data_8T1V
# 
_entry.id   8T1V 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8T1V         pdb_00008t1v 10.2210/pdb8t1v/pdb 
WWPDB D_1000275051 ?            ?                   
# 
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 
1 'Structure model' 1 0 2024-12-04 
2 'Structure model' 1 1 2024-12-18 
# 
_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' 'Data collection'      
2 2 'Structure model' 'Database references'  
3 2 'Structure model' 'Derived calculations' 
# 
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 2 'Structure model' pdbx_struct_assembly      
4 2 'Structure model' pdbx_struct_assembly_gen  
5 2 'Structure model' pdbx_struct_assembly_prop 
6 2 'Structure model' pdbx_struct_oper_list     
7 2 'Structure model' struct_biol               
# 
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.journal_volume'                  
2  2 'Structure model' '_citation.page_first'                      
3  2 'Structure model' '_citation.page_last'                       
4  2 'Structure model' '_citation.pdbx_database_id_PubMed'         
5  2 'Structure model' '_citation.title'                           
6  2 'Structure model' '_citation_author.identifier_ORCID'         
7  2 'Structure model' '_citation_author.name'                     
8  2 'Structure model' '_pdbx_struct_assembly.details'             
9  2 'Structure model' '_pdbx_struct_assembly.method_details'      
10 2 'Structure model' '_pdbx_struct_assembly.oligomeric_count'    
11 2 'Structure model' '_pdbx_struct_assembly.oligomeric_details'  
12 2 'Structure model' '_pdbx_struct_assembly_gen.oper_expression' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8T1V 
_pdbx_database_status.recvd_initial_deposition_date   2023-06-04 
_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              cherezov@usc.edu 
_pdbx_contact_author.name_first         Vadim 
_pdbx_contact_author.name_last          Cherezov 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5265-3914 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Barekatain, M.'   1  ? 
'Johansson, L.'    2  ? 
'Lam, J.H.'        3  ? 
'Sadybekov, A.V.'  4  ? 
'Han, G.W.'        5  ? 
'Popov, P.'        6  ? 
'Russo, J.'        7  ? 
'Bliesath, J.'     8  ? 
'Brice, N.'        9  ? 
'Beresford, M.'    10 ? 
'Carlson, L.'      11 ? 
'Saikatendu, K.S.' 12 ? 
'Sun, H.'          13 ? 
'Murphy, S.'       14 ? 
'Monenschein, H.'  15 ? 
'Schiffer, H.H.'   16 ? 
'Lutomski, C.'     17 ? 
'Robinson, C.V.'   18 ? 
'Liu, Z.'          19 ? 
'Hua, T.'          20 ? 
'Katritch, V.'     21 ? 
'Cherezov, V.'     22 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Sci.Signal. 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1937-9145 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            17 
_citation.language                  ? 
_citation.page_first                eado8741 
_citation.page_last                 eado8741 
_citation.title                     
;Structural insights into the high basal activity and inverse agonism of the orphan receptor GPR6 implicated in Parkinson's disease.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1126/scisignal.ado8741 
_citation.pdbx_database_id_PubMed   39626010 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Barekatain, M.'   1  0000-0003-4178-684X 
primary 'Johansson, L.C.'  2  ?                   
primary 'Lam, J.H.'        3  0000-0002-5496-6228 
primary 'Chang, H.'        4  0000-0003-1684-8201 
primary 'Sadybekov, A.V.'  5  0000-0003-3925-983X 
primary 'Han, G.W.'        6  0000-0003-4107-835X 
primary 'Russo, J.'        7  ?                   
primary 'Bliesath, J.'     8  ?                   
primary 'Brice, N.L.'      9  ?                   
primary 'Carlton, M.B.L.'  10 ?                   
primary 'Saikatendu, K.S.' 11 0000-0001-6734-237X 
primary 'Sun, H.'          12 ?                   
primary 'Murphy, S.T.'     13 0009-0000-5404-6512 
primary 'Monenschein, H.'  14 ?                   
primary 'Schiffer, H.H.'   15 ?                   
primary 'Popov, P.'        16 ?                   
primary 'Lutomski, C.A.'   17 0000-0001-7509-103X 
primary 'Robinson, C.V.'   18 0000-0001-7829-5505 
primary 'Liu, Z.J.'        19 0000-0001-7279-2893 
primary 'Hua, T.'          20 0000-0002-6132-2068 
primary 'Katritch, V.'     21 0000-0003-3883-4505 
primary 'Cherezov, V.'     22 0000-0002-5265-3914 
# 
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 'G-protein coupled receptor 6, Soluble cytochrome b562 chimera'                                         
49715.480 1 ? ? ? ? 
2 non-polymer syn '3-{4-[(2,4-difluorophenyl)methyl]piperazin-1-yl}-7-methyl-N-(propan-2-yl)pyrido[3,4-b]pyrazin-2-amine' 412.479 
1 ? ? ? ? 
3 non-polymer nat 'SODIUM ION'                                                                                            22.990 1 
? ? ? ? 
4 water       nat water                                                                                                   18.015 5 
? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Sphingosine 1-phosphate receptor GPR6,Cytochrome b-562' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MKTIIALSYIFCLVFADYKDDDDAGRAGGANGSLELSSQLSAGPPGLLLPAVNPWDVLLCVSGTVIAGENALVVALIAST
PALRTPMFVLVGSLATADLLAGLGLILHFVFQYLVPSETVSLLTVGFLVASFAASVSSLLAITVDRYLSLYNPLTYYSRR
TLLGVHLLLAATWTVSLGLGLLPVLGWNCLAERAACSVVRPLARSHVALLSAAFFMVFGIMLHLYVRICQVVWRHAADLE
DNWETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLANEGKV
KEAQAAAEQLKTTRNAYIQKYLAHLAATRKGVRTLAVVLGTFGACWLPFAIYCVVGSHEDPAVYTYATLLPATLNSMINP
IIYAFRNQEIQRALWLLLDGCFQSKVPFRSRSPSEVEFLEVLFQGPHHHHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKTIIALSYIFCLVFADYKDDDDAGRAGGANGSLELSSQLSAGPPGLLLPAVNPWDVLLCVSGTVIAGENALVVALIAST
PALRTPMFVLVGSLATADLLAGLGLILHFVFQYLVPSETVSLLTVGFLVASFAASVSSLLAITVDRYLSLYNPLTYYSRR
TLLGVHLLLAATWTVSLGLGLLPVLGWNCLAERAACSVVRPLARSHVALLSAAFFMVFGIMLHLYVRICQVVWRHAADLE
DNWETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLANEGKV
KEAQAAAEQLKTTRNAYIQKYLAHLAATRKGVRTLAVVLGTFGACWLPFAIYCVVGSHEDPAVYTYATLLPATLNSMINP
IIYAFRNQEIQRALWLLLDGCFQSKVPFRSRSPSEVEFLEVLFQGPHHHHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '3-{4-[(2,4-difluorophenyl)methyl]piperazin-1-yl}-7-methyl-N-(propan-2-yl)pyrido[3,4-b]pyrazin-2-amine' XY8 
3 'SODIUM ION'                                                                                            NA  
4 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   LYS n 
1 3   THR n 
1 4   ILE n 
1 5   ILE n 
1 6   ALA n 
1 7   LEU n 
1 8   SER n 
1 9   TYR n 
1 10  ILE n 
1 11  PHE n 
1 12  CYS n 
1 13  LEU n 
1 14  VAL n 
1 15  PHE n 
1 16  ALA n 
1 17  ASP n 
1 18  TYR n 
1 19  LYS n 
1 20  ASP n 
1 21  ASP n 
1 22  ASP n 
1 23  ASP n 
1 24  ALA n 
1 25  GLY n 
1 26  ARG n 
1 27  ALA n 
1 28  GLY n 
1 29  GLY n 
1 30  ALA n 
1 31  ASN n 
1 32  GLY n 
1 33  SER n 
1 34  LEU n 
1 35  GLU n 
1 36  LEU n 
1 37  SER n 
1 38  SER n 
1 39  GLN n 
1 40  LEU n 
1 41  SER n 
1 42  ALA n 
1 43  GLY n 
1 44  PRO n 
1 45  PRO n 
1 46  GLY n 
1 47  LEU n 
1 48  LEU n 
1 49  LEU n 
1 50  PRO n 
1 51  ALA n 
1 52  VAL n 
1 53  ASN n 
1 54  PRO n 
1 55  TRP n 
1 56  ASP n 
1 57  VAL n 
1 58  LEU n 
1 59  LEU n 
1 60  CYS n 
1 61  VAL n 
1 62  SER n 
1 63  GLY n 
1 64  THR n 
1 65  VAL n 
1 66  ILE n 
1 67  ALA n 
1 68  GLY n 
1 69  GLU n 
1 70  ASN n 
1 71  ALA n 
1 72  LEU n 
1 73  VAL n 
1 74  VAL n 
1 75  ALA n 
1 76  LEU n 
1 77  ILE n 
1 78  ALA n 
1 79  SER n 
1 80  THR n 
1 81  PRO n 
1 82  ALA n 
1 83  LEU n 
1 84  ARG n 
1 85  THR n 
1 86  PRO n 
1 87  MET n 
1 88  PHE n 
1 89  VAL n 
1 90  LEU n 
1 91  VAL n 
1 92  GLY n 
1 93  SER n 
1 94  LEU n 
1 95  ALA n 
1 96  THR n 
1 97  ALA n 
1 98  ASP n 
1 99  LEU n 
1 100 LEU n 
1 101 ALA n 
1 102 GLY n 
1 103 LEU n 
1 104 GLY n 
1 105 LEU n 
1 106 ILE n 
1 107 LEU n 
1 108 HIS n 
1 109 PHE n 
1 110 VAL n 
1 111 PHE n 
1 112 GLN n 
1 113 TYR n 
1 114 LEU n 
1 115 VAL n 
1 116 PRO n 
1 117 SER n 
1 118 GLU n 
1 119 THR n 
1 120 VAL n 
1 121 SER n 
1 122 LEU n 
1 123 LEU n 
1 124 THR n 
1 125 VAL n 
1 126 GLY n 
1 127 PHE n 
1 128 LEU n 
1 129 VAL n 
1 130 ALA n 
1 131 SER n 
1 132 PHE n 
1 133 ALA n 
1 134 ALA n 
1 135 SER n 
1 136 VAL n 
1 137 SER n 
1 138 SER n 
1 139 LEU n 
1 140 LEU n 
1 141 ALA n 
1 142 ILE n 
1 143 THR n 
1 144 VAL n 
1 145 ASP n 
1 146 ARG n 
1 147 TYR n 
1 148 LEU n 
1 149 SER n 
1 150 LEU n 
1 151 TYR n 
1 152 ASN n 
1 153 PRO n 
1 154 LEU n 
1 155 THR n 
1 156 TYR n 
1 157 TYR n 
1 158 SER n 
1 159 ARG n 
1 160 ARG n 
1 161 THR n 
1 162 LEU n 
1 163 LEU n 
1 164 GLY n 
1 165 VAL n 
1 166 HIS n 
1 167 LEU n 
1 168 LEU n 
1 169 LEU n 
1 170 ALA n 
1 171 ALA n 
1 172 THR n 
1 173 TRP n 
1 174 THR n 
1 175 VAL n 
1 176 SER n 
1 177 LEU n 
1 178 GLY n 
1 179 LEU n 
1 180 GLY n 
1 181 LEU n 
1 182 LEU n 
1 183 PRO n 
1 184 VAL n 
1 185 LEU n 
1 186 GLY n 
1 187 TRP n 
1 188 ASN n 
1 189 CYS n 
1 190 LEU n 
1 191 ALA n 
1 192 GLU n 
1 193 ARG n 
1 194 ALA n 
1 195 ALA n 
1 196 CYS n 
1 197 SER n 
1 198 VAL n 
1 199 VAL n 
1 200 ARG n 
1 201 PRO n 
1 202 LEU n 
1 203 ALA n 
1 204 ARG n 
1 205 SER n 
1 206 HIS n 
1 207 VAL n 
1 208 ALA n 
1 209 LEU n 
1 210 LEU n 
1 211 SER n 
1 212 ALA n 
1 213 ALA n 
1 214 PHE n 
1 215 PHE n 
1 216 MET n 
1 217 VAL n 
1 218 PHE n 
1 219 GLY n 
1 220 ILE n 
1 221 MET n 
1 222 LEU n 
1 223 HIS n 
1 224 LEU n 
1 225 TYR n 
1 226 VAL n 
1 227 ARG n 
1 228 ILE n 
1 229 CYS n 
1 230 GLN n 
1 231 VAL n 
1 232 VAL n 
1 233 TRP n 
1 234 ARG n 
1 235 HIS n 
1 236 ALA n 
1 237 ALA n 
1 238 ASP n 
1 239 LEU n 
1 240 GLU n 
1 241 ASP n 
1 242 ASN n 
1 243 TRP n 
1 244 GLU n 
1 245 THR n 
1 246 LEU n 
1 247 ASN n 
1 248 ASP n 
1 249 ASN n 
1 250 LEU n 
1 251 LYS n 
1 252 VAL n 
1 253 ILE n 
1 254 GLU n 
1 255 LYS n 
1 256 ALA n 
1 257 ASP n 
1 258 ASN n 
1 259 ALA n 
1 260 ALA n 
1 261 GLN n 
1 262 VAL n 
1 263 LYS n 
1 264 ASP n 
1 265 ALA n 
1 266 LEU n 
1 267 THR n 
1 268 LYS n 
1 269 MET n 
1 270 ARG n 
1 271 ALA n 
1 272 ALA n 
1 273 ALA n 
1 274 LEU n 
1 275 ASP n 
1 276 ALA n 
1 277 GLN n 
1 278 LYS n 
1 279 ALA n 
1 280 THR n 
1 281 PRO n 
1 282 PRO n 
1 283 LYS n 
1 284 LEU n 
1 285 GLU n 
1 286 ASP n 
1 287 LYS n 
1 288 SER n 
1 289 PRO n 
1 290 ASP n 
1 291 SER n 
1 292 PRO n 
1 293 GLU n 
1 294 MET n 
1 295 LYS n 
1 296 ASP n 
1 297 PHE n 
1 298 ARG n 
1 299 HIS n 
1 300 GLY n 
1 301 PHE n 
1 302 ASP n 
1 303 ILE n 
1 304 LEU n 
1 305 VAL n 
1 306 GLY n 
1 307 GLN n 
1 308 ILE n 
1 309 ASP n 
1 310 ASP n 
1 311 ALA n 
1 312 LEU n 
1 313 LYS n 
1 314 LEU n 
1 315 ALA n 
1 316 ASN n 
1 317 GLU n 
1 318 GLY n 
1 319 LYS n 
1 320 VAL n 
1 321 LYS n 
1 322 GLU n 
1 323 ALA n 
1 324 GLN n 
1 325 ALA n 
1 326 ALA n 
1 327 ALA n 
1 328 GLU n 
1 329 GLN n 
1 330 LEU n 
1 331 LYS n 
1 332 THR n 
1 333 THR n 
1 334 ARG n 
1 335 ASN n 
1 336 ALA n 
1 337 TYR n 
1 338 ILE n 
1 339 GLN n 
1 340 LYS n 
1 341 TYR n 
1 342 LEU n 
1 343 ALA n 
1 344 HIS n 
1 345 LEU n 
1 346 ALA n 
1 347 ALA n 
1 348 THR n 
1 349 ARG n 
1 350 LYS n 
1 351 GLY n 
1 352 VAL n 
1 353 ARG n 
1 354 THR n 
1 355 LEU n 
1 356 ALA n 
1 357 VAL n 
1 358 VAL n 
1 359 LEU n 
1 360 GLY n 
1 361 THR n 
1 362 PHE n 
1 363 GLY n 
1 364 ALA n 
1 365 CYS n 
1 366 TRP n 
1 367 LEU n 
1 368 PRO n 
1 369 PHE n 
1 370 ALA n 
1 371 ILE n 
1 372 TYR n 
1 373 CYS n 
1 374 VAL n 
1 375 VAL n 
1 376 GLY n 
1 377 SER n 
1 378 HIS n 
1 379 GLU n 
1 380 ASP n 
1 381 PRO n 
1 382 ALA n 
1 383 VAL n 
1 384 TYR n 
1 385 THR n 
1 386 TYR n 
1 387 ALA n 
1 388 THR n 
1 389 LEU n 
1 390 LEU n 
1 391 PRO n 
1 392 ALA n 
1 393 THR n 
1 394 LEU n 
1 395 ASN n 
1 396 SER n 
1 397 MET n 
1 398 ILE n 
1 399 ASN n 
1 400 PRO n 
1 401 ILE n 
1 402 ILE n 
1 403 TYR n 
1 404 ALA n 
1 405 PHE n 
1 406 ARG n 
1 407 ASN n 
1 408 GLN n 
1 409 GLU n 
1 410 ILE n 
1 411 GLN n 
1 412 ARG n 
1 413 ALA n 
1 414 LEU n 
1 415 TRP n 
1 416 LEU n 
1 417 LEU n 
1 418 LEU n 
1 419 ASP n 
1 420 GLY n 
1 421 CYS n 
1 422 PHE n 
1 423 GLN n 
1 424 SER n 
1 425 LYS n 
1 426 VAL n 
1 427 PRO n 
1 428 PHE n 
1 429 ARG n 
1 430 SER n 
1 431 ARG n 
1 432 SER n 
1 433 PRO n 
1 434 SER n 
1 435 GLU n 
1 436 VAL n 
1 437 GLU n 
1 438 PHE n 
1 439 LEU n 
1 440 GLU n 
1 441 VAL n 
1 442 LEU n 
1 443 PHE n 
1 444 GLN n 
1 445 GLY n 
1 446 PRO n 
1 447 HIS n 
1 448 HIS n 
1 449 HIS n 
1 450 HIS n 
1 451 HIS n 
1 452 HIS n 
1 453 HIS n 
1 454 HIS n 
1 455 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   236 human ? GPR6 ? ? ? ? ? ? 'Homo sapiens'     9606 ? ? ? ? ? ? ? human 'Homo sapiens' 9606 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 237 343 ?     ? cybC ? ? ? ? ? ? 'Escherichia coli' 562  ? ? ? ? ? ? ? human 'Homo sapiens' 9606 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 3 sample 'Biological sequence' 344 455 human ? GPR6 ? ? ? ? ? ? 'Homo sapiens'     9606 ? ? ? ? ? ? ? human 'Homo sapiens' 9606 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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  
HIS 'L-peptide linking' y HISTIDINE                                                                                               
? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                                                                                   
? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                                              
? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                                                                                 
? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                                                                                  
? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                                                                              
? 'C5 H11 N O2 S'  149.211 
NA  non-polymer         . 'SODIUM ION'                                                                                            
? 'Na 1'           22.990  
PHE 'L-peptide linking' y PHENYLALANINE                                                                                           
? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                                                                                 
? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                                                                                  
? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                                                                                               
? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                                              
? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                                                                                
? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                                                                                  
? 'C5 H11 N O2'    117.146 
XY8 non-polymer         . '3-{4-[(2,4-difluorophenyl)methyl]piperazin-1-yl}-7-methyl-N-(propan-2-yl)pyrido[3,4-b]pyrazin-2-amine' 
? 'C22 H26 F2 N6'  412.479 
# 
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   21   ?    ?   ?   A . n 
A 1 2   LYS 2   22   ?    ?   ?   A . n 
A 1 3   THR 3   23   ?    ?   ?   A . n 
A 1 4   ILE 4   24   ?    ?   ?   A . n 
A 1 5   ILE 5   25   ?    ?   ?   A . n 
A 1 6   ALA 6   26   ?    ?   ?   A . n 
A 1 7   LEU 7   27   ?    ?   ?   A . n 
A 1 8   SER 8   28   ?    ?   ?   A . n 
A 1 9   TYR 9   29   ?    ?   ?   A . n 
A 1 10  ILE 10  30   ?    ?   ?   A . n 
A 1 11  PHE 11  31   ?    ?   ?   A . n 
A 1 12  CYS 12  32   ?    ?   ?   A . n 
A 1 13  LEU 13  33   ?    ?   ?   A . n 
A 1 14  VAL 14  34   ?    ?   ?   A . n 
A 1 15  PHE 15  35   ?    ?   ?   A . n 
A 1 16  ALA 16  36   ?    ?   ?   A . n 
A 1 17  ASP 17  37   ?    ?   ?   A . n 
A 1 18  TYR 18  38   ?    ?   ?   A . n 
A 1 19  LYS 19  39   ?    ?   ?   A . n 
A 1 20  ASP 20  40   ?    ?   ?   A . n 
A 1 21  ASP 21  41   ?    ?   ?   A . n 
A 1 22  ASP 22  42   ?    ?   ?   A . n 
A 1 23  ASP 23  43   ?    ?   ?   A . n 
A 1 24  ALA 24  44   ?    ?   ?   A . n 
A 1 25  GLY 25  45   ?    ?   ?   A . n 
A 1 26  ARG 26  46   ?    ?   ?   A . n 
A 1 27  ALA 27  47   ?    ?   ?   A . n 
A 1 28  GLY 28  48   ?    ?   ?   A . n 
A 1 29  GLY 29  49   ?    ?   ?   A . n 
A 1 30  ALA 30  50   ?    ?   ?   A . n 
A 1 31  ASN 31  51   ?    ?   ?   A . n 
A 1 32  GLY 32  52   ?    ?   ?   A . n 
A 1 33  SER 33  53   ?    ?   ?   A . n 
A 1 34  LEU 34  54   ?    ?   ?   A . n 
A 1 35  GLU 35  55   ?    ?   ?   A . n 
A 1 36  LEU 36  56   ?    ?   ?   A . n 
A 1 37  SER 37  57   ?    ?   ?   A . n 
A 1 38  SER 38  58   ?    ?   ?   A . n 
A 1 39  GLN 39  59   ?    ?   ?   A . n 
A 1 40  LEU 40  60   ?    ?   ?   A . n 
A 1 41  SER 41  61   ?    ?   ?   A . n 
A 1 42  ALA 42  62   ?    ?   ?   A . n 
A 1 43  GLY 43  63   ?    ?   ?   A . n 
A 1 44  PRO 44  64   ?    ?   ?   A . n 
A 1 45  PRO 45  65   ?    ?   ?   A . n 
A 1 46  GLY 46  66   ?    ?   ?   A . n 
A 1 47  LEU 47  67   ?    ?   ?   A . n 
A 1 48  LEU 48  68   68   LEU LEU A . n 
A 1 49  LEU 49  69   69   LEU LEU A . n 
A 1 50  PRO 50  70   70   PRO PRO A . n 
A 1 51  ALA 51  71   71   ALA ALA A . n 
A 1 52  VAL 52  72   72   VAL VAL A . n 
A 1 53  ASN 53  73   73   ASN ASN A . n 
A 1 54  PRO 54  74   74   PRO PRO A . n 
A 1 55  TRP 55  75   75   TRP TRP A . n 
A 1 56  ASP 56  76   76   ASP ASP A . n 
A 1 57  VAL 57  77   77   VAL VAL A . n 
A 1 58  LEU 58  78   78   LEU LEU A . n 
A 1 59  LEU 59  79   79   LEU LEU A . n 
A 1 60  CYS 60  80   80   CYS CYS A . n 
A 1 61  VAL 61  81   81   VAL VAL A . n 
A 1 62  SER 62  82   82   SER SER A . n 
A 1 63  GLY 63  83   83   GLY GLY A . n 
A 1 64  THR 64  84   84   THR THR A . n 
A 1 65  VAL 65  85   85   VAL VAL A . n 
A 1 66  ILE 66  86   86   ILE ILE A . n 
A 1 67  ALA 67  87   87   ALA ALA A . n 
A 1 68  GLY 68  88   88   GLY GLY A . n 
A 1 69  GLU 69  89   89   GLU GLU A . n 
A 1 70  ASN 70  90   90   ASN ASN A . n 
A 1 71  ALA 71  91   91   ALA ALA A . n 
A 1 72  LEU 72  92   92   LEU LEU A . n 
A 1 73  VAL 73  93   93   VAL VAL A . n 
A 1 74  VAL 74  94   94   VAL VAL A . n 
A 1 75  ALA 75  95   95   ALA ALA A . n 
A 1 76  LEU 76  96   96   LEU LEU A . n 
A 1 77  ILE 77  97   97   ILE ILE A . n 
A 1 78  ALA 78  98   98   ALA ALA A . n 
A 1 79  SER 79  99   99   SER SER A . n 
A 1 80  THR 80  100  100  THR THR A . n 
A 1 81  PRO 81  101  101  PRO PRO A . n 
A 1 82  ALA 82  102  102  ALA ALA A . n 
A 1 83  LEU 83  103  103  LEU LEU A . n 
A 1 84  ARG 84  104  104  ARG ARG A . n 
A 1 85  THR 85  105  105  THR THR A . n 
A 1 86  PRO 86  106  106  PRO PRO A . n 
A 1 87  MET 87  107  107  MET MET A . n 
A 1 88  PHE 88  108  108  PHE PHE A . n 
A 1 89  VAL 89  109  109  VAL VAL A . n 
A 1 90  LEU 90  110  110  LEU LEU A . n 
A 1 91  VAL 91  111  111  VAL VAL A . n 
A 1 92  GLY 92  112  112  GLY GLY A . n 
A 1 93  SER 93  113  113  SER SER A . n 
A 1 94  LEU 94  114  114  LEU LEU A . n 
A 1 95  ALA 95  115  115  ALA ALA A . n 
A 1 96  THR 96  116  116  THR THR A . n 
A 1 97  ALA 97  117  117  ALA ALA A . n 
A 1 98  ASP 98  118  118  ASP ASP A . n 
A 1 99  LEU 99  119  119  LEU LEU A . n 
A 1 100 LEU 100 120  120  LEU LEU A . n 
A 1 101 ALA 101 121  121  ALA ALA A . n 
A 1 102 GLY 102 122  122  GLY GLY A . n 
A 1 103 LEU 103 123  123  LEU LEU A . n 
A 1 104 GLY 104 124  124  GLY GLY A . n 
A 1 105 LEU 105 125  125  LEU LEU A . n 
A 1 106 ILE 106 126  126  ILE ILE A . n 
A 1 107 LEU 107 127  127  LEU LEU A . n 
A 1 108 HIS 108 128  128  HIS HIS A . n 
A 1 109 PHE 109 129  129  PHE PHE A . n 
A 1 110 VAL 110 130  130  VAL VAL A . n 
A 1 111 PHE 111 131  131  PHE PHE A . n 
A 1 112 GLN 112 132  132  GLN GLN A . n 
A 1 113 TYR 113 133  133  TYR TYR A . n 
A 1 114 LEU 114 134  134  LEU LEU A . n 
A 1 115 VAL 115 135  135  VAL VAL A . n 
A 1 116 PRO 116 136  136  PRO PRO A . n 
A 1 117 SER 117 137  137  SER SER A . n 
A 1 118 GLU 118 138  138  GLU GLU A . n 
A 1 119 THR 119 139  139  THR THR A . n 
A 1 120 VAL 120 140  140  VAL VAL A . n 
A 1 121 SER 121 141  141  SER SER A . n 
A 1 122 LEU 122 142  142  LEU LEU A . n 
A 1 123 LEU 123 143  143  LEU LEU A . n 
A 1 124 THR 124 144  144  THR THR A . n 
A 1 125 VAL 125 145  145  VAL VAL A . n 
A 1 126 GLY 126 146  146  GLY GLY A . n 
A 1 127 PHE 127 147  147  PHE PHE A . n 
A 1 128 LEU 128 148  148  LEU LEU A . n 
A 1 129 VAL 129 149  149  VAL VAL A . n 
A 1 130 ALA 130 150  150  ALA ALA A . n 
A 1 131 SER 131 151  151  SER SER A . n 
A 1 132 PHE 132 152  152  PHE PHE A . n 
A 1 133 ALA 133 153  153  ALA ALA A . n 
A 1 134 ALA 134 154  154  ALA ALA A . n 
A 1 135 SER 135 155  155  SER SER A . n 
A 1 136 VAL 136 156  156  VAL VAL A . n 
A 1 137 SER 137 157  157  SER SER A . n 
A 1 138 SER 138 158  158  SER SER A . n 
A 1 139 LEU 139 159  159  LEU LEU A . n 
A 1 140 LEU 140 160  160  LEU LEU A . n 
A 1 141 ALA 141 161  161  ALA ALA A . n 
A 1 142 ILE 142 162  162  ILE ILE A . n 
A 1 143 THR 143 163  163  THR THR A . n 
A 1 144 VAL 144 164  164  VAL VAL A . n 
A 1 145 ASP 145 165  165  ASP ASP A . n 
A 1 146 ARG 146 166  166  ARG ARG A . n 
A 1 147 TYR 147 167  167  TYR TYR A . n 
A 1 148 LEU 148 168  168  LEU LEU A . n 
A 1 149 SER 149 169  169  SER SER A . n 
A 1 150 LEU 150 170  170  LEU LEU A . n 
A 1 151 TYR 151 171  171  TYR TYR A . n 
A 1 152 ASN 152 172  172  ASN ASN A . n 
A 1 153 PRO 153 173  173  PRO PRO A . n 
A 1 154 LEU 154 174  174  LEU LEU A . n 
A 1 155 THR 155 175  175  THR THR A . n 
A 1 156 TYR 156 176  176  TYR TYR A . n 
A 1 157 TYR 157 177  177  TYR TYR A . n 
A 1 158 SER 158 178  178  SER SER A . n 
A 1 159 ARG 159 179  179  ARG ARG A . n 
A 1 160 ARG 160 180  180  ARG ARG A . n 
A 1 161 THR 161 181  181  THR THR A . n 
A 1 162 LEU 162 182  182  LEU LEU A . n 
A 1 163 LEU 163 183  183  LEU LEU A . n 
A 1 164 GLY 164 184  184  GLY GLY A . n 
A 1 165 VAL 165 185  185  VAL VAL A . n 
A 1 166 HIS 166 186  186  HIS HIS A . n 
A 1 167 LEU 167 187  187  LEU LEU A . n 
A 1 168 LEU 168 188  188  LEU LEU A . n 
A 1 169 LEU 169 189  189  LEU LEU A . n 
A 1 170 ALA 170 190  190  ALA ALA A . n 
A 1 171 ALA 171 191  191  ALA ALA A . n 
A 1 172 THR 172 192  192  THR THR A . n 
A 1 173 TRP 173 193  193  TRP TRP A . n 
A 1 174 THR 174 194  194  THR THR A . n 
A 1 175 VAL 175 195  195  VAL VAL A . n 
A 1 176 SER 176 196  196  SER SER A . n 
A 1 177 LEU 177 197  197  LEU LEU A . n 
A 1 178 GLY 178 198  198  GLY GLY A . n 
A 1 179 LEU 179 199  199  LEU LEU A . n 
A 1 180 GLY 180 200  200  GLY GLY A . n 
A 1 181 LEU 181 201  201  LEU LEU A . n 
A 1 182 LEU 182 202  202  LEU LEU A . n 
A 1 183 PRO 183 203  203  PRO PRO A . n 
A 1 184 VAL 184 204  204  VAL VAL A . n 
A 1 185 LEU 185 205  205  LEU LEU A . n 
A 1 186 GLY 186 206  206  GLY GLY A . n 
A 1 187 TRP 187 207  207  TRP TRP A . n 
A 1 188 ASN 188 208  208  ASN ASN A . n 
A 1 189 CYS 189 209  209  CYS CYS A . n 
A 1 190 LEU 190 210  210  LEU LEU A . n 
A 1 191 ALA 191 211  211  ALA ALA A . n 
A 1 192 GLU 192 212  212  GLU GLU A . n 
A 1 193 ARG 193 213  213  ARG ARG A . n 
A 1 194 ALA 194 214  214  ALA ALA A . n 
A 1 195 ALA 195 215  215  ALA ALA A . n 
A 1 196 CYS 196 216  216  CYS CYS A . n 
A 1 197 SER 197 217  217  SER SER A . n 
A 1 198 VAL 198 218  218  VAL VAL A . n 
A 1 199 VAL 199 219  219  VAL VAL A . n 
A 1 200 ARG 200 220  220  ARG ARG A . n 
A 1 201 PRO 201 221  221  PRO PRO A . n 
A 1 202 LEU 202 222  222  LEU LEU A . n 
A 1 203 ALA 203 223  223  ALA ALA A . n 
A 1 204 ARG 204 224  224  ARG ARG A . n 
A 1 205 SER 205 225  225  SER SER A . n 
A 1 206 HIS 206 226  226  HIS HIS A . n 
A 1 207 VAL 207 227  227  VAL VAL A . n 
A 1 208 ALA 208 228  228  ALA ALA A . n 
A 1 209 LEU 209 229  229  LEU LEU A . n 
A 1 210 LEU 210 230  230  LEU LEU A . n 
A 1 211 SER 211 231  231  SER SER A . n 
A 1 212 ALA 212 232  232  ALA ALA A . n 
A 1 213 ALA 213 233  233  ALA ALA A . n 
A 1 214 PHE 214 234  234  PHE PHE A . n 
A 1 215 PHE 215 235  235  PHE PHE A . n 
A 1 216 MET 216 236  236  MET MET A . n 
A 1 217 VAL 217 237  237  VAL VAL A . n 
A 1 218 PHE 218 238  238  PHE PHE A . n 
A 1 219 GLY 219 239  239  GLY GLY A . n 
A 1 220 ILE 220 240  240  ILE ILE A . n 
A 1 221 MET 221 241  241  MET MET A . n 
A 1 222 LEU 222 242  242  LEU LEU A . n 
A 1 223 HIS 223 243  243  HIS HIS A . n 
A 1 224 LEU 224 244  244  LEU LEU A . n 
A 1 225 TYR 225 245  245  TYR TYR A . n 
A 1 226 VAL 226 246  246  VAL VAL A . n 
A 1 227 ARG 227 247  247  ARG ARG A . n 
A 1 228 ILE 228 248  248  ILE ILE A . n 
A 1 229 CYS 229 249  249  CYS CYS A . n 
A 1 230 GLN 230 250  250  GLN GLN A . n 
A 1 231 VAL 231 251  251  VAL VAL A . n 
A 1 232 VAL 232 252  252  VAL VAL A . n 
A 1 233 TRP 233 253  253  TRP TRP A . n 
A 1 234 ARG 234 254  254  ARG ARG A . n 
A 1 235 HIS 235 255  255  HIS HIS A . n 
A 1 236 ALA 236 256  256  ALA ALA A . n 
A 1 237 ALA 237 1001 1001 ALA ALA A . n 
A 1 238 ASP 238 1002 1002 ASP ASP A . n 
A 1 239 LEU 239 1003 1003 LEU LEU A . n 
A 1 240 GLU 240 1004 1004 GLU GLU A . n 
A 1 241 ASP 241 1005 1005 ASP ASP A . n 
A 1 242 ASN 242 1006 1006 ASN ASN A . n 
A 1 243 TRP 243 1007 1007 TRP TRP A . n 
A 1 244 GLU 244 1008 1008 GLU GLU A . n 
A 1 245 THR 245 1009 1009 THR THR A . n 
A 1 246 LEU 246 1010 1010 LEU LEU A . n 
A 1 247 ASN 247 1011 1011 ASN ASN A . n 
A 1 248 ASP 248 1012 1012 ASP ASP A . n 
A 1 249 ASN 249 1013 1013 ASN ASN A . n 
A 1 250 LEU 250 1014 1014 LEU LEU A . n 
A 1 251 LYS 251 1015 1015 LYS LYS A . n 
A 1 252 VAL 252 1016 1016 VAL VAL A . n 
A 1 253 ILE 253 1017 1017 ILE ILE A . n 
A 1 254 GLU 254 1018 1018 GLU GLU A . n 
A 1 255 LYS 255 1019 1019 LYS LYS A . n 
A 1 256 ALA 256 1020 1020 ALA ALA A . n 
A 1 257 ASP 257 1021 1021 ASP ASP A . n 
A 1 258 ASN 258 1022 1022 ASN ASN A . n 
A 1 259 ALA 259 1023 1023 ALA ALA A . n 
A 1 260 ALA 260 1024 1024 ALA ALA A . n 
A 1 261 GLN 261 1025 1025 GLN GLN A . n 
A 1 262 VAL 262 1026 1026 VAL VAL A . n 
A 1 263 LYS 263 1027 1027 LYS LYS A . n 
A 1 264 ASP 264 1028 1028 ASP ASP A . n 
A 1 265 ALA 265 1029 1029 ALA ALA A . n 
A 1 266 LEU 266 1030 1030 LEU LEU A . n 
A 1 267 THR 267 1031 1031 THR THR A . n 
A 1 268 LYS 268 1032 1032 LYS LYS A . n 
A 1 269 MET 269 1033 1033 MET MET A . n 
A 1 270 ARG 270 1034 1034 ARG ARG A . n 
A 1 271 ALA 271 1035 1035 ALA ALA A . n 
A 1 272 ALA 272 1036 1036 ALA ALA A . n 
A 1 273 ALA 273 1037 1037 ALA ALA A . n 
A 1 274 LEU 274 1038 1038 LEU LEU A . n 
A 1 275 ASP 275 1039 1039 ASP ASP A . n 
A 1 276 ALA 276 1040 1040 ALA ALA A . n 
A 1 277 GLN 277 1041 1041 GLN GLN A . n 
A 1 278 LYS 278 1042 1042 LYS LYS A . n 
A 1 279 ALA 279 1043 1043 ALA ALA A . n 
A 1 280 THR 280 1044 1044 THR THR A . n 
A 1 281 PRO 281 1045 1045 PRO PRO A . n 
A 1 282 PRO 282 1046 ?    ?   ?   A . n 
A 1 283 LYS 283 1047 ?    ?   ?   A . n 
A 1 284 LEU 284 1048 ?    ?   ?   A . n 
A 1 285 GLU 285 1049 ?    ?   ?   A . n 
A 1 286 ASP 286 1050 ?    ?   ?   A . n 
A 1 287 LYS 287 1051 ?    ?   ?   A . n 
A 1 288 SER 288 1052 ?    ?   ?   A . n 
A 1 289 PRO 289 1053 ?    ?   ?   A . n 
A 1 290 ASP 290 1054 ?    ?   ?   A . n 
A 1 291 SER 291 1055 ?    ?   ?   A . n 
A 1 292 PRO 292 1056 ?    ?   ?   A . n 
A 1 293 GLU 293 1057 ?    ?   ?   A . n 
A 1 294 MET 294 1058 ?    ?   ?   A . n 
A 1 295 LYS 295 1059 ?    ?   ?   A . n 
A 1 296 ASP 296 1060 ?    ?   ?   A . n 
A 1 297 PHE 297 1061 ?    ?   ?   A . n 
A 1 298 ARG 298 1062 ?    ?   ?   A . n 
A 1 299 HIS 299 1063 ?    ?   ?   A . n 
A 1 300 GLY 300 1064 ?    ?   ?   A . n 
A 1 301 PHE 301 1065 ?    ?   ?   A . n 
A 1 302 ASP 302 1066 1066 ASP ASP A . n 
A 1 303 ILE 303 1067 1067 ILE ILE A . n 
A 1 304 LEU 304 1068 1068 LEU LEU A . n 
A 1 305 VAL 305 1069 1069 VAL VAL A . n 
A 1 306 GLY 306 1070 1070 GLY GLY A . n 
A 1 307 GLN 307 1071 1071 GLN GLN A . n 
A 1 308 ILE 308 1072 1072 ILE ILE A . n 
A 1 309 ASP 309 1073 1073 ASP ASP A . n 
A 1 310 ASP 310 1074 1074 ASP ASP A . n 
A 1 311 ALA 311 1075 1075 ALA ALA A . n 
A 1 312 LEU 312 1076 1076 LEU LEU A . n 
A 1 313 LYS 313 1077 1077 LYS LYS A . n 
A 1 314 LEU 314 1078 1078 LEU LEU A . n 
A 1 315 ALA 315 1079 1079 ALA ALA A . n 
A 1 316 ASN 316 1080 1080 ASN ASN A . n 
A 1 317 GLU 317 1081 1081 GLU GLU A . n 
A 1 318 GLY 318 1082 1082 GLY GLY A . n 
A 1 319 LYS 319 1083 1083 LYS LYS A . n 
A 1 320 VAL 320 1084 1084 VAL VAL A . n 
A 1 321 LYS 321 1085 1085 LYS LYS A . n 
A 1 322 GLU 322 1086 1086 GLU GLU A . n 
A 1 323 ALA 323 1087 1087 ALA ALA A . n 
A 1 324 GLN 324 1088 1088 GLN GLN A . n 
A 1 325 ALA 325 1089 1089 ALA ALA A . n 
A 1 326 ALA 326 1090 1090 ALA ALA A . n 
A 1 327 ALA 327 1091 1091 ALA ALA A . n 
A 1 328 GLU 328 1092 1092 GLU GLU A . n 
A 1 329 GLN 329 1093 1093 GLN GLN A . n 
A 1 330 LEU 330 1094 1094 LEU LEU A . n 
A 1 331 LYS 331 1095 1095 LYS LYS A . n 
A 1 332 THR 332 1096 1096 THR THR A . n 
A 1 333 THR 333 1097 1097 THR THR A . n 
A 1 334 ARG 334 1098 1098 ARG ARG A . n 
A 1 335 ASN 335 1099 1099 ASN ASN A . n 
A 1 336 ALA 336 1100 1100 ALA ALA A . n 
A 1 337 TYR 337 1101 1101 TYR TYR A . n 
A 1 338 ILE 338 1102 1102 ILE ILE A . n 
A 1 339 GLN 339 1103 1103 GLN GLN A . n 
A 1 340 LYS 340 1104 1104 LYS LYS A . n 
A 1 341 TYR 341 1105 1105 TYR TYR A . n 
A 1 342 LEU 342 1106 1106 LEU LEU A . n 
A 1 343 ALA 343 900  900  ALA ALA A . n 
A 1 344 HIS 344 270  270  HIS HIS A . n 
A 1 345 LEU 345 271  271  LEU LEU A . n 
A 1 346 ALA 346 272  272  ALA ALA A . n 
A 1 347 ALA 347 273  273  ALA ALA A . n 
A 1 348 THR 348 274  274  THR THR A . n 
A 1 349 ARG 349 275  275  ARG ARG A . n 
A 1 350 LYS 350 276  276  LYS LYS A . n 
A 1 351 GLY 351 277  277  GLY GLY A . n 
A 1 352 VAL 352 278  278  VAL VAL A . n 
A 1 353 ARG 353 279  279  ARG ARG A . n 
A 1 354 THR 354 280  280  THR THR A . n 
A 1 355 LEU 355 281  281  LEU LEU A . n 
A 1 356 ALA 356 282  282  ALA ALA A . n 
A 1 357 VAL 357 283  283  VAL VAL A . n 
A 1 358 VAL 358 284  284  VAL VAL A . n 
A 1 359 LEU 359 285  285  LEU LEU A . n 
A 1 360 GLY 360 286  286  GLY GLY A . n 
A 1 361 THR 361 287  287  THR THR A . n 
A 1 362 PHE 362 288  288  PHE PHE A . n 
A 1 363 GLY 363 289  289  GLY GLY A . n 
A 1 364 ALA 364 290  290  ALA ALA A . n 
A 1 365 CYS 365 291  291  CYS CYS A . n 
A 1 366 TRP 366 292  292  TRP TRP A . n 
A 1 367 LEU 367 293  293  LEU LEU A . n 
A 1 368 PRO 368 294  294  PRO PRO A . n 
A 1 369 PHE 369 295  295  PHE PHE A . n 
A 1 370 ALA 370 296  296  ALA ALA A . n 
A 1 371 ILE 371 297  297  ILE ILE A . n 
A 1 372 TYR 372 298  298  TYR TYR A . n 
A 1 373 CYS 373 299  299  CYS CYS A . n 
A 1 374 VAL 374 300  300  VAL VAL A . n 
A 1 375 VAL 375 301  301  VAL VAL A . n 
A 1 376 GLY 376 302  302  GLY GLY A . n 
A 1 377 SER 377 303  303  SER SER A . n 
A 1 378 HIS 378 304  304  HIS HIS A . n 
A 1 379 GLU 379 305  305  GLU GLU A . n 
A 1 380 ASP 380 306  306  ASP ASP A . n 
A 1 381 PRO 381 307  307  PRO PRO A . n 
A 1 382 ALA 382 308  308  ALA ALA A . n 
A 1 383 VAL 383 309  309  VAL VAL A . n 
A 1 384 TYR 384 310  310  TYR TYR A . n 
A 1 385 THR 385 311  311  THR THR A . n 
A 1 386 TYR 386 312  312  TYR TYR A . n 
A 1 387 ALA 387 313  313  ALA ALA A . n 
A 1 388 THR 388 314  314  THR THR A . n 
A 1 389 LEU 389 315  315  LEU LEU A . n 
A 1 390 LEU 390 316  316  LEU LEU A . n 
A 1 391 PRO 391 317  317  PRO PRO A . n 
A 1 392 ALA 392 318  318  ALA ALA A . n 
A 1 393 THR 393 319  319  THR THR A . n 
A 1 394 LEU 394 320  320  LEU LEU A . n 
A 1 395 ASN 395 321  321  ASN ASN A . n 
A 1 396 SER 396 322  322  SER SER A . n 
A 1 397 MET 397 323  323  MET MET A . n 
A 1 398 ILE 398 324  324  ILE ILE A . n 
A 1 399 ASN 399 325  325  ASN ASN A . n 
A 1 400 PRO 400 326  326  PRO PRO A . n 
A 1 401 ILE 401 327  327  ILE ILE A . n 
A 1 402 ILE 402 328  328  ILE ILE A . n 
A 1 403 TYR 403 329  329  TYR TYR A . n 
A 1 404 ALA 404 330  330  ALA ALA A . n 
A 1 405 PHE 405 331  331  PHE PHE A . n 
A 1 406 ARG 406 332  332  ARG ARG A . n 
A 1 407 ASN 407 333  333  ASN ASN A . n 
A 1 408 GLN 408 334  334  GLN GLN A . n 
A 1 409 GLU 409 335  335  GLU GLU A . n 
A 1 410 ILE 410 336  336  ILE ILE A . n 
A 1 411 GLN 411 337  337  GLN GLN A . n 
A 1 412 ARG 412 338  338  ARG ARG A . n 
A 1 413 ALA 413 339  339  ALA ALA A . n 
A 1 414 LEU 414 340  340  LEU LEU A . n 
A 1 415 TRP 415 341  341  TRP TRP A . n 
A 1 416 LEU 416 342  342  LEU LEU A . n 
A 1 417 LEU 417 343  343  LEU LEU A . n 
A 1 418 LEU 418 344  344  LEU LEU A . n 
A 1 419 ASP 419 345  345  ASP ASP A . n 
A 1 420 GLY 420 346  346  GLY GLY A . n 
A 1 421 CYS 421 347  ?    ?   ?   A . n 
A 1 422 PHE 422 348  ?    ?   ?   A . n 
A 1 423 GLN 423 349  ?    ?   ?   A . n 
A 1 424 SER 424 350  ?    ?   ?   A . n 
A 1 425 LYS 425 351  ?    ?   ?   A . n 
A 1 426 VAL 426 352  ?    ?   ?   A . n 
A 1 427 PRO 427 353  ?    ?   ?   A . n 
A 1 428 PHE 428 354  ?    ?   ?   A . n 
A 1 429 ARG 429 355  ?    ?   ?   A . n 
A 1 430 SER 430 356  ?    ?   ?   A . n 
A 1 431 ARG 431 357  ?    ?   ?   A . n 
A 1 432 SER 432 358  ?    ?   ?   A . n 
A 1 433 PRO 433 359  ?    ?   ?   A . n 
A 1 434 SER 434 360  ?    ?   ?   A . n 
A 1 435 GLU 435 361  ?    ?   ?   A . n 
A 1 436 VAL 436 362  ?    ?   ?   A . n 
A 1 437 GLU 437 363  ?    ?   ?   A . n 
A 1 438 PHE 438 364  ?    ?   ?   A . n 
A 1 439 LEU 439 365  ?    ?   ?   A . n 
A 1 440 GLU 440 366  ?    ?   ?   A . n 
A 1 441 VAL 441 367  ?    ?   ?   A . n 
A 1 442 LEU 442 368  ?    ?   ?   A . n 
A 1 443 PHE 443 369  ?    ?   ?   A . n 
A 1 444 GLN 444 370  ?    ?   ?   A . n 
A 1 445 GLY 445 371  ?    ?   ?   A . n 
A 1 446 PRO 446 372  ?    ?   ?   A . n 
A 1 447 HIS 447 373  ?    ?   ?   A . n 
A 1 448 HIS 448 374  ?    ?   ?   A . n 
A 1 449 HIS 449 375  ?    ?   ?   A . n 
A 1 450 HIS 450 376  ?    ?   ?   A . n 
A 1 451 HIS 451 377  ?    ?   ?   A . n 
A 1 452 HIS 452 378  ?    ?   ?   A . n 
A 1 453 HIS 453 379  ?    ?   ?   A . n 
A 1 454 HIS 454 380  ?    ?   ?   A . n 
A 1 455 HIS 455 381  ?    ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        XY8 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   XY8 
_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 
B 2 XY8 1 1201 701 XY8 XY8 A . 
C 3 NA  1 1202 1   NA  NA  A . 
D 4 HOH 1 1301 4   HOH HOH A . 
D 4 HOH 2 1302 3   HOH HOH A . 
D 4 HOH 3 1303 5   HOH HOH A . 
D 4 HOH 4 1304 2   HOH HOH A . 
D 4 HOH 5 1305 1   HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LEU 69   ? CG  ? A LEU 49  CG  
2  1 Y 1 A LEU 69   ? CD1 ? A LEU 49  CD1 
3  1 Y 1 A LEU 69   ? CD2 ? A LEU 49  CD2 
4  1 Y 1 A LEU 134  ? CG  ? A LEU 114 CG  
5  1 Y 1 A LEU 134  ? CD1 ? A LEU 114 CD1 
6  1 Y 1 A LEU 134  ? CD2 ? A LEU 114 CD2 
7  1 Y 1 A VAL 135  ? CG1 ? A VAL 115 CG1 
8  1 Y 1 A VAL 135  ? CG2 ? A VAL 115 CG2 
9  1 Y 1 A TYR 177  ? CG  ? A TYR 157 CG  
10 1 Y 1 A TYR 177  ? CD1 ? A TYR 157 CD1 
11 1 Y 1 A TYR 177  ? CD2 ? A TYR 157 CD2 
12 1 Y 1 A TYR 177  ? CE1 ? A TYR 157 CE1 
13 1 Y 1 A TYR 177  ? CE2 ? A TYR 157 CE2 
14 1 Y 1 A TYR 177  ? CZ  ? A TYR 157 CZ  
15 1 Y 1 A TYR 177  ? OH  ? A TYR 157 OH  
16 1 Y 1 A GLU 212  ? CG  ? A GLU 192 CG  
17 1 Y 1 A GLU 212  ? CD  ? A GLU 192 CD  
18 1 Y 1 A GLU 212  ? OE1 ? A GLU 192 OE1 
19 1 Y 1 A GLU 212  ? OE2 ? A GLU 192 OE2 
20 1 Y 1 A ARG 220  ? CG  ? A ARG 200 CG  
21 1 Y 1 A ARG 220  ? CD  ? A ARG 200 CD  
22 1 Y 1 A ARG 220  ? NE  ? A ARG 200 NE  
23 1 Y 1 A ARG 220  ? CZ  ? A ARG 200 CZ  
24 1 Y 1 A ARG 220  ? NH1 ? A ARG 200 NH1 
25 1 Y 1 A ARG 220  ? NH2 ? A ARG 200 NH2 
26 1 Y 1 A GLN 1025 ? CG  ? A GLN 261 CG  
27 1 Y 1 A GLN 1025 ? CD  ? A GLN 261 CD  
28 1 Y 1 A GLN 1025 ? OE1 ? A GLN 261 OE1 
29 1 Y 1 A GLN 1025 ? NE2 ? A GLN 261 NE2 
30 1 Y 1 A GLN 1041 ? CG  ? A GLN 277 CG  
31 1 Y 1 A GLN 1041 ? CD  ? A GLN 277 CD  
32 1 Y 1 A GLN 1041 ? OE1 ? A GLN 277 OE1 
33 1 Y 1 A GLN 1041 ? NE2 ? A GLN 277 NE2 
34 1 Y 1 A ASP 1066 ? CG  ? A ASP 302 CG  
35 1 Y 1 A ASP 1066 ? OD1 ? A ASP 302 OD1 
36 1 Y 1 A ASP 1066 ? OD2 ? A ASP 302 OD2 
37 1 Y 1 A GLN 1103 ? CG  ? A GLN 339 CG  
38 1 Y 1 A GLN 1103 ? CD  ? A GLN 339 CD  
39 1 Y 1 A GLN 1103 ? OE1 ? A GLN 339 OE1 
40 1 Y 1 A GLN 1103 ? NE2 ? A GLN 339 NE2 
41 1 Y 1 A TYR 1105 ? CG  ? A TYR 341 CG  
42 1 Y 1 A TYR 1105 ? CD1 ? A TYR 341 CD1 
43 1 Y 1 A TYR 1105 ? CD2 ? A TYR 341 CD2 
44 1 Y 1 A TYR 1105 ? CE1 ? A TYR 341 CE1 
45 1 Y 1 A TYR 1105 ? CE2 ? A TYR 341 CE2 
46 1 Y 1 A TYR 1105 ? CZ  ? A TYR 341 CZ  
47 1 Y 1 A TYR 1105 ? OH  ? A TYR 341 OH  
48 1 Y 1 A ARG 338  ? CG  ? A ARG 412 CG  
49 1 Y 1 A ARG 338  ? CD  ? A ARG 412 CD  
50 1 Y 1 A ARG 338  ? NE  ? A ARG 412 NE  
51 1 Y 1 A ARG 338  ? CZ  ? A ARG 412 CZ  
52 1 Y 1 A ARG 338  ? NH1 ? A ARG 412 NH1 
53 1 Y 1 A ARG 338  ? NH2 ? A ARG 412 NH2 
54 1 Y 1 A LEU 340  ? CG  ? A LEU 414 CG  
55 1 Y 1 A LEU 340  ? CD1 ? A LEU 414 CD1 
56 1 Y 1 A LEU 340  ? CD2 ? A LEU 414 CD2 
57 1 Y 1 A LEU 344  ? CG  ? A LEU 418 CG  
58 1 Y 1 A LEU 344  ? CD1 ? A LEU 418 CD1 
59 1 Y 1 A LEU 344  ? CD2 ? A LEU 418 CD2 
60 1 Y 1 A ASP 345  ? CG  ? A ASP 419 CG  
61 1 Y 1 A ASP 345  ? OD1 ? A ASP 419 OD1 
62 1 Y 1 A ASP 345  ? OD2 ? A ASP 419 OD2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8T1V 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     63.136 
_cell.length_a_esd                 ? 
_cell.length_b                     63.136 
_cell.length_b_esd                 ? 
_cell.length_c                     249.670 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_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                         8T1V 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                154 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 32 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8T1V 
_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             2.89 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          57.43 
_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          'LIPIDIC CUBIC PHASE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'NaCH3COO, PEG 400, NaCl, PPG P40' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     123 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-08-10 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0332 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 23-ID-B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0332 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   23-ID-B 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8T1V 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.60 
_reflns.d_resolution_low                               50.0 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     14570 
_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                           78.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.986 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.147 
_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                                    2.60 
_reflns_shell.d_res_low                                     2.69 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.4 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             467 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.819 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.693 
_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                                 8T1V 
_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                            2.60 
_refine.ls_d_res_low                             41.13 
_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                     13293 
_refine.ls_number_reflns_R_free                  676 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    71.51 
_refine.ls_percent_reflns_R_free                 5.09 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2327 
_refine.ls_R_factor_R_free                       0.2576 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2296 
_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                          49.85 
_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       TWIN_LSQ_F 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 33.88 
_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 
_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                       2.60 
_refine_hist.d_res_low                        41.13 
_refine_hist.number_atoms_solvent             5 
_refine_hist.number_atoms_total               2671 
_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        2635 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         31 
_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' ? 0.002  ? 2727 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.442  ? 3738 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.174 ? 919  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.031  ? 464  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 458  ? 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' 2.60 2.80  . . 48  833  23.00 . . . . 0.3250 . . . . . . . . . . . 0.3181 
'X-RAY DIFFRACTION' 2.81 3.09  . . 70  1478 41.00 . . . . 0.2865 . . . . . . . . . . . 0.2585 
'X-RAY DIFFRACTION' 3.09 3.53  . . 137 3135 85.00 . . . . 0.2526 . . . . . . . . . . . 0.2729 
'X-RAY DIFFRACTION' 3.53 4.45  . . 206 3488 94.00 . . . . 0.2151 . . . . . . . . . . . 0.2324 
'X-RAY DIFFRACTION' 4.45 41.13 . . 202 3696 94.00 . . . . 0.2230 . . . . . . . . . . . 0.2714 
# 
_struct.entry_id                     8T1V 
_struct.title                        'Crystal structure of orphan G protein-coupled receptor 6 with bound inverse agonist 3h' 
_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        8T1V 
_struct_keywords.text            
;Orphan GPCR, GPR6, BRIL, inverse agonist, IAG3h, LCP, APS, membrane protein, Parkinson's Disease
;
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
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 4 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP GPR6_HUMAN P46095 ? 1 
;GGANGSLELSSQLSAGPPGLLLPAVNPWDVLLCVSGTVIAGENALVVALIASTPALRTPMFVLVGSLATADLLAGCGLIL
HFVFQYLVPSETVSLLTVGFLVASFAASVSSLLAITVDRYLSLYNALTYYSRRTLLGVHLLLAATWTVSLGLGLLPVLGW
NCLAERAACSVVRPLARSHVALLSAAFFMVFGIMLHLYVRICQVVWRHA
;
48  
2 UNP C562_ECOLX P0ABE7 ? 1 
;ADLEDNMETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLAN
EGKVKEAQAAAEQLKTTRNAYHQKYR
;
23  
3 UNP GPR6_HUMAN P46095 ? 1 
;HLAATRKGVGTLAVVLGTFGASWLPFAIYCVVGSHEDPAVYTYATLLPATYNSMINPIIYAFRNQEIQRALWLLLCGCFQ
SKVPFRSRSPSEV
;
270 
# 
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 8T1V A 28  ? 236 ? P46095 48  ? 256 ? 48   256  
2 2 8T1V A 237 ? 342 ? P0ABE7 23  ? 128 ? 1001 1106 
3 3 8T1V A 344 ? 436 ? P46095 270 ? 362 ? 270  362  
# 
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 8T1V MET A 1   ? UNP P46095 ?   ?   'initiating methionine' 21   1  
1 8T1V LYS A 2   ? UNP P46095 ?   ?   'expression tag'        22   2  
1 8T1V THR A 3   ? UNP P46095 ?   ?   'expression tag'        23   3  
1 8T1V ILE A 4   ? UNP P46095 ?   ?   'expression tag'        24   4  
1 8T1V ILE A 5   ? UNP P46095 ?   ?   'expression tag'        25   5  
1 8T1V ALA A 6   ? UNP P46095 ?   ?   'expression tag'        26   6  
1 8T1V LEU A 7   ? UNP P46095 ?   ?   'expression tag'        27   7  
1 8T1V SER A 8   ? UNP P46095 ?   ?   'expression tag'        28   8  
1 8T1V TYR A 9   ? UNP P46095 ?   ?   'expression tag'        29   9  
1 8T1V ILE A 10  ? UNP P46095 ?   ?   'expression tag'        30   10 
1 8T1V PHE A 11  ? UNP P46095 ?   ?   'expression tag'        31   11 
1 8T1V CYS A 12  ? UNP P46095 ?   ?   'expression tag'        32   12 
1 8T1V LEU A 13  ? UNP P46095 ?   ?   'expression tag'        33   13 
1 8T1V VAL A 14  ? UNP P46095 ?   ?   'expression tag'        34   14 
1 8T1V PHE A 15  ? UNP P46095 ?   ?   'expression tag'        35   15 
1 8T1V ALA A 16  ? UNP P46095 ?   ?   'expression tag'        36   16 
1 8T1V ASP A 17  ? UNP P46095 ?   ?   'expression tag'        37   17 
1 8T1V TYR A 18  ? UNP P46095 ?   ?   'expression tag'        38   18 
1 8T1V LYS A 19  ? UNP P46095 ?   ?   'expression tag'        39   19 
1 8T1V ASP A 20  ? UNP P46095 ?   ?   'expression tag'        40   20 
1 8T1V ASP A 21  ? UNP P46095 ?   ?   'expression tag'        41   21 
1 8T1V ASP A 22  ? UNP P46095 ?   ?   'expression tag'        42   22 
1 8T1V ASP A 23  ? UNP P46095 ?   ?   'expression tag'        43   23 
1 8T1V ALA A 24  ? UNP P46095 ?   ?   'expression tag'        44   24 
1 8T1V GLY A 25  ? UNP P46095 ?   ?   'expression tag'        45   25 
1 8T1V ARG A 26  ? UNP P46095 ?   ?   'expression tag'        46   26 
1 8T1V ALA A 27  ? UNP P46095 ?   ?   'expression tag'        47   27 
1 8T1V LEU A 103 ? UNP P46095 CYS 123 'engineered mutation'   123  28 
1 8T1V PRO A 153 ? UNP P46095 ALA 173 'engineered mutation'   173  29 
2 8T1V TRP A 243 ? UNP P0ABE7 MET 29  'engineered mutation'   1007 30 
2 8T1V ILE A 338 ? UNP P0ABE7 HIS 124 'engineered mutation'   1102 31 
2 8T1V LEU A 342 ? UNP P0ABE7 ARG 128 'engineered mutation'   1106 32 
2 8T1V ALA A 343 ? UNP P0ABE7 ?   ?   linker                  900  33 
3 8T1V ARG A 353 ? UNP P46095 GLY 279 'engineered mutation'   279  34 
3 8T1V CYS A 365 ? UNP P46095 SER 291 'engineered mutation'   291  35 
3 8T1V LEU A 394 ? UNP P46095 TYR 320 'engineered mutation'   320  36 
3 8T1V ASP A 419 ? UNP P46095 CYS 345 'engineered mutation'   345  37 
3 8T1V GLU A 437 ? UNP P46095 ?   ?   'expression tag'        363  38 
3 8T1V PHE A 438 ? UNP P46095 ?   ?   'expression tag'        364  39 
3 8T1V LEU A 439 ? UNP P46095 ?   ?   'expression tag'        365  40 
3 8T1V GLU A 440 ? UNP P46095 ?   ?   'expression tag'        366  41 
3 8T1V VAL A 441 ? UNP P46095 ?   ?   'expression tag'        367  42 
3 8T1V LEU A 442 ? UNP P46095 ?   ?   'expression tag'        368  43 
3 8T1V PHE A 443 ? UNP P46095 ?   ?   'expression tag'        369  44 
3 8T1V GLN A 444 ? UNP P46095 ?   ?   'expression tag'        370  45 
3 8T1V GLY A 445 ? UNP P46095 ?   ?   'expression tag'        371  46 
3 8T1V PRO A 446 ? UNP P46095 ?   ?   'expression tag'        372  47 
3 8T1V HIS A 447 ? UNP P46095 ?   ?   'expression tag'        373  48 
3 8T1V HIS A 448 ? UNP P46095 ?   ?   'expression tag'        374  49 
3 8T1V HIS A 449 ? UNP P46095 ?   ?   'expression tag'        375  50 
3 8T1V HIS A 450 ? UNP P46095 ?   ?   'expression tag'        376  51 
3 8T1V HIS A 451 ? UNP P46095 ?   ?   'expression tag'        377  52 
3 8T1V HIS A 452 ? UNP P46095 ?   ?   'expression tag'        378  53 
3 8T1V HIS A 453 ? UNP P46095 ?   ?   'expression tag'        379  54 
3 8T1V HIS A 454 ? UNP P46095 ?   ?   'expression tag'        380  55 
3 8T1V HIS A 455 ? UNP P46095 ?   ?   'expression tag'        381  56 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_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 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ALA A 51  ? THR A 80  ? ALA A 71   THR A 100  1 ? 30 
HELX_P HELX_P2  AA2 PRO A 81  ? ARG A 84  ? PRO A 101  ARG A 104  5 ? 4  
HELX_P HELX_P3  AA3 THR A 85  ? TYR A 113 ? THR A 105  TYR A 133  1 ? 29 
HELX_P HELX_P4  AA4 SER A 117 ? ASN A 152 ? SER A 137  ASN A 172  1 ? 36 
HELX_P HELX_P5  AA5 ARG A 159 ? LEU A 182 ? ARG A 179  LEU A 202  1 ? 24 
HELX_P HELX_P6  AA6 PRO A 183 ? GLY A 186 ? PRO A 203  GLY A 206  5 ? 4  
HELX_P HELX_P7  AA7 ALA A 203 ? LYS A 255 ? ALA A 223  LYS A 1019 1 ? 53 
HELX_P HELX_P8  AA8 ASN A 258 ? THR A 280 ? ASN A 1022 THR A 1044 1 ? 23 
HELX_P HELX_P9  AA9 ILE A 303 ? GLU A 317 ? ILE A 1067 GLU A 1081 1 ? 15 
HELX_P HELX_P10 AB1 LYS A 319 ? GLY A 376 ? LYS A 1083 GLY A 302  1 ? 58 
HELX_P HELX_P11 AB2 ALA A 382 ? ASN A 407 ? ALA A 308  ASN A 333  1 ? 26 
HELX_P HELX_P12 AB3 ASN A 407 ? LEU A 417 ? ASN A 333  LEU A 343  1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 189 SG  ? ? ? 1_555 A CYS 196 SG ? ? A CYS 209 A CYS 216  1_555 ? ? ? ? ? ? ? 2.028 ? ? 
metalc1 metalc ? ? A ASP 98  OD1 ? ? ? 1_555 C NA  .   NA ? ? A ASP 118 A NA  1202 1_555 ? ? ? ? ? ? ? 2.886 ? ? 
metalc2 metalc ? ? A ASN 395 OD1 ? ? ? 1_555 C NA  .   NA ? ? A ASN 321 A NA  1202 1_555 ? ? ? ? ? ? ? 2.422 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
_pdbx_struct_conn_angle.id                    1 
_pdbx_struct_conn_angle.ptnr1_label_atom_id   OD1 
_pdbx_struct_conn_angle.ptnr1_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr1_label_asym_id   A 
_pdbx_struct_conn_angle.ptnr1_label_comp_id   ASP 
_pdbx_struct_conn_angle.ptnr1_label_seq_id    98 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id    ASP 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id     118 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr1_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr2_label_atom_id   NA 
_pdbx_struct_conn_angle.ptnr2_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr2_label_asym_id   C 
_pdbx_struct_conn_angle.ptnr2_label_comp_id   NA 
_pdbx_struct_conn_angle.ptnr2_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id    NA 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id     1202 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr2_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr3_label_atom_id   OD1 
_pdbx_struct_conn_angle.ptnr3_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr3_label_asym_id   A 
_pdbx_struct_conn_angle.ptnr3_label_comp_id   ASN 
_pdbx_struct_conn_angle.ptnr3_label_seq_id    395 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id    ASN 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id     321 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr3_symmetry        1_555 
_pdbx_struct_conn_angle.value                 127.5 
_pdbx_struct_conn_angle.value_esd             ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       189 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      196 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        209 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       216 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          ARG 
_struct_mon_prot_cis.label_seq_id           200 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           ARG 
_struct_mon_prot_cis.auth_seq_id            220 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    201 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     221 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -1.04 
# 
_pdbx_entry_details.entry_id                   8T1V 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   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 LEU A 134  ? ? 60.81   65.62 
2 1 ASN A 172  ? ? -159.79 87.13 
3 1 LYS A 1019 ? ? -94.52  58.52 
4 1 GLU A 1081 ? ? -94.68  56.91 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined 16.348 -3.902 -1.875  0.1457 0.4177 0.2820 0.1897  0.0754  -0.0183 1.1868 1.8708 2.6263 0.2449  
0.2605  1.0409  -0.1376 0.2533 0.0958  0.1027  -0.1934 -0.3462 0.2031  0.7442  0.7953 
'X-RAY DIFFRACTION' 2 ? refined 9.710  10.547 -48.707 0.6362 0.8175 0.5382 -0.3486 -0.1041 0.0169  1.3100 0.3772 1.3554 -0.6314 
-1.2571 0.5004  -0.6236 0.2487 -0.0957 -0.2029 0.1320  -0.0192 -0.3910 -0.2196 1.0293 
'X-RAY DIFFRACTION' 3 ? refined 7.684  -9.701 -6.594  0.3477 0.2445 0.2705 0.1776  0.1325  -0.1217 1.9045 2.4947 1.1264 0.2678  
0.2921  -0.1640 -0.0719 0.0573 -0.1210 0.5318  -0.5464 -0.4057 -0.0857 1.2460  0.4647 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1 1 A 68   A 256  '( CHAIN A AND RESID 68:256 )'    ? ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 A 1001 A 1106 '( CHAIN A AND RESID 1001:1106 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 3 3 A 270  A 900  '( CHAIN A AND RESID 270:900 )'   ? ? ? ? ? 
# 
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 21   ? A MET 1   
2   1 Y 1 A LYS 22   ? A LYS 2   
3   1 Y 1 A THR 23   ? A THR 3   
4   1 Y 1 A ILE 24   ? A ILE 4   
5   1 Y 1 A ILE 25   ? A ILE 5   
6   1 Y 1 A ALA 26   ? A ALA 6   
7   1 Y 1 A LEU 27   ? A LEU 7   
8   1 Y 1 A SER 28   ? A SER 8   
9   1 Y 1 A TYR 29   ? A TYR 9   
10  1 Y 1 A ILE 30   ? A ILE 10  
11  1 Y 1 A PHE 31   ? A PHE 11  
12  1 Y 1 A CYS 32   ? A CYS 12  
13  1 Y 1 A LEU 33   ? A LEU 13  
14  1 Y 1 A VAL 34   ? A VAL 14  
15  1 Y 1 A PHE 35   ? A PHE 15  
16  1 Y 1 A ALA 36   ? A ALA 16  
17  1 Y 1 A ASP 37   ? A ASP 17  
18  1 Y 1 A TYR 38   ? A TYR 18  
19  1 Y 1 A LYS 39   ? A LYS 19  
20  1 Y 1 A ASP 40   ? A ASP 20  
21  1 Y 1 A ASP 41   ? A ASP 21  
22  1 Y 1 A ASP 42   ? A ASP 22  
23  1 Y 1 A ASP 43   ? A ASP 23  
24  1 Y 1 A ALA 44   ? A ALA 24  
25  1 Y 1 A GLY 45   ? A GLY 25  
26  1 Y 1 A ARG 46   ? A ARG 26  
27  1 Y 1 A ALA 47   ? A ALA 27  
28  1 Y 1 A GLY 48   ? A GLY 28  
29  1 Y 1 A GLY 49   ? A GLY 29  
30  1 Y 1 A ALA 50   ? A ALA 30  
31  1 Y 1 A ASN 51   ? A ASN 31  
32  1 Y 1 A GLY 52   ? A GLY 32  
33  1 Y 1 A SER 53   ? A SER 33  
34  1 Y 1 A LEU 54   ? A LEU 34  
35  1 Y 1 A GLU 55   ? A GLU 35  
36  1 Y 1 A LEU 56   ? A LEU 36  
37  1 Y 1 A SER 57   ? A SER 37  
38  1 Y 1 A SER 58   ? A SER 38  
39  1 Y 1 A GLN 59   ? A GLN 39  
40  1 Y 1 A LEU 60   ? A LEU 40  
41  1 Y 1 A SER 61   ? A SER 41  
42  1 Y 1 A ALA 62   ? A ALA 42  
43  1 Y 1 A GLY 63   ? A GLY 43  
44  1 Y 1 A PRO 64   ? A PRO 44  
45  1 Y 1 A PRO 65   ? A PRO 45  
46  1 Y 1 A GLY 66   ? A GLY 46  
47  1 Y 1 A LEU 67   ? A LEU 47  
48  1 Y 1 A PRO 1046 ? A PRO 282 
49  1 Y 1 A LYS 1047 ? A LYS 283 
50  1 Y 1 A LEU 1048 ? A LEU 284 
51  1 Y 1 A GLU 1049 ? A GLU 285 
52  1 Y 1 A ASP 1050 ? A ASP 286 
53  1 Y 1 A LYS 1051 ? A LYS 287 
54  1 Y 1 A SER 1052 ? A SER 288 
55  1 Y 1 A PRO 1053 ? A PRO 289 
56  1 Y 1 A ASP 1054 ? A ASP 290 
57  1 Y 1 A SER 1055 ? A SER 291 
58  1 Y 1 A PRO 1056 ? A PRO 292 
59  1 Y 1 A GLU 1057 ? A GLU 293 
60  1 Y 1 A MET 1058 ? A MET 294 
61  1 Y 1 A LYS 1059 ? A LYS 295 
62  1 Y 1 A ASP 1060 ? A ASP 296 
63  1 Y 1 A PHE 1061 ? A PHE 297 
64  1 Y 1 A ARG 1062 ? A ARG 298 
65  1 Y 1 A HIS 1063 ? A HIS 299 
66  1 Y 1 A GLY 1064 ? A GLY 300 
67  1 Y 1 A PHE 1065 ? A PHE 301 
68  1 Y 1 A CYS 347  ? A CYS 421 
69  1 Y 1 A PHE 348  ? A PHE 422 
70  1 Y 1 A GLN 349  ? A GLN 423 
71  1 Y 1 A SER 350  ? A SER 424 
72  1 Y 1 A LYS 351  ? A LYS 425 
73  1 Y 1 A VAL 352  ? A VAL 426 
74  1 Y 1 A PRO 353  ? A PRO 427 
75  1 Y 1 A PHE 354  ? A PHE 428 
76  1 Y 1 A ARG 355  ? A ARG 429 
77  1 Y 1 A SER 356  ? A SER 430 
78  1 Y 1 A ARG 357  ? A ARG 431 
79  1 Y 1 A SER 358  ? A SER 432 
80  1 Y 1 A PRO 359  ? A PRO 433 
81  1 Y 1 A SER 360  ? A SER 434 
82  1 Y 1 A GLU 361  ? A GLU 435 
83  1 Y 1 A VAL 362  ? A VAL 436 
84  1 Y 1 A GLU 363  ? A GLU 437 
85  1 Y 1 A PHE 364  ? A PHE 438 
86  1 Y 1 A LEU 365  ? A LEU 439 
87  1 Y 1 A GLU 366  ? A GLU 440 
88  1 Y 1 A VAL 367  ? A VAL 441 
89  1 Y 1 A LEU 368  ? A LEU 442 
90  1 Y 1 A PHE 369  ? A PHE 443 
91  1 Y 1 A GLN 370  ? A GLN 444 
92  1 Y 1 A GLY 371  ? A GLY 445 
93  1 Y 1 A PRO 372  ? A PRO 446 
94  1 Y 1 A HIS 373  ? A HIS 447 
95  1 Y 1 A HIS 374  ? A HIS 448 
96  1 Y 1 A HIS 375  ? A HIS 449 
97  1 Y 1 A HIS 376  ? A HIS 450 
98  1 Y 1 A HIS 377  ? A HIS 451 
99  1 Y 1 A HIS 378  ? A HIS 452 
100 1 Y 1 A HIS 379  ? A HIS 453 
101 1 Y 1 A HIS 380  ? A HIS 454 
102 1 Y 1 A HIS 381  ? A HIS 455 
# 
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 
HIS N    N  N N 137 
HIS CA   C  N S 138 
HIS C    C  N N 139 
HIS O    O  N N 140 
HIS CB   C  N N 141 
HIS CG   C  Y N 142 
HIS ND1  N  Y N 143 
HIS CD2  C  Y N 144 
HIS CE1  C  Y N 145 
HIS NE2  N  Y N 146 
HIS OXT  O  N N 147 
HIS H    H  N N 148 
HIS H2   H  N N 149 
HIS HA   H  N N 150 
HIS HB2  H  N N 151 
HIS HB3  H  N N 152 
HIS HD1  H  N N 153 
HIS HD2  H  N N 154 
HIS HE1  H  N N 155 
HIS HE2  H  N N 156 
HIS HXT  H  N N 157 
HOH O    O  N N 158 
HOH H1   H  N N 159 
HOH H2   H  N N 160 
ILE N    N  N N 161 
ILE CA   C  N S 162 
ILE C    C  N N 163 
ILE O    O  N N 164 
ILE CB   C  N S 165 
ILE CG1  C  N N 166 
ILE CG2  C  N N 167 
ILE CD1  C  N N 168 
ILE OXT  O  N N 169 
ILE H    H  N N 170 
ILE H2   H  N N 171 
ILE HA   H  N N 172 
ILE HB   H  N N 173 
ILE HG12 H  N N 174 
ILE HG13 H  N N 175 
ILE HG21 H  N N 176 
ILE HG22 H  N N 177 
ILE HG23 H  N N 178 
ILE HD11 H  N N 179 
ILE HD12 H  N N 180 
ILE HD13 H  N N 181 
ILE HXT  H  N N 182 
LEU N    N  N N 183 
LEU CA   C  N S 184 
LEU C    C  N N 185 
LEU O    O  N N 186 
LEU CB   C  N N 187 
LEU CG   C  N N 188 
LEU CD1  C  N N 189 
LEU CD2  C  N N 190 
LEU OXT  O  N N 191 
LEU H    H  N N 192 
LEU H2   H  N N 193 
LEU HA   H  N N 194 
LEU HB2  H  N N 195 
LEU HB3  H  N N 196 
LEU HG   H  N N 197 
LEU HD11 H  N N 198 
LEU HD12 H  N N 199 
LEU HD13 H  N N 200 
LEU HD21 H  N N 201 
LEU HD22 H  N N 202 
LEU HD23 H  N N 203 
LEU HXT  H  N N 204 
LYS N    N  N N 205 
LYS CA   C  N S 206 
LYS C    C  N N 207 
LYS O    O  N N 208 
LYS CB   C  N N 209 
LYS CG   C  N N 210 
LYS CD   C  N N 211 
LYS CE   C  N N 212 
LYS NZ   N  N N 213 
LYS OXT  O  N N 214 
LYS H    H  N N 215 
LYS H2   H  N N 216 
LYS HA   H  N N 217 
LYS HB2  H  N N 218 
LYS HB3  H  N N 219 
LYS HG2  H  N N 220 
LYS HG3  H  N N 221 
LYS HD2  H  N N 222 
LYS HD3  H  N N 223 
LYS HE2  H  N N 224 
LYS HE3  H  N N 225 
LYS HZ1  H  N N 226 
LYS HZ2  H  N N 227 
LYS HZ3  H  N N 228 
LYS HXT  H  N N 229 
MET N    N  N N 230 
MET CA   C  N S 231 
MET C    C  N N 232 
MET O    O  N N 233 
MET CB   C  N N 234 
MET CG   C  N N 235 
MET SD   S  N N 236 
MET CE   C  N N 237 
MET OXT  O  N N 238 
MET H    H  N N 239 
MET H2   H  N N 240 
MET HA   H  N N 241 
MET HB2  H  N N 242 
MET HB3  H  N N 243 
MET HG2  H  N N 244 
MET HG3  H  N N 245 
MET HE1  H  N N 246 
MET HE2  H  N N 247 
MET HE3  H  N N 248 
MET HXT  H  N N 249 
NA  NA   NA N N 250 
PHE N    N  N N 251 
PHE CA   C  N S 252 
PHE C    C  N N 253 
PHE O    O  N N 254 
PHE CB   C  N N 255 
PHE CG   C  Y N 256 
PHE CD1  C  Y N 257 
PHE CD2  C  Y N 258 
PHE CE1  C  Y N 259 
PHE CE2  C  Y N 260 
PHE CZ   C  Y N 261 
PHE OXT  O  N N 262 
PHE H    H  N N 263 
PHE H2   H  N N 264 
PHE HA   H  N N 265 
PHE HB2  H  N N 266 
PHE HB3  H  N N 267 
PHE HD1  H  N N 268 
PHE HD2  H  N N 269 
PHE HE1  H  N N 270 
PHE HE2  H  N N 271 
PHE HZ   H  N N 272 
PHE HXT  H  N N 273 
PRO N    N  N N 274 
PRO CA   C  N S 275 
PRO C    C  N N 276 
PRO O    O  N N 277 
PRO CB   C  N N 278 
PRO CG   C  N N 279 
PRO CD   C  N N 280 
PRO OXT  O  N N 281 
PRO H    H  N N 282 
PRO HA   H  N N 283 
PRO HB2  H  N N 284 
PRO HB3  H  N N 285 
PRO HG2  H  N N 286 
PRO HG3  H  N N 287 
PRO HD2  H  N N 288 
PRO HD3  H  N N 289 
PRO HXT  H  N N 290 
SER N    N  N N 291 
SER CA   C  N S 292 
SER C    C  N N 293 
SER O    O  N N 294 
SER CB   C  N N 295 
SER OG   O  N N 296 
SER OXT  O  N N 297 
SER H    H  N N 298 
SER H2   H  N N 299 
SER HA   H  N N 300 
SER HB2  H  N N 301 
SER HB3  H  N N 302 
SER HG   H  N N 303 
SER HXT  H  N N 304 
THR N    N  N N 305 
THR CA   C  N S 306 
THR C    C  N N 307 
THR O    O  N N 308 
THR CB   C  N R 309 
THR OG1  O  N N 310 
THR CG2  C  N N 311 
THR OXT  O  N N 312 
THR H    H  N N 313 
THR H2   H  N N 314 
THR HA   H  N N 315 
THR HB   H  N N 316 
THR HG1  H  N N 317 
THR HG21 H  N N 318 
THR HG22 H  N N 319 
THR HG23 H  N N 320 
THR HXT  H  N N 321 
TRP N    N  N N 322 
TRP CA   C  N S 323 
TRP C    C  N N 324 
TRP O    O  N N 325 
TRP CB   C  N N 326 
TRP CG   C  Y N 327 
TRP CD1  C  Y N 328 
TRP CD2  C  Y N 329 
TRP NE1  N  Y N 330 
TRP CE2  C  Y N 331 
TRP CE3  C  Y N 332 
TRP CZ2  C  Y N 333 
TRP CZ3  C  Y N 334 
TRP CH2  C  Y N 335 
TRP OXT  O  N N 336 
TRP H    H  N N 337 
TRP H2   H  N N 338 
TRP HA   H  N N 339 
TRP HB2  H  N N 340 
TRP HB3  H  N N 341 
TRP HD1  H  N N 342 
TRP HE1  H  N N 343 
TRP HE3  H  N N 344 
TRP HZ2  H  N N 345 
TRP HZ3  H  N N 346 
TRP HH2  H  N N 347 
TRP HXT  H  N N 348 
TYR N    N  N N 349 
TYR CA   C  N S 350 
TYR C    C  N N 351 
TYR O    O  N N 352 
TYR CB   C  N N 353 
TYR CG   C  Y N 354 
TYR CD1  C  Y N 355 
TYR CD2  C  Y N 356 
TYR CE1  C  Y N 357 
TYR CE2  C  Y N 358 
TYR CZ   C  Y N 359 
TYR OH   O  N N 360 
TYR OXT  O  N N 361 
TYR H    H  N N 362 
TYR H2   H  N N 363 
TYR HA   H  N N 364 
TYR HB2  H  N N 365 
TYR HB3  H  N N 366 
TYR HD1  H  N N 367 
TYR HD2  H  N N 368 
TYR HE1  H  N N 369 
TYR HE2  H  N N 370 
TYR HH   H  N N 371 
TYR HXT  H  N N 372 
VAL N    N  N N 373 
VAL CA   C  N S 374 
VAL C    C  N N 375 
VAL O    O  N N 376 
VAL CB   C  N N 377 
VAL CG1  C  N N 378 
VAL CG2  C  N N 379 
VAL OXT  O  N N 380 
VAL H    H  N N 381 
VAL H2   H  N N 382 
VAL HA   H  N N 383 
VAL HB   H  N N 384 
VAL HG11 H  N N 385 
VAL HG12 H  N N 386 
VAL HG13 H  N N 387 
VAL HG21 H  N N 388 
VAL HG22 H  N N 389 
VAL HG23 H  N N 390 
VAL HXT  H  N N 391 
XY8 C01  C  N N 392 
XY8 C02  C  N N 393 
XY8 C03  C  N N 394 
XY8 C05  C  Y N 395 
XY8 C07  C  Y N 396 
XY8 C08  C  Y N 397 
XY8 C09  C  Y N 398 
XY8 C11  C  Y N 399 
XY8 C12  C  N N 400 
XY8 C13  C  Y N 401 
XY8 C15  C  Y N 402 
XY8 C17  C  N N 403 
XY8 C18  C  N N 404 
XY8 C20  C  N N 405 
XY8 C21  C  Y N 406 
XY8 C22  C  Y N 407 
XY8 C24  C  Y N 408 
XY8 C25  C  Y N 409 
XY8 C27  C  Y N 410 
XY8 C28  C  Y N 411 
XY8 C29  C  N N 412 
XY8 C30  C  N N 413 
XY8 F23  F  N N 414 
XY8 F26  F  N N 415 
XY8 N04  N  N N 416 
XY8 N06  N  Y N 417 
XY8 N10  N  Y N 418 
XY8 N14  N  Y N 419 
XY8 N16  N  N N 420 
XY8 N19  N  N N 421 
XY8 H1   H  N N 422 
XY8 H2   H  N N 423 
XY8 H3   H  N N 424 
XY8 H4   H  N N 425 
XY8 H5   H  N N 426 
XY8 H6   H  N N 427 
XY8 H7   H  N N 428 
XY8 H8   H  N N 429 
XY8 H9   H  N N 430 
XY8 H10  H  N N 431 
XY8 H11  H  N N 432 
XY8 H12  H  N N 433 
XY8 H13  H  N N 434 
XY8 H14  H  N N 435 
XY8 H15  H  N N 436 
XY8 H16  H  N N 437 
XY8 H17  H  N N 438 
XY8 H18  H  N N 439 
XY8 H19  H  N N 440 
XY8 H20  H  N N 441 
XY8 H21  H  N N 442 
XY8 H22  H  N N 443 
XY8 H23  H  N N 444 
XY8 H24  H  N N 445 
XY8 H25  H  N N 446 
XY8 H26  H  N N 447 
# 
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 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
XY8 C01 C02  sing N N 376 
XY8 C03 C02  sing N N 377 
XY8 C02 N04  sing N N 378 
XY8 C27 C28  doub Y N 379 
XY8 C27 C25  sing Y N 380 
XY8 C28 C21  sing Y N 381 
XY8 N04 C05  sing N N 382 
XY8 F26 C25  sing N N 383 
XY8 C25 C24  doub Y N 384 
XY8 C29 C30  sing N N 385 
XY8 C29 N19  sing N N 386 
XY8 C21 C20  sing N N 387 
XY8 C21 C22  doub Y N 388 
XY8 C20 N19  sing N N 389 
XY8 C30 N16  sing N N 390 
XY8 C05 N06  doub Y N 391 
XY8 C05 C15  sing Y N 392 
XY8 C24 C22  sing Y N 393 
XY8 N19 C18  sing N N 394 
XY8 N06 C07  sing Y N 395 
XY8 C22 F23  sing N N 396 
XY8 N16 C15  sing N N 397 
XY8 N16 C17  sing N N 398 
XY8 C18 C17  sing N N 399 
XY8 C15 N14  doub Y N 400 
XY8 C07 C13  doub Y N 401 
XY8 C07 C08  sing Y N 402 
XY8 C13 C11  sing Y N 403 
XY8 N14 C08  sing Y N 404 
XY8 C08 C09  doub Y N 405 
XY8 C11 C12  sing N N 406 
XY8 C11 N10  doub Y N 407 
XY8 C09 N10  sing Y N 408 
XY8 C01 H1   sing N N 409 
XY8 C01 H2   sing N N 410 
XY8 C01 H3   sing N N 411 
XY8 C02 H4   sing N N 412 
XY8 C03 H5   sing N N 413 
XY8 C03 H6   sing N N 414 
XY8 C03 H7   sing N N 415 
XY8 C09 H8   sing N N 416 
XY8 C12 H9   sing N N 417 
XY8 C12 H10  sing N N 418 
XY8 C12 H11  sing N N 419 
XY8 C13 H12  sing N N 420 
XY8 C17 H13  sing N N 421 
XY8 C17 H14  sing N N 422 
XY8 C18 H15  sing N N 423 
XY8 C18 H16  sing N N 424 
XY8 C20 H17  sing N N 425 
XY8 C20 H18  sing N N 426 
XY8 C24 H19  sing N N 427 
XY8 C27 H20  sing N N 428 
XY8 C28 H21  sing N N 429 
XY8 C29 H22  sing N N 430 
XY8 C29 H23  sing N N 431 
XY8 C30 H24  sing N N 432 
XY8 C30 H25  sing N N 433 
XY8 N04 H26  sing N N 434 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           'R35 GM127086' 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_initial_refinement_model.id 
_pdbx_initial_refinement_model.entity_id_list 
_pdbx_initial_refinement_model.type 
_pdbx_initial_refinement_model.source_name 
_pdbx_initial_refinement_model.accession_code 
_pdbx_initial_refinement_model.details 
1 ? 'experimental model' PDB 4Z35 'all residues replaced with alanines and loops omitted' 
2 ? 'experimental model' PDB 1M6T BRIL                                                    
# 
_atom_sites.entry_id                    8T1V 
_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.fract_transf_matrix[1][1]   0.015839 
_atom_sites.fract_transf_matrix[1][2]   0.009145 
_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]   0.018289 
_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]   0.004005 
_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  
F  
N  
NA 
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . LEU A 1 48  ? -2.585 -21.957 10.059  1.00 92.64  ? 68   LEU A N   1 
ATOM   2    C  CA  . LEU A 1 48  ? -1.329 -21.784 10.778  1.00 93.37  ? 68   LEU A CA  1 
ATOM   3    C  C   . LEU A 1 48  ? -1.416 -20.639 11.784  1.00 97.27  ? 68   LEU A C   1 
ATOM   4    O  O   . LEU A 1 48  ? -0.399 -20.063 12.169  1.00 96.04  ? 68   LEU A O   1 
ATOM   5    C  CB  . LEU A 1 48  ? -0.182 -21.529 9.795   1.00 96.73  ? 68   LEU A CB  1 
ATOM   6    C  CG  . LEU A 1 48  ? 0.314  -22.731 8.989   1.00 101.84 ? 68   LEU A CG  1 
ATOM   7    C  CD1 . LEU A 1 48  ? 1.356  -22.293 7.969   1.00 98.27  ? 68   LEU A CD1 1 
ATOM   8    C  CD2 . LEU A 1 48  ? 0.884  -23.800 9.911   1.00 99.47  ? 68   LEU A CD2 1 
ATOM   9    N  N   . LEU A 1 49  ? -2.635 -20.306 12.207  1.00 99.75  ? 69   LEU A N   1 
ATOM   10   C  CA  . LEU A 1 49  ? -2.798 -19.233 13.186  1.00 89.23  ? 69   LEU A CA  1 
ATOM   11   C  C   . LEU A 1 49  ? -2.088 -19.540 14.496  1.00 101.72 ? 69   LEU A C   1 
ATOM   12   O  O   . LEU A 1 49  ? -1.309 -18.692 14.965  1.00 100.81 ? 69   LEU A O   1 
ATOM   13   C  CB  . LEU A 1 49  ? -4.290 -18.969 13.411  1.00 87.28  ? 69   LEU A CB  1 
ATOM   14   N  N   . PRO A 1 50  ? -2.290 -20.695 15.128  1.00 101.32 ? 70   PRO A N   1 
ATOM   15   C  CA  . PRO A 1 50  ? -1.549 -21.028 16.355  1.00 101.59 ? 70   PRO A CA  1 
ATOM   16   C  C   . PRO A 1 50  ? -0.212 -21.721 16.131  1.00 105.00 ? 70   PRO A C   1 
ATOM   17   O  O   . PRO A 1 50  ? 0.390  -22.176 17.109  1.00 99.73  ? 70   PRO A O   1 
ATOM   18   C  CB  . PRO A 1 50  ? -2.523 -21.973 17.071  1.00 98.25  ? 70   PRO A CB  1 
ATOM   19   C  CG  . PRO A 1 50  ? -3.203 -22.693 15.959  1.00 93.81  ? 70   PRO A CG  1 
ATOM   20   C  CD  . PRO A 1 50  ? -3.331 -21.697 14.829  1.00 96.03  ? 70   PRO A CD  1 
ATOM   21   N  N   . ALA A 1 51  ? 0.259  -21.813 14.891  1.00 108.16 ? 71   ALA A N   1 
ATOM   22   C  CA  . ALA A 1 51  ? 1.477  -22.540 14.539  1.00 105.87 ? 71   ALA A CA  1 
ATOM   23   C  C   . ALA A 1 51  ? 2.570  -21.526 14.204  1.00 105.27 ? 71   ALA A C   1 
ATOM   24   O  O   . ALA A 1 51  ? 2.725  -21.115 13.053  1.00 108.03 ? 71   ALA A O   1 
ATOM   25   C  CB  . ALA A 1 51  ? 1.209  -23.489 13.373  1.00 95.97  ? 71   ALA A CB  1 
ATOM   26   N  N   . VAL A 1 52  ? 3.347  -21.141 15.218  1.00 104.10 ? 72   VAL A N   1 
ATOM   27   C  CA  . VAL A 1 52  ? 4.380  -20.126 15.028  1.00 97.92  ? 72   VAL A CA  1 
