data_9DC8
# 
_entry.id   9DC8 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   9DC8         pdb_00009dc8 10.2210/pdb9dc8/pdb 
WWPDB D_1000287530 ?            ?                   
# 
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 2024-11-27 
2 'Structure model' 1 1 2025-01-29 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation.year'           
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DC8 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-25 
_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              sethh@gene.com 
_pdbx_contact_author.name_first         Seth 
_pdbx_contact_author.name_last          Harris 
_pdbx_contact_author.name_mi            F 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1728-9771 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Harris, S.F.' 1 0000-0003-1728-9771 
'Wu, P.'       2 ?                   
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Bioorg.Med.Chem.Lett. 
_citation.journal_id_ASTM           BMCLE8 
_citation.journal_id_CSD            1127 
_citation.journal_id_ISSN           1464-3405 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            117 
_citation.language                  ? 
_citation.page_first                130026 
_citation.page_last                 130026 
_citation.title                     
'Discovery of potent dihydro-oxazinoquinolinone inhibitors of GuaB for the treatment of tuberculosis.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bmcl.2024.130026 
_citation.pdbx_database_id_PubMed   39536836 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zhou, Y.'        1  ? 
primary 'Aliagas, I.'     2  ? 
primary 'Wang, S.'        3  ? 
primary 'Li, C.S.'        4  ? 
primary 'Liu, Z.'         5  ? 
primary 'Bowman, C.M.'    6  ? 
primary 'Burdick, D.J.'   7  ? 
primary 'Clark, K.R.'     8  ? 
primary 'Dening, T.J.'    9  ? 
primary 'Flygare, J.'     10 ? 
primary 'Ganti, A.'       11 ? 
primary 'Girgis, H.S.'    12 ? 
primary 'Hanan, E.J.'     13 ? 
primary 'Harris, S.F.'    14 ? 
primary 'Hu, C.'          15 ? 
primary 'Kapadia, S.B.'   16 ? 
primary 'Koehler, M.F.T.' 17 ? 
primary 'Lai, T.'         18 ? 
primary 'Liang, J.'       19 ? 
primary 'Liu, X.'         20 ? 
primary 'Ma, F.'          21 ? 
primary 'Mao, J.'         22 ? 
primary 'Nicolai, J.'     23 ? 
primary 'Sims, J.'        24 ? 
primary 'Unhayaker, S.'   25 ? 
primary 'Wai, J.'         26 ? 
primary 'Wang, X.'        27 ? 
primary 'Wu, P.'          28 ? 
primary 'Xu, Y.'          29 ? 
primary 'Yen, C.W.'       30 ? 
primary 'Zhang, R.'       31 ? 
primary 'Elfert, T.F.'    32 ? 
primary 'Tan, M.W.'       33 ? 
primary 'Kofoed, E.M.'    34 ? 
primary 'Crawford, T.D.'  35 ? 
# 
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 
;Inosine-5'-monophosphate dehydrogenase
;
43453.504 1   1.1.1.205 ? ? ? 
2 non-polymer syn 'INOSINIC ACID'                                                                           348.206   1   ? ? ? ? 
3 non-polymer syn 'N-(6-chloropyridin-3-yl)-N~2~-(1,4-dihydro-2H-pyrano[3,4-c]quinolin-9-yl)-L-alaninamide' 382.843   3   ? ? ? ? 
4 non-polymer nat 'SULFATE ION'                                                                             96.063    1   ? ? ? ? 
5 water       nat water                                                                                     18.015    203 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'IMP dehydrogenase,IMPD,IMPDH,IMPDH2' 
# 
_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       
;MHHHHHHGENLYFQGSSRGMSGLEDSSDLVVSPYVRMGGLTTDPVPTGGDDPHKVAMLGLTFDDVLLLPAASDVVPATAD
TSSQLTKKIRLKVPLVSSAMDTVTESRMAIAMARAGGMGVLHRNLPVAEQAGQVEMVKRSGGLLVGAAVGVGGDAWVRAM
MLVDAGVDVLVVDTAHAHNRLVLDMVGKLKSEVGDRVEVVGGNVATRSAAAALVDAGADAVKVGVGPGSICTTRVVAGVG
APQITAILEAVAACRPAGVPVIADGGLQYSGDIAKALAAGASTAMLGSLLAGTAEAPGELIFVNGKQYKSYRGMGSLGAM
RGRGGATSYSKDRYFADDALSEDKLVPEGIEGRVPFRGPLSSVIHQLTGGLRAAMGYTGSPTIEVLQQAQFVRITPAGLK
ESHPHDVAMTVEAPNYYARGNS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MHHHHHHGENLYFQGSSRGMSGLEDSSDLVVSPYVRMGGLTTDPVPTGGDDPHKVAMLGLTFDDVLLLPAASDVVPATAD
TSSQLTKKIRLKVPLVSSAMDTVTESRMAIAMARAGGMGVLHRNLPVAEQAGQVEMVKRSGGLLVGAAVGVGGDAWVRAM
MLVDAGVDVLVVDTAHAHNRLVLDMVGKLKSEVGDRVEVVGGNVATRSAAAALVDAGADAVKVGVGPGSICTTRVVAGVG
APQITAILEAVAACRPAGVPVIADGGLQYSGDIAKALAAGASTAMLGSLLAGTAEAPGELIFVNGKQYKSYRGMGSLGAM
RGRGGATSYSKDRYFADDALSEDKLVPEGIEGRVPFRGPLSSVIHQLTGGLRAAMGYTGSPTIEVLQQAQFVRITPAGLK
ESHPHDVAMTVEAPNYYARGNS
;
_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 'INOSINIC ACID'                                                                           IMP 
3 'N-(6-chloropyridin-3-yl)-N~2~-(1,4-dihydro-2H-pyrano[3,4-c]quinolin-9-yl)-L-alaninamide' VOA 
4 'SULFATE ION'                                                                             SO4 
5 water                                                                                     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   GLY n 
1 9   GLU n 
1 10  ASN n 
1 11  LEU n 
1 12  TYR n 
1 13  PHE n 
1 14  GLN n 
1 15  GLY n 
1 16  SER n 
1 17  SER n 
1 18  ARG n 
1 19  GLY n 
1 20  MET n 
1 21  SER n 
1 22  GLY n 
1 23  LEU n 
1 24  GLU n 
1 25  ASP n 
1 26  SER n 
1 27  SER n 
1 28  ASP n 
1 29  LEU n 
1 30  VAL n 
1 31  VAL n 
1 32  SER n 
1 33  PRO n 
1 34  TYR n 
1 35  VAL n 
1 36  ARG n 
1 37  MET n 
1 38  GLY n 
1 39  GLY n 
1 40  LEU n 
1 41  THR n 
1 42  THR n 
1 43  ASP n 
1 44  PRO n 
1 45  VAL n 
1 46  PRO n 
1 47  THR n 
1 48  GLY n 
1 49  GLY n 
1 50  ASP n 
1 51  ASP n 
1 52  PRO n 
1 53  HIS n 
1 54  LYS n 
1 55  VAL n 
1 56  ALA n 
1 57  MET n 
1 58  LEU n 
1 59  GLY n 
1 60  LEU n 
1 61  THR n 
1 62  PHE n 
1 63  ASP n 
1 64  ASP n 
1 65  VAL n 
1 66  LEU n 
1 67  LEU n 
1 68  LEU n 
1 69  PRO n 
1 70  ALA n 
1 71  ALA n 
1 72  SER n 
1 73  ASP n 
1 74  VAL n 
1 75  VAL n 
1 76  PRO n 
1 77  ALA n 
1 78  THR n 
1 79  ALA n 
1 80  ASP n 
1 81  THR n 
1 82  SER n 
1 83  SER n 
1 84  GLN n 
1 85  LEU n 
1 86  THR n 
1 87  LYS n 
1 88  LYS n 
1 89  ILE n 
1 90  ARG n 
1 91  LEU n 
1 92  LYS n 
1 93  VAL n 
1 94  PRO n 
1 95  LEU n 
1 96  VAL n 
1 97  SER n 
1 98  SER n 
1 99  ALA n 
1 100 MET n 
1 101 ASP n 
1 102 THR n 
1 103 VAL n 
1 104 THR n 
1 105 GLU n 
1 106 SER n 
1 107 ARG n 
1 108 MET n 
1 109 ALA n 
1 110 ILE n 
1 111 ALA n 
1 112 MET n 
1 113 ALA n 
1 114 ARG n 
1 115 ALA n 
1 116 GLY n 
1 117 GLY n 
1 118 MET n 
1 119 GLY n 
1 120 VAL n 
1 121 LEU n 
1 122 HIS n 
1 123 ARG n 
1 124 ASN n 
1 125 LEU n 
1 126 PRO n 
1 127 VAL n 
1 128 ALA n 
1 129 GLU n 
1 130 GLN n 
1 131 ALA n 
1 132 GLY n 
1 133 GLN n 
1 134 VAL n 
1 135 GLU n 
1 136 MET n 
1 137 VAL n 
1 138 LYS n 
1 139 ARG n 
1 140 SER n 
1 141 GLY n 
1 142 GLY n 
1 143 LEU n 
1 144 LEU n 
1 145 VAL n 
1 146 GLY n 
1 147 ALA n 
1 148 ALA n 
1 149 VAL n 
1 150 GLY n 
1 151 VAL n 
1 152 GLY n 
1 153 GLY n 
1 154 ASP n 
1 155 ALA n 
1 156 TRP n 
1 157 VAL n 
1 158 ARG n 
1 159 ALA n 
1 160 MET n 
1 161 MET n 
1 162 LEU n 
1 163 VAL n 
1 164 ASP n 
1 165 ALA n 
1 166 GLY n 
1 167 VAL n 
1 168 ASP n 
1 169 VAL n 
1 170 LEU n 
1 171 VAL n 
1 172 VAL n 
1 173 ASP n 
1 174 THR n 
1 175 ALA n 
1 176 HIS n 
1 177 ALA n 
1 178 HIS n 
1 179 ASN n 
1 180 ARG n 
1 181 LEU n 
1 182 VAL n 
1 183 LEU n 
1 184 ASP n 
1 185 MET n 
1 186 VAL n 
1 187 GLY n 
1 188 LYS n 
1 189 LEU n 
1 190 LYS n 
1 191 SER n 
1 192 GLU n 
1 193 VAL n 
1 194 GLY n 
1 195 ASP n 
1 196 ARG n 
1 197 VAL n 
1 198 GLU n 
1 199 VAL n 
1 200 VAL n 
1 201 GLY n 
1 202 GLY n 
1 203 ASN n 
1 204 VAL n 
1 205 ALA n 
1 206 THR n 
1 207 ARG n 
1 208 SER n 
1 209 ALA n 
1 210 ALA n 
1 211 ALA n 
1 212 ALA n 
1 213 LEU n 
1 214 VAL n 
1 215 ASP n 
1 216 ALA n 
1 217 GLY n 
1 218 ALA n 
1 219 ASP n 
1 220 ALA n 
1 221 VAL n 
1 222 LYS n 
1 223 VAL n 
1 224 GLY n 
1 225 VAL n 
1 226 GLY n 
1 227 PRO n 
1 228 GLY n 
1 229 SER n 
1 230 ILE n 
1 231 CYS n 
1 232 THR n 
1 233 THR n 
1 234 ARG n 
1 235 VAL n 
1 236 VAL n 
1 237 ALA n 
1 238 GLY n 
1 239 VAL n 
1 240 GLY n 
1 241 ALA n 
1 242 PRO n 
1 243 GLN n 
1 244 ILE n 
1 245 THR n 
1 246 ALA n 
1 247 ILE n 
1 248 LEU n 
1 249 GLU n 
1 250 ALA n 
1 251 VAL n 
1 252 ALA n 
1 253 ALA n 
1 254 CYS n 
1 255 ARG n 
1 256 PRO n 
1 257 ALA n 
1 258 GLY n 
1 259 VAL n 
1 260 PRO n 
1 261 VAL n 
1 262 ILE n 
1 263 ALA n 
1 264 ASP n 
1 265 GLY n 
1 266 GLY n 
1 267 LEU n 
1 268 GLN n 
1 269 TYR n 
1 270 SER n 
1 271 GLY n 
1 272 ASP n 
1 273 ILE n 
1 274 ALA n 
1 275 LYS n 
1 276 ALA n 
1 277 LEU n 
1 278 ALA n 
1 279 ALA n 
1 280 GLY n 
1 281 ALA n 
1 282 SER n 
1 283 THR n 
1 284 ALA n 
1 285 MET n 
1 286 LEU n 
1 287 GLY n 
1 288 SER n 
1 289 LEU n 
1 290 LEU n 
1 291 ALA n 
1 292 GLY n 
1 293 THR n 
1 294 ALA n 
1 295 GLU n 
1 296 ALA n 
1 297 PRO n 
1 298 GLY n 
1 299 GLU n 
1 300 LEU n 
1 301 ILE n 
1 302 PHE n 
1 303 VAL n 
1 304 ASN n 
1 305 GLY n 
1 306 LYS n 
1 307 GLN n 
1 308 TYR n 
1 309 LYS n 
1 310 SER n 
1 311 TYR n 
1 312 ARG n 
1 313 GLY n 
1 314 MET n 
1 315 GLY n 
1 316 SER n 
1 317 LEU n 
1 318 GLY n 
1 319 ALA n 
1 320 MET n 
1 321 ARG n 
1 322 GLY n 
1 323 ARG n 
1 324 GLY n 
1 325 GLY n 
1 326 ALA n 
1 327 THR n 
1 328 SER n 
1 329 TYR n 
1 330 SER n 
1 331 LYS n 
1 332 ASP n 
1 333 ARG n 
1 334 TYR n 
1 335 PHE n 
1 336 ALA n 
1 337 ASP n 
1 338 ASP n 
1 339 ALA n 
1 340 LEU n 
1 341 SER n 
1 342 GLU n 
1 343 ASP n 
1 344 LYS n 
1 345 LEU n 
1 346 VAL n 
1 347 PRO n 
1 348 GLU n 
1 349 GLY n 
1 350 ILE n 
1 351 GLU n 
1 352 GLY n 
1 353 ARG n 
1 354 VAL n 
1 355 PRO n 
1 356 PHE n 
1 357 ARG n 
1 358 GLY n 
1 359 PRO n 
1 360 LEU n 
1 361 SER n 
1 362 SER n 
1 363 VAL n 
1 364 ILE n 
1 365 HIS n 
1 366 GLN n 
1 367 LEU n 
1 368 THR n 
1 369 GLY n 
1 370 GLY n 
1 371 LEU n 
1 372 ARG n 
1 373 ALA n 
1 374 ALA n 
1 375 MET n 
1 376 GLY n 
1 377 TYR n 
1 378 THR n 
1 379 GLY n 
1 380 SER n 
1 381 PRO n 
1 382 THR n 
1 383 ILE n 
1 384 GLU n 
1 385 VAL n 
1 386 LEU n 
1 387 GLN n 
1 388 GLN n 
1 389 ALA n 
1 390 GLN n 
1 391 PHE n 
1 392 VAL n 
1 393 ARG n 
1 394 ILE n 
1 395 THR n 
1 396 PRO n 
1 397 ALA n 
1 398 GLY n 
1 399 LEU n 
1 400 LYS n 
1 401 GLU n 
1 402 SER n 
1 403 HIS n 
1 404 PRO n 
1 405 HIS n 
1 406 ASP n 
1 407 VAL n 
1 408 ALA n 
1 409 MET n 
1 410 THR n 
1 411 VAL n 
1 412 GLU n 
1 413 ALA n 
1 414 PRO n 
1 415 ASN n 
1 416 TYR n 
1 417 TYR n 
1 418 ALA n 
1 419 ARG n 
1 420 GLY n 
1 421 ASN n 
1 422 SER 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   142 ? ? 'guaB, guaB2, Rv3411c, MTCY78.17' ? ? ? ? ? ? 'Mycobacterium tuberculosis' 1773 ? ? ? 
? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 143 422 ? ? 'guaB, guaB2, Rv3411c, MTCY78.17' ? ? ? ? ? ? 'Mycobacterium tuberculosis' 1773 ? ? ? 
? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
IMP non-polymer         n 'INOSINIC ACID'                                                                           ? 
'C10 H13 N4 O8 P'  348.206 
LEU 'L-peptide linking' y LEUCINE                                                                                   ? 
'C6 H13 N O2'      131.173 
LYS 'L-peptide linking' y LYSINE                                                                                    ? 
'C6 H15 N2 O2 1'   147.195 
MET 'L-peptide linking' y METHIONINE                                                                                ? 
'C5 H11 N O2 S'    149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                                             ? 
'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                                                                                   ? 'C5 H9 N O2' 
115.130 
SER 'L-peptide linking' y SERINE                                                                                    ? 'C3 H7 N O3' 
105.093 
SO4 non-polymer         . 'SULFATE ION'                                                                             ? 'O4 S -2' 
96.063  
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 
VOA non-polymer         . 'N-(6-chloropyridin-3-yl)-N~2~-(1,4-dihydro-2H-pyrano[3,4-c]quinolin-9-yl)-L-alaninamide' ? 
'C20 H19 Cl N4 O2' 382.843 
# 
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   -14 ?   ?   ?   A . n 
A 1 2   HIS 2   -13 ?   ?   ?   A . n 
A 1 3   HIS 3   -12 ?   ?   ?   A . n 
A 1 4   HIS 4   -11 ?   ?   ?   A . n 
A 1 5   HIS 5   -10 ?   ?   ?   A . n 
A 1 6   HIS 6   -9  ?   ?   ?   A . n 
A 1 7   HIS 7   -8  ?   ?   ?   A . n 
A 1 8   GLY 8   -7  ?   ?   ?   A . n 
A 1 9   GLU 9   -6  ?   ?   ?   A . n 
A 1 10  ASN 10  -5  ?   ?   ?   A . n 
A 1 11  LEU 11  -4  ?   ?   ?   A . n 
A 1 12  TYR 12  -3  ?   ?   ?   A . n 
A 1 13  PHE 13  -2  ?   ?   ?   A . n 
A 1 14  GLN 14  -1  ?   ?   ?   A . n 
A 1 15  GLY 15  0   ?   ?   ?   A . n 
A 1 16  SER 16  1   ?   ?   ?   A . n 
A 1 17  SER 17  2   ?   ?   ?   A . n 
A 1 18  ARG 18  3   ?   ?   ?   A . n 
A 1 19  GLY 19  4   ?   ?   ?   A . n 
A 1 20  MET 20  5   ?   ?   ?   A . n 
A 1 21  SER 21  6   ?   ?   ?   A . n 
A 1 22  GLY 22  7   ?   ?   ?   A . n 
A 1 23  LEU 23  8   ?   ?   ?   A . n 
A 1 24  GLU 24  9   ?   ?   ?   A . n 
A 1 25  ASP 25  10  ?   ?   ?   A . n 
A 1 26  SER 26  11  ?   ?   ?   A . n 
A 1 27  SER 27  12  ?   ?   ?   A . n 
A 1 28  ASP 28  13  ?   ?   ?   A . n 
A 1 29  LEU 29  14  ?   ?   ?   A . n 
A 1 30  VAL 30  15  ?   ?   ?   A . n 
A 1 31  VAL 31  16  ?   ?   ?   A . n 
A 1 32  SER 32  17  ?   ?   ?   A . n 
A 1 33  PRO 33  18  ?   ?   ?   A . n 
A 1 34  TYR 34  19  ?   ?   ?   A . n 
A 1 35  VAL 35  20  ?   ?   ?   A . n 
A 1 36  ARG 36  21  ?   ?   ?   A . n 
A 1 37  MET 37  22  ?   ?   ?   A . n 
A 1 38  GLY 38  23  ?   ?   ?   A . n 
A 1 39  GLY 39  24  ?   ?   ?   A . n 
A 1 40  LEU 40  25  ?   ?   ?   A . n 
A 1 41  THR 41  26  ?   ?   ?   A . n 
A 1 42  THR 42  27  27  THR THR A . n 
A 1 43  ASP 43  28  28  ASP ASP A . n 
A 1 44  PRO 44  29  29  PRO PRO A . n 
A 1 45  VAL 45  30  30  VAL VAL A . n 
A 1 46  PRO 46  31  31  PRO PRO A . n 
A 1 47  THR 47  32  32  THR THR A . n 
A 1 48  GLY 48  33  33  GLY GLY A . n 
A 1 49  GLY 49  34  34  GLY GLY A . n 
A 1 50  ASP 50  35  35  ASP ASP A . n 
A 1 51  ASP 51  36  36  ASP ASP A . n 
A 1 52  PRO 52  37  37  PRO PRO A . n 
A 1 53  HIS 53  38  38  HIS HIS A . n 
A 1 54  LYS 54  39  39  LYS LYS A . n 
A 1 55  VAL 55  40  40  VAL VAL A . n 
A 1 56  ALA 56  41  41  ALA ALA A . n 
A 1 57  MET 57  42  42  MET MET A . n 
A 1 58  LEU 58  43  43  LEU LEU A . n 
A 1 59  GLY 59  44  44  GLY GLY A . n 
A 1 60  LEU 60  45  45  LEU LEU A . n 
A 1 61  THR 61  46  46  THR THR A . n 
A 1 62  PHE 62  47  47  PHE PHE A . n 
A 1 63  ASP 63  48  48  ASP ASP A . n 
A 1 64  ASP 64  49  49  ASP ASP A . n 
A 1 65  VAL 65  50  50  VAL VAL A . n 
A 1 66  LEU 66  51  51  LEU LEU A . n 
A 1 67  LEU 67  52  52  LEU LEU A . n 
A 1 68  LEU 68  53  53  LEU LEU A . n 
A 1 69  PRO 69  54  54  PRO PRO A . n 
A 1 70  ALA 70  55  55  ALA ALA A . n 
A 1 71  ALA 71  56  56  ALA ALA A . n 
A 1 72  SER 72  57  57  SER SER A . n 
A 1 73  ASP 73  58  58  ASP ASP A . n 
A 1 74  VAL 74  59  59  VAL VAL A . n 
A 1 75  VAL 75  60  60  VAL VAL A . n 
A 1 76  PRO 76  61  61  PRO PRO A . n 
A 1 77  ALA 77  62  62  ALA ALA A . n 
A 1 78  THR 78  63  63  THR THR A . n 
A 1 79  ALA 79  64  64  ALA ALA A . n 
A 1 80  ASP 80  65  65  ASP ASP A . n 
A 1 81  THR 81  66  66  THR THR A . n 
A 1 82  SER 82  67  67  SER SER A . n 
A 1 83  SER 83  68  68  SER SER A . n 
A 1 84  GLN 84  69  69  GLN GLN A . n 
A 1 85  LEU 85  70  70  LEU LEU A . n 
A 1 86  THR 86  71  71  THR THR A . n 
A 1 87  LYS 87  72  72  LYS LYS A . n 
A 1 88  LYS 88  73  73  LYS LYS A . n 
A 1 89  ILE 89  74  74  ILE ILE A . n 
A 1 90  ARG 90  75  75  ARG ARG A . n 
A 1 91  LEU 91  76  76  LEU LEU A . n 
A 1 92  LYS 92  77  77  LYS LYS A . n 
A 1 93  VAL 93  78  78  VAL VAL A . n 
A 1 94  PRO 94  79  79  PRO PRO A . n 
A 1 95  LEU 95  80  80  LEU LEU A . n 
A 1 96  VAL 96  81  81  VAL VAL A . n 
A 1 97  SER 97  82  82  SER SER A . n 
A 1 98  SER 98  83  83  SER SER A . n 
A 1 99  ALA 99  84  84  ALA ALA A . n 
A 1 100 MET 100 85  85  MET MET A . n 
A 1 101 ASP 101 86  86  ASP ASP A . n 
A 1 102 THR 102 87  87  THR THR A . n 
A 1 103 VAL 103 88  88  VAL VAL A . n 
A 1 104 THR 104 89  89  THR THR A . n 
A 1 105 GLU 105 90  90  GLU GLU A . n 
A 1 106 SER 106 91  91  SER SER A . n 
A 1 107 ARG 107 92  92  ARG ARG A . n 
A 1 108 MET 108 93  93  MET MET A . n 
A 1 109 ALA 109 94  94  ALA ALA A . n 
A 1 110 ILE 110 95  95  ILE ILE A . n 
A 1 111 ALA 111 96  96  ALA ALA A . n 
A 1 112 MET 112 97  97  MET MET A . n 
A 1 113 ALA 113 98  98  ALA ALA A . n 
A 1 114 ARG 114 99  99  ARG ARG A . n 
A 1 115 ALA 115 100 100 ALA ALA A . n 
A 1 116 GLY 116 101 101 GLY GLY A . n 
A 1 117 GLY 117 102 102 GLY GLY A . n 
A 1 118 MET 118 103 103 MET MET A . n 
A 1 119 GLY 119 104 104 GLY GLY A . n 
A 1 120 VAL 120 105 105 VAL VAL A . n 
A 1 121 LEU 121 106 106 LEU LEU A . n 
A 1 122 HIS 122 107 107 HIS HIS A . n 
A 1 123 ARG 123 108 108 ARG ARG A . n 
A 1 124 ASN 124 109 109 ASN ASN A . n 
A 1 125 LEU 125 110 110 LEU LEU A . n 
A 1 126 PRO 126 111 111 PRO PRO A . n 
A 1 127 VAL 127 112 112 VAL VAL A . n 
A 1 128 ALA 128 113 113 ALA ALA A . n 
A 1 129 GLU 129 114 114 GLU GLU A . n 
A 1 130 GLN 130 115 115 GLN GLN A . n 
A 1 131 ALA 131 116 116 ALA ALA A . n 
A 1 132 GLY 132 117 117 GLY GLY A . n 
A 1 133 GLN 133 118 118 GLN GLN A . n 
A 1 134 VAL 134 119 119 VAL VAL A . n 
A 1 135 GLU 135 120 120 GLU GLU A . n 
A 1 136 MET 136 121 121 MET MET A . n 
A 1 137 VAL 137 122 122 VAL VAL A . n 
A 1 138 LYS 138 123 123 LYS LYS A . n 
A 1 139 ARG 139 124 124 ARG ARG A . n 
A 1 140 SER 140 125 125 SER SER A . n 
A 1 141 GLY 141 126 126 GLY GLY A . n 
A 1 142 GLY 142 127 127 GLY GLY A . n 
A 1 143 LEU 143 253 253 LEU LEU A . n 
A 1 144 LEU 144 254 254 LEU LEU A . n 
A 1 145 VAL 145 255 255 VAL VAL A . n 
A 1 146 GLY 146 256 256 GLY GLY A . n 
A 1 147 ALA 147 257 257 ALA ALA A . n 
A 1 148 ALA 148 258 258 ALA ALA A . n 
A 1 149 VAL 149 259 259 VAL VAL A . n 
A 1 150 GLY 150 260 260 GLY GLY A . n 
A 1 151 VAL 151 261 261 VAL VAL A . n 
A 1 152 GLY 152 262 262 GLY GLY A . n 
A 1 153 GLY 153 263 263 GLY GLY A . n 
A 1 154 ASP 154 264 264 ASP ASP A . n 
A 1 155 ALA 155 265 265 ALA ALA A . n 
A 1 156 TRP 156 266 266 TRP TRP A . n 
A 1 157 VAL 157 267 267 VAL VAL A . n 
A 1 158 ARG 158 268 268 ARG ARG A . n 
A 1 159 ALA 159 269 269 ALA ALA A . n 
A 1 160 MET 160 270 270 MET MET A . n 
A 1 161 MET 161 271 271 MET MET A . n 
A 1 162 LEU 162 272 272 LEU LEU A . n 
A 1 163 VAL 163 273 273 VAL VAL A . n 
A 1 164 ASP 164 274 274 ASP ASP A . n 
A 1 165 ALA 165 275 275 ALA ALA A . n 
A 1 166 GLY 166 276 276 GLY GLY A . n 
A 1 167 VAL 167 277 277 VAL VAL A . n 
A 1 168 ASP 168 278 278 ASP ASP A . n 
A 1 169 VAL 169 279 279 VAL VAL A . n 
A 1 170 LEU 170 280 280 LEU LEU A . n 
A 1 171 VAL 171 281 281 VAL VAL A . n 
A 1 172 VAL 172 282 282 VAL VAL A . n 
A 1 173 ASP 173 283 283 ASP ASP A . n 
A 1 174 THR 174 284 284 THR THR A . n 
A 1 175 ALA 175 285 285 ALA ALA A . n 
A 1 176 HIS 176 286 286 HIS HIS A . n 
A 1 177 ALA 177 287 287 ALA ALA A . n 
A 1 178 HIS 178 288 288 HIS HIS A . n 
A 1 179 ASN 179 289 289 ASN ASN A . n 
A 1 180 ARG 180 290 290 ARG ARG A . n 
A 1 181 LEU 181 291 291 LEU LEU A . n 
A 1 182 VAL 182 292 292 VAL VAL A . n 
A 1 183 LEU 183 293 293 LEU LEU A . n 
A 1 184 ASP 184 294 294 ASP ASP A . n 
A 1 185 MET 185 295 295 MET MET A . n 
A 1 186 VAL 186 296 296 VAL VAL A . n 
A 1 187 GLY 187 297 297 GLY GLY A . n 
A 1 188 LYS 188 298 298 LYS LYS A . n 
A 1 189 LEU 189 299 299 LEU LEU A . n 
A 1 190 LYS 190 300 300 LYS LYS A . n 
A 1 191 SER 191 301 301 SER SER A . n 
A 1 192 GLU 192 302 302 GLU GLU A . n 
A 1 193 VAL 193 303 303 VAL VAL A . n 
A 1 194 GLY 194 304 304 GLY GLY A . n 
A 1 195 ASP 195 305 305 ASP ASP A . n 
A 1 196 ARG 196 306 306 ARG ARG A . n 
A 1 197 VAL 197 307 307 VAL VAL A . n 
A 1 198 GLU 198 308 308 GLU GLU A . n 
A 1 199 VAL 199 309 309 VAL VAL A . n 
A 1 200 VAL 200 310 310 VAL VAL A . n 
A 1 201 GLY 201 311 311 GLY GLY A . n 
A 1 202 GLY 202 312 312 GLY GLY A . n 
A 1 203 ASN 203 313 313 ASN ASN A . n 
A 1 204 VAL 204 314 314 VAL VAL A . n 
A 1 205 ALA 205 315 315 ALA ALA A . n 
A 1 206 THR 206 316 316 THR THR A . n 
A 1 207 ARG 207 317 317 ARG ARG A . n 
A 1 208 SER 208 318 318 SER SER A . n 
A 1 209 ALA 209 319 319 ALA ALA A . n 
A 1 210 ALA 210 320 320 ALA ALA A . n 
A 1 211 ALA 211 321 321 ALA ALA A . n 
A 1 212 ALA 212 322 322 ALA ALA A . n 
A 1 213 LEU 213 323 323 LEU LEU A . n 
A 1 214 VAL 214 324 324 VAL VAL A . n 
A 1 215 ASP 215 325 325 ASP ASP A . n 
A 1 216 ALA 216 326 326 ALA ALA A . n 
A 1 217 GLY 217 327 327 GLY GLY A . n 
A 1 218 ALA 218 328 328 ALA ALA A . n 
A 1 219 ASP 219 329 329 ASP ASP A . n 
A 1 220 ALA 220 330 330 ALA ALA A . n 
A 1 221 VAL 221 331 331 VAL VAL A . n 
A 1 222 LYS 222 332 332 LYS LYS A . n 
A 1 223 VAL 223 333 333 VAL VAL A . n 
A 1 224 GLY 224 334 334 GLY GLY A . n 
A 1 225 VAL 225 335 335 VAL VAL A . n 
A 1 226 GLY 226 336 336 GLY GLY A . n 
A 1 227 PRO 227 337 337 PRO PRO A . n 
A 1 228 GLY 228 338 338 GLY GLY A . n 
A 1 229 SER 229 339 339 SER SER A . n 
A 1 230 ILE 230 340 340 ILE ILE A . n 
A 1 231 CYS 231 341 341 CYS CYS A . n 
A 1 232 THR 232 342 342 THR THR A . n 
A 1 233 THR 233 343 343 THR THR A . n 
A 1 234 ARG 234 344 344 ARG ARG A . n 
A 1 235 VAL 235 345 345 VAL VAL A . n 
A 1 236 VAL 236 346 346 VAL VAL A . n 
A 1 237 ALA 237 347 347 ALA ALA A . n 
A 1 238 GLY 238 348 348 GLY GLY A . n 
A 1 239 VAL 239 349 349 VAL VAL A . n 
A 1 240 GLY 240 350 350 GLY GLY A . n 
A 1 241 ALA 241 351 351 ALA ALA A . n 
A 1 242 PRO 242 352 352 PRO PRO A . n 
A 1 243 GLN 243 353 353 GLN GLN A . n 
A 1 244 ILE 244 354 354 ILE ILE A . n 
A 1 245 THR 245 355 355 THR THR A . n 
A 1 246 ALA 246 356 356 ALA ALA A . n 
A 1 247 ILE 247 357 357 ILE ILE A . n 
A 1 248 LEU 248 358 358 LEU LEU A . n 
A 1 249 GLU 249 359 359 GLU GLU A . n 
A 1 250 ALA 250 360 360 ALA ALA A . n 
A 1 251 VAL 251 361 361 VAL VAL A . n 
A 1 252 ALA 252 362 362 ALA ALA A . n 
A 1 253 ALA 253 363 363 ALA ALA A . n 
A 1 254 CYS 254 364 364 CYS CYS A . n 
A 1 255 ARG 255 365 365 ARG ARG A . n 
A 1 256 PRO 256 366 366 PRO PRO A . n 
A 1 257 ALA 257 367 367 ALA ALA A . n 
A 1 258 GLY 258 368 368 GLY GLY A . n 
A 1 259 VAL 259 369 369 VAL VAL A . n 
A 1 260 PRO 260 370 370 PRO PRO A . n 
A 1 261 VAL 261 371 371 VAL VAL A . n 
A 1 262 ILE 262 372 372 ILE ILE A . n 
A 1 263 ALA 263 373 373 ALA ALA A . n 
A 1 264 ASP 264 374 374 ASP ASP A . n 
A 1 265 GLY 265 375 375 GLY GLY A . n 
A 1 266 GLY 266 376 376 GLY GLY A . n 
A 1 267 LEU 267 377 377 LEU LEU A . n 
A 1 268 GLN 268 378 378 GLN GLN A . n 
A 1 269 TYR 269 379 379 TYR TYR A . n 
A 1 270 SER 270 380 380 SER SER A . n 
A 1 271 GLY 271 381 381 GLY GLY A . n 
A 1 272 ASP 272 382 382 ASP ASP A . n 
A 1 273 ILE 273 383 383 ILE ILE A . n 
A 1 274 ALA 274 384 384 ALA ALA A . n 
A 1 275 LYS 275 385 385 LYS LYS A . n 
A 1 276 ALA 276 386 386 ALA ALA A . n 
A 1 277 LEU 277 387 387 LEU LEU A . n 
A 1 278 ALA 278 388 388 ALA ALA A . n 
A 1 279 ALA 279 389 389 ALA ALA A . n 
A 1 280 GLY 280 390 390 GLY GLY A . n 
A 1 281 ALA 281 391 391 ALA ALA A . n 
A 1 282 SER 282 392 392 SER SER A . n 
A 1 283 THR 283 393 393 THR THR A . n 
A 1 284 ALA 284 394 394 ALA ALA A . n 
A 1 285 MET 285 395 395 MET MET A . n 
A 1 286 LEU 286 396 396 LEU LEU A . n 
A 1 287 GLY 287 397 397 GLY GLY A . n 
A 1 288 SER 288 398 398 SER SER A . n 
A 1 289 LEU 289 399 399 LEU LEU A . n 
A 1 290 LEU 290 400 400 LEU LEU A . n 
A 1 291 ALA 291 401 401 ALA ALA A . n 
A 1 292 GLY 292 402 402 GLY GLY A . n 
A 1 293 THR 293 403 403 THR THR A . n 
A 1 294 ALA 294 404 404 ALA ALA A . n 
A 1 295 GLU 295 405 405 GLU GLU A . n 
A 1 296 ALA 296 406 406 ALA ALA A . n 
A 1 297 PRO 297 407 407 PRO PRO A . n 
A 1 298 GLY 298 408 408 GLY GLY A . n 
A 1 299 GLU 299 409 409 GLU GLU A . n 
A 1 300 LEU 300 410 410 LEU LEU A . n 
A 1 301 ILE 301 411 411 ILE ILE A . n 
A 1 302 PHE 302 412 412 PHE PHE A . n 
A 1 303 VAL 303 413 413 VAL VAL A . n 
A 1 304 ASN 304 414 414 ASN ASN A . n 
A 1 305 GLY 305 415 415 GLY GLY A . n 
A 1 306 LYS 306 416 416 LYS LYS A . n 
A 1 307 GLN 307 417 417 GLN GLN A . n 
A 1 308 TYR 308 418 418 TYR TYR A . n 
A 1 309 LYS 309 419 419 LYS LYS A . n 
A 1 310 SER 310 420 420 SER SER A . n 
A 1 311 TYR 311 421 421 TYR TYR A . n 
A 1 312 ARG 312 422 422 ARG ARG A . n 
A 1 313 GLY 313 423 423 GLY GLY A . n 
A 1 314 MET 314 424 424 MET MET A . n 
A 1 315 GLY 315 425 425 GLY GLY A . n 
A 1 316 SER 316 426 426 SER SER A . n 
A 1 317 LEU 317 427 427 LEU LEU A . n 
A 1 318 GLY 318 428 428 GLY GLY A . n 
A 1 319 ALA 319 429 429 ALA ALA A . n 
A 1 320 MET 320 430 430 MET MET A . n 
A 1 321 ARG 321 431 431 ARG ARG A . n 
A 1 322 GLY 322 432 ?   ?   ?   A . n 
A 1 323 ARG 323 433 ?   ?   ?   A . n 
A 1 324 GLY 324 434 ?   ?   ?   A . n 
A 1 325 GLY 325 435 ?   ?   ?   A . n 
A 1 326 ALA 326 436 ?   ?   ?   A . n 
A 1 327 THR 327 437 ?   ?   ?   A . n 
A 1 328 SER 328 438 ?   ?   ?   A . n 
A 1 329 TYR 329 439 ?   ?   ?   A . n 
A 1 330 SER 330 440 ?   ?   ?   A . n 
A 1 331 LYS 331 441 ?   ?   ?   A . n 
A 1 332 ASP 332 442 ?   ?   ?   A . n 
A 1 333 ARG 333 443 ?   ?   ?   A . n 
A 1 334 TYR 334 444 ?   ?   ?   A . n 
A 1 335 PHE 335 445 ?   ?   ?   A . n 
A 1 336 ALA 336 446 ?   ?   ?   A . n 
A 1 337 ASP 337 447 ?   ?   ?   A . n 
A 1 338 ASP 338 448 ?   ?   ?   A . n 
A 1 339 ALA 339 449 ?   ?   ?   A . n 
A 1 340 LEU 340 450 ?   ?   ?   A . n 
A 1 341 SER 341 451 ?   ?   ?   A . n 
A 1 342 GLU 342 452 ?   ?   ?   A . n 
A 1 343 ASP 343 453 ?   ?   ?   A . n 
A 1 344 LYS 344 454 ?   ?   ?   A . n 
A 1 345 LEU 345 455 455 LEU LEU A . n 
A 1 346 VAL 346 456 456 VAL VAL A . n 
A 1 347 PRO 347 457 457 PRO PRO A . n 
A 1 348 GLU 348 458 458 GLU GLU A . n 
A 1 349 GLY 349 459 459 GLY GLY A . n 
A 1 350 ILE 350 460 460 ILE ILE A . n 
A 1 351 GLU 351 461 461 GLU GLU A . n 
A 1 352 GLY 352 462 462 GLY GLY A . n 
A 1 353 ARG 353 463 463 ARG ARG A . n 
A 1 354 VAL 354 464 464 VAL VAL A . n 
A 1 355 PRO 355 465 465 PRO PRO A . n 
A 1 356 PHE 356 466 466 PHE PHE A . n 
A 1 357 ARG 357 467 467 ARG ARG A . n 
A 1 358 GLY 358 468 468 GLY GLY A . n 
A 1 359 PRO 359 469 469 PRO PRO A . n 
A 1 360 LEU 360 470 470 LEU LEU A . n 
A 1 361 SER 361 471 471 SER SER A . n 
A 1 362 SER 362 472 472 SER SER A . n 
A 1 363 VAL 363 473 473 VAL VAL A . n 
A 1 364 ILE 364 474 474 ILE ILE A . n 
A 1 365 HIS 365 475 475 HIS HIS A . n 
A 1 366 GLN 366 476 476 GLN GLN A . n 
A 1 367 LEU 367 477 477 LEU LEU A . n 
A 1 368 THR 368 478 478 THR THR A . n 
A 1 369 GLY 369 479 479 GLY GLY A . n 
A 1 370 GLY 370 480 480 GLY GLY A . n 
A 1 371 LEU 371 481 481 LEU LEU A . n 
A 1 372 ARG 372 482 482 ARG ARG A . n 
A 1 373 ALA 373 483 483 ALA ALA A . n 
A 1 374 ALA 374 484 484 ALA ALA A . n 
A 1 375 MET 375 485 485 MET MET A . n 
A 1 376 GLY 376 486 486 GLY GLY A . n 
A 1 377 TYR 377 487 487 TYR TYR A . n 
A 1 378 THR 378 488 488 THR THR A . n 
A 1 379 GLY 379 489 489 GLY GLY A . n 
A 1 380 SER 380 490 490 SER SER A . n 
A 1 381 PRO 381 491 491 PRO PRO A . n 
A 1 382 THR 382 492 492 THR THR A . n 
A 1 383 ILE 383 493 493 ILE ILE A . n 
A 1 384 GLU 384 494 494 GLU GLU A . n 
A 1 385 VAL 385 495 495 VAL VAL A . n 
A 1 386 LEU 386 496 496 LEU LEU A . n 
A 1 387 GLN 387 497 497 GLN GLN A . n 
A 1 388 GLN 388 498 498 GLN GLN A . n 
A 1 389 ALA 389 499 499 ALA ALA A . n 
A 1 390 GLN 390 500 500 GLN GLN A . n 
A 1 391 PHE 391 501 501 PHE PHE A . n 
A 1 392 VAL 392 502 502 VAL VAL A . n 
A 1 393 ARG 393 503 503 ARG ARG A . n 
A 1 394 ILE 394 504 504 ILE ILE A . n 
A 1 395 THR 395 505 505 THR THR A . n 
A 1 396 PRO 396 506 506 PRO PRO A . n 
A 1 397 ALA 397 507 507 ALA ALA A . n 
A 1 398 GLY 398 508 508 GLY GLY A . n 
A 1 399 LEU 399 509 509 LEU LEU A . n 
A 1 400 LYS 400 510 510 LYS LYS A . n 
A 1 401 GLU 401 511 511 GLU GLU A . n 
A 1 402 SER 402 512 512 SER SER A . n 
A 1 403 HIS 403 513 513 HIS HIS A . n 
A 1 404 PRO 404 514 514 PRO PRO A . n 
A 1 405 HIS 405 515 515 HIS HIS A . n 
A 1 406 ASP 406 516 516 ASP ASP A . n 
A 1 407 VAL 407 517 517 VAL VAL A . n 
A 1 408 ALA 408 518 518 ALA ALA A . n 
A 1 409 MET 409 519 519 MET MET A . n 
A 1 410 THR 410 520 520 THR THR A . n 
A 1 411 VAL 411 521 521 VAL VAL A . n 
A 1 412 GLU 412 522 522 GLU GLU A . n 
A 1 413 ALA 413 523 523 ALA ALA A . n 
A 1 414 PRO 414 524 524 PRO PRO A . n 
A 1 415 ASN 415 525 525 ASN ASN A . n 
A 1 416 TYR 416 526 ?   ?   ?   A . n 
A 1 417 TYR 417 527 ?   ?   ?   A . n 
A 1 418 ALA 418 528 ?   ?   ?   A . n 
A 1 419 ARG 419 529 ?   ?   ?   A . n 
A 1 420 GLY 420 530 ?   ?   ?   A . n 
A 1 421 ASN 421 531 ?   ?   ?   A . n 
A 1 422 SER 422 532 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        VOA 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   VOA 
_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 IMP 1   801  801 IMP IMP A . 
C 3 VOA 1   802  1   VOA DRG A . 
D 3 VOA 1   803  1   VOA DRG A . 
E 3 VOA 1   804  1   VOA DRG A . 
F 4 SO4 1   805  1   SO4 SO4 A . 
G 5 HOH 1   901  180 HOH HOH A . 
G 5 HOH 2   902  161 HOH HOH A . 
G 5 HOH 3   903  73  HOH HOH A . 
G 5 HOH 4   904  117 HOH HOH A . 
G 5 HOH 5   905  137 HOH HOH A . 
G 5 HOH 6   906  101 HOH HOH A . 
G 5 HOH 7   907  76  HOH HOH A . 
G 5 HOH 8   908  98  HOH HOH A . 
G 5 HOH 9   909  112 HOH HOH A . 
G 5 HOH 10  910  174 HOH HOH A . 
G 5 HOH 11  911  139 HOH HOH A . 
G 5 HOH 12  912  134 HOH HOH A . 
G 5 HOH 13  913  191 HOH HOH A . 
G 5 HOH 14  914  162 HOH HOH A . 
G 5 HOH 15  915  86  HOH HOH A . 
G 5 HOH 16  916  67  HOH HOH A . 
G 5 HOH 17  917  92  HOH HOH A . 
G 5 HOH 18  918  169 HOH HOH A . 
G 5 HOH 19  919  171 HOH HOH A . 
G 5 HOH 20  920  24  HOH HOH A . 
G 5 HOH 21  921  164 HOH HOH A . 
G 5 HOH 22  922  156 HOH HOH A . 
G 5 HOH 23  923  130 HOH HOH A . 
G 5 HOH 24  924  142 HOH HOH A . 
G 5 HOH 25  925  34  HOH HOH A . 
G 5 HOH 26  926  108 HOH HOH A . 
G 5 HOH 27  927  146 HOH HOH A . 
G 5 HOH 28  928  80  HOH HOH A . 
G 5 HOH 29  929  69  HOH HOH A . 
G 5 HOH 30  930  193 HOH HOH A . 
G 5 HOH 31  931  39  HOH HOH A . 
G 5 HOH 32  932  23  HOH HOH A . 
G 5 HOH 33  933  127 HOH HOH A . 
G 5 HOH 34  934  192 HOH HOH A . 
G 5 HOH 35  935  93  HOH HOH A . 
G 5 HOH 36  936  12  HOH HOH A . 
G 5 HOH 37  937  143 HOH HOH A . 
G 5 HOH 38  938  205 HOH HOH A . 
G 5 HOH 39  939  26  HOH HOH A . 
G 5 HOH 40  940  5   HOH HOH A . 
G 5 HOH 41  941  45  HOH HOH A . 
G 5 HOH 42  942  158 HOH HOH A . 
G 5 HOH 43  943  7   HOH HOH A . 
G 5 HOH 44  944  188 HOH HOH A . 
G 5 HOH 45  945  33  HOH HOH A . 
G 5 HOH 46  946  10  HOH HOH A . 
G 5 HOH 47  947  15  HOH HOH A . 
G 5 HOH 48  948  199 HOH HOH A . 
G 5 HOH 49  949  47  HOH HOH A . 
G 5 HOH 50  950  115 HOH HOH A . 
G 5 HOH 51  951  123 HOH HOH A . 
G 5 HOH 52  952  135 HOH HOH A . 
G 5 HOH 53  953  18  HOH HOH A . 
G 5 HOH 54  954  55  HOH HOH A . 
G 5 HOH 55  955  138 HOH HOH A . 
G 5 HOH 56  956  50  HOH HOH A . 
G 5 HOH 57  957  28  HOH HOH A . 
G 5 HOH 58  958  14  HOH HOH A . 
G 5 HOH 59  959  49  HOH HOH A . 
G 5 HOH 60  960  53  HOH HOH A . 
G 5 HOH 61  961  51  HOH HOH A . 
G 5 HOH 62  962  144 HOH HOH A . 
G 5 HOH 63  963  88  HOH HOH A . 
G 5 HOH 64  964  131 HOH HOH A . 
G 5 HOH 65  965  32  HOH HOH A . 
G 5 HOH 66  966  85  HOH HOH A . 
G 5 HOH 67  967  84  HOH HOH A . 
G 5 HOH 68  968  22  HOH HOH A . 
G 5 HOH 69  969  72  HOH HOH A . 
G 5 HOH 70  970  6   HOH HOH A . 
G 5 HOH 71  971  91  HOH HOH A . 
G 5 HOH 72  972  71  HOH HOH A . 
G 5 HOH 73  973  178 HOH HOH A . 
G 5 HOH 74  974  48  HOH HOH A . 
G 5 HOH 75  975  16  HOH HOH A . 
G 5 HOH 76  976  78  HOH HOH A . 
G 5 HOH 77  977  8   HOH HOH A . 
G 5 HOH 78  978  31  HOH HOH A . 
G 5 HOH 79  979  122 HOH HOH A . 
G 5 HOH 80  980  132 HOH HOH A . 
G 5 HOH 81  981  97  HOH HOH A . 
G 5 HOH 82  982  77  HOH HOH A . 
G 5 HOH 83  983  3   HOH HOH A . 
G 5 HOH 84  984  56  HOH HOH A . 
G 5 HOH 85  985  89  HOH HOH A . 
G 5 HOH 86  986  190 HOH HOH A . 
G 5 HOH 87  987  68  HOH HOH A . 
G 5 HOH 88  988  11  HOH HOH A . 
G 5 HOH 89  989  17  HOH HOH A . 
G 5 HOH 90  990  111 HOH HOH A . 
G 5 HOH 91  991  57  HOH HOH A . 
G 5 HOH 92  992  36  HOH HOH A . 
G 5 HOH 93  993  41  HOH HOH A . 
G 5 HOH 94  994  20  HOH HOH A . 
G 5 HOH 95  995  75  HOH HOH A . 
G 5 HOH 96  996  120 HOH HOH A . 
G 5 HOH 97  997  177 HOH HOH A . 
G 5 HOH 98  998  4   HOH HOH A . 
G 5 HOH 99  999  94  HOH HOH A . 
G 5 HOH 100 1000 179 HOH HOH A . 
G 5 HOH 101 1001 40  HOH HOH A . 
G 5 HOH 102 1002 27  HOH HOH A . 
G 5 HOH 103 1003 149 HOH HOH A . 
G 5 HOH 104 1004 82  HOH HOH A . 
G 5 HOH 105 1005 104 HOH HOH A . 
G 5 HOH 106 1006 163 HOH HOH A . 
G 5 HOH 107 1007 165 HOH HOH A . 
G 5 HOH 108 1008 79  HOH HOH A . 
G 5 HOH 109 1009 19  HOH HOH A . 
G 5 HOH 110 1010 59  HOH HOH A . 
G 5 HOH 111 1011 81  HOH HOH A . 
G 5 HOH 112 1012 124 HOH HOH A . 
G 5 HOH 113 1013 30  HOH HOH A . 
G 5 HOH 114 1014 140 HOH HOH A . 
G 5 HOH 115 1015 60  HOH HOH A . 
G 5 HOH 116 1016 195 HOH HOH A . 
G 5 HOH 117 1017 87  HOH HOH A . 
G 5 HOH 118 1018 113 HOH HOH A . 
G 5 HOH 119 1019 74  HOH HOH A . 
G 5 HOH 120 1020 21  HOH HOH A . 
G 5 HOH 121 1021 95  HOH HOH A . 
G 5 HOH 122 1022 9   HOH HOH A . 
G 5 HOH 123 1023 2   HOH HOH A . 
G 5 HOH 124 1024 13  HOH HOH A . 
G 5 HOH 125 1025 100 HOH HOH A . 
G 5 HOH 126 1026 106 HOH HOH A . 
G 5 HOH 127 1027 172 HOH HOH A . 
G 5 HOH 128 1028 44  HOH HOH A . 
G 5 HOH 129 1029 148 HOH HOH A . 
G 5 HOH 130 1030 25  HOH HOH A . 
G 5 HOH 131 1031 125 HOH HOH A . 
G 5 HOH 132 1032 42  HOH HOH A . 
G 5 HOH 133 1033 46  HOH HOH A . 
G 5 HOH 134 1034 62  HOH HOH A . 
G 5 HOH 135 1035 61  HOH HOH A . 
G 5 HOH 136 1036 151 HOH HOH A . 
G 5 HOH 137 1037 66  HOH HOH A . 
G 5 HOH 138 1038 63  HOH HOH A . 
G 5 HOH 139 1039 38  HOH HOH A . 
G 5 HOH 140 1040 35  HOH HOH A . 
G 5 HOH 141 1041 70  HOH HOH A . 
G 5 HOH 142 1042 64  HOH HOH A . 
G 5 HOH 143 1043 65  HOH HOH A . 
G 5 HOH 144 1044 58  HOH HOH A . 
G 5 HOH 145 1045 145 HOH HOH A . 
G 5 HOH 146 1046 96  HOH HOH A . 
G 5 HOH 147 1047 126 HOH HOH A . 
G 5 HOH 148 1048 141 HOH HOH A . 
G 5 HOH 149 1049 121 HOH HOH A . 
G 5 HOH 150 1050 109 HOH HOH A . 
G 5 HOH 151 1051 116 HOH HOH A . 
G 5 HOH 152 1052 99  HOH HOH A . 
G 5 HOH 153 1053 29  HOH HOH A . 
G 5 HOH 154 1054 37  HOH HOH A . 
G 5 HOH 155 1055 207 HOH HOH A . 
G 5 HOH 156 1056 159 HOH HOH A . 
G 5 HOH 157 1057 196 HOH HOH A . 
G 5 HOH 158 1058 103 HOH HOH A . 
G 5 HOH 159 1059 150 HOH HOH A . 
G 5 HOH 160 1060 119 HOH HOH A . 
G 5 HOH 161 1061 209 HOH HOH A . 
G 5 HOH 162 1062 52  HOH HOH A . 
G 5 HOH 163 1063 197 HOH HOH A . 
G 5 HOH 164 1064 201 HOH HOH A . 
G 5 HOH 165 1065 110 HOH HOH A . 
G 5 HOH 166 1066 114 HOH HOH A . 
G 5 HOH 167 1067 206 HOH HOH A . 
G 5 HOH 168 1068 133 HOH HOH A . 
G 5 HOH 169 1069 54  HOH HOH A . 
G 5 HOH 170 1070 189 HOH HOH A . 
G 5 HOH 171 1071 194 HOH HOH A . 
G 5 HOH 172 1072 166 HOH HOH A . 
G 5 HOH 173 1073 181 HOH HOH A . 
G 5 HOH 174 1074 90  HOH HOH A . 
G 5 HOH 175 1075 187 HOH HOH A . 
G 5 HOH 176 1076 202 HOH HOH A . 
G 5 HOH 177 1077 160 HOH HOH A . 
G 5 HOH 178 1078 153 HOH HOH A . 
G 5 HOH 179 1079 204 HOH HOH A . 
G 5 HOH 180 1080 154 HOH HOH A . 
G 5 HOH 181 1081 167 HOH HOH A . 
G 5 HOH 182 1082 198 HOH HOH A . 
G 5 HOH 183 1083 128 HOH HOH A . 
G 5 HOH 184 1084 147 HOH HOH A . 
G 5 HOH 185 1085 83  HOH HOH A . 
G 5 HOH 186 1086 208 HOH HOH A . 
G 5 HOH 187 1087 183 HOH HOH A . 
G 5 HOH 188 1088 176 HOH HOH A . 
G 5 HOH 189 1089 182 HOH HOH A . 
G 5 HOH 190 1090 185 HOH HOH A . 
G 5 HOH 191 1091 107 HOH HOH A . 
G 5 HOH 192 1092 136 HOH HOH A . 
G 5 HOH 193 1093 105 HOH HOH A . 
G 5 HOH 194 1094 173 HOH HOH A . 
G 5 HOH 195 1095 102 HOH HOH A . 
G 5 HOH 196 1096 175 HOH HOH A . 
G 5 HOH 197 1097 186 HOH HOH A . 
G 5 HOH 198 1098 118 HOH HOH A . 
G 5 HOH 199 1099 170 HOH HOH A . 
G 5 HOH 200 1100 200 HOH HOH A . 
G 5 HOH 201 1101 168 HOH HOH A . 
G 5 HOH 202 1102 184 HOH HOH A . 
G 5 HOH 203 1103 203 HOH HOH A . 
# 
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    ? ? ? 1.18.2-3874_final 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALEPACK ? ? ? .                 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .                 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? .                 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DC8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     89.586 
_cell.length_a_esd                 ? 
_cell.length_b                     89.586 
_cell.length_b_esd                 ? 
_cell.length_c                     85.905 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9DC8 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                79 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 4' 
_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                   9DC8 
_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             1.98 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          37.98 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M HEPES pH 7.5, 20% isopropanol, 10% PEG 4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-09-09 
_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   1.18057 
_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                        'CLSI BEAMLINE 08B1-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.18057 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   08B1-1 
_diffrn_source.pdbx_synchrotron_site       CLSI 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DC8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.19 
_reflns.d_resolution_low                               44.79 
_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                                     98857 
_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                           90.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.97 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.073 
_reflns.pdbx_Rpim_I_all                                0.030 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       569406 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.067 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.19 
_reflns_shell.d_res_low                                     1.21 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2342 
_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                               1.5 
_reflns_shell.pdbx_chi_squared                              0.86 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               6.590 
_reflns_shell.pdbx_Rpim_I_all                               4.477 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.01 
_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                                  4.811 
_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                                 9DC8 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.60 
_refine.ls_d_res_low                             44.79 
_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                     87790 
_refine.ls_number_reflns_R_free                  4464 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.59 
_refine.ls_percent_reflns_R_free                 5.08 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1469 
_refine.ls_R_factor_R_free                       0.1892 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1447 
_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                          0.07 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 20.57 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.17 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.60 
_refine_hist.d_res_low                        44.79 
_refine_hist.number_atoms_solvent             203 
_refine_hist.number_atoms_total               2798 
_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        2486 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         109 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  ? 2696 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.922  ? 3684 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 16.517 ? 955  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.058  ? 434  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 490  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.60 1.62  . . 138 2736 99.00  . . . . 0.2379 . . . . . . . . . . . 0.2721 
'X-RAY DIFFRACTION' 1.62 1.64  . . 204 2738 99.00  . . . . 0.2328 . . . . . . . . . . . 0.2571 
'X-RAY DIFFRACTION' 1.64 1.66  . . 205 2665 98.00  . . . . 0.2080 . . . . . . . . . . . 0.2489 
'X-RAY DIFFRACTION' 1.66 1.68  . . 137 2760 100.00 . . . . 0.1979 . . . . . . . . . . . 0.2506 
'X-RAY DIFFRACTION' 1.68 1.70  . . 98  2952 100.00 . . . . 0.1744 . . . . . . . . . . . 0.2543 
'X-RAY DIFFRACTION' 1.70 1.72  . . 126 2735 100.00 . . . . 0.1642 . . . . . . . . . . . 0.2413 
'X-RAY DIFFRACTION' 1.72 1.75  . . 101 2816 100.00 . . . . 0.1618 . . . . . . . . . . . 0.2001 
'X-RAY DIFFRACTION' 1.75 1.77  . . 160 2795 100.00 . . . . 0.1476 . . . . . . . . . . . 0.1818 
'X-RAY DIFFRACTION' 1.77 1.80  . . 142 2708 99.00  . . . . 0.1455 . . . . . . . . . . . 0.2032 
'X-RAY DIFFRACTION' 1.80 1.83  . . 160 2814 100.00 . . . . 0.1363 . . . . . . . . . . . 0.1813 
'X-RAY DIFFRACTION' 1.83 1.86  . . 167 2775 100.00 . . . . 0.1296 . . . . . . . . . . . 0.1678 
'X-RAY DIFFRACTION' 1.86 1.90  . . 118 2778 100.00 . . . . 0.1407 . . . . . . . . . . . 0.1997 
'X-RAY DIFFRACTION' 1.90 1.93  . . 170 2761 100.00 . . . . 0.1420 . . . . . . . . . . . 0.1816 
'X-RAY DIFFRACTION' 1.93 1.97  . . 158 2756 99.00  . . . . 0.1232 . . . . . . . . . . . 0.1785 
'X-RAY DIFFRACTION' 1.97 2.02  . . 146 2776 99.00  . . . . 0.1136 . . . . . . . . . . . 0.2228 
'X-RAY DIFFRACTION' 2.02 2.06  . . 144 2787 100.00 . . . . 0.1404 . . . . . . . . . . . 0.1701 
'X-RAY DIFFRACTION' 2.06 2.11  . . 137 2826 100.00 . . . . 0.1285 . . . . . . . . . . . 0.1422 
'X-RAY DIFFRACTION' 2.11 2.17  . . 168 2737 100.00 . . . . 0.1227 . . . . . . . . . . . 0.1969 
'X-RAY DIFFRACTION' 2.17 2.24  . . 134 2789 100.00 . . . . 0.1288 . . . . . . . . . . . 0.1945 
'X-RAY DIFFRACTION' 2.24 2.31  . . 152 2823 100.00 . . . . 0.1355 . . . . . . . . . . . 0.1931 
'X-RAY DIFFRACTION' 2.31 2.39  . . 114 2838 100.00 . . . . 0.1374 . . . . . . . . . . . 0.1472 
'X-RAY DIFFRACTION' 2.39 2.49  . . 164 2715 100.00 . . . . 0.1370 . . . . . . . . . . . 0.2011 
'X-RAY DIFFRACTION' 2.49 2.60  . . 121 2829 100.00 . . . . 0.1429 . . . . . . . . . . . 0.1669 
'X-RAY DIFFRACTION' 2.60 2.74  . . 176 2758 100.00 . . . . 0.1588 . . . . . . . . . . . 0.1672 
'X-RAY DIFFRACTION' 2.74 2.91  . . 161 2760 100.00 . . . . 0.1559 . . . . . . . . . . . 0.2075 
'X-RAY DIFFRACTION' 2.91 3.13  . . 153 2741 100.00 . . . . 0.1528 . . . . . . . . . . . 0.1817 
'X-RAY DIFFRACTION' 3.13 3.45  . . 176 2812 100.00 . . . . 0.1492 . . . . . . . . . . . 0.1844 
'X-RAY DIFFRACTION' 3.45 3.94  . . 116 2778 100.00 . . . . 0.1343 . . . . . . . . . . . 0.1711 
'X-RAY DIFFRACTION' 3.95 4.96  . . 173 2787 100.00 . . . . 0.1279 . . . . . . . . . . . 0.1870 
'X-RAY DIFFRACTION' 4.97 44.79 . . 145 2781 100.00 . . . . 0.1641 . . . . . . . . . . . 0.2071 
# 
_struct.entry_id                     9DC8 
_struct.title                        'Mtb GuaB dCBS in complex with inhibitor G1' 
_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        9DC8 
_struct_keywords.text            'Mycobacterium tuberculosis, GuaB, IMPDH, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
# 
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 IMDH_MYCTU P9WKI7 ? 1 
;SRGMSGLEDSSDLVVSPYVRMGGLTTDPVPTGGDDPHKVAMLGLTFDDVLLLPAASDVVPATADTSSQLTKKIRLKVPLV
SSAMDTVTESRMAIAMARAGGMGVLHRNLPVAEQAGQVEMVKRS
;
2   
2 UNP IMDH_MYCTU P9WKI7 ? 1 
;LLVGAAVGVGGDAWVRAMMLVDAGVDVLVVDTAHAHNRLVLDMVGKLKSEVGDRVEVVGGNVATRSAAAALVDAGADAVK
VGVGPGSICTTRVVAGVGAPQITAILEAVAACRPAGVPVIADGGLQYSGDIAKALAAGASTAMLGSLLAGTAEAPGELIF
VNGKQYKSYRGMGSLGAMRGRGGATSYSKDRYFADDALSEDKLVPEGIEGRVPFRGPLSSVIHQLTGGLRAAMGYTGSPT
IEVLQQAQFVRITPAGLKESHPHDVAMTVEAPNYYAR
;
253 
# 
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 9DC8 A 17  ? 140 ? P9WKI7 2   ? 125 ? 2   125 
2 2 9DC8 A 143 ? 419 ? P9WKI7 253 ? 529 ? 253 529 
# 
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 9DC8 MET A 1   ? UNP P9WKI7 ? ? 'initiating methionine' -14 1  
1 9DC8 HIS A 2   ? UNP P9WKI7 ? ? 'expression tag'        -13 2  
1 9DC8 HIS A 3   ? UNP P9WKI7 ? ? 'expression tag'        -12 3  
1 9DC8 HIS A 4   ? UNP P9WKI7 ? ? 'expression tag'        -11 4  
1 9DC8 HIS A 5   ? UNP P9WKI7 ? ? 'expression tag'        -10 5  
1 9DC8 HIS A 6   ? UNP P9WKI7 ? ? 'expression tag'        -9  6  
1 9DC8 HIS A 7   ? UNP P9WKI7 ? ? 'expression tag'        -8  7  
1 9DC8 GLY A 8   ? UNP P9WKI7 ? ? 'expression tag'        -7  8  
1 9DC8 GLU A 9   ? UNP P9WKI7 ? ? 'expression tag'        -6  9  
1 9DC8 ASN A 10  ? UNP P9WKI7 ? ? 'expression tag'        -5  10 
1 9DC8 LEU A 11  ? UNP P9WKI7 ? ? 'expression tag'        -4  11 
1 9DC8 TYR A 12  ? UNP P9WKI7 ? ? 'expression tag'        -3  12 
1 9DC8 PHE A 13  ? UNP P9WKI7 ? ? 'expression tag'        -2  13 
1 9DC8 GLN A 14  ? UNP P9WKI7 ? ? 'expression tag'        -1  14 
1 9DC8 GLY A 15  ? UNP P9WKI7 ? ? 'expression tag'        0   15 
1 9DC8 SER A 16  ? UNP P9WKI7 ? ? 'expression tag'        1   16 
1 9DC8 GLY A 141 ? UNP P9WKI7 ? ? linker                  126 17 
1 9DC8 GLY A 142 ? UNP P9WKI7 ? ? linker                  127 18 
2 9DC8 GLY A 420 ? UNP P9WKI7 ? ? 'expression tag'        530 19 
2 9DC8 ASN A 421 ? UNP P9WKI7 ? ? 'expression tag'        531 20 
2 9DC8 SER A 422 ? UNP P9WKI7 ? ? 'expression tag'        532 21 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 23630 ? 
1 MORE         -209  ? 
1 'SSA (A^2)'  47430 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3,4 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z   1.0000000000  0.0000000000  0.0000000000 0.0000000000 0.0000000000  1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 2_555 -x,-y,z -1.0000000000 0.0000000000  0.0000000000 0.0000000000 0.0000000000  -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
3 'crystal symmetry operation' 3_555 -y,x,z  0.0000000000  -1.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
4 'crystal symmetry operation' 4_555 y,-x,z  0.0000000000  1.0000000000  0.0000000000 0.0000000000 -1.0000000000 0.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 61  ? ASP A 63  ? THR A 46  ASP A 48  5 ? 3  
HELX_P HELX_P2  AA2 VAL A 75  ? ALA A 79  ? VAL A 60  ALA A 64  5 ? 5  
HELX_P HELX_P3  AA3 GLU A 105 ? ALA A 115 ? GLU A 90  ALA A 100 1 ? 11 
HELX_P HELX_P4  AA4 PRO A 126 ? ARG A 139 ? PRO A 111 ARG A 124 1 ? 14 
HELX_P HELX_P5  AA5 GLY A 152 ? ALA A 165 ? GLY A 262 ALA A 275 1 ? 14 
HELX_P HELX_P6  AA6 ASN A 179 ? GLY A 194 ? ASN A 289 GLY A 304 1 ? 16 
HELX_P HELX_P7  AA7 THR A 206 ? GLY A 217 ? THR A 316 GLY A 327 1 ? 12 
HELX_P HELX_P8  AA8 THR A 232 ? ALA A 237 ? THR A 342 ALA A 347 1 ? 6  
HELX_P HELX_P9  AA9 PRO A 242 ? ARG A 255 ? PRO A 352 ARG A 365 1 ? 14 
HELX_P HELX_P10 AB1 PRO A 256 ? GLY A 258 ? PRO A 366 GLY A 368 5 ? 3  
HELX_P HELX_P11 AB2 TYR A 269 ? ALA A 279 ? TYR A 379 ALA A 389 1 ? 11 
HELX_P HELX_P12 AB3 GLY A 287 ? GLY A 292 ? GLY A 397 GLY A 402 1 ? 6  
HELX_P HELX_P13 AB4 SER A 316 ? ARG A 321 ? SER A 426 ARG A 431 1 ? 6  
HELX_P HELX_P14 AB5 PRO A 359 ? GLY A 379 ? PRO A 469 GLY A 489 1 ? 21 
HELX_P HELX_P15 AB6 THR A 382 ? GLN A 387 ? THR A 492 GLN A 497 1 ? 6  
HELX_P HELX_P16 AB7 THR A 395 ? GLU A 401 ? THR A 505 GLU A 511 1 ? 7  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLY 
_struct_mon_prot_cis.label_seq_id           202 
_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           GLY 
_struct_mon_prot_cis.auth_seq_id            312 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   ASN 
_struct_mon_prot_cis.pdbx_label_seq_id_2    203 
_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    ASN 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     313 
_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       0.64 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 9 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA3 6 7 ? parallel      
AA3 7 8 ? parallel      
AA3 8 9 ? parallel      
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 65  ? LEU A 67  ? VAL A 50  LEU A 52  
AA1 2 PHE A 391 ? ARG A 393 ? PHE A 501 ARG A 503 
AA2 1 SER A 83  ? GLN A 84  ? SER A 68  GLN A 69  
AA2 2 ARG A 90  ? LEU A 91  ? ARG A 75  LEU A 76  
AA3 1 LEU A 95  ? SER A 97  ? LEU A 80  SER A 82  
AA3 2 MET A 118 ? LEU A 121 ? MET A 103 LEU A 106 
AA3 3 GLY A 146 ? VAL A 149 ? GLY A 256 VAL A 259 
AA3 4 VAL A 169 ? ASP A 173 ? VAL A 279 ASP A 283 
AA3 5 GLU A 198 ? VAL A 204 ? GLU A 308 VAL A 314 
AA3 6 ALA A 220 ? VAL A 223 ? ALA A 330 VAL A 333 
AA3 7 VAL A 261 ? ASP A 264 ? VAL A 371 ASP A 374 
AA3 8 THR A 283 ? LEU A 286 ? THR A 393 LEU A 396 
AA3 9 LEU A 95  ? SER A 97  ? LEU A 80  SER A 82  
AA4 1 ILE A 301 ? VAL A 303 ? ILE A 411 VAL A 413 
AA4 2 LYS A 306 ? ARG A 312 ? LYS A 416 ARG A 422 
AA4 3 GLU A 351 ? PRO A 355 ? GLU A 461 PRO A 465 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 66  ? N LEU A 51  O VAL A 392 ? O VAL A 502 
AA2 1 2 N SER A 83  ? N SER A 68  O LEU A 91  ? O LEU A 76  
AA3 1 2 N SER A 97  ? N SER A 82  O MET A 118 ? O MET A 103 
AA3 2 3 N LEU A 121 ? N LEU A 106 O GLY A 146 ? O GLY A 256 
AA3 3 4 N VAL A 149 ? N VAL A 259 O ASP A 173 ? O ASP A 283 
AA3 4 5 N VAL A 172 ? N VAL A 282 O VAL A 200 ? O VAL A 310 
AA3 5 6 N GLY A 201 ? N GLY A 311 O LYS A 222 ? O LYS A 332 
AA3 6 7 N VAL A 223 ? N VAL A 333 O ILE A 262 ? O ILE A 372 
AA3 7 8 N ALA A 263 ? N ALA A 373 O MET A 285 ? O MET A 395 
AA3 8 9 O LEU A 286 ? O LEU A 396 N VAL A 96  ? N VAL A 81  
AA4 1 2 N VAL A 303 ? N VAL A 413 O LYS A 306 ? O LYS A 416 
AA4 2 3 N TYR A 311 ? N TYR A 421 O GLY A 352 ? O GLY A 462 
# 
_pdbx_entry_details.entry_id                   9DC8 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A HOH 924 ? ? O A HOH 1056 ? ? 1.95 
2 1 OD2 A ASP 264 ? ? O A HOH 901  ? ? 1.96 
3 1 NH1 A ARG 365 ? ? O A HOH 902  ? ? 2.11 
# 
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 VAL A 88  ? ? -127.23 -54.16  
2 1 GLU A 90  ? ? -120.23 -159.87 
3 1 ASN A 109 ? ? -94.33  57.03   
4 1 PRO A 514 ? ? -33.86  107.78  
5 1 ASP A 516 ? ? 63.59   60.67   
6 1 ALA A 518 ? ? -49.31  102.06  
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     1097 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   G 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 1102 ? .    6.70 
2 1 O ? A HOH 1103 ? 7.15 .    
# 
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 -14 ? A MET 1   
2  1 Y 1 A HIS -13 ? A HIS 2   
3  1 Y 1 A HIS -12 ? A HIS 3   
4  1 Y 1 A HIS -11 ? A HIS 4   
5  1 Y 1 A HIS -10 ? A HIS 5   
6  1 Y 1 A HIS -9  ? A HIS 6   
7  1 Y 1 A HIS -8  ? A HIS 7   
8  1 Y 1 A GLY -7  ? A GLY 8   
9  1 Y 1 A GLU -6  ? A GLU 9   
10 1 Y 1 A ASN -5  ? A ASN 10  
11 1 Y 1 A LEU -4  ? A LEU 11  
12 1 Y 1 A TYR -3  ? A TYR 12  
13 1 Y 1 A PHE -2  ? A PHE 13  
14 1 Y 1 A GLN -1  ? A GLN 14  
15 1 Y 1 A GLY 0   ? A GLY 15  
16 1 Y 1 A SER 1   ? A SER 16  
17 1 Y 1 A SER 2   ? A SER 17  
18 1 Y 1 A ARG 3   ? A ARG 18  
19 1 Y 1 A GLY 4   ? A GLY 19  
20 1 Y 1 A MET 5   ? A MET 20  
21 1 Y 1 A SER 6   ? A SER 21  
22 1 Y 1 A GLY 7   ? A GLY 22  
23 1 Y 1 A LEU 8   ? A LEU 23  
24 1 Y 1 A GLU 9   ? A GLU 24  
25 1 Y 1 A ASP 10  ? A ASP 25  
26 1 Y 1 A SER 11  ? A SER 26  
27 1 Y 1 A SER 12  ? A SER 27  
28 1 Y 1 A ASP 13  ? A ASP 28  
29 1 Y 1 A LEU 14  ? A LEU 29  
30 1 Y 1 A VAL 15  ? A VAL 30  
31 1 Y 1 A VAL 16  ? A VAL 31  
32 1 Y 1 A SER 17  ? A SER 32  
33 1 Y 1 A PRO 18  ? A PRO 33  
34 1 Y 1 A TYR 19  ? A TYR 34  
35 1 Y 1 A VAL 20  ? A VAL 35  
36 1 Y 1 A ARG 21  ? A ARG 36  
37 1 Y 1 A MET 22  ? A MET 37  
38 1 Y 1 A GLY 23  ? A GLY 38  
39 1 Y 1 A GLY 24  ? A GLY 39  
40 1 Y 1 A LEU 25  ? A LEU 40  
41 1 Y 1 A THR 26  ? A THR 41  
42 1 Y 1 A GLY 432 ? A GLY 322 
43 1 Y 1 A ARG 433 ? A ARG 323 
44 1 Y 1 A GLY 434 ? A GLY 324 
45 1 Y 1 A GLY 435 ? A GLY 325 
46 1 Y 1 A ALA 436 ? A ALA 326 
47 1 Y 1 A THR 437 ? A THR 327 
48 1 Y 1 A SER 438 ? A SER 328 
49 1 Y 1 A TYR 439 ? A TYR 329 
50 1 Y 1 A SER 440 ? A SER 330 
51 1 Y 1 A LYS 441 ? A LYS 331 
52 1 Y 1 A ASP 442 ? A ASP 332 
53 1 Y 1 A ARG 443 ? A ARG 333 
54 1 Y 1 A TYR 444 ? A TYR 334 
55 1 Y 1 A PHE 445 ? A PHE 335 
56 1 Y 1 A ALA 446 ? A ALA 336 
57 1 Y 1 A ASP 447 ? A ASP 337 
58 1 Y 1 A ASP 448 ? A ASP 338 
59 1 Y 1 A ALA 449 ? A ALA 339 
60 1 Y 1 A LEU 450 ? A LEU 340 
61 1 Y 1 A SER 451 ? A SER 341 
62 1 Y 1 A GLU 452 ? A GLU 342 
63 1 Y 1 A ASP 453 ? A ASP 343 
64 1 Y 1 A LYS 454 ? A LYS 344 
65 1 Y 1 A TYR 526 ? A TYR 416 
66 1 Y 1 A TYR 527 ? A TYR 417 
67 1 Y 1 A ALA 528 ? A ALA 418 
68 1 Y 1 A ARG 529 ? A ARG 419 
69 1 Y 1 A GLY 530 ? A GLY 420 
70 1 Y 1 A ASN 531 ? A ASN 421 
71 1 Y 1 A SER 532 ? A SER 422 
# 
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 
IMP P      P  N N 183 
IMP O1P    O  N N 184 
IMP O2P    O  N N 185 
IMP O3P    O  N N 186 
IMP "O5'"  O  N N 187 
IMP "C5'"  C  N N 188 
IMP "C4'"  C  N R 189 
IMP "O4'"  O  N N 190 
IMP "C3'"  C  N S 191 
IMP "O3'"  O  N N 192 
IMP "C2'"  C  N R 193 
IMP "O2'"  O  N N 194 
IMP "C1'"  C  N R 195 
IMP N9     N  Y N 196 
IMP C8     C  Y N 197 
IMP N7     N  Y N 198 
IMP C5     C  Y N 199 
IMP C6     C  N N 200 
IMP O6     O  N N 201 
IMP N1     N  N N 202 
IMP C2     C  N N 203 
IMP N3     N  N N 204 
IMP C4     C  Y N 205 
IMP HOP2   H  N N 206 
IMP HOP3   H  N N 207 
IMP "H5'1" H  N N 208 
IMP "H5'2" H  N N 209 
IMP "H4'"  H  N N 210 
IMP "H3'"  H  N N 211 
IMP "HO3'" H  N N 212 
IMP "H2'"  H  N N 213 
IMP "HO2'" H  N N 214 
IMP "H1'"  H  N N 215 
IMP H8     H  N N 216 
IMP HN1    H  N N 217 
IMP H2     H  N N 218 
LEU N      N  N N 219 
LEU CA     C  N S 220 
LEU C      C  N N 221 
LEU O      O  N N 222 
LEU CB     C  N N 223 
LEU CG     C  N N 224 
LEU CD1    C  N N 225 
LEU CD2    C  N N 226 
LEU OXT    O  N N 227 
LEU H      H  N N 228 
LEU H2     H  N N 229 
LEU HA     H  N N 230 
LEU HB2    H  N N 231 
LEU HB3    H  N N 232 
LEU HG     H  N N 233 
LEU HD11   H  N N 234 
LEU HD12   H  N N 235 
LEU HD13   H  N N 236 
LEU HD21   H  N N 237 
LEU HD22   H  N N 238 
LEU HD23   H  N N 239 
LEU HXT    H  N N 240 
LYS N      N  N N 241 
LYS CA     C  N S 242 
LYS C      C  N N 243 
LYS O      O  N N 244 
LYS CB     C  N N 245 
LYS CG     C  N N 246 
LYS CD     C  N N 247 
LYS CE     C  N N 248 
LYS NZ     N  N N 249 
LYS OXT    O  N N 250 
LYS H      H  N N 251 
LYS H2     H  N N 252 
LYS HA     H  N N 253 
LYS HB2    H  N N 254 
LYS HB3    H  N N 255 
LYS HG2    H  N N 256 
LYS HG3    H  N N 257 
LYS HD2    H  N N 258 
LYS HD3    H  N N 259 
LYS HE2    H  N N 260 
LYS HE3    H  N N 261 
LYS HZ1    H  N N 262 
LYS HZ2    H  N N 263 
LYS HZ3    H  N N 264 
LYS HXT    H  N N 265 
MET N      N  N N 266 
MET CA     C  N S 267 
MET C      C  N N 268 
MET O      O  N N 269 
MET CB     C  N N 270 
MET CG     C  N N 271 
MET SD     S  N N 272 
MET CE     C  N N 273 
MET OXT    O  N N 274 
MET H      H  N N 275 
MET H2     H  N N 276 
MET HA     H  N N 277 
MET HB2    H  N N 278 
MET HB3    H  N N 279 
MET HG2    H  N N 280 
MET HG3    H  N N 281 
MET HE1    H  N N 282 
MET HE2    H  N N 283 
MET HE3    H  N N 284 
MET HXT    H  N N 285 
PHE N      N  N N 286 
PHE CA     C  N S 287 
PHE C      C  N N 288 
PHE O      O  N N 289 
PHE CB     C  N N 290 
PHE CG     C  Y N 291 
PHE CD1    C  Y N 292 
PHE CD2    C  Y N 293 
PHE CE1    C  Y N 294 
PHE CE2    C  Y N 295 
PHE CZ     C  Y N 296 
PHE OXT    O  N N 297 
PHE H      H  N N 298 
PHE H2     H  N N 299 
PHE HA     H  N N 300 
PHE HB2    H  N N 301 
PHE HB3    H  N N 302 
PHE HD1    H  N N 303 
PHE HD2    H  N N 304 
PHE HE1    H  N N 305 
PHE HE2    H  N N 306 
PHE HZ     H  N N 307 
PHE HXT    H  N N 308 
PRO N      N  N N 309 
PRO CA     C  N S 310 
PRO C      C  N N 311 
PRO O      O  N N 312 
PRO CB     C  N N 313 
PRO CG     C  N N 314 
PRO CD     C  N N 315 
PRO OXT    O  N N 316 
PRO H      H  N N 317 
PRO HA     H  N N 318 
PRO HB2    H  N N 319 
PRO HB3    H  N N 320 
PRO HG2    H  N N 321 
PRO HG3    H  N N 322 
PRO HD2    H  N N 323 
PRO HD3    H  N N 324 
PRO HXT    H  N N 325 
SER N      N  N N 326 
SER CA     C  N S 327 
SER C      C  N N 328 
SER O      O  N N 329 
SER CB     C  N N 330 
SER OG     O  N N 331 
SER OXT    O  N N 332 
SER H      H  N N 333 
SER H2     H  N N 334 
SER HA     H  N N 335 
SER HB2    H  N N 336 
SER HB3    H  N N 337 
SER HG     H  N N 338 
SER HXT    H  N N 339 
SO4 S      S  N N 340 
SO4 O1     O  N N 341 
SO4 O2     O  N N 342 
SO4 O3     O  N N 343 
SO4 O4     O  N N 344 
THR N      N  N N 345 
THR CA     C  N S 346 
THR C      C  N N 347 
THR O      O  N N 348 
THR CB     C  N R 349 
THR OG1    O  N N 350 
THR CG2    C  N N 351 
THR OXT    O  N N 352 
THR H      H  N N 353 
THR H2     H  N N 354 
THR HA     H  N N 355 
THR HB     H  N N 356 
THR HG1    H  N N 357 
THR HG21   H  N N 358 
THR HG22   H  N N 359 
THR HG23   H  N N 360 
THR HXT    H  N N 361 
TRP N      N  N N 362 
TRP CA     C  N S 363 
TRP C      C  N N 364 
TRP O      O  N N 365 
TRP CB     C  N N 366 
TRP CG     C  Y N 367 
TRP CD1    C  Y N 368 
TRP CD2    C  Y N 369 
TRP NE1    N  Y N 370 
TRP CE2    C  Y N 371 
TRP CE3    C  Y N 372 
TRP CZ2    C  Y N 373 
TRP CZ3    C  Y N 374 
TRP CH2    C  Y N 375 
TRP OXT    O  N N 376 
TRP H      H  N N 377 
TRP H2     H  N N 378 
TRP HA     H  N N 379 
TRP HB2    H  N N 380 
TRP HB3    H  N N 381 
TRP HD1    H  N N 382 
TRP HE1    H  N N 383 
TRP HE3    H  N N 384 
TRP HZ2    H  N N 385 
TRP HZ3    H  N N 386 
TRP HH2    H  N N 387 
TRP HXT    H  N N 388 
TYR N      N  N N 389 
TYR CA     C  N S 390 
TYR C      C  N N 391 
TYR O      O  N N 392 
TYR CB     C  N N 393 
TYR CG     C  Y N 394 
TYR CD1    C  Y N 395 
TYR CD2    C  Y N 396 
TYR CE1    C  Y N 397 
TYR CE2    C  Y N 398 
TYR CZ     C  Y N 399 
TYR OH     O  N N 400 
TYR OXT    O  N N 401 
TYR H      H  N N 402 
TYR H2     H  N N 403 
TYR HA     H  N N 404 
TYR HB2    H  N N 405 
TYR HB3    H  N N 406 
TYR HD1    H  N N 407 
TYR HD2    H  N N 408 
TYR HE1    H  N N 409 
TYR HE2    H  N N 410 
TYR HH     H  N N 411 
TYR HXT    H  N N 412 
VAL N      N  N N 413 
VAL CA     C  N S 414 
VAL C      C  N N 415 
VAL O      O  N N 416 
VAL CB     C  N N 417 
VAL CG1    C  N N 418 
VAL CG2    C  N N 419 
VAL OXT    O  N N 420 
VAL H      H  N N 421 
VAL H2     H  N N 422 
VAL HA     H  N N 423 
VAL HB     H  N N 424 
VAL HG11   H  N N 425 
VAL HG12   H  N N 426 
VAL HG13   H  N N 427 
VAL HG21   H  N N 428 
VAL HG22   H  N N 429 
VAL HG23   H  N N 430 
VAL HXT    H  N N 431 
VOA C4     C  N N 432 
VOA C7     C  Y N 433 
VOA C8     C  Y N 434 
VOA C9     C  Y N 435 
VOA C10    C  Y N 436 
VOA C12    C  Y N 437 
VOA C1     C  N N 438 
VOA C15    C  Y N 439 
VOA C16    C  Y N 440 
VOA C17    C  Y N 441 
VOA C18    C  Y N 442 
VOA C19    C  Y N 443 
VOA C2     C  N S 444 
VOA C20    C  Y N 445 
VOA C21    C  Y N 446 
VOA C22    C  Y N 447 
VOA C23    C  Y N 448 
VOA C25    C  N N 449 
VOA C27    C  N N 450 
VOA C28    C  N N 451 
VOA N11    N  Y N 452 
VOA N14    N  N N 453 
VOA N24    N  Y N 454 
VOA N6     N  N N 455 
VOA O26    O  N N 456 
VOA O5     O  N N 457 
VOA CL13   CL N N 458 
VOA H1     H  N N 459 
VOA H2     H  N N 460 
VOA H4     H  N N 461 
VOA H7     H  N N 462 
VOA H6     H  N N 463 
VOA H5     H  N N 464 
VOA H8     H  N N 465 
VOA H9     H  N N 466 
VOA H3     H  N N 467 
VOA H10    H  N N 468 
VOA H11    H  N N 469 
VOA H13    H  N N 470 
VOA H12    H  N N 471 
VOA H14    H  N N 472 
VOA H15    H  N N 473 
VOA H17    H  N N 474 
VOA H16    H  N N 475 
VOA H18    H  N N 476 
VOA H19    H  N N 477 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
GLN N     CA     sing N N 83  
GLN N     H      sing N N 84  
GLN N     H2     sing N N 85  
GLN CA    C      sing N N 86  
GLN CA    CB     sing N N 87  
GLN CA    HA     sing N N 88  
GLN C     O      doub N N 89  
GLN C     OXT    sing N N 90  
GLN CB    CG     sing N N 91  
GLN CB    HB2    sing N N 92  
GLN CB    HB3    sing N N 93  
GLN CG    CD     sing N N 94  
GLN CG    HG2    sing N N 95  
GLN CG    HG3    sing N N 96  
GLN CD    OE1    doub N N 97  
GLN CD    NE2    sing N N 98  
GLN NE2   HE21   sing N N 99  
GLN NE2   HE22   sing N N 100 
GLN OXT   HXT    sing N N 101 
GLU N     CA     sing N N 102 
GLU N     H      sing N N 103 
GLU N     H2     sing N N 104 
GLU CA    C      sing N N 105 
GLU CA    CB     sing N N 106 
GLU CA    HA     sing N N 107 
GLU C     O      doub N N 108 
GLU C     OXT    sing N N 109 
GLU CB    CG     sing N N 110 
GLU CB    HB2    sing N N 111 
GLU CB    HB3    sing N N 112 
GLU CG    CD     sing N N 113 
GLU CG    HG2    sing N N 114 
GLU CG    HG3    sing N N 115 
GLU CD    OE1    doub N N 116 
GLU CD    OE2    sing N N 117 
GLU OE2   HE2    sing N N 118 
GLU OXT   HXT    sing N N 119 
GLY N     CA     sing N N 120 
GLY N     H      sing N N 121 
GLY N     H2     sing N N 122 
GLY CA    C      sing N N 123 
GLY CA    HA2    sing N N 124 
GLY CA    HA3    sing N N 125 
GLY C     O      doub N N 126 
GLY C     OXT    sing N N 127 
GLY OXT   HXT    sing N N 128 
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 
IMP P     O1P    doub N N 173 
IMP P     O2P    sing N N 174 
IMP P     O3P    sing N N 175 
IMP P     "O5'"  sing N N 176 
IMP O2P   HOP2   sing N N 177 
IMP O3P   HOP3   sing N N 178 
IMP "O5'" "C5'"  sing N N 179 
IMP "C5'" "C4'"  sing N N 180 
IMP "C5'" "H5'1" sing N N 181 
IMP "C5'" "H5'2" sing N N 182 
IMP "C4'" "O4'"  sing N N 183 
IMP "C4'" "C3'"  sing N N 184 
IMP "C4'" "H4'"  sing N N 185 
IMP "O4'" "C1'"  sing N N 186 
IMP "C3'" "O3'"  sing N N 187 
IMP "C3'" "C2'"  sing N N 188 
IMP "C3'" "H3'"  sing N N 189 
IMP "O3'" "HO3'" sing N N 190 
IMP "C2'" "O2'"  sing N N 191 
IMP "C2'" "C1'"  sing N N 192 
IMP "C2'" "H2'"  sing N N 193 
IMP "O2'" "HO2'" sing N N 194 
IMP "C1'" N9     sing N N 195 
IMP "C1'" "H1'"  sing N N 196 
IMP N9    C8     sing Y N 197 
IMP N9    C4     sing Y N 198 
IMP C8    N7     doub Y N 199 
IMP C8    H8     sing N N 200 
IMP N7    C5     sing Y N 201 
IMP C5    C6     sing N N 202 
IMP C5    C4     doub Y N 203 
IMP C6    O6     doub N N 204 
IMP C6    N1     sing N N 205 
IMP N1    C2     sing N N 206 
IMP N1    HN1    sing N N 207 
IMP C2    N3     doub N N 208 
IMP C2    H2     sing N N 209 
IMP N3    C4     sing N N 210 
LEU N     CA     sing N N 211 
LEU N     H      sing N N 212 
LEU N     H2     sing N N 213 
LEU CA    C      sing N N 214 
LEU CA    CB     sing N N 215 
LEU CA    HA     sing N N 216 
LEU C     O      doub N N 217 
LEU C     OXT    sing N N 218 
LEU CB    CG     sing N N 219 
LEU CB    HB2    sing N N 220 
LEU CB    HB3    sing N N 221 
LEU CG    CD1    sing N N 222 
LEU CG    CD2    sing N N 223 
LEU CG    HG     sing N N 224 
LEU CD1   HD11   sing N N 225 
LEU CD1   HD12   sing N N 226 
LEU CD1   HD13   sing N N 227 
LEU CD2   HD21   sing N N 228 
LEU CD2   HD22   sing N N 229 
LEU CD2   HD23   sing N N 230 
LEU OXT   HXT    sing N N 231 
LYS N     CA     sing N N 232 
LYS N     H      sing N N 233 
LYS N     H2     sing N N 234 
LYS CA    C      sing N N 235 
LYS CA    CB     sing N N 236 
LYS CA    HA     sing N N 237 
LYS C     O      doub N N 238 
LYS C     OXT    sing N N 239 
LYS CB    CG     sing N N 240 
LYS CB    HB2    sing N N 241 
LYS CB    HB3    sing N N 242 
LYS CG    CD     sing N N 243 
LYS CG    HG2    sing N N 244 
LYS CG    HG3    sing N N 245 
LYS CD    CE     sing N N 246 
LYS CD    HD2    sing N N 247 
LYS CD    HD3    sing N N 248 
LYS CE    NZ     sing N N 249 
LYS CE    HE2    sing N N 250 
LYS CE    HE3    sing N N 251 
LYS NZ    HZ1    sing N N 252 
LYS NZ    HZ2    sing N N 253 
LYS NZ    HZ3    sing N N 254 
LYS OXT   HXT    sing N N 255 
MET N     CA     sing N N 256 
MET N     H      sing N N 257 
MET N     H2     sing N N 258 
MET CA    C      sing N N 259 
MET CA    CB     sing N N 260 
MET CA    HA     sing N N 261 
MET C     O      doub N N 262 
MET C     OXT    sing N N 263 
MET CB    CG     sing N N 264 
MET CB    HB2    sing N N 265 
MET CB    HB3    sing N N 266 
MET CG    SD     sing N N 267 
MET CG    HG2    sing N N 268 
MET CG    HG3    sing N N 269 
MET SD    CE     sing N N 270 
MET CE    HE1    sing N N 271 
MET CE    HE2    sing N N 272 
MET CE    HE3    sing N N 273 
MET OXT   HXT    sing N N 274 
PHE N     CA     sing N N 275 
PHE N     H      sing N N 276 
PHE N     H2     sing N N 277 
PHE CA    C      sing N N 278 
PHE CA    CB     sing N N 279 
PHE CA    HA     sing N N 280 
PHE C     O      doub N N 281 
PHE C     OXT    sing N N 282 
PHE CB    CG     sing N N 283 
PHE CB    HB2    sing N N 284 
PHE CB    HB3    sing N N 285 
PHE CG    CD1    doub Y N 286 
PHE CG    CD2    sing Y N 287 
PHE CD1   CE1    sing Y N 288 
PHE CD1   HD1    sing N N 289 
PHE CD2   CE2    doub Y N 290 
PHE CD2   HD2    sing N N 291 
PHE CE1   CZ     doub Y N 292 
PHE CE1   HE1    sing N N 293 
PHE CE2   CZ     sing Y N 294 
PHE CE2   HE2    sing N N 295 
PHE CZ    HZ     sing N N 296 
PHE OXT   HXT    sing N N 297 
PRO N     CA     sing N N 298 
PRO N     CD     sing N N 299 
PRO N     H      sing N N 300 
PRO CA    C      sing N N 301 
PRO CA    CB     sing N N 302 
PRO CA    HA     sing N N 303 
PRO C     O      doub N N 304 
PRO C     OXT    sing N N 305 
PRO CB    CG     sing N N 306 
PRO CB    HB2    sing N N 307 
PRO CB    HB3    sing N N 308 
PRO CG    CD     sing N N 309 
PRO CG    HG2    sing N N 310 
PRO CG    HG3    sing N N 311 
PRO CD    HD2    sing N N 312 
PRO CD    HD3    sing N N 313 
PRO OXT   HXT    sing N N 314 
SER N     CA     sing N N 315 
SER N     H      sing N N 316 
SER N     H2     sing N N 317 
SER CA    C      sing N N 318 
SER CA    CB     sing N N 319 
SER CA    HA     sing N N 320 
SER C     O      doub N N 321 
SER C     OXT    sing N N 322 
SER CB    OG     sing N N 323 
SER CB    HB2    sing N N 324 
SER CB    HB3    sing N N 325 
SER OG    HG     sing N N 326 
SER OXT   HXT    sing N N 327 
SO4 S     O1     doub N N 328 
SO4 S     O2     doub N N 329 
SO4 S     O3     sing N N 330 
SO4 S     O4     sing N N 331 
THR N     CA     sing N N 332 
THR N     H      sing N N 333 
THR N     H2     sing N N 334 
THR CA    C      sing N N 335 
THR CA    CB     sing N N 336 
THR CA    HA     sing N N 337 
THR C     O      doub N N 338 
THR C     OXT    sing N N 339 
THR CB    OG1    sing N N 340 
THR CB    CG2    sing N N 341 
THR CB    HB     sing N N 342 
THR OG1   HG1    sing N N 343 
THR CG2   HG21   sing N N 344 
THR CG2   HG22   sing N N 345 
THR CG2   HG23   sing N N 346 
THR OXT   HXT    sing N N 347 
TRP N     CA     sing N N 348 
TRP N     H      sing N N 349 
TRP N     H2     sing N N 350 
TRP CA    C      sing N N 351 
TRP CA    CB     sing N N 352 
TRP CA    HA     sing N N 353 
TRP C     O      doub N N 354 
TRP C     OXT    sing N N 355 
TRP CB    CG     sing N N 356 
TRP CB    HB2    sing N N 357 
TRP CB    HB3    sing N N 358 
TRP CG    CD1    doub Y N 359 
TRP CG    CD2    sing Y N 360 
TRP CD1   NE1    sing Y N 361 
TRP CD1   HD1    sing N N 362 
TRP CD2   CE2    doub Y N 363 
TRP CD2   CE3    sing Y N 364 
TRP NE1   CE2    sing Y N 365 
TRP NE1   HE1    sing N N 366 
TRP CE2   CZ2    sing Y N 367 
TRP CE3   CZ3    doub Y N 368 
TRP CE3   HE3    sing N N 369 
TRP CZ2   CH2    doub Y N 370 
TRP CZ2   HZ2    sing N N 371 
TRP CZ3   CH2    sing Y N 372 
TRP CZ3   HZ3    sing N N 373 
TRP CH2   HH2    sing N N 374 
TRP OXT   HXT    sing N N 375 
TYR N     CA     sing N N 376 
TYR N     H      sing N N 377 
TYR N     H2     sing N N 378 
TYR CA    C      sing N N 379 
TYR CA    CB     sing N N 380 
TYR CA    HA     sing N N 381 
TYR C     O      doub N N 382 
TYR C     OXT    sing N N 383 
TYR CB    CG     sing N N 384 
TYR CB    HB2    sing N N 385 
TYR CB    HB3    sing N N 386 
TYR CG    CD1    doub Y N 387 
TYR CG    CD2    sing Y N 388 
TYR CD1   CE1    sing Y N 389 
TYR CD1   HD1    sing N N 390 
TYR CD2   CE2    doub Y N 391 
TYR CD2   HD2    sing N N 392 
TYR CE1   CZ     doub Y N 393 
TYR CE1   HE1    sing N N 394 
TYR CE2   CZ     sing Y N 395 
TYR CE2   HE2    sing N N 396 
TYR CZ    OH     sing N N 397 
TYR OH    HH     sing N N 398 
TYR OXT   HXT    sing N N 399 
VAL N     CA     sing N N 400 
VAL N     H      sing N N 401 
VAL N     H2     sing N N 402 
VAL CA    C      sing N N 403 
VAL CA    CB     sing N N 404 
VAL CA    HA     sing N N 405 
VAL C     O      doub N N 406 
VAL C     OXT    sing N N 407 
VAL CB    CG1    sing N N 408 
VAL CB    CG2    sing N N 409 
VAL CB    HB     sing N N 410 
VAL CG1   HG11   sing N N 411 
VAL CG1   HG12   sing N N 412 
VAL CG1   HG13   sing N N 413 
VAL CG2   HG21   sing N N 414 
VAL CG2   HG22   sing N N 415 
VAL CG2   HG23   sing N N 416 
VAL OXT   HXT    sing N N 417 
VOA C1    C2     sing N N 418 
VOA N14   C15    sing N N 419 
VOA N14   C2     sing N N 420 
VOA C16   C17    doub Y N 421 
VOA C16   C15    sing Y N 422 
VOA C17   C18    sing Y N 423 
VOA C15   C20    doub Y N 424 
VOA C2    C4     sing N N 425 
VOA C20   C19    sing Y N 426 
VOA C18   N24    doub Y N 427 
VOA C18   C19    sing Y N 428 
VOA N24   C23    sing Y N 429 
VOA C19   C21    doub Y N 430 
VOA C4    O5     doub N N 431 
VOA C4    N6     sing N N 432 
VOA C23   C22    doub Y N 433 
VOA N6    C7     sing N N 434 
VOA C21   C22    sing Y N 435 
VOA C21   C28    sing N N 436 
VOA C22   C25    sing N N 437 
VOA C28   C27    sing N N 438 
VOA C7    C12    doub Y N 439 
VOA C7    C8     sing Y N 440 
VOA C25   O26    sing N N 441 
VOA O26   C27    sing N N 442 
VOA C12   N11    sing Y N 443 
VOA C8    C9     doub Y N 444 
VOA N11   C10    doub Y N 445 
VOA C9    C10    sing Y N 446 
VOA C10   CL13   sing N N 447 
VOA C8    H1     sing N N 448 
VOA C9    H2     sing N N 449 
VOA C12   H4     sing N N 450 
VOA C1    H7     sing N N 451 
VOA C1    H6     sing N N 452 
VOA C1    H5     sing N N 453 
VOA C16   H8     sing N N 454 
VOA C17   H9     sing N N 455 
VOA C2    H3     sing N N 456 
VOA C20   H10    sing N N 457 
VOA C23   H11    sing N N 458 
VOA C25   H13    sing N N 459 
VOA C25   H12    sing N N 460 
VOA C27   H14    sing N N 461 
VOA C27   H15    sing N N 462 
VOA C28   H17    sing N N 463 
VOA C28   H16    sing N N 464 
VOA N14   H18    sing N N 465 
VOA N6    H19    sing N N 466 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4IX2 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9DC8 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.011162 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011162 
_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]   0.011641 
_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  
CL 
H  
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . THR A 1 42  ? 16.904  5.878   28.126  1.00 66.93 ? 27   THR A N     1 
ATOM   2    C  CA    . THR A 1 42  ? 15.532  5.905   27.636  1.00 67.06 ? 27   THR A CA    1 
ATOM   3    C  C     . THR A 1 42  ? 15.470  5.568   26.144  1.00 64.87 ? 27   THR A C     1 
ATOM   4    O  O     . THR A 1 42  ? 16.297  6.024   25.348  1.00 64.92 ? 27   THR A O     1 
ATOM   5    C  CB    . THR A 1 42  ? 14.876  7.276   27.889  1.00 68.68 ? 27   THR A CB    1 
ATOM   6    O  OG1   . THR A 1 42  ? 13.494  7.232   27.511  1.00 69.51 ? 27   THR A OG1   1 
ATOM   7    C  CG2   . THR A 1 42  ? 15.582  8.362   27.096  1.00 69.83 ? 27   THR A CG2   1 
ATOM   8    N  N     . ASP A 1 43  ? 14.470  4.769   25.771  1.00 61.78 ? 28   ASP A N     1 
ATOM   9    C  CA    . ASP A 1 43  ? 14.392  4.228   24.424  1.00 57.62 ? 28   ASP A CA    1 
ATOM   10   C  C     . ASP A 1 43  ? 13.919  5.291   23.431  1.00 50.23 ? 28   ASP A C     1 
ATOM   11   O  O     . ASP A 1 43  ? 13.161  6.198   23.789  1.00 49.54 ? 28   ASP A O     1 
ATOM   12   C  CB    . ASP A 1 43  ? 13.444  3.033   24.381  1.00 60.49 ? 28   ASP A CB    1 
ATOM   13   C  CG    . ASP A 1 43  ? 13.819  1.947   25.374  1.00 62.59 ? 28   ASP A CG    1 
ATOM   14   O  OD1   . ASP A 1 43  ? 14.865  2.086   26.044  1.00 63.29 ? 28   ASP A OD1   1 
ATOM   15   O  OD2   . ASP A 1 43  ? 13.064  0.956   25.484  1.00 63.23 ? 28   ASP A OD2   1 
ATOM   16   N  N     . PRO A 1 44  ? 14.333  5.186   22.170  1.00 43.51 ? 29   PRO A N     1 
ATOM   17   C  CA    . PRO A 1 44  ? 13.908  6.172   21.171  1.00 37.95 ? 29   PRO A CA    1 
ATOM   18   C  C     . PRO A 1 44  ? 12.457  5.978   20.756  1.00 32.91 ? 29   PRO A C     1 
ATOM   19   O  O     . PRO A 1 44  ? 11.848  4.922   20.949  1.00 32.46 ? 29   PRO A O     1 
ATOM   20   C  CB    . PRO A 1 44  ? 14.853  5.913   19.995  1.00 38.71 ? 29   PRO A CB    1 
ATOM   21   C  CG    . PRO A 1 44  ? 15.186  4.462   20.118  1.00 40.89 ? 29   PRO A CG    1 
ATOM   22   C  CD    . PRO A 1 44  ? 15.250  4.183   21.600  1.00 41.93 ? 29   PRO A CD    1 
ATOM   23   N  N     . VAL A 1 45  ? 11.901  7.039   20.181  1.00 28.27 ? 30   VAL A N     1 
ATOM   24   C  CA    . VAL A 1 45  ? 10.612  6.901   19.498  1.00 25.86 ? 30   VAL A CA    1 
ATOM   25   C  C     . VAL A 1 45  ? 10.783  5.922   18.344  1.00 24.91 ? 30   VAL A C     1 
ATOM   26   O  O     . VAL A 1 45  ? 11.805  5.983   17.634  1.00 26.07 ? 30   VAL A O     1 
ATOM   27   C  CB    . VAL A 1 45  ? 10.130  8.272   18.999  1.00 23.78 ? 30   VAL A CB    1 
ATOM   28   C  CG1   . VAL A 1 45  ? 8.791   8.152   18.294  1.00 25.25 ? 30   VAL A CG1   1 
ATOM   29   C  CG2   . VAL A 1 45  ? 10.057  9.255   20.169  1.00 25.73 ? 30   VAL A CG2   1 
ATOM   30   N  N     . PRO A 1 46  ? 9.850   4.997   18.107  1.00 26.01 ? 31   PRO A N     1 
ATOM   31   C  CA    . PRO A 1 46  ? 10.112  3.941   17.112  1.00 25.86 ? 31   PRO A CA    1 
ATOM   32   C  C     . PRO A 1 46  ? 10.297  4.454   15.686  1.00 24.15 ? 31   PRO A C     1 
ATOM   33   O  O     . PRO A 1 46  ? 10.919  3.750   14.882  1.00 26.89 ? 31   PRO A O     1 
ATOM   34   C  CB    . PRO A 1 46  ? 8.890   3.016   17.237  1.00 28.08 ? 31   PRO A CB    1 
ATOM   35   C  CG    . PRO A 1 46  ? 7.862   3.804   17.973  1.00 31.59 ? 31   PRO A CG    1 
ATOM   36   C  CD    . PRO A 1 46  ? 8.599   4.775   18.849  1.00 29.11 ? 31   PRO A CD    1 
ATOM   37   N  N     . THR A 1 47  ? 9.820   5.658   15.350  1.00 20.56 ? 32   THR A N     1 
ATOM   38   C  CA    . THR A 1 47  ? 10.068  6.258   14.036  1.00 18.86 ? 32   THR A CA    1 
ATOM   39   C  C     . THR A 1 47  ? 11.253  7.231   14.023  1.00 18.98 ? 32   THR A C     1 
ATOM   40   O  O     . THR A 1 47  ? 11.536  7.829   12.975  1.00 18.99 ? 32   THR A O     1 
ATOM   41   C  CB    . THR A 1 47  ? 8.808   6.973   13.516  1.00 19.24 ? 32   THR A CB    1 
ATOM   42   O  OG1   . THR A 1 47  ? 8.276   7.816   14.544  1.00 20.19 ? 32   THR A OG1   1 
ATOM   43   C  CG2   . THR A 1 47  ? 7.732   5.959   13.086  1.00 20.16 ? 32   THR A CG2   1 
ATOM   44   N  N     . GLY A 1 48  ? 11.959  7.397   15.143  1.00 18.02 ? 33   GLY A N     1 
ATOM   45   C  CA    . GLY A 1 48  ? 13.188  8.179   15.149  1.00 18.07 ? 33   GLY A CA    1 
ATOM   46   C  C     . GLY A 1 48  ? 13.226  9.383   16.072  1.00 18.75 ? 33   GLY A C     1 
ATOM   47   O  O     . GLY A 1 48  ? 12.223  10.090  16.243  1.00 19.50 ? 33   GLY A O     1 
ATOM   48   N  N     . GLY A 1 49  ? 14.405  9.648   16.647  1.00 18.91 ? 34   GLY A N     1 
ATOM   49   C  CA    . GLY A 1 49  ? 14.577  10.721  17.615  1.00 19.49 ? 34   GLY A CA    1 
ATOM   50   C  C     . GLY A 1 49  ? 13.999  10.378  18.981  1.00 21.82 ? 34   GLY A C     1 
ATOM   51   O  O     . GLY A 1 49  ? 13.527  9.265   19.234  1.00 22.34 ? 34   GLY A O     1 
