRO B CB  
11532 C CG  . PRO B 283 ? 0.2126 0.1784 0.1541 0.0013  -0.0022 0.0295  283 PRO B CG  
11533 C CD  . PRO B 283 ? 0.2230 0.1638 0.1571 -0.0293 -0.0070 0.0200  283 PRO B CD  
11541 N N   . ASP B 284 ? 0.1880 0.1428 0.1550 -0.0158 -0.0019 0.0256  284 ASP B N   
11542 C CA  . ASP B 284 ? 0.1627 0.1662 0.1766 -0.0283 -0.0207 -0.0090 284 ASP B CA  
11543 C C   . ASP B 284 ? 0.1558 0.1506 0.1694 -0.0139 -0.0239 -0.0028 284 ASP B C   
11544 O O   . ASP B 284 ? 0.1883 0.1313 0.1777 -0.0004 -0.0324 0.0236  284 ASP B O   
11545 C CB  . ASP B 284 ? 0.2264 0.1782 0.1862 -0.0331 -0.0602 -0.0142 284 ASP B CB  
11546 C CG  . ASP B 284 ? 0.3002 0.1690 0.1859 -0.0365 -0.0983 -0.0097 284 ASP B CG  
11547 O OD1 . ASP B 284 ? 0.3407 0.2689 0.1977 0.0116  -0.1012 -0.0073 284 ASP B OD1 
11548 O OD2 . ASP B 284 ? 0.3197 0.1026 0.1916 -0.0207 -0.0746 0.0057  284 ASP B OD2 
11553 N N   . LEU B 285 ? 0.1549 0.1549 0.1673 -0.0186 -0.0103 0.0028  285 LEU B N   
11554 C CA  . LEU B 285 ? 0.1644 0.1209 0.1638 -0.0318 0.0141  0.0060  285 LEU B CA  
11555 C C   . LEU B 285 ? 0.1746 0.1412 0.1522 -0.0425 -0.0049 -0.0012 285 LEU B C   
11556 O O   . LEU B 285 ? 0.1642 0.1937 0.1508 -0.0485 -0.0159 0.0066  285 LEU B O   
11557 C CB  . LEU B 285 ? 0.1679 0.1423 0.1667 -0.0101 0.0101  -0.0216 285 LEU B CB  
11558 C CG  . LEU B 285 ? 0.1694 0.1513 0.1683 -0.0046 0.0011  0.0006  285 LEU B CG  
11559 C CD1 . LEU B 285 ? 0.1530 0.1440 0.1840 -0.0237 -0.0062 -0.0128 285 LEU B CD1 
11560 C CD2 . LEU B 285 ? 0.2039 0.1596 0.1842 -0.0219 -0.0009 -0.0065 285 LEU B CD2 
11572 N N   . ILE B 286 ? 0.1985 0.1740 0.1579 -0.0203 0.0108  0.0042  286 ILE B N   
11573 C CA  . ILE B 286 ? 0.1756 0.1530 0.1574 -0.0510 0.0249  0.0078  286 ILE B CA  
11574 C C   . ILE B 286 ? 0.1311 0.1535 0.1513 -0.0715 -0.0076 -0.0026 286 ILE B C   
11575 O O   . ILE B 286 ? 0.1879 0.1661 0.1674 -0.0207 -0.0141 0.0049  286 ILE B O   
11576 C CB  . ILE B 286 ? 0.1857 0.1281 0.1570 -0.0431 0.0095  0.0125  286 ILE B CB  
11577 C CG1 . ILE B 286 ? 0.2289 0.1511 0.1613 -0.0307 0.0312  0.0149  286 ILE B CG1 
11578 C CG2 . ILE B 286 ? 0.1880 0.1596 0.1611 -0.0085 0.0161  0.0392  286 ILE B CG2 
11579 C CD1 . ILE B 286 ? 0.2460 0.1578 0.1651 -0.0341 0.0142  0.0329  286 ILE B CD1 
11591 N N   . THR B 287 ? 0.1372 0.1440 0.1513 -0.0333 -0.0129 -0.0009 287 THR B N   
11592 C CA  . THR B 287 ? 0.1613 0.1257 0.1519 -0.0332 -0.0014 0.0124  287 THR B CA  
11593 C C   . THR B 287 ? 0.1868 0.1621 0.1606 -0.0488 -0.0150 0.0091  287 THR B C   
11594 O O   . THR B 287 ? 0.1908 0.1514 0.1691 -0.0750 0.0062  -0.0165 287 THR B O   
11595 C CB  . THR B 287 ? 0.1341 0.1497 0.1647 -0.0263 0.0229  0.0052  287 THR B CB  
11596 O OG1 . THR B 287 ? 0.2098 0.1544 0.1769 -0.0303 -0.0234 0.0290  287 THR B OG1 
11597 C CG2 . THR B 287 ? 0.1865 0.1207 0.1699 -0.0328 0.0192  -0.0086 287 THR B CG2 
11605 N N   . ILE B 288 ? 0.1812 0.1332 0.1579 -0.0396 0.0173  0.0255  288 ILE B N   
11606 C CA  . ILE B 288 ? 0.1832 0.1456 0.1629 -0.0270 0.0127  0.0265  288 ILE B CA  
11607 C C   . ILE B 288 ? 0.2152 0.1602 0.1542 -0.0523 -0.0032 0.0093  288 ILE B C   
11608 O O   . ILE B 288 ? 0.1974 0.1408 0.1576 -0.0348 0.0070  -0.0027 288 ILE B O   
11609 C CB  . ILE B 288 ? 0.1678 0.1098 0.1595 -0.0434 0.0192  0.0132  288 ILE B CB  
11610 C CG1 . ILE B 288 ? 0.2011 0.0787 0.1676 -0.0339 0.0062  -0.0072 288 ILE B CG1 
11611 C CG2 . ILE B 288 ? 0.2312 0.1298 0.1706 -0.0328 0.0143  0.0136  288 ILE B CG2 
11612 C CD1 . ILE B 288 ? 0.2248 0.1066 0.1741 -0.0009 0.0105  -0.0100 288 ILE B CD1 
11624 N N   . ALA B 289 ? 0.2191 0.1001 0.1557 -0.0111 0.0021  -0.0081 289 ALA B N   
11625 C CA  . ALA B 289 ? 0.1993 0.1294 0.1588 -0.0371 -0.0090 -0.0062 289 ALA B CA  
11626 C C   . ALA B 289 ? 0.2098 0.1624 0.1813 -0.0450 -0.0014 -0.0367 289 ALA B C   
11627 O O   . ALA B 289 ? 0.2399 0.2162 0.1815 -0.0618 -0.0079 -0.0081 289 ALA B O   
11628 C CB  . ALA B 289 ? 0.2179 0.1969 0.1647 -0.0599 -0.0329 -0.0200 289 ALA B CB  
11634 N N   . LYS B 290 ? 0.2391 0.1633 0.1978 -0.0585 0.0022  -0.0338 290 LYS B N   
11635 C CA  . LYS B 290 ? 0.2094 0.1777 0.2332 -0.0522 -0.0066 -0.0278 290 LYS B CA  
11636 C C   . LYS B 290 ? 0.2257 0.1555 0.2239 -0.0687 0.0136  -0.0529 290 LYS B C   
11637 O O   . LYS B 290 ? 0.2258 0.1352 0.2379 -0.0597 0.0147  -0.0345 290 LYS B O   
11638 C CB  . LYS B 290 ? 0.1993 0.1812 0.3136 -0.0482 -0.0128 -0.0206 290 LYS B CB  
11639 C CG  . LYS B 290 ? 0.1883 0.2467 0.4124 -0.1025 -0.0032 -0.0493 290 LYS B CG  
11640 C CD  . LYS B 290 ? 0.2892 0.3773 0.5498 -0.1265 0.0044  -0.1024 290 LYS B CD  
11641 C CE  . LYS B 290 ? 0.4530 0.5103 0.6837 -0.2130 0.0437  -0.1220 290 LYS B CE  
11642 N NZ  . LYS B 290 ? 0.6738 0.6874 0.8441 -0.1519 0.0446  -0.1098 290 LYS B NZ  
11654 N N   . GLY B 291 ? 0.2230 0.1862 0.2140 -0.0757 0.0184  -0.0478 291 GLY B N   
11655 C CA  . GLY B 291 ? 0.2310 0.1877 0.2058 -0.0745 0.0313  -0.0409 291 GLY B CA  
11656 C C   . GLY B 291 ? 0.2567 0.1468 0.2041 -0.0875 0.0273  -0.0091 291 GLY B C   
11657 O O   . GLY B 291 ? 0.2516 0.1701 0.2292 -0.0460 0.0428  0.0145  291 GLY B O   
11661 N N   . LEU B 292 ? 0.2335 0.1745 0.1886 -0.0593 0.0441  -0.0146 292 LEU B N   
11662 C CA  . LEU B 292 ? 0.2222 0.1625 0.1712 -0.0715 -0.0047 0.0015  292 LEU B CA  
11663 C C   . LEU B 292 ? 0.2135 0.1363 0.1824 -0.0170 -0.0001 -0.0065 292 LEU B C   
11664 O O   . LEU B 292 ? 0.2500 0.1355 0.1849 -0.0071 -0.0105 -0.0152 292 LEU B O   
11665 C CB  . LEU B 292 ? 0.2453 0.2099 0.1687 -0.0711 -0.0251 -0.0101 292 LEU B CB  
11666 C CG  . LEU B 292 ? 0.2370 0.2058 0.1696 -0.0588 -0.0127 -0.0079 292 LEU B CG  
11667 C CD1 . LEU B 292 ? 0.2446 0.2337 0.1760 -0.0140 -0.0152 0.0120  292 LEU B CD1 
11668 C CD2 . LEU B 292 ? 0.2449 0.2439 0.1780 -0.0773 -0.0203 -0.0217 292 LEU B CD2 
11680 N N   . THR B 293 ? 0.2164 0.1279 0.1993 -0.0527 0.0063  -0.0047 293 THR B N   
11681 C CA  . THR B 293 ? 0.1833 0.1198 0.1875 -0.0360 0.0054  -0.0046 293 THR B CA  
11682 C C   . THR B 293 ? 0.2386 0.1154 0.1818 -0.0136 0.0134  0.0176  293 THR B C   
11683 O O   . THR B 293 ? 0.1973 0.1625 0.1902 -0.0476 0.0091  -0.0022 293 THR B O   
11684 C CB  . THR B 293 ? 0.2232 0.1131 0.2158 -0.0825 0.0060  0.0161  293 THR B CB  
11685 O OG1 . THR B 293 ? 0.2155 0.1496 0.2119 -0.0419 -0.0041 -0.0054 293 THR B OG1 
11686 C CG2 . THR B 293 ? 0.2618 0.1274 0.2225 -0.0586 0.0154  0.0189  293 THR B CG2 
11694 N N   . SER B 294 ? 0.2488 0.1535 0.1697 -0.0366 0.0079  0.0059  294 SER B N   
11695 C CA  . SER B 294 ? 0.2241 0.1517 0.1734 -0.0427 0.0207  0.0349  294 SER B CA  
11696 C C   . SER B 294 ? 0.1896 0.1556 0.1766 -0.0837 0.0113  0.0312  294 SER B C   
11697 O O   . SER B 294 ? 0.1936 0.1992 0.1830 -0.0927 0.0054  0.0215  294 SER B O   
11698 C CB  . SER B 294 ? 0.2384 0.1679 0.1811 -0.0393 0.0107  0.0034  294 SER B CB  
11699 O OG  . SER B 294 ? 0.2141 0.1671 0.1846 -0.0549 0.0060  -0.0220 294 SER B OG  
11705 N N   . ALA B 295 ? 0.2305 0.1071 0.1891 -0.0175 0.0078  0.0407  295 ALA B N   
11706 C CA  . ALA B 295 ? 0.1925 0.1584 0.1912 -0.0202 -0.0061 0.0140  295 ALA B CA  
11707 C C   . ALA B 295 ? 0.2067 0.1737 0.1762 -0.0316 0.0054  0.0089  295 ALA B C   
11708 O O   . ALA B 295 ? 0.2224 0.1833 0.1704 -0.0259 0.0161  0.0135  295 ALA B O   
11709 C CB  . ALA B 295 ? 0.2055 0.1564 0.1892 -0.0119 -0.0281 0.0298  295 ALA B CB  
11715 N N   . TYR B 296 ? 0.2114 0.1314 0.1655 -0.0541 0.0012  0.0062  296 TYR B N   
11716 C CA  . TYR B 296 ? 0.2033 0.1590 0.1754 -0.0428 -0.0070 -0.0195 296 TYR B CA  
11717 C C   . TYR B 296 ? 0.2119 0.1624 0.1670 -0.0775 0.0036  0.0028  296 TYR B C   
11718 O O   . TYR B 296 ? 0.2407 0.1595 0.1703 -0.0676 0.0189  -0.0019 296 TYR B O   
11719 C CB  . TYR B 296 ? 0.2107 0.1610 0.1803 -0.0337 -0.0171 -0.0174 296 TYR B CB  
11720 C CG  . TYR B 296 ? 0.2179 0.1271 0.1846 -0.0599 0.0131  0.0064  296 TYR B CG  
11721 C CD1 . TYR B 296 ? 0.2179 0.1158 0.1865 -0.0636 0.0100  0.0086  296 TYR B CD1 
11722 C CD2 . TYR B 296 ? 0.1963 0.1335 0.1949 -0.0632 0.0104  -0.0114 296 TYR B CD2 
11723 C CE1 . TYR B 296 ? 0.2116 0.1449 0.1800 -0.0818 0.0334  -0.0133 296 TYR B CE1 
11724 C CE2 . TYR B 296 ? 0.2151 0.1837 0.1994 -0.0951 -0.0110 -0.0312 296 TYR B CE2 
11725 C CZ  . TYR B 296 ? 0.2163 0.1276 0.1994 -0.0836 0.0182  -0.0229 296 TYR B CZ  
11726 O OH  . TYR B 296 ? 0.2244 0.2062 0.2104 -0.0477 0.0003  0.0102  296 TYR B OH  
11736 N N   . GLN B 297 ? 0.1862 0.1463 0.1608 -0.0361 0.0025  0.0206  297 GLN B N   
11737 C CA  . GLN B 297 ? 0.1643 0.1823 0.1721 -0.0756 -0.0033 0.0148  297 GLN B CA  
11738 C C   . GLN B 297 ? 0.1964 0.1907 0.1758 -0.0426 0.0051  0.0057  297 GLN B C   
11739 O O   . GLN B 297 ? 0.1969 0.2034 0.1731 -0.0425 0.0008  0.0073  297 GLN B O   
11740 C CB  . GLN B 297 ? 0.1552 0.1535 0.1868 -0.0632 -0.0044 0.0042  297 GLN B CB  
11741 C CG  . GLN B 297 ? 0.1835 0.1392 0.1913 -0.0146 -0.0220 -0.0166 297 GLN B CG  
11742 C CD  . GLN B 297 ? 0.1851 0.1331 0.1915 0.0037  -0.0167 -0.0226 297 GLN B CD  
11743 O OE1 . GLN B 297 ? 0.1926 0.1843 0.1944 -0.0184 0.0034  -0.0060 297 GLN B OE1 
11744 N NE2 . GLN B 297 ? 0.1786 0.1638 0.1933 -0.0249 -0.0205 0.0157  297 GLN B NE2 
11753 N N   . PRO B 298 ? 0.1734 0.1631 0.1692 -0.0508 0.0208  -0.0046 298 PRO B N   
11754 C CA  . PRO B 298 ? 0.1667 0.1602 0.1782 -0.0379 0.0037  0.0001  298 PRO B CA  
11755 C C   . PRO B 298 ? 0.1644 0.2904 0.2028 0.0032  0.0143  -0.0386 298 PRO B C   
11756 O O   . PRO B 298 ? 0.2061 0.5745 0.2318 0.0132  0.0020  -0.1223 298 PRO B O   
11757 C CB  . PRO B 298 ? 0.2530 0.1781 0.1739 -0.0143 0.0077  0.0036  298 PRO B CB  
11758 C CG  . PRO B 298 ? 0.3328 0.1993 0.1656 -0.0420 0.0162  0.0058  298 PRO B CG  
11759 C CD  . PRO B 298 ? 0.2305 0.1817 0.1691 -0.0379 0.0203  0.0095  298 PRO B CD  
11767 N N   . LEU B 299 ? 0.1352 0.1763 0.1849 -0.0448 0.0048  -0.0003 299 LEU B N   
11768 C CA  . LEU B 299 ? 0.1308 0.1438 0.1749 0.0260  -0.0073 0.0045  299 LEU B CA  
11769 C C   . LEU B 299 ? 0.1715 0.1458 0.1698 -0.0676 0.0215  0.0168  299 LEU B C   
11770 O O   . LEU B 299 ? 0.2157 0.2109 0.1820 -0.0715 0.0403  -0.0154 299 LEU B O   
11771 C CB  . LEU B 299 ? 0.1749 0.1426 0.1774 0.0328  -0.0172 -0.0098 299 LEU B CB  
11772 C CG  . LEU B 299 ? 0.1601 0.1644 0.1772 -0.0081 -0.0039 0.0246  299 LEU B CG  
11773 C CD1 . LEU B 299 ? 0.1994 0.2204 0.1890 -0.0298 0.0130  0.0323  299 LEU B CD1 
11774 C CD2 . LEU B 299 ? 0.2089 0.1604 0.1953 -0.0143 0.0053  0.0155  299 LEU B CD2 
11786 N N   . SER B 300 ? 0.1768 0.1415 0.1546 -0.0365 0.0108  0.0090  300 SER B N   
11787 C CA  . SER B 300 ? 0.1666 0.1084 0.1615 -0.0294 0.0046  -0.0010 300 SER B CA  
11788 C C   . SER B 300 ? 0.1484 0.1005 0.1673 -0.0149 0.0210  0.0056  300 SER B C   
11789 O O   . SER B 300 ? 0.1632 0.1691 0.1706 -0.0262 0.0130  -0.0109 300 SER B O   
11790 C CB  . SER B 300 ? 0.1887 0.1479 0.1664 -0.0280 -0.0081 0.0022  300 SER B CB  
11791 O OG  . SER B 300 ? 0.1932 0.1675 0.1560 -0.0489 -0.0007 0.0004  300 SER B OG  
11797 N N   . GLY B 301 ? 0.1771 0.0969 0.1746 -0.0323 -0.0117 0.0084  301 GLY B N   
11798 C CA  . GLY B 301 ? 0.2001 0.1150 0.1572 -0.0104 -0.0155 0.0142  301 GLY B CA  
11799 C C   . GLY B 301 ? 0.1748 0.1346 0.1664 -0.0113 -0.0136 0.0040  301 GLY B C   
11800 O O   . GLY B 301 ? 0.1617 0.1762 0.1567 -0.0123 -0.0089 -0.0020 301 GLY B O   
11804 N N   . VAL B 302 ? 0.1960 0.1066 0.1618 -0.0180 -0.0119 0.0160  302 VAL B N   
11805 C CA  . VAL B 302 ? 0.1941 0.0729 0.1582 0.0063  0.0117  0.0148  302 VAL B CA  
11806 C C   . VAL B 302 ? 0.1624 0.1236 0.1507 0.0261  -0.0117 0.0170  302 VAL B C   
11807 O O   . VAL B 302 ? 0.1889 0.1773 0.1485 0.0110  0.0092  0.0290  302 VAL B O   
11808 C CB  . VAL B 302 ? 0.1943 0.0694 0.1736 -0.0229 -0.0114 0.0204  302 VAL B CB  
11809 C CG1 . VAL B 302 ? 0.2272 0.1238 0.1620 -0.0464 -0.0256 0.0029  302 VAL B CG1 
11810 C CG2 . VAL B 302 ? 0.2039 0.1321 0.1927 -0.0185 0.0075  0.0525  302 VAL B CG2 
11820 N N   . ILE B 303 ? 0.1666 0.1421 0.1545 0.0017  -0.0249 0.0159  303 ILE B N   
11821 C CA  . ILE B 303 ? 0.1558 0.1309 0.1569 -0.0204 -0.0160 0.0078  303 ILE B CA  
11822 C C   . ILE B 303 ? 0.1721 0.1320 0.1585 -0.0194 -0.0010 0.0080  303 ILE B C   
11823 O O   . ILE B 303 ? 0.1725 0.1674 0.1628 -0.0057 0.0084  -0.0007 303 ILE B O   
11824 C CB  . ILE B 303 ? 0.1542 0.1482 0.1537 -0.0129 -0.0183 0.0039  303 ILE B CB  
11825 C CG1 . ILE B 303 ? 0.1587 0.1720 0.1720 -0.0315 0.0101  0.0141  303 ILE B CG1 
11826 C CG2 . ILE B 303 ? 0.1797 0.1879 0.1750 -0.0152 -0.0169 -0.0134 303 ILE B CG2 
11827 C CD1 . ILE B 303 ? 0.2111 0.1537 0.1706 -0.0202 -0.0146 0.0114  303 ILE B CD1 
11839 N N   . ILE B 304 ? 0.1732 0.1677 0.1621 -0.0126 -0.0090 0.0013  304 ILE B N   
11840 C CA  . ILE B 304 ? 0.2109 0.1756 0.1493 -0.0224 -0.0343 -0.0004 304 ILE B CA  
11841 C C   . ILE B 304 ? 0.1956 0.1791 0.1641 -0.0303 -0.0309 -0.0003 304 ILE B C   
11842 O O   . ILE B 304 ? 0.2019 0.1435 0.1629 -0.0086 -0.0195 -0.0057 304 ILE B O   
11843 C CB  . ILE B 304 ? 0.1919 0.1959 0.1409 -0.0292 -0.0322 0.0110  304 ILE B CB  
11844 C CG1 . ILE B 304 ? 0.2212 0.1619 0.1458 -0.0296 -0.0179 -0.0040 304 ILE B CG1 
11845 C CG2 . ILE B 304 ? 0.2034 0.2372 0.1357 -0.0545 -0.0038 -0.0233 304 ILE B CG2 
11846 C CD1 . ILE B 304 ? 0.2331 0.1883 0.1651 -0.0361 0.0020  0.0086  304 ILE B CD1 
11858 N N   . GLY B 305 ? 0.1781 0.1550 0.1664 -0.0268 -0.0163 0.0142  305 GLY B N   
11859 C CA  . GLY B 305 ? 0.2083 0.1776 0.1639 -0.0320 -0.0276 0.0266  305 GLY B CA  
11860 C C   . GLY B 305 ? 0.2333 0.1786 0.1512 -0.0219 -0.0384 0.0289  305 GLY B C   
11861 O O   . GLY B 305 ? 0.2196 0.1864 0.1366 -0.0092 -0.0271 0.0229  305 GLY B O   
11865 N N   . ASP B 306 ? 0.2184 0.2220 0.1572 -0.0057 -0.0266 0.0203  306 ASP B N   
11866 C CA  . ASP B 306 ? 0.2243 0.2026 0.1537 0.0000  -0.0262 0.0181  306 ASP B CA  
11867 C C   . ASP B 306 ? 0.1629 0.1715 0.1643 0.0549  -0.0196 0.0176  306 ASP B C   
11868 O O   . ASP B 306 ? 0.1939 0.2279 0.1719 0.0229  -0.0324 0.0078  306 ASP B O   
11869 C CB  . ASP B 306 ? 0.2744 0.2418 0.1660 0.0416  -0.0086 0.0335  306 ASP B CB  
11870 C CG  . ASP B 306 ? 0.3599 0.2719 0.1947 0.0273  0.0229  0.0298  306 ASP B CG  
11871 O OD1 . ASP B 306 ? 0.3946 0.2490 0.2244 0.0368  -0.0070 0.0110  306 ASP B OD1 
11872 O OD2 . ASP B 306 ? 0.4275 0.3357 0.2357 0.0183  0.0560  0.0652  306 ASP B OD2 
11877 N N   . ARG B 307 ? 0.1697 0.1706 0.1824 0.0258  -0.0374 0.0123  307 ARG B N   
11878 C CA  . ARG B 307 ? 0.2416 0.1925 0.2102 -0.0369 -0.0036 -0.0159 307 ARG B CA  
11879 C C   . ARG B 307 ? 0.2029 0.1205 0.1954 -0.0628 -0.0477 -0.0234 307 ARG B C   
11880 O O   . ARG B 307 ? 0.2187 0.1877 0.2018 -0.0124 -0.0317 -0.0044 307 ARG B O   
11881 C CB  . ARG B 307 ? 0.3753 0.2579 0.2757 0.0127  0.0004  -0.0286 307 ARG B CB  
11882 C CG  . ARG B 307 ? 0.4944 0.3529 0.3017 0.0070  -0.0172 -0.0248 307 ARG B CG  
11883 C CD  . ARG B 307 ? 0.5692 0.3844 0.3379 0.0120  -0.0445 -0.0349 307 ARG B CD  
11884 N NE  . ARG B 307 ? 0.6496 0.3606 0.3587 0.0031  -0.0422 -0.0563 307 ARG B NE  
11885 C CZ  . ARG B 307 ? 0.7147 0.3249 0.3657 -0.0350 -0.0598 -0.0681 307 ARG B CZ  
11886 N NH1 . ARG B 307 ? 0.7095 0.2793 0.3687 -0.1327 -0.1096 -0.0578 307 ARG B NH1 
