data_5KAR # _entry.id 5KAR # _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 5KAR WWPDB D_1000221967 # _pdbx_database_related.content_type unspecified _pdbx_database_related.db_id 5KAS _pdbx_database_related.db_name PDB _pdbx_database_related.details . # _pdbx_database_status.status_code REL _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.entry_id 5KAR _pdbx_database_status.recvd_initial_deposition_date 2016-06-02 _pdbx_database_status.SG_entry N _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Gorelik, A.' 1 'Illes, K.' 2 'Heinz, L.X.' 3 'Superti-Furga, G.' 4 'Nagar, B.' 5 # _citation.abstract ? _citation.abstract_id_CAS ? _citation.book_id_ISBN ? _citation.book_publisher ? _citation.book_publisher_city ? _citation.book_title ? _citation.coordinate_linkage ? _citation.country US _citation.database_id_Medline ? _citation.details ? _citation.id primary _citation.journal_abbrev J.Biol.Chem. _citation.journal_id_ASTM JBCHA3 _citation.journal_id_CSD 0071 _citation.journal_id_ISSN 1083-351X _citation.journal_full ? _citation.journal_issue ? _citation.journal_volume 291 _citation.language ? _citation.page_first 24054 _citation.page_last 24064 _citation.title ;Crystal Structure of the Acid Sphingomyelinase-like Phosphodiesterase SMPDL3B Provides Insights into Determinants of Substrate Specificity. ; _citation.year 2016 _citation.database_id_CSD ? _citation.pdbx_database_id_DOI 10.1074/jbc.M116.755801 _citation.pdbx_database_id_PubMed 27687724 _citation.unpublished_flag ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Gorelik, A.' 1 primary 'Heinz, L.X.' 2 primary 'Illes, K.' 3 primary 'Superti-Furga, G.' 4 primary 'Nagar, B.' 5 # _cell.angle_alpha 90.00 _cell.angle_alpha_esd ? _cell.angle_beta 98.07 _cell.angle_beta_esd ? _cell.angle_gamma 90.00 _cell.angle_gamma_esd ? _cell.entry_id 5KAR _cell.details ? _cell.formula_units_Z ? _cell.length_a 50.892 _cell.length_a_esd ? _cell.length_b 47.031 _cell.length_b_esd ? _cell.length_c 93.861 _cell.length_c_esd ? _cell.volume ? _cell.volume_esd ? _cell.Z_PDB 2 _cell.reciprocal_angle_alpha ? _cell.reciprocal_angle_beta ? _cell.reciprocal_angle_gamma ? _cell.reciprocal_angle_alpha_esd ? _cell.reciprocal_angle_beta_esd ? _cell.reciprocal_angle_gamma_esd ? _cell.reciprocal_length_a ? _cell.reciprocal_length_b ? _cell.reciprocal_length_c ? _cell.reciprocal_length_a_esd ? _cell.reciprocal_length_b_esd ? _cell.reciprocal_length_c_esd ? _cell.pdbx_unique_axis ? # _symmetry.entry_id 5KAR _symmetry.cell_setting ? _symmetry.Int_Tables_number 3 _symmetry.space_group_name_Hall ? _symmetry.space_group_name_H-M 'P 1 2 1' _symmetry.pdbx_full_space_group_name_H-M ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man 'Acid sphingomyelinase-like phosphodiesterase 3b' 48814.629 1 3.1.4.- ? 'UNP residues 19-435' ? 2 non-polymer syn 'ZINC ION' 65.409 2 ? ? ? ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 6 ? ? ? ? 4 non-polymer man BETA-D-MANNOSE 180.156 1 ? ? ? ? 5 non-polymer man ALPHA-D-MANNOSE 180.156 2 ? ? ? ? 6 non-polymer man ALPHA-L-FUCOSE 164.156 1 ? ? ? ? 7 non-polymer syn 'NITRATE ION' 62.005 2 ? ? ? ? 8 non-polymer syn GLYCEROL 92.094 1 ? ? ? ? 9 water nat water 18.015 496 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'ASM-like phosphodiesterase 3b' # _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 ;DRHHHHHHKLQLGRFWHISDLHLDPNYTVSKDPLQVCPSAGSQPVLNAGPWGDYLCDSPWALINSSLYAMKEIEPKPDFI LWTGDDTPHVPNESLGEAAVLAIVERLTNLIKEVFPDTKVYAALGNHDFHPKNQFPAQSNRIYNQVAELWRPWLSNESYA LFKRGAFYSEKLPGPSRAGRVVVLNTNLYYSNNEQTAGMADPGEQFRWLGDVLSNASRDGEMVYVIGHVPPGFFEKTQNK AWFRESFNEEYLKVIQKHHRVIAGQFFGHHHTDSFRMFYDNTGAPINVMFLTPGVTPWKTTLPGVVDGANNPGIRIFEYD RATLNLKDLVTYFLNLRQANVQETPRWEQEYRLTEAYQVPDASVSSMHTALTRIASEPHILQRYYVYNSVSYNHLTCEDS CRIEHVCAIQHVAFNTYATCLHGLGAK ; _entity_poly.pdbx_seq_one_letter_code_can ;DRHHHHHHKLQLGRFWHISDLHLDPNYTVSKDPLQVCPSAGSQPVLNAGPWGDYLCDSPWALINSSLYAMKEIEPKPDFI LWTGDDTPHVPNESLGEAAVLAIVERLTNLIKEVFPDTKVYAALGNHDFHPKNQFPAQSNRIYNQVAELWRPWLSNESYA LFKRGAFYSEKLPGPSRAGRVVVLNTNLYYSNNEQTAGMADPGEQFRWLGDVLSNASRDGEMVYVIGHVPPGFFEKTQNK AWFRESFNEEYLKVIQKHHRVIAGQFFGHHHTDSFRMFYDNTGAPINVMFLTPGVTPWKTTLPGVVDGANNPGIRIFEYD RATLNLKDLVTYFLNLRQANVQETPRWEQEYRLTEAYQVPDASVSSMHTALTRIASEPHILQRYYVYNSVSYNHLTCEDS CRIEHVCAIQHVAFNTYATCLHGLGAK ; _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 ASP n 1 2 ARG n 1 3 HIS n 1 4 HIS n 1 5 HIS n 1 6 HIS n 1 7 HIS n 1 8 HIS n 1 9 LYS n 1 10 LEU n 1 11 GLN n 1 12 LEU n 1 13 GLY n 1 14 ARG n 1 15 PHE n 1 16 TRP n 1 17 HIS n 1 18 ILE n 1 19 SER n 1 20 ASP n 1 21 LEU n 1 22 HIS n 1 23 LEU n 1 24 ASP n 1 25 PRO n 1 26 ASN n 1 27 TYR n 1 28 THR n 1 29 VAL n 1 30 SER n 1 31 LYS n 1 32 ASP n 1 33 PRO n 1 34 LEU n 1 35 GLN n 1 36 VAL n 1 37 CYS n 1 38 PRO n 1 39 SER n 1 40 ALA n 1 41 GLY n 1 42 SER n 1 43 GLN n 1 44 PRO n 1 45 VAL n 1 46 LEU n 1 47 ASN n 1 48 ALA n 1 49 GLY n 1 50 PRO n 1 51 TRP n 1 52 GLY n 1 53 ASP n 1 54 TYR n 1 55 LEU n 1 56 CYS n 1 57 ASP n 1 58 SER n 1 59 PRO n 1 60 TRP n 1 61 ALA n 1 62 LEU n 1 63 ILE n 1 64 ASN n 1 65 SER n 1 66 SER n 1 67 LEU n 1 68 TYR n 1 69 ALA n 1 70 MET n 1 71 LYS n 1 72 GLU n 1 73 ILE n 1 74 GLU n 1 75 PRO n 1 76 LYS n 1 77 PRO n 1 78 ASP n 1 79 PHE n 1 80 ILE n 1 81 LEU n 1 82 TRP n 1 83 THR n 1 84 GLY n 1 85 ASP n 1 86 ASP n 1 87 THR n 1 88 PRO n 1 89 HIS n 1 90 VAL n 1 91 PRO n 1 92 ASN n 1 93 GLU n 1 94 SER n 1 95 LEU n 1 96 GLY n 1 97 GLU n 1 98 ALA n 1 99 ALA n 1 100 VAL n 1 101 LEU n 1 102 ALA n 1 103 ILE n 1 104 VAL n 1 105 GLU n 1 106 ARG n 1 107 LEU n 1 108 THR n 1 109 ASN n 1 110 LEU n 1 111 ILE n 1 112 LYS n 1 113 GLU n 1 114 VAL n 1 115 PHE n 1 116 PRO n 1 117 ASP n 1 118 THR n 1 119 LYS n 1 120 VAL n 1 121 TYR n 1 122 ALA n 1 123 ALA n 1 124 LEU n 1 125 GLY n 1 126 ASN n 1 127 HIS n 1 128 ASP n 1 129 PHE n 1 130 HIS n 1 131 PRO n 1 132 LYS n 1 133 ASN n 1 134 GLN n 1 135 PHE n 1 136 PRO n 1 137 ALA n 1 138 GLN n 1 139 SER n 1 140 ASN n 1 141 ARG n 1 142 ILE n 1 143 TYR n 1 144 ASN n 1 145 GLN n 1 146 VAL n 1 147 ALA n 1 148 GLU n 1 149 LEU n 1 150 TRP n 1 151 ARG n 1 152 PRO n 1 153 TRP n 1 154 LEU n 1 155 SER n 1 156 ASN n 1 157 GLU n 1 158 SER n 1 159 TYR n 1 160 ALA n 1 161 LEU n 1 162 PHE n 1 163 LYS n 1 164 ARG n 1 165 GLY n 1 166 ALA n 1 167 PHE n 1 168 TYR n 1 169 SER n 1 170 GLU n 1 171 LYS n 1 172 LEU n 1 173 PRO n 1 174 GLY n 1 175 PRO n 1 176 SER n 1 177 ARG n 1 178 ALA n 1 179 GLY n 1 180 ARG n 1 181 VAL n 1 182 VAL n 1 183 VAL n 1 184 LEU n 1 185 ASN n 1 186 THR n 1 187 ASN n 1 188 LEU n 1 189 TYR n 1 190 TYR n 1 191 SER n 1 192 ASN n 1 193 ASN n 1 194 GLU n 1 195 GLN n 1 196 THR n 1 197 ALA n 1 198 GLY n 1 199 MET n 1 200 ALA n 1 201 ASP n 1 202 PRO n 1 203 GLY n 1 204 GLU n 1 205 GLN n 1 206 PHE n 1 207 ARG n 1 208 TRP n 1 209 LEU n 1 210 GLY n 1 211 ASP n 1 212 VAL n 1 213 LEU n 1 214 SER n 1 215 ASN n 1 216 ALA n 1 217 SER n 1 218 ARG n 1 219 ASP n 1 220 GLY n 1 221 GLU n 1 222 MET n 1 223 VAL n 1 224 TYR n 1 225 VAL n 1 226 ILE n 1 227 GLY n 1 228 HIS n 1 229 VAL n 1 230 PRO n 1 231 PRO n 1 232 GLY n 1 233 PHE n 1 234 PHE n 1 235 GLU n 1 236 LYS n 1 237 THR n 1 238 GLN n 1 239 ASN n 1 240 LYS n 1 241 ALA n 1 242 TRP n 1 243 PHE n 1 244 ARG n 1 245 GLU n 1 246 SER n 1 247 PHE n 1 248 ASN n 1 249 GLU n 1 250 GLU n 1 251 TYR n 1 252 LEU n 1 253 LYS n 1 254 VAL n 1 255 ILE n 1 256 GLN n 1 257 LYS n 1 258 HIS n 1 259 HIS n 1 260 ARG n 1 261 VAL n 1 262 ILE n 1 263 ALA n 1 264 GLY n 1 265 GLN n 1 266 PHE n 1 267 PHE n 1 268 GLY n 1 269 HIS n 1 270 HIS n 1 271 HIS n 1 272 THR n 1 273 ASP n 1 274 SER n 1 275 PHE n 1 276 ARG n 1 277 MET n 1 278 PHE n 1 279 TYR n 1 280 ASP n 1 281 ASN n 1 282 THR n 1 283 GLY n 1 284 ALA n 1 285 PRO n 1 286 ILE n 1 287 ASN n 1 288 VAL n 1 289 MET n 1 290 PHE n 1 291 LEU n 1 292 THR n 1 293 PRO n 1 294 GLY n 1 295 VAL n 1 296 THR n 1 297 PRO n 1 298 TRP n 1 299 LYS n 1 300 THR n 1 301 THR n 1 302 LEU n 1 303 PRO n 1 304 GLY n 1 305 VAL n 1 306 VAL n 1 307 ASP n 1 308 GLY n 1 309 ALA n 1 310 ASN n 1 311 ASN n 1 312 PRO n 1 313 GLY n 1 314 ILE n 1 315 ARG n 1 316 ILE n 1 317 PHE n 1 318 GLU n 1 319 TYR n 1 320 ASP n 1 321 ARG n 1 322 ALA n 1 323 THR n 1 324 LEU n 1 325 ASN n 1 326 LEU n 1 327 LYS n 1 328 ASP n 1 329 LEU n 1 330 VAL n 1 331 THR n 1 332 TYR n 1 333 PHE n 1 334 LEU n 1 335 ASN n 1 336 LEU n 1 337 ARG n 1 338 GLN n 1 339 ALA n 1 340 ASN n 1 341 VAL n 1 342 GLN n 1 343 GLU n 1 344 THR n 1 345 PRO n 1 346 ARG n 1 347 TRP n 1 348 GLU n 1 349 GLN n 1 350 GLU n 1 351 TYR n 1 352 ARG n 1 353 LEU n 1 354 THR n 1 355 GLU n 1 356 ALA n 1 357 TYR n 1 358 GLN n 1 359 VAL n 1 360 PRO n 1 361 ASP n 1 362 ALA n 1 363 SER n 1 364 VAL n 1 365 SER n 1 366 SER n 1 367 MET n 1 368 HIS n 1 369 THR n 1 370 ALA n 1 371 LEU n 1 372 THR n 1 373 ARG n 1 374 ILE n 1 375 ALA n 1 376 SER n 1 377 GLU n 1 378 PRO n 1 379 HIS n 1 380 ILE n 1 381 LEU n 1 382 GLN n 1 383 ARG n 1 384 TYR n 1 385 TYR n 1 386 VAL n 1 387 TYR n 1 388 ASN n 1 389 SER n 1 390 VAL n 1 391 SER n 1 392 TYR n 1 393 ASN n 1 394 HIS n 1 395 LEU n 1 396 THR n 1 397 CYS n 1 398 GLU n 1 399 ASP n 1 400 SER n 1 401 CYS n 1 402 ARG n 1 403 ILE n 1 404 GLU n 1 405 HIS n 1 406 VAL n 1 407 CYS n 1 408 ALA n 1 409 ILE n 1 410 GLN n 1 411 HIS n 1 412 VAL n 1 413 ALA n 1 414 PHE n 1 415 ASN n 1 416 THR n 1 417 TYR n 1 418 ALA n 1 419 THR n 1 420 CYS n 1 421 LEU n 1 422 HIS n 1 423 GLY n 1 424 LEU n 1 425 GLY n 1 426 ALA n 1 427 LYS n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type 'Biological sequence' _entity_src_gen.pdbx_beg_seq_num 1 _entity_src_gen.pdbx_end_seq_num 427 _entity_src_gen.gene_src_common_name Mouse _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene 'Smpdl3b, Asml3b' _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'Mus musculus' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 10090 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name 'fall armyworm' _entity_src_gen.pdbx_host_org_scientific_name 'Spodoptera frugiperda' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 7108 _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type baculovirus _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code ASM3B_MOUSE _struct_ref.pdbx_db_accession P58242 _struct_ref.pdbx_db_isoform ? _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;QLGRFWHISDLHLDPNYTVSKDPLQVCPSAGSQPVLNAGPWGDYLCDSPWALINSSLYAMKEIEPKPDFILWTGDDTPHV PNESLGEAAVLAIVERLTNLIKEVFPDTKVYAALGNHDFHPKNQFPAQSNRIYNQVAELWRPWLSNESYALFKRGAFYSE KLPGPSRAGRVVVLNTNLYYSNNEQTAGMADPGEQFRWLGDVLSNASRDGEMVYVIGHVPPGFFEKTQNKAWFRESFNEE YLKVIQKHHRVIAGQFFGHHHTDSFRMFYDNTGAPINVMFLTPGVTPWKTTLPGVVDGANNPGIRIFEYDRATLNLKDLV TYFLNLRQANVQETPRWEQEYRLTEAYQVPDASVSSMHTALTRIASEPHILQRYYVYNSVSYNHLTCEDSCRIEHVCAIQ HVAFNTYATCLHGLGAK ; _struct_ref.pdbx_align_begin 19 # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 5KAR _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 11 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 427 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession P58242 _struct_ref_seq.db_align_beg 19 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 435 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 19 _struct_ref_seq.pdbx_auth_seq_align_end 435 # 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 5KAR ASP A 1 ? UNP P58242 ? ? 'expression tag' 9 1 1 5KAR ARG A 2 ? UNP P58242 ? ? 'expression tag' 10 2 1 5KAR HIS A 3 ? UNP P58242 ? ? 'expression tag' 11 3 1 5KAR HIS A 4 ? UNP P58242 ? ? 'expression tag' 12 4 1 5KAR HIS A 5 ? UNP P58242 ? ? 'expression tag' 13 5 1 5KAR HIS A 6 ? UNP P58242 ? ? 'expression tag' 14 6 1 5KAR HIS A 7 ? UNP P58242 ? ? 'expression tag' 15 7 1 5KAR HIS A 8 ? UNP P58242 ? ? 'expression tag' 16 8 1 5KAR LYS A 9 ? UNP P58242 ? ? 'expression tag' 17 9 1 5KAR LEU A 10 ? UNP P58242 ? ? 'expression tag' 18 10 # 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 FUC saccharide . ALPHA-L-FUCOSE ? 'C6 H12 O5' 164.156 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 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 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 NO3 non-polymer . 'NITRATE ION' ? 'N O3 -1' 62.005 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 ZN non-polymer . 'ZINC ION' ? 'Zn 2' 65.409 # _exptl.absorpt_coefficient_mu ? _exptl.absorpt_correction_T_max ? _exptl.absorpt_correction_T_min ? _exptl.absorpt_correction_type ? _exptl.absorpt_process_details ? _exptl.entry_id 5KAR _exptl.crystals_number 1 _exptl.details ? _exptl.method 'X-RAY DIFFRACTION' _exptl.method_details ? # _exptl_crystal.colour ? _exptl_crystal.density_diffrn ? _exptl_crystal.density_Matthews 2.28 _exptl_crystal.density_method ? _exptl_crystal.density_percent_sol 46.01 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.id 1 _exptl_crystal.preparation ? _exptl_crystal.size_max ? _exptl_crystal.size_mid ? _exptl_crystal.size_min ? _exptl_crystal.size_rad ? _exptl_crystal.colour_lustre ? _exptl_crystal.colour_modifier ? _exptl_crystal.colour_primary ? _exptl_crystal.density_meas ? _exptl_crystal.density_meas_esd ? _exptl_crystal.density_meas_gt ? _exptl_crystal.density_meas_lt ? _exptl_crystal.density_meas_temp ? _exptl_crystal.density_meas_temp_esd ? _exptl_crystal.density_meas_temp_gt ? _exptl_crystal.density_meas_temp_lt ? _exptl_crystal.pdbx_crystal_image_url ? _exptl_crystal.pdbx_crystal_image_format ? _exptl_crystal.pdbx_mosaicity ? _exptl_crystal.pdbx_mosaicity_esd ? # _exptl_crystal_grow.apparatus ? _exptl_crystal_grow.atmosphere ? _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.details ? _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.method_ref ? _exptl_crystal_grow.pH ? _exptl_crystal_grow.pressure ? _exptl_crystal_grow.pressure_esd ? _exptl_crystal_grow.seeding ? _exptl_crystal_grow.seeding_ref ? _exptl_crystal_grow.temp 295 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.temp_esd ? _exptl_crystal_grow.time ? _exptl_crystal_grow.pdbx_details 'PEG 3350, ammonium nitrate' _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.ambient_environment ? _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.ambient_temp_esd ? _diffrn.crystal_id 1 _diffrn.crystal_support ? _diffrn.crystal_treatment ? _diffrn.details ? _diffrn.id 1 _diffrn.ambient_pressure ? _diffrn.ambient_pressure_esd ? _diffrn.ambient_pressure_gt ? _diffrn.ambient_pressure_lt ? _diffrn.ambient_temp_gt ? _diffrn.ambient_temp_lt ? # _diffrn_detector.details ? _diffrn_detector.detector CCD _diffrn_detector.diffrn_id 1 _diffrn_detector.type 'ADSC QUANTUM 270' _diffrn_detector.area_resol_mean ? _diffrn_detector.dtime ? _diffrn_detector.pdbx_frames_total ? _diffrn_detector.pdbx_collection_time_total ? _diffrn_detector.pdbx_collection_date 2013-11-14 # _diffrn_radiation.collimation ? _diffrn_radiation.diffrn_id 1 _diffrn_radiation.filter_edge ? _diffrn_radiation.inhomogeneity ? _diffrn_radiation.monochromator ? _diffrn_radiation.polarisn_norm ? _diffrn_radiation.polarisn_ratio ? _diffrn_radiation.probe ? _diffrn_radiation.type ? _diffrn_radiation.xray_symbol ? _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.pdbx_wavelength_list ? _diffrn_radiation.pdbx_wavelength ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_analyzer ? _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.9179 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.current ? _diffrn_source.details ? _diffrn_source.diffrn_id 1 _diffrn_source.power ? _diffrn_source.size ? _diffrn_source.source SYNCHROTRON _diffrn_source.target ? _diffrn_source.type 'CHESS BEAMLINE F1' _diffrn_source.voltage ? _diffrn_source.take-off_angle ? _diffrn_source.pdbx_wavelength_list 0.9179 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_synchrotron_beamline F1 _diffrn_source.pdbx_synchrotron_site CHESS # _reflns.B_iso_Wilson_estimate ? _reflns.entry_id 5KAR _reflns.data_reduction_details ? _reflns.data_reduction_method ? _reflns.d_resolution_high 1.14 _reflns.d_resolution_low 36.833 _reflns.details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.number_all ? _reflns.number_obs 147638 _reflns.observed_criterion ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.observed_criterion_I_max ? _reflns.observed_criterion_I_min ? _reflns.observed_criterion_sigma_F ? _reflns.observed_criterion_sigma_I ? _reflns.percent_possible_obs 92.9 _reflns.R_free_details ? _reflns.Rmerge_F_all ? _reflns.Rmerge_F_obs ? _reflns.Friedel_coverage ? _reflns.number_gt ? _reflns.threshold_expression ? _reflns.pdbx_redundancy 5.9 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rmerge_I_all ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_av_sigmaI ? _reflns.pdbx_netI_over_sigmaI 17.4 _reflns.pdbx_res_netI_over_av_sigmaI_2 ? _reflns.pdbx_res_netI_over_sigmaI_2 ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_d_res_high_opt ? _reflns.pdbx_d_res_low_opt ? _reflns.pdbx_d_res_opt_method ? _reflns.phase_calculation_details ? _reflns.pdbx_Rrim_I_all ? _reflns.pdbx_Rpim_I_all ? _reflns.pdbx_d_opt ? _reflns.pdbx_number_measured_all ? _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.pdbx_CC_half ? _reflns.pdbx_R_split ? # _reflns_shell.d_res_high . _reflns_shell.d_res_low ? _reflns_shell.meanI_over_sigI_all ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_possible ? _reflns_shell.number_unique_all ? _reflns_shell.number_unique_obs ? _reflns_shell.percent_possible_all ? _reflns_shell.percent_possible_obs ? _reflns_shell.Rmerge_F_all ? _reflns_shell.Rmerge_F_obs ? _reflns_shell.Rmerge_I_all ? _reflns_shell.Rmerge_I_obs ? _reflns_shell.meanI_over_sigI_gt ? _reflns_shell.meanI_over_uI_all ? _reflns_shell.meanI_over_uI_gt ? _reflns_shell.number_measured_gt ? _reflns_shell.number_unique_gt ? _reflns_shell.percent_possible_gt ? _reflns_shell.Rmerge_F_gt ? _reflns_shell.Rmerge_I_gt ? _reflns_shell.pdbx_redundancy ? _reflns_shell.pdbx_Rsym_value ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_netI_over_sigmaI_all ? _reflns_shell.pdbx_netI_over_sigmaI_obs ? _reflns_shell.pdbx_Rrim_I_all ? _reflns_shell.pdbx_Rpim_I_all ? _reflns_shell.pdbx_rejects ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_CC_half ? _reflns_shell.pdbx_R_split ? # _refine.aniso_B[1][1] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][2] ? _refine.aniso_B[2][3] ? _refine.aniso_B[3][3] ? _refine.B_iso_max ? _refine.B_iso_mean ? _refine.B_iso_min ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.details ? _refine.diff_density_max ? _refine.diff_density_max_esd ? _refine.diff_density_min ? _refine.diff_density_min_esd ? _refine.diff_density_rms ? _refine.diff_density_rms_esd ? _refine.entry_id 5KAR _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.ls_abs_structure_details ? _refine.ls_abs_structure_Flack ? _refine.ls_abs_structure_Flack_esd ? _refine.ls_abs_structure_Rogers ? _refine.ls_abs_structure_Rogers_esd ? _refine.ls_d_res_high 1.142 _refine.ls_d_res_low 36.833 _refine.ls_extinction_coef ? _refine.ls_extinction_coef_esd ? _refine.ls_extinction_expression ? _refine.ls_extinction_method ? _refine.ls_goodness_of_fit_all ? _refine.ls_goodness_of_fit_all_esd ? _refine.ls_goodness_of_fit_obs ? _refine.ls_goodness_of_fit_obs_esd ? _refine.ls_hydrogen_treatment ? _refine.ls_matrix_type ? _refine.ls_number_constraints ? _refine.ls_number_parameters ? _refine.ls_number_reflns_all ? _refine.ls_number_reflns_obs 147421 _refine.ls_number_reflns_R_free 7396 _refine.ls_number_reflns_R_work ? _refine.ls_number_restraints ? _refine.ls_percent_reflns_obs 92.60 _refine.ls_percent_reflns_R_free 5.02 _refine.ls_R_factor_all ? _refine.ls_R_factor_obs 0.1355 _refine.ls_R_factor_R_free 0.1518 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_R_factor_R_work 0.1346 _refine.ls_R_Fsqd_factor_obs ? _refine.ls_R_I_factor_obs ? _refine.ls_redundancy_reflns_all ? _refine.ls_redundancy_reflns_obs ? _refine.ls_restrained_S_all ? _refine.ls_restrained_S_obs ? _refine.ls_shift_over_esd_max ? _refine.ls_shift_over_esd_mean ? _refine.ls_structure_factor_coef ? _refine.ls_weighting_details ? _refine.ls_weighting_scheme ? _refine.ls_wR_factor_all ? _refine.ls_wR_factor_obs ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.occupancy_max ? _refine.occupancy_min ? _refine.solvent_model_details ? _refine.solvent_model_param_bsol ? _refine.solvent_model_param_ksol ? _refine.ls_R_factor_gt ? _refine.ls_goodness_of_fit_gt ? _refine.ls_goodness_of_fit_ref ? _refine.ls_shift_over_su_max ? _refine.ls_shift_over_su_max_lt ? _refine.ls_shift_over_su_mean ? _refine.ls_shift_over_su_mean_lt ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 1.34 _refine.pdbx_ls_sigma_Fsqd ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_ls_cross_valid_method 'FREE R-VALUE' _refine.pdbx_method_to_determine_struct SAD _refine.pdbx_starting_model ? _refine.pdbx_stereochemistry_target_values ? _refine.pdbx_R_Free_selection_details ? _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.pdbx_solvent_vdw_probe_radii 1.11 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.90 _refine.pdbx_real_space_R ? _refine.pdbx_density_correlation ? _refine.pdbx_pd_number_of_powder_patterns ? _refine.pdbx_pd_number_of_points ? _refine.pdbx_pd_meas_number_of_points ? _refine.pdbx_pd_proc_ls_prof_R_factor ? _refine.pdbx_pd_proc_ls_prof_wR_factor ? _refine.pdbx_pd_Marquardt_correlation_coeff ? _refine.pdbx_pd_Fsqrd_R_factor ? _refine.pdbx_pd_ls_matrix_band_width ? _refine.pdbx_overall_phase_error 17.05 _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_diffrn_id 1 _refine.overall_SU_B ? _refine.overall_SU_ML 0.12 _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_average_fsc_overall ? _refine.pdbx_average_fsc_work ? _refine.pdbx_average_fsc_free ? # _refine_analyze.entry_id 5KAR _refine_analyze.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_analyze.Luzzati_coordinate_error_free ? _refine_analyze.Luzzati_coordinate_error_obs ? _refine_analyze.Luzzati_d_res_low_free ? _refine_analyze.Luzzati_d_res_low_obs ? _refine_analyze.Luzzati_sigma_a_free ? _refine_analyze.Luzzati_sigma_a_free_details ? _refine_analyze.Luzzati_sigma_a_obs ? _refine_analyze.Luzzati_sigma_a_obs_details ? _refine_analyze.number_disordered_residues ? _refine_analyze.occupancy_sum_hydrogen ? _refine_analyze.occupancy_sum_non_hydrogen ? _refine_analyze.RG_d_res_high ? _refine_analyze.RG_d_res_low ? _refine_analyze.RG_free ? _refine_analyze.RG_work ? _refine_analyze.RG_free_work_ratio ? _refine_analyze.pdbx_Luzzati_d_res_high_obs ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 3320 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 143 _refine_hist.number_atoms_solvent 496 _refine_hist.number_atoms_total 3959 _refine_hist.d_res_high 1.142 _refine_hist.d_res_low 36.833 # loop_ _refine_ls_restr.pdbx_refine_id _refine_ls_restr.criterion _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.number _refine_ls_restr.rejects _refine_ls_restr.type _refine_ls_restr.weight _refine_ls_restr.pdbx_restraint_function 'X-RAY DIFFRACTION' ? 0.009 ? 3649 ? f_bond_d ? ? 'X-RAY DIFFRACTION' ? 1.067 ? 5019 ? f_angle_d ? ? 'X-RAY DIFFRACTION' ? 13.564 ? 1363 ? f_dihedral_angle_d ? ? 'X-RAY DIFFRACTION' ? 0.083 ? 562 ? f_chiral_restr ? ? 'X-RAY DIFFRACTION' ? 0.009 ? 641 ? f_plane_restr ? ? # loop_ _refine_ls_shell.pdbx_refine_id _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.number_reflns_all _refine_ls_shell.number_reflns_obs _refine_ls_shell.number_reflns_R_free _refine_ls_shell.number_reflns_R_work _refine_ls_shell.percent_reflns_obs _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.R_factor_all _refine_ls_shell.R_factor_obs _refine_ls_shell.R_factor_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.R_factor_R_work _refine_ls_shell.redundancy_reflns_all _refine_ls_shell.redundancy_reflns_obs _refine_ls_shell.wR_factor_all _refine_ls_shell.wR_factor_obs _refine_ls_shell.wR_factor_R_free _refine_ls_shell.wR_factor_R_work _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.pdbx_phase_error _refine_ls_shell.pdbx_fsc_work _refine_ls_shell.pdbx_fsc_free 'X-RAY DIFFRACTION' 1.1421 1.1551 . . 118 2259 45.00 . . . 0.3742 . 0.3731 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.1551 1.1687 . . 142 2676 54.00 . . . 0.3603 . 0.3600 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.1687 1.1830 . . 165 3171 63.00 . . . 0.3478 . 0.3377 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.1830 1.1979 . . 189 3600 72.00 . . . 0.3103 . 0.3060 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.1979 1.2137 . . 209 3948 78.00 . . . 0.2863 . 0.2889 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.2137 1.2303 . . 228 4299 86.00 . . . 0.2931 . 0.2664 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.2303 1.2479 . . 245 4633 92.00 . . . 0.2941 . 0.2509 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.2479 1.2665 . . 259 4903 98.00 . . . 0.2467 . 0.2239 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.2665 1.2863 . . 261 4935 98.00 . . . 0.2432 . 0.2064 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.2863 1.3074 . . 261 5008 99.00 . . . 0.2462 . 0.1935 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.3074 1.3300 . . 258 4903 99.00 . . . 0.2216 . 0.1715 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.3300 1.3541 . . 261 4981 99.00 . . . 0.2027 . 0.1548 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.3541 1.3802 . . 263 5000 99.00 . . . 0.1663 . 0.1505 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.3802 1.4084 . . 261 4951 99.00 . . . 0.1857 . 0.1406 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.4084 1.4390 . . 264 5003 99.00 . . . 0.1437 . 0.1350 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.4390 1.4725 . . 267 5017 99.00 . . . 0.1725 . 0.1251 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.4725 1.5093 . . 263 4974 99.00 . . . 0.1524 . 0.1137 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.5093 1.5501 . . 266 5014 100.00 . . . 0.1473 . 0.1040 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.5501 1.5957 . . 265 5012 100.00 . . . 0.1316 . 0.1004 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.5957 1.6472 . . 267 5046 100.00 . . . 0.1330 . 0.0997 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.6472 1.7061 . . 265 5003 100.00 . . . 0.1321 . 0.1005 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.7061 1.7744 . . 267 5035 100.00 . . . 0.1265 . 0.1020 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.7744 1.8551 . . 279 5009 100.00 . . . 0.1413 . 0.1102 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.8551 1.9529 . . 264 5093 100.00 . . . 0.1287 . 0.1098 . . . . . . . . . . 'X-RAY DIFFRACTION' 1.9529 2.0753 . . 262 5029 100.00 . . . 0.1289 . 0.1099 . . . . . . . . . . 'X-RAY DIFFRACTION' 2.0753 2.2355 . . 256 5118 100.00 . . . 0.1275 . 0.1103 . . . . . . . . . . 'X-RAY DIFFRACTION' 2.2355 2.4604 . . 270 5059 100.00 . . . 0.1298 . 0.1149 . . . . . . . . . . 'X-RAY DIFFRACTION' 2.4604 2.8164 . . 253 5087 100.00 . . . 0.1310 . 0.1281 . . . . . . . . . . 'X-RAY DIFFRACTION' 2.8164 3.5479 . . 293 5093 100.00 . . . 0.1465 . 0.1347 . . . . . . . . . . 'X-RAY DIFFRACTION' 3.5479 36.8522 . . 275 5166 99.00 . . . 0.1464 . 0.1463 . . . . . . . . . . # _struct.entry_id 5KAR _struct.title 'Murine acid sphingomyelinase-like phosphodiesterase 3b (SMPDL3B)' _struct.pdbx_descriptor 'Acid sphingomyelinase-like phosphodiesterase 3b (E.C.3.1.4.-)' _struct.pdbx_model_details ? _struct.pdbx_formula_weight ? _struct.pdbx_formula_weight_method ? _struct.pdbx_model_type_details ? _struct.pdbx_CASP_flag N # _struct_keywords.entry_id 5KAR _struct_keywords.text 'phosphoesterase, extracellular, membrane, HYDROLASE' _struct_keywords.pdbx_keywords 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 3 ? E N N 3 ? F N N 4 ? G N N 5 ? H N N 3 ? I N N 5 ? J N N 3 ? K N N 6 ? L N N 3 ? M N N 3 ? N N N 7 ? O N N 7 ? P N N 8 ? Q N N 9 ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 AA1 CYS A 37 ? GLY A 41 ? CYS A 45 GLY A 49 5 ? 5 HELX_P HELX_P2 AA2 PRO A 59 ? GLU A 74 ? PRO A 67 GLU A 82 1 ? 16 HELX_P HELX_P3 AA3 PRO A 91 ? LEU A 95 ? PRO A 99 LEU A 103 5 ? 5 HELX_P HELX_P4 AA4 GLY A 96 ? PHE A 115 ? GLY A 104 PHE A 123 1 ? 20 HELX_P HELX_P5 AA5 ASN A 140 ? ARG A 151 ? ASN A 148 ARG A 159 1 ? 12 HELX_P HELX_P6 AA6 PRO A 152 ? LEU A 154 ? PRO A 160 LEU A 162 5 ? 3 HELX_P HELX_P7 AA7 SER A 155 ? ALA A 166 ? SER A 163 ALA A 174 1 ? 12 HELX_P HELX_P8 AA8 ASN A 185 ? TYR A 190 ? ASN A 193 TYR A 198 5 ? 6 HELX_P HELX_P9 AA9 ASN A 193 ? ALA A 197 ? ASN A 201 ALA A 205 5 ? 5 HELX_P HELX_P10 AB1 ASP A 201 ? GLY A 203 ? ASP A 209 GLY A 211 5 ? 3 HELX_P HELX_P11 AB2 GLU A 204 ? GLY A 220 ? GLU A 212 GLY A 228 1 ? 17 HELX_P HELX_P12 AB3 ARG A 244 ? HIS A 259 ? ARG A 252 HIS A 267 1 ? 16 HELX_P HELX_P13 AB4 ASN A 335 ? ASN A 340 ? ASN A 343 ASN A 348 1 ? 6 HELX_P HELX_P14 AB5 LEU A 353 ? GLN A 358 ? LEU A 361 GLN A 366 1 ? 6 HELX_P HELX_P15 AB6 SER A 363 ? GLU A 377 ? SER A 371 GLU A 385 1 ? 15 HELX_P HELX_P16 AB7 GLU A 377 ? SER A 389 ? GLU A 385 SER A 397 1 ? 13 HELX_P HELX_P17 AB8 GLU A 398 ? HIS A 411 ? GLU A 406 HIS A 419 1 ? 14 HELX_P HELX_P18 AB9 ALA A 413 ? HIS A 422 ? ALA A 421 HIS A 430 1 ? 10 # _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 37 SG ? ? ? 1_555 A CYS 56 SG ? ? A CYS 45 A CYS 64 1_555 ? ? ? ? ? ? ? 2.034 ? disulf2 disulf ? ? A CYS 397 SG ? ? ? 1_555 A CYS 401 SG ? ? A CYS 405 A CYS 409 1_555 ? ? ? ? ? ? ? 2.059 ? disulf3 disulf ? ? A CYS 407 SG ? ? ? 1_555 A CYS 420 SG ? ? A CYS 415 A CYS 428 1_555 ? ? ? ? ? ? ? 2.034 ? metalc1 metalc ? ? A ASP 20 OD1 ? ? ? 1_555 C ZN . ZN ? ? A ASP 28 A ZN 502 1_555 ? ? ? ? ? ? ? 2.018 ? metalc2 metalc ? ? A HIS 22 NE2 ? ? ? 1_555 C ZN . ZN ? ? A HIS 30 A ZN 502 1_555 ? ? ? ? ? ? ? 2.059 ? covale1 covale one ? A ASN 26 ND2 ? ? ? 1_555 L NAG . C1 ? ? A ASN 34 A NAG 511 1_555 ? ? ? ? ? ? ? 1.464 ? covale2 covale one ? A ASN 64 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 72 A NAG 503 1_555 ? ? ? ? ? ? ? 1.430 ? metalc3 metalc ? ? A ASP 85 OD2 ? ? ? 1_555 C ZN . ZN ? ? A ASP 93 A ZN 502 1_555 ? ? ? ? ? ? ? 2.324 ? metalc4 metalc ? ? A ASP 85 OD2 ? ? ? 1_555 B ZN . ZN ? ? A ASP 93 A ZN 501 1_555 ? ? ? ? ? ? ? 2.163 ? metalc5 metalc ? ? A ASN 126 OD1 ? ? ? 1_555 B ZN . ZN ? ? A ASN 134 A ZN 501 1_555 ? ? ? ? ? ? ? 2.064 ? covale3 covale one ? A ASN 215 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 223 A NAG 507 1_555 ? ? ? ? ? ? ? 1.427 ? metalc6 metalc ? ? A HIS 228 NE2 ? ? ? 1_555 B ZN . ZN ? ? A HIS 236 A ZN 501 1_555 ? ? ? ? ? ? ? 2.095 ? metalc7 metalc ? ? A HIS 269 ND1 ? ? ? 1_555 B ZN . ZN ? ? A HIS 277 A ZN 501 1_555 ? ? ? ? ? ? ? 2.135 ? metalc8 metalc ? ? A HIS 271 NE2 ? ? ? 1_555 C ZN . ZN ? ? A HIS 279 A ZN 502 1_555 ? ? ? ? ? ? ? 2.090 ? metalc9 metalc ? ? B ZN . ZN ? ? ? 1_555 Q HOH . O ? ? A ZN 501 A HOH 613 1_555 ? ? ? ? ? ? ? 2.049 ? metalc10 metalc ? ? C ZN . ZN ? ? ? 1_555 Q HOH . O ? ? A ZN 502 A HOH 613 1_555 ? ? ? ? ? ? ? 1.963 ? covale4 covale both ? D NAG . O4 ? ? ? 1_555 E NAG . C1 ? ? A NAG 503 A NAG 504 1_555 ? ? ? ? ? ? ? 1.416 ? covale5 covale both ? F BMA . C1 ? ? ? 1_555 J NAG . O4 ? ? A BMA 505 A NAG 509 1_555 ? ? ? ? ? ? ? 1.439 ? covale6 covale one ? F BMA . O3 ? ? ? 1_555 G MAN . C1 ? ? A BMA 505 A MAN 506 1_555 ? ? ? ? ? ? ? 1.470 ? covale7 covale one ? F BMA . O6 ? ? ? 1_555 I MAN . C1 ? ? A BMA 505 A MAN 508 1_555 ? ? ? ? ? ? ? 1.447 ? covale8 covale both ? H NAG . O4 ? ? ? 1_555 J NAG . C1 ? ? A NAG 507 A NAG 509 1_555 ? ? ? ? ? ? ? 1.424 ? covale9 covale one ? K FUC . C1 ? ? ? 1_555 L NAG . O6 ? ? A FUC 510 A NAG 511 1_555 ? ? ? ? ? ? ? 1.441 ? covale10 covale both ? L NAG . O4 ? ? ? 1_555 M NAG . C1 ? ? A NAG 511 A NAG 512 1_555 ? ? ? ? ? ? ? 1.434 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? metalc ? ? covale ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 HIS 130 A . ? HIS 138 A PRO 131 A ? PRO 139 A 1 -5.26 2 GLY 174 A . ? GLY 182 A PRO 175 A ? PRO 183 A 1 6.64 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA1 ? 6 ? AA2 ? 6 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense AA1 1 2 ? parallel AA1 2 3 ? parallel AA1 3 4 ? anti-parallel AA1 4 5 ? anti-parallel AA1 5 6 ? anti-parallel AA2 1 2 ? anti-parallel AA2 2 3 ? parallel AA2 3 4 ? parallel AA2 4 5 ? parallel AA2 5 6 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id AA1 1 VAL A 120 ? ALA A 122 ? VAL A 128 ALA A 130 AA1 2 PHE A 79 ? TRP A 82 ? PHE A 87 TRP A 90 AA1 3 GLY A 13 ? ILE A 18 ? GLY A 21 ILE A 26 AA1 4 GLY A 313 ? TYR A 319 ? GLY A 321 TYR A 327 AA1 5 LEU A 326 ? PHE A 333 ? LEU A 334 PHE A 341 AA1 6 GLU A 348 ? ARG A 352 ? GLU A 356 ARG A 360 AA2 1 TYR A 168 ? LYS A 171 ? TYR A 176 LYS A 179 AA2 2 GLY A 179 ? VAL A 183 ? GLY A 187 VAL A 191 AA2 3 MET A 222 ? ILE A 226 ? MET A 230 ILE A 234 AA2 4 ILE A 262 ? PHE A 267 ? ILE A 270 PHE A 275 AA2 5 PRO A 285 ? LEU A 291 ? PRO A 293 LEU A 299 AA2 6 SER A 274 ? TYR A 279 ? SER A 282 TYR A 287 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id AA1 1 2 O TYR A 121 ? O TYR A 129 N ILE A 80 ? N ILE A 88 AA1 2 3 O LEU A 81 ? O LEU A 89 N TRP A 16 ? N TRP A 24 AA1 3 4 N GLY A 13 ? N GLY A 21 O TYR A 319 ? O TYR A 327 AA1 4 5 N ILE A 314 ? N ILE A 322 O TYR A 332 ? O TYR A 340 AA1 5 6 N THR A 331 ? N THR A 339 O GLU A 350 ? O GLU A 358 AA2 1 2 N TYR A 168 ? N TYR A 176 O VAL A 183 ? O VAL A 191 AA2 2 3 N VAL A 182 ? N VAL A 190 O TYR A 224 ? O TYR A 232 AA2 3 4 N VAL A 225 ? N VAL A 233 O GLY A 264 ? O GLY A 272 AA2 4 5 N GLN A 265 ? N GLN A 273 O PHE A 290 ? O PHE A 298 AA2 5 6 O ILE A 286 ? O ILE A 294 N PHE A 278 ? N PHE A 286 # 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 A ZN 501 ? 6 'binding site for residue ZN A 501' AC2 Software A ZN 502 ? 6 'binding site for residue ZN A 502' AC3 Software A NO3 513 ? 6 'binding site for residue NO3 A 513' AC4 Software A NO3 514 ? 9 'binding site for residue NO3 A 514' AC5 Software A GOL 515 ? 8 'binding site for residue GOL A 515' AC6 Software A ASN 34 ? 15 'binding site for Poly-Saccharide residues FUC A 510 through NAG A 512 bound to ASN A 34' AC7 Software A ASN 72 ? 5 'binding site for Poly-Saccharide residues NAG A 503 through NAG A 504 bound to ASN A 72' AC8 Software A ASN 223 ? 17 'binding site for Poly-Saccharide residues BMA A 505 through NAG A 509 bound to ASN A 223' # 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 6 ASP A 85 ? ASP A 93 . ? 1_555 ? 2 AC1 6 ASN A 126 ? ASN A 134 . ? 1_555 ? 3 AC1 6 HIS A 228 ? HIS A 236 . ? 1_555 ? 4 AC1 6 HIS A 269 ? HIS A 277 . ? 1_555 ? 5 AC1 6 ZN C . ? ZN A 502 . ? 1_555 ? 6 AC1 6 HOH Q . ? HOH A 613 . ? 1_555 ? 7 AC2 6 ASP A 20 ? ASP A 28 . ? 1_555 ? 8 AC2 6 HIS A 22 ? HIS A 30 . ? 1_555 ? 9 AC2 6 ASP A 85 ? ASP A 93 . ? 1_555 ? 10 AC2 6 HIS A 271 ? HIS A 279 . ? 1_555 ? 11 AC2 6 ZN B . ? ZN A 501 . ? 1_555 ? 12 AC2 6 HOH Q . ? HOH A 613 . ? 1_555 ? 13 AC3 6 TYR A 351 ? TYR A 359 . ? 1_555 ? 14 AC3 6 ALA A 356 ? ALA A 364 . ? 1_555 ? 15 AC3 6 ARG A 383 ? ARG A 391 . ? 1_555 ? 16 AC3 6 TYR A 387 ? TYR A 395 . ? 1_555 ? 17 AC3 6 HOH Q . ? HOH A 601 . ? 1_555 ? 18 AC3 6 HOH Q . ? HOH A 791 . ? 1_555 ? 19 AC4 9 GLU A 250 ? GLU A 258 . ? 1_555 ? 20 AC4 9 LYS A 253 ? LYS A 261 . ? 1_555 ? 21 AC4 9 VAL A 254 ? VAL A 262 . ? 1_555 ? 22 AC4 9 LYS A 257 ? LYS A 265 . ? 1_555 ? 23 AC4 9 HIS A 258 ? HIS A 266 . ? 1_555 ? 24 AC4 9 HOH Q . ? HOH A 662 . ? 1_555 ? 25 AC4 9 HOH Q . ? HOH A 745 . ? 1_555 ? 26 AC4 9 HOH Q . ? HOH A 872 . ? 1_555 ? 27 AC4 9 HOH Q . ? HOH A 940 . ? 1_555 ? 28 AC5 8 PHE A 234 ? PHE A 242 . ? 1_555 ? 29 AC5 8 TRP A 242 ? TRP A 250 . ? 1_555 ? 30 AC5 8 HIS A 269 ? HIS A 277 . ? 1_555 ? 31 AC5 8 HIS A 270 ? HIS A 278 . ? 1_555 ? 32 AC5 8 HIS A 271 ? HIS A 279 . ? 1_555 ? 33 AC5 8 THR A 300 ? THR A 308 . ? 1_555 ? 34 AC5 8 HOH Q . ? HOH A 656 . ? 1_555 ? 35 AC5 8 HOH Q . ? HOH A 701 . ? 1_555 ? 36 AC6 15 ASN A 26 ? ASN A 34 . ? 1_555 ? 37 AC6 15 PRO A 38 ? PRO A 46 . ? 1_555 ? 38 AC6 15 PRO A 88 ? PRO A 96 . ? 1_555 ? 39 AC6 15 SER A 94 ? SER A 102 . ? 1_555 ? 40 AC6 15 TYR A 279 ? TYR A 287 . ? 1_455 ? 41 AC6 15 ASN A 281 ? ASN A 289 . ? 1_455 ? 42 AC6 15 HIS A 411 ? HIS A 419 . ? 1_455 ? 43 AC6 15 THR A 416 ? THR A 424 . ? 1_455 ? 44 AC6 15 HOH Q . ? HOH A 606 . ? 1_555 ? 45 AC6 15 HOH Q . ? HOH A 624 . ? 1_555 ? 46 AC6 15 HOH Q . ? HOH A 628 . ? 1_555 ? 47 AC6 15 HOH Q . ? HOH A 637 . ? 1_555 ? 48 AC6 15 HOH Q . ? HOH A 769 . ? 1_555 ? 49 AC6 15 HOH Q . ? HOH A 800 . ? 1_555 ? 50 AC6 15 HOH Q . ? HOH A 850 . ? 1_455 ? 51 AC7 5 ASN A 64 ? ASN A 72 . ? 1_555 ? 52 AC7 5 TYR A 68 ? TYR A 76 . ? 1_555 ? 53 AC7 5 HOH Q . ? HOH A 806 . ? 1_555 ? 54 AC7 5 HOH Q . ? HOH A 829 . ? 1_555 ? 55 AC7 5 HOH Q . ? HOH A 893 . ? 1_555 ? 56 AC8 17 ASN A 156 ? ASN A 164 . ? 1_555 ? 57 AC8 17 ASP A 211 ? ASP A 219 . ? 1_555 ? 58 AC8 17 VAL A 212 ? VAL A 220 . ? 1_555 ? 59 AC8 17 ASN A 215 ? ASN A 223 . ? 1_555 ? 60 AC8 17 ARG A 218 ? ARG A 226 . ? 1_555 ? 61 AC8 17 HOH Q . ? HOH A 626 . ? 1_555 ? 62 AC8 17 HOH Q . ? HOH A 633 . ? 1_555 ? 63 AC8 17 HOH Q . ? HOH A 648 . ? 1_555 ? 64 AC8 17 HOH Q . ? HOH A 684 . ? 1_555 ? 65 AC8 17 HOH Q . ? HOH A 727 . ? 1_555 ? 66 AC8 17 HOH Q . ? HOH A 743 . ? 1_555 ? 67 AC8 17 HOH Q . ? HOH A 756 . ? 1_555 ? 68 AC8 17 HOH Q . ? HOH A 824 . ? 1_555 ? 69 AC8 17 HOH Q . ? HOH A 867 . ? 1_555 ? 70 AC8 17 HOH Q . ? HOH A 896 . ? 1_555 ? 71 AC8 17 HOH Q . ? HOH A 898 . ? 1_555 ? 72 AC8 17 HOH Q . ? HOH A 952 . ? 1_555 ? # _atom_sites.entry_id 5KAR _atom_sites.fract_transf_matrix[1][1] 0.019649 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.002786 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.021263 _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] 0.010761 _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 H N O S ZN # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . LEU A 1 12 ? 13.309 -7.326 14.510 1.00 30.33 ? 20 LEU A N 1 ATOM 2 C CA . LEU A 1 12 ? 12.874 -5.915 14.465 1.00 27.02 ? 20 LEU A CA 1 ATOM 3 C C . LEU A 1 12 ? 11.497 -5.694 15.080 1.00 21.81 ? 20 LEU A C 1 ATOM 4 O O . LEU A 1 12 ? 10.494 -6.207 14.614 1.00 24.93 ? 20 LEU A O 1 ATOM 5 C CB . LEU A 1 12 ? 12.828 -5.441 13.027 1.00 32.12 ? 20 LEU A CB 1 ATOM 6 C CG . LEU A 1 12 ? 12.950 -3.937 12.841 1.00 33.28 ? 20 LEU A CG 1 ATOM 7 C CD1 . LEU A 1 12 ? 14.409 -3.536 12.959 1.00 34.25 ? 20 LEU A CD1 1 ATOM 8 C CD2 . LEU A 1 12 ? 12.390 -3.515 11.490 1.00 35.16 ? 20 LEU A CD2 1 ATOM 9 H HA . LEU A 1 12 ? 13.513 -5.367 14.946 1.00 32.43 ? 20 LEU A HA 1 ATOM 10 H HB2 . LEU A 1 12 ? 13.558 -5.856 12.542 1.00 38.55 ? 20 LEU A HB2 1 ATOM 11 H HB3 . LEU A 1 12 ? 11.982 -5.716 12.639 1.00 38.55 ? 20 LEU A HB3 1 ATOM 12 H HG . LEU A 1 12 ? 12.449 -3.484 13.537 1.00 39.94 ? 20 LEU A HG 1 ATOM 13 H HD11 . LEU A 1 12 ? 14.483 -2.577 12.840 1.00 41.10 ? 20 LEU A HD11 1 ATOM 14 H HD12 . LEU A 1 12 ? 14.735 -3.787 13.838 1.00 41.10 ? 20 LEU A HD12 1 ATOM 15 H HD13 . LEU A 1 12 ? 14.919 -3.996 12.273 1.00 41.10 ? 20 LEU A HD13 1 ATOM 16 H HD21 . LEU A 1 12 ? 12.480 -2.554 11.398 1.00 42.19 ? 20 LEU A HD21 1 ATOM 17 H HD22 . LEU A 1 12 ? 12.888 -3.963 10.788 1.00 42.19 ? 20 LEU A HD22 1 ATOM 18 H HD23 . LEU A 1 12 ? 11.454 -3.766 11.444 1.00 42.19 ? 20 LEU A HD23 1 ATOM 19 N N . GLY A 1 13 ? 11.452 -4.903 16.126 1.00 18.58 ? 21 GLY A N 1 ATOM 20 C CA . GLY A 1 13 ? 10.207 -4.520 16.743 1.00 18.20 ? 21 GLY A CA 1 ATOM 21 C C . GLY A 1 13 ? 9.775 -3.145 16.295 1.00 15.16 ? 21 GLY A C 1 ATOM 22 O O . GLY A 1 13 ? 10.543 -2.381 15.728 1.00 14.57 ? 21 GLY A O 1 ATOM 23 H H . GLY A 1 13 ? 12.146 -4.566 16.505 1.00 22.30 ? 21 GLY A H 1 ATOM 24 H HA2 . GLY A 1 13 ? 9.515 -5.157 16.506 1.00 21.84 ? 21 GLY A HA2 1 ATOM 25 H HA3 . GLY A 1 13 ? 10.308 -4.516 17.708 1.00 21.84 ? 21 GLY A HA3 1 ATOM 26 N N . ARG A 1 14 ? 8.516 -2.837 16.588 1.00 15.53 ? 22 ARG A N 1 ATOM 27 C CA . ARG A 1 14 ? 7.944 -1.539 16.290 1.00 14.75 ? 22 ARG A CA 1 ATOM 28 C C . ARG A 1 14 ? 7.163 -1.018 17.482 1.00 14.76 ? 22 ARG A C 1 ATOM 29 O O . ARG A 1 14 ? 6.585 -1.787 18.244 1.00 15.93 ? 22 ARG A O 1 ATOM 30 C CB . ARG A 1 14 ? 6.985 -1.630 15.125 1.00 15.90 ? 22 ARG A CB 1 ATOM 31 C CG . ARG A 1 14 ? 7.714 -1.912 13.841 1.00 19.63 ? 22 ARG A CG 1 ATOM 32 C CD . ARG A 1 14 ? 6.767 -2.350 12.739 1.00 23.20 ? 22 ARG A CD 1 ATOM 33 N NE . ARG A 1 14 ? 7.459 -2.325 11.464 1.00 27.35 ? 22 ARG A NE 1 ATOM 34 C CZ . ARG A 1 14 ? 8.215 -3.313 10.988 1.00 30.96 ? 22 ARG A CZ 1 ATOM 35 N NH1 . ARG A 1 14 ? 8.377 -4.434 11.685 1.00 31.27 ? 22 ARG A NH1 1 ATOM 36 N NH2 . ARG A 1 14 ? 8.809 -3.182 9.805 1.00 33.17 ? 22 ARG A NH2 1 ATOM 37 H H . ARG A 1 14 ? 7.965 -3.377 16.967 1.00 18.63 ? 22 ARG A H 1 ATOM 38 H HA . ARG A 1 14 ? 8.648 -0.908 16.073 1.00 17.70 ? 22 ARG A HA 1 ATOM 39 H HB2 . ARG A 1 14 ? 6.355 -2.350 15.282 1.00 19.08 ? 22 ARG A HB2 1 ATOM 40 H HB3 . ARG A 1 14 ? 6.515 -0.787 15.029 1.00 19.08 ? 22 ARG A HB3 1 ATOM 41 H HG2 . ARG A 1 14 ? 8.168 -1.107 13.548 1.00 23.56 ? 22 ARG A HG2 1 ATOM 42 H HG3 . ARG A 1 14 ? 8.356 -2.624 13.989 1.00 23.56 ? 22 ARG A HG3 1 ATOM 43 H HD2 . ARG A 1 14 ? 6.464 -3.255 12.910 1.00 27.84 ? 22 ARG A HD2 1 ATOM 44 H HD3 . ARG A 1 14 ? 6.014 -1.740 12.695 1.00 27.84 ? 22 ARG A HD3 1 ATOM 45 H HE . ARG A 1 14 ? 7.375 -1.619 10.980 1.00 32.82 ? 22 ARG A HE 1 ATOM 46 H HH11 . ARG A 1 14 ? 7.995 -4.523 12.450 1.00 37.53 ? 22 ARG A HH11 1 ATOM 47 H HH12 . ARG A 1 14 ? 8.865 -5.069 11.371 1.00 37.53 ? 22 ARG A HH12 1 ATOM 48 H HH21 . ARG A 1 14 ? 8.707 -2.460 9.350 1.00 39.80 ? 22 ARG A HH21 1 ATOM 49 H HH22 . ARG A 1 14 ? 9.295 -3.820 9.495 1.00 39.80 ? 22 ARG A HH22 1 ATOM 50 N N . PHE A 1 15 ? 7.155 0.293 17.644 1.00 13.58 ? 23 PHE A N 1 ATOM 51 C CA . PHE A 1 15 ? 6.298 0.907 18.645 1.00 13.56 ? 23 PHE A CA 1 ATOM 52 C C . PHE A 1 15 ? 5.790 2.236 18.116 1.00 12.44 ? 23 PHE A C 1 ATOM 53 O O . PHE A 1 15 ? 6.511 2.952 17.423 1.00 12.98 ? 23 PHE A O 1 ATOM 54 C CB . PHE A 1 15 ? 6.934 1.078 20.032 1.00 13.60 ? 23 PHE A CB 1 ATOM 55 C CG . PHE A 1 15 ? 8.220 1.877 20.088 1.00 13.45 ? 23 PHE A CG 1 ATOM 56 C CD1 . PHE A 1 15 ? 8.216 3.239 20.345 1.00 13.92 ? 23 PHE A CD1 1 ATOM 57 C CD2 . PHE A 1 15 ? 9.436 1.238 19.980 1.00 13.90 ? 23 PHE A CD2 1 ATOM 58 C CE1 . PHE A 1 15 ? 9.413 3.929 20.480 1.00 14.14 ? 23 PHE A CE1 1 ATOM 59 C CE2 . PHE A 1 15 ? 10.635 1.936 20.110 1.00 14.02 ? 23 PHE A CE2 1 ATOM 60 C CZ . PHE A 1 15 ? 10.626 3.274 20.374 1.00 14.02 ? 23 PHE A CZ 1 ATOM 61 H H . PHE A 1 15 ? 7.632 0.848 17.192 1.00 16.30 ? 23 PHE A H 1 ATOM 62 H HA . PHE A 1 15 ? 5.523 0.336 18.762 1.00 16.27 ? 23 PHE A HA 1 ATOM 63 H HB2 . PHE A 1 15 ? 6.293 1.524 20.607 1.00 16.32 ? 23 PHE A HB2 1 ATOM 64 H HB3 . PHE A 1 15 ? 7.127 0.197 20.388 1.00 16.32 ? 23 PHE A HB3 1 ATOM 65 H HD1 . PHE A 1 15 ? 7.408 3.688 20.450 1.00 16.70 ? 23 PHE A HD1 1 ATOM 66 H HD2 . PHE A 1 15 ? 9.457 0.320 19.831 1.00 16.68 ? 23 PHE A HD2 1 ATOM 67 H HE1 . PHE A 1 15 ? 9.399 4.845 20.642 1.00 16.97 ? 23 PHE A HE1 1 ATOM 68 H HE2 . PHE A 1 15 ? 11.445 1.487 20.024 1.00 16.82 ? 23 PHE A HE2 1 ATOM 69 H HZ . PHE A 1 15 ? 11.424 3.749 20.430 1.00 16.83 ? 23 PHE A HZ 1 ATOM 70 N N . TRP A 1 16 ? 4.526 2.543 18.412 1.00 12.33 ? 24 TRP A N 1 ATOM 71 C CA . TRP A 1 16 ? 3.980 3.854 18.108 1.00 12.04 ? 24 TRP A CA 1 ATOM 72 C C . TRP A 1 16 ? 4.370 4.843 19.195 1.00 11.48 ? 24 TRP A C 1 ATOM 73 O O . TRP A 1 16 ? 4.472 4.499 20.375 1.00 13.15 ? 24 TRP A O 1 ATOM 74 C CB . TRP A 1 16 ? 2.447 3.806 18.059 1.00 12.04 ? 24 TRP A CB 1 ATOM 75 C CG . TRP A 1 16 ? 1.911 3.126 16.833 1.00 11.99 ? 24 TRP A CG 1 ATOM 76 C CD1 . TRP A 1 16 ? 1.412 1.855 16.736 1.00 13.16 ? 24 TRP A CD1 1 ATOM 77 C CD2 . TRP A 1 16 ? 1.852 3.693 15.516 1.00 12.40 ? 24 TRP A CD2 1 ATOM 78 N NE1 . TRP A 1 16 ? 1.034 1.608 15.431 1.00 13.28 ? 24 TRP A NE1 1 ATOM 79 C CE2 . TRP A 1 16 ? 1.322 2.708 14.658 1.00 12.71 ? 24 TRP A CE2 1 ATOM 80 C CE3 . TRP A 1 16 ? 2.203 4.941 14.984 1.00 11.95 ? 24 TRP A CE3 1 ATOM 81 C CZ2 . TRP A 1 16 ? 1.135 2.943 13.302 1.00 14.33 ? 24 TRP A CZ2 1 ATOM 82 C CZ3 . TRP A 1 16 ? 2.027 5.159 13.648 1.00 13.32 ? 24 TRP A CZ3 1 ATOM 83 C CH2 . TRP A 1 16 ? 1.489 4.173 12.817 1.00 15.24 ? 24 TRP A CH2 1 ATOM 84 H H . TRP A 1 16 ? 3.969 2.006 18.788 1.00 14.79 ? 24 TRP A H 1 ATOM 85 H HA . TRP A 1 16 ? 4.317 4.169 17.254 1.00 14.45 ? 24 TRP A HA 1 ATOM 86 H HB2 . TRP A 1 16 ? 2.123 3.321 18.834 1.00 14.45 ? 24 TRP A HB2 1 ATOM 87 H HB3 . TRP A 1 16 ? 2.104 4.713 18.070 1.00 14.45 ? 24 TRP A HB3 1 ATOM 88 H HD1 . TRP A 1 16 ? 1.334 1.253 17.441 1.00 15.79 ? 24 TRP A HD1 1 ATOM 89 H HE1 . TRP A 1 16 ? 0.711 0.866 15.139 1.00 15.94 ? 24 TRP A HE1 1 ATOM 90 H HE3 . TRP A 1 16 ? 2.578 5.597 15.525 1.00 14.33 ? 24 TRP A HE3 1 ATOM 91 H HZ2 . TRP A 1 16 ? 0.763 2.296 12.748 1.00 17.20 ? 24 TRP A HZ2 1 ATOM 92 H HZ3 . TRP A 1 16 ? 2.264 5.982 13.285 1.00 15.99 ? 24 TRP A HZ3 1 ATOM 93 H HH2 . TRP A 1 16 ? 1.369 4.357 11.913 1.00 18.28 ? 24 TRP A HH2 1 ATOM 94 N N . HIS A 1 17 ? 4.581 6.089 18.792 1.00 11.30 ? 25 HIS A N 1 ATOM 95 C CA . HIS A 1 17 ? 4.664 7.220 19.711 1.00 10.79 ? 25 HIS A CA 1 ATOM 96 C C . HIS A 1 17 ? 3.648 8.242 19.231 1.00 11.79 ? 25 HIS A C 1 ATOM 97 O O . HIS A 1 17 ? 3.785 8.768 18.125 1.00 12.42 ? 25 HIS A O 1 ATOM 98 C CB . HIS A 1 17 ? 6.072 7.834 19.747 1.00 11.44 ? 25 HIS A CB 1 ATOM 99 C CG . HIS A 1 17 ? 6.203 8.979 20.703 1.00 10.91 ? 25 HIS A CG 1 ATOM 100 N ND1 . HIS A 1 17 ? 7.275 9.841 20.669 1.00 11.09 ? 25 HIS A ND1 1 ATOM 101 C CD2 . HIS A 1 17 ? 5.404 9.399 21.716 1.00 11.99 ? 25 HIS A CD2 1 ATOM 102 C CE1 . HIS A 1 17 ? 7.109 10.765 21.601 1.00 11.18 ? 25 HIS A CE1 1 ATOM 103 N NE2 . HIS A 1 17 ? 5.985 10.521 22.254 1.00 11.61 ? 25 HIS A NE2 1 ATOM 104 H H . HIS A 1 17 ? 4.682 6.312 17.968 1.00 13.55 ? 25 HIS A H 1 ATOM 105 H HA . HIS A 1 17 ? 4.423 6.936 20.606 1.00 12.94 ? 25 HIS A HA 1 ATOM 106 H HB2 . HIS A 1 17 ? 6.705 7.149 20.015 1.00 13.73 ? 25 HIS A HB2 1 ATOM 107 H HB3 . HIS A 1 17 ? 6.295 8.159 18.861 1.00 13.73 ? 25 HIS A HB3 1 ATOM 108 H HD2 . HIS A 1 17 ? 4.598 9.015 21.979 1.00 14.39 ? 25 HIS A HD2 1 ATOM 109 H HE1 . HIS A 1 17 ? 7.699 11.460 21.784 1.00 13.42 ? 25 HIS A HE1 1 ATOM 110 H HE2 . HIS A 1 17 ? 5.678 10.977 22.915 1.00 13.93 ? 25 HIS A HE2 1 ATOM 111 N N . ILE A 1 18 ? 2.666 8.525 20.062 1.00 12.01 ? 26 ILE A N 1 ATOM 112 C CA . ILE A 1 18 ? 1.693 9.572 19.768 1.00 12.83 ? 26 ILE A CA 1 ATOM 113 C C . ILE A 1 18 ? 1.630 10.556 20.925 1.00 11.50 ? 26 ILE A C 1 ATOM 114 O O . ILE A 1 18 ? 1.942 10.233 22.076 1.00 11.28 ? 26 ILE A O 1 ATOM 115 C CB . ILE A 1 18 ? 0.293 9.023 19.418 1.00 13.68 ? 26 ILE A CB 1 ATOM 116 C CG1 . ILE A 1 18 ? -0.248 8.188 20.593 1.00 15.07 ? 26 ILE A CG1 1 ATOM 117 C CG2 . ILE A 1 18 ? 0.392 8.237 18.115 1.00 15.02 ? 26 ILE A CG2 1 ATOM 118 C CD1 . ILE A 1 18 ? -1.722 7.854 20.449 1.00 16.00 ? 26 ILE A CD1 1 ATOM 119 H H . ILE A 1 18 ? 2.534 8.125 20.812 1.00 14.41 ? 26 ILE A H 1 ATOM 120 H HA . ILE A 1 18 ? 2.007 10.064 18.993 1.00 15.40 ? 26 ILE A HA 1 ATOM 121 H HB . ILE A 1 18 ? -0.304 9.775 19.277 1.00 16.42 ? 26 ILE A HB 1 ATOM 122 H HG12 . ILE A 1 18 ? 0.245 7.354 20.641 1.00 18.08 ? 26 ILE A HG12 1 ATOM 123 H HG13 . ILE A 1 18 ? -0.133 8.689 21.416 1.00 18.08 ? 26 ILE A HG13 1 ATOM 124 H HG21 . ILE A 1 18 ? -0.485 7.889 17.889 1.00 18.03 ? 26 ILE A HG21 1 ATOM 125 H HG22 . ILE A 1 18 ? 0.705 8.828 17.413 1.00 18.03 ? 26 ILE A HG22 1 ATOM 126 H HG23 . ILE A 1 18 ? 1.018 7.505 18.235 1.00 18.03 ? 26 ILE A HG23 1 ATOM 127 H HD11 . ILE A 1 18 ? -2.003 7.330 21.216 1.00 19.20 ? 26 ILE A HD11 1 ATOM 128 H HD12 . ILE A 1 18 ? -2.230 8.680 20.409 1.00 19.20 ? 26 ILE A HD12 1 ATOM 129 H HD13 . ILE A 1 18 ? -1.852 7.345 19.634 1.00 19.20 ? 26 ILE A HD13 1 ATOM 130 N N . SER A 1 19 ? 1.273 11.790 20.606 1.00 10.97 ? 27 SER A N 1 ATOM 131 C CA . SER A 1 19 ? 1.316 12.860 21.590 1.00 11.46 ? 27 SER A CA 1 ATOM 132 C C . SER A 1 19 ? 0.444 14.022 21.153 1.00 11.16 ? 27 SER A C 1 ATOM 133 O O . SER A 1 19 ? 0.188 14.227 19.965 1.00 11.38 ? 27 SER A O 1 ATOM 134 C CB . SER A 1 19 ? 2.749 13.361 21.735 1.00 11.27 ? 27 SER A CB 1 ATOM 135 O OG . SER A 1 19 ? 2.962 14.016 22.971 1.00 13.02 ? 27 SER A OG 1 ATOM 136 H H . SER A 1 19 ? 1.001 12.035 19.827 1.00 13.17 ? 27 SER A H 1 ATOM 137 H HA . SER A 1 19 ? 1.005 12.536 22.449 1.00 13.75 ? 27 SER A HA 1 ATOM 138 H HB2 . SER A 1 19 ? 3.351 12.603 21.676 1.00 13.53 ? 27 SER A HB2 1 ATOM 139 H HB3 . SER A 1 19 ? 2.936 13.985 21.016 1.00 13.53 ? 27 SER A HB3 1 ATOM 140 H HG . SER A 1 19 ? 2.451 14.678 23.037 1.00 15.63 ? 27 SER A HG 1 ATOM 141 N N . ASP A 1 20 ? 0.005 14.802 22.135 1.00 10.56 ? 28 ASP A N 1 ATOM 142 C CA . ASP A 1 20 ? -0.614 16.093 21.899 1.00 11.12 ? 28 ASP A CA 1 ATOM 143 C C . ASP A 1 20 ? -1.828 15.971 20.991 1.00 10.94 ? 28 ASP A C 1 ATOM 144 O O . ASP A 1 20 ? -1.958 16.665 19.999 1.00 11.56 ? 28 ASP A O 1 ATOM 145 C CB . ASP A 1 20 ? 0.407 17.091 21.391 1.00 10.71 ? 28 ASP A CB 1 ATOM 146 C CG . ASP A 1 20 ? 1.488 17.352 22.439 1.00 10.23 ? 28 ASP A CG 1 ATOM 147 O OD1 . ASP A 1 20 ? 1.327 18.293 23.244 1.00 11.48 ? 28 ASP A OD1 1 ATOM 148 O OD2 . ASP A 1 20 ? 2.518 16.646 22.453 1.00 10.92 ? 28 ASP A OD2 1 ATOM 149 H H . ASP A 1 20 ? 0.058 14.596 22.969 1.00 12.68 ? 28 ASP A H 1 ATOM 150 H HA . ASP A 1 20 ? -0.935 16.428 22.751 1.00 13.35 ? 28 ASP A HA 1 ATOM 151 H HB2 . ASP A 1 20 ? 0.833 16.738 20.595 1.00 12.85 ? 28 ASP A HB2 1 ATOM 152 H HB3 . ASP A 1 20 ? -0.036 17.931 21.193 1.00 12.85 ? 28 ASP A HB3 1 ATOM 153 N N . LEU A 1 21 ? -2.746 15.086 21.383 1.00 10.87 ? 29 LEU A N 1 ATOM 154 C CA . LEU A 1 21 ? -4.002 14.905 20.673 1.00 11.32 ? 29 LEU A CA 1 ATOM 155 C C . LEU A 1 21 ? -4.930 16.094 20.848 1.00 10.77 ? 29 LEU A C 1 ATOM 156 O O . LEU A 1 21 ? -5.703 16.393 19.941 1.00 11.77 ? 29 LEU A O 1 ATOM 157 C CB . LEU A 1 21 ? -4.639 13.582 21.083 1.00 12.93 ? 29 LEU A CB 1 ATOM 158 C CG . LEU A 1 21 ? -4.114 12.349 20.327 1.00 13.67 ? 29 LEU A CG 1 ATOM 159 C CD1 . LEU A 1 21 ? -2.603 12.169 20.352 1.00 14.14 ? 29 LEU A CD1 1 ATOM 160 C CD2 . LEU A 1 21 ? -4.840 11.092 20.821 1.00 16.65 ? 29 LEU A CD2 1 ATOM 161 H H . LEU A 1 21 ? -2.659 14.574 22.068 1.00 13.05 ? 29 LEU A H 1 ATOM 162 H HA . LEU A 1 21 ? -3.802 14.840 19.726 1.00 13.59 ? 29 LEU A HA 1 ATOM 163 H HB2 . LEU A 1 21 ? -4.474 13.439 22.027 1.00 15.52 ? 29 LEU A HB2 1 ATOM 164 H HB3 . LEU A 1 21 ? -5.595 13.638 20.924 1.00 15.52 ? 29 LEU A HB3 1 ATOM 165 H HG . LEU A 1 21 ? -4.359 12.457 19.394 1.00 16.40 ? 29 LEU A HG 1 ATOM 166 H HD11 . LEU A 1 21 ? -2.372 11.370 19.852 1.00 16.96 ? 29 LEU A HD11 1 ATOM 167 H HD12 . LEU A 1 21 ? -2.186 12.945 19.947 1.00 16.96 ? 29 LEU A HD12 1 ATOM 168 H HD13 . LEU A 1 21 ? -2.312 12.079 21.273 1.00 16.96 ? 29 LEU A HD13 1 ATOM 169 H HD21 . LEU A 1 21 ? -4.501 10.322 20.338 1.00 19.98 ? 29 LEU A HD21 1 ATOM 170 H HD22 . LEU A 1 21 ? -4.675 10.986 21.771 1.00 19.98 ? 29 LEU A HD22 1 ATOM 171 H HD23 . LEU A 1 21 ? -5.791 11.193 20.659 1.00 19.98 ? 29 LEU A HD23 1 ATOM 172 N N . HIS A 1 22 ? -4.931 16.730 22.023 1.00 11.02 ? 30 HIS A N 1 ATOM 173 C CA . HIS A 1 22 ? -5.686 17.938 22.326 1.00 10.95 ? 30 HIS A CA 1 ATOM 174 C C . HIS A 1 22 ? -7.089 17.946 21.705 1.00 11.25 ? 30 HIS A C 1 ATOM 175 O O . HIS A 1 22 ? -7.369 18.713 20.768 1.00 12.33 ? 30 HIS A O 1 ATOM 176 C CB . HIS A 1 22 ? -4.945 19.197 21.873 1.00 11.58 ? 30 HIS A CB 1 ATOM 177 C CG . HIS A 1 22 ? -3.704 19.533 22.640 1.00 10.52 ? 30 HIS A CG 1 ATOM 178 N ND1 . HIS A 1 22 ? -3.725 20.073 23.907 1.00 11.10 ? 30 HIS A ND1 1 ATOM 179 C CD2 . HIS A 1 22 ? -2.396 19.468 22.293 1.00 10.19 ? 30 HIS A CD2 1 ATOM 180 C CE1 . HIS A 1 22 ? -2.484 20.312 24.306 1.00 10.05 ? 30 HIS A CE1 1 ATOM 181 N NE2 . HIS A 1 22 ? -1.651 19.938 23.358 1.00 10.80 ? 30 HIS A NE2 1 ATOM 182 H H . HIS A 1 22 ? -4.471 16.457 22.696 1.00 13.23 ? 30 HIS A H 1 ATOM 183 H HA . HIS A 1 22 ? -5.794 17.996 23.288 1.00 13.14 ? 30 HIS A HA 1 ATOM 184 H HB2 . HIS A 1 22 ? -4.691 19.085 20.944 1.00 13.90 ? 30 HIS A HB2 1 ATOM 185 H HB3 . HIS A 1 22 ? -5.549 19.952 21.954 1.00 13.90 ? 30 HIS A HB3 1 ATOM 186 H HD1 . HIS A 1 22 ? -4.434 20.239 24.364 1.00 13.32 ? 30 HIS A HD1 1 ATOM 187 H HD2 . HIS A 1 22 ? -2.059 19.145 21.489 1.00 12.23 ? 30 HIS A HD2 1 ATOM 188 H HE1 . HIS A 1 22 ? -2.240 20.656 25.135 1.00 12.06 ? 30 HIS A HE1 1 ATOM 189 N N . LEU A 1 23 ? -7.986 17.125 22.238 1.00 11.20 ? 31 LEU A N 1 ATOM 190 C CA . LEU A 1 23 ? -9.386 17.178 21.830 1.00 11.61 ? 31 LEU A CA 1 ATOM 191 C C . LEU A 1 23 ? -9.996 18.540 22.124 1.00 12.32 ? 31 LEU A C 1 ATOM 192 O O . LEU A 1 23 ? -9.905 19.040 23.247 1.00 13.34 ? 31 LEU A O 1 ATOM 193 C CB . LEU A 1 23 ? -10.169 16.111 22.585 1.00 12.28 ? 31 LEU A CB 1 ATOM 194 C CG . LEU A 1 23 ? -11.690 16.076 22.383 1.00 12.78 ? 31 LEU A CG 1 ATOM 195 C CD1 . LEU A 1 23 ? -12.015 15.732 20.947 1.00 13.63 ? 31 LEU A CD1 1 ATOM 196 C CD2 . LEU A 1 23 ? -12.332 15.099 23.310 1.00 14.13 ? 31 LEU A CD2 1 ATOM 197 H H . LEU A 1 23 ? -7.812 16.530 22.834 1.00 13.45 ? 31 LEU A H 1 ATOM 198 H HA . LEU A 1 23 ? -9.457 17.003 20.879 1.00 13.93 ? 31 LEU A HA 1 ATOM 199 H HB2 . LEU A 1 23 ? -9.827 15.243 22.319 1.00 14.73 ? 31 LEU A HB2 1 ATOM 200 H HB3 . LEU A 1 23 ? -10.011 16.238 23.533 1.00 14.73 ? 31 LEU A HB3 1 ATOM 201 H HG . LEU A 1 23 ? -12.055 16.955 22.572 1.00 15.33 ? 31 LEU A HG 1 ATOM 202 H HD11 . LEU A 1 23 ? -12.978 15.715 20.837 1.00 16.36 ? 31 LEU A HD11 1 ATOM 203 H HD12 . LEU A 1 23 ? -11.627 16.406 20.366 1.00 16.36 ? 31 LEU A HD12 1 ATOM 204 H HD13 . LEU A 1 23 ? -11.641 14.862 20.739 1.00 16.36 ? 31 LEU A HD13 1 ATOM 205 H HD21 . LEU A 1 23 ? -13.290 15.102 23.158 1.00 16.96 ? 31 LEU A HD21 1 ATOM 206 H HD22 . LEU A 1 23 ? -11.971 14.216 23.136 1.00 16.96 ? 31 LEU A HD22 1 ATOM 207 H HD23 . LEU A 1 23 ? -12.141 15.361 24.225 1.00 16.96 ? 31 LEU A HD23 1 ATOM 208 N N . ASP A 1 24 ? -10.688 19.109 21.126 1.00 12.21 ? 32 ASP A N 1 ATOM 209 C CA . ASP A 1 24 ? -11.599 20.211 21.395 1.00 13.29 ? 32 ASP A CA 1 ATOM 210 C C . ASP A 1 24 ? -13.020 19.649 21.408 1.00 12.61 ? 32 ASP A C 1 ATOM 211 O O . ASP A 1 24 ? -13.570 19.334 20.343 1.00 13.12 ? 32 ASP A O 1 ATOM 212 C CB . ASP A 1 24 ? -11.486 21.348 20.378 1.00 14.37 ? 32 ASP A CB 1 ATOM 213 C CG . ASP A 1 24 ? -12.302 22.568 20.793 1.00 13.86 ? 32 ASP A CG 1 ATOM 214 O OD1 . ASP A 1 24 ? -13.314 22.395 21.509 1.00 15.52 ? 32 ASP A OD1 1 ATOM 215 O OD2 . ASP A 1 24 ? -11.923 23.695 20.387 1.00 14.46 ? 32 ASP A OD2 1 ATOM 216 H H . ASP A 1 24 ? -10.644 18.874 20.300 1.00 14.66 ? 32 ASP A H 1 ATOM 217 H HA . ASP A 1 24 ? -11.410 20.573 22.274 1.00 15.94 ? 32 ASP A HA 1 ATOM 218 H HB2 . ASP A 1 24 ? -10.557 21.617 20.303 1.00 17.24 ? 32 ASP A HB2 1 ATOM 219 H HB3 . ASP A 1 24 ? -11.816 21.042 19.519 1.00 17.24 ? 32 ASP A HB3 1 ATOM 220 N N . PRO A 1 25 ? -13.623 19.454 22.583 1.00 14.15 ? 33 PRO A N 1 ATOM 221 C CA . PRO A 1 25 ? -14.938 18.822 22.654 1.00 15.47 ? 33 PRO A CA 1 ATOM 222 C C . PRO A 1 25 ? -16.001 19.580 21.919 1.00 14.19 ? 33 PRO A C 1 ATOM 223 O O . PRO A 1 25 ? -17.033 18.991 21.565 1.00 16.69 ? 33 PRO A O 1 ATOM 224 C CB . PRO A 1 25 ? -15.254 18.826 24.159 1.00 17.69 ? 33 PRO A CB 1 ATOM 225 C CG . PRO A 1 25 ? -14.143 19.266 24.818 1.00 19.49 ? 33 PRO A CG 1 ATOM 226 C CD . PRO A 1 25 ? -13.129 19.818 23.916 1.00 15.73 ? 33 PRO A CD 1 ATOM 227 H HA . PRO A 1 25 ? -14.899 17.908 22.330 1.00 18.57 ? 33 PRO A HA 1 ATOM 228 H HB2 . PRO A 1 25 ? -16.001 19.423 24.326 1.00 21.22 ? 33 PRO A HB2 1 ATOM 229 H HB3 . PRO A 1 25 ? -15.476 17.925 24.442 1.00 21.22 ? 33 PRO A HB3 1 ATOM 230 H HG2 . PRO A 1 25 ? -14.415 19.951 25.448 1.00 23.39 ? 33 PRO A HG2 1 ATOM 231 H HG3 . PRO A 1 25 ? -13.763 18.517 25.304 1.00 23.39 ? 33 PRO A HG3 1 ATOM 232 H HD2 . PRO A 1 25 ? -13.084 20.783 24.008 1.00 18.88 ? 33 PRO A HD2 1 ATOM 233 H HD3 . PRO A 1 25 ? -12.267 19.405 24.082 1.00 18.88 ? 33 PRO A HD3 1 ATOM 234 N N . ASN A 1 26 ? -15.828 20.880 21.734 1.00 13.92 ? 34 ASN A N 1 ATOM 235 C CA . ASN A 1 26 ? -16.879 21.720 21.197 1.00 16.32 ? 34 ASN A CA 1 ATOM 236 C C . ASN A 1 26 ? -16.662 22.063 19.734 1.00 16.10 ? 34 ASN A C 1 ATOM 237 O O . ASN A 1 26 ? -17.393 22.899 19.201 1.00 17.99 ? 34 ASN A O 1 ATOM 238 C CB . ASN A 1 26 ? -17.041 22.972 22.070 1.00 18.88 ? 34 ASN A CB 1 ATOM 239 C CG . ASN A 1 26 ? -17.534 22.641 23.491 1.00 19.90 ? 34 ASN A CG 1 ATOM 240 O OD1 . ASN A 1 26 ? -17.906 21.505 23.777 1.00 23.55 ? 34 ASN A OD1 1 ATOM 241 N ND2 . ASN A 1 26 ? -17.543 23.627 24.369 1.00 21.77 ? 34 ASN A ND2 1 ATOM 242 H H . ASN A 1 26 ? -15.101 21.302 21.914 1.00 16.71 ? 34 ASN A H 1 ATOM 243 H HA . ASN A 1 26 ? -17.713 21.227 21.250 1.00 19.58 ? 34 ASN A HA 1 ATOM 244 H HB2 . ASN A 1 26 ? -16.183 23.419 22.145 1.00 22.66 ? 34 ASN A HB2 1 ATOM 245 H HB3 . ASN A 1 26 ? -17.689 23.564 21.657 1.00 22.66 ? 34 ASN A HB3 1 ATOM 246 H HD21 . ASN A 1 26 ? -17.266 24.405 24.133 1.00 26.13 ? 34 ASN A HD21 1 ATOM 247 N N . TYR A 1 27 ? -15.723 21.405 19.051 1.00 15.15 ? 35 TYR A N 1 ATOM 248 C CA . TYR A 1 27 ? -15.530 21.635 17.623 1.00 14.83 ? 35 TYR A CA 1 ATOM 249 C C . TYR A 1 27 ? -16.813 21.328 16.874 1.00 16.00 ? 35 TYR A C 1 ATOM 250 O O . TYR A 1 27 ? -17.338 20.218 16.963 1.00 17.08 ? 35 TYR A O 1 ATOM 251 C CB . TYR A 1 27 ? -14.417 20.750 17.084 1.00 14.86 ? 35 TYR A CB 1 ATOM 252 C CG . TYR A 1 27 ? -14.023 21.067 15.668 1.00 14.98 ? 35 TYR A CG 1 ATOM 253 C CD1 . TYR A 1 27 ? -14.765 20.612 14.592 1.00 14.98 ? 35 TYR A CD1 1 ATOM 254 C CD2 . TYR A 1 27 ? -12.895 21.815 15.396 1.00 16.76 ? 35 TYR A CD2 1 ATOM 255 C CE1 . TYR A 1 27 ? -14.388 20.901 13.291 1.00 15.45 ? 35 TYR A CE1 1 ATOM 256 C CE2 . TYR A 1 27 ? -12.525 22.114 14.100 1.00 16.91 ? 35 TYR A CE2 1 ATOM 257 C CZ . TYR A 1 27 ? -13.277 21.661 13.047 1.00 15.68 ? 35 TYR A CZ 1 ATOM 258 O OH . TYR A 1 27 ? -12.873 21.968 11.776 1.00 17.93 ? 35 TYR A OH 1 ATOM 259 H H . TYR A 1 27 ? -15.189 20.823 19.391 1.00 18.18 ? 35 TYR A H 1 ATOM 260 H HA . TYR A 1 27 ? -15.293 22.563 17.470 1.00 17.79 ? 35 TYR A HA 1 ATOM 261 H HB2 . TYR A 1 27 ? -13.632 20.860 17.642 1.00 17.83 ? 35 TYR A HB2 1 ATOM 262 H HB3 . TYR A 1 27 ? -14.712 19.827 17.110 1.00 17.83 ? 35 TYR A HB3 1 ATOM 263 H HD1 . TYR A 1 27 ? -15.526 20.101 14.745 1.00 17.97 ? 35 TYR A HD1 1 ATOM 264 H HD2 . TYR A 1 27 ? -12.381 22.135 16.102 1.00 20.11 ? 35 TYR A HD2 1 ATOM 265 H HE1 . TYR A 1 27 ? -14.903 20.592 12.580 1.00 18.54 ? 35 TYR A HE1 1 ATOM 266 H HE2 . TYR A 1 27 ? -11.763 22.623 13.941 1.00 20.29 ? 35 TYR A HE2 1 ATOM 267 H HH . TYR A 1 27 ? -13.399 21.626 11.217 1.00 21.52 ? 35 TYR A HH 1 ATOM 268 N N . THR A 1 28 ? -17.311 22.306 16.120 1.00 16.81 ? 36 THR A N 1 ATOM 269 C CA A THR A 1 28 ? -18.535 22.144 15.351 0.25 19.53 ? 36 THR A CA 1 ATOM 270 C CA B THR A 1 28 ? -18.535 22.153 15.355 0.75 19.91 ? 36 THR A CA 1 ATOM 271 C C . THR A 1 28 ? -18.371 22.883 14.036 1.00 20.23 ? 36 THR A C 1 ATOM 272 O O . THR A 1 28 ? -17.918 24.027 14.013 1.00 21.06 ? 36 THR A O 1 ATOM 273 C CB A THR A 1 28 ? -19.764 22.681 16.101 0.25 21.78 ? 36 THR A CB 1 ATOM 274 C CB B THR A 1 28 ? -19.699 22.793 16.120 0.75 22.41 ? 36 THR A CB 1 ATOM 275 O OG1 A THR A 1 28 ? -19.650 24.095 16.278 0.25 23.18 ? 36 THR A OG1 1 ATOM 276 O OG1 B THR A 1 28 ? -19.757 22.304 17.469 0.75 25.62 ? 36 THR A OG1 1 ATOM 277 C CG2 A THR A 1 28 ? -19.920 22.014 17.460 0.25 22.50 ? 36 THR A CG2 1 ATOM 278 C CG2 B THR A 1 28 ? -21.009 22.486 15.425 0.75 23.21 ? 36 THR A CG2 1 ATOM 279 H H . THR A 1 28 ? -16.948 23.082 16.039 1.00 20.17 ? 36 THR A H 1 ATOM 280 H HA . THR A 1 28 ? -18.701 21.209 15.176 1.00 23.90 ? 36 THR A HA 1 ATOM 281 H HB A THR A 1 28 ? -20.560 22.491 15.581 0.25 26.13 ? 36 THR A HB 1 ATOM 282 H HB B THR A 1 28 ? -19.581 23.756 16.134 0.75 26.89 ? 36 THR A HB 1 ATOM 283 H HG1 A THR A 1 28 ? -18.960 24.274 16.722 0.25 27.81 ? 36 THR A HG1 1 ATOM 284 H HG1 B THR A 1 28 ? -19.042 22.485 17.872 0.75 30.75 ? 36 THR A HG1 1 ATOM 285 H HG21 A THR A 1 28 ? -19.134 22.182 18.003 0.25 27.00 ? 36 THR A HG21 1 ATOM 286 H HG21 B THR A 1 28 ? -21.147 21.527 15.387 0.75 27.85 ? 36 THR A HG21 1 ATOM 287 H HG22 A THR A 1 28 ? -20.700 22.368 17.915 0.25 27.00 ? 36 THR A HG22 1 ATOM 288 H HG22 B THR A 1 28 ? -21.745 22.892 15.910 0.75 27.85 ? 36 THR A HG22 1 ATOM 289 H HG23 A THR A 1 28 ? -20.027 21.056 17.348 0.25 27.00 ? 36 THR A HG23 1 ATOM 290 H HG23 B THR A 1 28 ? -20.995 22.839 14.521 0.75 27.85 ? 36 THR A HG23 1 ATOM 291 N N . VAL A 1 29 ? -18.746 22.228 12.944 1.00 22.86 ? 37 VAL A N 1 ATOM 292 C CA . VAL A 1 29 ? -18.795 22.887 11.653 1.00 25.27 ? 37 VAL A CA 1 ATOM 293 C C . VAL A 1 29 ? -19.990 23.825 11.738 1.00 28.32 ? 37 VAL A C 1 ATOM 294 O O . VAL A 1 29 ? -21.144 23.390 11.727 1.00 33.33 ? 37 VAL A O 1 ATOM 295 C CB . VAL A 1 29 ? -18.904 21.842 10.530 1.00 26.80 ? 37 VAL A CB 1 ATOM 296 C CG1 . VAL A 1 29 ? -19.220 22.493 9.207 1.00 28.62 ? 37 VAL A CG1 1 ATOM 297 C CG2 . VAL A 1 29 ? -17.611 21.031 10.443 1.00 28.55 ? 37 VAL A CG2 1 ATOM 298 H H . VAL A 1 29 ? -18.978 21.400 12.928 1.00 27.43 ? 37 VAL A H 1 ATOM 299 H HA . VAL A 1 29 ? -17.990 23.412 11.518 1.00 30.33 ? 37 VAL A HA 1 ATOM 300 H HB . VAL A 1 29 ? -19.627 21.230 10.740 1.00 32.15 ? 37 VAL A HB 1 ATOM 301 H HG11 . VAL A 1 29 ? -19.281 21.807 8.524 1.00 34.35 ? 37 VAL A HG11 1 ATOM 302 H HG12 . VAL A 1 29 ? -20.065 22.964 9.280 1.00 34.35 ? 37 VAL A HG12 1 ATOM 303 H HG13 . VAL A 1 29 ? -18.511 23.118 8.986 1.00 34.35 ? 37 VAL A HG13 1 ATOM 304 H HG21 . VAL A 1 29 ? -17.695 20.377 9.731 1.00 34.26 ? 37 VAL A HG21 1 ATOM 305 H HG22 . VAL A 1 29 ? -16.873 21.632 10.255 1.00 34.26 ? 37 VAL A HG22 1 ATOM 306 H HG23 . VAL A 1 29 ? -17.464 20.581 11.290 1.00 34.26 ? 37 VAL A HG23 1 ATOM 307 N N . SER A 1 30 ? -19.722 25.111 11.892 1.00 29.19 ? 38 SER A N 1 ATOM 308 C CA . SER A 1 30 ? -20.753 26.110 12.117 1.00 30.61 ? 38 SER A CA 1 ATOM 309 C C . SER A 1 30 ? -20.617 27.210 11.086 1.00 32.18 ? 38 SER A C 1 ATOM 310 O O . SER A 1 30 ? -19.513 27.528 10.643 1.00 32.60 ? 38 SER A O 1 ATOM 311 C CB . SER A 1 30 ? -20.584 26.755 13.486 1.00 31.61 ? 38 SER A CB 1 ATOM 312 O OG . SER A 1 30 ? -21.397 27.903 13.577 1.00 31.44 ? 38 SER A OG 1 ATOM 313 H H . SER A 1 30 ? -18.928 25.439 11.869 1.00 35.03 ? 38 SER A H 1 ATOM 314 H HA . SER A 1 30 ? -21.635 25.711 12.052 1.00 36.73 ? 38 SER A HA 1 ATOM 315 H HB2 . SER A 1 30 ? -20.848 26.121 14.172 1.00 37.93 ? 38 SER A HB2 1 ATOM 316 H HB3 . SER A 1 30 ? -19.656 27.010 13.606 1.00 37.93 ? 38 SER A HB3 1 ATOM 317 H HG . SER A 1 30 ? -22.204 27.693 13.471 1.00 37.72 ? 38 SER A HG 1 ATOM 318 N N . LYS A 1 31 ? -21.758 27.791 10.707 1.00 32.36 ? 39 LYS A N 1 ATOM 319 C CA . LYS A 1 31 ? -21.757 28.963 9.838 1.00 33.63 ? 39 LYS A CA 1 ATOM 320 C C . LYS A 1 31 ? -21.260 30.221 10.551 1.00 33.33 ? 39 LYS A C 1 ATOM 321 O O . LYS A 1 31 ? -20.954 31.211 9.881 1.00 34.44 ? 39 LYS A O 1 ATOM 322 C CB . LYS A 1 31 ? -23.156 29.163 9.235 1.00 36.94 ? 39 LYS A CB 1 ATOM 323 C CG . LYS A 1 31 ? -23.550 28.065 8.239 1.00 38.80 ? 39 LYS A CG 1 ATOM 324 C CD . LYS A 1 31 ? -24.907 28.343 7.568 1.00 41.74 ? 39 LYS A CD 1 ATOM 325 C CE . LYS A 1 31 ? -24.776 28.485 6.049 1.00 45.17 ? 39 LYS A CE 1 ATOM 326 N NZ . LYS A 1 31 ? -26.063 28.855 5.381 1.00 47.42 ? 39 LYS A NZ 1 ATOM 327 H H . LYS A 1 31 ? -22.542 27.525 10.939 1.00 38.83 ? 39 LYS A H 1 ATOM 328 H HA . LYS A 1 31 ? -21.149 28.794 9.102 1.00 40.35 ? 39 LYS A HA 1 ATOM 329 H HB2 . LYS A 1 31 ? -23.809 29.165 9.951 1.00 44.33 ? 39 LYS A HB2 1 ATOM 330 H HB3 . LYS A 1 31 ? -23.177 30.012 8.766 1.00 44.33 ? 39 LYS A HB3 1 ATOM 331 H HG2 . LYS A 1 31 ? -22.876 28.009 7.544 1.00 46.56 ? 39 LYS A HG2 1 ATOM 332 H HG3 . LYS A 1 31 ? -23.615 27.218 8.709 1.00 46.56 ? 39 LYS A HG3 1 ATOM 333 H HD2 . LYS A 1 31 ? -25.510 27.607 7.752 1.00 50.08 ? 39 LYS A HD2 1 ATOM 334 H HD3 . LYS A 1 31 ? -25.272 29.170 7.919 1.00 50.08 ? 39 LYS A HD3 1 ATOM 335 H HE2 . LYS A 1 31 ? -24.127 29.178 5.852 1.00 54.20 ? 39 LYS A HE2 1 ATOM 336 H HE3 . LYS A 1 31 ? -24.479 27.639 5.678 1.00 54.20 ? 39 LYS A HE3 1 ATOM 337 H HZ1 . LYS A 1 31 ? -25.940 28.926 4.503 1.00 56.91 ? 39 LYS A HZ1 1 ATOM 338 H HZ2 . LYS A 1 31 ? -26.677 28.230 5.538 1.00 56.91 ? 39 LYS A HZ2 1 ATOM 339 H HZ3 . LYS A 1 31 ? -26.356 29.634 5.696 1.00 56.91 ? 39 LYS A HZ3 1 ATOM 340 N N . ASP A 1 32 ? -21.162 30.208 11.885 1.00 31.09 ? 40 ASP A N 1 ATOM 341 C CA . ASP A 1 32 ? -20.606 31.332 12.629 1.00 31.15 ? 40 ASP A CA 1 ATOM 342 C C . ASP A 1 32 ? -19.117 31.069 12.835 1.00 28.80 ? 40 ASP A C 1 ATOM 343 O O . ASP A 1 32 ? -18.761 30.127 13.564 1.00 27.26 ? 40 ASP A O 1 ATOM 344 C CB . ASP A 1 32 ? -21.312 31.467 13.972 1.00 33.87 ? 40 ASP A CB 1 ATOM 345 C CG . ASP A 1 32 ? -20.873 32.695 14.765 1.00 36.42 ? 40 ASP A CG 1 ATOM 346 O OD1 . ASP A 1 32 ? -19.760 33.218 14.539 1.00 37.13 ? 40 ASP A OD1 1 ATOM 347 O OD2 . ASP A 1 32 ? -21.654 33.132 15.645 1.00 39.21 ? 40 ASP A OD2 1 ATOM 348 H H . ASP A 1 32 ? -21.414 29.552 12.381 1.00 37.31 ? 40 ASP A H 1 ATOM 349 H HA . ASP A 1 32 ? -20.718 32.154 12.126 1.00 37.38 ? 40 ASP A HA 1 ATOM 350 H HB2 . ASP A 1 32 ? -22.268 31.538 13.819 1.00 40.64 ? 40 ASP A HB2 1 ATOM 351 H HB3 . ASP A 1 32 ? -21.121 30.682 14.508 1.00 40.64 ? 40 ASP A HB3 1 ATOM 352 N N . PRO A 1 33 ? -18.218 31.849 12.220 1.00 26.30 ? 41 PRO A N 1 ATOM 353 C CA . PRO A 1 33 ? -16.771 31.556 12.335 1.00 25.69 ? 41 PRO A CA 1 ATOM 354 C C . PRO A 1 33 ? -16.207 31.691 13.731 1.00 24.28 ? 41 PRO A C 1 ATOM 355 O O . PRO A 1 33 ? -15.064 31.256 13.951 1.00 23.29 ? 41 PRO A O 1 ATOM 356 C CB . PRO A 1 33 ? -16.112 32.577 11.397 1.00 26.59 ? 41 PRO A CB 1 ATOM 357 C CG . PRO A 1 33 ? -17.204 33.193 10.626 1.00 28.17 ? 41 PRO A CG 1 ATOM 358 C CD . PRO A 1 33 ? -18.482 33.025 11.379 1.00 28.23 ? 41 PRO A CD 1 ATOM 359 H HA . PRO A 1 33 ? -16.588 30.662 12.006 1.00 30.83 ? 41 PRO A HA 1 ATOM 360 H HB2 . PRO A 1 33 ? -15.648 33.247 11.923 1.00 31.91 ? 41 PRO A HB2 1 ATOM 361 H HB3 . PRO A 1 33 ? -15.494 32.120 10.805 1.00 31.91 ? 41 PRO A HB3 1 ATOM 362 H HG2 . PRO A 1 33 ? -17.012 34.136 10.505 1.00 33.81 ? 41 PRO A HG2 1 ATOM 363 H HG3 . PRO A 1 33 ? -17.268 32.754 9.763 1.00 33.81 ? 41 PRO A HG3 1 ATOM 364 H HD2 . PRO A 1 33 ? -18.656 33.804 11.929 1.00 33.87 ? 41 PRO A HD2 1 ATOM 365 H HD3 . PRO A 1 33 ? -19.215 32.848 10.768 1.00 33.87 ? 41 PRO A HD3 1 ATOM 366 N N . LEU A 1 34 ? -16.934 32.311 14.660 1.00 25.52 ? 42 LEU A N 1 ATOM 367 C CA . LEU A 1 34 ? -16.473 32.459 16.029 1.00 25.32 ? 42 LEU A CA 1 ATOM 368 C C . LEU A 1 34 ? -17.035 31.388 16.948 1.00 25.22 ? 42 LEU A C 1 ATOM 369 O O . LEU A 1 34 ? -16.743 31.407 18.149 1.00 27.56 ? 42 LEU A O 1 ATOM 370 C CB . LEU A 1 34 ? -16.843 33.852 16.557 1.00 27.29 ? 42 LEU A CB 1 ATOM 371 C CG . LEU A 1 34 ? -16.137 35.026 15.857 1.00 29.03 ? 42 LEU A CG 1 ATOM 372 C CD1 . LEU A 1 34 ? -16.630 36.372 16.391 1.00 30.04 ? 42 LEU A CD1 1 ATOM 373 C CD2 . LEU A 1 34 ? -14.627 34.900 16.007 1.00 30.25 ? 42 LEU A CD2 1 ATOM 374 H H . LEU A 1 34 ? -17.707 32.659 14.515 1.00 30.62 ? 42 LEU A H 1 ATOM 375 H HA . LEU A 1 34 ? -15.506 32.383 16.043 1.00 30.38 ? 42 LEU A HA 1 ATOM 376 H HB2 . LEU A 1 34 ? -17.799 33.979 16.448 1.00 32.75 ? 42 LEU A HB2 1 ATOM 377 H HB3 . LEU A 1 34 ? -16.616 33.895 17.499 1.00 32.75 ? 42 LEU A HB3 1 ATOM 378 H HG . LEU A 1 34 ? -16.343 34.992 14.909 1.00 34.84 ? 42 LEU A HG 1 ATOM 379 H HD11 . LEU A 1 34 ? -16.164 37.085 15.927 1.00 36.04 ? 42 LEU A HD11 1 ATOM 380 H HD12 . LEU A 1 34 ? -17.585 36.442 16.233 1.00 36.04 ? 42 LEU A HD12 1 ATOM 381 H HD13 . LEU A 1 34 ? -16.447 36.420 17.342 1.00 36.04 ? 42 LEU A HD13 1 ATOM 382 H HD21 . LEU A 1 34 ? -14.203 35.649 15.559 1.00 36.30 ? 42 LEU A HD21 1 ATOM 383 H HD22 . LEU A 1 34 ? -14.402 34.908 16.950 1.00 36.30 ? 42 LEU A HD22 1 ATOM 384 H HD23 . LEU A 1 34 ? -14.339 34.066 15.604 1.00 36.30 ? 42 LEU A HD23 1 ATOM 385 N N . GLN A 1 35 ? -17.831 30.457 16.417 1.00 23.49 ? 43 GLN A N 1 ATOM 386 C CA . GLN A 1 35 ? -18.408 29.373 17.204 1.00 24.27 ? 43 GLN A CA 1 ATOM 387 C C . GLN A 1 35 ? -18.081 28.007 16.606 1.00 21.24 ? 43 GLN A C 1 ATOM 388 O O . GLN A 1 35 ? -18.807 27.032 16.826 1.00 22.63 ? 43 GLN A O 1 ATOM 389 C CB . GLN A 1 35 ? -19.912 29.563 17.356 1.00 28.40 ? 43 GLN A CB 1 ATOM 390 C CG . GLN A 1 35 ? -20.282 30.786 18.188 1.00 33.54 ? 43 GLN A CG 1 ATOM 391 C CD . GLN A 1 35 ? -21.776 30.985 18.287 1.00 39.89 ? 43 GLN A CD 1 ATOM 392 O OE1 . GLN A 1 35 ? -22.555 30.244 17.682 1.00 43.62 ? 43 GLN A OE1 1 ATOM 393 N NE2 . GLN A 1 35 ? -22.188 31.984 19.050 1.00 39.70 ? 43 GLN A NE2 1 ATOM 394 H H . GLN A 1 35 ? -18.053 30.434 15.587 1.00 28.19 ? 43 GLN A H 1 ATOM 395 H HA . GLN A 1 35 ? -18.021 29.400 18.093 1.00 29.13 ? 43 GLN A HA 1 ATOM 396 H HB2 . GLN A 1 35 ? -20.306 29.670 16.476 1.00 34.08 ? 43 GLN A HB2 1 ATOM 397 H HB3 . GLN A 1 35 ? -20.285 28.781 17.792 1.00 34.08 ? 43 GLN A HB3 1 ATOM 398 H HG2 . GLN A 1 35 ? -19.933 30.676 19.087 1.00 40.24 ? 43 GLN A HG2 1 ATOM 399 H HG3 . GLN A 1 35 ? -19.899 31.577 17.777 1.00 40.24 ? 43 GLN A HG3 1 ATOM 400 H HE21 . GLN A 1 35 ? -21.614 32.478 19.458 1.00 47.64 ? 43 GLN A HE21 1 ATOM 401 H HE22 . GLN A 1 35 ? -23.029 32.138 19.139 1.00 47.64 ? 43 GLN A HE22 1 ATOM 402 N N . VAL A 1 36 ? -16.976 27.928 15.863 1.00 18.57 ? 44 VAL A N 1 ATOM 403 C CA . VAL A 1 36 ? -16.460 26.647 15.382 1.00 17.76 ? 44 VAL A CA 1 ATOM 404 C C . VAL A 1 36 ? -15.714 25.913 16.483 1.00 15.55 ? 44 VAL A C 1 ATOM 405 O O . VAL A 1 36 ? -15.953 24.730 16.730 1.00 16.23 ? 44 VAL A O 1 ATOM 406 C CB . VAL A 1 36 ? -15.559 26.860 14.156 1.00 17.09 ? 44 VAL A CB 1 ATOM 407 C CG1 . VAL A 1 36 ? -14.895 25.554 13.747 1.00 18.13 ? 44 VAL A CG1 1 ATOM 408 C CG2 . VAL A 1 36 ? -16.363 27.435 12.998 1.00 19.17 ? 44 VAL A CG2 1 ATOM 409 H H . VAL A 1 36 ? -16.505 28.606 15.622 1.00 22.28 ? 44 VAL A H 1 ATOM 410 H HA . VAL A 1 36 ? -17.207 26.092 15.108 1.00 21.31 ? 44 VAL A HA 1 ATOM 411 H HB . VAL A 1 36 ? -14.861 27.494 14.382 1.00 20.50 ? 44 VAL A HB 1 ATOM 412 H HG11 . VAL A 1 36 ? -14.333 25.715 12.973 1.00 21.76 ? 44 VAL A HG11 1 ATOM 413 H HG12 . VAL A 1 36 ? -14.357 25.230 14.486 1.00 21.76 ? 44 VAL A HG12 1 ATOM 414 H HG13 . VAL A 1 36 ? -15.583 24.906 13.528 1.00 21.76 ? 44 VAL A HG13 1 ATOM 415 H HG21 . VAL A 1 36 ? -15.775 27.561 12.237 1.00 23.01 ? 44 VAL A HG21 1 ATOM 416 H HG22 . VAL A 1 36 ? -17.074 26.816 12.769 1.00 23.01 ? 44 VAL A HG22 1 ATOM 417 H HG23 . VAL A 1 36 ? -16.741 28.287 13.269 1.00 23.01 ? 44 VAL A HG23 1 ATOM 418 N N . CYS A 1 37 ? -14.786 26.581 17.150 1.00 16.37 ? 45 CYS A N 1 ATOM 419 C CA . CYS A 1 37 ? -13.978 25.872 18.129 1.00 15.37 ? 45 CYS A CA 1 ATOM 420 C C . CYS A 1 37 ? -13.461 26.853 19.173 1.00 14.90 ? 45 CYS A C 1 ATOM 421 O O . CYS A 1 37 ? -12.800 27.835 18.812 1.00 16.40 ? 45 CYS A O 1 ATOM 422 C CB . CYS A 1 37 ? -12.806 25.142 17.457 1.00 14.51 ? 45 CYS A CB 1 ATOM 423 S SG . CYS A 1 37 ? -11.589 26.277 16.700 1.00 15.78 ? 45 CYS A SG 1 ATOM 424 H H . CYS A 1 37 ? -14.607 27.417 17.060 1.00 19.64 ? 45 CYS A H 1 ATOM 425 H HA . CYS A 1 37 ? -14.528 25.211 18.579 1.00 18.45 ? 45 CYS A HA 1 ATOM 426 H HB2 . CYS A 1 37 ? -12.344 24.609 18.122 1.00 17.41 ? 45 CYS A HB2 1 ATOM 427 H HB3 . CYS A 1 37 ? -13.154 24.568 16.757 1.00 17.41 ? 45 CYS A HB3 1 ATOM 428 N N . PRO A 1 38 ? -13.722 26.635 20.469 1.00 15.30 ? 46 PRO A N 1 ATOM 429 C CA . PRO A 1 38 ? -13.220 27.591 21.468 1.00 15.32 ? 46 PRO A CA 1 ATOM 430 C C . PRO A 1 38 ? -11.709 27.659 21.498 1.00 15.98 ? 46 PRO A C 1 ATOM 431 O O . PRO A 1 38 ? -11.156 28.679 21.912 1.00 16.55 ? 46 PRO A O 1 ATOM 432 C CB . PRO A 1 38 ? -13.797 27.069 22.793 1.00 17.43 ? 46 PRO A CB 1 ATOM 433 C CG . PRO A 1 38 ? -14.048 25.596 22.554 1.00 19.22 ? 46 PRO A CG 1 ATOM 434 C CD . PRO A 1 38 ? -14.524 25.567 21.092 1.00 16.42 ? 46 PRO A CD 1 ATOM 435 H HA . PRO A 1 38 ? -13.575 28.477 21.292 1.00 18.38 ? 46 PRO A HA 1 ATOM 436 H HB2 . PRO A 1 38 ? -13.150 27.197 23.504 1.00 20.92 ? 46 PRO A HB2 1 ATOM 437 H HB3 . PRO A 1 38 ? -14.626 27.531 22.994 1.00 20.92 ? 46 PRO A HB3 1 ATOM 438 H HG2 . PRO A 1 38 ? -13.225 25.095 22.663 1.00 23.06 ? 46 PRO A HG2 1 ATOM 439 H HG3 . PRO A 1 38 ? -14.739 25.273 23.153 1.00 23.06 ? 46 PRO A HG3 1 ATOM 440 H HD2 . PRO A 1 38 ? -14.324 24.710 20.685 1.00 19.71 ? 46 PRO A HD2 1 ATOM 441 H HD3 . PRO A 1 38 ? -15.470 25.777 21.038 1.00 19.71 ? 46 PRO A HD3 1 ATOM 442 N N . SER A 1 39 ? -11.019 26.610 21.047 1.00 14.71 ? 47 SER A N 1 ATOM 443 C CA . SER A 1 39 ? -9.567 26.602 21.043 1.00 14.04 ? 47 SER A CA 1 ATOM 444 C C . SER A 1 39 ? -8.970 27.621 20.075 1.00 14.24 ? 47 SER A C 1 ATOM 445 O O . SER A 1 39 ? -7.775 27.899 20.177 1.00 15.34 ? 47 SER A O 1 ATOM 446 C CB . SER A 1 39 ? -9.072 25.187 20.760 1.00 14.24 ? 47 SER A CB 1 ATOM 447 O OG . SER A 1 39 ? -9.608 24.674 19.548 1.00 14.32 ? 47 SER A OG 1 ATOM 448 H H . SER A 1 39 ? -11.375 25.891 20.737 1.00 17.65 ? 47 SER A H 1 ATOM 449 H HA . SER A 1 39 ? -9.261 26.840 21.932 1.00 16.84 ? 47 SER A HA 1 ATOM 450 H HB2 . SER A 1 39 ? -8.105 25.201 20.693 1.00 17.09 ? 47 SER A HB2 1 ATOM 451 H HB3 . SER A 1 39 ? -9.343 24.609 21.491 1.00 17.09 ? 47 SER A HB3 1 ATOM 452 H HG . SER A 1 39 ? -10.446 24.653 19.591 1.00 17.19 ? 47 SER A HG 1 ATOM 453 N N . ALA A 1 40 ? -9.750 28.177 19.149 1.00 14.85 ? 48 ALA A N 1 ATOM 454 C CA . ALA A 1 40 ? -9.264 29.240 18.282 1.00 14.83 ? 48 ALA A CA 1 ATOM 455 C C . ALA A 1 40 ? -9.380 30.619 18.922 1.00 16.19 ? 48 ALA A C 1 ATOM 456 O O . ALA A 1 40 ? -8.970 31.612 18.312 1.00 16.95 ? 48 ALA A O 1 ATOM 457 C CB . ALA A 1 40 ? -10.026 29.233 16.956 1.00 16.07 ? 48 ALA A CB 1 ATOM 458 H H . ALA A 1 40 ? -10.568 27.952 19.005 1.00 17.82 ? 48 ALA A H 1 ATOM 459 H HA . ALA A 1 40 ? -8.327 29.081 18.088 1.00 17.79 ? 48 ALA A HA 1 ATOM 460 H HB1 . ALA A 1 40 ? -9.688 29.947 16.394 1.00 19.28 ? 48 ALA A HB1 1 ATOM 461 H HB2 . ALA A 1 40 ? -9.892 28.377 16.520 1.00 19.28 ? 48 ALA A HB2 1 ATOM 462 H HB3 . ALA A 1 40 ? -10.970 29.370 17.134 1.00 19.28 ? 48 ALA A HB3 1 ATOM 463 N N . GLY A 1 41 ? -9.926 30.715 20.128 1.00 17.24 ? 49 GLY A N 1 ATOM 464 C CA . GLY A 1 41 ? -10.059 32.019 20.753 1.00 18.97 ? 49 GLY A CA 1 ATOM 465 C C . GLY A 1 41 ? -10.974 32.906 19.949 1.00 20.17 ? 49 GLY A C 1 ATOM 466 O O . GLY A 1 41 ? -12.072 32.504 19.561 1.00 21.50 ? 49 GLY A O 1 ATOM 467 H H . GLY A 1 41 ? -10.222 30.056 20.594 1.00 20.69 ? 49 GLY A H 1 ATOM 468 H HA2 . GLY A 1 41 ? -10.425 31.920 21.646 1.00 22.77 ? 49 GLY A HA2 1 ATOM 469 H HA3 . GLY A 1 41 ? -9.189 32.443 20.817 1.00 22.77 ? 49 GLY A HA3 1 ATOM 470 N N . SER A 1 42 ? -10.510 34.116 19.669 1.00 22.23 ? 50 SER A N 1 ATOM 471 C CA A SER A 1 42 ? -11.260 35.101 18.906 0.52 23.94 ? 50 SER A CA 1 ATOM 472 C CA B SER A 1 42 ? -11.261 35.100 18.903 0.48 23.75 ? 50 SER A CA 1 ATOM 473 C C . SER A 1 42 ? -10.912 35.089 17.419 1.00 22.42 ? 50 SER A C 1 ATOM 474 O O . SER A 1 42 ? -11.394 35.954 16.675 1.00 26.68 ? 50 SER A O 1 ATOM 475 C CB A SER A 1 42 ? -11.027 36.498 19.491 0.52 25.83 ? 50 SER A CB 1 ATOM 476 C CB B SER A 1 42 ? -11.026 36.501 19.473 0.48 25.50 ? 50 SER A CB 1 ATOM 477 O OG A SER A 1 42 ? -9.642 36.752 19.649 0.52 28.41 ? 50 SER A OG 1 ATOM 478 O OG B SER A 1 42 ? -11.340 36.535 20.848 0.48 28.33 ? 50 SER A OG 1 ATOM 479 H H . SER A 1 42 ? -9.737 34.396 19.923 1.00 26.68 ? 50 SER A H 1 ATOM 480 H HA . SER A 1 42 ? -12.207 34.901 18.986 1.00 28.50 ? 50 SER A HA 1 ATOM 481 H HB2 A SER A 1 42 ? -11.404 37.160 18.890 0.52 31.00 ? 50 SER A HB2 1 ATOM 482 H HB2 B SER A 1 42 ? -10.094 36.739 19.355 0.48 30.60 ? 50 SER A HB2 1 ATOM 483 H HB3 A SER A 1 42 ? -11.459 36.554 20.358 0.52 31.00 ? 50 SER A HB3 1 ATOM 484 H HB3 B SER A 1 42 ? -11.593 37.133 19.003 0.48 30.60 ? 50 SER A HB3 1 ATOM 485 H HG A SER A 1 42 ? -9.303 36.185 20.168 0.52 34.10 ? 50 SER A HG 1 ATOM 486 H HG B SER A 1 42 ? -10.856 35.990 21.267 0.48 34.00 ? 50 SER A HG 1 ATOM 487 N N . GLN A 1 43 ? -10.095 34.145 16.974 1.00 21.09 ? 51 GLN A N 1 ATOM 488 C CA . GLN A 1 43 ? -9.710 34.060 15.567 1.00 20.98 ? 51 GLN A CA 1 ATOM 489 C C . GLN A 1 43 ? -10.881 33.520 14.754 1.00 21.52 ? 51 GLN A C 1 ATOM 490 O O . GLN A 1 43 ? -11.359 32.417 15.040 1.00 21.80 ? 51 GLN A O 1 ATOM 491 C CB . GLN A 1 43 ? -8.526 33.116 15.389 1.00 20.24 ? 51 GLN A CB 1 ATOM 492 C CG . GLN A 1 43 ? -7.242 33.570 16.041 1.00 21.07 ? 51 GLN A CG 1 ATOM 493 C CD . GLN A 1 43 ? -6.194 32.478 16.062 1.00 21.62 ? 51 GLN A CD 1 ATOM 494 O OE1 . GLN A 1 43 ? -5.166 32.567 15.396 1.00 23.62 ? 51 GLN A OE1 1 ATOM 495 N NE2 . GLN A 1 43 ? -6.457 31.436 16.825 1.00 19.87 ? 51 GLN A NE2 1 ATOM 496 H H . GLN A 1 43 ? -9.745 33.534 17.469 1.00 25.31 ? 51 GLN A H 1 ATOM 497 H HA . GLN A 1 43 ? -9.470 34.939 15.233 1.00 25.18 ? 51 GLN A HA 1 ATOM 498 H HB2 . GLN A 1 43 ? -8.759 32.255 15.770 1.00 24.29 ? 51 GLN A HB2 1 ATOM 499 H HB3 . GLN A 1 43 ? -8.352 33.016 14.440 1.00 24.29 ? 51 GLN A HB3 1 ATOM 500 H HG2 . GLN A 1 43 ? -6.883 34.323 15.545 1.00 25.29 ? 51 GLN A HG2 1 ATOM 501 H HG3 . GLN A 1 43 ? -7.425 33.830 16.957 1.00 25.29 ? 51 GLN A HG3 1 ATOM 502 H HE21 . GLN A 1 43 ? -7.190 31.405 17.274 1.00 23.84 ? 51 GLN A HE21 1 ATOM 503 H HE22 . GLN A 1 43 ? -5.895 30.787 16.875 1.00 23.84 ? 51 GLN A HE22 1 ATOM 504 N N . PRO A 1 44 ? -11.345 34.216 13.722 1.00 22.16 ? 52 PRO A N 1 ATOM 505 C CA . PRO A 1 44 ? -12.425 33.665 12.896 1.00 22.97 ? 52 PRO A CA 1 ATOM 506 C C . PRO A 1 44 ? -11.975 32.412 12.163 1.00 20.96 ? 52 PRO A C 1 ATOM 507 O O . PRO A 1 44 ? -10.894 32.371 11.576 1.00 22.15 ? 52 PRO A O 1 ATOM 508 C CB . PRO A 1 44 ? -12.726 34.802 11.914 1.00 24.50 ? 52 PRO A CB 1 ATOM 509 C CG . PRO A 1 44 ? -12.249 36.021 12.601 1.00 25.16 ? 52 PRO A CG 1 ATOM 510 C CD . PRO A 1 44 ? -11.060 35.621 13.383 1.00 23.16 ? 52 PRO A CD 1 ATOM 511 H HA . PRO A 1 44 ? -13.211 33.473 13.432 1.00 27.57 ? 52 PRO A HA 1 ATOM 512 H HB2 . PRO A 1 44 ? -12.239 34.659 11.087 1.00 29.40 ? 52 PRO A HB2 1 ATOM 513 H HB3 . PRO A 1 44 ? -13.680 34.850 11.748 1.00 29.40 ? 52 PRO A HB3 1 ATOM 514 H HG2 . PRO A 1 44 ? -12.012 36.692 11.942 1.00 30.19 ? 52 PRO A HG2 1 ATOM 515 H HG3 . PRO A 1 44 ? -12.946 36.353 13.189 1.00 30.19 ? 52 PRO A HG3 1 ATOM 516 H HD2 . PRO A 1 44 ? -10.259 35.683 12.839 1.00 27.79 ? 52 PRO A HD2 1 ATOM 517 H HD3 . PRO A 1 44 ? -10.987 36.157 14.188 1.00 27.79 ? 52 PRO A HD3 1 ATOM 518 N N . VAL A 1 45 ? -12.812 31.383 12.200 1.00 19.29 ? 53 VAL A N 1 ATOM 519 C CA . VAL A 1 45 ? -12.532 30.110 11.546 1.00 19.17 ? 53 VAL A CA 1 ATOM 520 C C . VAL A 1 45 ? -13.497 29.993 10.371 1.00 21.04 ? 53 VAL A C 1 ATOM 521 O O . VAL A 1 45 ? -14.676 29.677 10.547 1.00 22.45 ? 53 VAL A O 1 ATOM 522 C CB . VAL A 1 45 ? -12.668 28.924 12.504 1.00 18.87 ? 53 VAL A CB 1 ATOM 523 C CG1 . VAL A 1 45 ? -12.297 27.622 11.793 1.00 20.64 ? 53 VAL A CG1 1 ATOM 524 C CG2 . VAL A 1 45 ? -11.801 29.126 13.747 1.00 19.69 ? 53 VAL A CG2 1 ATOM 525 H H . VAL A 1 45 ? -13.569 31.398 12.608 1.00 23.15 ? 53 VAL A H 1 ATOM 526 H HA . VAL A 1 45 ? -11.626 30.119 11.198 1.00 23.00 ? 53 VAL A HA 1 ATOM 527 H HB . VAL A 1 45 ? -13.592 28.856 12.791 1.00 22.64 ? 53 VAL A HB 1 ATOM 528 H HG11 . VAL A 1 45 ? -12.390 26.885 12.417 1.00 24.77 ? 53 VAL A HG11 1 ATOM 529 H HG12 . VAL A 1 45 ? -12.893 27.494 11.038 1.00 24.77 ? 53 VAL A HG12 1 ATOM 530 H HG13 . VAL A 1 45 ? -11.380 27.681 11.484 1.00 24.77 ? 53 VAL A HG13 1 ATOM 531 H HG21 . VAL A 1 45 ? -11.907 28.361 14.334 1.00 23.63 ? 53 VAL A HG21 1 ATOM 532 H HG22 . VAL A 1 45 ? -10.873 29.208 13.475 1.00 23.63 ? 53 VAL A HG22 1 ATOM 533 H HG23 . VAL A 1 45 ? -12.085 29.935 14.202 1.00 23.63 ? 53 VAL A HG23 1 ATOM 534 N N . LEU A 1 46 ? -12.993 30.243 9.174 1.00 24.14 ? 54 LEU A N 1 ATOM 535 C CA . LEU A 1 46 ? -13.818 30.330 7.974 1.00 29.09 ? 54 LEU A CA 1 ATOM 536 C C . LEU A 1 46 ? -13.909 28.963 7.296 1.00 32.11 ? 54 LEU A C 1 ATOM 537 O O . LEU A 1 46 ? -12.920 28.233 7.202 1.00 32.50 ? 54 LEU A O 1 ATOM 538 C CB . LEU A 1 46 ? -13.204 31.367 7.031 1.00 32.10 ? 54 LEU A CB 1 ATOM 539 C CG . LEU A 1 46 ? -12.953 32.721 7.712 1.00 34.51 ? 54 LEU A CG 1 ATOM 540 C CD1 . LEU A 1 46 ? -12.104 33.645 6.859 1.00 36.18 ? 54 LEU A CD1 1 ATOM 541 C CD2 . LEU A 1 46 ? -14.275 33.385 8.063 1.00 35.56 ? 54 LEU A CD2 1 ATOM 542 H H . LEU A 1 46 ? -12.156 30.370 9.025 1.00 28.97 ? 54 LEU A H 1 ATOM 543 H HA . LEU A 1 46 ? -14.713 30.619 8.213 1.00 34.90 ? 54 LEU A HA 1 ATOM 544 H HB2 . LEU A 1 46 ? -12.354 31.033 6.706 1.00 38.52 ? 54 LEU A HB2 1 ATOM 545 H HB3 . LEU A 1 46 ? -13.809 31.514 6.287 1.00 38.52 ? 54 LEU A HB3 1 ATOM 546 H HG . LEU A 1 46 ? -12.474 32.566 8.541 1.00 41.42 ? 54 LEU A HG 1 ATOM 547 H HD11 . LEU A 1 46 ? -11.975 34.482 7.332 1.00 43.42 ? 54 LEU A HD11 1 ATOM 548 H HD12 . LEU A 1 46 ? -11.246 33.222 6.694 1.00 43.42 ? 54 LEU A HD12 1 ATOM 549 H HD13 . LEU A 1 46 ? -12.560 33.806 6.018 1.00 43.42 ? 54 LEU A HD13 1 ATOM 550 H HD21 . LEU A 1 46 ? -14.097 34.237 8.492 1.00 42.67 ? 54 LEU A HD21 1 ATOM 551 H HD22 . LEU A 1 46 ? -14.784 33.524 7.249 1.00 42.67 ? 54 LEU A HD22 1 ATOM 552 H HD23 . LEU A 1 46 ? -14.768 32.807 8.667 1.00 42.67 ? 54 LEU A HD23 1 ATOM 553 N N . ASN A 1 47 ? -15.108 28.620 6.839 1.00 38.24 ? 55 ASN A N 1 ATOM 554 C CA . ASN A 1 47 ? -15.389 27.351 6.152 1.00 41.73 ? 55 ASN A CA 1 ATOM 555 C C . ASN A 1 47 ? -14.651 26.162 6.780 1.00 38.39 ? 55 ASN A C 1 ATOM 556 O O . ASN A 1 47 ? -13.886 25.450 6.129 1.00 38.61 ? 55 ASN A O 1 ATOM 557 C CB . ASN A 1 47 ? -15.106 27.449 4.657 1.00 48.20 ? 55 ASN A CB 1 ATOM 558 C CG . ASN A 1 47 ? -15.923 26.454 3.849 1.00 53.97 ? 55 ASN A CG 1 ATOM 559 O OD1 . ASN A 1 47 ? -17.129 26.632 3.664 1.00 56.50 ? 55 ASN A OD1 1 ATOM 560 N ND2 . ASN A 1 47 ? -15.274 25.401 3.368 1.00 55.57 ? 55 ASN A ND2 1 ATOM 561 H H . ASN A 1 47 ? -15.803 29.121 6.915 1.00 45.88 ? 55 ASN A H 1 ATOM 562 H HA . ASN A 1 47 ? -16.338 27.171 6.245 1.00 50.08 ? 55 ASN A HA 1 ATOM 563 H HB2 . ASN A 1 47 ? -15.328 28.342 4.349 1.00 57.84 ? 55 ASN A HB2 1 ATOM 564 H HB3 . ASN A 1 47 ? -14.166 27.266 4.499 1.00 57.84 ? 55 ASN A HB3 1 ATOM 565 H HD21 . ASN A 1 47 ? -15.695 24.812 2.905 1.00 66.68 ? 55 ASN A HD21 1 ATOM 566 H HD22 . ASN A 1 47 ? -14.432 25.309 3.519 1.00 66.68 ? 55 ASN A HD22 1 ATOM 567 N N . ALA A 1 48 ? -14.937 25.930 8.059 1.00 34.28 ? 56 ALA A N 1 ATOM 568 C CA . ALA A 1 48 ? -14.319 24.821 8.783 1.00 29.51 ? 56 ALA A CA 1 ATOM 569 C C . ALA A 1 48 ? -14.736 23.479 8.194 1.00 25.65 ? 56 ALA A C 1 ATOM 570 O O . ALA A 1 48 ? -15.873 23.301 7.741 1.00 28.28 ? 56 ALA A O 1 ATOM 571 C CB . ALA A 1 48 ? -14.729 24.866 10.249 1.00 30.80 ? 56 ALA A CB 1 ATOM 572 H H . ALA A 1 48 ? -15.484 26.398 8.529 1.00 41.13 ? 56 ALA A H 1 ATOM 573 H HA . ALA A 1 48 ? -13.353 24.896 8.729 1.00 35.41 ? 56 ALA A HA 1 ATOM 574 H HB1 . ALA A 1 48 ? -14.311 24.126 10.716 1.00 36.96 ? 56 ALA A HB1 1 ATOM 575 H HB2 . ALA A 1 48 ? -14.435 25.707 10.633 1.00 36.96 ? 56 ALA A HB2 1 ATOM 576 H HB3 . ALA A 1 48 ? -15.694 24.794 10.309 1.00 36.96 ? 56 ALA A HB3 1 ATOM 577 N N . GLY A 1 49 ? -13.806 22.531 8.209 1.00 21.70 ? 57 GLY A N 1 ATOM 578 C CA . GLY A 1 49 ? -14.062 21.209 7.680 1.00 19.48 ? 57 GLY A CA 1 ATOM 579 C C . GLY A 1 49 ? -14.227 20.149 8.750 1.00 16.58 ? 57 GLY A C 1 ATOM 580 O O . GLY A 1 49 ? -13.970 20.387 9.930 1.00 18.07 ? 57 GLY A O 1 ATOM 581 H H . GLY A 1 49 ? -13.013 22.634 8.525 1.00 26.04 ? 57 GLY A H 1 ATOM 582 H HA2 . GLY A 1 49 ? -14.872 21.230 7.147 1.00 23.38 ? 57 GLY A HA2 1 ATOM 583 H HA3 . GLY A 1 49 ? -13.327 20.947 7.105 1.00 23.38 ? 57 GLY A HA3 1 ATOM 584 N N . PRO A 1 50 ? -14.633 18.942 8.351 1.00 17.66 ? 58 PRO A N 1 ATOM 585 C CA . PRO A 1 50 ? -14.988 17.923 9.349 1.00 19.32 ? 58 PRO A CA 1 ATOM 586 C C . PRO A 1 50 ? -13.800 17.331 10.079 1.00 16.54 ? 58 PRO A C 1 ATOM 587 O O . PRO A 1 50 ? -13.957 16.771 11.179 1.00 18.72 ? 58 PRO A O 1 ATOM 588 C CB . PRO A 1 50 ? -15.720 16.859 8.514 1.00 23.00 ? 58 PRO A CB 1 ATOM 589 C CG . PRO A 1 50 ? -15.174 17.026 7.142 1.00 23.79 ? 58 PRO A CG 1 ATOM 590 C CD . PRO A 1 50 ? -14.971 18.518 6.981 1.00 20.19 ? 58 PRO A CD 1 ATOM 591 H HA . PRO A 1 50 ? -15.605 18.295 9.998 1.00 23.18 ? 58 PRO A HA 1 ATOM 592 H HB2 . PRO A 1 50 ? -15.520 15.975 8.860 1.00 27.60 ? 58 PRO A HB2 1 ATOM 593 H HB3 . PRO A 1 50 ? -16.674 17.028 8.529 1.00 27.60 ? 58 PRO A HB3 1 ATOM 594 H HG2 . PRO A 1 50 ? -14.330 16.554 7.065 1.00 28.55 ? 58 PRO A HG2 1 ATOM 595 H HG3 . PRO A 1 50 ? -15.813 16.694 6.492 1.00 28.55 ? 58 PRO A HG3 1 ATOM 596 H HD2 . PRO A 1 50 ? -14.234 18.698 6.377 1.00 24.23 ? 58 PRO A HD2 1 ATOM 597 H HD3 . PRO A 1 50 ? -15.791 18.943 6.685 1.00 24.23 ? 58 PRO A HD3 1 ATOM 598 N N . TRP A 1 51 ? -12.609 17.395 9.507 1.00 14.46 ? 59 TRP A N 1 ATOM 599 C CA . TRP A 1 51 ? -11.466 16.744 10.114 1.00 13.97 ? 