ATOM   52   N  N     . ASP A 1 50  ? 14.022  11.376  19.874  1.00 23.09 ? 35   ASP A N     1 
ATOM   53   C  CA    . ASP A 1 50  ? 13.551  11.215  21.250  1.00 23.16 ? 35   ASP A CA    1 
ATOM   54   C  C     . ASP A 1 50  ? 12.321  12.063  21.573  1.00 23.99 ? 35   ASP A C     1 
ATOM   55   O  O     . ASP A 1 50  ? 11.902  12.108  22.740  1.00 25.97 ? 35   ASP A O     1 
ATOM   56   C  CB    . ASP A 1 50  ? 14.669  11.548  22.247  1.00 26.41 ? 35   ASP A CB    1 
ATOM   57   C  CG    . ASP A 1 50  ? 15.858  10.596  22.148  1.00 28.19 ? 35   ASP A CG    1 
ATOM   58   O  OD1   . ASP A 1 50  ? 15.667  9.374   21.948  1.00 29.10 ? 35   ASP A OD1   1 
ATOM   59   O  OD2   . ASP A 1 50  ? 16.999  11.081  22.262  1.00 29.40 ? 35   ASP A OD2   1 
ATOM   60   N  N     . ASP A 1 51  ? 11.724  12.726  20.581  1.00 23.05 ? 36   ASP A N     1 
ATOM   61   C  CA    . ASP A 1 51  ? 10.592  13.623  20.794  1.00 22.09 ? 36   ASP A CA    1 
ATOM   62   C  C     . ASP A 1 51  ? 9.316   12.939  20.322  1.00 22.48 ? 36   ASP A C     1 
ATOM   63   O  O     . ASP A 1 51  ? 9.113   12.811  19.107  1.00 20.93 ? 36   ASP A O     1 
ATOM   64   C  CB    . ASP A 1 51  ? 10.812  14.936  20.034  1.00 21.67 ? 36   ASP A CB    1 
ATOM   65   C  CG    . ASP A 1 51  ? 9.654   15.924  20.169  1.00 23.64 ? 36   ASP A CG    1 
ATOM   66   O  OD1   . ASP A 1 51  ? 8.646   15.636  20.867  1.00 23.45 ? 36   ASP A OD1   1 
ATOM   67   O  OD2   . ASP A 1 51  ? 9.766   17.016  19.556  1.00 25.45 ? 36   ASP A OD2   1 
ATOM   68   N  N     . PRO A 1 52  ? 8.429   12.495  21.220  1.00 24.69 ? 37   PRO A N     1 
ATOM   69   C  CA    . PRO A 1 52  ? 7.221   11.778  20.779  1.00 25.12 ? 37   PRO A CA    1 
ATOM   70   C  C     . PRO A 1 52  ? 6.179   12.654  20.100  1.00 25.51 ? 37   PRO A C     1 
ATOM   71   O  O     . PRO A 1 52  ? 5.162   12.120  19.634  1.00 27.74 ? 37   PRO A O     1 
ATOM   72   C  CB    . PRO A 1 52  ? 6.669   11.194  22.087  1.00 27.07 ? 37   PRO A CB    1 
ATOM   73   C  CG    . PRO A 1 52  ? 7.133   12.147  23.133  1.00 27.94 ? 37   PRO A CG    1 
ATOM   74   C  CD    . PRO A 1 52  ? 8.492   12.625  22.687  1.00 24.70 ? 37   PRO A CD    1 
ATOM   75   N  N     . HIS A 1 53  ? 6.376   13.971  20.036  1.00 23.67 ? 38   HIS A N     1 
ATOM   76   C  CA    . HIS A 1 53  ? 5.437   14.858  19.365  1.00 23.66 ? 38   HIS A CA    1 
ATOM   77   C  C     . HIS A 1 53  ? 5.957   15.396  18.036  1.00 20.28 ? 38   HIS A C     1 
ATOM   78   O  O     . HIS A 1 53  ? 5.250   16.168  17.380  1.00 20.07 ? 38   HIS A O     1 
ATOM   79   C  CB    . HIS A 1 53  ? 5.049   16.018  20.292  1.00 29.41 ? 38   HIS A CB    1 
ATOM   80   C  CG    . HIS A 1 53  ? 4.322   15.579  21.527  1.00 35.30 ? 38   HIS A CG    1 
ATOM   81   N  ND1   . HIS A 1 53  ? 4.953   15.392  22.739  1.00 38.29 ? 38   HIS A ND1   1 
ATOM   82   C  CD2   . HIS A 1 53  ? 3.019   15.269  21.730  1.00 38.07 ? 38   HIS A CD2   1 
ATOM   83   C  CE1   . HIS A 1 53  ? 4.068   14.994  23.637  1.00 39.74 ? 38   HIS A CE1   1 
ATOM   84   N  NE2   . HIS A 1 53  ? 2.888   14.909  23.050  1.00 39.46 ? 38   HIS A NE2   1 
ATOM   85   N  N     . LYS A 1 54  ? 7.150   14.983  17.599  1.00 17.35 ? 39   LYS A N     1 
ATOM   86   C  CA    . LYS A 1 54  ? 7.686   15.457  16.321  1.00 17.11 ? 39   LYS A CA    1 
ATOM   87   C  C     . LYS A 1 54  ? 6.826   14.981  15.144  1.00 18.63 ? 39   LYS A C     1 
ATOM   88   O  O     . LYS A 1 54  ? 6.535   15.751  14.214  1.00 19.28 ? 39   LYS A O     1 
ATOM   89   C  CB    . LYS A 1 54  ? 9.141   14.989  16.167  1.00 16.80 ? 39   LYS A CB    1 
ATOM   90   C  CG    . LYS A 1 54  ? 9.845   15.496  14.909  1.00 15.97 ? 39   LYS A CG    1 
ATOM   91   C  CD    . LYS A 1 54  ? 10.031  17.026  14.952  1.00 16.92 ? 39   LYS A CD    1 
ATOM   92   C  CE    . LYS A 1 54  ? 10.976  17.507  13.864  1.00 16.65 ? 39   LYS A CE    1 
ATOM   93   N  NZ    . LYS A 1 54  ? 11.262  18.985  13.961  1.00 16.68 ? 39   LYS A NZ    1 
ATOM   94   N  N     . VAL A 1 55  ? 6.436   13.708  15.152  1.00 18.24 ? 40   VAL A N     1 
ATOM   95   C  CA    . VAL A 1 55  ? 5.404   13.193  14.260  1.00 18.02 ? 40   VAL A CA    1 
ATOM   96   C  C     . VAL A 1 55  ? 4.135   13.183  15.106  1.00 20.15 ? 40   VAL A C     1 
ATOM   97   O  O     . VAL A 1 55  ? 3.938   12.294  15.937  1.00 22.34 ? 40   VAL A O     1 
ATOM   98   C  CB    . VAL A 1 55  ? 5.751   11.802  13.714  1.00 19.11 ? 40   VAL A CB    1 
ATOM   99   C  CG1   . VAL A 1 55  ? 4.663   11.313  12.746  1.00 20.61 ? 40   VAL A CG1   1 
ATOM   100  C  CG2   . VAL A 1 55  ? 7.116   11.811  13.032  1.00 19.61 ? 40   VAL A CG2   1 
ATOM   101  N  N     . ALA A 1 56  ? 3.277   14.188  14.910  1.00 19.12 ? 41   ALA A N     1 
ATOM   102  C  CA    . ALA A 1 56  ? 2.255   14.543  15.891  1.00 21.38 ? 41   ALA A CA    1 
ATOM   103  C  C     . ALA A 1 56  ? 0.945   13.772  15.758  1.00 22.55 ? 41   ALA A C     1 
ATOM   104  O  O     . ALA A 1 56  ? 0.229   13.632  16.759  1.00 25.76 ? 41   ALA A O     1 
ATOM   105  C  CB    . ALA A 1 56  ? 1.943   16.043  15.810  1.00 24.31 ? 41   ALA A CB    1 
ATOM   106  N  N     A MET A 1 57  ? 0.626   13.266  14.564  0.49 21.04 ? 42   MET A N     1 
ATOM   107  N  N     B MET A 1 57  ? 0.603   13.285  14.566  0.51 22.73 ? 42   MET A N     1 
ATOM   108  C  CA    A MET A 1 57  ? -0.668  12.658  14.275  0.49 21.58 ? 42   MET A CA    1 
ATOM   109  C  CA    B MET A 1 57  ? -0.660  12.586  14.357  0.51 24.32 ? 42   MET A CA    1 
ATOM   110  C  C     A MET A 1 57  ? -0.503  11.624  13.169  0.49 20.81 ? 42   MET A C     1 
ATOM   111  C  C     B MET A 1 57  ? -0.529  11.646  13.167  0.51 21.67 ? 42   MET A C     1 
ATOM   112  O  O     A MET A 1 57  ? 0.493   11.626  12.441  0.49 20.34 ? 42   MET A O     1 
ATOM   113  O  O     B MET A 1 57  ? 0.412   11.741  12.376  0.51 20.28 ? 42   MET A O     1 
ATOM   114  C  CB    A MET A 1 57  ? -1.695  13.714  13.836  0.49 22.58 ? 42   MET A CB    1 
ATOM   115  C  CB    B MET A 1 57  ? -1.819  13.562  14.115  0.51 28.14 ? 42   MET A CB    1 
ATOM   116  C  CG    A MET A 1 57  ? -1.827  14.902  14.775  0.49 23.51 ? 42   MET A CG    1 
ATOM   117  C  CG    B MET A 1 57  ? -2.066  14.568  15.221  0.51 31.89 ? 42   MET A CG    1 
ATOM   118  S  SD    A MET A 1 57  ? -2.914  14.532  16.158  0.49 22.80 ? 42   MET A SD    1 
ATOM   119  S  SD    B MET A 1 57  ? -3.566  15.517  14.910  0.51 34.21 ? 42   MET A SD    1 
ATOM   120  C  CE    A MET A 1 57  ? -4.473  14.510  15.278  0.49 18.19 ? 42   MET A CE    1 
ATOM   121  C  CE    B MET A 1 57  ? -4.804  14.236  14.998  0.51 33.13 ? 42   MET A CE    1 
ATOM   122  N  N     . LEU A 1 58  ? -1.500  10.733  13.047  1.00 20.56 ? 43   LEU A N     1 
ATOM   123  C  CA    . LEU A 1 58  ? -1.664  9.863   11.875  1.00 19.69 ? 43   LEU A CA    1 
ATOM   124  C  C     . LEU A 1 58  ? -2.873  10.385  11.102  1.00 18.45 ? 43   LEU A C     1 
ATOM   125  O  O     . LEU A 1 58  ? -4.009  10.305  11.586  1.00 19.00 ? 43   LEU A O     1 
ATOM   126  C  CB    . LEU A 1 58  ? -1.858  8.394   12.264  1.00 23.26 ? 43   LEU A CB    1 
ATOM   127  C  CG    . LEU A 1 58  ? -2.150  7.458   11.075  1.00 24.14 ? 43   LEU A CG    1 
ATOM   128  C  CD1   . LEU A 1 58  ? -0.945  7.332   10.135  1.00 26.87 ? 43   LEU A CD1   1 
ATOM   129  C  CD2   . LEU A 1 58  ? -2.623  6.081   11.541  1.00 27.19 ? 43   LEU A CD2   1 
ATOM   130  N  N     . GLY A 1 59  ? -2.636  10.930  9.902   1.00 15.44 ? 44   GLY A N     1 
ATOM   131  C  CA    . GLY A 1 59  ? -3.697  11.592  9.147   1.00 16.47 ? 44   GLY A CA    1 
ATOM   132  C  C     . GLY A 1 59  ? -4.426  10.647  8.203   1.00 17.64 ? 44   GLY A C     1 
ATOM   133  O  O     . GLY A 1 59  ? -3.796  9.956   7.398   1.00 18.61 ? 44   GLY A O     1 
ATOM   134  N  N     . LEU A 1 60  ? -5.768  10.653  8.282   1.00 16.32 ? 45   LEU A N     1 
ATOM   135  C  CA    . LEU A 1 60  ? -6.641  9.850   7.421   1.00 16.53 ? 45   LEU A CA    1 
ATOM   136  C  C     . LEU A 1 60  ? -7.317  10.726  6.365   1.00 16.06 ? 45   LEU A C     1 
ATOM   137  O  O     . LEU A 1 60  ? -7.746  11.848  6.659   1.00 16.50 ? 45   LEU A O     1 
ATOM   138  C  CB    . LEU A 1 60  ? -7.737  9.133   8.235   1.00 17.61 ? 45   LEU A CB    1 
ATOM   139  C  CG    . LEU A 1 60  ? -7.326  8.251   9.429   1.00 17.40 ? 45   LEU A CG    1 
ATOM   140  C  CD1   . LEU A 1 60  ? -8.525  7.602   10.124  1.00 18.78 ? 45   LEU A CD1   1 
ATOM   141  C  CD2   . LEU A 1 60  ? -6.317  7.191   8.992   1.00 18.35 ? 45   LEU A CD2   1 
ATOM   142  N  N     . THR A 1 61  ? -7.438  10.202  5.142   1.00 15.60 ? 46   THR A N     1 
ATOM   143  C  CA    . THR A 1 61  ? -8.189  10.845  4.062   1.00 17.52 ? 46   THR A CA    1 
ATOM   144  C  C     . THR A 1 61  ? -9.481  10.057  3.796   1.00 17.71 ? 46   THR A C     1 
ATOM   145  O  O     . THR A 1 61  ? -9.781  9.072   4.482   1.00 17.10 ? 46   THR A O     1 
ATOM   146  C  CB    . THR A 1 61  ? -7.314  10.973  2.809   1.00 20.71 ? 46   THR A CB    1 
ATOM   147  O  OG1   . THR A 1 61  ? -7.973  11.795  1.839   1.00 24.98 ? 46   THR A OG1   1 
ATOM   148  C  CG2   . THR A 1 61  ? -7.003  9.596   2.214   1.00 22.68 ? 46   THR A CG2   1 
ATOM   149  N  N     . PHE A 1 62  ? -10.269 10.513  2.804   1.00 16.74 ? 47   PHE A N     1 
ATOM   150  C  CA    . PHE A 1 62  ? -11.576 9.890   2.548   1.00 16.55 ? 47   PHE A CA    1 
ATOM   151  C  C     . PHE A 1 62  ? -11.442 8.393   2.237   1.00 16.35 ? 47   PHE A C     1 
ATOM   152  O  O     . PHE A 1 62  ? -12.223 7.569   2.747   1.00 15.33 ? 47   PHE A O     1 
ATOM   153  C  CB    . PHE A 1 62  ? -12.316 10.611  1.406   1.00 16.60 ? 47   PHE A CB    1 
ATOM   154  C  CG    . PHE A 1 62  ? -12.640 12.063  1.693   1.00 17.15 ? 47   PHE A CG    1 
ATOM   155  C  CD1   . PHE A 1 62  ? -13.553 12.421  2.684   1.00 16.94 ? 47   PHE A CD1   1 
ATOM   156  C  CD2   . PHE A 1 62  ? -12.033 13.072  0.955   1.00 17.09 ? 47   PHE A CD2   1 
ATOM   157  C  CE1   . PHE A 1 62  ? -13.845 13.766  2.929   1.00 18.54 ? 47   PHE A CE1   1 
ATOM   158  C  CE2   . PHE A 1 62  ? -12.320 14.404  1.199   1.00 17.62 ? 47   PHE A CE2   1 
ATOM   159  C  CZ    . PHE A 1 62  ? -13.221 14.752  2.182   1.00 18.32 ? 47   PHE A CZ    1 
ATOM   160  N  N     . ASP A 1 63  ? -10.457 8.017   1.412   1.00 17.48 ? 48   ASP A N     1 
ATOM   161  C  CA    . ASP A 1 63  ? -10.279 6.614   1.020   1.00 16.48 ? 48   ASP A CA    1 
ATOM   162  C  C     . ASP A 1 63  ? -9.854  5.700   2.177   1.00 17.23 ? 48   ASP A C     1 
ATOM   163  O  O     . ASP A 1 63  ? -9.906  4.470   2.016   1.00 19.23 ? 48   ASP A O     1 
ATOM   164  C  CB    . ASP A 1 63  ? -9.248  6.490   -0.118  1.00 19.94 ? 48   ASP A CB    1 
ATOM   165  C  CG    . ASP A 1 63  ? -9.797  6.907   -1.487  1.00 23.51 ? 48   ASP A CG    1 
ATOM   166  O  OD1   . ASP A 1 63  ? -11.011 7.174   -1.621  1.00 24.84 ? 48   ASP A OD1   1 
ATOM   167  O  OD2   . ASP A 1 63  ? -8.994  6.973   -2.447  1.00 26.82 ? 48   ASP A OD2   1 
ATOM   168  N  N     . ASP A 1 64  ? -9.448  6.250   3.331   1.00 15.76 ? 49   ASP A N     1 
ATOM   169  C  CA    . ASP A 1 64  ? -9.055  5.448   4.495   1.00 16.15 ? 49   ASP A CA    1 
ATOM   170  C  C     . ASP A 1 64  ? -10.232 4.923   5.338   1.00 16.02 ? 49   ASP A C     1 
ATOM   171  O  O     . ASP A 1 64  ? -9.996  4.074   6.216   1.00 17.28 ? 49   ASP A O     1 
ATOM   172  C  CB    . ASP A 1 64  ? -8.124  6.267   5.421   1.00 18.23 ? 49   ASP A CB    1 
ATOM   173  C  CG    . ASP A 1 64  ? -6.717  6.438   4.870   1.00 18.74 ? 49   ASP A CG    1 
ATOM   174  O  OD1   . ASP A 1 64  ? -6.026  5.432   4.581   1.00 22.55 ? 49   ASP A OD1   1 
ATOM   175  O  OD2   . ASP A 1 64  ? -6.262  7.602   4.771   1.00 18.19 ? 49   ASP A OD2   1 
ATOM   176  N  N     . VAL A 1 65  ? -11.476 5.401   5.131   1.00 15.09 ? 50   VAL A N     1 
ATOM   177  C  CA    . VAL A 1 65  ? -12.594 5.067   6.016   1.00 17.08 ? 50   VAL A CA    1 
ATOM   178  C  C     . VAL A 1 65  ? -13.850 4.731   5.215   1.00 15.94 ? 50   VAL A C     1 
ATOM   179  O  O     . VAL A 1 65  ? -14.024 5.163   4.073   1.00 18.31 ? 50   VAL A O     1 
ATOM   180  C  CB    . VAL A 1 65  ? -12.922 6.215   7.014   1.00 15.89 ? 50   VAL A CB    1 
ATOM   181  C  CG1   . VAL A 1 65  ? -11.784 6.418   8.023   1.00 17.29 ? 50   VAL A CG1   1 
ATOM   182  C  CG2   . VAL A 1 65  ? -13.263 7.529   6.264   1.00 16.50 ? 50   VAL A CG2   1 
ATOM   183  N  N     . LEU A 1 66  ? -14.731 3.934   5.841   1.00 14.77 ? 51   LEU A N     1 
ATOM   184  C  CA    . LEU A 1 66  ? -16.110 3.726   5.392   1.00 14.31 ? 51   LEU A CA    1 
ATOM   185  C  C     . LEU A 1 66  ? -17.065 3.968   6.556   1.00 14.77 ? 51   LEU A C     1 
ATOM   186  O  O     . LEU A 1 66  ? -16.700 3.770   7.719   1.00 16.28 ? 51   LEU A O     1 
ATOM   187  C  CB    . LEU A 1 66  ? -16.351 2.297   4.841   1.00 16.15 ? 51   LEU A CB    1 
ATOM   188  C  CG    . LEU A 1 66  ? -15.624 1.890   3.562   1.00 17.40 ? 51   LEU A CG    1 
ATOM   189  C  CD1   . LEU A 1 66  ? -15.724 0.368   3.342   1.00 17.11 ? 51   LEU A CD1   1 
ATOM   190  C  CD2   . LEU A 1 66  ? -16.208 2.646   2.376   1.00 19.55 ? 51   LEU A CD2   1 
ATOM   191  N  N     . LEU A 1 67  ? -18.310 4.369   6.236   1.00 14.38 ? 52   LEU A N     1 
ATOM   192  C  CA    . LEU A 1 67  ? -19.350 4.529   7.257   1.00 14.06 ? 52   LEU A CA    1 
ATOM   193  C  C     . LEU A 1 67  ? -19.962 3.176   7.619   1.00 15.83 ? 52   LEU A C     1 
ATOM   194  O  O     . LEU A 1 67  ? -20.336 2.405   6.733   1.00 17.49 ? 52   LEU A O     1 
ATOM   195  C  CB    . LEU A 1 67  ? -20.453 5.470   6.763   1.00 15.21 ? 52   LEU A CB    1 
ATOM   196  C  CG    . LEU A 1 67  ? -20.089 6.958   6.676   1.00 17.47 ? 52   LEU A CG    1 
ATOM   197  C  CD1   . LEU A 1 67  ? -21.076 7.718   5.792   1.00 17.61 ? 52   LEU A CD1   1 
ATOM   198  C  CD2   . LEU A 1 67  ? -20.027 7.555   8.057   1.00 19.23 ? 52   LEU A CD2   1 
ATOM   199  N  N     . LEU A 1 68  ? -20.107 2.907   8.926   1.00 15.64 ? 53   LEU A N     1 
ATOM   200  C  CA    . LEU A 1 68  ? -20.717 1.646   9.373   1.00 15.80 ? 53   LEU A CA    1 
ATOM   201  C  C     . LEU A 1 68  ? -22.246 1.716   9.310   1.00 16.41 ? 53   LEU A C     1 
ATOM   202  O  O     . LEU A 1 68  ? -22.842 2.707   9.756   1.00 17.85 ? 53   LEU A O     1 
ATOM   203  C  CB    . LEU A 1 68  ? -20.277 1.299   10.801  1.00 16.64 ? 53   LEU A CB    1 
ATOM   204  C  CG    . LEU A 1 68  ? -18.861 0.732   10.942  1.00 17.16 ? 53   LEU A CG    1 
ATOM   205  C  CD1   . LEU A 1 68  ? -18.425 0.759   12.397  1.00 19.18 ? 53   LEU A CD1   1 
ATOM   206  C  CD2   . LEU A 1 68  ? -18.796 -0.697  10.393  1.00 18.99 ? 53   LEU A CD2   1 
ATOM   207  N  N     . PRO A 1 69  ? -22.912 0.691   8.783   1.00 16.61 ? 54   PRO A N     1 
ATOM   208  C  CA    . PRO A 1 69  ? -24.378 0.634   8.902   1.00 17.82 ? 54   PRO A CA    1 
ATOM   209  C  C     . PRO A 1 69  ? -24.817 0.579   10.364  1.00 18.22 ? 54   PRO A C     1 
ATOM   210  O  O     . PRO A 1 69  ? -24.097 0.073   11.230  1.00 18.99 ? 54   PRO A O     1 
ATOM   211  C  CB    . PRO A 1 69  ? -24.753 -0.658  8.154   1.00 18.94 ? 54   PRO A CB    1 
ATOM   212  C  CG    . PRO A 1 69  ? -23.535 -1.031  7.332   1.00 19.74 ? 54   PRO A CG    1 
ATOM   213  C  CD    . PRO A 1 69  ? -22.350 -0.491  8.105   1.00 17.53 ? 54   PRO A CD    1 
ATOM   214  N  N     . ALA A 1 70  ? -26.029 1.088   10.631  1.00 16.21 ? 55   ALA A N     1 
ATOM   215  C  CA    . ALA A 1 70  ? -26.559 1.160   11.991  1.00 17.24 ? 55   ALA A CA    1 
ATOM   216  C  C     . ALA A 1 70  ? -28.078 0.974   11.976  1.00 17.80 ? 55   ALA A C     1 
ATOM   217  O  O     . ALA A 1 70  ? -28.717 1.007   10.922  1.00 17.99 ? 55   ALA A O     1 
ATOM   218  C  CB    . ALA A 1 70  ? -26.197 2.492   12.660  1.00 18.20 ? 55   ALA A CB    1 
ATOM   219  N  N     . ALA A 1 71  ? -28.652 0.780   13.172  1.00 15.97 ? 56   ALA A N     1 
ATOM   220  C  CA    . ALA A 1 71  ? -30.104 0.628   13.307  1.00 16.53 ? 56   ALA A CA    1 
ATOM   221  C  C     . ALA A 1 71  ? -30.823 1.821   12.677  1.00 18.31 ? 56   ALA A C     1 
ATOM   222  O  O     . ALA A 1 71  ? -30.444 2.980   12.906  1.00 18.36 ? 56   ALA A O     1 
ATOM   223  C  CB    . ALA A 1 71  ? -30.482 0.490   14.784  1.00 17.36 ? 56   ALA A CB    1 
ATOM   224  N  N     . SER A 1 72  ? -31.876 1.546   11.887  1.00 17.63 ? 57   SER A N     1 
ATOM   225  C  CA    . SER A 1 72  ? -32.475 2.592   11.053  1.00 18.95 ? 57   SER A CA    1 
ATOM   226  C  C     . SER A 1 72  ? -33.988 2.475   10.892  1.00 20.95 ? 57   SER A C     1 
ATOM   227  O  O     . SER A 1 72  ? -34.532 1.382   10.682  1.00 22.09 ? 57   SER A O     1 
ATOM   228  C  CB    . SER A 1 72  ? -31.823 2.605   9.662   1.00 17.89 ? 57   SER A CB    1 
ATOM   229  O  OG    . SER A 1 72  ? -32.385 3.617   8.844   1.00 18.07 ? 57   SER A OG    1 
ATOM   230  N  N     . ASP A 1 73  ? -34.660 3.634   10.985  1.00 19.44 ? 58   ASP A N     1 
ATOM   231  C  CA    . ASP A 1 73  ? -36.038 3.821   10.544  1.00 23.18 ? 58   ASP A CA    1 
ATOM   232  C  C     . ASP A 1 73  ? -36.122 4.796   9.372   1.00 23.34 ? 58   ASP A C     1 
ATOM   233  O  O     . ASP A 1 73  ? -37.170 5.422   9.162   1.00 25.91 ? 58   ASP A O     1 
ATOM   234  C  CB    . ASP A 1 73  ? -36.915 4.327   11.693  1.00 28.92 ? 58   ASP A CB    1 
ATOM   235  C  CG    . ASP A 1 73  ? -37.194 3.268   12.740  1.00 38.86 ? 58   ASP A CG    1 
ATOM   236  O  OD1   . ASP A 1 73  ? -37.391 2.090   12.369  1.00 43.24 ? 58   ASP A OD1   1 
ATOM   237  O  OD2   . ASP A 1 73  ? -37.226 3.620   13.941  1.00 42.93 ? 58   ASP A OD2   1 
ATOM   238  N  N     . VAL A 1 74  ? -35.028 4.955   8.626   1.00 20.69 ? 59   VAL A N     1 
ATOM   239  C  CA    . VAL A 1 74  ? -34.897 5.926   7.541   1.00 19.84 ? 59   VAL A CA    1 
ATOM   240  C  C     . VAL A 1 74  ? -34.696 5.166   6.235   1.00 21.51 ? 59   VAL A C     1 
ATOM   241  O  O     . VAL A 1 74  ? -33.889 4.230   6.179   1.00 20.43 ? 59   VAL A O     1 
ATOM   242  C  CB    . VAL A 1 74  ? -33.704 6.879   7.777   1.00 19.99 ? 59   VAL A CB    1 
ATOM   243  C  CG1   . VAL A 1 74  ? -33.517 7.857   6.603   1.00 21.25 ? 59   VAL A CG1   1 
ATOM   244  C  CG2   . VAL A 1 74  ? -33.862 7.621   9.087   1.00 20.37 ? 59   VAL A CG2   1 
ATOM   245  N  N     . VAL A 1 75  ? -35.413 5.571   5.189   1.00 23.11 ? 60   VAL A N     1 
ATOM   246  C  CA    . VAL A 1 75  ? -35.128 5.124   3.824   1.00 23.81 ? 60   VAL A CA    1 
ATOM   247  C  C     . VAL A 1 75  ? -34.716 6.360   3.033   1.00 22.11 ? 60   VAL A C     1 
ATOM   248  O  O     . VAL A 1 75  ? -34.975 7.491   3.476   1.00 22.05 ? 60   VAL A O     1 
ATOM   249  C  CB    . VAL A 1 75  ? -36.325 4.398   3.180   1.00 23.29 ? 60   VAL A CB    1 
ATOM   250  C  CG1   . VAL A 1 75  ? -36.578 3.070   3.896   1.00 26.18 ? 60   VAL A CG1   1 
ATOM   251  C  CG2   . VAL A 1 75  ? -37.592 5.291   3.148   1.00 23.84 ? 60   VAL A CG2   1 
ATOM   252  N  N     . PRO A 1 76  ? -34.051 6.213   1.890   1.00 21.15 ? 61   PRO A N     1 
ATOM   253  C  CA    . PRO A 1 76  ? -33.508 7.410   1.226   1.00 21.41 ? 61   PRO A CA    1 
ATOM   254  C  C     . PRO A 1 76  ? -34.554 8.478   0.959   1.00 20.36 ? 61   PRO A C     1 
ATOM   255  O  O     . PRO A 1 76  ? -34.251 9.677   1.059   1.00 20.95 ? 61   PRO A O     1 
ATOM   256  C  CB    . PRO A 1 76  ? -32.907 6.837   -0.066  1.00 22.80 ? 61   PRO A CB    1 
ATOM   257  C  CG    . PRO A 1 76  ? -32.435 5.449   0.366   1.00 22.88 ? 61   PRO A CG    1 
ATOM   258  C  CD    . PRO A 1 76  ? -33.550 4.962   1.278   1.00 21.08 ? 61   PRO A CD    1 
ATOM   259  N  N     . ALA A 1 77  ? -35.796 8.076   0.678   1.00 21.21 ? 62   ALA A N     1 
ATOM   260  C  CA    . ALA A 1 77  ? -36.844 9.034   0.325   1.00 23.00 ? 62   ALA A CA    1 
ATOM   261  C  C     . ALA A 1 77  ? -37.258 9.918   1.499   1.00 23.23 ? 62   ALA A C     1 
ATOM   262  O  O     . ALA A 1 77  ? -37.760 11.028  1.284   1.00 24.12 ? 62   ALA A O     1 
ATOM   263  C  CB    . ALA A 1 77  ? -38.069 8.293   -0.215  1.00 25.24 ? 62   ALA A CB    1 
ATOM   264  N  N     . THR A 1 78  ? -37.095 9.458   2.738   1.00 23.25 ? 63   THR A N     1 
ATOM   265  C  CA    . THR A 1 78  ? -37.613 10.232  3.864   1.00 23.39 ? 63   THR A CA    1 
ATOM   266  C  C     . THR A 1 78  ? -36.543 11.059  4.571   1.00 23.36 ? 63   THR A C     1 
ATOM   267  O  O     . THR A 1 78  ? -36.881 11.832  5.473   1.00 26.02 ? 63   THR A O     1 
ATOM   268  C  CB    . THR A 1 78  ? -38.348 9.328   4.878   1.00 22.20 ? 63   THR A CB    1 
ATOM   269  O  OG1   . THR A 1 78  ? -37.450 8.375   5.467   1.00 23.66 ? 63   THR A OG1   1 
ATOM   270  C  CG2   . THR A 1 78  ? -39.476 8.585   4.198   1.00 22.83 ? 63   THR A CG2   1 
ATOM   271  N  N     . ALA A 1 79  ? -35.280 10.954  4.157   1.00 20.95 ? 64   ALA A N     1 
ATOM   272  C  CA    . ALA A 1 79  ? -34.215 11.758  4.748   1.00 19.68 ? 64   ALA A CA    1 
ATOM   273  C  C     . ALA A 1 79  ? -34.389 13.252  4.442   1.00 20.28 ? 64   ALA A C     1 
ATOM   274  O  O     . ALA A 1 79  ? -34.918 13.639  3.398   1.00 23.43 ? 64   ALA A O     1 
ATOM   275  C  CB    . ALA A 1 79  ? -32.855 11.280  4.238   1.00 21.58 ? 64   ALA A CB    1 
ATOM   276  N  N     . ASP A 1 80  ? -33.917 14.094  5.373   1.00 19.68 ? 65   ASP A N     1 
ATOM   277  C  CA    . ASP A 1 80  ? -33.919 15.558  5.253   1.00 19.82 ? 65   ASP A CA    1 
ATOM   278  C  C     . ASP A 1 80  ? -32.471 16.040  5.130   1.00 20.46 ? 65   ASP A C     1 
ATOM   279  O  O     . ASP A 1 80  ? -31.693 15.920  6.083   1.00 20.51 ? 65   ASP A O     1 
ATOM   280  C  CB    . ASP A 1 80  ? -34.622 16.168  6.472   1.00 21.88 ? 65   ASP A CB    1 
ATOM   281  C  CG    . ASP A 1 80  ? -34.547 17.698  6.542   1.00 26.53 ? 65   ASP A CG    1 
ATOM   282  O  OD1   . ASP A 1 80  ? -33.878 18.349  5.710   1.00 27.33 ? 65   ASP A OD1   1 
ATOM   283  O  OD2   . ASP A 1 80  ? -35.190 18.247  7.470   1.00 29.97 ? 65   ASP A OD2   1 
ATOM   284  N  N     . THR A 1 81  ? -32.111 16.596  3.967   1.00 18.96 ? 66   THR A N     1 
ATOM   285  C  CA    . THR A 1 81  ? -30.717 16.961  3.679   1.00 19.02 ? 66   THR A CA    1 
ATOM   286  C  C     . THR A 1 81  ? -30.340 18.409  4.038   1.00 18.18 ? 66   THR A C     1 
ATOM   287  O  O     . THR A 1 81  ? -29.209 18.820  3.743   1.00 18.74 ? 66   THR A O     1 
ATOM   288  C  CB    . THR A 1 81  ? -30.388 16.727  2.196   1.00 19.68 ? 66   THR A CB    1 
ATOM   289  O  OG1   . THR A 1 81  ? -31.209 17.575  1.372   1.00 21.51 ? 66   THR A OG1   1 
ATOM   290  C  CG2   . THR A 1 81  ? -30.564 15.243  1.793   1.00 20.37 ? 66   THR A CG2   1 
ATOM   291  N  N     . SER A 1 82  ? -31.216 19.183  4.682   1.00 17.31 ? 67   SER A N     1 
ATOM   292  C  CA    . SER A 1 82  ? -30.882 20.585  4.967   1.00 17.37 ? 67   SER A CA    1 
ATOM   293  C  C     . SER A 1 82  ? -29.777 20.714  6.026   1.00 17.72 ? 67   SER A C     1 
ATOM   294  O  O     . SER A 1 82  ? -29.592 19.834  6.878   1.00 18.11 ? 67   SER A O     1 
ATOM   295  C  CB    . SER A 1 82  ? -32.135 21.349  5.414   1.00 18.94 ? 67   SER A CB    1 
ATOM   296  O  OG    . SER A 1 82  ? -32.659 20.823  6.613   1.00 21.49 ? 67   SER A OG    1 
ATOM   297  N  N     . SER A 1 83  ? -29.026 21.827  5.966   1.00 18.08 ? 68   SER A N     1 
ATOM   298  C  CA    . SER A 1 83  ? -27.896 22.017  6.878   1.00 18.46 ? 68   SER A CA    1 
ATOM   299  C  C     . SER A 1 83  ? -27.441 23.478  6.868   1.00 19.05 ? 68   SER A C     1 
ATOM   300  O  O     . SER A 1 83  ? -27.626 24.186  5.873   1.00 19.57 ? 68   SER A O     1 
ATOM   301  C  CB    . SER A 1 83  ? -26.726 21.104  6.490   1.00 19.37 ? 68   SER A CB    1 
ATOM   302  O  OG    . SER A 1 83  ? -25.747 21.009  7.525   1.00 19.33 ? 68   SER A OG    1 
ATOM   303  N  N     . GLN A 1 84  ? -26.805 23.904  7.967   1.00 18.19 ? 69   GLN A N     1 
ATOM   304  C  CA    . GLN A 1 84  ? -26.285 25.272  8.072   1.00 18.71 ? 69   GLN A CA    1 
ATOM   305  C  C     . GLN A 1 84  ? -25.031 25.490  7.227   1.00 18.83 ? 69   GLN A C     1 
ATOM   306  O  O     . GLN A 1 84  ? -24.030 24.775  7.378   1.00 18.74 ? 69   GLN A O     1 
ATOM   307  C  CB    . GLN A 1 84  ? -25.949 25.624  9.523   1.00 20.57 ? 69   GLN A CB    1 
ATOM   308  C  CG    . GLN A 1 84  ? -27.092 25.516  10.519  1.00 23.41 ? 69   GLN A CG    1 
ATOM   309  C  CD    . GLN A 1 84  ? -28.235 26.476  10.248  1.00 24.45 ? 69   GLN A CD    1 
ATOM   310  O  OE1   . GLN A 1 84  ? -29.405 26.086  10.284  1.00 27.48 ? 69   GLN A OE1   1 
ATOM   311  N  NE2   . GLN A 1 84  ? -27.907 27.745  10.007  1.00 25.24 ? 69   GLN A NE2   1 
ATOM   312  N  N     . LEU A 1 85  ? -25.072 26.520  6.371   1.00 16.99 ? 70   LEU A N     1 
ATOM   313  C  CA    . LEU A 1 85  ? -23.856 27.049  5.748   1.00 16.93 ? 70   LEU A CA    1 
ATOM   314  C  C     . LEU A 1 85  ? -23.090 27.960  6.709   1.00 18.72 ? 70   LEU A C     1 
ATOM   315  O  O     . LEU A 1 85  ? -21.866 27.840  6.849   1.00 19.31 ? 70   LEU A O     1 
ATOM   316  C  CB    . LEU A 1 85  ? -24.202 27.809  4.459   1.00 17.27 ? 70   LEU A CB    1 
ATOM   317  C  CG    . LEU A 1 85  ? -23.033 28.450  3.698   1.00 17.71 ? 70   LEU A CG    1 
ATOM   318  C  CD1   . LEU A 1 85  ? -22.083 27.371  3.151   1.00 19.53 ? 70   LEU A CD1   1 
ATOM   319  C  CD2   . LEU A 1 85  ? -23.524 29.382  2.574   1.00 19.83 ? 70   LEU A CD2   1 
ATOM   320  N  N     . THR A 1 86  ? -23.791 28.892  7.363   1.00 19.54 ? 71   THR A N     1 
ATOM   321  C  CA    . THR A 1 86  ? -23.208 29.813  8.341   1.00 19.57 ? 71   THR A CA    1 
ATOM   322  C  C     . THR A 1 86  ? -24.140 29.872  9.544   1.00 21.19 ? 71   THR A C     1 
ATOM   323  O  O     . THR A 1 86  ? -25.185 29.213  9.576   1.00 21.43 ? 71   THR A O     1 
ATOM   324  C  CB    . THR A 1 86  ? -22.999 31.237  7.780   1.00 21.09 ? 71   THR A CB    1 
ATOM   325  O  OG1   . THR A 1 86  ? -24.270 31.861  7.562   1.00 22.26 ? 71   THR A OG1   1 
ATOM   326  C  CG2   . THR A 1 86  ? -22.212 31.241  6.466   1.00 20.64 ? 71   THR A CG2   1 
ATOM   327  N  N     . LYS A 1 87  ? -23.776 30.680  10.543  1.00 22.19 ? 72   LYS A N     1 
ATOM   328  C  CA    . LYS A 1 87  ? -24.641 30.804  11.718  1.00 24.35 ? 72   LYS A CA    1 
ATOM   329  C  C     . LYS A 1 87  ? -26.082 31.133  11.333  1.00 26.49 ? 72   LYS A C     1 
ATOM   330  O  O     . LYS A 1 87  ? -27.031 30.580  11.911  1.00 27.57 ? 72   LYS A O     1 
ATOM   331  C  CB    . LYS A 1 87  ? -24.099 31.867  12.677  1.00 26.20 ? 72   LYS A CB    1 
ATOM   332  C  CG    . LYS A 1 87  ? -22.867 31.446  13.472  1.00 28.19 ? 72   LYS A CG    1 
ATOM   333  C  CD    . LYS A 1 87  ? -22.451 32.556  14.422  1.00 31.20 ? 72   LYS A CD    1 
ATOM   334  C  CE    . LYS A 1 87  ? -21.282 32.143  15.298  1.00 33.82 ? 72   LYS A CE    1 
ATOM   335  N  NZ    . LYS A 1 87  ? -20.829 33.287  16.148  1.00 36.88 ? 72   LYS A NZ    1 
ATOM   336  N  N     . LYS A 1 88  ? -26.272 32.023  10.350  1.00 25.75 ? 73   LYS A N     1 
ATOM   337  C  CA    . LYS A 1 88  ? -27.606 32.527  10.034  1.00 26.73 ? 73   LYS A CA    1 
ATOM   338  C  C     . LYS A 1 88  ? -28.223 31.984  8.744   1.00 26.91 ? 73   LYS A C     1 
ATOM   339  O  O     . LYS A 1 88  ? -29.430 32.182  8.533   1.00 30.63 ? 73   LYS A O     1 
ATOM   340  C  CB    . LYS A 1 88  ? -27.575 34.064  9.984   1.00 29.62 ? 73   LYS A CB    1 
ATOM   341  C  CG    . LYS A 1 88  ? -27.366 34.684  11.365  1.00 32.59 ? 73   LYS A CG    1 
ATOM   342  C  CD    . LYS A 1 88  ? -26.836 36.117  11.311  1.00 37.93 ? 73   LYS A CD    1 
ATOM   343  C  CE    . LYS A 1 88  ? -27.816 37.073  10.671  1.00 40.11 ? 73   LYS A CE    1 
ATOM   344  N  NZ    . LYS A 1 88  ? -27.414 38.503  10.902  1.00 42.33 ? 73   LYS A NZ    1 
ATOM   345  N  N     . ILE A 1 89  ? -27.471 31.276  7.897   1.00 23.95 ? 74   ILE A N     1 
ATOM   346  C  CA    . ILE A 1 89  ? -27.980 30.806  6.603   1.00 23.36 ? 74   ILE A CA    1 
ATOM   347  C  C     . ILE A 1 89  ? -28.030 29.278  6.584   1.00 21.69 ? 74   ILE A C     1 
ATOM   348  O  O     . ILE A 1 89  ? -27.007 28.622  6.801   1.00 21.33 ? 74   ILE A O     1 
ATOM   349  C  CB    . ILE A 1 89  ? -27.119 31.334  5.447   1.00 22.76 ? 74   ILE A CB    1 
ATOM   350  C  CG1   . ILE A 1 89  ? -27.171 32.871  5.396   1.00 23.66 ? 74   ILE A CG1   1 
ATOM   351  C  CG2   . ILE A 1 89  ? -27.551 30.746  4.117   1.00 22.84 ? 74   ILE A CG2   1 
ATOM   352  C  CD1   . ILE A 1 89  ? -26.134 33.441  4.445   1.00 24.75 ? 74   ILE A CD1   1 
ATOM   353  N  N     . ARG A 1 90  ? -29.211 28.715  6.285   1.00 21.89 ? 75   ARG A N     1 
ATOM   354  C  CA    . ARG A 1 90  ? -29.414 27.274  6.122   1.00 22.39 ? 75   ARG A CA    1 
ATOM   355  C  C     . ARG A 1 90  ? -29.761 26.971  4.668   1.00 23.73 ? 75   ARG A C     1 
ATOM   356  O  O     . ARG A 1 90  ? -30.560 27.690  4.055   1.00 27.84 ? 75   ARG A O     1 
ATOM   357  C  CB    . ARG A 1 90  ? -30.542 26.761  7.050   1.00 23.73 ? 75   ARG A CB    1 
ATOM   358  C  CG    . ARG A 1 90  ? -30.687 25.219  7.157   1.00 23.47 ? 75   ARG A CG    1 
ATOM   359  C  CD    . ARG A 1 90  ? -31.703 24.810  8.245   1.00 24.76 ? 75   ARG A CD    1 
ATOM   360  N  NE    . ARG A 1 90  ? -31.795 23.354  8.440   1.00 26.62 ? 75   ARG A NE    1 
ATOM   361  C  CZ    . ARG A 1 90  ? -30.996 22.650  9.246   1.00 26.06 ? 75   ARG A CZ    1 
ATOM   362  N  NH1   . ARG A 1 90  ? -30.030 23.256  9.939   1.00 26.03 ? 75   ARG A NH1   1 
ATOM   363  N  NH2   . ARG A 1 90  ? -31.149 21.335  9.360   1.00 25.90 ? 75   ARG A NH2   1 
ATOM   364  N  N     . LEU A 1 91  ? -29.179 25.898  4.121   1.00 21.45 ? 76   LEU A N     1 
ATOM   365  C  CA    . LEU A 1 91  ? -29.411 25.451  2.750   1.00 19.58 ? 76   LEU A CA    1 
ATOM   366  C  C     . LEU A 1 91  ? -30.278 24.190  2.722   1.00 19.75 ? 76   LEU A C     1 
ATOM   367  O  O     . LEU A 1 91  ? -30.249 23.376  3.650   1.00 20.82 ? 76   LEU A O     1 
ATOM   368  C  CB    . LEU A 1 91  ? -28.081 25.145  2.033   1.00 18.58 ? 76   LEU A CB    1 
ATOM   369  C  CG    . LEU A 1 91  ? -27.043 26.269  1.935   1.00 18.69 ? 76   LEU A CG    1 
ATOM   370  C  CD1   . LEU A 1 91  ? -25.736 25.777  1.284   1.00 18.42 ? 76   LEU A CD1   1 
ATOM   371  C  CD2   . LEU A 1 91  ? -27.646 27.444  1.163   1.00 20.32 ? 76   LEU A CD2   1 
ATOM   372  N  N     . LYS A 1 92  ? -31.020 24.006  1.620   1.00 19.52 ? 77   LYS A N     1 
ATOM   373  C  CA    . LYS A 1 92  ? -31.803 22.781  1.441   1.00 19.81 ? 77   LYS A CA    1 
ATOM   374  C  C     . LYS A 1 92  ? -30.944 21.583  1.026   1.00 19.85 ? 77   LYS A C     1 
ATOM   375  O  O     . LYS A 1 92  ? -31.288 20.442  1.361   1.00 18.92 ? 77   LYS A O     1 
ATOM   376  C  CB    . LYS A 1 92  ? -32.903 23.006  0.400   1.00 22.52 ? 77   LYS A CB    1 
ATOM   377  C  CG    . LYS A 1 92  ? -34.002 23.940  0.861   1.00 26.38 ? 77   LYS A CG    1 
ATOM   378  C  CD    . LYS A 1 92  ? -34.968 24.233  -0.275  1.00 32.50 ? 77   LYS A CD    1 
ATOM   379  C  CE    . LYS A 1 92  ? -36.113 23.233  -0.314  1.00 38.20 ? 77   LYS A CE    1 
ATOM   380  N  NZ    . LYS A 1 92  ? -37.136 23.526  0.738   1.00 40.60 ? 77   LYS A NZ    1 
ATOM   381  N  N     . VAL A 1 93  ? -29.851 21.823  0.303   1.00 19.55 ? 78   VAL A N     1 
ATOM   382  C  CA    . VAL A 1 93  ? -28.862 20.818  -0.108  1.00 19.59 ? 78   VAL A CA    1 
ATOM   383  C  C     . VAL A 1 93  ? -27.497 21.320  0.357   1.00 18.60 ? 78   VAL A C     1 
ATOM   384  O  O     . VAL A 1 93  ? -27.152 22.476  0.088   1.00 19.82 ? 78   VAL A O     1 
ATOM   385  C  CB    . VAL A 1 93  ? -28.885 20.595  -1.632  1.00 21.99 ? 78   VAL A CB    1 
ATOM   386  C  CG1   . VAL A 1 93  ? -27.702 19.759  -2.083  1.00 23.55 ? 78   VAL A CG1   1 
ATOM   387  C  CG2   . VAL A 1 93  ? -30.201 19.943  -2.053  1.00 23.15 ? 78   VAL A CG2   1 
ATOM   388  N  N     . PRO A 1 94  ? -26.670 20.498  1.062   1.00 17.15 ? 79   PRO A N     1 
ATOM   389  C  CA    . PRO A 1 94  ? -25.488 21.016  1.768   1.00 18.21 ? 79   PRO A CA    1 
ATOM   390  C  C     . PRO A 1 94  ? -24.211 21.115  0.918   1.00 17.24 ? 79   PRO A C     1 
ATOM   391  O  O     . PRO A 1 94  ? -23.126 20.622  1.308   1.00 17.27 ? 79   PRO A O     1 
ATOM   392  C  CB    . PRO A 1 94  ? -25.319 20.017  2.918   1.00 17.59 ? 79   PRO A CB    1 
ATOM   393  C  CG    . PRO A 1 94  ? -25.778 18.694  2.307   1.00 17.63 ? 79   PRO A CG    1 
ATOM   394  C  CD    . PRO A 1 94  ? -26.918 19.067  1.351   1.00 16.89 ? 79   PRO A CD    1 
ATOM   395  N  N     . LEU A 1 95  ? -24.317 21.782  -0.242  1.00 16.37 ? 80   LEU A N     1 
ATOM   396  C  CA    . LEU A 1 95  ? -23.257 21.822  -1.253  1.00 17.21 ? 80   LEU A CA    1 
ATOM   397  C  C     . LEU A 1 95  ? -23.061 23.236  -1.790  1.00 17.63 ? 80   LEU A C     1 
ATOM   398  O  O     . LEU A 1 95  ? -24.038 23.942  -2.063  1.00 17.79 ? 80   LEU A O     1 
ATOM   399  C  CB    . LEU A 1 95  ? -23.589 20.890  -2.442  1.00 17.04 ? 80   LEU A CB    1 
ATOM   400  C  CG    . LEU A 1 95  ? -23.791 19.400  -2.130  1.00 18.90 ? 80   LEU A CG    1 
ATOM   401  C  CD1   . LEU A 1 95  ? -24.225 18.594  -3.356  1.00 20.10 ? 80   LEU A CD1   1 
ATOM   402  C  CD2   . LEU A 1 95  ? -22.524 18.816  -1.539  1.00 20.36 ? 80   LEU A CD2   1 
ATOM   403  N  N     A VAL A 1 96  ? -21.799 23.660  -1.920  0.72 17.63 ? 81   VAL A N     1 
ATOM   404  N  N     B VAL A 1 96  ? -21.799 23.625  -1.984  0.28 17.57 ? 81   VAL A N     1 
ATOM   405  C  CA    A VAL A 1 96  ? -21.469 24.935  -2.551  0.72 18.04 ? 81   VAL A CA    1 
ATOM   406  C  CA    B VAL A 1 96  ? -21.446 24.933  -2.532  0.28 17.29 ? 81   VAL A CA    1 
ATOM   407  C  C     A VAL A 1 96  ? -20.391 24.710  -3.605  0.72 17.18 ? 81   VAL A C     1 
ATOM   408  C  C     B VAL A 1 96  ? -20.347 24.751  -3.574  0.28 17.22 ? 81   VAL A C     1 
ATOM   409  O  O     A VAL A 1 96  ? -19.576 23.789  -3.496  0.72 17.02 ? 81   VAL A O     1 
ATOM   410  O  O     B VAL A 1 96  ? -19.478 23.886  -3.425  0.28 17.27 ? 81   VAL A O     1 
ATOM   411  C  CB    A VAL A 1 96  ? -21.014 25.994  -1.519  0.72 20.53 ? 81   VAL A CB    1 
ATOM   412  C  CB    B VAL A 1 96  ? -21.001 25.902  -1.415  0.28 17.68 ? 81   VAL A CB    1 
ATOM   413  C  CG1   A VAL A 1 96  ? -22.085 26.196  -0.445  0.72 19.78 ? 81   VAL A CG1   1 
ATOM   414  C  CG1   B VAL A 1 96  ? -19.948 25.256  -0.533  0.28 18.88 ? 81   VAL A CG1   1 
ATOM   415  C  CG2   A VAL A 1 96  ? -19.674 25.624  -0.897  0.72 22.28 ? 81   VAL A CG2   1 
ATOM   416  C  CG2   B VAL A 1 96  ? -20.486 27.209  -2.001  0.28 16.33 ? 81   VAL A CG2   1 
ATOM   417  N  N     . SER A 1 97  ? -20.385 25.562  -4.635  1.00 16.76 ? 82   SER A N     1 
ATOM   418  C  CA    . SER A 1 97  ? -19.387 25.474  -5.711  1.00 16.81 ? 82   SER A CA    1 
ATOM   419  C  C     . SER A 1 97  ? -18.147 26.342  -5.443  1.00 17.28 ? 82   SER A C     1 
ATOM   420  O  O     . SER A 1 97  ? -18.248 27.453  -4.900  1.00 18.03 ? 82   SER A O     1 
ATOM   421  C  CB    . SER A 1 97  ? -20.002 25.860  -7.062  1.00 17.46 ? 82   SER A CB    1 
ATOM   422  O  OG    . SER A 1 97  ? -20.531 27.186  -7.055  1.00 19.10 ? 82   SER A OG    1 
ATOM   423  N  N     . SER A 1 98  ? -16.976 25.840  -5.870  1.00 16.25 ? 83   SER A N     1 
ATOM   424  C  CA    . SER A 1 98  ? -15.685 26.484  -5.593  1.00 14.97 ? 83   SER A CA    1 
ATOM   425  C  C     . SER A 1 98  ? -15.543 27.850  -6.257  1.00 16.92 ? 83   SER A C     1 
ATOM   426  O  O     . SER A 1 98  ? -16.060 28.100  -7.352  1.00 17.40 ? 83   SER A O     1 
ATOM   427  C  CB    . SER A 1 98  ? -14.514 25.598  -6.063  1.00 15.98 ? 83   SER A CB    1 
ATOM   428  O  OG    . SER A 1 98  ? -14.388 24.416  -5.288  1.00 16.45 ? 83   SER A OG    1 
ATOM   429  N  N     . ALA A 1 99  ? -14.757 28.716  -5.610  1.00 16.25 ? 84   ALA A N     1 
ATOM   430  C  CA    . ALA A 1 99  ? -14.488 30.071  -6.106  1.00 15.83 ? 84   ALA A CA    1 
ATOM   431  C  C     . ALA A 1 99  ? -13.310 30.046  -7.093  1.00 16.68 ? 84   ALA A C     1 
ATOM   432  O  O     . ALA A 1 99  ? -12.196 30.516  -6.816  1.00 18.27 ? 84   ALA A O     1 
ATOM   433  C  CB    . ALA A 1 99  ? -14.241 31.017  -4.935  1.00 18.52 ? 84   ALA A CB    1 
ATOM   434  N  N     . MET A 1 100 ? -13.581 29.490  -8.282  1.00 17.04 ? 85   MET A N     1 
ATOM   435  C  CA    . MET A 1 100 ? -12.563 29.245  -9.304  1.00 17.19 ? 85   MET A CA    1 
ATOM   436  C  C     . MET A 1 100 ? -13.064 29.711  -10.667 1.00 18.55 ? 85   MET A C     1 
ATOM   437  O  O     . MET A 1 100 ? -14.261 29.594  -10.969 1.00 18.70 ? 85   MET A O     1 
ATOM   438  C  CB    . MET A 1 100 ? -12.176 27.741  -9.362  1.00 16.98 ? 85   MET A CB    1 
ATOM   439  C  CG    . MET A 1 100 ? -11.649 27.200  -8.027  1.00 16.40 ? 85   MET A CG    1 
ATOM   440  S  SD    . MET A 1 100 ? -11.369 25.405  -7.969  1.00 17.58 ? 85   MET A SD    1 
ATOM   441  C  CE    . MET A 1 100 ? -9.940  25.257  -9.048  1.00 19.03 ? 85   MET A CE    1 
ATOM   442  N  N     . ASP A 1 101 ? -12.148 30.240  -11.500 1.00 19.25 ? 86   ASP A N     1 
ATOM   443  C  CA    . ASP A 1 101 ? -12.548 30.816  -12.786 1.00 19.83 ? 86   ASP A CA    1 
ATOM   444  C  C     . ASP A 1 101 ? -12.853 29.767  -13.857 1.00 21.39 ? 86   ASP A C     1 
ATOM   445  O  O     . ASP A 1 101 ? -13.256 30.143  -14.967 1.00 23.57 ? 86   ASP A O     1 
ATOM   446  C  CB    . ASP A 1 101 ? -11.517 31.865  -13.290 1.00 21.75 ? 86   ASP A CB    1 
ATOM   447  C  CG    . ASP A 1 101 ? -10.125 31.305  -13.649 1.00 22.80 ? 86   ASP A CG    1 
ATOM   448  O  OD1   . ASP A 1 101 ? -9.876  30.085  -13.665 1.00 22.06 ? 86   ASP A OD1   1 
ATOM   449  O  OD2   . ASP A 1 101 ? -9.252  32.160  -13.954 1.00 24.23 ? 86   ASP A OD2   1 
ATOM   450  N  N     . THR A 1 102 ? -12.755 28.473  -13.539 1.00 20.05 ? 87   THR A N     1 
ATOM   451  C  CA    . THR A 1 102 ? -13.311 27.424  -14.391 1.00 20.79 ? 87   THR A CA    1 
ATOM   452  C  C     . THR A 1 102 ? -14.478 26.686  -13.730 1.00 21.17 ? 87   THR A C     1 
ATOM   453  O  O     . THR A 1 102 ? -14.883 25.618  -14.221 1.00 23.76 ? 87   THR A O     1 
ATOM   454  C  CB    . THR A 1 102 ? -12.224 26.427  -14.818 1.00 20.88 ? 87   THR A CB    1 
ATOM   455  O  OG1   . THR A 1 102 ? -11.561 25.891  -13.666 1.00 22.06 ? 87   THR A OG1   1 
ATOM   456  C  CG2   . THR A 1 102 ? -11.186 27.108  -15.708 1.00 23.02 ? 87   THR A CG2   1 
ATOM   457  N  N     . VAL A 1 103 ? -15.047 27.235  -12.646 1.00 19.04 ? 88   VAL A N     1 
ATOM   458  C  CA    . VAL A 1 103 ? -16.181 26.612  -11.953 1.00 18.10 ? 88   VAL A CA    1 
ATOM   459  C  C     . VAL A 1 103 ? -17.374 27.558  -11.764 1.00 19.07 ? 88   VAL A C     1 
ATOM   460  O  O     . VAL A 1 103 ? -18.499 27.206  -12.135 1.00 19.03 ? 88   VAL A O     1 
ATOM   461  C  CB    . VAL A 1 103 ? -15.751 26.016  -10.594 1.00 17.10 ? 88   VAL A CB    1 
ATOM   462  C  CG1   . VAL A 1 103 ? -16.940 25.345  -9.902  1.00 17.43 ? 88   VAL A CG1   1 
ATOM   463  C  CG2   . VAL A 1 103 ? -14.628 24.979  -10.791 1.00 19.04 ? 88   VAL A CG2   1 
ATOM   464  N  N     . THR A 1 104 ? -17.179 28.743  -11.165 1.00 19.04 ? 89   THR A N     1 
ATOM   465  C  CA    . THR A 1 104 ? -18.327 29.561  -10.737 1.00 19.65 ? 89   THR A CA    1 
ATOM   466  C  C     . THR A 1 104 ? -18.280 31.002  -11.244 1.00 19.87 ? 89   THR A C     1 
ATOM   467  O  O     . THR A 1 104 ? -17.550 31.837  -10.691 1.00 19.76 ? 89   THR A O     1 
ATOM   468  C  CB    . THR A 1 104 ? -18.460 29.578  -9.208  1.00 17.50 ? 89   THR A CB    1 
ATOM   469  O  OG1   . THR A 1 104 ? -18.472 28.239  -8.694  1.00 18.81 ? 89   THR A OG1   1 
ATOM   470  C  CG2   . THR A 1 104 ? -19.769 30.283  -8.791  1.00 18.80 ? 89   THR A CG2   1 
ATOM   471  N  N     . GLU A 1 105 ? -19.120 31.311  -12.244 1.00 19.86 ? 90   GLU A N     1 
ATOM   472  C  CA    . GLU A 1 105 ? -19.570 32.672  -12.534 1.00 19.21 ? 90   GLU A CA    1 
ATOM   473  C  C     . GLU A 1 105 ? -21.102 32.716  -12.417 1.00 21.47 ? 90   GLU A C     1 
ATOM   474  O  O     . GLU A 1 105 ? -21.683 31.846  -11.762 1.00 21.38 ? 90   GLU A O     1 
ATOM   475  C  CB    . GLU A 1 105 ? -19.043 33.130  -13.905 1.00 20.50 ? 90   GLU A CB    1 
ATOM   476  C  CG    . GLU A 1 105 ? -17.520 33.357  -13.886 1.00 23.55 ? 90   GLU A CG    1 
ATOM   477  C  CD    . GLU A 1 105 ? -16.922 33.858  -15.193 1.00 28.43 ? 90   GLU A CD    1 
ATOM   478  O  OE1   . GLU A 1 105 ? -17.592 33.808  -16.247 1.00 31.37 ? 90   GLU A OE1   1 
ATOM   479  O  OE2   . GLU A 1 105 ? -15.749 34.296  -15.160 1.00 29.97 ? 90   GLU A OE2   1 
ATOM   480  N  N     . SER A 1 106 ? -21.782 33.706  -13.013 1.00 23.71 ? 91   SER A N     1 
ATOM   481  C  CA    . SER A 1 106 ? -23.199 33.912  -12.687 1.00 24.20 ? 91   SER A CA    1 
ATOM   482  C  C     . SER A 1 106 ? -24.075 32.707  -13.051 1.00 24.79 ? 91   SER A C     1 
ATOM   483  O  O     . SER A 1 106 ? -24.989 32.352  -12.295 1.00 23.85 ? 91   SER A O     1 
ATOM   484  C  CB    . SER A 1 106 ? -23.729 35.186  -13.358 1.00 26.99 ? 91   SER A CB    1 
ATOM   485  O  OG    . SER A 1 106 ? -23.746 35.084  -14.768 1.00 28.87 ? 91   SER A OG    1 
ATOM   486  N  N     . ARG A 1 107 ? -23.833 32.070  -14.202 1.00 24.53 ? 92   ARG A N     1 
ATOM   487  C  CA    . ARG A 1 107 ? -24.686 30.945  -14.597 1.00 26.64 ? 92   ARG A CA    1 
ATOM   488  C  C     . ARG A 1 107 ? -24.618 29.793  -13.595 1.00 24.98 ? 92   ARG A C     1 
ATOM   489  O  O     . ARG A 1 107 ? -25.644 29.171  -13.282 1.00 26.19 ? 92   ARG A O     1 
ATOM   490  C  CB    . ARG A 1 107 ? -24.310 30.449  -15.991 1.00 31.74 ? 92   ARG A CB    1 
ATOM   491  C  CG    . ARG A 1 107 ? -25.163 31.039  -17.091 1.00 39.10 ? 92   ARG A CG    1 
ATOM   492  C  CD    . ARG A 1 107 ? -24.747 30.534  -18.462 1.00 45.33 ? 92   ARG A CD    1 
ATOM   493  N  NE    . ARG A 1 107 ? -24.741 29.076  -18.548 1.00 49.38 ? 92   ARG A NE    1 
ATOM   494  C  CZ    . ARG A 1 107 ? -24.795 28.408  -19.695 1.00 52.46 ? 92   ARG A CZ    1 
ATOM   495  N  NH1   . ARG A 1 107 ? -24.875 29.073  -20.843 1.00 54.97 ? 92   ARG A NH1   1 
ATOM   496  N  NH2   . ARG A 1 107 ? -24.781 27.084  -19.701 1.00 53.56 ? 92   ARG A NH2   1 
ATOM   497  N  N     . MET A 1 108 ? -23.421 29.470  -13.106 1.00 22.81 ? 93   MET A N     1 
ATOM   498  C  CA    . MET A 1 108 ? -23.298 28.413  -12.104 1.00 22.24 ? 93   MET A CA    1 
ATOM   499  C  C     . MET A 1 108 ? -23.942 28.825  -10.786 1.00 21.40 ? 93   MET A C     1 
ATOM   500  O  O     . MET A 1 108 ? -24.588 28.005  -10.119 1.00 22.11 ? 93   MET A O     1 
ATOM   501  C  CB    . MET A 1 108 ? -21.817 28.053  -11.894 1.00 21.28 ? 93   MET A CB    1 
ATOM   502  C  CG    . MET A 1 108 ? -21.528 27.094  -10.719 1.00 19.39 ? 93   MET A CG    1 
ATOM   503  S  SD    . MET A 1 108 ? -22.143 25.393  -10.933 1.00 21.14 ? 93   MET A SD    1 
ATOM   504  C  CE    . MET A 1 108 ? -20.959 24.755  -12.137 1.00 22.59 ? 93   MET A CE    1 
ATOM   505  N  N     . ALA A 1 109 ? -23.767 30.086  -10.381 1.00 20.81 ? 94   ALA A N     1 
ATOM   506  C  CA    . ALA A 1 109 ? -24.355 30.541  -9.126  1.00 21.60 ? 94   ALA A CA    1 
ATOM   507  C  C     . ALA A 1 109 ? -25.882 30.476  -9.166  1.00 22.18 ? 94   ALA A C     1 
ATOM   508  O  O     . ALA A 1 109 ? -26.516 30.087  -8.176  1.00 22.45 ? 94   ALA A O     1 
ATOM   509  C  CB    . ALA A 1 109 ? -23.869 31.957  -8.804  1.00 21.11 ? 94   ALA A CB    1 
ATOM   510  N  N     . ILE A 1 110 ? -26.495 30.843  -10.299 1.00 21.43 ? 95   ILE A N     1 
ATOM   511  C  CA    . ILE A 1 110 ? -27.953 30.755  -10.414 1.00 22.49 ? 95   ILE A CA    1 
ATOM   512  C  C     . ILE A 1 110 ? -28.412 29.299  -10.324 1.00 23.36 ? 95   ILE A C     1 
ATOM   513  O  O     . ILE A 1 110 ? -29.385 28.979  -9.623  1.00 23.98 ? 95   ILE A O     1 
ATOM   514  C  CB    . ILE A 1 110 ? -28.435 31.425  -11.718 1.00 21.85 ? 95   ILE A CB    1 
ATOM   515  C  CG1   . ILE A 1 110 ? -28.241 32.936  -11.645 1.00 22.96 ? 95   ILE A CG1   1 
ATOM   516  C  CG2   . ILE A 1 110 ? -29.918 31.125  -11.963 1.00 24.34 ? 95   ILE A CG2   1 
ATOM   517  C  CD1   . ILE A 1 110 ? -28.309 33.604  -12.980 1.00 23.63 ? 95   ILE A CD1   1 
ATOM   518  N  N     . ALA A 1 111 ? -27.725 28.392  -11.025 1.00 22.03 ? 96   ALA A N     1 
ATOM   519  C  CA    . ALA A 1 111 ? -28.153 26.991  -11.042 1.00 20.75 ? 96   ALA A CA    1 
ATOM   520  C  C     . ALA A 1 111 ? -27.986 26.337  -9.674  1.00 21.05 ? 96   ALA A C     1 
ATOM   521  O  O     . ALA A 1 111 ? -28.851 25.563  -9.242  1.00 21.32 ? 96   ALA A O     1 
ATOM   522  C  CB    . ALA A 1 111 ? -27.381 26.215  -12.108 1.00 20.19 ? 96   ALA A CB    1 
ATOM   523  N  N     . MET A 1 112 ? -26.886 26.643  -8.974  1.00 21.14 ? 97   MET A N     1 
ATOM   524  C  CA    . MET A 1 112 ? -26.678 26.093  -7.635  1.00 20.96 ? 97   MET A CA    1 
ATOM   525  C  C     . MET A 1 112 ? -27.767 26.550  -6.666  1.00 22.18 ? 97   MET A C     1 
ATOM   526  O  O     . MET A 1 112 ? -28.272 25.749  -5.868  1.00 21.62 ? 97   MET A O     1 
ATOM   527  C  CB    . MET A 1 112 ? -25.288 26.479  -7.107  1.00 20.56 ? 97   MET A CB    1 
ATOM   528  C  CG    . MET A 1 112 ? -24.113 25.683  -7.717  1.00 19.23 ? 97   MET A CG    1 
ATOM   529  S  SD    . MET A 1 112 ? -24.087 23.897  -7.335  1.00 19.85 ? 97   MET A SD    1 
ATOM   530  C  CE    . MET A 1 112 ? -23.932 23.928  -5.555  1.00 20.19 ? 97   MET A CE    1 
ATOM   531  N  N     . ALA A 1 113 ? -28.156 27.832  -6.721  1.00 23.21 ? 98   ALA A N     1 
ATOM   532  C  CA    . ALA A 1 113 ? -29.180 28.321  -5.801  1.00 22.10 ? 98   ALA A CA    1 
ATOM   533  C  C     . ALA A 1 113 ? -30.540 27.686  -6.094  1.00 23.54 ? 98   ALA A C     1 
ATOM   534  O  O     . ALA A 1 113 ? -31.273 27.326  -5.165  1.00 23.99 ? 98   ALA A O     1 
ATOM   535  C  CB    . ALA A 1 113 ? -29.272 29.851  -5.867  1.00 21.99 ? 98   ALA A CB    1 
ATOM   536  N  N     . ARG A 1 114 ? -30.884 27.521  -7.374  1.00 23.22 ? 99   ARG A N     1 
ATOM   537  C  CA    . ARG A 1 114 ? -32.160 26.891  -7.720  1.00 25.44 ? 99   ARG A CA    1 
ATOM   538  C  C     . ARG A 1 114 ? -32.195 25.414  -7.325  1.00 25.33 ? 99   ARG A C     1 
ATOM   539  O  O     . ARG A 1 114 ? -33.277 24.869  -7.055  1.00 26.86 ? 99   ARG A O     1 
ATOM   540  C  CB    . ARG A 1 114 ? -32.435 27.063  -9.214  1.00 26.45 ? 99   ARG A CB    1 
ATOM   541  C  CG    . ARG A 1 114 ? -32.838 28.488  -9.601  1.00 27.55 ? 99   ARG A CG    1 
ATOM   542  C  CD    . ARG A 1 114 ? -32.957 28.661  -11.112 1.00 30.82 ? 99   ARG A CD    1 
ATOM   543  N  NE    . ARG A 1 114 ? -33.430 29.999  -11.469 1.00 34.17 ? 99   ARG A NE    1 
ATOM   544  C  CZ    . ARG A 1 114 ? -33.382 30.513  -12.695 1.00 37.55 ? 99   ARG A CZ    1 
ATOM   545  N  NH1   . ARG A 1 114 ? -32.872 29.811  -13.699 1.00 37.27 ? 99   ARG A NH1   1 
ATOM   546  N  NH2   . ARG A 1 114 ? -33.837 31.739  -12.916 1.00 39.86 ? 99   ARG A NH2   1 
ATOM   547  N  N     . ALA A 1 115 ? -31.033 24.755  -7.271  1.00 23.41 ? 100  ALA A N     1 
ATOM   548  C  CA    . ALA A 1 115 ? -30.942 23.356  -6.858  1.00 22.59 ? 100  ALA A CA    1 
ATOM   549  C  C     . ALA A 1 115 ? -30.947 23.174  -5.345  1.00 23.84 ? 100  ALA A C     1 
ATOM   550  O  O     . ALA A 1 115 ? -30.909 22.028  -4.878  1.00 24.96 ? 100  ALA A O     1 
ATOM   551  C  CB    . ALA A 1 115 ? -29.676 22.718  -7.440  1.00 22.36 ? 100  ALA A CB    1 
ATOM   552  N  N     . GLY A 1 116 ? -30.977 24.261  -4.571  1.00 22.36 ? 101  GLY A N     1 
ATOM   553  C  CA    . GLY A 1 116 ? -30.985 24.180  -3.125  1.00 21.96 ? 101  GLY A CA    1 
ATOM   554  C  C     . GLY A 1 116 ? -29.652 24.445  -2.444  1.00 20.38 ? 101  GLY A C     1 
ATOM   555  O  O     . GLY A 1 116 ? -29.610 24.452  -1.207  1.00 21.37 ? 101  GLY A O     1 
ATOM   556  N  N     . GLY A 1 117 ? -28.571 24.670  -3.202  1.00 19.77 ? 102  GLY A N     1 
ATOM   557  C  CA    . GLY A 1 117 ? -27.263 25.004  -2.642  1.00 18.68 ? 102  GLY A CA    1 
ATOM   558  C  C     . GLY A 1 117 ? -26.855 26.457  -2.864  1.00 18.03 ? 102  GLY A C     1 
ATOM   559  O  O     . GLY A 1 117 ? -27.706 27.347  -2.790  1.00 19.71 ? 102  GLY A O     1 
ATOM   560  N  N     . MET A 1 118 ? -25.575 26.727  -3.147  1.00 19.20 ? 103  MET A N     1 
ATOM   561  C  CA    . MET A 1 118 ? -25.118 28.104  -3.350  1.00 18.01 ? 103  MET A CA    1 
ATOM   562  C  C     . MET A 1 118 ? -23.799 28.093  -4.115  1.00 18.36 ? 103  MET A C     1 
ATOM   563  O  O     . MET A 1 118 ? -23.032 27.134  -4.028  1.00 19.42 ? 103  MET A O     1 
ATOM   564  C  CB    . MET A 1 118 ? -24.938 28.856  -2.017  1.00 17.45 ? 103  MET A CB    1 
ATOM   565  C  CG    . MET A 1 118 ? -24.892 30.401  -2.173  1.00 18.29 ? 103  MET A CG    1 
ATOM   566  S  SD    . MET A 1 118 ? -24.410 31.317  -0.684  1.00 20.59 ? 103  MET A SD    1 
ATOM   567  C  CE    . MET A 1 118 ? -22.662 30.947  -0.649  1.00 21.70 ? 103  MET A CE    1 
ATOM   568  N  N     . GLY A 1 119 ? -23.534 29.178  -4.851  1.00 17.85 ? 104  GLY A N     1 
ATOM   569  C  CA    . GLY A 1 119 ? -22.257 29.379  -5.516  1.00 18.49 ? 104  GLY A CA    1 
ATOM   570  C  C     . GLY A 1 119 ? -21.445 30.470  -4.835  1.00 18.54 ? 104  GLY A C     1 
ATOM   571  O  O     . GLY A 1 119 ? -22.006 31.411  -4.263  1.00 19.84 ? 104  GLY A O     1 
ATOM   572  N  N     . VAL A 1 120 ? -20.114 30.339  -4.892  1.00 17.16 ? 105  VAL A N     1 
ATOM   573  C  CA    . VAL A 1 120 ? -19.187 31.404  -4.492  1.00 16.99 ? 105  VAL A CA    1 
ATOM   574  C  C     . VAL A 1 120 ? -18.457 31.905  -5.742  1.00 17.26 ? 105  VAL A C     1 
ATOM   575  O  O     . VAL A 1 120 ? -17.611 31.198  -6.305  1.00 17.65 ? 105  VAL A O     1 
ATOM   576  C  CB    . VAL A 1 120 ? -18.176 30.932  -3.432  1.00 16.86 ? 105  VAL A CB    1 
ATOM   577  C  CG1   . VAL A 1 120 ? -17.282 32.099  -3.001  1.00 16.91 ? 105  VAL A CG1   1 
ATOM   578  C  CG2   . VAL A 1 120 ? -18.886 30.321  -2.227  1.00 18.47 ? 105  VAL A CG2   1 
ATOM   579  N  N     . LEU A 1 121 ? -18.738 33.148  -6.142  1.00 16.69 ? 106  LEU A N     1 
ATOM   580  C  CA    . LEU A 1 121 ? -18.123 33.755  -7.327  1.00 17.03 ? 106  LEU A CA    1 
ATOM   581  C  C     . LEU A 1 121 ? -16.616 33.978  -7.153  1.00 19.62 ? 106  LEU A C     1 
ATOM   582  O  O     . LEU A 1 121 ? -16.165 34.497  -6.129  1.00 19.58 ? 106  LEU A O     1 
ATOM   583  C  CB    . LEU A 1 121 ? -18.792 35.101  -7.632  1.00 17.92 ? 106  LEU A CB    1 
ATOM   584  C  CG    . LEU A 1 121 ? -20.291 35.102  -7.953  1.00 18.66 ? 106  LEU A CG    1 
ATOM   585  C  CD1   . LEU A 1 121 ? -20.909 36.526  -7.880  1.00 21.60 ? 106  LEU A CD1   1 
ATOM   586  C  CD2   . LEU A 1 121 ? -20.535 34.514  -9.335  1.00 20.54 ? 106  LEU A CD2   1 
ATOM   587  N  N     . HIS A 1 122 ? -15.838 33.617  -8.182  1.00 19.28 ? 107  HIS A N     1 
ATOM   588  C  CA    . HIS A 1 122 ? -14.378 33.771  -8.136  1.00 19.87 ? 107  HIS A CA    1 
ATOM   589  C  C     . HIS A 1 122 ? -13.986 35.250  -8.229  1.00 19.80 ? 107  HIS A C     1 
ATOM   590  O  O     . HIS A 1 122 ? -14.798 36.110  -8.581  1.00 20.83 ? 107  HIS A O     1 
ATOM   591  C  CB    . HIS A 1 122 ? -13.695 32.962  -9.251  1.00 20.07 ? 107  HIS A CB    1 
ATOM   592  C  CG    . HIS A 1 122 ? -13.771 33.591  -10.610 1.00 20.58 ? 107  HIS A CG    1 
ATOM   593  N  ND1   . HIS A 1 122 ? -12.809 34.457  -11.091 1.00 19.92 ? 107  HIS A ND1   1 
ATOM   594  C  CD2   . HIS A 1 122 ? -14.690 33.462  -11.599 1.00 20.03 ? 107  HIS A CD2   1 
ATOM   595  C  CE1   . HIS A 1 122 ? -13.141 34.845  -12.311 1.00 21.06 ? 107  HIS A CE1   1 
ATOM   596  N  NE2   . HIS A 1 122 ? -14.279 34.256  -12.643 1.00 21.08 ? 107  HIS A NE2   1 
ATOM   597  N  N     . ARG A 1 123 ? -12.709 35.539  -7.909  1.00 20.20 ? 108  ARG A N     1 
ATOM   598  C  CA    . ARG A 1 123 ? -12.206 36.912  -7.788  1.00 17.97 ? 108  ARG A CA    1 
ATOM   599  C  C     . ARG A 1 123 ? -11.048 37.228  -8.741  1.00 19.80 ? 108  ARG A C     1 
ATOM   600  O  O     . ARG A 1 123 ? -10.333 38.216  -8.532  1.00 21.60 ? 108  ARG A O     1 
ATOM   601  C  CB    . ARG A 1 123 ? -11.795 37.205  -6.337  1.00 18.50 ? 108  ARG A CB    1 
ATOM   602  C  CG    . ARG A 1 123 ? -10.591 36.397  -5.784  1.00 18.91 ? 108  ARG A CG    1 
ATOM   603  C  CD    . ARG A 1 123 ? -10.343 36.739  -4.307  1.00 18.46 ? 108  ARG A CD    1 
ATOM   604  N  NE    . ARG A 1 123 ? -9.292  35.966  -3.645  1.00 20.38 ? 108  ARG A NE    1 
ATOM   605  C  CZ    . ARG A 1 123 ? -8.035  36.370  -3.486  1.00 20.66 ? 108  ARG A CZ    1 
ATOM   606  N  NH1   . ARG A 1 123 ? -7.638  37.542  -3.987  1.00 20.31 ? 108  ARG A NH1   1 
ATOM   607  N  NH2   . ARG A 1 123 ? -7.166  35.590  -2.836  1.00 20.95 ? 108  ARG A NH2   1 
ATOM   608  N  N     . ASN A 1 124 ? -10.869 36.447  -9.810  1.00 19.71 ? 109  ASN A N     1 
ATOM   609  C  CA    . ASN A 1 124 ? -9.823  36.704  -10.808 1.00 21.49 ? 109  ASN A CA    1 
ATOM   610  C  C     . ASN A 1 124 ? -10.385 37.524  -11.976 1.00 23.72 ? 109  ASN A C     1 
ATOM   611  O  O     . ASN A 1 124 ? -10.330 37.129  -13.141 1.00 25.33 ? 109  ASN A O     1 
ATOM   612  C  CB    . ASN A 1 124 ? -9.221  35.382  -11.287 1.00 22.78 ? 109  ASN A CB    1 
ATOM   613  C  CG    . ASN A 1 124 ? -7.925  35.562  -12.070 1.00 26.92 ? 109  ASN A CG    1 
ATOM   614  O  OD1   . ASN A 1 124 ? -7.236  36.571  -11.935 1.00 29.64 ? 109  ASN A OD1   1 
ATOM   615  N  ND2   . ASN A 1 124 ? -7.586  34.568  -12.893 1.00 27.68 ? 109  ASN A ND2   1 
ATOM   616  N  N     . LEU A 1 125 ? -10.937 38.699  -11.634 1.00 25.55 ? 110  LEU A N     1 
ATOM   617  C  CA    . LEU A 1 125 ? -11.519 39.627  -12.604 1.00 26.41 ? 110  LEU A CA    1 
ATOM   618  C  C     . LEU A 1 125 ? -11.709 40.995  -11.952 1.00 28.09 ? 110  LEU A C     1 
ATOM   619  O  O     . LEU A 1 125 ? -11.616 41.107  -10.722 1.00 28.05 ? 110  LEU A O     1 
ATOM   620  C  CB    . LEU A 1 125 ? -12.849 39.088  -13.150 1.00 27.35 ? 110  LEU A CB    1 
ATOM   621  C  CG    . LEU A 1 125 ? -14.130 39.166  -12.309 1.00 25.30 ? 110  LEU A CG    1 
ATOM   622  C  CD1   . LEU A 1 125 ? -15.298 38.477  -13.032 1.00 27.18 ? 110  LEU A CD1   1 
ATOM   623  C  CD2   . LEU A 1 125 ? -13.930 38.578  -10.917 1.00 23.59 ? 110  LEU A CD2   1 
ATOM   624  N  N     . PRO A 1 126 ? -11.968 42.055  -12.725 1.00 28.17 ? 111  PRO A N     1 
ATOM   625  C  CA    . PRO A 1 126 ? -12.084 43.391  -12.123 1.00 29.00 ? 111  PRO A CA    1 
ATOM   626  C  C     . PRO A 1 126 ? -13.217 43.472  -11.110 1.00 29.58 ? 111  PRO A C     1 
ATOM   627  O  O     . PRO A 1 126 ? -14.218 42.757  -11.199 1.00 30.66 ? 111  PRO A O     1 
ATOM   628  C  CB    . PRO A 1 126 ? -12.355 44.305  -13.327 1.00 30.04 ? 111  PRO A CB    1 
ATOM   629  C  CG    . PRO A 1 126 ? -11.808 43.570  -14.497 1.00 30.34 ? 111  PRO A CG    1 
ATOM   630  C  CD    . PRO A 1 126 ? -12.057 42.107  -14.194 1.00 28.89 ? 111  PRO A CD    1 
ATOM   631  N  N     . VAL A 1 127 ? -13.053 44.383  -10.148 1.00 28.20 ? 112  VAL A N     1 
ATOM   632  C  CA    . VAL A 1 127 ? -14.056 44.561  -9.098  1.00 28.20 ? 112  VAL A CA    1 
ATOM   633  C  C     . VAL A 1 127 ? -15.431 44.831  -9.706  1.00 28.50 ? 112  VAL A C     1 
ATOM   634  O  O     . VAL A 1 127 ? -16.440 44.247  -9.290  1.00 28.71 ? 112  VAL A O     1 
ATOM   635  C  CB    . VAL A 1 127 ? -13.639 45.693  -8.142  1.00 28.52 ? 112  VAL A CB    1 
ATOM   636  C  CG1   . VAL A 1 127 ? -14.798 46.051  -7.205  1.00 29.48 ? 112  VAL A CG1   1 
ATOM   637  C  CG2   . VAL A 1 127 ? -12.407 45.303  -7.353  1.00 29.06 ? 112  VAL A CG2   1 
ATOM   638  N  N     . ALA A 1 128 ? -15.495 45.742  -10.684 1.00 29.05 ? 113  ALA A N     1 
ATOM   639  C  CA    . ALA A 1 128 ? -16.777 46.098  -11.289 1.00 28.67 ? 113  ALA A CA    1 
ATOM   640  C  C     . ALA A 1 128 ? -17.441 44.911  -11.978 1.00 29.75 ? 113  ALA A C     1 
ATOM   641  O  O     . ALA A 1 128 ? -18.677 44.845  -12.037 1.00 32.24 ? 113  ALA A O     1 
ATOM   642  C  CB    . ALA A 1 128 ? -16.597 47.250  -12.283 1.00 29.11 ? 113  ALA A CB    1 
ATOM   643  N  N     . GLU A 1 129 ? -16.650 43.975  -12.519 1.00 28.43 ? 114  GLU A N     1 
ATOM   644  C  CA    . GLU A 1 129 ? -17.225 42.793  -13.162 1.00 29.91 ? 114  GLU A CA    1 
ATOM   645  C  C     . GLU A 1 129 ? -17.770 41.795  -12.143 1.00 26.97 ? 114  GLU A C     1 
ATOM   646  O  O     . GLU A 1 129 ? -18.816 41.184  -12.380 1.00 26.12 ? 114  GLU A O     1 
ATOM   647  C  CB    . GLU A 1 129 ? -16.191 42.100  -14.049 1.00 33.77 ? 114  GLU A CB    1 
ATOM   648  C  CG    . GLU A 1 129 ? -15.765 42.892  -15.275 1.00 37.93 ? 114  GLU A CG    1 
ATOM   649  C  CD    . GLU A 1 129 ? -14.963 42.056  -16.263 1.00 43.61 ? 114  GLU A CD    1 
ATOM   650  O  OE1   . GLU A 1 129 ? -15.107 40.813  -16.255 1.00 45.17 ? 114  GLU A OE1   1 
ATOM   651  O  OE2   . GLU A 1 129 ? -14.191 42.647  -17.048 1.00 47.16 ? 114  GLU A OE2   1 
ATOM   652  N  N     . GLN A 1 130 ? -17.062 41.594  -11.023 1.00 25.75 ? 115  GLN A N     1 
ATOM   653  C  CA    . GLN A 1 130 ? -17.536 40.667  -9.993  1.00 22.83 ? 115  GLN A CA    1 
ATOM   654  C  C     . GLN A 1 130 ? -18.803 41.197  -9.325  1.00 24.30 ? 115  GLN A C     1 
ATOM   655  O  O     . GLN A 1 130 ? -19.735 40.431  -9.043  1.00 25.63 ? 115  GLN A O     1 
ATOM   656  C  CB    . GLN A 1 130 ? -16.429 40.422  -8.953  1.00 20.81 ? 115  GLN A CB    1 
ATOM   657  C  CG    . GLN A 1 130 ? -16.665 39.200  -8.030  1.00 20.93 ? 115  GLN A CG    1 
ATOM   658  C  CD    . GLN A 1 130 ? -15.709 39.143  -6.834  1.00 21.34 ? 115  GLN A CD    1 
ATOM   659  O  OE1   . GLN A 1 130 ? -15.093 40.145  -6.472  1.00 21.56 ? 115  GLN A OE1   1 
ATOM   660  N  NE2   . GLN A 1 130 ? -15.578 37.960  -6.223  1.00 21.22 ? 115  GLN A NE2   1 
ATOM   661  N  N     . ALA A 1 131 ? -18.858 42.504  -9.064  1.00 24.63 ? 116  ALA A N     1 
ATOM   662  C  CA    . ALA A 1 131 ? -20.077 43.084  -8.511  1.00 25.07 ? 116  ALA A CA    1 
ATOM   663  C  C     . ALA A 1 131 ? -21.241 42.985  -9.489  1.00 27.46 ? 116  ALA A C     1 
ATOM   664  O  O     . ALA A 1 131 ? -22.388 42.786  -9.069  1.00 28.94 ? 116  ALA A O     1 
ATOM   665  C  CB    . ALA A 1 131 ? -19.833 44.542  -8.112  1.00 23.96 ? 116  ALA A CB    1 
ATOM   666  N  N     . GLY A 1 132 ? -20.971 43.114  -10.791 1.00 27.48 ? 117  GLY A N     1 
ATOM   667  C  CA    . GLY A 1 132 ? -22.028 42.971  -11.777 1.00 28.44 ? 117  GLY A CA    1 
ATOM   668  C  C     . GLY A 1 132 ? -22.601 41.569  -11.832 1.00 29.44 ? 117  GLY A C     1 
ATOM   669  O  O     . GLY A 1 132 ? -23.796 41.392  -12.090 1.00 30.10 ? 117  GLY A O     1 
ATOM   670  N  N     . GLN A 1 133 ? -21.768 40.555  -11.594 1.00 29.60 ? 118  GLN A N     1 
ATOM   671  C  CA    . GLN A 1 133 ? -22.274 39.186  -11.570 1.00 27.84 ? 118  GLN A CA    1 
ATOM   672  C  C     . GLN A 1 133 ? -23.138 38.928  -10.344 1.00 28.79 ? 118  GLN A C     1 
ATOM   673  O  O     . GLN A 1 133 ? -24.094 38.148  -10.419 1.00 30.18 ? 118  GLN A O     1 
ATOM   674  C  CB    . GLN A 1 133 ? -21.115 38.187  -11.645 1.00 28.19 ? 118  GLN A CB    1 
ATOM   675  C  CG    . GLN A 1 133 ? -20.438 38.202  -13.003 1.00 31.04 ? 118  GLN A CG    1 
ATOM   676  C  CD    . GLN A 1 133 ? -19.383 37.128  -13.176 1.00 33.51 ? 118  GLN A CD    1 
ATOM   677  O  OE1   . GLN A 1 133 ? -19.309 36.173  -12.396 1.00 36.79 ? 118  GLN A OE1   1 
ATOM   678  N  NE2   . GLN A 1 133 ? -18.560 37.275  -14.214 1.00 34.25 ? 118  GLN A NE2   1 
ATOM   679  N  N     . VAL A 1 134 ? -22.817 39.556  -9.210  1.00 29.40 ? 119  VAL A N     1 
ATOM   680  C  CA    . VAL A 1 134 ? -23.710 39.496  -8.054  1.00 29.54 ? 119  VAL A CA    1 
ATOM   681  C  C     . VAL A 1 134 ? -25.092 40.036  -8.423  1.00 31.01 ? 119  VAL A C     1 
ATOM   682  O  O     . VAL A 1 134 ? -26.123 39.447  -8.069  1.00 31.05 ? 119  VAL A O     1 
ATOM   683  C  CB    . VAL A 1 134 ? -23.103 40.263  -6.862  1.00 28.24 ? 119  VAL A CB    1 
ATOM   684  C  CG1   . VAL A 1 134 ? -24.121 40.387  -5.739  1.00 28.54 ? 119  VAL A CG1   1 
ATOM   685  C  CG2   . VAL A 1 134 ? -21.826 39.567  -6.357  1.00 26.79 ? 119  VAL A CG2   1 
ATOM   686  N  N     . GLU A 1 135 ? -25.137 41.165  -9.136  1.00 33.26 ? 120  GLU A N     1 
ATOM   687  C  CA    . GLU A 1 135 ? -26.426 41.750  -9.506  1.00 36.42 ? 120  GLU A CA    1 
ATOM   688  C  C     . GLU A 1 135 ? -27.214 40.829  -10.432 1.00 36.55 ? 120  GLU A C     1 
ATOM   689  O  O     . GLU A 1 135 ? -28.435 40.691  -10.287 1.00 37.74 ? 120  GLU A O     1 
ATOM   690  C  CB    . GLU A 1 135 ? -26.221 43.116  -10.160 1.00 41.77 ? 120  GLU A CB    1 
ATOM   691  C  CG    . GLU A 1 135 ? -25.846 44.224  -9.194  1.00 47.18 ? 120  GLU A CG    1 
ATOM   692  C  CD    . GLU A 1 135 ? -25.825 45.594  -9.861  1.00 52.46 ? 120  GLU A CD    1 
ATOM   693  O  OE1   . GLU A 1 135 ? -26.513 45.763  -10.894 1.00 55.94 ? 120  GLU A OE1   1 
ATOM   694  O  OE2   . GLU A 1 135 ? -25.120 46.497  -9.356  1.00 54.00 ? 120  GLU A OE2   1 
ATOM   695  N  N     . MET A 1 136 ? -26.538 40.199  -11.399 1.00 35.06 ? 121  MET A N     1 
ATOM   696  C  CA    . MET A 1 136 ? -27.238 39.296  -12.308 1.00 35.57 ? 121  MET A CA    1 
ATOM   697  C  C     . MET A 1 136 ? -27.922 38.174  -11.540 1.00 33.95 ? 121  MET A C     1 
ATOM   698  O  O     . MET A 1 136 ? -29.055 37.794  -11.860 1.00 35.78 ? 121  MET A O     1 
ATOM   699  C  CB    . MET A 1 136 ? -26.276 38.709  -13.340 1.00 39.27 ? 121  MET A CB    1 
ATOM   700  C  CG    . MET A 1 136 ? -25.460 39.711  -14.130 1.00 44.25 ? 121  MET A CG    1 
ATOM   701  S  SD    . MET A 1 136 ? -24.349 38.864  -15.279 1.00 49.58 ? 121  MET A SD    1 
ATOM   702  C  CE    . MET A 1 136 ? -23.190 40.176  -15.670 1.00 49.69 ? 121  MET A CE    1 
ATOM   703  N  N     . VAL A 1 137 ? -27.248 37.627  -10.525 1.00 30.90 ? 122  VAL A N     1 
ATOM   704  C  CA    . VAL A 1 137 ? -27.853 36.561  -9.732  1.00 30.38 ? 122  VAL A CA    1 
ATOM   705  C  C     . VAL A 1 137 ? -29.072 37.085  -8.985  1.00 33.44 ? 122  VAL A C     1 
ATOM   706  O  O     . VAL A 1 137 ? -30.129 36.441  -8.953  1.00 33.41 ? 122  VAL A O     1 
ATOM   707  C  CB    . VAL A 1 137 ? -26.824 35.944  -8.765  1.00 28.81 ? 122  VAL A CB    1 
ATOM   708  C  CG1   . VAL A 1 137 ? -27.491 34.844  -7.937  1.00 28.46 ? 122  VAL A CG1   1 
ATOM   709  C  CG2   . VAL A 1 137 ? -25.626 35.385  -9.529  1.00 27.47 ? 122  VAL A CG2   1 
ATOM   710  N  N     . LYS A 1 138 ? -28.941 38.266  -8.371  1.00 36.02 ? 123  LYS A N     1 
ATOM   711  C  CA    . LYS A 1 138 ? -30.043 38.817  -7.589  1.00 39.16 ? 123  LYS A CA    1 
ATOM   712  C  C     . LYS A 1 138 ? -31.237 39.175  -8.461  1.00 42.68 ? 123  LYS A C     1 
ATOM   713  O  O     . LYS A 1 138 ? -32.378 39.152  -7.983  1.00 45.75 ? 123  LYS A O     1 
ATOM   714  C  CB    . LYS A 1 138 ? -29.569 40.042  -6.808  1.00 38.24 ? 123  LYS A CB    1 
ATOM   715  C  CG    . LYS A 1 138 ? -28.722 39.700  -5.596  1.00 36.75 ? 123  LYS A CG    1 
ATOM   716  C  CD    . LYS A 1 138 ? -29.465 38.724  -4.705  1.00 35.44 ? 123  LYS A CD    1 
ATOM   717  C  CE    . LYS A 1 138 ? -28.704 38.416  -3.436  1.00 33.19 ? 123  LYS A CE    1 
ATOM   718  N  NZ    . LYS A 1 138 ? -29.500 37.522  -2.536  1.00 31.84 ? 123  LYS A NZ    1 
ATOM   719  N  N     . ARG A 1 139 ? -31.006 39.510  -9.731  1.00 44.30 ? 124  ARG A N     1 
ATOM   720  C  CA    . ARG A 1 139 ? -32.102 39.826  -10.640 1.00 46.93 ? 124  ARG A CA    1 
ATOM   721  C  C     . ARG A 1 139 ? -32.857 38.590  -11.108 1.00 45.84 ? 124  ARG A C     1 
ATOM   722  O  O     . ARG A 1 139 ? -33.872 38.734  -11.798 1.00 43.91 ? 124  ARG A O     1 
ATOM   723  C  CB    . ARG A 1 139 ? -31.573 40.584  -11.858 1.00 51.64 ? 124  ARG A CB    1 
ATOM   724  C  CG    . ARG A 1 139 ? -30.831 41.869  -11.522 1.00 56.30 ? 124  ARG A CG    1 
ATOM   725  C  CD    . ARG A 1 139 ? -29.797 42.193  -12.591 1.00 59.67 ? 124  ARG A CD    1 
ATOM   726  N  NE    . ARG A 1 139 ? -30.403 42.566  -13.866 1.00 62.53 ? 124  ARG A NE    1 
ATOM   727  C  CZ    . ARG A 1 139 ? -29.738 42.626  -15.017 1.00 65.01 ? 124  ARG A CZ    1 
ATOM   728  N  NH1   . ARG A 1 139 ? -28.446 42.326  -15.053 1.00 66.11 ? 124  ARG A NH1   1 
ATOM   729  N  NH2   . ARG A 1 139 ? -30.366 42.981  -16.133 1.00 65.84 ? 124  ARG A NH2   1 
ATOM   730  N  N     . SER A 1 140 ? -32.385 37.391  -10.757 1.00 46.23 ? 125  SER A N     1 
ATOM   731  C  CA    . SER A 1 140 ? -32.978 36.136  -11.199 1.00 46.79 ? 125  SER A CA    1 
ATOM   732  C  C     . SER A 1 140 ? -33.865 35.500  -10.134 1.00 47.44 ? 125  SER A C     1 
ATOM   733  O  O     . SER A 1 140 ? -34.078 34.282  -10.164 1.00 48.43 ? 125  SER A O     1 
ATOM   734  C  CB    . SER A 1 140 ? -31.884 35.152  -11.622 1.00 47.71 ? 125  SER A CB    1 
ATOM   735  O  OG    . SER A 1 140 ? -31.153 35.633  -12.740 1.00 49.07 ? 125  SER A OG    1 
ATOM   736  N  N     . GLY A 1 141 ? -34.372 36.289  -9.189  1.00 47.57 ? 126  GLY A N     1 
ATOM   737  C  CA    . GLY A 1 141 ? -35.317 35.779  -8.215  1.00 46.98 ? 126  GLY A CA    1 
ATOM   738  C  C     . GLY A 1 141 ? -34.908 35.926  -6.763  1.00 45.76 ? 126  GLY A C     1 
ATOM   739  O  O     . GLY A 1 141 ? -35.453 35.237  -5.895  1.00 45.68 ? 126  GLY A O     1 
ATOM   740  N  N     . GLY A 1 142 ? -33.963 36.818  -6.474  1.00 44.19 ? 127  GLY A N     1 
ATOM   741  C  CA    . GLY A 1 142 ? -33.515 36.981  -5.100  1.00 43.40 ? 127  GLY A CA    1 
ATOM   742  C  C     . GLY A 1 142 ? -32.819 35.761  -4.535  1.00 40.98 ? 127  GLY A C     1 
ATOM   743  O  O     . GLY A 1 142 ? -32.898 35.506  -3.329  1.00 43.03 ? 127  GLY A O     1 
ATOM   744  N  N     . LEU A 1 143 ? -32.146 34.995  -5.384  1.00 36.02 ? 253  LEU A N     1 
ATOM   745  C  CA    . LEU A 1 143 ? -31.418 33.805  -4.967  1.00 31.25 ? 253  LEU A CA    1 
ATOM   746  C  C     . LEU A 1 143 ? -30.241 34.171  -4.059  1.00 28.02 ? 253  LEU A C     1 
ATOM   747  O  O     . LEU A 1 143 ? -29.726 35.290  -4.104  1.00 28.60 ? 253  LEU A O     1 
ATOM   748  C  CB    . LEU A 1 143 ? -30.925 33.067  -6.209  1.00 30.64 ? 253  LEU A CB    1 
ATOM   749  C  CG    . LEU A 1 143 ? -32.023 32.765  -7.237  1.00 30.69 ? 253  LEU A CG    1 
ATOM   750  C  CD1   . LEU A 1 143 ? -31.468 32.468  -8.632  1.00 30.04 ? 253  LEU A CD1   1 
ATOM   751  C  CD2   . LEU A 1 143 ? -32.890 31.608  -6.749  1.00 32.02 ? 253  LEU A CD2   1 
ATOM   752  N  N     . LEU A 1 144 ? -29.817 33.216  -3.225  1.00 25.34 ? 254  LEU A N     1 
ATOM   753  C  CA    . LEU A 1 144 ? -28.624 33.383  -2.388  1.00 24.13 ? 254  LEU A CA    1 
ATOM   754  C  C     . LEU A 1 144 ? -27.345 33.334  -3.226  1.00 23.06 ? 254  LEU A C     1 
ATOM   755  O  O     . LEU A 1 144 ? -27.254 32.574  -4.195  1.00 21.94 ? 254  LEU A O     1 
ATOM   756  C  CB    . LEU A 1 144 ? -28.543 32.273  -1.329  1.00 26.10 ? 254  LEU A CB    1 
ATOM   757  C  CG    . LEU A 1 144 ? -29.484 32.224  -0.125  1.00 27.05 ? 254  LEU A CG    1 
ATOM   758  C  CD1   . LEU A 1 144 ? -29.486 30.820  0.479   1.00 28.33 ? 254  LEU A CD1   1 
ATOM   759  C  CD2   . LEU A 1 144 ? -29.042 33.246  0.910   1.00 27.09 ? 254  LEU A CD2   1 
ATOM   760  N  N     . VAL A 1 145 ? -26.332 34.128  -2.827  1.00 21.24 ? 255  VAL A N     1 
ATOM   761  C  CA    . VAL A 1 145 ? -25.039 34.102  -3.517  1.00 19.53 ? 255  VAL A CA    1 
ATOM   762  C  C     . VAL A 1 145 ? -23.905 34.558  -2.593  1.00 19.32 ? 255  VAL A C     1 
ATOM   763  O  O     . VAL A 1 145 ? -24.089 35.405  -1.716  1.00 20.60 ? 255  VAL A O     1 
ATOM   764  C  CB    . VAL A 1 145 ? -25.092 34.949  -4.814  1.00 21.56 ? 255  VAL A CB    1 
ATOM   765  C  CG1   . VAL A 1 145 ? -25.301 36.432  -4.489  1.00 23.41 ? 255  VAL A CG1   1 
ATOM   766  C  CG2   . VAL A 1 145 ? -23.828 34.722  -5.650  1.00 22.82 ? 255  VAL A CG2   1 
ATOM   767  N  N     . GLY A 1 146 ? -22.715 33.970  -2.797  1.00 18.22 ? 256  GLY A N     1 
ATOM   768  C  CA    . GLY A 1 146 ? -21.498 34.408  -2.142  1.00 17.98 ? 256  GLY A CA    1 
ATOM   769  C  C     . GLY A 1 146 ? -20.436 34.866  -3.142  1.00 17.58 ? 256  GLY A C     1 
ATOM   770  O  O     . GLY A 1 146 ? -20.565 34.658  -4.358  1.00 18.29 ? 256  GLY A O     1 
ATOM   771  N  N     . ALA A 1 147 ? -19.376 35.505  -2.614  1.00 17.40 ? 257  ALA A N     1 
ATOM   772  C  CA    . ALA A 1 147 ? -18.267 36.002  -3.431  1.00 18.25 ? 257  ALA A CA    1 
ATOM   773  C  C     . ALA A 1 147 ? -16.963 36.011  -2.637  1.00 18.63 ? 257  ALA A C     1 
ATOM   774  O  O     . ALA A 1 147 ? -16.962 36.325  -1.443  1.00 19.33 ? 257  ALA A O     1 
ATOM   775  C  CB    . ALA A 1 147 ? -18.543 37.424  -3.954  1.00 19.96 ? 257  ALA A CB    1 
ATOM   776  N  N     . ALA A 1 148 ? -15.851 35.685  -3.309  1.00 18.14 ? 258  ALA A N     1 
ATOM   777  C  CA    . ALA A 1 148 ? -14.529 35.647  -2.683  1.00 17.97 ? 258  ALA A CA    1 
ATOM   778  C  C     . ALA A 1 148 ? -13.831 37.011  -2.705  1.00 18.35 ? 258  ALA A C     1 
ATOM   779  O  O     . ALA A 1 148 ? -13.954 37.782  -3.664  1.00 19.87 ? 258  ALA A O     1 
ATOM   780  C  CB    . ALA A 1 148 ? -13.630 34.622  -3.382  1.00 19.26 ? 258  ALA A CB    1 
ATOM   781  N  N     . VAL A 1 149 ? -13.076 37.290  -1.634  1.00 16.51 ? 259  VAL A N     1 
ATOM   782  C  CA    . VAL A 1 149 ? -12.170 38.440  -1.557  1.00 16.41 ? 259  VAL A CA    1 
ATOM   783  C  C     . VAL A 1 149 ? -10.856 37.995  -0.907  1.00 18.32 ? 259  VAL A C     1 
ATOM   784  O  O     . VAL A 1 149 ? -10.795 36.976  -0.206  1.00 19.41 ? 259  VAL A O     1 
ATOM   785  C  CB    . VAL A 1 149 ? -12.776 39.636  -0.764  1.00 18.10 ? 259  VAL A CB    1 
ATOM   786  C  CG1   . VAL A 1 149 ? -14.122 40.083  -1.351  1.00 19.49 ? 259  VAL A CG1   1 
ATOM   787  C  CG2   . VAL A 1 149 ? -12.914 39.288  0.716   1.00 19.74 ? 259  VAL A CG2   1 
ATOM   788  N  N     . GLY A 1 150 ? -9.797  38.772  -1.144  1.00 17.32 ? 260  GLY A N     1 
ATOM   789  C  CA    . GLY A 1 150 ? -8.480  38.512  -0.565  1.00 18.82 ? 260  GLY A CA    1 
ATOM   790  C  C     . GLY A 1 150 ? -8.236  39.305  0.705   1.00 20.44 ? 260  GLY A C     1 
ATOM   791  O  O     . GLY A 1 150 ? -9.150  39.532  1.503   1.00 20.58 ? 260  GLY A O     1 
ATOM   792  N  N     . VAL A 1 151 ? -6.987  39.745  0.892   1.00 20.99 ? 261  VAL A N     1 
ATOM   793  C  CA    . VAL A 1 151 ? -6.565  40.484  2.083   1.00 23.08 ? 261  VAL A CA    1 
ATOM   794  C  C     . VAL A 1 151 ? -5.841  41.748  1.627   1.00 25.82 ? 261  VAL A C     1 
ATOM   795  O  O     . VAL A 1 151 ? -4.969  41.678  0.756   1.00 28.81 ? 261  VAL A O     1 
ATOM   796  C  CB    . VAL A 1 151 ? -5.646  39.633  2.984   1.00 24.48 ? 261  VAL A CB    1 
ATOM   797  C  CG1   . VAL A 1 151 ? -5.173  40.432  4.175   1.00 26.87 ? 261  VAL A CG1   1 
ATOM   798  C  CG2   . VAL A 1 151 ? -6.380  38.366  3.437   1.00 23.91 ? 261  VAL A CG2   1 
ATOM   799  N  N     . GLY A 1 152 ? -6.215  42.906  2.194   1.00 27.81 ? 262  GLY A N     1 
ATOM   800  C  CA    . GLY A 1 152 ? -5.535  44.158  1.905   1.00 32.74 ? 262  GLY A CA    1 
ATOM   801  C  C     . GLY A 1 152 ? -6.486  45.264  1.468   1.00 35.65 ? 262  GLY A C     1 
ATOM   802  O  O     . GLY A 1 152 ? -7.712  45.161  1.593   1.00 36.49 ? 262  GLY A O     1 
ATOM   803  N  N     . GLY A 1 153 ? -5.902  46.345  0.940   1.00 36.64 ? 263  GLY A N     1 
ATOM   804  C  CA    . GLY A 1 153 ? -6.693  47.517  0.595   1.00 35.75 ? 263  GLY A CA    1 
ATOM   805  C  C     . GLY A 1 153 ? -7.548  47.331  -0.649  1.00 35.44 ? 263  GLY A C     1 
ATOM   806  O  O     . GLY A 1 153 ? -8.696  47.788  -0.695  1.00 34.39 ? 263  GLY A O     1 
ATOM   807  N  N     . ASP A 1 154 ? -7.003  46.679  -1.683  1.00 35.84 ? 264  ASP A N     1 
ATOM   808  C  CA    . ASP A 1 154 ? -7.813  46.384  -2.868  1.00 36.04 ? 264  ASP A CA    1 
ATOM   809  C  C     . ASP A 1 154 ? -8.934  45.404  -2.543  1.00 29.57 ? 264  ASP A C     1 
ATOM   810  O  O     . ASP A 1 154 ? -10.063 45.555  -3.027  1.00 27.73 ? 264  ASP A O     1 
ATOM   811  C  CB    . ASP A 1 154 ? -6.933  45.831  -3.986  1.00 41.26 ? 264  ASP A CB    1 
ATOM   812  C  CG    . ASP A 1 154 ? -5.730  45.081  -3.457  1.00 47.54 ? 264  ASP A CG    1 
ATOM   813  O  OD1   . ASP A 1 154 ? -5.100  45.557  -2.484  1.00 49.16 ? 264  ASP A OD1   1 
ATOM   814  O  OD2   . ASP A 1 154 ? -5.418  44.007  -4.009  1.00 51.64 ? 264  ASP A OD2   1 
ATOM   815  N  N     . ALA A 1 155 ? -8.636  44.387  -1.734  1.00 25.32 ? 265  ALA A N     1 
ATOM   816  C  CA    . ALA A 1 155 ? -9.668  43.466  -1.274  1.00 22.36 ? 265  ALA A CA    1 
ATOM   817  C  C     . ALA A 1 155 ? -10.744 44.183  -0.462  1.00 21.77 ? 265  ALA A C     1 
ATOM   818  O  O     . ALA A 1 155 ? -11.912 43.760  -0.467  1.00 22.58 ? 265  ALA A O     1 
ATOM   819  C  CB    . ALA A 1 155 ? -9.024  42.355  -0.447  1.00 21.94 ? 265  ALA A CB    1 
ATOM   820  N  N     . TRP A 1 156 ? -10.375 45.253  0.252   1.00 23.15 ? 266  TRP A N     1 
ATOM   821  C  CA    . TRP A 1 156 ? -11.362 45.996  1.040   1.00 23.07 ? 266  TRP A CA    1 
ATOM   822  C  C     . TRP A 1 156 ? -12.367 46.719  0.142   1.00 22.71 ? 266  TRP A C     1 
ATOM   823  O  O     . TRP A 1 156 ? -13.586 46.608  0.339   1.00 20.82 ? 266  TRP A O     1 
ATOM   824  C  CB    . TRP A 1 156 ? -10.670 46.995  1.974   1.00 23.89 ? 266  TRP A CB    1 
ATOM   825  C  CG    . TRP A 1 156 ? -11.660 47.648  2.907   1.00 24.79 ? 266  TRP A CG    1 
ATOM   826  C  CD1   . TRP A 1 156 ? -12.243 48.888  2.766   1.00 25.63 ? 266  TRP A CD1   1 
ATOM   827  C  CD2   . TRP A 1 156 ? -12.216 47.082  4.100   1.00 26.95 ? 266  TRP A CD2   1 
ATOM   828  N  NE1   . TRP A 1 156 ? -13.107 49.123  3.806   1.00 26.49 ? 266  TRP A NE1   1 
ATOM   829  C  CE2   . TRP A 1 156 ? -13.118 48.030  4.633   1.00 28.23 ? 266  TRP A CE2   1 
ATOM   830  C  CE3   . TRP A 1 156 ? -12.038 45.866  4.772   1.00 28.50 ? 266  TRP A CE3   1 
ATOM   831  C  CZ2   . TRP A 1 156 ? -13.828 47.803  5.817   1.00 29.46 ? 266  TRP A CZ2   1 
ATOM   832  C  CZ3   . TRP A 1 156 ? -12.745 45.642  5.939   1.00 30.00 ? 266  TRP A CZ3   1 
ATOM   833  C  CH2   . TRP A 1 156 ? -13.633 46.605  6.450   1.00 31.07 ? 266  TRP A CH2   1 
ATOM   834  N  N     . VAL A 1 157 ? -11.873 47.484  -0.841  1.00 23.70 ? 267  VAL A N     1 
ATOM   835  C  CA    . VAL A 1 157 ? -12.759 48.130  -1.812  1.00 23.40 ? 267  VAL A CA    1 
ATOM   836  C  C     . VAL A 1 157 ? -13.620 47.090  -2.528  1.00 23.69 ? 267  VAL A C     1 
ATOM   837  O  O     . VAL A 1 157 ? -14.812 47.315  -2.778  1.00 24.36 ? 267  VAL A O     1 
ATOM   838  C  CB    . VAL A 1 157 ? -11.938 48.971  -2.811  1.00 25.54 ? 267  VAL A CB    1 
ATOM   839  C  CG1   . VAL A 1 157 ? -12.827 49.471  -3.931  1.00 26.84 ? 267  VAL A CG1   1 
ATOM   840  C  CG2   . VAL A 1 157 ? -11.276 50.144  -2.103  1.00 26.56 ? 267  VAL A CG2   1 
ATOM   841  N  N     . ARG A 1 158 ? -13.029 45.942  -2.883  1.00 21.47 ? 268  ARG A N     1 
ATOM   842  C  CA    . ARG A 1 158 ? -13.804 44.883  -3.527  1.00 22.40 ? 268  ARG A CA    1 
ATOM   843  C  C     . ARG A 1 158 ? -14.944 44.428  -2.622  1.00 22.46 ? 268  ARG A C     1 
ATOM   844  O  O     . ARG A 1 158 ? -16.101 44.341  -3.054  1.00 21.98 ? 268  ARG A O     1 
ATOM   845  C  CB    . ARG A 1 158 ? -12.888 43.711  -3.896  1.00 21.46 ? 268  ARG A CB    1 
ATOM   846  C  CG    . ARG A 1 158 ? -13.557 42.568  -4.682  1.00 22.06 ? 268  ARG A CG    1 
ATOM   847  C  CD    . ARG A 1 158 ? -12.565 41.423  -4.965  1.00 22.78 ? 268  ARG A CD    1 
ATOM   848  N  NE    . ARG A 1 158 ? -11.502 41.820  -5.891  1.00 23.01 ? 268  ARG A NE    1 
ATOM   849  C  CZ    . ARG A 1 158 ? -11.555 41.643  -7.208  1.00 23.35 ? 268  ARG A CZ    1 
ATOM   850  N  NH1   . ARG A 1 158 ? -12.630 41.079  -7.764  1.00 23.12 ? 268  ARG A NH1   1 
ATOM   851  N  NH2   . ARG A 1 158 ? -10.541 42.036  -7.973  1.00 24.20 ? 268  ARG A NH2   1 
ATOM   852  N  N     . ALA A 1 159 ? -14.638 44.161  -1.350  1.00 21.69 ? 269  ALA A N     1 
ATOM   853  C  CA    . ALA A 1 159 ? -15.670 43.734  -0.406  1.00 22.45 ? 269  ALA A CA    1 