11887 N NH2 . ARG B 307 ? 0.7423 0.3209 0.3696 -0.0730 -0.0301 -0.0729 307 ARG B NH2 
11901 N N   . VAL B 308 ? 0.1891 0.1241 0.1794 -0.0690 -0.0341 -0.0143 308 VAL B N   
11902 C CA  . VAL B 308 ? 0.2000 0.1771 0.1711 0.0042  -0.0442 0.0048  308 VAL B CA  
11903 C C   . VAL B 308 ? 0.1998 0.1556 0.1709 0.0206  -0.0246 0.0210  308 VAL B C   
11904 O O   . VAL B 308 ? 0.1956 0.1671 0.1772 -0.0201 -0.0208 0.0071  308 VAL B O   
11905 C CB  . VAL B 308 ? 0.1791 0.2052 0.1621 -0.0042 -0.0420 -0.0225 308 VAL B CB  
11906 C CG1 . VAL B 308 ? 0.2135 0.1982 0.1696 0.0039  -0.0551 -0.0071 308 VAL B CG1 
11907 C CG2 . VAL B 308 ? 0.1982 0.2164 0.1725 0.0252  -0.0500 -0.0114 308 VAL B CG2 
11917 N N   . TRP B 309 ? 0.1973 0.1865 0.1604 -0.0105 -0.0246 0.0224  309 TRP B N   
11918 C CA  . TRP B 309 ? 0.2111 0.1765 0.1602 -0.0354 -0.0309 0.0116  309 TRP B CA  
11919 C C   . TRP B 309 ? 0.2114 0.1878 0.1623 -0.0114 -0.0233 -0.0084 309 TRP B C   
11920 O O   . TRP B 309 ? 0.2301 0.1662 0.1678 0.0108  -0.0254 0.0132  309 TRP B O   
11921 C CB  . TRP B 309 ? 0.2494 0.1565 0.1644 -0.0117 -0.0163 0.0111  309 TRP B CB  
11922 C CG  . TRP B 309 ? 0.2519 0.1323 0.1788 -0.0329 -0.0331 0.0292  309 TRP B CG  
11923 C CD1 . TRP B 309 ? 0.2520 0.1337 0.1865 -0.0317 -0.0408 0.0222  309 TRP B CD1 
11924 C CD2 . TRP B 309 ? 0.2309 0.1681 0.1642 0.0110  -0.0274 0.0154  309 TRP B CD2 
11925 N NE1 . TRP B 309 ? 0.1974 0.1733 0.1744 -0.0009 -0.0295 0.0190  309 TRP B NE1 
11926 C CE2 . TRP B 309 ? 0.2058 0.1462 0.1596 0.0040  -0.0334 0.0028  309 TRP B CE2 
11927 C CE3 . TRP B 309 ? 0.2137 0.1213 0.1525 0.0032  -0.0250 -0.0005 309 TRP B CE3 
11928 C CZ2 . TRP B 309 ? 0.1753 0.1884 0.1600 0.0133  -0.0230 0.0007  309 TRP B CZ2 
11929 C CZ3 . TRP B 309 ? 0.1817 0.1928 0.1647 -0.0256 -0.0127 -0.0079 309 TRP B CZ3 
11930 C CH2 . TRP B 309 ? 0.2085 0.1936 0.1666 -0.0086 -0.0125 -0.0011 309 TRP B CH2 
11941 N N   . GLN B 310 ? 0.2094 0.1838 0.1677 0.0182  -0.0384 -0.0048 310 GLN B N   
11942 C CA  . GLN B 310 ? 0.2530 0.1577 0.1803 0.0152  -0.0490 0.0158  310 GLN B CA  
11943 C C   . GLN B 310 ? 0.1912 0.1657 0.1914 -0.0229 -0.0379 0.0219  310 GLN B C   
11944 O O   . GLN B 310 ? 0.1791 0.1741 0.1995 0.0202  -0.0267 0.0015  310 GLN B O   
11945 C CB  . GLN B 310 ? 0.2548 0.1502 0.1856 -0.0038 -0.0691 -0.0153 310 GLN B CB  
11946 C CG  . GLN B 310 ? 0.3100 0.2462 0.1958 -0.0577 -0.0604 0.0030  310 GLN B CG  
11947 C CD  . GLN B 310 ? 0.4220 0.3484 0.2261 -0.0611 -0.0366 -0.0177 310 GLN B CD  
11948 O OE1 . GLN B 310 ? 0.4672 0.4319 0.2687 -0.0760 -0.0263 -0.0557 310 GLN B OE1 
11949 N NE2 . GLN B 310 ? 0.4582 0.3683 0.2124 -0.0653 -0.0472 0.0274  310 GLN B NE2 
11958 N N   . VAL B 311 ? 0.1918 0.1729 0.1964 -0.0240 -0.0525 0.0246  311 VAL B N   
11959 C CA  . VAL B 311 ? 0.1964 0.1763 0.1890 -0.0140 -0.0529 -0.0025 311 VAL B CA  
11960 C C   . VAL B 311 ? 0.1857 0.1920 0.1790 -0.0073 -0.0226 0.0043  311 VAL B C   
11961 O O   . VAL B 311 ? 0.2196 0.1563 0.1996 -0.0046 -0.0139 0.0166  311 VAL B O   
11962 C CB  . VAL B 311 ? 0.2126 0.1263 0.1837 -0.0121 -0.0609 -0.0119 311 VAL B CB  
11963 C CG1 . VAL B 311 ? 0.2186 0.1670 0.1913 0.0218  -0.0451 0.0053  311 VAL B CG1 
11964 C CG2 . VAL B 311 ? 0.2234 0.1287 0.1784 0.0295  -0.0478 -0.0021 311 VAL B CG2 
11974 N N   . LEU B 312 ? 0.1671 0.1800 0.1677 0.0190  -0.0139 0.0148  312 LEU B N   
11975 C CA  . LEU B 312 ? 0.1675 0.1648 0.1823 -0.0146 -0.0094 0.0163  312 LEU B CA  
11976 C C   . LEU B 312 ? 0.1598 0.1577 0.1774 -0.0119 -0.0017 0.0097  312 LEU B C   
11977 O O   . LEU B 312 ? 0.1661 0.2134 0.1863 -0.0276 0.0130  0.0006  312 LEU B O   
11978 C CB  . LEU B 312 ? 0.1692 0.1662 0.1901 -0.0818 -0.0207 0.0149  312 LEU B CB  
11979 C CG  . LEU B 312 ? 0.1788 0.1863 0.2231 -0.0126 -0.0293 0.0394  312 LEU B CG  
11980 C CD1 . LEU B 312 ? 0.1989 0.2653 0.2180 -0.0561 -0.0614 0.0331  312 LEU B CD1 
11981 C CD2 . LEU B 312 ? 0.2484 0.2909 0.2832 -0.0537 -0.0389 0.0816  312 LEU B CD2 
11993 N N   . GLU B 313 ? 0.1708 0.1809 0.1761 -0.0080 -0.0256 -0.0041 313 GLU B N   
11994 C CA  . GLU B 313 ? 0.1486 0.1806 0.1911 -0.0092 -0.0300 0.0122  313 GLU B CA  
11995 C C   . GLU B 313 ? 0.1569 0.1690 0.1969 0.0259  -0.0213 0.0009  313 GLU B C   
11996 O O   . GLU B 313 ? 0.1794 0.1983 0.2131 -0.0135 -0.0038 -0.0207 313 GLU B O   
11997 C CB  . GLU B 313 ? 0.1727 0.2240 0.2079 0.0079  -0.0286 -0.0020 313 GLU B CB  
11998 C CG  . GLU B 313 ? 0.2073 0.2161 0.2194 0.0142  -0.0345 -0.0006 313 GLU B CG  
11999 C CD  . GLU B 313 ? 0.2474 0.1964 0.2249 0.0106  -0.0625 0.0104  313 GLU B CD  
12000 O OE1 . GLU B 313 ? 0.3402 0.2421 0.2442 -0.0225 -0.0766 0.0300  313 GLU B OE1 
12001 O OE2 . GLU B 313 ? 0.2286 0.1725 0.2149 0.0250  -0.0410 0.0090  313 GLU B OE2 
12008 N N   . GLN B 314 ? 0.2067 0.1821 0.1984 0.0084  -0.0148 -0.0139 314 GLN B N   
12009 C CA  . GLN B 314 ? 0.2264 0.1796 0.2149 -0.0541 -0.0180 0.0073  314 GLN B CA  
12010 C C   . GLN B 314 ? 0.1436 0.1974 0.2108 -0.0445 -0.0232 0.0201  314 GLN B C   
12011 O O   . GLN B 314 ? 0.1897 0.2019 0.2225 -0.0330 -0.0213 0.0075  314 GLN B O   
12012 C CB  . GLN B 314 ? 0.2649 0.1938 0.2295 -0.0337 -0.0398 0.0039  314 GLN B CB  
12013 C CG  . GLN B 314 ? 0.3192 0.2449 0.2442 -0.0642 -0.0414 -0.0497 314 GLN B CG  
12014 C CD  . GLN B 314 ? 0.3810 0.3070 0.2784 -0.0267 -0.0639 -0.0777 314 GLN B CD  
12015 O OE1 . GLN B 314 ? 0.3026 0.3357 0.3018 0.0297  -0.1116 -0.0702 314 GLN B OE1 
12016 N NE2 . GLN B 314 ? 0.4888 0.3664 0.2996 -0.0512 -0.0311 -0.0752 314 GLN B NE2 
12025 N N   . GLY B 315 ? 0.1374 0.2210 0.2112 -0.0003 -0.0505 0.0268  315 GLY B N   
12026 C CA  . GLY B 315 ? 0.1877 0.2372 0.2022 0.0067  -0.0617 0.0232  315 GLY B CA  
12027 C C   . GLY B 315 ? 0.1910 0.1876 0.1951 -0.0126 -0.0334 -0.0023 315 GLY B C   
12028 O O   . GLY B 315 ? 0.1992 0.1856 0.2099 -0.0521 -0.0115 0.0045  315 GLY B O   
12032 N N   . THR B 316 ? 0.1909 0.1474 0.1931 -0.0289 -0.0048 -0.0299 316 THR B N   
12033 C CA  . THR B 316 ? 0.2065 0.1709 0.1877 -0.0151 0.0022  -0.0263 316 THR B CA  
12034 C C   . THR B 316 ? 0.1981 0.2246 0.1809 0.0012  -0.0058 -0.0348 316 THR B C   
12035 O O   . THR B 316 ? 0.2018 0.2590 0.1823 -0.0258 -0.0148 -0.0198 316 THR B O   
12036 C CB  . THR B 316 ? 0.1763 0.1848 0.1952 -0.0234 -0.0209 -0.0038 316 THR B CB  
12037 O OG1 . THR B 316 ? 0.1799 0.2026 0.1903 0.0057  -0.0197 -0.0129 316 THR B OG1 
12038 C CG2 . THR B 316 ? 0.1874 0.1811 0.2147 -0.0612 -0.0010 -0.0236 316 THR B CG2 
12046 N N   . GLY B 317 ? 0.2004 0.2486 0.2104 -0.0240 -0.0189 -0.0267 317 GLY B N   
12047 C CA  . GLY B 317 ? 0.1794 0.2706 0.2302 -0.0085 -0.0192 -0.0436 317 GLY B CA  
12048 C C   . GLY B 317 ? 0.1342 0.2590 0.2485 0.0016  -0.0120 -0.0465 317 GLY B C   
12049 O O   . GLY B 317 ? 0.1755 0.2853 0.2752 -0.0251 -0.0241 -0.0490 317 GLY B O   
12053 N N   . GLU B 318 ? 0.1441 0.3018 0.2626 -0.0598 -0.0384 -0.0286 318 GLU B N   
12054 C CA  . GLU B 318 ? 0.2356 0.2943 0.2719 -0.0701 -0.0128 -0.0227 318 GLU B CA  
12055 C C   . GLU B 318 ? 0.1681 0.2480 0.2602 -0.0693 -0.0149 0.0231  318 GLU B C   
12056 O O   . GLU B 318 ? 0.2225 0.2853 0.2683 -0.0858 -0.0207 0.0301  318 GLU B O   
12057 C CB  . GLU B 318 ? 0.3392 0.2917 0.3138 -0.0795 -0.0136 -0.0032 318 GLU B CB  
12058 C CG  . GLU B 318 ? 0.4586 0.3938 0.3295 -0.0813 -0.0269 -0.0450 318 GLU B CG  
12059 C CD  . GLU B 318 ? 0.5590 0.4621 0.3662 -0.0724 -0.0136 -0.0614 318 GLU B CD  
12060 O OE1 . GLU B 318 ? 0.5154 0.4698 0.3529 -0.1070 0.0127  -0.0780 318 GLU B OE1 
12061 O OE2 . GLU B 318 ? 0.6097 0.4901 0.3961 -0.0845 -0.0288 -0.0783 318 GLU B OE2 
12068 N N   . PHE B 319 ? 0.1987 0.2248 0.2412 -0.0598 -0.0213 0.0212  319 PHE B N   
12069 C CA  . PHE B 319 ? 0.2002 0.2440 0.2371 -0.0527 -0.0311 0.0181  319 PHE B CA  
12070 C C   . PHE B 319 ? 0.2193 0.2736 0.2264 -0.0637 -0.0247 -0.0016 319 PHE B C   
12071 O O   . PHE B 319 ? 0.3458 0.2668 0.2103 -0.0187 -0.0282 0.0079  319 PHE B O   
12072 C CB  . PHE B 319 ? 0.2069 0.2304 0.2386 -0.0356 -0.0413 0.0174  319 PHE B CB  
12073 C CG  . PHE B 319 ? 0.2721 0.2291 0.2280 -0.0510 -0.0292 0.0366  319 PHE B CG  
12074 C CD1 . PHE B 319 ? 0.2943 0.2497 0.2358 -0.0373 -0.0431 0.0198  319 PHE B CD1 
12075 C CD2 . PHE B 319 ? 0.3643 0.2447 0.2398 -0.0176 0.0061  0.0453  319 PHE B CD2 
12076 C CE1 . PHE B 319 ? 0.3010 0.2562 0.2413 -0.0272 -0.0052 0.0199  319 PHE B CE1 
12077 C CE2 . PHE B 319 ? 0.3535 0.2296 0.2365 -0.0180 0.0196  0.0542  319 PHE B CE2 
12078 C CZ  . PHE B 319 ? 0.3133 0.2321 0.2344 -0.0111 -0.0003 0.0068  319 PHE B CZ  
12088 N N   . GLY B 320 ? 0.1743 0.2415 0.2277 -0.0245 -0.0053 -0.0127 320 GLY B N   
12089 C CA  . GLY B 320 ? 0.1632 0.1935 0.2096 -0.0178 0.0004  0.0018  320 GLY B CA  
12090 C C   . GLY B 320 ? 0.1808 0.1975 0.2032 -0.0013 0.0027  0.0124  320 GLY B C   
12091 O O   . GLY B 320 ? 0.1658 0.2103 0.2076 -0.0055 0.0101  0.0104  320 GLY B O   
12095 N N   . PRO B 321 ? 0.1207 0.2481 0.1967 -0.0003 -0.0099 0.0173  321 PRO B N   
12096 C CA  . PRO B 321 ? 0.1464 0.1938 0.1989 -0.0556 -0.0027 0.0420  321 PRO B CA  
12097 C C   . PRO B 321 ? 0.1492 0.1844 0.2022 -0.0452 -0.0028 0.0334  321 PRO B C   
12098 O O   . PRO B 321 ? 0.1795 0.2194 0.2189 -0.0161 0.0071  0.0361  321 PRO B O   
12099 C CB  . PRO B 321 ? 0.1767 0.2229 0.1992 -0.0057 -0.0334 0.0103  321 PRO B CB  
12100 C CG  . PRO B 321 ? 0.1877 0.2619 0.2028 -0.0092 -0.0166 -0.0134 321 PRO B CG  
12101 C CD  . PRO B 321 ? 0.1805 0.2744 0.1991 -0.0171 -0.0057 -0.0241 321 PRO B CD  
12109 N N   . ILE B 322 ? 0.1586 0.1596 0.1965 -0.0169 -0.0235 0.0124  322 ILE B N   
12110 C CA  . ILE B 322 ? 0.2128 0.0997 0.1943 -0.0212 -0.0380 0.0134  322 ILE B CA  
12111 C C   . ILE B 322 ? 0.1805 0.0721 0.1809 -0.0479 -0.0232 0.0016  322 ILE B C   
12112 O O   . ILE B 322 ? 0.1806 0.0906 0.2258 -0.0035 -0.0213 0.0015  322 ILE B O   
12113 C CB  . ILE B 322 ? 0.2369 0.1764 0.2045 0.0164  -0.0291 0.0362  322 ILE B CB  
12114 C CG1 . ILE B 322 ? 0.2446 0.2838 0.2189 0.0649  -0.0437 0.0311  322 ILE B CG1 
12115 C CG2 . ILE B 322 ? 0.2552 0.1987 0.2115 -0.0014 -0.0244 0.0769  322 ILE B CG2 
12116 C CD1 . ILE B 322 ? 0.3285 0.3173 0.2457 0.0692  -0.0585 0.0068  322 ILE B CD1 
12128 N N   . GLY B 323 ? 0.1811 0.1455 0.1669 -0.0081 -0.0382 0.0264  323 GLY B N   
12129 C CA  . GLY B 323 ? 0.1783 0.1820 0.1631 -0.0108 -0.0200 0.0363  323 GLY B CA  
12130 C C   . GLY B 323 ? 0.1651 0.1282 0.1624 0.0297  -0.0043 0.0372  323 GLY B C   
12131 O O   . GLY B 323 ? 0.1632 0.1200 0.1524 -0.0008 -0.0187 0.0196  323 GLY B O   
12135 N N   . HIS B 324 ? 0.1742 0.1348 0.1792 -0.0062 -0.0034 0.0426  324 HIS B N   
12136 C CA  . HIS B 324 ? 0.1562 0.1121 0.1633 -0.0350 -0.0079 0.0282  324 HIS B CA  
12137 C C   . HIS B 324 ? 0.1608 0.1279 0.1766 -0.0068 -0.0254 0.0106  324 HIS B C   
12138 O O   . HIS B 324 ? 0.1964 0.1250 0.1945 0.0378  -0.0206 -0.0089 324 HIS B O   
12139 C CB  . HIS B 324 ? 0.1697 0.1331 0.1601 0.0113  0.0001  0.0211  324 HIS B CB  
12140 C CG  . HIS B 324 ? 0.1673 0.1249 0.1561 -0.0027 -0.0006 -0.0097 324 HIS B CG  
12141 N ND1 . HIS B 324 ? 0.1756 0.1398 0.1587 0.0214  -0.0201 0.0086  324 HIS B ND1 
12142 C CD2 . HIS B 324 ? 0.1518 0.1059 0.1581 -0.0134 -0.0228 -0.0116 324 HIS B CD2 
12143 C CE1 . HIS B 324 ? 0.1759 0.1312 0.1548 -0.0092 -0.0263 0.0186  324 HIS B CE1 
12144 N NE2 . HIS B 324 ? 0.1786 0.1337 0.1580 -0.0293 -0.0331 -0.0031 324 HIS B NE2 
12152 N N   . GLY B 325 ? 0.1615 0.1283 0.1812 0.0115  -0.0246 0.0187  325 GLY B N   
12153 C CA  . GLY B 325 ? 0.1564 0.1324 0.1794 0.0193  0.0033  0.0177  325 GLY B CA  
12154 C C   . GLY B 325 ? 0.1446 0.1305 0.1742 0.0089  -0.0293 0.0167  325 GLY B C   
12155 O O   . GLY B 325 ? 0.2236 0.1100 0.1932 -0.0069 -0.0414 0.0152  325 GLY B O   
12159 N N   . TRP B 326 ? 0.1606 0.1538 0.1641 0.0060  -0.0270 0.0098  326 TRP B N   
12160 C CA  . TRP B 326 ? 0.1537 0.1465 0.1564 -0.0268 -0.0174 0.0028  326 TRP B CA  
12161 C C   . TRP B 326 ? 0.1430 0.1589 0.1678 -0.0143 -0.0293 -0.0104 326 TRP B C   
12162 O O   . TRP B 326 ? 0.1782 0.1574 0.1898 -0.0040 -0.0190 -0.0129 326 TRP B O   
12163 C CB  . TRP B 326 ? 0.1846 0.1482 0.1549 -0.0565 -0.0267 0.0242  326 TRP B CB  
12164 C CG  . TRP B 326 ? 0.1841 0.0954 0.1484 -0.0074 0.0028  0.0072  326 TRP B CG  
12165 C CD1 . TRP B 326 ? 0.1974 0.1229 0.1473 -0.0069 -0.0003 0.0372  326 TRP B CD1 
12166 C CD2 . TRP B 326 ? 0.1677 0.1117 0.1363 -0.0294 -0.0078 0.0077  326 TRP B CD2 
12167 N NE1 . TRP B 326 ? 0.1700 0.1403 0.1398 -0.0097 0.0038  0.0378  326 TRP B NE1 
12168 C CE2 . TRP B 326 ? 0.1791 0.1316 0.1417 -0.0608 -0.0037 0.0377  326 TRP B CE2 
12169 C CE3 . TRP B 326 ? 0.1783 0.1295 0.1494 -0.0347 0.0288  -0.0014 326 TRP B CE3 
12170 C CZ2 . TRP B 326 ? 0.1850 0.1473 0.1335 -0.0621 0.0054  0.0213  326 TRP B CZ2 
12171 C CZ3 . TRP B 326 ? 0.1706 0.1463 0.1470 -0.0663 -0.0045 0.0138  326 TRP B CZ3 
12172 C CH2 . TRP B 326 ? 0.1797 0.1298 0.1470 -0.0269 0.0232  0.0170  326 TRP B CH2 
12183 N N   . THR B 327 ? 0.1411 0.1434 0.1435 0.0153  -0.0200 -0.0241 327 THR B N   
12184 C CA  . THR B 327 ? 0.1769 0.1024 0.1466 0.0162  -0.0080 -0.0145 327 THR B CA  
12185 C C   . THR B 327 ? 0.1777 0.1156 0.1415 -0.0007 -0.0090 0.0086  327 THR B C   
12186 O O   . THR B 327 ? 0.1833 0.1385 0.1575 0.0028  0.0027  0.0130  327 THR B O   
12187 C CB  . THR B 327 ? 0.1863 0.1449 0.1608 0.0142  0.0049  0.0093  327 THR B CB  
12188 O OG1 . THR B 327 ? 0.2983 0.1651 0.1774 0.0040  0.0548  0.0292  327 THR B OG1 
12189 C CG2 . THR B 327 ? 0.2372 0.1224 0.1723 -0.0190 0.0201  -0.0108 327 THR B CG2 
12197 N N   . TYR B 328 ? 0.1865 0.1298 0.1341 -0.0414 -0.0243 0.0107  328 TYR B N   
12198 C CA  . TYR B 328 ? 0.1755 0.1132 0.1475 -0.0430 -0.0199 -0.0031 328 TYR B CA  
12199 C C   . TYR B 328 ? 0.2301 0.1495 0.1566 0.0006  -0.0216 0.0038  328 TYR B C   
12200 O O   . TYR B 328 ? 0.2251 0.1368 0.1472 -0.0208 -0.0244 0.0125  328 TYR B O   
12201 C CB  . TYR B 328 ? 0.1864 0.1734 0.1616 -0.0282 -0.0125 0.0152  328 TYR B CB  
12202 C CG  . TYR B 328 ? 0.1695 0.1010 0.1670 -0.0018 -0.0167 0.0119  328 TYR B CG  
12203 C CD1 . TYR B 328 ? 0.1851 0.1702 0.1678 -0.0131 -0.0111 -0.0019 328 TYR B CD1 
12204 C CD2 . TYR B 328 ? 0.2139 0.1325 0.1688 0.0083  -0.0158 0.0069  328 TYR B CD2 
12205 C CE1 . TYR B 328 ? 0.2173 0.1971 0.1723 -0.0055 -0.0090 -0.0063 328 TYR B CE1 
12206 C CE2 . TYR B 328 ? 0.2155 0.1328 0.1626 0.0056  -0.0183 0.0247  328 TYR B CE2 
12207 C CZ  . TYR B 328 ? 0.2111 0.1590 0.1655 0.0104  -0.0095 0.0115  328 TYR B CZ  
12208 O OH  . TYR B 328 ? 0.2173 0.2212 0.1804 -0.0166 0.0027  -0.0130 328 TYR B OH  
12218 N N   . SER B 329 ? 0.2165 0.1451 0.1504 0.0026  -0.0271 0.0052  329 SER B N   
12219 C CA  . SER B 329 ? 0.1926 0.1681 0.1475 -0.0232 -0.0297 -0.0017 329 SER B CA  
12220 C C   . SER B 329 ? 0.1846 0.1867 0.1607 0.0151  -0.0106 0.0051  329 SER B C   
12221 O O   . SER B 329 ? 0.1707 0.1605 0.1763 -0.0001 -0.0076 0.0116  329 SER B O   
12222 C CB  . SER B 329 ? 0.1383 0.1726 0.1393 -0.0269 -0.0162 -0.0259 329 SER B CB  
12223 O OG  . SER B 329 ? 0.1814 0.1764 0.1436 -0.0177 -0.0179 -0.0196 329 SER B OG  
12229 N N   . GLY B 330 ? 0.1739 0.1185 0.1650 0.0343  0.0087  0.0042  330 GLY B N   
