data_1T0O # _entry.id 1T0O # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 1T0O RCSB RCSB022165 WWPDB D_1000022165 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 1SZN 'THE STRUCTURE OF ALPHA-GALACTOSIDASE' unspecified BMCD C1RN 'Crystallization Data for Molecule - galactosidase, alpha-' unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 1T0O _pdbx_database_status.recvd_initial_deposition_date 2004-04-12 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf REL _pdbx_database_status.SG_entry . _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Golubev, A.M.' 1 'Nagem, R.A.P.' 2 'Brandao Neto, J.R.' 3 'Neustroev, K.N.' 4 'Eneyskaya, E.V.' 5 'Kulminskaya, A.A.' 6 'Shabalin, K.A.' 7 ;Savel'ev, A.N. ; 8 'Polikarpov, I.' 9 # loop_ _citation.id _citation.title _citation.journal_abbrev _citation.journal_volume _citation.page_first _citation.page_last _citation.year _citation.journal_id_ASTM _citation.country _citation.journal_id_ISSN _citation.journal_id_CSD _citation.book_publisher _citation.pdbx_database_id_PubMed _citation.pdbx_database_id_DOI primary ;Crystal structure of alpha-galactosidase from Trichoderma reesei and its complex with galactose: implications for catalytic mechanism ; J.Mol.Biol. 339 413 422 2004 JMOBAK UK 0022-2836 0070 ? 15136043 10.1016/j.jmb.2004.03.062 1 'Crystallization of alpha-galactosidase from Trichoderma reesei.' J.Mol.Biol. 231 933 934 1993 JMOBAK UK 0022-2836 0070 ? ? 10.1006/jmbi.1993.1340 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Golubev, A.M.' 1 primary 'Nagem, R.A.P.' 2 primary 'Brandao Neto, J.R.' 3 primary 'Neustroev, K.N.' 4 primary 'Eneyskaya, E.V.' 5 primary 'Kulminskaya, A.A.' 6 primary 'Shabalin, K.A.' 7 primary ;Savel'ev, A.N. ; 8 primary 'Polikarpov, I.' 9 1 'Golubev, A.M.' 10 1 'Neustroev, K.N.' 11 # _cell.entry_id 1T0O _cell.length_a 57.834 _cell.length_b 58.313 _cell.length_c 153.660 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1T0O _symmetry.space_group_name_H-M 'P 21 21 21' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 19 _symmetry.space_group_name_Hall ? # 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 nat alpha-galactosidase 45610.863 1 3.2.1.22 ? ? ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 8 ? ? ? ? 3 non-polymer man BETA-D-MANNOSE 180.156 2 ? ? ? ? 4 non-polymer man ALPHA-D-MANNOSE 180.156 5 ? ? ? ? 5 non-polymer man BETA-D-GALACTOSE 180.156 1 ? ? ? ? 6 water nat water 18.015 384 ? ? ? ? # _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 ;IVMPDGVTGKVPSLGWNSWNAYHCDIDESKFLSAAELIVSSGLLDAGYNYVNIDDCWSMKDGRVDGHIAPNATRFPDGID GLAKKVHALGLKLGIYSTAGTATCAGYPASLGYEDVDAADFADWGVDYLKYDNCNVPSDWQDEYVACNPDFVKTGPNGTC TTALDPTLAPPGYDWSTSKSAERFGAMRNALAKQSHEIVLSMCIWGQADVFSWGNSTGISWRMSDDISPNWGSVTRILNL NSFKLNSVDFWGHNDADMLEVGNGNLTAAETRTHFALWAAMKSPLLIGTDLAQLSQNNINLLKNKHLLAFNQDSVYGQPA TPYKWGINPDWTFNVTYPAEFWAGPSSKGHLVLMVNTLDITATKEAKWNEIPGLSAGHYEVRDVWSDKDLGCLSSYKAAV AAHDTAVILVGKKCQRW ; _entity_poly.pdbx_seq_one_letter_code_can ;IVMPDGVTGKVPSLGWNSWNAYHCDIDESKFLSAAELIVSSGLLDAGYNYVNIDDCWSMKDGRVDGHIAPNATRFPDGID GLAKKVHALGLKLGIYSTAGTATCAGYPASLGYEDVDAADFADWGVDYLKYDNCNVPSDWQDEYVACNPDFVKTGPNGTC TTALDPTLAPPGYDWSTSKSAERFGAMRNALAKQSHEIVLSMCIWGQADVFSWGNSTGISWRMSDDISPNWGSVTRILNL NSFKLNSVDFWGHNDADMLEVGNGNLTAAETRTHFALWAAMKSPLLIGTDLAQLSQNNINLLKNKHLLAFNQDSVYGQPA TPYKWGINPDWTFNVTYPAEFWAGPSSKGHLVLMVNTLDITATKEAKWNEIPGLSAGHYEVRDVWSDKDLGCLSSYKAAV AAHDTAVILVGKKCQRW ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ILE n 1 2 VAL n 1 3 MET n 1 4 PRO n 1 5 ASP n 1 6 GLY n 1 7 VAL n 1 8 THR n 1 9 GLY n 1 10 LYS n 1 11 VAL n 1 12 PRO n 1 13 SER n 1 14 LEU n 1 15 GLY n 1 16 TRP n 1 17 ASN n 1 18 SER n 1 19 TRP n 1 20 ASN n 1 21 ALA n 1 22 TYR n 1 23 HIS n 1 24 CYS n 1 25 ASP n 1 26 ILE n 1 27 ASP n 1 28 GLU n 1 29 SER n 1 30 LYS n 1 31 PHE n 1 32 LEU n 1 33 SER n 1 34 ALA n 1 35 ALA n 1 36 GLU n 1 37 LEU n 1 38 ILE n 1 39 VAL n 1 40 SER n 1 41 SER n 1 42 GLY n 1 43 LEU n 1 44 LEU n 1 45 ASP n 1 46 ALA n 1 47 GLY n 1 48 TYR n 1 49 ASN n 1 50 TYR n 1 51 VAL n 1 52 ASN n 1 53 ILE n 1 54 ASP n 1 55 ASP n 1 56 CYS n 1 57 TRP n 1 58 SER n 1 59 MET n 1 60 LYS n 1 61 ASP n 1 62 GLY n 1 63 ARG n 1 64 VAL n 1 65 ASP n 1 66 GLY n 1 67 HIS n 1 68 ILE n 1 69 ALA n 1 70 PRO n 1 71 ASN n 1 72 ALA n 1 73 THR n 1 74 ARG n 1 75 PHE n 1 76 PRO n 1 77 ASP n 1 78 GLY n 1 79 ILE n 1 80 ASP n 1 81 GLY n 1 82 LEU n 1 83 ALA n 1 84 LYS n 1 85 LYS n 1 86 VAL n 1 87 HIS n 1 88 ALA n 1 89 LEU n 1 90 GLY n 1 91 LEU n 1 92 LYS n 1 93 LEU n 1 94 GLY n 1 95 ILE n 1 96 TYR n 1 97 SER n 1 98 THR n 1 99 ALA n 1 100 GLY n 1 101 THR n 1 102 ALA n 1 103 THR n 1 104 CYS n 1 105 ALA n 1 106 GLY n 1 107 TYR n 1 108 PRO n 1 109 ALA n 1 110 SER n 1 111 LEU n 1 112 GLY n 1 113 TYR n 1 114 GLU n 1 115 ASP n 1 116 VAL n 1 117 ASP n 1 118 ALA n 1 119 ALA n 1 120 ASP n 1 121 PHE n 1 122 ALA n 1 123 ASP n 1 124 TRP n 1 125 GLY n 1 126 VAL n 1 127 ASP n 1 128 TYR n 1 129 LEU n 1 130 LYS n 1 131 TYR n 1 132 ASP n 1 133 ASN n 1 134 CYS n 1 135 ASN n 1 136 VAL n 1 137 PRO n 1 138 SER n 1 139 ASP n 1 140 TRP n 1 141 GLN n 1 142 ASP n 1 143 GLU n 1 144 TYR n 1 145 VAL n 1 146 ALA n 1 147 CYS n 1 148 ASN n 1 149 PRO n 1 150 ASP n 1 151 PHE n 1 152 VAL n 1 153 LYS n 1 154 THR n 1 155 GLY n 1 156 PRO n 1 157 ASN n 1 158 GLY n 1 159 THR n 1 160 CYS n 1 161 THR n 1 162 THR n 1 163 ALA n 1 164 LEU n 1 165 ASP n 1 166 PRO n 1 167 THR n 1 168 LEU n 1 169 ALA n 1 170 PRO n 1 171 PRO n 1 172 GLY n 1 173 TYR n 1 174 ASP n 1 175 TRP n 1 176 SER n 1 177 THR n 1 178 SER n 1 179 LYS n 1 180 SER n 1 181 ALA n 1 182 GLU n 1 183 ARG n 1 184 PHE n 1 185 GLY n 1 186 ALA n 1 187 MET n 1 188 ARG n 1 189 ASN n 1 190 ALA n 1 191 LEU n 1 192 ALA n 1 193 LYS n 1 194 GLN n 1 195 SER n 1 196 HIS n 1 197 GLU n 1 198 ILE n 1 199 VAL n 1 200 LEU n 1 201 SER n 1 202 MET n 1 203 CYS n 1 204 ILE n 1 205 TRP n 1 206 GLY n 1 207 GLN n 1 208 ALA n 1 209 ASP n 1 210 VAL n 1 211 PHE n 1 212 SER n 1 213 TRP n 1 214 GLY n 1 215 ASN n 1 216 SER n 1 217 THR n 1 218 GLY n 1 219 ILE n 1 220 SER n 1 221 TRP n 1 222 ARG n 1 223 MET n 1 224 SER n 1 225 ASP n 1 226 ASP n 1 227 ILE n 1 228 SER n 1 229 PRO n 1 230 ASN n 1 231 TRP n 1 232 GLY n 1 233 SER n 1 234 VAL n 1 235 THR n 1 236 ARG n 1 237 ILE n 1 238 LEU n 1 239 ASN n 1 240 LEU n 1 241 ASN n 1 242 SER n 1 243 PHE n 1 244 LYS n 1 245 LEU n 1 246 ASN n 1 247 SER n 1 248 VAL n 1 249 ASP n 1 250 PHE n 1 251 TRP n 1 252 GLY n 1 253 HIS n 1 254 ASN n 1 255 ASP n 1 256 ALA n 1 257 ASP n 1 258 MET n 1 259 LEU n 1 260 GLU n 1 261 VAL n 1 262 GLY n 1 263 ASN n 1 264 GLY n 1 265 ASN n 1 266 LEU n 1 267 THR n 1 268 ALA n 1 269 ALA n 1 270 GLU n 1 271 THR n 1 272 ARG n 1 273 THR n 1 274 HIS n 1 275 PHE n 1 276 ALA n 1 277 LEU n 1 278 TRP n 1 279 ALA n 1 280 ALA n 1 281 MET n 1 282 LYS n 1 283 SER n 1 284 PRO n 1 285 LEU n 1 286 LEU n 1 287 ILE n 1 288 GLY n 1 289 THR n 1 290 ASP n 1 291 LEU n 1 292 ALA n 1 293 GLN n 1 294 LEU n 1 295 SER n 1 296 GLN n 1 297 ASN n 1 298 ASN n 1 299 ILE n 1 300 ASN n 1 301 LEU n 1 302 LEU n 1 303 LYS n 1 304 ASN n 1 305 LYS n 1 306 HIS n 1 307 LEU n 1 308 LEU n 1 309 ALA n 1 310 PHE n 1 311 ASN n 1 312 GLN n 1 313 ASP n 1 314 SER n 1 315 VAL n 1 316 TYR n 1 317 GLY n 1 318 GLN n 1 319 PRO n 1 320 ALA n 1 321 THR n 1 322 PRO n 1 323 TYR n 1 324 LYS n 1 325 TRP n 1 326 GLY n 1 327 ILE n 1 328 ASN n 1 329 PRO n 1 330 ASP n 1 331 TRP n 1 332 THR n 1 333 PHE n 1 334 ASN n 1 335 VAL n 1 336 THR n 1 337 TYR n 1 338 PRO n 1 339 ALA n 1 340 GLU n 1 341 PHE n 1 342 TRP n 1 343 ALA n 1 344 GLY n 1 345 PRO n 1 346 SER n 1 347 SER n 1 348 LYS n 1 349 GLY n 1 350 HIS n 1 351 LEU n 1 352 VAL n 1 353 LEU n 1 354 MET n 1 355 VAL n 1 356 ASN n 1 357 THR n 1 358 LEU n 1 359 ASP n 1 360 ILE n 1 361 THR n 1 362 ALA n 1 363 THR n 1 364 LYS n 1 365 GLU n 1 366 ALA n 1 367 LYS n 1 368 TRP n 1 369 ASN n 1 370 GLU n 1 371 ILE n 1 372 PRO n 1 373 GLY n 1 374 LEU n 1 375 SER n 1 376 ALA n 1 377 GLY n 1 378 HIS n 1 379 TYR n 1 380 GLU n 1 381 VAL n 1 382 ARG n 1 383 ASP n 1 384 VAL n 1 385 TRP n 1 386 SER n 1 387 ASP n 1 388 LYS n 1 389 ASP n 1 390 LEU n 1 391 GLY n 1 392 CYS n 1 393 LEU n 1 394 SER n 1 395 SER n 1 396 TYR n 1 397 LYS n 1 398 ALA n 1 399 ALA n 1 400 VAL n 1 401 ALA n 1 402 ALA n 1 403 HIS n 1 404 ASP n 1 405 THR n 1 406 ALA n 1 407 VAL n 1 408 ILE n 1 409 LEU n 1 410 VAL n 1 411 GLY n 1 412 LYS n 1 413 LYS n 1 414 CYS n 1 415 GLN n 1 416 ARG n 1 417 TRP n # _entity_src_nat.entity_id 1 _entity_src_nat.pdbx_src_id 1 _entity_src_nat.pdbx_alt_source_flag sample _entity_src_nat.pdbx_beg_seq_num ? _entity_src_nat.pdbx_end_seq_num ? _entity_src_nat.common_name ? _entity_src_nat.pdbx_organism_scientific 'Hypocrea jecorina' _entity_src_nat.pdbx_ncbi_taxonomy_id 51453 _entity_src_nat.genus Hypocrea _entity_src_nat.species ? _entity_src_nat.strain ? _entity_src_nat.tissue ? _entity_src_nat.tissue_fraction ? _entity_src_nat.pdbx_secretion ? _entity_src_nat.pdbx_fragment ? _entity_src_nat.pdbx_variant ? _entity_src_nat.pdbx_cell_line ? _entity_src_nat.pdbx_atcc ? _entity_src_nat.pdbx_cellular_location ? _entity_src_nat.pdbx_organ ? _entity_src_nat.pdbx_organelle ? _entity_src_nat.pdbx_cell ? _entity_src_nat.pdbx_plasmid_name ? _entity_src_nat.pdbx_plasmid_details ? _entity_src_nat.details ? # _struct_ref.id 1 _struct_ref.db_name GB _struct_ref.db_code CAA93244 _struct_ref.pdbx_db_accession 1580816 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;IVMPDGVTGKVPSLGWNSWNAYHCDIDESKFLSAAEVIVSSGLLDAGYNYVNIDDCWSMKDGRVDGHIAVNTTRFPDGID GLAKKVHDLGLKLGIYSTAGTATCAGYPASLGYEDVDAADFADWGVDYLKYDNCNVPSDWQDEYVACAPDAVQTGPNGTC STALEPNLAPPGYDWSTSKSAERFNAMRNALAKQSREIVLSLCIWGVADVFSWGNETGISWRMSGDISPEWGSVTHIINM NSFKMNSVGFWGHNDADILEVGNGNLTAAETRTHFALWAAMKSPLLIGTDLAQLSQENIELLKNKHLLAFNQDSVYGQPA TPYKWGVNPDWTFNYTNPAEYWAGPSSKGHLVLMMNTLDHTVRKEAKWSEIPGLSAGRYEVRDVWTDKSLGCLSSYKTAV AAHDTAVILVGKKCRNW ; _struct_ref.pdbx_align_begin 28 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 1T0O _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 1 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 417 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession 1580816 _struct_ref_seq.db_align_beg 28 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 444 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 1 _struct_ref_seq.pdbx_auth_seq_align_end 417 # 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 1T0O LEU A 37 ? GB 1580816 VAL 64 'SEE REMARK 999' 37 1 1 1T0O PRO A 70 ? GB 1580816 VAL 97 'SEE REMARK 999' 70 2 1 1T0O ALA A 72 ? GB 1580816 THR 99 'SEE REMARK 999' 72 3 1 1T0O ALA A 88 ? GB 1580816 ASP 115 'SEE REMARK 999' 88 4 1 1T0O ASN A 148 ? GB 1580816 ALA 175 'SEE REMARK 999' 148 5 1 1T0O PHE A 151 ? GB 1580816 ALA 178 'SEE REMARK 999' 151 6 1 1T0O LYS A 153 ? GB 1580816 GLN 180 'SEE REMARK 999' 153 7 1 1T0O THR A 161 ? GB 1580816 SER 188 'SEE REMARK 999' 161 8 1 1T0O ASP A 165 ? GB 1580816 GLU 192 'SEE REMARK 999' 165 9 1 1T0O THR A 167 ? GB 1580816 ASN 194 'SEE REMARK 999' 167 10 1 1T0O GLY A 185 ? GB 1580816 ASN 212 'SEE REMARK 999' 185 11 1 1T0O HIS A 196 ? GB 1580816 ARG 223 'SEE REMARK 999' 196 12 1 1T0O MET A 202 ? GB 1580816 LEU 229 'SEE REMARK 999' 202 13 1 1T0O GLN A 207 ? GB 1580816 VAL 234 'SEE REMARK 999' 207 14 1 1T0O SER A 216 ? GB 1580816 GLU 243 'SEE REMARK 999' 216 15 1 1T0O ASP A 225 ? GB 1580816 GLY 252 'SEE REMARK 999' 225 16 1 1T0O ASN A 230 ? GB 1580816 GLU 257 'SEE REMARK 999' 230 17 1 1T0O ARG A 236 ? GB 1580816 HIS 263 'SEE REMARK 999' 236 18 1 1T0O LEU A 238 ? GB 1580816 ILE 265 'SEE REMARK 999' 238 19 1 1T0O LEU A 240 ? GB 1580816 MET 267 'SEE REMARK 999' 240 20 1 1T0O LEU A 245 ? GB 1580816 MET 272 'SEE REMARK 999' 245 21 1 1T0O ASP A 249 ? GB 1580816 GLY 276 'SEE REMARK 999' 249 22 1 1T0O MET A 258 ? GB 1580816 ILE 285 'SEE REMARK 999' 258 23 1 1T0O ASN A 297 ? GB 1580816 GLU 324 'SEE REMARK 999' 297 24 1 1T0O ASN A 300 ? GB 1580816 GLU 327 'SEE REMARK 999' 300 25 1 1T0O ILE A 327 ? GB 1580816 VAL 354 'SEE REMARK 999' 327 26 1 1T0O VAL A 335 ? GB 1580816 TYR 362 'SEE REMARK 999' 335 27 1 1T0O TYR A 337 ? GB 1580816 ASN 364 'SEE REMARK 999' 337 28 1 1T0O PHE A 341 ? GB 1580816 TYR 368 'SEE REMARK 999' 341 29 1 1T0O VAL A 355 ? GB 1580816 MET 382 'SEE REMARK 999' 355 30 1 1T0O ILE A 360 ? GB 1580816 HIS 387 'SEE REMARK 999' 360 31 1 1T0O ALA A 362 ? GB 1580816 VAL 389 'SEE REMARK 999' 362 32 1 1T0O THR A 363 ? GB 1580816 ARG 390 'SEE REMARK 999' 363 33 1 1T0O ASN A 369 ? GB 1580816 SER 396 'SEE REMARK 999' 369 34 1 1T0O HIS A 378 ? GB 1580816 ARG 405 'SEE REMARK 999' 378 35 1 1T0O SER A 386 ? GB 1580816 THR 413 'SEE REMARK 999' 386 36 1 1T0O ASP A 389 ? GB 1580816 SER 416 'SEE REMARK 999' 389 37 1 1T0O ALA A 398 ? GB 1580816 THR 425 'SEE REMARK 999' 398 38 1 1T0O GLN A 415 ? GB 1580816 ARG 442 'SEE REMARK 999' 415 39 1 1T0O ARG A 416 ? GB 1580816 ASN 443 'SEE REMARK 999' 416 40 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GAL D-saccharide . BETA-D-GALACTOSE ? 'C6 H12 O6' 180.156 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 1T0O _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_percent_sol 54.07 _exptl_crystal.description ? _exptl_crystal.density_Matthews 2.70 _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 293 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 6 _exptl_crystal_grow.pdbx_details 'EG 6000, potassium phosphate, sodium phosphate, D-galactose, VAPOR DIFFUSION, HANGING DROP, temperature 293K' _exptl_crystal_grow.pdbx_pH_range . # _diffrn.id 1 _diffrn.ambient_temp 277 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector 'IMAGE PLATE' _diffrn_detector.type MARRESEARCH _diffrn_detector.pdbx_collection_date 1998-09-25 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'Si 111 CHANNEL' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.54 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'LNLS BEAMLINE D03B-MX1' _diffrn_source.pdbx_synchrotron_site LNLS _diffrn_source.pdbx_synchrotron_beamline D03B-MX1 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1.54 # _reflns.entry_id 1T0O _reflns.observed_criterion_sigma_F 0 _reflns.observed_criterion_sigma_I 1 _reflns.d_resolution_high 2.0 _reflns.d_resolution_low 9.9 _reflns.number_all ? _reflns.number_obs 28741 _reflns.percent_possible_obs 63.6 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value 0.07 _reflns.pdbx_netI_over_sigmaI 10.1 _reflns.B_iso_Wilson_estimate 25.2 _reflns.pdbx_redundancy 2.9 _reflns.R_free_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.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 2.0 _reflns_shell.d_res_low 2.05 _reflns_shell.percent_possible_all 64 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value 0.364 _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_redundancy ? _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 1T0O _refine.ls_number_reflns_obs 24004 _refine.ls_number_reflns_all 26738 _refine.pdbx_ls_sigma_I 0 _refine.pdbx_ls_sigma_F 0 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 9.00 _refine.ls_d_res_high 1.96 _refine.ls_percent_reflns_obs 72.35 _refine.ls_R_factor_obs 0.15686 _refine.ls_R_factor_all 0.169 _refine.ls_R_factor_R_work 0.15141 _refine.ls_R_factor_R_free 0.20491 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 10.0 _refine.ls_number_reflns_R_free 2659 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.969 _refine.correlation_coeff_Fo_to_Fc_free 0.944 _refine.B_iso_mean 25.205 _refine.aniso_B[1][1] 1.78 _refine.aniso_B[2][2] -0.50 _refine.aniso_B[3][3] -1.29 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details 'BABINET MODEL WITH MASK' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.40 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ? _refine.pdbx_starting_model 'PDB ENTRY 1SZN' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.225 _refine.pdbx_overall_ESU_R_Free 0.184 _refine.overall_SU_ML 0.115 _refine.overall_SU_B 4.034 _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_phase_error ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 3213 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 201 _refine_hist.number_atoms_solvent 384 _refine_hist.number_atoms_total 3798 _refine_hist.d_res_high 1.96 _refine_hist.d_res_low 9.00 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.011 0.021 ? 3524 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.594 1.992 ? 4836 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.556 3.000 ? 416 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 17.975 15.000 ? 533 'X-RAY DIFFRACTION' ? r_chiral_restr 0.139 0.200 ? 562 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.004 0.020 ? 2599 'X-RAY DIFFRACTION' ? r_nbd_refined 0.217 0.300 ? 2006 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined 0.150 0.500 ? 543 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined 0.230 0.300 ? 34 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined 0.210 0.500 ? 20 'X-RAY DIFFRACTION' ? r_mcbond_it 0.663 1.500 ? 2069 'X-RAY DIFFRACTION' ? r_mcangle_it 1.237 2.000 ? 3312 'X-RAY DIFFRACTION' ? r_scbond_it 1.938 3.000 ? 1455 'X-RAY DIFFRACTION' ? r_scangle_it 3.118 4.500 ? 1524 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used 15 _refine_ls_shell.d_res_high 1.960 _refine_ls_shell.d_res_low 2.025 _refine_ls_shell.number_reflns_R_work 2111 _refine_ls_shell.R_factor_R_work 0.198 _refine_ls_shell.percent_reflns_obs ? _refine_ls_shell.R_factor_R_free 0.253 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 224 _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.number_reflns_all ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.R_factor_all ? # _struct.entry_id 1T0O _struct.title 'The structure of alpha-galactosidase from Trichoderma reesei complexed with beta-D-galactose' _struct.pdbx_descriptor 'alpha-galactosidase (E.C.3.2.1.22 )' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1T0O _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text '(beta/alpha)8 barrel, two domains, glycoprotein, complex, beta-D-galactose, HYDROLASE' # 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 2 ? D N N 2 ? E N N 2 ? F N N 3 ? G N N 4 ? H N N 4 ? I N N 4 ? J N N 4 ? K N N 2 ? L N N 2 ? M N N 3 ? N N N 4 ? O N N 2 ? P N N 2 ? Q N N 5 ? R N N 6 ? # _struct_biol.id 1 _struct_biol.details 'The biological assembly is a monomer' _struct_biol.pdbx_parent_biol_id ? # 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 1 SER A 18 ? HIS A 23 ? SER A 18 HIS A 23 1 ? 6 HELX_P HELX_P2 2 ASP A 27 ? SER A 41 ? ASP A 27 SER A 41 1 ? 15 HELX_P HELX_P3 3 GLY A 42 ? GLY A 47 ? GLY A 42 GLY A 47 1 ? 6 HELX_P HELX_P4 4 ASP A 77 ? LEU A 89 ? ASP A 77 LEU A 89 1 ? 13 HELX_P HELX_P5 5 TYR A 113 ? GLY A 125 ? TYR A 113 GLY A 125 1 ? 13 HELX_P HELX_P6 6 PRO A 137 ? GLN A 141 ? PRO A 137 GLN A 141 5 ? 5 HELX_P HELX_P7 7 GLY A 155 ? THR A 159 ? GLY A 155 THR A 159 5 ? 5 HELX_P HELX_P8 8 ASP A 174 ? THR A 177 ? ASP A 174 THR A 177 5 ? 4 HELX_P HELX_P9 9 SER A 178 ? LYS A 193 ? SER A 178 LYS A 193 1 ? 16 HELX_P HELX_P10 10 ASP A 209 ? GLY A 214 ? ASP A 209 GLY A 214 1 ? 6 HELX_P HELX_P11 11 ASN A 215 ? THR A 217 ? ASN A 215 THR A 217 5 ? 3 HELX_P HELX_P12 12 ASN A 230 ? PHE A 243 ? ASN A 230 PHE A 243 1 ? 14 HELX_P HELX_P13 13 LYS A 244 ? VAL A 248 ? LYS A 244 VAL A 248 5 ? 5 HELX_P HELX_P14 14 THR A 267 ? MET A 281 ? THR A 267 MET A 281 1 ? 15 HELX_P HELX_P15 15 SER A 295 ? LYS A 303 ? SER A 295 LYS A 303 1 ? 9 HELX_P HELX_P16 16 ASN A 304 ? GLN A 312 ? ASN A 304 GLN A 312 1 ? 9 HELX_P HELX_P17 17 LYS A 367 ? ILE A 371 ? LYS A 367 ILE A 371 5 ? 5 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 24 SG ? ? ? 1_555 A CYS 56 SG ? ? A CYS 24 A CYS 56 1_555 ? ? ? ? ? ? ? 2.000 ? disulf2 disulf ? ? A CYS 104 SG ? ? ? 1_555 A CYS 134 SG ? ? A CYS 104 A CYS 134 1_555 ? ? ? ? ? ? ? 1.998 ? disulf3 disulf ? ? A CYS 147 SG ? ? ? 1_555 A CYS 160 SG ? ? A CYS 147 A CYS 160 1_555 ? ? ? ? ? ? ? 2.002 ? disulf4 disulf ? ? A CYS 392 SG ? ? ? 1_555 A CYS 414 SG ? ? A CYS 392 A CYS 414 1_555 ? ? ? ? ? ? ? 2.026 ? covale1 covale ? ? A ASN 71 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 71 A NAG 500 1_555 ? ? ? ? ? ? ? 1.443 ? covale2 covale ? ? A ASN 157 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 157 A NAG 600 1_555 ? ? ? ? ? ? ? 1.447 ? covale3 covale ? ? A ASN 215 ND2 ? ? ? 1_555 K NAG . C1 ? ? A ASN 215 A NAG 700 1_555 ? ? ? ? ? ? ? 1.436 ? covale4 covale ? ? A ASN 334 ND2 ? ? ? 1_555 O NAG . C1 ? ? A ASN 334 A NAG 800 1_555 ? ? ? ? ? ? ? 1.427 ? covale5 covale ? ? B NAG . O4 ? ? ? 1_555 C NAG . C1 ? ? A NAG 500 A NAG 501 1_555 ? ? ? ? ? ? ? 1.439 ? covale6 covale ? ? D NAG . O4 ? ? ? 1_555 E NAG . C1 ? ? A NAG 600 A NAG 601 1_555 ? ? ? ? ? ? ? 1.439 ? covale7 covale ? ? E NAG . O4 ? ? ? 1_555 F BMA . C1 ? ? A NAG 601 A BMA 602 1_555 ? ? ? ? ? ? ? 1.433 ? covale8 covale ? ? F BMA . O3 ? ? ? 1_555 G MAN . C1 ? ? A BMA 602 A MAN 603 1_555 ? ? ? ? ? ? ? 1.453 ? covale9 covale ? ? F BMA . O6 ? ? ? 1_555 H MAN . C1 ? ? A BMA 602 A MAN 604 1_555 ? ? ? ? ? ? ? 1.424 ? covale10 covale ? ? H MAN . O3 ? ? ? 1_555 J MAN . C1 ? ? A MAN 604 A MAN 606 1_555 ? ? ? ? ? ? ? 1.395 ? covale11 covale ? ? H MAN . O6 ? ? ? 1_555 I MAN . C1 ? ? A MAN 604 A MAN 605 1_555 ? ? ? ? ? ? ? 1.436 ? covale12 covale ? ? K NAG . O4 ? ? ? 1_555 L NAG . C1 ? ? A NAG 700 A NAG 701 1_555 ? ? ? ? ? ? ? 1.422 ? covale13 covale ? ? L NAG . O4 ? ? ? 1_555 M BMA . C1 ? ? A NAG 701 A BMA 702 1_555 ? ? ? ? ? ? ? 1.442 ? covale14 covale ? ? M BMA . O3 ? ? ? 1_555 N MAN . C1 ? ? A BMA 702 A MAN 703 1_555 ? ? ? ? ? ? ? 1.451 ? covale15 covale ? ? O NAG . O4 ? ? ? 1_555 P NAG . C1 ? ? A NAG 800 A NAG 801 1_555 ? ? ? ? ? ? ? 1.439 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 8 ? B ? 6 ? C ? 2 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? parallel A 2 3 ? parallel A 3 4 ? parallel A 4 5 ? parallel A 5 6 ? parallel A 6 7 ? parallel A 7 8 ? parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel B 4 5 ? anti-parallel B 5 6 ? anti-parallel C 1 2 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 HIS A 253 ? ASP A 255 ? HIS A 253 ASP A 255 A 2 SER A 220 ? ARG A 222 ? SER A 220 ARG A 222 A 3 VAL A 199 ? MET A 202 ? VAL A 199 MET A 202 A 4 TYR A 128 ? ASP A 132 ? TYR A 128 ASP A 132 A 5 LYS A 92 ? THR A 98 ? LYS A 92 THR A 98 A 6 TYR A 50 ? ASN A 52 ? TYR A 50 ASN A 52 A 7 LEU A 14 ? ASN A 17 ? LEU A 14 ASN A 17 A 8 LEU A 285 ? ILE A 287 ? LEU A 285 ILE A 287 B 1 THR A 321 ? LYS A 324 ? THR A 321 LYS A 324 B 2 PHE A 341 ? GLY A 344 ? PHE A 341 GLY A 344 B 3 HIS A 350 ? VAL A 355 ? HIS A 350 VAL A 355 B 4 THR A 405 ? LYS A 413 ? THR A 405 LYS A 413 B 5 TYR A 379 ? ASP A 383 ? TYR A 379 ASP A 383 B 6 ASP A 389 ? LEU A 393 ? ASP A 389 LEU A 393 C 1 ALA A 362 ? ALA A 366 ? ALA A 362 ALA A 366 C 2 TYR A 396 ? VAL A 400 ? TYR A 396 VAL A 400 # 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 A 1 2 O ASP A 255 ? O ASP A 255 N TRP A 221 ? N TRP A 221 A 2 3 O SER A 220 ? O SER A 220 N MET A 202 ? N MET A 202 A 3 4 O SER A 201 ? O SER A 201 N LEU A 129 ? N LEU A 129 A 4 5 O TYR A 128 ? O TYR A 128 N ILE A 95 ? N ILE A 95 A 5 6 O LYS A 92 ? O LYS A 92 N VAL A 51 ? N VAL A 51 A 6 7 O ASN A 52 ? O ASN A 52 N TRP A 16 ? N TRP A 16 A 7 8 N GLY A 15 ? N GLY A 15 O ILE A 287 ? O ILE A 287 B 1 2 N TYR A 323 ? N TYR A 323 O PHE A 341 ? O PHE A 341 B 2 3 N TRP A 342 ? N TRP A 342 O LEU A 353 ? O LEU A 353 B 3 4 N HIS A 350 ? N HIS A 350 O VAL A 410 ? O VAL A 410 B 4 5 O GLY A 411 ? O GLY A 411 N GLU A 380 ? N GLU A 380 B 5 6 N TYR A 379 ? N TYR A 379 O LEU A 393 ? O LEU A 393 C 1 2 N ALA A 362 ? N ALA A 362 O VAL A 400 ? O VAL A 400 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG A 500' AC2 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 501' AC3 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 600' AC4 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG A 601' AC5 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE BMA A 602' AC6 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE MAN A 603' AC7 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE MAN A 604' AC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE MAN A 605' AC9 Software ? ? ? ? 11 'BINDING SITE FOR RESIDUE MAN A 606' BC1 Software ? ? ? ? 12 'BINDING SITE FOR RESIDUE NAG A 700' BC2 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE NAG A 701' BC3 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE BMA A 702' BC4 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE MAN A 703' BC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 800' BC6 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 801' BC7 Software ? ? ? ? 15 'BINDING SITE FOR RESIDUE GAL A 901' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 7 SER A 58 ? SER A 58 . ? 1_555 ? 2 AC1 7 MET A 59 ? MET A 59 . ? 1_555 ? 3 AC1 7 LYS A 60 ? LYS A 60 . ? 1_555 ? 4 AC1 7 ASP A 61 ? ASP A 61 . ? 1_555 ? 5 AC1 7 ASN A 71 ? ASN A 71 . ? 1_555 ? 6 AC1 7 ARG A 74 ? ARG A 74 . ? 1_555 ? 7 AC1 7 NAG C . ? NAG A 501 . ? 1_555 ? 8 AC2 1 NAG B . ? NAG A 500 . ? 1_555 ? 9 AC3 6 ASN A 157 ? ASN A 157 . ? 1_555 ? 10 AC3 6 PHE A 243 ? PHE A 243 . ? 1_555 ? 11 AC3 6 TRP A 331 ? TRP A 331 . ? 1_555 ? 12 AC3 6 NAG E . ? NAG A 601 . ? 1_555 ? 13 AC3 6 HOH R . ? HOH A 1043 . ? 1_555 ? 14 AC3 6 HOH R . ? HOH A 1251 . ? 1_555 ? 15 AC4 7 PHE A 243 ? PHE A 243 . ? 1_555 ? 16 AC4 7 TRP A 331 ? TRP A 331 . ? 1_555 ? 17 AC4 7 NAG D . ? NAG A 600 . ? 1_555 ? 18 AC4 7 BMA F . ? BMA A 602 . ? 1_555 ? 19 AC4 7 MAN H . ? MAN A 604 . ? 1_555 ? 20 AC4 7 MAN J . ? MAN A 606 . ? 1_555 ? 21 AC4 7 HOH R . ? HOH A 1179 . ? 1_555 ? 22 AC5 3 NAG E . ? NAG A 601 . ? 1_555 ? 23 AC5 3 MAN G . ? MAN A 603 . ? 1_555 ? 24 AC5 3 MAN H . ? MAN A 604 . ? 1_555 ? 25 AC6 3 BMA F . ? BMA A 602 . ? 1_555 ? 26 AC6 3 HOH R . ? HOH A 1025 . ? 1_555 ? 27 AC6 3 HOH R . ? HOH A 1151 . ? 1_555 ? 28 AC7 7 ASN A 246 ? ASN A 246 . ? 1_555 ? 29 AC7 7 NAG E . ? NAG A 601 . ? 1_555 ? 30 AC7 7 BMA F . ? BMA A 602 . ? 1_555 ? 31 AC7 7 MAN I . ? MAN A 605 . ? 1_555 ? 32 AC7 7 MAN J . ? MAN A 606 . ? 1_555 ? 33 AC7 7 HOH R . ? HOH A 1104 . ? 1_555 ? 34 AC7 7 HOH R . ? HOH A 1282 . ? 1_555 ? 35 AC8 4 ASN A 246 ? ASN A 246 . ? 1_555 ? 36 AC8 4 MAN H . ? MAN A 604 . ? 1_555 ? 37 AC8 4 HOH R . ? HOH A 1167 . ? 1_555 ? 38 AC8 4 HOH R . ? HOH A 1282 . ? 1_555 ? 39 AC9 11 SER A 242 ? SER A 242 . ? 1_555 ? 40 AC9 11 PHE A 243 ? PHE A 243 . ? 1_555 ? 41 AC9 11 LYS A 244 ? LYS A 244 . ? 1_555 ? 42 AC9 11 LEU A 245 ? LEU A 245 . ? 1_555 ? 43 AC9 11 THR A 321 ? THR A 321 . ? 1_555 ? 44 AC9 11 PRO A 322 ? PRO A 322 . ? 1_555 ? 45 AC9 11 TRP A 331 ? TRP A 331 . ? 1_555 ? 46 AC9 11 NAG E . ? NAG A 601 . ? 1_555 ? 47 AC9 11 MAN H . ? MAN A 604 . ? 1_555 ? 48 AC9 11 HOH R . ? HOH A 1000 . ? 1_555 ? 49 AC9 11 HOH R . ? HOH A 1077 . ? 1_555 ? 50 BC1 12 VAL A 2 ? VAL A 2 . ? 1_555 ? 51 BC1 12 ASN A 215 ? ASN A 215 . ? 1_555 ? 52 BC1 12 ASN A 246 ? ASN A 246 . ? 1_555 ? 53 BC1 12 ASP A 249 ? ASP A 249 . ? 1_555 ? 54 BC1 12 PHE A 250 ? PHE A 250 . ? 1_555 ? 55 BC1 12 TRP A 251 ? TRP A 251 . ? 1_555 ? 56 BC1 12 NAG L . ? NAG A 701 . ? 1_555 ? 57 BC1 12 HOH R . ? HOH A 948 . ? 1_555 ? 58 BC1 12 HOH R . ? HOH A 1084 . ? 1_555 ? 59 BC1 12 HOH R . ? HOH A 1111 . ? 1_555 ? 60 BC1 12 HOH R . ? HOH A 1182 . ? 1_555 ? 61 BC1 12 HOH R . ? HOH A 1185 . ? 1_555 ? 62 BC2 10 VAL A 2 ? VAL A 2 . ? 1_555 ? 63 BC2 10 LYS A 10 ? LYS A 10 . ? 1_555 ? 64 BC2 10 ASP A 249 ? ASP A 249 . ? 1_555 ? 65 BC2 10 PHE A 250 ? PHE A 250 . ? 1_555 ? 66 BC2 10 TRP A 251 ? TRP A 251 . ? 1_555 ? 67 BC2 10 NAG K . ? NAG A 700 . ? 1_555 ? 68 BC2 10 BMA M . ? BMA A 702 . ? 1_555 ? 69 BC2 10 HOH R . ? HOH A 943 . ? 1_555 ? 70 BC2 10 HOH R . ? HOH A 1062 . ? 1_555 ? 71 BC2 10 HOH R . ? HOH A 1281 . ? 1_555 ? 72 BC3 6 VAL A 315 ? VAL A 315 . ? 1_555 ? 73 BC3 6 NAG L . ? NAG A 701 . ? 1_555 ? 74 BC3 6 MAN N . ? MAN A 703 . ? 1_555 ? 75 BC3 6 HOH R . ? HOH A 1062 . ? 1_555 ? 76 BC3 6 HOH R . ? HOH A 1068 . ? 1_555 ? 77 BC3 6 HOH R . ? HOH A 1137 . ? 1_555 ? 78 BC4 2 BMA M . ? BMA A 702 . ? 1_555 ? 79 BC4 2 HOH R . ? HOH A 1258 . ? 1_555 ? 80 BC5 6 ASP A 65 ? ASP A 65 . ? 4_455 ? 81 BC5 6 ASN A 328 ? ASN A 328 . ? 1_555 ? 82 BC5 6 ASN A 334 ? ASN A 334 . ? 1_555 ? 83 BC5 6 TYR A 337 ? TYR A 337 . ? 1_555 ? 84 BC5 6 NAG P . ? NAG A 801 . ? 1_555 ? 85 BC5 6 HOH R . ? HOH A 1003 . ? 1_555 ? 86 BC6 5 ILE A 327 ? ILE A 327 . ? 1_555 ? 87 BC6 5 NAG O . ? NAG A 800 . ? 1_555 ? 88 BC6 5 HOH R . ? HOH A 1019 . ? 1_555 ? 89 BC6 5 HOH R . ? HOH A 1092 . ? 1_555 ? 90 BC6 5 HOH R . ? HOH A 1162 . ? 1_555 ? 91 BC7 15 TRP A 19 ? TRP A 19 . ? 1_555 ? 92 BC7 15 ASP A 54 ? ASP A 54 . ? 1_555 ? 93 BC7 15 ASP A 55 ? ASP A 55 . ? 1_555 ? 94 BC7 15 TYR A 96 ? TYR A 96 . ? 1_555 ? 95 BC7 15 CYS A 104 ? CYS A 104 . ? 1_555 ? 96 BC7 15 LYS A 130 ? LYS A 130 . ? 1_555 ? 97 BC7 15 ASP A 132 ? ASP A 132 . ? 1_555 ? 98 BC7 15 LYS A 193 ? LYS A 193 . ? 4_455 ? 99 BC7 15 CYS A 203 ? CYS A 203 . ? 1_555 ? 100 BC7 15 TRP A 205 ? TRP A 205 . ? 1_555 ? 101 BC7 15 ARG A 222 ? ARG A 222 . ? 1_555 ? 102 BC7 15 ASP A 226 ? ASP A 226 . ? 1_555 ? 103 BC7 15 MET A 258 ? MET A 258 . ? 1_555 ? 104 BC7 15 HOH R . ? HOH A 957 . ? 1_555 ? 105 BC7 15 HOH R . ? HOH A 1022 . ? 1_555 ? # _database_PDB_matrix.entry_id 1T0O _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 1T0O _atom_sites.fract_transf_matrix[1][1] 0.017291 _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] 0.017149 _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] 0.006508 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . ILE A 1 1 ? 22.041 13.212 13.242 1.00 21.36 ? 1 ILE A N 1 ATOM 2 C CA . ILE A 1 1 ? 23.471 13.359 12.840 1.00 22.49 ? 1 ILE A CA 1 ATOM 3 C C . ILE A 1 1 ? 24.088 14.573 13.521 1.00 22.46 ? 1 ILE A C 1 ATOM 4 O O . ILE A 1 1 ? 23.420 15.581 13.687 1.00 22.09 ? 1 ILE A O 1 ATOM 5 C CB . ILE A 1 1 ? 23.552 13.487 11.292 1.00 22.31 ? 1 ILE A CB 1 ATOM 6 C CG1 . ILE A 1 1 ? 24.966 13.210 10.781 1.00 23.51 ? 1 ILE A CG1 1 ATOM 7 C CG2 . ILE A 1 1 ? 23.039 14.860 10.827 1.00 21.72 ? 1 ILE A CG2 1 ATOM 8 C CD1 . ILE A 1 1 ? 25.069 13.310 9.262 1.00 26.06 ? 1 ILE A CD1 1 ATOM 9 N N . VAL A 1 2 ? 25.358 14.489 13.920 1.00 23.28 ? 2 VAL A N 1 ATOM 10 C CA . VAL A 1 2 ? 26.021 15.645 14.528 1.00 24.58 ? 2 VAL A CA 1 ATOM 11 C C . VAL A 1 2 ? 26.373 16.649 13.454 1.00 24.85 ? 2 VAL A C 1 ATOM 12 O O . VAL A 1 2 ? 26.806 16.280 12.371 1.00 25.17 ? 2 VAL A O 1 ATOM 13 C CB . VAL A 1 2 ? 27.342 15.282 15.221 1.00 24.85 ? 2 VAL A CB 1 ATOM 14 C CG1 . VAL A 1 2 ? 27.397 15.900 16.589 1.00 26.56 ? 2 VAL A CG1 1 ATOM 15 C CG2 . VAL A 1 2 ? 27.498 13.793 15.326 1.00 25.87 ? 2 VAL A CG2 1 ATOM 16 N N . MET A 1 3 ? 26.190 17.923 13.750 1.00 25.23 ? 3 MET A N 1 ATOM 17 C CA . MET A 1 3 ? 26.477 18.957 12.768 1.00 26.11 ? 3 MET A CA 1 ATOM 18 C C . MET A 1 3 ? 27.806 19.611 13.130 1.00 26.97 ? 3 MET A C 1 ATOM 19 O O . MET A 1 3 ? 28.143 19.660 14.294 1.00 26.93 ? 3 MET A O 1 ATOM 20 C CB . MET A 1 3 ? 25.336 19.962 12.756 1.00 25.99 ? 3 MET A CB 1 ATOM 21 C CG . MET A 1 3 ? 24.006 19.309 12.354 1.00 24.94 ? 3 MET A CG 1 ATOM 22 S SD . MET A 1 3 ? 24.204 18.666 10.694 1.00 25.79 ? 3 MET A SD 1 ATOM 23 C CE . MET A 1 3 ? 24.376 20.212 9.803 1.00 25.23 ? 3 MET A CE 1 ATOM 24 N N . PRO A 1 4 ? 28.548 20.105 12.143 1.00 28.28 ? 4 PRO A N 1 ATOM 25 C CA . PRO A 1 4 ? 29.900 20.645 12.380 1.00 29.13 ? 4 PRO A CA 1 ATOM 26 C C . PRO A 1 4 ? 29.981 21.760 13.423 1.00 30.14 ? 4 PRO A C 1 ATOM 27 O O . PRO A 1 4 ? 31.000 21.858 14.111 1.00 30.05 ? 4 PRO A O 1 ATOM 28 C CB . PRO A 1 4 ? 30.328 21.171 11.002 1.00 29.50 ? 4 PRO A CB 1 ATOM 29 C CG . PRO A 1 4 ? 29.490 20.421 10.012 1.00 29.38 ? 4 PRO A CG 1 ATOM 30 C CD . PRO A 1 4 ? 28.150 20.187 10.722 1.00 28.19 ? 4 PRO A CD 1 ATOM 31 N N . ASP A 1 5 ? 28.944 22.584 13.550 1.00 30.62 ? 5 ASP A N 1 ATOM 32 C CA . ASP A 1 5 ? 29.010 23.680 14.509 1.00 31.09 ? 5 ASP A CA 1 ATOM 33 C C . ASP A 1 5 ? 28.835 23.203 15.934 1.00 31.05 ? 5 ASP A C 1 ATOM 34 O O . ASP A 1 5 ? 28.906 23.988 16.874 1.00 31.72 ? 5 ASP A O 1 ATOM 35 C CB . ASP A 1 5 ? 28.021 24.799 14.161 1.00 31.55 ? 5 ASP A CB 1 ATOM 36 C CG . ASP A 1 5 ? 26.598 24.539 14.671 1.00 31.97 ? 5 ASP A CG 1 ATOM 37 O OD1 . ASP A 1 5 ? 26.279 23.436 15.172 1.00 29.91 ? 5 ASP A OD1 1 ATOM 38 O OD2 . ASP A 1 5 ? 25.725 25.422 14.595 1.00 32.52 ? 5 ASP A OD2 1 ATOM 39 N N . GLY A 1 6 ? 28.603 21.906 16.087 1.00 30.81 ? 6 GLY A N 1 ATOM 40 C CA . GLY A 1 6 ? 28.498 21.291 17.396 1.00 30.38 ? 6 GLY A CA 1 ATOM 41 C C . GLY A 1 6 ? 27.276 21.601 18.242 1.00 30.04 ? 6 GLY A C 1 ATOM 42 O O . GLY A 1 6 ? 27.169 21.115 19.371 1.00 30.24 ? 6 GLY A O 1 ATOM 43 N N . VAL A 1 7 ? 26.345 22.400 17.733 1.00 28.85 ? 7 VAL A N 1 ATOM 44 C CA . VAL A 1 7 ? 25.127 22.651 18.505 1.00 27.67 ? 7 VAL A CA 1 ATOM 45 C C . VAL A 1 7 ? 23.830 22.667 17.684 1.00 27.04 ? 7 VAL A C 1 ATOM 46 O O . VAL A 1 7 ? 22.790 22.238 18.160 1.00 26.52 ? 7 VAL A O 1 ATOM 47 C CB . VAL A 1 7 ? 25.224 23.956 19.324 1.00 27.90 ? 7 VAL A CB 1 ATOM 48 C CG1 . VAL A 1 7 ? 26.520 23.998 20.124 1.00 28.71 ? 7 VAL A CG1 1 ATOM 49 C CG2 . VAL A 1 7 ? 25.167 25.172 18.409 1.00 28.27 ? 7 VAL A CG2 1 ATOM 50 N N . THR A 1 8 ? 23.882 23.157 16.456 1.00 26.28 ? 8 THR A N 1 ATOM 51 C CA . THR A 1 8 ? 22.654 23.326 15.700 1.00 25.31 ? 8 THR A CA 1 ATOM 52 C C . THR A 1 8 ? 22.026 21.982 15.356 1.00 24.12 ? 8 THR A C 1 ATOM 53 O O . THR A 1 8 ? 22.584 21.208 14.591 1.00 24.44 ? 8 THR A O 1 ATOM 54 C CB . THR A 1 8 ? 22.897 24.185 14.469 1.00 25.56 ? 8 THR A CB 1 ATOM 55 O OG1 . THR A 1 8 ? 23.345 25.478 14.902 1.00 27.61 ? 8 THR A OG1 1 ATOM 56 C CG2 . THR A 1 8 ? 21.578 24.502 13.784 1.00 24.12 ? 8 THR A CG2 1 ATOM 57 N N . GLY A 1 9 ? 20.863 21.718 15.935 1.00 22.64 ? 9 GLY A N 1 ATOM 58 C CA . GLY A 1 9 ? 20.165 20.475 15.678 1.00 21.20 ? 9 GLY A CA 1 ATOM 59 C C . GLY A 1 9 ? 20.420 19.400 16.705 1.00 19.79 ? 9 GLY A C 1 ATOM 60 O O . GLY A 1 9 ? 19.904 18.293 16.586 1.00 19.28 ? 9 GLY A O 1 ATOM 61 N N . LYS A 1 10 ? 21.215 19.710 17.722 1.00 18.32 ? 10 LYS A N 1 ATOM 62 C CA . LYS A 1 10 ? 21.458 18.733 18.768 1.00 18.22 ? 10 LYS A CA 1 ATOM 63 C C . LYS A 1 10 ? 20.175 18.488 19.552 1.00 17.50 ? 10 LYS A C 1 ATOM 64 O O . LYS A 1 10 ? 19.804 17.353 19.848 1.00 17.54 ? 10 LYS A O 1 ATOM 65 C CB . LYS A 1 10 ? 22.570 19.213 19.694 1.00 17.91 ? 10 LYS A CB 1 ATOM 66 C CG . LYS A 1 10 ? 22.795 18.303 20.876 1.00 21.44 ? 10 LYS A CG 1 ATOM 67 C CD . LYS A 1 10 ? 24.072 18.668 21.599 1.00 23.93 ? 10 LYS A CD 1 ATOM 68 C CE . LYS A 1 10 ? 24.480 17.552 22.529 1.00 26.48 ? 10 LYS A CE 1 ATOM 69 N NZ . LYS A 1 10 ? 25.940 17.633 22.891 1.00 30.64 ? 10 LYS A NZ 1 ATOM 70 N N . VAL A 1 11 ? 19.491 19.567 19.895 1.00 17.54 ? 11 VAL A N 1 ATOM 71 C CA . VAL A 1 11 ? 18.204 19.436 20.557 1.00 17.47 ? 11 VAL A CA 1 ATOM 72 C C . VAL A 1 11 ? 17.173 19.730 19.461 1.00 16.89 ? 11 VAL A C 1 ATOM 73 O O . VAL A 1 11 ? 17.537 20.227 18.389 1.00 17.58 ? 11 VAL A O 1 ATOM 74 C CB . VAL A 1 11 ? 18.082 20.346 21.789 1.00 17.32 ? 11 VAL A CB 1 ATOM 75 C CG1 . VAL A 1 11 ? 19.182 19.991 22.804 1.00 19.47 ? 11 VAL A CG1 1 ATOM 76 C CG2 . VAL A 1 11 ? 18.174 21.816 21.394 1.00 18.60 ? 11 VAL A CG2 1 ATOM 77 N N . PRO A 1 12 ? 15.906 19.426 19.713 1.00 16.86 ? 12 PRO A N 1 ATOM 78 C CA . PRO A 1 12 ? 14.873 19.539 18.665 1.00 16.52 ? 12 PRO A CA 1 ATOM 79 C C . PRO A 1 12 ? 14.788 20.955 18.098 1.00 16.21 ? 12 PRO A C 1 ATOM 80 O O . PRO A 1 12 ? 14.910 21.908 18.864 1.00 16.12 ? 12 PRO A O 1 ATOM 81 C CB . PRO A 1 12 ? 13.593 19.160 19.397 1.00 15.90 ? 12 PRO A CB 1 ATOM 82 C CG . PRO A 1 12 ? 14.102 18.227 20.506 1.00 17.28 ? 12 PRO A CG 1 ATOM 83 C CD . PRO A 1 12 ? 15.360 18.949 20.997 1.00 16.17 ? 12 PRO A CD 1 ATOM 84 N N . SER A 1 13 ? 14.585 21.082 16.787 1.00 16.35 ? 13 SER A N 1 ATOM 85 C CA . SER A 1 13 ? 14.368 22.384 16.167 1.00 16.80 ? 13 SER A CA 1 ATOM 86 C C . SER A 1 13 ? 13.056 23.018 16.662 1.00 16.40 ? 13 SER A C 1 ATOM 87 O O . SER A 1 13 ? 12.070 22.330 16.899 1.00 17.15 ? 13 SER A O 1 ATOM 88 C CB . SER A 1 13 ? 14.284 22.262 14.655 1.00 15.96 ? 13 SER A CB 1 ATOM 89 O OG . SER A 1 13 ? 15.268 21.395 14.160 1.00 19.22 ? 13 SER A OG 1 ATOM 90 N N . LEU A 1 14 ? 13.056 24.329 16.812 1.00 16.49 ? 14 LEU A N 1 ATOM 91 C CA . LEU A 1 14 ? 11.868 25.045 17.249 1.00 16.51 ? 14 LEU A CA 1 ATOM 92 C C . LEU A 1 14 ? 11.627 26.167 16.259 1.00 16.49 ? 14 LEU A C 1 ATOM 93 O O . LEU A 1 14 ? 12.528 26.938 15.930 1.00 17.00 ? 14 LEU A O 1 ATOM 94 C CB . LEU A 1 14 ? 12.021 25.627 18.663 1.00 16.95 ? 14 LEU A CB 1 ATOM 95 C CG . LEU A 1 14 ? 12.459 24.757 19.844 1.00 17.12 ? 14 LEU A CG 1 ATOM 96 C CD1 . LEU A 1 14 ? 12.613 25.590 21.151 1.00 16.84 ? 14 LEU A CD1 1 ATOM 97 C CD2 . LEU A 1 14 ? 11.480 23.618 20.071 1.00 18.42 ? 14 LEU A CD2 1 ATOM 98 N N . GLY A 1 15 ? 10.406 26.264 15.773 1.00 16.49 ? 15 GLY A N 1 ATOM 99 C CA . GLY A 1 15 ? 10.092 27.355 14.885 1.00 16.16 ? 15 GLY A CA 1 ATOM 100 C C . GLY A 1 15 ? 8.666 27.353 14.403 1.00 15.53 ? 15 GLY A C 1 ATOM 101 O O . GLY A 1 15 ? 7.747 27.001 15.121 1.00 15.78 ? 15 GLY A O 1 ATOM 102 N N . TRP A 1 16 ? 8.505 27.752 13.160 1.00 15.88 ? 16 TRP A N 1 ATOM 103 C CA . TRP A 1 16 ? 7.212 27.968 12.557 1.00 16.41 ? 16 TRP A CA 1 ATOM 104 C C . TRP A 1 16 ? 7.312 27.540 11.103 1.00 16.49 ? 16 TRP A C 1 ATOM 105 O O . TRP A 1 16 ? 8.301 27.822 10.428 1.00 15.98 ? 16 TRP A O 1 ATOM 106 C CB . TRP A 1 16 ? 6.889 29.451 12.632 1.00 16.40 ? 16 TRP A CB 1 ATOM 107 C CG . TRP A 1 16 ? 5.585 29.760 12.083 1.00 18.51 ? 16 TRP A CG 1 ATOM 108 C CD1 . TRP A 1 16 ? 4.402 29.830 12.772 1.00 19.35 ? 16 TRP A CD1 1 ATOM 109 C CD2 . TRP A 1 16 ? 5.276 30.048 10.717 1.00 18.71 ? 16 TRP A CD2 1 ATOM 110 N NE1 . TRP A 1 16 ? 3.384 30.142 11.906 1.00 19.11 ? 16 TRP A NE1 1 ATOM 111 C CE2 . TRP A 1 16 ? 3.895 30.283 10.641 1.00 19.34 ? 16 TRP A CE2 1 ATOM 112 C CE3 . TRP A 1 16 ? 6.032 30.131 9.545 1.00 19.90 ? 16 TRP A CE3 1 ATOM 113 C CZ2 . TRP A 1 16 ? 3.251 30.596 9.446 1.00 18.01 ? 16 TRP A CZ2 1 ATOM 114 C CZ3 . TRP A 1 16 ? 5.388 30.446 8.355 1.00 21.02 ? 16 TRP A CZ3 1 ATOM 115 C CH2 . TRP A 1 16 ? 4.014 30.671 8.319 1.00 17.54 ? 16 TRP A CH2 1 ATOM 116 N N . ASN A 1 17 ? 6.286 26.857 10.626 1.00 16.50 ? 17 ASN A N 1 ATOM 117 C CA . ASN A 1 17 ? 6.267 26.363 9.259 1.00 17.28 ? 17 ASN A CA 1 ATOM 118 C C . ASN A 1 17 ? 4.927 26.780 8.628 1.00 18.04 ? 17 ASN A C 1 ATOM 119 O O . ASN A 1 17 ? 3.882 26.736 9.251 1.00 16.44 ? 17 ASN A O 1 ATOM 120 C CB . ASN A 1 17 ? 6.547 24.850 9.271 1.00 17.19 ? 17 ASN A CB 1 ATOM 121 C CG . ASN A 1 17 ? 6.433 24.192 7.926 1.00 16.68 ? 17 ASN A CG 1 ATOM 122 O OD1 . ASN A 1 17 ? 7.413 23.629 7.409 1.00 18.75 ? 17 ASN A OD1 1 ATOM 123 N ND2 . ASN A 1 17 ? 5.253 24.239 7.346 1.00 12.20 ? 17 ASN A ND2 1 ATOM 124 N N . SER A 1 18 ? 4.976 27.193 7.376 1.00 18.89 ? 18 SER A N 1 ATOM 125 C CA . SER A 1 18 ? 3.796 27.697 6.699 1.00 20.00 ? 18 SER A CA 1 ATOM 126 C C . SER A 1 18 ? 2.717 26.674 6.382 1.00 20.91 ? 18 SER A C 1 ATOM 127 O O . SER A 1 18 ? 1.548 27.040 6.227 1.00 21.44 ? 18 SER A O 1 ATOM 128 C CB . SER A 1 18 ? 4.235 28.393 5.402 1.00 20.87 ? 18 SER A CB 1 ATOM 129 O OG . SER A 1 18 ? 4.963 27.513 4.543 1.00 19.14 ? 18 SER A OG 1 ATOM 130 N N . TRP A 1 19 ? 3.084 25.400 6.286 1.00 21.11 ? 19 TRP A N 1 ATOM 131 C CA . TRP A 1 19 ? 2.131 24.387 5.845 1.00 21.67 ? 19 TRP A CA 1 ATOM 132 C C . TRP A 1 19 ? 0.780 24.340 6.598 1.00 22.20 ? 19 TRP A C 1 ATOM 133 O O . TRP A 1 19 ? -0.267 24.543 5.980 1.00 21.87 ? 19 TRP A O 1 ATOM 134 C CB . TRP A 1 19 ? 2.765 22.999 5.737 1.00 21.63 ? 19 TRP A CB 1 ATOM 135 C CG . TRP A 1 19 ? 1.874 22.028 5.007 1.00 22.23 ? 19 TRP A CG 1 ATOM 136 C CD1 . TRP A 1 19 ? 1.201 20.983 5.541 1.00 22.99 ? 19 TRP A CD1 1 ATOM 137 C CD2 . TRP A 1 19 ? 1.569 22.029 3.606 1.00 23.24 ? 19 TRP A CD2 1 ATOM 138 N NE1 . TRP A 1 19 ? 0.489 20.326 4.565 1.00 24.48 ? 19 TRP A NE1 1 ATOM 139 C CE2 . TRP A 1 19 ? 0.702 20.951 3.364 1.00 23.63 ? 19 TRP A CE2 1 ATOM 140 C CE3 . TRP A 1 19 ? 1.945 22.836 2.528 1.00 23.67 ? 19 TRP A CE3 1 ATOM 141 C CZ2 . TRP A 1 19 ? 0.207 20.658 2.099 1.00 23.47 ? 19 TRP A CZ2 1 ATOM 142 C CZ3 . TRP A 1 19 ? 1.459 22.549 1.276 1.00 24.86 ? 19 TRP A CZ3 1 ATOM 143 C CH2 . TRP A 1 19 ? 0.590 21.465 1.068 1.00 25.42 ? 19 TRP A CH2 1 ATOM 144 N N . ASN A 1 20 ? 0.765 24.081 7.907 1.00 22.81 ? 20 ASN A N 1 ATOM 145 C CA . ASN A 1 20 ? -0.560 23.918 8.548 1.00 23.12 ? 20 ASN A CA 1 ATOM 146 C C . ASN A 1 20 ? -1.343 25.233 8.562 1.00 23.58 ? 20 ASN A C 1 ATOM 147 O O . ASN A 1 20 ? -2.567 25.229 8.733 1.00 23.65 ? 20 ASN A O 1 ATOM 148 C CB . ASN A 1 20 ? -0.496 23.350 9.987 1.00 22.75 ? 20 ASN A CB 1 ATOM 149 C CG . ASN A 1 20 ? 0.064 21.924 10.059 1.00 22.90 ? 20 ASN A CG 1 ATOM 150 O OD1 . ASN A 1 20 ? 0.080 21.190 9.077 1.00 24.05 ? 20 ASN A OD1 1 ATOM 151 N ND2 . ASN A 1 20 ? 0.521 21.541 11.234 1.00 19.45 ? 20 ASN A ND2 1 ATOM 152 N N . ALA A 1 21 ? -0.622 26.343 8.384 1.00 23.98 ? 21 ALA A N 1 ATOM 153 C CA . ALA A 1 21 ? -1.197 27.686 8.396 1.00 24.65 ? 21 ALA A CA 1 ATOM 154 C C . ALA A 1 21 ? -1.790 28.040 7.062 1.00 25.47 ? 21 ALA A C 1 ATOM 155 O O . ALA A 1 21 ? -2.946 28.474 6.983 1.00 25.59 ? 21 ALA A O 1 ATOM 156 C CB . ALA A 1 21 ? -0.149 28.713 8.753 1.00 24.48 ? 21 ALA A CB 1 ATOM 157 N N . TYR A 1 22 ? -0.994 27.854 6.007 1.00 26.20 ? 22 TYR A N 1 ATOM 158 C CA . TYR A 1 22 ? -1.377 28.319 4.678 1.00 26.21 ? 22 TYR A CA 1 ATOM 159 C C . TYR A 1 22 ? -1.383 27.251 3.596 1.00 26.32 ? 22 TYR A C 1 ATOM 160 O O . TYR A 1 22 ? -1.819 27.516 2.477 1.00 25.86 ? 22 TYR A O 1 ATOM 161 C CB . TYR A 1 22 ? -0.479 29.481 4.245 1.00 27.00 ? 22 TYR A CB 1 ATOM 162 C CG . TYR A 1 22 ? -0.415 30.574 5.272 1.00 27.12 ? 22 TYR A CG 1 ATOM 163 C CD1 . TYR A 1 22 ? 0.768 30.874 5.926 1.00 26.62 ? 22 TYR A CD1 1 ATOM 164 C CD2 . TYR A 1 22 ? -1.553 31.313 5.591 1.00 28.12 ? 22 TYR A CD2 1 ATOM 165 C CE1 . TYR A 1 22 ? 0.823 31.878 6.871 1.00 27.07 ? 22 TYR A CE1 1 ATOM 166 C CE2 . TYR A 1 22 ? -1.509 32.318 6.532 1.00 27.62 ? 22 TYR A CE2 1 ATOM 167 C CZ . TYR A 1 22 ? -0.320 32.598 7.172 1.00 27.96 ? 22 TYR A CZ 1 ATOM 168 O OH . TYR A 1 22 ? -0.275 33.603 8.114 1.00 26.06 ? 22 TYR A OH 1 ATOM 169 N N . HIS A 1 23 ? -0.910 26.049 3.915 1.00 25.76 ? 23 HIS A N 1 ATOM 170 C CA . HIS A 1 23 ? -0.748 25.039 2.873 1.00 25.69 ? 23 HIS A CA 1 ATOM 171 C C . HIS A 1 23 ? -0.061 25.666 1.654 1.00 25.69 ? 23 HIS A C 1 ATOM 172 O O . HIS A 1 23 ? 0.979 26.290 1.802 1.00 25.38 ? 23 HIS A O 1 ATOM 173 C CB . HIS A 1 23 ? -2.077 24.335 2.576 1.00 25.26 ? 23 HIS A CB 1 ATOM 174 C CG . HIS A 1 23 ? -2.618 23.636 3.778 1.00 25.11 ? 23 HIS A CG 1 ATOM 175 N ND1 . HIS A 1 23 ? -2.321 22.322 4.075 1.00 25.65 ? 23 HIS A ND1 1 ATOM 176 C CD2 . HIS A 1 23 ? -3.429 24.073 4.767 1.00 25.15 ? 23 HIS A CD2 1 ATOM 177 C CE1 . HIS A 1 23 ? -2.932 21.978 5.196 1.00 23.62 ? 23 HIS A CE1 1 ATOM 178 N NE2 . HIS A 1 23 ? -3.611 23.023 5.637 1.00 26.22 ? 23 HIS A NE2 1 ATOM 179 N N . CYS A 1 24 ? -0.629 25.516 0.464 1.00 26.50 ? 24 CYS A N 1 ATOM 180 C CA . CYS A 1 24 ? 0.069 25.912 -0.759 1.00 27.22 ? 24 CYS A CA 1 ATOM 181 C C . CYS A 1 24 ? 0.026 27.412 -1.079 1.00 28.14 ? 24 CYS A C 1 ATOM 182 O O . CYS A 1 24 ? 0.657 27.879 -2.041 1.00 28.56 ? 24 CYS A O 1 ATOM 183 C CB . CYS A 1 24 ? -0.490 25.114 -1.941 1.00 26.93 ? 24 CYS A CB 1 ATOM 184 S SG . CYS A 1 24 ? 0.665 24.831 -3.291 1.00 26.25 ? 24 CYS A SG 1 ATOM 185 N N . ASP A 1 25 ? -0.709 28.160 -0.272 1.00 28.39 ? 25 ASP A N 1 ATOM 186 C CA . ASP A 1 25 ? -1.000 29.554 -0.572 1.00 29.21 ? 25 ASP A CA 1 ATOM 187 C C . ASP A 1 25 ? -0.086 30.438 0.247 1.00 28.77 ? 25 ASP A C 1 ATOM 188 O O . ASP A 1 25 ? -0.470 30.961 1.283 1.00 29.42 ? 25 ASP A O 1 ATOM 189 C CB . ASP A 1 25 ? -2.488 29.847 -0.270 1.00 30.01 ? 25 ASP A CB 1 ATOM 190 C CG . ASP A 1 25 ? -2.895 31.280 -0.597 1.00 32.02 ? 25 ASP A CG 1 ATOM 191 O OD1 . ASP A 1 25 ? -2.246 31.887 -1.473 1.00 34.53 ? 25 ASP A OD1 1 ATOM 192 O OD2 . ASP A 1 25 ? -3.847 31.869 -0.026 1.00 35.00 ? 25 ASP A OD2 1 ATOM 193 N N . ILE A 1 26 ? 1.143 30.607 -0.220 1.00 28.37 ? 26 ILE A N 1 ATOM 194 C CA . ILE A 1 26 ? 2.123 31.339 0.568 1.00 27.64 ? 26 ILE A CA 1 ATOM 195 C C . ILE A 1 26 ? 2.772 32.396 -0.284 1.00 28.07 ? 26 ILE A C 1 ATOM 196 O O . ILE A 1 26 ? 2.767 32.298 -1.501 1.00 29.23 ? 26 ILE A O 1 ATOM 197 C CB . ILE A 1 26 ? 3.204 30.376 1.165 1.00 27.08 ? 26 ILE A CB 1 ATOM 198 C CG1 . ILE A 1 26 ? 3.927 29.600 0.062 1.00 25.61 ? 26 ILE A CG1 1 ATOM 199 C CG2 . ILE A 1 26 ? 2.563 29.394 2.152 1.00 26.13 ? 26 ILE A CG2 1 ATOM 200 C CD1 . ILE A 1 26 ? 5.284 29.025 0.521 1.00 24.66 ? 26 ILE A CD1 1 ATOM 201 N N . ASP A 1 27 ? 3.333 33.405 0.363 1.00 28.20 ? 27 ASP A N 1 ATOM 202 C CA . ASP A 1 27 ? 4.121 34.418 -0.308 1.00 28.16 ? 27 ASP A CA 1 ATOM 203 C C . ASP A 1 27 ? 5.004 34.992 0.765 1.00 27.80 ? 27 ASP A C 1 ATOM 204 O O . ASP A 1 27 ? 4.909 34.602 1.930 1.00 27.62 ? 27 ASP A O 1 ATOM 205 C CB . ASP A 1 27 ? 