ATOM   854  C  C     . ALA A 1 159 ? -16.793 44.762  -0.295  1.00 22.58 ? 269  ALA A C     1 
ATOM   855  O  O     . ALA A 1 159 ? -17.978 44.401  -0.265  1.00 23.79 ? 269  ALA A O     1 
ATOM   856  C  CB    . ALA A 1 159 ? -15.050 43.484  0.970   1.00 23.25 ? 269  ALA A CB    1 
ATOM   857  N  N     . MET A 1 160 ? -16.450 46.049  -0.196  1.00 23.51 ? 270  MET A N     1 
ATOM   858  C  CA    . MET A 1 160 ? -17.503 47.050  -0.021  1.00 25.02 ? 270  MET A CA    1 
ATOM   859  C  C     . MET A 1 160 ? -18.427 47.107  -1.237  1.00 26.09 ? 270  MET A C     1 
ATOM   860  O  O     . MET A 1 160 ? -19.645 47.279  -1.089  1.00 25.44 ? 270  MET A O     1 
ATOM   861  C  CB    . MET A 1 160 ? -16.898 48.429  0.260   1.00 26.28 ? 270  MET A CB    1 
ATOM   862  C  CG    . MET A 1 160 ? -16.075 48.518  1.556   1.00 27.94 ? 270  MET A CG    1 
ATOM   863  S  SD    . MET A 1 160 ? -16.929 48.107  3.107   1.00 29.80 ? 270  MET A SD    1 
ATOM   864  C  CE    . MET A 1 160 ? -16.618 46.333  3.214   1.00 32.69 ? 270  MET A CE    1 
ATOM   865  N  N     . MET A 1 161 ? -17.874 46.970  -2.448  1.00 26.58 ? 271  MET A N     1 
ATOM   866  C  CA    . MET A 1 161 ? -18.705 46.987  -3.652  1.00 28.84 ? 271  MET A CA    1 
ATOM   867  C  C     . MET A 1 161 ? -19.612 45.762  -3.720  1.00 25.48 ? 271  MET A C     1 
ATOM   868  O  O     . MET A 1 161 ? -20.767 45.858  -4.168  1.00 26.70 ? 271  MET A O     1 
ATOM   869  C  CB    . MET A 1 161 ? -17.827 47.055  -4.899  1.00 36.82 ? 271  MET A CB    1 
ATOM   870  C  CG    . MET A 1 161 ? -16.726 48.087  -4.822  1.00 45.70 ? 271  MET A CG    1 
ATOM   871  S  SD    . MET A 1 161 ? -16.799 49.209  -6.218  1.00 54.88 ? 271  MET A SD    1 
ATOM   872  C  CE    . MET A 1 161 ? -18.425 49.913  -5.956  1.00 59.17 ? 271  MET A CE    1 
ATOM   873  N  N     . LEU A 1 162 ? -19.103 44.599  -3.300  1.00 23.51 ? 272  LEU A N     1 
ATOM   874  C  CA    . LEU A 1 162 ? -19.921 43.389  -3.296  1.00 22.75 ? 272  LEU A CA    1 
ATOM   875  C  C     . LEU A 1 162 ? -21.100 43.532  -2.341  1.00 23.50 ? 272  LEU A C     1 
ATOM   876  O  O     . LEU A 1 162 ? -22.218 43.099  -2.654  1.00 23.49 ? 272  LEU A O     1 
ATOM   877  C  CB    . LEU A 1 162 ? -19.060 42.172  -2.927  1.00 20.78 ? 272  LEU A CB    1 
ATOM   878  C  CG    . LEU A 1 162 ? -17.993 41.774  -3.960  1.00 20.90 ? 272  LEU A CG    1 
ATOM   879  C  CD1   . LEU A 1 162 ? -16.928 40.827  -3.400  1.00 19.30 ? 272  LEU A CD1   1 
ATOM   880  C  CD2   . LEU A 1 162 ? -18.616 41.175  -5.216  1.00 23.26 ? 272  LEU A CD2   1 
ATOM   881  N  N     . VAL A 1 163 ? -20.872 44.142  -1.174  1.00 23.73 ? 273  VAL A N     1 
ATOM   882  C  CA    . VAL A 1 163 ? -21.956 44.361  -0.218  1.00 26.01 ? 273  VAL A CA    1 
ATOM   883  C  C     . VAL A 1 163 ? -23.008 45.300  -0.805  1.00 27.23 ? 273  VAL A C     1 
ATOM   884  O  O     . VAL A 1 163 ? -24.214 45.057  -0.682  1.00 27.67 ? 273  VAL A O     1 
ATOM   885  C  CB    . VAL A 1 163 ? -21.397 44.896  1.115   1.00 28.36 ? 273  VAL A CB    1 
ATOM   886  C  CG1   . VAL A 1 163 ? -22.532 45.377  2.020   1.00 29.13 ? 273  VAL A CG1   1 
ATOM   887  C  CG2   . VAL A 1 163 ? -20.559 43.822  1.819   1.00 29.18 ? 273  VAL A CG2   1 
ATOM   888  N  N     . ASP A 1 164 ? -22.571 46.387  -1.449  1.00 26.70 ? 274  ASP A N     1 
ATOM   889  C  CA    . ASP A 1 164 ? -23.520 47.310  -2.064  1.00 28.85 ? 274  ASP A CA    1 
ATOM   890  C  C     . ASP A 1 164 ? -24.349 46.629  -3.148  1.00 29.22 ? 274  ASP A C     1 
ATOM   891  O  O     . ASP A 1 164 ? -25.500 47.017  -3.381  1.00 30.72 ? 274  ASP A O     1 
ATOM   892  C  CB    . ASP A 1 164 ? -22.784 48.518  -2.647  1.00 31.41 ? 274  ASP A CB    1 
ATOM   893  C  CG    . ASP A 1 164 ? -22.278 49.474  -1.580  1.00 36.00 ? 274  ASP A CG    1 
ATOM   894  O  OD1   . ASP A 1 164 ? -22.686 49.348  -0.405  1.00 37.50 ? 274  ASP A OD1   1 
ATOM   895  O  OD2   . ASP A 1 164 ? -21.459 50.352  -1.925  1.00 38.74 ? 274  ASP A OD2   1 
ATOM   896  N  N     . ALA A 1 165 ? -23.784 45.623  -3.825  1.00 27.84 ? 275  ALA A N     1 
ATOM   897  C  CA    . ALA A 1 165 ? -24.492 44.905  -4.879  1.00 28.50 ? 275  ALA A CA    1 
ATOM   898  C  C     . ALA A 1 165 ? -25.473 43.870  -4.344  1.00 28.27 ? 275  ALA A C     1 
ATOM   899  O  O     . ALA A 1 165 ? -26.239 43.306  -5.136  1.00 29.76 ? 275  ALA A O     1 
ATOM   900  C  CB    . ALA A 1 165 ? -23.494 44.217  -5.815  1.00 28.34 ? 275  ALA A CB    1 
ATOM   901  N  N     . GLY A 1 166 ? -25.458 43.597  -3.042  1.00 26.96 ? 276  GLY A N     1 
ATOM   902  C  CA    . GLY A 1 166 ? -26.413 42.695  -2.430  1.00 27.57 ? 276  GLY A CA    1 
ATOM   903  C  C     . GLY A 1 166 ? -25.913 41.303  -2.082  1.00 26.95 ? 276  GLY A C     1 
ATOM   904  O  O     . GLY A 1 166 ? -26.744 40.414  -1.854  1.00 26.96 ? 276  GLY A O     1 
ATOM   905  N  N     . VAL A 1 167 ? -24.596 41.077  -2.024  1.00 25.30 ? 277  VAL A N     1 
ATOM   906  C  CA    . VAL A 1 167 ? -24.109 39.722  -1.760  1.00 23.01 ? 277  VAL A CA    1 
ATOM   907  C  C     . VAL A 1 167 ? -24.554 39.271  -0.365  1.00 22.17 ? 277  VAL A C     1 
ATOM   908  O  O     . VAL A 1 167 ? -24.663 40.075  0.568   1.00 24.58 ? 277  VAL A O     1 
ATOM   909  C  CB    . VAL A 1 167 ? -22.578 39.651  -1.910  1.00 23.18 ? 277  VAL A CB    1 
ATOM   910  C  CG1   . VAL A 1 167 ? -21.879 40.185  -0.667  1.00 24.82 ? 277  VAL A CG1   1 
ATOM   911  C  CG2   . VAL A 1 167 ? -22.113 38.220  -2.245  1.00 23.29 ? 277  VAL A CG2   1 
ATOM   912  N  N     . ASP A 1 168 ? -24.808 37.960  -0.216  1.00 21.97 ? 278  ASP A N     1 
ATOM   913  C  CA    . ASP A 1 168 ? -25.237 37.406  1.068   1.00 22.41 ? 278  ASP A CA    1 
ATOM   914  C  C     . ASP A 1 168 ? -24.077 36.933  1.951   1.00 21.83 ? 278  ASP A C     1 
ATOM   915  O  O     . ASP A 1 168 ? -24.192 36.986  3.185   1.00 22.14 ? 278  ASP A O     1 
ATOM   916  C  CB    . ASP A 1 168 ? -26.204 36.234  0.838   1.00 25.12 ? 278  ASP A CB    1 
ATOM   917  C  CG    . ASP A 1 168 ? -27.445 36.636  0.050   1.00 26.29 ? 278  ASP A CG    1 
ATOM   918  O  OD1   . ASP A 1 168 ? -28.351 37.282  0.627   1.00 28.62 ? 278  ASP A OD1   1 
ATOM   919  O  OD2   . ASP A 1 168 ? -27.519 36.315  -1.156  1.00 26.04 ? 278  ASP A OD2   1 
ATOM   920  N  N     . VAL A 1 169 ? -22.973 36.469  1.354   1.00 20.50 ? 279  VAL A N     1 
ATOM   921  C  CA    . VAL A 1 169 ? -21.830 35.884  2.064   1.00 21.47 ? 279  VAL A CA    1 
ATOM   922  C  C     . VAL A 1 169 ? -20.541 36.379  1.413   1.00 20.90 ? 279  VAL A C     1 
ATOM   923  O  O     . VAL A 1 169 ? -20.383 36.265  0.194   1.00 21.83 ? 279  VAL A O     1 
ATOM   924  C  CB    . VAL A 1 169 ? -21.878 34.336  2.032   1.00 21.33 ? 279  VAL A CB    1 
ATOM   925  C  CG1   . VAL A 1 169 ? -20.690 33.722  2.763   1.00 21.06 ? 279  VAL A CG1   1 
ATOM   926  C  CG2   . VAL A 1 169 ? -23.192 33.824  2.610   1.00 23.60 ? 279  VAL A CG2   1 
ATOM   927  N  N     . LEU A 1 170 ? -19.626 36.939  2.216   1.00 19.96 ? 280  LEU A N     1 
ATOM   928  C  CA    . LEU A 1 170 ? -18.242 37.188  1.804   1.00 18.67 ? 280  LEU A CA    1 
ATOM   929  C  C     . LEU A 1 170 ? -17.346 36.048  2.288   1.00 19.02 ? 280  LEU A C     1 
ATOM   930  O  O     . LEU A 1 170 ? -17.422 35.657  3.456   1.00 19.64 ? 280  LEU A O     1 
ATOM   931  C  CB    . LEU A 1 170 ? -17.719 38.509  2.377   1.00 19.01 ? 280  LEU A CB    1 
ATOM   932  C  CG    . LEU A 1 170 ? -18.315 39.819  1.861   1.00 20.35 ? 280  LEU A CG    1 
ATOM   933  C  CD1   . LEU A 1 170 ? -17.836 40.986  2.726   1.00 21.55 ? 280  LEU A CD1   1 
ATOM   934  C  CD2   . LEU A 1 170 ? -17.940 40.032  0.398   1.00 20.71 ? 280  LEU A CD2   1 
ATOM   935  N  N     . VAL A 1 171 ? -16.471 35.545  1.408   1.00 18.58 ? 281  VAL A N     1 
ATOM   936  C  CA    . VAL A 1 171 ? -15.515 34.483  1.746   1.00 17.44 ? 281  VAL A CA    1 
ATOM   937  C  C     . VAL A 1 171 ? -14.101 35.070  1.670   1.00 17.51 ? 281  VAL A C     1 
ATOM   938  O  O     . VAL A 1 171 ? -13.601 35.364  0.575   1.00 18.70 ? 281  VAL A O     1 
ATOM   939  C  CB    . VAL A 1 171 ? -15.665 33.262  0.820   1.00 18.34 ? 281  VAL A CB    1 
ATOM   940  C  CG1   . VAL A 1 171 ? -14.614 32.216  1.146   1.00 19.07 ? 281  VAL A CG1   1 
ATOM   941  C  CG2   . VAL A 1 171 ? -17.056 32.644  0.960   1.00 18.32 ? 281  VAL A CG2   1 
ATOM   942  N  N     . VAL A 1 172 ? -13.454 35.246  2.825   1.00 17.59 ? 282  VAL A N     1 
ATOM   943  C  CA    . VAL A 1 172 ? -12.037 35.625  2.859   1.00 17.88 ? 282  VAL A CA    1 
ATOM   944  C  C     . VAL A 1 172 ? -11.236 34.392  2.432   1.00 18.16 ? 282  VAL A C     1 
ATOM   945  O  O     . VAL A 1 172 ? -11.229 33.368  3.125   1.00 18.46 ? 282  VAL A O     1 
ATOM   946  C  CB    . VAL A 1 172 ? -11.606 36.144  4.244   1.00 18.39 ? 282  VAL A CB    1 
ATOM   947  C  CG1   . VAL A 1 172 ? -10.121 36.567  4.252   1.00 19.75 ? 282  VAL A CG1   1 
ATOM   948  C  CG2   . VAL A 1 172 ? -12.465 37.352  4.677   1.00 19.34 ? 282  VAL A CG2   1 
ATOM   949  N  N     . ASP A 1 173 ? -10.592 34.483  1.271   1.00 17.09 ? 283  ASP A N     1 
ATOM   950  C  CA    . ASP A 1 173 ? -10.172 33.340  0.447   1.00 16.50 ? 283  ASP A CA    1 
ATOM   951  C  C     . ASP A 1 173 ? -8.645  33.286  0.384   1.00 17.36 ? 283  ASP A C     1 
ATOM   952  O  O     . ASP A 1 173 ? -8.038  33.965  -0.455  1.00 18.57 ? 283  ASP A O     1 
ATOM   953  C  CB    . ASP A 1 173 ? -10.818 33.494  -0.943  1.00 17.78 ? 283  ASP A CB    1 
ATOM   954  C  CG    . ASP A 1 173 ? -10.181 32.623  -2.022  1.00 18.79 ? 283  ASP A CG    1 
ATOM   955  O  OD1   . ASP A 1 173 ? -9.933  31.407  -1.775  1.00 18.27 ? 283  ASP A OD1   1 
ATOM   956  O  OD2   . ASP A 1 173 ? -9.979  33.150  -3.147  1.00 19.89 ? 283  ASP A OD2   1 
ATOM   957  N  N     . THR A 1 174 ? -8.018  32.475  1.255   1.00 16.08 ? 284  THR A N     1 
ATOM   958  C  CA    . THR A 1 174 ? -6.557  32.387  1.323   1.00 18.84 ? 284  THR A CA    1 
ATOM   959  C  C     . THR A 1 174 ? -6.089  30.935  1.411   1.00 18.22 ? 284  THR A C     1 
ATOM   960  O  O     . THR A 1 174 ? -6.856  30.005  1.714   1.00 18.18 ? 284  THR A O     1 
ATOM   961  C  CB    . THR A 1 174 ? -5.968  33.166  2.520   1.00 19.49 ? 284  THR A CB    1 
ATOM   962  O  OG1   . THR A 1 174 ? -6.189  32.445  3.740   1.00 19.80 ? 284  THR A OG1   1 
ATOM   963  C  CG2   . THR A 1 174 ? -6.565  34.599  2.631   1.00 20.37 ? 284  THR A CG2   1 
ATOM   964  N  N     . ALA A 1 175 ? -4.791  30.756  1.147   1.00 17.42 ? 285  ALA A N     1 
ATOM   965  C  CA    . ALA A 1 175 ? -4.156  29.449  1.274   1.00 16.61 ? 285  ALA A CA    1 
ATOM   966  C  C     . ALA A 1 175 ? -3.794  29.086  2.713   1.00 16.90 ? 285  ALA A C     1 
ATOM   967  O  O     . ALA A 1 175 ? -3.562  27.899  2.990   1.00 17.05 ? 285  ALA A O     1 
ATOM   968  C  CB    . ALA A 1 175 ? -2.891  29.396  0.418   1.00 19.41 ? 285  ALA A CB    1 
ATOM   969  N  N     . HIS A 1 176 ? -3.708  30.067  3.621   1.00 17.31 ? 286  HIS A N     1 
ATOM   970  C  CA    . HIS A 1 176 ? -3.207  29.830  4.985   1.00 16.94 ? 286  HIS A CA    1 
ATOM   971  C  C     . HIS A 1 176 ? -3.817  30.900  5.900   1.00 16.67 ? 286  HIS A C     1 
ATOM   972  O  O     . HIS A 1 176 ? -3.244  31.979  6.081   1.00 17.59 ? 286  HIS A O     1 
ATOM   973  C  CB    . HIS A 1 176 ? -1.678  29.857  5.011   1.00 16.72 ? 286  HIS A CB    1 
ATOM   974  C  CG    . HIS A 1 176 ? -1.085  29.533  6.348   1.00 18.26 ? 286  HIS A CG    1 
ATOM   975  N  ND1   . HIS A 1 176 ? -1.590  28.551  7.174   1.00 18.55 ? 286  HIS A ND1   1 
ATOM   976  C  CD2   . HIS A 1 176 ? -0.008  30.045  6.991   1.00 19.30 ? 286  HIS A CD2   1 
ATOM   977  C  CE1   . HIS A 1 176 ? -0.867  28.490  8.278   1.00 16.50 ? 286  HIS A CE1   1 
ATOM   978  N  NE2   . HIS A 1 176 ? 0.099   29.390  8.193   1.00 18.05 ? 286  HIS A NE2   1 
ATOM   979  N  N     . ALA A 1 177 ? -4.987  30.593  6.475   1.00 15.82 ? 287  ALA A N     1 
ATOM   980  C  CA    . ALA A 1 177 ? -5.673  31.593  7.290   1.00 15.14 ? 287  ALA A CA    1 
ATOM   981  C  C     . ALA A 1 177 ? -5.089  31.765  8.697   1.00 17.94 ? 287  ALA A C     1 
ATOM   982  O  O     . ALA A 1 177 ? -5.518  32.686  9.401   1.00 19.57 ? 287  ALA A O     1 
ATOM   983  C  CB    . ALA A 1 177 ? -7.176  31.268  7.387   1.00 16.70 ? 287  ALA A CB    1 
ATOM   984  N  N     . HIS A 1 178 ? -4.111  30.945  9.123   1.00 18.35 ? 288  HIS A N     1 
ATOM   985  C  CA    . HIS A 1 178 ? -3.546  31.068  10.471  1.00 17.65 ? 288  HIS A CA    1 
ATOM   986  C  C     . HIS A 1 178 ? -2.525  32.210  10.554  1.00 21.68 ? 288  HIS A C     1 
ATOM   987  O  O     . HIS A 1 178 ? -1.400  32.018  11.005  1.00 22.82 ? 288  HIS A O     1 
ATOM   988  C  CB    . HIS A 1 178 ? -2.920  29.728  10.905  1.00 17.91 ? 288  HIS A CB    1 
ATOM   989  C  CG    . HIS A 1 178 ? -2.912  29.498  12.392  1.00 17.84 ? 288  HIS A CG    1 
ATOM   990  N  ND1   . HIS A 1 178 ? -2.531  28.299  12.960  1.00 18.81 ? 288  HIS A ND1   1 
ATOM   991  C  CD2   . HIS A 1 178 ? -3.260  30.305  13.421  1.00 19.58 ? 288  HIS A CD2   1 
ATOM   992  C  CE1   . HIS A 1 178 ? -2.625  28.385  14.275  1.00 19.38 ? 288  HIS A CE1   1 
ATOM   993  N  NE2   . HIS A 1 178 ? -3.072  29.591  14.580  1.00 19.27 ? 288  HIS A NE2   1 
ATOM   994  N  N     . ASN A 1 179 ? -2.923  33.418  10.171  1.00 28.54 ? 289  ASN A N     1 
ATOM   995  C  CA    . ASN A 1 179 ? -2.024  34.569  10.108  1.00 32.49 ? 289  ASN A CA    1 
ATOM   996  C  C     . ASN A 1 179 ? -2.780  35.788  10.606  1.00 33.23 ? 289  ASN A C     1 
ATOM   997  O  O     . ASN A 1 179 ? -3.945  35.972  10.256  1.00 31.98 ? 289  ASN A O     1 
ATOM   998  C  CB    . ASN A 1 179 ? -1.520  34.787  8.675   1.00 34.57 ? 289  ASN A CB    1 
ATOM   999  C  CG    . ASN A 1 179 ? -0.662  36.037  8.524   1.00 39.05 ? 289  ASN A CG    1 
ATOM   1000 O  OD1   . ASN A 1 179 ? -1.027  37.128  8.969   1.00 42.65 ? 289  ASN A OD1   1 
ATOM   1001 N  ND2   . ASN A 1 179 ? 0.483   35.879  7.882   1.00 37.80 ? 289  ASN A ND2   1 
ATOM   1002 N  N     . ARG A 1 180 ? -2.127  36.623  11.421  1.00 33.70 ? 290  ARG A N     1 
ATOM   1003 C  CA    . ARG A 1 180 ? -2.858  37.744  12.007  1.00 37.22 ? 290  ARG A CA    1 
ATOM   1004 C  C     . ARG A 1 180 ? -3.430  38.662  10.935  1.00 34.97 ? 290  ARG A C     1 
ATOM   1005 O  O     . ARG A 1 180 ? -4.477  39.278  11.151  1.00 35.49 ? 290  ARG A O     1 
ATOM   1006 C  CB    . ARG A 1 180 ? -1.963  38.528  12.973  1.00 42.22 ? 290  ARG A CB    1 
ATOM   1007 C  CG    . ARG A 1 180 ? -0.751  39.153  12.329  1.00 47.95 ? 290  ARG A CG    1 
ATOM   1008 C  CD    . ARG A 1 180 ? 0.169   39.735  13.388  1.00 52.77 ? 290  ARG A CD    1 
ATOM   1009 N  NE    . ARG A 1 180 ? 0.325   38.814  14.511  1.00 58.03 ? 290  ARG A NE    1 
ATOM   1010 C  CZ    . ARG A 1 180 ? 1.310   38.875  15.401  1.00 61.44 ? 290  ARG A CZ    1 
ATOM   1011 N  NH1   . ARG A 1 180 ? 1.367   37.992  16.389  1.00 63.14 ? 290  ARG A NH1   1 
ATOM   1012 N  NH2   . ARG A 1 180 ? 2.243   39.812  15.297  1.00 62.72 ? 290  ARG A NH2   1 
ATOM   1013 N  N     . LEU A 1 181 ? -2.774  38.762  9.772   1.00 34.23 ? 291  LEU A N     1 
ATOM   1014 C  CA    . LEU A 1 181 ? -3.308  39.604  8.701   1.00 31.69 ? 291  LEU A CA    1 
ATOM   1015 C  C     . LEU A 1 181 ? -4.622  39.049  8.153   1.00 28.86 ? 291  LEU A C     1 
ATOM   1016 O  O     . LEU A 1 181 ? -5.529  39.818  7.813   1.00 29.96 ? 291  LEU A O     1 
ATOM   1017 C  CB    . LEU A 1 181 ? -2.284  39.759  7.570   1.00 31.23 ? 291  LEU A CB    1 
ATOM   1018 C  CG    . LEU A 1 181 ? -0.980  40.507  7.868   1.00 33.98 ? 291  LEU A CG    1 
ATOM   1019 C  CD1   . LEU A 1 181 ? -0.115  40.601  6.613   1.00 34.53 ? 291  LEU A CD1   1 
ATOM   1020 C  CD2   . LEU A 1 181 ? -1.269  41.887  8.429   1.00 35.02 ? 291  LEU A CD2   1 
ATOM   1021 N  N     . VAL A 1 182 ? -4.745  37.722  8.048   1.00 25.29 ? 292  VAL A N     1 
ATOM   1022 C  CA    . VAL A 1 182 ? -6.012  37.144  7.596   1.00 23.26 ? 292  VAL A CA    1 
ATOM   1023 C  C     . VAL A 1 182 ? -7.059  37.226  8.699   1.00 23.76 ? 292  VAL A C     1 
ATOM   1024 O  O     . VAL A 1 182 ? -8.220  37.573  8.449   1.00 23.52 ? 292  VAL A O     1 
ATOM   1025 C  CB    . VAL A 1 182 ? -5.814  35.694  7.112   1.00 23.87 ? 292  VAL A CB    1 
ATOM   1026 C  CG1   . VAL A 1 182 ? -7.146  35.121  6.626   1.00 22.93 ? 292  VAL A CG1   1 
ATOM   1027 C  CG2   . VAL A 1 182 ? -4.756  35.634  6.007   1.00 25.74 ? 292  VAL A CG2   1 
ATOM   1028 N  N     . LEU A 1 183 ? -6.669  36.914  9.937   1.00 25.45 ? 293  LEU A N     1 
ATOM   1029 C  CA    . LEU A 1 183 ? -7.596  37.042  11.057  1.00 25.24 ? 293  LEU A CA    1 
ATOM   1030 C  C     . LEU A 1 183 ? -8.080  38.484  11.210  1.00 27.23 ? 293  LEU A C     1 
ATOM   1031 O  O     . LEU A 1 183 ? -9.248  38.725  11.543  1.00 26.45 ? 293  LEU A O     1 
ATOM   1032 C  CB    . LEU A 1 183 ? -6.920  36.552  12.340  1.00 24.73 ? 293  LEU A CB    1 
ATOM   1033 C  CG    . LEU A 1 183 ? -6.331  35.141  12.301  1.00 24.17 ? 293  LEU A CG    1 
ATOM   1034 C  CD1   . LEU A 1 183 ? -5.469  34.881  13.534  1.00 25.63 ? 293  LEU A CD1   1 
ATOM   1035 C  CD2   . LEU A 1 183 ? -7.448  34.093  12.179  1.00 23.35 ? 293  LEU A CD2   1 
ATOM   1036 N  N     . ASP A 1 184 ? -7.193  39.456  10.967  1.00 29.43 ? 294  ASP A N     1 
ATOM   1037 C  CA    . ASP A 1 184 ? -7.574  40.863  11.061  1.00 31.40 ? 294  ASP A CA    1 
ATOM   1038 C  C     . ASP A 1 184 ? -8.631  41.229  10.026  1.00 29.66 ? 294  ASP A C     1 
ATOM   1039 O  O     . ASP A 1 184 ? -9.573  41.972  10.328  1.00 32.42 ? 294  ASP A O     1 
ATOM   1040 C  CB    . ASP A 1 184 ? -6.342  41.755  10.891  1.00 34.83 ? 294  ASP A CB    1 
ATOM   1041 C  CG    . ASP A 1 184 ? -5.420  41.716  12.094  1.00 40.55 ? 294  ASP A CG    1 
ATOM   1042 O  OD1   . ASP A 1 184 ? -5.926  41.680  13.236  1.00 41.49 ? 294  ASP A OD1   1 
ATOM   1043 O  OD2   . ASP A 1 184 ? -4.185  41.722  11.899  1.00 44.59 ? 294  ASP A OD2   1 
ATOM   1044 N  N     . MET A 1 185 ? -8.474  40.745  8.790   1.00 26.90 ? 295  MET A N     1 
ATOM   1045 C  CA    . MET A 1 185 ? -9.470  41.005  7.748   1.00 25.80 ? 295  MET A CA    1 
ATOM   1046 C  C     . MET A 1 185 ? -10.843 40.466  8.142   1.00 24.81 ? 295  MET A C     1 
ATOM   1047 O  O     . MET A 1 185 ? -11.861 41.145  7.961   1.00 25.18 ? 295  MET A O     1 
ATOM   1048 C  CB    . MET A 1 185 ? -9.010  40.384  6.424   1.00 26.60 ? 295  MET A CB    1 
ATOM   1049 C  CG    . MET A 1 185 ? -9.866  40.701  5.214   1.00 26.42 ? 295  MET A CG    1 
ATOM   1050 S  SD    . MET A 1 185 ? -9.720  42.402  4.651   1.00 30.30 ? 295  MET A SD    1 
ATOM   1051 C  CE    . MET A 1 185 ? -10.785 42.407  3.208   1.00 29.70 ? 295  MET A CE    1 
ATOM   1052 N  N     . VAL A 1 186 ? -10.895 39.235  8.658   1.00 24.38 ? 296  VAL A N     1 
ATOM   1053 C  CA    . VAL A 1 186 ? -12.169 38.652  9.087   1.00 24.27 ? 296  VAL A CA    1 
ATOM   1054 C  C     . VAL A 1 186 ? -12.825 39.523  10.156  1.00 25.68 ? 296  VAL A C     1 
ATOM   1055 O  O     . VAL A 1 186 ? -14.016 39.852  10.072  1.00 27.32 ? 296  VAL A O     1 
ATOM   1056 C  CB    . VAL A 1 186 ? -11.960 37.206  9.580   1.00 22.99 ? 296  VAL A CB    1 
ATOM   1057 C  CG1   . VAL A 1 186 ? -13.230 36.658  10.275  1.00 23.28 ? 296  VAL A CG1   1 
ATOM   1058 C  CG2   . VAL A 1 186 ? -11.564 36.319  8.412   1.00 22.29 ? 296  VAL A CG2   1 
ATOM   1059 N  N     . GLY A 1 187 ? -12.050 39.926  11.166  1.00 25.73 ? 297  GLY A N     1 
ATOM   1060 C  CA    . GLY A 1 187 ? -12.610 40.734  12.239  1.00 27.90 ? 297  GLY A CA    1 
ATOM   1061 C  C     . GLY A 1 187 ? -13.061 42.115  11.789  1.00 29.40 ? 297  GLY A C     1 
ATOM   1062 O  O     . GLY A 1 187 ? -14.101 42.611  12.230  1.00 30.34 ? 297  GLY A O     1 
ATOM   1063 N  N     . LYS A 1 188 ? -12.285 42.766  10.919  1.00 29.04 ? 298  LYS A N     1 
ATOM   1064 C  CA    . LYS A 1 188 ? -12.679 44.096  10.459  1.00 30.38 ? 298  LYS A CA    1 
ATOM   1065 C  C     . LYS A 1 188 ? -13.951 44.050  9.615   1.00 29.79 ? 298  LYS A C     1 
ATOM   1066 O  O     . LYS A 1 188 ? -14.803 44.941  9.723   1.00 30.93 ? 298  LYS A O     1 
ATOM   1067 C  CB    . LYS A 1 188 ? -11.545 44.752  9.678   1.00 32.40 ? 298  LYS A CB    1 
ATOM   1068 C  CG    . LYS A 1 188 ? -11.908 46.135  9.184   1.00 36.49 ? 298  LYS A CG    1 
ATOM   1069 C  CD    . LYS A 1 188 ? -10.782 46.764  8.396   1.00 39.95 ? 298  LYS A CD    1 
ATOM   1070 C  CE    . LYS A 1 188 ? -11.116 48.208  8.047   1.00 41.34 ? 298  LYS A CE    1 
ATOM   1071 N  NZ    . LYS A 1 188 ? -10.196 48.724  7.017   1.00 43.20 ? 298  LYS A NZ    1 
ATOM   1072 N  N     . LEU A 1 189 ? -14.095 43.032  8.757   1.00 28.02 ? 299  LEU A N     1 
ATOM   1073 C  CA    . LEU A 1 189 ? -15.316 42.898  7.962   1.00 28.16 ? 299  LEU A CA    1 
ATOM   1074 C  C     . LEU A 1 189 ? -16.521 42.677  8.868   1.00 30.64 ? 299  LEU A C     1 
ATOM   1075 O  O     . LEU A 1 189 ? -17.566 43.315  8.702   1.00 31.53 ? 299  LEU A O     1 
ATOM   1076 C  CB    . LEU A 1 189 ? -15.180 41.747  6.955   1.00 27.08 ? 299  LEU A CB    1 
ATOM   1077 C  CG    . LEU A 1 189 ? -14.334 41.956  5.692   1.00 26.52 ? 299  LEU A CG    1 
ATOM   1078 C  CD1   . LEU A 1 189 ? -14.237 40.651  4.891   1.00 25.88 ? 299  LEU A CD1   1 
ATOM   1079 C  CD2   . LEU A 1 189 ? -14.893 43.084  4.815   1.00 27.60 ? 299  LEU A CD2   1 
ATOM   1080 N  N     . LYS A 1 190 ? -16.389 41.769  9.840   1.00 32.42 ? 300  LYS A N     1 
ATOM   1081 C  CA    . LYS A 1 190 ? -17.481 41.542  10.781  1.00 33.98 ? 300  LYS A CA    1 
ATOM   1082 C  C     . LYS A 1 190 ? -17.828 42.820  11.538  1.00 34.58 ? 300  LYS A C     1 
ATOM   1083 O  O     . LYS A 1 190 ? -19.004 43.097  11.793  1.00 34.44 ? 300  LYS A O     1 
ATOM   1084 C  CB    . LYS A 1 190 ? -17.120 40.407  11.743  1.00 36.73 ? 300  LYS A CB    1 
ATOM   1085 C  CG    . LYS A 1 190 ? -18.008 39.158  11.599  1.00 38.72 ? 300  LYS A CG    1 
ATOM   1086 C  CD    . LYS A 1 190 ? -19.404 39.422  12.155  1.00 41.47 ? 300  LYS A CD    1 
ATOM   1087 C  CE    . LYS A 1 190 ? -20.402 38.347  11.770  1.00 41.51 ? 300  LYS A CE    1 
ATOM   1088 N  NZ    . LYS A 1 190 ? -21.398 38.773  10.729  1.00 40.22 ? 300  LYS A NZ    1 
ATOM   1089 N  N     . SER A 1 191 ? -16.820 43.626  11.888  1.00 33.59 ? 301  SER A N     1 
ATOM   1090 C  CA    . SER A 1 191 ? -17.092 44.874  12.600  1.00 36.98 ? 301  SER A CA    1 
ATOM   1091 C  C     . SER A 1 191 ? -17.857 45.863  11.729  1.00 38.04 ? 301  SER A C     1 
ATOM   1092 O  O     . SER A 1 191 ? -18.793 46.519  12.201  1.00 39.98 ? 301  SER A O     1 
ATOM   1093 C  CB    . SER A 1 191 ? -15.790 45.505  13.086  1.00 38.79 ? 301  SER A CB    1 
ATOM   1094 O  OG    . SER A 1 191 ? -15.389 44.932  14.312  1.00 41.62 ? 301  SER A OG    1 
ATOM   1095 N  N     . GLU A 1 192 ? -17.475 45.986  10.457  1.00 38.10 ? 302  GLU A N     1 
ATOM   1096 C  CA    . GLU A 1 192 ? -18.021 47.047  9.616   1.00 39.33 ? 302  GLU A CA    1 
ATOM   1097 C  C     . GLU A 1 192 ? -19.361 46.667  9.002   1.00 37.15 ? 302  GLU A C     1 
ATOM   1098 O  O     . GLU A 1 192 ? -20.283 47.488  8.972   1.00 37.43 ? 302  GLU A O     1 
ATOM   1099 C  CB    . GLU A 1 192 ? -17.025 47.402  8.513   1.00 44.45 ? 302  GLU A CB    1 
ATOM   1100 C  CG    . GLU A 1 192 ? -15.709 47.943  9.031   1.00 48.54 ? 302  GLU A CG    1 
ATOM   1101 C  CD    . GLU A 1 192 ? -15.861 49.310  9.659   1.00 51.72 ? 302  GLU A CD    1 
ATOM   1102 O  OE1   . GLU A 1 192 ? -16.761 50.062  9.225   1.00 52.95 ? 302  GLU A OE1   1 
ATOM   1103 O  OE2   . GLU A 1 192 ? -15.090 49.627  10.590  1.00 52.62 ? 302  GLU A OE2   1 
ATOM   1104 N  N     . VAL A 1 193 ? -19.490 45.442  8.502   1.00 34.47 ? 303  VAL A N     1 
ATOM   1105 C  CA    . VAL A 1 193 ? -20.656 45.091  7.702   1.00 34.46 ? 303  VAL A CA    1 
ATOM   1106 C  C     . VAL A 1 193 ? -21.315 43.823  8.226   1.00 35.75 ? 303  VAL A C     1 
ATOM   1107 O  O     . VAL A 1 193 ? -22.222 43.284  7.584   1.00 36.37 ? 303  VAL A O     1 
ATOM   1108 C  CB    . VAL A 1 193 ? -20.273 44.930  6.218   1.00 34.01 ? 303  VAL A CB    1 
ATOM   1109 C  CG1   . VAL A 1 193 ? -19.911 46.284  5.613   1.00 34.46 ? 303  VAL A CG1   1 
ATOM   1110 C  CG2   . VAL A 1 193 ? -19.114 43.932  6.059   1.00 34.15 ? 303  VAL A CG2   1 
ATOM   1111 N  N     . GLY A 1 194 ? -20.879 43.350  9.398   1.00 37.12 ? 304  GLY A N     1 
ATOM   1112 C  CA    . GLY A 1 194 ? -21.356 42.082  9.935   1.00 36.98 ? 304  GLY A CA    1 
ATOM   1113 C  C     . GLY A 1 194 ? -22.840 42.043  10.235  1.00 40.18 ? 304  GLY A C     1 
ATOM   1114 O  O     . GLY A 1 194 ? -23.408 40.954  10.391  1.00 40.49 ? 304  GLY A O     1 
ATOM   1115 N  N     . ASP A 1 195 ? -23.486 43.205  10.332  1.00 42.95 ? 305  ASP A N     1 
ATOM   1116 C  CA    . ASP A 1 195 ? -24.932 43.222  10.504  1.00 46.32 ? 305  ASP A CA    1 
ATOM   1117 C  C     . ASP A 1 195 ? -25.661 42.921  9.203   1.00 46.02 ? 305  ASP A C     1 
ATOM   1118 O  O     . ASP A 1 195 ? -26.802 42.445  9.230   1.00 48.28 ? 305  ASP A O     1 
ATOM   1119 C  CB    . ASP A 1 195 ? -25.385 44.579  11.045  1.00 50.20 ? 305  ASP A CB    1 
ATOM   1120 C  CG    . ASP A 1 195 ? -24.975 45.732  10.143  1.00 54.69 ? 305  ASP A CG    1 
ATOM   1121 O  OD1   . ASP A 1 195 ? -23.767 45.845  9.832   1.00 56.67 ? 305  ASP A OD1   1 
ATOM   1122 O  OD2   . ASP A 1 195 ? -25.861 46.516  9.736   1.00 56.92 ? 305  ASP A OD2   1 
ATOM   1123 N  N     . ARG A 1 196 ? -25.028 43.194  8.063   1.00 42.73 ? 306  ARG A N     1 
ATOM   1124 C  CA    . ARG A 1 196 ? -25.666 43.017  6.768   1.00 40.77 ? 306  ARG A CA    1 
ATOM   1125 C  C     . ARG A 1 196 ? -25.252 41.742  6.041   1.00 35.45 ? 306  ARG A C     1 
ATOM   1126 O  O     . ARG A 1 196 ? -26.028 41.243  5.220   1.00 38.13 ? 306  ARG A O     1 
ATOM   1127 C  CB    . ARG A 1 196 ? -25.362 44.216  5.859   1.00 43.60 ? 306  ARG A CB    1 
ATOM   1128 C  CG    . ARG A 1 196 ? -25.714 45.576  6.453   1.00 48.22 ? 306  ARG A CG    1 
ATOM   1129 C  CD    . ARG A 1 196 ? -25.323 46.688  5.493   1.00 50.50 ? 306  ARG A CD    1 
ATOM   1130 N  NE    . ARG A 1 196 ? -26.073 46.581  4.246   1.00 53.98 ? 306  ARG A NE    1 
ATOM   1131 C  CZ    . ARG A 1 196 ? -25.798 47.264  3.140   1.00 56.53 ? 306  ARG A CZ    1 
ATOM   1132 N  NH1   . ARG A 1 196 ? -24.774 48.108  3.115   1.00 56.79 ? 306  ARG A NH1   1 
ATOM   1133 N  NH2   . ARG A 1 196 ? -26.549 47.098  2.057   1.00 57.72 ? 306  ARG A NH2   1 
ATOM   1134 N  N     A VAL A 1 197 ? -24.056 41.208  6.290   0.50 31.53 ? 307  VAL A N     1 
ATOM   1135 N  N     B VAL A 1 197 ? -24.071 41.195  6.344   0.50 30.84 ? 307  VAL A N     1 
ATOM   1136 C  CA    A VAL A 1 197 ? -23.570 40.053  5.543   0.50 27.68 ? 307  VAL A CA    1 
ATOM   1137 C  CA    B VAL A 1 197 ? -23.475 40.105  5.577   0.50 26.70 ? 307  VAL A CA    1 
ATOM   1138 C  C     A VAL A 1 197 ? -22.855 39.090  6.481   0.50 25.36 ? 307  VAL A C     1 
ATOM   1139 C  C     B VAL A 1 197 ? -22.877 39.077  6.532   0.50 25.10 ? 307  VAL A C     1 
ATOM   1140 O  O     A VAL A 1 197 ? -22.326 39.485  7.525   0.50 25.71 ? 307  VAL A O     1 
ATOM   1141 O  O     B VAL A 1 197 ? -22.447 39.412  7.640   0.50 25.88 ? 307  VAL A O     1 
ATOM   1142 C  CB    A VAL A 1 197 ? -22.632 40.464  4.383   0.50 27.70 ? 307  VAL A CB    1 
ATOM   1143 C  CB    B VAL A 1 197 ? -22.390 40.638  4.609   0.50 25.86 ? 307  VAL A CB    1 
ATOM   1144 C  CG1   A VAL A 1 197 ? -23.344 41.420  3.434   0.50 28.85 ? 307  VAL A CG1   1 
ATOM   1145 C  CG1   B VAL A 1 197 ? -22.140 39.661  3.471   0.50 23.45 ? 307  VAL A CG1   1 
ATOM   1146 C  CG2   A VAL A 1 197 ? -21.343 41.076  4.920   0.50 27.08 ? 307  VAL A CG2   1 
ATOM   1147 C  CG2   B VAL A 1 197 ? -22.774 42.012  4.077   0.50 27.50 ? 307  VAL A CG2   1 
ATOM   1148 N  N     . GLU A 1 198 ? -22.848 37.812  6.094   1.00 22.96 ? 308  GLU A N     1 
ATOM   1149 C  CA    . GLU A 1 198 ? -22.123 36.759  6.807   1.00 21.83 ? 308  GLU A CA    1 
ATOM   1150 C  C     . GLU A 1 198 ? -20.697 36.657  6.266   1.00 22.15 ? 308  GLU A C     1 
ATOM   1151 O  O     . GLU A 1 198 ? -20.466 36.828  5.067   1.00 22.66 ? 308  GLU A O     1 
ATOM   1152 C  CB    . GLU A 1 198 ? -22.830 35.402  6.661   1.00 22.57 ? 308  GLU A CB    1 
ATOM   1153 C  CG    . GLU A 1 198 ? -24.251 35.354  7.257   1.00 23.29 ? 308  GLU A CG    1 
ATOM   1154 C  CD    . GLU A 1 198 ? -24.247 35.160  8.764   1.00 23.95 ? 308  GLU A CD    1 
ATOM   1155 O  OE1   . GLU A 1 198 ? -24.149 33.996  9.210   1.00 23.29 ? 308  GLU A OE1   1 
ATOM   1156 O  OE2   . GLU A 1 198 ? -24.308 36.177  9.498   1.00 26.40 ? 308  GLU A OE2   1 
ATOM   1157 N  N     . VAL A 1 199 ? -19.743 36.364  7.156   1.00 21.70 ? 309  VAL A N     1 
ATOM   1158 C  CA    . VAL A 1 199 ? -18.313 36.390  6.831   1.00 21.81 ? 309  VAL A CA    1 
ATOM   1159 C  C     . VAL A 1 199 ? -17.701 35.014  7.117   1.00 21.14 ? 309  VAL A C     1 
ATOM   1160 O  O     . VAL A 1 199 ? -17.682 34.573  8.271   1.00 21.85 ? 309  VAL A O     1 
ATOM   1161 C  CB    . VAL A 1 199 ? -17.583 37.490  7.626   1.00 21.80 ? 309  VAL A CB    1 
ATOM   1162 C  CG1   . VAL A 1 199 ? -16.087 37.510  7.300   1.00 22.79 ? 309  VAL A CG1   1 
ATOM   1163 C  CG2   . VAL A 1 199 ? -18.242 38.867  7.361   1.00 24.57 ? 309  VAL A CG2   1 
ATOM   1164 N  N     . VAL A 1 200 ? -17.161 34.357  6.065   1.00 19.10 ? 310  VAL A N     1 
ATOM   1165 C  CA    . VAL A 1 200 ? -16.459 33.072  6.154   1.00 19.89 ? 310  VAL A CA    1 
ATOM   1166 C  C     . VAL A 1 200 ? -14.954 33.310  6.057   1.00 19.41 ? 310  VAL A C     1 
ATOM   1167 O  O     . VAL A 1 200 ? -14.506 34.166  5.284   1.00 20.00 ? 310  VAL A O     1 
ATOM   1168 C  CB    . VAL A 1 200 ? -16.923 32.138  5.018   1.00 18.38 ? 310  VAL A CB    1 
ATOM   1169 C  CG1   . VAL A 1 200 ? -16.139 30.826  5.009   1.00 20.01 ? 310  VAL A CG1   1 
ATOM   1170 C  CG2   . VAL A 1 200 ? -18.420 31.865  5.097   1.00 20.69 ? 310  VAL A CG2   1 
ATOM   1171 N  N     . GLY A 1 201 ? -14.168 32.534  6.804   1.00 18.55 ? 311  GLY A N     1 
ATOM   1172 C  CA    . GLY A 1 201 ? -12.715 32.567  6.678   1.00 17.79 ? 311  GLY A CA    1 
ATOM   1173 C  C     . GLY A 1 201 ? -12.117 31.196  6.421   1.00 18.40 ? 311  GLY A C     1 
ATOM   1174 O  O     . GLY A 1 201 ? -12.617 30.186  6.908   1.00 19.18 ? 311  GLY A O     1 
ATOM   1175 N  N     . GLY A 1 202 ? -11.021 31.174  5.651   1.00 17.62 ? 312  GLY A N     1 
ATOM   1176 C  CA    . GLY A 1 202 ? -10.323 29.921  5.326   1.00 15.88 ? 312  GLY A CA    1 
ATOM   1177 C  C     . GLY A 1 202 ? -9.069  30.225  4.522   1.00 15.01 ? 312  GLY A C     1 
ATOM   1178 O  O     . GLY A 1 202 ? -8.827  31.371  4.119   1.00 15.78 ? 312  GLY A O     1 
ATOM   1179 N  N     . ASN A 1 203 ? -8.259  29.183  4.281   1.00 15.29 ? 313  ASN A N     1 
ATOM   1180 C  CA    . ASN A 1 203 ? -8.492  27.785  4.716   1.00 14.13 ? 313  ASN A CA    1 
ATOM   1181 C  C     . ASN A 1 203 ? -7.570  27.375  5.870   1.00 16.04 ? 313  ASN A C     1 
ATOM   1182 O  O     . ASN A 1 203 ? -6.444  27.895  6.003   1.00 16.29 ? 313  ASN A O     1 
ATOM   1183 C  CB    . ASN A 1 203 ? -8.292  26.796  3.541   1.00 14.82 ? 313  ASN A CB    1 
ATOM   1184 C  CG    . ASN A 1 203 ? -9.496  26.741  2.609   1.00 15.48 ? 313  ASN A CG    1 
ATOM   1185 O  OD1   . ASN A 1 203 ? -10.405 27.562  2.727   1.00 15.52 ? 313  ASN A OD1   1 
ATOM   1186 N  ND2   . ASN A 1 203 ? -9.497  25.785  1.662   1.00 15.19 ? 313  ASN A ND2   1 
ATOM   1187 N  N     . VAL A 1 204 ? -8.035  26.421  6.687   1.00 15.46 ? 314  VAL A N     1 
ATOM   1188 C  CA    . VAL A 1 204 ? -7.284  25.902  7.829   1.00 15.63 ? 314  VAL A CA    1 
ATOM   1189 C  C     . VAL A 1 204 ? -7.283  24.375  7.793   1.00 16.70 ? 314  VAL A C     1 
ATOM   1190 O  O     . VAL A 1 204 ? -8.059  23.741  7.073   1.00 17.20 ? 314  VAL A O     1 
ATOM   1191 C  CB    . VAL A 1 204 ? -7.841  26.406  9.183   1.00 15.35 ? 314  VAL A CB    1 
ATOM   1192 C  CG1   . VAL A 1 204 ? -7.843  27.939  9.226   1.00 17.08 ? 314  VAL A CG1   1 
ATOM   1193 C  CG2   . VAL A 1 204 ? -9.237  25.828  9.465   1.00 17.43 ? 314  VAL A CG2   1 
ATOM   1194 N  N     . ALA A 1 205 ? -6.391  23.782  8.606   1.00 16.39 ? 315  ALA A N     1 
ATOM   1195 C  CA    . ALA A 1 205 ? -6.283  22.327  8.675   1.00 16.91 ? 315  ALA A CA    1 
ATOM   1196 C  C     . ALA A 1 205 ? -5.979  21.806  10.076  1.00 17.06 ? 315  ALA A C     1 
ATOM   1197 O  O     . ALA A 1 205 ? -5.667  20.607  10.213  1.00 18.32 ? 315  ALA A O     1 
ATOM   1198 C  CB    . ALA A 1 205 ? -5.206  21.807  7.708   1.00 19.94 ? 315  ALA A CB    1 
ATOM   1199 N  N     . THR A 1 206 ? -6.039  22.654  11.111  1.00 16.43 ? 316  THR A N     1 
ATOM   1200 C  CA    . THR A 1 206 ? -5.728  22.270  12.484  1.00 18.35 ? 316  THR A CA    1 
ATOM   1201 C  C     . THR A 1 206 ? -6.763  22.845  13.453  1.00 17.89 ? 316  THR A C     1 
ATOM   1202 O  O     . THR A 1 206 ? -7.495  23.794  13.141  1.00 16.75 ? 316  THR A O     1 
ATOM   1203 C  CB    . THR A 1 206 ? -4.332  22.753  12.915  1.00 17.74 ? 316  THR A CB    1 
ATOM   1204 O  OG1   . THR A 1 206 ? -4.352  24.184  12.997  1.00 17.99 ? 316  THR A OG1   1 
ATOM   1205 C  CG2   . THR A 1 206 ? -3.261  22.332  11.912  1.00 18.65 ? 316  THR A CG2   1 
ATOM   1206 N  N     . ARG A 1 207 ? -6.801  22.240  14.645  1.00 16.79 ? 317  ARG A N     1 
ATOM   1207 C  CA    . ARG A 1 207 ? -7.643  22.715  15.740  1.00 16.94 ? 317  ARG A CA    1 
ATOM   1208 C  C     . ARG A 1 207 ? -7.278  24.138  16.168  1.00 18.06 ? 317  ARG A C     1 
ATOM   1209 O  O     . ARG A 1 207 ? -8.165  24.976  16.365  1.00 18.50 ? 317  ARG A O     1 
ATOM   1210 C  CB    . ARG A 1 207 ? -7.535  21.745  16.925  1.00 19.53 ? 317  ARG A CB    1 
ATOM   1211 C  CG    . ARG A 1 207 ? -8.566  21.947  18.028  1.00 19.76 ? 317  ARG A CG    1 
ATOM   1212 C  CD    . ARG A 1 207 ? -8.307  21.030  19.260  1.00 19.52 ? 317  ARG A CD    1 
ATOM   1213 N  NE    . ARG A 1 207 ? -8.304  19.597  18.950  1.00 19.50 ? 317  ARG A NE    1 
ATOM   1214 C  CZ    . ARG A 1 207 ? -8.737  18.655  19.787  1.00 20.23 ? 317  ARG A CZ    1 
ATOM   1215 N  NH1   . ARG A 1 207 ? -9.219  18.990  20.988  1.00 22.20 ? 317  ARG A NH1   1 
ATOM   1216 N  NH2   . ARG A 1 207 ? -8.708  17.379  19.429  1.00 19.83 ? 317  ARG A NH2   1 
ATOM   1217 N  N     A SER A 1 208 ? -5.978  24.429  16.322  0.67 19.12 ? 318  SER A N     1 
ATOM   1218 N  N     B SER A 1 208 ? -5.981  24.431  16.313  0.33 18.91 ? 318  SER A N     1 
ATOM   1219 C  CA    A SER A 1 208 ? -5.572  25.761  16.770  0.67 19.81 ? 318  SER A CA    1 
ATOM   1220 C  CA    B SER A 1 208 ? -5.574  25.765  16.755  0.33 19.49 ? 318  SER A CA    1 
ATOM   1221 C  C     A SER A 1 208 ? -5.900  26.843  15.740  0.67 19.37 ? 318  SER A C     1 
ATOM   1222 C  C     B SER A 1 208 ? -5.949  26.835  15.735  0.33 18.98 ? 318  SER A C     1 
ATOM   1223 O  O     A SER A 1 208 ? -6.238  27.975  16.119  0.67 19.58 ? 318  SER A O     1 
ATOM   1224 O  O     B SER A 1 208 ? -6.358  27.943  16.107  0.33 18.99 ? 318  SER A O     1 
ATOM   1225 C  CB    A SER A 1 208 ? -4.076  25.782  17.107  0.67 20.41 ? 318  SER A CB    1 
ATOM   1226 C  CB    B SER A 1 208 ? -4.069  25.795  17.028  0.33 20.01 ? 318  SER A CB    1 
ATOM   1227 O  OG    A SER A 1 208 ? -3.262  25.421  16.002  0.67 21.41 ? 318  SER A OG    1 
ATOM   1228 O  OG    B SER A 1 208 ? -3.622  27.122  17.250  0.33 20.90 ? 318  SER A OG    1 
ATOM   1229 N  N     . ALA A 1 209 ? -5.806  26.530  14.443  1.00 17.68 ? 319  ALA A N     1 
ATOM   1230 C  CA    . ALA A 1 209 ? -6.138  27.521  13.415  1.00 16.88 ? 319  ALA A CA    1 
ATOM   1231 C  C     . ALA A 1 209 ? -7.642  27.773  13.357  1.00 17.00 ? 319  ALA A C     1 
ATOM   1232 O  O     . ALA A 1 209 ? -8.083  28.924  13.212  1.00 16.92 ? 319  ALA A O     1 
ATOM   1233 C  CB    . ALA A 1 209 ? -5.618  27.076  12.045  1.00 17.37 ? 319  ALA A CB    1 
ATOM   1234 N  N     . ALA A 1 210 ? -8.446  26.707  13.466  1.00 16.39 ? 320  ALA A N     1 
ATOM   1235 C  CA    . ALA A 1 210 ? -9.897  26.876  13.548  1.00 16.94 ? 320  ALA A CA    1 
ATOM   1236 C  C     . ALA A 1 210 ? -10.293 27.733  14.751  1.00 18.75 ? 320  ALA A C     1 
ATOM   1237 O  O     . ALA A 1 210 ? -11.159 28.616  14.638  1.00 19.01 ? 320  ALA A O     1 
ATOM   1238 C  CB    . ALA A 1 210 ? -10.590 25.508  13.610  1.00 16.84 ? 320  ALA A CB    1 
ATOM   1239 N  N     . ALA A 1 211 ? -9.679  27.482  15.916  1.00 19.70 ? 321  ALA A N     1 
ATOM   1240 C  CA    . ALA A 1 211 ? -9.989  28.263  17.115  1.00 19.54 ? 321  ALA A CA    1 
ATOM   1241 C  C     . ALA A 1 211 ? -9.676  29.746  16.925  1.00 20.34 ? 321  ALA A C     1 
ATOM   1242 O  O     . ALA A 1 211 ? -10.400 30.611  17.438  1.00 19.75 ? 321  ALA A O     1 
ATOM   1243 C  CB    . ALA A 1 211 ? -9.219  27.716  18.318  1.00 19.41 ? 321  ALA A CB    1 
ATOM   1244 N  N     . ALA A 1 212 ? -8.596  30.061  16.198  1.00 18.16 ? 322  ALA A N     1 
ATOM   1245 C  CA    . ALA A 1 212 ? -8.238  31.460  15.968  1.00 19.19 ? 322  ALA A CA    1 
ATOM   1246 C  C     . ALA A 1 212 ? -9.278  32.171  15.104  1.00 20.05 ? 322  ALA A C     1 
ATOM   1247 O  O     . ALA A 1 212 ? -9.588  33.349  15.342  1.00 21.14 ? 322  ALA A O     1 
ATOM   1248 C  CB    . ALA A 1 212 ? -6.843  31.548  15.336  1.00 18.64 ? 322  ALA A CB    1 
ATOM   1249 N  N     . LEU A 1 213 ? -9.830  31.480  14.095  1.00 18.66 ? 323  LEU A N     1 
ATOM   1250 C  CA    . LEU A 1 213 ? -10.884 32.078  13.274  1.00 19.51 ? 323  LEU A CA    1 
ATOM   1251 C  C     . LEU A 1 213 ? -12.175 32.264  14.070  1.00 20.57 ? 323  LEU A C     1 
ATOM   1252 O  O     . LEU A 1 213 ? -12.870 33.275  13.903  1.00 19.74 ? 323  LEU A O     1 
ATOM   1253 C  CB    . LEU A 1 213 ? -11.139 31.236  12.018  1.00 17.65 ? 323  LEU A CB    1 
ATOM   1254 C  CG    . LEU A 1 213 ? -10.210 31.484  10.823  1.00 18.36 ? 323  LEU A CG    1 
ATOM   1255 C  CD1   . LEU A 1 213 ? -10.416 30.452  9.704   1.00 18.03 ? 323  LEU A CD1   1 
ATOM   1256 C  CD2   . LEU A 1 213 ? -10.389 32.913  10.294  1.00 19.49 ? 323  LEU A CD2   1 
ATOM   1257 N  N     . VAL A 1 214 ? -12.518 31.303  14.937  1.00 20.46 ? 324  VAL A N     1 
ATOM   1258 C  CA    . VAL A 1 214 ? -13.672 31.469  15.827  1.00 20.21 ? 324  VAL A CA    1 
ATOM   1259 C  C     . VAL A 1 214 ? -13.517 32.731  16.675  1.00 21.22 ? 324  VAL A C     1 
ATOM   1260 O  O     . VAL A 1 214 ? -14.457 33.530  16.820  1.00 22.25 ? 324  VAL A O     1 
ATOM   1261 C  CB    . VAL A 1 214 ? -13.852 30.217  16.710  1.00 19.70 ? 324  VAL A CB    1 
ATOM   1262 C  CG1   . VAL A 1 214 ? -14.903 30.478  17.796  1.00 21.43 ? 324  VAL A CG1   1 
ATOM   1263 C  CG2   . VAL A 1 214 ? -14.223 28.988  15.864  1.00 20.31 ? 324  VAL A CG2   1 
ATOM   1264 N  N     . ASP A 1 215 ? -12.335 32.913  17.278  1.00 21.66 ? 325  ASP A N     1 
ATOM   1265 C  CA    . ASP A 1 215 ? -12.112 34.077  18.137  1.00 24.76 ? 325  ASP A CA    1 
ATOM   1266 C  C     . ASP A 1 215 ? -12.138 35.380  17.348  1.00 25.02 ? 325  ASP A C     1 
ATOM   1267 O  O     . ASP A 1 215 ? -12.464 36.435  17.906  1.00 25.81 ? 325  ASP A O     1 
ATOM   1268 C  CB    . ASP A 1 215 ? -10.791 33.926  18.892  1.00 27.46 ? 325  ASP A CB    1 
ATOM   1269 C  CG    . ASP A 1 215 ? -10.862 32.868  19.980  1.00 33.87 ? 325  ASP A CG    1 
ATOM   1270 O  OD1   . ASP A 1 215 ? -11.989 32.429  20.310  1.00 36.46 ? 325  ASP A OD1   1 
ATOM   1271 O  OD2   . ASP A 1 215 ? -9.793  32.470  20.492  1.00 38.19 ? 325  ASP A OD2   1 
ATOM   1272 N  N     . ALA A 1 216 ? -11.821 35.337  16.055  1.00 25.61 ? 326  ALA A N     1 
ATOM   1273 C  CA    . ALA A 1 216 ? -11.873 36.551  15.244  1.00 24.10 ? 326  ALA A CA    1 
ATOM   1274 C  C     . ALA A 1 216 ? -13.289 36.917  14.809  1.00 24.26 ? 326  ALA A C     1 
ATOM   1275 O  O     . ALA A 1 216 ? -13.491 38.021  14.287  1.00 25.46 ? 326  ALA A O     1 
ATOM   1276 C  CB    . ALA A 1 216 ? -10.978 36.406  14.010  1.00 23.41 ? 326  ALA A CB    1 
ATOM   1277 N  N     . GLY A 1 217 ? -14.259 36.028  15.006  1.00 22.23 ? 327  GLY A N     1 
ATOM   1278 C  CA    . GLY A 1 217 ? -15.651 36.305  14.710  1.00 22.01 ? 327  GLY A CA    1 
ATOM   1279 C  C     . GLY A 1 217 ? -16.210 35.658  13.458  1.00 21.83 ? 327  GLY A C     1 
ATOM   1280 O  O     . GLY A 1 217 ? -17.265 36.096  12.974  1.00 23.72 ? 327  GLY A O     1 
ATOM   1281 N  N     . ALA A 1 218 ? -15.549 34.637  12.922  1.00 19.73 ? 328  ALA A N     1 
ATOM   1282 C  CA    . ALA A 1 218 ? -16.014 33.998  11.697  1.00 19.06 ? 328  ALA A CA    1 
ATOM   1283 C  C     . ALA A 1 218 ? -17.409 33.407  11.881  1.00 19.99 ? 328  ALA A C     1 
ATOM   1284 O  O     . ALA A 1 218 ? -17.716 32.824  12.923  1.00 22.25 ? 328  ALA A O     1 
ATOM   1285 C  CB    . ALA A 1 218 ? -15.039 32.890  11.287  1.00 18.81 ? 328  ALA A CB    1 
ATOM   1286 N  N     . ASP A 1 219 ? -18.247 33.526  10.838  1.00 17.90 ? 329  ASP A N     1 
ATOM   1287 C  CA    . ASP A 1 219 ? -19.575 32.914  10.840  1.00 18.89 ? 329  ASP A CA    1 
ATOM   1288 C  C     . ASP A 1 219 ? -19.564 31.471  10.332  1.00 18.85 ? 329  ASP A C     1 
ATOM   1289 O  O     . ASP A 1 219 ? -20.568 30.757  10.506  1.00 19.37 ? 329  ASP A O     1 
ATOM   1290 C  CB    . ASP A 1 219 ? -20.553 33.751  9.996   1.00 21.04 ? 329  ASP A CB    1 
ATOM   1291 C  CG    . ASP A 1 219 ? -20.828 35.128  10.602  1.00 22.31 ? 329  ASP A CG    1 
ATOM   1292 O  OD1   . ASP A 1 219 ? -21.106 35.229  11.823  1.00 22.35 ? 329  ASP A OD1   1 
ATOM   1293 O  OD2   . ASP A 1 219 ? -20.765 36.124  9.850   1.00 23.70 ? 329  ASP A OD2   1 
ATOM   1294 N  N     . ALA A 1 220 ? -18.459 31.032  9.728   1.00 18.31 ? 330  ALA A N     1 
ATOM   1295 C  CA    . ALA A 1 220 ? -18.174 29.663  9.301   1.00 17.60 ? 330  ALA A CA    1 
ATOM   1296 C  C     . ALA A 1 220 ? -16.677 29.563  9.038   1.00 16.88 ? 330  ALA A C     1 
ATOM   1297 O  O     . ALA A 1 220 ? -16.039 30.568  8.700   1.00 19.37 ? 330  ALA A O     1 
ATOM   1298 C  CB    . ALA A 1 220 ? -18.948 29.282  8.034   1.00 16.88 ? 330  ALA A CB    1 
ATOM   1299 N  N     . VAL A 1 221 ? -16.131 28.345  9.154   1.00 16.73 ? 331  VAL A N     1 
ATOM   1300 C  CA    . VAL A 1 221 ? -14.699 28.067  9.000   1.00 17.05 ? 331  VAL A CA    1 
ATOM   1301 C  C     . VAL A 1 221 ? -14.516 27.037  7.889   1.00 16.54 ? 331  VAL A C     1 
ATOM   1302 O  O     . VAL A 1 221 ? -15.124 25.960  7.933   1.00 17.91 ? 331  VAL A O     1 
ATOM   1303 C  CB    . VAL A 1 221 ? -14.075 27.567  10.321  1.00 15.42 ? 331  VAL A CB    1 
ATOM   1304 C  CG1   . VAL A 1 221 ? -12.654 27.027  10.110  1.00 16.44 ? 331  VAL A CG1   1 
ATOM   1305 C  CG2   . VAL A 1 221 ? -14.069 28.680  11.368  1.00 17.18 ? 331  VAL A CG2   1 
ATOM   1306 N  N     . LYS A 1 222 ? -13.671 27.356  6.902   1.00 16.27 ? 332  LYS A N     1 
ATOM   1307 C  CA    . LYS A 1 222 ? -13.456 26.487  5.740   1.00 15.54 ? 332  LYS A CA    1 
ATOM   1308 C  C     . LYS A 1 222 ? -12.144 25.708  5.875   1.00 15.21 ? 332  LYS A C     1 
ATOM   1309 O  O     . LYS A 1 222 ? -11.079 26.302  6.095   1.00 16.53 ? 332  LYS A O     1 
ATOM   1310 C  CB    . LYS A 1 222 ? -13.471 27.303  4.441   1.00 15.36 ? 332  LYS A CB    1 
ATOM   1311 C  CG    . LYS A 1 222 ? -13.564 26.457  3.153   1.00 15.16 ? 332  LYS A CG    1 
ATOM   1312 C  CD    . LYS A 1 222 ? -14.388 27.121  2.027   1.00 15.85 ? 332  LYS A CD    1 
ATOM   1313 C  CE    . LYS A 1 222 ? -13.724 28.372  1.417   1.00 15.57 ? 332  LYS A CE    1 
ATOM   1314 N  NZ    . LYS A 1 222 ? -12.429 28.106  0.702   1.00 14.95 ? 332  LYS A NZ    1 
ATOM   1315 N  N     . VAL A 1 223 ? -12.222 24.381  5.713   1.00 13.61 ? 333  VAL A N     1 
ATOM   1316 C  CA    . VAL A 1 223 ? -11.132 23.448  6.020   1.00 15.74 ? 333  VAL A CA    1 
ATOM   1317 C  C     . VAL A 1 223 ? -10.599 22.814  4.736   1.00 15.07 ? 333  VAL A C     1 
ATOM   1318 O  O     . VAL A 1 223 ? -11.369 22.237  3.952   1.00 16.50 ? 333  VAL A O     1 
ATOM   1319 C  CB    . VAL A 1 223 ? -11.621 22.356  6.993   1.00 15.40 ? 333  VAL A CB    1 
ATOM   1320 C  CG1   . VAL A 1 223 ? -10.559 21.255  7.171   1.00 15.99 ? 333  VAL A CG1   1 
ATOM   1321 C  CG2   . VAL A 1 223 ? -12.023 22.967  8.338   1.00 16.28 ? 333  VAL A CG2   1 
ATOM   1322 N  N     . GLY A 1 224 ? -9.273  22.870  4.547   1.00 13.84 ? 334  GLY A N     1 
ATOM   1323 C  CA    . GLY A 1 224 ? -8.594  22.237  3.420   1.00 15.56 ? 334  GLY A CA    1 
ATOM   1324 C  C     . GLY A 1 224 ? -7.268  22.895  3.058   1.00 15.66 ? 334  GLY A C     1 
ATOM   1325 O  O     . GLY A 1 224 ? -7.264  23.934  2.390   1.00 16.42 ? 334  GLY A O     1 
ATOM   1326 N  N     . VAL A 1 225 ? -6.132  22.327  3.488   1.00 16.01 ? 335  VAL A N     1 
ATOM   1327 C  CA    . VAL A 1 225 ? -4.809  22.810  3.068   1.00 17.11 ? 335  VAL A CA    1 
ATOM   1328 C  C     . VAL A 1 225 ? -4.143  21.636  2.355   1.00 19.44 ? 335  VAL A C     1 
ATOM   1329 O  O     . VAL A 1 225 ? -3.724  20.667  2.999   1.00 20.17 ? 335  VAL A O     1 
ATOM   1330 C  CB    . VAL A 1 225 ? -3.954  23.327  4.240   1.00 16.87 ? 335  VAL A CB    1 
ATOM   1331 C  CG1   . VAL A 1 225 ? -2.572  23.812  3.742   1.00 17.67 ? 335  VAL A CG1   1 
ATOM   1332 C  CG2   . VAL A 1 225 ? -4.645  24.488  4.966   1.00 17.66 ? 335  VAL A CG2   1 
ATOM   1333 N  N     . GLY A 1 226 ? -4.114  21.677  1.017   1.00 20.02 ? 336  GLY A N     1 
ATOM   1334 C  CA    . GLY A 1 226 ? -3.465  20.644  0.232   1.00 22.31 ? 336  GLY A CA    1 
ATOM   1335 C  C     . GLY A 1 226 ? -4.279  19.548  -0.466  1.00 22.84 ? 336  GLY A C     1 
ATOM   1336 O  O     . GLY A 1 226 ? -3.721  18.826  -1.300  1.00 23.22 ? 336  GLY A O     1 
ATOM   1337 N  N     . PRO A 1 227 ? -5.577  19.375  -0.170  1.00 20.66 ? 337  PRO A N     1 
ATOM   1338 C  CA    . PRO A 1 227 ? -6.288  18.183  -0.674  1.00 20.80 ? 337  PRO A CA    1 
ATOM   1339 C  C     . PRO A 1 227 ? -6.876  18.259  -2.081  1.00 21.76 ? 337  PRO A C     1 
ATOM   1340 O  O     . PRO A 1 227 ? -7.320  17.217  -2.587  1.00 21.63 ? 337  PRO A O     1 
ATOM   1341 C  CB    . PRO A 1 227 ? -7.425  18.019  0.349   1.00 21.23 ? 337  PRO A CB    1 
ATOM   1342 C  CG    . PRO A 1 227 ? -7.795  19.421  0.656   1.00 20.86 ? 337  PRO A CG    1 
ATOM   1343 C  CD    . PRO A 1 227 ? -6.461  20.195  0.679   1.00 21.67 ? 337  PRO A CD    1 
ATOM   1344 N  N     . GLY A 1 228 ? -6.903  19.432  -2.718  1.00 20.67 ? 338  GLY A N     1 
ATOM   1345 C  CA    . GLY A 1 228 ? -7.620  19.580  -3.978  1.00 21.40 ? 338  GLY A CA    1 
ATOM   1346 C  C     . GLY A 1 228 ? -7.045  18.749  -5.113  1.00 21.54 ? 338  GLY A C     1 
ATOM   1347 O  O     . GLY A 1 228 ? -5.846  18.462  -5.176  1.00 22.57 ? 338  GLY A O     1 
ATOM   1348 N  N     . SER A 1 229 ? -7.930  18.372  -6.047  1.00 20.11 ? 339  SER A N     1 
ATOM   1349 C  CA    . SER A 1 229 ? -7.536  17.512  -7.164  1.00 20.89 ? 339  SER A CA    1 
ATOM   1350 C  C     . SER A 1 229 ? -6.476  18.153  -8.057  1.00 21.36 ? 339  SER A C     1 
ATOM   1351 O  O     . SER A 1 229 ? -5.669  17.436  -8.666  1.00 23.28 ? 339  SER A O     1 
ATOM   1352 C  CB    . SER A 1 229 ? -8.764  17.139  -8.003  1.00 21.92 ? 339  SER A CB    1 
ATOM   1353 O  OG    . SER A 1 229 ? -9.278  18.275  -8.683  1.00 22.71 ? 339  SER A OG    1 
ATOM   1354 N  N     . ILE A 1 230 ? -6.471  19.485  -8.168  1.00 19.82 ? 340  ILE A N     1 
ATOM   1355 C  CA    . ILE A 1 230 ? -5.512  20.204  -9.003  1.00 22.38 ? 340  ILE A CA    1 
ATOM   1356 C  C     . ILE A 1 230 ? -4.380  20.815  -8.177  1.00 22.62 ? 340  ILE A C     1 
ATOM   1357 O  O     . ILE A 1 230 ? -3.623  21.651  -8.690  1.00 25.53 ? 340  ILE A O     1 
ATOM   1358 C  CB    . ILE A 1 230 ? -6.206  21.278  -9.868  1.00 21.46 ? 340  ILE A CB    1 
ATOM   1359 C  CG1   . ILE A 1 230 ? -7.300  22.029  -9.085  1.00 19.55 ? 340  ILE A CG1   1 
ATOM   1360 C  CG2   . ILE A 1 230 ? -6.812  20.656  -11.133 1.00 22.86 ? 340  ILE A CG2   1 
ATOM   1361 C  CD1   . ILE A 1 230 ? -6.805  22.781  -7.832  1.00 22.13 ? 340  ILE A CD1   1 
ATOM   1362 N  N     . CYS A 1 231 ? -4.230  20.405  -6.916  1.00 21.31 ? 341  CYS A N     1 
ATOM   1363 C  CA    . CYS A 1 231 ? -3.252  21.015  -6.016  1.00 23.03 ? 341  CYS A CA    1 
ATOM   1364 C  C     . CYS A 1 231 ? -1.881  20.357  -6.152  1.00 22.37 ? 341  CYS A C     1 
ATOM   1365 O  O     . CYS A 1 231 ? -1.776  19.134  -6.297  1.00 23.91 ? 341  CYS A O     1 
ATOM   1366 C  CB    . CYS A 1 231 ? -3.742  20.924  -4.565  1.00 28.38 ? 341  CYS A CB    1 
ATOM   1367 S  SG    . CYS A 1 231 ? -2.577  21.493  -3.284  1.00 31.21 ? 341  CYS A SG    1 
ATOM   1368 N  N     . THR A 1 232 ? -0.827  21.184  -6.118  1.00 19.42 ? 342  THR A N     1 
ATOM   1369 C  CA    . THR A 1 232 ? 0.540   20.684  -6.001  1.00 19.03 ? 342  THR A CA    1 
ATOM   1370 C  C     . THR A 1 232 ? 1.271   21.210  -4.767  1.00 18.37 ? 342  THR A C     1 
ATOM   1371 O  O     . THR A 1 232 ? 2.476   20.984  -4.646  1.00 18.82 ? 342  THR A O     1 
ATOM   1372 C  CB    . THR A 1 232 ? 1.362   21.009  -7.253  1.00 21.52 ? 342  THR A CB    1 
ATOM   1373 O  OG1   . THR A 1 232 ? 1.438   22.428  -7.429  1.00 20.57 ? 342  THR A OG1   1 
ATOM   1374 C  CG2   . THR A 1 232 ? 0.734   20.374  -8.494  1.00 23.41 ? 342  THR A CG2   1 
ATOM   1375 N  N     . THR A 1 233 ? 0.580   21.898  -3.851  1.00 18.24 ? 343  THR A N     1 
ATOM   1376 C  CA    . THR A 1 233 ? 1.179   22.320  -2.579  1.00 17.42 ? 343  THR A CA    1 
ATOM   1377 C  C     . THR A 1 233 ? 1.906   21.171  -1.869  1.00 17.33 ? 343  THR A C     1 
ATOM   1378 O  O     . THR A 1 233 ? 2.977   21.370  -1.270  1.00 16.95 ? 343  THR A O     1 
ATOM   1379 C  CB    . THR A 1 233 ? 0.077   22.896  -1.669  1.00 16.53 ? 343  THR A CB    1 
ATOM   1380 O  OG1   . THR A 1 233 ? -0.528  24.032  -2.295  1.00 18.15 ? 343  THR A OG1   1 
ATOM   1381 C  CG2   . THR A 1 233 ? 0.623   23.308  -0.304  1.00 17.19 ? 343  THR A CG2   1 
ATOM   1382 N  N     . ARG A 1 234 ? 1.331   19.961  -1.901  1.00 17.69 ? 344  ARG A N     1 
ATOM   1383 C  CA    . ARG A 1 234 ? 1.924   18.846  -1.160  1.00 18.72 ? 344  ARG A CA    1 
ATOM   1384 C  C     . ARG A 1 234 ? 3.298   18.451  -1.696  1.00 19.19 ? 344  ARG A C     1 
ATOM   1385 O  O     . ARG A 1 234 ? 4.146   17.986  -0.925  1.00 21.31 ? 344  ARG A O     1 
ATOM   1386 C  CB    . ARG A 1 234 ? 0.979   17.635  -1.171  1.00 22.59 ? 344  ARG A CB    1 
ATOM   1387 C  CG    . ARG A 1 234 ? -0.428  17.943  -0.670  1.00 31.74 ? 344  ARG A CG    1 
ATOM   1388 C  CD    . ARG A 1 234 ? -0.705  17.353  0.713   1.00 39.72 ? 344  ARG A CD    1 
ATOM   1389 N  NE    . ARG A 1 234 ? -1.714  16.288  0.726   1.00 43.57 ? 344  ARG A NE    1 
ATOM   1390 C  CZ    . ARG A 1 234 ? -2.916  16.384  1.302   1.00 46.96 ? 344  ARG A CZ    1 
ATOM   1391 N  NH1   . ARG A 1 234 ? -3.753  15.355  1.269   1.00 46.71 ? 344  ARG A NH1   1 
ATOM   1392 N  NH2   . ARG A 1 234 ? -3.291  17.510  1.907   1.00 48.31 ? 344  ARG A NH2   1 
ATOM   1393 N  N     A VAL A 1 235 ? 3.551   18.614  -2.997  0.62 18.92 ? 345  VAL A N     1 
ATOM   1394 N  N     B VAL A 1 235 ? 3.540   18.643  -2.993  0.38 20.48 ? 345  VAL A N     1 
ATOM   1395 C  CA    A VAL A 1 235 ? 4.877   18.269  -3.517  0.62 19.69 ? 345  VAL A CA    1 
ATOM   1396 C  CA    B VAL A 1 235 ? 4.814   18.277  -3.608  0.38 21.58 ? 345  VAL A CA    1 
ATOM   1397 C  C     A VAL A 1 235 ? 5.784   19.491  -3.656  0.62 19.48 ? 345  VAL A C     1 
ATOM   1398 C  C     B VAL A 1 235 ? 5.759   19.474  -3.701  0.38 20.27 ? 345  VAL A C     1 
ATOM   1399 O  O     A VAL A 1 235 ? 7.009   19.364  -3.546  0.62 22.00 ? 345  VAL A O     1 
ATOM   1400 O  O     B VAL A 1 235 ? 6.980   19.314  -3.592  0.38 21.51 ? 345  VAL A O     1 
ATOM   1401 C  CB    A VAL A 1 235 ? 4.789   17.511  -4.856  0.62 20.18 ? 345  VAL A CB    1 
ATOM   1402 C  CB    B VAL A 1 235 ? 4.585   17.649  -4.995  0.38 23.50 ? 345  VAL A CB    1 
ATOM   1403 C  CG1   A VAL A 1 235 ? 4.114   16.160  -4.656  0.62 21.54 ? 345  VAL A CG1   1 
ATOM   1404 C  CG1   B VAL A 1 235 ? 5.818   17.804  -5.855  0.38 24.69 ? 345  VAL A CG1   1 
ATOM   1405 C  CG2   A VAL A 1 235 ? 4.059   18.333  -5.890  0.62 18.97 ? 345  VAL A CG2   1 
ATOM   1406 C  CG2   B VAL A 1 235 ? 4.226   16.176  -4.846  0.38 24.43 ? 345  VAL A CG2   1 
ATOM   1407 N  N     . VAL A 1 236 ? 5.206   20.675  -3.900  1.00 19.23 ? 346  VAL A N     1 
ATOM   1408 C  CA    . VAL A 1 236 ? 6.020   21.887  -4.063  1.00 18.58 ? 346  VAL A CA    1 
ATOM   1409 C  C     . VAL A 1 236 ? 6.533   22.394  -2.714  1.00 17.35 ? 346  VAL A C     1 
ATOM   1410 O  O     . VAL A 1 236 ? 7.708   22.759  -2.571  1.00 17.37 ? 346  VAL A O     1 
ATOM   1411 C  CB    . VAL A 1 236 ? 5.202   22.976  -4.798  1.00 19.94 ? 346  VAL A CB    1 
ATOM   1412 C  CG1   . VAL A 1 236 ? 5.884   24.342  -4.692  1.00 21.76 ? 346  VAL A CG1   1 
ATOM   1413 C  CG2   . VAL A 1 236 ? 4.985   22.607  -6.266  1.00 22.43 ? 346  VAL A CG2   1 
ATOM   1414 N  N     . ALA A 1 237 ? 5.655   22.448  -1.709  1.00 16.67 ? 347  ALA A N     1 
ATOM   1415 C  CA    . ALA A 1 237 ? 6.025   22.906  -0.378  1.00 17.21 ? 347  ALA A CA    1 
ATOM   1416 C  C     . ALA A 1 237 ? 6.230   21.773  0.625   1.00 17.81 ? 347  ALA A C     1 
ATOM   1417 O  O     . ALA A 1 237 ? 6.847   22.006  1.673   1.00 17.82 ? 347  ALA A O     1 
ATOM   1418 C  CB    . ALA A 1 237 ? 4.956   23.867  0.162   1.00 16.57 ? 347  ALA A CB    1 
ATOM   1419 N  N     . GLY A 1 238 ? 5.720   20.568  0.345   1.00 16.70 ? 348  GLY A N     1 
ATOM   1420 C  CA    . GLY A 1 238 ? 5.765   19.487  1.322   1.00 16.41 ? 348  GLY A CA    1 
ATOM   1421 C  C     . GLY A 1 238 ? 4.805   19.633  2.493   1.00 15.64 ? 348  GLY A C     1 
ATOM   1422 O  O     . GLY A 1 238 ? 5.019   19.007  3.541   1.00 15.80 ? 348  GLY A O     1 
ATOM   1423 N  N     . VAL A 1 239 ? 3.746   20.437  2.331   1.00 16.07 ? 349  VAL A N     1 
ATOM   1424 C  CA    . VAL A 1 239 ? 2.830   20.856  3.392   1.00 15.34 ? 349  VAL A CA    1 
ATOM   1425 C  C     . VAL A 1 239 ? 1.438   20.308  3.098   1.00 18.07 ? 349  VAL A C     1 
ATOM   1426 O  O     . VAL A 1 239 ? 0.994   20.337  1.944   1.00 19.54 ? 349  VAL A O     1 
ATOM   1427 C  CB    . VAL A 1 239 ? 2.780   22.397  3.501   1.00 15.71 ? 349  VAL A CB    1 
ATOM   1428 C  CG1   . VAL A 1 239 ? 1.642   22.832  4.431   1.00 15.98 ? 349  VAL A CG1   1 
ATOM   1429 C  CG2   . VAL A 1 239 ? 4.119   22.957  3.989   1.00 16.49 ? 349  VAL A CG2   1 
ATOM   1430 N  N     . GLY A 1 240 ? 0.751   19.821  4.131   1.00 17.20 ? 350  GLY A N     1 
ATOM   1431 C  CA    . GLY A 1 240 ? -0.640  19.426  3.976   1.00 17.40 ? 350  GLY A CA    1 
ATOM   1432 C  C     . GLY A 1 240 ? -1.173  18.694  5.194   1.00 17.30 ? 350  GLY A C     1 
ATOM   1433 O  O     . GLY A 1 240 ? -0.492  18.537  6.214   1.00 18.93 ? 350  GLY A O     1 
ATOM   1434 N  N     . ALA A 1 241 ? -2.425  18.246  5.066   1.00 17.59 ? 351  ALA A N     1 
ATOM   1435 C  CA    . ALA A 1 241 ? -3.102  17.507  6.129   1.00 15.89 ? 351  ALA A CA    1 
ATOM   1436 C  C     . ALA A 1 241 ? -4.243  16.664  5.560   1.00 16.79 ? 351  ALA A C     1 
ATOM   1437 O  O     . ALA A 1 241 ? -5.209  17.222  5.026   1.00 17.70 ? 351  ALA A O     1 
ATOM   1438 C  CB    . ALA A 1 241 ? -3.636  18.471  7.189   1.00 18.85 ? 351  ALA A CB    1 
ATOM   1439 N  N     . PRO A 1 242 ? -4.177  15.332  5.658   1.00 15.92 ? 352  PRO A N     1 
ATOM   1440 C  CA    . PRO A 1 242 ? -5.291  14.493  5.180   1.00 15.94 ? 352  PRO A CA    1 
ATOM   1441 C  C     . PRO A 1 242 ? -6.646  14.966  5.731   1.00 15.57 ? 352  PRO A C     1 
ATOM   1442 O  O     . PRO A 1 242 ? -6.781  15.279  6.914   1.00 15.80 ? 352  PRO A O     1 
ATOM   1443 C  CB    . PRO A 1 242 ? -4.902  13.095  5.681   1.00 16.11 ? 352  PRO A CB    1 
ATOM   1444 C  CG    . PRO A 1 242 ? -3.359  13.119  5.635   1.00 16.05 ? 352  PRO A CG    1 
ATOM   1445 C  CD    . PRO A 1 242 ? -3.039  14.526  6.152   1.00 16.01 ? 352  PRO A CD    1 
ATOM   1446 N  N     A GLN A 1 243 ? -7.665  14.982  4.858   0.70 14.46 ? 353  GLN A N     1 
ATOM   1447 N  N     B GLN A 1 243 ? -7.661  14.970  4.858   0.30 15.25 ? 353  GLN A N     1 
ATOM   1448 C  CA    A GLN A 1 243 ? -8.867  15.790  5.089   0.70 14.86 ? 353  GLN A CA    1 
ATOM   1449 C  CA    B GLN A 1 243 ? -8.868  15.761  5.103   0.30 15.48 ? 353  GLN A CA    1 
ATOM   1450 C  C     A GLN A 1 243 ? -9.828  15.230  6.152   0.70 15.07 ? 353  GLN A C     1 
ATOM   1451 C  C     B GLN A 1 243 ? -9.711  15.227  6.263   0.30 15.80 ? 353  GLN A C     1 
ATOM   1452 O  O     A GLN A 1 243 ? -10.539 16.017  6.791   0.70 16.17 ? 353  GLN A O     1 
ATOM   1453 O  O     B GLN A 1 243 ? -10.230 16.017  7.062   0.30 16.86 ? 353  GLN A O     1 
ATOM   1454 C  CB    A GLN A 1 243 ? -9.604  15.984  3.761   0.70 18.05 ? 353  GLN A CB    1 
ATOM   1455 C  CB    B GLN A 1 243 ? -9.709  15.840  3.829   0.30 16.50 ? 353  GLN A CB    1 
ATOM   1456 C  CG    A GLN A 1 243 ? -10.733 17.006  3.784   0.70 18.89 ? 353  GLN A CG    1 
ATOM   1457 C  CG    B GLN A 1 243 ? -9.460  17.090  2.994   0.30 15.63 ? 353  GLN A CG    1 
ATOM   1458 C  CD    A GLN A 1 243 ? -10.246 18.460  3.737   0.70 19.06 ? 353  GLN A CD    1 
ATOM   1459 C  CD    B GLN A 1 243 ? -10.060 18.349  3.618   0.30 15.92 ? 353  GLN A CD    1 
ATOM   1460 O  OE1   A GLN A 1 243 ? -9.230  18.806  4.340   0.70 18.68 ? 353  GLN A OE1   1 
ATOM   1461 O  OE1   B GLN A 1 243 ? -9.596  18.833  4.653   0.30 15.79 ? 353  GLN A OE1   1 
ATOM   1462 N  NE2   A GLN A 1 243 ? -10.992 19.318  3.037   0.70 20.49 ? 353  GLN A NE2   1 
ATOM   1463 N  NE2   B GLN A 1 243 ? -11.107 18.875  2.990   0.30 17.55 ? 353  GLN A NE2   1 
ATOM   1464 N  N     . ILE A 1 244 ? -9.902  13.907  6.365   1.00 15.53 ? 354  ILE A N     1 
ATOM   1465 C  CA    . ILE A 1 244 ? -10.769 13.396  7.441   1.00 14.96 ? 354  ILE A CA    1 
ATOM   1466 C  C     . ILE A 1 244 ? -10.229 13.825  8.810   1.00 15.82 ? 354  ILE A C     1 
ATOM   1467 O  O     . ILE A 1 244 ? -10.969 14.352  9.658   1.00 16.88 ? 354  ILE A O     1 
ATOM   1468 C  CB    . ILE A 1 244 ? -10.965 11.866  7.338   1.00 15.52 ? 354  ILE A CB    1 
ATOM   1469 C  CG1   . ILE A 1 244 ? -11.935 11.525  6.195   1.00 16.41 ? 354  ILE A CG1   1 
ATOM   1470 C  CG2   . ILE A 1 244 ? -11.518 11.277  8.647   1.00 16.81 ? 354  ILE A CG2   1 
ATOM   1471 C  CD1   . ILE A 1 244 ? -13.417 11.932  6.454   1.00 16.20 ? 354  ILE A CD1   1 
ATOM   1472 N  N     . THR A 1 245 ? -8.919  13.662  9.031   1.00 15.51 ? 355  THR A N     1 
ATOM   1473 C  CA    . THR A 1 245 ? -8.316  14.134  10.278  1.00 15.66 ? 355  THR A CA    1 
ATOM   1474 C  C     . THR A 1 245 ? -8.404  15.666  10.421  1.00 17.28 ? 355  THR A C     1 
ATOM   1475 O  O     . THR A 1 245 ? -8.661  16.177  11.521  1.00 17.06 ? 355  THR A O     1 
ATOM   1476 C  CB    . THR A 1 245 ? -6.871  13.640  10.342  1.00 16.64 ? 355  THR A CB    1 
ATOM   1477 O  OG1   . THR A 1 245 ? -6.872  12.205  10.423  1.00 16.06 ? 355  THR A OG1   1 
ATOM   1478 C  CG2   . THR A 1 245 ? -6.137  14.214  11.563  1.00 18.32 ? 355  THR A CG2   1 
ATOM   1479 N  N     . ALA A 1 246 ? -8.193  16.416  9.328   1.00 14.53 ? 356  ALA A N     1 
ATOM   1480 C  CA    . ALA A 1 246 ? -8.316  17.877  9.388   1.00 15.04 ? 356  ALA A CA    1 
ATOM   1481 C  C     . ALA A 1 246 ? -9.723  18.315  9.818   1.00 16.86 ? 356  ALA A C     1 
ATOM   1482 O  O     . ALA A 1 246 ? -9.871  19.251  10.618  1.00 18.11 ? 356  ALA A O     1 
ATOM   1483 C  CB    . ALA A 1 246 ? -7.948  18.495  8.033   1.00 13.62 ? 356  ALA A CB    1 
ATOM   1484 N  N     . ILE A 1 247 ? -10.766 17.652  9.299   1.00 16.33 ? 357  ILE A N     1 
ATOM   1485 C  CA    . ILE A 1 247 ? -12.141 17.991  9.674   1.00 15.40 ? 357  ILE A CA    1 
ATOM   1486 C  C     . ILE A 1 247 ? -12.400 17.640  11.139  1.00 15.39 ? 357  ILE A C     1 
ATOM   1487 O  O     . ILE A 1 247 ? -12.985 18.436  11.890  1.00 15.81 ? 357  ILE A O     1 
ATOM   1488 C  CB    . ILE A 1 247 ? -13.154 17.283  8.752   1.00 14.25 ? 357  ILE A CB    1 
ATOM   1489 C  CG1   . ILE A 1 247 ? -13.056 17.799  7.317   1.00 14.50 ? 357  ILE A CG1   1 
ATOM   1490 C  CG2   . ILE A 1 247 ? -14.586 17.479  9.290   1.00 15.13 ? 357  ILE A CG2   1 
ATOM   1491 C  CD1   . ILE A 1 247 ? -13.781 16.902  6.292   1.00 14.96 ? 357  ILE A CD1   1 
ATOM   1492 N  N     . LEU A 1 248 ? -11.979 16.434  11.567  1.00 14.91 ? 358  LEU A N     1 
ATOM   1493 C  CA    . LEU A 1 248 ? -12.152 16.038  12.964  1.00 16.52 ? 358  LEU A CA    1 
ATOM   1494 C  C     . LEU A 1 248 ? -11.517 17.051  13.919  1.00 17.19 ? 358  LEU A C     1 
ATOM   1495 O  O     . LEU A 1 248 ? -12.113 17.400  14.950  1.00 16.91 ? 358  LEU A O     1 
ATOM   1496 C  CB    . LEU A 1 248 ? -11.572 14.635  13.205  1.00 16.10 ? 358  LEU A CB    1 
ATOM   1497 C  CG    . LEU A 1 248 ? -12.327 13.450  12.586  1.00 15.36 ? 358  LEU A CG    1 
ATOM   1498 C  CD1   . LEU A 1 248 ? -11.475 12.176  12.685  1.00 17.76 ? 358  LEU A CD1   1 
ATOM   1499 C  CD2   . LEU A 1 248 ? -13.729 13.211  13.215  1.00 15.86 ? 358  LEU A CD2   1 
ATOM   1500 N  N     . GLU A 1 249 ? -10.310 17.540  13.596  1.00 16.50 ? 359  GLU A N     1 
ATOM   1501 C  CA    . GLU A 1 249 ? -9.626  18.491  14.471  1.00 15.37 ? 359  GLU A CA    1 
ATOM   1502 C  C     . GLU A 1 249 ? -10.286 19.872  14.446  1.00 16.64 ? 359  GLU A C     1 
ATOM   1503 O  O     . GLU A 1 249 ? -10.449 20.505  15.497  1.00 17.13 ? 359  GLU A O     1 
ATOM   1504 C  CB    . GLU A 1 249 ? -8.137  18.580  14.084  1.00 16.62 ? 359  GLU A CB    1 
ATOM   1505 C  CG    . GLU A 1 249 ? -7.290  17.397  14.639  1.00 16.30 ? 359  GLU A CG    1 
ATOM   1506 C  CD    . GLU A 1 249 ? -7.202  17.415  16.162  1.00 18.47 ? 359  GLU A CD    1 
ATOM   1507 O  OE1   . GLU A 1 249 ? -6.589  18.353  16.711  1.00 19.70 ? 359  GLU A OE1   1 
ATOM   1508 O  OE2   . GLU A 1 249 ? -7.770  16.513  16.818  1.00 19.12 ? 359  GLU A OE2   1 
ATOM   1509 N  N     . ALA A 1 250 ? -10.662 20.364  13.261  1.00 15.35 ? 360  ALA A N     1 
ATOM   1510 C  CA    . ALA A 1 250 ? -11.324 21.665  13.180  1.00 15.77 ? 360  ALA A CA    1 
ATOM   1511 C  C     . ALA A 1 250 ? -12.669 21.651  13.904  1.00 16.07 ? 360  ALA A C     1 
ATOM   1512 O  O     . ALA A 1 250 ? -13.034 22.634  14.572  1.00 17.05 ? 360  ALA A O     1 
ATOM   1513 C  CB    . ALA A 1 250 ? -11.505 22.069  11.715  1.00 16.02 ? 360  ALA A CB    1 
ATOM   1514 N  N     . VAL A 1 251 ? -13.426 20.547  13.775  1.00 16.46 ? 361  VAL A N     1 
ATOM   1515 C  CA    . VAL A 1 251 ? -14.733 20.424  14.421  1.00 18.07 ? 361  VAL A CA    1 
ATOM   1516 C  C     . VAL A 1 251 ? -14.591 20.442  15.942  1.00 17.88 ? 361  VAL A C     1 
ATOM   1517 O  O     . VAL A 1 251 ? -15.442 21.000  16.650  1.00 18.20 ? 361  VAL A O     1 
ATOM   1518 C  CB    . VAL A 1 251 ? -15.448 19.150  13.909  1.00 17.91 ? 361  VAL A CB    1 
ATOM   1519 C  CG1   . VAL A 1 251 ? -16.658 18.761  14.781  1.00 21.18 ? 361  VAL A CG1   1 
ATOM   1520 C  CG2   . VAL A 1 251 ? -15.891 19.338  12.454  1.00 18.45 ? 361  VAL A CG2   1 
ATOM   1521 N  N     . ALA A 1 252 ? -13.502 19.878  16.470  1.00 17.20 ? 362  ALA A N     1 
ATOM   1522 C  CA    . ALA A 1 252 ? -13.291 19.888  17.916  1.00 17.19 ? 362  ALA A CA    1 
ATOM   1523 C  C     . ALA A 1 252 ? -13.199 21.309  18.486  1.00 19.14 ? 362  ALA A C     1 
ATOM   1524 O  O     . ALA A 1 252 ? -13.471 21.511  19.679  1.00 20.12 ? 362  ALA A O     1 
ATOM   1525 C  CB    . ALA A 1 252 ? -12.029 19.089  18.255  1.00 17.57 ? 362  ALA A CB    1 
ATOM   1526 N  N     . ALA A 1 253 ? -12.821 22.297  17.666  1.00 18.32 ? 363  ALA A N     1 
ATOM   1527 C  CA    . ALA A 1 253 ? -12.815 23.699  18.075  1.00 18.47 ? 363  ALA A CA    1 
ATOM   1528 C  C     . ALA A 1 253 ? -14.111 24.417  17.711  1.00 19.29 ? 363  ALA A C     1 
ATOM   1529 O  O     . ALA A 1 253 ? -14.594 25.242  18.494  1.00 21.41 ? 363  ALA A O     1 
ATOM   1530 C  CB    . ALA A 1 253 ? -11.626 24.430  17.439  1.00 19.25 ? 363  ALA A CB    1 
ATOM   1531 N  N     . CYS A 1 254 ? -14.688 24.115  16.538  1.00 17.61 ? 364  CYS A N     1 
ATOM   1532 C  CA    . CYS A 1 254 ? -15.826 24.888  16.028  1.00 17.33 ? 364  CYS A CA    1 
ATOM   1533 C  C     . CYS A 1 254 ? -17.171 24.425  16.597  1.00 18.40 ? 364  CYS A C     1 
ATOM   1534 O  O     . CYS A 1 254 ? -18.039 25.260  16.888  1.00 18.51 ? 364  CYS A O     1 
ATOM   1535 C  CB    . CYS A 1 254 ? -15.853 24.827  14.498  1.00 16.75 ? 364  CYS A CB    1 
ATOM   1536 S  SG    . CYS A 1 254 ? -14.486 25.683  13.680  1.00 17.13 ? 364  CYS A SG    1 
ATOM   1537 N  N     . ARG A 1 255 ? -17.382 23.113  16.755  1.00 19.59 ? 365  ARG A N     1 
ATOM   1538 C  CA    . ARG A 1 255 ? -18.682 22.639  17.240  1.00 21.31 ? 365  ARG A CA    1 
ATOM   1539 C  C     . ARG A 1 255 ? -19.025 23.170  18.630  1.00 22.82 ? 365  ARG A C     1 
ATOM   1540 O  O     . ARG A 1 255 ? -20.173 23.615  18.836  1.00 24.04 ? 365  ARG A O     1 
ATOM   1541 C  CB    . ARG A 1 255 ? -18.720 21.106  17.201  1.00 24.73 ? 365  ARG A CB    1 
ATOM   1542 C  CG    . ARG A 1 255 ? -20.058 20.483  17.590  1.00 31.63 ? 365  ARG A CG    1 
ATOM   1543 C  CD    . ARG A 1 255 ? -19.981 18.968  17.470  1.00 38.39 ? 365  ARG A CD    1 
ATOM   1544 N  NE    . ARG A 1 255 ? -21.266 18.319  17.710  1.00 45.63 ? 365  ARG A NE    1 
ATOM   1545 C  CZ    . ARG A 1 255 ? -22.132 17.998  16.753  1.00 50.99 ? 365  ARG A CZ    1 
ATOM   1546 N  NH1   . ARG A 1 255 ? -21.852 18.269  15.486  1.00 54.29 ? 365  ARG A NH1   1 
ATOM   1547 N  NH2   . ARG A 1 255 ? -23.279 17.406  17.064  1.00 53.40 ? 365  ARG A NH2   1 
ATOM   1548 N  N     . PRO A 1 256 ? -18.115 23.163  19.611  1.00 22.54 ? 366  PRO A N     1 
ATOM   1549 C  CA    . PRO A 1 256 ? -18.460 23.707  20.934  1.00 23.19 ? 366  PRO A CA    1 
ATOM   1550 C  C     . PRO A 1 256 ? -18.798 25.186  20.910  1.00 23.60 ? 366  PRO A C     1 
ATOM   1551 O  O     . PRO A 1 256 ? -19.469 25.669  21.833  1.00 24.94 ? 366  PRO A O     1 
ATOM   1552 C  CB    . PRO A 1 256 ? -17.201 23.434  21.770  1.00 24.23 ? 366  PRO A CB    1 
ATOM   1553 C  CG    . PRO A 1 256 ? -16.470 22.375  21.047  1.00 25.41 ? 366  PRO A CG    1 
ATOM   1554 C  CD    . PRO A 1 256 ? -16.756 22.589  19.589  1.00 23.44 ? 366  PRO A CD    1 
ATOM   1555 N  N     . ALA A 1 257 ? -18.354 25.918  19.890  1.00 22.42 ? 367  ALA A N     1 
ATOM   1556 C  CA    . ALA A 1 257 ? -18.663 27.334  19.733  1.00 22.83 ? 367  ALA A CA    1 
ATOM   1557 C  C     . ALA A 1 257 ? -19.878 27.598  18.839  1.00 24.15 ? 367  ALA A C     1 
ATOM   1558 O  O     . ALA A 1 257 ? -20.241 28.767  18.640  1.00 26.59 ? 367  ALA A O     1 
ATOM   1559 C  CB    . ALA A 1 257 ? -17.437 28.063  19.170  1.00 22.05 ? 367  ALA A CB    1 
ATOM   1560 N  N     . GLY A 1 258 ? -20.514 26.555  18.297  1.00 23.14 ? 368  GLY A N     1 
ATOM   1561 C  CA    . GLY A 1 258 ? -21.640 26.737  17.388  1.00 23.27 ? 368  GLY A CA    1 
ATOM   1562 C  C     . GLY A 1 258 ? -21.307 27.347  16.038  1.00 21.94 ? 368  GLY A C     1 
ATOM   1563 O  O     . GLY A 1 258 ? -22.154 28.039  15.455  1.00 24.56 ? 368  GLY A O     1 
ATOM   1564 N  N     . VAL A 1 259 ? -20.118 27.089  15.507  1.00 18.75 ? 369  VAL A N     1 
ATOM   1565 C  CA    . VAL A 1 259 ? -19.671 27.649  14.234  1.00 18.81 ? 369  VAL A CA    1 
ATOM   1566 C  C     . VAL A 1 259 ? -19.619 26.529  13.193  1.00 17.60 ? 369  VAL A C     1 
ATOM   1567 O  O     . VAL A 1 259 ? -18.862 25.562  13.372  1.00 19.00 ? 369  VAL A O     1 
ATOM   1568 C  CB    . VAL A 1 259 ? -18.301 28.335  14.377  1.00 19.25 ? 369  VAL A CB    1 
ATOM   1569 C  CG1   . VAL A 1 259 ? -17.790 28.760  13.013  1.00 20.44 ? 369  VAL A CG1   1 
ATOM   1570 C  CG2   . VAL A 1 259 ? -18.394 29.542  15.324  1.00 19.83 ? 369  VAL A CG2   1 
ATOM   1571 N  N     . PRO A 1 260 ? -20.376 26.616  12.089  1.00 16.70 ? 370  PRO A N     1 
ATOM   1572 C  CA    . PRO A 1 260 ? -20.354 25.531  11.085  1.00 16.89 ? 370  PRO A CA    1 
ATOM   1573 C  C     . PRO A 1 260 ? -19.021 25.420  10.349  1.00 16.70 ? 370  PRO A C     1 
ATOM   1574 O  O     . PRO A 1 260 ? -18.329 26.420  10.129  1.00 17.04 ? 370  PRO A O     1 
ATOM   1575 C  CB    . PRO A 1 260 ? -21.466 25.927  10.105  1.00 18.20 ? 370  PRO A CB    1 
ATOM   1576 C  CG    . PRO A 1 260 ? -22.353 26.860  10.883  1.00 19.92 ? 370  PRO A CG    1 
ATOM   1577 C  CD    . PRO A 1 260 ? -21.448 27.594  11.832  1.00 18.16 ? 370  PRO A CD    1 
ATOM   1578 N  N     . VAL A 1 261 ? -18.691 24.187  9.925   1.00 15.15 ? 371  VAL A N     1 
ATOM   1579 C  CA    . VAL A 1 261 ? -17.472 23.875  9.167   1.00 14.99 ? 371  VAL A CA    1 
ATOM   1580 C  C     . VAL A 1 261 ? -17.814 23.496  7.721   1.00 15.00 ? 371  VAL A C     1 
ATOM   1581 O  O     . VAL A 1 261 ? -18.656 22.621  7.479   1.00 15.24 ? 371  VAL A O     1 
ATOM   1582 C  CB    . VAL A 1 261 ? -16.683 22.742  9.847   1.00 15.79 ? 371  VAL A CB    1 
ATOM   1583 C  CG1   . VAL A 1 261 ? -15.634 22.152  8.903   1.00 16.71 ? 371  VAL A CG1   1 
ATOM   1584 C  CG2   . VAL A 1 261 ? -16.025 23.248  11.115  1.00 17.73 ? 371  VAL A CG2   1 
ATOM   1585 N  N     . ILE A 1 262 ? -17.124 24.125  6.761   1.00 15.62 ? 372  ILE A N     1 
ATOM   1586 C  CA    . ILE A 1 262 ? -17.219 23.806  5.330   1.00 15.40 ? 372  ILE A CA    1 
ATOM   1587 C  C     . ILE A 1 262 ? -16.021 22.939  4.933   1.00 16.06 ? 372  ILE A C     1 
ATOM   1588 O  O     . ILE A 1 262 ? -14.874 23.400  4.997   1.00 17.12 ? 372  ILE A O     1 
ATOM   1589 C  CB    . ILE A 1 262 ? -17.243 25.087  4.473   1.00 15.71 ? 372  ILE A CB    1 
ATOM   1590 C  CG1   . ILE A 1 262 ? -18.352 26.052  4.911   1.00 16.48 ? 372  ILE A CG1   1 
ATOM   1591 C  CG2   . ILE A 1 262 ? -17.404 24.751  2.986   1.00 16.18 ? 372  ILE A CG2   1 
ATOM   1592 C  CD1   . ILE A 1 262 ? -18.155 27.462  4.363   1.00 18.40 ? 372  ILE A CD1   1 
ATOM   1593 N  N     . ALA A 1 263 ? -16.273 21.708  4.472   1.00 13.95 ? 373  ALA A N     1 
ATOM   1594 C  CA    . ALA A 1 263 ? -15.212 20.806  3.986   1.00 14.37 ? 373  ALA A CA    1 
ATOM   1595 C  C     . ALA A 1 263 ? -14.863 21.122  2.524   1.00 15.04 ? 373  ALA A C     1 
ATOM   1596 O  O     . ALA A 1 263 ? -15.674 20.867  1.627   1.00 17.12 ? 373  ALA A O     1 
ATOM   1597 C  CB    . ALA A 1 263 ? -15.664 19.349  4.133   1.00 16.95 ? 373  ALA A CB    1 
ATOM   1598 N  N     . ASP A 1 264 ? -13.648 21.655  2.258   1.00 14.28 ? 374  ASP A N     1 
ATOM   1599 C  CA    . ASP A 1 264 ? -13.270 22.190  0.932   1.00 13.85 ? 374  ASP A CA    1 
ATOM   1600 C  C     . ASP A 1 264 ? -12.079 21.438  0.314   1.00 15.64 ? 374  ASP A C     1 
ATOM   1601 O  O     . ASP A 1 264 ? -10.934 21.642  0.738   1.00 15.67 ? 374  ASP A O     1 
ATOM   1602 C  CB    . ASP A 1 264 ? -12.940 23.686  1.060   1.00 15.98 ? 374  ASP A CB    1 
ATOM   1603 C  CG    . ASP A 1 264 ? -12.506 24.323  -0.259  1.00 15.93 ? 374  ASP A CG    1 
ATOM   1604 O  OD1   . ASP A 1 264 ? -12.781 23.753  -1.344  1.00 16.97 ? 374  ASP A OD1   1 
ATOM   1605 O  OD2   . ASP A 1 264 ? -11.888 25.416  -0.196  1.00 15.90 ? 374  ASP A OD2   1 
ATOM   1606 N  N     . GLY A 1 265 ? -12.333 20.589  -0.684  1.00 16.34 ? 375  GLY A N     1 
ATOM   1607 C  CA    . GLY A 1 265 ? -11.305 19.963  -1.503  1.00 15.61 ? 375  GLY A CA    1 
ATOM   1608 C  C     . GLY A 1 265 ? -11.155 18.460  -1.266  1.00 16.60 ? 375  GLY A C     1 
ATOM   1609 O  O     . GLY A 1 265 ? -11.351 17.949  -0.153  1.00 18.78 ? 375  GLY A O     1 
ATOM   1610 N  N     . GLY A 1 266 ? -10.780 17.741  -2.334  1.00 15.58 ? 376  GLY A N     1 
ATOM   1611 C  CA    . GLY A 1 266 ? -10.513 16.306  -2.247  1.00 16.51 ? 376  GLY A CA    1 
ATOM   1612 C  C     . GLY A 1 266 ? -11.708 15.382  -2.422  1.00 18.86 ? 376  GLY A C     1 
ATOM   1613 O  O     . GLY A 1 266 ? -11.524 14.150  -2.425  1.00 20.73 ? 376  GLY A O     1 
ATOM   1614 N  N     . LEU A 1 267 ? -12.924 15.912  -2.558  1.00 18.00 ? 377  LEU A N     1 
ATOM   1615 C  CA    . LEU A 1 267 ? -14.095 15.048  -2.723  1.00 17.31 ? 377  LEU A CA    1 
ATOM   1616 C  C     . LEU A 1 267 ? -14.161 14.557  -4.168  1.00 19.09 ? 377  LEU A C     1 
ATOM   1617 O  O     . LEU A 1 267 ? -14.213 15.364  -5.106  1.00 19.94 ? 377  LEU A O     1 
ATOM   1618 C  CB    . LEU A 1 267 ? -15.380 15.781  -2.328  1.00 18.01 ? 377  LEU A CB    1 
ATOM   1619 C  CG    . LEU A 1 267 ? -15.615 15.926  -0.822  1.00 19.44 ? 377  LEU A CG    1 
ATOM   1620 C  CD1   . LEU A 1 267 ? -14.911 17.155  -0.275  1.00 20.71 ? 377  LEU A CD1   1 
ATOM   1621 C  CD2   . LEU A 1 267 ? -17.116 15.981  -0.500  1.00 22.77 ? 377  LEU A CD2   1 
ATOM   1622 N  N     . GLN A 1 268 ? -14.148 13.230  -4.349  1.00 20.06 ? 378  GLN A N     1 
ATOM   1623 C  CA    . GLN A 1 268 ? -14.127 12.617  -5.673  1.00 23.39 ? 378  GLN A CA    1 
ATOM   1624 C  C     . GLN A 1 268 ? -15.411 11.884  -6.047  1.00 23.14 ? 378  GLN A C     1 
ATOM   1625 O  O     . GLN A 1 268 ? -15.636 11.652  -7.238  1.00 27.10 ? 378  GLN A O     1 
ATOM   1626 C  CB    . GLN A 1 268 ? -12.971 11.603  -5.787  1.00 27.94 ? 378  GLN A CB    1 
ATOM   1627 C  CG    . GLN A 1 268 ? -11.568 12.178  -5.675  1.00 34.13 ? 378  GLN A CG    1 
ATOM   1628 C  CD    . GLN A 1 268 ? -10.484 11.107  -5.799  1.00 40.82 ? 378  GLN A CD    1 
ATOM   1629 O  OE1   . GLN A 1 268 ? -9.679  11.126  -6.732  1.00 43.99 ? 378  GLN A OE1   1 
ATOM   1630 N  NE2   . GLN A 1 268 ? -10.462 10.170  -4.854  1.00 43.65 ? 378  GLN A NE2   1 
ATOM   1631 N  N     . TYR A 1 269 ? -16.228 11.490  -5.069  1.00 19.68 ? 379  TYR A N     1 
ATOM   1632 C  CA    . TYR A 1 269 ? -17.418 10.669  -5.284  1.00 20.74 ? 379  TYR A CA    1 
ATOM   1633 C  C     . TYR A 1 269 ? -18.533 11.176  -4.374  1.00 19.77 ? 379  TYR A C     1 
ATOM   1634 O  O     . TYR A 1 269 ? -18.276 11.864  -3.388  1.00 19.03 ? 379  TYR A O     1 
ATOM   1635 C  CB    . TYR A 1 269 ? -17.170 9.178   -4.976  1.00 24.10 ? 379  TYR A CB    1 
ATOM   1636 C  CG    . TYR A 1 269 ? -15.901 8.578   -5.546  1.00 27.84 ? 379  TYR A CG    1 
ATOM   1637 C  CD1   . TYR A 1 269 ? -15.832 8.168   -6.871  1.00 29.73 ? 379  TYR A CD1   1 
ATOM   1638 C  CD2   . TYR A 1 269 ? -14.785 8.383   -4.738  1.00 29.03 ? 379  TYR A CD2   1 
ATOM   1639 C  CE1   . TYR A 1 269 ? -14.670 7.605   -7.385  1.00 31.64 ? 379  TYR A CE1   1 
ATOM   1640 C  CE2   . TYR A 1 269 ? -13.626 7.825   -5.237  1.00 30.85 ? 379  TYR A CE2   1 
ATOM   1641 C  CZ    . TYR A 1 269 ? -13.570 7.436   -6.561  1.00 32.74 ? 379  TYR A CZ    1 
ATOM   1642 O  OH    . TYR A 1 269 ? -12.412 6.874   -7.061  1.00 36.86 ? 379  TYR A OH    1 
ATOM   1643 N  N     . SER A 1 270 ? -19.785 10.821  -4.696  1.00 20.52 ? 380  SER A N     1 
ATOM   1644 C  CA    . SER A 1 270 ? -20.895 11.225  -3.831  1.00 19.05 ? 380  SER A CA    1 
ATOM   1645 C  C     . SER A 1 270 ? -20.711 10.694  -2.412  1.00 17.76 ? 380  SER A C     1 
ATOM   1646 O  O     . SER A 1 270 ? -21.062 11.368  -1.438  1.00 17.24 ? 380  SER A O     1 
ATOM   1647 C  CB    . SER A 1 270 ? -22.243 10.766  -4.422  1.00 18.81 ? 380  SER A CB    1 
ATOM   1648 O  OG    . SER A 1 270 ? -22.300 9.354   -4.656  1.00 20.13 ? 380  SER A OG    1 
ATOM   1649 N  N     . GLY A 1 271 ? -20.142 9.490   -2.270  1.00 18.02 ? 381  GLY A N     1 
ATOM   1650 C  CA    . GLY A 1 271 ? -19.902 8.943   -0.943  1.00 18.88 ? 381  GLY A CA    1 
ATOM   1651 C  C     . GLY A 1 271 ? -18.963 9.778   -0.089  1.00 18.31 ? 381  GLY A C     1 
ATOM   1652 O  O     . GLY A 1 271 ? -19.037 9.731   1.146   1.00 17.86 ? 381  GLY A O     1 
ATOM   1653 N  N     . ASP A 1 272 ? -18.072 10.550  -0.723  1.00 18.12 ? 382  ASP A N     1 
ATOM   1654 C  CA    . ASP A 1 272 ? -17.168 11.414  0.042   1.00 17.53 ? 382  ASP A CA    1 