12230 C CA  . GLY B 330 ? 0.2045 0.1161 0.1633 0.0225  -0.0070 0.0254  330 GLY B CA  
12231 C C   . GLY B 330 ? 0.1960 0.1350 0.1728 -0.0098 -0.0163 0.0039  330 GLY B C   
12232 O O   . GLY B 330 ? 0.1807 0.1336 0.1920 -0.0157 -0.0228 -0.0013 330 GLY B O   
12236 N N   . HIS B 331 ? 0.1965 0.1641 0.1735 -0.0048 -0.0183 0.0019  331 HIS B N   
12237 C CA  . HIS B 331 ? 0.2151 0.1774 0.1774 -0.0080 -0.0176 -0.0032 331 HIS B CA  
12238 C C   . HIS B 331 ? 0.1894 0.1542 0.1773 -0.0253 0.0080  -0.0218 331 HIS B C   
12239 O O   . HIS B 331 ? 0.1801 0.1618 0.1957 -0.0518 0.0045  -0.0168 331 HIS B O   
12240 C CB  . HIS B 331 ? 0.1903 0.1718 0.1782 -0.0294 -0.0202 0.0056  331 HIS B CB  
12241 C CG  . HIS B 331 ? 0.1823 0.1319 0.1795 -0.0182 -0.0358 0.0100  331 HIS B CG  
12242 N ND1 . HIS B 331 ? 0.1913 0.1324 0.1727 -0.0303 -0.0298 0.0019  331 HIS B ND1 
12243 C CD2 . HIS B 331 ? 0.2128 0.1627 0.1782 -0.0230 -0.0155 -0.0025 331 HIS B CD2 
12244 C CE1 . HIS B 331 ? 0.2131 0.1733 0.1706 -0.0366 -0.0340 0.0116  331 HIS B CE1 
12245 N NE2 . HIS B 331 ? 0.2366 0.1571 0.1695 -0.0026 -0.0250 0.0206  331 HIS B NE2 
12253 N N   . ALA B 332 ? 0.2025 0.1054 0.1703 -0.0017 0.0286  -0.0141 332 ALA B N   
12254 C CA  . ALA B 332 ? 0.1932 0.0760 0.1734 -0.0037 0.0412  -0.0007 332 ALA B CA  
12255 C C   . ALA B 332 ? 0.2165 0.1606 0.1723 -0.0088 0.0044  0.0072  332 ALA B C   
12256 O O   . ALA B 332 ? 0.2325 0.1336 0.1773 -0.0038 -0.0153 -0.0050 332 ALA B O   
12257 C CB  . ALA B 332 ? 0.2432 0.1420 0.1919 0.0055  0.0074  -0.0017 332 ALA B CB  
12263 N N   . LEU B 333 ? 0.2381 0.1161 0.1816 -0.0068 0.0058  0.0126  333 LEU B N   
12264 C CA  . LEU B 333 ? 0.2239 0.1194 0.1949 -0.0088 -0.0031 -0.0038 333 LEU B CA  
12265 C C   . LEU B 333 ? 0.2281 0.1472 0.1973 -0.0099 -0.0001 0.0188  333 LEU B C   
12266 O O   . LEU B 333 ? 0.2263 0.1557 0.1933 -0.0339 -0.0285 0.0456  333 LEU B O   
12267 C CB  . LEU B 333 ? 0.1984 0.1078 0.1940 -0.0163 -0.0098 0.0108  333 LEU B CB  
12268 C CG  . LEU B 333 ? 0.2435 0.1130 0.1942 -0.0193 -0.0122 -0.0105 333 LEU B CG  
12269 C CD1 . LEU B 333 ? 0.2747 0.1624 0.1966 -0.0294 -0.0035 -0.0280 333 LEU B CD1 
12270 C CD2 . LEU B 333 ? 0.2472 0.1214 0.2166 -0.0215 -0.0048 -0.0458 333 LEU B CD2 
12282 N N   . GLY B 334 ? 0.2526 0.1323 0.2005 -0.0272 -0.0105 0.0133  334 GLY B N   
12283 C CA  . GLY B 334 ? 0.2469 0.1608 0.1944 -0.0174 -0.0201 0.0164  334 GLY B CA  
12284 C C   . GLY B 334 ? 0.2417 0.1599 0.1922 -0.0305 -0.0190 0.0149  334 GLY B C   
12285 O O   . GLY B 334 ? 0.2509 0.1525 0.1872 -0.0332 -0.0028 0.0209  334 GLY B O   
12289 N N   . CYS B 335 ? 0.1968 0.1434 0.1970 -0.0189 -0.0084 0.0184  335 CYS B N   
12290 C CA  . CYS B 335 ? 0.1857 0.1298 0.1946 -0.0240 -0.0046 0.0147  335 CYS B CA  
12291 C C   . CYS B 335 ? 0.2167 0.1524 0.2022 -0.0058 0.0182  0.0065  335 CYS B C   
12292 O O   . CYS B 335 ? 0.2520 0.1609 0.1994 -0.0373 0.0143  0.0333  335 CYS B O   
12293 C CB  . CYS B 335 ? 0.1669 0.1711 0.1961 -0.0332 -0.0151 -0.0161 335 CYS B CB  
12294 S SG  . CYS B 335 ? 0.2036 0.1730 0.2023 -0.0389 -0.0177 0.0146  335 CYS B SG  
12300 N N   . ALA B 336 ? 0.2174 0.1691 0.2090 -0.0637 0.0073  -0.0025 336 ALA B N   
12301 C CA  . ALA B 336 ? 0.1752 0.1501 0.2093 -0.0601 0.0156  -0.0204 336 ALA B CA  
12302 C C   . ALA B 336 ? 0.2380 0.1599 0.2039 -0.0483 -0.0054 0.0005  336 ALA B C   
12303 O O   . ALA B 336 ? 0.2986 0.1290 0.1963 -0.0338 0.0199  0.0160  336 ALA B O   
12304 C CB  . ALA B 336 ? 0.1991 0.1732 0.1956 -0.0273 0.0209  -0.0268 336 ALA B CB  
12310 N N   . ALA B 337 ? 0.2266 0.1714 0.1936 -0.0458 -0.0070 -0.0075 337 ALA B N   
12311 C CA  . ALA B 337 ? 0.1882 0.1413 0.1894 -0.0218 -0.0119 0.0075  337 ALA B CA  
12312 C C   . ALA B 337 ? 0.1731 0.1567 0.1876 -0.0415 0.0117  0.0279  337 ALA B C   
12313 O O   . ALA B 337 ? 0.2131 0.2045 0.1873 -0.0630 0.0134  0.0370  337 ALA B O   
12314 C CB  . ALA B 337 ? 0.2280 0.1650 0.1867 -0.0283 -0.0126 0.0362  337 ALA B CB  
12320 N N   . GLY B 338 ? 0.2130 0.1019 0.1899 -0.0301 -0.0123 -0.0055 338 GLY B N   
12321 C CA  . GLY B 338 ? 0.2315 0.1433 0.1844 -0.0517 -0.0288 -0.0064 338 GLY B CA  
12322 C C   . GLY B 338 ? 0.2550 0.1834 0.1868 -0.0452 -0.0140 0.0038  338 GLY B C   
12323 O O   . GLY B 338 ? 0.2399 0.1888 0.1866 -0.0441 0.0028  0.0130  338 GLY B O   
12327 N N   . LEU B 339 ? 0.2162 0.1977 0.1938 -0.0506 0.0048  0.0020  339 LEU B N   
12328 C CA  . LEU B 339 ? 0.2347 0.1925 0.2008 -0.0435 0.0093  0.0224  339 LEU B CA  
12329 C C   . LEU B 339 ? 0.2423 0.1786 0.2009 -0.0215 0.0017  0.0302  339 LEU B C   
12330 O O   . LEU B 339 ? 0.2504 0.2043 0.2181 -0.0438 0.0107  0.0212  339 LEU B O   
12331 C CB  . LEU B 339 ? 0.2261 0.1837 0.2128 -0.0582 0.0181  0.0144  339 LEU B CB  
12332 C CG  . LEU B 339 ? 0.2696 0.2006 0.2210 -0.0287 0.0236  0.0182  339 LEU B CG  
12333 C CD1 . LEU B 339 ? 0.2954 0.2343 0.2184 -0.0433 0.0073  0.0074  339 LEU B CD1 
12334 C CD2 . LEU B 339 ? 0.2519 0.1883 0.2244 -0.0407 0.0226  0.0513  339 LEU B CD2 
12346 N N   . ALA B 340 ? 0.2488 0.1374 0.1817 -0.0095 0.0179  0.0311  340 ALA B N   
12347 C CA  . ALA B 340 ? 0.2674 0.1548 0.1821 -0.0404 0.0247  0.0377  340 ALA B CA  
12348 C C   . ALA B 340 ? 0.2746 0.1803 0.1797 -0.0301 0.0358  0.0267  340 ALA B C   
12349 O O   . ALA B 340 ? 0.2698 0.1660 0.1834 -0.0241 0.0212  0.0333  340 ALA B O   
12350 C CB  . ALA B 340 ? 0.2954 0.1426 0.2025 -0.0645 0.0253  0.0183  340 ALA B CB  
12356 N N   . ASN B 341 ? 0.2757 0.1978 0.1787 -0.0339 0.0329  0.0130  341 ASN B N   
12357 C CA  . ASN B 341 ? 0.2686 0.1914 0.1860 -0.0345 0.0144  0.0218  341 ASN B CA  
12358 C C   . ASN B 341 ? 0.2675 0.2044 0.1885 -0.0232 0.0287  0.0366  341 ASN B C   
12359 O O   . ASN B 341 ? 0.2623 0.2011 0.1920 -0.0535 0.0136  0.0424  341 ASN B O   
12360 C CB  . ASN B 341 ? 0.2789 0.1342 0.1852 -0.0035 0.0052  0.0108  341 ASN B CB  
12361 C CG  . ASN B 341 ? 0.2456 0.1605 0.1825 0.0033  0.0182  0.0006  341 ASN B CG  
12362 O OD1 . ASN B 341 ? 0.2474 0.1797 0.1878 -0.0296 0.0267  0.0078  341 ASN B OD1 
12363 N ND2 . ASN B 341 ? 0.2601 0.1867 0.1751 0.0056  0.0133  0.0113  341 ASN B ND2 
12370 N N   . LEU B 342 ? 0.2602 0.2313 0.1834 0.0106  0.0123  0.0432  342 LEU B N   
12371 C CA  . LEU B 342 ? 0.2315 0.2044 0.1952 -0.0128 -0.0005 0.0359  342 LEU B CA  
12372 C C   . LEU B 342 ? 0.2794 0.2030 0.2009 -0.0187 -0.0117 0.0374  342 LEU B C   
12373 O O   . LEU B 342 ? 0.3127 0.1754 0.1945 -0.0397 -0.0150 0.0464  342 LEU B O   
12374 C CB  . LEU B 342 ? 0.2521 0.1896 0.2145 -0.0542 0.0135  0.0134  342 LEU B CB  
12375 C CG  . LEU B 342 ? 0.3019 0.2266 0.2379 -0.0899 0.0208  -0.0039 342 LEU B CG  
12376 C CD1 . LEU B 342 ? 0.3183 0.2157 0.2309 -0.0673 -0.0031 -0.0410 342 LEU B CD1 
12377 C CD2 . LEU B 342 ? 0.3312 0.2080 0.2571 -0.1000 0.0140  -0.0189 342 LEU B CD2 
12389 N N   . ALA B 343 ? 0.2988 0.1602 0.2019 -0.0183 0.0219  0.0368  343 ALA B N   
12390 C CA  . ALA B 343 ? 0.3044 0.1801 0.2215 -0.0540 0.0159  0.0259  343 ALA B CA  
12391 C C   . ALA B 343 ? 0.3025 0.1479 0.2250 0.0144  0.0300  0.0605  343 ALA B C   
12392 O O   . ALA B 343 ? 0.3615 0.2044 0.2340 -0.0074 0.0355  0.0869  343 ALA B O   
12393 C CB  . ALA B 343 ? 0.3221 0.2282 0.2282 -0.0030 0.0095  0.0224  343 ALA B CB  
12399 N N   . ILE B 344 ? 0.3468 0.1231 0.2121 0.0025  0.0233  0.0449  344 ILE B N   
12400 C CA  . ILE B 344 ? 0.2927 0.1460 0.2154 -0.0289 -0.0018 0.0311  344 ILE B CA  
12401 C C   . ILE B 344 ? 0.2767 0.1533 0.2196 -0.0820 0.0062  0.0396  344 ILE B C   
12402 O O   . ILE B 344 ? 0.3334 0.1679 0.2393 -0.0701 0.0333  0.0639  344 ILE B O   
12403 C CB  . ILE B 344 ? 0.3037 0.1913 0.2193 -0.0290 0.0009  0.0102  344 ILE B CB  
12404 C CG1 . ILE B 344 ? 0.3129 0.1549 0.2336 -0.0677 0.0053  0.0100  344 ILE B CG1 
12405 C CG2 . ILE B 344 ? 0.3243 0.2081 0.2197 -0.0497 0.0042  0.0019  344 ILE B CG2 
12406 C CD1 . ILE B 344 ? 0.3442 0.1746 0.2520 -0.0354 0.0341  -0.0019 344 ILE B CD1 
12418 N N   . ILE B 345 ? 0.3073 0.1754 0.2226 -0.0839 -0.0041 0.0059  345 ILE B N   
12419 C CA  . ILE B 345 ? 0.2649 0.1704 0.2158 -0.0472 0.0221  0.0145  345 ILE B CA  
12420 C C   . ILE B 345 ? 0.2488 0.1806 0.2189 -0.0284 0.0260  0.0354  345 ILE B C   
12421 O O   . ILE B 345 ? 0.2384 0.2384 0.2289 -0.0191 0.0067  0.0347  345 ILE B O   
12422 C CB  . ILE B 345 ? 0.2573 0.1793 0.2105 -0.0430 0.0198  0.0386  345 ILE B CB  
12423 C CG1 . ILE B 345 ? 0.2543 0.1224 0.2043 -0.0465 0.0096  0.0359  345 ILE B CG1 
12424 C CG2 . ILE B 345 ? 0.2542 0.1654 0.2156 -0.0468 0.0280  0.0385  345 ILE B CG2 
12425 C CD1 . ILE B 345 ? 0.2651 0.1238 0.1972 -0.0905 -0.0192 -0.0063 345 ILE B CD1 
12437 N N   A GLU B 346 ? 0.2674 0.1450 0.2244 -0.0369 -0.0020 0.0614  346 GLU B N   
12438 N N   B GLU B 346 ? 0.2715 0.1848 0.2184 -0.0221 0.0105  0.0453  346 GLU B N   
12439 C CA  A GLU B 346 ? 0.3352 0.1515 0.2360 -0.0313 -0.0014 0.0777  346 GLU B CA  
12440 C CA  B GLU B 346 ? 0.3581 0.2308 0.2275 -0.0068 0.0327  0.0381  346 GLU B CA  
12441 C C   A GLU B 346 ? 0.3583 0.1531 0.2397 -0.0275 0.0295  0.0558  346 GLU B C   
12442 C C   B GLU B 346 ? 0.3691 0.2011 0.2332 -0.0169 0.0513  0.0373  346 GLU B C   
12443 O O   A GLU B 346 ? 0.3689 0.1588 0.2426 0.0004  0.0320  0.0514  346 GLU B O   
12444 O O   B GLU B 346 ? 0.3824 0.2345 0.2352 -0.0066 0.0570  0.0416  346 GLU B O   
12445 C CB  A GLU B 346 ? 0.3562 0.1901 0.2496 -0.0497 -0.0273 0.1064  346 GLU B CB  
12446 C CB  B GLU B 346 ? 0.4024 0.3352 0.2392 -0.0050 0.0354  0.0294  346 GLU B CB  
12447 C CG  A GLU B 346 ? 0.3911 0.2534 0.2718 -0.0596 -0.0604 0.1220  346 GLU B CG  
12448 C CG  B GLU B 346 ? 0.4848 0.4566 0.2649 -0.0046 0.0321  0.0061  346 GLU B CG  
12449 C CD  A GLU B 346 ? 0.4206 0.2867 0.2985 -0.0670 -0.0789 0.1289  346 GLU B CD  
12450 C CD  B GLU B 346 ? 0.5585 0.5572 0.2904 -0.0063 0.0385  -0.0124 346 GLU B CD  
12451 O OE1 A GLU B 346 ? 0.3946 0.3159 0.3045 -0.0877 -0.0948 0.1428  346 GLU B OE1 
12452 O OE1 B GLU B 346 ? 0.5640 0.6030 0.3003 0.0271  0.0249  -0.0166 346 GLU B OE1 
12453 O OE2 A GLU B 346 ? 0.4671 0.2636 0.3095 -0.0512 -0.0725 0.1420  346 GLU B OE2 
12454 O OE2 B GLU B 346 ? 0.6164 0.6119 0.3081 -0.0338 0.0430  -0.0128 346 GLU B OE2 
12467 N N   . ARG B 347 ? 0.3522 0.1807 0.2417 -0.0513 0.0400  0.0492  347 ARG B N   
12468 C CA  . ARG B 347 ? 0.3582 0.1637 0.2603 -0.0327 0.0499  0.0257  347 ARG B CA  
12469 C C   . ARG B 347 ? 0.3401 0.1467 0.2570 -0.0561 0.0653  0.0427  347 ARG B C   
12470 O O   . ARG B 347 ? 0.3963 0.2080 0.2628 -0.0682 0.0549  0.0572  347 ARG B O   
12471 C CB  . ARG B 347 ? 0.4657 0.2268 0.2818 -0.0468 0.0466  0.0086  347 ARG B CB  
12472 C CG  . ARG B 347 ? 0.5800 0.2456 0.3069 -0.0605 0.0577  0.0109  347 ARG B CG  
12473 C CD  . ARG B 347 ? 0.6463 0.2777 0.3170 -0.0364 0.0313  0.0078  347 ARG B CD  
12474 N NE  . ARG B 347 ? 0.7140 0.2041 0.3274 -0.0121 0.0273  0.0484  347 ARG B NE  
12475 C CZ  . ARG B 347 ? 0.7354 0.1962 0.3429 -0.0045 0.0119  0.0436  347 ARG B CZ  
12476 N NH1 . ARG B 347 ? 0.7414 0.2024 0.3460 0.0355  0.0176  0.0479  347 ARG B NH1 
12477 N NH2 . ARG B 347 ? 0.7765 0.2412 0.3463 -0.0777 -0.0007 0.0351  347 ARG B NH2 
12492 N N   . GLU B 348 ? 0.3211 0.2003 0.2599 -0.0293 0.0529  0.0286  348 GLU B N   
12493 C CA  . GLU B 348 ? 0.3203 0.2169 0.2532 -0.0133 0.0524  0.0340  348 GLU B CA  
12494 C C   . GLU B 348 ? 0.2888 0.2238 0.2557 -0.0387 0.0601  0.0239  348 GLU B C   
12495 O O   . GLU B 348 ? 0.3253 0.2339 0.2818 -0.0479 0.0472  0.0570  348 GLU B O   
12496 C CB  . GLU B 348 ? 0.3619 0.1921 0.2546 -0.0314 0.0341  0.0489  348 GLU B CB  
12497 C CG  . GLU B 348 ? 0.3915 0.1923 0.2495 -0.0522 0.0370  0.0386  348 GLU B CG  
12498 C CD  . GLU B 348 ? 0.3981 0.1725 0.2525 -0.0615 0.0422  0.0226  348 GLU B CD  
12499 O OE1 . GLU B 348 ? 0.4078 0.2048 0.2524 -0.0983 0.0355  0.0226  348 GLU B OE1 
12500 O OE2 . GLU B 348 ? 0.4548 0.1760 0.2632 -0.0448 0.0314  0.0047  348 GLU B OE2 
12507 N N   . GLY B 349 ? 0.3054 0.2355 0.2393 -0.0387 0.0550  0.0315  349 GLY B N   
12508 C CA  . GLY B 349 ? 0.3010 0.2134 0.2299 -0.0348 0.0543  0.0438  349 GLY B CA  
12509 C C   . GLY B 349 ? 0.2862 0.2418 0.2235 -0.0471 0.0464  0.0283  349 GLY B C   
12510 O O   . GLY B 349 ? 0.2857 0.2655 0.2320 -0.0790 0.0201  0.0219  349 GLY B O   
12514 N N   . LEU B 350 ? 0.2810 0.2255 0.2028 -0.0657 0.0419  0.0079  350 LEU B N   
12515 C CA  . LEU B 350 ? 0.2694 0.2173 0.1912 -0.0586 0.0275  0.0232  350 LEU B CA  
12516 C C   . LEU B 350 ? 0.2604 0.2729 0.2067 -0.0622 0.0172  0.0219  350 LEU B C   
12517 O O   . LEU B 350 ? 0.2438 0.2296 0.2205 -0.0685 0.0043  0.0205  350 LEU B O   
12518 C CB  . LEU B 350 ? 0.2897 0.2089 0.1923 -0.0796 0.0190  0.0062  350 LEU B CB  
12519 C CG  . LEU B 350 ? 0.3124 0.1943 0.2153 -0.1382 0.0198  0.0034  350 LEU B CG  
12520 C CD1 . LEU B 350 ? 0.3125 0.2252 0.2171 -0.1043 0.0326  0.0135  350 LEU B CD1 
12521 C CD2 . LEU B 350 ? 0.3580 0.2345 0.2354 -0.0723 0.0205  0.0138  350 LEU B CD2 
12533 N N   . THR B 351 ? 0.2632 0.2376 0.2074 -0.0651 -0.0019 0.0286  351 THR B N   
12534 C CA  . THR B 351 ? 0.2714 0.2880 0.2063 -0.0814 0.0039  0.0175  351 THR B CA  
12535 C C   . THR B 351 ? 0.2728 0.2507 0.2037 -0.0749 0.0093  0.0238  351 THR B C   
12536 O O   . THR B 351 ? 0.2448 0.2270 0.2079 -0.0614 -0.0006 0.0574  351 THR B O   
12537 C CB  . THR B 351 ? 0.2746 0.3033 0.2239 -0.0597 0.0334  0.0247  351 THR B CB  
12538 O OG1 . THR B 351 ? 0.2729 0.3352 0.2539 -0.0904 0.0489  0.0077  351 THR B OG1 
12539 C CG2 . THR B 351 ? 0.2281 0.2745 0.2217 -0.0883 0.0100  0.0472  351 THR B CG2 
12547 N N   . ALA B 352 ? 0.2622 0.2277 0.1994 -0.0359 0.0254  0.0429  352 ALA B N   
12548 C CA  . ALA B 352 ? 0.2883 0.2376 0.2038 -0.0648 0.0387  0.0589  352 ALA B CA  
12549 C C   . ALA B 352 ? 0.3036 0.2251 0.2011 -0.0945 0.0321  0.0278  352 ALA B C   
12550 O O   . ALA B 352 ? 0.2961 0.2757 0.2052 -0.0958 0.0233  0.0213  352 ALA B O   
12551 C CB  . ALA B 352 ? 0.3341 0.2183 0.1970 -0.0667 0.0269  0.0492  352 ALA B CB  
12557 N N   . ASN B 353 ? 0.2813 0.2492 0.2028 -0.0736 0.0295  0.0062  353 ASN B N   
12558 C CA  . ASN B 353 ? 0.2405 0.2417 0.2107 -0.0849 0.0231  -0.0023 353 ASN B CA  
12559 C C   . ASN B 353 ? 0.2613 0.2624 0.2124 -0.1043 0.0439  0.0145  353 ASN B C   
12560 O O   . ASN B 353 ? 0.3022 0.2463 0.2159 -0.1005 0.0555  0.0191  353 ASN B O   
12561 C CB  . ASN B 353 ? 0.2486 0.2329 0.2275 -0.0893 0.0227  0.0144  353 ASN B CB  
12562 C CG  . ASN B 353 ? 0.2424 0.2334 0.2367 -0.0990 0.0508  0.0081  353 ASN B CG  
12563 O OD1 . ASN B 353 ? 0.2834 0.2713 0.2310 -0.1147 0.0474  0.0171  353 ASN B OD1 
12564 N ND2 . ASN B 353 ? 0.2644 0.2317 0.2527 -0.0957 0.0448  -0.0006 353 ASN B ND2 
12571 N N   . ALA B 354 ? 0.2518 0.2002 0.2133 -0.0771 0.0423  0.0255  354 ALA B N   
12572 C CA  . ALA B 354 ? 0.2529 0.2212 0.2132 -0.0922 0.0463  0.0545  354 ALA B CA  
12573 C C   . ALA B 354 ? 0.2695 0.2530 0.2108 -0.0743 0.0230  0.0321  354 ALA B C   
12574 O O   . ALA B 354 ? 0.2371 0.2272 0.2279 -0.0484 0.0012  0.0333  354 ALA B O   
12575 C CB  . ALA B 354 ? 0.2248 0.2431 0.2190 -0.0789 0.0757  0.0443  354 ALA B CB  
12581 N N   . ALA B 355 ? 0.3024 0.2491 0.2105 -0.0926 0.0278  0.0377  355 ALA B N   