3.253 35.515 -0.963 1.00 28.16 ? 27 ASP A CB 1 ATOM 206 C CG . ASP A 1 27 ? 2.382 36.281 0.027 1.00 30.00 ? 27 ASP A CG 1 ATOM 207 O OD1 . ASP A 1 27 ? 1.270 36.682 -0.370 1.00 33.53 ? 27 ASP A OD1 1 ATOM 208 O OD2 . ASP A 1 27 ? 2.696 36.541 1.206 1.00 28.50 ? 27 ASP A OD2 1 ATOM 209 N N . GLU A 1 28 ? 5.864 35.920 0.379 1.00 27.68 ? 28 GLU A N 1 ATOM 210 C CA . GLU A 1 28 ? 6.817 36.481 1.317 1.00 28.04 ? 28 GLU A CA 1 ATOM 211 C C . GLU A 1 28 ? 6.194 37.069 2.575 1.00 28.53 ? 28 GLU A C 1 ATOM 212 O O . GLU A 1 28 ? 6.665 36.811 3.693 1.00 27.83 ? 28 GLU A O 1 ATOM 213 C CB . GLU A 1 28 ? 7.682 37.538 0.629 1.00 27.81 ? 28 GLU A CB 1 ATOM 214 C CG . GLU A 1 28 ? 8.903 37.915 1.445 1.00 28.78 ? 28 GLU A CG 1 ATOM 215 C CD . GLU A 1 28 ? 9.609 39.164 0.950 1.00 29.86 ? 28 GLU A CD 1 ATOM 216 O OE1 . GLU A 1 28 ? 10.827 39.209 1.040 1.00 30.41 ? 28 GLU A OE1 1 ATOM 217 O OE2 . GLU A 1 28 ? 8.971 40.110 0.471 1.00 32.80 ? 28 GLU A OE2 1 ATOM 218 N N . SER A 1 29 ? 5.139 37.856 2.387 1.00 29.30 ? 29 SER A N 1 ATOM 219 C CA . SER A 1 29 ? 4.547 38.602 3.489 1.00 30.33 ? 29 SER A CA 1 ATOM 220 C C . SER A 1 29 ? 4.131 37.706 4.648 1.00 30.41 ? 29 SER A C 1 ATOM 221 O O . SER A 1 29 ? 4.227 38.082 5.817 1.00 30.99 ? 29 SER A O 1 ATOM 222 C CB . SER A 1 29 ? 3.366 39.445 3.006 1.00 30.54 ? 29 SER A CB 1 ATOM 223 O OG . SER A 1 29 ? 2.262 38.640 2.596 1.00 32.27 ? 29 SER A OG 1 ATOM 224 N N . LYS A 1 30 ? 3.668 36.517 4.302 1.00 30.48 ? 30 LYS A N 1 ATOM 225 C CA . LYS A 1 30 ? 3.254 35.530 5.278 1.00 30.33 ? 30 LYS A CA 1 ATOM 226 C C . LYS A 1 30 ? 4.432 35.071 6.111 1.00 30.03 ? 30 LYS A C 1 ATOM 227 O O . LYS A 1 30 ? 4.266 34.712 7.280 1.00 29.41 ? 30 LYS A O 1 ATOM 228 C CB . LYS A 1 30 ? 2.570 34.351 4.578 1.00 30.98 ? 30 LYS A CB 1 ATOM 229 C CG . LYS A 1 30 ? 1.228 34.731 3.999 1.00 31.43 ? 30 LYS A CG 1 ATOM 230 C CD . LYS A 1 30 ? 0.477 33.562 3.393 1.00 34.28 ? 30 LYS A CD 1 ATOM 231 C CE . LYS A 1 30 ? -0.980 33.970 3.141 1.00 34.48 ? 30 LYS A CE 1 ATOM 232 N NZ . LYS A 1 30 ? -1.711 33.107 2.161 1.00 35.77 ? 30 LYS A NZ 1 ATOM 233 N N . PHE A 1 31 ? 5.626 35.079 5.525 1.00 29.18 ? 31 PHE A N 1 ATOM 234 C CA . PHE A 1 31 ? 6.795 34.723 6.301 1.00 29.24 ? 31 PHE A CA 1 ATOM 235 C C . PHE A 1 31 ? 7.320 35.911 7.089 1.00 29.79 ? 31 PHE A C 1 ATOM 236 O O . PHE A 1 31 ? 7.811 35.747 8.204 1.00 29.44 ? 31 PHE A O 1 ATOM 237 C CB . PHE A 1 31 ? 7.869 34.084 5.416 1.00 29.17 ? 31 PHE A CB 1 ATOM 238 C CG . PHE A 1 31 ? 7.433 32.799 4.851 1.00 27.06 ? 31 PHE A CG 1 ATOM 239 C CD1 . PHE A 1 31 ? 7.529 31.645 5.599 1.00 24.88 ? 31 PHE A CD1 1 ATOM 240 C CD2 . PHE A 1 31 ? 6.914 32.732 3.576 1.00 26.76 ? 31 PHE A CD2 1 ATOM 241 C CE1 . PHE A 1 31 ? 7.117 30.439 5.081 1.00 23.44 ? 31 PHE A CE1 1 ATOM 242 C CE2 . PHE A 1 31 ? 6.506 31.531 3.060 1.00 27.50 ? 31 PHE A CE2 1 ATOM 243 C CZ . PHE A 1 31 ? 6.608 30.376 3.820 1.00 26.35 ? 31 PHE A CZ 1 ATOM 244 N N . LEU A 1 32 ? 7.211 37.100 6.500 1.00 30.31 ? 32 LEU A N 1 ATOM 245 C CA . LEU A 1 32 ? 7.675 38.323 7.143 1.00 31.13 ? 32 LEU A CA 1 ATOM 246 C C . LEU A 1 32 ? 6.795 38.609 8.348 1.00 31.33 ? 32 LEU A C 1 ATOM 247 O O . LEU A 1 32 ? 7.281 39.014 9.394 1.00 30.94 ? 32 LEU A O 1 ATOM 248 C CB . LEU A 1 32 ? 7.632 39.500 6.172 1.00 31.23 ? 32 LEU A CB 1 ATOM 249 C CG . LEU A 1 32 ? 8.684 39.514 5.062 1.00 32.32 ? 32 LEU A CG 1 ATOM 250 C CD1 . LEU A 1 32 ? 8.425 40.703 4.158 1.00 32.19 ? 32 LEU A CD1 1 ATOM 251 C CD2 . LEU A 1 32 ? 10.075 39.595 5.659 1.00 32.00 ? 32 LEU A CD2 1 ATOM 252 N N . SER A 1 33 ? 5.492 38.394 8.199 1.00 31.90 ? 33 SER A N 1 ATOM 253 C CA . SER A 1 33 ? 4.596 38.608 9.332 1.00 33.00 ? 33 SER A CA 1 ATOM 254 C C . SER A 1 33 ? 4.843 37.553 10.422 1.00 32.35 ? 33 SER A C 1 ATOM 255 O O . SER A 1 33 ? 4.983 37.902 11.584 1.00 32.38 ? 33 SER A O 1 ATOM 256 C CB . SER A 1 33 ? 3.133 38.670 8.894 1.00 33.49 ? 33 SER A CB 1 ATOM 257 O OG . SER A 1 33 ? 2.623 37.377 8.621 1.00 36.94 ? 33 SER A OG 1 ATOM 258 N N . ALA A 1 34 ? 4.897 36.275 10.039 1.00 31.99 ? 34 ALA A N 1 ATOM 259 C CA . ALA A 1 34 ? 5.247 35.188 10.962 1.00 31.42 ? 34 ALA A CA 1 ATOM 260 C C . ALA A 1 34 ? 6.489 35.526 11.756 1.00 31.23 ? 34 ALA A C 1 ATOM 261 O O . ALA A 1 34 ? 6.527 35.338 12.971 1.00 31.28 ? 34 ALA A O 1 ATOM 262 C CB . ALA A 1 34 ? 5.467 33.885 10.208 1.00 31.57 ? 34 ALA A CB 1 ATOM 263 N N . ALA A 1 35 ? 7.509 36.024 11.064 1.00 30.74 ? 35 ALA A N 1 ATOM 264 C CA . ALA A 1 35 ? 8.770 36.372 11.703 1.00 30.22 ? 35 ALA A CA 1 ATOM 265 C C . ALA A 1 35 ? 8.613 37.558 12.641 1.00 29.92 ? 35 ALA A C 1 ATOM 266 O O . ALA A 1 35 ? 9.121 37.534 13.756 1.00 29.02 ? 35 ALA A O 1 ATOM 267 C CB . ALA A 1 35 ? 9.818 36.670 10.665 1.00 30.50 ? 35 ALA A CB 1 ATOM 268 N N . GLU A 1 36 ? 7.912 38.594 12.190 1.00 29.85 ? 36 GLU A N 1 ATOM 269 C CA . GLU A 1 36 ? 7.733 39.784 13.022 1.00 30.34 ? 36 GLU A CA 1 ATOM 270 C C . GLU A 1 36 ? 7.047 39.377 14.304 1.00 29.48 ? 36 GLU A C 1 ATOM 271 O O . GLU A 1 36 ? 7.386 39.868 15.377 1.00 29.47 ? 36 GLU A O 1 ATOM 272 C CB . GLU A 1 36 ? 6.875 40.848 12.328 1.00 30.93 ? 36 GLU A CB 1 ATOM 273 C CG . GLU A 1 36 ? 7.492 41.544 11.122 1.00 34.64 ? 36 GLU A CG 1 ATOM 274 C CD . GLU A 1 36 ? 8.987 41.792 11.253 1.00 39.21 ? 36 GLU A CD 1 ATOM 275 O OE1 . GLU A 1 36 ? 9.467 42.104 12.366 1.00 42.38 ? 36 GLU A OE1 1 ATOM 276 O OE2 . GLU A 1 36 ? 9.694 41.672 10.222 1.00 43.00 ? 36 GLU A OE2 1 ATOM 277 N N . LEU A 1 37 ? 6.080 38.474 14.162 1.00 28.75 ? 37 LEU A N 1 ATOM 278 C CA . LEU A 1 37 ? 5.236 38.016 15.260 1.00 28.26 ? 37 LEU A CA 1 ATOM 279 C C . LEU A 1 37 ? 5.963 37.065 16.192 1.00 27.71 ? 37 LEU A C 1 ATOM 280 O O . LEU A 1 37 ? 5.756 37.101 17.407 1.00 27.03 ? 37 LEU A O 1 ATOM 281 C CB . LEU A 1 37 ? 3.944 37.405 14.714 1.00 28.59 ? 37 LEU A CB 1 ATOM 282 C CG . LEU A 1 37 ? 2.929 38.460 14.256 1.00 29.23 ? 37 LEU A CG 1 ATOM 283 C CD1 . LEU A 1 37 ? 1.796 37.852 13.432 1.00 29.48 ? 37 LEU A CD1 1 ATOM 284 C CD2 . LEU A 1 37 ? 2.373 39.231 15.464 1.00 30.68 ? 37 LEU A CD2 1 ATOM 285 N N . ILE A 1 38 ? 6.816 36.212 15.630 1.00 26.95 ? 38 ILE A N 1 ATOM 286 C CA . ILE A 1 38 ? 7.645 35.353 16.456 1.00 27.23 ? 38 ILE A CA 1 ATOM 287 C C . ILE A 1 38 ? 8.496 36.233 17.367 1.00 28.09 ? 38 ILE A C 1 ATOM 288 O O . ILE A 1 38 ? 8.718 35.913 18.542 1.00 27.72 ? 38 ILE A O 1 ATOM 289 C CB . ILE A 1 38 ? 8.534 34.424 15.588 1.00 26.91 ? 38 ILE A CB 1 ATOM 290 C CG1 . ILE A 1 38 ? 7.729 33.204 15.134 1.00 26.70 ? 38 ILE A CG1 1 ATOM 291 C CG2 . ILE A 1 38 ? 9.715 33.936 16.388 1.00 25.88 ? 38 ILE A CG2 1 ATOM 292 C CD1 . ILE A 1 38 ? 8.234 32.589 13.835 1.00 28.71 ? 38 ILE A CD1 1 ATOM 293 N N . VAL A 1 39 ? 8.974 37.350 16.822 1.00 28.96 ? 39 VAL A N 1 ATOM 294 C CA . VAL A 1 39 ? 9.815 38.254 17.601 1.00 30.07 ? 39 VAL A CA 1 ATOM 295 C C . VAL A 1 39 ? 8.979 38.985 18.646 1.00 30.22 ? 39 VAL A C 1 ATOM 296 O O . VAL A 1 39 ? 9.317 38.966 19.834 1.00 30.77 ? 39 VAL A O 1 ATOM 297 C CB . VAL A 1 39 ? 10.576 39.250 16.699 1.00 30.25 ? 39 VAL A CB 1 ATOM 298 C CG1 . VAL A 1 39 ? 11.194 40.350 17.531 1.00 32.12 ? 39 VAL A CG1 1 ATOM 299 C CG2 . VAL A 1 39 ? 11.657 38.524 15.911 1.00 30.87 ? 39 VAL A CG2 1 ATOM 300 N N . SER A 1 40 ? 7.891 39.617 18.201 1.00 30.40 ? 40 SER A N 1 ATOM 301 C CA . SER A 1 40 ? 7.103 40.506 19.057 1.00 30.56 ? 40 SER A CA 1 ATOM 302 C C . SER A 1 40 ? 6.227 39.799 20.085 1.00 30.86 ? 40 SER A C 1 ATOM 303 O O . SER A 1 40 ? 5.956 40.343 21.148 1.00 30.68 ? 40 SER A O 1 ATOM 304 C CB . SER A 1 40 ? 6.236 41.418 18.203 1.00 30.94 ? 40 SER A CB 1 ATOM 305 O OG . SER A 1 40 ? 5.139 40.691 17.663 1.00 30.96 ? 40 SER A OG 1 ATOM 306 N N . SER A 1 41 ? 5.783 38.588 19.759 1.00 30.81 ? 41 SER A N 1 ATOM 307 C CA . SER A 1 41 ? 5.019 37.756 20.681 1.00 30.50 ? 41 SER A CA 1 ATOM 308 C C . SER A 1 41 ? 5.900 37.110 21.749 1.00 29.75 ? 41 SER A C 1 ATOM 309 O O . SER A 1 41 ? 5.399 36.480 22.682 1.00 30.05 ? 41 SER A O 1 ATOM 310 C CB . SER A 1 41 ? 4.314 36.646 19.904 1.00 31.08 ? 41 SER A CB 1 ATOM 311 O OG . SER A 1 41 ? 5.262 35.690 19.447 1.00 32.55 ? 41 SER A OG 1 ATOM 312 N N . GLY A 1 42 ? 7.211 37.258 21.615 1.00 29.00 ? 42 GLY A N 1 ATOM 313 C CA . GLY A 1 42 ? 8.153 36.670 22.552 1.00 28.19 ? 42 GLY A CA 1 ATOM 314 C C . GLY A 1 42 ? 8.483 35.208 22.285 1.00 26.92 ? 42 GLY A C 1 ATOM 315 O O . GLY A 1 42 ? 9.182 34.564 23.071 1.00 27.14 ? 42 GLY A O 1 ATOM 316 N N . LEU A 1 43 ? 7.985 34.677 21.178 1.00 25.96 ? 43 LEU A N 1 ATOM 317 C CA . LEU A 1 43 ? 8.283 33.296 20.805 1.00 25.47 ? 43 LEU A CA 1 ATOM 318 C C . LEU A 1 43 ? 9.765 33.047 20.521 1.00 25.36 ? 43 LEU A C 1 ATOM 319 O O . LEU A 1 43 ? 10.310 32.003 20.891 1.00 25.64 ? 43 LEU A O 1 ATOM 320 C CB . LEU A 1 43 ? 7.407 32.851 19.634 1.00 24.58 ? 43 LEU A CB 1 ATOM 321 C CG . LEU A 1 43 ? 5.972 32.598 20.112 1.00 23.92 ? 43 LEU A CG 1 ATOM 322 C CD1 . LEU A 1 43 ? 5.019 32.482 18.934 1.00 23.64 ? 43 LEU A CD1 1 ATOM 323 C CD2 . LEU A 1 43 ? 5.919 31.369 20.999 1.00 20.47 ? 43 LEU A CD2 1 ATOM 324 N N . LEU A 1 44 ? 10.425 33.997 19.866 1.00 25.45 ? 44 LEU A N 1 ATOM 325 C CA . LEU A 1 44 ? 11.859 33.875 19.649 1.00 25.58 ? 44 LEU A CA 1 ATOM 326 C C . LEU A 1 44 ? 12.586 33.765 20.993 1.00 26.09 ? 44 LEU A C 1 ATOM 327 O O . LEU A 1 44 ? 13.398 32.850 21.205 1.00 25.23 ? 44 LEU A O 1 ATOM 328 C CB . LEU A 1 44 ? 12.407 35.064 18.849 1.00 25.93 ? 44 LEU A CB 1 ATOM 329 C CG . LEU A 1 44 ? 13.940 35.038 18.767 1.00 26.64 ? 44 LEU A CG 1 ATOM 330 C CD1 . LEU A 1 44 ? 14.459 33.805 18.046 1.00 27.16 ? 44 LEU A CD1 1 ATOM 331 C CD2 . LEU A 1 44 ? 14.476 36.299 18.125 1.00 27.86 ? 44 LEU A CD2 1 ATOM 332 N N . ASP A 1 45 ? 12.294 34.699 21.898 1.00 26.09 ? 45 ASP A N 1 ATOM 333 C CA . ASP A 1 45 ? 12.875 34.653 23.245 1.00 26.97 ? 45 ASP A CA 1 ATOM 334 C C . ASP A 1 45 ? 12.630 33.281 23.883 1.00 25.83 ? 45 ASP A C 1 ATOM 335 O O . ASP A 1 45 ? 13.495 32.762 24.586 1.00 25.22 ? 45 ASP A O 1 ATOM 336 C CB . ASP A 1 45 ? 12.301 35.764 24.134 1.00 28.19 ? 45 ASP A CB 1 ATOM 337 C CG . ASP A 1 45 ? 12.733 37.160 23.683 1.00 32.22 ? 45 ASP A CG 1 ATOM 338 O OD1 . ASP A 1 45 ? 13.845 37.295 23.115 1.00 35.06 ? 45 ASP A OD1 1 ATOM 339 O OD2 . ASP A 1 45 ? 12.023 38.176 23.856 1.00 36.54 ? 45 ASP A OD2 1 ATOM 340 N N . ALA A 1 46 ? 11.453 32.706 23.628 1.00 24.86 ? 46 ALA A N 1 ATOM 341 C CA . ALA A 1 46 ? 11.143 31.342 24.083 1.00 24.27 ? 46 ALA A CA 1 ATOM 342 C C . ALA A 1 46 ? 11.990 30.243 23.408 1.00 23.68 ? 46 ALA A C 1 ATOM 343 O O . ALA A 1 46 ? 12.163 29.161 23.963 1.00 23.83 ? 46 ALA A O 1 ATOM 344 C CB . ALA A 1 46 ? 9.665 31.050 23.925 1.00 24.26 ? 46 ALA A CB 1 ATOM 345 N N . GLY A 1 47 ? 12.519 30.509 22.218 1.00 22.94 ? 47 GLY A N 1 ATOM 346 C CA . GLY A 1 47 ? 13.385 29.535 21.574 1.00 22.16 ? 47 GLY A CA 1 ATOM 347 C C . GLY A 1 47 ? 13.039 29.245 20.127 1.00 21.80 ? 47 GLY A C 1 ATOM 348 O O . GLY A 1 47 ? 13.833 28.652 19.402 1.00 22.07 ? 47 GLY A O 1 ATOM 349 N N . TYR A 1 48 ? 11.855 29.665 19.700 1.00 21.25 ? 48 TYR A N 1 ATOM 350 C CA . TYR A 1 48 ? 11.392 29.369 18.350 1.00 21.18 ? 48 TYR A CA 1 ATOM 351 C C . TYR A 1 48 ? 12.114 30.281 17.375 1.00 21.34 ? 48 TYR A C 1 ATOM 352 O O . TYR A 1 48 ? 11.760 31.453 17.238 1.00 21.91 ? 48 TYR A O 1 ATOM 353 C CB . TYR A 1 48 ? 9.896 29.612 18.240 1.00 20.56 ? 48 TYR A CB 1 ATOM 354 C CG . TYR A 1 48 ? 9.052 28.718 19.103 1.00 21.30 ? 48 TYR A CG 1 ATOM 355 C CD1 . TYR A 1 48 ? 8.541 27.529 18.607 1.00 18.89 ? 48 TYR A CD1 1 ATOM 356 C CD2 . TYR A 1 48 ? 8.756 29.062 20.421 1.00 20.87 ? 48 TYR A CD2 1 ATOM 357 C CE1 . TYR A 1 48 ? 7.765 26.706 19.389 1.00 20.17 ? 48 TYR A CE1 1 ATOM 358 C CE2 . TYR A 1 48 ? 7.975 28.239 21.216 1.00 21.43 ? 48 TYR A CE2 1 ATOM 359 C CZ . TYR A 1 48 ? 7.482 27.059 20.693 1.00 20.28 ? 48 TYR A CZ 1 ATOM 360 O OH . TYR A 1 48 ? 6.704 26.222 21.460 1.00 20.23 ? 48 TYR A OH 1 ATOM 361 N N . ASN A 1 49 ? 13.125 29.751 16.698 1.00 20.86 ? 49 ASN A N 1 ATOM 362 C CA . ASN A 1 49 ? 13.925 30.588 15.818 1.00 20.93 ? 49 ASN A CA 1 ATOM 363 C C . ASN A 1 49 ? 13.964 30.236 14.327 1.00 20.31 ? 49 ASN A C 1 ATOM 364 O O . ASN A 1 49 ? 14.629 30.918 13.549 1.00 20.88 ? 49 ASN A O 1 ATOM 365 C CB . ASN A 1 49 ? 15.346 30.682 16.359 1.00 21.19 ? 49 ASN A CB 1 ATOM 366 C CG . ASN A 1 49 ? 16.067 29.343 16.362 1.00 22.95 ? 49 ASN A CG 1 ATOM 367 O OD1 . ASN A 1 49 ? 15.460 28.276 16.471 1.00 20.76 ? 49 ASN A OD1 1 ATOM 368 N ND2 . ASN A 1 49 ? 17.387 29.403 16.243 1.00 24.91 ? 49 ASN A ND2 1 ATOM 369 N N . TYR A 1 50 ? 13.269 29.186 13.920 1.00 19.40 ? 50 TYR A N 1 ATOM 370 C CA . TYR A 1 50 ? 13.202 28.869 12.500 1.00 19.18 ? 50 TYR A CA 1 ATOM 371 C C . TYR A 1 50 ? 11.887 29.403 11.959 1.00 19.31 ? 50 TYR A C 1 ATOM 372 O O . TYR A 1 50 ? 10.834 29.161 12.541 1.00 18.88 ? 50 TYR A O 1 ATOM 373 C CB . TYR A 1 50 ? 13.285 27.366 12.249 1.00 18.83 ? 50 TYR A CB 1 ATOM 374 C CG . TYR A 1 50 ? 14.667 26.768 12.439 1.00 18.02 ? 50 TYR A CG 1 ATOM 375 C CD1 . TYR A 1 50 ? 15.589 26.767 11.411 1.00 17.18 ? 50 TYR A CD1 1 ATOM 376 C CD2 . TYR A 1 50 ? 15.044 26.206 13.651 1.00 19.14 ? 50 TYR A CD2 1 ATOM 377 C CE1 . TYR A 1 50 ? 16.853 26.222 11.576 1.00 18.11 ? 50 TYR A CE1 1 ATOM 378 C CE2 . TYR A 1 50 ? 16.307 25.658 13.829 1.00 18.67 ? 50 TYR A CE2 1 ATOM 379 C CZ . TYR A 1 50 ? 17.204 25.670 12.783 1.00 18.66 ? 50 TYR A CZ 1 ATOM 380 O OH . TYR A 1 50 ? 18.457 25.131 12.950 1.00 18.56 ? 50 TYR A OH 1 ATOM 381 N N . VAL A 1 51 ? 11.963 30.128 10.849 1.00 18.71 ? 51 VAL A N 1 ATOM 382 C CA . VAL A 1 51 ? 10.789 30.491 10.072 1.00 18.75 ? 51 VAL A CA 1 ATOM 383 C C . VAL A 1 51 ? 10.986 29.629 8.818 1.00 18.15 ? 51 VAL A C 1 ATOM 384 O O . VAL A 1 51 ? 11.918 29.875 8.056 1.00 17.16 ? 51 VAL A O 1 ATOM 385 C CB . VAL A 1 51 ? 10.811 31.977 9.695 1.00 18.58 ? 51 VAL A CB 1 ATOM 386 C CG1 . VAL A 1 51 ? 9.690 32.305 8.743 1.00 21.20 ? 51 VAL A CG1 1 ATOM 387 C CG2 . VAL A 1 51 ? 10.744 32.851 10.961 1.00 20.53 ? 51 VAL A CG2 1 ATOM 388 N N . ASN A 1 52 ? 10.119 28.633 8.619 1.00 17.03 ? 52 ASN A N 1 ATOM 389 C CA . ASN A 1 52 ? 10.338 27.596 7.608 1.00 17.14 ? 52 ASN A CA 1 ATOM 390 C C . ASN A 1 52 ? 9.332 27.623 6.508 1.00 17.26 ? 52 ASN A C 1 ATOM 391 O O . ASN A 1 52 ? 8.111 27.509 6.721 1.00 16.78 ? 52 ASN A O 1 ATOM 392 C CB . ASN A 1 52 ? 10.375 26.179 8.202 1.00 16.89 ? 52 ASN A CB 1 ATOM 393 C CG . ASN A 1 52 ? 11.606 25.944 9.051 1.00 17.60 ? 52 ASN A CG 1 ATOM 394 O OD1 . ASN A 1 52 ? 12.508 26.752 9.053 1.00 15.84 ? 52 ASN A OD1 1 ATOM 395 N ND2 . ASN A 1 52 ? 11.638 24.834 9.770 1.00 18.34 ? 52 ASN A ND2 1 ATOM 396 N N . ILE A 1 53 ? 9.862 27.777 5.312 1.00 17.34 ? 53 ILE A N 1 ATOM 397 C CA . ILE A 1 53 ? 9.034 27.748 4.143 1.00 17.84 ? 53 ILE A CA 1 ATOM 398 C C . ILE A 1 53 ? 8.824 26.286 3.857 1.00 18.37 ? 53 ILE A C 1 ATOM 399 O O . ILE A 1 53 ? 9.777 25.510 3.854 1.00 18.96 ? 53 ILE A O 1 ATOM 400 C CB . ILE A 1 53 ? 9.762 28.393 2.950 1.00 17.64 ? 53 ILE A CB 1 ATOM 401 C CG1 . ILE A 1 53 ? 10.092 29.854 3.254 1.00 17.57 ? 53 ILE A CG1 1 ATOM 402 C CG2 . ILE A 1 53 ? 8.897 28.298 1.685 1.00 17.82 ? 53 ILE A CG2 1 ATOM 403 C CD1 . ILE A 1 53 ? 11.142 30.430 2.315 1.00 18.05 ? 53 ILE A CD1 1 ATOM 404 N N . ASP A 1 54 ? 7.574 25.921 3.620 1.00 18.30 ? 54 ASP A N 1 ATOM 405 C CA . ASP A 1 54 ? 7.240 24.585 3.218 1.00 18.91 ? 54 ASP A CA 1 ATOM 406 C C . ASP A 1 54 ? 7.048 24.536 1.688 1.00 19.14 ? 54 ASP A C 1 ATOM 407 O O . ASP A 1 54 ? 7.677 25.298 0.950 1.00 19.21 ? 54 ASP A O 1 ATOM 408 C CB . ASP A 1 54 ? 5.978 24.109 3.949 1.00 19.10 ? 54 ASP A CB 1 ATOM 409 C CG . ASP A 1 54 ? 5.979 22.622 4.161 1.00 19.15 ? 54 ASP A CG 1 ATOM 410 O OD1 . ASP A 1 54 ? 5.336 21.897 3.371 1.00 19.98 ? 54 ASP A OD1 1 ATOM 411 O OD2 . ASP A 1 54 ? 6.596 22.091 5.093 1.00 19.17 ? 54 ASP A OD2 1 ATOM 412 N N . ASP A 1 55 ? 6.195 23.649 1.211 1.00 18.94 ? 55 ASP A N 1 ATOM 413 C CA . ASP A 1 55 ? 5.981 23.485 -0.223 1.00 19.07 ? 55 ASP A CA 1 ATOM 414 C C . ASP A 1 55 ? 5.358 24.708 -0.885 1.00 19.65 ? 55 ASP A C 1 ATOM 415 O O . ASP A 1 55 ? 4.741 25.539 -0.212 1.00 20.62 ? 55 ASP A O 1 ATOM 416 C CB . ASP A 1 55 ? 5.085 22.275 -0.423 1.00 18.47 ? 55 ASP A CB 1 ATOM 417 C CG . ASP A 1 55 ? 5.296 21.592 -1.736 1.00 17.80 ? 55 ASP A CG 1 ATOM 418 O OD1 . ASP A 1 55 ? 5.914 22.165 -2.656 1.00 18.06 ? 55 ASP A OD1 1 ATOM 419 O OD2 . ASP A 1 55 ? 4.865 20.449 -1.941 1.00 17.01 ? 55 ASP A OD2 1 ATOM 420 N N . CYS A 1 56 ? 5.530 24.804 -2.205 1.00 20.19 ? 56 CYS A N 1 ATOM 421 C CA . CYS A 1 56 ? 4.852 25.789 -3.052 1.00 20.64 ? 56 CYS A CA 1 ATOM 422 C C . CYS A 1 56 ? 5.536 27.134 -3.167 1.00 20.71 ? 56 CYS A C 1 ATOM 423 O O . CYS A 1 56 ? 4.889 28.117 -3.530 1.00 20.24 ? 56 CYS A O 1 ATOM 424 C CB . CYS A 1 56 ? 3.399 25.996 -2.605 1.00 20.34 ? 56 CYS A CB 1 ATOM 425 S SG . CYS A 1 56 ? 2.454 24.460 -2.478 1.00 23.79 ? 56 CYS A SG 1 ATOM 426 N N . TRP A 1 57 ? 6.835 27.179 -2.864 1.00 19.72 ? 57 TRP A N 1 ATOM 427 C CA . TRP A 1 57 ? 7.590 28.423 -2.934 1.00 20.35 ? 57 TRP A CA 1 ATOM 428 C C . TRP A 1 57 ? 8.237 28.667 -4.291 1.00 20.75 ? 57 TRP A C 1 ATOM 429 O O . TRP A 1 57 ? 8.617 29.783 -4.622 1.00 21.50 ? 57 TRP A O 1 ATOM 430 C CB . TRP A 1 57 ? 8.677 28.449 -1.844 1.00 20.10 ? 57 TRP A CB 1 ATOM 431 C CG . TRP A 1 57 ? 9.716 27.330 -1.976 1.00 19.63 ? 57 TRP A CG 1 ATOM 432 C CD1 . TRP A 1 57 ? 9.668 26.085 -1.410 1.00 19.80 ? 57 TRP A CD1 1 ATOM 433 C CD2 . TRP A 1 57 ? 10.933 27.379 -2.720 1.00 20.98 ? 57 TRP A CD2 1 ATOM 434 N NE1 . TRP A 1 57 ? 10.784 25.358 -1.758 1.00 19.78 ? 57 TRP A NE1 1 ATOM 435 C CE2 . TRP A 1 57 ? 11.578 26.134 -2.563 1.00 20.43 ? 57 TRP A CE2 1 ATOM 436 C CE3 . TRP A 1 57 ? 11.552 28.353 -3.506 1.00 20.97 ? 57 TRP A CE3 1 ATOM 437 C CZ2 . TRP A 1 57 ? 12.802 25.846 -3.164 1.00 21.48 ? 57 TRP A CZ2 1 ATOM 438 C CZ3 . TRP A 1 57 ? 12.763 28.065 -4.100 1.00 22.36 ? 57 TRP A CZ3 1 ATOM 439 C CH2 . TRP A 1 57 ? 13.374 26.822 -3.925 1.00 22.76 ? 57 TRP A CH2 1 ATOM 440 N N . SER A 1 58 ? 8.365 27.625 -5.090 1.00 21.69 ? 58 SER A N 1 ATOM 441 C CA . SER A 1 58 ? 9.187 27.743 -6.283 1.00 22.83 ? 58 SER A CA 1 ATOM 442 C C . SER A 1 58 ? 8.345 27.971 -7.528 1.00 24.08 ? 58 SER A C 1 ATOM 443 O O . SER A 1 58 ? 7.112 27.907 -7.466 1.00 23.87 ? 58 SER A O 1 ATOM 444 C CB . SER A 1 58 ? 10.048 26.493 -6.413 1.00 21.83 ? 58 SER A CB 1 ATOM 445 O OG . SER A 1 58 ? 9.231 25.333 -6.494 1.00 23.57 ? 58 SER A OG 1 ATOM 446 N N . MET A 1 59 ? 9.000 28.243 -8.659 1.00 25.20 ? 59 MET A N 1 ATOM 447 C CA . MET A 1 59 ? 8.259 28.357 -9.913 1.00 26.90 ? 59 MET A CA 1 ATOM 448 C C . MET A 1 59 ? 7.812 26.958 -10.266 1.00 27.48 ? 59 MET A C 1 ATOM 449 O O . MET A 1 59 ? 8.621 26.056 -10.415 1.00 28.34 ? 59 MET A O 1 ATOM 450 C CB . MET A 1 59 ? 9.107 28.952 -11.020 1.00 26.85 ? 59 MET A CB 1 ATOM 451 C CG . MET A 1 59 ? 9.427 30.405 -10.786 1.00 29.97 ? 59 MET A CG 1 ATOM 452 S SD . MET A 1 59 ? 7.943 31.426 -10.927 1.00 35.88 ? 59 MET A SD 1 ATOM 453 C CE . MET A 1 59 ? 8.037 31.776 -12.719 1.00 33.10 ? 59 MET A CE 1 ATOM 454 N N . LYS A 1 60 ? 6.518 26.779 -10.400 1.00 28.35 ? 60 LYS A N 1 ATOM 455 C CA . LYS A 1 60 ? 5.970 25.434 -10.463 1.00 29.98 ? 60 LYS A CA 1 ATOM 456 C C . LYS A 1 60 ? 6.237 24.663 -11.741 1.00 30.73 ? 60 LYS A C 1 ATOM 457 O O . LYS A 1 60 ? 6.220 23.431 -11.754 1.00 31.64 ? 60 LYS A O 1 ATOM 458 C CB . LYS A 1 60 ? 4.473 25.483 -10.219 1.00 29.51 ? 60 LYS A CB 1 ATOM 459 C CG . LYS A 1 60 ? 3.829 24.126 -10.287 1.00 30.15 ? 60 LYS A CG 1 ATOM 460 C CD . LYS A 1 60 ? 2.456 24.163 -9.676 1.00 30.92 ? 60 LYS A CD 1 ATOM 461 C CE . LYS A 1 60 ? 1.912 22.765 -9.537 1.00 31.66 ? 60 LYS A CE 1 ATOM 462 N NZ . LYS A 1 60 ? 0.609 22.795 -8.847 1.00 34.07 ? 60 LYS A NZ 1 ATOM 463 N N . ASP A 1 61 ? 6.488 25.383 -12.816 1.00 31.36 ? 61 ASP A N 1 ATOM 464 C CA . ASP A 1 61 ? 6.561 24.738 -14.115 1.00 32.58 ? 61 ASP A CA 1 ATOM 465 C C . ASP A 1 61 ? 7.902 24.092 -14.476 1.00 32.02 ? 61 ASP A C 1 ATOM 466 O O . ASP A 1 61 ? 8.044 23.556 -15.564 1.00 32.57 ? 61 ASP A O 1 ATOM 467 C CB . ASP A 1 61 ? 6.137 25.712 -15.205 1.00 33.48 ? 61 ASP A CB 1 ATOM 468 C CG . ASP A 1 61 ? 6.609 27.125 -14.941 1.00 36.60 ? 61 ASP A CG 1 ATOM 469 O OD1 . ASP A 1 61 ? 6.033 28.042 -15.564 1.00 40.32 ? 61 ASP A OD1 1 ATOM 470 O OD2 . ASP A 1 61 ? 7.535 27.418 -14.141 1.00 40.64 ? 61 ASP A OD2 1 ATOM 471 N N . GLY A 1 62 ? 8.870 24.145 -13.579 1.00 30.86 ? 62 GLY A N 1 ATOM 472 C CA . GLY A 1 62 ? 10.147 23.511 -13.838 1.00 30.07 ? 62 GLY A CA 1 ATOM 473 C C . GLY A 1 62 ? 11.331 24.316 -13.362 1.00 29.79 ? 62 GLY A C 1 ATOM 474 O O . GLY A 1 62 ? 11.209 25.482 -12.980 1.00 28.83 ? 62 GLY A O 1 ATOM 475 N N . ARG A 1 63 ? 12.488 23.669 -13.390 1.00 29.79 ? 63 ARG A N 1 ATOM 476 C CA . ARG A 1 63 ? 13.749 24.321 -13.117 1.00 29.98 ? 63 ARG A CA 1 ATOM 477 C C . ARG A 1 63 ? 14.000 25.419 -14.130 1.00 30.50 ? 63 ARG A C 1 ATOM 478 O O . ARG A 1 63 ? 13.615 25.314 -15.287 1.00 31.32 ? 63 ARG A O 1 ATOM 479 C CB . ARG A 1 63 ? 14.896 23.312 -13.207 1.00 29.99 ? 63 ARG A CB 1 ATOM 480 C CG . ARG A 1 63 ? 14.886 22.330 -12.104 1.00 28.19 ? 63 ARG A CG 1 ATOM 481 C CD . ARG A 1 63 ? 16.069 21.387 -12.052 1.00 25.28 ? 63 ARG A CD 1 ATOM 482 N NE . ARG A 1 63 ? 15.896 20.692 -10.802 1.00 21.42 ? 63 ARG A NE 1 ATOM 483 C CZ . ARG A 1 63 ? 16.562 20.951 -9.691 1.00 20.68 ? 63 ARG A CZ 1 ATOM 484 N NH1 . ARG A 1 63 ? 17.481 21.904 -9.660 1.00 18.38 ? 63 ARG A NH1 1 ATOM 485 N NH2 . ARG A 1 63 ? 16.295 20.240 -8.608 1.00 16.07 ? 63 ARG A NH2 1 ATOM 486 N N . VAL A 1 64 ? 14.650 26.478 -13.688 1.00 30.77 ? 64 VAL A N 1 ATOM 487 C CA . VAL A 1 64 ? 15.019 27.542 -14.588 1.00 31.45 ? 64 VAL A CA 1 ATOM 488 C C . VAL A 1 64 ? 16.522 27.441 -14.698 1.00 30.96 ? 64 VAL A C 1 ATOM 489 O O . VAL A 1 64 ? 17.242 27.685 -13.735 1.00 30.79 ? 64 VAL A O 1 ATOM 490 C CB . VAL A 1 64 ? 14.561 28.934 -14.076 1.00 31.65 ? 64 VAL A CB 1 ATOM 491 C CG1 . VAL A 1 64 ? 15.122 30.056 -14.954 1.00 33.14 ? 64 VAL A CG1 1 ATOM 492 C CG2 . VAL A 1 64 ? 13.039 29.002 -14.013 1.00 33.09 ? 64 VAL A CG2 1 ATOM 493 N N . ASP A 1 65 ? 16.991 27.069 -15.889 1.00 30.88 ? 65 ASP A N 1 ATOM 494 C CA . ASP A 1 65 ? 18.410 26.923 -16.142 1.00 30.45 ? 65 ASP A CA 1 ATOM 495 C C . ASP A 1 65 ? 19.101 25.940 -15.184 1.00 29.12 ? 65 ASP A C 1 ATOM 496 O O . ASP A 1 65 ? 20.215 26.180 -14.724 1.00 28.85 ? 65 ASP A O 1 ATOM 497 C CB . ASP A 1 65 ? 19.082 28.302 -16.188 1.00 31.69 ? 65 ASP A CB 1 ATOM 498 C CG . ASP A 1 65 ? 18.429 29.227 -17.232 1.00 35.08 ? 65 ASP A CG 1 ATOM 499 O OD1 . ASP A 1 65 ? 18.587 28.982 -18.455 1.00 37.99 ? 65 ASP A OD1 1 ATOM 500 O OD2 . ASP A 1 65 ? 17.739 30.222 -16.927 1.00 39.06 ? 65 ASP A OD2 1 ATOM 501 N N . GLY A 1 66 ? 18.424 24.829 -14.898 1.00 27.56 ? 66 GLY A N 1 ATOM 502 C CA . GLY A 1 66 ? 18.975 23.791 -14.041 1.00 26.94 ? 66 GLY A CA 1 ATOM 503 C C . GLY A 1 66 ? 18.831 24.014 -12.539 1.00 25.46 ? 66 GLY A C 1 ATOM 504 O O . GLY A 1 66 ? 19.326 23.228 -11.742 1.00 25.87 ? 66 GLY A O 1 ATOM 505 N N . HIS A 1 67 ? 18.156 25.087 -12.152 1.00 25.23 ? 67 HIS A N 1 ATOM 506 C CA . HIS A 1 67 ? 18.013 25.418 -10.734 1.00 24.71 ? 67 HIS A CA 1 ATOM 507 C C . HIS A 1 67 ? 16.555 25.567 -10.385 1.00 24.20 ? 67 HIS A C 1 ATOM 508 O O . HIS A 1 67 ? 15.765 25.966 -11.232 1.00 24.43 ? 67 HIS A O 1 ATOM 509 C CB . HIS A 1 67 ? 18.673 26.760 -10.438 1.00 24.95 ? 67 HIS A CB 1 ATOM 510 C CG . HIS A 1 67 ? 20.162 26.729 -10.522 1.00 25.84 ? 67 HIS A CG 1 ATOM 511 N ND1 . HIS A 1 67 ? 20.839 26.734 -11.724 1.00 27.69 ? 67 HIS A ND1 1 ATOM 512 C CD2 . HIS A 1 67 ? 21.107 26.692 -9.556 1.00 24.66 ? 67 HIS A CD2 1 ATOM 513 C CE1 . HIS A 1 67 ? 22.140 26.700 -11.488 1.00 26.94 ? 67 HIS A CE1 1 ATOM 514 N NE2 . HIS A 1 67 ? 22.326 26.676 -10.181 1.00 28.21 ? 67 HIS A NE2 1 ATOM 515 N N . ILE A 1 68 ? 16.191 25.250 -9.146 1.00 23.75 ? 68 ILE A N 1 ATOM 516 C CA . ILE A 1 68 ? 14.847 25.556 -8.667 1.00 23.10 ? 68 ILE A CA 1 ATOM 517 C C . ILE A 1 68 ? 14.856 27.064 -8.460 1.00 23.16 ? 68 ILE A C 1 ATOM 518 O O . ILE A 1 68 ? 15.701 27.564 -7.758 1.00 22.96 ? 68 ILE A O 1 ATOM 519 C CB . ILE A 1 68 ? 14.574 24.803 -7.361 1.00 22.76 ? 68 ILE A CB 1 ATOM 520 C CG1 . ILE A 1 68 ? 14.835 23.319 -7.577 1.00 22.58 ? 68 ILE A CG1 1 ATOM 521 C CG2 . ILE A 1 68 ? 13.148 25.032 -6.868 1.00 22.31 ? 68 ILE A CG2 1 ATOM 522 C CD1 . ILE A 1 68 ? 14.618 22.464 -6.377 1.00 22.38 ? 68 ILE A CD1 1 ATOM 523 N N . ALA A 1 69 ? 13.919 27.772 -9.081 1.00 23.86 ? 69 ALA A N 1 ATOM 524 C CA . ALA A 1 69 ? 13.784 29.225 -8.963 1.00 24.91 ? 69 ALA A CA 1 ATOM 525 C C . ALA A 1 69 ? 12.645 29.585 -8.020 1.00 25.70 ? 69 ALA A C 1 ATOM 526 O O . ALA A 1 69 ? 11.596 28.954 -8.059 1.00 25.43 ? 69 ALA A O 1 ATOM 527 C CB . ALA A 1 69 ? 13.494 29.820 -10.315 1.00 24.53 ? 69 ALA A CB 1 ATOM 528 N N . PRO A 1 70 ? 12.844 30.592 -7.171 1.00 26.75 ? 70 PRO A N 1 ATOM 529 C CA . PRO A 1 70 ? 11.764 31.073 -6.313 1.00 27.65 ? 70 PRO A CA 1 ATOM 530 C C . PRO A 1 70 ? 10.691 31.654 -7.205 1.00 28.82 ? 70 PRO A C 1 ATOM 531 O O . PRO A 1 70 ? 11.012 32.267 -8.226 1.00 28.89 ? 70 PRO A O 1 ATOM 532 C CB . PRO A 1 70 ? 12.413 32.205 -5.493 1.00 27.74 ? 70 PRO A CB 1 ATOM 533 C CG . PRO A 1 70 ? 13.905 32.020 -5.643 1.00 27.41 ? 70 PRO A CG 1 ATOM 534 C CD . PRO A 1 70 ? 14.103 31.331 -6.973 1.00 26.99 ? 70 PRO A CD 1 ATOM 535 N N . ASN A 1 71 ? 9.436 31.460 -6.827 1.00 30.08 ? 71 ASN A N 1 ATOM 536 C CA . ASN A 1 71 ? 8.342 32.124 -7.507 1.00 31.02 ? 71 ASN A CA 1 ATOM 537 C C . ASN A 1 71 ? 8.493 33.581 -7.127 1.00 31.35 ? 71 ASN A C 1 ATOM 538 O O . ASN A 1 71 ? 8.260 33.970 -5.985 1.00 30.65 ? 71 ASN A O 1 ATOM 539 C CB . ASN A 1 71 ? 7.005 31.569 -7.046 1.00 31.71 ? 71 ASN A CB 1 ATOM 540 C CG . ASN A 1 71 ? 5.833 32.204 -7.760 1.00 33.65 ? 71 ASN A CG 1 ATOM 541 O OD1 . ASN A 1 71 ? 5.831 33.409 -8.029 1.00 36.58 ? 71 ASN A OD1 1 ATOM 542 N ND2 . ASN A 1 71 ? 4.826 31.394 -8.070 1.00 35.39 ? 71 ASN A ND2 1 ATOM 543 N N . ALA A 1 72 ? 8.891 34.394 -8.098 1.00 32.23 ? 72 ALA A N 1 ATOM 544 C CA . ALA A 1 72 ? 9.219 35.786 -7.827 1.00 33.05 ? 72 ALA A CA 1 ATOM 545 C C . ALA A 1 72 ? 8.006 36.657 -7.529 1.00 33.34 ? 72 ALA A C 1 ATOM 546 O O . ALA A 1 72 ? 8.136 37.754 -6.993 1.00 34.00 ? 72 ALA A O 1 ATOM 547 C CB . ALA A 1 72 ? 10.034 36.372 -8.983 1.00 33.50 ? 72 ALA A CB 1 ATOM 548 N N . THR A 1 73 ? 6.823 36.185 -7.869 1.00 33.34 ? 73 THR A N 1 ATOM 549 C CA . THR A 1 73 ? 5.663 36.968 -7.543 1.00 34.05 ? 73 THR A CA 1 ATOM 550 C C . THR A 1 73 ? 5.435 36.783 -6.051 1.00 34.04 ? 73 THR A C 1 ATOM 551 O O . THR A 1 73 ? 5.061 37.721 -5.348 1.00 33.99 ? 73 THR A O 1 ATOM 552 C CB . THR A 1 73 ? 4.466 36.513 -8.376 1.00 34.42 ? 73 THR A CB 1 ATOM 553 O OG1 . THR A 1 73 ? 4.731 36.801 -9.754 1.00 34.71 ? 73 THR A OG1 1 ATOM 554 C CG2 . THR A 1 73 ? 3.244 37.365 -8.075 1.00 34.69 ? 73 THR A CG2 1 ATOM 555 N N . ARG A 1 74 ? 5.673 35.561 -5.582 1.00 33.60 ? 74 ARG A N 1 ATOM 556 C CA . ARG A 1 74 ? 5.488 35.218 -4.178 1.00 33.87 ? 74 ARG A CA 1 ATOM 557 C C . ARG A 1 74 ? 6.639 35.737 -3.333 1.00 33.77 ? 74 ARG A C 1 ATOM 558 O O . ARG A 1 74 ? 6.452 36.108 -2.172 1.00 34.15 ? 74 ARG A O 1 ATOM 559 C CB . ARG A 1 74 ? 5.361 33.703 -4.013 1.00 33.59 ? 74 ARG A CB 1 ATOM 560 C CG . ARG A 1 74 ? 4.030 33.151 -4.493 1.00 34.38 ? 74 ARG A CG 1 ATOM 561 C CD . ARG A 1 74 ? 3.884 31.644 -4.367 1.00 35.30 ? 74 ARG A CD 1 ATOM 562 N NE . ARG A 1 74 ? 2.575 31.205 -4.830 1.00 36.54 ? 74 ARG A NE 1 ATOM 563 C CZ . ARG A 1 74 ? 1.942 30.126 -4.390 1.00 37.04 ? 74 ARG A CZ 1 ATOM 564 N NH1 . ARG A 1 74 ? 2.493 29.356 -3.464 1.00 35.42 ? 74 ARG A NH1 1 ATOM 565 N NH2 . ARG A 1 74 ? 0.749 29.816 -4.880 1.00 37.97 ? 74 ARG A NH2 1 ATOM 566 N N . PHE A 1 75 ? 7.828 35.760 -3.929 1.00 33.43 ? 75 PHE A N 1 ATOM 567 C CA . PHE A 1 75 ? 9.042 36.185 -3.249 1.00 33.42 ? 75 PHE A CA 1 ATOM 568 C C . PHE A 1 75 ? 9.833 37.183 -4.096 1.00 33.73 ? 75 PHE A C 1 ATOM 569 O O . PHE A 1 75 ? 10.816 36.831 -4.748 1.00 33.45 ? 75 PHE A O 1 ATOM 570 C CB . PHE A 1 75 ? 9.898 34.958 -2.889 1.00 33.35 ? 75 PHE A CB 1 ATOM 571 C CG . PHE A 1 75 ? 9.194 33.986 -1.976 1.00 32.15 ? 75 PHE A CG 1 ATOM 572 C CD1 . PHE A 1 75 ? 9.258 34.139 -0.603 1.00 30.47 ? 75 PHE A CD1 1 ATOM 573 C CD2 . PHE A 1 75 ? 8.471 32.925 -2.495 1.00 30.85 ? 75 PHE A CD2 1 ATOM 574 C CE1 . PHE A 1 75 ? 8.606 33.244 0.233 1.00 30.72 ? 75 PHE A CE1 1 ATOM 575 C CE2 . PHE A 1 75 ? 7.821 32.031 -1.666 1.00 30.01 ? 75 PHE A CE2 1 ATOM 576 C CZ . PHE A 1 75 ? 7.891 32.192 -0.303 1.00 30.20 ? 75 PHE A CZ 1 ATOM 577 N N . PRO A 1 76 ? 9.391 38.436 -4.073 1.00 34.44 ? 76 PRO A N 1 ATOM 578 C CA . PRO A 1 76 ? 9.957 39.498 -4.919 1.00 34.64 ? 76 PRO A CA 1 ATOM 579 C C . PRO A 1 76 ? 11.401 39.828 -4.611 1.00 34.93 ? 76 PRO A C 1 ATOM 580 O O . PRO A 1 76 ? 12.040 40.541 -5.385 1.00 35.21 ? 76 PRO A O 1 ATOM 581 C CB . PRO A 1 76 ? 9.079 40.708 -4.576 1.00 34.96 ? 76 PRO A CB 1 ATOM 582 C CG . PRO A 1 76 ? 7.843 40.111 -4.030 1.00 34.60 ? 76 PRO A CG 1 ATOM 583 C CD . PRO A 1 76 ? 8.298 38.937 -3.223 1.00 33.96 ? 76 PRO A CD 1 ATOM 584 N N . ASP A 1 77 ? 11.923 39.326 -3.503 1.00 34.65 ? 77 ASP A N 1 ATOM 585 C CA . ASP A 1 77 ? 13.324 39.561 -3.200 1.00 34.61 ? 77 ASP A CA 1 ATOM 586 C C . ASP A 1 77 ? 14.085 38.243 -3.179 1.00 33.70 ? 77 ASP A C 1 ATOM 587 O O . ASP A 1 77 ? 15.260 38.189 -2.824 1.00 33.31 ? 77 ASP A O 1 ATOM 588 C CB . ASP A 1 77 ? 13.485 40.364 -1.905 1.00 35.33 ? 77 ASP A CB 1 ATOM 589 C CG . ASP A 1 77 ? 13.128 41.839 -2.097 1.00 37.72 ? 77 ASP A CG 1 ATOM 590 O OD1 . ASP A 1 77 ? 13.651 42.449 -3.063 1.00 37.80 ? 77 ASP A OD1 1 ATOM 591 O OD2 . ASP A 1 77 ? 12.340 42.461 -1.342 1.00 39.65 ? 77 ASP A OD2 1 ATOM 592 N N . GLY A 1 78 ? 13.389 37.181 -3.571 1.00 32.92 ? 78 GLY A N 1 ATOM 593 C CA . GLY A 1 78 ? 13.979 35.861 -3.624 1.00 31.78 ? 78 GLY A CA 1 ATOM 594 C C . GLY A 1 78 ? 14.097 35.241 -2.241 1.00 31.01 ? 78 GLY A C 1 ATOM 595 O O . GLY A 1 78 ? 13.825 35.890 -1.222 1.00 31.10 ? 78 GLY A O 1 ATOM 596 N N . ILE A 1 79 ? 14.503 33.979 -2.211 1.00 30.23 ? 79 ILE A N 1 ATOM 597 C CA . ILE A 1 79 ? 14.801 33.308 -0.961 1.00 29.27 ? 79 ILE A CA 1 ATOM 598 C C . ILE A 1 79 ? 15.969 33.995 -0.253 1.00 29.31 ? 79 ILE A C 1 ATOM 599 O O . ILE A 1 79 ? 15.925 34.201 0.962 1.00 29.07 ? 79 ILE A O 1 ATOM 600 C CB . ILE A 1 79 ? 15.122 31.823 -1.205 1.00 29.09 ? 79 ILE A CB 1 ATOM 601 C CG1 . ILE A 1 79 ? 13.982 31.155 -1.967 1.00 28.02 ? 79 ILE A CG1 1 ATOM 602 C CG2 . ILE A 1 79 ? 15.396 31.108 0.125 1.00 28.34 ? 79 ILE A CG2 1 ATOM 603 C CD1 . ILE A 1 79 ? 12.613 31.393 -1.375 1.00 28.23 ? 79 ILE A CD1 1 ATOM 604 N N . ASP A 1 80 ? 17.007 34.349 -1.009 1.00 28.82 ? 80 ASP A N 1 ATOM 605 C CA . ASP A 1 80 ? 18.156 35.060 -0.449 1.00 28.61 ? 80 ASP A CA 1 ATOM 606 C C . ASP A 1 80 ? 17.771 36.358 0.250 1.00 28.32 ? 80 ASP A C 1 ATOM 607 O O . ASP A 1 80 ? 18.336 36.706 1.290 1.00 27.76 ? 80 ASP A O 1 ATOM 608 C CB . ASP A 1 80 ? 19.242 35.311 -1.506 1.00 29.23 ? 80 ASP A CB 1 ATOM 609 C CG . ASP A 1 80 ? 18.799 36.271 -2.607 1.00 30.92 ? 80 ASP A CG 1 ATOM 610 O OD1 . ASP A 1 80 ? 17.582 36.400 -2.872 1.00 32.34 ? 80 ASP A OD1 1 ATOM 611 O OD2 . ASP A 1 80 ? 19.610 36.947 -3.268 1.00 33.45 ? 80 ASP A OD2 1 ATOM 612 N N . GLY A 1 81 ? 16.814 37.068 -0.323 1.00 28.12 ? 81 GLY A N 1 ATOM 613 C CA . GLY A 1 81 ? 16.349 38.320 0.239 1.00 28.88 ? 81 GLY A CA 1 ATOM 614 C C . GLY A 1 81 ? 15.509 38.109 1.478 1.00 28.66 ? 81 GLY A C 1 ATOM 615 O O . GLY A 1 81 ? 15.668 38.819 2.472 1.00 29.23 ? 81 GLY A O 1 ATOM 616 N N . LEU A 1 82 ? 14.611 37.131 1.418 1.00 28.72 ? 82 LEU A N 1 ATOM 617 C CA . LEU A 1 82 ? 13.864 36.735 2.606 1.00 28.03 ? 82 LEU A CA 1 ATOM 618 C C . LEU A 1 82 ? 14.854 36.309 3.674 1.00 28.02 ? 82 LEU A C 1 ATOM 619 O O . LEU A 1 82 ? 14.719 36.709 4.832 1.00 28.20 ? 82 LEU A O 1 ATOM 620 C CB . LEU A 1 82 ? 12.879 35.597 2.310 1.00 28.09 ? 82 LEU A CB 1 ATOM 621 C CG . LEU A 1 82 ? 12.055 35.109 3.517 1.00 27.83 ? 82 LEU A CG 1 ATOM 622 C CD1 . LEU A 1 82 ? 11.266 36.251 4.154 1.00 28.57 ? 82 LEU A CD1 1 ATOM 623 C CD2 . LEU A 1 82 ? 11.123 34.002 3.082 1.00 27.78 ? 82 LEU A CD2 1 ATOM 624 N N . ALA A 1 83 ? 15.853 35.502 3.300 1.00 27.77 ? 83 ALA A N 1 ATOM 625 C CA . ALA A 1 83 ? 16.833 35.020 4.269 1.00 27.69 ? 83 ALA A CA 1 ATOM 626 C C . ALA A 1 83 ? 17.490 36.177 5.010 1.00 28.04 ? 83 ALA A C 1 ATOM 627 O O . ALA A 1 83 ? 17.701 36.111 6.223 1.00 27.31 ? 83 ALA A O 1 ATOM 628 C CB . ALA A 1 83 ? 17.885 34.148 3.598 1.00 27.72 ? 83 ALA A CB 1 ATOM 629 N N . LYS A 1 84 ? 17.807 37.237 4.274 1.00 28.16 ? 84 LYS A N 1 ATOM 630 C CA . LYS A 1 84 ? 18.497 38.376 4.858 1.00 29.08 ? 84 LYS A CA 1 ATOM 631 C C . LYS A 1 84 ? 17.579 39.080 5.829 1.00 28.60 ? 84 LYS A C 1 ATOM 632 O O . LYS A 1 84 ? 18.001 39.488 6.893 1.00 28.19 ? 84 LYS A O 1 ATOM 633 C CB . LYS A 1 84 ? 19.002 39.360 3.800 1.00 29.51 ? 84 LYS A CB 1 ATOM 634 C CG . LYS A 1 84 ? 20.010 40.355 4.366 1.00 32.78 ? 84 LYS A CG 1 ATOM 635 C CD . LYS A 1 84 ? 20.805 41.054 3.258 1.00 38.36 ? 84 LYS A CD 1 ATOM 636 C CE . LYS A 1 84 ? 22.323 40.981 3.508 1.00 40.46 ? 84 LYS A CE 1 ATOM 637 N NZ . LYS A 1 84 ? 22.691 40.814 4.957 1.00 43.05 ? 84 LYS A NZ 1 ATOM 638 N N . LYS A 1 85 ? 16.319 39.216 5.455 1.00 28.82 ? 85 LYS A N 1 ATOM 639 C CA . LYS A 1 85 ? 15.360 39.883 6.320 1.00 29.42 ? 85 LYS A CA 1 ATOM 640 C C . LYS A 1 85 ? 15.138 39.055 7.583 1.00 29.28 ? 85 LYS A C 1 ATOM 641 O O . LYS A 1 85 ? 15.024 39.589 8.671 1.00 29.67 ? 85 LYS A O 1 ATOM 642 C CB . LYS A 1 85 ? 14.046 40.106 5.572 1.00 29.18 ? 85 LYS A CB 1 ATOM 643 C CG . LYS A 1 85 ? 14.195 41.060 4.405 1.00 30.12 ? 85 LYS A CG 1 ATOM 644 C CD . LYS A 1 85 ? 12.866 41.322 3.741 1.00 31.66 ? 85 LYS A CD 1 ATOM 645 C CE . LYS A 1 85 ? 13.073 42.040 2.415 1.00 33.14 ? 85 LYS A CE 1 ATOM 646 N NZ . LYS A 1 85 ? 11.891 41.865 1.537 1.00 32.44 ? 85 LYS A NZ 1 ATOM 647 N N . VAL A 1 86 ? 15.084 37.742 7.420 1.00 29.12 ? 86 VAL A N 1 ATOM 648 C CA . VAL A 1 86 ? 14.834 36.850 8.541 1.00 29.29 ? 86 VAL A CA 1 ATOM 649 C C . VAL A 1 86 ? 16.058 36.755 9.455 1.00 29.25 ? 86 VAL A C 1 ATOM 650 O O . VAL A 1 86 ? 15.946 36.781 10.684 1.00 29.15 ? 86 VAL A O 1 ATOM 651 C CB . VAL A 1 86 ? 14.328 35.498 8.029 1.00 29.17 ? 86 VAL A CB 1 ATOM 652 C CG1 . VAL A 1 86 ? 14.444 34.426 9.080 1.00 30.11 ? 86 VAL A CG1 1 ATOM 653 C CG2 . VAL A 1 86 ? 12.875 35.655 7.569 1.00 28.95 ? 86 VAL A CG2 1 ATOM 654 N N . HIS A 1 87 ? 17.231 36.652 8.852 1.00 29.41 ? 87 HIS A N 1 ATOM 655 C CA . HIS A 1 87 ? 18.461 36.613 9.629 1.00 29.47 ? 87 HIS A CA 1 ATOM 656 C C . HIS A 1 87 ? 18.646 37.896 10.438 1.00 29.77 ? 87 HIS A C 1 ATOM 657 O O . HIS A 1 87 ? 19.203 37.861 11.528 1.00 29.48 ? 87 HIS A O 1 ATOM 658 C CB . HIS A 1 87 ? 19.676 36.404 8.727 1.00 29.30 ? 87 HIS A CB 1 ATOM 659 C CG . HIS A 1 87 ? 19.772 35.029 8.148 1.00 29.45 ? 87 HIS A CG 1 ATOM 660 N ND1 . HIS A 1 87 ? 19.146 33.939 8.709 1.00 29.02 ? 87 HIS A ND1 1 ATOM 661 C CD2 . HIS A 1 87 ? 20.425 34.569 7.058 1.00 29.04 ? 87 HIS A CD2 1 ATOM 662 C CE1 . HIS A 1 87 ? 19.409 32.866 7.987 1.00 28.50 ? 87 HIS A CE1 1 ATOM 663 N NE2 . HIS A 1 87 ? 20.184 33.222 6.980 1.00 30.76 ? 87 HIS A NE2 1 ATOM 664 N N . ALA A 1 88 ? 18.175 39.021 9.902 1.00 30.16 ? 88 ALA A N 1 ATOM 665 C CA . ALA A 1 88 ? 18.362 40.317 10.554 1.00 31.25 ? 88 ALA A CA 1 ATOM 666 C C . ALA A 1 88 ? 17.541 40.364 11.814 1.00 31.63 ? 88 ALA A C 1 ATOM 667 O O . ALA A 1 88 ? 17.920 41.012 12.790 1.00 32.30 ? 88 ALA A O 1 ATOM 668 C CB . ALA A 1 88 ? 17.952 41.457 9.623 1.00 31.54 ? 88 ALA A CB 1 ATOM 669 N N . LEU A 1 89 ? 16.410 39.669 11.775 1.00 31.70 ? 89 LEU A N 1 ATOM 670 C CA . LEU A 1 89 ? 15.522 39.556 12.924 1.00 31.89 ? 89 LEU A CA 1 ATOM 671 C C . LEU A 1 89 ? 16.049 38.584 13.990 1.00 31.22 ? 89 LEU A C 1 ATOM 672 O O . LEU A 1 89 ? 15.439 38.434 15.039 1.00 31.88 ? 89 LEU A O 1 ATOM 673 C CB . LEU A 1 89 ? 14.115 39.144 12.460 1.00 32.21 ? 89 LEU A CB 1 ATOM 674 C CG . LEU A 1 89 ? 13.293 40.199 11.718 1.00 33.51 ? 89 LEU A CG 1 ATOM 675 C CD1 . LEU A 1 89 ? 12.019 39.619 11.091 1.00 34.81 ? 89 LEU A CD1 1 ATOM 676 C CD2 . LEU A 1 89 ? 12.956 41.354 12.638 1.00 35.17 ? 89 LEU A CD2 1 ATOM 677 N N . GLY A 1 90 ? 17.181 37.926 13.723 1.00 30.48 ? 90 GLY A N 1 ATOM 678 C CA . GLY A 1 90 ? 17.749 36.964 14.657 1.00 28.76 ? 90 GLY A CA 1 ATOM 679 C C . GLY A 1 90 ? 17.122 35.586 14.515 1.00 28.07 ? 90 GLY A C 1 ATOM 680 O O . GLY A 1 90 ? 17.203 34.748 15.405 1.00 27.82 ? 90 GLY A O 1 ATOM 681 N N . LEU A 1 91 ? 16.487 35.356 13.374 1.00 27.39 ? 91 LEU A N 1 ATOM 682 C CA . LEU A 1 91 ? 15.865 34.078 13.080 1.00 26.21 ? 91 LEU A CA 1 ATOM 683 C C . LEU A 1 91 ? 16.636 33.287 12.016 1.00 25.57 ? 91 LEU A C 1 ATOM 684 O O . LEU A 1 91 ? 17.566 33.796 11.392 1.00 24.96 ? 91 LEU A O 1 ATOM 685 C CB . LEU A 1 91 ? 14.435 34.310 12.600 1.00 26.60 ? 91 LEU A CB 1 ATOM 686 C CG . LEU A 1 91 ? 13.565 35.158 13.524 1.00 26.47 ? 91 LEU A CG 1 ATOM 687 C CD1 . LEU A 1 91 ? 12.322 35.628 12.788 1.00 25.26 ? 91 LEU A CD1 1 ATOM 688 C CD2 . LEU A 1 91 ? 13.213 34.378 14.770 1.00 27.27 ? 91 LEU A CD2 1 ATOM 689 N N . LYS A 1 92 ? 16.225 32.038 11.829 1.00 24.43 ? 92 LYS A N 1 ATOM 690 C CA . LYS A 1 92 ? 16.783 31.168 10.820 1.00 23.52 ? 92 LYS A CA 1 ATOM 691 C C . LYS A 1 92 ? 15.710 30.840 9.777 1.00 23.32 ? 92 LYS A C 1 ATOM 692 O O . LYS A 1 92 ? 14.527 30.847 10.073 1.00 22.53 ? 92 LYS A O 1 ATOM 693 C CB . LYS A 1 92 ? 17.373 29.911 11.450 1.00 23.62 ? 92 LYS A CB 1 ATOM 694 C CG . LYS A 1 92 ? 18.643 30.194 12.249 1.00 25.27 ? 92 LYS A CG 1 ATOM 695 C CD . LYS A 1 92 ? 19.272 28.900 12.740 1.00 29.67 ? 92 LYS A CD 1 ATOM 696 C CE . LYS A 1 92 ? 20.429 29.162 13.688 1.00 32.70 ? 92 LYS A CE 1 ATOM 697 N NZ . LYS A 1 92 ? 21.473 30.041 13.083 1.00 34.14 ? 92 LYS A NZ 1 ATOM 698 N N . LEU A 1 93 ? 16.124 30.553 8.550 1.00 22.44 ? 93 LEU A N 1 ATOM 699 C CA . LEU A 1 93 ? 15.148 30.344 7.491 1.00 22.15 ? 93 LEU A CA 1 ATOM 700 C C . LEU A 1 93 ? 15.226 28.915 7.028 1.00 21.32 ? 93 LEU A C 1 ATOM 701 O O . LEU A 1 93 ? 16.296 28.406 6.774 1.00 21.78 ? 93 LEU A O 1 ATOM 702 C CB . LEU A 1 93 ? 15.414 31.294 6.320 1.00 22.44 ? 93 LEU A CB 1 ATOM 703 C CG . LEU A 1 93 ? 14.504 31.099 5.115 1.00 23.87 ? 93 LEU A CG 1 ATOM 704 C CD1 . LEU A 1 93 ? 13.149 31.638 5.459 1.00 25.15 ? 93 LEU A CD1 1 ATOM 705 C CD2 . LEU A 1 93 ? 15.066 31.812 3.895 1.00 25.49 ? 93 LEU A CD2 1 ATOM 706 N N . GLY A 1 94 ? 14.077 28.271 6.925 1.00 20.59 ? 94 GLY A N 1 ATOM 707 C CA . GLY A 1 94 ? 14.020 26.914 6.449 1.00 19.31 ? 94 GLY A CA 1 ATOM 708 C C . GLY A 1 94 ? 13.368 26.909 5.090 1.00 18.94 ? 94 GLY A C 1 ATOM 709 O O . GLY A 1 94 ? 12.544 27.778 4.765 1.00 19.18 ? 94 GLY A O 1 ATOM 710 N N . ILE A 1 95 ? 13.732 25.932 4.275 1.00 17.46 ? 95 ILE A N 1 ATOM 711 C CA . ILE A 1 95 ? 13.087 25.814 2.999 1.00 16.93 ? 95 ILE A CA 1 ATOM 712 C C . ILE A 1 95 ? 12.701 24.364 2.838 1.00 15.80 ? 95 ILE A C 1 ATOM 713 O O . ILE A 1 95 ? 12.931 23.566 3.721 1.00 15.34 ? 95 ILE A O 1 ATOM 714 C CB . ILE A 1 95 ? 14.001 26.330 1.856 1.00 17.49 ? 95 ILE A CB 1 ATOM 715 C CG1 . ILE A 1 95 ? 13.117 26.759 0.679 1.00 18.91 ? 95 ILE A CG1 1 ATOM 716 C CG2 . ILE A 1 95 ? 14.992 25.277 1.443 1.00 15.74 ? 95 ILE A CG2 1 ATOM 717 C CD1 . ILE A 1 95 ? 13.657 27.903 -0.100 1.00 22.31 ? 95 ILE A CD1 1 ATOM 718 N N . TYR A 1 96 ? 12.118 24.026 1.704 1.00 15.83 ? 96 TYR A N 1 ATOM 719 C CA . TYR A 1 96 ? 11.535 22.716 1.534 1.00 15.32 ? 96 TYR A CA 1 ATOM 720 C C . TYR A 1 96 ? 11.861 22.198 0.162 1.00 14.91 ? 96 TYR A C 1 ATOM 721 O O . TYR A 1 96 ? 11.806 22.941 -0.807 1.00 15.11 ? 96 TYR A O 1 ATOM 722 C CB . TYR A 1 96 ? 10.004 22.856 1.675 1.00 14.29 ? 96 TYR A CB 1 ATOM 723 C CG . TYR A 1 96 ? 9.194 21.681 1.192 1.00 15.42 ? 96 TYR A CG 1 ATOM 724 C CD1 . TYR A 1 96 ? 8.891 21.520 -0.163 1.00 15.95 ? 96 TYR A CD1 1 ATOM 725 C CD2 . TYR A 1 96 ? 8.726 20.731 2.088 1.00 14.64 ? 96 TYR A CD2 1 ATOM 726 C CE1 . TYR A 1 96 ? 8.150 20.444 -0.603 1.00 15.05 ? 96 TYR A CE1 1 ATOM 727 C CE2 . TYR A 1 96 ? 7.986 19.657 1.658 1.00 15.35 ? 96 TYR A CE2 1 ATOM 728 C CZ . TYR A 1 96 ? 7.700 19.522 0.311 1.00 16.41 ? 96 TYR A CZ 1 ATOM 729 O OH . TYR A 1 96 ? 6.969 18.465 -0.128 1.00 17.99 ? 96 TYR A OH 1 ATOM 730 N N . SER A 1 97 ? 12.199 20.924 0.085 1.00 14.20 ? 97 SER A N 1 ATOM 731 C CA . SER A 1 97 ? 12.293 20.253 -1.190 1.00 14.10 ? 97 SER A CA 1 ATOM 732 C C . SER A 1 97 ? 11.852 18.835 -0.956 1.00 14.71 ? 97 SER A C 1 ATOM 733 O O . SER A 1 97 ? 11.344 18.517 0.125 1.00 15.47 ? 97 SER A O 1 ATOM 734 C CB . SER A 1 97 ? 13.698 20.296 -1.777 1.00 14.23 ? 97 SER A CB 1 ATOM 735 O OG . SER A 1 97 ? 13.581 20.160 -3.177 1.00 11.62 ? 97 SER A OG 1 ATOM 736 N N . THR A 1 98 ? 12.048 17.998 -1.961 1.00 14.61 ? 98 THR A N 1 ATOM 737 C CA . THR A 1 98 ? 11.577 16.622 -1.982 1.00 14.70 ? 98 THR A CA 1 ATOM 738 C C . THR A 1 98 ? 12.630 15.760 -2.645 1.00 15.42 ? 98 THR A C 1 ATOM 739 O O . THR A 1 98 ? 13.240 16.176 -3.641 1.00 15.61 ? 98 THR A O 1 ATOM 740 C CB . THR A 1 98 ? 10.274 16.581 -2.777 1.00 15.47 ? 98 THR A CB 1 ATOM 741 O OG1 . THR A 1 98 ? 9.331 17.428 -2.113 1.00 16.33 ? 98 THR A OG1 1 ATOM 742 C CG2 . THR A 1 98 ? 9.606 15.184 -2.725 1.00 14.47 ? 98 THR A CG2 1 ATOM 743 N N . ALA A 1 99 ? 12.839 14.571 -2.079 1.00 15.70 ? 99 ALA A N 1 ATOM 744 C CA . ALA A 1 99 ? 13.716 13.546 -2.626 1.00 16.02 ? 99 ALA A CA 1 ATOM 745 C C . ALA A 1 99 ? 12.958 12.770 -3.677 1.00 16.49 ? 99 ALA A C 1 ATOM 746 O O . ALA A 1 99 ? 12.818 11.563 -3.578 1.00 17.58 ? 99 ALA A O 1 ATOM 747 C CB . ALA A 1 99 ? 14.136 12.605 -1.529 1.00 15.46 ? 99 ALA A CB 1 ATOM 748 N N . GLY A 1 100 ? 12.465 13.465 -4.688 1.00 17.39 ? 100 GLY A N 1 ATOM 749 C CA . GLY A 1 100 ? 11.622 12.854 -5.685 1.00 17.41 ? 100 GLY A CA 1 ATOM 750 C C . GLY A 1 100 ? 11.665 13.758 -6.890 1.00 18.68 ? 100 GLY A C 1 ATOM 751 O O . GLY A 1 100 ? 12.425 14.701 -6.915 1.00 18.74 ? 100 GLY A O 1 ATOM 752 N N . THR A 1 101 ? 10.856 13.492 -7.904 1.00 19.20 ? 101 THR A N 1 ATOM 753 C CA . THR A 1 101 ? 10.969 14.310 -9.088 1.00 20.59 ? 101 THR A CA 1 ATOM 754 C C . THR A 1 101 ? 10.129 15.586 -9.028 1.00 20.54 ? 101 THR A C 1 ATOM 755 O O . THR A 1 101 ? 10.293 16.477 -9.849 1.00 20.11 ? 101 THR A O 1 ATOM 756 C CB . THR A 1 101 ? 10.611 13.487 -10.317 1.00 21.16 ? 101 THR A CB 1 ATOM 757 O OG1 . THR A 1 101 ? 9.385 12.798 -10.077 1.00 21.57 ? 101 THR A OG1 1 ATOM 758 C CG2 . THR A 1 101 ? 11.603 12.365 -10.456 1.00 23.06 ? 101 THR A CG2 1 ATOM 759 N N . ALA A 1 102 ? 9.231 15.668 -8.058 1.00 19.74 ? 102 ALA A N 1 ATOM 760 C CA . ALA A 1 102 ? 8.485 16.900 -7.844 1.00 19.79 ? 102 ALA A CA 1 ATOM 761 C C . ALA A 1 102 ? 8.104 16.935 -6.381 1.00 19.05 ? 102 ALA A C 1 ATOM 762 O O . ALA A 1 102 ? 8.030 15.882 -5.738 1.00 19.32 ? 102 ALA A O 1 ATOM 763 C CB . ALA A 1 102 ? 7.236 16.947 -8.721 1.00 19.60 ? 102 ALA A CB 1 ATOM 764 N N . THR A 1 103 ? 7.861 18.121 -5.838 1.00 18.51 ? 103 THR A N 1 ATOM 765 C CA . THR A 1 103 ? 7.411 18.151 -4.449 1.00 18.11 ? 103 THR A CA 1 ATOM 766 C C . THR A 1 103 ? 6.034 17.514 -4.345 1.00 18.58 ? 103 THR A C 1 ATOM 767 O O . THR A 1 103 ? 5.400 17.167 -5.348 1.00 17.89 ? 103 THR A O 1 ATOM 768 C CB . THR A 1 103 ? 7.350 19.560 -3.874 1.00 18.59 ? 103 THR A CB 1 ATOM 769 O OG1 . THR A 1 103 ? 6.377 20.336 -4.595 1.00 16.77 ? 103 THR A OG1 1 ATOM 770 C CG2 . THR A 1 103 ? 8.688 20.263 -4.057 1.00 18.36 ? 103 THR A CG2 1 ATOM 771 N N . CYS A 1 104 ? 5.576 17.362 -3.115 1.00 17.93 ? 104 CYS A N 1 ATOM 772 C CA . CYS A 1 104 ? 4.285 16.782 -2.878 1.00 18.48 ? 104 CYS A CA 1 ATOM 773 C C . CYS A 1 104 ? 3.203 17.637 -3.497 1.00 18.34 ? 104 CYS A C 1 ATOM 774 O O . CYS A 1 104 ? 2.205 17.108 -3.914 1.00 18.19 ? 104 CYS A O 1 ATOM 775 C CB . CYS A 1 104 ? 4.047 16.617 -1.385 1.00 18.14 ? 104 CYS A CB 1 ATOM 776 S SG . CYS A 1 104 ? 5.048 15.296 -0.728 1.00 19.43 ? 104 CYS A SG 1 ATOM 777 N N . ALA A 1 105 ? 3.396 18.950 -3.557 1.00 18.83 ? 105 ALA A N 1 ATOM 778 C CA . ALA A 1 105 ? 2.416 19.800 -4.233 1.00 19.68 ? 105 ALA A CA 1 ATOM 779 C C . ALA A 1 105 ? 2.690 19.931 -5.723 1.00 20.44 ? 105 ALA A C 1 ATOM 780 O O . ALA A 1 105 ? 1.999 20.670 -6.409 1.00 20.90 ? 105 ALA A O 1 ATOM 781 C CB . ALA A 1 105 ? 2.328 21.161 -3.599 1.00 19.57 ? 105 ALA A CB 1 ATOM 782 N N . GLY A 1 106 ? 3.695 19.219 -6.226 1.00 20.57 ? 106 GLY A N 1 ATOM 783 C CA . GLY A 1 106 ? 3.951 19.215 -7.647 1.00 20.84 ? 106 GLY A CA 1 ATOM 784 C C . GLY A 1 106 ? 4.943 20.244 -8.159 1.00 21.40 ? 106 GLY A C 1 ATOM 785 O O . GLY A 1 106 ? 4.900 20.600 -9.341 1.00 20.75 ? 106 GLY A O 1 ATOM 786 N N . TYR A 1 107 ? 5.834 20.721 -7.288 1.00 20.54 ? 107 TYR A N 1 ATOM 787 C CA . TYR A 1 107 ? 6.815 21.720 -7.699 1.00 21.12 ? 107 TYR A CA 1 ATOM 788 C C . TYR A 1 107 ? 8.130 21.023 -8.024 1.00 20.77 ? 107 TYR A C 1 ATOM 789 O O . TYR A 1 107 ? 8.281 19.848 -7.748 1.00 21.07 ? 107 TYR A O 1 ATOM 790 C CB . TYR A 1 107 ? 7.002 22.788 -6.613 1.00 20.82 ? 107 TYR A CB 1 ATOM 791 C CG . TYR A 1 107 ? 