59 TRP A CA 1 ATOM 600 C C . TRP A 1 51 ? -10.619 17.684 10.951 1.00 13.59 ? 59 TRP A C 1 ATOM 601 O O . TRP A 1 51 ? -9.625 17.243 11.542 1.00 15.72 ? 59 TRP A O 1 ATOM 602 C CB . TRP A 1 51 ? -10.616 16.024 9.060 1.00 15.83 ? 59 TRP A CB 1 ATOM 603 C CG . TRP A 1 51 ? -11.409 15.298 8.058 1.00 16.99 ? 59 TRP A CG 1 ATOM 604 C CD1 . TRP A 1 51 ? -11.337 15.489 6.727 1.00 20.79 ? 59 TRP A CD1 1 ATOM 605 C CD2 . TRP A 1 51 ? -12.432 14.305 8.266 1.00 20.80 ? 59 TRP A CD2 1 ATOM 606 N NE1 . TRP A 1 51 ? -12.217 14.693 6.083 1.00 22.32 ? 59 TRP A NE1 1 ATOM 607 C CE2 . TRP A 1 51 ? -12.914 13.959 6.989 1.00 21.67 ? 59 TRP A CE2 1 ATOM 608 C CE3 . TRP A 1 51 ? -13.001 13.698 9.383 1.00 24.61 ? 59 TRP A CE3 1 ATOM 609 C CZ2 . TRP A 1 51 ? -13.924 13.034 6.785 1.00 27.36 ? 59 TRP A CZ2 1 ATOM 610 C CZ3 . TRP A 1 51 ? -14.016 12.759 9.174 1.00 27.78 ? 59 TRP A CZ3 1 ATOM 611 C CH2 . TRP A 1 51 ? -14.452 12.434 7.885 1.00 27.96 ? 59 TRP A CH2 1 ATOM 612 H H . TRP A 1 51 ? -12.438 17.806 8.771 1.00 17.35 ? 59 TRP A H 1 ATOM 613 H HA . TRP A 1 51 ? -11.801 16.061 10.716 1.00 16.76 ? 59 TRP A HA 1 ATOM 614 H HB2 . TRP A 1 51 ? -10.075 16.679 8.593 1.00 18.99 ? 59 TRP A HB2 1 ATOM 615 H HB3 . TRP A 1 51 ? -10.042 15.381 9.507 1.00 18.99 ? 59 TRP A HB3 1 ATOM 616 H HD1 . TRP A 1 51 ? -10.752 16.078 6.308 1.00 24.95 ? 59 TRP A HD1 1 ATOM 617 H HE1 . TRP A 1 51 ? -12.324 14.659 5.230 1.00 26.78 ? 59 TRP A HE1 1 ATOM 618 H HE3 . TRP A 1 51 ? -12.716 13.912 10.241 1.00 29.53 ? 59 TRP A HE3 1 ATOM 619 H HZ2 . TRP A 1 51 ? -14.211 12.811 5.929 1.00 32.83 ? 59 TRP A HZ2 1 ATOM 620 H HZ3 . TRP A 1 51 ? -14.400 12.333 9.906 1.00 33.33 ? 59 TRP A HZ3 1 ATOM 621 H HH2 . TRP A 1 51 ? -15.125 11.801 7.778 1.00 33.56 ? 59 TRP A HH2 1 ATOM 622 N N . GLY A 1 52 ? -11.013 18.947 11.051 1.00 14.06 ? 60 GLY A N 1 ATOM 623 C CA . GLY A 1 52 ? -10.294 19.926 11.839 1.00 14.10 ? 60 GLY A CA 1 ATOM 624 C C . GLY A 1 52 ? -9.999 21.174 11.036 1.00 14.12 ? 60 GLY A C 1 ATOM 625 O O . GLY A 1 52 ? -10.367 21.304 9.865 1.00 15.68 ? 60 GLY A O 1 ATOM 626 H H . GLY A 1 52 ? -11.711 19.265 10.661 1.00 16.87 ? 60 GLY A H 1 ATOM 627 H HA2 . GLY A 1 52 ? -10.822 20.173 12.614 1.00 16.92 ? 60 GLY A HA2 1 ATOM 628 H HA3 . GLY A 1 52 ? -9.455 19.547 12.143 1.00 16.92 ? 60 GLY A HA3 1 ATOM 629 N N . ASP A 1 53 ? -9.299 22.099 11.690 1.00 13.83 ? 61 ASP A N 1 ATOM 630 C CA . ASP A 1 53 ? -8.912 23.366 11.103 1.00 13.30 ? 61 ASP A CA 1 ATOM 631 C C . ASP A 1 53 ? -7.584 23.748 11.724 1.00 13.37 ? 61 ASP A C 1 ATOM 632 O O . ASP A 1 53 ? -7.357 23.471 12.901 1.00 13.03 ? 61 ASP A O 1 ATOM 633 C CB . ASP A 1 53 ? -9.920 24.471 11.400 1.00 14.46 ? 61 ASP A CB 1 ATOM 634 C CG . ASP A 1 53 ? -9.676 25.698 10.557 1.00 15.66 ? 61 ASP A CG 1 ATOM 635 O OD1 . ASP A 1 53 ? -8.902 26.558 11.007 1.00 17.12 ? 61 ASP A OD1 1 ATOM 636 O OD2 . ASP A 1 53 ? -10.264 25.774 9.447 1.00 18.77 ? 61 ASP A OD2 1 ATOM 637 H H . ASP A 1 53 ? -9.031 22.006 12.502 1.00 16.60 ? 61 ASP A H 1 ATOM 638 H HA . ASP A 1 53 ? -8.805 23.276 10.143 1.00 15.96 ? 61 ASP A HA 1 ATOM 639 H HB2 . ASP A 1 53 ? -10.814 24.147 11.210 1.00 17.36 ? 61 ASP A HB2 1 ATOM 640 H HB3 . ASP A 1 53 ? -9.847 24.726 12.333 1.00 17.36 ? 61 ASP A HB3 1 ATOM 641 N N . TYR A 1 54 ? -6.711 24.381 10.945 1.00 13.32 ? 62 TYR A N 1 ATOM 642 C CA . TYR A 1 54 ? -5.396 24.744 11.472 1.00 12.97 ? 62 TYR A CA 1 ATOM 643 C C . TYR A 1 54 ? -5.461 25.699 12.652 1.00 12.71 ? 62 TYR A C 1 ATOM 644 O O . TYR A 1 54 ? -4.498 25.758 13.413 1.00 14.44 ? 62 TYR A O 1 ATOM 645 C CB . TYR A 1 54 ? -4.500 25.307 10.373 1.00 13.58 ? 62 TYR A CB 1 ATOM 646 C CG . TYR A 1 54 ? -4.098 24.293 9.322 1.00 13.52 ? 62 TYR A CG 1 ATOM 647 C CD1 . TYR A 1 54 ? -3.278 23.226 9.638 1.00 12.88 ? 62 TYR A CD1 1 ATOM 648 C CD2 . TYR A 1 54 ? -4.555 24.404 8.012 1.00 14.89 ? 62 TYR A CD2 1 ATOM 649 C CE1 . TYR A 1 54 ? -2.899 22.316 8.694 1.00 12.12 ? 62 TYR A CE1 1 ATOM 650 C CE2 . TYR A 1 54 ? -4.180 23.505 7.031 1.00 14.88 ? 62 TYR A CE2 1 ATOM 651 C CZ . TYR A 1 54 ? -3.362 22.449 7.382 1.00 12.80 ? 62 TYR A CZ 1 ATOM 652 O OH . TYR A 1 54 ? -3.015 21.552 6.381 1.00 15.04 ? 62 TYR A OH 1 ATOM 653 H H . TYR A 1 54 ? -6.849 24.607 10.127 1.00 15.98 ? 62 TYR A H 1 ATOM 654 H HA . TYR A 1 54 ? -4.971 23.933 11.792 1.00 15.56 ? 62 TYR A HA 1 ATOM 655 H HB2 . TYR A 1 54 ? -4.971 26.027 9.925 1.00 16.29 ? 62 TYR A HB2 1 ATOM 656 H HB3 . TYR A 1 54 ? -3.688 25.650 10.778 1.00 16.29 ? 62 TYR A HB3 1 ATOM 657 H HD1 . TYR A 1 54 ? -2.965 23.136 10.509 1.00 15.46 ? 62 TYR A HD1 1 ATOM 658 H HD2 . TYR A 1 54 ? -5.102 25.121 7.783 1.00 17.87 ? 62 TYR A HD2 1 ATOM 659 H HE1 . TYR A 1 54 ? -2.345 21.605 8.924 1.00 14.54 ? 62 TYR A HE1 1 ATOM 660 H HE2 . TYR A 1 54 ? -4.494 23.594 6.160 1.00 17.86 ? 62 TYR A HE2 1 ATOM 661 H HH . TYR A 1 54 ? -2.510 20.957 6.692 1.00 18.04 ? 62 TYR A HH 1 ATOM 662 N N . LEU A 1 55 ? -6.556 26.439 12.838 1.00 13.26 ? 63 LEU A N 1 ATOM 663 C CA . LEU A 1 55 ? -6.706 27.335 13.980 1.00 13.51 ? 63 LEU A CA 1 ATOM 664 C C . LEU A 1 55 ? -7.222 26.628 15.229 1.00 13.12 ? 63 LEU A C 1 ATOM 665 O O . LEU A 1 55 ? -7.196 27.230 16.307 1.00 14.10 ? 63 LEU A O 1 ATOM 666 C CB . LEU A 1 55 ? -7.647 28.496 13.638 1.00 14.72 ? 63 LEU A CB 1 ATOM 667 C CG . LEU A 1 55 ? -7.154 29.383 12.509 1.00 16.70 ? 63 LEU A CG 1 ATOM 668 C CD1 . LEU A 1 55 ? -8.214 30.415 12.183 1.00 19.78 ? 63 LEU A CD1 1 ATOM 669 C CD2 . LEU A 1 55 ? -5.850 30.041 12.861 1.00 20.40 ? 63 LEU A CD2 1 ATOM 670 H H . LEU A 1 55 ? -7.234 26.437 12.308 1.00 15.92 ? 63 LEU A H 1 ATOM 671 H HA . LEU A 1 55 ? -5.838 27.711 14.194 1.00 16.21 ? 63 LEU A HA 1 ATOM 672 H HB2 . LEU A 1 55 ? -8.507 28.134 13.375 1.00 17.67 ? 63 LEU A HB2 1 ATOM 673 H HB3 . LEU A 1 55 ? -7.753 29.053 14.426 1.00 17.67 ? 63 LEU A HB3 1 ATOM 674 H HG . LEU A 1 55 ? -7.012 28.839 11.718 1.00 20.04 ? 63 LEU A HG 1 ATOM 675 H HD11 . LEU A 1 55 ? -7.895 30.978 11.461 1.00 23.74 ? 63 LEU A HD11 1 ATOM 676 H HD12 . LEU A 1 55 ? -9.026 29.958 11.913 1.00 23.74 ? 63 LEU A HD12 1 ATOM 677 H HD13 . LEU A 1 55 ? -8.384 30.952 12.973 1.00 23.74 ? 63 LEU A HD13 1 ATOM 678 H HD21 . LEU A 1 55 ? -5.567 30.597 12.118 1.00 24.47 ? 63 LEU A HD21 1 ATOM 679 H HD22 . LEU A 1 55 ? -5.975 30.586 13.653 1.00 24.47 ? 63 LEU A HD22 1 ATOM 680 H HD23 . LEU A 1 55 ? -5.186 29.355 13.032 1.00 24.47 ? 63 LEU A HD23 1 ATOM 681 N N . CYS A 1 56 ? -7.711 25.402 15.101 1.00 13.31 ? 64 CYS A N 1 ATOM 682 C CA . CYS A 1 56 ? -8.395 24.697 16.175 1.00 12.70 ? 64 CYS A CA 1 ATOM 683 C C . CYS A 1 56 ? -7.581 23.510 16.675 1.00 11.85 ? 64 CYS A C 1 ATOM 684 O O . CYS A 1 56 ? -6.788 22.906 15.942 1.00 12.12 ? 64 CYS A O 1 ATOM 685 C CB . CYS A 1 56 ? -9.723 24.141 15.651 1.00 13.52 ? 64 CYS A CB 1 ATOM 686 S SG . CYS A 1 56 ? -10.924 25.316 15.035 1.00 14.68 ? 64 CYS A SG 1 ATOM 687 H H . CYS A 1 56 ? -7.656 24.943 14.376 1.00 15.97 ? 64 CYS A H 1 ATOM 688 H HA . CYS A 1 56 ? -8.570 25.300 16.915 1.00 15.24 ? 64 CYS A HA 1 ATOM 689 H HB2 . CYS A 1 56 ? -9.526 23.529 14.925 1.00 16.23 ? 64 CYS A HB2 1 ATOM 690 H HB3 . CYS A 1 56 ? -10.149 23.652 16.372 1.00 16.23 ? 64 CYS A HB3 1 ATOM 691 N N . ASP A 1 57 ? -7.880 23.126 17.910 1.00 12.07 ? 65 ASP A N 1 ATOM 692 C CA . ASP A 1 57 ? -7.511 21.806 18.384 1.00 12.74 ? 65 ASP A CA 1 ATOM 693 C C . ASP A 1 57 ? -8.398 20.734 17.726 1.00 11.98 ? 65 ASP A C 1 ATOM 694 O O . ASP A 1 57 ? -9.316 21.019 16.956 1.00 11.96 ? 65 ASP A O 1 ATOM 695 C CB . ASP A 1 57 ? -7.569 21.769 19.914 1.00 12.31 ? 65 ASP A CB 1 ATOM 696 C CG . ASP A 1 57 ? -6.323 22.313 20.561 1.00 12.14 ? 65 ASP A CG 1 ATOM 697 O OD1 . ASP A 1 57 ? -5.192 21.968 20.120 1.00 12.44 ? 65 ASP A OD1 1 ATOM 698 O OD2 . ASP A 1 57 ? -6.482 23.069 21.541 1.00 13.58 ? 65 ASP A OD2 1 ATOM 699 H H . ASP A 1 57 ? -8.293 23.610 18.488 1.00 14.49 ? 65 ASP A H 1 ATOM 700 H HA . ASP A 1 57 ? -6.594 21.628 18.122 1.00 15.29 ? 65 ASP A HA 1 ATOM 701 H HB2 . ASP A 1 57 ? -8.321 22.304 20.214 1.00 14.77 ? 65 ASP A HB2 1 ATOM 702 H HB3 . ASP A 1 57 ? -7.680 20.850 20.203 1.00 14.77 ? 65 ASP A HB3 1 ATOM 703 N N . SER A 1 58 ? -8.069 19.480 17.983 1.00 12.42 ? 66 SER A N 1 ATOM 704 C CA . SER A 1 58 ? -8.562 18.353 17.193 1.00 11.62 ? 66 SER A CA 1 ATOM 705 C C . SER A 1 58 ? -10.044 18.084 17.446 1.00 11.15 ? 66 SER A C 1 ATOM 706 O O . SER A 1 58 ? -10.451 17.908 18.596 1.00 13.00 ? 66 SER A O 1 ATOM 707 C CB . SER A 1 58 ? -7.829 17.093 17.599 1.00 10.70 ? 66 SER A CB 1 ATOM 708 O OG . SER A 1 58 ? -6.444 17.188 17.413 1.00 11.45 ? 66 SER A OG 1 ATOM 709 H H . SER A 1 58 ? -7.548 19.245 18.626 1.00 14.91 ? 66 SER A H 1 ATOM 710 H HA . SER A 1 58 ? -8.422 18.516 16.247 1.00 13.94 ? 66 SER A HA 1 ATOM 711 H HB2 . SER A 1 58 ? -8.003 16.923 18.538 1.00 12.84 ? 66 SER A HB2 1 ATOM 712 H HB3 . SER A 1 58 ? -8.163 16.354 17.067 1.00 12.84 ? 66 SER A HB3 1 ATOM 713 H HG . SER A 1 58 ? -6.135 17.820 17.872 1.00 13.74 ? 66 SER A HG 1 ATOM 714 N N . PRO A 1 59 ? -10.870 17.972 16.415 1.00 11.75 ? 67 PRO A N 1 ATOM 715 C CA . PRO A 1 59 ? -12.173 17.354 16.627 1.00 12.08 ? 67 PRO A CA 1 ATOM 716 C C . PRO A 1 59 ? -12.010 15.877 16.928 1.00 11.27 ? 67 PRO A C 1 ATOM 717 O O . PRO A 1 59 ? -11.020 15.244 16.556 1.00 11.91 ? 67 PRO A O 1 ATOM 718 C CB . PRO A 1 59 ? -12.879 17.567 15.290 1.00 13.37 ? 67 PRO A CB 1 ATOM 719 C CG . PRO A 1 59 ? -11.826 17.717 14.302 1.00 14.15 ? 67 PRO A CG 1 ATOM 720 C CD . PRO A 1 59 ? -10.633 18.315 14.993 1.00 12.13 ? 67 PRO A CD 1 ATOM 721 H HA . PRO A 1 59 ? -12.661 17.794 17.340 1.00 14.50 ? 67 PRO A HA 1 ATOM 722 H HB2 . PRO A 1 59 ? -13.430 16.795 15.087 1.00 16.05 ? 67 PRO A HB2 1 ATOM 723 H HB3 . PRO A 1 59 ? -13.421 18.371 15.334 1.00 16.05 ? 67 PRO A HB3 1 ATOM 724 H HG2 . PRO A 1 59 ? -11.601 16.845 13.940 1.00 16.98 ? 67 PRO A HG2 1 ATOM 725 H HG3 . PRO A 1 59 ? -12.133 18.305 13.594 1.00 16.98 ? 67 PRO A HG3 1 ATOM 726 H HD2 . PRO A 1 59 ? -9.814 17.903 14.676 1.00 14.56 ? 67 PRO A HD2 1 ATOM 727 H HD3 . PRO A 1 59 ? -10.618 19.278 14.874 1.00 14.56 ? 67 PRO A HD3 1 ATOM 728 N N . TRP A 1 60 ? -13.019 15.316 17.587 1.00 11.95 ? 68 TRP A N 1 ATOM 729 C CA . TRP A 1 60 ? -13.007 13.883 17.835 1.00 12.02 ? 68 TRP A CA 1 ATOM 730 C C . TRP A 1 60 ? -12.763 13.106 16.545 1.00 12.10 ? 68 TRP A C 1 ATOM 731 O O . TRP A 1 60 ? -12.027 12.121 16.531 1.00 12.60 ? 68 TRP A O 1 ATOM 732 C CB . TRP A 1 60 ? -14.300 13.417 18.502 1.00 13.93 ? 68 TRP A CB 1 ATOM 733 C CG . TRP A 1 60 ? -14.249 11.944 18.781 1.00 14.98 ? 68 TRP A CG 1 ATOM 734 C CD1 . TRP A 1 60 ? -14.903 10.966 18.115 1.00 17.27 ? 68 TRP A CD1 1 ATOM 735 C CD2 . TRP A 1 60 ? -13.437 11.289 19.769 1.00 15.99 ? 68 TRP A CD2 1 ATOM 736 N NE1 . TRP A 1 60 ? -14.569 9.743 18.646 1.00 18.32 ? 68 TRP A NE1 1 ATOM 737 C CE2 . TRP A 1 60 ? -13.663 9.916 19.655 1.00 17.31 ? 68 TRP A CE2 1 ATOM 738 C CE3 . TRP A 1 60 ? -12.553 11.739 20.752 1.00 17.05 ? 68 TRP A CE3 1 ATOM 739 C CZ2 . TRP A 1 60 ? -13.048 8.983 20.502 1.00 19.05 ? 68 TRP A CZ2 1 ATOM 740 C CZ3 . TRP A 1 60 ? -11.934 10.819 21.571 1.00 18.46 ? 68 TRP A CZ3 1 ATOM 741 C CH2 . TRP A 1 60 ? -12.194 9.466 21.454 1.00 19.87 ? 68 TRP A CH2 1 ATOM 742 H H . TRP A 1 60 ? -13.706 15.732 17.893 1.00 14.34 ? 68 TRP A H 1 ATOM 743 H HA . TRP A 1 60 ? -12.277 13.682 18.440 1.00 14.43 ? 68 TRP A HA 1 ATOM 744 H HB2 . TRP A 1 60 ? -14.416 13.885 19.343 1.00 16.71 ? 68 TRP A HB2 1 ATOM 745 H HB3 . TRP A 1 60 ? -15.049 13.591 17.911 1.00 16.71 ? 68 TRP A HB3 1 ATOM 746 H HD1 . TRP A 1 60 ? -15.490 11.100 17.407 1.00 20.72 ? 68 TRP A HD1 1 ATOM 747 H HE1 . TRP A 1 60 ? -14.875 8.986 18.378 1.00 21.98 ? 68 TRP A HE1 1 ATOM 748 H HE3 . TRP A 1 60 ? -12.378 12.647 20.847 1.00 20.46 ? 68 TRP A HE3 1 ATOM 749 H HZ2 . TRP A 1 60 ? -13.214 8.072 20.419 1.00 22.86 ? 68 TRP A HZ2 1 ATOM 750 H HZ3 . TRP A 1 60 ? -11.346 11.116 22.228 1.00 22.15 ? 68 TRP A HZ3 1 ATOM 751 H HH2 . TRP A 1 60 ? -11.758 8.869 22.018 1.00 23.84 ? 68 TRP A HH2 1 ATOM 752 N N . ALA A 1 61 ? -13.371 13.545 15.444 1.00 12.24 ? 69 ALA A N 1 ATOM 753 C CA . ALA A 1 61 ? -13.210 12.809 14.196 1.00 12.91 ? 69 ALA A CA 1 ATOM 754 C C . ALA A 1 61 ? -11.748 12.659 13.808 1.00 12.49 ? 69 ALA A C 1 ATOM 755 O O . ALA A 1 61 ? -11.359 11.632 13.233 1.00 12.86 ? 69 ALA A O 1 ATOM 756 C CB . ALA A 1 61 ? -13.979 13.497 13.073 1.00 14.47 ? 69 ALA A CB 1 ATOM 757 H H . ALA A 1 61 ? -13.868 14.245 15.393 1.00 14.69 ? 69 ALA A H 1 ATOM 758 H HA . ALA A 1 61 ? -13.580 11.920 14.308 1.00 15.50 ? 69 ALA A HA 1 ATOM 759 H HB1 . ALA A 1 61 ? -13.859 12.993 12.254 1.00 17.37 ? 69 ALA A HB1 1 ATOM 760 H HB2 . ALA A 1 61 ? -14.920 13.528 13.308 1.00 17.37 ? 69 ALA A HB2 1 ATOM 761 H HB3 . ALA A 1 61 ? -13.636 14.398 12.962 1.00 17.37 ? 69 ALA A HB3 1 ATOM 762 N N . LEU A 1 62 ? -10.933 13.679 14.083 1.00 11.69 ? 70 LEU A N 1 ATOM 763 C CA . LEU A 1 62 ? -9.518 13.623 13.754 1.00 11.71 ? 70 LEU A CA 1 ATOM 764 C C . LEU A 1 62 ? -8.779 12.653 14.665 1.00 11.74 ? 70 LEU A C 1 ATOM 765 O O . LEU A 1 62 ? -7.985 11.838 14.201 1.00 11.28 ? 70 LEU A O 1 ATOM 766 C CB . LEU A 1 62 ? -8.905 15.020 13.874 1.00 11.93 ? 70 LEU A CB 1 ATOM 767 C CG . LEU A 1 62 ? -7.389 15.067 13.632 1.00 11.70 ? 70 LEU A CG 1 ATOM 768 C CD1 . LEU A 1 62 ? -7.007 14.575 12.226 1.00 13.17 ? 70 LEU A CD1 1 ATOM 769 C CD2 . LEU A 1 62 ? -6.861 16.480 13.879 1.00 12.56 ? 70 LEU A CD2 1 ATOM 770 H H . LEU A 1 62 ? -11.179 14.412 14.459 1.00 14.03 ? 70 LEU A H 1 ATOM 771 H HA . LEU A 1 62 ? -9.413 13.322 12.838 1.00 14.06 ? 70 LEU A HA 1 ATOM 772 H HB2 . LEU A 1 62 ? -9.326 15.602 13.221 1.00 14.32 ? 70 LEU A HB2 1 ATOM 773 H HB3 . LEU A 1 62 ? -9.072 15.357 14.768 1.00 14.32 ? 70 LEU A HB3 1 ATOM 774 H HG . LEU A 1 62 ? -6.958 14.479 14.273 1.00 14.04 ? 70 LEU A HG 1 ATOM 775 H HD11 . LEU A 1 62 ? -6.043 14.624 12.126 1.00 15.81 ? 70 LEU A HD11 1 ATOM 776 H HD12 . LEU A 1 62 ? -7.304 13.657 12.122 1.00 15.81 ? 70 LEU A HD12 1 ATOM 777 H HD13 . LEU A 1 62 ? -7.438 15.140 11.566 1.00 15.81 ? 70 LEU A HD13 1 ATOM 778 H HD21 . LEU A 1 62 ? -5.904 16.491 13.722 1.00 15.07 ? 70 LEU A HD21 1 ATOM 779 H HD22 . LEU A 1 62 ? -7.303 17.093 13.271 1.00 15.07 ? 70 LEU A HD22 1 ATOM 780 H HD23 . LEU A 1 62 ? -7.049 16.731 14.797 1.00 15.07 ? 70 LEU A HD23 1 ATOM 781 N N . ILE A 1 63 ? -9.052 12.708 15.958 1.00 11.82 ? 71 ILE A N 1 ATOM 782 C CA . ILE A 1 63 ? -8.408 11.797 16.891 1.00 12.54 ? 71 ILE A CA 1 ATOM 783 C C . ILE A 1 63 ? -8.777 10.359 16.570 1.00 12.05 ? 71 ILE A C 1 ATOM 784 O O . ILE A 1 63 ? -7.918 9.468 16.522 1.00 12.31 ? 71 ILE A O 1 ATOM 785 C CB . ILE A 1 63 ? -8.774 12.187 18.328 1.00 12.03 ? 71 ILE A CB 1 ATOM 786 C CG1 . ILE A 1 63 ? -7.993 13.467 18.708 1.00 12.33 ? 71 ILE A CG1 1 ATOM 787 C CG2 . ILE A 1 63 ? -8.459 11.042 19.281 1.00 14.21 ? 71 ILE A CG2 1 ATOM 788 C CD1 . ILE A 1 63 ? -8.437 14.108 19.987 1.00 13.59 ? 71 ILE A CD1 1 ATOM 789 H H . ILE A 1 63 ? -9.603 13.260 16.320 1.00 14.19 ? 71 ILE A H 1 ATOM 790 H HA . ILE A 1 63 ? -7.446 11.883 16.798 1.00 15.05 ? 71 ILE A HA 1 ATOM 791 H HB . ILE A 1 63 ? -9.725 12.376 18.369 1.00 14.43 ? 71 ILE A HB 1 ATOM 792 H HG12 . ILE A 1 63 ? -7.055 13.242 18.802 1.00 14.80 ? 71 ILE A HG12 1 ATOM 793 H HG13 . ILE A 1 63 ? -8.103 14.120 17.998 1.00 14.80 ? 71 ILE A HG13 1 ATOM 794 H HG21 . ILE A 1 63 ? -8.697 11.307 20.183 1.00 17.06 ? 71 ILE A HG21 1 ATOM 795 H HG22 . ILE A 1 63 ? -8.973 10.262 19.018 1.00 17.06 ? 71 ILE A HG22 1 ATOM 796 H HG23 . ILE A 1 63 ? -7.510 10.845 19.233 1.00 17.06 ? 71 ILE A HG23 1 ATOM 797 H HD11 . ILE A 1 63 ? -7.898 14.899 20.147 1.00 16.31 ? 71 ILE A HD11 1 ATOM 798 H HD12 . ILE A 1 63 ? -9.372 14.355 19.908 1.00 16.31 ? 71 ILE A HD12 1 ATOM 799 H HD13 . ILE A 1 63 ? -8.321 13.476 20.713 1.00 16.31 ? 71 ILE A HD13 1 ATOM 800 N N . ASN A 1 64 ? -10.064 10.116 16.313 1.00 12.13 ? 72 ASN A N 1 ATOM 801 C CA . ASN A 1 64 ? -10.506 8.790 15.920 1.00 13.17 ? 72 ASN A CA 1 ATOM 802 C C . ASN A 1 64 ? -9.809 8.335 14.647 1.00 12.94 ? 72 ASN A C 1 ATOM 803 O O . ASN A 1 64 ? -9.336 7.201 14.562 1.00 13.18 ? 72 ASN A O 1 ATOM 804 C CB . ASN A 1 64 ? -12.020 8.843 15.732 1.00 14.92 ? 72 ASN A CB 1 ATOM 805 C CG . ASN A 1 64 ? -12.591 7.518 15.408 1.00 16.90 ? 72 ASN A CG 1 ATOM 806 O OD1 . ASN A 1 64 ? -12.552 6.595 16.207 1.00 16.81 ? 72 ASN A OD1 1 ATOM 807 N ND2 . ASN A 1 64 ? -13.140 7.410 14.216 1.00 18.41 ? 72 ASN A ND2 1 ATOM 808 H H . ASN A 1 64 ? -10.693 10.701 16.360 1.00 14.56 ? 72 ASN A H 1 ATOM 809 H HA . ASN A 1 64 ? -10.303 8.157 16.627 1.00 15.80 ? 72 ASN A HA 1 ATOM 810 H HB2 . ASN A 1 64 ? -12.431 9.156 16.553 1.00 17.91 ? 72 ASN A HB2 1 ATOM 811 H HB3 . ASN A 1 64 ? -12.228 9.448 15.003 1.00 17.91 ? 72 ASN A HB3 1 ATOM 812 H HD21 . ASN A 1 64 ? -13.128 8.092 13.693 1.00 22.09 ? 72 ASN A HD21 1 ATOM 813 N N . SER A 1 65 ? -9.705 9.221 13.664 1.00 12.79 ? 73 SER A N 1 ATOM 814 C CA A SER A 1 65 ? -9.019 8.879 12.428 0.79 13.58 ? 73 SER A CA 1 ATOM 815 C CA B SER A 1 65 ? -9.022 8.862 12.427 0.21 12.93 ? 73 SER A CA 1 ATOM 816 C C . SER A 1 65 ? -7.565 8.496 12.694 1.00 12.90 ? 73 SER A C 1 ATOM 817 O O . SER A 1 65 ? -7.039 7.549 12.100 1.00 13.33 ? 73 SER A O 1 ATOM 818 C CB A SER A 1 65 ? -9.094 10.073 11.483 0.79 14.46 ? 73 SER A CB 1 ATOM 819 C CB B SER A 1 65 ? -9.144 9.978 11.391 0.21 12.73 ? 73 SER A CB 1 ATOM 820 O OG A SER A 1 65 ? -8.356 9.876 10.300 0.79 14.20 ? 73 SER A OG 1 ATOM 821 O OG B SER A 1 65 ? -8.179 10.987 11.584 0.21 12.44 ? 73 SER A OG 1 ATOM 822 H H . SER A 1 65 ? -10.018 10.022 13.684 1.00 15.35 ? 73 SER A H 1 ATOM 823 H HA . SER A 1 65 ? -9.459 8.101 12.033 1.00 15.51 ? 73 SER A HA 1 ATOM 824 H HB2 A SER A 1 65 ? -10.022 10.224 11.248 0.79 17.35 ? 73 SER A HB2 1 ATOM 825 H HB2 B SER A 1 65 ? -9.024 9.597 10.507 0.21 15.28 ? 73 SER A HB2 1 ATOM 826 H HB3 A SER A 1 65 ? -8.742 10.853 11.941 0.79 17.35 ? 73 SER A HB3 1 ATOM 827 H HB3 B SER A 1 65 ? -10.027 10.374 11.461 0.21 15.28 ? 73 SER A HB3 1 ATOM 828 H HG A SER A 1 65 ? -8.650 9.207 9.887 0.79 17.04 ? 73 SER A HG 1 ATOM 829 H HG B SER A 1 65 ? -8.271 11.331 12.345 0.21 14.93 ? 73 SER A HG 1 ATOM 830 N N . SER A 1 66 ? -6.898 9.223 13.592 1.00 12.29 ? 74 SER A N 1 ATOM 831 C CA . SER A 1 66 ? -5.487 8.940 13.863 1.00 12.00 ? 74 SER A CA 1 ATOM 832 C C . SER A 1 66 ? -5.293 7.541 14.442 1.00 12.11 ? 74 SER A C 1 ATOM 833 O O . SER A 1 66 ? -4.347 6.835 14.065 1.00 13.21 ? 74 SER A O 1 ATOM 834 C CB . SER A 1 66 ? -4.865 10.025 14.767 1.00 13.21 ? 74 SER A CB 1 ATOM 835 O OG . SER A 1 66 ? -5.186 9.898 16.136 1.00 13.11 ? 74 SER A OG 1 ATOM 836 H H . SER A 1 66 ? -7.230 9.871 14.048 1.00 14.74 ? 74 SER A H 1 ATOM 837 H HA . SER A 1 66 ? -5.009 8.966 13.019 1.00 14.40 ? 74 SER A HA 1 ATOM 838 H HB2 . SER A 1 66 ? -3.900 9.981 14.675 1.00 15.85 ? 74 SER A HB2 1 ATOM 839 H HB3 . SER A 1 66 ? -5.177 10.891 14.461 1.00 15.85 ? 74 SER A HB3 1 ATOM 840 H HG . SER A 1 66 ? -6.018 9.944 16.241 1.00 15.73 ? 74 SER A HG 1 ATOM 841 N N . LEU A 1 67 ? -6.173 7.115 15.350 1.00 12.66 ? 75 LEU A N 1 ATOM 842 C CA . LEU A 1 67 ? -6.038 5.806 15.966 1.00 13.08 ? 75 LEU A CA 1 ATOM 843 C C . LEU A 1 67 ? -6.295 4.708 14.956 1.00 13.54 ? 75 LEU A C 1 ATOM 844 O O . LEU A 1 67 ? -5.595 3.692 14.946 1.00 13.56 ? 75 LEU A O 1 ATOM 845 C CB . LEU A 1 67 ? -6.951 5.676 17.186 1.00 13.73 ? 75 LEU A CB 1 ATOM 846 C CG . LEU A 1 67 ? -6.273 5.909 18.532 1.00 14.23 ? 75 LEU A CG 1 ATOM 847 C CD1 . LEU A 1 67 ? -5.282 4.797 18.831 1.00 15.98 ? 75 LEU A CD1 1 ATOM 848 C CD2 . LEU A 1 67 ? -5.599 7.285 18.592 1.00 15.44 ? 75 LEU A CD2 1 ATOM 849 H H . LEU A 1 67 ? -6.852 7.567 15.622 1.00 15.19 ? 75 LEU A H 1 ATOM 850 H HA . LEU A 1 67 ? -5.124 5.706 16.276 1.00 15.69 ? 75 LEU A HA 1 ATOM 851 H HB2 . LEU A 1 67 ? -7.668 6.324 17.104 1.00 16.47 ? 75 LEU A HB2 1 ATOM 852 H HB3 . LEU A 1 67 ? -7.323 4.780 17.198 1.00 16.47 ? 75 LEU A HB3 1 ATOM 853 H HG . LEU A 1 67 ? -6.951 5.888 19.225 1.00 17.08 ? 75 LEU A HG 1 ATOM 854 H HD11 . LEU A 1 67 ? -4.866 4.968 19.690 1.00 19.18 ? 75 LEU A HD11 1 ATOM 855 H HD12 . LEU A 1 67 ? -5.756 3.951 18.856 1.00 19.18 ? 75 LEU A HD12 1 ATOM 856 H HD13 . LEU A 1 67 ? -4.608 4.779 18.134 1.00 19.18 ? 75 LEU A HD13 1 ATOM 857 H HD21 . LEU A 1 67 ? -5.181 7.395 19.460 1.00 18.53 ? 75 LEU A HD21 1 ATOM 858 H HD22 . LEU A 1 67 ? -4.928 7.339 17.893 1.00 18.53 ? 75 LEU A HD22 1 ATOM 859 H HD23 . LEU A 1 67 ? -6.271 7.972 18.459 1.00 18.53 ? 75 LEU A HD23 1 ATOM 860 N N . TYR A 1 68 ? -7.311 4.872 14.106 1.00 14.10 ? 76 TYR A N 1 ATOM 861 C CA . TYR A 1 68 ? -7.563 3.860 13.090 1.00 14.48 ? 76 TYR A CA 1 ATOM 862 C C . TYR A 1 68 ? -6.492 3.856 12.005 1.00 14.78 ? 76 TYR A C 1 ATOM 863 O O . TYR A 1 68 ? -6.190 2.803 11.446 1.00 16.14 ? 76 TYR A O 1 ATOM 864 C CB . TYR A 1 68 ? -8.996 3.986 12.537 1.00 15.66 ? 76 TYR A CB 1 ATOM 865 C CG . TYR A 1 68 ? -9.993 3.368 13.479 1.00 16.70 ? 76 TYR A CG 1 ATOM 866 C CD1 . TYR A 1 68 ? -10.212 2.000 13.463 1.00 19.73 ? 76 TYR A CD1 1 ATOM 867 C CD2 . TYR A 1 68 ? -10.649 4.128 14.434 1.00 17.52 ? 76 TYR A CD2 1 ATOM 868 C CE1 . TYR A 1 68 ? -11.082 1.403 14.343 1.00 21.41 ? 76 TYR A CE1 1 ATOM 869 C CE2 . TYR A 1 68 ? -11.539 3.537 15.327 1.00 18.33 ? 76 TYR A CE2 1 ATOM 870 C CZ . TYR A 1 68 ? -11.746 2.172 15.281 1.00 21.35 ? 76 TYR A CZ 1 ATOM 871 O OH . TYR A 1 68 ? -12.610 1.554 16.160 1.00 24.65 ? 76 TYR A OH 1 ATOM 872 H H . TYR A 1 68 ? -7.852 5.540 14.099 1.00 16.92 ? 76 TYR A H 1 ATOM 873 H HA . TYR A 1 68 ? -7.513 2.994 13.524 1.00 17.37 ? 76 TYR A HA 1 ATOM 874 H HB2 . TYR A 1 68 ? -9.218 4.924 12.430 1.00 18.80 ? 76 TYR A HB2 1 ATOM 875 H HB3 . TYR A 1 68 ? -9.054 3.526 11.685 1.00 18.80 ? 76 TYR A HB3 1 ATOM 876 H HD1 . TYR A 1 68 ? -9.764 1.475 12.839 1.00 23.68 ? 76 TYR A HD1 1 ATOM 877 H HD2 . TYR A 1 68 ? -10.505 5.046 14.468 1.00 21.02 ? 76 TYR A HD2 1 ATOM 878 H HE1 . TYR A 1 68 ? -11.222 0.484 14.310 1.00 25.69 ? 76 TYR A HE1 1 ATOM 879 H HE2 . TYR A 1 68 ? -11.982 4.056 15.959 1.00 21.99 ? 76 TYR A HE2 1 ATOM 880 H HH . TYR A 1 68 ? -12.949 2.123 16.677 1.00 29.58 ? 76 TYR A HH 1 ATOM 881 N N . ALA A 1 69 ? -5.867 4.996 11.741 1.00 14.45 ? 77 ALA A N 1 ATOM 882 C CA . ALA A 1 69 ? -4.719 5.013 10.847 1.00 14.16 ? 77 ALA A CA 1 ATOM 883 C C . ALA A 1 69 ? -3.566 4.211 11.436 1.00 14.08 ? 77 ALA A C 1 ATOM 884 O O . ALA A 1 69 ? -2.907 3.436 10.733 1.00 15.40 ? 77 ALA A O 1 ATOM 885 C CB . ALA A 1 69 ? -4.286 6.443 10.558 1.00 15.48 ? 77 ALA A CB 1 ATOM 886 H H . ALA A 1 69 ? -6.085 5.764 12.061 1.00 17.34 ? 77 ALA A H 1 ATOM 887 H HA . ALA A 1 69 ? -4.970 4.601 10.006 1.00 16.99 ? 77 ALA A HA 1 ATOM 888 H HB1 . ALA A 1 69 ? -3.521 6.426 9.961 1.00 18.57 ? 77 ALA A HB1 1 ATOM 889 H HB2 . ALA A 1 69 ? -5.022 6.916 10.139 1.00 18.57 ? 77 ALA A HB2 1 ATOM 890 H HB3 . ALA A 1 69 ? -4.046 6.874 11.392 1.00 18.57 ? 77 ALA A HB3 1 ATOM 891 N N . MET A 1 70 ? -3.313 4.376 12.728 1.00 14.07 ? 78 MET A N 1 ATOM 892 C CA . MET A 1 70 ? -2.283 3.566 13.356 1.00 13.80 ? 78 MET A CA 1 ATOM 893 C C . MET A 1 70 ? -2.595 2.090 13.239 1.00 14.60 ? 78 MET A C 1 ATOM 894 O O . MET A 1 70 ? -1.712 1.283 12.922 1.00 15.32 ? 78 MET A O 1 ATOM 895 C CB . MET A 1 70 ? -2.189 3.895 14.837 1.00 14.99 ? 78 MET A CB 1 ATOM 896 C CG . MET A 1 70 ? -1.671 5.277 15.145 1.00 14.42 ? 78 MET A CG 1 ATOM 897 S SD . MET A 1 70 ? -2.118 5.864 16.817 1.00 15.09 ? 78 MET A SD 1 ATOM 898 C CE . MET A 1 70 ? -1.229 4.692 17.860 1.00 15.83 ? 78 MET A CE 1 ATOM 899 H H . MET A 1 70 ? -3.710 4.934 13.249 1.00 16.88 ? 78 MET A H 1 ATOM 900 H HA . MET A 1 70 ? -1.426 3.751 12.942 1.00 16.56 ? 78 MET A HA 1 ATOM 901 H HB2 . MET A 1 70 ? -3.074 3.819 15.228 1.00 17.99 ? 78 MET A HB2 1 ATOM 902 H HB3 . MET A 1 70 ? -1.591 3.257 15.258 1.00 17.99 ? 78 MET A HB3 1 ATOM 903 H HG2 . MET A 1 70 ? -0.703 5.272 15.079 1.00 17.31 ? 78 MET A HG2 1 ATOM 904 H HG3 . MET A 1 70 ? -2.041 5.901 14.501 1.00 17.31 ? 78 MET A HG3 1 ATOM 905 H HE1 . MET A 1 70 ? -1.395 4.910 18.791 1.00 19.00 ? 78 MET A HE1 1 ATOM 906 H HE2 . MET A 1 70 ? -1.546 3.796 17.668 1.00 19.00 ? 78 MET A HE2 1 ATOM 907 H HE3 . MET A 1 70 ? -0.280 4.756 17.669 1.00 19.00 ? 78 MET A HE3 1 ATOM 908 N N . LYS A 1 71 ? -3.861 1.711 13.444 1.00 14.71 ? 79 LYS A N 1 ATOM 909 C CA . LYS A 1 71 ? -4.217 0.305 13.352 1.00 16.85 ? 79 LYS A CA 1 ATOM 910 C C . LYS A 1 71 ? -3.997 -0.221 11.942 1.00 15.94 ? 79 LYS A C 1 ATOM 911 O O . LYS A 1 71 ? -3.550 -1.354 11.755 1.00 17.19 ? 79 LYS A O 1 ATOM 912 C CB . LYS A 1 71 ? -5.669 0.127 13.750 1.00 18.54 ? 79 LYS A CB 1 ATOM 913 C CG . LYS A 1 71 ? -6.070 -1.322 13.742 1.00 21.61 ? 79 LYS A CG 1 ATOM 914 C CD . LYS A 1 71 ? -7.509 -1.522 14.143 1.00 25.87 ? 79 LYS A CD 1 ATOM 915 C CE . LYS A 1 71 ? -7.925 -2.977 14.014 1.00 31.16 ? 79 LYS A CE 1 ATOM 916 N NZ . LYS A 1 71 ? -9.405 -3.099 14.065 1.00 34.58 ? 79 LYS A NZ 1 ATOM 917 H H . LYS A 1 71 ? -4.513 2.239 13.633 1.00 17.65 ? 79 LYS A H 1 ATOM 918 H HA . LYS A 1 71 ? -3.666 -0.210 13.962 1.00 20.22 ? 79 LYS A HA 1 ATOM 919 H HB2 . LYS A 1 71 ? -5.800 0.474 14.646 1.00 22.25 ? 79 LYS A HB2 1 ATOM 920 H HB3 . LYS A 1 71 ? -6.234 0.602 13.120 1.00 22.25 ? 79 LYS A HB3 1 ATOM 921 H HG2 . LYS A 1 71 ? -5.954 -1.678 12.847 1.00 25.93 ? 79 LYS A HG2 1 ATOM 922 H HG3 . LYS A 1 71 ? -5.511 -1.808 14.369 1.00 25.93 ? 79 LYS A HG3 1 ATOM 923 H HD2 . LYS A 1 71 ? -7.623 -1.255 15.069 1.00 31.05 ? 79 LYS A HD2 1 ATOM 924 H HD3 . LYS A 1 71 ? -8.079 -0.991 13.567 1.00 31.05 ? 79 LYS A HD3 1 ATOM 925 H HE2 . LYS A 1 71 ? -7.616 -3.328 13.164 1.00 37.39 ? 79 LYS A HE2 1 ATOM 926 H HE3 . LYS A 1 71 ? -7.549 -3.488 14.748 1.00 37.39 ? 79 LYS A HE3 1 ATOM 927 H HZ1 . LYS A 1 71 ? -9.643 -3.953 13.988 1.00 41.50 ? 79 LYS A HZ1 1 ATOM 928 H HZ2 . LYS A 1 71 ? -9.710 -2.781 14.838 1.00 41.50 ? 79 LYS A HZ2 1 ATOM 929 H HZ3 . LYS A 1 71 ? -9.771 -2.636 13.398 1.00 41.50 ? 79 LYS A HZ3 1 ATOM 930 N N . GLU A 1 72 ? -4.344 0.569 10.929 1.00 17.37 ? 80 GLU A N 1 ATOM 931 C CA . GLU A 1 72 ? -4.126 0.126 9.556 1.00 17.85 ? 80 GLU A CA 1 ATOM 932 C C . GLU A 1 72 ? -2.637 -0.060 9.254 1.00 16.81 ? 80 GLU A C 1 ATOM 933 O O . GLU A 1 72 ? -2.258 -1.021 8.572 1.00 19.04 ? 80 GLU A O 1 ATOM 934 C CB . GLU A 1 72 ? -4.757 1.129 8.596 1.00 21.54 ? 80 GLU A CB 1 ATOM 935 C CG . GLU A 1 72 ? -4.558 0.789 7.123 1.00 28.92 ? 80 GLU A CG 1 ATOM 936 C CD . GLU A 1 72 ? -5.543 1.507 6.226 1.00 37.50 ? 80 GLU A CD 1 ATOM 937 O OE1 . GLU A 1 72 ? -6.247 2.405 6.734 1.00 41.00 ? 80 GLU A OE1 1 ATOM 938 O OE2 . GLU A 1 72 ? -5.617 1.177 5.018 1.00 41.69 ? 80 GLU A OE2 1 ATOM 939 H H . GLU A 1 72 ? -4.700 1.348 11.007 1.00 20.84 ? 80 GLU A H 1 ATOM 940 H HA . GLU A 1 72 ? -4.566 -0.729 9.428 1.00 21.42 ? 80 GLU A HA 1 ATOM 941 H HB2 . GLU A 1 72 ? -5.711 1.165 8.765 1.00 25.85 ? 80 GLU A HB2 1 ATOM 942 H HB3 . GLU A 1 72 ? -4.363 2.001 8.753 1.00 25.85 ? 80 GLU A HB3 1 ATOM 943 H HG2 . GLU A 1 72 ? -3.663 1.049 6.855 1.00 34.71 ? 80 GLU A HG2 1 ATOM 944 H HG3 . GLU A 1 72 ? -4.679 -0.166 6.999 1.00 34.71 ? 80 GLU A HG3 1 ATOM 945 N N . ILE A 1 73 ? -1.789 0.842 9.746 1.00 15.18 ? 81 ILE A N 1 ATOM 946 C CA . ILE A 1 73 ? -0.366 0.807 9.439 1.00 16.25 ? 81 ILE A CA 1 ATOM 947 C C . ILE A 1 73 ? 0.335 -0.302 10.202 1.00 16.11 ? 81 ILE A C 1 ATOM 948 O O . ILE A 1 73 ? 1.166 -1.019 9.633 1.00 18.17 ? 81 ILE A O 1 ATOM 949 C CB . ILE A 1 73 ? 0.285 2.179 9.702 1.00 17.02 ? 81 ILE A CB 1 ATOM 950 C CG1 . ILE A 1 73 ? -0.238 3.196 8.684 1.00 17.11 ? 81 ILE A CG1 1 ATOM 951 C CG2 . ILE A 1 73 ? 1.820 2.088 9.664 1.00 16.81 ? 81 ILE A CG2 1 ATOM 952 C CD1 . ILE A 1 73 ? -0.141 4.618 9.154 1.00 16.84 ? 81 ILE A CD1 1 ATOM 953 H H . ILE A 1 73 ? -2.018 1.489 10.264 1.00 18.22 ? 81 ILE A H 1 ATOM 954 H HA . ILE A 1 73 ? -0.263 0.615 8.494 1.00 19.50 ? 81 ILE A HA 1 ATOM 955 H HB . ILE A 1 73 ? 0.021 2.474 10.587 1.00 20.43 ? 81 ILE A HB 1 ATOM 956 H HG12 . ILE A 1 73 ? 0.279 3.117 7.867 1.00 20.54 ? 81 ILE A HG12 1 ATOM 957 H HG13 . ILE A 1 73 ? -1.172 3.006 8.502 1.00 20.54 ? 81 ILE A HG13 1 ATOM 958 H HG21 . ILE A 1 73 ? 2.192 2.967 9.833 1.00 20.17 ? 81 ILE A HG21 1 ATOM 959 H HG22 . ILE A 1 73 ? 2.116 1.466 10.348 1.00 20.17 ? 81 ILE A HG22 1 ATOM 960 H HG23 . ILE A 1 73 ? 2.096 1.773 8.789 1.00 20.17 ? 81 ILE A HG23 1 ATOM 961 H HD11 . ILE A 1 73 ? -0.488 5.203 8.462 1.00 20.21 ? 81 ILE A HD11 1 ATOM 962 H HD12 . ILE A 1 73 ? -0.663 4.718 9.965 1.00 20.21 ? 81 ILE A HD12 1 ATOM 963 H HD13 . ILE A 1 73 ? 0.789 4.829 9.330 1.00 20.21 ? 81 ILE A HD13 1 ATOM 964 N N . GLU A 1 74 ? 0.063 -0.417 11.503 1.00 15.34 ? 82 GLU A N 1 ATOM 965 C CA . GLU A 1 74 ? 0.710 -1.428 12.343 1.00 16.27 ? 82 GLU A CA 1 ATOM 966 C C . GLU A 1 74 ? -0.241 -1.781 13.471 1.00 15.66 ? 82 GLU A C 1 ATOM 967 O O . GLU A 1 74 ? -0.258 -1.121 14.520 1.00 15.81 ? 82 GLU A O 1 ATOM 968 C CB . GLU A 1 74 ? 2.052 -0.966 12.916 1.00 16.50 ? 82 GLU A CB 1 ATOM 969 C CG . GLU A 1 74 ? 2.664 -2.031 13.843 1.00 19.23 ? 82 GLU A CG 1 ATOM 970 C CD . GLU A 1 74 ? 2.707 -3.399 13.169 1.00 21.98 ? 82 GLU A CD 1 ATOM 971 O OE1 . GLU A 1 74 ? 3.535 -3.566 12.248 1.00 26.08 ? 82 GLU A OE1 1 ATOM 972 O OE2 . GLU A 1 74 ? 1.895 -4.290 13.540 1.00 23.10 ? 82 GLU A OE2 1 ATOM 973 H H . GLU A 1 74 ? -0.496 0.082 11.926 1.00 18.40 ? 82 GLU A H 1 ATOM 974 H HA . GLU A 1 74 ? 0.866 -2.228 11.816 1.00 19.52 ? 82 GLU A HA 1 ATOM 975 H HB2 . GLU A 1 74 ? 2.672 -0.804 12.187 1.00 19.80 ? 82 GLU A HB2 1 ATOM 976 H HB3 . GLU A 1 74 ? 1.918 -0.155 13.430 1.00 19.80 ? 82 GLU A HB3 1 ATOM 977 H HG2 . GLU A 1 74 ? 3.572 -1.775 14.069 1.00 23.08 ? 82 GLU A HG2 1 ATOM 978 H HG3 . GLU A 1 74 ? 2.126 -2.104 14.646 1.00 23.08 ? 82 GLU A HG3 1 ATOM 979 N N . PRO A 1 75 ? -1.056 -2.828 13.292 1.00 16.94 ? 83 PRO A N 1 ATOM 980 C CA . PRO A 1 75 ? -2.050 -3.186 14.312 1.00 16.89 ? 83 PRO A CA 1 ATOM 981 C C . PRO A 1 75 ? -1.492 -3.914 15.514 1.00 16.51 ? 83 PRO A C 1 ATOM 982 O O . PRO A 1 75 ? -2.213 -4.041 16.514 1.00 17.91 ? 83 PRO A O 1 ATOM 983 C CB . PRO A 1 75 ? -3.023 -4.089 13.537 1.00 18.62 ? 83 PRO A CB 1 ATOM 984 C CG . PRO A 1 75 ? -2.189 -4.704 12.485 1.00 19.28 ? 83 PRO A CG 1 ATOM 985 C CD . PRO A 1 75 ? -1.236 -3.605 12.062 1.00 18.45 ? 83 PRO A CD 1 ATOM 986 H HA . PRO A 1 75 ? -2.522 -2.393 14.611 1.00 20.26 ? 83 PRO A HA 1 ATOM 987 H HB2 . PRO A 1 75 ? -3.388 -4.766 14.129 1.00 22.34 ? 83 PRO A HB2 1 ATOM 988 H HB3 . PRO A 1 75 ? -3.731 -3.553 13.147 1.00 22.34 ? 83 PRO A HB3 1 ATOM 989 H HG2 . PRO A 1 75 ? -1.703 -5.460 12.851 1.00 23.14 ? 83 PRO A HG2 1 ATOM 990 H HG3 . PRO A 1 75 ? -2.748 -4.980 11.742 1.00 23.14 ? 83 PRO A HG3 1 ATOM 991 H HD2 . PRO A 1 75 ? -0.391 -3.983 11.773 1.00 22.14 ? 83 PRO A HD2 1 ATOM 992 H HD3 . PRO A 1 75 ? -1.638 -3.057 11.371 1.00 22.14 ? 83 PRO A HD3 1 ATOM 993 N N . LYS A 1 76 ? -0.267 -4.415 15.437 1.00 17.26 ? 84 LYS A N 1 ATOM 994 C CA . LYS A 1 76 ? 0.317 -5.256 16.478 1.00 19.35 ? 84 LYS A CA 1 ATOM 995 C C . LYS A 1 76 ? 1.687 -4.714 16.848 1.00 18.07 ? 84 LYS A C 1 ATOM 996 O O . LYS A 1 76 ? 2.695 -5.423 16.765 1.00 18.94 ? 84 LYS A O 1 ATOM 997 C CB . LYS A 1 76 ? 0.437 -6.699 15.991 1.00 21.94 ? 84 LYS A CB 1 ATOM 998 C CG . LYS A 1 76 ? -0.877 -7.396 15.786 1.00 26.58 ? 84 LYS A CG 1 ATOM 999 C CD . LYS A 1 76 ? -0.679 -8.914 15.645 1.00 32.81 ? 84 LYS A CD 1 ATOM 1000 C CE . LYS A 1 76 ? -0.710 -9.600 17.011 1.00 38.29 ? 84 LYS A CE 1 ATOM 1001 N NZ . LYS A 1 76 ? 0.445 -10.528 17.263 1.00 41.40 ? 84 LYS A NZ 1 ATOM 1002 H H . LYS A 1 76 ? 0.262 -4.279 14.772 1.00 20.71 ? 84 LYS A H 1 ATOM 1003 H HA . LYS A 1 76 ? -0.247 -5.239 17.267 1.00 23.23 ? 84 LYS A HA 1 ATOM 1004 H HB2 . LYS A 1 76 ? 0.908 -6.702 15.143 1.00 26.33 ? 84 LYS A HB2 1 ATOM 1005 H HB3 . LYS A 1 76 ? 0.941 -7.207 16.646 1.00 26.33 ? 84 LYS A HB3 1 ATOM 1006 H HG2 . LYS A 1 76 ? -1.451 -7.232 16.551 1.00 31.89 ? 84 LYS A HG2 1 ATOM 1007 H HG3 . LYS A 1 76 ? -1.293 -7.065 14.975 1.00 31.89 ? 84 LYS A HG3 1 ATOM 1008 H HD2 . LYS A 1 76 ? -1.393 -9.283 15.102 1.00 39.37 ? 84 LYS A HD2 1 ATOM 1009 H HD3 . LYS A 1 76 ? 0.183 -9.089 15.235 1.00 39.37 ? 84 LYS A HD3 1 ATOM 1010 H HE2 . LYS A 1 76 ? -0.696 -8.919 17.702 1.00 45.95 ? 84 LYS A HE2 1 ATOM 1011 H HE3 . LYS A 1 76 ? -1.526 -10.120 17.080 1.00 45.95 ? 84 LYS A HE3 1 ATOM 1012 H HZ1 . LYS A 1 76 ? 0.370 -10.895 18.070 1.00 49.69 ? 84 LYS A HZ1 1 ATOM 1013 H HZ2 . LYS A 1 76 ? 0.454 -11.175 16.651 1.00 49.69 ? 84 LYS A HZ2 1 ATOM 1014 H HZ3 . LYS A 1 76 ? 1.211 -10.078 17.219 1.00 49.69 ? 84 LYS A HZ3 1 ATOM 1015 N N . PRO A 1 77 ? 1.767 -3.456 17.276 1.00 15.91 ? 85 PRO A N 1 ATOM 1016 C CA . PRO A 1 77 ? 3.055 -2.928 17.735 1.00 15.50 ? 85 PRO A CA 1 ATOM 1017 C C . PRO A 1 77 ? 3.480 -3.654 19.003 1.00 15.95 ? 85 PRO A C 1 ATOM 1018 O O . PRO A 1 77 ? 2.654 -4.216 19.730 1.00 16.85 ? 85 PRO A O 1 ATOM 1019 C CB . PRO A 1 77 ? 2.727 -1.469 18.041 1.00 14.42 ? 85 PRO A CB 1 ATOM 1020 C CG . PRO A 1 77 ? 1.294 -1.534 18.490 1.00 15.50 ? 85 PRO A CG 1 ATOM 1021 C CD . PRO A 1 77 ? 0.664 -2.524 17.553 1.00 16.24 ? 85 PRO A CD 1 ATOM 1022 H HA . PRO A 1 77 ? 3.738 -2.992 17.049 1.00 18.60 ? 85 PRO A HA 1 ATOM 1023 H HB2 . PRO A 1 77 ? 3.300 -1.140 18.751 1.00 17.31 ? 85 PRO A HB2 1 ATOM 1024 H HB3 . PRO A 1 77 ? 2.817 -0.931 17.239 1.00 17.31 ? 85 PRO A HB3 1 ATOM 1025 H HG2 . PRO A 1 77 ? 1.250 -1.848 19.407 1.00 18.60 ? 85 PRO A HG2 1 ATOM 1026 H HG3 . PRO A 1 77 ? 0.881 -0.661 18.401 1.00 18.60 ? 85 PRO A HG3 1 ATOM 1027 H HD2 . PRO A 1 77 ? -0.070 -2.986 17.988 1.00 19.48 ? 85 PRO A HD2 1 ATOM 1028 H HD3 . PRO A 1 77 ? 0.377 -2.085 16.737 1.00 19.48 ? 85 PRO A HD3 1 ATOM 1029 N N . ASP A 1 78 ? 4.782 -3.614 19.295 1.00 15.23 ? 86 ASP A N 1 ATOM 1030 C CA A ASP A 1 78 ? 5.239 -4.201 20.545 0.65 16.71 ? 86 ASP A CA 1 ATOM 1031 C CA B ASP A 1 78 ? 5.262 -4.193 20.545 0.35 16.09 ? 86 ASP A CA 1 ATOM 1032 C C . ASP A 1 78 ? 4.654 -3.458 21.733 1.00 16.58 ? 86 ASP A C 1 ATOM 1033 O O . ASP A 1 78 ? 4.379 -4.063 22.772 1.00 17.36 ? 86 ASP A O 1 ATOM 1034 C CB A ASP A 1 78 ? 6.759 -4.230 20.596 0.65 17.84 ? 86 ASP A CB 1 ATOM 1035 C CB B ASP A 1 78 ? 6.798 -4.126 20.611 0.35 16.32 ? 86 ASP A CB 1 ATOM 1036 C CG A ASP A 1 78 ? 7.348 -5.274 19.676 0.65 18.24 ? 86 ASP A CG 1 ATOM 1037 C CG B ASP A 1 78 ? 7.500 -5.154 19.707 0.35 15.96 ? 86 ASP A CG 1 ATOM 1038 O OD1 A ASP A 1 78 ? 6.593 -6.027 18.998 0.65 19.11 ? 86 ASP A OD1 1 ATOM 1039 O OD1 B ASP A 1 78 ? 7.509 -4.969 18.466 0.35 15.10 ? 86 ASP A OD1 1 ATOM 1040 O OD2 A ASP A 1 78 ? 8.583 -5.340 19.640 0.65 16.98 ? 86 ASP A OD2 1 ATOM 1041 O OD2 B ASP A 1 78 ? 8.089 -6.129 20.238 0.35 16.54 ? 86 ASP A OD2 1 ATOM 1042 H H . ASP A 1 78 ? 5.399 -3.268 18.805 1.00 18.27 ? 86 ASP A H 1 ATOM 1043 H HA . ASP A 1 78 ? 4.960 -5.122 20.591 1.00 19.31 ? 86 ASP A HA 1 ATOM 1044 H HB2 A ASP A 1 78 ? 7.101 -3.364 20.327 0.65 21.41 ? 86 ASP A HB2 1 ATOM 1045 H HB2 B ASP A 1 78 ? 7.085 -3.242 20.334 0.35 19.59 ? 86 ASP A HB2 1 ATOM 1046 H HB3 A ASP A 1 78 ? 7.041 -4.433 21.502 0.65 21.41 ? 86 ASP A HB3 1 ATOM 1047 H HB3 B ASP A 1 78 ? 7.079 -4.293 21.524 0.35 19.59 ? 86 ASP A HB3 1 ATOM 1048 N N . PHE A 1 79 ? 4.459 -2.150 21.597 1.00 15.24 ? 87 PHE A N 1 ATOM 1049 C CA . PHE A 1 79 ? 3.861 -1.299 22.619 1.00 14.15 ? 87 PHE A CA 1 ATOM 1050 C C . PHE A 1 79 ? 3.583 0.056 21.983 1.00 13.53 ? 87 PHE A C 1 ATOM 1051 O O . PHE A 1 79 ? 3.964 0.317 20.838 1.00 13.67 ? 87 PHE A O 1 ATOM 1052 C CB . PHE A 1 79 ? 4.749 -1.144 23.868 1.00 14.79 ? 87 PHE A CB 1 ATOM 1053 C CG . PHE A 1 79 ? 6.146 -0.701 23.584 1.00 15.34 ? 87 PHE A CG 1 ATOM 1054 C CD1 . PHE A 1 79 ? 7.130 -1.629 23.314 1.00 16.94 ? 87 PHE A CD1 1 ATOM 1055 C CD2 . PHE A 1 79 ? 6.497 0.638 23.603 1.00 15.23 ? 87 PHE A CD2 1 ATOM 1056 C CE1 . PHE A 1 79 ? 8.423 -1.237 23.046 1.00 18.02 ? 87 PHE A CE1 1 ATOM 1057 C CE2 . PHE A 1 79 ? 7.799 1.036 23.333 1.00 16.48 ? 87 PHE A CE2 1 ATOM 1058 C CZ . PHE A 1 79 ? 8.759 0.096 23.049 1.00 16.89 ? 87 PHE A CZ 1 ATOM 1059 H H . PHE A 1 79 ? 4.676 -1.715 20.888 1.00 18.29 ? 87 PHE A H 1 ATOM 1060 H HA . PHE A 1 79 ? 3.014 -1.683 22.896 1.00 16.98 ? 87 PHE A HA 1 ATOM 1061 H HB2 . PHE A 1 79 ? 4.345 -0.485 24.455 1.00 17.75 ? 87 PHE A HB2 1 ATOM 1062 H HB3 . PHE A 1 79 ? 4.798 -1.999 24.322 1.00 17.75 ? 87 PHE A HB3 1 ATOM 1063 H HD1 . PHE A 1 79 ? 6.913 -2.533 23.298 1.00 20.33 ? 87 PHE A HD1 1 ATOM 1064 H HD2 . PHE A 1 79 ? 5.849 1.281 23.783 1.00 18.27 ? 87 PHE A HD2 1 ATOM 1065 H HE1 . PHE A 1 79 ? 9.072 -1.877 22.859 1.00 21.62 ? 87 PHE A HE1 1 ATOM 1066 H HE2 . PHE A 1 79 ? 8.021 1.939 23.341 1.00 19.77 ? 87 PHE A HE2 1 ATOM 1067 H HZ . PHE A 1 79 ? 9.634 0.359 22.877 1.00 20.27 ? 87 PHE A HZ 1 ATOM 1068 N N . ILE A 1 80 ? 2.920 0.915 22.750 1.00 12.79 ? 88 ILE A N 1 ATOM 1069 C CA . ILE A 1 80 ? 2.630 2.291 22.355 1.00 12.91 ? 88 ILE A CA 1 ATOM 1070 C C . ILE A 1 80 ? 3.149 3.206 23.452 1.00 12.58 ? 88 ILE A C 1 ATOM 1071 O O . ILE A 1 80 ? 2.894 2.951 24.632 1.00 13.04 ? 88 ILE A O 1 ATOM 1072 C CB . ILE A 1 80 ? 1.112 2.510 22.173 1.00 12.77 ? 88 ILE A CB 1 ATOM 1073 C CG1 . ILE A 1 80 ? 0.608 1.658 21.022 1.00 13.95 ? 88 ILE A CG1 1 ATOM 1074 C CG2 . ILE A 1 80 ? 0.780 3.982 21.974 1.00 13.46 ? 88 ILE A CG2 1 ATOM 1075 C CD1 . ILE A 1 80 ? -0.897 1.567 20.951 1.00 15.37 ? 88 ILE A CD1 1 ATOM 1076 H H . ILE A 1 80 ? 2.617 0.717 23.530 1.00 15.34 ? 88 ILE A H 1 ATOM 1077 H HA . ILE A 1 80 ? 3.083 2.503 21.524 1.00 15.49 ? 88 ILE A HA 1 ATOM 1078 H HB . ILE A 1 80 ? 0.669 2.211 22.983 1.00 15.33 ? 88 ILE A HB 1 ATOM 1079 H HG12 . ILE A 1 80 ? 0.922 2.040 20.188 1.00 16.74 ? 88 ILE A HG12 1 ATOM 1080 H HG13 . ILE A 1 80 ? 0.955 0.758 21.123 1.00 16.74 ? 88 ILE A HG13 1 ATOM 1081 H HG21 . ILE A 1 80 ? -0.180 4.077 21.864 1.00 16.15 ? 88 ILE A HG21 1 ATOM 1082 H HG22 . ILE A 1 80 ? 1.074 4.481 22.752 1.00 16.15 ? 88 ILE A HG22 1 ATOM 1083 H HG23 . ILE A 1 80 ? 1.237 4.304 21.181 1.00 16.15 ? 88 ILE A HG23 1 ATOM 1084 H HD11 . ILE A 1 80 ? -1.143 1.010 20.196 1.00 18.44 ? 88 ILE A HD11 1 ATOM 1085 H HD12 . ILE A 1 80 ? -1.228 1.175 21.774 1.00 18.44 ? 88 ILE A HD12 1 ATOM 1086 H HD13 . ILE A 1 80 ? -1.262 2.458 20.838 1.00 18.44 ? 88 ILE A HD13 1 ATOM 1087 N N . LEU A 1 81 ? 3.798 4.298 23.056 1.00 10.94 ? 89 LEU A N 1 ATOM 1088 C CA . LEU A 1 81 ? 4.144 5.408 23.933 1.00 10.86 ? 89 LEU A CA 1 ATOM 1089 C C . LEU A 1 81 ? 3.162 6.537 23.685 1.00 10.75 ? 89 LEU A C 1 ATOM 1090 O O . LEU A 1 81 ? 2.958 6.936 22.541 1.00 11.81 ? 89 LEU A O 1 ATOM 1091 C CB . LEU A 1 81 ? 5.550 5.921 23.636 1.00 12.29 ? 89 LEU A CB 1 ATOM 1092 C CG . LEU A 1 81 ? 6.672 4.891 23.665 1.00 12.05 ? 89 LEU A CG 1 ATOM 1093 C CD1 . LEU A 1 81 ? 8.016 5.531 23.332 1.00 13.56 ? 89 LEU A CD1 1 ATOM 1094 C CD2 . LEU A 1 81 ? 6.737 4.193 25.013 1.00 12.64 ? 89 LEU A CD2 1 ATOM 1095 H H . LEU A 1 81 ? 4.059 4.421 22.246 1.00 13.12 ? 89 LEU A H 1 ATOM 1096 H HA . LEU A 1 81 ? 4.091 5.134 24.862 1.00 13.03 ? 89 LEU A HA 1 ATOM 1097 H HB2 . LEU A 1 81 ? 5.547 6.317 22.751 1.00 14.75 ? 89 LEU A HB2 1 ATOM 1098 H HB3 . LEU A 1 81 ? 5.769 6.602 24.291 1.00 14.75 ? 89 LEU A HB3 1 ATOM 1099 H HG . LEU A 1 81 ? 6.492 4.216 22.992 1.00 14.46 ? 89 LEU A HG 1 ATOM 1100 H HD11 . LEU A 1 81 ? 8.706 4.849 23.359 1.00 16.28 ? 89 LEU A HD11 1 ATOM 1101 H HD12 . LEU A 1 81 ? 7.970 5.919 22.444 1.00 16.28 ? 89 LEU A HD12 1 ATOM 1102 H HD13 . LEU A 1 81 ? 8.208 6.221 23.986 1.00 16.28 ? 89 LEU A HD13 1 ATOM 1103 H HD21 . LEU A 1 81 ? 7.459 3.545 24.999 1.00 15.16 ? 89 LEU A HD21 1 ATOM 1104 H HD22 . LEU A 1 81 ? 6.899 4.855 25.704 1.00 15.16 ? 89 LEU A HD22 1 ATOM 1105 H HD23 . LEU A 1 81 ? 5.893 3.744 25.177 1.00 15.16 ? 89 LEU A HD23 1 ATOM 1106 N N . TRP A 1 82 ? 2.585 7.068 24.748 1.00 11.12 ? 90 TRP A N 1 ATOM 1107 C CA . TRP A 1 82 ? 1.562 8.105 24.650 1.00 11.04 ? 90 TRP A CA 1 ATOM 1108 C C . TRP A 1 82 ? 1.935 9.207 25.635 1.00 11.04 ? 90 TRP A C 1 ATOM 1109 O O . TRP A 1 82 ? 1.795 9.024 26.844 1.00 12.14 ? 90 TRP A O 1 ATOM 1110 C CB . TRP A 1 82 ? 0.188 7.536 24.955 1.00 12.02 ? 90 TRP A CB 1 ATOM 1111 C CG . TRP A 1 82 ? -0.926 8.550 24.913 1.00 11.70 ? 90 TRP A CG 1 ATOM 1112 C CD1 . TRP A 1 82 ? -0.961 9.727 24.215 1.00 11.85 ? 90 TRP A CD1 1 ATOM 1113 C CD2 . TRP A 1 82 ? -2.147 8.473 25.638 1.00 11.37 ? 90 TRP A CD2 1 ATOM 1114 N NE1 . TRP A 1 82 ? -2.154 10.367 24.440 1.00 11.66 ? 90 TRP A NE1 1 ATOM 1115 C CE2 . TRP A 1 82 ? -2.895 9.631 25.326 1.00 11.88 ? 90 TRP A CE2 1 ATOM 1116 C CE3 . TRP A 1 82 ? -2.679 7.533 26.526 1.00 11.65 ? 90 TRP A CE3 1 ATOM 1117 C CZ2 . TRP A 1 82 ? -4.149 9.870 25.881 1.00 13.22 ? 90 TRP A CZ2 1 ATOM 1118 C CZ3 . TRP A 1 82 ? -3.929 7.769 27.076 1.00 13.25 ? 90 TRP A CZ3 1 ATOM 1119 C CH2 . TRP A 1 82 ? -4.639 8.929 26.760 1.00 14.69 ? 90 TRP A CH2 1 ATOM 1120 H H . TRP A 1 82 ? 2.769 6.842 25.557 1.00 13.34 ? 90 TRP A H 1 ATOM 1121 H HA . TRP A 1 82 ? 1.555 8.476 23.754 1.00 13.24 ? 90 TRP A HA 1 ATOM 1122 H HB2 . TRP A 1 82 ? -0.015 6.847 24.303 1.00 14.42 ? 90 TRP A HB2 1 ATOM 1123 H HB3 . TRP A 1 82 ? 0.202 7.150 25.845 1.00 14.42 ? 90 TRP A HB3 1 ATOM 1124 H HD1 . TRP A 1 82 ? -0.293 10.028 23.643 1.00 14.22 ? 90 TRP A HD1 1 ATOM 1125 H HE1 . TRP A 1 82 ? -2.384 11.126 24.105 1.00 13.99 ? 90 TRP A HE1 1 ATOM 1126 H HE3 . TRP A 1 82 ? -2.199 6.769 26.751 1.00 13.98 ? 90 TRP A HE3 1 ATOM 1127 H HZ2 . TRP A 1 82 ? -4.636 10.632 25.666 1.00 15.87 ? 90 TRP A HZ2 1 ATOM 1128 H HZ3 . TRP A 1 82 ? -4.293 7.153 27.670 1.00 15.90 ? 90 TRP A HZ3 1 ATOM 1129 H HH2 . TRP A 1 82 ? -5.482 9.056 27.131 1.00 17.63 ? 90 TRP A HH2 1 ATOM 1130 N N . THR A 1 83 ? 2.407 10.348 25.140 1.00 11.10 ? 91 THR A N 1 ATOM 1131 C CA . THR A 1 83 ? 2.987 11.356 26.015 1.00 11.89 ? 91 THR A CA 1 ATOM 1132 C C . THR A 1 83 ? 2.084 12.563 26.278 1.00 12.91 ? 91 THR A C 1 ATOM 1133 O O . THR A 1 83 ? 2.583 13.644 26.578 1.00 14.37 ? 91 THR A O 1 ATOM 1134 C CB . THR A 1 83 ? 4.396 11.728 25.553 1.00 12.31 ? 91 THR A CB 1 ATOM 1135 O OG1 . THR A 1 83 ? 4.408 12.061 24.162 1.00 11.88 ? 91 THR A OG1 1 ATOM 1136 C CG2 . THR A 1 83 ? 5.349 10.592 25.720 1.00 12.84 ? 91 THR A CG2 1 ATOM 1137 H H . THR A 1 83 ? 2.402 10.559 24.307 1.00 13.32 ? 91 THR A H 1 ATOM 1138 H HA . THR A 1 83 ? 3.104 10.932 26.880 1.00 14.27 ? 91 THR A HA 1 ATOM 1139 H HB . THR A 1 83 ? 4.719 12.482 26.071 1.00 14.78 ? 91 THR A HB 1 ATOM 1140 H HG1 . THR A 1 83 ? 3.900 12.715 24.018 1.00 14.25 ? 91 THR A HG1 1 ATOM 1141 H HG21 . THR A 1 83 ? 6.234 10.855 25.420 1.00 15.41 ? 91 THR A HG21 1 ATOM 1142 H HG22 . THR A 1 83 ? 5.397 10.334 26.654 1.00 15.41 ? 91 THR A HG22 1 ATOM 1143 H HG23 . THR A 1 83 ? 5.052 9.831 25.198 1.00 15.41 ? 91 THR A HG23 1 ATOM 1144 N N . GLY A 1 84 ? 0.753 12.396 26.186 1.00 13.02 ? 92 GLY A N 1 ATOM 1145 C CA . GLY A 1 84 ? -0.168 13.287 26.859 1.00 14.42 ? 92 GLY A CA 1 ATOM 1146 C C . GLY A 1 84 ? -0.551 14.532 26.088 1.00 12.94 ? 92 GLY A C 1 ATOM 1147 O O . GLY A 1 84 ? -0.222 14.719 24.925 1.00 13.52 ? 92 GLY A O 1 ATOM 1148 H H . GLY A 1 84 ? 0.371 11.770 25.736 1.00 15.63 ? 92 GLY A H 1 ATOM 1149 H HA2 . GLY A 1 84 ? -0.983 12.801 27.060 1.00 17.31 ? 92 GLY A HA2 1 ATOM 1150 H HA3 . GLY A 1 84 ? 0.226 13.568 27.699 1.00 17.31 ? 92 GLY A HA3 1 ATOM 1151 N N . ASP A 1 85 ? -1.257 15.404 26.808 1.00 13.03 ? 93 ASP A N 1 ATOM 1152 C CA . ASP A 1 85 ? -1.868 16.663 26.339 1.00 12.99 ? 93 ASP A CA 1 ATOM 1153 C C . ASP A 1 85 ? -3.141 16.369 25.552 1.00 12.37 ? 93 ASP A C 1 ATOM 1154 O O . ASP A 1 85 ? -3.161 16.377 24.310 1.00 13.50 ? 93 ASP A O 1 ATOM 1155 C CB . ASP A 1 85 ? -0.896 17.542 25.561 1.00 12.10 ? 93 ASP A CB 1 ATOM 1156 C CG . ASP A 1 85 ? -0.338 18.700 26.364 1.00 11.66 ? 93 ASP A CG 1 ATOM 1157 O OD1 . ASP A 1 85 ? -0.527 18.745 27.582 1.00 14.17 ? 93 ASP A OD1 1 ATOM 1158 O OD2 . ASP A 1 85 ? 0.290 19.581 25.707 1.00 12.38 ? 93 ASP A OD2 1 ATOM 1159 H H . ASP A 1 85 ? -1.409 15.277 27.645 1.00 15.64 ? 93 ASP A H 1 ATOM 1160 H HA . ASP A 1 85 ? -2.135 17.170 27.122 1.00 15.58 ? 93 ASP A HA 1 ATOM 1161 H HB2 . ASP A 1 85 ? -0.149 16.997 25.268 1.00 14.52 ? 93 ASP A HB2 1 ATOM 1162 H HB3 . ASP A 1 85 ? -1.357 17.910 24.791 1.00 14.52 ? 93 ASP A HB3 1 ATOM 1163 N N . ASP A 1 86 ? -4.228 16.168 26.285 1.00 12.83 ? 94 ASP A N 1 ATOM 1164 C CA . ASP A 1 86 ? -5.459 15.626 25.749 1.00 12.87 ? 94 ASP A CA 1 ATOM 1165 C C . ASP A 1 86 ? -6.585 16.642 25.616 1.00 11.99 ? 94 ASP A C 1 ATOM 1166 O O . ASP A 1 86 ? -7.609 16.344 24.967 1.00 13.30 ? 94 ASP A O 1 ATOM 1167 C CB . ASP A 1 86 ? -5.976 14.506 26.655 1.00 13.39 ? 94 ASP A CB 1 ATOM 1168 C CG . ASP A 1 86 ? -4.962 13.406 26.902 1.00 13.71 ? 94 ASP A CG 1 ATOM 1169 O OD1 . ASP A 1 86 ? -4.014 13.260 26.118 1.00 13.91 ? 94 ASP A OD1 1 ATOM 1170 O OD2 . ASP A 1 86 ? -5.179 12.665 27.889 1.00 14.46 ? 94 ASP A OD2 1 ATOM 1171 H H . ASP A 1 86 ? -4.273 16.345 27.125 1.00 15.39 ? 94 ASP A H 1 ATOM 1172 H HA . ASP A 1 86 ? -5.285 15.250 24.872 1.00 15.45 ? 94 ASP A HA 1 ATOM 1173 H HB2 . ASP A 1 86 ? -6.218 14.885 27.514 1.00 16.07 ? 94 ASP A HB2 1 ATOM 1174 H HB3 . ASP A 1 86 ? -6.756 14.104 26.241 1.00 16.07 ? 94 ASP A HB3 1 ATOM 1175 N N . THR A 1 87 ? -6.456 17.788 26.266 1.00 12.81 ? 95 THR A N 1 ATOM 1176 C CA . THR A 1 87 ? -7.517 18.755 26.430 1.00 13.27 ? 95 THR A CA 1 ATOM 1177 C C . THR A 1 87 ? -7.203 19.994 25.599 1.00 12.79 ? 95 THR A C 1 ATOM 1178 O O . THR A 1 87 ? -6.077 20.178 25.129 1.00 14.78 ? 95 THR A O 1 ATOM 1179 C CB . THR A 1 87 ? -7.595 19.146 27.906 1.00 13.74 ? 95 THR A CB 1 ATOM 1180 O OG1 . THR A 1 87 ? -6.346 19.728 28.240 1.00 16.23 ? 95 THR A OG1 1 ATOM 1181 C CG2 . THR A 1 87 ? -7.848 17.953 28.806 1.00 16.16 ? 95 THR A CG2 1 ATOM 1182 H H . THR A 1 87 ? -5.722 18.035 26.639 1.00 15.37 ? 95 THR A H 1 ATOM 1183 H HA . THR A 1 87 ? -8.366 18.380 26.147 1.00 15.92 ? 95 THR A HA 1 ATOM 1184 H HB . THR A 1 87 ? -8.305 19.794 28.038 1.00 16.49 ? 95 THR A HB 1 ATOM 1185 H HG1 . THR A 1 87 ? -6.344 19.959 29.047 1.00 19.47 ? 95 THR A HG1 1 ATOM 1186 H HG21 . THR A 1 87 ? -7.891 18.239 29.732 1.00 19.39 ? 95 THR A HG21 1 ATOM 1187 H HG22 . THR A 1 87 ? -8.687 17.530 28.568 1.00 19.39 ? 95 THR A HG22 1 ATOM 1188 H HG23 . THR A 1 87 ? -7.130 17.307 28.709 1.00 19.39 ? 95 THR A HG23 1 ATOM 1189 N N . PRO A 1 88 ? -8.184 20.859 25.371 1.00 12.78 ? 96 PRO A N 1 ATOM 1190 C CA . PRO A 1 88 ? -7.984 21.966 24.437 1.00 13.94 ? 96 PRO A CA 1 ATOM 1191 C C . PRO A 1 88 ? -7.335 23.188 25.079 1.00 13.79 ? 96 PRO A C 1 ATOM 1192 O O . PRO A 1 88 ? -7.321 23.360 26.303 1.00 14.06 ? 96 PRO A O 1 ATOM 1193 C CB . PRO A 1 88 ? -9.421 22.279 23.997 1.00 15.91 ? 96 PRO A CB 1 ATOM 1194 C CG . PRO A 1 88 ? -10.219 21.993 25.185 1.00 15.43 ? 96 PRO A CG 1 ATOM 1195 C CD . PRO A 1 88 ? -9.587 20.742 25.793 1.00 13.30 ? 96 PRO A CD 1 ATOM 1196 H HA . PRO A 1 88 ? -7.462 21.680 23.671 1.00 16.73 ? 96 PRO A HA 1 ATOM 1197 H HB2 . PRO A 1 88 ? -9.494 23.214 23.747 1.00 19.09 ? 96 PRO A HB2 1 ATOM 1198 H HB3 . PRO A 1 88 ? -9.675 21.701 23.261 1.00 19.09 ? 96 PRO A HB3 1 ATOM 1199 H HG2 . PRO A 1 88 ? -10.167 22.740 25.802 1.00 18.51 ? 96 PRO A HG2 1 ATOM 1200 H HG3 . PRO A 1 88 ? -11.139 21.823 24.928 1.00 18.51 ? 96 PRO A HG3 1 ATOM 1201 H HD2 . PRO A 1 88 ? -9.655 20.762 26.761 1.00 15.96 ? 96 PRO A HD2 1 ATOM 1202 H HD3 . PRO A 1 88 ? -9.989 19.942 25.422 1.00 15.96 ? 96 PRO A HD3 1 ATOM 1203 N N . HIS A 1 89 ? -6.825 24.056 24.214 1.00 13.48 ? 97 HIS A N 1 ATOM 1204 C CA . HIS A 1 89 ? -6.192 25.312 24.609 1.00 13.77 ? 97 HIS A CA 1 ATOM 1205 C C . HIS A 1 89 ? -7.285 26.360 24.787 1.00 15.13 ? 97 HIS A C 1 ATOM 1206 O O . HIS A 1 89 ? -7.614 27.115 23.869 1.00 15.95 ? 97 HIS A O 1 ATOM 1207 C CB . HIS A 1 89 ? -5.187 25.757 23.562 1.00 13.39 ? 97 HIS A CB 1 ATOM 1208 C CG . HIS A 1 89 ? -4.036 24.832 23.372 1.00 12.94 ? 97 HIS A CG 1 ATOM 1209 N ND1 . HIS A 1 89 ? -4.115 23.729 22.565 1.00 12.83 ? 97 HIS A ND1 1 ATOM 1210 C CD2 . HIS A 1 89 ? -2.788 24.816 23.898 1.00 12.65 ? 97 HIS A CD2 1 ATOM 1211 C CE1 . HIS A 1 89 ? -2.962 23.091 22.561 1.00 12.91 ? 97 HIS A CE1 1 ATOM 1212 N NE2 . HIS A 1 89 ? -2.148 23.724 23.371 1.00 12.69 ? 97 HIS A NE2 1 ATOM 1213 H H . HIS A 1 89 ? -6.833 23.937 23.362 1.00 16.18 ? 97 HIS A H 1 ATOM 1214 H HA . HIS A 1 89 ? -5.731 25.196 25.455 1.00 16.52 ? 97 HIS A HA 1 ATOM 1215 H HB2 . HIS A 1 89 ? -5.643 25.837 22.709 1.00 16.06 ? 97 HIS A HB2 1 ATOM 1216 H HB3 . HIS A 1 89 ? -4.829 26.621 23.822 1.00 16.06 ? 97 HIS A HB3 1 ATOM 1217 H HD1 . HIS A 1 89 ? -4.804 23.505 22.102 1.00 15.39 ? 97 HIS A HD1 1 ATOM 1218 H HD2 . HIS A 1 89 ? -2.429 25.437 24.489 1.00 15.18 ? 97 HIS A HD2 1 ATOM 1219 H HE1 . HIS A 1 89 ? -2.770 22.312 22.091 1.00 15.50 ? 97 HIS A HE1 1 ATOM 1220 N N . VAL A 1 90 ? -7.873 26.356 25.979 1.00 14.97 ? 98 VAL A N 1 ATOM 1221 C CA . VAL A 1 90 ? -8.952 27.254 26.383 1.00 15.53 ? 98 VAL A CA 1 ATOM 1222 C C . VAL A 1 90 ? -8.690 27.730 27.806 1.00 17.10 ? 98 VAL A C 1 ATOM 1223 O O . VAL A 1 90 ? -7.826 27.174 28.505 1.00 17.46 ? 98 VAL A O 1 ATOM 1224 C CB . VAL A 1 90 ? -10.322 26.563 26.296 1.00 16.39 ? 98 VAL A CB 1 ATOM 1225 C CG1 . VAL A 1 90 ? -10.600 26.158 24.869 1.00 17.13 ? 98 VAL A CG1 1 ATOM 1226 C CG2 . VAL A 1 90 ? -10.397 25.373 27.246 1.00 18.38 ? 98 VAL A CG2 1 ATOM 1227 H H . VAL A 1 90 ? -7.650 25.809 26.605 1.00 17.97 ? 98 VAL A H 1 ATOM 1228 H HA . VAL A 1 90 ? -8.962 28.028 25.799 1.00 18.64 ? 98 VAL A HA 1 ATOM 1229 H HB . VAL A 1 90 ? -11.008 27.197 26.561 1.00 19.67 ? 98 VAL A HB 1 ATOM 1230 H HG11 . VAL A 1 90 ? -11.467 25.724 24.827 1.00 20.56 ? 98 VAL A HG11 1 ATOM 1231 H HG12 . VAL A 1 90 ? -10.600 26.951 24.310 1.00 20.56 ? 98 VAL A HG12 1 ATOM 1232 H HG13 . VAL A 1 90 ? -9.909 25.545 24.575 1.00 20.56 ? 98 VAL A HG13 1 ATOM 1233 H HG21 . VAL A 1 90 ? -11.271 24.961 27.166 1.00 22.06 ? 98 VAL A HG21 1 ATOM 1234 H HG22 . VAL A 1 90 ? -9.706 24.735 27.006 1.00 22.06 ? 98 VAL A HG22 1 ATOM 1235 H HG23 . VAL A 1 90 ? -10.259 25.686 28.154 1.00 22.06 ? 98 VAL A HG23 1 ATOM 1236 N N . PRO A 1 91 ? -9.380 28.768 28.267 1.00 17.57 ? 99 PRO A N 1 ATOM 1237 C CA . PRO A 1 91 ? -9.187 29.218 29.652 1.00 19.44 ? 99 PRO A CA 1 ATOM 1238 C C . PRO A 1 91 ? -9.574 28.139 30.653 1.00 18.85 ? 99 PRO A C 1 ATOM 1239 O O . PRO A 1 91 ? -10.441 27.309 30.410 1.00 19.11 ? 99 PRO A O 1 ATOM 1240 C CB . PRO A 1 91 ? -10.118 30.433 29.759 1.00 21.33 ? 99 PRO A CB 1 ATOM 1241 C CG . PRO A 1 91 ? -10.215 30.925 28.352 1.00 21.69 ? 99 PRO A CG 1 ATOM 1242 C CD . PRO A 1 91 ? -10.237 29.690 27.509 1.00 20.46 ? 99 PRO A CD 1 ATOM 1243 H HA . PRO A 1 91 ? -8.269 29.493 29.801 1.00 23.32 ? 99 PRO A HA 1 ATOM 1244 H HB2 . PRO A 1 91 ? -10.987 30.156 30.091 1.00 25.60 ? 99 PRO A HB2 1 ATOM 1245 H HB3 . PRO A 1 91 ? -9.722 31.104 30.336 1.00 25.60 ? 99 PRO A HB3 1 ATOM 1246 H HG2 . PRO A 1 91 ? -11.033 31.433 28.238 1.00 26.02 ? 99 PRO A HG2 1 ATOM 1247 H HG3 . PRO A 1 91 ? -9.440 31.469 28.142 1.00 26.02 ? 99 PRO A HG3 1 ATOM 1248 H HD2 . PRO A 1 91 ? -11.139 29.339 27.444 1.00 24.56 ? 99 PRO A HD2 1 ATOM 1249 H HD3 . PRO A 1 91 ? -9.857 29.867 26.635 1.00 24.56 ? 99 PRO A HD3 1 ATOM 1250 N N . ASN A 1 92 ? -8.945 28.190 31.822 1.00 20.22 ? 100 ASN A N 1 ATOM 1251 C CA . ASN A 1 92 ? -9.256 27.208 32.860 1.00 19.90 ? 100 ASN A CA 1 ATOM 1252 C C . ASN A 1 92 ? -10.743 27.183 33.186 1.00 20.06 ? 100 ASN A C 1 ATOM 1253 O O . ASN A 1 92 ? -11.309 26.116 33.455 1.00 21.14 ? 100 ASN A O 1 ATOM 1254 C CB . ASN A 1 92 ? -8.465 27.518 34.128 1.00 22.01 ? 100 ASN A CB 1 ATOM 1255 C CG . ASN A 1 92 ? -7.034 27.068 34.040 1.00 23.40 ? 100 ASN A CG 1 ATOM 1256 O OD1 . ASN A 1 92 ? -6.732 25.980 33.526 1.00 23.24 ? 100 ASN A OD1 1 ATOM 1257 N ND2 . ASN A 1 92 ? -6.139 27.878 34.571 1.00 25.89 ? 100 ASN A ND2 1 ATOM 1258 H H . ASN A 1 92 ? -8.347 28.769 32.039 1.00 24.26 ? 100 ASN A H 1 ATOM 1259 H HA . ASN A 1 92 ? -8.999 26.325 32.551 1.00 23.88 ? 100 ASN A HA 1 ATOM 1260 H HB2 . ASN A 1 92 ? -8.469 28.477 34.277 1.00 26.41 ? 100 ASN A HB2 1 ATOM 1261 H HB3 . ASN A 1 92 ? -8.878 27.063 34.878 1.00 26.41 ? 100 ASN A HB3 1 ATOM 1262 H HD21 . ASN A 1 92 ? -5.305 27.670 34.549 1.00 31.07 ? 100 ASN A HD21 1 ATOM 1263 H HD22 . ASN A 1 92 ? -6.389 28.614 34.938 1.00 31.07 ? 100 ASN A HD22 1 ATOM 1264 N N . GLU A 1 93 ? -11.393 28.349 33.166 1.00 21.23 ? 101 GLU A N 1 ATOM 1265 C CA . GLU A 1 93 ? -12.811 28.452 33.509 1.00 23.61 ? 101 GLU A CA 1 ATOM 1266 C C . GLU A 1 93 ? -13.703 27.685 32.537 1.00 22.22 ? 101 GLU A C 1 ATOM 1267 O O . GLU A 1 93 ? -14.863 27.398 32.860 1.00 24.75 ? 101 GLU A O 1 ATOM 1268 C CB . GLU A 1 93 ? -13.211 29.933 33.551 1.00 26.75 ? 101 GLU A CB 1 ATOM 1269 C CG . GLU A 1 93 ? -12.531 30.727 34.662 1.00 32.17 ? 101 GLU A CG 1 ATOM 1270 C CD . GLU A 1 93 ? -11.016 30.902 34.473 1.00 36.17 ? 101 GLU A CD 1 ATOM 1271 O OE1 . GLU A 1 93 ? -10.545 30.976 33.309 1.00 33.19 ? 101 GLU A OE1 1 ATOM 1272 O OE2 . GLU A 1 93 ? -10.300 30.969 35.508 1.00 40.96 ? 101 GLU A OE2 1 ATOM 1273 H H . GLU A 1 93 ? -11.031 29.100 32.955 1.00 25.48 ? 101 GLU A H 1 ATOM 1274 H HA . GLU A 1 93 ? -12.947 28.081 34.395 1.00 28.33 ? 101 GLU A HA 1 ATOM 1275 H HB2 . GLU A 1 93 ? -12.974 30.344 32.705 1.00 32.10 ? 101 GLU A HB2 1 ATOM 1276 H HB3 . GLU A 1 93 ? -14.170 29.993 33.688 1.00 32.10 ? 101 GLU A HB3 1 ATOM 1277 H HG2 . GLU A 1 93 ? -12.928 31.611 34.701 1.00 38.60 ? 101 GLU A HG2 1 ATOM 1278 H HG3 . GLU A 1 93 ? -12.672 30.267 35.504 1.00 38.60 ? 101 GLU A HG3 1 ATOM 1279 N N . SER A 1 94 ? -13.187 27.338 31.370 1.00 20.73 ? 102 SER A N 1 ATOM 1280 C CA . SER A 1 94 ? -13.905 26.594 30.353 1.00 22.27 ? 102 SER A CA 1 ATOM 1281 C C . SER A 1 94 ? -13.707 25.094 30.474 1.00 22.25 ? 102 SER A C 1 ATOM 1282 O O . SER A 1 94 ? -14.323 24.342 29.710 1.00 24.15 ? 102 SER A O 1 ATOM 1283 C CB . SER A 1 94 ? -13.393 27.030 28.982 1.00 23.83 ? 102 SER A CB 1 ATOM 1284 O OG . SER A 1 94 ? -13.782 28.362 28.711 1.00 26.98 ? 102 SER A OG 1 ATOM 1285 H H . SER A 1 94 ? -12.383 27.534 31.134 1.00 24.88 ? 102 SER A H 1 ATOM 1286 H HA . SER A 1 94 ? -14.854 26.790 30.410 1.00 26.72 ? 102 SER A HA 1 ATOM 1287 H HB2 . SER A 1 94 ? -12.425 26.974 28.972 1.00 28.59 ? 102 SER A HB2 1 ATOM 1288 H HB3 . SER A 1 94 ? -13.768 26.446 28.303 1.00 28.59 ? 102 SER A HB3 1 ATOM 1289 H HG . SER A 1 94 ? -13.498 28.596 27.956 1.00 32.37 ? 102 SER A HG 1 ATOM 1290 N N . LEU A 1 95 ? -12.854 24.641 31.400 1.00 20.72 ? 103 LEU A N 1 ATOM 1291 C CA . LEU A 1 95 ? -12.334 23.276 31.402 1.00 24.09 ? 103 LEU A CA 1 ATOM 1292 C C . LEU A 1 95 ? -11.963 22.877 32.839 1.00 24.40 ? 103 LEU A C 1 ATOM 1293 O O . LEU A 1 95 ? -10.801 22.915 33.259 1.00 25.67 ? 103 LEU A O 1 ATOM 1294 C CB . LEU A 1 95 ? -11.115 23.230 30.491 1.00 27.15 ? 103 LEU A CB 1 ATOM 1295 C CG . LEU A 1 95 ? -10.419 21.927 30.212 1.00 30.63 ? 103 LEU A CG 1 ATOM 1296 C CD1 . LEU A 1 95 ? -11.376 21.005 29.500 1.00 30.17 ? 103 LEU A CD1 1 ATOM 1297 C CD2 . LEU A 1 95 ? -9.211 22.292 29.377 1.00 31.42 ? 103 LEU A CD2 1 ATOM 1298 H H . LEU A 1 95 ? -12.557 25.120 32.050 1.00 24.87 ? 103 LEU A H 1 ATOM 1299 H HA . LEU A 1 95 ? -13.005 22.663 31.065 1.00 28.90 ? 103 LEU A HA 1 ATOM 1300 H HB2 . LEU A 1 95 ? -11.384 23.585 29.629 1.00 32.58 ? 103 LEU A HB2 1 ATOM 1301 H HB3 . LEU A 1 95 ? -10.446 23.820 30.873 1.00 32.58 ? 103 LEU A HB3 1 ATOM 1302 H HG . LEU A 1 95 ? -10.127 21.515 31.041 1.00 36.76 ? 103 LEU A HG 1 ATOM 1303 H HD11 . LEU A 1 95 ? -10.929 20.164 29.319 1.00 36.21 ? 103 LEU A HD11 1 ATOM 1304 H HD12 . LEU A 1 95 ? -12.149 20.855 30.066 1.00 36.21 ? 103 LEU A HD12 1 ATOM 1305 H HD13 . LEU A 1 95 ? -11.652 21.420 28.667 1.00 36.21 ? 103 LEU A HD13 1 ATOM 1306 H HD21 . LEU A 1 95 ? -8.719 21.483 29.164 1.00 37.70 ? 103 LEU A HD21 1 ATOM 1307 H HD22 . LEU A 1 95 ? -9.511 22.721 28.560 1.00 37.70 ? 103 LEU A HD22 1 ATOM 1308 H HD23 . LEU A 1 95 ? -8.649 22.898 29.883 1.00 37.70 ? 103 LEU A HD23 1 ATOM 1309 N N . GLY A 1 96 ? -12.965 22.447 33.592 1.00 21.76 ? 104 GLY A N 1 ATOM 1310 C CA . GLY A 1 96 ? -12.780 22.048 34.976 1.00 18.88 ? 104 GLY A CA 1 ATOM 1311 C C . GLY A 1 96 ? -12.271 20.626 35.120 1.00 16.93 ? 104 GLY A C 1 ATOM 1312 O O . GLY A 1 96 ? -12.033 19.912 34.155 1.00 16.80 ? 104 GLY A O 1 ATOM 1313 H H . GLY A 1 96 ? -13.777 22.377 33.318 1.00 26.11 ? 104 GLY A H 1 ATOM 1314 H HA2 . GLY A 1 96 ? -12.144 22.645 35.401 1.00 22.66 ? 104 GLY A HA2 1 ATOM 1315 H HA3 . GLY A 1 96 ? -13.626 22.118 35.446 1.00 22.66 ? 104 GLY A HA3 1 ATOM 1316 N N . GLU A 1 97 ? -12.087 20.213 36.373 1.00 16.81 ? 105 GLU A N 1 ATOM 1317 C CA . GLU A 1 97 ? -11.502 18.909 36.653 1.00 15.80 ? 105 GLU A CA 1 ATOM 1318 C C . GLU A 1 97 ? -12.318 17.764 36.056 1.00 15.37 ? 105 GLU A C 1 ATOM 1319 O O . GLU A 1 97 ? -11.754 16.812 35.512 1.00 15.31 ? 105 GLU A O 1 ATOM 1320 C CB . GLU A 1 97 ? -11.370 18.739 38.158 1.00 18.71 ? 105 GLU A CB 1 ATOM 1321 C CG . GLU A 1 97 ? -10.769 17.452 38.571 1.00 22.23 ? 105 GLU A CG 1 ATOM 1322 C CD . GLU A 1 97 ? -10.523 17.391 40.075 1.00 27.76 ? 105 GLU A CD 1 ATOM 1323 O OE1 . GLU A 1 97 ? -10.102 18.408 40.663 1.00 31.16 ? 105 GLU A OE1 1 ATOM 1324 O OE2 . GLU A 1 97 ? -10.781 16.340 40.670 1.00 30.26 ? 105 GLU A OE2 1 ATOM 1325 H H . GLU A 1 97 ? -12.292 20.668 37.073 1.00 20.18 ? 105 GLU A H 1 ATOM 1326 H HA . GLU A 1 97 ? -10.612 18.874 36.269 1.00 18.95 ? 105 GLU A HA 1 ATOM 1327 H HB2 . GLU A 1 97 ? -10.810 19.451 38.504 1.00 22.46 ? 105 GLU A HB2 1 ATOM 1328 H HB3 . GLU A 1 97 ? -12.253 18.794 38.556 1.00 22.46 ? 105 GLU A HB3 1 ATOM 1329 H HG2 . GLU A 1 97 ? -11.370 16.729 38.334 1.00 26.68 ? 105 GLU A HG2 1 ATOM 1330 H HG3 . GLU A 1 97 ? -9.917 17.339 38.121 1.00 26.68 ? 105 GLU A HG3 1 ATOM 1331 N N . ALA A 1 98 ? -13.644 17.812 36.163 1.00 15.75 ? 106 ALA A N 1 ATOM 1332 C CA . ALA A 1 98 ? -14.445 16.695 35.669 1.00 15.20 ? 106 ALA A CA 1 ATOM 1333 C C . ALA A 1 98 ? -14.276 16.531 34.170 1.00 14.55 ? 106 ALA A C 1 ATOM 1334 O O . ALA A 1 98 ? -14.124 15.412 33.686 1.00 14.97 ? 106 ALA A O 1 ATOM 1335 C CB . ALA A 1 98 ? -15.918 16.895 36.002 1.00 18.02 ? 106 ALA A CB 1 ATOM 1336 H H . ALA A 1 98 ? -14.093 18.460 36.507 1.00 18.90 ? 106 ALA A H 1 ATOM 1337 H HA . ALA A 1 98 ? -14.148 15.877 36.098 1.00 18.24 ? 106 ALA A HA 1 ATOM 1338 H HB1 . ALA A 1 98 ? -16.423 16.140 35.662 1.00 21.62 ? 106 ALA A HB1 1 ATOM 1339 H HB2 . ALA A 1 98 ? -16.018 16.956 36.964 1.00 21.62 ? 106 ALA A HB2 1 ATOM 1340 H HB3 . ALA A 1 98 ? -16.226 17.715 35.584 1.00 21.62 ? 106 ALA A HB3 1 ATOM 1341 N N . ALA A 1 99 ? -14.266 17.647 33.429 1.00 15.32 ? 107 ALA A N 1 ATOM 1342 C CA . ALA A 1 99 ? -14.060 17.591 31.985 1.00 14.95 ? 107 ALA A CA 1 ATOM 1343 C C . ALA A 1 99 ? -12.668 17.099 31.630 1.00 14.19 ? 107 ALA A C 1 ATOM 1344 O O . ALA A 1 99 ? -12.513 16.292 30.707 1.00 14.25 ? 107 ALA A O 1 ATOM 1345 C CB . ALA A 1 99 ? -14.303 18.954 31.360 1.00 16.34 ? 107 ALA A CB 1 ATOM 1346 H H . ALA A 1 99 ? -14.377 18.441 33.740 1.00 18.39 ? 107 ALA A H 1 ATOM 1347 H HA . ALA A 1 99 ? -14.700 16.971 31.602 1.00 17.94 ? 107 ALA A HA 1 ATOM 1348 H HB1 . ALA A 1 99 ? -14.160 18.892 30.403 1.00 19.60 ? 107 ALA A HB1 1 ATOM 1349 H HB2 . ALA A 1 99 ? -15.216 19.226 31.542 1.00 19.60 ? 107 ALA A HB2 1 ATOM 1350 H HB3 . ALA A 1 99 ? -13.684 19.592 31.747 1.00 19.60 ? 107 ALA A HB3 1 ATOM 1351 N N . VAL A 1 100 ? -11.642 17.536 32.367 1.00 13.58 ? 108 VAL A N 1 ATOM 1352 C CA . VAL A 1 100 ? -10.296 17.038 32.100 1.00 13.65 ? 108 VAL A CA 1 ATOM 1353 C C . VAL A 1 100 ? -10.282 15.529 32.241 1.00 13.24 ? 108 VAL A C 1 ATOM 1354 O O . VAL A 1 100 ? -9.816 14.798 31.361 1.00 13.56 ? 108 VAL A O 1 ATOM 1355 C CB . VAL A 1 100 ? -9.266 17.698 33.040 1.00 15.37 ? 108 VAL A CB 1 ATOM 1356 C CG1 . VAL A 1 100 ? -7.905 16.998 32.927 1.00 15.66 ? 108 VAL A CG1 1 ATOM 1357 C CG2 . VAL A 1 100 ? -9.107 19.178 32.729 1.00 16.67 ? 108 VAL A CG2 1 ATOM 1358 H H . VAL A 1 100 ? -11.698 18.106 33.009 1.00 16.30 ? 108 VAL A H 1 ATOM 1359 H HA . VAL A 1 100 ? -10.053 17.257 31.187 1.00 16.38 ? 108 VAL A HA 1 ATOM 1360 H HB . VAL A 1 100 ? -9.573 17.614 33.956 1.00 18.44 ? 108 VAL A HB 1 ATOM 1361 H HG11 . VAL A 1 100 ? -7.277 17.431 33.526 1.00 18.79 ? 108 VAL A HG11 1 ATOM 1362 H HG12 . VAL A 1 100 ? -8.008 16.066 33.173 1.00 18.79 ? 108 VAL A HG12 1 ATOM 1363 H HG13 . VAL A 1 100 ? -7.590 17.067 32.012 1.00 18.79 ? 108 VAL A HG13 1 ATOM 1364 H HG21 . VAL A 1 100 ? -8.454 19.559 33.337 1.00 20.01 ? 108 VAL A HG21 1 ATOM 1365 H HG22 . VAL A 1 100 ? -8.804 19.277 31.813 1.00 20.01 ? 108 VAL A HG22 1 ATOM 1366 H HG23 . VAL A 1 100 ? -9.963 19.618 32.844 1.00 20.01 ? 108 VAL A HG23 1 ATOM 1367 N N . LEU A 1 101 ? -10.801 15.026 33.365 1.00 13.65 ? 109 LEU A N 1 ATOM 1368 C CA . LEU A 1 101 ? -10.761 13.592 33.588 1.00 14.06 ? 109 LEU A CA 1 ATOM 1369 C C . LEU A 1 101 ? -11.606 12.832 32.577 1.00 13.31 ? 109 LEU A C 1 ATOM 1370 O O . LEU A 1 101 ? -11.232 11.735 32.151 1.00 14.35 ? 109 LEU A O 1 ATOM 1371 C CB . LEU A 1 101 ? -11.200 13.273 35.012 1.00 14.89 ? 109 LEU A CB 1 ATOM 1372 C CG . LEU A 1 101 ? -10.171 13.686 36.042 1.00 15.28 ? 109 LEU A CG 1 ATOM 1373 C CD1 . LEU A 1 101 ? -10.757 13.573 37.436 1.00 16.64 ? 109 LEU A CD1 1 ATOM 1374 C CD2 . LEU A 1 101 ? -8.935 12.813 35.928 1.00 17.48 ? 109 LEU A CD2 1 ATOM 1375 H H . LEU A 1 101 ? -11.170 15.484 33.993 1.00 16.38 ? 109 LEU A H 1 ATOM 1376 H HA . LEU A 1 101 ? -9.845 13.290 33.490 1.00 16.87 ? 109 LEU A HA 1 ATOM 1377 H HB2 . LEU A 1 101 ? -12.024 13.748 35.203 1.00 17.86 ? 109 LEU A HB2 1 ATOM 1378 H HB3 . LEU A 1 101 ? -11.341 12.317 35.093 1.00 17.86 ? 109 LEU A HB3 1 ATOM 1379 H HG . LEU A 1 101 ? -9.912 14.608 35.890 1.00 18.33 ? 109 LEU A HG 1 ATOM 1380 H HD11 . LEU A 1 101 ? -10.086 13.841 38.083 1.00 19.97 ? 109 LEU A HD11 1 ATOM 1381 H HD12 . LEU A 1 101 ? -11.530 14.156 37.501 1.00 19.97 ? 109 LEU A HD12 1 ATOM 1382 H HD13 . LEU A 1 101 ? -11.021 12.654 37.594 1.00 19.97 ? 109 LEU A HD13 1 ATOM 1383 H HD21 . LEU A 1 101 ? -8.289 13.093 36.595 1.00 20.98 ? 109 LEU A HD21 1 ATOM 1384 H HD22 . LEU A 1 101 ? -9.187 11.889 36.078 1.00 20.98 ? 109 LEU A HD22 1 ATOM 1385 H HD23 . LEU A 1 101 ? -8.559 12.914 35.040 1.00 20.98 ? 109 LEU A HD23 1 ATOM 1386 N N . ALA A 1 102 ? -12.755 13.380 32.189 1.00 13.50 ? 110 ALA A N 1 ATOM 1387 C CA . ALA A 1 102 ? -13.615 12.724 31.204 1.00 13.62 ? 110 ALA A CA 1 ATOM 1388 C C . ALA A 1 102 ? -12.936 12.648 29.846 1.00 12.36 ? 110 ALA A C 1 ATOM 1389 O O . ALA A 1 102 ? -13.053 11.644 29.132 1.00 13.32 ? 110 ALA A O 1 ATOM 1390 C CB . ALA A 1 102 ? -14.936 13.482 31.099 1.00 14.63 ? 110 ALA A CB 1 ATOM 1391 H H . ALA A 1 102 ? -13.060 14.129 32.480 1.00 16.20 ? 110 ALA A H 1 ATOM 1392 H HA . ALA A 1 102 ? -13.807 11.820 31.499 1.00 16.34 ? 110 ALA A HA 1 ATOM 1393 H HB1 . ALA A 1 102 ? -15.501 13.043 30.445 1.00 17.56 ? 110 ALA A HB1 1 ATOM 1394 H HB2 . ALA A 1 102 ? -15.370 13.481 31.967 1.00 17.56 ? 110 ALA A HB2 1 ATOM 1395 H HB3 . ALA A 1 102 ? -14.755 14.394 30.821 1.00 17.56 ? 110 ALA A HB3 1 ATOM 1396 N N . ILE A 1 103 ? -12.177 13.684 29.492 1.00 12.20 ? 111 ILE A N 1 ATOM 1397 C CA . ILE A 1 103 ? -11.454 13.695 28.232 1.00 12.83 ? 111 ILE A CA 1 ATOM 1398 C C . ILE A 1 103 ? -10.319 12.680 28.250 1.00 12.68 ? 111 ILE A C 1 ATOM 1399 O O . ILE A 1 103 ? -10.152 11.898 27.310 1.00 12.88 ? 111 ILE A O 1 ATOM 1400 C CB . ILE A 1 103 ? -10.997 15.122 27.882 1.00 13.53 ? 111 ILE A CB 1 ATOM 1401 C CG1 . ILE A 1 103 ? -12.216 15.998 27.536 1.00 14.40 ? 111 ILE A CG1 1 ATOM 1402 C CG2 . ILE A 1 103 ? -9.977 15.097 26.734 1.00 14.50 ? 111 ILE A CG2 1 ATOM 1403 C CD1 . ILE A 1 103 ? -11.917 17.458 27.461 1.00 15.95 ? 111 ILE A CD1 1 ATOM 1404 H H . ILE A 1 103 ? -12.068 14.392 29.968 1.00 14.64 ? 111 ILE A H 1 ATOM 1405 H HA . ILE A 1 103 ? -12.068 13.418 27.534 1.00 15.39 ? 111 ILE A HA 1 ATOM 1406 H HB . ILE A 1 103 ? -10.564 15.501 28.663 1.00 16.23 ? 111 ILE A HB 1 ATOM 1407 H HG12 . ILE A 1 103 ? -12.563 15.723 26.673 1.00 17.28 ? 111 ILE A HG12 1 ATOM 1408 H HG13 . ILE A 1 103 ? -12.895 15.870 28.217 1.00 17.28 ? 111 ILE A HG13 1 ATOM 1409 H HG21 . ILE A 1 103 ? -9.706 16.006 26.534 1.00 17.40 ? 111 ILE A HG21 1 ATOM 1410 H HG22 . ILE A 1 103 ? -9.208 14.574 27.008 1.00 17.40 ? 111 ILE A HG22 1 ATOM 1411 H HG23 . ILE A 1 103 ? -10.391 14.695 25.954 1.00 17.40 ? 111 ILE A HG23 1 ATOM 1412 H HD11 . ILE A 1 103 ? -12.732 17.936 27.240 1.00 19.14 ? 111 ILE A HD11 1 ATOM 1413 H HD12 . ILE A 1 103 ? -11.582 17.756 28.321 1.00 19.14 ? 111 ILE A HD12 1 ATOM 1414 H HD13 . ILE A 1 103 ? -11.249 17.608 26.775 1.00 19.14 ? 111 ILE A HD13 1 ATOM 1415 N N . VAL A 1 104 ? -9.537 12.645 29.334 1.00 12.60 ? 112 VAL A N 1 ATOM 1416 C CA . VAL A 1 104 ? -8.479 11.646 29.426 1.00 13.06 ? 112 VAL A CA 1 ATOM 1417 C C . VAL A 1 104 ? -9.065 10.247 29.321 1.00 13.25 ? 112 VAL A C 1 ATOM 1418 O O . VAL A 1 104 ? -8.530 9.386 28.609 1.00 14.44 ? 112 VAL A O 1 ATOM 1419 C CB . VAL A 1 104 ? -7.661 11.824 30.714 1.00 13.59 ? 112 VAL A CB 1 ATOM 1420 C CG1 . VAL A 1 104 ? -6.616 10.743 30.826 1.00 14.44 ? 112 VAL A CG1 1 ATOM 1421 C CG2 . VAL A 1 104 ? -6.993 13.209 30.754 1.00 14.30 ? 112 VAL A CG2 1 ATOM 1422 H H . VAL A 1 104 ? -9.597 13.174 30.009 1.00 15.12 ? 112 VAL A H 1 ATOM 1423 H HA . VAL A 1 104 ? -7.875 11.766 28.677 1.00 15.67 ? 112 VAL A HA 1 ATOM 1424 H HB . VAL A 1 104 ? -8.253 11.752 31.479 1.00 16.31 ? 112 VAL A HB 1 ATOM 1425 H HG11 . VAL A 1 104 ? -6.112 10.874 31.645 1.00 17.33 ? 112 VAL A HG11 1 ATOM 1426 H HG12 . VAL A 1 104 ? -7.056 9.879 30.844 1.00 17.33 ? 112 VAL A HG12 1 ATOM 1427 H HG13 . VAL A 1 104 ? -6.022 10.797 30.061 1.00 17.33 ? 112 VAL A HG13 1 ATOM 1428 H HG21 . VAL A 1 104 ? -6.486 13.291 31.577 1.00 17.16 ? 112 VAL A HG21 1 ATOM 1429 H HG22 . VAL A 1 104 ? -6.402 13.296 29.990 1.00 17.16 ? 112 VAL A HG22 1 ATOM 1430 H HG23 . VAL A 1 104 ? -7.681 13.892 30.720 1.00 17.16 ? 112 VAL A HG23 1 ATOM 1431 N N . GLU A 1 105 ? -10.191 10.014 29.988 1.00 13.42 ? 113 GLU A N 1 ATOM 1432 C CA A GLU A 1 105 ? -10.843 8.710 29.935 0.57 13.72 ? 113 GLU A CA 1 ATOM 1433 C CA B GLU A 1 105 ? -10.844 8.711 29.935 0.43 14.22 ? 113 GLU A CA 1 ATOM 1434 C C . GLU A 1 105 ? -11.313 8.375 28.522 1.00 13.38 ? 113 GLU A C 1 ATOM 1435 O O . GLU A 1 105 ? -11.142 7.237 28.057 1.00 14.21 ? 113 GLU A O 1 ATOM 1436 C CB A GLU A 1 105 ? -12.029 8.698 30.902 0.57 15.24 ? 113 GLU A CB 1 ATOM 1437 C CB B GLU A 1 105 ? -12.031 8.714 30.896 0.43 16.40 ? 113 GLU A CB 1 ATOM 1438 C CG A GLU A 1 105 ? -12.866 7.440 30.823 0.57 18.31 ? 113 GLU A CG 1 ATOM 1439 C CG B GLU A 1 105 ? -12.834 7.438 30.895 0.43 19.73 ? 113 GLU A CG 1 ATOM 1440 C CD A GLU A 1 105 ? -13.864 7.309 31.965 0.57 23.71 ? 113 GLU A CD 1 ATOM 1441 C CD B GLU A 1 105 ? -14.003 7.495 31.857 0.43 24.29 ? 113 GLU A CD 1 ATOM 1442 O OE1 A GLU A 1 105 ? -13.783 8.076 32.944 0.57 24.27 ? 113 GLU A OE1 1 ATOM 1443 O OE1 B GLU A 1 105 ? -14.833 8.424 31.728 0.43 26.06 ? 113 GLU A OE1 1 ATOM 1444 O OE2 A GLU A 1 105 ? -14.757 6.440 31.874 0.57 28.14 ? 113 GLU A OE2 1 ATOM 1445 O OE2 B GLU A 1 105 ? -14.094 6.619 32.743 0.43 25.91 ? 113 GLU A OE2 1 ATOM 1446 H H . GLU A 1 105 ? -10.597 10.591 30.479 1.00 16.11 ? 113 GLU A H 1 ATOM 1447 H HA . GLU A 1 105 ? -10.217 8.026 30.219 1.00 17.07 ? 113 GLU A HA 1 ATOM 1448 H HB2 A GLU A 1 105 ? -11.695 8.776 31.810 0.57 18.28 ? 113 GLU A HB2 1 ATOM 1449 H HB2 B GLU A 1 105 ? -11.701 8.854 31.798 0.43 19.68 ? 113 GLU A HB2 1 ATOM 1450 H HB3 A GLU A 1 105 ? -12.606 9.451 30.699 0.57 18.28 ? 113 GLU A HB3 1 ATOM 1451 H HB3 B GLU A 1 105 ? -12.628 9.438 30.651 0.43 19.68 ? 113 GLU A HB3 1 ATOM 1452 H HG2 A GLU A 1 105 ? -13.364 7.445 29.990 0.57 21.97 ? 113 GLU A HG2 1 ATOM 1453 H HG2 B GLU A 1 105 ? -13.184 7.284 30.004 0.43 23.67 ? 113 GLU A HG2 1 ATOM 1454 H HG3 A GLU A 1 105 ? -12.277 6.669 30.851 0.57 21.97 ? 113 GLU A HG3 1 ATOM 1455 H HG3 B GLU A 1 105 ? -12.261 6.702 31.161 0.43 23.67 ? 113 GLU A HG3 1 ATOM 1456 N N . ARG A 1 106 ? -11.906 9.345 27.815 1.00 14.04 ? 114 ARG A N 1 ATOM 1457 C CA . ARG A 1 106 ? -12.393 9.062 26.469 1.00 14.61 ? 114 ARG A CA 1 ATOM 1458 C C . ARG A 1 106 ? -11.246 8.663 25.546 1.00 13.44 ? 114 ARG A C 1 ATOM 1459 O O . ARG A 1 106 ? -11.362 7.695 24.779 1.00 13.66 ? 114 ARG A O 1 ATOM 1460 C CB . ARG A 1 106 ? -13.140 10.264 25.915 1.00 15.60 ? 114 ARG A CB 1 ATOM 1461 C CG . ARG A 1 106 ? -13.911 9.913 24.645 1.00 16.88 ? 114 ARG A CG 1 ATOM 1462 C CD . ARG A 1 106 ? -14.632 11.075 24.098 1.00 17.49 ? 114 ARG A CD 1 ATOM 1463 N NE . ARG A 1 106 ? -15.442 10.684 22.942 1.00 17.05 ? 114 ARG A NE 1 ATOM 1464 C CZ . ARG A 1 106 ? -15.984 11.544 22.091 1.00 17.87 ? 114 ARG A CZ 1 ATOM 1465 N NH1 . ARG A 1 106 ? -15.845 12.857 22.287 1.00 17.11 ? 114 ARG A NH1 1 ATOM 1466 N NH2 . ARG A 1 106 ? -16.646 11.086 21.048 1.00 17.43 ? 114 ARG A NH2 1 ATOM 1467 H H . ARG A 1 106 ? -12.034 10.151 28.086 1.00 16.85 ? 114 ARG A H 1 ATOM 1468 H HA . ARG A 1 106 ? -13.014 8.318 26.510 1.00 17.53 ? 114 ARG A HA 1 ATOM 1469 H HB2 . ARG A 1 106 ? -13.774 10.579 26.578 1.00 18.72 ? 114 ARG A HB2 1 ATOM 1470 H HB3 . ARG A 1 106 ? -12.504 10.964 25.700 1.00 18.72 ? 114 ARG A HB3 1 ATOM 1471 H HG2 . ARG A 1 106 ? -13.289 9.599 23.971 1.00 20.25 ? 114 ARG A HG2 1 ATOM 1472 H HG3 . ARG A 1 106 ? -14.561 9.223 24.848 1.00 20.25 ? 114 ARG A HG3 1 ATOM 1473 H HD2 . ARG A 1 106 ? -15.222 11.438 24.778 1.00 20.99 ? 114 ARG A HD2 1 ATOM 1474 H HD3 . ARG A 1 106 ? -13.992 11.745 23.812 1.00 20.99 ? 114 ARG A HD3 1 ATOM 1475 H HE . ARG A 1 106 ? -15.531 9.845 22.778 1.00 20.46 ? 114 ARG A HE 1 ATOM 1476 H HH11 . ARG A 1 106 ? -15.396 13.146 22.962 1.00 20.53 ? 114 ARG A HH11 1 ATOM 1477 H HH12 . ARG A 1 106 ? -16.203 13.414 21.738 1.00 20.53 ? 114 ARG A HH12 1 ATOM 1478 H HH21 . ARG A 1 106 ? -16.740 10.238 20.936 1.00 20.91 ? 114 ARG A HH21 1 ATOM 1479 H HH22 . ARG A 1 106 ? -17.022 11.635 20.503 1.00 20.91 ? 114 ARG A HH22 1 ATOM 1480 N N . LEU A 1 107 ? -10.106 9.379 25.618 1.00 12.97 ? 115 LEU A N 1 ATOM 1481 C CA A LEU A 1 107 ? -8.971 9.024 24.774 0.59 13.23 ? 115 LEU A CA 1 ATOM 1482 C CA B LEU A 1 107 ? -8.968 9.023 24.779 0.41 13.42 ? 115 LEU A CA 1 ATOM 1483 C C . LEU A 1 107 ? -8.384 7.681 25.189 1.00 13.36 ? 115 LEU A C 1 ATOM 1484 O O . LEU A 1 107 ? -8.022 6.869 24.331 1.00 13.66 ? 115 LEU A O 1 ATOM 1485 C CB A LEU A 1 107 ? -7.925 10.145 24.751 0.59 13.36 ? 115 LEU A CB 1 ATOM 1486 C CB B LEU A 1 107 ? -7.895 10.109 24.839 0.41 14.19 ? 115 LEU A CB 1 ATOM 1487 C CG A LEU A 1 107 ? -8.162 11.255 23.706 0.59 13.05 ? 115 LEU A CG 1 ATOM 1488 C CG B LEU A 1 107 ? -8.261 11.469 24.242 0.41 15.91 ? 115 LEU A CG 1 ATOM 1489 C CD1 A LEU A 1 107 ? -9.327 12.133 24.090 0.59 14.62 ? 115 LEU A CD1 1 ATOM 1490 C CD1 B LEU A 1 107 ? -7.053 12.371 24.229 0.41 17.58 ? 115 LEU A CD1 1 ATOM 1491 C CD2 A LEU A 1 107 ? -6.915 12.111 23.510 0.59 15.72 ? 115 LEU A CD2 1 ATOM 1492 C CD2 B LEU A 1 107 ? -8.776 11.330 22.847 0.41 17.36 ? 115 LEU A CD2 1 ATOM 1493 H H . LEU A 1 107 ? -9.973 10.055 26.132 1.00 15.56 ? 115 LEU A H 1 ATOM 1494 H HA . LEU A 1 107 ? -9.281 8.935 23.862 1.00 16.11 ? 115 LEU A HA 1 ATOM 1495 H HB2 A LEU A 1 107 ? -7.909 10.567 25.625 0.59 16.04 ? 115 LEU A HB2 1 ATOM 1496 H HB2 B LEU A 1 107 ? -7.666 10.257 25.770 0.41 17.03 ? 115 LEU A HB2 1 ATOM 1497 H HB3 A LEU A 1 107 ? -7.058 9.752 24.566 0.59 16.04 ? 115 LEU A HB3 1 ATOM 1498 H HB3 B LEU A 1 107 ? -7.113 9.788 24.363 0.41 17.03 ? 115 LEU A HB3 1 ATOM 1499 H HG A LEU A 1 107 ? -8.373 10.840 22.854 0.59 15.66 ? 115 LEU A HG 1 ATOM 1500 H HG B LEU A 1 107 ? -8.949 11.885 24.784 0.41 19.09 ? 115 LEU A HG 1 ATOM 1501 H HD11 A LEU A 1 107 ? -9.445 12.816 23.411 0.59 17.55 ? 115 LEU A HD11 1 ATOM 1502 H HD11 B LEU A 1 107 ? -7.303 13.227 23.848 0.41 21.10 ? 115 LEU A HD11 1 ATOM 1503 H HD12 A LEU A 1 107 ? -10.127 11.586 24.153 0.59 17.55 ? 115 LEU A HD12 1 ATOM 1504 H HD12 B LEU A 1 107 ? -6.740 12.492 25.139 0.41 21.10 ? 115 LEU A HD12 1 ATOM 1505 H HD13 A LEU A 1 107 ? -9.141 12.546 24.947 0.59 17.55 ? 115 LEU A HD13 1 ATOM 1506 H HD13 B LEU A 1 107 ? -6.358 11.960 23.692 0.41 21.10 ? 115 LEU A HD13 1 ATOM 1507 H HD21 A LEU A 1 107 ? -7.103 12.794 22.848 0.59 18.87 ? 115 LEU A HD21 1 ATOM 1508 H HD21 B LEU A 1 107 ? -8.996 12.210 22.502 0.41 20.83 ? 115 LEU A HD21 1 ATOM 1509 H HD22 A LEU A 1 107 ? -6.681 12.524 24.356 0.59 18.87 ? 115 LEU A HD22 1 ATOM 1510 H HD22 B LEU A 1 107 ? -8.089 10.921 22.296 0.41 20.83 ? 115 LEU A HD22 1 ATOM 1511 H HD23 A LEU A 1 107 ? -6.189 11.545 23.205 0.59 18.87 ? 115 LEU A HD23 1 ATOM 1512 H HD23 B LEU A 1 107 ? -9.568 10.770 22.857 0.41 20.83 ? 115 LEU A HD23 1 ATOM 1513 N N . THR A 1 108 ? -8.267 7.442 26.496 1.00 13.47 ? 116 THR A N 1 ATOM 1514 C CA . THR A 1 108 ? -7.787 6.153 26.990 1.00 14.35 ? 116 THR A CA 1 ATOM 1515 C C . THR A 1 108 ? -8.646 5.015 26.443 1.00 13.70 ? 116 THR A C 1 ATOM 1516 O O . THR A 1 108 ? -8.133 3.991 25.973 1.00 13.73 ? 116 THR A O 1 ATOM 1517 C CB . THR A 1 108 ? -7.814 6.154 28.527 1.00 14.50 ? 116 THR A CB 1 ATOM 1518 O OG1 . THR A 1 108 ? -6.917 7.160 29.025 1.00 13.35 ? 116 THR A OG1 1 ATOM 1519 C CG2 . THR A 1 108 ? -7.392 4.820 29.097 1.00 15.53 ? 116 THR A CG2 1 ATOM 1520 H H . THR A 1 108 ? -8.458 8.008 27.114 1.00 16.16 ? 116 THR A H 1 ATOM 1521 H HA . THR A 1 108 ? -6.872 6.015 26.698 1.00 17.22 ? 116 THR A HA 1 ATOM 1522 H HB . THR A 1 108 ? -8.714 6.345 28.833 1.00 17.40 ? 116 THR A HB 1 ATOM 1523 H HG1 . THR A 1 108 ? -7.151 7.917 28.746 1.00 16.02 ? 116 THR A HG1 1 ATOM 1524 H HG21 . THR A 1 108 ? -7.418 4.850 30.066 1.00 18.64 ? 116 THR A HG21 1 ATOM 1525 H HG22 . THR A 1 108 ? -7.991 4.123 28.787 1.00 18.64 ? 116 THR A HG22 1 ATOM 1526 H HG23 . THR A 1 108 ? -6.489 4.609 28.812 1.00 18.64 ? 116 THR A HG23 1 ATOM 1527 N N . ASN A 1 109 ? -9.970 5.174 26.516 1.00 13.59 ? 117 ASN A N 1 ATOM 1528 C CA . ASN A 1 109 ? -10.885 4.145 26.040 1.00 13.87 ? 117 ASN A CA 1 ATOM 1529 C C . ASN A 1 109 ? -10.750 3.912 24.540 1.00 14.19 ? 117 ASN A C 1 ATOM 1530 O O . ASN A 1 109 ? -10.829 2.768 24.078 1.00 15.44 ? 117 ASN A O 1 ATOM 1531 C CB . ASN A 1 109 ? -12.321 4.518 26.385 1.00 15.15 ? 117 ASN A CB 1 ATOM 1532 C CG . ASN A 1 109 ? -12.636 4.281 27.827 1.00 16.47 ? 117 ASN A CG 1 ATOM 1533 O OD1 . ASN A 1 109 ? -11.914 3.551 28.506 1.00 19.10 ? 117 ASN A OD1 1 ATOM 1534 N ND2 . ASN A 1 109 ? -13.721 4.882 28.305 1.00 18.87 ? 117 ASN A ND2 1 ATOM 1535 H H . ASN A 1 109 ? -10.360 5.871 26.838 1.00 16.31 ? 117 ASN A H 1 ATOM 1536 H HA . ASN A 1 109 ? -10.679 3.311 26.490 1.00 16.64 ? 117 ASN A HA 1 ATOM 1537 H HB2 . ASN A 1 109 ? -12.459 5.459 26.197 1.00 18.18 ? 117 ASN A HB2 1 ATOM 1538 H HB3 . ASN A 1 109 ? -12.926 3.979 25.852 1.00 18.18 ? 117 ASN A HB3 1 ATOM 1539 H HD21 . ASN A 1 109 ? -13.944 4.776 29.129 1.00 22.64 ? 117 ASN A HD21 1 ATOM 1540 H HD22 . ASN A 1 109 ? -14.200 5.376 27.790 1.00 22.64 ? 117 ASN A HD22 1 ATOM 1541 N N . LEU A 1 110 ? -10.519 4.966 23.759 1.00 13.95 ? 118 LEU A N 1 ATOM 1542 C CA . LEU A 1 110 ? -10.301 4.775 22.329 1.00 14.00 ? 118 LEU A CA 1 ATOM 1543 C C . LEU A 1 110 ? -9.059 3.937 22.076 1.00 13.68 ? 118 LEU A C 1 ATOM 1544 O O . LEU A 1 110 ? -9.070 3.017 21.259 1.00 14.07 ? 118 LEU A O 1 ATOM 1545 C CB . LEU A 1 110 ? -10.181 6.129 21.647 1.00 14.10 ? 118 LEU A CB 1 ATOM 1546 C CG . LEU A 1 110 ? -9.873 6.076 20.152 1.00 14.92 ? 118 LEU A CG 1 ATOM 1547 C CD1 . LEU A 1 110 ? -11.037 5.484 19.347 1.00 16.65 ? 118 LEU A CD1 1 ATOM 1548 C CD2 . LEU A 1 110 ? -9.523 7.472 19.635 1.00 16.07 ? 118 LEU A CD2 1 ATOM 1549 H H . LEU A 1 110 ? -10.484 5.783 24.026 1.00 16.74 ? 118 LEU A H 1 ATOM 1550 H HA . LEU A 1 110 ? -11.063 4.311 21.949 1.00 16.81 ? 118 LEU A HA 1 ATOM 1551 H HB2 . LEU A 1 110 ? -11.019 6.604 21.756 1.00 16.92 ? 118 LEU A HB2 1 ATOM 1552 H HB3 . LEU A 1 110 ? -9.467 6.627 22.075 1.00 16.92 ? 118 LEU A HB3 1 ATOM 1553 H HG . LEU A 1 110 ? -9.099 5.507 20.014 1.00 17.91 ? 118 LEU A HG 1 ATOM 1554 H HD11 . LEU A 1 110 ? -10.796 5.471 18.408 1.00 19.98 ? 118 LEU A HD11 1 ATOM 1555 H HD12 . LEU A 1 110 ? -11.209 4.582 19.658 1.00 19.98 ? 118 LEU A HD12 1 ATOM 1556 H HD13 . LEU A 1 110 ? -11.824 6.035 19.479 1.00 19.98 ? 118 LEU A HD13 1 ATOM 1557 H HD21 . LEU A 1 110 ? -9.331 7.417 18.686 1.00 19.28 ? 118 LEU A HD21 1 ATOM 1558 H HD22 . LEU A 1 110 ? -10.277 8.062 19.787 1.00 19.28 ? 118 LEU A HD22 1 ATOM 1559 H HD23 . LEU A 1 110 ? -8.745 7.799 20.112 1.00 19.28 ? 118 LEU A HD23 1 ATOM 1560 N N . ILE A 1 111 ? -7.957 4.247 22.758 1.00 13.01 ? 119 ILE A N 1 ATOM 1561 C CA . ILE A 1 111 ? -6.733 3.470 22.567 1.00 13.48 ? 119 ILE A CA 1 ATOM 1562 C C . ILE A 1 111 ? -6.962 2.015 22.956 1.00 14.37 ? 119 ILE A C 1 ATOM 1563 O O . ILE A 1 111 ? -6.537 1.094 22.250 1.00 15.21 ? 119 ILE A O 1 ATOM 1564 C CB . ILE A 1 111 ? -5.581 4.094 23.367 1.00 13.84 ? 119 ILE A CB 1 ATOM 1565 C CG1 . ILE A 1 111 ? -5.253 5.475 22.807 1.00 14.54 ? 119 ILE A CG1 1 ATOM 1566 C CG2 . ILE A 1 111 ? -4.365 3.191 23.325 1.00 15.78 ? 119 ILE A CG2 1 ATOM 1567 C CD1 . ILE A 1 111 ? -4.344 6.324 23.692 1.00 15.31 ? 119 ILE A CD1 1 ATOM 1568 H H . ILE A 1 111 ? -7.891 4.889 23.326 1.00 15.61 ? 119 ILE A H 1 ATOM 1569 H HA . ILE A 1 111 ? -6.490 3.493 21.629 1.00 16.18 ? 119 ILE A HA 1 ATOM 1570 H HB . ILE A 1 111 ? -5.862 4.193 24.290 1.00 16.61 ? 119 ILE A HB 1 ATOM 1571 H HG12 . ILE A 1 111 ? -4.810 5.365 21.951 1.00 17.45 ? 119 ILE A HG12 1 ATOM 1572 H HG13 . ILE A 1 111 ? -6.082 5.964 22.683 1.00 17.45 ? 119 ILE A HG13 1 ATOM 1573 H HG21 . ILE A 1 111 ? -3.649 3.601 23.835 1.00 18.93 ? 119 ILE A HG21 1 ATOM 1574 H HG22 . ILE A 1 111 ? -4.597 2.332 23.712 1.00 18.93 ? 119 ILE A HG22 1 ATOM 1575 H HG23 . ILE A 1 111 ? -4.090 3.075 22.403 1.00 18.93 ? 119 ILE A HG23 1 ATOM 1576 H HD11 . ILE A 1 111 ? -4.191 7.178 23.259 1.00 18.38 ? 119 ILE A HD11 1 ATOM 1577 H HD12 . ILE A 1 111 ? -4.776 6.460 24.549 1.00 18.38 ? 119 ILE A HD12 1 ATOM 1578 H HD13 . ILE A 1 111 ? -3.501 5.859 23.815 1.00 18.38 ? 119 ILE A HD13 1 ATOM 1579 N N . LYS A 1 112 ? -7.655 1.783 24.081 1.00 14.53 ? 120 LYS A N 1 ATOM 1580 C CA . LYS A 1 112 ? -7.959 0.432 24.537 1.00 16.05 ? 120 LYS A CA 1 ATOM 1581 C C . LYS A 1 112 ? -8.840 -0.308 23.544 1.00 16.91 ? 120 LYS A C 1 ATOM 1582 O O . LYS A 1 112 ? -8.706 -1.523 23.376 1.00 19.16 ? 120 LYS A O 1 ATOM 1583 C CB . LYS A 1 112 ? -8.663 0.510 25.899 1.00 16.66 ? 120 LYS A CB 1 ATOM 1584 C CG . LYS A 1 112 ? -7.761 0.906 27.073 1.00 16.59 ? 120 LYS A CG 1 ATOM 1585 C CD . LYS A 1 112 ? -8.570 1.002 28.370 1.00 18.31 ? 120 LYS A CD 1 ATOM 1586 C CE . LYS A 1 112 ? -7.716 1.332 29.577 1.00 19.51 ? 120 LYS A CE 1 ATOM 1587 N NZ . LYS A 1 112 ? -8.529 1.528 30.819 1.00 20.84 ? 120 LYS A NZ 1 ATOM 1588 H H . LYS A 1 112 ? -7.959 2.400 24.597 1.00 17.43 ? 120 LYS A H 1 ATOM 1589 H HA . LYS A 1 112 ? -7.133 -0.066 24.646 1.00 19.26 ? 120 LYS A HA 1 ATOM 1590 H HB2 . LYS A 1 112 ? -9.374 1.168 25.842 1.00 19.99 ? 120 LYS A HB2 1 ATOM 1591 H HB3 . LYS A 1 112 ? -9.041 -0.360 26.101 1.00 19.99 ? 120 LYS A HB3 1 ATOM 1592 H HG2 . LYS A 1 112 ? -7.071 0.234 27.190 1.00 19.90 ? 120 LYS A HG2 1 ATOM 1593 H HG3 . LYS A 1 112 ? -7.362 1.772 26.895 1.00 19.90 ? 120 LYS A HG3 1 ATOM 1594 H HD2 . LYS A 1 112 ? -9.236 1.700 28.275 1.00 21.97 ? 120 LYS A HD2 1 ATOM 1595 H HD3 . LYS A 1 112 ? -9.004 0.150 28.534 1.00 21.97 ? 120 LYS A HD3 1 ATOM 1596 H HE2 . LYS A 1 112 ? -7.096 0.603 29.735 1.00 23.41 ? 120 LYS A HE2 1 ATOM 1597 H HE3 . LYS A 1 112 ? -7.228 2.152 29.405 1.00 23.41 ? 120 LYS A HE3 1 ATOM 1598 H HZ1 . LYS A 1 112 ? -7.995 1.720 31.504 1.00 25.01 ? 120 LYS A HZ1 1 ATOM 1599 H HZ2 . LYS A 1 112 ? -9.103 2.198 30.703 1.00 25.01 ? 120 LYS A HZ2 1 ATOM 1600 H HZ3 . LYS A 1 112 ? -8.984 0.786 31.005 1.00 25.01 ? 120 LYS A HZ3 1 ATOM 1601 N N . GLU A 1 113 ? -9.763 0.409 22.901 1.00 16.16 ? 121 GLU A N 1 ATOM 1602 C CA . GLU A 1 113 ? -10.667 -0.198 21.932 1.00 18.14 ? 121 GLU A CA 1 ATOM 1603 C C . GLU A 1 113 ? -9.928 -0.598 20.660 1.00 17.50 ? 121 GLU A C 1 ATOM 1604 O O . GLU A 1 113 ? -10.152 -1.683 20.114 1.00 19.93 ? 121 GLU A O 1 ATOM 1605 C CB . GLU A 1 113 ? -11.771 0.798 21.592 1.00 19.72 ? 121 GLU A CB 1 ATOM 1606 C CG . GLU A 1 113 ? -12.725 0.298 20.536 1.00 26.59 ? 121 GLU A CG 1 ATOM 1607 C CD . GLU A 1 113 ? -13.854 1.271 20.223 1.00 33.81 ? 121 GLU A CD 1 ATOM 1608 O OE1 . GLU A 1 113 ? -13.935 2.340 20.868 1.00 35.92 ? 121 GLU A OE1 1 ATOM 1609 O OE2 . GLU A 1 113 ? -14.674 0.954 19.333 1.00 37.21 ? 121 GLU A OE2 1 ATOM 1610 H H . GLU A 1 113 ? -9.884 1.254 23.011 1.00 19.40 ? 121 GLU A H 1 ATOM 1611 H HA . GLU A 1 113 ? -11.072 -0.991 22.317 1.00 21.77 ? 121 GLU A HA 1 ATOM 1612 H HB2 . GLU A 1 113 ? -12.285 0.983 22.393 1.00 23.67 ? 121 GLU A HB2 1 ATOM 1613 H HB3 . GLU A 1 113 ? -11.366 1.616 21.264 1.00 23.67 ? 121 GLU A HB3 1 ATOM 1614 H HG2 . GLU A 1 113 ? -12.230 0.143 19.716 1.00 31.91 ? 121 GLU A HG2 1 ATOM 1615 H HG3 . GLU A 1 113 ? -13.124 -0.532 20.842 1.00 31.91 ? 121 GLU A HG3 1 ATOM 1616 N N . VAL A 1 114 ? -9.044 0.267 20.171 1.00 16.18 ? 122 VAL A N 1 ATOM 1617 C CA . VAL A 1 114 ? -8.393 0.017 18.894 1.00 15.91 ? 122 VAL A CA 1 ATOM 1618 C C . VAL A 1 114 ? -7.210 -0.922 19.061 1.00 16.36 ? 122 VAL A C 1 ATOM 1619 O O . VAL A 1 114 ? -6.891 -1.687 18.144 1.00 17.08 ? 122 VAL A O 1 ATOM 1620 C CB . VAL A 1 114 ? -7.996 1.364 18.266 1.00 16.23 ? 122 VAL A CB 1 ATOM 1621 C CG1 . VAL A 1 114 ? -7.229 1.155 16.979 1.00 18.55 ? 122 VAL A CG1 1 ATOM 1622 C CG2 . VAL A 1 114 ? -9.239 2.226 18.022 1.00 16.85 ? 122 VAL A CG2 1 ATOM 1623 H H . VAL A 1 114 ? -8.807 0.999 20.556 1.00 19.42 ? 122 VAL A H 1 ATOM 1624 H HA . VAL A 1 114 ? -9.028 -0.411 18.299 1.00 19.09 ? 122 VAL A HA 1 ATOM 1625 H HB . VAL A 1 114 ? -7.418 1.840 18.883 1.00 19.48 ? 122 VAL A HB 1 ATOM 1626 H HG11 . VAL A 1 114 ? -6.994 2.020 16.608 1.00 22.26 ? 122 VAL A HG11 1 ATOM 1627 H HG12 . VAL A 1 114 ? -6.426 0.646 17.169 1.00 22.26 ? 122 VAL A HG12 1 ATOM 1628 H HG13 . VAL A 1 114 ? -7.789 0.669 16.354 1.00 22.26 ? 122 VAL A HG13 1 ATOM 1629 H HG21 . VAL A 1 114 ? -8.966 3.068 17.627 1.00 20.22 ? 122 VAL A HG21 1 ATOM 1630 H HG22 . VAL A 1 114 ? -9.836 1.755 17.419 1.00 20.22 ? 122 VAL A HG22 1 ATOM 1631 H HG23 . VAL A 1 114 ? -9.683 2.386 18.870 1.00 20.22 ? 122 VAL A HG23 1 ATOM 1632 N N . PHE A 1 115 ? -6.537 -0.872 20.214 1.00 15.14 ? 123 PHE A N 1 ATOM 1633 C CA . PHE A 1 115 ? -5.383 -1.716 20.525 1.00 16.58 ? 123 PHE A CA 1 ATOM 1634 C C . PHE A 1 115 ? -5.630 -2.475 21.828 1.00 17.60 ? 123 PHE A C 1 ATOM 1635 O O . PHE A 1 115 ? -4.928 -2.269 22.825 1.00 17.35 ? 123 PHE A O 1 ATOM 1636 C CB . PHE A 1 115 ? -4.130 -0.848 20.624 1.00 15.41 ? 123 PHE A CB 1 ATOM 1637 C CG . PHE A 1 115 ? -3.663 -0.289 19.307 1.00 15.36 ? 123 PHE A CG 1 ATOM 1638 C CD1 . PHE A 1 115 ? -2.847 -1.040 18.485 1.00 15.03 ? 123 PHE A CD1 1 ATOM 1639 C CD2 . PHE A 1 115 ? -4.031 0.986 18.899 1.00 15.78 ? 123 PHE A CD2 1 ATOM 1640 C CE1 . PHE A 1 115 ? -2.444 -0.544 17.259 1.00 14.51 ? 123 PHE A CE1 1 ATOM 1641 C CE2 . PHE A 1 115 ? -3.620 1.484 17.680 1.00 15.40 ? 123 PHE A CE2 1 ATOM 1642 C CZ . PHE A 1 115 ? -2.825 0.726 16.861 1.00 15.41 ? 123 PHE A CZ 1 ATOM 1643 H H . PHE A 1 115 ? -6.740 -0.335 20.855 1.00 18.17 ? 123 PHE A H 1 ATOM 1644 H HA . PHE A 1 115 ? -5.254 -2.362 19.813 1.00 19.89 ? 123 PHE A HA 1 ATOM 1645 H HB2 . PHE A 1 115 ? -4.316 -0.100 21.213 1.00 18.50 ? 123 PHE A HB2 1 ATOM 1646 H HB3 . PHE A 1 115 ? -3.409 -1.383 20.991 1.00 18.50 ? 123 PHE A HB3 1 ATOM 1647 H HD1 . PHE A 1 115 ? -2.599 -1.899 18.741 1.00 18.04 ? 123 PHE A HD1 1 ATOM 1648 H HD2 . PHE A 1 115 ? -4.581 1.501 19.443 1.00 18.94 ? 123 PHE A HD2 1 ATOM 1649 H HE1 . PHE A 1 115 ? -1.897 -1.057 16.710 1.00 17.41 ? 123 PHE A HE1 1 ATOM 1650 H HE2 . PHE A 1 115 ? -3.877 2.338 17.416 1.00 18.48 ? 123 PHE A HE2 1 ATOM 1651 H HZ . PHE A 1 115 ? -2.538 1.066 16.044 1.00 18.49 ? 123 PHE A HZ 1 ATOM 1652 N N . PRO A 1 116 ? -6.578 -3.418 21.828 1.00 18.82 ? 124 PRO A N 1 ATOM 1653 C CA . PRO A 1 116 ? -6.992 -4.052 23.091 1.00 19.95 ? 124 PRO A CA 1 ATOM 1654 C C . PRO A 1 116 ? -5.941 -4.935 23.727 1.00 21.65 ? 124 PRO A C 1 ATOM 1655 O O . PRO A 1 116 ? -6.027 -5.199 24.932 1.00 25.12 ? 124 PRO A O 1 ATOM 1656 C CB . PRO A 1 116 ? -8.227 -4.864 22.694 1.00 21.12 ? 124 PRO A CB 1 ATOM 1657 C CG . PRO A 1 116 ? -8.058 -5.121 21.266 1.00 21.04 ? 124 PRO A CG 1 ATOM 1658 C CD . PRO A 1 116 ? -7.402 -3.874 20.699 1.00 20.14 ? 124 PRO A CD 1 ATOM 1659 H HA . PRO A 1 116 ? -7.256 -3.372 23.729 1.00 23.94 ? 124 PRO A HA 1 ATOM 1660 H HB2 . PRO A 1 116 ? -8.248 -5.696 23.193 1.00 25.34 ? 124 PRO A HB2 1 ATOM 1661 H HB3 . PRO A 1 116 ? -9.029 -4.343 22.857 1.00 25.34 ? 124 PRO A HB3 1 ATOM 1662 H HG2 . PRO A 1 116 ? -7.486 -5.894 21.140 1.00 25.25 ? 124 PRO A HG2 1 ATOM 1663 H HG3 . PRO A 1 116 ? -8.925 -5.267 20.856 1.00 25.25 ? 124 PRO A HG3 1 ATOM 1664 H HD2 . PRO A 1 116 ? -6.845 -4.097 19.937 1.00 24.16 ? 