12582 C CA  . ALA B 355 ? 0.3078 0.2694 0.1976 -0.1166 0.0277  0.0325  355 ALA B CA  
12583 C C   . ALA B 355 ? 0.2999 0.3005 0.2034 -0.0789 0.0346  0.0351  355 ALA B C   
12584 O O   . ALA B 355 ? 0.2513 0.2632 0.2055 -0.0556 0.0249  0.0189  355 ALA B O   
12585 C CB  . ALA B 355 ? 0.2708 0.2641 0.1829 -0.0886 0.0027  0.0146  355 ALA B CB  
12591 N N   . GLU B 356 ? 0.3108 0.2944 0.2155 -0.1046 0.0385  0.0438  356 GLU B N   
12592 C CA  . GLU B 356 ? 0.3070 0.3036 0.2368 -0.1285 0.0548  0.0530  356 GLU B CA  
12593 C C   . GLU B 356 ? 0.2771 0.2924 0.2396 -0.1241 0.0509  0.0201  356 GLU B C   
12594 O O   . GLU B 356 ? 0.2468 0.2753 0.2490 -0.1303 0.0582  -0.0071 356 GLU B O   
12595 C CB  . GLU B 356 ? 0.4049 0.3190 0.2711 -0.1590 0.0378  0.0898  356 GLU B CB  
12596 C CG  . GLU B 356 ? 0.5457 0.4323 0.3058 -0.1699 -0.0057 0.0820  356 GLU B CG  
12597 C CD  . GLU B 356 ? 0.7285 0.5241 0.3408 -0.1263 -0.0734 0.0917  356 GLU B CD  
12598 O OE1 . GLU B 356 ? 0.8292 0.5380 0.3643 -0.0623 -0.0930 0.0733  356 GLU B OE1 
12599 O OE2 . GLU B 356 ? 0.7805 0.5985 0.3613 -0.1480 -0.0692 0.1137  356 GLU B OE2 
12606 N N   . THR B 357 ? 0.3047 0.2801 0.2463 -0.0958 0.0392  0.0354  357 THR B N   
12607 C CA  . THR B 357 ? 0.2921 0.2899 0.2426 -0.0940 0.0191  0.0034  357 THR B CA  
12608 C C   . THR B 357 ? 0.2666 0.2631 0.2241 -0.0961 0.0206  -0.0022 357 THR B C   
12609 O O   . THR B 357 ? 0.2738 0.2599 0.2191 -0.0775 0.0359  -0.0159 357 THR B O   
12610 C CB  . THR B 357 ? 0.2997 0.2495 0.2538 -0.0859 0.0172  0.0073  357 THR B CB  
12611 O OG1 . THR B 357 ? 0.3492 0.2397 0.2585 -0.1006 0.0549  -0.0229 357 THR B OG1 
12612 C CG2 . THR B 357 ? 0.3015 0.2727 0.2558 -0.0472 0.0117  0.0027  357 THR B CG2 
12620 N N   . GLY B 358 ? 0.2516 0.2063 0.2244 -0.0956 0.0366  -0.0047 358 GLY B N   
12621 C CA  . GLY B 358 ? 0.2254 0.1954 0.2251 -0.1161 0.0524  -0.0045 358 GLY B CA  
12622 C C   . GLY B 358 ? 0.2526 0.2133 0.2087 -0.0930 0.0518  -0.0052 358 GLY B C   
12623 O O   . GLY B 358 ? 0.2421 0.1997 0.2155 -0.0449 0.0399  -0.0113 358 GLY B O   
12627 N N   . ALA B 359 ? 0.2860 0.2457 0.2099 -0.0910 0.0436  -0.0121 359 ALA B N   
12628 C CA  . ALA B 359 ? 0.2689 0.2732 0.2098 -0.0921 0.0584  -0.0364 359 ALA B CA  
12629 C C   . ALA B 359 ? 0.2747 0.2837 0.2209 -0.0920 0.0521  -0.0106 359 ALA B C   
12630 O O   . ALA B 359 ? 0.2636 0.2991 0.2269 -0.1121 0.0461  -0.0003 359 ALA B O   
12631 C CB  . ALA B 359 ? 0.2872 0.2536 0.2037 -0.0424 0.0956  -0.0053 359 ALA B CB  
12637 N N   . TYR B 360 ? 0.2638 0.2712 0.2242 -0.0963 0.0488  -0.0173 360 TYR B N   
12638 C CA  . TYR B 360 ? 0.2187 0.3107 0.2457 -0.1061 0.0656  -0.0277 360 TYR B CA  
12639 C C   . TYR B 360 ? 0.2013 0.2675 0.2537 -0.0892 0.0479  -0.0350 360 TYR B C   
12640 O O   . TYR B 360 ? 0.2104 0.2705 0.2729 -0.0926 0.0583  -0.0491 360 TYR B O   
12641 C CB  . TYR B 360 ? 0.2323 0.2901 0.2600 -0.0768 0.0700  -0.0225 360 TYR B CB  
12642 C CG  . TYR B 360 ? 0.2540 0.2968 0.2618 -0.1253 0.0909  -0.0371 360 TYR B CG  
12643 C CD1 . TYR B 360 ? 0.3352 0.3376 0.2689 -0.1730 0.0781  -0.0353 360 TYR B CD1 
12644 C CD2 . TYR B 360 ? 0.2767 0.2908 0.2640 -0.1586 0.0652  -0.0355 360 TYR B CD2 
12645 C CE1 . TYR B 360 ? 0.3859 0.3469 0.2723 -0.1664 0.0666  -0.0387 360 TYR B CE1 
12646 C CE2 . TYR B 360 ? 0.3003 0.2962 0.2632 -0.1704 0.0647  -0.0250 360 TYR B CE2 
12647 C CZ  . TYR B 360 ? 0.3438 0.3291 0.2699 -0.1967 0.0559  -0.0273 360 TYR B CZ  
12648 O OH  . TYR B 360 ? 0.3642 0.3300 0.2840 -0.2028 0.0551  -0.0239 360 TYR B OH  
12658 N N   . LEU B 361 ? 0.2354 0.2635 0.2289 -0.0815 0.0571  -0.0323 361 LEU B N   
12659 C CA  . LEU B 361 ? 0.2516 0.2675 0.2368 -0.0732 0.0455  -0.0381 361 LEU B CA  
12660 C C   . LEU B 361 ? 0.2525 0.2663 0.2511 -0.0994 0.0460  -0.0583 361 LEU B C   
12661 O O   . LEU B 361 ? 0.2838 0.2655 0.2701 -0.0919 0.0556  -0.0511 361 LEU B O   
12662 C CB  . LEU B 361 ? 0.2339 0.2653 0.2093 -0.0644 0.0325  -0.0386 361 LEU B CB  
12663 C CG  . LEU B 361 ? 0.2245 0.2394 0.2215 -0.0879 0.0289  -0.0304 361 LEU B CG  
12664 C CD1 . LEU B 361 ? 0.2228 0.3025 0.2315 -0.1026 0.0213  -0.0184 361 LEU B CD1 
12665 C CD2 . LEU B 361 ? 0.2566 0.2449 0.2150 -0.1094 0.0220  -0.0222 361 LEU B CD2 
12677 N N   . GLN B 362 ? 0.2190 0.2808 0.2435 -0.1066 0.0464  -0.0656 362 GLN B N   
12678 C CA  . GLN B 362 ? 0.2233 0.2996 0.2317 -0.1047 0.0503  -0.0495 362 GLN B CA  
12679 C C   . GLN B 362 ? 0.2328 0.3081 0.2486 -0.1221 0.0544  -0.0516 362 GLN B C   
12680 O O   . GLN B 362 ? 0.2418 0.3096 0.2550 -0.0858 0.0689  -0.0321 362 GLN B O   
12681 C CB  . GLN B 362 ? 0.2445 0.2923 0.2244 -0.1014 0.0600  -0.0427 362 GLN B CB  
12682 C CG  . GLN B 362 ? 0.2163 0.3047 0.2337 -0.0836 0.0392  -0.0403 362 GLN B CG  
12683 C CD  . GLN B 362 ? 0.2362 0.2893 0.2338 -0.0925 0.0406  -0.0468 362 GLN B CD  
12684 O OE1 . GLN B 362 ? 0.2745 0.2810 0.2545 -0.0803 0.0367  -0.0116 362 GLN B OE1 
12685 N NE2 . GLN B 362 ? 0.2357 0.2910 0.2158 -0.0668 0.0379  -0.0510 362 GLN B NE2 
12694 N N   . GLN B 363 ? 0.2461 0.3068 0.2614 -0.1227 0.0814  -0.0485 363 GLN B N   
12695 C CA  . GLN B 363 ? 0.2822 0.2995 0.2918 -0.1167 0.0955  -0.0179 363 GLN B CA  
12696 C C   . GLN B 363 ? 0.2732 0.2868 0.2832 -0.0988 0.0822  -0.0326 363 GLN B C   
12697 O O   . GLN B 363 ? 0.2737 0.3061 0.2968 -0.1090 0.0697  -0.0148 363 GLN B O   
12698 C CB  . GLN B 363 ? 0.3728 0.3368 0.3201 -0.1305 0.1142  0.0373  363 GLN B CB  
12699 C CG  . GLN B 363 ? 0.5309 0.3928 0.3529 -0.1067 0.0755  0.0693  363 GLN B CG  
12700 C CD  . GLN B 363 ? 0.6702 0.4659 0.3825 -0.1224 0.0463  0.0790  363 GLN B CD  
12701 O OE1 . GLN B 363 ? 0.7239 0.4621 0.4010 -0.1112 0.0559  0.0703  363 GLN B OE1 
12702 N NE2 . GLN B 363 ? 0.7311 0.5162 0.3923 -0.1158 0.0347  0.0904  363 GLN B NE2 
12711 N N   . CYS B 364 ? 0.2431 0.2895 0.2745 -0.1038 0.0788  -0.0403 364 CYS B N   
12712 C CA  . CYS B 364 ? 0.2370 0.3041 0.2796 -0.1176 0.0789  -0.0176 364 CYS B CA  
12713 C C   . CYS B 364 ? 0.2058 0.3054 0.2784 -0.1291 0.0623  -0.0256 364 CYS B C   
12714 O O   . CYS B 364 ? 0.2170 0.3509 0.2777 -0.1252 0.0662  -0.0543 364 CYS B O   
12715 C CB  . CYS B 364 ? 0.3086 0.3062 0.2917 -0.1168 0.0528  -0.0212 364 CYS B CB  
12716 S SG  . CYS B 364 ? 0.3264 0.3023 0.3174 -0.1067 0.0531  -0.0185 364 CYS B SG  
12722 N N   . MET B 365 ? 0.2094 0.3041 0.2681 -0.1203 0.0566  -0.0281 365 MET B N   
12723 C CA  . MET B 365 ? 0.2199 0.3274 0.2653 -0.0728 0.0390  -0.0315 365 MET B CA  
12724 C C   . MET B 365 ? 0.2225 0.3492 0.2702 -0.0722 0.0330  -0.0454 365 MET B C   
12725 O O   . MET B 365 ? 0.2324 0.3921 0.2523 -0.0708 0.0125  -0.0541 365 MET B O   
12726 C CB  . MET B 365 ? 0.2260 0.3406 0.2625 -0.0219 0.0591  -0.0192 365 MET B CB  
12727 C CG  . MET B 365 ? 0.2145 0.3508 0.2574 -0.0528 0.0399  -0.0222 365 MET B CG  
12728 S SD  . MET B 365 ? 0.2976 0.3201 0.2527 -0.0807 0.0340  -0.0291 365 MET B SD  
12729 C CE  . MET B 365 ? 0.3321 0.3636 0.2629 -0.0743 0.0685  -0.0253 365 MET B CE  
12739 N N   . GLN B 366 ? 0.2388 0.3480 0.2789 -0.0638 0.0526  -0.0308 366 GLN B N   
12740 C CA  . GLN B 366 ? 0.2356 0.3864 0.3031 -0.0312 0.0678  -0.0401 366 GLN B CA  
12741 C C   . GLN B 366 ? 0.2828 0.3913 0.3138 -0.0310 0.0662  -0.0214 366 GLN B C   
12742 O O   . GLN B 366 ? 0.2984 0.3579 0.3156 0.0054  0.0800  -0.0114 366 GLN B O   
12743 C CB  . GLN B 366 ? 0.3216 0.4200 0.3353 -0.1136 0.0751  -0.0318 366 GLN B CB  
12744 C CG  . GLN B 366 ? 0.4452 0.4480 0.3652 -0.0994 0.1056  -0.0590 366 GLN B CG  
12745 C CD  . GLN B 366 ? 0.5346 0.5212 0.3964 -0.1336 0.1053  -0.0635 366 GLN B CD  
12746 O OE1 . GLN B 366 ? 0.5725 0.5176 0.3982 -0.0753 0.1141  -0.1106 366 GLN B OE1 
12747 N NE2 . GLN B 366 ? 0.5419 0.5284 0.4081 -0.1716 0.1036  -0.0474 366 GLN B NE2 
12756 N N   . GLN B 367 ? 0.2326 0.4066 0.3247 -0.0761 0.0658  -0.0191 367 GLN B N   
12757 C CA  . GLN B 367 ? 0.2531 0.4586 0.3428 -0.0854 0.0766  -0.0162 367 GLN B CA  
12758 C C   . GLN B 367 ? 0.2220 0.4534 0.3313 -0.1172 0.0778  -0.0244 367 GLN B C   
12759 O O   . GLN B 367 ? 0.2683 0.5119 0.3286 -0.0914 0.0606  -0.0356 367 GLN B O   
12760 C CB  . GLN B 367 ? 0.3386 0.4907 0.3729 -0.1038 0.0744  -0.0107 367 GLN B CB  
12761 C CG  . GLN B 367 ? 0.4755 0.5586 0.4104 -0.1119 0.0817  0.0030  367 GLN B CG  
12762 C CD  . GLN B 367 ? 0.6195 0.6439 0.4401 -0.1035 0.0759  0.0041  367 GLN B CD  
12763 O OE1 . GLN B 367 ? 0.6825 0.6664 0.4590 -0.1094 0.0730  -0.0123 367 GLN B OE1 
12764 N NE2 . GLN B 367 ? 0.6561 0.6794 0.4427 -0.0916 0.0821  0.0232  367 GLN B NE2 
12773 N N   . THR B 368 ? 0.2242 0.3909 0.3183 -0.0944 0.0677  -0.0270 368 THR B N   
12774 C CA  . THR B 368 ? 0.2406 0.3781 0.3328 -0.1100 0.0543  -0.0406 368 THR B CA  
12775 C C   . THR B 368 ? 0.2261 0.3656 0.3340 -0.0700 0.0342  -0.0575 368 THR B C   
12776 O O   . THR B 368 ? 0.2326 0.3964 0.3605 -0.0214 0.0208  -0.0840 368 THR B O   
12777 C CB  . THR B 368 ? 0.2711 0.3942 0.3387 -0.0917 0.0638  -0.0452 368 THR B CB  
12778 O OG1 . THR B 368 ? 0.2879 0.3924 0.3401 -0.1127 0.0860  -0.0400 368 THR B OG1 
12779 C CG2 . THR B 368 ? 0.2544 0.4039 0.3451 -0.1039 0.0273  -0.0724 368 THR B CG2 
12787 N N   . PHE B 369 ? 0.2359 0.3501 0.3073 -0.0552 0.0439  -0.0831 369 PHE B N   
12788 C CA  . PHE B 369 ? 0.2556 0.3772 0.2969 -0.0648 0.0491  -0.0893 369 PHE B CA  
12789 C C   . PHE B 369 ? 0.2639 0.4092 0.3108 -0.0504 0.0464  -0.1054 369 PHE B C   
12790 O O   . PHE B 369 ? 0.2396 0.4195 0.3097 -0.0429 0.0430  -0.1099 369 PHE B O   
12791 C CB  . PHE B 369 ? 0.2537 0.3851 0.2797 -0.1133 0.0475  -0.0592 369 PHE B CB  
12792 C CG  . PHE B 369 ? 0.2285 0.3651 0.2747 -0.0976 0.0286  -0.0716 369 PHE B CG  
12793 C CD1 . PHE B 369 ? 0.2030 0.3661 0.2754 -0.1319 0.0279  -0.0758 369 PHE B CD1 
12794 C CD2 . PHE B 369 ? 0.2422 0.3512 0.2668 -0.1327 0.0266  -0.0629 369 PHE B CD2 
12795 C CE1 . PHE B 369 ? 0.2037 0.3977 0.2700 -0.0796 0.0328  -0.0635 369 PHE B CE1 
12796 C CE2 . PHE B 369 ? 0.2471 0.3895 0.2736 -0.1213 0.0047  -0.0598 369 PHE B CE2 
12797 C CZ  . PHE B 369 ? 0.2144 0.3971 0.2739 -0.0932 0.0046  -0.0728 369 PHE B CZ  
12807 N N   . GLY B 370 ? 0.2645 0.4280 0.3147 -0.0459 0.0375  -0.1203 370 GLY B N   
12808 C CA  . GLY B 370 ? 0.2910 0.4368 0.3291 -0.0069 0.0361  -0.1374 370 GLY B CA  
12809 C C   . GLY B 370 ? 0.3183 0.4836 0.3482 -0.0017 0.0342  -0.1428 370 GLY B C   
12810 O O   . GLY B 370 ? 0.3483 0.5221 0.3742 -0.0042 0.0235  -0.1270 370 GLY B O   
12814 N N   . GLU B 371 ? 0.3137 0.5134 0.3491 -0.0245 0.0410  -0.1175 371 GLU B N   
12815 C CA  . GLU B 371 ? 0.3323 0.5948 0.3687 -0.0131 0.0575  -0.1094 371 GLU B CA  
12816 C C   . GLU B 371 ? 0.2770 0.6029 0.3724 -0.0127 0.0445  -0.1178 371 GLU B C   
12817 O O   . GLU B 371 ? 0.2738 0.6111 0.3887 0.0114  0.0713  -0.1215 371 GLU B O   
12818 C CB  . GLU B 371 ? 0.3665 0.6714 0.4115 -0.0045 0.0636  -0.1127 371 GLU B CB  
12819 C CG  . GLU B 371 ? 0.4697 0.7405 0.4446 -0.0180 0.0610  -0.1122 371 GLU B CG  
12820 C CD  . GLU B 371 ? 0.6066 0.7947 0.4822 -0.0515 0.0378  -0.1220 371 GLU B CD  
12821 O OE1 . GLU B 371 ? 0.6478 0.8185 0.4945 -0.0639 0.0302  -0.1180 371 GLU B OE1 
12822 O OE2 . GLU B 371 ? 0.6715 0.8209 0.5077 -0.0659 0.0353  -0.1151 371 GLU B OE2 
12829 N N   . HIS B 372 ? 0.2221 0.5678 0.3517 -0.0040 0.0446  -0.1150 372 HIS B N   
12830 C CA  . HIS B 372 ? 0.2437 0.5105 0.3487 -0.0196 0.0238  -0.1096 372 HIS B CA  
12831 C C   . HIS B 372 ? 0.2810 0.5236 0.3640 0.0080  0.0135  -0.1073 372 HIS B C   
12832 O O   . HIS B 372 ? 0.3097 0.4995 0.3695 0.0104  0.0422  -0.1223 372 HIS B O   
12833 C CB  . HIS B 372 ? 0.2381 0.4682 0.3362 -0.0281 0.0009  -0.0980 372 HIS B CB  
12834 C CG  . HIS B 372 ? 0.2298 0.4444 0.3312 -0.0105 -0.0141 -0.0708 372 HIS B CG  
12835 N ND1 . HIS B 372 ? 0.2333 0.3978 0.3277 0.0102  0.0038  -0.0576 372 HIS B ND1 
12836 C CD2 . HIS B 372 ? 0.2151 0.4282 0.3312 -0.0446 -0.0017 -0.0597 372 HIS B CD2 
12837 C CE1 . HIS B 372 ? 0.2529 0.4075 0.3287 -0.0181 -0.0021 -0.0649 372 HIS B CE1 
12838 N NE2 . HIS B 372 ? 0.2273 0.4031 0.3273 -0.0204 -0.0142 -0.0668 372 HIS B NE2 
12846 N N   . PRO B 373 ? 0.2471 0.5222 0.3801 -0.0001 0.0033  -0.1096 373 PRO B N   
12847 C CA  . PRO B 373 ? 0.2658 0.5407 0.3865 0.0297  -0.0167 -0.1213 373 PRO B CA  
12848 C C   . PRO B 373 ? 0.2354 0.5032 0.3746 0.0357  0.0038  -0.1469 373 PRO B C   
12849 O O   . PRO B 373 ? 0.2799 0.5175 0.3811 0.0345  0.0227  -0.1443 373 PRO B O   
12850 C CB  . PRO B 373 ? 0.2341 0.5538 0.3986 0.0631  -0.0245 -0.1177 373 PRO B CB  
12851 C CG  . PRO B 373 ? 0.2519 0.5577 0.3942 0.0495  -0.0260 -0.1130 373 PRO B CG  
12852 C CD  . PRO B 373 ? 0.1780 0.5522 0.3846 0.0560  -0.0268 -0.1088 373 PRO B CD  
12860 N N   . LEU B 374 ? 0.2354 0.4717 0.3641 0.0319  -0.0152 -0.1456 374 LEU B N   
12861 C CA  . LEU B 374 ? 0.2439 0.4238 0.3519 0.0037  -0.0203 -0.1313 374 LEU B CA  
12862 C C   . LEU B 374 ? 0.2611 0.4026 0.3404 0.0233  -0.0224 -0.1180 374 LEU B C   
12863 O O   . LEU B 374 ? 0.2692 0.4013 0.3415 0.0275  -0.0402 -0.1080 374 LEU B O   
12864 C CB  . LEU B 374 ? 0.2215 0.4223 0.3516 -0.0359 -0.0107 -0.1255 374 LEU B CB  
12865 C CG  . LEU B 374 ? 0.2569 0.4274 0.3557 0.0103  -0.0350 -0.1042 374 LEU B CG  
12866 C CD1 . LEU B 374 ? 0.3768 0.4337 0.3600 0.0503  -0.0167 -0.0924 374 LEU B CD1 
12867 C CD2 . LEU B 374 ? 0.2740 0.4435 0.3583 0.0348  -0.0010 -0.0899 374 LEU B CD2 
12879 N N   . VAL B 375 ? 0.2368 0.3943 0.3282 0.0089  -0.0104 -0.0958 375 VAL B N   
12880 C CA  . VAL B 375 ? 0.2292 0.3660 0.3241 0.0035  -0.0303 -0.0793 375 VAL B CA  
12881 C C   . VAL B 375 ? 0.2238 0.3621 0.3131 0.0119  -0.0184 -0.0895 375 VAL B C   
12882 O O   . VAL B 375 ? 0.2909 0.3884 0.3265 -0.0006 -0.0068 -0.0893 375 VAL B O   
12883 C CB  . VAL B 375 ? 0.2220 0.3182 0.3203 -0.0189 -0.0174 -0.0715 375 VAL B CB  
12884 C CG1 . VAL B 375 ? 0.2436 0.3425 0.3222 -0.0557 0.0172  -0.0572 375 VAL B CG1 
12885 C CG2 . VAL B 375 ? 0.2077 0.3267 0.3217 0.0172  -0.0118 -0.0916 375 VAL B CG2 
12895 N N   . GLY B 376 ? 0.2131 0.3368 0.3039 -0.0160 -0.0141 -0.1150 376 GLY B N   
12896 C CA  . GLY B 376 ? 0.2657 0.3415 0.2947 -0.0398 -0.0075 -0.1035 376 GLY B CA  
12897 C C   . GLY B 376 ? 0.2439 0.3452 0.2864 -0.0280 0.0130  -0.1056 376 GLY B C   
12898 O O   . GLY B 376 ? 0.2240 0.3677 0.3014 -0.0356 0.0302  -0.1011 376 GLY B O   
12902 N N   . GLU B 377 ? 0.2284 0.3838 0.2802 -0.0007 -0.0035 -0.0720 377 GLU B N   
12903 C CA  . GLU B 377 ? 0.2430 0.3150 0.2697 -0.0397 0.0207  -0.0559 377 GLU B CA  
12904 C C   . GLU B 377 ? 0.2230 0.2796 0.2778 -0.0728 0.0229  -0.0530 377 GLU B C   
12905 O O   . GLU B 377 ? 0.2298 0.2644 0.2852 -0.0473 0.0248  -0.0458 377 GLU B O   
12906 C CB  . GLU B 377 ? 0.2221 0.2912 0.2532 -0.0472 0.0185  -0.0402 377 GLU B CB  
12907 C CG  . GLU B 377 ? 0.2283 0.2795 0.2404 -0.1192 0.0044  -0.0181 377 GLU B CG  
12908 C CD  . GLU B 377 ? 0.2672 0.2993 0.2313 -0.1081 0.0309  -0.0191 377 GLU B CD  
12909 O OE1 . GLU B 377 ? 0.2150 0.2671 0.2325 -0.0360 0.0087  -0.0015 377 GLU B OE1 
12910 O OE2 . GLU B 377 ? 0.3739 0.3809 0.2435 -0.1100 0.0664  -0.0083 377 GLU B OE2 
12917 N N   . VAL B 378 ? 0.2144 0.2383 0.2813 -0.0644 0.0134  -0.0478 378 VAL B N   