5.797 23.684 -6.504 1.00 22.27 ? 107 TYR A CG 1 ATOM 792 C CD1 . TYR A 1 107 ? 4.566 23.166 -6.083 1.00 22.15 ? 107 TYR A CD1 1 ATOM 793 C CD2 . TYR A 1 107 ? 5.870 25.029 -6.820 1.00 21.13 ? 107 TYR A CD2 1 ATOM 794 C CE1 . TYR A 1 107 ? 3.445 23.966 -5.978 1.00 24.96 ? 107 TYR A CE1 1 ATOM 795 C CE2 . TYR A 1 107 ? 4.738 25.843 -6.716 1.00 23.49 ? 107 TYR A CE2 1 ATOM 796 C CZ . TYR A 1 107 ? 3.532 25.300 -6.293 1.00 24.23 ? 107 TYR A CZ 1 ATOM 797 O OH . TYR A 1 107 ? 2.399 26.070 -6.176 1.00 23.81 ? 107 TYR A OH 1 ATOM 798 N N . PRO A 1 108 ? 9.072 21.743 -8.615 1.00 21.21 ? 108 PRO A N 1 ATOM 799 C CA . PRO A 1 108 ? 10.390 21.179 -8.912 1.00 21.35 ? 108 PRO A CA 1 ATOM 800 C C . PRO A 1 108 ? 11.031 20.668 -7.613 1.00 20.79 ? 108 PRO A C 1 ATOM 801 O O . PRO A 1 108 ? 10.955 21.316 -6.565 1.00 21.10 ? 108 PRO A O 1 ATOM 802 C CB . PRO A 1 108 ? 11.135 22.362 -9.522 1.00 21.65 ? 108 PRO A CB 1 ATOM 803 C CG . PRO A 1 108 ? 10.066 23.182 -10.090 1.00 22.70 ? 108 PRO A CG 1 ATOM 804 C CD . PRO A 1 108 ? 8.962 23.141 -9.057 1.00 21.41 ? 108 PRO A CD 1 ATOM 805 N N . ALA A 1 109 ? 11.651 19.500 -7.703 1.00 19.70 ? 109 ALA A N 1 ATOM 806 C CA . ALA A 1 109 ? 12.252 18.851 -6.555 1.00 18.95 ? 109 ALA A CA 1 ATOM 807 C C . ALA A 1 109 ? 13.670 18.397 -6.851 1.00 18.17 ? 109 ALA A C 1 ATOM 808 O O . ALA A 1 109 ? 14.175 18.585 -7.942 1.00 17.90 ? 109 ALA A O 1 ATOM 809 C CB . ALA A 1 109 ? 11.391 17.690 -6.058 1.00 18.06 ? 109 ALA A CB 1 ATOM 810 N N . SER A 1 110 ? 14.300 17.787 -5.856 1.00 17.98 ? 110 SER A N 1 ATOM 811 C CA . SER A 1 110 ? 15.749 17.697 -5.834 1.00 17.41 ? 110 SER A CA 1 ATOM 812 C C . SER A 1 110 ? 16.434 16.391 -6.172 1.00 17.68 ? 110 SER A C 1 ATOM 813 O O . SER A 1 110 ? 17.681 16.340 -6.185 1.00 18.80 ? 110 SER A O 1 ATOM 814 C CB . SER A 1 110 ? 16.204 18.095 -4.424 1.00 17.23 ? 110 SER A CB 1 ATOM 815 O OG . SER A 1 110 ? 15.879 19.434 -4.152 1.00 15.75 ? 110 SER A OG 1 ATOM 816 N N . LEU A 1 111 ? 15.663 15.342 -6.440 1.00 16.69 ? 111 LEU A N 1 ATOM 817 C CA . LEU A 1 111 ? 16.272 14.054 -6.676 1.00 16.35 ? 111 LEU A CA 1 ATOM 818 C C . LEU A 1 111 ? 17.115 14.152 -7.931 1.00 16.71 ? 111 LEU A C 1 ATOM 819 O O . LEU A 1 111 ? 16.617 14.550 -8.999 1.00 16.63 ? 111 LEU A O 1 ATOM 820 C CB . LEU A 1 111 ? 15.222 12.935 -6.820 1.00 16.30 ? 111 LEU A CB 1 ATOM 821 C CG . LEU A 1 111 ? 15.847 11.542 -6.999 1.00 16.56 ? 111 LEU A CG 1 ATOM 822 C CD1 . LEU A 1 111 ? 16.576 11.045 -5.737 1.00 15.36 ? 111 LEU A CD1 1 ATOM 823 C CD2 . LEU A 1 111 ? 14.788 10.521 -7.456 1.00 18.06 ? 111 LEU A CD2 1 ATOM 824 N N . GLY A 1 112 ? 18.385 13.791 -7.794 1.00 16.48 ? 112 GLY A N 1 ATOM 825 C CA . GLY A 1 112 ? 19.330 13.850 -8.890 1.00 16.49 ? 112 GLY A CA 1 ATOM 826 C C . GLY A 1 112 ? 19.927 15.223 -9.117 1.00 17.03 ? 112 GLY A C 1 ATOM 827 O O . GLY A 1 112 ? 20.780 15.392 -9.999 1.00 16.92 ? 112 GLY A O 1 ATOM 828 N N . TYR A 1 113 ? 19.486 16.205 -8.332 1.00 16.88 ? 113 TYR A N 1 ATOM 829 C CA . TYR A 1 113 ? 19.983 17.564 -8.451 1.00 17.09 ? 113 TYR A CA 1 ATOM 830 C C . TYR A 1 113 ? 20.451 18.075 -7.101 1.00 17.05 ? 113 TYR A C 1 ATOM 831 O O . TYR A 1 113 ? 20.532 19.286 -6.863 1.00 17.21 ? 113 TYR A O 1 ATOM 832 C CB . TYR A 1 113 ? 18.882 18.472 -8.951 1.00 17.30 ? 113 TYR A CB 1 ATOM 833 C CG . TYR A 1 113 ? 18.650 18.339 -10.420 1.00 19.41 ? 113 TYR A CG 1 ATOM 834 C CD1 . TYR A 1 113 ? 19.286 19.169 -11.316 1.00 18.18 ? 113 TYR A CD1 1 ATOM 835 C CD2 . TYR A 1 113 ? 17.791 17.373 -10.910 1.00 19.21 ? 113 TYR A CD2 1 ATOM 836 C CE1 . TYR A 1 113 ? 19.066 19.040 -12.669 1.00 22.38 ? 113 TYR A CE1 1 ATOM 837 C CE2 . TYR A 1 113 ? 17.565 17.236 -12.263 1.00 23.27 ? 113 TYR A CE2 1 ATOM 838 C CZ . TYR A 1 113 ? 18.202 18.067 -13.129 1.00 23.10 ? 113 TYR A CZ 1 ATOM 839 O OH . TYR A 1 113 ? 17.973 17.924 -14.474 1.00 27.03 ? 113 TYR A OH 1 ATOM 840 N N . GLU A 1 114 ? 20.760 17.149 -6.214 1.00 17.26 ? 114 GLU A N 1 ATOM 841 C CA . GLU A 1 114 ? 21.086 17.532 -4.851 1.00 18.11 ? 114 GLU A CA 1 ATOM 842 C C . GLU A 1 114 ? 22.218 18.537 -4.767 1.00 19.24 ? 114 GLU A C 1 ATOM 843 O O . GLU A 1 114 ? 22.136 19.513 -4.017 1.00 19.18 ? 114 GLU A O 1 ATOM 844 C CB . GLU A 1 114 ? 21.390 16.299 -4.016 1.00 18.76 ? 114 GLU A CB 1 ATOM 845 C CG . GLU A 1 114 ? 20.210 15.341 -3.908 1.00 16.85 ? 114 GLU A CG 1 ATOM 846 C CD . GLU A 1 114 ? 20.109 14.362 -5.068 1.00 18.78 ? 114 GLU A CD 1 ATOM 847 O OE1 . GLU A 1 114 ? 20.866 14.512 -6.058 1.00 19.31 ? 114 GLU A OE1 1 ATOM 848 O OE2 . GLU A 1 114 ? 19.264 13.437 -4.993 1.00 19.55 ? 114 GLU A OE2 1 ATOM 849 N N . ASP A 1 115 ? 23.282 18.314 -5.536 1.00 19.56 ? 115 ASP A N 1 ATOM 850 C CA . ASP A 1 115 ? 24.451 19.174 -5.405 1.00 20.06 ? 115 ASP A CA 1 ATOM 851 C C . ASP A 1 115 ? 24.152 20.594 -5.830 1.00 19.15 ? 115 ASP A C 1 ATOM 852 O O . ASP A 1 115 ? 24.582 21.520 -5.182 1.00 19.31 ? 115 ASP A O 1 ATOM 853 C CB . ASP A 1 115 ? 25.666 18.587 -6.132 1.00 21.25 ? 115 ASP A CB 1 ATOM 854 C CG . ASP A 1 115 ? 26.105 17.281 -5.516 1.00 24.40 ? 115 ASP A CG 1 ATOM 855 O OD1 . ASP A 1 115 ? 26.521 17.265 -4.320 1.00 29.54 ? 115 ASP A OD1 1 ATOM 856 O OD2 . ASP A 1 115 ? 26.064 16.218 -6.148 1.00 28.47 ? 115 ASP A OD2 1 ATOM 857 N N . VAL A 1 116 ? 23.412 20.760 -6.916 1.00 18.39 ? 116 VAL A N 1 ATOM 858 C CA . VAL A 1 116 ? 22.994 22.085 -7.329 1.00 18.73 ? 116 VAL A CA 1 ATOM 859 C C . VAL A 1 116 ? 21.970 22.716 -6.367 1.00 17.61 ? 116 VAL A C 1 ATOM 860 O O . VAL A 1 116 ? 22.041 23.903 -6.063 1.00 17.68 ? 116 VAL A O 1 ATOM 861 C CB . VAL A 1 116 ? 22.428 22.062 -8.764 1.00 18.46 ? 116 VAL A CB 1 ATOM 862 C CG1 . VAL A 1 116 ? 21.790 23.392 -9.104 1.00 20.18 ? 116 VAL A CG1 1 ATOM 863 C CG2 . VAL A 1 116 ? 23.544 21.764 -9.732 1.00 19.67 ? 116 VAL A CG2 1 ATOM 864 N N . ASP A 1 117 ? 21.014 21.933 -5.889 1.00 17.02 ? 117 ASP A N 1 ATOM 865 C CA . ASP A 1 117 ? 20.020 22.489 -4.960 1.00 16.61 ? 117 ASP A CA 1 ATOM 866 C C . ASP A 1 117 ? 20.654 22.863 -3.610 1.00 16.32 ? 117 ASP A C 1 ATOM 867 O O . ASP A 1 117 ? 20.370 23.918 -3.052 1.00 16.80 ? 117 ASP A O 1 ATOM 868 C CB . ASP A 1 117 ? 18.835 21.533 -4.799 1.00 16.43 ? 117 ASP A CB 1 ATOM 869 C CG . ASP A 1 117 ? 18.072 21.364 -6.081 1.00 17.51 ? 117 ASP A CG 1 ATOM 870 O OD1 . ASP A 1 117 ? 17.169 20.492 -6.176 1.00 17.90 ? 117 ASP A OD1 1 ATOM 871 O OD2 . ASP A 1 117 ? 18.323 22.085 -7.068 1.00 19.10 ? 117 ASP A OD2 1 ATOM 872 N N . ALA A 1 118 ? 21.509 21.995 -3.101 1.00 15.68 ? 118 ALA A N 1 ATOM 873 C CA . ALA A 1 118 ? 22.208 22.254 -1.851 1.00 16.30 ? 118 ALA A CA 1 ATOM 874 C C . ALA A 1 118 ? 23.031 23.545 -1.961 1.00 16.46 ? 118 ALA A C 1 ATOM 875 O O . ALA A 1 118 ? 22.989 24.390 -1.082 1.00 17.20 ? 118 ALA A O 1 ATOM 876 C CB . ALA A 1 118 ? 23.105 21.062 -1.462 1.00 15.20 ? 118 ALA A CB 1 ATOM 877 N N . ALA A 1 119 ? 23.783 23.694 -3.042 1.00 16.96 ? 119 ALA A N 1 ATOM 878 C CA . ALA A 1 119 ? 24.512 24.935 -3.257 1.00 17.46 ? 119 ALA A CA 1 ATOM 879 C C . ALA A 1 119 ? 23.589 26.164 -3.310 1.00 17.46 ? 119 ALA A C 1 ATOM 880 O O . ALA A 1 119 ? 23.919 27.201 -2.755 1.00 18.33 ? 119 ALA A O 1 ATOM 881 C CB . ALA A 1 119 ? 25.342 24.850 -4.552 1.00 17.30 ? 119 ALA A CB 1 ATOM 882 N N . ASP A 1 120 ? 22.447 26.062 -3.972 1.00 17.62 ? 120 ASP A N 1 ATOM 883 C CA . ASP A 1 120 ? 21.551 27.213 -4.036 1.00 18.99 ? 120 ASP A CA 1 ATOM 884 C C . ASP A 1 120 ? 21.033 27.535 -2.662 1.00 18.96 ? 120 ASP A C 1 ATOM 885 O O . ASP A 1 120 ? 20.939 28.709 -2.294 1.00 19.26 ? 120 ASP A O 1 ATOM 886 C CB . ASP A 1 120 ? 20.346 26.975 -4.931 1.00 19.07 ? 120 ASP A CB 1 ATOM 887 C CG . ASP A 1 120 ? 20.668 27.165 -6.381 1.00 21.08 ? 120 ASP A CG 1 ATOM 888 O OD1 . ASP A 1 120 ? 21.739 27.730 -6.679 1.00 23.37 ? 120 ASP A OD1 1 ATOM 889 O OD2 . ASP A 1 120 ? 19.913 26.780 -7.281 1.00 20.88 ? 120 ASP A OD2 1 ATOM 890 N N . PHE A 1 121 ? 20.697 26.487 -1.911 1.00 18.82 ? 121 PHE A N 1 ATOM 891 C CA . PHE A 1 121 ? 20.103 26.693 -0.595 1.00 18.61 ? 121 PHE A CA 1 ATOM 892 C C . PHE A 1 121 ? 21.180 27.351 0.266 1.00 19.25 ? 121 PHE A C 1 ATOM 893 O O . PHE A 1 121 ? 20.926 28.338 0.956 1.00 19.83 ? 121 PHE A O 1 ATOM 894 C CB . PHE A 1 121 ? 19.620 25.367 0.007 1.00 18.19 ? 121 PHE A CB 1 ATOM 895 C CG . PHE A 1 121 ? 18.472 24.701 -0.760 1.00 17.83 ? 121 PHE A CG 1 ATOM 896 C CD1 . PHE A 1 121 ? 17.625 25.432 -1.561 1.00 17.68 ? 121 PHE A CD1 1 ATOM 897 C CD2 . PHE A 1 121 ? 18.264 23.327 -0.657 1.00 18.17 ? 121 PHE A CD2 1 ATOM 898 C CE1 . PHE A 1 121 ? 16.589 24.816 -2.248 1.00 19.28 ? 121 PHE A CE1 1 ATOM 899 C CE2 . PHE A 1 121 ? 17.237 22.707 -1.336 1.00 16.35 ? 121 PHE A CE2 1 ATOM 900 C CZ . PHE A 1 121 ? 16.399 23.438 -2.131 1.00 17.83 ? 121 PHE A CZ 1 ATOM 901 N N . ALA A 1 122 ? 22.382 26.806 0.214 1.00 19.88 ? 122 ALA A N 1 ATOM 902 C CA . ALA A 1 122 ? 23.455 27.325 1.055 1.00 21.15 ? 122 ALA A CA 1 ATOM 903 C C . ALA A 1 122 ? 23.733 28.766 0.675 1.00 21.68 ? 122 ALA A C 1 ATOM 904 O O . ALA A 1 122 ? 23.856 29.636 1.539 1.00 21.57 ? 122 ALA A O 1 ATOM 905 C CB . ALA A 1 122 ? 24.682 26.484 0.927 1.00 20.11 ? 122 ALA A CB 1 ATOM 906 N N . ASP A 1 123 ? 23.827 29.012 -0.624 1.00 21.86 ? 123 ASP A N 1 ATOM 907 C CA . ASP A 1 123 ? 24.162 30.340 -1.116 1.00 22.99 ? 123 ASP A CA 1 ATOM 908 C C . ASP A 1 123 ? 23.051 31.350 -0.850 1.00 22.63 ? 123 ASP A C 1 ATOM 909 O O . ASP A 1 123 ? 23.284 32.551 -0.804 1.00 23.51 ? 123 ASP A O 1 ATOM 910 C CB . ASP A 1 123 ? 24.452 30.287 -2.608 1.00 22.94 ? 123 ASP A CB 1 ATOM 911 C CG . ASP A 1 123 ? 25.820 29.712 -2.914 1.00 25.24 ? 123 ASP A CG 1 ATOM 912 O OD1 . ASP A 1 123 ? 26.726 29.818 -2.066 1.00 25.69 ? 123 ASP A OD1 1 ATOM 913 O OD2 . ASP A 1 123 ? 26.068 29.135 -3.995 1.00 30.37 ? 123 ASP A OD2 1 ATOM 914 N N . TRP A 1 124 ? 21.838 30.856 -0.675 1.00 22.19 ? 124 TRP A N 1 ATOM 915 C CA . TRP A 1 124 ? 20.741 31.731 -0.311 1.00 22.22 ? 124 TRP A CA 1 ATOM 916 C C . TRP A 1 124 ? 20.704 32.072 1.169 1.00 21.51 ? 124 TRP A C 1 ATOM 917 O O . TRP A 1 124 ? 19.984 32.987 1.570 1.00 22.84 ? 124 TRP A O 1 ATOM 918 C CB . TRP A 1 124 ? 19.414 31.105 -0.684 1.00 22.28 ? 124 TRP A CB 1 ATOM 919 C CG . TRP A 1 124 ? 19.161 31.070 -2.119 1.00 23.32 ? 124 TRP A CG 1 ATOM 920 C CD1 . TRP A 1 124 ? 19.749 31.832 -3.088 1.00 24.31 ? 124 TRP A CD1 1 ATOM 921 C CD2 . TRP A 1 124 ? 18.233 30.220 -2.783 1.00 24.88 ? 124 TRP A CD2 1 ATOM 922 N NE1 . TRP A 1 124 ? 19.236 31.499 -4.321 1.00 25.00 ? 124 TRP A NE1 1 ATOM 923 C CE2 . TRP A 1 124 ? 18.302 30.511 -4.156 1.00 25.37 ? 124 TRP A CE2 1 ATOM 924 C CE3 . TRP A 1 124 ? 17.343 29.233 -2.353 1.00 25.92 ? 124 TRP A CE3 1 ATOM 925 C CZ2 . TRP A 1 124 ? 17.521 29.855 -5.092 1.00 26.21 ? 124 TRP A CZ2 1 ATOM 926 C CZ3 . TRP A 1 124 ? 16.573 28.588 -3.282 1.00 25.82 ? 124 TRP A CZ3 1 ATOM 927 C CH2 . TRP A 1 124 ? 16.664 28.898 -4.634 1.00 26.40 ? 124 TRP A CH2 1 ATOM 928 N N . GLY A 1 125 ? 21.456 31.353 1.986 1.00 20.64 ? 125 GLY A N 1 ATOM 929 C CA . GLY A 1 125 ? 21.450 31.626 3.412 1.00 20.54 ? 125 GLY A CA 1 ATOM 930 C C . GLY A 1 125 ? 20.377 30.833 4.142 1.00 20.39 ? 125 GLY A C 1 ATOM 931 O O . GLY A 1 125 ? 20.110 31.088 5.315 1.00 21.71 ? 125 GLY A O 1 ATOM 932 N N . VAL A 1 126 ? 19.767 29.882 3.442 1.00 19.61 ? 126 VAL A N 1 ATOM 933 C CA . VAL A 1 126 ? 18.862 28.891 4.049 1.00 19.73 ? 126 VAL A CA 1 ATOM 934 C C . VAL A 1 126 ? 19.600 28.106 5.138 1.00 19.46 ? 126 VAL A C 1 ATOM 935 O O . VAL A 1 126 ? 20.781 27.786 4.980 1.00 19.44 ? 126 VAL A O 1 ATOM 936 C CB . VAL A 1 126 ? 18.373 27.899 2.994 1.00 19.73 ? 126 VAL A CB 1 ATOM 937 C CG1 . VAL A 1 126 ? 17.729 26.646 3.637 1.00 20.67 ? 126 VAL A CG1 1 ATOM 938 C CG2 . VAL A 1 126 ? 17.413 28.597 2.040 1.00 20.12 ? 126 VAL A CG2 1 ATOM 939 N N . ASP A 1 127 ? 18.905 27.799 6.233 1.00 18.46 ? 127 ASP A N 1 ATOM 940 C CA . ASP A 1 127 ? 19.519 27.135 7.394 1.00 18.38 ? 127 ASP A CA 1 ATOM 941 C C . ASP A 1 127 ? 18.970 25.759 7.711 1.00 17.53 ? 127 ASP A C 1 ATOM 942 O O . ASP A 1 127 ? 19.537 25.015 8.521 1.00 18.06 ? 127 ASP A O 1 ATOM 943 C CB . ASP A 1 127 ? 19.304 27.990 8.634 1.00 18.01 ? 127 ASP A CB 1 ATOM 944 C CG . ASP A 1 127 ? 19.783 29.398 8.443 1.00 20.39 ? 127 ASP A CG 1 ATOM 945 O OD1 . ASP A 1 127 ? 21.011 29.565 8.240 1.00 20.88 ? 127 ASP A OD1 1 ATOM 946 O OD2 . ASP A 1 127 ? 19.010 30.386 8.479 1.00 20.88 ? 127 ASP A OD2 1 ATOM 947 N N . TYR A 1 128 ? 17.866 25.425 7.066 1.00 17.05 ? 128 TYR A N 1 ATOM 948 C CA . TYR A 1 128 ? 17.128 24.234 7.402 1.00 16.46 ? 128 TYR A CA 1 ATOM 949 C C . TYR A 1 128 ? 16.425 23.726 6.159 1.00 16.16 ? 128 TYR A C 1 ATOM 950 O O . TYR A 1 128 ? 15.805 24.492 5.427 1.00 15.48 ? 128 TYR A O 1 ATOM 951 C CB . TYR A 1 128 ? 16.104 24.647 8.463 1.00 16.62 ? 128 TYR A CB 1 ATOM 952 C CG . TYR A 1 128 ? 15.160 23.606 9.041 1.00 16.74 ? 128 TYR A CG 1 ATOM 953 C CD1 . TYR A 1 128 ? 14.180 22.996 8.262 1.00 16.37 ? 128 TYR A CD1 1 ATOM 954 C CD2 . TYR A 1 128 ? 15.254 23.250 10.373 1.00 15.92 ? 128 TYR A CD2 1 ATOM 955 C CE1 . TYR A 1 128 ? 13.323 22.052 8.803 1.00 16.14 ? 128 TYR A CE1 1 ATOM 956 C CE2 . TYR A 1 128 ? 14.411 22.311 10.930 1.00 16.97 ? 128 TYR A CE2 1 ATOM 957 C CZ . TYR A 1 128 ? 13.451 21.716 10.154 1.00 17.01 ? 128 TYR A CZ 1 ATOM 958 O OH . TYR A 1 128 ? 12.623 20.787 10.731 1.00 17.86 ? 128 TYR A OH 1 ATOM 959 N N . LEU A 1 129 ? 16.523 22.427 5.923 1.00 15.73 ? 129 LEU A N 1 ATOM 960 C CA . LEU A 1 129 ? 15.879 21.831 4.766 1.00 15.08 ? 129 LEU A CA 1 ATOM 961 C C . LEU A 1 129 ? 14.929 20.746 5.209 1.00 14.60 ? 129 LEU A C 1 ATOM 962 O O . LEU A 1 129 ? 15.340 19.748 5.764 1.00 14.95 ? 129 LEU A O 1 ATOM 963 C CB . LEU A 1 129 ? 16.903 21.203 3.819 1.00 14.98 ? 129 LEU A CB 1 ATOM 964 C CG . LEU A 1 129 ? 16.293 20.450 2.629 1.00 14.97 ? 129 LEU A CG 1 ATOM 965 C CD1 . LEU A 1 129 ? 15.312 21.362 1.908 1.00 15.71 ? 129 LEU A CD1 1 ATOM 966 C CD2 . LEU A 1 129 ? 17.405 20.040 1.664 1.00 14.32 ? 129 LEU A CD2 1 ATOM 967 N N . LYS A 1 130 ? 13.649 20.957 4.954 1.00 15.25 ? 130 LYS A N 1 ATOM 968 C CA . LYS A 1 130 ? 12.671 19.915 5.169 1.00 14.95 ? 130 LYS A CA 1 ATOM 969 C C . LYS A 1 130 ? 12.609 19.178 3.860 1.00 14.57 ? 130 LYS A C 1 ATOM 970 O O . LYS A 1 130 ? 12.356 19.773 2.820 1.00 14.30 ? 130 LYS A O 1 ATOM 971 C CB . LYS A 1 130 ? 11.303 20.493 5.455 1.00 14.72 ? 130 LYS A CB 1 ATOM 972 C CG . LYS A 1 130 ? 10.226 19.413 5.538 1.00 15.86 ? 130 LYS A CG 1 ATOM 973 C CD . LYS A 1 130 ? 8.881 20.005 5.917 1.00 14.51 ? 130 LYS A CD 1 ATOM 974 C CE . LYS A 1 130 ? 7.786 18.975 5.791 1.00 16.86 ? 130 LYS A CE 1 ATOM 975 N NZ . LYS A 1 130 ? 6.476 19.581 6.230 1.00 17.31 ? 130 LYS A NZ 1 ATOM 976 N N . TYR A 1 131 ? 12.826 17.881 3.908 1.00 14.23 ? 131 TYR A N 1 ATOM 977 C CA . TYR A 1 131 ? 13.020 17.146 2.685 1.00 14.66 ? 131 TYR A CA 1 ATOM 978 C C . TYR A 1 131 ? 11.988 16.020 2.571 1.00 14.88 ? 131 TYR A C 1 ATOM 979 O O . TYR A 1 131 ? 12.027 15.067 3.329 1.00 16.20 ? 131 TYR A O 1 ATOM 980 C CB . TYR A 1 131 ? 14.463 16.623 2.696 1.00 13.23 ? 131 TYR A CB 1 ATOM 981 C CG . TYR A 1 131 ? 15.052 16.359 1.334 1.00 13.81 ? 131 TYR A CG 1 ATOM 982 C CD1 . TYR A 1 131 ? 15.749 15.188 1.082 1.00 12.08 ? 131 TYR A CD1 1 ATOM 983 C CD2 . TYR A 1 131 ? 14.915 17.275 0.298 1.00 12.84 ? 131 TYR A CD2 1 ATOM 984 C CE1 . TYR A 1 131 ? 16.308 14.924 -0.177 1.00 14.13 ? 131 TYR A CE1 1 ATOM 985 C CE2 . TYR A 1 131 ? 15.463 17.023 -0.966 1.00 15.27 ? 131 TYR A CE2 1 ATOM 986 C CZ . TYR A 1 131 ? 16.157 15.845 -1.186 1.00 14.39 ? 131 TYR A CZ 1 ATOM 987 O OH . TYR A 1 131 ? 16.694 15.600 -2.425 1.00 15.16 ? 131 TYR A OH 1 ATOM 988 N N . ASP A 1 132 ? 11.077 16.146 1.615 1.00 15.00 ? 132 ASP A N 1 ATOM 989 C CA . ASP A 1 132 ? 9.895 15.288 1.551 1.00 15.46 ? 132 ASP A CA 1 ATOM 990 C C . ASP A 1 132 ? 10.092 14.024 0.730 1.00 15.31 ? 132 ASP A C 1 ATOM 991 O O . ASP A 1 132 ? 11.147 13.786 0.158 1.00 14.70 ? 132 ASP A O 1 ATOM 992 C CB . ASP A 1 132 ? 8.738 16.098 0.957 1.00 16.25 ? 132 ASP A CB 1 ATOM 993 C CG . ASP A 1 132 ? 7.397 15.839 1.643 1.00 18.11 ? 132 ASP A CG 1 ATOM 994 O OD1 . ASP A 1 132 ? 7.119 14.718 2.134 1.00 19.20 ? 132 ASP A OD1 1 ATOM 995 O OD2 . ASP A 1 132 ? 6.519 16.730 1.736 1.00 18.29 ? 132 ASP A OD2 1 ATOM 996 N N . ASN A 1 133 ? 9.047 13.216 0.675 1.00 14.79 ? 133 ASN A N 1 ATOM 997 C CA . ASN A 1 133 ? 9.145 11.882 0.122 1.00 14.72 ? 133 ASN A CA 1 ATOM 998 C C . ASN A 1 133 ? 8.234 11.606 -1.050 1.00 15.03 ? 133 ASN A C 1 ATOM 999 O O . ASN A 1 133 ? 8.091 10.454 -1.448 1.00 15.53 ? 133 ASN A O 1 ATOM 1000 C CB . ASN A 1 133 ? 8.855 10.879 1.245 1.00 14.79 ? 133 ASN A CB 1 ATOM 1001 C CG . ASN A 1 133 ? 9.531 9.546 1.040 1.00 16.54 ? 133 ASN A CG 1 ATOM 1002 O OD1 . ASN A 1 133 ? 10.638 9.475 0.508 1.00 15.44 ? 133 ASN A OD1 1 ATOM 1003 N ND2 . ASN A 1 133 ? 8.872 8.475 1.465 1.00 17.36 ? 133 ASN A ND2 1 ATOM 1004 N N . CYS A 1 134 ? 7.609 12.630 -1.620 1.00 14.75 ? 134 CYS A N 1 ATOM 1005 C CA . CYS A 1 134 ? 6.711 12.358 -2.755 1.00 15.26 ? 134 CYS A CA 1 ATOM 1006 C C . CYS A 1 134 ? 7.459 12.128 -4.054 1.00 15.66 ? 134 CYS A C 1 ATOM 1007 O O . CYS A 1 134 ? 8.619 12.485 -4.182 1.00 14.74 ? 134 CYS A O 1 ATOM 1008 C CB . CYS A 1 134 ? 5.734 13.503 -2.978 1.00 15.03 ? 134 CYS A CB 1 ATOM 1009 S SG . CYS A 1 134 ? 4.470 13.643 -1.689 1.00 16.02 ? 134 CYS A SG 1 ATOM 1010 N N . ASN A 1 135 ? 6.762 11.523 -5.007 1.00 16.46 ? 135 ASN A N 1 ATOM 1011 C CA . ASN A 1 135 ? 7.211 11.433 -6.387 1.00 17.78 ? 135 ASN A CA 1 ATOM 1012 C C . ASN A 1 135 ? 8.528 10.704 -6.558 1.00 18.23 ? 135 ASN A C 1 ATOM 1013 O O . ASN A 1 135 ? 9.438 11.179 -7.245 1.00 18.20 ? 135 ASN A O 1 ATOM 1014 C CB . ASN A 1 135 ? 7.216 12.841 -7.026 1.00 17.89 ? 135 ASN A CB 1 ATOM 1015 C CG . ASN A 1 135 ? 5.861 13.503 -6.950 1.00 20.39 ? 135 ASN A CG 1 ATOM 1016 O OD1 . ASN A 1 135 ? 5.708 14.632 -6.447 1.00 25.13 ? 135 ASN A OD1 1 ATOM 1017 N ND2 . ASN A 1 135 ? 4.858 12.807 -7.444 1.00 18.28 ? 135 ASN A ND2 1 ATOM 1018 N N . VAL A 1 136 ? 8.624 9.543 -5.926 1.00 18.74 ? 136 VAL A N 1 ATOM 1019 C CA . VAL A 1 136 ? 9.817 8.731 -6.072 1.00 19.93 ? 136 VAL A CA 1 ATOM 1020 C C . VAL A 1 136 ? 9.595 7.899 -7.328 1.00 20.65 ? 136 VAL A C 1 ATOM 1021 O O . VAL A 1 136 ? 8.619 7.192 -7.427 1.00 20.47 ? 136 VAL A O 1 ATOM 1022 C CB . VAL A 1 136 ? 10.036 7.831 -4.855 1.00 19.61 ? 136 VAL A CB 1 ATOM 1023 C CG1 . VAL A 1 136 ? 11.285 6.939 -5.040 1.00 20.44 ? 136 VAL A CG1 1 ATOM 1024 C CG2 . VAL A 1 136 ? 10.166 8.669 -3.596 1.00 20.07 ? 136 VAL A CG2 1 ATOM 1025 N N . PRO A 1 137 ? 10.503 7.985 -8.291 1.00 22.91 ? 137 PRO A N 1 ATOM 1026 C CA . PRO A 1 137 ? 10.356 7.230 -9.548 1.00 24.19 ? 137 PRO A CA 1 ATOM 1027 C C . PRO A 1 137 ? 10.495 5.720 -9.320 1.00 25.94 ? 137 PRO A C 1 ATOM 1028 O O . PRO A 1 137 ? 11.067 5.311 -8.298 1.00 24.66 ? 137 PRO A O 1 ATOM 1029 C CB . PRO A 1 137 ? 11.509 7.735 -10.422 1.00 24.42 ? 137 PRO A CB 1 ATOM 1030 C CG . PRO A 1 137 ? 12.139 8.862 -9.685 1.00 24.41 ? 137 PRO A CG 1 ATOM 1031 C CD . PRO A 1 137 ? 11.727 8.800 -8.244 1.00 22.07 ? 137 PRO A CD 1 ATOM 1032 N N . SER A 1 138 ? 9.978 4.915 -10.264 1.00 27.51 ? 138 SER A N 1 ATOM 1033 C CA . SER A 1 138 ? 9.909 3.452 -10.117 1.00 29.29 ? 138 SER A CA 1 ATOM 1034 C C . SER A 1 138 ? 11.259 2.834 -9.834 1.00 29.86 ? 138 SER A C 1 ATOM 1035 O O . SER A 1 138 ? 11.381 1.880 -9.060 1.00 30.54 ? 138 SER A O 1 ATOM 1036 C CB . SER A 1 138 ? 9.337 2.809 -11.397 1.00 29.85 ? 138 SER A CB 1 ATOM 1037 O OG . SER A 1 138 ? 8.063 3.352 -11.711 1.00 32.32 ? 138 SER A OG 1 ATOM 1038 N N . ASP A 1 139 ? 12.270 3.398 -10.476 1.00 29.96 ? 139 ASP A N 1 ATOM 1039 C CA . ASP A 1 139 ? 13.630 2.932 -10.369 1.00 31.27 ? 139 ASP A CA 1 ATOM 1040 C C . ASP A 1 139 ? 14.251 3.272 -9.030 1.00 30.44 ? 139 ASP A C 1 ATOM 1041 O O . ASP A 1 139 ? 15.295 2.729 -8.677 1.00 30.28 ? 139 ASP A O 1 ATOM 1042 C CB . ASP A 1 139 ? 14.460 3.589 -11.475 1.00 32.05 ? 139 ASP A CB 1 ATOM 1043 C CG . ASP A 1 139 ? 15.436 2.635 -12.111 1.00 36.15 ? 139 ASP A CG 1 ATOM 1044 O OD1 . ASP A 1 139 ? 16.222 1.987 -11.363 1.00 39.27 ? 139 ASP A OD1 1 ATOM 1045 O OD2 . ASP A 1 139 ? 15.491 2.468 -13.362 1.00 38.56 ? 139 ASP A OD2 1 ATOM 1046 N N . TRP A 1 140 ? 13.611 4.170 -8.287 1.00 29.64 ? 140 TRP A N 1 ATOM 1047 C CA . TRP A 1 140 ? 14.123 4.591 -6.993 1.00 29.77 ? 140 TRP A CA 1 ATOM 1048 C C . TRP A 1 140 ? 13.285 4.051 -5.844 1.00 29.46 ? 140 TRP A C 1 ATOM 1049 O O . TRP A 1 140 ? 13.551 4.334 -4.685 1.00 29.07 ? 140 TRP A O 1 ATOM 1050 C CB . TRP A 1 140 ? 14.186 6.112 -6.915 1.00 29.78 ? 140 TRP A CB 1 ATOM 1051 C CG . TRP A 1 140 ? 15.470 6.679 -7.405 1.00 30.23 ? 140 TRP A CG 1 ATOM 1052 C CD1 . TRP A 1 140 ? 15.689 7.301 -8.595 1.00 29.31 ? 140 TRP A CD1 1 ATOM 1053 C CD2 . TRP A 1 140 ? 16.719 6.680 -6.714 1.00 31.38 ? 140 TRP A CD2 1 ATOM 1054 N NE1 . TRP A 1 140 ? 17.003 7.689 -8.686 1.00 30.82 ? 140 TRP A NE1 1 ATOM 1055 C CE2 . TRP A 1 140 ? 17.657 7.319 -7.543 1.00 31.22 ? 140 TRP A CE2 1 ATOM 1056 C CE3 . TRP A 1 140 ? 17.145 6.200 -5.469 1.00 32.14 ? 140 TRP A CE3 1 ATOM 1057 C CZ2 . TRP A 1 140 ? 18.984 7.491 -7.174 1.00 32.25 ? 140 TRP A CZ2 1 ATOM 1058 C CZ3 . TRP A 1 140 ? 18.462 6.373 -5.105 1.00 32.49 ? 140 TRP A CZ3 1 ATOM 1059 C CH2 . TRP A 1 140 ? 19.366 7.011 -5.952 1.00 32.50 ? 140 TRP A CH2 1 ATOM 1060 N N . GLN A 1 141 ? 12.276 3.271 -6.190 1.00 29.93 ? 141 GLN A N 1 ATOM 1061 C CA . GLN A 1 141 ? 11.375 2.664 -5.220 1.00 30.06 ? 141 GLN A CA 1 ATOM 1062 C C . GLN A 1 141 ? 12.177 1.672 -4.383 1.00 29.11 ? 141 GLN A C 1 ATOM 1063 O O . GLN A 1 141 ? 13.042 0.976 -4.904 1.00 28.11 ? 141 GLN A O 1 ATOM 1064 C CB . GLN A 1 141 ? 10.271 1.928 -5.980 1.00 30.55 ? 141 GLN A CB 1 ATOM 1065 C CG . GLN A 1 141 ? 8.859 2.268 -5.585 1.00 35.48 ? 141 GLN A CG 1 ATOM 1066 C CD . GLN A 1 141 ? 8.405 3.615 -6.124 1.00 40.59 ? 141 GLN A CD 1 ATOM 1067 O OE1 . GLN A 1 141 ? 7.535 3.689 -7.003 1.00 42.83 ? 141 GLN A OE1 1 ATOM 1068 N NE2 . GLN A 1 141 ? 8.991 4.685 -5.600 1.00 42.98 ? 141 GLN A NE2 1 ATOM 1069 N N . ASP A 1 142 ? 11.898 1.607 -3.085 1.00 28.25 ? 142 ASP A N 1 ATOM 1070 C CA . ASP A 1 142 ? 12.478 0.554 -2.261 1.00 27.94 ? 142 ASP A CA 1 ATOM 1071 C C . ASP A 1 142 ? 11.960 -0.826 -2.692 1.00 28.25 ? 142 ASP A C 1 ATOM 1072 O O . ASP A 1 142 ? 10.821 -0.969 -3.136 1.00 27.20 ? 142 ASP A O 1 ATOM 1073 C CB . ASP A 1 142 ? 12.142 0.758 -0.781 1.00 27.56 ? 142 ASP A CB 1 ATOM 1074 C CG . ASP A 1 142 ? 12.767 2.012 -0.210 1.00 26.09 ? 142 ASP A CG 1 ATOM 1075 O OD1 . ASP A 1 142 ? 13.875 2.386 -0.664 1.00 24.79 ? 142 ASP A OD1 1 ATOM 1076 O OD2 . ASP A 1 142 ? 12.227 2.686 0.689 1.00 24.77 ? 142 ASP A OD2 1 ATOM 1077 N N . GLU A 1 143 ? 12.835 -1.814 -2.541 1.00 29.18 ? 143 GLU A N 1 ATOM 1078 C CA . GLU A 1 143 ? 12.564 -3.238 -2.722 1.00 30.45 ? 143 GLU A CA 1 ATOM 1079 C C . GLU A 1 143 ? 11.392 -3.643 -1.856 1.00 30.01 ? 143 GLU A C 1 ATOM 1080 O O . GLU A 1 143 ? 10.472 -4.362 -2.288 1.00 29.99 ? 143 GLU A O 1 ATOM 1081 C CB . GLU A 1 143 ? 13.780 -4.008 -2.208 1.00 30.83 ? 143 GLU A CB 1 ATOM 1082 C CG . GLU A 1 143 ? 14.084 -5.333 -2.880 1.00 35.54 ? 143 GLU A CG 1 ATOM 1083 C CD . GLU A 1 143 ? 15.439 -5.889 -2.457 1.00 40.35 ? 143 GLU A CD 1 ATOM 1084 O OE1 . GLU A 1 143 ? 16.317 -5.100 -2.038 1.00 42.16 ? 143 GLU A OE1 1 ATOM 1085 O OE2 . GLU A 1 143 ? 15.634 -7.122 -2.541 1.00 43.37 ? 143 GLU A OE2 1 ATOM 1086 N N . TYR A 1 144 ? 11.442 -3.165 -0.622 1.00 29.31 ? 144 TYR A N 1 ATOM 1087 C CA . TYR A 1 144 ? 10.524 -3.609 0.408 1.00 29.25 ? 144 TYR A CA 1 ATOM 1088 C C . TYR A 1 144 ? 9.772 -2.447 1.023 1.00 28.36 ? 144 TYR A C 1 ATOM 1089 O O . TYR A 1 144 ? 10.050 -1.286 0.716 1.00 28.28 ? 144 TYR A O 1 ATOM 1090 C CB . TYR A 1 144 ? 11.308 -4.333 1.501 1.00 29.85 ? 144 TYR A CB 1 ATOM 1091 C CG . TYR A 1 144 ? 12.057 -5.548 1.008 1.00 32.19 ? 144 TYR A CG 1 ATOM 1092 C CD1 . TYR A 1 144 ? 11.376 -6.619 0.443 1.00 34.24 ? 144 TYR A CD1 1 ATOM 1093 C CD2 . TYR A 1 144 ? 13.450 -5.625 1.108 1.00 33.87 ? 144 TYR A CD2 1 ATOM 1094 C CE1 . TYR A 1 144 ? 12.054 -7.735 -0.010 1.00 36.52 ? 144 TYR A CE1 1 ATOM 1095 C CE2 . TYR A 1 144 ? 14.139 -6.736 0.658 1.00 35.70 ? 144 TYR A CE2 1 ATOM 1096 C CZ . TYR A 1 144 ? 13.438 -7.786 0.101 1.00 37.85 ? 144 TYR A CZ 1 ATOM 1097 O OH . TYR A 1 144 ? 14.115 -8.896 -0.350 1.00 41.32 ? 144 TYR A OH 1 ATOM 1098 N N . VAL A 1 145 ? 8.812 -2.772 1.889 1.00 27.10 ? 145 VAL A N 1 ATOM 1099 C CA . VAL A 1 145 ? 8.187 -1.772 2.751 1.00 26.14 ? 145 VAL A CA 1 ATOM 1100 C C . VAL A 1 145 ? 8.580 -2.104 4.182 1.00 25.56 ? 145 VAL A C 1 ATOM 1101 O O . VAL A 1 145 ? 8.865 -3.257 4.512 1.00 25.40 ? 145 VAL A O 1 ATOM 1102 C CB . VAL A 1 145 ? 6.674 -1.661 2.562 1.00 26.24 ? 145 VAL A CB 1 ATOM 1103 C CG1 . VAL A 1 145 ? 6.356 -1.188 1.148 1.00 26.66 ? 145 VAL A CG1 1 ATOM 1104 C CG2 . VAL A 1 145 ? 5.984 -2.979 2.852 1.00 26.99 ? 145 VAL A CG2 1 ATOM 1105 N N . ALA A 1 146 ? 8.609 -1.093 5.037 1.00 24.66 ? 146 ALA A N 1 ATOM 1106 C CA . ALA A 1 146 ? 8.852 -1.321 6.449 1.00 23.28 ? 146 ALA A CA 1 ATOM 1107 C C . ALA A 1 146 ? 7.476 -1.345 7.115 1.00 23.38 ? 146 ALA A C 1 ATOM 1108 O O . ALA A 1 146 ? 6.474 -0.897 6.520 1.00 22.42 ? 146 ALA A O 1 ATOM 1109 C CB . ALA A 1 146 ? 9.700 -0.225 7.006 1.00 23.64 ? 146 ALA A CB 1 ATOM 1110 N N . CYS A 1 147 ? 7.407 -1.859 8.338 1.00 22.57 ? 147 CYS A N 1 ATOM 1111 C CA . CYS A 1 147 ? 6.124 -1.950 9.004 1.00 22.35 ? 147 CYS A CA 1 ATOM 1112 C C . CYS A 1 147 ? 5.702 -0.600 9.548 1.00 21.80 ? 147 CYS A C 1 ATOM 1113 O O . CYS A 1 147 ? 6.036 -0.238 10.673 1.00 22.09 ? 147 CYS A O 1 ATOM 1114 C CB . CYS A 1 147 ? 6.132 -2.975 10.120 1.00 22.61 ? 147 CYS A CB 1 ATOM 1115 S SG . CYS A 1 147 ? 4.465 -3.158 10.754 1.00 24.50 ? 147 CYS A SG 1 ATOM 1116 N N . ASN A 1 148 ? 4.964 0.135 8.731 1.00 20.63 ? 148 ASN A N 1 ATOM 1117 C CA . ASN A 1 148 ? 4.507 1.463 9.077 1.00 19.78 ? 148 ASN A CA 1 ATOM 1118 C C . ASN A 1 148 ? 2.994 1.416 8.985 1.00 19.41 ? 148 ASN A C 1 ATOM 1119 O O . ASN A 1 148 ? 2.433 1.406 7.894 1.00 18.33 ? 148 ASN A O 1 ATOM 1120 C CB . ASN A 1 148 ? 5.111 2.476 8.092 1.00 19.66 ? 148 ASN A CB 1 ATOM 1121 C CG . ASN A 1 148 ? 4.728 3.916 8.401 1.00 19.99 ? 148 ASN A CG 1 ATOM 1122 O OD1 . ASN A 1 148 ? 5.253 4.851 7.789 1.00 23.04 ? 148 ASN A OD1 1 ATOM 1123 N ND2 . ASN A 1 148 ? 3.822 4.104 9.337 1.00 17.57 ? 148 ASN A ND2 1 ATOM 1124 N N . PRO A 1 149 ? 2.333 1.388 10.140 1.00 19.40 ? 149 PRO A N 1 ATOM 1125 C CA . PRO A 1 149 ? 0.873 1.315 10.189 1.00 19.55 ? 149 PRO A CA 1 ATOM 1126 C C . PRO A 1 149 ? 0.178 2.465 9.465 1.00 19.24 ? 149 PRO A C 1 ATOM 1127 O O . PRO A 1 149 ? -0.967 2.272 9.102 1.00 19.01 ? 149 PRO A O 1 ATOM 1128 C CB . PRO A 1 149 ? 0.571 1.339 11.695 1.00 19.15 ? 149 PRO A CB 1 ATOM 1129 C CG . PRO A 1 149 ? 1.837 0.785 12.309 1.00 20.62 ? 149 PRO A CG 1 ATOM 1130 C CD . PRO A 1 149 ? 2.929 1.427 11.485 1.00 19.53 ? 149 PRO A CD 1 ATOM 1131 N N . ASP A 1 150 ? 0.822 3.613 9.258 1.00 19.25 ? 150 ASP A N 1 ATOM 1132 C CA . ASP A 1 150 ? 0.165 4.711 8.532 1.00 19.46 ? 150 ASP A CA 1 ATOM 1133 C C . ASP A 1 150 ? -0.002 4.399 7.045 1.00 20.09 ? 150 ASP A C 1 ATOM 1134 O O . ASP A 1 150 ? -0.836 5.001 6.367 1.00 20.12 ? 150 ASP A O 1 ATOM 1135 C CB . ASP A 1 150 ? 0.911 6.034 8.688 1.00 19.15 ? 150 ASP A CB 1 ATOM 1136 C CG . ASP A 1 150 ? 0.366 6.872 9.812 1.00 19.11 ? 150 ASP A CG 1 ATOM 1137 O OD1 . ASP A 1 150 ? 0.919 7.944 10.112 1.00 18.71 ? 150 ASP A OD1 1 ATOM 1138 O OD2 . ASP A 1 150 ? -0.619 6.528 10.458 1.00 17.59 ? 150 ASP A OD2 1 ATOM 1139 N N . PHE A 1 151 ? 0.791 3.459 6.537 1.00 20.73 ? 151 PHE A N 1 ATOM 1140 C CA . PHE A 1 151 ? 0.731 3.109 5.112 1.00 21.72 ? 151 PHE A CA 1 ATOM 1141 C C . PHE A 1 151 ? 0.415 1.643 4.813 1.00 22.96 ? 151 PHE A C 1 ATOM 1142 O O . PHE A 1 151 ? -0.191 1.341 3.788 1.00 24.10 ? 151 PHE A O 1 ATOM 1143 C CB . PHE A 1 151 ? 2.033 3.525 4.407 1.00 21.20 ? 151 PHE A CB 1 ATOM 1144 C CG . PHE A 1 151 ? 2.234 5.000 4.389 1.00 20.51 ? 151 PHE A CG 1 ATOM 1145 C CD1 . PHE A 1 151 ? 1.700 5.772 3.365 1.00 21.05 ? 151 PHE A CD1 1 ATOM 1146 C CD2 . PHE A 1 151 ? 2.946 5.629 5.395 1.00 19.28 ? 151 PHE A CD2 1 ATOM 1147 C CE1 . PHE A 1 151 ? 1.886 7.151 3.353 1.00 21.26 ? 151 PHE A CE1 1 ATOM 1148 C CE2 . PHE A 1 151 ? 3.129 7.001 5.382 1.00 20.22 ? 151 PHE A CE2 1 ATOM 1149 C CZ . PHE A 1 151 ? 2.599 7.760 4.362 1.00 20.06 ? 151 PHE A CZ 1 ATOM 1150 N N . VAL A 1 152 ? 0.812 0.726 5.686 1.00 23.24 ? 152 VAL A N 1 ATOM 1151 C CA . VAL A 1 152 ? 0.672 -0.684 5.335 1.00 23.50 ? 152 VAL A CA 1 ATOM 1152 C C . VAL A 1 152 ? -0.375 -1.388 6.155 1.00 24.45 ? 152 VAL A C 1 ATOM 1153 O O . VAL A 1 152 ? -0.690 -0.974 7.271 1.00 24.57 ? 152 VAL A O 1 ATOM 1154 C CB . VAL A 1 152 ? 2.006 -1.438 5.404 1.00 23.04 ? 152 VAL A CB 1 ATOM 1155 C CG1 . VAL A 1 152 ? 3.069 -0.659 4.656 1.00 23.21 ? 152 VAL A CG1 1 ATOM 1156 C CG2 . VAL A 1 152 ? 2.419 -1.671 6.835 1.00 22.60 ? 152 VAL A CG2 1 ATOM 1157 N N . LYS A 1 153 ? -0.907 -2.458 5.583 1.00 24.91 ? 153 LYS A N 1 ATOM 1158 C CA . LYS A 1 153 ? -1.973 -3.213 6.214 1.00 26.59 ? 153 LYS A CA 1 ATOM 1159 C C . LYS A 1 153 ? -1.416 -3.847 7.453 1.00 25.96 ? 153 LYS A C 1 ATOM 1160 O O . LYS A 1 153 ? -0.367 -4.474 7.404 1.00 26.08 ? 153 LYS A O 1 ATOM 1161 C CB . LYS A 1 153 ? -2.469 -4.319 5.271 1.00 27.08 ? 153 LYS A CB 1 ATOM 1162 C CG . LYS A 1 153 ? -3.539 -3.896 4.311 1.00 31.45 ? 153 LYS A CG 1 ATOM 1163 C CD . LYS A 1 153 ? -3.737 -4.937 3.185 1.00 38.10 ? 153 LYS A CD 1 ATOM 1164 C CE . LYS A 1 153 ? -3.536 -6.380 3.677 1.00 41.21 ? 153 LYS A CE 1 ATOM 1165 N NZ . LYS A 1 153 ? -3.169 -7.299 2.548 1.00 45.28 ? 153 LYS A NZ 1 ATOM 1166 N N . THR A 1 154 ? -2.108 -3.691 8.573 1.00 26.19 ? 154 THR A N 1 ATOM 1167 C CA . THR A 1 154 ? -1.625 -4.303 9.793 1.00 26.38 ? 154 THR A CA 1 ATOM 1168 C C . THR A 1 154 ? -2.632 -5.252 10.377 1.00 26.77 ? 154 THR A C 1 ATOM 1169 O O . THR A 1 154 ? -3.819 -5.156 10.101 1.00 26.70 ? 154 THR A O 1 ATOM 1170 C CB . THR A 1 154 ? -1.252 -3.238 10.844 1.00 26.42 ? 154 THR A CB 1 ATOM 1171 O OG1 . THR A 1 154 ? -2.342 -2.311 11.017 1.00 26.69 ? 154 THR A OG1 1 ATOM 1172 C CG2 . THR A 1 154 ? -0.115 -2.398 10.324 1.00 24.91 ? 154 THR A CG2 1 ATOM 1173 N N . GLY A 1 155 ? -2.131 -6.173 11.191 1.00 27.16 ? 155 GLY A N 1 ATOM 1174 C CA . GLY A 1 155 ? -2.986 -7.047 11.957 1.00 27.89 ? 155 GLY A CA 1 ATOM 1175 C C . GLY A 1 155 ? -3.244 -6.390 13.302 1.00 28.41 ? 155 GLY A C 1 ATOM 1176 O O . GLY A 1 155 ? -3.043 -5.180 13.469 1.00 28.07 ? 155 GLY A O 1 ATOM 1177 N N . PRO A 1 156 ? -3.693 -7.182 14.270 1.00 28.72 ? 156 PRO A N 1 ATOM 1178 C CA . PRO A 1 156 ? -3.955 -6.666 15.614 1.00 28.40 ? 156 PRO A CA 1 ATOM 1179 C C . PRO A 1 156 ? -2.647 -6.189 16.203 1.00 27.30 ? 156 PRO A C 1 ATOM 1180 O O . PRO A 1 156 ? -1.587 -6.785 15.961 1.00 27.28 ? 156 PRO A O 1 ATOM 1181 C CB . PRO A 1 156 ? -4.478 -7.891 16.365 1.00 28.88 ? 156 PRO A CB 1 ATOM 1182 C CG . PRO A 1 156 ? -5.021 -8.759 15.276 1.00 30.08 ? 156 PRO A CG 1 ATOM 1183 C CD . PRO A 1 156 ? -3.988 -8.621 14.165 1.00 29.28 ? 156 PRO A CD 1 ATOM 1184 N N . ASN A 1 157 ? -2.729 -5.113 16.971 1.00 26.29 ? 157 ASN A N 1 ATOM 1185 C CA . ASN A 1 157 ? -1.559 -4.557 17.629 1.00 25.37 ? 157 ASN A CA 1 ATOM 1186 C C . ASN A 1 157 ? -0.558 -3.940 16.667 1.00 25.23 ? 157 ASN A C 1 ATOM 1187 O O . ASN A 1 157 ? 0.637 -3.950 16.929 1.00 24.98 ? 157 ASN A O 1 ATOM 1188 C CB . ASN A 1 157 ? -0.881 -5.628 18.464 1.00 24.78 ? 157 ASN A CB 1 ATOM 1189 C CG . ASN A 1 157 ? 0.027 -5.049 19.540 1.00 24.47 ? 157 ASN A CG 1 ATOM 1190 O OD1 . ASN A 1 157 ? -0.312 -4.057 20.218 1.00 21.10 ? 157 ASN A OD1 1 ATOM 1191 N ND2 . ASN A 1 157 ? 1.191 -5.676 19.697 1.00 22.35 ? 157 ASN A ND2 1 ATOM 1192 N N . GLY A 1 158 ? -1.045 -3.404 15.556 1.00 25.18 ? 158 GLY A N 1 ATOM 1193 C CA . GLY A 1 158 ? -0.177 -2.716 14.603 1.00 26.19 ? 158 GLY A CA 1 ATOM 1194 C C . GLY A 1 158 ? 0.906 -3.592 13.999 1.00 26.66 ? 158 GLY A C 1 ATOM 1195 O O . GLY A 1 158 ? 1.950 -3.102 13.568 1.00 26.78 ? 158 GLY A O 1 ATOM 1196 N N . THR A 1 159 ? 0.669 -4.894 13.962 1.00 27.48 ? 159 THR A N 1 ATOM 1197 C CA . THR A 1 159 ? 1.680 -5.792 13.415 1.00 28.99 ? 159 THR A CA 1 ATOM 1198 C C . THR A 1 159 ? 1.582 -5.993 11.925 1.00 29.03 ? 159 THR A C 1 ATOM 1199 O O . THR A 1 159 ? 0.499 -5.979 11.344 1.00 29.54 ? 159 THR A O 1 ATOM 1200 C CB . THR A 1 159 ? 1.652 -7.164 14.101 1.00 28.93 ? 159 THR A CB 1 ATOM 1201 O OG1 . THR A 1 159 ? 0.324 -7.701 14.057 1.00 31.15 ? 159 THR A OG1 1 ATOM 1202 C CG2 . THR A 1 159 ? 1.952 -7.018 15.560 1.00 29.99 ? 159 THR A CG2 1 ATOM 1203 N N . CYS A 1 160 ? 2.741 -6.185 11.314 1.00 29.46 ? 160 CYS A N 1 ATOM 1204 C CA . CYS A 1 160 ? 2.810 -6.525 9.918 1.00 29.03 ? 160 CYS A CA 1 ATOM 1205 C C . CYS A 1 160 ? 3.267 -7.933 9.759 1.00 30.16 ? 160 CYS A C 1 ATOM 1206 O O . CYS A 1 160 ? 4.082 -8.433 10.525 1.00 29.84 ? 160 CYS A O 1 ATOM 1207 C CB . CYS A 1 160 ? 3.836 -5.673 9.209 1.00 29.02 ? 160 CYS A CB 1 ATOM 1208 S SG . CYS A 1 160 ? 3.399 -3.969 9.266 1.00 25.15 ? 160 CYS A SG 1 ATOM 1209 N N . THR A 1 161 ? 2.729 -8.574 8.741 1.00 31.18 ? 161 THR A N 1 ATOM 1210 C CA . THR A 1 161 ? 3.186 -9.885 8.379 1.00 32.71 ? 161 THR A CA 1 ATOM 1211 C C . THR A 1 161 ? 3.296 -9.935 6.868 1.00 33.70 ? 161 THR A C 1 ATOM 1212 O O . THR A 1 161 ? 2.819 -9.054 6.129 1.00 34.13 ? 161 THR A O 1 ATOM 1213 C CB . THR A 1 161 ? 2.183 -10.950 8.819 1.00 32.47 ? 161 THR A CB 1 ATOM 1214 O OG1 . THR A 1 161 ? 0.999 -10.810 8.035 1.00 32.58 ? 161 THR A OG1 1 ATOM 1215 C CG2 . THR A 1 161 ? 1.682 -10.693 10.231 1.00 33.49 ? 161 THR A CG2 1 ATOM 1216 N N . THR A 1 162 ? 3.937 -10.993 6.421 1.00 34.82 ? 162 THR A N 1 ATOM 1217 C CA . THR A 1 162 ? 4.107 -11.252 5.022 1.00 36.13 ? 162 THR A CA 1 ATOM 1218 C C . THR A 1 162 ? 2.768 -11.437 4.325 1.00 36.64 ? 162 THR A C 1 ATOM 1219 O O . THR A 1 162 ? 2.580 -10.956 3.206 1.00 36.76 ? 162 THR A O 1 ATOM 1220 C CB . THR A 1 162 ? 5.003 -12.473 4.889 1.00 35.97 ? 162 THR A CB 1 ATOM 1221 O OG1 . THR A 1 162 ? 6.358 -12.027 4.929 1.00 36.28 ? 162 THR A OG1 1 ATOM 1222 C CG2 . THR A 1 162 ? 4.867 -13.098 3.521 1.00 37.72 ? 162 THR A CG2 1 ATOM 1223 N N . ALA A 1 163 ? 1.843 -12.129 4.988 1.00 36.99 ? 163 ALA A N 1 ATOM 1224 C CA . ALA A 1 163 ? 0.544 -12.427 4.398 1.00 37.74 ? 163 ALA A CA 1 ATOM 1225 C C . ALA A 1 163 ? -0.271 -11.165 4.171 1.00 37.90 ? 163 ALA A C 1 ATOM 1226 O O . ALA A 1 163 ? -1.084 -11.086 3.251 1.00 37.71 ? 163 ALA A O 1 ATOM 1227 C CB . ALA A 1 163 ? -0.235 -13.409 5.278 1.00 37.86 ? 163 ALA A CB 1 ATOM 1228 N N . LEU A 1 164 ? -0.044 -10.175 5.022 1.00 38.05 ? 164 LEU A N 1 ATOM 1229 C CA . LEU A 1 164 ? -0.776 -8.923 4.926 1.00 38.05 ? 164 LEU A CA 1 ATOM 1230 C C . LEU A 1 164 ? -0.032 -8.005 3.985 1.00 38.14 ? 164 LEU A C 1 ATOM 1231 O O . LEU A 1 164 ? -0.628 -7.215 3.253 1.00 38.23 ? 164 LEU A O 1 ATOM 1232 C CB . LEU A 1 164 ? -0.865 -8.266 6.299 1.00 38.01 ? 164 LEU A CB 1 ATOM 1233 C CG . LEU A 1 164 ? -1.742 -8.956 7.341 1.00 37.75 ? 164 LEU A CG 1 ATOM 1234 C CD1 . LEU A 1 164 ? -1.544 -8.281 8.681 1.00 36.89 ? 164 LEU A CD1 1 ATOM 1235 C CD2 . LEU A 1 164 ? -3.202 -8.924 6.911 1.00 37.55 ? 164 LEU A CD2 1 ATOM 1236 N N . ASP A 1 165 ? 1.285 -8.120 4.016 1.00 38.63 ? 165 ASP A N 1 ATOM 1237 C CA . ASP A 1 165 ? 2.137 -7.320 3.157 1.00 39.21 ? 165 ASP A CA 1 ATOM 1238 C C . ASP A 1 165 ? 3.247 -8.150 2.572 1.00 38.78 ? 165 ASP A C 1 ATOM 1239 O O . ASP A 1 165 ? 4.287 -8.366 3.202 1.00 38.94 ? 165 ASP A O 1 ATOM 1240 C CB . ASP A 1 165 ? 2.690 -6.121 3.906 1.00 39.85 ? 165 ASP A CB 1 ATOM 1241 C CG . ASP A 1 165 ? 1.948 -4.870 3.564 1.00 42.11 ? 165 ASP A CG 1 ATOM 1242 O OD1 . ASP A 1 165 ? 1.070 -4.457 4.365 1.00 41.97 ? 165 ASP A OD1 1 ATOM 1243 O OD2 . ASP A 1 165 ? 2.194 -4.249 2.499 1.00 42.63 ? 165 ASP A OD2 1 ATOM 1244 N N . PRO A 1 166 ? 3.011 -8.617 1.354 1.00 38.69 ? 166 PRO A N 1 ATOM 1245 C CA . PRO A 1 166 ? 3.968 -9.458 0.628 1.00 38.40 ? 166 PRO A CA 1 ATOM 1246 C C . PRO A 1 166 ? 5.349 -8.838 0.482 1.00 38.00 ? 166 PRO A C 1 ATOM 1247 O O . PRO A 1 166 ? 6.319 -9.587 0.369 1.00 38.17 ? 166 PRO A O 1 ATOM 1248 C CB . PRO A 1 166 ? 3.315 -9.603 -0.745 1.00 38.46 ? 166 PRO A CB 1 ATOM 1249 C CG . PRO A 1 166 ? 1.868 -9.440 -0.469 1.00 38.93 ? 166 PRO A CG 1 ATOM 1250 C CD . PRO A 1 166 ? 1.788 -8.366 0.575 1.00 38.69 ? 166 PRO A CD 1 ATOM 1251 N N . THR A 1 167 ? 5.437 -7.509 0.486 1.00 37.59 ? 167 THR A N 1 ATOM 1252 C CA . THR A 1 167 ? 6.718 -6.832 0.282 1.00 37.40 ? 167 THR A CA 1 ATOM 1253 C C . THR A 1 167 ? 7.400 -6.409 1.576 1.00 37.16 ? 167 THR A C 1 ATOM 1254 O O . THR A 1 167 ? 8.395 -5.694 1.548 1.00 36.86 ? 167 THR A O 1 ATOM 1255 C CB . THR A 1 167 ? 6.558 -5.624 -0.677 1.00 37.53 ? 167 THR A CB 1 ATOM 1256 O OG1 . THR A 1 167 ? 5.675 -4.653 -0.101 1.00 37.60 ? 167 THR A OG1 1 ATOM 1257 C CG2 . THR A 1 167 ? 5.820 -6.053 -1.935 1.00 37.47 ? 167 THR A CG2 1 ATOM 1258 N N . LEU A 1 168 ? 6.868 -6.853 2.707 1.00 37.10 ? 168 LEU A N 1 ATOM 1259 C CA . LEU A 1 168 ? 7.459 -6.534 3.994 1.00 37.19 ? 168 LEU A CA 1 ATOM 1260 C C . LEU A 1 168 ? 8.896 -6.981 3.965 1.00 37.31 ? 168 LEU A C 1 ATOM 1261 O O . LEU A 1 168 ? 9.198 -8.058 3.472 1.00 37.29 ? 168 LEU A O 1 ATOM 1262 C CB . LEU A 1 168 ? 6.738 -7.271 5.110 1.00 37.06 ? 168 LEU A CB 1 ATOM 1263 C CG . LEU A 1 168 ? 7.035 -6.811 6.535 1.00 37.94 ? 168 LEU A CG 1 ATOM 1264 C CD1 . LEU A 1 168 ? 6.606 -5.364 6.721 1.00 37.55 ? 168 LEU A CD1 1 ATOM 1265 C CD2 . LEU A 1 168 ? 6.299 -7.749 7.499 1.00 39.11 ? 168 LEU A CD2 1 ATOM 1266 N N . ALA A 1 169 ? 9.780 -6.153 4.494 1.00 37.62 ? 169 ALA A N 1 ATOM 1267 C CA . ALA A 1 169 ? 11.192 -6.483 4.530 1.00 38.54 ? 169 ALA A CA 1 ATOM 1268 C C . ALA A 1 169 ? 11.434 -7.723 5.384 1.00 39.17 ? 169 ALA A C 1 ATOM 1269 O O . ALA A 1 169 ? 10.902 -7.841 6.492 1.00 39.02 ? 169 ALA A O 1 ATOM 1270 C CB . ALA A 1 169 ? 11.998 -5.306 5.055 1.00 38.49 ? 169 ALA A CB 1 ATOM 1271 N N . PRO A 1 170 ? 12.236 -8.643 4.853 1.00 39.99 ? 170 PRO A N 1 ATOM 1272 C CA . PRO A 1 170 ? 12.648 -9.846 5.583 1.00 40.49 ? 170 PRO A CA 1 ATOM 1273 C C . PRO A 1 170 ? 13.455 -9.438 6.807 1.00 40.84 ? 170 PRO A C 1 ATOM 1274 O O . PRO A 1 170 ? 14.128 -8.413 6.779 1.00 40.86 ? 170 PRO A O 1 ATOM 1275 C CB . PRO A 1 170 ? 13.548 -10.568 4.573 1.00 40.47 ? 170 PRO A CB 1 ATOM 1276 C CG . PRO A 1 170 ? 14.013 -9.469 3.648 1.00 40.72 ? 170 PRO A CG 1 ATOM 1277 C CD . PRO A 1 170 ? 12.806 -8.596 3.495 1.00 40.12 ? 170 PRO A CD 1 ATOM 1278 N N . PRO A 1 171 ? 13.389 -10.226 7.872 1.00 41.39 ? 171 PRO A N 1 ATOM 1279 C CA . PRO A 1 171 ? 14.153 -9.942 9.091 1.00 41.44 ? 171 PRO A CA 1 ATOM 1280 C C . PRO A 1 171 ? 15.631 -9.783 8.769 1.00 41.23 ? 171 PRO A C 1 ATOM 1281 O O . PRO A 1 171 ? 16.160 -10.542 7.958 1.00 41.31 ? 171 PRO A O 1 ATOM 1282 C CB . PRO A 1 171 ? 13.918 -11.189 9.935 1.00 41.81 ? 171 PRO A CB 1 ATOM 1283 C CG . PRO A 1 171 ? 12.581 -11.663 9.485 1.00 42.05 ? 171 PRO A CG 1 ATOM 1284 C CD . PRO A 1 171 ? 12.578 -11.449 7.996 1.00 41.64 ? 171 PRO A CD 1 ATOM 1285 N N . GLY A 1 172 ? 16.281 -8.807 9.396 1.00 40.68 ? 172 GLY A N 1 ATOM 1286 C CA . GLY A 1 172 ? 17.693 -8.565 9.176 1.00 39.88 ? 172 GLY A CA 1 ATOM 1287 C C . GLY A 1 172 ? 18.020 -7.694 7.977 1.00 39.43 ? 172 GLY A C 1 ATOM 1288 O O . GLY A 1 172 ? 19.194 -7.380 7.733 1.00 39.24 ? 172 GLY A O 1 ATOM 1289 N N . TYR A 1 173 ? 16.996 -7.303 7.223 1.00 38.14 ? 173 TYR A N 1 ATOM 1290 C CA . TYR A 1 173 ? 17.196 -6.387 6.106 1.00 36.85 ? 173 TYR A CA 1 ATOM 1291 C C . TYR A 1 173 ? 17.800 -5.072 6.610 1.00 35.80 ? 173 TYR A C 1 ATOM 1292 O O . TYR A 1 173 ? 17.335 -4.523 7.595 1.00 35.90 ? 173 TYR A O 1 ATOM 1293 C CB . TYR A 1 173 ? 15.878 -6.101 5.391 1.00 36.65 ? 173 TYR A CB 1 ATOM 1294 C CG . TYR A 1 173 ? 16.053 -5.091 4.281 1.00 36.58 ? 173 TYR A CG 1 ATOM 1295 C CD1 . TYR A 1 173 ? 16.538 -5.486 3.037 1.00 36.19 ? 173 TYR A CD1 1 ATOM 1296 C CD2 . TYR A 1 173 ? 15.740 -3.747 4.474 1.00 35.18 ? 173 TYR A CD2 1 ATOM 1297 C CE1 . TYR A 1 173 ? 16.705 -4.574 2.014 1.00 35.21 ? 173 TYR A CE1 1 ATOM 1298 C CE2 . TYR A 1 173 ? 15.902 -2.827 3.459 1.00 34.09 ? 173 TYR A CE2 1 ATOM 1299 C CZ . TYR A 1 173 ? 16.386 -3.248 2.229 1.00 32.79 ? 173 TYR A CZ 1 ATOM 1300 O OH . TYR A 1 173 ? 16.555 -2.345 1.209 1.00 29.33 ? 173 TYR A OH 1 ATOM 1301 N N . ASP A 1 174 ? 18.830 -4.570 5.933 1.00 33.93 ? 174 ASP A N 1 ATOM 1302 C CA . ASP A 1 174 ? 19.510 -3.341 6.354 1.00 32.11 ? 174 ASP A CA 1 ATOM 1303 C C . ASP A 1 174 ? 18.952 -2.129 5.626 1.00 29.93 ? 174 ASP A C 1 ATOM 1304 O O . ASP A 1 174 ? 19.243 -1.908 4.451 1.00 28.93 ? 174 ASP A O 1 ATOM 1305 C CB . ASP A 1 174 ? 21.016 -3.456 6.103 1.00 33.37 ? 174 ASP A CB 1 ATOM 1306 C CG . ASP A 1 174 ? 21.818 -2.297 6.698 1.00 35.83 ? 174 ASP A CG 1 ATOM 1307 O OD1 . ASP A 1 174 ? 21.221 -1.360 7.273 1.00 36.83 ? 174 ASP A OD1 1 ATOM 1308 O OD2 . ASP A 1 174 ? 23.072 -2.248 6.633 1.00 38.67 ? 174 ASP A OD2 1 ATOM 1309 N N . TRP A 1 175 ? 18.148 -1.342 6.335 1.00 27.04 ? 175 TRP A N 1 ATOM 1310 C CA . TRP A 1 175 ? 17.464 -0.224 5.718 1.00 25.12 ? 175 TRP A CA 1 ATOM 1311 C C . TRP A 1 175 ? 18.409 0.889 5.347 1.00 24.77 ? 175 TRP A C 1 ATOM 1312 O O . TRP A 1 175 ? 18.058 1.740 4.546 1.00 23.46 ? 175 TRP A O 1 ATOM 1313 C CB . TRP A 1 175 ? 16.311 0.291 6.606 1.00 24.64 ? 175 TRP A CB 1 ATOM 1314 C CG . TRP A 1 175 ? 15.079 -0.509 6.418 1.00 21.65 ? 175 TRP A CG 1 ATOM 1315 C CD1 . TRP A 1 175 ? 14.604 -1.483 7.237 1.00 21.04 ? 175 TRP A CD1 1 ATOM 1316 C CD2 . TRP A 1 175 ? 14.156 -0.410 5.334 1.00 21.09 ? 175 TRP A CD2 1 ATOM 1317 N NE1 . TRP A 1 175 ? 13.436 -2.000 6.733 1.00 21.03 ? 175 TRP A NE1 1 ATOM 1318 C CE2 . TRP A 1 175 ? 13.138 -1.358 5.561 1.00 20.85 ? 175 TRP A CE2 1 ATOM 1319 C CE3 . TRP A 1 175 ? 14.085 0.388 4.187 1.00 19.12 ? 175 TRP A CE3 1 ATOM 1320 C CZ2 . TRP A 1 175 ? 12.069 -1.529 4.693 1.00 18.93 ? 175 TRP A CZ2 1 ATOM 1321 C CZ3 . TRP A 1 175 ? 13.027 0.218 3.325 1.00 18.70 ? 175 TRP A CZ3 1 ATOM 1322 C CH2 . TRP A 1 175 ? 12.030 -0.731 3.580 1.00 19.29 ? 175 TRP A CH2 1 ATOM 1323 N N . SER A 1 176 ? 19.611 0.890 5.926 1.00 24.71 ? 176 SER A N 1 ATOM 1324 C CA . SER A 1 176 ? 20.584 1.906 5.557 1.00 24.79 ? 176 SER A CA 1 ATOM 1325 C C . SER A 1 176 ? 21.058 1.730 4.127 1.00 24.59 ? 176 SER A C 1 ATOM 1326 O O . SER A 1 176 ? 21.703 2.618 3.582 1.00 23.98 ? 176 SER A O 1 ATOM 1327 C CB . SER A 1 176 ? 21.794 1.886 6.490 1.00 25.94 ? 176 SER A CB 1 ATOM 1328 O OG . SER A 1 176 ? 22.449 0.633 6.424 1.00 27.14 ? 176 SER A OG 1 ATOM 1329 N N . THR A 1 177 ? 20.742 0.587 3.518 1.00 23.86 ? 177 THR A N 1 ATOM 1330 C CA . THR A 1 177 ? 21.181 0.322 2.157 1.00 23.79 ? 177 THR A CA 1 ATOM 1331 C C . THR A 1 177 ? 20.021 0.480 1.198 1.00 23.07 ? 177 THR A C 1 ATOM 1332 O O . THR A 1 177 ? 20.154 0.223 0.008 1.00 22.96 ? 177 THR A O 1 ATOM 1333 C CB . THR A 1 177 ? 21.761 -1.098 2.042 1.00 23.80 ? 177 THR A CB 1 ATOM 1334 O OG1 . THR A 1 177 ? 20.710 -2.059 2.223 1.00 25.10 ? 177 THR A OG1 1 ATOM 1335 C CG2 . THR A 1 177 ? 22.698 -1.375 3.195 1.00 26.21 ? 177 THR A CG2 1 ATOM 1336 N N . SER A 1 178 ? 18.876 0.907 1.715 1.00 21.44 ? 178 SER A N 1 ATOM 1337 C CA . SER A 1 178 ? 17.696 1.026 0.875 1.00 20.39 ? 178 SER A CA 1 ATOM 1338 C C . SER A 1 178 ? 17.812 2.214 -0.049 1.00 19.56 ? 178 SER A C 1 ATOM 1339 O O . SER A 1 178 ? 18.643 3.095 0.151 1.00 19.13 ? 178 SER A O 1 ATOM 1340 C CB . SER A 1 178 ? 16.419 1.166 1.718 1.00 20.14 ? 178 SER A CB 1 ATOM 1341 O OG . SER A 1 178 ? 16.416 2.393 2.433 1.00 19.35 ? 178 SER A OG 1 ATOM 1342 N N . LYS A 1 179 ? 16.972 2.241 -1.067 1.00 18.82 ? 179 LYS A N 1 ATOM 1343 C CA . LYS A 1 179 ? 16.936 3.414 -1.922 1.00 19.76 ? 179 LYS A CA 1 ATOM 1344 C C . LYS A 1 179 ? 16.514 4.667 -1.155 1.00 18.73 ? 179 LYS A C 1 ATOM 1345 O O . LYS A 1 179 ? 17.017 5.754 -1.435 1.00 17.96 ? 179 LYS A O 1 ATOM 1346 C CB . LYS A 1 179 ? 16.011 3.193 -3.118 1.00 20.74 ? 179 LYS A CB 1 ATOM 1347 C CG . LYS A 1 179 ? 16.473 2.072 -4.060 1.00 25.06 ? 179 LYS A CG 1 ATOM 1348 C CD . LYS A 1 179 ? 17.649 2.498 -4.939 1.00 28.42 ? 179 LYS A CD 1 ATOM 1349 C CE . LYS A 1 179 ? 18.001 1.408 -5.953 1.00 30.56 ? 179 LYS A CE 1 ATOM 1350 N NZ . LYS A 1 179 ? 16.750 0.819 -6.533 1.00 31.34 ? 179 LYS A NZ 1 ATOM 1351 N N . SER A 1 180 ? 15.596 4.528 -0.190 1.00 17.77 ? 180 SER A N 1 ATOM 1352 C CA . SER A 1 180 ? 15.178 5.697 0.599 1.00 17.49 ? 180 SER A CA 1 ATOM 1353 C C . SER A 1 180 ? 16.385 6.301 1.324 1.00 17.56 ? 180 SER A C 1 ATOM 1354 O O . SER A 1 180 ? 16.601 7.514 1.296 1.00 16.46 ? 180 SER A O 1 ATOM 1355 C CB . SER A 1 180 ? 13.989 5.378 1.534 1.00 16.85 ? 180 SER A CB 1 ATOM 1356 O OG . SER A 1 180 ? 12.822 5.182 0.771 1.00 16.91 ? 180 SER A OG 1 ATOM 1357 N N . ALA A 1 181 ? 17.167 5.448 1.967 1.00 18.13 ? 181 ALA A N 1 ATOM 1358 C CA . ALA A 1 181 ? 18.358 5.917 2.647 1.00 18.74 ? 181 ALA A CA 1 ATOM 1359 C C . ALA A 1 181 ? 19.321 6.603 1.681 1.00 19.60 ? 181 ALA A C 1 ATOM 1360 O O . ALA A 1 181 ? 19.943 7.618 2.008 1.00 19.47 ? 