ATOM   1655 C  C     . ASP A 1 272 ? -17.928 12.547  0.738   1.00 18.07 ? 382  ASP A C     1 
ATOM   1656 O  O     . ASP A 1 272 ? -17.494 13.032  1.795   1.00 17.29 ? 382  ASP A O     1 
ATOM   1657 C  CB    . ASP A 1 272 ? -16.076 11.995  -0.870  1.00 18.87 ? 382  ASP A CB    1 
ATOM   1658 C  CG    . ASP A 1 272 ? -15.116 10.935  -1.415  1.00 20.62 ? 382  ASP A CG    1 
ATOM   1659 O  OD1   . ASP A 1 272 ? -15.135 9.776   -0.942  1.00 21.35 ? 382  ASP A OD1   1 
ATOM   1660 O  OD2   . ASP A 1 272 ? -14.319 11.274  -2.324  1.00 21.51 ? 382  ASP A OD2   1 
ATOM   1661 N  N     . ILE A 1 273 ? -19.056 12.986  0.167   1.00 16.30 ? 383  ILE A N     1 
ATOM   1662 C  CA    . ILE A 1 273 ? -19.891 13.990  0.833   1.00 15.94 ? 383  ILE A CA    1 
ATOM   1663 C  C     . ILE A 1 273 ? -20.407 13.444  2.161   1.00 15.83 ? 383  ILE A C     1 
ATOM   1664 O  O     . ILE A 1 273 ? -20.329 14.110  3.201   1.00 15.86 ? 383  ILE A O     1 
ATOM   1665 C  CB    . ILE A 1 273 ? -21.050 14.426  -0.084  1.00 19.40 ? 383  ILE A CB    1 
ATOM   1666 C  CG1   . ILE A 1 273 ? -20.523 15.074  -1.370  1.00 21.17 ? 383  ILE A CG1   1 
ATOM   1667 C  CG2   . ILE A 1 273 ? -22.009 15.384  0.661   1.00 19.71 ? 383  ILE A CG2   1 
ATOM   1668 C  CD1   . ILE A 1 273 ? -21.571 15.173  -2.477  1.00 24.18 ? 383  ILE A CD1   1 
ATOM   1669 N  N     . ALA A 1 274 ? -20.933 12.208  2.151   1.00 16.19 ? 384  ALA A N     1 
ATOM   1670 C  CA    . ALA A 1 274 ? -21.423 11.608  3.391   1.00 15.45 ? 384  ALA A CA    1 
ATOM   1671 C  C     . ALA A 1 274 ? -20.303 11.442  4.417   1.00 16.49 ? 384  ALA A C     1 
ATOM   1672 O  O     . ALA A 1 274 ? -20.522 11.661  5.616   1.00 17.40 ? 384  ALA A O     1 
ATOM   1673 C  CB    . ALA A 1 274 ? -22.095 10.255  3.103   1.00 16.48 ? 384  ALA A CB    1 
ATOM   1674 N  N     . LYS A 1 275 ? -19.092 11.056  3.974   1.00 15.72 ? 385  LYS A N     1 
ATOM   1675 C  CA    . LYS A 1 275 ? -17.975 10.907  4.914   1.00 14.69 ? 385  LYS A CA    1 
ATOM   1676 C  C     . LYS A 1 275 ? -17.590 12.243  5.553   1.00 14.74 ? 385  LYS A C     1 
ATOM   1677 O  O     . LYS A 1 275 ? -17.340 12.308  6.768   1.00 16.02 ? 385  LYS A O     1 
ATOM   1678 C  CB    . LYS A 1 275 ? -16.751 10.277  4.218   1.00 15.98 ? 385  LYS A CB    1 
ATOM   1679 C  CG    . LYS A 1 275 ? -16.967 8.857   3.637   1.00 16.13 ? 385  LYS A CG    1 
ATOM   1680 C  CD    . LYS A 1 275 ? -15.710 8.334   2.889   1.00 15.74 ? 385  LYS A CD    1 
ATOM   1681 C  CE    . LYS A 1 275 ? -15.972 6.982   2.191   1.00 16.75 ? 385  LYS A CE    1 
ATOM   1682 N  NZ    . LYS A 1 275 ? -14.724 6.374   1.599   1.00 16.91 ? 385  LYS A NZ    1 
ATOM   1683 N  N     . ALA A 1 276 ? -17.536 13.317  4.753   1.00 14.51 ? 386  ALA A N     1 
ATOM   1684 C  CA    . ALA A 1 276 ? -17.158 14.638  5.267   1.00 14.25 ? 386  ALA A CA    1 
ATOM   1685 C  C     . ALA A 1 276 ? -18.138 15.131  6.328   1.00 16.52 ? 386  ALA A C     1 
ATOM   1686 O  O     . ALA A 1 276 ? -17.726 15.683  7.360   1.00 15.85 ? 386  ALA A O     1 
ATOM   1687 C  CB    . ALA A 1 276 ? -17.087 15.646  4.116   1.00 14.82 ? 386  ALA A CB    1 
ATOM   1688 N  N     . LEU A 1 277 ? -19.444 14.960  6.080   1.00 16.03 ? 387  LEU A N     1 
ATOM   1689 C  CA    . LEU A 1 277 ? -20.454 15.418  7.031   1.00 15.85 ? 387  LEU A CA    1 
ATOM   1690 C  C     . LEU A 1 277 ? -20.466 14.548  8.291   1.00 17.13 ? 387  LEU A C     1 
ATOM   1691 O  O     . LEU A 1 277 ? -20.622 15.066  9.406   1.00 18.47 ? 387  LEU A O     1 
ATOM   1692 C  CB    . LEU A 1 277 ? -21.839 15.453  6.356   1.00 16.74 ? 387  LEU A CB    1 
ATOM   1693 C  CG    . LEU A 1 277 ? -22.007 16.359  5.124   1.00 17.00 ? 387  LEU A CG    1 
ATOM   1694 C  CD1   . LEU A 1 277 ? -23.425 16.291  4.553   1.00 18.70 ? 387  LEU A CD1   1 
ATOM   1695 C  CD2   . LEU A 1 277 ? -21.656 17.835  5.425   1.00 18.44 ? 387  LEU A CD2   1 
ATOM   1696 N  N     . ALA A 1 278 ? -20.260 13.227  8.145   1.00 16.05 ? 388  ALA A N     1 
ATOM   1697 C  CA    . ALA A 1 278 ? -20.155 12.366  9.325   1.00 15.30 ? 388  ALA A CA    1 
ATOM   1698 C  C     . ALA A 1 278 ? -18.960 12.730  10.204  1.00 17.64 ? 388  ALA A C     1 
ATOM   1699 O  O     . ALA A 1 278 ? -19.030 12.569  11.432  1.00 18.18 ? 388  ALA A O     1 
ATOM   1700 C  CB    . ALA A 1 278 ? -20.068 10.885  8.922   1.00 16.56 ? 388  ALA A CB    1 
ATOM   1701 N  N     . ALA A 1 279 ? -17.851 13.199  9.608   1.00 16.78 ? 389  ALA A N     1 
ATOM   1702 C  CA    . ALA A 1 279 ? -16.719 13.671  10.404  1.00 16.12 ? 389  ALA A CA    1 
ATOM   1703 C  C     . ALA A 1 279 ? -17.020 14.973  11.147  1.00 17.99 ? 389  ALA A C     1 
ATOM   1704 O  O     . ALA A 1 279 ? -16.199 15.396  11.977  1.00 17.93 ? 389  ALA A O     1 
ATOM   1705 C  CB    . ALA A 1 279 ? -15.461 13.842  9.523   1.00 16.88 ? 389  ALA A CB    1 
ATOM   1706 N  N     . GLY A 1 280 ? -18.166 15.609  10.890  1.00 15.93 ? 390  GLY A N     1 
ATOM   1707 C  CA    . GLY A 1 280 ? -18.574 16.793  11.631  1.00 16.29 ? 390  GLY A CA    1 
ATOM   1708 C  C     . GLY A 1 280 ? -18.771 18.056  10.810  1.00 15.79 ? 390  GLY A C     1 
ATOM   1709 O  O     . GLY A 1 280 ? -19.310 19.035  11.352  1.00 17.21 ? 390  GLY A O     1 
ATOM   1710 N  N     . ALA A 1 281 ? -18.377 18.095  9.532   1.00 15.74 ? 391  ALA A N     1 
ATOM   1711 C  CA    . ALA A 1 281 ? -18.663 19.248  8.681   1.00 16.71 ? 391  ALA A CA    1 
ATOM   1712 C  C     . ALA A 1 281 ? -20.172 19.420  8.498   1.00 16.46 ? 391  ALA A C     1 
ATOM   1713 O  O     . ALA A 1 281 ? -20.945 18.472  8.649   1.00 16.76 ? 391  ALA A O     1 
ATOM   1714 C  CB    . ALA A 1 281 ? -17.995 19.096  7.309   1.00 17.18 ? 391  ALA A CB    1 
ATOM   1715 N  N     . SER A 1 282 ? -20.590 20.658  8.184   1.00 15.51 ? 392  SER A N     1 
ATOM   1716 C  CA    . SER A 1 282 ? -21.994 20.983  7.912   1.00 15.63 ? 392  SER A CA    1 
ATOM   1717 C  C     . SER A 1 282 ? -22.320 21.154  6.425   1.00 16.07 ? 392  SER A C     1 
ATOM   1718 O  O     . SER A 1 282 ? -23.482 20.962  6.039   1.00 15.85 ? 392  SER A O     1 
ATOM   1719 C  CB    . SER A 1 282 ? -22.394 22.266  8.671   1.00 17.30 ? 392  SER A CB    1 
ATOM   1720 O  OG    . SER A 1 282 ? -22.432 22.059  10.091  1.00 19.84 ? 392  SER A OG    1 
ATOM   1721 N  N     . THR A 1 283 ? -21.342 21.531  5.589   1.00 16.95 ? 393  THR A N     1 
ATOM   1722 C  CA    . THR A 1 283 ? -21.488 21.574  4.132   1.00 16.31 ? 393  THR A CA    1 
ATOM   1723 C  C     . THR A 1 283 ? -20.170 21.144  3.489   1.00 16.95 ? 393  THR A C     1 
ATOM   1724 O  O     . THR A 1 283 ? -19.140 21.032  4.163   1.00 16.17 ? 393  THR A O     1 
ATOM   1725 C  CB    . THR A 1 283 ? -21.869 22.979  3.613   1.00 15.32 ? 393  THR A CB    1 
ATOM   1726 O  OG1   . THR A 1 283 ? -20.861 23.923  4.008   1.00 16.68 ? 393  THR A OG1   1 
ATOM   1727 C  CG2   . THR A 1 283 ? -23.240 23.450  4.130   1.00 16.53 ? 393  THR A CG2   1 
ATOM   1728 N  N     . ALA A 1 284 ? -20.195 20.910  2.163   1.00 16.95 ? 394  ALA A N     1 
ATOM   1729 C  CA    . ALA A 1 284 ? -18.995 20.579  1.387   1.00 15.81 ? 394  ALA A CA    1 
ATOM   1730 C  C     . ALA A 1 284 ? -18.891 21.490  0.170   1.00 16.63 ? 394  ALA A C     1 
ATOM   1731 O  O     . ALA A 1 284 ? -19.911 21.842  -0.434  1.00 17.47 ? 394  ALA A O     1 
ATOM   1732 C  CB    . ALA A 1 284 ? -18.981 19.094  0.933   1.00 17.31 ? 394  ALA A CB    1 
ATOM   1733 N  N     . MET A 1 285 ? -17.658 21.896  -0.167  1.00 16.36 ? 395  MET A N     1 
ATOM   1734 C  CA    . MET A 1 285 ? -17.361 22.724  -1.342  1.00 15.84 ? 395  MET A CA    1 
ATOM   1735 C  C     . MET A 1 285 ? -16.699 21.871  -2.425  1.00 15.66 ? 395  MET A C     1 
ATOM   1736 O  O     . MET A 1 285 ? -15.753 21.119  -2.135  1.00 15.85 ? 395  MET A O     1 
ATOM   1737 C  CB    . MET A 1 285 ? -16.459 23.922  -0.968  1.00 16.39 ? 395  MET A CB    1 
ATOM   1738 C  CG    . MET A 1 285 ? -16.012 24.797  -2.163  1.00 16.06 ? 395  MET A CG    1 
ATOM   1739 S  SD    . MET A 1 285 ? -15.094 26.306  -1.761  1.00 16.00 ? 395  MET A SD    1 
ATOM   1740 C  CE    . MET A 1 285 ? -16.424 27.512  -1.607  1.00 18.29 ? 395  MET A CE    1 
ATOM   1741 N  N     . LEU A 1 286 ? -17.176 22.003  -3.670  1.00 15.67 ? 396  LEU A N     1 
ATOM   1742 C  CA    . LEU A 1 286 ? -16.812 21.114  -4.775  1.00 15.08 ? 396  LEU A CA    1 
ATOM   1743 C  C     . LEU A 1 286 ? -16.249 21.898  -5.956  1.00 16.23 ? 396  LEU A C     1 
ATOM   1744 O  O     . LEU A 1 286 ? -16.875 22.856  -6.435  1.00 16.33 ? 396  LEU A O     1 
ATOM   1745 C  CB    . LEU A 1 286 ? -18.030 20.304  -5.249  1.00 17.12 ? 396  LEU A CB    1 
ATOM   1746 C  CG    . LEU A 1 286 ? -18.825 19.500  -4.219  1.00 19.07 ? 396  LEU A CG    1 
ATOM   1747 C  CD1   . LEU A 1 286 ? -19.987 18.806  -4.908  1.00 20.86 ? 396  LEU A CD1   1 
ATOM   1748 C  CD2   . LEU A 1 286 ? -17.950 18.480  -3.516  1.00 22.25 ? 396  LEU A CD2   1 
ATOM   1749 N  N     . GLY A 1 287 ? -15.082 21.467  -6.445  1.00 16.92 ? 397  GLY A N     1 
ATOM   1750 C  CA    . GLY A 1 287 ? -14.521 21.996  -7.672  1.00 16.59 ? 397  GLY A CA    1 
ATOM   1751 C  C     . GLY A 1 287 ? -14.583 21.006  -8.824  1.00 18.03 ? 397  GLY A C     1 
ATOM   1752 O  O     . GLY A 1 287 ? -15.374 21.189  -9.749  1.00 20.04 ? 397  GLY A O     1 
ATOM   1753 N  N     A SER A 1 288 ? -13.756 19.957  -8.770  0.52 17.98 ? 398  SER A N     1 
ATOM   1754 N  N     B SER A 1 288 ? -13.784 19.931  -8.770  0.48 18.52 ? 398  SER A N     1 
ATOM   1755 C  CA    A SER A 1 288 ? -13.676 19.001  -9.873  0.52 19.35 ? 398  SER A CA    1 
ATOM   1756 C  CA    B SER A 1 288 ? -13.688 19.027  -9.918  0.48 19.92 ? 398  SER A CA    1 
ATOM   1757 C  C     A SER A 1 288 ? -15.045 18.420  -10.227 0.52 20.66 ? 398  SER A C     1 
ATOM   1758 C  C     B SER A 1 288 ? -15.015 18.334  -10.235 0.48 20.72 ? 398  SER A C     1 
ATOM   1759 O  O     A SER A 1 288 ? -15.399 18.326  -11.409 0.52 22.71 ? 398  SER A O     1 
ATOM   1760 O  O     B SER A 1 288 ? -15.304 18.069  -11.408 0.48 22.36 ? 398  SER A O     1 
ATOM   1761 C  CB    A SER A 1 288 ? -12.690 17.886  -9.518  0.52 18.85 ? 398  SER A CB    1 
ATOM   1762 C  CB    B SER A 1 288 ? -12.587 17.985  -9.691  0.48 20.22 ? 398  SER A CB    1 
ATOM   1763 O  OG    A SER A 1 288 ? -12.721 16.847  -10.478 0.52 19.40 ? 398  SER A OG    1 
ATOM   1764 O  OG    B SER A 1 288 ? -13.028 16.928  -8.858  0.48 20.90 ? 398  SER A OG    1 
ATOM   1765 N  N     . LEU A 1 289 ? -15.834 18.030  -9.222  1.00 20.60 ? 399  LEU A N     1 
ATOM   1766 C  CA    . LEU A 1 289 ? -17.110 17.357  -9.495  1.00 20.42 ? 399  LEU A CA    1 
ATOM   1767 C  C     . LEU A 1 289 ? -18.119 18.249  -10.212 1.00 21.32 ? 399  LEU A C     1 
ATOM   1768 O  O     . LEU A 1 289 ? -19.072 17.722  -10.805 1.00 23.16 ? 399  LEU A O     1 
ATOM   1769 C  CB    . LEU A 1 289 ? -17.727 16.821  -8.197  1.00 20.62 ? 399  LEU A CB    1 
ATOM   1770 C  CG    . LEU A 1 289 ? -17.015 15.599  -7.603  1.00 23.21 ? 399  LEU A CG    1 
ATOM   1771 C  CD1   . LEU A 1 289 ? -17.593 15.243  -6.234  1.00 22.50 ? 399  LEU A CD1   1 
ATOM   1772 C  CD2   . LEU A 1 289 ? -17.084 14.405  -8.544  1.00 27.44 ? 399  LEU A CD2   1 
ATOM   1773 N  N     . LEU A 1 290 ? -17.941 19.576  -10.173 1.00 18.77 ? 400  LEU A N     1 
ATOM   1774 C  CA    . LEU A 1 290 ? -18.838 20.505  -10.860 1.00 20.15 ? 400  LEU A CA    1 
ATOM   1775 C  C     . LEU A 1 290 ? -18.215 21.174  -12.083 1.00 22.00 ? 400  LEU A C     1 
ATOM   1776 O  O     . LEU A 1 290 ? -18.956 21.704  -12.916 1.00 24.29 ? 400  LEU A O     1 
ATOM   1777 C  CB    . LEU A 1 290 ? -19.349 21.590  -9.888  1.00 20.67 ? 400  LEU A CB    1 
ATOM   1778 C  CG    . LEU A 1 290 ? -20.046 21.084  -8.615  1.00 19.24 ? 400  LEU A CG    1 
ATOM   1779 C  CD1   . LEU A 1 290 ? -20.540 22.214  -7.689  1.00 18.64 ? 400  LEU A CD1   1 
ATOM   1780 C  CD2   . LEU A 1 290 ? -21.206 20.145  -8.988  1.00 19.96 ? 400  LEU A CD2   1 
ATOM   1781 N  N     . ALA A 1 291 ? -16.882 21.142  -12.226 1.00 23.21 ? 401  ALA A N     1 
ATOM   1782 C  CA    . ALA A 1 291 ? -16.221 21.735  -13.390 1.00 22.26 ? 401  ALA A CA    1 
ATOM   1783 C  C     . ALA A 1 291 ? -16.649 21.107  -14.713 1.00 25.79 ? 401  ALA A C     1 
ATOM   1784 O  O     . ALA A 1 291 ? -16.546 21.760  -15.757 1.00 29.54 ? 401  ALA A O     1 
ATOM   1785 C  CB    . ALA A 1 291 ? -14.699 21.621  -13.256 1.00 22.58 ? 401  ALA A CB    1 
ATOM   1786 N  N     . GLY A 1 292 ? -17.108 19.863  -14.718 1.00 25.42 ? 402  GLY A N     1 
ATOM   1787 C  CA    . GLY A 1 292 ? -17.510 19.317  -16.004 1.00 27.13 ? 402  GLY A CA    1 
ATOM   1788 C  C     . GLY A 1 292 ? -18.888 19.701  -16.523 1.00 28.05 ? 402  GLY A C     1 
ATOM   1789 O  O     . GLY A 1 292 ? -19.265 19.239  -17.604 1.00 31.27 ? 402  GLY A O     1 
ATOM   1790 N  N     . THR A 1 293 ? -19.651 20.531  -15.815 1.00 24.97 ? 403  THR A N     1 
ATOM   1791 C  CA    . THR A 1 293 ? -21.054 20.728  -16.151 1.00 23.88 ? 403  THR A CA    1 
ATOM   1792 C  C     . THR A 1 293 ? -21.239 21.846  -17.178 1.00 24.24 ? 403  THR A C     1 
ATOM   1793 O  O     . THR A 1 293 ? -20.359 22.687  -17.396 1.00 24.52 ? 403  THR A O     1 
ATOM   1794 C  CB    . THR A 1 293 ? -21.883 21.024  -14.894 1.00 23.61 ? 403  THR A CB    1 
ATOM   1795 O  OG1   . THR A 1 293 ? -21.413 22.232  -14.269 1.00 23.73 ? 403  THR A OG1   1 
ATOM   1796 C  CG2   . THR A 1 293 ? -21.817 19.849  -13.901 1.00 23.52 ? 403  THR A CG2   1 
ATOM   1797 N  N     . ALA A 1 294 ? -22.420 21.845  -17.809 1.00 24.48 ? 404  ALA A N     1 
ATOM   1798 C  CA    . ALA A 1 294 ? -22.731 22.839  -18.835 1.00 25.70 ? 404  ALA A CA    1 
ATOM   1799 C  C     . ALA A 1 294 ? -22.621 24.260  -18.295 1.00 25.65 ? 404  ALA A C     1 
ATOM   1800 O  O     . ALA A 1 294 ? -22.208 25.172  -19.023 1.00 25.26 ? 404  ALA A O     1 
ATOM   1801 C  CB    . ALA A 1 294 ? -24.135 22.593  -19.401 1.00 26.12 ? 404  ALA A CB    1 
ATOM   1802 N  N     . GLU A 1 295 ? -22.966 24.467  -17.022 1.00 24.12 ? 405  GLU A N     1 
ATOM   1803 C  CA    . GLU A 1 295 ? -23.028 25.806  -16.442 1.00 22.76 ? 405  GLU A CA    1 
ATOM   1804 C  C     . GLU A 1 295 ? -21.662 26.360  -16.042 1.00 22.57 ? 405  GLU A C     1 
ATOM   1805 O  O     . GLU A 1 295 ? -21.547 27.571  -15.816 1.00 23.21 ? 405  GLU A O     1 
ATOM   1806 C  CB    . GLU A 1 295 ? -23.971 25.793  -15.228 1.00 24.11 ? 405  GLU A CB    1 
ATOM   1807 C  CG    . GLU A 1 295 ? -25.473 25.763  -15.574 1.00 24.50 ? 405  GLU A CG    1 
ATOM   1808 C  CD    . GLU A 1 295 ? -26.034 24.368  -15.795 1.00 26.34 ? 405  GLU A CD    1 
ATOM   1809 O  OE1   . GLU A 1 295 ? -25.250 23.394  -15.856 1.00 27.14 ? 405  GLU A OE1   1 
ATOM   1810 O  OE2   . GLU A 1 295 ? -27.277 24.252  -15.915 1.00 27.10 ? 405  GLU A OE2   1 
ATOM   1811 N  N     . ALA A 1 296 ? -20.634 25.516  -15.944 1.00 21.49 ? 406  ALA A N     1 
ATOM   1812 C  CA    . ALA A 1 296 ? -19.296 25.992  -15.610 1.00 21.97 ? 406  ALA A CA    1 
ATOM   1813 C  C     . ALA A 1 296 ? -18.722 26.817  -16.765 1.00 24.41 ? 406  ALA A C     1 
ATOM   1814 O  O     . ALA A 1 296 ? -19.013 26.544  -17.934 1.00 27.83 ? 406  ALA A O     1 
ATOM   1815 C  CB    . ALA A 1 296 ? -18.375 24.813  -15.301 1.00 21.95 ? 406  ALA A CB    1 
ATOM   1816 N  N     . PRO A 1 297 ? -17.919 27.846  -16.465 1.00 23.67 ? 407  PRO A N     1 
ATOM   1817 C  CA    . PRO A 1 297 ? -17.340 28.661  -17.542 1.00 25.48 ? 407  PRO A CA    1 
ATOM   1818 C  C     . PRO A 1 297 ? -16.396 27.838  -18.407 1.00 32.48 ? 407  PRO A C     1 
ATOM   1819 O  O     . PRO A 1 297 ? -15.771 26.881  -17.945 1.00 33.18 ? 407  PRO A O     1 
ATOM   1820 C  CB    . PRO A 1 297 ? -16.581 29.772  -16.794 1.00 25.83 ? 407  PRO A CB    1 
ATOM   1821 C  CG    . PRO A 1 297 ? -17.022 29.707  -15.367 1.00 23.72 ? 407  PRO A CG    1 
ATOM   1822 C  CD    . PRO A 1 297 ? -17.495 28.299  -15.130 1.00 21.60 ? 407  PRO A CD    1 
ATOM   1823 N  N     . GLY A 1 298 ? -16.284 28.228  -19.669 1.00 37.08 ? 408  GLY A N     1 
ATOM   1824 C  CA    . GLY A 1 298 ? -15.413 27.546  -20.602 1.00 40.56 ? 408  GLY A CA    1 
ATOM   1825 C  C     . GLY A 1 298 ? -16.194 26.818  -21.688 1.00 43.53 ? 408  GLY A C     1 
ATOM   1826 O  O     . GLY A 1 298 ? -17.393 26.545  -21.566 1.00 41.91 ? 408  GLY A O     1 
ATOM   1827 N  N     . GLU A 1 299 ? -15.487 26.501  -22.770 1.00 46.15 ? 409  GLU A N     1 
ATOM   1828 C  CA    . GLU A 1 299 ? -16.076 25.863  -23.939 1.00 48.84 ? 409  GLU A CA    1 
ATOM   1829 C  C     . GLU A 1 299 ? -15.813 24.362  -23.933 1.00 47.46 ? 409  GLU A C     1 
ATOM   1830 O  O     . GLU A 1 299 ? -14.804 23.888  -23.403 1.00 46.61 ? 409  GLU A O     1 
ATOM   1831 C  CB    . GLU A 1 299 ? -15.517 26.468  -25.228 1.00 52.66 ? 409  GLU A CB    1 
ATOM   1832 C  CG    . GLU A 1 299 ? -15.542 27.985  -25.270 1.00 55.42 ? 409  GLU A CG    1 
ATOM   1833 C  CD    . GLU A 1 299 ? -14.558 28.547  -26.279 1.00 57.91 ? 409  GLU A CD    1 
ATOM   1834 O  OE1   . GLU A 1 299 ? -13.961 27.748  -27.035 1.00 59.10 ? 409  GLU A OE1   1 
ATOM   1835 O  OE2   . GLU A 1 299 ? -14.371 29.782  -26.310 1.00 58.54 ? 409  GLU A OE2   1 
ATOM   1836 N  N     . LEU A 1 300 ? -16.728 23.617  -24.547 1.00 47.36 ? 410  LEU A N     1 
ATOM   1837 C  CA    . LEU A 1 300 ? -16.548 22.179  -24.672 1.00 47.65 ? 410  LEU A CA    1 
ATOM   1838 C  C     . LEU A 1 300 ? -15.296 21.881  -25.491 1.00 48.02 ? 410  LEU A C     1 
ATOM   1839 O  O     . LEU A 1 300 ? -14.893 22.661  -26.359 1.00 49.04 ? 410  LEU A O     1 
ATOM   1840 C  CB    . LEU A 1 300 ? -17.785 21.549  -25.318 1.00 48.69 ? 410  LEU A CB    1 
ATOM   1841 C  CG    . LEU A 1 300 ? -18.039 20.062  -25.073 1.00 49.87 ? 410  LEU A CG    1 
ATOM   1842 C  CD1   . LEU A 1 300 ? -17.841 19.728  -23.606 1.00 51.14 ? 410  LEU A CD1   1 
ATOM   1843 C  CD2   . LEU A 1 300 ? -19.446 19.689  -25.512 1.00 49.35 ? 410  LEU A CD2   1 
ATOM   1844 N  N     . ILE A 1 301 ? -14.663 20.748  -25.192 1.00 47.62 ? 411  ILE A N     1 
ATOM   1845 C  CA    . ILE A 1 301 ? -13.458 20.302  -25.884 1.00 48.41 ? 411  ILE A CA    1 
ATOM   1846 C  C     . ILE A 1 301 ? -13.732 18.913  -26.441 1.00 49.54 ? 411  ILE A C     1 
ATOM   1847 O  O     . ILE A 1 301 ? -13.774 17.933  -25.686 1.00 49.28 ? 411  ILE A O     1 
ATOM   1848 C  CB    . ILE A 1 301 ? -12.229 20.283  -24.965 1.00 47.60 ? 411  ILE A CB    1 
ATOM   1849 C  CG1   . ILE A 1 301 ? -11.965 21.669  -24.373 1.00 47.37 ? 411  ILE A CG1   1 
ATOM   1850 C  CG2   . ILE A 1 301 ? -11.011 19.782  -25.722 1.00 47.45 ? 411  ILE A CG2   1 
ATOM   1851 C  CD1   . ILE A 1 301 ? -10.843 21.678  -23.352 1.00 46.64 ? 411  ILE A CD1   1 
ATOM   1852 N  N     . PHE A 1 302 ? -13.927 18.825  -27.755 1.00 52.17 ? 412  PHE A N     1 
ATOM   1853 C  CA    . PHE A 1 302 ? -14.083 17.548  -28.443 1.00 54.28 ? 412  PHE A CA    1 
ATOM   1854 C  C     . PHE A 1 302 ? -12.700 17.075  -28.878 1.00 58.07 ? 412  PHE A C     1 
ATOM   1855 O  O     . PHE A 1 302 ? -12.096 17.653  -29.788 1.00 58.50 ? 412  PHE A O     1 
ATOM   1856 C  CB    . PHE A 1 302 ? -15.011 17.682  -29.650 1.00 52.05 ? 412  PHE A CB    1 
ATOM   1857 C  CG    . PHE A 1 302 ? -16.455 17.948  -29.297 1.00 49.87 ? 412  PHE A CG    1 
ATOM   1858 C  CD1   . PHE A 1 302 ? -17.412 16.952  -29.434 1.00 48.66 ? 412  PHE A CD1   1 
ATOM   1859 C  CD2   . PHE A 1 302 ? -16.857 19.197  -28.854 1.00 47.92 ? 412  PHE A CD2   1 
ATOM   1860 C  CE1   . PHE A 1 302 ? -18.733 17.193  -29.127 1.00 48.08 ? 412  PHE A CE1   1 
ATOM   1861 C  CE2   . PHE A 1 302 ? -18.181 19.447  -28.543 1.00 47.12 ? 412  PHE A CE2   1 
ATOM   1862 C  CZ    . PHE A 1 302 ? -19.122 18.443  -28.678 1.00 47.78 ? 412  PHE A CZ    1 
ATOM   1863 N  N     . VAL A 1 303 ? -12.194 16.031  -28.231 1.00 61.38 ? 413  VAL A N     1 
ATOM   1864 C  CA    . VAL A 1 303 ? -10.898 15.460  -28.579 1.00 64.10 ? 413  VAL A CA    1 
ATOM   1865 C  C     . VAL A 1 303 ? -11.025 13.943  -28.569 1.00 65.91 ? 413  VAL A C     1 
ATOM   1866 O  O     . VAL A 1 303 ? -11.517 13.361  -27.597 1.00 65.80 ? 413  VAL A O     1 
ATOM   1867 C  CB    . VAL A 1 303 ? -9.782  15.931  -27.624 1.00 64.42 ? 413  VAL A CB    1 
ATOM   1868 C  CG1   . VAL A 1 303 ? -10.065 15.478  -26.201 1.00 65.32 ? 413  VAL A CG1   1 
ATOM   1869 C  CG2   . VAL A 1 303 ? -8.424  15.428  -28.097 1.00 64.17 ? 413  VAL A CG2   1 
ATOM   1870 N  N     . ASN A 1 304 ? -10.600 13.310  -29.662 1.00 67.78 ? 414  ASN A N     1 
ATOM   1871 C  CA    . ASN A 1 304 ? -10.630 11.854  -29.804 1.00 68.85 ? 414  ASN A CA    1 
ATOM   1872 C  C     . ASN A 1 304 ? -12.019 11.289  -29.508 1.00 67.62 ? 414  ASN A C     1 
ATOM   1873 O  O     . ASN A 1 304 ? -12.178 10.292  -28.800 1.00 67.33 ? 414  ASN A O     1 
ATOM   1874 C  CB    . ASN A 1 304 ? -9.569  11.199  -28.920 1.00 70.75 ? 414  ASN A CB    1 
ATOM   1875 C  CG    . ASN A 1 304 ? -8.331  10.808  -29.697 1.00 72.35 ? 414  ASN A CG    1 
ATOM   1876 O  OD1   . ASN A 1 304 ? -8.423  10.275  -30.802 1.00 73.06 ? 414  ASN A OD1   1 
ATOM   1877 N  ND2   . ASN A 1 304 ? -7.162  11.079  -29.128 1.00 73.32 ? 414  ASN A ND2   1 
ATOM   1878 N  N     . GLY A 1 305 ? -13.038 11.937  -30.071 1.00 66.71 ? 415  GLY A N     1 
ATOM   1879 C  CA    . GLY A 1 305 ? -14.401 11.461  -29.963 1.00 64.78 ? 415  GLY A CA    1 
ATOM   1880 C  C     . GLY A 1 305 ? -15.066 11.656  -28.620 1.00 63.55 ? 415  GLY A C     1 
ATOM   1881 O  O     . GLY A 1 305 ? -16.280 11.439  -28.517 1.00 63.18 ? 415  GLY A O     1 
ATOM   1882 N  N     . LYS A 1 306 ? -14.325 12.049  -27.589 1.00 61.96 ? 416  LYS A N     1 
ATOM   1883 C  CA    . LYS A 1 306 ? -14.890 12.325  -26.277 1.00 59.80 ? 416  LYS A CA    1 
ATOM   1884 C  C     . LYS A 1 306 ? -14.849 13.822  -26.001 1.00 53.80 ? 416  LYS A C     1 
ATOM   1885 O  O     . LYS A 1 306 ? -14.148 14.581  -26.674 1.00 53.54 ? 416  LYS A O     1 
ATOM   1886 C  CB    . LYS A 1 306 ? -14.142 11.553  -25.184 1.00 62.35 ? 416  LYS A CB    1 
ATOM   1887 C  CG    . LYS A 1 306 ? -14.324 10.047  -25.275 1.00 64.60 ? 416  LYS A CG    1 
ATOM   1888 C  CD    . LYS A 1 306 ? -13.688 9.325   -24.100 1.00 66.23 ? 416  LYS A CD    1 
ATOM   1889 C  CE    . LYS A 1 306 ? -13.959 7.831   -24.168 1.00 68.11 ? 416  LYS A CE    1 
ATOM   1890 N  NZ    . LYS A 1 306 ? -13.249 7.079   -23.095 1.00 69.19 ? 416  LYS A NZ    1 
ATOM   1891 N  N     . GLN A 1 307 ? -15.611 14.241  -24.993 1.00 49.10 ? 417  GLN A N     1 
ATOM   1892 C  CA    . GLN A 1 307 ? -15.813 15.650  -24.682 1.00 44.06 ? 417  GLN A CA    1 
ATOM   1893 C  C     . GLN A 1 307 ? -15.267 15.963  -23.297 1.00 39.59 ? 417  GLN A C     1 
ATOM   1894 O  O     . GLN A 1 307 ? -15.452 15.178  -22.361 1.00 39.30 ? 417  GLN A O     1 
ATOM   1895 C  CB    . GLN A 1 307 ? -17.294 15.998  -24.749 1.00 43.21 ? 417  GLN A CB    1 
ATOM   1896 C  CG    . GLN A 1 307 ? -17.945 15.548  -26.042 1.00 44.17 ? 417  GLN A CG    1 
ATOM   1897 C  CD    . GLN A 1 307 ? -19.445 15.412  -25.920 1.00 45.03 ? 417  GLN A CD    1 
ATOM   1898 O  OE1   . GLN A 1 307 ? -19.948 14.619  -25.120 1.00 44.92 ? 417  GLN A OE1   1 
ATOM   1899 N  NE2   . GLN A 1 307 ? -20.173 16.184  -26.717 1.00 45.71 ? 417  GLN A NE2   1 
ATOM   1900 N  N     . TYR A 1 308 ? -14.602 17.116  -23.174 1.00 36.47 ? 418  TYR A N     1 
ATOM   1901 C  CA    . TYR A 1 308 ? -13.966 17.553  -21.935 1.00 35.10 ? 418  TYR A CA    1 
ATOM   1902 C  C     . TYR A 1 308 ? -14.181 19.051  -21.748 1.00 33.48 ? 418  TYR A C     1 
ATOM   1903 O  O     . TYR A 1 308 ? -14.684 19.745  -22.635 1.00 32.81 ? 418  TYR A O     1 
ATOM   1904 C  CB    . TYR A 1 308 ? -12.461 17.260  -21.936 1.00 36.00 ? 418  TYR A CB    1 
ATOM   1905 C  CG    . TYR A 1 308 ? -12.097 15.815  -22.175 1.00 38.32 ? 418  TYR A CG    1 
ATOM   1906 C  CD1   . TYR A 1 308 ? -11.887 15.338  -23.462 1.00 39.55 ? 418  TYR A CD1   1 
ATOM   1907 C  CD2   . TYR A 1 308 ? -11.948 14.931  -21.115 1.00 39.80 ? 418  TYR A CD2   1 
ATOM   1908 C  CE1   . TYR A 1 308 ? -11.547 14.021  -23.687 1.00 41.07 ? 418  TYR A CE1   1 
ATOM   1909 C  CE2   . TYR A 1 308 ? -11.610 13.608  -21.330 1.00 41.79 ? 418  TYR A CE2   1 
ATOM   1910 C  CZ    . TYR A 1 308 ? -11.412 13.158  -22.620 1.00 42.80 ? 418  TYR A CZ    1 
ATOM   1911 O  OH    . TYR A 1 308 ? -11.073 11.844  -22.855 1.00 44.86 ? 418  TYR A OH    1 
ATOM   1912 N  N     . LYS A 1 309 ? -13.776 19.552  -20.576 1.00 30.97 ? 419  LYS A N     1 
ATOM   1913 C  CA    . LYS A 1 309 ? -13.725 20.984  -20.309 1.00 29.63 ? 419  LYS A CA    1 
ATOM   1914 C  C     . LYS A 1 309 ? -12.499 21.295  -19.463 1.00 27.24 ? 419  LYS A C     1 
ATOM   1915 O  O     . LYS A 1 309 ? -12.053 20.468  -18.665 1.00 28.23 ? 419  LYS A O     1 
ATOM   1916 C  CB    . LYS A 1 309 ? -14.986 21.497  -19.597 1.00 31.86 ? 419  LYS A CB    1 
ATOM   1917 C  CG    . LYS A 1 309 ? -16.205 21.554  -20.505 1.00 34.03 ? 419  LYS A CG    1 
ATOM   1918 C  CD    . LYS A 1 309 ? -17.424 22.121  -19.797 1.00 35.25 ? 419  LYS A CD    1 
ATOM   1919 C  CE    . LYS A 1 309 ? -17.306 23.622  -19.590 1.00 37.45 ? 419  LYS A CE    1 
ATOM   1920 N  NZ    . LYS A 1 309 ? -18.646 24.252  -19.387 1.00 38.02 ? 419  LYS A NZ    1 
ATOM   1921 N  N     . SER A 1 310 ? -11.972 22.507  -19.634 1.00 26.87 ? 420  SER A N     1 
ATOM   1922 C  CA    . SER A 1 310 ? -10.784 22.938  -18.902 1.00 27.48 ? 420  SER A CA    1 
ATOM   1923 C  C     . SER A 1 310 ? -11.066 23.130  -17.410 1.00 24.95 ? 420  SER A C     1 
ATOM   1924 O  O     . SER A 1 310 ? -12.131 23.618  -17.018 1.00 24.75 ? 420  SER A O     1 
ATOM   1925 C  CB    . SER A 1 310 ? -10.259 24.241  -19.505 1.00 31.01 ? 420  SER A CB    1 
ATOM   1926 O  OG    . SER A 1 310 ? -9.316  24.869  -18.652 1.00 35.14 ? 420  SER A OG    1 
ATOM   1927 N  N     . TYR A 1 311 ? -10.087 22.762  -16.574 1.00 21.02 ? 421  TYR A N     1 
ATOM   1928 C  CA    . TYR A 1 311 ? -10.165 22.924  -15.122 1.00 21.19 ? 421  TYR A CA    1 
ATOM   1929 C  C     . TYR A 1 311 ? -8.755  23.200  -14.602 1.00 21.62 ? 421  TYR A C     1 
ATOM   1930 O  O     . TYR A 1 311 ? -7.839  22.429  -14.905 1.00 22.92 ? 421  TYR A O     1 
ATOM   1931 C  CB    . TYR A 1 311 ? -10.772 21.670  -14.450 1.00 19.65 ? 421  TYR A CB    1 
ATOM   1932 C  CG    . TYR A 1 311 ? -10.881 21.757  -12.934 1.00 19.45 ? 421  TYR A CG    1 
ATOM   1933 C  CD1   . TYR A 1 311 ? -11.495 22.843  -12.318 1.00 19.09 ? 421  TYR A CD1   1 
ATOM   1934 C  CD2   . TYR A 1 311 ? -10.370 20.749  -12.117 1.00 18.68 ? 421  TYR A CD2   1 
ATOM   1935 C  CE1   . TYR A 1 311 ? -11.581 22.932  -10.933 1.00 18.14 ? 421  TYR A CE1   1 
ATOM   1936 C  CE2   . TYR A 1 311 ? -10.450 20.827  -10.735 1.00 18.14 ? 421  TYR A CE2   1 
ATOM   1937 C  CZ    . TYR A 1 311 ? -11.059 21.925  -10.145 1.00 17.26 ? 421  TYR A CZ    1 
ATOM   1938 O  OH    . TYR A 1 311 ? -11.143 22.015  -8.769  1.00 17.82 ? 421  TYR A OH    1 
ATOM   1939 N  N     . ARG A 1 312 ? -8.570  24.291  -13.840 1.00 19.58 ? 422  ARG A N     1 
ATOM   1940 C  CA    . ARG A 1 312 ? -7.224  24.717  -13.439 1.00 20.03 ? 422  ARG A CA    1 
ATOM   1941 C  C     . ARG A 1 312 ? -7.212  25.298  -12.027 1.00 19.35 ? 422  ARG A C     1 
ATOM   1942 O  O     . ARG A 1 312 ? -8.176  25.928  -11.585 1.00 20.10 ? 422  ARG A O     1 
ATOM   1943 C  CB    . ARG A 1 312 ? -6.649  25.759  -14.420 1.00 21.26 ? 422  ARG A CB    1 
ATOM   1944 C  CG    . ARG A 1 312 ? -7.304  27.132  -14.356 1.00 20.51 ? 422  ARG A CG    1 
ATOM   1945 C  CD    . ARG A 1 312 ? -6.697  28.085  -15.384 1.00 22.51 ? 422  ARG A CD    1 
ATOM   1946 N  NE    . ARG A 1 312 ? -7.244  29.440  -15.305 1.00 23.58 ? 422  ARG A NE    1 
ATOM   1947 C  CZ    . ARG A 1 312 ? -6.878  30.430  -16.110 1.00 25.16 ? 422  ARG A CZ    1 
ATOM   1948 N  NH1   . ARG A 1 312 ? -5.969  30.207  -17.055 1.00 27.85 ? 422  ARG A NH1   1 
ATOM   1949 N  NH2   . ARG A 1 312 ? -7.410  31.640  -15.973 1.00 24.60 ? 422  ARG A NH2   1 
ATOM   1950 N  N     . GLY A 1 313 ? -6.096  25.101  -11.322 1.00 19.81 ? 423  GLY A N     1 
ATOM   1951 C  CA    . GLY A 1 313 ? -5.936  25.727  -10.018 1.00 18.61 ? 423  GLY A CA    1 
ATOM   1952 C  C     . GLY A 1 313 ? -5.782  27.236  -10.122 1.00 19.15 ? 423  GLY A C     1 
ATOM   1953 O  O     . GLY A 1 313 ? -5.263  27.768  -11.107 1.00 21.24 ? 423  GLY A O     1 
ATOM   1954 N  N     . MET A 1 314 ? -6.253  27.945  -9.088  1.00 17.84 ? 424  MET A N     1 
ATOM   1955 C  CA    . MET A 1 314 ? -6.062  29.395  -9.044  1.00 19.00 ? 424  MET A CA    1 
ATOM   1956 C  C     . MET A 1 314 ? -4.626  29.794  -8.709  1.00 19.91 ? 424  MET A C     1 
ATOM   1957 O  O     . MET A 1 314 ? -4.286  30.985  -8.828  1.00 21.31 ? 424  MET A O     1 
ATOM   1958 C  CB    . MET A 1 314 ? -7.042  30.032  -8.047  1.00 20.22 ? 424  MET A CB    1 
ATOM   1959 C  CG    . MET A 1 314 ? -8.520  29.805  -8.407  1.00 19.71 ? 424  MET A CG    1 
ATOM   1960 S  SD    . MET A 1 314 ? -8.920  30.297  -10.105 1.00 25.53 ? 424  MET A SD    1 
ATOM   1961 C  CE    . MET A 1 314 ? -8.652  32.057  -10.008 1.00 26.68 ? 424  MET A CE    1 
ATOM   1962 N  N     . GLY A 1 315 ? -3.783  28.835  -8.301  1.00 18.45 ? 425  GLY A N     1 
ATOM   1963 C  CA    . GLY A 1 315 ? -2.353  29.040  -8.126  1.00 17.88 ? 425  GLY A CA    1 
ATOM   1964 C  C     . GLY A 1 315 ? -1.522  28.434  -9.245  1.00 19.97 ? 425  GLY A C     1 
ATOM   1965 O  O     . GLY A 1 315 ? -0.306  28.262  -9.094  1.00 20.68 ? 425  GLY A O     1 
ATOM   1966 N  N     . SER A 1 316 ? -2.159  28.099  -10.370 1.00 20.34 ? 426  SER A N     1 
ATOM   1967 C  CA    . SER A 1 316 ? -1.448  27.664  -11.570 1.00 21.02 ? 426  SER A CA    1 
ATOM   1968 C  C     . SER A 1 316 ? -0.834  28.858  -12.308 1.00 23.20 ? 426  SER A C     1 
ATOM   1969 O  O     . SER A 1 316 ? -1.240  30.009  -12.133 1.00 23.80 ? 426  SER A O     1 
ATOM   1970 C  CB    . SER A 1 316 ? -2.383  26.901  -12.522 1.00 22.08 ? 426  SER A CB    1 
ATOM   1971 O  OG    . SER A 1 316 ? -3.381  27.744  -13.093 1.00 22.16 ? 426  SER A OG    1 
ATOM   1972 N  N     . LEU A 1 317 ? 0.159   28.562  -13.155 1.00 24.96 ? 427  LEU A N     1 
ATOM   1973 C  CA    . LEU A 1 317 ? 0.826   29.615  -13.917 1.00 28.69 ? 427  LEU A CA    1 
ATOM   1974 C  C     . LEU A 1 317 ? -0.165  30.391  -14.784 1.00 29.28 ? 427  LEU A C     1 
ATOM   1975 O  O     . LEU A 1 317 ? -0.091  31.621  -14.875 1.00 30.36 ? 427  LEU A O     1 
ATOM   1976 C  CB    . LEU A 1 317 ? 1.941   29.000  -14.767 1.00 32.54 ? 427  LEU A CB    1 
ATOM   1977 C  CG    . LEU A 1 317 ? 3.091   29.864  -15.269 1.00 37.66 ? 427  LEU A CG    1 
ATOM   1978 C  CD1   . LEU A 1 317 ? 3.628   30.742  -14.152 1.00 39.67 ? 427  LEU A CD1   1 
ATOM   1979 C  CD2   . LEU A 1 317 ? 4.176   28.944  -15.796 1.00 37.43 ? 427  LEU A CD2   1 
ATOM   1980 N  N     . GLY A 1 318 ? -1.117  29.693  -15.409 1.00 29.12 ? 428  GLY A N     1 
ATOM   1981 C  CA    . GLY A 1 318 ? -2.072  30.370  -16.278 1.00 29.11 ? 428  GLY A CA    1 
ATOM   1982 C  C     . GLY A 1 318 ? -3.051  31.261  -15.532 1.00 29.03 ? 428  GLY A C     1 
ATOM   1983 O  O     . GLY A 1 318 ? -3.447  32.319  -16.033 1.00 30.86 ? 428  GLY A O     1 
ATOM   1984 N  N     . ALA A 1 319 ? -3.472  30.844  -14.335 1.00 28.35 ? 429  ALA A N     1 
ATOM   1985 C  CA    . ALA A 1 319 ? -4.387  31.673  -13.556 1.00 28.51 ? 429  ALA A CA    1 
ATOM   1986 C  C     . ALA A 1 319 ? -3.674  32.892  -12.982 1.00 33.63 ? 429  ALA A C     1 
ATOM   1987 O  O     . ALA A 1 319 ? -4.237  33.993  -12.959 1.00 34.53 ? 429  ALA A O     1 
ATOM   1988 C  CB    . ALA A 1 319 ? -5.035  30.849  -12.442 1.00 27.07 ? 429  ALA A CB    1 
ATOM   1989 N  N     . MET A 1 320 ? -2.433  32.720  -12.517 1.00 36.31 ? 430  MET A N     1 
ATOM   1990 C  CA    . MET A 1 320 ? -1.677  33.842  -11.973 1.00 41.02 ? 430  MET A CA    1 
ATOM   1991 C  C     . MET A 1 320 ? -1.293  34.854  -13.045 1.00 46.88 ? 430  MET A C     1 
ATOM   1992 O  O     . MET A 1 320 ? -0.879  35.968  -12.703 1.00 47.02 ? 430  MET A O     1 
ATOM   1993 C  CB    . MET A 1 320 ? -0.426  33.335  -11.239 1.00 40.24 ? 430  MET A CB    1 
ATOM   1994 C  CG    . MET A 1 320 ? -0.732  32.432  -10.035 1.00 41.79 ? 430  MET A CG    1 
ATOM   1995 S  SD    . MET A 1 320 ? 0.649   32.060  -8.919  1.00 44.70 ? 430  MET A SD    1 
ATOM   1996 C  CE    . MET A 1 320 ? 1.801   31.291  -10.049 1.00 43.50 ? 430  MET A CE    1 
ATOM   1997 N  N     . ARG A 1 321 ? -1.431  34.500  -14.320 1.00 52.86 ? 431  ARG A N     1 
ATOM   1998 C  CA    . ARG A 1 321 ? -1.189  35.427  -15.423 1.00 58.16 ? 431  ARG A CA    1 
ATOM   1999 C  C     . ARG A 1 321 ? -2.487  35.713  -16.174 1.00 59.34 ? 431  ARG A C     1 
ATOM   2000 O  O     . ARG A 1 321 ? -3.002  36.832  -16.151 1.00 60.08 ? 431  ARG A O     1 
ATOM   2001 C  CB    . ARG A 1 321 ? -0.142  34.860  -16.384 1.00 61.60 ? 431  ARG A CB    1 
ATOM   2002 C  CG    . ARG A 1 321 ? 1.220   34.617  -15.755 1.00 65.31 ? 431  ARG A CG    1 
ATOM   2003 C  CD    . ARG A 1 321 ? 2.153   33.874  -16.706 1.00 68.33 ? 431  ARG A CD    1 
ATOM   2004 N  NE    . ARG A 1 321 ? 3.533   33.865  -16.224 1.00 71.18 ? 431  ARG A NE    1 
ATOM   2005 C  CZ    . ARG A 1 321 ? 4.528   33.194  -16.800 1.00 73.36 ? 431  ARG A CZ    1 
ATOM   2006 N  NH1   . ARG A 1 321 ? 4.300   32.464  -17.884 1.00 73.62 ? 431  ARG A NH1   1 
ATOM   2007 N  NH2   . ARG A 1 321 ? 5.752   33.251  -16.288 1.00 74.29 ? 431  ARG A NH2   1 
ATOM   2008 N  N     . LEU A 1 345 ? 5.766   34.232  -6.907  1.00 43.87 ? 455  LEU A N     1 
ATOM   2009 C  CA    . LEU A 1 345 ? 5.471   32.914  -6.341  1.00 41.26 ? 455  LEU A CA    1 
ATOM   2010 C  C     . LEU A 1 345 ? 5.607   31.800  -7.359  1.00 37.50 ? 455  LEU A C     1 
ATOM   2011 O  O     . LEU A 1 345 ? 5.168   31.937  -8.500  1.00 40.96 ? 455  LEU A O     1 
ATOM   2012 C  CB    . LEU A 1 345 ? 4.057   32.869  -5.774  1.00 43.87 ? 455  LEU A CB    1 
ATOM   2013 C  CG    . LEU A 1 345 ? 3.732   33.897  -4.704  1.00 47.66 ? 455  LEU A CG    1 
ATOM   2014 C  CD1   . LEU A 1 345 ? 2.278   33.754  -4.308  1.00 48.86 ? 455  LEU A CD1   1 
ATOM   2015 C  CD2   . LEU A 1 345 ? 4.670   33.715  -3.517  1.00 47.95 ? 455  LEU A CD2   1 
ATOM   2016 N  N     . VAL A 1 346 ? 6.184   30.678  -6.939  1.00 29.51 ? 456  VAL A N     1 
ATOM   2017 C  CA    . VAL A 1 346 ? 6.191   29.494  -7.789  1.00 25.86 ? 456  VAL A CA    1 
ATOM   2018 C  C     . VAL A 1 346 ? 4.780   28.913  -7.760  1.00 22.83 ? 456  VAL A C     1 
ATOM   2019 O  O     . VAL A 1 346 ? 4.080   29.030  -6.742  1.00 23.84 ? 456  VAL A O     1 
ATOM   2020 C  CB    . VAL A 1 346 ? 7.253   28.482  -7.332  1.00 26.88 ? 456  VAL A CB    1 
ATOM   2021 C  CG1   . VAL A 1 346 ? 8.642   29.129  -7.359  1.00 27.74 ? 456  VAL A CG1   1 
ATOM   2022 C  CG2   . VAL A 1 346 ? 6.940   27.964  -5.944  1.00 26.79 ? 456  VAL A CG2   1 
ATOM   2023 N  N     . PRO A 1 347 ? 4.311   28.307  -8.846  1.00 21.80 ? 457  PRO A N     1 
ATOM   2024 C  CA    . PRO A 1 347 ? 2.931   27.796  -8.874  1.00 20.90 ? 457  PRO A CA    1 
ATOM   2025 C  C     . PRO A 1 347 ? 2.703   26.654  -7.895  1.00 20.83 ? 457  PRO A C     1 
ATOM   2026 O  O     . PRO A 1 347 ? 3.612   25.872  -7.596  1.00 22.09 ? 457  PRO A O     1 
ATOM   2027 C  CB    . PRO A 1 347 ? 2.759   27.311  -10.319 1.00 23.74 ? 457  PRO A CB    1 
ATOM   2028 C  CG    . PRO A 1 347 ? 3.834   27.989  -11.088 1.00 25.34 ? 457  PRO A CG    1 
ATOM   2029 C  CD    . PRO A 1 347 ? 4.980   28.178  -10.150 1.00 23.90 ? 457  PRO A CD    1 
ATOM   2030 N  N     . GLU A 1 348 ? 1.446   26.545  -7.421  1.00 18.67 ? 458  GLU A N     1 
ATOM   2031 C  CA    . GLU A 1 348 ? 1.004   25.463  -6.537  1.00 17.08 ? 458  GLU A CA    1 
ATOM   2032 C  C     . GLU A 1 348 ? -0.278  24.812  -7.056  1.00 18.05 ? 458  GLU A C     1 
ATOM   2033 O  O     . GLU A 1 348 ? -1.040  24.225  -6.278  1.00 18.28 ? 458  GLU A O     1 
ATOM   2034 C  CB    . GLU A 1 348 ? 0.808   25.950  -5.095  1.00 16.74 ? 458  GLU A CB    1 
ATOM   2035 C  CG    . GLU A 1 348 ? 2.127   26.346  -4.367  1.00 17.76 ? 458  GLU A CG    1 
ATOM   2036 C  CD    . GLU A 1 348 ? 1.916   26.844  -2.928  1.00 19.58 ? 458  GLU A CD    1 
ATOM   2037 O  OE1   . GLU A 1 348 ? 1.087   26.255  -2.181  1.00 19.40 ? 458  GLU A OE1   1 
ATOM   2038 O  OE2   . GLU A 1 348 ? 2.578   27.840  -2.549  1.00 19.94 ? 458  GLU A OE2   1 
ATOM   2039 N  N     . GLY A 1 349 ? -0.511  24.886  -8.371  1.00 17.47 ? 459  GLY A N     1 
ATOM   2040 C  CA    . GLY A 1 349 ? -1.613  24.188  -9.011  1.00 20.27 ? 459  GLY A CA    1 
ATOM   2041 C  C     . GLY A 1 349 ? -1.274  23.869  -10.454 1.00 22.40 ? 459  GLY A C     1 
ATOM   2042 O  O     . GLY A 1 349 ? -0.299  24.382  -11.012 1.00 22.52 ? 459  GLY A O     1 
ATOM   2043 N  N     . ILE A 1 350 ? -2.087  22.999  -11.059 1.00 23.57 ? 460  ILE A N     1 
ATOM   2044 C  CA    . ILE A 1 350 ? -1.895  22.577  -12.443 1.00 25.70 ? 460  ILE A CA    1 
ATOM   2045 C  C     . ILE A 1 350 ? -3.066  23.056  -13.300 1.00 24.42 ? 460  ILE A C     1 
ATOM   2046 O  O     . ILE A 1 350 ? -4.113  23.464  -12.798 1.00 23.29 ? 460  ILE A O     1 
ATOM   2047 C  CB    . ILE A 1 350 ? -1.737  21.050  -12.585 1.00 28.68 ? 460  ILE A CB    1 
ATOM   2048 C  CG1   . ILE A 1 350 ? -3.049  20.341  -12.225 1.00 30.61 ? 460  ILE A CG1   1 
ATOM   2049 C  CG2   . ILE A 1 350 ? -0.582  20.544  -11.747 1.00 31.39 ? 460  ILE A CG2   1 
ATOM   2050 C  CD1   . ILE A 1 350 ? -3.086  18.873  -12.626 1.00 32.58 ? 460  ILE A CD1   1 
ATOM   2051 N  N     . GLU A 1 351 ? -2.870  22.979  -14.617 1.00 24.35 ? 461  GLU A N     1 
ATOM   2052 C  CA    . GLU A 1 351 ? -3.904  23.257  -15.605 1.00 28.39 ? 461  GLU A CA    1 
ATOM   2053 C  C     . GLU A 1 351 ? -4.219  21.969  -16.351 1.00 28.18 ? 461  GLU A C     1 
ATOM   2054 O  O     . GLU A 1 351 ? -3.312  21.328  -16.895 1.00 29.86 ? 461  GLU A O     1 
ATOM   2055 C  CB    . GLU A 1 351 ? -3.451  24.343  -16.587 1.00 32.75 ? 461  GLU A CB    1 
ATOM   2056 C  CG    . GLU A 1 351 ? -2.885  25.583  -15.918 1.00 36.20 ? 461  GLU A CG    1 
ATOM   2057 C  CD    . GLU A 1 351 ? -2.182  26.524  -16.889 1.00 38.73 ? 461  GLU A CD    1 
ATOM   2058 O  OE1   . GLU A 1 351 ? -2.737  26.798  -17.979 1.00 40.65 ? 461  GLU A OE1   1 
ATOM   2059 O  OE2   . GLU A 1 351 ? -1.069  26.986  -16.556 1.00 38.11 ? 461  GLU A OE2   1 
ATOM   2060 N  N     . GLY A 1 352 ? -5.488  21.585  -16.371 1.00 27.91 ? 462  GLY A N     1 
ATOM   2061 C  CA    . GLY A 1 352 ? -5.888  20.306  -16.932 1.00 29.80 ? 462  GLY A CA    1 
ATOM   2062 C  C     . GLY A 1 352 ? -7.293  20.324  -17.495 1.00 30.41 ? 462  GLY A C     1 
ATOM   2063 O  O     . GLY A 1 352 ? -7.791  21.366  -17.933 1.00 29.92 ? 462  GLY A O     1 
ATOM   2064 N  N     . ARG A 1 353 ? -7.930  19.154  -17.489 1.00 32.42 ? 463  ARG A N     1 
ATOM   2065 C  CA    . ARG A 1 353 ? -9.256  18.988  -18.062 1.00 34.91 ? 463  ARG A CA    1 
ATOM   2066 C  C     . ARG A 1 353 ? -9.981  17.871  -17.325 1.00 34.14 ? 463  ARG A C     1 
ATOM   2067 O  O     . ARG A 1 353 ? -9.363  17.020  -16.682 1.00 35.10 ? 463  ARG A O     1 
ATOM   2068 C  CB    . ARG A 1 353 ? -9.178  18.680  -19.562 1.00 38.07 ? 463  ARG A CB    1 
ATOM   2069 C  CG    . ARG A 1 353 ? -8.667  17.286  -19.868 1.00 42.42 ? 463  ARG A CG    1 
ATOM   2070 C  CD    . ARG A 1 353 ? -8.349  17.112  -21.346 1.00 46.37 ? 463  ARG A CD    1 
ATOM   2071 N  NE    . ARG A 1 353 ? -8.188  15.704  -21.706 1.00 51.21 ? 463  ARG A NE    1 
ATOM   2072 C  CZ    . ARG A 1 353 ? -7.576  15.277  -22.805 1.00 54.17 ? 463  ARG A CZ    1 
ATOM   2073 N  NH1   . ARG A 1 353 ? -7.050  16.150  -23.654 1.00 55.34 ? 463  ARG A NH1   1 
ATOM   2074 N  NH2   . ARG A 1 353 ? -7.482  13.977  -23.052 1.00 56.19 ? 463  ARG A NH2   1 
ATOM   2075 N  N     . VAL A 1 354 ? -11.307 17.890  -17.421 1.00 31.68 ? 464  VAL A N     1 
ATOM   2076 C  CA    . VAL A 1 354 ? -12.154 16.850  -16.838 1.00 29.87 ? 464  VAL A CA    1 
ATOM   2077 C  C     . VAL A 1 354 ? -13.201 16.449  -17.866 1.00 29.56 ? 464  VAL A C     1 
ATOM   2078 O  O     . VAL A 1 354 ? -13.525 17.221  -18.781 1.00 30.17 ? 464  VAL A O     1 
ATOM   2079 C  CB    . VAL A 1 354 ? -12.833 17.323  -15.532 1.00 29.10 ? 464  VAL A CB    1 
ATOM   2080 C  CG1   . VAL A 1 354 ? -11.794 17.630  -14.451 1.00 28.29 ? 464  VAL A CG1   1 
ATOM   2081 C  CG2   . VAL A 1 354 ? -13.710 18.539  -15.795 1.00 29.51 ? 464  VAL A CG2   1 
ATOM   2082 N  N     . PRO A 1 355 ? -13.757 15.247  -17.742 1.00 30.85 ? 465  PRO A N     1 
ATOM   2083 C  CA    . PRO A 1 355 ? -14.818 14.832  -18.668 1.00 31.67 ? 465  PRO A CA    1 
ATOM   2084 C  C     . PRO A 1 355 ? -16.066 15.694  -18.531 1.00 32.12 ? 465  PRO A C     1 
ATOM   2085 O  O     . PRO A 1 355 ? -16.406 16.172  -17.445 1.00 32.39 ? 465  PRO A O     1 
ATOM   2086 C  CB    . PRO A 1 355 ? -15.104 13.377  -18.269 1.00 33.13 ? 465  PRO A CB    1 
ATOM   2087 C  CG    . PRO A 1 355 ? -14.534 13.214  -16.909 1.00 34.68 ? 465  PRO A CG    1 
ATOM   2088 C  CD    . PRO A 1 355 ? -13.407 14.198  -16.773 1.00 32.22 ? 465  PRO A CD    1 
ATOM   2089 N  N     . PHE A 1 356 ? -16.744 15.891  -19.662 1.00 30.57 ? 466  PHE A N     1 
ATOM   2090 C  CA    . PHE A 1 356 ? -18.017 16.606  -19.685 1.00 30.63 ? 466  PHE A CA    1 
ATOM   2091 C  C     . PHE A 1 356 ? -19.108 15.770  -19.024 1.00 31.06 ? 466  PHE A C     1 
ATOM   2092 O  O     . PHE A 1 356 ? -19.229 14.568  -19.281 1.00 30.52 ? 466  PHE A O     1 
ATOM   2093 C  CB    . PHE A 1 356 ? -18.401 16.940  -21.128 1.00 30.74 ? 466  PHE A CB    1 
ATOM   2094 C  CG    . PHE A 1 356 ? -19.699 17.694  -21.262 1.00 30.71 ? 466  PHE A CG    1 
ATOM   2095 C  CD1   . PHE A 1 356 ? -19.786 19.026  -20.892 1.00 31.13 ? 466  PHE A CD1   1 
ATOM   2096 C  CD2   . PHE A 1 356 ? -20.826 17.073  -21.787 1.00 31.06 ? 466  PHE A CD2   1 
ATOM   2097 C  CE1   . PHE A 1 356 ? -20.979 19.724  -21.024 1.00 32.39 ? 466  PHE A CE1   1 
ATOM   2098 C  CE2   . PHE A 1 356 ? -22.019 17.762  -21.918 1.00 31.27 ? 466  PHE A CE2   1 
ATOM   2099 C  CZ    . PHE A 1 356 ? -22.097 19.086  -21.540 1.00 31.82 ? 466  PHE A CZ    1 
ATOM   2100 N  N     . ARG A 1 357 ? -19.912 16.413  -18.171 1.00 31.47 ? 467  ARG A N     1 
ATOM   2101 C  CA    . ARG A 1 357 ? -20.888 15.701  -17.353 1.00 33.95 ? 467  ARG A CA    1 
ATOM   2102 C  C     . ARG A 1 357 ? -22.339 16.134  -17.543 1.00 30.67 ? 467  ARG A C     1 
ATOM   2103 O  O     . ARG A 1 357 ? -23.213 15.588  -16.861 1.00 32.59 ? 467  ARG A O     1 
ATOM   2104 C  CB    . ARG A 1 357 ? -20.522 15.830  -15.866 1.00 39.78 ? 467  ARG A CB    1 
ATOM   2105 C  CG    . ARG A 1 357 ? -19.369 14.932  -15.434 1.00 44.69 ? 467  ARG A CG    1 
ATOM   2106 C  CD    . ARG A 1 357 ? -19.846 13.516  -15.145 1.00 48.71 ? 467  ARG A CD    1 
ATOM   2107 N  NE    . ARG A 1 357 ? -18.765 12.542  -15.244 1.00 52.68 ? 467  ARG A NE    1 
ATOM   2108 C  CZ    . ARG A 1 357 ? -18.626 11.676  -16.246 1.00 55.59 ? 467  ARG A CZ    1 
ATOM   2109 N  NH1   . ARG A 1 357 ? -19.506 11.658  -17.241 1.00 57.12 ? 467  ARG A NH1   1 
ATOM   2110 N  NH2   . ARG A 1 357 ? -17.608 10.824  -16.254 1.00 55.26 ? 467  ARG A NH2   1 
ATOM   2111 N  N     . GLY A 1 358 ? -22.632 17.088  -18.425 1.00 26.69 ? 468  GLY A N     1 
ATOM   2112 C  CA    . GLY A 1 358 ? -24.007 17.467  -18.686 1.00 25.44 ? 468  GLY A CA    1 
ATOM   2113 C  C     . GLY A 1 358 ? -24.536 18.561  -17.772 1.00 24.72 ? 468  GLY A C     1 
ATOM   2114 O  O     . GLY A 1 358 ? -23.769 19.321  -17.170 1.00 24.94 ? 468  GLY A O     1 
ATOM   2115 N  N     . PRO A 1 359 ? -25.865 18.662  -17.654 1.00 23.79 ? 469  PRO A N     1 
ATOM   2116 C  CA    . PRO A 1 359 ? -26.457 19.753  -16.862 1.00 24.46 ? 469  PRO A CA    1 
ATOM   2117 C  C     . PRO A 1 359 ? -26.146 19.623  -15.380 1.00 25.00 ? 469  PRO A C     1 
ATOM   2118 O  O     . PRO A 1 359 ? -26.108 18.518  -14.829 1.00 27.04 ? 469  PRO A O     1 
ATOM   2119 C  CB    . PRO A 1 359 ? -27.965 19.604  -17.107 1.00 25.45 ? 469  PRO A CB    1 
ATOM   2120 C  CG    . PRO A 1 359 ? -28.105 18.686  -18.251 1.00 27.37 ? 469  PRO A CG    1 
ATOM   2121 C  CD    . PRO A 1 359 ? -26.887 17.837  -18.321 1.00 24.78 ? 469  PRO A CD    1 
ATOM   2122 N  N     . LEU A 1 360 ? -25.959 20.776  -14.728 1.00 23.72 ? 470  LEU A N     1 
ATOM   2123 C  CA    . LEU A 1 360 ? -25.719 20.800  -13.285 1.00 25.26 ? 470  LEU A CA    1 
ATOM   2124 C  C     . LEU A 1 360 ? -26.832 20.092  -12.525 1.00 26.42 ? 470  LEU A C     1 
ATOM   2125 O  O     . LEU A 1 360 ? -26.571 19.319  -11.598 1.00 24.97 ? 470  LEU A O     1 
ATOM   2126 C  CB    . LEU A 1 360 ? -25.591 22.240  -12.777 1.00 26.14 ? 470  LEU A CB    1 
ATOM   2127 C  CG    . LEU A 1 360 ? -25.464 22.191  -11.249 1.00 28.25 ? 470  LEU A CG    1 
ATOM   2128 C  CD1   . LEU A 1 360 ? -24.022 21.970  -10.822 1.00 26.40 ? 470  LEU A CD1   1 
ATOM   2129 C  CD2   . LEU A 1 360 ? -26.079 23.366  -10.544 1.00 29.65 ? 470  LEU A CD2   1 
ATOM   2130 N  N     . SER A 1 361 ? -28.089 20.381  -12.880 1.00 28.50 ? 471  SER A N     1 
ATOM   2131 C  CA    . SER A 1 361 ? -29.213 19.817  -12.140 1.00 31.17 ? 471  SER A CA    1 
ATOM   2132 C  C     . SER A 1 361 ? -29.116 18.300  -12.059 1.00 31.02 ? 471  SER A C     1 
ATOM   2133 O  O     . SER A 1 361 ? -29.420 17.705  -11.017 1.00 31.90 ? 471  SER A O     1 
ATOM   2134 C  CB    . SER A 1 361 ? -30.534 20.247  -12.786 1.00 33.74 ? 471  SER A CB    1 
ATOM   2135 O  OG    . SER A 1 361 ? -30.664 19.707  -14.090 1.00 36.49 ? 471  SER A OG    1 
ATOM   2136 N  N     . SER A 1 362 ? -28.656 17.661  -13.137 1.00 30.18 ? 472  SER A N     1 
ATOM   2137 C  CA    . SER A 1 362 ? -28.525 16.207  -13.144 1.00 30.83 ? 472  SER A CA    1 
ATOM   2138 C  C     . SER A 1 362 ? -27.375 15.737  -12.253 1.00 29.16 ? 472  SER A C     1 
ATOM   2139 O  O     . SER A 1 362 ? -27.481 14.695  -11.591 1.00 29.77 ? 472  SER A O     1 
ATOM   2140 C  CB    . SER A 1 362 ? -28.333 15.710  -14.579 1.00 33.02 ? 472  SER A CB    1 
ATOM   2141 O  OG    . SER A 1 362 ? -29.448 16.045  -15.393 1.00 35.58 ? 472  SER A OG    1 
ATOM   2142 N  N     . VAL A 1 363 ? -26.265 16.477  -12.225 1.00 25.53 ? 473  VAL A N     1 
ATOM   2143 C  CA    . VAL A 1 363 ? -25.160 16.084  -11.355 1.00 22.42 ? 473  VAL A CA    1 
ATOM   2144 C  C     . VAL A 1 363 ? -25.560 16.214  -9.889  1.00 22.02 ? 473  VAL A C     1 
ATOM   2145 O  O     . VAL A 1 363 ? -25.285 15.322  -9.077  1.00 22.85 ? 473  VAL A O     1 
ATOM   2146 C  CB    . VAL A 1 363 ? -23.894 16.903  -11.675 1.00 23.44 ? 473  VAL A CB    1 
ATOM   2147 C  CG1   . VAL A 1 363 ? -22.842 16.694  -10.585 1.00 22.49 ? 473  VAL A CG1   1 
ATOM   2148 C  CG2   . VAL A 1 363 ? -23.329 16.515  -13.040 1.00 25.51 ? 473  VAL A CG2   1 
ATOM   2149 N  N     . ILE A 1 364 ? -26.218 17.318  -9.520  1.00 20.06 ? 474  ILE A N     1 
ATOM   2150 C  CA    . ILE A 1 364 ? -26.618 17.482  -8.122  1.00 20.58 ? 474  ILE A CA    1 
ATOM   2151 C  C     . ILE A 1 364 ? -27.609 16.396  -7.702  1.00 21.53 ? 474  ILE A C     1 
ATOM   2152 O  O     . ILE A 1 364 ? -27.589 15.941  -6.550  1.00 20.92 ? 474  ILE A O     1 
ATOM   2153 C  CB    . ILE A 1 364 ? -27.180 18.902  -7.876  1.00 22.57 ? 474  ILE A CB    1 
ATOM   2154 C  CG1   . ILE A 1 364 ? -26.117 19.973  -8.174  1.00 24.13 ? 474  ILE A CG1   1 
ATOM   2155 C  CG2   . ILE A 1 364 ? -27.678 19.045  -6.437  1.00 23.80 ? 474  ILE A CG2   1 
ATOM   2156 C  CD1   . ILE A 1 364 ? -24.968 20.051  -7.143  1.00 25.30 ? 474  ILE A CD1   1 
ATOM   2157 N  N     . HIS A 1 365 ? -28.478 15.947  -8.618  1.00 23.45 ? 475  HIS A N     1 
ATOM   2158 C  CA    . HIS A 1 365 ? -29.409 14.866  -8.285  1.00 25.11 ? 475  HIS A CA    1 
ATOM   2159 C  C     . HIS A 1 365 ? -28.670 13.580  -7.931  1.00 23.80 ? 475  HIS A C     1 
ATOM   2160 O  O     . HIS A 1 365 ? -29.054 12.871  -6.991  1.00 23.11 ? 475  HIS A O     1 
ATOM   2161 C  CB    . HIS A 1 365 ? -30.377 14.611  -9.447  1.00 29.25 ? 475  HIS A CB    1 
ATOM   2162 C  CG    . HIS A 1 365 ? -31.225 13.386  -9.270  1.00 35.76 ? 475  HIS A CG    1 
ATOM   2163 N  ND1   . HIS A 1 365 ? -32.407 13.395  -8.560  1.00 37.97 ? 475  HIS A ND1   1 
ATOM   2164 C  CD2   . HIS A 1 365 ? -31.056 12.112  -9.701  1.00 37.09 ? 475  HIS A CD2   1 
ATOM   2165 C  CE1   . HIS A 1 365 ? -32.929 12.181  -8.561  1.00 38.64 ? 475  HIS A CE1   1 
ATOM   2166 N  NE2   . HIS A 1 365 ? -32.129 11.384  -9.246  1.00 38.09 ? 475  HIS A NE2   1 
ATOM   2167 N  N     . GLN A 1 366 ? -27.620 13.247  -8.688  1.00 23.93 ? 476  GLN A N     1 
ATOM   2168 C  CA    . GLN A 1 366 ? -26.858 12.039  -8.384  1.00 25.25 ? 476  GLN A CA    1 
ATOM   2169 C  C     . GLN A 1 366 ? -26.109 12.176  -7.066  1.00 21.65 ? 476  GLN A C     1 
ATOM   2170 O  O     . GLN A 1 366 ? -26.058 11.226  -6.274  1.00 22.11 ? 476  GLN A O     1 
ATOM   2171 C  CB    . GLN A 1 366 ? -25.890 11.719  -9.524  1.00 28.46 ? 476  GLN A CB    1 
ATOM   2172 C  CG    . GLN A 1 366 ? -26.575 11.265  -10.809 1.00 32.88 ? 476  GLN A CG    1 
ATOM   2173 C  CD    . GLN A 1 366 ? -27.302 9.930   -10.651 1.00 36.36 ? 476  GLN A CD    1 
ATOM   2174 O  OE1   . GLN A 1 366 ? -26.717 8.934   -10.219 1.00 38.05 ? 476  GLN A OE1   1 
ATOM   2175 N  NE2   . GLN A 1 366 ? -28.588 9.914   -10.989 1.00 38.01 ? 476  GLN A NE2   1 
ATOM   2176 N  N     . LEU A 1 367 ? -25.527 13.355  -6.809  1.00 18.87 ? 477  LEU A N     1 
ATOM   2177 C  CA    . LEU A 1 367 ? -24.787 13.570  -5.566  1.00 18.32 ? 477  LEU A CA    1 
ATOM   2178 C  C     . LEU A 1 367 ? -25.705 13.489  -4.346  1.00 18.97 ? 477  LEU A C     1 
ATOM   2179 O  O     . LEU A 1 367 ? -25.377 12.824  -3.355  1.00 17.93 ? 477  LEU A O     1 
ATOM   2180 C  CB    . LEU A 1 367 ? -24.058 14.920  -5.606  1.00 18.80 ? 477  LEU A CB    1 
ATOM   2181 C  CG    . LEU A 1 367 ? -22.935 15.084  -6.637  1.00 18.47 ? 477  LEU A CG    1 
ATOM   2182 C  CD1   . LEU A 1 367 ? -22.396 16.525  -6.666  1.00 20.30 ? 477  LEU A CD1   1 
ATOM   2183 C  CD2   . LEU A 1 367 ? -21.798 14.086  -6.383  1.00 19.08 ? 477  LEU A CD2   1 
ATOM   2184 N  N     . THR A 1 368 ? -26.862 14.165  -4.387  1.00 18.87 ? 478  THR A N     1 
ATOM   2185 C  CA    . THR A 1 368 ? -27.776 14.091  -3.242  1.00 19.25 ? 478  THR A CA    1 
ATOM   2186 C  C     . THR A 1 368 ? -28.381 12.699  -3.093  1.00 18.90 ? 478  THR A C     1 
ATOM   2187 O  O     . THR A 1 368 ? -28.674 12.277  -1.969  1.00 18.17 ? 478  THR A O     1 
ATOM   2188 C  CB    . THR A 1 368 ? -28.886 15.142  -3.353  1.00 21.53 ? 478  THR A CB    1 
ATOM   2189 O  OG1   . THR A 1 368 ? -29.716 14.859  -4.481  1.00 26.78 ? 478  THR A OG1   1 
ATOM   2190 C  CG2   . THR A 1 368 ? -28.276 16.524  -3.511  1.00 18.30 ? 478  THR A CG2   1 
ATOM   2191 N  N     . GLY A 1 369 ? -28.564 11.964  -4.195  1.00 17.92 ? 479  GLY A N     1 
ATOM   2192 C  CA    . GLY A 1 369 ? -29.065 10.594  -4.080  1.00 19.71 ? 479  GLY A CA    1 
ATOM   2193 C  C     . GLY A 1 369 ? -28.109 9.678   -3.332  1.00 18.64 ? 479  GLY A C     1 
ATOM   2194 O  O     . GLY A 1 369 ? -28.534 8.814   -2.559  1.00 18.88 ? 479  GLY A O     1 
ATOM   2195 N  N     . GLY A 1 370 ? -26.804 9.849   -3.554  1.00 17.93 ? 480  GLY A N     1 
ATOM   2196 C  CA    . GLY A 1 370 ? -25.827 9.082   -2.795  1.00 17.28 ? 480  GLY A CA    1 
ATOM   2197 C  C     . GLY A 1 370 ? -25.815 9.444   -1.322  1.00 16.75 ? 480  GLY A C     1 
ATOM   2198 O  O     . GLY A 1 370 ? -25.712 8.564   -0.461  1.00 17.51 ? 480  GLY A O     1 
ATOM   2199 N  N     . LEU A 1 371 ? -25.902 10.745  -1.013  1.00 16.34 ? 481  LEU A N     1 
ATOM   2200 C  CA    . LEU A 1 371 ? -26.033 11.181  0.381   1.00 16.42 ? 481  LEU A CA    1 
ATOM   2201 C  C     . LEU A 1 371 ? -27.279 10.581  1.041   1.00 16.13 ? 481  LEU A C     1 
ATOM   2202 O  O     . LEU A 1 371 ? -27.214 10.095  2.181   1.00 16.57 ? 481  LEU A O     1 
ATOM   2203 C  CB    . LEU A 1 371 ? -26.059 12.718  0.456   1.00 17.25 ? 481  LEU A CB    1 
ATOM   2204 C  CG    . LEU A 1 371 ? -26.299 13.397  1.816   1.00 16.25 ? 481  LEU A CG    1 
ATOM   2205 C  CD1   . LEU A 1 371 ? -25.243 13.006  2.849   1.00 18.57 ? 481  LEU A CD1   1 
ATOM   2206 C  CD2   . LEU A 1 371 ? -26.349 14.921  1.683   1.00 16.39 ? 481  LEU A CD2   1 
ATOM   2207 N  N     . ARG A 1 372 ? -28.423 10.599  0.348   1.00 15.91 ? 482  ARG A N     1 
ATOM   2208 C  CA    . ARG A 1 372 ? -29.646 10.010  0.913   1.00 16.84 ? 482  ARG A CA    1 
ATOM   2209 C  C     . ARG A 1 372 ? -29.486 8.508   1.190   1.00 17.79 ? 482  ARG A C     1 
ATOM   2210 O  O     . ARG A 1 372 ? -30.010 8.001   2.191   1.00 16.94 ? 482  ARG A O     1 
ATOM   2211 C  CB    . ARG A 1 372 ? -30.845 10.272  -0.015  1.00 17.75 ? 482  ARG A CB    1 
ATOM   2212 C  CG    . ARG A 1 372 ? -31.352 11.711  -0.013  1.00 20.27 ? 482  ARG A CG    1 
ATOM   2213 C  CD    . ARG A 1 372 ? -32.544 11.908  -0.990  1.00 22.44 ? 482  ARG A CD    1 
ATOM   2214 N  NE    . ARG A 1 372 ? -33.067 13.262  -0.882  1.00 25.82 ? 482  ARG A NE    1 
ATOM   2215 C  CZ    . ARG A 1 372 ? -33.932 13.648  0.051   1.00 26.78 ? 482  ARG A CZ    1 
ATOM   2216 N  NH1   . ARG A 1 372 ? -34.383 12.761  0.930   1.00 28.82 ? 482  ARG A NH1   1 
ATOM   2217 N  NH2   . ARG A 1 372 ? -34.342 14.912  0.106   1.00 28.61 ? 482  ARG A NH2   1 
ATOM   2218 N  N     . ALA A 1 373 ? -28.767 7.777   0.325   1.00 15.84 ? 483  ALA A N     1 
ATOM   2219 C  CA    . ALA A 1 373 ? -28.510 6.354   0.590   1.00 17.10 ? 483  ALA A CA    1 
ATOM   2220 C  C     . ALA A 1 373 ? -27.729 6.167   1.890   1.00 16.80 ? 483  ALA A C     1 
ATOM   2221 O  O     . ALA A 1 373 ? -28.078 5.321   2.728   1.00 17.88 ? 483  ALA A O     1 
ATOM   2222 C  CB    . ALA A 1 373 ? -27.767 5.719   -0.589  1.00 18.26 ? 483  ALA A CB    1 
ATOM   2223 N  N     . ALA A 1 374 ? -26.662 6.957   2.076   1.00 14.69 ? 484  ALA A N     1 
ATOM   2224 C  CA    . ALA A 1 374 ? -25.882 6.891   3.307   1.00 14.82 ? 484  ALA A CA    1 
ATOM   2225 C  C     . ALA A 1 374 ? -26.740 7.193   4.534   1.00 14.98 ? 484  ALA A C     1 
ATOM   2226 O  O     . ALA A 1 374 ? -26.541 6.593   5.598   1.00 16.24 ? 484  ALA A O     1 
ATOM   2227 C  CB    . ALA A 1 374 ? -24.700 7.857   3.228   1.00 16.38 ? 484  ALA A CB    1 
ATOM   2228 N  N     . MET A 1 375 ? -27.703 8.120   4.412   1.00 15.32 ? 485  MET A N     1 
ATOM   2229 C  CA    . MET A 1 375 ? -28.536 8.435   5.572   1.00 16.53 ? 485  MET A CA    1 
ATOM   2230 C  C     . MET A 1 375 ? -29.462 7.262   5.915   1.00 16.87 ? 485  MET A C     1 
ATOM   2231 O  O     . MET A 1 375 ? -29.696 6.970   7.097   1.00 16.64 ? 485  MET A O     1 
ATOM   2232 C  CB    . MET A 1 375 ? -29.312 9.742   5.325   1.00 16.04 ? 485  MET A CB    1 
ATOM   2233 C  CG    . MET A 1 375 ? -28.367 10.979  5.162   1.00 16.27 ? 485  MET A CG    1 
ATOM   2234 S  SD    . MET A 1 375 ? -29.177 12.561  4.774   1.00 16.81 ? 485  MET A SD    1 
ATOM   2235 C  CE    . MET A 1 375 ? -29.918 12.968  6.354   1.00 19.26 ? 485  MET A CE    1 
ATOM   2236 N  N     . GLY A 1 376 ? -29.958 6.546   4.900   1.00 16.76 ? 486  GLY A N     1 
ATOM   2237 C  CA    . GLY A 1 376 ? -30.703 5.315   5.161   1.00 16.15 ? 486  GLY A CA    1 
ATOM   2238 C  C     . GLY A 1 376 ? -29.877 4.241   5.866   1.00 15.75 ? 486  GLY A C     1 
ATOM   2239 O  O     . GLY A 1 376 ? -30.329 3.628   6.846   1.00 16.11 ? 486  GLY A O     1 
ATOM   2240 N  N     . TYR A 1 377 ? -28.659 3.980   5.365   1.00 14.79 ? 487  TYR A N     1 
ATOM   2241 C  CA    . TYR A 1 377 ? -27.803 2.937   5.950   1.00 14.97 ? 487  TYR A CA    1 
ATOM   2242 C  C     . TYR A 1 377 ? -27.408 3.243   7.398   1.00 16.71 ? 487  TYR A C     1 
ATOM   2243 O  O     . TYR A 1 377 ? -27.217 2.313   8.199   1.00 16.35 ? 487  TYR A O     1 
ATOM   2244 C  CB    . TYR A 1 377 ? -26.514 2.752   5.122   1.00 15.24 ? 487  TYR A CB    1 
ATOM   2245 C  CG    . TYR A 1 377 ? -26.650 2.001   3.807   1.00 15.70 ? 487  TYR A CG    1 
ATOM   2246 C  CD1   . TYR A 1 377 ? -26.997 0.639   3.778   1.00 16.43 ? 487  TYR A CD1   1 
ATOM   2247 C  CD2   . TYR A 1 377 ? -26.393 2.636   2.585   1.00 15.95 ? 487  TYR A CD2   1 
ATOM   2248 C  CE1   . TYR A 1 377 ? -27.106 -0.056  2.567   1.00 17.23 ? 487  TYR A CE1   1 
ATOM   2249 C  CE2   . TYR A 1 377 ? -26.495 1.947   1.374   1.00 16.61 ? 487  TYR A CE2   1 
ATOM   2250 C  CZ    . TYR A 1 377 ? -26.871 0.602   1.372   1.00 17.82 ? 487  TYR A CZ    1 
ATOM   2251 O  OH    . TYR A 1 377 ? -26.977 -0.086  0.185   1.00 18.41 ? 487  TYR A OH    1 
ATOM   2252 N  N     . THR A 1 378 ? -27.208 4.522   7.740   1.00 16.18 ? 488  THR A N     1 
ATOM   2253 C  CA    . THR A 1 378 ? -26.737 4.913   9.071   1.00 14.15 ? 488  THR A CA    1 
ATOM   2254 C  C     . THR A 1 378 ? -27.864 5.295   10.025  1.00 15.96 ? 488  THR A C     1 
ATOM   2255 O  O     . THR A 1 378 ? -27.584 5.601   11.189  1.00 16.31 ? 488  THR A O     1 
ATOM   2256 C  CB    . THR A 1 378 ? -25.725 6.087   8.985   1.00 14.25 ? 488  THR A CB    1 
ATOM   2257 O  OG1   . THR A 1 378 ? -26.358 7.251   8.426   1.00 16.36 ? 488  THR A OG1   1 
ATOM   2258 C  CG2   . THR A 1 378 ? -24.489 5.718   8.153   1.00 15.46 ? 488  THR A CG2   1 
ATOM   2259 N  N     . GLY A 1 379 ? -29.124 5.250   9.587   1.00 15.82 ? 489  GLY A N     1 
ATOM   2260 C  CA    . GLY A 1 379 ? -30.230 5.614   10.461  1.00 16.21 ? 489  GLY A CA    1 
ATOM   2261 C  C     . GLY A 1 379 ? -30.297 7.086   10.819  1.00 17.37 ? 489  GLY A C     1 
ATOM   2262 O  O     . GLY A 1 379 ? -30.689 7.427   11.943  1.00 19.29 ? 489  GLY A O     1 
ATOM   2263 N  N     . SER A 1 380 ? -29.942 7.967   9.883   1.00 17.02 ? 490  SER A N     1 
ATOM   2264 C  CA    . SER A 1 380 ? -29.869 9.406   10.137  1.00 16.83 ? 490  SER A CA    1 
ATOM   2265 C  C     . SER A 1 380 ? -31.036 10.135  9.469   1.00 18.06 ? 490  SER A C     1 
ATOM   2266 O  O     . SER A 1 380 ? -31.038 10.276  8.237   1.00 18.63 ? 490  SER A O     1 
ATOM   2267 C  CB    . SER A 1 380 ? -28.538 9.960   9.615   1.00 17.34 ? 490  SER A CB    1 
ATOM   2268 O  OG    . SER A 1 380 ? -27.405 9.345   10.206  1.00 17.82 ? 490  SER A OG    1 
ATOM   2269 N  N     . PRO A 1 381 ? -32.040 10.628  10.207  1.00 19.03 ? 491  PRO A N     1 
ATOM   2270 C  CA    . PRO A 1 381 ? -33.131 11.371  9.548   1.00 20.25 ? 491  PRO A CA    1 
ATOM   2271 C  C     . PRO A 1 381 ? -32.757 12.792  9.146   1.00 20.04 ? 491  PRO A C     1 
ATOM   2272 O  O     . PRO A 1 381 ? -33.463 13.382  8.310   1.00 21.18 ? 491  PRO A O     1 
ATOM   2273 C  CB    . PRO A 1 381 ? -34.245 11.375  10.608  1.00 21.80 ? 491  PRO A CB    1 
ATOM   2274 C  CG    . PRO A 1 381 ? -33.505 11.306  11.917  1.00 23.35 ? 491  PRO A CG    1 
ATOM   2275 C  CD    . PRO A 1 381 ? -32.290 10.428  11.648  1.00 20.71 ? 491  PRO A CD    1 
ATOM   2276 N  N     . THR A 1 382 ? -31.673 13.341  9.702   1.00 18.55 ? 492  THR A N     1 
ATOM   2277 C  CA    . THR A 1 382 ? -31.224 14.709  9.472   1.00 17.92 ? 492  THR A CA    1 
ATOM   2278 C  C     . THR A 1 382 ? -29.701 14.709  9.383   1.00 17.52 ? 492  THR A C     1 
ATOM   2279 O  O     . THR A 1 382 ? -29.044 13.735  9.771   1.00 18.87 ? 492  THR A O     1 
ATOM   2280 C  CB    . THR A 1 382 ? -31.663 15.651  10.602  1.00 19.35 ? 492  THR A CB    1 
ATOM   2281 O  OG1   . THR A 1 382 ? -31.105 15.199  11.844  1.00 20.75 ? 492  THR A OG1   1 
ATOM   2282 C  CG2   . THR A 1 382 ? -33.207 15.718  10.711  1.00 20.67 ? 492  THR A CG2   1 
ATOM   2283 N  N     . ILE A 1 383 ? -29.142 15.825  8.887   1.00 17.02 ? 493  ILE A N     1 
ATOM   2284 C  CA    . ILE A 1 383 ? -27.685 15.969  8.822   1.00 16.88 ? 493  ILE A CA    1 
ATOM   2285 C  C     . ILE A 1 383 ? -27.095 16.036  10.227  1.00 18.47 ? 493  ILE A C     1 
ATOM   2286 O  O     . ILE A 1 383 ? -25.982 15.549  10.466  1.00 17.60 ? 493  ILE A O     1 
ATOM   2287 C  CB    . ILE A 1 383 ? -27.270 17.202  7.981   1.00 16.95 ? 493  ILE A CB    1 
ATOM   2288 C  CG1   . ILE A 1 383 ? -27.707 17.058  6.517   1.00 18.54 ? 493  ILE A CG1   1 
ATOM   2289 C  CG2   . ILE A 1 383 ? -25.730 17.446  8.056   1.00 18.74 ? 493  ILE A CG2   1 
ATOM   2290 C  CD1   . ILE A 1 383 ? -27.217 15.782  5.791   1.00 17.68 ? 493  ILE A CD1   1 
ATOM   2291 N  N     . GLU A 1 384 ? -27.825 16.620  11.184  1.00 20.32 ? 494  GLU A N     1 
ATOM   2292 C  CA    . GLU A 1 384 ? -27.317 16.673  12.553  1.00 21.65 ? 494  GLU A CA    1 
ATOM   2293 C  C     . GLU A 1 384 ? -27.117 15.272  13.149  1.00 22.09 ? 494  GLU A C     1 
ATOM   2294 O  O     . GLU A 1 384 ? -26.191 15.068  13.948  1.00 21.98 ? 494  GLU A O     1 
ATOM   2295 C  CB    . GLU A 1 384 ? -28.247 17.534  13.420  1.00 23.90 ? 494  GLU A CB    1 
ATOM   2296 C  CG    . GLU A 1 384 ? -28.151 19.060  13.135  1.00 26.44 ? 494  GLU A CG    1 
ATOM   2297 C  CD    . GLU A 1 384 ? -28.911 19.525  11.882  1.00 27.38 ? 494  GLU A CD    1 
ATOM   2298 O  OE1   . GLU A 1 384 ? -29.776 18.778  11.382  1.00 27.34 ? 494  GLU A OE1   1 
ATOM   2299 O  OE2   . GLU A 1 384 ? -28.652 20.659  11.405  1.00 29.71 ? 494  GLU A OE2   1 
ATOM   2300 N  N     . VAL A 1 385 ? -27.951 14.294  12.770  1.00 20.07 ? 495  VAL A N     1 
ATOM   2301 C  CA    . VAL A 1 385 ? -27.752 12.921  13.242  1.00 19.29 ? 495  VAL A CA    1 
ATOM   2302 C  C     . VAL A 1 385 ? -26.637 12.230  12.459  1.00 19.08 ? 495  VAL A C     1 
ATOM   2303 O  O     . VAL A 1 385 ? -25.879 11.427  13.018  1.00 19.14 ? 495  VAL A O     1 
ATOM   2304 C  CB    . VAL A 1 385 ? -29.071 12.122  13.182  1.00 19.32 ? 495  VAL A CB    1 
ATOM   2305 C  CG1   . VAL A 1 385 ? -28.834 10.653  13.594  1.00 21.13 ? 495  VAL A CG1   1 
ATOM   2306 C  CG2   . VAL A 1 385 ? -30.104 12.760  14.101  1.00 21.15 ? 495  VAL A CG2   1 
ATOM   2307 N  N     . LEU A 1 386 ? -26.499 12.533  11.166  1.00 18.68 ? 496  LEU A N     1 
ATOM   2308 C  CA    . LEU A 1 386 ? -25.388 11.969  10.399  1.00 17.23 ? 496  LEU A CA    1 
ATOM   2309 C  C     . LEU A 1 386 ? -24.032 12.364  10.989  1.00 17.01 ? 496  LEU A C     1 
ATOM   2310 O  O     . LEU A 1 386 ? -23.068 11.583  10.910  1.00 16.18 ? 496  LEU A O     1 
ATOM   2311 C  CB    . LEU A 1 386 ? -25.490 12.406  8.936   1.00 16.66 ? 496  LEU A CB    1 
ATOM   2312 C  CG    . LEU A 1 386 ? -24.403 11.912  7.959   1.00 15.40 ? 496  LEU A CG    1 
ATOM   2313 C  CD1   . LEU A 1 386 ? -24.373 10.374  7.886   1.00 15.94 ? 496  LEU A CD1   1 
ATOM   2314 C  CD2   . LEU A 1 386 ? -24.592 12.514  6.563   1.00 16.11 ? 496  LEU A CD2   1 
ATOM   2315 N  N     . GLN A 1 387 ? -23.940 13.561  11.583  1.00 18.13 ? 497  GLN A N     1 
ATOM   2316 C  CA    . GLN A 1 387 ? -22.704 14.023  12.209  1.00 17.80 ? 497  GLN A CA    1 
ATOM   2317 C  C     . GLN A 1 387 ? -22.293 13.186  13.416  1.00 18.16 ? 497  GLN A C     1 
ATOM   2318 O  O     . GLN A 1 387 ? -21.166 13.364  13.908  1.00 19.67 ? 497  GLN A O     1 
ATOM   2319 C  CB    . GLN A 1 387 ? -22.847 15.508  12.599  1.00 18.36 ? 497  GLN A CB    1 
ATOM   2320 C  CG    . GLN A 1 387 ? -22.905 16.464  11.401  1.00 17.99 ? 497  GLN A CG    1 
ATOM   2321 C  CD    . GLN A 1 387 ? -23.276 17.917  11.761  1.00 17.81 ? 497  GLN A CD    1 
ATOM   2322 O  OE1   . GLN A 1 387 ? -23.921 18.184  12.784  1.00 19.33 ? 497  GLN A OE1   1 
ATOM   2323 N  NE2   . GLN A 1 387 ? -22.861 18.863  10.907  1.00 17.86 ? 497  GLN A NE2   1 
ATOM   2324 N  N     . GLN A 1 388 ? -23.155 12.267  13.877  1.00 18.77 ? 498  GLN A N     1 
ATOM   2325 C  CA    . GLN A 1 388 ? -22.864 11.361  14.983  1.00 20.77 ? 498  GLN A CA    1 
ATOM   2326 C  C     . GLN A 1 388 ? -22.515 9.936   14.537  1.00 17.90 ? 498  GLN A C     1 
ATOM   2327 O  O     . GLN A 1 388 ? -22.339 9.060   15.396  1.00 19.43 ? 498  GLN A O     1 
ATOM   2328 C  CB    . GLN A 1 388 ? -24.059 11.322  15.945  1.00 23.44 ? 498  GLN A CB    1 
ATOM   2329 C  CG    . GLN A 1 388 ? -24.481 12.709  16.463  1.00 27.42 ? 498  GLN A CG    1 
ATOM   2330 C  CD    . GLN A 1 388 ? -25.851 12.719  17.139  1.00 36.24 ? 498  GLN A CD    1 
ATOM   2331 O  OE1   . GLN A 1 388 ? -26.298 11.714  17.693  1.00 40.15 ? 498  GLN A OE1   1 
ATOM   2332 N  NE2   . GLN A 1 388 ? -26.522 13.867  17.094  1.00 39.29 ? 498  GLN A NE2   1 
ATOM   2333 N  N     . ALA A 1 389 ? -22.403 9.672   13.232  1.00 17.32 ? 499  ALA A N     1 
ATOM   2334 C  CA    . ALA A 1 389 ? -22.157 8.313   12.737  1.00 16.33 ? 499  ALA A CA    1 
ATOM   2335 C  C     . ALA A 1 389 ? -20.704 7.873   12.993  1.00 17.47 ? 499  ALA A C     1 
ATOM   2336 O  O     . ALA A 1 389 ? -19.822 8.695   13.256  1.00 19.63 ? 499  ALA A O     1 
ATOM   2337 C  CB    . ALA A 1 389 ? -22.471 8.238   11.243  1.00 17.45 ? 499  ALA A CB    1 
ATOM   2338 N  N     . GLN A 1 390 ? -20.451 6.557   12.884  1.00 15.05 ? 500  GLN A N     1 
ATOM   2339 C  CA    . GLN A 1 390 ? -19.132 5.974   13.148  1.00 15.52 ? 500  GLN A CA    1 
ATOM   2340 C  C     . GLN A 1 390 ? -18.480 5.434   11.875  1.00 16.12 ? 500  GLN A C     1 
ATOM   2341 O  O     . GLN A 1 390 ? -19.165 5.021   10.934  1.00 17.39 ? 500  GLN A O     1 
ATOM   2342 C  CB    . GLN A 1 390 ? -19.223 4.835   14.178  1.00 17.16 ? 500  GLN A CB    1 
ATOM   2343 C  CG    . GLN A 1 390 ? -19.588 5.262   15.598  1.00 19.18 ? 500  GLN A CG    1 
ATOM   2344 C  CD    . GLN A 1 390 ? -19.715 4.073   16.548  1.00 20.73 ? 500  GLN A CD    1 
ATOM   2345 O  OE1   . GLN A 1 390 ? -20.632 3.252   16.425  1.00 21.70 ? 500  GLN A OE1   1 
ATOM   2346 N  NE2   . GLN A 1 390 ? -18.780 3.960   17.485  1.00 23.19 ? 500  GLN A NE2   1 
ATOM   2347 N  N     . PHE A 1 391 ? -17.135 5.416   11.868  1.00 14.35 ? 501  PHE A N     1 
ATOM   2348 C  CA    . PHE A 1 391 ? -16.307 4.903   10.777  1.00 14.81 ? 501  PHE A CA    1 
ATOM   2349 C  C     . PHE A 1 391 ? -15.673 3.554   11.131  1.00 16.79 ? 501  PHE A C     1 
ATOM   2350 O  O     . PHE A 1 391 ? -15.448 3.243   12.307  1.00 17.24 ? 501  PHE A O     1 
ATOM   2351 C  CB    . PHE A 1 391 ? -15.148 5.869   10.431  1.00 14.65 ? 501  PHE A CB    1 
ATOM   2352 C  CG    . PHE A 1 391 ? -15.579 7.237   9.907   1.00 15.47 ? 501  PHE A CG    1 
ATOM   2353 C  CD1   . PHE A 1 391 ? -16.183 7.366   8.658   1.00 15.60 ? 501  PHE A CD1   1 
ATOM   2354 C  CD2   . PHE A 1 391 ? -15.307 8.397   10.634  1.00 17.43 ? 501  PHE A CD2   1 
ATOM   2355 C  CE1   . PHE A 1 391 ? -16.560 8.615   8.156   1.00 16.25 ? 501  PHE A CE1   1 
ATOM   2356 C  CE2   . PHE A 1 391 ? -15.686 9.666   10.139  1.00 18.22 ? 501  PHE A CE2   1 
ATOM   2357 C  CZ    . PHE A 1 391 ? -16.309 9.768   8.896   1.00 17.34 ? 501  PHE A CZ    1 
ATOM   2358 N  N     . VAL A 1 392 ? -15.348 2.767   10.093  1.00 16.43 ? 502  VAL A N     1 
ATOM   2359 C  CA    . VAL A 1 392 ? -14.366 1.685   10.178  1.00 16.07 ? 502  VAL A CA    1 
ATOM   2360 C  C     . VAL A 1 392 ? -13.186 2.047   9.280   1.00 18.18 ? 502  VAL A C     1 
ATOM   2361 O  O     . VAL A 1 392 ? -13.378 2.544   8.163   1.00 17.75 ? 502  VAL A O     1 
ATOM   2362 C  CB    . VAL A 1 392 ? -14.970 0.314   9.775   1.00 16.33 ? 502  VAL A CB    1 
ATOM   2363 C  CG1   . VAL A 1 392 ? -15.613 0.367   8.369   1.00 18.54 ? 502  VAL A CG1   1 
ATOM   2364 C  CG2   . VAL A 1 392 ? -13.906 -0.800  9.853   1.00 17.84 ? 502  VAL A CG2   1 
ATOM   2365 N  N     . ARG A 1 393 ? -11.962 1.819   9.770   1.00 17.42 ? 503  ARG A N     1 
ATOM   2366 C  CA    . ARG A 1 393 ? -10.770 2.102   8.972   1.00 18.03 ? 503  ARG A CA    1 
ATOM   2367 C  C     . ARG A 1 393 ? -10.445 0.903   8.087   1.00 19.97 ? 503  ARG A C     1 
ATOM   2368 O  O     . ARG A 1 393 ? -10.658 -0.242  8.487   1.00 20.22 ? 503  ARG A O     1 
ATOM   2369 C  CB    . ARG A 1 393 ? -9.577  2.442   9.871   1.00 19.86 ? 503  ARG A CB    1 
ATOM   2370 C  CG    . ARG A 1 393 ? -8.337  2.825   9.075   1.00 22.99 ? 503  ARG A CG    1 
ATOM   2371 C  CD    . ARG A 1 393 ? -7.199  3.330   9.936   1.00 24.53 ? 503  ARG A CD    1 
ATOM   2372 N  NE    . ARG A 1 393 ? -5.962  3.296   9.164   1.00 28.86 ? 503  ARG A NE    1 
ATOM   2373 C  CZ    . ARG A 1 393 ? -4.756  3.180   9.696   1.00 32.53 ? 503  ARG A CZ    1 
ATOM   2374 N  NH1   . ARG A 1 393 ? -4.629  3.092   11.012  1.00 34.59 ? 503  ARG A NH1   1 
ATOM   2375 N  NH2   . ARG A 1 393 ? -3.683  3.144   8.915   1.00 33.65 ? 503  ARG A NH2   1 
ATOM   2376 N  N     . ILE A 1 394 ? -9.961  1.161   6.870   1.00 20.00 ? 504  ILE A N     1 
ATOM   2377 C  CA    . ILE A 1 394 ? -9.663  0.059   5.961   1.00 21.84 ? 504  ILE A CA    1 
ATOM   2378 C  C     . ILE A 1 394 ? -8.191  0.096   5.551   1.00 22.27 ? 504  ILE A C     1 
ATOM   2379 O  O     . ILE A 1 394 ? -7.491  1.109   5.696   1.00 23.43 ? 504  ILE A O     1 
ATOM   2380 C  CB    . ILE A 1 394 ? -10.594 0.025   4.721   1.00 25.28 ? 504  ILE A CB    1 
ATOM   2381 C  CG1   . ILE A 1 394 ? -10.325 1.165   3.748   1.00 26.81 ? 504  ILE A CG1   1 
ATOM   2382 C  CG2   . ILE A 1 394 ? -12.071 0.064   5.143   1.00 25.35 ? 504  ILE A CG2   1 
ATOM   2383 C  CD1   . ILE A 1 394 ? -11.379 1.246   2.635   1.00 28.28 ? 504  ILE A CD1   1 
ATOM   2384 N  N     . THR A 1 395 ? -7.716  -1.053  5.073   1.00 23.45 ? 505  THR A N     1 
ATOM   2385 C  CA    . THR A 1 395 ? -6.335  -1.226  4.629   1.00 25.95 ? 505  THR A CA    1 
ATOM   2386 C  C     . THR A 1 395 ? -6.226  -0.978  3.134   1.00 27.46 ? 505  THR A C     1 
ATOM   2387 O  O     . THR A 1 395 ? -7.227  -0.832  2.424   1.00 27.78 ? 505  THR A O     1 
ATOM   2388 C  CB    . THR A 1 395 ? -5.856  -2.648  4.936   1.00 29.04 ? 505  THR A CB    1 
ATOM   2389 O  OG1   . THR A 1 395 ? -6.541  -3.556  4.072   1.00 31.91 ? 505  THR A OG1   1 
ATOM   2390 C  CG2   . THR A 1 395 ? -6.123  -3.048  6.381   1.00 28.94 ? 505  THR A CG2   1 
ATOM   2391 N  N     . PRO A 1 396 ? -5.006  -0.973  2.597   1.00 31.02 ? 506  PRO A N     1 
ATOM   2392 C  CA    . PRO A 1 396 ? -4.866  -0.886  1.135   1.00 33.06 ? 506  PRO A CA    1 
ATOM   2393 C  C     . PRO A 1 396 ? -5.581  -1.996  0.391   1.00 36.16 ? 506  PRO A C     1 
ATOM   2394 O  O     . PRO A 1 396 ? -6.061  -1.759  -0.724  1.00 38.72 ? 506  PRO A O     1 
ATOM   2395 C  CB    . PRO A 1 396 ? -3.347  -0.948  0.927   1.00 31.21 ? 506  PRO A CB    1 
ATOM   2396 C  CG    . PRO A 1 396 ? -2.784  -0.392  2.194   1.00 31.10 ? 506  PRO A CG    1 
ATOM   2397 C  CD    . PRO A 1 396 ? -3.705  -0.846  3.286   1.00 29.94 ? 506  PRO A CD    1 
ATOM   2398 N  N     . ALA A 1 397 ? -5.669  -3.202  0.966   1.00 35.08 ? 507  ALA A N     1 
ATOM   2399 C  CA    . ALA A 1 397 ? -6.378  -4.283  0.290   1.00 36.32 ? 507  ALA A CA    1 
ATOM   2400 C  C     . ALA A 1 397 ? -7.872  -4.001  0.180   1.00 37.65 ? 507  ALA A C     1 
ATOM   2401 O  O     . ALA A 1 397 ? -8.512  -4.426  -0.790  1.00 38.21 ? 507  ALA A O     1 
ATOM   2402 C  CB    . ALA A 1 397 ? -6.148  -5.612  1.016   1.00 35.84 ? 507  ALA A CB    1 
ATOM   2403 N  N     . GLY A 1 398 ? -8.445  -3.298  1.154   1.00 37.84 ? 508  GLY A N     1 
ATOM   2404 C  CA    . GLY A 1 398 ? -9.864  -3.000  1.130   1.00 41.29 ? 508  GLY A CA    1 
ATOM   2405 C  C     . GLY A 1 398 ? -10.223 -1.910  0.144   1.00 42.79 ? 508  GLY A C     1 
ATOM   2406 O  O     . GLY A 1 398 ? -11.274 -1.959  -0.504  1.00 43.95 ? 508  GLY A O     1 
ATOM   2407 N  N     . LEU A 1 399 ? -9.349  -0.913  0.022   1.00 44.21 ? 509  LEU A N     1 
ATOM   2408 C  CA    . LEU A 1 399 ? -9.603  0.178   -0.912  1.00 46.80 ? 509  LEU A CA    1 
ATOM   2409 C  C     . LEU A 1 399 ? -9.578  -0.316  -2.352  1.00 50.96 ? 509  LEU A C     1 
ATOM   2410 O  O     . LEU A 1 399 ? -10.531 -0.099  -3.110  1.00 49.98 ? 509  LEU A O     1 
ATOM   2411 C  CB    . LEU A 1 399 ? -8.574  1.288   -0.711  1.00 44.72 ? 509  LEU A CB    1 
ATOM   2412 C  CG    . LEU A 1 399 ? -8.727  2.499   -1.633  1.00 43.21 ? 509  LEU A CG    1 
ATOM   2413 C  CD1   . LEU A 1 399 ? -10.089 3.151   -1.413  1.00 42.63 ? 509  LEU A CD1   1 
ATOM   2414 C  CD2   . LEU A 1 399 ? -7.596  3.499   -1.406  1.00 42.65 ? 509  LEU A CD2   1 
ATOM   2415 N  N     . LYS A 1 400 ? -8.495  -0.994  -2.742  1.00 55.68 ? 510  LYS A N     1 
ATOM   2416 C  CA    . LYS A 1 400 ? -8.283  -1.365  -4.138  1.00 61.20 ? 510  LYS A CA    1 
ATOM   2417 C  C     . LYS A 1 400 ? -9.463  -2.121  -4.738  1.00 63.16 ? 510  LYS A C     1 
ATOM   2418 O  O     . LYS A 1 400 ? -9.625  -2.122  -5.965  1.00 63.19 ? 510  LYS A O     1 
ATOM   2419 C  CB    . LYS A 1 400 ? -7.004  -2.200  -4.254  1.00 64.15 ? 510  LYS A CB    1 
ATOM   2420 C  CG    . LYS A 1 400 ? -6.109  -1.810  -5.420  1.00 66.75 ? 510  LYS A CG    1 
ATOM   2421 C  CD    . LYS A 1 400 ? -4.633  -1.960  -5.061  1.00 69.38 ? 510  LYS A CD    1 
ATOM   2422 C  CE    . LYS A 1 400 ? -4.203  -0.924  -4.024  1.00 71.16 ? 510  LYS A CE    1 
ATOM   2423 N  NZ    . LYS A 1 400 ? -2.741  -0.989  -3.721  1.00 72.23 ? 510  LYS A NZ    1 
ATOM   2424 N  N     . GLU A 1 401 ? -10.292 -2.755  -3.910  1.00 64.43 ? 511  GLU A N     1 
ATOM   2425 C  CA    . GLU A 1 401 ? -11.451 -3.497  -4.390  1.00 65.40 ? 511  GLU A CA    1 
ATOM   2426 C  C     . GLU A 1 401 ? -12.738 -2.680  -4.378  1.00 68.01 ? 511  GLU A C     1 
ATOM   2427 O  O     . GLU A 1 401 ? -13.755 -3.152  -4.900  1.00 67.96 ? 511  GLU A O     1 
ATOM   2428 C  CB    . GLU A 1 401 ? -11.649 -4.762  -3.549  1.00 64.59 ? 511  GLU A CB    1 
ATOM   2429 C  CG    . GLU A 1 401 ? -11.895 -4.483  -2.074  1.00 63.73 ? 511  GLU A CG    1 
ATOM   2430 C  CD    . GLU A 1 401 ? -12.024 -5.752  -1.252  1.00 63.44 ? 511  GLU A CD    1 
ATOM   2431 O  OE1   . GLU A 1 401 ? -12.513 -5.669  -0.106  1.00 63.21 ? 511  GLU A OE1   1 
ATOM   2432 O  OE2   . GLU A 1 401 ? -11.637 -6.830  -1.751  1.00 64.33 ? 511  GLU A OE2   1 
ATOM   2433 N  N     . SER A 1 402 ? -12.724 -1.478  -3.792  1.00 70.28 ? 512  SER A N     1 
ATOM   2434 C  CA    . SER A 1 402 ? -13.925 -0.646  -3.760  1.00 72.15 ? 512  SER A CA    1 
ATOM   2435 C  C     . SER A 1 402 ? -14.206 -0.010  -5.117  1.00 74.32 ? 512  SER A C     1 
ATOM   2436 O  O     . SER A 1 402 ? -15.369 0.143   -5.502  1.00 74.14 ? 512  SER A O     1 
ATOM   2437 C  CB    . SER A 1 402 ? -13.795 0.427   -2.679  1.00 72.03 ? 512  SER A CB    1 
ATOM   2438 O  OG    . SER A 1 402 ? -13.832 -0.148  -1.383  1.00 72.06 ? 512  SER A OG    1 
ATOM   2439 N  N     . HIS A 1 403 ? -13.166 0.384   -5.841  1.00 76.76 ? 513  HIS A N     1 
ATOM   2440 C  CA    . HIS A 1 403 ? -13.337 0.722   -7.250  1.00 79.50 ? 513  HIS A CA    1 
ATOM   2441 C  C     . HIS A 1 403 ? -13.647 -0.561  -8.017  1.00 81.48 ? 513  HIS A C     1 
ATOM   2442 O  O     . HIS A 1 403 ? -12.859 -1.515  -7.953  1.00 82.45 ? 513  HIS A O     1 
ATOM   2443 C  CB    . HIS A 1 403 ? -12.085 1.400   -7.803  1.00 80.74 ? 513  HIS A CB    1 
ATOM   2444 C  CG    . HIS A 1 403 ? -12.348 2.733   -8.436  1.00 82.27 ? 513  HIS A CG    1 
ATOM   2445 N  ND1   . HIS A 1 403 ? -11.563 3.241   -9.450  1.00 82.69 ? 513  HIS A ND1   1 
ATOM   2446 C  CD2   . HIS A 1 403 ? -13.300 3.667   -8.195  1.00 83.45 ? 513  HIS A CD2   1 
ATOM   2447 C  CE1   . HIS A 1 403 ? -12.023 4.427   -9.809  1.00 83.41 ? 513  HIS A CE1   1 
ATOM   2448 N  NE2   . HIS A 1 403 ? -13.076 4.709   -9.064  1.00 83.75 ? 513  HIS A NE2   1 
ATOM   2449 N  N     . PRO A 1 404 ? -14.770 -0.618  -8.771  1.00 82.03 ? 514  PRO A N     1 
ATOM   2450 C  CA    . PRO A 1 404 ? -15.320 -1.911  -9.219  1.00 81.79 ? 514  PRO A CA    1 
ATOM   2451 C  C     . PRO A 1 404 ? -14.262 -2.963  -9.510  1.00 80.91 ? 514  PRO A C     1 
ATOM   2452 O  O     . PRO A 1 404 ? -13.546 -2.874  -10.512 1.00 81.65 ? 514  PRO A O     1 
ATOM   2453 C  CB    . PRO A 1 404 ? -16.096 -1.532  -10.485 1.00 82.13 ? 514  PRO A CB    1 
ATOM   2454 C  CG    . PRO A 1 404 ? -16.537 -0.129  -10.233 1.00 82.05 ? 514  PRO A CG    1 
ATOM   2455 C  CD    . PRO A 1 404 ? -15.438 0.523   -9.423  1.00 81.96 ? 514  PRO A CD    1 
ATOM   2456 N  N     . HIS A 1 405 ? -14.156 -3.967  -8.639  1.00 79.38 ? 515  HIS A N     1 