12918 C CA  . VAL B 378 ? 0.2074 0.2249 0.2738 -0.0727 0.0134  -0.0578 378 VAL B CA  
12919 C C   . VAL B 378 ? 0.1999 0.2108 0.2533 -0.0294 0.0225  -0.0490 378 VAL B C   
12920 O O   . VAL B 378 ? 0.2285 0.2865 0.2522 -0.0494 0.0411  -0.0581 378 VAL B O   
12921 C CB  . VAL B 378 ? 0.2155 0.2598 0.3137 -0.0585 -0.0018 -0.0602 378 VAL B CB  
12922 C CG1 . VAL B 378 ? 0.2579 0.2757 0.3266 -0.0408 0.0021  -0.0715 378 VAL B CG1 
12923 C CG2 . VAL B 378 ? 0.2280 0.3252 0.3273 -0.0554 0.0088  -0.0514 378 VAL B CG2 
12933 N N   . ARG B 379 ? 0.2401 0.2377 0.2432 -0.0395 0.0188  -0.0335 379 ARG B N   
12934 C CA  . ARG B 379 ? 0.1698 0.2618 0.2193 -0.0514 0.0241  -0.0040 379 ARG B CA  
12935 C C   . ARG B 379 ? 0.1722 0.2590 0.2131 -0.0327 0.0127  -0.0104 379 ARG B C   
12936 O O   . ARG B 379 ? 0.1904 0.2613 0.2279 -0.0262 0.0150  -0.0293 379 ARG B O   
12937 C CB  . ARG B 379 ? 0.1804 0.2758 0.2073 -0.0169 0.0281  -0.0140 379 ARG B CB  
12938 C CG  . ARG B 379 ? 0.1993 0.2959 0.2046 -0.0253 0.0504  -0.0171 379 ARG B CG  
12939 C CD  . ARG B 379 ? 0.1448 0.2918 0.2097 -0.0059 0.0323  -0.0291 379 ARG B CD  
12940 N NE  . ARG B 379 ? 0.1771 0.2826 0.2125 -0.0597 0.0145  -0.0175 379 ARG B NE  
12941 C CZ  . ARG B 379 ? 0.1785 0.2684 0.2184 -0.0665 0.0258  -0.0358 379 ARG B CZ  
12942 N NH1 . ARG B 379 ? 0.1785 0.2328 0.2328 -0.0177 0.0251  -0.0400 379 ARG B NH1 
12943 N NH2 . ARG B 379 ? 0.1954 0.2872 0.2062 -0.0061 0.0223  -0.0373 379 ARG B NH2 
12957 N N   . GLY B 380 ? 0.2034 0.2698 0.2080 -0.0255 0.0231  0.0016  380 GLY B N   
12958 C CA  . GLY B 380 ? 0.2138 0.2628 0.2010 -0.0635 0.0173  0.0075  380 GLY B CA  
12959 C C   . GLY B 380 ? 0.1966 0.2247 0.2040 -0.0548 0.0212  0.0110  380 GLY B C   
12960 O O   . GLY B 380 ? 0.2408 0.2372 0.2061 -0.0560 0.0223  -0.0110 380 GLY B O   
12964 N N   . VAL B 381 ? 0.2280 0.2202 0.2132 -0.0974 0.0242  0.0179  381 VAL B N   
12965 C CA  . VAL B 381 ? 0.2338 0.2131 0.1999 -0.0824 -0.0048 0.0036  381 VAL B CA  
12966 C C   . VAL B 381 ? 0.2315 0.2293 0.1922 -0.0709 0.0192  0.0154  381 VAL B C   
12967 O O   . VAL B 381 ? 0.1772 0.2614 0.1912 -0.0507 0.0106  0.0335  381 VAL B O   
12968 C CB  . VAL B 381 ? 0.2466 0.2290 0.1942 -0.0658 -0.0149 0.0102  381 VAL B CB  
12969 C CG1 . VAL B 381 ? 0.2745 0.2005 0.2011 -0.0564 -0.0374 0.0145  381 VAL B CG1 
12970 C CG2 . VAL B 381 ? 0.2800 0.2543 0.1888 -0.0590 -0.0144 0.0271  381 VAL B CG2 
12980 N N   . GLY B 382 ? 0.2241 0.2374 0.1866 -0.0217 0.0078  -0.0018 382 GLY B N   
12981 C CA  . GLY B 382 ? 0.2552 0.1909 0.1962 -0.0501 0.0079  0.0309  382 GLY B CA  
12982 C C   . GLY B 382 ? 0.2345 0.2146 0.1961 -0.0503 0.0340  0.0236  382 GLY B C   
12983 O O   . GLY B 382 ? 0.2403 0.2412 0.2088 -0.0280 0.0540  0.0137  382 GLY B O   
12987 N N   A MET B 383 ? 0.2204 0.2150 0.1903 -0.0634 0.0320  0.0011  383 MET B N   
12988 N N   B MET B 383 ? 0.2255 0.2171 0.1949 -0.0546 0.0293  0.0084  383 MET B N   
12989 C CA  A MET B 383 ? 0.2103 0.1944 0.1981 -0.0758 0.0259  0.0122  383 MET B CA  
12990 C CA  B MET B 383 ? 0.2225 0.2107 0.2010 -0.0535 0.0220  0.0108  383 MET B CA  
12991 C C   A MET B 383 ? 0.2087 0.2069 0.1881 -0.0735 0.0258  0.0168  383 MET B C   
12992 C C   B MET B 383 ? 0.2179 0.2148 0.1921 -0.0588 0.0205  0.0097  383 MET B C   
12993 O O   A MET B 383 ? 0.2107 0.2234 0.1910 -0.0636 0.0324  -0.0012 383 MET B O   
12994 O O   B MET B 383 ? 0.2197 0.2218 0.1950 -0.0567 0.0254  0.0013  383 MET B O   
12995 C CB  A MET B 383 ? 0.2389 0.2267 0.2227 -0.1050 0.0309  0.0151  383 MET B CB  
12996 C CB  B MET B 383 ? 0.2407 0.2316 0.2188 -0.0576 0.0213  0.0139  383 MET B CB  
12997 C CG  A MET B 383 ? 0.2377 0.2365 0.2394 -0.0882 0.0445  0.0206  383 MET B CG  
12998 C CG  B MET B 383 ? 0.2355 0.2387 0.2307 -0.0370 0.0264  0.0194  383 MET B CG  
12999 S SD  A MET B 383 ? 0.2629 0.2304 0.2425 -0.1040 0.0301  -0.0111 383 MET B SD  
13000 S SD  B MET B 383 ? 0.2408 0.2511 0.2377 -0.0434 0.0248  0.0105  383 MET B SD  
13001 C CE  A MET B 383 ? 0.3078 0.2597 0.2443 -0.1125 0.0462  -0.0183 383 MET B CE  
13002 C CE  B MET B 383 ? 0.2519 0.2469 0.2387 -0.0822 0.0194  -0.0037 383 MET B CE  
13021 N N   . LEU B 384 ? 0.2154 0.2105 0.1866 -0.0556 0.0061  -0.0058 384 LEU B N   
13022 C CA  . LEU B 384 ? 0.2110 0.1734 0.1923 -0.0878 0.0081  0.0014  384 LEU B CA  
13023 C C   . LEU B 384 ? 0.1703 0.2326 0.1834 -0.0562 0.0237  -0.0012 384 LEU B C   
13024 O O   . LEU B 384 ? 0.2333 0.2730 0.1921 -0.0417 0.0322  -0.0307 384 LEU B O   
13025 C CB  . LEU B 384 ? 0.1839 0.1933 0.2004 -0.0738 0.0139  0.0153  384 LEU B CB  
13026 C CG  . LEU B 384 ? 0.1731 0.2134 0.2179 -0.0932 0.0154  0.0246  384 LEU B CG  
13027 C CD1 . LEU B 384 ? 0.1974 0.1930 0.2246 -0.0514 0.0100  0.0195  384 LEU B CD1 
13028 C CD2 . LEU B 384 ? 0.2318 0.2355 0.2186 -0.0921 0.0036  0.0241  384 LEU B CD2 
13041 N N   . ALA B 385 ? 0.1728 0.2003 0.1858 -0.0534 0.0022  -0.0061 385 ALA B N   
13042 C CA  . ALA B 385 ? 0.1356 0.2161 0.1997 -0.0660 0.0005  -0.0083 385 ALA B CA  
13043 C C   . ALA B 385 ? 0.1990 0.2318 0.1897 -0.0259 -0.0030 -0.0068 385 ALA B C   
13044 O O   . ALA B 385 ? 0.1891 0.2679 0.1812 -0.0693 0.0105  -0.0258 385 ALA B O   
13045 C CB  . ALA B 385 ? 0.1648 0.2518 0.2261 -0.0733 0.0168  -0.0088 385 ALA B CB  
13051 N N   . ALA B 386 ? 0.2044 0.2408 0.2004 -0.0744 0.0004  -0.0116 386 ALA B N   
13052 C CA  . ALA B 386 ? 0.2029 0.2102 0.2140 -0.0812 0.0108  -0.0349 386 ALA B CA  
13053 C C   . ALA B 386 ? 0.2045 0.2697 0.2158 -0.0708 0.0162  -0.0318 386 ALA B C   
13054 O O   . ALA B 386 ? 0.2204 0.2592 0.2186 -0.0518 0.0246  -0.0281 386 ALA B O   
13055 C CB  . ALA B 386 ? 0.2097 0.2063 0.2258 -0.0572 0.0169  -0.0211 386 ALA B CB  
13061 N N   . LEU B 387 ? 0.1988 0.2584 0.2170 -0.0176 0.0053  -0.0334 387 LEU B N   
13062 C CA  . LEU B 387 ? 0.1893 0.2881 0.2319 -0.0213 0.0078  -0.0402 387 LEU B CA  
13063 C C   . LEU B 387 ? 0.2004 0.3054 0.2335 -0.0380 0.0080  -0.0460 387 LEU B C   
13064 O O   . LEU B 387 ? 0.2653 0.3181 0.2233 -0.0220 0.0060  -0.0155 387 LEU B O   
13065 C CB  . LEU B 387 ? 0.2013 0.2948 0.2430 -0.0423 -0.0012 -0.0386 387 LEU B CB  
13066 C CG  . LEU B 387 ? 0.1943 0.2649 0.2670 -0.0839 -0.0153 -0.0626 387 LEU B CG  
13067 C CD1 . LEU B 387 ? 0.2125 0.3044 0.2826 -0.1018 -0.0234 -0.0716 387 LEU B CD1 
13068 C CD2 . LEU B 387 ? 0.2407 0.2847 0.2672 -0.0674 -0.0240 -0.0679 387 LEU B CD2 
13080 N N   . GLU B 388 ? 0.1879 0.3028 0.2292 -0.0073 -0.0063 -0.0787 388 GLU B N   
13081 C CA  . GLU B 388 ? 0.2245 0.3303 0.2478 -0.0245 -0.0218 -0.0656 388 GLU B CA  
13082 C C   . GLU B 388 ? 0.2049 0.3242 0.2661 -0.0164 -0.0407 -0.0745 388 GLU B C   
13083 O O   . GLU B 388 ? 0.2316 0.3494 0.2835 -0.0110 -0.0357 -0.0519 388 GLU B O   
13084 C CB  . GLU B 388 ? 0.2217 0.2978 0.2434 -0.0477 -0.0370 -0.0379 388 GLU B CB  
13085 C CG  . GLU B 388 ? 0.2465 0.3036 0.2496 -0.0007 -0.0415 -0.0449 388 GLU B CG  
13086 C CD  . GLU B 388 ? 0.2395 0.2613 0.2444 0.0014  -0.0586 -0.0312 388 GLU B CD  
13087 O OE1 . GLU B 388 ? 0.2446 0.2782 0.2443 -0.0156 -0.0712 -0.0207 388 GLU B OE1 
13088 O OE2 . GLU B 388 ? 0.2946 0.2608 0.2418 -0.0181 -0.0656 -0.0358 388 GLU B OE2 
13095 N N   . PHE B 389 ? 0.2328 0.3582 0.2724 -0.0172 -0.0475 -0.0708 389 PHE B N   
13096 C CA  . PHE B 389 ? 0.1937 0.3216 0.2821 -0.0108 -0.0882 -0.1008 389 PHE B CA  
13097 C C   . PHE B 389 ? 0.2330 0.3771 0.3403 0.0288  -0.0846 -0.1062 389 PHE B C   
13098 O O   . PHE B 389 ? 0.2486 0.3986 0.3494 0.0343  -0.1058 -0.1242 389 PHE B O   
13099 C CB  . PHE B 389 ? 0.2358 0.3366 0.2712 0.0094  -0.0825 -0.0744 389 PHE B CB  
13100 C CG  . PHE B 389 ? 0.1770 0.3247 0.2600 0.0009  -0.0373 -0.0818 389 PHE B CG  
13101 C CD1 . PHE B 389 ? 0.2108 0.3180 0.2662 -0.0107 -0.0090 -0.0677 389 PHE B CD1 
13102 C CD2 . PHE B 389 ? 0.1958 0.3229 0.2544 -0.0014 -0.0205 -0.0758 389 PHE B CD2 
13103 C CE1 . PHE B 389 ? 0.2052 0.3133 0.2713 -0.0222 -0.0063 -0.0727 389 PHE B CE1 
13104 C CE2 . PHE B 389 ? 0.1733 0.3389 0.2568 -0.0284 -0.0160 -0.0663 389 PHE B CE2 
13105 C CZ  . PHE B 389 ? 0.1822 0.2924 0.2654 -0.0467 -0.0032 -0.0596 389 PHE B CZ  
13115 N N   . SER B 390 ? 0.2549 0.3888 0.3890 0.0245  -0.0962 -0.1411 390 SER B N   
13116 C CA  . SER B 390 ? 0.2583 0.3533 0.4237 0.0774  -0.1069 -0.1808 390 SER B CA  
13117 C C   . SER B 390 ? 0.2857 0.4275 0.4518 0.0843  -0.1054 -0.2000 390 SER B C   
13118 O O   . SER B 390 ? 0.3135 0.4540 0.4500 0.0628  -0.0780 -0.2158 390 SER B O   
13119 C CB  . SER B 390 ? 0.3317 0.3654 0.4315 0.1024  -0.1263 -0.1916 390 SER B CB  
13120 O OG  . SER B 390 ? 0.3405 0.3927 0.4399 0.1279  -0.1596 -0.1926 390 SER B OG  
13126 N N   . PRO B 391 ? 0.2781 0.4841 0.4810 0.1473  -0.1241 -0.2159 391 PRO B N   
13127 C CA  . PRO B 391 ? 0.3200 0.5175 0.4970 0.1828  -0.1059 -0.2302 391 PRO B CA  
13128 C C   . PRO B 391 ? 0.3476 0.5624 0.5244 0.1973  -0.1055 -0.2430 391 PRO B C   
13129 O O   . PRO B 391 ? 0.3834 0.5980 0.5243 0.1979  -0.0983 -0.2547 391 PRO B O   
13130 C CB  . PRO B 391 ? 0.3310 0.5064 0.4952 0.1833  -0.1055 -0.2351 391 PRO B CB  
13131 C CG  . PRO B 391 ? 0.3097 0.5070 0.4933 0.1661  -0.1243 -0.2218 391 PRO B CG  
13132 C CD  . PRO B 391 ? 0.2996 0.4930 0.4870 0.1720  -0.1257 -0.2153 391 PRO B CD  
13140 N N   . ALA B 392 ? 0.4035 0.5835 0.5431 0.2050  -0.1103 -0.2594 392 ALA B N   
13141 C CA  . ALA B 392 ? 0.3844 0.6229 0.5687 0.1880  -0.1152 -0.2555 392 ALA B CA  
13142 C C   . ALA B 392 ? 0.3743 0.6268 0.5781 0.1809  -0.0982 -0.2550 392 ALA B C   
13143 O O   . ALA B 392 ? 0.4033 0.6367 0.5793 0.1845  -0.1004 -0.2589 392 ALA B O   
13144 C CB  . ALA B 392 ? 0.4207 0.6539 0.5741 0.1687  -0.1303 -0.2631 392 ALA B CB  
13150 N N   . PRO B 393 ? 0.3154 0.6081 0.5856 0.1691  -0.0840 -0.2476 393 PRO B N   
13151 C CA  . PRO B 393 ? 0.3226 0.5976 0.5795 0.1804  -0.0763 -0.2502 393 PRO B CA  
13152 C C   . PRO B 393 ? 0.3981 0.6389 0.5840 0.1753  -0.0914 -0.2472 393 PRO B C   
13153 O O   . PRO B 393 ? 0.3759 0.6488 0.5813 0.1553  -0.0975 -0.2331 393 PRO B O   
13154 C CB  . PRO B 393 ? 0.2885 0.6012 0.5873 0.1413  -0.0667 -0.2482 393 PRO B CB  
13155 C CG  . PRO B 393 ? 0.3102 0.5888 0.5932 0.1261  -0.0681 -0.2311 393 PRO B CG  
13156 C CD  . PRO B 393 ? 0.2779 0.5971 0.5898 0.1493  -0.0685 -0.2329 393 PRO B CD  
13164 N N   . ALA B 394 ? 0.4658 0.6660 0.5848 0.1842  -0.1053 -0.2503 394 ALA B N   
13165 C CA  . ALA B 394 ? 0.5620 0.6680 0.5819 0.1421  -0.1387 -0.2670 394 ALA B CA  
13166 C C   . ALA B 394 ? 0.6726 0.6671 0.5811 0.1580  -0.1737 -0.2504 394 ALA B C   
13167 O O   . ALA B 394 ? 0.6949 0.6812 0.5870 0.1708  -0.1715 -0.2545 394 ALA B O   
13168 C CB  . ALA B 394 ? 0.5769 0.6856 0.5856 0.1091  -0.1267 -0.2698 394 ALA B CB  
13174 N N   . ARG B 395 ? 0.7675 0.6423 0.5761 0.1312  -0.2062 -0.2244 395 ARG B N   
13175 C CA  . ARG B 395 ? 0.8281 0.6150 0.5781 0.0971  -0.2423 -0.1946 395 ARG B CA  
13176 C C   . ARG B 395 ? 0.7507 0.5466 0.5696 0.0622  -0.2534 -0.1830 395 ARG B C   
13177 O O   . ARG B 395 ? 0.7990 0.5276 0.5711 0.0676  -0.2619 -0.1953 395 ARG B O   
13178 C CB  . ARG B 395 ? 0.9642 0.6454 0.5927 0.1147  -0.2540 -0.1684 395 ARG B CB  
13179 C CG  . ARG B 395 ? 1.0671 0.6780 0.6046 0.1058  -0.2578 -0.1477 395 ARG B CG  
13180 C CD  . ARG B 395 ? 1.1588 0.6996 0.6159 0.1044  -0.2508 -0.1262 395 ARG B CD  
13181 N NE  . ARG B 395 ? 1.2309 0.7241 0.6238 0.0989  -0.2369 -0.1134 395 ARG B NE  
13182 C CZ  . ARG B 395 ? 1.2696 0.7311 0.6280 0.0988  -0.2258 -0.1039 395 ARG B CZ  
13183 N NH1 . ARG B 395 ? 1.2874 0.7221 0.6306 0.0749  -0.2247 -0.0978 395 ARG B NH1 
13184 N NH2 . ARG B 395 ? 1.2674 0.7280 0.6254 0.1193  -0.2243 -0.1081 395 ARG B NH2 
13198 N N   . ARG B 396 ? 0.6400 0.5093 0.5590 0.0463  -0.2396 -0.1628 396 ARG B N   
13199 C CA  . ARG B 396 ? 0.5658 0.4806 0.5444 0.0293  -0.2104 -0.1503 396 ARG B CA  
13200 C C   . ARG B 396 ? 0.5659 0.5017 0.5608 0.0341  -0.2211 -0.1219 396 ARG B C   
13201 O O   . ARG B 396 ? 0.6581 0.5396 0.5685 0.0261  -0.2408 -0.0824 396 ARG B O   
13202 C CB  . ARG B 396 ? 0.4682 0.4389 0.5186 0.0195  -0.1854 -0.1548 396 ARG B CB  
13203 C CG  . ARG B 396 ? 0.3839 0.4393 0.4941 0.0494  -0.1209 -0.1458 396 ARG B CG  
13204 C CD  . ARG B 396 ? 0.2749 0.4488 0.4684 0.0300  -0.0833 -0.1264 396 ARG B CD  
13205 N NE  . ARG B 396 ? 0.2492 0.4324 0.4487 0.0392  -0.0476 -0.1141 396 ARG B NE  
13206 C CZ  . ARG B 396 ? 0.2338 0.4096 0.4357 0.0539  -0.0262 -0.1080 396 ARG B CZ  
13207 N NH1 . ARG B 396 ? 0.1809 0.4158 0.4260 0.0243  -0.0115 -0.0848 396 ARG B NH1 
13208 N NH2 . ARG B 396 ? 0.2686 0.4135 0.4246 0.0501  0.0049  -0.1542 396 ARG B NH2 
13222 N N   . ALA B 397 ? 0.4656 0.4389 0.5615 0.0471  -0.2084 -0.1491 397 ALA B N   
13223 C CA  . ALA B 397 ? 0.4284 0.3939 0.5636 0.0787  -0.2029 -0.1747 397 ALA B CA  
13224 C C   . ALA B 397 ? 0.4190 0.3639 0.5719 0.0926  -0.1953 -0.1639 397 ALA B C   
13225 O O   . ALA B 397 ? 0.4069 0.3356 0.5799 0.0990  -0.2002 -0.1388 397 ALA B O   
13226 C CB  . ALA B 397 ? 0.4266 0.4094 0.5654 0.1118  -0.1909 -0.1781 397 ALA B CB  
13232 N N   . PHE B 398 ? 0.4374 0.3553 0.5689 0.0816  -0.1941 -0.1708 398 PHE B N   
13233 C CA  . PHE B 398 ? 0.4526 0.3814 0.5770 0.1118  -0.1891 -0.1509 398 PHE B CA  
13234 C C   . PHE B 398 ? 0.4534 0.3637 0.5623 0.0933  -0.1872 -0.1270 398 PHE B C   
13235 O O   . PHE B 398 ? 0.4632 0.3715 0.5582 0.1128  -0.1834 -0.1149 398 PHE B O   
13236 C CB  . PHE B 398 ? 0.4730 0.4326 0.5975 0.1282  -0.1966 -0.1454 398 PHE B CB  
13237 C CG  . PHE B 398 ? 0.5370 0.4731 0.6135 0.1615  -0.2064 -0.1603 398 PHE B CG  
13238 C CD1 . PHE B 398 ? 0.5194 0.4674 0.6182 0.2144  -0.2122 -0.1607 398 PHE B CD1 
13239 C CD2 . PHE B 398 ? 0.5872 0.5145 0.6262 0.1819  -0.2180 -0.1524 398 PHE B CD2 
13240 C CE1 . PHE B 398 ? 0.5362 0.4985 0.6245 0.2156  -0.2272 -0.1668 398 PHE B CE1 
13241 C CE2 . PHE B 398 ? 0.5868 0.5196 0.6333 0.2196  -0.2313 -0.1533 398 PHE B CE2 
13242 C CZ  . PHE B 398 ? 0.5413 0.5148 0.6334 0.2323  -0.2328 -0.1624 398 PHE B CZ  
13252 N N   . PHE B 399 ? 0.4475 0.3563 0.5500 0.0566  -0.2007 -0.1334 399 PHE B N   
13253 C CA  . PHE B 399 ? 0.4385 0.3909 0.5392 0.0460  -0.2136 -0.1216 399 PHE B CA  
13254 C C   . PHE B 399 ? 0.4717 0.3377 0.5462 0.0399  -0.2436 -0.0943 399 PHE B C   
13255 O O   . PHE B 399 ? 0.5167 0.3259 0.5488 0.0687  -0.2429 -0.0755 399 PHE B O   
13256 C CB  . PHE B 399 ? 0.4174 0.4000 0.5217 0.0813  -0.1860 -0.1660 399 PHE B CB  
13257 C CG  . PHE B 399 ? 0.4238 0.3852 0.5050 0.1004  -0.1756 -0.1981 399 PHE B CG  
13258 C CD1 . PHE B 399 ? 0.4161 0.3913 0.4971 0.1235  -0.1989 -0.1886 399 PHE B CD1 
13259 C CD2 . PHE B 399 ? 0.3874 0.3573 0.4945 0.1364  -0.1766 -0.2157 399 PHE B CD2 
13260 C CE1 . PHE B 399 ? 0.4324 0.3732 0.4953 0.1178  -0.1787 -0.2073 399 PHE B CE1 
13261 C CE2 . PHE B 399 ? 0.3985 0.3707 0.4849 0.1234  -0.1828 -0.2224 399 PHE B CE2 
13262 C CZ  . PHE B 399 ? 0.4257 0.3689 0.4869 0.1333  -0.1725 -0.2182 399 PHE B CZ  
13272 N N   . ASP B 400 ? 0.5040 0.3334 0.5579 0.0486  -0.2311 -0.0851 400 ASP B N   
13273 C CA  . ASP B 400 ? 0.5261 0.3323 0.5631 0.0582  -0.2333 -0.0637 400 ASP B CA  
13274 C C   . ASP B 400 ? 0.5038 0.2506 0.5466 0.0334  -0.2144 -0.0580 400 ASP B C   