181 ALA A O 1 ATOM 1361 C CB . ALA A 1 181 ? 19.037 4.759 3.359 1.00 19.39 ? 181 ALA A CB 1 ATOM 1362 N N . GLU A 1 182 ? 19.444 6.046 0.485 1.00 19.83 ? 182 GLU A N 1 ATOM 1363 C CA . GLU A 1 182 ? 20.300 6.636 -0.531 1.00 20.98 ? 182 GLU A CA 1 ATOM 1364 C C . GLU A 1 182 ? 19.821 8.026 -0.960 1.00 19.81 ? 182 GLU A C 1 ATOM 1365 O O . GLU A 1 182 ? 20.623 8.941 -1.122 1.00 19.21 ? 182 GLU A O 1 ATOM 1366 C CB . GLU A 1 182 ? 20.377 5.718 -1.747 1.00 21.08 ? 182 GLU A CB 1 ATOM 1367 C CG . GLU A 1 182 ? 21.719 5.787 -2.440 1.00 27.07 ? 182 GLU A CG 1 ATOM 1368 C CD . GLU A 1 182 ? 21.706 5.053 -3.764 1.00 30.50 ? 182 GLU A CD 1 ATOM 1369 O OE1 . GLU A 1 182 ? 21.990 5.690 -4.792 1.00 32.56 ? 182 GLU A OE1 1 ATOM 1370 O OE2 . GLU A 1 182 ? 21.410 3.842 -3.757 1.00 34.33 ? 182 GLU A OE2 1 ATOM 1371 N N . ARG A 1 183 ? 18.512 8.163 -1.140 1.00 19.63 ? 183 ARG A N 1 ATOM 1372 C CA . ARG A 1 183 ? 17.896 9.406 -1.626 1.00 19.17 ? 183 ARG A CA 1 ATOM 1373 C C . ARG A 1 183 ? 18.119 10.504 -0.619 1.00 18.48 ? 183 ARG A C 1 ATOM 1374 O O . ARG A 1 183 ? 18.469 11.636 -0.948 1.00 18.62 ? 183 ARG A O 1 ATOM 1375 C CB . ARG A 1 183 ? 16.368 9.245 -1.809 1.00 18.90 ? 183 ARG A CB 1 ATOM 1376 C CG . ARG A 1 183 ? 15.936 8.474 -3.045 1.00 19.16 ? 183 ARG A CG 1 ATOM 1377 C CD . ARG A 1 183 ? 14.432 8.464 -3.319 1.00 16.78 ? 183 ARG A CD 1 ATOM 1378 N NE . ARG A 1 183 ? 13.679 7.713 -2.319 1.00 16.66 ? 183 ARG A NE 1 ATOM 1379 C CZ . ARG A 1 183 ? 12.827 8.238 -1.429 1.00 14.86 ? 183 ARG A CZ 1 ATOM 1380 N NH1 . ARG A 1 183 ? 12.586 9.537 -1.381 1.00 14.16 ? 183 ARG A NH1 1 ATOM 1381 N NH2 . ARG A 1 183 ? 12.214 7.446 -0.585 1.00 15.11 ? 183 ARG A NH2 1 ATOM 1382 N N . PHE A 1 184 ? 17.901 10.154 0.633 1.00 18.14 ? 184 PHE A N 1 ATOM 1383 C CA . PHE A 1 184 ? 18.137 11.101 1.694 1.00 17.23 ? 184 PHE A CA 1 ATOM 1384 C C . PHE A 1 184 ? 19.601 11.327 1.949 1.00 16.81 ? 184 PHE A C 1 ATOM 1385 O O . PHE A 1 184 ? 20.025 12.451 2.210 1.00 16.67 ? 184 PHE A O 1 ATOM 1386 C CB . PHE A 1 184 ? 17.314 10.710 2.930 1.00 17.26 ? 184 PHE A CB 1 ATOM 1387 C CG . PHE A 1 184 ? 15.867 11.047 2.763 1.00 17.56 ? 184 PHE A CG 1 ATOM 1388 C CD1 . PHE A 1 184 ? 15.386 12.285 3.162 1.00 18.35 ? 184 PHE A CD1 1 ATOM 1389 C CD2 . PHE A 1 184 ? 14.985 10.134 2.200 1.00 17.83 ? 184 PHE A CD2 1 ATOM 1390 C CE1 . PHE A 1 184 ? 14.060 12.603 3.006 1.00 17.37 ? 184 PHE A CE1 1 ATOM 1391 C CE2 . PHE A 1 184 ? 13.657 10.455 2.047 1.00 18.56 ? 184 PHE A CE2 1 ATOM 1392 C CZ . PHE A 1 184 ? 13.199 11.686 2.450 1.00 17.84 ? 184 PHE A CZ 1 ATOM 1393 N N . GLY A 1 185 ? 20.389 10.263 1.868 1.00 16.98 ? 185 GLY A N 1 ATOM 1394 C CA . GLY A 1 185 ? 21.818 10.404 2.087 1.00 16.55 ? 185 GLY A CA 1 ATOM 1395 C C . GLY A 1 185 ? 22.460 11.291 1.042 1.00 16.79 ? 185 GLY A C 1 ATOM 1396 O O . GLY A 1 185 ? 23.420 11.996 1.327 1.00 16.31 ? 185 GLY A O 1 ATOM 1397 N N . ALA A 1 186 ? 21.925 11.255 -0.174 1.00 16.93 ? 186 ALA A N 1 ATOM 1398 C CA . ALA A 1 186 ? 22.478 12.041 -1.258 1.00 17.26 ? 186 ALA A CA 1 ATOM 1399 C C . ALA A 1 186 ? 22.341 13.544 -0.963 1.00 17.26 ? 186 ALA A C 1 ATOM 1400 O O . ALA A 1 186 ? 23.206 14.340 -1.338 1.00 15.85 ? 186 ALA A O 1 ATOM 1401 C CB . ALA A 1 186 ? 21.805 11.689 -2.565 1.00 18.11 ? 186 ALA A CB 1 ATOM 1402 N N . MET A 1 187 ? 21.260 13.936 -0.296 1.00 16.27 ? 187 MET A N 1 ATOM 1403 C CA . MET A 1 187 ? 21.102 15.346 0.034 1.00 15.69 ? 187 MET A CA 1 ATOM 1404 C C . MET A 1 187 ? 21.937 15.675 1.269 1.00 15.60 ? 187 MET A C 1 ATOM 1405 O O . MET A 1 187 ? 22.478 16.768 1.367 1.00 15.44 ? 187 MET A O 1 ATOM 1406 C CB . MET A 1 187 ? 19.621 15.712 0.217 1.00 15.36 ? 187 MET A CB 1 ATOM 1407 C CG . MET A 1 187 ? 19.403 17.150 0.607 1.00 15.65 ? 187 MET A CG 1 ATOM 1408 S SD . MET A 1 187 ? 20.064 18.333 -0.573 1.00 18.59 ? 187 MET A SD 1 ATOM 1409 C CE . MET A 1 187 ? 18.734 18.351 -1.829 1.00 15.17 ? 187 MET A CE 1 ATOM 1410 N N . ARG A 1 188 ? 22.032 14.730 2.208 1.00 15.10 ? 188 ARG A N 1 ATOM 1411 C CA . ARG A 1 188 ? 22.947 14.895 3.346 1.00 16.49 ? 188 ARG A CA 1 ATOM 1412 C C . ARG A 1 188 ? 24.332 15.227 2.771 1.00 17.50 ? 188 ARG A C 1 ATOM 1413 O O . ARG A 1 188 ? 24.939 16.241 3.123 1.00 18.02 ? 188 ARG A O 1 ATOM 1414 C CB . ARG A 1 188 ? 23.045 13.621 4.174 1.00 16.35 ? 188 ARG A CB 1 ATOM 1415 C CG . ARG A 1 188 ? 24.262 13.570 5.144 1.00 16.25 ? 188 ARG A CG 1 ATOM 1416 C CD . ARG A 1 188 ? 24.666 12.171 5.600 1.00 19.79 ? 188 ARG A CD 1 ATOM 1417 N NE . ARG A 1 188 ? 25.071 11.343 4.463 1.00 20.60 ? 188 ARG A NE 1 ATOM 1418 C CZ . ARG A 1 188 ? 24.794 10.051 4.332 1.00 23.67 ? 188 ARG A CZ 1 ATOM 1419 N NH1 . ARG A 1 188 ? 24.101 9.418 5.277 1.00 24.93 ? 188 ARG A NH1 1 ATOM 1420 N NH2 . ARG A 1 188 ? 25.212 9.383 3.245 1.00 22.33 ? 188 ARG A NH2 1 ATOM 1421 N N . ASN A 1 189 ? 24.818 14.362 1.886 1.00 17.75 ? 189 ASN A N 1 ATOM 1422 C CA . ASN A 1 189 ? 26.178 14.539 1.309 1.00 18.49 ? 189 ASN A CA 1 ATOM 1423 C C . ASN A 1 189 ? 26.331 15.843 0.554 1.00 18.30 ? 189 ASN A C 1 ATOM 1424 O O . ASN A 1 189 ? 27.354 16.497 0.642 1.00 18.25 ? 189 ASN A O 1 ATOM 1425 C CB . ASN A 1 189 ? 26.526 13.391 0.368 1.00 18.75 ? 189 ASN A CB 1 ATOM 1426 C CG . ASN A 1 189 ? 26.587 12.078 1.078 1.00 17.66 ? 189 ASN A CG 1 ATOM 1427 O OD1 . ASN A 1 189 ? 26.774 12.036 2.285 1.00 19.91 ? 189 ASN A OD1 1 ATOM 1428 N ND2 . ASN A 1 189 ? 26.431 10.994 0.339 1.00 23.06 ? 189 ASN A ND2 1 ATOM 1429 N N . ALA A 1 190 ? 25.305 16.222 -0.195 1.00 17.33 ? 190 ALA A N 1 ATOM 1430 C CA . ALA A 1 190 ? 25.357 17.480 -0.940 1.00 17.68 ? 190 ALA A CA 1 ATOM 1431 C C . ALA A 1 190 ? 25.443 18.695 -0.014 1.00 17.19 ? 190 ALA A C 1 ATOM 1432 O O . ALA A 1 190 ? 26.251 19.592 -0.242 1.00 17.24 ? 190 ALA A O 1 ATOM 1433 C CB . ALA A 1 190 ? 24.135 17.594 -1.897 1.00 17.30 ? 190 ALA A CB 1 ATOM 1434 N N . LEU A 1 191 ? 24.610 18.726 1.029 1.00 17.03 ? 191 LEU A N 1 ATOM 1435 C CA . LEU A 1 191 ? 24.641 19.839 1.985 1.00 17.18 ? 191 LEU A CA 1 ATOM 1436 C C . LEU A 1 191 ? 25.947 19.965 2.739 1.00 17.79 ? 191 LEU A C 1 ATOM 1437 O O . LEU A 1 191 ? 26.412 21.077 3.002 1.00 17.45 ? 191 LEU A O 1 ATOM 1438 C CB . LEU A 1 191 ? 23.520 19.696 3.025 1.00 17.26 ? 191 LEU A CB 1 ATOM 1439 C CG . LEU A 1 191 ? 22.080 19.736 2.502 1.00 16.50 ? 191 LEU A CG 1 ATOM 1440 C CD1 . LEU A 1 191 ? 21.142 19.271 3.606 1.00 17.46 ? 191 LEU A CD1 1 ATOM 1441 C CD2 . LEU A 1 191 ? 21.699 21.128 2.045 1.00 15.69 ? 191 LEU A CD2 1 ATOM 1442 N N . ALA A 1 192 ? 26.517 18.818 3.084 1.00 18.43 ? 192 ALA A N 1 ATOM 1443 C CA . ALA A 1 192 ? 27.727 18.740 3.878 1.00 19.74 ? 192 ALA A CA 1 ATOM 1444 C C . ALA A 1 192 ? 28.903 19.449 3.224 1.00 20.19 ? 192 ALA A C 1 ATOM 1445 O O . ALA A 1 192 ? 29.817 19.916 3.913 1.00 20.42 ? 192 ALA A O 1 ATOM 1446 C CB . ALA A 1 192 ? 28.077 17.274 4.144 1.00 20.13 ? 192 ALA A CB 1 ATOM 1447 N N . LYS A 1 193 ? 28.887 19.532 1.900 1.00 20.56 ? 193 LYS A N 1 ATOM 1448 C CA . LYS A 1 193 ? 29.997 20.154 1.182 1.00 21.44 ? 193 LYS A CA 1 ATOM 1449 C C . LYS A 1 193 ? 29.884 21.662 1.084 1.00 22.42 ? 193 LYS A C 1 ATOM 1450 O O . LYS A 1 193 ? 30.862 22.316 0.700 1.00 22.79 ? 193 LYS A O 1 ATOM 1451 C CB . LYS A 1 193 ? 30.070 19.635 -0.244 1.00 21.28 ? 193 LYS A CB 1 ATOM 1452 C CG . LYS A 1 193 ? 30.281 18.164 -0.378 1.00 21.57 ? 193 LYS A CG 1 ATOM 1453 C CD . LYS A 1 193 ? 30.301 17.799 -1.845 1.00 22.04 ? 193 LYS A CD 1 ATOM 1454 C CE . LYS A 1 193 ? 30.872 16.430 -2.010 1.00 22.96 ? 193 LYS A CE 1 ATOM 1455 N NZ . LYS A 1 193 ? 30.862 16.005 -3.396 1.00 22.72 ? 193 LYS A NZ 1 ATOM 1456 N N . GLN A 1 194 ? 28.729 22.223 1.413 1.00 21.98 ? 194 GLN A N 1 ATOM 1457 C CA . GLN A 1 194 ? 28.560 23.663 1.294 1.00 22.98 ? 194 GLN A CA 1 ATOM 1458 C C . GLN A 1 194 ? 29.098 24.353 2.537 1.00 23.45 ? 194 GLN A C 1 ATOM 1459 O O . GLN A 1 194 ? 29.180 23.738 3.585 1.00 23.62 ? 194 GLN A O 1 ATOM 1460 C CB . GLN A 1 194 ? 27.072 23.992 1.075 1.00 22.99 ? 194 GLN A CB 1 ATOM 1461 C CG . GLN A 1 194 ? 26.375 23.045 0.111 1.00 23.54 ? 194 GLN A CG 1 ATOM 1462 C CD . GLN A 1 194 ? 26.999 23.047 -1.265 1.00 26.08 ? 194 GLN A CD 1 ATOM 1463 O OE1 . GLN A 1 194 ? 27.031 22.013 -1.932 1.00 26.82 ? 194 GLN A OE1 1 ATOM 1464 N NE2 . GLN A 1 194 ? 27.497 24.202 -1.697 1.00 26.65 ? 194 GLN A NE2 1 ATOM 1465 N N . SER A 1 195 ? 29.459 25.625 2.432 1.00 24.70 ? 195 SER A N 1 ATOM 1466 C CA . SER A 1 195 ? 30.071 26.314 3.576 1.00 26.80 ? 195 SER A CA 1 ATOM 1467 C C . SER A 1 195 ? 29.030 26.741 4.610 1.00 26.75 ? 195 SER A C 1 ATOM 1468 O O . SER A 1 195 ? 29.331 26.861 5.796 1.00 27.77 ? 195 SER A O 1 ATOM 1469 C CB . SER A 1 195 ? 30.898 27.526 3.118 1.00 27.09 ? 195 SER A CB 1 ATOM 1470 O OG . SER A 1 195 ? 30.129 28.335 2.240 1.00 31.09 ? 195 SER A OG 1 ATOM 1471 N N . HIS A 1 196 ? 27.804 26.969 4.156 1.00 26.15 ? 196 HIS A N 1 ATOM 1472 C CA . HIS A 1 196 ? 26.759 27.450 5.044 1.00 26.20 ? 196 HIS A CA 1 ATOM 1473 C C . HIS A 1 196 ? 26.035 26.202 5.536 1.00 25.56 ? 196 HIS A C 1 ATOM 1474 O O . HIS A 1 196 ? 25.600 25.376 4.739 1.00 25.44 ? 196 HIS A O 1 ATOM 1475 C CB . HIS A 1 196 ? 25.848 28.436 4.292 1.00 26.10 ? 196 HIS A CB 1 ATOM 1476 C CG . HIS A 1 196 ? 24.810 29.091 5.151 1.00 28.31 ? 196 HIS A CG 1 ATOM 1477 N ND1 . HIS A 1 196 ? 25.082 30.175 5.961 1.00 28.94 ? 196 HIS A ND1 1 ATOM 1478 C CD2 . HIS A 1 196 ? 23.496 28.813 5.324 1.00 28.86 ? 196 HIS A CD2 1 ATOM 1479 C CE1 . HIS A 1 196 ? 23.977 30.535 6.596 1.00 30.75 ? 196 HIS A CE1 1 ATOM 1480 N NE2 . HIS A 1 196 ? 23.001 29.723 6.227 1.00 30.12 ? 196 HIS A NE2 1 ATOM 1481 N N . GLU A 1 197 ? 25.909 26.067 6.848 1.00 25.04 ? 197 GLU A N 1 ATOM 1482 C CA . GLU A 1 197 ? 25.428 24.834 7.427 1.00 25.25 ? 197 GLU A CA 1 ATOM 1483 C C . GLU A 1 197 ? 23.920 24.768 7.335 1.00 24.13 ? 197 GLU A C 1 ATOM 1484 O O . GLU A 1 197 ? 23.223 25.701 7.743 1.00 24.32 ? 197 GLU A O 1 ATOM 1485 C CB . GLU A 1 197 ? 25.868 24.724 8.879 1.00 26.09 ? 197 GLU A CB 1 ATOM 1486 C CG . GLU A 1 197 ? 25.411 25.899 9.740 1.00 30.94 ? 197 GLU A CG 1 ATOM 1487 C CD . GLU A 1 197 ? 24.442 25.530 10.846 1.00 37.13 ? 197 GLU A CD 1 ATOM 1488 O OE1 . GLU A 1 197 ? 23.288 25.137 10.543 1.00 40.93 ? 197 GLU A OE1 1 ATOM 1489 O OE2 . GLU A 1 197 ? 24.838 25.641 12.031 1.00 39.80 ? 197 GLU A OE2 1 ATOM 1490 N N . ILE A 1 198 ? 23.417 23.664 6.797 1.00 22.21 ? 198 ILE A N 1 ATOM 1491 C CA . ILE A 1 198 ? 21.980 23.486 6.705 1.00 20.85 ? 198 ILE A CA 1 ATOM 1492 C C . ILE A 1 198 ? 21.623 22.164 7.365 1.00 19.88 ? 198 ILE A C 1 ATOM 1493 O O . ILE A 1 198 ? 22.228 21.129 7.062 1.00 19.97 ? 198 ILE A O 1 ATOM 1494 C CB . ILE A 1 198 ? 21.495 23.483 5.242 1.00 20.86 ? 198 ILE A CB 1 ATOM 1495 C CG1 . ILE A 1 198 ? 21.736 24.844 4.583 1.00 21.39 ? 198 ILE A CG1 1 ATOM 1496 C CG2 . ILE A 1 198 ? 20.017 23.126 5.214 1.00 19.18 ? 198 ILE A CG2 1 ATOM 1497 C CD1 . ILE A 1 198 ? 21.578 24.832 3.080 1.00 22.05 ? 198 ILE A CD1 1 ATOM 1498 N N . VAL A 1 199 ? 20.649 22.198 8.265 1.00 18.11 ? 199 VAL A N 1 ATOM 1499 C CA . VAL A 1 199 ? 20.197 20.973 8.890 1.00 16.97 ? 199 VAL A CA 1 ATOM 1500 C C . VAL A 1 199 ? 19.182 20.277 7.991 1.00 16.84 ? 199 VAL A C 1 ATOM 1501 O O . VAL A 1 199 ? 18.441 20.913 7.258 1.00 16.53 ? 199 VAL A O 1 ATOM 1502 C CB . VAL A 1 199 ? 19.669 21.196 10.331 1.00 16.61 ? 199 VAL A CB 1 ATOM 1503 C CG1 . VAL A 1 199 ? 20.803 21.714 11.215 1.00 16.26 ? 199 VAL A CG1 1 ATOM 1504 C CG2 . VAL A 1 199 ? 18.502 22.170 10.361 1.00 15.66 ? 199 VAL A CG2 1 ATOM 1505 N N . LEU A 1 200 ? 19.163 18.957 8.060 1.00 16.88 ? 200 LEU A N 1 ATOM 1506 C CA . LEU A 1 200 ? 18.274 18.196 7.226 1.00 16.83 ? 200 LEU A CA 1 ATOM 1507 C C . LEU A 1 200 ? 17.183 17.557 8.044 1.00 16.69 ? 200 LEU A C 1 ATOM 1508 O O . LEU A 1 200 ? 17.452 16.812 8.983 1.00 15.59 ? 200 LEU A O 1 ATOM 1509 C CB . LEU A 1 200 ? 19.047 17.143 6.452 1.00 17.30 ? 200 LEU A CB 1 ATOM 1510 C CG . LEU A 1 200 ? 18.227 16.236 5.545 1.00 18.54 ? 200 LEU A CG 1 ATOM 1511 C CD1 . LEU A 1 200 ? 17.621 17.031 4.371 1.00 18.69 ? 200 LEU A CD1 1 ATOM 1512 C CD2 . LEU A 1 200 ? 19.160 15.109 5.038 1.00 19.39 ? 200 LEU A CD2 1 ATOM 1513 N N . SER A 1 201 ? 15.948 17.869 7.661 1.00 16.52 ? 201 SER A N 1 ATOM 1514 C CA . SER A 1 201 ? 14.760 17.321 8.288 1.00 16.30 ? 201 SER A CA 1 ATOM 1515 C C . SER A 1 201 ? 14.186 16.389 7.241 1.00 16.36 ? 201 SER A C 1 ATOM 1516 O O . SER A 1 201 ? 13.911 16.797 6.111 1.00 17.19 ? 201 SER A O 1 ATOM 1517 C CB . SER A 1 201 ? 13.770 18.439 8.637 1.00 16.75 ? 201 SER A CB 1 ATOM 1518 O OG . SER A 1 201 ? 12.429 17.981 8.561 1.00 16.73 ? 201 SER A OG 1 ATOM 1519 N N . MET A 1 202 ? 14.010 15.139 7.620 1.00 15.84 ? 202 MET A N 1 ATOM 1520 C CA . MET A 1 202 ? 13.705 14.101 6.668 1.00 16.51 ? 202 MET A CA 1 ATOM 1521 C C . MET A 1 202 ? 12.218 13.824 6.721 1.00 15.59 ? 202 MET A C 1 ATOM 1522 O O . MET A 1 202 ? 11.730 13.077 7.567 1.00 16.09 ? 202 MET A O 1 ATOM 1523 C CB . MET A 1 202 ? 14.524 12.864 7.015 1.00 15.99 ? 202 MET A CB 1 ATOM 1524 C CG . MET A 1 202 ? 16.047 13.098 6.855 1.00 21.18 ? 202 MET A CG 1 ATOM 1525 S SD . MET A 1 202 ? 16.905 11.741 7.682 1.00 26.65 ? 202 MET A SD 1 ATOM 1526 C CE . MET A 1 202 ? 16.615 10.544 6.495 1.00 25.12 ? 202 MET A CE 1 ATOM 1527 N N . CYS A 1 203 ? 11.497 14.443 5.804 1.00 15.14 ? 203 CYS A N 1 ATOM 1528 C CA . CYS A 1 203 ? 10.059 14.263 5.798 1.00 15.06 ? 203 CYS A CA 1 ATOM 1529 C C . CYS A 1 203 ? 9.743 12.974 5.064 1.00 14.74 ? 203 CYS A C 1 ATOM 1530 O O . CYS A 1 203 ? 9.413 12.988 3.886 1.00 14.22 ? 203 CYS A O 1 ATOM 1531 C CB . CYS A 1 203 ? 9.371 15.453 5.133 1.00 15.06 ? 203 CYS A CB 1 ATOM 1532 S SG . CYS A 1 203 ? 7.591 15.345 5.352 1.00 15.38 ? 203 CYS A SG 1 ATOM 1533 N N . ILE A 1 204 ? 9.847 11.862 5.777 1.00 14.74 ? 204 ILE A N 1 ATOM 1534 C CA . ILE A 1 204 ? 9.694 10.566 5.156 1.00 15.35 ? 204 ILE A CA 1 ATOM 1535 C C . ILE A 1 204 ? 8.473 9.775 5.660 1.00 15.28 ? 204 ILE A C 1 ATOM 1536 O O . ILE A 1 204 ? 8.234 8.641 5.231 1.00 15.31 ? 204 ILE A O 1 ATOM 1537 C CB . ILE A 1 204 ? 11.013 9.778 5.319 1.00 15.42 ? 204 ILE A CB 1 ATOM 1538 C CG1 . ILE A 1 204 ? 11.084 8.614 4.340 1.00 15.98 ? 204 ILE A CG1 1 ATOM 1539 C CG2 . ILE A 1 204 ? 11.216 9.338 6.777 1.00 13.94 ? 204 ILE A CG2 1 ATOM 1540 C CD1 . ILE A 1 204 ? 12.463 7.953 4.354 1.00 18.28 ? 204 ILE A CD1 1 ATOM 1541 N N . TRP A 1 205 ? 7.713 10.387 6.563 1.00 14.95 ? 205 TRP A N 1 ATOM 1542 C CA . TRP A 1 205 ? 6.430 9.842 7.022 1.00 15.53 ? 205 TRP A CA 1 ATOM 1543 C C . TRP A 1 205 ? 6.581 8.517 7.747 1.00 15.77 ? 205 TRP A C 1 ATOM 1544 O O . TRP A 1 205 ? 5.665 7.697 7.747 1.00 15.32 ? 205 TRP A O 1 ATOM 1545 C CB . TRP A 1 205 ? 5.422 9.668 5.865 1.00 15.74 ? 205 TRP A CB 1 ATOM 1546 C CG . TRP A 1 205 ? 5.409 10.723 4.779 1.00 15.57 ? 205 TRP A CG 1 ATOM 1547 C CD1 . TRP A 1 205 ? 5.451 12.075 4.941 1.00 17.70 ? 205 TRP A CD1 1 ATOM 1548 C CD2 . TRP A 1 205 ? 5.345 10.499 3.354 1.00 16.78 ? 205 TRP A CD2 1 ATOM 1549 N NE1 . TRP A 1 205 ? 5.418 12.704 3.716 1.00 15.92 ? 205 TRP A NE1 1 ATOM 1550 C CE2 . TRP A 1 205 ? 5.354 11.760 2.726 1.00 16.63 ? 205 TRP A CE2 1 ATOM 1551 C CE3 . TRP A 1 205 ? 5.283 9.360 2.552 1.00 16.42 ? 205 TRP A CE3 1 ATOM 1552 C CZ2 . TRP A 1 205 ? 5.298 11.911 1.339 1.00 16.70 ? 205 TRP A CZ2 1 ATOM 1553 C CZ3 . TRP A 1 205 ? 5.232 9.508 1.174 1.00 17.67 ? 205 TRP A CZ3 1 ATOM 1554 C CH2 . TRP A 1 205 ? 5.239 10.774 0.583 1.00 19.55 ? 205 TRP A CH2 1 ATOM 1555 N N . GLY A 1 206 ? 7.746 8.318 8.363 1.00 15.70 ? 206 GLY A N 1 ATOM 1556 C CA . GLY A 1 206 ? 8.004 7.097 9.092 1.00 16.30 ? 206 GLY A CA 1 ATOM 1557 C C . GLY A 1 206 ? 8.253 5.917 8.192 1.00 15.99 ? 206 GLY A C 1 ATOM 1558 O O . GLY A 1 206 ? 8.241 4.797 8.653 1.00 17.00 ? 206 GLY A O 1 ATOM 1559 N N . GLN A 1 207 ? 8.473 6.158 6.910 1.00 16.26 ? 207 GLN A N 1 ATOM 1560 C CA . GLN A 1 207 ? 8.748 5.060 5.994 1.00 16.00 ? 207 GLN A CA 1 ATOM 1561 C C . GLN A 1 207 ? 10.184 4.547 6.096 1.00 16.62 ? 207 GLN A C 1 ATOM 1562 O O . GLN A 1 207 ? 11.063 5.195 6.677 1.00 15.48 ? 207 GLN A O 1 ATOM 1563 C CB . GLN A 1 207 ? 8.476 5.480 4.555 1.00 17.07 ? 207 GLN A CB 1 ATOM 1564 C CG . GLN A 1 207 ? 7.016 5.775 4.261 1.00 15.74 ? 207 GLN A CG 1 ATOM 1565 C CD . GLN A 1 207 ? 6.137 4.534 4.228 1.00 19.65 ? 207 GLN A CD 1 ATOM 1566 O OE1 . GLN A 1 207 ? 6.012 3.818 5.227 1.00 19.59 ? 207 GLN A OE1 1 ATOM 1567 N NE2 . GLN A 1 207 ? 5.522 4.276 3.073 1.00 19.50 ? 207 GLN A NE2 1 ATOM 1568 N N . ALA A 1 208 ? 10.384 3.368 5.517 1.00 16.82 ? 208 ALA A N 1 ATOM 1569 C CA . ALA A 1 208 ? 11.701 2.840 5.241 1.00 17.68 ? 208 ALA A CA 1 ATOM 1570 C C . ALA A 1 208 ? 12.494 2.627 6.505 1.00 18.29 ? 208 ALA A C 1 ATOM 1571 O O . ALA A 1 208 ? 13.720 2.670 6.502 1.00 18.98 ? 208 ALA A O 1 ATOM 1572 C CB . ALA A 1 208 ? 12.446 3.791 4.291 1.00 17.63 ? 208 ALA A CB 1 ATOM 1573 N N . ASP A 1 209 ? 11.785 2.399 7.596 1.00 18.96 ? 209 ASP A N 1 ATOM 1574 C CA . ASP A 1 209 ? 12.434 2.241 8.890 1.00 20.12 ? 209 ASP A CA 1 ATOM 1575 C C . ASP A 1 209 ? 13.495 3.318 9.134 1.00 19.34 ? 209 ASP A C 1 ATOM 1576 O O . ASP A 1 209 ? 14.627 3.031 9.469 1.00 20.60 ? 209 ASP A O 1 ATOM 1577 C CB . ASP A 1 209 ? 13.018 0.832 9.038 1.00 20.50 ? 209 ASP A CB 1 ATOM 1578 C CG . ASP A 1 209 ? 13.535 0.560 10.447 1.00 23.40 ? 209 ASP A CG 1 ATOM 1579 O OD1 . ASP A 1 209 ? 12.956 1.083 11.419 1.00 22.99 ? 209 ASP A OD1 1 ATOM 1580 O OD2 . ASP A 1 209 ? 14.520 -0.167 10.670 1.00 27.32 ? 209 ASP A OD2 1 ATOM 1581 N N . VAL A 1 210 ? 13.113 4.571 8.967 1.00 18.52 ? 210 VAL A N 1 ATOM 1582 C CA . VAL A 1 210 ? 14.042 5.676 9.090 1.00 17.66 ? 210 VAL A CA 1 ATOM 1583 C C . VAL A 1 210 ? 14.596 5.771 10.500 1.00 18.11 ? 210 VAL A C 1 ATOM 1584 O O . VAL A 1 210 ? 15.668 6.340 10.725 1.00 17.29 ? 210 VAL A O 1 ATOM 1585 C CB . VAL A 1 210 ? 13.356 7.002 8.746 1.00 17.98 ? 210 VAL A CB 1 ATOM 1586 C CG1 . VAL A 1 210 ? 12.199 7.259 9.717 1.00 17.52 ? 210 VAL A CG1 1 ATOM 1587 C CG2 . VAL A 1 210 ? 14.394 8.148 8.721 1.00 17.25 ? 210 VAL A CG2 1 ATOM 1588 N N . PHE A 1 211 ? 13.862 5.209 11.452 1.00 18.59 ? 211 PHE A N 1 ATOM 1589 C CA . PHE A 1 211 ? 14.303 5.195 12.838 1.00 19.73 ? 211 PHE A CA 1 ATOM 1590 C C . PHE A 1 211 ? 15.675 4.571 12.989 1.00 20.74 ? 211 PHE A C 1 ATOM 1591 O O . PHE A 1 211 ? 16.436 4.952 13.879 1.00 20.74 ? 211 PHE A O 1 ATOM 1592 C CB . PHE A 1 211 ? 13.292 4.423 13.697 1.00 19.57 ? 211 PHE A CB 1 ATOM 1593 C CG . PHE A 1 211 ? 11.877 4.884 13.481 1.00 19.78 ? 211 PHE A CG 1 ATOM 1594 C CD1 . PHE A 1 211 ? 11.396 5.995 14.153 1.00 20.28 ? 211 PHE A CD1 1 ATOM 1595 C CD2 . PHE A 1 211 ? 11.038 4.210 12.604 1.00 18.60 ? 211 PHE A CD2 1 ATOM 1596 C CE1 . PHE A 1 211 ? 10.111 6.419 13.956 1.00 17.25 ? 211 PHE A CE1 1 ATOM 1597 C CE2 . PHE A 1 211 ? 9.756 4.622 12.398 1.00 21.64 ? 211 PHE A CE2 1 ATOM 1598 C CZ . PHE A 1 211 ? 9.287 5.731 13.076 1.00 19.44 ? 211 PHE A CZ 1 ATOM 1599 N N . SER A 1 212 ? 15.998 3.614 12.129 1.00 21.66 ? 212 SER A N 1 ATOM 1600 C CA . SER A 1 212 ? 17.258 2.890 12.320 1.00 22.70 ? 212 SER A CA 1 ATOM 1601 C C . SER A 1 212 ? 18.445 3.564 11.648 1.00 22.32 ? 212 SER A C 1 ATOM 1602 O O . SER A 1 212 ? 19.574 3.397 12.072 1.00 23.15 ? 212 SER A O 1 ATOM 1603 C CB . SER A 1 212 ? 17.120 1.442 11.840 1.00 23.06 ? 212 SER A CB 1 ATOM 1604 O OG . SER A 1 212 ? 16.877 1.410 10.453 1.00 23.88 ? 212 SER A OG 1 ATOM 1605 N N . TRP A 1 213 ? 18.207 4.335 10.597 1.00 21.81 ? 213 TRP A N 1 ATOM 1606 C CA . TRP A 1 213 ? 19.326 4.992 9.941 1.00 20.96 ? 213 TRP A CA 1 ATOM 1607 C C . TRP A 1 213 ? 19.245 6.510 9.888 1.00 19.98 ? 213 TRP A C 1 ATOM 1608 O O . TRP A 1 213 ? 20.135 7.154 9.360 1.00 19.96 ? 213 TRP A O 1 ATOM 1609 C CB . TRP A 1 213 ? 19.480 4.440 8.531 1.00 21.32 ? 213 TRP A CB 1 ATOM 1610 C CG . TRP A 1 213 ? 18.217 4.481 7.779 1.00 21.62 ? 213 TRP A CG 1 ATOM 1611 C CD1 . TRP A 1 213 ? 17.267 3.510 7.727 1.00 21.37 ? 213 TRP A CD1 1 ATOM 1612 C CD2 . TRP A 1 213 ? 17.743 5.552 6.956 1.00 20.26 ? 213 TRP A CD2 1 ATOM 1613 N NE1 . TRP A 1 213 ? 16.231 3.907 6.923 1.00 19.57 ? 213 TRP A NE1 1 ATOM 1614 C CE2 . TRP A 1 213 ? 16.499 5.158 6.435 1.00 19.55 ? 213 TRP A CE2 1 ATOM 1615 C CE3 . TRP A 1 213 ? 18.248 6.808 6.605 1.00 19.90 ? 213 TRP A CE3 1 ATOM 1616 C CZ2 . TRP A 1 213 ? 15.751 5.969 5.586 1.00 18.67 ? 213 TRP A CZ2 1 ATOM 1617 C CZ3 . TRP A 1 213 ? 17.506 7.613 5.765 1.00 19.52 ? 213 TRP A CZ3 1 ATOM 1618 C CH2 . TRP A 1 213 ? 16.274 7.191 5.264 1.00 20.19 ? 213 TRP A CH2 1 ATOM 1619 N N . GLY A 1 214 ? 18.186 7.096 10.430 1.00 19.48 ? 214 GLY A N 1 ATOM 1620 C CA . GLY A 1 214 ? 17.978 8.521 10.228 1.00 18.37 ? 214 GLY A CA 1 ATOM 1621 C C . GLY A 1 214 ? 19.056 9.349 10.883 1.00 18.05 ? 214 GLY A C 1 ATOM 1622 O O . GLY A 1 214 ? 19.490 10.374 10.384 1.00 17.56 ? 214 GLY A O 1 ATOM 1623 N N . ASN A 1 215 ? 19.495 8.881 12.036 1.00 18.16 ? 215 ASN A N 1 ATOM 1624 C CA . ASN A 1 215 ? 20.542 9.568 12.763 1.00 19.01 ? 215 ASN A CA 1 ATOM 1625 C C . ASN A 1 215 ? 21.875 9.645 11.997 1.00 19.57 ? 215 ASN A C 1 ATOM 1626 O O . ASN A 1 215 ? 22.721 10.459 12.324 1.00 20.50 ? 215 ASN A O 1 ATOM 1627 C CB . ASN A 1 215 ? 20.736 8.916 14.122 1.00 18.53 ? 215 ASN A CB 1 ATOM 1628 C CG . ASN A 1 215 ? 21.408 9.832 15.119 1.00 20.17 ? 215 ASN A CG 1 ATOM 1629 O OD1 . ASN A 1 215 ? 21.323 11.063 15.021 1.00 19.91 ? 215 ASN A OD1 1 ATOM 1630 N ND2 . ASN A 1 215 ? 22.085 9.229 16.095 1.00 22.05 ? 215 ASN A ND2 1 ATOM 1631 N N . SER A 1 216 ? 22.064 8.810 10.987 1.00 19.99 ? 216 SER A N 1 ATOM 1632 C CA . SER A 1 216 ? 23.289 8.906 10.188 1.00 21.35 ? 216 SER A CA 1 ATOM 1633 C C . SER A 1 216 ? 23.067 9.886 9.042 1.00 20.98 ? 216 SER A C 1 ATOM 1634 O O . SER A 1 216 ? 23.964 10.149 8.257 1.00 21.67 ? 216 SER A O 1 ATOM 1635 C CB . SER A 1 216 ? 23.688 7.535 9.629 1.00 21.07 ? 216 SER A CB 1 ATOM 1636 O OG . SER A 1 216 ? 22.708 7.068 8.706 1.00 24.43 ? 216 SER A OG 1 ATOM 1637 N N . THR A 1 217 ? 21.866 10.436 8.944 1.00 20.66 ? 217 THR A N 1 ATOM 1638 C CA . THR A 1 217 ? 21.514 11.184 7.737 1.00 20.30 ? 217 THR A CA 1 ATOM 1639 C C . THR A 1 217 ? 21.074 12.613 7.998 1.00 19.16 ? 217 THR A C 1 ATOM 1640 O O . THR A 1 217 ? 21.516 13.526 7.315 1.00 18.92 ? 217 THR A O 1 ATOM 1641 C CB . THR A 1 217 ? 20.451 10.380 6.991 1.00 20.81 ? 217 THR A CB 1 ATOM 1642 O OG1 . THR A 1 217 ? 20.982 9.062 6.760 1.00 22.53 ? 217 THR A OG1 1 ATOM 1643 C CG2 . THR A 1 217 ? 20.161 10.934 5.608 1.00 20.28 ? 217 THR A CG2 1 ATOM 1644 N N . GLY A 1 218 ? 20.210 12.811 8.986 1.00 18.09 ? 218 GLY A N 1 ATOM 1645 C CA . GLY A 1 218 ? 19.655 14.129 9.222 1.00 17.28 ? 218 GLY A CA 1 ATOM 1646 C C . GLY A 1 218 ? 19.438 14.355 10.706 1.00 16.86 ? 218 GLY A C 1 ATOM 1647 O O . GLY A 1 218 ? 19.758 13.501 11.510 1.00 15.97 ? 218 GLY A O 1 ATOM 1648 N N . ILE A 1 219 ? 18.892 15.506 11.065 1.00 16.67 ? 219 ILE A N 1 ATOM 1649 C CA . ILE A 1 219 ? 18.714 15.820 12.483 1.00 16.21 ? 219 ILE A CA 1 ATOM 1650 C C . ILE A 1 219 ? 17.332 15.444 12.993 1.00 15.32 ? 219 ILE A C 1 ATOM 1651 O O . ILE A 1 219 ? 17.115 15.353 14.197 1.00 14.36 ? 219 ILE A O 1 ATOM 1652 C CB . ILE A 1 219 ? 18.993 17.307 12.759 1.00 17.04 ? 219 ILE A CB 1 ATOM 1653 C CG1 . ILE A 1 219 ? 17.973 18.180 12.012 1.00 17.17 ? 219 ILE A CG1 1 ATOM 1654 C CG2 . ILE A 1 219 ? 20.469 17.657 12.443 1.00 17.26 ? 219 ILE A CG2 1 ATOM 1655 C CD1 . ILE A 1 219 ? 17.604 19.425 12.774 1.00 20.73 ? 219 ILE A CD1 1 ATOM 1656 N N . SER A 1 220 ? 16.397 15.226 12.079 1.00 14.84 ? 220 SER A N 1 ATOM 1657 C CA . SER A 1 220 ? 15.074 14.751 12.476 1.00 15.01 ? 220 SER A CA 1 ATOM 1658 C C . SER A 1 220 ? 14.410 13.986 11.345 1.00 14.49 ? 220 SER A C 1 ATOM 1659 O O . SER A 1 220 ? 14.815 14.107 10.198 1.00 14.30 ? 220 SER A O 1 ATOM 1660 C CB . SER A 1 220 ? 14.182 15.904 12.952 1.00 14.23 ? 220 SER A CB 1 ATOM 1661 O OG . SER A 1 220 ? 13.983 16.856 11.933 1.00 15.05 ? 220 SER A OG 1 ATOM 1662 N N . TRP A 1 221 ? 13.396 13.199 11.678 1.00 15.16 ? 221 TRP A N 1 ATOM 1663 C CA . TRP A 1 221 ? 12.640 12.444 10.673 1.00 14.11 ? 221 TRP A CA 1 ATOM 1664 C C . TRP A 1 221 ? 11.191 12.330 11.107 1.00 13.66 ? 221 TRP A C 1 ATOM 1665 O O . TRP A 1 221 ? 10.905 11.880 12.219 1.00 13.23 ? 221 TRP A O 1 ATOM 1666 C CB . TRP A 1 221 ? 13.201 11.027 10.472 1.00 13.93 ? 221 TRP A CB 1 ATOM 1667 C CG . TRP A 1 221 ? 13.654 10.405 11.766 1.00 13.94 ? 221 TRP A CG 1 ATOM 1668 C CD1 . TRP A 1 221 ? 12.929 9.600 12.594 1.00 14.16 ? 221 TRP A CD1 1 ATOM 1669 C CD2 . TRP A 1 221 ? 14.936 10.547 12.364 1.00 15.39 ? 221 TRP A CD2 1 ATOM 1670 N NE1 . TRP A 1 221 ? 13.689 9.229 13.680 1.00 15.77 ? 221 TRP A NE1 1 ATOM 1671 C CE2 . TRP A 1 221 ? 14.928 9.798 13.564 1.00 16.54 ? 221 TRP A CE2 1 ATOM 1672 C CE3 . TRP A 1 221 ? 16.103 11.234 12.009 1.00 15.39 ? 221 TRP A CE3 1 ATOM 1673 C CZ2 . TRP A 1 221 ? 16.029 9.720 14.405 1.00 16.05 ? 221 TRP A CZ2 1 ATOM 1674 C CZ3 . TRP A 1 221 ? 17.208 11.152 12.855 1.00 16.59 ? 221 TRP A CZ3 1 ATOM 1675 C CH2 . TRP A 1 221 ? 17.162 10.406 14.026 1.00 17.19 ? 221 TRP A CH2 1 ATOM 1676 N N . ARG A 1 222 ? 10.288 12.747 10.213 1.00 13.30 ? 222 ARG A N 1 ATOM 1677 C CA . ARG A 1 222 ? 8.856 12.526 10.367 1.00 13.82 ? 222 ARG A CA 1 ATOM 1678 C C . ARG A 1 222 ? 8.654 11.034 10.599 1.00 14.19 ? 222 ARG A C 1 ATOM 1679 O O . ARG A 1 222 ? 9.296 10.218 9.957 1.00 14.94 ? 222 ARG A O 1 ATOM 1680 C CB . ARG A 1 222 ? 8.107 13.039 9.123 1.00 13.76 ? 222 ARG A CB 1 ATOM 1681 C CG . ARG A 1 222 ? 7.923 14.575 9.164 1.00 14.73 ? 222 ARG A CG 1 ATOM 1682 C CD . ARG A 1 222 ? 6.647 15.013 9.940 1.00 14.59 ? 222 ARG A CD 1 ATOM 1683 N NE . ARG A 1 222 ? 5.581 14.178 9.411 1.00 12.76 ? 222 ARG A NE 1 ATOM 1684 C CZ . ARG A 1 222 ? 4.914 14.460 8.304 1.00 14.36 ? 222 ARG A CZ 1 ATOM 1685 N NH1 . ARG A 1 222 ? 5.196 15.553 7.630 1.00 14.70 ? 222 ARG A NH1 1 ATOM 1686 N NH2 . ARG A 1 222 ? 3.962 13.648 7.875 1.00 13.54 ? 222 ARG A NH2 1 ATOM 1687 N N . MET A 1 223 ? 7.766 10.672 11.518 1.00 13.98 ? 223 MET A N 1 ATOM 1688 C CA . MET A 1 223 ? 7.595 9.264 11.872 1.00 14.29 ? 223 MET A CA 1 ATOM 1689 C C . MET A 1 223 ? 6.196 8.760 11.542 1.00 13.94 ? 223 MET A C 1 ATOM 1690 O O . MET A 1 223 ? 5.821 7.635 11.870 1.00 14.48 ? 223 MET A O 1 ATOM 1691 C CB . MET A 1 223 ? 7.973 9.001 13.332 1.00 13.80 ? 223 MET A CB 1 ATOM 1692 C CG . MET A 1 223 ? 7.537 10.097 14.296 1.00 15.34 ? 223 MET A CG 1 ATOM 1693 S SD . MET A 1 223 ? 5.784 10.319 14.392 1.00 16.64 ? 223 MET A SD 1 ATOM 1694 C CE . MET A 1 223 ? 5.258 8.737 14.883 1.00 13.06 ? 223 MET A CE 1 ATOM 1695 N N . SER A 1 224 ? 5.426 9.611 10.877 1.00 13.81 ? 224 SER A N 1 ATOM 1696 C CA . SER A 1 224 ? 4.064 9.265 10.536 1.00 13.58 ? 224 SER A CA 1 ATOM 1697 C C . SER A 1 224 ? 3.627 10.037 9.324 1.00 13.63 ? 224 SER A C 1 ATOM 1698 O O . SER A 1 224 ? 4.323 10.928 8.851 1.00 14.78 ? 224 SER A O 1 ATOM 1699 C CB . SER A 1 224 ? 3.128 9.645 11.695 1.00 12.73 ? 224 SER A CB 1 ATOM 1700 O OG . SER A 1 224 ? 3.070 11.059 11.810 1.00 11.27 ? 224 SER A OG 1 ATOM 1701 N N . ASP A 1 225 ? 2.458 9.684 8.821 1.00 14.31 ? 225 ASP A N 1 ATOM 1702 C CA . ASP A 1 225 ? 1.821 10.501 7.807 1.00 15.33 ? 225 ASP A CA 1 ATOM 1703 C C . ASP A 1 225 ? 1.284 11.793 8.473 1.00 14.85 ? 225 ASP A C 1 ATOM 1704 O O . ASP A 1 225 ? 1.212 11.887 9.698 1.00 15.27 ? 225 ASP A O 1 ATOM 1705 C CB . ASP A 1 225 ? 0.699 9.730 7.132 1.00 14.79 ? 225 ASP A CB 1 ATOM 1706 C CG . ASP A 1 225 ? 0.473 10.174 5.733 1.00 16.95 ? 225 ASP A CG 1 ATOM 1707 O OD1 . ASP A 1 225 ? 1.122 11.151 5.306 1.00 19.10 ? 225 ASP A OD1 1 ATOM 1708 O OD2 . ASP A 1 225 ? -0.338 9.605 4.977 1.00 18.57 ? 225 ASP A OD2 1 ATOM 1709 N N . ASP A 1 226 ? 0.920 12.757 7.634 1.00 14.66 ? 226 ASP A N 1 ATOM 1710 C CA . ASP A 1 226 ? 0.655 14.136 8.019 1.00 15.19 ? 226 ASP A CA 1 ATOM 1711 C C . ASP A 1 226 ? -0.300 14.264 9.176 1.00 15.55 ? 226 ASP A C 1 ATOM 1712 O O . ASP A 1 226 ? -1.336 13.616 9.202 1.00 15.24 ? 226 ASP A O 1 ATOM 1713 C CB . ASP A 1 226 ? 0.063 14.897 6.837 1.00 14.85 ? 226 ASP A CB 1 ATOM 1714 C CG . ASP A 1 226 ? 1.041 15.068 5.698 1.00 17.45 ? 226 ASP A CG 1 ATOM 1715 O OD1 . ASP A 1 226 ? 2.162 14.516 5.759 1.00 16.96 ? 226 ASP A OD1 1 ATOM 1716 O OD2 . ASP A 1 226 ? 0.768 15.741 4.695 1.00 19.44 ? 226 ASP A OD2 1 ATOM 1717 N N . ILE A 1 227 ? 0.043 15.100 10.136 1.00 15.21 ? 227 ILE A N 1 ATOM 1718 C CA . ILE A 1 227 ? -0.911 15.393 11.206 1.00 15.35 ? 227 ILE A CA 1 ATOM 1719 C C . ILE A 1 227 ? -2.092 16.192 10.602 1.00 14.98 ? 227 ILE A C 1 ATOM 1720 O O . ILE A 1 227 ? -1.943 16.836 9.584 1.00 15.35 ? 227 ILE A O 1 ATOM 1721 C CB . ILE A 1 227 ? -0.215 16.242 12.253 1.00 14.26 ? 227 ILE A CB 1 ATOM 1722 C CG1 . ILE A 1 227 ? -1.046 16.374 13.530 1.00 16.01 ? 227 ILE A CG1 1 ATOM 1723 C CG2 . ILE A 1 227 ? 0.088 17.604 11.677 1.00 14.97 ? 227 ILE A CG2 1 ATOM 1724 C CD1 . ILE A 1 227 ? -0.227 16.990 14.670 1.00 14.30 ? 227 ILE A CD1 1 ATOM 1725 N N . SER A 1 228 ? -3.242 16.124 11.259 1.00 15.47 ? 228 SER A N 1 ATOM 1726 C CA . SER A 1 228 ? -4.424 16.930 10.967 1.00 16.56 ? 228 SER A CA 1 ATOM 1727 C C . SER A 1 228 ? -4.860 17.503 12.309 1.00 15.73 ? 228 SER A C 1 ATOM 1728 O O . SER A 1 228 ? -4.560 16.896 13.319 1.00 16.21 ? 228 SER A O 1 ATOM 1729 C CB . SER A 1 228 ? -5.545 16.046 10.417 1.00 16.11 ? 228 SER A CB 1 ATOM 1730 O OG . SER A 1 228 ? -5.330 15.730 9.048 1.00 19.55 ? 228 SER A OG 1 ATOM 1731 N N . PRO A 1 229 ? -5.563 18.646 12.345 1.00 15.71 ? 229 PRO A N 1 ATOM 1732 C CA . PRO A 1 229 ? -5.849 19.328 13.622 1.00 15.61 ? 229 PRO A CA 1 ATOM 1733 C C . PRO A 1 229 ? -7.079 18.728 14.264 1.00 15.55 ? 229 PRO A C 1 ATOM 1734 O O . PRO A 1 229 ? -8.093 19.407 14.410 1.00 17.63 ? 229 PRO A O 1 ATOM 1735 C CB . PRO A 1 229 ? -6.123 20.783 13.194 1.00 15.70 ? 229 PRO A CB 1 ATOM 1736 C CG . PRO A 1 229 ? -6.679 20.664 11.799 1.00 15.27 ? 229 PRO A CG 1 ATOM 1737 C CD . PRO A 1 229 ? -6.135 19.375 11.197 1.00 15.28 ? 229 PRO A CD 1 ATOM 1738 N N . ASN A 1 230 ? -6.988 17.460 14.632 1.00 15.06 ? 230 ASN A N 1 ATOM 1739 C CA . ASN A 1 230 ? -8.023 16.811 15.411 1.00 15.23 ? 230 ASN A CA 1 ATOM 1740 C C . ASN A 1 230 ? -7.431 15.758 16.311 1.00 15.48 ? 230 ASN A C 1 ATOM 1741 O O . ASN A 1 230 ? -6.299 15.311 16.113 1.00 15.01 ? 230 ASN A O 1 ATOM 1742 C CB . ASN A 1 230 ? -9.141 16.201 14.541 1.00 15.48 ? 230 ASN A CB 1 ATOM 1743 C CG . ASN A 1 230 ? -8.631 15.191 13.530 1.00 17.02 ? 230 ASN A CG 1 ATOM 1744 O OD1 . ASN A 1 230 ? -8.171 14.108 13.886 1.00 19.22 ? 230 ASN A OD1 1 ATOM 1745 N ND2 . ASN A 1 230 ? -8.715 15.544 12.258 1.00 16.86 ? 230 ASN A ND2 1 ATOM 1746 N N . TRP A 1 231 ? -8.217 15.366 17.300 1.00 15.66 ? 231 TRP A N 1 ATOM 1747 C CA . TRP A 1 231 ? -7.786 14.425 18.316 1.00 16.43 ? 231 TRP A CA 1 ATOM 1748 C C . TRP A 1 231 ? -7.423 13.069 17.774 1.00 16.08 ? 231 TRP A C 1 ATOM 1749 O O . TRP A 1 231 ? -6.499 12.432 18.291 1.00 15.59 ? 231 TRP A O 1 ATOM 1750 C CB . TRP A 1 231 ? -8.894 14.266 19.335 1.00 16.19 ? 231 TRP A CB 1 ATOM 1751 C CG . TRP A 1 231 ? -8.599 13.355 20.473 1.00 16.06 ? 231 TRP A CG 1 ATOM 1752 C CD1 . TRP A 1 231 ? -9.240 12.186 20.763 1.00 14.57 ? 231 TRP A CD1 1 ATOM 1753 C CD2 . TRP A 1 231 ? -7.598 13.527 21.485 1.00 17.67 ? 231 TRP A CD2 1 ATOM 1754 N NE1 . TRP A 1 231 ? -8.699 11.618 21.893 1.00 16.46 ? 231 TRP A NE1 1 ATOM 1755 C CE2 . TRP A 1 231 ? -7.690 12.423 22.355 1.00 16.73 ? 231 TRP A CE2 1 ATOM 1756 C CE3 . TRP A 1 231 ? -6.627 14.504 21.746 1.00 19.86 ? 231 TRP A CE3 1 ATOM 1757 C CZ2 . TRP A 1 231 ? -6.859 12.271 23.453 1.00 19.20 ? 231 TRP A CZ2 1 ATOM 1758 C CZ3 . TRP A 1 231 ? -5.800 14.346 22.846 1.00 18.32 ? 231 TRP A CZ3 1 ATOM 1759 C CH2 . TRP A 1 231 ? -5.922 13.242 23.681 1.00 18.35 ? 231 TRP A CH2 1 ATOM 1760 N N . GLY A 1 232 ? -8.141 12.624 16.740 1.00 15.88 ? 232 GLY A N 1 ATOM 1761 C CA . GLY A 1 232 ? -7.801 11.378 16.076 1.00 15.55 ? 232 GLY A CA 1 ATOM 1762 C C . GLY A 1 232 ? -6.358 11.323 15.580 1.00 15.85 ? 232 GLY A C 1 ATOM 1763 O O . GLY A 1 232 ? -5.688 10.291 15.699 1.00 15.30 ? 232 GLY A O 1 ATOM 1764 N N . SER A 1 233 ? -5.866 12.420 15.019 1.00 15.91 ? 233 SER A N 1 ATOM 1765 C CA . SER A 1 233 ? -4.497 12.423 14.548 1.00 17.28 ? 233 SER A CA 1 ATOM 1766 C C . SER A 1 233 ? -3.529 12.571 15.700 1.00 16.55 ? 233 SER A C 1 ATOM 1767 O O . SER A 1 233 ? -2.430 12.025 15.649 1.00 16.83 ? 233 SER A O 1 ATOM 1768 C CB . SER A 1 233 ? -4.238 13.519 13.535 1.00 17.62 ? 233 SER A CB 1 ATOM 1769 O OG . SER A 1 233 ? -4.548 13.014 12.249 1.00 23.04 ? 233 SER A OG 1 ATOM 1770 N N . VAL A 1 234 ? -3.928 13.305 16.731 1.00 15.74 ? 234 VAL A N 1 ATOM 1771 C CA . VAL A 1 234 ? -3.039 13.482 17.873 1.00 15.45 ? 234 VAL A CA 1 ATOM 1772 C C . VAL A 1 234 ? -2.811 12.132 18.530 1.00 15.59 ? 234 VAL A C 1 ATOM 1773 O O . VAL A 1 234 ? -1.655 11.773 18.828 1.00 15.73 ? 234 VAL A O 1 ATOM 1774 C CB . VAL A 1 234 ? -3.546 14.539 18.869 1.00 15.64 ? 234 VAL A CB 1 ATOM 1775 C CG1 . VAL A 1 234 ? -2.745 14.484 20.197 1.00 14.42 ? 234 VAL A CG1 1 ATOM 1776 C CG2 . VAL A 1 234 ? -3.465 15.952 18.229 1.00 16.14 ? 234 VAL A CG2 1 ATOM 1777 N N . THR A 1 235 ? -3.883 11.371 18.762 1.00 14.27 ? 235 THR A N 1 ATOM 1778 C CA . THR A 1 235 ? -3.685 10.054 19.345 1.00 14.69 ? 235 THR A CA 1 ATOM 1779 C C . THR A 1 235 ? -3.034 9.084 18.351 1.00 14.42 ? 235 THR A C 1 ATOM 1780 O O . THR A 1 235 ? -2.195 8.301 18.741 1.00 15.16 ? 235 THR A O 1 ATOM 1781 C CB . THR A 1 235 ? -4.970 9.421 19.879 1.00 14.24 ? 235 THR A CB 1 ATOM 1782 O OG1 . THR A 1 235 ? -5.869 9.180 18.789 1.00 15.10 ? 235 THR A OG1 1 ATOM 1783 C CG2 . THR A 1 235 ? -5.688 10.375 20.782 1.00 15.06 ? 235 THR A CG2 1 ATOM 1784 N N . ARG A 1 236 ? -3.416 9.125 17.081 1.00 14.28 ? 236 ARG A N 1 ATOM 1785 C CA . ARG A 1 236 ? -2.736 8.276 16.109 1.00 14.59 ? 236 ARG A CA 1 ATOM 1786 C C . ARG A 1 236 ? -1.223 8.478 16.197 1.00 14.08 ? 236 ARG A C 1 ATOM 1787 O O . ARG A 1 236 ? -0.482 7.508 16.276 1.00 14.01 ? 236 ARG A O 1 ATOM 1788 C CB . ARG A 1 236 ? -3.197 8.544 14.673 1.00 14.57 ? 236 ARG A CB 1 ATOM 1789 C CG . ARG A 1 236 ? -2.525 7.653 13.617 1.00 17.19 ? 236 ARG A CG 1 ATOM 1790 C CD . ARG A 1 236 ? -2.847 7.997 12.125 1.00 19.58 ? 236 ARG A CD 1 ATOM 1791 N NE . ARG A 1 236 ? -3.096 9.434 11.899 1.00 19.54 ? 236 ARG A NE 1 ATOM 1792 C CZ . ARG A 1 236 ? -2.268 10.272 11.291 1.00 22.80 ? 236 ARG A CZ 1 ATOM 1793 N NH1 . ARG A 1 236 ? -2.631 11.550 11.159 1.00 25.34 ? 236 ARG A NH1 1 ATOM 1794 N NH2 . ARG A 1 236 ? -1.083 9.855 10.812 1.00 15.54 ? 236 ARG A NH2 1 ATOM 1795 N N . ILE A 1 237 ? -0.764 9.725 16.181 1.00 13.40 ? 237 ILE A N 1 ATOM 1796 C CA . ILE A 1 237 ? 0.675 9.955 16.094 1.00 14.20 ? 237 ILE A CA 1 ATOM 1797 C C . ILE A 1 237 ? 1.310 9.656 17.443 1.00 14.62 ? 237 ILE A C 1 ATOM 1798 O O . ILE A 1 237 ? 2.417 9.129 17.523 1.00 14.26 ? 237 ILE A O 1 ATOM 1799 C CB . ILE A 1 237 ? 0.987 11.398 15.612 1.00 14.36 ? 237 ILE A CB 1 ATOM 1800 C CG1 . ILE A 1 237 ? 0.629 11.528 14.127 1.00 14.87 ? 237 ILE A CG1 1 ATOM 1801 C CG2 . ILE A 1 237 ? 2.479 11.755 15.851 1.00 15.16 ? 237 ILE A CG2 1 ATOM 1802 C CD1 . ILE A 1 237 ? 0.392 12.957 13.657 1.00 15.47 ? 237 ILE A CD1 1 ATOM 1803 N N . LEU A 1 238 ? 0.601 9.996 18.512 1.00 13.55 ? 238 LEU A N 1 ATOM 1804 C CA . LEU A 1 238 ? 1.122 9.703 19.831 1.00 14.57 ? 238 LEU A CA 1 ATOM 1805 C C . LEU A 1 238 ? 1.371 8.195 19.948 1.00 14.62 ? 238 LEU A C 1 ATOM 1806 O O . LEU A 1 238 ? 2.425 7.747 20.415 1.00 15.56 ? 238 LEU A O 1 ATOM 1807 C CB . LEU A 1 238 ? 0.147 10.193 20.903 1.00 14.13 ? 238 LEU A CB 1 ATOM 1808 C CG . LEU A 1 238 ? 0.543 9.926 22.336 1.00 15.03 ? 238 LEU A CG 1 ATOM 1809 C CD1 . LEU A 1 238 ? 1.854 10.624 22.665 1.00 18.09 ? 238 LEU A CD1 1 ATOM 1810 C CD2 . LEU A 1 238 ? -0.578 10.462 23.218 1.00 17.82 ? 238 LEU A CD2 1 ATOM 1811 N N . ASN A 1 239 ? 0.400 7.408 19.522 1.00 14.70 ? 239 ASN A N 1 ATOM 1812 C CA . ASN A 1 239 ? 0.521 5.970 19.645 1.00 14.73 ? 239 ASN A CA 1 ATOM 1813 C C . ASN A 1 239 ? 1.693 5.435 18.812 1.00 14.48 ? 239 ASN A C 1 ATOM 1814 O O . ASN A 1 239 ? 2.491 4.660 19.297 1.00 14.71 ? 239 ASN A O 1 ATOM 1815 C CB . ASN A 1 239 ? -0.789 5.292 19.256 1.00 14.64 ? 239 ASN A CB 1 ATOM 1816 C CG . ASN A 1 239 ? -0.661 3.803 19.188 1.00 14.97 ? 239 ASN A CG 1 ATOM 1817 O OD1 . ASN A 1 239 ? -0.365 3.146 20.179 1.00 16.70 ? 239 ASN A OD1 1 ATOM 1818 N ND2 . ASN A 1 239 ? -0.886 3.253 18.009 1.00 15.91 ? 239 ASN A ND2 1 ATOM 1819 N N . LEU A 1 240 ? 1.787 5.859 17.564 1.00 14.08 ? 240 LEU A N 1 ATOM 1820 C CA . LEU A 1 240 ? 2.871 5.405 16.719 1.00 14.81 ? 240 LEU A CA 1 ATOM 1821 C C . LEU A 1 240 ? 4.217 5.741 17.359 1.00 14.49 ? 240 LEU A C 1 ATOM 1822 O O . LEU A 1 240 ? 5.094 4.876 17.492 1.00 16.05 ? 240 LEU A O 1 ATOM 1823 C CB . LEU A 1 240 ? 2.776 6.082 15.349 1.00 14.48 ? 240 LEU A CB 1 ATOM 1824 C CG . LEU A 1 240 ? 1.745 5.557 14.366 1.00 16.63 ? 240 LEU A CG 1 ATOM 1825 C CD1 . LEU A 1 240 ? 1.687 6.575 13.237 1.00 18.52 ? 240 LEU A CD1 1 ATOM 1826 C CD2 . LEU A 1 240 ? 2.232 4.196 13.854 1.00 17.83 ? 240 LEU A CD2 1 ATOM 1827 N N . ASN A 1 241 ? 4.390 6.993 17.760 1.00 14.12 ? 241 ASN A N 1 ATOM 1828 C CA . ASN A 1 241 ? 5.680 7.422 18.320 1.00 14.30 ? 241 ASN A CA 1 ATOM 1829 C C . ASN A 1 241 ? 6.061 6.732 19.607 1.00 15.00 ? 241 ASN A C 1 ATOM 1830 O O . ASN A 1 241 ? 7.247 6.486 19.877 1.00 14.30 ? 241 ASN A O 1 ATOM 1831 C CB . ASN A 1 241 ? 5.707 8.918 18.558 1.00 13.91 ? 241 ASN A CB 1 ATOM 1832 C CG . ASN A 1 241 ? 7.081 9.493 18.351 1.00 14.83 ? 241 ASN A CG 1 ATOM 1833 O OD1 . ASN A 1 241 ? 7.842 9.012 17.503 1.00 16.12 ? 241 ASN A OD1 1 ATOM 1834 N ND2 . ASN A 1 241 ? 7.414 10.518 19.108 1.00 11.62 ? 241 ASN A ND2 1 ATOM 1835 N N . SER A 1 242 ? 5.048 6.417 20.406 1.00 15.07 ? 242 SER A N 1 ATOM 1836 C CA . SER A 1 242 ? 5.294 5.810 21.702 1.00 15.70 ? 242 SER A CA 1 ATOM 1837 C C . SER A 1 242 ? 6.130 4.524 21.599 1.00 15.72 ? 242 SER A C 1 ATOM 1838 O O . SER A 1 242 ? 6.777 4.143 22.556 1.00 16.59 ? 242 SER A O 1 ATOM 1839 C CB . SER A 1 242 ? 3.988 5.579 22.451 1.00 15.12 ? 242 SER A CB 1 ATOM 1840 O OG . SER A 1 242 ? 3.235 4.555 21.853 1.00 17.11 ? 242 SER A OG 1 ATOM 1841 N N . PHE A 1 243 ? 6.113 3.869 20.445 1.00 16.09 ? 243 PHE A N 1 ATOM 1842 C CA . PHE A 1 243 ? 6.873 2.635 20.223 1.00 16.72 ? 243 PHE A CA 1 ATOM 1843 C C . PHE A 1 243 ? 8.242 2.884 19.594 1.00 16.63 ? 243 PHE A C 1 ATOM 1844 O O . PHE A 1 243 ? 9.006 1.957 19.369 1.00 17.72 ? 243 PHE A O 1 ATOM 1845 C CB . PHE A 1 243 ? 6.050 1.631 19.398 1.00 16.74 ? 243 PHE A CB 1 ATOM 1846 C CG . PHE A 1 243 ? 4.843 1.146 20.144 1.00 17.88 ? 243 PHE A CG 1 ATOM 1847 C CD1 . PHE A 1 243 ? 4.964 0.138 21.072 1.00 18.82 ? 243 PHE A CD1 1 ATOM 1848 C CD2 . PHE A 1 243 ? 3.594 1.710 19.926 1.00 18.57 ? 243 PHE A CD2 1 ATOM 1849 C CE1 . PHE A 1 243 ? 3.861 -0.319 21.779 1.00 20.44 ? 243 PHE A CE1 1 ATOM 1850 C CE2 . PHE A 1 243 ? 2.479 1.253 20.635 1.00 19.65 ? 243 PHE A CE2 1 ATOM 1851 C CZ . PHE A 1 243 ? 2.620 0.242 21.557 1.00 19.72 ? 243 PHE A CZ 1 ATOM 1852 N N . LYS A 1 244 ? 8.553 4.138 19.321 1.00 16.37 ? 244 LYS A N 1 ATOM 1853 C CA . LYS A 1 244 ? 9.735 4.450 18.527 1.00 15.91 ? 244 LYS A CA 1 ATOM 1854 C C . LYS A 1 244 ? 10.688 5.387 19.241 1.00 15.99 ? 244 LYS A C 1 ATOM 1855 O O . LYS A 1 244 ? 11.555 6.002 18.618 1.00 15.12 ? 244 LYS A O 1 ATOM 1856 C CB . LYS A 1 244 ? 9.295 5.065 17.196 1.00 16.13 ? 244 LYS A CB 1 ATOM 1857 C CG . LYS A 1 244 ? 8.394 4.169 16.381 1.00 15.29 ? 244 LYS A CG 1 ATOM 1858 C CD . LYS A 1 244 ? 9.184 3.036 15.754 1.00 21.83 ? 244 LYS A CD 1 ATOM 1859 C CE . LYS A 1 244 ? 8.232 2.101 14.999 1.00 25.06 ? 244 LYS A CE 1 ATOM 1860 N NZ . LYS A 1 244 ? 8.981 0.991 14.398 1.00 28.71 ? 244 LYS A NZ 1 ATOM 1861 N N . LEU A 1 245 ? 10.521 5.494 20.554 1.00 15.77 ? 245 LEU A N 1 ATOM 1862 C CA . LEU A 1 245 ? 11.282 6.463 21.318 1.00 16.19 ? 245 LEU A CA 1 ATOM 1863 C C . LEU A 1 245 ? 12.769 6.126 21.458 1.00 17.52 ? 245 LEU A C 1 ATOM 1864 O O . LEU A 1 245 ? 13.558 6.974 21.827 1.00 16.42 ? 245 LEU A O 1 ATOM 1865 C CB . LEU A 1 245 ? 10.607 6.720 22.661 1.00 16.21 ? 245 LEU A CB 1 ATOM 1866 C CG . LEU A 1 245 ? 9.219 7.355 22.426 1.00 14.43 ? 245 LEU A CG 1 ATOM 1867 C CD1 . LEU A 1 245 ? 8.462 7.484 23.737 1.00 14.80 ? 245 LEU A CD1 1 ATOM 1868 C CD2 . LEU A 1 245 ? 9.318 8.707 21.716 1.00 15.50 ? 245 LEU A CD2 1 ATOM 1869 N N . ASN A 1 246 ? 13.142 4.887 21.154 1.00 17.70 ? 246 ASN A N 1 ATOM 1870 C CA . ASN A 1 246 ? 14.530 4.496 21.326 1.00 18.52 ? 246 ASN A CA 1 ATOM 1871 C C . ASN A 1 246 ? 15.413 5.061 20.249 1.00 18.39 ? 246 ASN A C 1 ATOM 1872 O O . ASN A 1 246 ? 16.618 5.007 20.360 1.00 18.28 ? 246 ASN A O 1 ATOM 1873 C CB . ASN A 1 246 ? 14.667 2.989 21.452 1.00 18.89 ? 246 ASN A CB 1 ATOM 1874 C CG . ASN A 1 246 ? 14.155 2.503 22.789 1.00 19.43 ? 246 ASN A CG 1 ATOM 1875 O OD1 . ASN A 1 246 ? 13.336 1.583 22.865 1.00 24.25 ? 246 ASN A OD1 1 ATOM 1876 N ND2 . ASN A 1 246 ? 14.633 3.128 23.856 1.00 18.78 ? 246 ASN A ND2 1 ATOM 1877 N N . SER A 1 247 ? 14.786 5.605 19.214 1.00 17.70 ? 247 SER A N 1 ATOM 1878 C CA . SER A 1 247 ? 15.504 6.287 18.145 1.00 18.69 ? 247 SER A CA 1 ATOM 1879 C C . SER A 1 247 ? 15.725 7.742 18.488 1.00 17.82 ? 247 SER A C 1 ATOM 1880 O O . SER A 1 247 ? 16.330 8.462 17.724 1.00 18.06 ? 247 SER A O 1 ATOM 1881 C CB . SER A 1 247 ? 14.667 6.232 16.872 1.00 18.53 ? 247 SER A CB 1 ATOM 1882 O OG . SER A 1 247 ? 14.280 4.903 16.707 1.00 23.62 ? 247 SER A OG 1 ATOM 1883 N N . VAL A 1 248 ? 15.237 8.188 19.635 1.00 17.33 ? 248 VAL A N 1 ATOM 1884 C CA . VAL A 1 248 ? 15.280 9.618 19.916 1.00 16.71 ? 248 VAL A CA 1 ATOM 1885 C C . VAL A 1 248 ? 16.352 9.946 20.938 1.00 17.02 ? 248 VAL A C 1 ATOM 1886 O O . VAL A 1 248 ? 16.290 9.509 22.095 1.00 17.33 ? 248 VAL A O 1 ATOM 1887 C CB . VAL A 1 248 ? 13.916 10.149 20.430 1.00 17.60 ? 248 VAL A CB 1 ATOM 1888 C CG1 . VAL A 1 248 ? 13.965 11.655 20.614 1.00 15.50 ? 248 VAL A CG1 1 ATOM 1889 C CG2 . VAL A 1 248 ? 12.789 9.765 19.475 1.00 15.70 ? 248 VAL A CG2 1 ATOM 1890 N N . ASP A 1 249 ? 17.331 10.719 20.499 1.00 16.92 ? 249 ASP A N 1 ATOM 1891 C CA . ASP A 1 249 ? 18.364 11.219 21.375 1.00 17.62 ? 249 ASP A CA 1 ATOM 1892 C C . ASP A 1 249 ? 18.894 12.517 20.741 1.00 17.56 ? 249 ASP A C 1 ATOM 1893 O O . ASP A 1 249 ? 18.307 13.021 19.772 1.00 16.44 ? 249 ASP A O 1 ATOM 1894 C CB . ASP A 1 249 ? 19.445 10.165 21.487 1.00 17.57 ? 249 ASP A CB 1 ATOM 1895 C CG . ASP A 1 249 ? 20.175 10.212 22.803 1.00 20.59 ? 249 ASP A CG 1 ATOM 1896 O OD1 . ASP A 1 249 ? 20.584 11.315 23.232 1.00 17.72 ? 249 ASP A OD1 1 ATOM 1897 O OD2 . ASP A 1 249 ? 20.377 9.174 23.464 1.00 23.76 ? 249 ASP A OD2 1 ATOM 1898 N N . PHE A 1 250 ? 19.987 13.052 21.280 1.00 17.74 ? 250 PHE A N 1 ATOM 1899 C CA . PHE A 1 250 ? 20.648 14.228 20.717 1.00 17.42 ? 250 PHE A CA 1 ATOM 1900 C C . PHE A 1 250 ? 20.958 14.010 19.241 1.00 16.88 ? 250 PHE A C 1 ATOM 1901 O O . PHE A 1 250 ? 21.290 12.900 18.819 1.00 16.93 ? 250 PHE A O 1 ATOM 1902 C CB . PHE A 1 250 ? 21.999 14.505 21.423 1.00 18.10 ? 250 PHE A CB 1 ATOM 1903 C CG . PHE A 1 250 ? 21.867 14.978 22.847 1.00 19.03 ? 250 PHE A CG 1 ATOM 1904 C CD1 . PHE A 1 250 ? 21.103 16.087 23.162 1.00 19.07 ? 250 PHE A CD1 1 ATOM 1905 C CD2 . PHE A 1 250 ? 22.516 14.303 23.869 1.00 21.23 ? 250 PHE A CD2 1 ATOM 1906 C CE1 . PHE A 1 250 ? 20.983 16.526 24.490 1.00 19.95 ? 250 PHE A CE1 1 ATOM 1907 C CE2 . PHE A 1 250 ? 22.403 14.729 25.193 1.00 21.15 ? 250 PHE A CE2 1 ATOM 1908 C CZ . PHE A 1 250 ? 21.634 15.842 25.502 1.00 19.87 ? 250 PHE A CZ 1 ATOM 1909 N N . TRP A 1 251 ? 20.843 15.092 18.483 1.00 15.83 ? 251 TRP A N 1 ATOM 1910 C CA . TRP A 1 251 ? 21.108 15.125 17.051 1.00 16.02 ? 251 TRP A CA 1 ATOM 1911 C C . TRP A 1 251 ? 20.155 14.358 16.153 1.00 15.59 ? 251 TRP A C 1 ATOM 1912 O O . TRP A 1 251 ? 20.397 14.293 14.959 1.00 15.38 ? 251 TRP A O 1 ATOM 1913 C CB . TRP A 1 251 ? 22.534 14.624 16.752 1.00 16.22 ? 251 TRP A CB 1 ATOM 1914 C CG . TRP A 1 251 ? 23.601 15.418 17.427 1.00 16.49 ? 251 TRP A CG 1 ATOM 1915 C CD1 . TRP A 1 251 ? 24.403 15.021 18.467 1.00 18.56 ? 251 TRP A CD1 1 ATOM 1916 C CD2 . TRP A 1 251 ? 23.988 16.753 17.110 1.00 18.40 ? 251 TRP A CD2 1 ATOM 1917 N NE1 . TRP A 1 251 ? 25.268 16.037 18.812 1.00 19.62 ? 251 TRP A NE1 1 ATOM 1918 C CE2 . TRP A 1 251 ? 25.035 17.112 17.994 1.00 19.88 ? 251 TRP A CE2 1 ATOM 1919 C CE3 . TRP A 1 251 ? 23.559 17.686 16.167 1.00 16.87 ? 251 TRP A CE3 1 ATOM 1920 C CZ2 . TRP A 1 251 ? 25.652 18.369 17.956 1.00 22.05 ? 251 TRP A CZ2 1 ATOM 1921 C CZ3 . TRP A 1 251 ? 24.165 18.926 16.127 1.00 20.15 ? 251 TRP A CZ3 1 ATOM 1922 C CH2 . TRP A 1 251 ? 25.202 19.258 17.015 1.00 20.25 ? 251 TRP A CH2 1 ATOM 1923 N N . GLY A 1 252 ? 19.090 13.778 16.694 1.00 14.89 ? 252 GLY A N 1 ATOM 1924 C CA . GLY A 1 252 ? 18.316 12.850 15.887 1.00 14.81 ? 252 GLY A CA 1 ATOM 1925 C C . GLY A 1 252 ? 16.997 12.592 16.564 1.00 15.39 ? 252 GLY A C 1 ATOM 1926 O O . GLY A 1 252 ? 16.879 11.749 17.466 1.00 14.27 ? 252 GLY A O 1 ATOM 1927 N N . HIS A 1 253 ? 