ATOM   2457 C  CA    . HIS A 1 405 ? -13.028 -4.893  -8.664  1.00 77.16 ? 515  HIS A CA    1 
ATOM   2458 C  C     . HIS A 1 405 ? -13.359 -6.101  -9.536  1.00 78.17 ? 515  HIS A C     1 
ATOM   2459 O  O     . HIS A 1 405 ? -14.270 -6.878  -9.230  1.00 77.58 ? 515  HIS A O     1 
ATOM   2460 C  CB    . HIS A 1 405 ? -12.634 -5.308  -7.245  1.00 74.35 ? 515  HIS A CB    1 
ATOM   2461 C  CG    . HIS A 1 405 ? -13.585 -6.263  -6.588  1.00 73.07 ? 515  HIS A CG    1 
ATOM   2462 N  ND1   . HIS A 1 405 ? -13.512 -7.629  -6.770  1.00 72.84 ? 515  HIS A ND1   1 
ATOM   2463 C  CD2   . HIS A 1 405 ? -14.613 -6.052  -5.732  1.00 72.56 ? 515  HIS A CD2   1 
ATOM   2464 C  CE1   . HIS A 1 405 ? -14.459 -8.217  -6.060  1.00 72.81 ? 515  HIS A CE1   1 
ATOM   2465 N  NE2   . HIS A 1 405 ? -15.141 -7.283  -5.420  1.00 73.09 ? 515  HIS A NE2   1 
ATOM   2466 N  N     . ASP A 1 406 ? -12.629 -6.234  -10.643 1.00 79.49 ? 516  ASP A N     1 
ATOM   2467 C  CA    . ASP A 1 406 ? -12.564 -7.462  -11.435 1.00 79.94 ? 516  ASP A CA    1 
ATOM   2468 C  C     . ASP A 1 406 ? -13.922 -7.829  -12.043 1.00 77.54 ? 516  ASP A C     1 
ATOM   2469 O  O     . ASP A 1 406 ? -14.491 -8.893  -11.785 1.00 78.06 ? 516  ASP A O     1 
ATOM   2470 C  CB    . ASP A 1 406 ? -11.999 -8.610  -10.593 1.00 82.48 ? 516  ASP A CB    1 
ATOM   2471 C  CG    . ASP A 1 406 ? -11.682 -9.834  -11.422 1.00 84.15 ? 516  ASP A CG    1 
ATOM   2472 O  OD1   . ASP A 1 406 ? -12.547 -10.730 -11.511 1.00 85.12 ? 516  ASP A OD1   1 
ATOM   2473 O  OD2   . ASP A 1 406 ? -10.577 -9.888  -12.006 1.00 84.34 ? 516  ASP A OD2   1 
ATOM   2474 N  N     . VAL A 1 407 ? -14.429 -6.917  -12.874 1.00 74.92 ? 517  VAL A N     1 
ATOM   2475 C  CA    . VAL A 1 407 ? -15.568 -7.183  -13.748 1.00 73.03 ? 517  VAL A CA    1 
ATOM   2476 C  C     . VAL A 1 407 ? -15.526 -6.188  -14.898 1.00 72.34 ? 517  VAL A C     1 
ATOM   2477 O  O     . VAL A 1 407 ? -15.822 -5.001  -14.714 1.00 73.31 ? 517  VAL A O     1 
ATOM   2478 C  CB    . VAL A 1 407 ? -16.918 -7.093  -13.009 1.00 71.86 ? 517  VAL A CB    1 
ATOM   2479 C  CG1   . VAL A 1 407 ? -17.631 -8.434  -13.043 1.00 71.90 ? 517  VAL A CG1   1 
ATOM   2480 C  CG2   . VAL A 1 407 ? -16.734 -6.590  -11.583 1.00 71.58 ? 517  VAL A CG2   1 
ATOM   2481 N  N     . ALA A 1 408 ? -15.157 -6.660  -16.088 1.00 70.14 ? 518  ALA A N     1 
ATOM   2482 C  CA    . ALA A 1 408 ? -15.113 -5.796  -17.260 1.00 68.49 ? 518  ALA A CA    1 
ATOM   2483 C  C     . ALA A 1 408 ? -16.411 -5.010  -17.390 1.00 67.30 ? 518  ALA A C     1 
ATOM   2484 O  O     . ALA A 1 408 ? -17.433 -5.551  -17.826 1.00 66.67 ? 518  ALA A O     1 
ATOM   2485 C  CB    . ALA A 1 408 ? -14.849 -6.616  -18.525 1.00 68.10 ? 518  ALA A CB    1 
ATOM   2486 N  N     . MET A 1 409 ? -16.380 -3.736  -16.999 1.00 66.32 ? 519  MET A N     1 
ATOM   2487 C  CA    . MET A 1 409 ? -17.557 -2.883  -17.099 1.00 65.92 ? 519  MET A CA    1 
ATOM   2488 C  C     . MET A 1 409 ? -17.890 -2.620  -18.563 1.00 66.29 ? 519  MET A C     1 
ATOM   2489 O  O     . MET A 1 409 ? -17.013 -2.265  -19.357 1.00 66.25 ? 519  MET A O     1 
ATOM   2490 C  CB    . MET A 1 409 ? -17.316 -1.566  -16.363 1.00 65.87 ? 519  MET A CB    1 
ATOM   2491 C  CG    . MET A 1 409 ? -18.560 -0.716  -16.165 1.00 65.54 ? 519  MET A CG    1 
ATOM   2492 S  SD    . MET A 1 409 ? -18.212 0.822   -15.286 1.00 65.93 ? 519  MET A SD    1 
ATOM   2493 C  CE    . MET A 1 409 ? -17.206 0.222   -13.931 1.00 65.45 ? 519  MET A CE    1 
ATOM   2494 N  N     . THR A 1 410 ? -19.164 -2.792  -18.922 1.00 66.94 ? 520  THR A N     1 
ATOM   2495 C  CA    . THR A 1 410 ? -19.592 -2.678  -20.308 1.00 67.39 ? 520  THR A CA    1 
ATOM   2496 C  C     . THR A 1 410 ? -20.595 -1.563  -20.570 1.00 67.62 ? 520  THR A C     1 
ATOM   2497 O  O     . THR A 1 410 ? -20.719 -1.137  -21.724 1.00 67.28 ? 520  THR A O     1 
ATOM   2498 C  CB    . THR A 1 410 ? -20.204 -4.004  -20.795 1.00 67.11 ? 520  THR A CB    1 
ATOM   2499 O  OG1   . THR A 1 410 ? -21.484 -4.204  -20.181 1.00 67.01 ? 520  THR A OG1   1 
ATOM   2500 C  CG2   . THR A 1 410 ? -19.295 -5.168  -20.440 1.00 67.06 ? 520  THR A CG2   1 
ATOM   2501 N  N     . VAL A 1 411 ? -21.307 -1.079  -19.552 1.00 67.62 ? 521  VAL A N     1 
ATOM   2502 C  CA    . VAL A 1 411 ? -22.331 -0.061  -19.736 1.00 68.11 ? 521  VAL A CA    1 
ATOM   2503 C  C     . VAL A 1 411 ? -21.978 1.165   -18.900 1.00 69.52 ? 521  VAL A C     1 
ATOM   2504 O  O     . VAL A 1 411 ? -21.209 1.097   -17.935 1.00 68.99 ? 521  VAL A O     1 
ATOM   2505 C  CB    . VAL A 1 411 ? -23.739 -0.584  -19.375 1.00 67.06 ? 521  VAL A CB    1 
ATOM   2506 C  CG1   . VAL A 1 411 ? -24.805 0.430   -19.763 1.00 66.28 ? 521  VAL A CG1   1 
ATOM   2507 C  CG2   . VAL A 1 411 ? -24.000 -1.924  -20.052 1.00 67.07 ? 521  VAL A CG2   1 
ATOM   2508 N  N     . GLU A 1 412 ? -22.551 2.301   -19.296 1.00 70.74 ? 522  GLU A N     1 
ATOM   2509 C  CA    . GLU A 1 412 ? -22.345 3.557   -18.587 1.00 71.86 ? 522  GLU A CA    1 
ATOM   2510 C  C     . GLU A 1 412 ? -23.059 3.555   -17.238 1.00 69.92 ? 522  GLU A C     1 
ATOM   2511 O  O     . GLU A 1 412 ? -24.145 2.990   -17.083 1.00 70.05 ? 522  GLU A O     1 
ATOM   2512 C  CB    . GLU A 1 412 ? -22.850 4.730   -19.431 1.00 75.34 ? 522  GLU A CB    1 
ATOM   2513 C  CG    . GLU A 1 412 ? -21.833 5.324   -20.386 1.00 78.37 ? 522  GLU A CG    1 
ATOM   2514 C  CD    . GLU A 1 412 ? -20.839 6.226   -19.680 1.00 81.12 ? 522  GLU A CD    1 
ATOM   2515 O  OE1   . GLU A 1 412 ? -19.880 5.700   -19.075 1.00 82.24 ? 522  GLU A OE1   1 
ATOM   2516 O  OE2   . GLU A 1 412 ? -21.026 7.463   -19.720 1.00 81.43 ? 522  GLU A OE2   1 
ATOM   2517 N  N     . ALA A 1 413 ? -22.437 4.208   -16.257 1.00 67.75 ? 523  ALA A N     1 
ATOM   2518 C  CA    . ALA A 1 413 ? -23.026 4.398   -14.944 1.00 65.98 ? 523  ALA A CA    1 
ATOM   2519 C  C     . ALA A 1 413 ? -23.134 5.888   -14.647 1.00 63.83 ? 523  ALA A C     1 
ATOM   2520 O  O     . ALA A 1 413 ? -22.149 6.620   -14.820 1.00 63.26 ? 523  ALA A O     1 
ATOM   2521 C  CB    . ALA A 1 413 ? -22.190 3.704   -13.855 1.00 66.38 ? 523  ALA A CB    1 
ATOM   2522 N  N     . PRO A 1 414 ? -24.298 6.377   -14.201 1.00 62.17 ? 524  PRO A N     1 
ATOM   2523 C  CA    . PRO A 1 414 ? -24.443 7.826   -13.976 1.00 60.04 ? 524  PRO A CA    1 
ATOM   2524 C  C     . PRO A 1 414 ? -23.673 8.343   -12.775 1.00 57.51 ? 524  PRO A C     1 
ATOM   2525 O  O     . PRO A 1 414 ? -23.334 9.533   -12.747 1.00 57.79 ? 524  PRO A O     1 
ATOM   2526 C  CB    . PRO A 1 414 ? -25.955 8.002   -13.782 1.00 60.50 ? 524  PRO A CB    1 
ATOM   2527 C  CG    . PRO A 1 414 ? -26.411 6.690   -13.238 1.00 61.05 ? 524  PRO A CG    1 
ATOM   2528 C  CD    . PRO A 1 414 ? -25.534 5.639   -13.882 1.00 61.60 ? 524  PRO A CD    1 
ATOM   2529 N  N     . ASN A 1 415 ? -23.382 7.497   -11.792 1.00 55.45 ? 525  ASN A N     1 
ATOM   2530 C  CA    . ASN A 1 415 ? -22.703 7.931   -10.576 1.00 52.80 ? 525  ASN A CA    1 
ATOM   2531 C  C     . ASN A 1 415 ? -21.448 7.101   -10.306 1.00 53.29 ? 525  ASN A C     1 
ATOM   2532 O  O     . ASN A 1 415 ? -20.718 7.352   -9.344  1.00 52.92 ? 525  ASN A O     1 
ATOM   2533 C  CB    . ASN A 1 415 ? -23.661 7.856   -9.379  1.00 49.46 ? 525  ASN A CB    1 
ATOM   2534 C  CG    . ASN A 1 415 ? -24.384 6.515   -9.278  1.00 47.24 ? 525  ASN A CG    1 
ATOM   2535 O  OD1   . ASN A 1 415 ? -24.123 5.585   -10.045 1.00 46.06 ? 525  ASN A OD1   1 
ATOM   2536 N  ND2   . ASN A 1 415 ? -25.291 6.412   -8.316  1.00 44.14 ? 525  ASN A ND2   1 
HETATM 2537 P  P     . IMP B 2 .   ? -11.355 19.745  -5.715  1.00 16.41 ? 801  IMP A P     1 
HETATM 2538 O  O1P   . IMP B 2 .   ? -12.874 19.836  -5.478  1.00 18.45 ? 801  IMP A O1P   1 
HETATM 2539 O  O2P   . IMP B 2 .   ? -10.712 18.464  -5.137  1.00 17.50 ? 801  IMP A O2P   1 
HETATM 2540 O  O3P   . IMP B 2 .   ? -11.077 19.903  -7.206  1.00 17.61 ? 801  IMP A O3P   1 
HETATM 2541 O  "O5'" . IMP B 2 .   ? -10.708 21.037  -4.969  1.00 17.34 ? 801  IMP A "O5'" 1 
HETATM 2542 C  "C5'" . IMP B 2 .   ? -11.141 22.410  -5.137  1.00 16.06 ? 801  IMP A "C5'" 1 
HETATM 2543 C  "C4'" . IMP B 2 .   ? -10.468 23.292  -4.109  1.00 16.26 ? 801  IMP A "C4'" 1 
HETATM 2544 O  "O4'" . IMP B 2 .   ? -9.050  23.373  -4.363  1.00 16.12 ? 801  IMP A "O4'" 1 
HETATM 2545 C  "C3'" . IMP B 2 .   ? -10.893 24.752  -4.111  1.00 17.03 ? 801  IMP A "C3'" 1 
HETATM 2546 O  "O3'" . IMP B 2 .   ? -12.187 24.946  -3.538  1.00 16.67 ? 801  IMP A "O3'" 1 
HETATM 2547 C  "C2'" . IMP B 2 .   ? -9.742  25.411  -3.335  1.00 17.08 ? 801  IMP A "C2'" 1 
HETATM 2548 O  "O2'" . IMP B 2 .   ? -9.867  25.283  -1.919  1.00 16.56 ? 801  IMP A "O2'" 1 
HETATM 2549 C  "C1'" . IMP B 2 .   ? -8.541  24.568  -3.784  1.00 16.01 ? 801  IMP A "C1'" 1 
HETATM 2550 N  N9    . IMP B 2 .   ? -7.643  25.229  -4.761  1.00 16.18 ? 801  IMP A N9    1 
HETATM 2551 C  C8    . IMP B 2 .   ? -7.984  26.033  -5.818  1.00 17.11 ? 801  IMP A C8    1 
HETATM 2552 N  N7    . IMP B 2 .   ? -6.946  26.397  -6.555  1.00 16.87 ? 801  IMP A N7    1 
HETATM 2553 C  C5    . IMP B 2 .   ? -5.860  25.787  -5.943  1.00 17.10 ? 801  IMP A C5    1 
HETATM 2554 C  C6    . IMP B 2 .   ? -4.437  25.759  -6.295  1.00 19.11 ? 801  IMP A C6    1 
HETATM 2555 O  O6    . IMP B 2 .   ? -3.892  26.257  -7.285  1.00 18.37 ? 801  IMP A O6    1 
HETATM 2556 N  N1    . IMP B 2 .   ? -3.703  25.005  -5.376  1.00 19.26 ? 801  IMP A N1    1 
HETATM 2557 C  C2    . IMP B 2 .   ? -4.226  24.362  -4.307  1.00 19.60 ? 801  IMP A C2    1 
HETATM 2558 N  N3    . IMP B 2 .   ? -5.508  24.346  -3.977  1.00 18.27 ? 801  IMP A N3    1 
HETATM 2559 C  C4    . IMP B 2 .   ? -6.275  25.077  -4.828  1.00 17.90 ? 801  IMP A C4    1 
HETATM 2560 C  C4    . VOA C 3 .   ? -0.183  30.374  -2.599  1.00 17.02 ? 802  VOA A C4    1 
HETATM 2561 C  C7    . VOA C 3 .   ? 1.020   30.406  -0.425  1.00 16.52 ? 802  VOA A C7    1 
HETATM 2562 C  C8    . VOA C 3 .   ? 2.063   29.802  0.282   1.00 16.18 ? 802  VOA A C8    1 
HETATM 2563 C  C9    . VOA C 3 .   ? 2.356   30.229  1.573   1.00 16.96 ? 802  VOA A C9    1 
HETATM 2564 C  C10   . VOA C 3 .   ? 1.608   31.250  2.145   1.00 17.65 ? 802  VOA A C10   1 
HETATM 2565 C  C12   . VOA C 3 .   ? 0.301   31.420  0.222   1.00 18.41 ? 802  VOA A C12   1 
HETATM 2566 C  C1    . VOA C 3 .   ? 0.918   30.028  -4.796  1.00 18.99 ? 802  VOA A C1    1 
HETATM 2567 C  C15   . VOA C 3 .   ? -2.756  29.256  -4.152  1.00 16.98 ? 802  VOA A C15   1 
HETATM 2568 C  C16   . VOA C 3 .   ? -3.941  29.825  -4.623  1.00 19.43 ? 802  VOA A C16   1 
HETATM 2569 C  C17   . VOA C 3 .   ? -5.162  29.395  -4.190  1.00 18.14 ? 802  VOA A C17   1 
HETATM 2570 C  C18   . VOA C 3 .   ? -5.270  28.396  -3.207  1.00 17.64 ? 802  VOA A C18   1 
HETATM 2571 C  C19   . VOA C 3 .   ? -4.083  27.794  -2.708  1.00 17.99 ? 802  VOA A C19   1 
HETATM 2572 C  C2    . VOA C 3 .   ? -0.271  29.621  -3.915  1.00 17.76 ? 802  VOA A C2    1 
HETATM 2573 C  C20   . VOA C 3 .   ? -2.830  28.229  -3.214  1.00 17.61 ? 802  VOA A C20   1 
HETATM 2574 C  C21   . VOA C 3 .   ? -4.210  26.780  -1.714  1.00 16.22 ? 802  VOA A C21   1 
HETATM 2575 C  C22   . VOA C 3 .   ? -5.464  26.460  -1.257  1.00 17.55 ? 802  VOA A C22   1 
HETATM 2576 C  C23   . VOA C 3 .   ? -6.584  27.110  -1.792  1.00 17.50 ? 802  VOA A C23   1 
HETATM 2577 C  C25   . VOA C 3 .   ? -5.688  25.412  -0.192  1.00 16.75 ? 802  VOA A C25   1 
HETATM 2578 C  C27   . VOA C 3 .   ? -3.328  25.282  0.121   1.00 17.78 ? 802  VOA A C27   1 
HETATM 2579 C  C28   . VOA C 3 .   ? -2.982  26.111  -1.133  1.00 16.22 ? 802  VOA A C28   1 
HETATM 2580 N  N11   . VOA C 3 .   ? 0.613   31.800  1.461   1.00 19.27 ? 802  VOA A N11   1 
HETATM 2581 N  N14   . VOA C 3 .   ? -1.537  29.770  -4.658  1.00 18.04 ? 802  VOA A N14   1 
HETATM 2582 N  N24   . VOA C 3 .   ? -6.479  28.010  -2.749  1.00 19.17 ? 802  VOA A N24   1 
HETATM 2583 N  N6    . VOA C 3 .   ? 0.748   29.916  -1.723  1.00 16.57 ? 802  VOA A N6    1 
HETATM 2584 O  O26   . VOA C 3 .   ? -4.552  24.543  -0.066  1.00 17.12 ? 802  VOA A O26   1 
HETATM 2585 O  O5    . VOA C 3 .   ? -0.909  31.332  -2.361  1.00 18.58 ? 802  VOA A O5    1 
HETATM 2586 CL CL13  . VOA C 3 .   ? 1.968   31.797  3.760   1.00 19.64 ? 802  VOA A CL13  1 
HETATM 2587 H  H1    . VOA C 3 .   ? 2.638   29.008  -0.172  1.00 19.43 ? 802  VOA A H1    1 
HETATM 2588 H  H2    . VOA C 3 .   ? 3.161   29.770  2.128   1.00 20.37 ? 802  VOA A H2    1 
HETATM 2589 H  H4    . VOA C 3 .   ? -0.519  31.901  -0.291  1.00 22.12 ? 802  VOA A H4    1 
HETATM 2590 H  H7    . VOA C 3 .   ? 0.657   29.889  -5.845  1.00 22.81 ? 802  VOA A H7    1 
HETATM 2591 H  H6    . VOA C 3 .   ? 1.781   29.409  -4.551  1.00 22.81 ? 802  VOA A H6    1 
HETATM 2592 H  H5    . VOA C 3 .   ? 1.160   31.076  -4.617  1.00 22.81 ? 802  VOA A H5    1 
HETATM 2593 H  H8    . VOA C 3 .   ? -3.890  30.625  -5.347  1.00 23.34 ? 802  VOA A H8    1 
HETATM 2594 H  H9    . VOA C 3 .   ? -6.058  29.828  -4.609  1.00 21.79 ? 802  VOA A H9    1 
HETATM 2595 H  H3    . VOA C 3 .   ? -0.240  28.562  -3.656  1.00 21.33 ? 802  VOA A H3    1 
HETATM 2596 H  H10   . VOA C 3 .   ? -1.923  27.758  -2.867  1.00 21.16 ? 802  VOA A H10   1 
HETATM 2597 H  H11   . VOA C 3 .   ? -7.564  26.867  -1.408  1.00 21.03 ? 802  VOA A H11   1 
HETATM 2598 H  H13   . VOA C 3 .   ? -6.563  24.818  -0.455  1.00 20.12 ? 802  VOA A H13   1 
HETATM 2599 H  H12   . VOA C 3 .   ? -5.865  25.907  0.763   1.00 20.12 ? 802  VOA A H12   1 
HETATM 2600 H  H14   . VOA C 3 .   ? -3.447  25.956  0.970   1.00 21.36 ? 802  VOA A H14   1 
HETATM 2601 H  H15   . VOA C 3 .   ? -2.517  24.582  0.319   1.00 21.36 ? 802  VOA A H15   1 
HETATM 2602 H  H17   . VOA C 3 .   ? -2.256  26.877  -0.863  1.00 19.48 ? 802  VOA A H17   1 
HETATM 2603 H  H16   . VOA C 3 .   ? -2.549  25.452  -1.885  1.00 19.48 ? 802  VOA A H16   1 
HETATM 2604 H  H18   . VOA C 3 .   ? -1.535  30.230  -5.511  1.00 21.67 ? 802  VOA A H18   1 
HETATM 2605 H  H19   . VOA C 3 .   ? 1.289   29.168  -2.021  1.00 19.90 ? 802  VOA A H19   1 
HETATM 2606 C  C4    . VOA D 3 .   ? -3.556  33.757  -0.776  0.86 31.28 ? 803  VOA A C4    1 
HETATM 2607 C  C7    . VOA D 3 .   ? -2.837  35.347  0.947   0.86 36.26 ? 803  VOA A C7    1 
HETATM 2608 C  C8    . VOA D 3 .   ? -3.102  36.610  1.464   0.86 36.57 ? 803  VOA A C8    1 
HETATM 2609 C  C9    . VOA D 3 .   ? -2.528  36.971  2.668   0.86 35.88 ? 803  VOA A C9    1 
HETATM 2610 C  C10   . VOA D 3 .   ? -1.687  36.089  3.318   0.86 37.84 ? 803  VOA A C10   1 
HETATM 2611 C  C12   . VOA D 3 .   ? -1.954  34.518  1.642   0.86 37.37 ? 803  VOA A C12   1 
HETATM 2612 C  C1    . VOA D 3 .   ? -5.077  32.370  -2.285  0.86 33.57 ? 803  VOA A C1    1 
HETATM 2613 C  C15   . VOA D 3 .   ? -2.724  33.968  -4.305  0.86 38.51 ? 803  VOA A C15   1 
HETATM 2614 C  C16   . VOA D 3 .   ? -1.403  33.899  -4.793  0.86 40.23 ? 803  VOA A C16   1 
HETATM 2615 C  C17   . VOA D 3 .   ? -1.054  34.450  -5.986  0.86 42.10 ? 803  VOA A C17   1 
HETATM 2616 C  C18   . VOA D 3 .   ? -2.022  35.102  -6.768  0.86 45.01 ? 803  VOA A C18   1 
HETATM 2617 C  C19   . VOA D 3 .   ? -3.363  35.180  -6.305  0.86 44.84 ? 803  VOA A C19   1 
HETATM 2618 C  C2    . VOA D 3 .   ? -4.149  33.582  -2.163  0.86 33.08 ? 803  VOA A C2    1 
HETATM 2619 C  C20   . VOA D 3 .   ? -3.698  34.599  -5.059  0.86 41.57 ? 803  VOA A C20   1 
HETATM 2620 C  C21   . VOA D 3 .   ? -4.313  35.846  -7.124  0.86 47.42 ? 803  VOA A C21   1 
HETATM 2621 C  C22   . VOA D 3 .   ? -3.896  36.378  -8.310  0.86 48.16 ? 803  VOA A C22   1 
HETATM 2622 C  C23   . VOA D 3 .   ? -2.558  36.258  -8.692  0.86 47.66 ? 803  VOA A C23   1 
HETATM 2623 C  C25   . VOA D 3 .   ? -4.838  37.102  -9.240  0.86 49.14 ? 803  VOA A C25   1 
HETATM 2624 C  C27   . VOA D 3 .   ? -6.640  36.367  -7.881  0.86 49.05 ? 803  VOA A C27   1 
HETATM 2625 C  C28   . VOA D 3 .   ? -5.752  35.966  -6.695  0.86 49.02 ? 803  VOA A C28   1 
HETATM 2626 N  N11   . VOA D 3 .   ? -1.427  34.899  2.798   0.86 37.86 ? 803  VOA A N11   1 
HETATM 2627 N  N14   . VOA D 3 .   ? -2.989  33.368  -3.055  0.86 34.88 ? 803  VOA A N14   1 
HETATM 2628 N  N24   . VOA D 3 .   ? -1.681  35.644  -7.942  0.86 46.84 ? 803  VOA A N24   1 
HETATM 2629 N  N6    . VOA D 3 .   ? -3.415  35.016  -0.295  0.86 34.97 ? 803  VOA A N6    1 
HETATM 2630 O  O26   . VOA D 3 .   ? -6.039  37.473  -8.563  0.86 49.32 ? 803  VOA A O26   1 
HETATM 2631 O  O5    . VOA D 3 .   ? -3.155  32.804  -0.145  0.86 29.47 ? 803  VOA A O5    1 
HETATM 2632 CL CL13  . VOA D 3 .   ? -0.983  36.591  4.828   0.86 37.19 ? 803  VOA A CL13  1 
HETATM 2633 H  H1    . VOA D 3 .   ? -3.746  37.296  0.934   0.86 43.90 ? 803  VOA A H1    1 
HETATM 2634 H  H2    . VOA D 3 .   ? -2.736  37.940  3.099   0.86 43.08 ? 803  VOA A H2    1 
HETATM 2635 H  H4    . VOA D 3 .   ? -1.697  33.552  1.233   0.86 44.86 ? 803  VOA A H4    1 
HETATM 2636 H  H7    . VOA D 3 .   ? -5.597  32.406  -3.243  0.86 40.30 ? 803  VOA A H7    1 
HETATM 2637 H  H6    . VOA D 3 .   ? -5.807  32.388  -1.475  0.86 40.30 ? 803  VOA A H6    1 
HETATM 2638 H  H5    . VOA D 3 .   ? -4.490  31.454  -2.225  0.86 40.30 ? 803  VOA A H5    1 
HETATM 2639 H  H8    . VOA D 3 .   ? -0.650  33.396  -4.204  0.86 48.30 ? 803  VOA A H8    1 
HETATM 2640 H  H9    . VOA D 3 .   ? -0.033  34.387  -6.332  0.86 50.54 ? 803  VOA A H9    1 
HETATM 2641 H  H3    . VOA D 3 .   ? -4.753  34.455  -2.408  0.86 39.72 ? 803  VOA A H3    1 
HETATM 2642 H  H10   . VOA D 3 .   ? -4.714  34.648  -4.696  0.86 49.91 ? 803  VOA A H10   1 
HETATM 2643 H  H11   . VOA D 3 .   ? -2.240  36.684  -9.632  0.86 57.22 ? 803  VOA A H11   1 
HETATM 2644 H  H13   . VOA D 3 .   ? -5.086  36.450  -10.077 0.86 59.00 ? 803  VOA A H13   1 
HETATM 2645 H  H12   . VOA D 3 .   ? -4.348  37.999  -9.618  0.86 59.00 ? 803  VOA A H12   1 
HETATM 2646 H  H14   . VOA D 3 .   ? -7.626  36.656  -7.516  0.86 58.88 ? 803  VOA A H14   1 
HETATM 2647 H  H15   . VOA D 3 .   ? -6.735  35.524  -8.566  0.86 58.88 ? 803  VOA A H15   1 
HETATM 2648 H  H17   . VOA D 3 .   ? -5.831  36.724  -5.915  0.86 58.85 ? 803  VOA A H17   1 
HETATM 2649 H  H16   . VOA D 3 .   ? -6.089  35.007  -6.302  0.86 58.85 ? 803  VOA A H16   1 
HETATM 2650 H  H18   . VOA D 3 .   ? -2.325  32.735  -2.741  0.86 41.87 ? 803  VOA A H18   1 
HETATM 2651 H  H19   . VOA D 3 .   ? -3.737  35.745  -0.849  0.86 41.98 ? 803  VOA A H19   1 
HETATM 2652 C  C4    . VOA E 3 .   ? 0.159   39.037  0.424   0.74 34.86 ? 804  VOA A C4    1 
HETATM 2653 C  C7    . VOA E 3 .   ? 0.443   36.843  -0.569  0.74 36.82 ? 804  VOA A C7    1 
HETATM 2654 C  C8    . VOA E 3 .   ? 1.805   36.747  -0.279  0.74 37.38 ? 804  VOA A C8    1 
HETATM 2655 C  C9    . VOA E 3 .   ? 2.461   35.559  -0.539  0.74 38.37 ? 804  VOA A C9    1 
HETATM 2656 C  C10   . VOA E 3 .   ? 1.755   34.508  -1.093  0.74 40.31 ? 804  VOA A C10   1 
HETATM 2657 C  C12   . VOA E 3 .   ? -0.192  35.748  -1.139  0.74 38.04 ? 804  VOA A C12   1 
HETATM 2658 C  C1    . VOA E 3 .   ? -1.453  40.210  1.914   0.74 32.61 ? 804  VOA A C1    1 
HETATM 2659 C  C15   . VOA E 3 .   ? -1.350  40.914  -1.746  0.74 33.19 ? 804  VOA A C15   1 
HETATM 2660 C  C16   . VOA E 3 .   ? -2.402  41.330  -2.564  0.74 32.57 ? 804  VOA A C16   1 
HETATM 2661 C  C17   . VOA E 3 .   ? -2.173  41.838  -3.799  0.74 33.36 ? 804  VOA A C17   1 
HETATM 2662 C  C18   . VOA E 3 .   ? -0.860  41.943  -4.284  0.74 34.95 ? 804  VOA A C18   1 
HETATM 2663 C  C19   . VOA E 3 .   ? 0.224   41.520  -3.474  0.74 35.38 ? 804  VOA A C19   1 
HETATM 2664 C  C2    . VOA E 3 .   ? -0.690  40.268  0.590   0.74 33.56 ? 804  VOA A C2    1 
HETATM 2665 C  C20   . VOA E 3 .   ? -0.042  41.003  -2.189  0.74 34.27 ? 804  VOA A C20   1 
HETATM 2666 C  C21   . VOA E 3 .   ? 1.536   41.635  -3.994  0.74 37.18 ? 804  VOA A C21   1 
HETATM 2667 C  C22   . VOA E 3 .   ? 1.699   42.138  -5.250  0.74 37.34 ? 804  VOA A C22   1 
HETATM 2668 C  C23   . VOA E 3 .   ? 0.581   42.536  -5.985  0.74 36.50 ? 804  VOA A C23   1 
HETATM 2669 C  C25   . VOA E 3 .   ? 3.060   42.292  -5.884  0.74 38.17 ? 804  VOA A C25   1 
HETATM 2670 C  C27   . VOA E 3 .   ? 3.879   40.881  -4.134  0.74 38.76 ? 804  VOA A C27   1 
HETATM 2671 C  C28   . VOA E 3 .   ? 2.721   41.193  -3.183  0.74 37.83 ? 804  VOA A C28   1 
HETATM 2672 N  N11   . VOA E 3 .   ? 0.467   34.629  -1.372  0.74 39.21 ? 804  VOA A N11   1 
HETATM 2673 N  N14   . VOA E 3 .   ? -1.676  40.402  -0.487  0.74 33.51 ? 804  VOA A N14   1 
HETATM 2674 N  N24   . VOA E 3 .   ? -0.633  42.434  -5.504  0.74 36.57 ? 804  VOA A N24   1 
HETATM 2675 N  N6    . VOA E 3 .   ? -0.294  38.018  -0.344  0.74 35.69 ? 804  VOA A N6    1 
HETATM 2676 O  O26   . VOA E 3 .   ? 4.106   42.041  -4.942  0.74 38.94 ? 804  VOA A O26   1 
HETATM 2677 O  O5    . VOA E 3 .   ? 1.238   39.020  0.983   0.74 34.71 ? 804  VOA A O5    1 
HETATM 2678 CL CL13  . VOA E 3 .   ? 2.596   33.023  -1.423  0.74 43.19 ? 804  VOA A CL13  1 
HETATM 2679 H  H1    . VOA E 3 .   ? 2.338   37.587  0.142   0.74 44.88 ? 804  VOA A H1    1 
HETATM 2680 H  H2    . VOA E 3 .   ? 3.512   35.453  -0.312  0.74 46.07 ? 804  VOA A H2    1 
HETATM 2681 H  H4    . VOA E 3 .   ? -1.240  35.814  -1.394  0.74 45.67 ? 804  VOA A H4    1 
HETATM 2682 H  H7    . VOA E 3 .   ? -1.621  41.222  2.281   0.74 39.16 ? 804  VOA A H7    1 
HETATM 2683 H  H6    . VOA E 3 .   ? -0.869  39.651  2.646   0.74 39.16 ? 804  VOA A H6    1 
HETATM 2684 H  H5    . VOA E 3 .   ? -2.412  39.715  1.760   0.74 39.16 ? 804  VOA A H5    1 
HETATM 2685 H  H8    . VOA E 3 .   ? -3.418  41.243  -2.207  0.74 39.11 ? 804  VOA A H8    1 
HETATM 2686 H  H9    . VOA E 3 .   ? -3.001  42.164  -4.411  0.74 40.06 ? 804  VOA A H9    1 
HETATM 2687 H  H3    . VOA E 3 .   ? -0.013  41.122  0.566   0.74 40.29 ? 804  VOA A H3    1 
HETATM 2688 H  H10   . VOA E 3 .   ? 0.769   40.680  -1.555  0.74 41.15 ? 804  VOA A H10   1 
HETATM 2689 H  H11   . VOA E 3 .   ? 0.721   42.938  -6.978  0.74 43.82 ? 804  VOA A H11   1 
HETATM 2690 H  H13   . VOA E 3 .   ? 3.162   43.308  -6.266  0.74 45.83 ? 804  VOA A H13   1 
HETATM 2691 H  H12   . VOA E 3 .   ? 3.149   41.588  -6.711  0.74 45.83 ? 804  VOA A H12   1 
HETATM 2692 H  H14   . VOA E 3 .   ? 3.619   40.034  -4.768  0.74 46.53 ? 804  VOA A H14   1 
HETATM 2693 H  H15   . VOA E 3 .   ? 4.776   40.649  -3.560  0.74 46.53 ? 804  VOA A H15   1 
HETATM 2694 H  H17   . VOA E 3 .   ? 2.464   40.300  -2.613  0.74 45.41 ? 804  VOA A H17   1 
HETATM 2695 H  H16   . VOA E 3 .   ? 3.014   41.988  -2.497  0.74 45.41 ? 804  VOA A H16   1 
HETATM 2696 H  H18   . VOA E 3 .   ? -2.590  40.124  -0.319  0.74 40.23 ? 804  VOA A H18   1 
HETATM 2697 H  H19   . VOA E 3 .   ? -1.167  38.103  -0.758  0.74 42.85 ? 804  VOA A H19   1 
HETATM 2698 S  S     . SO4 F 4 .   ? -4.402  38.077  -1.815  1.00 52.37 ? 805  SO4 A S     1 
HETATM 2699 O  O1    . SO4 F 4 .   ? -2.973  37.754  -1.905  1.00 53.48 ? 805  SO4 A O1    1 
HETATM 2700 O  O2    . SO4 F 4 .   ? -4.866  38.619  -3.093  1.00 52.43 ? 805  SO4 A O2    1 
HETATM 2701 O  O3    . SO4 F 4 .   ? -5.152  36.864  -1.483  1.00 52.40 ? 805  SO4 A O3    1 
HETATM 2702 O  O4    . SO4 F 4 .   ? -4.614  39.071  -0.765  1.00 54.55 ? 805  SO4 A O4    1 
HETATM 2703 O  O     . HOH G 5 .   ? -5.179  43.316  -5.829  1.00 53.29 ? 901  HOH A O     1 
HETATM 2704 O  O     . HOH G 5 .   ? -20.479 18.569  13.916  1.00 35.49 ? 902  HOH A O     1 
HETATM 2705 O  O     . HOH G 5 .   ? -5.004  27.686  -18.332 1.00 48.67 ? 903  HOH A O     1 
HETATM 2706 O  O     . HOH G 5 .   ? -31.487 33.395  9.196   1.00 48.32 ? 904  HOH A O     1 
HETATM 2707 O  O     . HOH G 5 .   ? -11.663 10.202  -2.686  1.00 41.83 ? 905  HOH A O     1 
HETATM 2708 O  O     . HOH G 5 .   ? -0.873  24.677  15.664  1.00 44.58 ? 906  HOH A O     1 
HETATM 2709 O  O     . HOH G 5 .   ? -33.455 18.947  9.186   1.00 43.86 ? 907  HOH A O     1 
HETATM 2710 O  O     . HOH G 5 .   ? -13.004 -8.966  -2.079  1.00 35.40 ? 908  HOH A O     1 
HETATM 2711 O  O     . HOH G 5 .   ? -22.011 30.597  18.397  1.00 41.30 ? 909  HOH A O     1 
HETATM 2712 O  O     . HOH G 5 .   ? -13.625 25.741  -18.795 1.00 51.51 ? 910  HOH A O     1 
HETATM 2713 O  O     . HOH G 5 .   ? 5.222   36.653  -7.601  1.00 64.92 ? 911  HOH A O     1 
HETATM 2714 O  O     . HOH G 5 .   ? -27.809 23.266  -18.238 1.00 37.95 ? 912  HOH A O     1 
HETATM 2715 O  O     . HOH G 5 .   ? -32.125 18.894  12.450  1.00 45.15 ? 913  HOH A O     1 
HETATM 2716 O  O     . HOH G 5 .   ? 17.251  13.495  21.376  1.00 46.03 ? 914  HOH A O     1 
HETATM 2717 O  O     . HOH G 5 .   ? -13.294 24.462  -21.379 1.00 37.71 ? 915  HOH A O     1 
HETATM 2718 O  O     . HOH G 5 .   ? -6.064  3.165   6.386   1.00 32.12 ? 916  HOH A O     1 
HETATM 2719 O  O     . HOH G 5 .   ? -19.855 35.845  14.014  1.00 39.14 ? 917  HOH A O     1 
HETATM 2720 O  O     . HOH G 5 .   ? -32.157 28.236  2.078   1.00 43.65 ? 918  HOH A O     1 
HETATM 2721 O  O     . HOH G 5 .   ? -11.947 14.614  -8.369  1.00 40.83 ? 919  HOH A O     1 
HETATM 2722 O  O     . HOH G 5 .   ? -11.467 16.083  -5.875  1.00 24.98 ? 920  HOH A O     1 
HETATM 2723 O  O     . HOH G 5 .   ? -9.938  17.015  -10.869 1.00 49.14 ? 921  HOH A O     1 
HETATM 2724 O  O     . HOH G 5 .   ? -5.636  43.282  -1.319  1.00 34.34 ? 922  HOH A O     1 
HETATM 2725 O  O     . HOH G 5 .   ? -32.175 16.000  14.117  1.00 48.92 ? 923  HOH A O     1 
HETATM 2726 O  O     . HOH G 5 .   ? -11.522 32.972  -6.120  1.00 45.52 ? 924  HOH A O     1 
HETATM 2727 O  O     . HOH G 5 .   ? -25.564 31.119  -5.628  1.00 22.52 ? 925  HOH A O     1 
HETATM 2728 O  O     . HOH G 5 .   ? -23.876 35.781  12.089  1.00 35.76 ? 926  HOH A O     1 
HETATM 2729 O  O     . HOH G 5 .   ? 16.990  7.239   23.077  1.00 39.39 ? 927  HOH A O     1 
HETATM 2730 O  O     . HOH G 5 .   ? -24.997 38.740  9.177   1.00 39.56 ? 928  HOH A O     1 
HETATM 2731 O  O     . HOH G 5 .   ? -32.961 17.037  -0.749  1.00 38.60 ? 929  HOH A O     1 
HETATM 2732 O  O     . HOH G 5 .   ? -1.002  33.798  5.202   1.00 51.57 ? 930  HOH A O     1 
HETATM 2733 O  O     . HOH G 5 .   ? 4.921   15.425  -0.744  1.00 26.11 ? 931  HOH A O     1 
HETATM 2734 O  O     . HOH G 5 .   ? -13.385 7.790   -0.511  1.00 22.18 ? 932  HOH A O     1 
HETATM 2735 O  O     . HOH G 5 .   ? -39.048 3.019   10.470  1.00 52.17 ? 933  HOH A O     1 
HETATM 2736 O  O     . HOH G 5 .   ? -24.970 0.826   -15.721 1.00 44.02 ? 934  HOH A O     1 
HETATM 2737 O  O     . HOH G 5 .   ? -29.012 22.643  -14.629 1.00 40.45 ? 935  HOH A O     1 
HETATM 2738 O  O     . HOH G 5 .   ? -6.699  19.639  4.766   1.00 18.64 ? 936  HOH A O     1 
HETATM 2739 O  O     . HOH G 5 .   ? -13.470 18.380  1.772   1.00 40.22 ? 937  HOH A O     1 
HETATM 2740 O  O     . HOH G 5 .   ? -11.980 29.737  19.998  1.00 48.96 ? 938  HOH A O     1 
HETATM 2741 O  O     . HOH G 5 .   ? -10.120 27.741  -12.298 1.00 22.96 ? 939  HOH A O     1 
HETATM 2742 O  O     . HOH G 5 .   ? -31.081 17.852  7.991   1.00 19.53 ? 940  HOH A O     1 
HETATM 2743 O  O     . HOH G 5 .   ? -15.133 23.898  -16.677 1.00 36.55 ? 941  HOH A O     1 
HETATM 2744 O  O     . HOH G 5 .   ? -4.859  18.520  18.810  1.00 32.56 ? 942  HOH A O     1 
HETATM 2745 O  O     . HOH G 5 .   ? 9.490   10.174  15.180  1.00 18.82 ? 943  HOH A O     1 
HETATM 2746 O  O     . HOH G 5 .   ? -22.529 23.239  17.512  1.00 53.73 ? 944  HOH A O     1 
HETATM 2747 O  O     . HOH G 5 .   ? -22.980 0.329   13.707  1.00 20.28 ? 945  HOH A O     1 
HETATM 2748 O  O     . HOH G 5 .   ? -4.938  19.902  15.185  1.00 20.97 ? 946  HOH A O     1 
HETATM 2749 O  O     . HOH G 5 .   ? -26.423 21.722  10.082  1.00 27.23 ? 947  HOH A O     1 
HETATM 2750 O  O     . HOH G 5 .   ? -21.872 46.328  11.755  1.00 50.63 ? 948  HOH A O     1 
HETATM 2751 O  O     . HOH G 5 .   ? -4.075  27.607  7.864   1.00 20.78 ? 949  HOH A O     1 
HETATM 2752 O  O     . HOH G 5 .   ? -14.798 15.759  -12.805 1.00 48.28 ? 950  HOH A O     1 
HETATM 2753 O  O     . HOH G 5 .   ? -9.922  -3.459  -8.346  1.00 65.61 ? 951  HOH A O     1 
HETATM 2754 O  O     . HOH G 5 .   ? -36.492 16.934  9.508   1.00 35.11 ? 952  HOH A O     1 
HETATM 2755 O  O     . HOH G 5 .   ? -12.399 29.786  -1.492  1.00 17.40 ? 953  HOH A O     1 
HETATM 2756 O  O     . HOH G 5 .   ? -38.703 6.409   6.960   1.00 29.17 ? 954  HOH A O     1 
HETATM 2757 O  O     . HOH G 5 .   ? -28.562 40.169  0.232   1.00 52.67 ? 955  HOH A O     1 
HETATM 2758 O  O     . HOH G 5 .   ? -19.724 22.941  13.800  1.00 23.05 ? 956  HOH A O     1 
HETATM 2759 O  O     . HOH G 5 .   ? -13.879 18.995  -3.008  1.00 17.81 ? 957  HOH A O     1 
HETATM 2760 O  O     . HOH G 5 .   ? -19.925 21.818  11.310  1.00 18.26 ? 958  HOH A O     1 
HETATM 2761 O  O     . HOH G 5 .   ? 12.215  17.322  18.234  1.00 25.85 ? 959  HOH A O     1 
HETATM 2762 O  O     . HOH G 5 .   ? -22.658 3.048   14.503  1.00 19.96 ? 960  HOH A O     1 
HETATM 2763 O  O     . HOH G 5 .   ? -25.328 42.781  0.855   1.00 32.23 ? 961  HOH A O     1 
HETATM 2764 O  O     . HOH G 5 .   ? -21.463 47.710  -6.159  1.00 43.01 ? 962  HOH A O     1 
HETATM 2765 O  O     . HOH G 5 .   ? -31.665 19.671  -6.202  1.00 35.55 ? 963  HOH A O     1 
HETATM 2766 O  O     . HOH G 5 .   ? -29.466 7.015   14.438  1.00 44.80 ? 964  HOH A O     1 
HETATM 2767 O  O     . HOH G 5 .   ? 4.496   29.420  -3.881  1.00 21.34 ? 965  HOH A O     1 
HETATM 2768 O  O     . HOH G 5 .   ? -33.595 1.499   6.821   1.00 39.15 ? 966  HOH A O     1 
HETATM 2769 O  O     . HOH G 5 .   ? -14.655 19.491  21.254  1.00 36.83 ? 967  HOH A O     1 
HETATM 2770 O  O     . HOH G 5 .   ? -17.154 33.155  15.669  1.00 24.41 ? 968  HOH A O     1 
HETATM 2771 O  O     . HOH G 5 .   ? -5.693  29.380  18.508  1.00 28.05 ? 969  HOH A O     1 
HETATM 2772 O  O     . HOH G 5 .   ? -2.353  25.687  11.684  1.00 18.59 ? 970  HOH A O     1 
HETATM 2773 O  O     . HOH G 5 .   ? -5.279  42.620  7.542   1.00 42.48 ? 971  HOH A O     1 
HETATM 2774 O  O     . HOH G 5 .   ? -29.071 4.279   15.008  1.00 26.20 ? 972  HOH A O     1 
HETATM 2775 O  O     . HOH G 5 .   ? -13.523 32.507  -16.495 1.00 42.47 ? 973  HOH A O     1 
HETATM 2776 O  O     . HOH G 5 .   ? -9.301  -3.626  4.688   1.00 23.97 ? 974  HOH A O     1 
HETATM 2777 O  O     . HOH G 5 .   ? -20.853 29.998  -14.538 1.00 23.59 ? 975  HOH A O     1 
HETATM 2778 O  O     . HOH G 5 .   ? -20.516 9.350   17.545  1.00 36.25 ? 976  HOH A O     1 
HETATM 2779 O  O     . HOH G 5 .   ? -30.470 27.804  -2.351  1.00 24.11 ? 977  HOH A O     1 
HETATM 2780 O  O     . HOH G 5 .   ? -8.663  29.690  -3.641  1.00 21.80 ? 978  HOH A O     1 
HETATM 2781 O  O     . HOH G 5 .   ? -23.620 6.753   16.438  1.00 43.54 ? 979  HOH A O     1 
HETATM 2782 O  O     . HOH G 5 .   ? -18.993 32.176  18.004  1.00 53.94 ? 980  HOH A O     1 
HETATM 2783 O  O     . HOH G 5 .   ? -34.047 19.833  1.681   1.00 36.18 ? 981  HOH A O     1 
HETATM 2784 O  O     . HOH G 5 .   ? -26.564 37.673  4.600   1.00 30.67 ? 982  HOH A O     1 
HETATM 2785 O  O     . HOH G 5 .   ? -21.268 24.974  6.622   1.00 17.65 ? 983  HOH A O     1 
HETATM 2786 O  O     . HOH G 5 .   ? 12.026  19.549  16.654  1.00 28.73 ? 984  HOH A O     1 
HETATM 2787 O  O     . HOH G 5 .   ? -8.024  35.385  16.603  1.00 40.34 ? 985  HOH A O     1 
HETATM 2788 O  O     . HOH G 5 .   ? -24.540 20.746  13.897  1.00 52.17 ? 986  HOH A O     1 
HETATM 2789 O  O     . HOH G 5 .   ? -24.388 23.007  11.954  1.00 39.07 ? 987  HOH A O     1 
HETATM 2790 O  O     . HOH G 5 .   ? -8.776  22.975  -0.597  1.00 17.05 ? 988  HOH A O     1 
HETATM 2791 O  O     . HOH G 5 .   ? -14.888 17.990  -6.358  1.00 22.95 ? 989  HOH A O     1 
HETATM 2792 O  O     . HOH G 5 .   ? -6.415  41.039  -3.132  1.00 34.96 ? 990  HOH A O     1 
HETATM 2793 O  O     . HOH G 5 .   ? 2.949   23.260  -9.730  1.00 31.93 ? 991  HOH A O     1 
HETATM 2794 O  O     . HOH G 5 .   ? -14.256 16.167  16.422  1.00 24.85 ? 992  HOH A O     1 
HETATM 2795 O  O     . HOH G 5 .   ? 7.678   11.621  16.915  1.00 19.97 ? 993  HOH A O     1 
HETATM 2796 O  O     . HOH G 5 .   ? -9.630  29.754  0.563   1.00 18.65 ? 994  HOH A O     1 
HETATM 2797 O  O     . HOH G 5 .   ? 5.492   7.919   15.272  1.00 27.53 ? 995  HOH A O     1 
HETATM 2798 O  O     . HOH G 5 .   ? -31.632 12.794  -5.078  1.00 42.43 ? 996  HOH A O     1 
HETATM 2799 O  O     . HOH G 5 .   ? -17.056 36.428  -10.617 1.00 45.74 ? 997  HOH A O     1 
HETATM 2800 O  O     . HOH G 5 .   ? 11.669  12.593  17.560  1.00 21.24 ? 998  HOH A O     1 
HETATM 2801 O  O     . HOH G 5 .   ? -36.603 9.737   7.863   1.00 37.81 ? 999  HOH A O     1 
HETATM 2802 O  O     . HOH G 5 .   ? -6.436  23.797  -18.705 1.00 49.81 ? 1000 HOH A O     1 
HETATM 2803 O  O     . HOH G 5 .   ? -25.181 6.051   12.731  1.00 23.41 ? 1001 HOH A O     1 
HETATM 2804 O  O     . HOH G 5 .   ? -4.112  25.392  9.377   1.00 16.59 ? 1002 HOH A O     1 
HETATM 2805 O  O     . HOH G 5 .   ? -26.064 34.323  -16.328 1.00 50.69 ? 1003 HOH A O     1 
HETATM 2806 O  O     . HOH G 5 .   ? -30.531 24.089  -11.084 1.00 34.07 ? 1004 HOH A O     1 
HETATM 2807 O  O     . HOH G 5 .   ? -12.685 16.656  -32.446 1.00 51.26 ? 1005 HOH A O     1 
HETATM 2808 O  O     . HOH G 5 .   ? -13.430 47.525  -11.672 1.00 40.46 ? 1006 HOH A O     1 
HETATM 2809 O  O     . HOH G 5 .   ? -7.215  31.638  19.444  1.00 45.51 ? 1007 HOH A O     1 
HETATM 2810 O  O     . HOH G 5 .   ? -4.875  17.936  11.036  1.00 25.22 ? 1008 HOH A O     1 
HETATM 2811 O  O     . HOH G 5 .   ? -6.252  22.116  -1.815  1.00 22.66 ? 1009 HOH A O     1 
HETATM 2812 O  O     . HOH G 5 .   ? -24.278 8.989   -6.795  1.00 31.03 ? 1010 HOH A O     1 
HETATM 2813 O  O     . HOH G 5 .   ? -19.416 15.501  14.822  1.00 36.50 ? 1011 HOH A O     1 
HETATM 2814 O  O     . HOH G 5 .   ? 15.304  13.920  19.261  1.00 34.60 ? 1012 HOH A O     1 
HETATM 2815 O  O     . HOH G 5 .   ? 5.390   10.012  17.049  1.00 27.18 ? 1013 HOH A O     1 
HETATM 2816 O  O     . HOH G 5 .   ? -9.603  6.634   -5.288  1.00 43.48 ? 1014 HOH A O     1 
HETATM 2817 O  O     . HOH G 5 .   ? -28.155 28.992  -14.785 1.00 30.97 ? 1015 HOH A O     1 
HETATM 2818 O  O     . HOH G 5 .   ? -19.717 14.903  -11.316 1.00 49.07 ? 1016 HOH A O     1 
HETATM 2819 O  O     . HOH G 5 .   ? -8.232  32.081  -5.258  1.00 38.00 ? 1017 HOH A O     1 
HETATM 2820 O  O     . HOH G 5 .   ? -15.350 12.328  -21.640 1.00 51.41 ? 1018 HOH A O     1 
HETATM 2821 O  O     . HOH G 5 .   ? -20.255 9.667   -7.369  1.00 32.13 ? 1019 HOH A O     1 
HETATM 2822 O  O     . HOH G 5 .   ? -16.561 15.034  14.891  1.00 25.07 ? 1020 HOH A O     1 
HETATM 2823 O  O     . HOH G 5 .   ? -3.221  30.383  17.427  1.00 31.00 ? 1021 HOH A O     1 
HETATM 2824 O  O     . HOH G 5 .   ? -8.879  39.270  -6.167  1.00 22.97 ? 1022 HOH A O     1 
HETATM 2825 O  O     . HOH G 5 .   ? -6.778  14.516  1.749   1.00 22.41 ? 1023 HOH A O     1 
HETATM 2826 O  O     . HOH G 5 .   ? -11.596 30.473  2.550   1.00 19.88 ? 1024 HOH A O     1 
HETATM 2827 O  O     . HOH G 5 .   ? -25.760 8.551   13.792  1.00 32.94 ? 1025 HOH A O     1 
HETATM 2828 O  O     . HOH G 5 .   ? -22.658 4.626   12.033  1.00 31.52 ? 1026 HOH A O     1 
HETATM 2829 O  O     . HOH G 5 .   ? -22.574 -0.091  -15.562 1.00 40.14 ? 1027 HOH A O     1 
HETATM 2830 O  O     . HOH G 5 .   ? -10.481 28.601  -5.291  1.00 19.34 ? 1028 HOH A O     1 
HETATM 2831 O  O     . HOH G 5 .   ? -10.704 46.229  -10.313 1.00 42.00 ? 1029 HOH A O     1 
HETATM 2832 O  O     . HOH G 5 .   ? -12.622 27.933  -3.662  1.00 17.85 ? 1030 HOH A O     1 
HETATM 2833 O  O     . HOH G 5 .   ? -18.092 0.549   -4.317  1.00 50.97 ? 1031 HOH A O     1 
HETATM 2834 O  O     . HOH G 5 .   ? 1.250   25.742  -13.193 1.00 30.91 ? 1032 HOH A O     1 
HETATM 2835 O  O     . HOH G 5 .   ? -33.379 5.893   12.495  1.00 26.33 ? 1033 HOH A O     1 
HETATM 2836 O  O     . HOH G 5 .   ? -4.492  15.711  8.815   1.00 23.38 ? 1034 HOH A O     1 
HETATM 2837 O  O     . HOH G 5 .   ? -7.529  14.828  -0.767  1.00 39.93 ? 1035 HOH A O     1 
HETATM 2838 O  O     . HOH G 5 .   ? -23.300 12.550  -12.833 1.00 43.51 ? 1036 HOH A O     1 
HETATM 2839 O  O     . HOH G 5 .   ? -21.650 32.347  -16.289 1.00 39.55 ? 1037 HOH A O     1 
HETATM 2840 O  O     . HOH G 5 .   ? -34.500 17.257  2.208   1.00 30.45 ? 1038 HOH A O     1 
HETATM 2841 O  O     . HOH G 5 .   ? -9.314  10.120  -0.462  1.00 23.56 ? 1039 HOH A O     1 
HETATM 2842 O  O     . HOH G 5 .   ? -9.354  40.611  -3.534  1.00 22.87 ? 1040 HOH A O     1 
HETATM 2843 O  O     . HOH G 5 .   ? -14.717 51.708  3.940   1.00 39.70 ? 1041 HOH A O     1 
HETATM 2844 O  O     . HOH G 5 .   ? -36.387 5.355   -0.596  1.00 28.53 ? 1042 HOH A O     1 
HETATM 2845 O  O     . HOH G 5 .   ? -10.285 34.751  -15.225 1.00 36.29 ? 1043 HOH A O     1 
HETATM 2846 O  O     . HOH G 5 .   ? -31.692 30.515  6.222   1.00 37.19 ? 1044 HOH A O     1 
HETATM 2847 O  O     . HOH G 5 .   ? -17.897 1.677   19.343  1.00 45.56 ? 1045 HOH A O     1 
HETATM 2848 O  O     . HOH G 5 .   ? -31.275 17.396  -5.271  1.00 41.62 ? 1046 HOH A O     1 
HETATM 2849 O  O     . HOH G 5 .   ? -17.037 16.771  -13.600 1.00 48.68 ? 1047 HOH A O     1 
HETATM 2850 O  O     . HOH G 5 .   ? -0.905  28.442  17.893  1.00 48.30 ? 1048 HOH A O     1 
HETATM 2851 O  O     . HOH G 5 .   ? -15.949 33.012  -18.757 1.00 59.05 ? 1049 HOH A O     1 
HETATM 2852 O  O     . HOH G 5 .   ? -8.886  43.466  -5.514  1.00 35.08 ? 1050 HOH A O     1 
HETATM 2853 O  O     . HOH G 5 .   ? -9.693  21.669  22.512  1.00 41.79 ? 1051 HOH A O     1 
HETATM 2854 O  O     . HOH G 5 .   ? -31.380 30.553  -2.777  1.00 34.79 ? 1052 HOH A O     1 
HETATM 2855 O  O     . HOH G 5 .   ? -3.738  22.269  16.562  1.00 21.90 ? 1053 HOH A O     1 
HETATM 2856 O  O     . HOH G 5 .   ? -31.765 26.596  -0.078  1.00 26.83 ? 1054 HOH A O     1 
HETATM 2857 O  O     . HOH G 5 .   ? -17.891 30.864  -20.468 1.00 53.76 ? 1055 HOH A O     1 
HETATM 2858 O  O     . HOH G 5 .   ? -10.547 33.069  -7.807  1.00 42.03 ? 1056 HOH A O     1 
HETATM 2859 O  O     . HOH G 5 .   ? -30.604 7.430   -11.228 1.00 57.30 ? 1057 HOH A O     1 
HETATM 2860 O  O     . HOH G 5 .   ? -24.081 38.647  12.635  1.00 46.95 ? 1058 HOH A O     1 
HETATM 2861 O  O     . HOH G 5 .   ? -15.727 9.834   -18.784 1.00 57.16 ? 1059 HOH A O     1 
HETATM 2862 O  O     . HOH G 5 .   ? -37.194 8.556   10.420  1.00 40.17 ? 1060 HOH A O     1 
HETATM 2863 O  O     . HOH G 5 .   ? -30.601 27.296  -13.848 1.00 49.88 ? 1061 HOH A O     1 
HETATM 2864 O  O     . HOH G 5 .   ? 7.448   16.912  -1.197  1.00 22.53 ? 1062 HOH A O     1 
HETATM 2865 O  O     . HOH G 5 .   ? -25.422 13.431  -14.073 1.00 58.40 ? 1063 HOH A O     1 
HETATM 2866 O  O     . HOH G 5 .   ? -4.230  44.162  9.361   1.00 43.32 ? 1064 HOH A O     1 
HETATM 2867 O  O     . HOH G 5 .   ? -33.368 3.939   14.646  1.00 41.82 ? 1065 HOH A O     1 
HETATM 2868 O  O     . HOH G 5 .   ? 4.968   8.579   19.621  1.00 49.12 ? 1066 HOH A O     1 
HETATM 2869 O  O     . HOH G 5 .   ? -5.624  18.916  21.581  1.00 58.24 ? 1067 HOH A O     1 
HETATM 2870 O  O     . HOH G 5 .   ? -38.035 2.169   7.726   1.00 38.47 ? 1068 HOH A O     1 
HETATM 2871 O  O     . HOH G 5 .   ? 6.888   30.567  -3.339  1.00 24.83 ? 1069 HOH A O     1 
HETATM 2872 O  O     . HOH G 5 .   ? -26.090 19.649  16.313  1.00 42.39 ? 1070 HOH A O     1 
HETATM 2873 O  O     . HOH G 5 .   ? -22.534 13.072  -10.117 1.00 41.83 ? 1071 HOH A O     1 
HETATM 2874 O  O     . HOH G 5 .   ? -5.445  27.434  20.492  1.00 51.98 ? 1072 HOH A O     1 
HETATM 2875 O  O     . HOH G 5 .   ? -7.101  41.419  -6.154  1.00 42.95 ? 1073 HOH A O     1 
HETATM 2876 O  O     . HOH G 5 .   ? -18.504 7.691   18.432  1.00 29.42 ? 1074 HOH A O     1 
HETATM 2877 O  O     . HOH G 5 .   ? -19.476 19.746  20.973  1.00 41.93 ? 1075 HOH A O     1 
HETATM 2878 O  O     . HOH G 5 .   ? -3.659  43.649  5.139   1.00 47.36 ? 1076 HOH A O     1 
HETATM 2879 O  O     . HOH G 5 .   ? -33.857 -1.276  13.906  1.00 39.21 ? 1077 HOH A O     1 
HETATM 2880 O  O     . HOH G 5 .   ? 0.490   27.024  15.689  1.00 26.81 ? 1078 HOH A O     1 
HETATM 2881 O  O     . HOH G 5 .   ? -39.689 3.786   6.247   1.00 46.53 ? 1079 HOH A O     1 
HETATM 2882 O  O     . HOH G 5 .   ? -27.121 8.014   15.815  1.00 51.99 ? 1080 HOH A O     1 
HETATM 2883 O  O     . HOH G 5 .   ? -32.724 8.542   -3.174  1.00 41.85 ? 1081 HOH A O     1 
HETATM 2884 O  O     . HOH G 5 .   ? -13.673 51.821  0.545   1.00 44.04 ? 1082 HOH A O     1 
HETATM 2885 O  O     . HOH G 5 .   ? -30.839 3.958   17.057  1.00 51.89 ? 1083 HOH A O     1 
HETATM 2886 O  O     . HOH G 5 .   ? -22.219 23.268  14.790  1.00 45.35 ? 1084 HOH A O     1 
HETATM 2887 O  O     . HOH G 5 .   ? -3.487  18.587  13.372  1.00 31.71 ? 1085 HOH A O     1 
HETATM 2888 O  O     . HOH G 5 .   ? -33.942 28.791  6.567   1.00 58.64 ? 1086 HOH A O     1 
HETATM 2889 O  O     . HOH G 5 .   ? 7.639   39.832  -3.511  1.00 46.55 ? 1087 HOH A O     1 
HETATM 2890 O  O     . HOH G 5 .   ? -2.384  17.581  17.828  1.00 43.92 ? 1088 HOH A O     1 
HETATM 2891 O  O     . HOH G 5 .   ? 5.002   39.378  -1.449  1.00 50.63 ? 1089 HOH A O     1 
HETATM 2892 O  O     . HOH G 5 .   ? 2.071   43.438  0.433   1.00 56.38 ? 1090 HOH A O     1 
HETATM 2893 O  O     . HOH G 5 .   ? 12.895  15.168  16.825  1.00 27.39 ? 1091 HOH A O     1 
HETATM 2894 O  O     . HOH G 5 .   ? -27.088 3.553   16.440  1.00 39.74 ? 1092 HOH A O     1 
HETATM 2895 O  O     . HOH G 5 .   ? -3.857  21.393  18.997  1.00 51.13 ? 1093 HOH A O     1 
HETATM 2896 O  O     . HOH G 5 .   ? 6.109   19.769  20.377  1.00 48.68 ? 1094 HOH A O     1 
HETATM 2897 O  O     . HOH G 5 .   ? -21.036 -1.219  15.095  1.00 36.33 ? 1095 HOH A O     1 
HETATM 2898 O  O     . HOH G 5 .   ? -35.335 7.962   12.645  1.00 45.09 ? 1096 HOH A O     1 
HETATM 2899 O  O     . HOH G 5 .   ? 0.000   44.793  -1.155  0.50 50.63 ? 1097 HOH A O     1 
HETATM 2900 O  O     . HOH G 5 .   ? -25.039 35.418  14.590  1.00 41.59 ? 1098 HOH A O     1 
HETATM 2901 O  O     . HOH G 5 .   ? -25.095 4.732   15.341  1.00 42.27 ? 1099 HOH A O     1 
HETATM 2902 O  O     . HOH G 5 .   ? -1.877  18.964  15.542  1.00 59.89 ? 1100 HOH A O     1 
HETATM 2903 O  O     . HOH G 5 .   ? -14.133 22.908  24.607  1.00 49.09 ? 1101 HOH A O     1 
HETATM 2904 O  O     . HOH G 5 .   ? 10.213  40.346  -7.118  1.00 53.28 ? 1102 HOH A O     1 
HETATM 2905 O  O     . HOH G 5 .   ? 2.013   43.913  8.484   1.00 49.12 ? 1103 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     . THR A 42  ? 0.8139 0.8650 0.8639 -0.0824 -0.0579 -0.0392 27   THR A N     
2    C  CA    . THR A 42  ? 0.8188 0.8652 0.8638 -0.0749 -0.0473 -0.0291 27   THR A CA    
3    C  C     . THR A 42  ? 0.8031 0.8380 0.8238 -0.0686 -0.0408 0.0019  27   THR A C     
4    O  O     . THR A 42  ? 0.7975 0.8377 0.8316 -0.0687 -0.0388 0.0176  27   THR A O     
5    C  CB    . THR A 42  ? 0.8363 0.8838 0.8895 -0.0781 -0.0459 -0.0463 27   THR A CB    
6    O  OG1   . THR A 42  ? 0.8509 0.8866 0.9036 -0.0734 -0.0490 -0.0533 27   THR A OG1   
7    C  CG2   . THR A 42  ? 0.8456 0.9039 0.9037 -0.0811 -0.0391 -0.0496 27   THR A CG2   
8    N  N     . ASP A 43  ? 0.7821 0.8011 0.7642 -0.0591 -0.0416 0.0207  28   ASP A N     
9    C  CA    . ASP A 43  ? 0.7465 0.7445 0.6984 -0.0354 -0.0479 0.0485  28   ASP A CA    
10   C  C     . ASP A 43  ? 0.6575 0.6649 0.5860 -0.0158 -0.0441 0.0745  28   ASP A C     
11   O  O     . ASP A 43  ? 0.6445 0.6764 0.5612 -0.0184 -0.0421 0.1095  28   ASP A O     
12   C  CB    . ASP A 43  ? 0.7871 0.7697 0.7416 -0.0183 -0.0626 0.0528  28   ASP A CB    
13   C  CG    . ASP A 43  ? 0.8146 0.7877 0.7758 -0.0023 -0.0627 0.0671  28   ASP A CG    
14   O  OD1   . ASP A 43  ? 0.8293 0.7839 0.7916 0.0396  -0.0805 0.0637  28   ASP A OD1   
15   O  OD2   . ASP A 43  ? 0.8144 0.8095 0.7786 -0.0213 -0.0444 0.0856  28   ASP A OD2   
16   N  N     . PRO A 44  ? 0.5703 0.5790 0.5039 0.0088  -0.0447 0.0572  29   PRO A N     
17   C  CA    . PRO A 44  ? 0.4989 0.5019 0.4411 0.0120  -0.0361 0.0516  29   PRO A CA    
18   C  C     . PRO A 44  ? 0.4457 0.4332 0.3717 0.0243  -0.0320 0.0273  29   PRO A C     
19   O  O     . PRO A 44  ? 0.4356 0.4219 0.3758 0.0322  -0.0258 0.0340  29   PRO A O     
20   C  CB    . PRO A 44  ? 0.4991 0.5077 0.4639 0.0123  -0.0265 0.0610  29   PRO A CB    
21   C  CG    . PRO A 44  ? 0.5191 0.5451 0.4896 0.0239  -0.0123 0.0482  29   PRO A CG    
22   C  CD    . PRO A 44  ? 0.5449 0.5550 0.4933 0.0244  -0.0273 0.0595  29   PRO A CD    
23   N  N     . VAL A 45  ? 0.3855 0.3777 0.3110 0.0294  -0.0331 -0.0146 30   VAL A N     
24   C  CA    . VAL A 45  ? 0.3432 0.3362 0.3030 0.0336  0.0038  -0.0110 30   VAL A CA    
25   C  C     . VAL A 45  ? 0.3369 0.2838 0.3256 0.0062  0.0064  -0.0056 30   VAL A C     
26   O  O     . VAL A 45  ? 0.3411 0.3024 0.3471 0.0554  0.0178  0.0074  30   VAL A O     
27   C  CB    . VAL A 45  ? 0.3316 0.3035 0.2684 0.0688  0.0426  -0.0226 30   VAL A CB    
28   C  CG1   . VAL A 45  ? 0.3696 0.3346 0.2554 0.0644  0.0148  0.0102  30   VAL A CG1   
29   C  CG2   . VAL A 45  ? 0.3480 0.3252 0.3045 0.0595  0.0667  -0.0213 30   VAL A CG2   
30   N  N     . PRO A 46  ? 0.3534 0.2971 0.3376 -0.0230 0.0054  0.0139  31   PRO A N     
31   C  CA    . PRO A 46  ? 0.3658 0.2881 0.3285 -0.0290 0.0056  -0.0002 31   PRO A CA    
32   C  C     . PRO A 46  ? 0.3561 0.2789 0.2828 0.0123  0.0036  -0.0154 31   PRO A C     
33   O  O     . PRO A 46  ? 0.4133 0.2905 0.3179 0.0478  -0.0371 -0.0144 31   PRO A O     
34   C  CB    . PRO A 46  ? 0.3807 0.3248 0.3614 -0.0348 0.0209  -0.0169 31   PRO A CB    
35   C  CG    . PRO A 46  ? 0.4309 0.3658 0.4034 -0.0634 0.0139  -0.0219 31   PRO A CG    
36   C  CD    . PRO A 46  ? 0.4005 0.3259 0.3797 -0.0659 0.0061  -0.0039 31   PRO A CD    
37   N  N     . THR A 47  ? 0.2929 0.2366 0.2515 0.0061  0.0202  0.0090  32   THR A N     
38   C  CA    . THR A 47  ? 0.2402 0.2485 0.2280 0.0071  0.0025  0.0203  32   THR A CA    
39   C  C     . THR A 47  ? 0.2449 0.2453 0.2312 0.0074  -0.0024 0.0093  32   THR A C     
40   O  O     . THR A 47  ? 0.2476 0.2308 0.2431 0.0212  -0.0024 0.0090  32   THR A O     
41   C  CB    . THR A 47  ? 0.2351 0.2538 0.2422 -0.0074 0.0199  -0.0321 32   THR A CB    
42   O  OG1   . THR A 47  ? 0.2484 0.2579 0.2607 0.0336  0.0476  -0.0082 32   THR A OG1   
43   C  CG2   . THR A 47  ? 0.2612 0.2345 0.2703 -0.0118 0.0095  -0.0444 32   THR A CG2   
44   N  N     . GLY A 48  ? 0.1957 0.2488 0.2401 0.0094  -0.0194 -0.0310 33   GLY A N     
45   C  CA    . GLY A 48  ? 0.2265 0.2475 0.2126 -0.0060 -0.0166 -0.0087 33   GLY A CA    
46   C  C     . GLY A 48  ? 0.2465 0.2501 0.2156 0.0209  -0.0135 -0.0107 33   GLY A C     
47   O  O     . GLY A 48  ? 0.2566 0.2782 0.2061 0.0368  -0.0053 -0.0181 33   GLY A O     
48   N  N     . GLY A 49  ? 0.2664 0.2532 0.1989 0.0510  -0.0241 -0.0157 34   GLY A N     
49   C  CA    . GLY A 49  ? 0.2875 0.2299 0.2232 0.0577  -0.0273 -0.0397 34   GLY A CA    
50   C  C     . GLY A 49  ? 0.3208 0.2745 0.2335 0.0610  -0.0415 -0.0463 34   GLY A C     
51   O  O     . GLY A 49  ? 0.3449 0.2520 0.2520 0.0308  -0.0230 -0.0330 34   GLY A O     
52   N  N     . ASP A 50  ? 0.2987 0.3344 0.2443 0.0883  -0.0313 -0.0556 35   ASP A N     
53   C  CA    . ASP A 50  ? 0.2726 0.3685 0.2387 0.0872  -0.0195 -0.0646 35   ASP A CA    
54   C  C     . ASP A 50  ? 0.3190 0.3533 0.2390 0.0772  -0.0102 -0.0470 35   ASP A C     
55   O  O     . ASP A 50  ? 0.3426 0.4048 0.2393 0.1017  0.0071  -0.0388 35   ASP A O     
56   C  CB    . ASP A 50  ? 0.3110 0.4163 0.2760 0.0836  -0.0319 -0.0743 35   ASP A CB    
57   C  CG    . ASP A 50  ? 0.2921 0.4543 0.3249 0.0770  -0.0296 -0.0680 35   ASP A CG    
58   O  OD1   . ASP A 50  ? 0.3071 0.4747 0.3237 0.0883  0.0303  -0.0438 35   ASP A OD1   
59   O  OD2   . ASP A 50  ? 0.2857 0.4630 0.3684 0.0855  -0.0545 -0.0919 35   ASP A OD2   
60   N  N     . ASP A 51  ? 0.3037 0.3315 0.2406 0.0284  -0.0266 -0.0260 36   ASP A N     
61   C  CA    . ASP A 51  ? 0.2767 0.2948 0.2678 0.0154  0.0013  -0.0289 36   ASP A CA    
62   C  C     . ASP A 51  ? 0.2983 0.3000 0.2558 0.0362  0.0220  -0.0147 36   ASP A C     
63   O  O     . ASP A 51  ? 0.2854 0.2747 0.2351 0.0200  0.0001  -0.0238 36   ASP A O     
64   C  CB    . ASP A 51  ? 0.2380 0.2909 0.2944 0.0229  -0.0129 -0.0248 36   ASP A CB    
65   C  CG    . ASP A 51  ? 0.2606 0.3108 0.3270 0.0094  0.0104  -0.0201 36   ASP A CG    
66   O  OD1   . ASP A 51  ? 0.2476 0.3206 0.3228 0.0330  0.0026  -0.0046 36   ASP A OD1   
67   O  OD2   . ASP A 51  ? 0.2749 0.3334 0.3585 0.0263  0.0510  -0.0142 36   ASP A OD2   
68   N  N     . PRO A 52  ? 0.3556 0.3249 0.2577 0.0419  0.0189  0.0080  37   PRO A N     
69   C  CA    . PRO A 52  ? 0.3606 0.3389 0.2547 0.0019  0.0564  0.0429  37   PRO A CA    
70   C  C     . PRO A 52  ? 0.3228 0.3644 0.2820 0.0003  0.0559  0.0019  37   PRO A C     
71   O  O     . PRO A 52  ? 0.3373 0.3875 0.3293 0.0044  0.0376  -0.0185 37   PRO A O     
72   C  CB    . PRO A 52  ? 0.4135 0.3633 0.2519 -0.0052 0.0576  0.0282  37   PRO A CB    
73   C  CG    . PRO A 52  ? 0.4285 0.3774 0.2558 -0.0004 0.0682  0.0353  37   PRO A CG    
74   C  CD    . PRO A 52  ? 0.3704 0.3533 0.2148 0.0528  0.0602  0.0352  37   PRO A CD    
75   N  N     . HIS A 53  ? 0.3033 0.3381 0.2579 0.0236  0.0469  0.0170  38   HIS A N     
76   C  CA    . HIS A 53  ? 0.3033 0.3245 0.2712 0.0335  0.0510  0.0097  38   HIS A CA    
77   C  C     . HIS A 53  ? 0.2641 0.2531 0.2535 0.0311  0.0471  0.0095  38   HIS A C     
78   O  O     . HIS A 53  ? 0.2837 0.2111 0.2678 0.0333  0.0506  0.0180  38   HIS A O     
79   C  CB    . HIS A 53  ? 0.3720 0.4319 0.3137 0.0378  0.0523  0.0086  38   HIS A CB    
80   C  CG    . HIS A 53  ? 0.4385 0.5403 0.3625 0.0454  0.0693  -0.0039 38   HIS A CG    
81   N  ND1   . HIS A 53  ? 0.4744 0.5834 0.3971 0.0498  0.0825  -0.0033 38   HIS A ND1   
82   C  CD2   . HIS A 53  ? 0.4674 0.5981 0.3808 0.0199  0.0876  0.0020  38   HIS A CD2   
83   C  CE1   . HIS A 53  ? 0.4874 0.6117 0.4107 0.0460  0.0854  0.0063  38   HIS A CE1   
84   N  NE2   . HIS A 53  ? 0.4862 0.6205 0.3927 0.0251  0.0868  0.0038  38   HIS A NE2   
85   N  N     . LYS A 54  ? 0.2175 0.2216 0.2202 0.0172  0.0574  -0.0173 39   LYS A N     
86   C  CA    . LYS A 54  ? 0.1963 0.2187 0.2350 -0.0192 0.0544  -0.0051 39   LYS A CA    
87   C  C     . LYS A 54  ? 0.2140 0.2361 0.2579 -0.0278 -0.0025 -0.0064 39   LYS A C     
88   O  O     . LYS A 54  ? 0.2093 0.2521 0.2712 -0.0313 -0.0047 -0.0468 39   LYS A O     
89   C  CB    . LYS A 54  ? 0.2109 0.1862 0.2412 -0.0195 0.0241  0.0295  39   LYS A CB    
90   C  CG    . LYS A 54  ? 0.2084 0.1735 0.2251 -0.0361 0.0427  0.0170  39   LYS A CG    
91   C  CD    . LYS A 54  ? 0.2393 0.1817 0.2219 -0.0439 0.0309  0.0156  39   LYS A CD    
92   C  CE    . LYS A 54  ? 0.2366 0.1544 0.2416 -0.0569 0.0078  0.0439  39   LYS A CE    
93   N  NZ    . LYS A 54  ? 0.2327 0.1634 0.2376 -0.0323 0.0028  0.0389  39   LYS A NZ    
94   N  N     . VAL A 55  ? 0.1997 0.2467 0.2466 -0.0197 -0.0050 -0.0007 40   VAL A N     
95   C  CA    . VAL A 55  ? 0.1946 0.2224 0.2675 -0.0273 0.0052  0.0041  40   VAL A CA    
96   C  C     . VAL A 55  ? 0.2301 0.2512 0.2845 -0.0216 0.0036  0.0276  40   VAL A C     
97   O  O     . VAL A 55  ? 0.2646 0.2873 0.2968 -0.0195 -0.0101 0.0469  40   VAL A O     
98   C  CB    . VAL A 55  ? 0.2147 0.2506 0.2607 -0.0424 -0.0250 0.0033  40   VAL A CB    
99   C  CG1   . VAL A 55  ? 0.2229 0.2677 0.2926 -0.0403 -0.0140 0.0254  40   VAL A CG1   
100  C  CG2   . VAL A 55  ? 0.2424 0.2427 0.2599 0.0230  -0.0169 -0.0133 40   VAL A CG2   
101  N  N     . ALA A 56  ? 0.2028 0.2409 0.2828 -0.0045 -0.0065 0.0131  41   ALA A N     
102  C  CA    . ALA A 56  ? 0.2295 0.2735 0.3095 -0.0339 0.0337  -0.0220 41   ALA A CA    
103  C  C     . ALA A 56  ? 0.2344 0.3165 0.3059 -0.0259 0.0119  -0.0133 41   ALA A C     
104  O  O     . ALA A 56  ? 0.2559 0.3765 0.3464 -0.0330 -0.0113 -0.0586 41   ALA A O     
105  C  CB    . ALA A 56  ? 0.2692 0.3163 0.3384 -0.0112 0.0501  -0.0432 41   ALA A CB    
106  N  N     A MET A 57  ? 0.2265 0.2992 0.2735 -0.0259 -0.0078 -0.0309 42   MET A N     
107  N  N     B MET A 57  ? 0.2543 0.3152 0.2943 -0.0147 -0.0088 -0.0309 42   MET A N     
108  C  CA    A MET A 57  ? 0.2298 0.3151 0.2752 -0.0029 -0.0180 -0.0201 42   MET A CA    
109  C  CA    B MET A 57  ? 0.2741 0.3407 0.3093 0.0221  -0.0156 -0.0212 42   MET A CA    
110  C  C     A MET A 57  ? 0.2377 0.2990 0.2540 0.0027  -0.0274 -0.0053 42   MET A C     
111  C  C     B MET A 57  ? 0.2472 0.3031 0.2729 0.0234  -0.0284 0.0001  42   MET A C     
112  O  O     A MET A 57  ? 0.2327 0.2923 0.2479 0.0059  -0.0043 0.0063  42   MET A O     
113  O  O     B MET A 57  ? 0.2170 0.2851 0.2684 0.0444  -0.0087 0.0222  42   MET A O     
114  C  CB    A MET A 57  ? 0.2354 0.3210 0.3014 -0.0060 -0.0079 -0.0519 42   MET A CB    
115  C  CB    B MET A 57  ? 0.3243 0.3809 0.3638 0.0487  0.0096  -0.0592 42   MET A CB    
116  C  CG    A MET A 57  ? 0.2454 0.3306 0.3172 -0.0166 0.0063  -0.0149 42   MET A CG    
117  C  CG    B MET A 57  ? 0.3711 0.4357 0.4048 0.0649  0.0163  -0.0423 42   MET A CG    
118  S  SD    A MET A 57  ? 0.2363 0.3298 0.3001 -0.0313 0.0139  0.0081  42   MET A SD    
119  S  SD    B MET A 57  ? 0.4148 0.4614 0.4235 0.0904  0.0143  -0.0178 42   MET A SD    
120  C  CE    A MET A 57  ? 0.1560 0.2523 0.2827 -0.0846 -0.0213 0.0526  42   MET A CE    
121  C  CE    B MET A 57  ? 0.3980 0.4529 0.4079 0.0883  -0.0051 -0.0116 42   MET A CE    
122  N  N     . LEU A 58  ? 0.2371 0.2999 0.2440 -0.0109 -0.0363 0.0066  43   LEU A N     
123  C  CA    . LEU A 58  ? 0.2337 0.2362 0.2784 -0.0299 -0.0289 0.0243  43   LEU A CA    
124  C  C     . LEU A 58  ? 0.2150 0.2639 0.2220 0.0106  -0.0202 0.0190  43   LEU A C     
125  O  O     . LEU A 58  ? 0.2353 0.2893 0.1974 -0.0217 -0.0128 0.0180  43   LEU A O     
126  C  CB    . LEU A 58  ? 0.2907 0.2497 0.3435 -0.0316 -0.0517 -0.0053 43   LEU A CB    
127  C  CG    . LEU A 58  ? 0.3115 0.1969 0.4087 -0.0400 0.0205  0.0015  43   LEU A CG    
128  C  CD1   . LEU A 58  ? 0.3455 0.2355 0.4401 -0.0279 0.0087  -0.0260 43   LEU A CD1   
129  C  CD2   . LEU A 58  ? 0.3368 0.2429 0.4534 0.0063  0.0500  0.0053  43   LEU A CD2   
130  N  N     . GLY A 59  ? 0.1682 0.1965 0.2218 0.0090  -0.0212 0.0137  44   GLY A N     
131  C  CA    . GLY A 59  ? 0.1664 0.2108 0.2484 -0.0209 -0.0385 -0.0153 44   GLY A CA    
132  C  C     . GLY A 59  ? 0.1989 0.1975 0.2738 -0.0122 -0.0377 -0.0273 44   GLY A C     
133  O  O     . GLY A 59  ? 0.1879 0.2265 0.2929 -0.0009 -0.0176 -0.0355 44   GLY A O     
134  N  N     . LEU A 60  ? 0.1821 0.1856 0.2524 -0.0038 -0.0303 -0.0055 45   LEU A N     
135  C  CA    . LEU A 60  ? 0.1857 0.1873 0.2550 -0.0330 -0.0063 0.0471  45   LEU A CA    
136  C  C     . LEU A 60  ? 0.1918 0.1910 0.2275 -0.0209 -0.0038 0.0370  45   LEU A C     
137  O  O     . LEU A 60  ? 0.1884 0.1907 0.2478 -0.0151 0.0257  0.0201  45   LEU A O     
138  C  CB    . LEU A 60  ? 0.2028 0.2300 0.2364 -0.0257 0.0066  0.0631  45   LEU A CB    
139  C  CG    . LEU A 60  ? 0.2080 0.2315 0.2215 -0.0274 0.0168  0.0763  45   LEU A CG    
140  C  CD1   . LEU A 60  ? 0.2176 0.2721 0.2238 -0.0320 -0.0027 0.1001  45   LEU A CD1   
141  C  CD2   . LEU A 60  ? 0.2352 0.2124 0.2496 -0.0186 -0.0071 0.0393  45   LEU A CD2   
142  N  N     . THR A 61  ? 0.1947 0.1902 0.2079 0.0158  -0.0116 0.0151  46   THR A N     
143  C  CA    . THR A 61  ? 0.2215 0.2252 0.2189 -0.0170 -0.0350 0.0211  46   THR A CA    
144  C  C     . THR A 61  ? 0.2112 0.2324 0.2292 -0.0209 -0.0202 0.0111  46   THR A C     
145  O  O     . THR A 61  ? 0.1857 0.2321 0.2318 -0.0031 0.0298  0.0166  46   THR A O     
146  C  CB    . THR A 61  ? 0.2808 0.2618 0.2443 -0.0250 -0.0527 0.0517  46   THR A CB    
147  O  OG1   . THR A 61  ? 0.3433 0.3017 0.3040 -0.0806 -0.0446 0.0675  46   THR A OG1   
148  C  CG2   . THR A 61  ? 0.2819 0.3247 0.2551 -0.0023 -0.0240 0.0309  46   THR A CG2   
149  N  N     . PHE A 62  ? 0.1797 0.2275 0.2289 -0.0229 -0.0011 -0.0150 47   PHE A N     
150  C  CA    . PHE A 62  ? 0.1905 0.2090 0.2293 0.0358  -0.0089 0.0180  47   PHE A CA    
151  C  C     . PHE A 62  ? 0.1870 0.1889 0.2453 0.0093  0.0065  0.0164  47   PHE A C     
152  O  O     . PHE A 62  ? 0.1666 0.1728 0.2431 0.0083  0.0037  0.0135  47   PHE A O     
153  C  CB    . PHE A 62  ? 0.2203 0.1915 0.2188 0.0322  0.0047  0.0302  47   PHE A CB    
154  C  CG    . PHE A 62  ? 0.2205 0.1991 0.2318 0.0281  0.0195  0.0082  47   PHE A CG    
155  C  CD1   . PHE A 62  ? 0.2068 0.1817 0.2552 0.0395  0.0052  -0.0096 47   PHE A CD1   
156  C  CD2   . PHE A 62  ? 0.2463 0.1850 0.2181 0.0242  0.0071  0.0266  47   PHE A CD2   
157  C  CE1   . PHE A 62  ? 0.2281 0.2107 0.2656 0.0116  0.0274  0.0069  47   PHE A CE1   
158  C  CE2   . PHE A 62  ? 0.2289 0.1975 0.2430 -0.0004 0.0210  -0.0106 47   PHE A CE2   
159  C  CZ    . PHE A 62  ? 0.2303 0.2040 0.2620 -0.0085 0.0057  -0.0161 47   PHE A CZ    
160  N  N     . ASP A 63  ? 0.2121 0.2082 0.2438 0.0111  -0.0060 -0.0151 48   ASP A N     
161  C  CA    . ASP A 63  ? 0.2117 0.1865 0.2277 0.0308  0.0354  -0.0099 48   ASP A CA    
162  C  C     . ASP A 63  ? 0.2402 0.1885 0.2259 0.0148  0.0027  -0.0214 48   ASP A C     
163  O  O     . ASP A 63  ? 0.2958 0.1968 0.2380 -0.0176 -0.0013 -0.0122 48   ASP A O     
164  C  CB    . ASP A 63  ? 0.2513 0.2846 0.2216 0.0121  0.0586  -0.0016 48   ASP A CB    
165  C  CG    . ASP A 63  ? 0.2792 0.3838 0.2302 0.0207  0.0792  -0.0159 48   ASP A CG    
166  O  OD1   . ASP A 63  ? 0.3039 0.4038 0.2362 0.0649  0.0275  -0.0228 48   ASP A OD1   
167  O  OD2   . ASP A 63  ? 0.3530 0.4288 0.2370 0.0307  0.0846  0.0417  48   ASP A OD2   
168  N  N     . ASP A 64  ? 0.1677 0.2112 0.2198 0.0116  -0.0073 -0.0026 49   ASP A N     
169  C  CA    . ASP A 64  ? 0.1642 0.1888 0.2607 -0.0272 -0.0026 -0.0415 49   ASP A CA    
170  C  C     . ASP A 64  ? 0.1665 0.1905 0.2519 0.0150  0.0255  -0.0095 49   ASP A C     
171  O  O     . ASP A 64  ? 0.1882 0.2142 0.2541 0.0085  0.0179  -0.0030 49   ASP A O     
172  C  CB    . ASP A 64  ? 0.1746 0.2100 0.3081 -0.0312 -0.0181 -0.0472 49   ASP A CB    
173  C  CG    . ASP A 64  ? 0.1931 0.1956 0.3235 0.0100  -0.0059 -0.0633 49   ASP A CG    
174  O  OD1   . ASP A 64  ? 0.2038 0.2384 0.4146 0.0177  0.0321  -0.0322 49   ASP A OD1   
175  O  OD2   . ASP A 64  ? 0.1937 0.2059 0.2916 0.0023  -0.0193 -0.0102 49   ASP A OD2   
176  N  N     . VAL A 65  ? 0.1526 0.1893 0.2313 0.0093  0.0104  -0.0229 50   VAL A N     
177  C  CA    . VAL A 65  ? 0.1874 0.2211 0.2404 -0.0089 0.0058  -0.0191 50   VAL A CA    
178  C  C     . VAL A 65  ? 0.1608 0.1931 0.2518 -0.0289 0.0208  -0.0292 50   VAL A C     
179  O  O     . VAL A 65  ? 0.1989 0.2218 0.2751 -0.0365 -0.0205 -0.0145 50   VAL A O     
180  C  CB    . VAL A 65  ? 0.2094 0.2009 0.1936 0.0082  -0.0131 -0.0012 50   VAL A CB    
181  C  CG1   . VAL A 65  ? 0.2222 0.2387 0.1959 0.0171  -0.0209 -0.0109 50   VAL A CG1   
182  C  CG2   . VAL A 65  ? 0.2087 0.2113 0.2071 0.0168  0.0092  -0.0040 50   VAL A CG2   
183  N  N     . LEU A 66  ? 0.1164 0.1951 0.2497 -0.0311 0.0371  -0.0162 51   LEU A N     
184  C  CA    . LEU A 66  ? 0.1351 0.1785 0.2303 -0.0080 0.0177  -0.0299 51   LEU A CA    
185  C  C     . LEU A 66  ? 0.1455 0.1882 0.2274 -0.0116 0.0193  -0.0203 51   LEU A C     
186  O  O     . LEU A 66  ? 0.1878 0.2051 0.2256 0.0072  0.0053  -0.0147 51   LEU A O     
187  C  CB    . LEU A 66  ? 0.2028 0.1969 0.2138 0.0364  0.0085  -0.0380 51   LEU A CB    
188  C  CG    . LEU A 66  ? 0.2418 0.1909 0.2283 0.0393  -0.0035 -0.0434 51   LEU A CG    
189  C  CD1   . LEU A 66  ? 0.2457 0.1810 0.2234 0.0277  -0.0210 -0.0657 51   LEU A CD1   
190  C  CD2   . LEU A 66  ? 0.2553 0.2422 0.2454 0.0334  0.0096  -0.0251 51   LEU A CD2   
191  N  N     . LEU A 67  ? 0.1545 0.1829 0.2090 0.0130  0.0161  0.0119  52   LEU A N     
192  C  CA    . LEU A 67  ? 0.1654 0.1550 0.2137 0.0296  0.0267  0.0367  52   LEU A CA    
193  C  C     . LEU A 67  ? 0.1893 0.1832 0.2291 0.0074  0.0260  0.0182  52   LEU A C     
194  O  O     . LEU A 67  ? 0.1899 0.2142 0.2604 0.0202  0.0030  0.0249  52   LEU A O     
195  C  CB    . LEU A 67  ? 0.1988 0.1453 0.2336 -0.0078 0.0139  0.0106  52   LEU A CB    
196  C  CG    . LEU A 67  ? 0.2384 0.1607 0.2649 0.0168  -0.0243 -0.0056 52   LEU A CG    
197  C  CD1   . LEU A 67  ? 0.2209 0.1700 0.2783 0.0310  -0.0712 -0.0031 52   LEU A CD1   
198  C  CD2   . LEU A 67  ? 0.2412 0.2035 0.2857 0.0167  -0.0155 -0.0215 52   LEU A CD2   
199  N  N     . LEU A 68  ? 0.2033 0.1835 0.2075 -0.0087 0.0330  0.0562  53   LEU A N     
200  C  CA    . LEU A 68  ? 0.2086 0.1865 0.2052 0.0051  -0.0029 0.0732  53   LEU A CA    
201  C  C     . LEU A 68  ? 0.2086 0.1864 0.2287 0.0260  -0.0081 0.0557  53   LEU A C     
202  O  O     . LEU A 68  ? 0.2155 0.2172 0.2456 -0.0093 -0.0101 0.0624  53   LEU A O     
203  C  CB    . LEU A 68  ? 0.2120 0.1985 0.2217 0.0330  -0.0376 0.0300  53   LEU A CB    
204  C  CG    . LEU A 68  ? 0.2105 0.2096 0.2318 0.0113  -0.0243 0.0133  53   LEU A CG    
205  C  CD1   . LEU A 68  ? 0.2542 0.2429 0.2315 0.0179  -0.0446 0.0361  53   LEU A CD1   
206  C  CD2   . LEU A 68  ? 0.2403 0.2151 0.2661 0.0154  -0.0034 -0.0026 53   LEU A CD2   
207  N  N     . PRO A 69  ? 0.1960 0.1756 0.2595 0.0052  0.0131  0.0272  54   PRO A N     
208  C  CA    . PRO A 69  ? 0.1987 0.2140 0.2644 -0.0486 0.0127  0.0010  54   PRO A CA    
209  C  C     . PRO A 69  ? 0.1970 0.2369 0.2584 -0.0324 0.0356  -0.0051 54   PRO A C     
210  O  O     . PRO A 69  ? 0.1901 0.2656 0.2660 -0.0367 0.0432  -0.0089 54   PRO A O     
211  C  CB    . PRO A 69  ? 0.2200 0.2136 0.2859 -0.0386 0.0293  -0.0367 54   PRO A CB    
212  C  CG    . PRO A 69  ? 0.2206 0.2368 0.2928 -0.0465 0.0163  -0.0422 54   PRO A CG    
213  C  CD    . PRO A 69  ? 0.2003 0.2005 0.2654 -0.0404 -0.0211 0.0064  54   PRO A CD    
214  N  N     . ALA A 70  ? 0.1796 0.1999 0.2363 -0.0123 0.0244  0.0085  55   ALA A N     
215  C  CA    . ALA A 70  ? 0.2120 0.2052 0.2379 -0.0110 0.0256  0.0114  55   ALA A CA    
216  C  C     . ALA A 70  ? 0.2306 0.2053 0.2402 -0.0012 0.0446  0.0333  55   ALA A C     
217  O  O     . ALA A 70  ? 0.2238 0.2257 0.2341 0.0065  0.0246  0.0197  55   ALA A O     
218  C  CB    . ALA A 70  ? 0.2326 0.2140 0.2451 0.0039  0.0167  0.0021  55   ALA A CB    
219  N  N     . ALA A 71  ? 0.1942 0.2182 0.1944 -0.0042 0.0517  0.0330  56   ALA A N     
220  C  CA    . ALA A 71  ? 0.1970 0.2411 0.1898 0.0023  0.0682  0.0338  56   ALA A CA    
221  C  C     . ALA A 71  ? 0.2050 0.2422 0.2484 -0.0025 0.0341  0.0415  56   ALA A C     
222  O  O     . ALA A 71  ? 0.2130 0.2216 0.2629 -0.0226 0.0211  0.0206  56   ALA A O     
223  C  CB    . ALA A 71  ? 0.1831 0.2395 0.2370 0.0103  0.0857  0.0214  56   ALA A CB    
224  N  N     . SER A 72  ? 0.1906 0.2563 0.2228 0.0153  0.0233  0.0481  57   SER A N     
225  C  CA    . SER A 72  ? 0.1943 0.2778 0.2479 0.0012  0.0229  0.0577  57   SER A CA    
226  C  C     . SER A 72  ? 0.2292 0.2686 0.2983 0.0086  0.0334  0.0631  57   SER A C     
227  O  O     . SER A 72  ? 0.2353 0.2651 0.3390 0.0170  0.0184  0.0485  57   SER A O     
228  C  CB    . SER A 72  ? 0.1889 0.2797 0.2111 -0.0087 0.0232  0.0585  57   SER A CB    
229  O  OG    . SER A 72  ? 0.1897 0.2631 0.2337 0.0202  0.0124  0.0565  57   SER A OG    
230  N  N     . ASP A 73  ? 0.1897 0.2637 0.2852 0.0281  0.0344  0.0649  58   ASP A N     
231  C  CA    . ASP A 73  ? 0.2436 0.3027 0.3342 0.0353  0.0363  0.0275  58   ASP A CA    
232  C  C     . ASP A 73  ? 0.2329 0.3200 0.3338 0.0358  0.0139  0.0436  58   ASP A C     
233  O  O     . ASP A 73  ? 0.2366 0.3457 0.4021 0.0227  0.0409  0.0917  58   ASP A O     
234  C  CB    . ASP A 73  ? 0.3160 0.3984 0.3843 -0.0011 0.0506  0.0248  58   ASP A CB    
235  C  CG    . ASP A 73  ? 0.4912 0.5309 0.4543 -0.0229 0.0332  -0.0174 58   ASP A CG    
236  O  OD1   . ASP A 73  ? 0.5624 0.6010 0.4797 -0.0907 0.0369  0.0136  58   ASP A OD1   
237  O  OD2   . ASP A 73  ? 0.5516 0.5809 0.4987 -0.0045 0.0172  -0.0334 58   ASP A OD2   
238  N  N     . VAL A 74  ? 0.2100 0.2605 0.3154 0.0012  0.0299  0.0088  59   VAL A N     
239  C  CA    . VAL A 74  ? 0.2052 0.2304 0.3184 0.0054  0.0333  0.0059  59   VAL A CA    
240  C  C     . VAL A 74  ? 0.2330 0.2570 0.3274 -0.0045 0.0203  0.0113  59   VAL A C     
241  O  O     . VAL A 74  ? 0.2224 0.2497 0.3041 0.0083  0.0353  0.0146  59   VAL A O     
242  C  CB    . VAL A 74  ? 0.2023 0.2237 0.3334 -0.0104 0.0392  0.0472  59   VAL A CB    
243  C  CG1   . VAL A 74  ? 0.2234 0.2165 0.3675 0.0006  0.0320  0.0427  59   VAL A CG1   
244  C  CG2   . VAL A 74  ? 0.2096 0.2419 0.3224 0.0017  0.0315  0.0063  59   VAL A CG2   
245  N  N     . VAL A 75  ? 0.2646 0.2717 0.3420 -0.0345 -0.0013 0.0041  60   VAL A N     
246  C  CA    . VAL A 75  ? 0.2694 0.2613 0.3740 -0.0305 -0.0339 0.0269  60   VAL A CA    
247  C  C     . VAL A 75  ? 0.2374 0.2414 0.3613 -0.0195 -0.0181 0.0277  60   VAL A C     
248  O  O     . VAL A 75  ? 0.2390 0.2279 0.3708 -0.0194 -0.0066 0.0296  60   VAL A O     
249  C  CB    . VAL A 75  ? 0.2774 0.2258 0.3818 -0.0599 -0.0684 0.0708  60   VAL A CB    
250  C  CG1   . VAL A 75  ? 0.3321 0.2751 0.3875 -0.0760 -0.0964 0.0757  60   VAL A CG1   
251  C  CG2   . VAL A 75  ? 0.2224 0.2923 0.3910 -0.0441 -0.0576 0.0675  60   VAL A CG2   
252  N  N     . PRO A 76  ? 0.2268 0.2225 0.3543 0.0167  -0.0215 -0.0063 61   PRO A N     
253  C  CA    . PRO A 76  ? 0.2395 0.2232 0.3509 0.0025  0.0150  0.0157  61   PRO A CA    
254  C  C     . PRO A 76  ? 0.2451 0.1864 0.3421 -0.0143 0.0110  0.0357  61   PRO A C     
255  O  O     . PRO A 76  ? 0.2632 0.1798 0.3529 -0.0227 -0.0055 0.0242  61   PRO A O     
256  C  CB    . PRO A 76  ? 0.2693 0.2241 0.3729 0.0292  0.0332  0.0267  61   PRO A CB    
257  C  CG    . PRO A 76  ? 0.2520 0.2425 0.3748 0.0178  0.0158  0.0148  61   PRO A CG    
258  C  CD    . PRO A 76  ? 0.2258 0.2296 0.3453 0.0029  0.0201  -0.0141 61   PRO A CD    
259  N  N     . ALA A 77  ? 0.2318 0.2255 0.3487 0.0246  -0.0207 0.0440  62   ALA A N     
260  C  CA    . ALA A 77  ? 0.2301 0.2688 0.3750 0.0230  -0.0719 0.0317  62   ALA A CA    
261  C  C     . ALA A 77  ? 0.2348 0.2682 0.3795 0.0138  -0.0465 0.0348  62   ALA A C     
262  O  O     . ALA A 77  ? 0.2321 0.2686 0.4157 0.0160  -0.0134 0.0279  62   ALA A O     
263  C  CB    . ALA A 77  ? 0.2725 0.2970 0.3896 0.0114  -0.1073 0.0380  62   ALA A CB    
264  N  N     . THR A 78  ? 0.2586 0.2555 0.3693 -0.0429 -0.0285 0.0228  63   THR A N     
265  C  CA    . THR A 78  ? 0.2621 0.2524 0.3741 -0.0088 -0.0190 0.0165  63   THR A CA    
266  C  C     . THR A 78  ? 0.2312 0.2881 0.3682 -0.0198 -0.0186 -0.0122 63   THR A C     
267  O  O     . THR A 78  ? 0.2615 0.3322 0.3949 -0.0014 -0.0008 -0.0461 63   THR A O     
268  C  CB    . THR A 78  ? 0.2059 0.2466 0.3911 -0.0091 -0.0111 0.0300  63   THR A CB    
269  O  OG1   . THR A 78  ? 0.2248 0.2808 0.3932 0.0217  0.0067  0.0399  63   THR A OG1   
270  C  CG2   . THR A 78  ? 0.2300 0.2389 0.3986 -0.0264 -0.0237 0.0465  63   THR A CG2   
271  N  N     . ALA A 79  ? 0.1892 0.2602 0.3466 -0.0450 -0.0080 0.0427  64   ALA A N     
272  C  CA    . ALA A 79  ? 0.1792 0.2332 0.3354 -0.0115 -0.0075 0.0540  64   ALA A CA    
273  C  C     . ALA A 79  ? 0.2146 0.2154 0.3407 -0.0374 -0.0222 0.0391  64   ALA A C     
274  O  O     . ALA A 79  ? 0.2584 0.2497 0.3821 -0.0279 -0.0475 -0.0076 64   ALA A O     
275  C  CB    . ALA A 79  ? 0.1863 0.2883 0.3453 -0.0149 0.0038  0.0698  64   ALA A CB    
276  N  N     . ASP A 80  ? 0.1949 0.2121 0.3409 -0.0594 -0.0027 0.0219  65   ASP A N     
277  C  CA    . ASP A 80  ? 0.1748 0.2118 0.3663 -0.0119 0.0435  0.0113  65   ASP A CA    
278  C  C     . ASP A 80  ? 0.2072 0.2124 0.3578 -0.0178 0.0409  0.0158  65   ASP A C     
279  O  O     . ASP A 80  ? 0.2220 0.2008 0.3566 0.0259  0.0452  0.0353  65   ASP A O     
280  C  CB    . ASP A 80  ? 0.1848 0.2056 0.4408 0.0123  0.0620  -0.0345 65   ASP A CB    
281  C  CG    . ASP A 80  ? 0.1855 0.2816 0.5410 0.0372  0.0762  -0.0274 65   ASP A CG    
282  O  OD1   . ASP A 80  ? 0.2057 0.2621 0.5706 0.0309  0.0831  -0.0069 65   ASP A OD1   
283  O  OD2   . ASP A 80  ? 0.2357 0.3086 0.5943 0.0055  0.0512  -0.0386 65   ASP A OD2   
284  N  N     . THR A 81  ? 0.1998 0.1941 0.3267 -0.0398 0.0203  0.0302  66   THR A N     
285  C  CA    . THR A 81  ? 0.2318 0.1983 0.2925 -0.0208 0.0211  0.0420  66   THR A CA    
286  C  C     . THR A 81  ? 0.2136 0.1934 0.2838 -0.0103 0.0207  0.0325  66   THR A C     
287  O  O     . THR A 81  ? 0.2167 0.2197 0.2756 -0.0081 0.0021  0.0187  66   THR A O     
288  C  CB    . THR A 81  ? 0.2689 0.1926 0.2864 -0.0023 -0.0029 0.0560  66   THR A CB    
289  O  OG1   . THR A 81  ? 0.2855 0.2323 0.2994 -0.0071 -0.0059 0.0605  66   THR A OG1   
290  C  CG2   . THR A 81  ? 0.2969 0.1990 0.2780 -0.0137 -0.0069 0.0652  66   THR A CG2   
291  N  N     . SER A 82  ? 0.2029 0.1751 0.2797 0.0151  0.0122  0.0182  67   SER A N     
292  C  CA    . SER A 82  ? 0.2201 0.1477 0.2922 0.0315  0.0186  0.0301  67   SER A CA    
293  C  C     . SER A 82  ? 0.2153 0.1670 0.2909 -0.0117 0.0184  0.0270  67   SER A C     
294  O  O     . SER A 82  ? 0.1979 0.2109 0.2791 0.0171  0.0166  0.0117  67   SER A O     
295  C  CB    . SER A 82  ? 0.2430 0.1919 0.2848 0.0120  0.0335  0.0449  67   SER A CB    
296  O  OG    . SER A 82  ? 0.2763 0.2238 0.3166 0.0196  0.0418  0.0347  67   SER A OG    
297  N  N     . SER A 83  ? 0.1883 0.2057 0.2928 -0.0168 0.0203  -0.0168 68   SER A N     
298  C  CA    . SER A 83  ? 0.1963 0.2179 0.2873 -0.0266 0.0098  -0.0196 68   SER A CA    
299  C  C     . SER A 83  ? 0.2105 0.2287 0.2846 -0.0169 0.0271  -0.0119 68   SER A C     
300  O  O     . SER A 83  ? 0.2384 0.2181 0.2870 0.0007  0.0414  -0.0010 68   SER A O     
301  C  CB    . SER A 83  ? 0.1853 0.2464 0.3042 -0.0186 0.0033  -0.0107 68   SER A CB    
302  O  OG    . SER A 83  ? 0.1994 0.2257 0.3095 -0.0311 0.0216  -0.0069 68   SER A OG    
303  N  N     . GLN A 84  ? 0.2224 0.2338 0.2348 -0.0286 0.0327  -0.0191 69   GLN A N     
304  C  CA    . GLN A 84  ? 0.2397 0.2471 0.2242 -0.0475 0.0479  -0.0155 69   GLN A CA    
305  C  C     . GLN A 84  ? 0.2024 0.2479 0.2649 -0.0263 0.0121  -0.0071 69   GLN A C     
306  O  O     . GLN A 84  ? 0.2208 0.2437 0.2475 -0.0055 0.0202  0.0000  69   GLN A O     
307  C  CB    . GLN A 84  ? 0.2816 0.2661 0.2340 -0.0576 0.0531  -0.0013 69   GLN A CB    
308  C  CG    . GLN A 84  ? 0.2932 0.3073 0.2892 -0.0454 0.0829  -0.0084 69   GLN A CG    
309  C  CD    . GLN A 84  ? 0.3065 0.2925 0.3302 -0.0610 0.0920  -0.0188 69   GLN A CD    
310  O  OE1   . GLN A 84  ? 0.3554 0.2982 0.3905 -0.0653 0.0803  -0.0550 69   GLN A OE1   
311  N  NE2   . GLN A 84  ? 0.3160 0.3180 0.3250 -0.0302 0.0974  0.0094  69   GLN A NE2   
312  N  N     . LEU A 85  ? 0.1761 0.1935 0.2762 -0.0438 0.0089  0.0109  70   LEU A N     
313  C  CA    . LEU A 85  ? 0.1848 0.1827 0.2756 -0.0278 -0.0057 0.0174  70   LEU A CA    
314  C  C     . LEU A 85  ? 0.2408 0.1839 0.2866 -0.0027 -0.0157 0.0072  70   LEU A C     
315  O  O     . LEU A 85  ? 0.2700 0.1910 0.2727 0.0199  -0.0123 -0.0294 70   LEU A O     
316  C  CB    . LEU A 85  ? 0.1750 0.1949 0.2861 -0.0159 0.0257  0.0326  70   LEU A CB    
317  C  CG    . LEU A 85  ? 0.1880 0.1916 0.2934 0.0306  0.0236  0.0378  70   LEU A CG    
318  C  CD1   . LEU A 85  ? 0.2350 0.2101 0.2970 0.0234  0.0521  0.0010  70   LEU A CD1   
319  C  CD2   . LEU A 85  ? 0.2101 0.2348 0.3085 0.0171  0.0216  0.0497  70   LEU A CD2   
320  N  N     . THR A 86  ? 0.2774 0.1807 0.2842 -0.0082 0.0179  -0.0263 71   THR A N     
321  C  CA    . THR A 86  ? 0.2846 0.1630 0.2960 -0.0119 0.0206  -0.0338 71   THR A CA    
322  C  C     . THR A 86  ? 0.2991 0.1943 0.3116 -0.0035 0.0260  -0.0377 71   THR A C     
323  O  O     . THR A 86  ? 0.2994 0.2006 0.3144 -0.0193 0.0437  -0.0051 71   THR A O     
324  C  CB    . THR A 86  ? 0.2926 0.1883 0.3204 0.0421  0.0306  0.0164  71   THR A CB    
325  O  OG1   . THR A 86  ? 0.2836 0.2094 0.3527 0.0208  0.0048  0.0192  71   THR A OG1   
326  C  CG2   . THR A 86  ? 0.2919 0.2013 0.2909 0.0062  0.0153  0.0383  71   THR A CG2   
327  N  N     . LYS A 87  ? 0.2903 0.2414 0.3113 -0.0033 0.0221  -0.0562 72   LYS A N     
328  C  CA    . LYS A 87  ? 0.3089 0.2920 0.3242 -0.0219 0.0492  -0.0747 72   LYS A CA    
329  C  C     . LYS A 87  ? 0.3063 0.3295 0.3708 -0.0290 0.0652  -0.0555 72   LYS A C     
330  O  O     . LYS A 87  ? 0.3017 0.3419 0.4038 -0.0646 0.0842  -0.0488 72   LYS A O     
331  C  CB    . LYS A 87  ? 0.3346 0.3467 0.3143 -0.0377 0.0286  -0.1055 72   LYS A CB    
332  C  CG    . LYS A 87  ? 0.3703 0.3810 0.3199 -0.0545 -0.0228 -0.1189 72   LYS A CG    
333  C  CD    . LYS A 87  ? 0.4029 0.4284 0.3542 -0.0311 -0.0841 -0.1326 72   LYS A CD    
334  C  CE    . LYS A 87  ? 0.4497 0.4554 0.3798 -0.0268 -0.1294 -0.1571 72   LYS A CE    
335  N  NZ    . LYS A 87  ? 0.4984 0.4964 0.4065 0.0101  -0.1343 -0.1692 72   LYS A NZ    
336  N  N     . LYS A 88  ? 0.2870 0.3042 0.3872 0.0027  0.0692  -0.0530 73   LYS A N     
337  C  CA    . LYS A 88  ? 0.2863 0.3032 0.4261 -0.0097 0.0718  -0.0597 73   LYS A CA    
338  C  C     . LYS A 88  ? 0.2782 0.3175 0.4269 0.0005  0.0571  -0.0493 73   LYS A C     
339  O  O     . LYS A 88  ? 0.3049 0.4009 0.4581 -0.0384 0.0581  -0.0506 73   LYS A O     
340  C  CB    . LYS A 88  ? 0.3296 0.3259 0.4699 -0.0086 0.0524  -0.0684 73   LYS A CB    
341  C  CG    . LYS A 88  ? 0.3748 0.3575 0.5060 -0.0496 0.0300  -0.0649 73   LYS A CG    
342  C  CD    . LYS A 88  ? 0.4362 0.4427 0.5622 -0.0482 0.0247  -0.0296 73   LYS A CD    
343  C  CE    . LYS A 88  ? 0.4520 0.4717 0.6002 -0.0277 0.0240  -0.0247 73   LYS A CE    
344  N  NZ    . LYS A 88  ? 0.4650 0.5152 0.6282 -0.0070 0.0343  -0.0239 73   LYS A NZ    
345  N  N     . ILE A 89  ? 0.2666 0.2590 0.3843 0.0226  0.0400  -0.0327 74   ILE A N     
346  C  CA    . ILE A 89  ? 0.2796 0.2303 0.3779 0.0137  0.0186  -0.0069 74   ILE A CA    
347  C  C     . ILE A 89  ? 0.2484 0.2252 0.3506 0.0045  0.0004  0.0045  74   ILE A C     
348  O  O     . ILE A 89  ? 0.2281 0.2514 0.3309 0.0306  -0.0065 -0.0062 74   ILE A O     
349  C  CB    . ILE A 89  ? 0.2752 0.1930 0.3966 -0.0178 0.0056  0.0109  74   ILE A CB    
350  C  CG1   . ILE A 89  ? 0.2858 0.2073 0.4061 -0.0266 0.0080  0.0376  74   ILE A CG1   
351  C  CG2   . ILE A 89  ? 0.2644 0.2194 0.3841 -0.0130 -0.0093 0.0079  74   ILE A CG2   
352  C  CD1   . ILE A 89  ? 0.2845 0.2506 0.4052 -0.0306 -0.0207 0.0486  74   ILE A CD1   
353  N  N     . ARG A 90  ? 0.2499 0.2078 0.3739 -0.0126 0.0048  -0.0114 75   ARG A N     
354  C  CA    . ARG A 90  ? 0.2365 0.2382 0.3761 -0.0200 0.0226  -0.0077 75   ARG A CA    
355  C  C     . ARG A 90  ? 0.2602 0.2460 0.3955 0.0373  -0.0044 -0.0291 75   ARG A C     
356  O  O     . ARG A 90  ? 0.3240 0.3143 0.4197 0.0749  -0.0274 -0.0384 75   ARG A O     
357  C  CB    . ARG A 90  ? 0.2726 0.2601 0.3691 -0.0277 0.0398  -0.0143 75   ARG A CB    
358  C  CG    . ARG A 90  ? 0.2779 0.2806 0.3331 -0.0420 0.0711  -0.0018 75   ARG A CG    
359  C  CD    . ARG A 90  ? 0.3161 0.2915 0.3331 -0.0444 0.0623  -0.0214 75   ARG A CD    
360  N  NE    . ARG A 90  ? 0.3293 0.3392 0.3431 -0.0478 0.0808  -0.0277 75   ARG A NE    
361  C  CZ    . ARG A 90  ? 0.3162 0.3154 0.3584 -0.0634 0.0576  -0.0231 75   ARG A CZ    
362  N  NH1   . ARG A 90  ? 0.3085 0.3310 0.3494 -0.0628 0.0619  -0.0374 75   ARG A NH1   
363  N  NH2   . ARG A 90  ? 0.3056 0.3180 0.3604 -0.0421 0.0382  -0.0292 75   ARG A NH2   
364  N  N     . LEU A 91  ? 0.2220 0.2082 0.3848 -0.0100 0.0221  -0.0091 76   LEU A N     