ATOM   28   C  C   . VAL A 1 52  ? 5.632  -20.735 14.407  1.00 98.02  ? 72   VAL A C   1 
ATOM   29   O  O   . VAL A 1 52  ? 6.152  -20.230 13.406  1.00 104.87 ? 72   VAL A O   1 
ATOM   30   C  CB  . VAL A 1 52  ? 4.699  -19.435 16.365  1.00 91.15  ? 72   VAL A CB  1 
ATOM   31   C  CG1 . VAL A 1 52  ? 5.809  -18.411 16.184  1.00 84.93  ? 72   VAL A CG1 1 
ATOM   32   C  CG2 . VAL A 1 52  ? 3.452  -18.783 16.940  1.00 89.78  ? 72   VAL A CG2 1 
ATOM   33   N  N   . ASN A 1 53  ? 6.151  -21.811 14.997  1.00 104.99 ? 73   ASN A N   1 
ATOM   34   C  CA  . ASN A 1 53  ? 7.313  -22.464 14.402  1.00 98.34  ? 73   ASN A CA  1 
ATOM   35   C  C   . ASN A 1 53  ? 7.018  -22.974 12.998  1.00 102.01 ? 73   ASN A C   1 
ATOM   36   O  O   . ASN A 1 53  ? 7.857  -22.758 12.105  1.00 101.55 ? 73   ASN A O   1 
ATOM   37   C  CB  . ASN A 1 53  ? 7.807  -23.596 15.314  1.00 86.40  ? 73   ASN A CB  1 
ATOM   38   C  CG  . ASN A 1 53  ? 9.127  -24.185 14.852  1.00 70.44  ? 73   ASN A CG  1 
ATOM   39   O  OD1 . ASN A 1 53  ? 9.572  -23.944 13.731  1.00 85.42  ? 73   ASN A OD1 1 
ATOM   40   N  ND2 . ASN A 1 53  ? 9.758  -24.969 15.718  1.00 64.00  ? 73   ASN A ND2 1 
ATOM   41   N  N   . PRO A 1 54  ? 5.887  -23.629 12.723  1.00 88.02  ? 74   PRO A N   1 
ATOM   42   C  CA  . PRO A 1 54  ? 5.580  -23.978 11.328  1.00 86.14  ? 74   PRO A CA  1 
ATOM   43   C  C   . PRO A 1 54  ? 5.511  -22.772 10.408  1.00 86.35  ? 74   PRO A C   1 
ATOM   44   O  O   . PRO A 1 54  ? 5.781  -22.906 9.208   1.00 88.06  ? 74   PRO A O   1 
ATOM   45   C  CB  . PRO A 1 54  ? 4.229  -24.695 11.439  1.00 93.98  ? 74   PRO A CB  1 
ATOM   46   C  CG  . PRO A 1 54  ? 4.246  -25.281 12.807  1.00 93.13  ? 74   PRO A CG  1 
ATOM   47   C  CD  . PRO A 1 54  ? 4.919  -24.238 13.654  1.00 92.37  ? 74   PRO A CD  1 
ATOM   48   N  N   . TRP A 1 55  ? 5.148  -21.595 10.923  1.00 87.48  ? 75   TRP A N   1 
ATOM   49   C  CA  . TRP A 1 55  ? 5.325  -20.383 10.130  1.00 84.20  ? 75   TRP A CA  1 
ATOM   50   C  C   . TRP A 1 55  ? 6.798  -20.165 9.819   1.00 86.00  ? 75   TRP A C   1 
ATOM   51   O  O   . TRP A 1 55  ? 7.158  -19.800 8.693   1.00 86.44  ? 75   TRP A O   1 
ATOM   52   C  CB  . TRP A 1 55  ? 4.752  -19.167 10.862  1.00 80.52  ? 75   TRP A CB  1 
ATOM   53   C  CG  . TRP A 1 55  ? 3.305  -18.884 10.576  1.00 82.03  ? 75   TRP A CG  1 
ATOM   54   C  CD1 . TRP A 1 55  ? 2.294  -18.793 11.487  1.00 83.62  ? 75   TRP A CD1 1 
ATOM   55   C  CD2 . TRP A 1 55  ? 2.710  -18.644 9.294   1.00 84.22  ? 75   TRP A CD2 1 
ATOM   56   N  NE1 . TRP A 1 55  ? 1.107  -18.516 10.855  1.00 90.06  ? 75   TRP A NE1 1 
ATOM   57   C  CE2 . TRP A 1 55  ? 1.335  -18.419 9.507   1.00 86.34  ? 75   TRP A CE2 1 
ATOM   58   C  CE3 . TRP A 1 55  ? 3.205  -18.599 7.987   1.00 86.94  ? 75   TRP A CE3 1 
ATOM   59   C  CZ2 . TRP A 1 55  ? 0.450  -18.155 8.464   1.00 84.16  ? 75   TRP A CZ2 1 
ATOM   60   C  CZ3 . TRP A 1 55  ? 2.325  -18.337 6.953   1.00 84.90  ? 75   TRP A CZ3 1 
ATOM   61   C  CH2 . TRP A 1 55  ? 0.963  -18.118 7.198   1.00 83.02  ? 75   TRP A CH2 1 
ATOM   62   N  N   . ASP A 1 56  ? 7.668  -20.397 10.805  1.00 83.45  ? 76   ASP A N   1 
ATOM   63   C  CA  . ASP A 1 56  ? 9.099  -20.204 10.594  1.00 86.82  ? 76   ASP A CA  1 
ATOM   64   C  C   . ASP A 1 56  ? 9.661  -21.238 9.628   1.00 94.10  ? 76   ASP A C   1 
ATOM   65   O  O   . ASP A 1 56  ? 10.352 -20.888 8.665   1.00 95.19  ? 76   ASP A O   1 
ATOM   66   C  CB  . ASP A 1 56  ? 9.837  -20.264 11.930  1.00 85.45  ? 76   ASP A CB  1 
ATOM   67   C  CG  . ASP A 1 56  ? 9.551  -19.065 12.806  1.00 87.52  ? 76   ASP A CG  1 
ATOM   68   O  OD1 . ASP A 1 56  ? 8.398  -18.921 13.260  1.00 95.37  ? 76   ASP A OD1 1 
ATOM   69   O  OD2 . ASP A 1 56  ? 10.481 -18.263 13.036  1.00 92.02  ? 76   ASP A OD2 1 
ATOM   70   N  N   . VAL A 1 57  ? 9.363  -22.520 9.853   1.00 84.08  ? 77   VAL A N   1 
ATOM   71   C  CA  . VAL A 1 57  ? 9.936  -23.551 8.991   1.00 75.32  ? 77   VAL A CA  1 
ATOM   72   C  C   . VAL A 1 57  ? 9.581  -23.275 7.540   1.00 73.63  ? 77   VAL A C   1 
ATOM   73   O  O   . VAL A 1 57  ? 10.374 -23.551 6.632   1.00 78.98  ? 77   VAL A O   1 
ATOM   74   C  CB  . VAL A 1 57  ? 9.473  -24.957 9.425   1.00 77.84  ? 77   VAL A CB  1 
ATOM   75   C  CG1 . VAL A 1 57  ? 9.693  -25.159 10.919  1.00 79.92  ? 77   VAL A CG1 1 
ATOM   76   C  CG2 . VAL A 1 57  ? 8.021  -25.183 9.050   1.00 71.03  ? 77   VAL A CG2 1 
ATOM   77   N  N   . LEU A 1 58  ? 8.399  -22.707 7.296   1.00 72.18  ? 78   LEU A N   1 
ATOM   78   C  CA  . LEU A 1 58  ? 8.047  -22.308 5.940   1.00 71.63  ? 78   LEU A CA  1 
ATOM   79   C  C   . LEU A 1 58  ? 9.037  -21.281 5.408   1.00 74.13  ? 78   LEU A C   1 
ATOM   80   O  O   . LEU A 1 58  ? 9.507  -21.392 4.269   1.00 81.26  ? 78   LEU A O   1 
ATOM   81   C  CB  . LEU A 1 58  ? 6.622  -21.755 5.916   1.00 68.84  ? 78   LEU A CB  1 
ATOM   82   C  CG  . LEU A 1 58  ? 5.858  -21.901 4.598   1.00 74.27  ? 78   LEU A CG  1 
ATOM   83   C  CD1 . LEU A 1 58  ? 4.394  -21.537 4.793   1.00 74.78  ? 78   LEU A CD1 1 
ATOM   84   C  CD2 . LEU A 1 58  ? 6.483  -21.051 3.504   1.00 72.74  ? 78   LEU A CD2 1 
ATOM   85   N  N   . LEU A 1 59  ? 9.380  -20.280 6.221   1.00 76.81  ? 79   LEU A N   1 
ATOM   86   C  CA  . LEU A 1 59  ? 10.352 -19.284 5.788   1.00 69.76  ? 79   LEU A CA  1 
ATOM   87   C  C   . LEU A 1 59  ? 11.783 -19.794 5.913   1.00 73.05  ? 79   LEU A C   1 
ATOM   88   O  O   . LEU A 1 59  ? 12.649 -19.380 5.134   1.00 67.28  ? 79   LEU A O   1 
ATOM   89   C  CB  . LEU A 1 59  ? 10.173 -17.987 6.585   1.00 68.85  ? 79   LEU A CB  1 
ATOM   90   C  CG  . LEU A 1 59  ? 10.838 -17.862 7.960   1.00 72.96  ? 79   LEU A CG  1 
ATOM   91   C  CD1 . LEU A 1 59  ? 12.267 -17.346 7.855   1.00 74.61  ? 79   LEU A CD1 1 
ATOM   92   C  CD2 . LEU A 1 59  ? 10.015 -16.966 8.869   1.00 83.38  ? 79   LEU A CD2 1 
ATOM   93   N  N   . CYS A 1 60  ? 12.047 -20.692 6.866   1.00 86.30  ? 80   CYS A N   1 
ATOM   94   C  CA  . CYS A 1 60  ? 13.414 -21.150 7.091   1.00 73.96  ? 80   CYS A CA  1 
ATOM   95   C  C   . CYS A 1 60  ? 14.013 -21.725 5.817   1.00 81.52  ? 80   CYS A C   1 
ATOM   96   O  O   . CYS A 1 60  ? 15.096 -21.315 5.385   1.00 82.91  ? 80   CYS A O   1 
ATOM   97   C  CB  . CYS A 1 60  ? 13.444 -22.195 8.206   1.00 74.47  ? 80   CYS A CB  1 
ATOM   98   S  SG  . CYS A 1 60  ? 12.909 -21.587 9.816   1.00 75.10  ? 80   CYS A SG  1 
ATOM   99   N  N   . VAL A 1 61  ? 13.313 -22.671 5.194   1.00 66.10  ? 81   VAL A N   1 
ATOM   100  C  CA  . VAL A 1 61  ? 13.824 -23.258 3.961   1.00 66.30  ? 81   VAL A CA  1 
ATOM   101  C  C   . VAL A 1 61  ? 13.547 -22.348 2.769   1.00 67.53  ? 81   VAL A C   1 
ATOM   102  O  O   . VAL A 1 61  ? 14.272 -22.395 1.769   1.00 68.41  ? 81   VAL A O   1 
ATOM   103  C  CB  . VAL A 1 61  ? 13.233 -24.663 3.749   1.00 59.70  ? 81   VAL A CB  1 
ATOM   104  C  CG1 . VAL A 1 61  ? 13.825 -25.636 4.754   1.00 56.94  ? 81   VAL A CG1 1 
ATOM   105  C  CG2 . VAL A 1 61  ? 11.716 -24.641 3.864   1.00 72.09  ? 81   VAL A CG2 1 
ATOM   106  N  N   . SER A 1 62  ? 12.515 -21.504 2.849   1.00 70.95  ? 82   SER A N   1 
ATOM   107  C  CA  . SER A 1 62  ? 12.260 -20.560 1.766   1.00 72.96  ? 82   SER A CA  1 
ATOM   108  C  C   . SER A 1 62  ? 13.428 -19.604 1.580   1.00 68.37  ? 82   SER A C   1 
ATOM   109  O  O   . SER A 1 62  ? 13.680 -19.139 0.463   1.00 66.38  ? 82   SER A O   1 
ATOM   110  C  CB  . SER A 1 62  ? 10.977 -19.775 2.037   1.00 73.71  ? 82   SER A CB  1 
ATOM   111  O  OG  . SER A 1 62  ? 9.858  -20.639 2.132   1.00 80.18  ? 82   SER A OG  1 
ATOM   112  N  N   . GLY A 1 63  ? 14.146 -19.291 2.660   1.00 72.36  ? 83   GLY A N   1 
ATOM   113  C  CA  . GLY A 1 63  ? 15.342 -18.479 2.523   1.00 72.82  ? 83   GLY A CA  1 
ATOM   114  C  C   . GLY A 1 63  ? 16.405 -19.160 1.685   1.00 75.37  ? 83   GLY A C   1 
ATOM   115  O  O   . GLY A 1 63  ? 17.103 -18.513 0.901   1.00 75.69  ? 83   GLY A O   1 
ATOM   116  N  N   . THR A 1 64  ? 16.544 -20.479 1.841   1.00 68.48  ? 84   THR A N   1 
ATOM   117  C  CA  . THR A 1 64  ? 17.482 -21.219 1.004   1.00 74.05  ? 84   THR A CA  1 
ATOM   118  C  C   . THR A 1 64  ? 17.104 -21.101 -0.466  1.00 68.30  ? 84   THR A C   1 
ATOM   119  O  O   . THR A 1 64  ? 17.969 -20.891 -1.324  1.00 69.46  ? 84   THR A O   1 
ATOM   120  C  CB  . THR A 1 64  ? 17.522 -22.688 1.430   1.00 74.98  ? 84   THR A CB  1 
ATOM   121  O  OG1 . THR A 1 64  ? 17.910 -22.781 2.807   1.00 79.65  ? 84   THR A OG1 1 
ATOM   122  C  CG2 . THR A 1 64  ? 18.510 -23.472 0.574   1.00 73.23  ? 84   THR A CG2 1 
ATOM   123  N  N   . VAL A 1 65  ? 15.812 -21.221 -0.775  1.00 86.65  ? 85   VAL A N   1 
ATOM   124  C  CA  . VAL A 1 65  ? 15.363 -21.058 -2.154  1.00 83.01  ? 85   VAL A CA  1 
ATOM   125  C  C   . VAL A 1 65  ? 15.704 -19.662 -2.654  1.00 90.18  ? 85   VAL A C   1 
ATOM   126  O  O   . VAL A 1 65  ? 16.348 -19.493 -3.696  1.00 89.99  ? 85   VAL A O   1 
ATOM   127  C  CB  . VAL A 1 65  ? 13.853 -21.334 -2.261  1.00 78.99  ? 85   VAL A CB  1 
ATOM   128  C  CG1 . VAL A 1 65  ? 13.346 -20.985 -3.653  1.00 61.75  ? 85   VAL A CG1 1 
ATOM   129  C  CG2 . VAL A 1 65  ? 13.556 -22.780 -1.924  1.00 80.91  ? 85   VAL A CG2 1 
ATOM   130  N  N   . ILE A 1 66  ? 15.309 -18.640 -1.894  1.00 79.23  ? 86   ILE A N   1 
ATOM   131  C  CA  . ILE A 1 66  ? 15.541 -17.265 -2.323  1.00 79.88  ? 86   ILE A CA  1 
ATOM   132  C  C   . ILE A 1 66  ? 17.031 -17.000 -2.465  1.00 83.68  ? 86   ILE A C   1 
ATOM   133  O  O   . ILE A 1 66  ? 17.476 -16.362 -3.427  1.00 84.54  ? 86   ILE A O   1 
ATOM   134  C  CB  . ILE A 1 66  ? 14.883 -16.286 -1.337  1.00 70.60  ? 86   ILE A CB  1 
ATOM   135  C  CG1 . ILE A 1 66  ? 13.365 -16.465 -1.373  1.00 79.79  ? 86   ILE A CG1 1 
ATOM   136  C  CG2 . ILE A 1 66  ? 15.280 -14.855 -1.672  1.00 68.99  ? 86   ILE A CG2 1 
ATOM   137  C  CD1 . ILE A 1 66  ? 12.634 -15.720 -0.286  1.00 75.58  ? 86   ILE A CD1 1 
ATOM   138  N  N   . ALA A 1 67  ? 17.826 -17.474 -1.506  1.00 84.62  ? 87   ALA A N   1 
ATOM   139  C  CA  . ALA A 1 67  ? 19.270 -17.326 -1.617  1.00 76.49  ? 87   ALA A CA  1 
ATOM   140  C  C   . ALA A 1 67  ? 19.802 -18.069 -2.834  1.00 73.11  ? 87   ALA A C   1 
ATOM   141  O  O   . ALA A 1 67  ? 20.652 -17.551 -3.567  1.00 64.46  ? 87   ALA A O   1 
ATOM   142  C  CB  . ALA A 1 67  ? 19.945 -17.830 -0.343  1.00 72.02  ? 87   ALA A CB  1 
ATOM   143  N  N   . GLY A 1 68  ? 19.300 -19.281 -3.075  1.00 71.87  ? 88   GLY A N   1 
ATOM   144  C  CA  . GLY A 1 68  ? 19.814 -20.072 -4.180  1.00 81.65  ? 88   GLY A CA  1 
ATOM   145  C  C   . GLY A 1 68  ? 19.464 -19.482 -5.533  1.00 75.33  ? 88   GLY A C   1 
ATOM   146  O  O   . GLY A 1 68  ? 20.343 -19.245 -6.367  1.00 79.98  ? 88   GLY A O   1 
ATOM   147  N  N   . GLU A 1 69  ? 18.176 -19.224 -5.767  1.00 70.17  ? 89   GLU A N   1 
ATOM   148  C  CA  . GLU A 1 69  ? 17.757 -18.763 -7.087  1.00 66.86  ? 89   GLU A CA  1 
ATOM   149  C  C   . GLU A 1 69  ? 18.396 -17.423 -7.426  1.00 63.10  ? 89   GLU A C   1 
ATOM   150  O  O   . GLU A 1 69  ? 18.894 -17.229 -8.542  1.00 63.11  ? 89   GLU A O   1 
ATOM   151  C  CB  . GLU A 1 69  ? 16.231 -18.667 -7.155  1.00 64.74  ? 89   GLU A CB  1 
ATOM   152  C  CG  . GLU A 1 69  ? 15.487 -19.904 -6.646  1.00 75.38  ? 89   GLU A CG  1 
ATOM   153  C  CD  . GLU A 1 69  ? 16.207 -21.210 -6.948  1.00 79.72  ? 89   GLU A CD  1 
ATOM   154  O  OE1 . GLU A 1 69  ? 16.783 -21.343 -8.050  1.00 73.23  ? 89   GLU A OE1 1 
ATOM   155  O  OE2 . GLU A 1 69  ? 16.201 -22.107 -6.078  1.00 76.86  ? 89   GLU A OE2 1 
ATOM   156  N  N   . ASN A 1 70  ? 18.410 -16.491 -6.473  1.00 71.50  ? 90   ASN A N   1 
ATOM   157  C  CA  . ASN A 1 70  ? 19.051 -15.205 -6.721  1.00 66.01  ? 90   ASN A CA  1 
ATOM   158  C  C   . ASN A 1 70  ? 20.542 -15.378 -6.971  1.00 59.38  ? 90   ASN A C   1 
ATOM   159  O  O   . ASN A 1 70  ? 21.114 -14.717 -7.845  1.00 54.33  ? 90   ASN A O   1 
ATOM   160  C  CB  . ASN A 1 70  ? 18.799 -14.260 -5.547  1.00 66.06  ? 90   ASN A CB  1 
ATOM   161  C  CG  . ASN A 1 70  ? 17.375 -13.740 -5.516  1.00 64.46  ? 90   ASN A CG  1 
ATOM   162  O  OD1 . ASN A 1 70  ? 17.069 -12.703 -6.105  1.00 60.44  ? 90   ASN A OD1 1 
ATOM   163  N  ND2 . ASN A 1 70  ? 16.494 -14.462 -4.834  1.00 68.07  ? 90   ASN A ND2 1 
ATOM   164  N  N   . ALA A 1 71  ? 21.191 -16.268 -6.215  1.00 60.47  ? 91   ALA A N   1 
ATOM   165  C  CA  . ALA A 1 71  ? 22.604 -16.543 -6.454  1.00 64.94  ? 91   ALA A CA  1 
ATOM   166  C  C   . ALA A 1 71  ? 22.842 -17.024 -7.877  1.00 58.81  ? 91   ALA A C   1 
ATOM   167  O  O   . ALA A 1 71  ? 23.921 -16.798 -8.438  1.00 48.08  ? 91   ALA A O   1 
ATOM   168  C  CB  . ALA A 1 71  ? 23.117 -17.579 -5.455  1.00 70.04  ? 91   ALA A CB  1 
ATOM   169  N  N   . LEU A 1 72  ? 21.856 -17.697 -8.471  1.00 55.26  ? 92   LEU A N   1 
ATOM   170  C  CA  . LEU A 1 72  ? 21.975 -18.101 -9.867  1.00 59.84  ? 92   LEU A CA  1 
ATOM   171  C  C   . LEU A 1 72  ? 21.844 -16.903 -10.798 1.00 54.74  ? 92   LEU A C   1 
ATOM   172  O  O   . LEU A 1 72  ? 22.627 -16.755 -11.744 1.00 60.61  ? 92   LEU A O   1 
ATOM   173  C  CB  . LEU A 1 72  ? 20.918 -19.155 -10.197 1.00 62.03  ? 92   LEU A CB  1 
ATOM   174  C  CG  . LEU A 1 72  ? 20.709 -19.473 -11.680 1.00 59.14  ? 92   LEU A CG  1 
ATOM   175  C  CD1 . LEU A 1 72  ? 22.009 -19.918 -12.330 1.00 52.34  ? 92   LEU A CD1 1 
ATOM   176  C  CD2 . LEU A 1 72  ? 19.634 -20.536 -11.845 1.00 53.66  ? 92   LEU A CD2 1 
ATOM   177  N  N   . VAL A 1 73  ? 20.864 -16.036 -10.545 1.00 51.51  ? 93   VAL A N   1 
ATOM   178  C  CA  . VAL A 1 73  ? 20.635 -14.900 -11.432 1.00 56.59  ? 93   VAL A CA  1 
ATOM   179  C  C   . VAL A 1 73  ? 21.850 -13.980 -11.442 1.00 59.30  ? 93   VAL A C   1 
ATOM   180  O  O   . VAL A 1 73  ? 22.313 -13.547 -12.504 1.00 65.82  ? 93   VAL A O   1 
ATOM   181  C  CB  . VAL A 1 73  ? 19.361 -14.145 -11.017 1.00 55.36  ? 93   VAL A CB  1 
ATOM   182  C  CG1 . VAL A 1 73  ? 19.187 -12.893 -11.862 1.00 53.79  ? 93   VAL A CG1 1 
ATOM   183  C  CG2 . VAL A 1 73  ? 18.150 -15.053 -11.144 1.00 52.26  ? 93   VAL A CG2 1 
ATOM   184  N  N   . VAL A 1 74  ? 22.393 -13.678 -10.261 1.00 58.60  ? 94   VAL A N   1 
ATOM   185  C  CA  . VAL A 1 74  ? 23.532 -12.768 -10.199 1.00 53.13  ? 94   VAL A CA  1 
ATOM   186  C  C   . VAL A 1 74  ? 24.683 -13.315 -11.026 1.00 61.26  ? 94   VAL A C   1 
ATOM   187  O  O   . VAL A 1 74  ? 25.436 -12.551 -11.643 1.00 65.35  ? 94   VAL A O   1 
ATOM   188  C  CB  . VAL A 1 74  ? 23.958 -12.527 -8.736  1.00 56.96  ? 94   VAL A CB  1 
ATOM   189  C  CG1 . VAL A 1 74  ? 25.031 -11.447 -8.662  1.00 49.76  ? 94   VAL A CG1 1 
ATOM   190  C  CG2 . VAL A 1 74  ? 22.760 -12.147 -7.886  1.00 67.01  ? 94   VAL A CG2 1 
ATOM   191  N  N   . ALA A 1 75  ? 24.838 -14.639 -11.060 1.00 61.79  ? 95   ALA A N   1 
ATOM   192  C  CA  . ALA A 1 75  ? 25.914 -15.236 -11.841 1.00 64.65  ? 95   ALA A CA  1 
ATOM   193  C  C   . ALA A 1 75  ? 25.711 -15.008 -13.335 1.00 67.61  ? 95   ALA A C   1 
ATOM   194  O  O   . ALA A 1 75  ? 26.657 -14.650 -14.046 1.00 73.54  ? 95   ALA A O   1 
ATOM   195  C  CB  . ALA A 1 75  ? 26.014 -16.730 -11.535 1.00 66.31  ? 95   ALA A CB  1 
ATOM   196  N  N   . LEU A 1 76  ? 24.485 -15.204 -13.829 1.00 64.26  ? 96   LEU A N   1 
ATOM   197  C  CA  . LEU A 1 76  ? 24.247 -15.085 -15.265 1.00 66.20  ? 96   LEU A CA  1 
ATOM   198  C  C   . LEU A 1 76  ? 24.533 -13.673 -15.758 1.00 63.92  ? 96   LEU A C   1 
ATOM   199  O  O   . LEU A 1 76  ? 25.134 -13.491 -16.822 1.00 70.49  ? 96   LEU A O   1 
ATOM   200  C  CB  . LEU A 1 76  ? 22.810 -15.484 -15.602 1.00 70.68  ? 96   LEU A CB  1 
ATOM   201  C  CG  . LEU A 1 76  ? 22.464 -16.974 -15.528 1.00 64.55  ? 96   LEU A CG  1 
ATOM   202  C  CD1 . LEU A 1 76  ? 21.037 -17.204 -15.986 1.00 55.87  ? 96   LEU A CD1 1 
ATOM   203  C  CD2 . LEU A 1 76  ? 23.421 -17.803 -16.362 1.00 52.25  ? 96   LEU A CD2 1 
ATOM   204  N  N   . ILE A 1 77  ? 24.106 -12.661 -15.003 1.00 59.45  ? 97   ILE A N   1 
ATOM   205  C  CA  . ILE A 1 77  ? 24.397 -11.285 -15.389 1.00 62.35  ? 97   ILE A CA  1 
ATOM   206  C  C   . ILE A 1 77  ? 25.902 -11.056 -15.413 1.00 65.98  ? 97   ILE A C   1 
ATOM   207  O  O   . ILE A 1 77  ? 26.436 -10.416 -16.328 1.00 62.31  ? 97   ILE A O   1 
ATOM   208  C  CB  . ILE A 1 77  ? 23.685 -10.300 -14.442 1.00 68.37  ? 97   ILE A CB  1 
ATOM   209  C  CG1 . ILE A 1 77  ? 22.218 -10.121 -14.851 1.00 64.18  ? 97   ILE A CG1 1 
ATOM   210  C  CG2 . ILE A 1 77  ? 24.396 -8.953  -14.429 1.00 64.13  ? 97   ILE A CG2 1 
ATOM   211  C  CD1 . ILE A 1 77  ? 21.364 -11.360 -14.673 1.00 66.47  ? 97   ILE A CD1 1 
ATOM   212  N  N   . ALA A 1 78  ? 26.610 -11.578 -14.409 1.00 63.40  ? 98   ALA A N   1 
ATOM   213  C  CA  . ALA A 1 78  ? 28.056 -11.395 -14.343 1.00 64.84  ? 98   ALA A CA  1 
ATOM   214  C  C   . ALA A 1 78  ? 28.772 -12.199 -15.423 1.00 67.61  ? 98   ALA A C   1 
ATOM   215  O  O   . ALA A 1 78  ? 29.775 -11.740 -15.982 1.00 68.64  ? 98   ALA A O   1 
ATOM   216  C  CB  . ALA A 1 78  ? 28.568 -11.790 -12.958 1.00 59.40  ? 98   ALA A CB  1 
ATOM   217  N  N   . SER A 1 79  ? 28.276 -13.397 -15.731 1.00 62.03  ? 99   SER A N   1 
ATOM   218  C  CA  . SER A 1 79  ? 28.949 -14.311 -16.643 1.00 62.54  ? 99   SER A CA  1 
ATOM   219  C  C   . SER A 1 79  ? 28.406 -14.245 -18.066 1.00 67.05  ? 99   SER A C   1 
ATOM   220  O  O   . SER A 1 79  ? 28.780 -15.081 -18.894 1.00 72.98  ? 99   SER A O   1 
ATOM   221  C  CB  . SER A 1 79  ? 28.843 -15.744 -16.120 1.00 70.90  ? 99   SER A CB  1 
ATOM   222  O  OG  . SER A 1 79  ? 27.492 -16.161 -16.048 1.00 73.86  ? 99   SER A OG  1 
ATOM   223  N  N   . THR A 1 80  ? 27.539 -13.286 -18.370 1.00 81.02  ? 100  THR A N   1 
ATOM   224  C  CA  . THR A 1 80  ? 26.969 -13.144 -19.709 1.00 79.47  ? 100  THR A CA  1 
ATOM   225  C  C   . THR A 1 80  ? 27.190 -11.719 -20.198 1.00 91.79  ? 100  THR A C   1 
ATOM   226  O  O   . THR A 1 80  ? 26.592 -10.778 -19.638 1.00 87.03  ? 100  THR A O   1 
ATOM   227  C  CB  . THR A 1 80  ? 25.482 -13.486 -19.710 1.00 82.09  ? 100  THR A CB  1 
ATOM   228  O  OG1 . THR A 1 80  ? 25.293 -14.810 -19.195 1.00 57.50  ? 100  THR A OG1 1 
ATOM   229  C  CG2 . THR A 1 80  ? 24.921 -13.414 -21.119 1.00 82.59  ? 100  THR A CG2 1 
ATOM   230  N  N   . PRO A 1 81  ? 28.029 -11.504 -21.217 1.00 92.83  ? 101  PRO A N   1 
ATOM   231  C  CA  . PRO A 1 81  ? 28.234 -10.130 -21.701 1.00 89.23  ? 101  PRO A CA  1 
ATOM   232  C  C   . PRO A 1 81  ? 26.966 -9.494  -22.233 1.00 88.80  ? 101  PRO A C   1 
ATOM   233  O  O   . PRO A 1 81  ? 26.780 -8.280  -22.077 1.00 100.46 ? 101  PRO A O   1 
ATOM   234  C  CB  . PRO A 1 81  ? 29.290 -10.302 -22.801 1.00 102.46 ? 101  PRO A CB  1 
ATOM   235  C  CG  . PRO A 1 81  ? 29.116 -11.699 -23.274 1.00 102.67 ? 101  PRO A CG  1 
ATOM   236  C  CD  . PRO A 1 81  ? 28.715 -12.494 -22.066 1.00 107.42 ? 101  PRO A CD  1 
ATOM   237  N  N   . ALA A 1 82  ? 26.082 -10.280 -22.852 1.00 79.94  ? 102  ALA A N   1 
ATOM   238  C  CA  . ALA A 1 82  ? 24.839 -9.730  -23.377 1.00 80.66  ? 102  ALA A CA  1 
ATOM   239  C  C   . ALA A 1 82  ? 23.963 -9.152  -22.276 1.00 67.50  ? 102  ALA A C   1 
ATOM   240  O  O   . ALA A 1 82  ? 23.097 -8.319  -22.561 1.00 73.66  ? 102  ALA A O   1 
ATOM   241  C  CB  . ALA A 1 82  ? 24.068 -10.806 -24.141 1.00 85.13  ? 102  ALA A CB  1 
ATOM   242  N  N   . LEU A 1 83  ? 24.168 -9.573  -21.031 1.00 61.89  ? 103  LEU A N   1 
ATOM   243  C  CA  . LEU A 1 83  ? 23.414 -9.063  -19.897 1.00 61.29  ? 103  LEU A CA  1 
ATOM   244  C  C   . LEU A 1 83  ? 24.149 -7.950  -19.159 1.00 63.12  ? 103  LEU A C   1 
ATOM   245  O  O   . LEU A 1 83  ? 23.693 -7.520  -18.096 1.00 60.69  ? 103  LEU A O   1 
ATOM   246  C  CB  . LEU A 1 83  ? 23.086 -10.207 -18.935 1.00 66.96  ? 103  LEU A CB  1 
ATOM   247  C  CG  . LEU A 1 83  ? 22.308 -11.372 -19.556 1.00 67.65  ? 103  LEU A CG  1 
ATOM   248  C  CD1 . LEU A 1 83  ? 22.102 -12.484 -18.542 1.00 64.85  ? 103  LEU A CD1 1 
ATOM   249  C  CD2 . LEU A 1 83  ? 20.969 -10.901 -20.111 1.00 66.95  ? 103  LEU A CD2 1 
ATOM   250  N  N   . ARG A 1 84  ? 25.269 -7.468  -19.700 1.00 70.36  ? 104  ARG A N   1 
ATOM   251  C  CA  . ARG A 1 84  ? 26.020 -6.392  -19.068 1.00 77.14  ? 104  ARG A CA  1 
ATOM   252  C  C   . ARG A 1 84  ? 25.390 -5.025  -19.299 1.00 77.37  ? 104  ARG A C   1 
ATOM   253  O  O   . ARG A 1 84  ? 25.875 -4.035  -18.742 1.00 86.39  ? 104  ARG A O   1 
ATOM   254  C  CB  . ARG A 1 84  ? 27.465 -6.378  -19.579 1.00 79.09  ? 104  ARG A CB  1 
ATOM   255  C  CG  . ARG A 1 84  ? 28.448 -5.680  -18.640 1.00 80.77  ? 104  ARG A CG  1 
ATOM   256  C  CD  . ARG A 1 84  ? 29.690 -5.185  -19.372 1.00 84.13  ? 104  ARG A CD  1 
ATOM   257  N  NE  . ARG A 1 84  ? 29.377 -4.114  -20.311 1.00 91.24  ? 104  ARG A NE  1 
ATOM   258  C  CZ  . ARG A 1 84  ? 29.183 -2.847  -19.969 1.00 85.47  ? 104  ARG A CZ  1 
ATOM   259  N  NH1 . ARG A 1 84  ? 29.259 -2.450  -18.709 1.00 84.57  ? 104  ARG A NH1 1 
ATOM   260  N  NH2 . ARG A 1 84  ? 28.899 -1.956  -20.914 1.00 80.83  ? 104  ARG A NH2 1 
ATOM   261  N  N   . THR A 1 85  ? 24.327 -4.948  -20.096 1.00 59.19  ? 105  THR A N   1 
ATOM   262  C  CA  . THR A 1 85  ? 23.693 -3.670  -20.364 1.00 53.57  ? 105  THR A CA  1 
ATOM   263  C  C   . THR A 1 85  ? 23.175 -3.065  -19.060 1.00 50.23  ? 105  THR A C   1 
ATOM   264  O  O   . THR A 1 85  ? 22.863 -3.792  -18.111 1.00 50.94  ? 105  THR A O   1 
ATOM   265  C  CB  . THR A 1 85  ? 22.543 -3.840  -21.358 1.00 52.80  ? 105  THR A CB  1 
ATOM   266  O  OG1 . THR A 1 85  ? 21.913 -2.576  -21.598 1.00 61.43  ? 105  THR A OG1 1 
ATOM   267  C  CG2 . THR A 1 85  ? 21.508 -4.815  -20.826 1.00 58.86  ? 105  THR A CG2 1 
ATOM   268  N  N   . PRO A 1 86  ? 23.073 -1.736  -18.981 1.00 46.21  ? 106  PRO A N   1 
ATOM   269  C  CA  . PRO A 1 86  ? 22.634 -1.117  -17.720 1.00 48.52  ? 106  PRO A CA  1 
ATOM   270  C  C   . PRO A 1 86  ? 21.341 -1.694  -17.172 1.00 43.66  ? 106  PRO A C   1 
ATOM   271  O  O   . PRO A 1 86  ? 21.203 -1.834  -15.951 1.00 39.44  ? 106  PRO A O   1 
ATOM   272  C  CB  . PRO A 1 86  ? 22.476 0.357   -18.107 1.00 51.53  ? 106  PRO A CB  1 
ATOM   273  C  CG  . PRO A 1 86  ? 23.471 0.556   -19.190 1.00 58.63  ? 106  PRO A CG  1 
ATOM   274  C  CD  . PRO A 1 86  ? 23.472 -0.723  -19.976 1.00 47.43  ? 106  PRO A CD  1 
ATOM   275  N  N   . MET A 1 87  ? 20.389 -2.040  -18.039 1.00 42.56  ? 107  MET A N   1 
ATOM   276  C  CA  . MET A 1 87  ? 19.129 -2.592  -17.557 1.00 46.22  ? 107  MET A CA  1 
ATOM   277  C  C   . MET A 1 87  ? 19.368 -3.840  -16.720 1.00 38.43  ? 107  MET A C   1 
ATOM   278  O  O   . MET A 1 87  ? 18.871 -3.954  -15.594 1.00 40.75  ? 107  MET A O   1 
ATOM   279  C  CB  . MET A 1 87  ? 18.211 -2.911  -18.736 1.00 56.37  ? 107  MET A CB  1 
ATOM   280  C  CG  . MET A 1 87  ? 16.897 -3.562  -18.332 1.00 50.08  ? 107  MET A CG  1 
ATOM   281  S  SD  . MET A 1 87  ? 16.084 -4.382  -19.711 1.00 56.69  ? 107  MET A SD  1 
ATOM   282  C  CE  . MET A 1 87  ? 14.892 -5.383  -18.822 1.00 66.34  ? 107  MET A CE  1 
ATOM   283  N  N   . PHE A 1 88  ? 20.124 -4.795  -17.259 1.00 46.87  ? 108  PHE A N   1 
ATOM   284  C  CA  . PHE A 1 88  ? 20.313 -6.065  -16.569 1.00 48.38  ? 108  PHE A CA  1 
ATOM   285  C  C   . PHE A 1 88  ? 21.310 -5.958  -15.422 1.00 49.62  ? 108  PHE A C   1 
ATOM   286  O  O   . PHE A 1 88  ? 21.230 -6.737  -14.465 1.00 49.52  ? 108  PHE A O   1 
ATOM   287  C  CB  . PHE A 1 88  ? 20.751 -7.137  -17.564 1.00 46.97  ? 108  PHE A CB  1 
ATOM   288  C  CG  . PHE A 1 88  ? 19.625 -7.668  -18.401 1.00 49.59  ? 108  PHE A CG  1 
ATOM   289  C  CD1 . PHE A 1 88  ? 18.796 -8.663  -17.913 1.00 61.66  ? 108  PHE A CD1 1 
ATOM   290  C  CD2 . PHE A 1 88  ? 19.384 -7.164  -19.666 1.00 53.84  ? 108  PHE A CD2 1 
ATOM   291  C  CE1 . PHE A 1 88  ? 17.754 -9.151  -18.675 1.00 65.56  ? 108  PHE A CE1 1 
ATOM   292  C  CE2 . PHE A 1 88  ? 18.343 -7.649  -20.433 1.00 63.03  ? 108  PHE A CE2 1 
ATOM   293  C  CZ  . PHE A 1 88  ? 17.528 -8.643  -19.937 1.00 62.86  ? 108  PHE A CZ  1 
ATOM   294  N  N   . VAL A 1 89  ? 22.251 -5.015  -15.493 1.00 48.56  ? 109  VAL A N   1 
ATOM   295  C  CA  . VAL A 1 89  ? 23.143 -4.793  -14.360 1.00 45.00  ? 109  VAL A CA  1 
ATOM   296  C  C   . VAL A 1 89  ? 22.343 -4.337  -13.149 1.00 35.06  ? 109  VAL A C   1 
ATOM   297  O  O   . VAL A 1 89  ? 22.561 -4.809  -12.026 1.00 32.68  ? 109  VAL A O   1 
ATOM   298  C  CB  . VAL A 1 89  ? 24.241 -3.780  -14.732 1.00 50.93  ? 109  VAL A CB  1 
ATOM   299  C  CG1 . VAL A 1 89  ? 25.058 -3.409  -13.505 1.00 36.56  ? 109  VAL A CG1 1 
ATOM   300  C  CG2 . VAL A 1 89  ? 25.136 -4.350  -15.819 1.00 53.84  ? 109  VAL A CG2 1 
ATOM   301  N  N   . LEU A 1 90  ? 21.401 -3.414  -13.357 1.00 39.26  ? 110  LEU A N   1 
ATOM   302  C  CA  . LEU A 1 90  ? 20.547 -2.959  -12.264 1.00 39.20  ? 110  LEU A CA  1 
ATOM   303  C  C   . LEU A 1 90  ? 19.649 -4.081  -11.760 1.00 36.29  ? 110  LEU A C   1 
ATOM   304  O  O   . LEU A 1 90  ? 19.409 -4.199  -10.553 1.00 41.80  ? 110  LEU A O   1 
ATOM   305  C  CB  . LEU A 1 90  ? 19.711 -1.767  -12.722 1.00 36.83  ? 110  LEU A CB  1 
ATOM   306  C  CG  . LEU A 1 90  ? 20.517 -0.520  -13.087 1.00 33.11  ? 110  LEU A CG  1 
ATOM   307  C  CD1 . LEU A 1 90  ? 19.649 0.467   -13.844 1.00 36.73  ? 110  LEU A CD1 1 
ATOM   308  C  CD2 . LEU A 1 90  ? 21.100 0.120   -11.836 1.00 30.43  ? 110  LEU A CD2 1 
ATOM   309  N  N   . VAL A 1 91  ? 19.130 -4.906  -12.669 1.00 35.18  ? 111  VAL A N   1 
ATOM   310  C  CA  . VAL A 1 91  ? 18.351 -6.065  -12.248 1.00 35.86  ? 111  VAL A CA  1 
ATOM   311  C  C   . VAL A 1 91  ? 19.211 -6.998  -11.408 1.00 35.18  ? 111  VAL A C   1 
ATOM   312  O  O   . VAL A 1 91  ? 18.753 -7.550  -10.400 1.00 38.44  ? 111  VAL A O   1 
ATOM   313  C  CB  . VAL A 1 91  ? 17.762 -6.785  -13.474 1.00 40.35  ? 111  VAL A CB  1 
ATOM   314  C  CG1 . VAL A 1 91  ? 17.092 -8.077  -13.054 1.00 45.41  ? 111  VAL A CG1 1 
ATOM   315  C  CG2 . VAL A 1 91  ? 16.772 -5.881  -14.191 1.00 48.23  ? 111  VAL A CG2 1 
ATOM   316  N  N   . GLY A 1 92  ? 20.472 -7.186  -11.803 1.00 36.38  ? 112  GLY A N   1 
ATOM   317  C  CA  . GLY A 1 92  ? 21.363 -8.014  -11.011 1.00 40.02  ? 112  GLY A CA  1 
ATOM   318  C  C   . GLY A 1 92  ? 21.511 -7.504  -9.592  1.00 36.60  ? 112  GLY A C   1 
ATOM   319  O  O   . GLY A 1 92  ? 21.549 -8.287  -8.640  1.00 38.38  ? 112  GLY A O   1 
ATOM   320  N  N   . SER A 1 93  ? 21.584 -6.181  -9.430  1.00 34.03  ? 113  SER A N   1 
ATOM   321  C  CA  . SER A 1 93  ? 21.664 -5.603  -8.093  1.00 30.82  ? 113  SER A CA  1 
ATOM   322  C  C   . SER A 1 93  ? 20.444 -5.975  -7.265  1.00 40.62  ? 113  SER A C   1 
ATOM   323  O  O   . SER A 1 93  ? 20.562 -6.293  -6.076  1.00 41.33  ? 113  SER A O   1 
ATOM   324  C  CB  . SER A 1 93  ? 21.798 -4.086  -8.187  1.00 32.75  ? 113  SER A CB  1 
ATOM   325  O  OG  . SER A 1 93  ? 21.647 -3.486  -6.915  1.00 32.73  ? 113  SER A OG  1 
ATOM   326  N  N   . LEU A 1 94  ? 19.258 -5.937  -7.877  1.00 41.58  ? 114  LEU A N   1 
ATOM   327  C  CA  . LEU A 1 94  ? 18.058 -6.383  -7.181  1.00 39.42  ? 114  LEU A CA  1 
ATOM   328  C  C   . LEU A 1 94  ? 18.186 -7.838  -6.752  1.00 40.62  ? 114  LEU A C   1 
ATOM   329  O  O   . LEU A 1 94  ? 17.810 -8.199  -5.631  1.00 42.21  ? 114  LEU A O   1 
ATOM   330  C  CB  . LEU A 1 94  ? 16.837 -6.191  -8.077  1.00 35.43  ? 114  LEU A CB  1 
ATOM   331  C  CG  . LEU A 1 94  ? 15.549 -6.859  -7.596  1.00 29.90  ? 114  LEU A CG  1 
ATOM   332  C  CD1 . LEU A 1 94  ? 15.196 -6.410  -6.191  1.00 32.72  ? 114  LEU A CD1 1 
ATOM   333  C  CD2 . LEU A 1 94  ? 14.422 -6.549  -8.553  1.00 30.58  ? 114  LEU A CD2 1 
ATOM   334  N  N   . ALA A 1 95  ? 18.720 -8.690  -7.630  1.00 36.40  ? 115  ALA A N   1 
ATOM   335  C  CA  . ALA A 1 95  ? 18.934 -10.083 -7.259  1.00 48.84  ? 115  ALA A CA  1 
ATOM   336  C  C   . ALA A 1 95  ? 19.875 -10.190 -6.067  1.00 45.44  ? 115  ALA A C   1 
ATOM   337  O  O   . ALA A 1 95  ? 19.629 -10.969 -5.139  1.00 47.00  ? 115  ALA A O   1 
ATOM   338  C  CB  . ALA A 1 95  ? 19.486 -10.863 -8.449  1.00 59.33  ? 115  ALA A CB  1 
ATOM   339  N  N   . THR A 1 96  ? 20.954 -9.403  -6.066  1.00 45.25  ? 116  THR A N   1 
ATOM   340  C  CA  . THR A 1 96  ? 21.838 -9.382  -4.906  1.00 50.37  ? 116  THR A CA  1 
ATOM   341  C  C   . THR A 1 96  ? 21.092 -8.891  -3.672  1.00 50.69  ? 116  THR A C   1 
ATOM   342  O  O   . THR A 1 96  ? 21.300 -9.401  -2.566  1.00 59.97  ? 116  THR A O   1 
ATOM   343  C  CB  . THR A 1 96  ? 23.060 -8.502  -5.187  1.00 47.49  ? 116  THR A CB  1 
ATOM   344  O  OG1 . THR A 1 96  ? 23.711 -8.945  -6.386  1.00 45.47  ? 116  THR A OG1 1 
ATOM   345  C  CG2 . THR A 1 96  ? 24.054 -8.568  -4.033  1.00 43.42  ? 116  THR A CG2 1 
ATOM   346  N  N   . ALA A 1 97  ? 20.215 -7.900  -3.842  1.00 47.37  ? 117  ALA A N   1 
ATOM   347  C  CA  . ALA A 1 97  ? 19.385 -7.453  -2.729  1.00 44.83  ? 117  ALA A CA  1 
ATOM   348  C  C   . ALA A 1 97  ? 18.424 -8.552  -2.295  1.00 40.65  ? 117  ALA A C   1 
ATOM   349  O  O   . ALA A 1 97  ? 18.290 -8.844  -1.101  1.00 41.07  ? 117  ALA A O   1 
ATOM   350  C  CB  . ALA A 1 97  ? 18.618 -6.191  -3.120  1.00 56.21  ? 117  ALA A CB  1 
ATOM   351  N  N   . ASP A 1 98  ? 17.736 -9.169  -3.256  1.00 40.26  ? 118  ASP A N   1 
ATOM   352  C  CA  . ASP A 1 98  ? 16.900 -10.318 -2.930  1.00 48.19  ? 118  ASP A CA  1 
ATOM   353  C  C   . ASP A 1 98  ? 17.739 -11.495 -2.456  1.00 50.54  ? 118  ASP A C   1 
ATOM   354  O  O   . ASP A 1 98  ? 17.249 -12.342 -1.700  1.00 54.70  ? 118  ASP A O   1 
ATOM   355  C  CB  . ASP A 1 98  ? 16.058 -10.716 -4.141  1.00 51.57  ? 118  ASP A CB  1 
ATOM   356  C  CG  . ASP A 1 98  ? 14.913 -9.755  -4.395  1.00 52.02  ? 118  ASP A CG  1 
ATOM   357  O  OD1 . ASP A 1 98  ? 14.753 -8.799  -3.609  1.00 44.86  ? 118  ASP A OD1 1 
ATOM   358  O  OD2 . ASP A 1 98  ? 14.174 -9.956  -5.382  1.00 43.71  ? 118  ASP A OD2 1 
ATOM   359  N  N   . LEU A 1 99  ? 18.999 -11.567 -2.886  1.00 50.04  ? 119  LEU A N   1 
ATOM   360  C  CA  . LEU A 1 99  ? 19.892 -12.601 -2.380  1.00 49.26  ? 119  LEU A CA  1 
ATOM   361  C  C   . LEU A 1 99  ? 20.132 -12.422 -0.887  1.00 47.02  ? 119  LEU A C   1 
ATOM   362  O  O   . LEU A 1 99  ? 20.023 -13.376 -0.109  1.00 57.45  ? 119  LEU A O   1 
ATOM   363  C  CB  . LEU A 1 99  ? 21.211 -12.566 -3.151  1.00 50.73  ? 119  LEU A CB  1 
ATOM   364  C  CG  . LEU A 1 99  ? 22.328 -13.491 -2.673  1.00 54.46  ? 119  LEU A CG  1 
ATOM   365  C  CD1 . LEU A 1 99  ? 21.885 -14.945 -2.716  1.00 54.39  ? 119  LEU A CD1 1 
ATOM   366  C  CD2 . LEU A 1 99  ? 23.568 -13.272 -3.523  1.00 58.53  ? 119  LEU A CD2 1 
ATOM   367  N  N   . LEU A 1 100 ? 20.446 -11.194 -0.465  1.00 48.02  ? 120  LEU A N   1 
ATOM   368  C  CA  . LEU A 1 100 ? 20.683 -10.945 0.952   1.00 47.81  ? 120  LEU A CA  1 
ATOM   369  C  C   . LEU A 1 100 ? 19.453 -11.264 1.788   1.00 55.25  ? 120  LEU A C   1 
ATOM   370  O  O   . LEU A 1 100 ? 19.578 -11.614 2.967   1.00 66.06  ? 120  LEU A O   1 
ATOM   371  C  CB  . LEU A 1 100 ? 21.106 -9.492  1.172   1.00 35.54  ? 120  LEU A CB  1 
ATOM   372  C  CG  . LEU A 1 100 ? 22.615 -9.242  1.200   1.00 46.51  ? 120  LEU A CG  1 
ATOM   373  C  CD1 . LEU A 1 100 ? 23.248 -9.502  -0.158  1.00 50.21  ? 120  LEU A CD1 1 
ATOM   374  C  CD2 . LEU A 1 100 ? 22.910 -7.828  1.669   1.00 56.75  ? 120  LEU A CD2 1 
ATOM   375  N  N   . ALA A 1 101 ? 18.260 -11.145 1.203   1.00 58.44  ? 121  ALA A N   1 
ATOM   376  C  CA  . ALA A 1 101 ? 17.050 -11.501 1.934   1.00 53.14  ? 121  ALA A CA  1 
ATOM   377  C  C   . ALA A 1 101 ? 17.049 -12.979 2.298   1.00 54.24  ? 121  ALA A C   1 
ATOM   378  O  O   . ALA A 1 101 ? 16.724 -13.346 3.433   1.00 46.78  ? 121  ALA A O   1 
ATOM   379  C  CB  . ALA A 1 101 ? 15.816 -11.148 1.104   1.00 60.30  ? 121  ALA A CB  1 
ATOM   380  N  N   . GLY A 1 102 ? 17.418 -13.843 1.351   1.00 53.14  ? 122  GLY A N   1 
ATOM   381  C  CA  . GLY A 1 102 ? 17.477 -15.265 1.647   1.00 60.86  ? 122  GLY A CA  1 
ATOM   382  C  C   . GLY A 1 102 ? 18.564 -15.606 2.649   1.00 53.67  ? 122  GLY A C   1 
ATOM   383  O  O   . GLY A 1 102 ? 18.351 -16.406 3.563   1.00 50.21  ? 122  GLY A O   1 
ATOM   384  N  N   . LEU A 1 103 ? 19.746 -15.008 2.488   1.00 49.05  ? 123  LEU A N   1 
ATOM   385  C  CA  . LEU A 1 103 ? 20.832 -15.258 3.428   1.00 50.59  ? 123  LEU A CA  1 
ATOM   386  C  C   . LEU A 1 103 ? 20.491 -14.733 4.815   1.00 56.43  ? 123  LEU A C   1 
ATOM   387  O  O   . LEU A 1 103 ? 20.728 -15.416 5.818   1.00 62.99  ? 123  LEU A O   1 
ATOM   388  C  CB  . LEU A 1 103 ? 22.119 -14.608 2.925   1.00 58.21  ? 123  LEU A CB  1 
ATOM   389  C  CG  . LEU A 1 103 ? 22.556 -14.981 1.509   1.00 66.49  ? 123  LEU A CG  1 
ATOM   390  C  CD1 . LEU A 1 103 ? 23.831 -14.234 1.140   1.00 52.55  ? 123  LEU A CD1 1 
ATOM   391  C  CD2 . LEU A 1 103 ? 22.749 -16.487 1.377   1.00 62.97  ? 123  LEU A CD2 1 
ATOM   392  N  N   . GLY A 1 104 ? 19.930 -13.526 4.891   1.00 67.08  ? 124  GLY A N   1 
ATOM   393  C  CA  . GLY A 1 104 ? 19.695 -12.919 6.189   1.00 59.41  ? 124  GLY A CA  1 
ATOM   394  C  C   . GLY A 1 104 ? 18.779 -13.754 7.060   1.00 55.80  ? 124  GLY A C   1 
ATOM   395  O  O   . GLY A 1 104 ? 19.096 -14.046 8.215   1.00 63.35  ? 124  GLY A O   1 
ATOM   396  N  N   . LEU A 1 105 ? 17.639 -14.175 6.508   1.00 60.97  ? 125  LEU A N   1 
ATOM   397  C  CA  . LEU A 1 105 ? 16.701 -14.958 7.303   1.00 66.88  ? 125  LEU A CA  1 
ATOM   398  C  C   . LEU A 1 105 ? 17.228 -16.363 7.560   1.00 70.25  ? 125  LEU A C   1 
ATOM   399  O  O   . LEU A 1 105 ? 16.885 -16.975 8.578   1.00 71.91  ? 125  LEU A O   1 
ATOM   400  C  CB  . LEU A 1 105 ? 15.336 -15.009 6.614   1.00 56.61  ? 125  LEU A CB  1 
ATOM   401  C  CG  . LEU A 1 105 ? 15.191 -15.879 5.364   1.00 64.00  ? 125  LEU A CG  1 
ATOM   402  C  CD1 . LEU A 1 105 ? 15.037 -17.352 5.723   1.00 71.07  ? 125  LEU A CD1 1 
ATOM   403  C  CD2 . LEU A 1 105 ? 14.009 -15.405 4.537   1.00 70.98  ? 125  LEU A CD2 1 
ATOM   404  N  N   . ILE A 1 106 ? 18.048 -16.895 6.652   1.00 61.65  ? 126  ILE A N   1 
ATOM   405  C  CA  . ILE A 1 106 ? 18.654 -18.202 6.883   1.00 65.52  ? 126  ILE A CA  1 
ATOM   406  C  C   . ILE A 1 106 ? 19.561 -18.148 8.104   1.00 72.90  ? 126  ILE A C   1 
ATOM   407  O  O   . ILE A 1 106 ? 19.461 -18.977 9.015   1.00 75.40  ? 126  ILE A O   1 
ATOM   408  C  CB  . ILE A 1 106 ? 19.420 -18.667 5.631   1.00 71.58  ? 126  ILE A CB  1 
ATOM   409  C  CG1 . ILE A 1 106 ? 18.455 -19.292 4.619   1.00 73.31  ? 126  ILE A CG1 1 
ATOM   410  C  CG2 . ILE A 1 106 ? 20.535 -19.642 6.009   1.00 74.38  ? 126  ILE A CG2 1 
ATOM   411  C  CD1 . ILE A 1 106 ? 17.883 -20.635 5.044   1.00 75.31  ? 126  ILE A CD1 1 
ATOM   412  N  N   . LEU A 1 107 ? 20.458 -17.164 8.143   1.00 65.93  ? 127  LEU A N   1 
ATOM   413  C  CA  . LEU A 1 107 ? 21.289 -16.975 9.321   1.00 64.98  ? 127  LEU A CA  1 
ATOM   414  C  C   . LEU A 1 107 ? 20.471 -16.535 10.527  1.00 70.43  ? 127  LEU A C   1 
ATOM   415  O  O   . LEU A 1 107 ? 20.899 -16.750 11.665  1.00 71.71  ? 127  LEU A O   1 
ATOM   416  C  CB  . LEU A 1 107 ? 22.385 -15.954 9.021   1.00 64.11  ? 127  LEU A CB  1 
ATOM   417  C  CG  . LEU A 1 107 ? 23.319 -16.347 7.875   1.00 54.28  ? 127  LEU A CG  1 
ATOM   418  C  CD1 . LEU A 1 107 ? 23.681 -15.133 7.039   1.00 59.69  ? 127  LEU A CD1 1 
ATOM   419  C  CD2 . LEU A 1 107 ? 24.571 -17.011 8.418   1.00 55.72  ? 127  LEU A CD2 1 
ATOM   420  N  N   . HIS A 1 108 ? 19.302 -15.930 10.305  1.00 77.54  ? 128  HIS A N   1 
ATOM   421  C  CA  . HIS A 1 108 ? 18.450 -15.541 11.423  1.00 73.04  ? 128  HIS A CA  1 
ATOM   422  C  C   . HIS A 1 108 ? 17.926 -16.765 12.160  1.00 73.27  ? 128  HIS A C   1 
ATOM   423  O  O   . HIS A 1 108 ? 18.028 -16.852 13.388  1.00 80.48  ? 128  HIS A O   1 
ATOM   424  C  CB  . HIS A 1 108 ? 17.289 -14.682 10.927  1.00 68.16  ? 128  HIS A CB  1 
ATOM   425  C  CG  . HIS A 1 108 ? 16.324 -14.296 12.004  1.00 66.19  ? 128  HIS A CG  1 
ATOM   426  N  ND1 . HIS A 1 108 ? 16.638 -13.391 12.995  1.00 72.01  ? 128  HIS A ND1 1 
ATOM   427  C  CD2 . HIS A 1 108 ? 15.054 -14.696 12.249  1.00 67.09  ? 128  HIS A CD2 1 
ATOM   428  C  CE1 . HIS A 1 108 ? 15.601 -13.247 13.801  1.00 73.56  ? 128  HIS A CE1 1 
ATOM   429  N  NE2 . HIS A 1 108 ? 14.627 -14.028 13.371  1.00 73.42  ? 128  HIS A NE2 1 
ATOM   430  N  N   . PHE A 1 109 ? 17.354 -17.722 11.427  1.00 67.45  ? 129  PHE A N   1 
ATOM   431  C  CA  . PHE A 1 109 ? 16.904 -18.956 12.059  1.00 65.94  ? 129  PHE A CA  1 
ATOM   432  C  C   . PHE A 1 109 ? 18.078 -19.727 12.644  1.00 70.22  ? 129  PHE A C   1 
ATOM   433  O  O   . PHE A 1 109 ? 18.012 -20.209 13.781  1.00 66.79  ? 129  PHE A O   1 
ATOM   434  C  CB  . PHE A 1 109 ? 16.151 -19.820 11.049  1.00 74.60  ? 129  PHE A CB  1 
ATOM   435  C  CG  . PHE A 1 109 ? 16.070 -21.273 11.435  1.00 81.45  ? 129  PHE A CG  1 
ATOM   436  C  CD1 . PHE A 1 109 ? 15.062 -21.729 12.267  1.00 74.11  ? 129  PHE A CD1 1 
ATOM   437  C  CD2 . PHE A 1 109 ? 17.006 -22.183 10.966  1.00 74.01  ? 129  PHE A CD2 1 
ATOM   438  C  CE1 . PHE A 1 109 ? 14.987 -23.063 12.622  1.00 74.80  ? 129  PHE A CE1 1 
ATOM   439  C  CE2 . PHE A 1 109 ? 16.936 -23.517 11.321  1.00 76.08  ? 129  PHE A CE2 1 
ATOM   440  C  CZ  . PHE A 1 109 ? 15.925 -23.957 12.149  1.00 65.21  ? 129  PHE A CZ  1 
ATOM   441  N  N   . VAL A 1 110 ? 19.168 -19.844 11.883  1.00 70.04  ? 130  VAL A N   1 
ATOM   442  C  CA  . VAL A 1 110 ? 20.329 -20.586 12.358  1.00 68.53  ? 130  VAL A CA  1 
ATOM   443  C  C   . VAL A 1 110 ? 20.852 -19.984 13.651  1.00 70.66  ? 130  VAL A C   1 
ATOM   444  O  O   . VAL A 1 110 ? 21.430 -20.690 14.487  1.00 73.09  ? 130  VAL A O   1 
ATOM   445  C  CB  . VAL A 1 110 ? 21.419 -20.616 11.269  1.00 67.55  ? 130  VAL A CB  1 
ATOM   446  C  CG1 . VAL A 1 110 ? 22.709 -21.189 11.827  1.00 69.90  ? 130  VAL A CG1 1 
ATOM   447  C  CG2 . VAL A 1 110 ? 20.948 -21.427 10.072  1.00 70.97  ? 130  VAL A CG2 1 
ATOM   448  N  N   . PHE A 1 111 ? 20.659 -18.681 13.842  1.00 77.06  ? 131  PHE A N   1 
ATOM   449  C  CA  . PHE A 1 111 ? 21.117 -18.002 15.045  1.00 81.85  ? 131  PHE A CA  1 
ATOM   450  C  C   . PHE A 1 111 ? 19.995 -17.691 16.022  1.00 80.40  ? 131  PHE A C   1 
ATOM   451  O  O   . PHE A 1 111 ? 20.226 -17.696 17.234  1.00 74.90  ? 131  PHE A O   1 
ATOM   452  C  CB  . PHE A 1 111 ? 21.846 -16.707 14.669  1.00 79.82  ? 131  PHE A CB  1 
ATOM   453  C  CG  . PHE A 1 111 ? 23.201 -16.938 14.056  1.00 81.99  ? 131  PHE A CG  1 
ATOM   454  C  CD1 . PHE A 1 111 ? 23.333 -17.670 12.886  1.00 74.68  ? 131  PHE A CD1 1 
ATOM   455  C  CD2 . PHE A 1 111 ? 24.340 -16.426 14.649  1.00 81.57  ? 131  PHE A CD2 1 
ATOM   456  C  CE1 . PHE A 1 111 ? 24.574 -17.887 12.322  1.00 73.42  ? 131  PHE A CE1 1 
ATOM   457  C  CE2 . PHE A 1 111 ? 25.586 -16.641 14.088  1.00 74.36  ? 131  PHE A CE2 1 
ATOM   458  C  CZ  . PHE A 1 111 ? 25.702 -17.371 12.924  1.00 71.19  ? 131  PHE A CZ  1 
ATOM   459  N  N   . GLN A 1 112 ? 18.780 -17.440 15.536  1.00 77.01  ? 132  GLN A N   1 
ATOM   460  C  CA  . GLN A 1 112 ? 17.648 -17.337 16.447  1.00 74.27  ? 132  GLN A CA  1 
ATOM   461  C  C   . GLN A 1 112 ? 17.450 -18.626 17.228  1.00 74.59  ? 132  GLN A C   1 
ATOM   462  O  O   . GLN A 1 112 ? 16.821 -18.606 18.291  1.00 79.71  ? 132  GLN A O   1 
ATOM   463  C  CB  . GLN A 1 112 ? 16.377 -16.986 15.673  1.00 77.02  ? 132  GLN A CB  1 
ATOM   464  C  CG  . GLN A 1 112 ? 15.138 -16.871 16.540  1.00 77.63  ? 132  GLN A CG  1 
ATOM   465  C  CD  . GLN A 1 112 ? 13.955 -16.298 15.786  1.00 76.36  ? 132  GLN A CD  1 
ATOM   466  O  OE1 . GLN A 1 112 ? 13.917 -16.323 14.555  1.00 75.60  ? 132  GLN A OE1 1 
ATOM   467  N  NE2 . GLN A 1 112 ? 12.983 -15.772 16.522  1.00 65.98  ? 132  GLN A NE2 1 
ATOM   468  N  N   . TYR A 1 113 ? 17.974 -19.742 16.722  1.00 77.25  ? 133  TYR A N   1 
ATOM   469  C  CA  . TYR A 1 113 ? 17.936 -21.033 17.401  1.00 87.51  ? 133  TYR A CA  1 
ATOM   470  C  C   . TYR A 1 113 ? 19.370 -21.522 17.574  1.00 77.61  ? 133  TYR A C   1 
ATOM   471  O  O   . TYR A 1 113 ? 20.008 -21.941 16.603  1.00 76.85  ? 133  TYR A O   1 
ATOM   472  C  CB  . TYR A 1 113 ? 17.106 -22.044 16.606  1.00 84.59  ? 133  TYR A CB  1 
ATOM   473  C  CG  . TYR A 1 113 ? 15.667 -21.628 16.360  1.00 83.94  ? 133  TYR A CG  1 
ATOM   474  C  CD1 . TYR A 1 113 ? 15.356 -20.623 15.449  1.00 78.95  ? 133  TYR A CD1 1 
ATOM   475  C  CD2 . TYR A 1 113 ? 14.618 -22.253 17.024  1.00 77.80  ? 133  TYR A CD2 1 
ATOM   476  C  CE1 . TYR A 1 113 ? 14.043 -20.246 15.218  1.00 73.05  ? 133  TYR A CE1 1 
ATOM   477  C  CE2 . TYR A 1 113 ? 13.302 -21.882 16.798  1.00 70.55  ? 133  TYR A CE2 1 
ATOM   478  C  CZ  . TYR A 1 113 ? 13.021 -20.880 15.894  1.00 74.60  ? 133  TYR A CZ  1 
ATOM   479  O  OH  . TYR A 1 113 ? 11.715 -20.509 15.667  1.00 64.13  ? 133  TYR A OH  1 
ATOM   480  N  N   . LEU A 1 114 ? 19.869 -21.483 18.810  1.00 82.62  ? 134  LEU A N   1 
ATOM   481  C  CA  . LEU A 1 114 ? 21.203 -21.980 19.150  1.00 82.96  ? 134  LEU A CA  1 
ATOM   482  C  C   . LEU A 1 114 ? 22.292 -21.218 18.384  1.00 95.39  ? 134  LEU A C   1 
ATOM   483  O  O   . LEU A 1 114 ? 23.006 -21.764 17.539  1.00 87.44  ? 134  LEU A O   1 
ATOM   484  C  CB  . LEU A 1 114 ? 21.298 -23.486 18.879  1.00 88.13  ? 134  LEU A CB  1 
ATOM   485  N  N   . VAL A 1 115 ? 22.398 -19.931 18.707  1.00 94.59  ? 135  VAL A N   1 
ATOM   486  C  CA  . VAL A 1 115 ? 23.423 -19.060 18.127  1.00 91.59  ? 135  VAL A CA  1 
ATOM   487  C  C   . VAL A 1 115 ? 24.536 -18.812 19.139  1.00 94.97  ? 135  VAL A C   1 
ATOM   488  O  O   . VAL A 1 115 ? 24.354 -19.072 20.337  1.00 88.19  ? 135  VAL A O   1 
ATOM   489  C  CB  . VAL A 1 115 ? 22.832 -17.719 17.671  1.00 81.12  ? 135  VAL A CB  1 
ATOM   490  N  N   . PRO A 1 116 ? 25.700 -18.316 18.705  1.00 95.25  ? 136  PRO A N   1 
ATOM   491  C  CA  . PRO A 1 116 ? 26.719 -17.902 19.685  1.00 98.18  ? 136  PRO A CA  1 
ATOM   492  C  C   . PRO A 1 116 ? 26.233 -16.821 20.635  1.00 99.95  ? 136  PRO A C   1 
ATOM   493  O  O   . PRO A 1 116 ? 26.578 -16.844 21.824  1.00 103.05 ? 136  PRO A O   1 
ATOM   494  C  CB  . PRO A 1 116 ? 27.876 -17.409 18.801  1.00 86.23  ? 136  PRO A CB  1 
ATOM   495  C  CG  . PRO A 1 116 ? 27.257 -17.116 17.471  1.00 85.55  ? 136  PRO A CG  1 
ATOM   496  C  CD  . PRO A 1 116 ? 26.151 -18.110 17.320  1.00 85.95  ? 136  PRO A CD  1 
ATOM   497  N  N   . SER A 1 117 ? 25.438 -15.872 20.146  1.00 97.89  ? 137  SER A N   1 
ATOM   498  C  CA  . SER A 1 117 ? 24.927 -14.789 20.979  1.00 102.11 ? 137  SER A CA  1 
ATOM   499  C  C   . SER A 1 117 ? 23.827 -14.057 20.220  1.00 92.53  ? 137  SER A C   1 
ATOM   500  O  O   . SER A 1 117 ? 23.699 -14.186 18.999  1.00 87.23  ? 137  SER A O   1 
ATOM   501  C  CB  . SER A 1 117 ? 26.043 -13.818 21.381  1.00 99.38  ? 137  SER A CB  1 
ATOM   502  O  OG  . SER A 1 117 ? 26.628 -13.212 20.242  1.00 96.46  ? 137  SER A OG  1 
ATOM   503  N  N   . GLU A 1 118 ? 23.027 -13.294 20.971  1.00 91.10  ? 138  GLU A N   1 
ATOM   504  C  CA  . GLU A 1 118 ? 21.950 -12.506 20.378  1.00 88.09  ? 138  GLU A CA  1 
ATOM   505  C  C   . GLU A 1 118 ? 22.464 -11.275 19.643  1.00 85.56  ? 138  GLU A C   1 
ATOM   506  O  O   . GLU A 1 118 ? 21.809 -10.806 18.707  1.00 87.71  ? 138  GLU A O   1 
ATOM   507  C  CB  . GLU A 1 118 ? 20.958 -12.081 21.460  1.00 95.01  ? 138  GLU A CB  1 
ATOM   508  C  CG  . GLU A 1 118 ? 19.625 -11.559 20.927  1.00 90.72  ? 138  GLU A CG  1 
ATOM   509  C  CD  . GLU A 1 118 ? 19.675 -10.107 20.476  1.00 81.55  ? 138  GLU A CD  1 
ATOM   510  O  OE1 . GLU A 1 118 ? 20.676 -9.416  20.762  1.00 85.49  ? 138  GLU A OE1 1 
ATOM   511  O  OE2 . GLU A 1 118 ? 18.705 -9.656  19.832  1.00 73.47  ? 138  GLU A OE2 1 
ATOM   512  N  N   . THR A 1 119 ? 23.611 -10.729 20.053  1.00 83.98  ? 139  THR A N   1 
ATOM   513  C  CA  . THR A 1 119 ? 24.171 -9.588  19.337  1.00 76.04  ? 139  THR A CA  1 
ATOM   514  C  C   . THR A 1 119 ? 24.365 -9.909  17.862  1.00 85.48  ? 139  THR A C   1 
ATOM   515  O  O   . THR A 1 119 ? 24.178 -9.042  17.003  1.00 83.46  ? 139  THR A O   1 
ATOM   516  C  CB  . THR A 1 119 ? 25.496 -9.167  19.968  1.00 80.78  ? 139  THR A CB  1 
ATOM   517  O  OG1 . THR A 1 119 ? 25.256 -8.628  21.274  1.00 82.19  ? 139  THR A OG1 1 
ATOM   518  C  CG2 . THR A 1 119 ? 26.195 -8.123  19.106  1.00 70.80  ? 139  THR A CG2 1 
ATOM   519  N  N   . VAL A 1 120 ? 24.744 -11.149 17.548  1.00 84.10  ? 140  VAL A N   1 
ATOM   520  C  CA  . VAL A 1 120 ? 24.870 -11.545 16.149  1.00 78.29  ? 140  VAL A CA  1 
ATOM   521  C  C   . VAL A 1 120 ? 23.518 -11.458 15.456  1.00 75.25  ? 140  VAL A C   1 
ATOM   522  O  O   . VAL A 1 120 ? 23.417 -10.990 14.315  1.00 73.14  ? 140  VAL A O   1 
ATOM   523  C  CB  . VAL A 1 120 ? 25.467 -12.960 16.039  1.00 92.35  ? 140  VAL A CB  1 
ATOM   524  C  CG1 . VAL A 1 120 ? 25.620 -13.348 14.576  1.00 94.95  ? 140  VAL A CG1 1 
ATOM   525  C  CG2 . VAL A 1 120 ? 26.805 -13.037 16.760  1.00 91.37  ? 140  VAL A CG2 1 
ATOM   526  N  N   . SER A 1 121 ? 22.457 -11.906 16.133  1.00 90.14  ? 141  SER A N   1 
ATOM   527  C  CA  . SER A 1 121 ? 21.114 -11.779 15.576  1.00 88.40  ? 141  SER A CA  1 
ATOM   528  C  C   . SER A 1 121 ? 20.761 -10.325 15.290  1.00 86.46  ? 141  SER A C   1 
ATOM   529  O  O   . SER A 1 121 ? 19.913 -10.051 14.433  1.00 81.66  ? 141  SER A O   1 
ATOM   530  C  CB  . SER A 1 121 ? 20.086 -12.386 16.531  1.00 88.75  ? 141  SER A CB  1 
ATOM   531  O  OG  . SER A 1 121 ? 18.774 -12.266 16.009  1.00 84.25  ? 141  SER A OG  1 
ATOM   532  N  N   . LEU A 1 122 ? 21.386 -9.384  16.003  1.00 79.06  ? 142  LEU A N   1 
ATOM   533  C  CA  . LEU A 1 122 ? 21.188 -7.972  15.711  1.00 70.76  ? 142  LEU A CA  1 
ATOM   534  C  C   . LEU A 1 122 ? 21.907 -7.544  14.438  1.00 76.97  ? 142  LEU A C   1 
ATOM   535  O  O   . LEU A 1 122 ? 21.548 -6.516  13.856  1.00 81.00  ? 142  LEU A O   1 
ATOM   536  C  CB  . LEU A 1 122 ? 21.656 -7.132  16.901  1.00 66.93  ? 142  LEU A CB  1 
ATOM   537  C  CG  . LEU A 1 122 ? 21.499 -5.615  16.791  1.00 76.57  ? 142  LEU A CG  1 
ATOM   538  C  CD1 . LEU A 1 122 ? 21.191 -5.014  18.159  1.00 73.33  ? 142  LEU A CD1 1 
ATOM   539  C  CD2 . LEU A 1 122 ? 22.750 -4.984  16.190  1.00 73.45  ? 142  LEU A CD2 1 
ATOM   540  N  N   . LEU A 1 123 ? 22.929 -8.288  14.008  1.00 80.90  ? 143  LEU A N   1 
ATOM   541  C  CA  . LEU A 1 123 ? 23.511 -8.053  12.690  1.00 71.29  ? 143  LEU A CA  1 
ATOM   542  C  C   . LEU A 1 123 ? 22.639 -8.635  11.585  1.00 73.64  ? 143  LEU A C   1 
ATOM   543  O  O   . LEU A 1 123 ? 22.496 -8.028  10.518  1.00 69.31  ? 143  LEU A O   1 
ATOM   544  C  CB  . LEU A 1 123 ? 24.917 -8.648  12.607  1.00 74.06  ? 143  LEU A CB  1 
ATOM   545  C  CG  . LEU A 1 123 ? 26.025 -7.892  13.341  1.00 85.49  ? 143  LEU A CG  1 
ATOM   546  C  CD1 . LEU A 1 123 ? 26.213 -8.449  14.737  1.00 100.01 ? 143  LEU A CD1 1 
ATOM   547  C  CD2 . LEU A 1 123 ? 27.325 -7.950  12.556  1.00 83.78  ? 143  LEU A CD2 1 
ATOM   548  N  N   . THR A 1 124 ? 22.054 -9.812  11.820  1.00 82.62  ? 144  THR A N   1 
ATOM   549  C  CA  . THR A 1 124 ? 21.237 -10.446 10.791  1.00 88.17  ? 144  THR A CA  1 
ATOM   550  C  C   . THR A 1 124 ? 20.032 -9.586  10.444  1.00 90.61  ? 144  THR A C   1 
ATOM   551  O  O   . THR A 1 124 ? 19.673 -9.451  9.269   1.00 95.92  ? 144  THR A O   1 
ATOM   552  C  CB  . THR A 1 124 ? 20.780 -11.831 11.252  1.00 97.05  ? 144  THR A CB  1 
ATOM   553  O  OG1 . THR A 1 124 ? 19.942 -11.702 12.407  1.00 90.47  ? 144  THR A OG1 1 
ATOM   554  C  CG2 . THR A 1 124 ? 21.977 -12.711 11.587  1.00 100.94 ? 144  THR A CG2 1 
ATOM   555  N  N   . VAL A 1 125 ? 19.393 -8.989  11.454  1.00 70.71  ? 145  VAL A N   1 
ATOM   556  C  CA  . VAL A 1 125 ? 18.273 -8.099  11.177  1.00 57.51  ? 145  VAL A CA  1 
ATOM   557  C  C   . VAL A 1 125 ? 18.727 -6.965  10.272  1.00 65.09  ? 145  VAL A C   1 
ATOM   558  O  O   . VAL A 1 125 ? 17.954 -6.474  9.440   1.00 71.00  ? 145  VAL A O   1 
ATOM   559  C  CB  . VAL A 1 125 ? 17.668 -7.575  12.493  1.00 54.77  ? 145  VAL A CB  1 
ATOM   560  C  CG1 . VAL A 1 125 ? 18.506 -6.437  13.055  1.00 57.18  ? 145  VAL A CG1 1 
ATOM   561  C  CG2 . VAL A 1 125 ? 16.231 -7.140  12.277  1.00 48.83  ? 145  VAL A CG2 1 
ATOM   562  N  N   . GLY A 1 126 ? 19.985 -6.540  10.406  1.00 64.40  ? 146  GLY A N   1 
ATOM   563  C  CA  . GLY A 1 126 ? 20.526 -5.560  9.481   1.00 56.48  ? 146  GLY A CA  1 
ATOM   564  C  C   . GLY A 1 126 ? 20.568 -6.076  8.056   1.00 58.50  ? 146  GLY A C   1 
ATOM   565  O  O   . GLY A 1 126 ? 20.327 -5.326  7.107   1.00 57.71  ? 146  GLY A O   1 
ATOM   566  N  N   . PHE A 1 127 ? 20.875 -7.364  7.884   1.00 63.08  ? 147  PHE A N   1 
ATOM   567  C  CA  . PHE A 1 127 ? 20.834 -7.954  6.551   1.00 59.43  ? 147  PHE A CA  1 
ATOM   568  C  C   . PHE A 1 127 ? 19.436 -7.848  5.959   1.00 56.65  ? 147  PHE A C   1 
ATOM   569  O  O   . PHE A 1 127 ? 19.267 -7.455  4.799   1.00 65.94  ? 147  PHE A O   1 
ATOM   570  C  CB  . PHE A 1 127 ? 21.289 -9.417  6.603   1.00 61.12  ? 147  PHE A CB  1 
ATOM   571  C  CG  . PHE A 1 127 ? 22.743 -9.626  6.265   1.00 64.42  ? 147  PHE A CG  1 
ATOM   572  C  CD1 . PHE A 1 127 ? 23.677 -8.617  6.450   1.00 72.66  ? 147  PHE A CD1 1 
ATOM   573  C  CD2 . PHE A 1 127 ? 23.174 -10.840 5.756   1.00 65.80  ? 147  PHE A CD2 1 
ATOM   574  C  CE1 . PHE A 1 127 ? 25.007 -8.817  6.135   1.00 77.49  ? 147  PHE A CE1 1 
ATOM   575  C  CE2 . PHE A 1 127 ? 24.504 -11.045 5.439   1.00 68.59  ? 147  PHE A CE2 1 
ATOM   576  C  CZ  . PHE A 1 127 ? 25.420 -10.033 5.629   1.00 76.24  ? 147  PHE A CZ  1 
ATOM   577  N  N   . LEU A 1 128 ? 18.414 -8.182  6.750   1.00 65.43  ? 148  LEU A N   1 
ATOM   578  C  CA  . LEU A 1 128 ? 17.043 -8.043  6.271   1.00 63.78  ? 148  LEU A CA  1 
ATOM   579  C  C   . LEU A 1 128 ? 16.701 -6.581  6.012   1.00 46.24  ? 148  LEU A C   1 
ATOM   580  O  O   . LEU A 1 128 ? 16.021 -6.257  5.032   1.00 41.40  ? 148  LEU A O   1 
ATOM   581  C  CB  . LEU A 1 128 ? 16.065 -8.652  7.276   1.00 59.79  ? 148  LEU A CB  1 
ATOM   582  C  CG  . LEU A 1 128 ? 16.069 -10.177 7.437   1.00 50.57  ? 148  LEU A CG  1 
ATOM   583  C  CD1 . LEU A 1 128 ? 16.015 -10.872 6.090   1.00 50.99  ? 148  LEU A CD1 1 
ATOM   584  C  CD2 . LEU A 1 128 ? 17.274 -10.645 8.227   1.00 67.96  ? 148  LEU A CD2 1 
ATOM   585  N  N   . VAL A 1 129 ? 17.152 -5.684  6.890   1.00 53.91  ? 149  VAL A N   1 
ATOM   586  C  CA  . VAL A 1 129 ? 16.992 -4.256  6.635   1.00 58.24  ? 149  VAL A CA  1 
ATOM   587  C  C   . VAL A 1 129 ? 17.778 -3.854  5.397   1.00 59.76  ? 149  VAL A C   1 
ATOM   588  O  O   . VAL A 1 129 ? 17.282 -3.114  4.538   1.00 55.54  ? 149  VAL A O   1 
ATOM   589  C  CB  . VAL A 1 129 ? 17.429 -3.440  7.865   1.00 56.45  ? 149  VAL A CB  1 
ATOM   590  C  CG1 . VAL A 1 129 ? 17.512 -1.962  7.516   1.00 53.16  ? 149  VAL A CG1 1 
ATOM   591  C  CG2 . VAL A 1 129 ? 16.474 -3.664  9.019   1.00 55.38  ? 149  VAL A CG2 1 
ATOM   592  N  N   . ALA A 1 130 ? 19.019 -4.332  5.287   1.00 53.90  ? 150  ALA A N   1 
ATOM   593  C  CA  . ALA A 1 130 ? 19.849 -3.983  4.141   1.00 50.65  ? 150  ALA A CA  1 
ATOM   594  C  C   . ALA A 1 130 ? 19.246 -4.506  2.845   1.00 46.66  ? 150  ALA A C   1 
ATOM   595  O  O   . ALA A 1 130 ? 19.250 -3.809  1.824   1.00 48.78  ? 150  ALA A O   1 
ATOM   596  C  CB  . ALA A 1 130 ? 21.262 -4.531  4.334   1.00 54.82  ? 150  ALA A CB  1 
ATOM   597  N  N   . SER A 1 131 ? 18.721 -5.733  2.865   1.00 44.81  ? 151  SER A N   1 
ATOM   598  C  CA  . SER A 1 131 ? 18.118 -6.288  1.659   1.00 40.65  ? 151  SER A CA  1 
ATOM   599  C  C   . SER A 1 131 ? 16.931 -5.450  1.210   1.00 43.17  ? 151  SER A C   1 
ATOM   600  O  O   . SER A 1 131 ? 16.789 -5.146  0.020   1.00 42.30  ? 151  SER A O   1 
ATOM   601  C  CB  . SER A 1 131 ? 17.681 -7.731  1.905   1.00 49.89  ? 151  SER A CB  1 
ATOM   602  O  OG  . SER A 1 131 ? 16.634 -7.787  2.858   1.00 48.07  ? 151  SER A OG  1 
ATOM   603  N  N   . PHE A 1 132 ? 16.071 -5.059  2.151   1.00 46.50  ? 152  PHE A N   1 
ATOM   604  C  CA  . PHE A 1 132 ? 14.886 -4.291  1.792   1.00 35.17  ? 152  PHE A CA  1 
ATOM   605  C  C   . PHE A 1 132 ? 15.266 -2.948  1.180   1.00 36.51  ? 152  PHE A C   1 
ATOM   606  O  O   . PHE A 1 132 ? 14.698 -2.532  0.164   1.00 38.63  ? 152  PHE A O   1 
ATOM   607  C  CB  . PHE A 1 132 ? 14.004 -4.085  3.020   1.00 35.74  ? 152  PHE A CB  1 
ATOM   608  C  CG  . PHE A 1 132 ? 12.841 -3.181  2.769   1.00 32.44  ? 152  PHE A CG  1 
ATOM   609  C  CD1 . PHE A 1 132 ? 11.734 -3.639  2.082   1.00 31.22  ? 152  PHE A CD1 1 
ATOM   610  C  CD2 . PHE A 1 132 ? 12.861 -1.870  3.205   1.00 29.20  ? 152  PHE A CD2 1 
ATOM   611  C  CE1 . PHE A 1 132 ? 10.664 -2.810  1.842   1.00 30.26  ? 152  PHE A CE1 1 
ATOM   612  C  CE2 . PHE A 1 132 ? 11.793 -1.035  2.968   1.00 27.13  ? 152  PHE A CE2 1 
ATOM   613  C  CZ  . PHE A 1 132 ? 10.693 -1.507  2.285   1.00 28.06  ? 152  PHE A CZ  1 
ATOM   614  N  N   . ALA A 1 133 ? 16.225 -2.251  1.792   1.00 34.89  ? 153  ALA A N   1 
ATOM   615  C  CA  . ALA A 1 133 ? 16.686 -0.985  1.231   1.00 28.37  ? 153  ALA A CA  1 
ATOM   616  C  C   . ALA A 1 133 ? 17.375 -1.200  -0.109  1.00 33.11  ? 153  ALA A C   1 
ATOM   617  O  O   . ALA A 1 133 ? 17.187 -0.417  -1.046  1.00 35.44  ? 153  ALA A O   1 
ATOM   618  C  CB  . ALA A 1 133 ? 17.624 -0.288  2.214   1.00 34.73  ? 153  ALA A CB  1 
ATOM   619  N  N   . ALA A 1 134 ? 18.185 -2.256  -0.214  1.00 43.13  ? 154  ALA A N   1 
ATOM   620  C  CA  . ALA A 1 134 ? 18.874 -2.547  -1.467  1.00 43.60  ? 154  ALA A CA  1 
ATOM   621  C  C   . ALA A 1 134 ? 17.914 -3.015  -2.550  1.00 32.02  ? 154  ALA A C   1 
ATOM   622  O  O   . ALA A 1 134 ? 18.217 -2.878  -3.740  1.00 38.85  ? 154  ALA A O   1 
ATOM   623  C  CB  . ALA A 1 134 ? 19.953 -3.603  -1.239  1.00 52.68  ? 154  ALA A CB  1 
ATOM   624  N  N   . SER A 1 135 ? 16.767 -3.581  -2.166  1.00 42.26  ? 155  SER A N   1 
ATOM   625  C  CA  . SER A 1 135 ? 15.780 -4.010  -3.151  1.00 41.22  ? 155  SER A CA  1 
ATOM   626  C  C   . SER A 1 135 ? 14.950 -2.833  -3.648  1.00 21.64  ? 155  SER A C   1 
ATOM   627  O  O   . SER A 1 135 ? 14.814 -2.626  -4.858  1.00 19.95  ? 155  SER A O   1 
ATOM   628  C  CB  . SER A 1 135 ? 14.873 -5.083  -2.549  1.00 39.62  ? 155  SER A CB  1 
ATOM   629  O  OG  . SER A 1 135 ? 14.101 -4.551  -1.488  1.00 42.58  ? 155  SER A OG  1 
ATOM   630  N  N   . VAL A 1 136 ? 14.394 -2.044  -2.728  1.00 30.97  ? 156  VAL A N   1 
ATOM   631  C  CA  . VAL A 1 136 ? 13.588 -0.900  -3.139  1.00 29.84  ? 156  VAL A CA  1 
ATOM   632  C  C   . VAL A 1 136 ? 14.448 0.114   -3.879  1.00 30.14  ? 156  VAL A C   1 
ATOM   633  O  O   . VAL A 1 136 ? 14.052 0.633   -4.929  1.00 32.46  ? 156  VAL A O   1 
ATOM   634  C  CB  . VAL A 1 136 ? 12.886 -0.272  -1.919  1.00 30.94  ? 156  VAL A CB  1 
ATOM   635  C  CG1 . VAL A 1 136 ? 13.884 0.426   -1.006  1.00 35.63  ? 156  VAL A CG1 1 
ATOM   636  C  CG2 . VAL A 1 136 ? 11.807 0.699   -2.368  1.00 26.01  ? 156  VAL A CG2 1 
ATOM   637  N  N   . SER A 1 137 ? 15.647 0.391   -3.365  1.00 32.07  ? 157  SER A N   1 
ATOM   638  C  CA  . SER A 1 137 ? 16.497 1.400   -3.986  1.00 31.34  ? 157  SER A CA  1 
ATOM   639  C  C   . SER A 1 137 ? 16.812 1.031   -5.431  1.00 34.93  ? 157  SER A C   1 
ATOM   640  O  O   . SER A 1 137 ? 16.623 1.840   -6.346  1.00 38.79  ? 157  SER A O   1 
ATOM   641  C  CB  . SER A 1 137 ? 17.783 1.563   -3.175  1.00 41.93  ? 157  SER A CB  1 
ATOM   642  O  OG  . SER A 1 137 ? 18.622 2.556   -3.739  1.00 49.61  ? 157  SER A OG  1 
ATOM   643  N  N   . SER A 1 138 ? 17.277 -0.199  -5.658  1.00 34.35  ? 158  SER A N   1 
ATOM   644  C  CA  . SER A 1 138 ? 17.599 -0.618  -7.019  1.00 29.74  ? 158  SER A CA  1 
ATOM   645  C  C   . SER A 1 138 ? 16.347 -0.672  -7.885  1.00 32.57  ? 158  SER A C   1 
ATOM   646  O  O   . SER A 1 138 ? 16.404 -0.382  -9.086  1.00 29.27  ? 158  SER A O   1 
ATOM   647  C  CB  . SER A 1 138 ? 18.300 -1.976  -7.003  1.00 33.43  ? 158  SER A CB  1 
ATOM   648  O  OG  . SER A 1 138 ? 17.436 -2.998  -6.539  1.00 53.57  ? 158  SER A OG  1 
ATOM   649  N  N   . LEU A 1 139 ? 15.208 -1.044  -7.297  1.00 23.20  ? 159  LEU A N   1 
ATOM   650  C  CA  . LEU A 1 139 ? 13.966 -1.078  -8.061  1.00 21.86  ? 159  LEU A CA  1 
ATOM   651  C  C   . LEU A 1 139 ? 13.635 0.302   -8.611  1.00 26.59  ? 159  LEU A C   1 
ATOM   652  O  O   . LEU A 1 139 ? 13.153 0.430   -9.742  1.00 31.38  ? 159  LEU A O   1 
ATOM   653  C  CB  . LEU A 1 139 ? 12.828 -1.604  -7.186  1.00 31.61  ? 159  LEU A CB  1 
ATOM   654  C  CG  . LEU A 1 139 ? 11.609 -2.186  -7.908  1.00 30.27  ? 159  LEU A CG  1 
ATOM   655  C  CD1 . LEU A 1 139 ? 12.008 -3.340  -8.800  1.00 33.74  ? 159  LEU A CD1 1 
ATOM   656  C  CD2 . LEU A 1 139 ? 10.555 -2.648  -6.914  1.00 28.55  ? 159  LEU A CD2 1 
ATOM   657  N  N   . LEU A 1 140 ? 13.883 1.348   -7.822  1.00 29.22  ? 160  LEU A N   1 
ATOM   658  C  CA  . LEU A 1 140 ? 13.783 2.704   -8.350  1.00 23.73  ? 160  LEU A CA  1 
ATOM   659  C  C   . LEU A 1 140 ? 14.795 2.922   -9.466  1.00 26.91  ? 160  LEU A C   1 
ATOM   660  O  O   . LEU A 1 140 ? 14.478 3.534   -10.493 1.00 29.05  ? 160  LEU A O   1 
ATOM   661  C  CB  . LEU A 1 140 ? 14.000 3.716   -7.223  1.00 23.71  ? 160  LEU A CB  1 
ATOM   662  C  CG  . LEU A 1 140 ? 14.090 5.198   -7.594  1.00 21.02  ? 160  LEU A CG  1 
ATOM   663  C  CD1 . LEU A 1 140 ? 12.733 5.760   -7.963  1.00 24.64  ? 160  LEU A CD1 1 
ATOM   664  C  CD2 . LEU A 1 140 ? 14.692 5.983   -6.447  1.00 25.84  ? 160  LEU A CD2 1 
ATOM   665  N  N   . ALA A 1 141 ? 16.016 2.411   -9.288  1.00 31.03  ? 161  ALA A N   1 
ATOM   666  C  CA  . ALA A 1 141 ? 17.074 2.644   -10.266 1.00 25.53  ? 161  ALA A CA  1 
ATOM   667  C  C   . ALA A 1 141 ? 16.706 2.075   -11.628 1.00 28.71  ? 161  ALA A C   1 
ATOM   668  O  O   . ALA A 1 141 ? 17.023 2.670   -12.664 1.00 32.12  ? 161  ALA A O   1 
ATOM   669  C  CB  . ALA A 1 141 ? 18.385 2.036   -9.769  1.00 26.84  ? 161  ALA A CB  1 
ATOM   670  N  N   . ILE A 1 142 ? 16.043 0.918   -11.651 1.00 26.06  ? 162  ILE A N   1 
ATOM   671  C  CA  . ILE A 1 142 ? 15.634 0.340   -12.926 1.00 23.82  ? 162  ILE A CA  1 
ATOM   672  C  C   . ILE A 1 142 ? 14.627 1.245   -13.621 1.00 21.30  ? 162  ILE A C   1 
ATOM   673  O  O   . ILE A 1 142 ? 14.557 1.276   -14.856 1.00 21.21  ? 162  ILE A O   1 
ATOM   674  C  CB  . ILE A 1 142 ? 15.073 -1.080  -12.710 1.00 31.98  ? 162  ILE A CB  1 
ATOM   675  C  CG1 . ILE A 1 142 ? 16.107 -1.956  -11.995 1.00 30.06  ? 162  ILE A CG1 1 
ATOM   676  C  CG2 . ILE A 1 142 ? 14.682 -1.709  -14.045 1.00 39.08  ? 162  ILE A CG2 1 
ATOM   677  C  CD1 . ILE A 1 142 ? 15.599 -3.327  -11.615 1.00 27.80  ? 162  ILE A CD1 1 
ATOM   678  N  N   . THR A 1 143 ? 13.836 1.996   -12.851 1.00 26.23  ? 163  THR A N   1 
ATOM   679  C  CA  . THR A 1 143 ? 12.817 2.856   -13.449 1.00 29.19  ? 163  THR A CA  1 
ATOM   680  C  C   . THR A 1 143 ? 13.445 4.016   -14.213 1.00 32.30  ? 163  THR A C   1 
ATOM   681  O  O   . THR A 1 143 ? 13.079 4.282   -15.365 1.00 37.53  ? 163  THR A O   1 
ATOM   682  C  CB  . THR A 1 143 ? 11.871 3.382   -12.369 1.00 25.05  ? 163  THR A CB  1 
ATOM   683  O  OG1 . THR A 1 143 ? 11.197 2.286   -11.741 1.00 25.78  ? 163  THR A OG1 1 
ATOM   684  C  CG2 . THR A 1 143 ? 10.841 4.319   -12.974 1.00 28.81  ? 163  THR A CG2 1 
ATOM   685  N  N   . VAL A 1 144 ? 14.392 4.724   -13.591 1.00 28.08  ? 164  VAL A N   1 
ATOM   686  C  CA  . VAL A 1 144 ? 15.029 5.846   -14.274 1.00 31.25  ? 164  VAL A CA  1 
ATOM   687  C  C   . VAL A 1 144 ? 15.782 5.364   -15.499 1.00 27.59  ? 164  VAL A C   1 
ATOM   688  O  O   . VAL A 1 144 ? 15.815 6.050   -16.527 1.00 34.08  ? 164  VAL A O   1 
ATOM   689  C  CB  . VAL A 1 144 ? 15.950 6.620   -13.312 1.00 36.21  ? 164  VAL A CB  1 
ATOM   690  C  CG1 . VAL A 1 144 ? 15.153 7.154   -12.137 1.00 36.37  ? 164  VAL A CG1 1 
ATOM   691  C  CG2 . VAL A 1 144 ? 17.085 5.742   -12.825 1.00 33.75  ? 164  VAL A CG2 1 
ATOM   692  N  N   . ASP A 1 145 ? 16.389 4.179   -15.422 1.00 30.93  ? 165  ASP A N   1 
ATOM   693  C  CA  . ASP A 1 145 ? 17.052 3.629   -16.598 1.00 34.98  ? 165  ASP A CA  1 
ATOM   694  C  C   . ASP A 1 145 ? 16.059 3.436   -17.732 1.00 34.83  ? 165  ASP A C   1 
ATOM   695  O  O   . ASP A 1 145 ? 16.356 3.752   -18.890 1.00 40.58  ? 165  ASP A O   1 
ATOM   696  C  CB  . ASP A 1 145 ? 17.727 2.304   -16.249 1.00 35.63  ? 165  ASP A CB  1 
ATOM   697  C  CG  . ASP A 1 145 ? 18.657 1.821   -17.339 1.00 41.39  ? 165  ASP A CG  1 
ATOM   698  O  OD1 . ASP A 1 145 ? 19.668 2.512   -17.599 1.00 37.46  ? 165  ASP A OD1 1 
ATOM   699  O  OD2 . ASP A 1 145 ? 18.380 0.753   -17.933 1.00 52.07  ? 165  ASP A OD2 1 
ATOM   700  N  N   . ARG A 1 146 ? 14.869 2.925   -17.418 1.00 34.28  ? 166  ARG A N   1 
ATOM   701  C  CA  . ARG A 1 146 ? 13.843 2.774   -18.441 1.00 34.56  ? 166  ARG A CA  1 
ATOM   702  C  C   . ARG A 1 146 ? 13.394 4.132   -18.963 1.00 39.45  ? 166  ARG A C   1 
ATOM   703  O  O   . ARG A 1 146 ? 13.306 4.346   -20.178 1.00 43.62  ? 166  ARG A O   1 
ATOM   704  C  CB  . ARG A 1 146 ? 12.654 2.002   -17.878 1.00 32.82  ? 166  ARG A CB  1 
ATOM   705  C  CG  . ARG A 1 146 ? 11.638 1.604   -18.932 1.00 43.40  ? 166  ARG A CG  1 
ATOM   706  C  CD  . ARG A 1 146 ? 12.135 0.444   -19.769 1.00 42.21  ? 166  ARG A CD  1 
ATOM   707  N  NE  . ARG A 1 146 ? 12.318 -0.757  -18.966 1.00 50.02  ? 166  ARG A NE  1 
ATOM   708  C  CZ  . ARG A 1 146 ? 12.582 -1.957  -19.462 1.00 55.49  ? 166  ARG A CZ  1 
ATOM   709  N  NH1 . ARG A 1 146 ? 12.713 -2.152  -20.764 1.00 52.75  ? 166  ARG A NH1 1 
ATOM   710  N  NH2 . ARG A 1 146 ? 12.709 -2.988  -18.632 1.00 62.77  ? 166  ARG A NH2 1 
ATOM   711  N  N   . TYR A 1 147 ? 13.107 5.068   -18.057 1.00 35.58  ? 167  TYR A N   1 
ATOM   712  C  CA  . TYR A 1 147 ? 12.667 6.390   -18.483 1.00 29.11  ? 167  TYR A CA  1 
ATOM   713  C  C   . TYR A 1 147 ? 13.753 7.083   -19.292 1.00 36.06  ? 167  TYR A C   1 
ATOM   714  O  O   . TYR A 1 147 ? 13.504 7.571   -20.399 1.00 42.54  ? 167  TYR A O   1 
ATOM   715  C  CB  . TYR A 1 147 ? 12.279 7.231   -17.268 1.00 23.65  ? 167  TYR A CB  1 
ATOM   716  C  CG  . TYR A 1 147 ? 12.085 8.692   -17.590 1.00 30.06  ? 167  TYR A CG  1 
ATOM   717  C  CD1 . TYR A 1 147 ? 10.943 9.134   -18.243 1.00 36.40  ? 167  TYR A CD1 1 
ATOM   718  C  CD2 . TYR A 1 147 ? 13.045 9.632   -17.241 1.00 32.49  ? 167  TYR A CD2 1 
ATOM   719  C  CE1 . TYR A 1 147 ? 10.764 10.471  -18.541 1.00 41.26  ? 167  TYR A CE1 1 
ATOM   720  C  CE2 . TYR A 1 147 ? 12.875 10.971  -17.534 1.00 35.32  ? 167  TYR A CE2 1 
ATOM   721  C  CZ  . TYR A 1 147 ? 11.734 11.385  -18.184 1.00 40.19  ? 167  TYR A CZ  1 
ATOM   722  O  OH  . TYR A 1 147 ? 11.562 12.719  -18.476 1.00 41.17  ? 167  TYR A OH  1 
ATOM   723  N  N   . LEU A 1 148 ? 14.975 7.117   -18.759 1.00 32.58  ? 168  LEU A N   1 
ATOM   724  C  CA  . LEU A 1 148 ? 16.063 7.793   -19.456 1.00 36.39  ? 168  LEU A CA  1 
ATOM   725  C  C   . LEU A 1 148 ? 16.360 7.123   -20.790 1.00 39.93  ? 168  LEU A C   1 
ATOM   726  O  O   . LEU A 1 148 ? 16.590 7.803   -21.797 1.00 47.29  ? 168  LEU A O   1 
ATOM   727  C  CB  . LEU A 1 148 ? 17.312 7.814   -18.577 1.00 35.83  ? 168  LEU A CB  1 
ATOM   728  C  CG  . LEU A 1 148 ? 17.190 8.643   -17.299 1.00 25.66  ? 168  LEU A CG  1 
ATOM   729  C  CD1 . LEU A 1 148 ? 18.415 8.450   -16.432 1.00 38.85  ? 168  LEU A CD1 1 
ATOM   730  C  CD2 . LEU A 1 148 ? 16.994 10.110  -17.631 1.00 28.16  ? 168  LEU A CD2 1 
ATOM   731  N  N   . SER A 1 149 ? 16.359 5.790   -20.817 1.00 35.48  ? 169  SER A N   1 
ATOM   732  C  CA  . SER A 1 149 ? 16.608 5.083   -22.068 1.00 45.78  ? 169  SER A CA  1 
ATOM   733  C  C   . SER A 1 149 ? 15.540 5.415   -23.100 1.00 54.37  ? 169  SER A C   1 
ATOM   734  O  O   . SER A 1 149 ? 15.847 5.668   -24.269 1.00 56.80  ? 169  SER A O   1 
ATOM   735  C  CB  . SER A 1 149 ? 16.663 3.576   -21.815 1.00 47.32  ? 169  SER A CB  1 
ATOM   736  O  OG  . SER A 1 149 ? 15.427 3.101   -21.311 1.00 44.45  ? 169  SER A OG  1 
ATOM   737  N  N   . LEU A 1 150 ? 14.274 5.421   -22.682 1.00 54.44  ? 170  LEU A N   1 
ATOM   738  C  CA  . LEU A 1 150 ? 13.189 5.733   -23.603 1.00 53.87  ? 170  LEU A CA  1 
ATOM   739  C  C   . LEU A 1 150 ? 13.067 7.228   -23.866 1.00 43.55  ? 170  LEU A C   1 
ATOM   740  O  O   . LEU A 1 150 ? 12.666 7.626   -24.965 1.00 41.99  ? 170  LEU A O   1 
ATOM   741  C  CB  . LEU A 1 150 ? 11.870 5.186   -23.056 1.00 55.24  ? 170  LEU A CB  1 
ATOM   742  C  CG  . LEU A 1 150 ? 11.816 3.666   -22.891 1.00 45.58  ? 170  LEU A CG  1 
ATOM   743  C  CD1 . LEU A 1 150 ? 10.530 3.250   -22.198 1.00 38.93  ? 170  LEU A CD1 1 
ATOM   744  C  CD2 . LEU A 1 150 ? 11.952 2.969   -24.238 1.00 41.30  ? 170  LEU A CD2 1 
ATOM   745  N  N   . TYR A 1 151 ? 13.406 8.065   -22.884 1.00 42.38  ? 171  TYR A N   1 
ATOM   746  C  CA  . TYR A 1 151 ? 13.203 9.502   -23.033 1.00 45.19  ? 171  TYR A CA  1 
ATOM   747  C  C   . TYR A 1 151 ? 13.962 10.045  -24.237 1.00 48.72  ? 171  TYR A C   1 
ATOM   748  O  O   . TYR A 1 151 ? 13.401 10.772  -25.065 1.00 51.52  ? 171  TYR A O   1 
ATOM   749  C  CB  . TYR A 1 151 ? 13.634 10.226  -21.758 1.00 43.32  ? 171  TYR A CB  1 
ATOM   750  C  CG  . TYR A 1 151 ? 13.382 11.713  -21.798 1.00 42.04  ? 171  TYR A CG  1 
ATOM   751  C  CD1 . TYR A 1 151 ? 12.165 12.237  -21.390 1.00 46.84  ? 171  TYR A CD1 1 
ATOM   752  C  CD2 . TYR A 1 151 ? 14.356 12.592  -22.251 1.00 44.74  ? 171  TYR A CD2 1 
ATOM   753  C  CE1 . TYR A 1 151 ? 11.924 13.594  -21.426 1.00 51.97  ? 171  TYR A CE1 1 
ATOM   754  C  CE2 . TYR A 1 151 ? 14.124 13.953  -22.291 1.00 43.86  ? 171  TYR A CE2 1 
ATOM   755  C  CZ  . TYR A 1 151 ? 12.905 14.448  -21.877 1.00 40.10  ? 171  TYR A CZ  1 
ATOM   756  O  OH  . TYR A 1 151 ? 12.658 15.800  -21.911 1.00 39.04  ? 171  TYR A OH  1 
ATOM   757  N  N   . ASN A 1 152 ? 15.240 9.708   -24.348 1.00 57.57  ? 172  ASN A N   1 
ATOM   758  C  CA  . ASN A 1 152 ? 16.045 10.171  -25.468 1.00 73.96  ? 172  ASN A CA  1 
ATOM   759  C  C   . ASN A 1 152 ? 17.259 9.260   -25.609 1.00 72.01  ? 172  ASN A C   1 
ATOM   760  O  O   . ASN A 1 152 ? 18.321 9.545   -25.039 1.00 70.99  ? 172  ASN A O   1 
ATOM   761  C  CB  . ASN A 1 152 ? 16.461 11.628  -25.261 1.00 83.69  ? 172  ASN A CB  1 
ATOM   762  C  CG  . ASN A 1 152 ? 16.619 12.382  -26.565 1.00 80.13  ? 172  ASN A CG  1 
ATOM   763  O  OD1 . ASN A 1 152 ? 16.795 11.784  -27.626 1.00 77.60  ? 172  ASN A OD1 1 
ATOM   764  N  ND2 . ASN A 1 152 ? 16.553 13.706  -26.493 1.00 73.04  ? 172  ASN A ND2 1 
ATOM   765  N  N   . PRO A 1 153 ? 17.142 8.152   -26.345 1.00 67.17  ? 173  PRO A N   1 
ATOM   766  C  CA  . PRO A 1 153 ? 18.258 7.195   -26.396 1.00 70.25  ? 173  PRO A CA  1 