15.986 13.327 16.124 1.00 14.08 ? 253 HIS A N 1 ATOM 1928 C CA . HIS A 1 253 ? 14.715 13.240 16.821 1.00 14.49 ? 253 HIS A CA 1 ATOM 1929 C C . HIS A 1 253 ? 13.580 12.827 15.941 1.00 14.08 ? 253 HIS A C 1 ATOM 1930 O O . HIS A 1 253 ? 13.471 13.320 14.831 1.00 14.70 ? 253 HIS A O 1 ATOM 1931 C CB . HIS A 1 253 ? 14.382 14.594 17.420 1.00 13.96 ? 253 HIS A CB 1 ATOM 1932 C CG . HIS A 1 253 ? 15.318 14.996 18.514 1.00 15.54 ? 253 HIS A CG 1 ATOM 1933 N ND1 . HIS A 1 253 ? 16.466 15.717 18.283 1.00 15.55 ? 253 HIS A ND1 1 ATOM 1934 C CD2 . HIS A 1 253 ? 15.272 14.775 19.845 1.00 16.70 ? 253 HIS A CD2 1 ATOM 1935 C CE1 . HIS A 1 253 ? 17.089 15.925 19.427 1.00 15.84 ? 253 HIS A CE1 1 ATOM 1936 N NE2 . HIS A 1 253 ? 16.388 15.364 20.392 1.00 17.18 ? 253 HIS A NE2 1 ATOM 1937 N N . ASN A 1 254 ? 12.741 11.923 16.443 1.00 14.16 ? 254 ASN A N 1 ATOM 1938 C CA . ASN A 1 254 ? 11.513 11.594 15.741 1.00 14.57 ? 254 ASN A CA 1 ATOM 1939 C C . ASN A 1 254 ? 10.698 12.873 15.670 1.00 14.02 ? 254 ASN A C 1 ATOM 1940 O O . ASN A 1 254 ? 10.597 13.633 16.652 1.00 15.05 ? 254 ASN A O 1 ATOM 1941 C CB . ASN A 1 254 ? 10.681 10.537 16.470 1.00 14.28 ? 254 ASN A CB 1 ATOM 1942 C CG . ASN A 1 254 ? 11.368 9.181 16.535 1.00 16.09 ? 254 ASN A CG 1 ATOM 1943 O OD1 . ASN A 1 254 ? 12.486 9.005 16.055 1.00 15.00 ? 254 ASN A OD1 1 ATOM 1944 N ND2 . ASN A 1 254 ? 10.694 8.213 17.136 1.00 15.58 ? 254 ASN A ND2 1 ATOM 1945 N N . ASP A 1 255 ? 10.119 13.098 14.509 1.00 13.21 ? 255 ASP A N 1 ATOM 1946 C CA . ASP A 1 255 ? 9.347 14.299 14.247 1.00 12.94 ? 255 ASP A CA 1 ATOM 1947 C C . ASP A 1 255 ? 7.879 13.876 14.198 1.00 11.80 ? 255 ASP A C 1 ATOM 1948 O O . ASP A 1 255 ? 7.462 13.191 13.306 1.00 11.78 ? 255 ASP A O 1 ATOM 1949 C CB . ASP A 1 255 ? 9.868 14.914 12.934 1.00 13.37 ? 255 ASP A CB 1 ATOM 1950 C CG . ASP A 1 255 ? 9.128 16.164 12.519 1.00 13.34 ? 255 ASP A CG 1 ATOM 1951 O OD1 . ASP A 1 255 ? 9.519 16.738 11.476 1.00 13.40 ? 255 ASP A OD1 1 ATOM 1952 O OD2 . ASP A 1 255 ? 8.164 16.637 13.163 1.00 13.13 ? 255 ASP A OD2 1 ATOM 1953 N N . ALA A 1 256 ? 7.107 14.300 15.193 1.00 12.76 ? 256 ALA A N 1 ATOM 1954 C CA . ALA A 1 256 ? 5.701 13.954 15.312 1.00 12.17 ? 256 ALA A CA 1 ATOM 1955 C C . ALA A 1 256 ? 4.854 14.898 14.490 1.00 12.67 ? 256 ALA A C 1 ATOM 1956 O O . ALA A 1 256 ? 3.637 14.944 14.657 1.00 13.08 ? 256 ALA A O 1 ATOM 1957 C CB . ALA A 1 256 ? 5.260 14.007 16.748 1.00 11.75 ? 256 ALA A CB 1 ATOM 1958 N N . ASP A 1 257 ? 5.515 15.637 13.610 1.00 12.65 ? 257 ASP A N 1 ATOM 1959 C CA . ASP A 1 257 ? 4.892 16.600 12.707 1.00 13.92 ? 257 ASP A CA 1 ATOM 1960 C C . ASP A 1 257 ? 4.554 17.939 13.335 1.00 14.28 ? 257 ASP A C 1 ATOM 1961 O O . ASP A 1 257 ? 4.661 18.136 14.552 1.00 15.23 ? 257 ASP A O 1 ATOM 1962 C CB . ASP A 1 257 ? 3.673 16.022 11.991 1.00 13.38 ? 257 ASP A CB 1 ATOM 1963 C CG . ASP A 1 257 ? 3.519 16.557 10.579 1.00 14.91 ? 257 ASP A CG 1 ATOM 1964 O OD1 . ASP A 1 257 ? 4.276 17.478 10.132 1.00 13.64 ? 257 ASP A OD1 1 ATOM 1965 O OD2 . ASP A 1 257 ? 2.652 16.106 9.836 1.00 15.33 ? 257 ASP A OD2 1 ATOM 1966 N N . MET A 1 258 ? 4.145 18.850 12.470 1.00 14.22 ? 258 MET A N 1 ATOM 1967 C CA . MET A 1 258 ? 3.966 20.238 12.825 1.00 14.70 ? 258 MET A CA 1 ATOM 1968 C C . MET A 1 258 ? 2.804 20.422 13.756 1.00 14.93 ? 258 MET A C 1 ATOM 1969 O O . MET A 1 258 ? 1.807 19.718 13.641 1.00 14.70 ? 258 MET A O 1 ATOM 1970 C CB . MET A 1 258 ? 3.824 21.097 11.572 1.00 14.45 ? 258 MET A CB 1 ATOM 1971 C CG . MET A 1 258 ? 5.114 21.046 10.749 1.00 16.56 ? 258 MET A CG 1 ATOM 1972 S SD . MET A 1 258 ? 4.960 21.617 9.066 1.00 18.91 ? 258 MET A SD 1 ATOM 1973 C CE . MET A 1 258 ? 3.765 20.453 8.384 1.00 16.03 ? 258 MET A CE 1 ATOM 1974 N N . LEU A 1 259 ? 2.953 21.373 14.678 1.00 14.78 ? 259 LEU A N 1 ATOM 1975 C CA . LEU A 1 259 ? 1.925 21.649 15.680 1.00 15.45 ? 259 LEU A CA 1 ATOM 1976 C C . LEU A 1 259 ? 0.638 22.187 15.065 1.00 16.11 ? 259 LEU A C 1 ATOM 1977 O O . LEU A 1 259 ? 0.677 22.987 14.131 1.00 15.21 ? 259 LEU A O 1 ATOM 1978 C CB . LEU A 1 259 ? 2.440 22.643 16.697 1.00 14.93 ? 259 LEU A CB 1 ATOM 1979 C CG . LEU A 1 259 ? 3.694 22.135 17.429 1.00 17.20 ? 259 LEU A CG 1 ATOM 1980 C CD1 . LEU A 1 259 ? 4.269 23.226 18.274 1.00 17.69 ? 259 LEU A CD1 1 ATOM 1981 C CD2 . LEU A 1 259 ? 3.411 20.875 18.274 1.00 17.22 ? 259 LEU A CD2 1 ATOM 1982 N N . GLU A 1 260 ? -0.478 21.724 15.621 1.00 16.48 ? 260 GLU A N 1 ATOM 1983 C CA . GLU A 1 260 ? -1.810 22.112 15.225 1.00 16.99 ? 260 GLU A CA 1 ATOM 1984 C C . GLU A 1 260 ? -2.456 23.018 16.269 1.00 17.77 ? 260 GLU A C 1 ATOM 1985 O O . GLU A 1 260 ? -3.641 23.315 16.185 1.00 17.62 ? 260 GLU A O 1 ATOM 1986 C CB . GLU A 1 260 ? -2.655 20.860 15.009 1.00 16.94 ? 260 GLU A CB 1 ATOM 1987 C CG . GLU A 1 260 ? -2.177 20.019 13.832 1.00 15.98 ? 260 GLU A CG 1 ATOM 1988 C CD . GLU A 1 260 ? -2.519 20.615 12.469 1.00 16.99 ? 260 GLU A CD 1 ATOM 1989 O OE1 . GLU A 1 260 ? -2.873 21.807 12.376 1.00 18.01 ? 260 GLU A OE1 1 ATOM 1990 O OE2 . GLU A 1 260 ? -2.431 19.880 11.470 1.00 17.54 ? 260 GLU A OE2 1 ATOM 1991 N N . VAL A 1 261 ? -1.662 23.448 17.247 1.00 17.71 ? 261 VAL A N 1 ATOM 1992 C CA . VAL A 1 261 ? -2.076 24.496 18.157 1.00 18.94 ? 261 VAL A CA 1 ATOM 1993 C C . VAL A 1 261 ? -2.665 25.641 17.329 1.00 19.47 ? 261 VAL A C 1 ATOM 1994 O O . VAL A 1 261 ? -2.029 26.135 16.404 1.00 19.44 ? 261 VAL A O 1 ATOM 1995 C CB . VAL A 1 261 ? -0.889 25.016 18.961 1.00 19.06 ? 261 VAL A CB 1 ATOM 1996 C CG1 . VAL A 1 261 ? -1.351 26.095 19.903 1.00 20.16 ? 261 VAL A CG1 1 ATOM 1997 C CG2 . VAL A 1 261 ? -0.198 23.848 19.723 1.00 18.66 ? 261 VAL A CG2 1 ATOM 1998 N N . GLY A 1 262 ? -3.881 26.052 17.670 1.00 20.39 ? 262 GLY A N 1 ATOM 1999 C CA . GLY A 1 262 ? -4.584 27.094 16.944 1.00 20.93 ? 262 GLY A CA 1 ATOM 2000 C C . GLY A 1 262 ? -5.520 26.653 15.830 1.00 21.46 ? 262 GLY A C 1 ATOM 2001 O O . GLY A 1 262 ? -6.184 27.495 15.239 1.00 22.13 ? 262 GLY A O 1 ATOM 2002 N N . ASN A 1 263 ? -5.581 25.349 15.545 1.00 21.23 ? 263 ASN A N 1 ATOM 2003 C CA . ASN A 1 263 ? -6.195 24.852 14.320 1.00 20.96 ? 263 ASN A CA 1 ATOM 2004 C C . ASN A 1 263 ? -7.284 23.817 14.508 1.00 20.63 ? 263 ASN A C 1 ATOM 2005 O O . ASN A 1 263 ? -7.330 23.123 15.517 1.00 20.11 ? 263 ASN A O 1 ATOM 2006 C CB . ASN A 1 263 ? -5.121 24.243 13.387 1.00 20.32 ? 263 ASN A CB 1 ATOM 2007 C CG . ASN A 1 263 ? -4.025 25.217 13.032 1.00 21.37 ? 263 ASN A CG 1 ATOM 2008 O OD1 . ASN A 1 263 ? -4.216 26.433 13.086 1.00 22.34 ? 263 ASN A OD1 1 ATOM 2009 N ND2 . ASN A 1 263 ? -2.849 24.683 12.662 1.00 20.73 ? 263 ASN A ND2 1 ATOM 2010 N N . GLY A 1 264 ? -8.160 23.726 13.517 1.00 20.73 ? 264 GLY A N 1 ATOM 2011 C CA . GLY A 1 264 ? -9.226 22.737 13.518 1.00 21.49 ? 264 GLY A CA 1 ATOM 2012 C C . GLY A 1 264 ? -10.067 22.736 14.773 1.00 21.97 ? 264 GLY A C 1 ATOM 2013 O O . GLY A 1 264 ? -10.347 23.788 15.316 1.00 21.52 ? 264 GLY A O 1 ATOM 2014 N N . ASN A 1 265 ? -10.456 21.548 15.229 1.00 23.83 ? 265 ASN A N 1 ATOM 2015 C CA . ASN A 1 265 ? -11.436 21.403 16.312 1.00 25.19 ? 265 ASN A CA 1 ATOM 2016 C C . ASN A 1 265 ? -10.851 20.916 17.627 1.00 24.63 ? 265 ASN A C 1 ATOM 2017 O O . ASN A 1 265 ? -11.591 20.498 18.531 1.00 24.94 ? 265 ASN A O 1 ATOM 2018 C CB . ASN A 1 265 ? -12.579 20.456 15.893 1.00 26.78 ? 265 ASN A CB 1 ATOM 2019 C CG . ASN A 1 265 ? -12.090 19.007 15.676 1.00 30.70 ? 265 ASN A CG 1 ATOM 2020 O OD1 . ASN A 1 265 ? -10.903 18.726 15.821 1.00 34.41 ? 265 ASN A OD1 1 ATOM 2021 N ND2 . ASN A 1 265 ? -13.004 18.099 15.329 1.00 33.18 ? 265 ASN A ND2 1 ATOM 2022 N N . LEU A 1 266 ? -9.535 20.966 17.740 1.00 23.37 ? 266 LEU A N 1 ATOM 2023 C CA . LEU A 1 266 ? -8.913 20.601 19.002 1.00 22.68 ? 266 LEU A CA 1 ATOM 2024 C C . LEU A 1 266 ? -9.402 21.555 20.068 1.00 22.56 ? 266 LEU A C 1 ATOM 2025 O O . LEU A 1 266 ? -9.350 22.766 19.898 1.00 22.67 ? 266 LEU A O 1 ATOM 2026 C CB . LEU A 1 266 ? -7.407 20.693 18.904 1.00 21.83 ? 266 LEU A CB 1 ATOM 2027 C CG . LEU A 1 266 ? -6.782 19.726 17.916 1.00 21.63 ? 266 LEU A CG 1 ATOM 2028 C CD1 . LEU A 1 266 ? -5.388 20.235 17.582 1.00 21.46 ? 266 LEU A CD1 1 ATOM 2029 C CD2 . LEU A 1 266 ? -6.750 18.333 18.504 1.00 19.56 ? 266 LEU A CD2 1 ATOM 2030 N N . THR A 1 267 ? -9.876 20.989 21.163 1.00 22.53 ? 267 THR A N 1 ATOM 2031 C CA . THR A 1 267 ? -10.280 21.752 22.334 1.00 22.63 ? 267 THR A CA 1 ATOM 2032 C C . THR A 1 267 ? -9.035 22.247 23.041 1.00 22.28 ? 267 THR A C 1 ATOM 2033 O O . THR A 1 267 ? -7.910 21.886 22.675 1.00 22.53 ? 267 THR A O 1 ATOM 2034 C CB . THR A 1 267 ? -11.021 20.841 23.306 1.00 22.12 ? 267 THR A CB 1 ATOM 2035 O OG1 . THR A 1 267 ? -10.175 19.738 23.649 1.00 21.80 ? 267 THR A OG1 1 ATOM 2036 C CG2 . THR A 1 267 ? -12.189 20.174 22.622 1.00 22.96 ? 267 THR A CG2 1 ATOM 2037 N N . ALA A 1 268 ? -9.226 23.073 24.058 1.00 21.53 ? 268 ALA A N 1 ATOM 2038 C CA . ALA A 1 268 ? -8.103 23.566 24.812 1.00 21.16 ? 268 ALA A CA 1 ATOM 2039 C C . ALA A 1 268 ? -7.354 22.391 25.441 1.00 20.51 ? 268 ALA A C 1 ATOM 2040 O O . ALA A 1 268 ? -6.130 22.384 25.440 1.00 20.99 ? 268 ALA A O 1 ATOM 2041 C CB . ALA A 1 268 ? -8.550 24.543 25.870 1.00 21.85 ? 268 ALA A CB 1 ATOM 2042 N N . ALA A 1 269 ? -8.092 21.414 25.967 1.00 18.66 ? 269 ALA A N 1 ATOM 2043 C CA . ALA A 1 269 ? -7.508 20.211 26.581 1.00 18.13 ? 269 ALA A CA 1 ATOM 2044 C C . ALA A 1 269 ? -6.663 19.416 25.570 1.00 17.51 ? 269 ALA A C 1 ATOM 2045 O O . ALA A 1 269 ? -5.519 19.085 25.825 1.00 16.00 ? 269 ALA A O 1 ATOM 2046 C CB . ALA A 1 269 ? -8.602 19.327 27.160 1.00 17.60 ? 269 ALA A CB 1 ATOM 2047 N N . GLU A 1 270 ? -7.257 19.119 24.420 1.00 16.99 ? 270 GLU A N 1 ATOM 2048 C CA . GLU A 1 270 ? -6.543 18.431 23.359 1.00 17.15 ? 270 GLU A CA 1 ATOM 2049 C C . GLU A 1 270 ? -5.306 19.186 22.921 1.00 17.21 ? 270 GLU A C 1 ATOM 2050 O O . GLU A 1 270 ? -4.270 18.582 22.681 1.00 17.92 ? 270 GLU A O 1 ATOM 2051 C CB . GLU A 1 270 ? -7.481 18.160 22.188 1.00 16.90 ? 270 GLU A CB 1 ATOM 2052 C CG . GLU A 1 270 ? -8.649 17.326 22.661 1.00 15.87 ? 270 GLU A CG 1 ATOM 2053 C CD . GLU A 1 270 ? -9.735 17.216 21.631 1.00 17.74 ? 270 GLU A CD 1 ATOM 2054 O OE1 . GLU A 1 270 ? -9.747 18.069 20.714 1.00 18.43 ? 270 GLU A OE1 1 ATOM 2055 O OE2 . GLU A 1 270 ? -10.556 16.280 21.757 1.00 16.46 ? 270 GLU A OE2 1 ATOM 2056 N N . THR A 1 271 ? -5.412 20.506 22.817 1.00 17.46 ? 271 THR A N 1 ATOM 2057 C CA . THR A 1 271 ? -4.272 21.325 22.438 1.00 17.33 ? 271 THR A CA 1 ATOM 2058 C C . THR A 1 271 ? -3.114 21.164 23.435 1.00 17.56 ? 271 THR A C 1 ATOM 2059 O O . THR A 1 271 ? -1.953 21.058 23.055 1.00 16.50 ? 271 THR A O 1 ATOM 2060 C CB . THR A 1 271 ? -4.675 22.787 22.329 1.00 17.08 ? 271 THR A CB 1 ATOM 2061 O OG1 . THR A 1 271 ? -5.710 22.917 21.346 1.00 18.66 ? 271 THR A OG1 1 ATOM 2062 C CG2 . THR A 1 271 ? -3.522 23.610 21.738 1.00 18.32 ? 271 THR A CG2 1 ATOM 2063 N N . ARG A 1 272 ? -3.452 21.145 24.716 1.00 16.96 ? 272 ARG A N 1 ATOM 2064 C CA . ARG A 1 272 ? -2.460 21.030 25.767 1.00 17.29 ? 272 ARG A CA 1 ATOM 2065 C C . ARG A 1 272 ? -1.757 19.694 25.676 1.00 16.26 ? 272 ARG A C 1 ATOM 2066 O O . ARG A 1 272 ? -0.557 19.611 25.835 1.00 16.35 ? 272 ARG A O 1 ATOM 2067 C CB . ARG A 1 272 ? -3.153 21.121 27.136 1.00 17.15 ? 272 ARG A CB 1 ATOM 2068 C CG . ARG A 1 272 ? -3.214 22.540 27.696 1.00 20.65 ? 272 ARG A CG 1 ATOM 2069 C CD . ARG A 1 272 ? -3.566 22.628 29.170 1.00 22.92 ? 272 ARG A CD 1 ATOM 2070 N NE . ARG A 1 272 ? -4.910 22.165 29.479 1.00 25.46 ? 272 ARG A NE 1 ATOM 2071 C CZ . ARG A 1 272 ? -6.036 22.875 29.292 1.00 28.67 ? 272 ARG A CZ 1 ATOM 2072 N NH1 . ARG A 1 272 ? -5.989 24.103 28.786 1.00 27.97 ? 272 ARG A NH1 1 ATOM 2073 N NH2 . ARG A 1 272 ? -7.225 22.350 29.617 1.00 28.77 ? 272 ARG A NH2 1 ATOM 2074 N N . THR A 1 273 ? -2.543 18.661 25.420 1.00 15.67 ? 273 THR A N 1 ATOM 2075 C CA . THR A 1 273 ? -2.062 17.308 25.363 1.00 15.19 ? 273 THR A CA 1 ATOM 2076 C C . THR A 1 273 ? -1.122 17.259 24.179 1.00 15.34 ? 273 THR A C 1 ATOM 2077 O O . THR A 1 273 ? -0.007 16.751 24.258 1.00 14.67 ? 273 THR A O 1 ATOM 2078 C CB . THR A 1 273 ? -3.264 16.388 25.142 1.00 14.73 ? 273 THR A CB 1 ATOM 2079 O OG1 . THR A 1 273 ? -3.979 16.267 26.380 1.00 15.52 ? 273 THR A OG1 1 ATOM 2080 C CG2 . THR A 1 273 ? -2.819 14.968 24.859 1.00 13.80 ? 273 THR A CG2 1 ATOM 2081 N N . HIS A 1 274 ? -1.603 17.812 23.077 1.00 14.98 ? 274 HIS A N 1 ATOM 2082 C CA . HIS A 1 274 ? -0.842 17.814 21.850 1.00 15.43 ? 274 HIS A CA 1 ATOM 2083 C C . HIS A 1 274 ? 0.514 18.512 22.022 1.00 15.78 ? 274 HIS A C 1 ATOM 2084 O O . HIS A 1 274 ? 1.547 17.949 21.661 1.00 15.48 ? 274 HIS A O 1 ATOM 2085 C CB . HIS A 1 274 ? -1.646 18.438 20.717 1.00 15.46 ? 274 HIS A CB 1 ATOM 2086 C CG . HIS A 1 274 ? -0.859 18.609 19.460 1.00 17.65 ? 274 HIS A CG 1 ATOM 2087 N ND1 . HIS A 1 274 ? -0.949 19.734 18.668 1.00 18.78 ? 274 HIS A ND1 1 ATOM 2088 C CD2 . HIS A 1 274 ? 0.034 17.792 18.858 1.00 15.70 ? 274 HIS A CD2 1 ATOM 2089 C CE1 . HIS A 1 274 ? -0.142 19.605 17.631 1.00 16.38 ? 274 HIS A CE1 1 ATOM 2090 N NE2 . HIS A 1 274 ? 0.465 18.436 17.722 1.00 18.57 ? 274 HIS A NE2 1 ATOM 2091 N N . PHE A 1 275 ? 0.529 19.727 22.567 1.00 15.84 ? 275 PHE A N 1 ATOM 2092 C CA . PHE A 1 275 ? 1.796 20.432 22.718 1.00 15.55 ? 275 PHE A CA 1 ATOM 2093 C C . PHE A 1 275 ? 2.700 19.719 23.744 1.00 15.46 ? 275 PHE A C 1 ATOM 2094 O O . PHE A 1 275 ? 3.857 19.461 23.476 1.00 15.26 ? 275 PHE A O 1 ATOM 2095 C CB . PHE A 1 275 ? 1.580 21.907 23.110 1.00 15.95 ? 275 PHE A CB 1 ATOM 2096 C CG . PHE A 1 275 ? 2.853 22.675 23.243 1.00 17.52 ? 275 PHE A CG 1 ATOM 2097 C CD1 . PHE A 1 275 ? 3.566 23.042 22.120 1.00 18.38 ? 275 PHE A CD1 1 ATOM 2098 C CD2 . PHE A 1 275 ? 3.349 23.027 24.485 1.00 19.12 ? 275 PHE A CD2 1 ATOM 2099 C CE1 . PHE A 1 275 ? 4.735 23.742 22.227 1.00 17.35 ? 275 PHE A CE1 1 ATOM 2100 C CE2 . PHE A 1 275 ? 4.515 23.725 24.586 1.00 17.77 ? 275 PHE A CE2 1 ATOM 2101 C CZ . PHE A 1 275 ? 5.207 24.083 23.457 1.00 17.27 ? 275 PHE A CZ 1 ATOM 2102 N N . ALA A 1 276 ? 2.149 19.405 24.915 1.00 15.19 ? 276 ALA A N 1 ATOM 2103 C CA . ALA A 1 276 ? 2.916 18.797 25.990 1.00 14.48 ? 276 ALA A CA 1 ATOM 2104 C C . ALA A 1 276 ? 3.592 17.509 25.524 1.00 13.92 ? 276 ALA A C 1 ATOM 2105 O O . ALA A 1 276 ? 4.744 17.298 25.811 1.00 12.97 ? 276 ALA A O 1 ATOM 2106 C CB . ALA A 1 276 ? 2.026 18.516 27.213 1.00 14.61 ? 276 ALA A CB 1 ATOM 2107 N N . LEU A 1 277 ? 2.863 16.661 24.807 1.00 13.93 ? 277 LEU A N 1 ATOM 2108 C CA . LEU A 1 277 ? 3.432 15.375 24.407 1.00 13.99 ? 277 LEU A CA 1 ATOM 2109 C C . LEU A 1 277 ? 4.409 15.518 23.260 1.00 13.93 ? 277 LEU A C 1 ATOM 2110 O O . LEU A 1 277 ? 5.411 14.815 23.222 1.00 13.81 ? 277 LEU A O 1 ATOM 2111 C CB . LEU A 1 277 ? 2.369 14.327 24.091 1.00 13.09 ? 277 LEU A CB 1 ATOM 2112 C CG . LEU A 1 277 ? 1.926 13.424 25.249 1.00 15.24 ? 277 LEU A CG 1 ATOM 2113 C CD1 . LEU A 1 277 ? 3.042 12.428 25.630 1.00 15.10 ? 277 LEU A CD1 1 ATOM 2114 C CD2 . LEU A 1 277 ? 1.523 14.305 26.413 1.00 16.10 ? 277 LEU A CD2 1 ATOM 2115 N N . TRP A 1 278 ? 4.111 16.424 22.333 1.00 14.44 ? 278 TRP A N 1 ATOM 2116 C CA . TRP A 1 278 ? 5.068 16.763 21.275 1.00 14.28 ? 278 TRP A CA 1 ATOM 2117 C C . TRP A 1 278 ? 6.378 17.253 21.892 1.00 14.62 ? 278 TRP A C 1 ATOM 2118 O O . TRP A 1 278 ? 7.443 16.788 21.519 1.00 14.71 ? 278 TRP A O 1 ATOM 2119 C CB . TRP A 1 278 ? 4.475 17.783 20.294 1.00 14.05 ? 278 TRP A CB 1 ATOM 2120 C CG . TRP A 1 278 ? 3.838 17.117 19.050 1.00 12.51 ? 278 TRP A CG 1 ATOM 2121 C CD1 . TRP A 1 278 ? 4.128 17.395 17.756 1.00 11.16 ? 278 TRP A CD1 1 ATOM 2122 C CD2 . TRP A 1 278 ? 2.827 16.087 19.014 1.00 12.53 ? 278 TRP A CD2 1 ATOM 2123 N NE1 . TRP A 1 278 ? 3.371 16.613 16.917 1.00 10.66 ? 278 TRP A NE1 1 ATOM 2124 C CE2 . TRP A 1 278 ? 2.567 15.802 17.660 1.00 11.43 ? 278 TRP A CE2 1 ATOM 2125 C CE3 . TRP A 1 278 ? 2.117 15.378 19.983 1.00 12.25 ? 278 TRP A CE3 1 ATOM 2126 C CZ2 . TRP A 1 278 ? 1.641 14.852 17.255 1.00 11.19 ? 278 TRP A CZ2 1 ATOM 2127 C CZ3 . TRP A 1 278 ? 1.191 14.429 19.572 1.00 14.50 ? 278 TRP A CZ3 1 ATOM 2128 C CH2 . TRP A 1 278 ? 0.968 14.180 18.218 1.00 11.48 ? 278 TRP A CH2 1 ATOM 2129 N N . ALA A 1 279 ? 6.295 18.190 22.835 1.00 14.45 ? 279 ALA A N 1 ATOM 2130 C CA . ALA A 1 279 ? 7.488 18.691 23.531 1.00 14.35 ? 279 ALA A CA 1 ATOM 2131 C C . ALA A 1 279 ? 8.208 17.554 24.271 1.00 14.35 ? 279 ALA A C 1 ATOM 2132 O O . ALA A 1 279 ? 9.432 17.429 24.185 1.00 14.11 ? 279 ALA A O 1 ATOM 2133 C CB . ALA A 1 279 ? 7.125 19.813 24.501 1.00 13.69 ? 279 ALA A CB 1 ATOM 2134 N N . ALA A 1 280 ? 7.445 16.729 24.986 1.00 13.96 ? 280 ALA A N 1 ATOM 2135 C CA . ALA A 1 280 ? 8.031 15.712 25.867 1.00 14.26 ? 280 ALA A CA 1 ATOM 2136 C C . ALA A 1 280 ? 8.655 14.580 25.082 1.00 14.01 ? 280 ALA A C 1 ATOM 2137 O O . ALA A 1 280 ? 9.610 13.936 25.536 1.00 14.31 ? 280 ALA A O 1 ATOM 2138 C CB . ALA A 1 280 ? 6.981 15.164 26.857 1.00 14.24 ? 280 ALA A CB 1 ATOM 2139 N N . MET A 1 281 ? 8.116 14.342 23.901 1.00 14.00 ? 281 MET A N 1 ATOM 2140 C CA . MET A 1 281 ? 8.625 13.279 23.050 1.00 13.81 ? 281 MET A CA 1 ATOM 2141 C C . MET A 1 281 ? 9.844 13.767 22.306 1.00 13.30 ? 281 MET A C 1 ATOM 2142 O O . MET A 1 281 ? 10.457 13.007 21.573 1.00 13.45 ? 281 MET A O 1 ATOM 2143 C CB . MET A 1 281 ? 7.545 12.806 22.067 1.00 14.05 ? 281 MET A CB 1 ATOM 2144 C CG . MET A 1 281 ? 6.472 11.923 22.703 1.00 16.17 ? 281 MET A CG 1 ATOM 2145 S SD . MET A 1 281 ? 5.358 11.253 21.483 1.00 18.04 ? 281 MET A SD 1 ATOM 2146 C CE . MET A 1 281 ? 4.763 12.727 20.672 1.00 18.19 ? 281 MET A CE 1 ATOM 2147 N N . LYS A 1 282 ? 10.176 15.043 22.507 1.00 13.04 ? 282 LYS A N 1 ATOM 2148 C CA . LYS A 1 282 ? 11.324 15.690 21.887 1.00 12.51 ? 282 LYS A CA 1 ATOM 2149 C C . LYS A 1 282 ? 11.232 15.592 20.388 1.00 13.35 ? 282 LYS A C 1 ATOM 2150 O O . LYS A 1 282 ? 12.210 15.367 19.683 1.00 13.14 ? 282 LYS A O 1 ATOM 2151 C CB . LYS A 1 282 ? 12.649 15.178 22.448 1.00 12.26 ? 282 LYS A CB 1 ATOM 2152 C CG . LYS A 1 282 ? 12.738 15.525 23.905 1.00 11.49 ? 282 LYS A CG 1 ATOM 2153 C CD . LYS A 1 282 ? 14.134 15.328 24.460 1.00 11.74 ? 282 LYS A CD 1 ATOM 2154 C CE . LYS A 1 282 ? 14.147 15.746 25.906 1.00 12.44 ? 282 LYS A CE 1 ATOM 2155 N NZ . LYS A 1 282 ? 15.524 15.525 26.426 1.00 13.26 ? 282 LYS A NZ 1 ATOM 2156 N N . SER A 1 283 ? 10.009 15.765 19.915 1.00 12.95 ? 283 SER A N 1 ATOM 2157 C CA . SER A 1 283 ? 9.827 16.037 18.515 1.00 14.08 ? 283 SER A CA 1 ATOM 2158 C C . SER A 1 283 ? 10.308 17.479 18.332 1.00 14.12 ? 283 SER A C 1 ATOM 2159 O O . SER A 1 283 ? 10.267 18.272 19.258 1.00 13.67 ? 283 SER A O 1 ATOM 2160 C CB . SER A 1 283 ? 8.344 15.978 18.181 1.00 13.59 ? 283 SER A CB 1 ATOM 2161 O OG . SER A 1 283 ? 8.093 16.385 16.838 1.00 12.65 ? 283 SER A OG 1 ATOM 2162 N N . PRO A 1 284 ? 10.771 17.813 17.138 1.00 15.23 ? 284 PRO A N 1 ATOM 2163 C CA . PRO A 1 284 ? 10.865 19.220 16.760 1.00 15.12 ? 284 PRO A CA 1 ATOM 2164 C C . PRO A 1 284 ? 9.471 19.843 16.972 1.00 15.24 ? 284 PRO A C 1 ATOM 2165 O O . PRO A 1 284 ? 8.427 19.160 16.833 1.00 13.99 ? 284 PRO A O 1 ATOM 2166 C CB . PRO A 1 284 ? 11.155 19.173 15.263 1.00 15.85 ? 284 PRO A CB 1 ATOM 2167 C CG . PRO A 1 284 ? 11.289 17.748 14.898 1.00 16.87 ? 284 PRO A CG 1 ATOM 2168 C CD . PRO A 1 284 ? 11.226 16.898 16.090 1.00 15.26 ? 284 PRO A CD 1 ATOM 2169 N N . LEU A 1 285 ? 9.462 21.128 17.305 1.00 15.16 ? 285 LEU A N 1 ATOM 2170 C CA . LEU A 1 285 ? 8.236 21.833 17.614 1.00 15.67 ? 285 LEU A CA 1 ATOM 2171 C C . LEU A 1 285 ? 8.107 23.009 16.668 1.00 16.01 ? 285 LEU A C 1 ATOM 2172 O O . LEU A 1 285 ? 8.727 24.062 16.869 1.00 16.02 ? 285 LEU A O 1 ATOM 2173 C CB . LEU A 1 285 ? 8.249 22.353 19.048 1.00 15.16 ? 285 LEU A CB 1 ATOM 2174 C CG . LEU A 1 285 ? 8.370 21.363 20.195 1.00 15.16 ? 285 LEU A CG 1 ATOM 2175 C CD1 . LEU A 1 285 ? 8.303 22.141 21.493 1.00 14.68 ? 285 LEU A CD1 1 ATOM 2176 C CD2 . LEU A 1 285 ? 7.252 20.351 20.150 1.00 14.41 ? 285 LEU A CD2 1 ATOM 2177 N N . LEU A 1 286 ? 7.297 22.820 15.636 1.00 15.36 ? 286 LEU A N 1 ATOM 2178 C CA . LEU A 1 286 ? 7.188 23.798 14.583 1.00 16.12 ? 286 LEU A CA 1 ATOM 2179 C C . LEU A 1 286 ? 5.758 24.276 14.619 1.00 16.50 ? 286 LEU A C 1 ATOM 2180 O O . LEU A 1 286 ? 4.846 23.509 14.336 1.00 16.37 ? 286 LEU A O 1 ATOM 2181 C CB . LEU A 1 286 ? 7.513 23.164 13.212 1.00 16.17 ? 286 LEU A CB 1 ATOM 2182 C CG . LEU A 1 286 ? 8.951 22.662 12.950 1.00 17.20 ? 286 LEU A CG 1 ATOM 2183 C CD1 . LEU A 1 286 ? 9.207 22.279 11.466 1.00 18.18 ? 286 LEU A CD1 1 ATOM 2184 C CD2 . LEU A 1 286 ? 9.969 23.686 13.372 1.00 17.85 ? 286 LEU A CD2 1 ATOM 2185 N N . ILE A 1 287 ? 5.577 25.543 14.971 1.00 16.90 ? 287 ILE A N 1 ATOM 2186 C CA . ILE A 1 287 ? 4.257 26.132 14.993 1.00 17.80 ? 287 ILE A CA 1 ATOM 2187 C C . ILE A 1 287 ? 3.702 26.106 13.570 1.00 18.14 ? 287 ILE A C 1 ATOM 2188 O O . ILE A 1 287 ? 4.425 26.325 12.597 1.00 18.43 ? 287 ILE A O 1 ATOM 2189 C CB . ILE A 1 287 ? 4.286 27.555 15.614 1.00 17.57 ? 287 ILE A CB 1 ATOM 2190 C CG1 . ILE A 1 287 ? 4.975 27.524 16.995 1.00 18.63 ? 287 ILE A CG1 1 ATOM 2191 C CG2 . ILE A 1 287 ? 2.872 28.086 15.774 1.00 17.13 ? 287 ILE A CG2 1 ATOM 2192 C CD1 . ILE A 1 287 ? 5.480 28.874 17.450 1.00 20.29 ? 287 ILE A CD1 1 ATOM 2193 N N . GLY A 1 288 ? 2.411 25.832 13.441 1.00 18.59 ? 288 GLY A N 1 ATOM 2194 C CA . GLY A 1 288 ? 1.831 25.688 12.122 1.00 18.79 ? 288 GLY A CA 1 ATOM 2195 C C . GLY A 1 288 ? 0.522 26.448 12.017 1.00 19.46 ? 288 GLY A C 1 ATOM 2196 O O . GLY A 1 288 ? -0.480 25.916 11.609 1.00 19.23 ? 288 GLY A O 1 ATOM 2197 N N . THR A 1 289 ? 0.530 27.710 12.390 1.00 20.42 ? 289 THR A N 1 ATOM 2198 C CA . THR A 1 289 ? -0.720 28.440 12.393 1.00 21.93 ? 289 THR A CA 1 ATOM 2199 C C . THR A 1 289 ? -0.433 29.905 12.206 1.00 22.89 ? 289 THR A C 1 ATOM 2200 O O . THR A 1 289 ? 0.690 30.347 12.419 1.00 22.95 ? 289 THR A O 1 ATOM 2201 C CB . THR A 1 289 ? -1.454 28.202 13.728 1.00 21.84 ? 289 THR A CB 1 ATOM 2202 O OG1 . THR A 1 289 ? -2.772 28.758 13.657 1.00 21.97 ? 289 THR A OG1 1 ATOM 2203 C CG2 . THR A 1 289 ? -0.776 28.978 14.874 1.00 21.74 ? 289 THR A CG2 1 ATOM 2204 N N . ASP A 1 290 ? -1.451 30.659 11.809 1.00 24.25 ? 290 ASP A N 1 ATOM 2205 C CA . ASP A 1 290 ? -1.288 32.088 11.629 1.00 25.75 ? 290 ASP A CA 1 ATOM 2206 C C . ASP A 1 290 ? -1.191 32.765 12.985 1.00 26.31 ? 290 ASP A C 1 ATOM 2207 O O . ASP A 1 290 ? -2.151 32.779 13.770 1.00 26.74 ? 290 ASP A O 1 ATOM 2208 C CB . ASP A 1 290 ? -2.447 32.671 10.807 1.00 25.89 ? 290 ASP A CB 1 ATOM 2209 C CG . ASP A 1 290 ? -2.358 34.179 10.651 1.00 26.86 ? 290 ASP A CG 1 ATOM 2210 O OD1 . ASP A 1 290 ? -1.400 34.778 11.164 1.00 26.64 ? 290 ASP A OD1 1 ATOM 2211 O OD2 . ASP A 1 290 ? -3.213 34.849 10.022 1.00 28.98 ? 290 ASP A OD2 1 ATOM 2212 N N . LEU A 1 291 ? -0.025 33.331 13.247 1.00 27.30 ? 291 LEU A N 1 ATOM 2213 C CA . LEU A 1 291 ? 0.271 33.876 14.565 1.00 28.57 ? 291 LEU A CA 1 ATOM 2214 C C . LEU A 1 291 ? -0.516 35.130 14.900 1.00 29.06 ? 291 LEU A C 1 ATOM 2215 O O . LEU A 1 291 ? -0.678 35.472 16.066 1.00 29.57 ? 291 LEU A O 1 ATOM 2216 C CB . LEU A 1 291 ? 1.766 34.114 14.709 1.00 28.32 ? 291 LEU A CB 1 ATOM 2217 C CG . LEU A 1 291 ? 2.582 32.827 14.903 1.00 29.52 ? 291 LEU A CG 1 ATOM 2218 C CD1 . LEU A 1 291 ? 4.062 33.131 15.028 1.00 28.05 ? 291 LEU A CD1 1 ATOM 2219 C CD2 . LEU A 1 291 ? 2.106 32.051 16.125 1.00 28.67 ? 291 LEU A CD2 1 ATOM 2220 N N . ALA A 1 292 ? -1.002 35.811 13.874 1.00 29.81 ? 292 ALA A N 1 ATOM 2221 C CA . ALA A 1 292 ? -1.835 36.997 14.067 1.00 30.22 ? 292 ALA A CA 1 ATOM 2222 C C . ALA A 1 292 ? -3.219 36.622 14.601 1.00 30.54 ? 292 ALA A C 1 ATOM 2223 O O . ALA A 1 292 ? -3.896 37.428 15.233 1.00 30.82 ? 292 ALA A O 1 ATOM 2224 C CB . ALA A 1 292 ? -1.955 37.767 12.757 1.00 30.10 ? 292 ALA A CB 1 ATOM 2225 N N . GLN A 1 293 ? -3.626 35.385 14.338 1.00 30.79 ? 293 GLN A N 1 ATOM 2226 C CA . GLN A 1 293 ? -4.955 34.882 14.670 1.00 31.03 ? 293 GLN A CA 1 ATOM 2227 C C . GLN A 1 293 ? -4.921 34.025 15.924 1.00 30.04 ? 293 GLN A C 1 ATOM 2228 O O . GLN A 1 293 ? -5.960 33.615 16.428 1.00 29.85 ? 293 GLN A O 1 ATOM 2229 C CB . GLN A 1 293 ? -5.477 34.019 13.511 1.00 31.47 ? 293 GLN A CB 1 ATOM 2230 C CG . GLN A 1 293 ? -6.362 34.700 12.469 1.00 36.27 ? 293 GLN A CG 1 ATOM 2231 C CD . GLN A 1 293 ? -5.751 35.950 11.844 1.00 41.73 ? 293 GLN A CD 1 ATOM 2232 O OE1 . GLN A 1 293 ? -5.691 37.001 12.488 1.00 45.39 ? 293 GLN A OE1 1 ATOM 2233 N NE2 . GLN A 1 293 ? -5.302 35.841 10.589 1.00 43.16 ? 293 GLN A NE2 1 ATOM 2234 N N . LEU A 1 294 ? -3.723 33.752 16.425 1.00 29.21 ? 294 LEU A N 1 ATOM 2235 C CA . LEU A 1 294 ? -3.563 32.880 17.572 1.00 29.11 ? 294 LEU A CA 1 ATOM 2236 C C . LEU A 1 294 ? -3.881 33.625 18.864 1.00 29.39 ? 294 LEU A C 1 ATOM 2237 O O . LEU A 1 294 ? -3.366 34.720 19.098 1.00 29.30 ? 294 LEU A O 1 ATOM 2238 C CB . LEU A 1 294 ? -2.136 32.323 17.595 1.00 28.99 ? 294 LEU A CB 1 ATOM 2239 C CG . LEU A 1 294 ? -1.841 31.056 18.398 1.00 28.14 ? 294 LEU A CG 1 ATOM 2240 C CD1 . LEU A 1 294 ? -2.748 29.903 18.031 1.00 24.43 ? 294 LEU A CD1 1 ATOM 2241 C CD2 . LEU A 1 294 ? -0.379 30.672 18.198 1.00 26.10 ? 294 LEU A CD2 1 ATOM 2242 N N . SER A 1 295 ? -4.732 33.017 19.689 1.00 29.92 ? 295 SER A N 1 ATOM 2243 C CA . SER A 1 295 ? -5.111 33.560 20.992 1.00 30.51 ? 295 SER A CA 1 ATOM 2244 C C . SER A 1 295 ? -3.902 33.704 21.915 1.00 30.88 ? 295 SER A C 1 ATOM 2245 O O . SER A 1 295 ? -2.907 32.995 21.755 1.00 31.12 ? 295 SER A O 1 ATOM 2246 C CB . SER A 1 295 ? -6.152 32.656 21.647 1.00 30.75 ? 295 SER A CB 1 ATOM 2247 O OG . SER A 1 295 ? -5.577 31.422 22.067 1.00 31.40 ? 295 SER A OG 1 ATOM 2248 N N . GLN A 1 296 ? -3.975 34.614 22.883 1.00 30.53 ? 296 GLN A N 1 ATOM 2249 C CA . GLN A 1 296 ? -2.850 34.810 23.799 1.00 30.86 ? 296 GLN A CA 1 ATOM 2250 C C . GLN A 1 296 ? -2.678 33.563 24.649 1.00 30.19 ? 296 GLN A C 1 ATOM 2251 O O . GLN A 1 296 ? -1.593 33.275 25.121 1.00 30.71 ? 296 GLN A O 1 ATOM 2252 C CB . GLN A 1 296 ? -3.044 36.052 24.690 1.00 31.17 ? 296 GLN A CB 1 ATOM 2253 C CG . GLN A 1 296 ? -1.850 36.391 25.604 1.00 33.14 ? 296 GLN A CG 1 ATOM 2254 C CD . GLN A 1 296 ? -0.572 36.700 24.833 1.00 36.87 ? 296 GLN A CD 1 ATOM 2255 O OE1 . GLN A 1 296 ? 0.490 36.096 25.082 1.00 38.30 ? 296 GLN A OE1 1 ATOM 2256 N NE2 . GLN A 1 296 ? -0.666 37.639 23.897 1.00 37.29 ? 296 GLN A NE2 1 ATOM 2257 N N . ASN A 1 297 ? -3.768 32.833 24.830 1.00 29.60 ? 297 ASN A N 1 ATOM 2258 C CA . ASN A 1 297 ? -3.775 31.567 25.560 1.00 29.44 ? 297 ASN A CA 1 ATOM 2259 C C . ASN A 1 297 ? -2.925 30.472 24.864 1.00 28.31 ? 297 ASN A C 1 ATOM 2260 O O . ASN A 1 297 ? -2.075 29.835 25.468 1.00 27.87 ? 297 ASN A O 1 ATOM 2261 C CB . ASN A 1 297 ? -5.223 31.164 25.698 1.00 29.87 ? 297 ASN A CB 1 ATOM 2262 C CG . ASN A 1 297 ? -6.057 32.275 26.360 1.00 33.46 ? 297 ASN A CG 1 ATOM 2263 O OD1 . ASN A 1 297 ? -6.801 33.014 25.688 1.00 35.29 ? 297 ASN A OD1 1 ATOM 2264 N ND2 . ASN A 1 297 ? -5.925 32.395 27.682 1.00 32.86 ? 297 ASN A ND2 1 ATOM 2265 N N . ASN A 1 298 ? -3.167 30.265 23.583 1.00 27.45 ? 298 ASN A N 1 ATOM 2266 C CA . ASN A 1 298 ? -2.324 29.384 22.798 1.00 26.71 ? 298 ASN A CA 1 ATOM 2267 C C . ASN A 1 298 ? -0.890 29.896 22.671 1.00 26.10 ? 298 ASN A C 1 ATOM 2268 O O . ASN A 1 298 ? 0.051 29.097 22.620 1.00 26.44 ? 298 ASN A O 1 ATOM 2269 C CB . ASN A 1 298 ? -2.940 29.176 21.425 1.00 26.18 ? 298 ASN A CB 1 ATOM 2270 C CG . ASN A 1 298 ? -4.071 28.172 21.445 1.00 27.48 ? 298 ASN A CG 1 ATOM 2271 O OD1 . ASN A 1 298 ? -4.029 27.187 22.176 1.00 28.82 ? 298 ASN A OD1 1 ATOM 2272 N ND2 . ASN A 1 298 ? -5.092 28.417 20.637 1.00 28.41 ? 298 ASN A ND2 1 ATOM 2273 N N . ILE A 1 299 ? -0.697 31.213 22.614 1.00 25.52 ? 299 ILE A N 1 ATOM 2274 C CA . ILE A 1 299 ? 0.675 31.740 22.617 1.00 24.60 ? 299 ILE A CA 1 ATOM 2275 C C . ILE A 1 299 ? 1.398 31.402 23.937 1.00 24.47 ? 299 ILE A C 1 ATOM 2276 O O . ILE A 1 299 ? 2.573 30.978 23.942 1.00 23.60 ? 299 ILE A O 1 ATOM 2277 C CB . ILE A 1 299 ? 0.709 33.255 22.319 1.00 25.12 ? 299 ILE A CB 1 ATOM 2278 C CG1 . ILE A 1 299 ? 0.286 33.500 20.866 1.00 25.80 ? 299 ILE A CG1 1 ATOM 2279 C CG2 . ILE A 1 299 ? 2.108 33.823 22.581 1.00 23.18 ? 299 ILE A CG2 1 ATOM 2280 C CD1 . ILE A 1 299 ? 0.340 34.964 20.422 1.00 29.16 ? 299 ILE A CD1 1 ATOM 2281 N N . ASN A 1 300 ? 0.706 31.584 25.063 1.00 23.75 ? 300 ASN A N 1 ATOM 2282 C CA . ASN A 1 300 ? 1.286 31.201 26.353 1.00 23.45 ? 300 ASN A CA 1 ATOM 2283 C C . ASN A 1 300 ? 1.568 29.709 26.423 1.00 22.44 ? 300 ASN A C 1 ATOM 2284 O O . ASN A 1 300 ? 2.572 29.303 26.996 1.00 21.85 ? 300 ASN A O 1 ATOM 2285 C CB . ASN A 1 300 ? 0.374 31.596 27.528 1.00 24.28 ? 300 ASN A CB 1 ATOM 2286 C CG . ASN A 1 300 ? 0.247 33.101 27.672 1.00 26.87 ? 300 ASN A CG 1 ATOM 2287 O OD1 . ASN A 1 300 ? 1.203 33.836 27.407 1.00 28.97 ? 300 ASN A OD1 1 ATOM 2288 N ND2 . ASN A 1 300 ? -0.927 33.565 28.089 1.00 27.00 ? 300 ASN A ND2 1 ATOM 2289 N N . LEU A 1 301 ? 0.683 28.898 25.844 1.00 21.16 ? 301 LEU A N 1 ATOM 2290 C CA . LEU A 1 301 ? 0.905 27.459 25.792 1.00 20.97 ? 301 LEU A CA 1 ATOM 2291 C C . LEU A 1 301 ? 2.242 27.175 25.114 1.00 20.15 ? 301 LEU A C 1 ATOM 2292 O O . LEU A 1 301 ? 3.075 26.438 25.631 1.00 19.77 ? 301 LEU A O 1 ATOM 2293 C CB . LEU A 1 301 ? -0.205 26.795 24.991 1.00 21.30 ? 301 LEU A CB 1 ATOM 2294 C CG . LEU A 1 301 ? -0.607 25.348 25.289 1.00 24.54 ? 301 LEU A CG 1 ATOM 2295 C CD1 . LEU A 1 301 ? -1.049 24.669 24.015 1.00 25.45 ? 301 LEU A CD1 1 ATOM 2296 C CD2 . LEU A 1 301 ? 0.474 24.538 25.958 1.00 25.35 ? 301 LEU A CD2 1 ATOM 2297 N N . LEU A 1 302 ? 2.437 27.772 23.945 1.00 19.59 ? 302 LEU A N 1 ATOM 2298 C CA . LEU A 1 302 ? 3.657 27.552 23.165 1.00 19.91 ? 302 LEU A CA 1 ATOM 2299 C C . LEU A 1 302 ? 4.900 27.979 23.895 1.00 20.11 ? 302 LEU A C 1 ATOM 2300 O O . LEU A 1 302 ? 5.974 27.442 23.660 1.00 18.73 ? 302 LEU A O 1 ATOM 2301 C CB . LEU A 1 302 ? 3.580 28.296 21.846 1.00 19.52 ? 302 LEU A CB 1 ATOM 2302 C CG . LEU A 1 302 ? 2.477 27.775 20.931 1.00 18.84 ? 302 LEU A CG 1 ATOM 2303 C CD1 . LEU A 1 302 ? 2.394 28.755 19.772 1.00 19.41 ? 302 LEU A CD1 1 ATOM 2304 C CD2 . LEU A 1 302 ? 2.759 26.338 20.435 1.00 18.93 ? 302 LEU A CD2 1 ATOM 2305 N N . LYS A 1 303 ? 4.743 28.955 24.790 1.00 20.95 ? 303 LYS A N 1 ATOM 2306 C CA . LYS A 1 303 ? 5.884 29.519 25.485 1.00 22.03 ? 303 LYS A CA 1 ATOM 2307 C C . LYS A 1 303 ? 6.130 28.804 26.801 1.00 21.52 ? 303 LYS A C 1 ATOM 2308 O O . LYS A 1 303 ? 6.981 29.226 27.562 1.00 22.75 ? 303 LYS A O 1 ATOM 2309 C CB . LYS A 1 303 ? 5.674 31.016 25.748 1.00 22.77 ? 303 LYS A CB 1 ATOM 2310 C CG . LYS A 1 303 ? 5.626 31.873 24.485 1.00 26.72 ? 303 LYS A CG 1 ATOM 2311 C CD . LYS A 1 303 ? 6.071 33.283 24.756 1.00 30.33 ? 303 LYS A CD 1 ATOM 2312 C CE . LYS A 1 303 ? 4.916 34.181 25.038 1.00 33.03 ? 303 LYS A CE 1 ATOM 2313 N NZ . LYS A 1 303 ? 5.418 35.579 25.094 1.00 32.55 ? 303 LYS A NZ 1 ATOM 2314 N N . ASN A 1 304 ? 5.399 27.730 27.082 1.00 20.88 ? 304 ASN A N 1 ATOM 2315 C CA . ASN A 1 304 ? 5.605 27.037 28.358 1.00 20.30 ? 304 ASN A CA 1 ATOM 2316 C C . ASN A 1 304 ? 7.080 26.735 28.654 1.00 20.60 ? 304 ASN A C 1 ATOM 2317 O O . ASN A 1 304 ? 7.720 25.893 28.016 1.00 19.71 ? 304 ASN A O 1 ATOM 2318 C CB . ASN A 1 304 ? 4.754 25.793 28.465 1.00 20.73 ? 304 ASN A CB 1 ATOM 2319 C CG . ASN A 1 304 ? 4.734 25.268 29.846 1.00 18.84 ? 304 ASN A CG 1 ATOM 2320 O OD1 . ASN A 1 304 ? 3.740 25.396 30.567 1.00 21.05 ? 304 ASN A OD1 1 ATOM 2321 N ND2 . ASN A 1 304 ? 5.828 24.674 30.242 1.00 14.84 ? 304 ASN A ND2 1 ATOM 2322 N N . LYS A 1 305 ? 7.612 27.439 29.641 1.00 20.12 ? 305 LYS A N 1 ATOM 2323 C CA . LYS A 1 305 ? 9.038 27.402 29.893 1.00 21.15 ? 305 LYS A CA 1 ATOM 2324 C C . LYS A 1 305 ? 9.514 25.993 30.257 1.00 20.34 ? 305 LYS A C 1 ATOM 2325 O O . LYS A 1 305 ? 10.620 25.638 29.939 1.00 19.74 ? 305 LYS A O 1 ATOM 2326 C CB . LYS A 1 305 ? 9.439 28.448 30.948 1.00 21.17 ? 305 LYS A CB 1 ATOM 2327 C CG . LYS A 1 305 ? 8.984 28.114 32.359 1.00 25.64 ? 305 LYS A CG 1 ATOM 2328 C CD . LYS A 1 305 ? 8.353 29.331 33.067 1.00 32.49 ? 305 LYS A CD 1 ATOM 2329 C CE . LYS A 1 305 ? 8.522 29.267 34.596 1.00 34.79 ? 305 LYS A CE 1 ATOM 2330 N NZ . LYS A 1 305 ? 9.752 30.000 35.058 1.00 37.53 ? 305 LYS A NZ 1 ATOM 2331 N N . HIS A 1 306 ? 8.670 25.203 30.914 1.00 19.71 ? 306 HIS A N 1 ATOM 2332 C CA . HIS A 1 306 ? 9.100 23.893 31.412 1.00 19.07 ? 306 HIS A CA 1 ATOM 2333 C C . HIS A 1 306 ? 9.103 22.838 30.330 1.00 18.52 ? 306 HIS A C 1 ATOM 2334 O O . HIS A 1 306 ? 10.009 22.024 30.249 1.00 17.96 ? 306 HIS A O 1 ATOM 2335 C CB . HIS A 1 306 ? 8.238 23.458 32.612 1.00 19.08 ? 306 HIS A CB 1 ATOM 2336 C CG . HIS A 1 306 ? 8.333 24.403 33.771 1.00 20.98 ? 306 HIS A CG 1 ATOM 2337 N ND1 . HIS A 1 306 ? 7.274 25.175 34.193 1.00 23.37 ? 306 HIS A ND1 1 ATOM 2338 C CD2 . HIS A 1 306 ? 9.367 24.703 34.591 1.00 22.23 ? 306 HIS A CD2 1 ATOM 2339 C CE1 . HIS A 1 306 ? 7.650 25.908 35.226 1.00 23.81 ? 306 HIS A CE1 1 ATOM 2340 N NE2 . HIS A 1 306 ? 8.916 25.641 35.489 1.00 24.40 ? 306 HIS A NE2 1 ATOM 2341 N N . LEU A 1 307 ? 8.071 22.868 29.505 1.00 18.29 ? 307 LEU A N 1 ATOM 2342 C CA . LEU A 1 307 ? 7.968 21.970 28.384 1.00 17.74 ? 307 LEU A CA 1 ATOM 2343 C C . LEU A 1 307 ? 9.112 22.297 27.444 1.00 17.94 ? 307 LEU A C 1 ATOM 2344 O O . LEU A 1 307 ? 9.751 21.402 26.920 1.00 16.58 ? 307 LEU A O 1 ATOM 2345 C CB . LEU A 1 307 ? 6.617 22.164 27.711 1.00 17.51 ? 307 LEU A CB 1 ATOM 2346 C CG . LEU A 1 307 ? 5.478 21.593 28.572 1.00 18.52 ? 307 LEU A CG 1 ATOM 2347 C CD1 . LEU A 1 307 ? 4.109 21.919 27.972 1.00 17.94 ? 307 LEU A CD1 1 ATOM 2348 C CD2 . LEU A 1 307 ? 5.655 20.056 28.768 1.00 18.95 ? 307 LEU A CD2 1 ATOM 2349 N N . LEU A 1 308 ? 9.384 23.578 27.234 1.00 18.17 ? 308 LEU A N 1 ATOM 2350 C CA . LEU A 1 308 ? 10.467 23.943 26.328 1.00 18.88 ? 308 LEU A CA 1 ATOM 2351 C C . LEU A 1 308 ? 11.825 23.546 26.906 1.00 19.24 ? 308 LEU A C 1 ATOM 2352 O O . LEU A 1 308 ? 12.636 22.950 26.217 1.00 19.76 ? 308 LEU A O 1 ATOM 2353 C CB . LEU A 1 308 ? 10.421 25.436 25.987 1.00 19.08 ? 308 LEU A CB 1 ATOM 2354 C CG . LEU A 1 308 ? 9.228 25.862 25.106 1.00 19.60 ? 308 LEU A CG 1 ATOM 2355 C CD1 . LEU A 1 308 ? 9.224 27.361 24.856 1.00 17.51 ? 308 LEU A CD1 1 ATOM 2356 C CD2 . LEU A 1 308 ? 9.244 25.111 23.791 1.00 19.57 ? 308 LEU A CD2 1 ATOM 2357 N N . ALA A 1 309 ? 12.076 23.874 28.169 1.00 18.69 ? 309 ALA A N 1 ATOM 2358 C CA . ALA A 1 309 ? 13.339 23.480 28.764 1.00 18.47 ? 309 ALA A CA 1 ATOM 2359 C C . ALA A 1 309 ? 13.522 21.978 28.651 1.00 17.96 ? 309 ALA A C 1 ATOM 2360 O O . ALA A 1 309 ? 14.618 21.521 28.353 1.00 17.79 ? 309 ALA A O 1 ATOM 2361 C CB . ALA A 1 309 ? 13.436 23.913 30.222 1.00 18.93 ? 309 ALA A CB 1 ATOM 2362 N N . PHE A 1 310 ? 12.454 21.217 28.889 1.00 17.16 ? 310 PHE A N 1 ATOM 2363 C CA . PHE A 1 310 ? 12.570 19.768 28.856 1.00 17.33 ? 310 PHE A CA 1 ATOM 2364 C C . PHE A 1 310 ? 12.917 19.280 27.461 1.00 17.51 ? 310 PHE A C 1 ATOM 2365 O O . PHE A 1 310 ? 13.807 18.457 27.270 1.00 18.23 ? 310 PHE A O 1 ATOM 2366 C CB . PHE A 1 310 ? 11.284 19.075 29.332 1.00 17.44 ? 310 PHE A CB 1 ATOM 2367 C CG . PHE A 1 310 ? 11.374 17.574 29.267 1.00 17.47 ? 310 PHE A CG 1 ATOM 2368 C CD1 . PHE A 1 310 ? 11.059 16.904 28.096 1.00 18.22 ? 310 PHE A CD1 1 ATOM 2369 C CD2 . PHE A 1 310 ? 11.783 16.834 30.372 1.00 19.15 ? 310 PHE A CD2 1 ATOM 2370 C CE1 . PHE A 1 310 ? 11.143 15.527 28.019 1.00 18.13 ? 310 PHE A CE1 1 ATOM 2371 C CE2 . PHE A 1 310 ? 11.868 15.450 30.299 1.00 17.60 ? 310 PHE A CE2 1 ATOM 2372 C CZ . PHE A 1 310 ? 11.544 14.805 29.111 1.00 18.82 ? 310 PHE A CZ 1 ATOM 2373 N N . ASN A 1 311 ? 12.195 19.798 26.479 1.00 16.92 ? 311 ASN A N 1 ATOM 2374 C CA . ASN A 1 311 ? 12.442 19.449 25.100 1.00 16.75 ? 311 ASN A CA 1 ATOM 2375 C C . ASN A 1 311 ? 13.901 19.814 24.707 1.00 16.51 ? 311 ASN A C 1 ATOM 2376 O O . ASN A 1 311 ? 14.597 19.057 24.018 1.00 15.97 ? 311 ASN A O 1 ATOM 2377 C CB . ASN A 1 311 ? 11.385 20.204 24.285 1.00 16.31 ? 311 ASN A CB 1 ATOM 2378 C CG . ASN A 1 311 ? 11.540 20.019 22.824 1.00 15.90 ? 311 ASN A CG 1 ATOM 2379 O OD1 . ASN A 1 311 ? 12.359 20.677 22.197 1.00 17.65 ? 311 ASN A OD1 1 ATOM 2380 N ND2 . ASN A 1 311 ? 10.759 19.128 22.264 1.00 15.76 ? 311 ASN A ND2 1 ATOM 2381 N N . GLN A 1 312 ? 14.349 20.982 25.168 1.00 17.15 ? 312 GLN A N 1 ATOM 2382 C CA . GLN A 1 312 ? 15.609 21.565 24.749 1.00 17.25 ? 312 GLN A CA 1 ATOM 2383 C C . GLN A 1 312 ? 16.745 21.168 25.656 1.00 18.21 ? 312 GLN A C 1 ATOM 2384 O O . GLN A 1 312 ? 17.829 21.715 25.534 1.00 19.37 ? 312 GLN A O 1 ATOM 2385 C CB . GLN A 1 312 ? 15.511 23.100 24.738 1.00 17.05 ? 312 GLN A CB 1 ATOM 2386 C CG . GLN A 1 312 ? 14.540 23.680 23.713 1.00 17.65 ? 312 GLN A CG 1 ATOM 2387 C CD . GLN A 1 312 ? 15.052 23.520 22.299 1.00 18.47 ? 312 GLN A CD 1 ATOM 2388 O OE1 . GLN A 1 312 ? 15.882 24.304 21.848 1.00 19.42 ? 312 GLN A OE1 1 ATOM 2389 N NE2 . GLN A 1 312 ? 14.563 22.509 21.600 1.00 16.30 ? 312 GLN A NE2 1 ATOM 2390 N N . ASP A 1 313 ? 16.507 20.224 26.557 1.00 19.32 ? 313 ASP A N 1 ATOM 2391 C CA . ASP A 1 313 ? 17.532 19.820 27.535 1.00 20.62 ? 313 ASP A CA 1 ATOM 2392 C C . ASP A 1 313 ? 18.837 19.414 26.880 1.00 21.40 ? 313 ASP A C 1 ATOM 2393 O O . ASP A 1 313 ? 18.841 18.611 25.960 1.00 21.63 ? 313 ASP A O 1 ATOM 2394 C CB . ASP A 1 313 ? 17.048 18.658 28.376 1.00 20.65 ? 313 ASP A CB 1 ATOM 2395 C CG . ASP A 1 313 ? 17.807 18.541 29.681 1.00 20.48 ? 313 ASP A CG 1 ATOM 2396 O OD1 . ASP A 1 313 ? 18.996 18.148 29.661 1.00 21.85 ? 313 ASP A OD1 1 ATOM 2397 O OD2 . ASP A 1 313 ? 17.293 18.821 30.772 1.00 22.20 ? 313 ASP A OD2 1 ATOM 2398 N N . SER A 1 314 ? 19.950 19.963 27.362 1.00 22.64 ? 314 SER A N 1 ATOM 2399 C CA . SER A 1 314 ? 21.230 19.732 26.709 1.00 23.54 ? 314 SER A CA 1 ATOM 2400 C C . SER A 1 314 ? 22.110 18.697 27.407 1.00 23.72 ? 314 SER A C 1 ATOM 2401 O O . SER A 1 314 ? 23.256 18.481 27.013 1.00 24.03 ? 314 SER A O 1 ATOM 2402 C CB . SER A 1 314 ? 21.973 21.058 26.610 1.00 24.33 ? 314 SER A CB 1 ATOM 2403 O OG . SER A 1 314 ? 22.429 21.433 27.921 1.00 27.73 ? 314 SER A OG 1 ATOM 2404 N N . VAL A 1 315 ? 21.575 18.063 28.439 1.00 23.39 ? 315 VAL A N 1 ATOM 2405 C CA . VAL A 1 315 ? 22.275 17.031 29.176 1.00 23.36 ? 315 VAL A CA 1 ATOM 2406 C C . VAL A 1 315 ? 21.579 15.697 28.959 1.00 22.74 ? 315 VAL A C 1 ATOM 2407 O O . VAL A 1 315 ? 22.216 14.660 28.790 1.00 23.24 ? 315 VAL A O 1 ATOM 2408 C CB . VAL A 1 315 ? 22.263 17.343 30.706 1.00 23.32 ? 315 VAL A CB 1 ATOM 2409 C CG1 . VAL A 1 315 ? 23.001 16.274 31.487 1.00 24.22 ? 315 VAL A CG1 1 ATOM 2410 C CG2 . VAL A 1 315 ? 22.841 18.715 30.957 1.00 24.71 ? 315 VAL A CG2 1 ATOM 2411 N N . TYR A 1 316 ? 20.257 15.730 28.964 1.00 21.91 ? 316 TYR A N 1 ATOM 2412 C CA . TYR A 1 316 ? 19.473 14.527 28.775 1.00 22.02 ? 316 TYR A CA 1 ATOM 2413 C C . TYR A 1 316 ? 18.931 14.560 27.363 1.00 21.70 ? 316 TYR A C 1 ATOM 2414 O O . TYR A 1 316 ? 18.079 15.387 27.043 1.00 21.54 ? 316 TYR A O 1 ATOM 2415 C CB . TYR A 1 316 ? 18.326 14.473 29.774 1.00 22.06 ? 316 TYR A CB 1 ATOM 2416 C CG . TYR A 1 316 ? 18.819 14.375 31.191 1.00 24.60 ? 316 TYR A CG 1 ATOM 2417 C CD1 . TYR A 1 316 ? 19.205 15.512 31.893 1.00 26.68 ? 316 TYR A CD1 1 ATOM 2418 C CD2 . TYR A 1 316 ? 18.906 13.148 31.825 1.00 26.44 ? 316 TYR A CD2 1 ATOM 2419 C CE1 . TYR A 1 316 ? 19.665 15.428 33.199 1.00 28.59 ? 316 TYR A CE1 1 ATOM 2420 C CE2 . TYR A 1 316 ? 19.365 13.051 33.136 1.00 29.15 ? 316 TYR A CE2 1 ATOM 2421 C CZ . TYR A 1 316 ? 19.740 14.190 33.812 1.00 29.66 ? 316 TYR A CZ 1 ATOM 2422 O OH . TYR A 1 316 ? 20.193 14.088 35.102 1.00 30.32 ? 316 TYR A OH 1 ATOM 2423 N N . GLY A 1 317 ? 19.431 13.661 26.528 1.00 20.88 ? 317 GLY A N 1 ATOM 2424 C CA . GLY A 1 317 ? 19.017 13.612 25.139 1.00 20.57 ? 317 GLY A CA 1 ATOM 2425 C C . GLY A 1 317 ? 17.752 12.833 24.885 1.00 19.83 ? 317 GLY A C 1 ATOM 2426 O O . GLY A 1 317 ? 17.056 13.104 23.927 1.00 20.50 ? 317 GLY A O 1 ATOM 2427 N N . GLN A 1 318 ? 17.454 11.866 25.743 1.00 19.72 ? 318 GLN A N 1 ATOM 2428 C CA . GLN A 1 318 ? 16.286 11.022 25.543 1.00 19.68 ? 318 GLN A CA 1 ATOM 2429 C C . GLN A 1 318 ? 15.001 11.787 25.859 1.00 18.46 ? 318 GLN A C 1 ATOM 2430 O O . GLN A 1 318 ? 15.009 12.755 26.616 1.00 17.52 ? 318 GLN A O 1 ATOM 2431 C CB . GLN A 1 318 ? 16.388 9.751 26.389 1.00 20.93 ? 318 GLN A CB 1 ATOM 2432 C CG . GLN A 1 318 ? 17.436 8.718 25.881 1.00 26.86 ? 318 GLN A CG 1 ATOM 2433 C CD . GLN A 1 318 ? 17.145 8.188 24.483 1.00 33.04 ? 318 GLN A CD 1 ATOM 2434 O OE1 . GLN A 1 318 ? 15.978 7.916 24.122 1.00 39.25 ? 318 GLN A OE1 1 ATOM 2435 N NE2 . GLN A 1 318 ? 18.196 8.033 23.687 1.00 36.18 ? 318 GLN A NE2 1 ATOM 2436 N N . PRO A 1 319 ? 13.890 11.359 25.281 1.00 17.55 ? 319 PRO A N 1 ATOM 2437 C CA . PRO A 1 319 ? 12.623 12.010 25.563 1.00 16.88 ? 319 PRO A CA 1 ATOM 2438 C C . PRO A 1 319 ? 11.982 11.336 26.758 1.00 16.49 ? 319 PRO A C 1 ATOM 2439 O O . PRO A 1 319 ? 12.434 10.289 27.284 1.00 15.94 ? 319 PRO A O 1 ATOM 2440 C CB . PRO A 1 319 ? 11.822 11.717 24.298 1.00 16.20 ? 319 PRO A CB 1 ATOM 2441 C CG . PRO A 1 319 ? 12.228 10.316 23.986 1.00 17.26 ? 319 PRO A CG 1 ATOM 2442 C CD . PRO A 1 319 ? 13.718 10.246 24.329 1.00 17.29 ? 319 PRO A CD 1 ATOM 2443 N N . ALA A 1 320 ? 10.910 11.955 27.197 1.00 15.52 ? 320 ALA A N 1 ATOM 2444 C CA . ALA A 1 320 ? 10.025 11.297 28.132 1.00 15.18 ? 320 ALA A CA 1 ATOM 2445 C C . ALA A 1 320 ? 9.490 10.029 27.420 1.00 14.99 ? 320 ALA A C 1 ATOM 2446 O O . ALA A 1 320 ? 9.262 10.031 26.219 1.00 14.69 ? 320 ALA A O 1 ATOM 2447 C CB . ALA A 1 320 ? 8.898 12.237 28.495 1.00 14.20 ? 320 ALA A CB 1 ATOM 2448 N N . THR A 1 321 ? 9.294 8.953 28.169 1.00 15.09 ? 321 THR A N 1 ATOM 2449 C CA . THR A 1 321 ? 8.792 7.712 27.600 1.00 15.16 ? 321 THR A CA 1 ATOM 2450 C C . THR A 1 321 ? 7.656 7.246 28.450 1.00 15.16 ? 321 THR A C 1 ATOM 2451 O O . THR A 1 321 ? 7.569 7.650 29.588 1.00 15.17 ? 321 THR A O 1 ATOM 2452 C CB . THR A 1 321 ? 9.895 6.627 27.607 1.00 15.02 ? 321 THR A CB 1 ATOM 2453 O OG1 . THR A 1 321 ? 10.468 6.513 28.922 1.00 16.40 ? 321 THR A OG1 1 ATOM 2454 C CG2 . THR A 1 321 ? 11.085 7.090 26.753 1.00 14.23 ? 321 THR A CG2 1 ATOM 2455 N N . PRO A 1 322 ? 6.795 6.401 27.895 1.00 16.24 ? 322 PRO A N 1 ATOM 2456 C CA . PRO A 1 322 ? 5.673 5.839 28.638 1.00 16.83 ? 322 PRO A CA 1 ATOM 2457 C C . PRO A 1 322 ? 6.162 4.840 29.652 1.00 17.79 ? 322 PRO A C 1 ATOM 2458 O O . PRO A 1 322 ? 6.985 3.954 29.343 1.00 17.89 ? 322 PRO A O 1 ATOM 2459 C CB . PRO A 1 322 ? 4.824 5.136 27.570 1.00 16.46 ? 322 PRO A CB 1 ATOM 2460 C CG . PRO A 1 322 ? 5.614 5.127 26.325 1.00 17.19 ? 322 PRO A CG 1 ATOM 2461 C CD . PRO A 1 322 ? 6.850 5.924 26.503 1.00 15.83 ? 322 PRO A CD 1 ATOM 2462 N N . TYR A 1 323 ? 5.667 4.970 30.868 1.00 17.80 ? 323 TYR A N 1 ATOM 2463 C CA . TYR A 1 323 ? 6.034 3.989 31.875 1.00 18.92 ? 323 TYR A CA 1 ATOM 2464 C C . TYR A 1 323 ? 4.871 3.077 32.193 1.00 18.80 ? 323 TYR A C 1 ATOM 2465 O O . TYR A 1 323 ? 5.039 2.035 32.823 1.00 19.73 ? 323 TYR A O 1 ATOM 2466 C CB . TYR A 1 323 ? 6.604 4.638 33.124 1.00 18.42 ? 323 TYR A CB 1 ATOM 2467 C CG . TYR A 1 323 ? 5.675 5.535 33.904 1.00 19.14 ? 323 TYR A CG 1 ATOM 2468 C CD1 . TYR A 1 323 ? 4.854 5.025 34.903 1.00 18.92 ? 323 TYR A CD1 1 ATOM 2469 C CD2 . TYR A 1 323 ? 5.621 6.890 33.651 1.00 18.44 ? 323 TYR A CD2 1 ATOM 2470 C CE1 . TYR A 1 323 ? 4.006 5.854 35.619 1.00 20.37 ? 323 TYR A CE1 1 ATOM 2471 C CE2 . TYR A 1 323 ? 4.785 7.717 34.355 1.00 18.74 ? 323 TYR A CE2 1 ATOM 2472 C CZ . TYR A 1 323 ? 3.984 7.197 35.335 1.00 18.99 ? 323 TYR A CZ 1 ATOM 2473 O OH . TYR A 1 323 ? 3.161 8.043 36.020 1.00 20.13 ? 323 TYR A OH 1 ATOM 2474 N N . LYS A 1 324 ? 3.694 3.477 31.746 1.00 18.70 ? 324 LYS A N 1 ATOM 2475 C CA . LYS A 1 324 ? 2.505 2.723 32.002 1.00 19.15 ? 324 LYS A CA 1 ATOM 2476 C C . LYS A 1 324 ? 1.467 3.150 30.979 1.00 19.14 ? 324 LYS A C 1 ATOM 2477 O O . LYS A 1 324 ? 1.224 4.346 30.803 1.00 19.56 ? 324 LYS A O 1 ATOM 2478 C CB . LYS A 1 324 ? 2.037 3.046 33.411 1.00 19.16 ? 324 LYS A CB 1 ATOM 2479 C CG . LYS A 1 324 ? 0.723 2.494 33.750 1.00 19.58 ? 324 LYS A CG 1 ATOM 2480 C CD . LYS A 1 324 ? 0.549 2.462 35.286 1.00 22.39 ? 324 LYS A CD 1 ATOM 2481 C CE . LYS A 1 324 ? -0.155 3.717 35.797 1.00 23.28 ? 324 LYS A CE 1 ATOM 2482 N NZ . LYS A 1 324 ? -0.507 3.596 37.237 1.00 23.15 ? 324 LYS A NZ 1 ATOM 2483 N N . TRP A 1 325 ? 0.859 2.177 30.306 1.00 18.87 ? 325 TRP A N 1 ATOM 2484 C CA . TRP A 1 325 ? -0.100 2.488 29.254 1.00 19.61 ? 325 TRP A CA 1 ATOM 2485 C C . TRP A 1 325 ? -1.420 2.983 29.808 1.00 19.77 ? 325 TRP A C 1 ATOM 2486 O O . TRP A 1 325 ? -1.998 3.933 29.289 1.00 21.07 ? 325 TRP A O 1 ATOM 2487 C CB . TRP A 1 325 ? -0.281 1.308 28.288 1.00 19.42 ? 325 TRP A CB 1 ATOM 2488 C CG . TRP A 1 325 ? 0.563 1.466 27.029 1.00 19.90 ? 325 TRP A CG 1 ATOM 2489 C CD1 . TRP A 1 325 ? 0.105 1.648 25.766 1.00 20.69 ? 325 TRP A CD1 1 ATOM 2490 C CD2 . TRP A 1 325 ? 