365  C  CA    . LEU A 91  ? 0.1857 0.2033 0.3548 0.0003  0.0229  -0.0044 76   LEU A CA    
366  C  C     . LEU A 91  ? 0.2117 0.2038 0.3350 -0.0222 -0.0137 0.0320  76   LEU A C     
367  O  O     . LEU A 91  ? 0.2264 0.2397 0.3248 0.0018  -0.0190 0.0566  76   LEU A O     
368  C  CB    . LEU A 91  ? 0.1664 0.1929 0.3466 0.0285  0.0273  -0.0138 76   LEU A CB    
369  C  CG    . LEU A 91  ? 0.1841 0.1854 0.3406 0.0206  0.0114  -0.0017 76   LEU A CG    
370  C  CD1   . LEU A 91  ? 0.1902 0.1845 0.3250 -0.0002 -0.0258 -0.0015 76   LEU A CD1   
371  C  CD2   . LEU A 91  ? 0.2506 0.1693 0.3519 0.0302  0.0086  0.0116  76   LEU A CD2   
372  N  N     . LYS A 92  ? 0.1966 0.1952 0.3496 -0.0289 0.0056  0.0229  77   LYS A N     
373  C  CA    . LYS A 92  ? 0.1778 0.2279 0.3471 -0.0162 -0.0059 0.0083  77   LYS A CA    
374  C  C     . LYS A 92  ? 0.1870 0.2342 0.3330 -0.0066 0.0030  -0.0115 77   LYS A C     
375  O  O     . LYS A 92  ? 0.2009 0.2181 0.2997 -0.0121 -0.0196 -0.0140 77   LYS A O     
376  C  CB    . LYS A 92  ? 0.2037 0.2695 0.3825 -0.0243 -0.0243 0.0063  77   LYS A CB    
377  C  CG    . LYS A 92  ? 0.2489 0.3177 0.4358 -0.0054 -0.0415 0.0233  77   LYS A CG    
378  C  CD    . LYS A 92  ? 0.3172 0.4040 0.5137 -0.0189 -0.0114 0.0360  77   LYS A CD    
379  C  CE    . LYS A 92  ? 0.4070 0.4844 0.5601 0.0144  0.0296  0.0311  77   LYS A CE    
380  N  NZ    . LYS A 92  ? 0.4402 0.5218 0.5807 0.0465  0.0586  0.0177  77   LYS A NZ    
381  N  N     . VAL A 93  ? 0.1547 0.2547 0.3335 0.0115  0.0131  -0.0330 78   VAL A N     
382  C  CA    . VAL A 93  ? 0.1716 0.2464 0.3265 -0.0200 -0.0087 -0.0326 78   VAL A CA    
383  C  C     . VAL A 93  ? 0.1663 0.2189 0.3216 -0.0225 -0.0003 -0.0092 78   VAL A C     
384  O  O     . VAL A 93  ? 0.1792 0.2083 0.3654 -0.0130 -0.0037 0.0158  78   VAL A O     
385  C  CB    . VAL A 93  ? 0.1859 0.2783 0.3713 -0.0111 -0.0212 -0.0752 78   VAL A CB    
386  C  CG1   . VAL A 93  ? 0.2117 0.3120 0.3711 -0.0073 0.0121  -0.0867 78   VAL A CG1   
387  C  CG2   . VAL A 93  ? 0.2018 0.3005 0.3772 -0.0170 -0.0232 -0.0597 78   VAL A CG2   
388  N  N     . PRO A 94  ? 0.1866 0.1851 0.2799 -0.0239 0.0014  -0.0270 79   PRO A N     
389  C  CA    . PRO A 94  ? 0.2002 0.2167 0.2750 -0.0045 -0.0312 0.0064  79   PRO A CA    
390  C  C     . PRO A 94  ? 0.1805 0.2173 0.2573 0.0074  -0.0129 0.0081  79   PRO A C     
391  O  O     . PRO A 94  ? 0.1970 0.2029 0.2564 -0.0075 -0.0035 0.0336  79   PRO A O     
392  C  CB    . PRO A 94  ? 0.2178 0.1992 0.2513 -0.0152 -0.0514 -0.0095 79   PRO A CB    
393  C  CG    . PRO A 94  ? 0.2190 0.1816 0.2694 -0.0028 -0.0566 -0.0134 79   PRO A CG    
394  C  CD    . PRO A 94  ? 0.1846 0.1860 0.2710 0.0127  -0.0158 -0.0153 79   PRO A CD    
395  N  N     . LEU A 95  ? 0.1878 0.2001 0.2340 -0.0351 -0.0116 0.0207  80   LEU A N     
396  C  CA    . LEU A 95  ? 0.2164 0.2028 0.2346 -0.0386 0.0004  0.0102  80   LEU A CA    
397  C  C     . LEU A 95  ? 0.2031 0.2166 0.2501 -0.0147 -0.0072 0.0177  80   LEU A C     
398  O  O     . LEU A 95  ? 0.1911 0.2012 0.2836 0.0090  -0.0119 0.0090  80   LEU A O     
399  C  CB    . LEU A 95  ? 0.2450 0.1910 0.2114 -0.0155 -0.0332 0.0182  80   LEU A CB    
400  C  CG    . LEU A 95  ? 0.2915 0.1864 0.2404 -0.0294 -0.0379 0.0133  80   LEU A CG    
401  C  CD1   . LEU A 95  ? 0.3287 0.1840 0.2510 -0.0203 -0.0279 -0.0060 80   LEU A CD1   
402  C  CD2   . LEU A 95  ? 0.3223 0.1838 0.2676 0.0097  -0.0100 0.0549  80   LEU A CD2   
403  N  N     A VAL A 96  ? 0.2064 0.2170 0.2466 -0.0232 -0.0083 0.0417  81   VAL A N     
404  N  N     B VAL A 96  ? 0.2087 0.2093 0.2496 -0.0046 -0.0023 0.0334  81   VAL A N     
405  C  CA    A VAL A 96  ? 0.2228 0.2122 0.2503 -0.0412 0.0101  0.0084  81   VAL A CA    
406  C  CA    B VAL A 96  ? 0.2229 0.1933 0.2408 -0.0043 0.0022  0.0298  81   VAL A CA    
407  C  C     A VAL A 96  ? 0.1974 0.2121 0.2433 -0.0255 0.0036  0.0221  81   VAL A C     
408  C  C     B VAL A 96  ? 0.2017 0.2123 0.2403 0.0014  -0.0018 0.0298  81   VAL A C     
409  O  O     A VAL A 96  ? 0.1847 0.2365 0.2256 0.0038  -0.0016 0.0094  81   VAL A O     
410  O  O     B VAL A 96  ? 0.1916 0.2322 0.2325 0.0236  -0.0027 0.0191  81   VAL A O     
411  C  CB    A VAL A 96  ? 0.2262 0.2889 0.2651 -0.0579 0.0227  0.0061  81   VAL A CB    
412  C  CB    B VAL A 96  ? 0.2466 0.1924 0.2326 -0.0056 0.0023  0.0456  81   VAL A CB    
413  C  CG1   A VAL A 96  ? 0.2084 0.3002 0.2428 -0.0926 0.0496  -0.0314 81   VAL A CG1   
414  C  CG1   B VAL A 96  ? 0.2635 0.2143 0.2397 0.0108  0.0004  0.0517  81   VAL A CG1   
415  C  CG2   A VAL A 96  ? 0.2535 0.2973 0.2956 -0.0280 0.0309  0.0197  81   VAL A CG2   
416  C  CG2   B VAL A 96  ? 0.2555 0.1511 0.2138 -0.0181 0.0145  0.0484  81   VAL A CG2   
417  N  N     . SER A 97  ? 0.1816 0.2138 0.2415 -0.0078 -0.0038 0.0360  82   SER A N     
418  C  CA    . SER A 97  ? 0.2047 0.2036 0.2303 -0.0188 -0.0192 0.0199  82   SER A CA    
419  C  C     . SER A 97  ? 0.1833 0.2157 0.2576 -0.0163 -0.0281 -0.0066 82   SER A C     
420  O  O     . SER A 97  ? 0.1934 0.2312 0.2603 0.0114  -0.0279 0.0065  82   SER A O     
421  C  CB    . SER A 97  ? 0.2493 0.1854 0.2288 0.0028  -0.0294 0.0154  82   SER A CB    
422  O  OG    . SER A 97  ? 0.2587 0.2239 0.2430 0.0129  -0.0206 0.0169  82   SER A OG    
423  N  N     . SER A 98  ? 0.1594 0.2239 0.2341 -0.0148 -0.0297 0.0037  83   SER A N     
424  C  CA    . SER A 98  ? 0.1378 0.2157 0.2151 -0.0058 -0.0250 0.0332  83   SER A CA    
425  C  C     . SER A 98  ? 0.1812 0.2286 0.2329 0.0066  -0.0256 0.0095  83   SER A C     
426  O  O     . SER A 98  ? 0.2092 0.2131 0.2390 0.0106  -0.0150 0.0187  83   SER A O     
427  C  CB    . SER A 98  ? 0.1699 0.2230 0.2144 -0.0052 0.0013  0.0626  83   SER A CB    
428  O  OG    . SER A 98  ? 0.1957 0.2275 0.2019 -0.0216 -0.0197 0.0527  83   SER A OG    
429  N  N     . ALA A 99  ? 0.1788 0.1998 0.2388 -0.0277 0.0039  0.0403  84   ALA A N     
430  C  CA    . ALA A 99  ? 0.2220 0.1765 0.2030 -0.0400 -0.0150 0.0047  84   ALA A CA    
431  C  C     . ALA A 99  ? 0.2037 0.2234 0.2067 -0.0182 -0.0072 0.0185  84   ALA A C     
432  O  O     . ALA A 99  ? 0.2264 0.2749 0.1930 -0.0209 0.0015  0.0339  84   ALA A O     
433  C  CB    . ALA A 99  ? 0.2621 0.2196 0.2218 -0.0409 0.0048  0.0063  84   ALA A CB    
434  N  N     . MET A 100 ? 0.2178 0.2282 0.2015 0.0022  -0.0087 0.0446  85   MET A N     
435  C  CA    . MET A 100 ? 0.2357 0.2000 0.2174 0.0161  -0.0202 0.0349  85   MET A CA    
436  C  C     . MET A 100 ? 0.2312 0.2232 0.2505 -0.0048 -0.0331 0.0472  85   MET A C     
437  O  O     . MET A 100 ? 0.2151 0.2434 0.2518 0.0013  -0.0451 0.0384  85   MET A O     
438  C  CB    . MET A 100 ? 0.2397 0.1773 0.2283 0.0109  -0.0502 0.0495  85   MET A CB    
439  C  CG    . MET A 100 ? 0.2280 0.1723 0.2229 0.0180  -0.0602 0.0375  85   MET A CG    
440  S  SD    . MET A 100 ? 0.2215 0.2230 0.2234 -0.0068 -0.0093 0.0110  85   MET A SD    
441  C  CE    . MET A 100 ? 0.2117 0.2480 0.2634 -0.0291 0.0410  -0.0028 85   MET A CE    
442  N  N     . ASP A 101 ? 0.2380 0.2421 0.2512 0.0055  0.0036  0.0315  86   ASP A N     
443  C  CA    . ASP A 101 ? 0.2448 0.2367 0.2719 -0.0429 -0.0217 0.0458  86   ASP A CA    
444  C  C     . ASP A 101 ? 0.2819 0.2700 0.2608 -0.0465 0.0000  0.0297  86   ASP A C     
445  O  O     . ASP A 101 ? 0.3408 0.2854 0.2694 -0.0546 -0.0144 0.0298  86   ASP A O     
446  C  CB    . ASP A 101 ? 0.2601 0.2670 0.2994 -0.0391 -0.0013 0.0443  86   ASP A CB    
447  C  CG    . ASP A 101 ? 0.2941 0.2833 0.2890 -0.0728 0.0031  0.0584  86   ASP A CG    
448  O  OD1   . ASP A 101 ? 0.2792 0.2859 0.2732 -0.0521 -0.0157 0.0424  86   ASP A OD1   
449  O  OD2   . ASP A 101 ? 0.3252 0.2859 0.3096 -0.0179 0.0240  0.0692  86   ASP A OD2   
450  N  N     . THR A 102 ? 0.2604 0.2516 0.2499 -0.0484 0.0029  -0.0079 87   THR A N     
451  C  CA    . THR A 102 ? 0.2689 0.2580 0.2631 -0.0345 0.0045  0.0171  87   THR A CA    
452  C  C     . THR A 102 ? 0.2737 0.2549 0.2759 -0.0421 -0.0148 -0.0043 87   THR A C     
453  O  O     . THR A 102 ? 0.2924 0.2965 0.3138 -0.0449 -0.0004 -0.0175 87   THR A O     
454  C  CB    . THR A 102 ? 0.2745 0.2691 0.2496 -0.0390 -0.0048 0.0560  87   THR A CB    
455  O  OG1   . THR A 102 ? 0.3166 0.2706 0.2509 -0.0042 -0.0012 0.0292  87   THR A OG1   
456  C  CG2   . THR A 102 ? 0.3066 0.3107 0.2574 -0.0224 0.0045  0.0613  87   THR A CG2   
457  N  N     . VAL A 103 ? 0.2538 0.2502 0.2196 0.0005  0.0091  0.0122  88   VAL A N     
458  C  CA    . VAL A 103 ? 0.2312 0.2368 0.2198 -0.0122 -0.0192 0.0245  88   VAL A CA    
459  C  C     . VAL A 103 ? 0.2597 0.2305 0.2343 0.0059  -0.0240 0.0111  88   VAL A C     
460  O  O     . VAL A 103 ? 0.2529 0.2335 0.2365 0.0208  -0.0106 0.0371  88   VAL A O     
461  C  CB    . VAL A 103 ? 0.1963 0.2362 0.2174 0.0029  0.0142  0.0402  88   VAL A CB    
462  C  CG1   . VAL A 103 ? 0.1985 0.2555 0.2081 -0.0325 -0.0043 -0.0019 88   VAL A CG1   
463  C  CG2   . VAL A 103 ? 0.2283 0.2572 0.2377 0.0217  0.0107  0.0203  88   VAL A CG2   
464  N  N     . THR A 104 ? 0.2604 0.1990 0.2639 -0.0083 -0.0289 0.0033  89   THR A N     
465  C  CA    . THR A 104 ? 0.2580 0.2163 0.2724 0.0091  -0.0307 0.0212  89   THR A CA    
466  C  C     . THR A 104 ? 0.2416 0.2429 0.2705 -0.0185 -0.0479 0.0408  89   THR A C     
467  O  O     . THR A 104 ? 0.2449 0.2531 0.2530 -0.0163 -0.0345 0.0618  89   THR A O     
468  C  CB    . THR A 104 ? 0.2292 0.1583 0.2775 0.0532  -0.0116 0.0112  89   THR A CB    
469  O  OG1   . THR A 104 ? 0.2361 0.1781 0.3003 0.0179  -0.0439 0.0369  89   THR A OG1   
470  C  CG2   . THR A 104 ? 0.2358 0.1962 0.2824 0.0473  -0.0241 0.0168  89   THR A CG2   
471  N  N     . GLU A 105 ? 0.2378 0.2345 0.2824 0.0009  -0.0297 0.0926  90   GLU A N     
472  C  CA    . GLU A 105 ? 0.2148 0.2243 0.2907 0.0034  -0.0509 0.0919  90   GLU A CA    
473  C  C     . GLU A 105 ? 0.2570 0.2431 0.3159 0.0148  -0.0596 0.0614  90   GLU A C     
474  O  O     . GLU A 105 ? 0.2751 0.2314 0.3057 0.0115  -0.0509 0.0359  90   GLU A O     
475  C  CB    . GLU A 105 ? 0.2320 0.2422 0.3047 -0.0086 -0.0547 0.0853  90   GLU A CB    
476  C  CG    . GLU A 105 ? 0.2755 0.3078 0.3114 -0.0227 -0.0430 0.1159  90   GLU A CG    
477  C  CD    . GLU A 105 ? 0.3201 0.3967 0.3635 0.0002  -0.0688 0.1128  90   GLU A CD    
478  O  OE1   . GLU A 105 ? 0.3503 0.4829 0.3587 -0.0045 -0.0621 0.1121  90   GLU A OE1   
479  O  OE2   . GLU A 105 ? 0.3581 0.4023 0.3785 -0.0245 -0.0628 0.1093  90   GLU A OE2   
480  N  N     . SER A 106 ? 0.2557 0.3202 0.3249 0.0147  -0.0541 0.0638  91   SER A N     
481  C  CA    . SER A 106 ? 0.2908 0.3034 0.3255 0.0125  -0.0953 0.0736  91   SER A CA    
482  C  C     . SER A 106 ? 0.3053 0.3121 0.3244 0.0010  -0.0819 0.0534  91   SER A C     
483  O  O     . SER A 106 ? 0.2962 0.3156 0.2946 0.0241  -0.0840 0.0450  91   SER A O     
484  C  CB    . SER A 106 ? 0.3346 0.3546 0.3362 0.0134  -0.1068 0.1023  91   SER A CB    
485  O  OG    . SER A 106 ? 0.3742 0.3907 0.3320 0.0019  -0.1109 0.1287  91   SER A OG    
486  N  N     . ARG A 107 ? 0.3128 0.3038 0.3154 -0.0052 -0.0879 0.0769  92   ARG A N     
487  C  CA    . ARG A 107 ? 0.3302 0.3400 0.3422 0.0085  -0.0865 0.0780  92   ARG A CA    
488  C  C     . ARG A 107 ? 0.3039 0.2957 0.3497 0.0029  -0.0879 0.0651  92   ARG A C     
489  O  O     . ARG A 107 ? 0.3168 0.3088 0.3696 0.0106  -0.1204 0.0448  92   ARG A O     
490  C  CB    . ARG A 107 ? 0.4042 0.4207 0.3809 0.0363  -0.0761 0.0719  92   ARG A CB    
491  C  CG    . ARG A 107 ? 0.5227 0.5051 0.4578 0.0291  -0.0254 0.0404  92   ARG A CG    
492  C  CD    . ARG A 107 ? 0.6358 0.5590 0.5276 0.0211  0.0034  0.0518  92   ARG A CD    
493  N  NE    . ARG A 107 ? 0.7055 0.6005 0.5701 0.0133  0.0122  0.0765  92   ARG A NE    
494  C  CZ    . ARG A 107 ? 0.7457 0.6451 0.6023 0.0075  0.0049  0.0813  92   ARG A CZ    
495  N  NH1   . ARG A 107 ? 0.7632 0.6880 0.6375 -0.0015 0.0131  0.0715  92   ARG A NH1   
496  N  NH2   . ARG A 107 ? 0.7760 0.6264 0.6326 0.0156  -0.0084 0.1048  92   ARG A NH2   
497  N  N     . MET A 108 ? 0.2764 0.2611 0.3290 -0.0019 -0.0784 0.0733  93   MET A N     
498  C  CA    . MET A 108 ? 0.2573 0.2594 0.3282 0.0123  -0.0597 0.0680  93   MET A CA    
499  C  C     . MET A 108 ? 0.2336 0.2531 0.3263 0.0179  -0.0497 0.0512  93   MET A C     
500  O  O     . MET A 108 ? 0.2503 0.2648 0.3251 0.0274  -0.0816 0.0334  93   MET A O     
501  C  CB    . MET A 108 ? 0.2425 0.2617 0.3045 -0.0026 -0.0612 0.0429  93   MET A CB    
502  C  CG    . MET A 108 ? 0.2300 0.2216 0.2852 -0.0259 -0.0698 0.0298  93   MET A CG    
503  S  SD    . MET A 108 ? 0.2490 0.2515 0.3026 -0.0150 -0.0259 0.0027  93   MET A SD    
504  C  CE    . MET A 108 ? 0.2943 0.2610 0.3030 0.0102  -0.0379 -0.0081 93   MET A CE    
505  N  N     . ALA A 109 ? 0.2285 0.2544 0.3079 0.0213  -0.0365 0.0178  94   ALA A N     
506  C  CA    . ALA A 109 ? 0.2272 0.2776 0.3159 -0.0052 -0.0295 0.0181  94   ALA A CA    
507  C  C     . ALA A 109 ? 0.2393 0.2718 0.3316 0.0051  -0.0588 0.0256  94   ALA A C     
508  O  O     . ALA A 109 ? 0.2624 0.2445 0.3463 0.0286  -0.0667 0.0342  94   ALA A O     
509  C  CB    . ALA A 109 ? 0.2133 0.2833 0.3055 0.0158  -0.0285 -0.0026 94   ALA A CB    
510  N  N     . ILE A 110 ? 0.2160 0.2727 0.3254 -0.0169 -0.0849 0.0587  95   ILE A N     
511  C  CA    . ILE A 110 ? 0.2520 0.2773 0.3254 -0.0024 -0.0913 0.0708  95   ILE A CA    
512  C  C     . ILE A 110 ? 0.2731 0.2807 0.3337 -0.0232 -0.0831 0.0585  95   ILE A C     
513  O  O     . ILE A 110 ? 0.2796 0.2900 0.3416 0.0017  -0.0827 0.0554  95   ILE A O     
514  C  CB    . ILE A 110 ? 0.2371 0.2696 0.3233 -0.0149 -0.1029 0.0642  95   ILE A CB    
515  C  CG1   . ILE A 110 ? 0.2661 0.2830 0.3233 0.0083  -0.1082 0.0969  95   ILE A CG1   
516  C  CG2   . ILE A 110 ? 0.2724 0.3010 0.3516 -0.0200 -0.0702 0.0577  95   ILE A CG2   
517  C  CD1   . ILE A 110 ? 0.2955 0.2896 0.3128 0.0187  -0.0912 0.0830  95   ILE A CD1   
518  N  N     . ALA A 111 ? 0.2758 0.2566 0.3045 -0.0174 -0.0872 0.0442  96   ALA A N     
519  C  CA    . ALA A 111 ? 0.2698 0.2451 0.2737 -0.0157 -0.0408 0.0387  96   ALA A CA    
520  C  C     . ALA A 111 ? 0.2377 0.2720 0.2900 -0.0027 -0.0534 0.0384  96   ALA A C     
521  O  O     . ALA A 111 ? 0.2231 0.2938 0.2931 -0.0178 -0.0407 0.0501  96   ALA A O     
522  C  CB    . ALA A 111 ? 0.2884 0.2312 0.2476 0.0026  -0.0392 0.0373  96   ALA A CB    
523  N  N     . MET A 112 ? 0.2446 0.2843 0.2743 0.0020  -0.0679 0.0104  97   MET A N     
524  C  CA    . MET A 112 ? 0.2474 0.2786 0.2705 0.0135  -0.0641 0.0296  97   MET A CA    
525  C  C     . MET A 112 ? 0.2717 0.2772 0.2937 0.0342  -0.0614 0.0348  97   MET A C     
526  O  O     . MET A 112 ? 0.2544 0.2850 0.2820 0.0294  -0.0508 0.0490  97   MET A O     
527  C  CB    . MET A 112 ? 0.2468 0.2634 0.2711 0.0074  -0.0623 0.0251  97   MET A CB    
528  C  CG    . MET A 112 ? 0.2371 0.2309 0.2625 0.0142  -0.0312 0.0090  97   MET A CG    
529  S  SD    . MET A 112 ? 0.2490 0.2621 0.2430 0.0177  -0.0358 0.0183  97   MET A SD    
530  C  CE    . MET A 112 ? 0.2664 0.2496 0.2512 0.0294  -0.0486 0.0354  97   MET A CE    
531  N  N     . ALA A 113 ? 0.2744 0.2784 0.3291 0.0343  -0.0667 0.0342  98   ALA A N     
532  C  CA    . ALA A 113 ? 0.2405 0.2284 0.3707 0.0458  -0.0471 0.0092  98   ALA A CA    
533  C  C     . ALA A 113 ? 0.2207 0.2709 0.4029 0.0178  -0.0666 0.0261  98   ALA A C     
534  O  O     . ALA A 113 ? 0.2228 0.2856 0.4031 0.0080  -0.0616 0.0449  98   ALA A O     
535  C  CB    . ALA A 113 ? 0.2599 0.2157 0.3601 0.0613  -0.0172 0.0347  98   ALA A CB    
536  N  N     . ARG A 114 ? 0.2120 0.2668 0.4036 -0.0098 -0.0902 0.0423  99   ARG A N     
537  C  CA    . ARG A 114 ? 0.2648 0.3004 0.4016 -0.0449 -0.1172 0.0749  99   ARG A CA    
538  C  C     . ARG A 114 ? 0.2554 0.3100 0.3973 -0.0383 -0.0928 0.0592  99   ARG A C     
539  O  O     . ARG A 114 ? 0.2936 0.3334 0.3933 -0.0511 -0.0902 0.0700  99   ARG A O     
540  C  CB    . ARG A 114 ? 0.2950 0.2910 0.4189 -0.0523 -0.1310 0.1197  99   ARG A CB    
541  C  CG    . ARG A 114 ? 0.3151 0.2955 0.4363 -0.0369 -0.1470 0.1155  99   ARG A CG    
542  C  CD    . ARG A 114 ? 0.3817 0.3225 0.4668 -0.0291 -0.1336 0.1308  99   ARG A CD    
543  N  NE    . ARG A 114 ? 0.4220 0.3753 0.5009 -0.0435 -0.1462 0.1401  99   ARG A NE    
544  C  CZ    . ARG A 114 ? 0.4697 0.4094 0.5478 -0.0424 -0.1356 0.1245  99   ARG A CZ    
545  N  NH1   . ARG A 114 ? 0.4595 0.4113 0.5452 -0.0625 -0.1327 0.0980  99   ARG A NH1   
546  N  NH2   . ARG A 114 ? 0.5129 0.4331 0.5684 -0.0182 -0.1438 0.1366  99   ARG A NH2   
547  N  N     . ALA A 115 ? 0.2210 0.2944 0.3743 0.0023  -0.0613 0.0317  100  ALA A N     
548  C  CA    . ALA A 115 ? 0.2180 0.2900 0.3505 0.0052  -0.0399 0.0528  100  ALA A CA    
549  C  C     . ALA A 115 ? 0.2430 0.2849 0.3779 -0.0243 -0.0571 0.0529  100  ALA A C     
550  O  O     . ALA A 115 ? 0.2711 0.2938 0.3836 -0.0170 -0.0645 0.0493  100  ALA A O     
551  C  CB    . ALA A 115 ? 0.2101 0.2990 0.3407 0.0145  -0.0196 0.0417  100  ALA A CB    
552  N  N     . GLY A 116 ? 0.2265 0.2732 0.3500 -0.0210 -0.0862 0.0420  101  GLY A N     
553  C  CA    . GLY A 116 ? 0.2243 0.2672 0.3429 -0.0318 -0.0637 0.0322  101  GLY A CA    
554  C  C     . GLY A 116 ? 0.2150 0.2431 0.3164 -0.0363 -0.0669 0.0235  101  GLY A C     
555  O  O     . GLY A 116 ? 0.2335 0.2511 0.3275 0.0024  -0.0415 0.0227  101  GLY A O     
556  N  N     . GLY A 117 ? 0.1983 0.2398 0.3130 -0.0569 -0.0106 0.0121  102  GLY A N     
557  C  CA    . GLY A 117 ? 0.1790 0.2114 0.3195 -0.0573 0.0014  0.0102  102  GLY A CA    
558  C  C     . GLY A 117 ? 0.1774 0.1834 0.3241 -0.0576 0.0047  0.0332  102  GLY A C     
559  O  O     . GLY A 117 ? 0.1972 0.2221 0.3296 -0.0064 -0.0028 0.0221  102  GLY A O     
560  N  N     . MET A 118 ? 0.2214 0.2105 0.2976 -0.0281 -0.0071 0.0283  103  MET A N     
561  C  CA    . MET A 118 ? 0.2099 0.1878 0.2867 -0.0321 -0.0094 0.0009  103  MET A CA    
562  C  C     . MET A 118 ? 0.2039 0.2162 0.2776 -0.0085 -0.0170 0.0237  103  MET A C     
563  O  O     . MET A 118 ? 0.2256 0.2602 0.2522 0.0288  -0.0077 0.0406  103  MET A O     
564  C  CB    . MET A 118 ? 0.2005 0.1642 0.2985 -0.0115 -0.0201 0.0005  103  MET A CB    
565  C  CG    . MET A 118 ? 0.2120 0.1792 0.3037 0.0098  -0.0197 -0.0304 103  MET A CG    
566  S  SD    . MET A 118 ? 0.2235 0.2134 0.3454 0.0153  0.0058  0.0131  103  MET A SD    
567  C  CE    . MET A 118 ? 0.2199 0.2332 0.3715 0.0236  -0.0033 0.0445  103  MET A CE    
568  N  N     . GLY A 119 ? 0.1621 0.2206 0.2956 -0.0078 -0.0337 0.0157  104  GLY A N     
569  C  CA    . GLY A 119 ? 0.1717 0.2187 0.3123 -0.0327 -0.0488 0.0284  104  GLY A CA    
570  C  C     . GLY A 119 ? 0.1893 0.2181 0.2969 -0.0339 -0.0355 0.0281  104  GLY A C     
571  O  O     . GLY A 119 ? 0.2324 0.2335 0.2881 -0.0201 0.0088  0.0569  104  GLY A O     
572  N  N     . VAL A 120 ? 0.1859 0.1998 0.2664 -0.0065 -0.0274 0.0501  105  VAL A N     
573  C  CA    . VAL A 120 ? 0.1890 0.2025 0.2542 -0.0303 -0.0555 0.0345  105  VAL A CA    
574  C  C     . VAL A 120 ? 0.2160 0.1988 0.2411 -0.0140 -0.0304 0.0318  105  VAL A C     
575  O  O     . VAL A 120 ? 0.2232 0.2285 0.2190 -0.0105 -0.0327 -0.0011 105  VAL A O     
576  C  CB    . VAL A 120 ? 0.1942 0.2117 0.2345 -0.0542 -0.0284 0.0300  105  VAL A CB    
577  C  CG1   . VAL A 120 ? 0.1866 0.2244 0.2313 0.0141  -0.0335 -0.0007 105  VAL A CG1   
578  C  CG2   . VAL A 120 ? 0.2459 0.2250 0.2311 -0.0360 -0.0155 0.0188  105  VAL A CG2   
579  N  N     . LEU A 121 ? 0.2233 0.1671 0.2436 -0.0038 -0.0271 0.0457  106  LEU A N     
580  C  CA    . LEU A 121 ? 0.2060 0.1853 0.2559 0.0021  0.0000  0.0504  106  LEU A CA    
581  C  C     . LEU A 121 ? 0.2293 0.2365 0.2798 -0.0163 -0.0170 0.0373  106  LEU A C     
582  O  O     . LEU A 121 ? 0.2679 0.2332 0.2427 -0.0200 0.0135  0.0065  106  LEU A O     
583  C  CB    . LEU A 121 ? 0.2226 0.1896 0.2685 0.0187  -0.0469 0.0195  106  LEU A CB    
584  C  CG    . LEU A 121 ? 0.2399 0.1872 0.2821 0.0596  -0.0392 -0.0133 106  LEU A CG    
585  C  CD1   . LEU A 121 ? 0.2741 0.2344 0.3123 0.0608  -0.0354 0.0243  106  LEU A CD1   
586  C  CD2   . LEU A 121 ? 0.2945 0.2048 0.2810 0.0214  -0.0232 -0.0108 106  LEU A CD2   
587  N  N     . HIS A 122 ? 0.2233 0.2268 0.2823 0.0236  -0.0050 0.0441  107  HIS A N     
588  C  CA    . HIS A 122 ? 0.2469 0.2222 0.2858 0.0079  0.0055  0.0345  107  HIS A CA    
589  C  C     . HIS A 122 ? 0.2662 0.2140 0.2723 -0.0070 -0.0204 0.0103  107  HIS A C     
590  O  O     . HIS A 122 ? 0.2978 0.2293 0.2644 0.0071  -0.0202 -0.0105 107  HIS A O     
591  C  CB    . HIS A 122 ? 0.2776 0.2230 0.2620 0.0239  -0.0068 0.0492  107  HIS A CB    
592  C  CG    . HIS A 122 ? 0.2748 0.2379 0.2694 -0.0244 0.0080  0.0343  107  HIS A CG    
593  N  ND1   . HIS A 122 ? 0.2588 0.2468 0.2515 -0.0109 0.0103  0.0180  107  HIS A ND1   
594  C  CD2   . HIS A 122 ? 0.2563 0.2465 0.2580 -0.0371 0.0189  0.0430  107  HIS A CD2   
595  C  CE1   . HIS A 122 ? 0.2648 0.2559 0.2795 -0.0584 0.0060  0.0164  107  HIS A CE1   
596  N  NE2   . HIS A 122 ? 0.2622 0.2583 0.2806 -0.0564 0.0311  0.0569  107  HIS A NE2   
597  N  N     . ARG A 123 ? 0.2767 0.2221 0.2687 -0.0489 -0.0111 0.0126  108  ARG A N     
598  C  CA    . ARG A 123 ? 0.2521 0.1974 0.2333 -0.0415 -0.0234 0.0094  108  ARG A CA    
599  C  C     . ARG A 123 ? 0.2681 0.2245 0.2598 -0.0608 -0.0228 0.0093  108  ARG A C     
600  O  O     . ARG A 123 ? 0.2915 0.2697 0.2596 -0.0610 -0.0072 -0.0002 108  ARG A O     
601  C  CB    . ARG A 123 ? 0.2438 0.2202 0.2388 -0.0179 -0.0489 0.0064  108  ARG A CB    
602  C  CG    . ARG A 123 ? 0.2286 0.2453 0.2446 0.0253  -0.0635 0.0339  108  ARG A CG    
603  C  CD    . ARG A 123 ? 0.2136 0.2209 0.2668 0.0428  -0.0726 0.0733  108  ARG A CD    
604  N  NE    . ARG A 123 ? 0.2364 0.2366 0.3014 -0.0031 -0.0179 0.0553  108  ARG A NE    
605  C  CZ    . ARG A 123 ? 0.2456 0.2098 0.3297 -0.0011 -0.0326 0.0653  108  ARG A CZ    
606  N  NH1   . ARG A 123 ? 0.2405 0.2087 0.3224 0.0220  -0.0349 0.0598  108  ARG A NH1   
607  N  NH2   . ARG A 123 ? 0.2523 0.1888 0.3548 -0.0250 -0.0250 0.0464  108  ARG A NH2   
608  N  N     . ASN A 124 ? 0.2768 0.2269 0.2451 -0.0602 -0.0100 0.0212  109  ASN A N     
609  C  CA    . ASN A 124 ? 0.3207 0.2286 0.2673 -0.0316 0.0122  0.0304  109  ASN A CA    
610  C  C     . ASN A 124 ? 0.3573 0.2558 0.2882 -0.0224 -0.0077 0.0360  109  ASN A C     
611  O  O     . ASN A 124 ? 0.3738 0.2900 0.2985 -0.0149 -0.0196 0.0583  109  ASN A O     
612  C  CB    . ASN A 124 ? 0.3123 0.2483 0.3049 -0.0430 0.0690  0.0224  109  ASN A CB    
613  C  CG    . ASN A 124 ? 0.3420 0.2945 0.3864 -0.0524 0.0691  0.0027  109  ASN A CG    
614  O  OD1   . ASN A 124 ? 0.3539 0.3251 0.4472 -0.0665 0.0789  -0.0125 109  ASN A OD1   
615  N  ND2   . ASN A 124 ? 0.3330 0.3292 0.3898 -0.0687 0.0624  0.0175  109  ASN A ND2   
616  N  N     . LEU A 125 ? 0.3899 0.2729 0.3079 0.0117  -0.0415 0.0707  110  LEU A N     
617  C  CA    . LEU A 125 ? 0.3917 0.2710 0.3408 -0.0120 -0.0437 0.0569  110  LEU A CA    
618  C  C     . LEU A 125 ? 0.4350 0.2840 0.3483 -0.0098 -0.0257 0.0767  110  LEU A C     
619  O  O     . LEU A 125 ? 0.4560 0.2944 0.3153 -0.0301 -0.0135 0.0646  110  LEU A O     
620  C  CB    . LEU A 125 ? 0.3810 0.2957 0.3627 -0.0214 -0.0523 0.0419  110  LEU A CB    
621  C  CG    . LEU A 125 ? 0.3202 0.2948 0.3463 -0.0428 -0.0529 0.0606  110  LEU A CG    
622  C  CD1   . LEU A 125 ? 0.3348 0.3357 0.3620 -0.0475 -0.0391 0.0453  110  LEU A CD1   
623  C  CD2   . LEU A 125 ? 0.2998 0.2686 0.3281 -0.0353 -0.0588 0.0670  110  LEU A CD2   
624  N  N     . PRO A 126 ? 0.4597 0.2540 0.3568 0.0219  -0.0135 0.1030  111  PRO A N     
625  C  CA    . PRO A 126 ? 0.4729 0.2532 0.3760 0.0227  -0.0099 0.0877  111  PRO A CA    
626  C  C     . PRO A 126 ? 0.4777 0.2627 0.3836 0.0012  -0.0009 0.1005  111  PRO A C     
627  O  O     . PRO A 126 ? 0.4897 0.2753 0.3998 0.0185  -0.0338 0.1065  111  PRO A O     
628  C  CB    . PRO A 126 ? 0.4941 0.2635 0.3838 0.0392  0.0050  0.0644  111  PRO A CB    
629  C  CG    . PRO A 126 ? 0.4920 0.2755 0.3852 0.0307  0.0148  0.0641  111  PRO A CG    
630  C  CD    . PRO A 126 ? 0.4736 0.2511 0.3732 0.0290  0.0130  0.0968  111  PRO A CD    
631  N  N     . VAL A 127 ? 0.4491 0.2327 0.3898 0.0095  0.0048  0.0904  112  VAL A N     
632  C  CA    . VAL A 127 ? 0.4438 0.2464 0.3812 0.0012  -0.0098 0.0852  112  VAL A CA    
633  C  C     . VAL A 127 ? 0.4526 0.2550 0.3753 -0.0075 -0.0542 0.0819  112  VAL A C     
634  O  O     . VAL A 127 ? 0.4635 0.2607 0.3667 0.0006  -0.0796 0.0710  112  VAL A O     
635  C  CB    . VAL A 127 ? 0.4326 0.2671 0.3837 0.0201  -0.0195 0.0562  112  VAL A CB    
636  C  CG1   . VAL A 127 ? 0.4519 0.2808 0.3875 0.0067  -0.0176 0.0551  112  VAL A CG1   
637  C  CG2   . VAL A 127 ? 0.4423 0.2534 0.4082 0.0214  -0.0181 0.0762  112  VAL A CG2   
638  N  N     . ALA A 128 ? 0.4550 0.2524 0.3963 0.0139  -0.0553 0.0642  113  ALA A N     
639  C  CA    . ALA A 128 ? 0.4665 0.2249 0.3978 0.0240  -0.0622 0.0951  113  ALA A CA    
640  C  C     . ALA A 128 ? 0.4660 0.2565 0.4080 0.0321  -0.0766 0.1092  113  ALA A C     
641  O  O     . ALA A 128 ? 0.4934 0.2874 0.4441 0.0292  -0.0613 0.1056  113  ALA A O     
642  C  CB    . ALA A 128 ? 0.4740 0.2358 0.3961 0.0195  -0.0370 0.1035  113  ALA A CB    
643  N  N     . GLU A 129 ? 0.4604 0.2428 0.3769 0.0444  -0.0782 0.1151  114  GLU A N     
644  C  CA    . GLU A 129 ? 0.4656 0.3033 0.3676 0.0280  -0.0647 0.1182  114  GLU A CA    
645  C  C     . GLU A 129 ? 0.4101 0.2710 0.3436 0.0191  -0.0636 0.0884  114  GLU A C     
646  O  O     . GLU A 129 ? 0.4010 0.2605 0.3308 0.0195  -0.0728 0.0376  114  GLU A O     
647  C  CB    . GLU A 129 ? 0.5127 0.3842 0.3862 0.0335  -0.0457 0.1217  114  GLU A CB    
648  C  CG    . GLU A 129 ? 0.5707 0.4430 0.4276 0.0327  -0.0435 0.1061  114  GLU A CG    
649  C  CD    . GLU A 129 ? 0.6461 0.5303 0.4804 -0.0029 -0.0282 0.0956  114  GLU A CD    
650  O  OE1   . GLU A 129 ? 0.6910 0.5387 0.4865 0.0212  -0.0455 0.1068  114  GLU A OE1   
651  O  OE2   . GLU A 129 ? 0.6647 0.5995 0.5275 -0.0371 -0.0080 0.0645  114  GLU A OE2   
652  N  N     . GLN A 130 ? 0.3780 0.2772 0.3233 0.0212  -0.0773 0.0852  115  GLN A N     
653  C  CA    . GLN A 130 ? 0.3213 0.2320 0.3142 0.0462  -0.0710 0.0942  115  GLN A CA    
654  C  C     . GLN A 130 ? 0.3338 0.2345 0.3549 0.0289  -0.0609 0.0675  115  GLN A C     
655  O  O     . GLN A 130 ? 0.3379 0.2535 0.3824 0.0414  -0.0663 0.0354  115  GLN A O     
656  C  CB    . GLN A 130 ? 0.2807 0.2189 0.2910 0.0420  -0.0290 0.0626  115  GLN A CB    
657  C  CG    . GLN A 130 ? 0.2845 0.2130 0.2976 0.0191  -0.0309 0.0622  115  GLN A CG    
658  C  CD    . GLN A 130 ? 0.2857 0.2134 0.3120 0.0088  -0.0053 0.0562  115  GLN A CD    
659  O  OE1   . GLN A 130 ? 0.2891 0.2176 0.3127 -0.0190 -0.0258 0.0419  115  GLN A OE1   
660  N  NE2   . GLN A 130 ? 0.2538 0.2265 0.3261 0.0167  0.0119  0.0201  115  GLN A NE2   
661  N  N     . ALA A 131 ? 0.3472 0.2284 0.3601 0.0292  -0.0710 0.0697  116  ALA A N     
662  C  CA    . ALA A 131 ? 0.3385 0.2284 0.3857 0.0020  -0.0844 0.0497  116  ALA A CA    
663  C  C     . ALA A 131 ? 0.3707 0.2639 0.4088 0.0067  -0.1001 0.0611  116  ALA A C     
664  O  O     . ALA A 131 ? 0.4136 0.2516 0.4346 0.0220  -0.1333 0.0630  116  ALA A O     
665  C  CB    . ALA A 131 ? 0.3189 0.2021 0.3894 0.0040  -0.0522 0.0656  116  ALA A CB    
666  N  N     . GLY A 132 ? 0.3764 0.2832 0.3847 -0.0076 -0.1195 0.0689  117  GLY A N     
667  C  CA    . GLY A 132 ? 0.3982 0.2827 0.3995 -0.0023 -0.1172 0.0702  117  GLY A CA    
668  C  C     . GLY A 132 ? 0.4110 0.2929 0.4147 -0.0102 -0.1318 0.0823  117  GLY A C     
669  O  O     . GLY A 132 ? 0.3929 0.3154 0.4353 -0.0027 -0.1576 0.0878  117  GLY A O     
670  N  N     . GLN A 133 ? 0.4388 0.2785 0.4075 -0.0080 -0.1036 0.0991  118  GLN A N     
671  C  CA    . GLN A 133 ? 0.4425 0.2159 0.3993 0.0026  -0.0852 0.0921  118  GLN A CA    
672  C  C     . GLN A 133 ? 0.4389 0.2134 0.4417 0.0020  -0.0933 0.0619  118  GLN A C     
673  O  O     . GLN A 133 ? 0.4610 0.2311 0.4547 -0.0197 -0.1053 0.0617  118  GLN A O     
674  C  CB    . GLN A 133 ? 0.4534 0.2546 0.3629 -0.0336 -0.0148 0.1111  118  GLN A CB    
675  C  CG    . GLN A 133 ? 0.5121 0.3085 0.3589 -0.0329 0.0558  0.1100  118  GLN A CG    
676  C  CD    . GLN A 133 ? 0.5671 0.3247 0.3813 -0.0325 0.1149  0.1185  118  GLN A CD    
677  O  OE1   . GLN A 133 ? 0.6168 0.3492 0.4319 0.0102  0.1285  0.0965  118  GLN A OE1   
678  N  NE2   . GLN A 133 ? 0.5777 0.3367 0.3869 -0.0431 0.1201  0.0748  118  GLN A NE2   
679  N  N     . VAL A 134 ? 0.4145 0.2461 0.4565 0.0422  -0.1089 0.0416  119  VAL A N     
680  C  CA    . VAL A 134 ? 0.3837 0.2664 0.4725 0.0509  -0.1428 0.0337  119  VAL A CA    
681  C  C     . VAL A 134 ? 0.3919 0.2916 0.4949 0.0623  -0.1645 0.0548  119  VAL A C     
682  O  O     . VAL A 134 ? 0.3903 0.2898 0.4996 0.0142  -0.1368 0.0285  119  VAL A O     
683  C  CB    . VAL A 134 ? 0.3458 0.2526 0.4744 0.0644  -0.1355 0.0057  119  VAL A CB    
684  C  CG1   . VAL A 134 ? 0.3301 0.2705 0.4837 0.0549  -0.1183 -0.0158 119  VAL A CG1   
685  C  CG2   . VAL A 134 ? 0.3349 0.2290 0.4539 0.0756  -0.1496 0.0069  119  VAL A CG2   
686  N  N     . GLU A 135 ? 0.4150 0.3208 0.5277 0.0884  -0.1688 0.0689  120  GLU A N     
687  C  CA    . GLU A 135 ? 0.4481 0.3680 0.5675 0.0905  -0.1743 0.0859  120  GLU A CA    
688  C  C     . GLU A 135 ? 0.4374 0.3778 0.5736 0.0726  -0.1703 0.0770  120  GLU A C     
689  O  O     . GLU A 135 ? 0.4319 0.3936 0.6083 0.1032  -0.1653 0.0673  120  GLU A O     
690  C  CB    . GLU A 135 ? 0.5502 0.4110 0.6257 0.1053  -0.1659 0.1349  120  GLU A CB    
691  C  CG    . GLU A 135 ? 0.6472 0.4627 0.6828 0.1051  -0.1516 0.1570  120  GLU A CG    
692  C  CD    . GLU A 135 ? 0.7245 0.5342 0.7348 0.0918  -0.1455 0.1654  120  GLU A CD    
693  O  OE1   . GLU A 135 ? 0.7748 0.6003 0.7502 0.0736  -0.1221 0.1783  120  GLU A OE1   
694  O  OE2   . GLU A 135 ? 0.7456 0.5444 0.7616 0.0980  -0.1483 0.1628  120  GLU A OE2   
695  N  N     . MET A 136 ? 0.4432 0.3581 0.5308 0.0555  -0.1744 0.0827  121  MET A N     
696  C  CA    . MET A 136 ? 0.4551 0.3802 0.5162 0.0455  -0.1725 0.0862  121  MET A CA    
697  C  C     . MET A 136 ? 0.4182 0.3580 0.5137 0.0488  -0.1394 0.0795  121  MET A C     
698  O  O     . MET A 136 ? 0.4453 0.3688 0.5453 0.0671  -0.1266 0.0876  121  MET A O     
699  C  CB    . MET A 136 ? 0.5162 0.4440 0.5318 0.0156  -0.1793 0.0989  121  MET A CB    
700  C  CG    . MET A 136 ? 0.5990 0.5116 0.5707 -0.0127 -0.1530 0.0871  121  MET A CG    
701  S  SD    . MET A 136 ? 0.7105 0.5583 0.6151 -0.0543 -0.1321 0.0809  121  MET A SD    
702  C  CE    . MET A 136 ? 0.7058 0.5571 0.6251 -0.0648 -0.1210 0.0737  121  MET A CE    
703  N  N     . VAL A 137 ? 0.3734 0.3223 0.4782 0.0445  -0.1073 0.0685  122  VAL A N     
704  C  CA    . VAL A 137 ? 0.3364 0.3463 0.4716 0.0361  -0.0794 0.0430  122  VAL A CA    
705  C  C     . VAL A 137 ? 0.3647 0.3725 0.5334 0.0383  -0.0530 -0.0077 122  VAL A C     
706  O  O     . VAL A 137 ? 0.3315 0.3816 0.5563 0.0154  -0.0917 -0.0273 122  VAL A O     
707  C  CB    . VAL A 137 ? 0.3078 0.3535 0.4333 0.0121  -0.0672 0.0395  122  VAL A CB    
708  C  CG1   . VAL A 137 ? 0.3096 0.3644 0.4075 -0.0078 -0.0825 0.0250  122  VAL A CG1   
709  C  CG2   . VAL A 137 ? 0.2739 0.3511 0.4189 0.0050  -0.0944 0.0428  122  VAL A CG2   
710  N  N     . LYS A 138 ? 0.4195 0.3916 0.5576 0.0462  -0.0060 -0.0373 123  LYS A N     
711  C  CA    . LYS A 138 ? 0.4771 0.4221 0.5888 0.0212  0.0029  -0.0391 123  LYS A CA    
712  C  C     . LYS A 138 ? 0.5067 0.4631 0.6517 0.0036  -0.0141 -0.0343 123  LYS A C     
713  O  O     . LYS A 138 ? 0.5496 0.4971 0.6917 0.0351  -0.0200 -0.0382 123  LYS A O     
714  C  CB    . LYS A 138 ? 0.4877 0.4038 0.5615 0.0161  0.0124  -0.0497 123  LYS A CB    
715  C  CG    . LYS A 138 ? 0.4806 0.3814 0.5343 0.0144  0.0048  -0.0427 123  LYS A CG    
716  C  CD    . LYS A 138 ? 0.4638 0.3606 0.5223 0.0097  -0.0274 0.0045  123  LYS A CD    
717  C  CE    . LYS A 138 ? 0.4229 0.3391 0.4992 -0.0093 -0.0930 0.0297  123  LYS A CE    
718  N  NZ    . LYS A 138 ? 0.3884 0.3286 0.4928 -0.0214 -0.1061 0.0400  123  LYS A NZ    
719  N  N     . ARG A 139 ? 0.5095 0.4833 0.6905 -0.0156 -0.0518 -0.0126 124  ARG A N     
720  C  CA    . ARG A 139 ? 0.5121 0.5396 0.7316 -0.0092 -0.0841 0.0192  124  ARG A CA    
721  C  C     . ARG A 139 ? 0.4737 0.5280 0.7400 0.0128  -0.1087 0.0419  124  ARG A C     
722  O  O     . ARG A 139 ? 0.4375 0.4971 0.7336 0.0147  -0.1262 0.0564  124  ARG A O     
723  C  CB    . ARG A 139 ? 0.5829 0.6155 0.7635 -0.0001 -0.0797 0.0413  124  ARG A CB    
724  C  CG    . ARG A 139 ? 0.6671 0.6874 0.7847 0.0025  -0.0479 0.0528  124  ARG A CG    
725  C  CD    . ARG A 139 ? 0.7371 0.7398 0.7901 0.0077  -0.0211 0.0586  124  ARG A CD    
726  N  NE    . ARG A 139 ? 0.7930 0.7843 0.7986 0.0127  -0.0014 0.0664  124  ARG A NE    
727  C  CZ    . ARG A 139 ? 0.8262 0.8223 0.8217 0.0064  0.0164  0.0649  124  ARG A CZ    
728  N  NH1   . ARG A 139 ? 0.8413 0.8376 0.8329 0.0074  0.0229  0.0766  124  ARG A NH1   
729  N  NH2   . ARG A 139 ? 0.8425 0.8309 0.8282 0.0005  0.0251  0.0511  124  ARG A NH2   
730  N  N     . SER A 140 ? 0.4727 0.5420 0.7417 0.0519  -0.1024 0.0614  125  SER A N     
731  C  CA    . SER A 140 ? 0.4868 0.5672 0.7239 0.0773  -0.0896 0.0634  125  SER A CA    
732  C  C     . SER A 140 ? 0.5102 0.5914 0.7007 0.0740  -0.0792 0.0745  125  SER A C     
733  O  O     . SER A 140 ? 0.5193 0.6150 0.7057 0.0383  -0.0723 0.0852  125  SER A O     
734  C  CB    . SER A 140 ? 0.4997 0.5843 0.7285 0.0780  -0.0795 0.0440  125  SER A CB    
735  O  OG    . SER A 140 ? 0.5168 0.6097 0.7378 0.0873  -0.0917 0.0211  125  SER A OG    
736  N  N     . GLY A 141 ? 0.5280 0.6045 0.6748 0.0925  -0.0812 0.0727  126  GLY A N     
737  C  CA    . GLY A 141 ? 0.5196 0.6087 0.6568 0.1269  -0.0789 0.0637  126  GLY A CA    
738  C  C     . GLY A 141 ? 0.5121 0.5934 0.6332 0.1599  -0.0759 0.0585  126  GLY A C     
739  O  O     . GLY A 141 ? 0.5049 0.5850 0.6458 0.1728  -0.0547 0.0619  126  GLY A O     
740  N  N     . GLY A 142 ? 0.4982 0.5795 0.6013 0.1714  -0.0910 0.0534  127  GLY A N     
741  C  CA    . GLY A 142 ? 0.4956 0.5706 0.5826 0.1655  -0.0762 0.0371  127  GLY A CA    
742  C  C     . GLY A 142 ? 0.4652 0.5439 0.5480 0.1775  -0.0837 0.0415  127  GLY A C     
743  O  O     . GLY A 142 ? 0.5052 0.5735 0.5563 0.1801  -0.0635 0.0547  127  GLY A O     
744  N  N     . LEU A 143 ? 0.3892 0.4642 0.5153 0.1241  -0.0735 0.0111  253  LEU A N     
745  C  CA    . LEU A 143 ? 0.3343 0.3714 0.4816 0.0765  -0.0812 -0.0097 253  LEU A CA    
746  C  C     . LEU A 143 ? 0.3028 0.3179 0.4439 0.0478  -0.0689 -0.0186 253  LEU A C     
747  O  O     . LEU A 143 ? 0.3529 0.2793 0.4545 0.0258  -0.0460 -0.0088 253  LEU A O     
748  C  CB    . LEU A 143 ? 0.3178 0.3898 0.4566 0.0718  -0.0768 -0.0194 253  LEU A CB    
749  C  CG    . LEU A 143 ? 0.3332 0.3886 0.4444 0.0671  -0.0773 0.0148  253  LEU A CG    
750  C  CD1   . LEU A 143 ? 0.3365 0.3875 0.4175 0.0434  -0.0795 0.0275  253  LEU A CD1   
751  C  CD2   . LEU A 143 ? 0.3520 0.4072 0.4573 0.0437  -0.0935 0.0162  253  LEU A CD2   
752  N  N     . LEU A 144 ? 0.2573 0.2999 0.4056 0.0219  -0.0458 -0.0332 254  LEU A N     
753  C  CA    . LEU A 144 ? 0.2623 0.2810 0.3736 0.0200  -0.0389 -0.0234 254  LEU A CA    
754  C  C     . LEU A 144 ? 0.2311 0.2873 0.3578 0.0047  -0.0221 -0.0276 254  LEU A C     
755  O  O     . LEU A 144 ? 0.2172 0.2872 0.3291 0.0314  -0.0265 -0.0158 254  LEU A O     
756  C  CB    . LEU A 144 ? 0.3216 0.2930 0.3771 0.0151  -0.0079 -0.0245 254  LEU A CB    
757  C  CG    . LEU A 144 ? 0.3549 0.2637 0.4091 0.0021  -0.0133 -0.0062 254  LEU A CG    
758  C  CD1   . LEU A 144 ? 0.3481 0.2920 0.4365 0.0395  0.0042  0.0191  254  LEU A CD1   
759  C  CD2   . LEU A 144 ? 0.3663 0.2606 0.4024 -0.0463 -0.0370 -0.0257 254  LEU A CD2   
760  N  N     . VAL A 145 ? 0.2102 0.2577 0.3390 0.0186  -0.0243 0.0068  255  VAL A N     
761  C  CA    . VAL A 145 ? 0.1838 0.2413 0.3169 0.0201  -0.0074 0.0271  255  VAL A CA    
762  C  C     . VAL A 145 ? 0.2133 0.2078 0.3131 0.0203  0.0122  0.0220  255  VAL A C     
763  O  O     . VAL A 145 ? 0.2416 0.2189 0.3223 0.0234  0.0120  0.0265  255  VAL A O     
764  C  CB    . VAL A 145 ? 0.2418 0.2411 0.3365 0.0282  0.0070  -0.0300 255  VAL A CB    
765  C  CG1   . VAL A 145 ? 0.2820 0.2697 0.3377 0.0295  -0.0048 -0.0093 255  VAL A CG1   
766  C  CG2   . VAL A 145 ? 0.2668 0.2534 0.3470 0.0285  0.0009  -0.0163 255  VAL A CG2   
767  N  N     . GLY A 146 ? 0.1956 0.2114 0.2854 0.0300  -0.0031 0.0263  256  GLY A N     
768  C  CA    . GLY A 146 ? 0.1869 0.2283 0.2678 -0.0004 -0.0135 0.0332  256  GLY A CA    
769  C  C     . GLY A 146 ? 0.2091 0.1961 0.2626 -0.0098 -0.0049 0.0000  256  GLY A C     
770  O  O     . GLY A 146 ? 0.2331 0.1967 0.2652 0.0104  -0.0225 -0.0117 256  GLY A O     
771  N  N     . ALA A 147 ? 0.2236 0.1721 0.2655 -0.0072 -0.0075 0.0408  257  ALA A N     
772  C  CA    . ALA A 147 ? 0.2271 0.1897 0.2766 0.0207  -0.0343 0.0535  257  ALA A CA    
773  C  C     . ALA A 147 ? 0.2099 0.2144 0.2834 -0.0021 -0.0154 0.0444  257  ALA A C     
774  O  O     . ALA A 147 ? 0.2305 0.2333 0.2706 -0.0003 -0.0132 0.0145  257  ALA A O     
775  C  CB    . ALA A 147 ? 0.2595 0.2047 0.2943 0.0105  -0.0353 0.0908  257  ALA A CB    
776  N  N     . ALA A 148 ? 0.1720 0.2245 0.2927 0.0204  0.0233  0.0265  258  ALA A N     
777  C  CA    . ALA A 148 ? 0.1904 0.1916 0.3009 0.0427  0.0062  0.0070  258  ALA A CA    
778  C  C     . ALA A 148 ? 0.2289 0.1739 0.2944 0.0012  -0.0057 0.0099  258  ALA A C     
779  O  O     . ALA A 148 ? 0.2609 0.1915 0.3024 0.0015  -0.0149 0.0173  258  ALA A O     
780  C  CB    . ALA A 148 ? 0.1929 0.2247 0.3142 0.0447  -0.0035 -0.0156 258  ALA A CB    
781  N  N     . VAL A 149 ? 0.1927 0.1525 0.2821 -0.0048 0.0086  0.0038  259  VAL A N     
782  C  CA    . VAL A 149 ? 0.2029 0.1233 0.2975 0.0064  0.0111  0.0080  259  VAL A CA    
783  C  C     . VAL A 149 ? 0.2291 0.1649 0.3022 -0.0268 -0.0136 0.0048  259  VAL A C     
784  O  O     . VAL A 149 ? 0.2471 0.1838 0.3067 -0.0108 -0.0252 0.0205  259  VAL A O     
785  C  CB    . VAL A 149 ? 0.2060 0.1851 0.2966 0.0216  0.0024  0.0403  259  VAL A CB    
786  C  CG1   . VAL A 149 ? 0.2327 0.1948 0.3129 0.0495  0.0065  0.0145  259  VAL A CG1   
787  C  CG2   . VAL A 149 ? 0.2295 0.2033 0.3171 0.0327  -0.0255 0.0581  259  VAL A CG2   
788  N  N     . GLY A 150 ? 0.1749 0.1718 0.3116 0.0054  -0.0338 0.0177  260  GLY A N     
789  C  CA    . GLY A 150 ? 0.2073 0.1941 0.3138 -0.0050 -0.0015 -0.0171 260  GLY A CA    
790  C  C     . GLY A 150 ? 0.2389 0.2067 0.3310 -0.0046 -0.0123 -0.0079 260  GLY A C     
791  O  O     . GLY A 150 ? 0.2627 0.2063 0.3129 0.0122  0.0128  -0.0065 260  GLY A O     
792  N  N     . VAL A 151 ? 0.2590 0.1733 0.3653 -0.0286 -0.0377 -0.0248 261  VAL A N     
793  C  CA    . VAL A 151 ? 0.2913 0.1738 0.4120 -0.0163 -0.0471 0.0156  261  VAL A CA    
794  C  C     . VAL A 151 ? 0.3193 0.1878 0.4738 -0.0465 -0.0286 0.0243  261  VAL A C     
795  O  O     . VAL A 151 ? 0.3595 0.2441 0.4913 -0.0891 0.0002  0.0574  261  VAL A O     
796  C  CB    . VAL A 151 ? 0.3303 0.2054 0.3944 -0.0170 -0.0803 0.0128  261  VAL A CB    
797  C  CG1   . VAL A 151 ? 0.3528 0.2581 0.4101 -0.0285 -0.0926 0.0459  261  VAL A CG1   
798  C  CG2   . VAL A 151 ? 0.3249 0.2015 0.3822 0.0366  -0.0640 0.0060  261  VAL A CG2   
799  N  N     . GLY A 152 ? 0.3434 0.1922 0.5211 -0.0400 -0.0351 -0.0208 262  GLY A N     
800  C  CA    . GLY A 152 ? 0.3824 0.2745 0.5870 -0.0031 -0.0343 -0.0255 262  GLY A CA    
801  C  C     . GLY A 152 ? 0.4233 0.2957 0.6357 -0.0007 -0.0345 -0.0288 262  GLY A C     
802  O  O     . GLY A 152 ? 0.4177 0.3084 0.6603 0.0336  -0.0520 -0.0673 262  GLY A O     
803  N  N     . GLY A 153 ? 0.4490 0.3140 0.6292 -0.0016 -0.0375 -0.0126 263  GLY A N     
804  C  CA    . GLY A 153 ? 0.4517 0.3115 0.5953 -0.0196 -0.0370 -0.0484 263  GLY A CA    
805  C  C     . GLY A 153 ? 0.4628 0.3160 0.5679 -0.0492 -0.0339 -0.0758 263  GLY A C     
806  O  O     . GLY A 153 ? 0.4298 0.2910 0.5857 -0.0358 -0.0178 -0.0978 263  GLY A O     
807  N  N     . ASP A 154 ? 0.4979 0.3200 0.5438 -0.0945 -0.0407 -0.0560 264  ASP A N     
808  C  CA    . ASP A 154 ? 0.4878 0.3591 0.5224 -0.0716 -0.0212 0.0117  264  ASP A CA    
809  C  C     . ASP A 154 ? 0.3730 0.2949 0.4557 -0.0416 -0.0442 0.0587  264  ASP A C     
810  O  O     . ASP A 154 ? 0.3224 0.3121 0.4191 -0.0270 -0.0415 0.0630  264  ASP A O     
811  C  CB    . ASP A 154 ? 0.6044 0.4134 0.5499 -0.1061 0.0280  -0.0055 264  ASP A CB    
812  C  CG    . ASP A 154 ? 0.7274 0.4788 0.5999 -0.1463 0.0549  -0.0072 264  ASP A CG    
813  O  OD1   . ASP A 154 ? 0.7687 0.5072 0.5919 -0.1900 0.0645  0.0043  264  ASP A OD1   
814  O  OD2   . ASP A 154 ? 0.7683 0.5408 0.6531 -0.1274 0.0508  -0.0128 264  ASP A OD2   
815  N  N     . ALA A 155 ? 0.3121 0.2176 0.4323 -0.0247 -0.0426 0.0579  265  ALA A N     
816  C  CA    . ALA A 155 ? 0.2735 0.1875 0.3887 -0.0237 -0.0397 0.0652  265  ALA A CA    
817  C  C     . ALA A 155 ? 0.2646 0.1888 0.3737 -0.0331 -0.0229 0.0258  265  ALA A C     
818  O  O     . ALA A 155 ? 0.2821 0.2122 0.3636 -0.0199 -0.0286 0.0136  265  ALA A O     
819  C  CB    . ALA A 155 ? 0.2897 0.1766 0.3671 -0.0496 -0.0333 0.0733  265  ALA A CB    
820  N  N     . TRP A 156 ? 0.2985 0.2092 0.3720 -0.0158 -0.0432 0.0034  266  TRP A N     
821  C  CA    . TRP A 156 ? 0.3134 0.1942 0.3691 -0.0024 -0.0490 -0.0188 266  TRP A CA    
822  C  C     . TRP A 156 ? 0.3103 0.1965 0.3560 -0.0186 -0.0458 0.0352  266  TRP A C     
823  O  O     . TRP A 156 ? 0.2774 0.1689 0.3448 -0.0160 -0.0259 0.0225  266  TRP A O     
824  C  CB    . TRP A 156 ? 0.3308 0.2047 0.3721 -0.0140 -0.0496 -0.0162 266  TRP A CB    
825  C  CG    . TRP A 156 ? 0.3788 0.1897 0.3736 -0.0031 -0.0322 -0.0305 266  TRP A CG    
826  C  CD1   . TRP A 156 ? 0.3820 0.2039 0.3877 0.0059  -0.0161 -0.0528 266  TRP A CD1   
827  C  CD2   . TRP A 156 ? 0.4404 0.2011 0.3825 -0.0121 -0.0316 -0.0282 266  TRP A CD2   
828  N  NE1   . TRP A 156 ? 0.4072 0.2036 0.3956 -0.0027 -0.0322 -0.0604 266  TRP A NE1   
829  C  CE2   . TRP A 156 ? 0.4511 0.2296 0.3919 -0.0212 -0.0281 -0.0418 266  TRP A CE2   
830  C  CE3   . TRP A 156 ? 0.4842 0.2147 0.3838 -0.0457 -0.0114 -0.0170 266  TRP A CE3   
831  C  CZ2   . TRP A 156 ? 0.4900 0.2227 0.4068 -0.0451 -0.0151 -0.0369 266  TRP A CZ2   
832  C  CZ3   . TRP A 156 ? 0.5148 0.2247 0.4003 -0.0486 -0.0071 -0.0249 266  TRP A CZ3   
833  C  CH2   . TRP A 156 ? 0.5216 0.2490 0.4097 -0.0415 -0.0128 -0.0329 266  TRP A CH2   
834  N  N     . VAL A 157 ? 0.3332 0.2059 0.3615 -0.0074 -0.0615 0.0215  267  VAL A N     
835  C  CA    . VAL A 157 ? 0.3361 0.2024 0.3507 -0.0060 -0.0448 0.0118  267  VAL A CA    
836  C  C     . VAL A 157 ? 0.3357 0.2141 0.3502 0.0060  -0.0426 -0.0013 267  VAL A C     
837  O  O     . VAL A 157 ? 0.3375 0.2208 0.3675 -0.0065 -0.0453 -0.0026 267  VAL A O     
838  C  CB    . VAL A 157 ? 0.3733 0.2450 0.3520 -0.0381 -0.0649 0.0062  267  VAL A CB    
839  C  CG1   . VAL A 157 ? 0.3929 0.2595 0.3673 -0.0429 -0.0768 0.0000  267  VAL A CG1   
840  C  CG2   . VAL A 157 ? 0.3653 0.2908 0.3531 -0.0617 -0.0679 0.0050  267  VAL A CG2   
841  N  N     . ARG A 158 ? 0.3092 0.1679 0.3389 0.0143  -0.0495 -0.0085 268  ARG A N     
842  C  CA    . ARG A 158 ? 0.3011 0.2151 0.3350 0.0021  -0.0255 -0.0177 268  ARG A CA    
843  C  C     . ARG A 158 ? 0.2788 0.2257 0.3487 -0.0059 -0.0100 -0.0037 268  ARG A C     
844  O  O     . ARG A 158 ? 0.2700 0.1921 0.3731 0.0172  -0.0292 -0.0079 268  ARG A O     
845  C  CB    . ARG A 158 ? 0.2988 0.1964 0.3202 0.0098  -0.0338 -0.0168 268  ARG A CB    
846  C  CG    . ARG A 158 ? 0.2957 0.2061 0.3363 0.0341  -0.0177 -0.0333 268  ARG A CG    
847  C  CD    . ARG A 158 ? 0.2898 0.2507 0.3250 -0.0107 0.0323  -0.0137 268  ARG A CD    
848  N  NE    . ARG A 158 ? 0.3063 0.2287 0.3392 0.0015  0.0085  0.0250  268  ARG A NE    
849  C  CZ    . ARG A 158 ? 0.2987 0.2556 0.3330 -0.0125 0.0191  0.0534  268  ARG A CZ    
850  N  NH1   . ARG A 158 ? 0.3086 0.2559 0.3141 -0.0308 -0.0252 0.0552  268  ARG A NH1   
851  N  NH2   . ARG A 158 ? 0.2893 0.2811 0.3491 0.0079  0.0252  0.0665  268  ARG A NH2   
852  N  N     . ALA A 159 ? 0.2676 0.2359 0.3206 0.0209  0.0189  0.0009  269  ALA A N     
853  C  CA    . ALA A 159 ? 0.2969 0.2194 0.3367 -0.0057 0.0003  0.0068  269  ALA A CA    
854  C  C     . ALA A 159 ? 0.2873 0.1928 0.3780 0.0129  -0.0231 -0.0238 269  ALA A C     
855  O  O     . ALA A 159 ? 0.2979 0.1918 0.4142 0.0370  -0.0286 -0.0289 269  ALA A O     
856  C  CB    . ALA A 159 ? 0.3064 0.2367 0.3404 0.0065  -0.0053 0.0230  269  ALA A CB    
857  N  N     . MET A 160 ? 0.3076 0.1769 0.4087 0.0218  -0.0341 -0.0441 270  MET A N     
858  C  CA    . MET A 160 ? 0.3345 0.1660 0.4503 0.0225  -0.0315 -0.0423 270  MET A CA    
859  C  C     . MET A 160 ? 0.3424 0.1754 0.4737 0.0201  -0.0163 -0.0239 270  MET A C     
860  O  O     . MET A 160 ? 0.3288 0.1729 0.4651 0.0359  0.0341  0.0014  270  MET A O     
861  C  CB    . MET A 160 ? 0.3826 0.1764 0.4396 0.0137  -0.0281 -0.0468 270  MET A CB    
862  C  CG    . MET A 160 ? 0.4447 0.1967 0.4203 0.0203  -0.0121 -0.0458 270  MET A CG    
863  S  SD    . MET A 160 ? 0.4803 0.2172 0.4349 0.0609  0.0080  -0.0350 270  MET A SD    
864  C  CE    . MET A 160 ? 0.5606 0.2126 0.4687 0.0697  0.0501  -0.0431 270  MET A CE    
865  N  N     . MET A 161 ? 0.3341 0.1938 0.4821 -0.0042 -0.0282 -0.0189 271  MET A N     
866  C  CA    . MET A 161 ? 0.3544 0.2349 0.5063 -0.0111 -0.0735 -0.0388 271  MET A CA    
867  C  C     . MET A 161 ? 0.2662 0.2279 0.4738 0.0223  -0.0589 -0.0437 271  MET A C     
868  O  O     . MET A 161 ? 0.2743 0.2525 0.4878 0.0207  -0.0517 -0.0369 271  MET A O     
869  C  CB    . MET A 161 ? 0.4940 0.3223 0.5829 -0.0579 -0.0967 -0.0441 271  MET A CB    
870  C  CG    . MET A 161 ? 0.5917 0.4675 0.6773 -0.0586 -0.0930 -0.0258 271  MET A CG    
871  S  SD    . MET A 161 ? 0.6940 0.6353 0.7557 -0.0709 -0.0790 -0.0267 271  MET A SD    
872  C  CE    . MET A 161 ? 0.7087 0.7426 0.7968 -0.0452 -0.0694 -0.0304 271  MET A CE    
873  N  N     . LEU A 162 ? 0.2314 0.2151 0.4466 0.0185  -0.0472 -0.0239 272  LEU A N     
874  C  CA    . LEU A 162 ? 0.2402 0.2069 0.4172 0.0332  -0.0369 -0.0294 272  LEU A CA    
875  C  C     . LEU A 162 ? 0.2626 0.1987 0.4314 0.0165  -0.0431 -0.0199 272  LEU A C     
876  O  O     . LEU A 162 ? 0.2773 0.2070 0.4083 0.0103  -0.0529 -0.0060 272  LEU A O     
877  C  CB    . LEU A 162 ? 0.2266 0.1830 0.3800 0.0540  -0.0445 -0.0020 272  LEU A CB    
878  C  CG    . LEU A 162 ? 0.2322 0.2110 0.3508 0.0433  -0.0345 -0.0211 272  LEU A CG    
879  C  CD1   . LEU A 162 ? 0.2074 0.1948 0.3309 0.0479  -0.0025 0.0081  272  LEU A CD1   
880  C  CD2   . LEU A 162 ? 0.2655 0.2597 0.3584 0.0588  -0.0295 -0.0484 272  LEU A CD2   
881  N  N     . VAL A 163 ? 0.2866 0.1561 0.4591 0.0274  -0.0103 -0.0382 273  VAL A N     
882  C  CA    . VAL A 163 ? 0.2854 0.2196 0.4834 0.0498  0.0070  -0.0304 273  VAL A CA    
883  C  C     . VAL A 163 ? 0.3035 0.2335 0.4977 0.0458  0.0040  -0.0053 273  VAL A C     
884  O  O     . VAL A 163 ? 0.3025 0.2540 0.4947 0.0718  0.0080  -0.0074 273  VAL A O     
885  C  CB    . VAL A 163 ? 0.3071 0.2709 0.4995 0.0725  0.0324  -0.0259 273  VAL A CB    
886  C  CG1   . VAL A 163 ? 0.3127 0.2958 0.4981 0.0469  0.0555  -0.0207 273  VAL A CG1   
887  C  CG2   . VAL A 163 ? 0.3318 0.2665 0.5104 0.0516  0.0225  -0.0331 273  VAL A CG2   
888  N  N     . ASP A 164 ? 0.2947 0.2177 0.5021 0.0414  -0.0329 0.0216  274  ASP A N     
889  C  CA    . ASP A 164 ? 0.3230 0.2399 0.5333 0.0329  -0.0702 0.0434  274  ASP A CA    
890  C  C     . ASP A 164 ? 0.3217 0.2422 0.5464 0.0713  -0.0823 0.0765  274  ASP A C     
891  O  O     . ASP A 164 ? 0.3281 0.2574 0.5816 0.0773  -0.0815 0.0905  274  ASP A O     
892  C  CB    . ASP A 164 ? 0.3656 0.2652 0.5626 0.0047  -0.1010 0.0153  274  ASP A CB    
893  C  CG    . ASP A 164 ? 0.4510 0.3075 0.6091 -0.0129 -0.0827 0.0079  274  ASP A CG    
894  O  OD1   . ASP A 164 ? 0.4704 0.3240 0.6305 -0.0084 -0.0663 -0.0019 274  ASP A OD1   
895  O  OD2   . ASP A 164 ? 0.5077 0.3445 0.6199 -0.0336 -0.1185 -0.0135 274  ASP A OD2   
896  N  N     . ALA A 165 ? 0.3409 0.1936 0.5231 0.0367  -0.0871 0.0361  275  ALA A N     
897  C  CA    . ALA A 165 ? 0.3308 0.2282 0.5237 0.0646  -0.0760 0.0228  275  ALA A CA    
898  C  C     . ALA A 165 ? 0.3186 0.2216 0.5338 0.0505  -0.0707 0.0151  275  ALA A C     
899  O  O     . ALA A 165 ? 0.3314 0.2394 0.5601 0.0326  -0.0695 0.0096  275  ALA A O     
900  C  CB    . ALA A 165 ? 0.2923 0.2472 0.5371 0.0637  -0.0549 0.0034  275  ALA A CB    
901  N  N     . GLY A 166 ? 0.3117 0.2043 0.5085 0.0539  -0.0413 0.0379  276  GLY A N     
902  C  CA    . GLY A 166 ? 0.3044 0.2405 0.5025 0.0760  -0.0155 0.0456  276  GLY A CA    
903  C  C     . GLY A 166 ? 0.2990 0.2377 0.4874 0.0730  -0.0142 0.0412  276  GLY A C     
904  O  O     . GLY A 166 ? 0.3026 0.2404 0.4813 0.0444  -0.0141 0.0616  276  GLY A O     
905  N  N     . VAL A 167 ? 0.2646 0.2294 0.4673 0.0725  -0.0136 -0.0105 277  VAL A N     
906  C  CA    . VAL A 167 ? 0.2743 0.1822 0.4178 0.0463  -0.0022 -0.0019 277  VAL A CA    
907  C  C     . VAL A 167 ? 0.2723 0.1687 0.4014 0.0425  -0.0056 -0.0062 277  VAL A C     
908  O  O     . VAL A 167 ? 0.2957 0.2327 0.4054 0.0348  -0.0002 0.0198  277  VAL A O     
909  C  CB    . VAL A 167 ? 0.2954 0.1950 0.3903 0.0579  0.0242  -0.0108 277  VAL A CB    
910  C  CG1   . VAL A 167 ? 0.3176 0.2189 0.4066 0.0111  0.0263  -0.0300 277  VAL A CG1   
911  C  CG2   . VAL A 167 ? 0.2983 0.2038 0.3827 0.0596  0.0713  0.0389  277  VAL A CG2   
912  N  N     . ASP A 168 ? 0.2468 0.2002 0.3878 0.0165  -0.0225 0.0135  278  ASP A N     
913  C  CA    . ASP A 168 ? 0.2348 0.2178 0.3986 0.0175  -0.0166 0.0084  278  ASP A CA    
914  C  C     . ASP A 168 ? 0.2337 0.2058 0.3900 0.0316  -0.0091 0.0074  278  ASP A C     
915  O  O     . ASP A 168 ? 0.2425 0.2272 0.3717 0.0488  -0.0064 -0.0055 278  ASP A O     
916  C  CB    . ASP A 168 ? 0.2751 0.2681 0.4112 0.0124  -0.0142 -0.0075 278  ASP A CB    
917  C  CG    . ASP A 168 ? 0.2910 0.2542 0.4538 0.0289  -0.0023 -0.0389 278  ASP A CG    
918  O  OD1   . ASP A 168 ? 0.3093 0.2725 0.5057 0.0411  -0.0174 -0.0361 278  ASP A OD1   
919  O  OD2   . ASP A 168 ? 0.2917 0.2649 0.4330 0.0223  -0.0233 -0.0394 278  ASP A OD2   
920  N  N     . VAL A 169 ? 0.2096 0.1687 0.4007 0.0330  0.0023  -0.0035 279  VAL A N     
921  C  CA    . VAL A 169 ? 0.2345 0.1855 0.3956 0.0088  -0.0070 0.0160  279  VAL A CA    
922  C  C     . VAL A 169 ? 0.2280 0.2015 0.3646 0.0226  -0.0120 0.0005  279  VAL A C     
923  O  O     . VAL A 169 ? 0.2518 0.2358 0.3417 0.0017  0.0030  0.0011  279  VAL A O     
924  C  CB    . VAL A 169 ? 0.2126 0.2036 0.3945 -0.0072 0.0149  0.0287  279  VAL A CB    
925  C  CG1   . VAL A 169 ? 0.2081 0.2175 0.3745 0.0048  0.0153  0.0354  279  VAL A CG1   
926  C  CG2   . VAL A 169 ? 0.2614 0.2273 0.4079 -0.0207 0.0799  0.0316  279  VAL A CG2   
927  N  N     . LEU A 170 ? 0.2270 0.1772 0.3542 0.0330  -0.0081 0.0049  280  LEU A N     
928  C  CA    . LEU A 170 ? 0.2161 0.1534 0.3397 0.0183  0.0089  -0.0235 280  LEU A CA    
929  C  C     . LEU A 170 ? 0.2143 0.1933 0.3153 0.0347  0.0224  -0.0166 280  LEU A C     
930  O  O     . LEU A 170 ? 0.2280 0.2375 0.2809 0.0423  0.0482  -0.0116 280  LEU A O     
931  C  CB    . LEU A 170 ? 0.2185 0.1585 0.3454 0.0269  0.0104  -0.0064 280  LEU A CB    
932  C  CG    . LEU A 170 ? 0.2666 0.1620 0.3444 0.0290  -0.0165 0.0068  280  LEU A CG    
933  C  CD1   . LEU A 170 ? 0.3005 0.1555 0.3628 0.0384  -0.0306 -0.0093 280  LEU A CD1   
934  C  CD2   . LEU A 170 ? 0.2526 0.1997 0.3346 0.0149  0.0040  0.0308  280  LEU A CD2   
935  N  N     . VAL A 171 ? 0.2040 0.1847 0.3172 0.0273  -0.0175 -0.0093 281  VAL A N     
936  C  CA    . VAL A 171 ? 0.1926 0.1710 0.2989 -0.0006 -0.0189 -0.0323 281  VAL A CA    
937  C  C     . VAL A 171 ? 0.2023 0.1688 0.2943 -0.0114 -0.0157 -0.0065 281  VAL A C     
938  O  O     . VAL A 171 ? 0.2336 0.2035 0.2734 0.0074  -0.0112 -0.0118 281  VAL A O     
939  C  CB    . VAL A 171 ? 0.1937 0.1948 0.3082 0.0019  -0.0351 0.0041  281  VAL A CB    
940  C  CG1   . VAL A 171 ? 0.2407 0.1878 0.2959 0.0158  -0.0190 0.0250  281  VAL A CG1   
941  C  CG2   . VAL A 171 ? 0.2044 0.2267 0.2652 -0.0114 -0.0554 -0.0044 281  VAL A CG2   
942  N  N     . VAL A 172 ? 0.1982 0.1688 0.3013 0.0030  -0.0280 -0.0046 282  VAL A N     
943  C  CA    . VAL A 172 ? 0.1918 0.1856 0.3021 0.0021  -0.0200 -0.0267 282  VAL A CA    
944  C  C     . VAL A 172 ? 0.2187 0.1780 0.2931 0.0150  -0.0027 0.0095  282  VAL A C     
945  O  O     . VAL A 172 ? 0.2123 0.1906 0.2985 0.0100  -0.0309 -0.0023 282  VAL A O     
946  C  CB    . VAL A 172 ? 0.1821 0.2114 0.3052 0.0217  -0.0054 -0.0480 282  VAL A CB    
947  C  CG1   . VAL A 172 ? 0.2374 0.2269 0.2862 -0.0137 0.0057  -0.0188 282  VAL A CG1   
948  C  CG2   . VAL A 172 ? 0.1925 0.2303 0.3119 0.0096  -0.0040 -0.0661 282  VAL A CG2   
949  N  N     . ASP A 173 ? 0.2069 0.1608 0.2818 -0.0205 0.0327  0.0055  283  ASP A N     
950  C  CA    . ASP A 173 ? 0.2091 0.1818 0.2362 0.0119  0.0046  0.0176  283  ASP A CA    
951  C  C     . ASP A 173 ? 0.2123 0.1916 0.2557 -0.0152 -0.0070 0.0371  283  ASP A C     
952  O  O     . ASP A 173 ? 0.2384 0.2151 0.2519 -0.0205 -0.0408 0.0498  283  ASP A O     
953  C  CB    . ASP A 173 ? 0.2504 0.2025 0.2228 0.0260  0.0051  0.0008  283  ASP A CB    
954  C  CG    . ASP A 173 ? 0.2502 0.2142 0.2496 -0.0105 0.0148  0.0091  283  ASP A CG    
955  O  OD1   . ASP A 173 ? 0.2470 0.1821 0.2652 -0.0129 -0.0163 0.0153  283  ASP A OD1   
956  O  OD2   . ASP A 173 ? 0.2457 0.2422 0.2678 -0.0128 -0.0024 -0.0244 283  ASP A OD2   
957  N  N     . THR A 174 ? 0.1720 0.1986 0.2402 0.0159  0.0002  -0.0061 284  THR A N     
958  C  CA    . THR A 174 ? 0.2194 0.2193 0.2770 0.0098  0.0059  -0.0114 284  THR A CA    
959  C  C     . THR A 174 ? 0.2049 0.2157 0.2718 0.0203  0.0154  0.0013  284  THR A C     
960  O  O     . THR A 174 ? 0.2205 0.2123 0.2579 0.0273  0.0293  -0.0075 284  THR A O     
961  C  CB    . THR A 174 ? 0.2467 0.1957 0.2980 -0.0031 0.0099  0.0060  284  THR A CB    
962  O  OG1   . THR A 174 ? 0.2280 0.2201 0.3040 -0.0077 -0.0183 -0.0048 284  THR A OG1   
963  C  CG2   . THR A 174 ? 0.2678 0.1948 0.3112 0.0134  -0.0047 -0.0197 284  THR A CG2   
964  N  N     . ALA A 175 ? 0.1944 0.2229 0.2445 0.0328  0.0285  -0.0056 285  ALA A N     
965  C  CA    . ALA A 175 ? 0.1799 0.2210 0.2303 0.0169  0.0320  0.0243  285  ALA A CA    
966  C  C     . ALA A 175 ? 0.2175 0.2174 0.2072 0.0198  -0.0015 0.0236  285  ALA A C     
967  O  O     . ALA A 175 ? 0.2427 0.1862 0.2189 0.0021  0.0102  0.0067  285  ALA A O     
968  C  CB    . ALA A 175 ? 0.2078 0.2506 0.2789 0.0129  0.0364  -0.0041 285  ALA A CB    
969  N  N     . HIS A 176 ? 0.2092 0.2416 0.2069 0.0116  -0.0102 -0.0067 286  HIS A N     
970  C  CA    . HIS A 176 ? 0.1833 0.2389 0.2216 0.0148  -0.0201 -0.0272 286  HIS A CA    
971  C  C     . HIS A 176 ? 0.2139 0.2086 0.2106 -0.0015 -0.0010 -0.0378 286  HIS A C     
972  O  O     . HIS A 176 ? 0.2557 0.2024 0.2103 -0.0007 0.0079  -0.0427 286  HIS A O     
973  C  CB    . HIS A 176 ? 0.1748 0.2173 0.2432 0.0207  -0.0293 -0.0305 286  HIS A CB    
974  C  CG    . HIS A 176 ? 0.1994 0.2364 0.2578 -0.0065 -0.0202 -0.0172 286  HIS A CG    
975  N  ND1   . HIS A 176 ? 0.2111 0.2220 0.2719 0.0044  -0.0151 -0.0069 286  HIS A ND1   
976  C  CD2   . HIS A 176 ? 0.2220 0.2392 0.2723 0.0147  -0.0080 -0.0121 286  HIS A CD2   
977  C  CE1   . HIS A 176 ? 0.1669 0.1997 0.2602 -0.0279 -0.0251 -0.0541 286  HIS A CE1   
978  N  NE2   . HIS A 176 ? 0.2109 0.1944 0.2803 0.0164  -0.0063 -0.0231 286  HIS A NE2   
979  N  N     . ALA A 177 ? 0.1836 0.1998 0.2178 0.0067  -0.0082 -0.0280 287  ALA A N     
980  C  CA    . ALA A 177 ? 0.1419 0.2038 0.2294 -0.0071 -0.0113 -0.0412 287  ALA A CA    
981  C  C     . ALA A 177 ? 0.2155 0.2204 0.2456 0.0222  -0.0056 0.0094  287  ALA A C     
982  O  O     . ALA A 177 ? 0.2284 0.2609 0.2543 -0.0033 0.0071  0.0121  287  ALA A O     
983  C  CB    . ALA A 177 ? 0.1615 0.2215 0.2515 -0.0129 -0.0025 -0.0582 287  ALA A CB    
984  N  N     . HIS A 178 ? 0.2130 0.2302 0.2538 0.0151  -0.0054 0.0406  288  HIS A N     
985  C  CA    . HIS A 178 ? 0.2251 0.1976 0.2481 0.0072  -0.0345 0.0310  288  HIS A CA    
986  C  C     . HIS A 178 ? 0.2796 0.2265 0.3175 -0.0257 -0.0511 0.0498  288  HIS A C     
987  O  O     . HIS A 178 ? 0.3134 0.2248 0.3289 -0.0311 -0.0617 0.0461  288  HIS A O     
988  C  CB    . HIS A 178 ? 0.2556 0.2259 0.1989 0.0127  -0.0228 0.0273  288  HIS A CB    
989  C  CG    . HIS A 178 ? 0.2474 0.2173 0.2131 0.0107  -0.0356 0.0328  288  HIS A CG    
990  N  ND1   . HIS A 178 ? 0.2662 0.2690 0.1798 -0.0102 -0.0315 0.0027  288  HIS A ND1   
991  C  CD2   . HIS A 178 ? 0.2724 0.2548 0.2168 -0.0280 -0.0480 0.0275  288  HIS A CD2   
992  C  CE1   . HIS A 178 ? 0.2713 0.2645 0.2007 -0.0265 -0.0416 0.0182  288  HIS A CE1   
993  N  NE2   . HIS A 178 ? 0.2785 0.2279 0.2258 -0.0208 -0.0388 0.0305  288  HIS A NE2   
994  N  N     . ASN A 179 ? 0.3476 0.3285 0.4084 -0.1306 -0.0533 0.0965  289  ASN A N     
995  C  CA    . ASN A 179 ? 0.4033 0.3685 0.4626 -0.1582 -0.0876 0.1063  289  ASN A CA    
996  C  C     . ASN A 179 ? 0.4132 0.3769 0.4725 -0.1824 -0.1258 0.1359  289  ASN A C     
997  O  O     . ASN A 179 ? 0.3513 0.4034 0.4605 -0.1387 -0.1576 0.1470  289  ASN A O     
998  C  CB    . ASN A 179 ? 0.4341 0.4056 0.4739 -0.1900 -0.0645 0.1350  289  ASN A CB    
999  C  CG    . ASN A 179 ? 0.5205 0.4673 0.4960 -0.1760 -0.0336 0.1235  289  ASN A CG    
1000 O  OD1   . ASN A 179 ? 0.5978 0.4943 0.5283 -0.1509 0.0027  0.1328  289  ASN A OD1   
1001 N  ND2   . ASN A 179 ? 0.4820 0.4923 0.4618 -0.1900 -0.0208 0.1351  289  ASN A ND2   
1002 N  N     . ARG A 180 ? 0.4119 0.3989 0.4696 -0.1900 -0.1319 0.1331  290  ARG A N     
1003 C  CA    . ARG A 180 ? 0.4542 0.4599 0.5002 -0.1900 -0.1306 0.0811  290  ARG A CA    
1004 C  C     . ARG A 180 ? 0.4086 0.4721 0.4480 -0.1900 -0.1366 0.0983  290  ARG A C     
1005 O  O     . ARG A 180 ? 0.4117 0.5012 0.4356 -0.1900 -0.1037 0.1173  290  ARG A O     
1006 C  CB    . ARG A 180 ? 0.5122 0.5354 0.5565 -0.1899 -0.1406 0.0378  290  ARG A CB    
1007 C  CG    . ARG A 180 ? 0.5961 0.6165 0.6092 -0.1669 -0.1494 0.0098  290  ARG A CG    
1008 C  CD    . ARG A 180 ? 0.6717 0.6863 0.6469 -0.1329 -0.1480 0.0101  290  ARG A CD    
1009 N  NE    . ARG A 180 ? 0.7481 0.7532 0.7037 -0.1110 -0.1309 0.0224  290  ARG A NE    
1010 C  CZ    . ARG A 180 ? 0.7989 0.7962 0.7393 -0.1093 -0.1250 0.0414  290  ARG A CZ    
1011 N  NH1   . ARG A 180 ? 0.8236 0.8152 0.7602 -0.1107 -0.1161 0.0576  290  ARG A NH1   
1012 N  NH2   . ARG A 180 ? 0.8136 0.8160 0.7535 -0.1070 -0.1200 0.0390  290  ARG A NH2   
1013 N  N     . LEU A 181 ? 0.3795 0.4749 0.4464 -0.1795 -0.1537 0.0948  291  LEU A N     
1014 C  CA    . LEU A 181 ? 0.3552 0.4103 0.4386 -0.1666 -0.1184 0.1088  291  LEU A CA    
1015 C  C     . LEU A 181 ? 0.3233 0.3533 0.4199 -0.1398 -0.1058 0.1100  291  LEU A C     
1016 O  O     . LEU A 181 ? 0.3535 0.3429 0.4420 -0.1451 -0.1118 0.1264  291  LEU A O     
1017 C  CB    . LEU A 181 ? 0.3399 0.3917 0.4551 -0.1614 -0.1131 0.1043  291  LEU A CB    
1018 C  CG    . LEU A 181 ? 0.3896 0.4197 0.4818 -0.1403 -0.1083 0.0869  291  LEU A CG    
1019 C  CD1   . LEU A 181 ? 0.4111 0.4185 0.4826 -0.1310 -0.1145 0.0849  291  LEU A CD1   
1020 C  CD2   . LEU A 181 ? 0.4086 0.4325 0.4893 -0.1285 -0.0967 0.0694  291  LEU A CD2   
1021 N  N     . VAL A 182 ? 0.2722 0.3084 0.3801 -0.1116 -0.0706 0.1102  292  VAL A N     
1022 C  CA    . VAL A 182 ? 0.2620 0.2657 0.3559 -0.0710 -0.0682 0.0488  292  VAL A CA    
1023 C  C     . VAL A 182 ? 0.3016 0.2662 0.3351 -0.0547 -0.0587 0.0506  292  VAL A C     
1024 O  O     . VAL A 182 ? 0.3009 0.2427 0.3500 -0.0276 -0.0240 0.0388  292  VAL A O     
1025 C  CB    . VAL A 182 ? 0.2540 0.2904 0.3625 -0.0777 -0.0304 0.0015  292  VAL A CB    
1026 C  CG1   . VAL A 182 ? 0.2522 0.2619 0.3571 -0.0580 -0.0439 0.0026  292  VAL A CG1   
1027 C  CG2   . VAL A 182 ? 0.2911 0.3233 0.3636 -0.0562 -0.0447 -0.0127 292  VAL A CG2   
1028 N  N     . LEU A 183 ? 0.3594 0.2919 0.3157 -0.0688 -0.0411 0.0429  293  LEU A N     
1029 C  CA    . LEU A 183 ? 0.3580 0.3045 0.2967 -0.0824 -0.0423 0.0746  293  LEU A CA    
1030 C  C     . LEU A 183 ? 0.3971 0.3089 0.3286 -0.1026 -0.0403 0.0435  293  LEU A C     
1031 O  O     . LEU A 183 ? 0.3910 0.2794 0.3344 -0.0983 -0.0608 0.0045  293  LEU A O     
1032 C  CB    . LEU A 183 ? 0.3402 0.3163 0.2830 -0.0655 -0.0599 0.0860  293  LEU A CB    
1033 C  CG    . LEU A 183 ? 0.3112 0.3298 0.2774 -0.0813 -0.0825 0.0665  293  LEU A CG    
1034 C  CD1   . LEU A 183 ? 0.3271 0.3502 0.2967 -0.0655 -0.0591 0.0684  293  LEU A CD1   
1035 C  CD2   . LEU A 183 ? 0.3106 0.3151 0.2617 -0.0886 -0.0631 0.0250  293  LEU A CD2   
1036 N  N     . ASP A 184 ? 0.4324 0.3325 0.3532 -0.1380 -0.0308 0.0588  294  ASP A N     
1037 C  CA    . ASP A 184 ? 0.4682 0.3459 0.3789 -0.1857 -0.0415 0.0245  294  ASP A CA    
1038 C  C     . ASP A 184 ? 0.4481 0.3022 0.3766 -0.1700 -0.0332 0.0295  294  ASP A C     
1039 O  O     . ASP A 184 ? 0.4933 0.3445 0.3939 -0.1805 -0.0029 0.0459  294  ASP A O     
1040 C  CB    . ASP A 184 ? 0.4991 0.4245 0.3998 -0.1900 -0.0516 -0.0024 294  ASP A CB    
1041 C  CG    . ASP A 184 ? 0.5642 0.5320 0.4446 -0.1900 -0.0390 -0.0314 294  ASP A CG    
1042 O  OD1   . ASP A 184 ? 0.6049 0.5434 0.4279 -0.1900 -0.0455 -0.0356 294  ASP A OD1   
1043 O  OD2   . ASP A 184 ? 0.5950 0.6260 0.4733 -0.1331 -0.0540 -0.0446 294  ASP A OD2   
1044 N  N     . MET A 185 ? 0.4221 0.2528 0.3473 -0.1124 -0.0137 0.0224  295  MET A N     
1045 C  CA    . MET A 185 ? 0.4141 0.2168 0.3494 -0.0724 -0.0128 -0.0010 295  MET A CA    
1046 C  C     . MET A 185 ? 0.4063 0.2049 0.3316 -0.0458 -0.0006 0.0161  295  MET A C     
1047 O  O     . MET A 185 ? 0.4191 0.2043 0.3334 -0.0501 0.0095  0.0271  295  MET A O     
1048 C  CB    . MET A 185 ? 0.4220 0.2142 0.3748 -0.0582 -0.0135 -0.0131 295  MET A CB    
1049 C  CG    . MET A 185 ? 0.4515 0.1698 0.3825 -0.0237 -0.0331 0.0288  295  MET A CG    
1050 S  SD    . MET A 185 ? 0.5349 0.2120 0.4041 -0.0090 -0.0705 -0.0003 295  MET A SD    
1051 C  CE    . MET A 185 ? 0.5390 0.2046 0.3847 0.0171  -0.0792 -0.0017 295  MET A CE    
1052 N  N     . VAL A 186 ? 0.3943 0.1940 0.3379 -0.0623 0.0019  0.0003  296  VAL A N     
1053 C  CA    . VAL A 186 ? 0.3876 0.1927 0.3418 -0.0546 0.0012  -0.0095 296  VAL A CA    
1054 C  C     . VAL A 186 ? 0.4190 0.2044 0.3524 -0.0545 0.0236  -0.0343 296  VAL A C     
1055 O  O     . VAL A 186 ? 0.4420 0.2274 0.3686 -0.0516 0.0254  -0.0356 296  VAL A O     
1056 C  CB    . VAL A 186 ? 0.3469 0.1845 0.3419 -0.0486 -0.0050 -0.0053 296  VAL A CB    
1057 C  CG1   . VAL A 186 ? 0.3377 0.1852 0.3616 -0.0430 -0.0295 0.0187  296  VAL A CG1   
1058 C  CG2   . VAL A 186 ? 0.3262 0.1876 0.3331 -0.0033 -0.0038 0.0082  296  VAL A CG2   
1059 N  N     . GLY A 187 ? 0.4419 0.1901 0.3455 -0.0554 0.0342  -0.0372 297  GLY A N     
1060 C  CA    . GLY A 187 ? 0.4856 0.2239 0.3507 -0.0525 0.0273  -0.0557 297  GLY A CA    
1061 C  C     . GLY A 187 ? 0.5237 0.2385 0.3550 -0.0627 0.0020  -0.0370 297  GLY A C     
1062 O  O     . GLY A 187 ? 0.5459 0.2543 0.3525 -0.0535 -0.0210 -0.0280 297  GLY A O     
1063 N  N     . LYS A 188 ? 0.5392 0.2006 0.3636 -0.0942 -0.0128 -0.0272 298  LYS A N     
1064 C  CA    . LYS A 188 ? 0.5417 0.2203 0.3924 -0.0794 -0.0350 0.0048  298  LYS A CA    
1065 C  C     . LYS A 188 ? 0.5347 0.1990 0.3980 -0.0395 -0.0205 -0.0095 298  LYS A C     
1066 O  O     . LYS A 188 ? 0.5462 0.2015 0.4273 -0.0465 -0.0019 0.0042  298  LYS A O     
1067 C  CB    . LYS A 188 ? 0.5416 0.2552 0.4341 -0.0935 -0.0451 0.0248  298  LYS A CB    
1068 C  CG    . LYS A 188 ? 0.5607 0.3480 0.4778 -0.0791 -0.0458 0.0634  298  LYS A CG    
1069 C  CD    . LYS A 188 ? 0.5894 0.4011 0.5275 -0.0668 -0.0440 0.0942  298  LYS A CD    
1070 C  CE    . LYS A 188 ? 0.5936 0.4222 0.5552 -0.0398 -0.0447 0.1240  298  LYS A CE    
1071 N  NZ    . LYS A 188 ? 0.5972 0.4660 0.5781 -0.0190 -0.0427 0.1259  298  LYS A NZ    
1072 N  N     . LEU A 189 ? 0.5185 0.1910 0.3552 -0.0483 -0.0371 -0.0226 299  LEU A N     
1073 C  CA    . LEU A 189 ? 0.5222 0.2027 0.3450 -0.0173 -0.0229 -0.0284 299  LEU A CA    
1074 C  C     . LEU A 189 ? 0.5326 0.2510 0.3804 -0.0151 -0.0204 -0.0414 299  LEU A C     
1075 O  O     . LEU A 189 ? 0.5632 0.2456 0.3893 -0.0079 0.0097  -0.0609 299  LEU A O     
1076 C  CB    . LEU A 189 ? 0.5316 0.1860 0.3115 0.0278  -0.0383 -0.0180 299  LEU A CB    
1077 C  CG    . LEU A 189 ? 0.5330 0.1490 0.3256 0.0436  -0.0304 -0.0257 299  LEU A CG    
1078 C  CD1   . LEU A 189 ? 0.5085 0.1443 0.3305 0.0544  -0.0026 -0.0388 299  LEU A CD1   
1079 C  CD2   . LEU A 189 ? 0.5347 0.1677 0.3462 0.0457  -0.0411 -0.0137 299  LEU A CD2   
1080 N  N     . LYS A 190 ? 0.5295 0.2924 0.4098 -0.0259 -0.0314 -0.0305 300  LYS A N     
1081 C  CA    . LYS A 190 ? 0.5464 0.3141 0.4309 0.0145  -0.0179 -0.0191 300  LYS A CA    
1082 C  C     . LYS A 190 ? 0.5417 0.3458 0.4262 0.0061  0.0483  -0.0402 300  LYS A C     
1083 O  O     . LYS A 190 ? 0.5225 0.3608 0.4255 -0.0034 0.1015  -0.0509 300  LYS A O     
1084 C  CB    . LYS A 190 ? 0.5840 0.3376 0.4738 0.0446  -0.0406 -0.0162 300  LYS A CB    
1085 C  CG    . LYS A 190 ? 0.6188 0.3354 0.5171 0.1238  -0.0202 -0.0090 300  LYS A CG    
1086 C  CD    . LYS A 190 ? 0.6466 0.3606 0.5685 0.1247  0.0164  -0.0254 300  LYS A CD    
1087 C  CE    . LYS A 190 ? 0.6682 0.3032 0.6056 0.1731  0.0317  -0.0257 300  LYS A CE    
1088 N  NZ    . LYS A 190 ? 0.6390 0.2851 0.6042 0.2092  0.0452  -0.0054 300  LYS A NZ    
1089 N  N     . SER A 191 ? 0.5476 0.3183 0.4104 -0.0124 0.0580  -0.0584 301  SER A N     
1090 C  CA    . SER A 191 ? 0.5835 0.3707 0.4508 -0.0026 0.0665  -0.0299 301  SER A CA    
1091 C  C     . SER A 191 ? 0.5950 0.3553 0.4949 -0.0037 0.1164  -0.0547 301  SER A C     
1092 O  O     . SER A 191 ? 0.6249 0.3867 0.5074 0.0078  0.1530  -0.0398 301  SER A O     
1093 C  CB    . SER A 191 ? 0.6121 0.4085 0.4532 0.0123  0.0704  0.0426  301  SER A CB    
1094 O  OG    . SER A 191 ? 0.6321 0.4782 0.4710 0.0125  0.0952  0.0318  301  SER A OG    
1095 N  N     . GLU A 192 ? 0.5859 0.3453 0.5165 -0.0148 0.1093  -0.0600 302  GLU A N     
1096 C  CA    . GLU A 192 ? 0.5975 0.3525 0.5443 -0.0026 0.0726  -0.0472 302  GLU A CA    
1097 C  C     . GLU A 192 ? 0.5722 0.3175 0.5218 0.0239  0.0784  -0.0596 302  GLU A C     
1098 O  O     . GLU A 192 ? 0.5993 0.2967 0.5261 0.0318  0.0895  -0.0863 302  GLU A O     
1099 C  CB    . GLU A 192 ? 0.6531 0.4200 0.6157 -0.0174 0.0472  -0.0272 302  GLU A CB    
1100 C  CG    . GLU A 192 ? 0.7145 0.4653 0.6645 -0.0168 0.0307  -0.0334 302  GLU A CG    
1101 C  CD    . GLU A 192 ? 0.7555 0.5046 0.7051 -0.0229 0.0048  -0.0420 302  GLU A CD    
1102 O  OE1   . GLU A 192 ? 0.7699 0.5149 0.7272 -0.0141 0.0243  -0.0395 302  GLU A OE1   
1103 O  OE2   . GLU A 192 ? 0.7680 0.5185 0.7126 -0.0445 -0.0296 -0.0444 302  GLU A OE2   
1104 N  N     . VAL A 193 ? 0.5320 0.2867 0.4910 0.0064  0.0707  -0.0604 303  VAL A N     
1105 C  CA    . VAL A 193 ? 0.5065 0.2976 0.5052 0.0127  0.0674  -0.0186 303  VAL A CA    
1106 C  C     . VAL A 193 ? 0.5070 0.3214 0.5298 0.0161  0.0661  -0.0065 303  VAL A C     
1107 O  O     . VAL A 193 ? 0.5392 0.3196 0.5232 0.0636  0.0570  -0.0127 303  VAL A O     
1108 C  CB    . VAL A 193 ? 0.4862 0.3105 0.4954 0.0231  0.0521  0.0052  303  VAL A CB    
1109 C  CG1   . VAL A 193 ? 0.4707 0.3275 0.5111 0.0715  0.0445  0.0056  303  VAL A CG1   
1110 C  CG2   . VAL A 193 ? 0.4989 0.3098 0.4888 0.0258  0.0604  -0.0086 303  VAL A CG2   
1111 N  N     . GLY A 194 ? 0.4967 0.3494 0.5645 0.0140  0.0681  -0.0322 304  GLY A N     
1112 C  CA    . GLY A 194 ? 0.4925 0.3206 0.5918 0.0585  0.1013  -0.0806 304  GLY A CA    
1113 C  C     . GLY A 194 ? 0.5216 0.3787 0.6264 0.0694  0.1186  -0.1018 304  GLY A C     
1114 O  O     . GLY A 194 ? 0.5164 0.3986 0.6233 0.0434  0.1476  -0.1040 304  GLY A O     
1115 N  N     . ASP A 195 ? 0.5414 0.4421 0.6483 0.1134  0.1346  -0.1372 305  ASP A N     
1116 C  CA    . ASP A 195 ? 0.5692 0.5056 0.6849 0.1380  0.1263  -0.1292 305  ASP A CA    
1117 C  C     . ASP A 195 ? 0.5581 0.5129 0.6777 0.1482  0.1077  -0.1318 305  ASP A C     
1118 O  O     . ASP A 195 ? 0.5597 0.5697 0.7052 0.1410  0.0963  -0.1268 305  ASP A O     
1119 C  CB    . ASP A 195 ? 0.6150 0.5535 0.7387 0.1315  0.1415  -0.1051 305  ASP A CB    
1120 C  CG    . ASP A 195 ? 0.6604 0.6304 0.7872 0.1348  0.1462  -0.0959 305  ASP A CG    
1121 O  OD1   . ASP A 195 ? 0.6817 0.6756 0.7961 0.1366  0.1680  -0.1146 305  ASP A OD1   
1122 O  OD2   . ASP A 195 ? 0.6762 0.6783 0.8083 0.1254  0.1363  -0.0757 305  ASP A OD2   
1123 N  N     . ARG A 196 ? 0.5421 0.4496 0.6318 0.1834  0.0832  -0.1316 306  ARG A N     
1124 C  CA    . ARG A 196 ? 0.5150 0.4282 0.6058 0.1697  0.0302  -0.0914 306  ARG A CA    
1125 C  C     . ARG A 196 ? 0.4399 0.3688 0.5383 0.1293  0.0087  -0.0783 306  ARG A C     
1126 O  O     . ARG A 196 ? 0.4490 0.4232 0.5767 0.1239  -0.0237 -0.1039 306  ARG A O     
1127 C  CB    . ARG A 196 ? 0.5569 0.4631 0.6368 0.2051  0.0269  -0.0814 306  ARG A CB    
1128 C  CG    . ARG A 196 ? 0.6114 0.5472 0.6736 0.1985  0.0151  -0.0342 306  ARG A CG    
1129 C  CD    . ARG A 196 ? 0.6424 0.5780 0.6985 0.2276  0.0170  -0.0005 306  ARG A CD    
1130 N  NE    . ARG A 196 ? 0.6932 0.6304 0.7274 0.2004  0.0356  0.0083  306  ARG A NE    
1131 C  CZ    . ARG A 196 ? 0.7327 0.6712 0.7439 0.1626  0.0399  0.0003  306  ARG A CZ    
1132 N  NH1   . ARG A 196 ? 0.7313 0.6700 0.7566 0.1516  0.0459  -0.0306 306  ARG A NH1   
1133 N  NH2   . ARG A 196 ? 0.7507 0.6925 0.7499 0.1446  0.0304  0.0232  306  ARG A NH2   
1134 N  N     A VAL A 197 ? 0.3962 0.3136 0.4882 0.1036  0.0105  -0.0264 307  VAL A N     
1135 N  N     B VAL A 197 ? 0.3808 0.3063 0.4846 0.1135  0.0255  -0.0399 307  VAL A N     
1136 C  CA    A VAL A 197 ? 0.3629 0.2517 0.4372 0.0758  0.0297  0.0016  307  VAL A CA    
1137 C  CA    B VAL A 197 ? 0.3361 0.2442 0.4341 0.0987  0.0601  -0.0232 307  VAL A CA    
1138 C  C     A VAL A 197 ? 0.3256 0.2238 0.4140 0.0522  0.0494  -0.0058 307  VAL A C     
1139 C  C     B VAL A 197 ? 0.3111 0.2264 0.4163 0.0738  0.0543  -0.0298 307  VAL A C     
1140 O  O     A VAL A 197 ? 0.3261 0.2291 0.4217 0.0306  0.0563  -0.0045 307  VAL A O     
1141 O  O     B VAL A 197 ? 0.3115 0.2399 0.4321 0.0688  0.0449  -0.0434 307  VAL A O     
1142 C  CB    A VAL A 197 ? 0.3892 0.2411 0.4223 0.0445  0.0058  0.0332  307  VAL A CB    
1143 C  CB    B VAL A 197 ? 0.3412 0.2221 0.4191 0.0721  0.0699  0.0010  307  VAL A CB    
1144 C  CG1   A VAL A 197 ? 0.4023 0.2694 0.4243 -0.0017 0.0010  0.0483  307  VAL A CG1   
1145 C  CG1   B VAL A 197 ? 0.3081 0.1812 0.4016 0.0669  0.1340  -0.0007 307  VAL A CG1   
1146 C  CG2   A VAL A 197 ? 0.3965 0.2238 0.4086 0.0406  0.0187  0.0331  307  VAL A CG2   
1147 C  CG2   B VAL A 197 ? 0.3706 0.2528 0.4213 0.0421  0.0565  -0.0122 307  VAL A CG2   
1148 N  N     . GLU A 198 ? 0.2857 0.1888 0.3980 0.0461  0.0477  -0.0238 308  GLU A N     
1149 C  CA    . GLU A 198 ? 0.2524 0.1970 0.3802 0.0139  0.0433  -0.0092 308  GLU A CA    
1150 C  C     . GLU A 198 ? 0.2513 0.2246 0.3655 0.0358  0.0147  -0.0137 308  GLU A C     
1151 O  O     . GLU A 198 ? 0.2568 0.2738 0.3302 0.0198  -0.0107 -0.0167 308  GLU A O     
1152 C  CB    . GLU A 198 ? 0.2447 0.2243 0.3884 0.0349  0.0607  0.0127  308  GLU A CB    
1153 C  CG    . GLU A 198 ? 0.2478 0.2321 0.4051 0.0290  0.0762  -0.0158 308  GLU A CG    
1154 C  CD    . GLU A 198 ? 0.2710 0.2185 0.4206 -0.0045 0.0717  -0.0469 308  GLU A CD    
1155 O  OE1   . GLU A 198 ? 0.2622 0.2070 0.4156 -0.0297 0.0666  -0.0457 308  GLU A OE1   
1156 O  OE2   . GLU A 198 ? 0.2977 0.2531 0.4524 0.0062  0.0706  -0.0675 308  GLU A OE2   
1157 N  N     . VAL A 199 ? 0.2433 0.2093 0.3718 0.0380  0.0163  -0.0038 309  VAL A N     
1158 C  CA    . VAL A 199 ? 0.2521 0.2168 0.3599 0.0401  0.0183  -0.0209 309  VAL A CA    
1159 C  C     . VAL A 199 ? 0.2342 0.2258 0.3433 0.0386  0.0316  -0.0070 309  VAL A C     
1160 O  O     . VAL A 199 ? 0.2455 0.2441 0.3407 0.0328  0.0436  0.0110  309  VAL A O     
1161 C  CB    . VAL A 199 ? 0.2403 0.2170 0.3710 0.0604  -0.0089 -0.0144 309  VAL A CB    
1162 C  CG1   . VAL A 199 ? 0.2577 0.2472 0.3610 0.0125  -0.0618 -0.0321 309  VAL A CG1   
1163 C  CG2   . VAL A 199 ? 0.3119 0.2440 0.3777 0.0423  -0.0174 0.0043  309  VAL A CG2   
1164 N  N     . VAL A 200 ? 0.2090 0.1943 0.3224 0.0224  0.0264  -0.0092 310  VAL A N     
1165 C  CA    . VAL A 200 ? 0.2216 0.2102 0.3241 0.0078  0.0321  -0.0010 310  VAL A CA    
1166 C  C     . VAL A 200 ? 0.2305 0.2032 0.3038 0.0200  0.0205  -0.0334 310  VAL A C     
1167 O  O     . VAL A 200 ? 0.2592 0.1982 0.3025 0.0035  0.0319  0.0076  310  VAL A O     
1168 C  CB    . VAL A 200 ? 0.1833 0.1996 0.3152 0.0264  0.0085  0.0083  310  VAL A CB    
1169 C  CG1   . VAL A 200 ? 0.2191 0.2188 0.3225 0.0403  0.0175  0.0275  310  VAL A CG1   
1170 C  CG2   . VAL A 200 ? 0.1825 0.2533 0.3503 -0.0073 -0.0331 -0.0011 310  VAL A CG2   
1171 N  N     . GLY A 201 ? 0.2163 0.2085 0.2800 0.0344  0.0046  -0.0137 311  GLY A N     
1172 C  CA    . GLY A 201 ? 0.1781 0.2093 0.2884 0.0166  0.0011  -0.0230 311  GLY A CA    
1173 C  C     . GLY A 201 ? 0.1896 0.2166 0.2928 0.0130  0.0234  -0.0468 311  GLY A C     
1174 O  O     . GLY A 201 ? 0.2103 0.2058 0.3128 -0.0163 0.0208  -0.0305 311  GLY A O     
1175 N  N     . GLY A 202 ? 0.1855 0.1872 0.2968 0.0130  0.0023  -0.0361 312  GLY A N     
1176 C  CA    . GLY A 202 ? 0.1756 0.1617 0.2660 0.0362  0.0259  0.0101  312  GLY A CA    
1177 C  C     . GLY A 202 ? 0.1886 0.1462 0.2354 0.0001  -0.0106 0.0050  312  GLY A C     
1178 O  O     . GLY A 202 ? 0.2269 0.1373 0.2352 -0.0004 0.0031  0.0073  312  GLY A O     
1179 N  N     . ASN A 203 ? 0.2230 0.1432 0.2148 -0.0270 -0.0324 -0.0064 313  ASN A N     
1180 C  CA    . ASN A 203 ? 0.2288 0.1283 0.1798 -0.0186 -0.0184 -0.0035 313  ASN A CA    
1181 C  C     . ASN A 203 ? 0.2110 0.1801 0.2183 -0.0071 -0.0356 0.0078  313  ASN A C     
1182 O  O     . ASN A 203 ? 0.2111 0.1763 0.2316 -0.0162 -0.0205 0.0061  313  ASN A O     
1183 C  CB    . ASN A 203 ? 0.2002 0.1807 0.1824 0.0121  -0.0228 0.0025  313  ASN A CB    
1184 C  CG    . ASN A 203 ? 0.2317 0.2055 0.1508 -0.0019 -0.0077 -0.0103 313  ASN A CG    
1185 O  OD1   . ASN A 203 ? 0.1907 0.2162 0.1828 -0.0150 -0.0127 -0.0139 313  ASN A OD1   
1186 N  ND2   . ASN A 203 ? 0.2372 0.1893 0.1507 0.0203  0.0082  -0.0063 313  ASN A ND2   
1187 N  N     . VAL A 204 ? 0.2056 0.1876 0.1940 -0.0172 -0.0344 0.0129  314  VAL A N     
1188 C  CA    . VAL A 204 ? 0.2073 0.1835 0.2031 0.0123  -0.0244 -0.0114 314  VAL A CA    
1189 C  C     . VAL A 204 ? 0.2154 0.1951 0.2239 -0.0024 -0.0086 -0.0028 314  VAL A C     
1190 O  O     . VAL A 204 ? 0.2590 0.1802 0.2143 -0.0453 -0.0084 -0.0156 314  VAL A O     
1191 C  CB    . VAL A 204 ? 0.1927 0.1673 0.2231 -0.0113 0.0132  -0.0196 314  VAL A CB    
1192 C  CG1   . VAL A 204 ? 0.2441 0.1642 0.2409 0.0315  -0.0084 -0.0320 314  VAL A CG1   