124 PRO A HD2 1 ATOM 1665 H HD3 . PRO A 1 116 ? -8.071 -3.209 20.473 1.00 24.16 ? 124 PRO A HD3 1 ATOM 1666 N N . ASP A 1 117 ? -4.966 -5.421 22.970 1.00 20.81 ? 125 ASP A N 1 ATOM 1667 C CA . ASP A 1 117 ? -3.985 -6.352 23.508 1.00 22.45 ? 125 ASP A CA 1 ATOM 1668 C C . ASP A 1 117 ? -2.609 -5.721 23.661 1.00 21.68 ? 125 ASP A C 1 ATOM 1669 O O . ASP A 1 117 ? -1.628 -6.439 23.873 1.00 23.75 ? 125 ASP A O 1 ATOM 1670 C CB . ASP A 1 117 ? -3.902 -7.573 22.599 1.00 25.67 ? 125 ASP A CB 1 ATOM 1671 C CG . ASP A 1 117 ? -5.260 -8.189 22.332 1.00 31.32 ? 125 ASP A CG 1 ATOM 1672 O OD1 . ASP A 1 117 ? -6.043 -8.351 23.286 1.00 31.79 ? 125 ASP A OD1 1 ATOM 1673 O OD2 . ASP A 1 117 ? -5.543 -8.488 21.157 1.00 34.80 ? 125 ASP A OD2 1 ATOM 1674 H H . ASP A 1 117 ? -4.849 -5.226 22.141 1.00 24.98 ? 125 ASP A H 1 ATOM 1675 H HA . ASP A 1 117 ? -4.278 -6.649 24.384 1.00 26.94 ? 125 ASP A HA 1 ATOM 1676 H HB2 . ASP A 1 117 ? -3.519 -7.308 21.748 1.00 30.80 ? 125 ASP A HB2 1 ATOM 1677 H HB3 . ASP A 1 117 ? -3.344 -8.245 23.020 1.00 30.80 ? 125 ASP A HB3 1 ATOM 1678 N N . THR A 1 118 ? -2.513 -4.405 23.558 1.00 18.94 ? 126 THR A N 1 ATOM 1679 C CA . THR A 1 118 ? -1.234 -3.722 23.451 1.00 17.44 ? 126 THR A CA 1 ATOM 1680 C C . THR A 1 118 ? -0.892 -3.016 24.758 1.00 18.16 ? 126 THR A C 1 ATOM 1681 O O . THR A 1 118 ? -1.717 -2.274 25.309 1.00 21.08 ? 126 THR A O 1 ATOM 1682 C CB . THR A 1 118 ? -1.273 -2.711 22.311 1.00 15.87 ? 126 THR A CB 1 ATOM 1683 O OG1 . THR A 1 118 ? -1.651 -3.365 21.094 1.00 16.84 ? 126 THR A OG1 1 ATOM 1684 C CG2 . THR A 1 118 ? 0.057 -2.032 22.120 1.00 16.59 ? 126 THR A CG2 1 ATOM 1685 H H . THR A 1 118 ? -3.189 -3.874 23.548 1.00 22.73 ? 126 THR A H 1 ATOM 1686 H HA . THR A 1 118 ? -0.538 -4.370 23.262 1.00 20.93 ? 126 THR A HA 1 ATOM 1687 H HB . THR A 1 118 ? -1.930 -2.028 22.519 1.00 19.04 ? 126 THR A HB 1 ATOM 1688 H HG1 . THR A 1 118 ? -1.095 -3.967 20.907 1.00 20.21 ? 126 THR A HG1 1 ATOM 1689 H HG21 . THR A 1 118 ? 0.002 -1.396 21.390 1.00 19.91 ? 126 THR A HG21 1 ATOM 1690 H HG22 . THR A 1 118 ? 0.308 -1.562 22.931 1.00 19.91 ? 126 THR A HG22 1 ATOM 1691 H HG23 . THR A 1 118 ? 0.738 -2.691 21.914 1.00 19.91 ? 126 THR A HG23 1 ATOM 1692 N N . LYS A 1 119 ? 0.334 -3.202 25.226 1.00 18.03 ? 127 LYS A N 1 ATOM 1693 C CA . LYS A 1 119 ? 0.803 -2.427 26.356 1.00 19.44 ? 127 LYS A CA 1 ATOM 1694 C C . LYS A 1 119 ? 1.009 -0.980 25.941 1.00 16.43 ? 127 LYS A C 1 ATOM 1695 O O . LYS A 1 119 ? 1.605 -0.687 24.897 1.00 15.81 ? 127 LYS A O 1 ATOM 1696 C CB . LYS A 1 119 ? 2.121 -2.978 26.877 1.00 25.40 ? 127 LYS A CB 1 ATOM 1697 C CG . LYS A 1 119 ? 2.509 -2.341 28.160 1.00 28.74 ? 127 LYS A CG 1 ATOM 1698 C CD . LYS A 1 119 ? 2.583 -3.307 29.295 1.00 32.12 ? 127 LYS A CD 1 ATOM 1699 C CE . LYS A 1 119 ? 2.845 -2.532 30.576 1.00 34.12 ? 127 LYS A CE 1 ATOM 1700 N NZ . LYS A 1 119 ? 2.803 -3.366 31.799 1.00 37.25 ? 127 LYS A NZ 1 ATOM 1701 H H . LYS A 1 119 ? 0.904 -3.764 24.911 1.00 21.64 ? 127 LYS A H 1 ATOM 1702 H HA . LYS A 1 119 ? 0.148 -2.457 27.071 1.00 23.33 ? 127 LYS A HA 1 ATOM 1703 H HB2 . LYS A 1 119 ? 2.032 -3.932 27.027 1.00 30.47 ? 127 LYS A HB2 1 ATOM 1704 H HB3 . LYS A 1 119 ? 2.821 -2.804 26.228 1.00 30.47 ? 127 LYS A HB3 1 ATOM 1705 H HG2 . LYS A 1 119 ? 3.382 -1.933 28.057 1.00 34.48 ? 127 LYS A HG2 1 ATOM 1706 H HG3 . LYS A 1 119 ? 1.852 -1.664 28.386 1.00 34.48 ? 127 LYS A HG3 1 ATOM 1707 H HD2 . LYS A 1 119 ? 1.740 -3.779 29.382 1.00 38.55 ? 127 LYS A HD2 1 ATOM 1708 H HD3 . LYS A 1 119 ? 3.313 -3.929 29.151 1.00 38.55 ? 127 LYS A HD3 1 ATOM 1709 H HE2 . LYS A 1 119 ? 3.726 -2.129 30.523 1.00 40.95 ? 127 LYS A HE2 1 ATOM 1710 H HE3 . LYS A 1 119 ? 2.171 -1.840 30.666 1.00 40.95 ? 127 LYS A HE3 1 ATOM 1711 H HZ1 . LYS A 1 119 ? 2.963 -2.863 32.515 1.00 44.71 ? 127 LYS A HZ1 1 ATOM 1712 H HZ2 . LYS A 1 119 ? 2.001 -3.743 31.882 1.00 44.71 ? 127 LYS A HZ2 1 ATOM 1713 H HZ3 . LYS A 1 119 ? 3.420 -4.006 31.751 1.00 44.71 ? 127 LYS A HZ3 1 ATOM 1714 N N . VAL A 1 120 ? 0.537 -0.058 26.784 1.00 14.97 ? 128 VAL A N 1 ATOM 1715 C CA . VAL A 1 120 ? 0.703 1.368 26.560 1.00 13.40 ? 128 VAL A CA 1 ATOM 1716 C C . VAL A 1 120 ? 1.461 1.954 27.736 1.00 13.67 ? 128 VAL A C 1 ATOM 1717 O O . VAL A 1 120 ? 1.153 1.646 28.889 1.00 15.08 ? 128 VAL A O 1 ATOM 1718 C CB . VAL A 1 120 ? -0.676 2.047 26.409 1.00 14.83 ? 128 VAL A CB 1 ATOM 1719 C CG1 . VAL A 1 120 ? -0.513 3.550 26.168 1.00 15.57 ? 128 VAL A CG1 1 ATOM 1720 C CG2 . VAL A 1 120 ? -1.485 1.409 25.282 1.00 16.17 ? 128 VAL A CG2 1 ATOM 1721 H H . VAL A 1 120 ? 0.110 -0.244 27.507 1.00 17.96 ? 128 VAL A H 1 ATOM 1722 H HA . VAL A 1 120 ? 1.216 1.517 25.750 1.00 16.08 ? 128 VAL A HA 1 ATOM 1723 H HB . VAL A 1 120 ? -1.173 1.931 27.233 1.00 17.80 ? 128 VAL A HB 1 ATOM 1724 H HG11 . VAL A 1 120 ? -1.391 3.952 26.077 1.00 18.68 ? 128 VAL A HG11 1 ATOM 1725 H HG12 . VAL A 1 120 ? -0.047 3.942 26.923 1.00 18.68 ? 128 VAL A HG12 1 ATOM 1726 H HG13 . VAL A 1 120 ? -0.001 3.686 25.356 1.00 18.68 ? 128 VAL A HG13 1 ATOM 1727 H HG21 . VAL A 1 120 ? -2.342 1.858 25.216 1.00 19.40 ? 128 VAL A HG21 1 ATOM 1728 H HG22 . VAL A 1 120 ? -0.996 1.503 24.450 1.00 19.40 ? 128 VAL A HG22 1 ATOM 1729 H HG23 . VAL A 1 120 ? -1.619 0.469 25.483 1.00 19.40 ? 128 VAL A HG23 1 ATOM 1730 N N . TYR A 1 121 ? 2.416 2.812 27.440 1.00 12.44 ? 129 TYR A N 1 ATOM 1731 C CA . TYR A 1 121 ? 3.172 3.549 28.446 1.00 11.72 ? 129 TYR A CA 1 ATOM 1732 C C . TYR A 1 121 ? 2.782 5.010 28.271 1.00 11.79 ? 129 TYR A C 1 ATOM 1733 O O . TYR A 1 121 ? 3.127 5.641 27.272 1.00 12.40 ? 129 TYR A O 1 ATOM 1734 C CB . TYR A 1 121 ? 4.674 3.323 28.300 1.00 12.62 ? 129 TYR A CB 1 ATOM 1735 C CG . TYR A 1 121 ? 5.026 1.854 28.367 1.00 14.58 ? 129 TYR A CG 1 ATOM 1736 C CD1 . TYR A 1 121 ? 5.073 1.210 29.567 1.00 20.01 ? 129 TYR A CD1 1 ATOM 1737 C CD2 . TYR A 1 121 ? 5.281 1.102 27.231 1.00 15.25 ? 129 TYR A CD2 1 ATOM 1738 C CE1 . TYR A 1 121 ? 5.363 -0.125 29.636 1.00 22.09 ? 129 TYR A CE1 1 ATOM 1739 C CE2 . TYR A 1 121 ? 5.593 -0.238 27.297 1.00 16.77 ? 129 TYR A CE2 1 ATOM 1740 C CZ . TYR A 1 121 ? 5.622 -0.848 28.494 1.00 20.01 ? 129 TYR A CZ 1 ATOM 1741 O OH . TYR A 1 121 ? 5.900 -2.193 28.568 1.00 21.04 ? 129 TYR A OH 1 ATOM 1742 H H . TYR A 1 121 ? 2.656 2.995 26.635 1.00 14.93 ? 129 TYR A H 1 ATOM 1743 H HA . TYR A 1 121 ? 2.902 3.260 29.332 1.00 14.07 ? 129 TYR A HA 1 ATOM 1744 H HB2 . TYR A 1 121 ? 4.967 3.667 27.442 1.00 15.14 ? 129 TYR A HB2 1 ATOM 1745 H HB3 . TYR A 1 121 ? 5.137 3.779 29.020 1.00 15.14 ? 129 TYR A HB3 1 ATOM 1746 H HD1 . TYR A 1 121 ? 4.894 1.682 30.348 1.00 24.02 ? 129 TYR A HD1 1 ATOM 1747 H HD2 . TYR A 1 121 ? 5.257 1.518 26.400 1.00 18.30 ? 129 TYR A HD2 1 ATOM 1748 H HE1 . TYR A 1 121 ? 5.388 -0.548 30.464 1.00 26.51 ? 129 TYR A HE1 1 ATOM 1749 H HE2 . TYR A 1 121 ? 5.754 -0.721 26.520 1.00 20.13 ? 129 TYR A HE2 1 ATOM 1750 H HH . TYR A 1 121 ? 6.037 -2.501 27.799 1.00 25.24 ? 129 TYR A HH 1 ATOM 1751 N N . ALA A 1 122 ? 2.014 5.520 29.213 1.00 12.79 ? 130 ALA A N 1 ATOM 1752 C CA . ALA A 1 122 ? 1.391 6.824 29.113 1.00 11.82 ? 130 ALA A CA 1 ATOM 1753 C C . ALA A 1 122 ? 1.892 7.785 30.184 1.00 11.93 ? 130 ALA A C 1 ATOM 1754 O O . ALA A 1 122 ? 2.024 7.423 31.346 1.00 12.66 ? 130 ALA A O 1 ATOM 1755 C CB . ALA A 1 122 ? -0.126 6.680 29.259 1.00 13.09 ? 130 ALA A CB 1 ATOM 1756 H H . ALA A 1 122 ? 1.833 5.113 29.949 1.00 15.34 ? 130 ALA A H 1 ATOM 1757 H HA . ALA A 1 122 ? 1.581 7.208 28.243 1.00 14.18 ? 130 ALA A HA 1 ATOM 1758 H HB1 . ALA A 1 122 ? -0.534 7.557 29.191 1.00 15.71 ? 130 ALA A HB1 1 ATOM 1759 H HB2 . ALA A 1 122 ? -0.457 6.105 28.552 1.00 15.71 ? 130 ALA A HB2 1 ATOM 1760 H HB3 . ALA A 1 122 ? -0.324 6.289 30.124 1.00 15.71 ? 130 ALA A HB3 1 ATOM 1761 N N . ALA A 1 123 ? 2.168 9.010 29.743 1.00 11.86 ? 131 ALA A N 1 ATOM 1762 C CA . ALA A 1 123 ? 2.554 10.126 30.574 1.00 12.23 ? 131 ALA A CA 1 ATOM 1763 C C . ALA A 1 123 ? 1.495 11.213 30.484 1.00 11.07 ? 131 ALA A C 1 ATOM 1764 O O . ALA A 1 123 ? 0.873 11.414 29.437 1.00 12.52 ? 131 ALA A O 1 ATOM 1765 C CB . ALA A 1 123 ? 3.886 10.716 30.105 1.00 12.48 ? 131 ALA A CB 1 ATOM 1766 H H . ALA A 1 123 ? 2.133 9.222 28.910 1.00 14.24 ? 131 ALA A H 1 ATOM 1767 H HA . ALA A 1 123 ? 2.639 9.841 31.497 1.00 14.67 ? 131 ALA A HA 1 ATOM 1768 H HB1 . ALA A 1 123 ? 4.121 11.462 30.679 1.00 14.98 ? 131 ALA A HB1 1 ATOM 1769 H HB2 . ALA A 1 123 ? 4.570 10.030 30.157 1.00 14.98 ? 131 ALA A HB2 1 ATOM 1770 H HB3 . ALA A 1 123 ? 3.792 11.019 29.188 1.00 14.98 ? 131 ALA A HB3 1 ATOM 1771 N N . LEU A 1 124 ? 1.311 11.952 31.573 1.00 11.44 ? 132 LEU A N 1 ATOM 1772 C CA . LEU A 1 124 ? 0.454 13.128 31.532 1.00 11.29 ? 132 LEU A CA 1 ATOM 1773 C C . LEU A 1 124 ? 1.180 14.318 30.915 1.00 11.75 ? 132 LEU A C 1 ATOM 1774 O O . LEU A 1 124 ? 2.392 14.494 31.083 1.00 11.43 ? 132 LEU A O 1 ATOM 1775 C CB . LEU A 1 124 ? -0.048 13.468 32.936 1.00 12.65 ? 132 LEU A CB 1 ATOM 1776 C CG . LEU A 1 124 ? -1.094 12.486 33.499 1.00 13.82 ? 132 LEU A CG 1 ATOM 1777 C CD1 . LEU A 1 124 ? -1.308 12.760 34.980 1.00 15.45 ? 132 LEU A CD1 1 ATOM 1778 C CD2 . LEU A 1 124 ? -2.400 12.649 32.755 1.00 14.42 ? 132 LEU A CD2 1 ATOM 1779 H H . LEU A 1 124 ? 1.667 11.796 32.340 1.00 13.73 ? 132 LEU A H 1 ATOM 1780 H HA . LEU A 1 124 ? -0.319 12.933 30.980 1.00 13.55 ? 132 LEU A HA 1 ATOM 1781 H HB2 . LEU A 1 124 ? 0.708 13.471 33.544 1.00 15.19 ? 132 LEU A HB2 1 ATOM 1782 H HB3 . LEU A 1 124 ? -0.453 14.349 32.916 1.00 15.19 ? 132 LEU A HB3 1 ATOM 1783 H HG . LEU A 1 124 ? -0.782 11.574 33.390 1.00 16.58 ? 132 LEU A HG 1 ATOM 1784 H HD11 . LEU A 1 124 ? -1.967 12.137 35.324 1.00 18.54 ? 132 LEU A HD11 1 ATOM 1785 H HD12 . LEU A 1 124 ? -0.466 12.642 35.448 1.00 18.54 ? 132 LEU A HD12 1 ATOM 1786 H HD13 . LEU A 1 124 ? -1.623 13.670 35.091 1.00 18.54 ? 132 LEU A HD13 1 ATOM 1787 H HD21 . LEU A 1 124 ? -3.049 12.026 33.118 1.00 17.30 ? 132 LEU A HD21 1 ATOM 1788 H HD22 . LEU A 1 124 ? -2.716 13.559 32.868 1.00 17.30 ? 132 LEU A HD22 1 ATOM 1789 H HD23 . LEU A 1 124 ? -2.253 12.463 31.815 1.00 17.30 ? 132 LEU A HD23 1 ATOM 1790 N N . GLY A 1 125 ? 0.427 15.115 30.169 1.00 11.76 ? 133 GLY A N 1 ATOM 1791 C CA . GLY A 1 125 ? 0.907 16.370 29.647 1.00 12.03 ? 133 GLY A CA 1 ATOM 1792 C C . GLY A 1 125 ? 0.419 17.550 30.468 1.00 11.02 ? 133 GLY A C 1 ATOM 1793 O O . GLY A 1 125 ? -0.449 17.420 31.316 1.00 11.33 ? 133 GLY A O 1 ATOM 1794 H H . GLY A 1 125 ? -0.386 14.940 29.950 1.00 14.11 ? 133 GLY A H 1 ATOM 1795 H HA2 . GLY A 1 125 ? 1.877 16.372 29.648 1.00 14.43 ? 133 GLY A HA2 1 ATOM 1796 H HA3 . GLY A 1 125 ? 0.600 16.480 28.733 1.00 14.43 ? 133 GLY A HA3 1 ATOM 1797 N N . ASN A 1 126 ? 0.971 18.728 30.162 1.00 10.88 ? 134 ASN A N 1 ATOM 1798 C CA . ASN A 1 126 ? 0.751 19.886 31.015 1.00 11.09 ? 134 ASN A CA 1 ATOM 1799 C C . ASN A 1 126 ? -0.695 20.368 30.999 1.00 10.98 ? 134 ASN A C 1 ATOM 1800 O O . ASN A 1 126 ? -1.137 20.999 31.975 1.00 12.36 ? 134 ASN A O 1 ATOM 1801 C CB . ASN A 1 126 ? 1.737 21.013 30.686 1.00 12.38 ? 134 ASN A CB 1 ATOM 1802 C CG . ASN A 1 126 ? 1.638 21.481 29.253 1.00 11.73 ? 134 ASN A CG 1 ATOM 1803 O OD1 . ASN A 1 126 ? 1.914 20.729 28.339 1.00 14.02 ? 134 ASN A OD1 1 ATOM 1804 N ND2 . ASN A 1 126 ? 1.255 22.736 29.044 1.00 12.46 ? 134 ASN A ND2 1 ATOM 1805 H H . ASN A 1 126 ? 1.468 18.876 29.477 1.00 13.05 ? 134 ASN A H 1 ATOM 1806 H HA . ASN A 1 126 ? 0.939 19.614 31.927 1.00 13.31 ? 134 ASN A HA 1 ATOM 1807 H HB2 . ASN A 1 126 ? 1.553 21.771 31.262 1.00 14.85 ? 134 ASN A HB2 1 ATOM 1808 H HB3 . ASN A 1 126 ? 2.641 20.694 30.835 1.00 14.85 ? 134 ASN A HB3 1 ATOM 1809 H HD21 . ASN A 1 126 ? 1.188 23.037 28.242 1.00 14.95 ? 134 ASN A HD21 1 ATOM 1810 H HD22 . ASN A 1 126 ? 1.075 23.247 29.712 1.00 14.95 ? 134 ASN A HD22 1 ATOM 1811 N N . HIS A 1 127 ? -1.429 20.079 29.935 1.00 11.70 ? 135 HIS A N 1 ATOM 1812 C CA . HIS A 1 127 ? -2.848 20.395 29.863 1.00 12.58 ? 135 HIS A CA 1 ATOM 1813 C C . HIS A 1 127 ? -3.745 19.349 30.492 1.00 12.81 ? 135 HIS A C 1 ATOM 1814 O O . HIS A 1 127 ? -4.967 19.578 30.589 1.00 14.30 ? 135 HIS A O 1 ATOM 1815 C CB . HIS A 1 127 ? -3.248 20.590 28.401 1.00 12.78 ? 135 HIS A CB 1 ATOM 1816 C CG . HIS A 1 127 ? -2.757 21.874 27.833 1.00 13.26 ? 135 HIS A CG 1 ATOM 1817 N ND1 . HIS A 1 127 ? -3.481 23.041 27.891 1.00 15.55 ? 135 HIS A ND1 1 ATOM 1818 C CD2 . HIS A 1 127 ? -1.576 22.188 27.261 1.00 13.06 ? 135 HIS A CD2 1 ATOM 1819 C CE1 . HIS A 1 127 ? -2.780 24.021 27.358 1.00 15.52 ? 135 HIS A CE1 1 ATOM 1820 N NE2 . HIS A 1 127 ? -1.609 23.535 26.982 1.00 14.18 ? 135 HIS A NE2 1 ATOM 1821 H H . HIS A 1 127 ? -1.124 19.692 29.230 1.00 14.04 ? 135 HIS A H 1 ATOM 1822 H HA . HIS A 1 127 ? -3.002 21.233 30.327 1.00 15.09 ? 135 HIS A HA 1 ATOM 1823 H HB2 . HIS A 1 127 ? -2.874 19.867 27.873 1.00 15.34 ? 135 HIS A HB2 1 ATOM 1824 H HB3 . HIS A 1 127 ? -4.215 20.584 28.335 1.00 15.34 ? 135 HIS A HB3 1 ATOM 1825 H HD1 . HIS A 1 127 ? -4.272 23.119 28.220 1.00 18.66 ? 135 HIS A HD1 1 ATOM 1826 H HD2 . HIS A 1 127 ? -0.867 21.607 27.100 1.00 15.67 ? 135 HIS A HD2 1 ATOM 1827 H HE1 . HIS A 1 127 ? -3.057 24.904 27.268 1.00 18.62 ? 135 HIS A HE1 1 ATOM 1828 N N . ASP A 1 128 ? -3.193 18.231 30.950 1.00 12.69 ? 136 ASP A N 1 ATOM 1829 C CA . ASP A 1 128 ? -3.982 17.143 31.519 1.00 12.21 ? 136 ASP A CA 1 ATOM 1830 C C . ASP A 1 128 ? -4.169 17.353 33.017 1.00 13.75 ? 136 ASP A C 1 ATOM 1831 O O . ASP A 1 128 ? -3.933 16.469 33.831 1.00 14.46 ? 136 ASP A O 1 ATOM 1832 C CB . ASP A 1 128 ? -3.335 15.799 31.233 1.00 12.87 ? 136 ASP A CB 1 ATOM 1833 C CG . ASP A 1 128 ? -3.198 15.496 29.753 1.00 12.76 ? 136 ASP A CG 1 ATOM 1834 O OD1 . ASP A 1 128 ? -4.032 16.001 28.978 1.00 13.68 ? 136 ASP A OD1 1 ATOM 1835 O OD2 . ASP A 1 128 ? -2.264 14.732 29.372 1.00 13.11 ? 136 ASP A OD2 1 ATOM 1836 H H . ASP A 1 128 ? -2.348 18.075 30.941 1.00 15.23 ? 136 ASP A H 1 ATOM 1837 H HA . ASP A 1 128 ? -4.860 17.144 31.107 1.00 14.66 ? 136 ASP A HA 1 ATOM 1838 H HB2 . ASP A 1 128 ? -2.447 15.790 31.622 1.00 15.45 ? 136 ASP A HB2 1 ATOM 1839 H HB3 . ASP A 1 128 ? -3.877 15.100 31.631 1.00 15.45 ? 136 ASP A HB3 1 ATOM 1840 N N . PHE A 1 129 ? -4.594 18.554 33.387 1.00 13.48 ? 137 PHE A N 1 ATOM 1841 C CA . PHE A 1 129 ? -4.761 18.949 34.768 1.00 13.60 ? 137 PHE A CA 1 ATOM 1842 C C . PHE A 1 129 ? -5.655 20.171 34.794 1.00 14.13 ? 137 PHE A C 1 ATOM 1843 O O . PHE A 1 129 ? -5.745 20.915 33.826 1.00 15.68 ? 137 PHE A O 1 ATOM 1844 C CB . PHE A 1 129 ? -3.408 19.308 35.427 1.00 14.29 ? 137 PHE A CB 1 ATOM 1845 C CG . PHE A 1 129 ? -3.375 18.996 36.899 1.00 14.76 ? 137 PHE A CG 1 ATOM 1846 C CD1 . PHE A 1 129 ? -3.038 17.731 37.329 1.00 15.73 ? 137 PHE A CD1 1 ATOM 1847 C CD2 . PHE A 1 129 ? -3.716 19.946 37.844 1.00 15.37 ? 137 PHE A CD2 1 ATOM 1848 C CE1 . PHE A 1 129 ? -3.057 17.415 38.671 1.00 16.36 ? 137 PHE A CE1 1 ATOM 1849 C CE2 . PHE A 1 129 ? -3.746 19.621 39.189 1.00 17.27 ? 137 PHE A CE2 1 ATOM 1850 C CZ . PHE A 1 129 ? -3.422 18.355 39.588 1.00 17.07 ? 137 PHE A CZ 1 ATOM 1851 H H . PHE A 1 129 ? -4.798 19.176 32.830 1.00 16.18 ? 137 PHE A H 1 ATOM 1852 H HA . PHE A 1 129 ? -5.182 18.235 35.272 1.00 16.32 ? 137 PHE A HA 1 ATOM 1853 H HB2 . PHE A 1 129 ? -2.702 18.801 34.997 1.00 17.15 ? 137 PHE A HB2 1 ATOM 1854 H HB3 . PHE A 1 129 ? -3.247 20.259 35.319 1.00 17.15 ? 137 PHE A HB3 1 ATOM 1855 H HD1 . PHE A 1 129 ? -2.817 17.077 36.706 1.00 18.87 ? 137 PHE A HD1 1 ATOM 1856 H HD2 . PHE A 1 129 ? -3.965 20.799 37.570 1.00 18.44 ? 137 PHE A HD2 1 ATOM 1857 H HE1 . PHE A 1 129 ? -2.829 16.558 38.950 1.00 19.63 ? 137 PHE A HE1 1 ATOM 1858 H HE2 . PHE A 1 129 ? -3.974 20.265 39.820 1.00 20.72 ? 137 PHE A HE2 1 ATOM 1859 H HZ . PHE A 1 129 ? -3.407 18.146 40.495 1.00 20.48 ? 137 PHE A HZ 1 ATOM 1860 N N . HIS A 1 130 ? -6.323 20.366 35.913 1.00 15.00 ? 138 HIS A N 1 ATOM 1861 C CA . HIS A 1 130 ? -7.035 21.596 36.173 1.00 15.95 ? 138 HIS A CA 1 ATOM 1862 C C . HIS A 1 130 ? -6.589 22.101 37.538 1.00 17.16 ? 138 HIS A C 1 ATOM 1863 O O . HIS A 1 130 ? -6.723 21.369 38.510 1.00 18.70 ? 138 HIS A O 1 ATOM 1864 C CB . HIS A 1 130 ? -8.527 21.385 36.206 1.00 17.67 ? 138 HIS A CB 1 ATOM 1865 C CG . HIS A 1 130 ? -9.262 22.619 36.592 1.00 20.23 ? 138 HIS A CG 1 ATOM 1866 N ND1 . HIS A 1 130 ? -9.629 22.889 37.892 1.00 23.51 ? 138 HIS A ND1 1 ATOM 1867 C CD2 . HIS A 1 130 ? -9.658 23.683 35.856 1.00 23.51 ? 138 HIS A CD2 1 ATOM 1868 C CE1 . HIS A 1 130 ? -10.233 24.061 37.940 1.00 25.73 ? 138 HIS A CE1 1 ATOM 1869 N NE2 . HIS A 1 130 ? -10.263 24.561 36.721 1.00 24.39 ? 138 HIS A NE2 1 ATOM 1870 H H . HIS A 1 130 ? -6.379 19.790 36.549 1.00 18.00 ? 138 HIS A H 1 ATOM 1871 H HA . HIS A 1 130 ? -6.819 22.259 35.499 1.00 19.14 ? 138 HIS A HA 1 ATOM 1872 H HB2 . HIS A 1 130 ? -8.830 21.116 35.325 1.00 21.21 ? 138 HIS A HB2 1 ATOM 1873 H HB3 . HIS A 1 130 ? -8.736 20.694 36.855 1.00 21.21 ? 138 HIS A HB3 1 ATOM 1874 H HD2 . HIS A 1 130 ? -9.544 23.796 34.940 1.00 28.21 ? 138 HIS A HD2 1 ATOM 1875 H HE1 . HIS A 1 130 ? -10.583 24.463 38.702 1.00 30.88 ? 138 HIS A HE1 1 ATOM 1876 H HE2 . HIS A 1 130 ? -10.613 25.315 36.501 1.00 29.27 ? 138 HIS A HE2 1 ATOM 1877 N N . PRO A 1 131 ? -6.082 23.335 37.619 1.00 17.95 ? 139 PRO A N 1 ATOM 1878 C CA . PRO A 1 131 ? -5.790 24.268 36.525 1.00 17.27 ? 139 PRO A CA 1 ATOM 1879 C C . PRO A 1 131 ? -4.608 23.790 35.672 1.00 16.19 ? 139 PRO A C 1 ATOM 1880 O O . PRO A 1 131 ? -3.736 23.038 36.148 1.00 15.36 ? 139 PRO A O 1 ATOM 1881 C CB . PRO A 1 131 ? -5.457 25.582 37.250 1.00 20.82 ? 139 PRO A CB 1 ATOM 1882 C CG . PRO A 1 131 ? -5.777 25.360 38.645 1.00 22.51 ? 139 PRO A CG 1 ATOM 1883 C CD . PRO A 1 131 ? -5.791 23.924 38.927 1.00 21.12 ? 139 PRO A CD 1 ATOM 1884 H HA . PRO A 1 131 ? -6.571 24.393 35.963 1.00 20.72 ? 139 PRO A HA 1 ATOM 1885 H HB2 . PRO A 1 131 ? -4.514 25.781 37.145 1.00 24.98 ? 139 PRO A HB2 1 ATOM 1886 H HB3 . PRO A 1 131 ? -5.999 26.299 36.886 1.00 24.98 ? 139 PRO A HB3 1 ATOM 1887 H HG2 . PRO A 1 131 ? -5.107 25.797 39.193 1.00 27.01 ? 139 PRO A HG2 1 ATOM 1888 H HG3 . PRO A 1 131 ? -6.651 25.740 38.830 1.00 27.01 ? 139 PRO A HG3 1 ATOM 1889 H HD2 . PRO A 1 131 ? -4.922 23.633 39.245 1.00 25.35 ? 139 PRO A HD2 1 ATOM 1890 H HD3 . PRO A 1 131 ? -6.494 23.709 39.560 1.00 25.35 ? 139 PRO A HD3 1 ATOM 1891 N N . LYS A 1 132 ? -4.590 24.214 34.409 1.00 16.88 ? 140 LYS A N 1 ATOM 1892 C CA . LYS A 1 132 ? -3.539 23.775 33.506 1.00 16.67 ? 140 LYS A CA 1 ATOM 1893 C C . LYS A 1 132 ? -2.172 24.092 34.090 1.00 15.01 ? 140 LYS A C 1 ATOM 1894 O O . LYS A 1 132 ? -1.970 25.124 34.732 1.00 14.73 ? 140 LYS A O 1 ATOM 1895 C CB . LYS A 1 132 ? -3.671 24.436 32.140 1.00 19.07 ? 140 LYS A CB 1 ATOM 1896 C CG . LYS A 1 132 ? -3.464 25.918 32.073 1.00 26.81 ? 140 LYS A CG 1 ATOM 1897 C CD . LYS A 1 132 ? -3.545 26.398 30.617 1.00 31.71 ? 140 LYS A CD 1 ATOM 1898 C CE . LYS A 1 132 ? -3.011 27.816 30.488 1.00 35.70 ? 140 LYS A CE 1 ATOM 1899 N NZ . LYS A 1 132 ? -2.342 28.043 29.183 1.00 38.55 ? 140 LYS A NZ 1 ATOM 1900 H H . LYS A 1 132 ? -5.167 24.747 34.059 1.00 20.25 ? 140 LYS A H 1 ATOM 1901 H HA . LYS A 1 132 ? -3.602 22.815 33.386 1.00 20.00 ? 140 LYS A HA 1 ATOM 1902 H HB2 . LYS A 1 132 ? -3.020 24.031 31.546 1.00 22.89 ? 140 LYS A HB2 1 ATOM 1903 H HB3 . LYS A 1 132 ? -4.563 24.258 31.804 1.00 22.89 ? 140 LYS A HB3 1 ATOM 1904 H HG2 . LYS A 1 132 ? -4.157 26.365 32.584 1.00 32.17 ? 140 LYS A HG2 1 ATOM 1905 H HG3 . LYS A 1 132 ? -2.587 26.139 32.423 1.00 32.17 ? 140 LYS A HG3 1 ATOM 1906 H HD2 . LYS A 1 132 ? -3.010 25.816 30.056 1.00 38.05 ? 140 LYS A HD2 1 ATOM 1907 H HD3 . LYS A 1 132 ? -4.471 26.392 30.327 1.00 38.05 ? 140 LYS A HD3 1 ATOM 1908 H HE2 . LYS A 1 132 ? -3.748 28.442 30.562 1.00 42.85 ? 140 LYS A HE2 1 ATOM 1909 H HE3 . LYS A 1 132 ? -2.363 27.977 31.191 1.00 42.85 ? 140 LYS A HE3 1 ATOM 1910 H HZ1 . LYS A 1 132 ? -2.040 28.879 29.137 1.00 46.26 ? 140 LYS A HZ1 1 ATOM 1911 H HZ2 . LYS A 1 132 ? -1.656 27.483 29.091 1.00 46.26 ? 140 LYS A HZ2 1 ATOM 1912 H HZ3 . LYS A 1 132 ? -2.918 27.907 28.518 1.00 46.26 ? 140 LYS A HZ3 1 ATOM 1913 N N . ASN A 1 133 ? -1.233 23.176 33.882 1.00 14.46 ? 141 ASN A N 1 ATOM 1914 C CA . ASN A 1 133 ? 0.174 23.317 34.215 1.00 14.18 ? 141 ASN A CA 1 ATOM 1915 C C . ASN A 1 133 ? 0.448 23.189 35.710 1.00 14.55 ? 141 ASN A C 1 ATOM 1916 O O . ASN A 1 133 ? 1.599 23.119 36.074 1.00 14.79 ? 141 ASN A O 1 ATOM 1917 C CB . ASN A 1 133 ? 0.796 24.637 33.721 1.00 14.46 ? 141 ASN A CB 1 ATOM 1918 C CG . ASN A 1 133 ? 0.555 24.860 32.260 1.00 15.85 ? 141 ASN A CG 1 ATOM 1919 O OD1 . ASN A 1 133 ? 0.622 23.925 31.468 1.00 16.34 ? 141 ASN A OD1 1 ATOM 1920 N ND2 . ASN A 1 133 ? 0.230 26.079 31.899 1.00 19.89 ? 141 ASN A ND2 1 ATOM 1921 H H . ASN A 1 133 ? -1.405 22.414 33.523 1.00 17.35 ? 141 ASN A H 1 ATOM 1922 H HA . ASN A 1 133 ? 0.656 22.598 33.778 1.00 17.02 ? 141 ASN A HA 1 ATOM 1923 H HB2 . ASN A 1 133 ? 0.401 25.377 34.209 1.00 17.35 ? 141 ASN A HB2 1 ATOM 1924 H HB3 . ASN A 1 133 ? 1.754 24.613 33.869 1.00 17.35 ? 141 ASN A HB3 1 ATOM 1925 H HD21 . ASN A 1 133 ? 0.081 26.257 31.071 1.00 23.87 ? 141 ASN A HD21 1 ATOM 1926 H HD22 . ASN A 1 133 ? 0.165 26.700 32.491 1.00 23.87 ? 141 ASN A HD22 1 ATOM 1927 N N . GLN A 1 134 ? -0.551 23.158 36.578 1.00 14.80 ? 142 GLN A N 1 ATOM 1928 C CA . GLN A 1 134 ? -0.300 23.237 38.025 1.00 14.87 ? 142 GLN A CA 1 ATOM 1929 C C . GLN A 1 134 ? -0.195 21.837 38.643 1.00 14.66 ? 142 GLN A C 1 ATOM 1930 O O . GLN A 1 134 ? -0.960 21.441 39.519 1.00 15.67 ? 142 GLN A O 1 ATOM 1931 C CB . GLN A 1 134 ? -1.384 24.074 38.694 1.00 15.51 ? 142 GLN A CB 1 ATOM 1932 C CG . GLN A 1 134 ? -1.523 25.449 38.121 1.00 16.28 ? 142 GLN A CG 1 ATOM 1933 C CD . GLN A 1 134 ? -0.207 26.172 37.997 1.00 16.20 ? 142 GLN A CD 1 ATOM 1934 O OE1 . GLN A 1 134 ? 0.547 26.305 38.970 1.00 16.96 ? 142 GLN A OE1 1 ATOM 1935 N NE2 . GLN A 1 134 ? 0.089 26.651 36.804 1.00 17.85 ? 142 GLN A NE2 1 ATOM 1936 H H . GLN A 1 134 ? -1.382 23.092 36.365 1.00 17.75 ? 142 GLN A H 1 ATOM 1937 H HA . GLN A 1 134 ? 0.548 23.685 38.168 1.00 17.84 ? 142 GLN A HA 1 ATOM 1938 H HB2 . GLN A 1 134 ? -2.236 23.622 38.592 1.00 18.61 ? 142 GLN A HB2 1 ATOM 1939 H HB3 . GLN A 1 134 ? -1.170 24.166 39.636 1.00 18.61 ? 142 GLN A HB3 1 ATOM 1940 H HG2 . GLN A 1 134 ? -1.912 25.383 37.234 1.00 19.54 ? 142 GLN A HG2 1 ATOM 1941 H HG3 . GLN A 1 134 ? -2.100 25.974 38.697 1.00 19.54 ? 142 GLN A HG3 1 ATOM 1942 H HE21 . GLN A 1 134 ? -0.457 26.542 36.149 1.00 21.42 ? 142 GLN A HE21 1 ATOM 1943 H HE22 . GLN A 1 134 ? 0.829 27.072 36.681 1.00 21.42 ? 142 GLN A HE22 1 ATOM 1944 N N . PHE A 1 135 ? 0.783 21.083 38.162 1.00 13.79 ? 143 PHE A N 1 ATOM 1945 C CA . PHE A 1 135 ? 0.977 19.706 38.604 1.00 14.01 ? 143 PHE A CA 1 ATOM 1946 C C . PHE A 1 135 ? 1.633 19.674 39.979 1.00 14.79 ? 143 PHE A C 1 ATOM 1947 O O . PHE A 1 135 ? 2.785 20.120 40.115 1.00 14.78 ? 143 PHE A O 1 ATOM 1948 C CB . PHE A 1 135 ? 1.855 18.955 37.609 1.00 13.44 ? 143 PHE A CB 1 ATOM 1949 C CG . PHE A 1 135 ? 1.089 18.383 36.447 1.00 12.56 ? 143 PHE A CG 1 ATOM 1950 C CD1 . PHE A 1 135 ? 0.552 19.202 35.473 1.00 13.96 ? 143 PHE A CD1 1 ATOM 1951 C CD2 . PHE A 1 135 ? 0.906 17.022 36.360 1.00 12.98 ? 143 PHE A CD2 1 ATOM 1952 C CE1 . PHE A 1 135 ? -0.171 18.659 34.429 1.00 14.26 ? 143 PHE A CE1 1 ATOM 1953 C CE2 . PHE A 1 135 ? 0.176 16.472 35.327 1.00 13.76 ? 143 PHE A CE2 1 ATOM 1954 C CZ . PHE A 1 135 ? -0.348 17.288 34.358 1.00 14.13 ? 143 PHE A CZ 1 ATOM 1955 H H . PHE A 1 135 ? 1.353 21.345 37.574 1.00 16.55 ? 143 PHE A H 1 ATOM 1956 H HA . PHE A 1 135 ? 0.119 19.258 38.660 1.00 16.81 ? 143 PHE A HA 1 ATOM 1957 H HB2 . PHE A 1 135 ? 2.521 19.565 37.255 1.00 16.13 ? 143 PHE A HB2 1 ATOM 1958 H HB3 . PHE A 1 135 ? 2.292 18.220 38.068 1.00 16.13 ? 143 PHE A HB3 1 ATOM 1959 H HD1 . PHE A 1 135 ? 0.668 20.124 35.526 1.00 16.76 ? 143 PHE A HD1 1 ATOM 1960 H HD2 . PHE A 1 135 ? 1.256 16.469 37.020 1.00 15.57 ? 143 PHE A HD2 1 ATOM 1961 H HE1 . PHE A 1 135 ? -0.530 19.211 33.772 1.00 17.11 ? 143 PHE A HE1 1 ATOM 1962 H HE2 . PHE A 1 135 ? 0.062 15.550 35.274 1.00 16.51 ? 143 PHE A HE2 1 ATOM 1963 H HZ . PHE A 1 135 ? -0.829 16.919 33.653 1.00 16.95 ? 143 PHE A HZ 1 ATOM 1964 N N . PRO A 1 136 ? 0.970 19.120 41.002 1.00 14.67 ? 144 PRO A N 1 ATOM 1965 C CA . PRO A 1 136 ? 1.564 19.045 42.335 1.00 15.65 ? 144 PRO A CA 1 ATOM 1966 C C . PRO A 1 136 ? 2.613 17.964 42.438 1.00 14.37 ? 144 PRO A C 1 ATOM 1967 O O . PRO A 1 136 ? 2.570 16.935 41.766 1.00 15.30 ? 144 PRO A O 1 ATOM 1968 C CB . PRO A 1 136 ? 0.367 18.673 43.223 1.00 18.35 ? 144 PRO A CB 1 ATOM 1969 C CG . PRO A 1 136 ? -0.854 18.922 42.430 1.00 18.89 ? 144 PRO A CG 1 ATOM 1970 C CD . PRO A 1 136 ? -0.434 18.682 41.022 1.00 15.09 ? 144 PRO A CD 1 ATOM 1971 H HA . PRO A 1 136 ? 1.932 19.900 42.606 1.00 18.78 ? 144 PRO A HA 1 ATOM 1972 H HB2 . PRO A 1 136 ? 0.426 17.736 43.466 1.00 22.02 ? 144 PRO A HB2 1 ATOM 1973 H HB3 . PRO A 1 136 ? 0.372 19.229 44.018 1.00 22.02 ? 144 PRO A HB3 1 ATOM 1974 H HG2 . PRO A 1 136 ? -1.550 18.299 42.693 1.00 22.66 ? 144 PRO A HG2 1 ATOM 1975 H HG3 . PRO A 1 136 ? -1.145 19.839 42.552 1.00 22.66 ? 144 PRO A HG3 1 ATOM 1976 H HD2 . PRO A 1 136 ? -0.496 17.738 40.807 1.00 18.10 ? 144 PRO A HD2 1 ATOM 1977 H HD3 . PRO A 1 136 ? -0.965 19.220 40.415 1.00 18.10 ? 144 PRO A HD3 1 ATOM 1978 N N . ALA A 1 137 ? 3.530 18.171 43.375 1.00 15.59 ? 145 ALA A N 1 ATOM 1979 C CA . ALA A 1 137 ? 4.501 17.150 43.740 1.00 16.56 ? 145 ALA A CA 1 ATOM 1980 C C . ALA A 1 137 ? 3.977 16.207 44.804 1.00 17.46 ? 145 ALA A C 1 ATOM 1981 O O . ALA A 1 137 ? 4.726 15.812 45.694 1.00 23.57 ? 145 ALA A O 1 ATOM 1982 C CB . ALA A 1 137 ? 5.793 17.811 44.193 1.00 18.95 ? 145 ALA A CB 1 ATOM 1983 H H . ALA A 1 137 ? 3.612 18.903 43.818 1.00 18.70 ? 145 ALA A H 1 ATOM 1984 H HA . ALA A 1 137 ? 4.703 16.619 42.953 1.00 19.87 ? 145 ALA A HA 1 ATOM 1985 H HB1 . ALA A 1 137 ? 6.432 17.123 44.434 1.00 22.74 ? 145 ALA A HB1 1 ATOM 1986 H HB2 . ALA A 1 137 ? 6.143 18.349 43.465 1.00 22.74 ? 145 ALA A HB2 1 ATOM 1987 H HB3 . ALA A 1 137 ? 5.607 18.374 44.960 1.00 22.74 ? 145 ALA A HB3 1 ATOM 1988 N N . GLN A 1 138 ? 2.698 15.880 44.761 1.00 16.57 ? 146 GLN A N 1 ATOM 1989 C CA . GLN A 1 138 ? 2.077 14.997 45.723 1.00 17.91 ? 146 GLN A CA 1 ATOM 1990 C C . GLN A 1 138 ? 0.779 14.506 45.110 1.00 16.01 ? 146 GLN A C 1 ATOM 1991 O O . GLN A 1 138 ? 0.339 14.977 44.055 1.00 15.55 ? 146 GLN A O 1 ATOM 1992 C CB . GLN A 1 138 ? 1.832 15.737 47.044 1.00 20.03 ? 146 GLN A CB 1 ATOM 1993 C CG . GLN A 1 138 ? 0.949 16.960 46.848 1.00 22.06 ? 146 GLN A CG 1 ATOM 1994 C CD . GLN A 1 138 ? 0.694 17.717 48.132 1.00 26.83 ? 146 GLN A CD 1 ATOM 1995 O OE1 . GLN A 1 138 ? 0.749 17.151 49.223 1.00 28.64 ? 146 GLN A OE1 1 ATOM 1996 N NE2 . GLN A 1 138 ? 0.393 19.005 48.009 1.00 29.28 ? 146 GLN A NE2 1 ATOM 1997 H H . GLN A 1 138 ? 2.153 16.168 44.161 1.00 19.88 ? 146 GLN A H 1 ATOM 1998 H HA . GLN A 1 138 ? 2.653 14.236 45.892 1.00 21.49 ? 146 GLN A HA 1 ATOM 1999 H HB2 . GLN A 1 138 ? 1.389 15.139 47.667 1.00 24.04 ? 146 GLN A HB2 1 ATOM 2000 H HB3 . GLN A 1 138 ? 2.681 16.031 47.408 1.00 24.04 ? 146 GLN A HB3 1 ATOM 2001 H HG2 . GLN A 1 138 ? 1.382 17.565 46.226 1.00 26.47 ? 146 GLN A HG2 1 ATOM 2002 H HG3 . GLN A 1 138 ? 0.092 16.677 46.492 1.00 26.47 ? 146 GLN A HG3 1 ATOM 2003 H HE21 . GLN A 1 138 ? 0.353 19.364 47.228 1.00 35.14 ? 146 GLN A HE21 1 ATOM 2004 H HE22 . GLN A 1 138 ? 0.239 19.480 48.709 1.00 35.14 ? 146 GLN A HE22 1 ATOM 2005 N N . SER A 1 139 ? 0.176 13.537 45.785 1.00 15.12 ? 147 SER A N 1 ATOM 2006 C CA . SER A 1 139 ? -1.037 12.929 45.288 1.00 15.34 ? 147 SER A CA 1 ATOM 2007 C C . SER A 1 139 ? -2.171 13.945 45.249 1.00 14.85 ? 147 SER A C 1 ATOM 2008 O O . SER A 1 139 ? -2.152 14.977 45.914 1.00 16.42 ? 147 SER A O 1 ATOM 2009 C CB . SER A 1 139 ? -1.406 11.735 46.156 1.00 16.44 ? 147 SER A CB 1 ATOM 2010 O OG . SER A 1 139 ? -2.475 11.051 45.549 1.00 21.29 ? 147 SER A OG 1 ATOM 2011 H H . SER A 1 139 ? 0.453 13.217 46.534 1.00 18.14 ? 147 SER A H 1 ATOM 2012 H HA . SER A 1 139 ? -0.886 12.610 44.385 1.00 18.41 ? 147 SER A HA 1 ATOM 2013 H HB2 . SER A 1 139 ? -0.643 11.141 46.228 1.00 19.73 ? 147 SER A HB2 1 ATOM 2014 H HB3 . SER A 1 139 ? -1.678 12.046 47.033 1.00 19.73 ? 147 SER A HB3 1 ATOM 2015 H HG . SER A 1 139 ? -2.250 10.785 44.784 1.00 25.55 ? 147 SER A HG 1 ATOM 2016 N N . ASN A 1 140 ? -3.164 13.643 44.428 1.00 14.37 ? 148 ASN A N 1 ATOM 2017 C CA . ASN A 1 140 ? -4.311 14.511 44.205 1.00 14.54 ? 148 ASN A CA 1 ATOM 2018 C C . ASN A 1 140 ? -5.329 13.707 43.403 1.00 14.50 ? 148 ASN A C 1 ATOM 2019 O O . ASN A 1 140 ? -5.044 12.595 42.956 1.00 15.05 ? 148 ASN A O 1 ATOM 2020 C CB . ASN A 1 140 ? -3.901 15.773 43.460 1.00 15.23 ? 148 ASN A CB 1 ATOM 2021 C CG . ASN A 1 140 ? -3.241 15.452 42.146 1.00 14.21 ? 148 ASN A CG 1 ATOM 2022 O OD1 . ASN A 1 140 ? -3.921 15.134 41.177 1.00 14.91 ? 148 ASN A OD1 1 ATOM 2023 N ND2 . ASN A 1 140 ? -1.910 15.475 42.090 1.00 14.78 ? 148 ASN A ND2 1 ATOM 2024 H H . ASN A 1 140 ? -3.197 12.914 43.972 1.00 17.25 ? 148 ASN A H 1 ATOM 2025 H HA . ASN A 1 140 ? -4.707 14.761 45.055 1.00 17.45 ? 148 ASN A HA 1 ATOM 2026 H HB2 . ASN A 1 140 ? -4.690 16.308 43.280 1.00 18.28 ? 148 ASN A HB2 1 ATOM 2027 H HB3 . ASN A 1 140 ? -3.272 16.274 44.002 1.00 18.28 ? 148 ASN A HB3 1 ATOM 2028 H HD21 . ASN A 1 140 ? -1.508 15.296 41.351 1.00 17.74 ? 148 ASN A HD21 1 ATOM 2029 H HD22 . ASN A 1 140 ? -1.453 15.669 42.792 1.00 17.74 ? 148 ASN A HD22 1 ATOM 2030 N N . ARG A 1 141 ? -6.529 14.271 43.243 1.00 14.81 ? 149 ARG A N 1 ATOM 2031 C CA . ARG A 1 141 ? -7.612 13.527 42.594 1.00 15.51 ? 149 ARG A CA 1 ATOM 2032 C C . ARG A 1 141 ? -7.266 13.138 41.166 1.00 14.79 ? 149 ARG A C 1 ATOM 2033 O O . ARG A 1 141 ? -7.663 12.071 40.711 1.00 16.50 ? 149 ARG A O 1 ATOM 2034 C CB . ARG A 1 141 ? -8.909 14.339 42.595 1.00 16.24 ? 149 ARG A CB 1 ATOM 2035 C CG . ARG A 1 141 ? -9.561 14.434 43.932 1.00 16.36 ? 149 ARG A CG 1 ATOM 2036 C CD . ARG A 1 141 ? -10.868 15.182 43.839 1.00 18.23 ? 149 ARG A CD 1 ATOM 2037 N NE . ARG A 1 141 ? -10.644 16.563 43.454 1.00 19.22 ? 149 ARG A NE 1 ATOM 2038 C CZ . ARG A 1 141 ? -10.381 17.559 44.286 1.00 21.42 ? 149 ARG A CZ 1 ATOM 2039 N NH1 . ARG A 1 141 ? -10.353 17.339 45.603 1.00 20.70 ? 149 ARG A NH1 1 ATOM 2040 N NH2 . ARG A 1 141 ? -10.166 18.782 43.790 1.00 24.58 ? 149 ARG A NH2 1 ATOM 2041 H H . ARG A 1 141 ? -6.740 15.065 43.496 1.00 17.77 ? 149 ARG A H 1 ATOM 2042 H HA . ARG A 1 141 ? -7.773 12.711 43.093 1.00 18.62 ? 149 ARG A HA 1 ATOM 2043 H HB2 . ARG A 1 141 ? -8.713 15.241 42.296 1.00 19.49 ? 149 ARG A HB2 1 ATOM 2044 H HB3 . ARG A 1 141 ? -9.539 13.921 41.987 1.00 19.49 ? 149 ARG A HB3 1 ATOM 2045 H HG2 . ARG A 1 141 ? -9.742 13.542 44.266 1.00 19.63 ? 149 ARG A HG2 1 ATOM 2046 H HG3 . ARG A 1 141 ? -8.977 14.912 44.542 1.00 19.63 ? 149 ARG A HG3 1 ATOM 2047 H HD2 . ARG A 1 141 ? -11.431 14.765 43.168 1.00 21.88 ? 149 ARG A HD2 1 ATOM 2048 H HD3 . ARG A 1 141 ? -11.307 15.172 44.703 1.00 21.88 ? 149 ARG A HD3 1 ATOM 2049 H HE . ARG A 1 141 ? -10.687 16.751 42.616 1.00 23.07 ? 149 ARG A HE 1 ATOM 2050 H HH11 . ARG A 1 141 ? -10.486 16.547 45.910 1.00 24.84 ? 149 ARG A HH11 1 ATOM 2051 H HH12 . ARG A 1 141 ? -10.189 17.988 46.144 1.00 24.84 ? 149 ARG A HH12 1 ATOM 2052 H HH21 . ARG A 1 141 ? -10.197 18.913 42.941 1.00 29.49 ? 149 ARG A HH21 1 ATOM 2053 H HH22 . ARG A 1 141 ? -10.011 19.440 44.322 1.00 29.49 ? 149 ARG A HH22 1 ATOM 2054 N N . ILE A 1 142 ? -6.584 14.006 40.437 1.00 14.12 ? 150 ILE A N 1 ATOM 2055 C CA . ILE A 1 142 ? -6.243 13.701 39.058 1.00 14.57 ? 150 ILE A CA 1 ATOM 2056 C C . ILE A 1 142 ? -5.250 12.551 38.968 1.00 13.69 ? 150 ILE A C 1 ATOM 2057 O O . ILE A 1 142 ? -5.470 11.601 38.210 1.00 14.06 ? 150 ILE A O 1 ATOM 2058 C CB . ILE A 1 142 ? -5.813 14.968 38.305 1.00 15.32 ? 150 ILE A CB 1 ATOM 2059 C CG1 . ILE A 1 142 ? -7.055 15.879 38.170 1.00 18.56 ? 150 ILE A CG1 1 ATOM 2060 C CG2 . ILE A 1 142 ? -5.235 14.623 36.963 1.00 15.53 ? 150 ILE A CG2 1 ATOM 2061 C CD1 . ILE A 1 142 ? -6.776 17.243 37.638 1.00 19.94 ? 150 ILE A CD1 1 ATOM 2062 H H . ILE A 1 142 ? -6.308 14.773 40.713 1.00 16.95 ? 150 ILE A H 1 ATOM 2063 H HA . ILE A 1 142 ? -7.053 13.392 38.624 1.00 17.48 ? 150 ILE A HA 1 ATOM 2064 H HB . ILE A 1 142 ? -5.139 15.430 38.828 1.00 18.38 ? 150 ILE A HB 1 ATOM 2065 H HG12 . ILE A 1 142 ? -7.686 15.453 37.569 1.00 22.27 ? 150 ILE A HG12 1 ATOM 2066 H HG13 . ILE A 1 142 ? -7.459 15.982 39.046 1.00 22.27 ? 150 ILE A HG13 1 ATOM 2067 H HG21 . ILE A 1 142 ? -4.974 15.442 36.513 1.00 18.63 ? 150 ILE A HG21 1 ATOM 2068 H HG22 . ILE A 1 142 ? -4.461 14.053 37.089 1.00 18.63 ? 150 ILE A HG22 1 ATOM 2069 H HG23 . ILE A 1 142 ? -5.907 14.158 36.440 1.00 18.63 ? 150 ILE A HG23 1 ATOM 2070 H HD11 . ILE A 1 142 ? -7.608 17.739 37.588 1.00 23.93 ? 150 ILE A HD11 1 ATOM 2071 H HD12 . ILE A 1 142 ? -6.157 17.694 38.234 1.00 23.93 ? 150 ILE A HD12 1 ATOM 2072 H HD13 . ILE A 1 142 ? -6.385 17.163 36.754 1.00 23.93 ? 150 ILE A HD13 1 ATOM 2073 N N . TYR A 1 143 ? -4.160 12.593 39.742 1.00 13.45 ? 151 TYR A N 1 ATOM 2074 C CA . TYR A 1 143 ? -3.242 11.457 39.667 1.00 13.54 ? 151 TYR A CA 1 ATOM 2075 C C . TYR A 1 143 ? -3.960 10.181 40.077 1.00 13.54 ? 151 TYR A C 1 ATOM 2076 O O . TYR A 1 143 ? -3.730 9.125 39.482 1.00 14.55 ? 151 TYR A O 1 ATOM 2077 C CB . TYR A 1 143 ? -1.994 11.620 40.542 1.00 13.38 ? 151 TYR A CB 1 ATOM 2078 C CG . TYR A 1 143 ? -1.062 12.763 40.223 1.00 13.67 ? 151 TYR A CG 1 ATOM 2079 C CD1 . TYR A 1 143 ? -1.218 13.563 39.107 1.00 13.46 ? 151 TYR A CD1 1 ATOM 2080 C CD2 . TYR A 1 143 ? 0.011 13.040 41.074 1.00 14.25 ? 151 TYR A CD2 1 ATOM 2081 C CE1 . TYR A 1 143 ? -0.381 14.624 38.871 1.00 12.94 ? 151 TYR A CE1 1 ATOM 2082 C CE2 . TYR A 1 143 ? 0.883 14.093 40.816 1.00 13.85 ? 151 TYR A CE2 1 ATOM 2083 C CZ . TYR A 1 143 ? 0.670 14.892 39.737 1.00 12.58 ? 151 TYR A CZ 1 ATOM 2084 O OH . TYR A 1 143 ? 1.521 15.967 39.504 1.00 13.95 ? 151 TYR A OH 1 ATOM 2085 H H . TYR A 1 143 ? -3.941 13.223 40.285 1.00 16.14 ? 151 TYR A H 1 ATOM 2086 H HA . TYR A 1 143 ? -2.949 11.352 38.748 1.00 16.25 ? 151 TYR A HA 1 ATOM 2087 H HB2 . TYR A 1 143 ? -2.286 11.740 41.460 1.00 16.05 ? 151 TYR A HB2 1 ATOM 2088 H HB3 . TYR A 1 143 ? -1.475 10.803 40.478 1.00 16.05 ? 151 TYR A HB3 1 ATOM 2089 H HD1 . TYR A 1 143 ? -1.935 13.412 38.534 1.00 16.15 ? 151 TYR A HD1 1 ATOM 2090 H HD2 . TYR A 1 143 ? 0.144 12.512 41.828 1.00 17.10 ? 151 TYR A HD2 1 ATOM 2091 H HE1 . TYR A 1 143 ? -0.514 15.162 38.124 1.00 15.53 ? 151 TYR A HE1 1 ATOM 2092 H HE2 . TYR A 1 143 ? 1.577 14.280 41.406 1.00 16.62 ? 151 TYR A HE2 1 ATOM 2093 H HH . TYR A 1 143 ? 2.105 16.006 40.106 1.00 16.73 ? 151 TYR A HH 1 ATOM 2094 N N . ASN A 1 144 ? -4.815 10.259 41.100 1.00 13.98 ? 152 ASN A N 1 ATOM 2095 C CA . ASN A 1 144 ? -5.502 9.066 41.582 1.00 15.42 ? 152 ASN A CA 1 ATOM 2096 C C . ASN A 1 144 ? -6.438 8.502 40.521 1.00 15.33 ? 152 ASN A C 1 ATOM 2097 O O . ASN A 1 144 ? -6.468 7.286 40.282 1.00 16.21 ? 152 ASN A O 1 ATOM 2098 C CB . ASN A 1 144 ? -6.288 9.383 42.845 1.00 16.33 ? 152 ASN A CB 1 ATOM 2099 C CG . ASN A 1 144 ? -5.410 9.482 44.057 1.00 20.14 ? 152 ASN A CG 1 ATOM 2100 O OD1 . ASN A 1 144 ? -4.327 8.931 44.093 1.00 22.47 ? 152 ASN A OD1 1 ATOM 2101 N ND2 . ASN A 1 144 ? -5.884 10.174 45.061 1.00 25.23 ? 152 ASN A ND2 1 ATOM 2102 H H . ASN A 1 144 ? -5.011 10.981 41.524 1.00 16.78 ? 152 ASN A H 1 ATOM 2103 H HA . ASN A 1 144 ? -4.845 8.386 41.798 1.00 18.50 ? 152 ASN A HA 1 ATOM 2104 H HB2 . ASN A 1 144 ? -6.742 10.232 42.731 1.00 19.59 ? 152 ASN A HB2 1 ATOM 2105 H HB3 . ASN A 1 144 ? -6.936 8.678 43.000 1.00 19.59 ? 152 ASN A HB3 1 ATOM 2106 H HD21 . ASN A 1 144 ? -5.420 10.261 45.780 1.00 30.27 ? 152 ASN A HD21 1 ATOM 2107 H HD22 . ASN A 1 144 ? -6.659 10.540 45.003 1.00 30.27 ? 152 ASN A HD22 1 ATOM 2108 N N . GLN A 1 145 ? -7.218 9.363 39.866 1.00 15.13 ? 153 GLN A N 1 ATOM 2109 C CA . GLN A 1 145 ? -8.185 8.861 38.908 1.00 16.19 ? 153 GLN A CA 1 ATOM 2110 C C . GLN A 1 145 ? -7.498 8.397 37.630 1.00 15.39 ? 153 GLN A C 1 ATOM 2111 O O . GLN A 1 145 ? -7.899 7.390 37.035 1.00 15.21 ? 153 GLN A O 1 ATOM 2112 C CB . GLN A 1 145 ? -9.239 9.921 38.607 1.00 17.70 ? 153 GLN A CB 1 ATOM 2113 C CG . GLN A 1 145 ? -10.169 9.538 37.455 1.00 22.80 ? 153 GLN A CG 1 ATOM 2114 C CD . GLN A 1 145 ? -10.912 8.235 37.721 1.00 26.00 ? 153 GLN A CD 1 ATOM 2115 O OE1 . GLN A 1 145 ? -11.107 7.830 38.869 1.00 28.01 ? 153 GLN A OE1 1 ATOM 2116 N NE2 . GLN A 1 145 ? -11.319 7.578 36.670 1.00 29.43 ? 153 GLN A NE2 1 ATOM 2117 H H . GLN A 1 145 ? -7.204 10.218 39.957 1.00 18.16 ? 153 GLN A H 1 ATOM 2118 H HA . GLN A 1 145 ? -8.637 8.095 39.295 1.00 19.42 ? 153 GLN A HA 1 ATOM 2119 H HB2 . GLN A 1 145 ? -9.784 10.056 39.398 1.00 21.24 ? 153 GLN A HB2 1 ATOM 2120 H HB3 . GLN A 1 145 ? -8.793 10.749 38.368 1.00 21.24 ? 153 GLN A HB3 1 ATOM 2121 H HG2 . GLN A 1 145 ? -10.828 10.240 37.332 1.00 27.36 ? 153 GLN A HG2 1 ATOM 2122 H HG3 . GLN A 1 145 ? -9.645 9.427 36.647 1.00 27.36 ? 153 GLN A HG3 1 ATOM 2123 H HE21 . GLN A 1 145 ? -11.164 7.887 35.882 1.00 35.32 ? 153 GLN A HE21 1 ATOM 2124 H HE22 . GLN A 1 145 ? -11.743 6.836 36.764 1.00 35.32 ? 153 GLN A HE22 1 ATOM 2125 N N . VAL A 1 146 ? -6.446 9.089 37.195 1.00 13.93 ? 154 VAL A N 1 ATOM 2126 C CA . VAL A 1 146 ? -5.724 8.622 36.024 1.00 13.41 ? 154 VAL A CA 1 ATOM 2127 C C . VAL A 1 146 ? -5.053 7.284 36.307 1.00 13.37 ? 154 VAL A C 1 ATOM 2128 O O . VAL A 1 146 ? -5.010 6.413 35.436 1.00 14.67 ? 154 VAL A O 1 ATOM 2129 C CB . VAL A 1 146 ? -4.768 9.696 35.485 1.00 13.68 ? 154 VAL A CB 1 ATOM 2130 C CG1 . VAL A 1 146 ? -3.895 9.127 34.346 1.00 13.52 ? 154 VAL A CG1 1 ATOM 2131 C CG2 . VAL A 1 146 ? -5.576 10.916 35.033 1.00 15.55 ? 154 VAL A CG2 1 ATOM 2132 H H . VAL A 1 146 ? -6.140 9.809 37.551 1.00 16.71 ? 154 VAL A H 1 ATOM 2133 H HA . VAL A 1 146 ? -6.377 8.460 35.324 1.00 16.09 ? 154 VAL A HA 1 ATOM 2134 H HB . VAL A 1 146 ? -4.177 9.978 36.201 1.00 16.42 ? 154 VAL A HB 1 ATOM 2135 H HG11 . VAL A 1 146 ? -3.302 9.824 34.025 1.00 16.23 ? 154 VAL A HG11 1 ATOM 2136 H HG12 . VAL A 1 146 ? -3.376 8.382 34.688 1.00 16.23 ? 154 VAL A HG12 1 ATOM 2137 H HG13 . VAL A 1 146 ? -4.472 8.826 33.627 1.00 16.23 ? 154 VAL A HG13 1 ATOM 2138 H HG21 . VAL A 1 146 ? -4.967 11.590 34.695 1.00 18.66 ? 154 VAL A HG21 1 ATOM 2139 H HG22 . VAL A 1 146 ? -6.192 10.645 34.335 1.00 18.66 ? 154 VAL A HG22 1 ATOM 2140 H HG23 . VAL A 1 146 ? -6.069 11.267 35.792 1.00 18.66 ? 154 VAL A HG23 1 ATOM 2141 N N . ALA A 1 147 ? -4.533 7.084 37.525 1.00 13.84 ? 155 ALA A N 1 ATOM 2142 C CA . ALA A 1 147 ? -3.999 5.770 37.868 1.00 13.92 ? 155 ALA A CA 1 ATOM 2143 C C . ALA A 1 147 ? -5.044 4.685 37.687 1.00 14.98 ? 155 ALA A C 1 ATOM 2144 O O . ALA A 1 147 ? -4.712 3.573 37.266 1.00 16.45 ? 155 ALA A O 1 ATOM 2145 C CB . ALA A 1 147 ? -3.455 5.746 39.304 1.00 15.85 ? 155 ALA A CB 1 ATOM 2146 H H . ALA A 1 147 ? -4.481 7.675 38.148 1.00 16.61 ? 155 ALA A H 1 ATOM 2147 H HA . ALA A 1 147 ? -3.261 5.570 37.271 1.00 16.71 ? 155 ALA A HA 1 ATOM 2148 H HB1 . ALA A 1 147 ? -3.110 4.860 39.496 1.00 19.02 ? 155 ALA A HB1 1 ATOM 2149 H HB2 . ALA A 1 147 ? -2.745 6.403 39.383 1.00 19.02 ? 155 ALA A HB2 1 ATOM 2150 H HB3 . ALA A 1 147 ? -4.175 5.961 39.918 1.00 19.02 ? 155 ALA A HB3 1 ATOM 2151 N N . GLU A 1 148 ? -6.305 4.977 38.012 1.00 15.21 ? 156 GLU A N 1 ATOM 2152 C CA . GLU A 1 148 ? -7.365 3.994 37.801 1.00 16.24 ? 156 GLU A CA 1 ATOM 2153 C C . GLU A 1 148 ? -7.600 3.747 36.314 1.00 16.04 ? 156 GLU A C 1 ATOM 2154 O O . GLU A 1 148 ? -7.764 2.600 35.891 1.00 17.93 ? 156 GLU A O 1 ATOM 2155 C CB . GLU A 1 148 ? -8.654 4.447 38.476 1.00 18.06 ? 156 GLU A CB 1 ATOM 2156 C CG . GLU A 1 148 ? -8.557 4.658 39.980 1.00 21.14 ? 156 GLU A CG 1 ATOM 2157 C CD . GLU A 1 148 ? -8.029 3.459 40.781 1.00 25.21 ? 156 GLU A CD 1 ATOM 2158 O OE1 . GLU A 1 148 ? -8.095 2.303 40.324 1.00 29.12 ? 156 GLU A OE1 1 ATOM 2159 O OE2 . GLU A 1 148 ? -7.547 3.681 41.908 1.00 29.48 ? 156 GLU A OE2 1 ATOM 2160 H H . GLU A 1 148 ? -6.568 5.722 38.350 1.00 18.25 ? 156 GLU A H 1 ATOM 2161 H HA . GLU A 1 148 ? -7.097 3.153 38.204 1.00 19.49 ? 156 GLU A HA 1 ATOM 2162 H HB2 . GLU A 1 148 ? -8.929 5.288 38.080 1.00 21.68 ? 156 GLU A HB2 1 ATOM 2163 H HB3 . GLU A 1 148 ? -9.336 3.775 38.319 1.00 21.68 ? 156 GLU A HB3 1 ATOM 2164 H HG2 . GLU A 1 148 ? -7.962 5.405 40.147 1.00 25.37 ? 156 GLU A HG2 1 ATOM 2165 H HG3 . GLU A 1 148 ? -9.442 4.867 40.318 1.00 25.37 ? 156 GLU A HG3 1 ATOM 2166 N N . LEU A 1 149 ? -7.607 4.809 35.508 1.00 15.62 ? 157 LEU A N 1 ATOM 2167 C CA . LEU A 1 149 ? -7.808 4.651 34.066 1.00 15.63 ? 157 LEU A CA 1 ATOM 2168 C C . LEU A 1 149 ? -6.697 3.826 33.429 1.00 15.19 ? 157 LEU A C 1 ATOM 2169 O O . LEU A 1 149 ? -6.947 3.060 32.494 1.00 15.99 ? 157 LEU A O 1 ATOM 2170 C CB . LEU A 1 149 ? -7.843 6.027 33.397 1.00 15.79 ? 157 LEU A CB 1 ATOM 2171 C CG . LEU A 1 149 ? -8.960 6.991 33.800 1.00 16.62 ? 157 LEU A CG 1 ATOM 2172 C CD1 . LEU A 1 149 ? -8.785 8.307 33.132 1.00 17.37 ? 157 LEU A CD1 1 ATOM 2173 C CD2 . LEU A 1 149 ? -10.329 6.425 33.492 1.00 18.63 ? 157 LEU A CD2 1 ATOM 2174 H H . LEU A 1 149 ? -7.500 5.622 35.767 1.00 18.75 ? 157 LEU A H 1 ATOM 2175 H HA . LEU A 1 149 ? -8.654 4.207 33.903 1.00 18.76 ? 157 LEU A HA 1 ATOM 2176 H HB2 . LEU A 1 149 ? -7.003 6.473 33.587 1.00 18.95 ? 157 LEU A HB2 1 ATOM 2177 H HB3 . LEU A 1 149 ? -7.919 5.892 32.439 1.00 18.95 ? 157 LEU A HB3 1 ATOM 2178 H HG . LEU A 1 149 ? -8.912 7.138 34.757 1.00 19.94 ? 157 LEU A HG 1 ATOM 2179 H HD11 . LEU A 1 149 ? -9.505 8.897 33.405 1.00 20.84 ? 157 LEU A HD11 1 ATOM 2180 H HD12 . LEU A 1 149 ? -7.930 8.683 33.396 1.00 20.84 ? 157 LEU A HD12 1 ATOM 2181 H HD13 . LEU A 1 149 ? -8.808 8.178 32.171 1.00 20.84 ? 157 LEU A HD13 1 ATOM 2182 H HD21 . LEU A 1 149 ? -11.004 7.066 33.763 1.00 22.36 ? 157 LEU A HD21 1 ATOM 2183 H HD22 . LEU A 1 149 ? -10.394 6.258 32.538 1.00 22.36 ? 157 LEU A HD22 1 ATOM 2184 H HD23 . LEU A 1 149 ? -10.445 5.595 33.981 1.00 22.36 ? 157 LEU A HD23 1 ATOM 2185 N N . TRP A 1 150 ? -5.462 4.002 33.895 1.00 14.53 ? 158 TRP A N 1 ATOM 2186 C CA . TRP A 1 150 ? -4.300 3.374 33.289 1.00 14.42 ? 158 TRP A CA 1 ATOM 2187 C C . TRP A 1 150 ? -3.885 2.104 34.010 1.00 14.93 ? 158 TRP A C 1 ATOM 2188 O O . TRP A 1 150 ? -2.915 1.455 33.605 1.00 16.06 ? 158 TRP A O 1 ATOM 2189 C CB . TRP A 1 150 ? -3.151 4.392 33.180 1.00 14.20 ? 158 TRP A CB 1 ATOM 2190 C CG . TRP A 1 150 ? -3.492 5.542 32.260 1.00 13.20 ? 158 TRP A CG 1 ATOM 2191 C CD1 . TRP A 1 150 ? -4.595 5.650 31.456 1.00 13.85 ? 158 TRP A CD1 1 ATOM 2192 C CD2 . TRP A 1 150 ? -2.736 6.736 32.055 1.00 12.45 ? 158 TRP A CD2 1 ATOM 2193 N NE1 . TRP A 1 150 ? -4.575 6.833 30.769 1.00 13.28 ? 158 TRP A NE1 1 ATOM 2194 C CE2 . TRP A 1 150 ? -3.430 7.511 31.100 1.00 11.81 ? 158 TRP A CE2 1 ATOM 2195 C CE3 . TRP A 1 150 ? -1.533 7.220 32.575 1.00 12.02 ? 158 TRP A CE3 1 ATOM 2196 C CZ2 . TRP A 1 150 ? -2.975 8.756 30.685 1.00 11.76 ? 158 TRP A CZ2 1 ATOM 2197 C CZ3 . TRP A 1 150 ? -1.084 8.466 32.156 1.00 12.52 ? 158 TRP A CZ3 1 ATOM 2198 C CH2 . TRP A 1 150 ? -1.787 9.204 31.215 1.00 12.14 ? 158 TRP A CH2 1 ATOM 2199 H H . TRP A 1 150 ? -5.272 4.491 34.576 1.00 17.43 ? 158 TRP A H 1 ATOM 2200 H HA . TRP A 1 150 ? -4.537 3.119 32.383 1.00 17.30 ? 158 TRP A HA 1 ATOM 2201 H HB2 . TRP A 1 150 ? -2.963 4.754 34.060 1.00 17.04 ? 158 TRP A HB2 1 ATOM 2202 H HB3 . TRP A 1 150 ? -2.364 3.947 32.828 1.00 17.04 ? 158 TRP A HB3 1 ATOM 2203 H HD1 . TRP A 1 150 ? -5.263 5.007 31.385 1.00 16.61 ? 158 TRP A HD1 1 ATOM 2204 H HE1 . TRP A 1 150 ? -5.166 7.094 30.201 1.00 15.94 ? 158 TRP A HE1 1 ATOM 2205 H HE3 . TRP A 1 150 ? -1.053 6.727 33.201 1.00 14.42 ? 158 TRP A HE3 1 ATOM 2206 H HZ2 . TRP A 1 150 ? -3.447 9.261 30.062 1.00 14.11 ? 158 TRP A HZ2 1 ATOM 2207 H HZ3 . TRP A 1 150 ? -0.279 8.795 32.486 1.00 15.03 ? 158 TRP A HZ3 1 ATOM 2208 H HH2 . TRP A 1 150 ? -1.456 10.031 30.949 1.00 14.56 ? 158 TRP A HH2 1 ATOM 2209 N N . ARG A 1 151 ? -4.635 1.712 35.026 1.00 16.31 ? 159 ARG A N 1 ATOM 2210 C CA . ARG A 1 151 ? -4.304 0.526 35.803 1.00 17.89 ? 159 ARG A CA 1 ATOM 2211 C C . ARG A 1 151 ? -4.013 -0.727 34.983 1.00 17.94 ? 159 ARG A C 1 ATOM 2212 O O . ARG A 1 151 ? -3.069 -1.450 35.335 1.00 18.21 ? 159 ARG A O 1 ATOM 2213 C CB . ARG A 1 151 ? -5.431 0.280 36.814 1.00 21.66 ? 159 ARG A CB 1 ATOM 2214 C CG . ARG A 1 151 ? -5.248 -0.937 37.719 1.00 27.68 ? 159 ARG A CG 1 ATOM 2215 C CD . ARG A 1 151 ? -3.881 -0.985 38.365 1.00 32.78 ? 159 ARG A CD 1 ATOM 2216 N NE . ARG A 1 151 ? -3.884 -1.648 39.668 1.00 37.11 ? 159 ARG A NE 1 ATOM 2217 C CZ . ARG A 1 151 ? -2.909 -2.440 40.106 1.00 39.67 ? 159 ARG A CZ 1 ATOM 2218 N NH1 . ARG A 1 151 ? -1.855 -2.699 39.331 1.00 39.23 ? 159 ARG A NH1 1 ATOM 2219 N NH2 . ARG A 1 151 ? -2.993 -2.985 41.313 1.00 42.43 ? 159 ARG A NH2 1 ATOM 2220 H H . ARG A 1 151 ? -5.347 2.117 35.290 1.00 19.57 ? 159 ARG A H 1 ATOM 2221 H HA . ARG A 1 151 ? -3.503 0.719 36.314 1.00 21.47 ? 159 ARG A HA 1 ATOM 2222 H HB2 . ARG A 1 151 ? -5.504 1.059 37.387 1.00 25.99 ? 159 ARG A HB2 1 ATOM 2223 H HB3 . ARG A 1 151 ? -6.260 0.157 36.326 1.00 25.99 ? 159 ARG A HB3 1 ATOM 2224 H HG2 . ARG A 1 151 ? -5.912 -0.908 38.425 1.00 33.22 ? 159 ARG A HG2 1 ATOM 2225 H HG3 . ARG A 1 151 ? -5.359 -1.743 37.191 1.00 33.22 ? 159 ARG A HG3 1 ATOM 2226 H HD2 . ARG A 1 151 ? -3.275 -1.472 37.784 1.00 39.34 ? 159 ARG A HD2 1 ATOM 2227 H HD3 . ARG A 1 151 ? -3.560 -0.078 38.492 1.00 39.34 ? 159 ARG A HD3 1 ATOM 2228 H HE . ARG A 1 151 ? -4.570 -1.535 40.175 1.00 44.53 ? 159 ARG A HE 1 ATOM 2229 H HH11 . ARG A 1 151 ? -1.798 -2.343 38.550 1.00 47.08 ? 159 ARG A HH11 1 ATOM 2230 H HH12 . ARG A 1 151 ? -1.228 -3.215 39.615 1.00 47.08 ? 159 ARG A HH12 1 ATOM 2231 H HH21 . ARG A 1 151 ? -3.675 -2.824 41.811 1.00 50.92 ? 159 ARG A HH21 1 ATOM 2232 H HH22 . ARG A 1 151 ? -2.369 -3.506 41.594 1.00 50.92 ? 159 ARG A HH22 1 ATOM 2233 N N . PRO A 1 152 ? -4.741 -1.047 33.910 1.00 18.31 ? 160 PRO A N 1 ATOM 2234 C CA . PRO A 1 152 ? -4.406 -2.262 33.149 1.00 20.45 ? 160 PRO A CA 1 ATOM 2235 C C . PRO A 1 152 ? -3.011 -2.244 32.569 1.00 20.70 ? 160 PRO A C 1 ATOM 2236 O O . PRO A 1 152 ? -2.495 -3.296 32.171 1.00 23.24 ? 160 PRO A O 1 ATOM 2237 C CB . PRO A 1 152 ? -5.460 -2.279 32.037 1.00 23.32 ? 160 PRO A CB 1 ATOM 2238 C CG . PRO A 1 152 ? -6.577 -1.481 32.583 1.00 23.46 ? 160 PRO A CG 1 ATOM 2239 C CD . PRO A 1 152 ? -5.956 -0.403 33.391 1.00 20.50 ? 160 PRO A CD 1 ATOM 2240 H HA . PRO A 1 152 ? -4.513 -3.050 33.705 1.00 24.54 ? 160 PRO A HA 1 ATOM 2241 H HB2 . PRO A 1 152 ? -5.101 -1.867 31.236 1.00 27.99 ? 160 PRO A HB2 1 ATOM 2242 H HB3 . PRO A 1 152 ? -5.740 -3.191 31.862 1.00 27.99 ? 160 PRO A HB3 1 ATOM 2243 H HG2 . PRO A 1 152 ? -7.094 -1.105 31.854 1.00 28.16 ? 160 PRO A HG2 1 ATOM 2244 H HG3 . PRO A 1 152 ? -7.136 -2.045 33.140 1.00 28.16 ? 160 PRO A HG3 1 ATOM 2245 H HD2 . PRO A 1 152 ? -5.727 0.354 32.830 1.00 24.60 ? 160 PRO A HD2 1 ATOM 2246 H HD3 . PRO A 1 152 ? -6.542 -0.144 34.120 1.00 24.60 ? 160 PRO A HD3 1 ATOM 2247 N N . TRP A 1 153 ? -2.414 -1.069 32.447 1.00 20.17 ? 161 TRP A N 1 ATOM 2248 C CA . TRP A 1 153 ? -1.094 -0.884 31.878 1.00 20.40 ? 161 TRP A CA 1 ATOM 2249 C C . TRP A 1 153 ? 0.005 -0.778 32.932 1.00 21.44 ? 161 TRP A C 1 ATOM 2250 O O . TRP A 1 153 ? 1.186 -0.703 32.570 1.00 23.25 ? 161 TRP A O 1 ATOM 2251 C CB . TRP A 1 153 ? -1.095 0.391 31.039 1.00 20.48 ? 161 TRP A CB 1 ATOM 2252 C CG . TRP A 1 153 ? -2.076 0.426 29.873 1.00 21.55 ? 161 TRP A CG 1 ATOM 2253 C CD1 . TRP A 1 153 ? -2.544 -0.633 29.143 1.00 25.44 ? 161 TRP A CD1 1 ATOM 2254 C CD2 . TRP A 1 153 ? -2.685 1.598 29.320 1.00 20.89 ? 161 TRP A CD2 1 ATOM 2255 N NE1 . TRP A 1 153 ? -3.404 -0.181 28.165 1.00 25.03 ? 161 TRP A NE1 1 ATOM 2256 C CE2 . TRP A 1 153 ? -3.501 1.185 28.249 1.00 23.21 ? 161 TRP A CE2 1 ATOM 2257 C CE3 . TRP A 1 153 ? -2.604 2.959 29.614 1.00 20.20 ? 161 TRP A CE3 1 ATOM 2258 C CZ2 . TRP A 1 153 ? -4.231 2.087 27.485 1.00 22.20 ? 161 TRP A CZ2 1 ATOM 2259 C CZ3 . TRP A 1 153 ? -3.325 3.853 28.839 1.00 20.70 ? 161 TRP A CZ3 1 ATOM 2260 C CH2 . TRP A 1 153 ? -4.128 3.411 27.790 1.00 22.48 ? 161 TRP A CH2 1 ATOM 2261 H H . TRP A 1 153 ? -2.774 -0.330 32.701 1.00 24.21 ? 161 TRP A H 1 ATOM 2262 H HA . TRP A 1 153 ? -0.887 -1.633 31.297 1.00 24.48 ? 161 TRP A HA 1 ATOM 2263 H HB2 . TRP A 1 153 ? -1.311 1.137 31.620 1.00 24.57 ? 161 TRP A HB2 1 ATOM 2264 H HB3 . TRP A 1 153 ? -0.206 0.515 30.672 1.00 24.57 ? 161 TRP A HB3 1 ATOM 2265 H HD1 . TRP A 1 153 ? -2.319 -1.524 29.287 1.00 30.52 ? 161 TRP A HD1 1 ATOM 2266 H HE1 . TRP A 1 153 ? -3.813 -0.676 27.593 1.00 30.03 ? 161 TRP A HE1 1 ATOM 2267 H HE3 . TRP A 1 153 ? -2.059 3.262 30.304 1.00 24.25 ? 161 TRP A HE3 1 ATOM 2268 H HZ2 . TRP A 1 153 ? -4.771 1.797 26.786 1.00 26.65 ? 161 TRP A HZ2 1 ATOM 2269 H HZ3 . TRP A 1 153 ? -3.282 4.762 29.030 1.00 24.85 ? 161 TRP A HZ3 1 ATOM 2270 H HH2 . TRP A 1 153 ? -4.616 4.031 27.297 1.00 26.97 ? 161 TRP A HH2 1 ATOM 2271 N N . LEU A 1 154 ? -0.343 -0.773 34.219 1.00 21.30 ? 162 LEU A N 1 ATOM 2272 C CA . LEU A 1 154 ? 0.606 -0.495 35.287 1.00 21.48 ? 162 LEU A CA 1 ATOM 2273 C C . LEU A 1 154 ? 0.763 -1.698 36.204 1.00 21.96 ? 162 LEU A C 1 ATOM 2274 O O . LEU A 1 154 ? -0.226 -2.340 36.571 1.00 22.87 ? 162 LEU A O 1 ATOM 2275 C CB . LEU A 1 154 ? 0.107 0.684 36.132 1.00 19.02 ? 162 LEU A CB 1 ATOM 2276 C CG . LEU A 1 154 ? -0.166 1.999 35.407 1.00 18.28 ? 162 LEU A CG 1 ATOM 2277 C CD1 . LEU A 1 154 ? -0.787 3.015 36.344 1.00 19.36 ? 162 LEU A CD1 1 ATOM 2278 C CD2 . LEU A 1 154 ? 1.102 2.541 34.773 1.00 18.97 ? 162 LEU A CD2 1 ATOM 2279 H H . LEU A 1 154 ? -1.140 -0.932 34.501 1.00 25.57 ? 162 LEU A H 1 ATOM 2280 H HA . LEU A 1 154 ? 1.472 -0.269 34.911 1.00 25.78 ? 162 LEU A HA 1 ATOM 2281 H HB2 . LEU A 1 154 ? -0.722 0.417 36.559 1.00 22.83 ? 162 LEU A HB2 1 ATOM 2282 H HB3 . LEU A 1 154 ? 0.772 0.868 36.813 1.00 22.83 ? 162 LEU A HB3 1 ATOM 2283 H HG . LEU A 1 154 ? -0.802 1.832 34.694 1.00 21.93 ? 162 LEU A HG 1 ATOM 2284 H HD11 . LEU A 1 154 ? -0.948 3.838 35.855 1.00 23.23 ? 162 LEU A HD11 1 ATOM 2285 H HD12 . LEU A 1 154 ? -1.624 2.662 36.683 1.00 23.23 ? 162 LEU A HD12 1 ATOM 2286 H HD13 . LEU A 1 154 ? -0.176 3.181 37.079 1.00 23.23 ? 162 LEU A HD13 1 ATOM 2287 H HD21 . LEU A 1 154 ? 0.896 3.375 34.321 1.00 22.77 ? 162 LEU A HD21 1 ATOM 2288 H HD22 . LEU A 1 154 ? 1.761 2.694 35.467 1.00 22.77 ? 162 LEU A HD22 1 ATOM 2289 H HD23 . LEU A 1 154 ? 1.437 1.893 34.134 1.00 22.77 ? 162 LEU A HD23 1 ATOM 2290 N N . SER A 1 155 ? 2.011 -1.991 36.581 1.00 21.61 ? 163 SER A N 1 ATOM 2291 C CA . SER A 1 155 ? 2.275 -2.941 37.656 1.00 21.98 ? 163 SER A CA 1 ATOM 2292 C C . SER A 1 155 ? 1.762 -2.368 38.977 1.00 21.32 ? 163 SER A C 1 ATOM 2293 O O . SER A 1 155 ? 1.439 -1.181 39.084 1.00 20.30 ? 163 SER A O 1 ATOM 2294 C CB . SER A 1 155 ? 3.775 -3.187 37.805 1.00 21.58 ? 163 SER A CB 1 ATOM 2295 O OG . SER A 1 155 ? 4.413 -2.015 38.268 1.00 21.51 ? 163 SER A OG 1 ATOM 2296 H H . SER A 1 155 ? 2.719 -1.652 36.229 1.00 25.93 ? 163 SER A H 1 ATOM 2297 H HA . SER A 1 155 ? 1.828 -3.783 37.478 1.00 26.38 ? 163 SER A HA 1 ATOM 2298 H HB2 . SER A 1 155 ? 3.919 -3.902 38.444 1.00 25.90 ? 163 SER A HB2 1 ATOM 2299 H HB3 . SER A 1 155 ? 4.145 -3.431 36.942 1.00 25.90 ? 163 SER A HB3 1 ATOM 2300 H HG . SER A 1 155 ? 4.293 -1.388 37.722 1.00 25.81 ? 163 SER A HG 1 ATOM 2301 N N . ASN A 1 156 ? 1.689 -3.222 39.999 1.00 22.33 ? 164 ASN A N 1 ATOM 2302 C CA . ASN A 1 156 ? 1.280 -2.739 41.309 1.00 23.57 ? 164 ASN A CA 1 ATOM 2303 C C . ASN A 1 156 ? 2.199 -1.625 41.782 1.00 21.59 ? 164 ASN A C 1 ATOM 2304 O O . ASN A 1 156 ? 1.745 -0.624 42.349 1.00 22.20 ? 164 ASN A O 1 ATOM 2305 C CB . ASN A 1 156 ? 1.286 -3.896 42.301 1.00 27.96 ? 164 ASN A CB 1 ATOM 2306 C CG . ASN A 1 156 ? 0.137 -4.855 42.082 1.00 32.14 ? 164 ASN A CG 1 ATOM 2307 O OD1 . ASN A 1 156 ? -0.770 -4.575 41.302 1.00 32.59 ? 164 ASN A OD1 1 ATOM 2308 N ND2 . ASN A 1 156 ? 0.163 -5.994 42.786 1.00 35.67 ? 164 ASN A ND2 1 ATOM 2309 H H . ASN A 1 156 ? 1.866 -4.063 39.959 1.00 26.79 ? 164 ASN A H 1 ATOM 2310 H HA . ASN A 1 156 ? 0.377 -2.387 41.254 1.00 28.28 ? 164 ASN A HA 1 ATOM 2311 H HB2 . ASN A 1 156 ? 2.114 -4.391 42.205 1.00 33.55 ? 164 ASN A HB2 1 ATOM 2312 H HB3 . ASN A 1 156 ? 1.213 -3.541 43.201 1.00 33.55 ? 164 ASN A HB3 1 ATOM 2313 H HD21 . ASN A 1 156 ? -0.469 -6.571 42.694 1.00 42.80 ? 164 ASN A HD21 1 ATOM 2314 H HD22 . ASN A 1 156 ? 0.811 -6.150 43.329 1.00 42.80 ? 164 ASN A HD22 1 ATOM 2315 N N . GLU A 1 157 ? 3.502 -1.796 41.575 1.00 20.25 ? 165 GLU A N 1 ATOM 2316 C CA . GLU A 1 157 ? 4.450 -0.770 41.979 1.00 20.58 ? 165 GLU A CA 1 ATOM 2317 C C . GLU A 1 157 ? 4.190 0.528 41.239 1.00 19.49 ? 165 GLU A C 1 ATOM 2318 O O . GLU A 1 157 ? 4.181 1.603 41.843 1.00 18.94 ? 165 GLU A O 1 ATOM 2319 C CB . GLU A 1 157 ? 5.881 -1.249 41.737 1.00 22.59 ? 165 GLU A CB 1 ATOM 2320 C CG . GLU A 1 157 ? 6.908 -0.227 42.188 1.00 25.73 ? 165 GLU A CG 1 ATOM 2321 C CD . GLU A 1 157 ? 8.335 -0.670 41.946 1.00 30.21 ? 165 GLU A CD 1 ATOM 2322 O OE1 . GLU A 1 157 ? 8.535 -1.684 41.252 1.00 32.90 ? 165 GLU A OE1 1 ATOM 2323 O OE2 . GLU A 1 157 ? 9.256 0.017 42.436 1.00 33.18 ? 165 GLU A OE2 1 ATOM 2324 H H . GLU A 1 157 ? 3.856 -2.488 41.208 1.00 24.30 ? 165 GLU A H 1 ATOM 2325 H HA . GLU A 1 157 ? 4.347 -0.600 42.928 1.00 24.69 ? 165 GLU A HA 1 ATOM 2326 H HB2 . GLU A 1 157 ? 6.031 -2.068 42.235 1.00 27.10 ? 165 GLU A HB2 1 ATOM 2327 H HB3 . GLU A 1 157 ? 6.008 -1.406 40.789 1.00 27.10 ? 165 GLU A HB3 1 ATOM 2328 H HG2 . GLU A 1 157 ? 6.765 0.599 41.701 1.00 30.87 ? 165 GLU A HG2 1 ATOM 2329 H HG3 . GLU A 1 157 ? 6.800 -0.073 43.140 1.00 30.87 ? 165 GLU A HG3 1 ATOM 2330 N N . SER A 1 158 ? 3.980 0.444 39.928 1.00 17.61 ? 166 SER A N 1 ATOM 2331 C CA . SER A 1 158 ? 3.770 1.638 39.126 1.00 15.75 ? 166 SER A CA 1 ATOM 2332 C C . SER A 1 158 ? 2.459 2.332 39.448 1.00 16.43 ? 166 SER A C 1 ATOM 2333 O O . SER A 1 158 ? 2.398 3.564 39.424 1.00 16.17 ? 166 SER A O 1 ATOM 2334 C CB . SER A 1 158 ? 3.766 1.262 37.650 1.00 16.02 ? 166 SER A CB 1 ATOM 2335 O OG . SER A 1 158 ? 5.064 0.857 37.243 1.00 16.60 ? 166 SER A OG 1 ATOM 2336 H H . SER A 1 158 ? 3.954 -0.292 39.483 1.00 21.13 ? 166 SER A H 1 ATOM 2337 H HA . SER A 1 158 ? 4.495 2.263 39.282 1.00 18.90 ? 166 SER A HA 1 ATOM 2338 H HB2 . SER A 1 158 ? 3.146 0.529 37.510 1.00 19.22 ? 166 SER A HB2 1 ATOM 2339 H HB3 . SER A 1 158 ? 3.495 2.032 37.126 1.00 19.22 ? 166 SER A HB3 1 ATOM 2340 H HG . SER A 1 158 ? 5.058 0.650 36.429 1.00 19.92 ? 166 SER A HG 1 ATOM 2341 N N . TYR A 1 159 ? 1.424 1.560 39.774 1.00 16.80 ? 167 TYR A N 1 ATOM 2342 C CA . TYR A 1 159 ? 0.146 2.118 40.180 1.00 17.51 ? 167 TYR A CA 1 ATOM 2343 C C . TYR A 1 159 ? 0.311 2.959 41.436 1.00 18.40 ? 167 TYR A C 1 ATOM 2344 O O . TYR A 1 159 ? -0.174 4.097 41.497 1.00 18.28 ? 167 TYR A O 1 ATOM 2345 C CB . TYR A 1 159 ? -0.831 0.970 40.367 1.00 19.78 ? 167 TYR A CB 1 ATOM 2346 C CG . TYR A 1 159 ? -2.153 1.310 40.974 1.00 21.51 ? 167 TYR A CG 1 ATOM 2347 C CD1 . TYR A 1 159 ? -3.116 2.014 40.268 1.00 21.70 ? 167 TYR A CD1 1 ATOM 2348 C CD2 . TYR A 1 159 ? -2.469 0.867 42.250 1.00 24.59 ? 167 TYR A CD2 1 ATOM 2349 C CE1 . TYR A 1 159 ? -4.360 2.287 40.845 1.00 23.13 ? 167 TYR A CE1 1 ATOM 2350 C CE2 . TYR A 1 159 ? -3.684 1.136 42.816 1.00 26.39 ? 167 TYR A CE2 1 ATOM 2351 C CZ . TYR A 1 159 ? -4.621 1.842 42.120 1.00 26.55 ? 167 TYR A CZ 1 ATOM 2352 O OH . TYR A 1 159 ? -5.833 2.080 42.726 1.00 30.34 ? 167 TYR A OH 1 ATOM 2353 H H . TYR A 1 159 ? 1.441 0.700 39.768 1.00 20.16 ? 167 TYR A H 1 ATOM 2354 H HA . TYR A 1 159 ? -0.191 2.691 39.474 1.00 21.01 ? 167 TYR A HA 1 ATOM 2355 H HB2 . TYR A 1 159 ? -1.007 0.577 39.497 1.00 23.73 ? 167 TYR A HB2 1 ATOM 2356 H HB3 . TYR A 1 159 ? -0.414 0.307 40.939 1.00 23.73 ? 167 TYR A HB3 1 ATOM 2357 H HD1 . TYR A 1 159 ? -2.932 2.310 39.406 1.00 26.04 ? 167 TYR A HD1 1 ATOM 2358 H HD2 . TYR A 1 159 ? -1.838 0.384 42.733 1.00 29.51 ? 167 TYR A HD2 1 ATOM 2359 H HE1 . TYR A 1 159 ? -5.003 2.767 40.373 1.00 27.76 ? 167 TYR A HE1 1 ATOM 2360 H HE2 . TYR A 1 159 ? -3.872 0.837 43.676 1.00 31.67 ? 167 TYR A HE2 1 ATOM 2361 H HH . TYR A 1 159 ? -6.333 2.512 42.208 1.00 36.41 ? 167 TYR A HH 1 ATOM 2362 N N . ALA A 1 160 ? 1.034 2.431 42.437 1.00 19.30 ? 168 ALA A N 1 ATOM 2363 C CA . ALA A 1 160 ? 1.303 3.203 43.649 1.00 20.33 ? 168 ALA A CA 1 ATOM 2364 C C . ALA A 1 160 ? 2.141 4.443 43.350 1.00 18.71 ? 168 ALA A C 1 ATOM 2365 O O . ALA A 1 160 ? 1.833 5.539 43.828 1.00 19.39 ? 168 ALA A O 1 ATOM 2366 C CB . ALA A 1 160 ? 1.965 2.320 44.712 1.00 22.62 ? 168 ALA A CB 1 ATOM 2367 H H . ALA A 1 160 ? 1.372 1.640 42.434 1.00 23.16 ? 168 ALA A H 1 ATOM 2368 H HA . ALA A 1 160 ? 0.457 3.507 44.011 1.00 24.39 ? 168 ALA A HA 1 ATOM 2369 H HB1 . ALA A 1 160 ? 2.133 2.853 45.505 1.00 27.15 ? 168 ALA A HB1 1 ATOM 2370 H HB2 . ALA A 1 160 ? 1.369 1.586 44.928 1.00 27.15 ? 168 ALA A HB2 1 ATOM 2371 H HB3 . ALA A 1 160 ? 2.801 1.976 44.361 1.00 27.15 ? 168 ALA A HB3 1 ATOM 2372 N N . LEU A 1 161 ? 3.187 4.311 42.529 1.00 18.10 ? 169 LEU A N 1 ATOM 2373 C CA . LEU A 1 161 ? 3.987 5.489 42.202 1.00 18.41 ? 169 LEU A CA 1 ATOM 2374 C C . LEU A 1 161 ? 3.167 6.520 41.452 1.00 16.55 ? 169 LEU A C 1 ATOM 2375 O O . LEU A 1 161 ? 3.342 7.731 41.646 1.00 16.72 ? 169 LEU A O 1 ATOM 2376 C CB . LEU A 1 161 ? 5.212 5.111 41.373 1.00 17.99 ? 169 LEU A CB 1 ATOM 2377 C CG . LEU A 1 161 ? 6.363 4.486 42.143 1.00 19.58 ? 169 LEU A CG 1 ATOM 2378 C CD1 . LEU A 1 161 ? 7.393 3.937 41.190 1.00 20.52 ? 169 LEU A CD1 1 ATOM 2379 C CD2 . LEU A 1 161 ? 7.008 5.489 43.097 1.00 22.41 ? 169 LEU A CD2 1 ATOM 2380 H H . LEU A 1 161 ? 3.446 3.577 42.163 1.00 21.72 ? 169 LEU A H 1 ATOM 2381 H HA . LEU A 1 161 ? 4.297 5.897 43.025 1.00 22.10 ? 169 LEU A HA 1 ATOM 2382 H HB2 . LEU A 1 161 ? 4.938 4.474 40.694 1.00 21.59 ? 169 LEU A HB2 1 ATOM 2383 H HB3 . LEU A 1 161 ? 5.552 5.913 40.945 1.00 21.59 ? 169 LEU A HB3 1 ATOM 2384 H HG . LEU A 1 161 ? 6.022 3.748 42.672 1.00 23.50 ? 169 LEU A HG 1 ATOM 2385 H HD11 . LEU A 1 161 ? 8.117 3.543 41.701 1.00 24.62 ? 169 LEU A HD11 1 ATOM 2386 H HD12 . LEU A 1 161 ? 6.977 3.262 40.631 1.00 24.62 ? 169 LEU A HD12 1 ATOM 2387 H HD13 . LEU A 1 161 ? 7.731 4.661 40.640 1.00 24.62 ? 169 LEU A HD13 1 ATOM 2388 H HD21 . LEU A 1 161 ? 7.735 5.054 43.568 1.00 26.89 ? 169 LEU A HD21 1 ATOM 2389 H HD22 . LEU A 1 161 ? 7.347 6.239 42.584 1.00 26.89 ? 169 LEU A HD22 1 ATOM 2390 H HD23 . LEU A 1 161 ? 6.340 5.797 43.730 1.00 26.89 ? 169 LEU A HD23 1 ATOM 2391 N N . PHE A 1 162 ? 2.302 6.070 40.547 1.00 15.63 ? 170 PHE A N 1 ATOM 2392 C CA . PHE A 1 162 ? 1.559 7.029 39.740 1.00 14.04 ? 170 PHE A CA 1 ATOM 2393 C C . PHE A 1 162 ? 0.658 7.884 40.612 1.00 13.65 ? 170 PHE A C 1 ATOM 2394 O O . PHE A 1 162 ? 0.573 9.098 40.416 1.00 13.15 ? 170 PHE A O 1 ATOM 2395 C CB . PHE A 1 162 ? 0.725 6.313 38.678 1.00 14.76 ? 170 PHE A CB 1 ATOM 2396 C CG . PHE A 1 162 ? 0.253 7.241 37.603 1.00 13.06 ? 170 PHE A CG 1 ATOM 2397 C CD1 . PHE A 1 162 ? -0.795 8.126 37.818 1.00 13.64 ? 170 PHE A CD1 1 ATOM 2398 C CD2 . PHE A 1 162 ? 0.944 7.318 36.404 1.00 13.71 ? 170 PHE A CD2 1 ATOM 2399 C CE1 . PHE A 1 162 ? -1.178 9.010 36.834 1.00 14.05 ? 170 PHE A CE1 1 ATOM 2400 C CE2 . PHE A 1 162 ? 0.585 8.232 35.439 1.00 14.39 ? 170 PHE A CE2 1 ATOM 2401 C CZ . PHE A 1 162 ? -0.481 9.079 35.660 1.00 13.50 ? 170 PHE A CZ 1 ATOM 2402 H H . PHE A 1 162 ? 2.132 5.243 40.385 1.00 18.75 ? 170 PHE A H 1 ATOM 2403 H HA . PHE A 1 162 ? 2.185 7.616 39.287 1.00 16.85 ? 170 PHE A HA 1 ATOM 2404 H HB2 . PHE A 1 162 ? 1.264 5.622 38.264 1.00 17.72 ? 170 PHE A HB2 1 ATOM 2405 H HB3 . PHE A 1 162 ? -0.055 5.920 39.100 1.00 17.72 ? 170 PHE A HB3 1 ATOM 2406 H HD1 . PHE A 1 162 ? -1.265 8.098 38.619 1.00 16.37 ? 170 PHE A HD1 1 ATOM 2407 H HD2 . PHE A 1 162 ? 1.674 6.761 36.259 1.00 16.46 ? 170 PHE A HD2 1 ATOM 2408 H HE1 . PHE A 1 162 ? -1.891 9.588 36.983 1.00 16.86 ? 170 PHE A HE1 1 ATOM 2409 H HE2 . PHE A 1 162 ? 1.042 8.258 34.629 1.00 17.27 ? 170 PHE A HE2 1 ATOM 2410 H HZ . PHE A 1 162 ? -0.748 9.671 34.995 1.00 16.20 ? 170 PHE A HZ 1 ATOM 2411 N N . LYS A 1 163 ? 0.007 7.272 41.607 1.00 14.02 ? 171 LYS A N 1 ATOM 2412 C CA . LYS A 1 163 ? -0.858 8.036 42.497 1.00 15.52 ? 171 LYS A CA 1 ATOM 2413 C C . LYS A 1 163 ? -0.112 9.146 43.212 1.00 15.48 ? 171 LYS A C 1 ATOM 2414 O O . LYS A 1 163 ? -0.704 10.194 43.489 1.00 17.03 ? 171 LYS A O 1 ATOM 2415 C CB . LYS A 1 163 ? -1.534 7.123 43.511 1.00 16.55 ? 171 LYS A CB 1 ATOM 2416 C CG . LYS A 1 163 ? -2.539 6.196 42.825 1.00 18.85 ? 171 LYS A CG 1 ATOM 2417 C CD . LYS A 1 163 ? -3.478 5.524 43.756 1.00 25.87 ? 171 LYS A CD 1 ATOM 2418 C CE . LYS A 1 163 ? -2.809 4.453 44.542 1.00 31.70 ? 171 LYS A CE 1 ATOM 2419 N NZ . LYS A 1 163 ? -3.813 3.850 45.473 1.00 35.68 ? 171 LYS A NZ 1 ATOM 2420 H H . LYS A 1 163 ? 0.051 6.431 41.782 1.00 16.82 ? 171 LYS A H 1 ATOM 2421 H HA . LYS A 1 163 ? -1.556 8.450 41.966 1.00 18.63 ? 171 LYS A HA 1 ATOM 2422 H HB2 . LYS A 1 163 ? -0.864 6.576 43.949 1.00 19.86 ? 171 LYS A HB2 1 ATOM 2423 H HB3 . LYS A 1 163 ? -2.010 7.661 44.162 1.00 19.86 ? 171 LYS A HB3 1 ATOM 2424 H HG2 . LYS A 1 163 ? -3.066 6.716 42.199 1.00 22.62 ? 171 LYS A HG2 1 ATOM 2425 H HG3 . LYS A 1 163 ? -2.052 5.506 42.348 1.00 22.62 ? 171 LYS A HG3 1 ATOM 2426 H HD2 . LYS A 1 163 ? -3.833 6.178 44.377 1.00 31.04 ? 171 LYS A HD2 1 ATOM 2427 H HD3 . LYS A 1 163 ? -4.198 5.120 43.247 1.00 31.04 ? 171 LYS A HD3 1 ATOM 2428 H HE2 . LYS A 1 163 ? -2.481 3.762 43.946 1.00 38.04 ? 171 LYS A HE2 1 ATOM 2429 H HE3 . LYS A 1 163 ? -2.085 4.831 45.065 1.00 38.04 ? 171 LYS A HE3 1 ATOM 2430 H HZ1 . LYS A 1 163 ? -3.432 3.205 45.955 1.00 42.81 ? 171 LYS A HZ1 1 ATOM 2431 H HZ2 . LYS A 1 163 ? -4.130 4.473 46.024 1.00 42.81 ? 171 LYS A HZ2 1 ATOM 2432 H HZ3 . LYS A 1 163 ? -4.488 3.504 45.009 1.00 42.81 ? 171 LYS A HZ3 1 ATOM 2433 N N . ARG A 1 164 ? 1.171 8.943 43.515 1.00 16.43 ? 172 ARG A N 1 ATOM 2434 C CA . ARG A 1 164 ? 1.936 9.934 44.259 1.00 17.94 ? 172 ARG A CA 1 ATOM 2435 C C . ARG A 1 164 ? 2.515 11.038 43.378 1.00 17.06 ? 172 ARG A C 1 ATOM 2436 O O . ARG A 1 164 ? 2.603 12.191 43.817 1.00 18.68 ? 172 ARG A O 1 ATOM 2437 C CB . ARG A 1 164 ? 3.067 9.223 44.983 1.00 21.66 ? 172 ARG A CB 1 ATOM 2438 C CG . ARG A 1 164 ? 2.563 8.499 46.198 1.00 28.62 ? 172 ARG A CG 1 ATOM 2439 C CD . ARG A 1 164 ? 3.449 7.336 46.621 1.00 37.04 ? 172 ARG A CD 1 ATOM 2440 N NE . ARG A 1 164 ? 4.868 7.666 46.719 1.00 42.53 ? 172 ARG A NE 1 ATOM 2441 C CZ . ARG A 1 164 ? 5.845 6.766 46.582 1.00 47.63 ? 172 ARG A CZ 1 ATOM 2442 N NH1 . ARG A 1 164 ? 5.550 5.492 46.324 1.00 49.37 ? 172 ARG A NH1 1 ATOM 2443 N NH2 . ARG A 1 164 ? 7.119 7.132 46.687 1.00 49.05 ? 172 ARG A NH2 1 ATOM 2444 H H . ARG A 1 164 ? 1.617 8.240 43.302 1.00 19.71 ? 172 ARG A H 1 ATOM 2445 H HA . ARG A 1 164 ? 1.363 10.347 44.923 1.00 21.53 ? 172 ARG A HA 1 ATOM 2446 H HB2 . ARG A 1 164 ? 3.472 8.574 44.388 1.00 25.99 ? 172 ARG A HB2 1 ATOM 2447 H HB3 . ARG A 1 164 ? 3.726 9.876 45.269 1.00 25.99 ? 172 ARG A HB3 1 ATOM 2448 H HG2 . ARG A 1 164 ? 2.518 9.124 46.939 1.00 34.35 ? 172 ARG A HG2 1 ATOM 2449 H HG3 . ARG A 1 164 ? 1.679 8.147 46.009 1.00 34.35 ? 172 ARG A HG3 1 ATOM 2450 H HD2 . ARG A 1 164 ? 3.157 7.024 47.492 1.00 44.45 ? 172 ARG A HD2 1 ATOM 2451 H HD3 . ARG A 1 164 ? 3.356 6.623 45.970 1.00 44.45 ? 172 ARG A HD3 1 ATOM 2452 H HE . ARG A 1 164 ? 5.087 8.498 46.741 1.00 51.03 ? 172 ARG A HE 1 ATOM 2453 H HH11 . ARG A 1 164 ? 4.728 5.246 46.254 1.00 59.25 ? 172 ARG A HH11 1 ATOM 2454 H HH12 . ARG A 1 164 ? 6.180 4.914 46.233 1.00 59.25 ? 172 ARG A HH12 1 ATOM 2455 H HH21 . ARG A 1 164 ? 7.319 7.952 46.850 1.00 58.86 ? 172 ARG A HH21 1 ATOM 2456 H HH22 . ARG A 1 164 ? 7.743 6.548 46.593 1.00 58.86 ? 172 ARG A HH22 1 ATOM 2457 N N . GLY A 1 165 ? 2.943 10.717 42.156 1.00 15.43 ? 173 GLY A N 1 ATOM 2458 C CA . GLY A 1 165 ? 3.697 11.679 41.378 1.00 14.63 ? 173 GLY A CA 1 ATOM 2459 C C . GLY A 1 165 ? 3.515 11.587 39.872 1.00 13.57 ? 173 GLY A C 1 ATOM 2460 O O . GLY A 1 165 ? 4.145 12.349 39.155 1.00 13.53 ? 173 GLY A O 1 ATOM 2461 H H . GLY A 1 165 ? 2.809 9.963 41.766 1.00 18.52 ? 173 GLY A H 1 ATOM 2462 H HA2 . GLY A 1 165 ? 3.441 12.574 41.654 1.00 17.55 ? 173 GLY A HA2 1 ATOM 2463 H HA3 . GLY A 1 165 ? 4.641 11.566 41.571 1.00 17.55 ? 173 GLY A HA3 1 ATOM 2464 N N . ALA A 1 166 ? 2.694 10.666 39.380 1.00 13.46 ? 174 ALA A N 1 ATOM 2465 C CA . ALA A 1 166 ? 2.475 10.493 37.940 1.00 13.30 ? 174 ALA A CA 1 ATOM 2466 C C . ALA A 1 166 ? 3.756 10.135 37.200 1.00 12.82 ? 174 ALA A C 1 ATOM 2467 O O . ALA A 1 166 ? 3.944 10.530 36.052 1.00 12.54 ? 174 ALA A O 1 ATOM 2468 C CB . ALA A 1 166 ? 1.758 11.695 37.312 1.00 13.24 ? 174 ALA A CB 1 ATOM 2469 H H . ALA A 1 166 ? 2.243 10.118 39.865 1.00 16.16 ? 174 ALA A H 1 ATOM 2470 H HA . ALA A 1 166 ? 1.879 9.736 37.830 1.00 15.96 ? 174 ALA A HA 1 ATOM 2471 H HB1 . ALA A 1 166 ? 1.638 11.531 36.363 1.00 15.89 ? 174 ALA A HB1 1 ATOM 2472 H HB2 . ALA A 1 166 ? 0.895 11.807 37.740 1.00 15.89 ? 174 ALA A HB2 1 ATOM 2473 H HB3 . ALA A 1 166 ? 2.299 12.489 37.444 1.00 15.89 ? 174 ALA A HB3 1 ATOM 2474 N N . PHE A 1 167 ? 4.640 9.375 37.847 1.00 12.06 ? 175 PHE A N 1 ATOM 2475 C CA . PHE A 1 167 ? 5.826 8.828 37.214 1.00 11.82 ? 175 PHE A CA 1 ATOM 2476 C C . PHE A 1 167 ? 6.022 7.396 37.692 1.00 11.92 ? 175 PHE A C 1 ATOM 2477 O O . PHE A 1 167 ? 5.533 7.026 38.754 1.00 13.90 ? 175 PHE A O 1 ATOM 2478 C CB . PHE A 1 167 ? 7.055 9.718 37.426 1.00 12.85 ? 175 PHE A CB 1 ATOM 2479 C CG . PHE A 1 167 ? 7.512 9.892 38.873 1.00 13.05 ? 175 PHE A CG 1 ATOM 2480 C CD1 . PHE A 1 167 ? 8.300 8.941 39.495 1.00 15.07 ? 175 PHE A CD1 1 ATOM 2481 C CD2 . PHE A 1 167 ? 7.244 11.065 39.544 1.00 13.09 ? 175 PHE A CD2 1 ATOM 2482 C CE1 . PHE A 1 167 ? 8.783 9.150 40.784 1.00 15.19 ? 175 PHE A CE1 1 ATOM 2483 C CE2 . PHE A 1 167 ? 7.726 11.286 40.831 1.00 14.42 ? 175 PHE A CE2 1 ATOM 2484 C CZ . PHE A 1 167 ? 8.496 10.315 41.446 1.00 14.97 ? 175 PHE A CZ 1 ATOM 2485 H H . PHE A 1 167 ? 4.566 9.161 38.677 1.00 14.47 ? 175 PHE A H 1 ATOM 2486 H HA . PHE A 1 167 ? 5.666 8.789 36.258 1.00 14.18 ? 175 PHE A HA 1 ATOM 2487 H HB2 . PHE A 1 167 ? 7.797 9.335 36.932 1.00 15.42 ? 175 PHE A HB2 1 ATOM 2488 H HB3 . PHE A 1 167 ? 6.856 10.601 37.076 1.00 15.42 ? 175 PHE A HB3 1 ATOM 2489 H HD1 . PHE A 1 167 ? 8.512 8.154 39.047 1.00 18.09 ? 175 PHE A HD1 1 ATOM 2490 H HD2 . PHE A 1 167 ? 6.740 11.725 39.126 1.00 15.70 ? 175 PHE A HD2 1 ATOM 2491 H HE1 . PHE A 1 167 ? 9.294 8.494 41.200 1.00 18.22 ? 175 PHE A HE1 1 ATOM 2492 H HE2 . PHE A 1 167 ? 7.518 12.074 41.279 1.00 17.30 ? 175 PHE A HE2 1 ATOM 2493 H HZ . PHE A 1 167 ? 8.800 10.444 42.315 1.00 17.96 ? 175 PHE A HZ 1 ATOM 2494 N N . TYR A 1 168 ? 6.671 6.577 36.855 1.00 12.09 ? 176 TYR A N 1 ATOM 2495 C CA . TYR A 1 168 ? 6.789 5.148 37.114 1.00 11.86 ? 176 TYR A CA 1 ATOM 2496 C C . TYR A 1 168 ? 7.718 4.530 36.083 1.00 12.09 ? 176 TYR A C 1 ATOM 2497 O O . TYR A 1 168 ? 8.108 5.172 35.109 1.00 12.88 ? 176 TYR A O 1 ATOM 2498 C CB . TYR A 1 168 ? 5.416 4.464 37.072 1.00 13.35 ? 176 TYR A CB 1 ATOM 2499 C CG . TYR A 1 168 ? 4.746 4.501 35.718 1.00 12.58 ? 176 TYR A CG 1 ATOM 2500 C CD1 . TYR A 1 168 ? 4.013 5.594 35.329 1.00 13.51 ? 176 TYR A CD1 1 ATOM 2501 C CD2 . TYR A 1 168 ? 4.850 3.446 34.842 1.00 13.50 ? 176 TYR A CD2 1 ATOM 2502 C CE1 . TYR A 1 168 ? 3.372 5.642 34.090 1.00 14.78 ? 176 TYR A CE1 1 ATOM 2503 C CE2 . TYR A 1 168 ? 4.225 3.492 33.600 1.00 15.15 ? 176 TYR A CE2 1 ATOM 2504 C CZ . TYR A 1 168 ? 3.481 4.595 33.246 1.00 15.22 ? 176 TYR A CZ 1 ATOM 2505 O OH . TYR A 1 168 ? 2.865 4.653 32.025 1.00 17.77 ? 176 TYR A OH 1 ATOM 2506 H H . TYR A 1 168 ? 7.053 6.833 36.128 1.00 14.50 ? 176 TYR A H 1 ATOM 2507 H HA . TYR A 1 168 ? 7.172 5.010 37.994 1.00 14.23 ? 176 TYR A HA 1 ATOM 2508 H HB2 . TYR A 1 168 ? 5.525 3.533 37.322 1.00 16.01 ? 176 TYR A HB2 1 ATOM 2509 H HB3 . TYR A 1 168 ? 4.829 4.907 37.704 1.00 16.01 ? 176 TYR A HB3 1 ATOM 2510 H HD1 . TYR A 1 168 ? 3.927 6.314 35.912 1.00 16.21 ? 176 TYR A HD1 1 ATOM 2511 H HD2 . TYR A 1 168 ? 5.343 2.695 35.081 1.00 16.20 ? 176 TYR A HD2 1 ATOM 2512 H HE1 . TYR A 1 168 ? 2.878 6.392 33.846 1.00 17.74 ? 176 TYR A HE1 1 ATOM 2513 H HE2 . TYR A 1 168 ? 4.296 2.772 33.015 1.00 18.19 ? 176 TYR A HE2 1 ATOM 2514 H HH . TYR A 1 168 ? 2.463 5.386 31.940 1.00 21.33 ? 176 TYR A HH 1 ATOM 2515 N N . SER A 1 169 ? 8.081 3.274 36.294 1.00 13.64 ? 177 SER A N 1 ATOM 2516 C CA A SER A 1 169 ? 8.859 2.558 35.293 0.73 14.71 ? 177 SER A CA 1 ATOM 2517 C CA B SER A 1 169 ? 8.873 2.556 35.311 0.27 14.74 ? 177 SER A CA 1 ATOM 2518 C C . SER A 1 169 ? 8.330 1.140 35.183 1.00 15.11 ? 177 SER A C 1 ATOM 2519 O O . SER A 1 169 ? 7.822 0.574 36.148 1.00 18.88 ? 177 SER A O 1 ATOM 2520 C CB A SER A 1 169 ? 10.370 2.549 35.559 0.73 16.05 ? 177 SER A CB 1 ATOM 2521 C CB B SER A 1 169 ? 10.346 2.559 35.752 0.27 15.48 ? 177 SER A CB 1 ATOM 2522 O OG A SER A 1 169 ? 10.761 1.427 36.330 0.73 17.23 ? 177 SER A OG 1 ATOM 2523 O OG B SER A 1 169 ? 11.205 1.941 34.824 0.27 15.19 ? 177 SER A OG 1 ATOM 2524 H H . SER A 1 169 ? 7.889 2.814 36.995 1.00 16.37 ? 177 SER A H 1 ATOM 2525 H HA . SER A 1 169 ? 8.761 2.993 34.442 1.00 17.68 ? 177 SER A HA 1 ATOM 2526 H HB2 A SER A 1 169 ? 10.837 2.523 34.709 0.73 19.26 ? 177 SER A HB2 1 ATOM 2527 H HB2 B SER A 1 169 ? 10.630 3.480 35.869 0.27 18.58 ? 177 SER A HB2 1 ATOM 2528 H HB3 A SER A 1 169 ? 10.608 3.357 36.040 0.73 19.26 ? 177 SER A HB3 1 ATOM 2529 H HB3 B SER A 1 169 ? 10.416 2.089 36.597 0.27 18.58 ? 177 SER A HB3 1 ATOM 2530 H HG A SER A 1 169 ? 10.366 1.436 37.072 0.73 20.67 ? 177 SER A HG 1 ATOM 2531 H HG B SER A 1 169 ? 11.165 2.340 34.085 0.27 18.22 ? 177 SER A HG 1 ATOM 2532 N N . GLU A 1 170 ? 8.447 0.580 33.985 1.00 15.71 ? 178 GLU A N 1 ATOM 2533 C CA . GLU A 1 170 ? 7.857 -0.705 33.604 1.00 18.76 ? 178 GLU A CA 1 ATOM 2534 C C . GLU A 1 170 ? 8.855 -1.516 32.802 1.00 18.92 ? 178 GLU A C 1 ATOM 2535 O O . GLU A 1 170 ? 9.521 -0.989 31.919 1.00 20.35 ? 178 GLU A O 1 ATOM 2536 C CB . GLU A 1 170 ? 6.608 -0.527 32.709 1.00 22.44 ? 178 GLU A CB 1 ATOM 2537 C CG . GLU A 1 170 ? 5.378 -0.050 33.423 1.00 23.65 ? 178 GLU A CG 1 ATOM 2538 C CD . GLU A 1 170 ? 4.697 -1.131 34.244 1.00 22.45 ? 178 GLU A CD 1 ATOM 2539 O OE1 . GLU A 1 170 ? 4.578 -2.285 33.787 1.00 25.15 ? 178 GLU A OE1 1 ATOM 2540 O OE2 . GLU A 1 170 ? 4.272 -0.818 35.361 1.00 21.84 ? 178 GLU A OE2 1 ATOM 2541 H H . GLU A 1 170 ? 8.887 0.943 33.341 1.00 18.85 ? 178 GLU A H 1 ATOM 2542 H HA . GLU A 1 170 ? 7.609 -1.204 34.398 1.00 22.52 ? 178 GLU A HA 1 ATOM 2543 H HB2 . GLU A 1 170 ? 6.814 0.121 32.017 1.00 26.93 ? 178 GLU A HB2 1 ATOM 2544 H HB3 . GLU A 1 170 ? 6.396 -1.382 32.302 1.00 26.93 ? 178 GLU A HB3 1 ATOM 2545 H HG2 . GLU A 1 170 ? 5.624 0.670 34.025 1.00 28.38 ? 178 GLU A HG2 1 ATOM 2546 H HG3 . GLU A 1 170 ? 4.739 0.272 32.767 1.00 28.38 ? 178 GLU A HG3 1 ATOM 2547 N N . LYS A 1 171 ? 8.916 -2.813 33.069 1.00 20.74 ? 179 LYS A N 1 ATOM 2548 C CA . LYS A 1 171 ? 9.730 -3.703 32.253 1.00 23.76 ? 179 LYS A CA 1 ATOM 2549 C C . LYS A 1 171 ? 8.997 -3.994 30.949 1.00 26.17 ? 179 LYS A C 1 ATOM 2550 O O . LYS A 1 171 ? 7.817 -4.343 30.963 1.00 30.45 ? 179 LYS A O 1 ATOM 2551 C CB . LYS A 1 171 ? 9.990 -5.003 33.030 1.00 26.88 ? 179 LYS A CB 1 ATOM 2552 C CG . LYS A 1 171 ? 11.017 -5.913 32.389 1.00 33.38 ? 179 LYS A CG 1 ATOM 2553 C CD . LYS A 1 171 ? 11.852 -6.691 33.423 1.00 37.77 ? 179 LYS A CD 1 ATOM 2554 C CE . LYS A 1 171 ? 13.165 -7.204 32.808 1.00 40.48 ? 179 LYS A CE 1 ATOM 2555 N NZ . LYS A 1 171 ? 13.728 -6.281 31.748 1.00 40.92 ? 179 LYS A NZ 1 ATOM 2556 H H . LYS A 1 171 ? 8.498 -3.202 33.712 1.00 24.89 ? 179 LYS A H 1 ATOM 2557 H HA . LYS A 1 171 ? 10.579 -3.281 32.050 1.00 28.51 ? 179 LYS A HA 1 ATOM 2558 H HB2 . LYS A 1 171 ? 10.308 -4.777 33.918 1.00 32.26 ? 179 LYS A HB2 1 ATOM 2559 H HB3 . LYS A 1 171 ? 9.158 -5.498 33.097 1.00 32.26 ? 179 LYS A HB3 1 ATOM 2560 H HG2 . LYS A 1 171 ? 10.561 -6.557 31.826 1.00 40.06 ? 179 LYS A HG2 1 ATOM 2561 H HG3 . LYS A 1 171 ? 11.624 -5.377 31.855 1.00 40.06 ? 179 LYS A HG3 1 ATOM 2562 H HD2 . LYS A 1 171 ? 12.072 -6.106 34.164 1.00 45.32 ? 179 LYS A HD2 1 ATOM 2563 H HD3 . LYS A 1 171 ? 11.344 -7.455 33.736 1.00 45.32 ? 179 LYS A HD3 1 ATOM 2564 H HE2 . LYS A 1 171 ? 13.828 -7.292 33.510 1.00 48.58 ? 179 LYS A HE2 1 ATOM 2565 H HE3 . LYS A 1 171 ? 13.003 -8.067 32.397 1.00 48.58 ? 179 LYS A HE3 1 ATOM 2566 H HZ1 . LYS A 1 171 ? 14.484 -6.618 31.423 1.00 49.11 ? 179 LYS A HZ1 1 ATOM 2567 H HZ2 . LYS A 1 171 ? 13.142 -6.188 31.084 1.00 49.11 ? 179 LYS A HZ2 1 ATOM 2568 H HZ3 . LYS A 1 171 ? 13.895 -5.481 32.100 1.00 49.11 ? 179 LYS A HZ3 1 ATOM 2569 N N . LEU A 1 172 ? 9.682 -3.840 29.824 1.00 23.33 ? 180 LEU A N 1 ATOM 2570 C CA . LEU A 1 172 ? 9.107 -4.242 28.550 1.00 25.32 ? 180 LEU A CA 1 ATOM 2571 C C . LEU A 1 172 ? 8.875 -5.755 28.545 1.00 30.14 ? 180 LEU A C 1 ATOM 2572 O O . LEU A 1 172 ? 9.738 -6.525 28.984 1.00 30.92 ? 180 LEU A O 1 ATOM 2573 C CB . LEU A 1 172 ? 10.039 -3.883 27.396 1.00 23.72 ? 180 LEU A CB 1 ATOM 2574 C CG . LEU A 1 172 ? 10.151 -2.412 27.023 1.00 23.72 ? 180 LEU A CG 1 ATOM 2575 C CD1 . LEU A 1 172 ? 11.104 -2.287 25.859 1.00 24.21 ? 180 LEU A CD1 1 ATOM 2576 C CD2 . LEU A 1 172 ? 8.790 -1.780 26.676 1.00 25.57 ? 180 LEU A CD2 1 ATOM 2577 H H . LEU A 1 172 ? 10.474 -3.508 29.771 1.00 28.00 ? 180 LEU A H 1 ATOM 2578 H HA . LEU A 1 172 ? 8.256 -3.794 28.417 1.00 30.38 ? 180 LEU A HA 1 ATOM 2579 H HB2 . LEU A 1 172 ? 10.931 -4.188 27.624 1.00 28.46 ? 180 LEU A HB2 1 ATOM 2580 H HB3 . LEU A 1 172 ? 9.734 -4.355 26.605 1.00 28.46 ? 180 LEU A HB3 1 ATOM 2581 H HG . LEU A 1 172 ? 10.527 -1.924 27.772 1.00 28.46 ? 180 LEU A HG 1 ATOM 2582 H HD11 . LEU A 1 172 ? 11.182 -1.352 25.614 1.00 29.05 ? 180 LEU A HD11 1 ATOM 2583 H HD12 . LEU A 1 172 ? 11.971 -2.634 26.123 1.00 29.05 ? 180 LEU A HD12 1 ATOM 2584 H HD13 . LEU A 1 172 ? 10.757 -2.798 25.111 1.00 29.05 ? 180 LEU A HD13 1 ATOM 2585 H HD21 . LEU A 1 172 ? 8.925 -0.847 26.448 1.00 30.69 ? 180 LEU A HD21 1 ATOM 2586 H HD22 . LEU A 1 172 ? 8.405 -2.253 25.922 1.00 30.69 ? 180 LEU A HD22 1 ATOM 2587 H HD23 . LEU A 1 172 ? 8.204 -1.851 27.446 1.00 30.69 ? 180 LEU A HD23 1 ATOM 2588 N N . PRO A 1 173 ? 7.755 -6.216 28.025 1.00 34.60 ? 181 PRO A N 1 ATOM 2589 C CA . PRO A 1 173 ? 7.541 -7.657 27.864 1.00 35.82 ? 181 PRO A CA 1 ATOM 2590 C C . PRO A 1 173 ? 8.345 -8.192 26.686 1.00 35.43 ? 181 PRO A C 1 ATOM 2591 O O . PRO A 1 173 ? 8.874 -7.442 25.871 1.00 34.00 ? 181 PRO A O 1 ATOM 2592 C CB . PRO A 1 173 ? 6.052 -7.716 27.554 1.00 36.40 ? 181 PRO A CB 1 ATOM 2593 C CG . PRO A 1 173 ? 5.831 -6.480 26.720 1.00 35.64 ? 181 PRO A CG 1 ATOM 2594 C CD . PRO A 1 173 ? 6.747 -5.426 27.302 1.00 35.44 ? 181 PRO A CD 1 ATOM 2595 H HA . PRO A 1 173 ? 7.745 -8.146 28.677 1.00 42.99 ? 181 PRO A HA 1 ATOM 2596 H HB2 . PRO A 1 173 ? 5.849 -8.519 27.049 1.00 43.68 ? 181 PRO A HB2 1 ATOM 2597 H HB3 . PRO A 1 173 ? 5.539 -7.680 28.377 1.00 43.68 ? 181 PRO A HB3 1 ATOM 2598 H HG2 . PRO A 1 173 ? 6.066 -6.664 25.797 1.00 42.77 ? 181 PRO A HG2 1 ATOM 2599 H HG3 . PRO A 1 173 ? 4.904 -6.202 26.789 1.00 42.77 ? 181 PRO A HG3 1 ATOM 2600 H HD2 . PRO A 1 173 ? 7.164 -4.911 26.594 1.00 42.52 ? 181 PRO A HD2 1 ATOM 2601 H HD3 . PRO A 1 173 ? 6.259 -4.856 27.917 1.00 42.52 ? 181 PRO A HD3 1 ATOM 2602 N N . GLY A 1 174 ? 8.421 -9.516 26.597 1.00 36.43 ? 182 GLY A N 1 ATOM 2603 C CA . GLY A 1 174 ? 9.043 -10.139 25.443 1.00 36.18 ? 182 GLY A CA 1 ATOM 2604 C C . GLY A 1 174 ? 8.302 -9.741 24.172 1.00 36.05 ? 182 GLY A C 1 ATOM 2605 O O . GLY A 1 174 ? 7.134 -9.348 24.233 1.00 37.98 ? 182 GLY A O 1 ATOM 2606 H H . GLY A 1 174 ? 8.122 -10.067 27.186 1.00 43.71 ? 182 GLY A H 1 ATOM 2607 H HA2 . GLY A 1 174 ? 9.967 -9.854 25.371 1.00 43.42 ? 182 GLY A HA2 1 ATOM 2608 H HA3 . GLY A 1 174 ? 9.017 -11.104 25.534 1.00 43.42 ? 182 GLY A HA3 1 ATOM 2609 N N . PRO A 1 175 ? 8.955 -9.866 23.008 1.00 32.43 ? 183 PRO A N 1 ATOM 2610 C CA . PRO A 1 175 ? 10.272 -10.481 22.838 1.00 32.49 ? 183 PRO A CA 1 ATOM 2611 C C . PRO A 1 175 ? 11.436 -9.544 23.084 1.00 31.21 ? 183 PRO A C 1 ATOM 2612 O O . PRO A 1 175 ? 12.571 -9.959 22.836 1.00 33.91 ? 183 PRO A O 1 ATOM 2613 C CB . PRO A 1 175 ? 10.253 -10.933 21.370 1.00 33.58 ? 183 PRO A CB 1 ATOM 2614 C CG . PRO A 1 175 ? 9.354 -9.971 20.716 1.00 33.54 ? 183 PRO A CG 1 ATOM 2615 C CD . PRO A 1 175 ? 8.299 -9.628 21.709 1.00 33.27 ? 183 PRO A CD 1 ATOM 2616 H HA . PRO A 1 175 ? 10.357 -11.258 23.411 1.00 38.99 ? 183 PRO A HA 1 ATOM 2617 H HB2 . PRO A 1 175 ? 11.147 -10.880 20.996 1.00 40.30 ? 183 PRO A HB2 1 ATOM 2618 H HB3 . PRO A 1 175 ? 9.902 -11.835 21.306 1.00 40.30 ? 183 PRO A HB3 1 ATOM 2619 H HG2 . PRO A 1 175 ? 9.855 -9.179 20.467 1.00 40.25 ? 183 PRO A HG2 1 ATOM 2620 H HG3 . PRO A 1 175 ? 8.959 -10.382 19.931 1.00 40.25 ? 183 PRO A HG3 1 ATOM 2621 H HD2 . PRO A 1 175 ? 8.046 -8.695 21.624 1.00 39.93 ? 183 PRO A HD2 1 ATOM 2622 H HD3 . PRO A 1 175 ? 7.533 -10.214 21.605 1.00 39.93 ? 183 PRO A HD3 1 ATOM 2623 N N . SER A 1 176 ? 11.193 -8.323 23.575 1.00 28.76 ? 184 SER A N 1 ATOM 2624 C CA . SER A 1 176 ? 12.299 -7.464 23.975 1.00 27.86 ? 184 SER A CA 1 ATOM 2625 C C . SER A 1 176 ? 13.117 -8.168 25.047 1.00 27.65 ? 184 SER A C 1 ATOM 2626 O O . SER A 1 176 ? 12.566 -8.706 26.012 1.00 28.66 ? 184 SER A O 1 ATOM 2627 C CB . SER A 1 176 ? 11.780 -6.128 24.512 1.00 28.80 ? 184 SER A CB 1 ATOM 2628 O OG . SER A 1 176 ? 11.027 -5.430 23.534 1.00 31.58 ? 184 SER A OG 1 ATOM 2629 H H . SER A 1 176 ? 10.411 -7.979 23.681 1.00 34.51 ? 184 SER A H 1 ATOM 2630 H HA . SER A 1 176 ? 12.871 -7.290 23.212 1.00 33.44 ? 184 SER A HA 1 ATOM 2631 H HB2 . SER A 1 176 ? 11.214 -6.298 25.281 1.00 34.56 ? 184 SER A HB2 1 ATOM 2632 H HB3 . SER A 1 176 ? 12.537 -5.580 24.775 1.00 34.56 ? 184 SER A HB3 1 ATOM 2633 H HG . SER A 1 176 ? 10.366 -5.891 23.298 1.00 37.90 ? 184 SER A HG 1 ATOM 2634 N N . ARG A 1 177 ? 14.440 -8.163 24.879 1.00 28.13 ? 185 ARG A N 1 ATOM 2635 C CA . ARG A 1 177 ? 15.291 -9.023 25.697 1.00 30.03 ? 185 ARG A CA 1 ATOM 2636 C C . ARG A 1 177 ? 15.436 -8.498 27.119 1.00 29.72 ? 185 ARG A C 1 ATOM 2637 O O . ARG A 1 177 ? 15.325 -9.259 28.092 1.00 31.24 ? 185 ARG A O 1 ATOM 2638 C CB . ARG A 1 177 ? 16.674 -9.141 25.061 1.00 32.32 ? 185 ARG A CB 1 ATOM 2639 C CG . ARG A 1 177 ? 17.559 -10.137 25.777 1.00 34.27 ? 185 ARG A CG 1 ATOM 2640 C CD . ARG A 1 177 ? 18.944 -10.194 25.179 1.00 37.18 ? 185 ARG A CD 1 ATOM 2641 N NE . ARG A 1 177 ? 19.596 -8.892 25.233 1.00 39.76 ? 185 ARG A NE 1 ATOM 2642 C CZ . ARG A 1 177 ? 20.181 -8.393 26.319 1.00 41.92 ? 185 ARG A CZ 1 ATOM 2643 N NH1 . ARG A 1 177 ? 20.197 -9.083 27.458 1.00 41.21 ? 185 ARG A NH1 1 ATOM 2644 N NH2 . ARG A 1 177 ? 20.751 -7.194 26.266 1.00 43.38 ? 185 ARG A NH2 1 ATOM 2645 H H . ARG A 1 177 ? 14.862 -7.679 24.308 1.00 33.76 ? 185 ARG A H 1 ATOM 2646 H HA . ARG A 1 177 ? 14.900 -9.910 25.741 1.00 36.03 ? 185 ARG A HA 1 ATOM 2647 H HB2 . ARG A 1 177 ? 16.575 -9.433 24.141 1.00 38.78 ? 185 ARG A HB2 1 ATOM 2648 H HB3 . ARG A 1 177 ? 17.111 -8.275 25.090 1.00 38.78 ? 185 ARG A HB3 1 ATOM 2649 H HG2 . ARG A 1 177 ? 17.643 -9.878 26.708 1.00 41.12 ? 185 ARG A HG2 1 ATOM 2650 H HG3 . ARG A 1 177 ? 17.165 -11.021 25.710 1.00 41.12 ? 185 ARG A HG3 1 ATOM 2651 H HD2 . ARG A 1 177 ? 19.484 -10.826 25.678 1.00 44.62 ? 185 ARG A HD2 1 ATOM 2652 H HD3 . ARG A 1 177 ? 18.881 -10.464 24.249 1.00 44.62 ? 185 ARG A HD3 1 ATOM 2653 H HE . ARG A 1 177 ? 19.603 -8.416 24.517 1.00 47.71 ? 185 ARG A HE 1 ATOM 2654 H HH11 . ARG A 1 177 ? 19.829 -9.860 27.495 1.00 49.45 ? 185 ARG A HH11 1 ATOM 2655 H HH12 . ARG A 1 177 ? 20.577 -8.753 28.155 1.00 49.45 ? 185 ARG A HH12 1 ATOM 2656 H HH21 . ARG A 1 177 ? 20.742 -6.746 25.532 1.00 52.05 ? 185 ARG A HH21 1 ATOM 2657 H HH22 . ARG A 1 177 ? 21.129 -6.867 26.965 1.00 52.05 ? 185 ARG A HH22 1 ATOM 2658 N N . ALA A 1 178 ? 15.741 -7.214 27.261 1.00 26.74 ? 186 ALA A N 1 ATOM 2659 C CA . ALA A 1 178 ? 16.073 -6.665 28.570 1.00 25.59 ? 186 ALA A CA 1 ATOM 2660 C C . ALA A 1 178 ? 15.840 -5.163 28.540 1.00 22.41 ? 186 ALA A C 1 ATOM 2661 O O . ALA A 1 178 ? 16.779 -4.363 28.593 1.00 21.47 ? 186 ALA A O 1 ATOM 2662 C CB . ALA A 1 178 ? 17.524 -6.988 28.932 1.00 26.21 ? 186 ALA A CB 1 ATOM 2663 H H . ALA A 1 178 ? 15.764 -6.642 26.619 1.00 32.09 ? 186 ALA A H 1 ATOM 2664 H HA . ALA A 1 178 ? 15.493 -7.055 29.243 1.00 30.71 ? 186 ALA A HA 1 ATOM 2665 H HB1 . ALA A 1 178 ? 17.721 -6.613 29.805 1.00 31.45 ? 186 ALA A HB1 1 ATOM 2666 H HB2 . ALA A 1 178 ? 17.637 -7.951 28.952 1.00 31.45 ? 186 ALA A HB2 1 ATOM 2667 H HB3 . ALA A 1 178 ? 18.110 -6.599 28.265 1.00 31.45 ? 186 ALA A HB3 1 ATOM 2668 N N . GLY A 1 179 ? 14.578 -4.774 28.445 1.00 20.06 ? 187 GLY A N 1 ATOM 2669 C CA . GLY A 1 179 ? 14.240 -3.378 28.265 1.00 18.74 ? 187 GLY A CA 1 ATOM 2670 C C . GLY A 1 179 ? 13.303 -2.868 29.340 1.00 16.40 ? 187 GLY A C 1 ATOM 2671 O O . GLY A 1 179 ? 12.540 -3.628 29.950 1.00 18.18 ? 187 GLY A O 1 ATOM 2672 H H . GLY A 1 179 ? 13.900 -5.301 28.481 1.00 24.07 ? 187 GLY A H 1 ATOM 2673 H HA2 . GLY A 1 179 ? 15.050 -2.845 28.285 1.00 22.49 ? 187 GLY A HA2 1 ATOM 2674 H HA3 . GLY A 1 179 ? 13.814 -3.257 27.403 1.00 22.49 ? 187 GLY A HA3 1 ATOM 2675 N N . ARG A 1 180 ? 13.334 -1.560 29.532 1.00 16.07 ? 188 ARG A N 1 ATOM 2676 C CA . ARG A 1 180 ? 12.509 -0.910 30.527 1.00 15.26 ? 188 ARG A CA 1 ATOM 2677 C C . ARG A 1 180 ? 12.098 0.443 29.982 1.00 13.83 ? 188 ARG A C 1 ATOM 2678 O O . ARG A 1 180 ? 12.883 1.078 29.284 1.00 14.99 ? 188 ARG A O 1 ATOM 2679 C CB . ARG A 1 180 ? 13.347 -0.720 31.798 1.00 16.38 ? 188 ARG A CB 1 ATOM 2680 C CG . ARG A 1 180 ? 12.677 0.105 32.874 1.00 16.69 ? 188 ARG A CG 1 ATOM 2681 C CD . ARG A 1 180 ? 13.405 0.034 34.214 1.00 18.11 ? 188 ARG A CD 1 ATOM 2682 N NE . ARG A 1 180 ? 13.455 -1.331 34.704 1.00 18.00 ? 188 ARG A NE 1 ATOM 2683 C CZ . ARG A 1 180 ? 12.499 -1.908 35.413 1.00 21.03 ? 188 ARG A CZ 1 ATOM 2684 N NH1 . ARG A 1 180 ? 11.400 -1.243 35.733 1.00 22.17 ? 188 ARG A NH1 1 ATOM 2685 N NH2 . ARG A 1 180 ? 12.636 -3.160 35.802 1.00 25.23 ? 188 ARG A NH2 1 ATOM 2686 H H . ARG A 1 180 ? 13.834 -1.019 29.089 1.00 19.29 ? 188 ARG A H 1 ATOM 2687 H HA . ARG A 1 180 ? 11.722 -1.440 30.726 1.00 18.32 ? 188 ARG A HA 1 ATOM 2688 H HB2 . ARG A 1 180 ? 13.542 -1.593 32.175 1.00 19.66 ? 188 ARG A HB2 1 ATOM 2689 H HB3 . ARG A 1 180 ? 14.176 -0.275 31.560 1.00 19.66 ? 188 ARG A HB3 1 ATOM 2690 H HG2 . ARG A 1 180 ? 12.655 1.033 32.593 1.00 20.03 ? 188 ARG A HG2 1 ATOM 2691 H HG3 . ARG A 1 180 ? 11.774 -0.223 33.007 1.00 20.03 ? 188 ARG A HG3 1 ATOM 2692 H HD2 . ARG A 1 180 ? 14.315 0.353 34.104 1.00 21.73 ? 188 ARG A HD2 1 ATOM 2693 H HD3 . ARG A 1 180 ? 12.934 0.576 34.866 1.00 21.73 ? 188 ARG A HD3 1 ATOM 2694 H HE . ARG A 1 180 ? 14.155 -1.796 34.522 1.00 21.61 ? 188 ARG A HE 1 ATOM 2695 H HH11 . ARG A 1 180 ? 11.302 -0.427 35.480 1.00 26.60 ? 188 ARG A HH11 1 ATOM 2696 H HH12 . ARG A 1 180 ? 10.784 -1.627 36.195 1.00 26.60 ? 188 ARG A HH12 1 ATOM 2697 H HH21 . ARG A 1 180 ? 13.348 -3.598 35.600 1.00 30.27 ? 188 ARG A HH21 1 ATOM 2698 H HH22 . ARG A 1 180 ? 12.017 -3.536 36.266 1.00 30.27 ? 188 ARG A HH22 1 ATOM 2699 N N . VAL A 1 181 ? 10.866 0.868 30.276 1.00 13.18 ? 189 VAL A N 1 ATOM 2700 C CA . VAL A 1 181 ? 10.402 2.216 29.962 1.00 13.14 ? 189 VAL A CA 1 ATOM 2701 C C . VAL A 1 181 ? 10.280 2.984 31.262 1.00 13.16 ? 189 VAL A C 1 ATOM 2702 O O . VAL A 1 181 ? 9.650 2.518 32.215 1.00 16.45 ? 189 VAL A O 1 ATOM 2703 C CB . VAL A 1 181 ? 9.062 2.203 29.200 1.00 14.72 ? 189 VAL A CB 1 ATOM 2704 C CG1 . VAL A 1 181 ? 8.604 3.623 28.875 1.00 14.43 ? 189 VAL A CG1 1 ATOM 2705 C CG2 . VAL A 1 181 ? 9.183 1.411 27.912 1.00 17.57 ? 189 VAL A CG2 1 ATOM 2706 H H . VAL A 1 181 ? 10.273 0.382 30.666 1.00 15.81 ? 189 VAL A H 1 ATOM 2707 H HA . VAL A 1 181 ? 11.062 2.660 29.407 1.00 15.77 ? 189 VAL A HA 1 ATOM 2708 H HB . VAL A 1 181 ? 8.384 1.784 29.753 1.00 17.66 ? 189 VAL A HB 1 ATOM 2709 H HG11 . VAL A 1 181 ? 7.761 3.580 28.397 1.00 17.32 ? 189 VAL A HG11 1 ATOM 2710 H HG12 . VAL A 1 181 ? 8.491 4.115 29.703 1.00 17.32 ? 189 VAL A HG12 1 ATOM 2711 H HG13 . VAL A 1 181 ? 9.277 4.052 28.323 1.00 17.32 ? 189 VAL A HG13 1 ATOM 2712 H HG21 . VAL A 1 181 ? 8.327 1.421 27.455 1.00 21.09 ? 189 VAL A HG21 1 ATOM 2713 H HG22 . VAL A 1 181 ? 9.861 1.820 27.353 1.00 21.09 ? 189 VAL A HG22 1 ATOM 2714 H HG23 . VAL A 1 181 ? 9.434 0.499 28.125 1.00 21.09 ? 189 VAL A HG23 1 ATOM 2715 N N . VAL A 1 182 ? 