1.997 1.458 26.934 1.00 19.37 ? 325 TRP A CD2 1 ATOM 2491 N NE1 . TRP A 1 325 ? 1.152 1.751 24.886 1.00 22.19 ? 325 TRP A NE1 1 ATOM 2492 C CE2 . TRP A 1 325 ? 2.327 1.639 25.576 1.00 20.24 ? 325 TRP A CE2 1 ATOM 2493 C CE3 . TRP A 1 325 ? 3.038 1.313 27.859 1.00 18.42 ? 325 TRP A CE3 1 ATOM 2494 C CZ2 . TRP A 1 325 ? 3.640 1.682 25.118 1.00 19.23 ? 325 TRP A CZ2 1 ATOM 2495 C CZ3 . TRP A 1 325 ? 4.346 1.354 27.403 1.00 17.97 ? 325 TRP A CZ3 1 ATOM 2496 C CH2 . TRP A 1 325 ? 4.637 1.537 26.041 1.00 18.66 ? 325 TRP A CH2 1 ATOM 2497 N N . GLY A 1 326 ? -1.908 2.349 30.862 1.00 20.11 ? 326 GLY A N 1 ATOM 2498 C CA . GLY A 1 326 ? -3.116 2.832 31.499 1.00 19.70 ? 326 GLY A CA 1 ATOM 2499 C C . GLY A 1 326 ? -4.294 1.960 31.190 1.00 20.33 ? 326 GLY A C 1 ATOM 2500 O O . GLY A 1 326 ? -4.400 0.844 31.699 1.00 20.48 ? 326 GLY A O 1 ATOM 2501 N N . ILE A 1 327 ? -5.199 2.450 30.352 1.00 19.90 ? 327 ILE A N 1 ATOM 2502 C CA . ILE A 1 327 ? -6.379 1.662 30.086 1.00 20.25 ? 327 ILE A CA 1 ATOM 2503 C C . ILE A 1 327 ? -6.009 0.303 29.473 1.00 20.69 ? 327 ILE A C 1 ATOM 2504 O O . ILE A 1 327 ? -6.561 -0.739 29.863 1.00 20.52 ? 327 ILE A O 1 ATOM 2505 C CB . ILE A 1 327 ? -7.435 2.446 29.278 1.00 20.49 ? 327 ILE A CB 1 ATOM 2506 C CG1 . ILE A 1 327 ? -8.803 1.775 29.455 1.00 22.73 ? 327 ILE A CG1 1 ATOM 2507 C CG2 . ILE A 1 327 ? -7.040 2.617 27.786 1.00 19.98 ? 327 ILE A CG2 1 ATOM 2508 C CD1 . ILE A 1 327 ? -9.914 2.435 28.696 1.00 22.05 ? 327 ILE A CD1 1 ATOM 2509 N N . ASN A 1 328 ? -5.079 0.313 28.525 1.00 19.51 ? 328 ASN A N 1 ATOM 2510 C CA . ASN A 1 328 ? -4.570 -0.938 27.972 1.00 20.33 ? 328 ASN A CA 1 ATOM 2511 C C . ASN A 1 328 ? -3.331 -1.502 28.705 1.00 20.16 ? 328 ASN A C 1 ATOM 2512 O O . ASN A 1 328 ? -2.675 -0.795 29.464 1.00 19.93 ? 328 ASN A O 1 ATOM 2513 C CB . ASN A 1 328 ? -4.288 -0.767 26.484 1.00 19.39 ? 328 ASN A CB 1 ATOM 2514 C CG . ASN A 1 328 ? -5.546 -0.439 25.699 1.00 20.50 ? 328 ASN A CG 1 ATOM 2515 O OD1 . ASN A 1 328 ? -6.635 -0.809 26.102 1.00 21.87 ? 328 ASN A OD1 1 ATOM 2516 N ND2 . ASN A 1 328 ? -5.398 0.259 24.578 1.00 21.61 ? 328 ASN A ND2 1 ATOM 2517 N N . PRO A 1 329 ? -3.022 -2.776 28.476 1.00 20.18 ? 329 PRO A N 1 ATOM 2518 C CA . PRO A 1 329 ? -1.765 -3.359 28.955 1.00 20.09 ? 329 PRO A CA 1 ATOM 2519 C C . PRO A 1 329 ? -0.577 -2.574 28.401 1.00 20.54 ? 329 PRO A C 1 ATOM 2520 O O . PRO A 1 329 ? -0.688 -2.019 27.295 1.00 20.54 ? 329 PRO A O 1 ATOM 2521 C CB . PRO A 1 329 ? -1.810 -4.767 28.362 1.00 20.45 ? 329 PRO A CB 1 ATOM 2522 C CG . PRO A 1 329 ? -3.265 -5.070 28.295 1.00 19.82 ? 329 PRO A CG 1 ATOM 2523 C CD . PRO A 1 329 ? -3.848 -3.767 27.755 1.00 20.85 ? 329 PRO A CD 1 ATOM 2524 N N . ASP A 1 330 ? 0.529 -2.516 29.137 1.00 20.28 ? 330 ASP A N 1 ATOM 2525 C CA . ASP A 1 330 ? 1.731 -1.877 28.606 1.00 20.42 ? 330 ASP A CA 1 ATOM 2526 C C . ASP A 1 330 ? 2.088 -2.443 27.237 1.00 19.84 ? 330 ASP A C 1 ATOM 2527 O O . ASP A 1 330 ? 1.860 -3.617 26.973 1.00 19.52 ? 330 ASP A O 1 ATOM 2528 C CB . ASP A 1 330 ? 2.932 -2.082 29.515 1.00 20.24 ? 330 ASP A CB 1 ATOM 2529 C CG . ASP A 1 330 ? 2.759 -1.431 30.837 1.00 20.99 ? 330 ASP A CG 1 ATOM 2530 O OD1 . ASP A 1 330 ? 1.845 -0.585 30.960 1.00 19.73 ? 330 ASP A OD1 1 ATOM 2531 O OD2 . ASP A 1 330 ? 3.494 -1.711 31.801 1.00 20.65 ? 330 ASP A OD2 1 ATOM 2532 N N . TRP A 1 331 ? 2.651 -1.585 26.391 1.00 19.18 ? 331 TRP A N 1 ATOM 2533 C CA . TRP A 1 331 ? 3.034 -1.926 25.033 1.00 19.76 ? 331 TRP A CA 1 ATOM 2534 C C . TRP A 1 331 ? 1.882 -2.352 24.141 1.00 19.49 ? 331 TRP A C 1 ATOM 2535 O O . TRP A 1 331 ? 2.043 -3.204 23.274 1.00 19.80 ? 331 TRP A O 1 ATOM 2536 C CB . TRP A 1 331 ? 4.186 -2.937 25.014 1.00 19.85 ? 331 TRP A CB 1 ATOM 2537 C CG . TRP A 1 331 ? 5.372 -2.357 25.693 1.00 20.54 ? 331 TRP A CG 1 ATOM 2538 C CD1 . TRP A 1 331 ? 6.169 -1.346 25.235 1.00 19.83 ? 331 TRP A CD1 1 ATOM 2539 C CD2 . TRP A 1 331 ? 5.898 -2.745 26.953 1.00 20.81 ? 331 TRP A CD2 1 ATOM 2540 N NE1 . TRP A 1 331 ? 7.166 -1.088 26.145 1.00 20.51 ? 331 TRP A NE1 1 ATOM 2541 C CE2 . TRP A 1 331 ? 7.019 -1.935 27.208 1.00 21.43 ? 331 TRP A CE2 1 ATOM 2542 C CE3 . TRP A 1 331 ? 5.536 -3.702 27.899 1.00 22.56 ? 331 TRP A CE3 1 ATOM 2543 C CZ2 . TRP A 1 331 ? 7.780 -2.052 28.371 1.00 23.95 ? 331 TRP A CZ2 1 ATOM 2544 C CZ3 . TRP A 1 331 ? 6.287 -3.818 29.046 1.00 24.76 ? 331 TRP A CZ3 1 ATOM 2545 C CH2 . TRP A 1 331 ? 7.399 -2.997 29.274 1.00 25.14 ? 331 TRP A CH2 1 ATOM 2546 N N . THR A 1 332 ? 0.715 -1.759 24.352 1.00 19.34 ? 332 THR A N 1 ATOM 2547 C CA . THR A 1 332 ? -0.393 -2.022 23.473 1.00 19.47 ? 332 THR A CA 1 ATOM 2548 C C . THR A 1 332 ? -0.514 -0.940 22.434 1.00 19.63 ? 332 THR A C 1 ATOM 2549 O O . THR A 1 332 ? -0.779 0.224 22.745 1.00 18.73 ? 332 THR A O 1 ATOM 2550 C CB . THR A 1 332 ? -1.714 -2.071 24.202 1.00 19.97 ? 332 THR A CB 1 ATOM 2551 O OG1 . THR A 1 332 ? -1.657 -3.061 25.231 1.00 20.45 ? 332 THR A OG1 1 ATOM 2552 C CG2 . THR A 1 332 ? -2.811 -2.571 23.219 1.00 19.27 ? 332 THR A CG2 1 ATOM 2553 N N . PHE A 1 333 ? -0.320 -1.343 21.193 1.00 19.90 ? 333 PHE A N 1 ATOM 2554 C CA . PHE A 1 333 ? -0.524 -0.459 20.071 1.00 19.60 ? 333 PHE A CA 1 ATOM 2555 C C . PHE A 1 333 ? -2.016 -0.227 19.929 1.00 19.72 ? 333 PHE A C 1 ATOM 2556 O O . PHE A 1 333 ? -2.773 -1.165 19.691 1.00 20.52 ? 333 PHE A O 1 ATOM 2557 C CB . PHE A 1 333 ? -0.008 -1.134 18.814 1.00 19.21 ? 333 PHE A CB 1 ATOM 2558 C CG . PHE A 1 333 ? -0.122 -0.296 17.601 1.00 19.31 ? 333 PHE A CG 1 ATOM 2559 C CD1 . PHE A 1 333 ? -1.285 -0.313 16.828 1.00 20.29 ? 333 PHE A CD1 1 ATOM 2560 C CD2 . PHE A 1 333 ? 0.927 0.518 17.217 1.00 20.11 ? 333 PHE A CD2 1 ATOM 2561 C CE1 . PHE A 1 333 ? -1.394 0.473 15.683 1.00 18.93 ? 333 PHE A CE1 1 ATOM 2562 C CE2 . PHE A 1 333 ? 0.819 1.305 16.077 1.00 19.81 ? 333 PHE A CE2 1 ATOM 2563 C CZ . PHE A 1 333 ? -0.340 1.280 15.316 1.00 17.84 ? 333 PHE A CZ 1 ATOM 2564 N N . ASN A 1 334 ? -2.449 1.016 20.071 1.00 19.04 ? 334 ASN A N 1 ATOM 2565 C CA . ASN A 1 334 ? -3.871 1.311 19.992 1.00 18.92 ? 334 ASN A CA 1 ATOM 2566 C C . ASN A 1 334 ? -4.041 2.764 19.584 1.00 18.73 ? 334 ASN A C 1 ATOM 2567 O O . ASN A 1 334 ? -3.665 3.670 20.327 1.00 18.64 ? 334 ASN A O 1 ATOM 2568 C CB . ASN A 1 334 ? -4.527 1.058 21.350 1.00 18.97 ? 334 ASN A CB 1 ATOM 2569 C CG . ASN A 1 334 ? -6.015 1.224 21.311 1.00 18.83 ? 334 ASN A CG 1 ATOM 2570 O OD1 . ASN A 1 334 ? -6.530 2.271 20.915 1.00 17.45 ? 334 ASN A OD1 1 ATOM 2571 N ND2 . ASN A 1 334 ? -6.721 0.173 21.725 1.00 21.75 ? 334 ASN A ND2 1 ATOM 2572 N N . VAL A 1 335 ? -4.605 2.985 18.409 1.00 18.30 ? 335 VAL A N 1 ATOM 2573 C CA . VAL A 1 335 ? -4.656 4.334 17.839 1.00 18.92 ? 335 VAL A CA 1 ATOM 2574 C C . VAL A 1 335 ? -5.506 5.363 18.586 1.00 19.06 ? 335 VAL A C 1 ATOM 2575 O O . VAL A 1 335 ? -5.262 6.562 18.513 1.00 19.40 ? 335 VAL A O 1 ATOM 2576 C CB . VAL A 1 335 ? -5.080 4.286 16.345 1.00 19.03 ? 335 VAL A CB 1 ATOM 2577 C CG1 . VAL A 1 335 ? -4.090 3.489 15.594 1.00 19.95 ? 335 VAL A CG1 1 ATOM 2578 C CG2 . VAL A 1 335 ? -6.434 3.644 16.188 1.00 18.87 ? 335 VAL A CG2 1 ATOM 2579 N N . THR A 1 336 ? -6.503 4.892 19.305 1.00 18.41 ? 336 THR A N 1 ATOM 2580 C CA . THR A 1 336 ? -7.440 5.769 19.971 1.00 18.71 ? 336 THR A CA 1 ATOM 2581 C C . THR A 1 336 ? -7.063 5.961 21.422 1.00 17.55 ? 336 THR A C 1 ATOM 2582 O O . THR A 1 336 ? -7.328 7.003 22.004 1.00 17.31 ? 336 THR A O 1 ATOM 2583 C CB . THR A 1 336 ? -8.841 5.140 19.898 1.00 17.83 ? 336 THR A CB 1 ATOM 2584 O OG1 . THR A 1 336 ? -9.266 5.172 18.541 1.00 22.23 ? 336 THR A OG1 1 ATOM 2585 C CG2 . THR A 1 336 ? -9.839 6.056 20.528 1.00 19.96 ? 336 THR A CG2 1 ATOM 2586 N N . TYR A 1 337 ? -6.439 4.933 21.985 1.00 16.86 ? 337 TYR A N 1 ATOM 2587 C CA . TYR A 1 337 ? -6.071 4.913 23.384 1.00 17.92 ? 337 TYR A CA 1 ATOM 2588 C C . TYR A 1 337 ? -4.567 4.611 23.579 1.00 17.28 ? 337 TYR A C 1 ATOM 2589 O O . TYR A 1 337 ? -4.177 3.508 23.970 1.00 17.22 ? 337 TYR A O 1 ATOM 2590 C CB . TYR A 1 337 ? -6.977 3.915 24.114 1.00 18.47 ? 337 TYR A CB 1 ATOM 2591 C CG . TYR A 1 337 ? -8.382 4.444 24.164 1.00 20.29 ? 337 TYR A CG 1 ATOM 2592 C CD1 . TYR A 1 337 ? -9.319 4.067 23.226 1.00 20.54 ? 337 TYR A CD1 1 ATOM 2593 C CD2 . TYR A 1 337 ? -8.764 5.334 25.158 1.00 21.17 ? 337 TYR A CD2 1 ATOM 2594 C CE1 . TYR A 1 337 ? -10.610 4.559 23.273 1.00 24.75 ? 337 TYR A CE1 1 ATOM 2595 C CE2 . TYR A 1 337 ? -10.025 5.824 25.218 1.00 23.73 ? 337 TYR A CE2 1 ATOM 2596 C CZ . TYR A 1 337 ? -10.954 5.436 24.271 1.00 25.64 ? 337 TYR A CZ 1 ATOM 2597 O OH . TYR A 1 337 ? -12.232 5.931 24.329 1.00 29.72 ? 337 TYR A OH 1 ATOM 2598 N N . PRO A 1 338 ? -3.727 5.604 23.299 1.00 16.65 ? 338 PRO A N 1 ATOM 2599 C CA . PRO A 1 338 ? -2.277 5.406 23.376 1.00 15.74 ? 338 PRO A CA 1 ATOM 2600 C C . PRO A 1 338 ? -1.854 5.421 24.837 1.00 15.70 ? 338 PRO A C 1 ATOM 2601 O O . PRO A 1 338 ? -2.679 5.664 25.720 1.00 15.14 ? 338 PRO A O 1 ATOM 2602 C CB . PRO A 1 338 ? -1.693 6.639 22.679 1.00 16.31 ? 338 PRO A CB 1 ATOM 2603 C CG . PRO A 1 338 ? -2.794 7.680 22.662 1.00 17.47 ? 338 PRO A CG 1 ATOM 2604 C CD . PRO A 1 338 ? -4.103 6.970 22.904 1.00 15.86 ? 338 PRO A CD 1 ATOM 2605 N N . ALA A 1 339 ? -0.575 5.162 25.073 1.00 15.48 ? 339 ALA A N 1 ATOM 2606 C CA . ALA A 1 339 ? 0.025 5.176 26.398 1.00 15.33 ? 339 ALA A CA 1 ATOM 2607 C C . ALA A 1 339 ? -0.306 6.464 27.144 1.00 15.93 ? 339 ALA A C 1 ATOM 2608 O O . ALA A 1 339 ? -0.211 7.557 26.590 1.00 16.47 ? 339 ALA A O 1 ATOM 2609 C CB . ALA A 1 339 ? 1.497 5.023 26.266 1.00 13.91 ? 339 ALA A CB 1 ATOM 2610 N N . GLU A 1 340 ? -0.693 6.341 28.407 1.00 15.70 ? 340 GLU A N 1 ATOM 2611 C CA . GLU A 1 340 ? -1.209 7.510 29.109 1.00 16.39 ? 340 GLU A CA 1 ATOM 2612 C C . GLU A 1 340 ? -0.206 8.141 30.045 1.00 16.05 ? 340 GLU A C 1 ATOM 2613 O O . GLU A 1 340 ? -0.258 9.348 30.265 1.00 16.17 ? 340 GLU A O 1 ATOM 2614 C CB . GLU A 1 340 ? -2.454 7.138 29.925 1.00 16.16 ? 340 GLU A CB 1 ATOM 2615 C CG . GLU A 1 340 ? -3.690 6.750 29.113 1.00 16.54 ? 340 GLU A CG 1 ATOM 2616 C CD . GLU A 1 340 ? -4.578 5.785 29.886 1.00 18.16 ? 340 GLU A CD 1 ATOM 2617 O OE1 . GLU A 1 340 ? -4.594 5.880 31.121 1.00 17.03 ? 340 GLU A OE1 1 ATOM 2618 O OE2 . GLU A 1 340 ? -5.248 4.937 29.267 1.00 17.61 ? 340 GLU A OE2 1 ATOM 2619 N N . PHE A 1 341 ? 0.692 7.315 30.583 1.00 15.79 ? 341 PHE A N 1 ATOM 2620 C CA . PHE A 1 341 ? 1.642 7.735 31.613 1.00 16.32 ? 341 PHE A CA 1 ATOM 2621 C C . PHE A 1 341 ? 3.072 7.844 31.118 1.00 16.63 ? 341 PHE A C 1 ATOM 2622 O O . PHE A 1 341 ? 3.687 6.847 30.736 1.00 17.22 ? 341 PHE A O 1 ATOM 2623 C CB . PHE A 1 341 ? 1.577 6.772 32.804 1.00 16.44 ? 341 PHE A CB 1 ATOM 2624 C CG . PHE A 1 341 ? 0.247 6.780 33.502 1.00 16.49 ? 341 PHE A CG 1 ATOM 2625 C CD1 . PHE A 1 341 ? -0.824 6.078 32.988 1.00 15.46 ? 341 PHE A CD1 1 ATOM 2626 C CD2 . PHE A 1 341 ? 0.079 7.499 34.673 1.00 18.45 ? 341 PHE A CD2 1 ATOM 2627 C CE1 . PHE A 1 341 ? -2.066 6.092 33.651 1.00 19.52 ? 341 PHE A CE1 1 ATOM 2628 C CE2 . PHE A 1 341 ? -1.136 7.518 35.326 1.00 19.51 ? 341 PHE A CE2 1 ATOM 2629 C CZ . PHE A 1 341 ? -2.212 6.814 34.817 1.00 18.43 ? 341 PHE A CZ 1 ATOM 2630 N N . TRP A 1 342 ? 3.584 9.067 31.138 1.00 16.09 ? 342 TRP A N 1 ATOM 2631 C CA . TRP A 1 342 ? 4.872 9.384 30.556 1.00 16.46 ? 342 TRP A CA 1 ATOM 2632 C C . TRP A 1 342 ? 5.764 10.114 31.530 1.00 16.47 ? 342 TRP A C 1 ATOM 2633 O O . TRP A 1 342 ? 5.295 10.936 32.312 1.00 16.05 ? 342 TRP A O 1 ATOM 2634 C CB . TRP A 1 342 ? 4.672 10.298 29.353 1.00 16.73 ? 342 TRP A CB 1 ATOM 2635 C CG . TRP A 1 342 ? 3.889 9.714 28.242 1.00 17.30 ? 342 TRP A CG 1 ATOM 2636 C CD1 . TRP A 1 342 ? 2.569 9.386 28.237 1.00 18.15 ? 342 TRP A CD1 1 ATOM 2637 C CD2 . TRP A 1 342 ? 4.386 9.389 26.953 1.00 19.66 ? 342 TRP A CD2 1 ATOM 2638 N NE1 . TRP A 1 342 ? 2.209 8.870 27.014 1.00 19.23 ? 342 TRP A NE1 1 ATOM 2639 C CE2 . TRP A 1 342 ? 3.311 8.862 26.204 1.00 18.88 ? 342 TRP A CE2 1 ATOM 2640 C CE3 . TRP A 1 342 ? 5.645 9.488 26.344 1.00 17.97 ? 342 TRP A CE3 1 ATOM 2641 C CZ2 . TRP A 1 342 ? 3.455 8.437 24.882 1.00 18.59 ? 342 TRP A CZ2 1 ATOM 2642 C CZ3 . TRP A 1 342 ? 5.786 9.068 25.029 1.00 17.92 ? 342 TRP A CZ3 1 ATOM 2643 C CH2 . TRP A 1 342 ? 4.695 8.547 24.317 1.00 16.60 ? 342 TRP A CH2 1 ATOM 2644 N N . ALA A 1 343 ? 7.057 9.805 31.468 1.00 16.27 ? 343 ALA A N 1 ATOM 2645 C CA . ALA A 1 343 ? 8.032 10.445 32.314 1.00 16.56 ? 343 ALA A CA 1 ATOM 2646 C C . ALA A 1 343 ? 9.410 10.400 31.679 1.00 16.68 ? 343 ALA A C 1 ATOM 2647 O O . ALA A 1 343 ? 9.759 9.467 30.966 1.00 16.27 ? 343 ALA A O 1 ATOM 2648 C CB . ALA A 1 343 ? 8.072 9.772 33.683 1.00 16.93 ? 343 ALA A CB 1 ATOM 2649 N N . GLY A 1 344 ? 10.182 11.430 31.951 1.00 16.99 ? 344 GLY A N 1 ATOM 2650 C CA . GLY A 1 344 ? 11.580 11.419 31.611 1.00 17.66 ? 344 GLY A CA 1 ATOM 2651 C C . GLY A 1 344 ? 12.331 12.384 32.477 1.00 18.01 ? 344 GLY A C 1 ATOM 2652 O O . GLY A 1 344 ? 11.761 13.388 32.933 1.00 17.58 ? 344 GLY A O 1 ATOM 2653 N N . PRO A 1 345 ? 13.608 12.087 32.710 1.00 18.91 ? 345 PRO A N 1 ATOM 2654 C CA . PRO A 1 345 ? 14.476 12.985 33.478 1.00 19.55 ? 345 PRO A CA 1 ATOM 2655 C C . PRO A 1 345 ? 14.868 14.195 32.658 1.00 19.81 ? 345 PRO A C 1 ATOM 2656 O O . PRO A 1 345 ? 14.819 14.155 31.441 1.00 19.36 ? 345 PRO A O 1 ATOM 2657 C CB . PRO A 1 345 ? 15.712 12.123 33.770 1.00 19.37 ? 345 PRO A CB 1 ATOM 2658 C CG . PRO A 1 345 ? 15.750 11.126 32.664 1.00 20.34 ? 345 PRO A CG 1 ATOM 2659 C CD . PRO A 1 345 ? 14.308 10.869 32.260 1.00 18.46 ? 345 PRO A CD 1 ATOM 2660 N N . SER A 1 346 ? 15.252 15.261 33.338 1.00 20.35 ? 346 SER A N 1 ATOM 2661 C CA . SER A 1 346 ? 15.787 16.451 32.698 1.00 21.80 ? 346 SER A CA 1 ATOM 2662 C C . SER A 1 346 ? 16.649 17.189 33.726 1.00 22.86 ? 346 SER A C 1 ATOM 2663 O O . SER A 1 346 ? 16.721 16.778 34.883 1.00 23.29 ? 346 SER A O 1 ATOM 2664 C CB . SER A 1 346 ? 14.668 17.377 32.232 1.00 21.27 ? 346 SER A CB 1 ATOM 2665 O OG . SER A 1 346 ? 14.160 18.107 33.337 1.00 22.14 ? 346 SER A OG 1 ATOM 2666 N N . SER A 1 347 ? 17.295 18.273 33.305 1.00 23.83 ? 347 SER A N 1 ATOM 2667 C CA . SER A 1 347 ? 18.123 19.075 34.204 1.00 25.22 ? 347 SER A CA 1 ATOM 2668 C C . SER A 1 347 ? 17.275 19.718 35.305 1.00 25.97 ? 347 SER A C 1 ATOM 2669 O O . SER A 1 347 ? 17.740 19.921 36.429 1.00 25.54 ? 347 SER A O 1 ATOM 2670 C CB . SER A 1 347 ? 18.878 20.145 33.408 1.00 25.16 ? 347 SER A CB 1 ATOM 2671 O OG . SER A 1 347 ? 19.772 19.531 32.484 1.00 26.40 ? 347 SER A OG 1 ATOM 2672 N N . LYS A 1 348 ? 16.030 20.033 34.969 1.00 26.62 ? 348 LYS A N 1 ATOM 2673 C CA . LYS A 1 348 ? 15.121 20.686 35.904 1.00 27.59 ? 348 LYS A CA 1 ATOM 2674 C C . LYS A 1 348 ? 14.399 19.727 36.836 1.00 27.28 ? 348 LYS A C 1 ATOM 2675 O O . LYS A 1 348 ? 13.709 20.160 37.756 1.00 28.02 ? 348 LYS A O 1 ATOM 2676 C CB . LYS A 1 348 ? 14.079 21.485 35.135 1.00 28.65 ? 348 LYS A CB 1 ATOM 2677 C CG . LYS A 1 348 ? 14.286 22.984 35.147 1.00 31.21 ? 348 LYS A CG 1 ATOM 2678 C CD . LYS A 1 348 ? 15.527 23.368 34.378 1.00 35.08 ? 348 LYS A CD 1 ATOM 2679 C CE . LYS A 1 348 ? 16.673 23.724 35.308 1.00 35.24 ? 348 LYS A CE 1 ATOM 2680 N NZ . LYS A 1 348 ? 17.973 23.432 34.624 1.00 37.16 ? 348 LYS A NZ 1 ATOM 2681 N N . GLY A 1 349 ? 14.556 18.431 36.604 1.00 26.20 ? 349 GLY A N 1 ATOM 2682 C CA . GLY A 1 349 ? 13.801 17.452 37.362 1.00 25.47 ? 349 GLY A CA 1 ATOM 2683 C C . GLY A 1 349 ? 13.070 16.466 36.454 1.00 24.53 ? 349 GLY A C 1 ATOM 2684 O O . GLY A 1 349 ? 13.221 16.509 35.236 1.00 24.96 ? 349 GLY A O 1 ATOM 2685 N N . HIS A 1 350 ? 12.274 15.570 37.033 1.00 24.01 ? 350 HIS A N 1 ATOM 2686 C CA . HIS A 1 350 ? 11.570 14.576 36.218 1.00 23.41 ? 350 HIS A CA 1 ATOM 2687 C C . HIS A 1 350 ? 10.249 15.153 35.746 1.00 22.14 ? 350 HIS A C 1 ATOM 2688 O O . HIS A 1 350 ? 9.466 15.679 36.536 1.00 21.87 ? 350 HIS A O 1 ATOM 2689 C CB . HIS A 1 350 ? 11.324 13.261 36.966 1.00 23.90 ? 350 HIS A CB 1 ATOM 2690 C CG . HIS A 1 350 ? 12.506 12.348 36.989 1.00 27.47 ? 350 HIS A CG 1 ATOM 2691 N ND1 . HIS A 1 350 ? 12.560 11.180 36.257 1.00 30.49 ? 350 HIS A ND1 1 ATOM 2692 C CD2 . HIS A 1 350 ? 13.680 12.431 37.656 1.00 30.76 ? 350 HIS A CD2 1 ATOM 2693 C CE1 . HIS A 1 350 ? 13.717 10.581 36.473 1.00 32.10 ? 350 HIS A CE1 1 ATOM 2694 N NE2 . HIS A 1 350 ? 14.415 11.321 37.318 1.00 32.31 ? 350 HIS A NE2 1 ATOM 2695 N N . LEU A 1 351 ? 10.012 15.050 34.449 1.00 20.40 ? 351 LEU A N 1 ATOM 2696 C CA . LEU A 1 351 ? 8.763 15.505 33.889 1.00 19.06 ? 351 LEU A CA 1 ATOM 2697 C C . LEU A 1 351 ? 7.841 14.312 33.877 1.00 18.28 ? 351 LEU A C 1 ATOM 2698 O O . LEU A 1 351 ? 8.214 13.237 33.433 1.00 17.98 ? 351 LEU A O 1 ATOM 2699 C CB . LEU A 1 351 ? 8.967 16.007 32.469 1.00 18.58 ? 351 LEU A CB 1 ATOM 2700 C CG . LEU A 1 351 ? 7.755 16.666 31.796 1.00 19.54 ? 351 LEU A CG 1 ATOM 2701 C CD1 . LEU A 1 351 ? 7.398 17.937 32.523 1.00 18.14 ? 351 LEU A CD1 1 ATOM 2702 C CD2 . LEU A 1 351 ? 8.112 16.961 30.357 1.00 17.62 ? 351 LEU A CD2 1 ATOM 2703 N N . VAL A 1 352 ? 6.630 14.502 34.366 1.00 17.51 ? 352 VAL A N 1 ATOM 2704 C CA . VAL A 1 352 ? 5.650 13.429 34.360 1.00 17.20 ? 352 VAL A CA 1 ATOM 2705 C C . VAL A 1 352 ? 4.395 13.959 33.659 1.00 17.13 ? 352 VAL A C 1 ATOM 2706 O O . VAL A 1 352 ? 3.934 15.055 33.939 1.00 16.73 ? 352 VAL A O 1 ATOM 2707 C CB . VAL A 1 352 ? 5.344 12.926 35.772 1.00 17.18 ? 352 VAL A CB 1 ATOM 2708 C CG1 . VAL A 1 352 ? 4.370 11.775 35.719 1.00 17.58 ? 352 VAL A CG1 1 ATOM 2709 C CG2 . VAL A 1 352 ? 6.647 12.477 36.454 1.00 17.36 ? 352 VAL A CG2 1 ATOM 2710 N N . LEU A 1 353 ? 3.855 13.172 32.744 1.00 16.68 ? 353 LEU A N 1 ATOM 2711 C CA . LEU A 1 353 ? 2.685 13.583 31.977 1.00 17.13 ? 353 LEU A CA 1 ATOM 2712 C C . LEU A 1 353 ? 1.657 12.465 32.058 1.00 17.27 ? 353 LEU A C 1 ATOM 2713 O O . LEU A 1 353 ? 1.978 11.292 31.908 1.00 18.50 ? 353 LEU A O 1 ATOM 2714 C CB . LEU A 1 353 ? 3.058 13.875 30.523 1.00 16.72 ? 353 LEU A CB 1 ATOM 2715 C CG . LEU A 1 353 ? 4.235 14.834 30.273 1.00 16.29 ? 353 LEU A CG 1 ATOM 2716 C CD1 . LEU A 1 353 ? 5.536 14.080 30.176 1.00 15.51 ? 353 LEU A CD1 1 ATOM 2717 C CD2 . LEU A 1 353 ? 4.026 15.666 28.990 1.00 13.34 ? 353 LEU A CD2 1 ATOM 2718 N N . MET A 1 354 ? 0.414 12.825 32.297 1.00 16.69 ? 354 MET A N 1 ATOM 2719 C CA . MET A 1 354 ? -0.632 11.833 32.422 1.00 17.03 ? 354 MET A CA 1 ATOM 2720 C C . MET A 1 354 ? -1.749 12.293 31.522 1.00 16.96 ? 354 MET A C 1 ATOM 2721 O O . MET A 1 354 ? -2.365 13.329 31.785 1.00 16.16 ? 354 MET A O 1 ATOM 2722 C CB . MET A 1 354 ? -1.074 11.749 33.880 1.00 16.99 ? 354 MET A CB 1 ATOM 2723 C CG . MET A 1 354 ? 0.117 11.446 34.815 1.00 16.95 ? 354 MET A CG 1 ATOM 2724 S SD . MET A 1 354 ? -0.470 10.965 36.407 1.00 21.50 ? 354 MET A SD 1 ATOM 2725 C CE . MET A 1 354 ? -0.847 12.609 37.097 1.00 20.52 ? 354 MET A CE 1 ATOM 2726 N N . VAL A 1 355 ? -1.986 11.513 30.465 1.00 16.92 ? 355 VAL A N 1 ATOM 2727 C CA . VAL A 1 355 ? -2.912 11.877 29.415 1.00 17.10 ? 355 VAL A CA 1 ATOM 2728 C C . VAL A 1 355 ? -4.218 11.213 29.685 1.00 17.28 ? 355 VAL A C 1 ATOM 2729 O O . VAL A 1 355 ? -4.284 9.994 29.811 1.00 17.49 ? 355 VAL A O 1 ATOM 2730 C CB . VAL A 1 355 ? -2.450 11.399 28.019 1.00 16.93 ? 355 VAL A CB 1 ATOM 2731 C CG1 . VAL A 1 355 ? -3.518 11.765 26.963 1.00 15.55 ? 355 VAL A CG1 1 ATOM 2732 C CG2 . VAL A 1 355 ? -1.110 11.994 27.669 1.00 18.61 ? 355 VAL A CG2 1 ATOM 2733 N N . ASN A 1 356 ? -5.264 12.011 29.778 1.00 17.33 ? 356 ASN A N 1 ATOM 2734 C CA . ASN A 1 356 ? -6.570 11.415 29.912 1.00 17.31 ? 356 ASN A CA 1 ATOM 2735 C C . ASN A 1 356 ? -7.142 11.184 28.532 1.00 16.74 ? 356 ASN A C 1 ATOM 2736 O O . ASN A 1 356 ? -7.674 12.088 27.900 1.00 16.71 ? 356 ASN A O 1 ATOM 2737 C CB . ASN A 1 356 ? -7.511 12.261 30.763 1.00 17.71 ? 356 ASN A CB 1 ATOM 2738 C CG . ASN A 1 356 ? -8.876 11.641 30.865 1.00 17.84 ? 356 ASN A CG 1 ATOM 2739 O OD1 . ASN A 1 356 ? -9.023 10.437 30.648 1.00 19.82 ? 356 ASN A OD1 1 ATOM 2740 N ND2 . ASN A 1 356 ? -9.884 12.443 31.187 1.00 19.41 ? 356 ASN A ND2 1 ATOM 2741 N N . THR A 1 357 ? -7.035 9.961 28.052 1.00 17.28 ? 357 THR A N 1 ATOM 2742 C CA . THR A 1 357 ? -7.568 9.682 26.727 1.00 18.45 ? 357 THR A CA 1 ATOM 2743 C C . THR A 1 357 ? -9.068 9.470 26.727 1.00 19.20 ? 357 THR A C 1 ATOM 2744 O O . THR A 1 357 ? -9.665 9.334 25.659 1.00 19.50 ? 357 THR A O 1 ATOM 2745 C CB . THR A 1 357 ? -6.869 8.469 26.095 1.00 18.11 ? 357 THR A CB 1 ATOM 2746 O OG1 . THR A 1 357 ? -6.818 7.399 27.054 1.00 17.62 ? 357 THR A OG1 1 ATOM 2747 C CG2 . THR A 1 357 ? -5.398 8.819 25.792 1.00 18.26 ? 357 THR A CG2 1 ATOM 2748 N N . LEU A 1 358 ? -9.679 9.436 27.913 1.00 20.18 ? 358 LEU A N 1 ATOM 2749 C CA . LEU A 1 358 ? -11.118 9.197 28.006 1.00 21.69 ? 358 LEU A CA 1 ATOM 2750 C C . LEU A 1 358 ? -11.830 10.501 27.715 1.00 23.02 ? 358 LEU A C 1 ATOM 2751 O O . LEU A 1 358 ? -11.240 11.571 27.844 1.00 22.40 ? 358 LEU A O 1 ATOM 2752 C CB . LEU A 1 358 ? -11.524 8.711 29.404 1.00 21.95 ? 358 LEU A CB 1 ATOM 2753 C CG . LEU A 1 358 ? -10.989 7.369 29.907 1.00 21.84 ? 358 LEU A CG 1 ATOM 2754 C CD1 . LEU A 1 358 ? -11.463 7.125 31.338 1.00 20.92 ? 358 LEU A CD1 1 ATOM 2755 C CD2 . LEU A 1 358 ? -11.418 6.233 29.027 1.00 22.60 ? 358 LEU A CD2 1 ATOM 2756 N N . ASP A 1 359 ? -13.100 10.420 27.321 1.00 23.93 ? 359 ASP A N 1 ATOM 2757 C CA . ASP A 1 359 ? -13.816 11.638 26.989 1.00 26.01 ? 359 ASP A CA 1 ATOM 2758 C C . ASP A 1 359 ? -14.613 12.135 28.197 1.00 26.34 ? 359 ASP A C 1 ATOM 2759 O O . ASP A 1 359 ? -15.588 12.860 28.073 1.00 26.37 ? 359 ASP A O 1 ATOM 2760 C CB . ASP A 1 359 ? -14.677 11.466 25.734 1.00 26.78 ? 359 ASP A CB 1 ATOM 2761 C CG . ASP A 1 359 ? -15.014 12.802 25.075 1.00 30.48 ? 359 ASP A CG 1 ATOM 2762 O OD1 . ASP A 1 359 ? -14.120 13.691 25.052 1.00 31.64 ? 359 ASP A OD1 1 ATOM 2763 O OD2 . ASP A 1 359 ? -16.142 13.050 24.556 1.00 33.47 ? 359 ASP A OD2 1 ATOM 2764 N N . ILE A 1 360 ? -14.168 11.728 29.375 1.00 26.61 ? 360 ILE A N 1 ATOM 2765 C CA . ILE A 1 360 ? -14.765 12.186 30.605 1.00 27.56 ? 360 ILE A CA 1 ATOM 2766 C C . ILE A 1 360 ? -13.612 12.417 31.574 1.00 27.85 ? 360 ILE A C 1 ATOM 2767 O O . ILE A 1 360 ? -12.537 11.832 31.424 1.00 27.67 ? 360 ILE A O 1 ATOM 2768 C CB . ILE A 1 360 ? -15.747 11.132 31.147 1.00 27.68 ? 360 ILE A CB 1 ATOM 2769 C CG1 . ILE A 1 360 ? -15.261 9.723 30.822 1.00 28.36 ? 360 ILE A CG1 1 ATOM 2770 C CG2 . ILE A 1 360 ? -17.127 11.283 30.503 1.00 29.41 ? 360 ILE A CG2 1 ATOM 2771 C CD1 . ILE A 1 360 ? -14.736 8.956 32.007 1.00 31.78 ? 360 ILE A CD1 1 ATOM 2772 N N . THR A 1 361 ? -13.846 13.271 32.561 1.00 27.71 ? 361 THR A N 1 ATOM 2773 C CA . THR A 1 361 ? -12.897 13.492 33.623 1.00 27.53 ? 361 THR A CA 1 ATOM 2774 C C . THR A 1 361 ? -12.482 12.159 34.246 1.00 27.23 ? 361 THR A C 1 ATOM 2775 O O . THR A 1 361 ? -13.310 11.286 34.547 1.00 27.71 ? 361 THR A O 1 ATOM 2776 C CB . THR A 1 361 ? -13.501 14.445 34.663 1.00 28.01 ? 361 THR A CB 1 ATOM 2777 O OG1 . THR A 1 361 ? -13.749 15.717 34.032 1.00 28.45 ? 361 THR A OG1 1 ATOM 2778 C CG2 . THR A 1 361 ? -12.487 14.755 35.748 1.00 27.26 ? 361 THR A CG2 1 ATOM 2779 N N . ALA A 1 362 ? -11.183 12.004 34.430 1.00 26.01 ? 362 ALA A N 1 ATOM 2780 C CA . ALA A 1 362 ? -10.674 10.827 35.064 1.00 25.28 ? 362 ALA A CA 1 ATOM 2781 C C . ALA A 1 362 ? -9.611 11.278 36.034 1.00 24.90 ? 362 ALA A C 1 ATOM 2782 O O . ALA A 1 362 ? -8.970 12.325 35.850 1.00 24.78 ? 362 ALA A O 1 ATOM 2783 C CB . ALA A 1 362 ? -10.117 9.861 34.048 1.00 25.68 ? 362 ALA A CB 1 ATOM 2784 N N . THR A 1 363 ? -9.432 10.480 37.071 1.00 23.82 ? 363 THR A N 1 ATOM 2785 C CA . THR A 1 363 ? -8.436 10.759 38.074 1.00 23.67 ? 363 THR A CA 1 ATOM 2786 C C . THR A 1 363 ? -7.199 9.967 37.690 1.00 22.90 ? 363 THR A C 1 ATOM 2787 O O . THR A 1 363 ? -7.264 8.760 37.496 1.00 22.82 ? 363 THR A O 1 ATOM 2788 C CB . THR A 1 363 ? -8.983 10.294 39.417 1.00 24.20 ? 363 THR A CB 1 ATOM 2789 O OG1 . THR A 1 363 ? -10.092 11.125 39.763 1.00 25.91 ? 363 THR A OG1 1 ATOM 2790 C CG2 . THR A 1 363 ? -7.989 10.536 40.516 1.00 24.51 ? 363 THR A CG2 1 ATOM 2791 N N . LYS A 1 364 ? -6.067 10.636 37.576 1.00 22.04 ? 364 LYS A N 1 ATOM 2792 C CA . LYS A 1 364 ? -4.846 9.967 37.172 1.00 21.81 ? 364 LYS A CA 1 ATOM 2793 C C . LYS A 1 364 ? -3.859 10.190 38.285 1.00 21.75 ? 364 LYS A C 1 ATOM 2794 O O . LYS A 1 364 ? -3.772 11.285 38.823 1.00 22.09 ? 364 LYS A O 1 ATOM 2795 C CB . LYS A 1 364 ? -4.329 10.557 35.857 1.00 20.99 ? 364 LYS A CB 1 ATOM 2796 C CG . LYS A 1 364 ? -5.404 10.600 34.754 1.00 21.37 ? 364 LYS A CG 1 ATOM 2797 C CD . LYS A 1 364 ? -4.811 10.541 33.336 1.00 19.83 ? 364 LYS A CD 1 ATOM 2798 C CE . LYS A 1 364 ? -4.214 9.144 33.006 1.00 21.82 ? 364 LYS A CE 1 ATOM 2799 N NZ . LYS A 1 364 ? -5.274 8.072 32.803 1.00 19.85 ? 364 LYS A NZ 1 ATOM 2800 N N . GLU A 1 365 ? -3.111 9.164 38.640 1.00 21.78 ? 365 GLU A N 1 ATOM 2801 C CA . GLU A 1 365 ? -2.169 9.319 39.728 1.00 21.87 ? 365 GLU A CA 1 ATOM 2802 C C . GLU A 1 365 ? -0.753 8.961 39.327 1.00 21.78 ? 365 GLU A C 1 ATOM 2803 O O . GLU A 1 365 ? -0.475 7.871 38.831 1.00 21.72 ? 365 GLU A O 1 ATOM 2804 C CB . GLU A 1 365 ? -2.602 8.514 40.949 1.00 21.79 ? 365 GLU A CB 1 ATOM 2805 C CG . GLU A 1 365 ? -1.553 8.490 42.045 1.00 23.78 ? 365 GLU A CG 1 ATOM 2806 C CD . GLU A 1 365 ? -2.082 7.970 43.364 1.00 28.15 ? 365 GLU A CD 1 ATOM 2807 O OE1 . GLU A 1 365 ? -3.135 7.314 43.355 1.00 29.44 ? 365 GLU A OE1 1 ATOM 2808 O OE2 . GLU A 1 365 ? -1.441 8.223 44.409 1.00 30.32 ? 365 GLU A OE2 1 ATOM 2809 N N . ALA A 1 366 ? 0.139 9.909 39.551 1.00 22.04 ? 366 ALA A N 1 ATOM 2810 C CA . ALA A 1 366 ? 1.544 9.700 39.327 1.00 22.88 ? 366 ALA A CA 1 ATOM 2811 C C . ALA A 1 366 ? 2.082 9.070 40.610 1.00 23.31 ? 366 ALA A C 1 ATOM 2812 O O . ALA A 1 366 ? 2.008 9.681 41.668 1.00 23.58 ? 366 ALA A O 1 ATOM 2813 C CB . ALA A 1 366 ? 2.233 11.050 39.037 1.00 22.20 ? 366 ALA A CB 1 ATOM 2814 N N . LYS A 1 367 ? 2.618 7.855 40.517 1.00 23.66 ? 367 LYS A N 1 ATOM 2815 C CA . LYS A 1 367 ? 3.155 7.160 41.687 1.00 24.62 ? 367 LYS A CA 1 ATOM 2816 C C . LYS A 1 367 ? 4.639 7.019 41.475 1.00 24.72 ? 367 LYS A C 1 ATOM 2817 O O . LYS A 1 367 ? 5.061 6.387 40.507 1.00 24.45 ? 367 LYS A O 1 ATOM 2818 C CB . LYS A 1 367 ? 2.537 5.773 41.846 1.00 25.14 ? 367 LYS A CB 1 ATOM 2819 C CG . LYS A 1 367 ? 1.015 5.769 42.014 1.00 26.70 ? 367 LYS A CG 1 ATOM 2820 C CD . LYS A 1 367 ? 0.525 4.337 42.181 1.00 29.71 ? 367 LYS A CD 1 ATOM 2821 C CE . LYS A 1 367 ? -0.984 4.264 42.131 1.00 33.65 ? 367 LYS A CE 1 ATOM 2822 N NZ . LYS A 1 367 ? -1.556 3.566 43.336 1.00 35.71 ? 367 LYS A NZ 1 ATOM 2823 N N . TRP A 1 368 ? 5.426 7.599 42.370 1.00 24.51 ? 368 TRP A N 1 ATOM 2824 C CA . TRP A 1 368 ? 6.864 7.680 42.158 1.00 25.64 ? 368 TRP A CA 1 ATOM 2825 C C . TRP A 1 368 ? 7.562 6.329 41.970 1.00 26.14 ? 368 TRP A C 1 ATOM 2826 O O . TRP A 1 368 ? 8.494 6.224 41.171 1.00 25.75 ? 368 TRP A O 1 ATOM 2827 C CB . TRP A 1 368 ? 7.574 8.469 43.276 1.00 25.65 ? 368 TRP A CB 1 ATOM 2828 C CG . TRP A 1 368 ? 6.933 9.772 43.723 1.00 25.32 ? 368 TRP A CG 1 ATOM 2829 C CD1 . TRP A 1 368 ? 6.867 10.243 45.011 1.00 26.19 ? 368 TRP A CD1 1 ATOM 2830 C CD2 . TRP A 1 368 ? 6.286 10.757 42.910 1.00 25.45 ? 368 TRP A CD2 1 ATOM 2831 N NE1 . TRP A 1 368 ? 6.218 11.454 45.046 1.00 26.60 ? 368 TRP A NE1 1 ATOM 2832 C CE2 . TRP A 1 368 ? 5.850 11.794 43.770 1.00 27.02 ? 368 TRP A CE2 1 ATOM 2833 C CE3 . TRP A 1 368 ? 6.024 10.873 41.545 1.00 22.41 ? 368 TRP A CE3 1 ATOM 2834 C CZ2 . TRP A 1 368 ? 5.175 12.917 43.305 1.00 26.49 ? 368 TRP A CZ2 1 ATOM 2835 C CZ3 . TRP A 1 368 ? 5.360 11.981 41.090 1.00 25.40 ? 368 TRP A CZ3 1 ATOM 2836 C CH2 . TRP A 1 368 ? 4.940 12.992 41.963 1.00 26.33 ? 368 TRP A CH2 1 ATOM 2837 N N . ASN A 1 369 ? 7.124 5.307 42.694 1.00 27.01 ? 369 ASN A N 1 ATOM 2838 C CA . ASN A 1 369 ? 7.766 3.995 42.573 1.00 28.77 ? 369 ASN A CA 1 ATOM 2839 C C . ASN A 1 369 ? 7.587 3.360 41.187 1.00 28.69 ? 369 ASN A C 1 ATOM 2840 O O . ASN A 1 369 ? 8.391 2.518 40.790 1.00 29.12 ? 369 ASN A O 1 ATOM 2841 C CB . ASN A 1 369 ? 7.340 3.031 43.700 1.00 29.63 ? 369 ASN A CB 1 ATOM 2842 C CG . ASN A 1 369 ? 5.819 2.853 43.801 1.00 33.08 ? 369 ASN A CG 1 ATOM 2843 O OD1 . ASN A 1 369 ? 5.331 2.063 44.623 1.00 39.39 ? 369 ASN A OD1 1 ATOM 2844 N ND2 . ASN A 1 369 ? 5.072 3.574 42.982 1.00 33.44 ? 369 ASN A ND2 1 ATOM 2845 N N . GLU A 1 370 ? 6.540 3.768 40.464 1.00 28.11 ? 370 GLU A N 1 ATOM 2846 C CA . GLU A 1 370 ? 6.307 3.308 39.086 1.00 28.25 ? 370 GLU A CA 1 ATOM 2847 C C . GLU A 1 370 ? 7.194 4.019 38.060 1.00 27.76 ? 370 GLU A C 1 ATOM 2848 O O . GLU A 1 370 ? 7.413 3.518 36.957 1.00 27.75 ? 370 GLU A O 1 ATOM 2849 C CB . GLU A 1 370 ? 4.866 3.577 38.667 1.00 28.38 ? 370 GLU A CB 1 ATOM 2850 C CG . GLU A 1 370 ? 3.814 2.945 39.547 1.00 29.68 ? 370 GLU A CG 1 ATOM 2851 C CD . GLU A 1 370 ? 2.434 2.991 38.914 1.00 31.07 ? 370 GLU A CD 1 ATOM 2852 O OE1 . GLU A 1 370 ? 2.156 3.961 38.183 1.00 29.12 ? 370 GLU A OE1 1 ATOM 2853 O OE2 . GLU A 1 370 ? 1.626 2.055 39.150 1.00 32.92 ? 370 GLU A OE2 1 ATOM 2854 N N . ILE A 1 371 ? 7.702 5.188 38.422 1.00 27.16 ? 371 ILE A N 1 ATOM 2855 C CA . ILE A 1 371 ? 8.418 6.027 37.459 1.00 27.25 ? 371 ILE A CA 1 ATOM 2856 C C . ILE A 1 371 ? 9.910 5.742 37.471 1.00 27.37 ? 371 ILE A C 1 ATOM 2857 O O . ILE A 1 371 ? 10.567 5.931 38.486 1.00 27.73 ? 371 ILE A O 1 ATOM 2858 C CB . ILE A 1 371 ? 8.119 7.493 37.741 1.00 26.48 ? 371 ILE A CB 1 ATOM 2859 C CG1 . ILE A 1 371 ? 6.619 7.748 37.548 1.00 26.18 ? 371 ILE A CG1 1 ATOM 2860 C CG2 . ILE A 1 371 ? 8.970 8.401 36.850 1.00 27.12 ? 371 ILE A CG2 1 ATOM 2861 C CD1 . ILE A 1 371 ? 6.106 9.029 38.176 1.00 25.57 ? 371 ILE A CD1 1 ATOM 2862 N N . PRO A 1 372 ? 10.442 5.281 36.343 1.00 28.01 ? 372 PRO A N 1 ATOM 2863 C CA . PRO A 1 372 ? 11.881 4.999 36.232 1.00 28.31 ? 372 PRO A CA 1 ATOM 2864 C C . PRO A 1 372 ? 12.698 6.212 36.643 1.00 29.01 ? 372 PRO A C 1 ATOM 2865 O O . PRO A 1 372 ? 12.500 7.301 36.112 1.00 29.24 ? 372 PRO A O 1 ATOM 2866 C CB . PRO A 1 372 ? 12.059 4.705 34.745 1.00 28.46 ? 372 PRO A CB 1 ATOM 2867 C CG . PRO A 1 372 ? 10.750 4.150 34.356 1.00 28.50 ? 372 PRO A CG 1 ATOM 2868 C CD . PRO A 1 372 ? 9.718 4.984 35.091 1.00 27.81 ? 372 PRO A CD 1 ATOM 2869 N N . GLY A 1 373 ? 13.612 6.031 37.587 1.00 29.45 ? 373 GLY A N 1 ATOM 2870 C CA . GLY A 1 373 ? 14.464 7.126 38.006 1.00 30.01 ? 373 GLY A CA 1 ATOM 2871 C C . GLY A 1 373 ? 13.971 7.818 39.261 1.00 30.15 ? 373 GLY A C 1 ATOM 2872 O O . GLY A 1 373 ? 14.694 8.629 39.850 1.00 30.65 ? 373 GLY A O 1 ATOM 2873 N N . LEU A 1 374 ? 12.745 7.502 39.668 1.00 29.42 ? 374 LEU A N 1 ATOM 2874 C CA . LEU A 1 374 ? 12.210 7.984 40.935 1.00 29.49 ? 374 LEU A CA 1 ATOM 2875 C C . LEU A 1 374 ? 12.079 6.791 41.888 1.00 29.73 ? 374 LEU A C 1 ATOM 2876 O O . LEU A 1 374 ? 12.190 5.646 41.466 1.00 29.70 ? 374 LEU A O 1 ATOM 2877 C CB . LEU A 1 374 ? 10.847 8.657 40.742 1.00 28.63 ? 374 LEU A CB 1 ATOM 2878 C CG . LEU A 1 374 ? 10.861 9.944 39.914 1.00 28.30 ? 374 LEU A CG 1 ATOM 2879 C CD1 . LEU A 1 374 ? 9.502 10.625 39.897 1.00 23.04 ? 374 LEU A CD1 1 ATOM 2880 C CD2 . LEU A 1 374 ? 11.929 10.895 40.435 1.00 27.37 ? 374 LEU A CD2 1 ATOM 2881 N N . SER A 1 375 ? 11.844 7.058 43.166 1.00 30.08 ? 375 SER A N 1 ATOM 2882 C CA . SER A 1 375 ? 11.596 5.986 44.131 1.00 30.67 ? 375 SER A CA 1 ATOM 2883 C C . SER A 1 375 ? 10.511 6.461 45.071 1.00 30.64 ? 375 SER A C 1 ATOM 2884 O O . SER A 1 375 ? 10.197 7.642 45.102 1.00 30.88 ? 375 SER A O 1 ATOM 2885 C CB . SER A 1 375 ? 12.850 5.688 44.962 1.00 30.70 ? 375 SER A CB 1 ATOM 2886 O OG . SER A 1 375 ? 14.029 6.121 44.307 1.00 32.35 ? 375 SER A OG 1 ATOM 2887 N N . ALA A 1 376 ? 9.935 5.551 45.840 1.00 30.78 ? 376 ALA A N 1 ATOM 2888 C CA . ALA A 1 376 ? 9.010 5.980 46.871 1.00 31.04 ? 376 ALA A CA 1 ATOM 2889 C C . ALA A 1 376 ? 9.674 7.067 47.711 1.00 30.99 ? 376 ALA A C 1 ATOM 2890 O O . ALA A 1 376 ? 10.895 7.056 47.947 1.00 30.71 ? 376 ALA A O 1 ATOM 2891 C CB . ALA A 1 376 ? 8.573 4.814 47.736 1.00 31.32 ? 376 ALA A CB 1 ATOM 2892 N N . GLY A 1 377 ? 8.861 8.009 48.159 1.00 30.65 ? 377 GLY A N 1 ATOM 2893 C CA . GLY A 1 377 ? 9.345 9.089 48.994 1.00 30.80 ? 377 GLY A CA 1 ATOM 2894 C C . GLY A 1 377 ? 8.517 10.325 48.756 1.00 29.94 ? 377 GLY A C 1 ATOM 2895 O O . GLY A 1 377 ? 7.385 10.241 48.321 1.00 31.00 ? 377 GLY A O 1 ATOM 2896 N N . HIS A 1 378 ? 9.088 11.478 49.048 1.00 29.59 ? 378 HIS A N 1 ATOM 2897 C CA . HIS A 1 378 ? 8.389 12.734 48.859 1.00 28.92 ? 378 HIS A CA 1 ATOM 2898 C C . HIS A 1 378 ? 9.278 13.580 47.999 1.00 28.14 ? 378 HIS A C 1 ATOM 2899 O O . HIS A 1 378 ? 10.461 13.729 48.269 1.00 27.73 ? 378 HIS A O 1 ATOM 2900 C CB . HIS A 1 378 ? 8.144 13.459 50.184 1.00 29.44 ? 378 HIS A CB 1 ATOM 2901 C CG . HIS A 1 378 ? 7.025 12.888 50.994 1.00 30.33 ? 378 HIS A CG 1 ATOM 2902 N ND1 . HIS A 1 378 ? 5.763 13.443 51.014 1.00 32.82 ? 378 HIS A ND1 1 ATOM 2903 C CD2 . HIS A 1 378 ? 6.976 11.811 51.814 1.00 32.51 ? 378 HIS A CD2 1 ATOM 2904 C CE1 . HIS A 1 378 ? 4.982 12.734 51.811 1.00 33.39 ? 378 HIS A CE1 1 ATOM 2905 N NE2 . HIS A 1 378 ? 5.693 11.738 52.310 1.00 32.93 ? 378 HIS A NE2 1 ATOM 2906 N N . TYR A 1 379 ? 8.695 14.135 46.955 1.00 26.85 ? 379 TYR A N 1 ATOM 2907 C CA . TYR A 1 379 ? 9.403 15.034 46.093 1.00 26.24 ? 379 TYR A CA 1 ATOM 2908 C C . TYR A 1 379 ? 8.667 16.360 46.033 1.00 25.62 ? 379 TYR A C 1 ATOM 2909 O O . TYR A 1 379 ? 7.452 16.397 46.192 1.00 25.19 ? 379 TYR A O 1 ATOM 2910 C CB . TYR A 1 379 ? 9.431 14.451 44.682 1.00 26.44 ? 379 TYR A CB 1 ATOM 2911 C CG . TYR A 1 379 ? 10.290 13.222 44.528 1.00 25.97 ? 379 TYR A CG 1 ATOM 2912 C CD1 . TYR A 1 379 ? 9.764 11.949 44.696 1.00 26.55 ? 379 TYR A CD1 1 ATOM 2913 C CD2 . TYR A 1 379 ? 11.628 13.342 44.209 1.00 26.89 ? 379 TYR A CD2 1 ATOM 2914 C CE1 . TYR A 1 379 ? 10.572 10.817 44.549 1.00 28.75 ? 379 TYR A CE1 1 ATOM 2915 C CE2 . TYR A 1 379 ? 12.436 12.229 44.061 1.00 27.22 ? 379 TYR A CE2 1 ATOM 2916 C CZ . TYR A 1 379 ? 11.910 10.976 44.230 1.00 27.84 ? 379 TYR A CZ 1 ATOM 2917 O OH . TYR A 1 379 ? 12.730 9.879 44.077 1.00 29.87 ? 379 TYR A OH 1 ATOM 2918 N N . GLU A 1 380 ? 9.416 17.437 45.802 1.00 25.84 ? 380 GLU A N 1 ATOM 2919 C CA . GLU A 1 380 ? 8.821 18.736 45.518 1.00 25.70 ? 380 GLU A CA 1 ATOM 2920 C C . GLU A 1 380 ? 8.259 18.634 44.104 1.00 24.44 ? 380 GLU A C 1 ATOM 2921 O O . GLU A 1 380 ? 8.931 18.163 43.195 1.00 24.21 ? 380 GLU A O 1 ATOM 2922 C CB . GLU A 1 380 ? 9.862 19.853 45.624 1.00 26.24 ? 380 GLU A CB 1 ATOM 2923 C CG . GLU A 1 380 ? 10.030 20.360 47.048 1.00 30.29 ? 380 GLU A CG 1 ATOM 2924 C CD . GLU A 1 380 ? 11.274 21.200 47.215 1.00 35.23 ? 380 GLU A CD 1 ATOM 2925 O OE1 . GLU A 1 380 ? 11.526 21.654 48.353 1.00 37.80 ? 380 GLU A OE1 1 ATOM 2926 O OE2 . GLU A 1 380 ? 11.992 21.399 46.209 1.00 37.48 ? 380 GLU A OE2 1 ATOM 2927 N N . VAL A 1 381 ? 7.024 19.077 43.936 1.00 22.89 ? 381 VAL A N 1 ATOM 2928 C CA . VAL A 1 381 ? 6.322 18.978 42.669 1.00 22.33 ? 381 VAL A CA 1 ATOM 2929 C C . VAL A 1 381 ? 5.769 20.324 42.269 1.00 21.80 ? 381 VAL A C 1 ATOM 2930 O O . VAL A 1 381 ? 5.258 21.096 43.090 1.00 20.71 ? 381 VAL A O 1 ATOM 2931 C CB . VAL A 1 381 ? 5.150 17.975 42.752 1.00 21.90 ? 381 VAL A CB 1 ATOM 2932 C CG1 . VAL A 1 381 ? 4.377 17.930 41.447 1.00 21.74 ? 381 VAL A CG1 1 ATOM 2933 C CG2 . VAL A 1 381 ? 5.672 16.582 43.157 1.00 23.37 ? 381 VAL A CG2 1 ATOM 2934 N N . ARG A 1 382 ? 5.878 20.594 40.983 1.00 21.91 ? 382 ARG A N 1 ATOM 2935 C CA . ARG A 1 382 ? 5.425 21.845 40.421 1.00 21.96 ? 382 ARG A CA 1 ATOM 2936 C C . ARG A 1 382 ? 4.505 21.495 39.288 1.00 21.59 ? 382 ARG A C 1 ATOM 2937 O O . ARG A 1 382 ? 4.828 20.637 38.458 1.00 20.68 ? 382 ARG A O 1 ATOM 2938 C CB . ARG A 1 382 ? 6.630 22.676 39.953 1.00 22.37 ? 382 ARG A CB 1 ATOM 2939 C CG . ARG A 1 382 ? 6.282 24.016 39.330 1.00 25.65 ? 382 ARG A CG 1 ATOM 2940 C CD . ARG A 1 382 ? 7.470 24.954 39.216 1.00 29.52 ? 382 ARG A CD 1 ATOM 2941 N NE . ARG A 1 382 ? 8.091 25.165 40.514 1.00 32.17 ? 382 ARG A NE 1 ATOM 2942 C CZ . ARG A 1 382 ? 7.734 26.101 41.392 1.00 34.60 ? 382 ARG A CZ 1 ATOM 2943 N NH1 . ARG A 1 382 ? 6.745 26.940 41.125 1.00 34.68 ? 382 ARG A NH1 1 ATOM 2944 N NH2 . ARG A 1 382 ? 8.377 26.197 42.549 1.00 36.85 ? 382 ARG A NH2 1 ATOM 2945 N N . ASP A 1 383 ? 3.351 22.160 39.272 1.00 21.16 ? 383 ASP A N 1 ATOM 2946 C CA . ASP A 1 383 ? 2.412 22.088 38.175 1.00 21.96 ? 383 ASP A CA 1 ATOM 2947 C C . ASP A 1 383 ? 3.024 22.833 36.987 1.00 21.32 ? 383 ASP A C 1 ATOM 2948 O O . ASP A 1 383 ? 3.360 24.015 37.083 1.00 21.25 ? 383 ASP A O 1 ATOM 2949 C CB . ASP A 1 383 ? 1.093 22.737 38.587 1.00 22.61 ? 383 ASP A CB 1 ATOM 2950 C CG . ASP A 1 383 ? -0.031 22.419 37.637 1.00 24.08 ? 383 ASP A CG 1 ATOM 2951 O OD1 . ASP A 1 383 ? 0.175 22.538 36.413 1.00 25.96 ? 383 ASP A OD1 1 ATOM 2952 O OD2 . ASP A 1 383 ? -1.157 22.042 38.022 1.00 28.41 ? 383 ASP A OD2 1 ATOM 2953 N N . VAL A 1 384 ? 3.172 22.144 35.863 1.00 21.14 ? 384 VAL A N 1 ATOM 2954 C CA . VAL A 1 384 ? 3.803 22.769 34.703 1.00 20.66 ? 384 VAL A CA 1 ATOM 2955 C C . VAL A 1 384 ? 2.870 23.800 34.055 1.00 21.01 ? 384 VAL A C 1 ATOM 2956 O O . VAL A 1 384 ? 3.315 24.812 33.539 1.00 21.39 ? 384 VAL A O 1 ATOM 2957 C CB . VAL A 1 384 ? 4.372 21.729 33.709 1.00 21.19 ? 384 VAL A CB 1 ATOM 2958 C CG1 . VAL A 1 384 ? 4.675 22.361 32.354 1.00 19.54 ? 384 VAL A CG1 1 ATOM 2959 C CG2 . VAL A 1 384 ? 5.650 21.123 34.277 1.00 20.28 ? 384 VAL A CG2 1 ATOM 2960 N N . TRP A 1 385 ? 1.574 23.544 34.088 1.00 21.65 ? 385 TRP A N 1 ATOM 2961 C CA . TRP A 1 385 ? 0.626 24.450 33.443 1.00 22.67 ? 385 TRP A CA 1 ATOM 2962 C C . TRP A 1 385 ? 0.483 25.775 34.184 1.00 23.17 ? 385 TRP A C 1 ATOM 2963 O O . TRP A 1 385 ? 0.403 26.833 33.558 1.00 23.70 ? 385 TRP A O 1 ATOM 2964 C CB . TRP A 1 385 ? -0.737 23.791 33.344 1.00 21.98 ? 385 TRP A CB 1 ATOM 2965 C CG . TRP A 1 385 ? -0.749 22.600 32.457 1.00 22.05 ? 385 TRP A CG 1 ATOM 2966 C CD1 . TRP A 1 385 ? -1.243 21.370 32.752 1.00 21.58 ? 385 TRP A CD1 1 ATOM 2967 C CD2 . TRP A 1 385 ? -0.242 22.517 31.115 1.00 20.88 ? 385 TRP A CD2 1 ATOM 2968 N NE1 . TRP A 1 385 ? -1.077 20.520 31.682 1.00 21.92 ? 385 TRP A NE1 1 ATOM 2969 C CE2 . TRP A 1 385 ? -0.465 21.201 30.663 1.00 20.88 ? 385 TRP A CE2 1 ATOM 2970 C CE3 . TRP A 1 385 ? 0.378 23.420 30.251 1.00 21.92 ? 385 TRP A CE3 1 ATOM 2971 C CZ2 . TRP A 1 385 ? -0.094 20.768 29.388 1.00 20.13 ? 385 TRP A CZ2 1 ATOM 2972 C CZ3 . TRP A 1 385 ? 0.752 22.982 28.972 1.00 21.68 ? 385 TRP A CZ3 1 ATOM 2973 C CH2 . TRP A 1 385 ? 0.512 21.671 28.562 1.00 19.78 ? 385 TRP A CH2 1 ATOM 2974 N N . SER A 1 386 ? 0.450 25.717 35.513 1.00 24.02 ? 386 SER A N 1 ATOM 2975 C CA . SER A 1 386 ? 0.240 26.928 36.319 1.00 24.21 ? 386 SER A CA 1 ATOM 2976 C C . SER A 1 386 ? 1.534 27.491 36.891 1.00 25.01 ? 386 SER A C 1 ATOM 2977 O O . SER A 1 386 ? 1.575 28.635 37.391 1.00 24.94 ? 386 SER A O 1 ATOM 2978 C CB . SER A 1 386 ? -0.736 26.637 37.451 1.00 23.82 ? 386 SER A CB 1 ATOM 2979 O OG . SER A 1 386 ? -0.246 25.581 38.250 1.00 25.20 ? 386 SER A OG 1 ATOM 2980 N N . ASP A 1 387 ? 2.582 26.679 36.806 1.00 25.06 ? 387 ASP A N 1 ATOM 2981 C CA . ASP A 1 387 ? 3.851 26.978 37.450 1.00 26.25 ? 387 ASP A CA 1 ATOM 2982 C C . ASP A 1 387 ? 3.729 26.975 38.968 1.00 25.95 ? 387 ASP A C 1 ATOM 2983 O O . ASP A 1 387 ? 4.599 27.456 39.664 1.00 26.62 ? 387 ASP A O 1 ATOM 2984 C CB . ASP A 1 387 ? 4.434 28.297 36.980 1.00 27.06 ? 387 ASP A CB 1 ATOM 2985 C CG . ASP A 1 387 ? 5.919 28.371 37.211 1.00 28.69 ? 387 ASP A CG 1 ATOM 2986 O OD1 . ASP A 1 387 ? 6.446 29.496 37.333 1.00 31.45 ? 387 ASP A OD1 1 ATOM 2987 O OD2 . ASP A 1 387 ? 6.637 27.349 37.286 1.00 32.32 ? 387 ASP A OD2 1 ATOM 2988 N N . LYS A 1 388 ? 2.645 26.425 39.477 1.00 25.41 ? 388 LYS A N 1 ATOM 2989 C CA . LYS A 1 388 ? 2.448 26.380 40.918 1.00 25.41 ? 388 LYS A CA 1 ATOM 2990 C C . LYS A 1 388 ? 3.229 25.295 41.637 1.00 24.73 ? 388 LYS A C 1 ATOM 2991 O O . LYS A 1 388 ? 3.258 24.127 41.225 1.00 23.94 ? 388 LYS A O 1 ATOM 2992 C CB . LYS A 1 388 ? 0.976 26.235 41.249 1.00 25.63 ? 388 LYS A CB 1 ATOM 2993 C CG . LYS A 1 388 ? 0.221 27.521 41.035 1.00 27.61 ? 388 LYS A CG 1 ATOM 2994 C CD . LYS A 1 388 ? -1.279 27.286 41.133 1.00 29.01 ? 388 LYS A CD 1 ATOM 2995 C CE . LYS A 1 388 ? -1.811 27.658 42.494 1.00 28.01 ? 388 LYS A CE 1 ATOM 2996 N NZ . LYS A 1 388 ? -3.307 27.673 42.473 1.00 29.23 ? 388 LYS A NZ 1 ATOM 2997 N N . ASP A 1 389 ? 3.855 25.726 42.721 1.00 23.83 ? 389 ASP A N 1 ATOM 2998 C CA . ASP A 1 389 ? 4.433 24.850 43.721 1.00 23.52 ? 389 ASP A CA 1 ATOM 2999 C C . ASP A 1 389 ? 3.270 24.049 44.347 1.00 23.57 ? 389 ASP A C 1 ATOM 3000 O O . ASP A 1 389 ? 2.374 24.607 44.999 1.00 23.14 ? 389 ASP A O 1 ATOM 3001 C CB . ASP A 1 389 ? 5.131 25.735 44.764 1.00 23.43 ? 389 ASP A CB 1 ATOM 3002 C CG . ASP A 1 389 ? 5.889 24.948 45.793 1.00 24.32 ? 389 ASP A CG 1 ATOM 3003 O OD1 . ASP A 1 389 ? 5.922 23.708 45.679 1.00 22.97 ? 389 ASP A OD1 1 ATOM 3004 O OD2 . ASP A 1 389 ? 6.489 25.486 46.762 1.00 25.73 ? 389 ASP A OD2 1 ATOM 3005 N N . LEU A 1 390 ? 3.282 22.740 44.149 1.00 23.66 ? 390 LEU A N 1 ATOM 3006 C CA . LEU A 1 390 ? 2.261 21.877 44.717 1.00 24.62 ? 390 LEU A CA 1 ATOM 3007 C C . LEU A 1 390 ? 2.751 21.240 45.997 1.00 25.39 ? 390 LEU A C 1 ATOM 3008 O O . LEU A 1 390 ? 2.010 20.510 46.660 1.00 25.40 ? 390 LEU A O 1 ATOM 3009 C CB . LEU A 1 390 ? 1.875 20.782 43.743 1.00 24.91 ? 390 LEU A CB 1 ATOM 3010 C CG . LEU A 1 390 ? 1.400 21.314 42.397 1.00 24.38 ? 390 LEU A CG 1 ATOM 3011 C CD1 . LEU A 1 390 ? 1.226 20.141 41.460 1.00 26.28 ? 390 LEU A CD1 1 ATOM 3012 C CD2 . LEU A 1 390 ? 0.093 22.128 42.542 1.00 25.07 ? 390 LEU A CD2 1 ATOM 3013 N N . GLY A 1 391 ? 3.999 21.512 46.338 1.00 25.77 ? 391 GLY A N 1 ATOM 3014 C CA . GLY A 1 391 ? 4.537 21.053 47.604 1.00 27.30 ? 391 GLY A CA 1 ATOM 3015 C C . GLY A 1 391 ? 5.339 19.774 47.569 1.00 28.03 ? 391 GLY A C 1 ATOM 3016 O O . GLY A 1 391 ? 5.818 19.334 46.524 1.00 27.96 ? 391 GLY A O 1 ATOM 3017 N N . CYS A 1 392 ? 5.474 19.179 48.744 1.00 28.50 ? 392 CYS A N 1 ATOM 3018 C CA . CYS A 1 392 ? 6.261 17.986 48.935 1.00 29.19 ? 392 CYS A CA 1 ATOM 3019 C C . CYS A 1 392 ? 5.301 16.818 48.959 1.00 29.25 ? 392 CYS A C 1 ATOM 3020 O O . CYS A 1 392 ? 4.574 16.631 49.938 1.00 29.41 ? 392 CYS A O 1 ATOM 3021 C CB . CYS A 1 392 ? 6.963 18.115 50.279 1.00 30.04 ? 392 CYS A CB 1 ATOM 3022 S SG . CYS A 1 392 ? 8.081 16.775 50.580 1.00 33.87 ? 392 CYS A SG 1 ATOM 3023 N N . LEU A 1 393 ? 5.288 16.027 47.891 1.00 28.57 ? 393 LEU A N 1 ATOM 3024 C CA . LEU A 1 393 ? 4.218 15.045 47.689 1.00 28.10 ? 393 LEU A CA 1 ATOM 3025 C C . LEU A 1 393 ? 4.686 13.609 47.632 1.00 27.60 ? 393 LEU A C 1 ATOM 3026 O O . LEU A 1 393 ? 5.757 13.328 47.126 1.00 26.79 ? 393 LEU A O 1 ATOM 3027 C CB . LEU A 1 393 ? 3.456 15.363 46.387 1.00 28.13 ? 393 LEU A CB 1 ATOM 3028 C CG . LEU A 1 393 ? 2.747 16.719 46.355 1.00 28.67 ? 393 LEU A CG 1 ATOM 3029 C CD1 . LEU A 1 393 ? 2.090 16.982 45.006 1.00 29.03 ? 393 LEU A CD1 1 ATOM 3030 C CD2 . LEU A 1 393 ? 1.723 16.775 47.482 1.00 30.84 ? 393 LEU A CD2 1 ATOM 3031 N N . SER A 1 394 ? 3.865 12.702 48.157 1.00 27.63 ? 394 SER A N 1 ATOM 3032 C CA . SER A 1 394 ? 4.190 11.282 48.146 1.00 28.50 ? 394 SER A CA 1 ATOM 3033 C C . SER A 1 394 ? 3.654 10.634 46.866 1.00 28.60 ? 394 SER A C 1 ATOM 3034 O O . SER A 1 394 ? 3.965 9.490 46.538 1.00 28.48 ? 394 SER A O 1 ATOM 3035 C CB . SER A 1 394 ? 3.605 10.594 49.384 1.00 28.69 ? 394 SER A CB 1 ATOM 3036 O OG . SER A 1 394 ? 2.190 10.649 49.364 1.00 29.82 ? 394 SER A OG 1 ATOM 3037 N N . SER A 1 395 ? 2.840 11.388 46.145 1.00 28.90 ? 395 SER A N 1 ATOM 3038 C CA . SER A 1 395 ? 2.351 10.968 44.845 1.00 28.85 ? 395 SER A CA 1 ATOM 3039 C C . SER A 1 395 ? 1.571 12.160 44.379 1.00 28.29 ? 395 SER A C 1 ATOM 3040 O O . SER A 1 395 ? 1.407 13.122 45.136 1.00 28.16 ? 395 SER A O 1 ATOM 3041 C CB . SER A 1 395 ? 1.435 9.758 44.961 1.00 29.02 ? 395 SER A CB 1 ATOM 3042 O OG . SER A 1 395 ? 0.253 10.106 45.657 1.00 31.01 ? 395 SER A OG 1 ATOM 3043 N N . TYR A 1 396 ? 1.087 12.120 43.151 1.00 27.25 ? 396 TYR A N 1 ATOM 3044 C CA . TYR A 1 396 ? 0.308 13.236 42.667 1.00 27.27 ? 396 TYR A CA 1 ATOM 3045 C C . TYR A 1 396 ? -0.908 12.755 41.913 1.00 27.14 ? 396 TYR A C 1 ATOM 3046 O O . TYR A 1 396 ? -0.821 12.018 40.935 1.00 26.55 ? 396 TYR A O 1 ATOM 3047 C CB . TYR A 1 396 ? 1.151 14.195 41.835 1.00 27.15 ? 396 TYR A CB 1 ATOM 3048 C CG . TYR A 1 396 ? 0.352 15.181 41.033 1.00 27.27 ? 396 TYR A CG 1 ATOM 3049 C CD1 . TYR A 1 396 ? 0.135 14.964 39.690 1.00 29.07 ? 396 TYR A CD1 1 ATOM 3050 C CD2 . TYR A 1 396 ? -0.181 16.327 41.611 1.00 28.63 ? 396 TYR A CD2 1 ATOM 3051 C CE1 . TYR A 1 396 ? -0.586 15.843 38.934 1.00 28.98 ? 396 TYR A CE1 1 ATOM 3052 C CE2 . TYR A 1 396 ? -0.914 17.227 40.852 1.00 30.09 ? 396 TYR A CE2 1 ATOM 3053 C CZ . TYR A 1 396 ? -1.107 16.968 39.510 1.00 30.31 ? 396 TYR A CZ 1 ATOM 3054 O OH . TYR A 1 396 ? -1.823 17.821 38.712 1.00 33.59 ? 396 TYR A OH 1 ATOM 3055 N N . LYS A 1 397 ? -2.043 13.201 42.406 1.00 26.75 ? 