1193 C  CG2   . VAL A 204 ? 0.2038 0.2022 0.2563 -0.0202 -0.0313 -0.0027 314  VAL A CG2   
1194 N  N     . ALA A 205 ? 0.2374 0.1379 0.2475 0.0434  -0.0035 0.0111  315  ALA A N     
1195 C  CA    . ALA A 205 ? 0.2463 0.1518 0.2444 0.0453  0.0117  0.0116  315  ALA A CA    
1196 C  C     . ALA A 205 ? 0.2295 0.1754 0.2436 0.0193  -0.0130 0.0111  315  ALA A C     
1197 O  O     . ALA A 205 ? 0.2622 0.1897 0.2443 0.0157  -0.0205 -0.0004 315  ALA A O     
1198 C  CB    . ALA A 205 ? 0.2917 0.1963 0.2698 0.0486  0.0271  0.0135  315  ALA A CB    
1199 N  N     . THR A 206 ? 0.1716 0.2313 0.2212 0.0129  0.0213  0.0041  316  THR A N     
1200 C  CA    . THR A 206 ? 0.2052 0.2533 0.2386 0.0056  0.0044  0.0149  316  THR A CA    
1201 C  C     . THR A 206 ? 0.2255 0.2427 0.2115 0.0117  -0.0125 0.0246  316  THR A C     
1202 O  O     . THR A 206 ? 0.2098 0.2191 0.2076 -0.0275 -0.0166 -0.0010 316  THR A O     
1203 C  CB    . THR A 206 ? 0.2118 0.2180 0.2441 -0.0192 0.0272  -0.0254 316  THR A CB    
1204 O  OG1   . THR A 206 ? 0.2571 0.1796 0.2469 -0.0154 -0.0023 -0.0154 316  THR A OG1   
1205 C  CG2   . THR A 206 ? 0.2009 0.2387 0.2688 0.0328  0.0074  -0.0286 316  THR A CG2   
1206 N  N     . ARG A 207 ? 0.2194 0.2385 0.1801 -0.0300 -0.0128 0.0169  317  ARG A N     
1207 C  CA    . ARG A 207 ? 0.2364 0.2196 0.1876 -0.0236 0.0023  -0.0048 317  ARG A CA    
1208 C  C     . ARG A 207 ? 0.2212 0.2524 0.2127 -0.0482 0.0009  -0.0041 317  ARG A C     
1209 O  O     . ARG A 207 ? 0.2369 0.2569 0.2091 -0.0461 0.0197  -0.0207 317  ARG A O     
1210 C  CB    . ARG A 207 ? 0.2973 0.2493 0.1952 -0.0375 0.0268  -0.0095 317  ARG A CB    
1211 C  CG    . ARG A 207 ? 0.3230 0.2302 0.1975 -0.0481 0.0021  -0.0083 317  ARG A CG    
1212 C  CD    . ARG A 207 ? 0.3336 0.2098 0.1984 -0.0525 -0.0075 -0.0289 317  ARG A CD    
1213 N  NE    . ARG A 207 ? 0.3251 0.2229 0.1929 -0.0468 -0.0316 0.0068  317  ARG A NE    
1214 C  CZ    . ARG A 207 ? 0.3370 0.2606 0.1712 0.0069  -0.0281 -0.0033 317  ARG A CZ    
1215 N  NH1   . ARG A 207 ? 0.3689 0.3093 0.1653 0.0021  -0.0467 -0.0068 317  ARG A NH1   
1216 N  NH2   . ARG A 207 ? 0.2987 0.2627 0.1922 -0.0043 -0.0536 0.0244  317  ARG A NH2   
1217 N  N     A SER A 208 ? 0.2243 0.2675 0.2348 -0.0579 -0.0140 -0.0033 318  SER A N     
1218 N  N     B SER A 208 ? 0.2362 0.2631 0.2192 -0.0483 -0.0009 -0.0017 318  SER A N     
1219 C  CA    A SER A 208 ? 0.2178 0.2647 0.2702 -0.0635 -0.0380 0.0008  318  SER A CA    
1220 C  CA    B SER A 208 ? 0.2429 0.2631 0.2345 -0.0470 -0.0145 0.0001  318  SER A CA    
1221 C  C     A SER A 208 ? 0.2297 0.2338 0.2725 -0.0541 -0.0103 -0.0116 318  SER A C     
1222 C  C     B SER A 208 ? 0.2355 0.2423 0.2434 -0.0337 -0.0049 -0.0125 318  SER A C     
1223 O  O     A SER A 208 ? 0.2180 0.2274 0.2987 -0.0782 -0.0067 -0.0144 318  SER A O     
1224 O  O     B SER A 208 ? 0.2232 0.2445 0.2539 -0.0251 -0.0044 -0.0102 318  SER A O     
1225 C  CB    A SER A 208 ? 0.2248 0.2710 0.2797 -0.0841 -0.0480 0.0074  318  SER A CB    
1226 C  CB    B SER A 208 ? 0.2652 0.2669 0.2281 -0.0669 -0.0237 0.0092  318  SER A CB    
1227 O  OG    A SER A 208 ? 0.2360 0.2821 0.2952 -0.0736 -0.0540 0.0416  318  SER A OG    
1228 O  OG    B SER A 208 ? 0.2910 0.2760 0.2271 -0.0687 -0.0387 0.0249  318  SER A OG    
1229 N  N     . ALA A 209 ? 0.2113 0.2226 0.2380 -0.0378 -0.0081 -0.0296 319  ALA A N     
1230 C  CA    . ALA A 209 ? 0.2103 0.2001 0.2310 -0.0137 0.0236  -0.0263 319  ALA A CA    
1231 C  C     . ALA A 209 ? 0.2257 0.1857 0.2345 -0.0068 0.0176  -0.0292 319  ALA A C     
1232 O  O     . ALA A 209 ? 0.2359 0.2032 0.2040 -0.0087 0.0047  -0.0486 319  ALA A O     
1233 C  CB    . ALA A 209 ? 0.2179 0.2089 0.2332 -0.0041 0.0237  -0.0083 319  ALA A CB    
1234 N  N     . ALA A 210 ? 0.2275 0.1698 0.2254 -0.0467 0.0265  -0.0215 320  ALA A N     
1235 C  CA    . ALA A 210 ? 0.1928 0.1924 0.2586 -0.0442 0.0348  -0.0413 320  ALA A CA    
1236 C  C     . ALA A 210 ? 0.2242 0.2409 0.2473 -0.0079 0.0375  -0.0433 320  ALA A C     
1237 O  O     . ALA A 210 ? 0.2339 0.2319 0.2564 -0.0126 0.0542  -0.0360 320  ALA A O     
1238 C  CB    . ALA A 210 ? 0.1862 0.2025 0.2510 -0.0357 0.0213  -0.0360 320  ALA A CB    
1239 N  N     . ALA A 211 ? 0.2473 0.2613 0.2399 -0.0333 0.0332  -0.0339 321  ALA A N     
1240 C  CA    . ALA A 211 ? 0.2656 0.2342 0.2426 -0.0362 -0.0019 -0.0058 321  ALA A CA    
1241 C  C     . ALA A 211 ? 0.2766 0.2382 0.2579 -0.0402 -0.0010 -0.0266 321  ALA A C     
1242 O  O     . ALA A 211 ? 0.2644 0.2336 0.2525 -0.0275 -0.0003 -0.0357 321  ALA A O     
1243 C  CB    . ALA A 211 ? 0.2752 0.2412 0.2211 -0.0152 -0.0021 0.0190  321  ALA A CB    
1244 N  N     . ALA A 212 ? 0.2617 0.2142 0.2142 -0.0615 -0.0077 -0.0173 322  ALA A N     
1245 C  CA    . ALA A 212 ? 0.2566 0.2345 0.2380 -0.0461 -0.0236 -0.0179 322  ALA A CA    
1246 C  C     . ALA A 212 ? 0.2792 0.2236 0.2589 -0.0235 -0.0021 -0.0407 322  ALA A C     
1247 O  O     . ALA A 212 ? 0.2879 0.2348 0.2807 -0.0272 -0.0047 -0.0506 322  ALA A O     
1248 C  CB    . ALA A 212 ? 0.2406 0.2257 0.2418 -0.0524 -0.0413 -0.0198 322  ALA A CB    
1249 N  N     . LEU A 213 ? 0.2589 0.2045 0.2455 -0.0313 -0.0209 -0.0523 323  LEU A N     
1250 C  CA    . LEU A 213 ? 0.2722 0.2171 0.2520 -0.0083 -0.0156 -0.0493 323  LEU A CA    
1251 C  C     . LEU A 213 ? 0.2817 0.2354 0.2643 -0.0105 0.0147  -0.0526 323  LEU A C     
1252 O  O     . LEU A 213 ? 0.2718 0.1917 0.2867 -0.0276 0.0017  -0.0143 323  LEU A O     
1253 C  CB    . LEU A 213 ? 0.2660 0.2020 0.2026 -0.0133 -0.0100 -0.0172 323  LEU A CB    
1254 C  CG    . LEU A 213 ? 0.2715 0.1959 0.2303 -0.0031 -0.0147 -0.0183 323  LEU A CG    
1255 C  CD1   . LEU A 213 ? 0.2446 0.2216 0.2189 0.0020  -0.0060 -0.0259 323  LEU A CD1   
1256 C  CD2   . LEU A 213 ? 0.2868 0.2006 0.2532 -0.0174 -0.0035 -0.0161 323  LEU A CD2   
1257 N  N     . VAL A 214 ? 0.2706 0.2357 0.2712 -0.0246 0.0230  -0.0742 324  VAL A N     
1258 C  CA    . VAL A 214 ? 0.2601 0.2353 0.2725 -0.0137 0.0183  -0.0678 324  VAL A CA    
1259 C  C     . VAL A 214 ? 0.2809 0.2270 0.2985 0.0223  0.0060  -0.0626 324  VAL A C     
1260 O  O     . VAL A 214 ? 0.3027 0.2254 0.3174 0.0224  0.0317  -0.0600 324  VAL A O     
1261 C  CB    . VAL A 214 ? 0.2653 0.2469 0.2363 -0.0219 0.0376  -0.0452 324  VAL A CB    
1262 C  CG1   . VAL A 214 ? 0.2815 0.2907 0.2421 -0.0245 0.0375  -0.0179 324  VAL A CG1   
1263 C  CG2   . VAL A 214 ? 0.2590 0.2743 0.2384 -0.0010 -0.0145 -0.0227 324  VAL A CG2   
1264 N  N     . ASP A 215 ? 0.2915 0.2233 0.3083 -0.0199 -0.0126 -0.0633 325  ASP A N     
1265 C  CA    . ASP A 215 ? 0.3339 0.2768 0.3300 -0.0063 -0.0010 -0.0679 325  ASP A CA    
1266 C  C     . ASP A 215 ? 0.3572 0.2777 0.3159 -0.0104 0.0379  -0.0744 325  ASP A C     
1267 O  O     . ASP A 215 ? 0.3606 0.2939 0.3261 -0.0226 0.0354  -0.0745 325  ASP A O     
1268 C  CB    . ASP A 215 ? 0.3684 0.3065 0.3684 -0.0156 -0.0365 -0.0380 325  ASP A CB    
1269 C  CG    . ASP A 215 ? 0.4269 0.3993 0.4609 0.0018  -0.0539 -0.0218 325  ASP A CG    
1270 O  OD1   . ASP A 215 ? 0.4723 0.4355 0.4777 0.0330  -0.0442 -0.0368 325  ASP A OD1   
1271 O  OD2   . ASP A 215 ? 0.4844 0.4579 0.5088 -0.0144 -0.0650 -0.0017 325  ASP A OD2   
1272 N  N     . ALA A 216 ? 0.3772 0.2727 0.3231 -0.0068 0.0351  -0.0450 326  ALA A N     
1273 C  CA    . ALA A 216 ? 0.3714 0.2378 0.3065 -0.0241 0.0108  -0.0400 326  ALA A CA    
1274 C  C     . ALA A 216 ? 0.3743 0.2238 0.3237 -0.0072 0.0058  -0.0370 326  ALA A C     
1275 O  O     . ALA A 216 ? 0.3864 0.2461 0.3350 -0.0249 0.0028  -0.0193 326  ALA A O     
1276 C  CB    . ALA A 216 ? 0.3554 0.2535 0.2807 -0.0497 -0.0139 -0.0339 326  ALA A CB    
1277 N  N     . GLY A 217 ? 0.3476 0.2139 0.2829 -0.0173 -0.0183 -0.0868 327  GLY A N     
1278 C  CA    . GLY A 217 ? 0.3439 0.1995 0.2929 0.0328  -0.0034 -0.0632 327  GLY A CA    
1279 C  C     . GLY A 217 ? 0.3381 0.1954 0.2960 0.0335  0.0086  -0.0574 327  GLY A C     
1280 O  O     . GLY A 217 ? 0.3509 0.2312 0.3190 -0.0115 0.0182  -0.0725 327  GLY A O     
1281 N  N     . ALA A 218 ? 0.3045 0.1823 0.2629 0.0207  0.0300  -0.0367 328  ALA A N     
1282 C  CA    . ALA A 218 ? 0.2562 0.1979 0.2702 0.0005  0.0218  -0.0652 328  ALA A CA    
1283 C  C     . ALA A 218 ? 0.2410 0.2390 0.2793 -0.0131 0.0106  -0.0430 328  ALA A C     
1284 O  O     . ALA A 218 ? 0.2743 0.2837 0.2873 -0.0001 0.0103  -0.0528 328  ALA A O     
1285 C  CB    . ALA A 218 ? 0.2539 0.1706 0.2901 0.0246  0.0410  -0.0438 328  ALA A CB    
1286 N  N     . ASP A 219 ? 0.1997 0.2058 0.2747 -0.0057 -0.0042 -0.0321 329  ASP A N     
1287 C  CA    . ASP A 219 ? 0.2211 0.2144 0.2823 0.0262  0.0059  -0.0359 329  ASP A CA    
1288 C  C     . ASP A 219 ? 0.2326 0.2259 0.2577 -0.0274 0.0387  -0.0389 329  ASP A C     
1289 O  O     . ASP A 219 ? 0.2426 0.2536 0.2397 -0.0164 0.0771  -0.0245 329  ASP A O     
1290 C  CB    . ASP A 219 ? 0.2652 0.2054 0.3288 0.0295  -0.0013 -0.0383 329  ASP A CB    
1291 C  CG    . ASP A 219 ? 0.2959 0.2033 0.3484 0.0153  0.0277  -0.0213 329  ASP A CG    
1292 O  OD1   . ASP A 219 ? 0.3044 0.2089 0.3359 -0.0092 0.0472  -0.0278 329  ASP A OD1   
1293 O  OD2   . ASP A 219 ? 0.3228 0.1897 0.3880 0.0316  0.0495  -0.0274 329  ASP A OD2   
1294 N  N     . ALA A 220 ? 0.2497 0.2123 0.2336 -0.0110 0.0333  -0.0556 330  ALA A N     
1295 C  CA    . ALA A 220 ? 0.2251 0.1804 0.2632 -0.0223 0.0040  -0.0335 330  ALA A CA    
1296 C  C     . ALA A 220 ? 0.1756 0.2146 0.2513 -0.0122 -0.0070 -0.0242 330  ALA A C     
1297 O  O     . ALA A 220 ? 0.2333 0.2612 0.2413 0.0224  0.0115  -0.0519 330  ALA A O     
1298 C  CB    . ALA A 220 ? 0.2120 0.1576 0.2719 0.0064  -0.0136 -0.0222 330  ALA A CB    
1299 N  N     . VAL A 221 ? 0.1772 0.1996 0.2589 0.0112  0.0096  -0.0247 331  VAL A N     
1300 C  CA    . VAL A 221 ? 0.1979 0.2204 0.2296 -0.0213 0.0179  0.0058  331  VAL A CA    
1301 C  C     . VAL A 221 ? 0.1938 0.2164 0.2184 -0.0279 0.0296  0.0020  331  VAL A C     
1302 O  O     . VAL A 221 ? 0.2144 0.2253 0.2410 -0.0529 -0.0139 -0.0151 331  VAL A O     
1303 C  CB    . VAL A 221 ? 0.1943 0.1885 0.2030 0.0122  0.0168  -0.0280 331  VAL A CB    
1304 C  CG1   . VAL A 221 ? 0.1978 0.2201 0.2069 -0.0058 0.0037  -0.0156 331  VAL A CG1   
1305 C  CG2   . VAL A 221 ? 0.2209 0.2137 0.2182 -0.0047 0.0021  -0.0471 331  VAL A CG2   
1306 N  N     . LYS A 222 ? 0.2004 0.2183 0.1994 -0.0106 0.0003  0.0010  332  LYS A N     
1307 C  CA    . LYS A 222 ? 0.2097 0.1980 0.1829 0.0154  0.0022  -0.0060 332  LYS A CA    
1308 C  C     . LYS A 222 ? 0.2034 0.1726 0.2019 -0.0121 0.0096  0.0112  332  LYS A C     
1309 O  O     . LYS A 222 ? 0.2098 0.2022 0.2163 -0.0171 0.0059  0.0017  332  LYS A O     
1310 C  CB    . LYS A 222 ? 0.2104 0.1935 0.1796 0.0291  -0.0126 0.0122  332  LYS A CB    
1311 C  CG    . LYS A 222 ? 0.2020 0.2094 0.1644 0.0066  -0.0407 -0.0011 332  LYS A CG    
1312 C  CD    . LYS A 222 ? 0.2157 0.1838 0.2026 -0.0105 0.0206  0.0145  332  LYS A CD    
1313 C  CE    . LYS A 222 ? 0.2264 0.1669 0.1983 0.0019  0.0493  0.0094  332  LYS A CE    
1314 N  NZ    . LYS A 222 ? 0.2118 0.1628 0.1932 0.0069  0.0123  -0.0306 332  LYS A NZ    
1315 N  N     . VAL A 223 ? 0.2007 0.1335 0.1830 0.0016  0.0130  0.0227  333  VAL A N     
1316 C  CA    . VAL A 223 ? 0.2071 0.2003 0.1906 0.0076  -0.0182 0.0249  333  VAL A CA    
1317 C  C     . VAL A 223 ? 0.1701 0.2385 0.1639 0.0186  0.0096  0.0122  333  VAL A C     
1318 O  O     . VAL A 223 ? 0.2037 0.2257 0.1975 -0.0053 0.0074  -0.0032 333  VAL A O     
1319 C  CB    . VAL A 223 ? 0.2337 0.1639 0.1874 0.0051  -0.0054 0.0282  333  VAL A CB    
1320 C  CG1   . VAL A 223 ? 0.2329 0.1790 0.1958 0.0264  0.0106  0.0730  333  VAL A CG1   
1321 C  CG2   . VAL A 223 ? 0.2256 0.2179 0.1751 -0.0144 0.0195  0.0386  333  VAL A CG2   
1322 N  N     . GLY A 224 ? 0.1593 0.2310 0.1357 0.0210  0.0492  0.0165  334  GLY A N     
1323 C  CA    . GLY A 224 ? 0.1632 0.2369 0.1913 -0.0004 0.0209  0.0242  334  GLY A CA    
1324 C  C     . GLY A 224 ? 0.1495 0.2130 0.2328 0.0080  -0.0005 0.0204  334  GLY A C     
1325 O  O     . GLY A 224 ? 0.1858 0.1840 0.2541 0.0083  -0.0224 0.0335  334  GLY A O     
1326 N  N     . VAL A 225 ? 0.1604 0.2130 0.2350 -0.0068 0.0054  0.0098  335  VAL A N     
1327 C  CA    . VAL A 225 ? 0.1621 0.2265 0.2617 0.0022  -0.0083 -0.0092 335  VAL A CA    
1328 C  C     . VAL A 225 ? 0.1906 0.2619 0.2862 0.0260  -0.0225 -0.0382 335  VAL A C     
1329 O  O     . VAL A 225 ? 0.1967 0.2611 0.3085 0.0206  -0.0647 -0.0160 335  VAL A O     
1330 C  CB    . VAL A 225 ? 0.1577 0.2133 0.2701 -0.0103 0.0293  0.0181  335  VAL A CB    
1331 C  CG1   . VAL A 225 ? 0.1737 0.2417 0.2558 -0.0146 0.0048  0.0211  335  VAL A CG1   
1332 C  CG2   . VAL A 225 ? 0.2115 0.1958 0.2637 0.0183  0.0350  0.0402  335  VAL A CG2   
1333 N  N     . GLY A 226 ? 0.1996 0.2876 0.2735 0.0203  0.0183  -0.0435 336  GLY A N     
1334 C  CA    . GLY A 226 ? 0.2416 0.2841 0.3222 0.0191  -0.0143 -0.0753 336  GLY A CA    
1335 C  C     . GLY A 226 ? 0.2540 0.2835 0.3305 0.0143  -0.0129 -0.0840 336  GLY A C     
1336 O  O     . GLY A 226 ? 0.2632 0.2886 0.3305 0.0206  -0.0146 -0.0580 336  GLY A O     
1337 N  N     . PRO A 227 ? 0.2186 0.2699 0.2963 0.0254  -0.0104 -0.0783 337  PRO A N     
1338 C  CA    . PRO A 227 ? 0.2134 0.2802 0.2967 0.0180  -0.0393 -0.0521 337  PRO A CA    
1339 C  C     . PRO A 227 ? 0.2591 0.2559 0.3117 0.0299  -0.0450 -0.0206 337  PRO A C     
1340 O  O     . PRO A 227 ? 0.2691 0.2350 0.3179 0.0397  -0.0552 0.0335  337  PRO A O     
1341 C  CB    . PRO A 227 ? 0.2350 0.2845 0.2870 0.0247  -0.0454 -0.0509 337  PRO A CB    
1342 C  CG    . PRO A 227 ? 0.2157 0.2755 0.3012 0.0270  -0.0223 -0.0751 337  PRO A CG    
1343 C  CD    . PRO A 227 ? 0.2004 0.3083 0.3147 0.0146  0.0070  -0.0728 337  PRO A CD    
1344 N  N     . GLY A 228 ? 0.2495 0.2405 0.2952 0.0354  -0.0297 0.0170  338  GLY A N     
1345 C  CA    . GLY A 228 ? 0.2552 0.2644 0.2936 0.0119  -0.0398 0.0078  338  GLY A CA    
1346 C  C     . GLY A 228 ? 0.2496 0.2648 0.3040 0.0312  -0.0409 -0.0151 338  GLY A C     
1347 O  O     . GLY A 228 ? 0.2176 0.3217 0.3184 0.0392  -0.0261 -0.0212 338  GLY A O     
1348 N  N     . SER A 229 ? 0.2321 0.2449 0.2871 0.0077  -0.0336 -0.0172 339  SER A N     
1349 C  CA    . SER A 229 ? 0.2306 0.2610 0.3022 -0.0141 -0.0364 -0.0022 339  SER A CA    
1350 C  C     . SER A 229 ? 0.2437 0.2628 0.3052 0.0275  -0.0150 -0.0195 339  SER A C     
1351 O  O     . SER A 229 ? 0.2956 0.2821 0.3068 0.0089  0.0203  -0.0501 339  SER A O     
1352 C  CB    . SER A 229 ? 0.2234 0.2877 0.3217 -0.0088 -0.0576 0.0185  339  SER A CB    
1353 O  OG    . SER A 229 ? 0.2237 0.3194 0.3196 0.0053  -0.0523 0.0117  339  SER A OG    
1354 N  N     . ILE A 230 ? 0.2243 0.2372 0.2914 -0.0094 -0.0310 -0.0104 340  ILE A N     
1355 C  CA    . ILE A 230 ? 0.2557 0.2909 0.3037 0.0028  -0.0421 -0.0089 340  ILE A CA    
1356 C  C     . ILE A 230 ? 0.2488 0.2988 0.3118 -0.0014 -0.0506 -0.0364 340  ILE A C     
1357 O  O     . ILE A 230 ? 0.2773 0.3468 0.3459 0.0023  -0.0438 -0.0520 340  ILE A O     
1358 C  CB    . ILE A 230 ? 0.2654 0.2634 0.2865 0.0302  -0.0352 -0.0419 340  ILE A CB    
1359 C  CG1   . ILE A 230 ? 0.2515 0.2338 0.2578 -0.0011 -0.0468 -0.0564 340  ILE A CG1   
1360 C  CG2   . ILE A 230 ? 0.2686 0.3093 0.2909 0.0257  -0.0334 -0.0346 340  ILE A CG2   
1361 C  CD1   . ILE A 230 ? 0.3013 0.2413 0.2981 0.0012  -0.0421 -0.0531 340  ILE A CD1   
1362 N  N     . CYS A 231 ? 0.2297 0.3047 0.2753 -0.0046 -0.0442 -0.0256 341  CYS A N     
1363 C  CA    . CYS A 231 ? 0.2601 0.3471 0.2680 -0.0216 -0.0379 -0.0364 341  CYS A CA    
1364 C  C     . CYS A 231 ? 0.2541 0.2998 0.2961 -0.0379 -0.0343 -0.0437 341  CYS A C     
1365 O  O     . CYS A 231 ? 0.2810 0.2956 0.3317 -0.0473 -0.0433 -0.0106 341  CYS A O     
1366 C  CB    . CYS A 231 ? 0.3014 0.4959 0.2810 -0.0179 -0.0311 -0.0641 341  CYS A CB    
1367 S  SG    . CYS A 231 ? 0.3026 0.5979 0.2855 -0.0410 -0.0072 -0.1007 341  CYS A SG    
1368 N  N     . THR A 232 ? 0.1776 0.3024 0.2577 -0.0018 -0.0188 -0.0347 342  THR A N     
1369 C  CA    . THR A 232 ? 0.1994 0.2874 0.2362 0.0172  0.0127  -0.0159 342  THR A CA    
1370 C  C     . THR A 232 ? 0.2025 0.2540 0.2416 0.0080  0.0040  0.0078  342  THR A C     
1371 O  O     . THR A 232 ? 0.1844 0.2713 0.2595 0.0083  0.0024  0.0089  342  THR A O     
1372 C  CB    . THR A 232 ? 0.2622 0.3000 0.2554 0.0099  -0.0047 -0.0388 342  THR A CB    
1373 O  OG1   . THR A 232 ? 0.2526 0.2796 0.2494 -0.0072 0.0110  -0.0278 342  THR A OG1   
1374 C  CG2   . THR A 232 ? 0.3043 0.3321 0.2533 0.0110  -0.0198 -0.0361 342  THR A CG2   
1375 N  N     . THR A 233 ? 0.2105 0.2752 0.2075 0.0315  -0.0211 -0.0060 343  THR A N     
1376 C  CA    . THR A 233 ? 0.2071 0.2350 0.2199 0.0123  -0.0271 0.0042  343  THR A CA    
1377 C  C     . THR A 233 ? 0.1996 0.2262 0.2327 -0.0095 -0.0294 -0.0003 343  THR A C     
1378 O  O     . THR A 233 ? 0.1894 0.2172 0.2373 -0.0167 0.0037  0.0059  343  THR A O     
1379 C  CB    . THR A 233 ? 0.2169 0.2298 0.1814 0.0248  -0.0229 -0.0026 343  THR A CB    
1380 O  OG1   . THR A 233 ? 0.2754 0.1969 0.2172 0.0236  0.0338  0.0191  343  THR A OG1   
1381 C  CG2   . THR A 233 ? 0.2289 0.2542 0.1699 0.0173  -0.0158 -0.0184 343  THR A CG2   
1382 N  N     . ARG A 234 ? 0.2294 0.2260 0.2167 -0.0052 0.0024  0.0129  344  ARG A N     
1383 C  CA    . ARG A 234 ? 0.2322 0.2097 0.2696 -0.0094 0.0107  0.0238  344  ARG A CA    
1384 C  C     . ARG A 234 ? 0.2280 0.2174 0.2835 0.0028  -0.0029 -0.0007 344  ARG A C     
1385 O  O     . ARG A 234 ? 0.2439 0.3040 0.2617 0.0583  -0.0622 -0.0589 344  ARG A O     
1386 C  CB    . ARG A 234 ? 0.2856 0.2437 0.3290 -0.0799 0.0101  0.0397  344  ARG A CB    
1387 C  CG    . ARG A 234 ? 0.4123 0.3835 0.4102 -0.0829 -0.0084 0.0529  344  ARG A CG    
1388 C  CD    . ARG A 234 ? 0.5015 0.5217 0.4860 -0.0547 -0.0404 0.0761  344  ARG A CD    
1389 N  NE    . ARG A 234 ? 0.5517 0.5654 0.5384 -0.0353 -0.0884 0.0637  344  ARG A NE    
1390 C  CZ    . ARG A 234 ? 0.6179 0.6182 0.5483 -0.0383 -0.1090 0.1013  344  ARG A CZ    
1391 N  NH1   . ARG A 234 ? 0.6165 0.6271 0.5312 -0.0628 -0.1043 0.1909  344  ARG A NH1   
1392 N  NH2   . ARG A 234 ? 0.6586 0.6268 0.5501 -0.0090 -0.1209 0.1020  344  ARG A NH2   
1393 N  N     A VAL A 235 ? 0.2007 0.2130 0.3052 0.0140  0.0114  0.0028  345  VAL A N     
1394 N  N     B VAL A 235 ? 0.2433 0.2317 0.3033 0.0060  0.0138  -0.0070 345  VAL A N     
1395 C  CA    A VAL A 235 ? 0.1995 0.2385 0.3102 0.0050  0.0093  -0.0170 345  VAL A CA    
1396 C  CA    B VAL A 235 ? 0.2607 0.2500 0.3091 -0.0056 0.0236  -0.0284 345  VAL A CA    
1397 C  C     A VAL A 235 ? 0.1875 0.2492 0.3036 0.0078  0.0022  -0.0270 345  VAL A C     
1398 C  C     B VAL A 235 ? 0.2269 0.2428 0.3004 -0.0025 0.0161  -0.0303 345  VAL A C     
1399 O  O     A VAL A 235 ? 0.2109 0.2874 0.3376 0.0184  -0.0144 -0.0505 345  VAL A O     
1400 O  O     B VAL A 235 ? 0.2422 0.2546 0.3205 0.0066  0.0105  -0.0520 345  VAL A O     
1401 C  CB    A VAL A 235 ? 0.2176 0.2464 0.3028 -0.0382 0.0059  -0.0177 345  VAL A CB    
1402 C  CB    B VAL A 235 ? 0.3035 0.2762 0.3130 -0.0406 0.0362  -0.0347 345  VAL A CB    
1403 C  CG1   A VAL A 235 ? 0.2553 0.2594 0.3039 -0.0684 0.0292  -0.0277 345  VAL A CG1   
1404 C  CG1   B VAL A 235 ? 0.3205 0.3092 0.3085 -0.0642 0.0289  -0.0279 345  VAL A CG1   
1405 C  CG2   A VAL A 235 ? 0.1940 0.2470 0.2796 -0.0128 -0.0386 0.0123  345  VAL A CG2   
1406 C  CG2   B VAL A 235 ? 0.3257 0.2866 0.3160 -0.0465 0.0393  -0.0366 345  VAL A CG2   
1407 N  N     . VAL A 236 ? 0.2116 0.2329 0.2860 -0.0254 0.0157  -0.0180 346  VAL A N     
1408 C  CA    . VAL A 236 ? 0.1917 0.2498 0.2644 -0.0016 -0.0252 0.0116  346  VAL A CA    
1409 C  C     . VAL A 236 ? 0.1654 0.2363 0.2574 -0.0174 0.0030  0.0226  346  VAL A C     
1410 O  O     . VAL A 236 ? 0.1909 0.2080 0.2611 0.0034  -0.0095 0.0033  346  VAL A O     
1411 C  CB    . VAL A 236 ? 0.2260 0.2709 0.2607 -0.0645 -0.0274 0.0184  346  VAL A CB    
1412 C  CG1   . VAL A 236 ? 0.2424 0.3125 0.2719 -0.0642 -0.0032 -0.0035 346  VAL A CG1   
1413 C  CG2   . VAL A 236 ? 0.2623 0.3114 0.2785 -0.0213 -0.0330 0.0325  346  VAL A CG2   
1414 N  N     . ALA A 237 ? 0.1832 0.2438 0.2062 0.0091  0.0042  0.0347  347  ALA A N     
1415 C  CA    . ALA A 237 ? 0.2064 0.2179 0.2295 -0.0139 0.0185  0.0045  347  ALA A CA    
1416 C  C     . ALA A 237 ? 0.2247 0.2035 0.2483 -0.0241 0.0065  0.0292  347  ALA A C     
1417 O  O     . ALA A 237 ? 0.2219 0.1916 0.2635 -0.0121 0.0074  0.0100  347  ALA A O     
1418 C  CB    . ALA A 237 ? 0.2184 0.1989 0.2121 -0.0272 0.0113  -0.0314 347  ALA A CB    
1419 N  N     . GLY A 238 ? 0.2309 0.1790 0.2245 0.0033  0.0075  0.0267  348  GLY A N     
1420 C  CA    . GLY A 238 ? 0.2141 0.1973 0.2119 0.0200  0.0225  0.0378  348  GLY A CA    
1421 C  C     . GLY A 238 ? 0.2128 0.1800 0.2013 0.0042  0.0257  0.0204  348  GLY A C     
1422 O  O     . GLY A 238 ? 0.2341 0.1600 0.2063 0.0290  -0.0007 -0.0012 348  GLY A O     
1423 N  N     . VAL A 239 ? 0.1859 0.1701 0.2545 0.0252  0.0296  -0.0261 349  VAL A N     
1424 C  CA    . VAL A 239 ? 0.1621 0.1603 0.2605 -0.0107 0.0238  -0.0018 349  VAL A CA    
1425 C  C     . VAL A 239 ? 0.1820 0.2138 0.2909 0.0008  0.0038  0.0417  349  VAL A C     
1426 O  O     . VAL A 239 ? 0.1889 0.2554 0.2981 -0.0417 -0.0202 0.0662  349  VAL A O     
1427 C  CB    . VAL A 239 ? 0.1458 0.1699 0.2814 -0.0089 0.0487  -0.0022 349  VAL A CB    
1428 C  CG1   . VAL A 239 ? 0.1705 0.1510 0.2855 0.0137  0.0279  -0.0053 349  VAL A CG1   
1429 C  CG2   . VAL A 239 ? 0.1666 0.1671 0.2927 -0.0502 0.0204  0.0108  349  VAL A CG2   
1430 N  N     . GLY A 240 ? 0.1544 0.2082 0.2908 -0.0308 -0.0063 0.0620  350  GLY A N     
1431 C  CA    . GLY A 240 ? 0.1715 0.2128 0.2768 -0.0399 0.0339  0.0763  350  GLY A CA    
1432 C  C     . GLY A 240 ? 0.1687 0.2101 0.2786 -0.0498 0.0350  0.0162  350  GLY A C     
1433 O  O     . GLY A 240 ? 0.1814 0.2501 0.2879 -0.0512 0.0051  0.0262  350  GLY A O     
1434 N  N     . ALA A 241 ? 0.1717 0.2217 0.2749 -0.0494 0.0337  -0.0029 351  ALA A N     
1435 C  CA    . ALA A 241 ? 0.1677 0.2250 0.2111 -0.0373 0.0529  -0.0412 351  ALA A CA    
1436 C  C     . ALA A 241 ? 0.1868 0.2088 0.2423 -0.0210 0.0235  -0.0061 351  ALA A C     
1437 O  O     . ALA A 241 ? 0.2000 0.2048 0.2676 -0.0244 -0.0001 0.0181  351  ALA A O     
1438 C  CB    . ALA A 241 ? 0.2200 0.2516 0.2447 -0.0472 -0.0027 -0.0856 351  ALA A CB    
1439 N  N     . PRO A 242 ? 0.1845 0.1912 0.2291 0.0080  0.0152  0.0221  352  PRO A N     
1440 C  CA    . PRO A 242 ? 0.1717 0.1769 0.2570 -0.0079 0.0169  -0.0030 352  PRO A CA    
1441 C  C     . PRO A 242 ? 0.1561 0.1966 0.2388 -0.0123 -0.0096 0.0093  352  PRO A C     
1442 O  O     . PRO A 242 ? 0.1879 0.2119 0.2005 -0.0222 0.0073  0.0153  352  PRO A O     
1443 C  CB    . PRO A 242 ? 0.1440 0.1969 0.2714 -0.0111 0.0144  -0.0074 352  PRO A CB    
1444 C  CG    . PRO A 242 ? 0.1922 0.1563 0.2613 -0.0166 0.0030  -0.0233 352  PRO A CG    
1445 C  CD    . PRO A 242 ? 0.1850 0.1728 0.2505 -0.0103 -0.0033 -0.0145 352  PRO A CD    
1446 N  N     A GLN A 243 ? 0.1416 0.1832 0.2245 0.0098  -0.0256 0.0169  353  GLN A N     
1447 N  N     B GLN A 243 ? 0.1530 0.1884 0.2379 -0.0156 -0.0142 0.0063  353  GLN A N     
1448 C  CA    A GLN A 243 ? 0.1665 0.1833 0.2149 0.0241  -0.0440 0.0269  353  GLN A CA    
1449 C  CA    B GLN A 243 ? 0.1683 0.1920 0.2279 -0.0161 -0.0279 -0.0005 353  GLN A CA    
1450 C  C     A GLN A 243 ? 0.1748 0.1771 0.2206 0.0196  -0.0118 0.0251  353  GLN A C     
1451 C  C     B GLN A 243 ? 0.1854 0.1960 0.2189 -0.0078 -0.0144 -0.0050 353  GLN A C     
1452 O  O     A GLN A 243 ? 0.1685 0.2053 0.2406 0.0355  -0.0067 0.0262  353  GLN A O     
1453 O  O     B GLN A 243 ? 0.1994 0.2140 0.2271 0.0043  -0.0180 -0.0176 353  GLN A O     
1454 C  CB    A GLN A 243 ? 0.2232 0.2169 0.2460 0.0674  -0.0611 -0.0082 353  GLN A CB    
1455 C  CB    B GLN A 243 ? 0.1849 0.2008 0.2413 -0.0116 -0.0399 -0.0211 353  GLN A CB    
1456 C  CG    A GLN A 243 ? 0.2494 0.2066 0.2616 0.0660  -0.0483 0.0079  353  GLN A CG    
1457 C  CG    B GLN A 243 ? 0.1665 0.1782 0.2490 -0.0426 -0.0375 -0.0179 353  GLN A CG    
1458 C  CD    A GLN A 243 ? 0.2579 0.1852 0.2810 0.0400  -0.0395 0.0148  353  GLN A CD    
1459 C  CD    B GLN A 243 ? 0.1674 0.1653 0.2723 -0.0328 -0.0421 -0.0136 353  GLN A CD    
1460 O  OE1   A GLN A 243 ? 0.2643 0.1880 0.2575 0.0259  0.0023  0.0136  353  GLN A OE1   
1461 O  OE1   B GLN A 243 ? 0.1619 0.1653 0.2728 -0.0275 -0.0577 -0.0093 353  GLN A OE1   
1462 N  NE2   A GLN A 243 ? 0.2558 0.2103 0.3126 0.0437  -0.0567 -0.0134 353  GLN A NE2   
1463 N  NE2   B GLN A 243 ? 0.1953 0.1827 0.2888 -0.0258 -0.0271 -0.0075 353  GLN A NE2   
1464 N  N     . ILE A 244 ? 0.1755 0.2085 0.2061 -0.0218 -0.0053 -0.0069 354  ILE A N     
1465 C  CA    . ILE A 244 ? 0.1779 0.1701 0.2205 -0.0122 -0.0119 -0.0102 354  ILE A CA    
1466 C  C     . ILE A 244 ? 0.1640 0.1903 0.2467 -0.0008 -0.0060 -0.0070 354  ILE A C     
1467 O  O     . ILE A 244 ? 0.1822 0.2235 0.2355 -0.0327 -0.0157 0.0006  354  ILE A O     
1468 C  CB    . ILE A 244 ? 0.1813 0.2071 0.2015 -0.0501 0.0126  -0.0024 354  ILE A CB    
1469 C  CG1   . ILE A 244 ? 0.1676 0.2385 0.2172 0.0142  0.0342  -0.0065 354  ILE A CG1   
1470 C  CG2   . ILE A 244 ? 0.2066 0.2062 0.2257 -0.0254 0.0215  -0.0292 354  ILE A CG2   
1471 C  CD1   . ILE A 244 ? 0.1807 0.2222 0.2128 -0.0121 0.0141  0.0146  354  ILE A CD1   
1472 N  N     . THR A 245 ? 0.1687 0.1690 0.2516 -0.0102 -0.0055 -0.0184 355  THR A N     
1473 C  CA    . THR A 245 ? 0.1692 0.1753 0.2506 0.0096  -0.0225 0.0060  355  THR A CA    
1474 C  C     . THR A 245 ? 0.2041 0.2038 0.2488 0.0172  -0.0271 0.0168  355  THR A C     
1475 O  O     . THR A 245 ? 0.1886 0.2049 0.2546 -0.0252 0.0023  0.0105  355  THR A O     
1476 C  CB    . THR A 245 ? 0.2122 0.2018 0.2182 0.0235  -0.0221 0.0089  355  THR A CB    
1477 O  OG1   . THR A 245 ? 0.2237 0.2021 0.1846 0.0069  -0.0047 0.0196  355  THR A OG1   
1478 C  CG2   . THR A 245 ? 0.2161 0.2601 0.2198 0.0386  -0.0434 0.0063  355  THR A CG2   
1479 N  N     . ALA A 246 ? 0.1904 0.1481 0.2134 -0.0035 -0.0121 0.0093  356  ALA A N     
1480 C  CA    . ALA A 246 ? 0.1973 0.1678 0.2065 0.0228  0.0095  0.0484  356  ALA A CA    
1481 C  C     . ALA A 246 ? 0.2005 0.1966 0.2436 0.0023  0.0222  0.0056  356  ALA A C     
1482 O  O     . ALA A 246 ? 0.2067 0.2164 0.2650 -0.0221 0.0026  -0.0243 356  ALA A O     
1483 C  CB    . ALA A 246 ? 0.1748 0.1349 0.2077 -0.0133 -0.0115 0.0230  356  ALA A CB    
1484 N  N     . ILE A 247 ? 0.1824 0.1884 0.2497 -0.0144 0.0241  0.0160  357  ILE A N     
1485 C  CA    . ILE A 247 ? 0.1643 0.2029 0.2179 -0.0298 0.0147  0.0142  357  ILE A CA    
1486 C  C     . ILE A 247 ? 0.1794 0.1809 0.2243 0.0190  0.0421  0.0056  357  ILE A C     
1487 O  O     . ILE A 247 ? 0.1981 0.1818 0.2208 -0.0119 0.0085  -0.0160 357  ILE A O     
1488 C  CB    . ILE A 247 ? 0.1511 0.2028 0.1876 -0.0210 0.0125  0.0117  357  ILE A CB    
1489 C  CG1   . ILE A 247 ? 0.1839 0.1935 0.1738 -0.0205 -0.0232 0.0004  357  ILE A CG1   
1490 C  CG2   . ILE A 247 ? 0.1730 0.1965 0.2052 -0.0348 0.0353  0.0215  357  ILE A CG2   
1491 C  CD1   . ILE A 247 ? 0.2233 0.1788 0.1661 0.0128  -0.0161 0.0183  357  ILE A CD1   
1492 N  N     . LEU A 248 ? 0.1798 0.1590 0.2277 -0.0150 -0.0071 0.0321  358  LEU A N     
1493 C  CA    . LEU A 248 ? 0.2333 0.1623 0.2319 -0.0021 -0.0074 -0.0047 358  LEU A CA    
1494 C  C     . LEU A 248 ? 0.2331 0.1974 0.2226 -0.0407 -0.0035 -0.0134 358  LEU A C     
1495 O  O     . LEU A 248 ? 0.2227 0.2180 0.2018 -0.0220 -0.0028 0.0076  358  LEU A O     
1496 C  CB    . LEU A 248 ? 0.2355 0.1409 0.2352 0.0044  -0.0238 -0.0107 358  LEU A CB    
1497 C  CG    . LEU A 248 ? 0.2054 0.1318 0.2466 -0.0027 0.0234  -0.0011 358  LEU A CG    
1498 C  CD1   . LEU A 248 ? 0.2514 0.1316 0.2918 -0.0114 -0.0032 -0.0335 358  LEU A CD1   
1499 C  CD2   . LEU A 248 ? 0.1951 0.1802 0.2274 -0.0250 0.0242  0.0160  358  LEU A CD2   
1500 N  N     . GLU A 249 ? 0.2285 0.2043 0.1940 -0.0178 -0.0011 -0.0038 359  GLU A N     
1501 C  CA    . GLU A 249 ? 0.1923 0.2012 0.1904 0.0170  -0.0268 -0.0320 359  GLU A CA    
1502 C  C     . GLU A 249 ? 0.2301 0.2178 0.1843 -0.0060 -0.0184 -0.0113 359  GLU A C     
1503 O  O     . GLU A 249 ? 0.2683 0.2278 0.1547 -0.0154 0.0353  -0.0097 359  GLU A O     
1504 C  CB    . GLU A 249 ? 0.2007 0.2080 0.2226 0.0270  -0.0309 -0.0399 359  GLU A CB    
1505 C  CG    . GLU A 249 ? 0.2056 0.2109 0.2029 0.0117  -0.0315 -0.0395 359  GLU A CG    
1506 C  CD    . GLU A 249 ? 0.2402 0.2195 0.2422 -0.0213 -0.0130 0.0055  359  GLU A CD    
1507 O  OE1   . GLU A 249 ? 0.2570 0.2269 0.2648 -0.0189 -0.0216 0.0298  359  GLU A OE1   
1508 O  OE2   . GLU A 249 ? 0.2510 0.2259 0.2495 -0.0255 -0.0115 0.0004  359  GLU A OE2   
1509 N  N     . ALA A 250 ? 0.1924 0.1827 0.2081 0.0020  -0.0288 0.0094  360  ALA A N     
1510 C  CA    . ALA A 250 ? 0.1932 0.1986 0.2073 0.0167  -0.0014 0.0390  360  ALA A CA    
1511 C  C     . ALA A 250 ? 0.1956 0.1945 0.2203 -0.0060 -0.0055 0.0088  360  ALA A C     
1512 O  O     . ALA A 250 ? 0.2086 0.2167 0.2226 0.0102  0.0228  -0.0098 360  ALA A O     
1513 C  CB    . ALA A 250 ? 0.1928 0.2057 0.2101 0.0103  -0.0111 0.0452  360  ALA A CB    
1514 N  N     . VAL A 251 ? 0.1994 0.1990 0.2272 -0.0184 0.0074  -0.0051 361  VAL A N     
1515 C  CA    . VAL A 251 ? 0.2289 0.2249 0.2328 -0.0263 0.0035  -0.0417 361  VAL A CA    
1516 C  C     . VAL A 251 ? 0.2271 0.2405 0.2119 -0.0120 0.0065  -0.0137 361  VAL A C     
1517 O  O     . VAL A 251 ? 0.2287 0.2247 0.2380 -0.0103 0.0260  -0.0006 361  VAL A O     
1518 C  CB    . VAL A 251 ? 0.1884 0.2564 0.2357 -0.0271 0.0196  -0.0225 361  VAL A CB    
1519 C  CG1   . VAL A 251 ? 0.2325 0.3046 0.2676 -0.0574 0.0215  -0.0085 361  VAL A CG1   
1520 C  CG2   . VAL A 251 ? 0.1973 0.2615 0.2423 -0.0097 -0.0138 0.0180  361  VAL A CG2   
1521 N  N     . ALA A 252 ? 0.2389 0.2204 0.1943 -0.0090 -0.0115 -0.0085 362  ALA A N     
1522 C  CA    . ALA A 252 ? 0.2424 0.2250 0.1856 -0.0051 -0.0181 0.0010  362  ALA A CA    
1523 C  C     . ALA A 252 ? 0.2767 0.2547 0.1958 -0.0076 -0.0177 -0.0240 362  ALA A C     
1524 O  O     . ALA A 252 ? 0.3170 0.2729 0.1745 -0.0128 -0.0002 -0.0358 362  ALA A O     
1525 C  CB    . ALA A 252 ? 0.2438 0.2413 0.1826 -0.0070 -0.0100 0.0297  362  ALA A CB    
1526 N  N     . ALA A 253 ? 0.2594 0.2279 0.2089 -0.0279 -0.0241 -0.0293 363  ALA A N     
1527 C  CA    . ALA A 253 ? 0.2495 0.2275 0.2246 -0.0714 -0.0186 0.0065  363  ALA A CA    
1528 C  C     . ALA A 253 ? 0.2589 0.2405 0.2336 -0.0279 0.0116  -0.0147 363  ALA A C     
1529 O  O     . ALA A 253 ? 0.2823 0.2901 0.2412 0.0138  0.0016  -0.0528 363  ALA A O     
1530 C  CB    . ALA A 253 ? 0.2595 0.2159 0.2561 -0.0577 -0.0120 0.0152  363  ALA A CB    
1531 N  N     . CYS A 254 ? 0.2357 0.2254 0.2078 -0.0361 0.0252  -0.0261 364  CYS A N     
1532 C  CA    . CYS A 254 ? 0.2202 0.2361 0.2021 -0.0041 0.0156  -0.0132 364  CYS A CA    
1533 C  C     . CYS A 254 ? 0.2128 0.2532 0.2332 0.0279  0.0266  -0.0435 364  CYS A C     
1534 O  O     . CYS A 254 ? 0.2057 0.2686 0.2292 0.0372  0.0280  -0.0471 364  CYS A O     
1535 C  CB    . CYS A 254 ? 0.2089 0.2471 0.1805 -0.0027 0.0276  -0.0095 364  CYS A CB    
1536 S  SG    . CYS A 254 ? 0.2116 0.2277 0.2115 0.0012  0.0266  -0.0050 364  CYS A SG    
1537 N  N     . ARG A 255 ? 0.2331 0.2523 0.2590 -0.0163 0.0517  -0.0389 365  ARG A N     
1538 C  CA    . ARG A 255 ? 0.2288 0.2782 0.3026 -0.0040 0.0831  -0.0220 365  ARG A CA    
1539 C  C     . ARG A 255 ? 0.2381 0.3299 0.2991 0.0187  0.1217  -0.0108 365  ARG A C     
1540 O  O     . ARG A 255 ? 0.2705 0.3279 0.3149 0.0080  0.1169  -0.0129 365  ARG A O     
1541 C  CB    . ARG A 255 ? 0.2513 0.3183 0.3701 -0.0571 0.0760  0.0148  365  ARG A CB    
1542 C  CG    . ARG A 255 ? 0.3533 0.3935 0.4551 -0.0570 0.0695  0.0279  365  ARG A CG    
1543 C  CD    . ARG A 255 ? 0.4542 0.4804 0.5241 -0.1098 0.0642  0.0296  365  ARG A CD    
1544 N  NE    . ARG A 255 ? 0.5695 0.5696 0.5944 -0.1036 0.0343  0.0225  365  ARG A NE    
1545 C  CZ    . ARG A 255 ? 0.6553 0.6440 0.6382 -0.1041 0.0500  0.0411  365  ARG A CZ    
1546 N  NH1   . ARG A 255 ? 0.7303 0.7009 0.6318 -0.0906 0.0578  0.0271  365  ARG A NH1   
1547 N  NH2   . ARG A 255 ? 0.6796 0.6781 0.6714 -0.1054 0.0581  0.0647  365  ARG A NH2   
1548 N  N     . PRO A 256 ? 0.2436 0.3286 0.2842 0.0318  0.0894  -0.0327 366  PRO A N     
1549 C  CA    . PRO A 256 ? 0.2710 0.3388 0.2714 0.0271  0.0557  -0.0369 366  PRO A CA    
1550 C  C     . PRO A 256 ? 0.2924 0.3290 0.2753 0.0276  0.0426  -0.0402 366  PRO A C     
1551 O  O     . PRO A 256 ? 0.2933 0.3677 0.2866 0.0489  0.0352  -0.0487 366  PRO A O     
1552 C  CB    . PRO A 256 ? 0.2749 0.3698 0.2758 0.0416  0.0433  -0.0179 366  PRO A CB    
1553 C  CG    . PRO A 256 ? 0.2925 0.3763 0.2967 0.0478  0.0115  -0.0092 366  PRO A CG    
1554 C  CD    . PRO A 256 ? 0.2616 0.3512 0.2779 0.0349  0.0369  -0.0146 366  PRO A CD    
1555 N  N     . ALA A 257 ? 0.2664 0.3122 0.2733 -0.0213 0.0342  -0.0582 367  ALA A N     
1556 C  CA    . ALA A 257 ? 0.2680 0.3156 0.2837 -0.0439 0.0248  -0.0420 367  ALA A CA    
1557 C  C     . ALA A 257 ? 0.2697 0.3498 0.2981 0.0026  0.0426  -0.0556 367  ALA A C     
1558 O  O     . ALA A 257 ? 0.3060 0.3778 0.3263 0.0096  0.0485  -0.0700 367  ALA A O     
1559 C  CB    . ALA A 257 ? 0.2694 0.2990 0.2696 -0.0569 0.0173  -0.0592 367  ALA A CB    
1560 N  N     . GLY A 258 ? 0.2462 0.3668 0.2663 0.0217  0.0526  0.0036  368  GLY A N     
1561 C  CA    . GLY A 258 ? 0.2651 0.3666 0.2523 0.0491  0.0452  0.0125  368  GLY A CA    
1562 C  C     . GLY A 258 ? 0.2724 0.3185 0.2428 0.0643  0.0308  -0.0169 368  GLY A C     
1563 O  O     . GLY A 258 ? 0.3234 0.3542 0.2555 0.0429  0.0228  -0.0050 368  GLY A O     
1564 N  N     . VAL A 259 ? 0.2307 0.2610 0.2209 0.0275  0.0500  -0.0697 369  VAL A N     
1565 C  CA    . VAL A 259 ? 0.2477 0.2251 0.2421 -0.0064 0.0518  -0.0286 369  VAL A CA    
1566 C  C     . VAL A 259 ? 0.2292 0.1879 0.2515 -0.0046 0.0340  -0.0374 369  VAL A C     
1567 O  O     . VAL A 259 ? 0.2389 0.1881 0.2951 -0.0007 0.0144  -0.0301 369  VAL A O     
1568 C  CB    . VAL A 259 ? 0.2628 0.2112 0.2573 -0.0261 0.0419  -0.0661 369  VAL A CB    
1569 C  CG1   . VAL A 259 ? 0.2602 0.2499 0.2666 -0.0223 0.0388  -0.0252 369  VAL A CG1   
1570 C  CG2   . VAL A 259 ? 0.2397 0.2361 0.2775 0.0000  0.0031  -0.0598 369  VAL A CG2   
1571 N  N     . PRO A 260 ? 0.2159 0.1847 0.2340 0.0393  0.0271  -0.0352 370  PRO A N     
1572 C  CA    . PRO A 260 ? 0.2045 0.2034 0.2339 -0.0070 0.0119  -0.0495 370  PRO A CA    
1573 C  C     . PRO A 260 ? 0.2250 0.1986 0.2109 -0.0039 0.0260  -0.0509 370  PRO A C     
1574 O  O     . PRO A 260 ? 0.2342 0.2211 0.1921 -0.0253 0.0270  -0.0324 370  PRO A O     
1575 C  CB    . PRO A 260 ? 0.2139 0.2337 0.2441 0.0365  0.0064  -0.0443 370  PRO A CB    
1576 C  CG    . PRO A 260 ? 0.2538 0.2298 0.2732 0.0413  -0.0257 -0.0454 370  PRO A CG    
1577 C  CD    . PRO A 260 ? 0.2223 0.2354 0.2324 0.0152  -0.0276 -0.0325 370  PRO A CD    
1578 N  N     . VAL A 261 ? 0.2090 0.1865 0.1801 -0.0012 0.0295  -0.0249 371  VAL A N     
1579 C  CA    . VAL A 261 ? 0.2069 0.1735 0.1894 -0.0062 0.0128  -0.0018 371  VAL A CA    
1580 C  C     . VAL A 261 ? 0.2082 0.1688 0.1930 -0.0272 -0.0049 0.0068  371  VAL A C     
1581 O  O     . VAL A 261 ? 0.1960 0.1760 0.2069 -0.0260 -0.0001 -0.0202 371  VAL A O     
1582 C  CB    . VAL A 261 ? 0.2185 0.2050 0.1764 0.0044  -0.0008 -0.0246 371  VAL A CB    
1583 C  CG1   . VAL A 261 ? 0.2175 0.2193 0.1981 0.0030  0.0137  -0.0101 371  VAL A CG1   
1584 C  CG2   . VAL A 261 ? 0.2618 0.2232 0.1888 0.0101  -0.0313 -0.0381 371  VAL A CG2   
1585 N  N     . ILE A 262 ? 0.2175 0.1871 0.1889 -0.0113 -0.0017 0.0245  372  ILE A N     
1586 C  CA    . ILE A 262 ? 0.2218 0.1866 0.1766 0.0209  -0.0153 0.0048  372  ILE A CA    
1587 C  C     . ILE A 262 ? 0.2306 0.1888 0.1906 0.0181  -0.0035 -0.0151 372  ILE A C     
1588 O  O     . ILE A 262 ? 0.2544 0.1802 0.2157 0.0006  -0.0063 -0.0218 372  ILE A O     
1589 C  CB    . ILE A 262 ? 0.2188 0.2074 0.1705 0.0225  -0.0005 0.0079  372  ILE A CB    
1590 C  CG1   . ILE A 262 ? 0.2536 0.1739 0.1987 0.0139  0.0094  0.0421  372  ILE A CG1   
1591 C  CG2   . ILE A 262 ? 0.2451 0.2277 0.1419 0.0036  -0.0077 0.0346  372  ILE A CG2   
1592 C  CD1   . ILE A 262 ? 0.2661 0.1895 0.2435 0.0092  0.0321  0.0350  372  ILE A CD1   
1593 N  N     . ALA A 263 ? 0.2060 0.1423 0.1818 0.0363  0.0220  -0.0203 373  ALA A N     
1594 C  CA    . ALA A 263 ? 0.2252 0.1169 0.2040 -0.0216 0.0168  -0.0264 373  ALA A CA    
1595 C  C     . ALA A 263 ? 0.2037 0.1759 0.1919 -0.0137 0.0262  -0.0068 373  ALA A C     
1596 O  O     . ALA A 263 ? 0.2079 0.2236 0.2189 -0.0069 0.0059  -0.0053 373  ALA A O     
1597 C  CB    . ALA A 263 ? 0.2525 0.1506 0.2410 -0.0502 -0.0060 -0.0038 373  ALA A CB    
1598 N  N     . ASP A 264 ? 0.1853 0.1748 0.1826 -0.0066 0.0430  0.0199  374  ASP A N     
1599 C  CA    . ASP A 264 ? 0.1849 0.1445 0.1970 -0.0055 0.0206  0.0398  374  ASP A CA    
1600 C  C     . ASP A 264 ? 0.2038 0.1817 0.2088 -0.0099 -0.0151 -0.0013 374  ASP A C     
1601 O  O     . ASP A 264 ? 0.1976 0.2061 0.1916 0.0047  -0.0117 -0.0096 374  ASP A O     
1602 C  CB    . ASP A 264 ? 0.2167 0.1648 0.2255 -0.0163 -0.0016 0.0490  374  ASP A CB    
1603 C  CG    . ASP A 264 ? 0.2086 0.1439 0.2526 -0.0178 -0.0106 0.0251  374  ASP A CG    
1604 O  OD1   . ASP A 264 ? 0.1872 0.1766 0.2811 -0.0262 -0.0437 -0.0013 374  ASP A OD1   
1605 O  OD2   . ASP A 264 ? 0.2123 0.1690 0.2228 0.0121  -0.0073 0.0092  374  ASP A OD2   
1606 N  N     . GLY A 265 ? 0.2076 0.1776 0.2356 0.0115  -0.0114 -0.0048 375  GLY A N     
1607 C  CA    . GLY A 265 ? 0.2114 0.1392 0.2426 0.0168  0.0062  -0.0167 375  GLY A CA    
1608 C  C     . GLY A 265 ? 0.2474 0.1497 0.2338 0.0091  0.0098  -0.0097 375  GLY A C     
1609 O  O     . GLY A 265 ? 0.2790 0.2061 0.2286 0.0168  0.0553  -0.0103 375  GLY A O     
1610 N  N     . GLY A 266 ? 0.2315 0.1074 0.2531 -0.0050 -0.0043 -0.0013 376  GLY A N     
1611 C  CA    . GLY A 266 ? 0.2320 0.1405 0.2549 -0.0044 0.0194  -0.0059 376  GLY A CA    
1612 C  C     . GLY A 266 ? 0.2553 0.1725 0.2888 -0.0085 0.0437  0.0037  376  GLY A C     
1613 O  O     . GLY A 266 ? 0.2658 0.2096 0.3123 -0.0197 0.0430  -0.0023 376  GLY A O     
1614 N  N     . LEU A 267 ? 0.2404 0.1807 0.2629 -0.0191 -0.0054 0.0010  377  LEU A N     
1615 C  CA    . LEU A 267 ? 0.2203 0.1792 0.2584 -0.0286 0.0277  -0.0206 377  LEU A CA    
1616 C  C     . LEU A 267 ? 0.2804 0.1931 0.2519 -0.0264 0.0215  -0.0055 377  LEU A C     
1617 O  O     . LEU A 267 ? 0.2800 0.2162 0.2615 -0.0293 -0.0053 0.0153  377  LEU A O     
1618 C  CB    . LEU A 267 ? 0.2071 0.2209 0.2562 0.0165  0.0534  -0.0015 377  LEU A CB    
1619 C  CG    . LEU A 267 ? 0.1904 0.2531 0.2950 -0.0033 0.0360  -0.0487 377  LEU A CG    
1620 C  CD1   . LEU A 267 ? 0.2342 0.2401 0.3128 -0.0138 0.0273  -0.0109 377  LEU A CD1   
1621 C  CD2   . LEU A 267 ? 0.2320 0.3292 0.3040 -0.0051 0.0657  -0.0325 377  LEU A CD2   
1622 N  N     . GLN A 268 ? 0.2975 0.1914 0.2732 0.0009  0.0402  -0.0089 378  GLN A N     
1623 C  CA    . GLN A 268 ? 0.3312 0.2584 0.2992 -0.0061 0.0512  -0.0158 378  GLN A CA    
1624 C  C     . GLN A 268 ? 0.3398 0.2598 0.2796 -0.0355 0.0129  0.0191  378  GLN A C     
1625 O  O     . GLN A 268 ? 0.4054 0.3117 0.3125 -0.0492 0.0200  0.0419  378  GLN A O     
1626 C  CB    . GLN A 268 ? 0.3570 0.3511 0.3537 0.0052  0.0898  -0.0425 378  GLN A CB    
1627 C  CG    . GLN A 268 ? 0.4263 0.4387 0.4318 0.0575  0.1094  -0.0623 378  GLN A CG    
1628 C  CD    . GLN A 268 ? 0.5259 0.5212 0.5041 0.0860  0.0960  -0.0472 378  GLN A CD    
1629 O  OE1   . GLN A 268 ? 0.5693 0.5698 0.5324 0.1181  0.0922  -0.0779 378  GLN A OE1   
1630 N  NE2   . GLN A 268 ? 0.5805 0.5487 0.5294 0.0996  0.0637  -0.0099 378  GLN A NE2   
1631 N  N     . TYR A 269 ? 0.2943 0.1994 0.2539 -0.0486 0.0576  0.0269  379  TYR A N     
1632 C  CA    . TYR A 269 ? 0.2930 0.1980 0.2972 -0.0201 0.0607  0.0252  379  TYR A CA    
1633 C  C     . TYR A 269 ? 0.2682 0.2148 0.2680 -0.0196 0.0371  0.0288  379  TYR A C     
1634 O  O     . TYR A 269 ? 0.2629 0.2168 0.2435 -0.0268 0.0036  0.0032  379  TYR A O     
1635 C  CB    . TYR A 269 ? 0.3358 0.2326 0.3470 -0.0098 0.0995  -0.0286 379  TYR A CB    
1636 C  CG    . TYR A 269 ? 0.3648 0.2938 0.3992 -0.0207 0.1070  -0.0235 379  TYR A CG    
1637 C  CD1   . TYR A 269 ? 0.3944 0.3248 0.4105 -0.0087 0.1090  -0.0326 379  TYR A CD1   
1638 C  CD2   . TYR A 269 ? 0.3738 0.2940 0.4352 -0.0179 0.1320  -0.0452 379  TYR A CD2   
1639 C  CE1   . TYR A 269 ? 0.4154 0.3594 0.4275 -0.0011 0.1172  -0.0409 379  TYR A CE1   
1640 C  CE2   . TYR A 269 ? 0.3945 0.3243 0.4533 -0.0304 0.1259  -0.0521 379  TYR A CE2   
1641 C  CZ    . TYR A 269 ? 0.4245 0.3634 0.4562 0.0183  0.1559  -0.0369 379  TYR A CZ    
1642 O  OH    . TYR A 269 ? 0.4937 0.4105 0.4963 0.0144  0.1749  -0.0237 379  TYR A OH    
1643 N  N     . SER A 270 ? 0.2809 0.2392 0.2597 -0.0025 -0.0170 0.0420  380  SER A N     
1644 C  CA    . SER A 270 ? 0.2632 0.2120 0.2485 0.0076  -0.0571 0.0105  380  SER A CA    
1645 C  C     . SER A 270 ? 0.2454 0.1901 0.2393 -0.0095 -0.0316 0.0001  380  SER A C     
1646 O  O     . SER A 270 ? 0.2397 0.1815 0.2338 -0.0119 -0.0212 -0.0036 380  SER A O     
1647 C  CB    . SER A 270 ? 0.2608 0.2051 0.2488 0.0076  -0.0945 -0.0164 380  SER A CB    
1648 O  OG    . SER A 270 ? 0.2826 0.2276 0.2547 -0.0251 -0.0811 -0.0099 380  SER A OG    
1649 N  N     . GLY A 271 ? 0.2313 0.2034 0.2501 -0.0389 -0.0269 0.0233  381  GLY A N     
1650 C  CA    . GLY A 271 ? 0.2336 0.2141 0.2696 -0.0419 -0.0219 0.0220  381  GLY A CA    
1651 C  C     . GLY A 271 ? 0.2358 0.1975 0.2625 -0.0253 -0.0288 -0.0043 381  GLY A C     
1652 O  O     . GLY A 271 ? 0.2430 0.2141 0.2216 -0.0285 -0.0298 0.0245  381  GLY A O     
1653 N  N     . ASP A 272 ? 0.2036 0.1865 0.2983 -0.0239 -0.0059 0.0200  382  ASP A N     
1654 C  CA    . ASP A 272 ? 0.1840 0.1981 0.2838 -0.0316 -0.0100 0.0116  382  ASP A CA    
1655 C  C     . ASP A 272 ? 0.2162 0.2377 0.2328 -0.0141 -0.0096 0.0024  382  ASP A C     
1656 O  O     . ASP A 272 ? 0.1885 0.2600 0.2084 -0.0148 -0.0075 0.0378  382  ASP A O     
1657 C  CB    . ASP A 272 ? 0.2018 0.2131 0.3021 0.0104  0.0018  0.0349  382  ASP A CB    
1658 C  CG    . ASP A 272 ? 0.2355 0.2215 0.3265 -0.0266 0.0274  0.0286  382  ASP A CG    
1659 O  OD1   . ASP A 272 ? 0.2484 0.2258 0.3368 -0.0215 0.0243  0.0216  382  ASP A OD1   
1660 O  OD2   . ASP A 272 ? 0.2811 0.1930 0.3431 -0.0016 0.0391  0.0289  382  ASP A OD2   
1661 N  N     . ILE A 273 ? 0.2154 0.2186 0.1852 0.0204  -0.0138 -0.0135 383  ILE A N     
1662 C  CA    . ILE A 273 ? 0.2468 0.1790 0.1798 0.0279  -0.0257 -0.0006 383  ILE A CA    
1663 C  C     . ILE A 273 ? 0.2285 0.1808 0.1923 0.0036  -0.0027 -0.0327 383  ILE A C     
1664 O  O     . ILE A 273 ? 0.1879 0.1779 0.2368 -0.0295 -0.0203 -0.0214 383  ILE A O     
1665 C  CB    . ILE A 273 ? 0.3041 0.2363 0.1967 0.0299  -0.0657 -0.0079 383  ILE A CB    
1666 C  CG1   . ILE A 273 ? 0.3301 0.2753 0.1990 0.0732  -0.1163 0.0058  383  ILE A CG1   
1667 C  CG2   . ILE A 273 ? 0.3078 0.2260 0.2151 -0.0082 -0.0937 -0.0133 383  ILE A CG2   
1668 C  CD1   . ILE A 273 ? 0.3857 0.3067 0.2265 0.1097  -0.0746 -0.0325 383  ILE A CD1   
1669 N  N     . ALA A 274 ? 0.2264 0.1720 0.2166 -0.0097 -0.0036 0.0170  384  ALA A N     
1670 C  CA    . ALA A 274 ? 0.1893 0.1482 0.2494 -0.0257 -0.0139 0.0477  384  ALA A CA    
1671 C  C     . ALA A 274 ? 0.1729 0.2052 0.2484 0.0005  -0.0289 0.0449  384  ALA A C     
1672 O  O     . ALA A 274 ? 0.1738 0.2033 0.2841 -0.0008 -0.0185 0.0067  384  ALA A O     
1673 C  CB    . ALA A 274 ? 0.2008 0.1818 0.2436 -0.0173 -0.0328 0.0268  384  ALA A CB    
1674 N  N     . LYS A 275 ? 0.1540 0.1804 0.2628 0.0257  -0.0274 0.0316  385  LYS A N     
1675 C  CA    . LYS A 275 ? 0.1605 0.1657 0.2318 0.0205  -0.0198 -0.0001 385  LYS A CA    
1676 C  C     . LYS A 275 ? 0.1723 0.1606 0.2270 0.0143  -0.0408 0.0331  385  LYS A C     
1677 O  O     . LYS A 275 ? 0.1906 0.1829 0.2352 -0.0080 -0.0277 0.0342  385  LYS A O     
1678 C  CB    . LYS A 275 ? 0.1868 0.1645 0.2559 0.0310  -0.0149 -0.0382 385  LYS A CB    
1679 C  CG    . LYS A 275 ? 0.1910 0.1883 0.2337 0.0262  0.0288  -0.0698 385  LYS A CG    
1680 C  CD    . LYS A 275 ? 0.1986 0.1836 0.2161 0.0406  -0.0135 -0.0903 385  LYS A CD    
1681 C  CE    . LYS A 275 ? 0.2112 0.2062 0.2192 0.0476  0.0173  -0.0844 385  LYS A CE    
1682 N  NZ    . LYS A 275 ? 0.2118 0.2097 0.2212 0.0409  -0.0016 -0.0523 385  LYS A NZ    
1683 N  N     . ALA A 276 ? 0.1441 0.1805 0.2268 -0.0199 -0.0289 0.0074  386  ALA A N     
1684 C  CA    . ALA A 276 ? 0.1674 0.1812 0.1930 -0.0187 0.0277  0.0367  386  ALA A CA    
1685 C  C     . ALA A 276 ? 0.2060 0.2245 0.1973 -0.0112 0.0097  0.0008  386  ALA A C     
1686 O  O     . ALA A 276 ? 0.1927 0.2095 0.2001 0.0039  0.0072  0.0168  386  ALA A O     
1687 C  CB    . ALA A 276 ? 0.2225 0.1661 0.1743 -0.0197 0.0587  0.0143  386  ALA A CB    
1688 N  N     . LEU A 277 ? 0.1940 0.2229 0.1922 -0.0127 0.0144  0.0484  387  LEU A N     
1689 C  CA    . LEU A 277 ? 0.1732 0.2064 0.2226 -0.0094 -0.0106 0.0286  387  LEU A CA    
1690 C  C     . LEU A 277 ? 0.2078 0.1874 0.2557 0.0105  0.0325  0.0185  387  LEU A C     
1691 O  O     . LEU A 277 ? 0.2127 0.2125 0.2766 0.0186  0.0386  0.0213  387  LEU A O     
1692 C  CB    . LEU A 277 ? 0.1786 0.2246 0.2326 0.0087  -0.0184 0.0451  387  LEU A CB    
1693 C  CG    . LEU A 277 ? 0.1914 0.2085 0.2461 -0.0099 -0.0687 0.0278  387  LEU A CG    
1694 C  CD1   . LEU A 277 ? 0.1878 0.2416 0.2811 0.0094  -0.0626 0.0225  387  LEU A CD1   
1695 C  CD2   . LEU A 277 ? 0.2461 0.1908 0.2637 0.0021  -0.0562 -0.0160 387  LEU A CD2   
1696 N  N     . ALA A 278 ? 0.1884 0.1438 0.2777 -0.0062 0.0350  0.0434  388  ALA A N     
1697 C  CA    . ALA A 278 ? 0.1976 0.1246 0.2593 -0.0450 0.0172  -0.0019 388  ALA A CA    
1698 C  C     . ALA A 278 ? 0.2192 0.1965 0.2545 -0.0255 0.0213  -0.0013 388  ALA A C     
1699 O  O     . ALA A 278 ? 0.2337 0.2091 0.2478 -0.0072 0.0449  0.0047  388  ALA A O     
1700 C  CB    . ALA A 278 ? 0.2120 0.1369 0.2804 -0.0175 -0.0063 -0.0019 388  ALA A CB    
1701 N  N     . ALA A 279 ? 0.1876 0.1837 0.2665 -0.0089 0.0127  -0.0080 389  ALA A N     
1702 C  CA    . ALA A 279 ? 0.1558 0.1904 0.2663 0.0088  0.0480  0.0111  389  ALA A CA    
1703 C  C     . ALA A 279 ? 0.2013 0.2098 0.2723 0.0224  0.0308  0.0116  389  ALA A C     
1704 O  O     . ALA A 279 ? 0.2121 0.2113 0.2580 0.0216  0.0119  0.0203  389  ALA A O     
1705 C  CB    . ALA A 279 ? 0.1544 0.2201 0.2671 -0.0040 0.0361  0.0158  389  ALA A CB    
1706 N  N     . GLY A 280 ? 0.1987 0.1716 0.2349 0.0387  0.0553  0.0047  390  GLY A N     
1707 C  CA    . GLY A 280 ? 0.2058 0.1587 0.2543 0.0540  0.0297  0.0017  390  GLY A CA    
1708 C  C     . GLY A 280 ? 0.1915 0.1782 0.2301 0.0159  0.0088  0.0102  390  GLY A C     
1709 O  O     . GLY A 280 ? 0.1939 0.2241 0.2357 0.0206  0.0036  -0.0097 390  GLY A O     
1710 N  N     . ALA A 281 ? 0.1720 0.1866 0.2394 -0.0095 0.0166  0.0097  391  ALA A N     
1711 C  CA    . ALA A 281 ? 0.2031 0.2116 0.2204 0.0139  0.0315  0.0051  391  ALA A CA    
1712 C  C     . ALA A 281 ? 0.1844 0.2121 0.2288 -0.0011 0.0234  0.0152  391  ALA A C     
1713 O  O     . ALA A 281 ? 0.1866 0.1990 0.2512 -0.0256 0.0188  0.0042  391  ALA A O     
1714 C  CB    . ALA A 281 ? 0.2440 0.1879 0.2209 0.0223  0.0260  -0.0260 391  ALA A CB    
1715 N  N     . SER A 282 ? 0.1722 0.1989 0.2182 0.0195  0.0118  -0.0037 392  SER A N     
1716 C  CA    . SER A 282 ? 0.1888 0.2017 0.2035 0.0192  0.0307  -0.0089 392  SER A CA    
1717 C  C     . SER A 282 ? 0.1902 0.1995 0.2211 0.0258  0.0174  -0.0024 392  SER A C     
1718 O  O     . SER A 282 ? 0.1844 0.2141 0.2038 0.0129  0.0046  0.0155  392  SER A O     
1719 C  CB    . SER A 282 ? 0.2229 0.2427 0.1917 0.0138  0.0632  -0.0156 392  SER A CB    
1720 O  OG    . SER A 282 ? 0.2651 0.2584 0.2305 0.0243  0.0746  -0.0319 392  SER A OG    
1721 N  N     . THR A 283 ? 0.2328 0.1958 0.2152 0.0053  0.0153  0.0169  393  THR A N     
1722 C  CA    . THR A 283 ? 0.2045 0.2044 0.2107 0.0331  -0.0119 0.0289  393  THR A CA    
1723 C  C     . THR A 283 ? 0.2086 0.2048 0.2304 0.0272  -0.0077 0.0319  393  THR A C     
1724 O  O     . THR A 283 ? 0.1996 0.1744 0.2402 0.0088  0.0069  0.0122  393  THR A O     
1725 C  CB    . THR A 283 ? 0.1747 0.1860 0.2214 -0.0022 -0.0020 0.0062  393  THR A CB    
1726 O  OG1   . THR A 283 ? 0.1883 0.2099 0.2356 -0.0194 0.0064  -0.0032 393  THR A OG1   
1727 C  CG2   . THR A 283 ? 0.2239 0.1604 0.2439 0.0260  -0.0010 -0.0022 393  THR A CG2   
1728 N  N     . ALA A 284 ? 0.1896 0.2091 0.2455 0.0131  0.0089  0.0209  394  ALA A N     
1729 C  CA    . ALA A 284 ? 0.1748 0.1538 0.2723 0.0074  0.0387  0.0404  394  ALA A CA    
1730 C  C     . ALA A 284 ? 0.1973 0.1966 0.2381 0.0051  0.0131  0.0390  394  ALA A C     
1731 O  O     . ALA A 284 ? 0.2131 0.2024 0.2482 -0.0095 0.0021  0.0191  394  ALA A O     
1732 C  CB    . ALA A 284 ? 0.1957 0.1859 0.2761 0.0072  0.0309  0.0477  394  ALA A CB    
1733 N  N     . MET A 285 ? 0.2081 0.1633 0.2501 -0.0406 0.0366  0.0260  395  MET A N     
1734 C  CA    . MET A 285 ? 0.2026 0.1649 0.2342 -0.0311 0.0133  0.0214  395  MET A CA    
1735 C  C     . MET A 285 ? 0.1998 0.1817 0.2134 -0.0035 -0.0064 0.0060  395  MET A C     
1736 O  O     . MET A 285 ? 0.1857 0.2108 0.2057 -0.0234 -0.0139 0.0022  395  MET A O     
1737 C  CB    . MET A 285 ? 0.2037 0.1778 0.2412 -0.0105 0.0048  0.0168  395  MET A CB    
1738 C  CG    . MET A 285 ? 0.2068 0.1733 0.2299 -0.0224 -0.0028 0.0066  395  MET A CG    
1739 S  SD    . MET A 285 ? 0.2119 0.1948 0.2011 0.0007  -0.0087 -0.0075 395  MET A SD    
1740 C  CE    . MET A 285 ? 0.2549 0.1808 0.2593 0.0530  -0.0185 -0.0365 395  MET A CE    
1741 N  N     . LEU A 286 ? 0.1875 0.1945 0.2132 -0.0026 -0.0061 0.0052  396  LEU A N     
1742 C  CA    . LEU A 286 ? 0.1801 0.1912 0.2016 -0.0354 -0.0139 0.0060  396  LEU A CA    
1743 C  C     . LEU A 286 ? 0.2119 0.2040 0.2008 0.0209  -0.0148 0.0235  396  LEU A C     
1744 O  O     . LEU A 286 ? 0.2435 0.1779 0.1989 -0.0078 -0.0375 0.0173  396  LEU A O     
1745 C  CB    . LEU A 286 ? 0.2303 0.1958 0.2244 -0.0553 -0.0310 -0.0132 396  LEU A CB    
1746 C  CG    . LEU A 286 ? 0.2680 0.2167 0.2399 -0.0781 -0.0370 0.0120  396  LEU A CG    
1747 C  CD1   . LEU A 286 ? 0.2917 0.2757 0.2253 -0.0902 -0.0002 0.0055  396  LEU A CD1   
1748 C  CD2   . LEU A 286 ? 0.3142 0.2706 0.2607 -0.0637 -0.0616 0.0453  396  LEU A CD2   
1749 N  N     . GLY A 287 ? 0.2221 0.2445 0.1762 -0.0151 0.0255  0.0143  397  GLY A N     
1750 C  CA    . GLY A 287 ? 0.2147 0.2332 0.1823 -0.0215 0.0081  -0.0132 397  GLY A CA    
1751 C  C     . GLY A 287 ? 0.2301 0.2637 0.1915 0.0158  0.0124  -0.0143 397  GLY A C     
1752 O  O     . GLY A 287 ? 0.2476 0.3010 0.2128 0.0062  -0.0502 -0.0053 397  GLY A O     
1753 N  N     A SER A 288 ? 0.2203 0.2620 0.2008 0.0069  0.0359  -0.0264 398  SER A N     
1754 N  N     B SER A 288 ? 0.2209 0.2741 0.2088 0.0230  0.0256  -0.0193 398  SER A N     
1755 C  CA    A SER A 288 ? 0.2309 0.2742 0.2301 0.0099  0.0146  -0.0416 398  SER A CA    
1756 C  CA    B SER A 288 ? 0.2258 0.2862 0.2450 0.0313  0.0009  -0.0211 398  SER A CA    
1757 C  C     A SER A 288 ? 0.2486 0.2834 0.2532 -0.0031 -0.0063 -0.0646 398  SER A C     
1758 C  C     B SER A 288 ? 0.2503 0.2819 0.2549 0.0187  -0.0137 -0.0391 398  SER A C     
1759 O  O     A SER A 288 ? 0.2618 0.3176 0.2833 -0.0165 -0.0316 -0.0668 398  SER A O     
1760 O  O     B SER A 288 ? 0.2714 0.3047 0.2735 0.0237  -0.0390 -0.0148 398  SER A O     
1761 C  CB    A SER A 288 ? 0.2577 0.2473 0.2113 0.0224  0.0210  -0.0375 398  SER A CB    
1762 C  CB    B SER A 288 ? 0.2396 0.2796 0.2491 0.0412  -0.0020 -0.0067 398  SER A CB    
1763 O  OG    A SER A 288 ? 0.2736 0.2524 0.2112 0.0010  0.0030  -0.0472 398  SER A OG    
1764 O  OG    B SER A 288 ? 0.2299 0.2998 0.2643 0.0188  -0.0241 -0.0164 398  SER A OG    
1765 N  N     . LEU A 289 ? 0.2497 0.2610 0.2720 -0.0048 -0.0210 -0.0502 399  LEU A N     
1766 C  CA    . LEU A 289 ? 0.2576 0.2441 0.2744 0.0268  -0.0412 -0.0312 399  LEU A CA    
1767 C  C     . LEU A 289 ? 0.2562 0.2861 0.2676 0.0087  -0.0543 -0.0287 399  LEU A C     
1768 O  O     . LEU A 289 ? 0.2934 0.3002 0.2865 0.0080  -0.0612 -0.0185 399  LEU A O     
1769 C  CB    . LEU A 289 ? 0.2804 0.2017 0.3012 0.0323  -0.0515 -0.0011 399  LEU A CB    
1770 C  CG    . LEU A 289 ? 0.3644 0.2045 0.3128 0.0012  -0.0325 -0.0270 399  LEU A CG    
1771 C  CD1   . LEU A 289 ? 0.3379 0.2298 0.2873 -0.0155 0.0237  0.0357  399  LEU A CD1   
1772 C  CD2   . LEU A 289 ? 0.4413 0.2366 0.3646 0.0094  -0.0779 -0.0382 399  LEU A CD2   
1773 N  N     . LEU A 290 ? 0.2094 0.2700 0.2336 0.0183  -0.0490 -0.0210 400  LEU A N     
1774 C  CA    . LEU A 290 ? 0.2383 0.2930 0.2343 -0.0007 -0.0405 -0.0257 400  LEU A CA    
1775 C  C     . LEU A 290 ? 0.2302 0.3328 0.2728 -0.0134 -0.0481 -0.0155 400  LEU A C     
1776 O  O     . LEU A 290 ? 0.2849 0.3673 0.2706 -0.0402 -0.0634 -0.0202 400  LEU A O     
1777 C  CB    . LEU A 290 ? 0.2513 0.2845 0.2497 -0.0384 -0.0120 -0.0012 400  LEU A CB    
1778 C  CG    . LEU A 290 ? 0.2156 0.2816 0.2338 -0.0239 -0.0149 -0.0582 400  LEU A CG    
1779 C  CD1   . LEU A 290 ? 0.1952 0.2647 0.2481 -0.0115 -0.0031 -0.0714 400  LEU A CD1   
1780 C  CD2   . LEU A 290 ? 0.2273 0.2931 0.2379 -0.0272 -0.0394 -0.0330 400  LEU A CD2   
1781 N  N     . ALA A 291 ? 0.2173 0.3716 0.2932 -0.0086 -0.0587 -0.0045 401  ALA A N     
1782 C  CA    . ALA A 291 ? 0.2098 0.3821 0.2541 -0.0141 -0.0776 -0.0307 401  ALA A CA    
1783 C  C     . ALA A 291 ? 0.2729 0.4059 0.3013 -0.0087 -0.0599 -0.0180 401  ALA A C     
1784 O  O     . ALA A 291 ? 0.3536 0.4678 0.3009 0.0049  -0.0354 0.0300  401  ALA A O     
1785 C  CB    . ALA A 291 ? 0.2180 0.3943 0.2454 -0.0097 -0.0948 -0.0503 401  ALA A CB    
1786 N  N     . GLY A 292 ? 0.2586 0.4023 0.3049 -0.0279 -0.0751 -0.0918 402  GLY A N     
1787 C  CA    . GLY A 292 ? 0.2976 0.4299 0.3033 -0.0280 -0.1059 -0.0995 402  GLY A CA    
1788 C  C     . GLY A 292 ? 0.3308 0.4110 0.3238 -0.0037 -0.1268 -0.0930 402  GLY A C     
1789 O  O     . GLY A 292 ? 0.3636 0.4560 0.3686 0.0216  -0.1361 -0.1238 402  GLY A O     
1790 N  N     . THR A 293 ? 0.3159 0.3271 0.3055 0.0019  -0.1114 -0.0246 403  THR A N     
1791 C  CA    . THR A 293 ? 0.3259 0.2909 0.2904 -0.0014 -0.0967 -0.0060 403  THR A CA    
1792 C  C     . THR A 293 ? 0.3403 0.2959 0.2848 -0.0426 -0.1014 0.0009  403  THR A C     
1793 O  O     . THR A 293 ? 0.3437 0.3091 0.2789 -0.0401 -0.0962 -0.0344 403  THR A O     
1794 C  CB    . THR A 293 ? 0.3315 0.2711 0.2946 -0.0115 -0.0968 0.0133  403  THR A CB    
1795 O  OG1   . THR A 293 ? 0.3166 0.2874 0.2977 -0.0059 -0.1039 -0.0007 403  THR A OG1   
1796 C  CG2   . THR A 293 ? 0.3418 0.2545 0.2975 -0.0221 -0.0668 0.0225  403  THR A CG2   
1797 N  N     . ALA A 294 ? 0.3627 0.2896 0.2780 -0.0331 -0.1222 0.0252  404  ALA A N     
1798 C  CA    . ALA A 294 ? 0.3762 0.3111 0.2892 -0.0535 -0.1450 0.0035  404  ALA A CA    
1799 C  C     . ALA A 294 ? 0.3733 0.3153 0.2861 -0.0358 -0.0935 0.0189  404  ALA A C     
1800 O  O     . ALA A 294 ? 0.3659 0.3183 0.2757 -0.0118 -0.0947 0.0293  404  ALA A O     
1801 C  CB    . ALA A 294 ? 0.3922 0.3068 0.2934 -0.0700 -0.1517 0.0096  404  ALA A CB    
1802 N  N     . GLU A 295 ? 0.3475 0.3075 0.2614 -0.0579 -0.0904 -0.0005 405  GLU A N     
1803 C  CA    . GLU A 295 ? 0.3181 0.2946 0.2519 -0.0635 -0.0448 0.0197  405  GLU A CA    
1804 C  C     . GLU A 295 ? 0.3324 0.2764 0.2488 -0.0437 -0.0553 0.0136  405  GLU A C     
1805 O  O     . GLU A 295 ? 0.3532 0.2761 0.2526 -0.0535 -0.0496 0.0192  405  GLU A O     
1806 C  CB    . GLU A 295 ? 0.3086 0.3387 0.2686 -0.0540 -0.0567 0.0199  405  GLU A CB    
1807 C  CG    . GLU A 295 ? 0.3035 0.3358 0.2915 -0.0377 -0.0672 0.0331  405  GLU A CG    
1808 C  CD    . GLU A 295 ? 0.3062 0.3875 0.3069 -0.0384 -0.0809 0.0473  405  GLU A CD    
1809 O  OE1   . GLU A 295 ? 0.3210 0.4021 0.3081 -0.0567 -0.0538 0.0903  405  GLU A OE1   
1810 O  OE2   . GLU A 295 ? 0.3091 0.4006 0.3200 -0.0482 -0.0580 0.0056  405  GLU A OE2   
1811 N  N     . ALA A 296 ? 0.2910 0.2782 0.2473 -0.0315 -0.0519 0.0039  406  ALA A N     
1812 C  CA    . ALA A 296 ? 0.2777 0.2934 0.2638 -0.0256 -0.0595 0.0241  406  ALA A CA    
1813 C  C     . ALA A 296 ? 0.3423 0.3212 0.2640 -0.0462 -0.0579 0.0312  406  ALA A C     
1814 O  O     . ALA A 296 ? 0.4035 0.3705 0.2835 -0.0667 -0.0614 0.0225  406  ALA A O     
1815 C  CB    . ALA A 296 ? 0.2657 0.2990 0.2692 -0.0381 -0.0814 0.0125  406  ALA A CB    
1816 N  N     . PRO A 297 ? 0.3358 0.3042 0.2593 -0.0413 -0.0528 0.0462  407  PRO A N     
1817 C  CA    . PRO A 297 ? 0.3824 0.3196 0.2663 -0.0475 -0.0257 0.0308  407  PRO A CA    
1818 C  C     . PRO A 297 ? 0.4882 0.4043 0.3416 -0.0022 -0.0191 0.0270  407  PRO A C     
1819 O  O     . PRO A 297 ? 0.5238 0.3657 0.3711 0.0117  -0.0021 0.0319  407  PRO A O     
1820 C  CB    . PRO A 297 ? 0.3921 0.3252 0.2640 -0.0647 0.0089  0.0478  407  PRO A CB    
1821 C  CG    . PRO A 297 ? 0.3503 0.2937 0.2573 -0.0720 0.0079  0.0411  407  PRO A CG    
1822 C  CD    . PRO A 297 ? 0.3284 0.2465 0.2458 -0.0697 -0.0321 0.0517  407  PRO A CD    
1823 N  N     . GLY A 298 ? 0.5322 0.4865 0.3904 0.0142  -0.0192 0.0044  408  GLY A N     
1824 C  CA    . GLY A 298 ? 0.5703 0.5549 0.4161 -0.0146 -0.0238 -0.0551 408  GLY A CA    
1825 C  C     . GLY A 298 ? 0.6075 0.5878 0.4587 -0.0348 -0.0139 -0.0725 408  GLY A C     
1826 O  O     . GLY A 298 ? 0.5803 0.5905 0.4216 -0.0628 -0.0130 -0.0788 408  GLY A O     
1827 N  N     . GLU A 299 ? 0.6478 0.6003 0.5055 -0.0247 0.0017  -0.0653 409  GLU A N     
1828 C  CA    . GLU A 299 ? 0.6883 0.6169 0.5504 -0.0319 -0.0128 -0.0339 409  GLU A CA    
1829 C  C     . GLU A 299 ? 0.6702 0.5830 0.5501 -0.0285 -0.0397 -0.0362 409  GLU A C     
1830 O  O     . GLU A 299 ? 0.6526 0.5691 0.5493 -0.0368 -0.0645 -0.0292 409  GLU A O     
1831 C  CB    . GLU A 299 ? 0.7449 0.6701 0.5858 -0.0380 -0.0005 -0.0113 409  GLU A CB    
1832 C  CG    . GLU A 299 ? 0.7867 0.6961 0.6231 -0.0421 -0.0042 -0.0044 409  GLU A CG    
1833 C  CD    . GLU A 299 ? 0.8163 0.7144 0.6698 -0.0419 -0.0232 -0.0196 409  GLU A CD    
1834 O  OE1   . GLU A 299 ? 0.8200 0.7407 0.6848 -0.0434 -0.0379 -0.0216 409  GLU A OE1   
1835 O  OE2   . GLU A 299 ? 0.8331 0.7005 0.6904 -0.0441 -0.0242 -0.0266 409  GLU A OE2   
1836 N  N     . LEU A 300 ? 0.6730 0.5821 0.5443 0.0015  -0.0443 -0.0350 410  LEU A N     
1837 C  CA    . LEU A 300 ? 0.6874 0.5943 0.5289 0.0244  -0.0412 -0.0286 410  LEU A CA    
1838 C  C     . LEU A 300 ? 0.7052 0.5944 0.5251 0.0756  -0.0048 -0.0357 410  LEU A C     
1839 O  O     . LEU A 300 ? 0.7246 0.6015 0.5373 0.1018  0.0160  -0.0475 410  LEU A O     
1840 C  CB    . LEU A 300 ? 0.6948 0.6205 0.5345 0.0101  -0.0467 -0.0019 410  LEU A CB    
1841 C  CG    . LEU A 300 ? 0.6904 0.6546 0.5496 -0.0044 -0.0431 0.0051  410  LEU A CG    
1842 C  CD1   . LEU A 300 ? 0.7123 0.6665 0.5642 -0.0131 -0.0274 0.0320  410  LEU A CD1   
1843 C  CD2   . LEU A 300 ? 0.6640 0.6608 0.5503 0.0045  -0.0316 -0.0144 410  LEU A CD2   
1844 N  N     . ILE A 301 ? 0.6962 0.5934 0.5196 0.1083  -0.0007 -0.0388 411  ILE A N     
1845 C  CA    . ILE A 301 ? 0.6965 0.6068 0.5361 0.0998  -0.0029 -0.0304 411  ILE A CA    
1846 C  C     . ILE A 301 ? 0.7167 0.6081 0.5577 0.1348  -0.0010 -0.0471 411  ILE A C     
1847 O  O     . ILE A 301 ? 0.7264 0.6064 0.5396 0.1636  -0.0171 -0.0608 411  ILE A O     
1848 C  CB    . ILE A 301 ? 0.6661 0.5991 0.5433 0.0902  0.0042  -0.0199 411  ILE A CB    
1849 C  CG1   . ILE A 301 ? 0.6592 0.5886 0.5520 0.0809  0.0181  -0.0093 411  ILE A CG1   
1850 C  CG2   . ILE A 301 ? 0.6511 0.6085 0.5432 0.0770  0.0029  -0.0177 411  ILE A CG2   
1851 C  CD1   . ILE A 301 ? 0.6424 0.5720 0.5577 0.0856  0.0144  -0.0094 411  ILE A CD1   
1852 N  N     . PHE A 302 ? 0.7409 0.6365 0.6049 0.1426  0.0136  -0.0635 412  PHE A N     
1853 C  CA    . PHE A 302 ? 0.7458 0.6693 0.6473 0.1255  0.0162  -0.0631 412  PHE A CA    
1854 C  C     . PHE A 302 ? 0.8003 0.7245 0.6816 0.1178  0.0202  -0.0463 412  PHE A C     
1855 O  O     . PHE A 302 ? 0.8065 0.7304 0.6858 0.0868  0.0533  -0.0261 412  PHE A O     
1856 C  CB    . PHE A 302 ? 0.6978 0.6382 0.6417 0.0963  0.0181  -0.0768 412  PHE A CB    
1857 C  CG    . PHE A 302 ? 0.6713 0.5957 0.6279 0.0617  0.0298  -0.0803 412  PHE A CG    
1858 C  CD1   . PHE A 302 ? 0.6583 0.5750 0.6155 0.0537  0.0303  -0.0772 412  PHE A CD1   
1859 C  CD2   . PHE A 302 ? 0.6593 0.5571 0.6043 0.0391  0.0327  -0.1007 412  PHE A CD2   
1860 C  CE1   . PHE A 302 ? 0.6589 0.5591 0.6088 0.0246  0.0252  -0.0848 412  PHE A CE1   
1861 C  CE2   . PHE A 302 ? 0.6508 0.5429 0.5966 0.0330  0.0385  -0.0939 412  PHE A CE2   
1862 C  CZ    . PHE A 302 ? 0.6580 0.5531 0.6045 0.0339  0.0345  -0.0840 412  PHE A CZ    
1863 N  N     . VAL A 303 ? 0.8410 0.7716 0.7196 0.1358  0.0279  -0.0603 413  VAL A N     
1864 C  CA    . VAL A 303 ? 0.8751 0.8048 0.7556 0.1143  0.0172  -0.0491 413  VAL A CA    
1865 C  C     . VAL A 303 ? 0.8930 0.8244 0.7870 0.0953  0.0066  -0.0357 413  VAL A C     
1866 O  O     . VAL A 303 ? 0.8904 0.8261 0.7836 0.1082  0.0085  -0.0271 413  VAL A O     
1867 C  CB    . VAL A 303 ? 0.8831 0.8055 0.7590 0.1007  0.0080  -0.0488 413  VAL A CB    
1868 C  CG1   . VAL A 303 ? 0.9031 0.8049 0.7738 0.0960  -0.0033 -0.0405 413  VAL A CG1   
1869 C  CG2   . VAL A 303 ? 0.8710 0.8150 0.7522 0.0872  0.0107  -0.0503 413  VAL A CG2   
1870 N  N     . ASN A 304 ? 0.9205 0.8396 0.8150 0.0722  -0.0044 -0.0319 414  ASN A N     
1871 C  CA    . ASN A 304 ? 0.9244 0.8587 0.8330 0.0504  -0.0193 -0.0346 414  ASN A CA    
1872 C  C     . ASN A 304 ? 0.9085 0.8461 0.8148 0.0314  -0.0327 -0.0389 414  ASN A C     
1873 O  O     . ASN A 304 ? 0.9013 0.8416 0.8151 0.0246  -0.0230 -0.0362 414  ASN A O     
1874 C  CB    . ASN A 304 ? 0.9291 0.8962 0.8629 0.0515  -0.0204 -0.0420 414  ASN A CB    
1875 C  CG    . ASN A 304 ? 0.9373 0.9300 0.8816 0.0483  -0.0293 -0.0478 414  ASN A CG    
1876 O  OD1   . ASN A 304 ? 0.9444 0.9419 0.8895 0.0368  -0.0264 -0.0380 414  ASN A OD1   
1877 N  ND2   . ASN A 304 ? 0.9469 0.9444 0.8946 0.0572  -0.0381 -0.0555 414  ASN A ND2   
1878 N  N     . GLY A 305 ? 0.9057 0.8336 0.7954 0.0256  -0.0577 -0.0384 415  GLY A N     
1879 C  CA    . GLY A 305 ? 0.8985 0.7965 0.7665 0.0166  -0.0776 -0.0563 415  GLY A CA    
1880 C  C     . GLY A 305 ? 0.9034 0.7621 0.7491 0.0108  -0.0833 -0.0703 415  GLY A C     
1881 O  O     . GLY A 305 ? 0.9100 0.7366 0.7538 -0.0065 -0.0866 -0.0725 415  GLY A O     
1882 N  N     . LYS A 306 ? 0.9013 0.7419 0.7110 0.0210  -0.0896 -0.0885 416  LYS A N     
1883 C  CA    . LYS A 306 ? 0.8770 0.7170 0.6782 0.0226  -0.1074 -0.0939 416  LYS A CA    
1884 C  C     . LYS A 306 ? 0.8094 0.6502 0.5846 0.0341  -0.1248 -0.1105 416  LYS A C     
1885 O  O     . LYS A 306 ? 0.8279 0.6427 0.5638 0.0591  -0.1349 -0.1189 416  LYS A O     
1886 C  CB    . LYS A 306 ? 0.8986 0.7469 0.7235 0.0265  -0.1147 -0.0878 416  LYS A CB    
1887 C  CG    . LYS A 306 ? 0.9143 0.7794 0.7606 0.0252  -0.1126 -0.0849 416  LYS A CG    
1888 C  CD    . LYS A 306 ? 0.9255 0.8034 0.7877 0.0173  -0.1045 -0.0841 416  LYS A CD    
1889 C  CE    . LYS A 306 ? 0.9429 0.8312 0.8139 0.0107  -0.0964 -0.0745 416  LYS A CE    
1890 N  NZ    . LYS A 306 ? 0.9541 0.8445 0.8303 0.0105  -0.0884 -0.0722 416  LYS A NZ    
1891 N  N     . GLN A 307 ? 0.7313 0.6114 0.5230 0.0259  -0.1305 -0.1079 417  GLN A N     
1892 C  CA    . GLN A 307 ? 0.6567 0.5625 0.4550 0.0228  -0.1468 -0.1213 417  GLN A CA    
1893 C  C     . GLN A 307 ? 0.6064 0.5190 0.3790 -0.0019 -0.1618 -0.1669 417  GLN A C     
1894 O  O     . GLN A 307 ? 0.6201 0.5152 0.3578 -0.0200 -0.1655 -0.1865 417  GLN A O     
1895 C  CB    . GLN A 307 ? 0.6199 0.5667 0.4551 0.0144  -0.1560 -0.0889 417  GLN A CB    
1896 C  CG    . GLN A 307 ? 0.6139 0.5795 0.4850 0.0284  -0.1486 -0.0363 417  GLN A CG    
1897 C  CD    . GLN A 307 ? 0.6113 0.5828 0.5167 0.0407  -0.1551 0.0124  417  GLN A CD    
1898 O  OE1   . GLN A 307 ? 0.6087 0.5820 0.5159 0.0629  -0.1507 0.0262  417  GLN A OE1   
1899 N  NE2   . GLN A 307 ? 0.6215 0.5783 0.5368 0.0328  -0.1626 0.0447  417  GLN A NE2   
1900 N  N     . TYR A 308 ? 0.5424 0.4828 0.3605 0.0169  -0.1440 -0.1438 418  TYR A N     
1901 C  CA    . TYR A 308 ? 0.4840 0.4764 0.3732 0.0136  -0.1479 -0.1184 418  TYR A CA    
1902 C  C     . TYR A 308 ? 0.4250 0.4793 0.3678 -0.0061 -0.1273 -0.1037 418  TYR A C     
1903 O  O     . TYR A 308 ? 0.4122 0.4738 0.3607 0.0056  -0.1118 -0.0679 418  TYR A O     
1904 C  CB    . TYR A 308 ? 0.4998 0.4764 0.3919 0.0275  -0.1505 -0.1225 418  TYR A CB    
1905 C  CG    . TYR A 308 ? 0.5537 0.4798 0.4227 0.0354  -0.1158 -0.1392 418  TYR A CG    
1906 C  CD1   . TYR A 308 ? 0.5684 0.4863 0.4478 0.0343  -0.1046 -0.1301 418  TYR A CD1   
1907 C  CD2   . TYR A 308 ? 0.5869 0.4820 0.4432 0.0663  -0.1038 -0.1337 418  TYR A CD2   
1908 C  CE1   . TYR A 308 ? 0.6002 0.4951 0.4653 0.0621  -0.0929 -0.1249 418  TYR A CE1   
1909 C  CE2   . TYR A 308 ? 0.6206 0.4986 0.4687 0.0760  -0.0915 -0.1165 418  TYR A CE2   
1910 C  CZ    . TYR A 308 ? 0.6343 0.5021 0.4899 0.0829  -0.0813 -0.1072 418  TYR A CZ    
1911 O  OH    . TYR A 308 ? 0.6729 0.5164 0.5154 0.1002  -0.0735 -0.1062 418  TYR A OH    
1912 N  N     . LYS A 309 ? 0.3814 0.4468 0.3485 -0.0342 -0.1305 -0.1245 419  LYS A N     
1913 C  CA    . LYS A 309 ? 0.3454 0.4402 0.3403 -0.0298 -0.0994 -0.1039 419  LYS A CA    
1914 C  C     . LYS A 309 ? 0.3310 0.4144 0.2897 -0.0167 -0.0744 -0.0796 419  LYS A C     
1915 O  O     . LYS A 309 ? 0.3490 0.4270 0.2964 -0.0167 -0.0613 -0.0497 419  LYS A O     
1916 C  CB    . LYS A 309 ? 0.3674 0.4782 0.3651 -0.0333 -0.1133 -0.1059 419  LYS A CB    
1917 C  CG    . LYS A 309 ? 0.3827 0.5228 0.3873 -0.0256 -0.1157 -0.1057 419  LYS A CG    
1918 C  CD    . LYS A 309 ? 0.4242 0.5197 0.3955 -0.0076 -0.0929 -0.0837 419  LYS A CD    
1919 C  CE    . LYS A 309 ? 0.4563 0.5479 0.4188 -0.0080 -0.0831 -0.0513 419  LYS A CE    
1920 N  NZ    . LYS A 309 ? 0.4737 0.5469 0.4241 0.0113  -0.0532 -0.0257 419  LYS A NZ    
1921 N  N     . SER A 310 ? 0.3290 0.4241 0.2680 -0.0137 -0.0356 -0.0461 420  SER A N     
1922 C  CA    . SER A 310 ? 0.3401 0.4401 0.2641 -0.0549 -0.0199 -0.0323 420  SER A CA    
1923 C  C     . SER A 310 ? 0.3024 0.4157 0.2300 -0.0250 -0.0119 -0.0278 420  SER A C     
1924 O  O     . SER A 310 ? 0.3092 0.4142 0.2170 0.0083  -0.0356 -0.0278 420  SER A O     
1925 C  CB    . SER A 310 ? 0.3757 0.5025 0.3000 -0.0995 -0.0266 -0.0136 420  SER A CB    
1926 O  OG    . SER A 310 ? 0.4478 0.5444 0.3428 -0.1027 0.0158  0.0147  420  SER A OG    
1927 N  N     . TYR A 311 ? 0.2480 0.3531 0.1976 -0.0299 -0.0175 -0.0308 421  TYR A N     
1928 C  CA    . TYR A 311 ? 0.2566 0.3177 0.2306 -0.0389 -0.0034 -0.0078 421  TYR A CA    
1929 C  C     . TYR A 311 ? 0.2492 0.3287 0.2434 -0.0119 -0.0112 -0.0149 421  TYR A C     
1930 O  O     . TYR A 311 ? 0.2990 0.3064 0.2653 -0.0001 0.0054  -0.0256 421  TYR A O     
1931 C  CB    . TYR A 311 ? 0.2577 0.2792 0.2096 -0.0273 -0.0039 -0.0042 421  TYR A CB    
1932 C  CG    . TYR A 311 ? 0.2734 0.2690 0.1967 -0.0073 -0.0166 0.0022  421  TYR A CG    
1933 C  CD1   . TYR A 311 ? 0.2592 0.2923 0.1738 -0.0084 -0.0059 0.0269  421  TYR A CD1   
1934 C  CD2   . TYR A 311 ? 0.2685 0.2589 0.1825 -0.0069 -0.0023 -0.0314 421  TYR A CD2   
1935 C  CE1   . TYR A 311 ? 0.2469 0.2789 0.1636 -0.0107 -0.0137 0.0243  421  TYR A CE1   
1936 C  CE2   . TYR A 311 ? 0.2607 0.2503 0.1783 0.0036  -0.0027 -0.0319 421  TYR A CE2   
1937 C  CZ    . TYR A 311 ? 0.2441 0.2433 0.1684 0.0029  0.0000  -0.0179 421  TYR A CZ    
1938 O  OH    . TYR A 311 ? 0.2530 0.2177 0.2063 -0.0061 -0.0058 0.0174  421  TYR A OH    
1939 N  N     . ARG A 312 ? 0.2296 0.2946 0.2197 -0.0282 0.0286  -0.0008 422  ARG A N     
1940 C  CA    . ARG A 312 ? 0.2656 0.2861 0.2091 -0.0555 0.0298  -0.0041 422  ARG A CA    
1941 C  C     . ARG A 312 ? 0.2543 0.2679 0.2128 -0.0338 -0.0133 -0.0158 422  ARG A C     
1942 O  O     . ARG A 312 ? 0.2780 0.2797 0.2058 0.0007  0.0141  -0.0405 422  ARG A O     
1943 C  CB    . ARG A 312 ? 0.2911 0.2979 0.2188 -0.0207 0.0387  -0.0036 422  ARG A CB    
1944 C  CG    . ARG A 312 ? 0.3044 0.2672 0.2076 -0.0077 0.0366  0.0267  422  ARG A CG    
1945 C  CD    . ARG A 312 ? 0.3266 0.2763 0.2522 0.0285  0.0202  0.0231  422  ARG A CD    
1946 N  NE    . ARG A 312 ? 0.3152 0.3129 0.2678 0.0074  0.0041  0.0219  422  ARG A NE    
1947 C  CZ    . ARG A 312 ? 0.3257 0.3526 0.2777 0.0224  0.0132  0.0418  422  ARG A CZ    
1948 N  NH1   . ARG A 312 ? 0.3231 0.4389 0.2963 0.0045  0.0143  0.0468  422  ARG A NH1   
1949 N  NH2   . ARG A 312 ? 0.3297 0.3066 0.2982 0.0312  0.0079  0.0736  422  ARG A NH2   
1950 N  N     . GLY A 313 ? 0.2635 0.2567 0.2323 -0.0010 -0.0081 -0.0255 423  GLY A N     
1951 C  CA    . GLY A 313 ? 0.2470 0.2492 0.2108 0.0218  -0.0257 -0.0340 423  GLY A CA    
1952 C  C     . GLY A 313 ? 0.2483 0.2560 0.2232 0.0174  -0.0065 -0.0165 423  GLY A C     
1953 O  O     . GLY A 313 ? 0.2842 0.2857 0.2372 0.0093  -0.0397 0.0022  423  GLY A O     
1954 N  N     . MET A 314 ? 0.2380 0.2160 0.2239 -0.0246 -0.0046 -0.0119 424  MET A N     
1955 C  CA    . MET A 314 ? 0.2307 0.2263 0.2651 -0.0083 0.0193  -0.0266 424  MET A CA    
1956 C  C     . MET A 314 ? 0.2508 0.2346 0.2712 -0.0101 0.0043  -0.0095 424  MET A C     
1957 O  O     . MET A 314 ? 0.2789 0.2349 0.2960 -0.0244 0.0021  0.0142  424  MET A O     
1958 C  CB    . MET A 314 ? 0.2291 0.2629 0.2761 0.0018  -0.0152 -0.0026 424  MET A CB    
1959 C  CG    . MET A 314 ? 0.2135 0.2852 0.2504 0.0334  -0.0400 0.0742  424  MET A CG    
1960 S  SD    . MET A 314 ? 0.2677 0.3852 0.3173 -0.0150 -0.0250 0.0894  424  MET A SD    
1961 C  CE    . MET A 314 ? 0.2998 0.3566 0.3573 0.0492  -0.0611 0.0852  424  MET A CE    
1962 N  N     . GLY A 315 ? 0.1830 0.2864 0.2315 -0.0021 0.0339  -0.0013 425  GLY A N     
1963 C  CA    . GLY A 315 ? 0.1773 0.2796 0.2224 -0.0328 0.0421  0.0061  425  GLY A CA    
1964 C  C     . GLY A 315 ? 0.2304 0.2766 0.2517 -0.0231 0.0130  0.0081  425  GLY A C     
1965 O  O     . GLY A 315 ? 0.2623 0.2805 0.2429 -0.0158 0.0091  0.0126  425  GLY A O     
1966 N  N     . SER A 316 ? 0.2491 0.2800 0.2437 -0.0148 0.0199  0.0160  426  SER A N     
1967 C  CA    . SER A 316 ? 0.2658 0.2879 0.2451 -0.0162 0.0191  0.0256  426  SER A CA    
1968 C  C     . SER A 316 ? 0.2834 0.3324 0.2658 -0.0062 0.0463  0.0320  426  SER A C     
1969 O  O     . SER A 316 ? 0.2858 0.3374 0.2811 0.0116  0.0196  0.0525  426  SER A O     
1970 C  CB    . SER A 316 ? 0.3020 0.2872 0.2496 0.0154  0.0042  0.0330  426  SER A CB    
1971 O  OG    . SER A 316 ? 0.2963 0.3092 0.2366 0.0103  -0.0119 0.0573  426  SER A OG    
1972 N  N     . LEU A 317 ? 0.3169 0.3614 0.2699 -0.0404 0.0404  0.0535  427  LEU A N     
1973 C  CA    . LEU A 317 ? 0.3603 0.4115 0.3182 -0.0043 0.0867  0.0215  427  LEU A CA    
1974 C  C     . LEU A 317 ? 0.3755 0.3908 0.3461 -0.0103 0.0591  0.0573  427  LEU A C     
1975 O  O     . LEU A 317 ? 0.3989 0.4054 0.3490 -0.0202 0.0525  0.0733  427  LEU A O     
1976 C  CB    . LEU A 317 ? 0.4084 0.4670 0.3609 -0.0392 0.1361  -0.0114 427  LEU A CB    
1977 C  CG    . LEU A 317 ? 0.4751 0.5323 0.4236 -0.0149 0.1369  -0.0658 427  LEU A CG    
1978 C  CD1   . LEU A 317 ? 0.5075 0.5488 0.4509 -0.0129 0.1184  -0.0857 427  LEU A CD1   
1979 C  CD2   . LEU A 317 ? 0.4655 0.5400 0.4168 0.0083  0.1745  -0.0742 427  LEU A CD2   
1980 N  N     . GLY A 318 ? 0.3778 0.3868 0.3416 0.0184  0.0427  0.0709  428  GLY A N     
1981 C  CA    . GLY A 318 ? 0.3801 0.3897 0.3364 0.0218  0.0306  0.0722  428  GLY A CA    
1982 C  C     . GLY A 318 ? 0.3918 0.3757 0.3354 0.0358  0.0000  0.0865  428  GLY A C     
1983 O  O     . GLY A 318 ? 0.4208 0.3959 0.3556 0.0369  -0.0002 0.0815  428  GLY A O     
1984 N  N     . ALA A 319 ? 0.3685 0.3767 0.3320 0.0171  -0.0115 0.0845  429  ALA A N     
1985 C  CA    . ALA A 319 ? 0.3597 0.3638 0.3597 -0.0012 -0.0298 0.0819  429  ALA A CA    
1986 C  C     . ALA A 319 ? 0.4272 0.3990 0.4516 -0.0050 -0.0509 0.0482  429  ALA A C     
1987 O  O     . ALA A 319 ? 0.4320 0.3840 0.4958 -0.0035 -0.0581 0.0436  429  ALA A O     
1988 C  CB    . ALA A 319 ? 0.3252 0.3721 0.3312 -0.0140 -0.0149 0.0883  429  ALA A CB    
1989 N  N     . MET A 320 ? 0.4589 0.4363 0.4845 -0.0141 -0.0454 0.0110  430  MET A N     
1990 C  CA    . MET A 320 ? 0.5196 0.4927 0.5463 -0.0491 -0.0515 0.0079  430  MET A CA    
1991 C  C     . MET A 320 ? 0.6012 0.5685 0.6116 -0.0361 -0.0423 0.0111  430  MET A C     
1992 O  O     . MET A 320 ? 0.6182 0.5544 0.6140 -0.0079 -0.0279 0.0151  430  MET A O     
1993 C  CB    . MET A 320 ? 0.4875 0.4840 0.5575 -0.0877 -0.0748 -0.0082 430  MET A CB    
1994 C  CG    . MET A 320 ? 0.5100 0.5099 0.5678 -0.0825 -0.1105 -0.0169 430  MET A CG    
1995 S  SD    . MET A 320 ? 0.5642 0.5487 0.5854 -0.0761 -0.1157 -0.0228 430  MET A SD    
1996 C  CE    . MET A 320 ? 0.5538 0.5487 0.5503 -0.0525 -0.1089 -0.0383 430  MET A CE    
1997 N  N     . ARG A 321 ? 0.6780 0.6524 0.6779 -0.0268 -0.0384 0.0141  431  ARG A N     
1998 C  CA    . ARG A 321 ? 0.7417 0.7201 0.7481 -0.0152 -0.0239 0.0158  431  ARG A CA    
1999 C  C     . ARG A 321 ? 0.7635 0.7299 0.7612 -0.0074 -0.0289 0.0129  431  ARG A C     
2000 O  O     . ARG A 321 ? 0.7717 0.7420 0.7691 -0.0048 -0.0302 0.0016  431  ARG A O     
2001 C  CB    . ARG A 321 ? 0.7741 0.7712 0.7952 -0.0072 0.0003  0.0152  431  ARG A CB    
2002 C  CG    . ARG A 321 ? 0.8183 0.8229 0.8404 0.0077  0.0112  0.0053  431  ARG A CG    
2003 C  CD    . ARG A 321 ? 0.8538 0.8654 0.8771 0.0250  0.0131  0.0021  431  ARG A CD    
2004 N  NE    . ARG A 321 ? 0.8884 0.9050 0.9110 0.0414  0.0146  0.0061  431  ARG A NE    
2005 C  CZ    . ARG A 321 ? 0.9156 0.9334 0.9382 0.0450  0.0201  0.0119  431  ARG A CZ    
2006 N  NH1   . ARG A 321 ? 0.9353 0.9349 0.9269 0.0481  0.0247  -0.0041 431  ARG A NH1   
2007 N  NH2   . ARG A 321 ? 0.9138 0.9451 0.9636 0.0395  0.0213  0.0330  431  ARG A NH2   
2008 N  N     . LEU A 345 ? 0.6642 0.4366 0.5659 0.0304  -0.0277 0.0615  455  LEU A N     
2009 C  CA    . LEU A 345 ? 0.6032 0.4027 0.5618 0.0261  -0.0446 0.0713  455  LEU A CA    
2010 C  C     . LEU A 345 ? 0.5208 0.3870 0.5172 -0.0271 -0.0833 0.1075  455  LEU A C     
2011 O  O     . LEU A 345 ? 0.5804 0.4268 0.5491 -0.0486 -0.0827 0.1534  455  LEU A O     
2012 C  CB    . LEU A 345 ? 0.6202 0.4475 0.5990 0.0654  -0.0271 0.0120  455  LEU A CB    
2013 C  CG    . LEU A 345 ? 0.6416 0.5216 0.6478 0.0647  -0.0331 -0.0260 455  LEU A CG    
2014 C  CD1   . LEU A 345 ? 0.6452 0.5418 0.6695 0.0557  -0.0344 -0.0649 455  LEU A CD1   
2015 C  CD2   . LEU A 345 ? 0.6421 0.5340 0.6458 0.0782  -0.0412 -0.0165 455  LEU A CD2   
2016 N  N     . VAL A 346 ? 0.3599 0.3121 0.4492 -0.0586 -0.0794 0.0897  456  VAL A N     
2017 C  CA    . VAL A 346 ? 0.2715 0.3407 0.3703 -0.0184 -0.0393 0.0506  456  VAL A CA    
2018 C  C     . VAL A 346 ? 0.2535 0.3073 0.3065 -0.0044 -0.0076 0.0364  456  VAL A C     
2019 O  O     . VAL A 346 ? 0.2782 0.3018 0.3257 0.0024  -0.0437 0.0018  456  VAL A O     
2020 C  CB    . VAL A 346 ? 0.2560 0.4167 0.3488 -0.0143 -0.0160 0.0484  456  VAL A CB    