13275 O O   . ASP B 400 ? 0.5057 0.2346 0.5472 0.0111  -0.1970 -0.0548 400 ASP B O   
13276 C CB  . ASP B 400 ? 0.5717 0.3852 0.5871 0.1032  -0.2510 -0.0434 400 ASP B CB  
13277 C CG  . ASP B 400 ? 0.6371 0.4049 0.6114 0.1211  -0.2579 -0.0459 400 ASP B CG  
13278 O OD1 . ASP B 400 ? 0.6554 0.4130 0.6182 0.1375  -0.2530 -0.0504 400 ASP B OD1 
13279 O OD2 . ASP B 400 ? 0.7351 0.4150 0.6289 0.1209  -0.2331 -0.0604 400 ASP B OD2 
13284 N N   . PRO B 401 ? 0.5125 0.2489 0.5397 -0.0046 -0.1893 -0.0579 401 PRO B N   
13285 C CA  . PRO B 401 ? 0.5012 0.2947 0.5331 -0.0229 -0.1597 -0.0448 401 PRO B CA  
13286 C C   . PRO B 401 ? 0.4813 0.3388 0.5260 -0.0354 -0.1396 -0.0237 401 PRO B C   
13287 O O   . PRO B 401 ? 0.4637 0.3461 0.5301 -0.0148 -0.1253 -0.0187 401 PRO B O   
13288 C CB  . PRO B 401 ? 0.5193 0.3016 0.5352 -0.0418 -0.1518 -0.0498 401 PRO B CB  
13289 C CG  . PRO B 401 ? 0.5289 0.3384 0.5476 -0.0504 -0.1474 -0.0489 401 PRO B CG  
13290 C CD  . PRO B 401 ? 0.5302 0.3133 0.5487 -0.0271 -0.1702 -0.0573 401 PRO B CD  
13298 N N   . ALA B 402 ? 0.4832 0.3591 0.5137 -0.0286 -0.1482 -0.0174 402 ALA B N   
13299 C CA  . ALA B 402 ? 0.4668 0.3540 0.5028 0.0222  -0.1377 -0.0108 402 ALA B CA  
13300 C C   . ALA B 402 ? 0.4228 0.3251 0.4908 -0.0076 -0.1296 0.0047  402 ALA B C   
13301 O O   . ALA B 402 ? 0.4153 0.3418 0.4931 -0.0155 -0.1333 0.0223  402 ALA B O   
13302 C CB  . ALA B 402 ? 0.5113 0.3324 0.5030 0.0325  -0.1189 -0.0135 402 ALA B CB  
13308 N N   . LEU B 403 ? 0.3828 0.3038 0.4761 0.0128  -0.1184 -0.0135 403 LEU B N   
13309 C CA  . LEU B 403 ? 0.3336 0.2865 0.4699 0.0198  -0.1236 0.0154  403 LEU B CA  
13310 C C   . LEU B 403 ? 0.2613 0.3138 0.4509 0.0047  -0.1146 0.0234  403 LEU B C   
13311 O O   . LEU B 403 ? 0.2748 0.3200 0.4532 -0.0246 -0.0999 0.0137  403 LEU B O   
13312 C CB  . LEU B 403 ? 0.3778 0.3040 0.4821 0.0093  -0.1387 0.0120  403 LEU B CB  
13313 C CG  . LEU B 403 ? 0.3843 0.3690 0.4954 -0.0303 -0.1558 -0.0031 403 LEU B CG  
13314 C CD1 . LEU B 403 ? 0.4239 0.3768 0.4998 -0.0323 -0.1581 -0.0080 403 LEU B CD1 
13315 C CD2 . LEU B 403 ? 0.3903 0.3860 0.5100 0.0275  -0.1538 0.0048  403 LEU B CD2 
13327 N N   . LYS B 404 ? 0.2475 0.3299 0.4367 0.0063  -0.1165 0.0352  404 LYS B N   
13328 C CA  . LYS B 404 ? 0.2662 0.3336 0.4238 0.0376  -0.1136 0.0148  404 LYS B CA  
13329 C C   . LYS B 404 ? 0.2544 0.2693 0.3927 0.0047  -0.1139 -0.0199 404 LYS B C   
13330 O O   . LYS B 404 ? 0.2797 0.1784 0.3885 0.0233  -0.1243 -0.0247 404 LYS B O   
13331 C CB  . LYS B 404 ? 0.3468 0.4124 0.4421 0.0432  -0.1031 0.0255  404 LYS B CB  
13332 C CG  . LYS B 404 ? 0.4794 0.5317 0.4697 0.0677  -0.0839 0.0348  404 LYS B CG  
13333 C CD  . LYS B 404 ? 0.6157 0.6571 0.4876 0.0353  -0.0698 0.0326  404 LYS B CD  
13334 C CE  . LYS B 404 ? 0.7183 0.7611 0.4977 -0.0077 -0.0678 0.0364  404 LYS B CE  
13335 N NZ  . LYS B 404 ? 0.7674 0.8031 0.5074 -0.0168 -0.0622 0.0433  404 LYS B NZ  
13349 N N   . VAL B 405 ? 0.2695 0.2408 0.3697 -0.0264 -0.0946 -0.0313 405 VAL B N   
13350 C CA  . VAL B 405 ? 0.2517 0.2153 0.3487 -0.0420 -0.0787 -0.0239 405 VAL B CA  
13351 C C   . VAL B 405 ? 0.2008 0.2305 0.3278 -0.0552 -0.0718 -0.0348 405 VAL B C   
13352 O O   . VAL B 405 ? 0.1974 0.2260 0.3133 -0.0442 -0.0710 -0.0403 405 VAL B O   
13353 C CB  . VAL B 405 ? 0.2471 0.2143 0.3343 0.0094  -0.0923 -0.0070 405 VAL B CB  
13354 C CG1 . VAL B 405 ? 0.2599 0.2474 0.3286 0.0185  -0.0878 -0.0346 405 VAL B CG1 
13355 C CG2 . VAL B 405 ? 0.2596 0.2242 0.3352 0.0269  -0.0842 -0.0303 405 VAL B CG2 
13365 N N   . GLY B 406 ? 0.2037 0.2340 0.3199 0.0174  -0.0720 -0.0287 406 GLY B N   
13366 C CA  . GLY B 406 ? 0.2183 0.2230 0.3049 0.0006  -0.0716 -0.0055 406 GLY B CA  
13367 C C   . GLY B 406 ? 0.2423 0.2520 0.3033 -0.0384 -0.0464 -0.0132 406 GLY B C   
13368 O O   . GLY B 406 ? 0.1872 0.2580 0.3022 -0.0560 -0.0567 -0.0085 406 GLY B O   
13372 N N   . PRO B 407 ? 0.2377 0.2173 0.2879 -0.0587 -0.0368 -0.0086 407 PRO B N   
13373 C CA  . PRO B 407 ? 0.2051 0.2425 0.2847 -0.0233 -0.0286 -0.0058 407 PRO B CA  
13374 C C   . PRO B 407 ? 0.2074 0.2882 0.2782 -0.0115 -0.0376 -0.0216 407 PRO B C   
13375 O O   . PRO B 407 ? 0.2157 0.3262 0.2799 -0.0535 -0.0404 -0.0116 407 PRO B O   
13376 C CB  . PRO B 407 ? 0.2329 0.2287 0.2912 -0.0238 -0.0567 -0.0202 407 PRO B CB  
13377 C CG  . PRO B 407 ? 0.2481 0.2052 0.2838 -0.0060 -0.0611 -0.0569 407 PRO B CG  
13378 C CD  . PRO B 407 ? 0.2479 0.2352 0.2927 -0.0367 -0.0450 -0.0354 407 PRO B CD  
13386 N N   . ARG B 408 ? 0.1904 0.3065 0.2834 -0.0050 -0.0381 -0.0339 408 ARG B N   
13387 C CA  . ARG B 408 ? 0.2113 0.2925 0.2811 -0.0355 -0.0414 -0.0393 408 ARG B CA  
13388 C C   . ARG B 408 ? 0.1539 0.2709 0.2643 -0.0375 -0.0341 -0.0302 408 ARG B C   
13389 O O   . ARG B 408 ? 0.1829 0.3057 0.2685 -0.0361 0.0000  -0.0285 408 ARG B O   
13390 C CB  . ARG B 408 ? 0.2289 0.3035 0.2874 0.0021  -0.0815 -0.0456 408 ARG B CB  
13391 C CG  . ARG B 408 ? 0.2444 0.3268 0.2875 0.0486  -0.1002 -0.0421 408 ARG B CG  
13392 C CD  . ARG B 408 ? 0.2387 0.3556 0.3017 0.0256  -0.0855 -0.0547 408 ARG B CD  
13393 N NE  . ARG B 408 ? 0.2484 0.3453 0.3209 0.0489  -0.1139 -0.0556 408 ARG B NE  
13394 C CZ  . ARG B 408 ? 0.2541 0.3689 0.3275 0.0214  -0.0744 -0.0919 408 ARG B CZ  
13395 N NH1 . ARG B 408 ? 0.2530 0.4110 0.3375 0.0034  -0.0793 -0.1238 408 ARG B NH1 
13396 N NH2 . ARG B 408 ? 0.2529 0.3857 0.3239 0.0268  -0.0777 -0.0906 408 ARG B NH2 
13410 N N   . VAL B 409 ? 0.1875 0.2677 0.2690 -0.0466 -0.0213 -0.0277 409 VAL B N   
13411 C CA  . VAL B 409 ? 0.2126 0.2907 0.2570 -0.0281 -0.0226 -0.0161 409 VAL B CA  
13412 C C   . VAL B 409 ? 0.1926 0.2878 0.2607 -0.0623 -0.0170 -0.0223 409 VAL B C   
13413 O O   . VAL B 409 ? 0.1754 0.2658 0.2551 -0.0769 -0.0204 -0.0287 409 VAL B O   
13414 C CB  . VAL B 409 ? 0.2516 0.2969 0.2547 -0.0054 -0.0328 -0.0262 409 VAL B CB  
13415 C CG1 . VAL B 409 ? 0.2476 0.2843 0.2531 -0.0066 -0.0263 -0.0240 409 VAL B CG1 
13416 C CG2 . VAL B 409 ? 0.2698 0.3075 0.2511 -0.0261 -0.0322 -0.0278 409 VAL B CG2 
13426 N N   . SER B 410 ? 0.2072 0.2720 0.2599 -0.0498 -0.0053 -0.0228 410 SER B N   
13427 C CA  . SER B 410 ? 0.1888 0.2590 0.2529 -0.0290 -0.0156 -0.0108 410 SER B CA  
13428 C C   . SER B 410 ? 0.1837 0.2082 0.2455 0.0328  -0.0179 -0.0009 410 SER B C   
13429 O O   . SER B 410 ? 0.1972 0.2176 0.2475 -0.0277 -0.0206 -0.0484 410 SER B O   
13430 C CB  . SER B 410 ? 0.1701 0.2336 0.2487 -0.0239 -0.0073 -0.0110 410 SER B CB  
13431 O OG  . SER B 410 ? 0.1957 0.2436 0.2478 -0.0274 0.0060  0.0000  410 SER B OG  
13437 N N   . ALA B 411 ? 0.1960 0.2580 0.2416 -0.0254 -0.0147 0.0119  411 ALA B N   
13438 C CA  . ALA B 411 ? 0.2043 0.2524 0.2396 -0.0468 -0.0104 -0.0329 411 ALA B CA  
13439 C C   . ALA B 411 ? 0.1662 0.2421 0.2483 -0.0476 0.0010  -0.0399 411 ALA B C   
13440 O O   . ALA B 411 ? 0.2044 0.2564 0.2484 -0.0416 0.0033  -0.0428 411 ALA B O   
13441 C CB  . ALA B 411 ? 0.2572 0.2601 0.2350 -0.0446 -0.0039 -0.0533 411 ALA B CB  
13447 N N   . ALA B 412 ? 0.1865 0.2642 0.2650 -0.0632 0.0011  -0.0412 412 ALA B N   
13448 C CA  . ALA B 412 ? 0.1746 0.2658 0.2665 -0.0565 0.0158  -0.0361 412 ALA B CA  
13449 C C   . ALA B 412 ? 0.1915 0.3184 0.2574 -0.0411 0.0094  -0.0506 412 ALA B C   
13450 O O   . ALA B 412 ? 0.2017 0.2771 0.2669 -0.0325 0.0180  -0.0388 412 ALA B O   
13451 C CB  . ALA B 412 ? 0.1562 0.2707 0.2810 -0.0258 0.0193  -0.0175 412 ALA B CB  
13457 N N   . ALA B 413 ? 0.1834 0.3088 0.2395 -0.0173 0.0005  -0.0594 413 ALA B N   
13458 C CA  . ALA B 413 ? 0.2014 0.2581 0.2258 -0.0416 -0.0058 -0.0216 413 ALA B CA  
13459 C C   . ALA B 413 ? 0.1830 0.2550 0.2271 -0.0479 0.0203  -0.0176 413 ALA B C   
13460 O O   . ALA B 413 ? 0.1799 0.2831 0.2226 -0.0167 0.0091  -0.0334 413 ALA B O   
13461 C CB  . ALA B 413 ? 0.1811 0.2208 0.2166 -0.0410 -0.0079 -0.0038 413 ALA B CB  
13467 N N   . MET B 414 ? 0.2135 0.2673 0.2275 -0.0776 0.0150  -0.0236 414 MET B N   
13468 C CA  . MET B 414 ? 0.1781 0.2832 0.2470 -0.0829 0.0166  -0.0199 414 MET B CA  
13469 C C   . MET B 414 ? 0.1784 0.2855 0.2645 -0.0699 0.0167  -0.0178 414 MET B C   
13470 O O   . MET B 414 ? 0.2195 0.3074 0.2661 -0.0340 0.0170  -0.0312 414 MET B O   
13471 C CB  . MET B 414 ? 0.2661 0.3367 0.2541 -0.0129 0.0129  0.0010  414 MET B CB  
13472 C CG  . MET B 414 ? 0.2630 0.3659 0.2764 -0.0303 0.0115  0.0237  414 MET B CG  
13473 S SD  . MET B 414 ? 0.2218 0.4072 0.2844 -0.0496 0.0051  0.0355  414 MET B SD  
13474 C CE  . MET B 414 ? 0.2860 0.4089 0.2801 -0.1277 0.0142  0.0538  414 MET B CE  
13484 N N   . SER B 415 ? 0.2149 0.3016 0.2722 -0.0758 -0.0113 -0.0118 415 SER B N   
13485 C CA  . SER B 415 ? 0.2836 0.3370 0.2817 -0.0916 -0.0225 0.0002  415 SER B CA  
13486 C C   . SER B 415 ? 0.2553 0.2913 0.2745 -0.1155 -0.0124 -0.0117 415 SER B C   
13487 O O   . SER B 415 ? 0.2691 0.3745 0.2789 -0.0920 -0.0216 -0.0411 415 SER B O   
13488 C CB  . SER B 415 ? 0.3836 0.4147 0.3075 -0.0789 -0.0650 0.0417  415 SER B CB  
13489 O OG  . SER B 415 ? 0.4910 0.5160 0.3487 -0.0250 -0.0695 0.0356  415 SER B OG  
13495 N N   . GLU B 416 ? 0.2488 0.2651 0.2748 -0.0798 0.0063  -0.0455 416 GLU B N   
13496 C CA  . GLU B 416 ? 0.2398 0.2820 0.2810 -0.0961 0.0056  -0.0323 416 GLU B CA  
13497 C C   . GLU B 416 ? 0.1987 0.2532 0.2608 -0.0940 0.0273  -0.0355 416 GLU B C   
13498 O O   . GLU B 416 ? 0.1978 0.2767 0.2571 -0.0725 0.0062  -0.0496 416 GLU B O   
13499 C CB  . GLU B 416 ? 0.2294 0.3448 0.3086 -0.0810 0.0151  -0.0119 416 GLU B CB  
13500 C CG  . GLU B 416 ? 0.2675 0.3564 0.3380 -0.1064 0.0120  -0.0137 416 GLU B CG  
13501 C CD  . GLU B 416 ? 0.2697 0.4219 0.3639 -0.0805 0.0116  -0.0196 416 GLU B CD  
13502 O OE1 . GLU B 416 ? 0.2794 0.4303 0.3818 -0.1576 0.0049  -0.0533 416 GLU B OE1 
13503 O OE2 . GLU B 416 ? 0.3199 0.4547 0.3644 -0.0307 -0.0020 -0.0011 416 GLU B OE2 
13510 N N   . ASN B 417 ? 0.1641 0.2689 0.2425 -0.0915 0.0142  -0.0090 417 ASN B N   
13511 C CA  . ASN B 417 ? 0.1963 0.2373 0.2410 -0.0957 0.0043  -0.0173 417 ASN B CA  
13512 C C   . ASN B 417 ? 0.1927 0.2032 0.2239 -0.0656 -0.0002 -0.0103 417 ASN B C   
13513 O O   . ASN B 417 ? 0.1993 0.2421 0.2204 -0.0788 -0.0032 0.0013  417 ASN B O   
13514 C CB  . ASN B 417 ? 0.2384 0.2981 0.2660 -0.0789 -0.0034 -0.0325 417 ASN B CB  
13515 C CG  . ASN B 417 ? 0.3282 0.2866 0.2849 -0.1137 -0.0181 -0.0220 417 ASN B CG  
13516 O OD1 . ASN B 417 ? 0.3431 0.3019 0.2866 -0.0841 -0.0091 -0.0417 417 ASN B OD1 
13517 N ND2 . ASN B 417 ? 0.4184 0.3241 0.3116 -0.1331 -0.0658 -0.0076 417 ASN B ND2 
13524 N N   . LEU B 418 ? 0.1916 0.1819 0.2208 -0.0628 -0.0013 -0.0307 418 LEU B N   
13525 C CA  . LEU B 418 ? 0.1782 0.2179 0.2225 -0.0284 -0.0004 -0.0138 418 LEU B CA  
13526 C C   . LEU B 418 ? 0.1877 0.2069 0.2226 -0.0338 0.0174  -0.0185 418 LEU B C   
13527 O O   . LEU B 418 ? 0.2017 0.2157 0.2223 -0.0688 0.0212  -0.0311 418 LEU B O   
13528 C CB  . LEU B 418 ? 0.2046 0.2359 0.2185 -0.0355 0.0196  -0.0152 418 LEU B CB  
13529 C CG  . LEU B 418 ? 0.1833 0.2503 0.2072 -0.0319 0.0320  -0.0241 418 LEU B CG  
13530 C CD1 . LEU B 418 ? 0.2134 0.2390 0.2225 -0.0529 0.0317  -0.0261 418 LEU B CD1 
13531 C CD2 . LEU B 418 ? 0.2009 0.2824 0.1969 -0.0623 0.0570  -0.0305 418 LEU B CD2 
13543 N N   . ILE B 419 ? 0.2129 0.2001 0.2108 -0.0712 0.0085  -0.0360 419 ILE B N   
13544 C CA  . ILE B 419 ? 0.1583 0.2020 0.2067 -0.0533 0.0275  -0.0403 419 ILE B CA  
13545 C C   . ILE B 419 ? 0.2046 0.1975 0.2147 -0.0006 0.0166  -0.0351 419 ILE B C   
13546 O O   . ILE B 419 ? 0.2319 0.1908 0.2242 -0.0500 0.0240  -0.0189 419 ILE B O   
13547 C CB  . ILE B 419 ? 0.1931 0.2157 0.2047 -0.0544 0.0007  -0.0099 419 ILE B CB  
13548 C CG1 . ILE B 419 ? 0.2550 0.2381 0.2000 -0.0614 0.0154  0.0003  419 ILE B CG1 
13549 C CG2 . ILE B 419 ? 0.2076 0.2758 0.2126 -0.0370 0.0071  0.0101  419 ILE B CG2 
13550 C CD1 . ILE B 419 ? 0.2440 0.2465 0.1967 -0.0345 -0.0003 0.0014  419 ILE B CD1 
13562 N N   . ALA B 420 ? 0.1964 0.2301 0.2233 -0.0393 0.0217  -0.0421 420 ALA B N   
13563 C CA  . ALA B 420 ? 0.2281 0.2287 0.2379 -0.0651 0.0345  -0.0152 420 ALA B CA  
13564 C C   . ALA B 420 ? 0.1941 0.2363 0.2520 -0.0700 0.0150  -0.0005 420 ALA B C   
13565 O O   . ALA B 420 ? 0.2406 0.2181 0.2594 -0.0374 -0.0369 -0.0216 420 ALA B O   
13566 C CB  . ALA B 420 ? 0.2471 0.2091 0.2343 -0.0870 0.0443  -0.0163 420 ALA B CB  
13572 N N   A ARG B 421 ? 0.2061 0.2690 0.2536 -0.0636 0.0041  0.0032  421 ARG B N   
13573 N N   B ARG B 421 ? 0.2025 0.2646 0.2514 -0.0617 0.0020  0.0056  421 ARG B N   
13574 C CA  A ARG B 421 ? 0.1769 0.2947 0.2649 -0.0421 0.0194  0.0129  421 ARG B CA  
13575 C CA  B ARG B 421 ? 0.1683 0.2862 0.2621 -0.0395 0.0220  0.0200  421 ARG B CA  
13576 C C   A ARG B 421 ? 0.1833 0.2393 0.2577 -0.0413 0.0043  0.0242  421 ARG B C   
13577 C C   B ARG B 421 ? 0.1827 0.2340 0.2547 -0.0409 0.0044  0.0278  421 ARG B C   
13578 O O   A ARG B 421 ? 0.2246 0.2139 0.2558 -0.0638 0.0110  0.0019  421 ARG B O   
13579 O O   B ARG B 421 ? 0.2305 0.2062 0.2516 -0.0657 0.0116  0.0015  421 ARG B O   
13580 C CB  A ARG B 421 ? 0.1888 0.3841 0.2891 -0.0686 0.0317  0.0293  421 ARG B CB  
13581 C CB  B ARG B 421 ? 0.1652 0.3669 0.2865 -0.0730 0.0416  0.0490  421 ARG B CB  
13582 C CG  A ARG B 421 ? 0.2695 0.4918 0.3059 -0.0290 0.0248  0.0508  421 ARG B CG  
13583 C CG  B ARG B 421 ? 0.2461 0.4719 0.3022 -0.0078 0.0429  0.0820  421 ARG B CG  
13584 C CD  A ARG B 421 ? 0.3188 0.5734 0.3148 -0.0298 0.0267  0.0436  421 ARG B CD  
13585 C CD  B ARG B 421 ? 0.2615 0.5462 0.3089 0.0272  0.0765  0.0863  421 ARG B CD  
13586 N NE  A ARG B 421 ? 0.3560 0.6176 0.3308 -0.0553 0.0172  0.0355  421 ARG B NE  
13587 N NE  B ARG B 421 ? 0.3058 0.6217 0.3214 0.0825  0.0984  0.0622  421 ARG B NE  
13588 C CZ  A ARG B 421 ? 0.4241 0.6459 0.3339 -0.0642 0.0493  0.0281  421 ARG B CZ  
13589 C CZ  B ARG B 421 ? 0.3835 0.6647 0.3302 0.0534  0.1142  0.0618  421 ARG B CZ  
13590 N NH1 A ARG B 421 ? 0.3965 0.6133 0.3264 -0.0920 0.0322  0.0305  421 ARG B NH1 
13591 N NH1 B ARG B 421 ? 0.4173 0.6639 0.3373 0.0288  0.1216  0.0576  421 ARG B NH1 
13592 N NH2 A ARG B 421 ? 0.4364 0.6661 0.3319 -0.0332 0.0754  0.0243  421 ARG B NH2 
13593 N NH2 B ARG B 421 ? 0.4261 0.6548 0.3286 0.0433  0.1029  0.0757  421 ARG B NH2 
13620 N N   . ALA B 422 ? 0.1768 0.2092 0.2609 -0.0370 -0.0159 0.0218  422 ALA B N   
13621 C CA  . ALA B 422 ? 0.1645 0.2270 0.2644 -0.0250 -0.0404 0.0347  422 ALA B CA  
13622 C C   . ALA B 422 ? 0.1933 0.2052 0.2567 -0.0715 -0.0268 0.0250  422 ALA B C   
13623 O O   . ALA B 422 ? 0.2367 0.2420 0.2602 -0.0733 -0.0311 0.0144  422 ALA B O   
13624 C CB  . ALA B 422 ? 0.2115 0.2413 0.2666 -0.0573 -0.0545 0.0573  422 ALA B CB  
13630 N N   A MET B 423 ? 0.1969 0.1885 0.2586 -0.0740 -0.0203 -0.0254 423 MET B N   
13631 N N   B MET B 423 ? 0.2117 0.2322 0.2609 -0.0725 -0.0250 0.0196  423 MET B N   
13632 C CA  A MET B 423 ? 0.1990 0.2288 0.2606 -0.0638 -0.0352 0.0006  423 MET B CA  
13633 C CA  B MET B 423 ? 0.2270 0.2576 0.2629 -0.0737 -0.0276 0.0227  423 MET B CA  
13634 C C   A MET B 423 ? 0.2035 0.2659 0.2752 -0.0730 -0.0577 0.0153  423 MET B C   
13635 C C   B MET B 423 ? 0.2269 0.2653 0.2740 -0.0699 -0.0511 0.0263  423 MET B C   