10.844 4.178 31.278 1.00 11.55 ? 190 VAL A N 1 ATOM 2716 C CA . VAL A 1 182 ? 10.702 5.111 32.383 1.00 12.04 ? 190 VAL A CA 1 ATOM 2717 C C . VAL A 1 182 ? 9.781 6.217 31.932 1.00 11.73 ? 190 VAL A C 1 ATOM 2718 O O . VAL A 1 182 ? 10.028 6.849 30.900 1.00 13.58 ? 190 VAL A O 1 ATOM 2719 C CB . VAL A 1 182 ? 12.072 5.692 32.755 1.00 13.41 ? 190 VAL A CB 1 ATOM 2720 C CG1 . VAL A 1 182 ? 11.912 6.924 33.639 1.00 17.63 ? 190 VAL A CG1 1 ATOM 2721 C CG2 . VAL A 1 182 ? 12.929 4.623 33.394 1.00 17.01 ? 190 VAL A CG2 1 ATOM 2722 H H . VAL A 1 182 ? 11.330 4.483 30.637 1.00 13.86 ? 190 VAL A H 1 ATOM 2723 H HA . VAL A 1 182 ? 10.319 4.666 33.156 1.00 14.45 ? 190 VAL A HA 1 ATOM 2724 H HB . VAL A 1 182 ? 12.517 5.975 31.941 1.00 16.09 ? 190 VAL A HB 1 ATOM 2725 H HG11 . VAL A 1 182 ? 12.790 7.271 33.859 1.00 21.15 ? 190 VAL A HG11 1 ATOM 2726 H HG12 . VAL A 1 182 ? 11.402 7.594 33.158 1.00 21.15 ? 190 VAL A HG12 1 ATOM 2727 H HG13 . VAL A 1 182 ? 11.443 6.671 34.450 1.00 21.15 ? 190 VAL A HG13 1 ATOM 2728 H HG21 . VAL A 1 182 ? 13.791 5.005 33.623 1.00 20.41 ? 190 VAL A HG21 1 ATOM 2729 H HG22 . VAL A 1 182 ? 12.487 4.301 34.194 1.00 20.41 ? 190 VAL A HG22 1 ATOM 2730 H HG23 . VAL A 1 182 ? 13.047 3.895 32.764 1.00 20.41 ? 190 VAL A HG23 1 ATOM 2731 N N . VAL A 1 183 ? 8.740 6.462 32.709 1.00 11.67 ? 191 VAL A N 1 ATOM 2732 C CA . VAL A 1 183 ? 7.719 7.447 32.377 1.00 11.68 ? 191 VAL A CA 1 ATOM 2733 C C . VAL A 1 183 ? 7.823 8.584 33.387 1.00 12.06 ? 191 VAL A C 1 ATOM 2734 O O . VAL A 1 183 ? 7.568 8.388 34.577 1.00 12.15 ? 191 VAL A O 1 ATOM 2735 C CB . VAL A 1 183 ? 6.317 6.825 32.386 1.00 11.91 ? 191 VAL A CB 1 ATOM 2736 C CG1 . VAL A 1 183 ? 5.282 7.870 31.995 1.00 13.61 ? 191 VAL A CG1 1 ATOM 2737 C CG2 . VAL A 1 183 ? 6.241 5.634 31.432 1.00 13.59 ? 191 VAL A CG2 1 ATOM 2738 H H . VAL A 1 183 ? 8.598 6.061 33.457 1.00 14.01 ? 191 VAL A H 1 ATOM 2739 H HA . VAL A 1 183 ? 7.890 7.805 31.492 1.00 14.02 ? 191 VAL A HA 1 ATOM 2740 H HB . VAL A 1 183 ? 6.110 6.512 33.280 1.00 14.30 ? 191 VAL A HB 1 ATOM 2741 H HG11 . VAL A 1 183 ? 4.402 7.462 32.005 1.00 16.33 ? 191 VAL A HG11 1 ATOM 2742 H HG12 . VAL A 1 183 ? 5.316 8.600 32.633 1.00 16.33 ? 191 VAL A HG12 1 ATOM 2743 H HG13 . VAL A 1 183 ? 5.486 8.198 31.105 1.00 16.33 ? 191 VAL A HG13 1 ATOM 2744 H HG21 . VAL A 1 183 ? 5.344 5.264 31.460 1.00 16.31 ? 191 VAL A HG21 1 ATOM 2745 H HG22 . VAL A 1 183 ? 6.446 5.936 30.533 1.00 16.31 ? 191 VAL A HG22 1 ATOM 2746 H HG23 . VAL A 1 183 ? 6.884 4.964 31.711 1.00 16.31 ? 191 VAL A HG23 1 ATOM 2747 N N . LEU A 1 184 ? 8.146 9.772 32.909 1.00 11.37 ? 192 LEU A N 1 ATOM 2748 C CA . LEU A 1 184 ? 8.327 10.937 33.756 1.00 11.08 ? 192 LEU A CA 1 ATOM 2749 C C . LEU A 1 184 ? 7.116 11.855 33.747 1.00 11.11 ? 192 LEU A C 1 ATOM 2750 O O . LEU A 1 184 ? 6.325 11.889 32.800 1.00 11.07 ? 192 LEU A O 1 ATOM 2751 C CB . LEU A 1 184 ? 9.546 11.733 33.303 1.00 11.05 ? 192 LEU A CB 1 ATOM 2752 C CG . LEU A 1 184 ? 10.881 11.006 33.255 1.00 12.07 ? 192 LEU A CG 1 ATOM 2753 C CD1 . LEU A 1 184 ? 11.966 11.959 32.787 1.00 12.95 ? 192 LEU A CD1 1 ATOM 2754 C CD2 . LEU A 1 184 ? 11.212 10.404 34.606 1.00 14.46 ? 192 LEU A CD2 1 ATOM 2755 H H . LEU A 1 184 ? 8.269 9.934 32.074 1.00 13.64 ? 192 LEU A H 1 ATOM 2756 H HA . LEU A 1 184 ? 8.478 10.645 34.668 1.00 13.29 ? 192 LEU A HA 1 ATOM 2757 H HB2 . LEU A 1 184 ? 9.371 12.066 32.409 1.00 13.26 ? 192 LEU A HB2 1 ATOM 2758 H HB3 . LEU A 1 184 ? 9.654 12.485 33.907 1.00 13.26 ? 192 LEU A HB3 1 ATOM 2759 H HG . LEU A 1 184 ? 10.822 10.282 32.612 1.00 14.48 ? 192 LEU A HG 1 ATOM 2760 H HD11 . LEU A 1 184 ? 12.812 11.485 32.760 1.00 15.55 ? 192 LEU A HD11 1 ATOM 2761 H HD12 . LEU A 1 184 ? 11.740 12.284 31.902 1.00 15.55 ? 192 LEU A HD12 1 ATOM 2762 H HD13 . LEU A 1 184 ? 12.022 12.702 33.408 1.00 15.55 ? 192 LEU A HD13 1 ATOM 2763 H HD21 . LEU A 1 184 ? 12.066 9.948 34.546 1.00 17.35 ? 192 LEU A HD21 1 ATOM 2764 H HD22 . LEU A 1 184 ? 11.262 11.115 35.264 1.00 17.35 ? 192 LEU A HD22 1 ATOM 2765 H HD23 . LEU A 1 184 ? 10.516 9.774 34.849 1.00 17.35 ? 192 LEU A HD23 1 ATOM 2766 N N . ASN A 1 185 ? 7.013 12.611 34.829 1.00 11.47 ? 193 ASN A N 1 ATOM 2767 C CA . ASN A 1 185 ? 6.119 13.752 34.973 1.00 10.88 ? 193 ASN A CA 1 ATOM 2768 C C . ASN A 1 185 ? 6.989 15.008 34.909 1.00 10.80 ? 193 ASN A C 1 ATOM 2769 O O . ASN A 1 185 ? 7.431 15.545 35.923 1.00 12.04 ? 193 ASN A O 1 ATOM 2770 C CB . ASN A 1 185 ? 5.371 13.652 36.286 1.00 11.53 ? 193 ASN A CB 1 ATOM 2771 C CG . ASN A 1 185 ? 4.470 14.837 36.530 1.00 11.84 ? 193 ASN A CG 1 ATOM 2772 O OD1 . ASN A 1 185 ? 4.337 15.740 35.685 1.00 12.05 ? 193 ASN A OD1 1 ATOM 2773 N ND2 . ASN A 1 185 ? 3.821 14.826 37.672 1.00 12.43 ? 193 ASN A ND2 1 ATOM 2774 H H . ASN A 1 185 ? 7.481 12.473 35.538 1.00 13.76 ? 193 ASN A H 1 ATOM 2775 H HA . ASN A 1 185 ? 5.480 13.769 34.243 1.00 13.05 ? 193 ASN A HA 1 ATOM 2776 H HB2 . ASN A 1 185 ? 4.821 12.853 36.277 1.00 13.83 ? 193 ASN A HB2 1 ATOM 2777 H HB3 . ASN A 1 185 ? 6.012 13.607 37.012 1.00 13.83 ? 193 ASN A HB3 1 ATOM 2778 H HD21 . ASN A 1 185 ? 3.291 15.473 37.872 1.00 14.92 ? 193 ASN A HD21 1 ATOM 2779 H HD22 . ASN A 1 185 ? 3.926 14.171 38.220 1.00 14.92 ? 193 ASN A HD22 1 ATOM 2780 N N . THR A 1 186 ? 7.312 15.453 33.692 1.00 11.29 ? 194 THR A N 1 ATOM 2781 C CA . THR A 1 186 ? 8.143 16.651 33.554 1.00 10.46 ? 194 THR A CA 1 ATOM 2782 C C . THR A 1 186 ? 7.328 17.933 33.651 1.00 11.02 ? 194 THR A C 1 ATOM 2783 O O . THR A 1 186 ? 7.900 19.027 33.593 1.00 11.88 ? 194 THR A O 1 ATOM 2784 C CB . THR A 1 186 ? 9.037 16.607 32.322 1.00 10.92 ? 194 THR A CB 1 ATOM 2785 O OG1 . THR A 1 186 ? 8.200 16.417 31.183 1.00 11.72 ? 194 THR A OG1 1 ATOM 2786 C CG2 . THR A 1 186 ? 10.107 15.506 32.367 1.00 11.33 ? 194 THR A CG2 1 ATOM 2787 H H . THR A 1 186 ? 7.069 15.091 32.950 1.00 13.55 ? 194 THR A H 1 ATOM 2788 H HA . THR A 1 186 ? 8.744 16.663 34.315 1.00 12.56 ? 194 THR A HA 1 ATOM 2789 H HB . THR A 1 186 ? 9.492 17.459 32.236 1.00 13.11 ? 194 THR A HB 1 ATOM 2790 H HG1 . THR A 1 186 ? 8.667 16.389 30.485 1.00 14.07 ? 194 THR A HG1 1 ATOM 2791 H HG21 . THR A 1 186 ? 10.642 15.530 31.558 1.00 13.59 ? 194 THR A HG21 1 ATOM 2792 H HG22 . THR A 1 186 ? 10.688 15.640 33.133 1.00 13.59 ? 194 THR A HG22 1 ATOM 2793 H HG23 . THR A 1 186 ? 9.685 14.636 32.441 1.00 13.59 ? 194 THR A HG23 1 ATOM 2794 N N . ASN A 1 187 ? 6.014 17.821 33.832 1.00 10.91 ? 195 ASN A N 1 ATOM 2795 C CA . ASN A 1 187 ? 5.202 18.995 34.126 1.00 11.40 ? 195 ASN A CA 1 ATOM 2796 C C . ASN A 1 187 ? 5.577 19.600 35.466 1.00 11.29 ? 195 ASN A C 1 ATOM 2797 O O . ASN A 1 187 ? 5.325 20.791 35.697 1.00 12.61 ? 195 ASN A O 1 ATOM 2798 C CB . ASN A 1 187 ? 3.723 18.608 34.082 1.00 12.11 ? 195 ASN A CB 1 ATOM 2799 C CG . ASN A 1 187 ? 3.393 17.814 32.842 1.00 12.09 ? 195 ASN A CG 1 ATOM 2800 O OD1 . ASN A 1 187 ? 3.518 18.301 31.718 1.00 13.78 ? 195 ASN A OD1 1 ATOM 2801 N ND2 . ASN A 1 187 ? 3.045 16.566 33.032 1.00 13.43 ? 195 ASN A ND2 1 ATOM 2802 H H . ASN A 1 187 ? 5.574 17.083 33.790 1.00 13.09 ? 195 ASN A H 1 ATOM 2803 H HA . ASN A 1 187 ? 5.357 19.665 33.442 1.00 13.68 ? 195 ASN A HA 1 ATOM 2804 H HB2 . ASN A 1 187 ? 3.512 18.063 34.856 1.00 14.53 ? 195 ASN A HB2 1 ATOM 2805 H HB3 . ASN A 1 187 ? 3.182 19.413 34.080 1.00 14.53 ? 195 ASN A HB3 1 ATOM 2806 H HD21 . ASN A 1 187 ? 2.847 16.067 32.360 1.00 16.12 ? 195 ASN A HD21 1 ATOM 2807 H HD22 . ASN A 1 187 ? 3.016 16.244 33.829 1.00 16.12 ? 195 ASN A HD22 1 ATOM 2808 N N . LEU A 1 188 ? 6.222 18.817 36.326 1.00 11.89 ? 196 LEU A N 1 ATOM 2809 C CA . LEU A 1 188 ? 6.748 19.326 37.593 1.00 12.64 ? 196 LEU A CA 1 ATOM 2810 C C . LEU A 1 188 ? 7.789 20.413 37.389 1.00 12.60 ? 196 LEU A C 1 ATOM 2811 O O . LEU A 1 188 ? 8.056 21.174 38.323 1.00 14.53 ? 196 LEU A O 1 ATOM 2812 C CB . LEU A 1 188 ? 7.362 18.182 38.402 1.00 13.08 ? 196 LEU A CB 1 ATOM 2813 C CG . LEU A 1 188 ? 6.417 17.065 38.824 1.00 12.53 ? 196 LEU A CG 1 ATOM 2814 C CD1 . LEU A 1 188 ? 7.190 15.947 39.473 1.00 14.59 ? 196 LEU A CD1 1 ATOM 2815 C CD2 . LEU A 1 188 ? 5.359 17.569 39.776 1.00 14.56 ? 196 LEU A CD2 1 ATOM 2816 H H . LEU A 1 188 ? 6.370 17.979 36.200 1.00 14.26 ? 196 LEU A H 1 ATOM 2817 H HA . LEU A 1 188 ? 6.018 19.702 38.110 1.00 15.16 ? 196 LEU A HA 1 ATOM 2818 H HB2 . LEU A 1 188 ? 8.065 17.777 37.870 1.00 15.70 ? 196 LEU A HB2 1 ATOM 2819 H HB3 . LEU A 1 188 ? 7.747 18.554 39.211 1.00 15.70 ? 196 LEU A HB3 1 ATOM 2820 H HG . LEU A 1 188 ? 5.973 16.710 38.038 1.00 15.03 ? 196 LEU A HG 1 ATOM 2821 H HD11 . LEU A 1 188 ? 6.572 15.247 39.734 1.00 17.51 ? 196 LEU A HD11 1 ATOM 2822 H HD12 . LEU A 1 188 ? 7.835 15.599 38.838 1.00 17.51 ? 196 LEU A HD12 1 ATOM 2823 H HD13 . LEU A 1 188 ? 7.648 16.293 40.255 1.00 17.51 ? 196 LEU A HD13 1 ATOM 2824 H HD21 . LEU A 1 188 ? 4.779 16.831 40.021 1.00 17.47 ? 196 LEU A HD21 1 ATOM 2825 H HD22 . LEU A 1 188 ? 5.792 17.927 40.567 1.00 17.47 ? 196 LEU A HD22 1 ATOM 2826 H HD23 . LEU A 1 188 ? 4.845 18.264 39.336 1.00 17.47 ? 196 LEU A HD23 1 ATOM 2827 N N . TYR A 1 189 ? 8.402 20.486 36.202 1.00 12.01 ? 197 TYR A N 1 ATOM 2828 C CA . TYR A 1 189 ? 9.531 21.370 35.974 1.00 12.80 ? 197 TYR A CA 1 ATOM 2829 C C . TYR A 1 189 ? 9.168 22.600 35.164 1.00 13.34 ? 197 TYR A C 1 ATOM 2830 O O . TYR A 1 189 ? 10.012 23.471 34.984 1.00 13.17 ? 197 TYR A O 1 ATOM 2831 C CB . TYR A 1 189 ? 10.648 20.596 35.256 1.00 13.37 ? 197 TYR A CB 1 ATOM 2832 C CG . TYR A 1 189 ? 11.042 19.327 35.990 1.00 12.67 ? 197 TYR A CG 1 ATOM 2833 C CD1 . TYR A 1 189 ? 11.219 19.329 37.356 1.00 12.70 ? 197 TYR A CD1 1 ATOM 2834 C CD2 . TYR A 1 189 ? 11.225 18.132 35.322 1.00 12.40 ? 197 TYR A CD2 1 ATOM 2835 C CE1 . TYR A 1 189 ? 11.560 18.182 38.029 1.00 12.38 ? 197 TYR A CE1 1 ATOM 2836 C CE2 . TYR A 1 189 ? 11.581 16.983 35.991 1.00 13.14 ? 197 TYR A CE2 1 ATOM 2837 C CZ . TYR A 1 189 ? 11.744 17.009 37.350 1.00 12.89 ? 197 TYR A CZ 1 ATOM 2838 O OH . TYR A 1 189 ? 12.063 15.842 38.002 1.00 13.70 ? 197 TYR A OH 1 ATOM 2839 H H . TYR A 1 189 ? 8.174 20.026 35.511 1.00 14.41 ? 197 TYR A H 1 ATOM 2840 H HA . TYR A 1 189 ? 9.876 21.667 36.830 1.00 15.37 ? 197 TYR A HA 1 ATOM 2841 H HB2 . TYR A 1 189 ? 10.341 20.348 34.370 1.00 16.04 ? 197 TYR A HB2 1 ATOM 2842 H HB3 . TYR A 1 189 ? 11.433 21.162 35.190 1.00 16.04 ? 197 TYR A HB3 1 ATOM 2843 H HD1 . TYR A 1 189 ? 11.095 20.118 37.832 1.00 15.24 ? 197 TYR A HD1 1 ATOM 2844 H HD2 . TYR A 1 189 ? 11.114 18.104 34.399 1.00 14.88 ? 197 TYR A HD2 1 ATOM 2845 H HE1 . TYR A 1 189 ? 11.670 18.203 38.952 1.00 14.86 ? 197 TYR A HE1 1 ATOM 2846 H HE2 . TYR A 1 189 ? 11.691 16.187 35.524 1.00 15.77 ? 197 TYR A HE2 1 ATOM 2847 H HH . TYR A 1 189 ? 12.118 15.980 38.829 1.00 16.44 ? 197 TYR A HH 1 ATOM 2848 N N . TYR A 1 190 ? 7.950 22.678 34.650 1.00 14.22 ? 198 TYR A N 1 ATOM 2849 C CA . TYR A 1 190 ? 7.559 23.803 33.818 1.00 14.37 ? 198 TYR A CA 1 ATOM 2850 C C . TYR A 1 190 ? 7.568 25.088 34.646 1.00 14.43 ? 198 TYR A C 1 ATOM 2851 O O . TYR A 1 190 ? 7.073 25.140 35.770 1.00 17.70 ? 198 TYR A O 1 ATOM 2852 C CB . TYR A 1 190 ? 6.172 23.493 33.228 1.00 17.27 ? 198 TYR A CB 1 ATOM 2853 C CG . TYR A 1 190 ? 5.626 24.389 32.139 1.00 17.09 ? 198 TYR A CG 1 ATOM 2854 C CD1 . TYR A 1 190 ? 6.394 25.395 31.527 1.00 19.84 ? 198 TYR A CD1 1 ATOM 2855 C CD2 . TYR A 1 190 ? 4.306 24.280 31.751 1.00 21.89 ? 198 TYR A CD2 1 ATOM 2856 C CE1 . TYR A 1 190 ? 5.848 26.218 30.548 1.00 22.21 ? 198 TYR A CE1 1 ATOM 2857 C CE2 . TYR A 1 190 ? 3.775 25.091 30.786 1.00 23.23 ? 198 TYR A CE2 1 ATOM 2858 C CZ . TYR A 1 190 ? 4.540 26.054 30.200 1.00 24.22 ? 198 TYR A CZ 1 ATOM 2859 O OH . TYR A 1 190 ? 3.962 26.863 29.232 1.00 27.44 ? 198 TYR A OH 1 ATOM 2860 H H . TYR A 1 190 ? 7.331 22.093 34.767 1.00 17.07 ? 198 TYR A H 1 ATOM 2861 H HA . TYR A 1 190 ? 8.190 23.902 33.088 1.00 17.24 ? 198 TYR A HA 1 ATOM 2862 H HB2 . TYR A 1 190 ? 6.201 22.595 32.862 1.00 20.73 ? 198 TYR A HB2 1 ATOM 2863 H HB3 . TYR A 1 190 ? 5.530 23.515 33.955 1.00 20.73 ? 198 TYR A HB3 1 ATOM 2864 H HD1 . TYR A 1 190 ? 7.285 25.504 31.772 1.00 23.81 ? 198 TYR A HD1 1 ATOM 2865 H HD2 . TYR A 1 190 ? 3.769 23.630 32.144 1.00 26.27 ? 198 TYR A HD2 1 ATOM 2866 H HE1 . TYR A 1 190 ? 6.365 26.877 30.144 1.00 26.65 ? 198 TYR A HE1 1 ATOM 2867 H HE2 . TYR A 1 190 ? 2.884 24.993 30.538 1.00 27.88 ? 198 TYR A HE2 1 ATOM 2868 H HH . TYR A 1 190 ? 3.157 26.649 29.121 1.00 32.93 ? 198 TYR A HH 1 ATOM 2869 N N . SER A 1 191 ? 8.133 26.146 34.076 1.00 14.21 ? 199 SER A N 1 ATOM 2870 C CA . SER A 1 191 ? 8.286 27.389 34.811 1.00 17.25 ? 199 SER A CA 1 ATOM 2871 C C . SER A 1 191 ? 6.943 27.998 35.192 1.00 20.38 ? 199 SER A C 1 ATOM 2872 O O . SER A 1 191 ? 6.884 28.776 36.139 1.00 26.49 ? 199 SER A O 1 ATOM 2873 C CB . SER A 1 191 ? 9.102 28.380 33.990 1.00 20.88 ? 199 SER A CB 1 ATOM 2874 O OG . SER A 1 191 ? 8.417 28.735 32.805 1.00 22.53 ? 199 SER A OG 1 ATOM 2875 H H . SER A 1 191 ? 8.433 26.168 33.270 1.00 17.06 ? 199 SER A H 1 ATOM 2876 H HA . SER A 1 191 ? 8.773 27.210 35.631 1.00 20.70 ? 199 SER A HA 1 ATOM 2877 H HB2 . SER A 1 191 ? 9.255 29.179 34.519 1.00 25.06 ? 199 SER A HB2 1 ATOM 2878 H HB3 . SER A 1 191 ? 9.950 27.971 33.754 1.00 25.06 ? 199 SER A HB3 1 ATOM 2879 H HG . SER A 1 191 ? 8.277 28.051 32.338 1.00 27.03 ? 199 SER A HG 1 ATOM 2880 N N . ASN A 1 192 ? 5.872 27.654 34.481 1.00 20.70 ? 200 ASN A N 1 ATOM 2881 C CA . ASN A 1 192 ? 4.529 28.147 34.782 1.00 23.94 ? 200 ASN A CA 1 ATOM 2882 C C . ASN A 1 192 ? 3.829 27.355 35.873 1.00 22.70 ? 200 ASN A C 1 ATOM 2883 O O . ASN A 1 192 ? 2.719 27.727 36.268 1.00 23.84 ? 200 ASN A O 1 ATOM 2884 C CB . ASN A 1 192 ? 3.671 28.127 33.521 1.00 28.01 ? 200 ASN A CB 1 ATOM 2885 C CG . ASN A 1 192 ? 4.090 29.194 32.531 1.00 35.42 ? 200 ASN A CG 1 ATOM 2886 O OD1 . ASN A 1 192 ? 4.581 30.257 32.919 1.00 39.45 ? 200 ASN A OD1 1 ATOM 2887 N ND2 . ASN A 1 192 ? 3.904 28.924 31.260 1.00 39.09 ? 200 ASN A ND2 1 ATOM 2888 H H . ASN A 1 192 ? 5.897 27.124 33.804 1.00 24.84 ? 200 ASN A H 1 ATOM 2889 H HA . ASN A 1 192 ? 4.595 29.067 35.081 1.00 28.73 ? 200 ASN A HA 1 ATOM 2890 H HB2 . ASN A 1 192 ? 3.760 27.263 33.089 1.00 33.61 ? 200 ASN A HB2 1 ATOM 2891 H HB3 . ASN A 1 192 ? 2.746 28.286 33.763 1.00 33.61 ? 200 ASN A HB3 1 ATOM 2892 H HD21 . ASN A 1 192 ? 4.127 29.500 30.662 1.00 46.91 ? 200 ASN A HD21 1 ATOM 2893 H HD22 . ASN A 1 192 ? 3.560 28.172 31.026 1.00 46.91 ? 200 ASN A HD22 1 ATOM 2894 N N . ASN A 1 193 ? 4.453 26.296 36.379 1.00 19.72 ? 201 ASN A N 1 ATOM 2895 C CA . ASN A 1 193 ? 3.885 25.472 37.440 1.00 17.76 ? 201 ASN A CA 1 ATOM 2896 C C . ASN A 1 193 ? 4.262 26.071 38.791 1.00 18.82 ? 201 ASN A C 1 ATOM 2897 O O . ASN A 1 193 ? 5.383 25.901 39.278 1.00 20.41 ? 201 ASN A O 1 ATOM 2898 C CB . ASN A 1 193 ? 4.387 24.045 37.312 1.00 15.27 ? 201 ASN A CB 1 ATOM 2899 C CG . ASN A 1 193 ? 3.756 23.134 38.329 1.00 14.52 ? 201 ASN A CG 1 ATOM 2900 O OD1 . ASN A 1 193 ? 3.040 23.594 39.221 1.00 15.65 ? 201 ASN A OD1 1 ATOM 2901 N ND2 . ASN A 1 193 ? 4.012 21.852 38.226 1.00 13.86 ? 201 ASN A ND2 1 ATOM 2902 H H . ASN A 1 193 ? 5.227 26.028 36.116 1.00 23.66 ? 201 ASN A H 1 ATOM 2903 H HA . ASN A 1 193 ? 2.918 25.467 37.364 1.00 21.32 ? 201 ASN A HA 1 ATOM 2904 H HB2 . ASN A 1 193 ? 4.170 23.709 36.428 1.00 18.32 ? 201 ASN A HB2 1 ATOM 2905 H HB3 . ASN A 1 193 ? 5.348 24.032 37.448 1.00 18.32 ? 201 ASN A HB3 1 ATOM 2906 H HD21 . ASN A 1 193 ? 3.670 21.298 38.788 1.00 16.63 ? 201 ASN A HD21 1 ATOM 2907 H HD22 . ASN A 1 193 ? 4.522 21.565 37.596 1.00 16.63 ? 201 ASN A HD22 1 ATOM 2908 N N . GLU A 1 194 ? 3.303 26.743 39.430 1.00 20.28 ? 202 GLU A N 1 ATOM 2909 C CA . GLU A 1 194 ? 3.567 27.367 40.721 1.00 20.91 ? 202 GLU A CA 1 ATOM 2910 C C . GLU A 1 194 ? 3.641 26.357 41.856 1.00 20.39 ? 202 GLU A C 1 ATOM 2911 O O . GLU A 1 194 ? 4.174 26.679 42.923 1.00 21.02 ? 202 GLU A O 1 ATOM 2912 C CB . GLU A 1 194 ? 2.473 28.385 41.040 1.00 25.61 ? 202 GLU A CB 1 ATOM 2913 C CG . GLU A 1 194 ? 2.464 29.573 40.114 1.00 32.96 ? 202 GLU A CG 1 ATOM 2914 C CD . GLU A 1 194 ? 1.455 30.630 40.541 1.00 41.08 ? 202 GLU A CD 1 ATOM 2915 O OE1 . GLU A 1 194 ? 1.500 31.746 39.981 1.00 44.29 ? 202 GLU A OE1 1 ATOM 2916 O OE2 . GLU A 1 194 ? 0.622 30.352 41.435 1.00 44.35 ? 202 GLU A OE2 1 ATOM 2917 H H . GLU A 1 194 ? 2.501 26.850 39.139 1.00 24.33 ? 202 GLU A H 1 ATOM 2918 H HA . GLU A 1 194 ? 4.414 27.837 40.679 1.00 25.10 ? 202 GLU A HA 1 ATOM 2919 H HB2 . GLU A 1 194 ? 1.610 27.948 40.972 1.00 30.73 ? 202 GLU A HB2 1 ATOM 2920 H HB3 . GLU A 1 194 ? 2.605 28.713 41.944 1.00 30.73 ? 202 GLU A HB3 1 ATOM 2921 H HG2 . GLU A 1 194 ? 3.344 29.981 40.111 1.00 39.56 ? 202 GLU A HG2 1 ATOM 2922 H HG3 . GLU A 1 194 ? 2.231 29.278 39.220 1.00 39.56 ? 202 GLU A HG3 1 ATOM 2923 N N . GLN A 1 195 ? 3.140 25.139 41.650 1.00 18.67 ? 203 GLN A N 1 ATOM 2924 C CA . GLN A 1 195 ? 3.111 24.153 42.720 1.00 19.57 ? 203 GLN A CA 1 ATOM 2925 C C . GLN A 1 195 ? 4.500 23.685 43.113 1.00 19.94 ? 203 GLN A C 1 ATOM 2926 O O . GLN A 1 195 ? 4.678 23.198 44.230 1.00 22.47 ? 203 GLN A O 1 ATOM 2927 C CB . GLN A 1 195 ? 2.275 22.956 42.292 1.00 20.57 ? 203 GLN A CB 1 ATOM 2928 C CG . GLN A 1 195 ? 0.813 23.294 42.046 1.00 22.53 ? 203 GLN A CG 1 ATOM 2929 C CD . GLN A 1 195 ? 0.115 23.591 43.354 1.00 28.08 ? 203 GLN A CD 1 ATOM 2930 O OE1 . GLN A 1 195 ? -0.377 24.691 43.582 1.00 30.08 ? 203 GLN A OE1 1 ATOM 2931 N NE2 . GLN A 1 195 ? 0.119 22.611 44.249 1.00 31.52 ? 203 GLN A NE2 1 ATOM 2932 H H . GLN A 1 195 ? 2.815 24.864 40.903 1.00 22.40 ? 203 GLN A H 1 ATOM 2933 H HA . GLN A 1 195 ? 2.694 24.547 43.502 1.00 23.49 ? 203 GLN A HA 1 ATOM 2934 H HB2 . GLN A 1 195 ? 2.641 22.597 41.468 1.00 24.69 ? 203 GLN A HB2 1 ATOM 2935 H HB3 . GLN A 1 195 ? 2.312 22.283 42.990 1.00 24.69 ? 203 GLN A HB3 1 ATOM 2936 H HG2 . GLN A 1 195 ? 0.753 24.079 41.480 1.00 27.03 ? 203 GLN A HG2 1 ATOM 2937 H HG3 . GLN A 1 195 ? 0.372 22.538 41.626 1.00 27.03 ? 203 GLN A HG3 1 ATOM 2938 H HE21 . GLN A 1 195 ? 0.503 21.863 44.067 1.00 37.82 ? 203 GLN A HE21 1 ATOM 2939 H HE22 . GLN A 1 195 ? -0.263 22.723 45.011 1.00 37.82 ? 203 GLN A HE22 1 ATOM 2940 N N . THR A 1 196 ? 5.476 23.799 42.221 1.00 17.28 ? 204 THR A N 1 ATOM 2941 C CA . THR A 1 196 ? 6.816 23.292 42.483 1.00 17.19 ? 204 THR A CA 1 ATOM 2942 C C . THR A 1 196 ? 7.845 24.407 42.590 1.00 20.15 ? 204 THR A C 1 ATOM 2943 O O . THR A 1 196 ? 9.044 24.130 42.671 1.00 21.04 ? 204 THR A O 1 ATOM 2944 C CB . THR A 1 196 ? 7.234 22.300 41.401 1.00 17.50 ? 204 THR A CB 1 ATOM 2945 O OG1 . THR A 1 196 ? 7.175 22.950 40.130 1.00 19.13 ? 204 THR A OG1 1 ATOM 2946 C CG2 . THR A 1 196 ? 6.336 21.086 41.436 1.00 18.07 ? 204 THR A CG2 1 ATOM 2947 H H . THR A 1 196 ? 5.387 24.170 41.450 1.00 20.74 ? 204 THR A H 1 ATOM 2948 H HA . THR A 1 196 ? 6.808 22.818 43.329 1.00 20.63 ? 204 THR A HA 1 ATOM 2949 H HB . THR A 1 196 ? 8.144 22.009 41.569 1.00 21.00 ? 204 THR A HB 1 ATOM 2950 H HG1 . THR A 1 196 ? 7.403 22.415 39.523 1.00 22.96 ? 204 THR A HG1 1 ATOM 2951 H HG21 . THR A 1 196 ? 6.603 20.456 40.748 1.00 21.68 ? 204 THR A HG21 1 ATOM 2952 H HG22 . THR A 1 196 ? 6.398 20.652 42.301 1.00 21.68 ? 204 THR A HG22 1 ATOM 2953 H HG23 . THR A 1 196 ? 5.415 21.350 41.281 1.00 21.68 ? 204 THR A HG23 1 ATOM 2954 N N . ALA A 1 197 ? 7.411 25.664 42.580 1.00 22.84 ? 205 ALA A N 1 ATOM 2955 C CA . ALA A 1 197 ? 8.324 26.768 42.834 1.00 24.72 ? 205 ALA A CA 1 ATOM 2956 C C . ALA A 1 197 ? 9.078 26.536 44.134 1.00 26.28 ? 205 ALA A C 1 ATOM 2957 O O . ALA A 1 197 ? 8.495 26.156 45.156 1.00 27.19 ? 205 ALA A O 1 ATOM 2958 C CB . ALA A 1 197 ? 7.532 28.069 42.937 1.00 26.26 ? 205 ALA A CB 1 ATOM 2959 H H . ALA A 1 197 ? 6.598 25.901 42.430 1.00 27.41 ? 205 ALA A H 1 ATOM 2960 H HA . ALA A 1 197 ? 8.963 26.843 42.108 1.00 29.67 ? 205 ALA A HA 1 ATOM 2961 H HB1 . ALA A 1 197 ? 8.147 28.800 43.106 1.00 31.51 ? 205 ALA A HB1 1 ATOM 2962 H HB2 . ALA A 1 197 ? 7.061 28.218 42.102 1.00 31.51 ? 205 ALA A HB2 1 ATOM 2963 H HB3 . ALA A 1 197 ? 6.897 27.995 43.666 1.00 31.51 ? 205 ALA A HB3 1 ATOM 2964 N N . GLY A 1 198 ? 10.384 26.754 44.089 1.00 27.06 ? 206 GLY A N 1 ATOM 2965 C CA . GLY A 1 198 ? 11.191 26.631 45.278 1.00 26.65 ? 206 GLY A CA 1 ATOM 2966 C C . GLY A 1 198 ? 11.584 25.220 45.679 1.00 25.34 ? 206 GLY A C 1 ATOM 2967 O O . GLY A 1 198 ? 12.285 25.066 46.679 1.00 28.67 ? 206 GLY A O 1 ATOM 2968 H H . GLY A 1 198 ? 10.821 26.974 43.382 1.00 32.47 ? 206 GLY A H 1 ATOM 2969 H HA2 . GLY A 1 198 ? 12.007 27.139 45.152 1.00 31.98 ? 206 GLY A HA2 1 ATOM 2970 H HA3 . GLY A 1 198 ? 10.709 27.025 46.022 1.00 31.98 ? 206 GLY A HA3 1 ATOM 2971 N N . MET A 1 199 ? 11.176 24.191 44.944 1.00 22.26 ? 207 MET A N 1 ATOM 2972 C CA . MET A 1 199 ? 11.523 22.811 45.263 1.00 20.95 ? 207 MET A CA 1 ATOM 2973 C C . MET A 1 199 ? 12.684 22.380 44.391 1.00 21.32 ? 207 MET A C 1 ATOM 2974 O O . MET A 1 199 ? 12.614 22.499 43.169 1.00 21.81 ? 207 MET A O 1 ATOM 2975 C CB . MET A 1 199 ? 10.345 21.878 44.982 1.00 20.27 ? 207 MET A CB 1 ATOM 2976 C CG . MET A 1 199 ? 9.147 22.159 45.836 1.00 21.66 ? 207 MET A CG 1 ATOM 2977 S SD . MET A 1 199 ? 7.804 21.016 45.465 1.00 23.03 ? 207 MET A SD 1 ATOM 2978 C CE . MET A 1 199 ? 6.569 21.574 46.605 1.00 25.52 ? 207 MET A CE 1 ATOM 2979 H H . MET A 1 199 ? 10.687 24.268 44.240 1.00 26.72 ? 207 MET A H 1 ATOM 2980 H HA . MET A 1 199 ? 11.766 22.738 46.199 1.00 25.14 ? 207 MET A HA 1 ATOM 2981 H HB2 . MET A 1 199 ? 10.079 21.979 44.054 1.00 24.33 ? 207 MET A HB2 1 ATOM 2982 H HB3 . MET A 1 199 ? 10.621 20.964 45.148 1.00 24.33 ? 207 MET A HB3 1 ATOM 2983 H HG2 . MET A 1 199 ? 9.387 22.055 46.770 1.00 25.99 ? 207 MET A HG2 1 ATOM 2984 H HG3 . MET A 1 199 ? 8.835 23.062 45.667 1.00 25.99 ? 207 MET A HG3 1 ATOM 2985 H HE1 . MET A 1 199 ? 5.775 21.026 46.503 1.00 30.62 ? 207 MET A HE1 1 ATOM 2986 H HE2 . MET A 1 199 ? 6.913 21.494 47.508 1.00 30.62 ? 207 MET A HE2 1 ATOM 2987 H HE3 . MET A 1 199 ? 6.358 22.502 46.412 1.00 30.62 ? 207 MET A HE3 1 ATOM 2988 N N . ALA A 1 200 ? 13.745 21.865 45.018 1.00 20.62 ? 208 ALA A N 1 ATOM 2989 C CA . ALA A 1 200 ? 14.904 21.418 44.254 1.00 20.70 ? 208 ALA A CA 1 ATOM 2990 C C . ALA A 1 200 ? 14.617 20.138 43.476 1.00 18.96 ? 208 ALA A C 1 ATOM 2991 O O . ALA A 1 200 ? 15.095 19.978 42.351 1.00 19.33 ? 208 ALA A O 1 ATOM 2992 C CB . ALA A 1 200 ? 16.094 21.196 45.182 1.00 23.32 ? 208 ALA A CB 1 ATOM 2993 H H . ALA A 1 200 ? 13.815 21.765 45.869 1.00 24.74 ? 208 ALA A H 1 ATOM 2994 H HA . ALA A 1 200 ? 15.146 22.108 43.617 1.00 24.84 ? 208 ALA A HA 1 ATOM 2995 H HB1 . ALA A 1 200 ? 16.853 20.900 44.656 1.00 27.98 ? 208 ALA A HB1 1 ATOM 2996 H HB2 . ALA A 1 200 ? 16.306 22.030 45.629 1.00 27.98 ? 208 ALA A HB2 1 ATOM 2997 H HB3 . ALA A 1 200 ? 15.861 20.519 45.837 1.00 27.98 ? 208 ALA A HB3 1 ATOM 2998 N N . ASP A 1 201 ? 13.890 19.194 44.076 1.00 16.94 ? 209 ASP A N 1 ATOM 2999 C CA . ASP A 1 201 ? 13.614 17.887 43.475 1.00 15.56 ? 209 ASP A CA 1 ATOM 3000 C C . ASP A 1 201 ? 12.166 17.535 43.775 1.00 15.46 ? 209 ASP A C 1 ATOM 3001 O O . ASP A 1 201 ? 11.876 16.661 44.598 1.00 16.15 ? 209 ASP A O 1 ATOM 3002 C CB . ASP A 1 201 ? 14.571 16.832 44.039 1.00 16.12 ? 209 ASP A CB 1 ATOM 3003 C CG . ASP A 1 201 ? 14.483 15.500 43.311 1.00 15.71 ? 209 ASP A CG 1 ATOM 3004 O OD1 . ASP A 1 201 ? 13.786 15.431 42.270 1.00 16.03 ? 209 ASP A OD1 1 ATOM 3005 O OD2 . ASP A 1 201 ? 15.125 14.523 43.723 1.00 17.17 ? 209 ASP A OD2 1 ATOM 3006 H H . ASP A 1 201 ? 13.536 19.290 44.854 1.00 20.33 ? 209 ASP A H 1 ATOM 3007 H HA . ASP A 1 201 ? 13.732 17.935 42.514 1.00 18.67 ? 209 ASP A HA 1 ATOM 3008 H HB2 . ASP A 1 201 ? 15.482 17.157 43.958 1.00 19.35 ? 209 ASP A HB2 1 ATOM 3009 H HB3 . ASP A 1 201 ? 14.357 16.677 44.972 1.00 19.35 ? 209 ASP A HB3 1 ATOM 3010 N N . PRO A 1 202 ? 11.225 18.207 43.125 1.00 15.35 ? 210 PRO A N 1 ATOM 3011 C CA . PRO A 1 202 ? 9.807 17.942 43.398 1.00 15.27 ? 210 PRO A CA 1 ATOM 3012 C C . PRO A 1 202 ? 9.458 16.475 43.207 1.00 15.00 ? 210 PRO A C 1 ATOM 3013 O O . PRO A 1 202 ? 9.770 15.872 42.181 1.00 14.92 ? 210 PRO A O 1 ATOM 3014 C CB . PRO A 1 202 ? 9.068 18.865 42.412 1.00 16.12 ? 210 PRO A CB 1 ATOM 3015 C CG . PRO A 1 202 ? 10.064 19.215 41.389 1.00 15.95 ? 210 PRO A CG 1 ATOM 3016 C CD . PRO A 1 202 ? 11.407 19.210 42.080 1.00 14.99 ? 210 PRO A CD 1 ATOM 3017 H HA . PRO A 1 202 ? 9.587 18.206 44.305 1.00 18.32 ? 210 PRO A HA 1 ATOM 3018 H HB2 . PRO A 1 202 ? 8.322 18.388 42.015 1.00 19.35 ? 210 PRO A HB2 1 ATOM 3019 H HB3 . PRO A 1 202 ? 8.760 19.659 42.876 1.00 19.35 ? 210 PRO A HB3 1 ATOM 3020 H HG2 . PRO A 1 202 ? 10.046 18.553 40.680 1.00 19.14 ? 210 PRO A HG2 1 ATOM 3021 H HG3 . PRO A 1 202 ? 9.868 20.096 41.035 1.00 19.14 ? 210 PRO A HG3 1 ATOM 3022 H HD2 . PRO A 1 202 ? 12.105 18.937 41.465 1.00 17.99 ? 210 PRO A HD2 1 ATOM 3023 H HD3 . PRO A 1 202 ? 11.591 20.078 42.470 1.00 17.99 ? 210 PRO A HD3 1 ATOM 3024 N N . GLY A 1 203 ? 8.780 15.923 44.201 1.00 16.64 ? 211 GLY A N 1 ATOM 3025 C CA . GLY A 1 203 ? 8.380 14.531 44.218 1.00 16.43 ? 211 GLY A CA 1 ATOM 3026 C C . GLY A 1 203 ? 9.532 13.549 44.279 1.00 15.20 ? 211 GLY A C 1 ATOM 3027 O O . GLY A 1 203 ? 9.335 12.341 44.128 1.00 17.02 ? 211 GLY A O 1 ATOM 3028 H H . GLY A 1 203 ? 8.531 16.354 44.902 1.00 19.96 ? 211 GLY A H 1 ATOM 3029 H HA2 . GLY A 1 203 ? 7.812 14.375 44.989 1.00 19.71 ? 211 GLY A HA2 1 ATOM 3030 H HA3 . GLY A 1 203 ? 7.864 14.340 43.419 1.00 19.71 ? 211 GLY A HA3 1 ATOM 3031 N N . GLU A 1 204 ? 10.735 14.060 44.505 1.00 15.23 ? 212 GLU A N 1 ATOM 3032 C CA . GLU A 1 204 ? 11.964 13.262 44.475 1.00 15.37 ? 212 GLU A CA 1 ATOM 3033 C C . GLU A 1 204 ? 12.154 12.531 43.151 1.00 14.07 ? 212 GLU A C 1 ATOM 3034 O O . GLU A 1 204 ? 12.767 11.466 43.102 1.00 14.81 ? 212 GLU A O 1 ATOM 3035 C CB . GLU A 1 204 ? 12.067 12.292 45.654 1.00 19.49 ? 212 GLU A CB 1 ATOM 3036 C CG . GLU A 1 204 ? 12.175 13.030 47.005 1.00 27.19 ? 212 GLU A CG 1 ATOM 3037 C CD . GLU A 1 204 ? 12.840 12.179 48.072 1.00 36.16 ? 212 GLU A CD 1 ATOM 3038 O OE1 . GLU A 1 204 ? 12.321 11.078 48.347 1.00 39.72 ? 212 GLU A OE1 1 ATOM 3039 O OE2 . GLU A 1 204 ? 13.887 12.598 48.634 1.00 40.16 ? 212 GLU A OE2 1 ATOM 3040 H H . GLU A 1 204 ? 10.873 14.890 44.682 1.00 18.28 ? 212 GLU A H 1 ATOM 3041 H HA . GLU A 1 204 ? 12.710 13.876 44.560 1.00 18.45 ? 212 GLU A HA 1 ATOM 3042 H HB2 . GLU A 1 204 ? 11.274 11.734 45.677 1.00 23.38 ? 212 GLU A HB2 1 ATOM 3043 H HB3 . GLU A 1 204 ? 12.859 11.743 45.546 1.00 23.38 ? 212 GLU A HB3 1 ATOM 3044 H HG2 . GLU A 1 204 ? 12.705 13.834 46.886 1.00 32.62 ? 212 GLU A HG2 1 ATOM 3045 H HG3 . GLU A 1 204 ? 11.285 13.260 47.313 1.00 32.62 ? 212 GLU A HG3 1 ATOM 3046 N N . GLN A 1 205 ? 11.610 13.097 42.071 1.00 13.01 ? 213 GLN A N 1 ATOM 3047 C CA . GLN A 1 205 ? 11.670 12.406 40.795 1.00 12.56 ? 213 GLN A CA 1 ATOM 3048 C C . GLN A 1 205 ? 13.095 12.252 40.282 1.00 13.23 ? 213 GLN A C 1 ATOM 3049 O O . GLN A 1 205 ? 13.413 11.244 39.645 1.00 12.71 ? 213 GLN A O 1 ATOM 3050 C CB . GLN A 1 205 ? 10.772 13.085 39.763 1.00 12.58 ? 213 GLN A CB 1 ATOM 3051 C CG . GLN A 1 205 ? 10.694 12.305 38.449 1.00 12.27 ? 213 GLN A CG 1 ATOM 3052 C CD . GLN A 1 205 ? 9.724 12.911 37.447 1.00 12.43 ? 213 GLN A CD 1 ATOM 3053 O OE1 . GLN A 1 205 ? 8.877 12.215 36.883 1.00 12.97 ? 213 GLN A OE1 1 ATOM 3054 N NE2 . GLN A 1 205 ? 9.828 14.205 37.216 1.00 12.81 ? 213 GLN A NE2 1 ATOM 3055 H H . GLN A 1 205 ? 11.213 13.859 42.055 1.00 15.61 ? 213 GLN A H 1 ATOM 3056 H HA . GLN A 1 205 ? 11.320 11.510 40.926 1.00 15.07 ? 213 GLN A HA 1 ATOM 3057 H HB2 . GLN A 1 205 ? 9.874 13.158 40.123 1.00 15.09 ? 213 GLN A HB2 1 ATOM 3058 H HB3 . GLN A 1 205 ? 11.124 13.968 39.568 1.00 15.09 ? 213 GLN A HB3 1 ATOM 3059 H HG2 . GLN A 1 205 ? 11.574 12.289 38.041 1.00 14.73 ? 213 GLN A HG2 1 ATOM 3060 H HG3 . GLN A 1 205 ? 10.401 11.400 38.638 1.00 14.73 ? 213 GLN A HG3 1 ATOM 3061 H HE21 . GLN A 1 205 ? 10.426 14.668 37.625 1.00 15.37 ? 213 GLN A HE21 1 ATOM 3062 H HE22 . GLN A 1 205 ? 9.298 14.585 36.656 1.00 15.37 ? 213 GLN A HE22 1 ATOM 3063 N N . PHE A 1 206 ? 13.950 13.258 40.456 1.00 12.20 ? 214 PHE A N 1 ATOM 3064 C CA . PHE A 1 206 ? 15.315 13.118 39.967 1.00 12.63 ? 214 PHE A CA 1 ATOM 3065 C C . PHE A 1 206 ? 16.088 12.060 40.746 1.00 13.05 ? 214 PHE A C 1 ATOM 3066 O O . PHE A 1 206 ? 16.853 11.293 40.158 1.00 13.98 ? 214 PHE A O 1 ATOM 3067 C CB . PHE A 1 206 ? 16.079 14.437 40.053 1.00 14.01 ? 214 PHE A CB 1 ATOM 3068 C CG . PHE A 1 206 ? 15.687 15.454 39.017 1.00 14.74 ? 214 PHE A CG 1 ATOM 3069 C CD1 . PHE A 1 206 ? 15.816 15.176 37.669 1.00 15.62 ? 214 PHE A CD1 1 ATOM 3070 C CD2 . PHE A 1 206 ? 15.251 16.712 39.389 1.00 16.67 ? 214 PHE A CD2 1 ATOM 3071 C CE1 . PHE A 1 206 ? 15.497 16.136 36.708 1.00 17.41 ? 214 PHE A CE1 1 ATOM 3072 C CE2 . PHE A 1 206 ? 14.939 17.663 38.440 1.00 18.09 ? 214 PHE A CE2 1 ATOM 3073 C CZ . PHE A 1 206 ? 15.067 17.366 37.107 1.00 17.57 ? 214 PHE A CZ 1 ATOM 3074 H H . PHE A 1 206 ? 13.772 14.006 40.841 1.00 14.64 ? 214 PHE A H 1 ATOM 3075 H HA . PHE A 1 206 ? 15.290 12.847 39.036 1.00 15.16 ? 214 PHE A HA 1 ATOM 3076 H HB2 . PHE A 1 206 ? 15.921 14.831 40.926 1.00 16.82 ? 214 PHE A HB2 1 ATOM 3077 H HB3 . PHE A 1 206 ? 17.026 14.255 39.944 1.00 16.82 ? 214 PHE A HB3 1 ATOM 3078 H HD1 . PHE A 1 206 ? 16.121 14.339 37.399 1.00 18.75 ? 214 PHE A HD1 1 ATOM 3079 H HD2 . PHE A 1 206 ? 15.174 16.923 40.292 1.00 20.00 ? 214 PHE A HD2 1 ATOM 3080 H HE1 . PHE A 1 206 ? 15.577 15.938 35.803 1.00 20.89 ? 214 PHE A HE1 1 ATOM 3081 H HE2 . PHE A 1 206 ? 14.637 18.503 38.703 1.00 21.70 ? 214 PHE A HE2 1 ATOM 3082 H HZ . PHE A 1 206 ? 14.840 18.004 36.469 1.00 21.09 ? 214 PHE A HZ 1 ATOM 3083 N N . ARG A 1 207 ? 15.925 12.040 42.071 1.00 13.42 ? 215 ARG A N 1 ATOM 3084 C CA . ARG A 1 207 ? 16.541 10.999 42.891 1.00 14.22 ? 215 ARG A CA 1 ATOM 3085 C C . ARG A 1 207 ? 16.052 9.618 42.463 1.00 13.70 ? 215 ARG A C 1 ATOM 3086 O O . ARG A 1 207 ? 16.848 8.700 42.252 1.00 13.55 ? 215 ARG A O 1 ATOM 3087 C CB . ARG A 1 207 ? 16.211 11.267 44.361 1.00 14.63 ? 215 ARG A CB 1 ATOM 3088 C CG . ARG A 1 207 ? 16.768 10.234 45.313 1.00 15.48 ? 215 ARG A CG 1 ATOM 3089 C CD . ARG A 1 207 ? 16.460 10.616 46.748 1.00 17.92 ? 215 ARG A CD 1 ATOM 3090 N NE . ARG A 1 207 ? 17.080 9.695 47.690 1.00 17.40 ? 215 ARG A NE 1 ATOM 3091 C CZ . ARG A 1 207 ? 17.311 9.987 48.959 1.00 19.15 ? 215 ARG A CZ 1 ATOM 3092 N NH1 . ARG A 1 207 ? 16.986 11.181 49.429 1.00 21.77 ? 215 ARG A NH1 1 ATOM 3093 N NH2 . ARG A 1 207 ? 17.892 9.098 49.745 1.00 18.36 ? 215 ARG A NH2 1 ATOM 3094 H H . ARG A 1 207 ? 15.464 12.615 42.516 1.00 16.10 ? 215 ARG A H 1 ATOM 3095 H HA . ARG A 1 207 ? 17.505 11.031 42.782 1.00 17.06 ? 215 ARG A HA 1 ATOM 3096 H HB2 . ARG A 1 207 ? 16.579 12.129 44.612 1.00 17.56 ? 215 ARG A HB2 1 ATOM 3097 H HB3 . ARG A 1 207 ? 15.247 11.278 44.467 1.00 17.56 ? 215 ARG A HB3 1 ATOM 3098 H HG2 . ARG A 1 207 ? 16.360 9.373 45.130 1.00 18.57 ? 215 ARG A HG2 1 ATOM 3099 H HG3 . ARG A 1 207 ? 17.731 10.183 45.208 1.00 18.57 ? 215 ARG A HG3 1 ATOM 3100 H HD2 . ARG A 1 207 ? 16.804 11.506 46.923 1.00 21.50 ? 215 ARG A HD2 1 ATOM 3101 H HD3 . ARG A 1 207 ? 15.500 10.593 46.887 1.00 21.50 ? 215 ARG A HD3 1 ATOM 3102 H HE . ARG A 1 207 ? 17.404 8.961 47.381 1.00 20.88 ? 215 ARG A HE 1 ATOM 3103 H HH11 . ARG A 1 207 ? 16.613 11.760 48.914 1.00 26.13 ? 215 ARG A HH11 1 ATOM 3104 H HH12 . ARG A 1 207 ? 17.138 11.374 50.254 1.00 26.13 ? 215 ARG A HH12 1 ATOM 3105 H HH21 . ARG A 1 207 ? 18.104 8.324 49.436 1.00 22.04 ? 215 ARG A HH21 1 ATOM 3106 H HH22 . ARG A 1 207 ? 18.043 9.287 50.570 1.00 22.04 ? 215 ARG A HH22 1 ATOM 3107 N N . TRP A 1 208 ? 14.733 9.465 42.320 1.00 13.75 ? 216 TRP A N 1 ATOM 3108 C CA . TRP A 1 208 ? 14.145 8.214 41.843 1.00 13.47 ? 216 TRP A CA 1 ATOM 3109 C C . TRP A 1 208 ? 14.696 7.819 40.481 1.00 11.98 ? 216 TRP A C 1 ATOM 3110 O O . TRP A 1 208 ? 15.064 6.666 40.268 1.00 12.87 ? 216 TRP A O 1 ATOM 3111 C CB . TRP A 1 208 ? 12.621 8.383 41.782 1.00 12.87 ? 216 TRP A CB 1 ATOM 3112 C CG . TRP A 1 208 ? 11.917 7.256 41.134 1.00 12.88 ? 216 TRP A CG 1 ATOM 3113 C CD1 . TRP A 1 208 ? 11.523 6.086 41.718 1.00 13.56 ? 216 TRP A CD1 1 ATOM 3114 C CD2 . TRP A 1 208 ? 11.476 7.196 39.774 1.00 13.23 ? 216 TRP A CD2 1 ATOM 3115 N NE1 . TRP A 1 208 ? 10.875 5.292 40.792 1.00 15.03 ? 216 TRP A NE1 1 ATOM 3116 C CE2 . TRP A 1 208 ? 10.855 5.941 39.587 1.00 14.18 ? 216 TRP A CE2 1 ATOM 3117 C CE3 . TRP A 1 208 ? 11.590 8.064 38.696 1.00 14.04 ? 216 TRP A CE3 1 ATOM 3118 C CZ2 . TRP A 1 208 ? 10.289 5.559 38.367 1.00 14.72 ? 216 TRP A CZ2 1 ATOM 3119 C CZ3 . TRP A 1 208 ? 11.040 7.678 37.479 1.00 14.74 ? 216 TRP A CZ3 1 ATOM 3120 C CH2 . TRP A 1 208 ? 10.410 6.426 37.328 1.00 15.53 ? 216 TRP A CH2 1 ATOM 3121 H H . TRP A 1 208 ? 14.154 10.077 42.494 1.00 16.50 ? 216 TRP A H 1 ATOM 3122 H HA . TRP A 1 208 ? 14.348 7.503 42.472 1.00 16.16 ? 216 TRP A HA 1 ATOM 3123 H HB2 . TRP A 1 208 ? 12.279 8.464 42.686 1.00 15.44 ? 216 TRP A HB2 1 ATOM 3124 H HB3 . TRP A 1 208 ? 12.416 9.187 41.280 1.00 15.44 ? 216 TRP A HB3 1 ATOM 3125 H HD1 . TRP A 1 208 ? 11.671 5.858 42.607 1.00 16.27 ? 216 TRP A HD1 1 ATOM 3126 H HE1 . TRP A 1 208 ? 10.551 4.510 40.944 1.00 18.04 ? 216 TRP A HE1 1 ATOM 3127 H HE3 . TRP A 1 208 ? 12.005 8.891 38.792 1.00 16.85 ? 216 TRP A HE3 1 ATOM 3128 H HZ2 . TRP A 1 208 ? 9.878 4.731 38.262 1.00 17.66 ? 216 TRP A HZ2 1 ATOM 3129 H HZ3 . TRP A 1 208 ? 11.104 8.248 36.747 1.00 17.69 ? 216 TRP A HZ3 1 ATOM 3130 H HH2 . TRP A 1 208 ? 10.058 6.193 36.499 1.00 18.64 ? 216 TRP A HH2 1 ATOM 3131 N N . LEU A 1 209 ? 14.758 8.778 39.555 1.00 11.90 ? 217 LEU A N 1 ATOM 3132 C CA . LEU A 1 209 ? 15.211 8.483 38.203 1.00 11.73 ? 217 LEU A CA 1 ATOM 3133 C C . LEU A 1 209 ? 16.633 7.949 38.215 1.00 12.26 ? 217 LEU A C 1 ATOM 3134 O O . LEU A 1 209 ? 16.932 6.931 37.579 1.00 12.97 ? 217 LEU A O 1 ATOM 3135 C CB . LEU A 1 209 ? 15.107 9.746 37.353 1.00 13.17 ? 217 LEU A CB 1 ATOM 3136 C CG . LEU A 1 209 ? 15.587 9.627 35.920 1.00 13.02 ? 217 LEU A CG 1 ATOM 3137 C CD1 . LEU A 1 209 ? 14.917 8.465 35.183 1.00 14.03 ? 217 LEU A CD1 1 ATOM 3138 C CD2 . LEU A 1 209 ? 15.352 10.923 35.190 1.00 14.74 ? 217 LEU A CD2 1 ATOM 3139 H H . LEU A 1 209 ? 14.545 9.601 39.687 1.00 14.28 ? 217 LEU A H 1 ATOM 3140 H HA . LEU A 1 209 ? 14.635 7.806 37.814 1.00 14.07 ? 217 LEU A HA 1 ATOM 3141 H HB2 . LEU A 1 209 ? 14.176 10.017 37.324 1.00 15.81 ? 217 LEU A HB2 1 ATOM 3142 H HB3 . LEU A 1 209 ? 15.632 10.442 37.776 1.00 15.81 ? 217 LEU A HB3 1 ATOM 3143 H HG . LEU A 1 209 ? 16.543 9.460 35.925 1.00 15.62 ? 217 LEU A HG 1 ATOM 3144 H HD11 . LEU A 1 209 ? 15.255 8.431 34.274 1.00 16.83 ? 217 LEU A HD11 1 ATOM 3145 H HD12 . LEU A 1 209 ? 15.123 7.638 35.644 1.00 16.83 ? 217 LEU A HD12 1 ATOM 3146 H HD13 . LEU A 1 209 ? 13.958 8.610 35.173 1.00 16.83 ? 217 LEU A HD13 1 ATOM 3147 H HD21 . LEU A 1 209 ? 15.664 10.832 34.276 1.00 17.69 ? 217 LEU A HD21 1 ATOM 3148 H HD22 . LEU A 1 209 ? 14.402 11.122 35.197 1.00 17.69 ? 217 LEU A HD22 1 ATOM 3149 H HD23 . LEU A 1 209 ? 15.842 11.631 35.637 1.00 17.69 ? 217 LEU A HD23 1 ATOM 3150 N N . GLY A 1 210 ? 17.528 8.616 38.958 1.00 13.09 ? 218 GLY A N 1 ATOM 3151 C CA . GLY A 1 210 ? 18.887 8.124 39.066 1.00 13.37 ? 218 GLY A CA 1 ATOM 3152 C C . GLY A 1 210 ? 18.931 6.719 39.621 1.00 13.99 ? 218 GLY A C 1 ATOM 3153 O O . GLY A 1 210 ? 19.706 5.889 39.163 1.00 14.06 ? 218 GLY A O 1 ATOM 3154 H H . GLY A 1 210 ? 17.368 9.339 39.396 1.00 15.71 ? 218 GLY A H 1 ATOM 3155 H HA2 . GLY A 1 210 ? 19.303 8.124 38.190 1.00 16.05 ? 218 GLY A HA2 1 ATOM 3156 H HA3 . GLY A 1 210 ? 19.397 8.704 39.652 1.00 16.05 ? 218 GLY A HA3 1 ATOM 3157 N N . ASP A 1 211 ? 18.138 6.451 40.653 1.00 13.81 ? 219 ASP A N 1 ATOM 3158 C CA . ASP A 1 211 ? 18.091 5.116 41.224 1.00 13.78 ? 219 ASP A CA 1 ATOM 3159 C C . ASP A 1 211 ? 17.594 4.072 40.234 1.00 13.19 ? 219 ASP A C 1 ATOM 3160 O O . ASP A 1 211 ? 18.123 2.959 40.188 1.00 14.46 ? 219 ASP A O 1 ATOM 3161 C CB . ASP A 1 211 ? 17.255 5.115 42.504 1.00 15.15 ? 219 ASP A CB 1 ATOM 3162 C CG . ASP A 1 211 ? 17.913 5.863 43.657 1.00 18.46 ? 219 ASP A CG 1 ATOM 3163 O OD1 . ASP A 1 211 ? 19.093 6.257 43.557 1.00 19.97 ? 219 ASP A OD1 1 ATOM 3164 O OD2 . ASP A 1 211 ? 17.217 6.028 44.667 1.00 22.76 ? 219 ASP A OD2 1 ATOM 3165 H H . ASP A 1 211 ? 17.621 7.022 41.036 1.00 16.57 ? 219 ASP A H 1 ATOM 3166 H HA . ASP A 1 211 ? 18.994 4.864 41.473 1.00 16.53 ? 219 ASP A HA 1 ATOM 3167 H HB2 . ASP A 1 211 ? 16.402 5.539 42.322 1.00 18.18 ? 219 ASP A HB2 1 ATOM 3168 H HB3 . ASP A 1 211 ? 17.115 4.197 42.786 1.00 18.18 ? 219 ASP A HB3 1 ATOM 3169 N N . VAL A 1 212 ? 16.550 4.387 39.470 1.00 13.24 ? 220 VAL A N 1 ATOM 3170 C CA . VAL A 1 212 ? 16.067 3.461 38.451 1.00 13.03 ? 220 VAL A CA 1 ATOM 3171 C C . VAL A 1 212 ? 17.150 3.183 37.431 1.00 13.28 ? 220 VAL A C 1 ATOM 3172 O O . VAL A 1 212 ? 17.343 2.042 36.996 1.00 13.51 ? 220 VAL A O 1 ATOM 3173 C CB . VAL A 1 212 ? 14.810 4.030 37.768 1.00 13.88 ? 220 VAL A CB 1 ATOM 3174 C CG1 . VAL A 1 212 ? 14.449 3.194 36.537 1.00 15.54 ? 220 VAL A CG1 1 ATOM 3175 C CG2 . VAL A 1 212 ? 13.669 4.077 38.723 1.00 15.14 ? 220 VAL A CG2 1 ATOM 3176 H H . VAL A 1 212 ? 16.109 5.123 39.521 1.00 15.89 ? 220 VAL A H 1 ATOM 3177 H HA . VAL A 1 212 ? 15.828 2.621 38.873 1.00 15.64 ? 220 VAL A HA 1 ATOM 3178 H HB . VAL A 1 212 ? 14.992 4.936 37.473 1.00 16.66 ? 220 VAL A HB 1 ATOM 3179 H HG11 . VAL A 1 212 ? 13.656 3.568 36.123 1.00 18.65 ? 220 VAL A HG11 1 ATOM 3180 H HG12 . VAL A 1 212 ? 15.191 3.216 35.912 1.00 18.65 ? 220 VAL A HG12 1 ATOM 3181 H HG13 . VAL A 1 212 ? 14.278 2.280 36.815 1.00 18.65 ? 220 VAL A HG13 1 ATOM 3182 H HG21 . VAL A 1 212 ? 12.892 4.438 38.268 1.00 18.17 ? 220 VAL A HG21 1 ATOM 3183 H HG22 . VAL A 1 212 ? 13.482 3.178 39.035 1.00 18.17 ? 220 VAL A HG22 1 ATOM 3184 H HG23 . VAL A 1 212 ? 13.908 4.645 39.472 1.00 18.17 ? 220 VAL A HG23 1 ATOM 3185 N N . LEU A 1 213 ? 17.842 4.223 36.999 1.00 13.35 ? 221 LEU A N 1 ATOM 3186 C CA . LEU A 1 213 ? 18.861 4.046 35.981 1.00 13.39 ? 221 LEU A CA 1 ATOM 3187 C C . LEU A 1 213 ? 20.078 3.305 36.521 1.00 14.29 ? 221 LEU A C 1 ATOM 3188 O O . LEU A 1 213 ? 20.681 2.520 35.779 1.00 14.77 ? 221 LEU A O 1 ATOM 3189 C CB . LEU A 1 213 ? 19.229 5.401 35.361 1.00 13.32 ? 221 LEU A CB 1 ATOM 3190 C CG . LEU A 1 213 ? 18.066 6.117 34.657 1.00 13.19 ? 221 LEU A CG 1 ATOM 3191 C CD1 . LEU A 1 213 ? 18.456 7.508 34.282 1.00 14.40 ? 221 LEU A CD1 1 ATOM 3192 C CD2 . LEU A 1 213 ? 17.580 5.334 33.425 1.00 15.69 ? 221 LEU A CD2 1 ATOM 3193 H H . LEU A 1 213 ? 17.745 5.032 37.275 1.00 16.02 ? 221 LEU A H 1 ATOM 3194 H HA . LEU A 1 213 ? 18.486 3.501 35.272 1.00 16.07 ? 221 LEU A HA 1 ATOM 3195 H HB2 . LEU A 1 213 ? 19.552 5.987 36.064 1.00 15.98 ? 221 LEU A HB2 1 ATOM 3196 H HB3 . LEU A 1 213 ? 19.930 5.262 34.705 1.00 15.98 ? 221 LEU A HB3 1 ATOM 3197 H HG . LEU A 1 213 ? 17.322 6.178 35.276 1.00 15.82 ? 221 LEU A HG 1 ATOM 3198 H HD11 . LEU A 1 213 ? 17.707 7.938 33.841 1.00 17.27 ? 221 LEU A HD11 1 ATOM 3199 H HD12 . LEU A 1 213 ? 18.691 7.997 35.087 1.00 17.27 ? 221 LEU A HD12 1 ATOM 3200 H HD13 . LEU A 1 213 ? 19.217 7.472 33.683 1.00 17.27 ? 221 LEU A HD13 1 ATOM 3201 H HD21 . LEU A 1 213 ? 16.849 5.818 33.012 1.00 18.83 ? 221 LEU A HD21 1 ATOM 3202 H HD22 . LEU A 1 213 ? 18.315 5.246 32.798 1.00 18.83 ? 221 LEU A HD22 1 ATOM 3203 H HD23 . LEU A 1 213 ? 17.279 4.456 33.707 1.00 18.83 ? 221 LEU A HD23 1 ATOM 3204 N N . SER A 1 214 ? 20.433 3.518 37.794 1.00 14.60 ? 222 SER A N 1 ATOM 3205 C CA . SER A 1 214 ? 21.488 2.715 38.399 1.00 15.08 ? 222 SER A CA 1 ATOM 3206 C C . SER A 1 214 ? 21.082 1.258 38.476 1.00 14.50 ? 222 SER A C 1 ATOM 3207 O O . SER A 1 214 ? 21.881 0.368 38.170 1.00 15.74 ? 222 SER A O 1 ATOM 3208 C CB . SER A 1 214 ? 21.766 3.241 39.799 1.00 16.71 ? 222 SER A CB 1 ATOM 3209 O OG . SER A 1 214 ? 22.368 4.514 39.745 1.00 18.43 ? 222 SER A OG 1 ATOM 3210 H H . SER A 1 214 ? 20.085 4.109 38.314 1.00 17.52 ? 222 SER A H 1 ATOM 3211 H HA . SER A 1 214 ? 22.299 2.787 37.871 1.00 18.09 ? 222 SER A HA 1 ATOM 3212 H HB2 . SER A 1 214 ? 20.929 3.307 40.284 1.00 20.06 ? 222 SER A HB2 1 ATOM 3213 H HB3 . SER A 1 214 ? 22.365 2.627 40.254 1.00 20.06 ? 222 SER A HB3 1 ATOM 3214 H HG . SER A 1 214 ? 21.860 5.055 39.353 1.00 22.12 ? 222 SER A HG 1 ATOM 3215 N N . ASN A 1 215 ? 19.817 0.999 38.818 1.00 14.86 ? 223 ASN A N 1 ATOM 3216 C CA . ASN A 1 215 ? 19.328 -0.377 38.833 1.00 15.24 ? 223 ASN A CA 1 ATOM 3217 C C . ASN A 1 215 ? 19.388 -0.995 37.448 1.00 15.63 ? 223 ASN A C 1 ATOM 3218 O O . ASN A 1 215 ? 19.744 -2.166 37.301 1.00 16.69 ? 223 ASN A O 1 ATOM 3219 C CB . ASN A 1 215 ? 17.900 -0.427 39.353 1.00 16.48 ? 223 ASN A CB 1 ATOM 3220 C CG . ASN A 1 215 ? 17.800 -0.416 40.852 1.00 19.58 ? 223 ASN A CG 1 ATOM 3221 O OD1 . ASN A 1 215 ? 18.791 -0.296 41.604 1.00 20.71 ? 223 ASN A OD1 1 ATOM 3222 N ND2 . ASN A 1 215 ? 16.566 -0.568 41.317 1.00 19.86 ? 223 ASN A ND2 1 ATOM 3223 H H . ASN A 1 215 ? 19.235 1.591 39.042 1.00 17.83 ? 223 ASN A H 1 ATOM 3224 H HA . ASN A 1 215 ? 19.884 -0.907 39.425 1.00 18.29 ? 223 ASN A HA 1 ATOM 3225 H HB2 . ASN A 1 215 ? 17.418 0.346 39.018 1.00 19.77 ? 223 ASN A HB2 1 ATOM 3226 H HB3 . ASN A 1 215 ? 17.479 -1.241 39.034 1.00 19.77 ? 223 ASN A HB3 1 ATOM 3227 H HD21 . ASN A 1 215 ? 15.932 -0.693 40.749 1.00 23.84 ? 223 ASN A HD21 1 ATOM 3228 N N . ALA A 1 216 ? 19.040 -0.223 36.417 1.00 15.37 ? 224 ALA A N 1 ATOM 3229 C CA . ALA A 1 216 ? 19.086 -0.740 35.048 1.00 16.13 ? 224 ALA A CA 1 ATOM 3230 C C . ALA A 1 216 ? 20.497 -1.170 34.677 1.00 17.09 ? 224 ALA A C 1 ATOM 3231 O O . ALA A 1 216 ? 20.692 -2.235 34.075 1.00 18.12 ? 224 ALA A O 1 ATOM 3232 C CB . ALA A 1 216 ? 18.549 0.301 34.071 1.00 16.66 ? 224 ALA A CB 1 ATOM 3233 H H . ALA A 1 216 ? 18.777 0.593 36.481 1.00 18.45 ? 224 ALA A H 1 ATOM 3234 H HA . ALA A 1 216 ? 18.514 -1.521 34.991 1.00 19.36 ? 224 ALA A HA 1 ATOM 3235 H HB1 . ALA A 1 216 ? 18.588 -0.061 33.172 1.00 20.00 ? 224 ALA A HB1 1 ATOM 3236 H HB2 . ALA A 1 216 ? 17.631 0.509 34.305 1.00 20.00 ? 224 ALA A HB2 1 ATOM 3237 H HB3 . ALA A 1 216 ? 19.095 1.101 34.130 1.00 20.00 ? 224 ALA A HB3 1 ATOM 3238 N N . SER A 1 217 ? 21.499 -0.371 35.042 1.00 16.52 ? 225 SER A N 1 ATOM 3239 C CA . SER A 1 217 ? 22.889 -0.741 34.764 1.00 18.46 ? 225 SER A CA 1 ATOM 3240 C C . SER A 1 217 ? 23.249 -2.029 35.488 1.00 19.16 ? 225 SER A C 1 ATOM 3241 O O . SER A 1 217 ? 23.825 -2.942 34.894 1.00 19.49 ? 225 SER A O 1 ATOM 3242 C CB . SER A 1 217 ? 23.818 0.393 35.194 1.00 20.64 ? 225 SER A CB 1 ATOM 3243 O OG . SER A 1 217 ? 25.176 0.046 34.991 1.00 24.57 ? 225 SER A OG 1 ATOM 3244 H H . SER A 1 217 ? 21.405 0.382 35.447 1.00 19.82 ? 225 SER A H 1 ATOM 3245 H HA . SER A 1 217 ? 23.000 -0.884 33.811 1.00 22.15 ? 225 SER A HA 1 ATOM 3246 H HB2 . SER A 1 217 ? 23.613 1.183 34.670 1.00 24.76 ? 225 SER A HB2 1 ATOM 3247 H HB3 . SER A 1 217 ? 23.677 0.575 36.136 1.00 24.76 ? 225 SER A HB3 1 ATOM 3248 H HG . SER A 1 217 ? 25.313 -0.114 34.178 1.00 29.49 ? 225 SER A HG 1 ATOM 3249 N N . ARG A 1 218 ? 22.898 -2.120 36.776 1.00 17.65 ? 226 ARG A N 1 ATOM 3250 C CA . ARG A 1 218 ? 23.149 -3.332 37.551 1.00 18.04 ? 226 ARG A CA 1 ATOM 3251 C C . ARG A 1 218 ? 22.501 -4.544 36.910 1.00 18.66 ? 226 ARG A C 1 ATOM 3252 O O . ARG A 1 218 ? 23.088 -5.634 36.889 1.00 20.55 ? 226 ARG A O 1 ATOM 3253 C CB . ARG A 1 218 ? 22.595 -3.149 38.960 1.00 17.85 ? 226 ARG A CB 1 ATOM 3254 C CG . ARG A 1 218 ? 22.751 -4.339 39.881 1.00 18.77 ? 226 ARG A CG 1 ATOM 3255 C CD . ARG A 1 218 ? 21.903 -4.176 41.119 1.00 19.86 ? 226 ARG A CD 1 ATOM 3256 N NE . ARG A 1 218 ? 20.485 -4.156 40.785 1.00 20.39 ? 226 ARG A NE 1 ATOM 3257 C CZ . ARG A 1 218 ? 19.526 -3.645 41.547 1.00 20.34 ? 226 ARG A CZ 1 ATOM 3258 N NH1 . ARG A 1 218 ? 19.802 -3.115 42.742 1.00 20.80 ? 226 ARG A NH1 1 ATOM 3259 N NH2 . ARG A 1 218 ? 18.274 -3.678 41.092 1.00 21.23 ? 226 ARG A NH2 1 ATOM 3260 H H . ARG A 1 218 ? 22.513 -1.492 37.220 1.00 21.18 ? 226 ARG A H 1 ATOM 3261 H HA . ARG A 1 218 ? 24.105 -3.487 37.612 1.00 21.65 ? 226 ARG A HA 1 ATOM 3262 H HB2 . ARG A 1 218 ? 23.051 -2.399 39.374 1.00 21.42 ? 226 ARG A HB2 1 ATOM 3263 H HB3 . ARG A 1 218 ? 21.647 -2.954 38.895 1.00 21.42 ? 226 ARG A HB3 1 ATOM 3264 H HG2 . ARG A 1 218 ? 22.467 -5.143 39.419 1.00 22.53 ? 226 ARG A HG2 1 ATOM 3265 H HG3 . ARG A 1 218 ? 23.679 -4.415 40.154 1.00 22.53 ? 226 ARG A HG3 1 ATOM 3266 H HD2 . ARG A 1 218 ? 22.064 -4.921 41.719 1.00 23.83 ? 226 ARG A HD2 1 ATOM 3267 H HD3 . ARG A 1 218 ? 22.126 -3.338 41.553 1.00 23.83 ? 226 ARG A HD3 1 ATOM 3268 H HE . ARG A 1 218 ? 20.251 -4.504 40.034 1.00 24.47 ? 226 ARG A HE 1 ATOM 3269 H HH11 . ARG A 1 218 ? 20.614 -3.092 43.025 1.00 24.96 ? 226 ARG A HH11 1 ATOM 3270 H HH12 . ARG A 1 218 ? 19.169 -2.792 43.225 1.00 24.96 ? 226 ARG A HH12 1 ATOM 3271 H HH21 . ARG A 1 218 ? 18.104 -4.027 40.325 1.00 25.48 ? 226 ARG A HH21 1 ATOM 3272 H HH22 . ARG A 1 218 ? 17.634 -3.364 41.573 1.00 25.48 ? 226 ARG A HH22 1 ATOM 3273 N N . ASP A 1 219 ? 21.292 -4.378 36.387 1.00 19.29 ? 227 ASP A N 1 ATOM 3274 C CA . ASP A 1 219 ? 20.485 -5.499 35.938 1.00 20.08 ? 227 ASP A CA 1 ATOM 3275 C C . ASP A 1 219 ? 20.648 -5.791 34.453 1.00 20.59 ? 227 ASP A C 1 ATOM 3276 O O . ASP A 1 219 ? 19.964 -6.686 33.927 1.00 24.18 ? 227 ASP A O 1 ATOM 3277 C CB . ASP A 1 219 ? 19.018 -5.236 36.279 1.00 20.36 ? 227 ASP A CB 1 ATOM 3278 C CG . ASP A 1 219 ? 18.774 -5.171 37.780 1.00 22.77 ? 227 ASP A CG 1 ATOM 3279 O OD1 . ASP A 1 219 ? 19.584 -5.759 38.520 1.00 22.64 ? 227 ASP A OD1 1 ATOM 3280 O OD2 . ASP A 1 219 ? 17.799 -4.526 38.222 1.00 23.17 ? 227 ASP A OD2 1 ATOM 3281 H H . ASP A 1 219 ? 20.913 -3.614 36.281 1.00 23.15 ? 227 ASP A H 1 ATOM 3282 H HA . ASP A 1 219 ? 20.762 -6.292 36.424 1.00 24.10 ? 227 ASP A HA 1 ATOM 3283 H HB2 . ASP A 1 219 ? 18.751 -4.387 35.893 1.00 24.44 ? 227 ASP A HB2 1 ATOM 3284 H HB3 . ASP A 1 219 ? 18.475 -5.953 35.916 1.00 24.44 ? 227 ASP A HB3 1 ATOM 3285 N N . GLY A 1 220 ? 21.531 -5.069 33.766 1.00 19.11 ? 228 GLY A N 1 ATOM 3286 C CA . GLY A 1 220 ? 21.784 -5.361 32.366 1.00 19.73 ? 228 GLY A CA 1 ATOM 3287 C C . GLY A 1 220 ? 20.658 -4.938 31.445 1.00 19.26 ? 228 GLY A C 1 ATOM 3288 O O . GLY A 1 220 ? 20.490 -5.525 30.377 1.00 21.71 ? 228 GLY A O 1 ATOM 3289 H H . GLY A 1 220 ? 21.989 -4.414 34.085 1.00 22.93 ? 228 GLY A H 1 ATOM 3290 H HA2 . GLY A 1 220 ? 22.593 -4.905 32.086 1.00 23.68 ? 228 GLY A HA2 1 ATOM 3291 H HA3 . GLY A 1 220 ? 21.920 -6.316 32.260 1.00 23.68 ? 228 GLY A HA3 1 ATOM 3292 N N . GLU A 1 221 ? 19.883 -3.941 31.838 1.00 18.08 ? 229 GLU A N 1 ATOM 3293 C CA . GLU A 1 221 ? 18.762 -3.452 31.050 1.00 16.65 ? 229 GLU A CA 1 ATOM 3294 C C . GLU A 1 221 ? 19.130 -2.181 30.296 1.00 17.12 ? 229 GLU A C 1 ATOM 3295 O O . GLU A 1 221 ? 19.995 -1.415 30.714 1.00 20.04 ? 229 GLU A O 1 ATOM 3296 C CB . GLU A 1 221 ? 17.563 -3.138 31.958 1.00 18.30 ? 229 GLU A CB 1 ATOM 3297 C CG . GLU A 1 221 ? 16.947 -4.325 32.681 1.00 21.04 ? 229 GLU A CG 1 ATOM 3298 C CD . GLU A 1 221 ? 15.913 -3.900 33.710 1.00 25.33 ? 229 GLU A CD 1 ATOM 3299 O OE1 . GLU A 1 221 ? 15.962 -2.737 34.162 1.00 26.99 ? 229 GLU A OE1 1 ATOM 3300 O OE2 . GLU A 1 221 ? 15.057 -4.723 34.081 1.00 31.23 ? 229 GLU A OE2 1 ATOM 3301 H H . GLU A 1 221 ? 19.988 -3.519 32.580 1.00 21.70 ? 229 GLU A H 1 ATOM 3302 H HA . GLU A 1 221 ? 18.496 -4.127 30.407 1.00 19.99 ? 229 GLU A HA 1 ATOM 3303 H HB2 . GLU A 1 221 ? 17.850 -2.504 32.635 1.00 21.96 ? 229 GLU A HB2 1 ATOM 3304 H HB3 . GLU A 1 221 ? 16.866 -2.736 31.416 1.00 21.96 ? 229 GLU A HB3 1 ATOM 3305 H HG2 . GLU A 1 221 ? 16.509 -4.898 32.033 1.00 25.25 ? 229 GLU A HG2 1 ATOM 3306 H HG3 . GLU A 1 221 ? 17.647 -4.814 33.141 1.00 25.25 ? 229 GLU A HG3 1 ATOM 3307 N N . MET A 1 222 ? 18.444 -1.944 29.187 1.00 16.14 ? 230 MET A N 1 ATOM 3308 C CA A MET A 1 222 ? 18.452 -0.651 28.518 0.73 14.30 ? 230 MET A CA 1 ATOM 3309 C CA B MET A 1 222 ? 18.453 -0.650 28.520 0.27 14.79 ? 230 MET A CA 1 ATOM 3310 C C . MET A 1 222 ? 17.083 -0.016 28.701 1.00 14.42 ? 230 MET A C 1 ATOM 3311 O O . MET A 1 222 ? 16.087 -0.707 28.920 1.00 15.11 ? 230 MET A O 1 ATOM 3312 C CB A MET A 1 222 ? 18.761 -0.800 27.024 0.73 16.02 ? 230 MET A CB 1 ATOM 3313 C CB B MET A 1 222 ? 18.779 -0.786 27.029 0.27 15.13 ? 230 MET A CB 1 ATOM 3314 C CG A MET A 1 222 ? 20.162 -1.340 26.734 0.73 18.40 ? 230 MET A CG 1 ATOM 3315 C CG B MET A 1 222 ? 20.236 -1.139 26.741 0.27 15.37 ? 230 MET A CG 1 ATOM 3316 S SD A MET A 1 222 ? 21.516 -0.259 27.261 0.73 19.08 ? 230 MET A SD 1 ATOM 3317 S SD B MET A 1 222 ? 21.440 0.096 27.288 0.27 13.75 ? 230 MET A SD 1 ATOM 3318 C CE A MET A 1 222 ? 21.219 1.197 26.227 0.73 16.10 ? 230 MET A CE 1 ATOM 3319 C CE B MET A 1 222 ? 22.947 -0.764 26.863 0.27 11.38 ? 230 MET A CE 1 ATOM 3320 H H . MET A 1 222 ? 17.955 -2.532 28.794 1.00 19.37 ? 230 MET A H 1 ATOM 3321 H HA . MET A 1 222 ? 19.127 -0.083 28.923 1.00 17.75 ? 230 MET A HA 1 ATOM 3322 H HB2 A MET A 1 222 ? 18.120 -1.413 26.632 0.73 19.22 ? 230 MET A HB2 1 ATOM 3323 H HB2 B MET A 1 222 ? 18.225 -1.487 26.651 0.27 18.16 ? 230 MET A HB2 1 ATOM 3324 H HB3 A MET A 1 222 ? 18.686 0.070 26.602 0.73 19.22 ? 230 MET A HB3 1 ATOM 3325 H HB3 B MET A 1 222 ? 18.586 0.057 26.589 0.27 18.16 ? 230 MET A HB3 1 ATOM 3326 H HG2 A MET A 1 222 ? 20.267 -2.188 27.193 0.73 22.08 ? 230 MET A HG2 1 ATOM 3327 H HG2 B MET A 1 222 ? 20.446 -1.972 27.191 0.27 18.45 ? 230 MET A HG2 1 ATOM 3328 H HG3 A MET A 1 222 ? 20.249 -1.474 25.777 0.73 22.08 ? 230 MET A HG3 1 ATOM 3329 H HG3 B MET A 1 222 ? 20.344 -1.249 25.784 0.27 18.45 ? 230 MET A HG3 1 ATOM 3330 H HE1 A MET A 1 222 ? 21.896 1.865 26.421 0.73 19.32 ? 230 MET A HE1 1 ATOM 3331 H HE1 B MET A 1 222 ? 23.705 -0.209 27.105 0.27 13.65 ? 230 MET A HE1 1 ATOM 3332 H HE2 A MET A 1 222 ? 21.269 0.937 25.294 0.73 19.32 ? 230 MET A HE2 1 ATOM 3333 H HE2 B MET A 1 222 ? 22.981 -1.601 27.352 0.27 13.65 ? 230 MET A HE2 1 ATOM 3334 H HE3 A MET A 1 222 ? 20.338 1.551 26.426 0.73 19.32 ? 230 MET A HE3 1 ATOM 3335 H HE3 B MET A 1 222 ? 22.954 -0.936 25.909 0.27 13.65 ? 230 MET A HE3 1 ATOM 3336 N N . VAL A 1 223 ? 17.036 1.316 28.628 1.00 13.62 ? 231 VAL A N 1 ATOM 3337 C CA . VAL A 1 223 ? 15.863 2.079 29.041 1.00 12.96 ? 231 VAL A CA 1 ATOM 3338 C C . VAL A 1 223 ? 15.454 3.060 27.957 1.00 12.67 ? 231 VAL A C 1 ATOM 3339 O O . VAL A 1 223 ? 16.293 3.746 27.370 1.00 14.20 ? 231 VAL A O 1 ATOM 3340 C CB . VAL A 1 223 ? 16.183 2.857 30.345 1.00 15.04 ? 231 VAL A CB 1 ATOM 3341 C CG1 . VAL A 1 223 ? 15.024 3.696 30.805 1.00 17.53 ? 231 VAL A CG1 1 ATOM 3342 C CG2 . VAL A 1 223 ? 16.616 1.891 31.452 1.00 15.92 ? 231 VAL A CG2 1 ATOM 3343 H H . VAL A 1 223 ? 17.681 1.805 28.339 1.00 16.35 ? 231 VAL A H 1 ATOM 3344 H HA . VAL A 1 223 ? 15.123 1.475 29.211 1.00 15.55 ? 231 VAL A HA 1 ATOM 3345 H HB . VAL A 1 223 ? 16.927 3.456 30.172 1.00 18.04 ? 231 VAL A HB 1 ATOM 3346 H HG11 . VAL A 1 223 ? 15.274 4.160 31.619 1.00 21.04 ? 231 VAL A HG11 1 ATOM 3347 H HG12 . VAL A 1 223 ? 14.804 4.339 30.112 1.00 21.04 ? 231 VAL A HG12 1 ATOM 3348 H HG13 . VAL A 1 223 ? 14.263 3.118 30.974 1.00 21.04 ? 231 VAL A HG13 1 ATOM 3349 H HG21 . VAL A 1 223 ? 16.810 2.398 32.255 1.00 19.11 ? 231 VAL A HG21 1 ATOM 3350 H HG22 . VAL A 1 223 ? 15.895 1.264 31.622 1.00 19.11 ? 231 VAL A HG22 1 ATOM 3351 H HG23 . VAL A 1 223 ? 17.409 1.413 31.162 1.00 19.11 ? 231 VAL A HG23 1 ATOM 3352 N N . TYR A 1 224 ? 14.146 3.180 27.757 1.00 12.23 ? 232 TYR A N 1 ATOM 3353 C CA . TYR A 1 224 ? 13.552 4.295 27.026 1.00 12.07 ? 232 TYR A CA 1 ATOM 3354 C C . TYR A 1 224 ? 12.919 5.228 28.050 1.00 11.53 ? 232 TYR A C 1 ATOM 3355 O O . TYR A 1 224 ? 12.143 4.776 28.889 1.00 13.03 ? 232 TYR A O 1 ATOM 3356 C CB . TYR A 1 224 ? 12.470 3.788 26.058 1.00 12.21 ? 232 TYR A CB 1 ATOM 3357 C CG . TYR A 1 224 ? 12.961 2.989 24.851 1.00 12.28 ? 232 TYR A CG 1 ATOM 3358 C CD1 . TYR A 1 224 ? 14.173 3.266 24.234 1.00 13.11 ? 232 TYR A CD1 1 ATOM 3359 C CD2 . TYR A 1 224 ? 12.179 2.006 24.308 1.00 13.25 ? 232 TYR A CD2 1 ATOM 3360 C CE1 . TYR A 1 224 ? 14.590 2.564 23.107 1.00 12.35 ? 232 TYR A CE1 1 ATOM 3361 C CE2 . TYR A 1 224 ? 12.608 1.279 23.191 1.00 12.98 ? 232 TYR A CE2 1 ATOM 3362 C CZ . TYR A 1 224 ? 13.799 1.564 22.603 1.00 12.73 ? 232 TYR A CZ 1 ATOM 3363 O OH . TYR A 1 224 ? 14.198 0.850 21.490 1.00 13.76 ? 232 TYR A OH 1 ATOM 3364 H H . TYR A 1 224 ? 13.567 2.613 28.043 1.00 14.67 ? 232 TYR A H 1 ATOM 3365 H HA . TYR A 1 224 ? 14.232 4.775 26.529 1.00 14.49 ? 232 TYR A HA 1 ATOM 3366 H HB2 . TYR A 1 224 ? 11.862 3.218 26.553 1.00 14.65 ? 232 TYR A HB2 1 ATOM 3367 H HB3 . TYR A 1 224 ? 11.985 4.556 25.717 1.00 14.65 ? 232 TYR A HB3 1 ATOM 3368 H HD1 . TYR A 1 224 ? 14.711 3.944 24.573 1.00 15.73 ? 232 TYR A HD1 1 ATOM 3369 H HD2 . TYR A 1 224 ? 11.362 1.801 24.702 1.00 15.90 ? 232 TYR A HD2 1 ATOM 3370 H HE1 . TYR A 1 224 ? 15.410 2.755 22.714 1.00 14.82 ? 232 TYR A HE1 1 ATOM 3371 H HE2 . TYR A 1 224 ? 12.066 0.610 22.839 1.00 15.58 ? 232 TYR A HE2 1 ATOM 3372 H HH . TYR A 1 224 ? 14.943 1.130 21.221 1.00 16.52 ? 232 TYR A HH 1 ATOM 3373 N N . VAL A 1 225 ? 13.256 6.512 27.983 1.00 11.40 ? 233 VAL A N 1 ATOM 3374 C CA . VAL A 1 225 ? 12.700 7.528 28.866 1.00 11.27 ? 233 VAL A CA 1 ATOM 3375 C C . VAL A 1 225 ? 11.693 8.336 28.078 1.00 11.26 ? 233 VAL A C 1 ATOM 3376 O O . VAL A 1 225 ? 12.009 8.801 26.985 1.00 12.63 ? 233 VAL A O 1 ATOM 3377 C CB . VAL A 1 225 ? 13.823 8.448 29.390 1.00 12.52 ? 233 VAL A CB 1 ATOM 3378 C CG1 . VAL A 1 225 ? 13.271 9.575 30.239 1.00 13.56 ? 233 VAL A CG1 1 ATOM 3379 C CG2 . VAL A 1 225 ? 14.897 7.667 30.162 1.00 12.95 ? 233 VAL A CG2 1 ATOM 3380 H H . VAL A 1 225 ? 13.822 6.827 27.416 1.00 13.68 ? 233 VAL A H 1 ATOM 3381 H HA . VAL A 1 225 ? 12.254 7.110 29.619 1.00 13.53 ? 233 VAL A HA 1 ATOM 3382 H HB . VAL A 1 225 ? 14.260 8.855 28.625 1.00 15.03 ? 233 VAL A HB 1 ATOM 3383 H HG11 . VAL A 1 225 ? 14.007 10.127 30.547 1.00 16.27 ? 233 VAL A HG11 1 ATOM 3384 H HG12 . VAL A 1 225 ? 12.661 10.104 29.703 1.00 16.27 ? 233 VAL A HG12 1 ATOM 3385 H HG13 . VAL A 1 225 ? 12.801 9.196 30.999 1.00 16.27 ? 233 VAL A HG13 1 ATOM 3386 H HG21 . VAL A 1 225 ? 15.577 8.286 30.469 1.00 15.54 ? 233 VAL A HG21 1 ATOM 3387 H HG22 . VAL A 1 225 ? 14.482 7.227 30.921 1.00 15.54 ? 233 VAL A HG22 1 ATOM 3388 H HG23 . VAL A 1 225 ? 15.292 7.006 29.572 1.00 15.54 ? 233 VAL A HG23 1 ATOM 3389 N N . ILE A 1 226 ? 10.494 8.515 28.634 1.00 11.00 ? 234 ILE A N 1 ATOM 3390 C CA . ILE A 1 226 ? 9.429 9.272 27.986 1.00 10.70 ? 234 ILE A CA 1 ATOM 3391 C C . ILE A 1 226 ? 8.920 10.338 28.938 1.00 10.68 ? 234 ILE A C 1 ATOM 3392 O O . ILE A 1 226 ? 8.987 10.206 30.160 1.00 11.10 ? 234 ILE A O 1 ATOM 3393 C CB . ILE A 1 226 ? 8.279 8.406 27.405 1.00 12.04 ? 234 ILE A CB 1 ATOM 3394 C CG1 . ILE A 1 226 ? 7.241 8.060 28.471 1.00 12.00 ? 234 ILE A CG1 1 ATOM 3395 C CG2 . ILE A 1 226 ? 8.862 7.167 26.720 1.00 13.62 ? 234 ILE A CG2 1 ATOM 3396 C CD1 . ILE A 1 226 ? 6.014 7.260 27.920 1.00 12.96 ? 234 ILE A CD1 1 ATOM 3397 H H . ILE A 1 226 ? 10.271 8.199 29.403 1.00 13.20 ? 234 ILE A H 1 ATOM 3398 H HA . ILE A 1 226 ? 9.823 9.740 27.234 1.00 12.84 ? 234 ILE A HA 1 ATOM 3399 H HB . ILE A 1 226 ? 7.832 8.933 26.724 1.00 14.45 ? 234 ILE A HB 1 ATOM 3400 H HG12 . ILE A 1 226 ? 7.665 7.518 29.155 1.00 14.41 ? 234 ILE A HG12 1 ATOM 3401 H HG13 . ILE A 1 226 ? 6.908 8.882 28.862 1.00 14.41 ? 234 ILE A HG13 1 ATOM 3402 H HG21 . ILE A 1 226 ? 8.135 6.634 26.361 1.00 16.34 ? 234 ILE A HG21 1 ATOM 3403 H HG22 . ILE A 1 226 ? 9.450 7.451 26.003 1.00 16.34 ? 234 ILE A HG22 1 ATOM 3404 H HG23 . ILE A 1 226 ? 9.360 6.651 27.373 1.00 16.34 ? 234 ILE A HG23 1 ATOM 3405 H HD11 . ILE A 1 226 ? 5.402 7.078 28.650 1.00 15.55 ? 234 ILE A HD11 1 ATOM 3406 H HD12 . ILE A 1 226 ? 5.570 7.792 27.241 1.00 15.55 ? 234 ILE A HD12 1 ATOM 3407 H HD13 . ILE A 1 226 ? 6.327 6.427 27.535 1.00 15.55 ? 234 ILE A HD13 1 ATOM 3408 N N . GLY A 1 227 ? 8.391 11.396 28.360 1.00 10.55 ? 235 GLY A N 1 ATOM 3409 C CA . GLY A 1 227 ? 7.757 12.441 29.125 1.00 11.46 ? 235 GLY A CA 1 ATOM 3410 C C . GLY A 1 227 ? 7.077 13.403 28.184 1.00 10.66 ? 235 GLY A C 1 ATOM 3411 O O . GLY A 1 227 ? 7.155 13.261 26.964 1.00 10.89 ? 235 GLY A O 1 ATOM 3412 H H . GLY A 1 227 ? 8.386 11.532 27.511 1.00 12.65 ? 235 GLY A H 1 ATOM 3413 H HA2 . GLY A 1 227 ? 7.096 12.062 29.724 1.00 13.75 ? 235 GLY A HA2 1 ATOM 3414 H HA3 . GLY A 1 227 ? 8.420 12.922 29.645 1.00 13.75 ? 235 GLY A HA3 1 ATOM 3415 N N . HIS A 1 228 ? 6.444 14.409 28.767 1.00 10.61 ? 236 HIS A N 1 ATOM 3416 C CA . HIS A 1 228 ? 5.716 15.372 27.954 1.00 10.77 ? 236 HIS A CA 1 ATOM 3417 C C . HIS A 1 228 ? 6.575 16.586 27.626 1.00 10.60 ? 236 HIS A C 1 ATOM 3418 O O . HIS A 1 228 ? 6.929 16.787 26.465 1.00 10.71 ? 236 HIS A O 1 ATOM 3419 C CB . HIS A 1 228 ? 4.406 15.799 28.594 1.00 10.54 ? 236 HIS A CB 1 ATOM 3420 C CG . HIS A 1 228 ? 3.672 16.759 27.745 1.00 10.01 ? 236 HIS A CG 1 ATOM 3421 N ND1 . HIS A 1 228 ? 3.052 16.353 26.583 1.00 10.77 ? 236 HIS A ND1 1 ATOM 3422 C CD2 . HIS A 1 228 ? 3.564 18.105 27.789 1.00 10.69 ? 236 HIS A CD2 1 ATOM 3423 C CE1 . HIS A 1 228 ? 2.545 17.407 25.974 1.00 10.73 ? 236 HIS A CE1 1 ATOM 3424 N NE2 . HIS A 1 228 ? 2.817 18.482 26.686 1.00 10.81 ? 236 HIS A NE2 1 ATOM 3425 H H . HIS A 1 228 ? 6.419 14.556 29.614 1.00 12.73 ? 236 HIS A H 1 ATOM 3426 H HA . HIS A 1 228 ? 5.494 14.945 27.111 1.00 12.92 ? 236 HIS A HA 1 ATOM 3427 H HB2 . HIS A 1 228 ? 3.845 15.018 28.724 1.00 12.64 ? 236 HIS A HB2 1 ATOM 3428 H HB3 . HIS A 1 228 ? 4.590 16.225 29.446 1.00 12.64 ? 236 HIS A HB3 1 ATOM 3429 H HD1 . HIS A 1 228 ? 2.996 15.541 26.304 1.00 12.92 ? 236 HIS A HD1 1 ATOM 3430 H HD2 . HIS A 1 228 ? 3.889 18.665 28.457 1.00 12.82 ? 236 HIS A HD2 1 ATOM 3431 H HE1 . HIS A 1 228 ? 2.049 17.390 25.188 1.00 12.87 ? 236 HIS A HE1 1 ATOM 3432 N N . VAL A 1 229 ? 6.881 17.418 28.629 1.00 10.53 ? 237 VAL A N 1 ATOM 3433 C CA . VAL A 1 229 ? 7.643 18.657 28.443 1.00 10.52 ? 237 VAL A CA 1 ATOM 3434 C C . VAL A 1 229 ? 9.122 18.302 28.345 1.00 10.47 ? 237 VAL A C 1 ATOM 3435 O O . VAL A 1 229 ? 9.656 17.680 29.277 1.00 10.92 ? 237 VAL A O 1 ATOM 3436 C CB . VAL A 1 229 ? 7.412 19.634 29.609 1.00 10.95 ? 237 VAL A CB 1 ATOM 3437 C CG1 . VAL A 1 229 ? 8.183 20.926 29.358 1.00 11.98 ? 237 VAL A CG1 1 ATOM 3438 C CG2 . VAL A 1 229 ? 5.926 19.933 29.816 1.00 11.62 ? 237 VAL A CG2 1 ATOM 3439 H H . VAL A 1 229 ? 6.650 17.281 29.446 1.00 12.63 ? 237 VAL A H 1 ATOM 3440 H HA . VAL A 1 229 ? 7.372 19.088 27.617 1.00 12.62 ? 237 VAL A HA 1 ATOM 3441 H HB . VAL A 1 229 ? 7.753 19.236 30.425 1.00 13.14 ? 237 VAL A HB 1 ATOM 3442 H HG11 . VAL A 1 229 ? 8.030 21.534 30.098 1.00 14.38 ? 237 VAL A HG11 1 ATOM 3443 H HG12 . VAL A 1 229 ? 9.129 20.721 29.288 1.00 14.38 ? 237 VAL A HG12 1 ATOM 3444 H HG13 . VAL A 1 229 ? 7.869 21.325 28.531 1.00 14.38 ? 237 VAL A HG13 1 ATOM 3445 H HG21 . VAL A 1 229 ? 5.829 20.550 30.558 1.00 13.94 ? 237 VAL A HG21 1 ATOM 3446 H HG22 . VAL A 1 229 ? 5.568 20.329 29.007 1.00 13.94 ? 237 VAL A HG22 1 ATOM 3447 H HG23 . VAL A 1 229 ? 5.462 19.104 30.012 1.00 13.94 ? 237 VAL A HG23 1 ATOM 3448 N N . PRO A 1 230 ? 9.822 18.730 27.299 1.00 11.02 ? 238 PRO A N 1 ATOM 3449 C CA . PRO A 1 230 ? 11.255 18.425 27.189 1.00 10.79 ? 238 PRO A CA 1 ATOM 3450 C C . PRO A 1 230 ? 12.104 19.484 27.853 1.00 11.19 ? 238 PRO A C 1 ATOM 3451 O O . PRO A 1 230 ? 11.652 20.632 28.001 1.00 11.35 ? 238 PRO A O 1 ATOM 3452 C CB . PRO A 1 230 ? 11.492 18.446 25.675 1.00 11.33 ? 238 PRO A CB 1 ATOM 3453 C CG . PRO A 1 230 ? 10.544 19.490 25.210 1.00 11.97 ? 238 PRO A CG 1 ATOM 3454 C CD . PRO A 1 230 ? 9.304 19.348 26.056 1.00 11.14 ? 238 PRO A CD 1 ATOM 3455 H HA . PRO A 1 230 ? 11.460 17.548 27.551 1.00 12.94 ? 238 PRO A HA 1 ATOM 3456 H HB2 . PRO A 1 230 ? 12.410 18.696 25.484 1.00 13.59 ? 238 PRO A HB2 1 ATOM 3457 H HB3 . PRO A 1 230 ? 11.276 17.582 25.291 1.00 13.59 ? 238 PRO A HB3 1 ATOM 3458 H HG2 . PRO A 1 230 ? 10.942 20.366 25.335 1.00 14.37 ? 238 PRO A HG2 1 ATOM 3459 H HG3 . PRO A 1 230 ? 10.335 19.342 24.274 1.00 14.37 ? 238 PRO A HG3 1 ATOM 3460 H HD2 . PRO A 1 230 ? 8.920 20.219 26.244 1.00 13.36 ? 238 PRO A HD2 1 ATOM 3461 H HD3 . PRO A 1 230 ? 8.664 18.760 25.625 1.00 13.36 ? 238 PRO A HD3 1 ATOM 3462 N N . PRO A 1 231 ? 13.334 19.139 28.236 1.00 10.84 ? 239 PRO A N 1 ATOM 3463 C CA . PRO A 1 231 ? 14.332 20.151 28.597 1.00 11.58 ? 239 PRO A CA 1 ATOM 3464 C C . PRO A 1 231 ? 14.735 20.915 27.345 1.00 11.27 ? 239 PRO A C 1 ATOM 3465 O O . PRO A 1 231 ? 14.342 20.585 26.228 1.00 11.62 ? 239 PRO A O 1 ATOM 3466 C CB . PRO A 1 231 ? 15.479 19.292 29.134 1.00 12.16 ? 239 PRO A CB 1 ATOM 3467 C CG . PRO A 1 231 ? 15.415 18.064 28.253 1.00 12.00 ? 239 PRO A CG 1 ATOM 3468 C CD . PRO A 1 231 ? 13.938 17.814 28.064 1.00 11.18 ? 239 PRO A CD 1 ATOM 3469 H HA . PRO A 1 231 ? 14.002 20.754 29.281 1.00 13.90 ? 239 PRO A HA 1 ATOM 3470 H HB2 . PRO A 1 231 ? 16.323 19.757 29.025 1.00 14.60 ? 239 PRO A HB2 1 ATOM 3471 H HB3 . PRO A 1 231 ? 15.319 19.065 30.063 1.00 14.60 ? 239 PRO A HB3 1 ATOM 3472 H HG2 . PRO A 1 231 ? 15.845 18.246 27.403 1.00 14.40 ? 239 PRO A HG2 1 ATOM 3473 H HG3 . PRO A 1 231 ? 15.837 17.315 28.701 1.00 14.40 ? 239 PRO A HG3 1 ATOM 3474 H HD2 . PRO A 1 231 ? 13.764 17.477 27.171 1.00 13.42 ? 239 PRO A HD2 1 ATOM 3475 H HD3 . PRO A 1 231 ? 13.610 17.203 28.743 1.00 13.42 ? 239 PRO A HD3 1 ATOM 3476 N N . GLY A 1 232 ? 15.530 21.963 27.534 1.00 11.87 ? 240 GLY A N 1 ATOM 3477 C CA . GLY A 1 232 ? 15.985 22.732 26.396 1.00 12.69 ? 240 GLY A CA 1 ATOM 3478 C C . GLY A 1 232 ? 14.958 23.729 25.885 1.00 12.35 ? 240 GLY A C 1 ATOM 3479 O O . GLY A 1 232 ? 14.075 24.184 26.588 1.00 12.29 ? 240 GLY A O 1 ATOM 3480 H H . GLY A 1 232 ? 15.813 22.241 28.297 1.00 14.24 ? 240 GLY A H 1 ATOM 3481 H HA2 . GLY A 1 232 ? 16.786 23.221 26.641 1.00 15.22 ? 240 GLY A HA2 1 ATOM 3482 H HA3 . GLY A 1 232 ? 16.208 22.128 25.671 1.00 15.22 ? 240 GLY A HA3 1 ATOM 3483 N N . PHE A 1 233 ? 15.146 24.101 24.628 1.00 11.39 ? 241 PHE A N 1 ATOM 3484 C CA . PHE A 1 233 ? 14.492 25.257 24.037 1.00 12.30 ? 241 PHE A CA 1 ATOM 3485 C C . PHE A 1 233 ? 13.556 24.849 22.904 1.00 11.71 ? 241 PHE A C 1 ATOM 3486 O O . PHE A 1 233 ? 13.683 23.768 22.336 1.00 12.65 ? 241 PHE A O 1 ATOM 3487 C CB . PHE A 1 233 ? 15.522 26.265 23.530 1.00 13.04 ? 241 PHE A CB 1 ATOM 3488 C CG . PHE A 1 233 ? 16.293 26.892 24.651 1.00 13.33 ? 241 PHE A CG 1 ATOM 3489 C CD1 . PHE A 1 233 ? 17.352 26.230 25.249 1.00 13.81 ? 241 PHE A CD1 1 ATOM 3490 C CD2 . PHE A 1 233 ? 15.895 28.108 25.153 1.00 14.34 ? 241 PHE A CD2 1 ATOM 3491 C CE1 . PHE A 1 233 ? 18.004 26.789 26.332 1.00 15.02 ? 241 PHE A CE1 1 ATOM 3492 C CE2 . PHE A 1 233 ? 16.526 28.686 26.216 1.00 15.72 ? 241 PHE A CE2 1 ATOM 3493 C CZ . PHE A 1 233 ? 17.605 28.023 26.817 1.00 15.41 ? 241 PHE A CZ 1 ATOM 3494 H H . PHE A 1 233 ? 15.664 23.686 24.081 1.00 13.67 ? 241 PHE A H 1 ATOM 3495 H HA . PHE A 1 233 ? 13.959 25.695 24.718 1.00 14.76 ? 241 PHE A HA 1 ATOM 3496 H HB2 . PHE A 1 233 ? 16.151 25.812 22.947 1.00 15.64 ? 241 PHE A HB2 1 ATOM 3497 H HB3 . PHE A 1 233 ? 15.065 26.970 23.045 1.00 15.64 ? 241 PHE A HB3 1 ATOM 3498 H HD1 . PHE A 1 233 ? 17.615 25.396 24.931 1.00 16.58 ? 241 PHE A HD1 1 ATOM 3499 H HD2 . PHE A 1 233 ? 15.172 28.544 24.763 1.00 17.21 ? 241 PHE A HD2 1 ATOM 3500 H HE1 . PHE A 1 233 ? 18.726 26.348 26.719 1.00 18.02 ? 241 PHE A HE1 1 ATOM 3501 H HE2 . PHE A 1 233 ? 16.250 29.516 26.531 1.00 18.86 ? 241 PHE A HE2 1 ATOM 3502 H HZ . PHE A 1 233 ? 18.055 28.413 27.532 1.00 18.49 ? 241 PHE A HZ 1 ATOM 3503 N N . PHE A 1 234 ? 12.644 25.743 22.557 1.00 12.21 ? 242 PHE A N 1 ATOM 3504 C CA . PHE A 1 234 ? 11.656 25.511 21.515 1.00 12.39 ? 242 PHE A CA 1 ATOM 3505 C C . PHE A 1 234 ? 12.195 26.088 20.200 1.00 11.52 ? 242 PHE A C 1 ATOM 3506 O O . PHE A 1 234 ? 12.460 27.289 20.099 1.00 13.58 ? 242 PHE A O 1 ATOM 3507 C CB . PHE A 1 234 ? 10.347 26.172 21.922 1.00 11.62 ? 242 PHE A CB 1 ATOM 3508 C CG . PHE A 1 234 ? 9.186 25.954 20.962 1.00 12.41 ? 242 PHE A CG 1 ATOM 3509 C CD1 . PHE A 1 234 ? 9.069 24.820 20.180 1.00 12.70 ? 242 PHE A CD1 1 ATOM 3510 C CD2 . PHE A 1 234 ? 8.174 26.883 20.900 1.00 13.92 ? 242 PHE A CD2 1 ATOM 3511 C CE1 . PHE A 1 234 ? 7.980 24.647 19.342 1.00 14.17 ? 242 PHE A CE1 1 ATOM 3512 C CE2 . PHE A 1 234 ? 7.077 26.704 20.077 1.00 15.75 ? 242 PHE A CE2 1 ATOM 3513 C CZ . PHE A 1 234 ? 6.989 25.582 19.303 1.00 15.48 ? 242 PHE A CZ 1 ATOM 3514 H H . PHE A 1 234 ? 12.575 26.518 22.923 1.00 14.65 ? 242 PHE A H 1 ATOM 3515 H HA . PHE A 1 234 ? 11.507 24.559 21.404 1.00 14.86 ? 242 PHE A HA 1 ATOM 3516 H HB2 . PHE A 1 234 ? 10.082 25.823 22.786 1.00 13.94 ? 242 PHE A HB2 1 ATOM 3517 H HB3 . PHE A 1 234 ? 10.494 27.129 21.990 1.00 13.94 ? 242 PHE A HB3 1 ATOM 3518 H HD1 . PHE A 1 234 ? 9.736 24.172 20.206 1.00 15.24 ? 242 PHE A HD1 1 ATOM 3519 H HD2 . PHE A 1 234 ? 8.223 27.645 21.432 1.00 16.70 ? 242 PHE A HD2 1 ATOM 3520 H HE1 . PHE A 1 234 ? 7.918 23.883 18.816 1.00 17.01 ? 242 PHE A HE1 1 ATOM 3521 H HE2 . PHE A 1 234 ? 6.409 27.349 20.042 1.00 18.91 ? 242 PHE A HE2 1 ATOM 3522 H HZ . PHE A 1 234 ? 6.262 25.466 18.735 1.00 18.58 ? 242 PHE A HZ 1 ATOM 3523 N N . GLU A 1 235 ? 12.348 25.221 19.189 1.00 11.92 ? 243 GLU A N 1 ATOM 3524 C CA . GLU A 1 235 ? 13.019 25.591 17.962 1.00 12.69 ? 243 GLU A CA 1 ATOM 3525 C C . GLU A 1 235 ? 12.246 26.580 17.105 1.00 13.74 ? 243 GLU A C 1 ATOM 3526 O O . GLU A 1 235 ? 12.847 27.132 16.188 1.00 14.88 ? 243 GLU A O 1 ATOM 3527 C CB . GLU A 1 235 ? 13.353 24.328 17.180 1.00 12.35 ? 243 GLU A CB 1 ATOM 3528 C CG . GLU A 1 235 ? 12.180 23.619 16.488 1.00 12.80 ? 243 GLU A CG 1 ATOM 3529 C CD . GLU A 1 235 ? 11.347 22.703 17.362 1.00 11.83 ? 243 GLU A CD 1 ATOM 3530 O OE1 . GLU A 1 235 ? 11.565 22.608 18.596 1.00 11.65 ? 243 GLU A OE1 1 ATOM 3531 O OE2 . GLU A 1 235 ? 10.441 22.048 16.778 1.00 12.68 ? 243 GLU A OE2 1 ATOM 3532 H H . GLU A 1 235 ? 12.065 24.409 19.201 1.00 14.30 ? 243 GLU A H 1 ATOM 3533 H HA . GLU A 1 235 ? 13.860 26.014 18.195 1.00 15.23 ? 243 GLU A HA 1 ATOM 3534 H HB2 . GLU A 1 235 ? 13.996 24.559 16.491 1.00 14.82 ? 243 GLU A HB2 1 ATOM 3535 H HB3 . GLU A 1 235 ? 13.754 23.690 17.792 1.00 14.82 ? 243 GLU A HB3 1 ATOM 3536 H HG2 . GLU A 1 235 ? 11.585 24.295 16.128 1.00 15.37 ? 243 GLU A HG2 1 ATOM 3537 H HG3 . GLU A 1 235 ? 12.534 23.082 15.762 1.00 15.37 ? 243 GLU A HG3 1 ATOM 3538 N N . LYS A 1 236 ? 10.966 26.803 17.370 1.00 14.22 ? 244 LYS A N 1 ATOM 3539 C CA . LYS A 1 236 ? 10.157 27.722 16.576 1.00 15.46 ? 244 LYS A CA 1 ATOM 3540 C C . LYS A 1 236 ? 10.295 29.162 17.009 1.00 14.94 ? 244 LYS A C 1 ATOM 3541 O O . LYS A 1 236 ? 9.636 30.035 16.428 1.00 16.36 ? 244 LYS A O 1 ATOM 3542 C CB . LYS A 1 236 ? 8.688 27.321 16.660 1.00 17.80 ? 244 LYS A CB 1 ATOM 3543 C CG . LYS A 1 236 ? 8.382 25.990 16.024 1.00 20.76 ? 244 LYS A CG 1 ATOM 3544 C CD . LYS A 1 236 ? 8.466 26.048 14.520 1.00 24.53 ? 244 LYS A CD 1 ATOM 3545 C CE . LYS A 1 236 ? 7.396 26.958 13.941 1.00 28.02 ? 244 LYS A CE 1 ATOM 3546 N NZ . LYS A 1 236 ? 6.499 26.291 12.945 1.00 28.99 ? 244 LYS A NZ 1 ATOM 3547 H H . LYS A 1 236 ? 10.534 26.429 18.013 1.00 17.07 ? 244 LYS A H 1 ATOM 3548 H HA . LYS A 1 236 ? 10.432 27.661 15.648 1.00 18.56 ? 244 LYS A HA 1 ATOM 3549 H HB2 . LYS A 1 236 ? 8.431 27.270 17.594 1.00 21.36 ? 244 LYS A HB2 1 ATOM 3550 H HB3 . LYS A 1 236 ? 8.154 27.995 16.210 1.00 21.36 ? 244 LYS A HB3 1 ATOM 3551 H HG2 . LYS A 1 236 ? 9.023 25.333 16.338 1.00 24.91 ? 244 LYS A HG2 1 ATOM 3552 H HG3 . LYS A 1 236 ? 7.482 25.721 16.266 1.00 24.91 ? 244 LYS A HG3 1 ATOM 3553 H HD2 . LYS A 1 236 ? 9.334 26.395 14.260 1.00 29.44 ? 244 LYS A HD2 1 ATOM 3554 H HD3 . LYS A 1 236 ? 8.338 25.157 14.157 1.00 29.44 ? 244 LYS A HD3 1 ATOM 3555 H HE2 . LYS A 1 236 ? 6.840 27.286 14.666 1.00 33.62 ? 244 LYS A HE2 1 ATOM 3556 H HE3 . LYS A 1 236 ? 7.828 27.704 13.496 1.00 33.62 ? 244 LYS A HE3 1 ATOM 3557 H HZ1 . LYS A 1 236 ? 5.895 26.871 12.642 1.00 34.78 ? 244 LYS A HZ1 1 ATOM 3558 H HZ2 . LYS A 1 236 ? 6.978 25.988 12.259 1.00 34.78 ? 244 LYS A HZ2 1 ATOM 3559 H HZ3 . LYS A 1 236 ? 6.076 25.606 13.326 1.00 34.78 ? 244 LYS A HZ3 1 ATOM 3560 N N . THR A 1 237 ? 11.124 29.438 18.005 1.00 14.65 ? 245 THR A N 1 ATOM 3561 C CA . THR A 1 237 ? 11.312 30.798 18.493 1.00 15.35 ? 245 THR A CA 1 ATOM 3562 C C . THR A 1 237 ? 12.738 30.904 19.019 1.00 14.47 ? 245 THR A C 1 ATOM 3563 O O . THR A 1 237 ? 13.583 30.055 18.721 1.00 15.40 ? 245 THR A O 1 ATOM 3564 C CB . THR A 1 237 ? 10.223 31.145 19.526 1.00 16.56 ? 245 THR A CB 1 ATOM 3565 O OG1 . THR A 1 237 ? 10.301 32.519 19.910 1.00 18.28 ? 245 THR A OG1 1 ATOM 3566 C CG2 . THR A 1 237 ? 10.315 30.265 20.763 1.00 16.66 ? 245 THR A CG2 1 ATOM 3567 H H . THR A 1 237 ? 11.594 28.850 18.420 1.00 17.59 ? 245 THR A H 1 ATOM 3568 H HA . THR A 1 237 ? 11.223 31.414 17.749 1.00 18.42 ? 245 THR A HA 1 ATOM 3569 H HB . THR A 1 237 ? 9.355 30.988 19.121 1.00 19.87 ? 245 THR A HB 1 ATOM 3570 H HG1 . THR A 1 237 ? 10.196 33.012 19.238 1.00 21.94 ? 245 THR A HG1 1 ATOM 3571 H HG21 . THR A 1 237 ? 9.618 30.506 21.393 1.00 19.99 ? 245 THR A HG21 1 ATOM 3572 H HG22 . THR A 1 237 ? 10.208 29.333 20.516 1.00 19.99 ? 245 THR A HG22 1 ATOM 3573 H HG23 . THR A 1 237 ? 11.179 30.380 21.188 1.00 19.99 ? 245 THR A HG23 1 ATOM 3574 N N . GLN A 1 238 ? 13.016 31.990 19.730 1.00 14.97 ? 246 GLN A N 1 ATOM 3575 C CA . GLN A 1 238 ? 14.301 32.204 20.372 1.00 15.98 ? 246 GLN A CA 1 ATOM 3576 C C . GLN A 1 238 ? 14.078 32.347 21.867 1.00 16.27 ? 246 GLN A C 1 ATOM 3577 O O . GLN A 1 238 ? 13.102 32.965 22.299 1.00 17.41 ? 246 GLN A O 1 ATOM 3578 C CB . GLN A 1 238 ? 15.018 33.438 19.806 1.00 17.82 ? 246 GLN A CB 1 ATOM 3579 C CG . GLN A 1 238 ? 14.207 34.726 19.866 1.00 22.58 ? 246 GLN A CG 1 ATOM 3580 C CD . GLN A 1 238 ? 15.003 35.948 19.454 1.00 28.28 ? 246 GLN A CD 1 ATOM 3581 O OE1 . GLN A 1 238 ? 14.652 36.633 18.503 1.00 31.17 ? 246 GLN A OE1 1 ATOM 3582 N NE2 . GLN A 1 238 ? 16.070 36.226 20.171 1.00 30.04 ? 246 GLN A NE2 1 ATOM 3583 H H . GLN A 1 238 ? 12.459 32.633 19.857 1.00 17.96 ? 246 GLN A H 1 ATOM 3584 H HA . GLN A 1 238 ? 14.866 31.430 20.222 1.00 19.18 ? 246 GLN A HA 1 ATOM 3585 H HB2 . GLN A 1 238 ? 15.834 33.581 20.311 1.00 21.38 ? 246 GLN A HB2 1 ATOM 3586 H HB3 . GLN A 1 238 ? 15.235 33.271 18.876 1.00 21.38 ? 246 GLN A HB3 1 ATOM 3587 H HG2 . GLN A 1 238 ? 13.448 34.648 19.268 1.00 27.10 ? 246 GLN A HG2 1 ATOM 3588 H HG3 . GLN A 1 238 ? 13.899 34.863 20.776 1.00 27.10 ? 246 GLN A HG3 1 ATOM 3589 H HE21 . GLN A 1 238 ? 16.284 35.724 20.836 1.00 36.05 ? 246 GLN A HE21 1 ATOM 3590 H HE22 . GLN A 1 238 ? 16.554 36.909 19.975 1.00 36.05 ? 246 GLN A HE22 1 ATOM 3591 N N . ASN A 1 239 ? 14.993 31.767 22.651 1.00 17.11 ? 247 ASN A N 1 ATOM 3592 C CA . ASN A 1 239 ? 15.085 31.973 24.093 1.00 17.28 ? 247 ASN A CA 1 ATOM 3593 C C . ASN A 1 239 ? 13.900 31.446 24.889 1.00 16.97 ? 247 ASN A C 1 ATOM 3594 O O . ASN A 1 239 ? 13.700 31.877 26.020 1.00 19.20 ? 247 ASN A O 1 ATOM 3595 C CB . ASN A 1 239 ? 15.410 33.432 24.406 1.00 23.01 ? 247 ASN A CB 1 ATOM 3596 C CG . ASN A 1 239 ? 16.736 33.830 23.802 1.00 29.21 ? 247 ASN A CG 1 ATOM 3597 O OD1 . ASN A 1 239 ? 17.763 33.205 24.087 1.00 32.91 ? 247 ASN A OD1 1 ATOM 3598 N ND2 . ASN A 1 239 ? 16.720 34.812 22.927 1.00 32.76 ? 247 ASN A ND2 1 ATOM 3599 H H . ASN A 1 239 ? 15.594 31.229 22.353 1.00 20.53 ? 247 ASN A H 1 ATOM 3600 H HA . ASN A 1 239 ? 15.851 31.462 24.398 1.00 20.74 ? 247 ASN A HA 1 ATOM 3601 H HB2 . ASN A 1 239 ? 14.720 34.003 24.033 1.00 27.61 ? 247 ASN A HB2 1 ATOM 3602 H HB3 . ASN A 1 239 ? 15.463 33.551 25.367 1.00 27.61 ? 247 ASN A HB3 1 ATOM 3603 H HD21 . ASN A 1 239 ? 17.453 35.071 22.558 1.00 39.31 ? 247 ASN A HD21 1 ATOM 3604 H HD22 . ASN A 1 239 ? 15.978 35.195 22.723 1.00 39.31 ? 247 ASN A HD22 1 ATOM 3605 N N . LYS A 1 240 ? 13.150 30.454 24.373 1.00 14.76 ? 248 LYS A N 1 ATOM 3606 C CA . LYS A 1 240 ? 11.996 29.897 25.085 1.00 14.84 ? 248 LYS A CA 1 ATOM 3607 C C . LYS A 1 240 ? 12.355 28.504 25.572 1.00 13.78 ? 248 LYS A C 1 ATOM 3608 O O . LYS A 1 240 ? 12.441 27.562 24.771 1.00 13.67 ? 248 LYS A O 1 ATOM 3609 C CB . LYS A 1 240 ? 10.746 29.834 24.213 1.00 15.75 ? 248 LYS A CB 1 ATOM 3610 C CG . LYS A 1 240 ? 9.544 29.263 24.955 1.00 15.94 ? 248 LYS A CG 1 ATOM 3611 C CD . LYS A 1 240 ? 9.135 30.134 26.136 1.00 20.43 ? 248 LYS A CD 1 ATOM 3612 C CE . LYS A 1 240 ? 7.846 29.698 26.766 1.00 24.35 ? 248 LYS A CE 1 ATOM 3613 N NZ . LYS A 1 240 ? 7.527 30.495 27.977 1.00 28.39 ? 248 LYS A NZ 1 ATOM 3614 H H . LYS A 1 240 ? 13.294 30.089 23.607 1.00 17.71 ? 248 LYS A H 1 ATOM 3615 H HA . LYS A 1 240 ? 11.801 30.449 25.858 1.00 17.81 ? 248 LYS A HA 1 ATOM 3616 H HB2 . LYS A 1 240 ? 10.519 30.731 23.919 1.00 18.91 ? 248 LYS A HB2 1 ATOM 3617 H HB3 . LYS A 1 240 ? 10.922 29.268 23.446 1.00 18.91 ? 248 LYS A HB3 1 ATOM 3618 H HG2 . LYS A 1 240 ? 8.791 29.207 24.346 1.00 19.12 ? 248 LYS A HG2 1 ATOM 3619 H HG3 . LYS A 1 240 ? 9.767 28.382 25.293 1.00 19.12 ? 248 LYS A HG3 1 ATOM 3620 H HD2 . LYS A 1 240 ? 9.828 30.092 26.813 1.00 24.52 ? 248 LYS A HD2 1 ATOM 3621 H HD3 . LYS A 1 240 ? 9.025 31.047 25.830 1.00 24.52 ? 248 LYS A HD3 1 ATOM 3622 H HE2 . LYS A 1 240 ? 7.124 29.813 26.129 1.00 29.23 ? 248 LYS A HE2 1 ATOM 3623 H HE3 . LYS A 1 240 ? 7.917 28.766 27.027 1.00 29.23 ? 248 LYS A HE3 1 ATOM 3624 H HZ1 . LYS A 1 240 ? 6.759 30.216 28.330 1.00 34.07 ? 248 LYS A HZ1 1 ATOM 3625 H HZ2 . LYS A 1 240 ? 8.174 30.402 28.580 1.00 34.07 ? 248 LYS A HZ2 1 ATOM 3626 H HZ3 . LYS A 1 240 ? 7.452 31.355 27.763 1.00 34.07 ? 248 LYS A HZ3 1 ATOM 3627 N N . ALA A 1 241 ? 12.561 28.383 26.879 1.00 13.92 ? 249 ALA A N 1 ATOM 3628 C CA . ALA A 1 241 ? 12.712 27.104 27.546 1.00 13.50 ? 249 ALA A CA 1 ATOM 3629 C C . ALA A 1 241 ? 11.535 26.898 28.483 1.00 14.25 ? 249 ALA A C 1 ATOM 3630 O O . ALA A 1 241 ? 11.036 27.845 29.093 1.00 18.66 ? 249 ALA A O 1 ATOM 3631 C CB . ALA A 1 241 ? 14.013 27.050 28.336 1.00 14.36 ? 249 ALA A CB 1 ATOM 3632 H H . ALA A 1 241 ? 12.620 29.053 27.415 1.00 16.70 ? 249 ALA A H 1 ATOM 3633 H HA . ALA A 1 241 ? 12.716 26.391 26.889 1.00 16.20 ? 249 ALA A HA 1 ATOM 3634 H HB1 . ALA A 1 241 ? 14.083 26.185 28.769 1.00 17.24 ? 249 ALA A HB1 1 ATOM 3635 H HB2 . ALA A 1 241 ? 14.757 27.178 27.727 1.00 17.24 ? 249 ALA A HB2 1 ATOM 3636 H HB3 . ALA A 1 241 ? 14.006 27.755 29.003 1.00 17.24 ? 249 ALA A HB3 1 ATOM 3637 N N . TRP A 1 242 ? 11.104 25.652 28.607 1.00 12.72 ? 250 TRP A N 1 ATOM 3638 C CA . TRP A 1 242 ? 9.975 25.318 29.470 1.00 12.87 ? 250 TRP A CA 1 ATOM 3639 C C . TRP A 1 242 ? 10.421 25.082 30.900 1.00 12.51 ? 250 TRP A C 1 ATOM 3640 O O . TRP A 1 242 ? 9.771 25.561 31.842 1.00 13.68 ? 250 TRP A O 1 ATOM 3641 C CB . TRP A 1 242 ? 9.235 24.074 28.963 1.00 12.50 ? 250 TRP A CB 1 ATOM 3642 C CG . TRP A 1 242 ? 9.068 24.102 27.477 1.00 12.62 ? 250 TRP A CG 1 ATOM 3643 C CD1 . TRP A 1 242 ? 9.732 23.335 26.578 1.00 12.46 ? 250 TRP A CD1 1 ATOM 3644 C CD2 . TRP A 1 242 ? 8.181 24.939 26.720 1.00 12.72 ? 250 TRP A CD2 1 ATOM 3645 N NE1 . TRP A 1 242 ? 9.338 23.647 25.320 1.00 12.95 ? 250 TRP A NE1 1 ATOM 3646 C CE2 . TRP A 1 242 ? 8.385 24.628 25.372 1.00 12.55 ? 250 TRP A CE2 1 ATOM 3647 C CE3 . TRP A 1 242 ? 7.251 25.927 27.054 1.00 13.67 ? 250 TRP A CE3 1 ATOM 3648 C CZ2 . TRP A 1 242 ? 7.685 25.260 24.341 1.00 13.87 ? 250 TRP A CZ2 1 ATOM 3649 C CZ3 . TRP A 1 242 ? 6.540 26.545 26.034 1.00 14.61 ? 250 TRP A CZ3 1 ATOM 3650 C CH2 . TRP A 1 242 ? 6.763 26.205 24.692 1.00 15.39 ? 250 TRP A CH2 1 ATOM 3651 H H . TRP A 1 242 ? 11.448 24.976 28.202 1.00 15.27 ? 250 TRP A H 1 ATOM 3652 H HA . TRP A 1 242 ? 9.349 26.059 29.470 1.00 15.44 ? 250 TRP A HA 1 ATOM 3653 H HB2 . TRP A 1 242 ? 9.744 23.282 29.196 1.00 15.00 ? 250 TRP A HB2 1 ATOM 3654 H HB3 . TRP A 1 242 ? 8.354 24.039 29.367 1.00 15.00 ? 250 TRP A HB3 1 ATOM 3655 H HD1 . TRP A 1 242 ? 10.383 22.706 26.792 1.00 14.95 ? 250 TRP A HD1 1 ATOM 3656 H HE1 . TRP A 1 242 ? 9.634 23.280 24.601 1.00 15.54 ? 250 TRP A HE1 1 ATOM 3657 H HE3 . TRP A 1 242 ? 7.098 26.154 27.943 1.00 16.40 ? 250 TRP A HE3 1 ATOM 3658 H HZ2 . TRP A 1 242 ? 7.823 25.028 23.451 1.00 16.64 ? 250 TRP A HZ2 1 ATOM 3659 H HZ3 . TRP A 1 242 ? 5.920 27.205 26.242 1.00 17.53 ? 250 TRP A HZ3 1 ATOM 3660 H HH2 . TRP A 1 242 ? 6.283 26.643 24.026 1.00 18.47 ? 250 TRP A HH2 1 ATOM 3661 N N . PHE A 1 243 ? 11.517 24.345 31.075 1.00 12.57 ? 251 PHE A N 1 ATOM 3662 C CA . PHE A 1 243 ? 11.994 24.018 32.411 1.00 13.04 ? 251 PHE A CA 1 ATOM 3663 C C . PHE A 1 243 ? 12.576 25.263 33.085 1.00 13.05 ? 251 PHE A C 1 ATOM 3664 O O . PHE A 1 243 ? 13.278 26.067 32.461 1.00 14.32 ? 251 PHE A O 1 ATOM 3665 C CB . PHE A 1 243 ? 13.127 22.993 32.325 1.00 12.67 ? 251 PHE A CB 1 ATOM 3666 C CG . PHE A 1 243 ? 12.724 21.543 32.122 1.00 12.18 ? 251 PHE A CG 1 ATOM 3667 C CD1 . PHE A 1 243 ? 11.569 21.148 31.481 1.00 12.25 ? 251 PHE A CD1 1 ATOM 3668 C CD2 . PHE A 1 243 ? 13.591 20.557 32.548 1.00 13.33 ? 251 PHE A CD2 1 ATOM 3669 C CE1 . PHE A 1 243 ? 11.311 19.797 31.289 1.00 12.69 ? 251 PHE A CE1 1 ATOM 3670 C CE2 . PHE A 1 243 ? 13.329 19.230 32.359 1.00 12.83 ? 251 PHE A CE2 1 ATOM 3671 C CZ . PHE A 1 243 ? 12.166 18.846 31.704 1.00 12.70 ? 251 PHE A CZ 1 ATOM 3672 H H . PHE A 1 243 ? 11.999 24.026 30.438 1.00 15.09 ? 251 PHE A H 1 ATOM 3673 H HA . PHE A 1 243 ? 11.273 23.662 32.953 1.00 15.65 ? 251 PHE A HA 1 ATOM 3674 H HB2 . PHE A 1 243 ? 13.700 23.238 31.582 1.00 15.21 ? 251 PHE A HB2 1 ATOM 3675 H HB3 . PHE A 1 243 ? 13.636 23.036 33.150 1.00 15.21 ? 251 PHE A HB3 1 ATOM 3676 H HD1 . PHE A 1 243 ? 10.970 21.785 31.166 1.00 14.70 ? 251 PHE A HD1 1 ATOM 3677 H HD2 . PHE A 1 243 ? 14.382 20.804 32.969 1.00 16.00 ? 251 PHE A HD2 1 ATOM 3678 H HE1 . PHE A 1 243 ? 10.525 19.543 30.862 1.00 15.23 ? 251 PHE A HE1 1 ATOM 3679 H HE2 . PHE A 1 243 ? 13.929 18.587 32.661 1.00 15.39 ? 251 PHE A HE2 1 ATOM 3680 H HZ . PHE A 1 243 ? 11.965 17.945 31.587 1.00 15.24 ? 251 PHE A HZ 1 ATOM 3681 N N . ARG A 1 244 ? 12.352 25.379 34.391 1.00 14.03 ? 252 ARG A N 1 ATOM 3682 C CA . ARG A 1 244 ? 13.194 26.263 35.197 1.00 13.33 ? 252 ARG A CA 1 ATOM 3683 C C . ARG A 1 244 ? 14.649 25.827 35.066 1.00 13.82 ? 252 ARG A C 1 ATOM 3684 O O . ARG A 1 244 ? 14.950 24.636 34.936 1.00 13.96 ? 252 ARG A O 1 ATOM 3685 C CB . ARG A 1 244 ? 12.765 26.225 36.658 1.00 14.98 ? 252 ARG A CB 1 ATOM 3686 C CG . ARG A 1 244 ? 11.341 26.657 36.889 1.00 17.39 ? 252 ARG A CG 1 ATOM 3687 C CD . ARG A 1 244 ? 11.078 26.869 38.405 1.00 20.13 ? 252 ARG A CD 1 ATOM 3688 N NE . ARG A 1 244 ? 9.650 26.865 38.702 1.00 23.94 ? 252 ARG A NE 1 ATOM 3689 C CZ . ARG A 1 244 ? 8.877 27.936 38.779 1.00 29.45 ? 252 ARG A CZ 1 ATOM 3690 N NH1 . ARG A 1 244 ? 9.389 29.158 38.646 1.00 32.40 ? 252 ARG A NH1 1 ATOM 3691 N NH2 . ARG A 1 244 ? 7.577 27.763 39.005 1.00 29.34 ? 252 ARG A NH2 1 ATOM 3692 H H . ARG A 1 244 ? 11.735 24.968 34.827 1.00 16.83 ? 252 ARG A H 1 ATOM 3693 H HA . ARG A 1 244 ? 13.113 27.174 34.873 1.00 16.00 ? 252 ARG A HA 1 ATOM 3694 H HB2 . ARG A 1 244 ? 12.855 25.317 36.987 1.00 17.97 ? 252 ARG A HB2 1 ATOM 3695 H HB3 . ARG A 1 244 ? 13.340 26.817 37.168 1.00 17.97 ? 252 ARG A HB3 1 ATOM 3696 H HG2 . ARG A 1 244 ? 11.179 27.495 36.428 1.00 20.87 ? 252 ARG A HG2 1 ATOM 3697 H HG3 . ARG A 1 244 ? 10.738 25.969 36.565 1.00 20.87 ? 252 ARG A HG3 1 ATOM 3698 H HD2 . ARG A 1 244 ? 11.496 26.151 38.906 1.00 24.16 ? 252 ARG A HD2 1 ATOM 3699 H HD3 . ARG A 1 244 ? 11.443 27.726 38.677 1.00 24.16 ? 252 ARG A HD3 1 ATOM 3700 H HE . ARG A 1 244 ? 9.279 26.101 38.838 1.00 28.73 ? 252 ARG A HE 1 ATOM 3701 H HH11 . ARG A 1 244 ? 10.229 29.257 38.487 1.00 38.88 ? 252 ARG A HH11 1 ATOM 3702 H HH12 . ARG A 1 244 ? 8.879 29.847 38.707 1.00 38.88 ? 252 ARG A HH12 1 ATOM 3703 H HH21 . ARG A 1 244 ? 7.259 26.970 39.103 1.00 35.21 ? 252 ARG A HH21 1 ATOM 3704 H HH22 . ARG A 1 244 ? 7.060 28.446 39.085 1.00 35.21 ? 252 ARG A HH22 1 ATOM 3705 N N . GLU A 1 245 ? 15.543 26.812 35.115 1.00 15.30 ? 253 GLU A N 1 ATOM 3706 C CA . GLU A 1 245 ? 16.959 26.565 34.860 1.00 15.66 ? 253 GLU A CA 1 ATOM 3707 C C . GLU A 1 245 ? 17.528 25.450 35.736 1.00 15.22 ? 253 GLU A C 1 ATOM 3708 O O . GLU A 1 245 ? 18.253 24.583 35.242 1.00 15.11 ? 253 GLU A O 1 ATOM 3709 C CB . GLU A 1 245 ? 17.762 27.851 35.009 1.00 17.82 ? 253 GLU A CB 1 ATOM 3710 C CG . GLU A 1 245 ? 19.194 27.664 34.587 1.00 20.10 ? 253 GLU A CG 1 ATOM 3711 C CD . GLU A 1 245 ? 19.901 28.975 34.336 1.00 23.54 ? 253 GLU A CD 1 ATOM 3712 O OE1 . GLU A 1 245 ? 19.354 30.024 34.748 1.00 27.25 ? 253 GLU A OE1 1 ATOM 3713 O OE2 . GLU A 1 245 ? 20.987 28.958 33.713 1.00 25.30 ? 253 GLU A OE2 1 ATOM 3714 H H . GLU A 1 245 ? 15.355 27.632 35.293 1.00 18.36 ? 253 GLU A H 1 ATOM 3715 H HA . GLU A 1 245 ? 17.052 26.277 33.939 1.00 18.79 ? 253 GLU A HA 1 ATOM 3716 H HB2 . GLU A 1 245 ? 17.369 28.540 34.450 1.00 21.39 ? 253 GLU A HB2 1 ATOM 3717 H HB3 . GLU A 1 245 ? 17.754 28.128 35.939 1.00 21.39 ? 253 GLU A HB3 1 ATOM 3718 H HG2 . GLU A 1 245 ? 19.672 27.195 35.289 1.00 24.12 ? 253 GLU A HG2 1 ATOM 3719 H HG3 . GLU A 1 245 ? 19.217 27.148 33.766 1.00 24.12 ? 253 GLU A HG3 1 ATOM 3720 N N . SER A 1 246 ? 17.227 25.446 37.037 1.00 15.03 ? 254 SER A N 1 ATOM 3721 C CA . SER A 1 246 ? 17.827 24.422 37.892 1.00 15.83 ? 254 SER A CA 1 ATOM 3722 C C . SER A 1 246 ? 17.377 23.025 37.484 1.00 14.57 ? 254 SER A C 1 ATOM 3723 O O . SER A 1 246 ? 18.162 22.071 37.543 1.00 15.27 ? 254 SER A O 1 ATOM 3724 C CB . SER A 1 246 ? 17.530 24.668 39.371 1.00 19.60 ? 254 SER A CB 1 ATOM 3725 O OG . SER A 1 246 ? 16.173 24.402 39.672 1.00 22.43 ? 254 SER A OG 1 ATOM 3726 H H . SER A 1 246 ? 16.701 25.999 37.434 1.00 18.04 ? 254 SER A H 1 ATOM 3727 H HA . SER A 1 246 ? 18.790 24.460 37.780 1.00 18.99 ? 254 SER A HA 1 ATOM 3728 H HB2 . SER A 1 246 ? 18.091 24.085 39.905 1.00 23.52 ? 254 SER A HB2 1 ATOM 3729 H HB3 . SER A 1 246 ? 17.723 25.595 39.580 1.00 23.52 ? 254 SER A HB3 1 ATOM 3730 H HG . SER A 1 246 ? 15.991 23.601 39.496 1.00 26.91 ? 254 SER A HG 1 ATOM 3731 N N . PHE A 1 247 ? 16.111 22.877 37.068 1.00 13.49 ? 255 PHE A N 1 ATOM 3732 C CA . PHE A 1 247 ? 15.630 21.576 36.611 1.00 13.27 ? 255 PHE A CA 1 ATOM 3733 C C . PHE A 1 247 ? 16.281 21.175 35.297 1.00 12.66 ? 255 PHE A C 1 ATOM 3734 O O . PHE A 1 247 ? 16.554 19.994 35.070 1.00 13.52 ? 255 PHE A O 1 ATOM 3735 C CB . PHE A 1 247 ? 14.120 21.632 36.449 1.00 13.55 ? 255 PHE A CB 1 ATOM 3736 C CG . PHE A 1 247 ? 13.348 21.967 37.707 1.00 13.41 ? 255 PHE A CG 1 ATOM 3737 C CD1 . PHE A 1 247 ? 13.726 21.484 38.944 1.00 14.17 ? 255 PHE A CD1 1 ATOM 3738 C CD2 . PHE A 1 247 ? 12.184 22.721 37.640 1.00 13.20 ? 255 PHE A CD2 1 ATOM 3739 C CE1 . PHE A 1 247 ? 12.971 21.757 40.067 1.00 15.14 ? 255 PHE A CE1 1 ATOM 3740 C CE2 . PHE A 1 247 ? 11.431 22.980 38.755 1.00 13.71 ? 255 PHE A CE2 1 ATOM 3741 C CZ . PHE A 1 247 ? 11.845 22.505 39.974 1.00 15.10 ? 255 PHE A CZ 1 ATOM 3742 H H . PHE A 1 247 ? 15.525 23.505 37.042 1.00 16.19 ? 255 PHE A H 1 ATOM 3743 H HA . PHE A 1 247 ? 15.843 20.902 37.275 1.00 15.92 ? 255 PHE A HA 1 ATOM 3744 H HB2 . PHE A 1 247 ? 13.906 22.308 35.787 1.00 16.26 ? 255 PHE A HB2 1 ATOM 3745 H HB3 . PHE A 1 247 ? 13.811 20.766 36.140 1.00 16.26 ? 255 PHE A HB3 1 ATOM 3746 H HD1 . PHE A 1 247 ? 14.493 20.964 39.020 1.00 17.00 ? 255 PHE A HD1 1 ATOM 3747 H HD2 . PHE A 1 247 ? 11.897 23.039 36.814 1.00 15.84 ? 255 PHE A HD2 1 ATOM 3748 H HE1 . PHE A 1 247 ? 13.244 21.437 40.896 1.00 18.17 ? 255 PHE A HE1 1 ATOM 3749 H HE2 . PHE A 1 247 ? 10.663 23.501 38.692 1.00 16.45 ? 255 PHE A HE2 1 ATOM 3750 H HZ . PHE A 1 247 ? 11.349 22.693 40.738 1.00 18.13 ? 255 PHE A HZ 1 ATOM 3751 N N . ASN A 1 248 ? 16.482 22.139 34.396 1.00 13.01 ? 256 ASN A N 1 ATOM 3752 C CA . ASN A 1 248 ? 17.171 21.842 33.146 1.00 12.21 ? 256 ASN A CA 1 ATOM 3753 C C . ASN A 1 248 ? 18.573 21.312 33.435 1.00 12.57 ? 256 ASN A C 1 ATOM 3754 O O . ASN A 1 248 ? 19.004 20.312 32.850 1.00 13.31 ? 256 ASN A O 1 ATOM 3755 C CB . ASN A 1 248 ? 17.239 23.110 32.303 1.00 12.48 ? 256 ASN A CB 1 ATOM 3756 C CG . ASN A 1 248 ? 17.427 22.816 30.854 1.00 13.24 ? 256 ASN A CG 1 ATOM 3757 O OD1 . ASN A 1 248 ? 16.496 22.321 30.216 1.00 13.48 ? 256 ASN A OD1 1 ATOM 3758 N ND2 . ASN A 1 248 ? 18.595 23.129 30.311 1.00 14.37 ? 256 ASN A ND2 1 ATOM 3759 H H . ASN A 1 248 ? 16.233 22.957 34.484 1.00 15.61 ? 256 ASN A H 1 ATOM 3760 H HA . ASN A 1 248 ? 16.678 21.167 32.653 1.00 14.65 ? 256 ASN A HA 1 ATOM 3761 H HB2 . ASN A 1 248 ? 16.410 23.604 32.406 1.00 14.98 ? 256 ASN A HB2 1 ATOM 3762 H HB3 . ASN A 1 248 ? 17.988 23.649 32.601 1.00 14.98 ? 256 ASN A HB3 1 ATOM 3763 H HD21 . ASN A 1 248 ? 