2021 C  CG1   . VAL A 346 ? 0.2567 0.4596 0.3378 -0.0356 -0.0363 0.0053  456  VAL A CG1   
2022 C  CG2   . VAL A 346 ? 0.2731 0.4080 0.3368 -0.0013 0.0047  0.0638  456  VAL A CG2   
2023 N  N     . PRO A 347 ? 0.2490 0.3323 0.2473 0.0340  0.0113  0.0288  457  PRO A N     
2024 C  CA    . PRO A 347 ? 0.2532 0.3222 0.2186 -0.0250 0.0250  0.0203  457  PRO A CA    
2025 C  C     . PRO A 347 ? 0.2562 0.3268 0.2086 0.0014  0.0366  0.0096  457  PRO A C     
2026 O  O     . PRO A 347 ? 0.2591 0.3632 0.2170 0.0080  0.0045  0.0261  457  PRO A O     
2027 C  CB    . PRO A 347 ? 0.3031 0.3778 0.2212 -0.0312 0.0701  0.0346  457  PRO A CB    
2028 C  CG    . PRO A 347 ? 0.3025 0.4251 0.2353 -0.0480 0.0408  0.0186  457  PRO A CG    
2029 C  CD    . PRO A 347 ? 0.2876 0.3988 0.2218 0.0004  0.0085  0.0271  457  PRO A CD    
2030 N  N     . GLU A 348 ? 0.2249 0.2713 0.2131 -0.0191 0.0321  0.0075  458  GLU A N     
2031 C  CA    . GLU A 348 ? 0.2197 0.2603 0.1690 -0.0140 -0.0016 -0.0120 458  GLU A CA    
2032 C  C     . GLU A 348 ? 0.2258 0.2660 0.1940 0.0094  0.0042  -0.0281 458  GLU A C     
2033 O  O     . GLU A 348 ? 0.2219 0.2779 0.1949 0.0360  -0.0124 -0.0102 458  GLU A O     
2034 C  CB    . GLU A 348 ? 0.2155 0.2464 0.1740 -0.0128 -0.0073 -0.0198 458  GLU A CB    
2035 C  CG    . GLU A 348 ? 0.2278 0.2564 0.1906 0.0065  -0.0226 -0.0205 458  GLU A CG    
2036 C  CD    . GLU A 348 ? 0.2375 0.2641 0.2423 0.0178  -0.0104 -0.0396 458  GLU A CD    
2037 O  OE1   . GLU A 348 ? 0.2498 0.2388 0.2485 0.0512  0.0013  -0.0116 458  GLU A OE1   
2038 O  OE2   . GLU A 348 ? 0.2399 0.2773 0.2404 0.0274  0.0086  -0.0340 458  GLU A OE2   
2039 N  N     . GLY A 349 ? 0.2172 0.2596 0.1871 0.0131  -0.0474 -0.0182 459  GLY A N     
2040 C  CA    . GLY A 349 ? 0.2569 0.2938 0.2196 0.0051  -0.0256 -0.0360 459  GLY A CA    
2041 C  C     . GLY A 349 ? 0.2954 0.3307 0.2249 0.0163  -0.0351 -0.0134 459  GLY A C     
2042 O  O     . GLY A 349 ? 0.3034 0.3112 0.2410 0.0238  -0.0176 0.0268  459  GLY A O     
2043 N  N     . ILE A 350 ? 0.3208 0.3480 0.2266 0.0454  -0.0254 -0.0383 460  ILE A N     
2044 C  CA    . ILE A 350 ? 0.3546 0.3805 0.2414 0.0370  -0.0431 -0.0331 460  ILE A CA    
2045 C  C     . ILE A 350 ? 0.2998 0.3741 0.2539 0.0115  -0.0325 -0.0255 460  ILE A C     
2046 O  O     . ILE A 350 ? 0.3021 0.3617 0.2211 0.0239  -0.0061 -0.0377 460  ILE A O     
2047 C  CB    . ILE A 350 ? 0.4117 0.4022 0.2760 0.0642  -0.0461 -0.0444 460  ILE A CB    
2048 C  CG1   . ILE A 350 ? 0.4591 0.3972 0.3069 0.0398  -0.0190 -0.0070 460  ILE A CG1   
2049 C  CG2   . ILE A 350 ? 0.4577 0.4392 0.2959 0.1003  -0.0792 -0.0655 460  ILE A CG2   
2050 C  CD1   . ILE A 350 ? 0.4873 0.4353 0.3151 0.0412  -0.0097 0.0127  460  ILE A CD1   
2051 N  N     . GLU A 351 ? 0.2847 0.3816 0.2588 0.0133  -0.0506 -0.0078 461  GLU A N     
2052 C  CA    . GLU A 351 ? 0.3344 0.4261 0.3180 0.0040  -0.0399 -0.0088 461  GLU A CA    
2053 C  C     . GLU A 351 ? 0.3094 0.4311 0.3302 0.0108  -0.0216 -0.0511 461  GLU A C     
2054 O  O     . GLU A 351 ? 0.3601 0.4472 0.3272 0.0134  0.0011  -0.0583 461  GLU A O     
2055 C  CB    . GLU A 351 ? 0.4057 0.4720 0.3665 -0.0114 -0.0291 -0.0111 461  GLU A CB    
2056 C  CG    . GLU A 351 ? 0.4585 0.5086 0.4085 -0.0045 -0.0096 -0.0118 461  GLU A CG    
2057 C  CD    . GLU A 351 ? 0.4772 0.5391 0.4553 0.0052  0.0057  -0.0048 461  GLU A CD    
2058 O  OE1   . GLU A 351 ? 0.5157 0.5580 0.4707 0.0162  0.0178  0.0007  461  GLU A OE1   
2059 O  OE2   . GLU A 351 ? 0.4444 0.5271 0.4767 0.0018  0.0122  0.0005  461  GLU A OE2   
2060 N  N     . GLY A 352 ? 0.2887 0.4249 0.3470 -0.0100 -0.0437 -0.0934 462  GLY A N     
2061 C  CA    . GLY A 352 ? 0.2936 0.4474 0.3915 0.0062  -0.0607 -0.0901 462  GLY A CA    
2062 C  C     . GLY A 352 ? 0.3157 0.4524 0.3875 0.0053  -0.0564 -0.0969 462  GLY A C     
2063 O  O     . GLY A 352 ? 0.3473 0.4321 0.3575 0.0258  -0.0178 -0.1054 462  GLY A O     
2064 N  N     . ARG A 353 ? 0.3404 0.4695 0.4220 -0.0284 -0.0758 -0.0980 463  ARG A N     
2065 C  CA    . ARG A 353 ? 0.3636 0.5020 0.4610 -0.0159 -0.0955 -0.0642 463  ARG A CA    
2066 C  C     . ARG A 353 ? 0.3752 0.4744 0.4477 -0.0170 -0.1126 -0.0524 463  ARG A C     
2067 O  O     . ARG A 353 ? 0.3820 0.4616 0.4901 -0.0258 -0.1161 -0.0186 463  ARG A O     
2068 C  CB    . ARG A 353 ? 0.3878 0.5441 0.5145 -0.0048 -0.1004 -0.0662 463  ARG A CB    
2069 C  CG    . ARG A 353 ? 0.4498 0.6004 0.5614 0.0261  -0.0763 -0.0667 463  ARG A CG    
2070 C  CD    . ARG A 353 ? 0.5170 0.6471 0.5978 0.0603  -0.0515 -0.0684 463  ARG A CD    
2071 N  NE    . ARG A 353 ? 0.6064 0.7006 0.6386 0.0850  -0.0292 -0.0611 463  ARG A NE    
2072 C  CZ    . ARG A 353 ? 0.6593 0.7242 0.6748 0.0995  -0.0134 -0.0584 463  ARG A CZ    
2073 N  NH1   . ARG A 353 ? 0.6715 0.7452 0.6860 0.0968  0.0040  -0.0507 463  ARG A NH1   
2074 N  NH2   . ARG A 353 ? 0.6900 0.7362 0.7087 0.1031  -0.0164 -0.0534 463  ARG A NH2   
2075 N  N     . VAL A 354 ? 0.3607 0.4605 0.3826 0.0090  -0.1302 -0.0775 464  VAL A N     
2076 C  CA    . VAL A 354 ? 0.3621 0.4233 0.3497 0.0248  -0.1099 -0.0542 464  VAL A CA    
2077 C  C     . VAL A 354 ? 0.3524 0.4110 0.3597 0.0248  -0.1178 -0.0719 464  VAL A C     
2078 O  O     . VAL A 354 ? 0.3432 0.4422 0.3607 0.0331  -0.1056 -0.0882 464  VAL A O     
2079 C  CB    . VAL A 354 ? 0.3683 0.4221 0.3154 0.0051  -0.0925 -0.0465 464  VAL A CB    
2080 C  CG1   . VAL A 354 ? 0.3906 0.4090 0.2754 -0.0083 -0.1211 -0.0636 464  VAL A CG1   
2081 C  CG2   . VAL A 354 ? 0.3693 0.4271 0.3249 -0.0021 -0.0263 -0.0424 464  VAL A CG2   
2082 N  N     . PRO A 355 ? 0.3670 0.4178 0.3873 0.0442  -0.1352 -0.0694 465  PRO A N     
2083 C  CA    . PRO A 355 ? 0.3716 0.4278 0.4040 0.0474  -0.1625 -0.0769 465  PRO A CA    
2084 C  C     . PRO A 355 ? 0.3811 0.4358 0.4036 0.0496  -0.1414 -0.0803 465  PRO A C     
2085 O  O     . PRO A 355 ? 0.3869 0.4402 0.4037 0.0336  -0.1492 -0.0826 465  PRO A O     
2086 C  CB    . PRO A 355 ? 0.3916 0.4545 0.4125 0.0286  -0.1752 -0.0648 465  PRO A CB    
2087 C  CG    . PRO A 355 ? 0.4243 0.4716 0.4216 -0.0065 -0.1524 -0.0651 465  PRO A CG    
2088 C  CD    . PRO A 355 ? 0.3803 0.4370 0.4069 0.0026  -0.1298 -0.0671 465  PRO A CD    
2089 N  N     . PHE A 356 ? 0.3601 0.4280 0.3735 0.0381  -0.1462 -0.0779 466  PHE A N     
2090 C  CA    . PHE A 356 ? 0.3611 0.4396 0.3633 0.0304  -0.1290 -0.0469 466  PHE A CA    
2091 C  C     . PHE A 356 ? 0.3883 0.4503 0.3414 0.0348  -0.0918 -0.0217 466  PHE A C     
2092 O  O     . PHE A 356 ? 0.3951 0.4448 0.3196 0.0001  -0.0612 -0.0257 466  PHE A O     
2093 C  CB    . PHE A 356 ? 0.3465 0.4565 0.3650 0.0289  -0.1104 -0.0026 466  PHE A CB    
2094 C  CG    . PHE A 356 ? 0.3189 0.4832 0.3647 -0.0115 -0.1230 0.0159  466  PHE A CG    
2095 C  CD1   . PHE A 356 ? 0.3161 0.4897 0.3768 -0.0215 -0.1298 0.0177  466  PHE A CD1   
2096 C  CD2   . PHE A 356 ? 0.3202 0.4937 0.3661 -0.0172 -0.1232 0.0638  466  PHE A CD2   
2097 C  CE1   . PHE A 356 ? 0.3191 0.5217 0.3899 -0.0506 -0.1231 0.0095  466  PHE A CE1   
2098 C  CE2   . PHE A 356 ? 0.3098 0.5130 0.3653 -0.0440 -0.1237 0.0557  466  PHE A CE2   
2099 C  CZ    . PHE A 356 ? 0.3087 0.5206 0.3798 -0.0564 -0.1272 0.0412  466  PHE A CZ    
2100 N  N     . ARG A 357 ? 0.3972 0.4548 0.3436 0.0654  -0.0998 -0.0179 467  ARG A N     
2101 C  CA    . ARG A 357 ? 0.4390 0.4746 0.3763 0.0508  -0.0890 -0.0075 467  ARG A CA    
2102 C  C     . ARG A 357 ? 0.4000 0.4019 0.3633 0.0130  -0.0739 0.0126  467  ARG A C     
2103 O  O     . ARG A 357 ? 0.4490 0.3984 0.3910 0.0278  -0.0430 0.0350  467  ARG A O     
2104 C  CB    . ARG A 357 ? 0.5016 0.5572 0.4525 0.0806  -0.0789 0.0168  467  ARG A CB    
2105 C  CG    . ARG A 357 ? 0.5625 0.6043 0.5311 0.0724  -0.0680 0.0128  467  ARG A CG    
2106 C  CD    . ARG A 357 ? 0.6123 0.6378 0.6008 0.0565  -0.0597 -0.0074 467  ARG A CD    
2107 N  NE    . ARG A 357 ? 0.6622 0.6834 0.6559 0.0350  -0.0708 -0.0328 467  ARG A NE    
2108 C  CZ    . ARG A 357 ? 0.6992 0.7056 0.7073 0.0408  -0.0847 -0.0403 467  ARG A CZ    
2109 N  NH1   . ARG A 357 ? 0.7191 0.7321 0.7190 0.0557  -0.0955 -0.0405 467  ARG A NH1   
2110 N  NH2   . ARG A 357 ? 0.6997 0.6743 0.7258 0.0361  -0.0918 -0.0410 467  ARG A NH2   
2111 N  N     . GLY A 358 ? 0.3584 0.3407 0.3150 -0.0158 -0.0827 0.0244  468  GLY A N     
2112 C  CA    . GLY A 358 ? 0.3399 0.3307 0.2961 -0.0322 -0.0988 0.0251  468  GLY A CA    
2113 C  C     . GLY A 358 ? 0.3271 0.3423 0.2699 -0.0556 -0.0926 0.0556  468  GLY A C     
2114 O  O     . GLY A 358 ? 0.3239 0.3583 0.2654 -0.0697 -0.0994 0.0639  468  GLY A O     
2115 N  N     . PRO A 359 ? 0.3043 0.3318 0.2678 -0.0889 -0.0937 0.0561  469  PRO A N     
2116 C  CA    . PRO A 359 ? 0.3116 0.3539 0.2639 -0.0777 -0.0898 0.0926  469  PRO A CA    
2117 C  C     . PRO A 359 ? 0.3370 0.3607 0.2523 -0.0551 -0.0910 0.1000  469  PRO A C     
2118 O  O     . PRO A 359 ? 0.3553 0.3743 0.2977 -0.0781 -0.0767 0.1050  469  PRO A O     
2119 C  CB    . PRO A 359 ? 0.2992 0.3909 0.2770 -0.0809 -0.1282 0.0606  469  PRO A CB    
2120 C  CG    . PRO A 359 ? 0.3259 0.3932 0.3209 -0.0871 -0.1232 0.0503  469  PRO A CG    
2121 C  CD    . PRO A 359 ? 0.3011 0.3433 0.2973 -0.0624 -0.1207 0.0580  469  PRO A CD    
2122 N  N     . LEU A 360 ? 0.3282 0.3608 0.2123 -0.0177 -0.0943 0.0926  470  LEU A N     
2123 C  CA    . LEU A 360 ? 0.3382 0.3863 0.2352 -0.0031 -0.0766 0.1090  470  LEU A CA    
2124 C  C     . LEU A 360 ? 0.3063 0.4331 0.2643 0.0120  -0.0404 0.1206  470  LEU A C     
2125 O  O     . LEU A 360 ? 0.3114 0.4051 0.2321 0.0037  -0.0201 0.1219  470  LEU A O     
2126 C  CB    . LEU A 360 ? 0.3568 0.4017 0.2345 0.0161  -0.1280 0.0841  470  LEU A CB    
2127 C  CG    . LEU A 360 ? 0.3759 0.4262 0.2715 0.0425  -0.1732 0.0563  470  LEU A CG    
2128 C  CD1   . LEU A 360 ? 0.3076 0.3966 0.2991 0.0558  -0.1634 0.0582  470  LEU A CD1   
2129 C  CD2   . LEU A 360 ? 0.4317 0.4059 0.2889 0.0453  -0.1862 0.0258  470  LEU A CD2   
2130 N  N     . SER A 361 ? 0.2891 0.4862 0.3075 0.0339  -0.0375 0.1370  471  SER A N     
2131 C  CA    . SER A 361 ? 0.3132 0.5357 0.3354 0.0165  -0.0678 0.1459  471  SER A CA    
2132 C  C     . SER A 361 ? 0.3139 0.5162 0.3484 -0.0084 -0.0614 0.1592  471  SER A C     
2133 O  O     . SER A 361 ? 0.3184 0.5362 0.3573 0.0245  -0.0625 0.1751  471  SER A O     
2134 C  CB    . SER A 361 ? 0.3411 0.5891 0.3519 0.0347  -0.0922 0.1251  471  SER A CB    
2135 O  OG    . SER A 361 ? 0.3811 0.6341 0.3714 0.0284  -0.1155 0.1283  471  SER A OG    
2136 N  N     . SER A 362 ? 0.3285 0.4976 0.3207 -0.0557 -0.0971 0.1413  472  SER A N     
2137 C  CA    . SER A 362 ? 0.3562 0.5001 0.3149 -0.0472 -0.1014 0.0909  472  SER A CA    
2138 C  C     . SER A 362 ? 0.3603 0.4635 0.2843 -0.0534 -0.0808 0.0523  472  SER A C     
2139 O  O     . SER A 362 ? 0.3828 0.4549 0.2933 -0.0407 -0.1014 0.0698  472  SER A O     
2140 C  CB    . SER A 362 ? 0.3744 0.5402 0.3400 -0.0242 -0.1165 0.0782  472  SER A CB    
2141 O  OG    . SER A 362 ? 0.4256 0.5462 0.3800 -0.0245 -0.0783 0.0585  472  SER A OG    
2142 N  N     . VAL A 363 ? 0.3213 0.4067 0.2422 -0.0747 -0.0364 0.0232  473  VAL A N     
2143 C  CA    . VAL A 363 ? 0.2958 0.3446 0.2115 -0.0929 -0.0417 0.0351  473  VAL A CA    
2144 C  C     . VAL A 363 ? 0.2881 0.3255 0.2229 -0.0386 -0.0527 0.0545  473  VAL A C     
2145 O  O     . VAL A 363 ? 0.2856 0.3367 0.2458 -0.0499 -0.0633 0.0841  473  VAL A O     
2146 C  CB    . VAL A 363 ? 0.3140 0.3632 0.2134 -0.0974 -0.0149 0.0201  473  VAL A CB    
2147 C  CG1   . VAL A 363 ? 0.2778 0.3595 0.2173 -0.1080 -0.0039 0.0056  473  VAL A CG1   
2148 C  CG2   . VAL A 363 ? 0.3597 0.3605 0.2490 -0.1119 -0.0243 0.0234  473  VAL A CG2   
2149 N  N     . ILE A 364 ? 0.2607 0.2892 0.2122 -0.0020 -0.0544 0.0409  474  ILE A N     
2150 C  CA    . ILE A 364 ? 0.2829 0.2735 0.2255 0.0404  -0.0479 0.0351  474  ILE A CA    
2151 C  C     . ILE A 364 ? 0.2940 0.2892 0.2346 0.0263  -0.0665 0.0513  474  ILE A C     
2152 O  O     . ILE A 364 ? 0.2916 0.2903 0.2131 0.0338  -0.0402 0.0589  474  ILE A O     
2153 C  CB    . ILE A 364 ? 0.3296 0.2755 0.2525 -0.0001 -0.0204 0.0464  474  ILE A CB    
2154 C  CG1   . ILE A 364 ? 0.3164 0.3081 0.2922 0.0021  -0.0594 0.0643  474  ILE A CG1   
2155 C  CG2   . ILE A 364 ? 0.3527 0.2875 0.2640 0.0284  -0.0011 0.0277  474  ILE A CG2   
2156 C  CD1   . ILE A 364 ? 0.3358 0.3067 0.3188 -0.0222 -0.0815 0.0405  474  ILE A CD1   
2157 N  N     . HIS A 365 ? 0.3019 0.3186 0.2706 -0.0152 -0.0601 0.0560  475  HIS A N     
2158 C  CA    . HIS A 365 ? 0.3122 0.3592 0.2826 -0.0444 -0.0936 0.0259  475  HIS A CA    
2159 C  C     . HIS A 365 ? 0.3058 0.3331 0.2653 -0.0455 -0.0499 0.0408  475  HIS A C     
2160 O  O     . HIS A 365 ? 0.2736 0.3246 0.2799 -0.0511 -0.0201 0.0240  475  HIS A O     
2161 C  CB    . HIS A 365 ? 0.3354 0.4206 0.3553 -0.0878 -0.0938 0.0413  475  HIS A CB    
2162 C  CG    . HIS A 365 ? 0.4168 0.5065 0.4354 -0.0581 -0.0828 0.0408  475  HIS A CG    
2163 N  ND1   . HIS A 365 ? 0.4398 0.5393 0.4635 -0.0644 -0.0811 0.0434  475  HIS A ND1   
2164 C  CD2   . HIS A 365 ? 0.4327 0.5093 0.4671 -0.0585 -0.0777 0.0301  475  HIS A CD2   
2165 C  CE1   . HIS A 365 ? 0.4543 0.5414 0.4725 -0.0755 -0.0789 0.0411  475  HIS A CE1   
2166 N  NE2   . HIS A 365 ? 0.4434 0.5272 0.4767 -0.0437 -0.0885 0.0314  475  HIS A NE2   
2167 N  N     . GLN A 366 ? 0.3201 0.3169 0.2724 -0.0353 -0.0574 0.0252  476  GLN A N     
2168 C  CA    . GLN A 366 ? 0.3470 0.3315 0.2808 -0.0449 -0.0317 -0.0168 476  GLN A CA    
2169 C  C     . GLN A 366 ? 0.3036 0.2720 0.2471 -0.0325 -0.0500 -0.0091 476  GLN A C     
2170 O  O     . GLN A 366 ? 0.3060 0.2553 0.2786 -0.0159 -0.0378 -0.0371 476  GLN A O     
2171 C  CB    . GLN A 366 ? 0.4056 0.3840 0.2917 -0.0555 -0.0197 -0.0284 476  GLN A CB    
2172 C  CG    . GLN A 366 ? 0.4628 0.4330 0.3534 -0.0834 -0.0213 -0.0332 476  GLN A CG    
2173 C  CD    . GLN A 366 ? 0.5114 0.4710 0.3993 -0.0774 -0.0371 -0.0223 476  GLN A CD    
2174 O  OE1   . GLN A 366 ? 0.5451 0.4519 0.4486 -0.0796 -0.0314 -0.0706 476  GLN A OE1   
2175 N  NE2   . GLN A 366 ? 0.5345 0.5208 0.3890 -0.0788 -0.0537 0.0256  476  GLN A NE2   
2176 N  N     . LEU A 367 ? 0.2894 0.2101 0.2175 -0.0228 -0.0471 -0.0064 477  LEU A N     
2177 C  CA    . LEU A 367 ? 0.2655 0.2092 0.2215 -0.0463 -0.0122 0.0032  477  LEU A CA    
2178 C  C     . LEU A 367 ? 0.2572 0.2294 0.2341 -0.0333 -0.0109 0.0224  477  LEU A C     
2179 O  O     . LEU A 367 ? 0.2512 0.2202 0.2099 -0.0129 -0.0382 0.0056  477  LEU A O     
2180 C  CB    . LEU A 367 ? 0.2603 0.1935 0.2606 -0.0405 0.0041  0.0331  477  LEU A CB    
2181 C  CG    . LEU A 367 ? 0.2399 0.1898 0.2721 -0.0139 0.0034  0.0407  477  LEU A CG    
2182 C  CD1   . LEU A 367 ? 0.2543 0.2152 0.3018 -0.0412 -0.0362 0.0588  477  LEU A CD1   
2183 C  CD2   . LEU A 367 ? 0.2368 0.2162 0.2719 0.0169  0.0121  0.0359  477  LEU A CD2   
2184 N  N     . THR A 368 ? 0.2420 0.2277 0.2474 -0.0056 0.0206  0.0518  478  THR A N     
2185 C  CA    . THR A 368 ? 0.2558 0.2219 0.2538 -0.0068 -0.0005 0.0316  478  THR A CA    
2186 C  C     . THR A 368 ? 0.2413 0.2235 0.2534 -0.0166 -0.0077 0.0349  478  THR A C     
2187 O  O     . THR A 368 ? 0.2170 0.2500 0.2234 -0.0011 -0.0226 0.0235  478  THR A O     
2188 C  CB    . THR A 368 ? 0.2886 0.2480 0.2815 -0.0305 -0.0414 0.0187  478  THR A CB    
2189 O  OG1   . THR A 368 ? 0.3312 0.3280 0.3584 0.0028  -0.0227 0.0277  478  THR A OG1   
2190 C  CG2   . THR A 368 ? 0.2713 0.1770 0.2472 -0.0240 -0.0081 0.0358  478  THR A CG2   
2191 N  N     . GLY A 369 ? 0.2540 0.1660 0.2608 -0.0192 -0.0352 0.0254  479  GLY A N     
2192 C  CA    . GLY A 369 ? 0.2492 0.2072 0.2925 -0.0424 -0.0408 -0.0044 479  GLY A CA    
2193 C  C     . GLY A 369 ? 0.2262 0.2057 0.2764 -0.0356 -0.0214 0.0160  479  GLY A C     
2194 O  O     . GLY A 369 ? 0.2219 0.2106 0.2846 -0.0242 -0.0302 0.0166  479  GLY A O     
2195 N  N     . GLY A 370 ? 0.2155 0.2198 0.2458 -0.0311 -0.0445 -0.0039 480  GLY A N     
2196 C  CA    . GLY A 370 ? 0.2080 0.2222 0.2263 0.0091  -0.0218 -0.0229 480  GLY A CA    
2197 C  C     . GLY A 370 ? 0.1888 0.2183 0.2295 0.0115  -0.0121 -0.0075 480  GLY A C     
2198 O  O     . GLY A 370 ? 0.1947 0.2241 0.2464 0.0184  -0.0133 0.0010  480  GLY A O     
2199 N  N     . LEU A 371 ? 0.1911 0.1954 0.2343 0.0025  -0.0089 -0.0205 481  LEU A N     
2200 C  CA    . LEU A 371 ? 0.2173 0.1829 0.2238 -0.0156 0.0143  -0.0350 481  LEU A CA    
2201 C  C     . LEU A 371 ? 0.1881 0.1929 0.2320 -0.0342 0.0140  0.0078  481  LEU A C     
2202 O  O     . LEU A 371 ? 0.1866 0.2048 0.2380 -0.0087 -0.0198 -0.0039 481  LEU A O     
2203 C  CB    . LEU A 371 ? 0.2408 0.1844 0.2302 -0.0108 0.0225  -0.0243 481  LEU A CB    
2204 C  CG    . LEU A 371 ? 0.2301 0.1584 0.2289 -0.0024 -0.0095 0.0163  481  LEU A CG    
2205 C  CD1   . LEU A 371 ? 0.2449 0.2179 0.2426 -0.0076 -0.0351 0.0268  481  LEU A CD1   
2206 C  CD2   . LEU A 371 ? 0.2385 0.1496 0.2348 0.0152  -0.0155 0.0122  481  LEU A CD2   
2207 N  N     . ARG A 372 ? 0.1602 0.1967 0.2475 -0.0256 -0.0025 0.0486  482  ARG A N     
2208 C  CA    . ARG A 372 ? 0.1658 0.1904 0.2836 0.0183  -0.0341 0.0484  482  ARG A CA    
2209 C  C     . ARG A 372 ? 0.2058 0.1936 0.2764 -0.0086 -0.0130 0.0418  482  ARG A C     
2210 O  O     . ARG A 372 ? 0.2111 0.1727 0.2599 -0.0326 -0.0516 0.0258  482  ARG A O     
2211 C  CB    . ARG A 372 ? 0.1804 0.1731 0.3208 0.0477  -0.0284 0.0616  482  ARG A CB    
2212 C  CG    . ARG A 372 ? 0.1667 0.2124 0.3911 0.0617  -0.0477 0.0591  482  ARG A CG    
2213 C  CD    . ARG A 372 ? 0.2086 0.2078 0.4362 0.0603  -0.0357 0.0557  482  ARG A CD    
2214 N  NE    . ARG A 372 ? 0.2457 0.2834 0.4517 0.0603  -0.0317 0.0311  482  ARG A NE    
2215 C  CZ    . ARG A 372 ? 0.2459 0.3106 0.4610 0.0744  -0.0053 0.0609  482  ARG A CZ    
2216 N  NH1   . ARG A 372 ? 0.2832 0.3406 0.4711 0.0750  0.0225  0.0385  482  ARG A NH1   
2217 N  NH2   . ARG A 372 ? 0.2891 0.3231 0.4750 0.0458  -0.0165 0.0755  482  ARG A NH2   
2218 N  N     . ALA A 373 ? 0.1922 0.1580 0.2516 0.0084  -0.0170 0.0256  483  ALA A N     
2219 C  CA    . ALA A 373 ? 0.2161 0.1835 0.2502 0.0171  -0.0273 -0.0077 483  ALA A CA    
2220 C  C     . ALA A 373 ? 0.1905 0.1737 0.2740 0.0044  -0.0204 0.0259  483  ALA A C     
2221 O  O     . ALA A 373 ? 0.1860 0.1874 0.3060 0.0108  -0.0223 -0.0130 483  ALA A O     
2222 C  CB    . ALA A 373 ? 0.2519 0.1893 0.2527 0.0210  -0.0553 -0.0019 483  ALA A CB    
2223 N  N     . ALA A 374 ? 0.1484 0.1948 0.2148 -0.0211 -0.0292 0.0173  484  ALA A N     
2224 C  CA    . ALA A 374 ? 0.1564 0.1950 0.2116 -0.0253 -0.0227 0.0029  484  ALA A CA    
2225 C  C     . ALA A 374 ? 0.1607 0.1854 0.2230 0.0153  -0.0084 0.0057  484  ALA A C     
2226 O  O     . ALA A 374 ? 0.1961 0.1720 0.2488 0.0026  -0.0340 0.0178  484  ALA A O     
2227 C  CB    . ALA A 374 ? 0.1734 0.2225 0.2263 -0.0157 0.0006  0.0098  484  ALA A CB    
2228 N  N     . MET A 375 ? 0.1687 0.1717 0.2417 0.0172  0.0157  0.0014  485  MET A N     
2229 C  CA    . MET A 375 ? 0.1918 0.1678 0.2683 0.0343  0.0135  0.0065  485  MET A CA    
2230 C  C     . MET A 375 ? 0.2014 0.1881 0.2516 0.0113  0.0355  -0.0234 485  MET A C     
2231 O  O     . MET A 375 ? 0.1868 0.1891 0.2564 -0.0163 0.0283  -0.0248 485  MET A O     
2232 C  CB    . MET A 375 ? 0.1902 0.1447 0.2746 -0.0218 0.0236  0.0352  485  MET A CB    
2233 C  CG    . MET A 375 ? 0.2282 0.1341 0.2560 -0.0091 0.0153  0.0392  485  MET A CG    
2234 S  SD    . MET A 375 ? 0.2048 0.1827 0.2513 -0.0040 0.0218  0.0082  485  MET A SD    
2235 C  CE    . MET A 375 ? 0.2759 0.1958 0.2599 -0.0041 0.0378  0.0070  485  MET A CE    
2236 N  N     . GLY A 376 ? 0.1975 0.1938 0.2454 0.0049  0.0288  -0.0179 486  GLY A N     
2237 C  CA    . GLY A 376 ? 0.1860 0.1667 0.2610 0.0119  0.0103  0.0037  486  GLY A CA    
2238 C  C     . GLY A 376 ? 0.1836 0.1874 0.2272 0.0175  -0.0035 0.0099  486  GLY A C     
2239 O  O     . GLY A 376 ? 0.2006 0.1798 0.2315 -0.0063 -0.0048 0.0368  486  GLY A O     
2240 N  N     . TYR A 377 ? 0.1519 0.1927 0.2173 -0.0058 -0.0106 0.0021  487  TYR A N     
2241 C  CA    . TYR A 377 ? 0.1716 0.1991 0.1979 0.0282  0.0124  0.0059  487  TYR A CA    
2242 C  C     . TYR A 377 ? 0.1955 0.2253 0.2141 -0.0133 0.0140  -0.0017 487  TYR A C     
2243 O  O     . TYR A 377 ? 0.1911 0.2114 0.2187 -0.0230 0.0166  0.0057  487  TYR A O     
2244 C  CB    . TYR A 377 ? 0.1734 0.2059 0.1996 0.0369  0.0320  -0.0246 487  TYR A CB    
2245 C  CG    . TYR A 377 ? 0.1876 0.1975 0.2114 0.0061  -0.0042 -0.0394 487  TYR A CG    
2246 C  CD1   . TYR A 377 ? 0.1955 0.2123 0.2163 0.0191  -0.0075 -0.0512 487  TYR A CD1   
2247 C  CD2   . TYR A 377 ? 0.1791 0.1936 0.2333 0.0060  0.0012  -0.0377 487  TYR A CD2   
2248 C  CE1   . TYR A 377 ? 0.1836 0.2150 0.2560 -0.0113 0.0063  -0.0173 487  TYR A CE1   
2249 C  CE2   . TYR A 377 ? 0.1873 0.2061 0.2376 0.0071  -0.0257 -0.0268 487  TYR A CE2   
2250 C  CZ    . TYR A 377 ? 0.2123 0.2109 0.2539 -0.0186 -0.0171 -0.0472 487  TYR A CZ    
2251 O  OH    . TYR A 377 ? 0.2240 0.2015 0.2739 -0.0412 -0.0226 -0.0270 487  TYR A OH    
2252 N  N     . THR A 378 ? 0.1818 0.2124 0.2205 -0.0001 -0.0057 -0.0207 488  THR A N     
2253 C  CA    . THR A 378 ? 0.1565 0.1786 0.2024 -0.0378 0.0202  -0.0231 488  THR A CA    
2254 C  C     . THR A 378 ? 0.1852 0.2011 0.2201 -0.0177 -0.0081 -0.0081 488  THR A C     
2255 O  O     . THR A 378 ? 0.2135 0.2218 0.1846 -0.0081 0.0015  0.0176  488  THR A O     
2256 C  CB    . THR A 378 ? 0.1442 0.1779 0.2192 0.0127  0.0212  -0.0030 488  THR A CB    
2257 O  OG1   . THR A 378 ? 0.1786 0.2010 0.2420 0.0164  0.0098  -0.0104 488  THR A OG1   
2258 C  CG2   . THR A 378 ? 0.1449 0.2173 0.2251 0.0095  0.0249  0.0333  488  THR A CG2   
2259 N  N     . GLY A 379 ? 0.1606 0.2069 0.2338 0.0038  0.0325  0.0051  489  GLY A N     
2260 C  CA    . GLY A 379 ? 0.1742 0.2024 0.2392 0.0265  0.0482  0.0037  489  GLY A CA    
2261 C  C     . GLY A 379 ? 0.2277 0.1924 0.2398 0.0123  0.0455  0.0017  489  GLY A C     
2262 O  O     . GLY A 379 ? 0.2839 0.2041 0.2449 0.0345  0.0793  0.0113  489  GLY A O     
2263 N  N     . SER A 380 ? 0.2032 0.1789 0.2646 -0.0158 0.0354  0.0203  490  SER A N     
2264 C  CA    . SER A 380 ? 0.1877 0.1798 0.2720 -0.0067 0.0334  0.0050  490  SER A CA    
2265 C  C     . SER A 380 ? 0.2047 0.2114 0.2700 -0.0040 0.0336  -0.0134 490  SER A C     
2266 O  O     . SER A 380 ? 0.2113 0.2200 0.2764 0.0093  0.0066  -0.0138 490  SER A O     
2267 C  CB    . SER A 380 ? 0.1834 0.2172 0.2581 0.0109  0.0157  0.0161  490  SER A CB    
2268 O  OG    . SER A 380 ? 0.1879 0.2433 0.2459 -0.0016 0.0246  -0.0149 490  SER A OG    
2269 N  N     . PRO A 381 ? 0.2151 0.2152 0.2927 0.0174  0.0555  -0.0169 491  PRO A N     
2270 C  CA    . PRO A 381 ? 0.2279 0.2332 0.3084 0.0066  0.0533  -0.0037 491  PRO A CA    
2271 C  C     . PRO A 381 ? 0.2325 0.2047 0.3243 0.0183  0.0432  0.0213  491  PRO A C     
2272 O  O     . PRO A 381 ? 0.2661 0.1794 0.3591 -0.0102 0.0359  0.0326  491  PRO A O     
2273 C  CB    . PRO A 381 ? 0.2435 0.2674 0.3174 -0.0110 0.0515  -0.0004 491  PRO A CB    
2274 C  CG    . PRO A 381 ? 0.2664 0.2877 0.3329 0.0337  0.0816  0.0050  491  PRO A CG    
2275 C  CD    . PRO A 381 ? 0.2298 0.2593 0.2978 0.0579  0.0886  0.0093  491  PRO A CD    
2276 N  N     . THR A 382 ? 0.2135 0.1935 0.2977 -0.0098 0.0181  0.0018  492  THR A N     
2277 C  CA    . THR A 382 ? 0.1810 0.2013 0.2986 0.0081  0.0293  -0.0052 492  THR A CA    
2278 C  C     . THR A 382 ? 0.1627 0.1954 0.3076 0.0042  0.0223  -0.0111 492  THR A C     
2279 O  O     . THR A 382 ? 0.1600 0.2325 0.3245 0.0117  0.0226  0.0058  492  THR A O     
2280 C  CB    . THR A 382 ? 0.1918 0.2466 0.2969 0.0182  0.0251  0.0236  492  THR A CB    
2281 O  OG1   . THR A 382 ? 0.2288 0.2738 0.2857 0.0178  0.0348  0.0093  492  THR A OG1   
2282 C  CG2   . THR A 382 ? 0.1953 0.2503 0.3396 -0.0030 0.0378  0.0152  492  THR A CG2   
2283 N  N     . ILE A 383 ? 0.1784 0.2111 0.2572 -0.0137 0.0319  0.0050  493  ILE A N     
2284 C  CA    . ILE A 383 ? 0.1680 0.2206 0.2526 -0.0211 0.0379  0.0303  493  ILE A CA    
2285 C  C     . ILE A 383 ? 0.1928 0.2523 0.2567 -0.0038 0.0520  0.0023  493  ILE A C     
2286 O  O     . ILE A 383 ? 0.2081 0.2179 0.2428 0.0145  0.0080  -0.0043 493  ILE A O     
2287 C  CB    . ILE A 383 ? 0.1458 0.2225 0.2757 -0.0177 -0.0207 0.0235  493  ILE A CB    
2288 C  CG1   . ILE A 383 ? 0.1899 0.2354 0.2790 0.0280  0.0013  -0.0111 493  ILE A CG1   
2289 C  CG2   . ILE A 383 ? 0.1664 0.2346 0.3112 -0.0366 -0.0231 0.0124  493  ILE A CG2   
2290 C  CD1   . ILE A 383 ? 0.1858 0.2149 0.2710 0.0237  0.0107  -0.0190 493  ILE A CD1   
2291 N  N     . GLU A 384 ? 0.2455 0.2830 0.2435 -0.0120 0.0601  -0.0010 494  GLU A N     
2292 C  CA    . GLU A 384 ? 0.2782 0.2645 0.2797 0.0436  0.0558  -0.0313 494  GLU A CA    
2293 C  C     . GLU A 384 ? 0.2750 0.2830 0.2814 0.0026  0.0391  -0.0017 494  GLU A C     
2294 O  O     . GLU A 384 ? 0.2709 0.2976 0.2666 -0.0127 0.0316  0.0143  494  GLU A O     
2295 C  CB    . GLU A 384 ? 0.3242 0.2498 0.3340 0.0577  0.0476  -0.0154 494  GLU A CB    
2296 C  CG    . GLU A 384 ? 0.3672 0.2591 0.3784 0.0529  0.0238  -0.0106 494  GLU A CG    
2297 C  CD    . GLU A 384 ? 0.3801 0.2470 0.4132 0.0467  0.0200  -0.0128 494  GLU A CD    
2298 O  OE1   . GLU A 384 ? 0.3598 0.2356 0.4434 0.0532  -0.0192 -0.0481 494  GLU A OE1   
2299 O  OE2   . GLU A 384 ? 0.4112 0.2948 0.4228 0.0363  0.0434  -0.0174 494  GLU A OE2   
2300 N  N     . VAL A 385 ? 0.2394 0.2385 0.2849 0.0174  0.0420  -0.0144 495  VAL A N     
2301 C  CA    . VAL A 385 ? 0.2085 0.2323 0.2920 0.0006  0.0278  0.0158  495  VAL A CA    
2302 C  C     . VAL A 385 ? 0.2198 0.2286 0.2767 -0.0003 0.0235  0.0005  495  VAL A C     
2303 O  O     . VAL A 385 ? 0.2350 0.2362 0.2562 0.0130  0.0150  0.0222  495  VAL A O     
2304 C  CB    . VAL A 385 ? 0.2189 0.2018 0.3135 0.0173  0.0626  0.0114  495  VAL A CB    
2305 C  CG1   . VAL A 385 ? 0.2414 0.2556 0.3058 -0.0131 0.0565  0.0154  495  VAL A CG1   
2306 C  CG2   . VAL A 385 ? 0.2139 0.2345 0.3551 -0.0275 0.0805  -0.0151 495  VAL A CG2   
2307 N  N     . LEU A 386 ? 0.2095 0.2259 0.2744 0.0049  0.0140  0.0046  496  LEU A N     
2308 C  CA    . LEU A 386 ? 0.1885 0.2204 0.2457 -0.0030 0.0218  -0.0034 496  LEU A CA    
2309 C  C     . LEU A 386 ? 0.1878 0.2044 0.2540 0.0137  0.0106  -0.0059 496  LEU A C     
2310 O  O     . LEU A 386 ? 0.1842 0.2045 0.2263 -0.0060 0.0009  0.0023  496  LEU A O     
2311 C  CB    . LEU A 386 ? 0.1971 0.2286 0.2071 -0.0038 0.0372  0.0031  496  LEU A CB    
2312 C  CG    . LEU A 386 ? 0.2173 0.1889 0.1790 -0.0045 0.0513  0.0203  496  LEU A CG    
2313 C  CD1   . LEU A 386 ? 0.2294 0.2087 0.1674 -0.0146 0.0173  0.0148  496  LEU A CD1   
2314 C  CD2   . LEU A 386 ? 0.2254 0.2161 0.1707 -0.0066 0.0514  -0.0144 496  LEU A CD2   
2315 N  N     . GLN A 387 ? 0.2019 0.2232 0.2638 -0.0137 0.0049  -0.0028 497  GLN A N     
2316 C  CA    . GLN A 387 ? 0.1905 0.2178 0.2680 -0.0005 0.0144  0.0073  497  GLN A CA    
2317 C  C     . GLN A 387 ? 0.1997 0.2311 0.2592 -0.0209 0.0215  0.0091  497  GLN A C     
2318 O  O     . GLN A 387 ? 0.2337 0.2748 0.2390 0.0149  0.0349  0.0105  497  GLN A O     
2319 C  CB    . GLN A 387 ? 0.2129 0.2268 0.2577 0.0133  0.0247  -0.0103 497  GLN A CB    
2320 C  CG    . GLN A 387 ? 0.2285 0.2179 0.2370 0.0373  0.0137  -0.0158 497  GLN A CG    
2321 C  CD    . GLN A 387 ? 0.2231 0.2157 0.2378 0.0095  0.0700  -0.0013 497  GLN A CD    
2322 O  OE1   . GLN A 387 ? 0.2650 0.2365 0.2332 -0.0090 0.0736  -0.0281 497  GLN A OE1   
2323 N  NE2   . GLN A 387 ? 0.1989 0.2295 0.2501 0.0063  0.0061  -0.0290 497  GLN A NE2   
2324 N  N     . GLN A 388 ? 0.2422 0.2156 0.2554 -0.0018 0.0499  0.0288  498  GLN A N     
2325 C  CA    . GLN A 388 ? 0.2795 0.2701 0.2394 -0.0057 0.0573  0.0243  498  GLN A CA    
2326 C  C     . GLN A 388 ? 0.2417 0.2549 0.1836 0.0030  0.0604  0.0212  498  GLN A C     
2327 O  O     . GLN A 388 ? 0.2666 0.2807 0.1910 -0.0155 0.0328  0.0438  498  GLN A O     
2328 C  CB    . GLN A 388 ? 0.3680 0.2805 0.2420 0.0207  0.0838  0.0289  498  GLN A CB    
2329 C  CG    . GLN A 388 ? 0.4123 0.3291 0.3004 0.0571  0.1181  0.0460  498  GLN A CG    
2330 C  CD    . GLN A 388 ? 0.5570 0.4006 0.4194 0.0455  0.0989  0.0574  498  GLN A CD    
2331 O  OE1   . GLN A 388 ? 0.6221 0.4372 0.4663 0.0339  0.1098  0.0663  498  GLN A OE1   
2332 N  NE2   . GLN A 388 ? 0.6004 0.4431 0.4493 0.0450  0.0896  0.0551  498  GLN A NE2   
2333 N  N     . ALA A 389 ? 0.2191 0.2463 0.1928 0.0026  0.0676  -0.0263 499  ALA A N     
2334 C  CA    . ALA A 389 ? 0.2162 0.2094 0.1947 0.0030  0.0300  -0.0445 499  ALA A CA    
2335 C  C     . ALA A 389 ? 0.2141 0.2115 0.2383 0.0332  0.0134  -0.0197 499  ALA A C     
2336 O  O     . ALA A 389 ? 0.2437 0.2246 0.2774 0.0062  0.0010  0.0246  499  ALA A O     
2337 C  CB    . ALA A 389 ? 0.2428 0.2019 0.2181 -0.0298 -0.0068 -0.0659 499  ALA A CB    
2338 N  N     . GLN A 390 ? 0.1835 0.2018 0.1864 0.0264  0.0185  -0.0026 500  GLN A N     
2339 C  CA    . GLN A 390 ? 0.1975 0.2203 0.1718 0.0248  0.0576  0.0194  500  GLN A CA    
2340 C  C     . GLN A 390 ? 0.2017 0.2164 0.1943 0.0050  0.0317  0.0109  500  GLN A C     
2341 O  O     . GLN A 390 ? 0.2152 0.2062 0.2392 0.0092  0.0188  0.0422  500  GLN A O     
2342 C  CB    . GLN A 390 ? 0.2449 0.2365 0.1706 -0.0085 -0.0001 0.0276  500  GLN A CB    
2343 C  CG    . GLN A 390 ? 0.2804 0.2528 0.1955 -0.0271 -0.0089 0.0291  500  GLN A CG    
2344 C  CD    . GLN A 390 ? 0.2921 0.2757 0.2200 -0.0597 0.0001  0.0210  500  GLN A CD    
2345 O  OE1   . GLN A 390 ? 0.2925 0.2809 0.2510 -0.0462 -0.0009 0.0408  500  GLN A OE1   
2346 N  NE2   . GLN A 390 ? 0.3319 0.2922 0.2568 -0.0526 0.0100  0.0199  500  GLN A NE2   
2347 N  N     . PHE A 391 ? 0.1698 0.2020 0.1734 0.0023  0.0370  0.0191  501  PHE A N     
2348 C  CA    . PHE A 391 ? 0.1835 0.1837 0.1957 0.0086  0.0459  0.0407  501  PHE A CA    
2349 C  C     . PHE A 391 ? 0.2055 0.2013 0.2310 0.0057  0.0303  0.0124  501  PHE A C     
2350 O  O     . PHE A 391 ? 0.2185 0.2171 0.2194 -0.0079 0.0049  0.0324  501  PHE A O     
2351 C  CB    . PHE A 391 ? 0.1791 0.1863 0.1911 0.0141  0.0324  0.0214  501  PHE A CB    
2352 C  CG    . PHE A 391 ? 0.2300 0.1746 0.1831 0.0285  0.0040  0.0148  501  PHE A CG    
2353 C  CD1   . PHE A 391 ? 0.1966 0.2001 0.1961 0.0276  -0.0172 0.0243  501  PHE A CD1   
2354 C  CD2   . PHE A 391 ? 0.2435 0.1981 0.2205 0.0314  -0.0015 0.0166  501  PHE A CD2   
2355 C  CE1   . PHE A 391 ? 0.1991 0.1936 0.2249 0.0245  0.0236  0.0026  501  PHE A CE1   
2356 C  CE2   . PHE A 391 ? 0.2499 0.2209 0.2216 0.0244  -0.0278 0.0076  501  PHE A CE2   
2357 C  CZ    . PHE A 391 ? 0.2249 0.2207 0.2133 0.0431  0.0035  -0.0034 501  PHE A CZ    
2358 N  N     . VAL A 392 ? 0.1974 0.1876 0.2391 0.0173  -0.0032 0.0095  502  VAL A N     
2359 C  CA    . VAL A 392 ? 0.1829 0.1701 0.2577 0.0048  -0.0012 0.0228  502  VAL A CA    
2360 C  C     . VAL A 392 ? 0.1904 0.2244 0.2758 -0.0056 0.0052  -0.0092 502  VAL A C     
2361 O  O     . VAL A 392 ? 0.1998 0.2172 0.2574 -0.0052 0.0096  -0.0102 502  VAL A O     
2362 C  CB    . VAL A 392 ? 0.2000 0.1677 0.2528 0.0404  -0.0483 0.0550  502  VAL A CB    
2363 C  CG1   . VAL A 392 ? 0.2184 0.2055 0.2805 0.0152  -0.0382 0.0529  502  VAL A CG1   
2364 C  CG2   . VAL A 392 ? 0.2049 0.1842 0.2889 0.0219  0.0040  0.0328  502  VAL A CG2   
2365 N  N     . ARG A 393 ? 0.1616 0.2179 0.2825 -0.0257 0.0069  0.0022  503  ARG A N     
2366 C  CA    . ARG A 393 ? 0.1624 0.2167 0.3060 -0.0317 0.0050  0.0052  503  ARG A CA    
2367 C  C     . ARG A 393 ? 0.2250 0.2239 0.3099 0.0102  0.0077  0.0089  503  ARG A C     
2368 O  O     . ARG A 393 ? 0.2610 0.2006 0.3065 0.0274  0.0065  0.0148  503  ARG A O     
2369 C  CB    . ARG A 393 ? 0.1556 0.2676 0.3312 -0.0442 -0.0065 0.0151  503  ARG A CB    
2370 C  CG    . ARG A 393 ? 0.2157 0.2984 0.3594 -0.0571 -0.0039 -0.0478 503  ARG A CG    
2371 C  CD    . ARG A 393 ? 0.2321 0.2840 0.4161 -0.0505 0.0487  -0.0319 503  ARG A CD    
2372 N  NE    . ARG A 393 ? 0.3102 0.3155 0.4710 -0.0657 0.0367  -0.0069 503  ARG A NE    
2373 C  CZ    . ARG A 393 ? 0.3652 0.3838 0.4871 -0.0710 0.0632  0.0182  503  ARG A CZ    
2374 N  NH1   . ARG A 393 ? 0.4104 0.4245 0.4792 -0.0772 0.0777  0.0338  503  ARG A NH1   
2375 N  NH2   . ARG A 393 ? 0.3786 0.3970 0.5030 -0.0499 0.1009  0.0210  503  ARG A NH2   
2376 N  N     . ILE A 394 ? 0.2165 0.2155 0.3278 0.0349  0.0117  0.0165  504  ILE A N     
2377 C  CA    . ILE A 394 ? 0.2322 0.2424 0.3551 0.0349  0.0196  -0.0177 504  ILE A CA    
2378 C  C     . ILE A 394 ? 0.2323 0.2042 0.4096 0.0151  0.0451  -0.0111 504  ILE A C     
2379 O  O     . ILE A 394 ? 0.2592 0.1998 0.4312 0.0177  0.0235  -0.0400 504  ILE A O     
2380 C  CB    . ILE A 394 ? 0.2722 0.3128 0.3755 0.0286  0.0293  -0.0065 504  ILE A CB    
2381 C  CG1   . ILE A 394 ? 0.3193 0.3221 0.3771 -0.0273 -0.0090 0.0071  504  ILE A CG1   
2382 C  CG2   . ILE A 394 ? 0.2499 0.3431 0.3704 0.0410  0.0318  -0.0302 504  ILE A CG2   
2383 C  CD1   . ILE A 394 ? 0.3497 0.3192 0.4054 -0.0567 0.0166  0.0239  504  ILE A CD1   
2384 N  N     . THR A 395 ? 0.2609 0.2041 0.4261 0.0618  0.0751  0.0011  505  THR A N     
2385 C  CA    . THR A 395 ? 0.3202 0.1907 0.4750 0.1076  0.0641  -0.0088 505  THR A CA    
2386 C  C     . THR A 395 ? 0.3111 0.2370 0.4951 0.0775  0.0636  0.0321  505  THR A C     
2387 O  O     . THR A 395 ? 0.3302 0.2655 0.4598 0.0503  0.0505  0.0545  505  THR A O     
2388 C  CB    . THR A 395 ? 0.3813 0.2139 0.5082 0.0604  0.0489  0.0014  505  THR A CB    
2389 O  OG1   . THR A 395 ? 0.4444 0.2362 0.5318 0.0632  0.0467  -0.0061 505  THR A OG1   
2390 C  CG2   . THR A 395 ? 0.3857 0.2089 0.5051 0.0436  0.0233  0.0109  505  THR A CG2   
2391 N  N     . PRO A 396 ? 0.3253 0.3124 0.5409 0.0367  0.0227  0.0360  506  PRO A N     
2392 C  CA    . PRO A 396 ? 0.3672 0.3352 0.5539 0.0222  0.0421  -0.0049 506  PRO A CA    
2393 C  C     . PRO A 396 ? 0.4617 0.3621 0.5499 0.0255  0.0447  -0.0160 506  PRO A C     
2394 O  O     . PRO A 396 ? 0.4942 0.4062 0.5708 0.0352  0.0620  -0.0236 506  PRO A O     
2395 C  CB    . PRO A 396 ? 0.2848 0.3378 0.5633 0.0339  0.0397  0.0085  506  PRO A CB    
2396 C  CG    . PRO A 396 ? 0.2835 0.3382 0.5597 0.0418  0.0261  0.0359  506  PRO A CG    
2397 C  CD    . PRO A 396 ? 0.2489 0.3335 0.5550 0.0201  0.0240  0.0592  506  PRO A CD    
2398 N  N     . ALA A 397 ? 0.5053 0.2981 0.5294 -0.0076 0.0459  -0.0441 507  ALA A N     
2399 C  CA    . ALA A 397 ? 0.5524 0.3029 0.5249 0.0564  0.0293  -0.0359 507  ALA A CA    
2400 C  C     . ALA A 397 ? 0.5760 0.3304 0.5240 0.0439  -0.0066 -0.0580 507  ALA A C     
2401 O  O     . ALA A 397 ? 0.6093 0.3228 0.5197 0.0257  -0.0244 -0.0763 507  ALA A O     
2402 C  CB    . ALA A 397 ? 0.5509 0.2874 0.5235 0.0777  0.0216  -0.0114 507  ALA A CB    
2403 N  N     . GLY A 398 ? 0.5511 0.3585 0.5282 0.0870  0.0068  -0.0843 508  GLY A N     
2404 C  CA    . GLY A 398 ? 0.5843 0.4348 0.5499 0.0802  -0.0169 -0.0807 508  GLY A CA    
2405 C  C     . GLY A 398 ? 0.5990 0.4757 0.5509 0.0732  -0.0283 -0.0831 508  GLY A C     
2406 O  O     . GLY A 398 ? 0.6027 0.4987 0.5684 0.0711  -0.0410 -0.0747 508  GLY A O     
2407 N  N     . LEU A 399 ? 0.6081 0.5303 0.5414 0.0629  -0.0364 -0.0917 509  LEU A N     
2408 C  CA    . LEU A 399 ? 0.6378 0.5800 0.5605 0.0778  -0.0633 -0.0989 509  LEU A CA    
2409 C  C     . LEU A 399 ? 0.6828 0.6392 0.6140 0.1003  -0.0609 -0.0941 509  LEU A C     
2410 O  O     . LEU A 399 ? 0.6701 0.6161 0.6126 0.1326  -0.0663 -0.1091 509  LEU A O     
2411 C  CB    . LEU A 399 ? 0.6063 0.5531 0.5398 0.0576  -0.0867 -0.1195 509  LEU A CB    
2412 C  CG    . LEU A 399 ? 0.5792 0.5391 0.5235 0.0549  -0.1057 -0.1294 509  LEU A CG    
2413 C  CD1   . LEU A 399 ? 0.5693 0.5347 0.5160 0.0577  -0.1252 -0.1290 509  LEU A CD1   
2414 C  CD2   . LEU A 399 ? 0.5646 0.5328 0.5232 0.0517  -0.1014 -0.1459 509  LEU A CD2   
2415 N  N     . LYS A 400 ? 0.7228 0.7163 0.6764 0.0967  -0.0386 -0.0700 510  LYS A N     
2416 C  CA    . LYS A 400 ? 0.7735 0.7938 0.7581 0.0632  -0.0084 -0.0449 510  LYS A CA    
2417 C  C     . LYS A 400 ? 0.8062 0.8043 0.7893 0.0442  0.0273  -0.0291 510  LYS A C     
2418 O  O     . LYS A 400 ? 0.8058 0.8132 0.7821 0.0216  0.0384  -0.0354 510  LYS A O     
2419 C  CB    . LYS A 400 ? 0.7938 0.8455 0.7982 0.0493  -0.0099 -0.0330 510  LYS A CB    
2420 C  CG    . LYS A 400 ? 0.8171 0.8880 0.8310 0.0236  -0.0115 -0.0230 510  LYS A CG    
2421 C  CD    . LYS A 400 ? 0.8399 0.9369 0.8593 -0.0002 -0.0186 -0.0163 510  LYS A CD    
2422 C  CE    . LYS A 400 ? 0.8570 0.9638 0.8832 -0.0101 -0.0277 -0.0131 510  LYS A CE    
2423 N  NZ    . LYS A 400 ? 0.8656 0.9778 0.9011 -0.0184 -0.0343 -0.0144 510  LYS A NZ    
2424 N  N     . GLU A 401 ? 0.8331 0.8002 0.8146 0.0506  0.0531  0.0041  511  GLU A N     
2425 C  CA    . GLU A 401 ? 0.8563 0.7983 0.8301 0.0372  0.0565  0.0139  511  GLU A CA    
2426 C  C     . GLU A 401 ? 0.8982 0.8241 0.8616 0.0259  0.0502  0.0133  511  GLU A C     
2427 O  O     . GLU A 401 ? 0.9018 0.8201 0.8602 0.0042  0.0540  0.0024  511  GLU A O     
2428 C  CB    . GLU A 401 ? 0.8535 0.7830 0.8176 0.0344  0.0508  0.0132  511  GLU A CB    
2429 C  CG    . GLU A 401 ? 0.8570 0.7627 0.8018 0.0217  0.0633  0.0035  511  GLU A CG    
2430 C  CD    . GLU A 401 ? 0.8605 0.7479 0.8021 -0.0129 0.0750  0.0002  511  GLU A CD    
2431 O  OE1   . GLU A 401 ? 0.8638 0.7392 0.7987 -0.0293 0.0902  -0.0168 511  GLU A OE1   
2432 O  OE2   . GLU A 401 ? 0.8720 0.7567 0.8156 -0.0253 0.0625  0.0201  511  GLU A OE2   
2433 N  N     . SER A 402 ? 0.9299 0.8507 0.8896 0.0416  0.0456  0.0169  512  SER A N     
2434 C  CA    . SER A 402 ? 0.9507 0.8808 0.9097 0.0543  0.0400  0.0138  512  SER A CA    
2435 C  C     . SER A 402 ? 0.9729 0.9153 0.9357 0.0494  0.0229  0.0193  512  SER A C     
2436 O  O     . SER A 402 ? 0.9607 0.9167 0.9394 0.0499  0.0352  0.0132  512  SER A O     
2437 C  CB    . SER A 402 ? 0.9518 0.8760 0.9091 0.0746  0.0479  0.0084  512  SER A CB    
2438 O  OG    . SER A 402 ? 0.9532 0.8713 0.9136 0.0844  0.0468  0.0125  512  SER A OG    
2439 N  N     . HIS A 403 ? 1.0118 0.9467 0.9581 0.0389  0.0015  0.0298  513  HIS A N     
2440 C  CA    . HIS A 403 ? 1.0420 0.9804 0.9983 0.0306  -0.0049 0.0237  513  HIS A CA    
2441 C  C     . HIS A 403 ? 1.0699 1.0128 1.0130 0.0462  -0.0244 0.0109  513  HIS A C     
2442 O  O     . HIS A 403 ? 1.0829 1.0261 1.0238 0.0574  -0.0101 0.0035  513  HIS A O     
2443 C  CB    . HIS A 403 ? 1.0489 0.9904 1.0284 0.0161  0.0185  0.0242  513  HIS A CB    
2444 C  CG    . HIS A 403 ? 1.0625 1.0084 1.0549 0.0186  0.0436  0.0100  513  HIS A CG    
2445 N  ND1   . HIS A 403 ? 1.0696 1.0177 1.0545 0.0228  0.0451  0.0082  513  HIS A ND1   
2446 C  CD2   . HIS A 403 ? 1.0741 1.0255 1.0713 0.0268  0.0645  -0.0042 513  HIS A CD2   
2447 C  CE1   . HIS A 403 ? 1.0804 1.0290 1.0598 0.0295  0.0515  0.0035  513  HIS A CE1   
2448 N  NE2   . HIS A 403 ? 1.0827 1.0312 1.0682 0.0358  0.0628  -0.0049 513  HIS A NE2   
2449 N  N     . PRO A 404 ? 1.0818 1.0246 1.0102 0.0446  -0.0550 0.0053  514  PRO A N     
2450 C  CA    . PRO A 404 ? 1.0729 1.0249 1.0097 0.0369  -0.0650 0.0060  514  PRO A CA    
2451 C  C     . PRO A 404 ? 1.0462 1.0287 0.9992 0.0193  -0.0647 0.0197  514  PRO A C     
2452 O  O     . PRO A 404 ? 1.0485 1.0442 1.0095 0.0110  -0.0591 0.0238  514  PRO A O     
2453 C  CB    . PRO A 404 ? 1.0741 1.0278 1.0188 0.0432  -0.0713 -0.0039 514  PRO A CB    
2454 C  CG    . PRO A 404 ? 1.0718 1.0302 1.0155 0.0455  -0.0685 -0.0071 514  PRO A CG    
2455 C  CD    . PRO A 404 ? 1.0785 1.0272 1.0083 0.0456  -0.0653 -0.0009 514  PRO A CD    
2456 N  N     . HIS A 405 ? 1.0190 1.0200 0.9772 0.0065  -0.0676 0.0292  515  HIS A N     
2457 C  CA    . HIS A 405 ? 0.9769 1.0019 0.9528 -0.0169 -0.0675 0.0340  515  HIS A CA    
2458 C  C     . HIS A 405 ? 0.9785 1.0161 0.9755 -0.0262 -0.0568 0.0312  515  HIS A C     
2459 O  O     . HIS A 405 ? 0.9624 1.0182 0.9669 -0.0536 -0.0566 0.0367  515  HIS A O     
2460 C  CB    . HIS A 405 ? 0.9248 0.9842 0.9159 -0.0399 -0.0831 0.0380  515  HIS A CB    
2461 C  CG    . HIS A 405 ? 0.8839 0.9885 0.9039 -0.0565 -0.0944 0.0297  515  HIS A CG    
2462 N  ND1   . HIS A 405 ? 0.8658 0.9938 0.9081 -0.0592 -0.0994 0.0259  515  HIS A ND1   
2463 C  CD2   . HIS A 405 ? 0.8632 0.9930 0.9009 -0.0613 -0.1007 0.0126  515  HIS A CD2   
2464 C  CE1   . HIS A 405 ? 0.8527 1.0014 0.9123 -0.0673 -0.1040 0.0164  515  HIS A CE1   
2465 N  NE2   . HIS A 405 ? 0.8566 1.0088 0.9118 -0.0713 -0.0998 0.0131  515  HIS A NE2   
2466 N  N     . ASP A 406 ? 0.9887 1.0249 1.0067 -0.0092 -0.0487 0.0211  516  ASP A N     
2467 C  CA    . ASP A 406 ? 0.9940 1.0101 1.0332 0.0014  -0.0379 0.0300  516  ASP A CA    
2468 C  C     . ASP A 406 ? 0.9701 0.9818 0.9944 -0.0111 -0.0225 0.0464  516  ASP A C     
2469 O  O     . ASP A 406 ? 0.9696 0.9727 1.0236 -0.0264 -0.0092 0.0467  516  ASP A O     
2470 C  CB    . ASP A 406 ? 1.0243 1.0184 1.0913 0.0164  -0.0344 0.0322  516  ASP A CB    
2471 C  CG    . ASP A 406 ? 1.0434 1.0298 1.1242 0.0137  -0.0295 0.0506  516  ASP A CG    
2472 O  OD1   . ASP A 406 ? 1.0599 1.0316 1.1425 -0.0028 -0.0439 0.0513  516  ASP A OD1   
2473 O  OD2   . ASP A 406 ? 1.0358 1.0416 1.1272 0.0277  -0.0081 0.0680  516  ASP A OD2   
2474 N  N     . VAL A 407 ? 0.9402 0.9528 0.9537 -0.0109 -0.0228 0.0612  517  VAL A N     
2475 C  CA    . VAL A 407 ? 0.9276 0.9279 0.9194 -0.0237 -0.0126 0.0487  517  VAL A CA    
2476 C  C     . VAL A 407 ? 0.9328 0.9074 0.9083 -0.0310 -0.0052 0.0376  517  VAL A C     
2477 O  O     . VAL A 407 ? 0.9526 0.9115 0.9215 -0.0289 -0.0025 0.0347  517  VAL A O     
2478 C  CB    . VAL A 407 ? 0.9084 0.9225 0.8993 -0.0279 0.0042  0.0409  517  VAL A CB    
2479 C  CG1   . VAL A 407 ? 0.9155 0.9152 0.9013 -0.0287 0.0123  0.0092  517  VAL A CG1   
2480 C  CG2   . VAL A 407 ? 0.8959 0.9328 0.8910 -0.0238 0.0045  0.0600  517  VAL A CG2   
2481 N  N     . ALA A 408 ? 0.9030 0.8805 0.8816 -0.0383 -0.0032 0.0344  518  ALA A N     
2482 C  CA    . ALA A 408 ? 0.8752 0.8595 0.8676 -0.0382 -0.0114 0.0246  518  ALA A CA    
2483 C  C     . ALA A 408 ? 0.8556 0.8364 0.8650 -0.0400 -0.0051 0.0236  518  ALA A C     
2484 O  O     . ALA A 408 ? 0.8437 0.8205 0.8691 -0.0533 0.0006  0.0231  518  ALA A O     
2485 C  CB    . ALA A 408 ? 0.8678 0.8618 0.8580 -0.0401 -0.0185 0.0125  518  ALA A CB    
2486 N  N     . MET A 409 ? 0.8420 0.8231 0.8547 -0.0361 0.0021  0.0199  519  MET A N     
2487 C  CA    . MET A 409 ? 0.8376 0.8223 0.8447 -0.0355 0.0141  0.0104  519  MET A CA    
2488 C  C     . MET A 409 ? 0.8412 0.8294 0.8482 -0.0133 0.0112  0.0150  519  MET A C     
2489 O  O     . MET A 409 ? 0.8413 0.8327 0.8432 -0.0198 0.0193  0.0127  519  MET A O     
2490 C  CB    . MET A 409 ? 0.8371 0.8274 0.8383 -0.0541 0.0275  0.0091  519  MET A CB    
2491 C  CG    . MET A 409 ? 0.8294 0.8261 0.8347 -0.0695 0.0413  0.0150  519  MET A CG    
2492 S  SD    . MET A 409 ? 0.8250 0.8405 0.8396 -0.0772 0.0562  0.0271  519  MET A SD    
2493 C  CE    . MET A 409 ? 0.8106 0.8430 0.8330 -0.0816 0.0685  0.0443  519  MET A CE    
2494 N  N     . THR A 410 ? 0.8521 0.8364 0.8549 0.0195  0.0033  0.0329  520  THR A N     
2495 C  CA    . THR A 410 ? 0.8689 0.8369 0.8547 0.0450  0.0017  0.0243  520  THR A CA    
2496 C  C     . THR A 410 ? 0.8774 0.8358 0.8562 0.0473  0.0118  0.0142  520  THR A C     
2497 O  O     . THR A 410 ? 0.8762 0.8353 0.8449 0.0486  0.0015  0.0144  520  THR A O     
2498 C  CB    . THR A 410 ? 0.8751 0.8316 0.8431 0.0635  -0.0070 0.0085  520  THR A CB    
2499 O  OG1   . THR A 410 ? 0.8781 0.8326 0.8355 0.0551  -0.0137 0.0092  520  THR A OG1   
2500 C  CG2   . THR A 410 ? 0.8803 0.8247 0.8432 0.0844  -0.0072 -0.0004 520  THR A CG2   
2501 N  N     . VAL A 411 ? 0.8799 0.8316 0.8579 0.0512  0.0369  0.0047  521  VAL A N     
2502 C  CA    . VAL A 411 ? 0.8848 0.8408 0.8624 0.0412  0.0518  -0.0064 521  VAL A CA    
2503 C  C     . VAL A 411 ? 0.9006 0.8531 0.8876 0.0434  0.0581  -0.0085 521  VAL A C     
2504 O  O     . VAL A 411 ? 0.8870 0.8499 0.8846 0.0434  0.0473  -0.0108 521  VAL A O     
2505 C  CB    . VAL A 411 ? 0.8671 0.8389 0.8418 0.0282  0.0507  -0.0065 521  VAL A CB    
2506 C  CG1   . VAL A 411 ? 0.8524 0.8386 0.8272 0.0149  0.0468  -0.0032 521  VAL A CG1   
2507 C  CG2   . VAL A 411 ? 0.8680 0.8390 0.8413 0.0322  0.0558  -0.0086 521  VAL A CG2   
2508 N  N     . GLU A 412 ? 0.9181 0.8640 0.9057 0.0422  0.0701  -0.0042 522  GLU A N     
2509 C  CA    . GLU A 412 ? 0.9329 0.8686 0.9290 0.0269  0.0760  -0.0025 522  GLU A CA    
2510 C  C     . GLU A 412 ? 0.9173 0.8442 0.8951 0.0187  0.0787  0.0000  522  GLU A C     
2511 O  O     . GLU A 412 ? 0.9115 0.8551 0.8948 0.0137  0.0905  0.0131  522  GLU A O     
2512 C  CB    . GLU A 412 ? 0.9669 0.9101 0.9856 0.0162  0.0751  -0.0013 522  GLU A CB    
2513 C  CG    . GLU A 412 ? 0.9993 0.9492 1.0292 0.0224  0.0697  0.0027  522  GLU A CG    
2514 C  CD    . GLU A 412 ? 1.0326 0.9881 1.0615 0.0392  0.0660  0.0111  522  GLU A CD    
2515 O  OE1   . GLU A 412 ? 1.0446 1.0046 1.0754 0.0551  0.0550  0.0193  522  GLU A OE1   
2516 O  OE2   . GLU A 412 ? 1.0391 0.9927 1.0620 0.0431  0.0752  0.0107  522  GLU A OE2   
2517 N  N     . ALA A 413 ? 0.8995 0.8105 0.8643 0.0139  0.0716  -0.0114 523  ALA A N     
2518 C  CA    . ALA A 413 ? 0.8818 0.7846 0.8406 0.0143  0.0601  -0.0147 523  ALA A CA    
2519 C  C     . ALA A 413 ? 0.8521 0.7611 0.8120 0.0110  0.0586  -0.0165 523  ALA A C     
2520 O  O     . ALA A 413 ? 0.8335 0.7596 0.8103 0.0108  0.0711  -0.0284 523  ALA A O     
2521 C  CB    . ALA A 413 ? 0.8904 0.7863 0.8453 0.0173  0.0558  -0.0051 523  ALA A CB    
2522 N  N     . PRO A 414 ? 0.8363 0.7413 0.7845 -0.0010 0.0435  0.0078  524  PRO A N     
2523 C  CA    . PRO A 414 ? 0.8100 0.7167 0.7545 -0.0025 0.0280  0.0255  524  PRO A CA    
2524 C  C     . PRO A 414 ? 0.7791 0.6941 0.7119 -0.0097 0.0115  0.0512  524  PRO A C     
2525 O  O     . PRO A 414 ? 0.8049 0.6790 0.7117 0.0000  0.0189  0.0464  524  PRO A O     
2526 C  CB    . PRO A 414 ? 0.8169 0.7195 0.7621 0.0135  0.0314  0.0221  524  PRO A CB    
2527 C  CG    . PRO A 414 ? 0.8243 0.7269 0.7684 0.0023  0.0438  0.0260  524  PRO A CG    
2528 C  CD    . PRO A 414 ? 0.8322 0.7324 0.7759 -0.0077 0.0500  0.0187  524  PRO A CD    
2529 N  N     . ASN A 415 ? 0.7495 0.6776 0.6797 -0.0233 -0.0105 0.0762  525  ASN A N     
2530 C  CA    . ASN A 415 ? 0.6921 0.6626 0.6516 -0.0512 -0.0274 0.0694  525  ASN A CA    
2531 C  C     . ASN A 415 ? 0.6692 0.6798 0.6755 -0.0579 0.0028  0.0488  525  ASN A C     
2532 O  O     . ASN A 415 ? 0.6474 0.6805 0.6828 -0.0588 0.0342  0.0342  525  ASN A O     
2533 C  CB    . ASN A 415 ? 0.6495 0.6285 0.6014 -0.0741 -0.0406 0.0752  525  ASN A CB    
2534 C  CG    . ASN A 415 ? 0.6075 0.6099 0.5777 -0.0855 -0.0609 0.0803  525  ASN A CG    
2535 O  OD1   . ASN A 415 ? 0.5956 0.5822 0.5722 -0.0984 -0.0813 0.0636  525  ASN A OD1   
2536 N  ND2   . ASN A 415 ? 0.5500 0.5934 0.5336 -0.1087 -0.0414 0.1079  525  ASN A ND2   
2537 P  P     . IMP B .   ? 0.2189 0.1893 0.2151 -0.0037 0.0167  -0.0117 801  IMP A P     
2538 O  O1P   . IMP B .   ? 0.2438 0.2134 0.2437 -0.0084 -0.0155 -0.0347 801  IMP A O1P   
2539 O  O2P   . IMP B .   ? 0.2212 0.1635 0.2802 0.0197  -0.0083 0.0041  801  IMP A O2P   
2540 O  O3P   . IMP B .   ? 0.2358 0.2328 0.2005 -0.0104 0.0096  -0.0089 801  IMP A O3P   
2541 O  "O5'" . IMP B .   ? 0.2569 0.1499 0.2520 0.0082  -0.0059 -0.0238 801  IMP A "O5'" 
2542 C  "C5'" . IMP B .   ? 0.2436 0.1523 0.2142 0.0317  -0.0343 -0.0667 801  IMP A "C5'" 
2543 C  "C4'" . IMP B .   ? 0.2167 0.1772 0.2241 -0.0009 -0.0088 -0.0092 801  IMP A "C4'" 
2544 O  "O4'" . IMP B .   ? 0.1945 0.2256 0.1923 -0.0010 -0.0166 -0.0032 801  IMP A "O4'" 
2545 C  "C3'" . IMP B .   ? 0.2159 0.2041 0.2269 -0.0007 -0.0078 -0.0286 801  IMP A "C3'" 
2546 O  "O3'" . IMP B .   ? 0.2193 0.2244 0.1897 0.0059  -0.0091 -0.0368 801  IMP A "O3'" 
2547 C  "C2'" . IMP B .   ? 0.2156 0.2216 0.2118 -0.0024 0.0076  0.0029  801  IMP A "C2'" 
2548 O  "O2'" . IMP B .   ? 0.2144 0.2192 0.1957 -0.0159 0.0214  -0.0087 801  IMP A "O2'" 
2549 C  "C1'" . IMP B .   ? 0.1914 0.2055 0.2114 -0.0267 0.0093  0.0188  801  IMP A "C1'" 
2550 N  N9    . IMP B .   ? 0.1980 0.1877 0.2293 -0.0188 0.0032  0.0268  801  IMP A N9    
2551 C  C8    . IMP B .   ? 0.2298 0.1934 0.2270 0.0052  -0.0011 0.0150  801  IMP A C8    
2552 N  N7    . IMP B .   ? 0.1999 0.2186 0.2225 0.0084  -0.0121 0.0173  801  IMP A N7    
2553 C  C5    . IMP B .   ? 0.1909 0.2018 0.2568 0.0157  -0.0117 0.0147  801  IMP A C5    
2554 C  C6    . IMP B .   ? 0.2250 0.2275 0.2734 -0.0283 0.0205  0.0297  801  IMP A C6    
2555 O  O6    . IMP B .   ? 0.1986 0.2550 0.2444 -0.0250 0.0288  0.0124  801  IMP A O6    
2556 N  N1    . IMP B .   ? 0.1934 0.2547 0.2836 -0.0380 0.0035  0.0147  801  IMP A N1    
2557 C  C2    . IMP B .   ? 0.2084 0.2651 0.2711 -0.0412 0.0198  0.0181  801  IMP A C2    
2558 N  N3    . IMP B .   ? 0.1867 0.2518 0.2557 -0.0131 -0.0028 -0.0020 801  IMP A N3    
2559 C  C4    . IMP B .   ? 0.1990 0.2208 0.2604 -0.0039 -0.0023 0.0234  801  IMP A C4    
2560 C  C4    . VOA C .   ? 0.1880 0.2066 0.2523 0.0065  0.0101  -0.0385 802  VOA A C4    
2561 C  C7    . VOA C .   ? 0.2296 0.1834 0.2146 0.0213  0.0032  -0.0252 802  VOA A C7    
2562 C  C8    . VOA C .   ? 0.2387 0.1638 0.2122 0.0029  0.0077  -0.0032 802  VOA A C8    
2563 C  C9    . VOA C .   ? 0.2223 0.2204 0.2017 -0.0007 -0.0039 -0.0058 802  VOA A C9    
2564 C  C10   . VOA C .   ? 0.2286 0.2233 0.2187 -0.0076 -0.0138 -0.0189 802  VOA A C10   
2565 C  C12   . VOA C .   ? 0.2505 0.2348 0.2144 0.0136  -0.0063 -0.0227 802  VOA A C12   
2566 C  C1    . VOA C .   ? 0.2188 0.2037 0.2991 0.0267  0.0281  0.0148  802  VOA A C1    
2567 C  C15   . VOA C .   ? 0.1640 0.2219 0.2591 -0.0169 0.0326  -0.0204 802  VOA A C15   
2568 C  C16   . VOA C .   ? 0.2166 0.2394 0.2823 -0.0078 -0.0107 -0.0063 802  VOA A C16   
2569 C  C17   . VOA C .   ? 0.1793 0.2281 0.2818 -0.0336 -0.0283 -0.0041 802  VOA A C17   
2570 C  C18   . VOA C .   ? 0.1900 0.1987 0.2816 -0.0531 -0.0179 -0.0207 802  VOA A C18   
2571 C  C19   . VOA C .   ? 0.2015 0.2071 0.2751 -0.0366 -0.0163 -0.0135 802  VOA A C19   
2572 C  C2    . VOA C .   ? 0.1935 0.2157 0.2656 -0.0116 0.0369  0.0074  802  VOA A C2    
2573 C  C20   . VOA C .   ? 0.1850 0.2142 0.2699 -0.0060 0.0177  -0.0166 802  VOA A C20   
2574 C  C21   . VOA C .   ? 0.1900 0.1986 0.2278 -0.0341 -0.0093 0.0155  802  VOA A C21   
2575 C  C22   . VOA C .   ? 0.2151 0.2031 0.2488 -0.0229 -0.0071 0.0118  802  VOA A C22   
2576 C  C23   . VOA C .   ? 0.2201 0.2027 0.2423 -0.0450 0.0103  0.0212  802  VOA A C23   
2577 C  C25   . VOA C .   ? 0.1995 0.2158 0.2209 0.0214  -0.0127 0.0128  802  VOA A C25   
2578 C  C27   . VOA C .   ? 0.2180 0.2207 0.2369 -0.0301 -0.0185 0.0079  802  VOA A C27   
2579 C  C28   . VOA C .   ? 0.2055 0.1804 0.2303 -0.0187 -0.0084 0.0138  802  VOA A C28   
2580 N  N11   . VOA C .   ? 0.2469 0.2452 0.2399 0.0151  -0.0290 -0.0090 802  VOA A N11   
2581 N  N14   . VOA C .   ? 0.2072 0.2456 0.2325 -0.0079 0.0212  -0.0204 802  VOA A N14   
2582 N  N24   . VOA C .   ? 0.2382 0.2171 0.2732 -0.0224 -0.0207 -0.0110 802  VOA A N24   
2583 N  N6    . VOA C .   ? 0.2072 0.1756 0.2466 0.0192  0.0164  -0.0212 802  VOA A N6    
2584 O  O26   . VOA C .   ? 0.2071 0.2124 0.2309 -0.0029 -0.0242 0.0082  802  VOA A O26   
2585 O  O5    . VOA C .   ? 0.1963 0.2451 0.2646 0.0203  -0.0075 -0.0457 802  VOA A O5    
2586 CL CL13  . VOA C .   ? 0.2309 0.2503 0.2650 0.0084  -0.0086 -0.0169 802  VOA A CL13  
2606 C  C4    . VOA D .   ? 0.3126 0.4063 0.4697 -0.0341 0.0572  0.0585  803  VOA A C4    
2607 C  C7    . VOA D .   ? 0.4232 0.4988 0.4556 0.0142  0.0047  -0.0146 803  VOA A C7    
2608 C  C8    . VOA D .   ? 0.4367 0.4974 0.4554 0.0618  0.0311  -0.0494 803  VOA A C8    
2609 C  C9    . VOA D .   ? 0.4390 0.4976 0.4267 0.0550  0.0157  -0.0604 803  VOA A C9    
2610 C  C10   . VOA D .   ? 0.4729 0.5394 0.4255 0.0213  0.0279  -0.0493 803  VOA A C10   
2611 C  C12   . VOA D .   ? 0.4514 0.5250 0.4434 0.0166  0.0096  -0.0191 803  VOA A C12   
2612 C  C1    . VOA D .   ? 0.4520 0.3746 0.4488 -0.0208 0.0777  0.0314  803  VOA A C1    
2613 C  C15   . VOA D .   ? 0.4131 0.5637 0.4862 0.1387  0.0783  0.1138  803  VOA A C15   
2614 C  C16   . VOA D .   ? 0.4191 0.6077 0.5016 0.1534  0.0619  0.1321  803  VOA A C16   
2615 C  C17   . VOA D .   ? 0.4394 0.6536 0.5066 0.1872  0.0550  0.1373  803  VOA A C17   
2616 C  C18   . VOA D .   ? 0.4968 0.6947 0.5185 0.1618  0.0634  0.1387  803  VOA A C18   
2617 C  C19   . VOA D .   ? 0.4948 0.6940 0.5148 0.1661  0.0633  0.1389  803  VOA A C19   
2618 C  C2    . VOA D .   ? 0.3842 0.4094 0.4634 0.0104  0.0807  0.0684  803  VOA A C2    
2619 C  C20   . VOA D .   ? 0.4623 0.6298 0.4876 0.1417  0.0656  0.1364  803  VOA A C20   
2620 C  C21   . VOA D .   ? 0.5231 0.7430 0.5357 0.1797  0.0565  0.1501  803  VOA A C21   
2621 C  C22   . VOA D .   ? 0.5333 0.7484 0.5481 0.1769  0.0533  0.1534  803  VOA A C22   
2622 C  C23   . VOA D .   ? 0.5364 0.7320 0.5425 0.1677  0.0599  0.1528  803  VOA A C23   
2623 C  C25   . VOA D .   ? 0.5343 0.7691 0.5639 0.1873  0.0615  0.1469  803  VOA A C25   
2624 C  C27   . VOA D .   ? 0.5290 0.7780 0.5567 0.2141  0.0526  0.1512  803  VOA A C27   
2625 C  C28   . VOA D .   ? 0.5348 0.7758 0.5520 0.1978  0.0482  0.1419  803  VOA A C28   
2626 N  N11   . VOA D .   ? 0.4587 0.5470 0.4327 0.0190  0.0173  -0.0188 803  VOA A N11   
2627 N  N14   . VOA D .   ? 0.3932 0.4627 0.4692 0.0801  0.0707  0.1000  803  VOA A N14   
2628 N  N24   . VOA D .   ? 0.5248 0.7166 0.5383 0.1605  0.0640  0.1416  803  VOA A N24   
2629 N  N6    . VOA D .   ? 0.3848 0.4707 0.4732 0.0000  0.0214  0.0181  803  VOA A N6    
2630 O  O26   . VOA D .   ? 0.5320 0.7786 0.5635 0.2082  0.0589  0.1378  803  VOA A O26   
2631 O  O5    . VOA D .   ? 0.2721 0.3805 0.4673 -0.0816 0.0693  0.0821  803  VOA A O5    
2632 CL CL13  . VOA D .   ? 0.4663 0.4803 0.4663 -0.0025 0.0108  -0.0194 803  VOA A CL13  
2652 C  C4    . VOA E .   ? 0.4141 0.4081 0.5023 0.0008  -0.0317 -0.0131 804  VOA A C4    
2653 C  C7    . VOA E .   ? 0.4618 0.4381 0.4992 0.0006  0.0498  0.0460  804  VOA A C7    
2654 C  C8    . VOA E .   ? 0.4746 0.4431 0.5025 -0.0088 0.0334  0.0590  804  VOA A C8    
2655 C  C9    . VOA E .   ? 0.4785 0.4566 0.5229 -0.0153 0.0207  0.0750  804  VOA A C9    
2656 C  C10   . VOA E .   ? 0.5050 0.4785 0.5480 0.0183  0.0340  0.0812  804  VOA A C10   
2657 C  C12   . VOA E .   ? 0.4768 0.4538 0.5149 0.0244  0.0695  0.0641  804  VOA A C12   
2658 C  C1    . VOA E .   ? 0.3990 0.3600 0.4802 -0.0305 -0.0668 -0.0481 804  VOA A C1    
2659 C  C15   . VOA E .   ? 0.4236 0.3660 0.4714 -0.0055 0.0179  -0.0276 804  VOA A C15   
2660 C  C16   . VOA E .   ? 0.4089 0.3554 0.4733 0.0200  0.0317  -0.0356 804  VOA A C16   
2661 C  C17   . VOA E .   ? 0.4255 0.3741 0.4680 0.0319  0.0498  -0.0336 804  VOA A C17   
2662 C  C18   . VOA E .   ? 0.4601 0.3933 0.4747 0.0002  0.0640  -0.0057 804  VOA A C18   
2663 C  C19   . VOA E .   ? 0.4714 0.3999 0.4731 -0.0282 0.0565  -0.0034 804  VOA A C19   
2664 C  C2    . VOA E .   ? 0.4122 0.3772 0.4857 -0.0267 -0.0443 -0.0317 804  VOA A C2    
2665 C  C20   . VOA E .   ? 0.4464 0.3899 0.4659 -0.0178 0.0457  -0.0243 804  VOA A C20   
2666 C  C21   . VOA E .   ? 0.5046 0.4278 0.4804 -0.0310 0.0725  0.0079  804  VOA A C21   
2667 C  C22   . VOA E .   ? 0.4993 0.4411 0.4784 -0.0406 0.0978  0.0097  804  VOA A C22   
2668 C  C23   . VOA E .   ? 0.4880 0.4256 0.4732 -0.0265 0.1020  0.0095  804  VOA A C23   
2669 C  C25   . VOA E .   ? 0.5181 0.4497 0.4827 -0.0265 0.0887  0.0022  804  VOA A C25   
2670 C  C27   . VOA E .   ? 0.5449 0.4498 0.4780 -0.0314 0.0837  0.0084  804  VOA A C27   
2671 C  C28   . VOA E .   ? 0.5200 0.4321 0.4851 -0.0378 0.0791  0.0097  804  VOA A C28   
2672 N  N11   . VOA E .   ? 0.4971 0.4522 0.5406 0.0168  0.0476  0.0871  804  VOA A N11   
2673 N  N14   . VOA E .   ? 0.4077 0.3852 0.4802 -0.0068 -0.0196 -0.0226 804  VOA A N14   
2674 N  N24   . VOA E .   ? 0.4893 0.4175 0.4827 0.0015  0.0843  0.0004  804  VOA A N24   
2675 N  N6    . VOA E .   ? 0.4305 0.4200 0.5055 0.0115  0.0222  0.0139  804  VOA A N6    
2676 O  O26   . VOA E .   ? 0.5537 0.4520 0.4739 -0.0308 0.0901  0.0042  804  VOA A O26   
2677 O  O5    . VOA E .   ? 0.4075 0.3985 0.5128 0.0193  -0.0678 0.0025  804  VOA A O5    
2678 CL CL13  . VOA E .   ? 0.5323 0.5323 0.5764 0.0262  0.0287  0.0821  804  VOA A CL13  
2698 S  S     . SO4 F .   ? 0.4247 0.7292 0.8359 -0.1573 0.0207  0.2736  805  SO4 A S     
2699 O  O1    . SO4 F .   ? 0.4845 0.7157 0.8320 -0.1524 0.0342  0.2884  805  SO4 A O1    
2700 O  O2    . SO4 F .   ? 0.4221 0.7610 0.8092 -0.1900 0.0158  0.3016  805  SO4 A O2    
2701 O  O3    . SO4 F .   ? 0.4160 0.7370 0.8381 -0.1350 0.0196  0.2583  805  SO4 A O3    
2702 O  O4    . SO4 F .   ? 0.4697 0.7577 0.8452 -0.1001 0.0628  0.2542  805  SO4 A O4    
2703 O  O     . HOH G .   ? 0.6442 0.8531 0.5276 0.1443  0.0806  -0.1810 901  HOH A O     
2704 O  O     . HOH G .   ? 0.2819 0.6249 0.4416 0.0069  0.0844  0.0619  902  HOH A O     
2705 O  O     . HOH G .   ? 0.7130 0.5590 0.5772 0.2149  0.3003  0.0393  903  HOH A O     
2706 O  O     . HOH G .   ? 0.5043 0.5706 0.7610 0.1144  0.1546  0.1510  904  HOH A O     
2707 O  O     . HOH G .   ? 0.2837 0.7436 0.5622 0.0054  0.0795  0.2312  905  HOH A O     
2708 O  O     . HOH G .   ? 0.6973 0.3922 0.6042 0.1335  0.2479  -0.0191 906  HOH A O     
2709 O  O     . HOH G .   ? 0.6000 0.4033 0.6631 0.1059  0.2236  0.0154  907  HOH A O     
2710 O  O     . HOH G .   ? 0.3123 0.3919 0.6408 -0.0373 0.1133  -0.0328 908  HOH A O     
2711 O  O     . HOH G .   ? 0.6267 0.3699 0.5727 0.0790  0.1474  -0.0168 909  HOH A O     
2712 O  O     . HOH G .   ? 0.6061 0.5313 0.8198 0.0014  -0.0006 0.0637  910  HOH A O     
2713 O  O     . HOH G .   ? 0.9672 0.6943 0.8051 -0.0228 0.1590  -0.0774 911  HOH A O     
2714 O  O     . HOH G .   ? 0.6060 0.5304 0.3057 0.0824  0.0866  -0.0876 912  HOH A O     
2715 O  O     . HOH G .   ? 0.3584 0.5326 0.8243 -0.1051 0.1810  -0.1408 913  HOH A O     
2716 O  O     . HOH G .   ? 0.4761 0.7229 0.5501 0.0281  0.1152  0.0876  914  HOH A O     
2717 O  O     . HOH G .   ? 0.5051 0.5225 0.4051 -0.0987 -0.0722 0.0370  915  HOH A O     
2718 O  O     . HOH G .   ? 0.4008 0.2024 0.6172 -0.0599 -0.1895 0.0646  916  HOH A O     
2719 O  O     . HOH G .   ? 0.3395 0.6948 0.4529 0.0387  0.0601  -0.1309 917  HOH A O     
2720 O  O     . HOH G .   ? 0.3891 0.7423 0.5272 0.1785  0.0067  0.1231  918  HOH A O     
2721 O  O     . HOH G .   ? 0.4185 0.5411 0.5917 -0.0630 0.1258  0.0486  919  HOH A O     
2722 O  O     . HOH G .   ? 0.3762 0.2587 0.3144 -0.0558 0.1487  -0.0132 920  HOH A O     
2723 O  O     . HOH G .   ? 0.5076 0.4776 0.8821 -0.0409 0.1504  -0.1102 921  HOH A O     
2724 O  O     . HOH G .   ? 0.6175 0.3060 0.3815 0.0870  0.0390  0.0136  922  HOH A O     
2725 O  O     . HOH G .   ? 0.5129 0.7286 0.6173 0.1788  0.1839  -0.1888 923  HOH A O     
2726 O  O     . HOH G .   ? 0.6065 0.4994 0.6238 -0.1764 0.1224  0.0086  924  HOH A O     
2727 O  O     . HOH G .   ? 0.2281 0.2185 0.4089 0.0415  -0.0422 0.0251  925  HOH A O     
2728 O  O     . HOH G .   ? 0.4282 0.4043 0.5264 0.0720  0.0672  -0.0212 926  HOH A O     
2729 O  O     . HOH G .   ? 0.5157 0.4532 0.5276 0.0830  0.0639  0.0719  927  HOH A O     
2730 O  O     . HOH G .   ? 0.5267 0.2871 0.6895 -0.0097 0.2175  -0.0764 928  HOH A O     
2731 O  O     . HOH G .   ? 0.6331 0.4013 0.4323 -0.1900 -0.1521 0.1010  929  HOH A O     
2732 O  O     . HOH G .   ? 0.5971 0.6748 0.6876 0.3079  0.0845  0.0678  930  HOH A O     
2733 O  O     . HOH G .   ? 0.3325 0.2700 0.3896 0.0604  -0.0369 0.0043  931  HOH A O     
2734 O  O     . HOH G .   ? 0.2618 0.2497 0.3314 0.0222  -0.0080 0.0269  932  HOH A O     
2735 O  O     . HOH G .   ? 0.4282 1.0731 0.4809 0.0803  0.0340  0.3031  933  HOH A O     
2736 O  O     . HOH G .   ? 0.5640 0.4851 0.6235 -0.0270 -0.0965 -0.0254 934  HOH A O     
2737 O  O     . HOH G .   ? 0.3806 0.6514 0.5047 0.0369  -0.1757 0.2033  935  HOH A O     
2738 O  O     . HOH G .   ? 0.2027 0.2495 0.2559 0.0024  0.0153  0.0321  936  HOH A O     
2739 O  O     . HOH G .   ? 0.3728 0.5211 0.6341 0.0668  0.0219  0.0098  937  HOH A O     
2740 O  O     . HOH G .   ? 0.6646 0.7384 0.4572 0.1414  -0.1460 -0.1900 938  HOH A O     
2741 O  O     . HOH G .   ? 0.3275 0.2973 0.2474 0.0394  0.0805  0.0230  939  HOH A O     
2742 O  O     . HOH G .   ? 0.1772 0.1864 0.3783 0.0036  0.0173  0.0195  940  HOH A O     
2743 O  O     . HOH G .   ? 0.3584 0.6836 0.3468 -0.1201 0.0386  -0.1712 941  HOH A O     
2744 O  O     . HOH G .   ? 0.3571 0.5706 0.3096 -0.0604 -0.0541 0.0979  942  HOH A O     
2745 O  O     . HOH G .   ? 0.2509 0.2423 0.2217 0.0306  0.0218  0.0000  943  HOH A O     
2746 O  O     . HOH G .   ? 0.4601 0.7781 0.8031 0.2044  -0.0544 0.1563  944  HOH A O     
2747 O  O     . HOH G .   ? 0.3484 0.2431 0.1790 -0.0218 -0.0232 0.0227  945  HOH A O     
2748 O  O     . HOH G .   ? 0.2422 0.2959 0.2585 -0.0214 -0.0433 0.0512  946  HOH A O     
2749 O  O     . HOH G .   ? 0.3840 0.2950 0.3556 -0.0265 -0.0311 0.0366  947  HOH A O     
2750 O  O     . HOH G .   ? 0.5317 0.5679 0.8240 0.0291  -0.1151 0.0962  948  HOH A O     
2751 O  O     . HOH G .   ? 0.2768 0.2462 0.2667 -0.0345 -0.0232 -0.0330 949  HOH A O     
2752 O  O     . HOH G .   ? 0.8514 0.3716 0.6112 -0.0774 0.1530  -0.0039 950  HOH A O     
2753 O  O     . HOH G .   ? 1.0576 0.7545 0.6808 -0.1046 0.0391  0.2314  951  HOH A O     
2754 O  O     . HOH G .   ? 0.4400 0.3820 0.5121 0.0828  0.1334  0.0714  952  HOH A O     
2755 O  O     . HOH G .   ? 0.2291 0.1938 0.2384 0.0180  -0.0040 0.0225  953  HOH A O     
2756 O  O     . HOH G .   ? 0.2650 0.3965 0.4467 -0.0053 -0.0920 0.0967  954  HOH A O     
2757 O  O     . HOH G .   ? 0.6307 0.5604 0.8102 -0.1241 0.0861  -0.0055 955  HOH A O     
2758 O  O     . HOH G .   ? 0.3239 0.3157 0.2363 -0.0372 0.0216  -0.0259 956  HOH A O     
2759 O  O     . HOH G .   ? 0.2575 0.2370 0.1823 0.0123  0.0165  -0.0006 957  HOH A O     
2760 O  O     . HOH G .   ? 0.2219 0.2014 0.2705 -0.0162 0.0139  -0.0161 958  HOH A O     
2761 O  O     . HOH G .   ? 0.3398 0.3807 0.2617 -0.0225 -0.0024 0.0518  959  HOH A O     
2762 O  O     . HOH G .   ? 0.2710 0.2404 0.2469 -0.0203 0.0037  -0.0207 960  HOH A O     
2763 O  O     . HOH G .   ? 0.4176 0.2775 0.5297 -0.0132 0.0408  -0.0063 961  HOH A O     
2764 O  O     . HOH G .   ? 0.6587 0.4186 0.5569 0.0396  -0.1107 0.1508  962  HOH A O     
2765 O  O     . HOH G .   ? 0.3960 0.3255 0.6294 -0.0383 -0.1164 0.0277  963  HOH A O     
2766 O  O     . HOH G .   ? 0.9222 0.3734 0.4066 0.0849  -0.1900 -0.0455 964  HOH A O     
2767 O  O     . HOH G .   ? 0.2194 0.2926 0.2986 -0.0174 -0.0015 0.0429  965  HOH A O     
2768 O  O     . HOH G .   ? 0.8830 0.2734 0.3313 -0.0561 -0.1000 0.0162  966  HOH A O     
2769 O  O     . HOH G .   ? 0.6153 0.4608 0.3235 0.0205  0.1451  0.1531  967  HOH A O     
2770 O  O     . HOH G .   ? 0.3308 0.3164 0.2801 0.0030  0.0098  0.0107  968  HOH A O     
2771 O  O     . HOH G .   ? 0.3794 0.3844 0.3021 -0.0892 -0.0303 -0.0658 969  HOH A O     
2772 O  O     . HOH G .   ? 0.1907 0.2987 0.2170 -0.0039 -0.0167 -0.0235 970  HOH A O     
2773 O  O     . HOH G .   ? 0.6744 0.3021 0.6375 -0.1816 -0.1795 0.1007  971  HOH A O     
2774 O  O     . HOH G .   ? 0.3336 0.3036 0.3583 0.0138  -0.0195 -0.0451 972  HOH A O     
2775 O  O     . HOH G .   ? 0.5340 0.4494 0.6304 -0.0984 -0.1303 0.2013  973  HOH A O     
2776 O  O     . HOH G .   ? 0.3488 0.2430 0.3188 -0.0365 0.0893  -0.0114 974  HOH A O     
2777 O  O     . HOH G .   ? 0.3238 0.2473 0.3252 -0.0255 -0.0729 0.0291  975  HOH A O     
2778 O  O     . HOH G .   ? 0.4589 0.5718 0.3467 -0.0821 -0.0397 0.0566  976  HOH A O     
2779 O  O     . HOH G .   ? 0.1981 0.2804 0.4376 0.0294  0.0282  0.0013  977  HOH A O     
2780 O  O     . HOH G .   ? 0.2113 0.2423 0.3748 0.0056  0.0092  0.0126  978  HOH A O     
2781 O  O     . HOH G .   ? 0.7725 0.4386 0.4433 -0.1866 0.1776  0.0967  979  HOH A O     
2782 O  O     . HOH G .   ? 0.4600 0.9749 0.6144 0.1585  0.0021  -0.1900 980  HOH A O     
2783 O  O     . HOH G .   ? 0.2421 0.4034 0.7293 0.0054  0.0253  0.1733  981  HOH A O     
2784 O  O     . HOH G .   ? 0.2573 0.4046 0.5034 0.0239  0.0803  -0.0341 982  HOH A O     
2785 O  O     . HOH G .   ? 0.2168 0.2077 0.2460 0.0071  -0.0141 -0.0110 983  HOH A O     
2786 O  O     . HOH G .   ? 0.5690 0.2836 0.2389 -0.1179 -0.0032 0.0219  984  HOH A O     
2787 O  O     . HOH G .   ? 0.5134 0.3573 0.6622 -0.1161 -0.1489 -0.1459 985  HOH A O     
2788 O  O     . HOH G .   ? 0.7631 0.6291 0.5898 0.3360  0.0423  -0.1003 986  HOH A O     
2789 O  O     . HOH G .   ? 0.3532 0.5598 0.5715 0.0822  0.0598  0.0147  987  HOH A O     
2790 O  O     . HOH G .   ? 0.1529 0.2638 0.2311 0.0220  0.0078  0.0363  988  HOH A O     
2791 O  O     . HOH G .   ? 0.2958 0.2590 0.3171 -0.0218 -0.1050 -0.0405 989  HOH A O     
2792 O  O     . HOH G .   ? 0.4293 0.3986 0.5004 -0.1473 -0.0472 0.0319  990  HOH A O     
2793 O  O     . HOH G .   ? 0.4301 0.5733 0.2099 -0.1396 0.0376  0.0385  991  HOH A O     
2794 O  O     . HOH G .   ? 0.2889 0.3601 0.2952 -0.0658 0.0680  0.0384  992  HOH A O     
2795 O  O     . HOH G .   ? 0.2204 0.2924 0.2460 0.0188  0.0265  -0.0024 993  HOH A O     
2796 O  O     . HOH G .   ? 0.2327 0.2187 0.2572 -0.0134 -0.0076 0.0264  994  HOH A O     
2797 O  O     . HOH G .   ? 0.2946 0.2686 0.4826 0.0008  0.0155  0.0026  995  HOH A O     
2798 O  O     . HOH G .   ? 0.3553 0.6207 0.6362 -0.1900 -0.0534 0.2094  996  HOH A O     
2799 O  O     . HOH G .   ? 0.4190 0.6484 0.6704 -0.0345 -0.0769 0.3109  997  HOH A O     
2800 O  O     . HOH G .   ? 0.2934 0.2919 0.2218 0.0563  -0.0218 -0.0226 998  HOH A O     
2801 O  O     . HOH G .   ? 0.4956 0.3296 0.6115 0.0581  -0.1315 0.0809  999  HOH A O     
2802 O  O     . HOH G .   ? 0.5733 0.6883 0.6308 -0.0280 -0.0329 0.1692  1000 HOH A O     
2803 O  O     . HOH G .   ? 0.2771 0.2961 0.3161 -0.0330 -0.0641 -0.0085 1001 HOH A O     
2804 O  O     . HOH G .   ? 0.2298 0.1948 0.2057 -0.0067 0.0142  -0.0144 1002 HOH A O     
2805 O  O     . HOH G .   ? 0.5820 0.7948 0.5493 0.0699  -0.0564 0.1628  1003 HOH A O     
2806 O  O     . HOH G .   ? 0.2905 0.4152 0.5888 -0.0259 -0.0872 -0.0320 1004 HOH A O     
2807 O  O     . HOH G .   ? 0.4896 0.8799 0.5781 0.1903  0.0161  0.3106  1005 HOH A O     
2808 O  O     . HOH G .   ? 0.7037 0.3879 0.4455 -0.0024 0.0229  0.1198  1006 HOH A O     
2809 O  O     . HOH G .   ? 0.4830 0.8245 0.4215 -0.0442 -0.0695 -0.0834 1007 HOH A O     
2810 O  O     . HOH G .   ? 0.2547 0.2586 0.4451 0.0034  0.0199  0.1506  1008 HOH A O     
2811 O  O     . HOH G .   ? 0.2529 0.2669 0.3411 0.0254  0.0061  -0.0375 1009 HOH A O     
2812 O  O     . HOH G .   ? 0.3647 0.3087 0.5056 -0.0102 -0.1853 0.0101  1010 HOH A O     
2813 O  O     . HOH G .   ? 0.4534 0.4292 0.5041 -0.1896 0.0458  0.1165  1011 HOH A O     
2814 O  O     . HOH G .   ? 0.4071 0.3197 0.5878 -0.0847 -0.0250 -0.1476 1012 HOH A O     
2815 O  O     . HOH G .   ? 0.2870 0.3290 0.4168 -0.0314 0.0565  0.0525  1013 HOH A O     
2816 O  O     . HOH G .   ? 0.3906 0.8159 0.4454 0.0525  0.0292  -0.0571 1014 HOH A O     
2817 O  O     . HOH G .   ? 0.3590 0.4419 0.3760 -0.0152 -0.1296 0.0088  1015 HOH A O     
2818 O  O     . HOH G .   ? 0.5404 0.8300 0.4942 0.2720  -0.1900 -0.0936 1016 HOH A O     
2819 O  O     . HOH G .   ? 0.5851 0.2334 0.6252 0.0494  0.2938  0.0315  1017 HOH A O     
2820 O  O     . HOH G .   ? 0.7242 0.7242 0.5048 -0.0983 -0.0057 0.0023  1018 HOH A O     
2821 O  O     . HOH G .   ? 0.5435 0.4686 0.2088 -0.1045 -0.0375 -0.0491 1019 HOH A O     
2822 O  O     . HOH G .   ? 0.3444 0.3292 0.2788 -0.0327 0.0455  -0.0159 1020 HOH A O     
2823 O  O     . HOH G .   ? 0.3607 0.5281 0.2891 -0.1036 0.0286  -0.0534 1021 HOH A O     
2824 O  O     . HOH G .   ? 0.3289 0.2451 0.2989 -0.0339 -0.0515 0.0293  1022 HOH A O     
2825 O  O     . HOH G .   ? 0.4231 0.2063 0.2221 0.0356  0.0236  0.0447  1023 HOH A O     
2826 O  O     . HOH G .   ? 0.2626 0.2004 0.2923 0.0060  -0.0185 -0.0112 1024 HOH A O     
2827 O  O     . HOH G .   ? 0.4090 0.2434 0.5992 0.0170  0.0772  0.0426  1025 HOH A O     
2828 O  O     . HOH G .   ? 0.2516 0.2301 0.7159 -0.0194 -0.1560 -0.0141 1026 HOH A O     
2829 O  O     . HOH G .   ? 0.7738 0.3040 0.4472 -0.0788 -0.0887 0.1163  1027 HOH A O     
2830 O  O     . HOH G .   ? 0.2828 0.2124 0.2395 -0.0128 0.0411  0.0078  1028 HOH A O     
2831 O  O     . HOH G .   ? 0.6002 0.5916 0.4038 -0.1688 0.0844  -0.0877 1029 HOH A O     
2832 O  O     . HOH G .   ? 0.2412 0.2391 0.1982 -0.0070 -0.0311 0.0317  1030 HOH A O     
2833 O  O     . HOH G .   ? 0.7456 0.6833 0.5077 -0.0954 -0.1900 -0.0488 1031 HOH A O     
2834 O  O     . HOH G .   ? 0.4170 0.4045 0.3531 0.1066  0.0808  -0.0192 1032 HOH A O     
2835 O  O     . HOH G .   ? 0.3399 0.3317 0.3288 -0.0147 0.0549  -0.0400 1033 HOH A O     
2836 O  O     . HOH G .   ? 0.2857 0.3124 0.2904 -0.0017 0.0451  0.0078  1034 HOH A O     
2837 O  O     . HOH G .   ? 0.4883 0.4395 0.5894 0.0125  -0.0071 -0.1900 1035 HOH A O     
2838 O  O     . HOH G .   ? 0.6215 0.5148 0.5168 -0.0655 -0.0120 0.0752  1036 HOH A O     
2839 O  O     . HOH G .   ? 0.3360 0.7902 0.3766 -0.1540 -0.0445 -0.0554 1037 HOH A O     
2840 O  O     . HOH G .   ? 0.2573 0.3804 0.5193 -0.0024 -0.0795 0.1156  1038 HOH A O     
2841 O  O     . HOH G .   ? 0.3030 0.2833 0.3088 -0.0056 0.0385  0.0046  1039 HOH A O     
2842 O  O     . HOH G .   ? 0.2553 0.2463 0.3674 -0.0214 -0.0034 0.0752  1040 HOH A O     
2843 O  O     . HOH G .   ? 0.3188 0.2453 0.9445 0.0057  0.0099  -0.0697 1041 HOH A O     
2844 O  O     . HOH G .   ? 0.3455 0.2512 0.4872 0.0001  -0.1150 0.0242  1042 HOH A O     
2845 O  O     . HOH G .   ? 0.5046 0.3949 0.4794 0.0460  0.0047  0.0875  1043 HOH A O     
2846 O  O     . HOH G .   ? 0.3028 0.4046 0.7057 0.0895  -0.0346 -0.0716 1044 HOH A O     
2847 O  O     . HOH G .   ? 0.9054 0.4220 0.4034 0.1813  -0.0527 0.1256  1045 HOH A O     
2848 O  O     . HOH G .   ? 0.4714 0.4263 0.6838 0.0956  -0.0759 0.1301  1046 HOH A O     
2849 O  O     . HOH G .   ? 0.4440 0.8416 0.5639 -0.1854 -0.1850 0.1938  1047 HOH A O     
2850 O  O     . HOH G .   ? 0.4639 0.9350 0.4362 0.0792  0.0603  0.0910  1048 HOH A O     
2851 O  O     . HOH G .   ? 0.9482 0.6872 0.6081 -0.0992 0.0250  0.3286  1049 HOH A O     
2852 O  O     . HOH G .   ? 0.3744 0.3151 0.6433 -0.0191 -0.0985 -0.0536 1050 HOH A O     
2853 O  O     . HOH G .   ? 0.7797 0.3789 0.4293 -0.1377 0.1621  -0.1363 1051 HOH A O     
2854 O  O     . HOH G .   ? 0.3519 0.4517 0.5183 -0.0681 -0.0061 -0.0995 1052 HOH A O     
2855 O  O     . HOH G .   ? 0.2997 0.2718 0.2606 0.0052  -0.0398 -0.0243 1053 HOH A O     
2856 O  O     . HOH G .   ? 0.3250 0.2338 0.4607 -0.0070 0.0416  0.0228  1054 HOH A O     
2857 O  O     . HOH G .   ? 0.8839 0.6853 0.4734 0.0285  -0.0896 0.1843  1055 HOH A O     
2858 O  O     . HOH G .   ? 0.5884 0.5386 0.4698 -0.1281 -0.1900 0.0883  1056 HOH A O     
2859 O  O     . HOH G .   ? 0.7948 0.7929 0.5894 0.3106  -0.1900 0.0553  1057 HOH A O     
2860 O  O     . HOH G .   ? 0.6211 0.5408 0.6222 -0.0215 0.2298  -0.1900 1058 HOH A O     
2861 O  O     . HOH G .   ? 0.8344 0.4916 0.8458 -0.0819 0.1457  -0.1855 1059 HOH A O     
2862 O  O     . HOH G .   ? 0.3819 0.5262 0.6182 0.0405  0.1088  0.1074  1060 HOH A O     
2863 O  O     . HOH G .   ? 0.5449 0.9181 0.4323 0.1998  -0.1704 -0.1585 1061 HOH A O     
2864 O  O     . HOH G .   ? 0.2848 0.2534 0.3178 -0.0058 0.0043  0.0314  1062 HOH A O     
2865 O  O     . HOH G .   ? 0.7069 0.8094 0.7027 -0.0320 -0.0750 -0.0589 1063 HOH A O     
2866 O  O     . HOH G .   ? 0.6037 0.5383 0.5040 -0.1686 0.0363  0.0465  1064 HOH A O     
2867 O  O     . HOH G .   ? 0.5904 0.5734 0.4250 0.0732  -0.0199 -0.1438 1065 HOH A O     
2868 O  O     . HOH G .   ? 0.7284 0.6197 0.5182 -0.1543 0.2430  0.1008  1066 HOH A O     
2869 O  O     . HOH G .   ? 0.6979 0.8995 0.6155 0.2366  -0.0805 0.2315  1067 HOH A O     
2870 O  O     . HOH G .   ? 0.4892 0.4920 0.4806 0.0142  -0.0140 0.0087  1068 HOH A O     
2871 O  O     . HOH G .   ? 0.2872 0.2685 0.3879 0.0108  -0.0191 -0.0077 1069 HOH A O     
2872 O  O     . HOH G .   ? 0.5425 0.5596 0.5084 0.0176  0.0633  -0.0638 1070 HOH A O     
2873 O  O     . HOH G .   ? 0.4481 0.6279 0.5135 -0.0501 -0.0867 0.0624  1071 HOH A O     
2874 O  O     . HOH G .   ? 0.7483 0.6758 0.5508 0.0420  -0.1500 0.0551  1072 HOH A O     
2875 O  O     . HOH G .   ? 0.4261 0.4768 0.7292 -0.0783 0.0572  0.0760  1073 HOH A O     
2876 O  O     . HOH G .   ? 0.3115 0.4269 0.3796 -0.0016 0.0116  -0.0953 1074 HOH A O     
2877 O  O     . HOH G .   ? 0.6167 0.4603 0.5161 -0.0524 0.2711  -0.0651 1075 HOH A O     
2878 O  O     . HOH G .   ? 0.7273 0.4321 0.6399 -0.1900 0.0097  0.0507  1076 HOH A O     
2879 O  O     . HOH G .   ? 0.3947 0.5569 0.5380 -0.1148 0.0017  -0.1385 1077 HOH A O     
2880 O  O     . HOH G .   ? 0.3839 0.3886 0.2461 -0.0121 0.0525  0.0509  1078 HOH A O     
2881 O  O     . HOH G .   ? 0.5906 0.4282 0.7492 0.1098  -0.1352 -0.0314 1079 HOH A O     
2882 O  O     . HOH G .   ? 0.6363 0.5634 0.7758 0.0881  0.1643  0.3708  1080 HOH A O     
2883 O  O     . HOH G .   ? 0.5090 0.5097 0.5715 0.0761  0.0496  0.1747  1081 HOH A O     
2884 O  O     . HOH G .   ? 0.4297 0.4372 0.8063 -0.0081 -0.1900 0.0582  1082 HOH A O     
2885 O  O     . HOH G .   ? 0.7682 0.5735 0.6300 -0.0349 0.3065  0.0363  1083 HOH A O     
2886 O  O     . HOH G .   ? 0.5361 0.7327 0.4541 -0.0132 0.1809  -0.1800 1084 HOH A O     
2887 O  O     . HOH G .   ? 0.4256 0.3491 0.4300 0.0393  0.1398  0.0208  1085 HOH A O     
2888 O  O     . HOH G .   ? 0.4516 0.9895 0.7870 0.1478  0.0797  -0.0042 1086 HOH A O     
2889 O  O     . HOH G .   ? 0.7098 0.3229 0.7360 0.0327  -0.1900 -0.0719 1087 HOH A O     
2890 O  O     . HOH G .   ? 0.6252 0.5339 0.5098 0.1927  0.0255  0.0794  1088 HOH A O     
2891 O  O     . HOH G .   ? 0.3842 0.7253 0.8142 -0.0921 -0.1098 0.1412  1089 HOH A O     
2892 O  O     . HOH G .   ? 0.8548 0.6219 0.6654 -0.1555 0.0187  -0.0485 1090 HOH A O     
2893 O  O     . HOH G .   ? 0.2871 0.4595 0.2941 -0.0088 0.0304  -0.1031 1091 HOH A O     
2894 O  O     . HOH G .   ? 0.5654 0.6368 0.3079 0.1658  -0.0686 -0.1345 1092 HOH A O     
2895 O  O     . HOH G .   ? 0.5936 0.8345 0.5147 -0.0433 -0.1687 -0.0767 1093 HOH A O     
2896 O  O     . HOH G .   ? 0.5883 0.5551 0.7063 0.1992  0.1255  -0.1007 1094 HOH A O     
2897 O  O     . HOH G .   ? 0.6216 0.3333 0.4255 0.0779  -0.1344 0.0534  1095 HOH A O     
2898 O  O     . HOH G .   ? 0.5173 0.5758 0.6201 0.0869  0.2284  -0.0821 1096 HOH A O     
2899 O  O     . HOH G .   ? 0.6435 0.5881 0.6923 -0.0092 0.0000  0.0000  1097 HOH A O     
2900 O  O     . HOH G .   ? 0.4842 0.6274 0.4688 -0.0090 0.1659  -0.1230 1098 HOH A O     
2901 O  O     . HOH G .   ? 0.6987 0.4269 0.4805 -0.1900 0.0192  -0.0500 1099 HOH A O     
2902 O  O     . HOH G .   ? 0.7592 0.6906 0.8257 -0.1866 0.2254  0.0459  1100 HOH A O     
2903 O  O     . HOH G .   ? 0.4771 0.6691 0.7189 -0.0057 0.0319  -0.1171 1101 HOH A O     
2904 O  O     . HOH G .   ? 0.7412 0.6673 0.6160 -0.0029 0.0136  -0.0793 1102 HOH A O     
2905 O  O     . HOH G .   ? 0.5743 0.3754 0.9166 -0.1900 0.0527  -0.0593 1103 HOH A O     
# 