397 LYS A N 1 ATOM 3056 C CA . LYS A 1 397 ? -3.326 12.787 41.903 1.00 28.26 ? 397 LYS A CA 1 ATOM 3057 C C . LYS A 1 397 ? -4.007 14.028 41.352 1.00 27.89 ? 397 LYS A C 1 ATOM 3058 O O . LYS A 1 397 ? -4.080 15.051 42.027 1.00 28.36 ? 397 LYS A O 1 ATOM 3059 C CB . LYS A 1 397 ? -4.122 12.200 43.078 1.00 28.70 ? 397 LYS A CB 1 ATOM 3060 C CG . LYS A 1 397 ? -5.095 11.078 42.755 1.00 32.05 ? 397 LYS A CG 1 ATOM 3061 C CD . LYS A 1 397 ? -5.405 10.281 44.048 1.00 35.55 ? 397 LYS A CD 1 ATOM 3062 C CE . LYS A 1 397 ? -6.765 9.585 44.010 1.00 39.07 ? 397 LYS A CE 1 ATOM 3063 N NZ . LYS A 1 397 ? -7.037 8.863 45.300 1.00 39.74 ? 397 LYS A NZ 1 ATOM 3064 N N . ALA A 1 398 ? -4.498 13.943 40.122 1.00 27.23 ? 398 ALA A N 1 ATOM 3065 C CA . ALA A 1 398 ? -5.343 15.001 39.591 1.00 26.49 ? 398 ALA A CA 1 ATOM 3066 C C . ALA A 1 398 ? -6.537 14.439 38.839 1.00 25.95 ? 398 ALA A C 1 ATOM 3067 O O . ALA A 1 398 ? -6.473 13.368 38.207 1.00 25.03 ? 398 ALA A O 1 ATOM 3068 C CB . ALA A 1 398 ? -4.545 15.989 38.698 1.00 27.22 ? 398 ALA A CB 1 ATOM 3069 N N . ALA A 1 399 ? -7.622 15.202 38.943 1.00 25.16 ? 399 ALA A N 1 ATOM 3070 C CA . ALA A 1 399 ? -8.798 15.109 38.098 1.00 24.17 ? 399 ALA A CA 1 ATOM 3071 C C . ALA A 1 399 ? -8.423 15.740 36.754 1.00 23.55 ? 399 ALA A C 1 ATOM 3072 O O . ALA A 1 399 ? -8.239 16.968 36.646 1.00 23.57 ? 399 ALA A O 1 ATOM 3073 C CB . ALA A 1 399 ? -9.930 15.927 38.718 1.00 24.63 ? 399 ALA A CB 1 ATOM 3074 N N . VAL A 1 400 ? -8.310 14.919 35.722 1.00 22.50 ? 400 VAL A N 1 ATOM 3075 C CA . VAL A 1 400 ? -7.846 15.436 34.438 1.00 21.05 ? 400 VAL A CA 1 ATOM 3076 C C . VAL A 1 400 ? -9.003 15.480 33.481 1.00 20.63 ? 400 VAL A C 1 ATOM 3077 O O . VAL A 1 400 ? -9.690 14.469 33.249 1.00 20.46 ? 400 VAL A O 1 ATOM 3078 C CB . VAL A 1 400 ? -6.669 14.603 33.881 1.00 21.06 ? 400 VAL A CB 1 ATOM 3079 C CG1 . VAL A 1 400 ? -6.033 15.313 32.671 1.00 20.64 ? 400 VAL A CG1 1 ATOM 3080 C CG2 . VAL A 1 400 ? -5.640 14.366 34.975 1.00 20.47 ? 400 VAL A CG2 1 ATOM 3081 N N . ALA A 1 401 ? -9.230 16.656 32.916 1.00 20.29 ? 401 ALA A N 1 ATOM 3082 C CA . ALA A 1 401 ? -10.322 16.805 31.988 1.00 20.51 ? 401 ALA A CA 1 ATOM 3083 C C . ALA A 1 401 ? -10.236 15.796 30.830 1.00 20.45 ? 401 ALA A C 1 ATOM 3084 O O . ALA A 1 401 ? -9.178 15.221 30.555 1.00 19.64 ? 401 ALA A O 1 ATOM 3085 C CB . ALA A 1 401 ? -10.370 18.236 31.455 1.00 21.31 ? 401 ALA A CB 1 ATOM 3086 N N . ALA A 1 402 ? -11.365 15.590 30.162 1.00 19.55 ? 402 ALA A N 1 ATOM 3087 C CA . ALA A 1 402 ? -11.404 14.772 28.964 1.00 19.33 ? 402 ALA A CA 1 ATOM 3088 C C . ALA A 1 402 ? -10.331 15.245 27.961 1.00 18.92 ? 402 ALA A C 1 ATOM 3089 O O . ALA A 1 402 ? -10.276 16.425 27.582 1.00 18.19 ? 402 ALA A O 1 ATOM 3090 C CB . ALA A 1 402 ? -12.781 14.838 28.337 1.00 20.10 ? 402 ALA A CB 1 ATOM 3091 N N . HIS A 1 403 ? -9.483 14.306 27.546 1.00 18.31 ? 403 HIS A N 1 ATOM 3092 C CA . HIS A 1 403 ? -8.433 14.555 26.544 1.00 18.26 ? 403 HIS A CA 1 ATOM 3093 C C . HIS A 1 403 ? -7.361 15.559 27.006 1.00 17.74 ? 403 HIS A C 1 ATOM 3094 O O . HIS A 1 403 ? -6.572 16.050 26.201 1.00 18.91 ? 403 HIS A O 1 ATOM 3095 C CB . HIS A 1 403 ? -9.000 15.067 25.219 1.00 17.29 ? 403 HIS A CB 1 ATOM 3096 C CG . HIS A 1 403 ? -9.936 14.132 24.508 1.00 18.06 ? 403 HIS A CG 1 ATOM 3097 N ND1 . HIS A 1 403 ? -10.302 12.894 24.993 1.00 20.16 ? 403 HIS A ND1 1 ATOM 3098 C CD2 . HIS A 1 403 ? -10.583 14.277 23.327 1.00 17.91 ? 403 HIS A CD2 1 ATOM 3099 C CE1 . HIS A 1 403 ? -11.135 12.319 24.141 1.00 16.60 ? 403 HIS A CE1 1 ATOM 3100 N NE2 . HIS A 1 403 ? -11.321 13.138 23.122 1.00 19.46 ? 403 HIS A NE2 1 ATOM 3101 N N . ASP A 1 404 ? -7.330 15.865 28.284 1.00 17.66 ? 404 ASP A N 1 ATOM 3102 C CA . ASP A 1 404 ? -6.340 16.775 28.812 1.00 17.86 ? 404 ASP A CA 1 ATOM 3103 C C . ASP A 1 404 ? -5.128 15.984 29.310 1.00 16.94 ? 404 ASP A C 1 ATOM 3104 O O . ASP A 1 404 ? -5.179 14.761 29.411 1.00 17.20 ? 404 ASP A O 1 ATOM 3105 C CB . ASP A 1 404 ? -6.935 17.608 29.968 1.00 17.88 ? 404 ASP A CB 1 ATOM 3106 C CG . ASP A 1 404 ? -6.278 18.974 30.094 1.00 20.01 ? 404 ASP A CG 1 ATOM 3107 O OD1 . ASP A 1 404 ? -5.225 19.193 29.448 1.00 19.43 ? 404 ASP A OD1 1 ATOM 3108 O OD2 . ASP A 1 404 ? -6.738 19.894 30.809 1.00 20.98 ? 404 ASP A OD2 1 ATOM 3109 N N . THR A 1 405 ? -4.047 16.696 29.618 1.00 16.43 ? 405 THR A N 1 ATOM 3110 C CA . THR A 1 405 ? -2.838 16.095 30.171 1.00 16.52 ? 405 THR A CA 1 ATOM 3111 C C . THR A 1 405 ? -2.441 16.869 31.416 1.00 16.75 ? 405 THR A C 1 ATOM 3112 O O . THR A 1 405 ? -2.253 18.084 31.364 1.00 17.05 ? 405 THR A O 1 ATOM 3113 C CB . THR A 1 405 ? -1.727 16.145 29.129 1.00 17.62 ? 405 THR A CB 1 ATOM 3114 O OG1 . THR A 1 405 ? -2.088 15.294 28.036 1.00 15.35 ? 405 THR A OG1 1 ATOM 3115 C CG2 . THR A 1 405 ? -0.347 15.579 29.695 1.00 16.59 ? 405 THR A CG2 1 ATOM 3116 N N . ALA A 1 406 ? -2.325 16.152 32.530 1.00 16.87 ? 406 ALA A N 1 ATOM 3117 C CA . ALA A 1 406 ? -1.757 16.677 33.763 1.00 16.77 ? 406 ALA A CA 1 ATOM 3118 C C . ALA A 1 406 ? -0.251 16.650 33.567 1.00 16.93 ? 406 ALA A C 1 ATOM 3119 O O . ALA A 1 406 ? 0.293 15.618 33.157 1.00 16.97 ? 406 ALA A O 1 ATOM 3120 C CB . ALA A 1 406 ? -2.130 15.773 34.939 1.00 16.65 ? 406 ALA A CB 1 ATOM 3121 N N . VAL A 1 407 ? 0.429 17.760 33.845 1.00 16.41 ? 407 VAL A N 1 ATOM 3122 C CA . VAL A 1 407 ? 1.881 17.789 33.662 1.00 16.86 ? 407 VAL A CA 1 ATOM 3123 C C . VAL A 1 407 ? 2.593 18.410 34.859 1.00 17.19 ? 407 VAL A C 1 ATOM 3124 O O . VAL A 1 407 ? 2.320 19.540 35.242 1.00 17.02 ? 407 VAL A O 1 ATOM 3125 C CB . VAL A 1 407 ? 2.329 18.523 32.359 1.00 16.37 ? 407 VAL A CB 1 ATOM 3126 C CG1 . VAL A 1 407 ? 3.857 18.443 32.201 1.00 15.46 ? 407 VAL A CG1 1 ATOM 3127 C CG2 . VAL A 1 407 ? 1.650 17.918 31.125 1.00 16.19 ? 407 VAL A CG2 1 ATOM 3128 N N . ILE A 1 408 ? 3.513 17.660 35.444 1.00 18.10 ? 408 ILE A N 1 ATOM 3129 C CA . ILE A 1 408 ? 4.172 18.111 36.647 1.00 18.52 ? 408 ILE A CA 1 ATOM 3130 C C . ILE A 1 408 ? 5.655 17.924 36.477 1.00 19.07 ? 408 ILE A C 1 ATOM 3131 O O . ILE A 1 408 ? 6.109 17.093 35.693 1.00 18.86 ? 408 ILE A O 1 ATOM 3132 C CB . ILE A 1 408 ? 3.674 17.303 37.877 1.00 18.92 ? 408 ILE A CB 1 ATOM 3133 C CG1 . ILE A 1 408 ? 3.788 15.805 37.619 1.00 19.82 ? 408 ILE A CG1 1 ATOM 3134 C CG2 . ILE A 1 408 ? 2.239 17.710 38.243 1.00 17.90 ? 408 ILE A CG2 1 ATOM 3135 C CD1 . ILE A 1 408 ? 3.736 14.941 38.872 1.00 21.86 ? 408 ILE A CD1 1 ATOM 3136 N N . LEU A 1 409 ? 6.413 18.709 37.218 1.00 19.47 ? 409 LEU A N 1 ATOM 3137 C CA . LEU A 1 409 ? 7.847 18.562 37.223 1.00 20.95 ? 409 LEU A CA 1 ATOM 3138 C C . LEU A 1 409 ? 8.163 18.100 38.628 1.00 21.65 ? 409 LEU A C 1 ATOM 3139 O O . LEU A 1 409 ? 7.796 18.758 39.590 1.00 21.61 ? 409 LEU A O 1 ATOM 3140 C CB . LEU A 1 409 ? 8.512 19.902 36.907 1.00 20.92 ? 409 LEU A CB 1 ATOM 3141 C CG . LEU A 1 409 ? 10.021 20.030 36.662 1.00 23.60 ? 409 LEU A CG 1 ATOM 3142 C CD1 . LEU A 1 409 ? 10.570 18.959 35.712 1.00 23.26 ? 409 LEU A CD1 1 ATOM 3143 C CD2 . LEU A 1 409 ? 10.331 21.428 36.131 1.00 24.03 ? 409 LEU A CD2 1 ATOM 3144 N N . VAL A 1 410 ? 8.836 16.967 38.732 1.00 22.11 ? 410 VAL A N 1 ATOM 3145 C CA . VAL A 1 410 ? 9.167 16.386 40.018 1.00 22.60 ? 410 VAL A CA 1 ATOM 3146 C C . VAL A 1 410 ? 10.584 16.824 40.326 1.00 23.46 ? 410 VAL A C 1 ATOM 3147 O O . VAL A 1 410 ? 11.506 16.562 39.564 1.00 23.06 ? 410 VAL A O 1 ATOM 3148 C CB . VAL A 1 410 ? 8.999 14.858 40.032 1.00 22.11 ? 410 VAL A CB 1 ATOM 3149 C CG1 . VAL A 1 410 ? 9.322 14.310 41.409 1.00 21.88 ? 410 VAL A CG1 1 ATOM 3150 C CG2 . VAL A 1 410 ? 7.590 14.487 39.661 1.00 21.35 ? 410 VAL A CG2 1 ATOM 3151 N N . GLY A 1 411 ? 10.735 17.501 41.454 1.00 24.72 ? 411 GLY A N 1 ATOM 3152 C CA . GLY A 1 411 ? 11.980 18.146 41.771 1.00 27.57 ? 411 GLY A CA 1 ATOM 3153 C C . GLY A 1 411 ? 12.805 17.304 42.702 1.00 29.55 ? 411 GLY A C 1 ATOM 3154 O O . GLY A 1 411 ? 12.844 16.074 42.595 1.00 28.69 ? 411 GLY A O 1 ATOM 3155 N N . LYS A 1 412 ? 13.469 17.985 43.622 1.00 32.32 ? 412 LYS A N 1 ATOM 3156 C CA . LYS A 1 412 ? 14.320 17.301 44.573 1.00 34.92 ? 412 LYS A CA 1 ATOM 3157 C C . LYS A 1 412 ? 13.472 16.600 45.619 1.00 36.23 ? 412 LYS A C 1 ATOM 3158 O O . LYS A 1 412 ? 12.358 17.024 45.931 1.00 36.05 ? 412 LYS A O 1 ATOM 3159 C CB . LYS A 1 412 ? 15.328 18.263 45.214 1.00 35.45 ? 412 LYS A CB 1 ATOM 3160 C CG . LYS A 1 412 ? 14.814 19.674 45.454 1.00 36.81 ? 412 LYS A CG 1 ATOM 3161 C CD . LYS A 1 412 ? 15.865 20.537 46.142 1.00 39.73 ? 412 LYS A CD 1 ATOM 3162 C CE . LYS A 1 412 ? 15.581 20.629 47.645 1.00 41.07 ? 412 LYS A CE 1 ATOM 3163 N NZ . LYS A 1 412 ? 16.826 20.494 48.468 1.00 40.83 ? 412 LYS A NZ 1 ATOM 3164 N N . LYS A 1 413 ? 14.016 15.514 46.154 1.00 38.25 ? 413 LYS A N 1 ATOM 3165 C CA . LYS A 1 413 ? 13.378 14.810 47.252 1.00 40.31 ? 413 LYS A CA 1 ATOM 3166 C C . LYS A 1 413 ? 13.219 15.772 48.442 1.00 41.10 ? 413 LYS A C 1 ATOM 3167 O O . LYS A 1 413 ? 13.998 16.722 48.600 1.00 40.71 ? 413 LYS A O 1 ATOM 3168 C CB . LYS A 1 413 ? 14.202 13.577 47.640 1.00 40.58 ? 413 LYS A CB 1 ATOM 3169 C CG . LYS A 1 413 ? 13.334 12.431 48.141 1.00 42.39 ? 413 LYS A CG 1 ATOM 3170 C CD . LYS A 1 413 ? 13.582 11.148 47.359 1.00 44.11 ? 413 LYS A CD 1 ATOM 3171 C CE . LYS A 1 413 ? 12.422 10.164 47.558 1.00 45.41 ? 413 LYS A CE 1 ATOM 3172 N NZ . LYS A 1 413 ? 12.699 8.824 46.954 1.00 45.22 ? 413 LYS A NZ 1 ATOM 3173 N N . CYS A 1 414 ? 12.211 15.528 49.273 1.00 42.46 ? 414 CYS A N 1 ATOM 3174 C CA . CYS A 1 414 ? 11.964 16.397 50.414 1.00 43.92 ? 414 CYS A CA 1 ATOM 3175 C C . CYS A 1 414 ? 11.384 15.653 51.611 1.00 47.00 ? 414 CYS A C 1 ATOM 3176 O O . CYS A 1 414 ? 10.955 14.508 51.493 1.00 47.27 ? 414 CYS A O 1 ATOM 3177 C CB . CYS A 1 414 ? 11.028 17.533 50.000 1.00 43.07 ? 414 CYS A CB 1 ATOM 3178 S SG . CYS A 1 414 ? 9.540 16.934 49.183 1.00 36.40 ? 414 CYS A SG 1 ATOM 3179 N N . GLN A 1 415 ? 11.391 16.330 52.758 1.00 50.58 ? 415 GLN A N 1 ATOM 3180 C CA . GLN A 1 415 ? 10.673 15.915 53.974 1.00 54.25 ? 415 GLN A CA 1 ATOM 3181 C C . GLN A 1 415 ? 10.783 14.443 54.393 1.00 56.32 ? 415 GLN A C 1 ATOM 3182 O O . GLN A 1 415 ? 9.776 13.715 54.435 1.00 56.66 ? 415 GLN A O 1 ATOM 3183 C CB . GLN A 1 415 ? 9.197 16.331 53.835 1.00 54.21 ? 415 GLN A CB 1 ATOM 3184 C CG . GLN A 1 415 ? 8.501 16.684 55.131 1.00 56.07 ? 415 GLN A CG 1 ATOM 3185 C CD . GLN A 1 415 ? 7.414 15.692 55.496 1.00 58.35 ? 415 GLN A CD 1 ATOM 3186 O OE1 . GLN A 1 415 ? 6.731 15.155 54.612 1.00 58.23 ? 415 GLN A OE1 1 ATOM 3187 N NE2 . GLN A 1 415 ? 7.246 15.445 56.798 1.00 57.91 ? 415 GLN A NE2 1 ATOM 3188 N N . ARG A 1 416 ? 12.007 14.015 54.705 1.00 59.00 ? 416 ARG A N 1 ATOM 3189 C CA . ARG A 1 416 ? 12.263 12.641 55.139 1.00 61.61 ? 416 ARG A CA 1 ATOM 3190 C C . ARG A 1 416 ? 12.186 12.434 56.666 1.00 63.04 ? 416 ARG A C 1 ATOM 3191 O O . ARG A 1 416 ? 11.934 13.378 57.427 1.00 63.23 ? 416 ARG A O 1 ATOM 3192 C CB . ARG A 1 416 ? 13.603 12.132 54.594 1.00 61.92 ? 416 ARG A CB 1 ATOM 3193 C CG . ARG A 1 416 ? 14.830 12.792 55.203 1.00 63.72 ? 416 ARG A CG 1 ATOM 3194 C CD . ARG A 1 416 ? 15.646 13.650 54.236 1.00 66.95 ? 416 ARG A CD 1 ATOM 3195 N NE . ARG A 1 416 ? 16.667 14.420 54.951 1.00 69.31 ? 416 ARG A NE 1 ATOM 3196 C CZ . ARG A 1 416 ? 17.941 14.054 55.082 1.00 70.59 ? 416 ARG A CZ 1 ATOM 3197 N NH1 . ARG A 1 416 ? 18.374 12.920 54.547 1.00 71.39 ? 416 ARG A NH1 1 ATOM 3198 N NH2 . ARG A 1 416 ? 18.788 14.825 55.752 1.00 71.01 ? 416 ARG A NH2 1 ATOM 3199 N N . TRP A 1 417 ? 12.412 11.191 57.096 1.00 64.76 ? 417 TRP A N 1 ATOM 3200 C CA . TRP A 1 417 ? 12.126 10.762 58.471 1.00 66.40 ? 417 TRP A CA 1 ATOM 3201 C C . TRP A 1 417 ? 13.125 9.715 59.012 1.00 66.44 ? 417 TRP A C 1 ATOM 3202 O O . TRP A 1 417 ? 13.741 9.848 60.076 1.00 66.34 ? 417 TRP A O 1 ATOM 3203 C CB . TRP A 1 417 ? 10.666 10.255 58.542 1.00 67.08 ? 417 TRP A CB 1 ATOM 3204 C CG . TRP A 1 417 ? 10.425 9.119 59.507 1.00 70.32 ? 417 TRP A CG 1 ATOM 3205 C CD1 . TRP A 1 417 ? 10.085 9.217 60.834 1.00 72.74 ? 417 TRP A CD1 1 ATOM 3206 C CD2 . TRP A 1 417 ? 10.506 7.714 59.220 1.00 73.35 ? 417 TRP A CD2 1 ATOM 3207 N NE1 . TRP A 1 417 ? 9.951 7.962 61.383 1.00 74.10 ? 417 TRP A NE1 1 ATOM 3208 C CE2 . TRP A 1 417 ? 10.204 7.021 60.415 1.00 74.28 ? 417 TRP A CE2 1 ATOM 3209 C CE3 . TRP A 1 417 ? 10.804 6.966 58.068 1.00 74.11 ? 417 TRP A CE3 1 ATOM 3210 C CZ2 . TRP A 1 417 ? 10.192 5.623 60.490 1.00 75.13 ? 417 TRP A CZ2 1 ATOM 3211 C CZ3 . TRP A 1 417 ? 10.792 5.579 58.147 1.00 74.84 ? 417 TRP A CZ3 1 ATOM 3212 C CH2 . TRP A 1 417 ? 10.488 4.923 59.348 1.00 75.24 ? 417 TRP A CH2 1 ATOM 3213 O OXT . TRP A 1 417 ? 13.393 8.661 58.430 1.00 66.72 ? 417 TRP A OXT 1 HETATM 3214 C C1 . NAG B 2 . ? 3.721 32.098 -8.674 1.00 37.29 ? 500 NAG A C1 1 HETATM 3215 C C2 . NAG B 2 . ? 2.951 31.192 -9.630 1.00 39.17 ? 500 NAG A C2 1 HETATM 3216 C C3 . NAG B 2 . ? 1.707 31.894 -10.175 1.00 40.06 ? 500 NAG A C3 1 HETATM 3217 C C4 . NAG B 2 . ? 0.894 32.628 -9.116 1.00 41.57 ? 500 NAG A C4 1 HETATM 3218 C C5 . NAG B 2 . ? 1.821 33.422 -8.208 1.00 40.33 ? 500 NAG A C5 1 HETATM 3219 C C6 . NAG B 2 . ? 1.049 34.065 -7.053 1.00 39.69 ? 500 NAG A C6 1 HETATM 3220 C C7 . NAG B 2 . ? 4.490 29.675 -10.759 1.00 38.90 ? 500 NAG A C7 1 HETATM 3221 C C8 . NAG B 2 . ? 5.095 29.278 -12.077 1.00 39.04 ? 500 NAG A C8 1 HETATM 3222 N N2 . NAG B 2 . ? 3.792 30.811 -10.754 1.00 37.17 ? 500 NAG A N2 1 HETATM 3223 O O3 . NAG B 2 . ? 0.909 30.920 -10.797 1.00 41.32 ? 500 NAG A O3 1 HETATM 3224 O O4 . NAG B 2 . ? 0.024 33.567 -9.721 1.00 45.85 ? 500 NAG A O4 1 HETATM 3225 O O5 . NAG B 2 . ? 2.826 32.576 -7.697 1.00 38.31 ? 500 NAG A O5 1 HETATM 3226 O O6 . NAG B 2 . ? 0.563 33.062 -6.182 1.00 39.16 ? 500 NAG A O6 1 HETATM 3227 O O7 . NAG B 2 . ? 4.648 28.969 -9.753 1.00 37.66 ? 500 NAG A O7 1 HETATM 3228 C C1 . NAG C 2 . ? -1.242 32.980 -10.073 1.00 48.90 ? 501 NAG A C1 1 HETATM 3229 C C2 . NAG C 2 . ? -2.382 34.000 -10.007 1.00 50.23 ? 501 NAG A C2 1 HETATM 3230 C C3 . NAG C 2 . ? -3.699 33.300 -10.317 1.00 52.12 ? 501 NAG A C3 1 HETATM 3231 C C4 . NAG C 2 . ? -3.620 32.560 -11.653 1.00 52.43 ? 501 NAG A C4 1 HETATM 3232 C C5 . NAG C 2 . ? -2.353 31.702 -11.728 1.00 51.78 ? 501 NAG A C5 1 HETATM 3233 C C6 . NAG C 2 . ? -2.155 31.143 -13.131 1.00 51.77 ? 501 NAG A C6 1 HETATM 3234 C C7 . NAG C 2 . ? -1.969 35.772 -8.371 1.00 50.94 ? 501 NAG A C7 1 HETATM 3235 C C8 . NAG C 2 . ? -2.381 36.290 -7.022 1.00 52.34 ? 501 NAG A C8 1 HETATM 3236 N N2 . NAG C 2 . ? -2.503 34.599 -8.699 1.00 50.42 ? 501 NAG A N2 1 HETATM 3237 O O3 . NAG C 2 . ? -4.768 34.228 -10.312 1.00 54.13 ? 501 NAG A O3 1 HETATM 3238 O O4 . NAG C 2 . ? -4.762 31.737 -11.791 1.00 53.77 ? 501 NAG A O4 1 HETATM 3239 O O5 . NAG C 2 . ? -1.192 32.439 -11.372 1.00 49.51 ? 501 NAG A O5 1 HETATM 3240 O O6 . NAG C 2 . ? -0.785 31.204 -13.464 1.00 51.53 ? 501 NAG A O6 1 HETATM 3241 O O7 . NAG C 2 . ? -1.194 36.408 -9.091 1.00 50.29 ? 501 NAG A O7 1 HETATM 3242 C C1 . NAG D 2 . ? 2.122 -5.028 20.596 1.00 26.24 ? 600 NAG A C1 1 HETATM 3243 C C2 . NAG D 2 . ? 2.649 -6.197 21.420 1.00 27.86 ? 600 NAG A C2 1 HETATM 3244 C C3 . NAG D 2 . ? 3.806 -5.779 22.336 1.00 27.75 ? 600 NAG A C3 1 HETATM 3245 C C4 . NAG D 2 . ? 4.868 -4.979 21.560 1.00 27.03 ? 600 NAG A C4 1 HETATM 3246 C C5 . NAG D 2 . ? 4.172 -3.936 20.701 1.00 26.65 ? 600 NAG A C5 1 HETATM 3247 C C6 . NAG D 2 . ? 5.135 -3.146 19.835 1.00 27.70 ? 600 NAG A C6 1 HETATM 3248 C C7 . NAG D 2 . ? 1.140 -8.026 21.876 1.00 33.78 ? 600 NAG A C7 1 HETATM 3249 C C8 . NAG D 2 . ? -0.177 -8.448 22.473 1.00 34.38 ? 600 NAG A C8 1 HETATM 3250 N N2 . NAG D 2 . ? 1.580 -6.808 22.177 1.00 30.77 ? 600 NAG A N2 1 HETATM 3251 O O3 . NAG D 2 . ? 4.386 -6.937 22.909 1.00 28.04 ? 600 NAG A O3 1 HETATM 3252 O O4 . NAG D 2 . ? 5.696 -4.225 22.409 1.00 24.73 ? 600 NAG A O4 1 HETATM 3253 O O5 . NAG D 2 . ? 3.241 -4.570 19.874 1.00 25.45 ? 600 NAG A O5 1 HETATM 3254 O O6 . NAG D 2 . ? 5.878 -4.074 19.094 1.00 29.52 ? 600 NAG A O6 1 HETATM 3255 O O7 . NAG D 2 . ? 1.774 -8.782 21.145 1.00 37.16 ? 600 NAG A O7 1 HETATM 3256 C C1 . NAG E 2 . ? 6.717 -4.982 23.084 1.00 24.39 ? 601 NAG A C1 1 HETATM 3257 C C2 . NAG E 2 . ? 7.859 -4.046 23.463 1.00 24.32 ? 601 NAG A C2 1 HETATM 3258 C C3 . NAG E 2 . ? 8.857 -4.774 24.382 1.00 24.92 ? 601 NAG A C3 1 HETATM 3259 C C4 . NAG E 2 . ? 8.153 -5.432 25.569 1.00 26.10 ? 601 NAG A C4 1 HETATM 3260 C C5 . NAG E 2 . ? 7.074 -6.341 25.025 1.00 26.04 ? 601 NAG A C5 1 HETATM 3261 C C6 . NAG E 2 . ? 6.276 -7.034 26.134 1.00 25.65 ? 601 NAG A C6 1 HETATM 3262 C C7 . NAG E 2 . ? 8.345 -2.294 21.807 1.00 22.77 ? 601 NAG A C7 1 HETATM 3263 C C8 . NAG E 2 . ? 9.130 -1.886 20.579 1.00 23.05 ? 601 NAG A C8 1 HETATM 3264 N N2 . NAG E 2 . ? 8.506 -3.544 22.259 1.00 23.08 ? 601 NAG A N2 1 HETATM 3265 O O3 . NAG E 2 . ? 9.868 -3.910 24.842 1.00 24.26 ? 601 NAG A O3 1 HETATM 3266 O O4 . NAG E 2 . ? 9.059 -6.271 26.231 1.00 28.36 ? 601 NAG A O4 1 HETATM 3267 O O5 . NAG E 2 . ? 6.197 -5.549 24.257 1.00 24.83 ? 601 NAG A O5 1 HETATM 3268 O O6 . NAG E 2 . ? 5.312 -7.858 25.527 1.00 27.74 ? 601 NAG A O6 1 HETATM 3269 O O7 . NAG E 2 . ? 7.596 -1.478 22.343 1.00 21.44 ? 601 NAG A O7 1 HETATM 3270 C C1 . BMA F 3 . ? 9.509 -5.715 27.473 1.00 31.02 ? 602 BMA A C1 1 HETATM 3271 C C2 . BMA F 3 . ? 9.858 -6.856 28.427 1.00 33.98 ? 602 BMA A C2 1 HETATM 3272 C C3 . BMA F 3 . ? 10.312 -6.269 29.766 1.00 37.03 ? 602 BMA A C3 1 HETATM 3273 C C4 . BMA F 3 . ? 11.456 -5.302 29.535 1.00 35.39 ? 602 BMA A C4 1 HETATM 3274 C C5 . BMA F 3 . ? 10.893 -4.260 28.593 1.00 31.80 ? 602 BMA A C5 1 HETATM 3275 C C6 . BMA F 3 . ? 11.832 -3.080 28.472 1.00 31.74 ? 602 BMA A C6 1 HETATM 3276 O O2 . BMA F 3 . ? 10.884 -7.607 27.817 1.00 32.13 ? 602 BMA A O2 1 HETATM 3277 O O3 . BMA F 3 . ? 10.654 -7.250 30.719 1.00 43.16 ? 602 BMA A O3 1 HETATM 3278 O O4 . BMA F 3 . ? 11.781 -4.635 30.722 1.00 36.12 ? 602 BMA A O4 1 HETATM 3279 O O5 . BMA F 3 . ? 10.633 -4.872 27.345 1.00 28.77 ? 602 BMA A O5 1 HETATM 3280 O O6 . BMA F 3 . ? 12.001 -2.916 27.099 1.00 27.31 ? 602 BMA A O6 1 HETATM 3281 C C1 . MAN G 4 . ? 9.434 -7.563 31.444 1.00 49.79 ? 603 MAN A C1 1 HETATM 3282 C C2 . MAN G 4 . ? 9.477 -7.059 32.888 1.00 52.43 ? 603 MAN A C2 1 HETATM 3283 C C3 . MAN G 4 . ? 10.678 -7.683 33.600 1.00 53.56 ? 603 MAN A C3 1 HETATM 3284 C C4 . MAN G 4 . ? 10.764 -9.189 33.359 1.00 54.28 ? 603 MAN A C4 1 HETATM 3285 C C5 . MAN G 4 . ? 10.436 -9.549 31.912 1.00 54.73 ? 603 MAN A C5 1 HETATM 3286 C C6 . MAN G 4 . ? 10.418 -11.048 31.670 1.00 55.91 ? 603 MAN A C6 1 HETATM 3287 O O2 . MAN G 4 . ? 8.283 -7.394 33.584 1.00 52.64 ? 603 MAN A O2 1 HETATM 3288 O O3 . MAN G 4 . ? 10.632 -7.393 34.981 1.00 54.04 ? 603 MAN A O3 1 HETATM 3289 O O4 . MAN G 4 . ? 12.097 -9.574 33.608 1.00 55.88 ? 603 MAN A O4 1 HETATM 3290 O O5 . MAN G 4 . ? 9.221 -8.952 31.486 1.00 53.17 ? 603 MAN A O5 1 HETATM 3291 O O6 . MAN G 4 . ? 11.678 -11.381 31.135 1.00 57.24 ? 603 MAN A O6 1 HETATM 3292 C C1 . MAN H 4 . ? 12.744 -1.730 26.834 1.00 28.22 ? 604 MAN A C1 1 HETATM 3293 C C2 . MAN H 4 . ? 12.069 -0.560 26.107 1.00 25.68 ? 604 MAN A C2 1 HETATM 3294 C C3 . MAN H 4 . ? 11.431 -0.995 24.805 1.00 24.47 ? 604 MAN A C3 1 HETATM 3295 C C4 . MAN H 4 . ? 12.468 -1.758 24.006 1.00 25.93 ? 604 MAN A C4 1 HETATM 3296 C C5 . MAN H 4 . ? 13.024 -2.893 24.847 1.00 29.17 ? 604 MAN A C5 1 HETATM 3297 C C6 . MAN H 4 . ? 14.102 -3.626 24.080 1.00 34.06 ? 604 MAN A C6 1 HETATM 3298 O O2 . MAN H 4 . ? 13.138 0.322 25.808 1.00 25.94 ? 604 MAN A O2 1 HETATM 3299 O O3 . MAN H 4 . ? 11.084 0.140 24.063 1.00 20.97 ? 604 MAN A O3 1 HETATM 3300 O O4 . MAN H 4 . ? 11.900 -2.279 22.839 1.00 25.65 ? 604 MAN A O4 1 HETATM 3301 O O5 . MAN H 4 . ? 13.663 -2.303 25.950 1.00 27.34 ? 604 MAN A O5 1 HETATM 3302 O O6 . MAN H 4 . ? 15.060 -2.661 23.746 1.00 40.19 ? 604 MAN A O6 1 HETATM 3303 C C1 . MAN I 4 . ? 15.783 -3.183 22.620 1.00 47.23 ? 605 MAN A C1 1 HETATM 3304 C C2 . MAN I 4 . ? 17.219 -2.723 22.757 1.00 49.50 ? 605 MAN A C2 1 HETATM 3305 C C3 . MAN I 4 . ? 17.381 -1.267 22.334 1.00 51.05 ? 605 MAN A C3 1 HETATM 3306 C C4 . MAN I 4 . ? 16.775 -1.045 20.958 1.00 51.41 ? 605 MAN A C4 1 HETATM 3307 C C5 . MAN I 4 . ? 15.352 -1.569 20.908 1.00 50.82 ? 605 MAN A C5 1 HETATM 3308 C C6 . MAN I 4 . ? 14.799 -1.444 19.498 1.00 51.72 ? 605 MAN A C6 1 HETATM 3309 O O2 . MAN I 4 . ? 18.003 -3.560 21.943 1.00 50.67 ? 605 MAN A O2 1 HETATM 3310 O O3 . MAN I 4 . ? 18.754 -0.947 22.294 1.00 51.83 ? 605 MAN A O3 1 HETATM 3311 O O4 . MAN I 4 . ? 16.777 0.334 20.664 1.00 52.44 ? 605 MAN A O4 1 HETATM 3312 O O5 . MAN I 4 . ? 15.303 -2.925 21.302 1.00 49.61 ? 605 MAN A O5 1 HETATM 3313 O O6 . MAN I 4 . ? 14.466 -2.732 19.042 1.00 53.29 ? 605 MAN A O6 1 HETATM 3314 C C1 . MAN J 4 . ? 9.691 0.210 24.095 1.00 18.31 ? 606 MAN A C1 1 HETATM 3315 C C2 . MAN J 4 . ? 9.338 1.195 22.997 1.00 13.56 ? 606 MAN A C2 1 HETATM 3316 C C3 . MAN J 4 . ? 9.781 2.612 23.367 1.00 15.93 ? 606 MAN A C3 1 HETATM 3317 C C4 . MAN J 4 . ? 9.238 2.940 24.755 1.00 16.33 ? 606 MAN A C4 1 HETATM 3318 C C5 . MAN J 4 . ? 9.686 1.902 25.787 1.00 18.28 ? 606 MAN A C5 1 HETATM 3319 C C6 . MAN J 4 . ? 8.942 2.166 27.092 1.00 19.18 ? 606 MAN A C6 1 HETATM 3320 O O2 . MAN J 4 . ? 7.954 1.089 22.890 1.00 15.66 ? 606 MAN A O2 1 HETATM 3321 O O3 . MAN J 4 . ? 9.260 3.583 22.469 1.00 16.68 ? 606 MAN A O3 1 HETATM 3322 O O4 . MAN J 4 . ? 9.626 4.237 25.123 1.00 15.65 ? 606 MAN A O4 1 HETATM 3323 O O5 . MAN J 4 . ? 9.263 0.608 25.390 1.00 18.65 ? 606 MAN A O5 1 HETATM 3324 O O6 . MAN J 4 . ? 9.566 1.361 28.065 1.00 24.44 ? 606 MAN A O6 1 HETATM 3325 C C1 . NAG K 2 . ? 22.439 10.130 17.156 1.00 23.67 ? 700 NAG A C1 1 HETATM 3326 C C2 . NAG K 2 . ? 22.359 9.284 18.421 1.00 24.32 ? 700 NAG A C2 1 HETATM 3327 C C3 . NAG K 2 . ? 22.879 10.060 19.638 1.00 23.58 ? 700 NAG A C3 1 HETATM 3328 C C4 . NAG K 2 . ? 24.265 10.646 19.369 1.00 24.37 ? 700 NAG A C4 1 HETATM 3329 C C5 . NAG K 2 . ? 24.278 11.305 18.000 1.00 22.29 ? 700 NAG A C5 1 HETATM 3330 C C6 . NAG K 2 . ? 25.689 11.761 17.645 1.00 25.37 ? 700 NAG A C6 1 HETATM 3331 C C7 . NAG K 2 . ? 20.822 7.506 19.027 1.00 26.84 ? 700 NAG A C7 1 HETATM 3332 C C8 . NAG K 2 . ? 19.408 7.068 19.292 1.00 23.84 ? 700 NAG A C8 1 HETATM 3333 N N2 . NAG K 2 . ? 21.033 8.776 18.655 1.00 25.86 ? 700 NAG A N2 1 HETATM 3334 O O3 . NAG K 2 . ? 22.857 9.250 20.797 1.00 22.09 ? 700 NAG A O3 1 HETATM 3335 O O4 . NAG K 2 . ? 24.519 11.719 20.240 1.00 24.71 ? 700 NAG A O4 1 HETATM 3336 O O5 . NAG K 2 . ? 23.805 10.413 17.020 1.00 23.03 ? 700 NAG A O5 1 HETATM 3337 O O6 . NAG K 2 . ? 26.514 10.625 17.480 1.00 23.77 ? 700 NAG A O6 1 HETATM 3338 O O7 . NAG K 2 . ? 21.736 6.700 19.153 1.00 26.83 ? 700 NAG A O7 1 HETATM 3339 C C1 . NAG L 2 . ? 25.178 11.314 21.433 1.00 26.57 ? 701 NAG A C1 1 HETATM 3340 C C2 . NAG L 2 . ? 26.074 12.452 21.891 1.00 25.92 ? 701 NAG A C2 1 HETATM 3341 C C3 . NAG L 2 . ? 26.711 12.090 23.230 1.00 28.73 ? 701 NAG A C3 1 HETATM 3342 C C4 . NAG L 2 . ? 25.630 11.638 24.212 1.00 31.44 ? 701 NAG A C4 1 HETATM 3343 C C5 . NAG L 2 . ? 24.792 10.521 23.585 1.00 28.92 ? 701 NAG A C5 1 HETATM 3344 C C6 . NAG L 2 . ? 23.650 9.976 24.451 1.00 28.16 ? 701 NAG A C6 1 HETATM 3345 C C7 . NAG L 2 . ? 27.442 13.840 20.460 1.00 23.35 ? 701 NAG A C7 1 HETATM 3346 C C8 . NAG L 2 . ? 28.561 13.893 19.452 1.00 24.62 ? 701 NAG A C8 1 HETATM 3347 N N2 . NAG L 2 . ? 27.092 12.640 20.890 1.00 23.15 ? 701 NAG A N2 1 HETATM 3348 O O3 . NAG L 2 . ? 27.407 13.199 23.759 1.00 28.01 ? 701 NAG A O3 1 HETATM 3349 O O4 . NAG L 2 . ? 26.283 11.207 25.378 1.00 35.97 ? 701 NAG A O4 1 HETATM 3350 O O5 . NAG L 2 . ? 24.221 11.038 22.411 1.00 26.89 ? 701 NAG A O5 1 HETATM 3351 O O6 . NAG L 2 . ? 22.816 11.021 24.905 1.00 26.61 ? 701 NAG A O6 1 HETATM 3352 O O7 . NAG L 2 . ? 26.890 14.858 20.860 1.00 24.56 ? 701 NAG A O7 1 HETATM 3353 C C1 . BMA M 3 . ? 25.664 11.765 26.555 1.00 42.93 ? 702 BMA A C1 1 HETATM 3354 C C2 . BMA M 3 . ? 26.166 10.907 27.706 1.00 46.07 ? 702 BMA A C2 1 HETATM 3355 C C3 . BMA M 3 . ? 25.682 11.384 29.070 1.00 50.30 ? 702 BMA A C3 1 HETATM 3356 C C4 . BMA M 3 . ? 25.782 12.901 29.204 1.00 49.09 ? 702 BMA A C4 1 HETATM 3357 C C5 . BMA M 3 . ? 25.277 13.630 27.950 1.00 48.10 ? 702 BMA A C5 1 HETATM 3358 C C6 . BMA M 3 . ? 25.450 15.146 28.080 1.00 48.40 ? 702 BMA A C6 1 HETATM 3359 O O2 . BMA M 3 . ? 27.570 10.934 27.655 1.00 45.75 ? 702 BMA A O2 1 HETATM 3360 O O3 . BMA M 3 . ? 26.446 10.751 30.081 1.00 55.90 ? 702 BMA A O3 1 HETATM 3361 O O4 . BMA M 3 . ? 25.035 13.290 30.336 1.00 49.42 ? 702 BMA A O4 1 HETATM 3362 O O5 . BMA M 3 . ? 25.923 13.143 26.778 1.00 44.38 ? 702 BMA A O5 1 HETATM 3363 O O6 . BMA M 3 . ? 26.776 15.534 27.768 1.00 50.45 ? 702 BMA A O6 1 HETATM 3364 C C1 . MAN N 4 . ? 25.610 9.897 30.904 1.00 60.93 ? 703 MAN A C1 1 HETATM 3365 C C2 . MAN N 4 . ? 26.129 9.880 32.346 1.00 62.75 ? 703 MAN A C2 1 HETATM 3366 C C3 . MAN N 4 . ? 27.457 9.132 32.469 1.00 64.10 ? 703 MAN A C3 1 HETATM 3367 C C4 . MAN N 4 . ? 27.575 7.904 31.560 1.00 65.02 ? 703 MAN A C4 1 HETATM 3368 C C5 . MAN N 4 . ? 26.787 7.973 30.244 1.00 64.91 ? 703 MAN A C5 1 HETATM 3369 C C6 . MAN N 4 . ? 26.640 6.578 29.630 1.00 65.92 ? 703 MAN A C6 1 HETATM 3370 O O2 . MAN N 4 . ? 25.183 9.315 33.234 1.00 61.88 ? 703 MAN A O2 1 HETATM 3371 O O3 . MAN N 4 . ? 27.641 8.722 33.810 1.00 64.63 ? 703 MAN A O3 1 HETATM 3372 O O4 . MAN N 4 . ? 28.947 7.740 31.260 1.00 65.88 ? 703 MAN A O4 1 HETATM 3373 O O5 . MAN N 4 . ? 25.516 8.571 30.424 1.00 63.20 ? 703 MAN A O5 1 HETATM 3374 O O6 . MAN N 4 . ? 25.484 6.495 28.824 1.00 66.85 ? 703 MAN A O6 1 HETATM 3375 C C1 . NAG O 2 . ? -8.117 0.351 21.959 1.00 24.04 ? 800 NAG A C1 1 HETATM 3376 C C2 . NAG O 2 . ? -8.869 -0.906 21.484 1.00 27.34 ? 800 NAG A C2 1 HETATM 3377 C C3 . NAG O 2 . ? -10.339 -0.826 21.892 1.00 28.23 ? 800 NAG A C3 1 HETATM 3378 C C4 . NAG O 2 . ? -10.499 -0.381 23.345 1.00 28.27 ? 800 NAG A C4 1 HETATM 3379 C C5 . NAG O 2 . ? -9.568 0.753 23.742 1.00 25.53 ? 800 NAG A C5 1 HETATM 3380 C C6 . NAG O 2 . ? -9.609 0.868 25.261 1.00 24.18 ? 800 NAG A C6 1 HETATM 3381 C C7 . NAG O 2 . ? -8.222 -2.253 19.515 1.00 30.44 ? 800 NAG A C7 1 HETATM 3382 C C8 . NAG O 2 . ? -8.091 -2.316 18.014 1.00 30.83 ? 800 NAG A C8 1 HETATM 3383 N N2 . NAG O 2 . ? -8.794 -1.165 20.045 1.00 28.19 ? 800 NAG A N2 1 HETATM 3384 O O3 . NAG O 2 . ? -10.923 -2.100 21.699 1.00 27.92 ? 800 NAG A O3 1 HETATM 3385 O O4 . NAG O 2 . ? -11.798 0.086 23.615 1.00 33.42 ? 800 NAG A O4 1 HETATM 3386 O O5 . NAG O 2 . ? -8.272 0.415 23.355 1.00 24.58 ? 800 NAG A O5 1 HETATM 3387 O O6 . NAG O 2 . ? -9.135 -0.365 25.763 1.00 21.05 ? 800 NAG A O6 1 HETATM 3388 O O7 . NAG O 2 . ? -7.804 -3.193 20.188 1.00 32.53 ? 800 NAG A O7 1 HETATM 3389 C C1 . NAG P 2 . ? -12.519 -0.894 24.384 1.00 37.06 ? 801 NAG A C1 1 HETATM 3390 C C2 . NAG P 2 . ? -13.735 -0.231 25.008 1.00 37.49 ? 801 NAG A C2 1 HETATM 3391 C C3 . NAG P 2 . ? -14.617 -1.249 25.722 1.00 39.96 ? 801 NAG A C3 1 HETATM 3392 C C4 . NAG P 2 . ? -14.842 -2.515 24.897 1.00 41.24 ? 801 NAG A C4 1 HETATM 3393 C C5 . NAG P 2 . ? -13.576 -3.009 24.215 1.00 41.03 ? 801 NAG A C5 1 HETATM 3394 C C6 . NAG P 2 . ? -13.977 -3.967 23.117 1.00 42.81 ? 801 NAG A C6 1 HETATM 3395 C C7 . NAG P 2 . ? -13.325 2.066 25.688 1.00 37.24 ? 801 NAG A C7 1 HETATM 3396 C C8 . NAG P 2 . ? -12.919 2.995 26.797 1.00 36.83 ? 801 NAG A C8 1 HETATM 3397 N N2 . NAG P 2 . ? -13.316 0.766 25.974 1.00 37.62 ? 801 NAG A N2 1 HETATM 3398 O O3 . NAG P 2 . ? -15.854 -0.641 26.019 1.00 37.09 ? 801 NAG A O3 1 HETATM 3399 O O4 . NAG P 2 . ? -15.290 -3.545 25.750 1.00 44.54 ? 801 NAG A O4 1 HETATM 3400 O O5 . NAG P 2 . ? -12.914 -1.958 23.560 1.00 38.62 ? 801 NAG A O5 1 HETATM 3401 O O6 . NAG P 2 . ? -14.841 -3.230 22.279 1.00 43.98 ? 801 NAG A O6 1 HETATM 3402 O O7 . NAG P 2 . ? -13.644 2.502 24.583 1.00 36.04 ? 801 NAG A O7 1 HETATM 3403 C C1 . GAL Q 5 . ? 3.577 16.176 2.711 1.00 23.95 ? 901 GAL A C1 1 HETATM 3404 C C2 . GAL Q 5 . ? 4.163 16.453 4.200 1.00 22.82 ? 901 GAL A C2 1 HETATM 3405 C C3 . GAL Q 5 . ? 3.585 17.615 4.734 1.00 22.42 ? 901 GAL A C3 1 HETATM 3406 C C4 . GAL Q 5 . ? 3.669 18.862 3.803 1.00 23.88 ? 901 GAL A C4 1 HETATM 3407 C C5 . GAL Q 5 . ? 3.412 18.546 2.353 1.00 22.74 ? 901 GAL A C5 1 HETATM 3408 C C6 . GAL Q 5 . ? 3.731 19.615 1.331 1.00 20.32 ? 901 GAL A C6 1 HETATM 3409 O O1 . GAL Q 5 . ? 4.166 15.025 2.113 1.00 25.62 ? 901 GAL A O1 1 HETATM 3410 O O2 . GAL Q 5 . ? 3.965 15.268 5.008 1.00 23.73 ? 901 GAL A O2 1 HETATM 3411 O O3 . GAL Q 5 . ? 4.298 18.012 6.010 1.00 20.28 ? 901 GAL A O3 1 HETATM 3412 O O4 . GAL Q 5 . ? 5.099 19.122 3.708 1.00 24.11 ? 901 GAL A O4 1 HETATM 3413 O O5 . GAL Q 5 . ? 3.837 17.297 1.881 1.00 23.07 ? 901 GAL A O5 1 HETATM 3414 O O6 . GAL Q 5 . ? 3.060 19.332 0.109 1.00 21.31 ? 901 GAL A O6 1 HETATM 3415 O O . HOH R 6 . ? 13.863 19.321 12.783 1.00 17.05 ? 902 HOH A O 1 HETATM 3416 O O . HOH R 6 . ? 17.230 15.324 22.728 1.00 14.10 ? 903 HOH A O 1 HETATM 3417 O O . HOH R 6 . ? 5.258 12.535 11.627 1.00 11.15 ? 904 HOH A O 1 HETATM 3418 O O . HOH R 6 . ? 0.642 3.757 22.787 1.00 17.19 ? 905 HOH A O 1 HETATM 3419 O O . HOH R 6 . ? 9.900 12.383 19.012 1.00 20.43 ? 906 HOH A O 1 HETATM 3420 O O . HOH R 6 . ? 0.212 25.300 15.244 1.00 15.67 ? 907 HOH A O 1 HETATM 3421 O O . HOH R 6 . ? 20.040 25.320 11.146 1.00 18.66 ? 908 HOH A O 1 HETATM 3422 O O . HOH R 6 . ? 6.307 20.094 15.499 1.00 14.44 ? 909 HOH A O 1 HETATM 3423 O O . HOH R 6 . ? 17.547 17.076 16.050 1.00 12.54 ? 910 HOH A O 1 HETATM 3424 O O . HOH R 6 . ? 17.645 13.240 -2.851 1.00 17.55 ? 911 HOH A O 1 HETATM 3425 O O . HOH R 6 . ? 9.955 22.722 8.260 1.00 14.88 ? 912 HOH A O 1 HETATM 3426 O O . HOH R 6 . ? 6.058 1.210 4.679 1.00 18.06 ? 913 HOH A O 1 HETATM 3427 O O . HOH R 6 . ? 2.972 23.870 9.552 1.00 15.81 ? 914 HOH A O 1 HETATM 3428 O O . HOH R 6 . ? -2.815 1.342 24.171 1.00 23.98 ? 915 HOH A O 1 HETATM 3429 O O . HOH R 6 . ? 6.445 18.177 8.689 1.00 15.24 ? 916 HOH A O 1 HETATM 3430 O O . HOH R 6 . ? 15.196 18.429 15.481 1.00 21.89 ? 917 HOH A O 1 HETATM 3431 O O . HOH R 6 . ? 11.912 15.967 10.281 1.00 17.50 ? 918 HOH A O 1 HETATM 3432 O O . HOH R 6 . ? 15.649 25.684 17.132 1.00 15.56 ? 919 HOH A O 1 HETATM 3433 O O . HOH R 6 . ? 22.357 16.180 7.108 1.00 19.16 ? 920 HOH A O 1 HETATM 3434 O O . HOH R 6 . ? -9.012 8.972 23.053 1.00 17.17 ? 921 HOH A O 1 HETATM 3435 O O . HOH R 6 . ? 14.959 16.224 29.136 1.00 18.66 ? 922 HOH A O 1 HETATM 3436 O O . HOH R 6 . ? 7.634 19.278 13.002 1.00 15.46 ? 923 HOH A O 1 HETATM 3437 O O . HOH R 6 . ? 21.751 21.740 -12.643 1.00 21.10 ? 924 HOH A O 1 HETATM 3438 O O . HOH R 6 . ? -5.319 5.359 26.602 1.00 16.45 ? 925 HOH A O 1 HETATM 3439 O O . HOH R 6 . ? -7.015 12.397 12.138 1.00 21.90 ? 926 HOH A O 1 HETATM 3440 O O . HOH R 6 . ? 21.283 17.612 9.217 1.00 16.60 ? 927 HOH A O 1 HETATM 3441 O O . HOH R 6 . ? 1.311 15.700 0.391 1.00 19.03 ? 928 HOH A O 1 HETATM 3442 O O . HOH R 6 . ? 18.388 24.632 -7.596 1.00 21.64 ? 929 HOH A O 1 HETATM 3443 O O . HOH R 6 . ? 13.174 5.015 -2.249 1.00 19.06 ? 930 HOH A O 1 HETATM 3444 O O . HOH R 6 . ? 8.480 18.826 10.528 1.00 16.91 ? 931 HOH A O 1 HETATM 3445 O O . HOH R 6 . ? -1.754 5.461 38.370 1.00 22.32 ? 932 HOH A O 1 HETATM 3446 O O . HOH R 6 . ? 12.390 22.571 -3.586 1.00 28.13 ? 933 HOH A O 1 HETATM 3447 O O . HOH R 6 . ? -3.173 21.229 9.304 1.00 23.51 ? 934 HOH A O 1 HETATM 3448 O O . HOH R 6 . ? 9.093 2.518 8.644 1.00 22.33 ? 935 HOH A O 1 HETATM 3449 O O . HOH R 6 . ? 11.618 2.350 20.115 1.00 24.08 ? 936 HOH A O 1 HETATM 3450 O O . HOH R 6 . ? -1.346 4.997 15.779 1.00 21.25 ? 937 HOH A O 1 HETATM 3451 O O . HOH R 6 . ? 3.683 26.115 2.355 1.00 18.97 ? 938 HOH A O 1 HETATM 3452 O O . HOH R 6 . ? -11.350 17.860 25.100 1.00 23.68 ? 939 HOH A O 1 HETATM 3453 O O . HOH R 6 . ? 10.912 23.886 5.704 1.00 22.92 ? 940 HOH A O 1 HETATM 3454 O O . HOH R 6 . ? 10.184 5.982 1.401 1.00 22.93 ? 941 HOH A O 1 HETATM 3455 O O . HOH R 6 . ? 16.835 17.408 24.604 1.00 18.45 ? 942 HOH A O 1 HETATM 3456 O O . HOH R 6 . ? 21.753 11.831 27.117 1.00 30.92 ? 943 HOH A O 1 HETATM 3457 O O . HOH R 6 . ? 16.492 24.844 19.446 1.00 26.19 ? 944 HOH A O 1 HETATM 3458 O O . HOH R 6 . ? 2.031 -5.903 6.563 1.00 33.56 ? 945 HOH A O 1 HETATM 3459 O O . HOH R 6 . ? -0.345 25.104 45.299 1.00 22.39 ? 946 HOH A O 1 HETATM 3460 O O . HOH R 6 . ? 10.550 19.990 9.181 1.00 16.35 ? 947 HOH A O 1 HETATM 3461 O O . HOH R 6 . ? 19.204 10.295 17.777 1.00 25.54 ? 948 HOH A O 1 HETATM 3462 O O . HOH R 6 . ? -0.871 -0.235 31.346 1.00 16.95 ? 949 HOH A O 1 HETATM 3463 O O . HOH R 6 . ? -7.776 5.846 29.556 1.00 26.17 ? 950 HOH A O 1 HETATM 3464 O O . HOH R 6 . ? 24.557 17.281 5.915 1.00 19.88 ? 951 HOH A O 1 HETATM 3465 O O . HOH R 6 . ? 4.844 5.355 11.718 1.00 25.05 ? 952 HOH A O 1 HETATM 3466 O O . HOH R 6 . ? 26.723 22.801 11.655 1.00 31.61 ? 953 HOH A O 1 HETATM 3467 O O . HOH R 6 . ? -13.837 16.459 31.165 1.00 29.31 ? 954 HOH A O 1 HETATM 3468 O O . HOH R 6 . ? 9.823 1.635 1.539 1.00 27.26 ? 955 HOH A O 1 HETATM 3469 O O . HOH R 6 . ? 11.476 26.325 -10.264 1.00 26.70 ? 956 HOH A O 1 HETATM 3470 O O . HOH R 6 . ? 2.258 17.389 7.649 1.00 23.54 ? 957 HOH A O 1 HETATM 3471 O O . HOH R 6 . ? 7.159 7.818 -1.560 1.00 25.88 ? 958 HOH A O 1 HETATM 3472 O O . HOH R 6 . ? 20.733 27.457 -18.422 1.00 42.68 ? 959 HOH A O 1 HETATM 3473 O O . HOH R 6 . ? 18.458 6.651 13.498 1.00 26.86 ? 960 HOH A O 1 HETATM 3474 O O . HOH R 6 . ? 17.637 22.567 14.433 1.00 24.66 ? 961 HOH A O 1 HETATM 3475 O O . HOH R 6 . ? 11.208 37.684 -1.382 1.00 23.73 ? 962 HOH A O 1 HETATM 3476 O O . HOH R 6 . ? -5.887 9.768 12.071 1.00 24.98 ? 963 HOH A O 1 HETATM 3477 O O . HOH R 6 . ? -3.555 2.268 27.327 1.00 20.37 ? 964 HOH A O 1 HETATM 3478 O O . HOH R 6 . ? 9.066 -0.132 17.592 1.00 24.00 ? 965 HOH A O 1 HETATM 3479 O O . HOH R 6 . ? -2.966 -0.797 33.179 1.00 21.89 ? 966 HOH A O 1 HETATM 3480 O O . HOH R 6 . ? -0.261 18.784 8.185 1.00 20.53 ? 967 HOH A O 1 HETATM 3481 O O . HOH R 6 . ? -6.144 30.086 16.035 1.00 26.46 ? 968 HOH A O 1 HETATM 3482 O O . HOH R 6 . ? -4.112 6.830 37.834 1.00 25.26 ? 969 HOH A O 1 HETATM 3483 O O . HOH R 6 . ? 10.714 3.467 39.857 1.00 27.52 ? 970 HOH A O 1 HETATM 3484 O O . HOH R 6 . ? 14.397 12.434 29.398 1.00 32.31 ? 971 HOH A O 1 HETATM 3485 O O . HOH R 6 . ? 16.104 24.126 -16.358 1.00 30.29 ? 972 HOH A O 1 HETATM 3486 O O . HOH R 6 . ? 24.706 19.932 6.072 1.00 25.63 ? 973 HOH A O 1 HETATM 3487 O O . HOH R 6 . ? 10.363 23.292 -5.065 1.00 18.79 ? 974 HOH A O 1 HETATM 3488 O O . HOH R 6 . ? -10.573 16.932 17.805 1.00 22.18 ? 975 HOH A O 1 HETATM 3489 O O . HOH R 6 . ? -1.252 4.264 12.690 1.00 26.27 ? 976 HOH A O 1 HETATM 3490 O O . HOH R 6 . ? -5.949 6.624 34.900 1.00 22.33 ? 977 HOH A O 1 HETATM 3491 O O . HOH R 6 . ? -4.621 21.106 32.242 1.00 35.57 ? 978 HOH A O 1 HETATM 3492 O O . HOH R 6 . ? 29.635 15.455 1.563 1.00 23.11 ? 979 HOH A O 1 HETATM 3493 O O . HOH R 6 . ? -3.931 30.736 14.425 1.00 27.25 ? 980 HOH A O 1 HETATM 3494 O O . HOH R 6 . ? 1.755 6.605 37.960 1.00 26.99 ? 981 HOH A O 1 HETATM 3495 O O . HOH R 6 . ? 14.215 15.794 -9.592 1.00 26.77 ? 982 HOH A O 1 HETATM 3496 O O . HOH R 6 . ? 8.673 1.554 4.003 1.00 20.00 ? 983 HOH A O 1 HETATM 3497 O O . HOH R 6 . ? 22.883 28.159 9.049 1.00 28.23 ? 984 HOH A O 1 HETATM 3498 O O . HOH R 6 . ? 17.977 16.008 -15.991 1.00 24.80 ? 985 HOH A O 1 HETATM 3499 O O . HOH R 6 . ? -1.108 19.567 35.688 1.00 24.47 ? 986 HOH A O 1 HETATM 3500 O O . HOH R 6 . ? 11.262 21.764 32.687 1.00 31.88 ? 987 HOH A O 1 HETATM 3501 O O . HOH R 6 . ? 2.698 28.179 -7.401 1.00 38.71 ? 988 HOH A O 1 HETATM 3502 O O . HOH R 6 . ? -6.080 30.624 18.714 1.00 32.12 ? 989 HOH A O 1 HETATM 3503 O O . HOH R 6 . ? 23.148 18.503 -8.963 1.00 27.56 ? 990 HOH A O 1 HETATM 3504 O O . HOH R 6 . ? 21.471 7.475 4.370 1.00 21.24 ? 991 HOH A O 1 HETATM 3505 O O . HOH R 6 . ? -3.961 29.981 41.482 1.00 30.53 ? 992 HOH A O 1 HETATM 3506 O O . HOH R 6 . ? -0.793 17.920 5.241 1.00 27.08 ? 993 HOH A O 1 HETATM 3507 O O . HOH R 6 . ? -11.970 9.730 24.131 1.00 24.83 ? 994 HOH A O 1 HETATM 3508 O O . HOH R 6 . ? -8.789 9.465 19.014 1.00 30.84 ? 995 HOH A O 1 HETATM 3509 O O . HOH R 6 . ? -11.801 24.081 24.368 1.00 28.58 ? 996 HOH A O 1 HETATM 3510 O O . HOH R 6 . ? 12.772 3.283 17.498 1.00 27.03 ? 997 HOH A O 1 HETATM 3511 O O . HOH R 6 . ? 9.403 6.693 31.961 1.00 26.04 ? 998 HOH A O 1 HETATM 3512 O O . HOH R 6 . ? 5.807 29.330 31.061 1.00 25.46 ? 999 HOH A O 1 HETATM 3513 O O . HOH R 6 . ? 7.770 1.416 29.927 1.00 24.07 ? 1000 HOH A O 1 HETATM 3514 O O . HOH R 6 . ? 15.703 -0.623 -1.557 1.00 34.05 ? 1001 HOH A O 1 HETATM 3515 O O . HOH R 6 . ? 18.194 7.400 16.145 1.00 26.41 ? 1002 HOH A O 1 HETATM 3516 O O . HOH R 6 . ? -5.727 -2.405 22.136 1.00 26.63 ? 1003 HOH A O 1 HETATM 3517 O O . HOH R 6 . ? 8.113 24.241 -3.467 1.00 25.21 ? 1004 HOH A O 1 HETATM 3518 O O . HOH R 6 . ? 18.414 32.428 15.570 1.00 28.61 ? 1005 HOH A O 1 HETATM 3519 O O . HOH R 6 . ? 5.076 29.099 -6.039 1.00 36.26 ? 1006 HOH A O 1 HETATM 3520 O O . HOH R 6 . ? 4.863 2.865 15.811 1.00 32.66 ? 1007 HOH A O 1 HETATM 3521 O O . HOH R 6 . ? -6.836 8.087 15.553 1.00 38.05 ? 1008 HOH A O 1 HETATM 3522 O O . HOH R 6 . ? -7.546 18.666 33.377 1.00 24.09 ? 1009 HOH A O 1 HETATM 3523 O O . HOH R 6 . ? -2.982 16.904 6.887 1.00 28.65 ? 1010 HOH A O 1 HETATM 3524 O O . HOH R 6 . ? -5.944 4.406 32.825 1.00 28.53 ? 1011 HOH A O 1 HETATM 3525 O O . HOH R 6 . ? 1.264 14.561 -4.010 1.00 30.34 ? 1012 HOH A O 1 HETATM 3526 O O . HOH R 6 . ? 4.025 10.810 -4.266 1.00 31.99 ? 1013 HOH A O 1 HETATM 3527 O O . HOH R 6 . ? -2.503 19.777 6.783 1.00 34.02 ? 1014 HOH A O 1 HETATM 3528 O O . HOH R 6 . ? 4.545 1.765 2.315 1.00 26.25 ? 1015 HOH A O 1 HETATM 3529 O O . HOH R 6 . ? -11.088 21.465 26.684 1.00 26.52 ? 1016 HOH A O 1 HETATM 3530 O O . HOH R 6 . ? -7.581 8.267 31.397 1.00 22.12 ? 1017 HOH A O 1 HETATM 3531 O O . HOH R 6 . ? -11.838 18.761 28.124 1.00 33.11 ? 1018 HOH A O 1 HETATM 3532 O O . HOH R 6 . ? -13.399 2.297 21.881 1.00 33.01 ? 1019 HOH A O 1 HETATM 3533 O O . HOH R 6 . ? 2.010 27.716 29.407 1.00 34.68 ? 1020 HOH A O 1 HETATM 3534 O O . HOH R 6 . ? 11.012 37.089 21.003 1.00 29.14 ? 1021 HOH A O 1 HETATM 3535 O O . HOH R 6 . ? 0.949 18.309 -0.506 1.00 26.57 ? 1022 HOH A O 1 HETATM 3536 O O . HOH R 6 . ? 23.599 29.871 -6.174 1.00 35.47 ? 1023 HOH A O 1 HETATM 3537 O O . HOH R 6 . ? 25.207 13.896 -3.007 1.00 22.30 ? 1024 HOH A O 1 HETATM 3538 O O . HOH R 6 . ? 8.973 -8.176 36.584 1.00 38.59 ? 1025 HOH A O 1 HETATM 3539 O O . HOH R 6 . ? 12.434 27.461 28.730 1.00 27.02 ? 1026 HOH A O 1 HETATM 3540 O O . HOH R 6 . ? 22.552 8.479 -4.974 1.00 30.32 ? 1027 HOH A O 1 HETATM 3541 O O . HOH R 6 . ? 11.659 18.385 -10.584 1.00 31.58 ? 1028 HOH A O 1 HETATM 3542 O O . HOH R 6 . ? -8.081 24.614 18.108 1.00 26.17 ? 1029 HOH A O 1 HETATM 3543 O O . HOH R 6 . ? -2.698 0.113 9.392 1.00 34.22 ? 1030 HOH A O 1 HETATM 3544 O O . HOH R 6 . ? 27.017 28.113 8.445 1.00 36.93 ? 1031 HOH A O 1 HETATM 3545 O O . HOH R 6 . ? -4.624 26.483 4.728 1.00 34.11 ? 1032 HOH A O 1 HETATM 3546 O O . HOH R 6 . ? 20.783 39.844 7.479 1.00 42.06 ? 1033 HOH A O 1 HETATM 3547 O O . HOH R 6 . ? 23.887 23.893 -12.912 1.00 32.33 ? 1034 HOH A O 1 HETATM 3548 O O . HOH R 6 . ? 27.133 21.859 -5.431 1.00 31.29 ? 1035 HOH A O 1 HETATM 3549 O O . HOH R 6 . ? 16.121 27.096 22.775 1.00 27.25 ? 1036 HOH A O 1 HETATM 3550 O O . HOH R 6 . ? 13.122 20.218 32.053 1.00 33.45 ? 1037 HOH A O 1 HETATM 3551 O O . HOH R 6 . ? 29.262 18.459 16.207 1.00 41.38 ? 1038 HOH A O 1 HETATM 3552 O O . HOH R 6 . ? 24.815 22.696 4.361 1.00 33.12 ? 1039 HOH A O 1 HETATM 3553 O O . HOH R 6 . ? 24.954 18.694 25.145 1.00 41.68 ? 1040 HOH A O 1 HETATM 3554 O O . HOH R 6 . ? 9.034 27.906 38.155 1.00 45.10 ? 1041 HOH A O 1 HETATM 3555 O O . HOH R 6 . ? -3.573 24.961 -0.333 1.00 26.16 ? 1042 HOH A O 1 HETATM 3556 O O . HOH R 6 . ? 1.154 -5.836 24.879 1.00 33.46 ? 1043 HOH A O 1 HETATM 3557 O O . HOH R 6 . ? 6.591 -12.487 0.539 1.00 49.54 ? 1044 HOH A O 1 HETATM 3558 O O . HOH R 6 . ? 16.699 33.191 -3.936 1.00 33.51 ? 1045 HOH A O 1 HETATM 3559 O O . HOH R 6 . ? 0.684 9.219 48.131 1.00 39.64 ? 1046 HOH A O 1 HETATM 3560 O O . HOH R 6 . ? 2.699 2.670 44.830 1.00 38.94 ? 1047 HOH A O 1 HETATM 3561 O O . HOH R 6 . ? 22.414 27.035 16.776 1.00 45.93 ? 1048 HOH A O 1 HETATM 3562 O O . HOH R 6 . ? -0.421 19.842 46.284 1.00 29.87 ? 1049 HOH A O 1 HETATM 3563 O O . HOH R 6 . ? 3.644 30.552 29.071 1.00 31.33 ? 1050 HOH A O 1 HETATM 3564 O O . HOH R 6 . ? 18.150 22.564 17.514 1.00 39.29 ? 1051 HOH A O 1 HETATM 3565 O O . HOH R 6 . ? -3.641 -3.937 20.298 1.00 27.05 ? 1052 HOH A O 1 HETATM 3566 O O . HOH R 6 . ? 4.692 -0.086 16.612 1.00 37.80 ? 1053 HOH A O 1 HETATM 3567 O O . HOH R 6 . ? 14.160 26.192 26.810 1.00 28.25 ? 1054 HOH A O 1 HETATM 3568 O O . HOH R 6 . ? 10.003 3.784 -1.944 1.00 32.11 ? 1055 HOH A O 1 HETATM 3569 O O . HOH R 6 . ? 14.254 18.789 -11.366 1.00 31.78 ? 1056 HOH A O 1 HETATM 3570 O O . HOH R 6 . ? -13.871 7.364 26.138 1.00 38.91 ? 1057 HOH A O 1 HETATM 3571 O O . HOH R 6 . ? 6.889 20.718 -10.863 1.00 36.22 ? 1058 HOH A O 1 HETATM 3572 O O . HOH R 6 . ? -5.724 24.695 19.248 1.00 23.93 ? 1059 HOH A O 1 HETATM 3573 O O . HOH R 6 . ? 11.657 23.893 34.125 1.00 35.38 ? 1060 HOH A O 1 HETATM 3574 O O . HOH R 6 . ? -0.168 24.491 -6.978 1.00 27.38 ? 1061 HOH A O 1 HETATM 3575 O O . HOH R 6 . ? 28.841 13.400 26.309 1.00 37.23 ? 1062 HOH A O 1 HETATM 3576 O O . HOH R 6 . ? -7.759 29.636 22.657 1.00 34.00 ? 1063 HOH A O 1 HETATM 3577 O O . HOH R 6 . ? 9.779 4.449 30.635 1.00 32.02 ? 1064 HOH A O 1 HETATM 3578 O O . HOH R 6 . ? 16.234 28.021 20.006 1.00 36.50 ? 1065 HOH A O 1 HETATM 3579 O O . HOH R 6 . ? 23.621 8.274 -1.057 1.00 36.05 ? 1066 HOH A O 1 HETATM 3580 O O . HOH R 6 . ? 28.363 11.032 3.780 1.00 44.03 ? 1067 HOH A O 1 HETATM 3581 O O . HOH R 6 . ? 27.010 17.761 29.126 1.00 49.82 ? 1068 HOH A O 1 HETATM 3582 O O . HOH R 6 . ? 23.899 15.284 -6.244 1.00 33.71 ? 1069 HOH A O 1 HETATM 3583 O O . HOH R 6 . ? 9.474 30.475 27.843 1.00 32.36 ? 1070 HOH A O 1 HETATM 3584 O O . HOH R 6 . ? -10.881 9.432 20.971 1.00 47.94 ? 1071 HOH A O 1 HETATM 3585 O O . HOH R 6 . ? 17.863 -1.585 9.249 1.00 30.35 ? 1072 HOH A O 1 HETATM 3586 O O . HOH R 6 . ? 27.629 18.646 7.719 1.00 39.68 ? 1073 HOH A O 1 HETATM 3587 O O . HOH R 6 . ? 15.946 14.570 36.358 1.00 46.20 ? 1074 HOH A O 1 HETATM 3588 O O . HOH R 6 . ? 14.007 -1.556 0.878 1.00 33.81 ? 1075 HOH A O 1 HETATM 3589 O O . HOH R 6 . ? 23.583 6.046 6.307 1.00 51.61 ? 1076 HOH A O 1 HETATM 3590 O O . HOH R 6 . ? 12.699 4.195 25.314 1.00 31.01 ? 1077 HOH A O 1 HETATM 3591 O O . HOH R 6 . ? 7.168 -1.636 17.198 1.00 36.45 ? 1078 HOH A O 1 HETATM 3592 O O . HOH R 6 . ? 13.565 -6.123 8.657 1.00 40.15 ? 1079 HOH A O 1 HETATM 3593 O O . HOH R 6 . ? 4.694 -4.132 32.144 1.00 30.25 ? 1080 HOH A O 1 HETATM 3594 O O . HOH R 6 . ? 8.285 10.274 -10.135 1.00 30.26 ? 1081 HOH A O 1 HETATM 3595 O O . HOH R 6 . ? 16.988 23.005 28.860 1.00 32.58 ? 1082 HOH A O 1 HETATM 3596 O O . HOH R 6 . ? -6.767 -0.195 33.178 1.00 32.65 ? 1083 HOH A O 1 HETATM 3597 O O . HOH R 6 . ? 28.910 11.058 15.932 1.00 47.70 ? 1084 HOH A O 1 HETATM 3598 O O . HOH R 6 . ? 1.721 13.702 49.488 1.00 42.38 ? 1085 HOH A O 1 HETATM 3599 O O . HOH R 6 . ? 26.147 11.308 -2.522 1.00 35.54 ? 1086 HOH A O 1 HETATM 3600 O O . HOH R 6 . ? 18.851 26.782 15.809 1.00 34.36 ? 1087 HOH A O 1 HETATM 3601 O O . HOH R 6 . ? 27.261 19.608 -2.677 1.00 37.71 ? 1088 HOH A O 1 HETATM 3602 O O . HOH R 6 . ? 15.630 20.885 31.665 1.00 29.11 ? 1089 HOH A O 1 HETATM 3603 O O . HOH R 6 . ? 1.975 34.457 8.768 1.00 31.35 ? 1090 HOH A O 1 HETATM 3604 O O . HOH R 6 . ? 23.736 26.035 -7.623 1.00 34.01 ? 1091 HOH A O 1 HETATM 3605 O O . HOH R 6 . ? -17.585 -3.999 26.399 1.00 48.01 ? 1092 HOH A O 1 HETATM 3606 O O . HOH R 6 . ? 9.778 27.728 -14.555 1.00 39.23 ? 1093 HOH A O 1 HETATM 3607 O O . HOH R 6 . ? -4.019 20.134 35.012 1.00 49.82 ? 1094 HOH A O 1 HETATM 3608 O O . HOH R 6 . ? -2.367 20.551 39.461 1.00 37.04 ? 1095 HOH A O 1 HETATM 3609 O O . HOH R 6 . ? -5.852 0.458 17.251 1.00 38.22 ? 1096 HOH A O 1 HETATM 3610 O O . HOH R 6 . ? 5.802 5.698 45.315 1.00 40.28 ? 1097 HOH A O 1 HETATM 3611 O O . HOH R 6 . ? 5.919 7.750 47.193 1.00 38.74 ? 1098 HOH A O 1 HETATM 3612 O O . HOH R 6 . ? -3.556 3.574 9.248 1.00 31.43 ? 1099 HOH A O 1 HETATM 3613 O O . HOH R 6 . ? 3.910 7.396 44.933 1.00 28.00 ? 1100 HOH A O 1 HETATM 3614 O O . HOH R 6 . ? 30.597 14.075 16.438 1.00 46.67 ? 1101 HOH A O 1 HETATM 3615 O O . HOH R 6 . ? 2.192 30.408 39.286 1.00 26.42 ? 1102 HOH A O 1 HETATM 3616 O O . HOH R 6 . ? 24.438 27.681 -13.070 1.00 44.43 ? 1103 HOH A O 1 HETATM 3617 O O . HOH R 6 . ? 16.186 -3.233 27.088 1.00 34.15 ? 1104 HOH A O 1 HETATM 3618 O O . HOH R 6 . ? 17.600 30.006 -8.896 1.00 36.13 ? 1105 HOH A O 1 HETATM 3619 O O . HOH R 6 . ? 9.333 35.040 25.853 1.00 38.97 ? 1106 HOH A O 1 HETATM 3620 O O . HOH R 6 . ? 