ATOM   767  C  C   . PRO A 1 153 ? 19.558 7.798   -26.897 1.00 70.72  ? 173  PRO A C   1 
ATOM   768  O  O   . PRO A 1 153 ? 20.634 7.353   -26.479 1.00 72.25  ? 173  PRO A O   1 
ATOM   769  C  CB  . PRO A 1 153 ? 17.741 6.102   -27.341 1.00 81.49  ? 173  PRO A CB  1 
ATOM   770  C  CG  . PRO A 1 153 ? 16.263 6.206   -27.280 1.00 64.53  ? 173  PRO A CG  1 
ATOM   771  C  CD  . PRO A 1 153 ? 15.957 7.659   -27.066 1.00 63.30  ? 173  PRO A CD  1 
ATOM   772  N  N   . LEU A 1 154 ? 19.499 8.793   -27.786 1.00 70.43  ? 174  LEU A N   1 
ATOM   773  C  CA  . LEU A 1 154 ? 20.731 9.415   -28.260 1.00 68.88  ? 174  LEU A CA  1 
ATOM   774  C  C   . LEU A 1 154 ? 21.475 10.084  -27.113 1.00 66.28  ? 174  LEU A C   1 
ATOM   775  O  O   . LEU A 1 154 ? 22.703 9.984   -27.017 1.00 66.27  ? 174  LEU A O   1 
ATOM   776  C  CB  . LEU A 1 154 ? 20.421 10.421  -29.369 1.00 72.59  ? 174  LEU A CB  1 
ATOM   777  C  CG  . LEU A 1 154 ? 19.556 11.622  -28.985 1.00 77.77  ? 174  LEU A CG  1 
ATOM   778  C  CD1 . LEU A 1 154 ? 20.421 12.840  -28.683 1.00 74.63  ? 174  LEU A CD1 1 
ATOM   779  C  CD2 . LEU A 1 154 ? 18.555 11.929  -30.089 1.00 83.03  ? 174  LEU A CD2 1 
ATOM   780  N  N   . THR A 1 155 ? 20.747 10.769  -26.229 1.00 64.72  ? 175  THR A N   1 
ATOM   781  C  CA  . THR A 1 155 ? 21.368 11.290  -25.019 1.00 62.62  ? 175  THR A CA  1 
ATOM   782  C  C   . THR A 1 155 ? 21.685 10.175  -24.036 1.00 64.63  ? 175  THR A C   1 
ATOM   783  O  O   . THR A 1 155 ? 22.534 10.357  -23.158 1.00 64.95  ? 175  THR A O   1 
ATOM   784  C  CB  . THR A 1 155 ? 20.461 12.324  -24.351 1.00 62.78  ? 175  THR A CB  1 
ATOM   785  O  OG1 . THR A 1 155 ? 19.375 11.659  -23.694 1.00 62.75  ? 175  THR A OG1 1 
ATOM   786  C  CG2 . THR A 1 155 ? 19.912 13.302  -25.382 1.00 66.01  ? 175  THR A CG2 1 
ATOM   787  N  N   . TYR A 1 156 ? 21.028 9.023   -24.176 1.00 64.69  ? 176  TYR A N   1 
ATOM   788  C  CA  . TYR A 1 156 ? 21.325 7.841   -23.369 1.00 63.51  ? 176  TYR A CA  1 
ATOM   789  C  C   . TYR A 1 156 ? 22.621 7.206   -23.878 1.00 61.56  ? 176  TYR A C   1 
ATOM   790  O  O   . TYR A 1 156 ? 22.662 6.065   -24.340 1.00 57.21  ? 176  TYR A O   1 
ATOM   791  C  CB  . TYR A 1 156 ? 20.152 6.870   -23.428 1.00 56.27  ? 176  TYR A CB  1 
ATOM   792  C  CG  . TYR A 1 156 ? 20.209 5.701   -22.466 1.00 46.05  ? 176  TYR A CG  1 
ATOM   793  C  CD1 . TYR A 1 156 ? 19.777 5.831   -21.152 1.00 47.89  ? 176  TYR A CD1 1 
ATOM   794  C  CD2 . TYR A 1 156 ? 20.663 4.458   -22.884 1.00 48.40  ? 176  TYR A CD2 1 
ATOM   795  C  CE1 . TYR A 1 156 ? 19.815 4.760   -20.278 1.00 46.71  ? 176  TYR A CE1 1 
ATOM   796  C  CE2 . TYR A 1 156 ? 20.704 3.384   -22.017 1.00 56.09  ? 176  TYR A CE2 1 
ATOM   797  C  CZ  . TYR A 1 156 ? 20.277 3.540   -20.717 1.00 44.17  ? 176  TYR A CZ  1 
ATOM   798  O  OH  . TYR A 1 156 ? 20.317 2.476   -19.848 1.00 35.72  ? 176  TYR A OH  1 
ATOM   799  N  N   . TYR A 1 157 ? 23.690 7.994   -23.804 1.00 75.81  ? 177  TYR A N   1 
ATOM   800  C  CA  . TYR A 1 157 ? 24.978 7.596   -24.341 1.00 86.70  ? 177  TYR A CA  1 
ATOM   801  C  C   . TYR A 1 157 ? 25.699 6.658   -23.379 1.00 82.52  ? 177  TYR A C   1 
ATOM   802  O  O   . TYR A 1 157 ? 25.364 6.551   -22.196 1.00 81.87  ? 177  TYR A O   1 
ATOM   803  C  CB  . TYR A 1 157 ? 25.844 8.824   -24.620 1.00 67.98  ? 177  TYR A CB  1 
ATOM   804  N  N   . SER A 1 158 ? 26.712 5.974   -23.911 1.00 94.41  ? 178  SER A N   1 
ATOM   805  C  CA  . SER A 1 158 ? 27.489 5.028   -23.122 1.00 106.75 ? 178  SER A CA  1 
ATOM   806  C  C   . SER A 1 158 ? 28.346 5.707   -22.062 1.00 103.83 ? 178  SER A C   1 
ATOM   807  O  O   . SER A 1 158 ? 28.880 5.015   -21.188 1.00 103.81 ? 178  SER A O   1 
ATOM   808  C  CB  . SER A 1 158 ? 28.378 4.192   -24.045 1.00 110.81 ? 178  SER A CB  1 
ATOM   809  O  OG  . SER A 1 158 ? 27.598 3.472   -24.984 1.00 111.87 ? 178  SER A OG  1 
ATOM   810  N  N   . ARG A 1 159 ? 28.488 7.031   -22.108 1.00 88.61  ? 179  ARG A N   1 
ATOM   811  C  CA  . ARG A 1 159 ? 29.312 7.742   -21.134 1.00 90.80  ? 179  ARG A CA  1 
ATOM   812  C  C   . ARG A 1 159 ? 28.489 8.165   -19.920 1.00 83.47  ? 179  ARG A C   1 
ATOM   813  O  O   . ARG A 1 159 ? 28.797 7.777   -18.789 1.00 89.26  ? 179  ARG A O   1 
ATOM   814  C  CB  . ARG A 1 159 ? 29.993 8.954   -21.789 1.00 91.01  ? 179  ARG A CB  1 
ATOM   815  C  CG  . ARG A 1 159 ? 29.116 9.788   -22.722 1.00 87.31  ? 179  ARG A CG  1 
ATOM   816  C  CD  . ARG A 1 159 ? 29.926 10.887  -23.393 1.00 83.78  ? 179  ARG A CD  1 
ATOM   817  N  NE  . ARG A 1 159 ? 29.227 11.476  -24.530 1.00 87.72  ? 179  ARG A NE  1 
ATOM   818  C  CZ  . ARG A 1 159 ? 28.424 12.530  -24.462 1.00 87.17  ? 179  ARG A CZ  1 
ATOM   819  N  NH1 . ARG A 1 159 ? 28.177 13.141  -23.314 1.00 87.03  ? 179  ARG A NH1 1 
ATOM   820  N  NH2 . ARG A 1 159 ? 27.854 12.983  -25.574 1.00 86.26  ? 179  ARG A NH2 1 
ATOM   821  N  N   . ARG A 1 160 ? 27.432 8.948   -20.139 1.00 72.40  ? 180  ARG A N   1 
ATOM   822  C  CA  . ARG A 1 160 ? 26.607 9.381   -19.017 1.00 65.51  ? 180  ARG A CA  1 
ATOM   823  C  C   . ARG A 1 160 ? 25.928 8.195   -18.346 1.00 61.73  ? 180  ARG A C   1 
ATOM   824  O  O   . ARG A 1 160 ? 25.902 8.101   -17.113 1.00 59.61  ? 180  ARG A O   1 
ATOM   825  C  CB  . ARG A 1 160 ? 25.566 10.397  -19.493 1.00 75.17  ? 180  ARG A CB  1 
ATOM   826  C  CG  . ARG A 1 160 ? 26.135 11.781  -19.773 1.00 83.11  ? 180  ARG A CG  1 
ATOM   827  C  CD  . ARG A 1 160 ? 26.529 12.500  -18.485 1.00 80.35  ? 180  ARG A CD  1 
ATOM   828  N  NE  . ARG A 1 160 ? 25.384 13.120  -17.826 1.00 61.74  ? 180  ARG A NE  1 
ATOM   829  C  CZ  . ARG A 1 160 ? 25.332 14.381  -17.415 1.00 68.91  ? 180  ARG A CZ  1 
ATOM   830  N  NH1 . ARG A 1 160 ? 26.370 15.196  -17.534 1.00 57.26  ? 180  ARG A NH1 1 
ATOM   831  N  NH2 . ARG A 1 160 ? 24.212 14.836  -16.861 1.00 62.31  ? 180  ARG A NH2 1 
ATOM   832  N  N   . THR A 1 161 ? 25.384 7.274   -19.139 1.00 75.93  ? 181  THR A N   1 
ATOM   833  C  CA  . THR A 1 161 ? 24.657 6.143   -18.573 1.00 75.56  ? 181  THR A CA  1 
ATOM   834  C  C   . THR A 1 161 ? 25.580 5.264   -17.736 1.00 73.84  ? 181  THR A C   1 
ATOM   835  O  O   . THR A 1 161 ? 25.397 5.126   -16.522 1.00 72.83  ? 181  THR A O   1 
ATOM   836  C  CB  . THR A 1 161 ? 24.003 5.332   -19.692 1.00 71.13  ? 181  THR A CB  1 
ATOM   837  O  OG1 . THR A 1 161 ? 25.008 4.864   -20.600 1.00 88.70  ? 181  THR A OG1 1 
ATOM   838  C  CG2 . THR A 1 161 ? 22.995 6.183   -20.445 1.00 64.36  ? 181  THR A CG2 1 
ATOM   839  N  N   . LEU A 1 162 ? 26.595 4.672   -18.372 1.00 64.68  ? 182  LEU A N   1 
ATOM   840  C  CA  . LEU A 1 162 ? 27.482 3.764   -17.650 1.00 64.48  ? 182  LEU A CA  1 
ATOM   841  C  C   . LEU A 1 162 ? 28.123 4.447   -16.453 1.00 59.71  ? 182  LEU A C   1 
ATOM   842  O  O   . LEU A 1 162 ? 28.394 3.796   -15.437 1.00 52.06  ? 182  LEU A O   1 
ATOM   843  C  CB  . LEU A 1 162 ? 28.564 3.221   -18.583 1.00 61.93  ? 182  LEU A CB  1 
ATOM   844  C  CG  . LEU A 1 162 ? 28.153 2.090   -19.529 1.00 80.31  ? 182  LEU A CG  1 
ATOM   845  C  CD1 . LEU A 1 162 ? 27.897 0.800   -18.758 1.00 83.61  ? 182  LEU A CD1 1 
ATOM   846  C  CD2 . LEU A 1 162 ? 26.929 2.475   -20.344 1.00 72.39  ? 182  LEU A CD2 1 
ATOM   847  N  N   . LEU A 1 163 ? 28.387 5.749   -16.554 1.00 54.41  ? 183  LEU A N   1 
ATOM   848  C  CA  . LEU A 1 163 ? 28.840 6.489   -15.386 1.00 53.86  ? 183  LEU A CA  1 
ATOM   849  C  C   . LEU A 1 163 ? 27.779 6.465   -14.296 1.00 58.33  ? 183  LEU A C   1 
ATOM   850  O  O   . LEU A 1 163 ? 28.048 6.061   -13.159 1.00 60.81  ? 183  LEU A O   1 
ATOM   851  C  CB  . LEU A 1 163 ? 29.180 7.925   -15.781 1.00 74.05  ? 183  LEU A CB  1 
ATOM   852  C  CG  . LEU A 1 163 ? 29.417 8.901   -14.627 1.00 77.88  ? 183  LEU A CG  1 
ATOM   853  C  CD1 . LEU A 1 163 ? 30.516 8.389   -13.711 1.00 66.49  ? 183  LEU A CD1 1 
ATOM   854  C  CD2 . LEU A 1 163 ? 29.752 10.289  -15.159 1.00 71.05  ? 183  LEU A CD2 1 
ATOM   855  N  N   . GLY A 1 164 ? 26.550 6.858   -14.639 1.00 61.93  ? 184  GLY A N   1 
ATOM   856  C  CA  . GLY A 1 164 ? 25.490 6.905   -13.647 1.00 53.68  ? 184  GLY A CA  1 
ATOM   857  C  C   . GLY A 1 164 ? 25.135 5.543   -13.088 1.00 46.86  ? 184  GLY A C   1 
ATOM   858  O  O   . GLY A 1 164 ? 24.737 5.430   -11.927 1.00 48.90  ? 184  GLY A O   1 
ATOM   859  N  N   . VAL A 1 165 ? 25.274 4.494   -13.900 1.00 54.09  ? 185  VAL A N   1 
ATOM   860  C  CA  . VAL A 1 165 ? 24.914 3.152   -13.451 1.00 51.16  ? 185  VAL A CA  1 
ATOM   861  C  C   . VAL A 1 165 ? 25.766 2.742   -12.256 1.00 53.19  ? 185  VAL A C   1 
ATOM   862  O  O   . VAL A 1 165 ? 25.257 2.224   -11.256 1.00 47.00  ? 185  VAL A O   1 
ATOM   863  C  CB  . VAL A 1 165 ? 25.051 2.151   -14.611 1.00 65.96  ? 185  VAL A CB  1 
ATOM   864  C  CG1 . VAL A 1 165 ? 24.851 0.728   -14.116 1.00 66.34  ? 185  VAL A CG1 1 
ATOM   865  C  CG2 . VAL A 1 165 ? 24.057 2.484   -15.707 1.00 64.81  ? 185  VAL A CG2 1 
ATOM   866  N  N   . HIS A 1 166 ? 27.079 2.965   -12.342 1.00 57.19  ? 186  HIS A N   1 
ATOM   867  C  CA  . HIS A 1 166 ? 27.953 2.610   -11.230 1.00 55.43  ? 186  HIS A CA  1 
ATOM   868  C  C   . HIS A 1 166 ? 27.631 3.427   -9.988  1.00 50.52  ? 186  HIS A C   1 
ATOM   869  O  O   . HIS A 1 166 ? 27.746 2.921   -8.866  1.00 54.96  ? 186  HIS A O   1 
ATOM   870  C  CB  . HIS A 1 166 ? 29.417 2.794   -11.631 1.00 58.45  ? 186  HIS A CB  1 
ATOM   871  C  CG  . HIS A 1 166 ? 29.987 1.628   -12.376 1.00 57.26  ? 186  HIS A CG  1 
ATOM   872  N  ND1 . HIS A 1 166 ? 30.693 0.621   -11.753 1.00 60.71  ? 186  HIS A ND1 1 
ATOM   873  C  CD2 . HIS A 1 166 ? 29.948 1.302   -13.690 1.00 64.98  ? 186  HIS A CD2 1 
ATOM   874  C  CE1 . HIS A 1 166 ? 31.070 -0.271  -12.651 1.00 66.60  ? 186  HIS A CE1 1 
ATOM   875  N  NE2 . HIS A 1 166 ? 30.631 0.118   -13.835 1.00 70.01  ? 186  HIS A NE2 1 
ATOM   876  N  N   . LEU A 1 167 ? 27.234 4.690   -10.162 1.00 52.80  ? 187  LEU A N   1 
ATOM   877  C  CA  . LEU A 1 167 ? 26.824 5.497   -9.017  1.00 54.47  ? 187  LEU A CA  1 
ATOM   878  C  C   . LEU A 1 167 ? 25.489 5.031   -8.447  1.00 58.24  ? 187  LEU A C   1 
ATOM   879  O  O   . LEU A 1 167 ? 25.284 5.095   -7.229  1.00 56.08  ? 187  LEU A O   1 
ATOM   880  C  CB  . LEU A 1 167 ? 26.740 6.971   -9.409  1.00 52.71  ? 187  LEU A CB  1 
ATOM   881  C  CG  . LEU A 1 167 ? 28.073 7.722   -9.471  1.00 63.24  ? 187  LEU A CG  1 
ATOM   882  C  CD1 . LEU A 1 167 ? 28.860 7.370   -10.727 1.00 68.60  ? 187  LEU A CD1 1 
ATOM   883  C  CD2 . LEU A 1 167 ? 27.843 9.223   -9.389  1.00 72.81  ? 187  LEU A CD2 1 
ATOM   884  N  N   . LEU A 1 168 ? 24.572 4.568   -9.298  1.00 48.60  ? 188  LEU A N   1 
ATOM   885  C  CA  . LEU A 1 168 ? 23.302 4.053   -8.796  1.00 46.27  ? 188  LEU A CA  1 
ATOM   886  C  C   . LEU A 1 168 ? 23.529 2.867   -7.869  1.00 45.02  ? 188  LEU A C   1 
ATOM   887  O  O   . LEU A 1 168 ? 23.002 2.828   -6.751  1.00 52.60  ? 188  LEU A O   1 
ATOM   888  C  CB  . LEU A 1 168 ? 22.394 3.661   -9.963  1.00 42.48  ? 188  LEU A CB  1 
ATOM   889  C  CG  . LEU A 1 168 ? 21.805 4.814   -10.782 1.00 41.21  ? 188  LEU A CG  1 
ATOM   890  C  CD1 . LEU A 1 168 ? 21.014 4.281   -11.966 1.00 33.33  ? 188  LEU A CD1 1 
ATOM   891  C  CD2 . LEU A 1 168 ? 20.931 5.713   -9.920  1.00 41.09  ? 188  LEU A CD2 1 
ATOM   892  N  N   . LEU A 1 169 ? 24.318 1.887   -8.313  1.00 34.64  ? 189  LEU A N   1 
ATOM   893  C  CA  . LEU A 1 169 ? 24.642 0.768   -7.436  1.00 38.35  ? 189  LEU A CA  1 
ATOM   894  C  C   . LEU A 1 169 ? 25.445 1.238   -6.233  1.00 48.50  ? 189  LEU A C   1 
ATOM   895  O  O   . LEU A 1 169 ? 25.160 0.846   -5.096  1.00 46.97  ? 189  LEU A O   1 
ATOM   896  C  CB  . LEU A 1 169 ? 25.415 -0.300  -8.207  1.00 52.24  ? 189  LEU A CB  1 
ATOM   897  C  CG  . LEU A 1 169 ? 24.720 -0.860  -9.447  1.00 51.11  ? 189  LEU A CG  1 
ATOM   898  C  CD1 . LEU A 1 169 ? 25.466 -2.082  -9.958  1.00 36.97  ? 189  LEU A CD1 1 
ATOM   899  C  CD2 . LEU A 1 169 ? 23.266 -1.192  -9.148  1.00 43.97  ? 189  LEU A CD2 1 
ATOM   900  N  N   . ALA A 1 170 ? 26.444 2.093   -6.464  1.00 51.61  ? 190  ALA A N   1 
ATOM   901  C  CA  . ALA A 1 170 ? 27.253 2.601   -5.362  1.00 50.41  ? 190  ALA A CA  1 
ATOM   902  C  C   . ALA A 1 170 ? 26.398 3.392   -4.383  1.00 47.44  ? 190  ALA A C   1 
ATOM   903  O  O   . ALA A 1 170 ? 26.452 3.167   -3.169  1.00 48.43  ? 190  ALA A O   1 
ATOM   904  C  CB  . ALA A 1 170 ? 28.388 3.467   -5.905  1.00 47.62  ? 190  ALA A CB  1 
ATOM   905  N  N   . ALA A 1 171 ? 25.592 4.322   -4.896  1.00 46.41  ? 191  ALA A N   1 
ATOM   906  C  CA  . ALA A 1 171 ? 24.698 5.077   -4.030  1.00 65.85  ? 191  ALA A CA  1 
ATOM   907  C  C   . ALA A 1 171 ? 23.616 4.198   -3.422  1.00 58.60  ? 191  ALA A C   1 
ATOM   908  O  O   . ALA A 1 171 ? 22.987 4.601   -2.438  1.00 42.11  ? 191  ALA A O   1 
ATOM   909  C  CB  . ALA A 1 171 ? 24.054 6.227   -4.805  1.00 55.70  ? 191  ALA A CB  1 
ATOM   910  N  N   . THR A 1 172 ? 23.391 3.008   -3.980  1.00 49.14  ? 192  THR A N   1 
ATOM   911  C  CA  . THR A 1 172 ? 22.370 2.113   -3.450  1.00 46.37  ? 192  THR A CA  1 
ATOM   912  C  C   . THR A 1 172 ? 22.915 1.290   -2.290  1.00 46.09  ? 192  THR A C   1 
ATOM   913  O  O   . THR A 1 172 ? 22.379 1.329   -1.177  1.00 57.46  ? 192  THR A O   1 
ATOM   914  C  CB  . THR A 1 172 ? 21.849 1.195   -4.561  1.00 40.27  ? 192  THR A CB  1 
ATOM   915  O  OG1 . THR A 1 172 ? 21.023 1.946   -5.460  1.00 34.76  ? 192  THR A OG1 1 
ATOM   916  C  CG2 . THR A 1 172 ? 21.046 0.042   -3.981  1.00 42.54  ? 192  THR A CG2 1 
ATOM   917  N  N   . TRP A 1 173 ? 23.991 0.543   -2.532  1.00 42.17  ? 193  TRP A N   1 
ATOM   918  C  CA  . TRP A 1 173 ? 24.488 -0.374  -1.516  1.00 44.84  ? 193  TRP A CA  1 
ATOM   919  C  C   . TRP A 1 173 ? 25.195 0.357   -0.384  1.00 49.82  ? 193  TRP A C   1 
ATOM   920  O  O   . TRP A 1 173 ? 25.162 -0.104  0.762   1.00 51.40  ? 193  TRP A O   1 
ATOM   921  C  CB  . TRP A 1 173 ? 25.415 -1.395  -2.164  1.00 44.91  ? 193  TRP A CB  1 
ATOM   922  C  CG  . TRP A 1 173 ? 24.691 -2.272  -3.112  1.00 44.67  ? 193  TRP A CG  1 
ATOM   923  C  CD1 . TRP A 1 173 ? 24.607 -2.127  -4.464  1.00 48.77  ? 193  TRP A CD1 1 
ATOM   924  C  CD2 . TRP A 1 173 ? 23.918 -3.428  -2.781  1.00 51.92  ? 193  TRP A CD2 1 
ATOM   925  N  NE1 . TRP A 1 173 ? 23.836 -3.131  -4.998  1.00 50.12  ? 193  TRP A NE1 1 
ATOM   926  C  CE2 . TRP A 1 173 ? 23.400 -3.943  -3.984  1.00 45.27  ? 193  TRP A CE2 1 
ATOM   927  C  CE3 . TRP A 1 173 ? 23.618 -4.081  -1.582  1.00 54.20  ? 193  TRP A CE3 1 
ATOM   928  C  CZ2 . TRP A 1 173 ? 22.601 -5.081  -4.023  1.00 49.55  ? 193  TRP A CZ2 1 
ATOM   929  C  CZ3 . TRP A 1 173 ? 22.826 -5.209  -1.623  1.00 49.18  ? 193  TRP A CZ3 1 
ATOM   930  C  CH2 . TRP A 1 173 ? 22.325 -5.699  -2.834  1.00 49.66  ? 193  TRP A CH2 1 
ATOM   931  N  N   . THR A 1 174 ? 25.839 1.489   -0.675  1.00 47.87  ? 194  THR A N   1 
ATOM   932  C  CA  . THR A 1 174 ? 26.447 2.265   0.399   1.00 48.76  ? 194  THR A CA  1 
ATOM   933  C  C   . THR A 1 174 ? 25.394 2.762   1.380   1.00 48.02  ? 194  THR A C   1 
ATOM   934  O  O   . THR A 1 174 ? 25.681 2.929   2.571   1.00 53.89  ? 194  THR A O   1 
ATOM   935  C  CB  . THR A 1 174 ? 27.238 3.443   -0.174  1.00 50.17  ? 194  THR A CB  1 
ATOM   936  O  OG1 . THR A 1 174 ? 26.391 4.234   -1.016  1.00 63.48  ? 194  THR A OG1 1 
ATOM   937  C  CG2 . THR A 1 174 ? 28.432 2.945   -0.976  1.00 55.63  ? 194  THR A CG2 1 
ATOM   938  N  N   . VAL A 1 175 ? 24.173 2.990   0.906   1.00 46.39  ? 195  VAL A N   1 
ATOM   939  C  CA  . VAL A 1 175 ? 23.076 3.392   1.782   1.00 57.13  ? 195  VAL A CA  1 
ATOM   940  C  C   . VAL A 1 175 ? 22.387 2.177   2.385   1.00 59.66  ? 195  VAL A C   1 
ATOM   941  O  O   . VAL A 1 175 ? 22.170 2.110   3.598   1.00 62.75  ? 195  VAL A O   1 
ATOM   942  C  CB  . VAL A 1 175 ? 22.075 4.274   1.004   1.00 50.88  ? 195  VAL A CB  1 
ATOM   943  C  CG1 . VAL A 1 175 ? 20.878 4.615   1.873   1.00 34.84  ? 195  VAL A CG1 1 
ATOM   944  C  CG2 . VAL A 1 175 ? 22.752 5.540   0.509   1.00 42.16  ? 195  VAL A CG2 1 
ATOM   945  N  N   . SER A 1 176 ? 22.049 1.195   1.548   1.00 50.37  ? 196  SER A N   1 
ATOM   946  C  CA  . SER A 1 176 ? 21.332 0.022   2.033   1.00 49.66  ? 196  SER A CA  1 
ATOM   947  C  C   . SER A 1 176 ? 22.099 -0.656  3.160   1.00 59.73  ? 196  SER A C   1 
ATOM   948  O  O   . SER A 1 176 ? 21.536 -0.958  4.219   1.00 67.87  ? 196  SER A O   1 
ATOM   949  C  CB  . SER A 1 176 ? 21.093 -0.951  0.879   1.00 55.69  ? 196  SER A CB  1 
ATOM   950  O  OG  . SER A 1 176 ? 20.402 -0.315  -0.181  1.00 40.96  ? 196  SER A OG  1 
ATOM   951  N  N   . LEU A 1 177 ? 23.394 -0.898  2.953   1.00 58.63  ? 197  LEU A N   1 
ATOM   952  C  CA  . LEU A 1 177 ? 24.215 -1.462  4.017   1.00 53.05  ? 197  LEU A CA  1 
ATOM   953  C  C   . LEU A 1 177 ? 24.284 -0.517  5.208   1.00 53.12  ? 197  LEU A C   1 
ATOM   954  O  O   . LEU A 1 177 ? 24.158 -0.948  6.360   1.00 53.60  ? 197  LEU A O   1 
ATOM   955  C  CB  . LEU A 1 177 ? 25.615 -1.769  3.488   1.00 60.91  ? 197  LEU A CB  1 
ATOM   956  C  CG  . LEU A 1 177 ? 25.698 -2.928  2.491   1.00 64.01  ? 197  LEU A CG  1 
ATOM   957  C  CD1 . LEU A 1 177 ? 26.976 -2.848  1.667   1.00 67.60  ? 197  LEU A CD1 1 
ATOM   958  C  CD2 . LEU A 1 177 ? 25.614 -4.263  3.218   1.00 59.07  ? 197  LEU A CD2 1 
ATOM   959  N  N   . GLY A 1 178 ? 24.460 0.780   4.951   1.00 55.95  ? 198  GLY A N   1 
ATOM   960  C  CA  . GLY A 1 178 ? 24.527 1.732   6.046   1.00 49.09  ? 198  GLY A CA  1 
ATOM   961  C  C   . GLY A 1 178 ? 23.301 1.666   6.934   1.00 54.64  ? 198  GLY A C   1 
ATOM   962  O  O   . GLY A 1 178 ? 23.413 1.642   8.161   1.00 53.12  ? 198  GLY A O   1 
ATOM   963  N  N   . LEU A 1 179 ? 22.114 1.612   6.326   1.00 54.09  ? 199  LEU A N   1 
ATOM   964  C  CA  . LEU A 1 179 ? 20.897 1.442   7.111   1.00 52.47  ? 199  LEU A CA  1 
ATOM   965  C  C   . LEU A 1 179 ? 20.918 0.121   7.867   1.00 52.40  ? 199  LEU A C   1 
ATOM   966  O  O   . LEU A 1 179 ? 20.509 0.055   9.033   1.00 54.53  ? 199  LEU A O   1 
ATOM   967  C  CB  . LEU A 1 179 ? 19.668 1.520   6.204   1.00 51.11  ? 199  LEU A CB  1 
ATOM   968  C  CG  . LEU A 1 179 ? 19.119 2.913   5.876   1.00 47.46  ? 199  LEU A CG  1 
ATOM   969  C  CD1 . LEU A 1 179 ? 18.679 3.630   7.141   1.00 46.03  ? 199  LEU A CD1 1 
ATOM   970  C  CD2 . LEU A 1 179 ? 20.139 3.747   5.117   1.00 45.63  ? 199  LEU A CD2 1 
ATOM   971  N  N   . GLY A 1 180 ? 21.394 -0.945  7.220   1.00 49.10  ? 200  GLY A N   1 
ATOM   972  C  CA  . GLY A 1 180 ? 21.493 -2.231  7.883   1.00 52.97  ? 200  GLY A CA  1 
ATOM   973  C  C   . GLY A 1 180 ? 22.505 -2.261  9.006   1.00 58.63  ? 200  GLY A C   1 
ATOM   974  O  O   . GLY A 1 180 ? 22.408 -3.116  9.893   1.00 58.31  ? 200  GLY A O   1 
ATOM   975  N  N   . LEU A 1 181 ? 23.475 -1.347  8.990   1.00 55.87  ? 201  LEU A N   1 
ATOM   976  C  CA  . LEU A 1 181 ? 24.480 -1.285  10.041  1.00 56.82  ? 201  LEU A CA  1 
ATOM   977  C  C   . LEU A 1 181 ? 24.084 -0.357  11.181  1.00 53.90  ? 201  LEU A C   1 
ATOM   978  O  O   . LEU A 1 181 ? 24.592 -0.520  12.296  1.00 57.44  ? 201  LEU A O   1 
ATOM   979  C  CB  . LEU A 1 181 ? 25.824 -0.837  9.456   1.00 54.56  ? 201  LEU A CB  1 
ATOM   980  C  CG  . LEU A 1 181 ? 26.451 -1.765  8.410   1.00 54.19  ? 201  LEU A CG  1 
ATOM   981  C  CD1 . LEU A 1 181 ? 27.761 -1.182  7.897   1.00 59.62  ? 201  LEU A CD1 1 
ATOM   982  C  CD2 . LEU A 1 181 ? 26.671 -3.160  8.972   1.00 57.15  ? 201  LEU A CD2 1 
ATOM   983  N  N   . LEU A 1 182 ? 23.174 0.584   10.941  1.00 58.06  ? 202  LEU A N   1 
ATOM   984  C  CA  . LEU A 1 182 ? 22.707 1.461   12.010  1.00 57.95  ? 202  LEU A CA  1 
ATOM   985  C  C   . LEU A 1 182 ? 22.261 0.704   13.253  1.00 59.05  ? 202  LEU A C   1 
ATOM   986  O  O   . LEU A 1 182 ? 22.594 1.152   14.364  1.00 61.94  ? 202  LEU A O   1 
ATOM   987  C  CB  . LEU A 1 182 ? 21.562 2.345   11.495  1.00 60.67  ? 202  LEU A CB  1 
ATOM   988  C  CG  . LEU A 1 182 ? 21.956 3.476   10.544  1.00 66.63  ? 202  LEU A CG  1 
ATOM   989  C  CD1 . LEU A 1 182 ? 20.718 4.199   10.047  1.00 57.76  ? 202  LEU A CD1 1 
ATOM   990  C  CD2 . LEU A 1 182 ? 22.907 4.452   11.221  1.00 71.34  ? 202  LEU A CD2 1 
ATOM   991  N  N   . PRO A 1 183 ? 21.530 -0.410  13.163  1.00 62.39  ? 203  PRO A N   1 
ATOM   992  C  CA  . PRO A 1 183 ? 21.158 -1.116  14.397  1.00 71.11  ? 203  PRO A CA  1 
ATOM   993  C  C   . PRO A 1 183 ? 22.353 -1.546  15.226  1.00 80.52  ? 203  PRO A C   1 
ATOM   994  O  O   . PRO A 1 183 ? 22.234 -1.664  16.451  1.00 79.39  ? 203  PRO A O   1 
ATOM   995  C  CB  . PRO A 1 183 ? 20.358 -2.324  13.883  1.00 69.89  ? 203  PRO A CB  1 
ATOM   996  C  CG  . PRO A 1 183 ? 20.690 -2.434  12.432  1.00 79.45  ? 203  PRO A CG  1 
ATOM   997  C  CD  . PRO A 1 183 ? 20.905 -1.031  11.984  1.00 70.56  ? 203  PRO A CD  1 
ATOM   998  N  N   . VAL A 1 184 ? 23.505 -1.783  14.602  1.00 74.98  ? 204  VAL A N   1 
ATOM   999  C  CA  . VAL A 1 184 ? 24.667 -2.317  15.308  1.00 74.42  ? 204  VAL A CA  1 
ATOM   1000 C  C   . VAL A 1 184 ? 25.458 -1.160  15.896  1.00 81.21  ? 204  VAL A C   1 
ATOM   1001 O  O   . VAL A 1 184 ? 26.536 -1.360  16.465  1.00 83.88  ? 204  VAL A O   1 
ATOM   1002 C  CB  . VAL A 1 184 ? 25.553 -3.172  14.380  1.00 81.93  ? 204  VAL A CB  1 
ATOM   1003 C  CG1 . VAL A 1 184 ? 26.766 -3.732  15.132  1.00 73.91  ? 204  VAL A CG1 1 
ATOM   1004 C  CG2 . VAL A 1 184 ? 24.746 -4.304  13.759  1.00 94.77  ? 204  VAL A CG2 1 
ATOM   1005 N  N   . LEU A 1 185 ? 24.938 0.060   15.765  1.00 66.72  ? 205  LEU A N   1 
ATOM   1006 C  CA  . LEU A 1 185 ? 25.568 1.219   16.375  1.00 68.64  ? 205  LEU A CA  1 
ATOM   1007 C  C   . LEU A 1 185 ? 24.695 1.865   17.437  1.00 82.52  ? 205  LEU A C   1 
ATOM   1008 O  O   . LEU A 1 185 ? 25.082 2.905   17.981  1.00 103.51 ? 205  LEU A O   1 
ATOM   1009 C  CB  . LEU A 1 185 ? 25.941 2.271   15.318  1.00 67.41  ? 205  LEU A CB  1 
ATOM   1010 C  CG  . LEU A 1 185 ? 27.169 1.967   14.456  1.00 68.13  ? 205  LEU A CG  1 
ATOM   1011 C  CD1 . LEU A 1 185 ? 26.845 0.952   13.382  1.00 68.58  ? 205  LEU A CD1 1 
ATOM   1012 C  CD2 . LEU A 1 185 ? 27.733 3.242   13.836  1.00 59.18  ? 205  LEU A CD2 1 
ATOM   1013 N  N   . GLY A 1 186 ? 23.539 1.286   17.755  1.00 75.83  ? 206  GLY A N   1 
ATOM   1014 C  CA  . GLY A 1 186 ? 22.700 1.839   18.799  1.00 70.53  ? 206  GLY A CA  1 
ATOM   1015 C  C   . GLY A 1 186 ? 21.245 1.952   18.404  1.00 67.99  ? 206  GLY A C   1 
ATOM   1016 O  O   . GLY A 1 186 ? 20.377 2.096   19.267  1.00 74.55  ? 206  GLY A O   1 
ATOM   1017 N  N   . TRP A 1 187 ? 20.962 1.889   17.103  1.00 74.00  ? 207  TRP A N   1 
ATOM   1018 C  CA  . TRP A 1 187 ? 19.594 2.016   16.600  1.00 68.50  ? 207  TRP A CA  1 
ATOM   1019 C  C   . TRP A 1 187 ? 18.837 0.696   16.755  1.00 62.64  ? 207  TRP A C   1 
ATOM   1020 O  O   . TRP A 1 187 ? 18.399 0.077   15.788  1.00 74.55  ? 207  TRP A O   1 
ATOM   1021 C  CB  . TRP A 1 187 ? 19.609 2.464   15.145  1.00 66.48  ? 207  TRP A CB  1 
ATOM   1022 C  CG  . TRP A 1 187 ? 19.882 3.917   14.958  1.00 65.09  ? 207  TRP A CG  1 
ATOM   1023 C  CD1 . TRP A 1 187 ? 18.970 4.887   14.673  1.00 73.05  ? 207  TRP A CD1 1 
ATOM   1024 C  CD2 . TRP A 1 187 ? 21.154 4.571   15.038  1.00 68.13  ? 207  TRP A CD2 1 
ATOM   1025 N  NE1 . TRP A 1 187 ? 19.591 6.108   14.570  1.00 71.90  ? 207  TRP A NE1 1 
ATOM   1026 C  CE2 . TRP A 1 187 ? 20.933 5.941   14.790  1.00 68.88  ? 207  TRP A CE2 1 
ATOM   1027 C  CE3 . TRP A 1 187 ? 22.457 4.133   15.294  1.00 70.80  ? 207  TRP A CE3 1 
ATOM   1028 C  CZ2 . TRP A 1 187 ? 21.965 6.876   14.792  1.00 72.72  ? 207  TRP A CZ2 1 
ATOM   1029 C  CZ3 . TRP A 1 187 ? 23.481 5.063   15.296  1.00 81.13  ? 207  TRP A CZ3 1 
ATOM   1030 C  CH2 . TRP A 1 187 ? 23.229 6.419   15.046  1.00 82.53  ? 207  TRP A CH2 1 
ATOM   1031 N  N   . ASN A 1 188 ? 18.673 0.276   18.007  1.00 50.91  ? 208  ASN A N   1 
ATOM   1032 C  CA  . ASN A 1 188 ? 17.922 -0.928  18.344  1.00 50.44  ? 208  ASN A CA  1 
ATOM   1033 C  C   . ASN A 1 188 ? 16.909 -0.578  19.425  1.00 47.39  ? 208  ASN A C   1 
ATOM   1034 O  O   . ASN A 1 188 ? 16.823 0.567   19.876  1.00 54.85  ? 208  ASN A O   1 
ATOM   1035 C  CB  . ASN A 1 188 ? 18.843 -2.067  18.804  1.00 55.82  ? 208  ASN A CB  1 
ATOM   1036 C  CG  . ASN A 1 188 ? 19.567 -1.743  20.086  1.00 53.86  ? 208  ASN A CG  1 
ATOM   1037 O  OD1 . ASN A 1 188 ? 19.302 -2.330  21.133  1.00 51.90  ? 208  ASN A OD1 1 
ATOM   1038 N  ND2 . ASN A 1 188 ? 20.493 -0.800  20.009  1.00 60.48  ? 208  ASN A ND2 1 
ATOM   1039 N  N   . CYS A 1 189 ? 16.136 -1.581  19.844  1.00 46.34  ? 209  CYS A N   1 
ATOM   1040 C  CA  . CYS A 1 189 ? 15.030 -1.381  20.772  1.00 43.58  ? 209  CYS A CA  1 
ATOM   1041 C  C   . CYS A 1 189 ? 15.247 -2.062  22.114  1.00 46.54  ? 209  CYS A C   1 
ATOM   1042 O  O   . CYS A 1 189 ? 14.294 -2.183  22.893  1.00 50.69  ? 209  CYS A O   1 
ATOM   1043 C  CB  . CYS A 1 189 ? 13.731 -1.898  20.155  1.00 40.22  ? 209  CYS A CB  1 
ATOM   1044 S  SG  . CYS A 1 189 ? 13.608 -3.710  20.109  1.00 39.94  ? 209  CYS A SG  1 
ATOM   1045 N  N   . LEU A 1 190 ? 16.465 -2.508  22.409  1.00 49.03  ? 210  LEU A N   1 
ATOM   1046 C  CA  . LEU A 1 190 ? 16.739 -3.267  23.620  1.00 51.43  ? 210  LEU A CA  1 
ATOM   1047 C  C   . LEU A 1 190 ? 16.979 -2.382  24.839  1.00 44.13  ? 210  LEU A C   1 
ATOM   1048 O  O   . LEU A 1 190 ? 17.586 -2.841  25.813  1.00 43.43  ? 210  LEU A O   1 
ATOM   1049 C  CB  . LEU A 1 190 ? 17.942 -4.185  23.393  1.00 66.19  ? 210  LEU A CB  1 
ATOM   1050 C  CG  . LEU A 1 190 ? 17.801 -5.189  22.245  1.00 54.90  ? 210  LEU A CG  1 
ATOM   1051 C  CD1 . LEU A 1 190 ? 19.070 -6.011  22.094  1.00 53.67  ? 210  LEU A CD1 1 
ATOM   1052 C  CD2 . LEU A 1 190 ? 16.595 -6.096  22.452  1.00 52.44  ? 210  LEU A CD2 1 
ATOM   1053 N  N   . ALA A 1 191 ? 16.519 -1.137  24.809  1.00 53.86  ? 211  ALA A N   1 
ATOM   1054 C  CA  . ALA A 1 191 ? 16.643 -0.218  25.929  1.00 48.47  ? 211  ALA A CA  1 
ATOM   1055 C  C   . ALA A 1 191 ? 15.315 -0.105  26.670  1.00 53.55  ? 211  ALA A C   1 
ATOM   1056 O  O   . ALA A 1 191 ? 14.245 -0.392  26.128  1.00 57.16  ? 211  ALA A O   1 
ATOM   1057 C  CB  . ALA A 1 191 ? 17.094 1.162   25.445  1.00 53.94  ? 211  ALA A CB  1 
ATOM   1058 N  N   . GLU A 1 192 ? 15.398 0.314   27.935  1.00 55.24  ? 212  GLU A N   1 
ATOM   1059 C  CA  . GLU A 1 192 ? 14.193 0.492   28.736  1.00 55.54  ? 212  GLU A CA  1 
ATOM   1060 C  C   . GLU A 1 192 ? 13.358 1.680   28.273  1.00 65.32  ? 212  GLU A C   1 
ATOM   1061 O  O   . GLU A 1 192 ? 12.171 1.753   28.607  1.00 69.44  ? 212  GLU A O   1 
ATOM   1062 C  CB  . GLU A 1 192 ? 14.561 0.665   30.210  1.00 47.94  ? 212  GLU A CB  1 
ATOM   1063 N  N   . ARG A 1 193 ? 13.944 2.605   27.514  1.00 71.20  ? 213  ARG A N   1 
ATOM   1064 C  CA  . ARG A 1 193 ? 13.252 3.792   27.022  1.00 64.25  ? 213  ARG A CA  1 
ATOM   1065 C  C   . ARG A 1 193 ? 13.045 3.724   25.511  1.00 58.22  ? 213  ARG A C   1 
ATOM   1066 O  O   . ARG A 1 193 ? 13.153 4.728   24.807  1.00 57.91  ? 213  ARG A O   1 
ATOM   1067 C  CB  . ARG A 1 193 ? 14.021 5.057   27.400  1.00 67.85  ? 213  ARG A CB  1 
ATOM   1068 C  CG  . ARG A 1 193 ? 13.210 6.345   27.286  1.00 73.81  ? 213  ARG A CG  1 
ATOM   1069 C  CD  . ARG A 1 193 ? 12.143 6.442   28.372  1.00 78.04  ? 213  ARG A CD  1 
ATOM   1070 N  NE  . ARG A 1 193 ? 12.604 7.181   29.543  1.00 83.54  ? 213  ARG A NE  1 
ATOM   1071 C  CZ  . ARG A 1 193 ? 12.382 8.471   29.759  1.00 71.59  ? 213  ARG A CZ  1 
ATOM   1072 N  NH1 . ARG A 1 193 ? 11.710 9.215   28.894  1.00 63.69  ? 213  ARG A NH1 1 
ATOM   1073 N  NH2 . ARG A 1 193 ? 12.844 9.031   30.874  1.00 68.27  ? 213  ARG A NH2 1 
ATOM   1074 N  N   . ALA A 1 194 ? 12.744 2.532   24.999  1.00 54.31  ? 214  ALA A N   1 
ATOM   1075 C  CA  . ALA A 1 194 ? 12.527 2.335   23.572  1.00 46.44  ? 214  ALA A CA  1 
ATOM   1076 C  C   . ALA A 1 194 ? 11.609 1.140   23.380  1.00 45.56  ? 214  ALA A C   1 
ATOM   1077 O  O   . ALA A 1 194 ? 11.887 0.055   23.899  1.00 59.82  ? 214  ALA A O   1 
ATOM   1078 C  CB  . ALA A 1 194 ? 13.851 2.114   22.832  1.00 45.08  ? 214  ALA A CB  1 
ATOM   1079 N  N   . ALA A 1 195 ? 10.526 1.338   22.636  1.00 43.33  ? 215  ALA A N   1 
ATOM   1080 C  CA  . ALA A 1 195 ? 9.542  0.291   22.408  1.00 47.10  ? 215  ALA A CA  1 
ATOM   1081 C  C   . ALA A 1 195 ? 9.907  -0.508  21.164  1.00 43.69  ? 215  ALA A C   1 
ATOM   1082 O  O   . ALA A 1 195 ? 10.148 0.066   20.097  1.00 31.13  ? 215  ALA A O   1 
ATOM   1083 C  CB  . ALA A 1 195 ? 8.144  0.889   22.259  1.00 52.97  ? 215  ALA A CB  1 
ATOM   1084 N  N   . CYS A 1 196 ? 9.942  -1.829  21.305  1.00 45.75  ? 216  CYS A N   1 
ATOM   1085 C  CA  . CYS A 1 196 ? 10.313 -2.699  20.204  1.00 45.30  ? 216  CYS A CA  1 
ATOM   1086 C  C   . CYS A 1 196 ? 9.185  -2.793  19.184  1.00 42.22  ? 216  CYS A C   1 
ATOM   1087 O  O   . CYS A 1 196 ? 8.012  -2.547  19.480  1.00 36.21  ? 216  CYS A O   1 
ATOM   1088 C  CB  . CYS A 1 196 ? 10.671 -4.092  20.715  1.00 40.91  ? 216  CYS A CB  1 
ATOM   1089 S  SG  . CYS A 1 196 ? 12.266 -4.158  21.562  1.00 47.55  ? 216  CYS A SG  1 
ATOM   1090 N  N   . SER A 1 197 ? 9.567  -3.145  17.963  1.00 44.71  ? 217  SER A N   1 
ATOM   1091 C  CA  . SER A 1 197 ? 8.638  -3.314  16.863  1.00 46.34  ? 217  SER A CA  1 
ATOM   1092 C  C   . SER A 1 197 ? 8.288  -4.789  16.713  1.00 31.27  ? 217  SER A C   1 
ATOM   1093 O  O   . SER A 1 197 ? 8.699  -5.641  17.502  1.00 32.65  ? 217  SER A O   1 
ATOM   1094 C  CB  . SER A 1 197 ? 9.237  -2.759  15.570  1.00 43.96  ? 217  SER A CB  1 
ATOM   1095 O  OG  . SER A 1 197 ? 10.372 -3.512  15.178  1.00 38.83  ? 217  SER A OG  1 
ATOM   1096 N  N   . VAL A 1 198 ? 7.513  -5.090  15.671  1.00 34.49  ? 218  VAL A N   1 
ATOM   1097 C  CA  . VAL A 1 198 ? 7.130  -6.468  15.406  1.00 31.70  ? 218  VAL A CA  1 
ATOM   1098 C  C   . VAL A 1 198 ? 8.326  -7.314  14.990  1.00 37.18  ? 218  VAL A C   1 
ATOM   1099 O  O   . VAL A 1 198 ? 8.272  -8.546  15.085  1.00 47.81  ? 218  VAL A O   1 
ATOM   1100 C  CB  . VAL A 1 198 ? 6.026  -6.507  14.332  1.00 32.53  ? 218  VAL A CB  1 
ATOM   1101 C  CG1 . VAL A 1 198 ? 6.538  -5.940  13.014  1.00 33.45  ? 218  VAL A CG1 1 
ATOM   1102 C  CG2 . VAL A 1 198 ? 5.511  -7.921  14.148  1.00 40.68  ? 218  VAL A CG2 1 
ATOM   1103 N  N   . VAL A 1 199 ? 9.402  -6.691  14.529  1.00 39.84  ? 219  VAL A N   1 
ATOM   1104 C  CA  . VAL A 1 199 ? 10.613 -7.400  14.122  1.00 35.38  ? 219  VAL A CA  1 
ATOM   1105 C  C   . VAL A 1 199 ? 11.735 -6.899  15.023  1.00 36.91  ? 219  VAL A C   1 
ATOM   1106 O  O   . VAL A 1 199 ? 12.422 -5.923  14.714  1.00 47.29  ? 219  VAL A O   1 
ATOM   1107 C  CB  . VAL A 1 199 ? 10.942 -7.193  12.642  1.00 35.34  ? 219  VAL A CB  1 
ATOM   1108 C  CG1 . VAL A 1 199 ? 10.044 -8.065  11.779  1.00 40.43  ? 219  VAL A CG1 1 
ATOM   1109 C  CG2 . VAL A 1 199 ? 10.782 -5.727  12.253  1.00 32.56  ? 219  VAL A CG2 1 
ATOM   1110 N  N   . ARG A 1 200 ? 11.947 -7.587  16.141  1.00 36.44  ? 220  ARG A N   1 
ATOM   1111 C  CA  . ARG A 1 200 ? 12.998 -7.193  17.058  1.00 36.61  ? 220  ARG A CA  1 
ATOM   1112 C  C   . ARG A 1 200 ? 14.353 -7.548  16.459  1.00 38.22  ? 220  ARG A C   1 
ATOM   1113 O  O   . ARG A 1 200 ? 14.448 -8.430  15.604  1.00 44.46  ? 220  ARG A O   1 
ATOM   1114 C  CB  . ARG A 1 200 ? 12.824 -7.881  18.409  1.00 36.46  ? 220  ARG A CB  1 
ATOM   1115 N  N   . PRO A 1 201 ? 15.427 -6.874  16.893  1.00 37.58  ? 221  PRO A N   1 
ATOM   1116 C  CA  . PRO A 1 201 ? 15.477 -5.789  17.886  1.00 39.55  ? 221  PRO A CA  1 
ATOM   1117 C  C   . PRO A 1 201 ? 15.190 -4.413  17.292  1.00 37.91  ? 221  PRO A C   1 
ATOM   1118 O  O   . PRO A 1 201 ? 15.597 -3.406  17.862  1.00 41.38  ? 221  PRO A O   1 
ATOM   1119 C  CB  . PRO A 1 201 ? 16.922 -5.864  18.419  1.00 43.82  ? 221  PRO A CB  1 
ATOM   1120 C  CG  . PRO A 1 201 ? 17.546 -7.104  17.806  1.00 43.67  ? 221  PRO A CG  1 
ATOM   1121 C  CD  . PRO A 1 201 ? 16.776 -7.347  16.553  1.00 41.01  ? 221  PRO A CD  1 
ATOM   1122 N  N   . LEU A 1 202 ? 14.513 -4.328  16.150  1.00 36.47  ? 222  LEU A N   1 
ATOM   1123 C  CA  . LEU A 1 202 ? 14.241 -3.032  15.545  1.00 39.41  ? 222  LEU A CA  1 
ATOM   1124 C  C   . LEU A 1 202 ? 13.179 -2.279  16.340  1.00 42.82  ? 222  LEU A C   1 
ATOM   1125 O  O   . LEU A 1 202 ? 12.156 -2.846  16.736  1.00 35.69  ? 222  LEU A O   1 
ATOM   1126 C  CB  . LEU A 1 202 ? 13.785 -3.206  14.097  1.00 48.11  ? 222  LEU A CB  1 
ATOM   1127 C  CG  . LEU A 1 202 ? 14.780 -3.903  13.168  1.00 52.72  ? 222  LEU A CG  1 
ATOM   1128 C  CD1 . LEU A 1 202 ? 14.082 -4.409  11.919  1.00 49.37  ? 222  LEU A CD1 1 
ATOM   1129 C  CD2 . LEU A 1 202 ? 15.911 -2.958  12.800  1.00 61.03  ? 222  LEU A CD2 1 
ATOM   1130 N  N   . ALA A 1 203 ? 13.427 -0.991  16.566  1.00 44.38  ? 223  ALA A N   1 
ATOM   1131 C  CA  . ALA A 1 203 ? 12.506 -0.160  17.323  1.00 37.01  ? 223  ALA A CA  1 
ATOM   1132 C  C   . ALA A 1 203 ? 11.378 0.343   16.432  1.00 36.08  ? 223  ALA A C   1 
ATOM   1133 O  O   . ALA A 1 203 ? 11.533 0.484   15.216  1.00 35.16  ? 223  ALA A O   1 
ATOM   1134 C  CB  . ALA A 1 203 ? 13.246 1.022   17.949  1.00 35.40  ? 223  ALA A CB  1 
ATOM   1135 N  N   . ARG A 1 204 ? 10.227 0.616   17.053  1.00 42.92  ? 224  ARG A N   1 
ATOM   1136 C  CA  . ARG A 1 204 ? 9.092  1.129   16.294  1.00 42.79  ? 224  ARG A CA  1 
ATOM   1137 C  C   . ARG A 1 204 ? 9.436  2.453   15.627  1.00 37.18  ? 224  ARG A C   1 
ATOM   1138 O  O   . ARG A 1 204 ? 8.989  2.729   14.508  1.00 35.92  ? 224  ARG A O   1 
ATOM   1139 C  CB  . ARG A 1 204 ? 7.873  1.299   17.200  1.00 42.28  ? 224  ARG A CB  1 
ATOM   1140 C  CG  . ARG A 1 204 ? 7.302  -0.005  17.720  1.00 44.06  ? 224  ARG A CG  1 
ATOM   1141 C  CD  . ARG A 1 204 ? 5.865  0.153   18.204  1.00 46.25  ? 224  ARG A CD  1 
ATOM   1142 N  NE  . ARG A 1 204 ? 4.936  0.392   17.103  1.00 43.46  ? 224  ARG A NE  1 
ATOM   1143 C  CZ  . ARG A 1 204 ? 4.516  1.586   16.706  1.00 46.84  ? 224  ARG A CZ  1 
ATOM   1144 N  NH1 . ARG A 1 204 ? 4.908  2.698   17.307  1.00 61.38  ? 224  ARG A NH1 1 
ATOM   1145 N  NH2 . ARG A 1 204 ? 3.680  1.668   15.675  1.00 36.40  ? 224  ARG A NH2 1 
ATOM   1146 N  N   . SER A 1 205 ? 10.234 3.283   16.299  1.00 31.21  ? 225  SER A N   1 
ATOM   1147 C  CA  . SER A 1 205 ? 10.596 4.576   15.732  1.00 38.66  ? 225  SER A CA  1 
ATOM   1148 C  C   . SER A 1 205 ? 11.342 4.409   14.417  1.00 34.68  ? 225  SER A C   1 
ATOM   1149 O  O   . SER A 1 205 ? 11.062 5.115   13.441  1.00 39.93  ? 225  SER A O   1 
ATOM   1150 C  CB  . SER A 1 205 ? 11.446 5.360   16.731  1.00 43.38  ? 225  SER A CB  1 
ATOM   1151 O  OG  . SER A 1 205 ? 12.017 6.505   16.126  1.00 69.19  ? 225  SER A OG  1 
ATOM   1152 N  N   . HIS A 1 206 ? 12.289 3.473   14.367  1.00 36.91  ? 226  HIS A N   1 
ATOM   1153 C  CA  . HIS A 1 206 ? 13.136 3.339   13.189  1.00 36.67  ? 226  HIS A CA  1 
ATOM   1154 C  C   . HIS A 1 206 ? 12.429 2.589   12.068  1.00 36.04  ? 226  HIS A C   1 
ATOM   1155 O  O   . HIS A 1 206 ? 12.528 2.980   10.900  1.00 36.34  ? 226  HIS A O   1 
ATOM   1156 C  CB  . HIS A 1 206 ? 14.439 2.642   13.573  1.00 37.54  ? 226  HIS A CB  1 
ATOM   1157 C  CG  . HIS A 1 206 ? 15.159 3.308   14.703  1.00 47.27  ? 226  HIS A CG  1 
ATOM   1158 N  ND1 . HIS A 1 206 ? 15.866 2.606   15.656  1.00 49.68  ? 226  HIS A ND1 1 
ATOM   1159 C  CD2 . HIS A 1 206 ? 15.274 4.615   15.038  1.00 54.14  ? 226  HIS A CD2 1 
ATOM   1160 C  CE1 . HIS A 1 206 ? 16.387 3.452   16.527  1.00 55.49  ? 226  HIS A CE1 1 
ATOM   1161 N  NE2 . HIS A 1 206 ? 16.043 4.678   16.174  1.00 58.23  ? 226  HIS A NE2 1 
ATOM   1162 N  N   . VAL A 1 207 ? 11.704 1.517   12.396  1.00 31.74  ? 227  VAL A N   1 
ATOM   1163 C  CA  . VAL A 1 207 ? 10.951 0.812   11.364  1.00 34.42  ? 227  VAL A CA  1 
ATOM   1164 C  C   . VAL A 1 207 ? 9.897  1.729   10.767  1.00 31.82  ? 227  VAL A C   1 
ATOM   1165 O  O   . VAL A 1 207 ? 9.565  1.620   9.580   1.00 26.11  ? 227  VAL A O   1 
ATOM   1166 C  CB  . VAL A 1 207 ? 10.317 -0.476  11.929  1.00 38.27  ? 227  VAL A CB  1 
ATOM   1167 C  CG1 . VAL A 1 207 ? 11.387 -1.404  12.463  1.00 42.97  ? 227  VAL A CG1 1 
ATOM   1168 C  CG2 . VAL A 1 207 ? 9.299  -0.145  13.001  1.00 39.05  ? 227  VAL A CG2 1 
ATOM   1169 N  N   . ALA A 1 208 ? 9.344  2.637   11.574  1.00 40.87  ? 228  ALA A N   1 
ATOM   1170 C  CA  . ALA A 1 208 ? 8.362  3.583   11.056  1.00 35.48  ? 228  ALA A CA  1 
ATOM   1171 C  C   . ALA A 1 208 ? 8.984  4.530   10.037  1.00 29.10  ? 228  ALA A C   1 
ATOM   1172 O  O   . ALA A 1 208 ? 8.384  4.803   8.990   1.00 20.90  ? 228  ALA A O   1 
ATOM   1173 C  CB  . ALA A 1 208 ? 7.743  4.371   12.205  1.00 42.85  ? 228  ALA A CB  1 
ATOM   1174 N  N   . LEU A 1 209 ? 10.182 5.044   10.320  1.00 40.71  ? 229  LEU A N   1 
ATOM   1175 C  CA  . LEU A 1 209 ? 10.841 5.909   9.349   1.00 43.04  ? 229  LEU A CA  1 
ATOM   1176 C  C   . LEU A 1 209 ? 11.142 5.147   8.066   1.00 33.21  ? 229  LEU A C   1 
ATOM   1177 O  O   . LEU A 1 209 ? 10.949 5.672   6.964   1.00 39.48  ? 229  LEU A O   1 
ATOM   1178 C  CB  . LEU A 1 209 ? 12.119 6.504   9.943   1.00 39.55  ? 229  LEU A CB  1 
ATOM   1179 C  CG  . LEU A 1 209 ? 11.960 7.389   11.185  1.00 47.07  ? 229  LEU A CG  1 
ATOM   1180 C  CD1 . LEU A 1 209 ? 13.206 8.238   11.394  1.00 50.99  ? 229  LEU A CD1 1 
ATOM   1181 C  CD2 . LEU A 1 209 ? 10.720 8.272   11.103  1.00 41.22  ? 229  LEU A CD2 1 
ATOM   1182 N  N   . LEU A 1 210 ? 11.602 3.900   8.187   1.00 25.25  ? 230  LEU A N   1 
ATOM   1183 C  CA  . LEU A 1 210 ? 11.784 3.073   7.000   1.00 24.33  ? 230  LEU A CA  1 
ATOM   1184 C  C   . LEU A 1 210 ? 10.462 2.869   6.276   1.00 25.07  ? 230  LEU A C   1 
ATOM   1185 O  O   . LEU A 1 210 ? 10.404 2.926   5.043   1.00 21.44  ? 230  LEU A O   1 
ATOM   1186 C  CB  . LEU A 1 210 ? 12.391 1.724   7.382   1.00 34.24  ? 230  LEU A CB  1 
ATOM   1187 C  CG  . LEU A 1 210 ? 13.838 1.735   7.874   1.00 27.56  ? 230  LEU A CG  1 
ATOM   1188 C  CD1 . LEU A 1 210 ? 14.243 0.354   8.333   1.00 26.07  ? 230  LEU A CD1 1 
ATOM   1189 C  CD2 . LEU A 1 210 ? 14.772 2.218   6.788   1.00 20.09  ? 230  LEU A CD2 1 
ATOM   1190 N  N   . SER A 1 211 ? 9.389  2.623   7.028   1.00 29.89  ? 231  SER A N   1 
ATOM   1191 C  CA  . SER A 1 211 ? 8.079  2.452   6.410   1.00 22.19  ? 231  SER A CA  1 
ATOM   1192 C  C   . SER A 1 211 ? 7.621  3.740   5.740   1.00 21.99  ? 231  SER A C   1 
ATOM   1193 O  O   . SER A 1 211 ? 7.182  3.732   4.585   1.00 20.58  ? 231  SER A O   1 
ATOM   1194 C  CB  . SER A 1 211 ? 7.063  1.999   7.457   1.00 20.19  ? 231  SER A CB  1 
ATOM   1195 O  OG  . SER A 1 211 ? 5.802  1.753   6.863   1.00 17.38  ? 231  SER A OG  1 
ATOM   1196 N  N   . ALA A 1 212 ? 7.728  4.866   6.448   1.00 31.76  ? 232  ALA A N   1 
ATOM   1197 C  CA  . ALA A 1 212 ? 7.334  6.138   5.855   1.00 24.42  ? 232  ALA A CA  1 
ATOM   1198 C  C   . ALA A 1 212 ? 8.197  6.461   4.644   1.00 26.27  ? 232  ALA A C   1 
ATOM   1199 O  O   . ALA A 1 212 ? 7.696  6.943   3.623   1.00 32.15  ? 232  ALA A O   1 
ATOM   1200 C  CB  . ALA A 1 212 ? 7.425  7.254   6.893   1.00 33.67  ? 232  ALA A CB  1 
ATOM   1201 N  N   . ALA A 1 213 ? 9.500  6.195   4.739   1.00 28.74  ? 233  ALA A N   1 
ATOM   1202 C  CA  . ALA A 1 213 ? 10.378 6.420   3.597   1.00 28.41  ? 233  ALA A CA  1 
ATOM   1203 C  C   . ALA A 1 213 ? 9.990  5.524   2.429   1.00 27.08  ? 233  ALA A C   1 
ATOM   1204 O  O   . ALA A 1 213 ? 10.020 5.953   1.270   1.00 33.73  ? 233  ALA A O   1 
ATOM   1205 C  CB  . ALA A 1 213 ? 11.833 6.180   3.997   1.00 33.72  ? 233  ALA A CB  1 
ATOM   1206 N  N   . PHE A 1 214 ? 9.619  4.275   2.717   1.00 18.90  ? 234  PHE A N   1 
ATOM   1207 C  CA  . PHE A 1 214 ? 9.241  3.352   1.651   1.00 15.69  ? 234  PHE A CA  1 
ATOM   1208 C  C   . PHE A 1 214 ? 8.006  3.840   0.904   1.00 16.67  ? 234  PHE A C   1 
ATOM   1209 O  O   . PHE A 1 214 ? 7.939  3.743   -0.326  1.00 19.79  ? 234  PHE A O   1 
ATOM   1210 C  CB  . PHE A 1 214 ? 9.002  1.961   2.234   1.00 23.52  ? 234  PHE A CB  1 
ATOM   1211 C  CG  . PHE A 1 214 ? 8.295  1.021   1.298   1.00 24.53  ? 234  PHE A CG  1 
ATOM   1212 C  CD1 . PHE A 1 214 ? 8.834  0.715   0.061   1.00 23.92  ? 234  PHE A CD1 1 
ATOM   1213 C  CD2 . PHE A 1 214 ? 7.098  0.429   1.666   1.00 23.43  ? 234  PHE A CD2 1 
ATOM   1214 C  CE1 . PHE A 1 214 ? 8.185  -0.155  -0.797  1.00 22.37  ? 234  PHE A CE1 1 
ATOM   1215 C  CE2 . PHE A 1 214 ? 6.448  -0.441  0.814   1.00 26.98  ? 234  PHE A CE2 1 
ATOM   1216 C  CZ  . PHE A 1 214 ? 6.993  -0.733  -0.420  1.00 22.48  ? 234  PHE A CZ  1 
ATOM   1217 N  N   . PHE A 1 215 ? 7.016  4.367   1.625   1.00 16.24  ? 235  PHE A N   1 
ATOM   1218 C  CA  . PHE A 1 215 ? 5.816  4.858   0.957   1.00 18.39  ? 235  PHE A CA  1 
ATOM   1219 C  C   . PHE A 1 215 ? 6.160  5.967   -0.025  1.00 19.09  ? 235  PHE A C   1 
ATOM   1220 O  O   . PHE A 1 215 ? 5.720  5.952   -1.180  1.00 21.32  ? 235  PHE A O   1 
ATOM   1221 C  CB  . PHE A 1 215 ? 4.800  5.352   1.988   1.00 25.65  ? 235  PHE A CB  1 
ATOM   1222 C  CG  . PHE A 1 215 ? 3.908  4.273   2.523   1.00 16.49  ? 235  PHE A CG  1 
ATOM   1223 C  CD1 . PHE A 1 215 ? 2.762  3.909   1.841   1.00 18.17  ? 235  PHE A CD1 1 
ATOM   1224 C  CD2 . PHE A 1 215 ? 4.212  3.625   3.707   1.00 19.36  ? 235  PHE A CD2 1 
ATOM   1225 C  CE1 . PHE A 1 215 ? 1.937  2.917   2.329   1.00 17.70  ? 235  PHE A CE1 1 
ATOM   1226 C  CE2 . PHE A 1 215 ? 3.391  2.633   4.198   1.00 18.16  ? 235  PHE A CE2 1 
ATOM   1227 C  CZ  . PHE A 1 215 ? 2.251  2.279   3.507   1.00 17.71  ? 235  PHE A CZ  1 
ATOM   1228 N  N   . MET A 1 216 ? 6.964  6.935   0.412   1.00 23.70  ? 236  MET A N   1 
ATOM   1229 C  CA  . MET A 1 216 ? 7.318  8.040   -0.470  1.00 27.77  ? 236  MET A CA  1 
ATOM   1230 C  C   . MET A 1 216 ? 8.113  7.552   -1.674  1.00 24.65  ? 236  MET A C   1 
ATOM   1231 O  O   . MET A 1 216 ? 7.860  7.975   -2.808  1.00 25.42  ? 236  MET A O   1 
ATOM   1232 C  CB  . MET A 1 216 ? 8.105  9.092   0.306   1.00 37.25  ? 236  MET A CB  1 
ATOM   1233 C  CG  . MET A 1 216 ? 7.286  9.782   1.384   1.00 36.88  ? 236  MET A CG  1 
ATOM   1234 S  SD  . MET A 1 216 ? 8.199  11.097  2.201   1.00 52.15  ? 236  MET A SD  1 
ATOM   1235 C  CE  . MET A 1 216 ? 6.852  12.113  2.798   1.00 49.47  ? 236  MET A CE  1 
ATOM   1236 N  N   . VAL A 1 217 ? 9.071  6.651   -1.452  1.00 35.53  ? 237  VAL A N   1 
ATOM   1237 C  CA  . VAL A 1 217 ? 9.859  6.128   -2.563  1.00 26.11  ? 237  VAL A CA  1 
ATOM   1238 C  C   . VAL A 1 217 ? 8.964  5.392   -3.551  1.00 24.26  ? 237  VAL A C   1 
ATOM   1239 O  O   . VAL A 1 217 ? 9.079  5.574   -4.769  1.00 27.36  ? 237  VAL A O   1 
ATOM   1240 C  CB  . VAL A 1 217 ? 10.990 5.227   -2.038  1.00 29.27  ? 237  VAL A CB  1 
ATOM   1241 C  CG1 . VAL A 1 217 ? 11.658 4.498   -3.188  1.00 43.16  ? 237  VAL A CG1 1 
ATOM   1242 C  CG2 . VAL A 1 217 ? 12.008 6.057   -1.262  1.00 32.66  ? 237  VAL A CG2 1 
ATOM   1243 N  N   . PHE A 1 218 ? 8.055  4.555   -3.044  1.00 24.06  ? 238  PHE A N   1 
ATOM   1244 C  CA  . PHE A 1 218 ? 7.139  3.843   -3.929  1.00 22.26  ? 238  PHE A CA  1 
ATOM   1245 C  C   . PHE A 1 218 ? 6.162  4.797   -4.599  1.00 25.58  ? 238  PHE A C   1 
ATOM   1246 O  O   . PHE A 1 218 ? 5.700  4.525   -5.712  1.00 23.53  ? 238  PHE A O   1 
ATOM   1247 C  CB  . PHE A 1 218 ? 6.384  2.770   -3.145  1.00 23.28  ? 238  PHE A CB  1 
ATOM   1248 C  CG  . PHE A 1 218 ? 5.772  1.705   -4.006  1.00 23.41  ? 238  PHE A CG  1 
ATOM   1249 C  CD1 . PHE A 1 218 ? 4.561  1.916   -4.639  1.00 21.12  ? 238  PHE A CD1 1 
ATOM   1250 C  CD2 . PHE A 1 218 ? 6.403  0.480   -4.169  1.00 30.51  ? 238  PHE A CD2 1 
ATOM   1251 C  CE1 . PHE A 1 218 ? 3.993  0.930   -5.429  1.00 25.64  ? 238  PHE A CE1 1 
ATOM   1252 C  CE2 . PHE A 1 218 ? 5.840  -0.507  -4.956  1.00 23.62  ? 238  PHE A CE2 1 
ATOM   1253 C  CZ  . PHE A 1 218 ? 4.634  -0.283  -5.587  1.00 20.02  ? 238  PHE A CZ  1 
ATOM   1254 N  N   . GLY A 1 219 ? 5.825  5.907   -3.938  1.00 18.05  ? 239  GLY A N   1 
ATOM   1255 C  CA  . GLY A 1 219 ? 4.963  6.894   -4.560  1.00 17.01  ? 239  GLY A CA  1 
ATOM   1256 C  C   . GLY A 1 219 ? 5.608  7.576   -5.747  1.00 27.39  ? 239  GLY A C   1 
ATOM   1257 O  O   . GLY A 1 219 ? 4.923  7.932   -6.709  1.00 35.81  ? 239  GLY A O   1 
ATOM   1258 N  N   . ILE A 1 220 ? 6.925  7.774   -5.698  1.00 27.08  ? 240  ILE A N   1 
ATOM   1259 C  CA  . ILE A 1 220 ? 7.623  8.418   -6.806  1.00 25.47  ? 240  ILE A CA  1 
ATOM   1260 C  C   . ILE A 1 220 ? 7.839  7.440   -7.951  1.00 21.98  ? 240  ILE A C   1 
ATOM   1261 O  O   . ILE A 1 220 ? 7.722  7.806   -9.126  1.00 22.24  ? 240  ILE A O   1 
ATOM   1262 C  CB  . ILE A 1 220 ? 8.954  9.012   -6.313  1.00 28.02  ? 240  ILE A CB  1 
ATOM   1263 C  CG1 . ILE A 1 220 ? 8.691  10.091  -5.260  1.00 30.05  ? 240  ILE A CG1 1 
ATOM   1264 C  CG2 . ILE A 1 220 ? 9.740  9.572   -7.488  1.00 32.39  ? 240  ILE A CG2 1 
ATOM   1265 C  CD1 . ILE A 1 220 ? 9.939  10.595  -4.560  1.00 21.98  ? 240  ILE A CD1 1 
ATOM   1266 N  N   . MET A 1 221 ? 8.163  6.186   -7.632  1.00 30.68  ? 241  MET A N   1 
ATOM   1267 C  CA  . MET A 1 221 ? 8.365  5.187   -8.676  1.00 33.87  ? 241  MET A CA  1 
ATOM   1268 C  C   . MET A 1 221 ? 7.127  5.054   -9.552  1.00 30.37  ? 241  MET A C   1 
ATOM   1269 O  O   . MET A 1 221 ? 7.232  4.831   -10.764 1.00 27.60  ? 241  MET A O   1 
ATOM   1270 C  CB  . MET A 1 221 ? 8.731  3.847   -8.040  1.00 22.55  ? 241  MET A CB  1 
ATOM   1271 C  CG  . MET A 1 221 ? 10.078 3.876   -7.335  1.00 24.35  ? 241  MET A CG  1 
ATOM   1272 S  SD  . MET A 1 221 ? 10.318 2.602   -6.081  1.00 25.71  ? 241  MET A SD  1 
ATOM   1273 C  CE  . MET A 1 221 ? 10.119 1.110   -7.047  1.00 27.87  ? 241  MET A CE  1 
ATOM   1274 N  N   . LEU A 1 222 ? 5.943  5.195   -8.956  1.00 26.14  ? 242  LEU A N   1 
ATOM   1275 C  CA  . LEU A 1 222 ? 4.717  5.175   -9.746  1.00 24.97  ? 242  LEU A CA  1 
ATOM   1276 C  C   . LEU A 1 222 ? 4.660  6.364   -10.696 1.00 32.07  ? 242  LEU A C   1 
ATOM   1277 O  O   . LEU A 1 222 ? 4.254  6.224   -11.856 1.00 35.65  ? 242  LEU A O   1 
ATOM   1278 C  CB  . LEU A 1 222 ? 3.502  5.162   -8.819  1.00 24.59  ? 242  LEU A CB  1 
ATOM   1279 C  CG  . LEU A 1 222 ? 3.364  3.919   -7.935  1.00 22.38  ? 242  LEU A CG  1 
ATOM   1280 C  CD1 . LEU A 1 222 ? 2.194  4.067   -6.978  1.00 17.62  ? 242  LEU A CD1 1 
ATOM   1281 C  CD2 . LEU A 1 222 ? 3.207  2.659   -8.772  1.00 28.01  ? 242  LEU A CD2 1 
ATOM   1282 N  N   . HIS A 1 223 ? 5.070  7.544   -10.225 1.00 27.38  ? 243  HIS A N   1 
ATOM   1283 C  CA  . HIS A 1 223 ? 5.034  8.727   -11.078 1.00 23.35  ? 243  HIS A CA  1 
ATOM   1284 C  C   . HIS A 1 223 ? 5.951  8.565   -12.282 1.00 25.09  ? 243  HIS A C   1 
ATOM   1285 O  O   . HIS A 1 223 ? 5.577  8.918   -13.406 1.00 32.57  ? 243  HIS A O   1 
ATOM   1286 C  CB  . HIS A 1 223 ? 5.420  9.966   -10.272 1.00 23.80  ? 243  HIS A CB  1 
ATOM   1287 C  CG  . HIS A 1 223 ? 5.604  11.193  -11.107 1.00 27.82  ? 243  HIS A CG  1 
ATOM   1288 N  ND1 . HIS A 1 223 ? 4.732  11.546  -12.115 1.00 21.70  ? 243  HIS A ND1 1 
ATOM   1289 C  CD2 . HIS A 1 223 ? 6.561  12.151  -11.084 1.00 35.48  ? 243  HIS A CD2 1 
ATOM   1290 C  CE1 . HIS A 1 223 ? 5.144  12.668  -12.677 1.00 28.93  ? 243  HIS A CE1 1 
ATOM   1291 N  NE2 . HIS A 1 223 ? 6.252  13.057  -12.070 1.00 38.16  ? 243  HIS A NE2 1 
ATOM   1292 N  N   . LEU A 1 224 ? 7.156  8.030   -12.069 1.00 32.98  ? 244  LEU A N   1 
ATOM   1293 C  CA  . LEU A 1 224 ? 8.075  7.830   -13.184 1.00 34.83  ? 244  LEU A CA  1 
ATOM   1294 C  C   . LEU A 1 224 ? 7.511  6.839   -14.189 1.00 33.39  ? 244  LEU A C   1 
ATOM   1295 O  O   . LEU A 1 224 ? 7.661  7.022   -15.403 1.00 39.20  ? 244  LEU A O   1 
ATOM   1296 C  CB  . LEU A 1 224 ? 9.431  7.349   -12.675 1.00 31.86  ? 244  LEU A CB  1 
ATOM   1297 C  CG  . LEU A 1 224 ? 10.373 8.427   -12.147 1.00 35.68  ? 244  LEU A CG  1 
ATOM   1298 C  CD1 . LEU A 1 224 ? 11.635 7.790   -11.600 1.00 34.02  ? 244  LEU A CD1 1 
ATOM   1299 C  CD2 . LEU A 1 224 ? 10.708 9.421   -13.244 1.00 36.66  ? 244  LEU A CD2 1 
ATOM   1300 N  N   . TYR A 1 225 ? 6.862  5.779   -13.705 1.00 27.97  ? 245  TYR A N   1 
ATOM   1301 C  CA  . TYR A 1 225 ? 6.276  4.812   -14.624 1.00 33.07  ? 245  TYR A CA  1 
ATOM   1302 C  C   . TYR A 1 225 ? 5.266  5.481   -15.548 1.00 31.36  ? 245  TYR A C   1 
ATOM   1303 O  O   . TYR A 1 225 ? 5.195  5.160   -16.740 1.00 36.11  ? 245  TYR A O   1 
ATOM   1304 C  CB  . TYR A 1 225 ? 5.618  3.671   -13.850 1.00 26.11  ? 245  TYR A CB  1 
ATOM   1305 C  CG  . TYR A 1 225 ? 5.018  2.629   -14.762 1.00 22.29  ? 245  TYR A CG  1 
ATOM   1306 C  CD1 . TYR A 1 225 ? 5.806  1.632   -15.319 1.00 28.11  ? 245  TYR A CD1 1 
ATOM   1307 C  CD2 . TYR A 1 225 ? 3.669  2.653   -15.083 1.00 32.63  ? 245  TYR A CD2 1 
ATOM   1308 C  CE1 . TYR A 1 225 ? 5.267  0.682   -16.162 1.00 32.46  ? 245  TYR A CE1 1 
ATOM   1309 C  CE2 . TYR A 1 225 ? 3.119  1.706   -15.927 1.00 37.90  ? 245  TYR A CE2 1 
ATOM   1310 C  CZ  . TYR A 1 225 ? 3.924  0.724   -16.463 1.00 34.92  ? 245  TYR A CZ  1 
ATOM   1311 O  OH  . TYR A 1 225 ? 3.382  -0.221  -17.305 1.00 47.91  ? 245  TYR A OH  1 
ATOM   1312 N  N   . VAL A 1 226 ? 4.475  6.413   -15.019 1.00 17.58  ? 246  VAL A N   1 
ATOM   1313 C  CA  . VAL A 1 226 ? 3.567  7.172   -15.874 1.00 38.34  ? 246  VAL A CA  1 
ATOM   1314 C  C   . VAL A 1 226 ? 4.364  8.014   -16.860 1.00 37.69  ? 246  VAL A C   1 
ATOM   1315 O  O   . VAL A 1 226 ? 4.062  8.053   -18.059 1.00 34.36  ? 246  VAL A O   1 
ATOM   1316 C  CB  . VAL A 1 226 ? 2.627  8.041   -15.021 1.00 36.85  ? 246  VAL A CB  1 
ATOM   1317 C  CG1 . VAL A 1 226 ? 1.784  8.942   -15.911 1.00 40.35  ? 246  VAL A CG1 1 
ATOM   1318 C  CG2 . VAL A 1 226 ? 1.748  7.159   -14.165 1.00 29.80  ? 246  VAL A CG2 1 
ATOM   1319 N  N   . ARG A 1 227 ? 5.404  8.692   -16.370 1.00 27.71  ? 247  ARG A N   1 
ATOM   1320 C  CA  . ARG A 1 227 ? 6.260  9.459   -17.264 1.00 33.70  ? 247  ARG A CA  1 
ATOM   1321 C  C   . ARG A 1 227 ? 6.860  8.559   -18.334 1.00 30.22  ? 247  ARG A C   1 
ATOM   1322 O  O   . ARG A 1 227 ? 6.994  8.965   -19.494 1.00 31.40  ? 247  ARG A O   1 
ATOM   1323 C  CB  . ARG A 1 227 ? 7.355  10.164  -16.466 1.00 37.85  ? 247  ARG A CB  1 
ATOM   1324 C  CG  . ARG A 1 227 ? 6.844  11.322  -15.619 1.00 39.88  ? 247  ARG A CG  1 
ATOM   1325 C  CD  . ARG A 1 227 ? 7.949  11.941  -14.774 1.00 34.51  ? 247  ARG A CD  1 
ATOM   1326 N  NE  . ARG A 1 227 ? 9.024  12.497  -15.587 1.00 49.27  ? 247  ARG A NE  1 
ATOM   1327 C  CZ  . ARG A 1 227 ? 10.159 12.981  -15.099 1.00 56.07  ? 247  ARG A CZ  1 
ATOM   1328 N  NH1 . ARG A 1 227 ? 10.410 12.980  -13.800 1.00 45.10  ? 247  ARG A NH1 1 
ATOM   1329 N  NH2 . ARG A 1 227 ? 11.066 13.476  -15.936 1.00 50.26  ? 247  ARG A NH2 1 
ATOM   1330 N  N   . ILE A 1 228 ? 7.207  7.324   -17.967 1.00 31.12  ? 248  ILE A N   1 
ATOM   1331 C  CA  . ILE A 1 228 ? 7.658  6.357   -18.964 1.00 29.52  ? 248  ILE A CA  1 
ATOM   1332 C  C   . ILE A 1 228 ? 6.563  6.121   -19.995 1.00 28.76  ? 248  ILE A C   1 
ATOM   1333 O  O   . ILE A 1 228 ? 6.809  6.143   -21.206 1.00 40.90  ? 248  ILE A O   1 
ATOM   1334 C  CB  . ILE A 1 228 ? 8.079  5.042   -18.286 1.00 23.98  ? 248  ILE A CB  1 
ATOM   1335 C  CG1 . ILE A 1 228 ? 9.360  5.248   -17.481 1.00 29.48  ? 248  ILE A CG1 1 
ATOM   1336 C  CG2 . ILE A 1 228 ? 8.258  3.958   -19.331 1.00 28.95  ? 248  ILE A CG2 1 
ATOM   1337 C  CD1 . ILE A 1 228 ? 9.722  4.081   -16.599 1.00 28.07  ? 248  ILE A CD1 1 
ATOM   1338 N  N   . CYS A 1 229 ? 5.333  5.901   -19.528 1.00 33.13  ? 249  CYS A N   1 
ATOM   1339 C  CA  . CYS A 1 229 ? 4.223  5.717   -20.454 1.00 30.79  ? 249  CYS A CA  1 
ATOM   1340 C  C   . CYS A 1 229 ? 4.056  6.938   -21.345 1.00 35.67  ? 249  CYS A C   1 
ATOM   1341 O  O   . CYS A 1 229 ? 3.928  6.812   -22.569 1.00 36.26  ? 249  CYS A O   1 
ATOM   1342 C  CB  . CYS A 1 229 ? 2.935  5.444   -19.681 1.00 23.91  ? 249  CYS A CB  1 
ATOM   1343 S  SG  . CYS A 1 229 ? 2.907  3.850   -18.843 1.00 28.69  ? 249  CYS A SG  1 
ATOM   1344 N  N   . GLN A 1 230 ? 4.078  8.133   -20.752 1.00 33.46  ? 250  GLN A N   1 
ATOM   1345 C  CA  . GLN A 1 230 ? 3.982  9.347   -21.550 1.00 31.10  ? 250  GLN A CA  1 
ATOM   1346 C  C   . GLN A 1 230 ? 5.065  9.375   -22.617 1.00 33.23  ? 250  GLN A C   1 
ATOM   1347 O  O   . GLN A 1 230 ? 4.805  9.741   -23.769 1.00 37.69  ? 250  GLN A O   1 
ATOM   1348 C  CB  . GLN A 1 230 ? 4.085  10.573  -20.645 1.00 31.44  ? 250  GLN A CB  1 
ATOM   1349 C  CG  . GLN A 1 230 ? 2.948  10.692  -19.650 1.00 30.24  ? 250  GLN A CG  1 
ATOM   1350 C  CD  . GLN A 1 230 ? 3.161  11.812  -18.654 1.00 32.89  ? 250  GLN A CD  1 
ATOM   1351 O  OE1 . GLN A 1 230 ? 4.176  12.509  -18.689 1.00 39.44  ? 250  GLN A OE1 1 
ATOM   1352 N  NE2 . GLN A 1 230 ? 2.202  11.991  -17.755 1.00 34.84  ? 250  GLN A NE2 1 
ATOM   1353 N  N   . VAL A 1 231 ? 6.283  8.972   -22.257 1.00 33.46  ? 251  VAL A N   1 
ATOM   1354 C  CA  . VAL A 1 231 ? 7.366  8.927   -23.232 1.00 42.46  ? 251  VAL A CA  1 
ATOM   1355 C  C   . VAL A 1 231 ? 7.024  7.960   -24.356 1.00 38.23  ? 251  VAL A C   1 
ATOM   1356 O  O   . VAL A 1 231 ? 7.153  8.287   -25.542 1.00 34.15  ? 251  VAL A O   1 
ATOM   1357 C  CB  . VAL A 1 231 ? 8.687  8.542   -22.543 1.00 38.00  ? 251  VAL A CB  1 
ATOM   1358 C  CG1 . VAL A 1 231 ? 9.711  8.095   -23.571 1.00 50.80  ? 251  VAL A CG1 1 
ATOM   1359 C  CG2 . VAL A 1 231 ? 9.216  9.712   -21.729 1.00 51.38  ? 251  VAL A CG2 1 
ATOM   1360 N  N   . VAL A 1 232 ? 6.574  6.756   -24.003 1.00 45.23  ? 252  VAL A N   1 
ATOM   1361 C  CA  . VAL A 1 232 ? 6.259  5.772   -25.031 1.00 48.25  ? 252  VAL A CA  1 
ATOM   1362 C  C   . VAL A 1 232 ? 5.079  6.244   -25.866 1.00 37.81  ? 252  VAL A C   1 
ATOM   1363 O  O   . VAL A 1 232 ? 5.074  6.101   -27.094 1.00 38.15  ? 252  VAL A O   1 
ATOM   1364 C  CB  . VAL A 1 232 ? 5.990  4.393   -24.404 1.00 40.52  ? 252  VAL A CB  1 
ATOM   1365 C  CG1 . VAL A 1 232 ? 5.879  3.341   -25.490 1.00 40.96  ? 252  VAL A CG1 1 
ATOM   1366 C  CG2 . VAL A 1 232 ? 7.090  4.025   -23.424 1.00 30.08  ? 252  VAL A CG2 1 
ATOM   1367 N  N   . TRP A 1 233 ? 4.062  6.816   -25.219 1.00 33.67  ? 253  TRP A N   1 
ATOM   1368 C  CA  . TRP A 1 233 ? 2.945  7.384   -25.965 1.00 35.20  ? 253  TRP A CA  1 
ATOM   1369 C  C   . TRP A 1 233 ? 3.432  8.460   -26.924 1.00 44.69  ? 253  TRP A C   1 
ATOM   1370 O  O   . TRP A 1 233 ? 3.064  8.472   -28.103 1.00 52.91  ? 253  TRP A O   1 
ATOM   1371 C  CB  . TRP A 1 233 ? 1.912  7.971   -25.006 1.00 36.95  ? 253  TRP A CB  1 
ATOM   1372 C  CG  . TRP A 1 233 ? 1.289  6.980   -24.082 1.00 32.33  ? 253  TRP A CG  1 
ATOM   1373 C  CD1 . TRP A 1 233 ? 1.154  5.640   -24.283 1.00 31.52  ? 253  TRP A CD1 1 
ATOM   1374 C  CD2 . TRP A 1 233 ? 0.715  7.255   -22.799 1.00 33.42  ? 253  TRP A CD2 1 
ATOM   1375 N  NE1 . TRP A 1 233 ? 0.527  5.062   -23.205 1.00 38.32  ? 253  TRP A NE1 1 
ATOM   1376 C  CE2 . TRP A 1 233 ? 0.248  6.033   -22.280 1.00 32.23  ? 253  TRP A CE2 1 
ATOM   1377 C  CE3 . TRP A 1 233 ? 0.550  8.418   -22.040 1.00 36.82  ? 253  TRP A CE3 1 
ATOM   1378 C  CZ2 . TRP A 1 233 ? -0.373 5.940   -21.037 1.00 32.79  ? 253  TRP A CZ2 1 
ATOM   1379 C  CZ3 . TRP A 1 233 ? -0.064 8.324   -20.808 1.00 37.38  ? 253  TRP A CZ3 1 
ATOM   1380 C  CH2 . TRP A 1 233 ? -0.515 7.095   -20.317 1.00 39.64  ? 253  TRP A CH2 1 
ATOM   1381 N  N   . ARG A 1 234 ? 4.269  9.373   -26.430 1.00 46.29  ? 254  ARG A N   1 
ATOM   1382 C  CA  . ARG A 1 234 ? 4.759  10.450  -27.279 1.00 46.35  ? 254  ARG A CA  1 
ATOM   1383 C  C   . ARG A 1 234 ? 5.595  9.900   -28.425 1.00 50.37  ? 254  ARG A C   1 
ATOM   1384 O  O   . ARG A 1 234 ? 5.459  10.344  -29.570 1.00 57.87  ? 254  ARG A O   1 
ATOM   1385 C  CB  . ARG A 1 234 ? 5.570  11.443  -26.448 1.00 46.29  ? 254  ARG A CB  1 
ATOM   1386 C  CG  . ARG A 1 234 ? 5.437  12.893  -26.891 1.00 46.54  ? 254  ARG A CG  1 
ATOM   1387 C  CD  . ARG A 1 234 ? 4.000  13.405  -26.787 1.00 77.01  ? 254  ARG A CD  1 
ATOM   1388 N  NE  . ARG A 1 234 ? 3.362  13.048  -25.523 1.00 70.45  ? 254  ARG A NE  1 
ATOM   1389 C  CZ  . ARG A 1 234 ? 2.343  12.206  -25.390 1.00 58.21  ? 254  ARG A CZ  1 
ATOM   1390 N  NH1 . ARG A 1 234 ? 1.778  11.622  -26.436 1.00 60.83  ? 254  ARG A NH1 1 
ATOM   1391 N  NH2 . ARG A 1 234 ? 1.872  11.947  -24.173 1.00 51.19  ? 254  ARG A NH2 1 
ATOM   1392 N  N   . HIS A 1 235 ? 6.463  8.926   -28.138 1.00 49.57  ? 255  HIS A N   1 
ATOM   1393 C  CA  . HIS A 1 235 ? 7.228  8.296   -29.207 1.00 52.22  ? 255  HIS A CA  1 
ATOM   1394 C  C   . HIS A 1 235 ? 6.313  7.607   -30.206 1.00 54.06  ? 255  HIS A C   1 
ATOM   1395 O  O   . HIS A 1 235 ? 6.622  7.561   -31.402 1.00 63.14  ? 255  HIS A O   1 
ATOM   1396 C  CB  . HIS A 1 235 ? 8.227  7.296   -28.627 1.00 54.50  ? 255  HIS A CB  1 
ATOM   1397 C  CG  . HIS A 1 235 ? 9.356  7.936   -27.883 1.00 46.83  ? 255  HIS A CG  1 
ATOM   1398 N  ND1 . HIS A 1 235 ? 9.452  9.300   -27.710 1.00 47.22  ? 255  HIS A ND1 1 
ATOM   1399 C  CD2 . HIS A 1 235 ? 10.438 7.401   -27.271 1.00 48.59  ? 255  HIS A CD2 1 
ATOM   1400 C  CE1 . HIS A 1 235 ? 10.544 9.578   -27.020 1.00 56.12  ? 255  HIS A CE1 1 
ATOM   1401 N  NE2 . HIS A 1 235 ? 11.161 8.443   -26.742 1.00 59.33  ? 255  HIS A NE2 1 
ATOM   1402 N  N   . ALA A 1 236 ? 5.191  7.061   -29.740 1.00 56.15  ? 256  ALA A N   1 
ATOM   1403 C  CA  . ALA A 1 236 ? 4.218  6.448   -30.633 1.00 53.93  ? 256  ALA A CA  1 
ATOM   1404 C  C   . ALA A 1 236 ? 3.293  7.463   -31.292 1.00 60.88  ? 256  ALA A C   1 
ATOM   1405 O  O   . ALA A 1 236 ? 2.604  7.111   -32.256 1.00 59.13  ? 256  ALA A O   1 
ATOM   1406 C  CB  . ALA A 1 236 ? 3.379  5.422   -29.869 1.00 49.45  ? 256  ALA A CB  1 
ATOM   1407 N  N   A ALA A 1 237 ? 3.257  8.701   -30.800 0.49 63.88  ? 1001 ALA A N   1 
ATOM   1408 N  N   B ALA A 1 237 ? 3.257  8.701   -30.800 0.51 67.82  ? 1001 ALA A N   1 
ATOM   1409 C  CA  A ALA A 1 237 ? 2.390  9.728   -31.365 0.49 58.51  ? 1001 ALA A CA  1 
ATOM   1410 C  CA  B ALA A 1 237 ? 2.390  9.728   -31.365 0.51 60.85  ? 1001 ALA A CA  1 
ATOM   1411 C  C   A ALA A 1 237 ? 3.061  10.466  -32.517 0.49 74.68  ? 1001 ALA A C   1 
ATOM   1412 C  C   B ALA A 1 237 ? 3.061  10.467  -32.517 0.51 81.39  ? 1001 ALA A C   1 
ATOM   1413 O  O   A ALA A 1 237 ? 2.476  10.603  -33.596 0.49 73.26  ? 1001 ALA A O   1 
ATOM   1414 O  O   B ALA A 1 237 ? 2.475  10.604  -33.595 0.51 73.17  ? 1001 ALA A O   1 
ATOM   1415 C  CB  A ALA A 1 237 ? 1.972  10.719  -30.275 0.49 60.36  ? 1001 ALA A CB  1 
ATOM   1416 C  CB  B ALA A 1 237 ? 1.973  10.718  -30.275 0.51 60.28  ? 1001 ALA A CB  1 
ATOM   1417 N  N   . ASP A 1 238 ? 4.288  10.949  -32.305 1.00 64.32  ? 1002 ASP A N   1 
ATOM   1418 C  CA  . ASP A 1 238 ? 4.989  11.659  -33.367 1.00 68.28  ? 1002 ASP A CA  1 
ATOM   1419 C  C   . ASP A 1 238 ? 5.248  10.755  -34.564 1.00 68.70  ? 1002 ASP A C   1 
ATOM   1420 O  O   . ASP A 1 238 ? 5.346  11.239  -35.698 1.00 70.97  ? 1002 ASP A O   1 
ATOM   1421 C  CB  . ASP A 1 238 ? 6.304  12.234  -32.834 1.00 66.85  ? 1002 ASP A CB  1 
ATOM   1422 C  CG  . ASP A 1 238 ? 7.228  11.166  -32.286 1.00 75.25  ? 1002 ASP A CG  1 
ATOM   1423 O  OD1 . ASP A 1 238 ? 6.726  10.098  -31.879 1.00 85.49  ? 1002 ASP A OD1 1 
ATOM   1424 O  OD2 . ASP A 1 238 ? 8.455  11.395  -32.256 1.00 75.08  ? 1002 ASP A OD2 1 
ATOM   1425 N  N   . LEU A 1 239 ? 5.355  9.443   -34.337 1.00 69.15  ? 1003 LEU A N   1 
ATOM   1426 C  CA  . LEU A 1 239 ? 5.586  8.519   -35.442 1.00 65.28  ? 1003 LEU A CA  1 
ATOM   1427 C  C   . LEU A 1 239 ? 4.419  8.524   -36.421 1.00 70.83  ? 1003 LEU A C   1 
ATOM   1428 O  O   . LEU A 1 239 ? 4.622  8.524   -37.641 1.00 75.63  ? 1003 LEU A O   1 
ATOM   1429 C  CB  . LEU A 1 239 ? 5.825  7.109   -34.905 1.00 59.23  ? 1003 LEU A CB  1 
ATOM   1430 C  CG  . LEU A 1 239 ? 7.271  6.607   -34.960 1.00 77.24  ? 1003 LEU A CG  1 
ATOM   1431 C  CD1 . LEU A 1 239 ? 8.226  7.587   -34.285 1.00 75.80  ? 1003 LEU A CD1 1 
ATOM   1432 C  CD2 . LEU A 1 239 ? 7.377  5.222   -34.330 1.00 53.77  ? 1003 LEU A CD2 1 
ATOM   1433 N  N   . GLU A 1 240 ? 3.187  8.526   -35.909 1.00 69.16  ? 1004 GLU A N   1 
ATOM   1434 C  CA  . GLU A 1 240 ? 2.030  8.561   -36.796 1.00 64.20  ? 1004 GLU A CA  1 
ATOM   1435 C  C   . GLU A 1 240 ? 2.013  9.840   -37.624 1.00 66.02  ? 1004 GLU A C   1 
ATOM   1436 O  O   . GLU A 1 240 ? 1.722  9.807   -38.825 1.00 68.47  ? 1004 GLU A O   1 
ATOM   1437 C  CB  . GLU A 1 240 ? 0.741  8.424   -35.985 1.00 63.60  ? 1004 GLU A CB  1 
ATOM   1438 C  CG  . GLU A 1 240 ? -0.519 8.770   -36.767 1.00 72.01  ? 1004 GLU A CG  1 
ATOM   1439 C  CD  . GLU A 1 240 ? -1.789 8.327   -36.065 1.00 73.96  ? 1004 GLU A CD  1 
ATOM   1440 O  OE1 . GLU A 1 240 ? -1.712 7.446   -35.184 1.00 70.87  ? 1004 GLU A OE1 1 
ATOM   1441 O  OE2 . GLU A 1 240 ? -2.868 8.863   -36.396 1.00 88.90  ? 1004 GLU A OE2 1 
ATOM   1442 N  N   . ASP A 1 241 ? 2.333  10.978  -37.003 1.00 62.41  ? 1005 ASP A N   1 
ATOM   1443 C  CA  . ASP A 1 241 ? 2.351  12.234  -37.744 1.00 63.38  ? 1005 ASP A CA  1 
ATOM   1444 C  C   . ASP A 1 241 ? 3.362  12.181  -38.882 1.00 64.40  ? 1005 ASP A C   1 
ATOM   1445 O  O   . ASP A 1 241 ? 3.080  12.640  -39.995 1.00 65.92  ? 1005 ASP A O   1 
ATOM   1446 C  CB  . ASP A 1 241 ? 2.659  13.396  -36.800 1.00 72.52  ? 1005 ASP A CB  1 
ATOM   1447 C  CG  . ASP A 1 241 ? 1.524  13.681  -35.836 1.00 62.77  ? 1005 ASP A CG  1 
ATOM   1448 O  OD1 . ASP A 1 241 ? 0.350  13.584  -36.253 1.00 70.35  ? 1005 ASP A OD1 1 
ATOM   1449 O  OD2 . ASP A 1 241 ? 1.803  14.000  -34.661 1.00 53.18  ? 1005 ASP A OD2 1 
ATOM   1450 N  N   . ASN A 1 242 ? 4.544  11.617  -38.625 1.00 59.10  ? 1006 ASN A N   1 
ATOM   1451 C  CA  . ASN A 1 242 ? 5.523  11.444  -39.693 1.00 56.87  ? 1006 ASN A CA  1 
ATOM   1452 C  C   . ASN A 1 242 ? 4.974  10.549  -40.794 1.00 54.00  ? 1006 ASN A C   1 
ATOM   1453 O  O   . ASN A 1 242 ? 5.143  10.839  -41.984 1.00 55.39  ? 1006 ASN A O   1 
ATOM   1454 C  CB  . ASN A 1 242 ? 6.818  10.862  -39.131 1.00 57.09  ? 1006 ASN A CB  1 
ATOM   1455 C  CG  . ASN A 1 242 ? 7.485  11.782  -38.130 1.00 63.37  ? 1006 ASN A CG  1 
ATOM   1456 O  OD1 . ASN A 1 242 ? 7.691  11.416  -36.974 1.00 70.85  ? 1006 ASN A OD1 1 
ATOM   1457 N  ND2 . ASN A 1 242 ? 7.827  12.987  -38.571 1.00 68.46  ? 1006 ASN A ND2 1 
ATOM   1458 N  N   . TRP A 1 243 ? 4.310  9.455   -40.417 1.00 55.57  ? 1007 TRP A N   1 
ATOM   1459 C  CA  . TRP A 1 243 ? 3.700  8.580   -41.412 1.00 47.82  ? 1007 TRP A CA  1 
ATOM   1460 C  C   . TRP A 1 243 ? 2.654  9.326   -42.231 1.00 50.41  ? 1007 TRP A C   1 
ATOM   1461 O  O   . TRP A 1 243 ? 2.614  9.201   -43.460 1.00 49.92  ? 1007 TRP A O   1 
ATOM   1462 C  CB  . TRP A 1 243 ? 3.085  7.363   -40.718 1.00 52.81  ? 1007 TRP A CB  1 
ATOM   1463 C  CG  . TRP A 1 243 ? 2.137  6.556   -41.568 1.00 65.17  ? 1007 TRP A CG  1 
ATOM   1464 C  CD1 . TRP A 1 243 ? 0.799  6.777   -41.743 1.00 65.05  ? 1007 TRP A CD1 1 
ATOM   1465 C  CD2 . TRP A 1 243 ? 2.452  5.389   -42.340 1.00 62.27  ? 1007 TRP A CD2 1 
ATOM   1466 N  NE1 . TRP A 1 243 ? 0.266  5.827   -42.580 1.00 62.91  ? 1007 TRP A NE1 1 
ATOM   1467 C  CE2 . TRP A 1 243 ? 1.259  4.964   -42.960 1.00 60.52  ? 1007 TRP A CE2 1 
ATOM   1468 C  CE3 . TRP A 1 243 ? 3.626  4.666   -42.570 1.00 61.15  ? 1007 TRP A CE3 1 
ATOM   1469 C  CZ2 . TRP A 1 243 ? 1.208  3.847   -43.794 1.00 63.65  ? 1007 TRP A CZ2 1 
ATOM   1470 C  CZ3 . TRP A 1 243 ? 3.572  3.558   -43.401 1.00 62.90  ? 1007 TRP A CZ3 1 
ATOM   1471 C  CH2 . TRP A 1 243 ? 2.372  3.161   -44.003 1.00 59.89  ? 1007 TRP A CH2 1 
ATOM   1472 N  N   . GLU A 1 244 ? 1.806  10.118  -41.571 1.00 50.93  ? 1008 GLU A N   1 
ATOM   1473 C  CA  . GLU A 1 244 ? 0.782  10.862  -42.297 1.00 51.71  ? 1008 GLU A CA  1 
ATOM   1474 C  C   . GLU A 1 244 ? 1.415  11.860  -43.256 1.00 52.54  ? 1008 GLU A C   1 
ATOM   1475 O  O   . GLU A 1 244 ? 1.081  11.895  -44.445 1.00 62.37  ? 1008 GLU A O   1 
ATOM   1476 C  CB  . GLU A 1 244 ? -0.149 11.576  -41.318 1.00 60.05  ? 1008 GLU A CB  1 
ATOM   1477 C  CG  . GLU A 1 244 ? -1.018 10.645  -40.493 1.00 54.54  ? 1008 GLU A CG  1 
ATOM   1478 C  CD  . GLU A 1 244 ? -1.930 11.396  -39.544 1.00 49.73  ? 1008 GLU A CD  1 
ATOM   1479 O  OE1 . GLU A 1 244 ? -2.036 12.632  -39.676 1.00 51.62  ? 1008 GLU A OE1 1 
ATOM   1480 O  OE2 . GLU A 1 244 ? -2.539 10.751  -38.666 1.00 54.55  ? 1008 GLU A OE2 1 
ATOM   1481 N  N   . THR A 1 245 ? 2.344  12.677  -42.755 1.00 50.14  ? 1009 THR A N   1 
ATOM   1482 C  CA  . THR A 1 245 ? 3.019  13.634  -43.624 1.00 52.59  ? 1009 THR A CA  1 
ATOM   1483 C  C   . THR A 1 245 ? 3.810  12.918  -44.709 1.00 53.60  ? 1009 THR A C   1 
ATOM   1484 O  O   . THR A 1 245 ? 3.802  13.334  -45.874 1.00 57.58  ? 1009 THR A O   1 
ATOM   1485 C  CB  . THR A 1 245 ? 3.939  14.538  -42.804 1.00 52.92  ? 1009 THR A CB  1 
ATOM   1486 O  OG1 . THR A 1 245 ? 4.901  13.740  -42.102 1.00 47.95  ? 1009 THR A OG1 1 
ATOM   1487 C  CG2 . THR A 1 245 ? 3.132  15.361  -41.808 1.00 48.33  ? 1009 THR A CG2 1 
ATOM   1488 N  N   . LEU A 1 246 ? 4.493  11.831  -44.348 1.00 55.97  ? 1010 LEU A N   1 
ATOM   1489 C  CA  . LEU A 1 246 ? 5.268  11.091  -45.337 1.00 57.47  ? 1010 LEU A CA  1 
ATOM   1490 C  C   . LEU A 1 246 ? 4.371  10.575  -46.455 1.00 51.51  ? 1010 LEU A C   1 
ATOM   1491 O  O   . LEU A 1 246 ? 4.721  10.672  -47.637 1.00 50.61  ? 1010 LEU A O   1 
ATOM   1492 C  CB  . LEU A 1 246 ? 6.005  9.934   -44.659 1.00 55.15  ? 1010 LEU A CB  1 
ATOM   1493 C  CG  . LEU A 1 246 ? 7.139  9.283   -45.448 1.00 50.67  ? 1010 LEU A CG  1 
ATOM   1494 C  CD1 . LEU A 1 246 ? 8.458  9.967   -45.124 1.00 64.32  ? 1010 LEU A CD1 1 
ATOM   1495 C  CD2 . LEU A 1 246 ? 7.212  7.795   -45.151 1.00 54.77  ? 1010 LEU A CD2 1 
ATOM   1496 N  N   . ASN A 1 247 ? 3.203  10.033  -46.101 1.00 53.76  ? 1011 ASN A N   1 
ATOM   1497 C  CA  . ASN A 1 247 ? 2.278  9.540   -47.118 1.00 50.11  ? 1011 ASN A CA  1 
ATOM   1498 C  C   . ASN A 1 247 ? 1.618  10.688  -47.870 1.00 52.03  ? 1011 ASN A C   1 
ATOM   1499 O  O   . ASN A 1 247 ? 1.432  10.611  -49.090 1.00 51.96  ? 1011 ASN A O   1 
ATOM   1500 C  CB  . ASN A 1 247 ? 1.217  8.646   -46.477 1.00 46.47  ? 1011 ASN A CB  1 
ATOM   1501 C  CG  . ASN A 1 247 ? 1.772  7.309   -46.032 1.00 54.74  ? 1011 ASN A CG  1 
ATOM   1502 O  OD1 . ASN A 1 247 ? 2.979  7.156   -45.836 1.00 54.38  ? 1011 ASN A OD1 1 
ATOM   1503 N  ND2 . ASN A 1 247 ? 0.891  6.328   -45.874 1.00 57.43  ? 1011 ASN A ND2 1 
ATOM   1504 N  N   . ASP A 1 248 ? 1.252  11.759  -47.162 1.00 55.45  ? 1012 ASP A N   1 
ATOM   1505 C  CA  . ASP A 1 248 ? 0.694  12.925  -47.836 1.00 46.71  ? 1012 ASP A CA  1 