13636 O O   A MET B 423 ? 0.2426 0.2075 0.2992 -0.0559 -0.0491 -0.0050 423 MET B O   
13637 O O   B MET B 423 ? 0.2422 0.2625 0.2794 -0.0567 -0.0501 0.0238  423 MET B O   
13638 C CB  A MET B 423 ? 0.1983 0.2242 0.2541 -0.0606 0.0090  -0.0032 423 MET B CB  
13639 C CB  B MET B 423 ? 0.2430 0.2713 0.2529 -0.0833 -0.0031 0.0212  423 MET B CB  
13640 C CG  A MET B 423 ? 0.1987 0.2502 0.2672 -0.0192 -0.0126 0.0293  423 MET B CG  
13641 C CG  B MET B 423 ? 0.2548 0.2804 0.2438 -0.0861 0.0114  0.0243  423 MET B CG  
13642 S SD  A MET B 423 ? 0.2221 0.2356 0.2627 -0.0877 -0.0385 0.0203  423 MET B SD  
13643 S SD  B MET B 423 ? 0.2629 0.2803 0.2312 -0.0999 0.0255  0.0220  423 MET B SD  
13644 C CE  A MET B 423 ? 0.2241 0.2672 0.2865 -0.0927 -0.0194 0.0127  423 MET B CE  
13645 C CE  B MET B 423 ? 0.2667 0.2932 0.2377 -0.1022 0.0287  0.0179  423 MET B CE  
13664 N N   . PRO B 424 ? 0.2269 0.2549 0.2821 -0.0822 -0.0766 0.0310  424 PRO B N   
13665 C CA  . PRO B 424 ? 0.2365 0.3418 0.3120 -0.0786 -0.0721 0.0517  424 PRO B CA  
13666 C C   . PRO B 424 ? 0.2344 0.2749 0.3368 -0.0428 -0.0894 0.0465  424 PRO B C   
13667 O O   . PRO B 424 ? 0.2308 0.2387 0.3295 -0.0504 -0.0958 0.0142  424 PRO B O   
13668 C CB  . PRO B 424 ? 0.2065 0.3804 0.3163 -0.0759 -0.0615 0.0521  424 PRO B CB  
13669 C CG  . PRO B 424 ? 0.2099 0.3763 0.3093 -0.0553 -0.0376 0.0600  424 PRO B CG  
13670 C CD  . PRO B 424 ? 0.1872 0.3005 0.2884 -0.1180 -0.0678 0.0181  424 PRO B CD  
13678 N N   . GLN B 425 ? 0.2388 0.2990 0.3652 -0.0562 -0.0805 0.0500  425 GLN B N   
13679 C CA  . GLN B 425 ? 0.2346 0.2910 0.3792 -0.0470 -0.1160 0.0218  425 GLN B CA  
13680 C C   . GLN B 425 ? 0.2719 0.2577 0.3938 -0.0087 -0.1305 0.0100  425 GLN B C   
13681 O O   . GLN B 425 ? 0.2690 0.2705 0.4221 0.0088  -0.1334 -0.0347 425 GLN B O   
13682 C CB  . GLN B 425 ? 0.2282 0.3266 0.3640 -0.0457 -0.1026 0.0388  425 GLN B CB  
13683 C CG  . GLN B 425 ? 0.1635 0.3671 0.3193 -0.0787 -0.0097 0.0206  425 GLN B CG  
13684 C CD  . GLN B 425 ? 0.1071 0.3530 0.2909 -0.0599 0.0120  -0.0163 425 GLN B CD  
13685 O OE1 . GLN B 425 ? 0.1511 0.3111 0.2630 -0.0447 0.0409  0.0029  425 GLN B OE1 
13686 N NE2 . GLN B 425 ? 0.2013 0.4140 0.3034 -0.0211 0.0322  -0.0470 425 GLN B NE2 
13695 N N   . GLY B 426 ? 0.2997 0.2577 0.3931 -0.0213 -0.1050 0.0111  426 GLY B N   
13696 C CA  . GLY B 426 ? 0.3065 0.2961 0.3800 -0.0176 -0.0949 -0.0176 426 GLY B CA  
13697 C C   . GLY B 426 ? 0.2372 0.3036 0.3552 -0.0416 -0.1032 -0.0222 426 GLY B C   
13698 O O   . GLY B 426 ? 0.2221 0.3177 0.3485 -0.0521 -0.0779 -0.0229 426 GLY B O   
13702 N N   . ASP B 427 ? 0.2463 0.2785 0.3335 -0.0313 -0.0874 -0.0175 427 ASP B N   
13703 C CA  . ASP B 427 ? 0.2034 0.2808 0.3162 -0.0061 -0.0724 -0.0478 427 ASP B CA  
13704 C C   . ASP B 427 ? 0.2112 0.2535 0.2929 0.0116  -0.0398 -0.0429 427 ASP B C   
13705 O O   . ASP B 427 ? 0.2462 0.2425 0.2975 -0.0248 -0.0339 -0.0504 427 ASP B O   
13706 C CB  . ASP B 427 ? 0.2278 0.2953 0.3355 -0.0231 -0.0983 -0.0446 427 ASP B CB  
13707 C CG  . ASP B 427 ? 0.3130 0.2783 0.3732 -0.0037 -0.1114 -0.0409 427 ASP B CG  
13708 O OD1 . ASP B 427 ? 0.3135 0.2898 0.3615 0.0044  -0.1037 -0.0187 427 ASP B OD1 
13709 O OD2 . ASP B 427 ? 0.3868 0.3240 0.4105 0.0298  -0.1171 -0.0341 427 ASP B OD2 
13714 N N   . ILE B 428 ? 0.1938 0.2356 0.2630 0.0184  -0.0393 -0.0611 428 ILE B N   
13715 C CA  . ILE B 428 ? 0.2123 0.2166 0.2458 -0.0451 -0.0076 -0.0316 428 ILE B CA  
13716 C C   . ILE B 428 ? 0.2207 0.2210 0.2341 -0.0577 -0.0111 -0.0184 428 ILE B C   
13717 O O   . ILE B 428 ? 0.2138 0.2548 0.2328 -0.0321 -0.0313 -0.0148 428 ILE B O   
13718 C CB  . ILE B 428 ? 0.2147 0.1574 0.2441 -0.0429 -0.0163 -0.0409 428 ILE B CB  
13719 C CG1 . ILE B 428 ? 0.1820 0.1811 0.2477 -0.0741 -0.0071 -0.0292 428 ILE B CG1 
13720 C CG2 . ILE B 428 ? 0.2505 0.2093 0.2503 -0.0195 -0.0394 -0.0367 428 ILE B CG2 
13721 C CD1 . ILE B 428 ? 0.2174 0.2113 0.2454 -0.0666 0.0022  -0.0102 428 ILE B CD1 
13733 N N   . LEU B 429 ? 0.1949 0.2348 0.2224 -0.0582 -0.0290 -0.0125 429 LEU B N   
13734 C CA  . LEU B 429 ? 0.2012 0.2267 0.2261 -0.0961 -0.0161 -0.0223 429 LEU B CA  
13735 C C   . LEU B 429 ? 0.2109 0.2096 0.2094 -0.0209 -0.0023 -0.0326 429 LEU B C   
13736 O O   . LEU B 429 ? 0.1698 0.2585 0.1993 -0.0376 0.0158  -0.0301 429 LEU B O   
13737 C CB  . LEU B 429 ? 0.2233 0.2247 0.2308 -0.0991 -0.0125 -0.0269 429 LEU B CB  
13738 C CG  . LEU B 429 ? 0.2251 0.2156 0.2525 -0.0410 -0.0185 -0.0267 429 LEU B CG  
13739 C CD1 . LEU B 429 ? 0.2165 0.2290 0.2544 -0.0213 -0.0087 -0.0193 429 LEU B CD1 
13740 C CD2 . LEU B 429 ? 0.2210 0.2057 0.2648 0.0040  -0.0283 -0.0212 429 LEU B CD2 
13752 N N   . GLY B 430 ? 0.1975 0.2420 0.2100 -0.0584 -0.0063 -0.0184 430 GLY B N   
13753 C CA  . GLY B 430 ? 0.1567 0.2045 0.2103 -0.0399 0.0147  -0.0060 430 GLY B CA  
13754 C C   . GLY B 430 ? 0.1941 0.2064 0.1951 -0.0777 0.0028  -0.0467 430 GLY B C   
13755 O O   . GLY B 430 ? 0.2103 0.2337 0.1846 -0.0513 -0.0032 -0.0349 430 GLY B O   
13759 N N   . PHE B 431 ? 0.1878 0.2122 0.1999 -0.0624 0.0156  -0.0241 431 PHE B N   
13760 C CA  . PHE B 431 ? 0.1706 0.1917 0.2075 -0.0693 0.0177  -0.0154 431 PHE B CA  
13761 C C   . PHE B 431 ? 0.1937 0.1861 0.1943 -0.0593 0.0098  -0.0071 431 PHE B C   
13762 O O   . PHE B 431 ? 0.2003 0.1926 0.1817 -0.0455 0.0183  -0.0014 431 PHE B O   
13763 C CB  . PHE B 431 ? 0.1789 0.2410 0.2187 -0.0582 0.0058  0.0025  431 PHE B CB  
13764 C CG  . PHE B 431 ? 0.1785 0.2300 0.2316 -0.0449 0.0046  -0.0011 431 PHE B CG  
13765 C CD1 . PHE B 431 ? 0.1713 0.2660 0.2282 -0.0476 0.0230  -0.0065 431 PHE B CD1 
13766 C CD2 . PHE B 431 ? 0.1812 0.2305 0.2423 -0.0578 0.0073  -0.0105 431 PHE B CD2 
13767 C CE1 . PHE B 431 ? 0.1784 0.2604 0.2352 -0.0597 0.0241  -0.0017 431 PHE B CE1 
13768 C CE2 . PHE B 431 ? 0.1599 0.2925 0.2474 -0.0676 -0.0151 -0.0348 431 PHE B CE2 
13769 C CZ  . PHE B 431 ? 0.1573 0.2633 0.2455 -0.0672 0.0040  -0.0242 431 PHE B CZ  
13779 N N   . ALA B 432 ? 0.1986 0.1868 0.1982 -0.0647 0.0202  0.0104  432 ALA B N   
13780 C CA  . ALA B 432 ? 0.2112 0.1746 0.1946 -0.0946 0.0193  -0.0168 432 ALA B CA  
13781 C C   . ALA B 432 ? 0.1924 0.1735 0.1977 -0.0987 0.0158  -0.0203 432 ALA B C   
13782 O O   . ALA B 432 ? 0.1757 0.2258 0.2015 -0.0679 0.0172  0.0101  432 ALA B O   
13783 C CB  . ALA B 432 ? 0.2400 0.1971 0.1736 -0.0799 0.0175  -0.0166 432 ALA B CB  
13789 N N   . PRO B 433 ? 0.2181 0.2281 0.2030 -0.0683 0.0417  0.0026  433 PRO B N   
13790 C CA  . PRO B 433 ? 0.2380 0.2162 0.2058 -0.0657 0.0208  -0.0067 433 PRO B CA  
13791 C C   . PRO B 433 ? 0.2379 0.1890 0.2037 -0.0768 0.0198  -0.0114 433 PRO B C   
13792 O O   . PRO B 433 ? 0.2385 0.1943 0.2100 -0.0761 0.0342  -0.0127 433 PRO B O   
13793 C CB  . PRO B 433 ? 0.2629 0.2307 0.2162 -0.0436 0.0178  0.0180  433 PRO B CB  
13794 C CG  . PRO B 433 ? 0.2785 0.2704 0.2235 -0.0752 0.0308  0.0051  433 PRO B CG  
13795 C CD  . PRO B 433 ? 0.2193 0.2253 0.2143 -0.0763 0.0372  0.0044  433 PRO B CD  
13803 N N   . PRO B 434 ? 0.2265 0.1807 0.1912 -0.0684 0.0229  -0.0172 434 PRO B N   
13804 C CA  . PRO B 434 ? 0.2371 0.1628 0.1947 -0.0572 0.0131  -0.0161 434 PRO B CA  
13805 C C   . PRO B 434 ? 0.2249 0.1739 0.1928 -0.0839 0.0296  0.0035  434 PRO B C   
13806 O O   . PRO B 434 ? 0.2313 0.2299 0.1945 -0.0875 0.0172  0.0080  434 PRO B O   
13807 C CB  . PRO B 434 ? 0.2452 0.1958 0.2045 -0.0930 0.0091  0.0045  434 PRO B CB  
13808 C CG  . PRO B 434 ? 0.2713 0.2044 0.2059 -0.0722 0.0301  0.0025  434 PRO B CG  
13809 C CD  . PRO B 434 ? 0.2066 0.1775 0.2026 -0.0352 0.0049  -0.0199 434 PRO B CD  
13817 N N   . LEU B 435 ? 0.2197 0.1787 0.1862 -0.0844 0.0164  0.0026  435 LEU B N   
13818 C CA  . LEU B 435 ? 0.2391 0.1767 0.1930 -0.0499 0.0118  0.0181  435 LEU B CA  
13819 C C   . LEU B 435 ? 0.2588 0.1877 0.1990 -0.0605 0.0065  0.0338  435 LEU B C   
13820 O O   . LEU B 435 ? 0.2699 0.2511 0.2004 -0.0751 0.0041  0.0304  435 LEU B O   
13821 C CB  . LEU B 435 ? 0.2140 0.2062 0.1968 -0.0476 0.0174  0.0203  435 LEU B CB  
13822 C CG  . LEU B 435 ? 0.2158 0.2383 0.1939 -0.0886 0.0162  -0.0184 435 LEU B CG  
13823 C CD1 . LEU B 435 ? 0.2105 0.2443 0.1998 -0.0748 0.0192  -0.0550 435 LEU B CD1 
13824 C CD2 . LEU B 435 ? 0.2461 0.2378 0.1914 -0.0732 0.0349  -0.0249 435 LEU B CD2 
13836 N N   . VAL B 436 ? 0.2811 0.1765 0.2066 -0.0659 -0.0040 0.0248  436 VAL B N   
13837 C CA  . VAL B 436 ? 0.3061 0.1799 0.2117 -0.0764 0.0098  0.0258  436 VAL B CA  
13838 C C   . VAL B 436 ? 0.2632 0.1948 0.2243 -0.0814 0.0088  0.0286  436 VAL B C   
13839 O O   . VAL B 436 ? 0.2522 0.1858 0.2495 -0.0743 0.0368  0.0101  436 VAL B O   
13840 C CB  . VAL B 436 ? 0.3118 0.1818 0.2153 -0.0781 0.0083  0.0048  436 VAL B CB  
13841 C CG1 . VAL B 436 ? 0.3125 0.2342 0.2140 -0.0563 0.0429  -0.0356 436 VAL B CG1 
13842 C CG2 . VAL B 436 ? 0.3296 0.2206 0.2286 -0.1126 0.0197  0.0242  436 VAL B CG2 
13852 N N   . THR B 437 ? 0.1824 0.2079 0.2083 -0.0617 0.0156  0.0063  437 THR B N   
13853 C CA  . THR B 437 ? 0.1760 0.2321 0.2101 -0.0865 0.0376  -0.0058 437 THR B CA  
13854 C C   . THR B 437 ? 0.2112 0.2320 0.2049 -0.0943 0.0312  0.0197  437 THR B C   
13855 O O   . THR B 437 ? 0.2630 0.2184 0.2059 -0.0643 0.0202  0.0268  437 THR B O   
13856 C CB  . THR B 437 ? 0.1911 0.2648 0.2231 -0.0941 0.0311  -0.0030 437 THR B CB  
13857 O OG1 . THR B 437 ? 0.2291 0.2474 0.2168 -0.1064 0.0299  -0.0113 437 THR B OG1 
13858 C CG2 . THR B 437 ? 0.1759 0.2845 0.2400 -0.0670 0.0256  -0.0059 437 THR B CG2 
13866 N N   . THR B 438 ? 0.2382 0.2384 0.2073 -0.0928 0.0300  0.0281  438 THR B N   
13867 C CA  . THR B 438 ? 0.2273 0.2327 0.2175 -0.1126 0.0217  0.0085  438 THR B CA  
13868 C C   . THR B 438 ? 0.2646 0.2335 0.2243 -0.1263 0.0558  -0.0057 438 THR B C   
13869 O O   . THR B 438 ? 0.2658 0.2421 0.2388 -0.1178 0.0487  -0.0268 438 THR B O   
13870 C CB  . THR B 438 ? 0.2891 0.2134 0.2247 -0.0914 0.0271  0.0063  438 THR B CB  
13871 O OG1 . THR B 438 ? 0.3084 0.2087 0.2322 -0.0780 0.0369  -0.0059 438 THR B OG1 
13872 C CG2 . THR B 438 ? 0.2956 0.2224 0.2339 -0.0569 0.0043  -0.0122 438 THR B CG2 
13880 N N   . ARG B 439 ? 0.2787 0.2155 0.2267 -0.1135 0.0547  -0.0186 439 ARG B N   
13881 C CA  . ARG B 439 ? 0.3069 0.2180 0.2297 -0.1371 0.0571  -0.0131 439 ARG B CA  
13882 C C   . ARG B 439 ? 0.3160 0.2271 0.2388 -0.1312 0.0574  0.0096  439 ARG B C   
13883 O O   . ARG B 439 ? 0.3122 0.1892 0.2413 -0.1025 0.0724  -0.0138 439 ARG B O   
13884 C CB  . ARG B 439 ? 0.3293 0.2680 0.2341 -0.1544 0.0187  0.0020  439 ARG B CB  
13885 C CG  . ARG B 439 ? 0.3664 0.3746 0.2321 -0.1268 0.0090  -0.0057 439 ARG B CG  
13886 C CD  . ARG B 439 ? 0.4178 0.5007 0.2543 -0.1010 0.0151  -0.0287 439 ARG B CD  
13887 N NE  . ARG B 439 ? 0.5146 0.5914 0.2866 -0.1349 0.0237  -0.0583 439 ARG B NE  
13888 C CZ  . ARG B 439 ? 0.5896 0.6864 0.3256 -0.1208 0.0223  -0.0791 439 ARG B CZ  
13889 N NH1 . ARG B 439 ? 0.5976 0.7291 0.3420 -0.1111 0.0437  -0.0732 439 ARG B NH1 
13890 N NH2 . ARG B 439 ? 0.6329 0.7272 0.3404 -0.1150 -0.0049 -0.1011 439 ARG B NH2 
13904 N N   . ALA B 440 ? 0.2665 0.2321 0.2384 -0.1326 0.0261  -0.0012 440 ALA B N   
13905 C CA  . ALA B 440 ? 0.2917 0.2088 0.2419 -0.1405 0.0362  -0.0019 440 ALA B CA  
13906 C C   . ALA B 440 ? 0.2851 0.1916 0.2383 -0.1200 0.0446  0.0106  440 ALA B C   
13907 O O   . ALA B 440 ? 0.3110 0.2429 0.2443 -0.0729 0.0517  -0.0001 440 ALA B O   
13908 C CB  . ALA B 440 ? 0.3272 0.2104 0.2585 -0.1448 0.0113  -0.0219 440 ALA B CB  
13914 N N   . GLU B 441 ? 0.2651 0.1891 0.2308 -0.0939 0.0541  0.0246  441 GLU B N   
13915 C CA  . GLU B 441 ? 0.2678 0.1924 0.2258 -0.0494 0.0466  0.0115  441 GLU B CA  
13916 C C   . GLU B 441 ? 0.2533 0.2175 0.2224 -0.0549 0.0274  0.0064  441 GLU B C   
13917 O O   . GLU B 441 ? 0.2489 0.2342 0.2247 -0.0842 0.0239  -0.0075 441 GLU B O   
13918 C CB  . GLU B 441 ? 0.2597 0.1996 0.2294 -0.0341 0.0506  -0.0244 441 GLU B CB  
13919 C CG  . GLU B 441 ? 0.2965 0.2086 0.2358 -0.0766 0.0297  -0.0505 441 GLU B CG  
13920 C CD  . GLU B 441 ? 0.3204 0.2394 0.2485 -0.0778 0.0289  -0.0350 441 GLU B CD  
13921 O OE1 . GLU B 441 ? 0.2941 0.2251 0.2359 -0.0929 0.0059  0.0069  441 GLU B OE1 
13922 O OE2 . GLU B 441 ? 0.3121 0.2287 0.2785 -0.0573 0.0177  -0.0559 441 GLU B OE2 
13929 N N   . VAL B 442 ? 0.2377 0.2442 0.2276 -0.1084 0.0213  0.0264  442 VAL B N   
13930 C CA  . VAL B 442 ? 0.2314 0.2483 0.2409 -0.0618 0.0318  0.0265  442 VAL B CA  
13931 C C   . VAL B 442 ? 0.2151 0.2076 0.2363 -0.0876 0.0361  0.0113  442 VAL B C   
13932 O O   . VAL B 442 ? 0.2375 0.2334 0.2381 -0.0763 0.0335  -0.0354 442 VAL B O   
13933 C CB  . VAL B 442 ? 0.2025 0.2187 0.2617 -0.0696 0.0419  0.0070  442 VAL B CB  
13934 C CG1 . VAL B 442 ? 0.2613 0.2853 0.2712 -0.0746 0.0283  0.0161  442 VAL B CG1 
13935 C CG2 . VAL B 442 ? 0.2283 0.2405 0.2614 -0.0542 0.0269  0.0002  442 VAL B CG2 
13945 N N   . ASP B 443 ? 0.2541 0.2034 0.2424 -0.0679 0.0374  -0.0109 443 ASP B N   
13946 C CA  . ASP B 443 ? 0.2327 0.2133 0.2516 -0.0960 0.0339  -0.0309 443 ASP B CA  
13947 C C   . ASP B 443 ? 0.2247 0.2318 0.2638 -0.1025 0.0364  0.0000  443 ASP B C   
13948 O O   . ASP B 443 ? 0.2594 0.2351 0.2752 -0.0889 0.0295  -0.0308 443 ASP B O   
13949 C CB  . ASP B 443 ? 0.2673 0.2338 0.2514 -0.1121 0.0279  -0.0223 443 ASP B CB  
13950 C CG  . ASP B 443 ? 0.2890 0.2210 0.2532 -0.1283 0.0280  -0.0308 443 ASP B CG  
13951 O OD1 . ASP B 443 ? 0.2869 0.2381 0.2595 -0.1498 0.0310  -0.0506 443 ASP B OD1 
13952 O OD2 . ASP B 443 ? 0.3697 0.2546 0.2448 -0.1011 0.0472  -0.0124 443 ASP B OD2 
13957 N N   . GLU B 444 ? 0.2255 0.2366 0.2623 -0.0927 0.0139  0.0121  444 GLU B N   
13958 C CA  . GLU B 444 ? 0.2250 0.2919 0.2510 -0.0932 0.0339  -0.0068 444 GLU B CA  
13959 C C   . GLU B 444 ? 0.1883 0.2862 0.2443 -0.1098 0.0271  -0.0165 444 GLU B C   
13960 O O   . GLU B 444 ? 0.2470 0.3328 0.2556 -0.1182 0.0316  -0.0326 444 GLU B O   
13961 C CB  . GLU B 444 ? 0.2706 0.3196 0.2709 -0.1108 0.0334  -0.0056 444 GLU B CB  
13962 C CG  . GLU B 444 ? 0.3389 0.3177 0.2784 -0.1371 0.0197  0.0165  444 GLU B CG  
13963 C CD  . GLU B 444 ? 0.4057 0.3134 0.2879 -0.1842 0.0168  0.0298  444 GLU B CD  
13964 O OE1 . GLU B 444 ? 0.4014 0.3513 0.2986 -0.2100 0.0143  0.0409  444 GLU B OE1 
13965 O OE2 . GLU B 444 ? 0.4244 0.3182 0.3026 -0.2032 0.0054  0.0128  444 GLU B OE2 
13972 N N   . ILE B 445 ? 0.2083 0.2642 0.2493 -0.0747 0.0292  0.0128  445 ILE B N   
13973 C CA  . ILE B 445 ? 0.2191 0.2646 0.2520 -0.0650 0.0529  0.0124  445 ILE B CA  
13974 C C   . ILE B 445 ? 0.2354 0.2749 0.2501 -0.0556 0.0536  -0.0196 445 ILE B C   
13975 O O   . ILE B 445 ? 0.2340 0.2617 0.2417 -0.0813 0.0514  -0.0221 445 ILE B O   
13976 C CB  . ILE B 445 ? 0.2039 0.2529 0.2450 -0.0774 0.0578  0.0109  445 ILE B CB  
13977 C CG1 . ILE B 445 ? 0.2100 0.2841 0.2486 -0.0748 0.0659  -0.0093 445 ILE B CG1 
13978 C CG2 . ILE B 445 ? 0.2127 0.2326 0.2414 -0.0655 0.0855  0.0173  445 ILE B CG2 
13979 C CD1 . ILE B 445 ? 0.2172 0.3329 0.2416 -0.0757 0.0914  -0.0345 445 ILE B CD1 
13991 N N   . VAL B 446 ? 0.2204 0.2543 0.2575 -0.0392 0.0589  -0.0379 446 VAL B N   
13992 C CA  . VAL B 446 ? 0.1780 0.2253 0.2674 -0.0513 0.0536  -0.0591 446 VAL B CA  