18.737 22.973 29.477 1.00 17.24 ? 256 ASN A HD21 1 ATOM 3764 H HD22 . ASN A 1 248 ? 19.211 23.488 30.792 1.00 17.24 ? 256 ASN A HD22 1 ATOM 3765 N N . GLU A 1 249 ? 19.280 21.948 34.382 1.00 13.10 ? 257 GLU A N 1 ATOM 3766 C CA . GLU A 1 249 ? 20.629 21.527 34.740 1.00 14.46 ? 257 GLU A CA 1 ATOM 3767 C C . GLU A 1 249 ? 20.618 20.129 35.328 1.00 14.88 ? 257 GLU A C 1 ATOM 3768 O O . GLU A 1 249 ? 21.471 19.294 34.991 1.00 15.71 ? 257 GLU A O 1 ATOM 3769 C CB . GLU A 1 249 ? 21.213 22.516 35.746 1.00 16.37 ? 257 GLU A CB 1 ATOM 3770 C CG . GLU A 1 249 ? 21.535 23.854 35.135 1.00 18.84 ? 257 GLU A CG 1 ATOM 3771 C CD . GLU A 1 249 ? 21.966 24.885 36.139 1.00 25.25 ? 257 GLU A CD 1 ATOM 3772 O OE1 . GLU A 1 249 ? 21.752 24.678 37.353 1.00 27.24 ? 257 GLU A OE1 1 ATOM 3773 O OE2 . GLU A 1 249 ? 22.511 25.919 35.698 1.00 26.49 ? 257 GLU A OE2 1 ATOM 3774 H H . GLU A 1 249 ? 18.994 22.625 34.828 1.00 15.72 ? 257 GLU A H 1 ATOM 3775 H HA . GLU A 1 249 ? 21.189 21.524 33.948 1.00 17.35 ? 257 GLU A HA 1 ATOM 3776 H HB2 . GLU A 1 249 ? 20.570 22.659 36.458 1.00 19.65 ? 257 GLU A HB2 1 ATOM 3777 H HB3 . GLU A 1 249 ? 22.034 22.149 36.111 1.00 19.65 ? 257 GLU A HB3 1 ATOM 3778 H HG2 . GLU A 1 249 ? 22.256 23.741 34.496 1.00 22.61 ? 257 GLU A HG2 1 ATOM 3779 H HG3 . GLU A 1 249 ? 20.744 24.190 34.684 1.00 22.61 ? 257 GLU A HG3 1 ATOM 3780 N N . GLU A 1 250 ? 19.657 19.851 36.209 1.00 14.11 ? 258 GLU A N 1 ATOM 3781 C CA . GLU A 1 250 ? 19.595 18.527 36.809 1.00 15.04 ? 258 GLU A CA 1 ATOM 3782 C C . GLU A 1 250 ? 19.290 17.454 35.774 1.00 14.47 ? 258 GLU A C 1 ATOM 3783 O O . GLU A 1 250 ? 19.849 16.353 35.831 1.00 14.19 ? 258 GLU A O 1 ATOM 3784 C CB . GLU A 1 250 ? 18.558 18.512 37.921 1.00 18.15 ? 258 GLU A CB 1 ATOM 3785 C CG . GLU A 1 250 ? 18.564 17.229 38.738 1.00 24.69 ? 258 GLU A CG 1 ATOM 3786 C CD . GLU A 1 250 ? 19.918 16.875 39.295 1.00 32.70 ? 258 GLU A CD 1 ATOM 3787 O OE1 . GLU A 1 250 ? 20.653 17.793 39.729 1.00 32.44 ? 258 GLU A OE1 1 ATOM 3788 O OE2 . GLU A 1 250 ? 20.242 15.660 39.303 1.00 38.19 ? 258 GLU A OE2 1 ATOM 3789 H H . GLU A 1 250 ? 19.046 20.397 36.468 1.00 16.94 ? 258 GLU A H 1 ATOM 3790 H HA . GLU A 1 250 ? 20.457 18.321 37.204 1.00 18.04 ? 258 GLU A HA 1 ATOM 3791 H HB2 . GLU A 1 250 ? 18.735 19.250 38.525 1.00 21.78 ? 258 GLU A HB2 1 ATOM 3792 H HB3 . GLU A 1 250 ? 17.676 18.611 37.528 1.00 21.78 ? 258 GLU A HB3 1 ATOM 3793 H HG2 . GLU A 1 250 ? 17.953 17.330 39.484 1.00 29.63 ? 258 GLU A HG2 1 ATOM 3794 H HG3 . GLU A 1 250 ? 18.275 16.496 38.172 1.00 29.63 ? 258 GLU A HG3 1 ATOM 3795 N N . TYR A 1 251 ? 18.372 17.733 34.849 1.00 13.57 ? 259 TYR A N 1 ATOM 3796 C CA . TYR A 1 251 ? 18.060 16.747 33.822 1.00 14.15 ? 259 TYR A CA 1 ATOM 3797 C C . TYR A 1 251 ? 19.311 16.409 33.025 1.00 12.63 ? 259 TYR A C 1 ATOM 3798 O O . TYR A 1 251 ? 19.615 15.241 32.776 1.00 13.77 ? 259 TYR A O 1 ATOM 3799 C CB . TYR A 1 251 ? 16.935 17.278 32.925 1.00 13.61 ? 259 TYR A CB 1 ATOM 3800 C CG . TYR A 1 251 ? 16.347 16.185 32.036 1.00 13.27 ? 259 TYR A CG 1 ATOM 3801 C CD1 . TYR A 1 251 ? 15.190 15.511 32.389 1.00 14.07 ? 259 TYR A CD1 1 ATOM 3802 C CD2 . TYR A 1 251 ? 16.953 15.825 30.849 1.00 12.99 ? 259 TYR A CD2 1 ATOM 3803 C CE1 . TYR A 1 251 ? 14.679 14.493 31.611 1.00 14.24 ? 259 TYR A CE1 1 ATOM 3804 C CE2 . TYR A 1 251 ? 16.441 14.819 30.057 1.00 12.90 ? 259 TYR A CE2 1 ATOM 3805 C CZ . TYR A 1 251 ? 15.307 14.155 30.451 1.00 13.14 ? 259 TYR A CZ 1 ATOM 3806 O OH . TYR A 1 251 ? 14.794 13.118 29.716 1.00 14.68 ? 259 TYR A OH 1 ATOM 3807 H H . TYR A 1 251 ? 17.928 18.467 34.795 1.00 16.28 ? 259 TYR A H 1 ATOM 3808 H HA . TYR A 1 251 ? 17.747 15.934 34.248 1.00 16.98 ? 259 TYR A HA 1 ATOM 3809 H HB2 . TYR A 1 251 ? 16.224 17.630 33.482 1.00 16.33 ? 259 TYR A HB2 1 ATOM 3810 H HB3 . TYR A 1 251 ? 17.288 17.977 32.352 1.00 16.33 ? 259 TYR A HB3 1 ATOM 3811 H HD1 . TYR A 1 251 ? 14.768 15.725 33.190 1.00 16.88 ? 259 TYR A HD1 1 ATOM 3812 H HD2 . TYR A 1 251 ? 17.732 16.260 30.586 1.00 15.59 ? 259 TYR A HD2 1 ATOM 3813 H HE1 . TYR A 1 251 ? 13.910 14.041 31.877 1.00 17.09 ? 259 TYR A HE1 1 ATOM 3814 H HE2 . TYR A 1 251 ? 16.875 14.577 29.271 1.00 15.48 ? 259 TYR A HE2 1 ATOM 3815 H HH . TYR A 1 251 ? 15.257 12.998 29.025 1.00 17.62 ? 259 TYR A HH 1 ATOM 3816 N N . LEU A 1 252 ? 20.053 17.434 32.610 1.00 13.22 ? 260 LEU A N 1 ATOM 3817 C CA . LEU A 1 252 ? 21.307 17.218 31.900 1.00 13.83 ? 260 LEU A CA 1 ATOM 3818 C C . LEU A 1 252 ? 22.293 16.400 32.712 1.00 14.18 ? 260 LEU A C 1 ATOM 3819 O O . LEU A 1 252 ? 22.957 15.508 32.170 1.00 14.64 ? 260 LEU A O 1 ATOM 3820 C CB . LEU A 1 252 ? 21.920 18.557 31.521 1.00 14.83 ? 260 LEU A CB 1 ATOM 3821 C CG . LEU A 1 252 ? 21.264 19.208 30.309 1.00 15.77 ? 260 LEU A CG 1 ATOM 3822 C CD1 . LEU A 1 252 ? 21.633 20.669 30.240 1.00 17.03 ? 260 LEU A CD1 1 ATOM 3823 C CD2 . LEU A 1 252 ? 21.730 18.499 29.050 1.00 19.27 ? 260 LEU A CD2 1 ATOM 3824 H H . LEU A 1 252 ? 19.851 18.262 32.728 1.00 15.86 ? 260 LEU A H 1 ATOM 3825 H HA . LEU A 1 252 ? 21.123 16.733 31.080 1.00 16.59 ? 260 LEU A HA 1 ATOM 3826 H HB2 . LEU A 1 252 ? 21.829 19.166 32.270 1.00 17.80 ? 260 LEU A HB2 1 ATOM 3827 H HB3 . LEU A 1 252 ? 22.859 18.425 31.315 1.00 17.80 ? 260 LEU A HB3 1 ATOM 3828 H HG . LEU A 1 252 ? 20.300 19.130 30.374 1.00 18.92 ? 260 LEU A HG 1 ATOM 3829 H HD11 . LEU A 1 252 ? 21.207 21.065 29.463 1.00 20.43 ? 260 LEU A HD11 1 ATOM 3830 H HD12 . LEU A 1 252 ? 21.326 21.110 31.047 1.00 20.43 ? 260 LEU A HD12 1 ATOM 3831 H HD13 . LEU A 1 252 ? 22.597 20.748 30.165 1.00 20.43 ? 260 LEU A HD13 1 ATOM 3832 H HD21 . LEU A 1 252 ? 21.311 18.916 28.281 1.00 23.12 ? 260 LEU A HD21 1 ATOM 3833 H HD22 . LEU A 1 252 ? 22.695 18.576 28.984 1.00 23.12 ? 260 LEU A HD22 1 ATOM 3834 H HD23 . LEU A 1 252 ? 21.475 17.565 29.101 1.00 23.12 ? 260 LEU A HD23 1 ATOM 3835 N N . LYS A 1 253 ? 22.387 16.670 34.007 1.00 14.17 ? 261 LYS A N 1 ATOM 3836 C CA . LYS A 1 253 ? 23.285 15.899 34.857 1.00 15.09 ? 261 LYS A CA 1 ATOM 3837 C C . LYS A 1 253 ? 22.906 14.423 34.862 1.00 14.45 ? 261 LYS A C 1 ATOM 3838 O O . LYS A 1 253 ? 23.776 13.553 34.804 1.00 15.57 ? 261 LYS A O 1 ATOM 3839 C CB . LYS A 1 253 ? 23.252 16.457 36.275 1.00 17.63 ? 261 LYS A CB 1 ATOM 3840 C CG . LYS A 1 253 ? 24.116 15.713 37.269 1.00 24.57 ? 261 LYS A CG 1 ATOM 3841 C CD . LYS A 1 253 ? 23.982 16.269 38.678 1.00 30.92 ? 261 LYS A CD 1 ATOM 3842 C CE . LYS A 1 253 ? 24.927 15.526 39.624 1.00 37.65 ? 261 LYS A CE 1 ATOM 3843 N NZ . LYS A 1 253 ? 24.709 14.031 39.624 1.00 41.13 ? 261 LYS A NZ 1 ATOM 3844 H H . LYS A 1 253 ? 21.947 17.287 34.415 1.00 17.01 ? 261 LYS A H 1 ATOM 3845 H HA . LYS A 1 253 ? 24.191 15.979 34.520 1.00 18.11 ? 261 LYS A HA 1 ATOM 3846 H HB2 . LYS A 1 253 ? 23.557 17.378 36.252 1.00 21.16 ? 261 LYS A HB2 1 ATOM 3847 H HB3 . LYS A 1 253 ? 22.338 16.425 36.598 1.00 21.16 ? 261 LYS A HB3 1 ATOM 3848 H HG2 . LYS A 1 253 ? 23.850 14.781 37.287 1.00 29.49 ? 261 LYS A HG2 1 ATOM 3849 H HG3 . LYS A 1 253 ? 25.046 15.789 37.002 1.00 29.49 ? 261 LYS A HG3 1 ATOM 3850 H HD2 . LYS A 1 253 ? 24.220 17.210 38.680 1.00 37.11 ? 261 LYS A HD2 1 ATOM 3851 H HD3 . LYS A 1 253 ? 23.072 16.147 38.991 1.00 37.11 ? 261 LYS A HD3 1 ATOM 3852 H HE2 . LYS A 1 253 ? 25.842 15.695 39.351 1.00 45.18 ? 261 LYS A HE2 1 ATOM 3853 H HE3 . LYS A 1 253 ? 24.786 15.849 40.527 1.00 45.18 ? 261 LYS A HE3 1 ATOM 3854 H HZ1 . LYS A 1 253 ? 25.278 13.641 40.186 1.00 49.36 ? 261 LYS A HZ1 1 ATOM 3855 H HZ2 . LYS A 1 253 ? 23.877 13.844 39.879 1.00 49.36 ? 261 LYS A HZ2 1 ATOM 3856 H HZ3 . LYS A 1 253 ? 24.841 13.704 38.806 1.00 49.36 ? 261 LYS A HZ3 1 ATOM 3857 N N . VAL A 1 254 ? 21.611 14.115 34.915 1.00 14.60 ? 262 VAL A N 1 ATOM 3858 C CA . VAL A 1 254 ? 21.180 12.716 34.885 1.00 15.42 ? 262 VAL A CA 1 ATOM 3859 C C . VAL A 1 254 ? 21.592 12.046 33.580 1.00 13.99 ? 262 VAL A C 1 ATOM 3860 O O . VAL A 1 254 ? 22.075 10.909 33.580 1.00 13.88 ? 262 VAL A O 1 ATOM 3861 C CB . VAL A 1 254 ? 19.663 12.605 35.109 1.00 15.90 ? 262 VAL A CB 1 ATOM 3862 C CG1 . VAL A 1 254 ? 19.186 11.172 34.866 1.00 16.16 ? 262 VAL A CG1 1 ATOM 3863 C CG2 . VAL A 1 254 ? 19.299 13.069 36.516 1.00 17.55 ? 262 VAL A CG2 1 ATOM 3864 H H . VAL A 1 254 ? 20.971 14.687 34.968 1.00 17.53 ? 262 VAL A H 1 ATOM 3865 H HA . VAL A 1 254 ? 21.618 12.242 35.609 1.00 18.50 ? 262 VAL A HA 1 ATOM 3866 H HB . VAL A 1 254 ? 19.208 13.183 34.477 1.00 19.09 ? 262 VAL A HB 1 ATOM 3867 H HG11 . VAL A 1 254 ? 18.229 11.128 35.013 1.00 19.40 ? 262 VAL A HG11 1 ATOM 3868 H HG12 . VAL A 1 254 ? 19.392 10.922 33.951 1.00 19.40 ? 262 VAL A HG12 1 ATOM 3869 H HG13 . VAL A 1 254 ? 19.644 10.578 35.482 1.00 19.40 ? 262 VAL A HG13 1 ATOM 3870 H HG21 . VAL A 1 254 ? 18.340 12.991 36.635 1.00 21.06 ? 262 VAL A HG21 1 ATOM 3871 H HG22 . VAL A 1 254 ? 19.760 12.511 37.161 1.00 21.06 ? 262 VAL A HG22 1 ATOM 3872 H HG23 . VAL A 1 254 ? 19.572 13.994 36.623 1.00 21.06 ? 262 VAL A HG23 1 ATOM 3873 N N . ILE A 1 255 ? 21.344 12.704 32.442 1.00 13.91 ? 263 ILE A N 1 ATOM 3874 C CA . ILE A 1 255 ? 21.733 12.116 31.162 1.00 13.82 ? 263 ILE A CA 1 ATOM 3875 C C . ILE A 1 255 ? 23.241 11.919 31.096 1.00 13.62 ? 263 ILE A C 1 ATOM 3876 O O . ILE A 1 255 ? 23.722 10.892 30.607 1.00 14.99 ? 263 ILE A O 1 ATOM 3877 C CB . ILE A 1 255 ? 21.207 12.966 29.985 1.00 13.83 ? 263 ILE A CB 1 ATOM 3878 C CG1 . ILE A 1 255 ? 19.691 13.160 30.062 1.00 13.65 ? 263 ILE A CG1 1 ATOM 3879 C CG2 . ILE A 1 255 ? 21.617 12.311 28.657 1.00 14.82 ? 263 ILE A CG2 1 ATOM 3880 C CD1 . ILE A 1 255 ? 18.885 11.895 30.101 1.00 15.14 ? 263 ILE A CD1 1 ATOM 3881 H H . ILE A 1 255 ? 20.961 13.472 32.386 1.00 16.70 ? 263 ILE A H 1 ATOM 3882 H HA . ILE A 1 255 ? 21.323 11.239 31.092 1.00 16.58 ? 263 ILE A HA 1 ATOM 3883 H HB . ILE A 1 255 ? 21.625 13.840 30.033 1.00 16.60 ? 263 ILE A HB 1 ATOM 3884 H HG12 . ILE A 1 255 ? 19.485 13.661 30.867 1.00 16.38 ? 263 ILE A HG12 1 ATOM 3885 H HG13 . ILE A 1 255 ? 19.405 13.664 29.284 1.00 16.38 ? 263 ILE A HG13 1 ATOM 3886 H HG21 . ILE A 1 255 ? 21.283 12.850 27.923 1.00 17.79 ? 263 ILE A HG21 1 ATOM 3887 H HG22 . ILE A 1 255 ? 22.585 12.259 28.617 1.00 17.79 ? 263 ILE A HG22 1 ATOM 3888 H HG23 . ILE A 1 255 ? 21.235 11.420 28.614 1.00 17.79 ? 263 ILE A HG23 1 ATOM 3889 H HD11 . ILE A 1 255 ? 17.943 12.123 30.149 1.00 18.16 ? 263 ILE A HD11 1 ATOM 3890 H HD12 . ILE A 1 255 ? 19.061 11.384 29.295 1.00 18.16 ? 263 ILE A HD12 1 ATOM 3891 H HD13 . ILE A 1 255 ? 19.142 11.381 30.882 1.00 18.16 ? 263 ILE A HD13 1 ATOM 3892 N N . GLN A 1 256 ? 24.008 12.908 31.540 1.00 14.35 ? 264 GLN A N 1 ATOM 3893 C CA . GLN A 1 256 ? 25.456 12.779 31.502 1.00 15.26 ? 264 GLN A CA 1 ATOM 3894 C C . GLN A 1 256 ? 25.942 11.615 32.355 1.00 15.73 ? 264 GLN A C 1 ATOM 3895 O O . GLN A 1 256 ? 26.909 10.943 31.982 1.00 18.24 ? 264 GLN A O 1 ATOM 3896 C CB . GLN A 1 256 ? 26.107 14.109 31.880 1.00 17.05 ? 264 GLN A CB 1 ATOM 3897 C CG . GLN A 1 256 ? 25.941 15.142 30.744 1.00 20.62 ? 264 GLN A CG 1 ATOM 3898 C CD . GLN A 1 256 ? 25.993 16.577 31.223 1.00 23.99 ? 264 GLN A CD 1 ATOM 3899 O OE1 . GLN A 1 256 ? 26.411 16.856 32.343 1.00 25.37 ? 264 GLN A OE1 1 ATOM 3900 N NE2 . GLN A 1 256 ? 25.528 17.497 30.386 1.00 24.57 ? 264 GLN A NE2 1 ATOM 3901 H H . GLN A 1 256 ? 23.719 13.652 31.863 1.00 17.22 ? 264 GLN A H 1 ATOM 3902 H HA . GLN A 1 256 ? 25.715 12.587 30.588 1.00 18.31 ? 264 GLN A HA 1 ATOM 3903 H HB2 . GLN A 1 256 ? 25.682 14.461 32.678 1.00 20.47 ? 264 GLN A HB2 1 ATOM 3904 H HB3 . GLN A 1 256 ? 27.055 13.972 32.034 1.00 20.47 ? 264 GLN A HB3 1 ATOM 3905 H HG2 . GLN A 1 256 ? 26.656 15.017 30.100 1.00 24.75 ? 264 GLN A HG2 1 ATOM 3906 H HG3 . GLN A 1 256 ? 25.083 15.002 30.315 1.00 24.75 ? 264 GLN A HG3 1 ATOM 3907 H HE21 . GLN A 1 256 ? 25.220 17.264 29.618 1.00 29.49 ? 264 GLN A HE21 1 ATOM 3908 H HE22 . GLN A 1 256 ? 25.536 18.327 30.613 1.00 29.49 ? 264 GLN A HE22 1 ATOM 3909 N N . LYS A 1 257 ? 25.305 11.356 33.500 1.00 14.61 ? 265 LYS A N 1 ATOM 3910 C CA . LYS A 1 257 ? 25.739 10.256 34.354 1.00 15.69 ? 265 LYS A CA 1 ATOM 3911 C C . LYS A 1 257 ? 25.273 8.912 33.811 1.00 15.68 ? 265 LYS A C 1 ATOM 3912 O O . LYS A 1 257 ? 26.004 7.923 33.881 1.00 17.46 ? 265 LYS A O 1 ATOM 3913 C CB . LYS A 1 257 ? 25.222 10.455 35.780 1.00 16.15 ? 265 LYS A CB 1 ATOM 3914 C CG . LYS A 1 257 ? 25.571 9.296 36.700 1.00 18.23 ? 265 LYS A CG 1 ATOM 3915 C CD . LYS A 1 257 ? 25.286 9.606 38.169 1.00 22.76 ? 265 LYS A CD 1 ATOM 3916 C CE . LYS A 1 257 ? 25.623 8.407 39.041 1.00 27.21 ? 265 LYS A CE 1 ATOM 3917 N NZ . LYS A 1 257 ? 25.314 8.662 40.469 1.00 31.73 ? 265 LYS A NZ 1 ATOM 3918 H H . LYS A 1 257 ? 24.629 11.797 33.798 1.00 17.53 ? 265 LYS A H 1 ATOM 3919 H HA . LYS A 1 257 ? 26.709 10.246 34.386 1.00 18.83 ? 265 LYS A HA 1 ATOM 3920 H HB2 . LYS A 1 257 ? 25.617 11.261 36.149 1.00 19.39 ? 265 LYS A HB2 1 ATOM 3921 H HB3 . LYS A 1 257 ? 24.256 10.540 35.757 1.00 19.39 ? 265 LYS A HB3 1 ATOM 3922 H HG2 . LYS A 1 257 ? 25.043 8.522 36.448 1.00 21.87 ? 265 LYS A HG2 1 ATOM 3923 H HG3 . LYS A 1 257 ? 26.516 9.096 36.613 1.00 21.87 ? 265 LYS A HG3 1 ATOM 3924 H HD2 . LYS A 1 257 ? 25.832 10.356 38.453 1.00 27.31 ? 265 LYS A HD2 1 ATOM 3925 H HD3 . LYS A 1 257 ? 24.345 9.811 38.280 1.00 27.31 ? 265 LYS A HD3 1 ATOM 3926 H HE2 . LYS A 1 257 ? 25.102 7.643 38.749 1.00 32.65 ? 265 LYS A HE2 1 ATOM 3927 H HE3 . LYS A 1 257 ? 26.571 8.215 38.966 1.00 32.65 ? 265 LYS A HE3 1 ATOM 3928 H HZ1 . LYS A 1 257 ? 25.520 7.947 40.957 1.00 38.07 ? 265 LYS A HZ1 1 ATOM 3929 H HZ2 . LYS A 1 257 ? 25.784 9.358 40.762 1.00 38.07 ? 265 LYS A HZ2 1 ATOM 3930 H HZ3 . LYS A 1 257 ? 24.446 8.838 40.565 1.00 38.07 ? 265 LYS A HZ3 1 ATOM 3931 N N . HIS A 1 258 ? 24.066 8.843 33.263 1.00 14.23 ? 266 HIS A N 1 ATOM 3932 C CA . HIS A 1 258 ? 23.417 7.562 33.021 1.00 14.04 ? 266 HIS A CA 1 ATOM 3933 C C . HIS A 1 258 ? 23.225 7.220 31.548 1.00 13.91 ? 266 HIS A C 1 ATOM 3934 O O . HIS A 1 258 ? 22.507 6.262 31.242 1.00 13.98 ? 266 HIS A O 1 ATOM 3935 C CB . HIS A 1 258 ? 22.070 7.509 33.733 1.00 13.68 ? 266 HIS A CB 1 ATOM 3936 C CG . HIS A 1 258 ? 22.182 7.520 35.223 1.00 14.20 ? 266 HIS A CG 1 ATOM 3937 N ND1 . HIS A 1 258 ? 22.575 6.417 35.941 1.00 15.58 ? 266 HIS A ND1 1 ATOM 3938 C CD2 . HIS A 1 258 ? 21.943 8.497 36.129 1.00 15.82 ? 266 HIS A CD2 1 ATOM 3939 C CE1 . HIS A 1 258 ? 22.571 6.711 37.229 1.00 16.93 ? 266 HIS A CE1 1 ATOM 3940 N NE2 . HIS A 1 258 ? 22.198 7.970 37.372 1.00 17.29 ? 266 HIS A NE2 1 ATOM 3941 H H . HIS A 1 258 ? 23.601 9.525 33.022 1.00 17.08 ? 266 HIS A H 1 ATOM 3942 H HA . HIS A 1 258 ? 23.972 6.866 33.406 1.00 16.85 ? 266 HIS A HA 1 ATOM 3943 H HB2 . HIS A 1 258 ? 21.545 8.281 33.468 1.00 16.42 ? 266 HIS A HB2 1 ATOM 3944 H HB3 . HIS A 1 258 ? 21.610 6.695 33.475 1.00 16.42 ? 266 HIS A HB3 1 ATOM 3945 H HD1 . HIS A 1 258 ? 22.783 5.653 35.605 1.00 18.70 ? 266 HIS A HD1 1 ATOM 3946 H HD2 . HIS A 1 258 ? 21.662 9.364 35.945 1.00 18.98 ? 266 HIS A HD2 1 ATOM 3947 H HE1 . HIS A 1 258 ? 22.804 6.132 37.919 1.00 20.32 ? 266 HIS A HE1 1 ATOM 3948 N N . HIS A 1 259 ? 23.824 7.977 30.624 1.00 13.69 ? 267 HIS A N 1 ATOM 3949 C CA . HIS A 1 259 ? 23.514 7.792 29.208 1.00 13.82 ? 267 HIS A CA 1 ATOM 3950 C C . HIS A 1 259 ? 23.739 6.371 28.719 1.00 13.15 ? 267 HIS A C 1 ATOM 3951 O O . HIS A 1 259 ? 23.086 5.958 27.765 1.00 14.14 ? 267 HIS A O 1 ATOM 3952 C CB . HIS A 1 259 ? 24.312 8.760 28.338 1.00 14.65 ? 267 HIS A CB 1 ATOM 3953 C CG . HIS A 1 259 ? 25.801 8.618 28.448 1.00 16.04 ? 267 HIS A CG 1 ATOM 3954 N ND1 . HIS A 1 259 ? 26.559 7.829 27.607 1.00 16.47 ? 267 HIS A ND1 1 ATOM 3955 C CD2 . HIS A 1 259 ? 26.680 9.255 29.251 1.00 17.98 ? 267 HIS A CD2 1 ATOM 3956 C CE1 . HIS A 1 259 ? 27.837 7.949 27.921 1.00 18.18 ? 267 HIS A CE1 1 ATOM 3957 N NE2 . HIS A 1 259 ? 27.937 8.803 28.923 1.00 19.65 ? 267 HIS A NE2 1 ATOM 3958 H H . HIS A 1 259 ? 24.403 8.592 30.788 1.00 16.43 ? 267 HIS A H 1 ATOM 3959 H HA . HIS A 1 259 ? 22.574 7.995 29.076 1.00 16.59 ? 267 HIS A HA 1 ATOM 3960 H HB2 . HIS A 1 259 ? 24.071 8.613 27.410 1.00 17.58 ? 267 HIS A HB2 1 ATOM 3961 H HB3 . HIS A 1 259 ? 24.084 9.667 28.595 1.00 17.58 ? 267 HIS A HB3 1 ATOM 3962 H HD1 . HIS A 1 259 ? 26.246 7.323 26.987 1.00 19.77 ? 267 HIS A HD1 1 ATOM 3963 H HD2 . HIS A 1 259 ? 26.471 9.860 29.926 1.00 21.58 ? 267 HIS A HD2 1 ATOM 3964 H HE1 . HIS A 1 259 ? 28.543 7.502 27.513 1.00 21.81 ? 267 HIS A HE1 1 ATOM 3965 N N . ARG A 1 260 ? 24.686 5.636 29.292 1.00 13.66 ? 268 ARG A N 1 ATOM 3966 C CA . ARG A 1 260 ? 25.009 4.320 28.744 1.00 14.86 ? 268 ARG A CA 1 ATOM 3967 C C . ARG A 1 260 ? 23.861 3.323 28.847 1.00 14.34 ? 268 ARG A C 1 ATOM 3968 O O . ARG A 1 260 ? 23.852 2.342 28.099 1.00 17.40 ? 268 ARG A O 1 ATOM 3969 C CB . ARG A 1 260 ? 26.232 3.744 29.441 1.00 16.71 ? 268 ARG A CB 1 ATOM 3970 C CG . ARG A 1 260 ? 27.497 4.472 29.102 1.00 22.70 ? 268 ARG A CG 1 ATOM 3971 C CD . ARG A 1 260 ? 28.666 4.038 29.993 1.00 27.92 ? 268 ARG A CD 1 ATOM 3972 N NE . ARG A 1 260 ? 29.797 4.945 29.836 1.00 33.51 ? 268 ARG A NE 1 ATOM 3973 C CZ . ARG A 1 260 ? 29.937 6.088 30.500 1.00 35.97 ? 268 ARG A CZ 1 ATOM 3974 N NH1 . ARG A 1 260 ? 29.022 6.468 31.383 1.00 33.99 ? 268 ARG A NH1 1 ATOM 3975 N NH2 . ARG A 1 260 ? 31.001 6.855 30.281 1.00 38.99 ? 268 ARG A NH2 1 ATOM 3976 H H . ARG A 1 260 ? 25.147 5.866 29.981 1.00 16.39 ? 268 ARG A H 1 ATOM 3977 H HA . ARG A 1 260 ? 25.226 4.422 27.804 1.00 17.83 ? 268 ARG A HA 1 ATOM 3978 H HB2 . ARG A 1 260 ? 26.102 3.800 30.400 1.00 20.05 ? 268 ARG A HB2 1 ATOM 3979 H HB3 . ARG A 1 260 ? 26.339 2.818 29.174 1.00 20.05 ? 268 ARG A HB3 1 ATOM 3980 H HG2 . ARG A 1 260 ? 27.734 4.286 28.180 1.00 27.24 ? 268 ARG A HG2 1 ATOM 3981 H HG3 . ARG A 1 260 ? 27.360 5.424 29.226 1.00 27.24 ? 268 ARG A HG3 1 ATOM 3982 H HD2 . ARG A 1 260 ? 28.387 4.053 30.922 1.00 33.51 ? 268 ARG A HD2 1 ATOM 3983 H HD3 . ARG A 1 260 ? 28.951 3.146 29.740 1.00 33.51 ? 268 ARG A HD3 1 ATOM 3984 H HE . ARG A 1 260 ? 30.413 4.727 29.277 1.00 40.21 ? 268 ARG A HE 1 ATOM 3985 H HH11 . ARG A 1 260 ? 28.332 5.975 31.525 1.00 40.78 ? 268 ARG A HH11 1 ATOM 3986 H HH12 . ARG A 1 260 ? 29.119 7.207 31.811 1.00 40.78 ? 268 ARG A HH12 1 ATOM 3987 H HH21 . ARG A 1 260 ? 31.597 6.611 29.711 1.00 46.79 ? 268 ARG A HH21 1 ATOM 3988 H HH22 . ARG A 1 260 ? 31.096 7.593 30.713 1.00 46.79 ? 268 ARG A HH22 1 ATOM 3989 N N . VAL A 1 261 ? 22.886 3.550 29.728 1.00 14.16 ? 269 VAL A N 1 ATOM 3990 C CA . VAL A 1 261 ? 21.718 2.687 29.806 1.00 14.16 ? 269 VAL A CA 1 ATOM 3991 C C . VAL A 1 261 ? 20.515 3.265 29.104 1.00 13.87 ? 269 VAL A C 1 ATOM 3992 O O . VAL A 1 261 ? 19.490 2.593 29.049 1.00 15.33 ? 269 VAL A O 1 ATOM 3993 C CB . VAL A 1 261 ? 21.341 2.275 31.246 1.00 15.35 ? 269 VAL A CB 1 ATOM 3994 C CG1 . VAL A 1 261 ? 22.483 1.575 31.921 1.00 20.55 ? 269 VAL A CG1 1 ATOM 3995 C CG2 . VAL A 1 261 ? 20.828 3.455 32.053 1.00 15.62 ? 269 VAL A CG2 1 ATOM 3996 H H . VAL A 1 261 ? 22.881 4.200 30.291 1.00 16.99 ? 269 VAL A H 1 ATOM 3997 H HA . VAL A 1 261 ? 21.937 1.867 29.337 1.00 16.99 ? 269 VAL A HA 1 ATOM 3998 H HB . VAL A 1 261 ? 20.614 1.635 31.191 1.00 18.43 ? 269 VAL A HB 1 ATOM 3999 H HG11 . VAL A 1 261 ? 22.216 1.330 32.820 1.00 24.66 ? 269 VAL A HG11 1 ATOM 4000 H HG12 . VAL A 1 261 ? 22.710 0.780 31.414 1.00 24.66 ? 269 VAL A HG12 1 ATOM 4001 H HG13 . VAL A 1 261 ? 23.245 2.175 31.954 1.00 24.66 ? 269 VAL A HG13 1 ATOM 4002 H HG21 . VAL A 1 261 ? 20.605 3.151 32.947 1.00 18.74 ? 269 VAL A HG21 1 ATOM 4003 H HG22 . VAL A 1 261 ? 21.521 4.132 32.097 1.00 18.74 ? 269 VAL A HG22 1 ATOM 4004 H HG23 . VAL A 1 261 ? 20.040 3.815 31.619 1.00 18.74 ? 269 VAL A HG23 1 ATOM 4005 N N . ILE A 1 262 ? 20.595 4.485 28.579 1.00 13.00 ? 270 ILE A N 1 ATOM 4006 C CA . ILE A 1 262 ? 19.434 5.145 27.984 1.00 13.34 ? 270 ILE A CA 1 ATOM 4007 C C . ILE A 1 262 ? 19.534 4.978 26.471 1.00 12.74 ? 270 ILE A C 1 ATOM 4008 O O . ILE A 1 262 ? 20.384 5.583 25.819 1.00 13.25 ? 270 ILE A O 1 ATOM 4009 C CB . ILE A 1 262 ? 19.344 6.623 28.377 1.00 12.94 ? 270 ILE A CB 1 ATOM 4010 C CG1 . ILE A 1 262 ? 19.251 6.780 29.896 1.00 13.09 ? 270 ILE A CG1 1 ATOM 4011 C CG2 . ILE A 1 262 ? 18.155 7.260 27.675 1.00 13.66 ? 270 ILE A CG2 1 ATOM 4012 C CD1 . ILE A 1 262 ? 19.418 8.198 30.383 1.00 14.61 ? 270 ILE A CD1 1 ATOM 4013 H H . ILE A 1 262 ? 21.315 4.955 28.555 1.00 15.59 ? 270 ILE A H 1 ATOM 4014 H HA . ILE A 1 262 ? 18.625 4.702 28.285 1.00 16.01 ? 270 ILE A HA 1 ATOM 4015 H HB . ILE A 1 262 ? 20.151 7.069 28.074 1.00 15.53 ? 270 ILE A HB 1 ATOM 4016 H HG12 . ILE A 1 262 ? 18.380 6.469 30.188 1.00 15.71 ? 270 ILE A HG12 1 ATOM 4017 H HG13 . ILE A 1 262 ? 19.945 6.243 30.308 1.00 15.71 ? 270 ILE A HG13 1 ATOM 4018 H HG21 . ILE A 1 262 ? 18.103 8.195 27.928 1.00 16.39 ? 270 ILE A HG21 1 ATOM 4019 H HG22 . ILE A 1 262 ? 18.276 7.182 26.716 1.00 16.39 ? 270 ILE A HG22 1 ATOM 4020 H HG23 . ILE A 1 262 ? 17.345 6.799 27.946 1.00 16.39 ? 270 ILE A HG23 1 ATOM 4021 H HD11 . ILE A 1 262 ? 19.346 8.210 31.351 1.00 17.53 ? 270 ILE A HD11 1 ATOM 4022 H HD12 . ILE A 1 262 ? 20.291 8.523 30.112 1.00 17.53 ? 270 ILE A HD12 1 ATOM 4023 H HD13 . ILE A 1 262 ? 18.723 8.750 29.993 1.00 17.53 ? 270 ILE A HD13 1 ATOM 4024 N N . ALA A 1 263 ? 18.644 4.176 25.906 1.00 13.03 ? 271 ALA A N 1 ATOM 4025 C CA . ALA A 1 263 ? 18.625 3.889 24.472 1.00 13.85 ? 271 ALA A CA 1 ATOM 4026 C C . ALA A 1 263 ? 17.747 4.843 23.687 1.00 15.67 ? 271 ALA A C 1 ATOM 4027 O O . ALA A 1 263 ? 17.722 4.753 22.465 1.00 17.67 ? 271 ALA A O 1 ATOM 4028 C CB . ALA A 1 263 ? 18.111 2.466 24.224 1.00 15.58 ? 271 ALA A CB 1 ATOM 4029 H H . ALA A 1 263 ? 18.021 3.773 26.342 1.00 15.63 ? 271 ALA A H 1 ATOM 4030 H HA . ALA A 1 263 ? 19.528 3.950 24.123 1.00 16.62 ? 271 ALA A HA 1 ATOM 4031 H HB1 . ALA A 1 263 ? 18.105 2.295 23.270 1.00 18.70 ? 271 ALA A HB1 1 ATOM 4032 H HB2 . ALA A 1 263 ? 18.698 1.836 24.671 1.00 18.70 ? 271 ALA A HB2 1 ATOM 4033 H HB3 . ALA A 1 263 ? 17.211 2.390 24.580 1.00 18.70 ? 271 ALA A HB3 1 ATOM 4034 N N . GLY A 1 264 ? 16.999 5.705 24.351 1.00 14.25 ? 272 GLY A N 1 ATOM 4035 C CA . GLY A 1 264 ? 16.183 6.676 23.641 1.00 16.10 ? 272 GLY A CA 1 ATOM 4036 C C . GLY A 1 264 ? 15.400 7.515 24.613 1.00 12.89 ? 272 GLY A C 1 ATOM 4037 O O . GLY A 1 264 ? 15.118 7.068 25.724 1.00 12.20 ? 272 GLY A O 1 ATOM 4038 H H . GLY A 1 264 ? 16.945 5.751 25.208 1.00 17.10 ? 272 GLY A H 1 ATOM 4039 H HA2 . GLY A 1 264 ? 16.749 7.257 23.110 1.00 19.32 ? 272 GLY A HA2 1 ATOM 4040 H HA3 . GLY A 1 264 ? 15.563 6.218 23.052 1.00 19.32 ? 272 GLY A HA3 1 ATOM 4041 N N . GLN A 1 265 ? 15.085 8.736 24.209 1.00 12.15 ? 273 GLN A N 1 ATOM 4042 C CA . GLN A 1 265 ? 14.187 9.619 24.947 1.00 11.13 ? 273 GLN A CA 1 ATOM 4043 C C . GLN A 1 265 ? 13.130 10.113 23.977 1.00 10.78 ? 273 GLN A C 1 ATOM 4044 O O . GLN A 1 265 ? 13.455 10.450 22.830 1.00 11.15 ? 273 GLN A O 1 ATOM 4045 C CB . GLN A 1 265 ? 14.952 10.814 25.529 1.00 11.08 ? 273 GLN A CB 1 ATOM 4046 C CG . GLN A 1 265 ? 16.082 10.456 26.486 1.00 12.47 ? 273 GLN A CG 1 ATOM 4047 C CD . GLN A 1 265 ? 16.850 11.690 26.886 1.00 13.76 ? 273 GLN A CD 1 ATOM 4048 O OE1 . GLN A 1 265 ? 16.337 12.546 27.585 1.00 16.94 ? 273 GLN A OE1 1 ATOM 4049 N NE2 . GLN A 1 265 ? 18.072 11.808 26.403 1.00 15.05 ? 273 GLN A NE2 1 ATOM 4050 H H . GLN A 1 265 ? 15.389 9.090 23.487 1.00 14.58 ? 273 GLN A H 1 ATOM 4051 H HA . GLN A 1 265 ? 13.757 9.133 25.668 1.00 13.35 ? 273 GLN A HA 1 ATOM 4052 H HB2 . GLN A 1 265 ? 15.339 11.319 24.797 1.00 13.30 ? 273 GLN A HB2 1 ATOM 4053 H HB3 . GLN A 1 265 ? 14.325 11.374 26.014 1.00 13.30 ? 273 GLN A HB3 1 ATOM 4054 H HG2 . GLN A 1 265 ? 15.711 10.052 27.287 1.00 14.97 ? 273 GLN A HG2 1 ATOM 4055 H HG3 . GLN A 1 265 ? 16.693 9.842 26.049 1.00 14.97 ? 273 GLN A HG3 1 ATOM 4056 H HE21 . GLN A 1 265 ? 18.391 11.198 25.887 1.00 18.05 ? 273 GLN A HE21 1 ATOM 4057 H HE22 . GLN A 1 265 ? 18.549 12.495 26.602 1.00 18.05 ? 273 GLN A HE22 1 ATOM 4058 N N . PHE A 1 266 ? 11.881 10.163 24.453 1.00 10.52 ? 274 PHE A N 1 ATOM 4059 C CA . PHE A 1 266 ? 10.714 10.390 23.593 1.00 10.79 ? 274 PHE A CA 1 ATOM 4060 C C . PHE A 1 266 ? 9.781 11.378 24.278 1.00 10.29 ? 274 PHE A C 1 ATOM 4061 O O . PHE A 1 266 ? 9.228 11.075 25.339 1.00 11.61 ? 274 PHE A O 1 ATOM 4062 C CB . PHE A 1 266 ? 9.988 9.071 23.301 1.00 11.66 ? 274 PHE A CB 1 ATOM 4063 C CG . PHE A 1 266 ? 10.900 7.968 22.824 1.00 11.83 ? 274 PHE A CG 1 ATOM 4064 C CD1 . PHE A 1 266 ? 11.636 7.199 23.715 1.00 12.34 ? 274 PHE A CD1 1 ATOM 4065 C CD2 . PHE A 1 266 ? 11.110 7.744 21.486 1.00 11.86 ? 274 PHE A CD2 1 ATOM 4066 C CE1 . PHE A 1 266 ? 12.480 6.212 23.262 1.00 13.59 ? 274 PHE A CE1 1 ATOM 4067 C CE2 . PHE A 1 266 ? 11.960 6.749 21.026 1.00 13.66 ? 274 PHE A CE2 1 ATOM 4068 C CZ . PHE A 1 266 ? 12.658 6.006 21.921 1.00 13.72 ? 274 PHE A CZ 1 ATOM 4069 H H . PHE A 1 266 ? 11.682 10.066 25.284 1.00 12.62 ? 274 PHE A H 1 ATOM 4070 H HA . PHE A 1 266 ? 11.004 10.774 22.751 1.00 12.95 ? 274 PHE A HA 1 ATOM 4071 H HB2 . PHE A 1 266 ? 9.554 8.766 24.113 1.00 13.99 ? 274 PHE A HB2 1 ATOM 4072 H HB3 . PHE A 1 266 ? 9.324 9.226 22.610 1.00 13.99 ? 274 PHE A HB3 1 ATOM 4073 H HD1 . PHE A 1 266 ? 11.531 7.329 24.630 1.00 14.81 ? 274 PHE A HD1 1 ATOM 4074 H HD2 . PHE A 1 266 ? 10.639 8.253 20.866 1.00 14.23 ? 274 PHE A HD2 1 ATOM 4075 H HE1 . PHE A 1 266 ? 12.956 5.697 23.873 1.00 16.31 ? 274 PHE A HE1 1 ATOM 4076 H HE2 . PHE A 1 266 ? 12.072 6.612 20.113 1.00 16.40 ? 274 PHE A HE2 1 ATOM 4077 H HZ . PHE A 1 266 ? 13.228 5.334 21.624 1.00 16.47 ? 274 PHE A HZ 1 ATOM 4078 N N . PHE A 1 267 ? 9.662 12.584 23.707 1.00 10.25 ? 275 PHE A N 1 ATOM 4079 C CA . PHE A 1 267 ? 8.925 13.687 24.322 1.00 9.90 ? 275 PHE A CA 1 ATOM 4080 C C . PHE A 1 267 ? 8.004 14.322 23.292 1.00 9.69 ? 275 PHE A C 1 ATOM 4081 O O . PHE A 1 267 ? 8.062 14.000 22.096 1.00 11.20 ? 275 PHE A O 1 ATOM 4082 C CB . PHE A 1 267 ? 9.892 14.711 24.935 1.00 10.20 ? 275 PHE A CB 1 ATOM 4083 C CG . PHE A 1 267 ? 10.474 14.277 26.271 1.00 10.80 ? 275 PHE A CG 1 ATOM 4084 C CD1 . PHE A 1 267 ? 11.424 13.259 26.358 1.00 12.12 ? 275 PHE A CD1 1 ATOM 4085 C CD2 . PHE A 1 267 ? 10.065 14.882 27.440 1.00 12.18 ? 275 PHE A CD2 1 ATOM 4086 C CE1 . PHE A 1 267 ? 11.919 12.869 27.584 1.00 13.04 ? 275 PHE A CE1 1 ATOM 4087 C CE2 . PHE A 1 267 ? 10.578 14.514 28.647 1.00 13.07 ? 275 PHE A CE2 1 ATOM 4088 C CZ . PHE A 1 267 ? 11.510 13.494 28.732 1.00 13.03 ? 275 PHE A CZ 1 ATOM 4089 H H . PHE A 1 267 ? 10.008 12.788 22.947 1.00 12.29 ? 275 PHE A H 1 ATOM 4090 H HA . PHE A 1 267 ? 8.373 13.335 25.037 1.00 11.88 ? 275 PHE A HA 1 ATOM 4091 H HB2 . PHE A 1 267 ? 10.630 14.852 24.321 1.00 12.24 ? 275 PHE A HB2 1 ATOM 4092 H HB3 . PHE A 1 267 ? 9.417 15.545 25.075 1.00 12.24 ? 275 PHE A HB3 1 ATOM 4093 H HD1 . PHE A 1 267 ? 11.708 12.825 25.586 1.00 14.54 ? 275 PHE A HD1 1 ATOM 4094 H HD2 . PHE A 1 267 ? 9.438 15.569 27.402 1.00 14.62 ? 275 PHE A HD2 1 ATOM 4095 H HE1 . PHE A 1 267 ? 12.555 12.192 27.630 1.00 15.65 ? 275 PHE A HE1 1 ATOM 4096 H HE2 . PHE A 1 267 ? 10.284 14.936 29.422 1.00 15.68 ? 275 PHE A HE2 1 ATOM 4097 H HZ . PHE A 1 267 ? 11.853 13.237 29.557 1.00 15.64 ? 275 PHE A HZ 1 ATOM 4098 N N . GLY A 1 268 ? 7.131 15.202 23.757 1.00 10.85 ? 276 GLY A N 1 ATOM 4099 C CA . GLY A 1 268 ? 6.168 15.894 22.922 1.00 11.53 ? 276 GLY A CA 1 ATOM 4100 C C . GLY A 1 268 ? 6.165 17.390 23.217 1.00 10.87 ? 276 GLY A C 1 ATOM 4101 O O . GLY A 1 268 ? 7.236 18.004 23.274 1.00 11.03 ? 276 GLY A O 1 ATOM 4102 H H . GLY A 1 268 ? 7.077 15.421 24.586 1.00 13.02 ? 276 GLY A H 1 ATOM 4103 H HA2 . GLY A 1 268 ? 6.389 15.760 21.987 1.00 13.83 ? 276 GLY A HA2 1 ATOM 4104 H HA3 . GLY A 1 268 ? 5.279 15.542 23.087 1.00 13.83 ? 276 GLY A HA3 1 ATOM 4105 N N . HIS A 1 269 ? 4.975 17.955 23.457 1.00 10.30 ? 277 HIS A N 1 ATOM 4106 C CA . HIS A 1 269 ? 4.729 19.320 23.891 1.00 9.47 ? 277 HIS A CA 1 ATOM 4107 C C . HIS A 1 269 ? 4.887 20.367 22.808 1.00 10.76 ? 277 HIS A C 1 ATOM 4108 O O . HIS A 1 269 ? 4.081 21.298 22.751 1.00 11.78 ? 277 HIS A O 1 ATOM 4109 C CB . HIS A 1 269 ? 5.577 19.643 25.130 1.00 10.52 ? 277 HIS A CB 1 ATOM 4110 C CG . HIS A 1 269 ? 5.318 20.990 25.715 1.00 10.58 ? 277 HIS A CG 1 ATOM 4111 N ND1 . HIS A 1 269 ? 4.102 21.368 26.240 1.00 11.26 ? 277 HIS A ND1 1 ATOM 4112 C CD2 . HIS A 1 269 ? 6.137 22.061 25.820 1.00 11.83 ? 277 HIS A CD2 1 ATOM 4113 C CE1 . HIS A 1 269 ? 4.200 22.610 26.682 1.00 11.86 ? 277 HIS A CE1 1 ATOM 4114 N NE2 . HIS A 1 269 ? 5.431 23.047 26.448 1.00 12.11 ? 277 HIS A NE2 1 ATOM 4115 H H . HIS A 1 269 ? 4.241 17.518 23.364 1.00 12.36 ? 277 HIS A H 1 ATOM 4116 H HA . HIS A 1 269 ? 3.803 19.366 24.177 1.00 11.37 ? 277 HIS A HA 1 ATOM 4117 H HB2 . HIS A 1 269 ? 5.391 18.983 25.816 1.00 12.63 ? 277 HIS A HB2 1 ATOM 4118 H HB3 . HIS A 1 269 ? 6.515 19.604 24.884 1.00 12.63 ? 277 HIS A HB3 1 ATOM 4119 H HD2 . HIS A 1 269 ? 7.028 22.102 25.556 1.00 14.20 ? 277 HIS A HD2 1 ATOM 4120 H HE1 . HIS A 1 269 ? 3.518 23.097 27.085 1.00 14.23 ? 277 HIS A HE1 1 ATOM 4121 H HE2 . HIS A 1 269 ? 5.726 23.834 26.631 1.00 14.54 ? 277 HIS A HE2 1 ATOM 4122 N N . HIS A 1 270 ? 5.863 20.228 21.934 1.00 10.30 ? 278 HIS A N 1 ATOM 4123 C CA . HIS A 1 270 ? 6.086 21.240 20.908 1.00 10.49 ? 278 HIS A CA 1 ATOM 4124 C C . HIS A 1 270 ? 5.074 21.171 19.785 1.00 10.81 ? 278 HIS A C 1 ATOM 4125 O O . HIS A 1 270 ? 4.812 22.187 19.157 1.00 12.69 ? 278 HIS A O 1 ATOM 4126 C CB . HIS A 1 270 ? 7.459 21.090 20.323 1.00 11.01 ? 278 HIS A CB 1 ATOM 4127 C CG . HIS A 1 270 ? 8.543 21.486 21.267 1.00 11.34 ? 278 HIS A CG 1 ATOM 4128 N ND1 . HIS A 1 270 ? 9.867 21.234 21.020 1.00 11.54 ? 278 HIS A ND1 1 ATOM 4129 C CD2 . HIS A 1 270 ? 8.504 22.141 22.453 1.00 12.59 ? 278 HIS A CD2 1 ATOM 4130 C CE1 . HIS A 1 270 ? 10.598 21.714 22.012 1.00 11.71 ? 278 HIS A CE1 1 ATOM 4131 N NE2 . HIS A 1 270 ? 9.800 22.254 22.903 1.00 12.54 ? 278 HIS A NE2 1 ATOM 4132 H H . HIS A 1 270 ? 6.410 19.565 21.908 1.00 12.36 ? 278 HIS A H 1 ATOM 4133 H HA . HIS A 1 270 ? 6.026 22.119 21.313 1.00 12.59 ? 278 HIS A HA 1 ATOM 4134 H HB2 . HIS A 1 270 ? 7.598 20.162 20.080 1.00 13.21 ? 278 HIS A HB2 1 ATOM 4135 H HB3 . HIS A 1 270 ? 7.528 21.652 19.535 1.00 13.21 ? 278 HIS A HB3 1 ATOM 4136 H HD1 . HIS A 1 270 ? 10.176 20.833 20.324 1.00 13.85 ? 278 HIS A HD1 1 ATOM 4137 H HD2 . HIS A 1 270 ? 7.741 22.444 22.890 1.00 15.11 ? 278 HIS A HD2 1 ATOM 4138 H HE1 . HIS A 1 270 ? 11.523 21.657 22.079 1.00 14.06 ? 278 HIS A HE1 1 ATOM 4139 N N . HIS A 1 271 ? 4.586 19.989 19.464 1.00 10.27 ? 279 HIS A N 1 ATOM 4140 C CA . HIS A 1 271 ? 3.690 19.658 18.349 1.00 10.74 ? 279 HIS A CA 1 ATOM 4141 C C . HIS A 1 271 ? 4.425 19.573 17.028 1.00 10.98 ? 279 HIS A C 1 ATOM 4142 O O . HIS A 1 271 ? 3.832 19.149 16.030 1.00 13.25 ? 279 HIS A O 1 ATOM 4143 C CB . HIS A 1 271 ? 2.477 20.592 18.196 1.00 10.90 ? 279 HIS A CB 1 ATOM 4144 C CG . HIS A 1 271 ? 1.672 20.718 19.439 1.00 10.74 ? 279 HIS A CG 1 ATOM 4145 N ND1 . HIS A 1 271 ? 0.583 21.547 19.525 1.00 11.26 ? 279 HIS A ND1 1 ATOM 4146 C CD2 . HIS A 1 271 ? 1.794 20.143 20.661 1.00 10.73 ? 279 HIS A CD2 1 ATOM 4147 C CE1 . HIS A 1 271 ? 0.063 21.473 20.745 1.00 11.61 ? 279 HIS A CE1 1 ATOM 4148 N NE2 . HIS A 1 271 ? 0.779 20.619 21.456 1.00 11.36 ? 279 HIS A NE2 1 ATOM 4149 H H . HIS A 1 271 ? 4.777 19.287 19.923 1.00 12.33 ? 279 HIS A H 1 ATOM 4150 H HA . HIS A 1 271 ? 3.333 18.773 18.521 1.00 12.88 ? 279 HIS A HA 1 ATOM 4151 H HB2 . HIS A 1 271 ? 2.790 21.477 17.952 1.00 13.08 ? 279 HIS A HB2 1 ATOM 4152 H HB3 . HIS A 1 271 ? 1.898 20.243 17.500 1.00 13.08 ? 279 HIS A HB3 1 ATOM 4153 H HD1 . HIS A 1 271 ? 0.283 22.039 18.887 1.00 13.51 ? 279 HIS A HD1 1 ATOM 4154 H HD2 . HIS A 1 271 ? 2.444 19.527 20.914 1.00 12.87 ? 279 HIS A HD2 1 ATOM 4155 H HE1 . HIS A 1 271 ? -0.684 21.938 21.046 1.00 13.93 ? 279 HIS A HE1 1 ATOM 4156 N N . THR A 1 272 ? 5.691 19.967 16.987 1.00 11.89 ? 280 THR A N 1 ATOM 4157 C CA . THR A 1 272 ? 6.547 20.019 15.821 1.00 11.89 ? 280 THR A CA 1 ATOM 4158 C C . THR A 1 272 ? 7.606 18.929 15.924 1.00 12.19 ? 280 THR A C 1 ATOM 4159 O O . THR A 1 272 ? 7.911 18.439 17.007 1.00 13.80 ? 280 THR A O 1 ATOM 4160 C CB . THR A 1 272 ? 7.196 21.407 15.735 1.00 13.75 ? 280 THR A CB 1 ATOM 4161 O OG1 . THR A 1 272 ? 7.748 21.743 17.010 1.00 14.93 ? 280 THR A OG1 1 ATOM 4162 C CG2 . THR A 1 272 ? 6.164 22.452 15.338 1.00 16.41 ? 280 THR A CG2 1 ATOM 4163 H H . THR A 1 272 ? 6.105 20.231 17.693 1.00 14.26 ? 280 THR A H 1 ATOM 4164 H HA . THR A 1 272 ? 6.020 19.870 15.020 1.00 14.27 ? 280 THR A HA 1 ATOM 4165 H HB . THR A 1 272 ? 7.900 21.397 15.068 1.00 16.50 ? 280 THR A HB 1 ATOM 4166 H HG1 . THR A 1 272 ? 8.107 22.501 16.976 1.00 17.92 ? 280 THR A HG1 1 ATOM 4167 H HG21 . THR A 1 272 ? 6.581 23.327 15.286 1.00 19.69 ? 280 THR A HG21 1 ATOM 4168 H HG22 . THR A 1 272 ? 5.784 22.232 14.473 1.00 19.69 ? 280 THR A HG22 1 ATOM 4169 H HG23 . THR A 1 272 ? 5.452 22.482 15.996 1.00 19.69 ? 280 THR A HG23 1 ATOM 4170 N N . ASP A 1 273 ? 8.189 18.586 14.796 1.00 10.61 ? 281 ASP A N 1 ATOM 4171 C CA . ASP A 1 273 ? 9.083 17.431 14.668 1.00 10.92 ? 281 ASP A CA 1 ATOM 4172 C C . ASP A 1 273 ? 10.522 17.910 14.752 1.00 10.10 ? 281 ASP A C 1 ATOM 4173 O O . ASP A 1 273 ? 11.012 18.588 13.844 1.00 11.04 ? 281 ASP A O 1 ATOM 4174 C CB . ASP A 1 273 ? 8.810 16.764 13.324 1.00 11.62 ? 281 ASP A CB 1 ATOM 4175 C CG . ASP A 1 273 ? 9.598 15.508 13.089 1.00 11.79 ? 281 ASP A CG 1 ATOM 4176 O OD1 . ASP A 1 273 ? 10.575 15.263 13.815 1.00 12.09 ? 281 ASP A OD1 1 ATOM 4177 O OD2 . ASP A 1 273 ? 9.250 14.769 12.120 1.00 11.90 ? 281 ASP A OD2 1 ATOM 4178 H H . ASP A 1 273 ? 8.084 19.016 14.059 1.00 12.73 ? 281 ASP A H 1 ATOM 4179 H HA . ASP A 1 273 ? 8.915 16.796 15.381 1.00 13.10 ? 281 ASP A HA 1 ATOM 4180 H HB2 . ASP A 1 273 ? 7.869 16.536 13.276 1.00 13.94 ? 281 ASP A HB2 1 ATOM 4181 H HB3 . ASP A 1 273 ? 9.033 17.389 12.616 1.00 13.94 ? 281 ASP A HB3 1 ATOM 4182 N N . SER A 1 274 ? 11.209 17.575 15.842 1.00 10.50 ? 282 SER A N 1 ATOM 4183 C CA . SER A 1 274 ? 12.624 17.936 15.949 1.00 10.40 ? 282 SER A CA 1 ATOM 4184 C C . SER A 1 274 ? 13.302 16.900 16.826 1.00 10.86 ? 282 SER A C 1 ATOM 4185 O O . SER A 1 274 ? 12.698 15.908 17.224 1.00 10.91 ? 282 SER A O 1 ATOM 4186 C CB . SER A 1 274 ? 12.733 19.381 16.470 1.00 11.06 ? 282 SER A CB 1 ATOM 4187 O OG . SER A 1 274 ? 14.057 19.919 16.356 1.00 11.60 ? 282 SER A OG 1 ATOM 4188 H H . SER A 1 274 ? 10.891 17.149 16.519 1.00 12.61 ? 282 SER A H 1 ATOM 4189 H HA . SER A 1 274 ? 13.030 17.900 15.069 1.00 12.48 ? 282 SER A HA 1 ATOM 4190 H HB2 . SER A 1 274 ? 12.128 19.941 15.958 1.00 13.27 ? 282 SER A HB2 1 ATOM 4191 H HB3 . SER A 1 274 ? 12.474 19.393 17.405 1.00 13.27 ? 282 SER A HB3 1 ATOM 4192 H HG . SER A 1 274 ? 14.297 19.923 15.551 1.00 13.92 ? 282 SER A HG 1 ATOM 4193 N N . PHE A 1 275 ? 14.564 17.136 17.160 1.00 10.71 ? 283 PHE A N 1 ATOM 4194 C CA . PHE A 1 275 ? 15.308 16.227 18.019 1.00 10.97 ? 283 PHE A CA 1 ATOM 4195 C C . PHE A 1 275 ? 16.330 17.032 18.804 1.00 10.38 ? 283 PHE A C 1 ATOM 4196 O O . PHE A 1 275 ? 16.630 18.171 18.445 1.00 11.02 ? 283 PHE A O 1 ATOM 4197 C CB . PHE A 1 275 ? 15.955 15.060 17.242 1.00 11.37 ? 283 PHE A CB 1 ATOM 4198 C CG . PHE A 1 275 ? 17.000 15.462 16.231 1.00 11.42 ? 283 PHE A CG 1 ATOM 4199 C CD1 . PHE A 1 275 ? 16.626 15.946 14.993 1.00 11.90 ? 283 PHE A CD1 1 ATOM 4200 C CD2 . PHE A 1 275 ? 18.357 15.323 16.498 1.00 11.39 ? 283 PHE A CD2 1 ATOM 4201 C CE1 . PHE A 1 275 ? 17.558 16.242 14.042 1.00 13.17 ? 283 PHE A CE1 1 ATOM 4202 C CE2 . PHE A 1 275 ? 19.292 15.648 15.570 1.00 12.37 ? 283 PHE A CE2 1 ATOM 4203 C CZ . PHE A 1 275 ? 18.905 16.108 14.332 1.00 13.19 ? 283 PHE A CZ 1 ATOM 4204 H H . PHE A 1 275 ? 15.014 17.821 16.900 1.00 12.86 ? 283 PHE A H 1 ATOM 4205 H HA . PHE A 1 275 ? 14.692 15.840 18.660 1.00 13.16 ? 283 PHE A HA 1 ATOM 4206 H HB2 . PHE A 1 275 ? 16.380 14.464 17.878 1.00 13.65 ? 283 PHE A HB2 1 ATOM 4207 H HB3 . PHE A 1 275 ? 15.258 14.583 16.766 1.00 13.65 ? 283 PHE A HB3 1 ATOM 4208 H HD1 . PHE A 1 275 ? 15.722 16.020 14.786 1.00 14.28 ? 283 PHE A HD1 1 ATOM 4209 H HD2 . PHE A 1 275 ? 18.629 14.998 17.325 1.00 13.67 ? 283 PHE A HD2 1 ATOM 4210 H HE1 . PHE A 1 275 ? 17.290 16.574 13.215 1.00 15.80 ? 283 PHE A HE1 1 ATOM 4211 H HE2 . PHE A 1 275 ? 20.195 15.550 15.768 1.00 14.85 ? 283 PHE A HE2 1 ATOM 4212 H HZ . PHE A 1 275 ? 19.545 16.340 13.699 1.00 15.83 ? 283 PHE A HZ 1 ATOM 4213 N N . ARG A 1 276 ? 16.847 16.444 19.874 1.00 10.36 ? 284 ARG A N 1 ATOM 4214 C CA . ARG A 1 276 ? 17.813 17.121 20.730 1.00 11.53 ? 284 ARG A CA 1 ATOM 4215 C C . ARG A 1 276 ? 18.995 16.200 20.945 1.00 11.39 ? 284 ARG A C 1 ATOM 4216 O O . ARG A 1 276 ? 18.829 15.046 21.355 1.00 12.58 ? 284 ARG A O 1 ATOM 4217 C CB . ARG A 1 276 ? 17.210 17.492 22.082 1.00 12.11 ? 284 ARG A CB 1 ATOM 4218 C CG . ARG A 1 276 ? 16.016 18.430 21.995 1.00 11.63 ? 284 ARG A CG 1 ATOM 4219 C CD . ARG A 1 276 ? 16.424 19.828 21.547 1.00 11.91 ? 284 ARG A CD 1 ATOM 4220 N NE . ARG A 1 276 ? 15.271 20.717 21.397 1.00 11.42 ? 284 ARG A NE 1 ATOM 4221 C CZ . ARG A 1 276 ? 14.668 21.004 20.249 1.00 11.90 ? 284 ARG A CZ 1 ATOM 4222 N NH1 . ARG A 1 276 ? 15.025 20.400 19.112 1.00 11.88 ? 284 ARG A NH1 1 ATOM 4223 N NH2 . ARG A 1 276 ? 13.669 21.869 20.243 1.00 12.37 ? 284 ARG A NH2 1 ATOM 4224 H H . ARG A 1 276 ? 16.653 15.646 20.130 1.00 12.43 ? 284 ARG A H 1 ATOM 4225 H HA . ARG A 1 276 ? 18.124 17.930 20.295 1.00 13.84 ? 284 ARG A HA 1 ATOM 4226 H HB2 . ARG A 1 276 ? 16.917 16.681 22.525 1.00 14.54 ? 284 ARG A HB2 1 ATOM 4227 H HB3 . ARG A 1 276 ? 17.891 17.930 22.616 1.00 14.54 ? 284 ARG A HB3 1 ATOM 4228 H HG2 . ARG A 1 276 ? 15.380 18.079 21.352 1.00 13.95 ? 284 ARG A HG2 1 ATOM 4229 H HG3 . ARG A 1 276 ? 15.602 18.501 22.870 1.00 13.95 ? 284 ARG A HG3 1 ATOM 4230 H HD2 . ARG A 1 276 ? 17.019 20.213 22.209 1.00 14.30 ? 284 ARG A HD2 1 ATOM 4231 H HD3 . ARG A 1 276 ? 16.873 19.768 20.689 1.00 14.30 ? 284 ARG A HD3 1 ATOM 4232 H HE . ARG A 1 276 ? 14.959 21.083 22.109 1.00 13.70 ? 284 ARG A HE 1 ATOM 4233 H HH11 . ARG A 1 276 ? 15.682 19.845 19.109 1.00 14.26 ? 284 ARG A HH11 1 ATOM 4234 H HH12 . ARG A 1 276 ? 14.615 20.585 18.380 1.00 14.26 ? 284 ARG A HH12 1 ATOM 4235 H HH21 . ARG A 1 276 ? 13.422 22.245 20.976 1.00 14.85 ? 284 ARG A HH21 1 ATOM 4236 H HH22 . ARG A 1 276 ? 13.249 22.036 19.512 1.00 14.85 ? 284 ARG A HH22 1 ATOM 4237 N N . MET A 1 277 ? 20.178 16.719 20.697 1.00 11.56 ? 285 MET A N 1 ATOM 4238 C CA . MET A 1 277 ? 21.435 16.027 20.962 1.00 11.92 ? 285 MET A CA 1 ATOM 4239 C C . MET A 1 277 ? 21.882 16.303 22.389 1.00 12.13 ? 285 MET A C 1 ATOM 4240 O O . MET A 1 277 ? 21.645 17.380 22.933 1.00 14.19 ? 285 MET A O 1 ATOM 4241 C CB . MET A 1 277 ? 22.495 16.492 19.968 1.00 12.76 ? 285 MET A CB 1 ATOM 4242 C CG . MET A 1 277 ? 22.145 16.160 18.501 1.00 13.61 ? 285 MET A CG 1 ATOM 4243 S SD . MET A 1 277 ? 21.964 14.414 18.174 1.00 15.36 ? 285 MET A SD 1 ATOM 4244 C CE . MET A 1 277 ? 23.515 13.753 18.758 1.00 16.98 ? 285 MET A CE 1 ATOM 4245 H H . MET A 1 277 ? 20.290 17.503 20.361 1.00 13.87 ? 285 MET A H 1 ATOM 4246 H HA . MET A 1 277 ? 21.306 15.072 20.845 1.00 14.30 ? 285 MET A HA 1 ATOM 4247 H HB2 . MET A 1 277 ? 22.594 17.454 20.041 1.00 15.32 ? 285 MET A HB2 1 ATOM 4248 H HB3 . MET A 1 277 ? 23.336 16.057 20.179 1.00 15.32 ? 285 MET A HB3 1 ATOM 4249 H HG2 . MET A 1 277 ? 21.306 16.592 18.276 1.00 16.33 ? 285 MET A HG2 1 ATOM 4250 H HG3 . MET A 1 277 ? 22.851 16.497 17.928 1.00 16.33 ? 285 MET A HG3 1 ATOM 4251 H HE1 . MET A 1 277 ? 23.519 12.792 18.623 1.00 20.37 ? 285 MET A HE1 1 ATOM 4252 H HE2 . MET A 1 277 ? 24.240 14.161 18.259 1.00 20.37 ? 285 MET A HE2 1 ATOM 4253 H HE3 . MET A 1 277 ? 23.608 13.955 19.702 1.00 20.37 ? 285 MET A HE3 1 ATOM 4254 N N . PHE A 1 278 ? 22.558 15.322 22.970 1.00 12.03 ? 286 PHE A N 1 ATOM 4255 C CA . PHE A 1 278 ? 23.207 15.454 24.267 1.00 11.46 ? 286 PHE A CA 1 ATOM 4256 C C . PHE A 1 278 ? 24.663 15.069 24.100 1.00 12.11 ? 286 PHE A C 1 ATOM 4257 O O . PHE A 1 278 ? 24.966 14.069 23.431 1.00 12.67 ? 286 PHE A O 1 ATOM 4258 C CB . PHE A 1 278 ? 22.569 14.543 25.289 1.00 12.45 ? 286 PHE A CB 1 ATOM 4259 C CG . PHE A 1 278 ? 21.180 14.950 25.646 1.00 12.20 ? 286 PHE A CG 1 ATOM 4260 C CD1 . PHE A 1 278 ? 20.147 14.642 24.802 1.00 12.58 ? 286 PHE A CD1 1 ATOM 4261 C CD2 . PHE A 1 278 ? 20.909 15.634 26.817 1.00 13.02 ? 286 PHE A CD2 1 ATOM 4262 C CE1 . PHE A 1 278 ? 18.854 15.021 25.114 1.00 13.68 ? 286 PHE A CE1 1 ATOM 4263 C CE2 . PHE A 1 278 ? 19.631 16.020 27.132 1.00 14.13 ? 286 PHE A CE2 1 ATOM 4264 C CZ . PHE A 1 278 ? 18.584 15.707 26.274 1.00 14.23 ? 286 PHE A CZ 1 ATOM 4265 H H . PHE A 1 278 ? 22.658 14.543 22.621 1.00 14.44 ? 286 PHE A H 1 ATOM 4266 H HA . PHE A 1 278 ? 23.153 16.372 24.577 1.00 13.75 ? 286 PHE A HA 1 ATOM 4267 H HB2 . PHE A 1 278 ? 22.534 13.643 24.930 1.00 14.94 ? 286 PHE A HB2 1 ATOM 4268 H HB3 . PHE A 1 278 ? 23.102 14.556 26.099 1.00 14.94 ? 286 PHE A HB3 1 ATOM 4269 H HD1 . PHE A 1 278 ? 20.316 14.182 24.011 1.00 15.10 ? 286 PHE A HD1 1 ATOM 4270 H HD2 . PHE A 1 278 ? 21.607 15.850 27.392 1.00 15.63 ? 286 PHE A HD2 1 ATOM 4271 H HE1 . PHE A 1 278 ? 18.160 14.808 24.533 1.00 16.41 ? 286 PHE A HE1 1 ATOM 4272 H HE2 . PHE A 1 278 ? 19.464 16.479 27.924 1.00 16.95 ? 286 PHE A HE2 1 ATOM 4273 H HZ . PHE A 1 278 ? 17.713 15.956 26.483 1.00 17.07 ? 286 PHE A HZ 1 ATOM 4274 N N . TYR A 1 279 ? 25.552 15.851 24.703 1.00 12.99 ? 287 TYR A N 1 ATOM 4275 C CA . TYR A 1 279 ? 27.000 15.659 24.598 1.00 13.17 ? 287 TYR A CA 1 ATOM 4276 C C . TYR A 1 279 ? 27.609 15.619 25.995 1.00 14.05 ? 287 TYR A C 1 ATOM 4277 O O . TYR A 1 279 ? 27.063 16.198 26.927 1.00 14.85 ? 287 TYR A O 1 ATOM 4278 C CB . TYR A 1 279 ? 27.665 16.831 23.839 1.00 15.51 ? 287 TYR A CB 1 ATOM 4279 C CG . TYR A 1 279 ? 27.160 16.973 22.434 1.00 15.18 ? 287 TYR A CG 1 ATOM 4280 C CD1 . TYR A 1 279 ? 27.740 16.276 21.393 1.00 16.46 ? 287 TYR A CD1 1 ATOM 4281 C CD2 . TYR A 1 279 ? 26.088 17.813 22.148 1.00 14.10 ? 287 TYR A CD2 1 ATOM 4282 C CE1 . TYR A 1 279 ? 27.259 16.383 20.111 1.00 16.33 ? 287 TYR A CE1 1 ATOM 4283 C CE2 . TYR A 1 279 ? 25.600 17.947 20.852 1.00 15.30 ? 287 TYR A CE2 1 ATOM 4284 C CZ . TYR A 1 279 ? 26.190 17.209 19.843 1.00 16.74 ? 287 TYR A CZ 1 ATOM 4285 O OH . TYR A 1 279 ? 25.742 17.282 18.542 1.00 18.77 ? 287 TYR A OH 1 ATOM 4286 H H . TYR A 1 279 ? 25.336 16.521 25.195 1.00 15.59 ? 287 TYR A H 1 ATOM 4287 H HA . TYR A 1 279 ? 27.198 14.828 24.139 1.00 15.80 ? 287 TYR A HA 1 ATOM 4288 H HB2 . TYR A 1 279 ? 27.478 17.659 24.309 1.00 18.61 ? 287 TYR A HB2 1 ATOM 4289 H HB3 . TYR A 1 279 ? 28.622 16.680 23.799 1.00 18.61 ? 287 TYR A HB3 1 ATOM 4290 H HD1 . TYR A 1 279 ? 28.451 15.702 21.568 1.00 19.75 ? 287 TYR A HD1 1 ATOM 4291 H HD2 . TYR A 1 279 ? 25.688 18.292 22.837 1.00 16.92 ? 287 TYR A HD2 1 ATOM 4292 H HE1 . TYR A 1 279 ? 27.655 15.898 19.424 1.00 19.59 ? 287 TYR A HE1 1 ATOM 4293 H HE2 . TYR A 1 279 ? 24.874 18.500 20.673 1.00 18.36 ? 287 TYR A HE2 1 ATOM 4294 H HH . TYR A 1 279 ? 25.091 17.811 18.491 1.00 22.53 ? 287 TYR A HH 1 ATOM 4295 N N . ASP A 1 280 ? 28.745 14.935 26.142 1.00 13.91 ? 288 ASP A N 1 ATOM 4296 C CA . ASP A 1 280 ? 29.481 14.982 27.396 1.00 14.69 ? 288 ASP A CA 1 ATOM 4297 C C . ASP A 1 280 ? 30.561 16.042 27.332 1.00 14.74 ? 288 ASP A C 1 ATOM 4298 O O . ASP A 1 280 ? 30.734 16.742 26.333 1.00 15.30 ? 288 ASP A O 1 ATOM 4299 C CB . ASP A 1 280 ? 29.962 13.597 27.835 1.00 15.96 ? 288 ASP A CB 1 ATOM 4300 C CG . ASP A 1 280 ? 31.085 13.034 26.991 1.00 16.84 ? 288 ASP A CG 1 ATOM 4301 O OD1 . ASP A 1 280 ? 31.749 13.776 26.229 1.00 16.04 ? 288 ASP A OD1 1 ATOM 4302 O OD2 . ASP A 1 280 ? 31.315 11.805 27.139 1.00 19.25 ? 288 ASP A OD2 1 ATOM 4303 H H . ASP A 1 280 ? 29.103 14.442 25.535 1.00 16.70 ? 288 ASP A H 1 ATOM 4304 H HA . ASP A 1 280 ? 28.859 15.276 28.080 1.00 17.63 ? 288 ASP A HA 1 ATOM 4305 H HB2 . ASP A 1 280 ? 30.280 13.653 28.750 1.00 19.15 ? 288 ASP A HB2 1 ATOM 4306 H HB3 . ASP A 1 280 ? 29.216 12.978 27.785 1.00 19.15 ? 288 ASP A HB3 1 ATOM 4307 N N . ASN A 1 281 ? 31.299 16.161 28.431 1.00 15.17 ? 289 ASN A N 1 ATOM 4308 C CA . ASN A 1 281 ? 32.342 17.172 28.548 1.00 15.87 ? 289 ASN A CA 1 ATOM 4309 C C . ASN A 1 281 ? 33.580 16.859 27.729 1.00 15.28 ? 289 ASN A C 1 ATOM 4310 O O . ASN A 1 281 ? 34.547 17.633 27.780 1.00 19.38 ? 289 ASN A O 1 ATOM 4311 C CB . ASN A 1 281 ? 32.700 17.453 30.016 1.00 16.96 ? 289 ASN A CB 1 ATOM 4312 C CG . ASN A 1 281 ? 33.118 16.226 30.765 1.00 16.34 ? 289 ASN A CG 1 ATOM 4313 O OD1 . ASN A 1 281 ? 33.254 15.128 30.210 1.00 18.13 ? 289 ASN A OD1 1 ATOM 4314 N ND2 . ASN A 1 281 ? 33.380 16.415 32.042 1.00 18.15 ? 289 ASN A ND2 1 ATOM 4315 H H . ASN A 1 281 ? 31.214 15.664 29.128 1.00 18.20 ? 289 ASN A H 1 ATOM 4316 H HA . ASN A 1 281 ? 31.982 17.999 28.192 1.00 19.04 ? 289 ASN A HA 1 ATOM 4317 H HB2 . ASN A 1 281 ? 33.435 18.085 30.045 1.00 20.35 ? 289 ASN A HB2 1 ATOM 4318 H HB3 . ASN A 1 281 ? 31.925 17.826 30.464 1.00 20.35 ? 289 ASN A HB3 1 ATOM 4319 H HD21 . ASN A 1 281 ? 33.626 15.754 32.533 1.00 21.78 ? 289 ASN A HD21 1 ATOM 4320 H HD22 . ASN A 1 281 ? 33.305 17.201 32.384 1.00 21.78 ? 289 ASN A HD22 1 ATOM 4321 N N . THR A 1 282 ? 33.604 15.760 26.986 1.00 14.53 ? 290 THR A N 1 ATOM 4322 C CA . THR A 1 282 ? 34.651 15.518 26.001 1.00 15.12 ? 290 THR A CA 1 ATOM 4323 C C . THR A 1 282 ? 34.174 15.838 24.596 1.00 14.94 ? 290 THR A C 1 ATOM 4324 O O . THR A 1 282 ? 34.935 15.665 23.648 1.00 16.89 ? 290 THR A O 1 ATOM 4325 C CB . THR A 1 282 ? 35.157 14.072 26.021 1.00 16.30 ? 290 THR A CB 1 ATOM 4326 O OG1 . THR A 1 282 ? 34.223 13.210 25.376 1.00 16.62 ? 290 THR A OG1 1 ATOM 4327 C CG2 . THR A 1 282 ? 35.460 13.588 27.430 1.00 16.90 ? 290 THR A CG2 1 ATOM 4328 H H . THR A 1 282 ? 33.019 15.132 27.033 1.00 17.44 ? 290 THR A H 1 ATOM 4329 H HA . THR A 1 282 ? 35.404 16.097 26.198 1.00 18.14 ? 290 THR A HA 1 ATOM 4330 H HB . THR A 1 282 ? 35.989 14.038 25.524 1.00 19.56 ? 290 THR A HB 1 ATOM 4331 H HG1 . THR A 1 282 ? 33.483 13.242 25.771 1.00 19.94 ? 290 THR A HG1 1 ATOM 4332 H HG21 . THR A 1 282 ? 35.777 12.672 27.405 1.00 20.28 ? 290 THR A HG21 1 ATOM 4333 H HG22 . THR A 1 282 ? 36.143 14.147 27.832 1.00 20.28 ? 290 THR A HG22 1 ATOM 4334 H HG23 . THR A 1 282 ? 34.658 13.630 27.974 1.00 20.28 ? 290 THR A HG23 1 ATOM 4335 N N . GLY A 1 283 ? 32.921 16.274 24.448 1.00 15.30 ? 291 GLY A N 1 ATOM 4336 C CA . GLY A 1 283 ? 32.334 16.547 23.169 1.00 15.03 ? 291 GLY A CA 1 ATOM 4337 C C . GLY A 1 283 ? 31.701 15.347 22.519 1.00 14.08 ? 291 GLY A C 1 ATOM 4338 O O . GLY A 1 283 ? 31.142 15.483 21.420 1.00 16.55 ? 291 GLY A O 1 ATOM 4339 H H . GLY A 1 283 ? 32.386 16.420 25.106 1.00 18.35 ? 291 GLY A H 1 ATOM 4340 H HA2 . GLY A 1 283 ? 31.652 17.230 23.271 1.00 18.04 ? 291 GLY A HA2 1 ATOM 4341 H HA3 . GLY A 1 283 ? 33.017 16.889 22.572 1.00 18.04 ? 291 GLY A HA3 1 ATOM 4342 N N . ALA A 1 284 ? 31.711 14.204 23.170 1.00 14.87 ? 292 ALA A N 1 ATOM 4343 C CA . ALA A 1 284 ? 31.148 13.012 22.571 1.00 15.46 ? 292 ALA A CA 1 ATOM 4344 C C . ALA A 1 284 ? 29.630 13.107 22.576 1.00 13.96 ? 292 ALA A C 1 ATOM 4345 O O . ALA A 1 284 ? 29.039 13.471 23.607 1.00 13.59 ? 292 ALA A O 1 ATOM 4346 C CB . ALA A 1 284 ? 31.522 11.796 23.393 1.00 15.81 ? 292 ALA A CB 1 ATOM 4347 H H . ALA A 1 284 ? 32.036 14.090 23.958 1.00 17.85 ? 292 ALA A H 1 ATOM 4348 H HA . ALA A 1 284 ? 31.466 12.902 21.661 1.00 18.55 ? 292 ALA A HA 1 ATOM 4349 H HB1 . ALA A 1 284 ? 31.138 11.006 22.980 1.00 18.98 ? 292 ALA A HB1 1 ATOM 4350 H HB2 . ALA A 1 284 ? 32.488 11.719 23.421 1.00 18.98 ? 292 ALA A HB2 1 ATOM 4351 H HB3 . ALA A 1 284 ? 31.172 11.903 24.291 1.00 18.98 ? 292 ALA A HB3 1 ATOM 4352 N N . PRO A 1 285 ? 28.965 12.790 21.468 1.00 14.89 ? 293 PRO A N 1 ATOM 4353 C CA . PRO A 1 285 ? 27.518 12.632 21.510 1.00 13.70 ? 293 PRO A CA 1 ATOM 4354 C C . PRO A 1 285 ? 27.170 11.424 22.362 1.00 13.55 ? 293 PRO A C 1 ATOM 4355 O O . PRO A 1 285 ? 27.720 10.337 22.166 1.00 17.22 ? 293 PRO A O 1 ATOM 4356 C CB . PRO A 1 285 ? 27.149 12.411 20.038 1.00 17.02 ? 293 PRO A CB 1 ATOM 4357 C CG . PRO A 1 285 ? 28.327 12.588 19.254 1.00 19.63 ? 293 PRO A CG 1 ATOM 4358 C CD . PRO A 1 285 ? 29.516 12.517 20.126 1.00 16.45 ? 293 PRO A CD 1 ATOM 4359 H HA . PRO A 1 285 ? 27.084 13.429 21.854 1.00 16.44 ? 293 PRO A HA 1 ATOM 4360 H HB2 . PRO A 1 285 ? 26.807 11.509 19.928 1.00 20.43 ? 293 PRO A HB2 1 ATOM 4361 H HB3 . PRO A 1 285 ? 26.474 13.058 19.779 1.00 20.43 ? 293 PRO A HB3 1 ATOM 4362 H HG2 . PRO A 1 285 ? 28.367 11.887 18.585 1.00 23.56 ? 293 PRO A HG2 1 ATOM 4363 H HG3 . PRO A 1 285 ? 28.288 13.455 18.820 1.00 23.56 ? 293 PRO A HG3 1 ATOM 4364 H HD2 . PRO A 1 285 ? 29.907 11.630 20.094 1.00 19.74 ? 293 PRO A HD2 1 ATOM 4365 H HD3 . PRO A 1 285 ? 30.159 13.200 19.878 1.00 19.74 ? 293 PRO A HD3 1 ATOM 4366 N N . ILE A 1 286 ? 26.250 11.617 23.305 1.00 13.35 ? 294 ILE A N 1 ATOM 4367 C CA . ILE A 1 286 ? 25.922 10.573 24.273 1.00 13.74 ? 294 ILE A CA 1 ATOM 4368 C C . ILE A 1 286 ? 24.455 10.167 24.278 1.00 13.28 ? 294 ILE A C 1 ATOM 4369 O O . ILE A 1 286 ? 24.130 9.130 24.871 1.00 13.99 ? 294 ILE A O 1 ATOM 4370 C CB . ILE A 1 286 ? 26.381 10.941 25.704 1.00 14.91 ? 294 ILE A CB 1 ATOM 4371 C CG1 . ILE A 1 286 ? 25.736 12.275 26.138 1.00 14.13 ? 294 ILE A CG1 1 ATOM 4372 C CG2 . ILE A 1 286 ? 27.911 10.956 25.788 1.00 15.81 ? 294 ILE A CG2 1 ATOM 4373 C CD1 . ILE A 1 286 ? 25.816 12.575 27.649 1.00 15.40 ? 294 ILE A CD1 1 ATOM 4374 H H . ILE A 1 286 ? 25.802 12.344 23.406 1.00 16.02 ? 294 ILE A H 1 ATOM 4375 H HA . ILE A 1 286 ? 26.422 9.781 24.021 1.00 16.49 ? 294 ILE A HA 1 ATOM 4376 H HB . ILE A 1 286 ? 26.060 10.250 26.304 1.00 17.89 ? 294 ILE A HB 1 ATOM 4377 H HG12 . ILE A 1 286 ? 26.183 12.999 25.673 1.00 16.95 ? 294 ILE A HG12 1 ATOM 4378 H HG13 . ILE A 1 286 ? 24.798 12.259 25.892 1.00 16.95 ? 294 ILE A HG13 1 ATOM 4379 H HG21 . ILE A 1 286 ? 28.175 11.188 26.692 1.00 18.97 ? 294 ILE A HG21 1 ATOM 4380 H HG22 . ILE A 1 286 ? 28.248 10.075 25.561 1.00 18.97 ? 294 ILE A HG22 1 ATOM 4381 H HG23 . ILE A 1 286 ? 28.255 11.614 25.163 1.00 18.97 ? 294 ILE A HG23 1 ATOM 4382 H HD11 . ILE A 1 286 ? 25.387 13.427 27.824 1.00 18.48 ? 294 ILE A HD11 1 ATOM 4383 H HD12 . ILE A 1 286 ? 25.360 11.869 28.135 1.00 18.48 ? 294 ILE A HD12 1 ATOM 4384 H HD13 . ILE A 1 286 ? 26.748 12.611 27.915 1.00 18.48 ? 294 ILE A HD13 1 ATOM 4385 N N . ASN A 1 287 ? 23.549 10.934 23.682 1.00 12.21 ? 295 ASN A N 1 ATOM 4386 C CA . ASN A 1 287 ? 22.150 10.551 23.699 1.00 11.98 ? 295 ASN A CA 1 ATOM 4387 C C . ASN A 1 287 ? 21.394 11.432 22.727 1.00 11.38 ? 295 ASN A C 1 ATOM 4388 O O . ASN A 1 287 ? 21.871 12.492 22.333 1.00 12.76 ? 295 ASN A O 1 ATOM 4389 C CB . ASN A 1 287 ? 21.545 10.680 25.105 1.00 13.10 ? 295 ASN A CB 1 ATOM 4390 C CG . ASN A 1 287 ? 20.744 9.468 25.493 1.00 13.56 ? 295 ASN A CG 1 ATOM 4391 O OD1 . ASN A 1 287 ? 19.510 9.514 25.540 1.00 15.97 ? 295 ASN A OD1 1 ATOM 4392 N ND2 . ASN A 1 287 ? 21.405 8.361 25.694 1.00 14.77 ? 295 ASN A ND2 1 ATOM 4393 H H . ASN A 1 287 ? 23.717 11.669 23.268 1.00 14.65 ? 295 ASN A H 1 ATOM 4394 H HA . ASN A 1 287 ? 22.063 9.629 23.410 1.00 14.37 ? 295 ASN A HA 1 ATOM 4395 H HB2 . ASN A 1 287 ? 22.261 10.787 25.751 1.00 15.72 ? 295 ASN A HB2 1 ATOM 4396 H HB3 . ASN A 1 287 ? 20.956 11.451 25.129 1.00 15.72 ? 295 ASN A HB3 1 ATOM 4397 H HD21 . ASN A 1 287 ? 20.986 7.644 25.917 1.00 17.72 ? 295 ASN A HD21 1 ATOM 4398 H HD22 . ASN A 1 287 ? 22.260 8.349 25.603 1.00 17.72 ? 295 ASN A HD22 1 ATOM 4399 N N . VAL A 1 288 ? 20.201 10.987 22.357 1.00 11.52 ? 296 VAL A N 1 ATOM 4400 C CA . VAL A 1 288 ? 19.303 11.772 21.522 1.00 12.15 ? 296 VAL A CA 1 ATOM 4401 C C . VAL A 1 288 ? 17.889 11.660 22.054 1.00 11.22 ? 296 VAL A C 1 ATOM 4402 O O . VAL A 1 288 ? 17.441 10.586 22.485 1.00 13.18 ? 296 VAL A O 1 ATOM 4403 C CB . VAL A 1 288 ? 19.440 11.462 20.013 1.00 16.39 ? 296 VAL A CB 1 ATOM 4404 C CG1 . VAL A 1 288 ? 19.265 10.027 19.717 1.00 19.48 ? 296 VAL A CG1 1 ATOM 4405 C CG2 . VAL A 1 288 ? 18.487 12.328 19.213 1.00 16.47 ? 296 VAL A CG2 1 ATOM 4406 H H . VAL A 1 288 ? 19.882 10.220 22.582 1.00 13.83 ? 296 VAL A H 1 ATOM 4407 H HA . VAL A 1 288 ? 19.557 12.702 21.627 1.00 14.58 ? 296 VAL A HA 1 ATOM 4408 H HB . VAL A 1 288 ? 20.339 11.701 19.738 1.00 19.67 ? 296 VAL A HB 1 ATOM 4409 H HG11 . VAL A 1 288 ? 19.360 9.888 18.762 1.00 23.37 ? 296 VAL A HG11 1 ATOM 4410 H HG12 . VAL A 1 288 ? 19.942 9.522 20.194 1.00 23.37 ? 296 VAL A HG12 1 ATOM 4411 H HG13 . VAL A 1 288 ? 18.381 9.751 20.006 1.00 23.37 ? 296 VAL A HG13 1 ATOM 4412 H HG21 . VAL A 1 288 ? 18.587 12.120 18.271 1.00 19.76 ? 296 VAL A HG21 1 ATOM 4413 H HG22 . VAL A 1 288 ? 17.578 12.144 19.498 1.00 19.76 ? 296 VAL A HG22 1 ATOM 4414 H HG23 . VAL A 1 288 ? 18.700 13.261 19.370 1.00 19.76 ? 296 VAL A HG23 1 ATOM 4415 N N . MET A 1 289 ? 17.188 12.783 22.020 1.00 11.37 ? 297 MET A N 1 ATOM 4416 C CA . MET A 1 289 ? 15.771 12.855 22.327 1.00 11.03 ? 297 MET A CA 1 ATOM 4417 C C . MET A 1 289 ? 15.001 13.165 21.053 1.00 10.26 ? 297 MET A C 1 ATOM 4418 O O . MET A 1 289 ? 15.342 14.101 20.330 1.00 11.53 ? 297 MET A O 1 ATOM 4419 C CB . MET A 1 289 ? 15.531 13.954 23.365 1.00 10.65 ? 297 MET A CB 1 ATOM 4420 C CG . MET A 1 289 ? 14.075 14.219 23.710 1.00 11.97 ? 297 MET A CG 1 ATOM 4421 S SD . MET A 1 289 ? 13.875 15.529 24.938 1.00 13.99 ? 297 MET A SD 1 ATOM 4422 C CE . MET A 1 289 ? 14.633 14.757 26.366 1.00 14.46 ? 297 MET A CE 1 ATOM 4423 H H . MET A 1 289 ? 17.527 13.546 21.812 1.00 13.64 ? 297 MET A H 1 ATOM 4424 H HA . MET A 1 289 ? 15.472 12.009 22.694 1.00 13.23 ? 297 MET A HA 1 ATOM 4425 H HB2 . MET A 1 289 ? 15.984 13.705 24.186 1.00 12.78 ? 297 MET A HB2 1 ATOM 4426 H HB3 . MET A 1 289 ? 15.906 14.783 23.027 1.00 12.78 ? 297 MET A HB3 1 ATOM 4427 H HG2 . MET A 1 289 ? 13.604 14.488 22.906 1.00 14.36 ? 297 MET A HG2 1 ATOM 4428 H HG3 . MET A 1 289 ? 13.683 13.408 24.070 1.00 14.36 ? 297 MET A HG3 1 ATOM 4429 H HE1 . MET A 1 289 ? 14.591 15.371 27.116 1.00 17.35 ? 297 MET A HE1 1 ATOM 4430 H HE2 . MET A 1 289 ? 14.151 13.942 26.577 1.00 17.35 ? 297 MET A HE2 1 ATOM 4431 H HE3 . MET A 1 289 ? 15.558 14.550 26.158 1.00 17.35 ? 297 MET A HE3 1 ATOM 4432 N N . PHE A 1 290 ? 13.927 12.429 20.823 1.00 10.59 ? 298 PHE A N 1 ATOM 4433 C CA . PHE A 1 290 ? 13.074 12.582 19.657 1.00 9.95 ? 298 PHE A CA 1 ATOM 4434 C C . PHE A 1 290 ? 11.786 13.273 20.076 1.00 11.50 ? 298 PHE A C 1 ATOM 4435 O O . PHE A 1 290 ? 11.056 12.761 20.937 1.00 11.74 ? 298 PHE A O 1 ATOM 4436 C CB . PHE A 1 290 ? 12.748 11.206 19.071 1.00 11.71 ? 298 PHE A CB 1 ATOM 4437 C CG . PHE A 1 290 ? 13.953 10.493 18.548 1.00 12.35 ? 298 PHE A CG 1 ATOM 4438 C CD1 . PHE A 1 290 ? 14.413 10.664 17.266 1.00 13.37 ? 298 PHE A CD1 1 ATOM 4439 C CD2 . PHE A 1 290 ? 14.667 9.654 19.392 1.00 13.64 ? 298 PHE A CD2 1 ATOM 4440 C CE1 . PHE A 1 290 ? 15.584 9.985 16.842 1.00 15.09 ? 298 PHE A CE1 1 ATOM 4441 C CE2 . PHE A 1 290 ? 15.804 8.995 18.973 1.00 15.19 ? 298 PHE A CE2 1 ATOM 4442 C CZ . PHE A 1 290 ? 16.250 9.152 17.715 1.00 14.81 ? 298 PHE A CZ 1 ATOM 4443 H H . PHE A 1 290 ? 13.660 11.807 21.354 1.00 12.70 ? 298 PHE A H 1 ATOM 4444 H HA . PHE A 1 290 ? 13.520 13.118 18.983 1.00 11.94 ? 298 PHE A HA 1 ATOM 4445 H HB2 . PHE A 1 290 ? 12.352 10.655 19.764 1.00 14.05 ? 298 PHE A HB2 1 ATOM 4446 H HB3 . PHE A 1 290 ? 12.123 11.316 18.338 1.00 14.05 ? 298 PHE A HB3 1 ATOM 4447 H HD1 . PHE A 1 290 ? 13.962 11.228 16.680 1.00 16.04 ? 298 PHE A HD1 1 ATOM 4448 H HD2 . PHE A 1 290 ? 14.372 9.536 20.267 1.00 16.37 ? 298 PHE A HD2 1 ATOM 4449 H HE1 . PHE A 1 290 ? 15.893 10.090 15.971 1.00 18.11 ? 298 PHE A HE1 1 ATOM 4450 H HE2 . PHE A 1 290 ? 16.257 8.433 19.559 1.00 18.23 ? 298 PHE A HE2 1 ATOM 4451 H HZ . PHE A 1 290 ? 17.014 8.702 17.434 1.00 17.77 ? 298 PHE A HZ 1 ATOM 4452 N N . LEU A 1 291 ? 11.548 14.457 19.511 1.00 10.10 ? 299 LEU A N 1 ATOM 4453 C CA . LEU A 1 291 ? 10.353 15.246 19.779 1.00 9.88 ? 299 LEU A CA 1 ATOM 4454 C C . LEU A 1 291 ? 9.339 14.994 18.671 1.00 11.08 ? 299 LEU A C 1 ATOM 4455 O O . LEU A 1 291 ? 9.537 15.406 17.511 1.00 11.61 ? 299 LEU A O 1 ATOM 4456 C CB . LEU A 1 291 ? 10.701 16.728 19.866 1.00 10.77 ? 299 LEU A CB 1 ATOM 4457 C CG . LEU A 1 291 ? 11.758 17.038 20.928 1.00 11.57 ? 299 LEU A CG 1 ATOM 4458 C CD1 . LEU A 1 291 ? 12.213 18.470 20.861 1.00 14.23 ? 299 LEU A CD1 1 ATOM 4459 C CD2 . LEU A 1 291 ? 11.320 16.677 22.310 1.00 17.15 ? 299 LEU A CD2 1 ATOM 4460 H H . LEU A 1 291 ? 12.083 14.833 18.952 1.00 12.12 ? 299 LEU A H 1 ATOM 4461 H HA . LEU A 1 291 ? 9.963 14.969 20.623 1.00 11.85 ? 299 LEU A HA 1 ATOM 4462 H HB2 . LEU A 1 291 ? 11.045 17.021 19.008 1.00 12.93 ? 299 LEU A HB2 1 ATOM 4463 H HB3 . LEU A 1 291 ? 9.899 17.226 20.088 1.00 12.93 ? 299 LEU A HB3 1 ATOM 4464 H HG . LEU A 1 291 ? 12.535 16.492 20.734 1.00 13.88 ? 299 LEU A HG 1 ATOM 4465 H HD11 . LEU A 1 291 ? 12.880 18.621 21.549 1.00 17.08 ? 299 LEU A HD11 1 ATOM 4466 H HD12 . LEU A 1 291 ? 12.596 18.639 19.986 1.00 17.08 ? 299 LEU A HD12 1 ATOM 4467 H HD13 . LEU A 1 291 ? 11.450 19.051 21.006 1.00 17.08 ? 299 LEU A HD13 1 ATOM 4468 H HD21 . LEU A 1 291 ? 12.030 16.897 22.933 1.00 20.58 ? 299 LEU A HD21 1 ATOM 4469 H HD22 . LEU A 1 291 ? 10.520 17.180 22.528 1.00 20.58 ? 299 LEU A HD22 1 ATOM 4470 H HD23 . LEU A 1 291 ? 11.134 15.726 22.343 1.00 20.58 ? 299 LEU A HD23 1 ATOM 4471 N N . THR A 1 292 ? 8.304 14.276 19.014 1.00 10.41 ? 300 THR A N 1 ATOM 4472 C CA . THR A 1 292 ? 7.359 13.834 18.018 1.00 10.99 ? 300 THR A CA 1 ATOM 4473 C C . THR A 1 292 ? 6.292 14.892 17.803 1.00 11.26 ? 300 THR A C 1 ATOM 4474 O O . THR A 1 292 ? 5.856 15.551 18.756 1.00 11.99 ? 300 THR A O 1 ATOM 4475 C CB . THR A 1 292 ? 6.713 12.499 18.435 1.00 12.30 ? 300 THR A CB 1 ATOM 4476 O OG1 . THR A 1 292 ? 6.321 11.765 17.260 1.00 15.70 ? 300 THR A OG1 1 ATOM 4477 C CG2 . THR A 1 292 ? 5.483 12.671 19.387 1.00 13.15 ? 300 THR A CG2 1 ATOM 4478 H H . THR A 1 292 ? 8.122 14.028 19.817 1.00 12.49 ? 300 THR A H 1 ATOM 4479 H HA . THR A 1 292 ? 7.823 13.696 17.177 1.00 13.19 ? 300 THR A HA 1 ATOM 4480 H HB . THR A 1 292 ? 7.376 11.977 18.913 1.00 14.76 ? 300 THR A HB 1 ATOM 4481 H HG1 . THR A 1 292 ? 5.767 12.212 16.814 1.00 18.84 ? 300 THR A HG1 1 ATOM 4482 H HG21 . THR A 1 292 ? 5.117 11.803 19.616 1.00 15.78 ? 300 THR A HG21 1 ATOM 4483 H HG22 . THR A 1 292 ? 5.755 13.124 20.201 1.00 15.78 ? 300 THR A HG22 1 ATOM 4484 H HG23 . THR A 1 292 ? 4.796 13.197 18.949 1.00 15.78 ? 300 THR A HG23 1 ATOM 4485 N N . PRO A 1 293 ? 5.786 15.040 16.586 1.00 11.70 ? 301 PRO A N 1 ATOM 4486 C CA . PRO A 1 293 ? 4.755 16.053 16.347 1.00 11.70 ? 301 PRO A CA 1 ATOM 4487 C C . PRO A 1 293 ? 3.417 15.651 16.954 1.00 11.82 ? 301 PRO A C 1 ATOM 4488 O O . PRO A 1 293 ? 3.198 14.528 17.409 1.00 13.35 ? 301 PRO A O 1 ATOM 4489 C CB . PRO A 1 293 ? 4.681 16.121 14.826 1.00 14.31 ? 301 PRO A CB 1 ATOM 4490 C CG . PRO A 1 293 ? 5.125 14.802 14.363 1.00 13.93 ? 301 PRO A CG 1 ATOM 4491 C CD . PRO A 1 293 ? 6.199 14.373 15.342 1.00 12.58 ? 301 PRO A CD 1 ATOM 4492 H HA . PRO A 1 293 ? 5.031 16.913 16.700 1.00 14.04 ? 301 PRO A HA 1 ATOM 4493 H HB2 . PRO A 1 293 ? 3.767 16.292 14.551 1.00 17.17 ? 301 PRO A HB2 1 ATOM 4494 H HB3 . PRO A 1 293 ? 5.274 16.817 14.501 1.00 17.17 ? 301 PRO A HB3 1 ATOM 4495 H HG2 . PRO A 1 293 ? 4.379 14.182 14.380 1.00 16.72 ? 301 PRO A HG2 1 ATOM 4496 H HG3 . PRO A 1 293 ? 5.488 14.876 13.466 1.00 16.72 ? 301 PRO A HG3 1 ATOM 4497 H HD2 . PRO A 1 293 ? 6.193 13.409 15.454 1.00 15.09 ? 301 PRO A HD2 1 ATOM 4498 H HD3 . PRO A 1 293 ? 7.068 14.695 15.056 1.00 15.09 ? 301 PRO A HD3 1 ATOM 4499 N N . GLY A 1 294 ? 2.505 16.622 16.980 1.00 11.73 ? 302 GLY A N 1 ATOM 4500 C CA . GLY A 1 294 ? 1.191 16.381 17.546 1.00 12.46 ? 302 GLY A CA 1 ATOM 4501 C C . GLY A 1 294 ? 0.156 15.962 16.533 1.00 10.90 ? 302 GLY A C 1 ATOM 4502 O O . GLY A 1 294 ? 0.300 16.200 15.334 1.00 11.58 ? 302 GLY A O 1 ATOM 4503 H H . GLY A 1 294 ? 2.625 17.419 16.680 1.00 14.07 ? 302 GLY A H 1 ATOM 4504 H HA2 . GLY A 1 294 ? 1.257 15.683 18.217 1.00 14.95 ? 302 GLY A HA2 1 ATOM 4505 H HA3 . GLY A 1 294 ? 0.878 17.190 17.980 1.00 14.95 ? 302 GLY A HA3 1 ATOM 4506 N N . VAL A 1 295 ? -0.890 15.311 17.038 1.00 10.84 ? 303 VAL A N 1 ATOM 4507 C CA . VAL A 1 295 ? -2.088 15.093 16.225 1.00 10.51 ? 303 VAL A CA 1 ATOM 4508 C C . VAL A 1 295 ? -2.833 16.403 16.043 1.00 10.30 ? 303 VAL A C 1 ATOM 4509 O O . VAL A 1 295 ? -3.362 16.683 14.957 1.00 11.81 ? 303 VAL A O 1 ATOM 4510 C CB . VAL A 1 295 ? -2.974 13.996 16.834 1.00 11.33 ? 303 VAL A CB 1 ATOM 4511 C CG1 . VAL A 1 295 ? -4.338 13.948 16.145 1.00 12.52 ? 303 VAL A CG1 1 ATOM 4512 C CG2 . VAL A 1 295 ? -2.298 12.642 16.725 1.00 13.06 ? 303 VAL A CG2 1 ATOM 4513 H H . VAL A 1 295 ? -0.933 14.989 17.834 1.00 13.01 ? 303 VAL A H 1 ATOM 4514 H HA . VAL A 1 295 ? -1.812 14.790 15.346 1.00 12.61 ? 303 VAL A HA 1 ATOM 4515 H HB . VAL A 1 295 ? -3.117 14.188 17.774 1.00 13.59 ? 303 VAL A HB 1 ATOM 4516 H HG11 . VAL A 1 295 ? -4.872 13.248 16.551 1.00 15.02 ? 303 VAL A HG11 1 ATOM 4517 H HG12 . VAL A 1 295 ? -4.777 14.806 16.255 1.00 15.02 ? 303 VAL A HG12 1 ATOM 4518 H HG13 . VAL A 1 295 ? -4.208 13.761 15.202 1.00 15.02 ? 303 VAL A HG13 1 ATOM 4519 H HG21 . VAL A 1 295 ? -2.876 11.969 17.116 1.00 15.67 ? 303 VAL A HG21 1 ATOM 4520 H HG22 . VAL A 1 295 ? -2.141 12.442 15.789 1.00 15.67 ? 303 VAL A HG22 1 ATOM 4521 H HG23 . VAL A 1 295 ? -1.454 12.672 17.203 1.00 15.67 ? 303 VAL A HG23 1 ATOM 4522 N N . THR A 1 296 ? -2.910 17.242 17.080 1.00 10.33 ? 304 THR A N 1 ATOM 4523 C CA . THR A 1 296 ? -3.586 18.515 16.913 1.00 11.00 ? 304 THR A CA 1 ATOM 4524 C C . THR A 1 296 ? -2.832 19.376 15.904 1.00 10.34 ? 304 THR A C 1 ATOM 4525 O O . THR A 1 296 ? -1.587 19.402 15.911 1.00 11.32 ? 304 THR A O 1 ATOM 4526 C CB . THR A 1 296 ? -3.736 19.272 18.225 1.00 11.26 ? 304 THR A CB 1 ATOM 4527 O OG1 . THR A 1 296 ? -4.658 20.336 17.999 1.00 13.02 ? 304 THR A OG1 1 ATOM 4528 C CG2 . THR A 1 296 ? -2.434 19.840 18.749 1.00 11.64 ? 304 THR A CG2 1 ATOM 4529 H H . THR A 1 296 ? -2.589 17.097 17.865 1.00 12.39 ? 304 THR A H 1 ATOM 4530 H HA . THR A 1 296 ? -4.475 18.354 16.561 1.00 13.20 ? 304 THR A HA 1 ATOM 4531 H HB . THR A 1 296 ? -4.098 18.674 18.898 1.00 13.51 ? 304 THR A HB 1 ATOM 4532 H HG1 . THR A 1 296 ? -4.766 20.778 18.705 1.00 15.62 ? 304 THR A HG1 1 ATOM 4533 H HG21 . THR A 1 296 ? -2.589 20.309 19.584 1.00 13.97 ? 304 THR A HG21 1 ATOM 4534 H HG22 . THR A 1 296 ? -1.798 19.124 18.904 1.00 13.97 ? 304 THR A HG22 1 ATOM 4535 H HG23 . THR A 1 296 ? -2.059 20.460 18.104 1.00 13.97 ? 304 THR A HG23 1 ATOM 4536 N N . PRO A 1 297 ? -3.539 20.115 15.042 1.00 10.70 ? 305 PRO A N 1 ATOM 4537 C CA . PRO A 1 297 ? -2.891 21.024 14.088 1.00 10.69 ? 305 PRO A CA 1 ATOM 4538 C C . PRO A 1 297 ? -2.748 22.453 14.588 1.00 11.41 ? 305 PRO A C 1 ATOM 4539 O O . PRO A 1 297 ? -2.113 23.274 13.922 1.00 12.71 ? 305 PRO A O 1 ATOM 4540 C CB . PRO A 1 297 ? -3.847 20.961 12.888 1.00 11.45 ? 305 PRO A CB 1 ATOM 4541 C CG . PRO A 1 297 ? -5.204 20.843 13.549 1.00 11.58 ? 305 PRO A CG 1 ATOM 4542 C CD . PRO A 1 297 ? -4.969 19.921 14.730 1.00 11.05 ? 305 PRO A CD 1 ATOM 4543 H HA . PRO A 1 297 ? -2.022 20.682 13.828 1.00 12.83 ? 305 PRO A HA 1 ATOM 4544 H HB2 . PRO A 1 297 ? -3.781 21.776 12.365 1.00 13.74 ? 305 PRO A HB2 1 ATOM 4545 H HB3 . PRO A 1 297 ? -3.652 20.180 12.347 1.00 13.74 ? 305 PRO A HB3 1 ATOM 4546 H HG2 . PRO A 1 297 ? -5.502 21.717 13.848 1.00 13.89 ? 305 PRO A HG2 1 ATOM 4547 H HG3 . PRO A 1 297 ? -5.840 20.454 12.929 1.00 13.89 ? 305 PRO A HG3 1 ATOM 4548 H HD2 . PRO A 1 297 ? -5.518 20.189 15.483 1.00 13.26 ? 305 PRO A HD2 1 ATOM 4549 H HD3 . PRO A 1 297 ? -5.137 18.999 14.478 1.00 13.26 ? 305 PRO A HD3 1 ATOM 4550 N N . TRP A 1 298 ? -3.351 22.734 15.733 1.00 10.99 ? 306 TRP A N 1 ATOM 4551 C CA . TRP A 1 298 ? -3.610 24.062 16.301 1.00 12.09 ? 306 TRP A CA 1 ATOM 4552 C C . TRP A 1 298 ? -2.465 25.048 16.114 1.00 11.08 ? 306 TRP A C 1 ATOM 4553 O O . TRP A 1 298 ? -1.332 24.820 16.548 1.00 12.41 ? 306 TRP A O 1 ATOM 4554 C CB . TRP A 1 298 ? -3.855 23.840 17.791 1.00 12.08 ? 306 TRP A CB 1 ATOM 4555 C CG . TRP A 1 298 ? -4.086 25.028 18.648 1.00 12.65 ? 306 TRP A CG 1 ATOM 4556 C CD1 . TRP A 1 298 ? -5.220 25.739 18.763 1.00 13.43 ? 306 TRP A CD1 1 ATOM 4557 C CD2 . TRP A 1 298 ? -3.167 25.590 19.573 1.00 13.06 ? 306 TRP A CD2 1 ATOM 4558 N NE1 . TRP A 1 298 ? -5.068 26.752 19.679 1.00 14.71 ? 306 TRP A NE1 1 ATOM 4559 C CE2 . TRP A 1 298 ? -3.808 26.675 20.195 1.00 14.10 ? 306 TRP A CE2 1 ATOM 4560 C CE3 . TRP A 1 298 ? -1.857 25.282 19.933 1.00 14.25 ? 306 TRP A CE3 1 ATOM 4561 C CZ2 . TRP A 1 298 ? -3.192 27.452 21.172 1.00 15.48 ? 306 TRP A CZ2 1 ATOM 4562 C CZ3 . TRP A 1 298 ? -1.249 26.048 20.903 1.00 15.22 ? 306 TRP A CZ3 1 ATOM 4563 C CH2 . TRP A 1 298 ? -1.912 27.130 21.504 1.00 15.18 ? 306 TRP A CH2 1 ATOM 4564 H H . TRP A 1 298 ? -3.647 22.113 16.249 1.00 13.18 ? 306 TRP A H 1 ATOM 4565 H HA . TRP A 1 298 ? -4.412 24.437 15.905 1.00 14.51 ? 306 TRP A HA 1 ATOM 4566 H HB2 . TRP A 1 298 ? -4.636 23.272 17.883 1.00 14.50 ? 306 TRP A HB2 1 ATOM 4567 H HB3 . TRP A 1 298 ? -3.084 23.377 18.154 1.00 14.50 ? 306 TRP A HB3 1 ATOM 4568 H HD1 . TRP A 1 298 ? -5.989 25.590 18.262 1.00 16.12 ? 306 TRP A HD1 1 ATOM 4569 H HE1 . TRP A 1 298 ? -5.667 27.330 19.895 1.00 17.65 ? 306 TRP A HE1 1 ATOM 4570 H HE3 . TRP A 1 298 ? -1.412 24.565 19.543 1.00 17.10 ? 306 TRP A HE3 1 ATOM 4571 H HZ2 . TRP A 1 298 ? -3.631 28.168 21.571 1.00 18.57 ? 306 TRP A HZ2 1 ATOM 4572 H HZ3 . TRP A 1 298 ? -0.370 25.862 21.145 1.00 18.26 ? 306 TRP A HZ3 1 ATOM 4573 H HH2 . TRP A 1 298 ? -1.467 27.638 22.143 1.00 18.21 ? 306 TRP A HH2 1 ATOM 4574 N N . LYS A 1 299 ? -2.791 26.185 15.523 1.00 11.83 ? 307 LYS A N 1 ATOM 4575 C CA . LYS A 1 299 ? -1.824 27.249 15.316 1.00 12.93 ? 307 LYS A CA 1 ATOM 4576 C C . LYS A 1 299 ? -1.475 27.890 16.650 1.00 13.15 ? 307 LYS A C 1 ATOM 4577 O O . LYS A 1 299 ? -2.331 28.476 17.298 1.00 14.55 ? 307 LYS A O 1 ATOM 4578 C CB . LYS A 1 299 ? -2.436 28.289 14.382 1.00 14.05 ? 307 LYS A CB 1 ATOM 4579 C CG . LYS A 1 299 ? -1.441 29.365 13.964 1.00 16.60 ? 307 LYS A CG 1 ATOM 4580 C CD . LYS A 1 299 ? -2.048 30.325 12.937 1.00 20.94 ? 307 LYS A CD 1 ATOM 4581 C CE . LYS A 1 299 ? -2.293 29.632 11.556 1.00 27.52 ? 307 LYS A CE 1 ATOM 4582 N NZ . LYS A 1 299 ? -2.783 30.531 10.438 1.00 32.81 ? 307 LYS A NZ 1 ATOM 4583 H H . LYS A 1 299 ? -3.578 26.368 15.229 1.00 14.20 ? 307 LYS A H 1 ATOM 4584 H HA . LYS A 1 299 ? -1.017 26.894 14.912 1.00 15.51 ? 307 LYS A HA 1 ATOM 4585 H HB2 . LYS A 1 299 ? -2.752 27.846 13.579 1.00 16.86 ? 307 LYS A HB2 1 ATOM 4586 H HB3 . LYS A 1 299 ? -3.175 28.724 14.834 1.00 16.86 ? 307 LYS A HB3 1 ATOM 4587 H HG2 . LYS A 1 299 ? -1.180 29.879 14.744 1.00 19.92 ? 307 LYS A HG2 1 ATOM 4588 H HG3 . LYS A 1 299 ? -0.664 28.944 13.564 1.00 19.92 ? 307 LYS A HG3 1 ATOM 4589 H HD2 . LYS A 1 299 ? -2.901 30.648 13.269 1.00 25.13 ? 307 LYS A HD2 1 ATOM 4590 H HD3 . LYS A 1 299 ? -1.441 31.068 12.799 1.00 25.13 ? 307 LYS A HD3 1 ATOM 4591 H HE2 . LYS A 1 299 ? -1.459 29.233 11.263 1.00 33.02 ? 307 LYS A HE2 1 ATOM 4592 H HE3 . LYS A 1 299 ? -2.957 28.935 11.679 1.00 33.02 ? 307 LYS A HE3 1 ATOM 4593 H HZ1 . LYS A 1 299 ? -2.895 30.056 9.693 1.00 39.38 ? 307 LYS A HZ1 1 ATOM 4594 H HZ2 . LYS A 1 299 ? -3.560 30.902 10.664 1.00 39.38 ? 307 LYS A HZ2 1 ATOM 4595 H HZ3 . LYS A 1 299 ? -2.189 31.175 10.284 1.00 39.38 ? 307 LYS A HZ3 1 ATOM 4596 N N . THR A 1 300 ? -0.227 27.768 17.072 1.00 12.74 ? 308 THR A N 1 ATOM 4597 C CA . THR A 1 300 ? 0.120 28.188 18.414 1.00 13.11 ? 308 THR A CA 1 ATOM 4598 C C . THR A 1 300 ? -0.077 29.686 18.604 1.00 13.28 ? 308 THR A C 1 ATOM 4599 O O . THR A 1 300 ? 0.167 30.497 17.720 1.00 14.27 ? 308 THR A O 1 ATOM 4600 C CB . THR A 1 300 ? 1.542 27.777 18.781 1.00 13.84 ? 308 THR A CB 1 ATOM 4601 O OG1 . THR A 1 300 ? 1.776 28.205 20.124 1.00 15.59 ? 308 THR A OG1 1 ATOM 4602 C CG2 . THR A 1 300 ? 2.582 28.401 17.905 1.00 15.62 ? 308 THR A CG2 1 ATOM 4603 H H . THR A 1 300 ? 0.425 27.452 16.610 1.00 15.29 ? 308 THR A H 1 ATOM 4604 H HA . THR A 1 300 ? -0.477 27.740 19.034 1.00 15.73 ? 308 THR A HA 1 ATOM 4605 H HB . THR A 1 300 ? 1.628 26.812 18.727 1.00 16.61 ? 308 THR A HB 1 ATOM 4606 H HG1 . THR A 1 300 ? 1.224 27.840 20.642 1.00 18.70 ? 308 THR A HG1 1 ATOM 4607 H HG21 . THR A 1 300 ? 3.466 28.108 18.179 1.00 18.75 ? 308 THR A HG21 1 ATOM 4608 H HG22 . THR A 1 300 ? 2.437 28.141 16.982 1.00 18.75 ? 308 THR A HG22 1 ATOM 4609 H HG23 . THR A 1 300 ? 2.535 29.367 17.972 1.00 18.75 ? 308 THR A HG23 1 ATOM 4610 N N . THR A 1 301 ? -0.474 30.049 19.814 1.00 13.69 ? 309 THR A N 1 ATOM 4611 C CA . THR A 1 301 ? -0.595 31.435 20.234 1.00 15.24 ? 309 THR A CA 1 ATOM 4612 C C . THR A 1 301 ? 0.662 31.936 20.937 1.00 16.50 ? 309 THR A C 1 ATOM 4613 O O . THR A 1 301 ? 0.661 33.059 21.434 1.00 18.24 ? 309 THR A O 1 ATOM 4614 C CB . THR A 1 301 ? -1.770 31.557 21.193 1.00 17.96 ? 309 THR A CB 1 ATOM 4615 O OG1 . THR A 1 301 ? -1.570 30.641 22.270 1.00 19.99 ? 309 THR A OG1 1 ATOM 4616 C CG2 . THR A 1 301 ? -3.090 31.256 20.501 1.00 19.55 ? 309 THR A CG2 1 ATOM 4617 H H . THR A 1 301 ? -0.687 29.488 20.431 1.00 16.42 ? 309 THR A H 1 ATOM 4618 H HA . THR A 1 301 ? -0.765 31.997 19.462 1.00 18.28 ? 309 THR A HA 1 ATOM 4619 H HB . THR A 1 301 ? -1.808 32.461 21.543 1.00 21.56 ? 309 THR A HB 1 ATOM 4620 H HG1 . THR A 1 301 ? -2.209 30.692 22.813 1.00 23.99 ? 309 THR A HG1 1 ATOM 4621 H HG21 . THR A 1 301 ? -3.822 31.340 21.132 1.00 23.46 ? 309 THR A HG21 1 ATOM 4622 H HG22 . THR A 1 301 ? -3.231 31.879 19.771 1.00 23.46 ? 309 THR A HG22 1 ATOM 4623 H HG23 . THR A 1 301 ? -3.081 30.353 20.148 1.00 23.46 ? 309 THR A HG23 1 ATOM 4624 N N . LEU A 1 302 ? 1.723 31.141 20.987 1.00 15.58 ? 310 LEU A N 1 ATOM 4625 C CA . LEU A 1 302 ? 2.941 31.577 21.653 1.00 15.81 ? 310 LEU A CA 1 ATOM 4626 C C . LEU A 1 302 ? 3.425 32.863 20.999 1.00 17.17 ? 310 LEU A C 1 ATOM 4627 O O . LEU A 1 302 ? 3.592 32.904 19.768 1.00 16.30 ? 310 LEU A O 1 ATOM 4628 C CB . LEU A 1 302 ? 4.024 30.505 21.575 1.00 17.12 ? 310 LEU A CB 1 ATOM 4629 C CG . LEU A 1 302 ? 5.268 30.804 22.401 1.00 19.04 ? 310 LEU A CG 1 ATOM 4630 C CD1 . LEU A 1 302 ? 4.990 30.749 23.899 1.00 22.63 ? 310 LEU A CD1 1 ATOM 4631 C CD2 . LEU A 1 302 ? 6.376 29.843 22.019 1.00 19.49 ? 310 LEU A CD2 1 ATOM 4632 H H . LEU A 1 302 ? 1.764 30.352 20.647 1.00 18.69 ? 310 LEU A H 1 ATOM 4633 H HA . LEU A 1 302 ? 2.753 31.758 22.587 1.00 18.97 ? 310 LEU A HA 1 ATOM 4634 H HB2 . LEU A 1 302 ? 3.655 29.666 21.892 1.00 20.54 ? 310 LEU A HB2 1 ATOM 4635 H HB3 . LEU A 1 302 ? 4.301 30.410 20.650 1.00 20.54 ? 310 LEU A HB3 1 ATOM 4636 H HG . LEU A 1 302 ? 5.572 31.701 22.191 1.00 22.85 ? 310 LEU A HG 1 ATOM 4637 H HD11 . LEU A 1 302 ? 5.809 30.945 24.379 1.00 27.16 ? 310 LEU A HD11 1 ATOM 4638 H HD12 . LEU A 1 302 ? 4.311 31.406 24.118 1.00 27.16 ? 310 LEU A HD12 1 ATOM 4639 H HD13 . LEU A 1 302 ? 4.676 29.860 24.129 1.00 27.16 ? 310 LEU A HD13 1 ATOM 4640 H HD21 . LEU A 1 302 ? 7.163 30.041 22.550 1.00 23.38 ? 310 LEU A HD21 1 ATOM 4641 H HD22 . LEU A 1 302 ? 6.079 28.936 22.192 1.00 23.38 ? 310 LEU A HD22 1 ATOM 4642 H HD23 . LEU A 1 302 ? 6.576 29.952 21.076 1.00 23.38 ? 310 LEU A HD23 1 ATOM 4643 N N . PRO A 1 303 ? 3.645 33.929 21.765 1.00 19.89 ? 311 PRO A N 1 ATOM 4644 C CA . PRO A 1 303 ? 3.990 35.207 21.138 1.00 21.27 ? 311 PRO A CA 1 ATOM 4645 C C . PRO A 1 303 ? 5.252 35.089 20.304 1.00 21.82 ? 311 PRO A C 1 ATOM 4646 O O . PRO A 1 303 ? 6.240 34.479 20.717 1.00 24.09 ? 311 PRO A O 1 ATOM 4647 C CB . PRO A 1 303 ? 4.191 36.145 22.330 1.00 25.25 ? 311 PRO A CB 1 ATOM 4648 C CG . PRO A 1 303 ? 3.280 35.587 23.365 1.00 26.82 ? 311 PRO A CG 1 ATOM 4649 C CD . PRO A 1 303 ? 3.402 34.097 23.209 1.00 23.29 ? 311 PRO A CD 1 ATOM 4650 H HA . PRO A 1 303 ? 3.259 35.529 20.587 1.00 25.52 ? 311 PRO A HA 1 ATOM 4651 H HB2 . PRO A 1 303 ? 5.114 36.113 22.626 1.00 30.31 ? 311 PRO A HB2 1 ATOM 4652 H HB3 . PRO A 1 303 ? 3.932 37.048 22.089 1.00 30.31 ? 311 PRO A HB3 1 ATOM 4653 H HG2 . PRO A 1 303 ? 3.573 35.866 24.247 1.00 32.18 ? 311 PRO A HG2 1 ATOM 4654 H HG3 . PRO A 1 303 ? 2.371 35.878 23.195 1.00 32.18 ? 311 PRO A HG3 1 ATOM 4655 H HD2 . PRO A 1 303 ? 4.155 33.764 23.721 1.00 27.95 ? 311 PRO A HD2 1 ATOM 4656 H HD3 . PRO A 1 303 ? 2.574 33.661 23.466 1.00 27.95 ? 311 PRO A HD3 1 ATOM 4657 N N . GLY A 1 304 ? 5.216 35.702 19.124 1.00 22.94 ? 312 GLY A N 1 ATOM 4658 C CA . GLY A 1 304 ? 6.359 35.730 18.248 1.00 25.97 ? 312 GLY A CA 1 ATOM 4659 C C . GLY A 1 304 ? 6.426 34.608 17.235 1.00 25.56 ? 312 GLY A C 1 ATOM 4660 O O . GLY A 1 304 ? 7.234 34.685 16.308 1.00 29.65 ? 312 GLY A O 1 ATOM 4661 H H . GLY A 1 304 ? 4.526 36.111 18.813 1.00 27.52 ? 312 GLY A H 1 ATOM 4662 H HA2 . GLY A 1 304 ? 6.360 36.570 17.762 1.00 31.16 ? 312 GLY A HA2 1 ATOM 4663 H HA3 . GLY A 1 304 ? 7.166 35.695 18.785 1.00 31.16 ? 312 GLY A HA3 1 ATOM 4664 N N . VAL A 1 305 ? 5.624 33.560 17.371 1.00 21.17 ? 313 VAL A N 1 ATOM 4665 C CA . VAL A 1 305 ? 5.630 32.480 16.393 1.00 17.98 ? 313 VAL A CA 1 ATOM 4666 C C . VAL A 1 305 ? 4.613 32.816 15.310 1.00 18.39 ? 313 VAL A C 1 ATOM 4667 O O . VAL A 1 305 ? 3.426 32.964 15.603 1.00 19.25 ? 313 VAL A O 1 ATOM 4668 C CB . VAL A 1 305 ? 5.300 31.137 17.056 1.00 17.48 ? 313 VAL A CB 1 ATOM 4669 C CG1 . VAL A 1 305 ? 5.287 30.029 16.020 1.00 18.27 ? 313 VAL A CG1 1 ATOM 4670 C CG2 . VAL A 1 305 ? 6.289 30.818 18.157 1.00 18.22 ? 313 VAL A CG2 1 ATOM 4671 H H . VAL A 1 305 ? 5.068 33.450 18.018 1.00 25.40 ? 313 VAL A H 1 ATOM 4672 H HA . VAL A 1 305 ? 6.507 32.416 15.984 1.00 21.57 ? 313 VAL A HA 1 ATOM 4673 H HB . VAL A 1 305 ? 4.416 31.189 17.451 1.00 20.98 ? 313 VAL A HB 1 ATOM 4674 H HG11 . VAL A 1 305 ? 5.077 29.190 16.459 1.00 21.93 ? 313 VAL A HG11 1 ATOM 4675 H HG12 . VAL A 1 305 ? 4.615 30.231 15.351 1.00 21.93 ? 313 VAL A HG12 1 ATOM 4676 H HG13 . VAL A 1 305 ? 6.162 29.976 15.605 1.00 21.93 ? 313 VAL A HG13 1 ATOM 4677 H HG21 . VAL A 1 305 ? 6.054 29.965 18.555 1.00 21.87 ? 313 VAL A HG21 1 ATOM 4678 H HG22 . VAL A 1 305 ? 7.180 30.771 17.776 1.00 21.87 ? 313 VAL A HG22 1 ATOM 4679 H HG23 . VAL A 1 305 ? 6.252 31.518 18.827 1.00 21.87 ? 313 VAL A HG23 1 ATOM 4680 N N . VAL A 1 306 ? 5.078 32.919 14.064 1.00 19.02 ? 314 VAL A N 1 ATOM 4681 C CA . VAL A 1 306 ? 4.233 33.256 12.925 1.00 18.69 ? 314 VAL A CA 1 ATOM 4682 C C . VAL A 1 306 ? 3.757 31.968 12.271 1.00 17.24 ? 314 VAL A C 1 ATOM 4683 O O . VAL A 1 306 ? 4.549 31.064 11.973 1.00 19.35 ? 314 VAL A O 1 ATOM 4684 C CB . VAL A 1 306 ? 4.976 34.146 11.914 1.00 22.81 ? 314 VAL A CB 1 ATOM 4685 C CG1 . VAL A 1 306 ? 4.118 34.403 10.702 1.00 24.51 ? 314 VAL A CG1 1 ATOM 4686 C CG2 . VAL A 1 306 ? 5.347 35.462 12.555 1.00 25.73 ? 314 VAL A CG2 1 ATOM 4687 H H . VAL A 1 306 ? 5.902 32.796 13.852 1.00 22.83 ? 314 VAL A H 1 ATOM 4688 H HA . VAL A 1 306 ? 3.454 33.741 13.239 1.00 22.43 ? 314 VAL A HA 1 ATOM 4689 H HB . VAL A 1 306 ? 5.789 33.703 11.628 1.00 27.37 ? 314 VAL A HB 1 ATOM 4690 H HG11 . VAL A 1 306 ? 4.608 34.965 10.082 1.00 29.42 ? 314 VAL A HG11 1 ATOM 4691 H HG12 . VAL A 1 306 ? 3.904 33.555 10.282 1.00 29.42 ? 314 VAL A HG12 1 ATOM 4692 H HG13 . VAL A 1 306 ? 3.303 34.849 10.981 1.00 29.42 ? 314 VAL A HG13 1 ATOM 4693 H HG21 . VAL A 1 306 ? 5.813 36.010 11.904 1.00 30.87 ? 314 VAL A HG21 1 ATOM 4694 H HG22 . VAL A 1 306 ? 4.537 35.911 12.846 1.00 30.87 ? 314 VAL A HG22 1 ATOM 4695 H HG23 . VAL A 1 306 ? 5.922 35.291 13.317 1.00 30.87 ? 314 VAL A HG23 1 ATOM 4696 N N . ASP A 1 307 ? 2.461 31.882 12.053 1.00 19.16 ? 315 ASP A N 1 ATOM 4697 C CA . ASP A 1 307 ? 1.872 30.783 11.300 1.00 20.75 ? 315 ASP A CA 1 ATOM 4698 C C . ASP A 1 307 ? 2.303 29.413 11.837 1.00 17.74 ? 315 ASP A C 1 ATOM 4699 O O . ASP A 1 307 ? 2.604 28.490 11.074 1.00 19.01 ? 315 ASP A O 1 ATOM 4700 C CB . ASP A 1 307 ? 2.197 30.914 9.814 1.00 23.74 ? 315 ASP A CB 1 ATOM 4701 C CG . ASP A 1 307 ? 1.292 30.073 8.950 1.00 26.16 ? 315 ASP A CG 1 ATOM 4702 O OD1 . ASP A 1 307 ? 0.171 29.742 9.415 1.00 25.52 ? 315 ASP A OD1 1 ATOM 4703 O OD2 . ASP A 1 307 ? 1.693 29.744 7.807 1.00 29.66 ? 315 ASP A OD2 1 ATOM 4704 H H . ASP A 1 307 ? 1.887 32.457 12.334 1.00 22.99 ? 315 ASP A H 1 ATOM 4705 H HA . ASP A 1 307 ? 0.907 30.836 11.389 1.00 24.90 ? 315 ASP A HA 1 ATOM 4706 H HB2 . ASP A 1 307 ? 2.093 31.840 9.548 1.00 28.49 ? 315 ASP A HB2 1 ATOM 4707 H HB3 . ASP A 1 307 ? 3.111 30.625 9.663 1.00 28.49 ? 315 ASP A HB3 1 ATOM 4708 N N . GLY A 1 308 ? 2.242 29.257 13.157 1.00 16.88 ? 316 GLY A N 1 ATOM 4709 C CA . GLY A 1 308 ? 2.738 28.078 13.841 1.00 15.45 ? 316 GLY A CA 1 ATOM 4710 C C . GLY A 1 308 ? 1.764 26.921 13.943 1.00 13.59 ? 316 GLY A C 1 ATOM 4711 O O . GLY A 1 308 ? 1.579 26.360 15.020 1.00 13.38 ? 316 GLY A O 1 ATOM 4712 H H . GLY A 1 308 ? 1.906 29.843 13.689 1.00 20.26 ? 316 GLY A H 1 ATOM 4713 H HA2 . GLY A 1 308 ? 3.530 27.760 13.379 1.00 18.54 ? 316 GLY A HA2 1 ATOM 4714 H HA3 . GLY A 1 308 ? 2.999 28.327 14.741 1.00 18.54 ? 316 GLY A HA3 1 ATOM 4715 N N . ALA A 1 309 ? 1.142 26.552 12.834 1.00 13.37 ? 317 ALA A N 1 ATOM 4716 C CA . ALA A 1 309 ? 0.294 25.380 12.750 1.00 13.56 ? 317 ALA A CA 1 ATOM 4717 C C . ALA A 1 309 ? 1.102 24.214 12.198 1.00 12.51 ? 317 ALA A C 1 ATOM 4718 O O . ALA A 1 309 ? 2.210 24.368 11.693 1.00 13.70 ? 317 ALA A O 1 ATOM 4719 C CB . ALA A 1 309 ? -0.927 25.673 11.869 1.00 13.63 ? 317 ALA A CB 1 ATOM 4720 H H . ALA A 1 309 ? 1.198 26.983 12.092 1.00 16.05 ? 317 ALA A H 1 ATOM 4721 H HA . ALA A 1 309 ? -0.018 25.143 13.638 1.00 16.28 ? 317 ALA A HA 1 ATOM 4722 H HB1 . ALA A 1 309 ? -1.482 24.878 11.825 1.00 16.36 ? 317 ALA A HB1 1 ATOM 4723 H HB2 . ALA A 1 309 ? -1.429 26.406 12.259 1.00 16.36 ? 317 ALA A HB2 1 ATOM 4724 H HB3 . ALA A 1 309 ? -0.624 25.915 10.980 1.00 16.36 ? 317 ALA A HB3 1 ATOM 4725 N N . ASN A 1 310 ? 0.527 23.028 12.287 1.00 11.68 ? 318 ASN A N 1 ATOM 4726 C CA . ASN A 1 310 ? 1.141 21.824 11.751 1.00 10.82 ? 318 ASN A CA 1 ATOM 4727 C C . ASN A 1 310 ? 0.058 20.922 11.184 1.00 11.00 ? 318 ASN A C 1 ATOM 4728 O O . ASN A 1 310 ? -1.100 21.017 11.575 1.00 12.07 ? 318 ASN A O 1 ATOM 4729 C CB . ASN A 1 310 ? 1.989 21.065 12.807 1.00 11.33 ? 318 ASN A CB 1 ATOM 4730 C CG . ASN A 1 310 ? 1.216 20.737 14.060 1.00 11.91 ? 318 ASN A CG 1 ATOM 4731 O OD1 . ASN A 1 310 ? 1.099 21.564 14.959 1.00 12.83 ? 318 ASN A OD1 1 ATOM 4732 N ND2 . ASN A 1 310 ? 0.667 19.538 14.135 1.00 11.80 ? 318 ASN A ND2 1 ATOM 4733 H H . ASN A 1 310 ? -0.235 22.890 12.661 1.00 14.01 ? 318 ASN A H 1 ATOM 4734 H HA . ASN A 1 310 ? 1.730 22.072 11.022 1.00 12.99 ? 318 ASN A HA 1 ATOM 4735 H HB2 . ASN A 1 310 ? 2.300 20.231 12.421 1.00 13.60 ? 318 ASN A HB2 1 ATOM 4736 H HB3 . ASN A 1 310 ? 2.746 21.617 13.058 1.00 13.60 ? 318 ASN A HB3 1 ATOM 4737 H HD21 . ASN A 1 310 ? 0.219 19.312 14.833 1.00 14.16 ? 318 ASN A HD21 1 ATOM 4738 H HD22 . ASN A 1 310 ? 0.759 18.982 13.485 1.00 14.16 ? 318 ASN A HD22 1 ATOM 4739 N N . ASN A 1 311 ? 0.435 20.030 10.276 1.00 11.00 ? 319 ASN A N 1 ATOM 4740 C CA . ASN A 1 311 ? -0.474 18.936 9.977 1.00 11.42 ? 319 ASN A CA 1 ATOM 4741 C C . ASN A 1 311 ? -0.476 17.902 11.104 1.00 11.10 ? 319 ASN A C 1 ATOM 4742 O O . ASN A 1 311 ? 0.528 17.728 11.803 1.00 11.24 ? 319 ASN A O 1 ATOM 4743 C CB . ASN A 1 311 ? -0.121 18.237 8.683 1.00 11.30 ? 319 ASN A CB 1 ATOM 4744 C CG . ASN A 1 311 ? -0.531 19.023 7.478 1.00 12.49 ? 319 ASN A CG 1 ATOM 4745 O OD1 . ASN A 1 311 ? -1.683 19.455 7.359 1.00 12.38 ? 319 ASN A OD1 1 ATOM 4746 N ND2 . ASN A 1 311 ? 0.398 19.218 6.584 1.00 13.01 ? 319 ASN A ND2 1 ATOM 4747 H H . ASN A 1 311 ? 1.175 20.033 9.838 1.00 13.19 ? 319 ASN A H 1 ATOM 4748 H HA . ASN A 1 311 ? -1.374 19.288 9.892 1.00 13.70 ? 319 ASN A HA 1 ATOM 4749 H HB2 . ASN A 1 311 ? 0.839 18.106 8.645 1.00 13.56 ? 319 ASN A HB2 1 ATOM 4750 H HB3 . ASN A 1 311 ? -0.575 17.380 8.652 1.00 13.56 ? 319 ASN A HB3 1 ATOM 4751 H HD21 . ASN A 1 311 ? 0.221 19.663 5.870 1.00 15.61 ? 319 ASN A HD21 1 ATOM 4752 H HD22 . ASN A 1 311 ? 1.188 18.901 6.709 1.00 15.61 ? 319 ASN A HD22 1 ATOM 4753 N N . PRO A 1 312 ? -1.587 17.191 11.284 1.00 11.04 ? 320 PRO A N 1 ATOM 4754 C CA . PRO A 1 312 ? -1.618 16.074 12.229 1.00 10.73 ? 320 PRO A CA 1 ATOM 4755 C C . PRO A 1 312 ? -0.576 15.024 11.881 1.00 10.85 ? 320 PRO A C 1 ATOM 4756 O O . PRO A 1 312 ? -0.435 14.634 10.723 1.00 11.51 ? 320 PRO A O 1 ATOM 4757 C CB . PRO A 1 312 ? -3.041 15.528 12.079 1.00 10.76 ? 320 PRO A CB 1 ATOM 4758 C CG . PRO A 1 312 ? -3.813 16.714 11.604 1.00 11.49 ? 320 PRO A CG 1 ATOM 4759 C CD . PRO A 1 312 ? -2.901 17.407 10.675 1.00 11.36 ? 320 PRO A CD 1 ATOM 4760 H HA . PRO A 1 312 ? -1.481 16.386 13.137 1.00 12.87 ? 320 PRO A HA 1 ATOM 4761 H HB2 . PRO A 1 312 ? -3.056 14.815 11.420 1.00 12.91 ? 320 PRO A HB2 1 ATOM 4762 H HB3 . PRO A 1 312 ? -3.371 15.218 12.937 1.00 12.91 ? 320 PRO A HB3 1 ATOM 4763 H HG2 . PRO A 1 312 ? -4.615 16.420 11.144 1.00 13.79 ? 320 PRO A HG2 1 ATOM 4764 H HG3 . PRO A 1 312 ? -4.036 17.283 12.357 1.00 13.79 ? 320 PRO A HG3 1 ATOM 4765 H HD2 . PRO A 1 312 ? -2.938 17.000 9.795 1.00 13.63 ? 320 PRO A HD2 1 ATOM 4766 H HD3 . PRO A 1 312 ? -3.108 18.354 10.640 1.00 13.63 ? 320 PRO A HD3 1 ATOM 4767 N N . GLY A 1 313 ? 0.161 14.565 12.902 1.00 10.95 ? 321 GLY A N 1 ATOM 4768 C CA . GLY A 1 313 ? 1.203 13.568 12.719 1.00 11.31 ? 321 GLY A CA 1 ATOM 4769 C C . GLY A 1 313 ? 1.136 12.446 13.737 1.00 11.20 ? 321 GLY A C 1 ATOM 4770 O O . GLY A 1 313 ? 0.687 12.631 14.871 1.00 11.89 ? 321 GLY A O 1 ATOM 4771 H H . GLY A 1 313 ? 0.069 14.824 13.717 1.00 13.14 ? 321 GLY A H 1 ATOM 4772 H HA2 . GLY A 1 313 ? 1.125 13.180 11.833 1.00 13.58 ? 321 GLY A HA2 1 ATOM 4773 H HA3 . GLY A 1 313 ? 2.072 13.994 12.791 1.00 13.58 ? 321 GLY A HA3 1 ATOM 4774 N N . ILE A 1 314 ? 1.595 11.257 13.309 1.00 11.56 ? 322 ILE A N 1 ATOM 4775 C CA . ILE A 1 314 ? 1.775 10.073 14.154 1.00 11.62 ? 322 ILE A CA 1 ATOM 4776 C C . ILE A 1 314 ? 3.109 9.441 13.759 1.00 11.42 ? 322 ILE A C 1 ATOM 4777 O O . ILE A 1 314 ? 3.631 9.708 12.682 1.00 12.44 ? 322 ILE A O 1 ATOM 4778 C CB . ILE A 1 314 ? 0.626 9.062 14.021 1.00 12.62 ? 322 ILE A CB 1 ATOM 4779 C CG1 . ILE A 1 314 ? 0.495 8.624 12.566 1.00 13.59 ? 322 ILE A CG1 1 ATOM 4780 C CG2 . ILE A 1 314 ? -0.664 9.661 14.569 1.00 13.68 ? 322 ILE A CG2 1 ATOM 4781 C CD1 . ILE A 1 314 ? -0.620 7.583 12.289 1.00 14.47 ? 322 ILE A CD1 1 ATOM 4782 H H . ILE A 1 314 ? 1.817 11.112 12.491 1.00 13.87 ? 322 ILE A H 1 ATOM 4783 H HA . ILE A 1 314 ? 1.831 10.348 15.083 1.00 13.95 ? 322 ILE A HA 1 ATOM 4784 H HB . ILE A 1 314 ? 0.847 8.282 14.553 1.00 15.15 ? 322 ILE A HB 1 ATOM 4785 H HG12 . ILE A 1 314 ? 0.306 9.406 12.024 1.00 16.31 ? 322 ILE A HG12 1 ATOM 4786 H HG13 . ILE A 1 314 ? 1.337 8.231 12.286 1.00 16.31 ? 322 ILE A HG13 1 ATOM 4787 H HG21 . ILE A 1 314 ? -1.378 9.010 14.476 1.00 16.42 ? 322 ILE A HG21 1 ATOM 4788 H HG22 . ILE A 1 314 ? -0.537 9.882 15.504 1.00 16.42 ? 322 ILE A HG22 1 ATOM 4789 H HG23 . ILE A 1 314 ? -0.879 10.461 14.065 1.00 16.42 ? 322 ILE A HG23 1 ATOM 4790 H HD11 . ILE A 1 314 ? -0.624 7.369 11.343 1.00 17.36 ? 322 ILE A HD11 1 ATOM 4791 H HD12 . ILE A 1 314 ? -0.442 6.783 12.808 1.00 17.36 ? 322 ILE A HD12 1 ATOM 4792 H HD13 . ILE A 1 314 ? -1.476 7.961 12.546 1.00 17.36 ? 322 ILE A HD13 1 ATOM 4793 N N . ARG A 1 315 ? 3.655 8.573 14.618 1.00 11.49 ? 323 ARG A N 1 ATOM 4794 C CA . ARG A 1 315 ? 5.021 8.120 14.403 1.00 11.02 ? 323 ARG A CA 1 ATOM 4795 C C . ARG A 1 315 ? 5.220 6.697 14.869 1.00 11.52 ? 323 ARG A C 1 ATOM 4796 O O . ARG A 1 315 ? 4.808 6.342 15.971 1.00 11.96 ? 323 ARG A O 1 ATOM 4797 C CB . ARG A 1 315 ? 5.999 9.007 15.162 1.00 12.00 ? 323 ARG A CB 1 ATOM 4798 C CG . ARG A 1 315 ? 7.435 8.549 15.084 1.00 12.91 ? 323 ARG A CG 1 ATOM 4799 C CD . ARG A 1 315 ? 8.326 9.583 15.724 1.00 12.81 ? 323 ARG A CD 1 ATOM 4800 N NE . ARG A 1 315 ? 8.520 10.711 14.826 1.00 13.01 ? 323 ARG A NE 1 ATOM 4801 C CZ . ARG A 1 315 ? 9.282 11.744 15.112 1.00 12.74 ? 323 ARG A CZ 1 ATOM 4802 N NH1 . ARG A 1 315 ? 9.821 11.859 16.310 1.00 12.49 ? 323 ARG A NH1 1 ATOM 4803 N NH2 . ARG A 1 315 ? 9.504 12.662 14.208 1.00 13.61 ? 323 ARG A NH2 1 ATOM 4804 H H . ARG A 1 315 ? 3.265 8.243 15.310 1.00 13.79 ? 323 ARG A H 1 ATOM 4805 H HA . ARG A 1 315 ? 5.233 8.167 13.457 1.00 13.22 ? 323 ARG A HA 1 ATOM 4806 H HB2 . ARG A 1 315 ? 5.954 9.904 14.795 1.00 14.40 ? 323 ARG A HB2 1 ATOM 4807 H HB3 . ARG A 1 315 ? 5.744 9.022 16.097 1.00 14.40 ? 323 ARG A HB3 1 ATOM 4808 H HG2 . ARG A 1 315 ? 7.537 7.712 15.563 1.00 15.49 ? 323 ARG A HG2 1 ATOM 4809 H HG3 . ARG A 1 315 ? 7.696 8.447 14.155 1.00 15.49 ? 