ATOM   1506 C  C   . ASP A 1 248 ? 1.697  13.510  -48.819 1.00 54.69  ? 1012 ASP A C   1 
ATOM   1507 O  O   . ASP A 1 248 ? 1.331  13.904  -49.931 1.00 58.56  ? 1012 ASP A O   1 
ATOM   1508 C  CB  . ASP A 1 248 ? 0.272  13.978  -46.810 1.00 44.91  ? 1012 ASP A CB  1 
ATOM   1509 C  CG  . ASP A 1 248 ? -0.832 13.492  -45.891 1.00 49.54  ? 1012 ASP A CG  1 
ATOM   1510 O  OD1 . ASP A 1 248 ? -1.347 12.375  -46.113 1.00 49.69  ? 1012 ASP A OD1 1 
ATOM   1511 O  OD2 . ASP A 1 248 ? -1.183 14.227  -44.943 1.00 43.26  ? 1012 ASP A OD2 1 
ATOM   1512 N  N   . ASN A 1 249 ? 2.972  13.569  -48.426 1.00 56.20  ? 1013 ASN A N   1 
ATOM   1513 C  CA  . ASN A 1 249 ? 4.002  14.072  -49.329 1.00 48.78  ? 1013 ASN A CA  1 
ATOM   1514 C  C   . ASN A 1 249 ? 4.126  13.195  -50.567 1.00 53.92  ? 1013 ASN A C   1 
ATOM   1515 O  O   . ASN A 1 249 ? 4.269  13.702  -51.685 1.00 65.77  ? 1013 ASN A O   1 
ATOM   1516 C  CB  . ASN A 1 249 ? 5.341  14.159  -48.600 1.00 50.08  ? 1013 ASN A CB  1 
ATOM   1517 C  CG  . ASN A 1 249 ? 5.373  15.274  -47.575 1.00 57.26  ? 1013 ASN A CG  1 
ATOM   1518 O  OD1 . ASN A 1 249 ? 5.671  15.050  -46.401 1.00 59.69  ? 1013 ASN A OD1 1 
ATOM   1519 N  ND2 . ASN A 1 249 ? 5.062  16.487  -48.016 1.00 65.78  ? 1013 ASN A ND2 1 
ATOM   1520 N  N   . LEU A 1 250 ? 4.074  11.874  -50.391 1.00 56.34  ? 1014 LEU A N   1 
ATOM   1521 C  CA  . LEU A 1 250 ? 4.160  10.981  -51.540 1.00 56.21  ? 1014 LEU A CA  1 
ATOM   1522 C  C   . LEU A 1 250 ? 2.997  11.203  -52.498 1.00 58.16  ? 1014 LEU A C   1 
ATOM   1523 O  O   . LEU A 1 250 ? 3.188  11.246  -53.719 1.00 63.48  ? 1014 LEU A O   1 
ATOM   1524 C  CB  . LEU A 1 250 ? 4.199  9.527   -51.069 1.00 54.71  ? 1014 LEU A CB  1 
ATOM   1525 C  CG  . LEU A 1 250 ? 5.574  9.010   -50.647 1.00 48.82  ? 1014 LEU A CG  1 
ATOM   1526 C  CD1 . LEU A 1 250 ? 5.432  7.760   -49.800 1.00 51.85  ? 1014 LEU A CD1 1 
ATOM   1527 C  CD2 . LEU A 1 250 ? 6.433  8.729   -51.869 1.00 52.15  ? 1014 LEU A CD2 1 
ATOM   1528 N  N   . LYS A 1 251 ? 1.784  11.353  -51.964 1.00 57.71  ? 1015 LYS A N   1 
ATOM   1529 C  CA  . LYS A 1 251 ? 0.617  11.521  -52.823 1.00 59.64  ? 1015 LYS A CA  1 
ATOM   1530 C  C   . LYS A 1 251 ? 0.649  12.856  -53.556 1.00 68.95  ? 1015 LYS A C   1 
ATOM   1531 O  O   . LYS A 1 251 ? 0.381  12.914  -54.761 1.00 71.09  ? 1015 LYS A O   1 
ATOM   1532 C  CB  . LYS A 1 251 ? -0.660 11.393  -51.997 1.00 49.98  ? 1015 LYS A CB  1 
ATOM   1533 C  CG  . LYS A 1 251 ? -1.037 9.954   -51.696 1.00 62.84  ? 1015 LYS A CG  1 
ATOM   1534 C  CD  . LYS A 1 251 ? -1.968 9.848   -50.500 1.00 63.64  ? 1015 LYS A CD  1 
ATOM   1535 C  CE  . LYS A 1 251 ? -2.385 8.408   -50.254 1.00 58.23  ? 1015 LYS A CE  1 
ATOM   1536 N  NZ  . LYS A 1 251 ? -3.261 7.884   -51.338 1.00 56.28  ? 1015 LYS A NZ  1 
ATOM   1537 N  N   . VAL A 1 252 ? 0.974  13.942  -52.850 1.00 68.31  ? 1016 VAL A N   1 
ATOM   1538 C  CA  . VAL A 1 252 ? 1.023  15.245  -53.501 1.00 70.38  ? 1016 VAL A CA  1 
ATOM   1539 C  C   . VAL A 1 252 ? 2.142  15.306  -54.531 1.00 73.58  ? 1016 VAL A C   1 
ATOM   1540 O  O   . VAL A 1 252 ? 2.074  16.115  -55.465 1.00 77.63  ? 1016 VAL A O   1 
ATOM   1541 C  CB  . VAL A 1 252 ? 1.182  16.377  -52.468 1.00 61.99  ? 1016 VAL A CB  1 
ATOM   1542 C  CG1 . VAL A 1 252 ? 0.002  16.388  -51.499 1.00 61.68  ? 1016 VAL A CG1 1 
ATOM   1543 C  CG2 . VAL A 1 252 ? 2.496  16.243  -51.726 1.00 57.66  ? 1016 VAL A CG2 1 
ATOM   1544 N  N   . ILE A 1 253 ? 3.175  14.473  -54.388 1.00 67.05  ? 1017 ILE A N   1 
ATOM   1545 C  CA  . ILE A 1 253 ? 4.224  14.422  -55.402 1.00 72.82  ? 1017 ILE A CA  1 
ATOM   1546 C  C   . ILE A 1 253 ? 3.631  14.031  -56.748 1.00 71.53  ? 1017 ILE A C   1 
ATOM   1547 O  O   . ILE A 1 253 ? 3.997  14.586  -57.792 1.00 78.50  ? 1017 ILE A O   1 
ATOM   1548 C  CB  . ILE A 1 253 ? 5.342  13.456  -54.969 1.00 68.65  ? 1017 ILE A CB  1 
ATOM   1549 C  CG1 . ILE A 1 253 ? 6.263  14.144  -53.958 1.00 65.83  ? 1017 ILE A CG1 1 
ATOM   1550 C  CG2 . ILE A 1 253 ? 6.132  12.974  -56.178 1.00 71.65  ? 1017 ILE A CG2 1 
ATOM   1551 C  CD1 . ILE A 1 253 ? 7.201  13.205  -53.232 1.00 69.30  ? 1017 ILE A CD1 1 
ATOM   1552 N  N   . GLU A 1 254 ? 2.706  13.071  -56.745 1.00 66.10  ? 1018 GLU A N   1 
ATOM   1553 C  CA  . GLU A 1 254 ? 2.056  12.662  -57.984 1.00 70.87  ? 1018 GLU A CA  1 
ATOM   1554 C  C   . GLU A 1 254 ? 1.118  13.741  -58.510 1.00 74.74  ? 1018 GLU A C   1 
ATOM   1555 O  O   . GLU A 1 254 ? 0.956  13.881  -59.727 1.00 74.73  ? 1018 GLU A O   1 
ATOM   1556 C  CB  . GLU A 1 254 ? 1.288  11.361  -57.759 1.00 65.07  ? 1018 GLU A CB  1 
ATOM   1557 C  CG  . GLU A 1 254 ? 2.136  10.236  -57.184 1.00 66.45  ? 1018 GLU A CG  1 
ATOM   1558 C  CD  . GLU A 1 254 ? 1.302  9.082   -56.664 1.00 83.09  ? 1018 GLU A CD  1 
ATOM   1559 O  OE1 . GLU A 1 254 ? 0.059  9.151   -56.761 1.00 88.54  ? 1018 GLU A OE1 1 
ATOM   1560 O  OE2 . GLU A 1 254 ? 1.892  8.106   -56.154 1.00 88.42  ? 1018 GLU A OE2 1 
ATOM   1561 N  N   . LYS A 1 255 ? 0.500  14.510  -57.616 1.00 80.58  ? 1019 LYS A N   1 
ATOM   1562 C  CA  . LYS A 1 255 ? -0.499 15.508  -58.000 1.00 77.94  ? 1019 LYS A CA  1 
ATOM   1563 C  C   . LYS A 1 255 ? 0.148  16.886  -58.165 1.00 89.76  ? 1019 LYS A C   1 
ATOM   1564 O  O   . LYS A 1 255 ? -0.214 17.861  -57.504 1.00 98.61  ? 1019 LYS A O   1 
ATOM   1565 C  CB  . LYS A 1 255 ? -1.620 15.548  -56.966 1.00 78.28  ? 1019 LYS A CB  1 
ATOM   1566 C  CG  . LYS A 1 255 ? -2.237 14.191  -56.648 1.00 72.67  ? 1019 LYS A CG  1 
ATOM   1567 C  CD  . LYS A 1 255 ? -3.034 13.647  -57.819 1.00 56.28  ? 1019 LYS A CD  1 
ATOM   1568 C  CE  . LYS A 1 255 ? -3.676 12.313  -57.480 1.00 49.41  ? 1019 LYS A CE  1 
ATOM   1569 N  NZ  . LYS A 1 255 ? -4.530 11.813  -58.589 1.00 47.75  ? 1019 LYS A NZ  1 
ATOM   1570 N  N   . ALA A 1 256 ? 1.127  16.957  -59.065 1.00 90.51  ? 1020 ALA A N   1 
ATOM   1571 C  CA  . ALA A 1 256 ? 1.783  18.225  -59.357 1.00 98.91  ? 1020 ALA A CA  1 
ATOM   1572 C  C   . ALA A 1 256 ? 2.668  18.062  -60.583 1.00 100.47 ? 1020 ALA A C   1 
ATOM   1573 O  O   . ALA A 1 256 ? 3.375  17.059  -60.711 1.00 103.13 ? 1020 ALA A O   1 
ATOM   1574 C  CB  . ALA A 1 256 ? 2.616  18.707  -58.163 1.00 101.28 ? 1020 ALA A CB  1 
ATOM   1575 N  N   . ASP A 1 257 ? 2.624  19.050  -61.475 1.00 93.66  ? 1021 ASP A N   1 
ATOM   1576 C  CA  . ASP A 1 257 ? 3.456  19.063  -62.671 1.00 89.89  ? 1021 ASP A CA  1 
ATOM   1577 C  C   . ASP A 1 257 ? 4.634  20.024  -62.562 1.00 91.37  ? 1021 ASP A C   1 
ATOM   1578 O  O   . ASP A 1 257 ? 5.391  20.166  -63.527 1.00 93.19  ? 1021 ASP A O   1 
ATOM   1579 C  CB  . ASP A 1 257 ? 2.611  19.424  -63.898 1.00 77.19  ? 1021 ASP A CB  1 
ATOM   1580 C  CG  . ASP A 1 257 ? 3.271  19.015  -65.203 1.00 68.02  ? 1021 ASP A CG  1 
ATOM   1581 O  OD1 . ASP A 1 257 ? 4.330  18.355  -65.154 1.00 60.36  ? 1021 ASP A OD1 1 
ATOM   1582 O  OD2 . ASP A 1 257 ? 2.731  19.351  -66.278 1.00 71.77  ? 1021 ASP A OD2 1 
ATOM   1583 N  N   . ASN A 1 258 ? 4.808  20.684  -61.419 1.00 79.26  ? 1022 ASN A N   1 
ATOM   1584 C  CA  . ASN A 1 258 ? 5.935  21.580  -61.205 1.00 75.03  ? 1022 ASN A CA  1 
ATOM   1585 C  C   . ASN A 1 258 ? 7.084  20.835  -60.542 1.00 69.39  ? 1022 ASN A C   1 
ATOM   1586 O  O   . ASN A 1 258 ? 6.875  20.020  -59.639 1.00 75.61  ? 1022 ASN A O   1 
ATOM   1587 C  CB  . ASN A 1 258 ? 5.526  22.771  -60.337 1.00 75.92  ? 1022 ASN A CB  1 
ATOM   1588 C  CG  . ASN A 1 258 ? 4.955  23.919  -61.149 1.00 99.98  ? 1022 ASN A CG  1 
ATOM   1589 O  OD1 . ASN A 1 258 ? 5.696  24.745  -61.686 1.00 93.96  ? 1022 ASN A OD1 1 
ATOM   1590 N  ND2 . ASN A 1 258 ? 3.632  23.981  -61.238 1.00 104.83 ? 1022 ASN A ND2 1 
ATOM   1591 N  N   . ALA A 1 259 ? 8.304  21.124  -60.996 1.00 65.69  ? 1023 ALA A N   1 
ATOM   1592 C  CA  . ALA A 1 259 ? 9.489  20.500  -60.423 1.00 62.39  ? 1023 ALA A CA  1 
ATOM   1593 C  C   . ALA A 1 259 ? 9.769  20.960  -58.999 1.00 62.23  ? 1023 ALA A C   1 
ATOM   1594 O  O   . ALA A 1 259 ? 10.599 20.345  -58.322 1.00 62.09  ? 1023 ALA A O   1 
ATOM   1595 C  CB  . ALA A 1 259 ? 10.707 20.788  -61.301 1.00 73.49  ? 1023 ALA A CB  1 
ATOM   1596 N  N   . ALA A 1 260 ? 9.112  22.022  -58.534 1.00 62.33  ? 1024 ALA A N   1 
ATOM   1597 C  CA  . ALA A 1 260 ? 9.310  22.504  -57.174 1.00 64.54  ? 1024 ALA A CA  1 
ATOM   1598 C  C   . ALA A 1 260 ? 8.418  21.780  -56.177 1.00 60.29  ? 1024 ALA A C   1 
ATOM   1599 O  O   . ALA A 1 260 ? 8.857  21.477  -55.062 1.00 60.19  ? 1024 ALA A O   1 
ATOM   1600 C  CB  . ALA A 1 260 ? 9.050  24.010  -57.104 1.00 77.88  ? 1024 ALA A CB  1 
ATOM   1601 N  N   . GLN A 1 261 ? 7.172  21.492  -56.560 1.00 61.35  ? 1025 GLN A N   1 
ATOM   1602 C  CA  . GLN A 1 261 ? 6.280  20.757  -55.669 1.00 60.10  ? 1025 GLN A CA  1 
ATOM   1603 C  C   . GLN A 1 261 ? 6.903  19.434  -55.248 1.00 62.59  ? 1025 GLN A C   1 
ATOM   1604 O  O   . GLN A 1 261 ? 6.709  18.980  -54.114 1.00 58.75  ? 1025 GLN A O   1 
ATOM   1605 C  CB  . GLN A 1 261 ? 4.934  20.522  -56.354 1.00 56.47  ? 1025 GLN A CB  1 
ATOM   1606 N  N   . VAL A 1 262 ? 7.656  18.801  -56.150 1.00 64.83  ? 1026 VAL A N   1 
ATOM   1607 C  CA  . VAL A 1 262 ? 8.374  17.580  -55.797 1.00 67.82  ? 1026 VAL A CA  1 
ATOM   1608 C  C   . VAL A 1 262 ? 9.439  17.873  -54.748 1.00 68.41  ? 1026 VAL A C   1 
ATOM   1609 O  O   . VAL A 1 262 ? 9.603  17.118  -53.782 1.00 79.84  ? 1026 VAL A O   1 
ATOM   1610 C  CB  . VAL A 1 262 ? 8.981  16.938  -57.058 1.00 73.11  ? 1026 VAL A CB  1 
ATOM   1611 C  CG1 . VAL A 1 262 ? 9.904  15.786  -56.684 1.00 73.97  ? 1026 VAL A CG1 1 
ATOM   1612 C  CG2 . VAL A 1 262 ? 7.878  16.461  -57.992 1.00 84.24  ? 1026 VAL A CG2 1 
ATOM   1613 N  N   . LYS A 1 263 ? 10.182 18.968  -54.920 1.00 62.94  ? 1027 LYS A N   1 
ATOM   1614 C  CA  . LYS A 1 263 ? 11.232 19.292  -53.959 1.00 66.56  ? 1027 LYS A CA  1 
ATOM   1615 C  C   . LYS A 1 263 ? 10.648 19.555  -52.575 1.00 68.33  ? 1027 LYS A C   1 
ATOM   1616 O  O   . LYS A 1 263 ? 11.183 19.078  -51.567 1.00 74.62  ? 1027 LYS A O   1 
ATOM   1617 C  CB  . LYS A 1 263 ? 12.038 20.500  -54.441 1.00 68.86  ? 1027 LYS A CB  1 
ATOM   1618 C  CG  . LYS A 1 263 ? 13.335 20.709  -53.663 1.00 79.10  ? 1027 LYS A CG  1 
ATOM   1619 C  CD  . LYS A 1 263 ? 13.683 22.182  -53.471 1.00 84.46  ? 1027 LYS A CD  1 
ATOM   1620 C  CE  . LYS A 1 263 ? 14.471 22.746  -54.644 1.00 86.31  ? 1027 LYS A CE  1 
ATOM   1621 N  NZ  . LYS A 1 263 ? 15.064 24.076  -54.319 1.00 76.17  ? 1027 LYS A NZ  1 
ATOM   1622 N  N   . ASP A 1 264 ? 9.545  20.304  -52.505 1.00 66.08  ? 1028 ASP A N   1 
ATOM   1623 C  CA  . ASP A 1 264 ? 8.945  20.618  -51.211 1.00 62.74  ? 1028 ASP A CA  1 
ATOM   1624 C  C   . ASP A 1 264 ? 8.520  19.351  -50.482 1.00 68.26  ? 1028 ASP A C   1 
ATOM   1625 O  O   . ASP A 1 264 ? 8.809  19.178  -49.292 1.00 71.22  ? 1028 ASP A O   1 
ATOM   1626 C  CB  . ASP A 1 264 ? 7.744  21.544  -51.399 1.00 63.04  ? 1028 ASP A CB  1 
ATOM   1627 C  CG  . ASP A 1 264 ? 8.144  22.935  -51.831 1.00 71.83  ? 1028 ASP A CG  1 
ATOM   1628 O  OD1 . ASP A 1 264 ? 8.619  23.089  -52.976 1.00 73.70  ? 1028 ASP A OD1 1 
ATOM   1629 O  OD2 . ASP A 1 264 ? 7.985  23.875  -51.025 1.00 79.26  ? 1028 ASP A OD2 1 
ATOM   1630 N  N   . ALA A 1 265 ? 7.827  18.452  -51.182 1.00 64.54  ? 1029 ALA A N   1 
ATOM   1631 C  CA  . ALA A 1 265 ? 7.352  17.230  -50.545 1.00 62.78  ? 1029 ALA A CA  1 
ATOM   1632 C  C   . ALA A 1 265 ? 8.518  16.378  -50.061 1.00 69.63  ? 1029 ALA A C   1 
ATOM   1633 O  O   . ALA A 1 265 ? 8.504  15.866  -48.936 1.00 73.34  ? 1029 ALA A O   1 
ATOM   1634 C  CB  . ALA A 1 265 ? 6.478  16.443  -51.519 1.00 57.24  ? 1029 ALA A CB  1 
ATOM   1635 N  N   . LEU A 1 266 ? 9.545  16.221  -50.897 1.00 67.50  ? 1030 LEU A N   1 
ATOM   1636 C  CA  . LEU A 1 266 ? 10.710 15.444  -50.490 1.00 70.82  ? 1030 LEU A CA  1 
ATOM   1637 C  C   . LEU A 1 266 ? 11.410 16.088  -49.301 1.00 76.70  ? 1030 LEU A C   1 
ATOM   1638 O  O   . LEU A 1 266 ? 11.834 15.392  -48.370 1.00 76.42  ? 1030 LEU A O   1 
ATOM   1639 C  CB  . LEU A 1 266 ? 11.676 15.295  -51.665 1.00 75.14  ? 1030 LEU A CB  1 
ATOM   1640 C  CG  . LEU A 1 266 ? 11.261 14.296  -52.744 1.00 68.21  ? 1030 LEU A CG  1 
ATOM   1641 C  CD1 . LEU A 1 266 ? 12.027 14.556  -54.033 1.00 64.87  ? 1030 LEU A CD1 1 
ATOM   1642 C  CD2 . LEU A 1 266 ? 11.483 12.868  -52.263 1.00 70.64  ? 1030 LEU A CD2 1 
ATOM   1643 N  N   . THR A 1 267 ? 11.545 17.416  -49.314 1.00 84.39  ? 1031 THR A N   1 
ATOM   1644 C  CA  . THR A 1 267 ? 12.166 18.104  -48.187 1.00 90.86  ? 1031 THR A CA  1 
ATOM   1645 C  C   . THR A 1 267 ? 11.332 17.938  -46.922 1.00 84.16  ? 1031 THR A C   1 
ATOM   1646 O  O   . THR A 1 267 ? 11.864 17.636  -45.848 1.00 90.96  ? 1031 THR A O   1 
ATOM   1647 C  CB  . THR A 1 267 ? 12.364 19.584  -48.518 1.00 86.44  ? 1031 THR A CB  1 
ATOM   1648 O  OG1 . THR A 1 267 ? 11.153 20.124  -49.061 1.00 92.78  ? 1031 THR A OG1 1 
ATOM   1649 C  CG2 . THR A 1 267 ? 13.496 19.764  -49.523 1.00 81.60  ? 1031 THR A CG2 1 
ATOM   1650 N  N   . LYS A 1 268 ? 10.014 18.131  -47.029 1.00 66.09  ? 1032 LYS A N   1 
ATOM   1651 C  CA  . LYS A 1 268 ? 9.135  17.832  -45.906 1.00 65.86  ? 1032 LYS A CA  1 
ATOM   1652 C  C   . LYS A 1 268 ? 9.089  16.340  -45.611 1.00 72.10  ? 1032 LYS A C   1 
ATOM   1653 O  O   . LYS A 1 268 ? 8.742  15.949  -44.492 1.00 73.17  ? 1032 LYS A O   1 
ATOM   1654 C  CB  . LYS A 1 268 ? 7.721  18.349  -46.182 1.00 61.10  ? 1032 LYS A CB  1 
ATOM   1655 C  CG  . LYS A 1 268 ? 7.621  19.859  -46.349 1.00 79.65  ? 1032 LYS A CG  1 
ATOM   1656 C  CD  . LYS A 1 268 ? 6.182  20.293  -46.610 1.00 74.94  ? 1032 LYS A CD  1 
ATOM   1657 C  CE  . LYS A 1 268 ? 6.074  21.791  -46.877 1.00 75.50  ? 1032 LYS A CE  1 
ATOM   1658 N  NZ  . LYS A 1 268 ? 5.837  22.584  -45.638 1.00 77.82  ? 1032 LYS A NZ  1 
ATOM   1659 N  N   . MET A 1 269 ? 9.428  15.504  -46.594 1.00 71.67  ? 1033 MET A N   1 
ATOM   1660 C  CA  . MET A 1 269 ? 9.477  14.063  -46.384 1.00 67.86  ? 1033 MET A CA  1 
ATOM   1661 C  C   . MET A 1 269 ? 10.771 13.647  -45.693 1.00 73.70  ? 1033 MET A C   1 
ATOM   1662 O  O   . MET A 1 269 ? 10.753 12.793  -44.800 1.00 72.91  ? 1033 MET A O   1 
ATOM   1663 C  CB  . MET A 1 269 ? 9.333  13.348  -47.727 1.00 69.68  ? 1033 MET A CB  1 
ATOM   1664 C  CG  . MET A 1 269 ? 9.179  11.845  -47.641 1.00 67.36  ? 1033 MET A CG  1 
ATOM   1665 S  SD  . MET A 1 269 ? 9.272  11.064  -49.265 1.00 52.28  ? 1033 MET A SD  1 
ATOM   1666 C  CE  . MET A 1 269 ? 7.995  11.953  -50.149 1.00 51.63  ? 1033 MET A CE  1 
ATOM   1667 N  N   . ARG A 1 270 ? 11.901 14.240  -46.091 1.00 70.84  ? 1034 ARG A N   1 
ATOM   1668 C  CA  . ARG A 1 270 ? 13.170 13.930  -45.438 1.00 66.21  ? 1034 ARG A CA  1 
ATOM   1669 C  C   . ARG A 1 270 ? 13.146 14.347  -43.974 1.00 69.53  ? 1034 ARG A C   1 
ATOM   1670 O  O   . ARG A 1 270 ? 13.643 13.620  -43.105 1.00 76.37  ? 1034 ARG A O   1 
ATOM   1671 C  CB  . ARG A 1 270 ? 14.323 14.623  -46.165 1.00 68.16  ? 1034 ARG A CB  1 
ATOM   1672 C  CG  . ARG A 1 270 ? 15.708 14.177  -45.701 1.00 80.65  ? 1034 ARG A CG  1 
ATOM   1673 C  CD  . ARG A 1 270 ? 16.758 15.252  -45.943 1.00 74.08  ? 1034 ARG A CD  1 
ATOM   1674 N  NE  . ARG A 1 270 ? 18.061 14.881  -45.400 1.00 78.21  ? 1034 ARG A NE  1 
ATOM   1675 C  CZ  . ARG A 1 270 ? 19.111 14.504  -46.120 1.00 80.43  ? 1034 ARG A CZ  1 
ATOM   1676 N  NH1 . ARG A 1 270 ? 19.067 14.450  -47.442 1.00 78.84  ? 1034 ARG A NH1 1 
ATOM   1677 N  NH2 . ARG A 1 270 ? 20.241 14.179  -45.496 1.00 73.03  ? 1034 ARG A NH2 1 
ATOM   1678 N  N   . ALA A 1 271 ? 12.578 15.519  -43.682 1.00 79.43  ? 1035 ALA A N   1 
ATOM   1679 C  CA  . ALA A 1 271 ? 12.482 15.964  -42.296 1.00 76.88  ? 1035 ALA A CA  1 
ATOM   1680 C  C   . ALA A 1 271 ? 11.654 14.992  -41.467 1.00 84.98  ? 1035 ALA A C   1 
ATOM   1681 O  O   . ALA A 1 271 ? 12.018 14.665  -40.332 1.00 82.21  ? 1035 ALA A O   1 
ATOM   1682 C  CB  . ALA A 1 271 ? 11.880 17.367  -42.239 1.00 73.42  ? 1035 ALA A CB  1 
ATOM   1683 N  N   . ALA A 1 272 ? 10.535 14.517  -42.019 1.00 75.18  ? 1036 ALA A N   1 
ATOM   1684 C  CA  . ALA A 1 272 ? 9.726  13.529  -41.314 1.00 66.35  ? 1036 ALA A CA  1 
ATOM   1685 C  C   . ALA A 1 272 ? 10.507 12.241  -41.091 1.00 70.96  ? 1036 ALA A C   1 
ATOM   1686 O  O   . ALA A 1 272 ? 10.418 11.628  -40.021 1.00 72.49  ? 1036 ALA A O   1 
ATOM   1687 C  CB  . ALA A 1 272 ? 8.443  13.249  -42.095 1.00 68.41  ? 1036 ALA A CB  1 
ATOM   1688 N  N   . ALA A 1 273 ? 11.274 11.810  -42.096 1.00 74.76  ? 1037 ALA A N   1 
ATOM   1689 C  CA  . ALA A 1 273 ? 12.103 10.621  -41.934 1.00 71.37  ? 1037 ALA A CA  1 
ATOM   1690 C  C   . ALA A 1 273 ? 13.160 10.829  -40.856 1.00 85.21  ? 1037 ALA A C   1 
ATOM   1691 O  O   . ALA A 1 273 ? 13.444 9.918   -40.070 1.00 86.42  ? 1037 ALA A O   1 
ATOM   1692 C  CB  . ALA A 1 273 ? 12.761 10.259  -43.264 1.00 72.61  ? 1037 ALA A CB  1 
ATOM   1693 N  N   . LEU A 1 274 ? 13.759 12.021  -40.808 1.00 89.34  ? 1038 LEU A N   1 
ATOM   1694 C  CA  . LEU A 1 274 ? 14.788 12.291  -39.809 1.00 87.45  ? 1038 LEU A CA  1 
ATOM   1695 C  C   . LEU A 1 274 ? 14.203 12.326  -38.402 1.00 88.15  ? 1038 LEU A C   1 
ATOM   1696 O  O   . LEU A 1 274 ? 14.819 11.823  -37.455 1.00 87.23  ? 1038 LEU A O   1 
ATOM   1697 C  CB  . LEU A 1 274 ? 15.493 13.609  -40.131 1.00 86.25  ? 1038 LEU A CB  1 
ATOM   1698 C  CG  . LEU A 1 274 ? 16.393 13.588  -41.370 1.00 96.87  ? 1038 LEU A CG  1 
ATOM   1699 C  CD1 . LEU A 1 274 ? 16.842 14.995  -41.735 1.00 100.22 ? 1038 LEU A CD1 1 
ATOM   1700 C  CD2 . LEU A 1 274 ? 17.596 12.687  -41.139 1.00 106.88 ? 1038 LEU A CD2 1 
ATOM   1701 N  N   . ASP A 1 275 ? 13.013 12.913  -38.242 1.00 82.02  ? 1039 ASP A N   1 
ATOM   1702 C  CA  . ASP A 1 275 ? 12.417 13.019  -36.914 1.00 82.05  ? 1039 ASP A CA  1 
ATOM   1703 C  C   . ASP A 1 275 ? 12.179 11.649  -36.294 1.00 78.84  ? 1039 ASP A C   1 
ATOM   1704 O  O   . ASP A 1 275 ? 12.229 11.506  -35.067 1.00 78.31  ? 1039 ASP A O   1 
ATOM   1705 C  CB  . ASP A 1 275 ? 11.104 13.800  -36.989 1.00 87.93  ? 1039 ASP A CB  1 
ATOM   1706 C  CG  . ASP A 1 275 ? 11.311 15.261  -37.342 1.00 78.90  ? 1039 ASP A CG  1 
ATOM   1707 O  OD1 . ASP A 1 275 ? 12.474 15.668  -37.539 1.00 73.96  ? 1039 ASP A OD1 1 
ATOM   1708 O  OD2 . ASP A 1 275 ? 10.309 16.001  -37.420 1.00 93.50  ? 1039 ASP A OD2 1 
ATOM   1709 N  N   . ALA A 1 276 ? 11.915 10.633  -37.117 1.00 77.83  ? 1040 ALA A N   1 
ATOM   1710 C  CA  . ALA A 1 276 ? 11.714 9.287   -36.594 1.00 86.93  ? 1040 ALA A CA  1 
ATOM   1711 C  C   . ALA A 1 276 ? 13.007 8.669   -36.078 1.00 85.46  ? 1040 ALA A C   1 
ATOM   1712 O  O   . ALA A 1 276 ? 12.953 7.697   -35.318 1.00 84.63  ? 1040 ALA A O   1 
ATOM   1713 C  CB  . ALA A 1 276 ? 11.106 8.390   -37.672 1.00 86.72  ? 1040 ALA A CB  1 
ATOM   1714 N  N   . GLN A 1 277 ? 14.163 9.207   -36.471 1.00 85.71  ? 1041 GLN A N   1 
ATOM   1715 C  CA  . GLN A 1 277 ? 15.433 8.641   -36.033 1.00 89.41  ? 1041 GLN A CA  1 
ATOM   1716 C  C   . GLN A 1 277 ? 15.853 9.184   -34.672 1.00 99.39  ? 1041 GLN A C   1 
ATOM   1717 O  O   . GLN A 1 277 ? 16.320 8.424   -33.816 1.00 104.39 ? 1041 GLN A O   1 
ATOM   1718 C  CB  . GLN A 1 277 ? 16.516 8.922   -37.074 1.00 94.81  ? 1041 GLN A CB  1 
ATOM   1719 N  N   . LYS A 1 278 ? 15.702 10.494  -34.453 1.00 95.93  ? 1042 LYS A N   1 
ATOM   1720 C  CA  . LYS A 1 278 ? 16.093 11.074  -33.172 1.00 98.12  ? 1042 LYS A CA  1 
ATOM   1721 C  C   . LYS A 1 278 ? 15.227 10.553  -32.032 1.00 100.00 ? 1042 LYS A C   1 
ATOM   1722 O  O   . LYS A 1 278 ? 15.662 10.553  -30.875 1.00 101.93 ? 1042 LYS A O   1 
ATOM   1723 C  CB  . LYS A 1 278 ? 16.012 12.602  -33.237 1.00 99.00  ? 1042 LYS A CB  1 
ATOM   1724 C  CG  . LYS A 1 278 ? 14.632 13.177  -32.920 1.00 94.85  ? 1042 LYS A CG  1 
ATOM   1725 C  CD  . LYS A 1 278 ? 14.558 14.677  -33.184 1.00 89.75  ? 1042 LYS A CD  1 
ATOM   1726 C  CE  . LYS A 1 278 ? 15.635 15.445  -32.427 1.00 92.99  ? 1042 LYS A CE  1 
ATOM   1727 N  NZ  . LYS A 1 278 ? 15.693 15.085  -30.981 1.00 92.40  ? 1042 LYS A NZ  1 
ATOM   1728 N  N   . ALA A 1 279 ? 14.004 10.114  -32.334 1.00 99.60  ? 1043 ALA A N   1 
ATOM   1729 C  CA  . ALA A 1 279 ? 13.093 9.663   -31.287 1.00 95.81  ? 1043 ALA A CA  1 
ATOM   1730 C  C   . ALA A 1 279 ? 13.659 8.457   -30.545 1.00 84.34  ? 1043 ALA A C   1 
ATOM   1731 O  O   . ALA A 1 279 ? 13.945 8.526   -29.345 1.00 76.48  ? 1043 ALA A O   1 
ATOM   1732 C  CB  . ALA A 1 279 ? 11.728 9.334   -31.894 1.00 86.79  ? 1043 ALA A CB  1 
ATOM   1733 N  N   . THR A 1 280 ? 13.826 7.338   -31.247 1.00 84.42  ? 1044 THR A N   1 
ATOM   1734 C  CA  . THR A 1 280 ? 14.266 6.080   -30.644 1.00 92.08  ? 1044 THR A CA  1 
ATOM   1735 C  C   . THR A 1 280 ? 15.383 5.470   -31.484 1.00 100.37 ? 1044 THR A C   1 
ATOM   1736 O  O   . THR A 1 280 ? 15.179 4.469   -32.182 1.00 93.00  ? 1044 THR A O   1 
ATOM   1737 C  CB  . THR A 1 280 ? 13.098 5.101   -30.506 1.00 91.50  ? 1044 THR A CB  1 
ATOM   1738 O  OG1 . THR A 1 280 ? 12.784 4.537   -31.785 1.00 88.17  ? 1044 THR A OG1 1 
ATOM   1739 C  CG2 . THR A 1 280 ? 11.868 5.810   -29.957 1.00 85.82  ? 1044 THR A CG2 1 
ATOM   1740 N  N   . PRO A 1 281 ? 16.594 6.050   -31.434 1.00 111.50 ? 1045 PRO A N   1 
ATOM   1741 C  CA  . PRO A 1 281 ? 17.732 5.469   -32.155 1.00 111.87 ? 1045 PRO A CA  1 
ATOM   1742 C  C   . PRO A 1 281 ? 18.273 4.211   -31.483 1.00 107.49 ? 1045 PRO A C   1 
ATOM   1743 O  O   . PRO A 1 281 ? 17.880 3.923   -30.353 1.00 108.73 ? 1045 PRO A O   1 
ATOM   1744 C  CB  . PRO A 1 281 ? 18.773 6.591   -32.129 1.00 114.22 ? 1045 PRO A CB  1 
ATOM   1745 C  CG  . PRO A 1 281 ? 18.456 7.365   -30.903 1.00 112.14 ? 1045 PRO A CG  1 
ATOM   1746 C  CD  . PRO A 1 281 ? 16.958 7.300   -30.745 1.00 115.02 ? 1045 PRO A CD  1 
ATOM   1747 N  N   . ASP A 1 302 ? 18.190 4.642   -42.815 1.00 60.66  ? 1066 ASP A N   1 
ATOM   1748 C  CA  . ASP A 1 302 ? 19.395 4.886   -43.596 1.00 74.70  ? 1066 ASP A CA  1 
ATOM   1749 C  C   . ASP A 1 302 ? 19.090 4.788   -45.082 1.00 64.10  ? 1066 ASP A C   1 
ATOM   1750 O  O   . ASP A 1 302 ? 19.242 5.759   -45.823 1.00 71.07  ? 1066 ASP A O   1 
ATOM   1751 C  CB  . ASP A 1 302 ? 20.495 3.892   -43.215 1.00 63.44  ? 1066 ASP A CB  1 
ATOM   1752 N  N   . ILE A 1 303 ? 18.649 3.607   -45.514 1.00 60.64  ? 1067 ILE A N   1 
ATOM   1753 C  CA  . ILE A 1 303 ? 18.330 3.415   -46.923 1.00 60.07  ? 1067 ILE A CA  1 
ATOM   1754 C  C   . ILE A 1 303 ? 17.176 4.320   -47.328 1.00 65.87  ? 1067 ILE A C   1 
ATOM   1755 O  O   . ILE A 1 303 ? 17.150 4.854   -48.443 1.00 68.24  ? 1067 ILE A O   1 
ATOM   1756 C  CB  . ILE A 1 303 ? 18.019 1.934   -47.205 1.00 69.10  ? 1067 ILE A CB  1 
ATOM   1757 C  CG1 . ILE A 1 303 ? 18.122 1.651   -48.705 1.00 71.13  ? 1067 ILE A CG1 1 
ATOM   1758 C  CG2 . ILE A 1 303 ? 16.633 1.564   -46.688 1.00 58.08  ? 1067 ILE A CG2 1 
ATOM   1759 C  CD1 . ILE A 1 303 ? 17.836 0.211   -49.078 1.00 66.22  ? 1067 ILE A CD1 1 
ATOM   1760 N  N   . LEU A 1 304 ? 16.209 4.515   -46.430 1.00 65.26  ? 1068 LEU A N   1 
ATOM   1761 C  CA  . LEU A 1 304 ? 15.090 5.403   -46.723 1.00 61.10  ? 1068 LEU A CA  1 
ATOM   1762 C  C   . LEU A 1 304 ? 15.586 6.813   -47.013 1.00 60.28  ? 1068 LEU A C   1 
ATOM   1763 O  O   . LEU A 1 304 ? 15.400 7.340   -48.115 1.00 67.35  ? 1068 LEU A O   1 
ATOM   1764 C  CB  . LEU A 1 304 ? 14.104 5.399   -45.553 1.00 69.24  ? 1068 LEU A CB  1 
ATOM   1765 C  CG  . LEU A 1 304 ? 12.811 6.203   -45.723 1.00 67.24  ? 1068 LEU A CG  1 
ATOM   1766 C  CD1 . LEU A 1 304 ? 11.761 5.713   -44.744 1.00 83.05  ? 1068 LEU A CD1 1 
ATOM   1767 C  CD2 . LEU A 1 304 ? 13.042 7.695   -45.529 1.00 56.53  ? 1068 LEU A CD2 1 
ATOM   1768 N  N   . VAL A 1 305 ? 16.230 7.441   -46.027 1.00 59.82  ? 1069 VAL A N   1 
ATOM   1769 C  CA  . VAL A 1 305 ? 16.756 8.785   -46.235 1.00 68.13  ? 1069 VAL A CA  1 
ATOM   1770 C  C   . VAL A 1 305 ? 17.758 8.783   -47.381 1.00 74.62  ? 1069 VAL A C   1 
ATOM   1771 O  O   . VAL A 1 305 ? 17.774 9.697   -48.215 1.00 75.95  ? 1069 VAL A O   1 
ATOM   1772 C  CB  . VAL A 1 305 ? 17.380 9.324   -44.935 1.00 60.33  ? 1069 VAL A CB  1 
ATOM   1773 C  CG1 . VAL A 1 305 ? 18.001 10.691  -45.170 1.00 67.10  ? 1069 VAL A CG1 1 
ATOM   1774 C  CG2 . VAL A 1 305 ? 16.333 9.401   -43.841 1.00 59.17  ? 1069 VAL A CG2 1 
ATOM   1775 N  N   . GLY A 1 306 ? 18.604 7.754   -47.446 1.00 74.15  ? 1070 GLY A N   1 
ATOM   1776 C  CA  . GLY A 1 306 ? 19.540 7.655   -48.553 1.00 74.71  ? 1070 GLY A CA  1 
ATOM   1777 C  C   . GLY A 1 306 ? 18.839 7.614   -49.896 1.00 69.94  ? 1070 GLY A C   1 
ATOM   1778 O  O   . GLY A 1 306 ? 19.270 8.263   -50.853 1.00 68.31  ? 1070 GLY A O   1 
ATOM   1779 N  N   . GLN A 1 307 ? 17.746 6.853   -49.987 1.00 64.76  ? 1071 GLN A N   1 
ATOM   1780 C  CA  . GLN A 1 307 ? 16.971 6.827   -51.222 1.00 64.81  ? 1071 GLN A CA  1 
ATOM   1781 C  C   . GLN A 1 307 ? 16.218 8.133   -51.435 1.00 66.49  ? 1071 GLN A C   1 
ATOM   1782 O  O   . GLN A 1 307 ? 16.012 8.546   -52.581 1.00 73.20  ? 1071 GLN A O   1 
ATOM   1783 C  CB  . GLN A 1 307 ? 16.005 5.645   -51.213 1.00 57.76  ? 1071 GLN A CB  1 
ATOM   1784 C  CG  . GLN A 1 307 ? 16.693 4.304   -51.403 1.00 64.51  ? 1071 GLN A CG  1 
ATOM   1785 C  CD  . GLN A 1 307 ? 15.736 3.136   -51.295 1.00 67.88  ? 1071 GLN A CD  1 
ATOM   1786 O  OE1 . GLN A 1 307 ? 14.553 3.312   -51.005 1.00 62.83  ? 1071 GLN A OE1 1 
ATOM   1787 N  NE2 . GLN A 1 307 ? 16.245 1.932   -51.530 1.00 67.54  ? 1071 GLN A NE2 1 
ATOM   1788 N  N   . ILE A 1 308 ? 15.791 8.790   -50.355 1.00 61.42  ? 1072 ILE A N   1 
ATOM   1789 C  CA  . ILE A 1 308 ? 15.229 10.129  -50.495 1.00 60.57  ? 1072 ILE A CA  1 
ATOM   1790 C  C   . ILE A 1 308 ? 16.285 11.086  -51.027 1.00 68.48  ? 1072 ILE A C   1 
ATOM   1791 O  O   . ILE A 1 308 ? 16.003 11.932  -51.883 1.00 68.57  ? 1072 ILE A O   1 
ATOM   1792 C  CB  . ILE A 1 308 ? 14.646 10.616  -49.156 1.00 57.58  ? 1072 ILE A CB  1 
ATOM   1793 C  CG1 . ILE A 1 308 ? 13.369 9.839   -48.834 1.00 56.57  ? 1072 ILE A CG1 1 
ATOM   1794 C  CG2 . ILE A 1 308 ? 14.381 12.120  -49.214 1.00 63.62  ? 1072 ILE A CG2 1 
ATOM   1795 C  CD1 . ILE A 1 308 ? 12.665 10.293  -47.575 1.00 64.02  ? 1072 ILE A CD1 1 
ATOM   1796 N  N   . ASP A 1 309 ? 17.516 10.974  -50.523 1.00 73.03  ? 1073 ASP A N   1 
ATOM   1797 C  CA  . ASP A 1 309 ? 18.597 11.815  -51.026 1.00 69.61  ? 1073 ASP A CA  1 
ATOM   1798 C  C   . ASP A 1 309 ? 18.793 11.602  -52.520 1.00 74.09  ? 1073 ASP A C   1 
ATOM   1799 O  O   . ASP A 1 309 ? 18.904 12.565  -53.288 1.00 73.41  ? 1073 ASP A O   1 
ATOM   1800 C  CB  . ASP A 1 309 ? 19.890 11.515  -50.269 1.00 64.10  ? 1073 ASP A CB  1 
ATOM   1801 C  CG  . ASP A 1 309 ? 19.765 11.768  -48.782 1.00 71.25  ? 1073 ASP A CG  1 
ATOM   1802 O  OD1 . ASP A 1 309 ? 18.683 12.211  -48.343 1.00 78.07  ? 1073 ASP A OD1 1 
ATOM   1803 O  OD2 . ASP A 1 309 ? 20.749 11.525  -48.052 1.00 76.86  ? 1073 ASP A OD2 1 
ATOM   1804 N  N   . ASP A 1 310 ? 18.823 10.341  -52.954 1.00 77.82  ? 1074 ASP A N   1 
ATOM   1805 C  CA  . ASP A 1 310 ? 18.902 10.060  -54.383 1.00 77.35  ? 1074 ASP A CA  1 
ATOM   1806 C  C   . ASP A 1 310 ? 17.683 10.613  -55.108 1.00 77.39  ? 1074 ASP A C   1 
ATOM   1807 O  O   . ASP A 1 310 ? 17.804 11.182  -56.199 1.00 80.84  ? 1074 ASP A O   1 
ATOM   1808 C  CB  . ASP A 1 310 ? 19.029 8.556   -54.618 1.00 77.24  ? 1074 ASP A CB  1 
ATOM   1809 C  CG  . ASP A 1 310 ? 20.234 7.956   -53.919 1.00 86.42  ? 1074 ASP A CG  1 
ATOM   1810 O  OD1 . ASP A 1 310 ? 20.914 8.686   -53.167 1.00 83.90  ? 1074 ASP A OD1 1 
ATOM   1811 O  OD2 . ASP A 1 310 ? 20.502 6.753   -54.124 1.00 91.96  ? 1074 ASP A OD2 1 
ATOM   1812 N  N   . ALA A 1 311 ? 16.497 10.453  -54.516 1.00 73.29  ? 1075 ALA A N   1 
ATOM   1813 C  CA  . ALA A 1 311 ? 15.301 11.063  -55.086 1.00 70.80  ? 1075 ALA A CA  1 
ATOM   1814 C  C   . ALA A 1 311 ? 15.409 12.582  -55.084 1.00 75.10  ? 1075 ALA A C   1 
ATOM   1815 O  O   . ALA A 1 311 ? 15.031 13.241  -56.060 1.00 73.87  ? 1075 ALA A O   1 
ATOM   1816 C  CB  . ALA A 1 311 ? 14.064 10.612  -54.312 1.00 70.01  ? 1075 ALA A CB  1 
ATOM   1817 N  N   . LEU A 1 312 ? 15.916 13.159  -53.991 1.00 74.84  ? 1076 LEU A N   1 
ATOM   1818 C  CA  . LEU A 1 312 ? 16.095 14.606  -53.940 1.00 70.39  ? 1076 LEU A CA  1 
ATOM   1819 C  C   . LEU A 1 312 ? 17.126 15.066  -54.960 1.00 75.79  ? 1076 LEU A C   1 
ATOM   1820 O  O   . LEU A 1 312 ? 16.948 16.107  -55.604 1.00 75.55  ? 1076 LEU A O   1 
ATOM   1821 C  CB  . LEU A 1 312 ? 16.514 15.039  -52.535 1.00 62.29  ? 1076 LEU A CB  1 
ATOM   1822 C  CG  . LEU A 1 312 ? 15.523 15.924  -51.776 1.00 63.38  ? 1076 LEU A CG  1 
ATOM   1823 C  CD1 . LEU A 1 312 ? 16.084 16.293  -50.415 1.00 71.41  ? 1076 LEU A CD1 1 
ATOM   1824 C  CD2 . LEU A 1 312 ? 15.179 17.177  -52.571 1.00 65.70  ? 1076 LEU A CD2 1 
ATOM   1825 N  N   . LYS A 1 313 ? 18.211 14.305  -55.120 1.00 80.26  ? 1077 LYS A N   1 
ATOM   1826 C  CA  . LYS A 1 313 ? 19.255 14.699  -56.059 1.00 81.86  ? 1077 LYS A CA  1 
ATOM   1827 C  C   . LYS A 1 313 ? 18.714 14.804  -57.478 1.00 81.80  ? 1077 LYS A C   1 
ATOM   1828 O  O   . LYS A 1 313 ? 19.218 15.601  -58.276 1.00 72.78  ? 1077 LYS A O   1 
ATOM   1829 C  CB  . LYS A 1 313 ? 20.412 13.699  -55.999 1.00 72.49  ? 1077 LYS A CB  1 
ATOM   1830 C  CG  . LYS A 1 313 ? 21.595 14.056  -56.885 1.00 86.00  ? 1077 LYS A CG  1 
ATOM   1831 C  CD  . LYS A 1 313 ? 22.698 13.009  -56.797 1.00 80.87  ? 1077 LYS A CD  1 
ATOM   1832 C  CE  . LYS A 1 313 ? 23.879 13.366  -57.692 1.00 70.63  ? 1077 LYS A CE  1 
ATOM   1833 N  NZ  . LYS A 1 313 ? 24.543 14.634  -57.275 1.00 72.25  ? 1077 LYS A NZ  1 
ATOM   1834 N  N   . LEU A 1 314 ? 17.694 14.012  -57.812 1.00 78.23  ? 1078 LEU A N   1 
ATOM   1835 C  CA  . LEU A 1 314 ? 17.128 14.050  -59.156 1.00 75.30  ? 1078 LEU A CA  1 
ATOM   1836 C  C   . LEU A 1 314 ? 16.158 15.213  -59.325 1.00 75.42  ? 1078 LEU A C   1 
ATOM   1837 O  O   . LEU A 1 314 ? 16.121 15.844  -60.387 1.00 73.61  ? 1078 LEU A O   1 
ATOM   1838 C  CB  . LEU A 1 314 ? 16.426 12.727  -59.458 1.00 65.81  ? 1078 LEU A CB  1 
ATOM   1839 C  CG  . LEU A 1 314 ? 17.316 11.487  -59.372 1.00 72.56  ? 1078 LEU A CG  1 
ATOM   1840 C  CD1 . LEU A 1 314 ? 16.482 10.255  -59.075 1.00 86.36  ? 1078 LEU A CD1 1 
ATOM   1841 C  CD2 . LEU A 1 314 ? 18.104 11.301  -60.658 1.00 80.77  ? 1078 LEU A CD2 1 
ATOM   1842 N  N   . ALA A 1 315 ? 15.376 15.517  -58.286 1.00 79.89  ? 1079 ALA A N   1 
ATOM   1843 C  CA  . ALA A 1 315 ? 14.342 16.538  -58.410 1.00 84.57  ? 1079 ALA A CA  1 
ATOM   1844 C  C   . ALA A 1 315 ? 14.939 17.902  -58.733 1.00 85.51  ? 1079 ALA A C   1 
ATOM   1845 O  O   . ALA A 1 315 ? 14.394 18.647  -59.556 1.00 85.33  ? 1079 ALA A O   1 
ATOM   1846 C  CB  . ALA A 1 315 ? 13.520 16.607  -57.122 1.00 84.05  ? 1079 ALA A CB  1 
ATOM   1847 N  N   . ASN A 1 316 ? 16.056 18.251  -58.092 1.00 90.26  ? 1080 ASN A N   1 
ATOM   1848 C  CA  . ASN A 1 316 ? 16.636 19.575  -58.293 1.00 96.65  ? 1080 ASN A CA  1 
ATOM   1849 C  C   . ASN A 1 316 ? 17.055 19.787  -59.744 1.00 96.26  ? 1080 ASN A C   1 
ATOM   1850 O  O   . ASN A 1 316 ? 16.816 20.857  -60.316 1.00 100.62 ? 1080 ASN A O   1 
ATOM   1851 C  CB  . ASN A 1 316 ? 17.830 19.771  -57.358 1.00 100.95 ? 1080 ASN A CB  1 
ATOM   1852 C  CG  . ASN A 1 316 ? 17.418 19.902  -55.904 1.00 94.14  ? 1080 ASN A CG  1 
ATOM   1853 O  OD1 . ASN A 1 316 ? 17.318 21.007  -55.372 1.00 88.07  ? 1080 ASN A OD1 1 
ATOM   1854 N  ND2 . ASN A 1 316 ? 17.173 18.770  -55.254 1.00 99.87  ? 1080 ASN A ND2 1 
ATOM   1855 N  N   . GLU A 1 317 ? 17.676 18.781  -60.358 1.00 88.15  ? 1081 GLU A N   1 
ATOM   1856 C  CA  . GLU A 1 317 ? 18.238 18.927  -61.703 1.00 80.04  ? 1081 GLU A CA  1 
ATOM   1857 C  C   . GLU A 1 317 ? 17.243 18.449  -62.763 1.00 78.48  ? 1081 GLU A C   1 
ATOM   1858 O  O   . GLU A 1 317 ? 17.525 17.578  -63.584 1.00 82.03  ? 1081 GLU A O   1 
ATOM   1859 C  CB  . GLU A 1 317 ? 19.567 18.183  -61.807 1.00 78.90  ? 1081 GLU A CB  1 
ATOM   1860 C  CG  . GLU A 1 317 ? 19.602 16.825  -61.119 1.00 84.35  ? 1081 GLU A CG  1 
ATOM   1861 C  CD  . GLU A 1 317 ? 20.917 16.098  -61.323 1.00 77.97  ? 1081 GLU A CD  1 
ATOM   1862 O  OE1 . GLU A 1 317 ? 21.648 16.442  -62.275 1.00 88.42  ? 1081 GLU A OE1 1 
ATOM   1863 O  OE2 . GLU A 1 317 ? 21.223 15.184  -60.528 1.00 73.16  ? 1081 GLU A OE2 1 
ATOM   1864 N  N   . GLY A 1 318 ? 16.061 19.061  -62.734 1.00 80.44  ? 1082 GLY A N   1 
ATOM   1865 C  CA  . GLY A 1 318 ? 15.049 18.851  -63.754 1.00 90.23  ? 1082 GLY A CA  1 
ATOM   1866 C  C   . GLY A 1 318 ? 14.848 17.408  -64.168 1.00 89.37  ? 1082 GLY A C   1 
ATOM   1867 O  O   . GLY A 1 318 ? 15.103 17.049  -65.321 1.00 84.16  ? 1082 GLY A O   1 
ATOM   1868 N  N   . LYS A 1 319 ? 14.399 16.569  -63.237 1.00 78.35  ? 1083 LYS A N   1 
ATOM   1869 C  CA  . LYS A 1 319 ? 14.091 15.166  -63.503 1.00 77.16  ? 1083 LYS A CA  1 
ATOM   1870 C  C   . LYS A 1 319 ? 12.758 14.794  -62.876 1.00 80.05  ? 1083 LYS A C   1 
ATOM   1871 O  O   . LYS A 1 319 ? 12.628 13.791  -62.172 1.00 84.27  ? 1083 LYS A O   1 
ATOM   1872 C  CB  . LYS A 1 319 ? 15.195 14.243  -62.996 1.00 80.16  ? 1083 LYS A CB  1 
ATOM   1873 C  CG  . LYS A 1 319 ? 16.536 14.450  -63.675 1.00 86.95  ? 1083 LYS A CG  1 
ATOM   1874 C  CD  . LYS A 1 319 ? 17.510 13.347  -63.315 1.00 88.36  ? 1083 LYS A CD  1 
ATOM   1875 C  CE  . LYS A 1 319 ? 18.838 13.524  -64.027 1.00 84.45  ? 1083 LYS A CE  1 
ATOM   1876 N  NZ  . LYS A 1 319 ? 19.748 12.367  -63.799 1.00 89.22  ? 1083 LYS A NZ  1 
ATOM   1877 N  N   . VAL A 1 320 ? 11.738 15.615  -63.132 1.00 78.88  ? 1084 VAL A N   1 
ATOM   1878 C  CA  . VAL A 1 320 ? 10.431 15.398  -62.516 1.00 75.02  ? 1084 VAL A CA  1 
ATOM   1879 C  C   . VAL A 1 320 ? 9.922  13.995  -62.822 1.00 77.51  ? 1084 VAL A C   1 
ATOM   1880 O  O   . VAL A 1 320 ? 9.468  13.271  -61.928 1.00 78.09  ? 1084 VAL A O   1 
ATOM   1881 C  CB  . VAL A 1 320 ? 9.436  16.472  -62.990 1.00 72.73  ? 1084 VAL A CB  1 
ATOM   1882 C  CG1 . VAL A 1 320 ? 8.062  16.224  -62.391 1.00 83.69  ? 1084 VAL A CG1 1 
ATOM   1883 C  CG2 . VAL A 1 320 ? 9.939  17.856  -62.625 1.00 84.85  ? 1084 VAL A CG2 1 
ATOM   1884 N  N   . LYS A 1 321 ? 9.991  13.587  -64.091 1.00 80.51  ? 1085 LYS A N   1 
ATOM   1885 C  CA  . LYS A 1 321 ? 9.459  12.281  -64.469 1.00 74.31  ? 1085 LYS A CA  1 
ATOM   1886 C  C   . LYS A 1 321 ? 10.210 11.156  -63.767 1.00 78.47  ? 1085 LYS A C   1 
ATOM   1887 O  O   . LYS A 1 321 ? 9.595  10.218  -63.246 1.00 78.76  ? 1085 LYS A O   1 
ATOM   1888 C  CB  . LYS A 1 321 ? 9.523  12.109  -65.987 1.00 77.66  ? 1085 LYS A CB  1 
ATOM   1889 C  CG  . LYS A 1 321 ? 8.559  12.999  -66.759 1.00 81.68  ? 1085 LYS A CG  1 
ATOM   1890 C  CD  . LYS A 1 321 ? 7.108  12.612  -66.500 1.00 88.82  ? 1085 LYS A CD  1 
ATOM   1891 C  CE  . LYS A 1 321 ? 6.143  13.446  -67.333 1.00 85.93  ? 1085 LYS A CE  1 
ATOM   1892 N  NZ  . LYS A 1 321 ? 4.723  13.236  -66.924 1.00 85.51  ? 1085 LYS A NZ  1 
ATOM   1893 N  N   . GLU A 1 322 ? 11.543 11.230  -63.740 1.00 72.25  ? 1086 GLU A N   1 
ATOM   1894 C  CA  . GLU A 1 322 ? 12.323 10.168  -63.116 1.00 73.15  ? 1086 GLU A CA  1 
ATOM   1895 C  C   . GLU A 1 322 ? 12.425 10.338  -61.605 1.00 74.47  ? 1086 GLU A C   1 
ATOM   1896 O  O   . GLU A 1 322 ? 12.515 9.341   -60.881 1.00 76.04  ? 1086 GLU A O   1 
ATOM   1897 C  CB  . GLU A 1 322 ? 13.726 10.112  -63.720 1.00 71.61  ? 1086 GLU A CB  1 
ATOM   1898 C  CG  . GLU A 1 322 ? 14.457 8.811   -63.426 1.00 74.44  ? 1086 GLU A CG  1 
ATOM   1899 C  CD  . GLU A 1 322 ? 15.960 8.935   -63.570 1.00 77.31  ? 1086 GLU A CD  1 
ATOM   1900 O  OE1 . GLU A 1 322 ? 16.443 10.052  -63.847 1.00 87.95  ? 1086 GLU A OE1 1 
ATOM   1901 O  OE2 . GLU A 1 322 ? 16.660 7.915   -63.402 1.00 76.01  ? 1086 GLU A OE2 1 
ATOM   1902 N  N   . ALA A 1 323 ? 12.418 11.580  -61.113 1.00 76.65  ? 1087 ALA A N   1 
ATOM   1903 C  CA  . ALA A 1 323 ? 12.465 11.797  -59.671 1.00 71.11  ? 1087 ALA A CA  1 
ATOM   1904 C  C   . ALA A 1 323 ? 11.246 11.190  -58.992 1.00 76.07  ? 1087 ALA A C   1 
ATOM   1905 O  O   . ALA A 1 323 ? 11.349 10.621  -57.899 1.00 78.07  ? 1087 ALA A O   1 
ATOM   1906 C  CB  . ALA A 1 323 ? 12.558 13.291  -59.366 1.00 73.31  ? 1087 ALA A CB  1 
ATOM   1907 N  N   . GLN A 1 324 ? 10.078 11.306  -59.626 1.00 81.55  ? 1088 GLN A N   1 
ATOM   1908 C  CA  . GLN A 1 324 ? 8.878  10.679  -59.085 1.00 76.21  ? 1088 GLN A CA  1 
ATOM   1909 C  C   . GLN A 1 324 ? 9.027  9.164   -59.042 1.00 77.32  ? 1088 GLN A C   1 
ATOM   1910 O  O   . GLN A 1 324 ? 8.559  8.513   -58.101 1.00 73.63  ? 1088 GLN A O   1 
ATOM   1911 C  CB  . GLN A 1 324 ? 7.667  11.081  -59.923 1.00 67.78  ? 1088 GLN A CB  1 
ATOM   1912 C  CG  . GLN A 1 324 ? 7.335  12.558  -59.832 1.00 69.82  ? 1088 GLN A CG  1 
ATOM   1913 C  CD  . GLN A 1 324 ? 6.547  13.060  -61.024 1.00 77.85  ? 1088 GLN A CD  1 
ATOM   1914 O  OE1 . GLN A 1 324 ? 6.738  12.601  -62.149 1.00 89.82  ? 1088 GLN A OE1 1 
ATOM   1915 N  NE2 . GLN A 1 324 ? 5.653  14.011  -60.782 1.00 82.80  ? 1088 GLN A NE2 1 
ATOM   1916 N  N   . ALA A 1 325 ? 9.681  8.585   -60.051 1.00 65.99  ? 1089 ALA A N   1 
ATOM   1917 C  CA  . ALA A 1 325 ? 9.899  7.143   -60.055 1.00 68.49  ? 1089 ALA A CA  1 
ATOM   1918 C  C   . ALA A 1 325 ? 10.689 6.708   -58.828 1.00 67.34  ? 1089 ALA A C   1 
ATOM   1919 O  O   . ALA A 1 325 ? 10.366 5.694   -58.198 1.00 69.08  ? 1089 ALA A O   1 
ATOM   1920 C  CB  . ALA A 1 325 ? 10.621 6.729   -61.337 1.00 73.40  ? 1089 ALA A CB  1 
ATOM   1921 N  N   . ALA A 1 326 ? 11.728 7.467   -58.468 1.00 69.97  ? 1090 ALA A N   1 
ATOM   1922 C  CA  . ALA A 1 326 ? 12.496 7.142   -57.272 1.00 65.30  ? 1090 ALA A CA  1 
ATOM   1923 C  C   . ALA A 1 326 ? 11.647 7.286   -56.017 1.00 58.64  ? 1090 ALA A C   1 
ATOM   1924 O  O   . ALA A 1 326 ? 11.826 6.531   -55.055 1.00 62.82  ? 1090 ALA A O   1 
ATOM   1925 C  CB  . ALA A 1 326 ? 13.736 8.033   -57.184 1.00 70.60  ? 1090 ALA A CB  1 
ATOM   1926 N  N   . ALA A 1 327 ? 10.723 8.249   -56.005 1.00 59.69  ? 1091 ALA A N   1 
ATOM   1927 C  CA  . ALA A 1 327 ? 9.831  8.391   -54.861 1.00 60.62  ? 1091 ALA A CA  1 
ATOM   1928 C  C   . ALA A 1 327 ? 8.952  7.160   -54.684 1.00 60.89  ? 1091 ALA A C   1 
ATOM   1929 O  O   . ALA A 1 327 ? 8.627  6.789   -53.550 1.00 63.56  ? 1091 ALA A O   1 
ATOM   1930 C  CB  . ALA A 1 327 ? 8.969  9.643   -55.020 1.00 64.62  ? 1091 ALA A CB  1 
ATOM   1931 N  N   . GLU A 1 328 ? 8.559  6.515   -55.784 1.00 60.66  ? 1092 GLU A N   1 
ATOM   1932 C  CA  . GLU A 1 328 ? 7.696  5.345   -55.697 1.00 57.53  ? 1092 GLU A CA  1 
ATOM   1933 C  C   . GLU A 1 328 ? 8.455  4.082   -55.310 1.00 61.48  ? 1092 GLU A C   1 
ATOM   1934 O  O   . GLU A 1 328 ? 7.831  3.132   -54.825 1.00 64.23  ? 1092 GLU A O   1 
ATOM   1935 C  CB  . GLU A 1 328 ? 6.964  5.130   -57.026 1.00 64.67  ? 1092 GLU A CB  1 
ATOM   1936 C  CG  . GLU A 1 328 ? 6.169  6.347   -57.503 1.00 74.36  ? 1092 GLU A CG  1 
ATOM   1937 C  CD  . GLU A 1 328 ? 5.030  6.718   -56.573 1.00 66.38  ? 1092 GLU A CD  1 
ATOM   1938 O  OE1 . GLU A 1 328 ? 4.708  5.915   -55.675 1.00 62.94  ? 1092 GLU A OE1 1 
ATOM   1939 O  OE2 . GLU A 1 328 ? 4.457  7.814   -56.743 1.00 66.84  ? 1092 GLU A OE2 1 
ATOM   1940 N  N   . GLN A 1 329 ? 9.777  4.039   -55.503 1.00 56.96  ? 1093 GLN A N   1 
ATOM   1941 C  CA  . GLN A 1 329 ? 10.546 2.915   -54.984 1.00 57.32  ? 1093 GLN A CA  1 
ATOM   1942 C  C   . GLN A 1 329 ? 10.761 3.028   -53.485 1.00 59.15  ? 1093 GLN A C   1 
ATOM   1943 O  O   . GLN A 1 329 ? 11.039 2.017   -52.833 1.00 60.85  ? 1093 GLN A O   1 
ATOM   1944 C  CB  . GLN A 1 329 ? 11.902 2.801   -55.692 1.00 68.80  ? 1093 GLN A CB  1 
ATOM   1945 C  CG  . GLN A 1 329 ? 12.938 3.860   -55.308 1.00 70.44  ? 1093 GLN A CG  1 
ATOM   1946 C  CD  . GLN A 1 329 ? 14.366 3.363   -55.455 1.00 69.73  ? 1093 GLN A CD  1 
ATOM   1947 O  OE1 . GLN A 1 329 ? 14.612 2.296   -56.021 1.00 59.13  ? 1093 GLN A OE1 1 
ATOM   1948 N  NE2 . GLN A 1 329 ? 15.317 4.135   -54.937 1.00 64.34  ? 1093 GLN A NE2 1 
ATOM   1949 N  N   . LEU A 1 330 ? 10.632 4.234   -52.925 1.00 64.74  ? 1094 LEU A N   1 
ATOM   1950 C  CA  . LEU A 1 330 ? 10.715 4.379   -51.478 1.00 62.80  ? 1094 LEU A CA  1 
ATOM   1951 C  C   . LEU A 1 330 ? 9.709  3.475   -50.788 1.00 67.78  ? 1094 LEU A C   1 
ATOM   1952 O  O   . LEU A 1 330 ? 9.968  2.985   -49.683 1.00 75.52  ? 1094 LEU A O   1 
ATOM   1953 C  CB  . LEU A 1 330 ? 10.475 5.835   -51.074 1.00 62.35  ? 1094 LEU A CB  1 
ATOM   1954 C  CG  . LEU A 1 330 ? 11.386 6.889   -51.705 1.00 53.80  ? 1094 LEU A CG  1 
ATOM   1955 C  CD1 . LEU A 1 330 ? 11.058 8.270   -51.158 1.00 53.49  ? 1094 LEU A CD1 1 
ATOM   1956 C  CD2 . LEU A 1 330 ? 12.852 6.555   -51.474 1.00 71.94  ? 1094 LEU A CD2 1 
ATOM   1957 N  N   . LYS A 1 331 ? 8.564  3.229   -51.430 1.00 68.10  ? 1095 LYS A N   1 
ATOM   1958 C  CA  . LYS A 1 331 ? 7.567  2.336   -50.851 1.00 69.12  ? 1095 LYS A CA  1 
ATOM   1959 C  C   . LYS A 1 331 ? 8.164  0.969   -50.550 1.00 70.06  ? 1095 LYS A C   1 
ATOM   1960 O  O   . LYS A 1 331 ? 7.829  0.347   -49.535 1.00 66.50  ? 1095 LYS A O   1 
ATOM   1961 C  CB  . LYS A 1 331 ? 6.375  2.201   -51.796 1.00 65.92  ? 1095 LYS A CB  1 
ATOM   1962 C  CG  . LYS A 1 331 ? 5.626  3.499   -52.031 1.00 59.80  ? 1095 LYS A CG  1 
ATOM   1963 C  CD  . LYS A 1 331 ? 4.497  3.316   -53.037 1.00 64.03  ? 1095 LYS A CD  1 
ATOM   1964 C  CE  . LYS A 1 331 ? 3.635  4.564   -53.144 1.00 73.88  ? 1095 LYS A CE  1 
ATOM   1965 N  NZ  . LYS A 1 331 ? 2.590  4.442   -54.201 1.00 77.45  ? 1095 LYS A NZ  1 
ATOM   1966 N  N   . THR A 1 332 ? 9.055  0.485   -51.417 1.00 60.71  ? 1096 THR A N   1 
ATOM   1967 C  CA  . THR A 1 332 ? 9.686  -0.806  -51.173 1.00 64.55  ? 1096 THR A CA  1 
ATOM   1968 C  C   . THR A 1 332 ? 10.451 -0.786  -49.859 1.00 70.08  ? 1096 THR A C   1 
ATOM   1969 O  O   . THR A 1 332 ? 10.313 -1.692  -49.029 1.00 63.96  ? 1096 THR A O   1 
ATOM   1970 C  CB  . THR A 1 332 ? 10.621 -1.167  -52.329 1.00 56.13  ? 1096 THR A CB  1 
ATOM   1971 O  OG1 . THR A 1 332 ? 11.725 -0.256  -52.351 1.00 68.97  ? 1096 THR A OG1 1 
ATOM   1972 C  CG2 . THR A 1 332 ? 9.888  -1.098  -53.659 1.00 63.19  ? 1096 THR A CG2 1 
ATOM   1973 N  N   . THR A 1 333 ? 11.261 0.252   -49.644 1.00 68.72  ? 1097 THR A N   1 
ATOM   1974 C  CA  . THR A 1 333 ? 11.966 0.374   -48.375 1.00 69.96  ? 1097 THR A CA  1 
ATOM   1975 C  C   . THR A 1 333 ? 11.015 0.815   -47.270 1.00 71.78  ? 1097 THR A C   1 
ATOM   1976 O  O   . THR A 1 333 ? 11.093 0.319   -46.141 1.00 71.39  ? 1097 THR A O   1 
ATOM   1977 C  CB  . THR A 1 333 ? 13.131 1.356   -48.505 1.00 59.35  ? 1097 THR A CB  1 
ATOM   1978 O  OG1 . THR A 1 333 ? 12.665 2.594   -49.060 1.00 60.48  ? 1097 THR A OG1 1 
ATOM   1979 C  CG2 . THR A 1 333 ? 14.218 0.780   -49.395 1.00 62.09  ? 1097 THR A CG2 1 
ATOM   1980 N  N   . ARG A 1 334 ? 10.100 1.738   -47.582 1.00 70.66  ? 1098 ARG A N   1 
ATOM   1981 C  CA  . ARG A 1 334 ? 9.197  2.258   -46.561 1.00 66.98  ? 1098 ARG A CA  1 
ATOM   1982 C  C   . ARG A 1 334 ? 8.336  1.149   -45.975 1.00 71.89  ? 1098 ARG A C   1 
ATOM   1983 O  O   . ARG A 1 334 ? 8.081  1.123   -44.765 1.00 73.33  ? 1098 ARG A O   1 
ATOM   1984 C  CB  . ARG A 1 334 ? 8.322  3.367   -47.144 1.00 72.42  ? 1098 ARG A CB  1 
ATOM   1985 C  CG  . ARG A 1 334 ? 7.336  3.962   -46.147 1.00 64.65  ? 1098 ARG A CG  1 
ATOM   1986 C  CD  . ARG A 1 334 ? 5.915  3.478   -46.397 1.00 65.40  ? 1098 ARG A CD  1 
ATOM   1987 N  NE  . ARG A 1 334 ? 5.360  4.027   -47.629 1.00 69.74  ? 1098 ARG A NE  1 
ATOM   1988 C  CZ  . ARG A 1 334 ? 4.114  3.838   -48.043 1.00 68.09  ? 1098 ARG A CZ  1 
ATOM   1989 N  NH1 . ARG A 1 334 ? 3.255  3.110   -47.347 1.00 65.34  ? 1098 ARG A NH1 1 
ATOM   1990 N  NH2 . ARG A 1 334 ? 3.718  4.394   -49.185 1.00 57.90  ? 1098 ARG A NH2 1 
ATOM   1991 N  N   . ASN A 1 335 ? 7.873  0.223   -46.818 1.00 72.55  ? 1099 ASN A N   1 
ATOM   1992 C  CA  . ASN A 1 335 ? 7.124  -0.920  -46.306 1.00 77.55  ? 1099 ASN A CA  1 
ATOM   1993 C  C   . ASN A 1 335 ? 7.979  -1.748  -45.357 1.00 76.40  ? 1099 ASN A C   1 
ATOM   1994 O  O   . ASN A 1 335 ? 7.500  -2.203  -44.311 1.00 68.29  ? 1099 ASN A O   1 
ATOM   1995 C  CB  . ASN A 1 335 ? 6.619  -1.777  -47.465 1.00 77.17  ? 1099 ASN A CB  1 
ATOM   1996 C  CG  . ASN A 1 335 ? 5.483  -1.119  -48.221 1.00 69.48  ? 1099 ASN A CG  1 
ATOM   1997 O  OD1 . ASN A 1 335 ? 4.871  -0.167  -47.738 1.00 55.28  ? 1099 ASN A OD1 1 
ATOM   1998 N  ND2 . ASN A 1 335 ? 5.188  -1.630  -49.411 1.00 77.00  ? 1099 ASN A ND2 1 
ATOM   1999 N  N   . ALA A 1 336 ? 9.251  -1.957  -45.706 1.00 86.10  ? 1100 ALA A N   1 
ATOM   2000 C  CA  . ALA A 1 336 ? 10.167 -2.606  -44.777 1.00 86.84  ? 1100 ALA A CA  1 
ATOM   2001 C  C   . ALA A 1 336 ? 10.567 -1.668  -43.647 1.00 92.86  ? 1100 ALA A C   1 
ATOM   2002 O  O   . ALA A 1 336 ? 10.841 -2.125  -42.532 1.00 99.19  ? 1100 ALA A O   1 
ATOM   2003 C  CB  . ALA A 1 336 ? 11.409 -3.097  -45.520 1.00 93.45  ? 1100 ALA A CB  1 
ATOM   2004 N  N   . TYR A 1 337 ? 10.604 -0.359  -43.913 1.00 83.09  ? 1101 TYR A N   1 
ATOM   2005 C  CA  . TYR A 1 337 ? 10.967 0.600   -42.874 1.00 80.75  ? 1101 TYR A CA  1 
ATOM   2006 C  C   . TYR A 1 337 ? 9.899  0.669   -41.790 1.00 77.43  ? 1101 TYR A C   1 
ATOM   2007 O  O   . TYR A 1 337 ? 10.218 0.684   -40.596 1.00 78.98  ? 1101 TYR A O   1 
ATOM   2008 C  CB  . TYR A 1 337 ? 11.190 1.981   -43.494 1.00 80.00  ? 1101 TYR A CB  1 
ATOM   2009 C  CG  . TYR A 1 337 ? 12.390 2.727   -42.949 1.00 85.90  ? 1101 TYR A CG  1 
ATOM   2010 C  CD1 . TYR A 1 337 ? 13.674 2.434   -43.392 1.00 83.40  ? 1101 TYR A CD1 1 
ATOM   2011 C  CD2 . TYR A 1 337 ? 12.238 3.732   -42.003 1.00 93.27  ? 1101 TYR A CD2 1 
ATOM   2012 C  CE1 . TYR A 1 337 ? 14.772 3.115   -42.900 1.00 80.60  ? 1101 TYR A CE1 1 
ATOM   2013 C  CE2 . TYR A 1 337 ? 13.330 4.419   -41.507 1.00 84.18  ? 1101 TYR A CE2 1 
ATOM   2014 C  CZ  . TYR A 1 337 ? 14.593 4.107   -41.961 1.00 79.59  ? 1101 TYR A CZ  1 
ATOM   2015 O  OH  . TYR A 1 337 ? 15.681 4.788   -41.467 1.00 85.62  ? 1101 TYR A OH  1 
ATOM   2016 N  N   . ILE A 1 338 ? 8.625  0.709   -42.184 1.00 75.62  ? 1102 ILE A N   1 
ATOM   2017 C  CA  . ILE A 1 338 ? 7.552  0.819   -41.201 1.00 74.64  ? 1102 ILE A CA  1 
ATOM   2018 C  C   . ILE A 1 338 ? 7.420  -0.473  -40.404 1.00 78.60  ? 1102 ILE A C   1 
ATOM   2019 O  O   . ILE A 1 338 ? 7.207  -0.447  -39.186 1.00 80.71  ? 1102 ILE A O   1 
ATOM   2020 C  CB  . ILE A 1 338 ? 6.229  1.198   -41.895 1.00 74.52  ? 1102 ILE A CB  1 
ATOM   2021 C  CG1 . ILE A 1 338 ? 5.138  1.490   -40.859 1.00 75.69  ? 1102 ILE A CG1 1 
ATOM   2022 C  CG2 . ILE A 1 338 ? 5.770  0.087   -42.831 1.00 76.10  ? 1102 ILE A CG2 1 
ATOM   2023 C  CD1 . ILE A 1 338 ? 5.429  2.689   -39.977 1.00 75.39  ? 1102 ILE A CD1 1 
ATOM   2024 N  N   . GLN A 1 339 ? 7.553  -1.623  -41.070 1.00 86.86  ? 1103 GLN A N   1 
ATOM   2025 C  CA  . GLN A 1 339 ? 7.399  -2.900  -40.384 1.00 79.90  ? 1103 GLN A CA  1 
ATOM   2026 C  C   . GLN A 1 339 ? 8.461  -3.108  -39.314 1.00 75.04  ? 1103 GLN A C   1 
ATOM   2027 O  O   . GLN A 1 339 ? 8.297  -3.979  -38.453 1.00 75.98  ? 1103 GLN A O   1 
ATOM   2028 C  CB  . GLN A 1 339 ? 7.449  -4.047  -41.394 1.00 79.98  ? 1103 GLN A CB  1 
ATOM   2029 N  N   . LYS A 1 340 ? 9.546  -2.333  -39.350 1.00 71.04  ? 1104 LYS A N   1 
ATOM   2030 C  CA  . LYS A 1 340 ? 10.609 -2.496  -38.366 1.00 71.39  ? 1104 LYS A CA  1 
ATOM   2031 C  C   . LYS A 1 340 ? 10.279 -1.776  -37.062 1.00 70.26  ? 1104 LYS A C   1 
ATOM   2032 O  O   . LYS A 1 340 ? 10.463 -2.337  -35.976 1.00 71.69  ? 1104 LYS A O   1 
ATOM   2033 C  CB  . LYS A 1 340 ? 11.928 -1.979  -38.944 1.00 76.59  ? 1104 LYS A CB  1 
ATOM   2034 C  CG  . LYS A 1 340 ? 13.173 -2.457  -38.208 1.00 81.55  ? 1104 LYS A CG  1 
ATOM   2035 C  CD  . LYS A 1 340 ? 14.432 -1.772  -38.730 1.00 76.87  ? 1104 LYS A CD  1 
ATOM   2036 C  CE  . LYS A 1 340 ? 14.562 -0.350  -38.199 1.00 77.79  ? 1104 LYS A CE  1 
ATOM   2037 N  NZ  . LYS A 1 340 ? 15.709 0.385   -38.807 1.00 67.28  ? 1104 LYS A NZ  1 
ATOM   2038 N  N   . TYR A 1 341 ? 9.777  -0.542  -37.150 1.00 78.19  ? 1105 TYR A N   1 
ATOM   2039 C  CA  . TYR A 1 341 ? 9.540  0.247   -35.945 1.00 62.01  ? 1105 TYR A CA  1 
ATOM   2040 C  C   . TYR A 1 341 ? 8.482  -0.398  -35.060 1.00 71.94  ? 1105 TYR A C   1 
ATOM   2041 O  O   . TYR A 1 341 ? 8.579  -0.349  -33.829 1.00 76.90  ? 1105 TYR A O   1 
ATOM   2042 C  CB  . TYR A 1 341 ? 9.126  1.668   -36.326 1.00 56.82  ? 1105 TYR A CB  1 
ATOM   2043 N  N   . LEU A 1 342 ? 7.464  -1.008  -35.671 1.00 68.42  ? 1106 LEU A N   1 
ATOM   2044 C  CA  . LEU A 1 342 ? 6.375  -1.591  -34.894 1.00 61.41  ? 1106 LEU A CA  1 
ATOM   2045 C  C   . LEU A 1 342 ? 6.893  -2.633  -33.911 1.00 58.27  ? 1106 LEU A C   1 
ATOM   2046 O  O   . LEU A 1 342 ? 6.457  -2.678  -32.754 1.00 57.07  ? 1106 LEU A O   1 
ATOM   2047 C  CB  . LEU A 1 342 ? 5.343  -2.211  -35.835 1.00 71.15  ? 1106 LEU A CB  1 
ATOM   2048 C  CG  . LEU A 1 342 ? 4.715  -1.254  -36.851 1.00 71.97  ? 1106 LEU A CG  1 
ATOM   2049 C  CD1 . LEU A 1 342 ? 3.858  -2.018  -37.848 1.00 84.54  ? 1106 LEU A CD1 1 
ATOM   2050 C  CD2 . LEU A 1 342 ? 3.895  -0.190  -36.143 1.00 64.25  ? 1106 LEU A CD2 1 
ATOM   2051 N  N   . ALA A 1 343 ? 7.829  -3.476  -34.350 1.00 61.86  ? 900  ALA A N   1 
ATOM   2052 C  CA  . ALA A 1 343 ? 8.356  -4.516  -33.473 1.00 58.85  ? 900  ALA A CA  1 
ATOM   2053 C  C   . ALA A 1 343 ? 9.083  -3.918  -32.274 1.00 66.27  ? 900  ALA A C   1 
ATOM   2054 O  O   . ALA A 1 343 ? 8.962  -4.423  -31.152 1.00 65.96  ? 900  ALA A O   1 
ATOM   2055 C  CB  . ALA A 1 343 ? 9.287  -5.439  -34.258 1.00 74.14  ? 900  ALA A CB  1 
ATOM   2056 N  N   . HIS A 1 344 ? 9.845  -2.842  -32.488 1.00 73.38  ? 270  HIS A N   1 
ATOM   2057 C  CA  . HIS A 1 344 ? 10.607 -2.252  -31.391 1.00 69.46  ? 270  HIS A CA  1 
ATOM   2058 C  C   . HIS A 1 344 ? 9.686  -1.761  -30.281 1.00 66.59  ? 270  HIS A C   1 
ATOM   2059 O  O   . HIS A 1 344 ? 9.971  -1.958  -29.094 1.00 64.20  ? 270  HIS A O   1 
ATOM   2060 C  CB  . HIS A 1 344 ? 11.476 -1.106  -31.907 1.00 68.95  ? 270  HIS A CB  1 
ATOM   2061 C  CG  . HIS A 1 344 ? 12.440 -0.575  -30.890 1.00 80.55  ? 270  HIS A CG  1 
ATOM   2062 N  ND1 . HIS A 1 344 ? 12.839 0.744   -30.859 1.00 83.01  ? 270  HIS A ND1 1 
ATOM   2063 C  CD2 . HIS A 1 344 ? 13.089 -1.188  -29.872 1.00 76.11  ? 270  HIS A CD2 1 
ATOM   2064 C  CE1 . HIS A 1 344 ? 13.689 0.922   -29.863 1.00 76.98  ? 270  HIS A CE1 1 
ATOM   2065 N  NE2 . HIS A 1 344 ? 13.858 -0.235  -29.248 1.00 78.42  ? 270  HIS A NE2 1 
ATOM   2066 N  N   . LEU A 1 345 ? 8.578  -1.112  -30.646 1.00 64.05  ? 271  LEU A N   1 
ATOM   2067 C  CA  . LEU A 1 345 ? 7.617  -0.676  -29.638 1.00 63.43  ? 271  LEU A CA  1 
ATOM   2068 C  C   . LEU A 1 345 ? 6.995  -1.869  -28.925 1.00 54.85  ? 271  LEU A C   1 
ATOM   2069 O  O   . LEU A 1 345 ? 6.711  -1.807  -27.723 1.00 51.77  ? 271  LEU A O   1 
ATOM   2070 C  CB  . LEU A 1 345 ? 6.537  0.192   -30.280 1.00 65.22  ? 271  LEU A CB  1 
ATOM   2071 C  CG  . LEU A 1 345 ? 6.908  1.664   -30.472 1.00 62.18  ? 271  LEU A CG  1 
ATOM   2072 C  CD1 . LEU A 1 345 ? 8.201  1.809   -31.265 1.00 62.52  ? 271  LEU A CD1 1 
ATOM   2073 C  CD2 . LEU A 1 345 ? 5.771  2.406   -31.152 1.00 57.03  ? 271  LEU A CD2 1 
ATOM   2074 N  N   . ALA A 1 346 ? 6.767  -2.964  -29.651 1.00 55.34  ? 272  ALA A N   1 
ATOM   2075 C  CA  . ALA A 1 346 ? 6.316  -4.186  -28.997 1.00 65.20  ? 272  ALA A CA  1 
ATOM   2076 C  C   . ALA A 1 346 ? 7.330  -4.642  -27.958 1.00 60.89  ? 272  ALA A C   1 
ATOM   2077 O  O   . ALA A 1 346 ? 6.957  -5.081  -26.865 1.00 64.09  ? 272  ALA A O   1 
ATOM   2078 C  CB  . ALA A 1 346 ? 6.073  -5.282  -30.035 1.00 66.75  ? 272  ALA A CB  1 
ATOM   2079 N  N   . ALA A 1 347 ? 8.621  -4.534  -28.278 1.00 56.80  ? 273  ALA A N   1 
ATOM   2080 C  CA  . ALA A 1 347 ? 9.653  -4.832  -27.291 1.00 51.64  ? 273  ALA A CA  1 
ATOM   2081 C  C   . ALA A 1 347 ? 9.643  -3.809  -26.164 1.00 47.73  ? 273  ALA A C   1 
ATOM   2082 O  O   . ALA A 1 347 ? 9.858  -4.159  -24.998 1.00 55.29  ? 273  ALA A O   1 
ATOM   2083 C  CB  . ALA A 1 347 ? 11.024 -4.872  -27.961 1.00 54.78  ? 273  ALA A CB  1 
ATOM   2084 N  N   . THR A 1 348 ? 9.407  -2.538  -26.492 1.00 52.01  ? 274  THR A N   1 
ATOM   2085 C  CA  . THR A 1 348 ? 9.349  -1.514  -25.456 1.00 57.57  ? 274  THR A CA  1 
ATOM   2086 C  C   . THR A 1 348 ? 8.148  -1.719  -24.542 1.00 49.81  ? 274  THR A C   1 
ATOM   2087 O  O   . THR A 1 348 ? 8.276  -1.635  -23.315 1.00 46.75  ? 274  THR A O   1 
ATOM   2088 C  CB  . THR A 1 348 ? 9.304  -0.125  -26.091 1.00 53.47  ? 274  THR A CB  1 
ATOM   2089 O  OG1 . THR A 1 348 ? 10.526 0.123   -26.797 1.00 59.90  ? 274  THR A OG1 1 
ATOM   2090 C  CG2 . THR A 1 348 ? 9.115  0.940   -25.026 1.00 48.55  ? 274  THR A CG2 1 
ATOM   2091 N  N   . ARG A 1 349 ? 6.974  -1.994  -25.115 1.00 48.52  ? 275  ARG A N   1 
ATOM   2092 C  CA  . ARG A 1 349 ? 5.781  -2.159  -24.292 1.00 48.38  ? 275  ARG A CA  1 
ATOM   2093 C  C   . ARG A 1 349 ? 5.937  -3.331  -23.334 1.00 47.07  ? 275  ARG A C   1 
ATOM   2094 O  O   . ARG A 1 349 ? 5.617  -3.224  -22.145 1.00 51.92  ? 275  ARG A O   1 
ATOM   2095 C  CB  . ARG A 1 349 ? 4.550  -2.355  -25.174 1.00 57.15  ? 275  ARG A CB  1 
ATOM   2096 C  CG  . ARG A 1 349 ? 4.070  -1.091  -25.856 1.00 56.10  ? 275  ARG A CG  1 
ATOM   2097 C  CD  . ARG A 1 349 ? 2.618  -1.221  -26.282 1.00 53.99  ? 275  ARG A CD  1 
ATOM   2098 N  NE  . ARG A 1 349 ? 2.135  -0.011  -26.936 1.00 62.01  ? 275  ARG A NE  1 
ATOM   2099 C  CZ  . ARG A 1 349 ? 2.235  0.233   -28.235 1.00 58.67  ? 275  ARG A CZ  1 
ATOM   2100 N  NH1 . ARG A 1 349 ? 2.798  -0.634  -29.061 1.00 60.76  ? 275  ARG A NH1 1 
ATOM   2101 N  NH2 . ARG A 1 349 ? 1.760  1.378   -28.718 1.00 62.38  ? 275  ARG A NH2 1 
ATOM   2102 N  N   . LYS A 1 350 ? 6.432  -4.462  -23.836 1.00 40.33  ? 276  LYS A N   1 
ATOM   2103 C  CA  . LYS A 1 350 ? 6.644  -5.609  -22.963 1.00 43.01  ? 276  LYS A CA  1 
ATOM   2104 C  C   . LYS A 1 350 ? 7.673  -5.287  -21.887 1.00 45.62  ? 276  LYS A C   1 
ATOM   2105 O  O   . LYS A 1 350 ? 7.483  -5.627  -20.714 1.00 49.33  ? 276  LYS A O   1 
ATOM   2106 C  CB  . LYS A 1 350 ? 7.077  -6.821  -23.786 1.00 52.35  ? 276  LYS A CB  1 
ATOM   2107 C  CG  . LYS A 1 350 ? 6.035  -7.292  -24.801 1.00 63.10  ? 276  LYS A CG  1 
ATOM   2108 C  CD  . LYS A 1 350 ? 4.692  -7.618  -24.150 1.00 63.61  ? 276  LYS A CD  1 
ATOM   2109 C  CE  . LYS A 1 350 ? 3.697  -6.471  -24.291 1.00 68.84  ? 276  LYS A CE  1 
ATOM   2110 N  NZ  . LYS A 1 350 ? 2.370  -6.795  -23.690 1.00 63.89  ? 276  LYS A NZ  1 
ATOM   2111 N  N   . GLY A 1 351 ? 8.760  -4.611  -22.264 1.00 43.40  ? 277  GLY A N   1 
ATOM   2112 C  CA  . GLY A 1 351 ? 9.744  -4.210  -21.273 1.00 44.56  ? 277  GLY A CA  1 
ATOM   2113 C  C   . GLY A 1 351 ? 9.155  -3.295  -20.219 1.00 42.38  ? 277  GLY A C   1 
ATOM   2114 O  O   . GLY A 1 351 ? 9.450  -3.429  -19.029 1.00 46.06  ? 277  GLY A O   1 
ATOM   2115 N  N   . VAL A 1 352 ? 8.319  -2.346  -20.642 1.00 42.31  ? 278  VAL A N   1 
ATOM   2116 C  CA  . VAL A 1 352 ? 7.618  -1.501  -19.683 1.00 44.63  ? 278  VAL A CA  1 
ATOM   2117 C  C   . VAL A 1 352 ? 6.556  -2.306  -18.949 1.00 37.01  ? 278  VAL A C   1 
ATOM   2118 O  O   . VAL A 1 352 ? 6.361  -2.143  -17.739 1.00 31.89  ? 278  VAL A O   1 
ATOM   2119 C  CB  . VAL A 1 352 ? 7.014  -0.278  -20.394 1.00 47.06  ? 278  VAL A CB  1 
ATOM   2120 C  CG1 . VAL A 1 352 ? 6.181  0.534   -19.428 1.00 48.22  ? 278  VAL A CG1 1 
ATOM   2121 C  CG2 . VAL A 1 352 ? 8.114  0.581   -20.991 1.00 52.33  ? 278  VAL A CG2 1 
ATOM   2122 N  N   . ARG A 1 353 ? 5.858  -3.191  -19.664 1.00 42.57  ? 279  ARG A N   1 
ATOM   2123 C  CA  . ARG A 1 353 ? 4.842  -4.016  -19.021 1.00 37.83  ? 279  ARG A CA  1 
ATOM   2124 C  C   . ARG A 1 353 ? 5.450  -4.879  -17.928 1.00 33.23  ? 279  ARG A C   1 
ATOM   2125 O  O   . ARG A 1 353 ? 4.873  -5.023  -16.844 1.00 31.84  ? 279  ARG A O   1 
ATOM   2126 C  CB  . ARG A 1 353 ? 4.146  -4.898  -20.055 1.00 40.65  ? 279  ARG A CB  1 
ATOM   2127 C  CG  . ARG A 1 353 ? 2.898  -4.294  -20.661 1.00 45.05  ? 279  ARG A CG  1 
ATOM   2128 C  CD  . ARG A 1 353 ? 1.826  -4.097  -19.607 1.00 48.64  ? 279  ARG A CD  1 
ATOM   2129 N  NE  . ARG A 1 353 ? 1.706  -2.701  -19.205 1.00 51.59  ? 279  ARG A NE  1 
ATOM   2130 C  CZ  . ARG A 1 353 ? 1.108  -2.289  -18.097 1.00 48.00  ? 279  ARG A CZ  1 
ATOM   2131 N  NH1 . ARG A 1 353 ? 0.601  -3.145  -17.225 1.00 42.57  ? 279  ARG A NH1 1 
ATOM   2132 N  NH2 . ARG A 1 353 ? 1.017  -0.984  -17.856 1.00 48.12  ? 279  ARG A NH2 1 
ATOM   2133 N  N   . THR A 1 354 ? 6.612  -5.472  -18.198 1.00 45.22  ? 280  THR A N   1 
ATOM   2134 C  CA  . THR A 1 354 ? 7.289  -6.249  -17.167 1.00 62.21  ? 280  THR A CA  1 
ATOM   2135 C  C   . THR A 1 354 ? 7.665  -5.363  -15.988 1.00 41.97  ? 280  THR A C   1 
ATOM   2136 O  O   . THR A 1 354 ? 7.545  -5.774  -14.828 1.00 42.59  ? 280  THR A O   1 
ATOM   2137 C  CB  . THR A 1 354 ? 8.527  -6.930  -17.747 1.00 46.10  ? 280  THR A CB  1 
ATOM   2138 O  OG1 . THR A 1 354 ? 8.144  -7.776  -18.838 1.00 49.06  ? 280  THR A OG1 1 
ATOM   2139 C  CG2 . THR A 1 354 ? 9.218  -7.766  -16.687 1.00 46.48  ? 280  THR A CG2 1 
ATOM   2140 N  N   . LEU A 1 355 ? 8.112  -4.139  -16.264 1.00 27.35  ? 281  LEU A N   1 
ATOM   2141 C  CA  . LEU A 1 355 ? 8.380  -3.202  -15.181 1.00 31.30  ? 281  LEU A CA  1 
ATOM   2142 C  C   . LEU A 1 355 ? 7.122  -2.955  -14.362 1.00 28.18  ? 281  LEU A C   1 
ATOM   2143 O  O   . LEU A 1 355 ? 7.179  -2.857  -13.131 1.00 24.43  ? 281  LEU A O   1 
ATOM   2144 C  CB  . LEU A 1 355 ? 8.920  -1.892  -15.752 1.00 35.64  ? 281  LEU A CB  1 
ATOM   2145 C  CG  . LEU A 1 355 ? 9.300  -0.802  -14.752 1.00 26.65  ? 281  LEU A CG  1 
ATOM   2146 C  CD1 . LEU A 1 355 ? 10.459 -1.248  -13.883 1.00 29.41  ? 281  LEU A CD1 1 
ATOM   2147 C  CD2 . LEU A 1 355 ? 9.647  0.473   -15.498 1.00 31.48  ? 281  LEU A CD2 1 
ATOM   2148 N  N   . ALA A 1 356 ? 5.972  -2.861  -15.029 1.00 30.63  ? 282  ALA A N   1 
ATOM   2149 C  CA  . ALA A 1 356 ? 4.721  -2.648  -14.314 1.00 22.60  ? 282  ALA A CA  1 
ATOM   2150 C  C   . ALA A 1 356 ? 4.429  -3.810  -13.377 1.00 24.44  ? 282  ALA A C   1 
ATOM   2151 O  O   . ALA A 1 356 ? 4.077  -3.612  -12.209 1.00 22.17  ? 282  ALA A O   1 
ATOM   2152 C  CB  . ALA A 1 356 ? 3.579  -2.464  -15.310 1.00 27.67  ? 282  ALA A CB  1 
ATOM   2153 N  N   . VAL A 1 357 ? 4.590  -5.038  -13.871 1.00 28.45  ? 283  VAL A N   1 
ATOM   2154 C  CA  . VAL A 1 357 ? 4.271  -6.208  -13.059 1.00 27.04  ? 283  VAL A CA  1 
ATOM   2155 C  C   . VAL A 1 357 ? 5.165  -6.260  -11.831 1.00 30.85  ? 283  VAL A C   1 
ATOM   2156 O  O   . VAL A 1 357 ? 4.702  -6.534  -10.718 1.00 29.79  ? 283  VAL A O   1 
ATOM   2157 C  CB  . VAL A 1 357 ? 4.396  -7.489  -13.902 1.00 31.05  ? 283  VAL A CB  1 
ATOM   2158 C  CG1 . VAL A 1 357 ? 4.479  -8.705  -13.000 1.00 30.03  ? 283  VAL A CG1 1 
ATOM   2159 C  CG2 . VAL A 1 357 ? 3.219  -7.605  -14.859 1.00 48.31  ? 283  VAL A CG2 1 
ATOM   2160 N  N   . VAL A 1 358 ? 6.459  -5.999  -12.011 1.00 35.96  ? 284  VAL A N   1 
ATOM   2161 C  CA  . VAL A 1 358 ? 7.393  -6.077  -10.894 1.00 29.32  ? 284  VAL A CA  1 
ATOM   2162 C  C   . VAL A 1 358 ? 7.015  -5.078  -9.812  1.00 32.53  ? 284  VAL A C   1 
ATOM   2163 O  O   . VAL A 1 358 ? 7.007  -5.404  -8.619  1.00 31.69  ? 284  VAL A O   1 
ATOM   2164 C  CB  . VAL A 1 358 ? 8.830  -5.852  -11.392 1.00 27.06  ? 284  VAL A CB  1 
ATOM   2165 C  CG1 . VAL A 1 358 ? 9.782  -5.744  -10.220 1.00 42.31  ? 284  VAL A CG1 1 
ATOM   2166 C  CG2 . VAL A 1 358 ? 9.240  -6.976  -12.318 1.00 35.43  ? 284  VAL A CG2 1 
ATOM   2167 N  N   . LEU A 1 359 ? 6.696  -3.845  -10.208 1.00 35.42  ? 285  LEU A N   1 
ATOM   2168 C  CA  . LEU A 1 359 ? 6.328  -2.835  -9.224  1.00 27.67  ? 285  LEU A CA  1 
ATOM   2169 C  C   . LEU A 1 359 ? 5.079  -3.247  -8.459  1.00 21.10  ? 285  LEU A C   1 
ATOM   2170 O  O   . LEU A 1 359 ? 5.015  -3.098  -7.234  1.00 26.60  ? 285  LEU A O   1 
ATOM   2171 C  CB  . LEU A 1 359 ? 6.112  -1.490  -9.915  1.00 33.49  ? 285  LEU A CB  1 
ATOM   2172 C  CG  . LEU A 1 359 ? 7.350  -0.882  -10.570 1.00 23.33  ? 285  LEU A CG  1 
ATOM   2173 C  CD1 . LEU A 1 359 ? 6.961  0.263   -11.478 1.00 25.80  ? 285  LEU A CD1 1 
ATOM   2174 C  CD2 . LEU A 1 359 ? 8.316  -0.410  -9.505  1.00 28.12  ? 285  LEU A CD2 1 
ATOM   2175 N  N   . GLY A 1 360 ? 4.078  -3.775  -9.164  1.00 29.45  ? 286  GLY A N   1 
ATOM   2176 C  CA  . GLY A 1 360 ? 2.852  -4.174  -8.496  1.00 28.76  ? 286  GLY A CA  1 
ATOM   2177 C  C   . GLY A 1 360 ? 3.080  -5.266  -7.472  1.00 27.30  ? 286  GLY A C   1 
ATOM   2178 O  O   . GLY A 1 360 ? 2.536  -5.220  -6.367  1.00 39.11  ? 286  GLY A O   1 
ATOM   2179 N  N   . THR A 1 361 ? 3.891  -6.263  -7.822  1.00 30.11  ? 287  THR A N   1 
ATOM   2180 C  CA  . THR A 1 361 ? 4.181  -7.336  -6.879  1.00 32.58  ? 287  THR A CA  1 
ATOM   2181 C  C   . THR A 1 361 ? 4.959  -6.817  -5.680  1.00 33.85  ? 287  THR A C   1 
ATOM   2182 O  O   . THR A 1 361 ? 4.685  -7.209  -4.539  1.00 39.31  ? 287  THR A O   1 
ATOM   2183 C  CB  . THR A 1 361 ? 4.965  -8.451  -7.568  1.00 39.74  ? 287  THR A CB  1 
ATOM   2184 O  OG1 . THR A 1 361 ? 6.224  -7.945  -8.029  1.00 44.57  ? 287  THR A OG1 1 
ATOM   2185 C  CG2 . THR A 1 361 ? 4.179  -9.011  -8.747  1.00 54.32  ? 287  THR A CG2 1 
ATOM   2186 N  N   . PHE A 1 362 ? 5.932  -5.936  -5.917  1.00 35.07  ? 288  PHE A N   1 
ATOM   2187 C  CA  . PHE A 1 362 ? 6.769  -5.450  -4.826  1.00 35.32  ? 288  PHE A CA  1 
ATOM   2188 C  C   . PHE A 1 362 ? 5.924  -4.776  -3.753  1.00 38.55  ? 288  PHE A C   1 
ATOM   2189 O  O   . PHE A 1 362 ? 6.019  -5.112  -2.566  1.00 39.01  ? 288  PHE A O   1 
ATOM   2190 C  CB  . PHE A 1 362 ? 7.831  -4.492  -5.368  1.00 25.66  ? 288  PHE A CB  1 
ATOM   2191 C  CG  . PHE A 1 362 ? 8.893  -4.137  -4.365  1.00 27.51  ? 288  PHE A CG  1 
ATOM   2192 C  CD1 . PHE A 1 362 ? 9.873  -5.056  -4.021  1.00 48.30  ? 288  PHE A CD1 1 
ATOM   2193 C  CD2 . PHE A 1 362 ? 8.911  -2.892  -3.763  1.00 24.80  ? 288  PHE A CD2 1 
ATOM   2194 C  CE1 . PHE A 1 362 ? 10.851 -4.736  -3.097  1.00 40.02  ? 288  PHE A CE1 1 
ATOM   2195 C  CE2 . PHE A 1 362 ? 9.886  -2.568  -2.839  1.00 24.00  ? 288  PHE A CE2 1 
ATOM   2196 C  CZ  . PHE A 1 362 ? 10.857 -3.490  -2.506  1.00 32.76  ? 288  PHE A CZ  1 
ATOM   2197 N  N   . GLY A 1 363 ? 5.072  -3.832  -4.158  1.00 23.80  ? 289  GLY A N   1 
ATOM   2198 C  CA  . GLY A 1 363 ? 4.197  -3.183  -3.197  1.00 28.60  ? 289  GLY A CA  1 
ATOM   2199 C  C   . GLY A 1 363 ? 3.190  -4.139  -2.590  1.00 35.05  ? 289  GLY A C   1 
ATOM   2200 O  O   . GLY A 1 363 ? 2.978  -4.136  -1.375  1.00 37.43  ? 289  GLY A O   1 
ATOM   2201 N  N   . ALA A 1 364 ? 2.564  -4.974  -3.423  1.00 37.92  ? 290  ALA A N   1 
ATOM   2202 C  CA  . ALA A 1 364 ? 1.553  -5.902  -2.933  1.00 43.68  ? 290  ALA A CA  1 
ATOM   2203 C  C   . ALA A 1 364 ? 2.122  -6.903  -1.939  1.00 26.96  ? 290  ALA A C   1 
ATOM   2204 O  O   . ALA A 1 364 ? 1.356  -7.500  -1.177  1.00 38.71  ? 290  ALA A O   1 
ATOM   2205 C  CB  . ALA A 1 364 ? 0.914  -6.644  -4.107  1.00 41.87  ? 290  ALA A CB  1 
ATOM   2206 N  N   . CYS A 1 365 ? 3.441  -7.102  -1.932  1.00 47.20  ? 291  CYS A N   1 
ATOM   2207 C  CA  . CYS A 1 365 ? 4.078  -8.048  -1.029  1.00 53.38  ? 291  CYS A CA  1 
ATOM   2208 C  C   . CYS A 1 365 ? 4.797  -7.391  0.137   1.00 54.72  ? 291  CYS A C   1 
ATOM   2209 O  O   . CYS A 1 365 ? 5.073  -8.072  1.128   1.00 60.62  ? 291  CYS A O   1 
ATOM   2210 C  CB  . CYS A 1 365 ? 5.089  -8.918  -1.792  1.00 46.43  ? 291  CYS A CB  1 
ATOM   2211 S  SG  . CYS A 1 365 ? 4.370  -10.010 -3.034  1.00 70.82  ? 291  CYS A SG  1 
ATOM   2212 N  N   . TRP A 1 366 ? 5.111  -6.097  0.048   1.00 34.27  ? 292  TRP A N   1 
ATOM   2213 C  CA  . TRP A 1 366 ? 5.816  -5.406  1.115   1.00 29.89  ? 292  TRP A CA  1 
ATOM   2214 C  C   . TRP A 1 366 ? 4.948  -4.412  1.867   1.00 23.78  ? 292  TRP A C   1 
ATOM   2215 O  O   . TRP A 1 366 ? 5.237  -4.130  3.033   1.00 23.83  ? 292  TRP A O   1 
ATOM   2216 C  CB  . TRP A 1 366 ? 7.041  -4.664  0.557   1.00 32.16  ? 292  TRP A CB  1 
ATOM   2217 C  CG  . TRP A 1 366 ? 8.290  -5.484  0.550   1.00 28.56  ? 292  TRP A CG  1 
ATOM   2218 C  CD1 . TRP A 1 366 ? 8.936  -5.984  -0.541  1.00 37.41  ? 292  TRP A CD1 1 
ATOM   2219 C  CD2 . TRP A 1 366 ? 9.048  -5.903  1.692   1.00 28.14  ? 292  TRP A CD2 1 
ATOM   2220 N  NE1 . TRP A 1 366 ? 10.048 -6.689  -0.152  1.00 39.34  ? 292  TRP A NE1 1 
ATOM   2221 C  CE2 . TRP A 1 366 ? 10.140 -6.654  1.214   1.00 35.62  ? 292  TRP A CE2 1 
ATOM   2222 C  CE3 . TRP A 1 366 ? 8.909  -5.716  3.071   1.00 27.29  ? 292  TRP A CE3 1 
ATOM   2223 C  CZ2 . TRP A 1 366 ? 11.086 -7.218  2.066   1.00 39.03  ? 292  TRP A CZ2 1 
ATOM   2224 C  CZ3 . TRP A 1 366 ? 9.849  -6.276  3.913   1.00 34.09  ? 292  TRP A CZ3 1 
ATOM   2225 C  CH2 . TRP A 1 366 ? 10.924 -7.018  3.408   1.00 37.18  ? 292  TRP A CH2 1 
ATOM   2226 N  N   . LEU A 1 367 ? 3.887  -3.901  1.250   1.00 26.00  ? 293  LEU A N   1 
ATOM   2227 C  CA  . LEU A 1 367 ? 3.089  -2.851  1.867   1.00 27.56  ? 293  LEU A CA  1 
ATOM   2228 C  C   . LEU A 1 367 ? 2.377  -3.346  3.122   1.00 21.94  ? 293  LEU A C   1 
ATOM   2229 O  O   . LEU A 1 367 ? 2.388  -2.644  4.140   1.00 26.93  ? 293  LEU A O   1 
ATOM   2230 C  CB  . LEU A 1 367 ? 2.089  -2.281  0.860   1.00 28.93  ? 293  LEU A CB  1 
ATOM   2231 C  CG  . LEU A 1 367 ? 2.706  -1.215  -0.053  1.00 26.41  ? 293  LEU A CG  1 
ATOM   2232 C  CD1 . LEU A 1 367 ? 1.830  -0.945  -1.263  1.00 18.13  ? 293  LEU A CD1 1 
ATOM   2233 C  CD2 . LEU A 1 367 ? 2.949  0.081   0.719   1.00 21.93  ? 293  LEU A CD2 1 
ATOM   2234 N  N   . PRO A 1 368 ? 1.761  -4.534  3.109   1.00 21.16  ? 294  PRO A N   1 
ATOM   2235 C  CA  . PRO A 1 368 ? 1.103  -5.016  4.338   1.00 16.23  ? 294  PRO A CA  1 
ATOM   2236 C  C   . PRO A 1 368 ? 2.021  -4.997  5.544   1.00 18.79  ? 294  PRO A C   1 
ATOM   2237 O  O   . PRO A 1 368 ? 1.598  -4.600  6.636   1.00 17.99  ? 294  PRO A O   1 
ATOM   2238 C  CB  . PRO A 1 368 ? 0.676  -6.443  3.965   1.00 14.13  ? 294  PRO A CB  1 
ATOM   2239 C  CG  . PRO A 1 368 ? 0.497  -6.403  2.489   1.00 12.42  ? 294  PRO A CG  1 
ATOM   2240 C  CD  . PRO A 1 368 ? 1.527  -5.437  1.969   1.00 25.59  ? 294  PRO A CD  1 
ATOM   2241 N  N   . PHE A 1 369 ? 3.281  -5.395  5.373   1.00 21.07  ? 295  PHE A N   1 
ATOM   2242 C  CA  . PHE A 1 369 ? 4.229  -5.270  6.469   1.00 20.16  ? 295  PHE A CA  1 
ATOM   2243 C  C   . PHE A 1 369 ? 4.550  -3.811  6.742   1.00 22.49  ? 295  PHE A C   1 
ATOM   2244 O  O   . PHE A 1 369 ? 4.724  -3.419  7.901   1.00 25.40  ? 295  PHE A O   1 