13993 C C   . VAL B 446 ? 0.2307 0.2509 0.2701 -0.0490 0.0388  -0.0505 446 VAL B C   
13994 O O   . VAL B 446 ? 0.2249 0.2941 0.2719 -0.0143 0.0618  -0.0348 446 VAL B O   
13995 C CB  . VAL B 446 ? 0.1979 0.2834 0.2705 -0.0581 0.0509  -0.0655 446 VAL B CB  
13996 C CG1 . VAL B 446 ? 0.2768 0.3300 0.2632 -0.0044 0.0762  -0.0367 446 VAL B CG1 
13997 C CG2 . VAL B 446 ? 0.2259 0.2986 0.2697 -0.0416 0.0334  -0.0878 446 VAL B CG2 
14007 N N   . ALA B 447 ? 0.2647 0.2736 0.2765 -0.0821 0.0539  -0.0393 447 ALA B N   
14008 C CA  . ALA B 447 ? 0.2514 0.2800 0.2854 -0.0834 0.0386  -0.0495 447 ALA B CA  
14009 C C   . ALA B 447 ? 0.2461 0.3019 0.2909 -0.0759 0.0460  -0.0511 447 ALA B C   
14010 O O   . ALA B 447 ? 0.2374 0.3362 0.2939 -0.0365 0.0507  -0.0649 447 ALA B O   
14011 C CB  . ALA B 447 ? 0.2447 0.2748 0.2849 -0.0783 0.0289  -0.0453 447 ALA B CB  
14017 N N   . ARG B 448 ? 0.2326 0.2805 0.2922 -0.0668 0.0290  -0.0609 448 ARG B N   
14018 C CA  . ARG B 448 ? 0.1979 0.2680 0.2893 -0.0850 0.0463  -0.0235 448 ARG B CA  
14019 C C   . ARG B 448 ? 0.2427 0.2803 0.2920 -0.0635 0.0434  -0.0377 448 ARG B C   
14020 O O   . ARG B 448 ? 0.2283 0.2234 0.2938 -0.0382 0.0388  -0.0397 448 ARG B O   
14021 C CB  . ARG B 448 ? 0.2201 0.2574 0.2792 -0.0340 0.0285  -0.0051 448 ARG B CB  
14022 C CG  . ARG B 448 ? 0.2186 0.2727 0.2740 -0.0651 0.0352  -0.0229 448 ARG B CG  
14023 C CD  . ARG B 448 ? 0.2744 0.2671 0.2748 -0.1077 0.0242  -0.0146 448 ARG B CD  
14024 N NE  . ARG B 448 ? 0.3024 0.2459 0.2625 -0.1185 0.0296  -0.0163 448 ARG B NE  
14025 C CZ  . ARG B 448 ? 0.3025 0.2602 0.2661 -0.1434 0.0474  -0.0146 448 ARG B CZ  
14026 N NH1 . ARG B 448 ? 0.3193 0.2944 0.2628 -0.1240 0.0893  -0.0162 448 ARG B NH1 
14027 N NH2 . ARG B 448 ? 0.3026 0.2917 0.2727 -0.1266 0.0469  -0.0234 448 ARG B NH2 
14041 N N   . ALA B 449 ? 0.2380 0.3034 0.2943 -0.0952 0.0247  -0.0493 449 ALA B N   
14042 C CA  . ALA B 449 ? 0.2113 0.2922 0.2928 -0.0586 0.0322  -0.0662 449 ALA B CA  
14043 C C   . ALA B 449 ? 0.2104 0.2954 0.2945 -0.0665 0.0463  -0.0735 449 ALA B C   
14044 O O   . ALA B 449 ? 0.2173 0.3356 0.3049 -0.0966 0.0586  -0.0532 449 ALA B O   
14045 C CB  . ALA B 449 ? 0.1964 0.2908 0.2841 -0.0222 0.0235  -0.0476 449 ALA B CB  
14051 N N   . LYS B 450 ? 0.2143 0.3214 0.2987 -0.0776 0.0489  -0.0708 450 LYS B N   
14052 C CA  . LYS B 450 ? 0.2344 0.3394 0.3073 -0.0859 0.0486  -0.0409 450 LYS B CA  
14053 C C   . LYS B 450 ? 0.2009 0.3246 0.3100 -0.0746 0.0413  -0.0563 450 LYS B C   
14054 O O   . LYS B 450 ? 0.2046 0.3385 0.3072 -0.0352 0.0311  -0.0608 450 LYS B O   
14055 C CB  . LYS B 450 ? 0.2833 0.3680 0.3207 -0.0866 0.0589  -0.0340 450 LYS B CB  
14056 C CG  . LYS B 450 ? 0.2699 0.4086 0.3319 -0.0351 0.0699  -0.0071 450 LYS B CG  
14057 C CD  . LYS B 450 ? 0.3288 0.4573 0.3535 -0.0030 0.0895  0.0018  450 LYS B CD  
14058 C CE  . LYS B 450 ? 0.3941 0.5146 0.3697 0.0395  0.1260  0.0169  450 LYS B CE  
14059 N NZ  . LYS B 450 ? 0.4254 0.5461 0.3799 0.0645  0.1248  0.0299  450 LYS B NZ  
14073 N N   . ARG B 451 ? 0.2097 0.3159 0.3129 -0.1166 0.0370  -0.0560 451 ARG B N   
14074 C CA  . ARG B 451 ? 0.2474 0.3470 0.3262 -0.1206 0.0237  -0.0564 451 ARG B CA  
14075 C C   . ARG B 451 ? 0.2360 0.3495 0.3046 -0.1090 0.0319  -0.0444 451 ARG B C   
14076 O O   . ARG B 451 ? 0.2637 0.3671 0.3045 -0.0982 0.0458  -0.0511 451 ARG B O   
14077 C CB  . ARG B 451 ? 0.2858 0.3540 0.3579 -0.1374 0.0237  -0.0622 451 ARG B CB  
14078 C CG  . ARG B 451 ? 0.3398 0.3935 0.3892 -0.1643 0.0248  -0.0720 451 ARG B CG  
14079 C CD  . ARG B 451 ? 0.4007 0.4468 0.4124 -0.1402 0.0394  -0.0690 451 ARG B CD  
14080 N NE  . ARG B 451 ? 0.4319 0.4860 0.4437 -0.1636 0.0556  -0.0534 451 ARG B NE  
14081 C CZ  . ARG B 451 ? 0.4666 0.5323 0.4703 -0.1372 0.0694  -0.0609 451 ARG B CZ  
14082 N NH1 . ARG B 451 ? 0.5095 0.5141 0.4669 -0.1560 0.0591  -0.0527 451 ARG B NH1 
14083 N NH2 . ARG B 451 ? 0.4308 0.5502 0.4986 -0.1181 0.0688  -0.0693 451 ARG B NH2 
14097 N N   . ALA B 452 ? 0.1893 0.3512 0.2916 -0.0923 0.0394  -0.0405 452 ALA B N   
14098 C CA  . ALA B 452 ? 0.1742 0.3291 0.2897 -0.1154 0.0300  -0.0416 452 ALA B CA  
14099 C C   . ALA B 452 ? 0.1849 0.3347 0.2927 -0.0549 -0.0127 -0.0556 452 ALA B C   
14100 O O   . ALA B 452 ? 0.2370 0.3532 0.3017 -0.0563 -0.0072 -0.0560 452 ALA B O   
14101 C CB  . ALA B 452 ? 0.1609 0.3480 0.2831 -0.0855 0.0533  -0.0334 452 ALA B CB  
14107 N N   . VAL B 453 ? 0.2020 0.3452 0.2924 -0.0803 -0.0379 -0.0474 453 VAL B N   
14108 C CA  . VAL B 453 ? 0.1883 0.3617 0.2893 -0.0776 -0.0285 -0.0294 453 VAL B CA  
14109 C C   . VAL B 453 ? 0.1992 0.3769 0.3051 -0.0434 -0.0388 -0.0219 453 VAL B C   
14110 O O   . VAL B 453 ? 0.2351 0.3571 0.3110 -0.0316 -0.0379 0.0034  453 VAL B O   
14111 C CB  . VAL B 453 ? 0.1523 0.3209 0.2738 -0.0485 -0.0359 -0.0392 453 VAL B CB  
14112 C CG1 . VAL B 453 ? 0.2211 0.3437 0.2678 0.0073  -0.0142 -0.0589 453 VAL B CG1 
14113 C CG2 . VAL B 453 ? 0.1681 0.3124 0.2725 -0.0260 -0.0090 -0.0200 453 VAL B CG2 
14123 N N   . ASP B 454 ? 0.1793 0.4078 0.3142 0.0011  0.0086  -0.0266 454 ASP B N   
14124 C CA  . ASP B 454 ? 0.1565 0.4268 0.3193 -0.0296 -0.0180 -0.0547 454 ASP B CA  
14125 C C   . ASP B 454 ? 0.1884 0.4164 0.3168 -0.0047 0.0054  -0.0644 454 ASP B C   
14126 O O   . ASP B 454 ? 0.1947 0.4274 0.3233 -0.0211 -0.0068 -0.0820 454 ASP B O   
14127 C CB  . ASP B 454 ? 0.2023 0.4804 0.3374 -0.0560 -0.0170 -0.0343 454 ASP B CB  
14128 C CG  . ASP B 454 ? 0.2457 0.5345 0.3506 -0.0527 0.0037  -0.0414 454 ASP B CG  
14129 O OD1 . ASP B 454 ? 0.2247 0.5639 0.3460 -0.0509 -0.0126 -0.0591 454 ASP B OD1 
14130 O OD2 . ASP B 454 ? 0.2671 0.5553 0.3646 -0.0902 0.0340  -0.0314 454 ASP B OD2 
14135 N N   . LYS B 455 ? 0.1975 0.3804 0.2958 -0.0417 0.0000  -0.0799 455 LYS B N   
14136 C CA  . LYS B 455 ? 0.2203 0.4262 0.3099 -0.0642 -0.0063 -0.0788 455 LYS B CA  
14137 C C   . LYS B 455 ? 0.1941 0.4159 0.3065 -0.0310 -0.0069 -0.0594 455 LYS B C   
14138 O O   . LYS B 455 ? 0.2152 0.4254 0.3224 -0.0431 0.0013  -0.0482 455 LYS B O   
14139 C CB  . LYS B 455 ? 0.3298 0.4900 0.3336 -0.0459 0.0037  -0.0909 455 LYS B CB  
14140 C CG  . LYS B 455 ? 0.4060 0.5907 0.3485 -0.0330 -0.0066 -0.1035 455 LYS B CG  
14141 C CD  . LYS B 455 ? 0.5233 0.6645 0.3562 -0.0296 0.0112  -0.1049 455 LYS B CD  
14142 C CE  . LYS B 455 ? 0.6352 0.7061 0.3754 -0.0541 0.0041  -0.1006 455 LYS B CE  
14143 N NZ  . LYS B 455 ? 0.6950 0.7365 0.3813 -0.0593 0.0056  -0.1023 455 LYS B NZ  
14157 N N   . VAL B 456 ? 0.1682 0.3968 0.3019 -0.0329 0.0122  -0.0644 456 VAL B N   
14158 C CA  . VAL B 456 ? 0.1965 0.3945 0.3143 -0.0019 -0.0065 -0.0631 456 VAL B CA  
14159 C C   . VAL B 456 ? 0.2080 0.3997 0.3290 0.0233  -0.0034 -0.0483 456 VAL B C   
14160 O O   . VAL B 456 ? 0.2131 0.3918 0.3350 0.0239  -0.0228 -0.0702 456 VAL B O   
14161 C CB  . VAL B 456 ? 0.1614 0.3529 0.3163 -0.0245 -0.0252 -0.0635 456 VAL B CB  
14162 C CG1 . VAL B 456 ? 0.2303 0.4060 0.3233 -0.0172 -0.0222 -0.0665 456 VAL B CG1 
14163 C CG2 . VAL B 456 ? 0.1594 0.3333 0.3226 -0.0680 -0.0197 -0.0260 456 VAL B CG2 
14173 N N   . THR B 457 ? 0.2095 0.3957 0.3323 -0.0133 -0.0034 -0.0405 457 THR B N   
14174 C CA  . THR B 457 ? 0.2028 0.3966 0.3391 0.0149  -0.0118 -0.0578 457 THR B CA  
14175 C C   . THR B 457 ? 0.2240 0.4338 0.3432 0.0142  -0.0287 -0.0772 457 THR B C   
14176 O O   . THR B 457 ? 0.2475 0.4109 0.3320 0.0339  -0.0274 -0.1002 457 THR B O   
14177 C CB  . THR B 457 ? 0.1787 0.3840 0.3417 0.0729  -0.0032 -0.0612 457 THR B CB  
14178 O OG1 . THR B 457 ? 0.1625 0.4591 0.3399 0.0580  -0.0223 -0.0719 457 THR B OG1 
14179 C CG2 . THR B 457 ? 0.2866 0.3761 0.3362 0.0587  -0.0298 -0.0488 457 THR B CG2 
14187 N N   . ASP B 458 ? 0.2036 0.4625 0.3574 -0.0006 -0.0312 -0.0795 458 ASP B N   
14188 C CA  . ASP B 458 ? 0.2096 0.4849 0.3674 0.0105  -0.0376 -0.0928 458 ASP B CA  
14189 C C   . ASP B 458 ? 0.2243 0.4855 0.3446 0.0447  -0.0419 -0.1078 458 ASP B C   
14190 O O   . ASP B 458 ? 0.2293 0.5412 0.3411 0.0516  -0.0637 -0.1108 458 ASP B O   
14191 C CB  . ASP B 458 ? 0.2746 0.5007 0.3971 -0.0027 -0.0384 -0.0995 458 ASP B CB  
14192 C CG  . ASP B 458 ? 0.3417 0.5440 0.4251 0.0249  -0.0222 -0.0957 458 ASP B CG  
14193 O OD1 . ASP B 458 ? 0.3381 0.5472 0.4269 0.0590  0.0296  -0.0852 458 ASP B OD1 
14194 O OD2 . ASP B 458 ? 0.3960 0.5904 0.4481 0.0085  -0.0304 -0.0792 458 ASP B OD2 
14199 N N   . GLU B 459 ? 0.2519 0.4275 0.3291 -0.0078 -0.0366 -0.1298 459 GLU B N   
14200 C CA  . GLU B 459 ? 0.2744 0.4126 0.3244 -0.0057 -0.0533 -0.1260 459 GLU B CA  
14201 C C   . GLU B 459 ? 0.2861 0.4799 0.3261 0.0373  -0.0570 -0.1042 459 GLU B C   
14202 O O   . GLU B 459 ? 0.2858 0.5176 0.3296 0.1033  -0.0716 -0.1138 459 GLU B O   
14203 C CB  . GLU B 459 ? 0.2808 0.3592 0.3261 -0.0018 -0.0308 -0.1217 459 GLU B CB  
14204 C CG  . GLU B 459 ? 0.2990 0.3379 0.3394 0.0005  -0.0066 -0.1165 459 GLU B CG  
14205 C CD  . GLU B 459 ? 0.3729 0.3754 0.3631 -0.0310 0.0495  -0.1136 459 GLU B CD  
14206 O OE1 . GLU B 459 ? 0.2807 0.3531 0.3821 0.0151  0.0481  -0.0631 459 GLU B OE1 
14207 O OE2 . GLU B 459 ? 0.4679 0.4326 0.3804 -0.1107 0.1005  -0.1389 459 GLU B OE2 
14214 N N   . LEU B 460 ? 0.2538 0.4692 0.3238 0.0091  -0.0739 -0.0870 460 LEU B N   
14215 C CA  . LEU B 460 ? 0.2493 0.4772 0.3411 0.0274  -0.0568 -0.0909 460 LEU B CA  
14216 C C   . LEU B 460 ? 0.2667 0.5197 0.3642 0.0567  -0.0421 -0.1037 460 LEU B C   
14217 O O   . LEU B 460 ? 0.2655 0.5139 0.3695 0.0372  -0.0481 -0.1117 460 LEU B O   
14218 C CB  . LEU B 460 ? 0.2519 0.4473 0.3365 0.0198  -0.0704 -0.1058 460 LEU B CB  
14219 C CG  . LEU B 460 ? 0.2525 0.4301 0.3366 0.0122  -0.0840 -0.0841 460 LEU B CG  
14220 C CD1 . LEU B 460 ? 0.2699 0.4020 0.3439 -0.0191 -0.0898 -0.0650 460 LEU B CD1 
14221 C CD2 . LEU B 460 ? 0.3275 0.4827 0.3352 0.0108  -0.0876 -0.0811 460 LEU B CD2 
14233 N N   . THR B 461 ? 0.2642 0.5594 0.3802 0.0559  -0.0320 -0.1237 461 THR B N   
14234 C CA  . THR B 461 ? 0.2567 0.5812 0.3896 0.1012  -0.0270 -0.1342 461 THR B CA  
14235 C C   . THR B 461 ? 0.2835 0.6147 0.3876 0.0947  -0.0523 -0.1352 461 THR B C   
14236 O O   . THR B 461 ? 0.3153 0.6175 0.3855 0.1276  -0.0582 -0.1228 461 THR B O   
14237 C CB  . THR B 461 ? 0.2605 0.5866 0.4001 0.1132  -0.0184 -0.1312 461 THR B CB  
14238 O OG1 . THR B 461 ? 0.2917 0.5927 0.4069 0.1026  -0.0296 -0.1499 461 THR B OG1 
14239 C CG2 . THR B 461 ? 0.3055 0.5820 0.4060 0.0568  -0.0187 -0.1182 461 THR B CG2 
14247 N N   . ARG B 462 ? 0.2471 0.6236 0.3781 0.1023  -0.0736 -0.1528 462 ARG B N   
14248 C CA  . ARG B 462 ? 0.3078 0.6055 0.3832 0.1205  -0.0882 -0.1645 462 ARG B CA  
14249 C C   . ARG B 462 ? 0.3770 0.6036 0.4033 0.1558  -0.0995 -0.1740 462 ARG B C   
14250 O O   . ARG B 462 ? 0.4451 0.6135 0.4120 0.1622  -0.1036 -0.1658 462 ARG B O   
14251 C CB  . ARG B 462 ? 0.3119 0.6118 0.3704 0.0643  -0.0947 -0.1646 462 ARG B CB  
14252 C CG  . ARG B 462 ? 0.3215 0.6070 0.3640 0.0549  -0.1071 -0.1386 462 ARG B CG  
14253 C CD  . ARG B 462 ? 0.3497 0.6263 0.3587 0.0655  -0.1080 -0.1274 462 ARG B CD  
14254 N NE  . ARG B 462 ? 0.4556 0.6425 0.3588 0.0482  -0.0985 -0.1012 462 ARG B NE  
14255 C CZ  . ARG B 462 ? 0.4747 0.6159 0.3635 0.0674  -0.1115 -0.0442 462 ARG B CZ  
14256 N NH1 . ARG B 462 ? 0.4499 0.6317 0.3609 0.0510  -0.1383 -0.0219 462 ARG B NH1 
14257 N NH2 . ARG B 462 ? 0.4894 0.6085 0.3705 0.0785  -0.1092 -0.0209 462 ARG B NH2 
14271 N N   . SER B 463 ? 0.3840 0.6055 0.4189 0.1504  -0.1099 -0.1659 463 SER B N   
14272 C CA  . SER B 463 ? 0.4178 0.5969 0.4350 0.1642  -0.1138 -0.1482 463 SER B CA  
14273 C C   . SER B 463 ? 0.4511 0.5985 0.4649 0.1641  -0.0923 -0.1451 463 SER B C   
14274 O O   . SER B 463 ? 0.4805 0.5903 0.4824 0.1788  -0.0747 -0.1272 463 SER B O   
14275 C CB  . SER B 463 ? 0.3919 0.6104 0.4226 0.1627  -0.1519 -0.1128 463 SER B CB  
14276 O OG  . SER B 463 ? 0.4337 0.6242 0.4176 0.1510  -0.1450 -0.1021 463 SER B OG  
14282 N N   . GLY B 464 ? 0.4360 0.5948 0.4643 0.1888  -0.0915 -0.1610 464 GLY B N   
14283 C CA  . GLY B 464 ? 0.4294 0.5989 0.4700 0.1595  -0.0870 -0.1778 464 GLY B CA  
14284 C C   . GLY B 464 ? 0.5188 0.6250 0.4799 0.1430  -0.0788 -0.1685 464 GLY B C   
14285 O O   . GLY B 464 ? 0.5383 0.6282 0.4840 0.1138  -0.0764 -0.1817 464 GLY B O   
14289 N N   . ASP B 465 ? 0.4863 0.6288 0.4850 0.1496  -0.0835 -0.1416 465 ASP B N   
14290 C CA  . ASP B 465 ? 0.4981 0.6358 0.4961 0.1563  -0.0864 -0.1279 465 ASP B CA  
14291 C C   . ASP B 465 ? 0.5254 0.6648 0.5000 0.1816  -0.1038 -0.0979 465 ASP B C   
14292 O O   . ASP B 465 ? 0.5201 0.6626 0.5065 0.2038  -0.0957 -0.0829 465 ASP B O   
14293 C CB  . ASP B 465 ? 0.4665 0.6354 0.5050 0.1305  -0.0699 -0.1424 465 ASP B CB  
14294 C CG  . ASP B 465 ? 0.4785 0.6295 0.5135 0.1030  -0.0543 -0.1632 465 ASP B CG  
14295 O OD1 . ASP B 465 ? 0.5080 0.6327 0.5163 0.1126  -0.0501 -0.1836 465 ASP B OD1 
14296 O OD2 . ASP B 465 ? 0.4893 0.6243 0.5150 0.0422  -0.0494 -0.1595 465 ASP B OD2 
14301 N N   . LEU B 466 ? 0.5793 0.7050 0.4995 0.1604  -0.1224 -0.0798 466 LEU B N   
14302 C CA  . LEU B 466 ? 0.6329 0.7422 0.4985 0.1298  -0.1167 -0.0498 466 LEU B CA  
14303 C C   . LEU B 466 ? 0.7037 0.7718 0.5038 0.1238  -0.1231 -0.0276 466 LEU B C   
14304 O O   . LEU B 466 ? 0.7319 0.7793 0.5084 0.1305  -0.1479 -0.0023 466 LEU B O   
14305 C CB  . LEU B 466 ? 0.6243 0.7684 0.4927 0.0738  -0.1032 -0.0522 466 LEU B CB  
14306 C CG  . LEU B 466 ? 0.5924 0.7853 0.4847 0.0468  -0.0852 -0.0636 466 LEU B CG  
14307 C CD1 . LEU B 466 ? 0.5882 0.8033 0.4851 0.0343  -0.0724 -0.0636 466 LEU B CD1 
14308 C CD2 . LEU B 466 ? 0.6218 0.7887 0.4830 0.0458  -0.0848 -0.0686 466 LEU B CD2 
14320 C C1  . GOL C .   ? 0.3504 0.5067 0.6471 -0.0073 -0.0737 -0.0376 501 GOL A C1  
14321 O O1  . GOL C .   ? 0.3883 0.5098 0.6435 -0.0044 -0.0690 -0.0319 501 GOL A O1  
14322 C C2  . GOL C .   ? 0.3740 0.5522 0.6424 0.0627  -0.0349 -0.0123 501 GOL A C2  
14323 O O2  . GOL C .   ? 0.3711 0.5535 0.6222 0.1590  0.0199  -0.0212 501 GOL A O2  
14324 C C3  . GOL C .   ? 0.4126 0.5595 0.6411 0.0381  -0.0311 0.0087  501 GOL A C3  
14325 O O3  . GOL C .   ? 0.4239 0.5339 0.6351 0.0167  -0.0412 0.0212  501 GOL A O3  
14334 C C1  . GOL D .   ? 0.6345 0.6883 0.8097 -0.2041 -0.0313 -0.0984 502 GOL A C1  
14335 O O1  . GOL D .   ? 0.7113 0.7180 0.8184 -0.2171 -0.0482 -0.1071 502 GOL A O1  
14336 C C2  . GOL D .   ? 0.5526 0.6439 0.7995 -0.1848 -0.0286 -0.1032 502 GOL A C2  
14337 O O2  . GOL D .   ? 0.5430 0.6100 0.7920 -0.1785 -0.0094 -0.0991 502 GOL A O2  
14338 C C3  . GOL D .   ? 0.4832 0.6319 0.7977 -0.1279 -0.0426 -0.1189 502 GOL A C3  
14339 O O3  . GOL D .   ? 0.4627 0.6574 0.8025 -0.0781 -0.0649 -0.1366 502 GOL A O3  
14347 C C1  . GOL E .   ? 0.3233 0.5470 0.7480 -0.1329 -0.0130 -0.0437 503 GOL A C1  
14348 O O1  . GOL E .   ? 0.2581 0.4674 0.7515 -0.1392 -0.0157 -0.0024 503 GOL A O1  
14349 C C2  . GOL E .   ? 0.3257 0.6124 0.7430 -0.1502 0.0024  -0.0789 503 GOL A C2  
14350 O O2  . GOL E .   ? 0.2897 0.5552 0.7257 -0.1630 -0.0055 -0.1255 503 GOL A O2  
14351 C C3  . GOL E .   ? 0.3548 0.6876 0.7509 -0.1149 0.0187  -0.0618 503 GOL A C3  
14352 O O3  . GOL E .   ? 0.3543 0.7192 0.7539 -0.0984 0.0658  -0.0581 503 GOL A O3  
# 