323 ARG A HG3 1 ATOM 4810 H HD2 . ARG A 1 315 ? 7.912 9.906 16.539 1.00 15.38 ? 323 ARG A HD2 1 ATOM 4811 H HD3 . ARG A 1 315 ? 9.192 9.190 15.915 1.00 15.38 ? 323 ARG A HD3 1 ATOM 4812 H HE . ARG A 1 315 ? 8.218 10.643 14.024 1.00 15.62 ? 323 ARG A HE 1 ATOM 4813 H HH11 . ARG A 1 315 ? 9.705 11.240 16.895 1.00 14.99 ? 323 ARG A HH11 1 ATOM 4814 H HH12 . ARG A 1 315 ? 10.305 12.544 16.499 1.00 14.99 ? 323 ARG A HH12 1 ATOM 4815 H HH21 . ARG A 1 315 ? 9.129 12.603 13.436 1.00 16.33 ? 323 ARG A HH21 1 ATOM 4816 H HH22 . ARG A 1 315 ? 9.956 13.364 14.412 1.00 16.33 ? 323 ARG A HH22 1 ATOM 4817 N N . ILE A 1 316 ? 5.922 5.921 14.062 1.00 11.00 ? 324 ILE A N 1 ATOM 4818 C CA . ILE A 1 316 ? 6.354 4.596 14.458 1.00 12.38 ? 324 ILE A CA 1 ATOM 4819 C C . ILE A 1 316 ? 7.881 4.532 14.492 1.00 12.29 ? 324 ILE A C 1 ATOM 4820 O O . ILE A 1 316 ? 8.571 5.108 13.643 1.00 13.76 ? 324 ILE A O 1 ATOM 4821 C CB . ILE A 1 316 ? 5.716 3.520 13.553 1.00 16.59 ? 324 ILE A CB 1 ATOM 4822 C CG1 . ILE A 1 316 ? 5.723 2.158 14.234 1.00 18.63 ? 324 ILE A CG1 1 ATOM 4823 C CG2 . ILE A 1 316 ? 6.330 3.528 12.213 1.00 18.86 ? 324 ILE A CG2 1 ATOM 4824 C CD1 . ILE A 1 316 ? 4.795 1.184 13.545 1.00 20.63 ? 324 ILE A CD1 1 ATOM 4825 H H . ILE A 1 316 ? 6.164 6.143 13.267 1.00 13.19 ? 324 ILE A H 1 ATOM 4826 H HA . ILE A 1 316 ? 6.041 4.433 15.361 1.00 14.86 ? 324 ILE A HA 1 ATOM 4827 H HB . ILE A 1 316 ? 4.786 3.768 13.435 1.00 19.90 ? 324 ILE A HB 1 ATOM 4828 H HG12 . ILE A 1 316 ? 6.621 1.792 14.208 1.00 22.36 ? 324 ILE A HG12 1 ATOM 4829 H HG13 . ILE A 1 316 ? 5.429 2.259 15.153 1.00 22.36 ? 324 ILE A HG13 1 ATOM 4830 H HG21 . ILE A 1 316 ? 5.910 2.844 11.670 1.00 22.63 ? 324 ILE A HG21 1 ATOM 4831 H HG22 . ILE A 1 316 ? 6.196 4.400 11.810 1.00 22.63 ? 324 ILE A HG22 1 ATOM 4832 H HG23 . ILE A 1 316 ? 7.279 3.346 12.300 1.00 22.63 ? 324 ILE A HG23 1 ATOM 4833 H HD11 . ILE A 1 316 ? 4.830 0.334 14.010 1.00 24.75 ? 324 ILE A HD11 1 ATOM 4834 H HD12 . ILE A 1 316 ? 3.892 1.538 13.569 1.00 24.75 ? 324 ILE A HD12 1 ATOM 4835 H HD13 . ILE A 1 316 ? 5.083 1.072 12.626 1.00 24.75 ? 324 ILE A HD13 1 ATOM 4836 N N . PHE A 1 317 ? 8.412 3.863 15.514 1.00 11.63 ? 325 PHE A N 1 ATOM 4837 C CA . PHE A 1 317 ? 9.828 3.554 15.604 1.00 11.66 ? 325 PHE A CA 1 ATOM 4838 C C . PHE A 1 317 ? 10.048 2.080 15.323 1.00 12.99 ? 325 PHE A C 1 ATOM 4839 O O . PHE A 1 317 ? 9.234 1.237 15.721 1.00 14.03 ? 325 PHE A O 1 ATOM 4840 C CB . PHE A 1 317 ? 10.389 3.836 17.002 1.00 12.57 ? 325 PHE A CB 1 ATOM 4841 C CG . PHE A 1 317 ? 10.556 5.292 17.287 1.00 13.08 ? 325 PHE A CG 1 ATOM 4842 C CD1 . PHE A 1 317 ? 11.790 5.889 17.106 1.00 13.31 ? 325 PHE A CD1 1 ATOM 4843 C CD2 . PHE A 1 317 ? 9.526 6.044 17.796 1.00 12.74 ? 325 PHE A CD2 1 ATOM 4844 C CE1 . PHE A 1 317 ? 11.981 7.215 17.362 1.00 13.31 ? 325 PHE A CE1 1 ATOM 4845 C CE2 . PHE A 1 317 ? 9.695 7.393 18.045 1.00 12.79 ? 325 PHE A CE2 1 ATOM 4846 C CZ . PHE A 1 317 ? 10.946 7.965 17.850 1.00 12.37 ? 325 PHE A CZ 1 ATOM 4847 H H . PHE A 1 317 ? 7.956 3.572 16.182 1.00 13.96 ? 325 PHE A H 1 ATOM 4848 H HA . PHE A 1 317 ? 10.323 4.077 14.953 1.00 14.00 ? 325 PHE A HA 1 ATOM 4849 H HB2 . PHE A 1 317 ? 9.783 3.470 17.664 1.00 15.08 ? 325 PHE A HB2 1 ATOM 4850 H HB3 . PHE A 1 317 ? 11.259 3.415 17.082 1.00 15.08 ? 325 PHE A HB3 1 ATOM 4851 H HD1 . PHE A 1 317 ? 12.496 5.383 16.774 1.00 15.97 ? 325 PHE A HD1 1 ATOM 4852 H HD2 . PHE A 1 317 ? 8.691 5.654 17.922 1.00 15.29 ? 325 PHE A HD2 1 ATOM 4853 H HE1 . PHE A 1 317 ? 12.815 7.603 17.224 1.00 15.97 ? 325 PHE A HE1 1 ATOM 4854 H HE2 . PHE A 1 317 ? 8.993 7.901 18.383 1.00 15.34 ? 325 PHE A HE2 1 ATOM 4855 H HZ . PHE A 1 317 ? 11.072 8.869 18.026 1.00 14.84 ? 325 PHE A HZ 1 ATOM 4856 N N . GLU A 1 318 ? 11.162 1.780 14.661 1.00 13.03 ? 326 GLU A N 1 ATOM 4857 C CA . GLU A 1 318 ? 11.639 0.422 14.474 1.00 13.26 ? 326 GLU A CA 1 ATOM 4858 C C . GLU A 1 318 ? 12.868 0.265 15.369 1.00 13.36 ? 326 GLU A C 1 ATOM 4859 O O . GLU A 1 318 ? 13.727 1.142 15.385 1.00 14.47 ? 326 GLU A O 1 ATOM 4860 C CB . GLU A 1 318 ? 11.993 0.203 13.000 1.00 15.09 ? 326 GLU A CB 1 ATOM 4861 C CG . GLU A 1 318 ? 10.758 0.224 12.108 1.00 17.77 ? 326 GLU A CG 1 ATOM 4862 C CD . GLU A 1 318 ? 11.035 0.271 10.619 1.00 19.55 ? 326 GLU A CD 1 ATOM 4863 O OE1 . GLU A 1 318 ? 12.212 0.226 10.198 1.00 20.64 ? 326 GLU A OE1 1 ATOM 4864 O OE2 . GLU A 1 318 ? 10.051 0.347 9.845 1.00 22.44 ? 326 GLU A OE2 1 ATOM 4865 H H . GLU A 1 318 ? 11.673 2.371 14.301 1.00 15.64 ? 326 GLU A H 1 ATOM 4866 H HA . GLU A 1 318 ? 10.960 -0.216 14.742 1.00 15.91 ? 326 GLU A HA 1 ATOM 4867 H HB2 . GLU A 1 318 ? 12.589 0.910 12.708 1.00 18.11 ? 326 GLU A HB2 1 ATOM 4868 H HB3 . GLU A 1 318 ? 12.423 -0.660 12.901 1.00 18.11 ? 326 GLU A HB3 1 ATOM 4869 H HG2 . GLU A 1 318 ? 10.240 -0.577 12.282 1.00 21.32 ? 326 GLU A HG2 1 ATOM 4870 H HG3 . GLU A 1 318 ? 10.231 1.006 12.331 1.00 21.32 ? 326 GLU A HG3 1 ATOM 4871 N N . TYR A 1 319 ? 12.951 -0.837 16.110 1.00 13.95 ? 327 TYR A N 1 ATOM 4872 C CA . TYR A 1 319 ? 14.014 -1.001 17.098 1.00 14.09 ? 327 TYR A CA 1 ATOM 4873 C C . TYR A 1 319 ? 14.454 -2.457 17.168 1.00 15.03 ? 327 TYR A C 1 ATOM 4874 O O . TYR A 1 319 ? 13.710 -3.382 16.819 1.00 15.07 ? 327 TYR A O 1 ATOM 4875 C CB . TYR A 1 319 ? 13.601 -0.486 18.501 1.00 14.63 ? 327 TYR A CB 1 ATOM 4876 C CG . TYR A 1 319 ? 12.681 -1.405 19.259 1.00 14.56 ? 327 TYR A CG 1 ATOM 4877 C CD1 . TYR A 1 319 ? 11.342 -1.529 18.921 1.00 14.98 ? 327 TYR A CD1 1 ATOM 4878 C CD2 . TYR A 1 319 ? 13.141 -2.134 20.328 1.00 16.43 ? 327 TYR A CD2 1 ATOM 4879 C CE1 . TYR A 1 319 ? 10.506 -2.367 19.621 1.00 17.52 ? 327 TYR A CE1 1 ATOM 4880 C CE2 . TYR A 1 319 ? 12.307 -2.982 21.034 1.00 16.53 ? 327 TYR A CE2 1 ATOM 4881 C CZ . TYR A 1 319 ? 10.997 -3.092 20.673 1.00 15.11 ? 327 TYR A CZ 1 ATOM 4882 O OH . TYR A 1 319 ? 10.179 -3.924 21.372 1.00 17.83 ? 327 TYR A OH 1 ATOM 4883 H H . TYR A 1 319 ? 12.407 -1.501 16.061 1.00 16.74 ? 327 TYR A H 1 ATOM 4884 H HA . TYR A 1 319 ? 14.780 -0.479 16.812 1.00 16.91 ? 327 TYR A HA 1 ATOM 4885 H HB2 . TYR A 1 319 ? 14.401 -0.365 19.034 1.00 17.56 ? 327 TYR A HB2 1 ATOM 4886 H HB3 . TYR A 1 319 ? 13.146 0.365 18.397 1.00 17.56 ? 327 TYR A HB3 1 ATOM 4887 H HD1 . TYR A 1 319 ? 11.006 -1.043 18.203 1.00 17.98 ? 327 TYR A HD1 1 ATOM 4888 H HD2 . TYR A 1 319 ? 14.035 -2.067 20.574 1.00 19.72 ? 327 TYR A HD2 1 ATOM 4889 H HE1 . TYR A 1 319 ? 9.611 -2.445 19.377 1.00 21.02 ? 327 TYR A HE1 1 ATOM 4890 H HE2 . TYR A 1 319 ? 12.637 -3.474 21.751 1.00 19.84 ? 327 TYR A HE2 1 ATOM 4891 H HH . TYR A 1 319 ? 10.611 -4.303 21.986 1.00 21.39 ? 327 TYR A HH 1 ATOM 4892 N N . ASP A 1 320 ? 15.698 -2.643 17.603 1.00 15.04 ? 328 ASP A N 1 ATOM 4893 C CA . ASP A 1 320 ? 16.248 -3.977 17.854 1.00 16.46 ? 328 ASP A CA 1 ATOM 4894 C C . ASP A 1 320 ? 15.762 -4.462 19.213 1.00 16.86 ? 328 ASP A C 1 ATOM 4895 O O . ASP A 1 320 ? 16.073 -3.861 20.244 1.00 17.30 ? 328 ASP A O 1 ATOM 4896 C CB . ASP A 1 320 ? 17.776 -3.885 17.845 1.00 19.73 ? 328 ASP A CB 1 ATOM 4897 C CG . ASP A 1 320 ? 18.464 -5.203 18.118 1.00 24.91 ? 328 ASP A CG 1 ATOM 4898 O OD1 . ASP A 1 320 ? 17.830 -6.275 18.056 1.00 28.54 ? 328 ASP A OD1 1 ATOM 4899 O OD2 . ASP A 1 320 ? 19.678 -5.162 18.365 1.00 29.51 ? 328 ASP A OD2 1 ATOM 4900 H H . ASP A 1 320 ? 16.251 -2.005 17.763 1.00 18.05 ? 328 ASP A H 1 ATOM 4901 H HA . ASP A 1 320 ? 15.958 -4.598 17.167 1.00 19.75 ? 328 ASP A HA 1 ATOM 4902 H HB2 . ASP A 1 320 ? 18.066 -3.573 16.974 1.00 23.68 ? 328 ASP A HB2 1 ATOM 4903 H HB3 . ASP A 1 320 ? 18.056 -3.257 18.529 1.00 23.68 ? 328 ASP A HB3 1 ATOM 4904 N N . ARG A 1 321 ? 15.010 -5.554 19.215 1.00 18.03 ? 329 ARG A N 1 ATOM 4905 C CA . ARG A 1 321 ? 14.427 -6.057 20.442 1.00 18.40 ? 329 ARG A CA 1 ATOM 4906 C C . ARG A 1 321 ? 15.492 -6.521 21.425 1.00 20.10 ? 329 ARG A C 1 ATOM 4907 O O . ARG A 1 321 ? 15.243 -6.524 22.631 1.00 23.04 ? 329 ARG A O 1 ATOM 4908 C CB . ARG A 1 321 ? 13.481 -7.193 20.100 1.00 18.48 ? 329 ARG A CB 1 ATOM 4909 C CG . ARG A 1 321 ? 12.180 -6.724 19.497 1.00 18.55 ? 329 ARG A CG 1 ATOM 4910 C CD . ARG A 1 321 ? 11.494 -7.842 18.778 1.00 19.58 ? 329 ARG A CD 1 ATOM 4911 N NE . ARG A 1 321 ? 10.117 -7.493 18.458 1.00 19.29 ? 329 ARG A NE 1 ATOM 4912 C CZ . ARG A 1 321 ? 9.387 -8.116 17.544 1.00 19.29 ? 329 ARG A CZ 1 ATOM 4913 N NH1 . ARG A 1 321 ? 9.910 -9.117 16.846 1.00 20.26 ? 329 ARG A NH1 1 ATOM 4914 N NH2 . ARG A 1 321 ? 8.128 -7.758 17.327 1.00 18.21 ? 329 ARG A NH2 1 ATOM 4915 H H . ARG A 1 321 ? 14.823 -6.019 18.517 1.00 21.64 ? 329 ARG A H 1 ATOM 4916 H HA . ARG A 1 321 ? 13.913 -5.351 20.864 1.00 22.08 ? 329 ARG A HA 1 ATOM 4917 H HB2 . ARG A 1 321 ? 13.912 -7.779 19.458 1.00 22.17 ? 329 ARG A HB2 1 ATOM 4918 H HB3 . ARG A 1 321 ? 13.274 -7.685 20.910 1.00 22.17 ? 329 ARG A HB3 1 ATOM 4919 H HG2 . ARG A 1 321 ? 11.593 -6.408 20.202 1.00 22.26 ? 329 ARG A HG2 1 ATOM 4920 H HG3 . ARG A 1 321 ? 12.357 -6.013 18.860 1.00 22.26 ? 329 ARG A HG3 1 ATOM 4921 H HD2 . ARG A 1 321 ? 11.963 -8.026 17.949 1.00 23.50 ? 329 ARG A HD2 1 ATOM 4922 H HD3 . ARG A 1 321 ? 11.486 -8.630 19.343 1.00 23.50 ? 329 ARG A HD3 1 ATOM 4923 H HE . ARG A 1 321 ? 9.775 -6.807 18.847 1.00 23.15 ? 329 ARG A HE 1 ATOM 4924 H HH11 . ARG A 1 321 ? 10.722 -9.361 16.986 1.00 24.31 ? 329 ARG A HH11 1 ATOM 4925 H HH12 . ARG A 1 321 ? 9.436 -9.520 16.252 1.00 24.31 ? 329 ARG A HH12 1 ATOM 4926 H HH21 . ARG A 1 321 ? 7.783 -7.108 17.772 1.00 21.85 ? 329 ARG A HH21 1 ATOM 4927 H HH22 . ARG A 1 321 ? 7.664 -8.162 16.726 1.00 21.85 ? 329 ARG A HH22 1 ATOM 4928 N N . ALA A 1 322 ? 16.672 -6.916 20.942 1.00 21.12 ? 330 ALA A N 1 ATOM 4929 C CA . ALA A 1 322 ? 17.713 -7.436 21.826 1.00 24.41 ? 330 ALA A CA 1 ATOM 4930 C C . ALA A 1 322 ? 18.495 -6.351 22.557 1.00 23.55 ? 330 ALA A C 1 ATOM 4931 O O . ALA A 1 322 ? 19.097 -6.642 23.595 1.00 27.09 ? 330 ALA A O 1 ATOM 4932 C CB . ALA A 1 322 ? 18.700 -8.282 21.025 1.00 27.47 ? 330 ALA A CB 1 ATOM 4933 H H . ALA A 1 322 ? 16.893 -6.893 20.111 1.00 25.34 ? 330 ALA A H 1 ATOM 4934 H HA . ALA A 1 322 ? 17.302 -8.007 22.493 1.00 29.29 ? 330 ALA A HA 1 ATOM 4935 H HB1 . ALA A 1 322 ? 19.384 -8.620 21.624 1.00 32.97 ? 330 ALA A HB1 1 ATOM 4936 H HB2 . ALA A 1 322 ? 18.222 -9.022 20.617 1.00 32.97 ? 330 ALA A HB2 1 ATOM 4937 H HB3 . ALA A 1 322 ? 19.104 -7.730 20.338 1.00 32.97 ? 330 ALA A HB3 1 ATOM 4938 N N . THR A 1 323 ? 18.549 -5.131 22.031 1.00 20.21 ? 331 THR A N 1 ATOM 4939 C CA . THR A 1 323 ? 19.403 -4.077 22.569 1.00 20.04 ? 331 THR A CA 1 ATOM 4940 C C . THR A 1 323 ? 18.689 -2.764 22.809 1.00 17.38 ? 331 THR A C 1 ATOM 4941 O O . THR A 1 323 ? 19.263 -1.883 23.457 1.00 17.46 ? 331 THR A O 1 ATOM 4942 C CB . THR A 1 323 ? 20.543 -3.780 21.588 1.00 21.05 ? 331 THR A CB 1 ATOM 4943 O OG1 . THR A 1 323 ? 19.967 -3.287 20.378 1.00 21.17 ? 331 THR A OG1 1 ATOM 4944 C CG2 . THR A 1 323 ? 21.384 -5.030 21.307 1.00 22.85 ? 331 THR A CG2 1 ATOM 4945 H H . THR A 1 323 ? 18.089 -4.884 21.348 1.00 24.25 ? 331 THR A H 1 ATOM 4946 H HA . THR A 1 323 ? 19.790 -4.373 23.408 1.00 24.05 ? 331 THR A HA 1 ATOM 4947 H HB . THR A 1 323 ? 21.123 -3.101 21.967 1.00 25.27 ? 331 THR A HB 1 ATOM 4948 H HG1 . THR A 1 323 ? 19.451 -3.862 20.051 1.00 25.40 ? 331 THR A HG1 1 ATOM 4949 H HG21 . THR A 1 323 ? 22.097 -4.817 20.685 1.00 27.42 ? 331 THR A HG21 1 ATOM 4950 H HG22 . THR A 1 323 ? 21.773 -5.360 22.132 1.00 27.42 ? 331 THR A HG22 1 ATOM 4951 H HG23 . THR A 1 323 ? 20.827 -5.725 20.922 1.00 27.42 ? 331 THR A HG23 1 ATOM 4952 N N . LEU A 1 324 ? 17.479 -2.591 22.276 1.00 15.33 ? 332 LEU A N 1 ATOM 4953 C CA . LEU A 1 324 ? 16.749 -1.327 22.221 1.00 14.77 ? 332 LEU A CA 1 ATOM 4954 C C . LEU A 1 324 ? 17.367 -0.315 21.262 1.00 14.67 ? 332 LEU A C 1 ATOM 4955 O O . LEU A 1 324 ? 16.876 0.804 21.182 1.00 14.97 ? 332 LEU A O 1 ATOM 4956 C CB . LEU A 1 324 ? 16.456 -0.695 23.592 1.00 15.46 ? 332 LEU A CB 1 ATOM 4957 C CG . LEU A 1 324 ? 15.603 -1.503 24.558 1.00 18.96 ? 332 LEU A CG 1 ATOM 4958 C CD1 . LEU A 1 324 ? 14.996 -0.590 25.619 1.00 17.46 ? 332 LEU A CD1 1 ATOM 4959 C CD2 . LEU A 1 324 ? 14.577 -2.342 23.935 1.00 21.62 ? 332 LEU A CD2 1 ATOM 4960 H H . LEU A 1 324 ? 17.037 -3.236 21.919 1.00 18.39 ? 332 LEU A H 1 ATOM 4961 H HA . LEU A 1 324 ? 15.879 -1.535 21.846 1.00 17.72 ? 332 LEU A HA 1 ATOM 4962 H HB2 . LEU A 1 324 ? 17.303 -0.525 24.032 1.00 18.55 ? 332 LEU A HB2 1 ATOM 4963 H HB3 . LEU A 1 324 ? 15.999 0.147 23.444 1.00 18.55 ? 332 LEU A HB3 1 ATOM 4964 H HG . LEU A 1 324 ? 16.198 -2.108 25.028 1.00 22.76 ? 332 LEU A HG 1 ATOM 4965 H HD11 . LEU A 1 324 ? 14.457 -1.124 26.224 1.00 20.95 ? 332 LEU A HD11 1 ATOM 4966 H HD12 . LEU A 1 324 ? 15.712 -0.156 26.109 1.00 20.95 ? 332 LEU A HD12 1 ATOM 4967 H HD13 . LEU A 1 324 ? 14.442 0.076 25.182 1.00 20.95 ? 332 LEU A HD13 1 ATOM 4968 H HD21 . LEU A 1 324 ? 14.090 -2.813 24.629 1.00 25.95 ? 332 LEU A HD21 1 ATOM 4969 H HD22 . LEU A 1 324 ? 13.970 -1.777 23.431 1.00 25.95 ? 332 LEU A HD22 1 ATOM 4970 H HD23 . LEU A 1 324 ? 15.006 -2.978 23.342 1.00 25.95 ? 332 LEU A HD23 1 ATOM 4971 N N . ASN A 1 325 ? 18.387 -0.679 20.491 1.00 16.01 ? 333 ASN A N 1 ATOM 4972 C CA . ASN A 1 325 ? 18.936 0.272 19.523 1.00 15.14 ? 333 ASN A CA 1 ATOM 4973 C C . ASN A 1 325 ? 17.849 0.684 18.548 1.00 14.92 ? 333 ASN A C 1 ATOM 4974 O O . ASN A 1 325 ? 17.146 -0.155 18.005 1.00 15.58 ? 333 ASN A O 1 ATOM 4975 C CB . ASN A 1 325 ? 20.102 -0.334 18.744 1.00 17.38 ? 333 ASN A CB 1 ATOM 4976 C CG . ASN A 1 325 ? 21.347 -0.488 19.568 1.00 22.04 ? 333 ASN A CG 1 ATOM 4977 O OD1 . ASN A 1 325 ? 21.557 0.246 20.514 1.00 24.93 ? 333 ASN A OD1 1 ATOM 4978 N ND2 . ASN A 1 325 ? 22.202 -1.433 19.187 1.00 24.58 ? 333 ASN A ND2 1 ATOM 4979 H H . ASN A 1 325 ? 18.772 -1.448 20.505 1.00 19.21 ? 333 ASN A H 1 ATOM 4980 H HA . ASN A 1 325 ? 19.252 1.063 19.988 1.00 18.16 ? 333 ASN A HA 1 ATOM 4981 H HB2 . ASN A 1 325 ? 19.844 -1.213 18.426 1.00 20.85 ? 333 ASN A HB2 1 ATOM 4982 H HB3 . ASN A 1 325 ? 20.311 0.242 17.992 1.00 20.85 ? 333 ASN A HB3 1 ATOM 4983 H HD21 . ASN A 1 325 ? 22.929 -1.558 19.629 1.00 29.50 ? 333 ASN A HD21 1 ATOM 4984 H HD22 . ASN A 1 325 ? 22.027 -1.919 18.500 1.00 29.50 ? 333 ASN A HD22 1 ATOM 4985 N N . LEU A 1 326 ? 17.741 1.981 18.298 1.00 14.07 ? 334 LEU A N 1 ATOM 4986 C CA . LEU A 1 326 ? 16.732 2.502 17.390 1.00 13.80 ? 334 LEU A CA 1 ATOM 4987 C C . LEU A 1 326 ? 17.236 2.404 15.959 1.00 13.62 ? 334 LEU A C 1 ATOM 4988 O O . LEU A 1 326 ? 18.282 2.955 15.602 1.00 14.83 ? 334 LEU A O 1 ATOM 4989 C CB . LEU A 1 326 ? 16.395 3.947 17.755 1.00 13.21 ? 334 LEU A CB 1 ATOM 4990 C CG . LEU A 1 326 ? 15.737 4.098 19.134 1.00 14.22 ? 334 LEU A CG 1 ATOM 4991 C CD1 . LEU A 1 326 ? 15.663 5.566 19.525 1.00 16.63 ? 334 LEU A CD1 1 ATOM 4992 C CD2 . LEU A 1 326 ? 14.349 3.466 19.167 1.00 14.67 ? 334 LEU A CD2 1 ATOM 4993 H H . LEU A 1 326 ? 18.245 2.586 18.644 1.00 16.88 ? 334 LEU A H 1 ATOM 4994 H HA . LEU A 1 326 ? 15.924 1.971 17.467 1.00 16.55 ? 334 LEU A HA 1 ATOM 4995 H HB2 . LEU A 1 326 ? 17.214 4.468 17.759 1.00 15.85 ? 334 LEU A HB2 1 ATOM 4996 H HB3 . LEU A 1 326 ? 15.782 4.302 17.093 1.00 15.85 ? 334 LEU A HB3 1 ATOM 4997 H HG . LEU A 1 326 ? 16.285 3.643 19.793 1.00 17.07 ? 334 LEU A HG 1 ATOM 4998 H HD11 . LEU A 1 326 ? 15.245 5.640 20.397 1.00 19.95 ? 334 LEU A HD11 1 ATOM 4999 H HD12 . LEU A 1 326 ? 16.562 5.929 19.556 1.00 19.95 ? 334 LEU A HD12 1 ATOM 5000 H HD13 . LEU A 1 326 ? 15.137 6.042 18.863 1.00 19.95 ? 334 LEU A HD13 1 ATOM 5001 H HD21 . LEU A 1 326 ? 13.970 3.583 20.052 1.00 17.60 ? 334 LEU A HD21 1 ATOM 5002 H HD22 . LEU A 1 326 ? 13.789 3.902 18.506 1.00 17.60 ? 334 LEU A HD22 1 ATOM 5003 H HD23 . LEU A 1 326 ? 14.428 2.521 18.963 1.00 17.60 ? 334 LEU A HD23 1 ATOM 5004 N N . LYS A 1 327 ? 16.459 1.725 15.134 1.00 13.84 ? 335 LYS A N 1 ATOM 5005 C CA . LYS A 1 327 ? 16.830 1.455 13.759 1.00 14.40 ? 335 LYS A CA 1 ATOM 5006 C C . LYS A 1 327 ? 16.240 2.456 12.782 1.00 13.72 ? 335 LYS A C 1 ATOM 5007 O O . LYS A 1 327 ? 16.862 2.734 11.757 1.00 15.29 ? 335 LYS A O 1 ATOM 5008 C CB . LYS A 1 327 ? 16.433 0.029 13.384 1.00 16.22 ? 335 LYS A CB 1 ATOM 5009 C CG . LYS A 1 327 ? 17.175 -1.031 14.211 1.00 18.60 ? 335 LYS A CG 1 ATOM 5010 C CD . LYS A 1 327 ? 18.694 -0.971 14.019 1.00 23.27 ? 335 LYS A CD 1 ATOM 5011 C CE . LYS A 1 327 ? 19.416 -2.120 14.722 1.00 27.79 ? 335 LYS A CE 1 ATOM 5012 N NZ . LYS A 1 327 ? 20.893 -2.053 14.531 1.00 30.57 ? 335 LYS A NZ 1 ATOM 5013 H H . LYS A 1 327 ? 15.693 1.403 15.354 1.00 16.61 ? 335 LYS A H 1 ATOM 5014 H HA . LYS A 1 327 ? 17.795 1.516 13.687 1.00 17.28 ? 335 LYS A HA 1 ATOM 5015 H HB2 . LYS A 1 327 ? 15.482 -0.085 13.535 1.00 19.46 ? 335 LYS A HB2 1 ATOM 5016 H HB3 . LYS A 1 327 ? 16.641 -0.121 12.448 1.00 19.46 ? 335 LYS A HB3 1 ATOM 5017 H HG2 . LYS A 1 327 ? 16.986 -0.888 15.152 1.00 22.32 ? 335 LYS A HG2 1 ATOM 5018 H HG3 . LYS A 1 327 ? 16.873 -1.912 13.942 1.00 22.32 ? 335 LYS A HG3 1 ATOM 5019 H HD2 . LYS A 1 327 ? 18.896 -1.023 13.072 1.00 27.92 ? 335 LYS A HD2 1 ATOM 5020 H HD3 . LYS A 1 327 ? 19.027 -0.137 14.385 1.00 27.92 ? 335 LYS A HD3 1 ATOM 5021 H HE2 . LYS A 1 327 ? 19.232 -2.077 15.673 1.00 33.35 ? 335 LYS A HE2 1 ATOM 5022 H HE3 . LYS A 1 327 ? 19.102 -2.963 14.359 1.00 33.35 ? 335 LYS A HE3 1 ATOM 5023 H HZ1 . LYS A 1 327 ? 21.285 -2.733 14.951 1.00 36.69 ? 335 LYS A HZ1 1 ATOM 5024 H HZ2 . LYS A 1 327 ? 21.090 -2.096 13.665 1.00 36.69 ? 335 LYS A HZ2 1 ATOM 5025 H HZ3 . LYS A 1 327 ? 21.208 -1.289 14.862 1.00 36.69 ? 335 LYS A HZ3 1 ATOM 5026 N N . ASP A 1 328 ? 15.061 3.004 13.057 1.00 12.89 ? 336 ASP A N 1 ATOM 5027 C CA . ASP A 1 328 ? 14.455 3.954 12.130 1.00 13.08 ? 336 ASP A CA 1 ATOM 5028 C C . ASP A 1 328 ? 13.232 4.543 12.799 1.00 13.17 ? 336 ASP A C 1 ATOM 5029 O O . ASP A 1 328 ? 12.776 4.091 13.853 1.00 13.52 ? 336 ASP A O 1 ATOM 5030 C CB . ASP A 1 328 ? 14.042 3.304 10.797 1.00 14.32 ? 336 ASP A CB 1 ATOM 5031 C CG . ASP A 1 328 ? 14.355 4.169 9.591 1.00 14.74 ? 336 ASP A CG 1 ATOM 5032 O OD1 . ASP A 1 328 ? 14.385 5.423 9.726 1.00 14.20 ? 336 ASP A OD1 1 ATOM 5033 O OD2 . ASP A 1 328 ? 14.543 3.567 8.492 1.00 16.28 ? 336 ASP A OD2 1 ATOM 5034 H H . ASP A 1 328 ? 14.597 2.846 13.764 1.00 15.46 ? 336 ASP A H 1 ATOM 5035 H HA . ASP A 1 328 ? 15.081 4.671 11.944 1.00 15.70 ? 336 ASP A HA 1 ATOM 5036 H HB2 . ASP A 1 328 ? 14.518 2.465 10.694 1.00 17.18 ? 336 ASP A HB2 1 ATOM 5037 H HB3 . ASP A 1 328 ? 13.085 3.142 10.808 1.00 17.18 ? 336 ASP A HB3 1 ATOM 5038 N N . LEU A 1 329 ? 12.732 5.589 12.192 1.00 13.08 ? 337 LEU A N 1 ATOM 5039 C CA . LEU A 1 329 ? 11.393 6.036 12.506 1.00 13.07 ? 337 LEU A CA 1 ATOM 5040 C C . LEU A 1 329 ? 10.714 6.445 11.213 1.00 12.32 ? 337 LEU A C 1 ATOM 5041 O O . LEU A 1 329 ? 11.363 6.854 10.252 1.00 13.81 ? 337 LEU A O 1 ATOM 5042 C CB . LEU A 1 329 ? 11.346 7.161 13.542 1.00 14.64 ? 337 LEU A CB 1 ATOM 5043 C CG . LEU A 1 329 ? 11.894 8.543 13.203 1.00 15.60 ? 337 LEU A CG 1 ATOM 5044 C CD1 . LEU A 1 329 ? 10.914 9.401 12.380 1.00 15.94 ? 337 LEU A CD1 1 ATOM 5045 C CD2 . LEU A 1 329 ? 12.231 9.342 14.451 1.00 16.21 ? 337 LEU A CD2 1 ATOM 5046 H H . LEU A 1 329 ? 13.139 6.059 11.598 1.00 15.70 ? 337 LEU A H 1 ATOM 5047 H HA . LEU A 1 329 ? 10.898 5.286 12.871 1.00 15.68 ? 337 LEU A HA 1 ATOM 5048 H HB2 . LEU A 1 329 ? 10.417 7.287 13.790 1.00 17.57 ? 337 LEU A HB2 1 ATOM 5049 H HB3 . LEU A 1 329 ? 11.836 6.856 14.322 1.00 17.57 ? 337 LEU A HB3 1 ATOM 5050 H HG . LEU A 1 329 ? 12.708 8.440 12.685 1.00 18.72 ? 337 LEU A HG 1 ATOM 5051 H HD11 . LEU A 1 329 ? 11.323 10.262 12.200 1.00 19.13 ? 337 LEU A HD11 1 ATOM 5052 H HD12 . LEU A 1 329 ? 10.720 8.946 11.545 1.00 19.13 ? 337 LEU A HD12 1 ATOM 5053 H HD13 . LEU A 1 329 ? 10.097 9.523 12.888 1.00 19.13 ? 337 LEU A HD13 1 ATOM 5054 H HD21 . LEU A 1 329 ? 12.574 10.210 14.186 1.00 19.45 ? 337 LEU A HD21 1 ATOM 5055 H HD22 . LEU A 1 329 ? 11.427 9.452 14.982 1.00 19.45 ? 337 LEU A HD22 1 ATOM 5056 H HD23 . LEU A 1 329 ? 12.902 8.862 14.961 1.00 19.45 ? 337 LEU A HD23 1 ATOM 5057 N N . VAL A 1 330 ? 9.399 6.305 11.201 1.00 11.89 ? 338 VAL A N 1 ATOM 5058 C CA . VAL A 1 330 ? 8.567 6.722 10.074 1.00 12.88 ? 338 VAL A CA 1 ATOM 5059 C C . VAL A 1 330 ? 7.485 7.621 10.657 1.00 11.75 ? 338 VAL A C 1 ATOM 5060 O O . VAL A 1 330 ? 6.800 7.243 11.616 1.00 12.80 ? 338 VAL A O 1 ATOM 5061 C CB . VAL A 1 330 ? 7.949 5.544 9.298 1.00 14.10 ? 338 VAL A CB 1 ATOM 5062 C CG1 . VAL A 1 330 ? 7.146 6.077 8.120 1.00 15.24 ? 338 VAL A CG1 1 ATOM 5063 C CG2 . VAL A 1 330 ? 9.034 4.594 8.835 1.00 15.73 ? 338 VAL A CG2 1 ATOM 5064 H H . VAL A 1 330 ? 8.949 5.963 11.849 1.00 14.27 ? 338 VAL A H 1 ATOM 5065 H HA . VAL A 1 330 ? 9.101 7.246 9.458 1.00 15.45 ? 338 VAL A HA 1 ATOM 5066 H HB . VAL A 1 330 ? 7.346 5.057 9.882 1.00 16.92 ? 338 VAL A HB 1 ATOM 5067 H HG11 . VAL A 1 330 ? 6.760 5.329 7.637 1.00 18.29 ? 338 VAL A HG11 1 ATOM 5068 H HG12 . VAL A 1 330 ? 6.441 6.654 8.454 1.00 18.29 ? 338 VAL A HG12 1 ATOM 5069 H HG13 . VAL A 1 330 ? 7.737 6.579 7.537 1.00 18.29 ? 338 VAL A HG13 1 ATOM 5070 H HG21 . VAL A 1 330 ? 8.625 3.861 8.349 1.00 18.88 ? 338 VAL A HG21 1 ATOM 5071 H HG22 . VAL A 1 330 ? 9.647 5.074 8.256 1.00 18.88 ? 338 VAL A HG22 1 ATOM 5072 H HG23 . VAL A 1 330 ? 9.508 4.255 9.610 1.00 18.88 ? 338 VAL A HG23 1 ATOM 5073 N N . THR A 1 331 ? 7.372 8.818 10.128 1.00 11.84 ? 339 THR A N 1 ATOM 5074 C CA . THR A 1 331 ? 6.329 9.731 10.548 1.00 11.89 ? 339 THR A CA 1 ATOM 5075 C C . THR A 1 331 ? 5.279 9.739 9.443 1.00 12.06 ? 339 THR A C 1 ATOM 5076 O O . THR A 1 331 ? 5.616 9.780 8.254 1.00 12.41 ? 339 THR A O 1 ATOM 5077 C CB . THR A 1 331 ? 6.903 11.131 10.820 1.00 12.13 ? 339 THR A CB 1 ATOM 5078 O OG1 . THR A 1 331 ? 7.944 11.012 11.792 1.00 12.80 ? 339 THR A OG1 1 ATOM 5079 C CG2 . THR A 1 331 ? 5.850 12.069 11.367 1.00 13.12 ? 339 THR A CG2 1 ATOM 5080 H H . THR A 1 331 ? 7.890 9.132 9.517 1.00 14.21 ? 339 THR A H 1 ATOM 5081 H HA . THR A 1 331 ? 5.918 9.403 11.362 1.00 14.27 ? 339 THR A HA 1 ATOM 5082 H HB . THR A 1 331 ? 7.260 11.506 10.000 1.00 14.56 ? 339 THR A HB 1 ATOM 5083 H HG1 . THR A 1 331 ? 8.272 11.767 11.956 1.00 15.36 ? 339 THR A HG1 1 ATOM 5084 H HG21 . THR A 1 331 ? 6.238 12.943 11.530 1.00 15.75 ? 339 THR A HG21 1 ATOM 5085 H HG22 . THR A 1 331 ? 5.125 12.160 10.730 1.00 15.75 ? 339 THR A HG22 1 ATOM 5086 H HG23 . THR A 1 331 ? 5.497 11.721 12.200 1.00 15.75 ? 339 THR A HG23 1 ATOM 5087 N N . TYR A 1 332 ? 4.018 9.646 9.852 1.00 12.34 ? 340 TYR A N 1 ATOM 5088 C CA . TYR A 1 332 ? 2.868 9.668 8.965 1.00 12.65 ? 340 TYR A CA 1 ATOM 5089 C C . TYR A 1 332 ? 2.068 10.924 9.258 1.00 12.06 ? 340 TYR A C 1 ATOM 5090 O O . TYR A 1 332 ? 2.134 11.464 10.367 1.00 12.35 ? 340 TYR A O 1 ATOM 5091 C CB . TYR A 1 332 ? 1.987 8.425 9.171 1.00 13.21 ? 340 TYR A CB 1 ATOM 5092 C CG . TYR A 1 332 ? 2.694 7.115 8.948 1.00 14.46 ? 340 TYR A CG 1 ATOM 5093 C CD1 . TYR A 1 332 ? 3.415 6.521 9.979 1.00 15.84 ? 340 TYR A CD1 1 ATOM 5094 C CD2 . TYR A 1 332 ? 2.649 6.469 7.721 1.00 16.77 ? 340 TYR A CD2 1 ATOM 5095 C CE1 . TYR A 1 332 ? 4.082 5.362 9.803 1.00 18.68 ? 340 TYR A CE1 1 ATOM 5096 C CE2 . TYR A 1 332 ? 3.334 5.264 7.534 1.00 18.68 ? 340 TYR A CE2 1 ATOM 5097 C CZ . TYR A 1 332 ? 4.041 4.734 8.594 1.00 20.14 ? 340 TYR A CZ 1 ATOM 5098 O OH . TYR A 1 332 ? 4.726 3.560 8.463 1.00 24.51 ? 340 TYR A OH 1 ATOM 5099 H H . TYR A 1 332 ? 3.798 9.566 10.679 1.00 14.80 ? 340 TYR A H 1 ATOM 5100 H HA . TYR A 1 332 ? 3.165 9.693 8.041 1.00 15.18 ? 340 TYR A HA 1 ATOM 5101 H HB2 . TYR A 1 332 ? 1.654 8.429 10.082 1.00 15.85 ? 340 TYR A HB2 1 ATOM 5102 H HB3 . TYR A 1 332 ? 1.242 8.467 8.551 1.00 15.85 ? 340 TYR A HB3 1 ATOM 5103 H HD1 . TYR A 1 332 ? 3.459 6.948 10.805 1.00 19.00 ? 340 TYR A HD1 1 ATOM 5104 H HD2 . TYR A 1 332 ? 2.176 6.848 7.015 1.00 20.12 ? 340 TYR A HD2 1 ATOM 5105 H HE1 . TYR A 1 332 ? 4.561 4.988 10.507 1.00 22.42 ? 340 TYR A HE1 1 ATOM 5106 H HE2 . TYR A 1 332 ? 3.312 4.829 6.712 1.00 22.41 ? 340 TYR A HE2 1 ATOM 5107 H HH . TYR A 1 332 ? 4.635 3.259 7.684 1.00 29.41 ? 340 TYR A HH 1 ATOM 5108 N N . PHE A 1 333 ? 1.271 11.373 8.279 1.00 12.20 ? 341 PHE A N 1 ATOM 5109 C CA . PHE A 1 333 ? 0.548 12.612 8.490 1.00 12.03 ? 341 PHE A CA 1 ATOM 5110 C C . PHE A 1 333 ? -0.750 12.610 7.723 1.00 13.04 ? 341 PHE A C 1 ATOM 5111 O O . PHE A 1 333 ? -0.935 11.860 6.756 1.00 13.96 ? 341 PHE A O 1 ATOM 5112 C CB . PHE A 1 333 ? 1.372 13.857 8.154 1.00 12.95 ? 341 PHE A CB 1 ATOM 5113 C CG . PHE A 1 333 ? 1.555 14.167 6.674 1.00 13.56 ? 341 PHE A CG 1 ATOM 5114 C CD1 . PHE A 1 333 ? 2.153 13.290 5.772 1.00 13.63 ? 341 PHE A CD1 1 ATOM 5115 C CD2 . PHE A 1 333 ? 1.176 15.416 6.207 1.00 13.82 ? 341 PHE A CD2 1 ATOM 5116 C CE1 . PHE A 1 333 ? 2.358 13.657 4.454 1.00 15.40 ? 341 PHE A CE1 1 ATOM 5117 C CE2 . PHE A 1 333 ? 1.398 15.787 4.905 1.00 15.23 ? 341 PHE A CE2 1 ATOM 5118 C CZ . PHE A 1 333 ? 1.975 14.905 4.021 1.00 15.45 ? 341 PHE A CZ 1 ATOM 5119 H H . PHE A 1 333 ? 1.140 10.992 7.519 1.00 14.64 ? 341 PHE A H 1 ATOM 5120 H HA . PHE A 1 333 ? 0.322 12.669 9.432 1.00 14.44 ? 341 PHE A HA 1 ATOM 5121 H HB2 . PHE A 1 333 ? 0.940 14.626 8.558 1.00 15.54 ? 341 PHE A HB2 1 ATOM 5122 H HB3 . PHE A 1 333 ? 2.257 13.748 8.536 1.00 15.54 ? 341 PHE A HB3 1 ATOM 5123 H HD1 . PHE A 1 333 ? 2.429 12.451 6.063 1.00 16.35 ? 341 PHE A HD1 1 ATOM 5124 H HD2 . PHE A 1 333 ? 0.803 16.029 6.799 1.00 16.59 ? 341 PHE A HD2 1 ATOM 5125 H HE1 . PHE A 1 333 ? 2.747 13.057 3.859 1.00 18.48 ? 341 PHE A HE1 1 ATOM 5126 H HE2 . PHE A 1 333 ? 1.123 16.625 4.609 1.00 18.27 ? 341 PHE A HE2 1 ATOM 5127 H HZ . PHE A 1 333 ? 2.093 15.147 3.131 1.00 18.54 ? 341 PHE A HZ 1 ATOM 5128 N N . LEU A 1 334 ? -1.614 13.515 8.136 1.00 12.58 ? 342 LEU A N 1 ATOM 5129 C CA . LEU A 1 334 ? -2.837 13.832 7.428 1.00 12.38 ? 342 LEU A CA 1 ATOM 5130 C C . LEU A 1 334 ? -2.663 15.230 6.862 1.00 13.52 ? 342 LEU A C 1 ATOM 5131 O O . LEU A 1 334 ? -2.428 16.172 7.615 1.00 14.10 ? 342 LEU A O 1 ATOM 5132 C CB . LEU A 1 334 ? -4.040 13.780 8.364 1.00 12.55 ? 342 LEU A CB 1 ATOM 5133 C CG . LEU A 1 334 ? -5.372 13.973 7.628 1.00 13.25 ? 342 LEU A CG 1 ATOM 5134 C CD1 . LEU A 1 334 ? -5.664 12.763 6.768 1.00 14.69 ? 342 LEU A CD1 1 ATOM 5135 C CD2 . LEU A 1 334 ? -6.460 14.153 8.653 1.00 15.96 ? 342 LEU A CD2 1 ATOM 5136 H H . LEU A 1 334 ? -1.509 13.978 8.853 1.00 15.10 ? 342 LEU A H 1 ATOM 5137 H HA . LEU A 1 334 ? -2.973 13.207 6.698 1.00 14.85 ? 342 LEU A HA 1 ATOM 5138 H HB2 . LEU A 1 334 ? -4.063 12.916 8.803 1.00 15.06 ? 342 LEU A HB2 1 ATOM 5139 H HB3 . LEU A 1 334 ? -3.958 14.486 9.024 1.00 15.06 ? 342 LEU A HB3 1 ATOM 5140 H HG . LEU A 1 334 ? -5.332 14.762 7.065 1.00 15.91 ? 342 LEU A HG 1 ATOM 5141 H HD11 . LEU A 1 334 ? -6.507 12.898 6.309 1.00 17.62 ? 342 LEU A HD11 1 ATOM 5142 H HD12 . LEU A 1 334 ? -4.948 12.655 6.122 1.00 17.62 ? 342 LEU A HD12 1 ATOM 5143 H HD13 . LEU A 1 334 ? -5.717 11.978 7.336 1.00 17.62 ? 342 LEU A HD13 1 ATOM 5144 H HD21 . LEU A 1 334 ? -7.307 14.275 8.196 1.00 19.15 ? 342 LEU A HD21 1 ATOM 5145 H HD22 . LEU A 1 334 ? -6.498 13.362 9.215 1.00 19.15 ? 342 LEU A HD22 1 ATOM 5146 H HD23 . LEU A 1 334 ? -6.259 14.933 9.193 1.00 19.15 ? 342 LEU A HD23 1 ATOM 5147 N N . ASN A 1 335 ? -2.736 15.368 5.537 1.00 13.32 ? 343 ASN A N 1 ATOM 5148 C CA . ASN A 1 335 ? -2.674 16.698 4.933 1.00 13.81 ? 343 ASN A CA 1 ATOM 5149 C C . ASN A 1 335 ? -4.050 17.320 5.106 1.00 13.11 ? 343 ASN A C 1 ATOM 5150 O O . ASN A 1 335 ? -4.986 17.004 4.373 1.00 14.34 ? 343 ASN A O 1 ATOM 5151 C CB . ASN A 1 335 ? -2.276 16.596 3.472 1.00 15.22 ? 343 ASN A CB 1 ATOM 5152 C CG . ASN A 1 335 ? -2.214 17.941 2.799 1.00 18.75 ? 343 ASN A CG 1 ATOM 5153 O OD1 . ASN A 1 335 ? -2.699 18.933 3.328 1.00 19.84 ? 343 ASN A OD1 1 ATOM 5154 N ND2 . ASN A 1 335 ? -1.640 17.978 1.613 1.00 23.95 ? 343 ASN A ND2 1 ATOM 5155 H H . ASN A 1 335 ? -2.819 14.721 4.976 1.00 15.98 ? 343 ASN A H 1 ATOM 5156 H HA . ASN A 1 335 ? -2.021 17.243 5.399 1.00 16.57 ? 343 ASN A HA 1 ATOM 5157 H HB2 . ASN A 1 335 ? -1.398 16.188 3.409 1.00 18.26 ? 343 ASN A HB2 1 ATOM 5158 H HB3 . ASN A 1 335 ? -2.929 16.054 3.002 1.00 18.26 ? 343 ASN A HB3 1 ATOM 5159 H HD21 . ASN A 1 335 ? -1.580 18.723 1.188 1.00 28.75 ? 343 ASN A HD21 1 ATOM 5160 H HD22 . ASN A 1 335 ? -1.326 17.257 1.265 1.00 28.75 ? 343 ASN A HD22 1 ATOM 5161 N N . LEU A 1 336 ? -4.188 18.167 6.121 1.00 12.89 ? 344 LEU A N 1 ATOM 5162 C CA . LEU A 1 336 ? -5.500 18.577 6.584 1.00 15.06 ? 344 LEU A CA 1 ATOM 5163 C C . LEU A 1 336 ? -6.235 19.362 5.517 1.00 15.21 ? 344 LEU A C 1 ATOM 5164 O O . LEU A 1 336 ? -7.433 19.155 5.303 1.00 17.46 ? 344 LEU A O 1 ATOM 5165 C CB . LEU A 1 336 ? -5.382 19.348 7.906 1.00 16.57 ? 344 LEU A CB 1 ATOM 5166 C CG . LEU A 1 336 ? -6.667 19.759 8.598 1.00 16.74 ? 344 LEU A CG 1 ATOM 5167 C CD1 . LEU A 1 336 ? -7.516 18.541 8.950 1.00 18.96 ? 344 LEU A CD1 1 ATOM 5168 C CD2 . LEU A 1 336 ? -6.310 20.550 9.822 1.00 17.82 ? 344 LEU A CD2 1 ATOM 5169 H H . LEU A 1 336 ? -3.534 18.516 6.557 1.00 15.47 ? 344 LEU A H 1 ATOM 5170 H HA . LEU A 1 336 ? -6.021 17.779 6.762 1.00 18.07 ? 344 LEU A HA 1 ATOM 5171 H HB2 . LEU A 1 336 ? -4.888 18.795 8.531 1.00 19.88 ? 344 LEU A HB2 1 ATOM 5172 H HB3 . LEU A 1 336 ? -4.881 20.160 7.735 1.00 19.88 ? 344 LEU A HB3 1 ATOM 5173 H HG . LEU A 1 336 ? -7.182 20.329 8.006 1.00 20.09 ? 344 LEU A HG 1 ATOM 5174 H HD11 . LEU A 1 336 ? -8.328 18.839 9.390 1.00 22.76 ? 344 LEU A HD11 1 ATOM 5175 H HD12 . LEU A 1 336 ? -7.738 18.064 8.135 1.00 22.76 ? 344 LEU A HD12 1 ATOM 5176 H HD13 . LEU A 1 336 ? -7.010 17.965 9.544 1.00 22.76 ? 344 LEU A HD13 1 ATOM 5177 H HD21 . LEU A 1 336 ? -7.126 20.818 10.273 1.00 21.39 ? 344 LEU A HD21 1 ATOM 5178 H HD22 . LEU A 1 336 ? -5.773 19.996 10.410 1.00 21.39 ? 344 LEU A HD22 1 ATOM 5179 H HD23 . LEU A 1 336 ? -5.806 21.335 9.555 1.00 21.39 ? 344 LEU A HD23 1 ATOM 5180 N N . ARG A 1 337 ? -5.525 20.222 4.798 1.00 16.02 ? 345 ARG A N 1 ATOM 5181 C CA . ARG A 1 337 ? -6.147 21.001 3.732 1.00 20.78 ? 345 ARG A CA 1 ATOM 5182 C C . ARG A 1 337 ? -6.759 20.094 2.677 1.00 18.41 ? 345 ARG A C 1 ATOM 5183 O O . ARG A 1 337 ? -7.857 20.366 2.183 1.00 21.14 ? 345 ARG A O 1 ATOM 5184 C CB . ARG A 1 337 ? -5.089 21.909 3.103 1.00 25.83 ? 345 ARG A CB 1 ATOM 5185 C CG . ARG A 1 337 ? -5.651 23.025 2.236 1.00 31.50 ? 345 ARG A CG 1 ATOM 5186 C CD . ARG A 1 337 ? -4.516 23.863 1.628 1.00 36.10 ? 345 ARG A CD 1 ATOM 5187 N NE . ARG A 1 337 ? -3.360 24.018 2.526 1.00 41.76 ? 345 ARG A NE 1 ATOM 5188 C CZ . ARG A 1 337 ? -3.257 24.940 3.482 1.00 45.09 ? 345 ARG A CZ 1 ATOM 5189 N NH1 . ARG A 1 337 ? -4.250 25.796 3.709 1.00 46.18 ? 345 ARG A NH1 1 ATOM 5190 N NH2 . ARG A 1 337 ? -2.160 25.000 4.229 1.00 46.88 ? 345 ARG A NH2 1 ATOM 5191 H H . ARG A 1 337 ? -4.685 20.374 4.905 1.00 19.23 ? 345 ARG A H 1 ATOM 5192 H HA . ARG A 1 337 ? -6.849 21.557 4.104 1.00 24.94 ? 345 ARG A HA 1 ATOM 5193 H HB2 . ARG A 1 337 ? -4.572 22.320 3.813 1.00 30.99 ? 345 ARG A HB2 1 ATOM 5194 H HB3 . ARG A 1 337 ? -4.508 21.368 2.546 1.00 30.99 ? 345 ARG A HB3 1 ATOM 5195 H HG2 . ARG A 1 337 ? -6.170 22.641 1.513 1.00 37.80 ? 345 ARG A HG2 1 ATOM 5196 H HG3 . ARG A 1 337 ? -6.205 23.608 2.779 1.00 37.80 ? 345 ARG A HG3 1 ATOM 5197 H HD2 . ARG A 1 337 ? -4.208 23.431 0.816 1.00 43.32 ? 345 ARG A HD2 1 ATOM 5198 H HD3 . ARG A 1 337 ? -4.855 24.748 1.422 1.00 43.32 ? 345 ARG A HD3 1 ATOM 5199 H HE . ARG A 1 337 ? -2.702 23.473 2.425 1.00 50.11 ? 345 ARG A HE 1 ATOM 5200 H HH11 . ARG A 1 337 ? -4.963 25.766 3.228 1.00 55.41 ? 345 ARG A HH11 1 ATOM 5201 H HH12 . ARG A 1 337 ? -4.177 26.386 4.331 1.00 55.41 ? 345 ARG A HH12 1 ATOM 5202 H HH21 . ARG A 1 337 ? -1.516 24.447 4.092 1.00 56.25 ? 345 ARG A HH21 1 ATOM 5203 H HH22 . ARG A 1 337 ? -2.097 25.589 4.852 1.00 56.25 ? 345 ARG A HH22 1 ATOM 5204 N N . GLN A 1 338 ? -6.077 19.005 2.313 1.00 16.77 ? 346 GLN A N 1 ATOM 5205 C CA . GLN A 1 338 ? -6.620 18.066 1.339 1.00 17.01 ? 346 GLN A CA 1 ATOM 5206 C C . GLN A 1 338 ? -7.733 17.207 1.943 1.00 15.73 ? 346 GLN A C 1 ATOM 5207 O O . GLN A 1 338 ? -8.786 16.996 1.332 1.00 16.87 ? 346 GLN A O 1 ATOM 5208 C CB . GLN A 1 338 ? -5.476 17.183 0.875 1.00 17.37 ? 346 GLN A CB 1 ATOM 5209 C CG . GLN A 1 338 ? -5.822 16.221 -0.236 1.00 18.69 ? 346 GLN A CG 1 ATOM 5210 C CD . GLN A 1 338 ? -5.887 16.898 -1.620 1.00 19.85 ? 346 GLN A CD 1 ATOM 5211 O OE1 . GLN A 1 338 ? -5.730 18.114 -1.750 1.00 22.65 ? 346 GLN A OE1 1 ATOM 5212 N NE2 . GLN A 1 338 ? -6.100 16.099 -2.656 1.00 19.65 ? 346 GLN A NE2 1 ATOM 5213 H H . GLN A 1 338 ? -5.301 18.792 2.616 1.00 20.13 ? 346 GLN A H 1 ATOM 5214 H HA . GLN A 1 338 ? -6.974 18.549 0.576 1.00 20.41 ? 346 GLN A HA 1 ATOM 5215 H HB2 . GLN A 1 338 ? -4.757 17.750 0.557 1.00 20.85 ? 346 GLN A HB2 1 ATOM 5216 H HB3 . GLN A 1 338 ? -5.166 16.658 1.630 1.00 20.85 ? 346 GLN A HB3 1 ATOM 5217 H HG2 . GLN A 1 338 ? -5.147 15.527 -0.274 1.00 22.42 ? 346 GLN A HG2 1 ATOM 5218 H HG3 . GLN A 1 338 ? -6.691 15.829 -0.055 1.00 22.42 ? 346 GLN A HG3 1 ATOM 5219 H HE21 . GLN A 1 338 ? -6.195 15.253 -2.534 1.00 23.58 ? 346 GLN A HE21 1 ATOM 5220 H HE22 . GLN A 1 338 ? -6.145 16.427 -3.449 1.00 23.58 ? 346 GLN A HE22 1 ATOM 5221 N N . ALA A 1 339 ? -7.524 16.716 3.163 1.00 14.96 ? 347 ALA A N 1 ATOM 5222 C CA . ALA A 1 339 ? -8.495 15.826 3.778 1.00 15.84 ? 347 ALA A CA 1 ATOM 5223 C C . ALA A 1 339 ? -9.847 16.491 3.883 1.00 14.48 ? 347 ALA A C 1 ATOM 5224 O O . ALA A 1 339 ? -10.883 15.839 3.710 1.00 15.03 ? 347 ALA A O 1 ATOM 5225 C CB . ALA A 1 339 ? -7.998 15.415 5.158 1.00 18.20 ? 347 ALA A CB 1 ATOM 5226 H H . ALA A 1 339 ? -6.833 16.883 3.649 1.00 17.95 ? 347 ALA A H 1 ATOM 5227 H HA . ALA A 1 339 ? -8.589 15.028 3.236 1.00 19.01 ? 347 ALA A HA 1 ATOM 5228 H HB1 . ALA A 1 339 ? -8.650 14.822 5.564 1.00 21.84 ? 347 ALA A HB1 1 ATOM 5229 H HB2 . ALA A 1 339 ? -7.148 14.958 5.064 1.00 21.84 ? 347 ALA A HB2 1 ATOM 5230 H HB3 . ALA A 1 339 ? -7.888 16.209 5.704 1.00 21.84 ? 347 ALA A HB3 1 ATOM 5231 N N . ASN A 1 340 ? -9.858 17.796 4.148 1.00 14.92 ? 348 ASN A N 1 ATOM 5232 C CA . ASN A 1 340 ? -11.120 18.490 4.350 1.00 15.69 ? 348 ASN A CA 1 ATOM 5233 C C . ASN A 1 340 ? -11.936 18.666 3.085 1.00 16.60 ? 348 ASN A C 1 ATOM 5234 O O . ASN A 1 340 ? -13.100 19.056 3.200 1.00 19.49 ? 348 ASN A O 1 ATOM 5235 C CB . ASN A 1 340 ? -10.899 19.828 5.026 1.00 15.94 ? 348 ASN A CB 1 ATOM 5236 C CG . ASN A 1 340 ? -10.859 19.695 6.533 1.00 16.08 ? 348 ASN A CG 1 ATOM 5237 O OD1 . ASN A 1 340 ? -11.539 18.863 7.116 1.00 18.05 ? 348 ASN A OD1 1 ATOM 5238 N ND2 . ASN A 1 340 ? -10.040 20.493 7.166 1.00 17.51 ? 348 ASN A ND2 1 ATOM 5239 H H . ASN A 1 340 ? -9.158 18.292 4.214 1.00 17.90 ? 348 ASN A H 1 ATOM 5240 H HA . ASN A 1 340 ? -11.656 17.955 4.956 1.00 18.83 ? 348 ASN A HA 1 ATOM 5241 H HB2 . ASN A 1 340 ? -10.052 20.198 4.732 1.00 19.13 ? 348 ASN A HB2 1 ATOM 5242 H HB3 . ASN A 1 340 ? -11.626 20.427 4.793 1.00 19.13 ? 348 ASN A HB3 1 ATOM 5243 H HD21 . ASN A 1 340 ? -9.981 20.456 8.023 1.00 21.01 ? 348 ASN A HD21 1 ATOM 5244 H HD22 . ASN A 1 340 ? -9.561 21.055 6.725 1.00 21.01 ? 348 ASN A HD22 1 ATOM 5245 N N . VAL A 1 341 ? -11.405 18.350 1.902 1.00 16.12 ? 349 VAL A N 1 ATOM 5246 C CA . VAL A 1 341 ? -12.254 18.297 0.710 1.00 17.22 ? 349 VAL A CA 1 ATOM 5247 C C . VAL A 1 341 ? -12.603 16.866 0.311 1.00 17.82 ? 349 VAL A C 1 ATOM 5248 O O . VAL A 1 341 ? -13.149 16.664 -0.764 1.00 19.82 ? 349 VAL A O 1 ATOM 5249 C CB . VAL A 1 341 ? -11.711 19.108 -0.477 1.00 19.63 ? 349 VAL A CB 1 ATOM 5250 C CG1 . VAL A 1 341 ? -11.465 20.545 -0.089 1.00 21.18 ? 349 VAL A CG1 1 ATOM 5251 C CG2 . VAL A 1 341 ? -10.480 18.461 -1.056 1.00 21.11 ? 349 VAL A CG2 1 ATOM 5252 H H . VAL A 1 341 ? -10.577 18.166 1.764 1.00 19.34 ? 349 VAL A H 1 ATOM 5253 H HA . VAL A 1 341 ? -13.096 18.716 0.950 1.00 20.67 ? 349 VAL A HA 1 ATOM 5254 H HB . VAL A 1 341 ? -12.386 19.113 -1.174 1.00 23.56 ? 349 VAL A HB 1 ATOM 5255 H HG11 . VAL A 1 341 ? -11.124 21.026 -0.859 1.00 25.41 ? 349 VAL A HG11 1 ATOM 5256 H HG12 . VAL A 1 341 ? -12.301 20.940 0.205 1.00 25.41 ? 349 VAL A HG12 1 ATOM 5257 H HG13 . VAL A 1 341 ? -10.815 20.570 0.632 1.00 25.41 ? 349 VAL A HG13 1 ATOM 5258 H HG21 . VAL A 1 341 ? -10.163 18.996 -1.801 1.00 25.33 ? 349 VAL A HG21 1 ATOM 5259 H HG22 . VAL A 1 341 ? -9.797 18.412 -0.369 1.00 25.33 ? 349 VAL A HG22 1 ATOM 5260 H HG23 . VAL A 1 341 ? -10.707 17.569 -1.362 1.00 25.33 ? 349 VAL A HG23 1 ATOM 5261 N N . GLN A 1 342 ? -12.339 15.879 1.159 1.00 17.64 ? 350 GLN A N 1 ATOM 5262 C CA . GLN A 1 342 ? -12.540 14.477 0.826 1.00 18.47 ? 350 GLN A CA 1 ATOM 5263 C C . GLN A 1 342 ? -13.494 13.802 1.801 1.00 18.85 ? 350 GLN A C 1 ATOM 5264 O O . GLN A 1 342 ? -13.718 14.285 2.912 1.00 20.19 ? 350 GLN A O 1 ATOM 5265 C CB . GLN A 1 342 ? -11.207 13.736 0.852 1.00 18.81 ? 350 GLN A CB 1 ATOM 5266 C CG . GLN A 1 342 ? -10.222 14.348 -0.118 1.00 19.62 ? 350 GLN A CG 1 ATOM 5267 C CD . GLN A 1 342 ? -8.949 13.578 -0.248 1.00 22.83 ? 350 GLN A CD 1 ATOM 5268 O OE1 . GLN A 1 342 ? -8.288 13.254 0.750 1.00 26.41 ? 350 GLN A OE1 1 ATOM 5269 N NE2 . GLN A 1 342 ? -8.564 13.305 -1.486 1.00 25.27 ? 350 GLN A NE2 1 ATOM 5270 H H . GLN A 1 342 ? -12.034 16.002 1.953 1.00 21.17 ? 350 GLN A H 1 ATOM 5271 H HA . GLN A 1 342 ? -12.913 14.407 -0.067 1.00 22.16 ? 350 GLN A HA 1 ATOM 5272 H HB2 . GLN A 1 342 ? -10.828 13.787 1.744 1.00 22.57 ? 350 GLN A HB2 1 ATOM 5273 H HB3 . GLN A 1 342 ? -11.349 12.811 0.599 1.00 22.57 ? 350 GLN A HB3 1 ATOM 5274 H HG2 . GLN A 1 342 ? -10.633 14.392 -0.996 1.00 23.54 ? 350 GLN A HG2 1 ATOM 5275 H HG3 . GLN A 1 342 ? -9.998 15.242 0.185 1.00 23.54 ? 350 GLN A HG3 1 ATOM 5276 H HE21 . GLN A 1 342 ? -9.039 13.569 -2.152 1.00 30.32 ? 350 GLN A HE21 1 ATOM 5277 H HE22 . GLN A 1 342 ? -7.839 12.864 -1.623 1.00 30.32 ? 350 GLN A HE22 1 ATOM 5278 N N . GLU A 1 343 ? -14.050 12.668 1.356 1.00 21.71 ? 351 GLU A N 1 ATOM 5279 C CA . GLU A 1 343 ? -15.064 11.948 2.115 1.00 23.40 ? 351 GLU A CA 1 ATOM 5280 C C . GLU A 1 343 ? -14.491 11.254 3.330 1.00 24.31 ? 351 GLU A C 1 ATOM 5281 O O . GLU A 1 343 ? -15.185 11.113 4.344 1.00 27.55 ? 351 GLU A O 1 ATOM 5282 C CB . GLU A 1 343 ? -15.695 10.867 1.243 1.00 26.64 ? 351 GLU A CB 1 ATOM 5283 C CG . GLU A 1 343 ? -16.569 11.364 0.152 1.00 29.56 ? 351 GLU A CG 1 ATOM 5284 C CD . GLU A 1 343 ? -17.961 11.768 0.635 1.00 31.61 ? 351 GLU A CD 1 ATOM 5285 O OE1 . GLU A 1 343 ? -18.520 11.120 1.556 1.00 33.98 ? 351 GLU A OE1 1 ATOM 5286 O OE2 . GLU A 1 343 ? -18.505 12.735 0.062 1.00 31.75 ? 351 GLU A OE2 1 ATOM 5287 H H . GLU A 1 343 ? -13.849 12.296 0.607 1.00 26.06 ? 351 GLU A H 1 ATOM 5288 H HA . GLU A 1 343 ? -15.757 12.562 2.403 1.00 28.08 ? 351 GLU A HA 1 ATOM 5289 H HB2 . GLU A 1 343 ? -14.985 10.348 0.834 1.00 31.96 ? 351 GLU A HB2 1 ATOM 5290 H HB3 . GLU A 1 343 ? -16.233 10.291 1.808 1.00 31.96 ? 351 GLU A HB3 1 ATOM 5291 H HG2 . GLU A 1 343 ? -16.156 12.143 -0.253 1.00 35.47 ? 351 GLU A HG2 1 ATOM 5292 H HG3 . GLU A 1 343 ? -16.675 10.664 -0.511 1.00 35.47 ? 351 GLU A HG3 1 ATOM 5293 N N . THR A 1 344 ? -13.269 10.743 3.229 1.00 26.99 ? 352 THR A N 1 ATOM 5294 C CA . THR A 1 344 ? -12.619 10.078 4.340 1.00 29.91 ? 352 THR A CA 1 ATOM 5295 C C . THR A 1 344 ? -11.201 10.619 4.453 1.00 29.41 ? 352 THR A C 1 ATOM 5296 O O . THR A 1 344 ? -10.531 10.774 3.440 1.00 28.54 ? 352 THR A O 1 ATOM 5297 C CB . THR A 1 344 ? -12.546 8.567 4.076 1.00 33.11 ? 352 THR A CB 1 ATOM 5298 O OG1 . THR A 1 344 ? -13.816 8.077 3.627 1.00 36.21 ? 352 THR A OG1 1 ATOM 5299 C CG2 . THR A 1 344 ? -12.176 7.845 5.335 1.00 35.43 ? 352 THR A CG2 1 ATOM 5300 H H . THR A 1 344 ? -12.791 10.773 2.514 1.00 32.39 ? 352 THR A H 1 ATOM 5301 H HA . THR A 1 344 ? -13.099 10.242 5.167 1.00 35.89 ? 352 THR A HA 1 ATOM 5302 H HB . THR A 1 344 ? -11.870 8.385 3.404 1.00 39.73 ? 352 THR A HB 1 ATOM 5303 H HG1 . THR A 1 344 ? -13.772 7.251 3.484 1.00 43.46 ? 352 THR A HG1 1 ATOM 5304 H HG21 . THR A 1 344 ? -12.130 6.890 5.168 1.00 42.52 ? 352 THR A HG21 1 ATOM 5305 H HG22 . THR A 1 344 ? -11.313 8.152 5.653 1.00 42.52 ? 352 THR A HG22 1 ATOM 5306 H HG23 . THR A 1 344 ? -12.842 8.012 6.021 1.00 42.52 ? 352 THR A HG23 1 ATOM 5307 N N . PRO A 1 345 ? -10.696 10.884 5.654 1.00 29.86 ? 353 PRO A N 1 ATOM 5308 C CA . PRO A 1 345 ? -9.287 11.287 5.753 1.00 30.63 ? 353 PRO A CA 1 ATOM 5309 C C . PRO A 1 345 ? -8.394 10.072 5.526 1.00 32.12 ? 353 PRO A C 1 ATOM 5310 O O . PRO A 1 345 ? -8.632 9.000 6.095 1.00 34.47 ? 353 PRO A O 1 ATOM 5311 C CB . PRO A 1 345 ? -9.171 11.833 7.182 1.00 34.03 ? 353 PRO A CB 1 ATOM 5312 C CG . PRO A 1 345 ? -10.254 11.121 7.951 1.00 33.77 ? 353 PRO A CG 1 ATOM 5313 C CD . PRO A 1 345 ? -11.325 10.719 6.979 1.00 31.25 ? 353 PRO A CD 1 ATOM 5314 H HA . PRO A 1 345 ? -9.076 11.983 5.111 1.00 36.75 ? 353 PRO A HA 1 ATOM 5315 H HB2 . PRO A 1 345 ? -8.296 11.622 7.544 1.00 40.84 ? 353 PRO A HB2 1 ATOM 5316 H HB3 . PRO A 1 345 ? -9.322 12.791 7.180 1.00 40.84 ? 353 PRO A HB3 1 ATOM 5317 H HG2 . PRO A 1 345 ? -9.877 10.335 8.378 1.00 40.52 ? 353 PRO A HG2 1 ATOM 5318 H HG3 . PRO A 1 345 ? -10.617 11.722 8.620 1.00 40.52 ? 353 PRO A HG3 1 ATOM 5319 H HD2 . PRO A 1 345 ? -11.575 9.792 7.119 1.00 37.50 ? 353 PRO A HD2 1 ATOM 5320 H HD3 . PRO A 1 345 ? -12.092 11.307 7.062 1.00 37.50 ? 353 PRO A HD3 1 ATOM 5321 N N . ARG A 1 346 ? -7.384 10.225 4.664 1.00 28.87 ? 354 ARG A N 1 ATOM 5322 C CA . ARG A 1 346 ? -6.402 9.162 4.447 1.00 27.25 ? 354 ARG A CA 1 ATOM 5323 C C . ARG A 1 346 ? -4.995 9.632 4.792 1.00 21.54 ? 354 ARG A C 1 ATOM 5324 O O . ARG A 1 346 ? -4.463 10.566 4.181 1.00 19.92 ? 354 ARG A O 1 ATOM 5325 C CB . ARG A 1 346 ? -6.497 8.598 3.040 1.00 34.11 ? 354 ARG A CB 1 ATOM 5326 C CG . ARG A 1 346 ? -7.789 7.782 2.920 1.00 38.88 ? 354 ARG A CG 1 ATOM 5327 C CD . ARG A 1 346 ? -8.092 7.269 1.541 1.00 44.73 ? 354 ARG A CD 1 ATOM 5328 N NE . ARG A 1 346 ? -9.323 6.477 1.561 1.00 48.88 ? 354 ARG A NE 1 ATOM 5329 C CZ . ARG A 1 346 ? -10.209 6.429 0.570 1.00 52.15 ? 354 ARG A CZ 1 ATOM 5330 N NH1 . ARG A 1 346 ? -10.017 7.137 -0.533 1.00 52.88 ? 354 ARG A NH1 1 ATOM 5331 N NH2 . ARG A 1 346 ? -11.298 5.675 0.690 1.00 53.26 ? 354 ARG A NH2 1 ATOM 5332 H H . ARG A 1 346 ? -7.247 10.933 4.195 1.00 34.64 ? 354 ARG A H 1 ATOM 5333 H HA . ARG A 1 346 ? -6.612 8.436 5.055 1.00 32.70 ? 354 ARG A HA 1 ATOM 5334 H HB2 . ARG A 1 346 ? -6.524 9.323 2.396 1.00 40.94 ? 354 ARG A HB2 1 ATOM 5335 H HB3 . ARG A 1 346 ? -5.741 8.013 2.869 1.00 40.94 ? 354 ARG A HB3 1 ATOM 5336 H HG2 . ARG A 1 346 ? -7.725 7.014 3.509 1.00 46.66 ? 354 ARG A HG2 1 ATOM 5337 H HG3 . ARG A 1 346 ? -8.533 8.341 3.194 1.00 46.66 ? 354 ARG A HG3 1 ATOM 5338 H HD2 . ARG A 1 346 ? -8.216 8.017 0.936 1.00 53.68 ? 354 ARG A HD2 1 ATOM 5339 H HD3 . ARG A 1 346 ? -7.366 6.703 1.237 1.00 53.68 ? 354 ARG A HD3 1 ATOM 5340 H HE . ARG A 1 346 ? -9.486 6.010 2.265 1.00 58.65 ? 354 ARG A HE 1 ATOM 5341 H HH11 . ARG A 1 346 ? -9.314 7.626 -0.613 1.00 63.46 ? 354 ARG A HH11 1 ATOM 5342 H HH12 . ARG A 1 346 ? -10.593 7.104 -1.171 1.00 63.46 ? 354 ARG A HH12 1 ATOM 5343 H HH21 . ARG A 1 346 ? -11.426 5.215 1.405 1.00 63.92 ? 354 ARG A HH21 1 ATOM 5344 H HH22 . ARG A 1 346 ? -11.872 5.645 0.051 1.00 63.92 ? 354 ARG A HH22 1 ATOM 5345 N N . TRP A 1 347 ? -4.402 8.975 5.772 1.00 19.15 ? 355 TRP A N 1 ATOM 5346 C CA . TRP A 1 347 ? -3.067 9.306 6.228 1.00 16.29 ? 355 TRP A CA 1 ATOM 5347 C C . TRP A 1 347 ? -2.036 8.720 5.272 1.00 16.99 ? 355 TRP A C 1 ATOM 5348 O O . TRP A 1 347 ? -2.296 7.738 4.570 1.00 19.30 ? 355 TRP A O 1 ATOM 5349 C CB . TRP A 1 347 ? -2.888 8.748 7.639 1.00 16.02 ? 355 TRP A CB 1 ATOM 5350 C CG . TRP A 1 347 ? -3.755 9.435 8.662 1.00 14.40 ? 355 TRP A CG 1 ATOM 5351 C CD1 . TRP A 1 347 ? -5.123 9.401 8.749 1.00 17.53 ? 355 TRP A CD1 1 ATOM 5352 C CD2 . TRP A 1 347 ? -3.308 10.227 9.769 1.00 14.61 ? 355 TRP A CD2 1 ATOM 5353 N NE1 . TRP A 1 347 ? -5.547 10.157 9.820 1.00 16.91 ? 355 TRP A NE1 1 ATOM 5354 C CE2 . TRP A 1 347 ? -4.452 10.665 10.468 1.00 16.30 ? 355 TRP A CE2 1 ATOM 5355 C CE3 . TRP A 1 347 ? -2.057 10.626 10.219 1.00 15.03 ? 355 TRP A CE3 1 ATOM 5356 C CZ2 . TRP A 1 347 ? -4.371 11.498 11.586 1.00 16.93 ? 355 TRP A CZ2 1 ATOM 5357 C CZ3 . TRP A 1 347 ? -1.976 11.448 11.331 1.00 15.72 ? 355 TRP A CZ3 1 ATOM 5358 C CH2 . TRP A 1 347 ? -3.117 11.855 12.009 1.00 16.70 ? 355 TRP A CH2 1 ATOM 5359 H H . TRP A 1 347 ? -4.760 8.319 6.198 1.00 22.98 ? 355 TRP A H 1 ATOM 5360 H HA . TRP A 1 347 ? -2.958 10.269 6.256 1.00 19.55 ? 355 TRP A HA 1 ATOM 5361 H HB2 . TRP A 1 347 ? -3.118 7.806 7.637 1.00 19.22 ? 355 TRP A HB2 1 ATOM 5362 H HB3 . TRP A 1 347 ? -1.963 8.862 7.907 1.00 19.22 ? 355 TRP A HB3 1 ATOM 5363 H HD1 . TRP A 1 347 ? -5.684 8.951 8.160 1.00 21.04 ? 355 TRP A HD1 1 ATOM 5364 H HE1 . TRP A 1 347 ? -6.366 10.273 10.056 1.00 20.30 ? 355 TRP A HE1 1 ATOM 5365 H HE3 . TRP A 1 347 ? -1.287 10.361 9.770 1.00 18.03 ? 355 TRP A HE3 1 ATOM 5366 H HZ2 . TRP A 1 347 ? -5.133 11.771 12.044 1.00 20.32 ? 355 TRP A HZ2 1 ATOM 5367 H HZ3 . TRP A 1 347 ? -1.141 11.712 11.644 1.00 18.86 ? 355 TRP A HZ3 1 ATOM 5368 H HH2 . TRP A 1 347 ? -3.030 12.401 12.756 1.00 20.04 ? 355 TRP A HH2 1 ATOM 5369 N N . GLU A 1 348 ? -0.878 9.361 5.199 1.00 15.83 ? 356 GLU A N 1 ATOM 5370 C CA . GLU A 1 348 ? 0.173 8.930 4.296 1.00 16.14 ? 356 GLU A CA 1 ATOM 5371 C C . GLU A 1 348 ? 1.514 9.038 4.998 1.00 15.54 ? 356 GLU A C 1 ATOM 5372 O O . GLU A 1 348 ? 1.661 9.756 5.980 1.00 15.04 ? 356 GLU A O 1 ATOM 5373 C CB . GLU A 1 348 ? 0.241 9.789 3.045 1.00 21.69 ? 356 GLU A CB 1 ATOM 5374 C CG . GLU A 1 348 ? 0.313 11.259 3.311 1.00 27.90 ? 356 GLU A CG 1 ATOM 5375 C CD . GLU A 1 348 ? -0.001 12.080 2.064 1.00 33.07 ? 356 GLU A CD 1 ATOM 5376 O OE1 . GLU A 1 348 ? 0.737 11.953 1.066 1.00 36.84 ? 356 GLU A OE1 1 ATOM 5377 O OE2 . GLU A 1 348 ? -0.998 12.839 2.059 1.00 34.29 ? 356 GLU A OE2 1 ATOM 5378 H H . GLU A 1 348 ? -0.677 10.055 5.666 1.00 19.00 ? 356 GLU A H 1 ATOM 5379 H HA . GLU A 1 348 ? 0.027 8.007 4.036 1.00 19.37 ? 356 GLU A HA 1 ATOM 5380 H HB2 . GLU A 1 348 ? 1.033 9.542 2.541 1.00 26.03 ? 356 GLU A HB2 1 ATOM 5381 H HB3 . GLU A 1 348 ? -0.551 9.624 2.510 1.00 26.03 ? 356 GLU A HB3 1 ATOM 5382 H HG2 . GLU A 1 348 ? -0.334 11.490 3.996 1.00 33.48 ? 356 GLU A HG2 1 ATOM 5383 H HG3 . GLU A 1 348 ? 1.208 11.486 3.606 1.00 33.48 ? 356 GLU A HG3 1 ATOM 5384 N N . GLN A 1 349 ? 2.496 8.327 4.468 1.00 14.47 ? 357 GLN A N 1 ATOM 5385 C CA . GLN A 1 349 ? 3.850 8.443 4.969 1.00 13.95 ? 357 GLN A CA 1 ATOM 5386 C C . GLN A 1 349 ? 4.395 9.827 4.664 1.00 14.13 ? 357 GLN A C 1 ATOM 5387 O O . GLN A 1 349 ? 4.327 10.302 3.531 1.00 16.20 ? 357 GLN A O 1 ATOM 5388 C CB . GLN A 1 349 ? 4.731 7.387 4.325 1.00 15.06 ? 357 GLN A CB 1 ATOM 5389 C CG . GLN A 1 349 ? 6.168 7.511 4.778 1.00 16.61 ? 357 GLN A CG 1 ATOM 5390 C CD . GLN A 1 349 ? 7.037 6.326 4.406 1.00 19.58 ? 357 GLN A CD 1 ATOM 5391 O OE1 . GLN A 1 349 ? 6.702 5.182 4.664 1.00 22.03 ? 357 GLN A OE1 1 ATOM 5392 N NE2 . GLN A 1 349 ? 8.178 6.612 3.816 1.00 24.12 ? 357 GLN A NE2 1 ATOM 5393 H H . GLN A 1 349 ? 2.404 7.771 3.818 1.00 17.37 ? 357 GLN A H 1 ATOM 5394 H HA . GLN A 1 349 ? 3.856 8.311 5.930 1.00 16.73 ? 357 GLN A HA 1 ATOM 5395 H HB2 . GLN A 1 349 ? 4.409 6.507 4.574 1.00 18.07 ? 357 GLN A HB2 1 ATOM 5396 H HB3 . GLN A 1 349 ? 4.706 7.494 3.361 1.00 18.07 ? 357 GLN A HB3 1 ATOM 5397 H HG2 . GLN A 1 349 ? 6.556 8.301 4.371 1.00 19.94 ? 357 GLN A HG2 1 ATOM 5398 H HG3 . GLN A 1 349 ? 6.185 7.597 5.744 1.00 19.94 ? 357 GLN A HG3 1 ATOM 5399 H HE21 . GLN A 1 349 ? 8.390 7.432 3.663 1.00 28.95 ? 357 GLN A HE21 1 ATOM 5400 H HE22 . GLN A 1 349 ? 8.711 5.980 3.582 1.00 28.95 ? 357 GLN A HE22 1 ATOM 5401 N N . GLU A 1 350 ? 4.930 10.492 5.680 1.00 13.41 ? 358 GLU A N 1 ATOM 5402 C CA . GLU A 1 350 ? 5.632 11.746 5.473 1.00 12.63 ? 358 GLU A CA 1 ATOM 5403 C C . GLU A 1 350 ? 7.086 11.472 5.117 1.00 12.92 ? 358 GLU A C 1 ATOM 5404 O O . GLU A 1 350 ? 7.562 11.910 4.058 1.00 14.99 ? 358 GLU A O 1 ATOM 5405 C CB . GLU A 1 350 ? 5.522 12.633 6.713 1.00 13.28 ? 358 GLU A CB 1 ATOM 5406 C CG . GLU A 1 350 ? 5.982 14.044 6.434 1.00 13.56 ? 358 GLU A CG 1 ATOM 5407 C CD . GLU A 1 350 ? 6.204 14.846 7.684 1.00 12.66 ? 358 GLU A CD 1 ATOM 5408 O OE1 . GLU A 1 350 ? 6.422 14.233 8.759 1.00 12.95 ? 358 GLU A OE1 1 ATOM 5409 O OE2 . GLU A 1 350 ? 6.176 16.102 7.619 1.00 12.54 ? 358 GLU A OE2 1 ATOM 5410 H H . GLU A 1 350 ? 4.900 10.236 6.501 1.00 16.10 ? 358 GLU A H 1 ATOM 5411 H HA . GLU A 1 350 ? 5.225 12.217 4.730 1.00 15.15 ? 358 GLU A HA 1 ATOM 5412 H HB2 . GLU A 1 350 ? 4.595 12.667 6.999 1.00 15.94 ? 358 GLU A HB2 1 ATOM 5413 H HB3 . GLU A 1 350 ? 6.077 12.266 7.418 1.00 15.94 ? 358 GLU A HB3 1 ATOM 5414 H HG2 . GLU A 1 350 ? 6.820 14.012 5.947 1.00 16.27 ? 358 GLU A HG2 1 ATOM 5415 H HG3 . GLU A 1 350 ? 5.308 14.497 5.904 1.00 16.27 ? 358 GLU A HG3 1 ATOM 5416 N N . TYR A 1 351 ? 7.806 10.762 5.992 1.00 12.75 ? 359 TYR A N 1 ATOM 5417 C CA . TYR A 1 351 ? 9.182 10.405 5.691 1.00 12.28 ? 359 TYR A CA 1 ATOM 5418 C C . TYR A 1 351 ? 9.638 9.274 6.588 1.00 12.33 ? 359 TYR A C 1 ATOM 5419 O O . TYR A 1 351 ? 9.059 9.007 7.643 1.00 12.82 ? 359 TYR A O 1 ATOM 5420 C CB . TYR A 1 351 ? 10.124 11.597 5.872 1.00 13.91 ? 359 TYR A CB 1 ATOM 5421 C CG . TYR A 1 351 ? 10.379 12.005 7.315 1.00 12.78 ? 359 TYR A CG 1 ATOM 5422 C CD1 . TYR A 1 351 ? 9.484 12.791 7.999 1.00 12.44 ? 359 TYR A CD1 1 ATOM 5423 C CD2 . TYR A 1 351 ? 11.560 11.671 7.957 1.00 14.36 ? 359 TYR A CD2 1 ATOM 5424 C CE1 . TYR A 1 351 ? 9.705 13.193 9.295 1.00 11.48 ? 359 TYR A CE1 1 ATOM 5425 C CE2 . TYR A 1 351 ? 11.790 12.075 9.258 1.00 14.03 ? 359 TYR A CE2 1 ATOM 5426 C CZ . TYR A 1 351 ? 10.880 12.856 9.916 1.00 13.46 ? 359 TYR A CZ 1 ATOM 5427 O OH . TYR A 1 351 ? 11.175 13.262 11.195 1.00 14.19 ? 359 TYR A OH 1 ATOM 5428 H H . TYR A 1 351 ? 7.521 10.482 6.754 1.00 15.31 ? 359 TYR A H 1 ATOM 5429 H HA . TYR A 1 351 ? 9.242 10.107 4.770 1.00 14.73 ? 359 TYR A HA 1 ATOM 5430 H HB2 . TYR A 1 351 ? 10.981 11.376 5.476 1.00 16.69 ? 359 TYR A HB2 1 ATOM 5431 H HB3 . TYR A 1 351 ? 9.743 12.363 5.415 1.00 16.69 ? 359 TYR A HB3 1 ATOM 5432 H HD1 . TYR A 1 351 ? 8.690 13.036 7.581 1.00 14.92 ? 359 TYR A HD1 1 ATOM 5433 H HD2 . TYR A 1 351 ? 12.193 11.152 7.517 1.00 17.23 ? 359 TYR A HD2 1 ATOM 5434 H HE1 . TYR A 1 351 ? 9.082 13.728 9.732 1.00 13.78 ? 359 TYR A HE1 1 ATOM 5435 H HE2 . TYR A 1 351 ? 12.589 11.846 9.676 1.00 16.84 ? 359 TYR A HE2 1 ATOM 5436 H HH . TYR A 1 351 ? 10.543 13.723 11.503 1.00 17.02 ? 359 TYR A HH 1 ATOM 5437 N N . ARG A 1 352 ? 10.675 8.596 6.113 1.00 13.23 ? 360 ARG A N 1 ATOM 5438 C CA . ARG A 1 352 ? 11.449 7.615 6.860 1.00 13.13 ? 360 ARG A CA 1 ATOM 5439 C C . ARG A 1 352 ? 12.800 8.262 7.177 1.00 12.65 ? 360 ARG A C 1 ATOM 5440 O O . ARG A 1 352 ? 13.476 8.776 6.279 1.00 13.41 ? 360 ARG A O 1 ATOM 5441 C CB . ARG A 1 352 ? 11.594 6.333 6.039 1.00 13.97 ? 360 ARG A CB 1 ATOM 5442 C CG . ARG A 1 352 ? 12.522 5.292 6.647 1.00 13.95 ? 360 ARG A CG 1 ATOM 5443 C CD . ARG A 1 352 ? 12.547 3.991 5.839 1.00 14.77 ? 360 ARG A CD 1 ATOM 5444 N NE . ARG A 1 352 ? 11.341 3.192 6.049 1.00 16.55 ? 360 ARG A NE 1 ATOM 5445 C CZ . ARG A 1 352 ? 11.162 2.340 7.057 1.00 16.66 ? 360 ARG A CZ 1 ATOM 5446 N NH1 . ARG A 1 352 ? 12.114 2.153 7.960 1.00 18.04 ? 360 ARG A NH1 1 ATOM 5447 N NH2 . ARG A 1 352 ? 10.037 1.646 7.151 1.00 18.63 ? 360 ARG A NH2 1 ATOM 5448 H H . ARG A 1 352 ? 10.965 8.695 5.309 1.00 15.88 ? 360 ARG A H 1 ATOM 5449 H HA . ARG A 1 352 ? 10.999 7.405 7.693 1.00 15.76 ? 360 ARG A HA 1 ATOM 5450 H HB2 . ARG A 1 352 ? 10.718 5.926 5.943 1.00 16.76 ? 360 ARG A HB2 1 ATOM 5451 H HB3 . ARG A 1 352 ? 11.944 6.563 5.164 1.00 16.76 ? 360 ARG A HB3 1 ATOM 5452 H HG2 . ARG A 1 352 ? 13.424 5.648 6.673 1.00 16.74 ? 360 ARG A HG2 1 ATOM 5453 H HG3 . ARG A 1 352 ? 12.220 5.084 7.545 1.00 16.74 ? 360 ARG A HG3 1 ATOM 5454 H HD2 . ARG A 1 352 ? 12.608 4.203 4.895 1.00 17.72 ? 360 ARG A HD2 1 ATOM 5455 H HD3 . ARG A 1 352 ? 13.312 3.461 6.113 1.00 17.72 ? 360 ARG A HD3 1 ATOM 5456 H HE . ARG A 1 352 ? 10.701 3.279 5.481 1.00 19.87 ? 360 ARG A HE 1 ATOM 5457 H HH11 . ARG A 1 352 ? 12.851 2.593 7.905 1.00 21.65 ? 360 ARG A HH11 1 ATOM 5458 H HH12 . ARG A 1 352 ? 11.990 1.599 8.606 1.00 21.65 ? 360 ARG A HH12 1 ATOM 5459 H HH21 . ARG A 1 352 ? 9.412 1.758 6.571 1.00 22.35 ? 360 ARG A HH21 1 ATOM 5460 H HH22 . ARG A 1 352 ? 9.924 1.097 7.804 1.00 22.35 ? 360 ARG A HH22 1 ATOM 5461 N N . LEU A 1 353 ? 13.194 8.224 8.452 1.00 12.61 ? 361 LEU A N 1 ATOM 5462 C CA A LEU A 1 353 ? 14.363 8.981 8.898 0.74 13.23 ? 361 LEU A CA 1 ATOM 5463 C CA B LEU A 1 353 ? 14.363 8.972 8.914 0.26 13.85 ? 361 LEU A CA 1 ATOM 5464 C C . LEU A 1 353 ? 15.629 8.591 8.151 1.00 13.80 ? 361 LEU A C 1 ATOM 5465 O O . LEU A 1 353 ? 16.391 9.463 7.726 1.00 13.82 ? 361 LEU A O 1 ATOM 5466 C CB A LEU A 1 353 ? 14.553 8.803 10.404 0.74 14.02 ? 361 LEU A CB 1 ATOM 5467 C CB B LEU A 1 353 ? 14.534 8.710 10.414 0.26 15.22 ? 361 LEU A CB 1 ATOM 5468 C CG A LEU A 1 353 ? 15.709 9.586 11.039 0.74 15.83 ? 361 LEU A CG 1 ATOM 5469 C CG B LEU A 1 353 ? 15.633 9.352 11.277 0.26 16.39 ? 361 LEU A CG 1 ATOM 5470 C CD1 A LEU A 1 353 ? 15.258 10.074 12.427 0.74 19.67 ? 361 LEU A CD1 1 ATOM 5471 C CD1 B LEU A 1 353 ? 17.045 8.988 10.846 0.26 18.55 ? 361 LEU A CD1 1 ATOM 5472 C CD2 A LEU A 1 353 ? 16.935 8.735 11.222 0.74 20.15 ? 361 LEU A CD2 1 ATOM 5473 C CD2 B LEU A 1 353 ? 15.464 10.854 11.375 0.26 14.51 ? 361 LEU A CD2 1 ATOM 5474 H H . LEU A 1 353 ? 12.803 7.773 9.072 1.00 15.13 ? 361 LEU A H 1 ATOM 5475 H HA . LEU A 1 353 ? 14.205 9.922 8.760 1.00 16.62 ? 361 LEU A HA 1 ATOM 5476 H HB2 A LEU A 1 353 ? 13.737 9.081 10.848 0.74 16.83 ? 361 LEU A HB2 1 ATOM 5477 H HB2 B LEU A 1 353 ? 13.696 8.957 10.834 0.26 18.26 ? 361 LEU A HB2 1 ATOM 5478 H HB3 A LEU A 1 353 ? 14.711 7.862 10.581 0.74 16.83 ? 361 LEU A HB3 1 ATOM 5479 H HB3 B LEU A 1 353 ? 14.650 7.753 10.515 0.26 18.26 ? 361 LEU A HB3 1 ATOM 5480 H HG A LEU A 1 353 ? 15.934 10.354 10.490 0.74 19.00 ? 361 LEU A HG 1 ATOM 5481 H HG B LEU A 1 353 ? 15.527 9.008 12.177 0.26 19.67 ? 361 LEU A HG 1 ATOM 5482 H HD11 A LEU A 1 353 ? 15.983 10.571 12.837 0.74 23.60 ? 361 LEU A HD11 1 ATOM 5483 H HD11 B LEU A 1 353 ? 17.678 9.429 11.435 0.26 22.26 ? 361 LEU A HD11 1 ATOM 5484 H HD12 A LEU A 1 353 ? 14.481 10.645 12.323 0.74 23.60 ? 361 LEU A HD12 1 ATOM 5485 H HD12 B LEU A 1 353 ? 17.154 8.026 10.904 0.26 22.26 ? 361 LEU A HD12 1 ATOM 5486 H HD13 A LEU A 1 353 ? 15.033 9.305 12.973 0.74 23.60 ? 361 LEU A HD13 1 ATOM 5487 H HD13 B LEU A 1 353 ? 17.182 9.283 9.932 0.26 22.26 ? 361 LEU A HD13 1 ATOM 5488 H HD21 A LEU A 1 353 ? 17.635 9.272 11.624 0.74 24.18 ? 361 LEU A HD21 1 ATOM 5489 H HD21 B LEU A 1 353 ? 16.176 11.216 11.926 0.26 17.41 ? 361 LEU A HD21 1 ATOM 5490 H HD22 A LEU A 1 353 ? 16.717 7.988 11.801 0.74 24.18 ? 361 LEU A HD22 1 ATOM 5491 H HD22 B LEU A 1 353 ? 15.509 11.235 10.484 0.26 17.41 ? 361 LEU A HD22 1 ATOM 5492 H HD23 A LEU A 1 353 ? 17.225 8.409 10.355 0.74 24.18 ? 361 LEU A HD23 1 ATOM 5493 H HD23 B LEU A 1 353 ? 14.603 11.049 11.776 0.26 17.41 ? 361 LEU A HD23 1 ATOM 5494 N N . THR A 1 354 ? 15.895 7.290 8.003 1.00 13.74 ? 362 THR A N 1 ATOM 5495 C CA . THR A 1 354 ? 17.138 6.885 7.349 1.00 15.25 ? 362 THR A CA 1 ATOM 5496 C C . THR A 1 354 ? 17.227 7.436 5.927 1.00 15.04 ? 362 THR A C 1 ATOM 5497 O O . THR A 1 354 ? 18.319 7.765 5.451 1.00 16.41 ? 362 THR A O 1 ATOM 5498 C CB . THR A 1 354 ? 17.294 5.369 7.338 1.00 15.62 ? 362 THR A CB 1 ATOM 5499 O OG1 . THR A 1 354 ? 16.125 4.776 6.764 1.00 16.30 ? 362 THR A OG1 1 ATOM 5500 C CG2 . THR A 1 354 ? 17.577 4.816 8.722 1.00 16.44 ? 362 THR A CG2 1 ATOM 5501 H H . THR A 1 354 ? 15.390 6.643 8.262 1.00 16.49 ? 362 THR A H 1 ATOM 5502 H HA . THR A 1 354 ? 17.882 7.252 7.851 1.00 18.30 ? 362 THR A HA 1 ATOM 5503 H HB . THR A 1 354 ? 18.054 5.146 6.778 1.00 18.74 ? 362 THR A HB 1 ATOM 5504 H HG1 . THR A 1 354 ? 15.447 4.982 7.215 1.00 19.56 ? 362 THR A HG1 1 ATOM 5505 H HG21 . THR A 1 354 ? 17.670 3.852 8.681 1.00 19.72 ? 362 THR A HG21 1 ATOM 5506 H HG22 . THR A 1 354 ? 18.398 5.198 9.070 1.00 19.72 ? 362 THR A HG22 1 ATOM 5507 H HG23 . THR A 1 354 ? 16.847 5.037 9.322 1.00 19.72 ? 362 THR A HG23 1 ATOM 5508 N N . GLU A 1 355 ? 16.089 7.512 5.234 1.00 15.71 ? 363 GLU A N 1 ATOM 5509 C CA . GLU A 1 355 ? 16.054 8.039 3.868 1.00 17.10 ? 363 GLU A CA 1 ATOM 5510 C C . GLU A 1 355 ? 16.230 9.555 3.863 1.00 15.13 ? 363 GLU A C 1 ATOM 5511 O O . GLU A 1 355 ? 16.983 10.102 3.046 1.00 18.28 ? 363 GLU A O 1 ATOM 5512 C CB . GLU A 1 355 ? 14.705 7.707 3.222 1.00 19.22 ? 363 GLU A CB 1 ATOM 5513 C CG . GLU A 1 355 ? 14.427 6.260 2.993 1.00 23.57 ? 363 GLU A CG 1 ATOM 5514 C CD . GLU A 1 355 ? 13.047 5.985 2.381 1.00 26.69 ? 363 GLU A CD 1 ATOM 5515 O OE1 . GLU A 1 355 ? 12.271 6.934 2.100 1.00 26.55 ? 363 GLU A OE1 1 ATOM 5516 O OE2 . GLU A 1 355 ? 12.751 4.793 2.163 1.00 30.61 ? 363 GLU A OE2 1 ATOM 5517 H H . GLU A 1 355 ? 15.322 7.265 5.533 1.00 18.85 ? 363 GLU A H 1 ATOM 5518 H HA . GLU A 1 355 ? 16.762 7.638 3.341 1.00 20.52 ? 363 GLU A HA 1 ATOM 5519 H HB2 . GLU A 1 355 ? 14.001 8.050 3.794 1.00 23.07 ? 363 GLU A HB2 1 ATOM 5520 H HB3 . GLU A 1 355 ? 14.664 8.150 2.360 1.00 23.07 ? 363 GLU A HB3 1 ATOM 5521 H HG2 . GLU A 1 355 ? 15.096 5.905 2.387 1.00 28.29 ? 363 GLU A HG2 1 ATOM 5522 H HG3 . GLU A 1 355 ? 14.472 5.795 3.842 1.00 28.29 ? 363 GLU A HG3 1 ATOM 5523 N N . ALA A 1 356 ? 15.539 10.254 4.772 1.00 15.14 ? 364 ALA A N 1 ATOM 5524 C CA . ALA A 1 356 ? 15.582 11.709 4.806 1.00 15.64 ? 364 ALA A CA 1 ATOM 5525 C C . ALA A 1 356 ? 16.986 12.239 5.067 1.00 15.31 ? 364 ALA A C 1 ATOM 5526 O O . ALA A 1 356 ? 17.376 13.273 4.506 1.00 16.98 ? 364 ALA A O 1 ATOM 5527 C CB . ALA A 1 356 ? 14.647 12.219 5.888 1.00 15.44 ? 364 ALA A CB 1 ATOM 5528 H H . ALA A 1 356 ? 15.040 9.903 5.378 1.00 18.16 ? 364 ALA A H 1 ATOM 5529 H HA . ALA A 1 356 ? 15.279 12.058 3.953 1.00 18.77 ? 364 ALA A HA 1 ATOM 5530 H HB1 . ALA A 1 356 ? 14.682 13.189 5.903 1.00 18.52 ? 364 ALA A HB1 1 ATOM 5531 H HB2 . ALA A 1 356 ? 13.745 11.923 5.690 1.00 18.52 ? 364 ALA A HB2 1 ATOM 5532 H HB3 . ALA A 1 356 ? 14.932 11.864 6.744 1.00 18.52 ? 364 ALA A HB3 1 ATOM 5533 N N . TYR A 1 357 ? 17.743 11.584 5.948 1.00 14.88 ? 365 TYR A N 1 ATOM 5534 C CA . TYR A 1 357 ? 19.064 12.067 6.330 1.00 14.99 ? 365 TYR A CA 1 ATOM 5535 C C . TYR A 1 357 ? 20.195 11.216 5.793 1.00 16.24 ? 365 TYR A C 1 ATOM 5536 O O . TYR A 1 357 ? 21.360 11.557 5.994 1.00 16.76 ? 365 TYR A O 1 ATOM 5537 C CB . TYR A 1 357 ? 19.153 12.260 7.852 1.00 15.30 ? 365 TYR A CB 1 ATOM 5538 C CG . TYR A 1 357 ? 18.126 13.280 8.301 1.00 15.16 ? 365 TYR A CG 1 ATOM 5539 C CD1 . TYR A 1 357 ? 18.243 14.605 7.940 1.00 16.36 ? 365 TYR A CD1 1 ATOM 5540 C CD2 . TYR A 1 357 ? 16.991 12.900 8.987 1.00 15.68 ? 365 TYR A CD2 1 ATOM 5541 C CE1 . TYR A 1 357 ? 17.301 15.536 8.281 1.00 16.96 ? 365 TYR A CE1 1 ATOM 5542 C CE2 . TYR A 1 357 ? 16.025 13.838 9.344 1.00 15.70 ? 365 TYR A CE2 1 ATOM 5543 C CZ . TYR A 1 357 ? 16.182 15.150 8.982 1.00 15.71 ? 365 TYR A CZ 1 ATOM 5544 O OH . TYR A 1 357 ? 15.226 16.075 9.320 1.00 17.62 ? 365 TYR A OH 1 ATOM 5545 H H . TYR A 1 357 ? 17.510 10.854 6.339 1.00 17.86 ? 365 TYR A H 1 ATOM 5546 H HA . TYR A 1 357 ? 19.175 12.947 5.937 1.00 17.98 ? 365 TYR A HA 1 ATOM 5547 H HB2 . TYR A 1 357 ? 18.968 11.419 8.298 1.00 18.36 ? 365 TYR A HB2 1 ATOM 5548 H HB3 . TYR A 1 357 ? 20.036 12.585 8.088 1.00 18.36 ? 365 TYR A HB3 1 ATOM 5549 H HD1 . TYR A 1 357 ? 18.991 14.876 7.458 1.00 19.63 ? 365 TYR A HD1 1 ATOM 5550 H HD2 . TYR A 1 357 ? 16.877 12.008 9.227 1.00 18.82 ? 365 TYR A HD2 1 ATOM 5551 H HE1 . TYR A 1 357 ? 17.413 16.426 8.033 1.00 20.35 ? 365 TYR A HE1 1 ATOM 5552 H HE2 . TYR A 1 357 ? 15.269 13.573 9.817 1.00 18.85 ? 365 TYR A HE2 1 ATOM 5553 H HH . TYR A 1 357 ? 15.448 16.834 9.038 1.00 21.14 ? 365 TYR A HH 1 ATOM 5554 N N . GLN A 1 358 ? 19.895 10.147 5.072 1.00 15.97 ? 366 GLN A N 1 ATOM 5555 C CA . GLN A 1 358 ? 20.914 9.278 4.493 1.00 16.60 ? 366 GLN A CA 1 ATOM 5556 C C . GLN A 1 358 ? 21.875 8.777 5.570 1.00 17.13 ? 366 GLN A C 1 ATOM 5557 O O . GLN A 1 358 ? 23.099 8.898 5.474 1.00 18.71 ? 366 GLN A O 1 ATOM 5558 C CB . GLN A 1 358 ? 21.613 9.957 3.309 1.00 19.43 ? 366 GLN A CB 1 ATOM 5559 C CG . GLN A 1 358 ? 20.655 10.257 2.162 1.00 22.52 ? 366 GLN A CG 1 ATOM 5560 C CD . GLN A 1 358 ? 20.193 9.002 1.469 1.00 25.09 ? 366 GLN A CD 1 ATOM 5561 O OE1 . GLN A 1 358 ? 20.995 8.277 0.868 1.00 29.39 ? 366 GLN A OE1 1 ATOM 5562 N NE2 . GLN A 1 358 ? 18.898 8.735 1.531 1.00 25.71 ? 366 GLN A NE2 1 ATOM 5563 H H . GLN A 1 358 ? 19.091 9.896 4.898 1.00 19.16 ? 366 GLN A H 1 ATOM 5564 H HA . GLN A 1 358 ? 20.465 8.495 4.137 1.00 19.92 ? 366 GLN A HA 1 ATOM 5565 H HB2 . GLN A 1 358 ? 21.997 10.797 3.607 1.00 23.32 ? 366 GLN A HB2 1 ATOM 5566 H HB3 . GLN A 1 358 ? 22.310 9.372 2.975 1.00 23.32 ? 366 GLN A HB3 1 ATOM 5567 H HG2 . GLN A 1 358 ? 19.875 10.715 2.510 1.00 27.02 ? 366 GLN A HG2 1 ATOM 5568 H HG3 . GLN A 1 358 ? 21.106 10.814 1.508 1.00 27.02 ? 366 GLN A HG3 1 ATOM 5569 H HE21 . GLN A 1 358 ? 18.368 9.266 1.951 1.00 30.86 ? 366 GLN A HE21 1 ATOM 5570 H HE22 . GLN A 1 358 ? 18.586 8.029 1.150 1.00 30.86 ? 366 GLN A HE22 1 ATOM 5571 N N . VAL A 1 359 ? 21.279 8.165 6.586 1.00 17.00 ? 367 VAL A N 1 ATOM 5572 C CA . VAL A 1 359 ? 22.009 7.603 7.722 1.00 16.18 ? 367 VAL A CA 1 ATOM 5573 C C . VAL A 1 359 ? 21.568 6.155 7.893 1.00 17.09 ? 367 VAL A C 1 ATOM 5574 O O . VAL A 1 359 ? 20.482 5.769 7.442 1.00 17.40 ? 367 VAL A O 1 ATOM 5575 C CB . VAL A 1 359 ? 21.774 8.415 9.020 1.00 16.95 ? 367 VAL A CB 1 ATOM 5576 C CG1 . VAL A 1 359 ? 22.458 9.777 8.910 1.00 17.96 ? 367 VAL A CG1 1 ATOM 5577 C CG2 . VAL A 1 359 ? 20.269 8.526 9.349 1.00 16.62 ? 367 VAL A CG2 1 ATOM 5578 H H . VAL A 1 359 ? 20.427 8.059 6.643 1.00 20.40 ? 367 VAL A H 1 ATOM 5579 H HA . VAL A 1 359 ? 22.959 7.610 7.527 1.00 19.41 ? 367 VAL A HA 1 ATOM 5580 H HB . VAL A 1 359 ? 22.194 7.942 9.755 1.00 20.34 ? 367 VAL A HB 1 ATOM 5581 H HG11 . VAL A 1 359 ? 22.303 10.274 9.728 1.00 21.55 ? 367 VAL A HG11 1 ATOM 5582 H HG12 . VAL A 1 359 ? 23.409 9.642 8.779 1.00 21.55 ? 367 VAL A HG12 1 ATOM 5583 H HG13 . VAL A 1 359 ? 22.084 10.257 8.154 1.00 21.55 ? 367 VAL A HG13 1 ATOM 5584 H HG21 . VAL A 1 359 ? 20.161 9.040 10.165 1.00 19.94 ? 367 VAL A HG21 1 ATOM 5585 H HG22 . VAL A 1 359 ? 19.818 8.972 8.615 1.00 19.94 ? 367 VAL A HG22 1 ATOM 5586 H HG23 . VAL A 1 359 ? 19.905 7.635 9.468 1.00 19.94 ? 367 VAL A HG23 1 ATOM 5587 N N . PRO A 1 360 ? 22.385 5.325 8.547 1.00 17.62 ? 368 PRO A N 1 ATOM 5588 C CA . PRO A 1 360 ? 22.081 3.886 8.580 1.00 16.94 ? 368 PRO A CA 1 ATOM 5589 C C . PRO A 1 360 ? 21.051 3.482 9.604 1.00 17.07 ? 368 PRO A C 1 ATOM 5590 O O . PRO A 1 360 ? 20.516 2.371 9.508 1.00 19.16 ? 368 PRO A O 1 ATOM 5591 C CB . PRO A 1 360 ? 23.442 3.256 8.904 1.00 19.10 ? 368 PRO A CB 1 ATOM 5592 C CG . PRO A 1 360 ? 24.169 4.327 9.646 1.00 18.82 ? 368 PRO A CG 1 ATOM 5593 C CD . PRO A 1 360 ? 23.764 5.596 8.980 1.00 17.24 ? 368 PRO A CD 1 ATOM 5594 H HA . PRO A 1 360 ? 21.793 3.586 7.704 1.00 20.32 ? 368 PRO A HA 1 ATOM 5595 H HB2 . PRO A 1 360 ? 23.318 2.472 9.462 1.00 22.92 ? 368 PRO A HB2 1 ATOM 5596 H HB3 . PRO A 1 360 ? 23.904 3.029 8.083 1.00 22.92 ? 368 PRO A HB3 1 ATOM 5597 H HG2 . PRO A 1 360 ? 23.896 4.325 10.576 1.00 22.58 ? 368 PRO A HG2 1 ATOM 5598 H HG3 . PRO A 1 360 ? 25.126 4.188 9.567 1.00 22.58 ? 368 PRO A HG3 1 ATOM 5599 H HD2 . PRO A 1 360 ? 23.782 6.331 9.613 1.00 20.69 ? 368 PRO A HD2 1 ATOM 5600 H HD3 . PRO A 1 360 ? 24.332 5.773 8.214 1.00 20.69 ? 368 PRO A HD3 1 ATOM 5601 N N . ASP A 1 361 ? 20.771 4.316 10.583 1.00 16.34 ? 369 ASP A N 1 ATOM 5602 C CA . ASP A 1 361 ? 19.887 3.957 11.686 1.00 15.33 ? 369 ASP A CA 1 ATOM 5603 C C . ASP A 1 361 ? 19.541 5.248 12.415 1.00 14.07 ? 369 ASP A C 1 ATOM 5604 O O . ASP A 1 361 ? 19.823 6.345 11.923 1.00 15.15 ? 369 ASP A O 1 ATOM 5605 C CB . ASP A 1 361 ? 20.536 2.908 12.596 1.00 16.67 ? 369 ASP A CB 1 ATOM 5606 C CG . ASP A 1 361 ? 21.891 3.322 13.080 1.00 18.36 ? 369 ASP A CG 1 ATOM 5607 O OD1 . ASP A 1 361 ? 22.056 4.523 13.395 1.00 16.89 ? 369 ASP A OD1 1 ATOM 5608 O OD2 . ASP A 1 361 ? 22.778 2.446 13.131 1.00 21.54 ? 369 ASP A OD2 1 ATOM 5609 H H . ASP A 1 361 ? 21.083 5.115 10.638 1.00 19.60 ? 369 ASP A H 1 ATOM 5610 H HA . ASP A 1 361 ? 19.067 3.582 11.329 1.00 18.39 ? 369 ASP A HA 1 ATOM 5611 H HB2 . ASP A 1 361 ? 19.970 2.769 13.372 1.00 20.01 ? 369 ASP A HB2 1 ATOM 5612 H HB3 . ASP A 1 361 ? 20.633 2.078 12.103 1.00 20.01 ? 369 ASP A HB3 1 ATOM 5613 N N . ALA A 1 362 ? 18.916 5.128 13.596 1.00 14.80 ? 370 ALA A N 1 ATOM 5614 C CA . ALA A 1 362 ? 18.546 6.283 14.402 1.00 14.14 ? 370 ALA A CA 1 ATOM 5615 C C . ALA A 1 362 ? 19.389 6.371 15.674 1.00 14.53 ? 370 ALA A C 1 ATOM 5616 O O . ALA A 1 362 ? 18.955 6.928 16.684 1.00 15.93 ? 370 ALA A O 1 ATOM 5617 C CB . ALA A 1 362 ? 17.047 6.282 14.708 1.00 15.04 ? 370 ALA A CB 1 ATOM 5618 H H . ALA A 1 362 ? 18.696 4.375 13.949 1.00 17.77 ? 370 ALA A H 1 ATOM 5619 H HA . ALA A 1 362 ? 18.730 7.082 13.884 1.00 16.97 ? 370 ALA A HA 1 ATOM 5620 H HB1 . ALA A 1 362 ? 16.834 7.062 15.245 1.00 18.05 ? 370 ALA A HB1 1 ATOM 5621 H HB2 . ALA A 1 362 ? 16.554 6.310 13.873 1.00 18.05 ? 370 ALA A HB2 1 ATOM 5622 H HB3 . ALA A 1 362 ? 16.825 5.474 15.197 1.00 18.05 ? 370 ALA A HB3 1 ATOM 5623 N N . SER A 1 363 ? 20.611 5.836 15.621 1.00 14.75 ? 371 SER A N 1 ATOM 5624 C CA . SER A 1 363 ? 21.560 5.896 16.723 1.00 14.89 ? 371 SER A CA 1 ATOM 5625 C C . SER A 1 363 ? 21.989 7.333 16.978 1.00 14.76 ? 371 SER A C 1 ATOM 5626 O O . SER A 1 363 ? 21.773 8.240 16.165 1.00 14.33 ? 371 SER A O 1 ATOM 5627 C CB . SER A 1 363 ? 22.805 5.089 16.367 1.00 15.68 ? 371 SER A CB 1 ATOM 5628 O OG . SER A 1 363 ? 23.572 5.713 15.346 1.00 16.51 ? 371 SER A OG 1 ATOM 5629 H H . SER A 1 363 ? 20.917 5.421 14.933 1.00 17.70 ? 371 SER A H 1 ATOM 5630 H HA . SER A 1 363 ? 21.163 5.532 17.530 1.00 17.86 ? 371 SER A HA 1 ATOM 5631 H HB2 . SER A 1 363 ? 23.356 5.001 17.161 1.00 18.81 ? 371 SER A HB2 1 ATOM 5632 H HB3 . SER A 1 363 ? 22.530 4.212 16.059 1.00 18.81 ? 371 SER A HB3 1 ATOM 5633 H HG . SER A 1 363 ? 23.110 5.795 14.649 1.00 19.81 ? 371 SER A HG 1 ATOM 5634 N N . VAL A 1 364 ? 22.656 7.524 18.112 1.00 15.26 ? 372 VAL A N 1 ATOM 5635 C CA . VAL A 1 364 ? 23.190 8.841 18.429 1.00 16.32 ? 372 VAL A CA 1 ATOM 5636 C C . VAL A 1 364 ? 24.131 9.322 17.326 1.00 15.05 ? 372 VAL A C 1 ATOM 5637 O O . VAL A 1 364 ? 24.116 10.501 16.959 1.00 15.60 ? 372 VAL A O 1 ATOM 5638 C CB . VAL A 1 364 ? 23.873 8.854 19.810 1.00 18.52 ? 372 VAL A CB 1 ATOM 5639 C CG1 . VAL A 1 364 ? 24.349 10.232 20.126 1.00 22.98 ? 372 VAL A CG1 1 ATOM 5640 C CG2 . VAL A 1 364 ? 22.925 8.407 20.880 1.00 19.54 ? 372 VAL A CG2 1 ATOM 5641 H H . VAL A 1 364 ? 22.811 6.919 18.704 1.00 18.31 ? 372 VAL A H 1 ATOM 5642 H HA . VAL A 1 364 ? 22.451 9.468 18.469 1.00 19.59 ? 372 VAL A HA 1 ATOM 5643 H HB . VAL A 1 364 ? 24.637 8.256 19.802 1.00 22.23 ? 372 VAL A HB 1 ATOM 5644 H HG11 . VAL A 1 364 ? 24.777 10.226 20.997 1.00 27.58 ? 372 VAL A HG11 1 ATOM 5645 H HG12 . VAL A 1 364 ? 24.984 10.509 19.447 1.00 27.58 ? 372 VAL A HG12 1 ATOM 5646 H HG13 . VAL A 1 364 ? 23.589 10.834 20.134 1.00 27.58 ? 372 VAL A HG13 1 ATOM 5647 H HG21 . VAL A 1 364 ? 23.383 8.425 21.735 1.00 23.45 ? 372 VAL A HG21 1 ATOM 5648 H HG22 . VAL A 1 364 ? 22.165 9.008 20.899 1.00 23.45 ? 372 VAL A HG22 1 ATOM 5649 H HG23 . VAL A 1 364 ? 22.629 7.505 20.682 1.00 23.45 ? 372 VAL A HG23 1 ATOM 5650 N N . SER A 1 365 ? 25.021 8.445 16.827 1.00 15.50 ? 373 SER A N 1 ATOM 5651 C CA A SER A 1 365 ? 25.942 8.868 15.777 0.45 15.66 ? 373 SER A CA 1 ATOM 5652 C CA B SER A 1 365 ? 25.941 8.853 15.770 0.36 15.91 ? 373 SER A CA 1 ATOM 5653 C CA C SER A 1 365 ? 25.941 8.855 15.771 0.19 15.61 ? 373 SER A CA 1 ATOM 5654 C C . SER A 1 365 ? 25.182 9.280 14.520 1.00 15.56 ? 373 SER A C 1 ATOM 5655 O O . SER A 1 365 ? 25.543 10.267 13.867 1.00 16.82 ? 373 SER A O 1 ATOM 5656 C CB A SER A 1 365 ? 26.993 7.793 15.488 0.45 18.36 ? 373 SER A CB 1 ATOM 5657 C CB B SER A 1 365 ? 26.890 7.697 15.448 0.36 18.78 ? 373 SER A CB 1 ATOM 5658 C CB C SER A 1 365 ? 26.905 7.712 15.439 0.19 16.61 ? 373 SER A CB 1 ATOM 5659 O OG A SER A 1 365 ? 26.425 6.588 15.036 0.45 19.03 ? 373 SER A OG 1 ATOM 5660 O OG B SER A 1 365 ? 27.508 7.861 14.183 0.36 20.86 ? 373 SER A OG 1 ATOM 5661 O OG C SER A 1 365 ? 27.821 7.463 16.496 0.19 16.19 ? 373 SER A OG 1 ATOM 5662 H H . SER A 1 365 ? 25.109 7.626 17.075 1.00 18.60 ? 373 SER A H 1 ATOM 5663 H HA . SER A 1 365 ? 26.450 9.624 16.083 1.00 18.73 ? 373 SER A HA 1 ATOM 5664 H HB2 A SER A 1 365 ? 27.597 8.126 14.806 0.45 22.04 ? 373 SER A HB2 1 ATOM 5665 H HB2 B SER A 1 365 ? 27.579 7.658 16.130 0.36 22.54 ? 373 SER A HB2 1 ATOM 5666 H HB2 C SER A 1 365 ? 26.390 6.906 15.277 0.19 19.93 ? 373 SER A HB2 1 ATOM 5667 H HB3 A SER A 1 365 ? 27.487 7.616 16.304 0.45 22.04 ? 373 SER A HB3 1 ATOM 5668 H HB3 B SER A 1 365 ? 26.384 6.869 15.444 0.36 22.54 ? 373 SER A HB3 1 ATOM 5669 H HB3 C SER A 1 365 ? 27.406 7.947 14.642 0.19 19.93 ? 373 SER A HB3 1 ATOM 5670 H HG A SER A 1 365 ? 25.997 6.721 14.326 0.45 22.84 ? 373 SER A HG 1 ATOM 5671 H HG B SER A 1 365 ? 26.925 7.893 13.580 0.36 25.04 ? 373 SER A HG 1 ATOM 5672 H HG C SER A 1 365 ? 27.404 7.254 17.194 0.19 19.43 ? 373 SER A HG 1 ATOM 5673 N N . SER A 1 366 ? 24.123 8.553 14.172 1.00 13.91 ? 374 SER A N 1 ATOM 5674 C CA . SER A 1 366 ? 23.348 8.914 12.989 1.00 15.11 ? 374 SER A CA 1 ATOM 5675 C C . SER A 1 366 ? 22.634 10.248 13.170 1.00 14.41 ? 374 SER A C 1 ATOM 5676 O O . SER A 1 366 ? 22.593 11.066 12.245 1.00 15.01 ? 374 SER A O 1 ATOM 5677 C CB . SER A 1 366 ? 22.338 7.820 12.694 1.00 15.07 ? 374 SER A CB 1 ATOM 5678 O OG . SER A 1 366 ? 22.997 6.698 12.123 1.00 16.28 ? 374 SER A OG 1 ATOM 5679 H H . SER A 1 366 ? 23.838 7.861 14.594 1.00 16.69 ? 374 SER A H 1 ATOM 5680 H HA . SER A 1 366 ? 23.944 8.990 12.227 1.00 18.13 ? 374 SER A HA 1 ATOM 5681 H HB2 . SER A 1 366 ? 21.909 7.551 13.522 1.00 18.09 ? 374 SER A HB2 1 ATOM 5682 H HB3 . SER A 1 366 ? 21.678 8.156 12.068 1.00 18.09 ? 374 SER A HB3 1 ATOM 5683 H HG . SER A 1 366 ? 22.441 6.090 11.959 1.00 19.53 ? 374 SER A HG 1 ATOM 5684 N N . MET A 1 367 ? 22.080 10.497 14.351 1.00 13.69 ? 375 MET A N 1 ATOM 5685 C CA . MET A 1 367 ? 21.420 11.770 14.590 1.00 12.80 ? 375 MET A CA 1 ATOM 5686 C C . MET A 1 367 ? 22.422 12.915 14.628 1.00 14.11 ? 375 MET A C 1 ATOM 5687 O O . MET A 1 367 ? 22.122 14.026 14.169 1.00 13.94 ? 375 MET A O 1 ATOM 5688 C CB . MET A 1 367 ? 20.554 11.685 15.834 1.00 13.09 ? 375 MET A CB 1 ATOM 5689 C CG . MET A 1 367 ? 19.418 10.651 15.711 1.00 13.52 ? 375 MET A CG 1 ATOM 5690 S SD . MET A 1 367 ? 18.413 10.757 14.231 1.00 15.26 ? 375 MET A SD 1 ATOM 5691 C CE . MET A 1 367 ? 17.617 12.321 14.546 1.00 16.65 ? 375 MET A CE 1 ATOM 5692 H H . MET A 1 367 ? 22.072 9.954 15.018 1.00 16.43 ? 375 MET A H 1 ATOM 5693 H HA . MET A 1 367 ? 20.819 11.933 13.846 1.00 15.36 ? 375 MET A HA 1 ATOM 5694 H HB2 . MET A 1 367 ? 21.109 11.431 16.587 1.00 15.71 ? 375 MET A HB2 1 ATOM 5695 H HB3 . MET A 1 367 ? 20.151 12.553 15.997 1.00 15.71 ? 375 MET A HB3 1 ATOM 5696 H HG2 . MET A 1 367 ? 19.810 9.764 15.731 1.00 16.23 ? 375 MET A HG2 1 ATOM 5697 H HG3 . MET A 1 367 ? 18.825 10.758 16.471 1.00 16.23 ? 375 MET A HG3 1 ATOM 5698 H HE1 . MET A 1 367 ? 17.020 12.525 13.809 1.00 19.98 ? 375 MET A HE1 1 ATOM 5699 H HE2 . MET A 1 367 ? 17.113 12.257 15.373 1.00 19.98 ? 375 MET A HE2 1 ATOM 5700 H HE3 . MET A 1 367 ? 18.295 13.010 14.624 1.00 19.98 ? 375 MET A HE3 1 ATOM 5701 N N . HIS A 1 368 ? 23.632 12.661 15.115 1.00 14.25 ? 376 HIS A N 1 ATOM 5702 C CA . HIS A 1 368 ? 24.660 13.685 15.039 1.00 14.83 ? 376 HIS A CA 1 ATOM 5703 C C . HIS A 1 368 ? 24.969 14.017 13.585 1.00 14.00 ? 376 HIS A C 1 ATOM 5704 O O . HIS A 1 368 ? 25.059 15.193 13.210 1.00 14.91 ? 376 HIS A O 1 ATOM 5705 C CB . HIS A 1 368 ? 25.911 13.238 15.779 1.00 15.73 ? 376 HIS A CB 1 ATOM 5706 C CG . HIS A 1 368 ? 27.009 14.232 15.686 1.00 18.69 ? 376 HIS A CG 1 ATOM 5707 N ND1 . HIS A 1 368 ? 27.000 15.424 16.374 1.00 21.60 ? 376 HIS A ND1 1 ATOM 5708 C CD2 . HIS A 1 368 ? 28.115 14.253 14.909 1.00 22.27 ? 376 HIS A CD2 1 ATOM 5709 C CE1 . HIS A 1 368 ? 28.096 16.099 16.086 1.00 21.26 ? 376 HIS A CE1 1 ATOM 5710 N NE2 . HIS A 1 368 ? 28.785 15.420 15.189 1.00 25.85 ? 376 HIS A NE2 1 ATOM 5711 H H . HIS A 1 368 ? 23.877 11.924 15.484 1.00 17.10 ? 376 HIS A H 1 ATOM 5712 H HA . HIS A 1 368 ? 24.333 14.492 15.466 1.00 17.80 ? 376 HIS A HA 1 ATOM 5713 H HB2 . HIS A 1 368 ? 25.697 13.112 16.716 1.00 18.88 ? 376 HIS A HB2 1 ATOM 5714 H HB3 . HIS A 1 368 ? 26.227 12.405 15.394 1.00 18.88 ? 376 HIS A HB3 1 ATOM 5715 H HD1 . HIS A 1 368 ? 26.403 15.664 16.945 1.00 25.93 ? 376 HIS A HD1 1 ATOM 5716 H HD2 . HIS A 1 368 ? 28.393 13.585 14.325 1.00 26.72 ? 376 HIS A HD2 1 ATOM 5717 H HE1 . HIS A 1 368 ? 28.326 16.932 16.430 1.00 25.51 ? 376 HIS A HE1 1 ATOM 5718 N N . THR A 1 369 ? 25.087 12.989 12.742 1.00 14.97 ? 377 THR A N 1 ATOM 5719 C CA . THR A 1 369 ? 25.268 13.231 11.310 1.00 16.41 ? 377 THR A CA 1 ATOM 5720 C C . THR A 1 369 ? 24.100 14.021 10.736 1.00 15.36 ? 377 THR A C 1 ATOM 5721 O O . THR A 1 369 ? 24.300 14.946 9.936 1.00 16.11 ? 377 THR A O 1 ATOM 5722 C CB . THR A 1 369 ? 25.454 11.913 10.581 1.00 18.07 ? 377 THR A CB 1 ATOM 5723 O OG1 . THR A 1 369 ? 26.667 11.314 11.035 1.00 20.31 ? 377 THR A OG1 1 ATOM 5724 C CG2 . THR A 1 369 ? 25.550 12.123 9.067 1.00 19.85 ? 377 THR A CG2 1 ATOM 5725 H H . THR A 1 369 ? 25.065 12.159 12.967 1.00 17.97 ? 377 THR A H 1 ATOM 5726 H HA . THR A 1 369 ? 26.073 13.757 11.182 1.00 19.69 ? 377 THR A HA 1 ATOM 5727 H HB . THR A 1 369 ? 24.706 11.324 10.769 1.00 21.69 ? 377 THR A HB 1 ATOM 5728 H HG1 . THR A 1 369 ? 26.790 10.581 10.644 1.00 24.38 ? 377 THR A HG1 1 ATOM 5729 H HG21 . THR A 1 369 ? 25.668 11.270 8.620 1.00 23.82 ? 377 THR A HG21 1 ATOM 5730 H HG22 . THR A 1 369 ? 24.739 12.541 8.739 1.00 23.82 ? 377 THR A HG22 1 ATOM 5731 H HG23 . THR A 1 369 ? 26.305 12.695 8.859 1.00 23.82 ? 377 THR A HG23 1 ATOM 5732 N N . ALA A 1 370 ? 22.872 13.667 11.112 1.00 15.17 ? 378 ALA A N 1 ATOM 5733 C CA . ALA A 1 370 ? 21.716 14.417 10.625 1.00 14.77 ? 378 ALA A CA 1 ATOM 5734 C C . ALA A 1 370 ? 21.826 15.889 10.983 1.00 13.64 ? 378 ALA A C 1 ATOM 5735 O O . ALA A 1 370 ? 21.614 16.760 10.133 1.00 14.14 ? 378 ALA A O 1 ATOM 5736 C CB . ALA A 1 370 ? 20.430 13.816 11.163 1.00 14.46 ? 378 ALA A CB 1 ATOM 5737 H H . ALA A 1 370 ? 22.684 13.011 11.636 1.00 18.20 ? 378 ALA A H 1 ATOM 5738 H HA . ALA A 1 370 ? 21.689 14.351 9.658 1.00 17.73 ? 378 ALA A HA 1 ATOM 5739 H HB1 . ALA A 1 370 ? 19.678 14.328 10.827 1.00 17.35 ? 378 ALA A HB1 1 ATOM 5740 H HB2 . ALA A 1 370 ? 20.363 12.895 10.864 1.00 17.35 ? 378 ALA A HB2 1 ATOM 5741 H HB3 . ALA A 1 370 ? 20.448 13.849 12.132 1.00 17.35 ? 378 ALA A HB3 1 ATOM 5742 N N . LEU A 1 371 ? 22.199 16.189 12.230 1.00 13.74 ? 379 LEU A N 1 ATOM 5743 C CA . LEU A 1 371 ? 22.346 17.580 12.616 1.00 13.73 ? 379 LEU A CA 1 ATOM 5744 C C . LEU A 1 371 ? 23.424 18.257 11.789 1.00 14.07 ? 379 LEU A C 1 ATOM 5745 O O . LEU A 1 371 ? 23.257 19.395 11.339 1.00 14.48 ? 379 LEU A O 1 ATOM 5746 C CB . LEU A 1 371 ? 22.678 17.670 14.101 1.00 13.69 ? 379 LEU A CB 1 ATOM 5747 C CG . LEU A 1 371 ? 22.925 19.077 14.660 1.00 15.81 ? 379 LEU A CG 1 ATOM 5748 C CD1 . LEU A 1 371 ? 24.317 19.587 14.405 1.00 20.65 ? 379 LEU A CD1 1 ATOM 5749 C CD2 . LEU A 1 371 ? 21.902 20.134 14.243 1.00 16.34 ? 379 LEU A CD2 1 ATOM 5750 H H . LEU A 1 371 ? 22.366 15.618 12.851 1.00 16.49 ? 379 LEU A H 1 ATOM 5751 H HA . LEU A 1 371 ? 21.509 18.045 12.463 1.00 16.48 ? 379 LEU A HA 1 ATOM 5752 H HB2 . LEU A 1 371 ? 21.940 17.287 14.601 1.00 16.42 ? 379 LEU A HB2 1 ATOM 5753 H HB3 . LEU A 1 371 ? 23.480 17.150 14.265 1.00 16.42 ? 379 LEU A HB3 1 ATOM 5754 H HG . LEU A 1 371 ? 22.846 19.006 15.625 1.00 18.97 ? 379 LEU A HG 1 ATOM 5755 H HD11 . LEU A 1 371 ? 24.401 20.476 14.784 1.00 24.78 ? 379 LEU A HD11 1 ATOM 5756 H HD12 . LEU A 1 371 ? 24.954 18.987 14.823 1.00 24.78 ? 379 LEU A HD12 1 ATOM 5757 H HD13 . LEU A 1 371 ? 24.470 19.619 13.448 1.00 24.78 ? 379 LEU A HD13 1 ATOM 5758 H HD21 . LEU A 1 371 ? 22.144 20.983 14.645 1.00 19.61 ? 379 LEU A HD21 1 ATOM 5759 H HD22 . LEU A 1 371 ? 21.906 20.213 13.276 1.00 19.61 ? 379 LEU A HD22 1 ATOM 5760 H HD23 . LEU A 1 371 ? 21.023 19.862 14.550 1.00 19.61 ? 379 LEU A HD23 1 ATOM 5761 N N . THR A 1 372 ? 24.566 17.609 11.630 1.00 14.47 ? 380 THR A N 1 ATOM 5762 C CA A THR A 1 372 ? 25.645 18.240 10.885 0.48 15.37 ? 380 THR A CA 1 ATOM 5763 C CA B THR A 1 372 ? 25.644 18.258 10.888 0.52 15.36 ? 380 THR A CA 1 ATOM 5764 C C . THR A 1 372 ? 25.207 18.562 9.460 1.00 14.77 ? 380 THR A C 1 ATOM 5765 O O . THR A 1 372 ? 25.603 19.592 8.902 1.00 16.98 ? 380 THR A O 1 ATOM 5766 C CB A THR A 1 372 ? 26.855 17.311 10.899 0.48 17.71 ? 380 THR A CB 1 ATOM 5767 C CB B THR A 1 372 ? 26.960 17.467 10.928 0.52 18.11 ? 380 THR A CB 1 ATOM 5768 O OG1 A THR A 1 372 ? 27.331 17.200 12.244 0.48 18.33 ? 380 THR A OG1 1 ATOM 5769 O OG1 B THR A 1 372 ? 26.861 16.276 10.155 0.52 19.05 ? 380 THR A OG1 1 ATOM 5770 C CG2 A THR A 1 372 ? 27.950 17.842 10.030 0.48 18.41 ? 380 THR A CG2 1 ATOM 5771 C CG2 B THR A 1 372 ? 27.331 17.108 12.341 0.52 18.13 ? 380 THR A CG2 1 ATOM 5772 H H . THR A 1 372 ? 24.749 16.823 11.928 1.00 17.37 ? 380 THR A H 1 ATOM 5773 H HA . THR A 1 372 ? 25.856 19.091 11.318 1.00 18.43 ? 380 THR A HA 1 ATOM 5774 H HB A THR A 1 372 ? 26.598 16.435 10.572 0.48 21.25 ? 380 THR A HB 1 ATOM 5775 H HB B THR A 1 372 ? 27.670 18.020 10.565 0.52 21.73 ? 380 THR A HB 1 ATOM 5776 H HG1 A THR A 1 372 ? 26.729 16.885 12.737 0.48 22.00 ? 380 THR A HG1 1 ATOM 5777 H HG1 B THR A 1 372 ? 26.689 16.466 9.355 0.52 22.86 ? 380 THR A HG1 1 ATOM 5778 H HG21 A THR A 1 372 ? 28.710 17.240 10.051 0.48 22.10 ? 380 THR A HG21 1 ATOM 5779 H HG21 B THR A 1 372 ? 28.163 16.610 12.349 0.52 21.76 ? 380 THR A HG21 1 ATOM 5780 H HG22 A THR A 1 372 ? 27.637 17.923 9.116 0.48 22.10 ? 380 THR A HG22 1 ATOM 5781 H HG22 B THR A 1 372 ? 27.441 17.914 12.870 0.52 21.76 ? 380 THR A HG22 1 ATOM 5782 H HG23 A THR A 1 372 ? 28.230 18.715 10.346 0.48 22.10 ? 380 THR A HG23 1 ATOM 5783 H HG23 B THR A 1 372 ? 26.633 16.563 12.738 0.52 21.76 ? 380 THR A HG23 1 ATOM 5784 N N . ARG A 1 373 ? 24.375 17.696 8.865 1.00 15.49 ? 381 ARG A N 1 ATOM 5785 C CA . ARG A 1 373 ? 23.872 17.943 7.514 1.00 15.67 ? 381 ARG A CA 1 ATOM 5786 C C . ARG A 1 373 ? 22.828 19.059 7.498 1.00 14.39 ? 381 ARG A C 1 ATOM 5787 O O . ARG A 1 373 ? 22.863 19.942 6.638 1.00 16.09 ? 381 ARG A O 1 ATOM 5788 C CB . ARG A 1 373 ? 23.293 16.667 6.917 1.00 17.35 ? 381 ARG A CB 1 ATOM 5789 C CG . ARG A 1 373 ? 24.280 15.554 6.685 1.00 19.34 ? 381 ARG A CG 1 ATOM 5790 C CD . ARG A 1 373 ? 23.602 14.488 5.848 1.00 23.21 ? 381 ARG A CD 1 ATOM 5791 N NE . ARG A 1 373 ? 23.518 14.945 4.458 1.00 24.91 ? 381 ARG A NE 1 ATOM 5792 C CZ . ARG A 1 373 ? 22.766 14.401 3.497 1.00 25.11 ? 381 ARG A CZ 1 ATOM 5793 N NH1 . ARG A 1 373 ? 21.971 13.365 3.751 1.00 26.44 ? 381 ARG A NH1 1 ATOM 5794 N NH2 . ARG A 1 373 ? 22.796 14.911 2.270 1.00 26.41 ? 381 ARG A NH2 1 ATOM 5795 H H . ARG A 1 373 ? 24.092 16.966 9.221 1.00 18.59 ? 381 ARG A H 1 ATOM 5796 H HA . ARG A 1 373 ? 24.611 18.223 6.952 1.00 18.80 ? 381 ARG A HA 1 ATOM 5797 H HB2 . ARG A 1 373 ? 22.611 16.330 7.518 1.00 20.82 ? 381 ARG A HB2 1 ATOM 5798 H HB3 . ARG A 1 373 ? 22.892 16.884 6.061 1.00 20.82 ? 381 ARG A HB3 1 ATOM 5799 H HG2 . ARG A 1 373 ? 25.050 15.891 6.201 1.00 23.21 ? 381 ARG A HG2 1 ATOM 5800 H HG3 . ARG A 1 373 ? 24.546 15.165 7.533 1.00 23.21 ? 381 ARG A HG3 1 ATOM 5801 H HD2 . ARG A 1 373 ? 24.123 13.670 5.875 1.00 27.86 ? 381 ARG A HD2 1 ATOM 5802 H HD3 . ARG A 1 373 ? 22.704 14.334 6.179 1.00 27.86 ? 381 ARG A HD3 1 ATOM 5803 H HE . ARG A 1 373 ? 23.996 15.626 4.242 1.00 29.89 ? 381 ARG A HE 1 ATOM 5804 H HH11 . ARG A 1 373 ? 21.945 13.026 4.541 1.00 31.73 ? 381 ARG A HH11 1 ATOM 5805 H HH12 . ARG A 1 373 ? 21.489 13.028 3.123 1.00 31.73 ? 381 ARG A HH12 1 ATOM 5806 H HH21 . ARG A 1 373 ? 23.301 15.585 2.096 1.00 31.70 ? 381 ARG A HH21 1 ATOM 5807 H HH22 . ARG A 1 373 ? 22.306 14.570 1.650 1.00 31.70 ? 381 ARG A HH22 1 ATOM 5808 N N . ILE A 1 374 ? 21.930 19.063 8.472 1.00 14.00 ? 382 ILE A N 1 ATOM 5809 C CA . ILE A 1 374 ? 20.991 20.170 8.609 1.00 13.60 ? 382 ILE A CA 1 ATOM 5810 C C . ILE A 1 374 ? 21.733 21.496 8.703 1.00 14.94 ? 382 ILE A C 1 ATOM 5811 O O . ILE A 1 374 ? 21.304 22.498 8.110 1.00 15.56 ? 382 ILE A O 1 ATOM 5812 C CB . ILE A 1 374 ? 20.089 19.957 9.835 1.00 14.09 ? 382 ILE A CB 1 ATOM 5813 C CG1 . ILE A 1 374 ? 19.133 18.792 9.581 1.00 13.88 ? 382 ILE A CG1 1 ATOM 5814 C CG2 . ILE A 1 374 ? 19.349 21.257 10.200 1.00 14.56 ? 382 ILE A CG2 1 ATOM 5815 C CD1 . ILE A 1 374 ? 18.472 18.282 10.866 1.00 14.51 ? 382 ILE A CD1 1 ATOM 5816 H H . ILE A 1 374 ? 21.842 18.445 9.063 1.00 16.80 ? 382 ILE A H 1 ATOM 5817 H HA . ILE A 1 374 ? 20.424 20.201 7.823 1.00 16.32 ? 382 ILE A HA 1 ATOM 5818 H HB . ILE A 1 374 ? 20.657 19.717 10.584 1.00 16.91 ? 382 ILE A HB 1 ATOM 5819 H HG12 . ILE A 1 374 ? 18.432 19.084 8.977 1.00 16.65 ? 382 ILE A HG12 1 ATOM 5820 H HG13 . ILE A 1 374 ? 19.627 18.057 9.185 1.00 16.65 ? 382 ILE A HG13 1 ATOM 5821 H HG21 . ILE A 1 374 ? 18.788 21.093 10.975 1.00 17.48 ? 382 ILE A HG21 1 ATOM 5822 H HG22 . ILE A 1 374 ? 20.001 21.945 10.403 1.00 17.48 ? 382 ILE A HG22 1 ATOM 5823 H HG23 . ILE A 1 374 ? 18.802 21.530 9.447 1.00 17.48 ? 382 ILE A HG23 1 ATOM 5824 H HD11 . ILE A 1 374 ? 17.878 17.547 10.645 1.00 17.41 ? 382 ILE A HD11 1 ATOM 5825 H HD12 . ILE A 1 374 ? 19.161 17.979 11.477 1.00 17.41 ? 382 ILE A HD12 1 ATOM 5826 H HD13 . ILE A 1 374 ? 17.967 19.006 11.269 1.00 17.41 ? 382 ILE A HD13 1 ATOM 5827 N N . ALA A 1 375 ? 22.853 21.523 9.442 1.00 15.11 ? 383 ALA A N 1 ATOM 5828 C CA . ALA A 1 375 ? 23.570 22.768 9.691 1.00 16.29 ? 383 ALA A CA 1 ATOM 5829 C C . ALA A 1 375 ? 24.475 23.183 8.550 1.00 17.81 ? 383 ALA A C 1 ATOM 5830 O O . ALA A 1 375 ? 25.000 24.291 8.598 1.00 21.50 ? 383 ALA A O 1 ATOM 5831 C CB . ALA A 1 375 ? 24.418 22.639 10.954 1.00 17.10 ? 383 ALA A CB 1 ATOM 5832 H H . ALA A 1 375 ? 23.212 20.832 9.807 1.00 18.13 ? 383 ALA A H 1 ATOM 5833 H HA . ALA A 1 375 ? 22.926 23.478 9.835 1.00 19.55 ? 383 ALA A HA 1 ATOM 5834 H HB1 . ALA A 1 375 ? 24.887 23.474 11.105 1.00 20.51 ? 383 ALA A HB1 1 ATOM 5835 H HB2 . ALA A 1 375 ? 23.836 22.445 11.706 1.00 20.51 ? 383 ALA A HB2 1 ATOM 5836 H HB3 . ALA A 1 375 ? 25.055 21.917 10.834 1.00 20.51 ? 383 ALA A HB3 1 ATOM 5837 N N . SER A 1 376 ? 24.704 22.327 7.570 1.00 17.39 ? 384 SER A N 1 ATOM 5838 C CA . SER A 1 376 ? 25.650 22.625 6.503 1.00 19.17 ? 384 SER A CA 1 ATOM 5839 C C . SER A 1 376 ? 25.102 22.502 5.087 1.00 20.65 ? 384 SER A C 1 ATOM 5840 O O . SER A 1 376 ? 25.724 23.036 4.175 1.00 24.12 ? 384 SER A O 1 ATOM 5841 C CB . SER A 1 376 ? 26.884 21.727 6.614 1.00 20.73 ? 384 SER A CB 1 ATOM 5842 O OG . SER A 1 376 ? 26.540 20.377 6.408 1.00 22.15 ? 384 SER A OG 1 ATOM 5843 H H . SER A 1 376 ? 24.324 21.559 7.497 1.00 20.87 ? 384 SER A H 1 ATOM 5844 H HA . SER A 1 376 ? 25.950 23.540 6.614 1.00 23.01 ? 384 SER A HA 1 ATOM 5845 H HB2 . SER A 1 376 ? 27.531 21.995 5.943 1.00 24.88 ? 384 SER A HB2 1 ATOM 5846 H HB3 . SER A 1 376 ? 27.266 21.824 7.501 1.00 24.88 ? 384 SER A HB3 1 ATOM 5847 H HG . SER A 1 376 ? 25.979 20.132 6.983 1.00 26.58 ? 384 SER A HG 1 ATOM 5848 N N . GLU A 1 377 ? 23.989 21.827 4.860 1.00 18.17 ? 385 GLU A N 1 ATOM 5849 C CA . GLU A 1 377 ? 23.498 21.590 3.501 1.00 18.26 ? 385 GLU A CA 1 ATOM 5850 C C . GLU A 1 377 ? 22.125 22.217 3.338 1.00 18.32 ? 385 GLU A C 1 ATOM 5851 O O . GLU A 1 377 ? 21.165 21.764 3.984 1.00 18.33 ? 385 GLU A O 1 ATOM 5852 C CB . GLU A 1 377 ? 23.436 20.092 3.246 1.00 19.48 ? 385 GLU A CB 1 ATOM 5853 C CG . GLU A 1 377 ? 24.767 19.393 3.355 1.00 20.93 ? 385 GLU A CG 1 ATOM 5854 C CD . GLU A 1 377 ? 24.642 17.926 3.073 1.00 25.80 ? 385 GLU A CD 1 ATOM 5855 O OE1 . GLU A 1 377 ? 23.900 17.561 2.146 1.00 29.28 ? 385 GLU A OE1 1 ATOM 5856 O OE2 . GLU A 1 377 ? 25.295 17.134 3.765 1.00 30.76 ? 385 GLU A OE2 1 ATOM 5857 H H . GLU A 1 377 ? 23.492 21.491 5.476 1.00 21.80 ? 385 GLU A H 1 ATOM 5858 H HA . GLU A 1 377 ? 24.103 21.992 2.858 1.00 21.91 ? 385 GLU A HA 1 ATOM 5859 H HB2 . GLU A 1 377 ? 22.837 19.690 3.895 1.00 23.38 ? 385 GLU A HB2 1 ATOM 5860 H HB3 . GLU A 1 377 ? 23.097 19.943 2.350 1.00 23.38 ? 385 GLU A HB3 1 ATOM 5861 H HG2 . GLU A 1 377 ? 25.383 19.775 2.711 1.00 25.11 ? 