ATOM   2245 C  CB  . PHE A 1 369 ? 5.507  -6.039  6.152   1.00 23.79  ? 295  PHE A CB  1 
ATOM   2246 C  CG  . PHE A 1 369 ? 6.548  -5.934  7.221   1.00 18.80  ? 295  PHE A CG  1 
ATOM   2247 C  CD1 . PHE A 1 369 ? 6.448  -6.689  8.376   1.00 19.10  ? 295  PHE A CD1 1 
ATOM   2248 C  CD2 . PHE A 1 369 ? 7.622  -5.079  7.075   1.00 22.89  ? 295  PHE A CD2 1 
ATOM   2249 C  CE1 . PHE A 1 369 ? 7.401  -6.592  9.365   1.00 21.72  ? 295  PHE A CE1 1 
ATOM   2250 C  CE2 . PHE A 1 369 ? 8.580  -4.978  8.061   1.00 30.72  ? 295  PHE A CE2 1 
ATOM   2251 C  CZ  . PHE A 1 369 ? 8.469  -5.736  9.208   1.00 30.90  ? 295  PHE A CZ  1 
ATOM   2252 N  N   . ALA A 1 370 ? 4.615  -2.991  5.691   1.00 18.02  ? 296  ALA A N   1 
ATOM   2253 C  CA  . ALA A 1 370 ? 4.927  -1.581  5.876   1.00 18.32  ? 296  ALA A CA  1 
ATOM   2254 C  C   . ALA A 1 370 ? 3.899  -0.893  6.760   1.00 16.27  ? 296  ALA A C   1 
ATOM   2255 O  O   . ALA A 1 370 ? 4.234  0.054   7.478   1.00 19.07  ? 296  ALA A O   1 
ATOM   2256 C  CB  . ALA A 1 370 ? 5.011  -0.883  4.520   1.00 21.58  ? 296  ALA A CB  1 
ATOM   2257 N  N   . ILE A 1 371 ? 2.652  -1.347  6.722   1.00 15.28  ? 297  ILE A N   1 
ATOM   2258 C  CA  . ILE A 1 371 ? 1.608  -0.767  7.560   1.00 17.90  ? 297  ILE A CA  1 
ATOM   2259 C  C   . ILE A 1 371 ? 1.564  -1.436  8.926   1.00 25.31  ? 297  ILE A C   1 
ATOM   2260 O  O   . ILE A 1 371 ? 1.472  -0.761  9.954   1.00 24.69  ? 297  ILE A O   1 
ATOM   2261 C  CB  . ILE A 1 371 ? 0.242  -0.863  6.850   1.00 13.42  ? 297  ILE A CB  1 
ATOM   2262 C  CG1 . ILE A 1 371 ? 0.258  -0.034  5.566   1.00 13.68  ? 297  ILE A CG1 1 
ATOM   2263 C  CG2 . ILE A 1 371 ? -0.856 -0.380  7.770   1.00 15.72  ? 297  ILE A CG2 1 
ATOM   2264 C  CD1 . ILE A 1 371 ? -0.959 -0.225  4.692   1.00 15.68  ? 297  ILE A CD1 1 
ATOM   2265 N  N   . TYR A 1 372 ? 1.637  -2.769  8.960   1.00 24.76  ? 298  TYR A N   1 
ATOM   2266 C  CA  . TYR A 1 372 ? 1.463  -3.476  10.224  1.00 26.29  ? 298  TYR A CA  1 
ATOM   2267 C  C   . TYR A 1 372 ? 2.558  -3.110  11.215  1.00 20.48  ? 298  TYR A C   1 
ATOM   2268 O  O   . TYR A 1 372 ? 2.303  -2.999  12.420  1.00 25.37  ? 298  TYR A O   1 
ATOM   2269 C  CB  . TYR A 1 372 ? 1.436  -4.985  9.990   1.00 25.58  ? 298  TYR A CB  1 
ATOM   2270 C  CG  . TYR A 1 372 ? 1.169  -5.789  11.248  1.00 30.24  ? 298  TYR A CG  1 
ATOM   2271 C  CD1 . TYR A 1 372 ? -0.090 -5.802  11.835  1.00 25.60  ? 298  TYR A CD1 1 
ATOM   2272 C  CD2 . TYR A 1 372 ? 2.176  -6.538  11.845  1.00 35.66  ? 298  TYR A CD2 1 
ATOM   2273 C  CE1 . TYR A 1 372 ? -0.337 -6.535  12.985  1.00 31.55  ? 298  TYR A CE1 1 
ATOM   2274 C  CE2 . TYR A 1 372 ? 1.938  -7.274  12.992  1.00 31.83  ? 298  TYR A CE2 1 
ATOM   2275 C  CZ  . TYR A 1 372 ? 0.681  -7.269  13.557  1.00 29.52  ? 298  TYR A CZ  1 
ATOM   2276 O  OH  . TYR A 1 372 ? 0.447  -8.002  14.699  1.00 39.15  ? 298  TYR A OH  1 
ATOM   2277 N  N   . CYS A 1 373 ? 3.784  -2.919  10.733  1.00 25.69  ? 299  CYS A N   1 
ATOM   2278 C  CA  . CYS A 1 373 ? 4.867  -2.563  11.639  1.00 37.01  ? 299  CYS A CA  1 
ATOM   2279 C  C   . CYS A 1 373 ? 4.706  -1.164  12.227  1.00 28.76  ? 299  CYS A C   1 
ATOM   2280 O  O   . CYS A 1 373 ? 5.558  -0.752  13.026  1.00 26.65  ? 299  CYS A O   1 
ATOM   2281 C  CB  . CYS A 1 373 ? 6.215  -2.675  10.920  1.00 24.86  ? 299  CYS A CB  1 
ATOM   2282 S  SG  . CYS A 1 373 ? 6.538  -1.361  9.726   1.00 35.17  ? 299  CYS A SG  1 
ATOM   2283 N  N   . VAL A 1 374 ? 3.653  -0.428  11.862  1.00 18.01  ? 300  VAL A N   1 
ATOM   2284 C  CA  . VAL A 1 374 ? 3.453  0.929   12.360  1.00 34.17  ? 300  VAL A CA  1 
ATOM   2285 C  C   . VAL A 1 374 ? 2.143  1.048   13.135  1.00 29.70  ? 300  VAL A C   1 
ATOM   2286 O  O   . VAL A 1 374 ? 2.033  1.876   14.047  1.00 19.05  ? 300  VAL A O   1 
ATOM   2287 C  CB  . VAL A 1 374 ? 3.493  1.944   11.203  1.00 26.98  ? 300  VAL A CB  1 
ATOM   2288 C  CG1 . VAL A 1 374 ? 3.206  3.344   11.719  1.00 27.19  ? 300  VAL A CG1 1 
ATOM   2289 C  CG2 . VAL A 1 374 ? 4.839  1.893   10.488  1.00 27.12  ? 300  VAL A CG2 1 
ATOM   2290 N  N   . VAL A 1 375 ? 1.154  0.215   12.801  1.00 33.08  ? 301  VAL A N   1 
ATOM   2291 C  CA  . VAL A 1 375 ? -0.174 0.281   13.404  1.00 35.26  ? 301  VAL A CA  1 
ATOM   2292 C  C   . VAL A 1 375 ? -0.479 -0.943  14.234  1.00 36.05  ? 301  VAL A C   1 
ATOM   2293 O  O   . VAL A 1 375 ? -1.531 -0.995  14.882  1.00 50.02  ? 301  VAL A O   1 
ATOM   2294 C  CB  . VAL A 1 375 ? -1.271 0.482   12.340  1.00 27.54  ? 301  VAL A CB  1 
ATOM   2295 C  CG1 . VAL A 1 375 ? -0.993 1.725   11.515  1.00 24.35  ? 301  VAL A CG1 1 
ATOM   2296 C  CG2 . VAL A 1 375 ? -1.406 -0.763  11.457  1.00 34.02  ? 301  VAL A CG2 1 
ATOM   2297 N  N   . GLY A 1 376 ? 0.401  -1.934  14.231  1.00 21.68  ? 302  GLY A N   1 
ATOM   2298 C  CA  . GLY A 1 376 ? 0.190  -3.109  15.041  1.00 43.94  ? 302  GLY A CA  1 
ATOM   2299 C  C   . GLY A 1 376 ? 0.460  -2.844  16.510  1.00 61.81  ? 302  GLY A C   1 
ATOM   2300 O  O   . GLY A 1 376 ? 1.031  -1.821  16.887  1.00 56.70  ? 302  GLY A O   1 
ATOM   2301 N  N   . SER A 1 377 ? 0.025  -3.793  17.342  1.00 45.24  ? 303  SER A N   1 
ATOM   2302 C  CA  . SER A 1 377 ? 0.227  -3.737  18.781  1.00 47.22  ? 303  SER A CA  1 
ATOM   2303 C  C   . SER A 1 377 ? 0.880  -5.029  19.248  1.00 53.29  ? 303  SER A C   1 
ATOM   2304 O  O   . SER A 1 377 ? 0.650  -6.097  18.677  1.00 60.95  ? 303  SER A O   1 
ATOM   2305 C  CB  . SER A 1 377 ? -1.100 -3.533  19.520  1.00 49.00  ? 303  SER A CB  1 
ATOM   2306 O  OG  . SER A 1 377 ? -0.889 -3.282  20.899  1.00 67.37  ? 303  SER A OG  1 
ATOM   2307 N  N   . HIS A 1 378 ? 1.681  -4.932  20.311  1.00 54.46  ? 304  HIS A N   1 
ATOM   2308 C  CA  . HIS A 1 378 ? 2.294  -6.135  20.863  1.00 63.75  ? 304  HIS A CA  1 
ATOM   2309 C  C   . HIS A 1 378 ? 1.274  -7.017  21.565  1.00 64.91  ? 304  HIS A C   1 
ATOM   2310 O  O   . HIS A 1 378 ? 1.597  -8.157  21.922  1.00 62.90  ? 304  HIS A O   1 
ATOM   2311 C  CB  . HIS A 1 378 ? 3.454  -5.779  21.808  1.00 67.30  ? 304  HIS A CB  1 
ATOM   2312 C  CG  . HIS A 1 378 ? 3.072  -4.898  22.958  1.00 71.98  ? 304  HIS A CG  1 
ATOM   2313 N  ND1 . HIS A 1 378 ? 2.571  -3.626  22.784  1.00 74.99  ? 304  HIS A ND1 1 
ATOM   2314 C  CD2 . HIS A 1 378 ? 3.147  -5.090  24.296  1.00 77.41  ? 304  HIS A CD2 1 
ATOM   2315 C  CE1 . HIS A 1 378 ? 2.337  -3.080  23.962  1.00 75.29  ? 304  HIS A CE1 1 
ATOM   2316 N  NE2 . HIS A 1 378 ? 2.679  -3.947  24.898  1.00 82.05  ? 304  HIS A NE2 1 
ATOM   2317 N  N   . GLU A 1 379 ? 0.049  -6.529  21.740  1.00 59.21  ? 305  GLU A N   1 
ATOM   2318 C  CA  . GLU A 1 379 ? -1.061 -7.351  22.189  1.00 57.28  ? 305  GLU A CA  1 
ATOM   2319 C  C   . GLU A 1 379 ? -1.745 -8.063  21.029  1.00 52.37  ? 305  GLU A C   1 
ATOM   2320 O  O   . GLU A 1 379 ? -2.767 -8.725  21.239  1.00 50.56  ? 305  GLU A O   1 
ATOM   2321 C  CB  . GLU A 1 379 ? -2.088 -6.507  22.951  1.00 63.58  ? 305  GLU A CB  1 
ATOM   2322 C  CG  . GLU A 1 379 ? -1.654 -6.109  24.346  1.00 69.37  ? 305  GLU A CG  1 
ATOM   2323 C  CD  . GLU A 1 379 ? -0.493 -5.139  24.339  1.00 81.66  ? 305  GLU A CD  1 
ATOM   2324 O  OE1 . GLU A 1 379 ? -0.027 -4.779  23.237  1.00 78.93  ? 305  GLU A OE1 1 
ATOM   2325 O  OE2 . GLU A 1 379 ? -0.047 -4.736  25.435  1.00 82.05  ? 305  GLU A OE2 1 
ATOM   2326 N  N   . ASP A 1 380 ? -1.183 -7.937  19.757  1.00 52.17  ? 306  ASP A N   1 
ATOM   2327 C  CA  . ASP A 1 380 ? -1.824 -8.588  18.623  1.00 58.21  ? 306  ASP A CA  1 
ATOM   2328 C  C   . ASP A 1 380 ? -1.222 -9.975  18.403  1.00 57.48  ? 306  ASP A C   1 
ATOM   2329 O  O   . ASP A 1 380 ? -0.041 -10.194 18.689  1.00 57.94  ? 306  ASP A O   1 
ATOM   2330 C  CB  . ASP A 1 380 ? -1.663 -7.746  17.352  1.00 45.68  ? 306  ASP A CB  1 
ATOM   2331 C  CG  . ASP A 1 380 ? -2.907 -6.930  17.020  1.00 50.40  ? 306  ASP A CG  1 
ATOM   2332 O  OD1 . ASP A 1 380 ? -3.991 -7.226  17.571  1.00 58.36  ? 306  ASP A OD1 1 
ATOM   2333 O  OD2 . ASP A 1 380 ? -2.805 -5.994  16.194  1.00 47.97  ? 306  ASP A OD2 1 
ATOM   2334 N  N   . PRO A 1 381 ? -2.007 -10.931 17.901  1.00 47.41  ? 307  PRO A N   1 
ATOM   2335 C  CA  . PRO A 1 381 ? -1.472 -12.273 17.635  1.00 49.28  ? 307  PRO A CA  1 
ATOM   2336 C  C   . PRO A 1 381 ? -0.274 -12.259 16.695  1.00 58.13  ? 307  PRO A C   1 
ATOM   2337 O  O   . PRO A 1 381 ? -0.041 -11.302 15.954  1.00 56.44  ? 307  PRO A O   1 
ATOM   2338 C  CB  . PRO A 1 381 ? -2.659 -12.998 16.996  1.00 50.58  ? 307  PRO A CB  1 
ATOM   2339 C  CG  . PRO A 1 381 ? -3.859 -12.322 17.550  1.00 48.08  ? 307  PRO A CG  1 
ATOM   2340 C  CD  . PRO A 1 381 ? -3.469 -10.878 17.701  1.00 46.02  ? 307  PRO A CD  1 
ATOM   2341 N  N   . ALA A 1 382 ? 0.483  -13.364 16.730  1.00 54.69  ? 308  ALA A N   1 
ATOM   2342 C  CA  . ALA A 1 382 ? 1.682  -13.486 15.908  1.00 52.73  ? 308  ALA A CA  1 
ATOM   2343 C  C   . ALA A 1 382 ? 1.342  -13.747 14.447  1.00 53.30  ? 308  ALA A C   1 
ATOM   2344 O  O   . ALA A 1 382 ? 2.110  -13.365 13.559  1.00 51.85  ? 308  ALA A O   1 
ATOM   2345 C  CB  . ALA A 1 382 ? 2.571  -14.606 16.450  1.00 55.31  ? 308  ALA A CB  1 
ATOM   2346 N  N   . VAL A 1 383 ? 0.202  -14.390 14.175  1.00 58.57  ? 309  VAL A N   1 
ATOM   2347 C  CA  . VAL A 1 383 ? -0.149 -14.725 12.797  1.00 53.81  ? 309  VAL A CA  1 
ATOM   2348 C  C   . VAL A 1 383 ? -0.196 -13.471 11.939  1.00 46.88  ? 309  VAL A C   1 
ATOM   2349 O  O   . VAL A 1 383 ? 0.149  -13.508 10.751  1.00 43.08  ? 309  VAL A O   1 
ATOM   2350 C  CB  . VAL A 1 383 ? -1.488 -15.491 12.757  1.00 61.88  ? 309  VAL A CB  1 
ATOM   2351 C  CG1 . VAL A 1 383 ? -2.633 -14.618 13.257  1.00 46.72  ? 309  VAL A CG1 1 
ATOM   2352 C  CG2 . VAL A 1 383 ? -1.769 -15.992 11.351  1.00 74.92  ? 309  VAL A CG2 1 
ATOM   2353 N  N   . TYR A 1 384 ? -0.609 -12.342 12.518  1.00 42.37  ? 310  TYR A N   1 
ATOM   2354 C  CA  . TYR A 1 384 ? -0.600 -11.090 11.771  1.00 40.10  ? 310  TYR A CA  1 
ATOM   2355 C  C   . TYR A 1 384 ? 0.810  -10.710 11.349  1.00 40.11  ? 310  TYR A C   1 
ATOM   2356 O  O   . TYR A 1 384 ? 0.989  -10.013 10.345  1.00 43.13  ? 310  TYR A O   1 
ATOM   2357 C  CB  . TYR A 1 384 ? -1.210 -9.966  12.608  1.00 37.11  ? 310  TYR A CB  1 
ATOM   2358 C  CG  . TYR A 1 384 ? -2.693 -10.109 12.884  1.00 40.90  ? 310  TYR A CG  1 
ATOM   2359 C  CD1 . TYR A 1 384 ? -3.438 -11.135 12.316  1.00 36.20  ? 310  TYR A CD1 1 
ATOM   2360 C  CD2 . TYR A 1 384 ? -3.351 -9.204  13.709  1.00 42.96  ? 310  TYR A CD2 1 
ATOM   2361 C  CE1 . TYR A 1 384 ? -4.789 -11.259 12.567  1.00 34.68  ? 310  TYR A CE1 1 
ATOM   2362 C  CE2 . TYR A 1 384 ? -4.702 -9.321  13.965  1.00 37.50  ? 310  TYR A CE2 1 
ATOM   2363 C  CZ  . TYR A 1 384 ? -5.416 -10.349 13.392  1.00 39.67  ? 310  TYR A CZ  1 
ATOM   2364 O  OH  . TYR A 1 384 ? -6.763 -10.468 13.646  1.00 53.04  ? 310  TYR A OH  1 
ATOM   2365 N  N   . THR A 1 385 ? 1.819  -11.149 12.102  1.00 32.06  ? 311  THR A N   1 
ATOM   2366 C  CA  . THR A 1 385 ? 3.198  -10.840 11.742  1.00 41.10  ? 311  THR A CA  1 
ATOM   2367 C  C   . THR A 1 385 ? 3.626  -11.629 10.513  1.00 36.08  ? 311  THR A C   1 
ATOM   2368 O  O   . THR A 1 385 ? 4.062  -11.058 9.507   1.00 39.10  ? 311  THR A O   1 
ATOM   2369 C  CB  . THR A 1 385 ? 4.126  -11.140 12.919  1.00 42.81  ? 311  THR A CB  1 
ATOM   2370 O  OG1 . THR A 1 385 ? 3.736  -10.356 14.053  1.00 38.01  ? 311  THR A OG1 1 
ATOM   2371 C  CG2 . THR A 1 385 ? 5.570  -10.829 12.554  1.00 38.44  ? 311  THR A CG2 1 
ATOM   2372 N  N   . TYR A 1 386 ? 3.507  -12.954 10.578  1.00 42.70  ? 312  TYR A N   1 
ATOM   2373 C  CA  . TYR A 1 386 ? 3.935  -13.782 9.460   1.00 52.12  ? 312  TYR A CA  1 
ATOM   2374 C  C   . TYR A 1 386 ? 3.063  -13.553 8.235   1.00 39.48  ? 312  TYR A C   1 
ATOM   2375 O  O   . TYR A 1 386 ? 3.555  -13.629 7.103   1.00 37.71  ? 312  TYR A O   1 
ATOM   2376 C  CB  . TYR A 1 386 ? 3.919  -15.252 9.872   1.00 59.20  ? 312  TYR A CB  1 
ATOM   2377 C  CG  . TYR A 1 386 ? 4.765  -15.533 11.092  1.00 58.15  ? 312  TYR A CG  1 
ATOM   2378 C  CD1 . TYR A 1 386 ? 6.151  -15.547 11.009  1.00 78.55  ? 312  TYR A CD1 1 
ATOM   2379 C  CD2 . TYR A 1 386 ? 4.181  -15.776 12.328  1.00 61.51  ? 312  TYR A CD2 1 
ATOM   2380 C  CE1 . TYR A 1 386 ? 6.931  -15.799 12.119  1.00 80.83  ? 312  TYR A CE1 1 
ATOM   2381 C  CE2 . TYR A 1 386 ? 4.955  -16.029 13.445  1.00 76.16  ? 312  TYR A CE2 1 
ATOM   2382 C  CZ  . TYR A 1 386 ? 6.329  -16.039 13.334  1.00 73.67  ? 312  TYR A CZ  1 
ATOM   2383 O  OH  . TYR A 1 386 ? 7.104  -16.290 14.442  1.00 65.98  ? 312  TYR A OH  1 
ATOM   2384 N  N   . ALA A 1 387 ? 1.777  -13.259 8.435   1.00 37.66  ? 313  ALA A N   1 
ATOM   2385 C  CA  . ALA A 1 387 ? 0.909  -12.967 7.302   1.00 37.51  ? 313  ALA A CA  1 
ATOM   2386 C  C   . ALA A 1 387 ? 1.409  -11.759 6.522   1.00 32.24  ? 313  ALA A C   1 
ATOM   2387 O  O   . ALA A 1 387 ? 1.126  -11.633 5.326   1.00 34.69  ? 313  ALA A O   1 
ATOM   2388 C  CB  . ALA A 1 387 ? -0.523 -12.739 7.783   1.00 43.58  ? 313  ALA A CB  1 
ATOM   2389 N  N   . THR A 1 388 ? 2.150  -10.866 7.178   1.00 32.66  ? 314  THR A N   1 
ATOM   2390 C  CA  . THR A 1 388 ? 2.753  -9.723  6.505   1.00 32.08  ? 314  THR A CA  1 
ATOM   2391 C  C   . THR A 1 388 ? 4.181  -9.999  6.053   1.00 32.59  ? 314  THR A C   1 
ATOM   2392 O  O   . THR A 1 388 ? 4.636  -9.411  5.064   1.00 25.32  ? 314  THR A O   1 
ATOM   2393 C  CB  . THR A 1 388 ? 2.742  -8.500  7.427   1.00 23.70  ? 314  THR A CB  1 
ATOM   2394 O  OG1 . THR A 1 388 ? 3.539  -8.763  8.587   1.00 33.16  ? 314  THR A OG1 1 
ATOM   2395 C  CG2 . THR A 1 388 ? 1.320  -8.164  7.854   1.00 22.48  ? 314  THR A CG2 1 
ATOM   2396 N  N   . LEU A 1 389 ? 4.905  -10.866 6.763   1.00 35.81  ? 315  LEU A N   1 
ATOM   2397 C  CA  . LEU A 1 389 ? 6.234  -11.270 6.316   1.00 36.31  ? 315  LEU A CA  1 
ATOM   2398 C  C   . LEU A 1 389 ? 6.168  -12.299 5.196   1.00 34.31  ? 315  LEU A C   1 
ATOM   2399 O  O   . LEU A 1 389 ? 7.016  -12.295 4.298   1.00 41.49  ? 315  LEU A O   1 
ATOM   2400 C  CB  . LEU A 1 389 ? 7.033  -11.829 7.489   1.00 31.22  ? 315  LEU A CB  1 
ATOM   2401 C  CG  . LEU A 1 389 ? 7.419  -10.794 8.538   1.00 31.91  ? 315  LEU A CG  1 
ATOM   2402 C  CD1 . LEU A 1 389 ? 7.994  -11.486 9.755   1.00 37.90  ? 315  LEU A CD1 1 
ATOM   2403 C  CD2 . LEU A 1 389 ? 8.414  -9.801  7.958   1.00 40.76  ? 315  LEU A CD2 1 
ATOM   2404 N  N   . LEU A 1 390 ? 5.181  -13.190 5.230   1.00 38.14  ? 316  LEU A N   1 
ATOM   2405 C  CA  . LEU A 1 390 ? 5.103  -14.237 4.214   1.00 46.63  ? 316  LEU A CA  1 
ATOM   2406 C  C   . LEU A 1 390 ? 5.093  -13.670 2.802   1.00 41.98  ? 316  LEU A C   1 
ATOM   2407 O  O   . LEU A 1 390 ? 5.880  -14.144 1.967   1.00 51.72  ? 316  LEU A O   1 
ATOM   2408 C  CB  . LEU A 1 390 ? 3.868  -15.112 4.474   1.00 47.31  ? 316  LEU A CB  1 
ATOM   2409 C  CG  . LEU A 1 390 ? 3.658  -16.284 3.510   1.00 57.29  ? 316  LEU A CG  1 
ATOM   2410 C  CD1 . LEU A 1 390 ? 4.743  -17.340 3.686   1.00 52.42  ? 316  LEU A CD1 1 
ATOM   2411 C  CD2 . LEU A 1 390 ? 2.272  -16.890 3.699   1.00 69.53  ? 316  LEU A CD2 1 
ATOM   2412 N  N   . PRO A 1 391 ? 4.276  -12.669 2.467   1.00 40.97  ? 317  PRO A N   1 
ATOM   2413 C  CA  . PRO A 1 391 ? 4.365  -12.108 1.111   1.00 45.10  ? 317  PRO A CA  1 
ATOM   2414 C  C   . PRO A 1 391 ? 5.680  -11.397 0.867   1.00 32.66  ? 317  PRO A C   1 
ATOM   2415 O  O   . PRO A 1 391 ? 6.273  -11.543 -0.209  1.00 52.20  ? 317  PRO A O   1 
ATOM   2416 C  CB  . PRO A 1 391 ? 3.172  -11.142 1.047   1.00 40.63  ? 317  PRO A CB  1 
ATOM   2417 C  CG  . PRO A 1 391 ? 2.316  -11.479 2.227   1.00 36.21  ? 317  PRO A CG  1 
ATOM   2418 C  CD  . PRO A 1 391 ? 3.244  -11.992 3.266   1.00 38.45  ? 317  PRO A CD  1 
ATOM   2419 N  N   . ALA A 1 392 ? 6.158  -10.629 1.848   1.00 44.41  ? 318  ALA A N   1 
ATOM   2420 C  CA  . ALA A 1 392 ? 7.428  -9.931  1.686   1.00 37.38  ? 318  ALA A CA  1 
ATOM   2421 C  C   . ALA A 1 392 ? 8.573  -10.918 1.521   1.00 49.55  ? 318  ALA A C   1 
ATOM   2422 O  O   . ALA A 1 392 ? 9.461  -10.719 0.684   1.00 48.77  ? 318  ALA A O   1 
ATOM   2423 C  CB  . ALA A 1 392 ? 7.675  -9.017  2.884   1.00 27.35  ? 318  ALA A CB  1 
ATOM   2424 N  N   . THR A 1 393 ? 8.569  -11.994 2.308   1.00 49.87  ? 319  THR A N   1 
ATOM   2425 C  CA  . THR A 1 393 ? 9.615  -12.999 2.175   1.00 50.23  ? 319  THR A CA  1 
ATOM   2426 C  C   . THR A 1 393 ? 9.588  -13.626 0.787   1.00 56.64  ? 319  THR A C   1 
ATOM   2427 O  O   . THR A 1 393 ? 10.607 -13.660 0.088   1.00 68.49  ? 319  THR A O   1 
ATOM   2428 C  CB  . THR A 1 393 ? 9.459  -14.072 3.254   1.00 65.40  ? 319  THR A CB  1 
ATOM   2429 O  OG1 . THR A 1 393 ? 8.121  -14.585 3.236   1.00 78.11  ? 319  THR A OG1 1 
ATOM   2430 C  CG2 . THR A 1 393 ? 9.768  -13.502 4.633   1.00 59.46  ? 319  THR A CG2 1 
ATOM   2431 N  N   . LEU A 1 394 ? 8.421  -14.103 0.355   1.00 47.26  ? 320  LEU A N   1 
ATOM   2432 C  CA  . LEU A 1 394 ? 8.329  -14.771 -0.936  1.00 51.63  ? 320  LEU A CA  1 
ATOM   2433 C  C   . LEU A 1 394 ? 8.366  -13.798 -2.106  1.00 51.54  ? 320  LEU A C   1 
ATOM   2434 O  O   . LEU A 1 394 ? 8.389  -14.244 -3.259  1.00 51.44  ? 320  LEU A O   1 
ATOM   2435 C  CB  . LEU A 1 394 ? 7.058  -15.626 -1.005  1.00 47.37  ? 320  LEU A CB  1 
ATOM   2436 C  CG  . LEU A 1 394 ? 5.705  -14.913 -0.996  1.00 48.55  ? 320  LEU A CG  1 
ATOM   2437 C  CD1 . LEU A 1 394 ? 5.274  -14.509 -2.399  1.00 52.40  ? 320  LEU A CD1 1 
ATOM   2438 C  CD2 . LEU A 1 394 ? 4.653  -15.799 -0.349  1.00 47.17  ? 320  LEU A CD2 1 
ATOM   2439 N  N   . ASN A 1 395 ? 8.364  -12.489 -1.845  1.00 47.59  ? 321  ASN A N   1 
ATOM   2440 C  CA  . ASN A 1 395 ? 8.537  -11.528 -2.928  1.00 45.91  ? 321  ASN A CA  1 
ATOM   2441 C  C   . ASN A 1 395 ? 9.884  -11.716 -3.607  1.00 50.75  ? 321  ASN A C   1 
ATOM   2442 O  O   . ASN A 1 395 ? 9.981  -11.659 -4.838  1.00 53.52  ? 321  ASN A O   1 
ATOM   2443 C  CB  . ASN A 1 395 ? 8.408  -10.103 -2.398  1.00 50.74  ? 321  ASN A CB  1 
ATOM   2444 C  CG  . ASN A 1 395 ? 8.876  -9.070  -3.401  1.00 42.46  ? 321  ASN A CG  1 
ATOM   2445 O  OD1 . ASN A 1 395 ? 10.002 -8.586  -3.326  1.00 31.84  ? 321  ASN A OD1 1 
ATOM   2446 N  ND2 . ASN A 1 395 ? 8.017  -8.737  -4.354  1.00 47.79  ? 321  ASN A ND2 1 
ATOM   2447 N  N   . SER A 1 396 ? 10.939 -11.928 -2.818  1.00 45.50  ? 322  SER A N   1 
ATOM   2448 C  CA  . SER A 1 396 ? 12.249 -12.219 -3.384  1.00 51.09  ? 322  SER A CA  1 
ATOM   2449 C  C   . SER A 1 396 ? 12.283 -13.563 -4.100  1.00 58.95  ? 322  SER A C   1 
ATOM   2450 O  O   . SER A 1 396 ? 13.141 -13.769 -4.964  1.00 58.16  ? 322  SER A O   1 
ATOM   2451 C  CB  . SER A 1 396 ? 13.307 -12.189 -2.281  1.00 58.40  ? 322  SER A CB  1 
ATOM   2452 O  OG  . SER A 1 396 ? 13.433 -10.889 -1.730  1.00 53.73  ? 322  SER A OG  1 
ATOM   2453 N  N   . MET A 1 397 ? 11.381 -14.485 -3.753  1.00 57.86  ? 323  MET A N   1 
ATOM   2454 C  CA  . MET A 1 397 ? 11.289 -15.751 -4.471  1.00 55.50  ? 323  MET A CA  1 
ATOM   2455 C  C   . MET A 1 397 ? 10.584 -15.590 -5.810  1.00 58.46  ? 323  MET A C   1 
ATOM   2456 O  O   . MET A 1 397 ? 10.863 -16.348 -6.747  1.00 65.19  ? 323  MET A O   1 
ATOM   2457 C  CB  . MET A 1 397 ? 10.544 -16.788 -3.628  1.00 56.08  ? 323  MET A CB  1 
ATOM   2458 C  CG  . MET A 1 397 ? 10.723 -18.225 -4.112  1.00 63.48  ? 323  MET A CG  1 
ATOM   2459 S  SD  . MET A 1 397 ? 9.260  -19.261 -3.881  1.00 72.29  ? 323  MET A SD  1 
ATOM   2460 C  CE  . MET A 1 397 ? 8.169  -18.593 -5.137  1.00 67.82  ? 323  MET A CE  1 
ATOM   2461 N  N   . ILE A 1 398 ? 9.672  -14.626 -5.916  1.00 58.50  ? 324  ILE A N   1 
ATOM   2462 C  CA  . ILE A 1 398 ? 8.906  -14.444 -7.141  1.00 48.06  ? 324  ILE A CA  1 
ATOM   2463 C  C   . ILE A 1 398 ? 9.629  -13.548 -8.142  1.00 42.98  ? 324  ILE A C   1 
ATOM   2464 O  O   . ILE A 1 398 ? 9.445  -13.706 -9.353  1.00 40.46  ? 324  ILE A O   1 
ATOM   2465 C  CB  . ILE A 1 398 ? 7.511  -13.886 -6.808  1.00 45.59  ? 324  ILE A CB  1 
ATOM   2466 C  CG1 . ILE A 1 398 ? 6.598  -15.019 -6.329  1.00 60.27  ? 324  ILE A CG1 1 
ATOM   2467 C  CG2 . ILE A 1 398 ? 6.910  -13.167 -8.016  1.00 51.87  ? 324  ILE A CG2 1 
ATOM   2468 C  CD1 . ILE A 1 398 ? 5.208  -14.574 -5.934  1.00 60.12  ? 324  ILE A CD1 1 
ATOM   2469 N  N   . ASN A 1 399 ? 10.447 -12.608 -7.670  1.00 49.67  ? 325  ASN A N   1 
ATOM   2470 C  CA  . ASN A 1 399 ? 11.120 -11.695 -8.592  1.00 50.75  ? 325  ASN A CA  1 
ATOM   2471 C  C   . ASN A 1 399 ? 11.976 -12.435 -9.608  1.00 53.82  ? 325  ASN A C   1 
ATOM   2472 O  O   . ASN A 1 399 ? 11.885 -12.117 -10.807 1.00 54.42  ? 325  ASN A O   1 
ATOM   2473 C  CB  . ASN A 1 399 ? 11.947 -10.680 -7.798  1.00 47.10  ? 325  ASN A CB  1 
ATOM   2474 C  CG  . ASN A 1 399 ? 11.085 -9.678  -7.068  1.00 45.58  ? 325  ASN A CG  1 
ATOM   2475 O  OD1 . ASN A 1 399 ? 9.911  -9.932  -6.797  1.00 41.17  ? 325  ASN A OD1 1 
ATOM   2476 N  ND2 . ASN A 1 399 ? 11.663 -8.527  -6.747  1.00 46.78  ? 325  ASN A ND2 1 
ATOM   2477 N  N   . PRO A 1 400 ? 12.804 -13.411 -9.228  1.00 57.84  ? 326  PRO A N   1 
ATOM   2478 C  CA  . PRO A 1 400 ? 13.562 -14.150 -10.250 1.00 54.64  ? 326  PRO A CA  1 
ATOM   2479 C  C   . PRO A 1 400 ? 12.667 -14.824 -11.272 1.00 47.00  ? 326  PRO A C   1 
ATOM   2480 O  O   . PRO A 1 400 ? 13.064 -14.976 -12.433 1.00 42.33  ? 326  PRO A O   1 
ATOM   2481 C  CB  . PRO A 1 400 ? 14.356 -15.174 -9.425  1.00 60.72  ? 326  PRO A CB  1 
ATOM   2482 C  CG  . PRO A 1 400 ? 14.420 -14.598 -8.050  1.00 57.68  ? 326  PRO A CG  1 
ATOM   2483 C  CD  . PRO A 1 400 ? 13.134 -13.857 -7.864  1.00 54.40  ? 326  PRO A CD  1 
ATOM   2484 N  N   . ILE A 1 401 ? 11.461 -15.228 -10.872 1.00 49.40  ? 327  ILE A N   1 
ATOM   2485 C  CA  . ILE A 1 401 ? 10.570 -15.948 -11.774 1.00 42.38  ? 327  ILE A CA  1 
ATOM   2486 C  C   . ILE A 1 401 ? 9.993  -15.022 -12.837 1.00 45.09  ? 327  ILE A C   1 
ATOM   2487 O  O   . ILE A 1 401 ? 9.789  -15.439 -13.983 1.00 55.47  ? 327  ILE A O   1 
ATOM   2488 C  CB  . ILE A 1 401 ? 9.457  -16.635 -10.962 1.00 45.84  ? 327  ILE A CB  1 
ATOM   2489 C  CG1 . ILE A 1 401 ? 10.066 -17.681 -10.021 1.00 56.02  ? 327  ILE A CG1 1 
ATOM   2490 C  CG2 . ILE A 1 401 ? 8.432  -17.266 -11.891 1.00 45.33  ? 327  ILE A CG2 1 
ATOM   2491 C  CD1 . ILE A 1 401 ? 9.107  -18.206 -8.969  1.00 66.92  ? 327  ILE A CD1 1 
ATOM   2492 N  N   . ILE A 1 402 ? 9.711  -13.765 -12.487 1.00 51.54  ? 328  ILE A N   1 
ATOM   2493 C  CA  . ILE A 1 402 ? 9.011  -12.872 -13.410 1.00 52.50  ? 328  ILE A CA  1 
ATOM   2494 C  C   . ILE A 1 402 ? 9.834  -12.648 -14.674 1.00 57.87  ? 328  ILE A C   1 
ATOM   2495 O  O   . ILE A 1 402 ? 9.333  -12.792 -15.796 1.00 60.59  ? 328  ILE A O   1 
ATOM   2496 C  CB  . ILE A 1 402 ? 8.674  -11.541 -12.714 1.00 56.66  ? 328  ILE A CB  1 
ATOM   2497 C  CG1 . ILE A 1 402 ? 7.462  -11.719 -11.796 1.00 41.67  ? 328  ILE A CG1 1 
ATOM   2498 C  CG2 . ILE A 1 402 ? 8.411  -10.452 -13.745 1.00 59.58  ? 328  ILE A CG2 1 
ATOM   2499 C  CD1 . ILE A 1 402 ? 7.295  -10.613 -10.777 1.00 41.15  ? 328  ILE A CD1 1 
ATOM   2500 N  N   . TYR A 1 403 ? 11.111 -12.290 -14.514 1.00 58.69  ? 329  TYR A N   1 
ATOM   2501 C  CA  . TYR A 1 403 ? 11.927 -11.935 -15.672 1.00 64.49  ? 329  TYR A CA  1 
ATOM   2502 C  C   . TYR A 1 403 ? 12.104 -13.109 -16.626 1.00 66.85  ? 329  TYR A C   1 
ATOM   2503 O  O   . TYR A 1 403 ? 12.178 -12.910 -17.844 1.00 67.40  ? 329  TYR A O   1 
ATOM   2504 C  CB  . TYR A 1 403 ? 13.289 -11.417 -15.211 1.00 62.19  ? 329  TYR A CB  1 
ATOM   2505 C  CG  . TYR A 1 403 ? 13.249 -10.002 -14.686 1.00 57.81  ? 329  TYR A CG  1 
ATOM   2506 C  CD1 . TYR A 1 403 ? 12.682 -9.715  -13.451 1.00 57.68  ? 329  TYR A CD1 1 
ATOM   2507 C  CD2 . TYR A 1 403 ? 13.778 -8.952  -15.424 1.00 61.02  ? 329  TYR A CD2 1 
ATOM   2508 C  CE1 . TYR A 1 403 ? 12.642 -8.423  -12.967 1.00 54.62  ? 329  TYR A CE1 1 
ATOM   2509 C  CE2 . TYR A 1 403 ? 13.743 -7.656  -14.948 1.00 65.74  ? 329  TYR A CE2 1 
ATOM   2510 C  CZ  . TYR A 1 403 ? 13.174 -7.397  -13.718 1.00 58.11  ? 329  TYR A CZ  1 
ATOM   2511 O  OH  . TYR A 1 403 ? 13.137 -6.109  -13.239 1.00 55.77  ? 329  TYR A OH  1 
ATOM   2512 N  N   . ALA A 1 404 ? 12.183 -14.332 -16.099 1.00 57.62  ? 330  ALA A N   1 
ATOM   2513 C  CA  . ALA A 1 404 ? 12.359 -15.491 -16.967 1.00 65.87  ? 330  ALA A CA  1 
ATOM   2514 C  C   . ALA A 1 404 ? 11.173 -15.663 -17.909 1.00 67.73  ? 330  ALA A C   1 
ATOM   2515 O  O   . ALA A 1 404 ? 11.352 -15.925 -19.104 1.00 74.93  ? 330  ALA A O   1 
ATOM   2516 C  CB  . ALA A 1 404 ? 12.557 -16.750 -16.124 1.00 67.87  ? 330  ALA A CB  1 
ATOM   2517 N  N   . PHE A 1 405 ? 9.954  -15.509 -17.392 1.00 58.70  ? 331  PHE A N   1 
ATOM   2518 C  CA  . PHE A 1 405 ? 8.751  -15.740 -18.183 1.00 61.64  ? 331  PHE A CA  1 
ATOM   2519 C  C   . PHE A 1 405 ? 8.411  -14.579 -19.105 1.00 60.52  ? 331  PHE A C   1 
ATOM   2520 O  O   . PHE A 1 405 ? 7.583  -14.750 -20.007 1.00 58.43  ? 331  PHE A O   1 
ATOM   2521 C  CB  . PHE A 1 405 ? 7.562  -16.013 -17.258 1.00 63.85  ? 331  PHE A CB  1 
ATOM   2522 C  CG  . PHE A 1 405 ? 7.585  -17.375 -16.622 1.00 57.11  ? 331  PHE A CG  1 
ATOM   2523 C  CD1 . PHE A 1 405 ? 8.612  -17.739 -15.766 1.00 52.17  ? 331  PHE A CD1 1 
ATOM   2524 C  CD2 . PHE A 1 405 ? 6.574  -18.289 -16.872 1.00 66.55  ? 331  PHE A CD2 1 
ATOM   2525 C  CE1 . PHE A 1 405 ? 8.635  -18.990 -15.180 1.00 51.31  ? 331  PHE A CE1 1 
ATOM   2526 C  CE2 . PHE A 1 405 ? 6.592  -19.541 -16.286 1.00 72.51  ? 331  PHE A CE2 1 
ATOM   2527 C  CZ  . PHE A 1 405 ? 7.623  -19.892 -15.439 1.00 58.32  ? 331  PHE A CZ  1 
ATOM   2528 N  N   . ARG A 1 406 ? 9.019  -13.413 -18.904 1.00 58.62  ? 332  ARG A N   1 
ATOM   2529 C  CA  . ARG A 1 406 ? 8.709  -12.222 -19.682 1.00 61.41  ? 332  ARG A CA  1 
ATOM   2530 C  C   . ARG A 1 406 ? 9.875  -11.756 -20.539 1.00 67.72  ? 332  ARG A C   1 
ATOM   2531 O  O   . ARG A 1 406 ? 9.727  -11.605 -21.756 1.00 70.60  ? 332  ARG A O   1 
ATOM   2532 C  CB  . ARG A 1 406 ? 8.272  -11.093 -18.739 1.00 59.35  ? 332  ARG A CB  1 
ATOM   2533 C  CG  . ARG A 1 406 ? 7.159  -11.487 -17.778 1.00 53.52  ? 332  ARG A CG  1 
ATOM   2534 C  CD  . ARG A 1 406 ? 5.923  -11.990 -18.511 1.00 63.08  ? 332  ARG A CD  1 
ATOM   2535 N  NE  . ARG A 1 406 ? 5.463  -11.046 -19.522 1.00 66.01  ? 332  ARG A NE  1 
ATOM   2536 C  CZ  . ARG A 1 406 ? 4.776  -9.942  -19.260 1.00 56.25  ? 332  ARG A CZ  1 
ATOM   2537 N  NH1 . ARG A 1 406 ? 4.464  -9.600  -18.021 1.00 45.36  ? 332  ARG A NH1 1 
ATOM   2538 N  NH2 . ARG A 1 406 ? 4.398  -9.158  -20.266 1.00 54.92  ? 332  ARG A NH2 1 
ATOM   2539 N  N   . ASN A 1 407 ? 11.039 -11.529 -19.936 1.00 72.38  ? 333  ASN A N   1 
ATOM   2540 C  CA  . ASN A 1 407 ? 12.190 -11.018 -20.670 1.00 75.60  ? 333  ASN A CA  1 
ATOM   2541 C  C   . ASN A 1 407 ? 12.863 -12.165 -21.413 1.00 70.16  ? 333  ASN A C   1 
ATOM   2542 O  O   . ASN A 1 407 ? 13.348 -13.117 -20.793 1.00 70.32  ? 333  ASN A O   1 
ATOM   2543 C  CB  . ASN A 1 407 ? 13.169 -10.336 -19.717 1.00 73.59  ? 333  ASN A CB  1 
ATOM   2544 C  CG  . ASN A 1 407 ? 14.269 -9.591  -20.447 1.00 71.27  ? 333  ASN A CG  1 
ATOM   2545 O  OD1 . ASN A 1 407 ? 14.921 -10.137 -21.337 1.00 69.79  ? 333  ASN A OD1 1 
ATOM   2546 N  ND2 . ASN A 1 407 ? 14.473 -8.331  -20.080 1.00 69.98  ? 333  ASN A ND2 1 
ATOM   2547 N  N   . GLN A 1 408 ? 12.890 -12.071 -22.743 1.00 77.42  ? 334  GLN A N   1 
ATOM   2548 C  CA  . GLN A 1 408 ? 13.454 -13.140 -23.558 1.00 70.71  ? 334  GLN A CA  1 
ATOM   2549 C  C   . GLN A 1 408 ? 14.975 -13.139 -23.533 1.00 69.00  ? 334  GLN A C   1 
ATOM   2550 O  O   . GLN A 1 408 ? 15.592 -14.208 -23.596 1.00 68.55  ? 334  GLN A O   1 
ATOM   2551 C  CB  . GLN A 1 408 ? 12.957 -13.012 -25.000 1.00 68.90  ? 334  GLN A CB  1 
ATOM   2552 C  CG  . GLN A 1 408 ? 13.300 -14.196 -25.887 1.00 74.32  ? 334  GLN A CG  1 
ATOM   2553 C  CD  . GLN A 1 408 ? 12.602 -15.469 -25.450 1.00 84.29  ? 334  GLN A CD  1 
ATOM   2554 O  OE1 . GLN A 1 408 ? 11.640 -15.430 -24.681 1.00 59.06  ? 334  GLN A OE1 1 
ATOM   2555 N  NE2 . GLN A 1 408 ? 13.086 -16.606 -25.937 1.00 77.74  ? 334  GLN A NE2 1 
ATOM   2556 N  N   . GLU A 1 409 ? 15.594 -11.962 -23.430 1.00 69.11  ? 335  GLU A N   1 
ATOM   2557 C  CA  . GLU A 1 409 ? 17.048 -11.888 -23.511 1.00 77.81  ? 335  GLU A CA  1 
ATOM   2558 C  C   . GLU A 1 409 ? 17.706 -12.705 -22.406 1.00 76.05  ? 335  GLU A C   1 
ATOM   2559 O  O   . GLU A 1 409 ? 18.702 -13.398 -22.644 1.00 81.26  ? 335  GLU A O   1 
ATOM   2560 C  CB  . GLU A 1 409 ? 17.500 -10.431 -23.441 1.00 73.80  ? 335  GLU A CB  1 
ATOM   2561 C  CG  . GLU A 1 409 ? 18.984 -10.241 -23.677 1.00 80.39  ? 335  GLU A CG  1 
ATOM   2562 C  CD  . GLU A 1 409 ? 19.365 -8.783  -23.829 1.00 87.29  ? 335  GLU A CD  1 
ATOM   2563 O  OE1 . GLU A 1 409 ? 18.565 -7.913  -23.420 1.00 86.74  ? 335  GLU A OE1 1 
ATOM   2564 O  OE2 . GLU A 1 409 ? 20.459 -8.507  -24.364 1.00 93.04  ? 335  GLU A OE2 1 
ATOM   2565 N  N   . ILE A 1 410 ? 17.164 -12.633 -21.190 1.00 71.25  ? 336  ILE A N   1 
ATOM   2566 C  CA  . ILE A 1 410 ? 17.710 -13.418 -20.086 1.00 70.20  ? 336  ILE A CA  1 
ATOM   2567 C  C   . ILE A 1 410 ? 17.154 -14.837 -20.081 1.00 67.09  ? 336  ILE A C   1 
ATOM   2568 O  O   . ILE A 1 410 ? 17.823 -15.764 -19.611 1.00 83.87  ? 336  ILE A O   1 
ATOM   2569 C  CB  . ILE A 1 410 ? 17.441 -12.720 -18.742 1.00 68.91  ? 336  ILE A CB  1 
ATOM   2570 C  CG1 . ILE A 1 410 ? 17.895 -13.618 -17.590 1.00 70.42  ? 336  ILE A CG1 1 
ATOM   2571 C  CG2 . ILE A 1 410 ? 15.956 -12.365 -18.597 1.00 73.26  ? 336  ILE A CG2 1 
ATOM   2572 C  CD1 . ILE A 1 410 ? 18.041 -12.899 -16.274 1.00 74.24  ? 336  ILE A CD1 1 
ATOM   2573 N  N   . GLN A 1 411 ? 15.932 -15.035 -20.579 1.00 66.74  ? 337  GLN A N   1 
ATOM   2574 C  CA  . GLN A 1 411 ? 15.370 -16.380 -20.623 1.00 77.60  ? 337  GLN A CA  1 
ATOM   2575 C  C   . GLN A 1 411 ? 16.179 -17.293 -21.533 1.00 88.91  ? 337  GLN A C   1 
ATOM   2576 O  O   . GLN A 1 411 ? 16.230 -18.507 -21.307 1.00 86.79  ? 337  GLN A O   1 
ATOM   2577 C  CB  . GLN A 1 411 ? 13.917 -16.323 -21.091 1.00 75.34  ? 337  GLN A CB  1 
ATOM   2578 C  CG  . GLN A 1 411 ? 13.180 -17.644 -20.967 1.00 71.68  ? 337  GLN A CG  1 
ATOM   2579 C  CD  . GLN A 1 411 ? 11.754 -17.564 -21.470 1.00 78.39  ? 337  GLN A CD  1 
ATOM   2580 O  OE1 . GLN A 1 411 ? 11.452 -16.813 -22.397 1.00 74.03  ? 337  GLN A OE1 1 
ATOM   2581 N  NE2 . GLN A 1 411 ? 10.868 -18.336 -20.854 1.00 79.57  ? 337  GLN A NE2 1 
ATOM   2582 N  N   . ARG A 1 412 ? 16.821 -16.730 -22.560 1.00 83.43  ? 338  ARG A N   1 
ATOM   2583 C  CA  . ARG A 1 412 ? 17.605 -17.549 -23.479 1.00 73.32  ? 338  ARG A CA  1 
ATOM   2584 C  C   . ARG A 1 412 ? 18.747 -18.245 -22.753 1.00 81.68  ? 338  ARG A C   1 
ATOM   2585 O  O   . ARG A 1 412 ? 18.985 -19.442 -22.956 1.00 93.69  ? 338  ARG A O   1 
ATOM   2586 C  CB  . ARG A 1 412 ? 18.142 -16.684 -24.619 1.00 70.68  ? 338  ARG A CB  1 
ATOM   2587 N  N   . ALA A 1 413 ? 19.460 -17.517 -21.892 1.00 78.48  ? 339  ALA A N   1 
ATOM   2588 C  CA  . ALA A 1 413 ? 20.561 -18.127 -21.156 1.00 87.16  ? 339  ALA A CA  1 
ATOM   2589 C  C   . ALA A 1 413 ? 20.066 -19.199 -20.195 1.00 87.90  ? 339  ALA A C   1 
ATOM   2590 O  O   . ALA A 1 413 ? 20.775 -20.181 -19.946 1.00 89.55  ? 339  ALA A O   1 
ATOM   2591 C  CB  . ALA A 1 413 ? 21.345 -17.059 -20.395 1.00 81.76  ? 339  ALA A CB  1 
ATOM   2592 N  N   . LEU A 1 414 ? 18.860 -19.033 -19.647 1.00 89.77  ? 340  LEU A N   1 
ATOM   2593 C  CA  . LEU A 1 414 ? 18.335 -20.017 -18.706 1.00 100.91 ? 340  LEU A CA  1 
ATOM   2594 C  C   . LEU A 1 414 ? 18.160 -21.375 -19.376 1.00 98.02  ? 340  LEU A C   1 
ATOM   2595 O  O   . LEU A 1 414 ? 18.587 -22.406 -18.841 1.00 94.19  ? 340  LEU A O   1 
ATOM   2596 C  CB  . LEU A 1 414 ? 17.008 -19.525 -18.123 1.00 76.48  ? 340  LEU A CB  1 
ATOM   2597 N  N   . TRP A 1 415 ? 17.530 -21.397 -20.549 1.00 90.93  ? 341  TRP A N   1 
ATOM   2598 C  CA  . TRP A 1 415 ? 17.344 -22.624 -21.312 1.00 100.97 ? 341  TRP A CA  1 
ATOM   2599 C  C   . TRP A 1 415 ? 18.526 -22.924 -22.224 1.00 111.95 ? 341  TRP A C   1 
ATOM   2600 O  O   . TRP A 1 415 ? 18.504 -23.936 -22.933 1.00 102.53 ? 341  TRP A O   1 
ATOM   2601 C  CB  . TRP A 1 415 ? 16.051 -22.542 -22.139 1.00 97.77  ? 341  TRP A CB  1 
ATOM   2602 C  CG  . TRP A 1 415 ? 14.792 -22.757 -21.334 1.00 106.16 ? 341  TRP A CG  1 
ATOM   2603 C  CD1 . TRP A 1 415 ? 14.710 -23.164 -20.033 1.00 104.36 ? 341  TRP A CD1 1 
ATOM   2604 C  CD2 . TRP A 1 415 ? 13.441 -22.577 -21.782 1.00 114.70 ? 341  TRP A CD2 1 
ATOM   2605 N  NE1 . TRP A 1 415 ? 13.395 -23.249 -19.644 1.00 108.41 ? 341  TRP A NE1 1 
ATOM   2606 C  CE2 . TRP A 1 415 ? 12.596 -22.893 -20.698 1.00 112.48 ? 341  TRP A CE2 1 
ATOM   2607 C  CE3 . TRP A 1 415 ? 12.864 -22.178 -22.992 1.00 111.65 ? 341  TRP A CE3 1 
ATOM   2608 C  CZ2 . TRP A 1 415 ? 11.206 -22.823 -20.789 1.00 114.28 ? 341  TRP A CZ2 1 
ATOM   2609 C  CZ3 . TRP A 1 415 ? 11.483 -22.109 -23.080 1.00 109.84 ? 341  TRP A CZ3 1 
ATOM   2610 C  CH2 . TRP A 1 415 ? 10.671 -22.430 -21.985 1.00 110.12 ? 341  TRP A CH2 1 
ATOM   2611 N  N   . LEU A 1 416 ? 19.559 -22.078 -22.213 1.00 102.78 ? 342  LEU A N   1 
ATOM   2612 C  CA  . LEU A 1 416 ? 20.749 -22.353 -23.010 1.00 99.36  ? 342  LEU A CA  1 
ATOM   2613 C  C   . LEU A 1 416 ? 21.370 -23.684 -22.613 1.00 114.67 ? 342  LEU A C   1 
ATOM   2614 O  O   . LEU A 1 416 ? 21.815 -24.454 -23.472 1.00 125.99 ? 342  LEU A O   1 
ATOM   2615 C  CB  . LEU A 1 416 ? 21.763 -21.220 -22.842 1.00 96.34  ? 342  LEU A CB  1 
ATOM   2616 C  CG  . LEU A 1 416 ? 23.032 -21.287 -23.696 1.00 88.39  ? 342  LEU A CG  1 
ATOM   2617 C  CD1 . LEU A 1 416 ? 22.794 -20.647 -25.055 1.00 88.12  ? 342  LEU A CD1 1 
ATOM   2618 C  CD2 . LEU A 1 416 ? 24.195 -20.621 -22.977 1.00 86.90  ? 342  LEU A CD2 1 
ATOM   2619 N  N   . LEU A 1 417 ? 21.400 -23.975 -21.316 1.00 108.05 ? 343  LEU A N   1 
ATOM   2620 C  CA  . LEU A 1 417 ? 22.025 -25.194 -20.810 1.00 114.56 ? 343  LEU A CA  1 
ATOM   2621 C  C   . LEU A 1 417 ? 20.995 -26.310 -20.909 1.00 122.69 ? 343  LEU A C   1 
ATOM   2622 O  O   . LEU A 1 417 ? 20.041 -26.359 -20.130 1.00 111.39 ? 343  LEU A O   1 
ATOM   2623 C  CB  . LEU A 1 417 ? 22.508 -24.992 -19.379 1.00 104.29 ? 343  LEU A CB  1 
ATOM   2624 C  CG  . LEU A 1 417 ? 23.046 -23.589 -19.075 1.00 106.24 ? 343  LEU A CG  1 
ATOM   2625 C  CD1 . LEU A 1 417 ? 23.548 -23.507 -17.646 1.00 94.55  ? 343  LEU A CD1 1 
ATOM   2626 C  CD2 . LEU A 1 417 ? 24.146 -23.194 -20.054 1.00 116.54 ? 343  LEU A CD2 1 
ATOM   2627 N  N   . LEU A 1 418 ? 21.180 -27.206 -21.880 1.00 129.72 ? 344  LEU A N   1 
ATOM   2628 C  CA  . LEU A 1 418 ? 20.193 -28.231 -22.189 1.00 130.49 ? 344  LEU A CA  1 
ATOM   2629 C  C   . LEU A 1 418 ? 20.712 -29.656 -22.073 1.00 137.45 ? 344  LEU A C   1 
ATOM   2630 O  O   . LEU A 1 418 ? 19.921 -30.552 -21.772 1.00 138.16 ? 344  LEU A O   1 
ATOM   2631 C  CB  . LEU A 1 418 ? 19.647 -28.024 -23.612 1.00 124.14 ? 344  LEU A CB  1 
ATOM   2632 N  N   . ASP A 1 419 ? 22.003 -29.895 -22.299 1.00 144.78 ? 345  ASP A N   1 
ATOM   2633 C  CA  . ASP A 1 419 ? 22.536 -31.250 -22.299 1.00 142.50 ? 345  ASP A CA  1 
ATOM   2634 C  C   . ASP A 1 419 ? 24.001 -31.220 -21.887 1.00 146.29 ? 345  ASP A C   1 
ATOM   2635 O  O   . ASP A 1 419 ? 24.643 -30.167 -21.882 1.00 151.53 ? 345  ASP A O   1 
ATOM   2636 C  CB  . ASP A 1 419 ? 22.384 -31.909 -23.674 1.00 140.62 ? 345  ASP A CB  1 
ATOM   2637 N  N   . GLY A 1 420 ? 24.520 -32.395 -21.539 1.00 142.29 ? 346  GLY A N   1 
ATOM   2638 C  CA  . GLY A 1 420 ? 25.907 -32.539 -21.129 1.00 131.67 ? 346  GLY A CA  1 
ATOM   2639 C  C   . GLY A 1 420 ? 26.890 -32.060 -22.178 1.00 128.83 ? 346  GLY A C   1 
ATOM   2640 O  O   . GLY A 1 420 ? 28.093 -31.986 -21.926 1.00 134.16 ? 346  GLY A O   1 
HETATM 2641 C  C01 . XY8 B 2 .   ? 12.979 -10.467 3.784   1.00 38.54  ? 1201 XY8 A C01 1 
HETATM 2642 C  C02 . XY8 B 2 .   ? 12.141 -10.727 5.030   1.00 44.83  ? 1201 XY8 A C02 1 
HETATM 2643 C  C03 . XY8 B 2 .   ? 10.663 -10.441 4.767   1.00 46.90  ? 1201 XY8 A C03 1 
HETATM 2644 C  C05 . XY8 B 2 .   ? 12.503 -10.144 7.465   1.00 44.11  ? 1201 XY8 A C05 1 
HETATM 2645 C  C07 . XY8 B 2 .   ? 12.167 -11.704 9.173   1.00 51.68  ? 1201 XY8 A C07 1 
HETATM 2646 C  C08 . XY8 B 2 .   ? 12.248 -10.672 10.119  1.00 59.97  ? 1201 XY8 A C08 1 
HETATM 2647 C  C09 . XY8 B 2 .   ? 12.108 -11.020 11.459  1.00 63.19  ? 1201 XY8 A C09 1 
HETATM 2648 C  C11 . XY8 B 2 .   ? 11.826 -13.258 10.983  1.00 63.88  ? 1201 XY8 A C11 1 
HETATM 2649 C  C12 . XY8 B 2 .   ? 11.597 -14.655 11.472  1.00 69.54  ? 1201 XY8 A C12 1 
HETATM 2650 C  C13 . XY8 B 2 .   ? 11.954 -13.010 9.615   1.00 55.68  ? 1201 XY8 A C13 1 
HETATM 2651 C  C15 . XY8 B 2 .   ? 12.585 -9.106  8.417   1.00 40.91  ? 1201 XY8 A C15 1 
HETATM 2652 C  C17 . XY8 B 2 .   ? 13.440 -6.886  9.019   1.00 43.01  ? 1201 XY8 A C17 1 
HETATM 2653 C  C18 . XY8 B 2 .   ? 13.855 -5.565  8.376   1.00 41.48  ? 1201 XY8 A C18 1 
HETATM 2654 C  C20 . XY8 B 2 .   ? 12.938 -3.525  7.186   1.00 39.92  ? 1201 XY8 A C20 1 
HETATM 2655 C  C21 . XY8 B 2 .   ? 11.669 -2.746  6.949   1.00 43.51  ? 1201 XY8 A C21 1 
HETATM 2656 C  C22 . XY8 B 2 .   ? 11.154 -1.875  7.919   1.00 39.10  ? 1201 XY8 A C22 1 
HETATM 2657 C  C24 . XY8 B 2 .   ? 9.977  -1.168  7.706   1.00 33.29  ? 1201 XY8 A C24 1 
HETATM 2658 C  C25 . XY8 B 2 .   ? 9.298  -1.338  6.507   1.00 30.96  ? 1201 XY8 A C25 1 
HETATM 2659 C  C27 . XY8 B 2 .   ? 9.778  -2.196  5.528   1.00 37.18  ? 1201 XY8 A C27 1 
HETATM 2660 C  C28 . XY8 B 2 .   ? 10.959 -2.897  5.752   1.00 42.66  ? 1201 XY8 A C28 1 
HETATM 2661 C  C29 . XY8 B 2 .   ? 12.092 -5.854  6.659   1.00 32.87  ? 1201 XY8 A C29 1 
HETATM 2662 C  C30 . XY8 B 2 .   ? 11.653 -7.143  7.337   1.00 35.26  ? 1201 XY8 A C30 1 
HETATM 2663 F  F23 . XY8 B 2 .   ? 11.805 -1.707  9.082   1.00 43.46  ? 1201 XY8 A F23 1 
HETATM 2664 F  F26 . XY8 B 2 .   ? 8.160  -0.664  6.284   1.00 30.38  ? 1201 XY8 A F26 1 
HETATM 2665 N  N04 . XY8 B 2 .   ? 12.638 -9.843  6.089   1.00 40.47  ? 1201 XY8 A N04 1 
HETATM 2666 N  N06 . XY8 B 2 .   ? 12.295 -11.424 7.860   1.00 49.34  ? 1201 XY8 A N06 1 
HETATM 2667 N  N10 . XY8 B 2 .   ? 11.901 -12.275 11.909  1.00 67.28  ? 1201 XY8 A N10 1 
HETATM 2668 N  N14 . XY8 B 2 .   ? 12.453 -9.396  9.735   1.00 50.08  ? 1201 XY8 A N14 1 
HETATM 2669 N  N16 . XY8 B 2 .   ? 12.797 -7.754  8.018   1.00 37.51  ? 1201 XY8 A N16 1 
HETATM 2670 N  N19 . XY8 B 2 .   ? 12.657 -4.923  7.710   1.00 31.74  ? 1201 XY8 A N19 1 
HETATM 2671 NA NA  . NA  C 3 .   ? 12.167 -7.520  -3.533  1.00 55.45  ? 1202 NA  A NA  1 
HETATM 2672 O  O   . HOH D 4 .   ? 4.696  -7.815  3.466   1.00 31.35  ? 1301 HOH A O   1 
HETATM 2673 O  O   . HOH D 4 .   ? 16.106 -0.136  15.210  1.00 38.11  ? 1302 HOH A O   1 
HETATM 2674 O  O   . HOH D 4 .   ? 1.221  0.338   18.281  1.00 44.49  ? 1303 HOH A O   1 
HETATM 2675 O  O   . HOH D 4 .   ? 14.297 -8.234  1.399   1.00 39.07  ? 1304 HOH A O   1 
HETATM 2676 O  O   . HOH D 4 .   ? 3.759  15.759  -68.321 1.00 38.25  ? 1305 HOH A 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   . LEU A 48  ? 1.6241 0.8783 1.0175 -0.0666 0.2230  0.0380  68   LEU A N   
2    C CA  . LEU A 48  ? 1.6457 0.8845 1.0173 -0.0381 0.2102  0.0483  68   LEU A CA  
3    C C   . LEU A 48  ? 1.6788 0.9488 1.0684 -0.0406 0.2107  0.0503  68   LEU A C   
4    O O   . LEU A 48  ? 1.6596 0.9390 1.0506 -0.0172 0.1993  0.0571  68   LEU A O   
5    C CB  . LEU A 48  ? 1.6757 0.9322 1.0675 -0.0103 0.1973  0.0506  68   LEU A CB  
6    C CG  . LEU A 48  ? 1.7619 0.9803 1.1273 0.0023  0.1919  0.0508  68   LEU A CG  
7    C CD1 . LEU A 48  ? 1.6970 0.9446 1.0923 0.0279  0.1803  0.0509  68   LEU A CD1 
8    C CD2 . LEU A 48  ? 1.7719 0.9301 1.0774 0.0161  0.1849  0.0580  68   LEU A CD2 
9    N N   . LEU A 49  ? 1.6993 0.9873 1.1035 -0.0685 0.2234  0.0436  69   LEU A N   
10   C CA  . LEU A 49  ? 1.5505 0.8682 0.9718 -0.0723 0.2244  0.0446  69   LEU A CA  
11   C C   . LEU A 49  ? 1.7385 1.0153 1.1111 -0.0587 0.2184  0.0546  69   LEU A C   
12   O O   . LEU A 49  ? 1.7169 1.0139 1.0996 -0.0411 0.2091  0.0601  69   LEU A O   
13   C CB  . LEU A 49  ? 1.5104 0.8524 0.9536 -0.1042 0.2389  0.0341  69   LEU A CB  
14   N N   . PRO A 50  ? 1.7703 0.9903 1.0891 -0.0653 0.2224  0.0573  70   PRO A N   
15   C CA  . PRO A 50  ? 1.8042 0.9824 1.0735 -0.0503 0.2145  0.0671  70   PRO A CA  
16   C C   . PRO A 50  ? 1.8694 1.0127 1.1075 -0.0179 0.1977  0.0749  70   PRO A C   
17   O O   . PRO A 50  ? 1.8313 0.9343 1.0237 -0.0046 0.1897  0.0823  70   PRO A O   
18   C CB  . PRO A 50  ? 1.7913 0.9242 1.0176 -0.0759 0.2279  0.0653  70   PRO A CB  
19   C CG  . PRO A 50  ? 1.7337 0.8621 0.9685 -0.0908 0.2360  0.0577  70   PRO A CG  
20   C CD  . PRO A 50  ? 1.7183 0.9113 1.0192 -0.0901 0.2352  0.0508  70   PRO A CD  
21   N N   . ALA A 51  ? 1.8964 1.0552 1.1582 -0.0045 0.1918  0.0727  71   ALA A N   
22   C CA  . ALA A 51  ? 1.8853 1.0151 1.1221 0.0264  0.1759  0.0777  71   ALA A CA  
23   C C   . ALA A 51  ? 1.8499 1.0260 1.1240 0.0537  0.1619  0.0796  71   ALA A C   
24   O O   . ALA A 51  ? 1.8594 1.0714 1.1738 0.0582  0.1610  0.0755  71   ALA A O   
25   C CB  . ALA A 51  ? 1.7672 0.8784 1.0007 0.0213  0.1798  0.0730  71   ALA A CB  
26   N N   . VAL A 52  ? 1.8406 1.0150 1.0998 0.0719  0.1504  0.0857  72   VAL A N   
27   C CA  . VAL A 52  ? 1.7352 0.9560 1.0293 0.0969  0.1369  0.0870  72   VAL A CA  
28   C C   . VAL A 52  ? 1.7413 0.9541 1.0289 0.1297  0.1196  0.0874  72   VAL A C   
29   O O   . VAL A 52  ? 1.8010 1.0546 1.1289 0.1424  0.1145  0.0839  72   VAL A O   
30   C CB  . VAL A 52  ? 1.6511 0.8779 0.9344 0.1027  0.1308  0.0922  72   VAL A CB  
31   C CG1 . VAL A 52  ? 1.5441 0.8200 0.8629 0.1290  0.1158  0.0929  72   VAL A CG1 
32   C CG2 . VAL A 52  ? 1.6252 0.8660 0.9201 0.0702  0.1481  0.0903  72   VAL A CG2 
33   N N   . ASN A 53  ? 1.8631 1.0250 1.1009 0.1442  0.1100  0.0909  73   ASN A N   
34   C CA  . ASN A 53  ? 1.7828 0.9381 1.0157 0.1753  0.0933  0.0894  73   ASN A CA  
35   C C   . ASN A 53  ? 1.8227 0.9801 1.0730 0.1694  0.0999  0.0840  73   ASN A C   
36   O O   . ASN A 53  ? 1.7949 0.9863 1.0772 0.1902  0.0899  0.0799  73   ASN A O   
37   C CB  . ASN A 53  ? 1.6717 0.7666 0.8445 0.1900  0.0824  0.0939  73   ASN A CB  
38   C CG  . ASN A 53  ? 1.4706 0.5644 0.6412 0.2255  0.0625  0.0914  73   ASN A CG  
39   O OD1 . ASN A 53  ? 1.6341 0.7666 0.8448 0.2361  0.0591  0.0856  73   ASN A OD1 
40   N ND2 . ASN A 53  ? 1.4194 0.4692 0.5432 0.2438  0.0491  0.0949  73   ASN A ND2 
41   N N   . PRO A 54  ? 1.6617 0.7877 0.8949 0.1418  0.1159  0.0826  74   PRO A N   
42   C CA  . PRO A 54  ? 1.6277 0.7622 0.8829 0.1351  0.1220  0.0766  74   PRO A CA  
43   C C   . PRO A 54  ? 1.5884 0.7876 0.9049 0.1315  0.1257  0.0720  74   PRO A C   
44   O O   . PRO A 54  ? 1.5965 0.8125 0.9368 0.1387  0.1238  0.0671  74   PRO A O   
45   C CB  . PRO A 54  ? 1.7488 0.8446 0.9772 0.1012  0.1398  0.0754  74   PRO A CB  
46   C CG  . PRO A 54  ? 1.7727 0.8188 0.9473 0.1016  0.1373  0.0818  74   PRO A CG  
47   C CD  . PRO A 54  ? 1.7476 0.8253 0.9367 0.1173  0.1276  0.0857  74   PRO A CD  
48   N N   . TRP A 55  ? 1.5823 0.8172 0.9245 0.1205  0.1311  0.0734  75   TRP A N   
49   C CA  . TRP A 55  ? 1.5017 0.7973 0.9000 0.1232  0.1310  0.0702  75   TRP A CA  
50   C C   . TRP A 55  ? 1.5105 0.8322 0.9249 0.1588  0.1123  0.0699  75   TRP A C   
51   O O   . TRP A 55  ? 1.4915 0.8493 0.9435 0.1665  0.1100  0.0650  75   TRP A O   
52   C CB  . TRP A 55  ? 1.4375 0.7644 0.8574 0.1072  0.1385  0.0721  75   TRP A CB  
53   C CG  . TRP A 55  ? 1.4469 0.7843 0.8857 0.0716  0.1572  0.0673  75   TRP A CG  
54   C CD1 . TRP A 55  ? 1.4741 0.8018 0.9012 0.0467  0.1685  0.0669  75   TRP A CD1 
55   C CD2 . TRP A 55  ? 1.4532 0.8177 0.9291 0.0574  0.1656  0.0604  75   TRP A CD2 
56   N NE1 . TRP A 55  ? 1.5378 0.8888 0.9954 0.0186  0.1825  0.0592  75   TRP A NE1 
57   C CE2 . TRP A 55  ? 1.4736 0.8463 0.9605 0.0244  0.1807  0.0554  75   TRP A CE2 
58   C CE3 . TRP A 55  ? 1.4723 0.8568 0.9742 0.0694  0.1611  0.0570  75   TRP A CE3 
59   C CZ2 . TRP A 55  ? 1.4244 0.8256 0.9477 0.0040  0.1900  0.0469  75   TRP A CZ2 
60   C CZ3 . TRP A 55  ? 1.4281 0.8355 0.9622 0.0481  0.1718  0.0499  75   TRP A CZ3 
61   C CH2 . TRP A 55  ? 1.3978 0.8141 0.9426 0.0159  0.1854  0.0448  75   TRP A CH2 
62   N N   . ASP A 56  ? 1.4922 0.7985 0.8799 0.1803  0.0983  0.0739  76   ASP A N   
63   C CA  . ASP A 56  ? 1.5184 0.8557 0.9247 0.2135  0.0793  0.0713  76   ASP A CA  
64   C C   . ASP A 56  ? 1.6173 0.9400 1.0183 0.2289  0.0727  0.0660  76   ASP A C   
65   O O   . ASP A 56  ? 1.6035 0.9695 1.0438 0.2426  0.0665  0.0596  76   ASP A O   
66   C CB  . ASP A 56  ? 1.5156 0.8384 0.8929 0.2314  0.0655  0.0756  76   ASP A CB  
67   C CG  . ASP A 56  ? 1.5281 0.8779 0.9194 0.2217  0.0686  0.0795  76   ASP A CG  
68   O OD1 . ASP A 56  ? 1.6382 0.9688 1.0165 0.1944  0.0841  0.0829  76   ASP A OD1 
69   O OD2 . ASP A 56  ? 1.5621 0.9550 0.9794 0.2406  0.0556  0.0780  76   ASP A OD2 
70   N N   . VAL A 57  ? 1.5264 0.7887 0.8795 0.2258  0.0744  0.0679  77   VAL A N   
71   C CA  . VAL A 57  ? 1.4238 0.6688 0.7692 0.2420  0.0672  0.0627  77   VAL A CA  
72   C C   . VAL A 57  ? 1.3783 0.6552 0.7643 0.2316  0.0761  0.0561  77   VAL A C   
73   O O   . VAL A 57  ? 1.4333 0.7289 0.8386 0.2501  0.0678  0.0492  77   VAL A O   
74   C CB  . VAL A 57  ? 1.5003 0.6712 0.7860 0.2355  0.0700  0.0662  77   VAL A CB  
75   C CG1 . VAL A 57  ? 1.5522 0.6892 0.7953 0.2422  0.0627  0.0732  77   VAL A CG1 
76   C CG2 . VAL A 57  ? 1.4240 0.5726 0.7024 0.1998  0.0906  0.0666  77   VAL A CG2 
77   N N   . LEU A 58  ? 1.3520 0.6375 0.7530 0.2018  0.0930  0.0569  78   LEU A N   
78   C CA  . LEU A 58  ? 1.3203 0.6395 0.7620 0.1915  0.1009  0.0503  78   LEU A CA  
79   C C   . LEU A 58  ? 1.3139 0.6975 0.8053 0.2111  0.0912  0.0457  78   LEU A C   
80   O O   . LEU A 58  ? 1.3880 0.7949 0.9046 0.2204  0.0881  0.0380  78   LEU A O   
81   C CB  . LEU A 58  ? 1.2806 0.6028 0.7322 0.1564  0.1195  0.0514  78   LEU A CB  
82   C CG  . LEU A 58  ? 1.3402 0.6692 0.8125 0.1376  0.1305  0.0443  78   LEU A CG  
83   C CD1 . LEU A 58  ? 1.3457 0.6733 0.8222 0.1015  0.1479  0.0444  78   LEU A CD1 
84   C CD2 . LEU A 58  ? 1.2856 0.6701 0.8079 0.1501  0.1258  0.0381  78   LEU A CD2 
85   N N   . LEU A 59  ? 1.3325 0.7470 0.8389 0.2167  0.0863  0.0495  79   LEU A N   
86   C CA  . LEU A 59  ? 1.2057 0.6846 0.7601 0.2336  0.0767  0.0446  79   LEU A CA  
87   C C   . LEU A 59  ? 1.2456 0.7332 0.7968 0.2647  0.0583  0.0403  79   LEU A C   
88   O O   . LEU A 59  ? 1.1426 0.6803 0.7335 0.2776  0.0514  0.0323  79   LEU A O   
89   C CB  . LEU A 59  ? 1.1771 0.6881 0.7508 0.2269  0.0782  0.0494  79   LEU A CB  
90   C CG  . LEU A 59  ? 1.2377 0.7436 0.7907 0.2420  0.0661  0.0543  79   LEU A CG  
91   C CD1 . LEU A 59  ? 1.2297 0.7893 0.8160 0.2672  0.0492  0.0482  79   LEU A CD1 
92   C CD2 . LEU A 59  ? 1.3701 0.8770 0.9211 0.2237  0.0751  0.0613  79   LEU A CD2 
93   N N   . CYS A 60  ? 1.4443 0.8849 0.9496 0.2757  0.0506  0.0446  80   CYS A N   
94   C CA  . CYS A 60  ? 1.2864 0.7353 0.7885 0.3059  0.0322  0.0400  80   CYS A CA  
95   C C   . CYS A 60  ? 1.3709 0.8341 0.8926 0.3180  0.0290  0.0300  80   CYS A C   
96   O O   . CYS A 60  ? 1.3589 0.8737 0.9175 0.3350  0.0192  0.0217  80   CYS A O   
97   C CB  . CYS A 60  ? 1.3337 0.7190 0.7770 0.3141  0.0258  0.0461  80   CYS A CB  
98   S SG  . CYS A 60  ? 1.3563 0.7241 0.7730 0.3025  0.0279  0.0564  80   CYS A SG  
99   N N   . VAL A 61  ? 1.1981 0.6173 0.6961 0.3079  0.0379  0.0297  81   VAL A N   
100  C CA  . VAL A 61  ? 1.1918 0.6213 0.7061 0.3187  0.0357  0.0196  81   VAL A CA  
101  C C   . VAL A 61  ? 1.1730 0.6551 0.7375 0.3049  0.0454  0.0134  81   VAL A C   
102  O O   . VAL A 61  ? 1.1632 0.6789 0.7570 0.3162  0.0418  0.0030  81   VAL A O   
103  C CB  . VAL A 61  ? 1.1464 0.5073 0.6147 0.3139  0.0404  0.0209  81   VAL A CB  
104  C CG1 . VAL A 61  ? 1.1426 0.4564 0.5644 0.3341  0.0273  0.0245  81   VAL A CG1 
105  C CG2 . VAL A 61  ? 1.3213 0.6480 0.7698 0.2810  0.0578  0.0280  81   VAL A CG2 
106  N N   . SER A 62  ? 1.2101 0.7006 0.7852 0.2804  0.0578  0.0187  82   SER A N   
107  C CA  . SER A 62  ? 1.2031 0.7440 0.8251 0.2678  0.0660  0.0129  82   SER A CA  
108  C C   . SER A 62  ? 1.1066 0.7167 0.7745 0.2826  0.0561  0.0067  82   SER A C   
109  O O   . SER A 62  ? 1.0544 0.7079 0.7599 0.2799  0.0590  -0.0018 82   SER A O   
110  C CB  . SER A 62  ? 1.2127 0.7504 0.8375 0.2404  0.0799  0.0197  82   SER A CB  
111  O OG  . SER A 62  ? 1.3272 0.8059 0.9135 0.2218  0.0907  0.0237  82   SER A OG  
112  N N   . GLY A 63  ? 1.1544 0.7760 0.8191 0.2963  0.0449  0.0102  83   GLY A N   
113  C CA  . GLY A 63  ? 1.1246 0.8109 0.8315 0.3090  0.0349  0.0032  83   GLY A CA  
114  C C   . GLY A 63  ? 1.1478 0.8494 0.8666 0.3274  0.0278  -0.0083 83   GLY A C   
115  O O   . GLY A 63  ? 1.1186 0.8769 0.8802 0.3282  0.0270  -0.0171 83   GLY A O   
116  N N   . THR A 64  ? 1.0904 0.7409 0.7706 0.3416  0.0230  -0.0085 84   THR A N   
117  C CA  . THR A 64  ? 1.1546 0.8149 0.8440 0.3598  0.0172  -0.0202 84   THR A CA  
118  C C   . THR A 64  ? 1.0665 0.7468 0.7819 0.3465  0.0291  -0.0278 84   THR A C   
119  O O   . THR A 64  ? 1.0545 0.7807 0.8041 0.3539  0.0275  -0.0391 84   THR A O   
120  C CB  . THR A 64  ? 1.2053 0.7993 0.8442 0.3754  0.0108  -0.0182 84   THR A CB  
121  O OG1 . THR A 64  ? 1.2793 0.8547 0.8922 0.3882  -0.0010 -0.0116 84   THR A OG1 
122  C CG2 . THR A 64  ? 1.1765 0.7804 0.8255 0.3962  0.0046  -0.0312 84   THR A CG2 
123  N N   . VAL A 65  ? 1.3155 0.9623 1.0144 0.3256  0.0416  -0.0226 85   VAL A N   
124  C CA  . VAL A 65  ? 1.2559 0.9207 0.9775 0.3115  0.0528  -0.0301 85   VAL A CA  
125  C C   . VAL A 65  ? 1.3061 1.0420 1.0783 0.3026  0.0553  -0.0342 85   VAL A C   
126  O O   . VAL A 65  ? 1.2807 1.0560 1.0824 0.3054  0.0565  -0.0451 85   VAL A O   
127  C CB  . VAL A 65  ? 1.2296 0.8469 0.9246 0.2883  0.0656  -0.0235 85   VAL A CB  
128  C CG1 . VAL A 65  ? 0.9948 0.6361 0.7153 0.2722  0.0766  -0.0316 85   VAL A CG1 
129  C CG2 . VAL A 65  ? 1.2943 0.8410 0.9391 0.2941  0.0641  -0.0207 85   VAL A CG2 
130  N N   . ILE A 66  ? 1.1588 0.9113 0.9404 0.2912  0.0563  -0.0257 86   ILE A N   
131  C CA  . ILE A 66  ? 1.1304 0.9468 0.9577 0.2797  0.0587  -0.0285 86   ILE A CA  
132  C C   . ILE A 66  ? 1.1526 1.0180 1.0087 0.2950  0.0490  -0.0371 86   ILE A C   
133  O O   . ILE A 66  ? 1.1363 1.0488 1.0272 0.2878  0.0527  -0.0450 86   ILE A O   
134  C CB  . ILE A 66  ? 1.0109 0.8317 0.8398 0.2668  0.0602  -0.0178 86   ILE A CB  
135  C CG1 . ILE A 66  ? 1.1493 0.9271 0.9552 0.2481  0.0728  -0.0111 86   ILE A CG1 
136  C CG2 . ILE A 66  ? 0.9531 0.8397 0.8284 0.2560  0.0602  -0.0206 86   ILE A CG2 
137  C CD1 . ILE A 66  ? 1.1004 0.8711 0.9002 0.2371  0.0757  -0.0006 86   ILE A CD1 
138  N N   . ALA A 67  ? 1.1736 1.0276 1.0140 0.3150  0.0370  -0.0360 87   ALA A N   
139  C CA  . ALA A 67  ? 1.0474 0.9455 0.9135 0.3304  0.0279  -0.0455 87   ALA A CA  
140  C C   . ALA A 67  ? 1.0000 0.9038 0.8739 0.3390  0.0308  -0.0577 87   ALA A C   
141  O O   . ALA A 67  ? 0.8621 0.8163 0.7708 0.3381  0.0320  -0.0671 87   ALA A O   
142  C CB  . ALA A 67  ? 1.0051 0.8836 0.8477 0.3519  0.0136  -0.0427 87   ALA A CB  
143  N N   . GLY A 68  ? 1.0133 0.8640 0.8536 0.3460  0.0329  -0.0579 88   GLY A N   
144  C CA  . GLY A 68  ? 1.1351 0.9874 0.9799 0.3560  0.0353  -0.0703 88   GLY A CA  
145  C C   . GLY A 68  ? 1.0352 0.9194 0.9077 0.3367  0.0484  -0.0767 88   GLY A C   
146  O O   . GLY A 68  ? 1.0701 0.9975 0.9715 0.3397  0.0504  -0.0877 88   GLY A O   
147  N N   . GLU A 69  ? 0.9800 0.8433 0.8430 0.3160  0.0580  -0.0702 89   GLU A N   
148  C CA  . GLU A 69  ? 0.9231 0.8107 0.8066 0.2981  0.0699  -0.0767 89   GLU A CA  
149  C C   . GLU A 69  ? 0.8395 0.7928 0.7652 0.2876  0.0714  -0.0792 89   GLU A C   
150  O O   . GLU A 69  ? 0.8219 0.8075 0.7687 0.2838  0.0775  -0.0891 89   GLU A O   
151  C CB  . GLU A 69  ? 0.9136 0.7675 0.7787 0.2778  0.0785  -0.0691 89   GLU A CB  
152  C CG  . GLU A 69  ? 1.0873 0.8703 0.9066 0.2829  0.0779  -0.0640 89   GLU A CG  
153  C CD  . GLU A 69  ? 1.1570 0.9140 0.9582 0.3041  0.0729  -0.0726 89   GLU A CD  
154  O OE1 . GLU A 69  ? 1.0597 0.8431 0.8795 0.3080  0.0761  -0.0851 89   GLU A OE1 
155  O OE2 . GLU A 69  ? 1.1481 0.8571 0.9150 0.3167  0.0660  -0.0671 89   GLU A OE2 
156  N N   . ASN A 70  ? 0.9363 0.9079 0.8726 0.2819  0.0665  -0.0704 90   ASN A N   
157  C CA  . ASN A 70  ? 0.8349 0.8645 0.8087 0.2703  0.0672  -0.0720 90   ASN A CA  
158  C C   . ASN A 70  ? 0.7339 0.7965 0.7257 0.2859  0.0624  -0.0824 90   ASN A C   
159  O O   . ASN A 70  ? 0.6472 0.7513 0.6657 0.2763  0.0681  -0.0888 90   ASN A O   
160  C CB  . ASN A 70  ? 0.8312 0.8690 0.8098 0.2626  0.0618  -0.0612 90   ASN A CB  
161  C CG  . ASN A 70  ? 0.8188 0.8397 0.7906 0.2425  0.0690  -0.0524 90   ASN A CG  
162  O OD1 . ASN A 70  ? 0.7505 0.8010 0.7447 0.2227  0.0746  -0.0518 90   ASN A OD1 
163  N ND2 . ASN A 70  ? 0.8922 0.8630 0.8311 0.2469  0.0690  -0.0455 90   ASN A ND2 
164  N N   . ALA A 71  ? 0.7595 0.8029 0.7351 0.3099  0.0521  -0.0843 91   ALA A N   
165  C CA  . ALA A 71  ? 0.8006 0.8745 0.7925 0.3272  0.0471  -0.0957 91   ALA A CA  
166  C C   . ALA A 71  ? 0.7174 0.8001 0.7168 0.3274  0.0569  -0.1077 91   ALA A C   
167  O O   . ALA A 71  ? 0.5598 0.6835 0.5834 0.3316  0.0582  -0.1177 91   ALA A O   
168  C CB  . ALA A 71  ? 0.8835 0.9269 0.8509 0.3547  0.0336  -0.0961 91   ALA A CB  
169  N N   . LEU A 72  ? 0.6926 0.7366 0.6703 0.3227  0.0641  -0.1074 92   LEU A N   
170  C CA  . LEU A 72  ? 0.7465 0.7977 0.7296 0.3206  0.0746  -0.1190 92   LEU A CA  
171  C C   . LEU A 72  ? 0.6593 0.7522 0.6684 0.2956  0.0857  -0.1196 92   LEU A C   
172  O O   . LEU A 72  ? 0.7165 0.8426 0.7437 0.2949  0.0922  -0.1296 92   LEU A O   
173  C CB  . LEU A 72  ? 0.8039 0.7991 0.7538 0.3213  0.0786  -0.1189 92   LEU A CB  
174  C CG  . LEU A 72  ? 0.7661 0.7635 0.7174 0.3134  0.0910  -0.1300 92   LEU A CG  
175  C CD1 . LEU A 72  ? 0.6661 0.6907 0.6321 0.3302  0.0917  -0.1444 92   LEU A CD1 
176  C CD2 . LEU A 72  ? 0.7285 0.6660 0.6442 0.3136  0.0932  -0.1296 92   LEU A CD2 
177  N N   . VAL A 73  ? 0.6191 0.7094 0.6287 0.2749  0.0882  -0.1087 93   VAL A N   
178  C CA  . VAL A 73  ? 0.6658 0.7892 0.6953 0.2506  0.0979  -0.1079 93   VAL A CA  
179  C C   . VAL A 73  ? 0.6736 0.8473 0.7322 0.2483  0.0963  -0.1101 93   VAL A C   
180  O O   . VAL A 73  ? 0.7417 0.9445 0.8146 0.2388  0.1049  -0.1161 93   VAL A O   
181  C CB  . VAL A 73  ? 0.6563 0.7664 0.6807 0.2311  0.0987  -0.0957 93   VAL A CB  
182  C CG1 . VAL A 73  ? 0.6189 0.7621 0.6628 0.2067  0.1065  -0.0936 93   VAL A CG1 
183  C CG2 . VAL A 73  ? 0.6430 0.7044 0.6381 0.2313  0.1018  -0.0949 93   VAL A CG2 
184  N N   . VAL A 74  ? 0.6592 0.8425 0.7247 0.2566  0.0855  -0.1055 94   VAL A N   
185  C CA  . VAL A 74  ? 0.5654 0.7954 0.6577 0.2531  0.0835  -0.1080 94   VAL A CA  
186  C C   . VAL A 74  ? 0.6571 0.9109 0.7597 0.2662  0.0871  -0.1223 94   VAL A C   
187  O O   . VAL A 74  ? 0.6887 0.9821 0.8123 0.2563  0.0924  -0.1267 94   VAL A O   
188  C CB  . VAL A 74  ? 0.6121 0.8452 0.7067 0.2630  0.0702  -0.1028 94   VAL A CB  
189  C CG1 . VAL A 74  ? 0.4960 0.7768 0.6181 0.2555  0.0685  -0.1053 94   VAL A CG1 
190  C CG2 . VAL A 74  ? 0.7534 0.9586 0.8342 0.2524  0.0672  -0.0895 94   VAL A CG2 
191  N N   . ALA A 75  ? 0.6774 0.9063 0.7642 0.2885  0.0846  -0.1300 95   ALA A N   
192  C CA  . ALA A 75  ? 0.7032 0.9537 0.7995 0.3029  0.0881  -0.1449 95   ALA A CA  
193  C C   . ALA A 75  ? 0.7352 0.9982 0.8356 0.2867  0.1036  -0.1503 95   ALA A C   
194  O O   . ALA A 75  ? 0.7908 1.0931 0.9102 0.2845  0.1096  -0.1591 95   ALA A O   
195  C CB  . ALA A 75  ? 0.7435 0.9576 0.8183 0.3305  0.0811  -0.1513 95   ALA A CB  
196  N N   . LEU A 76  ? 0.7099 0.9402 0.7913 0.2748  0.1104  -0.1456 96   LEU A N   
197  C CA  . LEU A 76  ? 0.7324 0.9702 0.8126 0.2606  0.1247  -0.1512 96   LEU A CA  
198  C C   . LEU A 76  ? 0.6837 0.9616 0.7834 0.2380  0.1307  -0.1467 96   LEU A C   
199  O O   . LEU A 76  ? 0.7555 1.0596 0.8630 0.2329  0.1404  -0.1547 96   LEU A O   
200  C CB  . LEU A 76  ? 0.8117 1.0070 0.8670 0.2509  0.1293  -0.1469 96   LEU A CB  
201  C CG  . LEU A 76  ? 0.7571 0.9076 0.7878 0.2701  0.1268  -0.1537 96   LEU A CG  
202  C CD1 . LEU A 76  ? 0.6672 0.7808 0.6750 0.2558  0.1326  -0.1505 96   LEU A CD1 
203  C CD2 . LEU A 76  ? 0.5973 0.7579 0.6300 0.2861  0.1319  -0.1696 96   LEU A CD2 
204  N N   . ILE A 77  ? 0.6238 0.9053 0.7298 0.2239  0.1252  -0.1339 97   ILE A N   
205  C CA  . ILE A 77  ? 0.6437 0.9589 0.7662 0.2026  0.1293  -0.1289 97   ILE A CA  
206  C C   . ILE A 77  ? 0.6683 1.0259 0.8127 0.2104  0.1284  -0.1381 97   ILE A C   
207  O O   . ILE A 77  ? 0.6088 0.9958 0.7630 0.1980  0.1369  -0.1418 97   ILE A O   
208  C CB  . ILE A 77  ? 0.7218 1.0295 0.8465 0.1886  0.1219  -0.1143 97   ILE A CB  
209  C CG1 . ILE A 77  ? 0.6839 0.9627 0.7919 0.1726  0.1265  -0.1060 97   ILE A CG1 
210  C CG2 . ILE A 77  ? 0.6493 0.9933 0.7940 0.1736  0.1215  -0.1108 97   ILE A CG2 
211  C CD1 . ILE A 77  ? 0.7336 0.9721 0.8201 0.1849  0.1259  -0.1085 97   ILE A CD1 
212  N N   . ALA A 78  ? 0.6321 0.9936 0.7832 0.2312  0.1179  -0.1423 98   ALA A N   
213  C CA  . ALA A 78  ? 0.6288 1.0328 0.8021 0.2400  0.1158  -0.1526 98   ALA A CA  
214  C C   . ALA A 78  ? 0.6581 1.0769 0.8337 0.2516  0.1248  -0.1683 98   ALA A C   
215  O O   . ALA A 78  ? 0.6513 1.1113 0.8453 0.2475  0.1303  -0.1769 98   ALA A O   
216  C CB  . ALA A 78  ? 0.5592 0.9614 0.7363 0.2607  0.1008  -0.1533 98   ALA A CB  
217  N N   . SER A 79  ? 0.6050 0.9904 0.7616 0.2657  0.1266  -0.1729 99   SER A N   
218  C CA  . SER A 79  ? 0.6082 1.0028 0.7651 0.2804  0.1339  -0.1890 99   SER A CA  
219  C C   . SER A 79  ? 0.6709 1.0604 0.8163 0.2641  0.1496  -0.1911 99   SER A C   
220  O O   . SER A 79  ? 0.7474 1.1375 0.8882 0.2754  0.1570  -0.2044 99   SER A O   
221  C CB  . SER A 79  ? 0.7315 1.0899 0.8723 0.3082  0.1256  -0.1946 99   SER A CB  
222  O OG  . SER A 79  ? 0.7943 1.1032 0.9090 0.3030  0.1259  -0.1856 99   SER A OG  
223  N N   . THR A 80  ? 0.8518 1.2355 0.9911 0.2386  0.1543  -0.1787 100  THR A N   
224  C CA  . THR A 80  ? 0.8389 1.2167 0.9640 0.2221  0.1679  -0.1794 100  THR A CA  
225  C C   . THR A 80  ? 0.9803 1.3906 1.1167 0.1972  0.1733  -0.1729 100  THR A C   
226  O O   . THR A 80  ? 0.9215 1.3262 1.0590 0.1820  0.1677  -0.1589 100  THR A O   
227  C CB  . THR A 80  ? 0.8962 1.2268 0.9959 0.2156  0.1678  -0.1709 100  THR A CB  
228  O OG1 . THR A 80  ? 0.6000 0.8973 0.6875 0.2382  0.1621  -0.1769 100  THR A OG1 
229  C CG2 . THR A 80  ? 0.9104 1.2347 0.9929 0.2002  0.1810  -0.1729 100  THR A CG2 
230  N N   . PRO A 81  ? 0.9800 1.4232 1.1239 0.1923  0.1837  -0.1827 101  PRO A N   
231  C CA  . PRO A 81  ? 0.9225 1.3936 1.0741 0.1674  0.1886  -0.1762 101  PRO A CA  
232  C C   . PRO A 81  ? 0.9326 1.3782 1.0633 0.1456  0.1915  -0.1628 101  PRO A C   
233  O O   . PRO A 81  ? 1.0759 1.5300 1.2112 0.1266  0.1888  -0.1516 101  PRO A O   
234  C CB  . PRO A 81  ? 1.0761 1.5822 1.2348 0.1685  0.2009  -0.1916 101  PRO A CB  
235  C CG  . PRO A 81  ? 1.0912 1.5748 1.2351 0.1875  0.2055  -0.2028 101  PRO A CG  
236  C CD  . PRO A 81  ? 1.1621 1.6151 1.3043 0.2073  0.1926  -0.2000 101  PRO A CD  
237  N N   . ALA A 82  ? 0.8388 1.2525 0.9460 0.1482  0.1962  -0.1642 102  ALA A N   
238  C CA  . ALA A 82  ? 0.8627 1.2529 0.9492 0.1288  0.1978  -0.1525 102  ALA A CA  
239  C C   . ALA A 82  ? 0.7020 1.0725 0.7904 0.1227  0.1864  -0.1376 102  ALA A C   
240  O O   . ALA A 82  ? 0.7864 1.1475 0.8649 0.1040  0.1855  -0.1263 102  ALA A O   
241  C CB  . ALA A 82  ? 0.9386 1.2970 0.9988 0.1348  0.2041  -0.1587 102  ALA A CB  
242  N N   . LEU A 83  ? 0.6290 0.9934 0.7292 0.1384  0.1771  -0.1376 103  LEU A N   
243  C CA  . LEU A 83  ? 0.6263 0.9735 0.7291 0.1338  0.1665  -0.1246 103  LEU A CA  
244  C C   . LEU A 83  ? 0.6328 1.0080 0.7575 0.1270  0.1600  -0.1190 103  LEU A C   
245  O O   . LEU A 83  ? 0.6045 0.9682 0.7332 0.1250  0.1506  -0.1095 103  LEU A O   
246  C CB  . LEU A 83  ? 0.7091 1.0282 0.8069 0.1542  0.1597  -0.1273 103  LEU A CB  
247  C CG  . LEU A 83  ? 0.7369 1.0226 0.8111 0.1612  0.1654  -0.1337 103  LEU A CG  
248  C CD1 . LEU A 83  ? 0.7128 0.9698 0.7814 0.1817  0.1576  -0.1368 103  LEU A CD1 
249  C CD2 . LEU A 83  ? 0.7406 1.0059 0.7972 0.1418  0.1685  -0.1248 103  LEU A CD2 
250  N N   . ARG A 84  ? 0.7081 1.1194 0.8459 0.1226  0.1652  -0.1256 104  ARG A N   
251  C CA  . ARG A 84  ? 0.7783 1.2168 0.9359 0.1147  0.1599  -0.1220 104  ARG A CA  
252  C C   . ARG A 84  ? 0.7840 1.2188 0.9369 0.0899  0.1593  -0.1089 104  ARG A C   
253  O O   . ARG A 84  ? 0.8880 1.3398 1.0546 0.0814  0.1545  -0.1048 104  ARG A O   
254  C CB  . ARG A 84  ? 0.7837 1.2638 0.9576 0.1182  0.1664  -0.1353 104  ARG A CB  
255  C CG  . ARG A 84  ? 0.7876 1.2966 0.9845 0.1187  0.1591  -0.1363 104  ARG A CG  
256  C CD  . ARG A 84  ? 0.8105 1.3636 1.0225 0.1110  0.1677  -0.1469 104  ARG A CD  
257  N NE  . ARG A 84  ? 0.9026 1.4586 1.1053 0.0851  0.1754  -0.1400 104  ARG A NE  
258  C CZ  . ARG A 84  ? 0.8285 1.3856 1.0333 0.0668  0.1711  -0.1297 104  ARG A CZ  
259  N NH1 . ARG A 84  ? 0.8132 1.3711 1.0291 0.0704  0.1595  -0.1256 104  ARG A NH1 
260  N NH2 . ARG A 84  ? 0.7735 1.3308 0.9670 0.0444  0.1780  -0.1241 104  ARG A NH2 
261  N N   . THR A 85  ? 0.5676 0.9804 0.7009 0.0788  0.1633  -0.1029 105  THR A N   
262  C CA  . THR A 85  ? 0.5001 0.9079 0.6273 0.0566  0.1615  -0.0908 105  THR A CA  
263  C C   . THR A 85  ? 0.4602 0.8536 0.5947 0.0551  0.1498  -0.0801 105  THR A C   
264  O O   . THR A 85  ? 0.4740 0.8512 0.6102 0.0696  0.1439  -0.0801 105  THR A O   
265  C CB  . THR A 85  ? 0.5059 0.8907 0.6095 0.0478  0.1658  -0.0868 105  THR A CB  
266  O OG1 . THR A 85  ? 0.6190 0.9986 0.7164 0.0273  0.1623  -0.0751 105  THR A OG1 
267  C CG2 . THR A 85  ? 0.5968 0.9494 0.6904 0.0600  0.1618  -0.0854 105  THR A CG2 
268  N N   . PRO A 86  ? 0.4070 0.8045 0.5444 0.0379  0.1463  -0.0713 106  PRO A N   
269  C CA  . PRO A 86  ? 0.4384 0.8225 0.5827 0.0368  0.1354  -0.0622 106  PRO A CA  
270  C C   . PRO A 86  ? 0.3912 0.7424 0.5255 0.0429  0.1303  -0.0563 106  PRO A C   
271  O O   . PRO A 86  ? 0.3385 0.6802 0.4796 0.0512  0.1227  -0.0539 106  PRO A O   
272  C CB  . PRO A 86  ? 0.4757 0.8645 0.6177 0.0155  0.1342  -0.0544 106  PRO A CB  
273  C CG  . PRO A 86  ? 0.5561 0.9724 0.6991 0.0080  0.1441  -0.0617 106  PRO A CG  
274  C CD  . PRO A 86  ? 0.4174 0.8326 0.5519 0.0191  0.1522  -0.0703 106  PRO A CD  
275  N N   . MET A 87  ? 0.3883 0.7228 0.5058 0.0384  0.1343  -0.0546 107  MET A N   
276  C CA  . MET A 87  ? 0.4476 0.7527 0.5558 0.0428  0.1304  -0.0501 107  MET A CA  
277  C C   . MET A 87  ? 0.3503 0.6480 0.4617 0.0629  0.1295  -0.0570 107  MET A C   
278  O O   . MET A 87  ? 0.3839 0.6663 0.4981 0.0679  0.1226  -0.0528 107  MET A O   
279  C CB  . MET A 87  ? 0.5867 0.8793 0.6758 0.0361  0.1359  -0.0500 107  MET A CB  
280  C CG  . MET A 87  ? 0.5197 0.7842 0.5989 0.0400  0.1332  -0.0471 107  MET A CG  
281  S SD  . MET A 87  ? 0.6155 0.8677 0.6707 0.0377  0.1412  -0.0521 107  MET A SD  
282  C CE  . MET A 87  ? 0.7502 0.9717 0.7985 0.0474  0.1389  -0.0522 107  MET A CE  
283  N N   . PHE A 88  ? 0.4544 0.7622 0.5644 0.0749  0.1362  -0.0680 108  PHE A N   
284  C CA  . PHE A 88  ? 0.4772 0.7743 0.5868 0.0956  0.1347  -0.0753 108  PHE A CA  
285  C C   . PHE A 88  ? 0.4818 0.7949 0.6087 0.1062  0.1272  -0.0769 108  PHE A C   
286  O O   . PHE A 88  ? 0.4858 0.7847 0.6112 0.1215  0.1216  -0.0785 108  PHE A O   
287  C CB  . PHE A 88  ? 0.4613 0.7610 0.5622 0.1061  0.1438  -0.0875 108  PHE A CB  
288  C CG  . PHE A 88  ? 0.5102 0.7847 0.5894 0.1015  0.1497  -0.0878 108  PHE A CG  
289  C CD1 . PHE A 88  ? 0.6775 0.9210 0.7444 0.1116  0.1481  -0.0896 108  PHE A CD1 
290  C CD2 . PHE A 88  ? 0.5650 0.8464 0.6343 0.0866  0.1563  -0.0867 108  PHE A CD2 
291  C CE1 . PHE A 88  ? 0.7414 0.9620 0.7876 0.1066  0.1536  -0.0911 108  PHE A CE1 
292  C CE2 . PHE A 88  ? 0.6960 0.9552 0.7436 0.0825  0.1607  -0.0875 108  PHE A CE2 
293  C CZ  . PHE A 88  ? 0.7076 0.9367 0.7442 0.0924  0.1596  -0.0900 108  PHE A CZ  
294  N N   . VAL A 89  ? 0.4540 0.7959 0.5953 0.0986  0.1268  -0.0769 109  VAL A N   
295  C CA  . VAL A 89  ? 0.3982 0.7561 0.5554 0.1069  0.1189  -0.0783 109  VAL A CA  
296  C C   . VAL A 89  ? 0.2795 0.6171 0.4353 0.1036  0.1095  -0.0680 109  VAL A C   
297  O O   . VAL A 89  ? 0.2501 0.5832 0.4086 0.1175  0.1021  -0.0690 109  VAL A O   
298  C CB  . VAL A 89  ? 0.4568 0.8495 0.6288 0.0964  0.1212  -0.0809 109  VAL A CB  
299  C CG1 . VAL A 89  ? 0.2636 0.6747 0.4508 0.1031  0.1118  -0.0824 109  VAL A CG1 
300  C CG2 . VAL A 89  ? 0.4850 0.9011 0.6598 0.1019  0.1308  -0.0932 109  VAL A CG2 
301  N N   . LEU A 90  ? 0.3389 0.6636 0.4894 0.0857  0.1094  -0.0582 110  LEU A N   
302  C CA  . LEU A 90  ? 0.3451 0.6500 0.4942 0.0818  0.1014  -0.0492 110  LEU A CA  
303  C C   . LEU A 90  ? 0.3212 0.5992 0.4583 0.0933  0.1001  -0.0494 110  LEU A C   
304  O O   . LEU A 90  ? 0.3947 0.6619 0.5317 0.0997  0.0930  -0.0464 110  LEU A O   
305  C CB  . LEU A 90  ? 0.3187 0.6165 0.4641 0.0617  0.1013  -0.0403 110  LEU A CB  
306  C CG  . LEU A 90  ? 0.2597 0.5844 0.4138 0.0495  0.1009  -0.0400 110  LEU A CG  
307  C CD1 . LEU A 90  ? 0.3117 0.6264 0.4576 0.0315  0.1016  -0.0322 110  LEU A CD1 
308  C CD2 . LEU A 90  ? 0.2180 0.5549 0.3831 0.0515  0.0925  -0.0393 110  LEU A CD2 
309  N N   . VAL A 91  ? 0.3152 0.5815 0.4402 0.0957  0.1072  -0.0532 111  VAL A N   
310  C CA  . VAL A 91  ? 0.3370 0.5768 0.4486 0.1075  0.1069  -0.0551 111  VAL A CA  
311  C C   . VAL A 91  ? 0.3276 0.5686 0.4403 0.1294  0.1021  -0.0614 111  VAL A C   
312  O O   . VAL A 91  ? 0.3787 0.5991 0.4828 0.1394  0.0965  -0.0591 111  VAL A O   
313  C CB  . VAL A 91  ? 0.4028 0.6304 0.5000 0.1061  0.1161  -0.0600 111  VAL A CB  
314  C CG1 . VAL A 91  ? 0.4818 0.6803 0.5632 0.1198  0.1161  -0.0640 111  VAL A CG1 
315  C CG2 . VAL A 91  ? 0.5051 0.7290 0.5984 0.0857  0.1187  -0.0525 111  VAL A CG2 
316  N N   . GLY A 92  ? 0.3318 0.5968 0.4537 0.1380  0.1037  -0.0694 112  GLY A N   
317  C CA  . GLY A 92  ? 0.3761 0.6445 0.4999 0.1602  0.0974  -0.0757 112  GLY A CA  
318  C C   . GLY A 92  ? 0.3305 0.6004 0.4598 0.1625  0.0868  -0.0695 112  GLY A C   
319  O O   . GLY A 92  ? 0.3613 0.6155 0.4813 0.1799  0.0797  -0.0700 112  GLY A O   
320  N N   . SER A 93  ? 0.2884 0.5746 0.4301 0.1453  0.0853  -0.0634 113  SER A N   