21.226 22.510 20.235 1.00 34.55 ? 1107 HOH A O 1 HETATM 3621 O O . HOH R 6 . ? 22.212 2.867 10.354 1.00 40.76 ? 1108 HOH A O 1 HETATM 3622 O O . HOH R 6 . ? 15.010 10.459 42.710 1.00 39.66 ? 1109 HOH A O 1 HETATM 3623 O O . HOH R 6 . ? 12.970 8.554 29.381 1.00 29.85 ? 1110 HOH A O 1 HETATM 3624 O O . HOH R 6 . ? 24.922 9.841 14.220 1.00 50.01 ? 1111 HOH A O 1 HETATM 3625 O O . HOH R 6 . ? 10.454 24.115 41.573 1.00 54.79 ? 1112 HOH A O 1 HETATM 3626 O O . HOH R 6 . ? -13.023 24.906 17.038 1.00 42.01 ? 1113 HOH A O 1 HETATM 3627 O O . HOH R 6 . ? 32.528 24.092 -0.209 1.00 42.68 ? 1114 HOH A O 1 HETATM 3628 O O . HOH R 6 . ? 2.084 33.423 11.363 1.00 29.98 ? 1115 HOH A O 1 HETATM 3629 O O . HOH R 6 . ? 20.256 34.236 12.851 1.00 40.81 ? 1116 HOH A O 1 HETATM 3630 O O . HOH R 6 . ? 27.783 28.378 1.164 1.00 40.90 ? 1117 HOH A O 1 HETATM 3631 O O . HOH R 6 . ? 3.821 -1.984 14.457 1.00 37.86 ? 1118 HOH A O 1 HETATM 3632 O O . HOH R 6 . ? 0.530 36.877 10.197 1.00 44.09 ? 1119 HOH A O 1 HETATM 3633 O O . HOH R 6 . ? 3.516 -5.270 0.773 1.00 35.48 ? 1120 HOH A O 1 HETATM 3634 O O . HOH R 6 . ? 3.596 19.566 50.813 1.00 43.58 ? 1121 HOH A O 1 HETATM 3635 O O . HOH R 6 . ? 0.462 33.083 -2.839 1.00 44.15 ? 1122 HOH A O 1 HETATM 3636 O O . HOH R 6 . ? 22.080 31.781 9.300 1.00 39.27 ? 1123 HOH A O 1 HETATM 3637 O O . HOH R 6 . ? -3.683 29.447 10.648 1.00 33.88 ? 1124 HOH A O 1 HETATM 3638 O O . HOH R 6 . ? -5.387 -5.040 18.748 1.00 39.64 ? 1125 HOH A O 1 HETATM 3639 O O . HOH R 6 . ? -4.595 29.702 8.272 1.00 39.79 ? 1126 HOH A O 1 HETATM 3640 O O . HOH R 6 . ? 15.336 40.267 16.897 1.00 37.90 ? 1127 HOH A O 1 HETATM 3641 O O . HOH R 6 . ? -15.822 8.779 27.434 1.00 50.24 ? 1128 HOH A O 1 HETATM 3642 O O . HOH R 6 . ? 29.020 26.525 -0.915 1.00 46.09 ? 1129 HOH A O 1 HETATM 3643 O O . HOH R 6 . ? 26.760 16.062 7.287 1.00 34.18 ? 1130 HOH A O 1 HETATM 3644 O O . HOH R 6 . ? 20.264 10.443 -5.818 1.00 36.58 ? 1131 HOH A O 1 HETATM 3645 O O . HOH R 6 . ? 17.990 -2.999 -0.580 1.00 41.76 ? 1132 HOH A O 1 HETATM 3646 O O . HOH R 6 . ? 21.257 36.212 4.933 1.00 43.56 ? 1133 HOH A O 1 HETATM 3647 O O . HOH R 6 . ? 14.062 27.071 24.516 1.00 41.69 ? 1134 HOH A O 1 HETATM 3648 O O . HOH R 6 . ? 1.827 -5.864 28.206 1.00 32.62 ? 1135 HOH A O 1 HETATM 3649 O O . HOH R 6 . ? 26.626 9.840 8.135 1.00 35.57 ? 1136 HOH A O 1 HETATM 3650 O O . HOH R 6 . ? 22.667 12.686 30.370 1.00 31.22 ? 1137 HOH A O 1 HETATM 3651 O O . HOH R 6 . ? -7.597 34.247 18.645 1.00 48.82 ? 1138 HOH A O 1 HETATM 3652 O O . HOH R 6 . ? -0.688 14.454 2.812 1.00 48.94 ? 1139 HOH A O 1 HETATM 3653 O O . HOH R 6 . ? 6.556 3.850 10.881 1.00 43.64 ? 1140 HOH A O 1 HETATM 3654 O O . HOH R 6 . ? 22.150 28.725 -14.700 1.00 36.71 ? 1141 HOH A O 1 HETATM 3655 O O . HOH R 6 . ? -8.862 24.543 29.619 1.00 40.67 ? 1142 HOH A O 1 HETATM 3656 O O . HOH R 6 . ? -5.870 25.799 23.524 1.00 36.53 ? 1143 HOH A O 1 HETATM 3657 O O . HOH R 6 . ? -3.031 1.609 35.002 1.00 35.14 ? 1144 HOH A O 1 HETATM 3658 O O . HOH R 6 . ? 11.367 8.138 33.875 1.00 32.74 ? 1145 HOH A O 1 HETATM 3659 O O . HOH R 6 . ? -0.329 34.144 0.138 1.00 47.79 ? 1146 HOH A O 1 HETATM 3660 O O . HOH R 6 . ? 27.505 10.724 11.129 1.00 39.23 ? 1147 HOH A O 1 HETATM 3661 O O . HOH R 6 . ? 20.581 10.179 -8.579 1.00 40.61 ? 1148 HOH A O 1 HETATM 3662 O O . HOH R 6 . ? 15.508 8.373 29.449 1.00 45.83 ? 1149 HOH A O 1 HETATM 3663 O O . HOH R 6 . ? -1.802 35.065 31.056 1.00 37.66 ? 1150 HOH A O 1 HETATM 3664 O O . HOH R 6 . ? 6.734 -6.014 31.870 1.00 51.55 ? 1151 HOH A O 1 HETATM 3665 O O . HOH R 6 . ? 0.089 16.908 50.288 1.00 51.58 ? 1152 HOH A O 1 HETATM 3666 O O . HOH R 6 . ? 21.409 29.932 16.756 1.00 49.03 ? 1153 HOH A O 1 HETATM 3667 O O . HOH R 6 . ? 11.688 29.026 26.624 1.00 36.24 ? 1154 HOH A O 1 HETATM 3668 O O . HOH R 6 . ? -7.568 27.844 24.609 1.00 31.88 ? 1155 HOH A O 1 HETATM 3669 O O . HOH R 6 . ? 26.818 11.932 13.346 1.00 32.31 ? 1156 HOH A O 1 HETATM 3670 O O . HOH R 6 . ? 2.945 -2.740 16.921 1.00 40.61 ? 1157 HOH A O 1 HETATM 3671 O O . HOH R 6 . ? 13.626 14.484 40.372 1.00 42.53 ? 1158 HOH A O 1 HETATM 3672 O O . HOH R 6 . ? -4.467 -2.012 8.297 1.00 37.70 ? 1159 HOH A O 1 HETATM 3673 O O . HOH R 6 . ? 27.734 18.893 20.819 1.00 45.79 ? 1160 HOH A O 1 HETATM 3674 O O . HOH R 6 . ? 6.295 5.973 0.570 1.00 33.02 ? 1161 HOH A O 1 HETATM 3675 O O . HOH R 6 . ? -12.948 0.438 28.739 1.00 46.52 ? 1162 HOH A O 1 HETATM 3676 O O . HOH R 6 . ? 22.814 37.058 7.756 1.00 57.23 ? 1163 HOH A O 1 HETATM 3677 O O . HOH R 6 . ? -8.942 7.197 17.233 1.00 34.04 ? 1164 HOH A O 1 HETATM 3678 O O . HOH R 6 . ? -8.215 25.340 21.589 1.00 49.74 ? 1165 HOH A O 1 HETATM 3679 O O . HOH R 6 . ? 18.727 4.484 -7.957 1.00 57.43 ? 1166 HOH A O 1 HETATM 3680 O O . HOH R 6 . ? 11.609 -2.491 18.258 1.00 38.11 ? 1167 HOH A O 1 HETATM 3681 O O . HOH R 6 . ? 12.439 20.763 43.742 1.00 47.17 ? 1168 HOH A O 1 HETATM 3682 O O . HOH R 6 . ? 18.501 35.014 17.609 1.00 37.38 ? 1169 HOH A O 1 HETATM 3683 O O . HOH R 6 . ? -4.572 7.604 45.983 1.00 56.45 ? 1170 HOH A O 1 HETATM 3684 O O . HOH R 6 . ? 18.607 11.112 28.282 1.00 38.84 ? 1171 HOH A O 1 HETATM 3685 O O . HOH R 6 . ? 5.692 3.262 13.324 1.00 45.46 ? 1172 HOH A O 1 HETATM 3686 O O . HOH R 6 . ? -3.435 3.701 40.320 1.00 50.87 ? 1173 HOH A O 1 HETATM 3687 O O . HOH R 6 . ? 18.658 20.492 -15.825 1.00 35.24 ? 1174 HOH A O 1 HETATM 3688 O O . HOH R 6 . ? 31.718 21.941 4.355 1.00 40.12 ? 1175 HOH A O 1 HETATM 3689 O O . HOH R 6 . ? 4.972 -6.310 12.934 1.00 35.91 ? 1176 HOH A O 1 HETATM 3690 O O . HOH R 6 . ? -4.815 -1.722 17.885 1.00 44.16 ? 1177 HOH A O 1 HETATM 3691 O O . HOH R 6 . ? -9.633 17.998 11.026 1.00 44.94 ? 1178 HOH A O 1 HETATM 3692 O O . HOH R 6 . ? 10.221 -5.255 20.945 1.00 37.35 ? 1179 HOH A O 1 HETATM 3693 O O . HOH R 6 . ? -3.243 22.503 36.529 1.00 34.68 ? 1180 HOH A O 1 HETATM 3694 O O . HOH R 6 . ? -8.784 5.097 31.810 1.00 36.87 ? 1181 HOH A O 1 HETATM 3695 O O . HOH R 6 . ? 22.204 6.346 16.183 1.00 44.43 ? 1182 HOH A O 1 HETATM 3696 O O . HOH R 6 . ? 23.648 10.891 -5.637 1.00 37.95 ? 1183 HOH A O 1 HETATM 3697 O O . HOH R 6 . ? -1.973 35.785 7.206 1.00 42.72 ? 1184 HOH A O 1 HETATM 3698 O O . HOH R 6 . ? 24.067 6.103 20.765 1.00 40.98 ? 1185 HOH A O 1 HETATM 3699 O O . HOH R 6 . ? -8.337 28.438 20.500 1.00 49.49 ? 1186 HOH A O 1 HETATM 3700 O O . HOH R 6 . ? 16.285 30.795 -18.774 1.00 49.38 ? 1187 HOH A O 1 HETATM 3701 O O . HOH R 6 . ? 16.885 9.822 36.479 1.00 43.94 ? 1188 HOH A O 1 HETATM 3702 O O . HOH R 6 . ? 12.383 21.514 -14.955 1.00 33.37 ? 1189 HOH A O 1 HETATM 3703 O O . HOH R 6 . ? 16.729 6.676 -12.157 1.00 43.35 ? 1190 HOH A O 1 HETATM 3704 O O . HOH R 6 . ? 13.718 38.619 21.134 1.00 47.91 ? 1191 HOH A O 1 HETATM 3705 O O . HOH R 6 . ? -4.623 28.324 2.823 1.00 50.80 ? 1192 HOH A O 1 HETATM 3706 O O . HOH R 6 . ? 8.829 3.935 0.761 1.00 44.32 ? 1193 HOH A O 1 HETATM 3707 O O . HOH R 6 . ? 12.961 -8.495 -3.358 1.00 58.04 ? 1194 HOH A O 1 HETATM 3708 O O . HOH R 6 . ? -6.023 20.711 7.506 1.00 39.27 ? 1195 HOH A O 1 HETATM 3709 O O . HOH R 6 . ? 10.023 19.488 -12.395 1.00 38.91 ? 1196 HOH A O 1 HETATM 3710 O O . HOH R 6 . ? 17.216 3.505 16.356 1.00 39.59 ? 1197 HOH A O 1 HETATM 3711 O O . HOH R 6 . ? -7.911 25.581 11.164 1.00 37.44 ? 1198 HOH A O 1 HETATM 3712 O O . HOH R 6 . ? 20.724 35.803 2.298 1.00 35.88 ? 1199 HOH A O 1 HETATM 3713 O O . HOH R 6 . ? 6.534 -0.851 13.696 1.00 54.79 ? 1200 HOH A O 1 HETATM 3714 O O . HOH R 6 . ? 28.679 24.448 10.371 1.00 51.59 ? 1201 HOH A O 1 HETATM 3715 O O . HOH R 6 . ? 15.889 36.701 21.807 1.00 47.87 ? 1202 HOH A O 1 HETATM 3716 O O . HOH R 6 . ? -13.256 16.374 24.124 1.00 40.67 ? 1203 HOH A O 1 HETATM 3717 O O . HOH R 6 . ? 2.802 15.652 -6.772 1.00 42.17 ? 1204 HOH A O 1 HETATM 3718 O O . HOH R 6 . ? 15.083 8.148 34.899 1.00 46.11 ? 1205 HOH A O 1 HETATM 3719 O O . HOH R 6 . ? 22.809 14.047 34.662 1.00 54.20 ? 1206 HOH A O 1 HETATM 3720 O O . HOH R 6 . ? -4.246 23.481 9.853 1.00 31.47 ? 1207 HOH A O 1 HETATM 3721 O O . HOH R 6 . ? 11.775 -4.074 8.324 1.00 40.38 ? 1208 HOH A O 1 HETATM 3722 O O . HOH R 6 . ? 2.164 0.854 1.205 1.00 58.77 ? 1209 HOH A O 1 HETATM 3723 O O . HOH R 6 . ? 11.988 24.700 37.089 1.00 38.83 ? 1210 HOH A O 1 HETATM 3724 O O . HOH R 6 . ? -1.705 -5.495 24.642 1.00 45.19 ? 1211 HOH A O 1 HETATM 3725 O O . HOH R 6 . ? 20.853 8.505 26.049 1.00 41.92 ? 1212 HOH A O 1 HETATM 3726 O O . HOH R 6 . ? 27.271 31.876 6.036 1.00 38.13 ? 1213 HOH A O 1 HETATM 3727 O O . HOH R 6 . ? 24.799 4.385 26.439 1.00 50.12 ? 1214 HOH A O 1 HETATM 3728 O O . HOH R 6 . ? 12.924 -10.975 -1.552 1.00 62.81 ? 1215 HOH A O 1 HETATM 3729 O O . HOH R 6 . ? 6.915 -6.960 11.357 1.00 45.35 ? 1216 HOH A O 1 HETATM 3730 O O . HOH R 6 . ? -12.429 14.936 20.021 1.00 42.25 ? 1217 HOH A O 1 HETATM 3731 O O . HOH R 6 . ? 31.305 30.680 -0.150 1.00 43.40 ? 1218 HOH A O 1 HETATM 3732 O O . HOH R 6 . ? 4.386 41.653 15.342 1.00 45.91 ? 1219 HOH A O 1 HETATM 3733 O O . HOH R 6 . ? -6.504 16.761 7.068 1.00 47.82 ? 1220 HOH A O 1 HETATM 3734 O O . HOH R 6 . ? 16.612 25.323 27.598 1.00 52.09 ? 1221 HOH A O 1 HETATM 3735 O O . HOH R 6 . ? 28.277 9.366 19.799 1.00 43.32 ? 1222 HOH A O 1 HETATM 3736 O O . HOH R 6 . ? 29.127 29.962 -1.265 1.00 41.71 ? 1223 HOH A O 1 HETATM 3737 O O . HOH R 6 . ? 17.240 34.875 20.897 1.00 42.87 ? 1224 HOH A O 1 HETATM 3738 O O . HOH R 6 . ? -11.188 20.966 29.904 1.00 54.15 ? 1225 HOH A O 1 HETATM 3739 O O . HOH R 6 . ? 2.549 37.516 23.582 1.00 44.77 ? 1226 HOH A O 1 HETATM 3740 O O . HOH R 6 . ? 9.479 -2.720 9.760 1.00 37.15 ? 1227 HOH A O 1 HETATM 3741 O O . HOH R 6 . ? -6.621 28.338 12.622 1.00 42.12 ? 1228 HOH A O 1 HETATM 3742 O O . HOH R 6 . ? 6.164 8.165 -4.925 1.00 32.78 ? 1229 HOH A O 1 HETATM 3743 O O . HOH R 6 . ? -2.511 31.265 29.292 1.00 43.36 ? 1230 HOH A O 1 HETATM 3744 O O . HOH R 6 . ? -4.292 -1.295 14.748 1.00 50.74 ? 1231 HOH A O 1 HETATM 3745 O O . HOH R 6 . ? 14.249 6.474 48.116 1.00 55.19 ? 1232 HOH A O 1 HETATM 3746 O O . HOH R 6 . ? 17.065 23.166 31.506 1.00 48.08 ? 1233 HOH A O 1 HETATM 3747 O O . HOH R 6 . ? 9.643 20.637 40.944 1.00 33.70 ? 1234 HOH A O 1 HETATM 3748 O O . HOH R 6 . ? 25.449 31.725 2.372 1.00 38.40 ? 1235 HOH A O 1 HETATM 3749 O O . HOH R 6 . ? -6.926 18.216 39.711 1.00 42.45 ? 1236 HOH A O 1 HETATM 3750 O O . HOH R 6 . ? 27.570 16.019 9.694 1.00 37.56 ? 1237 HOH A O 1 HETATM 3751 O O . HOH R 6 . ? -13.253 8.069 34.415 1.00 55.11 ? 1238 HOH A O 1 HETATM 3752 O O . HOH R 6 . ? 13.595 30.214 -18.424 1.00 42.89 ? 1239 HOH A O 1 HETATM 3753 O O . HOH R 6 . ? 4.247 -9.228 28.172 1.00 49.08 ? 1240 HOH A O 1 HETATM 3754 O O . HOH R 6 . ? -12.713 6.955 19.739 1.00 47.59 ? 1241 HOH A O 1 HETATM 3755 O O . HOH R 6 . ? 16.789 4.429 24.833 1.00 48.85 ? 1242 HOH A O 1 HETATM 3756 O O . HOH R 6 . ? -19.092 -0.955 26.496 1.00 56.62 ? 1243 HOH A O 1 HETATM 3757 O O . HOH R 6 . ? 9.884 -7.133 -3.066 1.00 42.79 ? 1244 HOH A O 1 HETATM 3758 O O . HOH R 6 . ? 13.837 23.210 45.915 1.00 54.35 ? 1245 HOH A O 1 HETATM 3759 O O . HOH R 6 . ? 8.560 -1.009 -1.857 1.00 47.75 ? 1246 HOH A O 1 HETATM 3760 O O . HOH R 6 . ? 27.947 13.339 6.035 1.00 56.31 ? 1247 HOH A O 1 HETATM 3761 O O . HOH R 6 . ? -15.058 21.569 12.954 1.00 51.71 ? 1248 HOH A O 1 HETATM 3762 O O . HOH R 6 . ? 20.152 2.557 14.878 1.00 50.72 ? 1249 HOH A O 1 HETATM 3763 O O . HOH R 6 . ? -18.422 -0.143 28.964 1.00 44.85 ? 1250 HOH A O 1 HETATM 3764 O O . HOH R 6 . ? 2.184 -8.252 18.332 1.00 36.08 ? 1251 HOH A O 1 HETATM 3765 O O . HOH R 6 . ? -4.921 24.990 25.689 1.00 34.66 ? 1252 HOH A O 1 HETATM 3766 O O . HOH R 6 . ? 18.246 4.821 22.754 1.00 45.11 ? 1253 HOH A O 1 HETATM 3767 O O . HOH R 6 . ? 13.596 15.215 -12.371 1.00 46.39 ? 1254 HOH A O 1 HETATM 3768 O O . HOH R 6 . ? -3.293 20.062 42.148 1.00 46.24 ? 1255 HOH A O 1 HETATM 3769 O O . HOH R 6 . ? 33.315 20.808 2.538 1.00 44.00 ? 1256 HOH A O 1 HETATM 3770 O O . HOH R 6 . ? 19.524 6.143 26.651 1.00 56.22 ? 1257 HOH A O 1 HETATM 3771 O O . HOH R 6 . ? 23.384 7.249 27.065 1.00 51.39 ? 1258 HOH A O 1 HETATM 3772 O O . HOH R 6 . ? 6.308 38.553 25.566 1.00 47.19 ? 1259 HOH A O 1 HETATM 3773 O O . HOH R 6 . ? 13.128 34.380 -9.462 1.00 44.89 ? 1260 HOH A O 1 HETATM 3774 O O . HOH R 6 . ? 20.488 1.465 -2.682 1.00 42.44 ? 1261 HOH A O 1 HETATM 3775 O O . HOH R 6 . ? 24.331 -4.420 4.870 1.00 47.72 ? 1262 HOH A O 1 HETATM 3776 O O . HOH R 6 . ? 30.790 24.708 11.769 1.00 46.05 ? 1263 HOH A O 1 HETATM 3777 O O . HOH R 6 . ? 12.641 21.341 39.799 1.00 50.61 ? 1264 HOH A O 1 HETATM 3778 O O . HOH R 6 . ? 22.291 27.369 11.603 1.00 39.45 ? 1265 HOH A O 1 HETATM 3779 O O . HOH R 6 . ? 1.390 13.994 -8.919 1.00 49.37 ? 1266 HOH A O 1 HETATM 3780 O O . HOH R 6 . ? 0.393 19.905 -8.848 1.00 39.97 ? 1267 HOH A O 1 HETATM 3781 O O . HOH R 6 . ? 33.226 19.487 14.246 1.00 47.13 ? 1268 HOH A O 1 HETATM 3782 O O . HOH R 6 . ? 16.639 12.817 -11.344 1.00 41.16 ? 1269 HOH A O 1 HETATM 3783 O O . HOH R 6 . ? -0.966 37.386 18.265 1.00 58.07 ? 1270 HOH A O 1 HETATM 3784 O O . HOH R 6 . ? -2.248 36.014 28.811 1.00 40.62 ? 1271 HOH A O 1 HETATM 3785 O O . HOH R 6 . ? -16.805 14.286 32.373 1.00 51.76 ? 1272 HOH A O 1 HETATM 3786 O O . HOH R 6 . ? -1.896 19.192 44.625 1.00 48.84 ? 1273 HOH A O 1 HETATM 3787 O O . HOH R 6 . ? 24.584 9.924 -3.740 1.00 43.32 ? 1274 HOH A O 1 HETATM 3788 O O . HOH R 6 . ? 11.722 23.869 -17.489 1.00 45.14 ? 1275 HOH A O 1 HETATM 3789 O O . HOH R 6 . ? 21.503 24.322 27.931 1.00 51.11 ? 1276 HOH A O 1 HETATM 3790 O O . HOH R 6 . ? 22.214 4.523 -7.004 1.00 42.02 ? 1277 HOH A O 1 HETATM 3791 O O . HOH R 6 . ? -1.375 3.699 45.943 1.00 52.33 ? 1278 HOH A O 1 HETATM 3792 O O . HOH R 6 . ? 1.476 38.973 19.097 1.00 41.43 ? 1279 HOH A O 1 HETATM 3793 O O . HOH R 6 . ? 13.518 28.349 31.157 1.00 44.56 ? 1280 HOH A O 1 HETATM 3794 O O . HOH R 6 . ? 26.423 15.567 24.237 1.00 40.10 ? 1281 HOH A O 1 HETATM 3795 O O . HOH R 6 . ? 12.428 -1.588 20.653 1.00 47.32 ? 1282 HOH A O 1 HETATM 3796 O O . HOH R 6 . ? -5.116 3.131 34.341 1.00 40.79 ? 1283 HOH A O 1 HETATM 3797 O O . HOH R 6 . ? -0.325 40.879 16.757 1.00 48.59 ? 1284 HOH A O 1 HETATM 3798 O O . HOH R 6 . ? 12.847 1.575 -13.139 1.00 57.34 ? 1285 HOH A O 1 # 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 ILE 1 1 1 ILE ILE A . n A 1 2 VAL 2 2 2 VAL VAL A . n A 1 3 MET 3 3 3 MET MET A . n A 1 4 PRO 4 4 4 PRO PRO A . n A 1 5 ASP 5 5 5 ASP ASP A . n A 1 6 GLY 6 6 6 GLY GLY A . n A 1 7 VAL 7 7 7 VAL VAL A . n A 1 8 THR 8 8 8 THR THR A . n A 1 9 GLY 9 9 9 GLY GLY A . n A 1 10 LYS 10 10 10 LYS LYS A . n A 1 11 VAL 11 11 11 VAL VAL A . n A 1 12 PRO 12 12 12 PRO PRO A . n A 1 13 SER 13 13 13 SER SER A . n A 1 14 LEU 14 14 14 LEU LEU A . n A 1 15 GLY 15 15 15 GLY GLY A . n A 1 16 TRP 16 16 16 TRP TRP A . n A 1 17 ASN 17 17 17 ASN ASN A . n A 1 18 SER 18 18 18 SER SER A . n A 1 19 TRP 19 19 19 TRP TRP A . n A 1 20 ASN 20 20 20 ASN ASN A . n A 1 21 ALA 21 21 21 ALA ALA A . n A 1 22 TYR 22 22 22 TYR TYR A . n A 1 23 HIS 23 23 23 HIS HIS A . n A 1 24 CYS 24 24 24 CYS CYS A . n A 1 25 ASP 25 25 25 ASP ASP A . n A 1 26 ILE 26 26 26 ILE ILE A . n A 1 27 ASP 27 27 27 ASP ASP A . n A 1 28 GLU 28 28 28 GLU GLU A . n A 1 29 SER 29 29 29 SER SER A . n A 1 30 LYS 30 30 30 LYS LYS A . n A 1 31 PHE 31 31 31 PHE PHE A . n A 1 32 LEU 32 32 32 LEU LEU A . n A 1 33 SER 33 33 33 SER SER A . n A 1 34 ALA 34 34 34 ALA ALA A . n A 1 35 ALA 35 35 35 ALA ALA A . n A 1 36 GLU 36 36 36 GLU GLU A . n A 1 37 LEU 37 37 37 LEU LEU A . n A 1 38 ILE 38 38 38 ILE ILE A . n A 1 39 VAL 39 39 39 VAL VAL A . n A 1 40 SER 40 40 40 SER SER A . n A 1 41 SER 41 41 41 SER SER A . n A 1 42 GLY 42 42 42 GLY GLY A . n A 1 43 LEU 43 43 43 LEU LEU A . n A 1 44 LEU 44 44 44 LEU LEU A . n A 1 45 ASP 45 45 45 ASP ASP A . n A 1 46 ALA 46 46 46 ALA ALA A . n A 1 47 GLY 47 47 47 GLY GLY A . n A 1 48 TYR 48 48 48 TYR TYR A . n A 1 49 ASN 49 49 49 ASN ASN A . n A 1 50 TYR 50 50 50 TYR TYR A . n A 1 51 VAL 51 51 51 VAL VAL A . n A 1 52 ASN 52 52 52 ASN ASN A . n A 1 53 ILE 53 53 53 ILE ILE A . n A 1 54 ASP 54 54 54 ASP ASP A . n A 1 55 ASP 55 55 55 ASP ASP A . n A 1 56 CYS 56 56 56 CYS CYS A . n A 1 57 TRP 57 57 57 TRP TRP A . n A 1 58 SER 58 58 58 SER SER A . n A 1 59 MET 59 59 59 MET MET A . n A 1 60 LYS 60 60 60 LYS LYS A . n A 1 61 ASP 61 61 61 ASP ASP A . n A 1 62 GLY 62 62 62 GLY GLY A . n A 1 63 ARG 63 63 63 ARG ARG A . n A 1 64 VAL 64 64 64 VAL VAL A . n A 1 65 ASP 65 65 65 ASP ASP A . n A 1 66 GLY 66 66 66 GLY GLY A . n A 1 67 HIS 67 67 67 HIS HIS A . n A 1 68 ILE 68 68 68 ILE ILE A . n A 1 69 ALA 69 69 69 ALA ALA A . n A 1 70 PRO 70 70 70 PRO PRO A . n A 1 71 ASN 71 71 71 ASN ASN A . n A 1 72 ALA 72 72 72 ALA ALA A . n A 1 73 THR 73 73 73 THR THR A . n A 1 74 ARG 74 74 74 ARG ARG A . n A 1 75 PHE 75 75 75 PHE PHE A . n A 1 76 PRO 76 76 76 PRO PRO A . n A 1 77 ASP 77 77 77 ASP ASP A . n A 1 78 GLY 78 78 78 GLY GLY A . n A 1 79 ILE 79 79 79 ILE ILE A . n A 1 80 ASP 80 80 80 ASP ASP A . n A 1 81 GLY 81 81 81 GLY GLY A . n A 1 82 LEU 82 82 82 LEU LEU A . n A 1 83 ALA 83 83 83 ALA ALA A . n A 1 84 LYS 84 84 84 LYS LYS A . n A 1 85 LYS 85 85 85 LYS LYS A . n A 1 86 VAL 86 86 86 VAL VAL A . n A 1 87 HIS 87 87 87 HIS HIS A . n A 1 88 ALA 88 88 88 ALA ALA A . n A 1 89 LEU 89 89 89 LEU LEU A . n A 1 90 GLY 90 90 90 GLY GLY A . n A 1 91 LEU 91 91 91 LEU LEU A . n A 1 92 LYS 92 92 92 LYS LYS A . n A 1 93 LEU 93 93 93 LEU LEU A . n A 1 94 GLY 94 94 94 GLY GLY A . n A 1 95 ILE 95 95 95 ILE ILE A . n A 1 96 TYR 96 96 96 TYR TYR A . n A 1 97 SER 97 97 97 SER SER A . n A 1 98 THR 98 98 98 THR THR A . n A 1 99 ALA 99 99 99 ALA ALA A . n A 1 100 GLY 100 100 100 GLY GLY A . n A 1 101 THR 101 101 101 THR THR A . n A 1 102 ALA 102 102 102 ALA ALA A . n A 1 103 THR 103 103 103 THR THR A . n A 1 104 CYS 104 104 104 CYS CYS A . n A 1 105 ALA 105 105 105 ALA ALA A . n A 1 106 GLY 106 106 106 GLY GLY A . n A 1 107 TYR 107 107 107 TYR TYR A . n A 1 108 PRO 108 108 108 PRO PRO A . n A 1 109 ALA 109 109 109 ALA ALA A . n A 1 110 SER 110 110 110 SER SER A . n A 1 111 LEU 111 111 111 LEU LEU A . n A 1 112 GLY 112 112 112 GLY GLY A . n A 1 113 TYR 113 113 113 TYR TYR A . n A 1 114 GLU 114 114 114 GLU GLU A . n A 1 115 ASP 115 115 115 ASP ASP A . n A 1 116 VAL 116 116 116 VAL VAL A . n A 1 117 ASP 117 117 117 ASP ASP A . n A 1 118 ALA 118 118 118 ALA ALA A . n A 1 119 ALA 119 119 119 ALA ALA A . n A 1 120 ASP 120 120 120 ASP ASP A . n A 1 121 PHE 121 121 121 PHE PHE A . n A 1 122 ALA 122 122 122 ALA ALA A . n A 1 123 ASP 123 123 123 ASP ASP A . n A 1 124 TRP 124 124 124 TRP TRP A . n A 1 125 GLY 125 125 125 GLY GLY A . n A 1 126 VAL 126 126 126 VAL VAL A . n A 1 127 ASP 127 127 127 ASP ASP A . n A 1 128 TYR 128 128 128 TYR TYR A . n A 1 129 LEU 129 129 129 LEU LEU A . n A 1 130 LYS 130 130 130 LYS LYS A . n A 1 131 TYR 131 131 131 TYR TYR A . n A 1 132 ASP 132 132 132 ASP ASP A . n A 1 133 ASN 133 133 133 ASN ASN A . n A 1 134 CYS 134 134 134 CYS CYS A . n A 1 135 ASN 135 135 135 ASN ASN A . n A 1 136 VAL 136 136 136 VAL VAL A . n A 1 137 PRO 137 137 137 PRO PRO A . n A 1 138 SER 138 138 138 SER SER A . n A 1 139 ASP 139 139 139 ASP ASP A . n A 1 140 TRP 140 140 140 TRP TRP A . n A 1 141 GLN 141 141 141 GLN GLN A . n A 1 142 ASP 142 142 142 ASP ASP A . n A 1 143 GLU 143 143 143 GLU GLU A . n A 1 144 TYR 144 144 144 TYR TYR A . n A 1 145 VAL 145 145 145 VAL VAL A . n A 1 146 ALA 146 146 146 ALA ALA A . n A 1 147 CYS 147 147 147 CYS CYS A . n A 1 148 ASN 148 148 148 ASN ASN A . n A 1 149 PRO 149 149 149 PRO PRO A . n A 1 150 ASP 150 150 150 ASP ASP A . n A 1 151 PHE 151 151 151 PHE PHE A . n A 1 152 VAL 152 152 152 VAL VAL A . n A 1 153 LYS 153 153 153 LYS LYS A . n A 1 154 THR 154 154 154 THR THR A . n A 1 155 GLY 155 155 155 GLY GLY A . n A 1 156 PRO 156 156 156 PRO PRO A . n A 1 157 ASN 157 157 157 ASN ASN A . n A 1 158 GLY 158 158 158 GLY GLY A . n A 1 159 THR 159 159 159 THR THR A . n A 1 160 CYS 160 160 160 CYS CYS A . n A 1 161 THR 161 161 161 THR THR A . n A 1 162 THR 162 162 162 THR THR A . n A 1 163 ALA 163 163 163 ALA ALA A . n A 1 164 LEU 164 164 164 LEU LEU A . n A 1 165 ASP 165 165 165 ASP ASP A . n A 1 166 PRO 166 166 166 PRO PRO A . n A 1 167 THR 167 167 167 THR THR A . n A 1 168 LEU 168 168 168 LEU LEU A . n A 1 169 ALA 169 169 169 ALA ALA A . n A 1 170 PRO 170 170 170 PRO PRO A . n A 1 171 PRO 171 171 171 PRO PRO A . n A 1 172 GLY 172 172 172 GLY GLY A . n A 1 173 TYR 173 173 173 TYR TYR A . n A 1 174 ASP 174 174 174 ASP ASP A . n A 1 175 TRP 175 175 175 TRP TRP A . n A 1 176 SER 176 176 176 SER SER A . n A 1 177 THR 177 177 177 THR THR A . n A 1 178 SER 178 178 178 SER SER A . n A 1 179 LYS 179 179 179 LYS LYS A . n A 1 180 SER 180 180 180 SER SER A . n A 1 181 ALA 181 181 181 ALA ALA A . n A 1 182 GLU 182 182 182 GLU GLU A . n A 1 183 ARG 183 183 183 ARG ARG A . n A 1 184 PHE 184 184 184 PHE PHE A . n A 1 185 GLY 185 185 185 GLY GLY A . n A 1 186 ALA 186 186 186 ALA ALA A . n A 1 187 MET 187 187 187 MET MET A . n A 1 188 ARG 188 188 188 ARG ARG A . n A 1 189 ASN 189 189 189 ASN ASN A . n A 1 190 ALA 190 190 190 ALA ALA A . n A 1 191 LEU 191 191 191 LEU LEU A . n A 1 192 ALA 192 192 192 ALA ALA A . n A 1 193 LYS 193 193 193 LYS LYS A . n A 1 194 GLN 194 194 194 GLN GLN A . n A 1 195 SER 195 195 195 SER SER A . n A 1 196 HIS 196 196 196 HIS HIS A . n A 1 197 GLU 197 197 197 GLU GLU A . n A 1 198 ILE 198 198 198 ILE ILE A . n A 1 199 VAL 199 199 199 VAL VAL A . n A 1 200 LEU 200 200 200 LEU LEU A . n A 1 201 SER 201 201 201 SER SER A . n A 1 202 MET 202 202 202 MET MET A . n A 1 203 CYS 203 203 203 CYS CYS A . n A 1 204 ILE 204 204 204 ILE ILE A . n A 1 205 TRP 205 205 205 TRP TRP A . n A 1 206 GLY 206 206 206 GLY GLY A . n A 1 207 GLN 207 207 207 GLN GLN A . n A 1 208 ALA 208 208 208 ALA ALA A . n A 1 209 ASP 209 209 209 ASP ASP A . n A 1 210 VAL 210 210 210 VAL VAL A . n A 1 211 PHE 211 211 211 PHE PHE A . n A 1 212 SER 212 212 212 SER SER A . n A 1 213 TRP 213 213 213 TRP TRP A . n A 1 214 GLY 214 214 214 GLY GLY A . n A 1 215 ASN 215 215 215 ASN ASN A . n A 1 216 SER 216 216 216 SER SER A . n A 1 217 THR 217 217 217 THR THR A . n A 1 218 GLY 218 218 218 GLY GLY A . n A 1 219 ILE 219 219 219 ILE ILE A . n A 1 220 SER 220 220 220 SER SER A . n A 1 221 TRP 221 221 221 TRP TRP A . n A 1 222 ARG 222 222 222 ARG ARG A . n A 1 223 MET 223 223 223 MET MET A . n A 1 224 SER 224 224 224 SER SER A . n A 1 225 ASP 225 225 225 ASP ASP A . n A 1 226 ASP 226 226 226 ASP ASP A . n A 1 227 ILE 227 227 227 ILE ILE A . n A 1 228 SER 228 228 228 SER SER A . n A 1 229 PRO 229 229 229 PRO PRO A . n A 1 230 ASN 230 230 230 ASN ASN A . n A 1 231 TRP 231 231 231 TRP TRP A . n A 1 232 GLY 232 232 232 GLY GLY A . n A 1 233 SER 233 233 233 SER SER A . n A 1 234 VAL 234 234 234 VAL VAL A . n A 1 235 THR 235 235 235 THR THR A . n A 1 236 ARG 236 236 236 ARG ARG A . n A 1 237 ILE 237 237 237 ILE ILE A . n A 1 238 LEU 238 238 238 LEU LEU A . n A 1 239 ASN 239 239 239 ASN ASN A . n A 1 240 LEU 240 240 240 LEU LEU A . n A 1 241 ASN 241 241 241 ASN ASN A . n A 1 242 SER 242 242 242 SER SER A . n A 1 243 PHE 243 243 243 PHE PHE A . n A 1 244 LYS 244 244 244 LYS LYS A . n A 1 245 LEU 245 245 245 LEU LEU A . n A 1 246 ASN 246 246 246 ASN ASN A . n A 1 247 SER 247 247 247 SER SER A . n A 1 248 VAL 248 248 248 VAL VAL A . n A 1 249 ASP 249 249 249 ASP ASP A . n A 1 250 PHE 250 250 250 PHE PHE A . n A 1 251 TRP 251 251 251 TRP TRP A . n A 1 252 GLY 252 252 252 GLY GLY A . n A 1 253 HIS 253 253 253 HIS HIS A . n A 1 254 ASN 254 254 254 ASN ASN A . n A 1 255 ASP 255 255 255 ASP ASP A . n A 1 256 ALA 256 256 256 ALA ALA A . n A 1 257 ASP 257 257 257 ASP ASP A . n A 1 258 MET 258 258 258 MET MET A . n A 1 259 LEU 259 259 259 LEU LEU A . n A 1 260 GLU 260 260 260 GLU GLU A . n A 1 261 VAL 261 261 261 VAL VAL A . n A 1 262 GLY 262 262 262 GLY GLY A . n A 1 263 ASN 263 263 263 ASN ASN A . n A 1 264 GLY 264 264 264 GLY GLY A . n A 1 265 ASN 265 265 265 ASN ASN A . n A 1 266 LEU 266 266 266 LEU LEU A . n A 1 267 THR 267 267 267 THR THR A . n A 1 268 ALA 268 268 268 ALA ALA A . n A 1 269 ALA 269 269 269 ALA ALA A . n A 1 270 GLU 270 270 270 GLU GLU A . n A 1 271 THR 271 271 271 THR THR A . n A 1 272 ARG 272 272 272 ARG ARG A . n A 1 273 THR 273 273 273 THR THR A . n A 1 274 HIS 274 274 274 HIS HIS A . n A 1 275 PHE 275 275 275 PHE PHE A . n A 1 276 ALA 276 276 276 ALA ALA A . n A 1 277 LEU 277 277 277 LEU LEU A . n A 1 278 TRP 278 278 278 TRP TRP A . n A 1 279 ALA 279 279 279 ALA ALA A . n A 1 280 ALA 280 280 280 ALA ALA A . n A 1 281 MET 281 281 281 MET MET A . n A 1 282 LYS 282 282 282 LYS LYS A . n A 1 283 SER 283 283 283 SER SER A . n A 1 284 PRO 284 284 284 PRO PRO A . n A 1 285 LEU 285 285 285 LEU LEU A . n A 1 286 LEU 286 286 286 LEU LEU A . n A 1 287 ILE 287 287 287 ILE ILE A . n A 1 288 GLY 288 288 288 GLY GLY A . n A 1 289 THR 289 289 289 THR THR A . n A 1 290 ASP 290 290 290 ASP ASP A . n A 1 291 LEU 291 291 291 LEU LEU A . n A 1 292 ALA 292 292 292 ALA ALA A . n A 1 293 GLN 293 293 293 GLN GLN A . n A 1 294 LEU 294 294 294 LEU LEU A . n A 1 295 SER 295 295 295 SER SER A . n A 1 296 GLN 296 296 296 GLN GLN A . n A 1 297 ASN 297 297 297 ASN ASN A . n A 1 298 ASN 298 298 298 ASN ASN A . n A 1 299 ILE 299 299 299 ILE ILE A . n A 1 300 ASN 300 300 300 ASN ASN A . n A 1 301 LEU 301 301 301 LEU LEU A . n A 1 302 LEU 302 302 302 LEU LEU A . n A 1 303 LYS 303 303 303 LYS LYS A . n A 1 304 ASN 304 304 304 ASN ASN A . n A 1 305 LYS 305 305 305 LYS LYS A . n A 1 306 HIS 306 306 306 HIS HIS A . n A 1 307 LEU 307 307 307 LEU LEU A . n A 1 308 LEU 308 308 308 LEU LEU A . n A 1 309 ALA 309 309 309 ALA ALA A . n A 1 310 PHE 310 310 310 PHE PHE A . n A 1 311 ASN 311 311 311 ASN ASN A . n A 1 312 GLN 312 312 312 GLN GLN A . n A 1 313 ASP 313 313 313 ASP ASP A . n A 1 314 SER 314 314 314 SER SER A . n A 1 315 VAL 315 315 315 VAL VAL A . n A 1 316 TYR 316 316 316 TYR TYR A . n A 1 317 GLY 317 317 317 GLY GLY A . n A 1 318 GLN 318 318 318 GLN GLN A . n A 1 319 PRO 319 319 319 PRO PRO A . n A 1 320 ALA 320 320 320 ALA ALA A . n A 1 321 THR 321 321 321 THR THR A . n A 1 322 PRO 322 322 322 PRO PRO A . n A 1 323 TYR 323 323 323 TYR TYR A . n A 1 324 LYS 324 324 324 LYS LYS A . n A 1 325 TRP 325 325 325 TRP TRP A . n A 1 326 GLY 326 326 326 GLY GLY A . n A 1 327 ILE 327 327 327 ILE ILE A . n A 1 328 ASN 328 328 328 ASN ASN A . n A 1 329 PRO 329 329 329 PRO PRO A . n A 1 330 ASP 330 330 330 ASP ASP A . n A 1 331 TRP 331 331 331 TRP TRP A . n A 1 332 THR 332 332 332 THR THR A . n A 1 333 PHE 333 333 333 PHE PHE A . n A 1 334 ASN 334 334 334 ASN ASN A . n A 1 335 VAL 335 335 335 VAL VAL A . n A 1 336 THR 336 336 336 THR THR A . n A 1 337 TYR 337 337 337 TYR TYR A . n A 1 338 PRO 338 338 338 PRO PRO A . n A 1 339 ALA 339 339 339 ALA ALA A . n A 1 340 GLU 340 340 340 GLU GLU A . n A 1 341 PHE 341 341 341 PHE PHE A . n A 1 342 TRP 342 342 342 TRP TRP A . n A 1 343 ALA 343 343 343 ALA ALA A . n A 1 344 GLY 344 344 344 GLY GLY A . n A 1 345 PRO 345 345 345 PRO PRO A . n A 1 346 SER 346 346 346 SER SER A . n A 1 347 SER 347 347 347 SER SER A . n A 1 348 LYS 348 348 348 LYS LYS A . n A 1 349 GLY 349 349 349 GLY GLY A . n A 1 350 HIS 350 350 350 HIS HIS A . n A 1 351 LEU 351 351 351 LEU LEU A . n A 1 352 VAL 352 352 352 VAL VAL A . n A 1 353 LEU 353 353 353 LEU LEU A . n A 1 354 MET 354 354 354 MET MET A . n A 1 355 VAL 355 355 355 VAL VAL A . n A 1 356 ASN 356 356 356 ASN ASN A . n A 1 357 THR 357 357 357 THR THR A . n A 1 358 LEU 358 358 358 LEU LEU A . n A 1 359 ASP 359 359 359 ASP ASP A . n A 1 360 ILE 360 360 360 ILE ILE A . n A 1 361 THR 361 361 361 THR THR A . n A 1 362 ALA 362 362 362 ALA ALA A . n A 1 363 THR 363 363 363 THR THR A . n A 1 364 LYS 364 364 364 LYS LYS A . n A 1 365 GLU 365 365 365 GLU GLU A . n A 1 366 ALA 366 366 366 ALA ALA A . n A 1 367 LYS 367 367 367 LYS LYS A . n A 1 368 TRP 368 368 368 TRP TRP A . n A 1 369 ASN 369 369 369 ASN ASN A . n A 1 370 GLU 370 370 370 GLU GLU A . n A 1 371 ILE 371 371 371 ILE ILE A . n A 1 372 PRO 372 372 372 PRO PRO A . n A 1 373 GLY 373 373 373 GLY GLY A . n A 1 374 LEU 374 374 374 LEU LEU A . n A 1 375 SER 375 375 375 SER SER A . n A 1 376 ALA 376 376 376 ALA ALA A . n A 1 377 GLY 377 377 377 GLY GLY A . n A 1 378 HIS 378 378 378 HIS HIS A . n A 1 379 TYR 379 379 379 TYR TYR A . n A 1 380 GLU 380 380 380 GLU GLU A . n A 1 381 VAL 381 381 381 VAL VAL A . n A 1 382 ARG 382 382 382 ARG ARG A . n A 1 383 ASP 383 383 383 ASP ASP A . n A 1 384 VAL 384 384 384 VAL VAL A . n A 1 385 TRP 385 385 385 TRP TRP A . n A 1 386 SER 386 386 386 SER SER A . n A 1 387 ASP 387 387 387 ASP ASP A . n A 1 388 LYS 388 388 388 LYS LYS A . n A 1 389 ASP 389 389 389 ASP ASP A . n A 1 390 LEU 390 390 390 LEU LEU A . n A 1 391 GLY 391 391 391 GLY GLY A . n A 1 392 CYS 392 392 392 CYS CYS A . n A 1 393 LEU 393 393 393 LEU LEU A . n A 1 394 SER 394 394 394 SER SER A . n A 1 395 SER 395 395 395 SER SER A . n A 1 396 TYR 396 396 396 TYR TYR A . n A 1 397 LYS 397 397 397 LYS LYS A . n A 1 398 ALA 398 398 398 ALA ALA A . n A 1 399 ALA 399 399 399 ALA ALA A . n A 1 400 VAL 400 400 400 VAL VAL A . n A 1 401 ALA 401 401 401 ALA ALA A . n A 1 402 ALA 402 402 402 ALA ALA A . n A 1 403 HIS 403 403 403 HIS HIS A . n A 1 404 ASP 404 404 404 ASP ASP A . n A 1 405 THR 405 405 405 THR THR A . n A 1 406 ALA 406 406 406 ALA ALA A . n A 1 407 VAL 407 407 407 VAL VAL A . n A 1 408 ILE 408 408 408 ILE ILE A . n A 1 409 LEU 409 409 409 LEU LEU A . n A 1 410 VAL 410 410 410 VAL VAL A . n A 1 411 GLY 411 411 411 GLY GLY A . n A 1 412 LYS 412 412 412 LYS LYS A . n A 1 413 LYS 413 413 413 LYS LYS A . n A 1 414 CYS 414 414 414 CYS CYS A . n A 1 415 GLN 415 415 415 GLN GLN A . n A 1 416 ARG 416 416 416 ARG ARG A . n A 1 417 TRP 417 417 417 TRP TRP A . n # 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 NAG 1 500 500 NAG NAG A . C 2 NAG 2 501 501 NAG NAG A . D 2 NAG 1 600 600 NAG NAG A . E 2 NAG 2 601 601 NAG NAG A . F 3 BMA 3 602 602 BMA MAN A . G 4 MAN 4 603 603 MAN MAN A . H 4 MAN 5 604 604 MAN MAN A . I 4 MAN 6 605 605 MAN MAN A . J 4 MAN 7 606 606 MAN MAN A . K 2 NAG 1 700 700 NAG NAG A . L 2 NAG 2 701 701 NAG NAG A . M 3 BMA 3 702 702 BMA MAN A . N 4 MAN 4 703 703 MAN MAN A . O 2 NAG 1 800 800 NAG NAG A . P 2 NAG 2 801 801 NAG NAG A . Q 5 GAL 1 901 1 GAL GLB A . R 6 HOH 1 902 1 HOH HOH A . R 6 HOH 2 903 2 HOH HOH A . R 6 HOH 3 904 3 HOH HOH A . R 6 HOH 4 905 4 HOH HOH A . R 6 HOH 5 906 5 HOH HOH A . R 6 HOH 6 907 6 HOH HOH A . R 6 HOH 7 908 7 HOH HOH A . R 6 HOH 8 909 8 HOH HOH A . R 6 HOH 9 910 9 HOH HOH A . R 6 HOH 10 911 10 HOH HOH A . R 6 HOH 11 912 11 HOH HOH A . R 6 HOH 12 913 12 HOH HOH A . R 6 HOH 13 914 13 HOH HOH A . R 6 HOH 14 915 14 HOH HOH A . R 6 HOH 15 916 15 HOH HOH A . R 6 HOH 16 917 16 HOH HOH A . R 6 HOH 17 918 17 HOH HOH A . R 6 HOH 18 919 18 HOH HOH A . R 6 HOH 19 920 19 HOH HOH A . R 6 HOH 20 921 20 HOH HOH A . R 6 HOH 21 922 21 HOH HOH A . R 6 HOH 22 923 22 HOH HOH A . R 6 HOH 23 924 23 HOH HOH A . R 6 HOH 24 925 24 HOH HOH A . R 6 HOH 25 926 25 HOH HOH A . R 6 HOH 26 927 26 HOH HOH A . R 6 HOH 27 928 27 HOH HOH A . R 6 HOH 28 929 28 HOH HOH A . R 6 HOH 29 930 29 HOH HOH A . R 6 HOH 30 931 30 HOH HOH A . R 6 HOH 31 932 31 HOH HOH A . R 6 HOH 32 933 32 HOH HOH A . R 6 HOH 33 934 33 HOH HOH A . R 6 HOH 34 935 34 HOH HOH A . R 6 HOH 35 936 35 HOH HOH A . R 6 HOH 36 937 36 HOH HOH A . R 6 HOH 37 938 37 HOH HOH A . R 6 HOH 38 939 38 HOH HOH A . R 6 HOH 39 940 39 HOH HOH A . R 6 HOH 40 941 40 HOH HOH A . R 6 HOH 41 942 41 HOH HOH A . R 6 HOH 42 943 42 HOH HOH A . R 6 HOH 43 944 43 HOH HOH A . R 6 HOH 44 945 44 HOH HOH A . R 6 HOH 45 946 45 HOH HOH A . R 6 HOH 46 947 46 HOH HOH A . R 6 HOH 47 948 47 HOH HOH A . R 6 HOH 48 949 48 HOH HOH A . R 6 HOH 49 950 49 HOH HOH A . R 6 HOH 50 951 50 HOH HOH A . R 6 HOH 51 952 51 HOH HOH A . R 6 HOH 52 953 52 HOH HOH A . R 6 HOH 53 954 53 HOH HOH A . R 6 HOH 54 955 54 HOH HOH A . R 6 HOH 55 956 55 HOH HOH A . R 6 HOH 56 957 56 HOH HOH A . R 6 HOH 57 958 57 HOH HOH A . R 6 HOH 58 959 58 HOH HOH A . R 6 HOH 59 960 59 HOH HOH A . R 6 HOH 60 961 60 HOH HOH A . R 6 HOH 61 962 61 HOH HOH A . R 6 HOH 62 963 62 HOH HOH A . R 6 HOH 63 964 63 HOH HOH A . R 6 HOH 64 965 64 HOH HOH A . R 6 HOH 65 966 65 HOH HOH A . R 6 HOH 66 967 66 HOH HOH A . R 6 HOH 67 968 67 HOH HOH A . R 6 HOH 68 969 68 HOH HOH A . R 6 HOH 69 970 69 HOH HOH A . R 6 HOH 70 971 70 HOH HOH A . R 6 HOH 71 972 71 HOH HOH A . R 6 HOH 72 973 72 HOH HOH A . R 6 HOH 73 974 73 HOH HOH A . R 6 HOH 74 975 74 HOH HOH A . R 6 HOH 75 976 75 HOH HOH A . R 6 HOH 76 977 76 HOH HOH A . R 6 HOH 77 978 77 HOH HOH A . R 6 HOH 78 979 78 HOH HOH A . R 6 HOH 79 980 79 HOH HOH A . R 6 HOH 80 981 80 HOH HOH A . R 6 HOH 81 982 81 HOH HOH A . R 6 HOH 82 983 82 HOH HOH A . R 6 HOH 83 984 83 HOH HOH A . R 6 HOH 84 985 84 HOH HOH A . R 6 HOH 85 986 85 HOH HOH A . R 6 HOH 86 987 86 HOH HOH A . R 6 HOH 87 988 87 HOH HOH A . R 6 HOH 88 989 88 HOH HOH A . R 6 HOH 89 990 89 HOH HOH A . R 6 HOH 90 991 90 HOH HOH A . R 6 HOH 91 992 91 HOH HOH A . R 6 HOH 92 993 92 HOH HOH A . R 6 HOH 93 994 93 HOH HOH A . R 6 HOH 94 995 94 HOH HOH A . R 6 HOH 95 996 95 HOH HOH A . R 6 HOH 96 997 96 HOH HOH A . R 6 HOH 97 998 97 HOH HOH A . R 6 HOH 98 999 98 HOH HOH A . R 6 HOH 99 1000 99 HOH HOH A . R 6 HOH 100 1001 100 HOH HOH A . R 6 HOH 101 1002 101 HOH HOH A . R 6 HOH 102 1003 102 HOH HOH A . R 6 HOH 103 1004 103 HOH HOH A . R 6 HOH 104 1005 104 HOH HOH A . R 6 HOH 105 1006 105 HOH HOH A . R 6 HOH 106 1007 106 HOH HOH A . R 6 HOH 107 1008 107 HOH HOH A . R 6 HOH 108 1009 108 HOH HOH A . R 6 HOH 109 1010 109 HOH HOH A . R 6 HOH 110 1011 110 HOH HOH A . R 6 HOH 111 1012 111 HOH HOH A . R 6 HOH 112 1013 112 HOH HOH A . R 6 HOH 113 1014 113 HOH HOH A . R 6 HOH 114 1015 114 HOH HOH A . R 6 HOH 115 1016 115 HOH HOH A . R 6 HOH 116 1017 116 HOH HOH A . R 6 HOH 117 1018 117 HOH HOH A . R 6 HOH 118 1019 118 HOH HOH A . R 6 HOH 119 1020 119 HOH HOH A . R 6 HOH 120 1021 120 HOH HOH A . R 6 HOH 121 1022 121 HOH HOH A . R 6 HOH 122 1023 122 HOH HOH A . R 6 HOH 123 1024 123 HOH HOH A . R 6 HOH 124 1025 124 HOH HOH A . R 6 HOH 125 1026 125 HOH HOH A . R 6 HOH 126 1027 126 HOH HOH A . R 6 HOH 127 1028 127 HOH HOH A . R 6 HOH 128 1029 128 HOH HOH A . R 6 HOH 129 1030 129 HOH HOH A . R 6 HOH 130 1031 130 HOH HOH A . R 6 HOH 131 1032 131 HOH HOH A . R 6 HOH 132 1033 132 HOH HOH A . R 6 HOH 133 1034 133 HOH HOH A . R 6 HOH 134 1035 134 HOH HOH A . R 6 HOH 135 1036 135 HOH HOH A . R 6 HOH 136 1037 136 HOH HOH A . R 6 HOH 137 1038 137 HOH HOH A . R 6 HOH 138 1039 138 HOH HOH A . R 6 HOH 139 1040 139 HOH HOH A . R 6 HOH 140 1041 140 HOH HOH A . R 6 HOH 141 1042 141 HOH HOH A . R 6 HOH 142 1043 142 HOH HOH A . R 6 HOH 143 1044 143 HOH HOH A . R 6 HOH 144 1045 144 HOH HOH A . R 6 HOH 145 1046 145 HOH HOH A . R 6 HOH 146 1047 146 HOH HOH A . R 6 HOH 147 1048 147 HOH HOH A . R 6 HOH 148 1049 148 HOH HOH A . R 6 HOH 149 1050 149 HOH HOH A . R 6 HOH 150 1051 150 HOH HOH A . R 6 HOH 151 1052 151 HOH HOH A . R 6 HOH 152 1053 152 HOH HOH A . R 6 HOH 153 1054 153 HOH HOH A . R 6 HOH 154 1055 154 HOH HOH A . R 6 HOH 155 1056 155 HOH HOH A . R 6 HOH 156 1057 156 HOH HOH A . R 6 HOH 157 1058 157 HOH HOH A . R 6 HOH 158 1059 158 HOH HOH A . R 6 HOH 159 1060 159 HOH HOH A . R 6 HOH 160 1061 160 HOH HOH A . R 6 HOH 161 1062 161 HOH HOH A . R 6 HOH 162 1063 162 HOH HOH A . R 6 HOH 163 1064 163 HOH HOH A . R 6 HOH 164 1065 164 HOH HOH A . R 6 HOH 165 1066 165 HOH HOH A . R 6 HOH 166 1067 166 HOH HOH A . R 6 HOH 167 1068 167 HOH HOH A . R 6 HOH 168 1069 168 HOH HOH A . R 6 HOH 169 1070 169 HOH HOH A . R 6 HOH 170 1071 170 HOH HOH A . R 6 HOH 171 1072 171 HOH HOH A . R 6 HOH 172 1073 172 HOH HOH A . R 6 HOH 173 1074 173 HOH HOH A . R 6 HOH 174 1075 174 HOH HOH A . R 6 HOH 175 1076 175 HOH HOH A . R 6 HOH 176 1077 176 HOH HOH A . R 6 HOH 177 1078 177 HOH HOH A . R 6 HOH 178 1079 178 HOH HOH A . R 6 HOH 179 1080 179 HOH HOH A . R 6 HOH 180 1081 180 HOH HOH A . R 6 HOH 181 1082 181 HOH HOH A . R 6 HOH 182 1083 182 HOH HOH A . R 6 HOH 183 1084 183 HOH HOH A . R 6 HOH 184 1085 184 HOH HOH A . R 6 HOH 185 1086 185 HOH HOH A . R 6 HOH 186 1087 186 HOH HOH A . R 6 HOH 187 1088 187 HOH HOH A . R 6 HOH 188 1089 188 HOH HOH A . R 6 HOH 189 1090 189 HOH HOH A . R 6 HOH 190 1091 190 HOH HOH A . R 6 HOH 191 1092 191 HOH HOH A . R 6 HOH 192 1093 192 HOH HOH A . R 6 HOH 193 1094 193 HOH HOH A . R 6 HOH 194 1095 194 HOH HOH A . R 6 HOH 195 1096 195 HOH HOH A . R 6 HOH 196 1097 196 HOH HOH A . R 6 HOH 197 1098 197 HOH HOH A . R 6 HOH 198 1099 198 HOH HOH A . R 6 HOH 199 1100 199 HOH HOH A . R 6 HOH 200 1101 200 HOH HOH A . R 6 HOH 201 1102 201 HOH HOH A . R 6 HOH 202 1103 202 HOH HOH A . R 6 HOH 203 1104 203 HOH HOH A . R 6 HOH 204 1105 204 HOH HOH A . R 6 HOH 205 1106 205 HOH HOH A . R 6 HOH 206 1107 206 HOH HOH A . R 6 HOH 207 1108 207 HOH HOH A . R 6 HOH 208 1109 208 HOH HOH A . R 6 HOH 209 1110 209 HOH HOH A . R 6 HOH 210 1111 210 HOH HOH A . R 6 HOH 211 1112 211 HOH HOH A . R 6 HOH 212 1113 212 HOH HOH A . R 6 HOH 213 1114 213 HOH HOH A . R 6 HOH 214 1115 214 HOH HOH A . R 6 HOH 215 1116 215 HOH HOH A . R 6 HOH 216 1117 216 HOH HOH A . R 6 HOH 217 1118 217 HOH HOH A . R 6 HOH 218 1119 218 HOH HOH A . R 6 HOH 219 1120 219 HOH HOH A . R 6 HOH 220 1121 220 HOH HOH A . R 6 HOH 221 1122 221 HOH HOH A . R 6 HOH 222 1123 222 HOH HOH A . R 6 HOH 223 1124 223 HOH HOH A . R 6 HOH 224 1125 224 HOH HOH A . R 6 HOH 225 1126 225 HOH HOH A . R 6 HOH 226 1127 226 HOH HOH A . R 6 HOH 227 1128 227 HOH HOH A . R 6 HOH 228 1129 228 HOH HOH A . R 6 HOH 229 1130 229 HOH HOH A . R 6 HOH 230 1131 230 HOH HOH A . R 6 HOH 231 1132 231 HOH HOH A . R 6 HOH 232 1133 232 HOH HOH A . R 6 HOH 233 1134 233 HOH HOH A . R 6 HOH 234 1135 234 HOH HOH A . R 6 HOH 235 1136 235 HOH HOH A . R 6 HOH 236 1137 236 HOH HOH A . R 6 HOH 237 1138 237 HOH HOH A . R 6 HOH 238 1139 238 HOH HOH A . R 6 HOH 239 1140 239 HOH HOH A . R 6 HOH 240 1141 240 HOH HOH A . R 6 HOH 241 1142 241 HOH HOH A . R 6 HOH 242 1143 242 HOH HOH A . R 6 HOH 243 1144 243 HOH HOH A . R 6 HOH 244 1145 244 HOH HOH A . R 6 HOH 245 1146 245 HOH HOH A . R 6 HOH 246 1147 246 HOH HOH A . R 6 HOH 247 1148 247 HOH HOH A . R 6 HOH 248 1149 248 HOH HOH A . R 6 HOH 249 1150 249 HOH HOH A . R 6 HOH 250 1151 250 HOH HOH A . R 6 HOH 251 1152 251 HOH HOH A . R 6 HOH 252 1153 252 HOH HOH A . R 6 HOH 253 1154 253 HOH HOH A . R 6 HOH 254 1155 254 HOH HOH A . R 6 HOH 255 1156 255 HOH HOH A . R 6 HOH 256 1157 256 HOH HOH A . R 6 HOH 257 1158 257 HOH HOH A . R 6 HOH 258 1159 258 HOH HOH A . R 6 HOH 259 1160 259 HOH HOH A . R 6 HOH 260 1161 260 HOH HOH A . R 6 HOH 261 1162 261 HOH HOH A . R 6 HOH 262 1163 262 HOH HOH A . R 6 HOH 263 1164 263 HOH HOH A . R 6 HOH 264 1165 264 HOH HOH A . R 6 HOH 265 1166 265 HOH HOH A . R 6 HOH 266 1167 266 HOH HOH A . R 6 HOH 267 1168 267 HOH HOH A . R 6 HOH 268 1169 268 HOH HOH A . R 6 HOH 269 1170 269 HOH HOH A . R 6 HOH 270 1171 270 HOH HOH A . R 6 HOH 271 1172 271 HOH HOH A . R 6 HOH 272 1173 272 HOH HOH A . R 6 HOH 273 1174 273 HOH HOH A . R 6 HOH 274 1175 274 HOH HOH A . R 6 HOH 275 1176 275 HOH HOH A . R 6 HOH 276 1177 276 HOH HOH A . R 6 HOH 277 1178 277 HOH HOH A . R 6 HOH 278 1179 278 HOH HOH A . R 6 HOH 279 1180 279 HOH HOH A . R 6 HOH 280 1181 280 HOH HOH A . R 6 HOH 281 1182 281 HOH HOH A . R 6 HOH 282 1183 282 HOH HOH A . R 6 HOH 283 1184 283 HOH HOH A . R 6 HOH 284 1185 284 HOH HOH A . R 6 HOH 285 1186 285 HOH HOH A . R 6 HOH 286 1187 286 HOH HOH A . R 6 HOH 287 1188 287 HOH HOH A . R 6 HOH 288 1189 288 HOH HOH A . R 6 HOH 289 1190 289 HOH HOH A . R 6 HOH 290 1191 290 HOH HOH A . R 6 HOH 291 1192 291 HOH HOH A . R 6 HOH 292 1193 292 HOH HOH A . R 6 HOH 293 1194 293 HOH HOH A . R 6 HOH 294 1195 294 HOH HOH A . R 6 HOH 295 1196 295 HOH HOH A . R 6 HOH 296 1197 296 HOH HOH A . R 6 HOH 297 1198 297 HOH HOH A . R 6 HOH 298 1199 298 HOH HOH A . R 6 HOH 299 1200 299 HOH HOH A . R 6 HOH 300 1201 300 HOH HOH A . R 6 HOH 301 1202 301 HOH HOH A . R 6 HOH 302 1203 302 HOH HOH A . R 6 HOH 303 1204 303 HOH HOH A . R 6 HOH 304 1205 304 HOH HOH A . R 6 HOH 305 1206 305 HOH HOH A . R 6 HOH 306 1207 306 HOH HOH A . R 6 HOH 307 1208 307 HOH HOH A . R 6 HOH 308 1209 308 HOH HOH A . R 6 HOH 309 1210 309 HOH HOH A . R 6 HOH 310 1211 310 HOH HOH A . R 6 HOH 311 1212 311 HOH HOH A . R 6 HOH 312 1213 312 HOH HOH A . R 6 HOH 313 1214 313 HOH HOH A . R 6 HOH 314 1215 314 HOH HOH A . R 6 HOH 315 1216 315 HOH HOH A . R 6 HOH 316 1217 316 HOH HOH A . R 6 HOH 317 1218 317 HOH HOH A . R 6 HOH 318 1219 318 HOH HOH A . R 6 HOH 319 1220 319 HOH HOH A . R 6 HOH 320 1221 320 HOH HOH A . R 6 HOH 321 1222 321 HOH HOH A . R 6 HOH 322 1223 322 HOH HOH A . R 6 HOH 323 1224 323 HOH HOH A . R 6 HOH 324 1225 324 HOH HOH A . R 6 HOH 325 1226 325 HOH HOH A . R 6 HOH 326 1227 326 HOH HOH A . R 6 HOH 327 1228 327 HOH HOH A . R 6 HOH 328 1229 328 HOH HOH A . R 6 HOH 329 1230 329 HOH HOH A . R 6 HOH 330 1231 330 HOH HOH A . R 6 HOH 331 1232 331 HOH HOH A . R 6 HOH 332 1233 332 HOH HOH A . R 6 HOH 333 1234 333 HOH HOH A . R 6 HOH 334 1235 334 HOH HOH A . R 6 HOH 335 1236 335 HOH HOH A . R 6 HOH 336 1237 336 HOH HOH A . R 6 HOH 337 1238 337 HOH HOH A . R 6 HOH 338 1239 338 HOH HOH A . R 6 HOH 339 1240 339 HOH HOH A . R 6 HOH 340 1241 340 HOH HOH A . R 6 HOH 341 1242 341 HOH HOH A . R 6 HOH 342 1243 342 HOH HOH A . R 6 HOH 343 1244 343 HOH HOH A . R 6 HOH 344 1245 344 HOH HOH A . R 6 HOH 345 1246 345 HOH HOH A . R 6 HOH 346 1247 346 HOH HOH A . R 6 HOH 347 1248 347 HOH HOH A . R 6 HOH 348 1249 348 HOH HOH A . R 6 HOH 349 1250 349 HOH HOH A . R 6 HOH 350 1251 350 HOH HOH A . R 6 HOH 351 1252 351 HOH HOH A . R 6 HOH 352 1253 352 HOH HOH A . R 6 HOH 353 1254 353 HOH HOH A . R 6 HOH 354 1255 354 HOH HOH A . R 6 HOH 355 1256 355 HOH HOH A . R 6 HOH 356 1257 356 HOH HOH A . R 6 HOH 357 1258 357 HOH HOH A . R 6 HOH 358 1259 358 HOH HOH A . R 6 HOH 359 1260 359 HOH HOH A . R 6 HOH 360 1261 360 HOH HOH A . R 6 HOH 361 1262 361 HOH HOH A . R 6 HOH 362 1263 362 HOH HOH A . R 6 HOH 363 1264 363 HOH HOH A . R 6 HOH 364 1265 364 HOH HOH A . R 6 HOH 365 1266 365 HOH HOH A . R 6 HOH 366 1267 366 HOH HOH A . R 6 HOH 367 1268 367 HOH HOH A . R 6 HOH 368 1269 368 HOH HOH A . R 6 HOH 369 1270 369 HOH HOH A . R 6 HOH 370 1271 370 HOH HOH A . R 6 HOH 371 1272 371 HOH HOH A . R 6 HOH 372 1273 372 HOH HOH A . R 6 HOH 373 1274 373 HOH HOH A . R 6 HOH 374 1275 374 HOH HOH A . R 6 HOH 375 1276 375 HOH HOH A . R 6 HOH 376 1277 376 HOH HOH A . R 6 HOH 377 1278 377 HOH HOH A . R 6 HOH 378 1279 378 HOH HOH A . R 6 HOH 379 1280 379 HOH HOH A . R 6 HOH 380 1281 380 HOH HOH A . R 6 HOH 381 1282 381 HOH HOH A . R 6 HOH 382 1283 382 HOH HOH A . R 6 HOH 383 1284 383 HOH HOH A . R 6 HOH 384 1285 384 HOH HOH A . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 71 A ASN 71 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 157 A ASN 157 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 215 A ASN 215 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 334 A ASN 334 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_defined_assembly _pdbx_struct_assembly.method_details ? _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _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 2004-10-12 2 'Structure model' 1 1 2008-04-30 3 'Structure model' 1 2 2011-07-13 # _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 ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Non-polymer description' 3 3 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.0 ? 1 DENZO 'data reduction' . ? 2 SCALEPACK 'data scaling' . ? 3 AMoRE phasing . ? 4 # _pdbx_database_remark.id 999 _pdbx_database_remark.text ;SEQUENCE Leu37, Pro70, Ala72, Ala88, Asn148, Phe151, Lys153, Thr161, Asp165, Thr167, Gly185, His196, Met202, Gln207, Ser216, Asp225, Asn230, Arg236, Leu238, Leu240, Leu245, Asp249, Met258, Asn297, Asn300, Ile327, Val335, Tyr337, Phe341, Val355, Ile360, Ala362, Thr363, Asn369, His378, Ser386, Asp389, Ala398, Gln415, Arg416 differ from the sequence database. These residues were used on the basis of the electron density map. The difference may be due to the use of different strains of Trichoderma reesei for sequencing and for the X-ray structure. ; # 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 OD1 A ASP 226 ? ? O2 A GAL 901 ? ? 2.09 2 1 O6 A BMA 602 ? ? O5 A MAN 604 ? ? 2.11 3 1 O A HOH 1011 ? ? O A HOH 1283 ? ? 2.15 # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 CB A ASP 27 ? ? CG A ASP 27 ? ? OD2 A ASP 27 ? ? 125.06 118.30 6.76 0.90 N 2 1 CB A ASP 61 ? ? CG A ASP 61 ? ? OD2 A ASP 61 ? ? 123.92 118.30 5.62 0.90 N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 VAL A 7 ? ? -139.03 -35.04 2 1 HIS A 23 ? ? 46.38 -128.11 3 1 ASP A 54 ? ? -99.10 -149.83 4 1 CYS A 56 ? ? 86.56 20.22 5 1 ASP A 257 ? ? 79.83 172.11 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 BETA-D-MANNOSE BMA 4 ALPHA-D-MANNOSE MAN 5 BETA-D-GALACTOSE GAL 6 water HOH #