385 GLU A HG2 1 ATOM 5862 H HG3 . GLU A 1 377 ? 25.113 19.501 4.255 1.00 25.11 ? 385 GLU A HG3 1 ATOM 5863 N N . PRO A 1 378 ? 21.982 23.244 2.504 1.00 19.06 ? 386 PRO A N 1 ATOM 5864 C CA . PRO A 1 378 ? 20.679 23.903 2.366 1.00 19.50 ? 386 PRO A CA 1 ATOM 5865 C C . PRO A 1 378 ? 19.531 22.960 2.116 1.00 16.99 ? 386 PRO A C 1 ATOM 5866 O O . PRO A 1 378 ? 18.446 23.171 2.675 1.00 18.32 ? 386 PRO A O 1 ATOM 5867 C CB . PRO A 1 378 ? 20.893 24.870 1.193 1.00 21.90 ? 386 PRO A CB 1 ATOM 5868 C CG . PRO A 1 378 ? 22.333 25.199 1.244 1.00 24.24 ? 386 PRO A CG 1 ATOM 5869 C CD . PRO A 1 378 ? 23.043 23.966 1.777 1.00 21.23 ? 386 PRO A CD 1 ATOM 5870 H HA . PRO A 1 378 ? 20.489 24.420 3.165 1.00 23.40 ? 386 PRO A HA 1 ATOM 5871 H HB2 . PRO A 1 378 ? 20.669 24.429 0.359 1.00 26.28 ? 386 PRO A HB2 1 ATOM 5872 H HB3 . PRO A 1 378 ? 20.353 25.665 1.320 1.00 26.28 ? 386 PRO A HB3 1 ATOM 5873 H HG2 . PRO A 1 378 ? 22.647 25.411 0.351 1.00 29.09 ? 386 PRO A HG2 1 ATOM 5874 H HG3 . PRO A 1 378 ? 22.471 25.953 1.839 1.00 29.09 ? 386 PRO A HG3 1 ATOM 5875 H HD2 . PRO A 1 378 ? 23.378 23.426 1.044 1.00 25.48 ? 386 PRO A HD2 1 ATOM 5876 H HD3 . PRO A 1 378 ? 23.755 24.222 2.385 1.00 25.48 ? 386 PRO A HD3 1 ATOM 5877 N N . HIS A 1 379 ? 19.705 21.931 1.278 1.00 18.47 ? 387 HIS A N 1 ATOM 5878 C CA . HIS A 1 379 ? 18.556 21.105 0.954 1.00 18.78 ? 387 HIS A CA 1 ATOM 5879 C C . HIS A 1 379 ? 18.145 20.230 2.127 1.00 16.40 ? 387 HIS A C 1 ATOM 5880 O O . HIS A 1 379 ? 16.961 19.908 2.261 1.00 16.92 ? 387 HIS A O 1 ATOM 5881 C CB . HIS A 1 379 ? 18.762 20.316 -0.347 1.00 23.72 ? 387 HIS A CB 1 ATOM 5882 C CG . HIS A 1 379 ? 19.553 19.046 -0.222 1.00 28.94 ? 387 HIS A CG 1 ATOM 5883 N ND1 . HIS A 1 379 ? 20.932 19.023 -0.188 1.00 32.66 ? 387 HIS A ND1 1 ATOM 5884 C CD2 . HIS A 1 379 ? 19.160 17.748 -0.218 1.00 32.03 ? 387 HIS A CD2 1 ATOM 5885 C CE1 . HIS A 1 379 ? 21.354 17.772 -0.119 1.00 33.18 ? 387 HIS A CE1 1 ATOM 5886 N NE2 . HIS A 1 379 ? 20.298 16.977 -0.142 1.00 33.58 ? 387 HIS A NE2 1 ATOM 5887 H H . HIS A 1 379 ? 20.445 21.705 0.903 1.00 22.16 ? 387 HIS A H 1 ATOM 5888 H HA . HIS A 1 379 ? 17.810 21.703 0.791 1.00 22.54 ? 387 HIS A HA 1 ATOM 5889 H HB2 . HIS A 1 379 ? 17.891 20.081 -0.703 1.00 28.46 ? 387 HIS A HB2 1 ATOM 5890 H HB3 . HIS A 1 379 ? 19.227 20.886 -0.979 1.00 28.46 ? 387 HIS A HB3 1 ATOM 5891 H HD1 . HIS A 1 379 ? 21.440 19.717 -0.189 1.00 39.19 ? 387 HIS A HD1 1 ATOM 5892 H HD2 . HIS A 1 379 ? 18.284 17.437 -0.242 1.00 38.44 ? 387 HIS A HD2 1 ATOM 5893 H HE1 . HIS A 1 379 ? 22.241 17.498 -0.070 1.00 39.82 ? 387 HIS A HE1 1 ATOM 5894 N N . ILE A 1 380 ? 19.081 19.872 3.001 1.00 15.30 ? 388 ILE A N 1 ATOM 5895 C CA . ILE A 1 380 ? 18.744 19.072 4.174 1.00 14.71 ? 388 ILE A CA 1 ATOM 5896 C C . ILE A 1 380 ? 18.129 19.943 5.253 1.00 14.70 ? 388 ILE A C 1 ATOM 5897 O O . ILE A 1 380 ? 17.153 19.544 5.895 1.00 14.20 ? 388 ILE A O 1 ATOM 5898 C CB . ILE A 1 380 ? 19.971 18.286 4.675 1.00 15.75 ? 388 ILE A CB 1 ATOM 5899 C CG1 . ILE A 1 380 ? 20.515 17.366 3.582 1.00 16.73 ? 388 ILE A CG1 1 ATOM 5900 C CG2 . ILE A 1 380 ? 19.594 17.474 5.904 1.00 15.20 ? 388 ILE A CG2 1 ATOM 5901 C CD1 . ILE A 1 380 ? 19.527 16.331 3.097 1.00 19.02 ? 388 ILE A CD1 1 ATOM 5902 H H . ILE A 1 380 ? 19.913 20.079 2.938 1.00 18.36 ? 388 ILE A H 1 ATOM 5903 H HA . ILE A 1 380 ? 18.074 18.421 3.914 1.00 17.65 ? 388 ILE A HA 1 ATOM 5904 H HB . ILE A 1 380 ? 20.664 18.919 4.922 1.00 18.90 ? 388 ILE A HB 1 ATOM 5905 H HG12 . ILE A 1 380 ? 20.775 17.907 2.820 1.00 20.08 ? 388 ILE A HG12 1 ATOM 5906 H HG13 . ILE A 1 380 ? 21.290 16.895 3.929 1.00 20.08 ? 388 ILE A HG13 1 ATOM 5907 H HG21 . ILE A 1 380 ? 20.374 16.985 6.210 1.00 18.24 ? 388 ILE A HG21 1 ATOM 5908 H HG22 . ILE A 1 380 ? 19.288 18.078 6.599 1.00 18.24 ? 388 ILE A HG22 1 ATOM 5909 H HG23 . ILE A 1 380 ? 18.886 16.855 5.668 1.00 18.24 ? 388 ILE A HG23 1 ATOM 5910 H HD11 . ILE A 1 380 ? 19.947 15.791 2.409 1.00 22.83 ? 388 ILE A HD11 1 ATOM 5911 H HD12 . ILE A 1 380 ? 19.265 15.770 3.844 1.00 22.83 ? 388 ILE A HD12 1 ATOM 5912 H HD13 . ILE A 1 380 ? 18.749 16.783 2.734 1.00 22.83 ? 388 ILE A HD13 1 ATOM 5913 N N . LEU A 1 381 ? 18.636 21.165 5.425 1.00 14.29 ? 389 LEU A N 1 ATOM 5914 C CA . LEU A 1 381 ? 17.956 22.120 6.282 1.00 14.07 ? 389 LEU A CA 1 ATOM 5915 C C . LEU A 1 381 ? 16.497 22.255 5.862 1.00 13.44 ? 389 LEU A C 1 ATOM 5916 O O . LEU A 1 381 ? 15.597 22.254 6.697 1.00 13.23 ? 389 LEU A O 1 ATOM 5917 C CB . LEU A 1 381 ? 18.635 23.481 6.234 1.00 14.96 ? 389 LEU A CB 1 ATOM 5918 C CG . LEU A 1 381 ? 17.918 24.600 6.993 1.00 15.91 ? 389 LEU A CG 1 ATOM 5919 C CD1 . LEU A 1 381 ? 17.823 24.321 8.481 1.00 17.50 ? 389 LEU A CD1 1 ATOM 5920 C CD2 . LEU A 1 381 ? 18.560 25.939 6.684 1.00 17.90 ? 389 LEU A CD2 1 ATOM 5921 H H . LEU A 1 381 ? 19.359 21.456 5.062 1.00 17.15 ? 389 LEU A H 1 ATOM 5922 H HA . LEU A 1 381 ? 17.980 21.801 7.198 1.00 16.88 ? 389 LEU A HA 1 ATOM 5923 H HB2 . LEU A 1 381 ? 19.523 23.394 6.615 1.00 17.96 ? 389 LEU A HB2 1 ATOM 5924 H HB3 . LEU A 1 381 ? 18.706 23.757 5.307 1.00 17.96 ? 389 LEU A HB3 1 ATOM 5925 H HG . LEU A 1 381 ? 17.008 24.644 6.660 1.00 19.09 ? 389 LEU A HG 1 ATOM 5926 H HD11 . LEU A 1 381 ? 17.361 25.059 8.910 1.00 21.00 ? 389 LEU A HD11 1 ATOM 5927 H HD12 . LEU A 1 381 ? 17.329 23.498 8.616 1.00 21.00 ? 389 LEU A HD12 1 ATOM 5928 H HD13 . LEU A 1 381 ? 18.718 24.235 8.843 1.00 21.00 ? 389 LEU A HD13 1 ATOM 5929 H HD21 . LEU A 1 381 ? 18.092 26.634 7.173 1.00 21.47 ? 389 LEU A HD21 1 ATOM 5930 H HD22 . LEU A 1 381 ? 19.491 25.912 6.955 1.00 21.47 ? 389 LEU A HD22 1 ATOM 5931 H HD23 . LEU A 1 381 ? 18.498 26.106 5.730 1.00 21.47 ? 389 LEU A HD23 1 ATOM 5932 N N . GLN A 1 382 ? 16.244 22.460 4.569 1.00 14.18 ? 390 GLN A N 1 ATOM 5933 C CA . GLN A 1 382 ? 14.876 22.726 4.139 1.00 14.36 ? 390 GLN A CA 1 ATOM 5934 C C . GLN A 1 382 ? 13.993 21.503 4.323 1.00 12.21 ? 390 GLN A C 1 ATOM 5935 O O . GLN A 1 382 ? 12.810 21.634 4.652 1.00 12.48 ? 390 GLN A O 1 ATOM 5936 C CB . GLN A 1 382 ? 14.876 23.230 2.693 1.00 16.15 ? 390 GLN A CB 1 ATOM 5937 C CG . GLN A 1 382 ? 13.483 23.635 2.216 1.00 16.41 ? 390 GLN A CG 1 ATOM 5938 C CD . GLN A 1 382 ? 12.904 24.805 2.979 1.00 16.97 ? 390 GLN A CD 1 ATOM 5939 O OE1 . GLN A 1 382 ? 13.628 25.553 3.641 1.00 18.68 ? 390 GLN A OE1 1 ATOM 5940 N NE2 . GLN A 1 382 ? 11.596 24.979 2.896 1.00 16.62 ? 390 GLN A NE2 1 ATOM 5941 H H . GLN A 1 382 ? 16.830 22.450 3.939 1.00 17.02 ? 390 GLN A H 1 ATOM 5942 H HA . GLN A 1 382 ? 14.512 23.434 4.693 1.00 17.23 ? 390 GLN A HA 1 ATOM 5943 H HB2 . GLN A 1 382 ? 15.453 24.006 2.627 1.00 19.38 ? 390 GLN A HB2 1 ATOM 5944 H HB3 . GLN A 1 382 ? 15.199 22.524 2.111 1.00 19.38 ? 390 GLN A HB3 1 ATOM 5945 H HG2 . GLN A 1 382 ? 13.531 23.884 1.280 1.00 19.70 ? 390 GLN A HG2 1 ATOM 5946 H HG3 . GLN A 1 382 ? 12.882 22.881 2.326 1.00 19.70 ? 390 GLN A HG3 1 ATOM 5947 H HE21 . GLN A 1 382 ? 11.119 24.440 2.425 1.00 19.95 ? 390 GLN A HE21 1 ATOM 5948 H HE22 . GLN A 1 382 ? 11.221 25.631 3.313 1.00 19.95 ? 390 GLN A HE22 1 ATOM 5949 N N . ARG A 1 383 ? 14.538 20.321 4.065 1.00 12.88 ? 391 ARG A N 1 ATOM 5950 C CA . ARG A 1 383 ? 13.813 19.079 4.284 1.00 13.41 ? 391 ARG A CA 1 ATOM 5951 C C . ARG A 1 383 ? 13.399 18.947 5.745 1.00 11.78 ? 391 ARG A C 1 ATOM 5952 O O . ARG A 1 383 ? 12.226 18.731 6.059 1.00 12.59 ? 391 ARG A O 1 ATOM 5953 C CB . ARG A 1 383 ? 14.685 17.913 3.834 1.00 13.46 ? 391 ARG A CB 1 ATOM 5954 C CG . ARG A 1 383 ? 14.084 16.540 4.011 1.00 14.77 ? 391 ARG A CG 1 ATOM 5955 C CD . ARG A 1 383 ? 15.004 15.439 3.489 1.00 15.24 ? 391 ARG A CD 1 ATOM 5956 N NE . ARG A 1 383 ? 15.279 15.622 2.071 1.00 15.40 ? 391 ARG A NE 1 ATOM 5957 C CZ . ARG A 1 383 ? 16.205 14.983 1.372 1.00 16.11 ? 391 ARG A CZ 1 ATOM 5958 N NH1 . ARG A 1 383 ? 17.003 14.102 1.943 1.00 17.33 ? 391 ARG A NH1 1 ATOM 5959 N NH2 . ARG A 1 383 ? 16.299 15.233 0.074 1.00 18.80 ? 391 ARG A NH2 1 ATOM 5960 H H . ARG A 1 383 ? 15.335 20.211 3.760 1.00 15.46 ? 391 ARG A H 1 ATOM 5961 H HA . ARG A 1 383 ? 13.008 19.081 3.743 1.00 16.09 ? 391 ARG A HA 1 ATOM 5962 H HB2 . ARG A 1 383 ? 14.881 18.024 2.890 1.00 16.15 ? 391 ARG A HB2 1 ATOM 5963 H HB3 . ARG A 1 383 ? 15.512 17.935 4.340 1.00 16.15 ? 391 ARG A HB3 1 ATOM 5964 H HG2 . ARG A 1 383 ? 13.928 16.380 4.955 1.00 17.72 ? 391 ARG A HG2 1 ATOM 5965 H HG3 . ARG A 1 383 ? 13.248 16.492 3.521 1.00 17.72 ? 391 ARG A HG3 1 ATOM 5966 H HD2 . ARG A 1 383 ? 15.846 15.468 3.970 1.00 18.29 ? 391 ARG A HD2 1 ATOM 5967 H HD3 . ARG A 1 383 ? 14.576 14.577 3.609 1.00 18.29 ? 391 ARG A HD3 1 ATOM 5968 H HE . ARG A 1 383 ? 14.798 16.197 1.650 1.00 18.48 ? 391 ARG A HE 1 ATOM 5969 H HH11 . ARG A 1 383 ? 16.928 13.935 2.783 1.00 20.80 ? 391 ARG A HH11 1 ATOM 5970 H HH12 . ARG A 1 383 ? 17.600 13.698 1.475 1.00 20.80 ? 391 ARG A HH12 1 ATOM 5971 H HH21 . ARG A 1 383 ? 15.779 15.813 -0.291 1.00 22.56 ? 391 ARG A HH21 1 ATOM 5972 H HH22 . ARG A 1 383 ? 16.902 14.840 -0.397 1.00 22.56 ? 391 ARG A HH22 1 ATOM 5973 N N . TYR A 1 384 ? 14.364 19.103 6.657 1.00 12.23 ? 392 TYR A N 1 ATOM 5974 C CA . TYR A 1 384 ? 14.076 19.110 8.090 1.00 12.06 ? 392 TYR A CA 1 ATOM 5975 C C . TYR A 1 384 ? 13.014 20.156 8.424 1.00 11.52 ? 392 TYR A C 1 ATOM 5976 O O . TYR A 1 384 ? 12.094 19.897 9.197 1.00 12.00 ? 392 TYR A O 1 ATOM 5977 C CB . TYR A 1 384 ? 15.389 19.382 8.859 1.00 12.04 ? 392 TYR A CB 1 ATOM 5978 C CG . TYR A 1 384 ? 15.120 19.913 10.235 1.00 11.94 ? 392 TYR A CG 1 ATOM 5979 C CD1 . TYR A 1 384 ? 14.808 19.062 11.299 1.00 12.42 ? 392 TYR A CD1 1 ATOM 5980 C CD2 . TYR A 1 384 ? 15.110 21.284 10.471 1.00 11.99 ? 392 TYR A CD2 1 ATOM 5981 C CE1 . TYR A 1 384 ? 14.488 19.582 12.553 1.00 11.96 ? 392 TYR A CE1 1 ATOM 5982 C CE2 . TYR A 1 384 ? 14.767 21.803 11.680 1.00 12.78 ? 392 TYR A CE2 1 ATOM 5983 C CZ . TYR A 1 384 ? 14.450 20.952 12.721 1.00 12.51 ? 392 TYR A CZ 1 ATOM 5984 O OH . TYR A 1 384 ? 14.099 21.437 13.964 1.00 13.01 ? 392 TYR A OH 1 ATOM 5985 H H . TYR A 1 384 ? 15.197 19.207 6.468 1.00 14.68 ? 392 TYR A H 1 ATOM 5986 H HA . TYR A 1 384 ? 13.741 18.239 8.356 1.00 14.48 ? 392 TYR A HA 1 ATOM 5987 H HB2 . TYR A 1 384 ? 15.887 18.554 8.945 1.00 14.44 ? 392 TYR A HB2 1 ATOM 5988 H HB3 . TYR A 1 384 ? 15.912 20.041 8.376 1.00 14.44 ? 392 TYR A HB3 1 ATOM 5989 H HD1 . TYR A 1 384 ? 14.798 18.142 11.165 1.00 14.91 ? 392 TYR A HD1 1 ATOM 5990 H HD2 . TYR A 1 384 ? 15.282 21.863 9.765 1.00 14.39 ? 392 TYR A HD2 1 ATOM 5991 H HE1 . TYR A 1 384 ? 14.262 19.015 13.255 1.00 14.35 ? 392 TYR A HE1 1 ATOM 5992 H HE2 . TYR A 1 384 ? 14.757 22.724 11.808 1.00 15.33 ? 392 TYR A HE2 1 ATOM 5993 H HH . TYR A 1 384 ? 14.107 22.277 13.957 1.00 15.61 ? 392 TYR A HH 1 ATOM 5994 N N . TYR A 1 385 ? 13.123 21.350 7.828 1.00 12.53 ? 393 TYR A N 1 ATOM 5995 C CA . TYR A 1 385 ? 12.222 22.438 8.165 1.00 12.10 ? 393 TYR A CA 1 ATOM 5996 C C . TYR A 1 385 ? 10.800 22.133 7.720 1.00 12.43 ? 393 TYR A C 1 ATOM 5997 O O . TYR A 1 385 ? 9.843 22.369 8.463 1.00 12.53 ? 393 TYR A O 1 ATOM 5998 C CB . TYR A 1 385 ? 12.709 23.726 7.534 1.00 12.69 ? 393 TYR A CB 1 ATOM 5999 C CG . TYR A 1 385 ? 11.784 24.880 7.825 1.00 14.25 ? 393 TYR A CG 1 ATOM 6000 C CD1 . TYR A 1 385 ? 11.667 25.391 9.120 1.00 15.60 ? 393 TYR A CD1 1 ATOM 6001 C CD2 . TYR A 1 385 ? 11.007 25.440 6.833 1.00 16.79 ? 393 TYR A CD2 1 ATOM 6002 C CE1 . TYR A 1 385 ? 10.822 26.446 9.407 1.00 18.59 ? 393 TYR A CE1 1 ATOM 6003 C CE2 . TYR A 1 385 ? 10.154 26.487 7.122 1.00 20.04 ? 393 TYR A CE2 1 ATOM 6004 C CZ . TYR A 1 385 ? 10.076 26.990 8.401 1.00 21.14 ? 393 TYR A CZ 1 ATOM 6005 O OH . TYR A 1 385 ? 9.236 28.039 8.703 1.00 26.40 ? 393 TYR A OH 1 ATOM 6006 H H . TYR A 1 385 ? 13.709 21.546 7.230 1.00 15.03 ? 393 TYR A H 1 ATOM 6007 H HA . TYR A 1 385 ? 12.217 22.558 9.127 1.00 14.53 ? 393 TYR A HA 1 ATOM 6008 H HB2 . TYR A 1 385 ? 13.585 23.943 7.889 1.00 15.23 ? 393 TYR A HB2 1 ATOM 6009 H HB3 . TYR A 1 385 ? 12.756 23.611 6.572 1.00 15.23 ? 393 TYR A HB3 1 ATOM 6010 H HD1 . TYR A 1 385 ? 12.183 25.025 9.801 1.00 18.73 ? 393 TYR A HD1 1 ATOM 6011 H HD2 . TYR A 1 385 ? 11.060 25.112 5.964 1.00 20.15 ? 393 TYR A HD2 1 ATOM 6012 H HE1 . TYR A 1 385 ? 10.764 26.782 10.272 1.00 22.31 ? 393 TYR A HE1 1 ATOM 6013 H HE2 . TYR A 1 385 ? 9.643 26.868 6.444 1.00 24.04 ? 393 TYR A HE2 1 ATOM 6014 H HH . TYR A 1 385 ? 8.830 28.291 8.012 1.00 31.68 ? 393 TYR A HH 1 ATOM 6015 N N . VAL A 1 386 ? 10.642 21.600 6.514 1.00 12.33 ? 394 VAL A N 1 ATOM 6016 C CA . VAL A 1 386 ? 9.308 21.221 6.054 1.00 12.53 ? 394 VAL A CA 1 ATOM 6017 C C . VAL A 1 386 ? 8.714 20.177 6.990 1.00 11.55 ? 394 VAL A C 1 ATOM 6018 O O . VAL A 1 386 ? 7.558 20.282 7.416 1.00 12.16 ? 394 VAL A O 1 ATOM 6019 C CB . VAL A 1 386 ? 9.372 20.740 4.598 1.00 12.80 ? 394 VAL A CB 1 ATOM 6020 C CG1 . VAL A 1 386 ? 8.035 20.155 4.158 1.00 13.54 ? 394 VAL A CG1 1 ATOM 6021 C CG2 . VAL A 1 386 ? 9.707 21.923 3.679 1.00 14.82 ? 394 VAL A CG2 1 ATOM 6022 H H . VAL A 1 386 ? 11.275 21.449 5.952 1.00 14.79 ? 394 VAL A H 1 ATOM 6023 H HA . VAL A 1 386 ? 8.735 22.003 6.082 1.00 15.03 ? 394 VAL A HA 1 ATOM 6024 H HB . VAL A 1 386 ? 10.060 20.063 4.503 1.00 15.36 ? 394 VAL A HB 1 ATOM 6025 H HG11 . VAL A 1 386 ? 8.107 19.861 3.237 1.00 16.24 ? 394 VAL A HG11 1 ATOM 6026 H HG12 . VAL A 1 386 ? 7.817 19.402 4.730 1.00 16.24 ? 394 VAL A HG12 1 ATOM 6027 H HG13 . VAL A 1 386 ? 7.351 20.839 4.235 1.00 16.24 ? 394 VAL A HG13 1 ATOM 6028 H HG21 . VAL A 1 386 ? 9.745 21.609 2.762 1.00 17.78 ? 394 VAL A HG21 1 ATOM 6029 H HG22 . VAL A 1 386 ? 9.017 22.599 3.770 1.00 17.78 ? 394 VAL A HG22 1 ATOM 6030 H HG23 . VAL A 1 386 ? 10.567 22.291 3.939 1.00 17.78 ? 394 VAL A HG23 1 ATOM 6031 N N . TYR A 1 387 ? 9.497 19.158 7.335 1.00 11.60 ? 395 TYR A N 1 ATOM 6032 C CA . TYR A 1 387 ? 9.004 18.134 8.243 1.00 11.15 ? 395 TYR A CA 1 ATOM 6033 C C . TYR A 1 387 ? 8.737 18.673 9.641 1.00 10.80 ? 395 TYR A C 1 ATOM 6034 O O . TYR A 1 387 ? 7.907 18.127 10.368 1.00 11.19 ? 395 TYR A O 1 ATOM 6035 C CB . TYR A 1 387 ? 9.961 16.945 8.283 1.00 11.79 ? 395 TYR A CB 1 ATOM 6036 C CG . TYR A 1 387 ? 10.179 16.232 6.960 1.00 11.93 ? 395 TYR A CG 1 ATOM 6037 C CD1 . TYR A 1 387 ? 9.253 16.274 5.934 1.00 13.28 ? 395 TYR A CD1 1 ATOM 6038 C CD2 . TYR A 1 387 ? 11.312 15.470 6.769 1.00 12.75 ? 395 TYR A CD2 1 ATOM 6039 C CE1 . TYR A 1 387 ? 9.468 15.610 4.749 1.00 15.11 ? 395 TYR A CE1 1 ATOM 6040 C CE2 . TYR A 1 387 ? 11.531 14.795 5.592 1.00 13.25 ? 395 TYR A CE2 1 ATOM 6041 C CZ . TYR A 1 387 ? 10.610 14.875 4.569 1.00 14.91 ? 395 TYR A CZ 1 ATOM 6042 O OH . TYR A 1 387 ? 10.803 14.174 3.388 1.00 17.03 ? 395 TYR A OH 1 ATOM 6043 H H . TYR A 1 387 ? 10.304 19.039 7.062 1.00 13.91 ? 395 TYR A H 1 ATOM 6044 H HA . TYR A 1 387 ? 8.158 17.808 7.897 1.00 13.38 ? 395 TYR A HA 1 ATOM 6045 H HB2 . TYR A 1 387 ? 10.826 17.258 8.590 1.00 14.14 ? 395 TYR A HB2 1 ATOM 6046 H HB3 . TYR A 1 387 ? 9.612 16.293 8.910 1.00 14.14 ? 395 TYR A HB3 1 ATOM 6047 H HD1 . TYR A 1 387 ? 8.479 16.779 6.039 1.00 15.93 ? 395 TYR A HD1 1 ATOM 6048 H HD2 . TYR A 1 387 ? 11.945 15.418 7.448 1.00 15.29 ? 395 TYR A HD2 1 ATOM 6049 H HE1 . TYR A 1 387 ? 8.834 15.657 4.071 1.00 18.14 ? 395 TYR A HE1 1 ATOM 6050 H HE2 . TYR A 1 387 ? 12.306 14.293 5.482 1.00 15.90 ? 395 TYR A HE2 1 ATOM 6051 H HH . TYR A 1 387 ? 11.539 13.770 3.410 1.00 20.44 ? 395 TYR A HH 1 ATOM 6052 N N . ASN A 1 388 ? 9.367 19.780 10.011 1.00 10.76 ? 396 ASN A N 1 ATOM 6053 C CA . ASN A 1 388 ? 9.194 20.308 11.361 1.00 11.03 ? 396 ASN A CA 1 ATOM 6054 C C . ASN A 1 388 ? 7.733 20.669 11.641 1.00 10.94 ? 396 ASN A C 1 ATOM 6055 O O . ASN A 1 388 ? 7.241 20.466 12.755 1.00 11.64 ? 396 ASN A O 1 ATOM 6056 C CB . ASN A 1 388 ? 10.136 21.489 11.568 1.00 11.88 ? 396 ASN A CB 1 ATOM 6057 C CG . ASN A 1 388 ? 9.986 22.136 12.929 1.00 12.19 ? 396 ASN A CG 1 ATOM 6058 O OD1 . ASN A 1 388 ? 9.468 23.232 13.070 1.00 13.70 ? 396 ASN A OD1 1 ATOM 6059 N ND2 . ASN A 1 388 ? 10.521 21.483 13.937 1.00 12.28 ? 396 ASN A ND2 1 ATOM 6060 H H . ASN A 1 388 ? 9.893 20.240 9.510 1.00 12.91 ? 396 ASN A H 1 ATOM 6061 H HA . ASN A 1 388 ? 9.448 19.619 11.994 1.00 13.24 ? 396 ASN A HA 1 ATOM 6062 H HB2 . ASN A 1 388 ? 11.051 21.180 11.484 1.00 14.26 ? 396 ASN A HB2 1 ATOM 6063 H HB3 . ASN A 1 388 ? 9.950 22.162 10.895 1.00 14.26 ? 396 ASN A HB3 1 ATOM 6064 H HD21 . ASN A 1 388 ? 10.467 21.802 14.734 1.00 14.74 ? 396 ASN A HD21 1 ATOM 6065 H HD22 . ASN A 1 388 ? 10.924 20.736 13.799 1.00 14.74 ? 396 ASN A HD22 1 ATOM 6066 N N . SER A 1 389 ? 7.023 21.214 10.638 1.00 11.49 ? 397 SER A N 1 ATOM 6067 C CA . SER A 1 389 ? 5.615 21.546 10.738 1.00 11.72 ? 397 SER A CA 1 ATOM 6068 C C . SER A 1 389 ? 4.719 20.433 10.204 1.00 11.35 ? 397 SER A C 1 ATOM 6069 O O . SER A 1 389 ? 3.541 20.673 9.926 1.00 11.94 ? 397 SER A O 1 ATOM 6070 C CB . SER A 1 389 ? 5.324 22.856 10.004 1.00 13.18 ? 397 SER A CB 1 ATOM 6071 O OG . SER A 1 389 ? 5.428 22.691 8.585 1.00 14.52 ? 397 SER A OG 1 ATOM 6072 H H . SER A 1 389 ? 7.359 21.403 9.869 1.00 13.78 ? 397 SER A H 1 ATOM 6073 H HA . SER A 1 389 ? 5.394 21.678 11.673 1.00 14.07 ? 397 SER A HA 1 ATOM 6074 H HB2 . SER A 1 389 ? 4.424 23.145 10.221 1.00 15.81 ? 397 SER A HB2 1 ATOM 6075 H HB3 . SER A 1 389 ? 5.965 23.526 10.290 1.00 15.81 ? 397 SER A HB3 1 ATOM 6076 H HG . SER A 1 389 ? 6.203 22.442 8.380 1.00 17.42 ? 397 SER A HG 1 ATOM 6077 N N . VAL A 1 390 ? 5.265 19.235 10.047 1.00 11.68 ? 398 VAL A N 1 ATOM 6078 C CA . VAL A 1 390 ? 4.536 18.104 9.466 1.00 11.56 ? 398 VAL A CA 1 ATOM 6079 C C . VAL A 1 390 ? 4.051 18.494 8.071 1.00 11.31 ? 398 VAL A C 1 ATOM 6080 O O . VAL A 1 390 ? 2.915 18.232 7.674 1.00 12.13 ? 398 VAL A O 1 ATOM 6081 C CB . VAL A 1 390 ? 3.433 17.531 10.394 1.00 11.35 ? 398 VAL A CB 1 ATOM 6082 C CG1 . VAL A 1 390 ? 3.096 16.117 9.938 1.00 11.44 ? 398 VAL A CG1 1 ATOM 6083 C CG2 . VAL A 1 390 ? 3.885 17.523 11.849 1.00 11.93 ? 398 VAL A CG2 1 ATOM 6084 H H . VAL A 1 390 ? 6.073 19.043 10.272 1.00 14.01 ? 398 VAL A H 1 ATOM 6085 H HA . VAL A 1 390 ? 5.176 17.386 9.338 1.00 13.87 ? 398 VAL A HA 1 ATOM 6086 H HB . VAL A 1 390 ? 2.634 18.077 10.322 1.00 13.62 ? 398 VAL A HB 1 ATOM 6087 H HG11 . VAL A 1 390 ? 2.406 15.755 10.516 1.00 13.73 ? 398 VAL A HG11 1 ATOM 6088 H HG12 . VAL A 1 390 ? 2.778 16.148 9.022 1.00 13.73 ? 398 VAL A HG12 1 ATOM 6089 H HG13 . VAL A 1 390 ? 3.895 15.569 9.992 1.00 13.73 ? 398 VAL A HG13 1 ATOM 6090 H HG21 . VAL A 1 390 ? 3.173 17.160 12.399 1.00 14.32 ? 398 VAL A HG21 1 ATOM 6091 H HG22 . VAL A 1 390 ? 4.679 16.972 11.930 1.00 14.32 ? 398 VAL A HG22 1 ATOM 6092 H HG23 . VAL A 1 390 ? 4.084 18.432 12.123 1.00 14.32 ? 398 VAL A HG23 1 ATOM 6093 N N . SER A 1 391 ? 4.936 19.150 7.327 1.00 12.68 ? 399 SER A N 1 ATOM 6094 C CA . SER A 1 391 ? 4.720 19.468 5.922 1.00 13.65 ? 399 SER A CA 1 ATOM 6095 C C . SER A 1 391 ? 3.562 20.422 5.714 1.00 14.57 ? 399 SER A C 1 ATOM 6096 O O . SER A 1 391 ? 2.960 20.428 4.661 1.00 17.13 ? 399 SER A O 1 ATOM 6097 C CB . SER A 1 391 ? 4.607 18.198 5.085 1.00 14.53 ? 399 SER A CB 1 ATOM 6098 O OG . SER A 1 391 ? 5.796 17.418 5.210 1.00 14.64 ? 399 SER A OG 1 ATOM 6099 H H . SER A 1 391 ? 5.693 19.430 7.625 1.00 15.22 ? 399 SER A H 1 ATOM 6100 H HA . SER A 1 391 ? 5.512 19.931 5.607 1.00 16.38 ? 399 SER A HA 1 ATOM 6101 H HB2 . SER A 1 391 ? 3.850 17.678 5.397 1.00 17.43 ? 399 SER A HB2 1 ATOM 6102 H HB3 . SER A 1 391 ? 4.483 18.442 4.154 1.00 17.43 ? 399 SER A HB3 1 ATOM 6103 H HG . SER A 1 391 ? 5.915 17.203 6.013 1.00 17.56 ? 399 SER A HG 1 ATOM 6104 N N . TYR A 1 392 ? 3.333 21.313 6.672 1.00 14.06 ? 400 TYR A N 1 ATOM 6105 C CA . TYR A 1 392 ? 2.343 22.381 6.558 1.00 14.82 ? 400 TYR A CA 1 ATOM 6106 C C . TYR A 1 392 ? 2.905 23.605 5.859 1.00 16.36 ? 400 TYR A C 1 ATOM 6107 O O . TYR A 1 392 ? 2.247 24.169 4.986 1.00 18.42 ? 400 TYR A O 1 ATOM 6108 C CB . TYR A 1 392 ? 1.814 22.781 7.944 1.00 14.92 ? 400 TYR A CB 1 ATOM 6109 C CG . TYR A 1 392 ? 1.054 24.099 8.014 1.00 14.53 ? 400 TYR A CG 1 ATOM 6110 C CD1 . TYR A 1 392 ? -0.239 24.202 7.541 1.00 15.59 ? 400 TYR A CD1 1 ATOM 6111 C CD2 . TYR A 1 392 ? 1.619 25.221 8.608 1.00 16.18 ? 400 TYR A CD2 1 ATOM 6112 C CE1 . TYR A 1 392 ? -0.930 25.418 7.604 1.00 16.36 ? 400 TYR A CE1 1 ATOM 6113 C CE2 . TYR A 1 392 ? 0.945 26.406 8.691 1.00 17.63 ? 400 TYR A CE2 1 ATOM 6114 C CZ . TYR A 1 392 ? -0.333 26.498 8.199 1.00 17.25 ? 400 TYR A CZ 1 ATOM 6115 O OH . TYR A 1 392 ? -1.040 27.691 8.269 1.00 20.89 ? 400 TYR A OH 1 ATOM 6116 H H . TYR A 1 392 ? 3.753 21.319 7.423 1.00 16.87 ? 400 TYR A H 1 ATOM 6117 H HA . TYR A 1 392 ? 1.593 22.058 6.035 1.00 17.79 ? 400 TYR A HA 1 ATOM 6118 H HB2 . TYR A 1 392 ? 1.214 22.084 8.254 1.00 17.90 ? 400 TYR A HB2 1 ATOM 6119 H HB3 . TYR A 1 392 ? 2.568 22.849 8.550 1.00 17.90 ? 400 TYR A HB3 1 ATOM 6120 H HD1 . TYR A 1 392 ? -0.640 23.466 7.138 1.00 18.71 ? 400 TYR A HD1 1 ATOM 6121 H HD2 . TYR A 1 392 ? 2.484 25.168 8.945 1.00 19.42 ? 400 TYR A HD2 1 ATOM 6122 H HE1 . TYR A 1 392 ? -1.799 25.482 7.279 1.00 19.64 ? 400 TYR A HE1 1 ATOM 6123 H HE2 . TYR A 1 392 ? 1.348 27.146 9.085 1.00 21.15 ? 400 TYR A HE2 1 ATOM 6124 H HH . TYR A 1 392 ? -0.575 28.277 8.652 1.00 25.06 ? 400 TYR A HH 1 ATOM 6125 N N . ASN A 1 393 ? 4.114 23.999 6.217 1.00 17.62 ? 401 ASN A N 1 ATOM 6126 C CA . ASN A 1 393 ? 4.743 25.214 5.729 1.00 19.84 ? 401 ASN A CA 1 ATOM 6127 C C . ASN A 1 393 ? 5.950 24.866 4.867 1.00 20.37 ? 401 ASN A C 1 ATOM 6128 O O . ASN A 1 393 ? 6.915 24.266 5.349 1.00 22.06 ? 401 ASN A O 1 ATOM 6129 C CB . ASN A 1 393 ? 5.167 26.069 6.912 1.00 22.81 ? 401 ASN A CB 1 ATOM 6130 C CG . ASN A 1 393 ? 5.867 27.311 6.485 1.00 26.46 ? 401 ASN A CG 1 ATOM 6131 O OD1 . ASN A 1 393 ? 5.701 27.779 5.362 1.00 27.66 ? 401 ASN A OD1 1 ATOM 6132 N ND2 . ASN A 1 393 ? 6.681 27.840 7.365 1.00 29.95 ? 401 ASN A ND2 1 ATOM 6133 H H . ASN A 1 393 ? 4.611 23.560 6.765 1.00 21.15 ? 401 ASN A H 1 ATOM 6134 H HA . ASN A 1 393 ? 4.111 25.717 5.191 1.00 23.81 ? 401 ASN A HA 1 ATOM 6135 H HB2 . ASN A 1 393 ? 4.380 26.325 7.417 1.00 27.38 ? 401 ASN A HB2 1 ATOM 6136 H HB3 . ASN A 1 393 ? 5.772 25.559 7.472 1.00 27.38 ? 401 ASN A HB3 1 ATOM 6137 H HD21 . ASN A 1 393 ? 7.113 28.559 7.173 1.00 35.94 ? 401 ASN A HD21 1 ATOM 6138 H HD22 . ASN A 1 393 ? 6.784 27.470 8.134 1.00 35.94 ? 401 ASN A HD22 1 ATOM 6139 N N . HIS A 1 394 ? 5.911 25.292 3.613 1.00 20.25 ? 402 HIS A N 1 ATOM 6140 C CA . HIS A 1 394 ? 6.943 25.024 2.622 1.00 19.60 ? 402 HIS A CA 1 ATOM 6141 C C . HIS A 1 394 ? 7.808 26.228 2.296 1.00 20.45 ? 402 HIS A C 1 ATOM 6142 O O . HIS A 1 394 ? 8.643 26.149 1.386 1.00 22.12 ? 402 HIS A O 1 ATOM 6143 C CB . HIS A 1 394 ? 6.306 24.494 1.338 1.00 21.59 ? 402 HIS A CB 1 ATOM 6144 C CG . HIS A 1 394 ? 5.624 23.191 1.539 1.00 23.74 ? 402 HIS A CG 1 ATOM 6145 N ND1 . HIS A 1 394 ? 6.259 21.979 1.390 1.00 24.39 ? 402 HIS A ND1 1 ATOM 6146 C CD2 . HIS A 1 394 ? 4.354 22.912 1.893 1.00 26.25 ? 402 HIS A CD2 1 ATOM 6147 C CE1 . HIS A 1 394 ? 5.409 21.006 1.651 1.00 23.90 ? 402 HIS A CE1 1 ATOM 6148 N NE2 . HIS A 1 394 ? 4.243 21.542 1.956 1.00 27.15 ? 402 HIS A NE2 1 ATOM 6149 H H . HIS A 1 394 ? 5.262 25.762 3.298 1.00 24.30 ? 402 HIS A H 1 ATOM 6150 H HA . HIS A 1 394 ? 7.527 24.331 2.966 1.00 23.52 ? 402 HIS A HA 1 ATOM 6151 H HB2 . HIS A 1 394 ? 5.647 25.133 1.025 1.00 25.91 ? 402 HIS A HB2 1 ATOM 6152 H HB3 . HIS A 1 394 ? 6.996 24.373 0.668 1.00 25.91 ? 402 HIS A HB3 1 ATOM 6153 H HD2 . HIS A 1 394 ? 3.681 23.529 2.067 1.00 31.50 ? 402 HIS A HD2 1 ATOM 6154 H HE1 . HIS A 1 394 ? 5.596 20.096 1.614 1.00 28.67 ? 402 HIS A HE1 1 ATOM 6155 H HE2 . HIS A 1 394 ? 3.529 21.107 2.158 1.00 32.58 ? 402 HIS A HE2 1 ATOM 6156 N N . LEU A 1 395 ? 7.623 27.347 2.982 1.00 20.47 ? 403 LEU A N 1 ATOM 6157 C CA . LEU A 1 395 ? 8.488 28.490 2.764 1.00 21.13 ? 403 LEU A CA 1 ATOM 6158 C C . LEU A 1 395 ? 9.915 28.153 3.187 1.00 20.48 ? 403 LEU A C 1 ATOM 6159 O O . LEU A 1 395 ? 10.163 27.228 3.957 1.00 19.74 ? 403 LEU A O 1 ATOM 6160 C CB . LEU A 1 395 ? 7.963 29.693 3.533 1.00 23.18 ? 403 LEU A CB 1 ATOM 6161 C CG . LEU A 1 395 ? 6.559 30.166 3.129 1.00 25.55 ? 403 LEU A CG 1 ATOM 6162 C CD1 . LEU A 1 395 ? 6.111 31.323 4.001 1.00 27.06 ? 403 LEU A CD1 1 ATOM 6163 C CD2 . LEU A 1 395 ? 6.509 30.559 1.666 1.00 27.37 ? 403 LEU A CD2 1 ATOM 6164 H H . LEU A 1 395 ? 7.010 27.467 3.574 1.00 24.56 ? 403 LEU A H 1 ATOM 6165 H HA . LEU A 1 395 ? 8.494 28.711 1.819 1.00 25.36 ? 403 LEU A HA 1 ATOM 6166 H HB2 . LEU A 1 395 ? 7.935 29.468 4.476 1.00 27.81 ? 403 LEU A HB2 1 ATOM 6167 H HB3 . LEU A 1 395 ? 8.571 30.436 3.395 1.00 27.81 ? 403 LEU A HB3 1 ATOM 6168 H HG . LEU A 1 395 ? 5.934 29.436 3.261 1.00 30.66 ? 403 LEU A HG 1 ATOM 6169 H HD11 . LEU A 1 395 ? 5.224 31.601 3.725 1.00 32.47 ? 403 LEU A HD11 1 ATOM 6170 H HD12 . LEU A 1 395 ? 6.095 31.033 4.926 1.00 32.47 ? 403 LEU A HD12 1 ATOM 6171 H HD13 . LEU A 1 395 ? 6.736 32.057 3.895 1.00 32.47 ? 403 LEU A HD13 1 ATOM 6172 H HD21 . LEU A 1 395 ? 5.610 30.851 1.449 1.00 32.84 ? 403 LEU A HD21 1 ATOM 6173 H HD22 . LEU A 1 395 ? 7.138 31.282 1.512 1.00 32.84 ? 403 LEU A HD22 1 ATOM 6174 H HD23 . LEU A 1 395 ? 6.748 29.791 1.124 1.00 32.84 ? 403 LEU A HD23 1 ATOM 6175 N N . THR A 1 396 ? 10.857 28.905 2.634 1.00 20.78 ? 404 THR A N 1 ATOM 6176 C CA . THR A 1 396 ? 12.269 28.638 2.847 1.00 19.96 ? 404 THR A CA 1 ATOM 6177 C C . THR A 1 396 ? 12.703 29.058 4.243 1.00 19.79 ? 404 THR A C 1 ATOM 6178 O O . THR A 1 396 ? 12.467 30.196 4.668 1.00 21.72 ? 404 THR A O 1 ATOM 6179 C CB . THR A 1 396 ? 13.094 29.415 1.830 1.00 22.96 ? 404 THR A CB 1 ATOM 6180 O OG1 . THR A 1 396 ? 12.777 28.952 0.520 1.00 25.10 ? 404 THR A OG1 1 ATOM 6181 C CG2 . THR A 1 396 ? 14.577 29.219 2.087 1.00 22.55 ? 404 THR A CG2 1 ATOM 6182 H H . THR A 1 396 ? 10.701 29.582 2.127 1.00 24.94 ? 404 THR A H 1 ATOM 6183 H HA . THR A 1 396 ? 12.445 27.691 2.735 1.00 23.95 ? 404 THR A HA 1 ATOM 6184 H HB . THR A 1 396 ? 12.890 30.361 1.899 1.00 27.55 ? 404 THR A HB 1 ATOM 6185 H HG1 . THR A 1 396 ? 12.952 28.134 0.454 1.00 30.13 ? 404 THR A HG1 1 ATOM 6186 H HG21 . THR A 1 396 ? 15.095 29.717 1.435 1.00 27.06 ? 404 THR A HG21 1 ATOM 6187 H HG22 . THR A 1 396 ? 14.804 29.533 2.976 1.00 27.06 ? 404 THR A HG22 1 ATOM 6188 H HG23 . THR A 1 396 ? 14.804 28.278 2.017 1.00 27.06 ? 404 THR A HG23 1 ATOM 6189 N N . CYS A 1 397 ? 13.403 28.160 4.922 1.00 18.98 ? 405 CYS A N 1 ATOM 6190 C CA . CYS A 1 397 ? 13.997 28.473 6.213 1.00 20.03 ? 405 CYS A CA 1 ATOM 6191 C C . CYS A 1 397 ? 15.268 29.284 5.980 1.00 22.61 ? 405 CYS A C 1 ATOM 6192 O O . CYS A 1 397 ? 16.282 28.747 5.522 1.00 22.74 ? 405 CYS A O 1 ATOM 6193 C CB . CYS A 1 397 ? 14.276 27.175 6.965 1.00 18.88 ? 405 CYS A CB 1 ATOM 6194 S SG . CYS A 1 397 ? 15.039 27.348 8.607 1.00 19.43 ? 405 CYS A SG 1 ATOM 6195 H H . CYS A 1 397 ? 13.549 27.356 4.656 1.00 22.77 ? 405 CYS A H 1 ATOM 6196 H HA . CYS A 1 397 ? 13.379 29.008 6.735 1.00 24.04 ? 405 CYS A HA 1 ATOM 6197 H HB2 . CYS A 1 397 ? 13.435 26.707 7.086 1.00 22.66 ? 405 CYS A HB2 1 ATOM 6198 H HB3 . CYS A 1 397 ? 14.871 26.633 6.425 1.00 22.66 ? 405 CYS A HB3 1 ATOM 6199 N N . GLU A 1 398 ? 15.204 30.583 6.284 1.00 23.06 ? 406 GLU A N 1 ATOM 6200 C CA . GLU A 1 398 ? 16.294 31.515 6.033 1.00 26.26 ? 406 GLU A CA 1 ATOM 6201 C C . GLU A 1 398 ? 17.250 31.555 7.227 1.00 24.78 ? 406 GLU A C 1 ATOM 6202 O O . GLU A 1 398 ? 17.199 30.709 8.116 1.00 23.04 ? 406 GLU A O 1 ATOM 6203 C CB . GLU A 1 398 ? 15.728 32.899 5.721 1.00 31.46 ? 406 GLU A CB 1 ATOM 6204 C CG . GLU A 1 398 ? 14.680 32.917 4.622 1.00 35.30 ? 406 GLU A CG 1 ATOM 6205 C CD . GLU A 1 398 ? 15.299 32.925 3.253 1.00 41.51 ? 406 GLU A CD 1 ATOM 6206 O OE1 . GLU A 1 398 ? 16.466 32.490 3.145 1.00 43.59 ? 406 GLU A OE1 1 ATOM 6207 O OE2 . GLU A 1 398 ? 14.632 33.375 2.290 1.00 44.13 ? 406 GLU A OE2 1 ATOM 6208 H H . GLU A 1 398 ? 14.517 30.953 6.647 1.00 27.67 ? 406 GLU A H 1 ATOM 6209 H HA . GLU A 1 398 ? 16.794 31.214 5.259 1.00 31.51 ? 406 GLU A HA 1 ATOM 6210 H HB2 . GLU A 1 398 ? 15.319 33.255 6.524 1.00 37.75 ? 406 GLU A HB2 1 ATOM 6211 H HB3 . GLU A 1 398 ? 16.457 33.476 5.442 1.00 37.75 ? 406 GLU A HB3 1 ATOM 6212 H HG2 . GLU A 1 398 ? 14.124 32.126 4.698 1.00 42.36 ? 406 GLU A HG2 1 ATOM 6213 H HG3 . GLU A 1 398 ? 14.137 33.716 4.713 1.00 42.36 ? 406 GLU A HG3 1 ATOM 6214 N N . ASP A 1 399 ? 18.126 32.558 7.269 1.00 25.23 ? 407 ASP A N 1 ATOM 6215 C CA . ASP A 1 399 ? 19.255 32.515 8.201 1.00 26.47 ? 407 ASP A CA 1 ATOM 6216 C C . ASP A 1 399 ? 18.808 32.489 9.663 1.00 24.29 ? 407 ASP A C 1 ATOM 6217 O O . ASP A 1 399 ? 19.369 31.741 10.473 1.00 23.50 ? 407 ASP A O 1 ATOM 6218 C CB . ASP A 1 399 ? 20.187 33.707 7.968 1.00 32.37 ? 407 ASP A CB 1 ATOM 6219 C CG . ASP A 1 399 ? 21.174 33.482 6.839 1.00 38.88 ? 407 ASP A CG 1 ATOM 6220 O OD1 . ASP A 1 399 ? 21.247 32.368 6.284 1.00 42.39 ? 407 ASP A OD1 1 ATOM 6221 O OD2 . ASP A 1 399 ? 21.910 34.441 6.521 1.00 42.56 ? 407 ASP A OD2 1 ATOM 6222 H H . ASP A 1 399 ? 18.092 33.263 6.778 1.00 30.28 ? 407 ASP A H 1 ATOM 6223 H HA . ASP A 1 399 ? 19.764 31.706 8.034 1.00 31.76 ? 407 ASP A HA 1 ATOM 6224 H HB2 . ASP A 1 399 ? 19.652 34.486 7.747 1.00 38.84 ? 407 ASP A HB2 1 ATOM 6225 H HB3 . ASP A 1 399 ? 20.693 33.873 8.779 1.00 38.84 ? 407 ASP A HB3 1 ATOM 6226 N N . SER A 1 400 ? 17.837 33.323 10.044 1.00 24.92 ? 408 SER A N 1 ATOM 6227 C CA . SER A 1 400 ? 17.443 33.358 11.455 1.00 25.45 ? 408 SER A CA 1 ATOM 6228 C C . SER A 1 400 ? 16.695 32.087 11.849 1.00 22.17 ? 408 SER A C 1 ATOM 6229 O O . SER A 1 400 ? 16.898 31.546 12.942 1.00 21.06 ? 408 SER A O 1 ATOM 6230 C CB . SER A 1 400 ? 16.601 34.594 11.739 1.00 29.24 ? 408 SER A CB 1 ATOM 6231 O OG . SER A 1 400 ? 15.474 34.610 10.894 1.00 33.75 ? 408 SER A OG 1 ATOM 6232 H H . SER A 1 400 ? 17.406 33.860 9.528 1.00 29.91 ? 408 SER A H 1 ATOM 6233 H HA . SER A 1 400 ? 18.243 33.412 12.001 1.00 30.54 ? 408 SER A HA 1 ATOM 6234 H HB2 . SER A 1 400 ? 16.306 34.574 12.663 1.00 35.09 ? 408 SER A HB2 1 ATOM 6235 H HB3 . SER A 1 400 ? 17.133 35.388 11.574 1.00 35.09 ? 408 SER A HB3 1 ATOM 6236 H HG . SER A 1 400 ? 15.717 34.623 10.090 1.00 40.50 ? 408 SER A HG 1 ATOM 6237 N N . CYS A 1 401 ? 15.865 31.576 10.951 1.00 20.69 ? 409 CYS A N 1 ATOM 6238 C CA . CYS A 1 401 ? 15.239 30.274 11.144 1.00 18.66 ? 409 CYS A CA 1 ATOM 6239 C C . CYS A 1 401 ? 16.296 29.191 11.345 1.00 17.69 ? 409 CYS A C 1 ATOM 6240 O O . CYS A 1 401 ? 16.217 28.392 12.289 1.00 16.74 ? 409 CYS A O 1 ATOM 6241 C CB . CYS A 1 401 ? 14.360 29.997 9.915 1.00 20.37 ? 409 CYS A CB 1 ATOM 6242 S SG . CYS A 1 401 ? 13.679 28.347 9.786 1.00 20.25 ? 409 CYS A SG 1 ATOM 6243 H H . CYS A 1 401 ? 15.646 31.965 10.216 1.00 24.83 ? 409 CYS A H 1 ATOM 6244 H HA . CYS A 1 401 ? 14.671 30.300 11.930 1.00 22.39 ? 409 CYS A HA 1 ATOM 6245 H HB2 . CYS A 1 401 ? 13.614 30.616 9.928 1.00 24.44 ? 409 CYS A HB2 1 ATOM 6246 H HB3 . CYS A 1 401 ? 14.892 30.152 9.119 1.00 24.44 ? 409 CYS A HB3 1 ATOM 6247 N N . ARG A 1 402 ? 17.318 29.174 10.488 1.00 17.07 ? 410 ARG A N 1 ATOM 6248 C CA . ARG A 1 402 ? 18.352 28.152 10.587 1.00 17.28 ? 410 ARG A CA 1 ATOM 6249 C C . ARG A 1 402 ? 18.995 28.165 11.969 1.00 15.84 ? 410 ARG A C 1 ATOM 6250 O O . ARG A 1 402 ? 19.156 27.114 12.606 1.00 16.20 ? 410 ARG A O 1 ATOM 6251 C CB . ARG A 1 402 ? 19.404 28.363 9.510 1.00 17.98 ? 410 ARG A CB 1 ATOM 6252 C CG . ARG A 1 402 ? 20.581 27.436 9.645 1.00 18.83 ? 410 ARG A CG 1 ATOM 6253 C CD . ARG A 1 402 ? 21.652 27.776 8.653 1.00 19.44 ? 410 ARG A CD 1 ATOM 6254 N NE . ARG A 1 402 ? 22.825 26.993 8.995 1.00 22.31 ? 410 ARG A NE 1 ATOM 6255 C CZ . ARG A 1 402 ? 23.682 27.309 9.954 1.00 24.30 ? 410 ARG A CZ 1 ATOM 6256 N NH1 . ARG A 1 402 ? 23.553 28.443 10.633 1.00 25.68 ? 410 ARG A NH1 1 ATOM 6257 N NH2 . ARG A 1 402 ? 24.675 26.482 10.216 1.00 24.56 ? 410 ARG A NH2 1 ATOM 6258 H H . ARG A 1 402 ? 17.433 29.738 9.848 1.00 20.49 ? 410 ARG A H 1 ATOM 6259 H HA . ARG A 1 402 ? 17.950 27.279 10.450 1.00 20.73 ? 410 ARG A HA 1 ATOM 6260 H HB2 . ARG A 1 402 ? 19.000 28.210 8.641 1.00 21.58 ? 410 ARG A HB2 1 ATOM 6261 H HB3 . ARG A 1 402 ? 19.733 29.274 9.566 1.00 21.58 ? 410 ARG A HB3 1 ATOM 6262 H HG2 . ARG A 1 402 ? 20.954 27.517 10.537 1.00 22.60 ? 410 ARG A HG2 1 ATOM 6263 H HG3 . ARG A 1 402 ? 20.293 26.524 9.482 1.00 22.60 ? 410 ARG A HG3 1 ATOM 6264 H HD2 . ARG A 1 402 ? 21.364 27.539 7.757 1.00 23.32 ? 410 ARG A HD2 1 ATOM 6265 H HD3 . ARG A 1 402 ? 21.873 28.719 8.711 1.00 23.32 ? 410 ARG A HD3 1 ATOM 6266 H HE . ARG A 1 402 ? 22.974 26.275 8.546 1.00 26.77 ? 410 ARG A HE 1 ATOM 6267 H HH11 . ARG A 1 402 ? 22.894 28.970 10.469 1.00 30.81 ? 410 ARG A HH11 1 ATOM 6268 H HH12 . ARG A 1 402 ? 24.122 28.645 11.246 1.00 30.81 ? 410 ARG A HH12 1 ATOM 6269 H HH21 . ARG A 1 402 ? 24.762 25.758 9.761 1.00 29.48 ? 410 ARG A HH21 1 ATOM 6270 H HH22 . ARG A 1 402 ? 25.258 26.688 10.814 1.00 29.48 ? 410 ARG A HH22 1 ATOM 6271 N N . ILE A 1 403 ? 19.402 29.347 12.432 1.00 16.55 ? 411 ILE A N 1 ATOM 6272 C CA A ILE A 1 403 ? 20.109 29.416 13.706 0.47 17.23 ? 411 ILE A CA 1 ATOM 6273 C CA B ILE A 1 403 ? 20.107 29.431 13.708 0.53 16.71 ? 411 ILE A CA 1 ATOM 6274 C C . ILE A 1 403 ? 19.196 29.004 14.859 1.00 15.20 ? 411 ILE A C 1 ATOM 6275 O O . ILE A 1 403 ? 19.631 28.338 15.806 1.00 15.62 ? 411 ILE A O 1 ATOM 6276 C CB A ILE A 1 403 ? 20.748 30.803 13.909 0.47 21.56 ? 411 ILE A CB 1 ATOM 6277 C CB B ILE A 1 403 ? 20.664 30.860 13.898 0.53 20.43 ? 411 ILE A CB 1 ATOM 6278 C CG1 A ILE A 1 403 ? 21.794 30.750 15.021 0.47 24.79 ? 411 ILE A CG1 1 ATOM 6279 C CG1 B ILE A 1 403 ? 21.771 31.155 12.882 0.53 22.41 ? 411 ILE A CG1 1 ATOM 6280 C CG2 A ILE A 1 403 ? 19.716 31.841 14.257 0.47 21.44 ? 411 ILE A CG2 1 ATOM 6281 C CG2 B ILE A 1 403 ? 21.221 31.058 15.289 0.53 20.84 ? 411 ILE A CG2 1 ATOM 6282 C CD1 A ILE A 1 403 ? 23.034 29.972 14.667 0.47 26.59 ? 411 ILE A CD1 1 ATOM 6283 C CD1 B ILE A 1 403 ? 22.172 32.626 12.794 0.53 24.37 ? 411 ILE A CD1 1 ATOM 6284 H HA . ILE A 1 403 ? 20.848 28.797 13.683 1.00 20.05 ? 411 ILE A HA 1 ATOM 6285 H HB A ILE A 1 403 ? 21.186 31.066 13.084 0.47 25.88 ? 411 ILE A HB 1 ATOM 6286 H HB B ILE A 1 403 ? 19.943 31.493 13.761 0.53 24.52 ? 411 ILE A HB 1 ATOM 6287 H HG12 A ILE A 1 403 ? 22.066 31.656 15.236 0.47 29.75 ? 411 ILE A HG12 1 ATOM 6288 H HG12 B ILE A 1 403 ? 22.561 30.649 13.129 0.53 26.89 ? 411 ILE A HG12 1 ATOM 6289 H HG13 A ILE A 1 403 ? 21.397 30.333 15.801 0.47 29.75 ? 411 ILE A HG13 1 ATOM 6290 H HG13 B ILE A 1 403 ? 21.468 30.879 12.003 0.53 26.89 ? 411 ILE A HG13 1 ATOM 6291 H HG21 A ILE A 1 403 ? 20.157 32.697 14.376 0.47 25.73 ? 411 ILE A HG21 1 ATOM 6292 H HG21 B ILE A 1 403 ? 21.560 31.964 15.367 0.53 25.01 ? 411 ILE A HG21 1 ATOM 6293 H HG22 A ILE A 1 403 ? 19.071 31.899 13.535 0.47 25.73 ? 411 ILE A HG22 1 ATOM 6294 H HG22 B ILE A 1 403 ? 20.514 30.912 15.936 0.53 25.01 ? 411 ILE A HG22 1 ATOM 6295 H HG23 A ILE A 1 403 ? 19.271 31.581 15.079 0.47 25.73 ? 411 ILE A HG23 1 ATOM 6296 H HG23 B ILE A 1 403 ? 21.939 30.422 15.435 0.53 25.01 ? 411 ILE A HG23 1 ATOM 6297 H HD11 A ILE A 1 403 ? 23.643 29.987 15.423 0.47 31.91 ? 411 ILE A HD11 1 ATOM 6298 H HD11 B ILE A 1 403 ? 22.874 32.722 12.131 0.53 29.25 ? 411 ILE A HD11 1 ATOM 6299 H HD12 A ILE A 1 403 ? 22.785 29.057 14.462 0.47 31.91 ? 411 ILE A HD12 1 ATOM 6300 H HD12 B ILE A 1 403 ? 21.398 33.149 12.534 0.53 29.25 ? 411 ILE A HD12 1 ATOM 6301 H HD13 A ILE A 1 403 ? 23.455 30.382 13.895 0.47 31.91 ? 411 ILE A HD13 1 ATOM 6302 H HD13 B ILE A 1 403 ? 22.493 32.918 13.661 0.53 29.25 ? 411 ILE A HD13 1 ATOM 6303 N N . GLU A 1 404 ? 17.909 29.364 14.795 1.00 14.63 ? 412 GLU A N 1 ATOM 6304 C CA . GLU A 1 404 ? 16.991 28.990 15.866 1.00 15.00 ? 412 GLU A CA 1 ATOM 6305 C C . GLU A 1 404 ? 16.854 27.484 15.939 1.00 14.05 ? 412 GLU A C 1 ATOM 6306 O O . GLU A 1 404 ? 16.816 26.915 17.030 1.00 14.75 ? 412 GLU A O 1 ATOM 6307 C CB . GLU A 1 404 ? 15.634 29.682 15.689 1.00 15.83 ? 412 GLU A CB 1 ATOM 6308 C CG . GLU A 1 404 ? 15.712 31.165 16.011 1.00 18.73 ? 412 GLU A CG 1 ATOM 6309 C CD . GLU A 1 404 ? 14.403 31.917 15.966 1.00 22.66 ? 412 GLU A CD 1 ATOM 6310 O OE1 . GLU A 1 404 ? 13.394 31.418 15.439 1.00 24.01 ? 412 GLU A OE1 1 ATOM 6311 O OE2 . GLU A 1 404 ? 14.385 33.056 16.472 1.00 25.65 ? 412 GLU A OE2 1 ATOM 6312 H H . GLU A 1 404 ? 17.552 29.815 14.156 1.00 17.55 ? 412 GLU A H 1 ATOM 6313 H HA . GLU A 1 404 ? 17.364 29.290 16.710 1.00 18.01 ? 412 GLU A HA 1 ATOM 6314 H HB2 . GLU A 1 404 ? 15.345 29.587 14.768 1.00 19.00 ? 412 GLU A HB2 1 ATOM 6315 H HB3 . GLU A 1 404 ? 14.988 29.276 16.287 1.00 19.00 ? 412 GLU A HB3 1 ATOM 6316 H HG2 . GLU A 1 404 ? 16.073 31.265 16.906 1.00 22.47 ? 412 GLU A HG2 1 ATOM 6317 H HG3 . GLU A 1 404 ? 16.310 31.586 15.373 1.00 22.47 ? 412 GLU A HG3 1 ATOM 6318 N N . HIS A 1 405 ? 16.777 26.816 14.790 1.00 13.46 ? 413 HIS A N 1 ATOM 6319 C CA . HIS A 1 405 ? 16.639 25.363 14.818 1.00 13.06 ? 413 HIS A CA 1 ATOM 6320 C C . HIS A 1 405 ? 17.944 24.669 15.187 1.00 12.92 ? 413 HIS A C 1 ATOM 6321 O O . HIS A 1 405 ? 17.959 23.772 16.040 1.00 13.28 ? 413 HIS A O 1 ATOM 6322 C CB . HIS A 1 405 ? 16.121 24.853 13.486 1.00 13.33 ? 413 HIS A CB 1 ATOM 6323 C CG . HIS A 1 405 ? 14.672 25.133 13.274 1.00 13.66 ? 413 HIS A CG 1 ATOM 6324 N ND1 . HIS A 1 405 ? 13.691 24.218 13.606 1.00 13.10 ? 413 HIS A ND1 1 ATOM 6325 C CD2 . HIS A 1 405 ? 14.024 26.236 12.827 1.00 15.35 ? 413 HIS A CD2 1 ATOM 6326 C CE1 . HIS A 1 405 ? 12.506 24.740 13.345 1.00 13.61 ? 413 HIS A CE1 1 ATOM 6327 N NE2 . HIS A 1 405 ? 12.677 25.959 12.861 1.00 15.38 ? 413 HIS A NE2 1 ATOM 6328 H H . HIS A 1 405 ? 16.802 27.167 14.006 1.00 16.15 ? 413 HIS A H 1 ATOM 6329 H HA . HIS A 1 405 ? 15.984 25.129 15.494 1.00 15.67 ? 413 HIS A HA 1 ATOM 6330 H HB2 . HIS A 1 405 ? 16.616 25.283 12.771 1.00 16.00 ? 413 HIS A HB2 1 ATOM 6331 H HB3 . HIS A 1 405 ? 16.248 23.892 13.445 1.00 16.00 ? 413 HIS A HB3 1 ATOM 6332 H HD2 . HIS A 1 405 ? 14.418 27.024 12.528 1.00 18.42 ? 413 HIS A HD2 1 ATOM 6333 H HE1 . HIS A 1 405 ? 11.687 24.316 13.469 1.00 16.34 ? 413 HIS A HE1 1 ATOM 6334 H HE2 . HIS A 1 405 ? 12.050 26.495 12.620 1.00 18.45 ? 413 HIS A HE2 1 ATOM 6335 N N . VAL A 1 406 ? 19.039 25.037 14.530 1.00 13.08 ? 414 VAL A N 1 ATOM 6336 C CA . VAL A 1 406 ? 20.312 24.377 14.800 1.00 13.87 ? 414 VAL A CA 1 ATOM 6337 C C . VAL A 1 406 ? 20.703 24.532 16.266 1.00 13.29 ? 414 VAL A C 1 ATOM 6338 O O . VAL A 1 406 ? 21.123 23.572 16.920 1.00 13.73 ? 414 VAL A O 1 ATOM 6339 C CB . VAL A 1 406 ? 21.412 24.893 13.860 1.00 15.11 ? 414 VAL A CB 1 ATOM 6340 C CG1 . VAL A 1 406 ? 22.781 24.415 14.348 1.00 16.92 ? 414 VAL A CG1 1 ATOM 6341 C CG2 . VAL A 1 406 ? 21.178 24.407 12.437 1.00 16.97 ? 414 VAL A CG2 1 ATOM 6342 H H . VAL A 1 406 ? 19.072 25.654 13.932 1.00 15.69 ? 414 VAL A H 1 ATOM 6343 H HA . VAL A 1 406 ? 20.207 23.428 14.628 1.00 16.65 ? 414 VAL A HA 1 ATOM 6344 H HB . VAL A 1 406 ? 21.407 25.863 13.859 1.00 18.13 ? 414 VAL A HB 1 ATOM 6345 H HG11 . VAL A 1 406 ? 23.464 24.749 13.745 1.00 20.30 ? 414 VAL A HG11 1 ATOM 6346 H HG12 . VAL A 1 406 ? 22.933 24.756 15.243 1.00 20.30 ? 414 VAL A HG12 1 ATOM 6347 H HG13 . VAL A 1 406 ? 22.791 23.445 14.356 1.00 20.30 ? 414 VAL A HG13 1 ATOM 6348 H HG21 . VAL A 1 406 ? 21.885 24.748 11.868 1.00 20.36 ? 414 VAL A HG21 1 ATOM 6349 H HG22 . VAL A 1 406 ? 21.185 23.437 12.430 1.00 20.36 ? 414 VAL A HG22 1 ATOM 6350 H HG23 . VAL A 1 406 ? 20.318 24.735 12.129 1.00 20.36 ? 414 VAL A HG23 1 ATOM 6351 N N . CYS A 1 407 ? 20.565 25.733 16.812 1.00 12.95 ? 415 CYS A N 1 ATOM 6352 C CA . CYS A 1 407 ? 20.940 25.930 18.211 1.00 13.61 ? 415 CYS A CA 1 ATOM 6353 C C . CYS A 1 407 ? 20.052 25.137 19.167 1.00 13.53 ? 415 CYS A C 1 ATOM 6354 O O . CYS A 1 407 ? 20.543 24.612 20.169 1.00 13.67 ? 415 CYS A O 1 ATOM 6355 C CB . CYS A 1 407 ? 20.936 27.413 18.557 1.00 14.10 ? 415 CYS A CB 1 ATOM 6356 S SG . CYS A 1 407 ? 22.229 28.371 17.703 1.00 16.89 ? 415 CYS A SG 1 ATOM 6357 H H . CYS A 1 407 ? 20.265 26.433 16.412 1.00 15.54 ? 415 CYS A H 1 ATOM 6358 H HA . CYS A 1 407 ? 21.848 25.610 18.330 1.00 16.33 ? 415 CYS A HA 1 ATOM 6359 H HB2 . CYS A 1 407 ? 20.077 27.789 18.310 1.00 16.92 ? 415 CYS A HB2 1 ATOM 6360 H HB3 . CYS A 1 407 ? 21.076 27.512 19.511 1.00 16.92 ? 415 CYS A HB3 1 ATOM 6361 N N . ALA A 1 408 ? 18.743 25.067 18.902 1.00 12.71 ? 416 ALA A N 1 ATOM 6362 C CA . ALA A 1 408 ? 17.871 24.289 19.765 1.00 12.11 ? 416 ALA A CA 1 ATOM 6363 C C . ALA A 1 408 ? 18.187 22.806 19.690 1.00 11.60 ? 416 ALA A C 1 ATOM 6364 O O . ALA A 1 408 ? 18.098 22.113 20.695 1.00 12.82 ? 416 ALA A O 1 ATOM 6365 C CB . ALA A 1 408 ? 16.401 24.518 19.397 1.00 13.31 ? 416 ALA A CB 1 ATOM 6366 H H . ALA A 1 408 ? 18.349 25.453 18.242 1.00 15.25 ? 416 ALA A H 1 ATOM 6367 H HA . ALA A 1 408 ? 17.999 24.576 20.683 1.00 14.53 ? 416 ALA A HA 1 ATOM 6368 H HB1 . ALA A 1 408 ? 15.842 23.988 19.987 1.00 15.97 ? 416 ALA A HB1 1 ATOM 6369 H HB2 . ALA A 1 408 ? 16.192 25.459 19.500 1.00 15.97 ? 416 ALA A HB2 1 ATOM 6370 H HB3 . ALA A 1 408 ? 16.260 24.247 18.476 1.00 15.97 ? 416 ALA A HB3 1 ATOM 6371 N N . ILE A 1 409 ? 18.488 22.275 18.502 1.00 11.97 ? 417 ILE A N 1 ATOM 6372 C CA . ILE A 1 409 ? 18.813 20.858 18.369 1.00 12.00 ? 417 ILE A CA 1 ATOM 6373 C C . ILE A 1 409 ? 20.101 20.536 19.117 1.00 12.40 ? 417 ILE A C 1 ATOM 6374 O O . ILE A 1 409 ? 20.209 19.509 19.793 1.00 13.14 ? 417 ILE A O 1 ATOM 6375 C CB . ILE A 1 409 ? 18.950 20.468 16.882 1.00 11.74 ? 417 ILE A CB 1 ATOM 6376 C CG1 . ILE A 1 409 ? 17.612 20.573 16.175 1.00 11.67 ? 417 ILE A CG1 1 ATOM 6377 C CG2 . ILE A 1 409 ? 19.498 19.050 16.736 1.00 13.27 ? 417 ILE A CG2 1 ATOM 6378 C CD1 . ILE A 1 409 ? 17.739 20.560 14.654 1.00 13.97 ? 417 ILE A CD1 1 ATOM 6379 H H . ILE A 1 409 ? 18.510 22.713 17.762 1.00 14.36 ? 417 ILE A H 1 ATOM 6380 H HA . ILE A 1 409 ? 18.098 20.329 18.756 1.00 14.39 ? 417 ILE A HA 1 ATOM 6381 H HB . ILE A 1 409 ? 19.570 21.082 16.459 1.00 14.08 ? 417 ILE A HB 1 ATOM 6382 H HG12 . ILE A 1 409 ? 17.058 19.821 16.436 1.00 14.01 ? 417 ILE A HG12 1 ATOM 6383 H HG13 . ILE A 1 409 ? 17.185 21.405 16.432 1.00 14.01 ? 417 ILE A HG13 1 ATOM 6384 H HG21 . ILE A 1 409 ? 19.573 18.836 15.792 1.00 15.93 ? 417 ILE A HG21 1 ATOM 6385 H HG22 . ILE A 1 409 ? 20.372 19.005 17.155 1.00 15.93 ? 417 ILE A HG22 1 ATOM 6386 H HG23 . ILE A 1 409 ? 18.891 18.431 17.169 1.00 15.93 ? 417 ILE A HG23 1 ATOM 6387 H HD11 . ILE A 1 409 ? 16.854 20.630 14.263 1.00 16.76 ? 417 ILE A HD11 1 ATOM 6388 H HD12 . ILE A 1 409 ? 18.285 21.313 14.376 1.00 16.76 ? 417 ILE A HD12 1 ATOM 6389 H HD13 . ILE A 1 409 ? 18.158 19.729 14.379 1.00 16.76 ? 417 ILE A HD13 1 ATOM 6390 N N . GLN A 1 410 ? 21.092 21.418 19.016 1.00 13.14 ? 418 GLN A N 1 ATOM 6391 C CA A GLN A 1 410 ? 22.434 21.113 19.494 0.55 14.02 ? 418 GLN A CA 1 ATOM 6392 C CA B GLN A 1 410 ? 22.435 21.121 19.500 0.45 13.42 ? 418 GLN A CA 1 ATOM 6393 C C . GLN A 1 410 ? 22.622 21.389 20.979 1.00 14.54 ? 418 GLN A C 1 ATOM 6394 O O . GLN A 1 410 ? 23.469 20.743 21.609 1.00 15.85 ? 418 GLN A O 1 ATOM 6395 C CB A GLN A 1 410 ? 23.443 21.922 18.680 0.55 16.86 ? 418 GLN A CB 1 ATOM 6396 C CB B GLN A 1 410 ? 23.443 21.997 18.760 0.45 14.48 ? 418 GLN A CB 1 ATOM 6397 C CG A GLN A 1 410 ? 24.880 21.533 18.899 0.55 19.92 ? 418 GLN A CG 1 ATOM 6398 C CG B GLN A 1 410 ? 23.842 21.483 17.424 0.45 14.75 ? 418 GLN A CG 1 ATOM 6399 C CD A GLN A 1 410 ? 25.253 20.253 18.207 0.55 23.77 ? 418 GLN A CD 1 ATOM 6400 C CD B GLN A 1 410 ? 24.674 20.243 17.536 0.45 16.98 ? 418 GLN A CD 1 ATOM 6401 O OE1 A GLN A 1 410 ? 24.414 19.383 17.997 0.55 25.10 ? 418 GLN A OE1 1 ATOM 6402 O OE1 B GLN A 1 410 ? 24.173 19.176 17.905 0.45 18.96 ? 418 GLN A OE1 1 ATOM 6403 N NE2 A GLN A 1 410 ? 26.520 20.136 17.828 0.55 24.71 ? 418 GLN A NE2 1 ATOM 6404 N NE2 B GLN A 1 410 ? 25.967 20.377 17.263 0.45 18.35 ? 418 GLN A NE2 1 ATOM 6405 H H . GLN A 1 410 ? 21.011 22.202 18.670 1.00 15.77 ? 418 GLN A H 1 ATOM 6406 H HA . GLN A 1 410 ? 22.630 20.181 19.334 1.00 16.10 ? 418 GLN A HA 1 ATOM 6407 H HB2 A GLN A 1 410 ? 23.247 21.803 17.737 0.55 20.23 ? 418 GLN A HB2 1 ATOM 6408 H HB2 B GLN A 1 410 ? 23.054 22.877 18.633 0.45 17.38 ? 418 GLN A HB2 1 ATOM 6409 H HB3 A GLN A 1 410 ? 23.352 22.858 18.916 0.55 20.23 ? 418 GLN A HB3 1 ATOM 6410 H HB3 B GLN A 1 410 ? 24.246 22.069 19.300 0.45 17.38 ? 418 GLN A HB3 1 ATOM 6411 H HG2 A GLN A 1 410 ? 25.453 22.237 18.557 0.55 23.90 ? 418 GLN A HG2 1 ATOM 6412 H HG2 B GLN A 1 410 ? 23.046 21.270 16.912 0.45 17.70 ? 418 GLN A HG2 1 ATOM 6413 H HG3 A GLN A 1 410 ? 25.033 21.414 19.850 0.55 23.90 ? 418 GLN A HG3 1 ATOM 6414 H HG3 B GLN A 1 410 ? 24.365 22.159 16.964 0.45 17.70 ? 418 GLN A HG3 1 ATOM 6415 H HE21 A GLN A 1 410 ? 27.075 20.774 17.982 0.55 29.65 ? 418 GLN A HE21 1 ATOM 6416 H HE21 B GLN A 1 410 ? 26.281 21.144 17.037 0.45 22.02 ? 418 GLN A HE21 1 ATOM 6417 H HE22 A GLN A 1 410 ? 26.784 19.423 17.427 0.55 29.65 ? 418 GLN A HE22 1 ATOM 6418 H HE22 B GLN A 1 410 ? 26.489 19.695 17.313 0.45 22.02 ? 418 GLN A HE22 1 ATOM 6419 N N . HIS A 1 411 ? 21.887 22.347 21.544 1.00 13.79 ? 419 HIS A N 1 ATOM 6420 C CA . HIS A 1 411 ? 22.181 22.883 22.873 1.00 13.82 ? 419 HIS A CA 1 ATOM 6421 C C . HIS A 1 411 ? 20.973 22.877 23.789 1.00 13.51 ? 419 HIS A C 1 ATOM 6422 O O . HIS A 1 411 ? 20.140 23.788 23.728 1.00 14.26 ? 419 HIS A O 1 ATOM 6423 C CB . HIS A 1 411 ? 22.715 24.292 22.734 1.00 15.41 ? 419 HIS A CB 1 ATOM 6424 C CG . HIS A 1 411 ? 23.955 24.355 21.935 1.00 17.32 ? 419 HIS A CG 1 ATOM 6425 N ND1 . HIS A 1 411 ? 25.133 23.768 22.347 1.00 21.38 ? 419 HIS A ND1 1 ATOM 6426 C CD2 . HIS A 1 411 ? 24.198 24.898 20.722 1.00 17.64 ? 419 HIS A CD2 1 ATOM 6427 C CE1 . HIS A 1 411 ? 26.058 23.977 21.427 1.00 22.03 ? 419 HIS A CE1 1 ATOM 6428 N NE2 . HIS A 1 411 ? 25.519 24.665 20.438 1.00 19.85 ? 419 HIS A NE2 1 ATOM 6429 H H . HIS A 1 411 ? 21.202 22.709 21.170 1.00 16.54 ? 419 HIS A H 1 ATOM 6430 H HA . HIS A 1 411 ? 22.871 22.340 23.285 1.00 16.59 ? 419 HIS A HA 1 ATOM 6431 H HB2 . HIS A 1 411 ? 22.047 24.842 22.295 1.00 18.50 ? 419 HIS A HB2 1 ATOM 6432 H HB3 . HIS A 1 411 ? 22.908 24.645 23.617 1.00 18.50 ? 419 HIS A HB3 1 ATOM 6433 H HD2 . HIS A 1 411 ? 23.593 25.365 20.194 1.00 21.16 ? 419 HIS A HD2 1 ATOM 6434 H HE1 . HIS A 1 411 ? 26.942 23.690 21.470 1.00 26.43 ? 419 HIS A HE1 1 ATOM 6435 H HE2 . HIS A 1 411 ? 25.927 24.913 19.722 1.00 23.82 ? 419 HIS A HE2 1 ATOM 6436 N N . VAL A 1 412 ? 20.902 21.861 24.636 1.00 13.10 ? 420 VAL A N 1 ATOM 6437 C CA . VAL A 1 412 ? 19.882 21.823 25.668 1.00 13.27 ? 420 VAL A CA 1 ATOM 6438 C C . VAL A 1 412 ? 20.234 22.737 26.833 1.00 13.75 ? 420 VAL A C 1 ATOM 6439 O O . VAL A 1 412 ? 19.336 23.258 27.501 1.00 14.47 ? 420 VAL A O 1 ATOM 6440 C CB . VAL A 1 412 ? 19.661 20.365 26.100 1.00 13.79 ? 420 VAL A CB 1 ATOM 6441 C CG1 . VAL A 1 412 ? 18.749 20.266 27.301 1.00 15.94 ? 420 VAL A CG1 1 ATOM 6442 C CG2 . VAL A 1 412 ? 19.113 19.525 24.937 1.00 15.98 ? 420 VAL A CG2 1 ATOM 6443 H H . VAL A 1 412 ? 21.432 21.183 24.634 1.00 15.72 ? 420 VAL A H 1 ATOM 6444 H HA . VAL A 1 412 ? 19.049 22.144 25.288 1.00 15.92 ? 420 VAL A HA 1 ATOM 6445 H HB . VAL A 1 412 ? 20.518 19.987 26.354 1.00 16.54 ? 420 VAL A HB 1 ATOM 6446 H HG11 . VAL A 1 412 ? 18.639 19.331 27.537 1.00 19.12 ? 420 VAL A HG11 1 ATOM 6447 H HG12 . VAL A 1 412 ? 19.147 20.750 28.041 1.00 19.12 ? 420 VAL A HG12 1 ATOM 6448 H HG13 . VAL A 1 412 ? 17.889 20.654 27.076 1.00 19.12 ? 420 VAL A HG13 1 ATOM 6449 H HG21 . VAL A 1 412 ? 18.985 18.613 25.240 1.00 19.18 ? 420 VAL A HG21 1 ATOM 6450 H HG22 . VAL A 1 412 ? 18.267 19.901 24.648 1.00 19.18 ? 420 VAL A HG22 1 ATOM 6451 H HG23 . VAL A 1 412 ? 19.751 19.545 24.206 1.00 19.18 ? 420 VAL A HG23 1 ATOM 6452 N N . ALA A 1 413 ? 21.525 22.942 27.092 1.00 14.00 ? 421 ALA A N 1 ATOM 6453 C CA . ALA A 1 413 ? 21.962 23.781 28.206 1.00 14.71 ? 421 ALA A CA 1 ATOM 6454 C C . ALA A 1 413 ? 21.694 25.259 27.922 1.00 14.69 ? 421 ALA A C 1 ATOM 6455 O O . ALA A 1 413 ? 21.890 25.742 26.806 1.00 15.98 ? 421 ALA A O 1 ATOM 6456 C CB . ALA A 1 413 ? 23.455 23.562 28.458 1.00 15.82 ? 421 ALA A CB 1 ATOM 6457 H H . ALA A 1 413 ? 22.170 22.605 26.634 1.00 16.81 ? 421 ALA A H 1 ATOM 6458 H HA . ALA A 1 413 ? 21.476 23.531 29.007 1.00 17.66 ? 421 ALA A HA 1 ATOM 6459 H HB1 . ALA A 1 413 ? 23.735 24.123 29.198 1.00 18.98 ? 421 ALA A HB1 1 ATOM 6460 H HB2 . ALA A 1 413 ? 23.605 22.629 28.674 1.00 18.98 ? 421 ALA A HB2 1 ATOM 6461 H HB3 . ALA A 1 413 ? 23.948 23.800 27.657 1.00 18.98 ? 421 ALA A HB3 1 ATOM 6462 N N . PHE A 1 414 ? 21.282 25.997 28.956 1.00 15.34 ? 422 PHE A N 1 ATOM 6463 C CA . PHE A 1 414 ? 20.893 27.392 28.759 1.00 16.08 ? 422 PHE A CA 1 ATOM 6464 C C . PHE A 1 414 ? 22.048 28.247 28.240 1.00 17.99 ? 422 PHE A C 1 ATOM 6465 O O . PHE A 1 414 ? 21.862 29.085 27.352 1.00 17.64 ? 422 PHE A O 1 ATOM 6466 C CB . PHE A 1 414 ? 20.386 28.022 30.062 1.00 16.17 ? 422 PHE A CB 1 ATOM 6467 C CG . PHE A 1 414 ? 18.944 27.704 30.413 1.00 16.04 ? 422 PHE A CG 1 ATOM 6468 C CD1 . PHE A 1 414 ? 18.314 26.526 30.024 1.00 16.53 ? 422 PHE A CD1 1 ATOM 6469 C CD2 . PHE A 1 414 ? 18.237 28.594 31.185 1.00 18.90 ? 422 PHE A CD2 1 ATOM 6470 C CE1 . PHE A 1 414 ? 17.018 26.278 30.395 1.00 16.26 ? 422 PHE A CE1 1 ATOM 6471 C CE2 . PHE A 1 414 ? 16.942 28.342 31.538 1.00 19.88 ? 422 PHE A CE2 1 ATOM 6472 C CZ . PHE A 1 414 ? 16.333 27.193 31.144 1.00 18.47 ? 422 PHE A CZ 1 ATOM 6473 H H . PHE A 1 414 ? 21.219 25.717 29.767 1.00 18.41 ? 422 PHE A H 1 ATOM 6474 H HA . PHE A 1 414 ? 20.175 27.431 28.108 1.00 19.30 ? 422 PHE A HA 1 ATOM 6475 H HB2 . PHE A 1 414 ? 20.941 27.707 30.792 1.00 19.40 ? 422 PHE A HB2 1 ATOM 6476 H HB3 . PHE A 1 414 ? 20.463 28.986 29.988 1.00 19.40 ? 422 PHE A HB3 1 ATOM 6477 H HD1 . PHE A 1 414 ? 18.775 25.902 29.512 1.00 19.84 ? 422 PHE A HD1 1 ATOM 6478 H HD2 . PHE A 1 414 ? 18.641 29.386 31.458 1.00 22.68 ? 422 PHE A HD2 1 ATOM 6479 H HE1 . PHE A 1 414 ? 16.598 25.494 30.122 1.00 19.52 ? 422 PHE A HE1 1 ATOM 6480 H HE2 . PHE A 1 414 ? 16.475 28.960 32.053 1.00 23.85 ? 422 PHE A HE2 1 ATOM 6481 H HZ . PHE A 1 414 ? 15.453 27.026 31.391 1.00 22.17 ? 422 PHE A HZ 1 ATOM 6482 N N . ASN A 1 415 ? 23.233 28.124 28.832 1.00 19.28 ? 423 ASN A N 1 ATOM 6483 C CA . ASN A 1 415 ? 24.294 29.066 28.493 1.00 21.88 ? 423 ASN A CA 1 ATOM 6484 C C . ASN A 1 415 ? 24.875 28.792 27.113 1.00 19.53 ? 423 ASN A C 1 ATOM 6485 O O . ASN A 1 415 ? 25.223 29.731 26.392 1.00 20.20 ? 423 ASN A O 1 ATOM 6486 C CB . ASN A 1 415 ? 25.369 29.056 29.580 1.00 27.06 ? 423 ASN A CB 1 ATOM 6487 C CG . ASN A 1 415 ? 24.872 29.646 30.890 1.00 33.39 ? 423 ASN A CG 1 ATOM 6488 O OD1 . ASN A 1 415 ? 23.894 30.401 30.917 1.00 35.30 ? 423 ASN A OD1 1 ATOM 6489 N ND2 . ASN A 1 415 ? 25.555 29.321 31.983 1.00 36.81 ? 423 ASN A ND2 1 ATOM 6490 H H . ASN A 1 415 ? 23.443 27.526 29.413 1.00 23.14 ? 423 ASN A H 1 ATOM 6491 H HA . ASN A 1 415 ? 23.914 29.958 28.473 1.00 26.25 ? 423 ASN A HA 1 ATOM 6492 H HB2 . ASN A 1 415 ? 25.644 28.141 29.746 1.00 32.47 ? 423 ASN A HB2 1 ATOM 6493 H HB3 . ASN A 1 415 ? 26.128 29.582 29.281 1.00 32.47 ? 423 ASN A HB3 1 ATOM 6494 H HD21 . ASN A 1 415 ? 25.313 29.630 32.749 1.00 44.17 ? 423 ASN A HD21 1 ATOM 6495 H HD22 . ASN A 1 415 ? 26.239 28.803 31.925 1.00 44.17 ? 423 ASN A HD22 1 ATOM 6496 N N . THR A 1 416 ? 25.006 27.522 26.724 1.00 18.25 ? 424 THR A N 1 ATOM 6497 C CA . THR A 1 416 ? 25.544 27.257 25.393 1.00 19.05 ? 424 THR A CA 1 ATOM 6498 C C . THR A 1 416 ? 24.515 27.526 24.309 1.00 16.77 ? 424 THR A C 1 ATOM 6499 O O . THR A 1 416 ? 24.891 27.936 23.204 1.00 17.52 ? 424 THR A O 1 ATOM 6500 C CB . THR A 1 416 ? 26.104 25.845 25.282 1.00 23.14 ? 424 THR A CB 1 ATOM 6501 O OG1 . THR A 1 416 ? 25.070 24.899 25.505 1.00 25.52 ? 424 THR A OG1 1 ATOM 6502 C CG2 . THR A 1 416 ? 27.178 25.632 26.298 1.00 27.00 ? 424 THR A CG2 1 ATOM 6503 H H . THR A 1 416 ? 24.802 26.828 27.189 1.00 21.90 ? 424 THR A H 1 ATOM 6504 H HA . THR A 1 416 ? 26.282 27.868 25.241 1.00 22.87 ? 424 THR A HA 1 ATOM 6505 H HB . THR A 1 416 ? 26.482 25.713 24.398 1.00 27.77 ? 424 THR A HB 1 ATOM 6506 H HG1 . THR A 1 416 ? 25.376 24.119 25.444 1.00 30.63 ? 424 THR A HG1 1 ATOM 6507 H HG21 . THR A 1 416 ? 27.532 24.732 26.223 1.00 32.40 ? 424 THR A HG21 1 ATOM 6508 H HG22 . THR A 1 416 ? 27.898 26.266 26.157 1.00 32.40 ? 424 THR A HG22 1 ATOM 6509 H HG23 . THR A 1 416 ? 26.819 25.756 27.190 1.00 32.40 ? 424 THR A HG23 1 ATOM 6510 N N . TYR A 1 417 ? 23.232 27.314 24.595 1.00 15.18 ? 425 TYR A N 1 ATOM 6511 C CA . TYR A 1 417 ? 22.210 27.746 23.648 1.00 14.93 ? 425 TYR A CA 1 ATOM 6512 C C . TYR A 1 417 ? 22.300 29.253 23.420 1.00 16.17 ? 425 TYR A C 1 ATOM 6513 O O . TYR A 1 417 ? 22.295 29.724 22.277 1.00 16.07 ? 425 TYR A O 1 ATOM 6514 C CB . TYR A 1 417 ? 20.848 27.373 24.175 1.00 14.89 ? 425 TYR A CB 1 ATOM 6515 C CG . TYR A 1 417 ? 19.710 27.943 23.356 1.00 14.18 ? 425 TYR A CG 1 ATOM 6516 C CD1 . TYR A 1 417 ? 19.162 29.162 23.689 1.00 14.70 ? 425 TYR A CD1 1 ATOM 6517 C CD2 . TYR A 1 417 ? 19.183 27.262 22.261 1.00 13.92 ? 425 TYR A CD2 1 ATOM 6518 C CE1 . TYR A 1 417 ? 18.120 29.696 22.963 1.00 15.98 ? 425 TYR A CE1 1 ATOM 6519 C CE2 . TYR A 1 417 ? 18.123 27.798 21.512 1.00 14.26 ? 425 TYR A CE2 1 ATOM 6520 C CZ . TYR A 1 417 ? 17.606 29.022 21.879 1.00 14.67 ? 425 TYR A CZ 1 ATOM 6521 O OH . TYR A 1 417 ? 16.548 29.596 21.207 1.00 15.66 ? 425 TYR A OH 1 ATOM 6522 H H . TYR A 1 417 ? 22.935 26.934 25.307 1.00 18.21 ? 425 TYR A H 1 ATOM 6523 H HA . TYR A 1 417 ? 22.345 27.297 22.799 1.00 17.91 ? 425 TYR A HA 1 ATOM 6524 H HB2 . TYR A 1 417 ? 20.763 26.407 24.171 1.00 17.87 ? 425 TYR A HB2 1 ATOM 6525 H HB3 . TYR A 1 417 ? 20.759 27.708 25.081 1.00 17.87 ? 425 TYR A HB3 1 ATOM 6526 H HD1 . TYR A 1 417 ? 19.499 29.630 24.419 1.00 17.64 ? 425 TYR A HD1 1 ATOM 6527 H HD2 . TYR A 1 417 ? 19.540 26.437 22.021 1.00 16.71 ? 425 TYR A HD2 1 ATOM 6528 H HE1 . TYR A 1 417 ? 17.761 30.519 23.207 1.00 19.18 ? 425 TYR A HE1 1 ATOM 6529 H HE2 . TYR A 1 417 ? 17.774 27.334 20.785 1.00 17.11 ? 425 TYR A HE2 1 ATOM 6530 H HH . TYR A 1 417 ? 16.313 29.105 20.567 1.00 18.79 ? 425 TYR A HH 1 ATOM 6531 N N . ALA A 1 418 ? 22.434 30.028 24.506 1.00 17.61 ? 426 ALA A N 1 ATOM 6532 C CA . ALA A 1 418 ? 22.509 31.484 24.377 1.00 18.97 ? 426 ALA A CA 1 ATOM 6533 C C . ALA A 1 418 ? 23.689 31.906 23.504 1.00 20.22 ? 426 ALA A C 1 ATOM 6534 O O . ALA A 1 418 ? 23.555 32.776 22.629 1.00 20.09 ? 426 ALA A O 1 ATOM 6535 C CB . ALA A 1 418 ? 22.608 32.117 25.765 1.00 21.40 ? 426 ALA A CB 1 ATOM 6536 H H . ALA A 1 418 ? 22.483 29.738 25.315 1.00 21.13 ? 426 ALA A H 1 ATOM 6537 H HA . ALA A 1 418 ? 21.696 31.806 23.958 1.00 22.76 ? 426 ALA A HA 1 ATOM 6538 H HB1 . ALA A 1 418 ? 22.658 33.081 25.669 1.00 25.68 ? 426 ALA A HB1 1 ATOM 6539 H HB2 . ALA A 1 418 ? 21.822 31.875 26.279 1.00 25.68 ? 426 ALA A HB2 1 ATOM 6540 H HB3 . ALA A 1 418 ? 23.407 31.787 26.206 1.00 25.68 ? 426 ALA A HB3 1 ATOM 6541 N N . THR A 1 419 ? 24.855 31.296 23.725 1.00 19.97 ? 427 THR A N 1 ATOM 6542 C CA . THR A 1 419 ? 26.033 31.644 22.936 1.00 21.01 ? 427 THR A CA 1 ATOM 6543 C C . THR A 1 419 ? 25.850 31.271 21.478 1.00 19.54 ? 427 THR A C 1 ATOM 6544 O O . THR A 1 419 ? 26.252 32.020 20.581 1.00 19.02 ? 427 THR A O 1 ATOM 6545 C CB . THR A 1 419 ? 27.253 30.935 23.520 1.00 24.00 ? 427 THR A CB 1 ATOM 6546 O OG1 . THR A 1 419 ? 27.486 31.445 24.833 1.00 28.07 ? 427 THR A OG1 1 ATOM 6547 C CG2 . THR A 1 419 ? 28.489 31.170 22.663 1.00 26.67 ? 427 THR A CG2 1 ATOM 6548 H H . THR A 1 419 ? 24.988 30.686 24.316 1.00 23.97 ? 427 THR A H 1 ATOM 6549 H HA . THR A 1 419 ? 26.183 32.601 22.988 1.00 25.21 ? 427 THR A HA 1 ATOM 6550 H HB . THR A 1 419 ? 27.085 29.981 23.566 1.00 28.80 ? 427 THR A HB 1 ATOM 6551 H HG1 . THR A 1 419 ? 26.816 31.304 25.319 1.00 33.68 ? 427 THR A HG1 1 ATOM 6552 H HG21 . THR A 1 419 ? 29.252 30.713 23.049 1.00 32.01 ? 427 THR A HG21 1 ATOM 6553 H HG22 . THR A 1 419 ? 28.339 30.832 21.766 1.00 32.01 ? 427 THR A HG22 1 ATOM 6554 H HG23 . THR A 1 419 ? 28.682 32.120 22.614 1.00 32.01 ? 427 THR A HG23 1 ATOM 6555 N N . CYS A 1 420 ? 25.255 30.109 21.227 1.00 17.98 ? 428 CYS A N 1 ATOM 6556 C CA . CYS A 1 420 ? 25.021 29.677 19.859 1.00 16.93 ? 428 CYS A CA 1 ATOM 6557 C C . CYS A 1 420 ? 24.163 30.689 19.115 1.00 17.44 ? 428 CYS A C 1 ATOM 6558 O O . CYS A 1 420 ? 24.416 30.983 17.939 1.00 18.16 ? 428 CYS A O 1 ATOM 6559 C CB . CYS A 1 420 ? 24.353 28.310 19.895 1.00 16.60 ? 428 CYS A CB 1 ATOM 6560 S SG . CYS A 1 420 ? 24.000 27.568 18.298 1.00 17.21 ? 428 CYS A SG 1 ATOM 6561 H H . CYS A 1 420 ? 24.980 29.558 21.827 1.00 21.58 ? 428 CYS A H 1 ATOM 6562 H HA . CYS A 1 420 ? 25.869 29.594 19.396 1.00 20.31 ? 428 CYS A HA 1 ATOM 6563 H HB2 . CYS A 1 420 ? 24.934 27.699 20.376 1.00 19.92 ? 428 CYS A HB2 1 ATOM 6564 H HB3 . CYS A 1 420 ? 23.511 28.394 20.368 1.00 19.92 ? 428 CYS A HB3 1 ATOM 6565 N N . LEU A 1 421 ? 23.159 31.263 19.791 1.00 20.10 ? 429 LEU A N 1 ATOM 6566 C CA . LEU A 1 421 ? 22.265 32.217 19.135 1.00 24.63 ? 429 LEU A CA 1 ATOM 6567 C C . LEU A 1 421 ? 22.975 33.486 18.694 1.00 29.07 ? 429 LEU A C 1 ATOM 6568 O O . LEU A 1 421 ? 22.475 34.161 17.799 1.00 30.77 ? 429 LEU A O 1 ATOM 6569 C CB . LEU A 1 421 ? 21.083 32.607 20.026 1.00 26.14 ? 429 LEU A CB 1 ATOM 6570 C CG . LEU A 1 421 ? 19.871 31.684 20.008 1.00 27.38 ? 429 LEU A CG 1 ATOM 6571 C CD1 . LEU A 1 421 ? 18.720 32.341 20.745 1.00 27.39 ? 429 LEU A CD1 1 ATOM 6572 C CD2 . LEU A 1 421 ? 19.420 31.321 18.612 1.00 29.21 ? 429 LEU A CD2 1 ATOM 6573 H H . LEU A 1 421 ? 22.978 31.116 20.619 1.00 24.12 ? 429 LEU A H 1 ATOM 6574 H HA . LEU A 1 421 ? 21.902 31.797 18.340 1.00 29.56 ? 429 LEU A HA 1 ATOM 6575 H HB2 . LEU A 1 421 ? 21.397 32.649 20.943 1.00 31.37 ? 429 LEU A HB2 1 ATOM 6576 H HB3 . LEU A 1 421 ? 20.776 33.486 19.754 1.00 31.37 ? 429 LEU A HB3 1 ATOM 6577 H HG . LEU A 1 421 ? 20.095 30.863 20.473 1.00 32.85 ? 429 LEU A HG 1 ATOM 6578 H HD11 . LEU A 1 421 ? 17.954 31.746 20.728 1.00 32.86 ? 429 LEU A HD11 1 ATOM 6579 H HD12 . LEU A 1 421 ? 18.988 32.509 21.662 1.00 32.86 ? 429 LEU A HD12 1 ATOM 6580 H HD13 . LEU A 1 421 ? 18.500 33.177 20.306 1.00 32.86 ? 429 LEU A HD13 1 ATOM 6581 H HD21 . LEU A 1 421 ? 18.649 30.735 18.672 1.00 35.05 ? 429 LEU A HD21 1 ATOM 6582 H HD22 . LEU A 1 421 ? 19.182 32.132 18.136 1.00 35.05 ? 429 LEU A HD22 1 ATOM 6583 H HD23 . LEU A 1 421 ? 20.145 30.868 18.153 1.00 35.05 ? 429 LEU A HD23 1 ATOM 6584 N N . HIS A 1 422 ? 24.126 33.821 19.289 1.00 31.29 ? 430 HIS A N 1 ATOM 6585 C CA . HIS A 1 422 ? 24.940 34.936 18.801 1.00 38.13 ? 430 HIS A CA 1 ATOM 6586 C C . HIS A 1 422 ? 25.450 34.728 17.373 1.00 40.41 ? 430 HIS A C 1 ATOM 6587 O O . HIS A 1 422 ? 25.851 35.701 16.720 1.00 41.10 ? 430 HIS A O 1 ATOM 6588 C CB . HIS A 1 422 ? 26.142 35.128 19.722 1.00 42.05 ? 430 HIS A CB 1 ATOM 6589 C CG . HIS A 1 422 ? 25.770 35.463 21.129 1.00 45.66 ? 430 HIS A CG 1 ATOM 6590 N ND1 . HIS A 1 422 ? 26.656 35.352 22.180 1.00 47.15 ? 430 HIS A ND1 1 ATOM 6591 C CD2 . HIS A 1 422 ? 24.604 35.900 21.661 1.00 47.24 ? 430 HIS A CD2 1 ATOM 6592 C CE1 . HIS A 1 422 ? 26.050 35.708 23.301 1.00 48.05 ? 430 HIS A CE1 1 ATOM 6593 N NE2 . HIS A 1 422 ? 24.806 36.048 23.013 1.00 48.14 ? 430 HIS A NE2 1 ATOM 6594 H H . HIS A 1 422 ? 24.455 33.419 19.975 1.00 37.55 ? 430 HIS A H 1 ATOM 6595 H HA . HIS A 1 422 ? 24.410 35.749 18.818 1.00 45.75 ? 430 HIS A HA 1 ATOM 6596 H HB2 . HIS A 1 422 ? 26.658 34.306 19.739 1.00 50.47 ? 430 HIS A HB2 1 ATOM 6597 H HB3 . HIS A 1 422 ? 26.688 35.852 19.379 1.00 50.47 ? 430 HIS A HB3 1 ATOM 6598 H HD2 . HIS A 1 422 ? 23.816 36.071 21.198 1.00 56.69 ? 430 HIS A HD2 1 ATOM 6599 H HE1 . HIS A 1 422 ? 26.436 35.722 24.147 1.00 57.66 ? 430 HIS A HE1 1 ATOM 6600 H HE2 . HIS A 1 422 ? 24.217 36.316 23.579 1.00 57.76 ? 430 HIS A HE2 1 ATOM 6601 N N . GLY A 1 423 ? 25.469 33.494 16.878 1.00 41.29 ? 431 GLY A N 1 ATOM 6602 C CA . GLY A 1 423 ? 25.993 33.218 15.549 1.00 42.01 ? 431 GLY A CA 1 ATOM 6603 C C . GLY A 1 423 ? 25.304 33.995 14.444 1.00 42.36 ? 431 GLY A C 1 ATOM 6604 O O . GLY A 1 423 ? 24.184 34.473 14.623 1.00 42.94 ? 431 GLY A O 1 ATOM 6605 H H . GLY A 1 423 ? 25.181 32.799 17.294 1.00 49.54 ? 431 GLY A H 1 ATOM 6606 H HA2 . GLY A 1 423 ? 26.938 33.436 15.528 1.00 50.41 ? 431 GLY A HA2 1 ATOM 6607 H HA3 . GLY A 1 423 ? 25.896 32.271 15.359 1.00 50.41 ? 431 GLY A HA3 1 HETATM 6608 ZN ZN . ZN B 2 . ? 2.180 20.442 26.312 1.00 12.31 ? 501 ZN A ZN 1 HETATM 6609 ZN ZN . ZN C 2 . ? 0.402 20.076 23.439 1.00 11.78 ? 502 ZN A ZN 1 HETATM 6610 C C1 . NAG D 3 . ? -13.717 6.202 13.714 1.00 21.59 ? 503 NAG A C1 1 HETATM 6611 C C2 . NAG D 3 . ? -15.193 6.384 13.357 1.00 25.39 ? 503 NAG A C2 1 HETATM 6612 C C3 . NAG D 3 . ? -15.739 5.119 12.701 1.00 27.83 ? 503 NAG A C3 1 HETATM 6613 C C4 . NAG D 3 . ? -14.839 4.649 11.568 1.00 27.47 ? 503 NAG A C4 1 HETATM 6614 C C5 . NAG D 3 . ? -13.384 4.584 12.003 1.00 24.59 ? 503 NAG A C5 1 HETATM 6615 C C6 . NAG D 3 . ? -12.432 4.264 10.876 1.00 25.84 ? 503 NAG A C6 1 HETATM 6616 C C7 . NAG D 3 . ? -16.358 7.965 14.830 1.00 28.83 ? 503 NAG A C7 1 HETATM 6617 C C8 . NAG D 3 . ? -17.118 8.136 16.113 1.00 31.36 ? 503 NAG A C8 1 HETATM 6618 N N2 . NAG D 3 . ? -15.971 6.720 14.540 1.00 27.12 ? 503 NAG A N2 1 HETATM 6619 O O3 . NAG D 3 . ? -17.049 5.355 12.192 1.00 31.65 ? 503 NAG A O3 1 HETATM 6620 O O4 . NAG D 3 . ? -15.228 3.324 11.227 1.00 32.44 ? 503 NAG A O4 1 HETATM 6621 O O5 . NAG D 3 . ? -12.982 5.847 12.546 1.00 21.48 ? 503 NAG A O5 1 HETATM 6622 O O6 . NAG D 3 . ? -12.569 5.179 9.799 1.00 27.52 ? 503 NAG A O6 1 HETATM 6623 O O7 . NAG D 3 . ? -16.079 8.920 14.106 1.00 30.23 ? 503 NAG A O7 1 HETATM 6624 H H1 . NAG D 3 . ? -13.631 5.490 14.377 1.00 25.91 ? 503 NAG A H1 1 HETATM 6625 H H2 . NAG D 3 . ? -15.267 7.116 12.715 1.00 30.47 ? 503 NAG A H2 1 HETATM 6626 H H3 . NAG D 3 . ? -15.788 4.415 13.375 1.00 33.40 ? 503 NAG A H3 1 HETATM 6627 H H4 . NAG D 3 . ? -14.935 5.237 10.795 1.00 32.96 ? 503 NAG A H4 1 HETATM 6628 H H5 . NAG D 3 . ? -13.293 3.901 12.695 1.00 29.51 ? 503 NAG A H5 1 HETATM 6629 H H61 . NAG D 3 . ? -12.614 3.362 10.551 1.00 31.01 ? 503 NAG A H61 1 HETATM 6630 H H62 . NAG D 3 . ? -11.516 4.303 11.211 1.00 31.01 ? 503 NAG A H62 1 HETATM 6631 H H81 . NAG D 3 . ? -16.564 7.844 16.861 1.00 37.64 ? 503 NAG A H81 1 HETATM 6632 H H82 . NAG D 3 . ? -17.933 7.599 16.083 1.00 37.64 ? 503 NAG A H82 1 HETATM 6633 H H83 . NAG D 3 . ? -17.352 9.076 16.230 1.00 37.64 ? 503 NAG A H83 1 HETATM 6634 H HN2 . NAG D 3 . ? -16.188 6.051 15.122 1.00 32.54 ? 503 NAG A HN2 1 HETATM 6635 H HO3 . NAG D 3 . ? -17.321 4.645 11.733 1.00 37.99 ? 503 NAG A HO3 1 HETATM 6636 H HO6 . NAG D 3 . ? -12.432 6.005 10.094 1.00 33.03 ? 503 NAG A HO6 1 HETATM 6637 C C1 . NAG E 3 . ? -15.607 3.217 9.867 1.00 36.82 ? 504 NAG A C1 1 HETATM 6638 C C2 . NAG E 3 . ? -15.526 1.739 9.506 1.00 38.06 ? 504 NAG A C2 1 HETATM 6639 C C3 . NAG E 3 . ? -16.050 1.508 8.092 1.00 41.53 ? 504 NAG A C3 1 HETATM 6640 C C4 . NAG E 3 . ? -17.417 2.151 7.899 1.00 43.43 ? 504 NAG A C4 1 HETATM 6641 C C5 . NAG E 3 . ? -17.420 3.596 8.385 1.00 42.84 ? 504 NAG A C5 1 HETATM 6642 C C6 . NAG E 3 . ? -18.804 4.207 8.411 1.00 45.48 ? 504 NAG A C6 1 HETATM 6643 C C7 . NAG E 3 . ? -13.721 0.516 10.659 1.00 40.50 ? 504 NAG A C7 1 HETATM 6644 C C8 . NAG E 3 . ? -12.284 0.089 10.596 1.00 40.72 ? 504 NAG A C8 1 HETATM 6645 N N2 . NAG E 3 . ? -14.161 1.242 9.625 1.00 39.66 ? 504 NAG A N2 1 HETATM 6646 O O3 . NAG E 3 . ? -16.156 0.107 7.872 1.00 43.51 ? 504 NAG A O3 1 HETATM 6647 O O4 . NAG E 3 . ? -17.750 2.125 6.514 1.00 45.50 ? 504 NAG A O4 1 HETATM 6648 O O5 . NAG E 3 . ? -16.922 3.666 9.728 1.00 39.12 ? 504 NAG A O5 1 HETATM 6649 O O6 . NAG E 3 . ? -19.563 3.739 9.519 1.00 46.80 ? 504 NAG A O6 1 HETATM 6650 O O7 . NAG E 3 . ? -14.446 0.223 11.609 1.00 41.61 ? 504 NAG A O7 1 HETATM 6651 H H1 . NAG E 3 . ? -15.006 3.739 9.301 1.00 44.19 ? 504 NAG A H1 1 HETATM 6652 H H2 . NAG E 3 . ? -16.093 1.241 10.124 1.00 45.68 ? 504 NAG A H2 1 HETATM 6653 H H3 . NAG E 3 . ? -15.422 1.888 7.449 1.00 49.83 ? 504 NAG A H3 1 HETATM 6654 H H4 . NAG E 3 . ? -18.084 1.642 8.398 1.00 52.11 ? 504 NAG A H4 1 HETATM 6655 H H5 . NAG E 3 . ? -16.847 4.129 7.803 1.00 51.41 ? 504 NAG A H5 1 HETATM 6656 H H61 . NAG E 3 . ? -19.270 3.976 7.585 1.00 54.58 ? 504 NAG A H61 1 HETATM 6657 H H62 . NAG E 3 . ? -18.721 5.178 8.469 1.00 54.58 ? 504 NAG A H62 1 HETATM 6658 H H81 . NAG E 3 . ? -11.712 0.878 10.555 1.00 48.87 ? 504 NAG A H81 1 HETATM 6659 H H82 . NAG E 3 . ? -12.142 -0.458 9.800 1.00 48.87 ? 504 NAG A H82 1 HETATM 6660 H H83 . NAG E 3 . ? -12.064 -0.432 11.392 1.00 48.87 ? 504 NAG A H83 1 HETATM 6661 H HN2 . NAG E 3 . ? -13.577 1.426 8.949 1.00 47.59 ? 504 NAG A HN2 1 HETATM 6662 H HO3 . NAG E 3 . ? -16.633 -0.042 7.137 1.00 52.21 ? 504 NAG A HO3 1 HETATM 6663 H HO4 . NAG E 3 . ? -18.519 2.551 6.387 1.00 54.60 ? 504 NAG A HO4 1 HETATM 6664 H HO6 . NAG E 3 . ? -20.019 4.414 9.871 1.00 56.17 ? 504 NAG A HO6 1 HETATM 6665 C C1 . BMA F 4 . ? 8.447 -3.932 48.479 1.00 37.02 ? 505 BMA A C1 1 HETATM 6666 C C2 . BMA F 4 . ? 7.054 -4.346 48.003 1.00 38.37 ? 505 BMA A C2 1 HETATM 6667 C C3 . BMA F 4 . ? 6.025 -3.878 49.048 1.00 39.15 ? 505 BMA A C3 1 HETATM 6668 C C4 . BMA F 4 . ? 6.399 -4.360 50.466 1.00 40.79 ? 505 BMA A C4 1 HETATM 6669 C C5 . BMA F 4 . ? 7.860 -3.957 50.802 1.00 39.94 ? 505 BMA A C5 1 HETATM 6670 C C6 . BMA F 4 . ? 8.369 -4.560 52.100 1.00 39.54 ? 505 BMA A C6 1 HETATM 6671 O O2 . BMA F 4 . ? 6.970 -5.768 47.877 1.00 37.83 ? 505 BMA A O2 1 HETATM 6672 O O3 . BMA F 4 . ? 4.664 -4.241 48.677 1.00 37.33 ? 505 BMA A O3 1 HETATM 6673 O O4 . BMA F 4 . ? 5.527 -3.772 51.424 1.00 42.37 ? 505 BMA A O4 1 HETATM 6674 O O5 . BMA F 4 . ? 8.721 -4.439 49.762 1.00 38.24 ? 505 BMA A O5 1 HETATM 6675 O O6 . BMA F 4 . ? 8.223 -5.981 51.966 1.00 38.11 ? 505 BMA A O6 1 HETATM 6676 H H1 . BMA F 4 . ? 8.525 -2.828 48.492 1.00 44.43 ? 505 BMA A H1 1 HETATM 6677 H H2 . BMA F 4 . ? 6.855 -3.861 47.035 1.00 46.05 ? 505 BMA A H2 1 HETATM 6678 H H3 . BMA F 4 . ? 6.030 -2.780 49.073 1.00 46.98 ? 505 BMA A H3 1 HETATM 6679 H H4 . BMA F 4 . ? 6.335 -5.460 50.486 1.00 48.94 ? 505 BMA A H4 1 HETATM 6680 H H5 . BMA F 4 . ? 7.934 -2.859 50.877 1.00 47.93 ? 505 BMA A H5 1 HETATM 6681 H H61 . BMA F 4 . ? 7.776 -4.158 52.936 1.00 47.45 ? 505 BMA A H61 1 HETATM 6682 H H62 . BMA F 4 . ? 9.416 -4.255 52.229 1.00 47.45 ? 505 BMA A H62 1 HETATM 6683 H HO2 . BMA F 4 . ? 7.802 -6.051 47.466 1.00 45.40 ? 505 BMA A HO2 1 HETATM 6684 H HO4 . BMA F 4 . ? 5.444 -4.430 52.132 1.00 50.85 ? 505 BMA A HO4 1 HETATM 6685 C C1 . MAN G 5 . ? 4.308 -3.361 47.555 1.00 36.12 ? 506 MAN A C1 1 HETATM 6686 C C2 . MAN G 5 . ? 3.174 -2.487 48.027 1.00 36.29 ? 506 MAN A C2 1 HETATM 6687 C C3 . MAN G 5 . ? 2.073 -3.394 48.551 1.00 34.87 ? 506 MAN A C3 1 HETATM 6688 C C4 . MAN G 5 . ? 1.606 -4.395 47.484 1.00 34.40 ? 506 MAN A C4 1 HETATM 6689 C C5 . MAN G 5 . ? 2.739 -4.987 46.589 1.00 33.85 ? 506 MAN A C5 1 HETATM 6690 C C6 . MAN G 5 . ? 2.173 -5.285 45.234 1.00 32.96 ? 506 MAN A C6 1 HETATM 6691 O O2 . MAN G 5 . ? 2.588 -1.729 46.925 1.00 40.02 ? 506 MAN A O2 1 HETATM 6692 O O3 . MAN G 5 . ? 0.972 -2.614 48.981 1.00 36.81 ? 506 MAN A O3 1 HETATM 6693 O O4 . MAN G 5 . ? 0.922 -5.491 48.089 1.00 36.24 ? 506 MAN A O4 1 HETATM 6694 O O5 . MAN G 5 . ? 3.899 -4.076 46.400 1.00 35.75 ? 506 MAN A O5 1 HETATM 6695 O O6 . MAN G 5 . ? 3.094 -6.017 44.460 1.00 36.76 ? 506 MAN A O6 1 HETATM 6696 H H1 . MAN G 5 . ? 5.169 -2.755 47.234 1.00 43.34 ? 506 MAN A H1 1 HETATM 6697 H H2 . MAN G 5 . ? 3.533 -1.824 48.825 1.00 43.55 ? 506 MAN A H2 1 HETATM 6698 H H3 . MAN G 5 . ? 2.437 -3.949 49.422 1.00 41.84 ? 506 MAN A H3 1 HETATM 6699 H H4 . MAN G 5 . ? 0.918 -3.854 46.812 1.00 41.28 ? 506 MAN A H4 1 HETATM 6700 H H5 . MAN G 5 . ? 3.080 -5.932 47.032 1.00 40.62 ? 506 MAN A H5 1 HETATM 6701 H H61 . MAN G 5 . ? 1.920 -4.328 44.751 1.00 39.56 ? 506 MAN A H61 1 HETATM 6702 H H62 . MAN G 5 . ? 1.240 -5.844 45.384 1.00 39.56 ? 506 MAN A H62 1 HETATM 6703 H HO2 . MAN G 5 . ? 1.917 -1.130 47.276 1.00 48.02 ? 506 MAN A HO2 1 HETATM 6704 H HO3 . MAN G 5 . ? 1.358 -1.892 49.503 1.00 44.17 ? 506 MAN A HO3 1 HETATM 6705 H HO4 . MAN G 5 . ? 0.991 -6.218 47.451 1.00 43.48 ? 506 MAN A HO4 1 HETATM 6706 H HO6 . MAN G 5 . ? 3.704 -6.453 45.069 1.00 44.11 ? 506 MAN A HO6 1 HETATM 6707 C C1 . NAG H 3 . ? 16.235 -0.707 42.698 1.00 18.26 ? 507 NAG A C1 1 HETATM 6708 C C2 . NAG H 3 . ? 14.850 -0.160 42.985 1.00 17.62 ? 507 NAG A C2 1 HETATM 6709 C C3 . NAG H 3 . ? 14.353 -0.619 44.351 1.00 19.55 ? 507 NAG A C3 1 HETATM 6710 C C4 . NAG H 3 . ? 14.465 -2.124 44.505 1.00 20.47 ? 507 NAG A C4 1 HETATM 6711 C C5 . NAG H 3 . ? 15.888 -2.542 44.214 1.00 19.69 ? 507 NAG A C5 1 HETATM 6712 C C6 . NAG H 3 . ? 16.096 -4.037 44.274 1.00 21.85 ? 507 NAG A C6 1 HETATM 6713 C C7 . NAG H 3 . ? 13.988 1.986 42.194 1.00 18.89 ? 507 NAG A C7 1 HETATM 6714 C C8 . NAG H 3 . ? 14.064 3.466 42.335 1.00 19.36 ? 507 NAG A C8 1 HETATM 6715 N N2 . NAG H 3 . ? 14.840 1.285 42.943 1.00 17.19 ? 507 NAG A N2 1 HETATM 6716 O O3 . NAG H 3 . ? 13.004 -0.200 44.510 1.00 22.09 ? 507 NAG A O3 1 HETATM 6717 O O4 . NAG H 3 . ? 14.209 -2.468 45.863 1.00 22.70 ? 507 NAG A O4 1 HETATM 6718 O O5 . NAG H 3 . ? 16.245 -2.123 42.895 1.00 19.29 ? 507 NAG A O5 1 HETATM 6719 O O6 . NAG H 3 . ? 17.488 -4.314 44.295 1.00 25.64 ? 507 NAG A O6 1 HETATM 6720 O O7 . NAG H 3 . ? 13.231 1.447 41.401 1.00 20.81 ? 507 NAG A O7 1 HETATM 6721 H H1 . NAG H 3 . ? 16.878 -0.293 43.305 1.00 21.91 ? 507 NAG A H1 1 HETATM 6722 H H2 . NAG H 3 . ? 14.235 -0.499 42.307 1.00 21.15 ? 507 NAG A H2 1 HETATM 6723 H H3 . NAG H 3 . ? 14.897 -0.192 45.041 1.00 23.46 ? 507 NAG A H3 1 HETATM 6724 H H4 . NAG H 3 . ? 13.841 -2.581 43.909 1.00 24.56 ? 507 NAG A H4 1 HETATM 6725 H H5 . NAG H 3 . ? 16.483 -2.113 44.857 1.00 23.63 ? 507 NAG A H5 1 HETATM 6726 H H61 . NAG H 3 . ? 15.692 -4.454 43.489 1.00 26.22 ? 507 NAG A H61 1 HETATM 6727 H H62 . NAG H 3 . ? 15.680 -4.392 45.082 1.00 26.22 ? 507 NAG A H62 1 HETATM 6728 H H81 . NAG H 3 . ? 13.881 3.715 43.261 1.00 23.23 ? 507 NAG A H81 1 HETATM 6729 H H82 . NAG H 3 . ? 13.404 3.882 41.749 1.00 23.23 ? 507 NAG A H82 1 HETATM 6730 H H83 . NAG H 3 . ? 14.958 3.770 42.087 1.00 23.23 ? 507 NAG A H83 1 HETATM 6731 H HN2 . NAG H 3 . ? 15.368 1.737 43.533 1.00 20.62 ? 507 NAG A HN2 1 HETATM 6732 H HO3 . NAG H 3 . ? 12.979 0.541 45.000 1.00 26.50 ? 507 NAG A HO3 1 HETATM 6733 H HO6 . NAG H 3 . ? 17.727 -4.692 43.528 1.00 30.77 ? 507 NAG A HO6 1 HETATM 6734 C C1 . MAN I 5 . ? 8.539 -6.695 53.184 1.00 36.86 ? 508 MAN A C1 1 HETATM 6735 C C2 . MAN I 5 . ? 7.864 -8.074 53.059 1.00 36.45 ? 508 MAN A C2 1 HETATM 6736 C C3 . MAN I 5 . ? 6.341 -7.879 53.102 1.00 35.80 ? 508 MAN A C3 1 HETATM 6737 C C4 . MAN I 5 . ? 5.934 -7.165 54.394 1.00 35.22 ? 508 MAN A C4 1 HETATM 6738 C C5 . MAN I 5 . ? 6.660 -5.825 54.514 1.00 35.10 ? 508 MAN A C5 1 HETATM 6739 C C6 . MAN I 5 . ? 6.459 -5.173 55.868 1.00 35.03 ? 508 MAN A C6 1 HETATM 6740 O O2 . MAN I 5 . ? 8.206 -8.913 54.159 1.00 38.62 ? 508 MAN A O2 1 HETATM 6741 O O3 . MAN I 5 . ? 5.599 -9.112 52.938 1.00 38.31 ? 508 MAN A O3 1 HETATM 6742 O O4 . MAN I 5 . ? 4.550 -6.903 54.372 1.00 38.22 ? 508 MAN A O4 1 HETATM 6743 O O5 . MAN I 5 . ? 8.099 -5.998 54.356 1.00 37.30 ? 508 MAN A O5 1 HETATM 6744 O O6 . MAN I 5 . ? 7.703 -5.254 56.571 1.00 37.00 ? 508 MAN A O6 1 HETATM 6745 H H1 . MAN I 5 . ? 9.628 -6.801 53.305 1.00 44.23 ? 508 MAN A H1 1 HETATM 6746 H H2 . MAN I 5 . ? 8.159 -8.530 52.105 1.00 43.74 ? 508 MAN A H2 1 HETATM 6747 H H3 . MAN I 5 . ? 6.051 -7.240 52.262 1.00 42.97 ? 508 MAN A H3 1 HETATM 6748 H H4 . MAN I 5 . ? 6.212 -7.797 55.255 1.00 42.26 ? 508 MAN A H4 1 HETATM 6749 H H5 . MAN I 5 . ? 6.279 -5.142 53.743 1.00 42.12 ? 508 MAN A H5 1 HETATM 6750 H H61 . MAN I 5 . ? 5.654 -5.704 56.399 1.00 42.04 ? 508 MAN A H61 1 HETATM 6751 H H62 . MAN I 5 . ? 6.144 -4.134 55.701 1.00 42.04 ? 508 MAN A H62 1 HETATM 6752 H HO2 . MAN I 5 . ? 8.555 -9.747 53.821 1.00 46.34 ? 508 MAN A HO2 1 HETATM 6753 H HO3 . MAN I 5 . ? 4.795 -8.866 52.454 1.00 45.98 ? 508 MAN A HO3 1 HETATM 6754 H HO4 . MAN I 5 . ? 4.433 -6.206 53.708 1.00 45.87 ? 508 MAN A HO4 1 HETATM 6755 H HO6 . MAN I 5 . ? 7.977 -6.180 56.572 1.00 44.40 ? 508 MAN A HO6 1 HETATM 6756 C C1 . NAG J 3 . ? 13.004 -3.209 46.024 1.00 25.50 ? 509 NAG A C1 1 HETATM 6757 C C2 . NAG J 3 . ? 13.076 -3.887 47.394 1.00 26.40 ? 509 NAG A C2 1 HETATM 6758 C C3 . NAG J 3 . ? 11.763 -4.603 47.707 1.00 28.79 ? 509 NAG A C3 1 HETATM 6759 C C4 . NAG J 3 . ? 10.567 -3.689 47.483 1.00 30.36 ? 509 NAG A C4 1 HETATM 6760 C C5 . NAG J 3 . ? 10.642 -3.025 46.111 1.00 29.88 ? 509 NAG A C5 1 HETATM 6761 C C6 . NAG J 3 . ? 9.545 -2.008 45.859 1.00 32.28 ? 509 NAG A C6 1 HETATM 6762 C C7 . NAG J 3 . ? 15.350 -4.584 48.059 1.00 22.29 ? 509 NAG A C7 1 HETATM 6763 C C8 . NAG J 3 . ? 16.359 -5.687 48.009 1.00 23.85 ? 509 NAG A C8 1 HETATM 6764 N N2 . NAG J 3 . ? 14.185 -4.829 47.450 1.00 24.46 ? 509 NAG A N2 1 HETATM 6765 O O3 . NAG J 3 . ? 11.787 -5.044 49.062 1.00 30.73 ? 509 NAG A O3 1 HETATM 6766 O O4 . NAG J 3 . ? 9.381 -4.473 47.528 1.00 33.43 ? 509 NAG A O4 1 HETATM 6767 O O5 . NAG J 3 . ? 11.897 -2.344 45.978 1.00 27.41 ? 509 NAG A O5 1 HETATM 6768 O O6 . NAG J 3 . ? 9.509 -0.984 46.845 1.00 34.40 ? 509 NAG A O6 1 HETATM 6769 O O7 . NAG J 3 . ? 15.584 -3.520 48.619 1.00 24.23 ? 509 NAG A O7 1 HETATM 6770 H H1 . NAG J 3 . ? 12.929 -3.884 45.323 1.00 30.61 ? 509 NAG A H1 1 HETATM 6771 H H2 . NAG J 3 . ? 13.216 -3.198 48.072 1.00 31.68 ? 509 NAG A H2 1 HETATM 6772 H H3 . NAG J 3 . ? 11.680 -5.380 47.123 1.00 34.55 ? 509 NAG A H3 1 HETATM 6773 H H4 . NAG J 3 . ? 10.538 -3.005 48.179 1.00 36.43 ? 509 NAG A H4 1 HETATM 6774 H H5 . NAG J 3 . ? 10.588 -3.719 45.426 1.00 35.85 ? 509 NAG A H5 1 HETATM 6775 H H61 . NAG J 3 . ? 8.685 -2.469 45.852 1.00 38.74 ? 509 NAG A H61 1 HETATM 6776 H H62 . NAG J 3 . ? 9.691 -1.599 44.985 1.00 38.74 ? 509 NAG A H62 1 HETATM 6777 H H81 . NAG J 3 . ? 16.576 -5.887 47.079 1.00 28.62 ? 509 NAG A H81 1 HETATM 6778 H H82 . NAG J 3 . ? 15.992 -6.483 48.437 1.00 28.62 ? 509 NAG A H82 1 HETATM 6779 H H83 . NAG J 3 . ? 17.168 -5.409 48.480 1.00 28.62 ? 509 NAG A H83 1 HETATM 6780 H HN2 . NAG J 3 . ? 14.073 -5.643 47.052 1.00 29.35 ? 509 NAG A HN2 1 HETATM 6781 H HO3 . NAG J 3 . ? 11.177 -4.600 49.530 1.00 36.88 ? 509 NAG A HO3 1 HETATM 6782 H HO6 . NAG J 3 . ? 9.256 -0.220 46.469 1.00 41.28 ? 509 NAG A HO6 1 HETATM 6783 C C1 . FUC K 6 . ? -22.960 22.281 27.458 1.00 33.72 ? 510 FUC A C1 1 HETATM 6784 C C2 . FUC K 6 . ? -23.829 21.690 26.368 1.00 34.41 ? 510 FUC A C2 1 HETATM 6785 C C3 . FUC K 6 . ? -23.091 20.508 25.692 1.00 32.44 ? 510 FUC A C3 1 HETATM 6786 C C4 . FUC K 6 . ? -22.716 19.456 26.754 1.00 31.85 ? 510 FUC A C4 1 HETATM 6787 C C5 . FUC K 6 . ? -21.897 20.101 27.872 1.00 32.32 ? 510 FUC A C5 1 HETATM 6788 C C6 . FUC K 6 . ? -21.631 19.175 29.058 1.00 32.79 ? 510 FUC A C6 1 HETATM 6789 O O2 . FUC K 6 . ? -24.218 22.681 25.417 1.00 37.42 ? 510 FUC A O2 1 HETATM 6790 O O3 . FUC K 6 . ? -23.939 19.883 24.761 1.00 33.19 ? 510 FUC A O3 1 HETATM 6791 O O4 . FUC K 6 . ? -23.910 18.942 27.284 1.00 32.80 ? 510 FUC A O4 1 HETATM 6792 O O5 . FUC K 6 . ? -22.576 21.277 28.399 1.00 31.85 ? 510 FUC A O5 1 HETATM 6793 H H1 . FUC K 6 . ? -23.493 23.052 28.028 1.00 40.46 ? 510 FUC A H1 1 HETATM 6794 H H2 . FUC K 6 . ? -24.743 21.308 26.830 1.00 41.30 ? 510 FUC A H2 1 HETATM 6795 H H3 . FUC K 6 . ? -22.177 20.878 25.202 1.00 38.93 ? 510 FUC A H3 1 HETATM 6796 H H4 . FUC K 6 . ? -22.107 18.661 26.289 1.00 38.23 ? 510 FUC A H4 1 HETATM 6797 H H5 . FUC K 6 . ? -20.946 20.424 27.424 1.00 38.79 ? 510 FUC A H5 1 HETATM 6798 H H61 . FUC K 6 . ? -22.577 18.845 29.498 1.00 39.34 ? 510 FUC A H61 1 HETATM 6799 H H62 . FUC K 6 . ? -21.045 19.700 29.816 1.00 39.34 ? 510 FUC A H62 1 HETATM 6800 H H63 . FUC K 6 . ? -21.071 18.292 28.732 1.00 39.34 ? 510 FUC A H63 1 HETATM 6801 H HO2 . FUC K 6 . ? -25.054 22.366 25.039 1.00 44.91 ? 510 FUC A HO2 1 HETATM 6802 H HO3 . FUC K 6 . ? -23.426 19.813 23.942 1.00 39.83 ? 510 FUC A HO3 1 HETATM 6803 H HO4 . FUC K 6 . ? -23.639 18.182 27.823 1.00 39.35 ? 510 FUC A HO4 1 HETATM 6804 C C1 . NAG L 3 . ? -17.965 23.430 25.757 1.00 24.60 ? 511 NAG A C1 1 HETATM 6805 C C2 . NAG L 3 . ? -16.939 24.120 26.684 1.00 25.71 ? 511 NAG A C2 1 HETATM 6806 C C3 . NAG L 3 . ? -17.383 24.118 28.161 1.00 25.44 ? 511 NAG A C3 1 HETATM 6807 C C4 . NAG L 3 . ? -18.855 24.433 28.337 1.00 29.19 ? 511 NAG A C4 1 HETATM 6808 C C5 . NAG L 3 . ? -19.654 23.576 27.387 1.00 28.89 ? 511 NAG A C5 1 HETATM 6809 C C6 . NAG L 3 . ? -21.135 23.807 27.510 1.00 31.10 ? 511 NAG A C6 1 HETATM 6810 C C7 . NAG L 3 . ? -14.523 24.012 26.193 1.00 28.84 ? 511 NAG A C7 1 HETATM 6811 C C8 . NAG L 3 . ? -13.332 23.117 26.170 1.00 27.78 ? 511 NAG A C8 1 HETATM 6812 N N2 . NAG L 3 . ? -15.662 23.436 26.575 1.00 27.40 ? 511 NAG A N2 1 HETATM 6813 O O3 . NAG L 3 . ? -16.599 25.070 28.870 1.00 26.89 ? 511 NAG A O3 1 HETATM 6814 O O4 . NAG L 3 . ? -19.233 24.076 29.662 1.00 34.19 ? 511 NAG A O4 1 HETATM 6815 O O5 . NAG L 3 . ? -19.262 23.893 26.046 1.00 27.74 ? 511 NAG A O5 1 HETATM 6816 O O6 . NAG L 3 . ? -21.846 22.849 26.742 1.00 32.52 ? 511 NAG A O6 1 HETATM 6817 O O7 . NAG L 3 . ? -14.460 25.196 25.869 1.00 30.92 ? 511 NAG A O7 1 HETATM 6818 H H1 . NAG L 3 . ? -17.928 22.465 25.898 1.00 29.52 ? 511 NAG A H1 1 HETATM 6819 H H2 . NAG L 3 . ? -16.829 25.046 26.396 1.00 30.85 ? 511 NAG A H2 1 HETATM 6820 H H3 . NAG L 3 . ? -17.209 23.233 28.535 1.00 30.53 ? 511 NAG A H3 1 HETATM 6821 H H4 . NAG L 3 . ? -19.026 25.380 28.173 1.00 35.03 ? 511 NAG A H4 1 HETATM 6822 H H5 . NAG L 3 . ? -19.460 22.635 27.564 1.00 34.67 ? 511 NAG A H5 1 HETATM 6823 H H61 . NAG L 3 . ? -21.350 24.703 27.187 1.00 37.32 ? 511 NAG A H61 1 HETATM 6824 H H62 . NAG L 3 . ? -21.398 23.729 28.447 1.00 37.32 ? 511 NAG A H62 1 HETATM 6825 H H81 . NAG L 3 . ? -12.550 23.624 25.880 1.00 33.34 ? 511 NAG A H81 1 HETATM 6826 H H82 . NAG L 3 . ? -13.490 22.380 25.551 1.00 33.34 ? 511 NAG A H82 1 HETATM 6827 H H83 . NAG L 3 . ? -13.175 22.762 27.066 1.00 33.34 ? 511 NAG A H83 1 HETATM 6828 H HN2 . NAG L 3 . ? -15.634 22.554 26.805 1.00 32.88 ? 511 NAG A HN2 1 HETATM 6829 H HO3 . NAG L 3 . ? -16.552 24.837 29.725 1.00 32.26 ? 511 NAG A HO3 1 HETATM 6830 C C1 . NAG M 3 . ? -19.752 25.182 30.412 1.00 39.53 ? 512 NAG A C1 1 HETATM 6831 C C2 . NAG M 3 . ? -20.170 24.623 31.766 1.00 42.95 ? 512 NAG A C2 1 HETATM 6832 C C3 . NAG M 3 . ? -20.738 25.735 32.639 1.00 44.68 ? 512 NAG A C3 1 HETATM 6833 C C4 . NAG M 3 . ? -19.756 26.898 32.726 1.00 45.15 ? 512 NAG A C4 1 HETATM 6834 C C5 . NAG M 3 . ? -19.322 27.341 31.329 1.00 43.63 ? 512 NAG A C5 1 HETATM 6835 C C6 . NAG M 3 . ? -18.248 28.403 31.351 1.00 45.27 ? 512 NAG A C6 1 HETATM 6836 C C7 . NAG M 3 . ? -20.892 22.290 32.022 1.00 46.67 ? 512 NAG A C7 1 HETATM 6837 C C8 . NAG M 3 . ? -21.999 21.297 31.803 1.00 46.97 ? 512 NAG A C8 1 HETATM 6838 N N2 . NAG M 3 . ? -21.134 23.543 31.620 1.00 44.72 ? 512 NAG A N2 1 HETATM 6839 O O3 . NAG M 3 . ? -21.003 25.217 33.938 1.00 46.21 ? 512 NAG A O3 1 HETATM 6840 O O4 . NAG M 3 . ? -20.373 27.995 33.390 1.00 46.49 ? 512 NAG A O4 1 HETATM 6841 O O5 . NAG M 3 . ? -18.787 26.224 30.600 1.00 41.31 ? 512 NAG A O5 1 HETATM 6842 O O6 . NAG M 3 . ? -18.168 29.075 30.101 1.00 47.25 ? 512 NAG A O6 1 HETATM 6843 O O7 . NAG M 3 . ? -19.826 21.970 32.540 1.00 49.26 ? 512 NAG A O7 1 HETATM 6844 H H1 . NAG M 3 . ? -20.535 25.546 29.957 1.00 47.44 ? 512 NAG A H1 1 HETATM 6845 H H2 . NAG M 3 . ? -19.375 24.270 32.209 1.00 51.54 ? 512 NAG A H2 1 HETATM 6846 H H3 . NAG M 3 . ? -21.573 26.053 32.246 1.00 53.62 ? 512 NAG A H3 1 HETATM 6847 H H4 . NAG M 3 . ? -18.970 26.617 33.232 1.00 54.18 ? 512 NAG A H4 1 HETATM 6848 H H5 . NAG M 3 . ? -20.100 27.687 30.852 1.00 52.36 ? 512 NAG A H5 1 HETATM 6849 H H61 . NAG M 3 . ? -17.388 27.985 31.545 1.00 54.32 ? 512 NAG A H61 1 HETATM 6850 H H62 . NAG M 3 . ? -18.454 29.052 32.050 1.00 54.32 ? 512 NAG A H62 1 HETATM 6851 H H81 . NAG M 3 . ? -22.200 21.239 30.849 1.00 56.37 ? 512 NAG A H81 1 HETATM 6852 H H82 . NAG M 3 . ? -22.796 21.586 32.287 1.00 56.37 ? 512 NAG A H82 1 HETATM 6853 H H83 . NAG M 3 . ? -21.719 20.421 32.130 1.00 56.37 ? 512 NAG A H83 1 HETATM 6854 H HN2 . NAG M 3 . ? -21.943 23.730 31.243 1.00 53.67 ? 512 NAG A HN2 1 HETATM 6855 H HO3 . NAG M 3 . ? -21.867 25.025 34.009 1.00 55.45 ? 512 NAG A HO3 1 HETATM 6856 H HO4 . NAG M 3 . ? -20.241 27.924 34.266 1.00 55.79 ? 512 NAG A HO4 1 HETATM 6857 H HO6 . NAG M 3 . ? -17.384 29.487 30.036 1.00 56.70 ? 512 NAG A HO6 1 HETATM 6858 N N . NO3 N 7 . ? 13.103 12.022 2.140 1.00 30.75 ? 513 NO3 A N 1 HETATM 6859 O O1 . NO3 N 7 . ? 12.572 11.960 3.281 1.00 28.47 ? 513 NO3 A O1 1 HETATM 6860 O O2 . NO3 N 7 . ? 13.633 13.088 1.780 1.00 33.25 ? 513 NO3 A O2 1 HETATM 6861 O O3 . NO3 N 7 . ? 13.090 11.035 1.355 1.00 35.56 ? 513 NO3 A O3 1 HETATM 6862 N N . NO3 O 7 . ? 22.082 11.912 38.653 1.00 38.93 ? 514 NO3 A N 1 HETATM 6863 O O1 . NO3 O 7 . ? 21.458 10.818 38.531 1.00 33.24 ? 514 NO3 A O1 1 HETATM 6864 O O2 . NO3 O 7 . ? 21.661 12.826 39.427 1.00 42.16 ? 514 NO3 A O2 1 HETATM 6865 O O3 . NO3 O 7 . ? 23.133 12.105 37.988 1.00 39.91 ? 514 NO3 A O3 1 HETATM 6866 C C1 . GOL P 8 . ? 2.441 24.300 20.990 1.00 31.33 ? 515 GOL A C1 1 HETATM 6867 O O1 . GOL P 8 . ? 2.645 23.187 21.798 1.00 33.41 ? 515 GOL A O1 1 HETATM 6868 C C2 . GOL P 8 . ? 3.784 24.998 20.899 1.00 31.18 ? 515 GOL A C2 1 HETATM 6869 O O2 . GOL P 8 . ? 3.736 25.991 19.905 1.00 29.77 ? 515 GOL A O2 1 HETATM 6870 C C3 . GOL P 8 . ? 4.095 25.631 22.240 1.00 32.67 ? 515 GOL A C3 1 HETATM 6871 O O3 . GOL P 8 . ? 3.254 26.739 22.405 1.00 33.13 ? 515 GOL A O3 1 HETATM 6872 H H11 . GOL P 8 . ? 2.101 23.995 20.000 1.00 37.59 ? 515 GOL A H11 1 HETATM 6873 H H12 . GOL P 8 . ? 1.696 24.961 21.432 1.00 37.59 ? 515 GOL A H12 1 HETATM 6874 H HO1 . GOL P 8 . ? 1.790 22.731 21.947 1.00 40.10 ? 515 GOL A HO1 1 HETATM 6875 H H2 . GOL P 8 . ? 4.554 24.264 20.663 1.00 37.41 ? 515 GOL A H2 1 HETATM 6876 H HO2 . GOL P 8 . ? 3.045 26.648 20.133 1.00 35.72 ? 515 GOL A HO2 1 HETATM 6877 H H31 . GOL P 8 . ? 3.927 24.912 23.041 1.00 39.20 ? 515 GOL A H31 1 HETATM 6878 H H32 . GOL P 8 . ? 5.138 25.946 22.271 1.00 39.20 ? 515 GOL A H32 1 HETATM 6879 H HO3 . GOL P 8 . ? 2.320 26.444 22.401 1.00 39.76 ? 515 GOL A HO3 1 HETATM 6880 O O . HOH Q 9 . ? 12.443 9.901 -0.317 1.00 34.42 ? 601 HOH A O 1 HETATM 6881 O O . HOH Q 9 . ? 16.941 -8.248 18.196 1.00 41.65 ? 602 HOH A O 1 HETATM 6882 O O . HOH Q 9 . ? -6.461 5.517 42.453 1.00 35.23 ? 603 HOH A O 1 HETATM 6883 O O . HOH Q 9 . ? 0.864 28.836 5.814 1.00 41.33 ? 604 HOH A O 1 HETATM 6884 O O . HOH Q 9 . ? 8.299 21.504 0.332 1.00 40.72 ? 605 HOH A O 1 HETATM 6885 O O . HOH Q 9 . ? -25.321 21.322 23.487 1.00 40.87 ? 606 HOH A O 1 HETATM 6886 O O . HOH Q 9 . ? -10.681 27.897 8.023 1.00 36.10 ? 607 HOH A O 1 HETATM 6887 O O . HOH Q 9 . ? -14.667 4.180 31.035 1.00 38.12 ? 608 HOH A O 1 HETATM 6888 O O . HOH Q 9 . ? 14.267 2.966 2.735 1.00 33.48 ? 609 HOH A O 1 HETATM 6889 O O . HOH Q 9 . ? 2.713 -10.119 18.088 1.00 42.31 ? 610 HOH A O 1 HETATM 6890 O O . HOH Q 9 . ? 22.142 21.162 -0.177 1.00 32.12 ? 611 HOH A O 1 HETATM 6891 O O . HOH Q 9 . ? 20.847 0.406 22.872 1.00 30.76 ? 612 HOH A O 1 HETATM 6892 O O . HOH Q 9 . ? 1.762 21.100 24.417 1.00 13.29 ? 613 HOH A O 1 HETATM 6893 O O . HOH Q 9 . ? -13.664 4.112 22.584 1.00 32.27 ? 614 HOH A O 1 HETATM 6894 O O . HOH Q 9 . ? 5.621 -7.919 20.284 1.00 42.68 ? 615 HOH A O 1 HETATM 6895 O O . HOH Q 9 . ? -12.513 14.558 40.572 1.00 29.42 ? 616 HOH A O 1 HETATM 6896 O O . HOH Q 9 . ? 8.117 33.006 21.467 1.00 43.90 ? 617 HOH A O 1 HETATM 6897 O O . HOH Q 9 . ? 27.375 16.220 34.564 1.00 33.42 ? 618 HOH A O 1 HETATM 6898 O O . HOH Q 9 . ? 5.464 -3.494 31.078 1.00 31.84 ? 619 HOH A O 1 HETATM 6899 O O . HOH Q 9 . ? 23.490 8.313 0.628 1.00 42.35 ? 620 HOH A O 1 HETATM 6900 O O . HOH Q 9 . ? 8.825 -6.493 22.949 1.00 36.87 ? 621 HOH A O 1 HETATM 6901 O O . HOH Q 9 . ? -7.453 12.699 3.056 1.00 32.65 ? 622 HOH A O 1 HETATM 6902 O O . HOH Q 9 . ? 7.050 15.601 10.776 1.00 11.66 ? 623 HOH A O 1 HETATM 6903 O O . HOH Q 9 . ? -25.887 20.129 28.304 1.00 41.87 ? 624 HOH A O 1 HETATM 6904 O O . HOH Q 9 . ? 1.080 14.866 50.247 1.00 26.50 ? 625 HOH A O 1 HETATM 6905 O O . HOH Q 9 . ? 5.330 -2.836 44.727 1.00 50.03 ? 626 HOH A O 1 HETATM 6906 O O . HOH Q 9 . ? -9.865 9.783 1.212 1.00 36.96 ? 627 HOH A O 1 HETATM 6907 O O . HOH Q 9 . ? -17.005 27.727 28.306 1.00 42.73 ? 628 HOH A O 1 HETATM 6908 O O . HOH Q 9 . ? -4.660 33.703 13.194 1.00 39.23 ? 629 HOH A O 1 HETATM 6909 O O . HOH Q 9 . ? 