321  C CA  . SER A 93  ? 0.2461 0.5329 0.3920 0.1456  0.0759  -0.0578 113  SER A CA  
322  C C   . SER A 93  ? 0.3864 0.6404 0.5164 0.1477  0.0725  -0.0508 113  SER A C   
323  O O   . SER A 93  ? 0.4001 0.6460 0.5243 0.1601  0.0646  -0.0491 113  SER A O   
324  C CB  . SER A 93  ? 0.2606 0.5643 0.4196 0.1251  0.0760  -0.0527 113  SER A CB  
325  O OG  . SER A 93  ? 0.2612 0.5608 0.4216 0.1235  0.0677  -0.0470 113  SER A OG  
326  N N   . LEU A 94  ? 0.4075 0.6431 0.5293 0.1358  0.0785  -0.0468 114  LEU A N   
327  C CA  . LEU A 94  ? 0.3954 0.6008 0.5015 0.1378  0.0769  -0.0415 114  LEU A CA  
328  C C   . LEU A 94  ? 0.4236 0.6077 0.5119 0.1611  0.0749  -0.0455 114  LEU A C   
329  O O   . LEU A 94  ? 0.4551 0.6187 0.5299 0.1704  0.0695  -0.0408 114  LEU A O   
330  C CB  . LEU A 94  ? 0.3508 0.5436 0.4518 0.1220  0.0842  -0.0389 114  LEU A CB  
331  C CG  . LEU A 94  ? 0.2970 0.4588 0.3801 0.1247  0.0852  -0.0355 114  LEU A CG  
332  C CD1 . LEU A 94  ? 0.3356 0.4902 0.4174 0.1247  0.0785  -0.0282 114  LEU A CD1 
333  C CD2 . LEU A 94  ? 0.3083 0.4641 0.3895 0.1077  0.0918  -0.0344 114  LEU A CD2 
334  N N   . ALA A 95  ? 0.3707 0.5563 0.4560 0.1714  0.0792  -0.0540 115  ALA A N   
335  C CA  . ALA A 95  ? 0.5428 0.7038 0.6091 0.1949  0.0760  -0.0584 115  ALA A CA  
336  C C   . ALA A 95  ? 0.4972 0.6650 0.5645 0.2114  0.0651  -0.0582 115  ALA A C   
337  O O   . ALA A 95  ? 0.5341 0.6718 0.5798 0.2267  0.0591  -0.0550 115  ALA A O   
338  C CB  . ALA A 95  ? 0.6743 0.8399 0.7403 0.2027  0.0822  -0.0692 115  ALA A CB  
339  N N   . THR A 96  ? 0.4747 0.6801 0.5644 0.2083  0.0622  -0.0614 116  THR A N   
340  C CA  . THR A 96  ? 0.5355 0.7510 0.6275 0.2224  0.0512  -0.0619 116  THR A CA  
341  C C   . THR A 96  ? 0.5481 0.7471 0.6306 0.2174  0.0458  -0.0516 116  THR A C   
342  O O   . THR A 96  ? 0.6757 0.8596 0.7431 0.2341  0.0369  -0.0498 116  THR A O   
343  C CB  . THR A 96  ? 0.4753 0.7351 0.5938 0.2165  0.0504  -0.0677 116  THR A CB  
344  O OG1 . THR A 96  ? 0.4416 0.7176 0.5683 0.2204  0.0571  -0.0776 116  THR A OG1 
345  C CG2 . THR A 96  ? 0.4187 0.6913 0.5398 0.2329  0.0385  -0.0705 116  THR A CG2 
346  N N   . ALA A 97  ? 0.5033 0.7039 0.5928 0.1950  0.0508  -0.0449 117  ALA A N   
347  C CA  . ALA A 97  ? 0.4795 0.6639 0.5598 0.1898  0.0472  -0.0358 117  ALA A CA  
348  C C   . ALA A 97  ? 0.4508 0.5923 0.5014 0.2014  0.0482  -0.0314 117  ALA A C   
349  O O   . ALA A 97  ? 0.4687 0.5904 0.5013 0.2125  0.0421  -0.0264 117  ALA A O   
350  C CB  . ALA A 97  ? 0.6159 0.8096 0.7102 0.1638  0.0523  -0.0308 117  ALA A CB  
351  N N   . ASP A 98  ? 0.4546 0.5782 0.4967 0.1986  0.0565  -0.0331 118  ASP A N   
352  C CA  . ASP A 98  ? 0.5814 0.6583 0.5914 0.2098  0.0586  -0.0296 118  ASP A CA  
353  C C   . ASP A 98  ? 0.6241 0.6817 0.6144 0.2356  0.0510  -0.0334 118  ASP A C   
354  O O   . ASP A 98  ? 0.7021 0.7161 0.6602 0.2470  0.0491  -0.0281 118  ASP A O   
355  C CB  . ASP A 98  ? 0.6304 0.6933 0.6358 0.2005  0.0691  -0.0324 118  ASP A CB  
356  C CG  . ASP A 98  ? 0.6309 0.6997 0.6460 0.1774  0.0756  -0.0270 118  ASP A CG  
357  O OD1 . ASP A 98  ? 0.5325 0.6143 0.5577 0.1687  0.0721  -0.0210 118  ASP A OD1 
358  O OD2 . ASP A 98  ? 0.5294 0.5899 0.5417 0.1679  0.0837  -0.0294 118  ASP A OD2 
359  N N   . LEU A 99  ? 0.6023 0.6895 0.6096 0.2446  0.0469  -0.0423 119  LEU A N   
360  C CA  . LEU A 99  ? 0.6022 0.6756 0.5937 0.2703  0.0378  -0.0468 119  LEU A CA  
361  C C   . LEU A 99  ? 0.5801 0.6465 0.5598 0.2797  0.0271  -0.0407 119  LEU A C   
362  O O   . LEU A 99  ? 0.7365 0.7627 0.6836 0.2968  0.0211  -0.0374 119  LEU A O   
363  C CB  . LEU A 99  ? 0.5993 0.7125 0.6158 0.2767  0.0365  -0.0586 119  LEU A CB  
364  C CG  . LEU A 99  ? 0.6509 0.7604 0.6580 0.3039  0.0258  -0.0655 119  LEU A CG  
365  C CD1 . LEU A 99  ? 0.6790 0.7365 0.6513 0.3207  0.0250  -0.0655 119  LEU A CD1 
366  C CD2 . LEU A 99  ? 0.6772 0.8326 0.7139 0.3066  0.0269  -0.0777 119  LEU A CD2 
367  N N   . LEU A 100 ? 0.5731 0.6753 0.5762 0.2678  0.0246  -0.0391 120  LEU A N   
368  C CA  . LEU A 100 ? 0.5752 0.6735 0.5679 0.2758  0.0146  -0.0343 120  LEU A CA  
369  C C   . LEU A 100 ? 0.6959 0.7476 0.6557 0.2751  0.0165  -0.0233 120  LEU A C   
370  O O   . LEU A 100 ? 0.8486 0.8777 0.7839 0.2888  0.0081  -0.0191 120  LEU A O   
371  C CB  . LEU A 100 ? 0.3949 0.5371 0.4183 0.2596  0.0132  -0.0348 120  LEU A CB  
372  C CG  . LEU A 100 ? 0.5138 0.6950 0.5584 0.2683  0.0055  -0.0444 120  LEU A CG  
373  C CD1 . LEU A 100 ? 0.5472 0.7502 0.6103 0.2680  0.0114  -0.0539 120  LEU A CD1 
374  C CD2 . LEU A 100 ? 0.6250 0.8389 0.6922 0.2521  0.0036  -0.0433 120  LEU A CD2 
375  N N   . ALA A 101 ? 0.7425 0.7783 0.6996 0.2591  0.0279  -0.0186 121  ALA A N   
376  C CA  . ALA A 101 ? 0.7019 0.6907 0.6264 0.2574  0.0322  -0.0084 121  ALA A CA  
377  C C   . ALA A 101 ? 0.7477 0.6831 0.6300 0.2770  0.0288  -0.0070 121  ALA A C   
378  O O   . ALA A 101 ? 0.6768 0.5747 0.5259 0.2842  0.0254  0.0006  121  ALA A O   
379  C CB  . ALA A 101 ? 0.7919 0.7757 0.7235 0.2367  0.0456  -0.0057 121  ALA A CB  
380  N N   . GLY A 102 ? 0.7365 0.6652 0.6173 0.2852  0.0298  -0.0143 122  GLY A N   
381  C CA  . GLY A 102 ? 0.8653 0.7415 0.7056 0.3035  0.0256  -0.0136 122  GLY A CA  
382  C C   . GLY A 102 ? 0.7783 0.6542 0.6066 0.3255  0.0106  -0.0151 122  GLY A C   
383  O O   . GLY A 102 ? 0.7649 0.5912 0.5515 0.3365  0.0056  -0.0089 122  GLY A O   
384  N N   . LEU A 103 ? 0.6903 0.6200 0.5533 0.3311  0.0034  -0.0236 123  LEU A N   
385  C CA  . LEU A 103 ? 0.7109 0.6455 0.5659 0.3521  -0.0116 -0.0267 123  LEU A CA  
386  C C   . LEU A 103 ? 0.7947 0.7170 0.6324 0.3499  -0.0164 -0.0175 123  LEU A C   
387  O O   . LEU A 103 ? 0.9008 0.7886 0.7040 0.3669  -0.0264 -0.0145 123  LEU A O   
388  C CB  . LEU A 103 ? 0.7720 0.7694 0.6704 0.3547  -0.0161 -0.0384 123  LEU A CB  
389  C CG  . LEU A 103 ? 0.8632 0.8803 0.7827 0.3556  -0.0101 -0.0487 123  LEU A CG  
390  C CD1 . LEU A 103 ? 0.6526 0.7313 0.6129 0.3556  -0.0135 -0.0595 123  LEU A CD1 
391  C CD2 . LEU A 103 ? 0.8434 0.8176 0.7317 0.3782  -0.0148 -0.0522 123  LEU A CD2 
392  N N   . GLY A 104 ? 0.9135 0.8620 0.7732 0.3292  -0.0096 -0.0132 124  GLY A N   
393  C CA  . GLY A 104 ? 0.8222 0.7655 0.6697 0.3271  -0.0142 -0.0061 124  GLY A CA  
394  C C   . GLY A 104 ? 0.8161 0.6927 0.6112 0.3318  -0.0127 0.0045  124  GLY A C   
395  O O   . GLY A 104 ? 0.9284 0.7829 0.6955 0.3450  -0.0228 0.0074  124  GLY A O   
396  N N   . LEU A 105 ? 0.8988 0.7400 0.6778 0.3199  0.0002  0.0099  125  LEU A N   
397  C CA  . LEU A 105 ? 1.0135 0.7874 0.7404 0.3193  0.0042  0.0202  125  LEU A CA  
398  C C   . LEU A 105 ? 1.0841 0.8131 0.7721 0.3400  -0.0049 0.0188  125  LEU A C   
399  O O   . LEU A 105 ? 1.1378 0.8149 0.7795 0.3441  -0.0074 0.0263  125  LEU A O   
400  C CB  . LEU A 105 ? 0.8934 0.6424 0.6152 0.2983  0.0216  0.0252  125  LEU A CB  
401  C CG  . LEU A 105 ? 0.9921 0.7260 0.7135 0.2979  0.0275  0.0200  125  LEU A CG  
402  C CD1 . LEU A 105 ? 1.1217 0.7881 0.7906 0.3079  0.0254  0.0232  125  LEU A CD1 
403  C CD2 . LEU A 105 ? 1.0746 0.8110 0.8114 0.2742  0.0439  0.0217  125  LEU A CD2 
404  N N   . ILE A 106 ? 0.9638 0.7103 0.6684 0.3524  -0.0096 0.0092  126  ILE A N   
405  C CA  . ILE A 106 ? 1.0374 0.7445 0.7077 0.3746  -0.0200 0.0067  126  ILE A CA  
406  C C   . ILE A 106 ? 1.1336 0.8446 0.7915 0.3930  -0.0362 0.0062  126  ILE A C   
407  O O   . ILE A 106 ? 1.1992 0.8565 0.8092 0.4035  -0.0425 0.0119  126  ILE A O   
408  C CB  . ILE A 106 ? 1.0971 0.8295 0.7932 0.3849  -0.0215 -0.0051 126  ILE A CB  
409  C CG1 . ILE A 106 ? 1.1336 0.8332 0.8187 0.3722  -0.0078 -0.0038 126  ILE A CG1 
410  C CG2 . ILE A 106 ? 1.1441 0.8614 0.8208 0.4135  -0.0374 -0.0113 126  ILE A CG2 
411  C CD1 . ILE A 106 ? 1.2040 0.8261 0.8315 0.3773  -0.0077 0.0026  126  ILE A CD1 
412  N N   . LEU A 107 ? 1.0103 0.7842 0.7104 0.3959  -0.0430 -0.0009 127  LEU A N   
413  C CA  . LEU A 107 ? 0.9983 0.7805 0.6901 0.4113  -0.0582 -0.0022 127  LEU A CA  
414  C C   . LEU A 107 ? 1.0861 0.8402 0.7496 0.4010  -0.0560 0.0092  127  LEU A C   
415  O O   . LEU A 107 ? 1.1176 0.8529 0.7541 0.4148  -0.0681 0.0109  127  LEU A O   
416  C CB  . LEU A 107 ? 0.9443 0.8016 0.6898 0.4124  -0.0639 -0.0132 127  LEU A CB  
417  C CG  . LEU A 107 ? 0.7995 0.6885 0.5741 0.4228  -0.0659 -0.0258 127  LEU A CG  
418  C CD1 . LEU A 107 ? 0.8266 0.7838 0.6573 0.4058  -0.0591 -0.0328 127  LEU A CD1 
419  C CD2 . LEU A 107 ? 0.8209 0.7107 0.5856 0.4512  -0.0836 -0.0341 127  LEU A CD2 
420  N N   . HIS A 108 ? 1.1758 0.9260 0.8443 0.3774  -0.0408 0.0165  128  HIS A N   
421  C CA  . HIS A 108 ? 1.1379 0.8592 0.7783 0.3666  -0.0368 0.0271  128  HIS A CA  
422  C C   . HIS A 108 ? 1.1876 0.8315 0.7648 0.3719  -0.0371 0.0352  128  HIS A C   
423  O O   . HIS A 108 ? 1.2981 0.9165 0.8432 0.3785  -0.0448 0.0398  128  HIS A O   
424  C CB  . HIS A 108 ? 1.0652 0.7989 0.7259 0.3407  -0.0196 0.0322  128  HIS A CB  
425  C CG  . HIS A 108 ? 1.0599 0.7629 0.6921 0.3280  -0.0131 0.0426  128  HIS A CG  
426  N ND1 . HIS A 108 ? 1.1230 0.8504 0.7625 0.3294  -0.0204 0.0434  128  HIS A ND1 
427  C CD2 . HIS A 108 ? 1.1010 0.7508 0.6974 0.3120  0.0007  0.0520  128  HIS A CD2 
428  C CE1 . HIS A 108 ? 1.1652 0.8557 0.7739 0.3160  -0.0114 0.0531  128  HIS A CE1 
429  N NE2 . HIS A 108 ? 1.1878 0.8314 0.7706 0.3042  0.0020  0.0584  128  HIS A NE2 
430  N N   . PHE A 109 ? 1.1337 0.7381 0.6911 0.3676  -0.0284 0.0369  129  PHE A N   
431  C CA  . PHE A 109 ? 1.1600 0.6890 0.6563 0.3708  -0.0285 0.0438  129  PHE A CA  
432  C C   . PHE A 109 ? 1.2262 0.7415 0.7004 0.3994  -0.0480 0.0394  129  PHE A C   
433  O O   . PHE A 109 ? 1.2135 0.6826 0.6414 0.4051  -0.0542 0.0455  129  PHE A O   
434  C CB  . PHE A 109 ? 1.2855 0.7796 0.7692 0.3601  -0.0159 0.0446  129  PHE A CB  
435  C CG  . PHE A 109 ? 1.4152 0.8379 0.8415 0.3689  -0.0197 0.0480  129  PHE A CG  
436  C CD1 . PHE A 109 ? 1.3592 0.7210 0.7356 0.3528  -0.0109 0.0579  129  PHE A CD1 
437  C CD2 . PHE A 109 ? 1.3243 0.7412 0.7466 0.3925  -0.0318 0.0407  129  PHE A CD2 
438  C CE1 . PHE A 109 ? 1.4084 0.7032 0.7305 0.3593  -0.0143 0.0610  129  PHE A CE1 
439  C CE2 . PHE A 109 ? 1.3911 0.7403 0.7593 0.4012  -0.0360 0.0439  129  PHE A CE2 
440  C CZ  . PHE A 109 ? 1.2910 0.5783 0.6082 0.3842  -0.0274 0.0543  129  PHE A CZ  
441  N N   . VAL A 110 ? 1.1995 0.7549 0.7066 0.4174  -0.0577 0.0283  130  VAL A N   
442  C CA  . VAL A 110 ? 1.1894 0.7351 0.6792 0.4462  -0.0767 0.0225  130  VAL A CA  
443  C C   . VAL A 110 ? 1.2141 0.7727 0.6980 0.4546  -0.0891 0.0237  130  VAL A C   
444  O O   . VAL A 110 ? 1.2676 0.7936 0.7158 0.4748  -0.1038 0.0237  130  VAL A O   
445  C CB  . VAL A 110 ? 1.1445 0.7424 0.6795 0.4612  -0.0831 0.0087  130  VAL A CB  
446  C CG1 . VAL A 110 ? 1.1776 0.7763 0.7021 0.4918  -0.1038 0.0010  130  VAL A CG1 
447  C CG2 . VAL A 110 ? 1.1966 0.7714 0.7284 0.4564  -0.0728 0.0073  130  VAL A CG2 
448  N N   . PHE A 111 ? 1.2685 0.8732 0.7861 0.4396  -0.0840 0.0244  131  PHE A N   
449  C CA  . PHE A 111 ? 1.3248 0.9453 0.8400 0.4455  -0.0950 0.0250  131  PHE A CA  
450  C C   . PHE A 111 ? 1.3308 0.9125 0.8115 0.4273  -0.0859 0.0375  131  PHE A C   
451  O O   . PHE A 111 ? 1.2776 0.8391 0.7292 0.4355  -0.0960 0.0407  131  PHE A O   
452  C CB  . PHE A 111 ? 1.2507 0.9534 0.8287 0.4424  -0.0976 0.0155  131  PHE A CB  
453  C CG  . PHE A 111 ? 1.2538 0.9982 0.8634 0.4625  -0.1098 0.0017  131  PHE A CG  
454  C CD1 . PHE A 111 ? 1.1587 0.9011 0.7776 0.4671  -0.1057 -0.0034 131  PHE A CD1 
455  C CD2 . PHE A 111 ? 1.2279 1.0136 0.8578 0.4763  -0.1249 -0.0068 131  PHE A CD2 
456  C CE1 . PHE A 111 ? 1.1202 0.9013 0.7680 0.4853  -0.1159 -0.0167 131  PHE A CE1 
457  C CE2 . PHE A 111 ? 1.1136 0.9386 0.7731 0.4939  -0.1351 -0.0204 131  PHE A CE2 
458  C CZ  . PHE A 111 ? 1.0712 0.8940 0.7396 0.4985  -0.1303 -0.0253 131  PHE A CZ  
459  N N   . GLN A 112 ? 1.2913 0.8610 0.7737 0.4028  -0.0670 0.0441  132  GLN A N   
460  C CA  . GLN A 112 ? 1.2843 0.8093 0.7284 0.3845  -0.0566 0.0557  132  GLN A CA  
461  C C   . GLN A 112 ? 1.3357 0.7842 0.7140 0.3915  -0.0604 0.0621  132  GLN A C   
462  O O   . GLN A 112 ? 1.4257 0.8363 0.7664 0.3809  -0.0566 0.0705  132  GLN A O   
463  C CB  . GLN A 112 ? 1.3153 0.8386 0.7726 0.3572  -0.0350 0.0603  132  GLN A CB  
464  C CG  . GLN A 112 ? 1.3496 0.8293 0.7706 0.3348  -0.0216 0.0710  132  GLN A CG  
465  C CD  . GLN A 112 ? 1.3223 0.8129 0.7660 0.3079  -0.0011 0.0738  132  GLN A CD  
466  O OE1 . GLN A 112 ? 1.2951 0.8079 0.7693 0.3056  0.0043  0.0692  132  GLN A OE1 
467  N NE2 . GLN A 112 ? 1.2006 0.6762 0.6301 0.2870  0.0106  0.0807  132  GLN A NE2 
468  N N   . TYR A 113 ? 1.3824 0.8071 0.7456 0.4083  -0.0677 0.0581  133  TYR A N   
469  C CA  . TYR A 113 ? 1.5577 0.9094 0.8581 0.4181  -0.0738 0.0632  133  TYR A CA  
470  C C   . TYR A 113 ? 1.4284 0.7913 0.7290 0.4517  -0.0967 0.0548  133  TYR A C   
471  O O   . TYR A 113 ? 1.4042 0.7874 0.7281 0.4655  -0.1015 0.0463  133  TYR A O   
472  C CB  . TYR A 113 ? 1.5446 0.8484 0.8209 0.4058  -0.0602 0.0663  133  TYR A CB  
473  C CG  . TYR A 113 ? 1.5393 0.8329 0.8172 0.3717  -0.0370 0.0730  133  TYR A CG  
474  C CD1 . TYR A 113 ? 1.4393 0.7890 0.7714 0.3580  -0.0264 0.0696  133  TYR A CD1 
475  C CD2 . TYR A 113 ? 1.5009 0.7290 0.7262 0.3523  -0.0254 0.0821  133  TYR A CD2 
476  C CE1 . TYR A 113 ? 1.3666 0.7077 0.7012 0.3277  -0.0058 0.0749  133  TYR A CE1 
477  C CE2 . TYR A 113 ? 1.4096 0.6319 0.6392 0.3200  -0.0037 0.0865  133  TYR A CE2 
478  C CZ  . TYR A 113 ? 1.4238 0.7026 0.7083 0.3086  0.0056  0.0828  133  TYR A CZ  
479  O OH  . TYR A 113 ? 1.2908 0.5650 0.5810 0.2770  0.0266  0.0862  133  TYR A OH  
480  N N   . LEU A 114 ? 1.5052 0.8544 0.7795 0.4646  -0.1108 0.0567  134  LEU A N   
481  C CA  . LEU A 114 ? 1.5097 0.8640 0.7784 0.4973  -0.1339 0.0489  134  LEU A CA  
482  C C   . LEU A 114 ? 1.6167 1.0546 0.9529 0.5098  -0.1420 0.0350  134  LEU A C   
483  O O   . LEU A 114 ? 1.5050 0.9583 0.8591 0.5261  -0.1482 0.0259  134  LEU A O   
484  C CB  . LEU A 114 ? 1.6103 0.9033 0.8351 0.5117  -0.1389 0.0495  134  LEU A CB  
485  N N   . VAL A 115 ? 1.5766 1.0680 0.9494 0.5004  -0.1411 0.0333  135  VAL A N   
486  C CA  . VAL A 115 ? 1.4902 1.0630 0.9267 0.5081  -0.1479 0.0202  135  VAL A CA  
487  C C   . VAL A 115 ? 1.5264 1.1194 0.9627 0.5292  -0.1687 0.0140  135  VAL A C   
488  O O   . VAL A 115 ? 1.4709 1.0192 0.8607 0.5338  -0.1760 0.0215  135  VAL A O   
489  C CB  . VAL A 115 ? 1.3251 0.9491 0.8080 0.4819  -0.1325 0.0211  135  VAL A CB  
490  N N   . PRO A 116 ? 1.4911 1.1505 0.9776 0.5414  -0.1785 0.0001  136  PRO A N   
491  C CA  . PRO A 116 ? 1.5176 1.2033 1.0094 0.5583  -0.1974 -0.0066 136  PRO A CA  
492  C C   . PRO A 116 ? 1.5369 1.2326 1.0282 0.5415  -0.1942 0.0000  136  PRO A C   
493  O O   . PRO A 116 ? 1.5915 1.2693 1.0546 0.5534  -0.2083 0.0016  136  PRO A O   
494  C CB  . PRO A 116 ? 1.3199 1.0822 0.8744 0.5660  -0.2023 -0.0230 136  PRO A CB  
495  C CG  . PRO A 116 ? 1.2925 1.0774 0.8806 0.5447  -0.1826 -0.0226 136  PRO A CG  
496  C CD  . PRO A 116 ? 1.3376 1.0506 0.8774 0.5394  -0.1725 -0.0105 136  PRO A CD  
497  N N   . SER A 117 ? 1.4918 1.2149 1.0128 0.5148  -0.1767 0.0036  137  SER A N   
498  C CA  . SER A 117 ? 1.5406 1.2754 1.0638 0.4980  -0.1728 0.0093  137  SER A CA  
499  C C   . SER A 117 ? 1.4062 1.1557 0.9537 0.4694  -0.1511 0.0147  137  SER A C   
500  O O   . SER A 117 ? 1.3244 1.0911 0.8988 0.4631  -0.1412 0.0116  137  SER A O   
501  C CB  . SER A 117 ? 1.4714 1.2699 1.0346 0.5052  -0.1862 -0.0022 137  SER A CB  
502  O OG  . SER A 117 ? 1.3924 1.2566 1.0161 0.4994  -0.1817 -0.0137 137  SER A OG  
503  N N   . GLU A 118 ? 1.3944 1.1360 0.9310 0.4525  -0.1443 0.0229  138  GLU A N   
504  C CA  . GLU A 118 ? 1.3442 1.1001 0.9028 0.4261  -0.1249 0.0280  138  GLU A CA  
505  C C   . GLU A 118 ? 1.2642 1.0979 0.8888 0.4169  -0.1232 0.0179  138  GLU A C   
506  O O   . GLU A 118 ? 1.2761 1.1286 0.9281 0.3988  -0.1083 0.0192  138  GLU A O   
507  C CB  . GLU A 118 ? 1.4540 1.1769 0.9790 0.4116  -0.1186 0.0392  138  GLU A CB  
508  C CG  . GLU A 118 ? 1.3981 1.1172 0.9316 0.3854  -0.0973 0.0466  138  GLU A CG  
509  C CD  . GLU A 118 ? 1.2405 1.0272 0.8308 0.3721  -0.0931 0.0408  138  GLU A CD  
510  O OE1 . GLU A 118 ? 1.2648 1.0989 0.8844 0.3799  -0.1060 0.0317  138  GLU A OE1 
511  O OE2 . GLU A 118 ? 1.1316 0.9231 0.7367 0.3530  -0.0769 0.0451  138  GLU A OE2 
512  N N   . THR A 119 ? 1.2211 1.0989 0.8708 0.4275  -0.1378 0.0078  139  THR A N   
513  C CA  . THR A 119 ? 1.0762 1.0257 0.7871 0.4164  -0.1355 -0.0025 139  THR A CA  
514  C C   . THR A 119 ? 1.1784 1.1492 0.9202 0.4135  -0.1274 -0.0079 139  THR A C   
515  O O   . THR A 119 ? 1.1254 1.1369 0.9088 0.3946  -0.1166 -0.0107 139  THR A O   
516  C CB  . THR A 119 ? 1.1170 1.1059 0.8466 0.4300  -0.1531 -0.0137 139  THR A CB  
517  O OG1 . THR A 119 ? 1.1461 1.1230 0.8535 0.4284  -0.1593 -0.0091 139  THR A OG1 
518  C CG2 . THR A 119 ? 0.9463 1.0060 0.7378 0.4175  -0.1498 -0.0253 139  THR A CG2 
519  N N   . VAL A 120 ? 1.1774 1.1197 0.8981 0.4320  -0.1328 -0.0096 140  VAL A N   
520  C CA  . VAL A 120 ? 1.0905 1.0482 0.8361 0.4298  -0.1248 -0.0144 140  VAL A CA  
521  C C   . VAL A 120 ? 1.0600 0.9967 0.8024 0.4085  -0.1058 -0.0047 140  VAL A C   
522  O O   . VAL A 120 ? 1.0091 0.9803 0.7897 0.3942  -0.0954 -0.0083 140  VAL A O   
523  C CB  . VAL A 120 ? 1.2887 1.2134 1.0067 0.4552  -0.1349 -0.0177 140  VAL A CB  
524  C CG1 . VAL A 120 ? 1.3068 1.2492 1.0515 0.4530  -0.1266 -0.0235 140  VAL A CG1 
525  C CG2 . VAL A 120 ? 1.2680 1.2143 0.9894 0.4778  -0.1547 -0.0279 140  VAL A CG2 
526  N N   . SER A 121 ? 1.2835 1.1622 0.9793 0.4054  -0.1008 0.0075  141  SER A N   
527  C CA  . SER A 121 ? 1.2697 1.1277 0.9613 0.3846  -0.0825 0.0166  141  SER A CA  
528  C C   . SER A 121 ? 1.2142 1.1219 0.9490 0.3631  -0.0739 0.0156  141  SER A C   
529  O O   . SER A 121 ? 1.1471 1.0583 0.8972 0.3461  -0.0594 0.0190  141  SER A O   
530  C CB  . SER A 121 ? 1.3168 1.1054 0.9500 0.3824  -0.0782 0.0294  141  SER A CB  
531  O OG  . SER A 121 ? 1.2677 1.0362 0.8970 0.3615  -0.0596 0.0374  141  SER A OG  
532  N N   . LEU A 122 ? 1.1018 1.0465 0.8556 0.3634  -0.0829 0.0108  142  LEU A N   
533  C CA  . LEU A 122 ? 0.9661 0.9599 0.7626 0.3431  -0.0762 0.0084  142  LEU A CA  
534  C C   . LEU A 122 ? 1.0104 1.0566 0.8575 0.3356  -0.0735 -0.0017 142  LEU A C   
535  O O   . LEU A 122 ? 1.0394 1.1180 0.9202 0.3149  -0.0644 -0.0024 142  LEU A O   
536  C CB  . LEU A 122 ? 0.9105 0.9240 0.7087 0.3451  -0.0869 0.0058  142  LEU A CB  
537  C CG  . LEU A 122 ? 1.0032 1.0643 0.8419 0.3243  -0.0818 0.0029  142  LEU A CG  
538  C CD1 . LEU A 122 ? 0.9723 1.0236 0.7902 0.3238  -0.0872 0.0068  142  LEU A CD1 
539  C CD2 . LEU A 122 ? 0.9289 1.0473 0.8145 0.3214  -0.0873 -0.0100 142  LEU A CD2 
540  N N   . LEU A 123 ? 1.0559 1.1101 0.9079 0.3515  -0.0814 -0.0097 143  LEU A N   
541  C CA  . LEU A 123 ? 0.9064 1.0020 0.8002 0.3437  -0.0765 -0.0183 143  LEU A CA  
542  C C   . LEU A 123 ? 0.9451 1.0179 0.8348 0.3360  -0.0632 -0.0133 143  LEU A C   
543  O O   . LEU A 123 ? 0.8692 0.9717 0.7926 0.3182  -0.0534 -0.0158 143  LEU A O   
544  C CB  . LEU A 123 ? 0.9329 1.0469 0.8341 0.3645  -0.0892 -0.0295 143  LEU A CB  
545  C CG  . LEU A 123 ? 1.0577 1.2115 0.9788 0.3690  -0.1013 -0.0383 143  LEU A CG  
546  C CD1 . LEU A 123 ? 1.2655 1.3870 1.1473 0.3901  -0.1158 -0.0359 143  LEU A CD1 
547  C CD2 . LEU A 123 ? 1.0108 1.2074 0.9651 0.3757  -0.1055 -0.0517 143  LEU A CD2 
548  N N   . THR A 124 ? 1.0916 1.1092 0.9384 0.3482  -0.0627 -0.0064 144  THR A N   
549  C CA  . THR A 124 ? 1.1724 1.1651 1.0127 0.3415  -0.0503 -0.0024 144  THR A CA  
550  C C   . THR A 124 ? 1.1973 1.1944 1.0509 0.3169  -0.0358 0.0044  144  THR A C   
551  O O   . THR A 124 ? 1.2525 1.2633 1.1287 0.3040  -0.0256 0.0030  144  THR A O   
552  C CB  . THR A 124 ? 1.3250 1.2508 1.1115 0.3566  -0.0521 0.0044  144  THR A CB  
553  O OG1 . THR A 124 ? 1.2657 1.1543 1.0173 0.3527  -0.0507 0.0148  144  THR A OG1 
554  C CG2 . THR A 124 ? 1.3809 1.3008 1.1536 0.3826  -0.0678 -0.0028 144  THR A CG2 
555  N N   . VAL A 125 ? 0.9538 0.9396 0.7932 0.3107  -0.0349 0.0115  145  VAL A N   
556  C CA  . VAL A 125 ? 0.7792 0.7725 0.6335 0.2887  -0.0218 0.0171  145  VAL A CA  
557  C C   . VAL A 125 ? 0.8379 0.8903 0.7451 0.2721  -0.0195 0.0094  145  VAL A C   
558  O O   . VAL A 125 ? 0.9031 0.9647 0.8296 0.2540  -0.0081 0.0113  145  VAL A O   
559  C CB  . VAL A 125 ? 0.7577 0.7337 0.5897 0.2866  -0.0225 0.0245  145  VAL A CB  
560  C CG1 . VAL A 125 ? 0.7628 0.7867 0.6233 0.2844  -0.0324 0.0179  145  VAL A CG1 
561  C CG2 . VAL A 125 ? 0.6878 0.6489 0.5185 0.2687  -0.0067 0.0328  145  VAL A CG2 
562  N N   . GLY A 126 ? 0.8092 0.8993 0.7386 0.2770  -0.0300 0.0005  146  GLY A N   
563  C CA  . GLY A 126 ? 0.6776 0.8163 0.6520 0.2600  -0.0271 -0.0068 146  GLY A CA  
564  C C   . GLY A 126 ? 0.6978 0.8398 0.6852 0.2563  -0.0198 -0.0100 146  GLY A C   
565  O O   . GLY A 126 ? 0.6713 0.8354 0.6862 0.2363  -0.0116 -0.0112 146  GLY A O   
566  N N   . PHE A 127 ? 0.7712 0.8887 0.7370 0.2757  -0.0231 -0.0116 147  PHE A N   
567  C CA  . PHE A 127 ? 0.7223 0.8388 0.6968 0.2738  -0.0158 -0.0148 147  PHE A CA  
568  C C   . PHE A 127 ? 0.6951 0.7914 0.6660 0.2571  -0.0025 -0.0074 147  PHE A C   
569  O O   . PHE A 127 ? 0.7982 0.9139 0.7934 0.2417  0.0056  -0.0101 147  PHE A O   
570  C CB  . PHE A 127 ? 0.7633 0.8492 0.7098 0.2988  -0.0221 -0.0173 147  PHE A CB  
571  C CG  . PHE A 127 ? 0.7879 0.9061 0.7535 0.3119  -0.0306 -0.0290 147  PHE A CG  
572  C CD1 . PHE A 127 ? 0.8667 1.0314 0.8627 0.3060  -0.0355 -0.0356 147  PHE A CD1 
573  C CD2 . PHE A 127 ? 0.8155 0.9165 0.7682 0.3302  -0.0332 -0.0339 147  PHE A CD2 
574  C CE1 . PHE A 127 ? 0.9118 1.1069 0.9256 0.3182  -0.0423 -0.0470 147  PHE A CE1 
575  C CE2 . PHE A 127 ? 0.8342 0.9665 0.8055 0.3434  -0.0406 -0.0456 147  PHE A CE2 
576  C CZ  . PHE A 127 ? 0.9047 1.0850 0.9070 0.3374  -0.0449 -0.0523 147  PHE A CZ  
577  N N   . LEU A 128 ? 0.8303 0.8863 0.7695 0.2595  0.0004  0.0019  148  LEU A N   
578  C CA  . LEU A 128 ? 0.8166 0.8540 0.7528 0.2436  0.0138  0.0085  148  LEU A CA  
579  C C   . LEU A 128 ? 0.5703 0.6453 0.5413 0.2204  0.0184  0.0082  148  LEU A C   
580  O O   . LEU A 128 ? 0.5014 0.5829 0.4886 0.2039  0.0277  0.0083  148  LEU A O   
581  C CB  . LEU A 128 ? 0.7985 0.7823 0.6911 0.2501  0.0173  0.0185  148  LEU A CB  
582  C CG  . LEU A 128 ? 0.7139 0.6443 0.5633 0.2676  0.0155  0.0208  148  LEU A CG  
583  C CD1 . LEU A 128 ? 0.7182 0.6443 0.5747 0.2661  0.0216  0.0161  148  LEU A CD1 
584  C CD2 . LEU A 128 ? 0.9388 0.8690 0.7743 0.2890  -0.0001 0.0169  148  LEU A CD2 
585  N N   . VAL A 129 ? 0.6567 0.7541 0.6377 0.2183  0.0112  0.0076  149  VAL A N   
586  C CA  . VAL A 129 ? 0.6896 0.8205 0.7029 0.1957  0.0138  0.0062  149  VAL A CA  
587  C C   . VAL A 129 ? 0.6884 0.8503 0.7319 0.1850  0.0142  -0.0014 149  VAL A C   
588  O O   . VAL A 129 ? 0.6252 0.7975 0.6878 0.1648  0.0208  -0.0014 149  VAL A O   
589  C CB  . VAL A 129 ? 0.6613 0.8070 0.6765 0.1971  0.0054  0.0059  149  VAL A CB  
590  C CG1 . VAL A 129 ? 0.5980 0.7758 0.6461 0.1738  0.0067  0.0028  149  VAL A CG1 
591  C CG2 . VAL A 129 ? 0.6684 0.7826 0.6534 0.2043  0.0075  0.0143  149  VAL A CG2 
592  N N   . ALA A 130 ? 0.6088 0.7840 0.6551 0.1989  0.0073  -0.0081 150  ALA A N   
593  C CA  . ALA A 130 ? 0.5493 0.7533 0.6219 0.1904  0.0090  -0.0154 150  ALA A CA  
594  C C   . ALA A 130 ? 0.5022 0.6952 0.5755 0.1845  0.0184  -0.0152 150  ALA A C   
595  O O   . ALA A 130 ? 0.5167 0.7264 0.6102 0.1671  0.0240  -0.0173 150  ALA A O   
596  C CB  . ALA A 130 ? 0.5962 0.8163 0.6704 0.2093  0.0002  -0.0233 150  ALA A CB  
597  N N   . SER A 131 ? 0.4976 0.6589 0.5460 0.1989  0.0204  -0.0128 151  SER A N   
598  C CA  . SER A 131 ? 0.4494 0.5985 0.4966 0.1940  0.0295  -0.0134 151  SER A CA  
599  C C   . SER A 131 ? 0.4784 0.6266 0.5352 0.1709  0.0377  -0.0087 151  SER A C   
600  O O   . SER A 131 ? 0.4587 0.6180 0.5304 0.1575  0.0435  -0.0116 151  SER A O   
601  C CB  . SER A 131 ? 0.5915 0.6988 0.6052 0.2130  0.0304  -0.0109 151  SER A CB  
602  O OG  . SER A 131 ? 0.5865 0.6628 0.5771 0.2127  0.0326  -0.0019 151  SER A OG  
603  N N   . PHE A 132 ? 0.5282 0.6629 0.5756 0.1665  0.0382  -0.0018 152  PHE A N   
604  C CA  . PHE A 132 ? 0.3822 0.5153 0.4386 0.1457  0.0453  0.0019  152  PHE A CA  
605  C C   . PHE A 132 ? 0.3802 0.5424 0.4647 0.1258  0.0434  -0.0017 152  PHE A C   
606  O O   . PHE A 132 ? 0.4032 0.5670 0.4975 0.1102  0.0483  -0.0026 152  PHE A O   
607  C CB  . PHE A 132 ? 0.3999 0.5158 0.4422 0.1461  0.0466  0.0091  152  PHE A CB  
608  C CG  . PHE A 132 ? 0.3531 0.4715 0.4079 0.1245  0.0525  0.0116  152  PHE A CG  
609  C CD1 . PHE A 132 ? 0.3455 0.4461 0.3945 0.1177  0.0622  0.0135  152  PHE A CD1 
610  C CD2 . PHE A 132 ? 0.3004 0.4369 0.3721 0.1108  0.0479  0.0110  152  PHE A CD2 
611  C CE1 . PHE A 132 ? 0.3281 0.4321 0.3893 0.0978  0.0658  0.0143  152  PHE A CE1 
612  C CE2 . PHE A 132 ? 0.2711 0.4067 0.3528 0.0917  0.0513  0.0116  152  PHE A CE2 
613  C CZ  . PHE A 132 ? 0.2893 0.4103 0.3664 0.0853  0.0594  0.0130  152  PHE A CZ  
614  N N   . ALA A 133 ? 0.3500 0.5313 0.4444 0.1266  0.0362  -0.0036 153  ALA A N   
615  C CA  . ALA A 133 ? 0.2535 0.4549 0.3695 0.1092  0.0353  -0.0063 153  ALA A CA  
616  C C   . ALA A 133 ? 0.3063 0.5200 0.4318 0.1077  0.0388  -0.0111 153  ALA A C   
617  O O   . ALA A 133 ? 0.3307 0.5501 0.4658 0.0924  0.0423  -0.0110 153  ALA A O   
618  C CB  . ALA A 133 ? 0.3263 0.5444 0.4489 0.1121  0.0278  -0.0077 153  ALA A CB  
619  N N   . ALA A 134 ? 0.4333 0.6518 0.5537 0.1254  0.0376  -0.0154 154  ALA A N   
620  C CA  . ALA A 134 ? 0.4319 0.6639 0.5609 0.1257  0.0418  -0.0210 154  ALA A CA  
621  C C   . ALA A 134 ? 0.2924 0.5087 0.4155 0.1195  0.0499  -0.0202 154  ALA A C   
622  O O   . ALA A 134 ? 0.3725 0.5996 0.5039 0.1127  0.0549  -0.0235 154  ALA A O   
623  C CB  . ALA A 134 ? 0.5457 0.7856 0.6702 0.1482  0.0377  -0.0272 154  ALA A CB  
624  N N   . SER A 135 ? 0.4354 0.6270 0.5431 0.1220  0.0518  -0.0160 155  SER A N   
625  C CA  . SER A 135 ? 0.4291 0.6062 0.5309 0.1155  0.0595  -0.0159 155  SER A CA  
626  C C   . SER A 135 ? 0.1771 0.3560 0.2890 0.0928  0.0615  -0.0130 155  SER A C   
627  O O   . SER A 135 ? 0.1526 0.3357 0.2696 0.0830  0.0660  -0.0149 155  SER A O   
628  C CB  . SER A 135 ? 0.4263 0.5737 0.5054 0.1273  0.0618  -0.0124 155  SER A CB  
629  O OG  . SER A 135 ? 0.4681 0.6065 0.5432 0.1219  0.0601  -0.0060 155  SER A OG  
630  N N   . VAL A 136 ? 0.2963 0.4708 0.4097 0.0851  0.0577  -0.0086 156  VAL A N   
631  C CA  . VAL A 136 ? 0.2801 0.4522 0.4013 0.0656  0.0578  -0.0070 156  VAL A CA  
632  C C   . VAL A 136 ? 0.2738 0.4656 0.4058 0.0584  0.0563  -0.0071 156  VAL A C   
633  O O   . VAL A 136 ? 0.3023 0.4948 0.4363 0.0476  0.0588  -0.0062 156  VAL A O   
634  C CB  . VAL A 136 ? 0.2973 0.4614 0.4168 0.0611  0.0538  -0.0036 156  VAL A CB  
635  C CG1 . VAL A 136 ? 0.3502 0.5282 0.4754 0.0651  0.0477  -0.0026 156  VAL A CG1 
636  C CG2 . VAL A 136 ? 0.2354 0.3949 0.3578 0.0452  0.0536  -0.0021 156  VAL A CG2 
637  N N   . SER A 137 ? 0.2905 0.4998 0.4283 0.0649  0.0524  -0.0083 157  SER A N   
638  C CA  . SER A 137 ? 0.2711 0.5015 0.4181 0.0575  0.0516  -0.0089 157  SER A CA  
639  C C   . SER A 137 ? 0.3137 0.5516 0.4620 0.0558  0.0578  -0.0118 157  SER A C   
640  O O   . SER A 137 ? 0.3607 0.6023 0.5107 0.0437  0.0597  -0.0099 157  SER A O   
641  C CB  . SER A 137 ? 0.3963 0.6470 0.5499 0.0660  0.0469  -0.0120 157  SER A CB  
642  O OG  . SER A 137 ? 0.4831 0.7557 0.6461 0.0576  0.0469  -0.0137 157  SER A OG  
643  N N   . SER A 138 ? 0.3067 0.5456 0.4527 0.0686  0.0611  -0.0165 158  SER A N   
644  C CA  . SER A 138 ? 0.2457 0.4919 0.3922 0.0679  0.0680  -0.0203 158  SER A CA  
645  C C   . SER A 138 ? 0.2903 0.5177 0.4294 0.0578  0.0728  -0.0174 158  SER A C   
646  O O   . SER A 138 ? 0.2463 0.4804 0.3854 0.0500  0.0774  -0.0176 158  SER A O   
647  C CB  . SER A 138 ? 0.2925 0.5405 0.4371 0.0855  0.0702  -0.0269 158  SER A CB  
648  O OG  . SER A 138 ? 0.5596 0.7841 0.6917 0.0943  0.0705  -0.0264 158  SER A OG  
649  N N   . LEU A 139 ? 0.1812 0.3864 0.3136 0.0575  0.0718  -0.0152 159  LEU A N   
650  C CA  . LEU A 139 ? 0.1715 0.3609 0.2981 0.0475  0.0757  -0.0137 159  LEU A CA  
651  C C   . LEU A 139 ? 0.2285 0.4232 0.3585 0.0331  0.0729  -0.0086 159  LEU A C   
652  O O   . LEU A 139 ? 0.2913 0.4832 0.4179 0.0255  0.0765  -0.0075 159  LEU A O   
653  C CB  . LEU A 139 ? 0.3034 0.4753 0.4224 0.0496  0.0744  -0.0130 159  LEU A CB  
654  C CG  . LEU A 139 ? 0.2934 0.4532 0.4036 0.0449  0.0797  -0.0140 159  LEU A CG  
655  C CD1 . LEU A 139 ? 0.3397 0.5005 0.4419 0.0546  0.0870  -0.0189 159  LEU A CD1 
656  C CD2 . LEU A 139 ? 0.2791 0.4250 0.3808 0.0472  0.0787  -0.0124 159  LEU A CD2 
657  N N   . LEU A 140 ? 0.2579 0.4593 0.3931 0.0297  0.0664  -0.0054 160  LEU A N   
658  C CA  . LEU A 140 ? 0.1858 0.3926 0.3233 0.0175  0.0635  -0.0015 160  LEU A CA  
659  C C   . LEU A 140 ? 0.2191 0.4446 0.3586 0.0147  0.0676  -0.0030 160  LEU A C   
660  O O   . LEU A 140 ? 0.2474 0.4729 0.3835 0.0049  0.0688  -0.0004 160  LEU A O   
661  C CB  . LEU A 140 ? 0.1828 0.3930 0.3250 0.0157  0.0569  0.0006  160  LEU A CB  
662  C CG  . LEU A 140 ? 0.1461 0.3621 0.2907 0.0044  0.0537  0.0038  160  LEU A CG  
663  C CD1 . LEU A 140 ? 0.1989 0.3981 0.3390 -0.0037 0.0514  0.0072  160  LEU A CD1 
664  C CD2 . LEU A 140 ? 0.2027 0.4263 0.3530 0.0050  0.0489  0.0038  160  LEU A CD2 
665  N N   . ALA A 141 ? 0.2640 0.5066 0.4084 0.0235  0.0697  -0.0078 161  ALA A N   
666  C CA  . ALA A 141 ? 0.1860 0.4504 0.3337 0.0205  0.0742  -0.0109 161  ALA A CA  
667  C C   . ALA A 141 ? 0.2303 0.4902 0.3703 0.0179  0.0814  -0.0118 161  ALA A C   
668  O O   . ALA A 141 ? 0.2706 0.5412 0.4088 0.0084  0.0847  -0.0114 161  ALA A O   
669  C CB  . ALA A 141 ? 0.1933 0.4777 0.3490 0.0327  0.0748  -0.0177 161  ALA A CB  
670  N N   . ILE A 142 ? 0.2043 0.4477 0.3383 0.0256  0.0845  -0.0135 162  ILE A N   
671  C CA  . ILE A 142 ? 0.1808 0.4182 0.3059 0.0232  0.0919  -0.0148 162  ILE A CA  
672  C C   . ILE A 142 ? 0.1540 0.3821 0.2730 0.0091  0.0897  -0.0082 162  ILE A C   
673  O O   . ILE A 142 ? 0.1543 0.3862 0.2654 0.0030  0.0944  -0.0082 162  ILE A O   
674  C CB  . ILE A 142 ? 0.2916 0.5137 0.4098 0.0344  0.0956  -0.0188 162  ILE A CB  
675  C CG1 . ILE A 142 ? 0.2628 0.4936 0.3858 0.0504  0.0959  -0.0255 162  ILE A CG1 
676  C CG2 . ILE A 142 ? 0.3859 0.6067 0.4920 0.0328  0.1032  -0.0215 162  ILE A CG2 
677  C CD1 . ILE A 142 ? 0.2426 0.4574 0.3564 0.0633  0.0981  -0.0300 162  ILE A CD1 
678  N N   . THR A 143 ? 0.2193 0.4367 0.3408 0.0042  0.0822  -0.0032 163  THR A N   
679  C CA  . THR A 143 ? 0.2615 0.4696 0.3781 -0.0074 0.0786  0.0023  163  THR A CA  
680  C C   . THR A 143 ? 0.2966 0.5186 0.4119 -0.0179 0.0780  0.0049  163  THR A C   
681  O O   . THR A 143 ? 0.3663 0.5866 0.4729 -0.0262 0.0799  0.0073  163  THR A O   
682  C CB  . THR A 143 ? 0.2123 0.4068 0.3328 -0.0087 0.0709  0.0053  163  THR A CB  
683  O OG1 . THR A 143 ? 0.2263 0.4071 0.3462 -0.0014 0.0728  0.0026  163  THR A OG1 
684  C CG2 . THR A 143 ? 0.2638 0.4501 0.3807 -0.0192 0.0661  0.0102  163  THR A CG2 
685  N N   . VAL A 144 ? 0.2361 0.4716 0.3591 -0.0186 0.0756  0.0043  164  VAL A N   
686  C CA  . VAL A 144 ? 0.2724 0.5208 0.3941 -0.0300 0.0763  0.0064  164  VAL A CA  
687  C C   . VAL A 144 ? 0.2231 0.4858 0.3394 -0.0322 0.0852  0.0027  164  VAL A C   
688  O O   . VAL A 144 ? 0.3071 0.5727 0.4151 -0.0440 0.0874  0.0056  164  VAL A O   
689  C CB  . VAL A 144 ? 0.3275 0.5889 0.4593 -0.0304 0.0730  0.0054  164  VAL A CB  
690  C CG1 . VAL A 144 ? 0.3337 0.5797 0.4686 -0.0288 0.0649  0.0087  164  VAL A CG1 
691  C CG2 . VAL A 144 ? 0.2878 0.5668 0.4280 -0.0193 0.0767  -0.0017 164  VAL A CG2 
692  N N   . ASP A 145 ? 0.2614 0.5325 0.3811 -0.0207 0.0907  -0.0039 165  ASP A N   
693  C CA  . ASP A 145 ? 0.3102 0.5944 0.4244 -0.0214 0.1000  -0.0088 165  ASP A CA  
694  C C   . ASP A 145 ? 0.3179 0.5893 0.4162 -0.0280 0.1023  -0.0058 165  ASP A C   
695  O O   . ASP A 145 ? 0.3905 0.6723 0.4788 -0.0380 0.1073  -0.0063 165  ASP A O   
696  C CB  . ASP A 145 ? 0.3139 0.6058 0.4339 -0.0055 0.1047  -0.0171 165  ASP A CB  
697  C CG  . ASP A 145 ? 0.3816 0.6922 0.4989 -0.0050 0.1147  -0.0242 165  ASP A CG  
698  O OD1 . ASP A 145 ? 0.3221 0.6558 0.4452 -0.0120 0.1171  -0.0268 165  ASP A OD1 
699  O OD2 . ASP A 145 ? 0.5212 0.8277 0.6295 0.0018  0.1201  -0.0289 165  ASP A OD2 
700  N N   . ARG A 146 ? 0.3185 0.5711 0.4131 -0.0238 0.0986  -0.0036 166  ARG A N   
701  C CA  . ARG A 146 ? 0.3295 0.5746 0.4089 -0.0313 0.0990  -0.0014 166  ARG A CA  
702  C C   . ARG A 146 ? 0.3944 0.6372 0.4671 -0.0469 0.0934  0.0062  166  ARG A C   
703  O O   . ARG A 146 ? 0.4508 0.6983 0.5083 -0.0577 0.0961  0.0072  166  ARG A O   
704  C CB  . ARG A 146 ? 0.3134 0.5410 0.3928 -0.0245 0.0960  -0.0009 166  ARG A CB  
705  C CG  . ARG A 146 ? 0.4541 0.6768 0.5180 -0.0311 0.0972  -0.0008 166  ARG A CG  
706  C CD  . ARG A 146 ? 0.4404 0.6700 0.4933 -0.0255 0.1073  -0.0093 166  ARG A CD  
707  N NE  . ARG A 146 ? 0.5396 0.7630 0.5981 -0.0095 0.1114  -0.0152 166  ARG A NE  
708  C CZ  . ARG A 146 ? 0.6121 0.8353 0.6609 -0.0008 0.1198  -0.0238 166  ARG A CZ  
709  N NH1 . ARG A 146 ? 0.5804 0.8101 0.6137 -0.0064 0.1254  -0.0283 166  ARG A NH1 
710  N NH2 . ARG A 146 ? 0.7062 0.9202 0.7586 0.0141  0.1226  -0.0287 166  ARG A NH2 
711  N N   . TYR A 147 ? 0.3451 0.5796 0.4272 -0.0485 0.0854  0.0112  167  TYR A N   
712  C CA  . TYR A 147 ? 0.2668 0.4973 0.3421 -0.0623 0.0794  0.0185  167  TYR A CA  
713  C C   . TYR A 147 ? 0.3522 0.5974 0.4206 -0.0731 0.0847  0.0188  167  TYR A C   
714  O O   . TYR A 147 ? 0.4399 0.6850 0.4914 -0.0865 0.0850  0.0228  167  TYR A O   
715  C CB  . TYR A 147 ? 0.1975 0.4164 0.2848 -0.0600 0.0710  0.0219  167  TYR A CB  
716  C CG  . TYR A 147 ? 0.2816 0.4975 0.3630 -0.0732 0.0653  0.0289  167  TYR A CG  
717  C CD1 . TYR A 147 ? 0.3687 0.5756 0.4389 -0.0821 0.0587  0.0353  167  TYR A CD1 
718  C CD2 . TYR A 147 ? 0.3085 0.5308 0.3952 -0.0776 0.0661  0.0295  167  TYR A CD2 
719  C CE1 . TYR A 147 ? 0.4344 0.6363 0.4971 -0.0947 0.0526  0.0431  167  TYR A CE1 
720  C CE2 . TYR A 147 ? 0.3483 0.5658 0.4279 -0.0905 0.0612  0.0364  167  TYR A CE2 
721  C CZ  . TYR A 147 ? 0.4180 0.6241 0.4848 -0.0989 0.0542  0.0436  167  TYR A CZ  
722  O OH  . TYR A 147 ? 0.4362 0.6346 0.4937 -0.1123 0.0482  0.0517  167  TYR A OH  
723  N N   . LEU A 148 ? 0.2997 0.5580 0.3801 -0.0685 0.0890  0.0143  168  LEU A N   
724  C CA  . LEU A 148 ? 0.3439 0.6186 0.4201 -0.0798 0.0949  0.0136  168  LEU A CA  
725  C C   . LEU A 148 ? 0.3901 0.6753 0.4517 -0.0843 0.1040  0.0095  168  LEU A C   
726  O O   . LEU A 148 ? 0.4870 0.7762 0.5337 -0.0996 0.1072  0.0123  168  LEU A O   
727  C CB  . LEU A 148 ? 0.3252 0.6173 0.4188 -0.0735 0.0974  0.0080  168  LEU A CB  
728  C CG  . LEU A 148 ? 0.1943 0.4817 0.2990 -0.0727 0.0888  0.0109  168  LEU A CG  
729  C CD1 . LEU A 148 ? 0.3489 0.6583 0.4691 -0.0660 0.0906  0.0039  168  LEU A CD1 
730  C CD2 . LEU A 148 ? 0.2310 0.5110 0.3281 -0.0885 0.0854  0.0183  168  LEU A CD2 
731  N N   . SER A 149 ? 0.3321 0.6204 0.3958 -0.0717 0.1085  0.0028  169  SER A N   
732  C CA  . SER A 149 ? 0.4644 0.7616 0.5136 -0.0746 0.1177  -0.0025 169  SER A CA  
733  C C   . SER A 149 ? 0.5853 0.8689 0.6115 -0.0878 0.1147  0.0036  169  SER A C   
734  O O   . SER A 149 ? 0.6201 0.9093 0.6286 -0.1002 0.1204  0.0034  169  SER A O   
735  C CB  . SER A 149 ? 0.4816 0.7803 0.5362 -0.0573 0.1222  -0.0109 169  SER A CB  
736  O OG  . SER A 149 ? 0.4521 0.7312 0.5057 -0.0510 0.1157  -0.0078 169  SER A OG  
737  N N   . LEU A 150 ? 0.5924 0.8583 0.6176 -0.0859 0.1057  0.0090  170  LEU A N   
738  C CA  . LEU A 150 ? 0.5966 0.8502 0.6002 -0.0984 0.1009  0.0150  170  LEU A CA  
739  C C   . LEU A 150 ? 0.4712 0.7183 0.4654 -0.1147 0.0943  0.0250  170  LEU A C   
740  O O   . LEU A 150 ? 0.4619 0.7019 0.4316 -0.1291 0.0929  0.0300  170  LEU A O   
741  C CB  . LEU A 150 ? 0.6170 0.8571 0.6249 -0.0913 0.0935  0.0164  170  LEU A CB  
742  C CG  . LEU A 150 ? 0.4928 0.7342 0.5046 -0.0771 0.0999  0.0072  170  LEU A CG  
743  C CD1 . LEU A 150 ? 0.4108 0.6391 0.4292 -0.0718 0.0929  0.0088  170  LEU A CD1 
744  C CD2 . LEU A 150 ? 0.4445 0.6901 0.4344 -0.0819 0.1081  0.0014  170  LEU A CD2 
745  N N   . TYR A 151 ? 0.4510 0.6980 0.4615 -0.1130 0.0900  0.0280  171  TYR A N   
746  C CA  . TYR A 151 ? 0.4930 0.7301 0.4940 -0.1277 0.0830  0.0377  171  TYR A CA  
747  C C   . TYR A 151 ? 0.5432 0.7851 0.5230 -0.1444 0.0897  0.0393  171  TYR A C   
748  O O   . TYR A 151 ? 0.5915 0.8186 0.5472 -0.1595 0.0844  0.0480  171  TYR A O   
749  C CB  . TYR A 151 ? 0.4619 0.6999 0.4842 -0.1222 0.0794  0.0382  171  TYR A CB  
750  C CG  . TYR A 151 ? 0.4528 0.6784 0.4662 -0.1363 0.0718  0.0479  171  TYR A CG  
751  C CD1 . TYR A 151 ? 0.5194 0.7277 0.5326 -0.1364 0.0595  0.0553  171  TYR A CD1 
752  C CD2 . TYR A 151 ? 0.4881 0.7188 0.4930 -0.1499 0.0767  0.0497  171  TYR A CD2 
753  C CE1 . TYR A 151 ? 0.5921 0.7864 0.5960 -0.1488 0.0516  0.0646  171  TYR A CE1 
754  C CE2 . TYR A 151 ? 0.4855 0.7011 0.4797 -0.1634 0.0696  0.0590  171  TYR A CE2 
755  C CZ  . TYR A 151 ? 0.4447 0.6410 0.4380 -0.1623 0.0566  0.0667  171  TYR A CZ  
756  O OH  . TYR A 151 ? 0.4411 0.6194 0.4226 -0.1751 0.0483  0.0764  171  TYR A OH  
757  N N   . ASN A 152 ? 0.6463 0.9078 0.6335 -0.1424 0.1011  0.0312  172  ASN A N   
758  C CA  . ASN A 152 ? 0.8578 1.1262 0.8261 -0.1586 0.1095  0.0313  172  ASN A CA  
759  C C   . ASN A 152 ? 0.8207 1.1149 0.8006 -0.1509 0.1227  0.0191  172  ASN A C   
760  O O   . ASN A 152 ? 0.7963 1.1073 0.7937 -0.1494 0.1271  0.0148  172  ASN A O   
761  C CB  . ASN A 152 ? 0.9835 1.2470 0.9494 -0.1726 0.1065  0.0383  172  ASN A CB  
762  C CG  . ASN A 152 ? 0.9519 1.2064 0.8861 -0.1945 0.1097  0.0442  172  ASN A CG  
763  O OD1 . ASN A 152 ? 0.9240 1.1832 0.8411 -0.1990 0.1175  0.0405  172  ASN A OD1 
764  N ND2 . ASN A 152 ? 0.8705 1.1097 0.7948 -0.2084 0.1036  0.0535  172  ASN A ND2 
765  N N   . PRO A 153 ? 0.7611 1.0593 0.7318 -0.1457 0.1289  0.0128  173  PRO A N   
766  C CA  . PRO A 153 ? 0.7876 1.1102 0.7714 -0.1356 0.1407  0.0005  173  PRO A CA  
767  C C   . PRO A 153 ? 0.7870 1.1299 0.7700 -0.1482 0.1508  -0.0031 173  PRO A C   
768  O O   . PRO A 153 ? 0.7917 1.1584 0.7949 -0.1395 0.1577  -0.0125 173  PRO A O   
769  C CB  . PRO A 153 ? 0.9374 1.2554 0.9035 -0.1320 0.1453  -0.0043 173  PRO A CB  
770  C CG  . PRO A 153 ? 0.7348 1.0280 0.6892 -0.1333 0.1337  0.0042  173  PRO A CG  
771  C CD  . PRO A 153 ? 0.7248 1.0058 0.6743 -0.1473 0.1247  0.0159  173  PRO A CD  
772  N N   . LEU A 154 ? 0.7943 1.1284 0.7534 -0.1692 0.1516  0.0039  174  LEU A N   
773  C CA  . LEU A 154 ? 0.7688 1.1220 0.7262 -0.1837 0.1621  0.0004  174  LEU A CA  
774  C C   . LEU A 154 ? 0.7230 1.0889 0.7062 -0.1818 0.1598  -0.0003 174  LEU A C   
775  O O   . LEU A 154 ? 0.7086 1.1023 0.7069 -0.1820 0.1691  -0.0095 174  LEU A O   
776  C CB  . LEU A 154 ? 0.8335 1.1683 0.7565 -0.2076 0.1621  0.0099  174  LEU A CB  
777  C CG  . LEU A 154 ? 0.9118 1.2184 0.8247 -0.2169 0.1486  0.0239  174  LEU A CG  
778  C CD1 . LEU A 154 ? 0.8687 1.1811 0.7858 -0.2314 0.1509  0.0265  174  LEU A CD1 
779  C CD2 . LEU A 154 ? 1.0006 1.2785 0.8755 -0.2301 0.1431  0.0337  174  LEU A CD2 
780  N N   . THR A 155 ? 0.7079 1.0547 0.6964 -0.1798 0.1475  0.0086  175  THR A N   
781  C CA  . THR A 155 ? 0.6695 1.0268 0.6831 -0.1753 0.1444  0.0071  175  THR A CA  
782  C C   . THR A 155 ? 0.6809 1.0531 0.7218 -0.1520 0.1440  -0.0018 175  THR A C   
783  O O   . THR A 155 ? 0.6722 1.0611 0.7345 -0.1473 0.1444  -0.0065 175  THR A O   
784  C CB  . THR A 155 ? 0.6812 1.0124 0.6918 -0.1791 0.1315  0.0186  175  THR A CB  
785  O OG1 . THR A 155 ? 0.6834 0.9998 0.7012 -0.1621 0.1222  0.0206  175  THR A OG1 
786  C CG2 . THR A 155 ? 0.7401 1.0493 0.7186 -0.2004 0.1294  0.0291  175  THR A CG2 
787  N N   . TYR A 156 ? 0.6846 1.0501 0.7232 -0.1381 0.1432  -0.0044 176  TYR A N   
788  C CA  . TYR A 156 ? 0.6590 1.0354 0.7187 -0.1164 0.1435  -0.0128 176  TYR A CA  
789  C C   . TYR A 156 ? 0.6216 1.0288 0.6885 -0.1144 0.1561  -0.0251 176  TYR A C   
790  O O   . TYR A 156 ? 0.5654 0.9783 0.6301 -0.1041 0.1618  -0.0323 176  TYR A O   
791  C CB  . TYR A 156 ? 0.5764 0.9333 0.6283 -0.1046 0.1392  -0.0113 176  TYR A CB  
792  C CG  . TYR A 156 ? 0.4402 0.7994 0.5102 -0.0826 0.1375  -0.0177 176  TYR A CG  
793  C CD1 . TYR A 156 ? 0.4630 0.8098 0.5467 -0.0732 0.1278  -0.0137 176  TYR A CD1 
794  C CD2 . TYR A 156 ? 0.4655 0.8369 0.5364 -0.0715 0.1457  -0.0276 176  TYR A CD2 
795  C CE1 . TYR A 156 ? 0.4441 0.7900 0.5406 -0.0544 0.1262  -0.0187 176  TYR A CE1 
796  C CE2 . TYR A 156 ? 0.5588 0.9292 0.6432 -0.0517 0.1438  -0.0329 176  TYR A CE2 
797  C CZ  . TYR A 156 ? 0.4083 0.7654 0.5046 -0.0439 0.1340  -0.0280 176  TYR A CZ  
798  O OH  . TYR A 156 ? 0.2988 0.6527 0.4056 -0.0254 0.1322  -0.0327 176  TYR A OH  
799  N N   . TYR A 157 ? 0.7923 1.2203 0.8680 -0.1251 0.1606  -0.0279 177  TYR A N   
800  C CA  . TYR A 157 ? 0.9167 1.3777 1.0000 -0.1267 0.1730  -0.0400 177  TYR A CA  
801  C C   . TYR A 157 ? 0.8476 1.3306 0.9571 -0.1062 0.1722  -0.0509 177  TYR A C   
802  O O   . TYR A 157 ? 0.8382 1.3126 0.9600 -0.0941 0.1619  -0.0485 177  TYR A O   
803  C CB  . TYR A 157 ? 0.6744 1.1516 0.7568 -0.1482 0.1785  -0.0399 177  TYR A CB  
804  N N   . SER A 158 ? 0.9859 1.4983 1.1029 -0.1024 0.1830  -0.0637 178  SER A N   
805  C CA  . SER A 158 ? 1.1265 1.6624 1.2671 -0.0824 0.1825  -0.0755 178  SER A CA  
806  C C   . SER A 158 ? 1.0747 1.6336 1.2369 -0.0842 0.1776  -0.0792 178  SER A C   
807  O O   . SER A 158 ? 1.0627 1.6374 1.2443 -0.0664 0.1737  -0.0874 178  SER A O   
808  C CB  . SER A 158 ? 1.1680 1.7312 1.3111 -0.0784 0.1957  -0.0893 178  SER A CB  
809  O OG  . SER A 158 ? 1.1953 1.7376 1.3176 -0.0753 0.2002  -0.0873 178  SER A OG  
810  N N   . ARG A 159 ? 0.8829 1.4430 1.0411 -0.1049 0.1775  -0.0736 179  ARG A N   
811  C CA  . ARG A 159 ? 0.8969 1.4788 1.0744 -0.1084 0.1735  -0.0775 179  ARG A CA  
812  C C   . ARG A 159 ? 0.8123 1.3678 0.9914 -0.1024 0.1593  -0.0673 179  ARG A C   
813  O O   . ARG A 159 ? 0.8768 1.4415 1.0731 -0.0872 0.1522  -0.0718 179  ARG A O   
814  C CB  . ARG A 159 ? 0.8959 1.4938 1.0682 -0.1348 0.1819  -0.0781 179  ARG A CB  
815  C CG  . ARG A 159 ? 0.8689 1.4357 1.0127 -0.1543 0.1837  -0.0648 179  ARG A CG  
816  C CD  . ARG A 159 ? 0.8206 1.4043 0.9582 -0.1807 0.1935  -0.0666 179  ARG A CD  
817  N NE  . ARG A 159 ? 0.8898 1.4462 0.9967 -0.1987 0.1974  -0.0557 179  ARG A NE  
818  C CZ  . ARG A 159 ? 0.8994 1.4234 0.9892 -0.2109 0.1901  -0.0417 179  ARG A CZ  
819  N NH1 . ARG A 159 ? 0.8973 1.4116 0.9979 -0.2077 0.1792  -0.0368 179  ARG A NH1 
820  N NH2 . ARG A 159 ? 0.9056 1.4058 0.9659 -0.2264 0.1937  -0.0326 179  ARG A NH2 
821  N N   . ARG A 160 ? 0.6892 1.2119 0.8498 -0.1137 0.1549  -0.0538 180  ARG A N   
822  C CA  . ARG A 160 ? 0.6097 1.1075 0.7717 -0.1084 0.1422  -0.0447 180  ARG A CA  
823  C C   . ARG A 160 ? 0.5655 1.0484 0.7314 -0.0854 0.1354  -0.0446 180  ARG A C   
824  O O   . ARG A 160 ? 0.5354 1.0164 0.7130 -0.0742 0.1268  -0.0449 180  ARG A O   
825  C CB  . ARG A 160 ? 0.7497 1.2155 0.8909 -0.1239 0.1390  -0.0312 180  ARG A CB  
826  C CG  . ARG A 160 ? 0.8492 1.3224 0.9861 -0.1468 0.1426  -0.0289 180  ARG A CG  
827  C CD  . ARG A 160 ? 0.8066 1.2868 0.9595 -0.1465 0.1355  -0.0297 180  ARG A CD  
828  N NE  . ARG A 160 ? 0.5844 1.0311 0.7305 -0.1451 0.1244  -0.0182 180  ARG A NE  
829  C CZ  . ARG A 160 ? 0.6789 1.1162 0.8232 -0.1580 0.1204  -0.0125 180  ARG A CZ  
830  N NH1 . ARG A 160 ? 0.5231 0.9811 0.6716 -0.1743 0.1264  -0.0168 180  ARG A NH1 
831  N NH2 . ARG A 160 ? 0.6074 1.0140 0.7459 -0.1546 0.1105  -0.0030 180  ARG A NH2 
832  N N   . THR A 161 ? 0.7528 1.2243 0.9077 -0.0788 0.1394  -0.0445 181  THR A N   
833  C CA  . THR A 161 ? 0.7538 1.2075 0.9097 -0.0589 0.1338  -0.0440 181  THR A CA  
834  C C   . THR A 161 ? 0.7179 1.1945 0.8931 -0.0411 0.1329  -0.0548 181  THR A C   
835  O O   . THR A 161 ? 0.7049 1.1742 0.8882 -0.0302 0.1239  -0.0533 181  THR A O   
836  C CB  . THR A 161 ? 0.7078 1.1471 0.8476 -0.0568 0.1399  -0.0432 181  THR A CB  
837  O OG1 . THR A 161 ? 0.9208 1.3870 1.0626 -0.0579 0.1515  -0.0536 181  THR A OG1 
838  C CG2 . THR A 161 ? 0.6370 1.0518 0.7567 -0.0729 0.1387  -0.0320 181  THR A CG2 
839  N N   . LEU A 162 ? 0.5902 1.0952 0.7723 -0.0378 0.1421  -0.0662 182  LEU A N   
840  C CA  . LEU A 162 ? 0.5741 1.1015 0.7743 -0.0189 0.1407  -0.0775 182  LEU A CA  
841  C C   . LEU A 162 ? 0.5030 1.0465 0.7192 -0.0190 0.1331  -0.0792 182  LEU A C   
842  O O   . LEU A 162 ? 0.4011 0.9488 0.6282 -0.0015 0.1263  -0.0835 182  LEU A O   
843  C CB  . LEU A 162 ? 0.5287 1.0888 0.7356 -0.0175 0.1524  -0.0908 182  LEU A CB  
844  C CG  . LEU A 162 ? 0.7695 1.3177 0.9643 -0.0085 0.1597  -0.0935 182  LEU A CG  
845  C CD1 . LEU A 162 ? 0.8144 1.3492 1.0132 0.0164  0.1537  -0.0964 182  LEU A CD1 
846  C CD2 . LEU A 162 ? 0.6879 1.2037 0.8590 -0.0218 0.1613  -0.0815 182  LEU A CD2 
847  N N   . LEU A 163 ? 0.4330 0.9847 0.6495 -0.0386 0.1341  -0.0761 183  LEU A N   
848  C CA  . LEU A 163 ? 0.4184 0.9805 0.6477 -0.0399 0.1265  -0.0766 183  LEU A CA  
849  C C   . LEU A 163 ? 0.4878 1.0168 0.7115 -0.0310 0.1149  -0.0666 183  LEU A C   
850  O O   . LEU A 163 ? 0.5142 1.0480 0.7483 -0.0167 0.1075  -0.0700 183  LEU A O   
851  C CB  . LEU A 163 ? 0.6716 1.2429 0.8990 -0.0643 0.1305  -0.0740 183  LEU A CB  
852  C CG  . LEU A 163 ? 0.7160 1.2904 0.9526 -0.0692 0.1227  -0.0721 183  LEU A CG  
853  C CD1 . LEU A 163 ? 0.5538 1.1606 0.8121 -0.0551 0.1194  -0.0847 183  LEU A CD1 
854  C CD2 . LEU A 163 ? 0.6286 1.2099 0.8612 -0.0946 0.1281  -0.0697 183  LEU A CD2 
855  N N   . GLY A 164 ? 0.5501 1.0458 0.7569 -0.0390 0.1132  -0.0548 184  GLY A N   
856  C CA  . GLY A 164 ? 0.4575 0.9228 0.6593 -0.0322 0.1031  -0.0460 184  GLY A CA  
857  C C   . GLY A 164 ? 0.3747 0.8290 0.5770 -0.0113 0.0995  -0.0479 184  GLY A C   
858  O O   . GLY A 164 ? 0.4044 0.8453 0.6084 -0.0024 0.0912  -0.0449 184  GLY A O   
859  N N   . VAL A 165 ? 0.4655 0.9243 0.6652 -0.0034 0.1062  -0.0532 185  VAL A N   
860  C CA  . VAL A 165 ? 0.4334 0.8787 0.6316 0.0163  0.1037  -0.0551 185  VAL A CA  
861  C C   . VAL A 165 ? 0.4487 0.9111 0.6610 0.0314  0.0975  -0.0620 185  VAL A C   
862  O O   . VAL A 165 ? 0.3775 0.8212 0.5872 0.0434  0.0903  -0.0589 185  VAL A O   
863  C CB  . VAL A 165 ? 0.6211 1.0706 0.8144 0.0217  0.1132  -0.0611 185  VAL A CB  
864  C CG1 . VAL A 165 ? 0.6305 1.0673 0.8230 0.0430  0.1111  -0.0647 185  VAL A CG1 
865  C CG2 . VAL A 165 ? 0.6190 1.0477 0.7956 0.0081  0.1179  -0.0535 185  VAL A CG2 
866  N N   . HIS A 166 ? 0.4824 0.9811 0.7093 0.0307  0.1002  -0.0720 186  HIS A N   
867  C CA  . HIS A 166 ? 0.4491 0.9670 0.6899 0.0455  0.0934  -0.0797 186  HIS A CA  
868  C C   . HIS A 166 ? 0.3904 0.8975 0.6316 0.0419  0.0839  -0.0730 186  HIS A C   
869  O O   . HIS A 166 ? 0.4466 0.9509 0.6907 0.0569  0.0759  -0.0744 186  HIS A O   
870  C CB  . HIS A 166 ? 0.4668 1.0293 0.7249 0.0435  0.0985  -0.0929 186  HIS A CB  
871  C CG  . HIS A 166 ? 0.4452 1.0232 0.7074 0.0570  0.1050  -0.1035 186  HIS A CG  
872  N ND1 . HIS A 166 ? 0.4807 1.0730 0.7532 0.0794  0.1001  -0.1134 186  HIS A ND1 
873  C CD2 . HIS A 166 ? 0.5438 1.1245 0.8005 0.0520  0.1159  -0.1062 186  HIS A CD2 
874  C CE1 . HIS A 166 ? 0.5511 1.1542 0.8252 0.0881  0.1078  -0.1221 186  HIS A CE1 
875  N NE2 . HIS A 166 ? 0.5997 1.1963 0.8641 0.0714  0.1179  -0.1181 186  HIS A NE2 
876  N N   . LEU A 167 ? 0.4229 0.9231 0.6601 0.0227  0.0845  -0.0658 187  LEU A N   
877  C CA  . LEU A 167 ? 0.4489 0.9357 0.6852 0.0191  0.0761  -0.0594 187  LEU A CA  
878  C C   . LEU A 167 ? 0.5138 0.9626 0.7366 0.0264  0.0708  -0.0500 187  LEU A C   
879  O O   . LEU A 167 ? 0.4893 0.9290 0.7123 0.0328  0.0631  -0.0477 187  LEU A O   
880  C CB  . LEU A 167 ? 0.4268 0.9144 0.6618 -0.0028 0.0785  -0.0546 187  LEU A CB  
881  C CG  . LEU A 167 ? 0.5426 1.0675 0.7926 -0.0123 0.0816  -0.0635 187  LEU A CG  
882  C CD1 . LEU A 167 ? 0.6003 1.1511 0.8549 -0.0163 0.0920  -0.0718 187  LEU A CD1 
883  C CD2 . LEU A 167 ? 0.6671 1.1849 0.9145 -0.0318 0.0808  -0.0571 187  LEU A CD2 
884  N N   . LEU A 168 ? 0.4028 0.8299 0.6138 0.0248  0.0752  -0.0451 188  LEU A N   
885  C CA  . LEU A 168 ? 0.3884 0.7817 0.5879 0.0311  0.0711  -0.0376 188  LEU A CA  
886  C C   . LEU A 168 ? 0.3727 0.7642 0.5737 0.0510  0.0668  -0.0417 188  LEU A C   
887  O O   . LEU A 168 ? 0.4756 0.8505 0.6726 0.0561  0.0602  -0.0375 188  LEU A O   
888  C CB  . LEU A 168 ? 0.3505 0.7252 0.5384 0.0264  0.0772  -0.0337 188  LEU A CB  
889  C CG  . LEU A 168 ? 0.3392 0.7060 0.5207 0.0077  0.0792  -0.0271 188  LEU A CG  
890  C CD1 . LEU A 168 ? 0.2483 0.6000 0.4183 0.0051  0.0850  -0.0247 188  LEU A CD1 
891  C CD2 . LEU A 168 ? 0.3455 0.6922 0.5237 0.0018  0.0718  -0.0194 188  LEU A CD2 
892  N N   . LEU A 169 ? 0.2343 0.6421 0.4400 0.0629  0.0705  -0.0501 189  LEU A N   
893  C CA  . LEU A 169 ? 0.2814 0.6877 0.4879 0.0835  0.0656  -0.0545 189  LEU A CA  
894  C C   . LEU A 169 ? 0.4008 0.8250 0.6168 0.0881  0.0574  -0.0577 189  LEU A C   
895  O O   . LEU A 169 ? 0.3880 0.7979 0.5988 0.0989  0.0502  -0.0552 189  LEU A O   
896  C CB  . LEU A 169 ? 0.4508 0.8728 0.6615 0.0961  0.0709  -0.0643 189  LEU A CB  
897  C CG  . LEU A 169 ? 0.4451 0.8510 0.6459 0.0926  0.0798  -0.0628 189  LEU A CG  
898  C CD1 . LEU A 169 ? 0.2610 0.6786 0.4649 0.1094  0.0840  -0.0733 189  LEU A CD1 
899  C CD2 . LEU A 169 ? 0.3726 0.7395 0.5584 0.0917  0.0784  -0.0534 189  LEU A CD2 
900  N N   . ALA A 170 ? 0.4253 0.8811 0.6546 0.0795  0.0587  -0.0635 190  ALA A N   
901  C CA  . ALA A 170 ? 0.4001 0.8756 0.6396 0.0828  0.0512  -0.0678 190  ALA A CA  
902  C C   . ALA A 170 ? 0.3726 0.8254 0.6046 0.0753  0.0454  -0.0584 190  ALA A C   
903  O O   . ALA A 170 ? 0.3870 0.8355 0.6176 0.0860  0.0375  -0.0584 190  ALA A O   
904  C CB  . ALA A 170 ? 0.3470 0.8600 0.6024 0.0713  0.0553  -0.0760 190  ALA A CB  
905  N N   . ALA A 171 ? 0.3665 0.8041 0.5929 0.0575  0.0490  -0.0507 191  ALA A N   
906  C CA  . ALA A 171 ? 0.6226 1.0375 0.8419 0.0508  0.0441  -0.0424 191  ALA A CA  
907  C C   . ALA A 171 ? 0.5455 0.9293 0.7518 0.0612  0.0411  -0.0365 191  ALA A C   
908  O O   . ALA A 171 ? 0.3437 0.7115 0.5449 0.0599  0.0361  -0.0315 191  ALA A O   
909  C CB  . ALA A 171 ? 0.4987 0.9033 0.7145 0.0312  0.0481  -0.0360 191  ALA A CB  
910  N N   . THR A 172 ? 0.4303 0.8055 0.6311 0.0711  0.0446  -0.0376 192  THR A N   
911  C CA  . THR A 172 ? 0.4095 0.7550 0.5975 0.0801  0.0428  -0.0326 192  THR A CA  
912  C C   . THR A 172 ? 0.4053 0.7536 0.5922 0.0988  0.0361  -0.0363 192  THR A C   
913  O O   . THR A 172 ? 0.5570 0.8894 0.7367 0.1018  0.0309  -0.0319 192  THR A O   
914  C CB  . THR A 172 ? 0.3386 0.6714 0.5201 0.0822  0.0498  -0.0324 192  THR A CB  
915  O OG1 . THR A 172 ? 0.2732 0.5958 0.4516 0.0654  0.0544  -0.0272 192  THR A OG1 
916  C CG2 . THR A 172 ? 0.3804 0.6862 0.5499 0.0944  0.0485  -0.0299 192  THR A CG2 
917  N N   . TRP A 173 ? 0.3469 0.7154 0.5402 0.1121  0.0358  -0.0447 193  TRP A N   
918  C CA  . TRP A 173 ? 0.3820 0.7500 0.5717 0.1326  0.0284  -0.0483 193  TRP A CA  
919  C C   . TRP A 173 ? 0.4368 0.8228 0.6335 0.1339  0.0202  -0.0509 193  TRP A C   
920  O O   . TRP A 173 ? 0.4630 0.8385 0.6514 0.1469  0.0127  -0.0498 193  TRP A O   
921  C CB  . TRP A 173 ? 0.3759 0.7599 0.5706 0.1479  0.0299  -0.0577 193  TRP A CB  
922  C CG  . TRP A 173 ? 0.3832 0.7456 0.5686 0.1494  0.0373  -0.0557 193  TRP A CG  
923  C CD1 . TRP A 173 ? 0.4315 0.8005 0.6212 0.1388  0.0465  -0.0572 193  TRP A CD1 
924  C CD2 . TRP A 173 ? 0.4916 0.8209 0.6604 0.1618  0.0365  -0.0521 193  TRP A CD2 
925  N NE1 . TRP A 173 ? 0.4612 0.8042 0.6390 0.1441  0.0514  -0.0554 193  TRP A NE1 
926  C CE2 . TRP A 173 ? 0.4123 0.7307 0.5772 0.1581  0.0454  -0.0525 193  TRP A CE2 
927  C CE3 . TRP A 173 ? 0.5321 0.8415 0.6856 0.1769  0.0286  -0.0494 193  TRP A CE3 
928  C CZ2 . TRP A 173 ? 0.4821 0.7719 0.6287 0.1691  0.0468  -0.0511 193  TRP A CZ2 
929  C CZ3 . TRP A 173 ? 0.4852 0.7645 0.6188 0.1881  0.0300  -0.0470 193  TRP A CZ3 
930  C CH2 . TRP A 173 ? 0.4954 0.7652 0.6264 0.1840  0.0391  -0.0482 193  TRP A CH2 
931  N N   . THR A 174 ? 0.3986 0.8109 0.6094 0.1207  0.0215  -0.0544 194  THR A N   
932  C CA  . THR A 174 ? 0.4021 0.8307 0.6199 0.1201  0.0142  -0.0571 194  THR A CA  
933  C C   . THR A 174 ? 0.4054 0.8074 0.6118 0.1143  0.0109  -0.0480 194  THR A C   
934  O O   . THR A 174 ? 0.4788 0.8844 0.6845 0.1208  0.0031  -0.0492 194  THR A O   
935  C CB  . THR A 174 ? 0.4043 0.8633 0.6386 0.1044  0.0176  -0.0623 194  THR A CB  
936  O OG1 . THR A 174 ? 0.5789 1.0233 0.8096 0.0851  0.0248  -0.0550 194  THR A OG1 
937  C CG2 . THR A 174 ? 0.4582 0.9497 0.7059 0.1114  0.0204  -0.0736 194  THR A CG2 
938  N N   . VAL A 175 ? 0.3962 0.7724 0.5939 0.1026  0.0164  -0.0396 195  VAL A N   
939  C CA  . VAL A 175 ? 0.5441 0.8951 0.7316 0.0975  0.0141  -0.0318 195  VAL A CA  
940  C C   . VAL A 175 ? 0.5896 0.9153 0.7619 0.1117  0.0123  -0.0282 195  VAL A C   
941  O O   . VAL A 175 ? 0.6344 0.9506 0.7991 0.1182  0.0067  -0.0261 195  VAL A O   
942  C CB  . VAL A 175 ? 0.4701 0.8066 0.6564 0.0786  0.0202  -0.0255 195  VAL A CB  
943  C CG1 . VAL A 175 ? 0.2786 0.5898 0.4554 0.0743  0.0183  -0.0188 195  VAL A CG1 
944  C CG2 . VAL A 175 ? 0.3483 0.7065 0.5470 0.0646  0.0215  -0.0284 195  VAL A CG2 
945  N N   . SER A 176 ? 0.4778 0.7917 0.6445 0.1168  0.0174  -0.0276 196  SER A N   
946  C CA  . SER A 176 ? 0.4833 0.7697 0.6340 0.1292  0.0167  -0.0241 196  SER A CA  
947  C C   . SER A 176 ? 0.6116 0.9021 0.7556 0.1495  0.0078  -0.0274 196  SER A C   
948  O O   . SER A 176 ? 0.7259 0.9995 0.8535 0.1578  0.0036  -0.0234 196  SER A O   
949  C CB  . SER A 176 ? 0.5639 0.8409 0.7113 0.1328  0.0234  -0.0252 196  SER A CB  
950  O OG  . SER A 176 ? 0.3767 0.6512 0.5285 0.1152  0.0306  -0.0225 196  SER A OG  
951  N N   . LEU A 177 ? 0.5861 0.9014 0.7403 0.1593  0.0043  -0.0355 197  LEU A N   
952  C CA  . LEU A 177 ? 0.5151 0.8382 0.6625 0.1803  -0.0063 -0.0403 197  LEU A CA  
953  C C   . LEU A 177 ? 0.5133 0.8427 0.6622 0.1754  -0.0126 -0.0389 197  LEU A C   
954  O O   . LEU A 177 ? 0.5291 0.8466 0.6609 0.1898  -0.0203 -0.0374 197  LEU A O   
955  C CB  . LEU A 177 ? 0.5995 0.9527 0.7620 0.1902  -0.0086 -0.0510 197  LEU A CB  
956  C CG  . LEU A 177 ? 0.6421 0.9895 0.8004 0.2015  -0.0043 -0.0545 197  LEU A CG  
957  C CD1 . LEU A 177 ? 0.6685 1.0520 0.8481 0.2032  -0.0029 -0.0654 197  LEU A CD1 
958  C CD2 . LEU A 177 ? 0.5955 0.9194 0.7296 0.2273  -0.0121 -0.0547 197  LEU A CD2 
959  N N   . GLY A 178 ? 0.5376 0.8851 0.7033 0.1566  -0.0098 -0.0396 198  GLY A N   
960  C CA  . GLY A 178 ? 0.4480 0.8016 0.6156 0.1514  -0.0155 -0.0390 198  GLY A CA  
961  C C   . GLY A 178 ? 0.5342 0.8576 0.6841 0.1508  -0.0160 -0.0306 198  GLY A C   
962  O O   . GLY A 178 ? 0.5185 0.8413 0.6583 0.1611  -0.0240 -0.0311 198  GLY A O   
963  N N   . LEU A 179 ? 0.5367 0.8376 0.6809 0.1405  -0.0079 -0.0239 199  LEU A N   
964  C CA  . LEU A 179 ? 0.5306 0.8066 0.6566 0.1419  -0.0073 -0.0171 199  LEU A CA  
965  C C   . LEU A 179 ? 0.5425 0.8041 0.6442 0.1664  -0.0127 -0.0164 199  LEU A C   
966  O O   . LEU A 179 ? 0.5793 0.8288 0.6637 0.1745  -0.0170 -0.0131 199  LEU A O   
967  C CB  . LEU A 179 ? 0.5197 0.7767 0.6457 0.1274  0.0025  -0.0116 199  LEU A CB  
968  C CG  . LEU A 179 ? 0.4690 0.7260 0.6082 0.1049  0.0063  -0.0096 199  LEU A CG  
969  C CD1 . LEU A 179 ? 0.4536 0.7068 0.5888 0.1023  0.0025  -0.0076 199  LEU A CD1 
970  C CD2 . LEU A 179 ? 0.4316 0.7155 0.5867 0.0972  0.0060  -0.0146 199  LEU A CD2 
971  N N   . GLY A 180 ? 0.5028 0.7624 0.6003 0.1794  -0.0126 -0.0193 200  GLY A N   
972  C CA  . GLY A 180 ? 0.5675 0.8070 0.6384 0.2043  -0.0187 -0.0187 200  GLY A CA  
973  C C   . GLY A 180 ? 0.6369 0.8884 0.7025 0.2203  -0.0313 -0.0237 200  GLY A C   
974  O O   . GLY A 180 ? 0.6504 0.8778 0.6874 0.2400  -0.0379 -0.0213 200  GLY A O   
975  N N   . LEU A 181 ? 0.5825 0.8678 0.6726 0.2124  -0.0348 -0.0307 201  LEU A N   
976  C CA  . LEU A 181 ? 0.5900 0.8908 0.6782 0.2266  -0.0472 -0.0368 201  LEU A CA  
977  C C   . LEU A 181 ? 0.5545 0.8549 0.6385 0.2195  -0.0508 -0.0339 201  LEU A C   
978  O O   . LEU A 181 ? 0.6031 0.9047 0.6746 0.2347  -0.0620 -0.0368 201  LEU A O   
979  C CB  . LEU A 181 ? 0.5387 0.8785 0.6558 0.2235  -0.0493 -0.0472 201  LEU A CB  
980  C CG  . LEU A 181 ? 0.5297 0.8765 0.6527 0.2338  -0.0473 -0.0528 201  LEU A CG  
981  C CD1 . LEU A 181 ? 0.5748 0.9633 0.7271 0.2292  -0.0484 -0.0634 201  LEU A CD1 
982  C CD2 . LEU A 181 ? 0.5828 0.9089 0.6798 0.2625  -0.0566 -0.0542 201  LEU A CD2 
983  N N   . LEU A 182 ? 0.6053 0.9026 0.6981 0.1978  -0.0422 -0.0286 202  LEU A N   
984  C CA  . LEU A 182 ? 0.6059 0.9018 0.6942 0.1913  -0.0450 -0.0262 202  LEU A CA  
985  C C   . LEU A 182 ? 0.6396 0.9102 0.6941 0.2110  -0.0518 -0.0220 202  LEU A C   
986  O O   . LEU A 182 ? 0.6755 0.9533 0.7245 0.2161  -0.0605 -0.0246 202  LEU A O   
987  C CB  . LEU A 182 ? 0.6398 0.9278 0.7376 0.1680  -0.0341 -0.0203 202  LEU A CB  
988  C CG  . LEU A 182 ? 0.6992 1.0067 0.8258 0.1462  -0.0291 -0.0234 202  LEU A CG  
989  C CD1 . LEU A 182 ? 0.5907 0.8823 0.7214 0.1265  -0.0198 -0.0172 202  LEU A CD1 
990  C CD2 . LEU A 182 ? 0.7462 1.0784 0.8860 0.1429  -0.0364 -0.0297 202  LEU A CD2 
991  N N   . PRO A 183 ? 0.7013 0.9394 0.7298 0.2227  -0.0484 -0.0154 203  PRO A N   
992  C CA  . PRO A 183 ? 0.8350 1.0419 0.8249 0.2419  -0.0550 -0.0102 203  PRO A CA  
993  C C   . PRO A 183 ? 0.9560 1.1683 0.9350 0.2622  -0.0701 -0.0167 203  PRO A C   
994  O O   . PRO A 183 ? 0.9568 1.1511 0.9084 0.2737  -0.0780 -0.0140 203  PRO A O   
995  C CB  . PRO A 183 ? 0.8407 1.0093 0.8055 0.2500  -0.0476 -0.0027 203  PRO A CB  
996  C CG  . PRO A 183 ? 0.9467 1.1332 0.9387 0.2409  -0.0412 -0.0070 203  PRO A CG  
997  C CD  . PRO A 183 ? 0.8095 1.0328 0.8388 0.2179  -0.0378 -0.0114 203  PRO A CD  
998  N N   . VAL A 184 ? 0.8712 1.1077 0.8700 0.2674  -0.0744 -0.0252 204  VAL A N   
999  C CA  . VAL A 184 ? 0.8653 1.1076 0.8548 0.2891  -0.0893 -0.0323 204  VAL A CA  
1000 C C   . VAL A 184 ? 0.9311 1.2106 0.9439 0.2817  -0.0964 -0.0401 204  VAL A C   
1001 O O   . VAL A 184 ? 0.9601 1.2542 0.9730 0.2971  -0.1092 -0.0479 204  VAL A O   
1002 C CB  . VAL A 184 ? 0.9536 1.2058 0.9534 0.3006  -0.0909 -0.0390 204  VAL A CB  
1003 C CG1 . VAL A 184 ? 0.8526 1.1120 0.8437 0.3249  -0.1074 -0.0473 204  VAL A CG1 
1004 C CG2 . VAL A 184 ? 1.1369 1.3505 1.1135 0.3068  -0.0836 -0.0316 204  VAL A CG2 
1005 N N   . LEU A 185 ? 0.7361 1.0305 0.7684 0.2584  -0.0885 -0.0385 205  LEU A N   
1006 C CA  . LEU A 185 ? 0.7440 1.0687 0.7955 0.2497  -0.0945 -0.0452 205  LEU A CA  
1007 C C   . LEU A 185 ? 0.9297 1.2406 0.9650 0.2443  -0.0955 -0.0400 205  LEU A C   
1008 O O   . LEU A 185 ? 1.1832 1.5167 1.2331 0.2354  -0.0999 -0.0453 205  LEU A O   
1009 C CB  . LEU A 185 ? 0.7050 1.0614 0.7951 0.2260  -0.0858 -0.0496 205  LEU A CB  
1010 C CG  . LEU A 185 ? 0.6979 1.0810 0.8097 0.2304  -0.0872 -0.0583 205  LEU A CG  
1011 C CD1 . LEU A 185 ? 0.7109 1.0777 0.8173 0.2351  -0.0796 -0.0547 205  LEU A CD1 
1012 C CD2 . LEU A 185 ? 0.5627 0.9779 0.7080 0.2082  -0.0820 -0.0636 205  LEU A CD2 
1013 N N   . GLY A 186 ? 0.8673 1.1416 0.8722 0.2496  -0.0913 -0.0303 206  GLY A N   
1014 C CA  . GLY A 186 ? 0.8107 1.0716 0.7974 0.2463  -0.0922 -0.0256 206  GLY A CA  
1015 C C   . GLY A 186 ? 0.7875 1.0281 0.7677 0.2343  -0.0784 -0.0164 206  GLY A C   
1016 O O   . GLY A 186 ? 0.8853 1.1062 0.8412 0.2360  -0.0780 -0.0106 206  GLY A O   
1017 N N   . TRP A 187 ? 0.8555 1.1003 0.8561 0.2222  -0.0672 -0.0149 207  TRP A N   
1018 C CA  . TRP A 187 ? 0.7916 1.0203 0.7908 0.2099  -0.0538 -0.0070 207  TRP A CA  
1019 C C   . TRP A 187 ? 0.7445 0.9305 0.7050 0.2263  -0.0504 0.0025  207  TRP A C   
1020 O O   . TRP A 187 ? 0.8993 1.0723 0.8610 0.2240  -0.0414 0.0062  207  TRP A O   
1021 C CB  . TRP A 187 ? 0.7489 0.9948 0.7821 0.1900  -0.0441 -0.0091 207  TRP A CB  
1022 C CG  . TRP A 187 ? 0.7123 0.9848 0.7760 0.1687  -0.0433 -0.0144 207  TRP A CG  
1023 C CD1 . TRP A 187 ? 0.8089 1.0810 0.8858 0.1488  -0.0351 -0.0121 207  TRP A CD1 
1024 C CD2 . TRP A 187 ? 0.7352 1.0352 0.8182 0.1656  -0.0508 -0.0229 207  TRP A CD2 
1025 N NE1 . TRP A 187 ? 0.7797 1.0723 0.8799 0.1338  -0.0374 -0.0178 207  TRP A NE1 
1026 C CE2 . TRP A 187 ? 0.7338 1.0449 0.8384 0.1434  -0.0464 -0.0243 207  TRP A CE2 
1027 C CE3 . TRP A 187 ? 0.7635 1.0790 0.8475 0.1800  -0.0609 -0.0296 207  TRP A CE3 
1028 C CZ2 . TRP A 187 ? 0.7675 1.1029 0.8926 0.1349  -0.0510 -0.0313 207  TRP A CZ2 
1029 C CZ3 . TRP A 187 ? 0.8769 1.2214 0.9844 0.1712  -0.0653 -0.0375 207  TRP A CZ3 
1030 C CH2 . TRP A 187 ? 0.8851 1.2386 1.0120 0.1486  -0.0600 -0.0379 207  TRP A CH2 
1031 N N   . ASN A 188 ? 0.6179 0.7769 0.5398 0.2419  -0.0576 0.0069  208  ASN A N   
1032 C CA  . ASN A 188 ? 0.6453 0.7513 0.5200 0.2555  -0.0541 0.0178  208  ASN A CA  
1033 C C   . ASN A 188 ? 0.6258 0.7067 0.4683 0.2535  -0.0514 0.0262  208  ASN A C   
1034 O O   . ASN A 188 ? 0.7050 0.8140 0.5650 0.2441  -0.0535 0.0222  208  ASN A O   
1035 C CB  . ASN A 188 ? 0.7309 0.8134 0.5767 0.2769  -0.0661 0.0164  208  ASN A CB  
1036 C CG  . ASN A 188 ? 0.7086 0.7969 0.5411 0.2863  -0.0810 0.0123  208  ASN A CG  
1037 O OD1 . ASN A 188 ? 0.7134 0.7596 0.4990 0.2970  -0.0858 0.0190  208  ASN A OD1 
1038 N ND2 . ASN A 188 ? 0.7629 0.9003 0.6346 0.2803  -0.0878 0.0012  208  ASN A ND2 
1039 N N   . CYS A 189 ? 0.6485 0.6722 0.4398 0.2601  -0.0458 0.0378  209  CYS A N   
1040 C CA  . CYS A 189 ? 0.6384 0.6280 0.3893 0.2515  -0.0381 0.0474  209  CYS A CA  
1041 C C   . CYS A 189 ? 0.7093 0.6543 0.4047 0.2613  -0.0462 0.0515  209  CYS A C   
1042 O O   . CYS A 189 ? 0.7901 0.6945 0.4416 0.2503  -0.0360 0.0596  209  CYS A O   
1043 C CB  . CYS A 189 ? 0.6107 0.5653 0.3521 0.2314  -0.0151 0.0536  209  CYS A CB  
1044 S SG  . CYS A 189 ? 0.6505 0.5342 0.3330 0.2470  -0.0134 0.0654  209  CYS A SG  
1045 N N   . LEU A 190 ? 0.7381 0.6897 0.4350 0.2783  -0.0624 0.0449  210  LEU A N   
1046 C CA  . LEU A 190 ? 0.8002 0.7080 0.4462 0.2892  -0.0713 0.0487  210  LEU A CA  
1047 C C   . LEU A 190 ? 0.7053 0.6279 0.3435 0.2875  -0.0810 0.0451  210  LEU A C   
1048 O O   . LEU A 190 ? 0.7134 0.6152 0.3216 0.2997  -0.0936 0.0449  210  LEU A O   
1049 C CB  . LEU A 190 ? 0.9861 0.8937 0.6350 0.3100  -0.0849 0.0430  210  LEU A CB  
1050 C CG  . LEU A 190 ? 0.8484 0.7377 0.4998 0.3133  -0.0768 0.0452  210  LEU A CG  
1051 C CD1 . LEU A 190 ? 0.8304 0.7241 0.4846 0.3343  -0.0915 0.0378  210  LEU A CD1 
1052 C CD2 . LEU A 190 ? 0.8570 0.6787 0.4568 0.3051  -0.0626 0.0582  210  LEU A CD2 
1053 N N   . ALA A 191 ? 0.8085 0.7658 0.4720 0.2728  -0.0759 0.0419  211  ALA A N   
1054 C CA  . ALA A 191 ? 0.7379 0.7097 0.3940 0.2686  -0.0836 0.0374  211  ALA A CA  
1055 C C   . ALA A 191 ? 0.8304 0.7627 0.4416 0.2512  -0.0678 0.0455  211  ALA A C   
1056 O O   . ALA A 191 ? 0.8873 0.7964 0.4880 0.2380  -0.0488 0.0525  211  ALA A O   
1057 C CB  . ALA A 191 ? 0.7649 0.8038 0.4807 0.2617  -0.0885 0.0253  211  ALA A CB  
1058 N N   . GLU A 192 ? 0.8627 0.7881 0.4479 0.2491  -0.0743 0.0432  212  GLU A N   
1059 C CA  . GLU A 192 ? 0.8912 0.7831 0.4359 0.2293  -0.0572 0.0477  212  GLU A CA  
1060 C C   . GLU A 192 ? 0.9932 0.9192 0.5696 0.2093  -0.0422 0.0410  212  GLU A C   
1061 O O   . GLU A 192 ? 1.0597 0.9615 0.6173 0.1878  -0.0208 0.0424  212  GLU A O   
1062 C CB  . GLU A 192 ? 0.8107 0.6892 0.3215 0.2320  -0.0684 0.0457  212  GLU A CB  
1063 N N   . ARG A 193 ? 1.0271 1.0110 0.6672 0.2095  -0.0500 0.0305  213  ARG A N   
1064 C CA  . ARG A 193 ? 0.9107 0.9296 0.6008 0.1858  -0.0359 0.0210  213  ARG A CA  
1065 C C   . ARG A 193 ? 0.8116 0.8504 0.5500 0.1798  -0.0268 0.0213  213  ARG A C   
1066 O O   . ARG A 193 ? 0.7752 0.8577 0.5673 0.1706  -0.0267 0.0128  213  ARG A O   
1067 C CB  . ARG A 193 ? 0.9300 0.9963 0.6518 0.1868  -0.0513 0.0083  213  ARG A CB  
1068 C CG  . ARG A 193 ? 0.9854 1.0759 0.7433 0.1626  -0.0377 -0.0018 213  ARG A CG  
1069 C CD  . ARG A 193 ? 1.0637 1.1213 0.7803 0.1489  -0.0229 -0.0023 213  ARG A CD  
1070 N NE  . ARG A 193 ? 1.1356 1.2030 0.8356 0.1514  -0.0354 -0.0107 213  ARG A NE  
1071 C CZ  . ARG A 193 ? 0.9652 1.0605 0.6943 0.1381  -0.0335 -0.0236 213  ARG A CZ  
1072 N NH1 . ARG A 193 ? 0.8423 0.9587 0.6189 0.1221  -0.0207 -0.0293 213  ARG A NH1 
1073 N NH2 . ARG A 193 ? 0.9285 1.0289 0.6367 0.1415  -0.0457 -0.0312 213  ARG A NH2 
1074 N N   . ALA A 194 ? 0.7809 0.7849 0.4976 0.1846  -0.0193 0.0314  214  ALA A N   
1075 C CA  . ALA A 194 ? 0.6635 0.6816 0.4196 0.1796  -0.0106 0.0322  214  ALA A CA  
1076 C C   . ALA A 194 ? 0.6818 0.6480 0.4011 0.1741  0.0057  0.0425  214  ALA A C   
1077 O O   . ALA A 194 ? 0.8935 0.8172 0.5624 0.1888  0.0002  0.0513  214  ALA A O   
1078 C CB  . ALA A 194 ? 0.6273 0.6754 0.4102 0.2010  -0.0288 0.0304  214  ALA A CB  
1079 N N   . ALA A 195 ? 0.6445 0.6135 0.3884 0.1531  0.0249  0.0411  215  ALA A N   
1080 C CA  . ALA A 195 ? 0.7173 0.6409 0.4312 0.1432  0.0425  0.0489  215  ALA A CA  
1081 C C   . ALA A 195 ? 0.6695 0.5915 0.3988 0.1531  0.0402  0.0528  215  ALA A C   
1082 O O   . ALA A 195 ? 0.4797 0.4426 0.2604 0.1513  0.0381  0.0471  215  ALA A O   
1083 C CB  . ALA A 195 ? 0.7830 0.7129 0.5167 0.1156  0.0639  0.0435  215  ALA A CB  
1084 N N   . CYS A 196 ? 0.7281 0.6001 0.4102 0.1631  0.0408  0.0624  216  CYS A N   
1085 C CA  . CYS A 196 ? 0.7222 0.5866 0.4124 0.1745  0.0384  0.0656  216  CYS A CA  
1086 C C   . CYS A 196 ? 0.6757 0.5393 0.3894 0.1522  0.0581  0.0643  216  CYS A C   
1087 O O   . CYS A 196 ? 0.6043 0.4578 0.3135 0.1291  0.0752  0.0632  216  CYS A O   
1088 C CB  . CYS A 196 ? 0.7068 0.5122 0.3354 0.1927  0.0321  0.0760  216  CYS A CB  
1089 S SG  . CYS A 196 ? 0.7955 0.6075 0.4038 0.2275  0.0027  0.0765  216  CYS A SG  
1090 N N   . SER A 197 ? 0.6939 0.5708 0.4341 0.1597  0.0553  0.0632  217  SER A N   
1091 C CA  . SER A 197 ? 0.7069 0.5842 0.4698 0.1417  0.0709  0.0617  217  SER A CA  
1092 C C   . SER A 197 ? 0.5502 0.3696 0.2685 0.1438  0.0783  0.0695  217  SER A C   
1093 O O   . SER A 197 ? 0.5989 0.3749 0.2667 0.1583  0.0720  0.0769  217  SER A O   
1094 C CB  . SER A 197 ? 0.6422 0.5686 0.4595 0.1465  0.0642  0.0553  217  SER A CB  
1095 O OG  . SER A 197 ? 0.5810 0.5034 0.3908 0.1714  0.0512  0.0569  217  SER A OG  
1096 N N   . VAL A 198 ? 0.5858 0.4029 0.3217 0.1289  0.0911  0.0677  218  VAL A N   
1097 C CA  . VAL A 198 ? 0.5817 0.3443 0.2784 0.1282  0.0990  0.0739  218  VAL A CA  
1098 C C   . VAL A 198 ? 0.6604 0.4089 0.3434 0.1573  0.0837  0.0766  218  VAL A C   
1099 O O   . VAL A 198 ? 0.8288 0.5216 0.4661 0.1638  0.0856  0.0832  218  VAL A O   
1100 C CB  . VAL A 198 ? 0.5809 0.3505 0.3047 0.1048  0.1152  0.0693  218  VAL A CB  
1101 C CG1 . VAL A 198 ? 0.5581 0.3773 0.3355 0.1109  0.1079  0.0626  218  VAL A CG1 
1102 C CG2 . VAL A 198 ? 0.7184 0.4283 0.3990 0.0998  0.1251  0.0749  218  VAL A CG2 
1103 N N   . VAL A 199 ? 0.6651 0.4621 0.3863 0.1747  0.0689  0.0711  219  VAL A N   
1104 C CA  . VAL A 199 ? 0.6118 0.4052 0.3272 0.2042  0.0538  0.0709  219  VAL A CA  
1105 C C   . VAL A 199 ? 0.6240 0.4402 0.3383 0.2255  0.0350  0.0699  219  VAL A C   
1106 O O   . VAL A 199 ? 0.7208 0.5951 0.4809 0.2297  0.0266  0.0623  219  VAL A O   
1107 C CB  . VAL A 199 ? 0.5815 0.4159 0.3451 0.2055  0.0540  0.0632  219  VAL A CB  
1108 C CG1 . VAL A 199 ? 0.6614 0.4612 0.4135 0.1920  0.0685  0.0645  219  VAL A CG1 
1109 C CG2 . VAL A 199 ? 0.5076 0.4035 0.3259 0.1891  0.0562  0.0564  219  VAL A CG2 
1110 N N   . ARG A 200 ? 0.6509 0.4213 0.3123 0.2379  0.0280  0.0767  220  ARG A N   
1111 C CA  . ARG A 200 ? 0.6449 0.4388 0.3074 0.2533  0.0097  0.0720  220  ARG A CA  
1112 C C   . ARG A 200 ? 0.6460 0.4714 0.3348 0.2724  -0.0053 0.0614  220  ARG A C   
1113 O O   . ARG A 200 ? 0.7304 0.5410 0.4178 0.2762  -0.0026 0.0596  220  ARG A O   
1114 C CB  . ARG A 200 ? 0.6803 0.4202 0.2847 0.2541  0.0076  0.0779  220  ARG A CB  
1115 N N   . PRO A 201 ? 0.6153 0.4846 0.3278 0.2822  -0.0206 0.0534  221  PRO A N   
1116 C CA  . PRO A 201 ? 0.6311 0.5232 0.3483 0.2787  -0.0262 0.0531  221  PRO A CA  
1117 C C   . PRO A 201 ? 0.5751 0.5216 0.3435 0.2641  -0.0204 0.0493  221  PRO A C   
1118 O O   . PRO A 201 ? 0.6009 0.5830 0.3883 0.2622  -0.0283 0.0443  221  PRO A O   
1119 C CB  . PRO A 201 ? 0.6755 0.5905 0.3988 0.2962  -0.0457 0.0438  221  PRO A CB  
1120 C CG  . PRO A 201 ? 0.6828 0.5795 0.3968 0.3103  -0.0499 0.0408  221  PRO A CG  
1121 C CD  . PRO A 201 ? 0.6462 0.5380 0.3741 0.2988  -0.0346 0.0434  221  PRO A CD  
1122 N N   . LEU A 202 ? 0.5464 0.5005 0.3387 0.2527  -0.0070 0.0506  222  LEU A N   
1123 C CA  . LEU A 202 ? 0.5497 0.5550 0.3929 0.2374  -0.0014 0.0458  222  LEU A CA  
1124 C C   . LEU A 202 ? 0.5985 0.5950 0.4336 0.2137  0.0092  0.0479  222  LEU A C   
1125 O O   . LEU A 202 ? 0.5355 0.4858 0.3348 0.2020  0.0218  0.0545  222  LEU A O   
1126 C CB  . LEU A 202 ? 0.6478 0.6615 0.5187 0.2260  0.0112  0.0440  222  LEU A CB  
1127 C CG  . LEU A 202 ? 0.6982 0.7233 0.5815 0.2321  0.0048  0.0369  222  LEU A CG  
1128 C CD1 . LEU A 202 ? 0.6573 0.6702 0.5482 0.2234  0.0180  0.0384  222  LEU A CD1 
1129 C CD2 . LEU A 202 ? 0.7702 0.8518 0.6970 0.2247  -0.0047 0.0257  222  LEU A CD2 
1130 N N   . ALA A 203 ? 0.5920 0.6334 0.4608 0.2057  0.0045  0.0412  223  ALA A N   
1131 C CA  . ALA A 203 ? 0.5007 0.5394 0.3663 0.1851  0.0133  0.0406  223  ALA A CA  
1132 C C   . ALA A 203 ? 0.4757 0.5238 0.3714 0.1603  0.0302  0.0387  223  ALA A C   
1133 O O   . ALA A 203 ? 0.4443 0.5170 0.3745 0.1578  0.0317  0.0360  223  ALA A O   
1134 C CB  . ALA A 203 ? 0.4589 0.5391 0.3469 0.1874  0.0002  0.0333  223  ALA A CB  
1135 N N   . ARG A 204 ? 0.5735 0.6024 0.4550 0.1420  0.0430  0.0395  224  ARG A N   
1136 C CA  . ARG A 204 ? 0.5586 0.5979 0.4693 0.1196  0.0577  0.0363  224  ARG A CA  
1137 C C   . ARG A 204 ? 0.4532 0.5434 0.4161 0.1138  0.0518  0.0288  224  ARG A C   
1138 O O   . ARG A 204 ? 0.4221 0.5274 0.4155 0.1032  0.0578  0.0270  224  ARG A O   
1139 C CB  . ARG A 204 ? 0.5666 0.5834 0.4564 0.1023  0.0715  0.0358  224  ARG A CB  
1140 C CG  . ARG A 204 ? 0.6245 0.5873 0.4623 0.1012  0.0819  0.0435  224  ARG A CG  
1141 C CD  . ARG A 204 ? 0.6602 0.6080 0.4890 0.0778  0.1009  0.0409  224  ARG A CD  
1142 N NE  . ARG A 204 ? 0.6068 0.5714 0.4731 0.0614  0.1120  0.0361  224  ARG A NE  
1143 C CZ  . ARG A 204 ? 0.6217 0.6250 0.5330 0.0511  0.1128  0.0276  224  ARG A CZ  
1144 N NH1 . ARG A 204 ? 0.7921 0.8215 0.7184 0.0537  0.1046  0.0223  224  ARG A NH1 
1145 N NH2 . ARG A 204 ? 0.4760 0.4903 0.4167 0.0383  0.1212  0.0241  224  ARG A NH2 
1146 N N   . SER A 205 ? 0.3664 0.4816 0.3379 0.1201  0.0395  0.0244  225  SER A N   
1147 C CA  . SER A 205 ? 0.4306 0.5903 0.4481 0.1130  0.0338  0.0175  225  SER A CA  
1148 C C   . SER A 205 ? 0.3631 0.5464 0.4080 0.1188  0.0294  0.0175  225  SER A C   
1149 O O   . SER A 205 ? 0.4193 0.6079 0.4899 0.0979  0.0301  0.0142  225  SER A O   
1150 C CB  . SER A 205 ? 0.4834 0.6635 0.5015 0.1196  0.0204  0.0123  225  SER A CB  
1151 O OG  . SER A 205 ? 0.7822 1.0042 0.8427 0.1138  0.0135  0.0059  225  SER A OG  
1152 N N   . HIS A 206 ? 0.3982 0.5767 0.4276 0.1382  0.0215  0.0200  226  HIS A N   
1153 C CA  . HIS A 206 ? 0.3870 0.5733 0.4330 0.1313  0.0155  0.0169  226  HIS A CA  
1154 C C   . HIS A 206 ? 0.3847 0.5537 0.4309 0.1261  0.0261  0.0206  226  HIS A C   
1155 O O   . HIS A 206 ? 0.3791 0.5548 0.4469 0.1097  0.0259  0.0171  226  HIS A O   
1156 C CB  . HIS A 206 ? 0.4024 0.5905 0.4333 0.1512  0.0034  0.0153  226  HIS A CB  
1157 C CG  . HIS A 206 ? 0.5210 0.7253 0.5498 0.1567  -0.0081 0.0107  226  HIS A CG  
1158 N ND1 . HIS A 206 ? 0.5639 0.7590 0.5650 0.1790  -0.0187 0.0112  226  HIS A ND1 
1159 C CD2 . HIS A 206 ? 0.5945 0.8197 0.6430 0.1423  -0.0112 0.0052  226  HIS A CD2 
1160 C CE1 . HIS A 206 ? 0.6295 0.8434 0.6355 0.1779  -0.0279 0.0057  226  HIS A CE1 
1161 N NE2 . HIS A 206 ? 0.6481 0.8811 0.6832 0.1559  -0.0230 0.0019  226  HIS A NE2 
1162 N N   . VAL A 207 ? 0.3488 0.4897 0.3673 0.1402  0.0363  0.0276  227  VAL A N   
1163 C CA  . VAL A 207 ? 0.3892 0.5118 0.4070 0.1334  0.0480  0.0304  227  VAL A CA  
1164 C C   . VAL A 207 ? 0.3449 0.4759 0.3882 0.1063  0.0549  0.0274  227  VAL A C   
1165 O O   . VAL A 207 ? 0.2691 0.3979 0.3251 0.0940  0.0567  0.0257  227  VAL A O   
1166 C CB  . VAL A 207 ? 0.4711 0.5406 0.4426 0.1376  0.0555  0.0368  227  VAL A CB  
1167 C CG1 . VAL A 207 ? 0.5464 0.5984 0.4878 0.1632  0.0441  0.0395  227  VAL A CG1 
1168 C CG2 . VAL A 207 ? 0.4936 0.5432 0.4469 0.1233  0.0634  0.0381  227  VAL A CG2 
1169 N N   . ALA A 208 ? 0.4554 0.5934 0.5043 0.0973  0.0571  0.0254  228  ALA A N   
1170 C CA  . ALA A 208 ? 0.3787 0.5194 0.4501 0.0727  0.0591  0.0201  228  ALA A CA  
1171 C C   . ALA A 208 ? 0.2858 0.4387 0.3812 0.0604  0.0466  0.0134  228  ALA A C   
1172 O O   . ALA A 208 ? 0.1808 0.3266 0.2869 0.0466  0.0469  0.0091  228  ALA A O   
1173 C CB  . ALA A 208 ? 0.4711 0.6151 0.5418 0.0673  0.0631  0.0176  228  ALA A CB  
1174 N N   . LEU A 209 ? 0.4263 0.5938 0.5266 0.0656  0.0366  0.0117  229  LEU A N   
1175 C CA  . LEU A 209 ? 0.4488 0.6202 0.5665 0.0543  0.0295  0.0068  229  LEU A CA  
1176 C C   . LEU A 209 ? 0.3256 0.4928 0.4434 0.0547  0.0306  0.0071  229  LEU A C   
1177 O O   . LEU A 209 ? 0.4034 0.5659 0.5309 0.0433  0.0304  0.0041  229  LEU A O   
1178 C CB  . LEU A 209 ? 0.3977 0.5857 0.5193 0.0593  0.0208  0.0052  229  LEU A CB  
1179 C CG  . LEU A 209 ? 0.4902 0.6856 0.6126 0.0586  0.0182  0.0036  229  LEU A CG  
1180 C CD1 . LEU A 209 ? 0.5319 0.7422 0.6632 0.0576  0.0095  0.0002  229  LEU A CD1 
1181 C CD2 . LEU A 209 ? 0.4173 0.6000 0.5489 0.0444  0.0230  0.0015  229  LEU A CD2 
1182 N N   . LEU A 210 ? 0.2289 0.3975 0.3330 0.0706  0.0319  0.0111  230  LEU A N   
1183 C CA  . LEU A 210 ? 0.2191 0.3831 0.3224 0.0722  0.0342  0.0111  230  LEU A CA  
1184 C C   . LEU A 210 ? 0.2333 0.3827 0.3365 0.0615  0.0417  0.0112  230  LEU A C   
1185 O O   . LEU A 210 ? 0.1855 0.3330 0.2960 0.0530  0.0416  0.0078  230  LEU A O   
1186 C CB  . LEU A 210 ? 0.3516 0.5130 0.4362 0.0943  0.0345  0.0149  230  LEU A CB  
1187 C CG  . LEU A 210 ? 0.2620 0.4391 0.3462 0.1065  0.0248  0.0120  230  LEU A CG  
1188 C CD1 . LEU A 210 ? 0.2553 0.4204 0.3150 0.1308  0.0236  0.0148  230  LEU A CD1 
1189 C CD2 . LEU A 210 ? 0.1561 0.3478 0.2595 0.0970  0.0215  0.0065  230  LEU A CD2 
1190 N N   . SER A 211 ? 0.3008 0.4400 0.3949 0.0617  0.0489  0.0147  231  SER A N   
1191 C CA  . SER A 211 ? 0.2072 0.3342 0.3019 0.0498  0.0556  0.0134  231  SER A CA  
1192 C C   . SER A 211 ? 0.1985 0.3289 0.3080 0.0325  0.0489  0.0042  231  SER A C   
1193 O O   . SER A 211 ? 0.1809 0.3089 0.2922 0.0252  0.0482  0.0013  231  SER A O   
1194 C CB  . SER A 211 ? 0.1907 0.3044 0.2720 0.0516  0.0671  0.0182  231  SER A CB  
1195 O OG  . SER A 211 ? 0.1586 0.2613 0.2404 0.0386  0.0731  0.0161  231  SER A OG  
1196 N N   . ALA A 212 ? 0.3183 0.4530 0.4353 0.0284  0.0445  0.0005  232  ALA A N   
1197 C CA  . ALA A 212 ? 0.2211 0.3591 0.3475 0.0189  0.0401  -0.0022 232  ALA A CA  
1198 C C   . ALA A 212 ? 0.2410 0.3843 0.3727 0.0182  0.0360  -0.0004 232  ALA A C   
1199 O O   . ALA A 212 ? 0.3155 0.4574 0.4489 0.0116  0.0348  -0.0017 232  ALA A O   
1200 C CB  . ALA A 212 ? 0.3347 0.4763 0.4683 0.0175  0.0373  -0.0042 232  ALA A CB  
1201 N N   . ALA A 213 ? 0.2693 0.4207 0.4021 0.0254  0.0340  0.0022  233  ALA A N   
1202 C CA  . ALA A 213 ? 0.2609 0.4204 0.3981 0.0243  0.0318  0.0032  233  ALA A CA  
1203 C C   . ALA A 213 ? 0.2473 0.4015 0.3802 0.0237  0.0356  0.0032  233  ALA A C   
1204 O O   . ALA A 213 ? 0.3298 0.4859 0.4659 0.0181  0.0350  0.0032  233  ALA A O   
1205 C CB  . ALA A 213 ? 0.3230 0.4964 0.4617 0.0329  0.0290  0.0040  233  ALA A CB  
1206 N N   . PHE A 214 ? 0.1488 0.2958 0.2737 0.0297  0.0399  0.0032  234  PHE A N   
1207 C CA  . PHE A 214 ? 0.1113 0.2531 0.2319 0.0293  0.0439  0.0027  234  PHE A CA  
1208 C C   . PHE A 214 ? 0.1254 0.2620 0.2461 0.0185  0.0440  0.0013  234  PHE A C   
1209 O O   . PHE A 214 ? 0.1643 0.3018 0.2859 0.0151  0.0446  0.0008  234  PHE A O   
1210 C CB  . PHE A 214 ? 0.2170 0.3497 0.3268 0.0384  0.0494  0.0035  234  PHE A CB  
1211 C CG  . PHE A 214 ? 0.2344 0.3597 0.3378 0.0375  0.0553  0.0045  234  PHE A CG  
1212 C CD1 . PHE A 214 ? 0.2243 0.3540 0.3307 0.0377  0.0552  0.0020  234  PHE A CD1 
1213 C CD2 . PHE A 214 ? 0.2275 0.3403 0.3223 0.0359  0.0625  0.0083  234  PHE A CD2 
1214 C CE1 . PHE A 214 ? 0.2089 0.3320 0.3091 0.0372  0.0610  0.0027  234  PHE A CE1 
1215 C CE2 . PHE A 214 ? 0.2775 0.3808 0.3668 0.0344  0.0691  0.0097  234  PHE A CE2 
1216 C CZ  . PHE A 214 ? 0.2177 0.3270 0.3094 0.0356  0.0678  0.0069  234  PHE A CZ  
1217 N N   . PHE A 215 ? 0.1216 0.2545 0.2411 0.0137  0.0433  0.0004  235  PHE A N   
1218 C CA  . PHE A 215 ? 0.1497 0.2806 0.2683 0.0055  0.0418  -0.0003 235  PHE A CA  
1219 C C   . PHE A 215 ? 0.1551 0.2902 0.2799 0.0012  0.0372  -0.0005 235  PHE A C   
1220 O O   . PHE A 215 ? 0.1841 0.3181 0.3078 -0.0026 0.0367  0.0000  235  PHE A O   
1221 C CB  . PHE A 215 ? 0.2426 0.3722 0.3596 0.0027  0.0414  -0.0004 235  PHE A CB  
1222 C CG  . PHE A 215 ? 0.1314 0.2539 0.2412 0.0029  0.0476  0.0016  235  PHE A CG  
1223 C CD1 . PHE A 215 ? 0.1547 0.2718 0.2637 -0.0020 0.0493  0.0036  235  PHE A CD1 
1224 C CD2 . PHE A 215 ? 0.1707 0.2898 0.2753 0.0078  0.0528  0.0014  235  PHE A CD2 
1225 C CE1 . PHE A 215 ? 0.1538 0.2611 0.2576 -0.0035 0.0566  0.0049  235  PHE A CE1 
1226 C CE2 . PHE A 215 ? 0.1618 0.2708 0.2574 0.0067  0.0607  0.0036  235  PHE A CE2 
1227 C CZ  . PHE A 215 ? 0.1583 0.2608 0.2539 0.0002  0.0629  0.0051  235  PHE A CZ  
1228 N N   . MET A 216 ? 0.2100 0.3493 0.3411 0.0017  0.0341  -0.0006 236  MET A N   
1229 C CA  . MET A 216 ? 0.2587 0.4014 0.3949 -0.0028 0.0307  0.0004  236  MET A CA  
1230 C C   . MET A 216 ? 0.2176 0.3641 0.3548 -0.0023 0.0328  0.0026  236  MET A C   
1231 O O   . MET A 216 ? 0.2273 0.3736 0.3650 -0.0072 0.0319  0.0037  236  MET A O   
1232 C CB  . MET A 216 ? 0.3749 0.5228 0.5178 -0.0027 0.0278  0.0003  236  MET A CB  
1233 C CG  . MET A 216 ? 0.3722 0.5162 0.5129 -0.0039 0.0254  -0.0023 236  MET A CG  
1234 S SD  . MET A 216 ? 0.5609 0.7102 0.7105 -0.0046 0.0218  -0.0032 236  MET A SD  
1235 C CE  . MET A 216 ? 0.5298 0.6774 0.6726 -0.0080 0.0187  -0.0064 236  MET A CE  
1236 N N   . VAL A 217 ? 0.3537 0.5053 0.4909 0.0041  0.0355  0.0033  237  VAL A N   
1237 C CA  . VAL A 217 ? 0.2320 0.3903 0.3697 0.0054  0.0381  0.0045  237  VAL A CA  
1238 C C   . VAL A 217 ? 0.2124 0.3634 0.3458 0.0030  0.0412  0.0033  237  VAL A C   
1239 O O   . VAL A 217 ? 0.2506 0.4042 0.3848 -0.0009 0.0422  0.0045  237  VAL A O   
1240 C CB  . VAL A 217 ? 0.2691 0.4359 0.4071 0.0150  0.0400  0.0041  237  VAL A CB  
1241 C CG1 . VAL A 217 ? 0.4426 0.6166 0.5807 0.0175  0.0439  0.0035  237  VAL A CG1 
1242 C CG2 . VAL A 217 ? 0.3063 0.4849 0.4499 0.0164  0.0363  0.0047  237  VAL A CG2 
1243 N N   . PHE A 218 ? 0.2144 0.3575 0.3423 0.0046  0.0432  0.0011  238  PHE A N   
1244 C CA  . PHE A 218 ? 0.1948 0.3330 0.3179 0.0012  0.0459  -0.0007 238  PHE A CA  
1245 C C   . PHE A 218 ? 0.2378 0.3731 0.3610 -0.0067 0.0416  0.0000  238  PHE A C   
1246 O O   . PHE A 218 ? 0.2131 0.3465 0.3344 -0.0104 0.0426  -0.0005 238  PHE A O   
1247 C CB  . PHE A 218 ? 0.2121 0.3451 0.3272 0.0041  0.0489  -0.0016 238  PHE A CB  
1248 C CG  . PHE A 218 ? 0.2170 0.3473 0.3251 0.0027  0.0528  -0.0023 238  PHE A CG  
1249 C CD1 . PHE A 218 ? 0.1891 0.3182 0.2950 -0.0045 0.0504  -0.0003 238  PHE A CD1 
1250 C CD2 . PHE A 218 ? 0.3085 0.4382 0.4127 0.0100  0.0587  -0.0043 238  PHE A CD2 
1251 C CE1 . PHE A 218 ? 0.2486 0.3763 0.3492 -0.0058 0.0539  0.0011  238  PHE A CE1 
1252 C CE2 . PHE A 218 ? 0.2243 0.3507 0.3224 0.0102  0.0642  -0.0027 238  PHE A CE2 
1253 C CZ  . PHE A 218 ? 0.1791 0.3056 0.2761 0.0011  0.0618  -0.0003 238  PHE A CZ  
1254 N N   . GLY A 219 ? 0.1418 0.2769 0.2673 -0.0088 0.0371  0.0008  239  GLY A N   
1255 C CA  . GLY A 219 ? 0.1285 0.2623 0.2554 -0.0145 0.0327  0.0017  239  GLY A CA  
1256 C C   . GLY A 219 ? 0.2571 0.3943 0.3892 -0.0178 0.0320  0.0040  239  GLY A C   
1257 O O   . GLY A 219 ? 0.3641 0.4998 0.4968 -0.0222 0.0299  0.0050  239  GLY A O   
1258 N N   . ILE A 220 ? 0.2504 0.3933 0.3850 -0.0159 0.0333  0.0062  240  ILE A N   
1259 C CA  . ILE A 220 ? 0.2276 0.3765 0.3637 -0.0201 0.0330  0.0101  240  ILE A CA  
1260 C C   . ILE A 220 ? 0.1835 0.3346 0.3170 -0.0201 0.0378  0.0106  240  ILE A C   
1261 O O   . ILE A 220 ? 0.1868 0.3395 0.3186 -0.0255 0.0374  0.0135  240  ILE A O   
1262 C CB  . ILE A 220 ? 0.2554 0.4141 0.3952 -0.0194 0.0328  0.0115  240  ILE A CB  
1263 C CG1 . ILE A 220 ? 0.2810 0.4369 0.4239 -0.0204 0.0283  0.0108  240  ILE A CG1 
1264 C CG2 . ILE A 220 ? 0.3078 0.4756 0.4475 -0.0253 0.0339  0.0151  240  ILE A CG2 
1265 C CD1 . ILE A 220 ? 0.1738 0.3396 0.3219 -0.0196 0.0281  0.0109  240  ILE A CD1 
1266 N N   . MET A 221 ? 0.2940 0.4454 0.4264 -0.0140 0.0427  0.0079  241  MET A N   
1267 C CA  . MET A 221 ? 0.3347 0.4878 0.4645 -0.0131 0.0485  0.0075  241  MET A CA  
1268 C C   . MET A 221 ? 0.2936 0.4387 0.4217 -0.0183 0.0483  0.0074  241  MET A C   
1269 O O   . MET A 221 ? 0.2585 0.4062 0.3840 -0.0210 0.0512  0.0094  241  MET A O   
1270 C CB  . MET A 221 ? 0.1920 0.3443 0.3206 -0.0049 0.0536  0.0036  241  MET A CB  
1271 C CG  . MET A 221 ? 0.2102 0.3735 0.3415 0.0016  0.0535  0.0038  241  MET A CG  
1272 S SD  . MET A 221 ? 0.2292 0.3893 0.3584 0.0128  0.0558  0.0001  241  MET A SD  
1273 C CE  . MET A 221 ? 0.2601 0.4151 0.3838 0.0163  0.0640  -0.0041 241  MET A CE  
1274 N N   . LEU A 222 ? 0.2429 0.3796 0.3707 -0.0198 0.0444  0.0048  242  LEU A N   
1275 C CA  . LEU A 222 ? 0.2302 0.3610 0.3574 -0.0246 0.0423  0.0042  242  LEU A CA  
1276 C C   . LEU A 222 ? 0.3173 0.4531 0.4481 -0.0306 0.0378  0.0090  242  LEU A C   
1277 O O   . LEU A 222 ? 0.3630 0.4987 0.4929 -0.0346 0.0377  0.0110  242  LEU A O   
1278 C CB  . LEU A 222 ? 0.2279 0.3551 0.3515 -0.0254 0.0382  -0.0005 242  LEU A CB  
1279 C CG  . LEU A 222 ? 0.2024 0.3322 0.3157 -0.0223 0.0408  -0.0024 242  LEU A CG  
1280 C CD1 . LEU A 222 ? 0.1419 0.2735 0.2541 -0.0224 0.0368  0.0025  242  LEU A CD1 
1281 C CD2 . LEU A 222 ? 0.2754 0.4086 0.3800 -0.0233 0.0441  -0.0025 242  LEU A CD2 
1282 N N   . HIS A 223 ? 0.2568 0.3953 0.3881 -0.0314 0.0331  0.0116  243  HIS A N   
1283 C CA  . HIS A 223 ? 0.2054 0.3461 0.3358 -0.0378 0.0278  0.0169  243  HIS A CA  
1284 C C   . HIS A 223 ? 0.2271 0.3746 0.3516 -0.0418 0.0318  0.0210  243  HIS A C   
1285 O O   . HIS A 223 ? 0.3232 0.4705 0.4437 -0.0484 0.0293  0.0247  243  HIS A O   
1286 C CB  . HIS A 223 ? 0.2101 0.3517 0.3426 -0.0383 0.0236  0.0188  243  HIS A CB  
1287 C CG  . HIS A 223 ? 0.2611 0.4041 0.3917 -0.0460 0.0190  0.0250  243  HIS A CG  
1288 N ND1 . HIS A 223 ? 0.1854 0.3247 0.3144 -0.0513 0.0138  0.0283  243  HIS A ND1 
1289 C CD2 . HIS A 223 ? 0.3570 0.5042 0.4867 -0.0504 0.0186  0.0288  243  HIS A CD2 
1290 C CE1 . HIS A 223 ? 0.2782 0.4173 0.4036 -0.0590 0.0102  0.0346  243  HIS A CE1 
1291 N NE2 . HIS A 223 ? 0.3935 0.5374 0.5193 -0.0590 0.0137  0.0348  243  HIS A NE2 
1292 N N   . LEU A 224 ? 0.3251 0.4798 0.4483 -0.0383 0.0380  0.0201  244  LEU A N   
1293 C CA  . LEU A 224 ? 0.3475 0.5115 0.4645 -0.0419 0.0432  0.0223  244  LEU A CA  
1294 C C   . LEU A 224 ? 0.3318 0.4932 0.4437 -0.0426 0.0470  0.0215  244  LEU A C   
1295 O O   . LEU A 224 ? 0.4057 0.5758 0.5080 -0.0505 0.0477  0.0256  244  LEU A O   
1296 C CB  . LEU A 224 ? 0.3055 0.4804 0.4247 -0.0364 0.0488  0.0195  244  LEU A CB  
1297 C CG  . LEU A 224 ? 0.3498 0.5332 0.4725 -0.0391 0.0467  0.0210  244  LEU A CG  
1298 C CD1 . LEU A 224 ? 0.3231 0.5195 0.4502 -0.0324 0.0514  0.0171  244  LEU A CD1 
1299 C CD2 . LEU A 224 ? 0.3624 0.5511 0.4793 -0.0504 0.0466  0.0256  244  LEU A CD2 
1300 N N   . TYR A 225 ? 0.2644 0.4186 0.3799 -0.0364 0.0492  0.0175  245  TYR A N   
1301 C CA  . TYR A 225 ? 0.3298 0.4869 0.4396 -0.0383 0.0525  0.0178  245  TYR A CA  
1302 C C   . TYR A 225 ? 0.3085 0.4683 0.4146 -0.0486 0.0449  0.0223  245  TYR A C   
1303 O O   . TYR A 225 ? 0.3694 0.5383 0.4645 -0.0559 0.0463  0.0242  245  TYR A O   
1304 C CB  . TYR A 225 ? 0.2430 0.3906 0.3583 -0.0316 0.0561  0.0137  245  TYR A CB  
1305 C CG  . TYR A 225 ? 0.1953 0.3476 0.3039 -0.0343 0.0600  0.0135  245  TYR A CG  
1306 C CD1 . TYR A 225 ? 0.2700 0.4297 0.3684 -0.0306 0.0691  0.0109  245  TYR A CD1 
1307 C CD2 . TYR A 225 ? 0.3258 0.4763 0.4377 -0.0409 0.0545  0.0139  245  TYR A CD2 
1308 C CE1 . TYR A 225 ? 0.3272 0.4904 0.4159 -0.0342 0.0736  0.0073  245  TYR A CE1 
1309 C CE2 . TYR A 225 ? 0.3934 0.5492 0.4974 -0.0463 0.0578  0.0108  245  TYR A CE2 
1310 C CZ  . TYR A 225 ? 0.3583 0.5194 0.4492 -0.0434 0.0681  0.0067  245  TYR A CZ  
1311 O OH  . TYR A 225 ? 0.5259 0.6888 0.6058 -0.0502 0.0730  -0.0004 245  TYR A OH  
1312 N N   . VAL A 226 ? 0.1338 0.2864 0.2478 -0.0499 0.0364  0.0231  246  VAL A N   
1313 C CA  . VAL A 226 ? 0.3964 0.5525 0.5080 -0.0596 0.0267  0.0288  246  VAL A CA  
1314 C C   . VAL A 226 ? 0.3900 0.5543 0.4878 -0.0697 0.0252  0.0370  246  VAL A C   
1315 O O   . VAL A 226 ? 0.3498 0.5203 0.4354 -0.0810 0.0215  0.0425  246  VAL A O   
1316 C CB  . VAL A 226 ? 0.3765 0.5238 0.5000 -0.0569 0.0181  0.0268  246  VAL A CB  
1317 C CG1 . VAL A 226 ? 0.4201 0.5706 0.5424 -0.0664 0.0051  0.0346  246  VAL A CG1 
1318 C CG2 . VAL A 226 ? 0.2861 0.4260 0.4201 -0.0501 0.0209  0.0171  246  VAL A CG2 
1319 N N   . ARG A 227 ? 0.2636 0.4276 0.3617 -0.0677 0.0279  0.0375  247  ARG A N   
1320 C CA  . ARG A 227 ? 0.3416 0.5127 0.4261 -0.0786 0.0285  0.0442  247  ARG A CA  
1321 C C   . ARG A 227 ? 0.2989 0.4801 0.3694 -0.0825 0.0371  0.0426  247  ARG A C   
1322 O O   . ARG A 227 ? 0.3184 0.5034 0.3712 -0.0956 0.0361  0.0485  247  ARG A O   
1323 C CB  . ARG A 227 ? 0.3925 0.5634 0.4825 -0.0753 0.0316  0.0425  247  ARG A CB  
1324 C CG  . ARG A 227 ? 0.4184 0.5799 0.5169 -0.0749 0.0231  0.0448  247  ARG A CG  
1325 C CD  . ARG A 227 ? 0.3483 0.5107 0.4523 -0.0724 0.0268  0.0417  247  ARG A CD  
1326 N NE  . ARG A 227 ? 0.5357 0.7069 0.6296 -0.0832 0.0305  0.0463  247  ARG A NE  
1327 C CZ  . ARG A 227 ? 0.6185 0.7949 0.7170 -0.0836 0.0349  0.0439  247  ARG A CZ  
1328 N NH1 . ARG A 227 ? 0.4750 0.6529 0.5857 -0.0752 0.0343  0.0390  247  ARG A NH1 
1329 N NH2 . ARG A 227 ? 0.5454 0.7303 0.6340 -0.0953 0.0389  0.0475  247  ARG A NH2 
1330 N N   . ILE A 228 ? 0.3076 0.4913 0.3835 -0.0719 0.0457  0.0346  248  ILE A N   
1331 C CA  . ILE A 228 ? 0.2886 0.4816 0.3516 -0.0739 0.0543  0.0313  248  ILE A CA  
1332 C C   . ILE A 228 ? 0.2833 0.4762 0.3332 -0.0844 0.0500  0.0341  248  ILE A C   
1333 O O   . ILE A 228 ? 0.4421 0.6402 0.4718 -0.0952 0.0526  0.0360  248  ILE A O   
1334 C CB  . ILE A 228 ? 0.2156 0.4086 0.2870 -0.0598 0.0626  0.0231  248  ILE A CB  
1335 C CG1 . ILE A 228 ? 0.2810 0.4773 0.3617 -0.0522 0.0664  0.0208  248  ILE A CG1 
1336 C CG2 . ILE A 228 ? 0.2807 0.4812 0.3381 -0.0610 0.0710  0.0184  248  ILE A CG2 
1337 C CD1 . ILE A 228 ? 0.2613 0.4549 0.3504 -0.0386 0.0719  0.0147  248  ILE A CD1 
1338 N N   . CYS A 229 ? 0.3373 0.5239 0.3978 -0.0823 0.0431  0.0339  249  CYS A N   
1339 C CA  . CYS A 229 ? 0.3103 0.4983 0.3613 -0.0941 0.0367  0.0362  249  CYS A CA  
1340 C C   . CYS A 229 ? 0.3776 0.5643 0.4132 -0.1100 0.0266  0.0477  249  CYS A C   
1341 O O   . CYS A 229 ? 0.3929 0.5803 0.4046 -0.1231 0.0260  0.0509  249  CYS A O   
1342 C CB  . CYS A 229 ? 0.2186 0.4006 0.2893 -0.0892 0.0292  0.0330  249  CYS A CB  
1343 S SG  . CYS A 229 ? 0.2772 0.4554 0.3574 -0.0760 0.0410  0.0216  249  CYS A SG  
1344 N N   . GLN A 230 ? 0.3488 0.5292 0.3934 -0.1094 0.0184  0.0541  250  GLN A N   
1345 C CA  . GLN A 230 ? 0.3270 0.5005 0.3541 -0.1252 0.0078  0.0669  250  GLN A CA  
1346 C C   . GLN A 230 ? 0.3630 0.5381 0.3613 -0.1347 0.0175  0.0687  250  GLN A C   
1347 O O   . GLN A 230 ? 0.4322 0.5981 0.4017 -0.1502 0.0116  0.0774  250  GLN A O   
1348 C CB  . GLN A 230 ? 0.3294 0.4951 0.3699 -0.1214 0.0007  0.0715  250  GLN A CB  
1349 C CG  . GLN A 230 ? 0.3071 0.4683 0.3736 -0.1112 -0.0096 0.0685  250  GLN A CG  
1350 C CD  . GLN A 230 ? 0.3395 0.4928 0.4174 -0.1055 -0.0133 0.0702  250  GLN A CD  
1351 O OE1 . GLN A 230 ? 0.4261 0.5782 0.4942 -0.1104 -0.0090 0.0741  250  GLN A OE1 
1352 N NE2 . GLN A 230 ? 0.3593 0.5072 0.4574 -0.0954 -0.0206 0.0656  250  GLN A NE2 
1353 N N   . VAL A 231 ? 0.3610 0.5452 0.3652 -0.1252 0.0313  0.0599  251  VAL A N   
1354 C CA  . VAL A 231 ? 0.4806 0.6692 0.4635 -0.1323 0.0412  0.0583  251  VAL A CA  
1355 C C   . VAL A 231 ? 0.4339 0.6238 0.3950 -0.1377 0.0454  0.0550  251  VAL A C   
1356 O O   . VAL A 231 ? 0.3945 0.5775 0.3257 -0.1511 0.0449  0.0596  251  VAL A O   
1357 C CB  . VAL A 231 ? 0.4145 0.6151 0.4142 -0.1198 0.0535  0.0488  251  VAL A CB  
1358 C CG1 . VAL A 231 ? 0.5790 0.7889 0.5621 -0.1244 0.0652  0.0437  251  VAL A CG1 
1359 C CG2 . VAL A 231 ? 0.5809 0.7789 0.5924 -0.1198 0.0500  0.0525  251  VAL A CG2 
1360 N N   . VAL A 232 ? 0.5168 0.7123 0.4895 -0.1275 0.0495  0.0464  252  VAL A N   
1361 C CA  . VAL A 232 ? 0.5623 0.7581 0.5129 -0.1322 0.0544  0.0412  252  VAL A CA  
1362 C C   . VAL A 232 ? 0.4428 0.6237 0.3700 -0.1463 0.0398  0.0503  252  VAL A C   
1363 O O   . VAL A 232 ? 0.4611 0.6332 0.3552 -0.1548 0.0394  0.0503  252  VAL A O   
1364 C CB  . VAL A 232 ? 0.4570 0.6581 0.4244 -0.1185 0.0616  0.0295  252  VAL A CB  
1365 C CG1 . VAL A 232 ? 0.4713 0.6717 0.4131 -0.1222 0.0690  0.0214  252  VAL A CG1 
1366 C CG2 . VAL A 232 ? 0.3154 0.5228 0.3048 -0.1016 0.0705  0.0230  252  VAL A CG2 
1367 N N   . TRP A 233 ? 0.3880 0.5577 0.3335 -0.1422 0.0229  0.0548  253  TRP A N   
1368 C CA  . TRP A 233 ? 0.4206 0.5681 0.3486 -0.1469 0.0018  0.0604  253  TRP A CA  
1369 C C   . TRP A 233 ? 0.5566 0.6913 0.4500 -0.1616 -0.0024 0.0730  253  TRP A C   
1370 O O   . TRP A 233 ? 0.6773 0.7962 0.5370 -0.1687 -0.0108 0.0752  253  TRP A O   
1371 C CB  . TRP A 233 ? 0.4349 0.5768 0.3924 -0.1392 -0.0145 0.0624  253  TRP A CB  
1372 C CG  . TRP A 233 ? 0.3628 0.5142 0.3513 -0.1273 -0.0112 0.0506  253  TRP A CG  
1373 C CD1 . TRP A 233 ? 0.3521 0.5070 0.3386 -0.1235 -0.0022 0.0390  253  TRP A CD1 
1374 C CD2 . TRP A 233 ? 0.3635 0.5195 0.3869 -0.1189 -0.0160 0.0492  253  TRP A CD2 
1375 N NE1 . TRP A 233 ? 0.4265 0.5862 0.4432 -0.1144 -0.0010 0.0313  253  TRP A NE1 
1376 C CE2 . TRP A 233 ? 0.3410 0.5029 0.3808 -0.1116 -0.0089 0.0372  253  TRP A CE2 
1377 C CE3 . TRP A 233 ? 0.4014 0.5556 0.4420 -0.1174 -0.0253 0.0565  253  TRP A CE3 
1378 C CZ2 . TRP A 233 ? 0.3355 0.5028 0.4074 -0.1040 -0.0099 0.0327  253  TRP A CZ2 
1379 C CZ3 . TRP A 233 ? 0.3950 0.5562 0.4690 -0.1084 -0.0265 0.0510  253  TRP A CZ3 
1380 C CH2 . TRP A 233 ? 0.4163 0.5846 0.5052 -0.1023 -0.0184 0.0394  253  TRP A CH2 
1381 N N   . ARG A 234 ? 0.5733 0.7132 0.4723 -0.1675 0.0033  0.0814  254  ARG A N   
1382 C CA  . ARG A 234 ? 0.5908 0.7153 0.4551 -0.1841 0.0004  0.0943  254  ARG A CA  
1383 C C   . ARG A 234 ? 0.6499 0.7782 0.4859 -0.1902 0.0145  0.0878  254  ARG A C   
1384 O O   . ARG A 234 ? 0.7642 0.8717 0.5627 -0.2009 0.0071  0.0943  254  ARG A O   
1385 C CB  . ARG A 234 ? 0.5822 0.7104 0.4661 -0.1837 0.0039  0.0974  254  ARG A CB  
1386 C CG  . ARG A 234 ? 0.6031 0.7028 0.4626 -0.1955 -0.0106 0.1117  254  ARG A CG  
1387 C CD  . ARG A 234 ? 0.9979 1.0734 0.8547 -0.1929 -0.0359 0.1217  254  ARG A CD  
1388 N NE  . ARG A 234 ? 0.8947 0.9846 0.7977 -0.1757 -0.0397 0.1128  254  ARG A NE  
1389 C CZ  . ARG A 234 ? 0.7325 0.8269 0.6523 -0.1627 -0.0471 0.1028  254  ARG A CZ  
1390 N NH1 . ARG A 234 ? 0.7764 0.8622 0.6727 -0.1635 -0.0537 0.0998  254  ARG A NH1 
1391 N NH2 . ARG A 234 ? 0.6258 0.7334 0.5860 -0.1497 -0.0476 0.0953  254  ARG A NH2 
1392 N N   . HIS A 235 ? 0.6255 0.7771 0.4808 -0.1804 0.0329  0.0736  255  HIS A N   
1393 C CA  . HIS A 235 ? 0.6648 0.8207 0.4986 -0.1832 0.0458  0.0653  255  HIS A CA  
1394 C C   . HIS A 235 ? 0.7025 0.8464 0.5052 -0.1879 0.0396  0.0641  255  HIS A C   
1395 O O   . HIS A 235 ? 0.8308 0.9660 0.6022 -0.1957 0.0427  0.0630  255  HIS A O   
1396 C CB  . HIS A 235 ? 0.6763 0.8566 0.5378 -0.1687 0.0633  0.0506  255  HIS A CB  
1397 C CG  . HIS A 235 ? 0.5678 0.7593 0.4522 -0.1647 0.0695  0.0501  255  HIS A CG  
1398 N ND1 . HIS A 235 ? 0.5771 0.7584 0.4587 -0.1742 0.0617  0.0607  255  HIS A ND1 
1399 C CD2 . HIS A 235 ? 0.5759 0.7861 0.4843 -0.1524 0.0815  0.0401  255  HIS A CD2 
1400 C CE1 . HIS A 235 ? 0.6780 0.8730 0.5811 -0.1688 0.0696  0.0564  255  HIS A CE1 
1401 N NE2 . HIS A 235 ? 0.7073 0.9201 0.6269 -0.1554 0.0810  0.0443  255  HIS A NE2 
1402 N N   . ALA A 236 ? 0.7268 0.8699 0.5368 -0.1832 0.0308  0.0636  256  ALA A N   
1403 C CA  . ALA A 236 ? 0.7114 0.8381 0.4995 -0.1820 0.0189  0.0583  256  ALA A CA  
1404 C C   . ALA A 236 ? 0.8171 0.9157 0.5802 -0.1889 -0.0060 0.0706  256  ALA A C   
1405 O O   . ALA A 236 ? 0.8088 0.8929 0.5449 -0.1909 -0.0171 0.0676  256  ALA A O   
1406 C CB  . ALA A 236 ? 0.6421 0.7737 0.4630 -0.1665 0.0153  0.0460  256  ALA A CB  
1407 N N   A ALA A 237 ? 0.6580 1.0011 0.7681 0.0337  -0.0992 -0.0076 1001 ALA A N   
1408 N N   B ALA A 237 ? 0.7078 1.0510 0.8180 0.0337  -0.0992 -0.0076 1001 ALA A N   
1409 C CA  A ALA A 237 ? 0.6092 0.8990 0.7150 -0.0004 -0.1271 -0.0167 1001 ALA A CA  
1410 C CA  B ALA A 237 ? 0.6387 0.9286 0.7446 -0.0004 -0.1271 -0.0167 1001 ALA A CA  
1411 C C   A ALA A 237 ? 0.8184 1.1070 0.9120 -0.0409 -0.1408 -0.0205 1001 ALA A C   
1412 C C   B ALA A 237 ? 0.9035 1.1920 0.9970 -0.0409 -0.1408 -0.0205 1001 ALA A C   
1413 O O   A ALA A 237 ? 0.8210 1.0583 0.9041 -0.0647 -0.1472 -0.0212 1001 ALA A O   
1414 O O   B ALA A 237 ? 0.8199 1.0571 0.9030 -0.0648 -0.1472 -0.0212 1001 ALA A O   
1415 C CB  A ALA A 237 ? 0.6267 0.9238 0.7429 0.0015  -0.1505 -0.0257 1001 ALA A CB  
1416 C CB  B ALA A 237 ? 0.6257 0.9228 0.7419 0.0015  -0.1505 -0.0257 1001 ALA A CB  
1417 N N   . ASP A 238 ? 0.6678 1.0136 0.7624 -0.0488 -0.1449 -0.0235 1002 ASP A N   
1418 C CA  . ASP A 238 ? 0.7215 1.0679 0.8050 -0.0871 -0.1561 -0.0271 1002 ASP A CA  
1419 C C   . ASP A 238 ? 0.7363 1.0664 0.8075 -0.0918 -0.1364 -0.0180 1002 ASP A C   
1420 O O   . ASP A 238 ? 0.7779 1.0818 0.8368 -0.1246 -0.1458 -0.0196 1002 ASP A O   
1421 C CB  . ASP A 238 ? 0.6778 1.0948 0.7673 -0.0919 -0.1608 -0.0330 1002 ASP A CB  
1422 C CG  . ASP A 238 ? 0.7619 1.2406 0.8567 -0.0578 -0.1347 -0.0252 1002 ASP A CG  
1423 O OD1 . ASP A 238 ? 0.8936 1.3633 0.9914 -0.0238 -0.1148 -0.0161 1002 ASP A OD1 
1424 O OD2 . ASP A 238 ? 0.7401 1.2765 0.8361 -0.0646 -0.1332 -0.0282 1002 ASP A OD2 
1425 N N   . LEU A 239 ? 0.7364 1.0808 0.8104 -0.0591 -0.1080 -0.0083 1003 LEU A N   
1426 C CA  . LEU A 239 ? 0.6961 1.0249 0.7592 -0.0621 -0.0871 -0.0001 1003 LEU A CA  
1427 C C   . LEU A 239 ? 0.7932 1.0500 0.8479 -0.0807 -0.0936 -0.0019 1003 LEU A C   
1428 O O   . LEU A 239 ? 0.8648 1.1021 0.9066 -0.1050 -0.0934 -0.0008 1003 LEU A O   
1429 C CB  . LEU A 239 ? 0.6093 0.9634 0.6779 -0.0207 -0.0535 0.0105  1003 LEU A CB  
1430 C CG  . LEU A 239 ? 0.8175 1.2339 0.8835 -0.0112 -0.0350 0.0172  1003 LEU A CG  
1431 C CD1 . LEU A 239 ? 0.7773 1.2539 0.8491 -0.0189 -0.0528 0.0100  1003 LEU A CD1 
1432 C CD2 . LEU A 239 ? 0.5119 0.9484 0.5827 0.0337  -0.0008 0.0289  1003 LEU A CD2 
1433 N N   . GLU A 240 ? 0.7825 1.0009 0.8442 -0.0692 -0.0996 -0.0050 1004 GLU A N   
1434 C CA  . GLU A 240 ? 0.7438 0.8971 0.7984 -0.0861 -0.1070 -0.0083 1004 GLU A CA  
1435 C C   . GLU A 240 ? 0.7782 0.9096 0.8209 -0.1263 -0.1357 -0.0147 1004 GLU A C   
1436 O O   . GLU A 240 ? 0.8251 0.9212 0.8551 -0.1472 -0.1375 -0.0148 1004 GLU A O   
1437 C CB  . GLU A 240 ? 0.7434 0.8641 0.8091 -0.0662 -0.1096 -0.0115 1004 GLU A CB  
1438 C CG  . GLU A 240 ? 0.8730 0.9303 0.9326 -0.0863 -0.1249 -0.0178 1004 GLU A CG  
1439 C CD  . GLU A 240 ? 0.9043 0.9297 0.9760 -0.0634 -0.1203 -0.0205 1004 GLU A CD  
1440 O OE1 . GLU A 240 ? 0.8546 0.9005 0.9377 -0.0302 -0.0977 -0.0155 1004 GLU A OE1 
1441 O OE2 . GLU A 240 ? 1.1096 1.0894 1.1789 -0.0780 -0.1386 -0.0274 1004 GLU A OE2 
1442 N N   . ASP A 241 ? 0.7242 0.8766 0.7706 -0.1373 -0.1574 -0.0204 1005 ASP A N   
1443 C CA  . ASP A 241 ? 0.7476 0.8781 0.7824 -0.1750 -0.1825 -0.0259 1005 ASP A CA  
1444 C C   . ASP A 241 ? 0.7604 0.9049 0.7816 -0.1969 -0.1757 -0.0221 1005 ASP A C   
1445 O O   . ASP A 241 ? 0.7970 0.9040 0.8036 -0.2236 -0.1861 -0.0228 1005 ASP A O   
1446 C CB  . ASP A 241 ? 0.8520 1.0085 0.8950 -0.1817 -0.2027 -0.0335 1005 ASP A CB  
1447 C CG  . ASP A 241 ? 0.7330 0.8653 0.7866 -0.1666 -0.2147 -0.0381 1005 ASP A CG  
1448 O OD1 . ASP A 241 ? 0.8484 0.9270 0.8975 -0.1684 -0.2198 -0.0383 1005 ASP A OD1 
1449 O OD2 . ASP A 241 ? 0.5952 0.7638 0.6617 -0.1528 -0.2191 -0.0422 1005 ASP A OD2 
1450 N N   . ASN A 242 ? 0.6736 0.8730 0.6990 -0.1848 -0.1579 -0.0178 1006 ASN A N   
1451 C CA  . ASN A 242 ? 0.6444 0.8588 0.6576 -0.2031 -0.1488 -0.0135 1006 ASN A CA  
1452 C C   . ASN A 242 ? 0.6253 0.7989 0.6276 -0.2037 -0.1348 -0.0080 1006 ASN A C   
1453 O O   . ASN A 242 ? 0.6548 0.8077 0.6419 -0.2302 -0.1397 -0.0073 1006 ASN A O   
1454 C CB  . ASN A 242 ? 0.6219 0.9046 0.6427 -0.1848 -0.1301 -0.0095 1006 ASN A CB  
1455 C CG  . ASN A 242 ? 0.6819 1.0123 0.7137 -0.1872 -0.1440 -0.0172 1006 ASN A CG  
1456 O OD1 . ASN A 242 ? 0.7587 1.1295 0.8039 -0.1582 -0.1362 -0.0172 1006 ASN A OD1 
1457 N ND2 . ASN A 242 ? 0.7497 1.0759 0.7756 -0.2216 -0.1639 -0.0243 1006 ASN A ND2 
1458 N N   . TRP A 243 ? 0.6467 0.8082 0.6565 -0.1747 -0.1165 -0.0047 1007 TRP A N   
1459 C CA  . TRP A 243 ? 0.5644 0.6866 0.5661 -0.1750 -0.1022 -0.0021 1007 TRP A CA  
1460 C C   . TRP A 243 ? 0.6194 0.6853 0.6106 -0.2005 -0.1245 -0.0082 1007 TRP A C   
1461 O O   . TRP A 243 ? 0.6256 0.6683 0.6027 -0.2190 -0.1231 -0.0074 1007 TRP A O   
1462 C CB  . TRP A 243 ? 0.6251 0.7422 0.6394 -0.1392 -0.0785 0.0007  1007 TRP A CB  
1463 C CG  . TRP A 243 ? 0.7990 0.8683 0.8090 -0.1392 -0.0662 -0.0007 1007 TRP A CG  
1464 C CD1 . TRP A 243 ? 0.8137 0.8333 0.8245 -0.1447 -0.0788 -0.0080 1007 TRP A CD1 
1465 C CD2 . TRP A 243 ? 0.7639 0.8329 0.7691 -0.1333 -0.0384 0.0041  1007 TRP A CD2 
1466 N NE1 . TRP A 243 ? 0.7974 0.7878 0.8051 -0.1433 -0.0608 -0.0093 1007 TRP A NE1 
1467 C CE2 . TRP A 243 ? 0.7589 0.7775 0.7631 -0.1367 -0.0355 -0.0020 1007 TRP A CE2 
1468 C CE3 . TRP A 243 ? 0.7381 0.8452 0.7400 -0.1256 -0.0153 0.0124  1007 TRP A CE3 
1469 C CZ2 . TRP A 243 ? 0.8041 0.8093 0.8048 -0.1335 -0.0100 -0.0011 1007 TRP A CZ2 
1470 C CZ3 . TRP A 243 ? 0.7670 0.8585 0.7643 -0.1218 0.0101  0.0148  1007 TRP A CZ3 
1471 C CH2 . TRP A 243 ? 0.7459 0.7867 0.7430 -0.1263 0.0127  0.0076  1007 TRP A CH2 
1472 N N   . GLU A 244 ? 0.6312 0.6758 0.6283 -0.2010 -0.1453 -0.0142 1008 GLU A N   
1473 C CA  . GLU A 244 ? 0.6620 0.6543 0.6485 -0.2229 -0.1669 -0.0196 1008 GLU A CA  
1474 C C   . GLU A 244 ? 0.6790 0.6689 0.6483 -0.2568 -0.1826 -0.0191 1008 GLU A C   
1475 O O   . GLU A 244 ? 0.8192 0.7773 0.7732 -0.2744 -0.1859 -0.0188 1008 GLU A O   
1476 C CB  . GLU A 244 ? 0.7704 0.7445 0.7668 -0.2162 -0.1860 -0.0255 1008 GLU A CB  
1477 C CG  . GLU A 244 ? 0.6985 0.6633 0.7104 -0.1845 -0.1720 -0.0265 1008 GLU A CG  
1478 C CD  . GLU A 244 ? 0.6406 0.5873 0.6617 -0.1788 -0.1919 -0.0323 1008 GLU A CD  
1479 O OE1 . GLU A 244 ? 0.6714 0.6048 0.6852 -0.2012 -0.2171 -0.0360 1008 GLU A OE1 
1480 O OE2 . GLU A 244 ? 0.6975 0.6423 0.7330 -0.1516 -0.1813 -0.0330 1008 GLU A OE2 
1481 N N   . THR A 245 ? 0.6362 0.6608 0.6079 -0.2663 -0.1916 -0.0195 1009 THR A N   
1482 C CA  . THR A 245 ? 0.6726 0.6951 0.6306 -0.2881 -0.1966 -0.0185 1009 THR A CA  
1483 C C   . THR A 245 ? 0.6853 0.7207 0.6304 -0.3054 -0.1857 -0.0129 1009 THR A C   
1484 O O   . THR A 245 ? 0.7497 0.7584 0.6795 -0.3138 -0.1834 -0.0103 1009 THR A O   
1485 C CB  . THR A 245 ? 0.6611 0.7218 0.6279 -0.2899 -0.2017 -0.0218 1009 THR A CB  
1486 O OG1 . THR A 245 ? 0.5746 0.6954 0.5518 -0.2852 -0.1936 -0.0202 1009 THR A OG1 
1487 C CG2 . THR A 245 ? 0.6043 0.6492 0.5828 -0.2740 -0.2110 -0.0283 1009 THR A CG2 
1488 N N   . LEU A 246 ? 0.6992 0.7739 0.6534 -0.2845 -0.1624 -0.0087 1010 LEU A N   
1489 C CA  . LEU A 246 ? 0.7173 0.8051 0.6612 -0.2899 -0.1439 -0.0025 1010 LEU A CA  
1490 C C   . LEU A 246 ? 0.6618 0.7018 0.5935 -0.2952 -0.1405 -0.0022 1010 LEU A C   
1491 O O   . LEU A 246 ? 0.6593 0.6891 0.5747 -0.3158 -0.1402 0.0004  1010 LEU A O   
1492 C CB  . LEU A 246 ? 0.6681 0.8029 0.6246 -0.2609 -0.1174 0.0025  1010 LEU A CB  
1493 C CG  . LEU A 246 ? 0.6046 0.7682 0.5527 -0.2655 -0.0979 0.0092  1010 LEU A CG  
1494 C CD1 . LEU A 246 ? 0.7594 0.9746 0.7096 -0.2766 -0.1026 0.0091  1010 LEU A CD1 
1495 C CD2 . LEU A 246 ? 0.6484 0.8281 0.6046 -0.2335 -0.0676 0.0149  1010 LEU A CD2 
1496 N N   . ASN A 247 ? 0.6972 0.7086 0.6370 -0.2769 -0.1376 -0.0056 1011 ASN A N   
1497 C CA  . ASN A 247 ? 0.6684 0.6369 0.5986 -0.2816 -0.1346 -0.0080 1011 ASN A CA  
1498 C C   . ASN A 247 ? 0.7112 0.6401 0.6258 -0.3079 -0.1615 -0.0117 1011 ASN A C   
1499 O O   . ASN A 247 ? 0.7214 0.6303 0.6223 -0.3129 -0.1569 -0.0107 1011 ASN A O   
1500 C CB  . ASN A 247 ? 0.6231 0.5740 0.5683 -0.2549 -0.1229 -0.0121 1011 ASN A CB  
1501 C CG  . ASN A 247 ? 0.7140 0.6952 0.6706 -0.2285 -0.0907 -0.0072 1011 ASN A CG  
1502 O OD1 . ASN A 247 ? 0.6953 0.7188 0.6522 -0.2252 -0.0799 -0.0006 1011 ASN A OD1 
1503 N ND2 . ASN A 247 ? 0.7521 0.7119 0.7182 -0.2090 -0.0741 -0.0107 1011 ASN A ND2 
1504 N N   . ASP A 248 ? 0.7537 0.6778 0.6753 -0.2967 -0.1740 -0.0136 1012 ASP A N   
1505 C CA  . ASP A 248 ? 0.6549 0.5525 0.5675 -0.2928 -0.1810 -0.0133 1012 ASP A CA  
1506 C C   . ASP A 248 ? 0.7586 0.6646 0.6549 -0.3102 -0.1800 -0.0073 1012 ASP A C   
1507 O O   . ASP A 248 ? 0.8200 0.7030 0.7021 -0.3130 -0.1807 -0.0049 1012 ASP A O   
1508 C CB  . ASP A 248 ? 0.6290 0.5250 0.5524 -0.2810 -0.1910 -0.0162 1012 ASP A CB  
1509 C CG  . ASP A 248 ? 0.6867 0.5709 0.6248 -0.2628 -0.1922 -0.0218 1012 ASP A CG  
1510 O OD1 . ASP A 248 ? 0.6916 0.5644 0.6319 -0.2590 -0.1851 -0.0240 1012 ASP A OD1 
1511 O OD2 . ASP A 248 ? 0.6035 0.4890 0.5511 -0.2527 -0.1991 -0.0244 1012 ASP A OD2 
1512 N N   . ASN A 249 ? 0.7651 0.7070 0.6632 -0.3222 -0.1783 -0.0049 1013 ASN A N   
1513 C CA  . ASN A 249 ? 0.6728 0.6245 0.5562 -0.3397 -0.1758 0.0005  1013 ASN A CA  
1514 C C   . ASN A 249 ? 0.7454 0.6895 0.6140 -0.3494 -0.1661 0.0042  1013 ASN A C   
1515 O O   . ASN A 249 ? 0.9062 0.8347 0.7580 -0.3581 -0.1666 0.0083  1013 ASN A O   
1516 C CB  . ASN A 249 ? 0.6707 0.6702 0.5621 -0.3496 -0.1738 0.0007  1013 ASN A CB  
1517 C CG  . ASN A 249 ? 0.7552 0.7617 0.6586 -0.3430 -0.1832 -0.0039 1013 ASN A CG  
1518 O OD1 . ASN A 249 ? 0.7696 0.8092 0.6892 -0.3371 -0.1848 -0.0079 1013 ASN A OD1 
1519 N ND2 . ASN A 249 ? 0.8752 0.8533 0.7710 -0.3442 -0.1890 -0.0035 1013 ASN A ND2 
1520 N N   . LEU A 250 ? 0.7703 0.7257 0.6448 -0.3490 -0.1562 0.0026  1014 LEU A N   
1521 C CA  . LEU A 250 ? 0.7753 0.7233 0.6372 -0.3584 -0.1443 0.0046  1014 LEU A CA  
1522 C C   . LEU A 250 ? 0.8176 0.7230 0.6694 -0.3500 -0.1486 0.0024  1014 LEU A C   
1523 O O   . LEU A 250 ? 0.8937 0.7897 0.7285 -0.3594 -0.1459 0.0056  1014 LEU A O   
1524 C CB  . LEU A 250 ? 0.7457 0.7123 0.6207 -0.3453 -0.1239 0.0035  1014 LEU A CB  
1525 C CG  . LEU A 250 ? 0.6514 0.6699 0.5337 -0.3365 -0.1045 0.0099  1014 LEU A CG  
1526 C CD1 . LEU A 250 ? 0.6781 0.7137 0.5782 -0.3040 -0.0807 0.0104  1014 LEU A CD1 
1527 C CD2 . LEU A 250 ? 0.6958 0.7234 0.5621 -0.3527 -0.0939 0.0152  1014 LEU A CD2 
1528 N N   . LYS A 251 ? 0.8157 0.6989 0.6781 -0.3323 -0.1552 -0.0033 1015 LYS A N   
1529 C CA  . LYS A 251 ? 0.8528 0.7044 0.7087 -0.3234 -0.1586 -0.0064 1015 LYS A CA  
1530 C C   . LYS A 251 ? 0.9797 0.8196 0.8204 -0.3280 -0.1689 -0.0009 1015 LYS A C   
1531 O O   . LYS A 251 ? 1.0168 0.8421 0.8421 -0.3327 -0.1690 0.0008  1015 LYS A O   
1532 C CB  . LYS A 251 ? 0.7298 0.5663 0.6028 -0.3036 -0.1619 -0.0140 1015 LYS A CB  
1533 C CG  . LYS A 251 ? 0.8897 0.7242 0.7738 -0.2991 -0.1492 -0.0208 1015 LYS A CG  
1534 C CD  . LYS A 251 ? 0.8961 0.7226 0.7995 -0.2813 -0.1520 -0.0270 1015 LYS A CD  
1535 C CE  . LYS A 251 ? 0.8270 0.6450 0.7405 -0.2776 -0.1368 -0.0339 1015 LYS A CE  
1536 N NZ  . LYS A 251 ? 0.8096 0.6083 0.7204 -0.2740 -0.1295 -0.0414 1015 LYS A NZ  
1537 N N   . VAL A 252 ? 0.9684 0.8143 0.8129 -0.3275 -0.1770 0.0018  1016 VAL A N   
1538 C CA  . VAL A 252 ? 1.0041 0.8364 0.8337 -0.3337 -0.1851 0.0073  1016 VAL A CA  
1539 C C   . VAL A 252 ? 1.0482 0.8884 0.8590 -0.3536 -0.1810 0.0141  1016 VAL A C   
1540 O O   . VAL A 252 ? 1.1111 0.9343 0.9041 -0.3607 -0.1860 0.0193  1016 VAL A O   
1541 C CB  . VAL A 252 ? 0.8930 0.7303 0.7321 -0.3304 -0.1924 0.0072  1016 VAL A CB  
1542 C CG1 . VAL A 252 ? 0.8866 0.7146 0.7424 -0.3106 -0.1964 0.0010  1016 VAL A CG1 
1543 C CG2 . VAL A 252 ? 0.8244 0.6946 0.6717 -0.3401 -0.1885 0.0073  1016 VAL A CG2 
1544 N N   . ILE A 253 ? 0.9558 0.8227 0.7692 -0.3635 -0.1716 0.0147  1017 ILE A N   
1545 C CA  . ILE A 253 ? 1.0315 0.9081 0.8272 -0.3824 -0.1658 0.0209  1017 ILE A CA  
1546 C C   . ILE A 253 ? 1.0283 0.8826 0.8070 -0.3842 -0.1641 0.0220  1017 ILE A C   
1547 O O   . ILE A 253 ? 1.1262 0.9718 0.8848 -0.3965 -0.1660 0.0280  1017 ILE A O   
1548 C CB  . ILE A 253 ? 0.9638 0.8775 0.7671 -0.3917 -0.1541 0.0209  1017 ILE A CB  
1549 C CG1 . ILE A 253 ? 0.9150 0.8572 0.7293 -0.3961 -0.1569 0.0211  1017 ILE A CG1 
1550 C CG2 . ILE A 253 ? 1.0053 0.9264 0.7908 -0.4084 -0.1446 0.0259  1017 ILE A CG2 
1551 C CD1 . ILE A 253 ? 0.9398 0.9266 0.7667 -0.4016 -0.1467 0.0201  1017 ILE A CD1 
1552 N N   . GLU A 254 ? 0.9599 0.8052 0.7463 -0.3727 -0.1604 0.0155  1018 GLU A N   
1553 C CA  . GLU A 254 ? 1.0312 0.8578 0.8037 -0.3735 -0.1589 0.0141  1018 GLU A CA  
1554 C C   . GLU A 254 ? 1.0923 0.8928 0.8546 -0.3677 -0.1719 0.0159  1018 GLU A C   
1555 O O   . GLU A 254 ? 1.1031 0.8907 0.8458 -0.3752 -0.1739 0.0188  1018 GLU A O   
1556 C CB  . GLU A 254 ? 0.9537 0.7785 0.7402 -0.3628 -0.1500 0.0044  1018 GLU A CB  
1557 C CG  . GLU A 254 ? 0.9597 0.8089 0.7560 -0.3691 -0.1351 0.0032  1018 GLU A CG  
1558 C CD  . GLU A 254 ? 1.1668 1.0102 0.9800 -0.3573 -0.1256 -0.0067 1018 GLU A CD  
1559 O OE1 . GLU A 254 ? 1.2410 1.0634 1.0598 -0.3434 -0.1313 -0.0136 1018 GLU A OE1 
1560 O OE2 . GLU A 254 ? 1.2258 1.0867 1.0471 -0.3628 -0.1108 -0.0075 1018 GLU A OE2 
1561 N N   . LYS A 255 ? 1.1647 0.9580 0.9388 -0.3554 -0.1804 0.0145  1019 LYS A N   
1562 C CA  . LYS A 255 ? 1.1423 0.9115 0.9077 -0.3491 -0.1918 0.0162  1019 LYS A CA  
1563 C C   . LYS A 255 ? 1.2989 1.0620 1.0494 -0.3608 -0.1990 0.0255  1019 LYS A C   
1564 O O   . LYS A 255 ? 1.4120 1.1671 1.1676 -0.3545 -0.2064 0.0264  1019 LYS A O   
1565 C CB  . LYS A 255 ? 1.1413 0.9056 0.9275 -0.3292 -0.1954 0.0091  1019 LYS A CB  
1566 C CG  . LYS A 255 ? 1.0625 0.8325 0.8661 -0.3179 -0.1868 -0.0012 1019 LYS A CG  
1567 C CD  . LYS A 255 ? 0.8619 0.6201 0.6565 -0.3172 -0.1856 -0.0057 1019 LYS A CD  
1568 C CE  . LYS A 255 ? 0.7669 0.5297 0.5809 -0.3066 -0.1755 -0.0178 1019 LYS A CE  
1569 N NZ  . LYS A 255 ? 0.7509 0.5043 0.5591 -0.3054 -0.1742 -0.0249 1019 LYS A NZ  
1570 N N   . ALA A 256 ? 1.3135 1.0803 1.0451 -0.3788 -0.1959 0.0320  1020 ALA A N   
1571 C CA  . ALA A 256 ? 1.4277 1.1870 1.1434 -0.3924 -0.2012 0.0403  1020 ALA A CA  
1572 C C   . ALA A 256 ? 1.4545 1.2156 1.1471 -0.4116 -0.1966 0.0468  1020 ALA A C   
1573 O O   . ALA A 256 ? 1.4802 1.2619 1.1762 -0.4172 -0.1864 0.0450  1020 ALA A O   
1574 C CB  . ALA A 256 ? 1.4459 1.2242 1.1780 -0.3941 -0.1993 0.0392  1020 ALA A CB  
1575 N N   . ASP A 257 ? 1.3836 1.1230 1.0520 -0.4221 -0.2037 0.0545  1021 ASP A N   
1576 C CA  . ASP A 257 ? 1.3444 1.0827 0.9882 -0.4415 -0.2001 0.0615  1021 ASP A CA  
1577 C C   . ASP A 257 ? 1.3634 1.1075 1.0009 -0.4577 -0.1983 0.0671  1021 ASP A C   
1578 O O   . ASP A 257 ? 1.3939 1.1366 1.0105 -0.4750 -0.1950 0.0733  1021 ASP A O   
1579 C CB  . ASP A 257 ? 1.2023 0.9112 0.8193 -0.4444 -0.2091 0.0664  1021 ASP A CB  
1580 C CG  . ASP A 257 ? 1.0938 0.8037 0.6868 -0.4616 -0.2040 0.0714  1021 ASP A CG  
1581 O OD1 . ASP A 257 ? 0.9867 0.7212 0.5855 -0.4699 -0.1927 0.0706  1021 ASP A OD1 
1582 O OD2 . ASP A 257 ? 1.1576 0.8444 0.7251 -0.4672 -0.2115 0.0763  1021 ASP A OD2 
1583 N N   . ASN A 258 ? 1.2017 0.9527 0.8571 -0.4530 -0.1999 0.0642  1022 ASN A N   
1584 C CA  . ASN A 258 ? 1.1457 0.9054 0.7996 -0.4682 -0.1969 0.0667  1022 ASN A CA  
1585 C C   . ASN A 258 ? 1.0553 0.8537 0.7275 -0.4725 -0.1859 0.0620  1022 ASN A C   
1586 O O   . ASN A 258 ? 1.1206 0.9375 0.8146 -0.4594 -0.1834 0.0556  1022 ASN A O   
1587 C CB  . ASN A 258 ? 1.1581 0.9052 0.8214 -0.4625 -0.2041 0.0647  1022 ASN A CB  
1588 C CG  . ASN A 258 ? 1.4836 1.1938 1.1215 -0.4688 -0.2130 0.0722  1022 ASN A CG  
1589 O OD1 . ASN A 258 ? 1.4154 1.1175 1.0373 -0.4864 -0.2112 0.0772  1022 ASN A OD1 
1590 N ND2 . ASN A 258 ? 1.5539 1.2416 1.1875 -0.4548 -0.2223 0.0728  1022 ASN A ND2 
1591 N N   . ALA A 259 ? 1.0073 0.8185 0.6701 -0.4914 -0.1793 0.0654  1023 ALA A N   
1592 C CA  . ALA A 259 ? 0.9470 0.7982 0.6254 -0.4976 -0.1688 0.0615  1023 ALA A CA  
1593 C C   . ALA A 259 ? 0.9299 0.8008 0.6337 -0.4922 -0.1697 0.0542  1023 ALA A C   
1594 O O   . ALA A 259 ? 0.9105 0.8184 0.6303 -0.4940 -0.1624 0.0498  1023 ALA A O   
1595 C CB  . ALA A 259 ? 1.0900 0.9503 0.7518 -0.5195 -0.1614 0.0665  1023 ALA A CB  
1596 N N   . ALA A 260 ? 0.9373 0.7864 0.6447 -0.4863 -0.1783 0.0525  1024 ALA A N   
1597 C CA  . ALA A 260 ? 0.9512 0.8180 0.6830 -0.4808 -0.1795 0.0444  1024 ALA A CA  
1598 C C   . ALA A 260 ? 0.8890 0.7614 0.6406 -0.4592 -0.1831 0.0389  1024 ALA A C   
1599 O O   . ALA A 260 ? 0.8703 0.7732 0.6437 -0.4547 -0.1806 0.0320  1024 ALA A O   
1600 C CB  . ALA A 260 ? 1.1303 0.9714 0.8575 -0.4853 -0.1857 0.0445  1024 ALA A CB  
1601 N N   . GLN A 261 ? 0.9140 0.7588 0.6584 -0.4460 -0.1889 0.0414  1025 GLN A N   
1602 C CA  . GLN A 261 ? 0.8906 0.7392 0.6537 -0.4256 -0.1913 0.0357  1025 GLN A CA  
1603 C C   . GLN A 261 ? 0.9066 0.7893 0.6822 -0.4246 -0.1826 0.0326  1025 GLN A C   
1604 O O   . GLN A 261 ? 0.8454 0.7451 0.6417 -0.4126 -0.1827 0.0264  1025 GLN A O   
1605 C CB  . GLN A 261 ? 0.8588 0.6759 0.6107 -0.4140 -0.1969 0.0384  1025 GLN A CB  
1606 N N   . VAL A 262 ? 0.9357 0.8294 0.6980 -0.4377 -0.1748 0.0370  1026 VAL A N   
1607 C CA  . VAL A 262 ? 0.9584 0.8878 0.7309 -0.4396 -0.1651 0.0349  1026 VAL A CA  
1608 C C   . VAL A 262 ? 0.9474 0.9152 0.7367 -0.4453 -0.1623 0.0305  1026 VAL A C   
1609 O O   . VAL A 262 ? 1.0764 1.0738 0.8835 -0.4381 -0.1592 0.0260  1026 VAL A O   
1610 C CB  . VAL A 262 ? 1.0304 0.9637 0.7838 -0.4537 -0.1565 0.0408  1026 VAL A CB  
1611 C CG1 . VAL A 262 ? 1.0237 0.9994 0.7874 -0.4586 -0.1446 0.0393  1026 VAL A CG1 
1612 C CG2 . VAL A 262 ? 1.1866 1.0877 0.9265 -0.4463 -0.1588 0.0427  1026 VAL A CG2 
1613 N N   . LYS A 263 ? 0.8793 0.8490 0.6632 -0.4588 -0.1632 0.0312  1027 LYS A N   
1614 C CA  . LYS A 263 ? 0.9062 0.9157 0.7071 -0.4650 -0.1602 0.0252  1027 LYS A CA  
1615 C C   . LYS A 263 ? 0.9197 0.9341 0.7426 -0.4491 -0.1673 0.0173  1027 LYS A C   
1616 O O   . LYS A 263 ? 0.9797 1.0347 0.8207 -0.4457 -0.1645 0.0117  1027 LYS A O   
1617 C CB  . LYS A 263 ? 0.9398 0.9454 0.7312 -0.4829 -0.1594 0.0259  1027 LYS A CB  
1618 C CG  . LYS A 263 ? 1.0482 1.1016 0.8556 -0.4929 -0.1536 0.0187  1027 LYS A CG  
1619 C CD  . LYS A 263 ? 1.1183 1.1626 0.9282 -0.5029 -0.1566 0.0137  1027 LYS A CD  
1620 C CE  . LYS A 263 ? 1.1514 1.1864 0.9417 -0.5240 -0.1507 0.0188  1027 LYS A CE  
1621 N NZ  . LYS A 263 ? 1.0201 1.0568 0.8172 -0.5363 -0.1505 0.0117  1027 LYS A NZ  
1622 N N   . ASP A 264 ? 0.9044 0.8806 0.7258 -0.4388 -0.1763 0.0169  1028 ASP A N   
1623 C CA  . ASP A 264 ? 0.8544 0.8332 0.6962 -0.4235 -0.1829 0.0093  1028 ASP A CA  
1624 C C   . ASP A 264 ? 0.9141 0.9103 0.7692 -0.4084 -0.1816 0.0069  1028 ASP A C   
1625 O O   . ASP A 264 ? 0.9347 0.9624 0.8091 -0.4019 -0.1823 0.0002  1028 ASP A O   
1626 C CB  . ASP A 264 ? 0.8750 0.8095 0.7108 -0.4149 -0.1914 0.0105  1028 ASP A CB  
1627 C CG  . ASP A 264 ? 0.9946 0.9140 0.8207 -0.4294 -0.1930 0.0115  1028 ASP A CG  
1628 O OD1 . ASP A 264 ? 1.0281 0.9377 0.8344 -0.4444 -0.1894 0.0183  1028 ASP A OD1 
1629 O OD2 . ASP A 264 ? 1.0853 1.0025 0.9235 -0.4264 -0.1973 0.0053  1028 ASP A OD2 
1630 N N   . ALA A 265 ? 0.8766 0.8537 0.7218 -0.4027 -0.1797 0.0117  1029 ALA A N   
1631 C CA  . ALA A 265 ? 0.8462 0.8357 0.7034 -0.3895 -0.1775 0.0092  1029 ALA A CA  
1632 C C   . ALA A 265 ? 0.9127 0.9542 0.7788 -0.3971 -0.1690 0.0082  1029 ALA A C   
1633 O O   . ALA A 265 ? 0.9446 1.0140 0.8282 -0.3874 -0.1694 0.0037  1029 ALA A O   
1634 C CB  . ALA A 265 ? 0.7902 0.7500 0.6345 -0.3849 -0.1752 0.0133  1029 ALA A CB  
1635 N N   . LEU A 266 ? 0.8838 0.9428 0.7381 -0.4142 -0.1609 0.0128  1030 LEU A N   
1636 C CA  . LEU A 266 ? 0.9039 1.0198 0.7670 -0.4218 -0.1513 0.0121  1030 LEU A CA  
1637 C C   . LEU A 266 ? 0.9593 1.1147 0.8404 -0.4204 -0.1545 0.0049  1030 LEU A C   
1638 O O   . LEU A 266 ? 0.9338 1.1388 0.8310 -0.4142 -0.1508 0.0016  1030 LEU A O   
1639 C CB  . LEU A 266 ? 0.9608 1.0866 0.8075 -0.4406 -0.1417 0.0180  1030 LEU A CB  
1640 C CG  . LEU A 266 ? 0.8848 0.9899 0.7169 -0.4428 -0.1345 0.0241  1030 LEU A CG  
1641 C CD1 . LEU A 266 ? 0.8509 0.9510 0.6629 -0.4606 -0.1287 0.0300  1030 LEU A CD1 
1642 C CD2 . LEU A 266 ? 0.8977 1.0434 0.7428 -0.4398 -0.1232 0.0239  1030 LEU A CD2 
1643 N N   . THR A 267 ? 1.0631 1.2008 0.9425 -0.4257 -0.1606 0.0018  1031 THR A N   
1644 C CA  . THR A 267 ? 1.1275 1.2999 1.0248 -0.4245 -0.1635 -0.0072 1031 THR A CA  
1645 C C   . THR A 267 ? 1.0358 1.2110 0.9508 -0.4043 -0.1711 -0.0129 1031 THR A C   
1646 O O   . THR A 267 ? 1.0994 1.3249 1.0316 -0.3977 -0.1701 -0.0189 1031 THR A O   
1647 C CB  . THR A 267 ? 1.0818 1.2286 0.9737 -0.4356 -0.1676 -0.0098 1031 THR A CB  
1648 O OG1 . THR A 267 ? 1.1854 1.2736 1.0660 -0.4296 -0.1748 -0.0058 1031 THR A OG1 
1649 C CG2 . THR A 267 ? 1.0210 1.1802 0.8992 -0.4569 -0.1590 -0.0061 1031 THR A CG2 
1650 N N   . LYS A 268 ? 0.8252 0.9498 0.7363 -0.3928 -0.1785 -0.0114 1032 LYS A N   
1651 C CA  . LYS A 268 ? 0.8171 0.9415 0.7436 -0.3732 -0.1848 -0.0161 1032 LYS A CA  
1652 C C   . LYS A 268 ? 0.8849 1.0382 0.8163 -0.3658 -0.1793 -0.0133 1032 LYS A C   
1653 O O   . LYS A 268 ? 0.8864 1.0603 0.8333 -0.3510 -0.1828 -0.0174 1032 LYS A O   
1654 C CB  . LYS A 268 ? 0.7782 0.8443 0.6991 -0.3627 -0.1922 -0.0150 1032 LYS A CB  
1655 C CG  . LYS A 268 ? 1.0227 1.0632 0.9405 -0.3680 -0.1973 -0.0176 1032 LYS A CG  
1656 C CD  . LYS A 268 ? 0.9814 0.9727 0.8935 -0.3559 -0.2031 -0.0158 1032 LYS A CD  
1657 C CE  . LYS A 268 ? 0.9983 0.9655 0.9049 -0.3628 -0.2070 -0.0168 1032 LYS A CE  
1658 N NZ  . LYS A 268 ? 1.0192 0.9935 0.9440 -0.3542 -0.2122 -0.0262 1032 LYS A NZ  
1659 N N   . MET A 269 ? 0.8826 1.0394 0.8014 -0.3761 -0.1701 -0.0064 1033 MET A N   
1660 C CA  . MET A 269 ? 0.8215 1.0113 0.7458 -0.3720 -0.1620 -0.0037 1033 MET A CA  
1661 C C   . MET A 269 ? 0.8667 1.1293 0.8042 -0.3652 -0.1499 -0.0045 1033 MET A C   
1662 O O   . MET A 269 ? 0.8427 1.1338 0.7937 -0.3342 -0.1373 -0.0031 1033 MET A O   
1663 C CB  . MET A 269 ? 0.8589 1.0229 0.7657 -0.3826 -0.1533 0.0033  1033 MET A CB  
1664 C CG  . MET A 269 ? 0.8243 0.9984 0.7366 -0.3538 -0.1304 0.0084  1033 MET A CG  
1665 S SD  . MET A 269 ? 0.6480 0.7982 0.5403 -0.3644 -0.1158 0.0155  1033 MET A SD  
1666 C CE  . MET A 269 ? 0.6683 0.7496 0.5437 -0.3867 -0.1394 0.0122  1033 MET A CE  
1667 N N   . ARG A 270 ? 0.8222 1.1136 0.7557 -0.3881 -0.1503 -0.0062 1034 ARG A N   
1668 C CA  . ARG A 270 ? 0.7355 1.0983 0.6820 -0.3782 -0.1378 -0.0079 1034 ARG A CA  
1669 C C   . ARG A 270 ? 0.7595 1.1565 0.7259 -0.3635 -0.1463 -0.0170 1034 ARG A C   
1670 O O   . ARG A 270 ? 0.8245 1.2732 0.8041 -0.3358 -0.1331 -0.0164 1034 ARG A O   
1671 C CB  . ARG A 270 ? 0.7563 1.1382 0.6951 -0.4069 -0.1374 -0.0097 1034 ARG A CB  
1672 C CG  . ARG A 270 ? 0.8845 1.3449 0.8351 -0.3997 -0.1233 -0.0113 1034 ARG A CG  
1673 C CD  . ARG A 270 ? 0.7963 1.2731 0.7453 -0.4225 -0.1255 -0.0182 1034 ARG A CD  
1674 N NE  . ARG A 270 ? 0.8155 1.3773 0.7787 -0.4189 -0.1154 -0.0226 1034 ARG A NE  
1675 C CZ  . ARG A 270 ? 0.8339 1.4300 0.7921 -0.4306 -0.1029 -0.0189 1034 ARG A CZ  
1676 N NH1 . ARG A 270 ? 0.8342 1.3884 0.7729 -0.4498 -0.0995 -0.0108 1034 ARG A NH1 
1677 N NH2 . ARG A 270 ? 0.7108 1.3819 0.6822 -0.4185 -0.0919 -0.0229 1034 ARG A NH2 
1678 N N   . ALA A 271 ? 0.8977 1.2555 0.8648 -0.3692 -0.1614 -0.0237 1035 ALA A N   
1679 C CA  . ALA A 271 ? 0.8509 1.2336 0.8365 -0.3530 -0.1686 -0.0328 1035 ALA A CA  
1680 C C   . ALA A 271 ? 0.9456 1.3417 0.9414 -0.3294 -0.1697 -0.0307 1035 ALA A C   
1681 O O   . ALA A 271 ? 0.8883 1.3350 0.9001 -0.3046 -0.1639 -0.0339 1035 ALA A O   
1682 C CB  . ALA A 271 ? 0.8268 1.1523 0.8107 -0.3567 -0.1799 -0.0385 1035 ALA A CB  
1683 N N   . ALA A 272 ? 0.8443 1.1823 0.8301 -0.3234 -0.1691 -0.0238 1036 ALA A N   
1684 C CA  . ALA A 272 ? 0.7320 1.0630 0.7262 -0.2876 -0.1593 -0.0195 1036 ALA A CA  
1685 C C   . ALA A 272 ? 0.7727 1.1517 0.7719 -0.2596 -0.1326 -0.0119 1036 ALA A C   
1686 O O   . ALA A 272 ? 0.7782 1.1855 0.7905 -0.2270 -0.1230 -0.0107 1036 ALA A O   
1687 C CB  . ALA A 272 ? 0.7852 1.0465 0.7676 -0.2899 -0.1623 -0.0152 1036 ALA A CB  
1688 N N   . ALA A 273 ? 0.8215 1.2096 0.8094 -0.2707 -0.1196 -0.0059 1037 ALA A N   
1689 C CA  . ALA A 273 ? 0.7617 1.1969 0.7532 -0.2450 -0.0933 0.0020  1037 ALA A CA  
1690 C C   . ALA A 273 ? 0.9074 1.4170 0.9133 -0.2326 -0.0915 -0.0029 1037 ALA A C   
1691 O O   . ALA A 273 ? 0.9066 1.4557 0.9214 -0.1978 -0.0734 0.0022  1037 ALA A O   
1692 C CB  . ALA A 273 ? 0.7842 1.2146 0.7602 -0.2631 -0.0818 0.0084  1037 ALA A CB  
1693 N N   . LEU A 274 ? 0.9517 1.4826 0.9602 -0.2604 -0.1090 -0.0132 1038 LEU A N   
1694 C CA  . LEU A 274 ? 0.8977 1.5038 0.9212 -0.2514 -0.1085 -0.0208 1038 LEU A CA  
1695 C C   . LEU A 274 ? 0.8965 1.5174 0.9354 -0.2238 -0.1144 -0.0256 1038 LEU A C   
1696 O O   . LEU A 274 ? 0.8604 1.5432 0.9108 -0.1949 -0.1030 -0.0256 1038 LEU A O   
1697 C CB  . LEU A 274 ? 0.8777 1.4980 0.9014 -0.2909 -0.1254 -0.0329 1038 LEU A CB  
1698 C CG  . LEU A 274 ? 1.0151 1.6396 1.0259 -0.3163 -0.1173 -0.0290 1038 LEU A CG  
1699 C CD1 . LEU A 274 ? 1.0595 1.6793 1.0690 -0.3564 -0.1338 -0.0408 1038 LEU A CD1 
1700 C CD2 . LEU A 274 ? 1.1163 1.8122 1.1323 -0.2951 -0.0958 -0.0247 1038 LEU A CD2 
1701 N N   . ASP A 275 ? 0.8372 1.4033 0.8761 -0.2308 -0.1317 -0.0295 1039 ASP A N   
1702 C CA  . ASP A 275 ? 0.8288 1.4063 0.8823 -0.2062 -0.1386 -0.0346 1039 ASP A CA  
1703 C C   . ASP A 275 ? 0.7817 1.3741 0.8396 -0.1609 -0.1159 -0.0235 1039 ASP A C   
1704 O O   . ASP A 275 ? 0.7572 1.3899 0.8284 -0.1328 -0.1140 -0.0261 1039 ASP A O   
1705 C CB  . ASP A 275 ? 0.9271 1.4361 0.9777 -0.2216 -0.1597 -0.0390 1039 ASP A CB  
1706 C CG  . ASP A 275 ? 0.8175 1.3147 0.8657 -0.2624 -0.1819 -0.0506 1039 ASP A CG  
1707 O OD1 . ASP A 275 ? 0.7424 1.2764 0.7911 -0.2762 -0.1777 -0.0553 1039 ASP A OD1 
1708 O OD2 . ASP A 275 ? 1.0252 1.4581 1.0692 -0.2701 -0.1952 -0.0532 1039 ASP A OD2 
1709 N N   . ALA A 276 ? 0.7834 1.3436 0.8303 -0.1529 -0.0976 -0.0114 1040 ALA A N   
1710 C CA  . ALA A 276 ? 0.8940 1.4647 0.9444 -0.1105 -0.0722 -0.0004 1040 ALA A CA  
1711 C C   . ALA A 276 ? 0.8475 1.4965 0.9031 -0.0866 -0.0530 0.0038  1040 ALA A C   
1712 O O   . ALA A 276 ? 0.8279 1.4987 0.8889 -0.0465 -0.0328 0.0121  1040 ALA A O   
1713 C CB  . ALA A 276 ? 0.9142 1.4290 0.9520 -0.1111 -0.0566 0.0095  1040 ALA A CB  
1714 N N   . GLN A 277 ? 0.8370 1.5289 0.8908 -0.1095 -0.0578 -0.0015 1041 GLN A N   
1715 C CA  . GLN A 277 ? 0.8562 1.6264 0.9146 -0.0876 -0.0401 0.0019  1041 GLN A CA  
1716 C C   . GLN A 277 ? 0.9559 1.7903 1.0303 -0.0722 -0.0500 -0.0086 1041 GLN A C   
1717 O O   . GLN A 277 ? 0.9990 1.8877 1.0796 -0.0336 -0.0327 -0.0030 1041 GLN A O   
1718 C CB  . GLN A 277 ? 0.9205 1.7113 0.9705 -0.1185 -0.0394 0.0003  1041 GLN A CB  
1719 N N   . LYS A 278 ? 0.9112 1.7414 0.9923 -0.1011 -0.0768 -0.0241 1042 LYS A N   
1720 C CA  . LYS A 278 ? 0.9128 1.8051 1.0102 -0.0891 -0.0873 -0.0366 1042 LYS A CA  
1721 C C   . LYS A 278 ? 0.9358 1.8230 1.0406 -0.0486 -0.0828 -0.0318 1042 LYS A C   
1722 O O   . LYS A 278 ? 0.9350 1.8861 1.0519 -0.0228 -0.0818 -0.0370 1042 LYS A O   
1723 C CB  . LYS A 278 ? 0.9263 1.8060 1.0291 -0.1308 -0.1158 -0.0546 1042 LYS A CB  
1724 C CG  . LYS A 278 ? 0.8947 1.7101 0.9991 -0.1358 -0.1339 -0.0581 1042 LYS A CG  
1725 C CD  . LYS A 278 ? 0.8407 1.6242 0.9451 -0.1777 -0.1566 -0.0730 1042 LYS A CD  
1726 C CE  . LYS A 278 ? 0.8648 1.6915 0.9771 -0.1781 -0.1546 -0.0865 1042 LYS A CE  
1727 N NZ  . LYS A 278 ? 0.8364 1.7135 0.9610 -0.1397 -0.1495 -0.0894 1042 LYS A NZ  
1728 N N   . ALA A 279 ? 0.9575 1.7712 1.0556 -0.0423 -0.0797 -0.0227 1043 ALA A N   
1729 C CA  . ALA A 279 ? 0.9111 1.7129 1.0164 -0.0060 -0.0754 -0.0185 1043 ALA A CA  
1730 C C   . ALA A 279 ? 0.7464 1.6038 0.8544 0.0426  -0.0474 -0.0068 1043 ALA A C   
1731 O O   . ALA A 279 ? 0.6245 1.5380 0.7435 0.0694  -0.0481 -0.0109 1043 ALA A O   
1732 C CB  . ALA A 279 ? 0.8291 1.5419 0.9264 -0.0102 -0.0746 -0.0112 1043 ALA A CB  
1733 N N   . THR A 280 ? 0.7557 1.5988 0.8532 0.0556  -0.0215 0.0081  1044 THR A N   
1734 C CA  . THR A 280 ? 0.8386 1.7238 0.9360 0.1038  0.0094  0.0221  1044 THR A CA  
1735 C C   . THR A 280 ? 0.9365 1.8527 1.0244 0.1004  0.0284  0.0299  1044 THR A C   
1736 O O   . THR A 280 ? 0.8585 1.7387 0.9364 0.1097  0.0516  0.0432  1044 THR A O   
1737 C CB  . THR A 280 ? 0.8520 1.6777 0.9468 0.1320  0.0283  0.0347  1044 THR A CB  
1738 O OG1 . THR A 280 ? 0.8331 1.6009 0.9161 0.1148  0.0405  0.0421  1044 THR A OG1 
1739 C CG2 . THR A 280 ? 0.7926 1.5729 0.8953 0.1257  0.0063  0.0261  1044 THR A CG2 
1740 N N   . PRO A 281 ? 1.0536 2.0381 1.1450 0.0868  0.0197  0.0209  1045 PRO A N   
1741 C CA  . PRO A 281 ? 1.0487 2.0701 1.1317 0.0858  0.0381  0.0282  1045 PRO A CA  
1742 C C   . PRO A 281 ? 0.9766 2.0489 1.0585 0.1383  0.0701  0.0432  1045 PRO A C   
1743 O O   . PRO A 281 ? 0.9953 2.0603 1.0756 0.1714  0.0702  0.0462  1045 PRO A O   
1744 C CB  . PRO A 281 ? 1.0560 2.1375 1.1463 0.0558  0.0170  0.0111  1045 PRO A CB  
1745 C CG  . PRO A 281 ? 1.0158 2.1243 1.1206 0.0640  -0.0023 -0.0020 1045 PRO A CG  
1746 C CD  . PRO A 281 ? 1.0788 2.1087 1.1827 0.0693  -0.0074 0.0022  1045 PRO A CD  
1747 N N   . ASP A 302 ? 0.5395 1.2457 0.5196 -0.1370 0.0613  0.0554  1066 ASP A N   
1748 C CA  . ASP A 302 ? 0.7082 1.4488 0.6812 -0.1599 0.0627  0.0552  1066 ASP A CA  
1749 C C   . ASP A 302 ? 0.5985 1.2821 0.5548 -0.1879 0.0636  0.0586  1066 ASP A C   
1750 O O   . ASP A 302 ? 0.6943 1.3619 0.6441 -0.2253 0.0447  0.0520  1066 ASP A O   
1751 C CB  . ASP A 302 ? 0.5431 1.3493 0.5182 -0.1283 0.0898  0.0645  1066 ASP A CB  
1752 N N   . ILE A 303 ? 0.5672 1.2202 0.5167 -0.1692 0.0867  0.0687  1067 ILE A N   
1753 C CA  . ILE A 303 ? 0.5824 1.1836 0.5163 -0.1932 0.0892  0.0713  1067 ILE A CA  
1754 C C   . ILE A 303 ? 0.6780 1.2167 0.6081 -0.2200 0.0631  0.0629  1067 ILE A C   
1755 O O   . ILE A 303 ? 0.7225 1.2307 0.6396 -0.2525 0.0518  0.0608  1067 ILE A O   
1756 C CB  . ILE A 303 ? 0.7050 1.2861 0.6346 -0.1660 0.1207  0.0818  1067 ILE A CB  
1757 C CG1 . ILE A 303 ? 0.7470 1.2954 0.6601 -0.1901 0.1272  0.0848  1067 ILE A CG1 
1758 C CG2 . ILE A 303 ? 0.5791 1.1127 0.5152 -0.1475 0.1223  0.0803  1067 ILE A CG2 
1759 C CD1 . ILE A 303 ? 0.6934 1.2203 0.6023 -0.1670 0.1593  0.0934  1067 ILE A CD1 
1760 N N   . LEU A 304 ? 0.6733 1.1926 0.6137 -0.2058 0.0535  0.0585  1068 LEU A N   
1761 C CA  . LEU A 304 ? 0.6407 1.1031 0.5779 -0.2289 0.0282  0.0506  1068 LEU A CA  
1762 C C   . LEU A 304 ? 0.6285 1.0997 0.5620 -0.2647 0.0025  0.0429  1068 LEU A C   
1763 O O   . LEU A 304 ? 0.7351 1.1690 0.6548 -0.2950 -0.0085 0.0415  1068 LEU A O   
1764 C CB  . LEU A 304 ? 0.7435 1.1931 0.6943 -0.2054 0.0227  0.0470  1068 LEU A CB  
1765 C CG  . LEU A 304 ? 0.7387 1.1285 0.6875 -0.2234 -0.0017 0.0393  1068 LEU A CG  
1766 C CD1 . LEU A 304 ? 0.9412 1.3123 0.9021 -0.1936 0.0030  0.0386  1068 LEU A CD1 
1767 C CD2 . LEU A 304 ? 0.5998 0.9981 0.5498 -0.2508 -0.0306 0.0305  1068 LEU A CD2 
1768 N N   . VAL A 305 ? 0.6018 1.1232 0.5479 -0.2614 -0.0062 0.0373  1069 VAL A N   
1769 C CA  . VAL A 305 ? 0.7039 1.2361 0.6487 -0.2957 -0.0280 0.0285  1069 VAL A CA  
1770 C C   . VAL A 305 ? 0.7861 1.3310 0.7180 -0.3189 -0.0207 0.0322  1069 VAL A C   
1771 O O   . VAL A 305 ? 0.8157 1.3330 0.7371 -0.3531 -0.0356 0.0286  1069 VAL A O   
1772 C CB  . VAL A 305 ? 0.5790 1.1719 0.5415 -0.2858 -0.0350 0.0203  1069 VAL A CB  
1773 C CG1 . VAL A 305 ? 0.6604 1.2663 0.6228 -0.3230 -0.0545 0.0097  1069 VAL A CG1 
1774 C CG2 . VAL A 305 ? 0.5659 1.1422 0.5400 -0.2646 -0.0439 0.0165  1069 VAL A CG2 
1775 N N   . GLY A 306 ? 0.7666 1.3524 0.6985 -0.2997 0.0034  0.0401  1070 GLY A N   
1776 C CA  . GLY A 306 ? 0.7739 1.3713 0.6934 -0.3198 0.0121  0.0444  1070 GLY A CA  
1777 C C   . GLY A 306 ? 0.7417 1.2729 0.6427 -0.3407 0.0095  0.0483  1070 GLY A C   
1778 O O   . GLY A 306 ? 0.7286 1.2491 0.6177 -0.3720 0.0017  0.0474  1070 GLY A O   
1779 N N   . GLN A 307 ? 0.6919 1.1787 0.5901 -0.3233 0.0165  0.0522  1071 GLN A N   
1780 C CA  . GLN A 307 ? 0.7186 1.1439 0.6001 -0.3419 0.0126  0.0539  1071 GLN A CA  
1781 C C   . GLN A 307 ? 0.7557 1.1384 0.6321 -0.3690 -0.0161 0.0464  1071 GLN A C   
1782 O O   . GLN A 307 ? 0.8587 1.2041 0.7184 -0.3944 -0.0240 0.0471  1071 GLN A O   
1783 C CB  . GLN A 307 ? 0.6397 1.0327 0.5221 -0.3160 0.0290  0.0578  1071 GLN A CB  
1784 C CG  . GLN A 307 ? 0.7162 1.1372 0.5978 -0.2942 0.0604  0.0667  1071 GLN A CG  
1785 C CD  . GLN A 307 ? 0.7684 1.1576 0.6531 -0.2680 0.0793  0.0692  1071 GLN A CD  
1786 O OE1 . GLN A 307 ? 0.7163 1.0656 0.6053 -0.2648 0.0685  0.0638  1071 GLN A OE1 
1787 N NE2 . GLN A 307 ? 0.7591 1.1653 0.6420 -0.2492 0.1088  0.0772  1071 GLN A NE2 
1788 N N   . ILE A 308 ? 0.6856 1.0727 0.5752 -0.3632 -0.0313 0.0395  1072 ILE A N   
1789 C CA  . ILE A 308 ? 0.6882 1.0400 0.5733 -0.3897 -0.0579 0.0325  1072 ILE A CA  
1790 C C   . ILE A 308 ? 0.7836 1.1561 0.6620 -0.4211 -0.0652 0.0303  1072 ILE A C   
1791 O O   . ILE A 308 ? 0.8028 1.1356 0.6668 -0.4490 -0.0791 0.0294  1072 ILE A O   
1792 C CB  . ILE A 308 ? 0.6429 1.0001 0.5448 -0.3760 -0.0712 0.0251  1072 ILE A CB  
1793 C CG1 . ILE A 308 ? 0.6411 0.9617 0.5465 -0.3509 -0.0669 0.0267  1072 ILE A CG1 
1794 C CG2 . ILE A 308 ? 0.7287 1.0613 0.6271 -0.4055 -0.0970 0.0174  1072 ILE A CG2 
1795 C CD1 . ILE A 308 ? 0.7308 1.0502 0.6515 -0.3370 -0.0803 0.0201  1072 ILE A CD1 
1796 N N   . ASP A 309 ? 0.8168 1.2526 0.7056 -0.4165 -0.0553 0.0292  1073 ASP A N   
1797 C CA  . ASP A 309 ? 0.7670 1.2266 0.6513 -0.4464 -0.0595 0.0261  1073 ASP A CA  
1798 C C   . ASP A 309 ? 0.8405 1.2711 0.7036 -0.4653 -0.0526 0.0339  1073 ASP A C   
1799 O O   . ASP A 309 ? 0.8443 1.2496 0.6953 -0.4963 -0.0640 0.0323  1073 ASP A O   
1800 C CB  . ASP A 309 ? 0.6660 1.2038 0.5655 -0.4342 -0.0470 0.0236  1073 ASP A CB  
1801 C CG  . ASP A 309 ? 0.7383 1.3105 0.6586 -0.4154 -0.0542 0.0149  1073 ASP A CG  
1802 O OD1 . ASP A 309 ? 0.8366 1.3699 0.7596 -0.4132 -0.0692 0.0110  1073 ASP A OD1 
1803 O OD2 . ASP A 309 ? 0.7823 1.4221 0.7160 -0.4020 -0.0450 0.0119  1073 ASP A OD2 
1804 N N   . ASP A 310 ? 0.8888 1.3212 0.7466 -0.4465 -0.0329 0.0426  1074 ASP A N   
1805 C CA  . ASP A 310 ? 0.8997 1.3022 0.7370 -0.4625 -0.0262 0.0497  1074 ASP A CA  
1806 C C   . ASP A 310 ? 0.9282 1.2615 0.7507 -0.4778 -0.0427 0.0490  1074 ASP A C   
1807 O O   . ASP A 310 ? 0.9867 1.2936 0.7915 -0.5038 -0.0486 0.0513  1074 ASP A O   
1808 C CB  . ASP A 310 ? 0.8947 1.3092 0.7308 -0.4371 -0.0011 0.0578  1074 ASP A CB  
1809 C CG  . ASP A 310 ? 0.9835 1.4675 0.8325 -0.4188 0.0167  0.0599  1074 ASP A CG  
1810 O OD1 . ASP A 310 ? 0.9337 1.4597 0.7946 -0.4244 0.0085  0.0536  1074 ASP A OD1 
1811 O OD2 . ASP A 310 ? 1.0496 1.5474 0.8969 -0.3985 0.0395  0.0675  1074 ASP A OD2 
1812 N N   . ALA A 311 ? 0.8839 1.1880 0.7128 -0.4608 -0.0499 0.0461  1075 ALA A N   
1813 C CA  . ALA A 311 ? 0.8772 1.1193 0.6934 -0.4740 -0.0676 0.0444  1075 ALA A CA  
1814 C C   . ALA A 311 ? 0.9383 1.1656 0.7494 -0.4965 -0.0873 0.0399  1075 ALA A C   
1815 O O   . ALA A 311 ? 0.9457 1.1250 0.7360 -0.5019 -0.0939 0.0425  1075 ALA A O   
1816 C CB  . ALA A 311 ? 0.8713 1.0904 0.6982 -0.4495 -0.0708 0.0410  1075 ALA A CB  
1817 N N   . LEU A 312 ? 0.9177 1.1802 0.7455 -0.4938 -0.0922 0.0336  1076 LEU A N   
1818 C CA  . LEU A 312 ? 0.8700 1.1120 0.6926 -0.4994 -0.1030 0.0296  1076 LEU A CA  
1819 C C   . LEU A 312 ? 0.9422 1.1881 0.7493 -0.5185 -0.0966 0.0331  1076 LEU A C   
1820 O O   . LEU A 312 ? 0.9579 1.1628 0.7500 -0.5259 -0.1033 0.0343  1076 LEU A O   
1821 C CB  . LEU A 312 ? 0.7455 1.0300 0.5911 -0.4926 -0.1069 0.0206  1076 LEU A CB  
1822 C CG  . LEU A 312 ? 0.7692 1.0176 0.6213 -0.4804 -0.1214 0.0150  1076 LEU A CG  
1823 C CD1 . LEU A 312 ? 0.8472 1.1439 0.7221 -0.4743 -0.1236 0.0053  1076 LEU A CD1 
1824 C CD2 . LEU A 312 ? 0.8225 1.0160 0.6580 -0.4887 -0.1288 0.0168  1076 LEU A CD2 
1825 N N   . LYS A 313 ? 0.9804 1.2775 0.7916 -0.5260 -0.0826 0.0352  1077 LYS A N   
1826 C CA  . LYS A 313 ? 1.0032 1.3070 0.8003 -0.5438 -0.0758 0.0380  1077 LYS A CA  
1827 C C   . LYS A 313 ? 1.0303 1.2773 0.8005 -0.5504 -0.0774 0.0458  1077 LYS A C   
1828 O O   . LYS A 313 ? 0.9265 1.1574 0.6814 -0.5642 -0.0778 0.0475  1077 LYS A O   
1829 C CB  . LYS A 313 ? 0.8589 1.2292 0.6662 -0.5470 -0.0587 0.0401  1077 LYS A CB  
1830 C CG  . LYS A 313 ? 1.0298 1.4133 0.8245 -0.5643 -0.0508 0.0420  1077 LYS A CG  
1831 C CD  . LYS A 313 ? 0.9385 1.3897 0.7446 -0.5630 -0.0322 0.0451  1077 LYS A CD  
1832 C CE  . LYS A 313 ? 0.8093 1.2720 0.6023 -0.5793 -0.0248 0.0462  1077 LYS A CE  
1833 N NZ  . LYS A 313 ? 0.8247 1.2983 0.6222 -0.5906 -0.0323 0.0358  1077 LYS A NZ  
1834 N N   . LEU A 314 ? 0.9966 1.2148 0.7611 -0.5405 -0.0778 0.0498  1078 LEU A N   
1835 C CA  . LEU A 314 ? 0.9842 1.1531 0.7237 -0.5446 -0.0797 0.0560  1078 LEU A CA  
1836 C C   . LEU A 314 ? 1.0069 1.1226 0.7361 -0.5411 -0.0954 0.0551  1078 LEU A C   
1837 O O   . LEU A 314 ? 1.0015 1.0858 0.7096 -0.5502 -0.0984 0.0596  1078 LEU A O   
1838 C CB  . LEU A 314 ? 0.8667 1.0281 0.6056 -0.5352 -0.0721 0.0588  1078 LEU A CB  
1839 C CG  . LEU A 314 ? 0.9314 1.1444 0.6812 -0.5365 -0.0518 0.0622  1078 LEU A CG  
1840 C CD1 . LEU A 314 ? 1.1046 1.3132 0.8637 -0.5175 -0.0421 0.0628  1078 LEU A CD1 
1841 C CD2 . LEU A 314 ? 1.0415 1.2551 0.7722 -0.5482 -0.0415 0.0683  1078 LEU A CD2 
1842 N N   . ALA A 315 ? 1.0615 1.1684 0.8056 -0.5275 -0.1049 0.0499  1079 ALA A N   
1843 C CA  . ALA A 315 ? 1.1396 1.1975 0.8760 -0.5212 -0.1184 0.0498  1079 ALA A CA  
1844 C C   . ALA A 315 ? 1.1578 1.2059 0.8853 -0.5351 -0.1215 0.0503  1079 ALA A C   
1845 O O   . ALA A 315 ? 1.1752 1.1823 0.8845 -0.5382 -0.1279 0.0547  1079 ALA A O   
1846 C CB  . ALA A 315 ? 1.1267 1.1830 0.8836 -0.5038 -0.1265 0.0434  1079 ALA A CB  
1847 N N   . ASN A 316 ? 1.2005 1.2876 0.9412 -0.5441 -0.1166 0.0454  1080 ASN A N   
1848 C CA  . ASN A 316 ? 1.2861 1.3645 1.0215 -0.5580 -0.1181 0.0438  1080 ASN A CA  
1849 C C   . ASN A 316 ? 1.2961 1.3554 1.0059 -0.5737 -0.1135 0.0515  1080 ASN A C   
1850 O O   . ASN A 316 ? 1.3678 1.3918 1.0636 -0.5809 -0.1184 0.0541  1080 ASN A O   
1851 C CB  . ASN A 316 ? 1.3165 1.4468 1.0722 -0.5650 -0.1120 0.0352  1080 ASN A CB  
1852 C CG  . ASN A 316 ? 1.2171 1.3628 0.9972 -0.5506 -0.1185 0.0265  1080 ASN A CG  
1853 O OD1 . ASN A 316 ? 1.1412 1.2758 0.9292 -0.5516 -0.1244 0.0204  1080 ASN A OD1 
1854 N ND2 . ASN A 316 ? 1.2767 1.4487 1.0693 -0.5373 -0.1168 0.0256  1080 ASN A ND2 
1855 N N   . GLU A 317 ? 1.1880 1.2703 0.8911 -0.5792 -0.1035 0.0554  1081 GLU A N   
1856 C CA  . GLU A 317 ? 1.0969 1.1674 0.7769 -0.5946 -0.0978 0.0621  1081 GLU A CA  
1857 C C   . GLU A 317 ? 1.0972 1.1287 0.7560 -0.5890 -0.1017 0.0696  1081 GLU A C   
1858 O O   . GLU A 317 ? 1.1433 1.1823 0.7911 -0.5925 -0.0941 0.0740  1081 GLU A O   
1859 C CB  . GLU A 317 ? 1.0643 1.1844 0.7493 -0.6043 -0.0840 0.0615  1081 GLU A CB  
1860 C CG  . GLU A 317 ? 1.1147 1.2737 0.8165 -0.5928 -0.0776 0.0598  1081 GLU A CG  
1861 C CD  . GLU A 317 ? 1.0158 1.2252 0.7213 -0.6016 -0.0627 0.0605  1081 GLU A CD  
1862 O OE1 . GLU A 317 ? 1.1546 1.3603 0.8448 -0.6157 -0.0577 0.0637  1081 GLU A OE1 
1863 O OE2 . GLU A 317 ? 0.9337 1.1881 0.6579 -0.5937 -0.0555 0.0581  1081 GLU A OE2 
1864 N N   . GLY A 318 ? 1.1373 1.1281 0.7909 -0.5798 -0.1136 0.0704  1082 GLY A N   
1865 C CA  . GLY A 318 ? 1.2812 1.2335 0.9136 -0.5752 -0.1192 0.0765  1082 GLY A CA  
1866 C C   . GLY A 318 ? 1.2672 1.2306 0.8978 -0.5692 -0.1128 0.0776  1082 GLY A C   
1867 O O   . GLY A 318 ? 1.2094 1.1673 0.8209 -0.5779 -0.1077 0.0827  1082 GLY A O   
1868 N N   . LYS A 319 ? 1.1158 1.0948 0.7664 -0.5547 -0.1119 0.0725  1083 LYS A N   
1869 C CA  . LYS A 319 ? 1.0973 1.0850 0.7494 -0.5479 -0.1044 0.0721  1083 LYS A CA  
1870 C C   . LYS A 319 ? 1.1365 1.1054 0.7998 -0.5291 -0.1117 0.0674  1083 LYS A C   
1871 O O   . LYS A 319 ? 1.1774 1.1666 0.8581 -0.5200 -0.1052 0.0632  1083 LYS A O   
1872 C CB  . LYS A 319 ? 1.1136 1.1511 0.7812 -0.5516 -0.0898 0.0706  1083 LYS A CB  
1873 C CG  . LYS A 319 ? 1.1955 1.2552 0.8530 -0.5689 -0.0807 0.0746  1083 LYS A CG  
1874 C CD  . LYS A 319 ? 1.1916 1.3020 0.8636 -0.5698 -0.0645 0.0741  1083 LYS A CD  
1875 C CE  . LYS A 319 ? 1.1376 1.2709 0.8001 -0.5852 -0.0552 0.0776  1083 LYS A CE  
1876 N NZ  . LYS A 319 ? 1.1772 1.3601 0.8527 -0.5829 -0.0375 0.0785  1083 LYS A NZ  
1877 N N   . VAL A 320 ? 1.1378 1.0680 0.7914 -0.5231 -0.1246 0.0682  1084 VAL A N   
1878 C CA  . VAL A 320 ? 1.0911 1.0028 0.7565 -0.5042 -0.1323 0.0632  1084 VAL A CA  
1879 C C   . VAL A 320 ? 1.1211 1.0353 0.7888 -0.4972 -0.1246 0.0598  1084 VAL A C   
1880 O O   . VAL A 320 ? 1.1188 1.0423 0.8061 -0.4844 -0.1220 0.0538  1084 VAL A O   
1881 C CB  . VAL A 320 ? 1.0806 0.9516 0.7315 -0.5005 -0.1461 0.0658  1084 VAL A CB  
1882 C CG1 . VAL A 320 ? 1.2207 1.0746 0.8844 -0.4801 -0.1535 0.0600  1084 VAL A CG1 
1883 C CG2 . VAL A 320 ? 1.2355 1.1030 0.8857 -0.5082 -0.1515 0.0682  1084 VAL A CG2 
1884 N N   . LYS A 321 ? 1.1685 1.0742 0.8163 -0.5060 -0.1200 0.0629  1085 LYS A N   
1885 C CA  . LYS A 321 ? 1.0893 0.9950 0.7389 -0.5003 -0.1114 0.0581  1085 LYS A CA  
1886 C C   . LYS A 321 ? 1.1235 1.0660 0.7918 -0.5005 -0.0952 0.0556  1085 LYS A C   
1887 O O   . LYS A 321 ? 1.1216 1.0660 0.8050 -0.4894 -0.0890 0.0493  1085 LYS A O   
1888 C CB  . LYS A 321 ? 1.1445 1.0377 0.7686 -0.5118 -0.1088 0.0618  1085 LYS A CB  
1889 C CG  . LYS A 321 ? 1.2141 1.0708 0.8187 -0.5106 -0.1239 0.0640  1085 LYS A CG  
1890 C CD  . LYS A 321 ? 1.3074 1.1454 0.9218 -0.4930 -0.1301 0.0557  1085 LYS A CD  
1891 C CE  . LYS A 321 ? 1.2884 1.0938 0.8826 -0.4922 -0.1445 0.0582  1085 LYS A CE  
1892 N NZ  . LYS A 321 ? 1.2839 1.0740 0.8911 -0.4734 -0.1516 0.0496  1085 LYS A NZ  
1893 N N   . GLU A 322 ? 1.0347 1.0078 0.7028 -0.5130 -0.0867 0.0607  1086 GLU A N   
1894 C CA  . GLU A 322 ? 1.0268 1.0401 0.7125 -0.5134 -0.0691 0.0603  1086 GLU A CA  
1895 C C   . GLU A 322 ? 1.0280 1.0639 0.7378 -0.5057 -0.0718 0.0573  1086 GLU A C   
1896 O O   . GLU A 322 ? 1.0332 1.0948 0.7614 -0.4997 -0.0584 0.0559  1086 GLU A O   
1897 C CB  . GLU A 322 ? 1.0004 1.0428 0.6776 -0.5281 -0.0575 0.0668  1086 GLU A CB  
1898 C CG  . GLU A 322 ? 1.0181 1.1008 0.7095 -0.5254 -0.0339 0.0689  1086 GLU A CG  
1899 C CD  . GLU A 322 ? 1.0419 1.1637 0.7320 -0.5352 -0.0239 0.0747  1086 GLU A CD  
1900 O OE1 . GLU A 322 ? 1.1817 1.2986 0.8613 -0.5469 -0.0357 0.0758  1086 GLU A OE1 
1901 O OE2 . GLU A 322 ? 1.0103 1.1678 0.7098 -0.5287 -0.0025 0.0782  1086 GLU A OE2 
1902 N N   . ALA A 323 ? 1.0580 1.0859 0.7685 -0.5056 -0.0868 0.0569  1087 ALA A N   
1903 C CA  . ALA A 323 ? 0.9731 1.0225 0.7063 -0.4976 -0.0907 0.0528  1087 ALA A CA  
1904 C C   . ALA A 323 ? 1.0369 1.0700 0.7835 -0.4805 -0.0933 0.0471  1087 ALA A C   
1905 O O   . ALA A 323 ? 1.0459 1.1072 0.8133 -0.4744 -0.0877 0.0442  1087 ALA A O   
1906 C CB  . ALA A 323 ? 1.0059 1.0431 0.7365 -0.4997 -0.1049 0.0525  1087 ALA A CB  
1907 N N   . GLN A 324 ? 1.1242 1.1145 0.8597 -0.4727 -0.1014 0.0451  1088 GLN A N   
1908 C CA  . GLN A 324 ? 1.0582 1.0314 0.8061 -0.4563 -0.1027 0.0384  1088 GLN A CA  
1909 C C   . GLN A 324 ? 1.0625 1.0552 0.8198 -0.4571 -0.0828 0.0367  1088 GLN A C   
1910 O O   . GLN A 324 ? 1.0076 1.0064 0.7835 -0.4403 -0.0764 0.0324  1088 GLN A O   
1911 C CB  . GLN A 324 ? 0.9706 0.9001 0.7046 -0.4488 -0.1136 0.0365  1088 GLN A CB  
1912 C CG  . GLN A 324 ? 1.0053 0.9141 0.7336 -0.4458 -0.1303 0.0390  1088 GLN A CG  
1913 C CD  . GLN A 324 ? 1.1252 0.9999 0.8329 -0.4460 -0.1385 0.0411  1088 GLN A CD  
1914 O OE1 . GLN A 324 ? 1.2832 1.1550 0.9745 -0.4555 -0.1327 0.0431  1088 GLN A OE1 
1915 N NE2 . GLN A 324 ? 1.1956 1.0464 0.9040 -0.4358 -0.1517 0.0406  1088 GLN A NE2 
1916 N N   . ALA A 325 ? 0.9199 0.9222 0.6651 -0.4688 -0.0690 0.0409  1089 ALA A N   
1917 C CA  . ALA A 325 ? 0.9424 0.9634 0.6967 -0.4510 -0.0426 0.0407  1089 ALA A CA  
1918 C C   . ALA A 325 ? 0.9066 0.9704 0.6814 -0.4326 -0.0284 0.0436  1089 ALA A C   
1919 O O   . ALA A 325 ? 0.9214 0.9921 0.7113 -0.4084 -0.0115 0.0413  1089 ALA A O   
1920 C CB  . ALA A 325 ? 1.0083 1.0354 0.7452 -0.4639 -0.0300 0.0457  1089 ALA A CB  
1921 N N   . ALA A 326 ? 0.9296 1.0237 0.7054 -0.4432 -0.0342 0.0483  1090 ALA A N   
1922 C CA  . ALA A 326 ? 0.8487 0.9886 0.6437 -0.4253 -0.0228 0.0502  1090 ALA A CA  
1923 C C   . ALA A 326 ? 0.7608 0.8940 0.5733 -0.4071 -0.0315 0.0446  1090 ALA A C   
1924 O O   . ALA A 326 ? 0.7990 0.9597 0.6283 -0.3818 -0.0161 0.0454  1090 ALA A O   
1925 C CB  . ALA A 326 ? 0.9051 1.0795 0.6979 -0.4433 -0.0293 0.0536  1090 ALA A CB  
1926 N N   . ALA A 327 ? 0.7875 0.8845 0.5958 -0.4187 -0.0554 0.0395  1091 ALA A N   
1927 C CA  . ALA A 327 ? 0.7974 0.8844 0.6216 -0.4018 -0.0644 0.0339  1091 ALA A CA  
1928 C C   . ALA A 327 ? 0.8030 0.8744 0.6362 -0.3771 -0.0479 0.0309  1091 ALA A C   
1929 O O   . ALA A 327 ? 0.8274 0.9091 0.6784 -0.3540 -0.0425 0.0289  1091 ALA A O   
1930 C CB  . ALA A 327 ? 0.8642 0.9115 0.6798 -0.4197 -0.0925 0.0295  1091 ALA A CB  
1931 N N   . GLU A 328 ? 0.8120 0.8592 0.6337 -0.3815 -0.0389 0.0300  1092 GLU A N   
1932 C CA  . GLU A 328 ? 0.7750 0.8052 0.6058 -0.3606 -0.0215 0.0251  1092 GLU A CA  
1933 C C   . GLU A 328 ? 0.8101 0.8741 0.6516 -0.3382 0.0103  0.0302  1092 GLU A C   
1934 O O   . GLU A 328 ? 0.8434 0.8993 0.6979 -0.3155 0.0275  0.0269  1092 GLU A O   
1935 C CB  . GLU A 328 ? 0.8827 0.8764 0.6979 -0.3740 -0.0235 0.0199  1092 GLU A CB  
1936 C CG  . GLU A 328 ? 1.0215 0.9805 0.8233 -0.3942 -0.0538 0.0159  1092 GLU A CG  
1937 C CD  . GLU A 328 ? 0.9234 0.8609 0.7379 -0.3831 -0.0684 0.0089  1092 GLU A CD  
1938 O OE1 . GLU A 328 ? 0.8712 0.8157 0.7047 -0.3596 -0.0537 0.0060  1092 GLU A OE1 
1939 O OE2 . GLU A 328 ? 0.9405 0.8534 0.7457 -0.3963 -0.0935 0.0070  1092 GLU A OE2 
1940 N N   . GLN A 329 ? 0.7421 0.8436 0.5787 -0.3434 0.0197  0.0383  1093 GLN A N   
1941 C CA  . GLN A 329 ? 0.7309 0.8687 0.5781 -0.3192 0.0494  0.0444  1093 GLN A CA  
1942 C C   . GLN A 329 ? 0.7380 0.9064 0.6031 -0.2972 0.0498  0.0463  1093 GLN A C   
1943 O O   . GLN A 329 ? 0.7482 0.9392 0.6245 -0.2696 0.0750  0.0506  1093 GLN A O   
1944 C CB  . GLN A 329 ? 0.8693 1.0398 0.7052 -0.3309 0.0599  0.0523  1093 GLN A CB  
1945 C CG  . GLN A 329 ? 0.8780 1.0851 0.7133 -0.3442 0.0444  0.0560  1093 GLN A CG  
1946 C CD  . GLN A 329 ? 0.8536 1.1087 0.6871 -0.3409 0.0640  0.0643  1093 GLN A CD  
1947 O OE1 . GLN A 329 ? 0.7201 0.9772 0.5494 -0.3321 0.0880  0.0684  1093 GLN A OE1 
1948 N NE2 . GLN A 329 ? 0.7707 1.0659 0.6080 -0.3481 0.0545  0.0660  1093 GLN A NE2 
1949 N N   . LEU A 330 ? 0.8076 0.9771 0.6753 -0.3079 0.0233  0.0432  1094 LEU A N   
1950 C CA  . LEU A 330 ? 0.7679 0.9651 0.6532 -0.2868 0.0218  0.0432  1094 LEU A CA  
1951 C C   . LEU A 330 ? 0.8331 1.0105 0.7316 -0.2580 0.0361  0.0408  1094 LEU A C   
1952 O O   . LEU A 330 ? 0.9166 1.1237 0.8292 -0.2305 0.0499  0.0443  1094 LEU A O   
1953 C CB  . LEU A 330 ? 0.7643 0.9548 0.6500 -0.3049 -0.0100 0.0379  1094 LEU A CB  
1954 C CG  . LEU A 330 ? 0.6552 0.8603 0.5287 -0.3357 -0.0253 0.0389  1094 LEU A CG  
1955 C CD1 . LEU A 330 ? 0.6533 0.8492 0.5297 -0.3504 -0.0536 0.0328  1094 LEU A CD1 
1956 C CD2 . LEU A 330 ? 0.8641 1.1280 0.7413 -0.3300 -0.0091 0.0449  1094 LEU A CD2 
1957 N N   . LYS A 331 ? 0.8548 0.9836 0.7491 -0.2634 0.0341  0.0346  1095 LYS A N   
1958 C CA  . LYS A 331 ? 0.8705 0.9776 0.7781 -0.2380 0.0496  0.0308  1095 LYS A CA  
1959 C C   . LYS A 331 ? 0.8715 1.0042 0.7863 -0.2105 0.0865  0.0380  1095 LYS A C   
1960 O O   . LYS A 331 ? 0.8200 0.9572 0.7494 -0.1816 0.1020  0.0392  1095 LYS A O   
1961 C CB  . LYS A 331 ? 0.8493 0.9051 0.7502 -0.2509 0.0444  0.0216  1095 LYS A CB  
1962 C CG  . LYS A 331 ? 0.7839 0.8107 0.6775 -0.2736 0.0093  0.0150  1095 LYS A CG  
1963 C CD  . LYS A 331 ? 0.8552 0.8367 0.7410 -0.2852 0.0049  0.0055  1095 LYS A CD  
1964 C CE  . LYS A 331 ? 0.9920 0.9438 0.8713 -0.3027 -0.0288 -0.0004 1095 LYS A CE  
1965 N NZ  . LYS A 331 ? 1.0534 0.9662 0.9232 -0.3143 -0.0345 -0.0098 1095 LYS A NZ  
1966 N N   . THR A 332 ? 0.7512 0.9001 0.6552 -0.2181 0.1020  0.0435  1096 THR A N   
1967 C CA  . THR A 332 ? 0.7900 0.9634 0.6992 -0.1918 0.1384  0.0514  1096 THR A CA  
1968 C C   . THR A 332 ? 0.8401 1.0620 0.7605 -0.1668 0.1443  0.0594  1096 THR A C   
1969 O O   . THR A 332 ? 0.7563 0.9858 0.6881 -0.1344 0.1689  0.0635  1096 THR A O   
1970 C CB  . THR A 332 ? 0.6839 0.8705 0.5784 -0.2066 0.1506  0.0564  1096 THR A CB  
1971 O OG1 . THR A 332 ? 0.8361 1.0607 0.7237 -0.2224 0.1337  0.0614  1096 THR A OG1 
1972 C CG2 . THR A 332 ? 0.7922 0.9345 0.6744 -0.2321 0.1423  0.0478  1096 THR A CG2 
1973 N N   . THR A 333 ? 0.8126 1.0685 0.7299 -0.1811 0.1226  0.0611  1097 THR A N   
1974 C CA  . THR A 333 ? 0.8079 1.1141 0.7363 -0.1585 0.1251  0.0663  1097 THR A CA  
1975 C C   . THR A 333 ? 0.8312 1.1232 0.7730 -0.1456 0.1107  0.0607  1097 THR A C   
1976 O O   . THR A 333 ? 0.8140 1.1307 0.7678 -0.1134 0.1252  0.0651  1097 THR A O   
1977 C CB  . THR A 333 ? 0.6612 1.0100 0.5839 -0.1797 0.1071  0.0673  1097 THR A CB  
1978 O OG1 . THR A 333 ? 0.6879 1.0066 0.6033 -0.2140 0.0750  0.0591  1097 THR A OG1 
1979 C CG2 . THR A 333 ? 0.6916 1.0643 0.6032 -0.1857 0.1260  0.0746  1097 THR A CG2 
1980 N N   . ARG A 334 ? 0.8312 1.0831 0.7703 -0.1692 0.0827  0.0515  1098 ARG A N   
1981 C CA  . ARG A 334 ? 0.7854 1.0231 0.7365 -0.1593 0.0666  0.0458  1098 ARG A CA  
1982 C C   . ARG A 334 ? 0.8509 1.0672 0.8133 -0.1276 0.0905  0.0466  1098 ARG A C   
1983 O O   . ARG A 334 ? 0.8604 1.0898 0.8358 -0.1032 0.0919  0.0473  1098 ARG A O   
1984 C CB  . ARG A 334 ? 0.8712 1.0652 0.8152 -0.1902 0.0347  0.0364  1098 ARG A CB  
1985 C CG  . ARG A 334 ? 0.7749 0.9510 0.7306 -0.1819 0.0165  0.0301  1098 ARG A CG  
1986 C CD  . ARG A 334 ? 0.8014 0.9236 0.7597 -0.1771 0.0198  0.0240  1098 ARG A CD  
1987 N NE  . ARG A 334 ? 0.8746 0.9568 0.8186 -0.2079 0.0019  0.0178  1098 ARG A NE  
1988 C CZ  . ARG A 334 ? 0.8692 0.9050 0.8131 -0.2108 -0.0014 0.0101  1098 ARG A CZ  
1989 N NH1 . ARG A 334 ? 0.8350 0.8547 0.7931 -0.1865 0.0124  0.0068  1098 ARG A NH1 
1990 N NH2 . ARG A 334 ? 0.7551 0.7608 0.6840 -0.2383 -0.0184 0.0052  1098 ARG A NH2 
1991 N N   . ASN A 335 ? 0.8717 1.0552 0.8297 -0.1276 0.1104  0.0457  1099 ASN A N   
1992 C CA  . ASN A 335 ? 0.9380 1.1010 0.9074 -0.0977 0.1381  0.0460  1099 ASN A CA  
1993 C C   . ASN A 335 ? 0.9061 1.1140 0.8829 -0.0619 0.1669  0.0578  1099 ASN A C   
1994 O O   . ASN A 335 ? 0.7995 1.0062 0.7889 -0.0321 0.1800  0.0597  1099 ASN A O   
1995 C CB  . ASN A 335 ? 0.9480 1.0725 0.9114 -0.1066 0.1565  0.0416  1099 ASN A CB  
1996 C CG  . ASN A 335 ? 0.8681 0.9450 0.8269 -0.1339 0.1311  0.0288  1099 ASN A CG  
1997 O OD1 . ASN A 335 ? 0.6908 0.7563 0.6534 -0.1408 0.1036  0.0235  1099 ASN A OD1 
1998 N ND2 . ASN A 335 ? 0.9750 1.0250 0.9256 -0.1487 0.1406  0.0234  1099 ASN A ND2 
1999 N N   . ALA A 336 ? 1.0182 1.2667 0.9867 -0.0630 0.1777  0.0662  1100 ALA A N   
2000 C CA  . ALA A 336 ? 1.0090 1.3077 0.9830 -0.0288 0.2019  0.0779  1100 ALA A CA  
2001 C C   . ALA A 336 ? 1.0686 1.4097 1.0498 -0.0219 0.1798  0.0781  1100 ALA A C   
2002 O O   . ALA A 336 ? 1.1351 1.5088 1.1251 0.0130  0.1959  0.0852  1100 ALA A O   
2003 C CB  . ALA A 336 ? 1.0856 1.4167 1.0484 -0.0325 0.2196  0.0863  1100 ALA A CB  
2004 N N   . TYR A 337 ? 0.9460 1.2875 0.9235 -0.0540 0.1440  0.0701  1101 TYR A N   
2005 C CA  . TYR A 337 ? 0.9006 1.2817 0.8859 -0.0509 0.1221  0.0677  1101 TYR A CA  
2006 C C   . TYR A 337 ? 0.8609 1.2216 0.8593 -0.0303 0.1171  0.0640  1101 TYR A C   
2007 O O   . TYR A 337 ? 0.8640 1.2648 0.8720 -0.0039 0.1199  0.0672  1101 TYR A O   
2008 C CB  . TYR A 337 ? 0.8943 1.2731 0.8723 -0.0923 0.0874  0.0593  1101 TYR A CB  
2009 C CG  . TYR A 337 ? 0.9471 1.3892 0.9277 -0.0961 0.0756  0.0591  1101 TYR A CG  
2010 C CD1 . TYR A 337 ? 0.9027 1.3892 0.8769 -0.0987 0.0887  0.0651  1101 TYR A CD1 
2011 C CD2 . TYR A 337 ? 1.0317 1.4903 1.0221 -0.0980 0.0516  0.0517  1101 TYR A CD2 
2012 C CE1 . TYR A 337 ? 0.8457 1.3930 0.8238 -0.1031 0.0783  0.0630  1101 TYR A CE1 
2013 C CE2 . TYR A 337 ? 0.8950 1.4138 0.8895 -0.1028 0.0414  0.0490  1101 TYR A CE2 
2014 C CZ  . TYR A 337 ? 0.8239 1.3875 0.8125 -0.1056 0.0548  0.0543  1101 TYR A CZ  
2015 O OH  . TYR A 337 ? 0.8775 1.5039 0.8716 -0.1110 0.0451  0.0498  1101 TYR A OH  
2016 N N   . ILE A 338 ? 0.8579 1.1585 0.8568 -0.0412 0.1096  0.0570  1102 ILE A N   
2017 C CA  . ILE A 338 ? 0.8488 1.1270 0.8601 -0.0237 0.1035  0.0528  1102 ILE A CA  
2018 C C   . ILE A 338 ? 0.8938 1.1786 0.9141 0.0195  0.1396  0.0614  1102 ILE A C   
2019 O O   . ILE A 338 ? 0.9114 1.2127 0.9425 0.0459  0.1405  0.0632  1102 ILE A O   
2020 C CB  . ILE A 338 ? 0.8695 1.0832 0.8787 -0.0474 0.0862  0.0423  1102 ILE A CB  
2021 C CG1 . ILE A 338 ? 0.8871 1.0794 0.9093 -0.0324 0.0754  0.0370  1102 ILE A CG1 
2022 C CG2 . ILE A 338 ? 0.9033 1.0797 0.9083 -0.0465 0.1120  0.0425  1102 ILE A CG2 
2023 C CD1 . ILE A 338 ? 0.8715 1.0944 0.8984 -0.0368 0.0469  0.0340  1102 ILE A CD1 
2024 N N   . GLN A 339 ? 1.0043 1.2761 1.0199 0.0280  0.1711  0.0671  1103 GLN A N   
2025 C CA  . GLN A 339 ? 0.9135 1.1858 0.9367 0.0689  0.2094  0.0759  1103 GLN A CA  
2026 C C   . GLN A 339 ? 0.8296 1.1660 0.8556 0.1017  0.2222  0.0875  1103 GLN A C   
2027 O O   . GLN A 339 ? 0.8375 1.1790 0.8706 0.1404  0.2502  0.0956  1103 GLN A O   
2028 C CB  . GLN A 339 ? 0.9249 1.1726 0.9415 0.0686  0.2413  0.0791  1103 GLN A CB  
2029 N N   . LYS A 340 ? 0.7640 1.1506 0.7847 0.0877  0.2033  0.0881  1104 LYS A N   
2030 C CA  . LYS A 340 ? 0.7448 1.1993 0.7683 0.1181  0.2140  0.0976  1104 LYS A CA  
2031 C C   . LYS A 340 ? 0.7199 1.1948 0.7548 0.1328  0.1945  0.0935  1104 LYS A C   
2032 O O   . LYS A 340 ? 0.7255 1.2316 0.7666 0.1732  0.2138  0.1020  1104 LYS A O   
2033 C CB  . LYS A 340 ? 0.7975 1.3005 0.8120 0.0965  0.2029  0.0981  1104 LYS A CB  
2034 C CG  . LYS A 340 ? 0.8360 1.4117 0.8508 0.1291  0.2226  0.1092  1104 LYS A CG  
2035 C CD  . LYS A 340 ? 0.7624 1.3880 0.7705 0.1039  0.2069  0.1068  1104 LYS A CD  
2036 C CE  . LYS A 340 ? 0.7624 1.4156 0.7775 0.0832  0.1689  0.0945  1104 LYS A CE  
2037 N NZ  . LYS A 340 ? 0.6174 1.3122 0.6269 0.0533  0.1534  0.0898  1104 LYS A NZ  
2038 N N   . TYR A 341 ? 0.8256 1.2826 0.8629 0.1015  0.1572  0.0809  1105 TYR A N   
2039 C CA  . TYR A 341 ? 0.6096 1.0890 0.6576 0.1119  0.1363  0.0757  1105 TYR A CA  
2040 C C   . TYR A 341 ? 0.7420 1.1917 0.7997 0.1454  0.1522  0.0789  1105 TYR A C   
2041 O O   . TYR A 341 ? 0.7903 1.2750 0.8563 0.1750  0.1535  0.0817  1105 TYR A O   
2042 C CB  . TYR A 341 ? 0.5514 1.0085 0.5989 0.0700  0.0954  0.0617  1105 TYR A CB  
2043 N N   . LEU A 342 ? 0.7187 1.1050 0.7757 0.1412  0.1649  0.0778  1106 LEU A N   
2044 C CA  . LEU A 342 ? 0.6378 0.9903 0.7050 0.1697  0.1801  0.0792  1106 LEU A CA  
2045 C C   . LEU A 342 ? 0.5844 0.9746 0.6549 0.2193  0.2158  0.0936  1106 LEU A C   
2046 O O   . LEU A 342 ? 0.5640 0.9606 0.6437 0.2482  0.2187  0.0958  1106 LEU A O   
2047 C CB  . LEU A 342 ? 0.7845 1.0682 0.8505 0.1564  0.1929  0.0749  1106 LEU A CB  
2048 C CG  . LEU A 342 ? 0.8102 1.0530 0.8715 0.1103  0.1595  0.0612  1106 LEU A CG  
2049 C CD1 . LEU A 342 ? 0.9893 1.1739 1.0489 0.0997  0.1765  0.0567  1106 LEU A CD1 
2050 C CD2 . LEU A 342 ? 0.7142 0.9435 0.7836 0.1029  0.1271  0.0519  1106 LEU A CD2 
2051 N N   . ALA A 343 ? 0.8445 1.0644 0.4414 0.0116  0.2105  -0.1323 900  ALA A N   
2052 C CA  . ALA A 343 ? 0.8178 1.0024 0.4158 0.0308  0.2213  -0.1441 900  ALA A CA  
2053 C C   . ALA A 343 ? 0.8831 1.0913 0.5438 0.0359  0.2223  -0.1308 900  ALA A C   
2054 O O   . ALA A 343 ? 0.8799 1.0684 0.5580 0.0421  0.2176  -0.1335 900  ALA A O   
2055 C CB  . ALA A 343 ? 1.0359 1.1919 0.5894 0.0491  0.2471  -0.1609 900  ALA A CB  
2056 N N   . HIS A 344 ? 0.9469 1.1996 0.6418 0.0331  0.2266  -0.1172 270  HIS A N   
2057 C CA  . HIS A 344 ? 0.8687 1.1478 0.6227 0.0387  0.2245  -0.1062 270  HIS A CA  
2058 C C   . HIS A 344 ? 0.8186 1.1045 0.6070 0.0278  0.1999  -0.0956 270  HIS A C   
2059 O O   . HIS A 344 ? 0.7808 1.0600 0.5985 0.0358  0.1969  -0.0947 270  HIS A O   
2060 C CB  . HIS A 344 ? 0.8375 1.1634 0.6189 0.0365  0.2292  -0.0928 270  HIS A CB  
2061 C CG  . HIS A 344 ? 0.9581 1.3082 0.7942 0.0452  0.2274  -0.0836 270  HIS A CG  
2062 N ND1 . HIS A 344 ? 0.9621 1.3557 0.8362 0.0391  0.2176  -0.0659 270  HIS A ND1 
2063 C CD2 . HIS A 344 ? 0.8999 1.2352 0.7567 0.0596  0.2326  -0.0896 270  HIS A CD2 
2064 C CE1 . HIS A 344 ? 0.8695 1.2724 0.7830 0.0497  0.2160  -0.0617 270  HIS A CE1 
2065 N NE2 . HIS A 344 ? 0.9017 1.2712 0.8067 0.0619  0.2251  -0.0757 270  HIS A NE2 
2066 N N   . LEU A 345 ? 0.7827 1.0823 0.5685 0.0088  0.1823  -0.0875 271  LEU A N   
2067 C CA  . LEU A 345 ? 0.7628 1.0675 0.5798 -0.0029 0.1603  -0.0789 271  LEU A CA  
2068 C C   . LEU A 345 ? 0.6758 0.9356 0.4726 0.0023  0.1595  -0.0917 271  LEU A C   
2069 O O   . LEU A 345 ? 0.6281 0.8846 0.4545 0.0020  0.1495  -0.0873 271  LEU A O   
2070 C CB  . LEU A 345 ? 0.7776 1.1054 0.5953 -0.0254 0.1430  -0.0691 271  LEU A CB  
2071 C CG  . LEU A 345 ? 0.7104 1.0864 0.5657 -0.0333 0.1338  -0.0509 271  LEU A CG  
2072 C CD1 . LEU A 345 ? 0.7126 1.1035 0.5594 -0.0218 0.1528  -0.0506 271  LEU A CD1 
2073 C CD2 . LEU A 345 ? 0.6397 1.0345 0.4926 -0.0560 0.1168  -0.0422 271  LEU A CD2 
2074 N N   . ALA A 346 ? 0.7118 0.9354 0.4556 0.0074  0.1687  -0.1080 272  ALA A N   
2075 C CA  . ALA A 346 ? 0.8577 1.0395 0.5801 0.0147  0.1678  -0.1225 272  ALA A CA  
2076 C C   . ALA A 346 ? 0.8020 0.9665 0.5451 0.0343  0.1798  -0.1229 272  ALA A C   
2077 O O   . ALA A 346 ? 0.8452 0.9903 0.5996 0.0369  0.1728  -0.1240 272  ALA A O   
2078 C CB  . ALA A 346 ? 0.9090 1.0573 0.5697 0.0190  0.1746  -0.1426 272  ALA A CB  
2079 N N   . ALA A 347 ? 0.7428 0.9211 0.4942 0.0461  0.1974  -0.1235 273  ALA A N   
2080 C CA  . ALA A 347 ? 0.6688 0.8435 0.4499 0.0611  0.2068  -0.1243 273  ALA A CA  
2081 C C   . ALA A 347 ? 0.5901 0.7970 0.4264 0.0550  0.1906  -0.1073 273  ALA A C   
2082 O O   . ALA A 347 ? 0.6836 0.8771 0.5400 0.0624  0.1884  -0.1072 273  ALA A O   
2083 C CB  . ALA A 347 ? 0.7035 0.8920 0.4860 0.0731  0.2283  -0.1293 273  ALA A CB  
2084 N N   . THR A 348 ? 0.6232 0.8706 0.4825 0.0416  0.1783  -0.0930 274  THR A N   
2085 C CA  . THR A 348 ? 0.6689 0.9430 0.5756 0.0357  0.1605  -0.0776 274  THR A CA  
2086 C C   . THR A 348 ? 0.5763 0.8307 0.4854 0.0268  0.1456  -0.0766 274  THR A C   
2087 O O   . THR A 348 ? 0.5303 0.7808 0.4653 0.0308  0.1385  -0.0718 274  THR A O   
2088 C CB  . THR A 348 ? 0.5962 0.9135 0.5219 0.0230  0.1496  -0.0634 274  THR A CB  
2089 O OG1 . THR A 348 ? 0.6702 1.0076 0.5982 0.0323  0.1640  -0.0626 274  THR A OG1 
2090 C CG2 . THR A 348 ? 0.5140 0.8506 0.4799 0.0168  0.1284  -0.0487 274  THR A CG2 
2091 N N   . ARG A 349 ? 0.5736 0.8149 0.4550 0.0142  0.1405  -0.0814 275  ARG A N   
2092 C CA  . ARG A 349 ? 0.5757 0.8010 0.4614 0.0040  0.1267  -0.0806 275  ARG A CA  
2093 C C   . ARG A 349 ? 0.5768 0.7611 0.4505 0.0185  0.1339  -0.0897 275  ARG A C   
2094 O O   . ARG A 349 ? 0.6322 0.8119 0.5287 0.0170  0.1252  -0.0842 275  ARG A O   
2095 C CB  . ARG A 349 ? 0.6989 0.9176 0.5550 -0.0126 0.1200  -0.0862 275  ARG A CB  
2096 C CG  . ARG A 349 ? 0.6661 0.9247 0.5409 -0.0315 0.1075  -0.0741 275  ARG A CG  
2097 C CD  . ARG A 349 ? 0.6437 0.9045 0.5034 -0.0550 0.0954  -0.0795 275  ARG A CD  
2098 N NE  . ARG A 349 ? 0.7261 1.0256 0.6044 -0.0740 0.0825  -0.0669 275  ARG A NE  
2099 C CZ  . ARG A 349 ? 0.6859 1.0009 0.5423 -0.0799 0.0853  -0.0666 275  ARG A CZ  
2100 N NH1 . ARG A 349 ? 0.7342 1.0279 0.5467 -0.0681 0.1009  -0.0793 275  ARG A NH1 
2101 N NH2 . ARG A 349 ? 0.7143 1.0648 0.5910 -0.0975 0.0715  -0.0533 275  ARG A NH2 
2102 N N   . LYS A 350 ? 0.5148 0.6669 0.3505 0.0328  0.1495  -0.1039 276  LYS A N   
2103 C CA  . LYS A 350 ? 0.5671 0.6775 0.3895 0.0476  0.1560  -0.1127 276  LYS A CA  
2104 C C   . LYS A 350 ? 0.5821 0.7059 0.4454 0.0569  0.1594  -0.1050 276  LYS A C   
2105 O O   . LYS A 350 ? 0.6320 0.7371 0.5053 0.0601  0.1548  -0.1033 276  LYS A O   
2106 C CB  . LYS A 350 ? 0.7135 0.7874 0.4883 0.0615  0.1717  -0.1304 276  LYS A CB  
2107 C CG  . LYS A 350 ? 0.8680 0.9301 0.5993 0.0527  0.1641  -0.1434 276  LYS A CG  
2108 C CD  . LYS A 350 ? 0.8793 0.9286 0.6090 0.0407  0.1455  -0.1472 276  LYS A CD  
2109 C CE  . LYS A 350 ? 0.9240 1.0116 0.6801 0.0138  0.1307  -0.1359 276  LYS A CE  
2110 N NZ  . LYS A 350 ? 0.8653 0.9393 0.6230 -0.0033 0.1160  -0.1407 276  LYS A NZ  
2111 N N   . GLY A 351 ? 0.5349 0.6923 0.4219 0.0609  0.1654  -0.1004 277  GLY A N   
2112 C CA  . GLY A 351 ? 0.5303 0.7052 0.4578 0.0690  0.1636  -0.0931 277  GLY A CA  
2113 C C   . GLY A 351 ? 0.4874 0.6778 0.4452 0.0589  0.1437  -0.0788 277  GLY A C   
2114 O O   . GLY A 351 ? 0.5309 0.7126 0.5068 0.0647  0.1397  -0.0760 277  GLY A O   
2115 N N   . VAL A 352 ? 0.4771 0.6901 0.4403 0.0429  0.1307  -0.0702 278  VAL A N   
2116 C CA  . VAL A 352 ? 0.4950 0.7179 0.4828 0.0318  0.1118  -0.0588 278  VAL A CA  
2117 C C   . VAL A 352 ? 0.4142 0.6038 0.3881 0.0281  0.1100  -0.0636 278  VAL A C   
2118 O O   . VAL A 352 ? 0.3462 0.5288 0.3367 0.0276  0.1020  -0.0580 278  VAL A O   
2119 C CB  . VAL A 352 ? 0.5122 0.7667 0.5091 0.0153  0.0980  -0.0498 278  VAL A CB  
2120 C CG1 . VAL A 352 ? 0.5202 0.7768 0.5352 0.0038  0.0788  -0.0406 278  VAL A CG1 
2121 C CG2 . VAL A 352 ? 0.5643 0.8498 0.5741 0.0201  0.0989  -0.0429 278  VAL A CG2 
2122 N N   . ARG A 353 ? 0.5041 0.6704 0.4431 0.0258  0.1169  -0.0744 279  ARG A N   
2123 C CA  . ARG A 353 ? 0.4614 0.5939 0.3823 0.0232  0.1138  -0.0797 279  ARG A CA  
2124 C C   . ARG A 353 ? 0.4147 0.5160 0.3317 0.0404  0.1212  -0.0825 279  ARG A C   
2125 O O   . ARG A 353 ? 0.3998 0.4872 0.3228 0.0385  0.1142  -0.0790 279  ARG A O   
2126 C CB  . ARG A 353 ? 0.5182 0.6297 0.3965 0.0196  0.1170  -0.0942 279  ARG A CB  
2127 C CG  . ARG A 353 ? 0.5650 0.6994 0.4473 -0.0061 0.1047  -0.0940 279  ARG A CG  
2128 C CD  . ARG A 353 ? 0.6040 0.7370 0.5070 -0.0216 0.0933  -0.0904 279  ARG A CD  
2129 N NE  . ARG A 353 ? 0.6173 0.7821 0.5608 -0.0312 0.0821  -0.0732 279  ARG A NE  
2130 C CZ  . ARG A 353 ? 0.5649 0.7275 0.5314 -0.0387 0.0727  -0.0660 279  ARG A CZ  
2131 N NH1 . ARG A 353 ? 0.5077 0.6441 0.4658 -0.0400 0.0755  -0.0734 279  ARG A NH1 
2132 N NH2 . ARG A 353 ? 0.5497 0.7361 0.5426 -0.0460 0.0588  -0.0547 279  ARG A NH2 
2133 N N   . THR A 354 ? 0.5735 0.6634 0.4814 0.0558  0.1358  -0.0896 280  THR A N   
2134 C CA  . THR A 354 ? 0.7965 0.8594 0.7077 0.0685  0.1432  -0.0935 280  THR A CA  
2135 C C   . THR A 354 ? 0.5175 0.6055 0.4716 0.0663  0.1330  -0.0809 280  THR A C   
2136 O O   . THR A 354 ? 0.5310 0.5979 0.4892 0.0686  0.1308  -0.0801 280  THR A O   
2137 C CB  . THR A 354 ? 0.5952 0.6533 0.5029 0.0799  0.1587  -0.1061 280  THR A CB  
2138 O OG1 . THR A 354 ? 0.6566 0.6870 0.5206 0.0810  0.1652  -0.1178 280  THR A OG1 
2139 C CG2 . THR A 354 ? 0.6001 0.6413 0.5244 0.0874  0.1606  -0.1140 280  THR A CG2 
2140 N N   . LEU A 355 ? 0.3089 0.4392 0.2912 0.0615  0.1248  -0.0711 281  LEU A N   
2141 C CA  . LEU A 355 ? 0.3419 0.4913 0.3562 0.0590  0.1111  -0.0590 281  LEU A CA  
2142 C C   . LEU A 355 ? 0.3062 0.4441 0.3206 0.0472  0.1004  -0.0528 281  LEU A C   
2143 O O   . LEU A 355 ? 0.2573 0.3872 0.2838 0.0487  0.0948  -0.0479 281  LEU A O   
2144 C CB  . LEU A 355 ? 0.3772 0.5660 0.4108 0.0547  0.1023  -0.0498 281  LEU A CB  
2145 C CG  . LEU A 355 ? 0.2510 0.4542 0.3074 0.0527  0.0872  -0.0376 281  LEU A CG  
2146 C CD1 . LEU A 355 ? 0.2844 0.4817 0.3515 0.0672  0.0907  -0.0391 281  LEU A CD1 
2147 C CD2 . LEU A 355 ? 0.2993 0.5333 0.3636 0.0471  0.0794  -0.0291 281  LEU A CD2 
2148 N N   . ALA A 356 ? 0.3413 0.4800 0.3427 0.0348  0.0970  -0.0538 282  ALA A N   
2149 C CA  . ALA A 356 ? 0.2410 0.3723 0.2454 0.0221  0.0866  -0.0495 282  ALA A CA  
2150 C C   . ALA A 356 ? 0.2830 0.3771 0.2684 0.0314  0.0928  -0.0538 282  ALA A C   
2151 O O   . ALA A 356 ? 0.2525 0.3409 0.2488 0.0290  0.0864  -0.0476 282  ALA A O   
2152 C CB  . ALA A 356 ? 0.3051 0.4456 0.3005 0.0051  0.0817  -0.0531 282  ALA A CB  
2153 N N   . VAL A 357 ? 0.3547 0.4200 0.3064 0.0437  0.1035  -0.0652 283  VAL A N   
2154 C CA  . VAL A 357 ? 0.3570 0.3864 0.2841 0.0550  0.1011  -0.0712 283  VAL A CA  
2155 C C   . VAL A 357 ? 0.4037 0.4222 0.3464 0.0638  0.1021  -0.0629 283  VAL A C   
2156 O O   . VAL A 357 ? 0.3914 0.4083 0.3323 0.0687  0.0882  -0.0624 283  VAL A O   
2157 C CB  . VAL A 357 ? 0.4278 0.4326 0.3193 0.0661  0.1043  -0.0886 283  VAL A CB  
2158 C CG1 . VAL A 357 ? 0.4210 0.4123 0.3079 0.0795  0.0921  -0.1033 283  VAL A CG1 
2159 C CG2 . VAL A 357 ? 0.6508 0.6579 0.5269 0.0478  0.1020  -0.1021 283  VAL A CG2 
2160 N N   . VAL A 358 ? 0.4552 0.4863 0.4246 0.0623  0.1130  -0.0673 284  VAL A N   
2161 C CA  . VAL A 358 ? 0.3584 0.3981 0.3576 0.0655  0.1101  -0.0723 284  VAL A CA  
2162 C C   . VAL A 358 ? 0.3893 0.4407 0.4062 0.0593  0.0987  -0.0579 284  VAL A C   
2163 O O   . VAL A 358 ? 0.3785 0.4223 0.4033 0.0589  0.0921  -0.0620 284  VAL A O   
2164 C CB  . VAL A 358 ? 0.3148 0.3817 0.3318 0.0796  0.1145  -0.0751 284  VAL A CB  
2165 C CG1 . VAL A 358 ? 0.4974 0.5736 0.5365 0.0909  0.1055  -0.0711 284  VAL A CG1 
2166 C CG2 . VAL A 358 ? 0.4317 0.4836 0.4310 0.0872  0.1266  -0.0917 284  VAL A CG2 
2167 N N   . LEU A 359 ? 0.4137 0.4913 0.4408 0.0532  0.0930  -0.0458 285  LEU A N   
2168 C CA  . LEU A 359 ? 0.3064 0.3946 0.3503 0.0452  0.0807  -0.0347 285  LEU A CA  
2169 C C   . LEU A 359 ? 0.2370 0.3013 0.2634 0.0414  0.0779  -0.0295 285  LEU A C   
2170 O O   . LEU A 359 ? 0.3080 0.3635 0.3391 0.0408  0.0727  -0.0239 285  LEU A O   
2171 C CB  . LEU A 359 ? 0.3667 0.4845 0.4213 0.0344  0.0687  -0.0276 285  LEU A CB  
2172 C CG  . LEU A 359 ? 0.2264 0.3696 0.2905 0.0403  0.0663  -0.0266 285  LEU A CG  
2173 C CD1 . LEU A 359 ? 0.2503 0.4147 0.3152 0.0295  0.0574  -0.0217 285  LEU A CD1 
2174 C CD2 . LEU A 359 ? 0.2820 0.4289 0.3575 0.0467  0.0596  -0.0215 285  LEU A CD2 
2175 N N   . GLY A 360 ? 0.3504 0.4125 0.3561 0.0394  0.0785  -0.0350 286  GLY A N   
2176 C CA  . GLY A 360 ? 0.3478 0.3993 0.3457 0.0292  0.0725  -0.0402 286  GLY A CA  
2177 C C   . GLY A 360 ? 0.3419 0.3710 0.3245 0.0418  0.0706  -0.0499 286  GLY A C   
2178 O O   . GLY A 360 ? 0.4945 0.5097 0.4819 0.0326  0.0681  -0.0470 286  GLY A O   
2179 N N   . THR A 361 ? 0.3834 0.4059 0.3548 0.0566  0.0694  -0.0634 287  THR A N   
2180 C CA  . THR A 361 ? 0.4246 0.4186 0.3947 0.0617  0.0699  -0.0767 287  THR A CA  
2181 C C   . THR A 361 ? 0.4302 0.4329 0.4233 0.0637  0.0665  -0.0697 287  THR A C   
2182 O O   . THR A 361 ? 0.5121 0.4853 0.4962 0.0648  0.0653  -0.0647 287  THR A O   
2183 C CB  . THR A 361 ? 0.5206 0.5028 0.4865 0.0713  0.0751  -0.0933 287  THR A CB  
2184 O OG1 . THR A 361 ? 0.5639 0.5729 0.5568 0.0710  0.0815  -0.0935 287  THR A OG1 
2185 C CG2 . THR A 361 ? 0.7196 0.6869 0.6574 0.0693  0.0784  -0.1022 287  THR A CG2 
2186 N N   . PHE A 362 ? 0.4279 0.4575 0.4472 0.0608  0.0684  -0.0652 288  PHE A N   
2187 C CA  . PHE A 362 ? 0.4261 0.4557 0.4601 0.0679  0.0665  -0.0553 288  PHE A CA  
2188 C C   . PHE A 362 ? 0.4673 0.4977 0.4996 0.0594  0.0584  -0.0467 288  PHE A C   
2189 O O   . PHE A 362 ? 0.4828 0.4922 0.5073 0.0657  0.0556  -0.0416 288  PHE A O   
2190 C CB  . PHE A 362 ? 0.2893 0.3431 0.3427 0.0704  0.0685  -0.0465 288  PHE A CB  
2191 C CG  . PHE A 362 ? 0.3082 0.3673 0.3699 0.0812  0.0601  -0.0371 288  PHE A CG  
2192 C CD1 . PHE A 362 ? 0.5763 0.6234 0.6353 0.0987  0.0603  -0.0402 288  PHE A CD1 
2193 C CD2 . PHE A 362 ? 0.2658 0.3398 0.3365 0.0734  0.0516  -0.0261 288  PHE A CD2 
2194 C CE1 . PHE A 362 ? 0.4670 0.5196 0.5341 0.1076  0.0526  -0.0323 288  PHE A CE1 
2195 C CE2 . PHE A 362 ? 0.2525 0.3308 0.3285 0.0816  0.0445  -0.0198 288  PHE A CE2 
2196 C CZ  . PHE A 362 ? 0.3668 0.4359 0.4421 0.0985  0.0450  -0.0227 288  PHE A CZ  
2197 N N   . GLY A 363 ? 0.2733 0.3241 0.3068 0.0457  0.0535  -0.0406 289  GLY A N   
2198 C CA  . GLY A 363 ? 0.3364 0.3835 0.3667 0.0387  0.0507  -0.0291 289  GLY A CA  
2199 C C   . GLY A 363 ? 0.4377 0.4451 0.4489 0.0343  0.0572  -0.0291 289  GLY A C   
2200 O O   . GLY A 363 ? 0.4751 0.4645 0.4828 0.0323  0.0571  -0.0237 289  GLY A O   
2201 N N   . ALA A 364 ? 0.4847 0.4749 0.4811 0.0309  0.0629  -0.0361 290  ALA A N   
2202 C CA  . ALA A 364 ? 0.5801 0.5232 0.5564 0.0202  0.0723  -0.0374 290  ALA A CA  
2203 C C   . ALA A 364 ? 0.3857 0.2950 0.3436 0.0338  0.0716  -0.0381 290  ALA A C   
2204 O O   . ALA A 364 ? 0.5526 0.4262 0.4920 0.0252  0.0761  -0.0341 290  ALA A O   
2205 C CB  . ALA A 364 ? 0.5672 0.4946 0.5291 0.0122  0.0781  -0.0470 290  ALA A CB  
2206 N N   . CYS A 365 ? 0.6357 0.5573 0.6005 0.0527  0.0654  -0.0425 291  CYS A N   
2207 C CA  . CYS A 365 ? 0.7290 0.6192 0.6800 0.0654  0.0634  -0.0416 291  CYS A CA  
2208 C C   . CYS A 365 ? 0.7382 0.6404 0.7006 0.0717  0.0572  -0.0325 291  CYS A C   
2209 O O   . CYS A 365 ? 0.8282 0.7008 0.7742 0.0793  0.0551  -0.0280 291  CYS A O   
2210 C CB  . CYS A 365 ? 0.6410 0.5294 0.5936 0.0807  0.0631  -0.0525 291  CYS A CB  
2211 S SG  . CYS A 365 ? 0.9650 0.8288 0.8970 0.0763  0.0691  -0.0657 291  CYS A SG  
2212 N N   . TRP A 366 ? 0.4565 0.4004 0.4452 0.0675  0.0526  -0.0299 292  TRP A N   
2213 C CA  . TRP A 366 ? 0.3945 0.3485 0.3926 0.0722  0.0466  -0.0215 292  TRP A CA  
2214 C C   . TRP A 366 ? 0.3143 0.2751 0.3142 0.0589  0.0464  -0.0137 292  TRP A C   
2215 O O   . TRP A 366 ? 0.3178 0.2730 0.3147 0.0619  0.0424  -0.0076 292  TRP A O   
2216 C CB  . TRP A 366 ? 0.4038 0.3921 0.4260 0.0782  0.0430  -0.0211 292  TRP A CB  
2217 C CG  . TRP A 366 ? 0.3612 0.3409 0.3831 0.0956  0.0416  -0.0230 292  TRP A CG  
2218 C CD1 . TRP A 366 ? 0.4691 0.4551 0.4971 0.1034  0.0460  -0.0301 292  TRP A CD1 
2219 C CD2 . TRP A 366 ? 0.3635 0.3269 0.3788 0.1077  0.0354  -0.0178 292  TRP A CD2 
2220 N NE1 . TRP A 366 ? 0.4974 0.4725 0.5249 0.1201  0.0430  -0.0296 292  TRP A NE1 
2221 C CE2 . TRP A 366 ? 0.4573 0.4187 0.4773 0.1228  0.0357  -0.0219 292  TRP A CE2 
2222 C CE3 . TRP A 366 ? 0.3605 0.3107 0.3659 0.1072  0.0296  -0.0104 292  TRP A CE3 
2223 C CZ2 . TRP A 366 ? 0.5060 0.4534 0.5234 0.1373  0.0292  -0.0183 292  TRP A CZ2 
2224 C CZ3 . TRP A 366 ? 0.4532 0.3889 0.4531 0.1211  0.0228  -0.0069 292  TRP A CZ3 
2225 C CH2 . TRP A 366 ? 0.4904 0.4251 0.4974 0.1359  0.0221  -0.0106 292  TRP A CH2 
2226 N N   . LEU A 367 ? 0.3376 0.3085 0.3417 0.0439  0.0508  -0.0133 293  LEU A N   
2227 C CA  . LEU A 367 ? 0.3523 0.3306 0.3642 0.0295  0.0511  -0.0050 293  LEU A CA  
2228 C C   . LEU A 367 ? 0.3002 0.2421 0.2914 0.0254  0.0597  0.0003  293  LEU A C   
2229 O O   . LEU A 367 ? 0.3611 0.3068 0.3555 0.0235  0.0578  0.0061  293  LEU A O   
2230 C CB  . LEU A 367 ? 0.3624 0.3509 0.3858 0.0133  0.0521  -0.0054 293  LEU A CB  
2231 C CG  . LEU A 367 ? 0.3139 0.3363 0.3531 0.0143  0.0428  -0.0054 293  LEU A CG  
2232 C CD1 . LEU A 367 ? 0.2066 0.2333 0.2490 0.0037  0.0421  -0.0080 293  LEU A CD1 
2233 C CD2 . LEU A 367 ? 0.2519 0.2829 0.2983 0.0118  0.0344  -0.0001 293  LEU A CD2 
2234 N N   . PRO A 368 ? 0.3114 0.2161 0.2765 0.0226  0.0693  -0.0015 294  PRO A N   
2235 C CA  . PRO A 368 ? 0.2679 0.1423 0.2066 0.0171  0.0756  0.0027  294  PRO A CA  
2236 C C   . PRO A 368 ? 0.3066 0.1726 0.2346 0.0316  0.0671  0.0066  294  PRO A C   
2237 O O   . PRO A 368 ? 0.3009 0.1623 0.2204 0.0259  0.0696  0.0101  294  PRO A O   
2238 C CB  . PRO A 368 ? 0.2603 0.1020 0.1747 0.0159  0.0780  -0.0019 294  PRO A CB  
2239 C CG  . PRO A 368 ? 0.2288 0.0849 0.1584 0.0111  0.0802  -0.0080 294  PRO A CG  
2240 C CD  . PRO A 368 ? 0.3740 0.2671 0.3312 0.0218  0.0723  -0.0090 294  PRO A CD  
2241 N N   . PHE A 369 ? 0.3340 0.2020 0.2645 0.0499  0.0569  0.0044  295  PHE A N   
2242 C CA  . PHE A 369 ? 0.3247 0.1906 0.2508 0.0625  0.0473  0.0083  295  PHE A CA  
2243 C C   . PHE A 369 ? 0.3328 0.2363 0.2854 0.0603  0.0425  0.0105  295  PHE A C   
2244 O O   . PHE A 369 ? 0.3740 0.2723 0.3186 0.0623  0.0385  0.0148  295  PHE A O   
2245 C CB  . PHE A 369 ? 0.3700 0.2344 0.2996 0.0800  0.0386  0.0050  295  PHE A CB  
2246 C CG  . PHE A 369 ? 0.3070 0.1715 0.2359 0.0916  0.0278  0.0095  295  PHE A CG  
2247 C CD1 . PHE A 369 ? 0.3340 0.1609 0.2310 0.0952  0.0256  0.0146  295  PHE A CD1 
2248 C CD2 . PHE A 369 ? 0.3356 0.2377 0.2963 0.0961  0.0194  0.0087  295  PHE A CD2 
2249 C CE1 . PHE A 369 ? 0.3677 0.1943 0.2634 0.1054  0.0146  0.0190  295  PHE A CE1 
2250 C CE2 . PHE A 369 ? 0.4356 0.3367 0.3950 0.1058  0.0096  0.0133  295  PHE A CE2 
2251 C CZ  . PHE A 369 ? 0.4601 0.3248 0.3892 0.1105  0.0063  0.0183  295  PHE A CZ  
2252 N N   . ALA A 370 ? 0.2536 0.1945 0.2364 0.0544  0.0410  0.0069  296  ALA A N   
2253 C CA  . ALA A 370 ? 0.2380 0.2134 0.2445 0.0491  0.0346  0.0088  296  ALA A CA  
2254 C C   . ALA A 370 ? 0.2152 0.1850 0.2179 0.0370  0.0402  0.0137  296  ALA A C   
2255 O O   . ALA A 370 ? 0.2430 0.2272 0.2543 0.0363  0.0343  0.0158  296  ALA A O   
2256 C CB  . ALA A 370 ? 0.2627 0.2672 0.2899 0.0418  0.0334  0.0067  296  ALA A CB  
2257 N N   . ILE A 371 ? 0.2153 0.1606 0.2047 0.0258  0.0551  0.0165  297  ILE A N   
2258 C CA  . ILE A 371 ? 0.2487 0.1922 0.2395 0.0131  0.0548  0.0144  297  ILE A CA  
2259 C C   . ILE A 371 ? 0.3661 0.2769 0.3188 0.0202  0.0662  0.0142  297  ILE A C   
2260 O O   . ILE A 371 ? 0.3586 0.2696 0.3098 0.0197  0.0643  0.0136  297  ILE A O   
2261 C CB  . ILE A 371 ? 0.1885 0.1348 0.1868 0.0044  0.0514  0.0024  297  ILE A CB  
2262 C CG1 . ILE A 371 ? 0.1790 0.1419 0.1987 0.0017  0.0439  0.0014  297  ILE A CG1 
2263 C CG2 . ILE A 371 ? 0.2204 0.1618 0.2150 -0.0011 0.0552  -0.0028 297  ILE A CG2 
2264 C CD1 . ILE A 371 ? 0.2048 0.1667 0.2244 -0.0043 0.0458  -0.0067 297  ILE A CD1 
2265 N N   . TYR A 372 ? 0.3803 0.2577 0.3029 0.0244  0.0662  0.0150  298  TYR A N   
2266 C CA  . TYR A 372 ? 0.4222 0.2657 0.3112 0.0253  0.0643  0.0163  298  TYR A CA  
2267 C C   . TYR A 372 ? 0.3528 0.1919 0.2334 0.0386  0.0529  0.0215  298  TYR A C   
2268 O O   . TYR A 372 ? 0.4269 0.2495 0.2876 0.0357  0.0525  0.0228  298  TYR A O   
2269 C CB  . TYR A 372 ? 0.4322 0.2433 0.2964 0.0284  0.0646  0.0166  298  TYR A CB  
2270 C CG  . TYR A 372 ? 0.5146 0.2900 0.3444 0.0277  0.0642  0.0191  298  TYR A CG  
2271 C CD1 . TYR A 372 ? 0.4597 0.2300 0.2828 0.0131  0.0723  0.0161  298  TYR A CD1 
2272 C CD2 . TYR A 372 ? 0.5992 0.3488 0.4068 0.0426  0.0544  0.0240  298  TYR A CD2 
2273 C CE1 . TYR A 372 ? 0.5567 0.2938 0.3481 0.0120  0.0729  0.0192  298  TYR A CE1 
2274 C CE2 . TYR A 372 ? 0.5731 0.2884 0.3479 0.0415  0.0541  0.0274  298  TYR A CE2 
2275 C CZ  . TYR A 372 ? 0.5496 0.2574 0.3146 0.0256  0.0643  0.0255  298  TYR A CZ  
2276 O OH  . TYR A 372 ? 0.6941 0.3674 0.4262 0.0242  0.0645  0.0295  298  TYR A OH  
2277 N N   . CYS A 373 ? 0.4065 0.2643 0.3052 0.0532  0.0417  0.0229  299  CYS A N   
2278 C CA  . CYS A 373 ? 0.5487 0.4106 0.4467 0.0653  0.0278  0.0258  299  CYS A CA  
2279 C C   . CYS A 373 ? 0.4324 0.3157 0.3446 0.0598  0.0268  0.0268  299  CYS A C   
2280 O O   . CYS A 373 ? 0.4035 0.2924 0.3165 0.0677  0.0143  0.0287  299  CYS A O   
2281 C CB  . CYS A 373 ? 0.3775 0.2645 0.3024 0.0780  0.0161  0.0239  299  CYS A CB  
2282 S SG  . CYS A 373 ? 0.4727 0.4152 0.4484 0.0707  0.0139  0.0189  299  CYS A SG  
2283 N N   . VAL A 374 ? 0.2872 0.1838 0.2134 0.0457  0.0395  0.0251  300  VAL A N   
2284 C CA  . VAL A 374 ? 0.4791 0.3965 0.4226 0.0403  0.0401  0.0258  300  VAL A CA  
2285 C C   . VAL A 374 ? 0.4334 0.3334 0.3618 0.0240  0.0512  0.0214  300  VAL A C   
2286 O O   . VAL A 374 ? 0.2988 0.2002 0.2250 0.0203  0.0495  0.0217  300  VAL A O   
2287 C CB  . VAL A 374 ? 0.3564 0.3216 0.3473 0.0339  0.0406  0.0252  300  VAL A CB  
2288 C CG1 . VAL A 374 ? 0.3457 0.3304 0.3570 0.0246  0.0379  0.0263  300  VAL A CG1 
2289 C CG2 . VAL A 374 ? 0.3442 0.3334 0.3528 0.0412  0.0221  0.0199  300  VAL A CG2 
2290 N N   . VAL A 375 ? 0.4823 0.3706 0.4041 0.0145  0.0582  0.0154  301  VAL A N   
2291 C CA  . VAL A 375 ? 0.5128 0.3956 0.4312 0.0016  0.0629  0.0087  301  VAL A CA  
2292 C C   . VAL A 375 ? 0.5495 0.3931 0.4273 0.0007  0.0675  0.0104  301  VAL A C   
2293 O O   . VAL A 375 ? 0.7351 0.5646 0.6007 -0.0082 0.0755  0.0053  301  VAL A O   
2294 C CB  . VAL A 375 ? 0.4020 0.2999 0.3446 -0.0052 0.0678  -0.0010 301  VAL A CB  
2295 C CG1 . VAL A 375 ? 0.3382 0.2687 0.3184 -0.0031 0.0590  -0.0022 301  VAL A CG1 
2296 C CG2 . VAL A 375 ? 0.4914 0.3775 0.4238 -0.0044 0.0724  -0.0016 301  VAL A CG2 
2297 N N   . GLY A 376 ? 0.3841 0.2033 0.2364 0.0112  0.0638  0.0165  302  GLY A N   
2298 C CA  . GLY A 376 ? 0.6919 0.4720 0.5058 0.0114  0.0656  0.0190  302  GLY A CA  
2299 C C   . GLY A 376 ? 0.9346 0.6932 0.7205 0.0135  0.0619  0.0225  302  GLY A C   
2300 O O   . GLY A 376 ? 0.8631 0.6351 0.6563 0.0176  0.0558  0.0240  302  GLY A O   
2301 N N   . SER A 377 ? 0.7474 0.4716 0.4998 0.0104  0.0654  0.0244  303  SER A N   
2302 C CA  . SER A 377 ? 0.7926 0.4901 0.5112 0.0117  0.0622  0.0284  303  SER A CA  
2303 C C   . SER A 377 ? 0.8942 0.5542 0.5765 0.0217  0.0547  0.0357  303  SER A C   
2304 O O   . SER A 377 ? 0.9963 0.6443 0.6752 0.0215  0.0579  0.0364  303  SER A O   
2305 C CB  . SER A 377 ? 0.8188 0.5108 0.5323 -0.0037 0.0747  0.0241  303  SER A CB  
2306 O OG  . SER A 377 ? 1.0700 0.7386 0.7513 -0.0034 0.0723  0.0278  303  SER A OG  
2307 N N   . HIS A 378 ? 0.9239 0.5657 0.5798 0.0303  0.0436  0.0413  304  HIS A N   
2308 C CA  . HIS A 378 ? 1.0642 0.6709 0.6871 0.0399  0.0345  0.0489  304  HIS A CA  
2309 C C   . HIS A 378 ? 1.1001 0.6736 0.6928 0.0282  0.0458  0.0511  304  HIS A C   
2310 O O   . HIS A 378 ? 1.0938 0.6360 0.6600 0.0340  0.0404  0.0581  304  HIS A O   
2311 C CB  . HIS A 378 ? 1.1171 0.7171 0.7230 0.0525  0.0169  0.0544  304  HIS A CB  
2312 C CG  . HIS A 378 ? 1.1842 0.7790 0.7717 0.0443  0.0194  0.0538  304  HIS A CG  
2313 N ND1 . HIS A 378 ? 1.2054 0.8278 0.8163 0.0356  0.0269  0.0473  304  HIS A ND1 
2314 C CD2 . HIS A 378 ? 1.2760 0.8411 0.8240 0.0437  0.0149  0.0593  304  HIS A CD2 
2315 C CE1 . HIS A 378 ? 1.2215 0.8310 0.8081 0.0299  0.0277  0.0479  304  HIS A CE1 
2316 N NE2 . HIS A 378 ? 1.3319 0.9067 0.8789 0.0345  0.0206  0.0551  304  HIS A NE2 
2317 N N   . GLU A 379 ? 1.0229 0.6044 0.6225 0.0123  0.0609  0.0455  305  GLU A N   
2318 C CA  . GLU A 379 ? 1.0126 0.5705 0.5934 0.0002  0.0734  0.0466  305  GLU A CA  
2319 C C   . GLU A 379 ? 0.9398 0.5072 0.5429 -0.0052 0.0811  0.0430  305  GLU A C   
2320 O O   . GLU A 379 ? 0.9272 0.4763 0.5174 -0.0159 0.0926  0.0428  305  GLU A O   
2321 C CB  . GLU A 379 ? 1.0899 0.6545 0.6714 -0.0136 0.0854  0.0420  305  GLU A CB  
2322 C CG  . GLU A 379 ? 1.1821 0.7251 0.7286 -0.0116 0.0804  0.0470  305  GLU A CG  
2323 C CD  . GLU A 379 ? 1.3294 0.8893 0.8839 -0.0001 0.0659  0.0469  305  GLU A CD  
2324 O OE1 . GLU A 379 ? 1.2740 0.8626 0.8623 0.0062  0.0609  0.0434  305  GLU A OE1 
2325 O OE2 . GLU A 379 ? 1.3483 0.8938 0.8753 0.0025  0.0592  0.0507  305  GLU A OE2 
2326 N N   . ASP A 380 ? 0.9193 0.5115 0.5516 0.0023  0.0757  0.0399  306  ASP A N   
2327 C CA  . ASP A 380 ? 0.9876 0.5868 0.6373 -0.0030 0.0826  0.0361  306  ASP A CA  
2328 C C   . ASP A 380 ? 0.9943 0.5642 0.6253 0.0059  0.0757  0.0430  306  ASP A C   
2329 O O   . ASP A 380 ? 1.0096 0.5656 0.6262 0.0205  0.0632  0.0485  306  ASP A O   
2330 C CB  . ASP A 380 ? 0.8016 0.4421 0.4918 -0.0014 0.0817  0.0294  306  ASP A CB  
2331 C CG  . ASP A 380 ? 0.8459 0.5102 0.5588 -0.0151 0.0940  0.0200  306  ASP A CG  
2332 O OD1 . ASP A 380 ? 0.9566 0.6050 0.6560 -0.0259 0.1046  0.0180  306  ASP A OD1 
2333 O OD2 . ASP A 380 ? 0.7925 0.4919 0.5384 -0.0144 0.0926  0.0149  306  ASP A OD2 
2334 N N   . PRO A 381 ? 0.8724 0.4284 0.5006 -0.0016 0.0836  0.0422  307  PRO A N   
2335 C CA  . PRO A 381 ? 0.9104 0.4378 0.5244 0.0067  0.0768  0.0484  307  PRO A CA  
2336 C C   . PRO A 381 ? 1.0128 0.5526 0.6431 0.0223  0.0658  0.0473  307  PRO A C   
2337 O O   . PRO A 381 ? 0.9705 0.5452 0.6286 0.0240  0.0653  0.0416  307  PRO A O   
2338 C CB  . PRO A 381 ? 0.9286 0.4480 0.5453 -0.0064 0.0886  0.0450  307  PRO A CB  
2339 C CG  . PRO A 381 ? 0.8938 0.4222 0.5108 -0.0213 0.1015  0.0407  307  PRO A CG  
2340 C CD  . PRO A 381 ? 0.8510 0.4119 0.4858 -0.0181 0.0988  0.0361  307  PRO A CD  
2341 N N   . ALA A 382 ? 0.9849 0.4947 0.5985 0.0342  0.0570  0.0531  308  ALA A N   
2342 C CA  . ALA A 382 ? 0.9518 0.4705 0.5812 0.0513  0.0461  0.0519  308  ALA A CA  
2343 C C   . ALA A 382 ? 0.9459 0.4794 0.5998 0.0480  0.0516  0.0446  308  ALA A C   
2344 O O   . ALA A 382 ? 0.9122 0.4687 0.5891 0.0582  0.0466  0.0404  308  ALA A O   
2345 C CB  . ALA A 382 ? 1.0038 0.4865 0.6113 0.0658  0.0343  0.0598  308  ALA A CB  
2346 N N   . VAL A 383 ? 1.0178 0.5394 0.6682 0.0337  0.0615  0.0430  309  VAL A N   
2347 C CA  . VAL A 383 ? 0.9472 0.4793 0.6182 0.0300  0.0654  0.0361  309  VAL A CA  
2348 C C   . VAL A 383 ? 0.8343 0.4112 0.5357 0.0270  0.0682  0.0293  309  VAL A C   
2349 O O   . VAL A 383 ? 0.7758 0.3658 0.4954 0.0318  0.0668  0.0241  309  VAL A O   
2350 C CB  . VAL A 383 ? 1.0580 0.5723 0.7208 0.0134  0.0752  0.0357  309  VAL A CB  
2351 C CG1 . VAL A 383 ? 0.8597 0.3915 0.5238 -0.0028 0.0864  0.0339  309  VAL A CG1 
2352 C CG2 . VAL A 383 ? 1.2163 0.7346 0.8958 0.0107  0.0771  0.0287  309  VAL A CG2 
2353 N N   . TYR A 384 ? 0.7673 0.3674 0.4751 0.0193  0.0722  0.0291  310  TYR A N   
2354 C CA  . TYR A 384 ? 0.7144 0.3568 0.4525 0.0170  0.0739  0.0237  310  TYR A CA  
2355 C C   . TYR A 384 ? 0.7070 0.3612 0.4558 0.0345  0.0641  0.0242  310  TYR A C   
2356 O O   . TYR A 384 ? 0.7264 0.4108 0.5014 0.0350  0.0647  0.0199  310  TYR A O   
2357 C CB  . TYR A 384 ? 0.6689 0.3299 0.4112 0.0077  0.0790  0.0229  310  TYR A CB  
2358 C CG  . TYR A 384 ? 0.7214 0.3758 0.4567 -0.0088 0.0915  0.0194  310  TYR A CG  
2359 C CD1 . TYR A 384 ? 0.6695 0.3068 0.3989 -0.0161 0.0969  0.0182  310  TYR A CD1 
2360 C CD2 . TYR A 384 ? 0.7434 0.4086 0.4801 -0.0165 0.0975  0.0168  310  TYR A CD2 
2361 C CE1 . TYR A 384 ? 0.6529 0.2859 0.3791 -0.0305 0.1075  0.0152  310  TYR A CE1 
2362 C CE2 . TYR A 384 ? 0.6770 0.3372 0.4106 -0.0301 0.1087  0.0128  310  TYR A CE2 
2363 C CZ  . TYR A 384 ? 0.7111 0.3562 0.4401 -0.0370 0.1136  0.0125  310  TYR A CZ  
2364 O OH  . TYR A 384 ? 0.8819 0.5232 0.6104 -0.0502 0.1241  0.0093  310  TYR A OH  
2365 N N   . THR A 385 ? 0.6180 0.2510 0.3493 0.0492  0.0543  0.0295  311  THR A N   
2366 C CA  . THR A 385 ? 0.7219 0.3706 0.4690 0.0675  0.0432  0.0293  311  THR A CA  
2367 C C   . THR A 385 ? 0.6550 0.3017 0.4143 0.0758  0.0419  0.0244  311  THR A C   
2368 O O   . THR A 385 ? 0.6742 0.3510 0.4606 0.0804  0.0413  0.0193  311  THR A O   
2369 C CB  . THR A 385 ? 0.7566 0.3854 0.4845 0.0808  0.0315  0.0361  311  THR A CB  
2370 O OG1 . THR A 385 ? 0.6997 0.3296 0.4148 0.0729  0.0327  0.0394  311  THR A OG1 
2371 C CG2 . THR A 385 ? 0.6859 0.3373 0.4374 0.0996  0.0192  0.0354  311  THR A CG2 
2372 N N   . TYR A 386 ? 0.7572 0.3680 0.4972 0.0780  0.0416  0.0254  312  TYR A N   
2373 C CA  . TYR A 386 ? 0.8749 0.4800 0.6253 0.0868  0.0403  0.0193  312  TYR A CA  
2374 C C   . TYR A 386 ? 0.7043 0.3262 0.4696 0.0737  0.0497  0.0116  312  TYR A C   
2375 O O   . TYR A 386 ? 0.6714 0.3068 0.4548 0.0813  0.0489  0.0042  312  TYR A O   
2376 C CB  . TYR A 386 ? 0.9875 0.5477 0.7140 0.0909  0.0378  0.0223  312  TYR A CB  
2377 C CG  . TYR A 386 ? 0.9858 0.5273 0.6964 0.1036  0.0273  0.0310  312  TYR A CG  
2378 C CD1 . TYR A 386 ? 1.2356 0.7874 0.9617 0.1238  0.0164  0.0308  312  TYR A CD1 
2379 C CD2 . TYR A 386 ? 1.0465 0.5620 0.7285 0.0950  0.0282  0.0393  312  TYR A CD2 
2380 C CE1 . TYR A 386 ? 1.2738 0.8099 0.9875 0.1350  0.0053  0.0394  312  TYR A CE1 
2381 C CE2 . TYR A 386 ? 1.2436 0.7409 0.9093 0.1063  0.0174  0.0478  312  TYR A CE2 
2382 C CZ  . TYR A 386 ? 1.2031 0.7109 0.8850 0.1263  0.0053  0.0480  312  TYR A CZ  
2383 O OH  . TYR A 386 ? 1.1161 0.6072 0.7838 0.1371  -0.0069 0.0571  312  TYR A OH  
2384 N N   . ALA A 387 ? 0.6825 0.3060 0.4423 0.0541  0.0585  0.0128  313  ALA A N   
2385 C CA  . ALA A 387 ? 0.6688 0.3114 0.4452 0.0407  0.0661  0.0063  313  ALA A CA  
2386 C C   . ALA A 387 ? 0.5793 0.2623 0.3832 0.0444  0.0653  0.0027  313  ALA A C   
2387 O O   . ALA A 387 ? 0.6004 0.2983 0.4192 0.0396  0.0686  -0.0038 313  ALA A O   
2388 C CB  . ALA A 387 ? 0.7463 0.3913 0.5184 0.0202  0.0745  0.0083  313  ALA A CB  
2389 N N   . THR A 388 ? 0.5763 0.2772 0.3873 0.0526  0.0603  0.0069  314  THR A N   
2390 C CA  . THR A 388 ? 0.5462 0.2865 0.3861 0.0576  0.0582  0.0043  314  THR A CA  
2391 C C   . THR A 388 ? 0.5459 0.2941 0.3982 0.0783  0.0494  0.0009  314  THR A C   
2392 O O   . THR A 388 ? 0.4346 0.2146 0.3127 0.0821  0.0490  -0.0045 314  THR A O   
2393 C CB  . THR A 388 ? 0.4312 0.1916 0.2775 0.0540  0.0573  0.0098  314  THR A CB  
2394 O OG1 . THR A 388 ? 0.5618 0.3057 0.3923 0.0662  0.0487  0.0150  314  THR A OG1 
2395 C CG2 . THR A 388 ? 0.4180 0.1778 0.2581 0.0337  0.0672  0.0108  314  THR A CG2 
2396 N N   . LEU A 389 ? 0.6003 0.3230 0.4372 0.0913  0.0426  0.0038  315  LEU A N   
2397 C CA  . LEU A 389 ? 0.5992 0.3296 0.4510 0.1105  0.0353  -0.0001 315  LEU A CA  
2398 C C   . LEU A 389 ? 0.5790 0.2947 0.4300 0.1135  0.0395  -0.0092 315  LEU A C   
2399 O O   . LEU A 389 ? 0.6558 0.3923 0.5284 0.1244  0.0385  -0.0164 315  LEU A O   
2400 C CB  . LEU A 389 ? 0.5466 0.2551 0.3844 0.1232  0.0258  0.0068  315  LEU A CB  
2401 C CG  . LEU A 389 ? 0.5478 0.2747 0.3900 0.1238  0.0190  0.0140  315  LEU A CG  
2402 C CD1 . LEU A 389 ? 0.6402 0.3381 0.4617 0.1337  0.0095  0.0213  315  LEU A CD1 
2403 C CD2 . LEU A 389 ? 0.6315 0.4054 0.5119 0.1307  0.0144  0.0109  315  LEU A CD2 
2404 N N   . LEU A 390 ? 0.6467 0.3279 0.4744 0.1033  0.0446  -0.0096 316  LEU A N   
2405 C CA  . LEU A 390 ? 0.7610 0.4246 0.5863 0.1060  0.0476  -0.0193 316  LEU A CA  
2406 C C   . LEU A 390 ? 0.6839 0.3798 0.5313 0.1036  0.0522  -0.0297 316  LEU A C   
2407 O O   . LEU A 390 ? 0.8022 0.5026 0.6604 0.1163  0.0518  -0.0390 316  LEU A O   
2408 C CB  . LEU A 390 ? 0.7902 0.4168 0.5904 0.0909  0.0523  -0.0175 316  LEU A CB  
2409 C CG  . LEU A 390 ? 0.9262 0.5291 0.7214 0.0918  0.0546  -0.0278 316  LEU A CG  
2410 C CD1 . LEU A 390 ? 0.8736 0.4525 0.6656 0.1119  0.0487  -0.0298 316  LEU A CD1 
2411 C CD2 . LEU A 390 ? 1.0963 0.6723 0.8731 0.0725  0.0594  -0.0256 316  LEU A CD2 
2412 N N   . PRO A 391 ? 0.6605 0.3802 0.5160 0.0882  0.0569  -0.0289 317  PRO A N   
2413 C CA  . PRO A 391 ? 0.6952 0.4472 0.5714 0.0870  0.0601  -0.0386 317  PRO A CA  
2414 C C   . PRO A 391 ? 0.5161 0.3056 0.4190 0.1017  0.0560  -0.0402 317  PRO A C   
2415 O O   . PRO A 391 ? 0.7536 0.5597 0.6701 0.1090  0.0579  -0.0503 317  PRO A O   
2416 C CB  . PRO A 391 ? 0.6323 0.3997 0.5117 0.0666  0.0650  -0.0343 317  PRO A CB  
2417 C CG  . PRO A 391 ? 0.5931 0.3315 0.4513 0.0556  0.0667  -0.0250 317  PRO A CG  
2418 C CD  . PRO A 391 ? 0.6309 0.3513 0.4789 0.0712  0.0602  -0.0199 317  PRO A CD  
2419 N N   . ALA A 392 ? 0.6572 0.4616 0.5687 0.1049  0.0507  -0.0307 318  ALA A N   
2420 C CA  . ALA A 392 ? 0.5462 0.3877 0.4864 0.1160  0.0459  -0.0310 318  ALA A CA  
2421 C C   . ALA A 392 ? 0.7032 0.5332 0.6462 0.1340  0.0436  -0.0354 318  ALA A C   
2422 O O   . ALA A 392 ? 0.6766 0.5336 0.6427 0.1412  0.0451  -0.0413 318  ALA A O   
2423 C CB  . ALA A 392 ? 0.4128 0.2673 0.3590 0.1148  0.0393  -0.0202 318  ALA A CB  
2424 N N   . THR A 393 ? 0.7285 0.5177 0.6486 0.1408  0.0405  -0.0322 319  THR A N   
2425 C CA  . THR A 393 ? 0.7364 0.5117 0.6603 0.1585  0.0382  -0.0364 319  THR A CA  
2426 C C   . THR A 393 ? 0.8168 0.5910 0.7443 0.1608  0.0462  -0.0505 319  THR A C   
2427 O O   . THR A 393 ? 0.9528 0.7476 0.9021 0.1721  0.0482  -0.0571 319  THR A O   
2428 C CB  . THR A 393 ? 0.9532 0.6818 0.8501 0.1633  0.0331  -0.0300 319  THR A CB  
2429 O OG1 . THR A 393 ? 1.1335 0.8309 1.0034 0.1489  0.0382  -0.0308 319  THR A OG1 
2430 C CG2 . THR A 393 ? 0.8778 0.6094 0.7719 0.1644  0.0242  -0.0171 319  THR A CG2 
2431 N N   . LEU A 394 ? 0.7126 0.4636 0.6193 0.1489  0.0514  -0.0558 320  LEU A N   
2432 C CA  . LEU A 394 ? 0.7699 0.5160 0.6760 0.1503  0.0583  -0.0707 320  LEU A CA  
2433 C C   . LEU A 394 ? 0.7475 0.5374 0.6735 0.1443  0.0639  -0.0780 320  LEU A C   
2434 O O   . LEU A 394 ? 0.7458 0.5370 0.6717 0.1457  0.0702  -0.0916 320  LEU A O   
2435 C CB  . LEU A 394 ? 0.7386 0.4448 0.6165 0.1377  0.0605  -0.0737 320  LEU A CB  
2436 C CG  . LEU A 394 ? 0.7546 0.4663 0.6239 0.1160  0.0626  -0.0691 320  LEU A CG  
2437 C CD1 . LEU A 394 ? 0.7929 0.5282 0.6696 0.1076  0.0681  -0.0808 320  LEU A CD1 
2438 C CD2 . LEU A 394 ? 0.7608 0.4281 0.6034 0.1047  0.0623  -0.0643 320  LEU A CD2 
2439 N N   . ASN A 395 ? 0.6804 0.5053 0.6226 0.1370  0.0618  -0.0698 321  ASN A N   
2440 C CA  . ASN A 395 ? 0.6373 0.5058 0.6013 0.1312  0.0665  -0.0752 321  ASN A CA  
2441 C C   . ASN A 395 ? 0.6870 0.5726 0.6689 0.1464  0.0706  -0.0813 321  ASN A C   
2442 O O   . ASN A 395 ? 0.7148 0.6170 0.7017 0.1448  0.0786  -0.0916 321  ASN A O   
2443 C CB  . ASN A 395 ? 0.6825 0.5829 0.6624 0.1216  0.0623  -0.0638 321  ASN A CB  
2444 C CG  . ASN A 395 ? 0.5559 0.4993 0.5581 0.1184  0.0664  -0.0653 321  ASN A CG  
2445 O OD1 . ASN A 395 ? 0.4086 0.3729 0.4282 0.1275  0.0648  -0.0598 321  ASN A OD1 
2446 N ND2 . ASN A 395 ? 0.6197 0.5758 0.6203 0.1049  0.0710  -0.0720 321  ASN A ND2 
2447 N N   . SER A 396 ? 0.6191 0.5005 0.6093 0.1614  0.0655  -0.0744 322  SER A N   
2448 C CA  . SER A 396 ? 0.6801 0.5740 0.6872 0.1780  0.0695  -0.0795 322  SER A CA  
2449 C C   . SER A 396 ? 0.7927 0.6584 0.7885 0.1864  0.0764  -0.0945 322  SER A C   
2450 O O   . SER A 396 ? 0.7740 0.6531 0.7827 0.1969  0.0841  -0.1030 322  SER A O   
2451 C CB  . SER A 396 ? 0.7685 0.6628 0.7876 0.1917  0.0605  -0.0687 322  SER A CB  
2452 O OG  . SER A 396 ? 0.6954 0.6191 0.7268 0.1844  0.0543  -0.0568 322  SER A OG  
2453 N N   . MET A 397 ? 0.8000 0.6262 0.7722 0.1818  0.0741  -0.0977 323  MET A N   
2454 C CA  . MET A 397 ? 0.7845 0.5810 0.7431 0.1881  0.0799  -0.1128 323  MET A CA  
2455 C C   . MET A 397 ? 0.8207 0.6291 0.7715 0.1763  0.0885  -0.1264 323  MET A C   
2456 O O   . MET A 397 ? 0.9098 0.7099 0.8574 0.1829  0.0962  -0.1419 323  MET A O   
2457 C CB  . MET A 397 ? 0.8178 0.5637 0.7492 0.1870  0.0738  -0.1095 323  MET A CB  
2458 C CG  . MET A 397 ? 0.9271 0.6369 0.8480 0.1975  0.0775  -0.1232 323  MET A CG  
2459 S SD  . MET A 397 ? 1.0682 0.7250 0.9536 0.1840  0.0745  -0.1253 323  MET A SD  
2460 C CE  . MET A 397 ? 1.0065 0.6857 0.8846 0.1642  0.0806  -0.1357 323  MET A CE  
2461 N N   . ILE A 398 ? 0.8157 0.6435 0.7636 0.1589  0.0872  -0.1215 324  ILE A N   
2462 C CA  . ILE A 398 ? 0.6826 0.5219 0.6215 0.1463  0.0932  -0.1335 324  ILE A CA  
2463 C C   . ILE A 398 ? 0.5957 0.4807 0.5566 0.1455  0.1017  -0.1373 324  ILE A C   
2464 O O   . ILE A 398 ? 0.5637 0.4563 0.5173 0.1412  0.1096  -0.1511 324  ILE A O   
2465 C CB  . ILE A 398 ? 0.6568 0.4930 0.5823 0.1277  0.0874  -0.1260 324  ILE A CB  
2466 C CG1 . ILE A 398 ? 0.8693 0.6539 0.7667 0.1239  0.0836  -0.1268 324  ILE A CG1 
2467 C CG2 . ILE A 398 ? 0.7260 0.5929 0.6518 0.1146  0.0911  -0.1337 324  ILE A CG2 
2468 C CD1 . ILE A 398 ? 0.8747 0.6506 0.7589 0.1045  0.0797  -0.1176 324  ILE A CD1 
2469 N N   . ASN A 399 ? 0.6639 0.5763 0.6470 0.1499  0.1003  -0.1238 325  ASN A N   
2470 C CA  . ASN A 399 ? 0.6593 0.6100 0.6590 0.1491  0.1087  -0.1228 325  ASN A CA  
2471 C C   . ASN A 399 ? 0.6987 0.6477 0.6986 0.1619  0.1204  -0.1370 325  ASN A C   
2472 O O   . ASN A 399 ? 0.7019 0.6679 0.6980 0.1546  0.1309  -0.1444 325  ASN A O   
2473 C CB  . ASN A 399 ? 0.5972 0.5728 0.6196 0.1543  0.1021  -0.1051 325  ASN A CB  
2474 C CG  . ASN A 399 ? 0.5743 0.5594 0.5979 0.1388  0.0934  -0.0924 325  ASN A CG  
2475 O OD1 . ASN A 399 ? 0.5298 0.4967 0.5378 0.1276  0.0904  -0.0953 325  ASN A OD1 
2476 N ND2 . ASN A 399 ? 0.5736 0.5876 0.6162 0.1380  0.0886  -0.0789 325  ASN A ND2 
2477 N N   . PRO A 400 ? 0.7552 0.6837 0.7587 0.1805  0.1203  -0.1414 326  PRO A N   
2478 C CA  . PRO A 400 ? 0.7151 0.6415 0.7194 0.1926  0.1331  -0.1573 326  PRO A CA  
2479 C C   . PRO A 400 ? 0.6324 0.5418 0.6118 0.1825  0.1401  -0.1763 326  PRO A C   
2480 O O   . PRO A 400 ? 0.5707 0.4902 0.5475 0.1848  0.1534  -0.1893 326  PRO A O   
2481 C CB  . PRO A 400 ? 0.7985 0.6984 0.8102 0.2127  0.1286  -0.1578 326  PRO A CB  
2482 C CG  . PRO A 400 ? 0.7558 0.6585 0.7771 0.2127  0.1146  -0.1383 326  PRO A CG  
2483 C CD  . PRO A 400 ? 0.7175 0.6244 0.7251 0.1914  0.1092  -0.1318 326  PRO A CD  
2484 N N   . ILE A 401 ? 0.6774 0.5618 0.6376 0.1711  0.1310  -0.1783 327  ILE A N   
2485 C CA  . ILE A 401 ? 0.6035 0.4692 0.5374 0.1632  0.1337  -0.1964 327  ILE A CA  
2486 C C   . ILE A 401 ? 0.6293 0.5272 0.5569 0.1451  0.1380  -0.1979 327  ILE A C   
2487 O O   . ILE A 401 ? 0.7669 0.6636 0.6772 0.1415  0.1442  -0.2131 327  ILE A O   
2488 C CB  . ILE A 401 ? 0.6680 0.4933 0.5803 0.1581  0.1209  -0.1935 327  ILE A CB  
2489 C CG1 . ILE A 401 ? 0.8084 0.5971 0.7228 0.1750  0.1173  -0.1909 327  ILE A CG1 
2490 C CG2 . ILE A 401 ? 0.6772 0.4837 0.5616 0.1484  0.1204  -0.2100 327  ILE A CG2 
2491 C CD1 . ILE A 401 ? 0.9659 0.7147 0.8621 0.1688  0.1058  -0.1815 327  ILE A CD1 
2492 N N   . ILE A 402 ? 0.6975 0.6231 0.6376 0.1327  0.1336  -0.1806 328  ILE A N   
2493 C CA  . ILE A 402 ? 0.7035 0.6549 0.6364 0.1131  0.1350  -0.1778 328  ILE A CA  
2494 C C   . ILE A 402 ? 0.7674 0.7330 0.6985 0.1142  0.1522  -0.1820 328  ILE A C   
2495 O O   . ILE A 402 ? 0.8086 0.7744 0.7192 0.1031  0.1572  -0.1920 328  ILE A O   
2496 C CB  . ILE A 402 ? 0.7435 0.7166 0.6929 0.1011  0.1286  -0.1566 328  ILE A CB  
2497 C CG1 . ILE A 402 ? 0.5612 0.5210 0.5011 0.0968  0.1118  -0.1546 328  ILE A CG1 
2498 C CG2 . ILE A 402 ? 0.7765 0.7668 0.7204 0.0844  0.1379  -0.1464 328  ILE A CG2 
2499 C CD1 . ILE A 402 ? 0.5426 0.5190 0.5017 0.0896  0.1048  -0.1357 328  ILE A CD1 
2500 N N   . TYR A 403 ? 0.7669 0.7454 0.7175 0.1300  0.1603  -0.1744 329  TYR A N   
2501 C CA  . TYR A 403 ? 0.8351 0.8310 0.7842 0.1347  0.1758  -0.1758 329  TYR A CA  
2502 C C   . TYR A 403 ? 0.8775 0.8553 0.8071 0.1398  0.1864  -0.1990 329  TYR A C   
2503 O O   . TYR A 403 ? 0.8883 0.8721 0.8003 0.1344  0.1988  -0.2032 329  TYR A O   
2504 C CB  . TYR A 403 ? 0.7870 0.8075 0.7686 0.1530  0.1781  -0.1659 329  TYR A CB  
2505 C CG  . TYR A 403 ? 0.7158 0.7645 0.7164 0.1463  0.1690  -0.1436 329  TYR A CG  
2506 C CD1 . TYR A 403 ? 0.7134 0.7564 0.7217 0.1408  0.1539  -0.1327 329  TYR A CD1 
2507 C CD2 . TYR A 403 ? 0.7420 0.8241 0.7525 0.1453  0.1730  -0.1332 329  TYR A CD2 
2508 C CE1 . TYR A 403 ? 0.6607 0.7291 0.6857 0.1341  0.1437  -0.1133 329  TYR A CE1 
2509 C CE2 . TYR A 403 ? 0.7865 0.8957 0.8158 0.1386  0.1605  -0.1136 329  TYR A CE2 
2510 C CZ  . TYR A 403 ? 0.6901 0.7915 0.7262 0.1329  0.1460  -0.1041 329  TYR A CZ  
2511 O OH  . TYR A 403 ? 0.6464 0.7728 0.6998 0.1254  0.1331  -0.0866 329  TYR A OH  
2512 N N   . ALA A 404 ? 0.7688 0.7216 0.6989 0.1515  0.1817  -0.2133 330  ALA A N   
2513 C CA  . ALA A 404 ? 0.8851 0.8194 0.7982 0.1581  0.1905  -0.2368 330  ALA A CA  
2514 C C   . ALA A 404 ? 0.9206 0.8503 0.8028 0.1390  0.1876  -0.2485 330  ALA A C   
2515 O O   . ALA A 404 ? 1.0171 0.9484 0.8816 0.1369  0.1996  -0.2622 330  ALA A O   
2516 C CB  . ALA A 404 ? 0.9198 0.8210 0.8380 0.1749  0.1838  -0.2469 330  ALA A CB  
2517 N N   . PHE A 405 ? 0.8099 0.7359 0.6845 0.1271  0.1703  -0.2437 331  PHE A N   
2518 C CA  . PHE A 405 ? 0.8561 0.7827 0.7034 0.1156  0.1595  -0.2556 331  PHE A CA  
2519 C C   . PHE A 405 ? 0.8322 0.7919 0.6751 0.0952  0.1638  -0.2469 331  PHE A C   
2520 O O   . PHE A 405 ? 0.8080 0.7848 0.6270 0.0979  0.1472  -0.2585 331  PHE A O   
2521 C CB  . PHE A 405 ? 0.8949 0.7991 0.7322 0.1156  0.1380  -0.2506 331  PHE A CB  
2522 C CG  . PHE A 405 ? 0.8288 0.6829 0.6581 0.1278  0.1365  -0.2616 331  PHE A CG  
2523 C CD1 . PHE A 405 ? 0.7632 0.6049 0.6143 0.1420  0.1435  -0.2582 331  PHE A CD1 
2524 C CD2 . PHE A 405 ? 0.9709 0.7868 0.7708 0.1249  0.1274  -0.2739 331  PHE A CD2 
2525 C CE1 . PHE A 405 ? 0.7697 0.5652 0.6147 0.1535  0.1408  -0.2670 331  PHE A CE1 
2526 C CE2 . PHE A 405 ? 1.0641 0.8316 0.8592 0.1332  0.1266  -0.2832 331  PHE A CE2 
2527 C CZ  . PHE A 405 ? 0.8800 0.6382 0.6977 0.1480  0.1330  -0.2792 331  PHE A CZ  
2528 N N   . ARG A 406 ? 0.8063 0.7632 0.6579 0.0871  0.1811  -0.2202 332  ARG A N   
2529 C CA  . ARG A 406 ? 0.8641 0.7952 0.6742 0.0808  0.1934  -0.1889 332  ARG A CA  
2530 C C   . ARG A 406 ? 0.9361 0.8888 0.7483 0.0947  0.2075  -0.1863 332  ARG A C   
2531 O O   . ARG A 406 ? 0.9884 0.9319 0.7621 0.0970  0.2139  -0.1846 332  ARG A O   
2532 C CB  . ARG A 406 ? 0.8318 0.7702 0.6531 0.0822  0.1810  -0.1602 332  ARG A CB  
2533 C CG  . ARG A 406 ? 0.7683 0.6808 0.5843 0.0718  0.1688  -0.1583 332  ARG A CG  
2534 C CD  . ARG A 406 ? 0.8924 0.8419 0.6626 0.1195  0.1154  -0.1689 332  ARG A CD  
2535 N NE  . ARG A 406 ? 0.9400 0.8800 0.6882 0.0995  0.1307  -0.1573 332  ARG A NE  
2536 C CZ  . ARG A 406 ? 0.8017 0.7655 0.5699 0.0800  0.1277  -0.1461 332  ARG A CZ  
2537 N NH1 . ARG A 406 ? 0.6529 0.6230 0.4475 0.0761  0.1198  -0.1366 332  ARG A NH1 
2538 N NH2 . ARG A 406 ? 0.7796 0.7653 0.5416 0.0652  0.1312  -0.1453 332  ARG A NH2 
2539 N N   . ASN A 407 ? 0.9702 0.9547 0.8251 0.1082  0.2101  -0.1867 333  ASN A N   
2540 C CA  . ASN A 407 ? 0.9979 1.0114 0.8633 0.1208  0.2233  -0.1852 333  ASN A CA  
2541 C C   . ASN A 407 ? 0.9373 0.9374 0.7910 0.1299  0.2385  -0.2093 333  ASN A C   
2542 O O   . ASN A 407 ? 0.9356 0.9280 0.8081 0.1410  0.2376  -0.2239 333  ASN A O   
2543 C CB  . ASN A 407 ? 0.9450 0.9927 0.8582 0.1331  0.2188  -0.1737 333  ASN A CB  
2544 C CG  . ASN A 407 ? 0.8978 0.9824 0.8277 0.1425  0.2305  -0.1692 333  ASN A CG  
2545 O OD1 . ASN A 407 ? 0.8832 0.9659 0.8024 0.1504  0.2465  -0.1831 333  ASN A OD1 
2546 N ND2 . ASN A 407 ? 0.8605 0.9803 0.8181 0.1401  0.2203  -0.1495 333  ASN A ND2 
2547 N N   . GLN A 408 ? 1.0409 1.0382 0.8623 0.1275  0.2513  -0.2134 334  GLN A N   
2548 C CA  . GLN A 408 ? 0.9656 0.9490 0.7719 0.1343  0.2671  -0.2378 334  GLN A CA  
2549 C C   . GLN A 408 ? 0.9227 0.9346 0.7643 0.1550  0.2803  -0.2425 334  GLN A C   
2550 O O   . GLN A 408 ? 0.9185 0.9198 0.7663 0.1671  0.2887  -0.2633 334  GLN A O   
2551 C CB  . GLN A 408 ? 0.9659 0.9326 0.7192 0.1259  0.2763  -0.2388 334  GLN A CB  
2552 C CG  . GLN A 408 ? 1.0492 0.9951 0.7793 0.1283  0.2918  -0.2667 334  GLN A CG  
2553 C CD  . GLN A 408 ? 1.1823 1.1066 0.9139 0.1187  0.2813  -0.2908 334  GLN A CD  
2554 O OE1 . GLN A 408 ? 0.8623 0.7818 0.5999 0.1074  0.2629  -0.2854 334  GLN A OE1 
2555 N NE2 . GLN A 408 ? 1.0992 1.0225 0.8320 0.1265  0.2897  -0.3215 334  GLN A NE2 
2556 N N   . GLU A 409 ? 0.9030 0.9523 0.7708 0.1599  0.2811  -0.2239 335  GLU A N   
2557 C CA  . GLU A 409 ? 0.9923 1.0702 0.8938 0.1784  0.2942  -0.2270 335  GLU A CA  
2558 C C   . GLU A 409 ? 0.9612 1.0320 0.8965 0.1950  0.2890  -0.2347 335  GLU A C   
2559 O O   . GLU A 409 ? 1.0223 1.0943 0.9711 0.2117  0.3021  -0.2491 335  GLU A O   
2560 C CB  . GLU A 409 ? 0.9174 1.0394 0.8472 0.1776  0.2914  -0.2050 335  GLU A CB  
2561 C CG  . GLU A 409 ? 0.9786 1.1330 0.9427 0.1942  0.3059  -0.2070 335  GLU A CG  
2562 C CD  . GLU A 409 ? 1.0433 1.2425 1.0309 0.1894  0.3003  -0.1853 335  GLU A CD  
2563 O OE1 . GLU A 409 ? 1.0337 1.2405 1.0215 0.1760  0.2818  -0.1679 335  GLU A OE1 
2564 O OE2 . GLU A 409 ? 1.1002 1.3274 1.1075 0.1987  0.3140  -0.1862 335  GLU A OE2 
2565 N N   . ILE A 410 ? 0.8987 0.9613 0.8473 0.1917  0.2699  -0.2247 336  ILE A N   
2566 C CA  . ILE A 410 ? 0.8799 0.9313 0.8560 0.2082  0.2627  -0.2297 336  ILE A CA  
2567 C C   . ILE A 410 ? 0.8616 0.8724 0.8150 0.2090  0.2614  -0.2511 336  ILE A C   
2568 O O   . ILE A 410 ? 1.0731 1.0702 1.0435 0.2271  0.2623  -0.2617 336  ILE A O   
2569 C CB  . ILE A 410 ? 0.8531 0.9129 0.8523 0.2055  0.2429  -0.2094 336  ILE A CB  
2570 C CG1 . ILE A 410 ? 0.8715 0.9123 0.8917 0.2222  0.2343  -0.2137 336  ILE A CG1 
2571 C CG2 . ILE A 410 ? 0.9219 0.9673 0.8945 0.1832  0.2308  -0.2021 336  ILE A CG2 
2572 C CD1 . ILE A 410 ? 0.9069 0.9607 0.9531 0.2236  0.2156  -0.1919 336  ILE A CD1 
2573 N N   . GLN A 411 ? 0.8760 0.8670 0.7929 0.1897  0.2578  -0.2574 337  GLN A N   
2574 C CA  . GLN A 411 ? 1.0312 0.9879 0.9293 0.1895  0.2541  -0.2796 337  GLN A CA  
2575 C C   . GLN A 411 ? 1.1788 1.1283 1.0710 0.2032  0.2720  -0.3028 337  GLN A C   
2576 O O   . GLN A 411 ? 1.1607 1.0838 1.0530 0.2143  0.2696  -0.3209 337  GLN A O   
2577 C CB  . GLN A 411 ? 1.0178 0.9628 0.8818 0.1645  0.2455  -0.2826 337  GLN A CB  
2578 C CG  . GLN A 411 ? 0.9858 0.9018 0.8358 0.1647  0.2343  -0.3048 337  GLN A CG  
2579 C CD  . GLN A 411 ? 1.0810 0.9957 0.9016 0.1436  0.2217  -0.3099 337  GLN A CD  
2580 O OE1 . GLN A 411 ? 1.0273 0.9562 0.8292 0.1266  0.2290  -0.3047 337  GLN A OE1 
2581 N NE2 . GLN A 411 ? 1.1054 0.9983 0.9196 0.1460  0.2022  -0.3178 337  GLN A NE2 
2582 N N   . ARG A 412 ? 1.1041 1.0750 0.9909 0.2038  0.2901  -0.3023 338  ARG A N   
2583 C CA  . ARG A 412 ? 0.9798 0.9456 0.8605 0.2163  0.3093  -0.3251 338  ARG A CA  
2584 C C   . ARG A 412 ? 1.0736 1.0373 0.9926 0.2428  0.3119  -0.3309 338  ARG A C   
2585 O O   . ARG A 412 ? 1.2347 1.1750 1.1502 0.2544  0.3173  -0.3534 338  ARG A O   
2586 C CB  . ARG A 412 ? 0.9413 0.9330 0.8114 0.2130  0.3287  -0.3197 338  ARG A CB  
2587 N N   . ALA A 413 ? 1.0127 1.0001 0.9693 0.2529  0.3068  -0.3108 339  ALA A N   
2588 C CA  . ALA A 413 ? 1.1105 1.0959 1.1052 0.2777  0.3075  -0.3136 339  ALA A CA  
2589 C C   . ALA A 413 ? 1.1332 1.0795 1.1271 0.2834  0.2918  -0.3199 339  ALA A C   
2590 O O   . ALA A 413 ? 1.1542 1.0830 1.1655 0.3033  0.2955  -0.3318 339  ALA A O   
2591 C CB  . ALA A 413 ? 1.0171 1.0376 1.0520 0.2846  0.3017  -0.2897 339  ALA A CB  
2592 N N   . LEU A 414 ? 1.1683 1.0996 1.1431 0.2668  0.2745  -0.3116 340  LEU A N   
2593 C CA  . LEU A 414 ? 1.3228 1.2158 1.2955 0.2714  0.2592  -0.3159 340  LEU A CA  
2594 C C   . LEU A 414 ? 1.3041 1.1637 1.2564 0.2766  0.2658  -0.3435 340  LEU A C   
2595 O O   . LEU A 414 ? 1.2605 1.0920 1.2262 0.2942  0.2636  -0.3516 340  LEU A O   
2596 C CB  . LEU A 414 ? 1.0215 0.9080 0.9763 0.2506  0.2411  -0.3029 340  LEU A CB  
2597 N N   . TRP A 415 ? 1.2247 1.0860 1.1443 0.2614  0.2732  -0.3581 341  TRP A N   
2598 C CA  . TRP A 415 ? 1.3685 1.2014 1.2666 0.2651  0.2793  -0.3864 341  TRP A CA  
2599 C C   . TRP A 415 ? 1.5008 1.3452 1.4078 0.2806  0.3026  -0.4025 341  TRP A C   
2600 O O   . TRP A 415 ? 1.3941 1.2170 1.2846 0.2854  0.3101  -0.4281 341  TRP A O   
2601 C CB  . TRP A 415 ? 1.3426 1.1725 1.1998 0.2417  0.2733  -0.3959 341  TRP A CB  
2602 C CG  . TRP A 415 ? 1.4613 1.2667 1.3055 0.2315  0.2502  -0.3895 341  TRP A CG  
2603 C CD1 . TRP A 415 ? 1.4415 1.2214 1.3023 0.2404  0.2369  -0.3790 341  TRP A CD1 
2604 C CD2 . TRP A 415 ? 1.5807 1.3846 1.3928 0.2109  0.2376  -0.3926 341  TRP A CD2 
2605 N NE1 . TRP A 415 ? 1.5061 1.2666 1.3463 0.2262  0.2188  -0.3753 341  TRP A NE1 
2606 C CE2 . TRP A 415 ? 1.5621 1.3379 1.3739 0.2087  0.2180  -0.3837 341  TRP A CE2 
2607 C CE3 . TRP A 415 ? 1.5448 1.3686 1.3286 0.1946  0.2400  -0.4016 341  TRP A CE3 
2608 C CZ2 . TRP A 415 ? 1.5964 1.3632 1.3825 0.1919  0.2012  -0.3833 341  TRP A CZ2 
2609 C CZ3 . TRP A 415 ? 1.5320 1.3502 1.2912 0.1794  0.2204  -0.4014 341  TRP A CZ3 
2610 C CH2 . TRP A 415 ? 1.5446 1.3337 1.3057 0.1786  0.2016  -0.3923 341  TRP A CH2 
2611 N N   . LEU A 416 ? 1.3643 1.2426 1.2982 0.2890  0.3139  -0.3886 342  LEU A N   
2612 C CA  . LEU A 416 ? 1.3122 1.2035 1.2596 0.3053  0.3368  -0.4030 342  LEU A CA  
2613 C C   . LEU A 416 ? 1.5096 1.3705 1.4767 0.3287  0.3382  -0.4195 342  LEU A C   
2614 O O   . LEU A 416 ? 1.6580 1.5102 1.6188 0.3378  0.3546  -0.4438 342  LEU A O   
2615 C CB  . LEU A 416 ? 1.2487 1.1821 1.2296 0.3122  0.3446  -0.3824 342  LEU A CB  
2616 C CG  . LEU A 416 ? 1.1349 1.0901 1.1336 0.3277  0.3694  -0.3942 342  LEU A CG  
2617 C CD1 . LEU A 416 ? 1.1362 1.1104 1.1014 0.3111  0.3863  -0.3992 342  LEU A CD1 
2618 C CD2 . LEU A 416 ? 1.0884 1.0756 1.1379 0.3435  0.3693  -0.3750 342  LEU A CD2 
2619 N N   . LEU A 417 ? 1.4240 1.2670 1.4143 0.3384  0.3215  -0.4065 343  LEU A N   
2620 C CA  . LEU A 417 ? 1.5094 1.3213 1.5220 0.3612  0.3213  -0.4177 343  LEU A CA  
2621 C C   . LEU A 417 ? 1.6385 1.4040 1.6191 0.3547  0.3124  -0.4360 343  LEU A C   
2622 O O   . LEU A 417 ? 1.5065 1.2508 1.4750 0.3440  0.2930  -0.4253 343  LEU A O   
2623 C CB  . LEU A 417 ? 1.3671 1.1791 1.4164 0.3734  0.3064  -0.3939 343  LEU A CB  
2624 C CG  . LEU A 417 ? 1.3680 1.2271 1.4414 0.3707  0.3058  -0.3696 343  LEU A CG  
2625 C CD1 . LEU A 417 ? 1.2090 1.0658 1.3179 0.3835  0.2896  -0.3484 343  LEU A CD1 
2626 C CD2 . LEU A 417 ? 1.4804 1.3758 1.5718 0.3794  0.3286  -0.3771 343  LEU A CD2 
2627 N N   . LEU A 418 ? 1.7371 1.4870 1.7045 0.3609  0.3266  -0.4641 344  LEU A N   
2628 C CA  . LEU A 418 ? 1.7715 1.4803 1.7062 0.3534  0.3190  -0.4846 344  LEU A CA  
2629 C C   . LEU A 418 ? 1.8686 1.5372 1.8168 0.3748  0.3232  -0.5042 344  LEU A C   
2630 O O   . LEU A 418 ? 1.8982 1.5229 1.8285 0.3728  0.3104  -0.5124 344  LEU A O   
2631 C CB  . LEU A 418 ? 1.6994 1.4226 1.5948 0.3367  0.3292  -0.5038 344  LEU A CB  
2632 N N   . ASP A 419 ? 1.9471 1.6275 1.9265 0.3962  0.3407  -0.5115 345  ASP A N   
2633 C CA  . ASP A 419 ? 1.9257 1.5689 1.9196 0.4169  0.3467  -0.5319 345  ASP A CA  
2634 C C   . ASP A 419 ? 1.9511 1.6118 1.9953 0.4419  0.3577  -0.5240 345  ASP A C   
2635 O O   . ASP A 419 ? 1.9962 1.7011 2.0602 0.4425  0.3643  -0.5082 345  ASP A O   
2636 C CB  . ASP A 419 ? 1.9146 1.5488 1.8795 0.4145  0.3622  -0.5664 345  ASP A CB  
2637 N N   . GLY A 420 ? 1.9050 1.5300 1.9713 0.4624  0.3589  -0.5346 346  GLY A N   
2638 C CA  . GLY A 420 ? 1.7495 1.3866 1.8668 0.4879  0.3680  -0.5286 346  GLY A CA  
2639 C C   . GLY A 420 ? 1.6942 1.3747 1.8260 0.4951  0.3935  -0.5411 346  GLY A C   
2640 O O   . GLY A 420 ? 1.7399 1.4403 1.9173 0.5149  0.4023  -0.5348 346  GLY A O   
# 