21.956 26.690 33.130 1.00 20.66 ? 630 HOH A O 1 HETATM 6910 O O . HOH Q 9 . ? 28.368 18.946 16.552 1.00 33.55 ? 631 HOH A O 1 HETATM 6911 O O . HOH Q 9 . ? -3.010 11.907 28.983 1.00 14.37 ? 632 HOH A O 1 HETATM 6912 O O . HOH Q 9 . ? 3.192 -4.494 52.133 1.00 48.25 ? 633 HOH A O 1 HETATM 6913 O O . HOH Q 9 . ? 21.378 -7.820 29.715 1.00 37.50 ? 634 HOH A O 1 HETATM 6914 O O . HOH Q 9 . ? 29.542 9.164 17.307 1.00 40.43 ? 635 HOH A O 1 HETATM 6915 O O . HOH Q 9 . ? -12.693 -0.982 16.447 1.00 40.78 ? 636 HOH A O 1 HETATM 6916 O O . HOH Q 9 . ? -15.608 27.486 25.854 1.00 35.71 ? 637 HOH A O 1 HETATM 6917 O O . HOH Q 9 . ? 4.198 28.698 44.508 1.00 39.30 ? 638 HOH A O 1 HETATM 6918 O O . HOH Q 9 . ? 8.872 28.763 30.130 1.00 28.83 ? 639 HOH A O 1 HETATM 6919 O O . HOH Q 9 . ? -6.138 2.742 45.191 1.00 48.44 ? 640 HOH A O 1 HETATM 6920 O O . HOH Q 9 . ? -13.762 30.584 30.008 1.00 41.68 ? 641 HOH A O 1 HETATM 6921 O O . HOH Q 9 . ? 5.997 -4.930 16.377 1.00 25.19 ? 642 HOH A O 1 HETATM 6922 O O . HOH Q 9 . ? 8.488 29.762 6.925 1.00 42.40 ? 643 HOH A O 1 HETATM 6923 O O . HOH Q 9 . ? 21.410 -7.085 18.336 1.00 35.84 ? 644 HOH A O 1 HETATM 6924 O O . HOH Q 9 . ? -20.833 13.764 -0.417 1.00 39.63 ? 645 HOH A O 1 HETATM 6925 O O . HOH Q 9 . ? 29.162 35.084 21.527 1.00 44.10 ? 646 HOH A O 1 HETATM 6926 O O . HOH Q 9 . ? 24.967 4.594 39.887 1.00 41.94 ? 647 HOH A O 1 HETATM 6927 O O . HOH Q 9 . ? 11.416 -1.428 42.649 1.00 30.33 ? 648 HOH A O 1 HETATM 6928 O O . HOH Q 9 . ? 6.158 29.116 12.618 1.00 40.20 ? 649 HOH A O 1 HETATM 6929 O O . HOH Q 9 . ? -9.298 20.854 40.244 1.00 37.82 ? 650 HOH A O 1 HETATM 6930 O O . HOH Q 9 . ? -0.599 26.273 41.509 1.00 27.54 ? 651 HOH A O 1 HETATM 6931 O O . HOH Q 9 . ? 15.657 28.234 19.152 1.00 15.38 ? 652 HOH A O 1 HETATM 6932 O O . HOH Q 9 . ? 17.184 6.885 47.147 1.00 28.88 ? 653 HOH A O 1 HETATM 6933 O O . HOH Q 9 . ? 11.980 16.363 40.608 1.00 15.64 ? 654 HOH A O 1 HETATM 6934 O O . HOH Q 9 . ? -16.019 16.410 12.780 1.00 25.76 ? 655 HOH A O 1 HETATM 6935 O O . HOH Q 9 . ? 1.046 26.999 23.822 1.00 45.82 ? 656 HOH A O 1 HETATM 6936 O O . HOH Q 9 . ? 27.245 17.961 5.341 1.00 40.38 ? 657 HOH A O 1 HETATM 6937 O O . HOH Q 9 . ? -9.260 22.597 2.371 1.00 37.44 ? 658 HOH A O 1 HETATM 6938 O O . HOH Q 9 . ? 25.266 1.949 25.898 1.00 36.64 ? 659 HOH A O 1 HETATM 6939 O O . HOH Q 9 . ? -14.535 21.172 3.883 1.00 34.30 ? 660 HOH A O 1 HETATM 6940 O O . HOH Q 9 . ? 8.545 36.445 14.828 1.00 34.43 ? 661 HOH A O 1 HETATM 6941 O O . HOH Q 9 . ? 19.632 14.086 41.348 1.00 43.56 ? 662 HOH A O 1 HETATM 6942 O O . HOH Q 9 . ? 7.451 0.247 10.392 1.00 33.48 ? 663 HOH A O 1 HETATM 6943 O O . HOH Q 9 . ? -0.309 22.442 17.160 1.00 14.50 ? 664 HOH A O 1 HETATM 6944 O O . HOH Q 9 . ? 4.956 29.070 28.124 1.00 36.56 ? 665 HOH A O 1 HETATM 6945 O O . HOH Q 9 . ? -5.370 28.084 29.002 1.00 40.18 ? 666 HOH A O 1 HETATM 6946 O O . HOH Q 9 . ? 4.060 -7.220 18.186 1.00 35.69 ? 667 HOH A O 1 HETATM 6947 O O . HOH Q 9 . ? -12.948 38.107 16.423 1.00 36.35 ? 668 HOH A O 1 HETATM 6948 O O . HOH Q 9 . ? -8.301 -5.227 26.326 1.00 46.85 ? 669 HOH A O 1 HETATM 6949 O O . HOH Q 9 . ? 16.388 3.523 4.422 1.00 28.97 ? 670 HOH A O 1 HETATM 6950 O O . HOH Q 9 . ? 0.134 -5.058 19.994 1.00 20.12 ? 671 HOH A O 1 HETATM 6951 O O . HOH Q 9 . ? 20.402 -4.973 27.766 1.00 32.93 ? 672 HOH A O 1 HETATM 6952 O O . HOH Q 9 . ? -11.266 23.380 8.446 1.00 21.83 ? 673 HOH A O 1 HETATM 6953 O O . HOH Q 9 . ? -7.829 28.119 9.123 1.00 38.73 ? 674 HOH A O 1 HETATM 6954 O O . HOH Q 9 . ? 3.770 11.155 16.749 1.00 15.26 ? 675 HOH A O 1 HETATM 6955 O O . HOH Q 9 . ? 15.778 1.209 8.239 1.00 25.96 ? 676 HOH A O 1 HETATM 6956 O O . HOH Q 9 . ? 4.152 26.338 10.721 1.00 33.09 ? 677 HOH A O 1 HETATM 6957 O O . HOH Q 9 . ? 12.505 29.187 14.258 1.00 20.29 ? 678 HOH A O 1 HETATM 6958 O O . HOH Q 9 . ? 9.685 1.576 38.780 1.00 29.07 ? 679 HOH A O 1 HETATM 6959 O O . HOH Q 9 . ? 22.767 19.580 23.975 1.00 14.83 ? 680 HOH A O 1 HETATM 6960 O O . HOH Q 9 . ? 18.304 0.983 10.124 1.00 24.55 ? 681 HOH A O 1 HETATM 6961 O O . HOH Q 9 . ? 7.748 24.012 8.111 1.00 17.26 ? 682 HOH A O 1 HETATM 6962 O O . HOH Q 9 . ? -20.917 34.781 17.634 1.00 41.80 ? 683 HOH A O 1 HETATM 6963 O O . HOH Q 9 . ? 15.634 -0.856 48.270 1.00 29.77 ? 684 HOH A O 1 HETATM 6964 O O . HOH Q 9 . ? -12.202 9.821 34.240 1.00 24.84 ? 685 HOH A O 1 HETATM 6965 O O . HOH Q 9 . ? 32.512 12.856 31.445 1.00 24.17 ? 686 HOH A O 1 HETATM 6966 O O . HOH Q 9 . ? -1.031 10.460 27.788 1.00 13.07 ? 687 HOH A O 1 HETATM 6967 O O . HOH Q 9 . ? 8.246 24.542 38.235 1.00 22.97 ? 688 HOH A O 1 HETATM 6968 O O . HOH Q 9 . ? 2.589 1.249 31.347 1.00 21.77 ? 689 HOH A O 1 HETATM 6969 O O . HOH Q 9 . ? 5.028 13.306 44.212 1.00 27.26 ? 690 HOH A O 1 HETATM 6970 O O . HOH Q 9 . ? 2.017 -4.917 23.760 1.00 22.91 ? 691 HOH A O 1 HETATM 6971 O O . HOH Q 9 . ? 7.098 31.157 33.305 1.00 40.51 ? 692 HOH A O 1 HETATM 6972 O O . HOH Q 9 . ? -10.537 8.310 41.465 1.00 29.60 ? 693 HOH A O 1 HETATM 6973 O O . HOH Q 9 . ? 16.155 26.335 4.187 1.00 24.44 ? 694 HOH A O 1 HETATM 6974 O O . HOH Q 9 . ? 2.056 -1.123 7.084 1.00 44.55 ? 695 HOH A O 1 HETATM 6975 O O . HOH Q 9 . ? -0.106 23.336 3.662 1.00 31.49 ? 696 HOH A O 1 HETATM 6976 O O . HOH Q 9 . ? 13.054 15.540 10.840 1.00 15.02 ? 697 HOH A O 1 HETATM 6977 O O . HOH Q 9 . ? 0.087 -0.860 44.474 1.00 32.00 ? 698 HOH A O 1 HETATM 6978 O O . HOH Q 9 . ? 17.944 25.826 2.533 1.00 29.94 ? 699 HOH A O 1 HETATM 6979 O O . HOH Q 9 . ? 21.284 0.812 7.432 1.00 47.18 ? 700 HOH A O 1 HETATM 6980 O O . HOH Q 9 . ? 4.008 24.396 17.732 1.00 18.17 ? 701 HOH A O 1 HETATM 6981 O O . HOH Q 9 . ? 28.935 12.171 9.826 1.00 40.16 ? 702 HOH A O 1 HETATM 6982 O O . HOH Q 9 . ? 26.743 25.083 18.057 1.00 41.35 ? 703 HOH A O 1 HETATM 6983 O O . HOH Q 9 . ? 24.524 -2.943 32.273 1.00 25.65 ? 704 HOH A O 1 HETATM 6984 O O . HOH Q 9 . ? 23.252 3.937 35.061 1.00 22.21 ? 705 HOH A O 1 HETATM 6985 O O . HOH Q 9 . ? -3.354 -5.987 18.034 1.00 30.75 ? 706 HOH A O 1 HETATM 6986 O O . HOH Q 9 . ? 2.638 23.773 15.363 1.00 16.20 ? 707 HOH A O 1 HETATM 6987 O O . HOH Q 9 . ? 25.319 3.253 13.683 1.00 33.99 ? 708 HOH A O 1 HETATM 6988 O O . HOH Q 9 . ? -14.744 33.015 19.682 1.00 41.51 ? 709 HOH A O 1 HETATM 6989 O O . HOH Q 9 . ? 0.351 -4.539 31.584 1.00 43.94 ? 710 HOH A O 1 HETATM 6990 O O . HOH Q 9 . ? 8.661 30.029 13.879 1.00 31.22 ? 711 HOH A O 1 HETATM 6991 O O . HOH Q 9 . ? -7.775 34.788 19.980 1.00 30.69 ? 712 HOH A O 1 HETATM 6992 O O . HOH Q 9 . ? -8.808 34.090 11.183 1.00 29.83 ? 713 HOH A O 1 HETATM 6993 O O . HOH Q 9 . ? 12.692 28.629 31.715 1.00 26.41 ? 714 HOH A O 1 HETATM 6994 O O . HOH Q 9 . ? 14.863 -0.427 10.306 1.00 26.59 ? 715 HOH A O 1 HETATM 6995 O O . HOH Q 9 . ? 30.293 10.470 29.294 1.00 25.14 ? 716 HOH A O 1 HETATM 6996 O O . HOH Q 9 . ? 2.036 -5.899 39.569 1.00 35.03 ? 717 HOH A O 1 HETATM 6997 O O . HOH Q 9 . ? 13.698 21.276 23.662 1.00 12.29 ? 718 HOH A O 1 HETATM 6998 O O . HOH Q 9 . ? 0.378 30.938 24.172 1.00 39.42 ? 719 HOH A O 1 HETATM 6999 O O . HOH Q 9 . ? 16.266 14.640 46.210 1.00 30.46 ? 720 HOH A O 1 HETATM 7000 O O . HOH Q 9 . ? -3.690 29.999 23.883 1.00 30.82 ? 721 HOH A O 1 HETATM 7001 O O . HOH Q 9 . ? -18.176 25.523 19.095 1.00 25.66 ? 722 HOH A O 1 HETATM 7002 O O . HOH Q 9 . ? -15.143 13.213 34.965 1.00 20.74 ? 723 HOH A O 1 HETATM 7003 O O . HOH Q 9 . ? 4.512 24.141 13.163 1.00 21.61 ? 724 HOH A O 1 HETATM 7004 O O . HOH Q 9 . ? 11.983 34.367 16.629 1.00 36.98 ? 725 HOH A O 1 HETATM 7005 O O . HOH Q 9 . ? 23.243 -7.899 35.353 1.00 41.95 ? 726 HOH A O 1 HETATM 7006 O O . HOH Q 9 . ? 10.658 2.374 41.204 1.00 18.85 ? 727 HOH A O 1 HETATM 7007 O O . HOH Q 9 . ? -3.325 27.499 34.954 1.00 22.44 ? 728 HOH A O 1 HETATM 7008 O O . HOH Q 9 . ? 1.348 -6.557 12.095 1.00 37.03 ? 729 HOH A O 1 HETATM 7009 O O . HOH Q 9 . ? 16.315 -2.626 36.912 1.00 24.40 ? 730 HOH A O 1 HETATM 7010 O O . HOH Q 9 . ? 17.724 31.947 26.526 1.00 37.81 ? 731 HOH A O 1 HETATM 7011 O O . HOH Q 9 . ? -4.367 -1.478 25.394 1.00 29.85 ? 732 HOH A O 1 HETATM 7012 O O . HOH Q 9 . ? 27.000 13.694 38.148 1.00 39.34 ? 733 HOH A O 1 HETATM 7013 O O . HOH Q 9 . ? -3.122 12.952 3.944 1.00 22.08 ? 734 HOH A O 1 HETATM 7014 O O . HOH Q 9 . ? 5.376 14.151 31.559 1.00 12.03 ? 735 HOH A O 1 HETATM 7015 O O . HOH Q 9 . ? 23.130 0.235 11.535 1.00 37.49 ? 736 HOH A O 1 HETATM 7016 O O . HOH Q 9 . ? -12.103 30.227 23.978 1.00 39.96 ? 737 HOH A O 1 HETATM 7017 O O . HOH Q 9 . ? 5.761 8.960 42.104 1.00 27.77 ? 738 HOH A O 1 HETATM 7018 O O . HOH Q 9 . ? 13.952 22.106 47.752 1.00 32.96 ? 739 HOH A O 1 HETATM 7019 O O . HOH Q 9 . ? 4.084 17.140 20.139 1.00 14.94 ? 740 HOH A O 1 HETATM 7020 O O . HOH Q 9 . ? 26.617 27.088 12.073 1.00 37.16 ? 741 HOH A O 1 HETATM 7021 O O . HOH Q 9 . ? 6.973 -1.807 37.272 1.00 23.75 ? 742 HOH A O 1 HETATM 7022 O O . HOH Q 9 . ? 18.857 -3.312 46.466 0.50 34.11 ? 743 HOH A O 1 HETATM 7023 O O . HOH Q 9 . ? 17.457 23.064 23.202 1.00 12.97 ? 744 HOH A O 1 HETATM 7024 O O . HOH Q 9 . ? 19.538 11.048 40.737 1.00 17.77 ? 745 HOH A O 1 HETATM 7025 O O . HOH Q 9 . ? -12.966 31.516 17.092 1.00 21.63 ? 746 HOH A O 1 HETATM 7026 O O . HOH Q 9 . ? -15.205 9.881 29.415 1.00 20.49 ? 747 HOH A O 1 HETATM 7027 O O . HOH Q 9 . ? 1.474 31.042 15.266 1.00 16.25 ? 748 HOH A O 1 HETATM 7028 O O . HOH Q 9 . ? 29.905 9.093 21.026 1.00 44.63 ? 749 HOH A O 1 HETATM 7029 O O . HOH Q 9 . ? 10.000 34.328 17.846 1.00 35.36 ? 750 HOH A O 1 HETATM 7030 O O . HOH Q 9 . ? -9.857 8.115 8.793 1.00 25.36 ? 751 HOH A O 1 HETATM 7031 O O . HOH Q 9 . ? -5.794 -1.745 41.660 1.00 45.93 ? 752 HOH A O 1 HETATM 7032 O O . HOH Q 9 . ? -10.329 3.780 30.756 1.00 24.52 ? 753 HOH A O 1 HETATM 7033 O O . HOH Q 9 . ? 13.858 26.470 -0.030 1.00 32.27 ? 754 HOH A O 1 HETATM 7034 O O . HOH Q 9 . ? 13.640 29.053 21.868 1.00 15.05 ? 755 HOH A O 1 HETATM 7035 O O . HOH Q 9 . ? 11.995 -3.179 51.090 1.00 36.11 ? 756 HOH A O 1 HETATM 7036 O O . HOH Q 9 . ? 14.483 6.401 44.818 1.00 29.73 ? 757 HOH A O 1 HETATM 7037 O O . HOH Q 9 . ? -4.004 -4.634 20.393 1.00 20.36 ? 758 HOH A O 1 HETATM 7038 O O . HOH Q 9 . ? 28.016 6.702 19.146 1.00 39.76 ? 759 HOH A O 1 HETATM 7039 O O . HOH Q 9 . ? 3.454 11.582 33.543 1.00 13.27 ? 760 HOH A O 1 HETATM 7040 O O . HOH Q 9 . ? 25.648 6.363 25.447 1.00 24.37 ? 761 HOH A O 1 HETATM 7041 O O . HOH Q 9 . ? 14.000 26.035 40.180 1.00 47.96 ? 762 HOH A O 1 HETATM 7042 O O . HOH Q 9 . ? 8.296 1.656 44.448 1.00 44.37 ? 763 HOH A O 1 HETATM 7043 O O . HOH Q 9 . ? 3.183 22.001 34.099 1.00 18.95 ? 764 HOH A O 1 HETATM 7044 O O . HOH Q 9 . ? -14.235 5.152 17.864 1.00 34.53 ? 765 HOH A O 1 HETATM 7045 O O . HOH Q 9 . ? 3.137 10.268 1.031 1.00 34.24 ? 766 HOH A O 1 HETATM 7046 O O . HOH Q 9 . ? 8.282 24.846 11.158 1.00 24.35 ? 767 HOH A O 1 HETATM 7047 O O . HOH Q 9 . ? 6.776 11.333 44.450 1.00 32.99 ? 768 HOH A O 1 HETATM 7048 O O . HOH Q 9 . ? -26.875 21.966 25.740 1.00 27.34 ? 769 HOH A O 1 HETATM 7049 O O . HOH Q 9 . ? 22.094 19.965 38.789 1.00 31.00 ? 770 HOH A O 1 HETATM 7050 O O . HOH Q 9 . ? 1.437 12.396 17.600 1.00 12.78 ? 771 HOH A O 1 HETATM 7051 O O . HOH Q 9 . ? -12.963 9.580 12.284 1.00 16.03 ? 772 HOH A O 1 HETATM 7052 O O . HOH Q 9 . ? -8.128 23.552 32.892 1.00 21.33 ? 773 HOH A O 1 HETATM 7053 O O . HOH Q 9 . ? 12.168 13.381 16.213 1.00 13.69 ? 774 HOH A O 1 HETATM 7054 O O . HOH Q 9 . ? -8.905 -3.282 17.100 1.00 33.82 ? 775 HOH A O 1 HETATM 7055 O O . HOH Q 9 . ? 22.303 24.920 7.201 1.00 23.64 ? 776 HOH A O 1 HETATM 7056 O O . HOH Q 9 . ? 15.125 19.963 0.183 1.00 20.12 ? 777 HOH A O 1 HETATM 7057 O O . HOH Q 9 . ? 1.598 33.373 17.898 1.00 24.45 ? 778 HOH A O 1 HETATM 7058 O O . HOH Q 9 . ? 12.601 23.150 28.699 1.00 12.69 ? 779 HOH A O 1 HETATM 7059 O O . HOH Q 9 . ? 7.134 1.865 38.794 1.00 22.05 ? 780 HOH A O 1 HETATM 7060 O O . HOH Q 9 . ? -9.760 10.780 42.004 1.00 28.13 ? 781 HOH A O 1 HETATM 7061 O O . HOH Q 9 . ? -2.479 13.224 23.797 1.00 12.63 ? 782 HOH A O 1 HETATM 7062 O O . HOH Q 9 . ? 19.660 30.741 27.755 1.00 26.92 ? 783 HOH A O 1 HETATM 7063 O O . HOH Q 9 . ? 15.485 -0.031 36.905 1.00 23.70 ? 784 HOH A O 1 HETATM 7064 O O . HOH Q 9 . ? -10.030 -3.091 25.260 1.00 39.40 ? 785 HOH A O 1 HETATM 7065 O O . HOH Q 9 . ? 25.347 7.301 5.873 1.00 45.69 ? 786 HOH A O 1 HETATM 7066 O O . HOH Q 9 . ? -6.081 30.042 19.627 1.00 22.05 ? 787 HOH A O 1 HETATM 7067 O O . HOH Q 9 . ? -15.712 29.394 19.778 1.00 34.40 ? 788 HOH A O 1 HETATM 7068 O O . HOH Q 9 . ? -5.075 28.932 17.115 1.00 16.77 ? 789 HOH A O 1 HETATM 7069 O O . HOH Q 9 . ? 20.786 2.386 16.688 1.00 21.91 ? 790 HOH A O 1 HETATM 7070 O O . HOH Q 9 . ? 11.350 9.257 3.339 1.00 18.97 ? 791 HOH A O 1 HETATM 7071 O O . HOH Q 9 . ? 26.190 8.660 10.314 1.00 33.14 ? 792 HOH A O 1 HETATM 7072 O O . HOH Q 9 . ? 23.895 20.414 34.176 1.00 27.13 ? 793 HOH A O 1 HETATM 7073 O O . HOH Q 9 . ? 19.029 3.883 20.156 1.00 17.41 ? 794 HOH A O 1 HETATM 7074 O O . HOH Q 9 . ? 10.028 23.861 0.583 1.00 21.09 ? 795 HOH A O 1 HETATM 7075 O O . HOH Q 9 . ? 13.340 15.642 13.703 1.00 15.09 ? 796 HOH A O 1 HETATM 7076 O O . HOH Q 9 . ? -8.480 21.080 14.291 1.00 12.17 ? 797 HOH A O 1 HETATM 7077 O O . HOH Q 9 . ? -6.113 23.184 28.823 1.00 19.00 ? 798 HOH A O 1 HETATM 7078 O O . HOH Q 9 . ? 16.214 -5.519 25.084 1.00 31.43 ? 799 HOH A O 1 HETATM 7079 O O . HOH Q 9 . ? -21.266 23.261 24.034 1.00 38.47 ? 800 HOH A O 1 HETATM 7080 O O . HOH Q 9 . ? -6.934 30.118 32.108 1.00 33.08 ? 801 HOH A O 1 HETATM 7081 O O . HOH Q 9 . ? 0.731 26.490 4.583 1.00 30.89 ? 802 HOH A O 1 HETATM 7082 O O . HOH Q 9 . ? 21.571 -0.019 41.833 1.00 24.99 ? 803 HOH A O 1 HETATM 7083 O O . HOH Q 9 . ? -4.983 -3.431 10.531 1.00 26.69 ? 804 HOH A O 1 HETATM 7084 O O . HOH Q 9 . ? 34.565 20.435 27.902 1.00 33.43 ? 805 HOH A O 1 HETATM 7085 O O . HOH Q 9 . ? -17.121 7.140 10.025 1.00 47.03 ? 806 HOH A O 1 HETATM 7086 O O . HOH Q 9 . ? -16.813 10.404 31.511 1.00 36.54 ? 807 HOH A O 1 HETATM 7087 O O . HOH Q 9 . ? 25.793 6.442 12.217 1.00 25.59 ? 808 HOH A O 1 HETATM 7088 O O . HOH Q 9 . ? 7.102 17.904 19.657 1.00 15.58 ? 809 HOH A O 1 HETATM 7089 O O . HOH Q 9 . ? -4.210 32.828 11.206 1.00 53.26 ? 810 HOH A O 1 HETATM 7090 O O . HOH Q 9 . ? 25.567 -6.116 38.130 1.00 32.84 ? 811 HOH A O 1 HETATM 7091 O O . HOH Q 9 . ? -11.726 -3.745 21.207 1.00 29.98 ? 812 HOH A O 1 HETATM 7092 O O . HOH Q 9 . ? 26.033 1.450 32.706 1.00 38.13 ? 813 HOH A O 1 HETATM 7093 O O . HOH Q 9 . ? 14.529 33.212 8.640 1.00 38.48 ? 814 HOH A O 1 HETATM 7094 O O . HOH Q 9 . ? -3.414 8.338 46.690 1.00 23.69 ? 815 HOH A O 1 HETATM 7095 O O . HOH Q 9 . ? 0.604 33.890 12.729 1.00 40.15 ? 816 HOH A O 1 HETATM 7096 O O . HOH Q 9 . ? 16.601 22.015 41.118 1.00 31.44 ? 817 HOH A O 1 HETATM 7097 O O . HOH Q 9 . ? 22.728 -2.067 30.489 1.00 22.22 ? 818 HOH A O 1 HETATM 7098 O O . HOH Q 9 . ? -17.378 26.316 23.540 1.00 26.99 ? 819 HOH A O 1 HETATM 7099 O O . HOH Q 9 . ? 19.392 6.616 19.455 1.00 19.64 ? 820 HOH A O 1 HETATM 7100 O O . HOH Q 9 . ? -7.452 36.806 17.868 1.00 42.69 ? 821 HOH A O 1 HETATM 7101 O O . HOH Q 9 . ? -12.498 0.898 25.380 1.00 27.67 ? 822 HOH A O 1 HETATM 7102 O O . HOH Q 9 . ? 27.796 21.113 9.828 1.00 23.43 ? 823 HOH A O 1 HETATM 7103 O O . HOH Q 9 . ? 13.605 -7.135 45.924 1.00 41.89 ? 824 HOH A O 1 HETATM 7104 O O . HOH Q 9 . ? -16.449 17.534 16.941 1.00 24.14 ? 825 HOH A O 1 HETATM 7105 O O . HOH Q 9 . ? 0.521 3.522 30.916 1.00 18.49 ? 826 HOH A O 1 HETATM 7106 O O . HOH Q 9 . ? 8.464 17.104 46.754 1.00 27.82 ? 827 HOH A O 1 HETATM 7107 O O . HOH Q 9 . ? -2.790 22.324 41.491 1.00 22.52 ? 828 HOH A O 1 HETATM 7108 O O . HOH Q 9 . ? -12.249 7.981 10.075 1.00 24.99 ? 829 HOH A O 1 HETATM 7109 O O . HOH Q 9 . ? 3.526 23.810 46.747 1.00 44.19 ? 830 HOH A O 1 HETATM 7110 O O . HOH Q 9 . ? 12.451 30.959 28.394 1.00 23.78 ? 831 HOH A O 1 HETATM 7111 O O . HOH Q 9 . ? 21.166 2.648 21.969 1.00 40.43 ? 832 HOH A O 1 HETATM 7112 O O . HOH Q 9 . ? 12.786 19.139 46.688 1.00 30.55 ? 833 HOH A O 1 HETATM 7113 O O . HOH Q 9 . ? 0.335 18.692 51.569 1.00 38.65 ? 834 HOH A O 1 HETATM 7114 O O . HOH Q 9 . ? 3.345 20.478 45.019 1.00 28.18 ? 835 HOH A O 1 HETATM 7115 O O . HOH Q 9 . ? 26.233 5.948 31.854 1.00 17.56 ? 836 HOH A O 1 HETATM 7116 O O . HOH Q 9 . ? 25.686 11.304 41.442 1.00 42.91 ? 837 HOH A O 1 HETATM 7117 O O . HOH Q 9 . ? -13.555 28.837 25.917 1.00 33.64 ? 838 HOH A O 1 HETATM 7118 O O . HOH Q 9 . ? -14.785 17.091 19.087 1.00 13.51 ? 839 HOH A O 1 HETATM 7119 O O . HOH Q 9 . ? 10.099 19.819 18.512 1.00 13.26 ? 840 HOH A O 1 HETATM 7120 O O . HOH Q 9 . ? 26.080 29.812 15.951 1.00 43.05 ? 841 HOH A O 1 HETATM 7121 O O . HOH Q 9 . ? -16.643 28.000 9.353 1.00 31.79 ? 842 HOH A O 1 HETATM 7122 O O . HOH Q 9 . ? 31.695 9.387 31.383 1.00 42.47 ? 843 HOH A O 1 HETATM 7123 O O . HOH Q 9 . ? -15.979 9.397 6.473 1.00 43.83 ? 844 HOH A O 1 HETATM 7124 O O . HOH Q 9 . ? -2.433 -4.171 35.886 1.00 41.37 ? 845 HOH A O 1 HETATM 7125 O O . HOH Q 9 . ? 24.417 11.421 5.357 1.00 29.94 ? 846 HOH A O 1 HETATM 7126 O O . HOH Q 9 . ? 7.832 32.649 13.385 1.00 28.20 ? 847 HOH A O 1 HETATM 7127 O O . HOH Q 9 . ? -7.007 16.870 44.311 1.00 25.89 ? 848 HOH A O 1 HETATM 7128 O O . HOH Q 9 . ? 1.979 6.810 2.111 1.00 24.60 ? 849 HOH A O 1 HETATM 7129 O O . HOH Q 9 . ? 24.515 18.284 25.768 1.00 17.13 ? 850 HOH A O 1 HETATM 7130 O O . HOH Q 9 . ? 22.071 31.010 9.918 1.00 33.71 ? 851 HOH A O 1 HETATM 7131 O O . HOH Q 9 . ? 19.052 29.120 4.943 1.00 34.72 ? 852 HOH A O 1 HETATM 7132 O O . HOH Q 9 . ? -13.755 6.519 23.759 1.00 17.75 ? 853 HOH A O 1 HETATM 7133 O O . HOH Q 9 . ? 29.036 9.135 32.582 1.00 31.53 ? 854 HOH A O 1 HETATM 7134 O O . HOH Q 9 . ? -9.781 -1.023 31.102 1.00 36.64 ? 855 HOH A O 1 HETATM 7135 O O . HOH Q 9 . ? -10.219 30.912 9.044 1.00 29.27 ? 856 HOH A O 1 HETATM 7136 O O . HOH Q 9 . ? 0.520 5.630 46.364 1.00 22.75 ? 857 HOH A O 1 HETATM 7137 O O . HOH Q 9 . ? 10.448 27.303 -0.505 1.00 38.42 ? 858 HOH A O 1 HETATM 7138 O O . HOH Q 9 . ? 12.541 -6.771 28.265 1.00 28.86 ? 859 HOH A O 1 HETATM 7139 O O . HOH Q 9 . ? 27.492 27.451 22.106 1.00 31.31 ? 860 HOH A O 1 HETATM 7140 O O . HOH Q 9 . ? 26.508 13.976 35.555 1.00 20.84 ? 861 HOH A O 1 HETATM 7141 O O . HOH Q 9 . ? 21.466 -3.331 17.070 1.00 34.93 ? 862 HOH A O 1 HETATM 7142 O O . HOH Q 9 . ? 11.647 17.833 11.139 1.00 11.84 ? 863 HOH A O 1 HETATM 7143 O O . HOH Q 9 . ? 3.286 13.238 0.770 1.00 36.30 ? 864 HOH A O 1 HETATM 7144 O O . HOH Q 9 . ? 24.366 16.467 27.878 1.00 20.32 ? 865 HOH A O 1 HETATM 7145 O O . HOH Q 9 . ? 9.553 10.681 19.133 1.00 14.78 ? 866 HOH A O 1 HETATM 7146 O O . HOH Q 9 . ? 16.617 2.442 44.883 1.00 30.86 ? 867 HOH A O 1 HETATM 7147 O O . HOH Q 9 . ? 24.673 0.475 38.859 1.00 32.00 ? 868 HOH A O 1 HETATM 7148 O O . HOH Q 9 . ? -8.099 0.750 10.795 1.00 24.99 ? 869 HOH A O 1 HETATM 7149 O O . HOH Q 9 . ? 33.189 10.013 25.890 1.00 34.07 ? 870 HOH A O 1 HETATM 7150 O O . HOH Q 9 . ? -0.544 20.670 4.118 1.00 20.02 ? 871 HOH A O 1 HETATM 7151 O O . HOH Q 9 . ? 22.144 8.414 40.216 1.00 24.23 ? 872 HOH A O 1 HETATM 7152 O O . HOH Q 9 . ? -17.788 13.308 19.617 1.00 19.21 ? 873 HOH A O 1 HETATM 7153 O O . HOH Q 9 . ? -14.562 29.467 16.188 1.00 18.51 ? 874 HOH A O 1 HETATM 7154 O O . HOH Q 9 . ? 33.028 19.016 33.233 1.00 26.36 ? 875 HOH A O 1 HETATM 7155 O O . HOH Q 9 . ? -15.829 7.853 22.553 1.00 22.42 ? 876 HOH A O 1 HETATM 7156 O O . HOH Q 9 . ? -13.100 21.863 38.511 1.00 23.18 ? 877 HOH A O 1 HETATM 7157 O O . HOH Q 9 . ? 23.076 5.333 19.945 1.00 20.68 ? 878 HOH A O 1 HETATM 7158 O O . HOH Q 9 . ? 34.636 15.375 20.790 1.00 18.41 ? 879 HOH A O 1 HETATM 7159 O O . HOH Q 9 . ? -9.151 1.128 33.827 1.00 26.66 ? 880 HOH A O 1 HETATM 7160 O O . HOH Q 9 . ? 23.928 26.470 31.098 1.00 24.99 ? 881 HOH A O 1 HETATM 7161 O O . HOH Q 9 . ? 22.025 0.506 15.257 1.00 30.88 ? 882 HOH A O 1 HETATM 7162 O O . HOH Q 9 . ? -16.161 15.166 4.182 1.00 43.34 ? 883 HOH A O 1 HETATM 7163 O O . HOH Q 9 . ? -11.076 34.711 23.078 1.00 50.83 ? 884 HOH A O 1 HETATM 7164 O O . HOH Q 9 . ? 24.449 -0.165 29.415 1.00 28.64 ? 885 HOH A O 1 HETATM 7165 O O . HOH Q 9 . ? 25.669 32.311 27.625 1.00 34.58 ? 886 HOH A O 1 HETATM 7166 O O . HOH Q 9 . ? -4.970 -3.140 16.510 1.00 25.04 ? 887 HOH A O 1 HETATM 7167 O O . HOH Q 9 . ? 7.359 34.116 23.370 1.00 41.04 ? 888 HOH A O 1 HETATM 7168 O O . HOH Q 9 . ? 6.975 -3.817 34.980 1.00 30.44 ? 889 HOH A O 1 HETATM 7169 O O . HOH Q 9 . ? -8.655 -8.834 22.114 1.00 51.82 ? 890 HOH A O 1 HETATM 7170 O O . HOH Q 9 . ? 29.834 15.232 30.760 1.00 20.45 ? 891 HOH A O 1 HETATM 7171 O O . HOH Q 9 . ? -7.904 6.473 9.545 1.00 26.17 ? 892 HOH A O 1 HETATM 7172 O O . HOH Q 9 . ? -15.529 10.244 11.578 1.00 31.86 ? 893 HOH A O 1 HETATM 7173 O O . HOH Q 9 . ? 21.466 6.302 41.852 1.00 23.27 ? 894 HOH A O 1 HETATM 7174 O O . HOH Q 9 . ? 20.408 21.954 39.387 1.00 29.19 ? 895 HOH A O 1 HETATM 7175 O O . HOH Q 9 . ? 14.466 -0.447 39.307 1.00 29.95 ? 896 HOH A O 1 HETATM 7176 O O . HOH Q 9 . ? -12.034 32.753 31.550 1.00 43.45 ? 897 HOH A O 1 HETATM 7177 O O . HOH Q 9 . ? 4.888 -0.169 46.060 1.00 40.34 ? 898 HOH A O 1 HETATM 7178 O O . HOH Q 9 . ? 23.160 5.301 24.930 1.00 25.23 ? 899 HOH A O 1 HETATM 7179 O O . HOH Q 9 . ? -6.266 29.323 22.532 1.00 32.05 ? 900 HOH A O 1 HETATM 7180 O O . HOH Q 9 . ? -2.722 31.464 16.538 1.00 24.17 ? 901 HOH A O 1 HETATM 7181 O O . HOH Q 9 . ? 16.719 31.248 34.470 1.00 36.64 ? 902 HOH A O 1 HETATM 7182 O O . HOH Q 9 . ? 31.155 15.341 13.484 1.00 44.73 ? 903 HOH A O 1 HETATM 7183 O O . HOH Q 9 . ? 3.874 27.072 2.509 1.00 30.02 ? 904 HOH A O 1 HETATM 7184 O O . HOH Q 9 . ? 15.935 17.835 -1.205 1.00 25.40 ? 905 HOH A O 1 HETATM 7185 O O . HOH Q 9 . ? 25.864 5.814 17.919 1.00 22.86 ? 906 HOH A O 1 HETATM 7186 O O . HOH Q 9 . ? -6.943 21.674 31.124 1.00 22.41 ? 907 HOH A O 1 HETATM 7187 O O . HOH Q 9 . ? 18.060 14.790 -2.226 1.00 36.31 ? 908 HOH A O 1 HETATM 7188 O O . HOH Q 9 . ? 18.857 7.664 46.466 0.30 18.52 ? 909 HOH A O 1 HETATM 7189 O O . HOH Q 9 . ? -5.706 13.174 -2.135 1.00 24.02 ? 910 HOH A O 1 HETATM 7190 O O . HOH Q 9 . ? 20.285 5.317 4.549 1.00 31.48 ? 911 HOH A O 1 HETATM 7191 O O . HOH Q 9 . ? 4.652 -4.448 41.065 1.00 29.75 ? 912 HOH A O 1 HETATM 7192 O O . HOH Q 9 . ? -7.798 24.784 8.184 1.00 20.17 ? 913 HOH A O 1 HETATM 7193 O O . HOH Q 9 . ? 27.422 6.290 35.877 1.00 40.33 ? 914 HOH A O 1 HETATM 7194 O O . HOH Q 9 . ? -15.129 19.934 37.561 1.00 26.46 ? 915 HOH A O 1 HETATM 7195 O O . HOH Q 9 . ? 6.536 -9.173 15.294 1.00 34.66 ? 916 HOH A O 1 HETATM 7196 O O . HOH Q 9 . ? -9.770 19.238 47.777 1.00 30.91 ? 917 HOH A O 1 HETATM 7197 O O . HOH Q 9 . ? -23.145 27.253 15.861 1.00 41.17 ? 918 HOH A O 1 HETATM 7198 O O . HOH Q 9 . ? 5.996 17.348 47.868 1.00 36.46 ? 919 HOH A O 1 HETATM 7199 O O . HOH Q 9 . ? 28.299 11.269 13.533 1.00 35.11 ? 920 HOH A O 1 HETATM 7200 O O . HOH Q 9 . ? 7.415 -5.557 14.241 1.00 33.33 ? 921 HOH A O 1 HETATM 7201 O O . HOH Q 9 . ? 9.969 30.983 0.733 1.00 35.48 ? 922 HOH A O 1 HETATM 7202 O O . HOH Q 9 . ? 1.326 12.369 48.243 1.00 26.33 ? 923 HOH A O 1 HETATM 7203 O O . HOH Q 9 . ? 10.825 28.230 12.449 1.00 26.07 ? 924 HOH A O 1 HETATM 7204 O O . HOH Q 9 . ? 1.786 18.744 2.526 1.00 35.03 ? 925 HOH A O 1 HETATM 7205 O O . HOH Q 9 . ? 5.608 13.093 46.470 1.00 42.97 ? 926 HOH A O 1 HETATM 7206 O O . HOH Q 9 . ? 25.603 29.241 12.618 1.00 42.51 ? 927 HOH A O 1 HETATM 7207 O O . HOH Q 9 . ? -15.688 15.394 15.331 1.00 18.02 ? 928 HOH A O 1 HETATM 7208 O O . HOH Q 9 . ? 14.594 29.623 35.010 1.00 25.04 ? 929 HOH A O 1 HETATM 7209 O O . HOH Q 9 . ? 15.962 27.687 38.518 1.00 24.85 ? 930 HOH A O 1 HETATM 7210 O O . HOH Q 9 . ? 4.447 -7.037 22.668 1.00 31.46 ? 931 HOH A O 1 HETATM 7211 O O . HOH Q 9 . ? 18.404 -4.222 26.101 1.00 26.93 ? 932 HOH A O 1 HETATM 7212 O O . HOH Q 9 . ? 20.963 24.476 31.516 1.00 17.36 ? 933 HOH A O 1 HETATM 7213 O O . HOH Q 9 . ? 5.517 1.880 44.493 1.00 30.38 ? 934 HOH A O 1 HETATM 7214 O O . HOH Q 9 . ? 19.399 2.336 42.874 1.00 33.54 ? 935 HOH A O 1 HETATM 7215 O O . HOH Q 9 . ? 10.448 -1.827 38.962 1.00 45.03 ? 936 HOH A O 1 HETATM 7216 O O . HOH Q 9 . ? -0.194 28.176 33.986 1.00 26.34 ? 937 HOH A O 1 HETATM 7217 O O . HOH Q 9 . ? 11.139 33.615 24.464 1.00 30.71 ? 938 HOH A O 1 HETATM 7218 O O . HOH Q 9 . ? -15.225 6.306 26.143 1.00 21.93 ? 939 HOH A O 1 HETATM 7219 O O . HOH Q 9 . ? 23.142 10.733 41.194 1.00 44.87 ? 940 HOH A O 1 HETATM 7220 O O . HOH Q 9 . ? -15.582 20.163 34.394 1.00 19.77 ? 941 HOH A O 1 HETATM 7221 O O . HOH Q 9 . ? 15.998 32.529 27.840 1.00 49.29 ? 942 HOH A O 1 HETATM 7222 O O . HOH Q 9 . ? 11.873 -1.576 7.815 1.00 35.86 ? 943 HOH A O 1 HETATM 7223 O O . HOH Q 9 . ? 16.702 35.512 8.301 1.00 41.64 ? 944 HOH A O 1 HETATM 7224 O O . HOH Q 9 . ? -22.913 24.088 9.397 1.00 28.15 ? 945 HOH A O 1 HETATM 7225 O O . HOH Q 9 . ? -19.903 19.457 13.251 1.00 29.97 ? 946 HOH A O 1 HETATM 7226 O O . HOH Q 9 . ? -14.871 10.732 33.887 1.00 44.88 ? 947 HOH A O 1 HETATM 7227 O O . HOH Q 9 . ? 12.719 31.808 7.492 1.00 31.81 ? 948 HOH A O 1 HETATM 7228 O O . HOH Q 9 . ? 26.168 -1.236 37.556 1.00 40.75 ? 949 HOH A O 1 HETATM 7229 O O . HOH Q 9 . ? 10.708 30.324 10.056 1.00 35.08 ? 950 HOH A O 1 HETATM 7230 O O . HOH Q 9 . ? 22.024 2.895 19.102 1.00 27.24 ? 951 HOH A O 1 HETATM 7231 O O . HOH Q 9 . ? 13.099 -0.054 47.579 1.00 41.63 ? 952 HOH A O 1 HETATM 7232 O O . HOH Q 9 . ? 9.716 -3.197 37.347 1.00 41.88 ? 953 HOH A O 1 HETATM 7233 O O . HOH Q 9 . ? -22.636 27.852 19.567 1.00 46.37 ? 954 HOH A O 1 HETATM 7234 O O . HOH Q 9 . ? -8.930 0.584 37.858 1.00 38.89 ? 955 HOH A O 1 HETATM 7235 O O . HOH Q 9 . ? 24.625 -2.414 20.766 1.00 43.24 ? 956 HOH A O 1 HETATM 7236 O O . HOH Q 9 . ? -8.494 22.872 6.024 1.00 42.40 ? 957 HOH A O 1 HETATM 7237 O O . HOH Q 9 . ? -7.183 30.568 35.622 1.00 44.13 ? 958 HOH A O 1 HETATM 7238 O O . HOH Q 9 . ? -5.104 28.998 9.132 1.00 41.91 ? 959 HOH A O 1 HETATM 7239 O O . HOH Q 9 . ? -15.716 22.261 32.235 1.00 31.07 ? 960 HOH A O 1 HETATM 7240 O O . HOH Q 9 . ? 33.335 13.991 33.933 1.00 22.51 ? 961 HOH A O 1 HETATM 7241 O O . HOH Q 9 . ? 6.839 8.862 44.160 1.00 35.28 ? 962 HOH A O 1 HETATM 7242 O O . HOH Q 9 . ? 8.557 9.302 2.368 1.00 29.69 ? 963 HOH A O 1 HETATM 7243 O O . HOH Q 9 . ? 6.934 26.070 9.893 1.00 33.67 ? 964 HOH A O 1 HETATM 7244 O O . HOH Q 9 . ? 28.230 19.654 13.904 1.00 49.19 ? 965 HOH A O 1 HETATM 7245 O O . HOH Q 9 . ? -15.950 4.063 16.155 1.00 43.63 ? 966 HOH A O 1 HETATM 7246 O O . HOH Q 9 . ? 19.973 7.886 22.235 1.00 25.35 ? 967 HOH A O 1 HETATM 7247 O O . HOH Q 9 . ? 13.185 12.856 13.540 1.00 19.06 ? 968 HOH A O 1 HETATM 7248 O O . HOH Q 9 . ? 18.949 -1.207 45.054 1.00 35.47 ? 969 HOH A O 1 HETATM 7249 O O . HOH Q 9 . ? -5.687 6.453 7.087 1.00 30.94 ? 970 HOH A O 1 HETATM 7250 O O . HOH Q 9 . ? -5.147 14.159 3.075 1.00 31.58 ? 971 HOH A O 1 HETATM 7251 O O . HOH Q 9 . ? -17.129 8.133 20.110 1.00 36.25 ? 972 HOH A O 1 HETATM 7252 O O . HOH Q 9 . ? -13.931 7.538 0.532 1.00 41.84 ? 973 HOH A O 1 HETATM 7253 O O . HOH Q 9 . ? -13.609 25.331 35.452 1.00 42.94 ? 974 HOH A O 1 HETATM 7254 O O . HOH Q 9 . ? -0.825 33.419 17.082 1.00 44.14 ? 975 HOH A O 1 HETATM 7255 O O . HOH Q 9 . ? 11.873 25.284 41.728 1.00 37.79 ? 976 HOH A O 1 HETATM 7256 O O . HOH Q 9 . ? -23.445 21.464 12.717 1.00 37.26 ? 977 HOH A O 1 HETATM 7257 O O . HOH Q 9 . ? -8.993 10.685 44.741 1.00 28.44 ? 978 HOH A O 1 HETATM 7258 O O . HOH Q 9 . ? -17.591 20.873 6.640 1.00 38.33 ? 979 HOH A O 1 HETATM 7259 O O . HOH Q 9 . ? 31.143 17.551 14.895 1.00 47.48 ? 980 HOH A O 1 HETATM 7260 O O . HOH Q 9 . ? -1.148 20.761 0.128 1.00 41.20 ? 981 HOH A O 1 HETATM 7261 O O . HOH Q 9 . ? 4.656 26.179 15.864 1.00 34.98 ? 982 HOH A O 1 HETATM 7262 O O . HOH Q 9 . ? -2.101 4.728 5.663 1.00 42.38 ? 983 HOH A O 1 HETATM 7263 O O . HOH Q 9 . ? 2.672 -4.660 34.808 1.00 44.62 ? 984 HOH A O 1 HETATM 7264 O O . HOH Q 9 . ? 29.555 16.611 32.955 1.00 45.17 ? 985 HOH A O 1 HETATM 7265 O O . HOH Q 9 . ? -6.169 -2.752 27.035 1.00 44.81 ? 986 HOH A O 1 HETATM 7266 O O . HOH Q 9 . ? -4.338 27.068 26.832 1.00 33.76 ? 987 HOH A O 1 HETATM 7267 O O . HOH Q 9 . ? 27.862 16.931 7.132 1.00 54.42 ? 988 HOH A O 1 HETATM 7268 O O . HOH Q 9 . ? 18.352 14.534 43.252 1.00 36.23 ? 989 HOH A O 1 HETATM 7269 O O . HOH Q 9 . ? -3.846 33.848 18.094 1.00 44.03 ? 990 HOH A O 1 HETATM 7270 O O . HOH Q 9 . ? -3.420 4.610 7.717 1.00 32.72 ? 991 HOH A O 1 HETATM 7271 O O . HOH Q 9 . ? -17.295 21.080 30.631 1.00 35.23 ? 992 HOH A O 1 HETATM 7272 O O . HOH Q 9 . ? -23.936 24.399 13.163 1.00 39.79 ? 993 HOH A O 1 HETATM 7273 O O . HOH Q 9 . ? -6.589 13.079 46.466 0.50 33.48 ? 994 HOH A O 1 HETATM 7274 O O . HOH Q 9 . ? 23.266 5.110 5.353 1.00 38.64 ? 995 HOH A O 1 HETATM 7275 O O . HOH Q 9 . ? -20.449 19.675 22.643 1.00 45.84 ? 996 HOH A O 1 HETATM 7276 O O . HOH Q 9 . ? -7.060 17.339 41.528 1.00 37.82 ? 997 HOH A O 1 HETATM 7277 O O . HOH Q 9 . ? -0.997 26.779 26.347 1.00 42.88 ? 998 HOH A O 1 HETATM 7278 O O . HOH Q 9 . ? 26.096 3.570 16.490 1.00 29.40 ? 999 HOH A O 1 HETATM 7279 O O . HOH Q 9 . ? 29.764 12.706 31.675 1.00 29.34 ? 1000 HOH A O 1 HETATM 7280 O O . HOH Q 9 . ? 9.732 8.032 44.734 1.00 44.43 ? 1001 HOH A O 1 HETATM 7281 O O . HOH Q 9 . ? -1.969 -2.709 44.536 1.00 42.08 ? 1002 HOH A O 1 HETATM 7282 O O . HOH Q 9 . ? 10.999 33.699 26.969 1.00 45.39 ? 1003 HOH A O 1 HETATM 7283 O O . HOH Q 9 . ? 7.065 -4.310 39.607 1.00 45.02 ? 1004 HOH A O 1 HETATM 7284 O O . HOH Q 9 . ? 21.758 5.609 22.674 1.00 33.60 ? 1005 HOH A O 1 HETATM 7285 O O . HOH Q 9 . ? 28.811 12.560 34.346 1.00 29.76 ? 1006 HOH A O 1 HETATM 7286 O O . HOH Q 9 . ? 3.811 19.376 47.517 1.00 42.88 ? 1007 HOH A O 1 HETATM 7287 O O . HOH Q 9 . ? -14.617 2.261 24.282 1.00 42.40 ? 1008 HOH A O 1 HETATM 7288 O O . HOH Q 9 . ? -11.970 21.342 40.882 1.00 40.06 ? 1009 HOH A O 1 HETATM 7289 O O . HOH Q 9 . ? -6.086 32.889 19.976 1.00 28.15 ? 1010 HOH A O 1 HETATM 7290 O O . HOH Q 9 . ? -12.328 3.606 32.661 1.00 44.39 ? 1011 HOH A O 1 HETATM 7291 O O . HOH Q 9 . ? -0.632 7.494 1.454 1.00 35.42 ? 1012 HOH A O 1 HETATM 7292 O O . HOH Q 9 . ? 29.563 19.658 8.159 1.00 33.88 ? 1013 HOH A O 1 HETATM 7293 O O . HOH Q 9 . ? -6.589 15.800 46.466 0.50 32.00 ? 1014 HOH A O 1 HETATM 7294 O O . HOH Q 9 . ? -14.085 15.363 38.732 1.00 29.42 ? 1015 HOH A O 1 HETATM 7295 O O . HOH Q 9 . ? 24.701 11.677 2.156 1.00 46.32 ? 1016 HOH A O 1 HETATM 7296 O O . HOH Q 9 . ? 12.658 0.771 3.742 1.00 43.12 ? 1017 HOH A O 1 HETATM 7297 O O . HOH Q 9 . ? -17.053 23.820 0.674 1.00 41.53 ? 1018 HOH A O 1 HETATM 7298 O O . HOH Q 9 . ? 22.961 -3.742 28.414 1.00 38.67 ? 1019 HOH A O 1 HETATM 7299 O O . HOH Q 9 . ? 24.176 -0.495 16.274 1.00 48.06 ? 1020 HOH A O 1 HETATM 7300 O O . HOH Q 9 . ? -0.628 3.338 47.173 1.00 45.57 ? 1021 HOH A O 1 HETATM 7301 O O . HOH Q 9 . ? 27.006 4.341 12.192 1.00 46.49 ? 1022 HOH A O 1 HETATM 7302 O O . HOH Q 9 . ? 13.284 8.727 45.635 1.00 40.98 ? 1023 HOH A O 1 HETATM 7303 O O . HOH Q 9 . ? 6.698 33.418 25.796 1.00 41.42 ? 1024 HOH A O 1 HETATM 7304 O O . HOH Q 9 . ? -3.390 25.137 41.405 1.00 29.49 ? 1025 HOH A O 1 HETATM 7305 O O . HOH Q 9 . ? -15.016 22.503 0.982 1.00 32.11 ? 1026 HOH A O 1 HETATM 7306 O O . HOH Q 9 . ? -12.408 24.393 1.143 1.00 33.46 ? 1027 HOH A O 1 HETATM 7307 O O . HOH Q 9 . ? 22.087 26.243 4.780 1.00 40.05 ? 1028 HOH A O 1 HETATM 7308 O O . HOH Q 9 . ? -13.867 24.364 37.840 1.00 43.01 ? 1029 HOH A O 1 HETATM 7309 O O . HOH Q 9 . ? 14.581 7.102 48.868 1.00 43.11 ? 1030 HOH A O 1 HETATM 7310 O O . HOH Q 9 . ? -15.241 17.950 39.601 1.00 44.94 ? 1031 HOH A O 1 HETATM 7311 O O . HOH Q 9 . ? -0.785 8.000 47.096 1.00 32.34 ? 1032 HOH A O 1 HETATM 7312 O O . HOH Q 9 . ? -17.601 18.471 13.537 1.00 48.83 ? 1033 HOH A O 1 HETATM 7313 O O . HOH Q 9 . ? -3.175 28.630 37.519 1.00 34.54 ? 1034 HOH A O 1 HETATM 7314 O O . HOH Q 9 . ? -14.447 8.264 8.344 1.00 40.21 ? 1035 HOH A O 1 HETATM 7315 O O . HOH Q 9 . ? 1.947 8.472 -0.196 1.00 34.60 ? 1036 HOH A O 1 HETATM 7316 O O . HOH Q 9 . ? 18.294 4.826 2.842 1.00 44.39 ? 1037 HOH A O 1 HETATM 7317 O O . HOH Q 9 . ? 25.034 3.733 33.017 1.00 27.67 ? 1038 HOH A O 1 HETATM 7318 O O . HOH Q 9 . ? 28.493 21.032 21.137 1.00 46.87 ? 1039 HOH A O 1 HETATM 7319 O O . HOH Q 9 . ? -17.553 27.624 20.802 1.00 40.66 ? 1040 HOH A O 1 HETATM 7320 O O . HOH Q 9 . ? 14.524 29.676 37.694 1.00 38.75 ? 1041 HOH A O 1 HETATM 7321 O O . HOH Q 9 . ? 25.199 3.434 37.102 1.00 37.10 ? 1042 HOH A O 1 HETATM 7322 O O . HOH Q 9 . ? -17.233 14.485 11.292 1.00 35.41 ? 1043 HOH A O 1 HETATM 7323 O O . HOH Q 9 . ? 11.159 -3.548 53.554 1.00 41.74 ? 1044 HOH A O 1 HETATM 7324 O O . HOH Q 9 . ? 29.095 11.235 16.081 1.00 35.65 ? 1045 HOH A O 1 HETATM 7325 O O . HOH Q 9 . ? 24.635 1.600 18.214 1.00 42.35 ? 1046 HOH A O 1 HETATM 7326 O O . HOH Q 9 . ? -7.483 -1.791 10.067 1.00 35.79 ? 1047 HOH A O 1 HETATM 7327 O O . HOH Q 9 . ? -0.818 32.873 14.621 1.00 51.30 ? 1048 HOH A O 1 HETATM 7328 O O . HOH Q 9 . ? -16.730 26.145 -0.316 1.00 43.05 ? 1049 HOH A O 1 HETATM 7329 O O . HOH Q 9 . ? -16.831 4.014 25.894 1.00 46.04 ? 1050 HOH A O 1 HETATM 7330 O O . HOH Q 9 . ? 19.145 21.695 41.471 1.00 36.29 ? 1051 HOH A O 1 HETATM 7331 O O . HOH Q 9 . ? 31.224 14.889 35.147 1.00 39.81 ? 1052 HOH A O 1 HETATM 7332 O O . HOH Q 9 . ? 12.142 29.814 34.064 1.00 35.82 ? 1053 HOH A O 1 HETATM 7333 O O . HOH Q 9 . ? -7.044 35.111 12.784 1.00 41.57 ? 1054 HOH A O 1 HETATM 7334 O O . HOH Q 9 . ? -6.919 27.067 6.596 1.00 54.07 ? 1055 HOH A O 1 HETATM 7335 O O . HOH Q 9 . ? -4.307 36.211 17.160 1.00 43.10 ? 1056 HOH A O 1 HETATM 7336 O O . HOH Q 9 . ? 30.478 21.669 6.086 1.00 36.55 ? 1057 HOH A O 1 HETATM 7337 O O . HOH Q 9 . ? -11.282 40.693 20.339 1.00 40.63 ? 1058 HOH A O 1 HETATM 7338 O O . HOH Q 9 . ? -11.969 -4.160 23.524 1.00 46.13 ? 1059 HOH A O 1 HETATM 7339 O O . HOH Q 9 . ? 18.857 13.537 46.466 0.50 31.45 ? 1060 HOH A O 1 HETATM 7340 O O . HOH Q 9 . ? 28.202 14.539 6.481 1.00 46.95 ? 1061 HOH A O 1 HETATM 7341 O O . HOH Q 9 . ? 23.740 2.888 23.774 1.00 47.28 ? 1062 HOH A O 1 HETATM 7342 O O . HOH Q 9 . ? 25.446 21.029 0.000 0.50 33.65 ? 1063 HOH A O 1 HETATM 7343 O O . HOH Q 9 . ? 18.417 -1.448 9.859 1.00 46.85 ? 1064 HOH A O 1 HETATM 7344 O O . HOH Q 9 . ? 26.507 -0.263 30.837 1.00 45.82 ? 1065 HOH A O 1 HETATM 7345 O O . HOH Q 9 . ? -12.106 12.174 40.879 1.00 32.82 ? 1066 HOH A O 1 HETATM 7346 O O . HOH Q 9 . ? 25.227 -7.534 40.205 1.00 49.08 ? 1067 HOH A O 1 HETATM 7347 O O . HOH Q 9 . ? -16.210 8.575 27.329 1.00 23.50 ? 1068 HOH A O 1 HETATM 7348 O O . HOH Q 9 . ? 26.668 7.821 7.934 1.00 51.98 ? 1069 HOH A O 1 HETATM 7349 O O . HOH Q 9 . ? 0.175 9.681 48.881 1.00 33.54 ? 1070 HOH A O 1 HETATM 7350 O O . HOH Q 9 . ? 19.288 21.827 -3.320 1.00 47.48 ? 1071 HOH A O 1 HETATM 7351 O O . HOH Q 9 . ? -6.501 32.969 9.656 1.00 43.59 ? 1072 HOH A O 1 HETATM 7352 O O . HOH Q 9 . ? 4.184 12.035 48.107 1.00 39.78 ? 1073 HOH A O 1 HETATM 7353 O O . HOH Q 9 . ? 27.114 -2.428 31.749 1.00 42.74 ? 1074 HOH A O 1 HETATM 7354 O O . HOH Q 9 . ? -19.679 29.321 21.703 1.00 41.90 ? 1075 HOH A O 1 HETATM 7355 O O . HOH Q 9 . ? 2.697 -8.043 24.163 1.00 38.01 ? 1076 HOH A O 1 HETATM 7356 O O . HOH Q 9 . ? -19.156 18.509 8.382 1.00 49.80 ? 1077 HOH A O 1 HETATM 7357 O O . HOH Q 9 . ? -11.504 6.274 43.143 1.00 40.58 ? 1078 HOH A O 1 HETATM 7358 O O . HOH Q 9 . ? -17.037 20.815 36.790 1.00 41.14 ? 1079 HOH A O 1 HETATM 7359 O O . HOH Q 9 . ? 14.499 30.617 30.372 1.00 32.06 ? 1080 HOH A O 1 HETATM 7360 O O . HOH Q 9 . ? 27.067 3.679 25.120 1.00 41.80 ? 1081 HOH A O 1 HETATM 7361 O O . HOH Q 9 . ? -15.021 13.235 37.622 1.00 35.89 ? 1082 HOH A O 1 HETATM 7362 O O . HOH Q 9 . ? -6.035 -5.471 12.014 1.00 37.71 ? 1083 HOH A O 1 HETATM 7363 O O . HOH Q 9 . ? 20.147 27.442 3.381 1.00 34.79 ? 1084 HOH A O 1 HETATM 7364 O O . HOH Q 9 . ? 29.317 24.342 6.987 1.00 35.16 ? 1085 HOH A O 1 HETATM 7365 O O . HOH Q 9 . ? 16.793 31.230 29.414 1.00 39.16 ? 1086 HOH A O 1 HETATM 7366 O O . HOH Q 9 . ? -14.270 38.567 14.112 1.00 39.03 ? 1087 HOH A O 1 HETATM 7367 O O . HOH Q 9 . ? 23.282 39.240 19.986 1.00 43.36 ? 1088 HOH A O 1 HETATM 7368 O O . HOH Q 9 . ? -10.838 32.419 24.743 1.00 41.07 ? 1089 HOH A O 1 HETATM 7369 O O . HOH Q 9 . ? 23.373 23.003 32.097 1.00 23.95 ? 1090 HOH A O 1 HETATM 7370 O O . HOH Q 9 . ? -16.821 12.314 10.907 1.00 43.76 ? 1091 HOH A O 1 HETATM 7371 O O . HOH Q 9 . ? -9.698 36.426 9.457 1.00 42.18 ? 1092 HOH A O 1 HETATM 7372 O O . HOH Q 9 . ? -4.219 19.985 42.789 1.00 43.20 ? 1093 HOH A O 1 HETATM 7373 O O . HOH Q 9 . ? -19.113 16.686 6.144 1.00 46.01 ? 1094 HOH A O 1 HETATM 7374 O O . HOH Q 9 . ? -12.465 37.116 8.856 1.00 41.79 ? 1095 HOH A O 1 HETATM 7375 O O . HOH Q 9 . ? -13.270 37.368 6.192 1.00 45.17 ? 1096 HOH A O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . LEU A 12 ? 0.3604 0.3496 0.4426 0.0325 0.0819 -0.0796 20 LEU A N 2 C CA . LEU A 12 ? 0.3380 0.3082 0.3806 0.0181 0.0267 -0.0628 20 LEU A CA 3 C C . LEU A 12 ? 0.3119 0.2032 0.3136 0.0006 -0.0126 -0.0410 20 LEU A C 4 O O . LEU A 12 ? 0.3700 0.2591 0.3183 -0.0638 -0.0114 -0.0369 20 LEU A O 5 C CB . LEU A 12 ? 0.4059 0.4050 0.4095 -0.0095 0.0240 -0.0413 20 LEU A CB 6 C CG . LEU A 12 ? 0.4462 0.4061 0.4124 0.0055 -0.0080 -0.0428 20 LEU A CG 7 C CD1 . LEU A 12 ? 0.4459 0.4458 0.4095 0.0013 -0.0307 -0.0189 20 LEU A CD1 8 C CD2 . LEU A 12 ? 0.4909 0.4297 0.4151 -0.0043 -0.0008 -0.0653 20 LEU A CD2 19 N N . GLY A 13 ? 0.2608 0.1667 0.2786 0.0512 -0.0087 -0.0339 21 GLY A N 20 C CA . GLY A 13 ? 0.2497 0.1589 0.2828 0.0481 0.0269 -0.0031 21 GLY A CA 21 C C . GLY A 13 ? 0.1976 0.1293 0.2492 0.0017 0.0019 -0.0274 21 GLY A C 22 O O . GLY A 13 ? 0.1757 0.1525 0.2252 0.0100 -0.0073 -0.0244 21 GLY A O 26 N N . ARG A 14 ? 0.1901 0.1359 0.2639 0.0002 0.0201 0.0001 22 ARG A N 27 C CA . ARG A 14 ? 0.2134 0.1190 0.2281 0.0121 -0.0010 -0.0184 22 ARG A CA 28 C C . ARG A 14 ? 0.1920 0.1509 0.2177 0.0345 0.0073 0.0040 22 ARG A C 29 O O . ARG A 14 ? 0.2097 0.1531 0.2426 0.0148 0.0266 0.0032 22 ARG A O 30 C CB . ARG A 14 ? 0.2223 0.1548 0.2268 0.0304 0.0173 -0.0149 22 ARG A CB 31 C CG . ARG A 14 ? 0.2501 0.2444 0.2513 0.0047 0.0077 -0.0358 22 ARG A CG 32 C CD . ARG A 14 ? 0.3026 0.3113 0.2677 0.0203 0.0111 -0.0691 22 ARG A CD 33 N NE . ARG A 14 ? 0.4010 0.3630 0.2751 0.0202 0.0169 -0.0670 22 ARG A NE 34 C CZ . ARG A 14 ? 0.4815 0.3883 0.3067 0.0571 0.0542 -0.0627 22 ARG A CZ 35 N NH1 . ARG A 14 ? 0.4989 0.3672 0.3222 0.0800 0.0590 -0.0765 22 ARG A NH1 36 N NH2 . ARG A 14 ? 0.5068 0.4331 0.3203 0.0487 0.0689 -0.0567 22 ARG A NH2 50 N N . PHE A 15 ? 0.1553 0.1735 0.1874 0.0260 0.0001 -0.0168 23 PHE A N 51 C CA . PHE A 15 ? 0.1696 0.1587 0.1868 0.0246 0.0118 -0.0019 23 PHE A CA 52 C C . PHE A 15 ? 0.1525 0.1572 0.1629 -0.0246 0.0213 0.0157 23 PHE A C 53 O O . PHE A 15 ? 0.1429 0.1683 0.1821 0.0047 0.0020 0.0144 23 PHE A O 54 C CB . PHE A 15 ? 0.1699 0.1635 0.1833 0.0103 0.0062 0.0037 23 PHE A CB 55 C CG . PHE A 15 ? 0.1684 0.1687 0.1740 0.0138 0.0137 0.0152 23 PHE A CG 56 C CD1 . PHE A 15 ? 0.1904 0.1806 0.1578 0.0076 0.0160 0.0109 23 PHE A CD1 57 C CD2 . PHE A 15 ? 0.1751 0.2007 0.1522 0.0196 0.0073 0.0006 23 PHE A CD2 58 C CE1 . PHE A 15 ? 0.1990 0.1802 0.1580 -0.0027 0.0394 -0.0151 23 PHE A CE1 59 C CE2 . PHE A 15 ? 0.1843 0.1837 0.1647 0.0187 0.0056 -0.0127 23 PHE A CE2 60 C CZ . PHE A 15 ? 0.1904 0.1786 0.1639 -0.0014 0.0108 -0.0212 23 PHE A CZ 70 N N . TRP A 16 ? 0.1352 0.1788 0.1543 -0.0126 0.0173 -0.0129 24 TRP A N 71 C CA . TRP A 16 ? 0.1660 0.1338 0.1576 0.0112 -0.0070 -0.0037 24 TRP A CA 72 C C . TRP A 16 ? 0.1482 0.1379 0.1500 0.0002 0.0209 -0.0319 24 TRP A C 73 O O . TRP A 16 ? 0.1865 0.1572 0.1560 -0.0007 0.0021 -0.0010 24 TRP A O 74 C CB . TRP A 16 ? 0.1511 0.1312 0.1751 0.0007 0.0144 -0.0070 24 TRP A CB 75 C CG . TRP A 16 ? 0.1445 0.1382 0.1728 -0.0150 0.0030 -0.0053 24 TRP A CG 76 C CD1 . TRP A 16 ? 0.1599 0.1512 0.1889 -0.0172 0.0085 0.0078 24 TRP A CD1 77 C CD2 . TRP A 16 ? 0.1447 0.1453 0.1810 -0.0024 0.0086 -0.0203 24 TRP A CD2 78 N NE1 . TRP A 16 ? 0.1694 0.1510 0.1842 -0.0356 -0.0162 -0.0058 24 TRP A NE1 79 C CE2 . TRP A 16 ? 0.1642 0.1407 0.1779 -0.0158 0.0015 -0.0175 24 TRP A CE2 80 C CE3 . TRP A 16 ? 0.1347 0.1379 0.1813 -0.0070 -0.0049 -0.0118 24 TRP A CE3 81 C CZ2 . TRP A 16 ? 0.1756 0.1903 0.1787 -0.0324 -0.0099 -0.0122 24 TRP A CZ2 82 C CZ3 . TRP A 16 ? 0.1548 0.1791 0.1723 -0.0160 -0.0345 -0.0039 24 TRP A CZ3 83 C CH2 . TRP A 16 ? 0.1850 0.2128 0.1810 -0.0235 -0.0179 -0.0156 24 TRP A CH2 94 N N . HIS A 17 ? 0.1492 0.1442 0.1358 -0.0099 0.0214 -0.0337 25 HIS A N 95 C CA . HIS A 17 ? 0.1093 0.1483 0.1522 -0.0059 0.0199 0.0025 25 HIS A CA 96 C C . HIS A 17 ? 0.1301 0.1535 0.1644 -0.0154 0.0068 -0.0133 25 HIS A C 97 O O . HIS A 17 ? 0.1562 0.1465 0.1694 0.0029 -0.0001 0.0028 25 HIS A O 98 C CB . HIS A 17 ? 0.1323 0.1438 0.1584 -0.0001 0.0196 0.0043 25 HIS A CB 99 C CG . HIS A 17 ? 0.1161 0.1454 0.1529 -0.0171 0.0032 -0.0126 25 HIS A CG 100 N ND1 . HIS A 17 ? 0.1208 0.1480 0.1525 0.0017 -0.0055 0.0069 25 HIS A ND1 101 C CD2 . HIS A 17 ? 0.1248 0.1616 0.1694 -0.0170 0.0048 0.0000 25 HIS A CD2 102 C CE1 . HIS A 17 ? 0.1285 0.1331 0.1634 -0.0205 -0.0109 -0.0073 25 HIS A CE1 103 N NE2 . HIS A 17 ? 0.1294 0.1417 0.1700 -0.0291 -0.0254 -0.0023 25 HIS A NE2 111 N N . ILE A 18 ? 0.1344 0.1639 0.1581 0.0049 -0.0100 -0.0180 26 ILE A N 112 C CA . ILE A 18 ? 0.1328 0.1839 0.1710 0.0146 0.0079 -0.0302 26 ILE A CA 113 C C . ILE A 18 ? 0.1112 0.1639 0.1621 0.0029 0.0088 -0.0125 26 ILE A C 114 O O . ILE A 18 ? 0.1204 0.1613 0.1470 0.0031 0.0038 -0.0003 26 ILE A O 115 C CB . ILE A 18 ? 0.1346 0.1960 0.1893 -0.0126 -0.0001 -0.0179 26 ILE A CB 116 C CG1 . ILE A 18 ? 0.1240 0.2338 0.2146 -0.0203 0.0162 -0.0107 26 ILE A CG1 117 C CG2 . ILE A 18 ? 0.1655 0.2049 0.2004 0.0026 -0.0131 -0.0283 26 ILE A CG2 118 C CD1 . ILE A 18 ? 0.1425 0.2286 0.2368 -0.0150 -0.0010 -0.0380 26 ILE A CD1 130 N N . SER A 19 ? 0.1159 0.1605 0.1406 0.0052 -0.0006 -0.0059 27 SER A N 131 C CA . SER A 19 ? 0.1472 0.1430 0.1453 -0.0099 0.0220 -0.0134 27 SER A CA 132 C C . SER A 19 ? 0.1183 0.1523 0.1534 0.0058 0.0059 -0.0259 27 SER A C 133 O O . SER A 19 ? 0.1225 0.1699 0.1398 0.0008 0.0083 -0.0104 27 SER A O 134 C CB . SER A 19 ? 0.0964 0.1776 0.1543 -0.0142 0.0077 -0.0021 27 SER A CB 135 O OG . SER A 19 ? 0.1233 0.1898 0.1817 0.0000 -0.0104 -0.0183 27 SER A OG 141 N N . ASP A 20 ? 0.1056 0.1591 0.1367 -0.0012 -0.0002 -0.0119 28 ASP A N 142 C CA . ASP A 20 ? 0.1004 0.1747 0.1474 -0.0071 0.0145 0.0122 28 ASP A CA 143 C C . ASP A 20 ? 0.1220 0.1606 0.1333 0.0011 0.0026 0.0160 28 ASP A C 144 O O . ASP A 20 ? 0.1085 0.1831 0.1475 -0.0003 0.0031 0.0182 28 ASP A O 145 C CB . ASP A 20 ? 0.0998 0.1753 0.1317 0.0193 0.0049 -0.0174 28 ASP A CB 146 C CG . ASP A 20 ? 0.1006 0.1291 0.1592 0.0200 0.0059 -0.0026 28 ASP A CG 147 O OD1 . ASP A 20 ? 0.1390 0.1491 0.1479 0.0268 0.0100 -0.0143 28 ASP A OD1 148 O OD2 . ASP A 20 ? 0.1013 0.1558 0.1578 0.0039 -0.0009 -0.0067 28 ASP A OD2 153 N N . LEU A 21 ? 0.1077 0.1518 0.1537 -0.0126 0.0066 0.0130 29 LEU A N 154 C CA . LEU A 21 ? 0.0900 0.1859 0.1542 0.0044 0.0023 -0.0019 29 LEU A CA 155 C C . LEU A 21 ? 0.0889 0.1731 0.1473 -0.0187 0.0060 -0.0015 29 LEU A C 156 O O . LEU A 21 ? 0.1056 0.2004 0.1413 0.0006 -0.0126 0.0067 29 LEU A O 157 C CB . LEU A 21 ? 0.1129 0.1871 0.1914 -0.0038 -0.0120 0.0101 29 LEU A CB 158 C CG . LEU A 21 ? 0.1106 0.1713 0.2374 -0.0124 -0.0113 -0.0009 29 LEU A CG 159 C CD1 . LEU A 21 ? 0.1720 0.1666 0.1984 -0.0091 -0.0126 -0.0021 29 LEU A CD1 160 C CD2 . LEU A 21 ? 0.1558 0.1984 0.2783 -0.0307 0.0103 -0.0011 29 LEU A CD2 172 N N . HIS A 22 ? 0.1054 0.1814 0.1320 -0.0069 0.0052 0.0034 30 HIS A N 173 C CA . HIS A 22 ? 0.1002 0.1723 0.1438 -0.0014 -0.0055 -0.0126 30 HIS A CA 174 C C . HIS A 22 ? 0.1158 0.1655 0.1461 0.0001 0.0199 -0.0164 30 HIS A C 175 O O . HIS A 22 ? 0.1116 0.1932 0.1636 -0.0027 0.0088 0.0013 30 HIS A O 176 C CB . HIS A 22 ? 0.1085 0.1811 0.1505 -0.0069 0.0031 -0.0030 30 HIS A CB 177 C CG . HIS A 22 ? 0.1125 0.1459 0.1413 0.0084 0.0104 -0.0085 30 HIS A CG 178 N ND1 . HIS A 22 ? 0.1089 0.1679 0.1449 0.0073 0.0084 -0.0082 30 HIS A ND1 179 C CD2 . HIS A 22 ? 0.1019 0.1611 0.1240 0.0081 0.0011 -0.0063 30 HIS A CD2 180 C CE1 . HIS A 22 ? 0.0735 0.1735 0.1348 0.0083 0.0042 -0.0185 30 HIS A CE1 181 N NE2 . HIS A 22 ? 0.1056 0.1755 0.1293 0.0112 0.0043 0.0026 30 HIS A NE2 189 N N . LEU A 23 ? 0.0967 0.1919 0.1372 -0.0095 0.0047 0.0036 31 LEU A N 190 C CA . LEU A 23 ? 0.1237 0.1720 0.1453 -0.0179 -0.0081 -0.0147 31 LEU A CA 191 C C . LEU A 23 ? 0.1070 0.2020 0.1592 -0.0216 0.0052 -0.0472 31 LEU A C 192 O O . LEU A 23 ? 0.1159 0.2126 0.1782 0.0042 0.0036 -0.0395 31 LEU A O 193 C CB . LEU A 23 ? 0.1111 0.1999 0.1555 -0.0079 0.0070 -0.0017 31 LEU A CB 194 C CG . LEU A 23 ? 0.1033 0.2345 0.1476 -0.0308 -0.0019 0.0196 31 LEU A CG 195 C CD1 . LEU A 23 ? 0.1291 0.2364 0.1525 -0.0488 -0.0143 0.0239 31 LEU A CD1 196 C CD2 . LEU A 23 ? 0.1317 0.2488 0.1566 -0.0155 0.0031 0.0036 31 LEU A CD2 208 N N . ASP A 24 ? 0.0941 0.1979 0.1720 0.0145 -0.0073 -0.0191 32 ASP A N 209 C CA . ASP A 24 ? 0.1091 0.2076 0.1881 -0.0086 0.0201 -0.0296 32 ASP A CA 210 C C . ASP A 24 ? 0.0960 0.1966 0.1866 -0.0016 -0.0103 -0.0153 32 ASP A C 211 O O . ASP A 24 ? 0.1177 0.1913 0.1894 0.0025 -0.0003 -0.0151 32 ASP A O 212 C CB . ASP A 24 ? 0.1095 0.2246 0.2119 -0.0152 0.0184 -0.0277 32 ASP A CB 213 C CG . ASP A 24 ? 0.1007 0.2016 0.2243 -0.0289 0.0199 -0.0047 32 ASP A CG 214 O OD1 . ASP A 24 ? 0.1236 0.2088 0.2574 0.0041 0.0173 -0.0112 32 ASP A OD1 215 O OD2 . ASP A 24 ? 0.1339 0.1959 0.2196 -0.0163 0.0036 0.0020 32 ASP A OD2 220 N N . PRO A 25 ? 0.1141 0.2393 0.1842 -0.0315 0.0026 -0.0138 33 PRO A N 221 C CA . PRO A 25 ? 0.1338 0.2473 0.2068 -0.0259 -0.0023 -0.0001 33 PRO A CA 222 C C . PRO A 25 ? 0.1071 0.2179 0.2140 -0.0198 0.0002 -0.0117 33 PRO A C 223 O O . PRO A 25 ? 0.1061 0.2552 0.2729 -0.0195 0.0003 0.0036 33 PRO A O 224 C CB . PRO A 25 ? 0.1686 0.2888 0.2147 -0.0171 0.0170 0.0003 33 PRO A CB 225 C CG . PRO A 25 ? 0.1660 0.3725 0.2019 -0.0356 0.0412 -0.0066 33 PRO A CG 226 C CD . PRO A 25 ? 0.1331 0.2776 0.1870 -0.0202 0.0264 -0.0270 33 PRO A CD 234 N N . ASN A 26 ? 0.1029 0.2053 0.2208 -0.0012 0.0048 -0.0054 34 ASN A N 235 C CA . ASN A 26 ? 0.1183 0.2531 0.2487 0.0080 0.0056 -0.0292 34 ASN A CA 236 C C . ASN A 26 ? 0.1219 0.2492 0.2408 -0.0026 -0.0077 -0.0069 34 ASN A C 237 O O . ASN A 26 ? 0.1707 0.2536 0.2592 0.0478 -0.0002 0.0108 34 ASN A O 238 C CB . ASN A 26 ? 0.1598 0.2829 0.2748 0.0233 0.0182 -0.0689 34 ASN A CB 239 C CG . ASN A 26 ? 0.1422 0.3265 0.2874 0.0115 0.0171 -0.0873 34 ASN A CG 240 O OD1 . ASN A 26 ? 0.2230 0.3876 0.2842 -0.0154 0.0502 -0.0877 34 ASN A OD1 241 N ND2 . ASN A 26 ? 0.1772 0.3635 0.2865 0.0041 -0.0155 -0.1098 34 ASN A ND2 247 N N . TYR A 27 ? 0.1459 0.2150 0.2147 -0.0031 -0.0098 -0.0096 35 TYR A N 248 C CA . TYR A 27 ? 0.1240 0.2245 0.2149 0.0133 -0.0200 -0.0060 35 TYR A CA 249 C C . TYR A 27 ? 0.1303 0.2356 0.2420 0.0053 -0.0254 -0.0241 35 TYR A C 250 O O . TYR A 27 ? 0.1659 0.2279 0.2551 -0.0189 -0.0331 -0.0281 35 TYR A O 251 C CB . TYR A 27 ? 0.1622 0.2087 0.1937 0.0285 -0.0204 -0.0059 35 TYR A CB 252 C CG . TYR A 27 ? 0.1224 0.2361 0.2105 0.0236 -0.0205 -0.0080 35 TYR A CG 253 C CD1 . TYR A 27 ? 0.1500 0.2220 0.1971 0.0077 -0.0299 -0.0080 35 TYR A CD1 254 C CD2 . TYR A 27 ? 0.1716 0.2545 0.2107 -0.0212 -0.0099 -0.0298 35 TYR A CD2 255 C CE1 . TYR A 27 ? 0.1603 0.2286 0.1981 0.0253 -0.0345 -0.0201 35 TYR A CE1 256 C CE2 . TYR A 27 ? 0.2146 0.2291 0.1988 -0.0204 -0.0203 -0.0439 35 TYR A CE2 257 C CZ . TYR A 27 ? 0.1955 0.2089 0.1912 -0.0020 -0.0253 -0.0139 35 TYR A CZ 258 O OH . TYR A 27 ? 0.2254 0.2545 0.2014 -0.0188 -0.0285 -0.0216 35 TYR A OH 268 N N . THR A 28 ? 0.1519 0.2378 0.2491 0.0008 -0.0564 -0.0145 36 THR A N 269 C CA A THR A 28 ? 0.1830 0.2693 0.2898 -0.0104 -0.0680 0.0077 36 THR A CA 270 C CA B THR A 28 ? 0.1670 0.2976 0.2921 -0.0066 -0.0741 0.0105 36 THR A CA 271 C C . THR A 28 ? 0.1805 0.2771 0.3110 -0.0122 -0.1091 0.0273 36 THR A C 272 O O . THR A 28 ? 0.2341 0.2515 0.3145 -0.0363 -0.0897 0.0385 36 THR A O 273 C CB A THR A 28 ? 0.2122 0.2996 0.3156 -0.0188 -0.0384 0.0160 36 THR A CB 274 C CB B THR A 28 ? 0.1407 0.3802 0.3306 -0.0014 -0.0697 0.0259 36 THR A CB 275 O OG1 A THR A 28 ? 0.2309 0.3107 0.3391 -0.0468 -0.0118 0.0124 36 THR A OG1 276 O OG1 B THR A 28 ? 0.1880 0.4258 0.3598 0.0098 -0.0159 0.0192 36 THR A OG1 277 C CG2 A THR A 28 ? 0.2268 0.3064 0.3218 -0.0204 -0.0134 0.0225 36 THR A CG2 278 C CG2 B THR A 28 ? 0.1237 0.4000 0.3582 -0.0251 -0.0650 0.0275 36 THR A CG2 291 N N . VAL A 29 ? 0.2505 0.2859 0.3322 -0.0222 -0.1284 0.0497 37 VAL A N 292 C CA . VAL A 29 ? 0.2809 0.2967 0.3826 -0.0086 -0.1160 0.0463 37 VAL A CA 293 C C . VAL A 29 ? 0.2677 0.3596 0.4486 -0.0251 -0.1312 0.0306 37 VAL A C 294 O O . VAL A 29 ? 0.3529 0.4092 0.5043 -0.0514 -0.0515 -0.0104 37 VAL A O 295 C CB . VAL A 29 ? 0.3228 0.3340 0.3614 0.0035 -0.0973 0.0313 37 VAL A CB 296 C CG1 . VAL A 29 ? 0.3671 0.3438 0.3766 0.0186 -0.0572 0.0313 37 VAL A CG1 297 C CG2 . VAL A 29 ? 0.3626 0.3618 0.3604 -0.0144 -0.0756 0.0018 37 VAL A CG2 307 N N . SER A 30 ? 0.2393 0.3778 0.4922 -0.0200 -0.1266 0.0572 38 SER A N 308 C CA . SER A 30 ? 0.2504 0.4002 0.5123 -0.0073 -0.1064 0.0780 38 SER A CA 309 C C . SER A 30 ? 0.2655 0.4322 0.5250 0.0036 -0.0767 0.0905 38 SER A C 310 O O . SER A 30 ? 0.2617 0.4342 0.5426 0.0086 -0.0513 0.0822 38 SER A O 311 C CB . SER A 30 ? 0.2590 0.4043 0.5378 0.0101 -0.0824 0.0920 38 SER A CB 312 O OG . SER A 30 ? 0.2489 0.3926 0.5529 0.0145 -0.0751 0.1077 38 SER A OG 318 N N . LYS A 31 ? 0.2590 0.4562 0.5143 0.0347 -0.0803 0.1219 39 LYS A N 319 C CA . LYS A 31 ? 0.3064 0.4635 0.5079 0.0790 -0.0589 0.1379 39 LYS A CA 320 C C . LYS A 31 ? 0.3113 0.4445 0.5107 0.0935 -0.0299 0.1366 39 LYS A C 321 O O . LYS A 31 ? 0.3590 0.4199 0.5296 0.0694 0.0022 0.1392 39 LYS A O 322 C CB . LYS A 31 ? 0.3617 0.5336 0.5082 0.0704 -0.0712 0.1218 39 LYS A CB 323 C CG . LYS A 31 ? 0.3896 0.5744 0.5103 0.0848 -0.0960 0.1133 39 LYS A CG 324 C CD . LYS A 31 ? 0.4471 0.6219 0.5169 0.0803 -0.0878 0.0993 39 LYS A CD 325 C CE . LYS A 31 ? 0.5142 0.6685 0.5335 0.0776 -0.0714 0.0693 39 LYS A CE 326 N NZ . LYS A 31 ? 0.5544 0.7031 0.5444 0.0652 -0.0493 0.0475 39 LYS A NZ 340 N N . ASP A 32 ? 0.2469 0.4281 0.5063 0.0924 -0.0410 0.1180 40 ASP A N 341 C CA . ASP A 32 ? 0.2617 0.4101 0.5117 0.0795 -0.0052 0.0848 40 ASP A CA 342 C C . ASP A 32 ? 0.2474 0.3605 0.4864 0.0729 -0.0160 0.0914 40 ASP A C 343 O O . ASP A 32 ? 0.2349 0.3187 0.4822 0.0614 -0.0192 0.0941 40 ASP A O 344 C CB . ASP A 32 ? 0.2726 0.4600 0.5542 0.1157 0.0301 0.0524 40 ASP A CB 345 C CG . ASP A 32 ? 0.3023 0.4821 0.5995 0.1610 0.0725 0.0372 40 ASP A CG 346 O OD1 . ASP A 32 ? 0.3286 0.4626 0.6196 0.1875 0.0675 0.0437 40 ASP A OD1 347 O OD2 . ASP A 32 ? 0.3461 0.5313 0.6123 0.1192 0.0928 0.0333 40 ASP A OD2 352 N N . PRO A 33 ? 0.2258 0.3117 0.4618 0.0540 -0.0173 0.1180 41 PRO A N 353 C CA . PRO A 33 ? 0.2261 0.2955 0.4544 0.0522 0.0111 0.0843 41 PRO A CA 354 C C . PRO A 33 ? 0.2183 0.2641 0.4402 0.0454 0.0175 0.0515 41 PRO A C 355 O O . PRO A 33 ? 0.2039 0.2524 0.4285 0.0373 -0.0054 0.0476 41 PRO A O 356 C CB . PRO A 33 ? 0.2529 0.3020 0.4555 0.0671 0.0099 0.0955 41 PRO A CB 357 C CG . PRO A 33 ? 0.2470 0.3573 0.4660 0.0572 0.0035 0.1037 41 PRO A CG 358 C CD . PRO A 33 ? 0.2509 0.3559 0.4657 0.0601 -0.0083 0.1159 41 PRO A CD 366 N N . LEU A 34 ? 0.2660 0.2679 0.4357 0.0780 0.0259 0.0425 42 LEU A N 367 C CA . LEU A 34 ? 0.2736 0.2423 0.4461 0.0801 0.0459 -0.0026 42 LEU A CA 368 C C . LEU A 34 ? 0.2874 0.2311 0.4397 0.0680 0.0642 -0.0037 42 LEU A C 369 O O . LEU A 34 ? 0.3258 0.2694 0.4519 0.0302 0.0900 -0.0175 42 LEU A O 370 C CB . LEU A 34 ? 0.3265 0.2476 0.4630 0.0505 0.0577 -0.0040 42 LEU A CB 371 C CG . LEU A 34 ? 0.3560 0.2779 0.4692 0.0636 0.0417 0.0212 42 LEU A CG 372 C CD1 . LEU A 34 ? 0.3889 0.2807 0.4716 0.0486 0.0527 0.0276 42 LEU A CD1 373 C CD2 . LEU A 34 ? 0.3637 0.3050 0.4806 0.0422 0.0518 0.0053 42 LEU A CD2 385 N N . GLN A 35 ? 0.2250 0.2355 0.4321 0.0637 0.0561 0.0245 43 GLN A N 386 C CA . GLN A 35 ? 0.2177 0.2657 0.4389 0.0641 0.0753 0.0217 43 GLN A CA 387 C C . GLN A 35 ? 0.1943 0.2210 0.3918 0.0284 0.0109 0.0151 43 GLN A C 388 O O . GLN A 35 ? 0.1849 0.2735 0.4016 0.0408 0.0171 0.0232 43 GLN A O 389 C CB . GLN A 35 ? 0.2640 0.3148 0.5003 0.0919 0.1048 0.0273 43 GLN A CB 390 C CG . GLN A 35 ? 0.3238 0.3940 0.5564 0.0903 0.1506 0.0121 43 GLN A CG 391 C CD . GLN A 35 ? 0.4096 0.5031 0.6029 0.0440 0.1669 -0.0050 43 GLN A CD 392 O OE1 . GLN A 35 ? 0.4577 0.5724 0.6271 0.0417 0.1614 -0.0164 43 GLN A OE1 393 N NE2 . GLN A 35 ? 0.4081 0.4923 0.6080 0.0467 0.1812 0.0086 43 GLN A NE2 402 N N . VAL A 36 ? 0.1558 0.2206 0.3291 0.0144 -0.0292 0.0096 44 VAL A N 403 C CA . VAL A 36 ? 0.1702 0.2263 0.2784 0.0188 -0.0366 0.0014 44 VAL A CA 404 C C . VAL A 36 ? 0.1374 0.2020 0.2515 -0.0063 -0.0411 -0.0154 44 VAL A C 405 O O . VAL A 36 ? 0.1429 0.2196 0.2542 -0.0058 -0.0311 -0.0135 44 VAL A O 406 C CB . VAL A 36 ? 0.1637 0.2159 0.2696 0.0203 -0.0259 -0.0041 44 VAL A CB 407 C CG1 . VAL A 36 ? 0.1799 0.2585 0.2505 0.0097 -0.0464 -0.0100 44 VAL A CG1 408 C CG2 . VAL A 36 ? 0.1945 0.2729 0.2611 0.0267 -0.0517 0.0102 44 VAL A CG2 418 N N . CYS A 37 ? 0.1400 0.2182 0.2637 0.0185 -0.0077 -0.0119 45 CYS A N 419 C CA . CYS A 37 ? 0.1424 0.2069 0.2347 0.0153 0.0027 -0.0206 45 CYS A CA 420 C C . CYS A 37 ? 0.1479 0.1822 0.2359 0.0114 -0.0071 -0.0334 45 CYS A C 421 O O . CYS A 37 ? 0.1767 0.1919 0.2546 0.0035 -0.0261 -0.0295 45 CYS A O 422 C CB . CYS A 37 ? 0.1576 0.1702 0.2234 -0.0046 0.0017 -0.0080 45 CYS A CB 423 S SG . CYS A 37 ? 0.1474 0.2052 0.2468 0.0154 -0.0209 -0.0287 45 CYS A SG 428 N N . PRO A 38 ? 0.1344 0.2124 0.2345 0.0103 -0.0010 -0.0286 46 PRO A N 429 C CA . PRO A 38 ? 0.1354 0.2065 0.2400 0.0136 0.0010 -0.0513 46 PRO A CA 430 C C . PRO A 38 ? 0.1577 0.2049 0.2446 0.0051 0.0111 -0.0629 46 PRO A C 431 O O . PRO A 38 ? 0.1497 0.2212 0.2578 0.0181 0.0103 -0.0506 46 PRO A O 432 C CB . PRO A 38 ? 0.1684 0.2500 0.2440 -0.0010 0.0189 -0.0584 46 PRO A CB 433 C CG . PRO A 38 ? 0.2084 0.2641 0.2578 0.0062 0.0203 -0.0226 46 PRO A CG 434 C CD . PRO A 38 ? 0.1601 0.2262 0.2377 -0.0151 0.0254 -0.0520 46 PRO A CD 442 N N . SER A 39 ? 0.1237 0.2043 0.2307 0.0158 0.0059 -0.0529 47 SER A N 443 C CA . SER A 39 ? 0.1287 0.1997 0.2049 0.0120 -0.0147 -0.0416 47 SER A CA 444 C C . SER A 39 ? 0.1209 0.1999 0.2201 0.0262 -0.0163 -0.0441 47 SER A C 445 O O . SER A 39 ? 0.1346 0.2123 0.2361 0.0260 -0.0125 -0.0354 47 SER A O 446 C CB . SER A 39 ? 0.1259 0.2127 0.2024 0.0168 -0.0137 -0.0413 47 SER A CB 447 O OG . SER A 39 ? 0.1311 0.2008 0.2124 0.0242 -0.0010 -0.0459 47 SER A OG 453 N N . ALA A 40 ? 0.1319 0.2008 0.2314 0.0025 -0.0037 -0.0290 48 ALA A N 454 C CA . ALA A 40 ? 0.1342 0.1703 0.2588 0.0098 -0.0029 -0.0237 48 ALA A CA 455 C C . ALA A 40 ? 0.1446 0.1841 0.2866 0.0186 0.0111 -0.0294 48 ALA A C 456 O O . ALA A 40 ? 0.1614 0.1936 0.2890 0.0013 0.0184 -0.0323 48 ALA A O 457 C CB . ALA A 40 ? 0.1687 0.1819 0.2599 0.0053 0.0007 -0.0228 48 ALA A CB 463 N N . GLY A 41 ? 0.1723 0.1924 0.2904 0.0034 0.0158 -0.0534 49 GLY A N 464 C CA . GLY A 41 ? 0.2160 0.1927 0.3122 0.0093 -0.0117 -0.0715 49 GLY A CA 465 C C . GLY A 41 ? 0.2243 0.1946 0.3475 0.0243 -0.0034 -0.0752 49 GLY A C 466 O O . GLY A 41 ? 0.2269 0.2230 0.3671 0.0314 -0.0135 -0.0646 49 GLY A O 470 N N . SER A 42 ? 0.2830 0.1863 0.3754 0.0347 -0.0026 -0.0521 50 SER A N 471 C CA A SER A 42 ? 0.3290 0.1884 0.3921 0.0403 0.0066 -0.0345 50 SER A CA 472 C CA B SER A 42 ? 0.3176 0.1933 0.3914 0.0517 0.0104 -0.0324 50 SER A CA 473 C C . SER A 42 ? 0.3053 0.1656 0.3811 0.0575 -0.0129 -0.0109 50 SER A C 474 O O . SER A 42 ? 0.3778 0.2348 0.4012 0.0535 -0.0108 0.0058 50 SER A O 475 C CB A SER A 42 ? 0.3775 0.1957 0.4082 0.0328 0.0081 -0.0370 50 SER A CB 476 C CB B SER A 42 ? 0.3465 0.2154 0.4071 0.0661 0.0199 -0.0286 50 SER A CB 477 O OG A SER A 42 ? 0.4242 0.2295 0.4260 -0.0138 0.0282 -0.0422 50 SER A OG 478 O OG B SER A 42 ? 0.3769 0.2741 0.4256 0.0369 0.0533 -0.0315 50 SER A OG 487 N N . GLN A 43 ? 0.2415 0.1821 0.3778 0.0093 -0.0529 0.0049 51 GLN A N 488 C CA . GLN A 43 ? 0.2406 0.1943 0.3623 0.0180 -0.0296 0.0297 51 GLN A CA 489 C C . GLN A 43 ? 0.2437 0.2089 0.3649 0.0245 -0.0219 0.0284 51 GLN A C 490 O O . GLN A 43 ? 0.2585 0.2121 0.3577 -0.0190 -0.0253 0.0166 51 GLN A O 491 C CB . GLN A 43 ? 0.2222 0.1912 0.3556 0.0165 -0.0052 0.0244 51 GLN A CB 492 C CG . GLN A 43 ? 0.2412 0.1917 0.3678 -0.0098 0.0152 0.0163 51 GLN A CG 493 C CD . GLN A 43 ? 0.2376 0.2128 0.3712 -0.0214 0.0356 -0.0078 51 GLN A CD 494 O OE1 . GLN A 43 ? 0.2506 0.2712 0.3755 -0.0260 0.0409 -0.0137 51 GLN A OE1 495 N NE2 . GLN A 43 ? 0.2132 0.1862 0.3556 0.0040 0.0230 -0.0306 51 GLN A NE2 504 N N . PRO A 44 ? 0.2616 0.2146 0.3659 0.0231 -0.0201 0.0315 52 PRO A N 505 C CA . PRO A 44 ? 0.2706 0.2493 0.3530 0.0375 -0.0376 0.0430 52 PRO A CA 506 C C . PRO A 44 ? 0.2238 0.2341 0.3385 0.0118 -0.0385 0.0496 52 PRO A C 507 O O . PRO A 44 ? 0.2282 0.2615 0.3519 -0.0083 -0.0132 0.0664 52 PRO A O 508 C CB . PRO A 44 ? 0.3121 0.2518 0.3671 0.0585 -0.0306 0.0555 52 PRO A CB 509 C CG . PRO A 44 ? 0.2958 0.2801 0.3801 0.0195 -0.0223 0.0401 52 PRO A CG 510 C CD . PRO A 44 ? 0.2806 0.2287 0.3706 0.0243 -0.0279 0.0239 52 PRO A CD 518 N N . VAL A 45 ? 0.2062 0.2102 0.3165 0.0083 -0.0382 0.0382 53 VAL A N 519 C CA . VAL A 45 ? 0.1965 0.2216 0.3102 0.0210 -0.0377 0.0262 53 VAL A CA 520 C C . VAL A 45 ? 0.2359 0.2485 0.3151 0.0191 -0.0445 0.0276 53 VAL A C 521 O O . VAL A 45 ? 0.2323 0.3192 0.3015 0.0122 -0.0521 0.0232 53 VAL A O 522 C CB . VAL A 45 ? 0.1994 0.2172 0.3003 0.0231 -0.0382 0.0292 53 VAL A CB 523 C CG1 . VAL A 45 ? 0.2209 0.2486 0.3147 0.0202 -0.0306 0.0135 53 VAL A CG1 524 C CG2 . VAL A 45 ? 0.1987 0.2609 0.2885 0.0109 -0.0229 0.0336 53 VAL A CG2 534 N N . LEU A 46 ? 0.2976 0.3065 0.3133 0.0248 -0.0498 0.0708 54 LEU A N 535 C CA . LEU A 46 ? 0.3785 0.3976 0.3292 0.0331 -0.0422 0.0956 54 LEU A CA 536 C C . LEU A 46 ? 0.4080 0.4619 0.3503 -0.0027 -0.0586 0.0673 54 LEU A C 537 O O . LEU A 46 ? 0.4180 0.4520 0.3649 -0.0011 -0.0275 0.0718 54 LEU A O 538 C CB . LEU A 46 ? 0.4172 0.4508 0.3516 0.0308 0.0067 0.0876 54 LEU A CB 539 C CG . LEU A 46 ? 0.4551 0.4810 0.3752 0.0396 0.0486 0.1264 54 LEU A CG 540 C CD1 . LEU A 46 ? 0.4860 0.5019 0.3869 0.0341 0.0656 0.1261 54 LEU A CD1 541 C CD2 . LEU A 46 ? 0.4783 0.4888 0.3841 0.0700 0.0503 0.1337 54 LEU A CD2 553 N N . ASN A 47 ? 0.5347 0.5289 0.3892 0.0190 -0.0179 0.0441 55 ASN A N 554 C CA . ASN A 47 ? 0.6239 0.5588 0.4028 0.0717 0.0078 0.0475 55 ASN A CA 555 C C . ASN A 47 ? 0.6035 0.4747 0.3806 0.0926 0.0133 0.0514 55 ASN A C 556 O O . ASN A 47 ? 0.6181 0.4673 0.3818 0.0892 0.0551 0.0690 55 ASN A O 557 C CB . ASN A 47 ? 0.7037 0.6804 0.4472 0.0759 0.0445 0.0362 55 ASN A CB 558 C CG . ASN A 47 ? 0.7706 0.7893 0.4909 0.0843 0.0597 0.0292 55 ASN A CG 559 O OD1 . ASN A 47 ? 0.7938 0.8412 0.5116 0.0790 0.0605 0.0198 55 ASN A OD1 560 N ND2 . ASN A 47 ? 0.7952 0.8124 0.5038 0.0927 0.0682 0.0290 55 ASN A ND2 567 N N . ALA A 48 ? 0.5859 0.3743 0.3420 0.0694 -0.0048 0.0119 56 ALA A N 568 C CA . ALA A 48 ? 0.5298 0.2929 0.2985 0.0714 -0.0356 -0.0186 56 ALA A CA 569 C C . ALA A 48 ? 0.4435 0.2561 0.2751 0.0181 -0.0513 -0.0193 56 ALA A C 570 O O . ALA A 48 ? 0.4813 0.3038 0.2895 0.0601 -0.0420 -0.0011 56 ALA A O 571 C CB . ALA A 48 ? 0.5708 0.2963 0.3030 0.0733 -0.0106 -0.0386 56 ALA A CB 577 N N . GLY A 49 ? 0.3425 0.2490 0.2331 0.0148 -0.0230 -0.0068 57 GLY A N 578 C CA . GLY A 49 ? 0.2664 0.2535 0.2202 0.0068 -0.0540 -0.0054 57 GLY A CA 579 C C . GLY A 49 ? 0.1769 0.2353 0.2178 -0.0079 -0.0355 -0.0173 57 GLY A C 580 O O . GLY A 49 ? 0.2156 0.2659 0.2050 -0.0011 -0.0237 -0.0227 57 GLY A O 584 N N . PRO A 50 ? 0.1864 0.2510 0.2337 -0.0007 -0.0551 0.0050 58 PRO A N 585 C CA . PRO A 50 ? 0.1884 0.2981 0.2476 -0.0237 -0.0400 -0.0020 58 PRO A CA 586 C C . PRO A 50 ? 0.1868 0.2516 0.1899 0.0024 -0.0283 -0.0118 58 PRO A C 587 O O . PRO A 50 ? 0.2171 0.2438 0.2501 0.0026 0.0252 0.0122 58 PRO A O 588 C CB . PRO A 50 ? 0.2292 0.3487 0.2961 -0.0428 -0.0791 -0.0066 58 PRO A CB 589 C CG . PRO A 50 ? 0.2883 0.3287 0.2871 -0.0566 -0.1142 -0.0285 58 PRO A CG 590 C CD . PRO A 50 ? 0.2449 0.2581 0.2641 -0.0309 -0.1013 0.0023 58 PRO A CD 598 N N . TRP A 51 ? 0.1609 0.2230 0.1656 -0.0175 -0.0025 -0.0088 59 TRP A N 599 C CA . TRP A 51 ? 0.1413 0.2107 0.1786 -0.0099 -0.0083 -0.0016 59 TRP A CA 600 C C . TRP A 51 ? 0.1426 0.1906 0.1831 -0.0272 -0.0047 0.0221 59 TRP A C 601 O O . TRP A 51 ? 0.1712 0.2345 0.1914 -0.0172 -0.0290 0.0176 59 TRP A O 602 C CB . TRP A 51 ? 0.1888 0.2218 0.1908 -0.0150 0.0046 0.0044 59 TRP A CB 603 C CG . TRP A 51 ? 0.2138 0.2531 0.1786 -0.0079 -0.0203 0.0117 59 TRP A CG 604 C CD1 . TRP A 51 ? 0.3156 0.2686 0.2057 -0.0146 -0.0143 -0.0033 59 TRP A CD1 605 C CD2 . TRP A 51 ? 0.2992 0.2929 0.1983 -0.0520 0.0262 -0.0232 59 TRP A CD2 606 N NE1 . TRP A 51 ? 0.3281 0.2874 0.2324 -0.0063 -0.0267 -0.0368 59 TRP A NE1 607 C CE2 . TRP A 51 ? 0.2829 0.3063 0.2343 -0.0695 -0.0127 -0.0955 59 TRP A CE2 608 C CE3 . TRP A 51 ? 0.3928 0.3112 0.2311 -0.1071 0.0529 -0.0476 59 TRP A CE3 609 C CZ2 . TRP A 51 ? 0.3834 0.3825 0.2738 -0.0699 0.0106 -0.0962 59 TRP A CZ2 610 C CZ3 . TRP A 51 ? 0.4214 0.3766 0.2574 -0.0974 0.0600 -0.0375 59 TRP A CZ3 611 C CH2 . TRP A 51 ? 0.4127 0.3773 0.2725 -0.0909 0.0450 -0.0508 59 TRP A CH2 622 N N . GLY A 52 ? 0.1637 0.1965 0.1739 -0.0114 -0.0180 0.0147 60 GLY A N 623 C CA . GLY A 52 ? 0.1659 0.1869 0.1828 -0.0339 -0.0296 -0.0123 60 GLY A CA 624 C C . GLY A 52 ? 0.1513 0.1989 0.1863 -0.0378 -0.0078 -0.0012 60 GLY A C 625 O O . GLY A 52 ? 0.1894 0.2256 0.1807 -0.0513 -0.0423 0.0196 60 GLY A O 629 N N . ASP A 53 ? 0.1559 0.1904 0.1793 -0.0403 -0.0137 0.0124 61 ASP A N 630 C CA . ASP A 53 ? 0.1200 0.2113 0.1741 -0.0095 -0.0135 0.0220 61 ASP A CA 631 C C . ASP A 53 ? 0.1502 0.1881 0.1697 -0.0161 0.0018 0.0080 61 ASP A C 632 O O . ASP A 53 ? 0.1434 0.1867 0.1648 -0.0065 -0.0031 0.0011 61 ASP A O 633 C CB . ASP A 53 ? 0.1388 0.2017 0.2090 -0.0143 -0.0330 0.0163 61 ASP A CB 634 C CG . ASP A 53 ? 0.1561 0.2129 0.2262 -0.0068 -0.0365 0.0026 61 ASP A CG 635 O OD1 . ASP A 53 ? 0.1610 0.2361 0.2534 0.0009 -0.0395 -0.0004 61 ASP A OD1 636 O OD2 . ASP A 53 ? 0.1897 0.2995 0.2239 -0.0186 -0.0660 0.0108 61 ASP A OD2 641 N N . TYR A 54 ? 0.1383 0.2050 0.1627 -0.0076 -0.0219 0.0317 62 TYR A N 642 C CA . TYR A 54 ? 0.1285 0.1843 0.1800 -0.0054 -0.0007 -0.0002 62 TYR A CA 643 C C . TYR A 54 ? 0.1293 0.1593 0.1945 0.0058 0.0051 0.0122 62 TYR A C 644 O O . TYR A 54 ? 0.1393 0.2092 0.2002 0.0120 -0.0263 -0.0174 62 TYR A O 645 C CB . TYR A 54 ? 0.1216 0.2015 0.1928 -0.0120 -0.0161 0.0087 62 TYR A CB 646 C CG . TYR A 54 ? 0.1448 0.1890 0.1801 -0.0056 -0.0188 0.0128 62 TYR A CG 647 C CD1 . TYR A 54 ? 0.1441 0.1797 0.1656 -0.0200 0.0025 0.0154 62 TYR A CD1 648 C CD2 . TYR A 54 ? 0.1584 0.2159 0.1914 0.0222 -0.0188 -0.0055 62 TYR A CD2 649 C CE1 . TYR A 54 ? 0.1071 0.1898 0.1635 -0.0072 -0.0145 0.0115 62 TYR A CE1 650 C CE2 . TYR A 54 ? 0.1558 0.2375 0.1722 0.0273 -0.0382 0.0113 62 TYR A CE2 651 C CZ . TYR A 54 ? 0.1178 0.1999 0.1686 0.0012 -0.0066 0.0117 62 TYR A CZ 652 O OH . TYR A 54 ? 0.1619 0.2297 0.1797 0.0214 -0.0196 -0.0036 62 TYR A OH 662 N N . LEU A 55 ? 0.1202 0.1838 0.1999 0.0057 -0.0084 0.0045 63 LEU A N 663 C CA . LEU A 55 ? 0.1469 0.1593 0.2071 0.0003 0.0059 -0.0031 63 LEU A CA 664 C C . LEU A 55 ? 0.1301 0.1634 0.2051 0.0147 -0.0134 -0.0104 63 LEU A C 665 O O . LEU A 55 ? 0.1597 0.1647 0.2115 0.0014 -0.0094 -0.0276 63 LEU A O 666 C CB . LEU A 55 ? 0.1577 0.1673 0.2344 0.0061 0.0033 0.0145 63 LEU A CB 667 C CG . LEU A 55 ? 0.1651 0.2061 0.2632 -0.0019 -0.0200 0.0463 63 LEU A CG 668 C CD1 . LEU A 55 ? 0.2302 0.2258 0.2958 0.0171 0.0168 0.0628 63 LEU A CD1 669 C CD2 . LEU A 55 ? 0.2075 0.2753 0.2922 -0.0439 -0.0095 0.0604 63 LEU A CD2 681 N N . CYS A 56 ? 0.1350 0.1633 0.2074 -0.0041 -0.0127 -0.0006 64 CYS A N 682 C CA . CYS A 56 ? 0.1265 0.1620 0.1939 -0.0014 -0.0070 -0.0160 64 CYS A CA 683 C C . CYS A 56 ? 0.1052 0.1628 0.1823 0.0024 0.0067 -0.0025 64 CYS A C 684 O O . CYS A 56 ? 0.1162 0.1840 0.1604 0.0096 0.0055 0.0054 64 CYS A O 685 C CB . CYS A 56 ? 0.1034 0.1928 0.2176 0.0042 -0.0212 -0.0055 64 CYS A CB 686 S SG . CYS A 56 ? 0.1395 0.1939 0.2245 0.0210 -0.0239 -0.0030 64 CYS A SG 691 N N . ASP A 57 ? 0.1077 0.1904 0.1606 0.0139 0.0061 -0.0197 65 ASP A N 692 C CA . ASP A 57 ? 0.1272 0.1964 0.1604 0.0024 0.0004 -0.0214 65 ASP A CA 693 C C . ASP A 57 ? 0.1011 0.1857 0.1684 0.0163 -0.0089 -0.0191 65 ASP A C 694 O O . ASP A 57 ? 0.1032 0.1790 0.1722 0.0019 -0.0103 -0.0094 65 ASP A O 695 C CB . ASP A 57 ? 0.1155 0.1882 0.1639 -0.0076 0.0057 -0.0270 65 ASP A CB 696 C CG . ASP A 57 ? 0.1234 0.1803 0.1575 0.0208 0.0211 -0.0205 65 ASP A CG 697 O OD1 . ASP A 57 ? 0.1349 0.1826 0.1551 0.0073 0.0103 -0.0178 65 ASP A OD1 698 O OD2 . ASP A 57 ? 0.1315 0.2150 0.1695 0.0237 0.0032 -0.0581 65 ASP A OD2 703 N N . SER A 58 ? 0.1217 0.1760 0.1743 0.0084 -0.0180 -0.0192 66 SER A N 704 C CA . SER A 58 ? 0.1168 0.1717 0.1531 -0.0016 0.0065 -0.0143 66 SER A CA 705 C C . SER A 58 ? 0.1133 0.1518 0.1587 -0.0044 0.0167 0.0013 66 SER A C 706 O O . SER A 58 ? 0.1230 0.2149 0.1561 -0.0153 0.0162 -0.0164 66 SER A O 707 C CB . SER A 58 ? 0.1082 0.1542 0.1441 -0.0071 -0.0034 -0.0012 66 SER A CB 708 O OG . SER A 58 ? 0.1153 0.1710 0.1485 -0.0110 -0.0006 -0.0135 66 SER A OG 714 N N . PRO A 59 ? 0.1045 0.1768 0.1651 -0.0134 -0.0001 -0.0003 67 PRO A N 715 C CA . PRO A 59 ? 0.0993 0.1845 0.1752 -0.0102 0.0071 -0.0183 67 PRO A CA 716 C C . PRO A 59 ? 0.0966 0.1716 0.1600 -0.0233 0.0081 -0.0028 67 PRO A C 717 O O . PRO A 59 ? 0.0917 0.2011 0.1596 -0.0049 0.0081 -0.0069 67 PRO A O 718 C CB . PRO A 59 ? 0.1171 0.2157 0.1752 -0.0063 -0.0165 0.0008 67 PRO A CB 719 C CG . PRO A 59 ? 0.1157 0.2496 0.1724 -0.0087 -0.0014 -0.0059 67 PRO A CG 720 C CD . PRO A 59 ? 0.1034 0.1857 0.1719 0.0021 0.0101 0.0005 67 PRO A CD 728 N N . TRP A 60 ? 0.0970 0.2021 0.1550 -0.0081 0.0092 -0.0010 68 TRP A N 729 C CA . TRP A 60 ? 0.0942 0.2046 0.1579 -0.0158 0.0093 0.0141 68 TRP A CA 730 C C . TRP A 60 ? 0.1008 0.2017 0.1572 -0.0268 0.0032 -0.0045 68 TRP A C 731 O O . TRP A 60 ? 0.1237 0.1866 0.1686 -0.0216 0.0156 -0.0081 68 TRP A O 732 C CB . TRP A 60 ? 0.1167 0.2324 0.1799 -0.0156 0.0039 0.0000 68 TRP A CB 733 C CG . TRP A 60 ? 0.1501 0.2165 0.2024 -0.0407 0.0363 -0.0070 68 TRP A CG 734 C CD1 . TRP A 60 ? 0.1863 0.2454 0.2243 -0.0445 0.0493 0.0144 68 TRP A CD1 735 C CD2 . TRP A 60 ? 0.1757 0.2090 0.2228 -0.0213 0.0528 0.0070 68 TRP A CD2 736 N NE1 . TRP A 60 ? 0.2285 0.2293 0.2382 -0.0683 0.0577 -0.0130 68 TRP A NE1 737 C CE2 . TRP A 60 ? 0.2315 0.2055 0.2207 -0.0157 0.0757 0.0004 68 TRP A CE2 738 C CE3 . TRP A 60 ? 0.1623 0.2518 0.2338 -0.0108 0.0227 0.0354 68 TRP A CE3 739 C CZ2 . TRP A 60 ? 0.2490 0.2321 0.2425 -0.0094 0.0724 0.0089 68 TRP A CZ2 740 C CZ3 . TRP A 60 ? 0.1982 0.2545 0.2487 0.0334 0.0168 0.0406 68 TRP A CZ3 741 C CH2 . TRP A 60 ? 0.2498 0.2470 0.2582 0.0295 0.0586 0.0376 68 TRP A CH2 752 N N . ALA A 61 ? 0.1030 0.1988 0.1635 -0.0150 -0.0028 -0.0176 69 ALA A N 753 C CA . ALA A 61 ? 0.1096 0.2023 0.1788 -0.0170 -0.0085 -0.0267 69 ALA A CA 754 C C . ALA A 61 ? 0.1217 0.1914 0.1614 -0.0097 -0.0200 -0.0185 69 ALA A C 755 O O . ALA A 61 ? 0.1361 0.1937 0.1589 -0.0180 -0.0036 -0.0199 69 ALA A O 756 C CB . ALA A 61 ? 0.1171 0.2576 0.1752 -0.0168 -0.0142 -0.0241 69 ALA A CB 762 N N . LEU A 62 ? 0.1030 0.1827 0.1584 -0.0137 0.0100 -0.0173 70 LEU A N 763 C CA . LEU A 62 ? 0.1172 0.1879 0.1400 -0.0141 0.0147 -0.0041 70 LEU A CA 764 C C . LEU A 62 ? 0.1157 0.1817 0.1486 -0.0180 0.0059 -0.0139 70 LEU A C 765 O O . LEU A 62 ? 0.1191 0.1587 0.1508 -0.0153 0.0050 -0.0104 70 LEU A O 766 C CB . LEU A 62 ? 0.1044 0.1970 0.1519 -0.0068 0.0153 -0.0112 70 LEU A CB 767 C CG . LEU A 62 ? 0.1088 0.1768 0.1588 0.0001 0.0056 -0.0142 70 LEU A CG 768 C CD1 . LEU A 62 ? 0.1170 0.2155 0.1680 0.0023 0.0206 -0.0494 70 LEU A CD1 769 C CD2 . LEU A 62 ? 0.1375 0.1751 0.1646 -0.0145 0.0096 -0.0071 70 LEU A CD2 781 N N . ILE A 63 ? 0.1213 0.1754 0.1525 -0.0119 -0.0011 0.0080 71 ILE A N 782 C CA . ILE A 63 ? 0.1399 0.1753 0.1613 0.0086 -0.0091 -0.0152 71 ILE A CA 783 C C . ILE A 63 ? 0.1401 0.1673 0.1505 -0.0033 -0.0103 0.0055 71 ILE A C 784 O O . ILE A 63 ? 0.1352 0.1728 0.1598 -0.0021 -0.0170 -0.0074 71 ILE A O 785 C CB . ILE A 63 ? 0.1256 0.1736 0.1577 0.0034 -0.0017 -0.0059 71 ILE A CB 786 C CG1 . ILE A 63 ? 0.1252 0.1799 0.1635 0.0113 0.0050 -0.0054 71 ILE A CG1 787 C CG2 . ILE A 63 ? 0.1862 0.1811 0.1727 -0.0119 0.0024 -0.0141 71 ILE A CG2 788 C CD1 . ILE A 63 ? 0.1502 0.1976 0.1687 0.0196 -0.0039 -0.0245 71 ILE A CD1 800 N N . ASN A 64 ? 0.1281 0.1664 0.1664 -0.0070 -0.0075 -0.0064 72 ASN A N 801 C CA . ASN A 64 ? 0.1230 0.1895 0.1879 -0.0176 0.0032 -0.0214 72 ASN A CA 802 C C . ASN A 64 ? 0.1168 0.1814 0.1937 -0.0164 0.0067 -0.0078 72 ASN A C 803 O O . ASN A 64 ? 0.1432 0.1872 0.1704 -0.0260 -0.0080 -0.0084 72 ASN A O 804 C CB . ASN A 64 ? 0.1419 0.2228 0.2023 -0.0469 0.0158 -0.0213 72 ASN A CB 805 C CG . ASN A 64 ? 0.1645 0.2559 0.2216 -0.0350 -0.0189 -0.0195 72 ASN A CG 806 O OD1 . ASN A 64 ? 0.1799 0.2349 0.2238 -0.0505 -0.0073 -0.0120 72 ASN A OD1 807 N ND2 . ASN A 64 ? 0.2153 0.2260 0.2582 -0.0758 -0.0426 -0.0118 72 ASN A ND2 813 N N . SER A 65 ? 0.1265 0.1762 0.1833 -0.0247 -0.0054 -0.0234 73 SER A N 814 C CA A SER A 65 ? 0.1342 0.2013 0.1807 -0.0387 -0.0077 -0.0154 73 SER A CA 815 C CA B SER A 65 ? 0.1328 0.1798 0.1786 -0.0230 -0.0025 -0.0202 73 SER A CA 816 C C . SER A 65 ? 0.1286 0.1877 0.1741 -0.0156 0.0120 -0.0037 73 SER A C 817 O O . SER A 65 ? 0.1425 0.1936 0.1703 -0.0053 -0.0099 -0.0167 73 SER A O 818 C CB A SER A 65 ? 0.1563 0.2115 0.1815 -0.0116 -0.0120 -0.0297 73 SER A CB 819 C CB B SER A 65 ? 0.1416 0.1653 0.1769 -0.0133 -0.0092 -0.0418 73 SER A CB 820 O OG A SER A 65 ? 0.1372 0.2213 0.1810 -0.0131 0.0040 -0.0262 73 SER A OG 821 O OG B SER A 65 ? 0.1298 0.1656 0.1773 0.0114 -0.0128 -0.0544 73 SER A OG 830 N N . SER A 66 ? 0.1334 0.1831 0.1503 -0.0253 -0.0053 -0.0104 74 SER A N 831 C CA . SER A 66 ? 0.1370 0.1567 0.1621 -0.0319 -0.0071 0.0059 74 SER A CA 832 C C . SER A 66 ? 0.1333 0.1666 0.1603 -0.0275 0.0080 -0.0063 74 SER A C 833 O O . SER A 66 ? 0.1502 0.1728 0.1789 -0.0121 0.0014 -0.0046 74 SER A O 834 C CB . SER A 66 ? 0.1280 0.1993 0.1745 -0.0083 0.0149 -0.0047 74 SER A CB 835 O OG . SER A 66 ? 0.1264 0.2046 0.1669 -0.0230 -0.0006 -0.0248 74 SER A OG 841 N N . LEU A 67 ? 0.1330 0.1857 0.1624 -0.0207 0.0003 -0.0064 75 LEU A N 842 C CA . LEU A 67 ? 0.1510 0.1660 0.1800 -0.0149 0.0155 -0.0055 75 LEU A CA 843 C C . LEU A 67 ? 0.1666 0.1657 0.1821 -0.0078 0.0168 0.0038 75 LEU A C 844 O O . LEU A 67 ? 0.1688 0.1721 0.1742 -0.0197 0.0006 -0.0132 75 LEU A O 845 C CB . LEU A 67 ? 0.1495 0.1795 0.1926 -0.0231 0.0179 0.0027 75 LEU A CB 846 C CG . LEU A 67 ? 0.1669 0.1928 0.1811 -0.0196 0.0223 -0.0167 75 LEU A CG 847 C CD1 . LEU A 67 ? 0.2048 0.2287 0.1737 0.0009 0.0198 -0.0075 75 LEU A CD1 848 C CD2 . LEU A 67 ? 0.1695 0.2248 0.1924 -0.0166 -0.0030 -0.0019 75 LEU A CD2 860 N N . TYR A 68 ? 0.1535 0.1826 0.1996 -0.0178 -0.0041 -0.0199 76 TYR A N 861 C CA . TYR A 68 ? 0.1580 0.1843 0.2078 -0.0220 -0.0010 -0.0361 76 TYR A CA 862 C C . TYR A 68 ? 0.1787 0.1857 0.1973 -0.0142 -0.0134 -0.0236 76 TYR A C 863 O O . TYR A 68 ? 0.1935 0.2114 0.2084 -0.0183 -0.0206 -0.0367 76 TYR A O 864 C CB . TYR A 68 ? 0.1700 0.1974 0.2278 -0.0353 -0.0066 -0.0385 76 TYR A CB 865 C CG . TYR A 68 ? 0.1768 0.2106 0.2471 -0.0571 -0.0331 -0.0291 76 TYR A CG 866 C CD1 . TYR A 68 ? 0.2173 0.2321 0.3004 -0.0919 0.0300 -0.0425 76 TYR A CD1 867 C CD2 . TYR A 68 ? 0.1814 0.2312 0.2531 -0.0581 -0.0290 -0.0210 76 TYR A CD2 868 C CE1 . TYR A 68 ? 0.2317 0.2600 0.3218 -0.0994 0.0393 -0.0268 76 TYR A CE1 869 C CE2 . TYR A 68 ? 0.1991 0.2205 0.2767 -0.0599 -0.0093 -0.0169 76 TYR A CE2 870 C CZ . TYR A 68 ? 0.2349 0.2755 0.3006 -0.0966 0.0058 -0.0078 76 TYR A CZ 871 O OH . TYR A 68 ? 0.3007 0.3054 0.3303 -0.1265 0.0313 0.0046 76 TYR A OH 881 N N . ALA A 69 ? 0.1857 0.1929 0.1703 -0.0074 -0.0187 -0.0230 77 ALA A N 882 C CA . ALA A 69 ? 0.1775 0.1939 0.1667 -0.0227 -0.0051 -0.0404 77 ALA A CA 883 C C . ALA A 69 ? 0.1728 0.1790 0.1831 -0.0175 0.0174 -0.0315 77 ALA A C 884 O O . ALA A 69 ? 0.1840 0.2078 0.1933 0.0044 -0.0001 -0.0532 77 ALA A O 885 C CB . ALA A 69 ? 0.1986 0.2016 0.1879 0.0102 0.0044 -0.0094 77 ALA A CB 891 N N . MET A 70 ? 0.1720 0.1936 0.1690 -0.0146 -0.0004 -0.0207 78 MET A N 892 C CA . MET A 70 ? 0.1911 0.1687 0.1647 0.0133 0.0001 -0.0180 78 MET A CA 893 C C . MET A 70 ? 0.1904 0.1802 0.1842 -0.0091 0.0078 -0.0348 78 MET A C 894 O O . MET A 70 ? 0.1992 0.1801 0.2027 -0.0067 0.0025 -0.0564 78 MET A O 895 C CB . MET A 70 ? 0.1920 0.2010 0.1766 -0.0072 0.0216 -0.0382 78 MET A CB 896 C CG . MET A 70 ? 0.1798 0.1910 0.1771 -0.0055 -0.0271 -0.0399 78 MET A CG 897 S SD . MET A 70 ? 0.1741 0.2029 0.1965 -0.0080 -0.0087 -0.0335 78 MET A SD 898 C CE . MET A 70 ? 0.1841 0.2293 0.1882 0.0082 -0.0051 -0.0182 78 MET A CE 908 N N . LYS A 71 ? 0.1805 0.1738 0.2044 -0.0012 0.0083 -0.0333 79 LYS A N 909 C CA . LYS A 71 ? 0.2379 0.1802 0.2221 -0.0037 0.0126 -0.0406 79 LYS A CA 910 C C . LYS A 71 ? 0.2121 0.1707 0.2229 -0.0024 0.0044 -0.0414 79 LYS A C 911 O O . LYS A 71 ? 0.2431 0.1742 0.2358 -0.0094 -0.0042 -0.0472 79 LYS A O 912 C CB . LYS A 71 ? 0.2540 0.1988 0.2516 -0.0281 0.0370 -0.0648 79 LYS A CB 913 C CG . LYS A 71 ? 0.2881 0.2341 0.2988 -0.0499 0.0587 -0.0475 79 LYS A CG 914 C CD . LYS A 71 ? 0.3600 0.2725 0.3505 -0.1008 0.0847 -0.0605 79 LYS A CD 915 C CE . LYS A 71 ? 0.4133 0.3720 0.3986 -0.1108 0.1002 -0.0476 79 LYS A CE 916 N NZ . LYS A 71 ? 0.4496 0.4355 0.4289 -0.1270 0.0947 -0.0280 79 LYS A NZ 930 N N . GLU A 72 ? 0.2211 0.2269 0.2120 -0.0142 -0.0041 -0.0549 80 GLU A N 931 C CA . GLU A 72 ? 0.2376 0.2285 0.2121 -0.0313 0.0059 -0.0486 80 GLU A CA 932 C C . GLU A 72 ? 0.2276 0.2007 0.2104 -0.0294 0.0023 -0.0494 80 GLU A C 933 O O . GLU A 72 ? 0.2372 0.2253 0.2610 -0.0244 0.0030 -0.0918 80 GLU A O 934 C CB . GLU A 72 ? 0.3049 0.2731 0.2405 0.0017 -0.0193 -0.0542 80 GLU A CB 935 C CG . GLU A 72 ? 0.4342 0.3808 0.2839 0.0552 -0.0371 -0.0631 80 GLU A CG 936 C CD . GLU A 72 ? 0.5983 0.5063 0.3202 0.0699 -0.0345 -0.0741 80 GLU A CD 937 O OE1 . GLU A 72 ? 0.6663 0.5413 0.3501 0.0730 -0.0507 -0.0531 80 GLU A OE1 938 O OE2 . GLU A 72 ? 0.6623 0.5727 0.3490 0.0501 -0.0257 -0.0608 80 GLU A OE2 945 N N . ILE A 73 ? 0.2105 0.1854 0.1811 -0.0377 0.0048 -0.0317 81 ILE A N 946 C CA . ILE A 73 ? 0.2234 0.2125 0.1817 -0.0412 0.0286 -0.0509 81 ILE A CA 947 C C . ILE A 73 ? 0.2181 0.1926 0.2015 -0.0389 0.0139 -0.0660 81 ILE A C 948 O O . ILE A 73 ? 0.2402 0.2307 0.2196 -0.0108 0.0229 -0.0483 81 ILE A O 949 C CB . ILE A 73 ? 0.2288 0.2208 0.1973 -0.0433 0.0096 -0.0422 81 ILE A CB 950 C CG1 . ILE A 73 ? 0.2591 0.2022 0.1889 -0.0209 -0.0010 -0.0285 81 ILE A CG1 951 C CG2 . ILE A 73 ? 0.2272 0.2005 0.2111 -0.0347 0.0068 -0.0343 81 ILE A CG2 952 C CD1 . ILE A 73 ? 0.2474 0.1992 0.1935 -0.0461 -0.0037 -0.0099 81 ILE A CD1 964 N N . GLU A 74 ? 0.2008 0.1656 0.2164 -0.0152 -0.0043 -0.0532 82 GLU A N 965 C CA . GLU A 74 ? 0.2054 0.1790 0.2338 -0.0044 -0.0146 -0.0482 82 GLU A CA 966 C C . GLU A 74 ? 0.2266 0.1390 0.2295 0.0001 0.0142 -0.0318 82 GLU A C 967 O O . GLU A 74 ? 0.2191 0.1678 0.2140 -0.0160 0.0087 -0.0389 82 GLU A O 968 C CB . GLU A 74 ? 0.2072 0.1830 0.2367 0.0012 -0.0169 -0.0327 82 GLU A CB 969 C CG . GLU A 74 ? 0.2259 0.2519 0.2529 0.0118 -0.0076 -0.0236 82 GLU A CG 970 C CD . GLU A 74 ? 0.2788 0.2664 0.2898 0.0188 0.0436 -0.0060 82 GLU A CD 971 O OE1 . GLU A 74 ? 0.3250 0.3355 0.3303 0.0110 0.0727 -0.0392 82 GLU A OE1 972 O OE2 . GLU A 74 ? 0.3116 0.2619 0.3042 -0.0185 0.0427 -0.0195 82 GLU A OE2 979 N N . PRO A 75 ? 0.2541 0.1626 0.2271 -0.0200 -0.0086 -0.0410 83 PRO A N 980 C CA . PRO A 75 ? 0.2448 0.1662 0.2306 -0.0374 -0.0263 -0.0505 83 PRO A CA 981 C C . PRO A 75 ? 0.2303 0.1516 0.2454 -0.0447 -0.0143 -0.0287 83 PRO A C 982 O O . PRO A 75 ? 0.2460 0.1710 0.2637 -0.0463 0.0159 -0.0141 83 PRO A O 983 C CB . PRO A 75 ? 0.2612 0.2129 0.2333 -0.0257 -0.0414 -0.0528 83 PRO A CB 984 C CG . PRO A 75 ? 0.2807 0.2045 0.2474 -0.0354 -0.0449 -0.0576 83 PRO A CG 985 C CD . PRO A 75 ? 0.2806 0.1796 0.2408 -0.0297 -0.0341 -0.0681 83 PRO A CD 993 N N . LYS A 76 ? 0.2632 0.1445 0.2479 -0.0139 -0.0260 -0.0309 84 LYS A N 994 C CA . LYS A 76 ? 0.3215 0.1373 0.2765 -0.0254 -0.0112 -0.0176 84 LYS A CA 995 C C . LYS A 76 ? 0.2802 0.1493 0.2572 0.0033 0.0015 -0.0225 84 LYS A C 996 O O . LYS A 76 ? 0.2826 0.1753 0.2618 0.0052 0.0167 -0.0447 84 LYS A O 997 C CB . LYS A 76 ? 0.3420 0.1777 0.3139 -0.0367 -0.0524 -0.0285 84 LYS A CB 998 C CG . LYS A 76 ? 0.4125 0.2397 0.3576 -0.0039 -0.0404 -0.0416 84 LYS A CG 999 C CD . LYS A 76 ? 0.5010 0.3395 0.4060 0.0073 -0.0155 -0.0126 84 LYS A CD 1000 C CE . LYS A 76 ? 0.5648 0.4511 0.4390 0.0509 -0.0014 0.0085 84 LYS A CE 1001 N NZ . LYS A 76 ? 0.5967 0.5179 0.4586 0.0461 0.0017 0.0156 84 LYS A NZ 1015 N N . PRO A 77 ? 0.2451 0.1353 0.2242 0.0089 -0.0167 -0.0176 85 PRO A N 1016 C CA . PRO A 77 ? 0.2080 0.1619 0.2188 -0.0043 -0.0088 -0.0158 85 PRO A CA 1017 C C . PRO A 77 ? 0.2108 0.1630 0.2323 -0.0164 0.0023 -0.0114 85 PRO A C 1018 O O . PRO A 77 ? 0.2268 0.1680 0.2453 -0.0221 0.0132 -0.0055 85 PRO A O 1019 C CB . PRO A 77 ? 0.1848 0.1554 0.2078 -0.0183 -0.0144 0.0105 85 PRO A CB 1020 C CG . PRO A 77 ? 0.2066 0.1668 0.2154 -0.0095 -0.0074 -0.0027 85 PRO A CG 1021 C CD . PRO A 77 ? 0.2282 0.1673 0.2214 -0.0169 -0.0137 -0.0133 85 PRO A CD 1029 N N . ASP A 78 ? 0.2239 0.1429 0.2117 -0.0094 0.0010 -0.0103 86 ASP A N 1030 C CA A ASP A 78 ? 0.2491 0.1680 0.2177 0.0063 0.0069 -0.0070 86 ASP A CA 1031 C CA B ASP A 78 ? 0.2402 0.1596 0.2117 0.0062 0.0026 -0.0048 86 ASP A CA 1032 C C . ASP A 78 ? 0.2464 0.1766 0.2068 -0.0012 -0.0074 -0.0046 86 ASP A C 1033 O O . ASP A 78 ? 0.2587 0.1781 0.2230 0.0039 0.0042 0.0226 86 ASP A O 1034 C CB A ASP A 78 ? 0.2631 0.1856 0.2292 0.0151 0.0068 -0.0212 86 ASP A CB 1035 C CB B ASP A 78 ? 0.2422 0.1643 0.2138 0.0231 0.0017 -0.0076 86 ASP A CB 1036 C CG A ASP A 78 ? 0.2616 0.1846 0.2467 -0.0072 -0.0001 -0.0247 86 ASP A CG 1037 C CG B ASP A 78 ? 0.2296 0.1581 0.2186 0.0168 -0.0071 -0.0044 86 ASP A CG 1038 O OD1 A ASP A 78 ? 0.2774 0.1841 0.2646 -0.0381 0.0150 -0.0497 86 ASP A OD1 1039 O OD1 B ASP A 78 ? 0.2095 0.1450 0.2192 0.0107 0.0100 -0.0102 86 ASP A OD1 1040 O OD2 A ASP A 78 ? 0.2094 0.1868 0.2489 -0.0292 0.0128 -0.0312 86 ASP A OD2 1041 O OD2 B ASP A 78 ? 0.2261 0.1724 0.2300 -0.0003 -0.0026 -0.0133 86 ASP A OD2 1048 N N . PHE A 79 ? 0.2308 0.1570 0.1913 -0.0091 -0.0109 -0.0083 87 PHE A N 1049 C CA . PHE A 79 ? 0.1901 0.1627 0.1847 -0.0019 -0.0038 -0.0246 87 PHE A CA 1050 C C . PHE A 79 ? 0.1739 0.1710 0.1691 -0.0057 -0.0105 -0.0263 87 PHE A C 1051 O O . PHE A 79 ? 0.1754 0.1736 0.1705 0.0035 0.0024 -0.0180 87 PHE A O 1052 C CB . PHE A 79 ? 0.2137 0.1627 0.1855 -0.0002 0.0158 0.0010 87 PHE A CB 1053 C CG . PHE A 79 ? 0.1962 0.2142 0.1726 0.0505 0.0097 -0.0131 87 PHE A CG 1054 C CD1 . PHE A 79 ? 0.2164 0.2322 0.1952 0.0437 -0.0134 -0.0238 87 PHE A CD1 1055 C CD2 . PHE A 79 ? 0.1765 0.2267 0.1753 0.0420 -0.0117 -0.0216 87 PHE A CD2 1056 C CE1 . PHE A 79 ? 0.2099 0.2701 0.2044 0.0802 -0.0239 -0.0100 87 PHE A CE1 1057 C CE2 . PHE A 79 ? 0.1990 0.2502 0.1769 0.0281 -0.0066 -0.0047 87 PHE A CE2 1058 C CZ . PHE A 79 ? 0.1847 0.2710 0.1860 0.0389 -0.0152 -0.0123 87 PHE A CZ 1068 N N . ILE A 80 ? 0.1816 0.1501 0.1541 -0.0126 -0.0032 -0.0172 88 ILE A N 1069 C CA . ILE A 80 ? 0.1639 0.1645 0.1621 -0.0178 0.0026 -0.0036 88 ILE A CA 1070 C C . ILE A 80 ? 0.1581 0.1636 0.1564 -0.0365 0.0073 0.0115 88 ILE A C 1071 O O . ILE A 80 ? 0.1634 0.1611 0.1710 -0.0448 0.0231 -0.0071 88 ILE A O 1072 C CB . ILE A 80 ? 0.1578 0.1550 0.1725 -0.0333 0.0006 -0.0225 88 ILE A CB 1073 C CG1 . ILE A 80 ? 0.1794 0.1796 0.1712 -0.0452 0.0200 -0.0026 88 ILE A CG1 1074 C CG2 . ILE A 80 ? 0.1555 0.1743 0.1815 -0.0191 -0.0114 -0.0173 88 ILE A CG2 1075 C CD1 . ILE A 80 ? 0.1823 0.2044 0.1971 -0.0325 0.0054 -0.0118 88 ILE A CD1 1087 N N . LEU A 81 ? 0.1358 0.1464 0.1333 0.0079 0.0034 -0.0110 89 LEU A N 1088 C CA . LEU A 81 ? 0.1267 0.1481 0.1376 -0.0204 0.0052 -0.0091 89 LEU A CA 1089 C C . LEU A 81 ? 0.1206 0.1429 0.1450 -0.0087 0.0135 -0.0068 89 LEU A C 1090 O O . LEU A 81 ? 0.1480 0.1668 0.1339 0.0012 0.0061 -0.0026 89 LEU A O 1091 C CB . LEU A 81 ? 0.1535 0.1728 0.1407 0.0072 0.0111 -0.0217 89 LEU A CB 1092 C CG . LEU A 81 ? 0.1371 0.1657 0.1548 0.0057 -0.0039 -0.0336 89 LEU A CG 1093 C CD1 . LEU A 81 ? 0.1417 0.2001 0.1736 -0.0038 0.0123 -0.0291 89 LEU A CD1 1094 C CD2 . LEU A 81 ? 0.1494 0.1545 0.1761 0.0004 -0.0028 -0.0170 89 LEU A CD2 1106 N N . TRP A 82 ? 0.1118 0.1575 0.1533 -0.0022 0.0149 -0.0179 90 TRP A N 1107 C CA . TRP A 82 ? 0.1109 0.1576 0.1508 -0.0151 0.0219 -0.0137 90 TRP A CA 1108 C C . TRP A 82 ? 0.1288 0.1479 0.1429 -0.0005 0.0030 -0.0089 90 TRP A C 1109 O O . TRP A 82 ? 0.1545 0.1678 0.1390 -0.0136 0.0302 -0.0010 90 TRP A O 1110 C CB . TRP A 82 ? 0.1267 0.1727 0.1573 -0.0182 0.0336 -0.0173 90 TRP A CB 1111 C CG . TRP A 82 ? 0.0936 0.1815 0.1696 0.0060 0.0304 -0.0302 90 TRP A CG 1112 C CD1 . TRP A 82 ? 0.0968 0.1851 0.1685 -0.0097 0.0098 -0.0178 90 TRP A CD1 1113 C CD2 . TRP A 82 ? 0.1336 0.1433 0.1550 -0.0009 0.0035 -0.0071 90 TRP A CD2 1114 N NE1 . TRP A 82 ? 0.1268 0.1757 0.1405 -0.0107 -0.0018 0.0125 90 TRP A NE1 1115 C CE2 . TRP A 82 ? 0.1107 0.1857 0.1551 -0.0163 0.0070 -0.0013 90 TRP A CE2 1116 C CE3 . TRP A 82 ? 0.1348 0.1653 0.1424 -0.0315 -0.0160 -0.0068 90 TRP A CE3 1117 C CZ2 . TRP A 82 ? 0.1103 0.2058 0.1862 -0.0332 0.0023 0.0078 90 TRP A CZ2 1118 C CZ3 . TRP A 82 ? 0.1357 0.2098 0.1579 -0.0236 0.0001 -0.0013 90 TRP A CZ3 1119 C CH2 . TRP A 82 ? 0.1343 0.2309 0.1929 -0.0436 0.0069 0.0085 90 TRP A CH2 1130 N N . THR A 83 ? 0.1330 0.1507 0.1382 -0.0061 -0.0131 -0.0048 91 THR A N 1131 C CA . THR A 83 ? 0.1450 0.1792 0.1278 -0.0161 -0.0049 -0.0007 91 THR A CA 1132 C C . THR A 83 ? 0.1651 0.1713 0.1542 -0.0198 -0.0139 -0.0052 91 THR A C 1133 O O . THR A 83 ? 0.1739 0.1979 0.1742 -0.0177 -0.0083 -0.0175 91 THR A O 1134 C CB . THR A 83 ? 0.1591 0.1520 0.1568 -0.0099 0.0016 -0.0034 91 THR A CB 1135 O OG1 . THR A 83 ? 0.1293 0.1794 0.1427 -0.0179 0.0097 0.0029 91 THR A OG1 1136 C CG2 . THR A 83 ? 0.1482 0.1794 0.1603 -0.0208 -0.0130 0.0098 91 THR A CG2 1144 N N . GLY A 84 ? 0.1776 0.1636 0.1536 0.0104 0.0093 -0.0103 92 GLY A N 1145 C CA . GLY A 84 ? 0.1975 0.1855 0.1650 0.0265 0.0467 -0.0016 92 GLY A CA 1146 C C . GLY A 84 ? 0.1369 0.2003 0.1544 0.0061 0.0133 0.0036 92 GLY A C 1147 O O . GLY A 84 ? 0.1526 0.2095 0.1514 0.0046 0.0127 0.0010 92 GLY A O 1151 N N . ASP A 85 ? 0.1225 0.2258 0.1468 0.0099 0.0099 -0.0029 93 ASP A N 1152 C CA . ASP A 85 ? 0.1204 0.2263 0.1467 0.0043 -0.0075 -0.0217 93 ASP A CA 1153 C C . ASP A 85 ? 0.1293 0.1999 0.1409 0.0120 0.0063 0.0046 93 ASP A C 1154 O O . ASP A 85 ? 0.1290 0.2427 0.1412 0.0026 -0.0051 0.0114 93 ASP A O 1155 C CB . ASP A 85 ? 0.1244 0.1785 0.1570 -0.0138 0.0145 -0.0119 93 ASP A CB 1156 C CG . ASP A 85 ? 0.0874 0.2111 0.1446 0.0180 0.0249 0.0080 93 ASP A CG 1157 O OD1 . ASP A 85 ? 0.1557 0.2309 0.1518 -0.0099 0.0152 -0.0155 93 ASP A OD1 1158 O OD2 . ASP A 85 ? 0.1342 0.1864 0.1498 -0.0025 -0.0033 -0.0132 93 ASP A OD2 1163 N N . ASP A 86 ? 0.1063 0.2280 0.1531 0.0122 0.0156 -0.0229 94 ASP A N 1164 C CA . ASP A 86 ? 0.0971 0.2321 0.1600 -0.0041 0.0063 0.0059 94 ASP A CA 1165 C C . ASP A 86 ? 0.1087 0.1960 0.1507 -0.0037 0.0104 0.0031 94 ASP A C 1166 O O . ASP A 86 ? 0.1059 0.2385 0.1607 -0.0195 0.0118 0.0210 94 ASP A O 1167 C CB . ASP A 86 ? 0.1208 0.2402 0.1477 -0.0157 0.0168 0.0145 94 ASP A CB 1168 C CG . ASP A 86 ? 0.1215 0.2416 0.1579 0.0143 0.0476 -0.0028 94 ASP A CG 1169 O OD1 . ASP A 86 ? 0.1373 0.2102 0.1811 0.0152 0.0230 0.0137 94 ASP A OD1 1170 O OD2 . ASP A 86 ? 0.1631 0.2324 0.1540 0.0040 0.0451 0.0154 94 ASP A OD2 1175 N N . THR A 87 ? 0.1114 0.2094 0.1659 -0.0116 0.0132 -0.0226 95 THR A N 1176 C CA . THR A 87 ? 0.1154 0.2354 0.1533 0.0011 0.0210 0.0096 95 THR A CA 1177 C C . THR A 87 ? 0.1088 0.2093 0.1677 -0.0004 0.0441 -0.0119 95 THR A C 1178 O O . THR A 87 ? 0.1239 0.2408 0.1969 0.0005 0.0558 -0.0022 95 THR A O 1179 C CB . THR A 87 ? 0.1277 0.2325 0.1618 -0.0105 0.0038 0.0166 95 THR A CB 1180 O OG1 . THR A 87 ? 0.1535 0.2750 0.1881 -0.0521 -0.0098 0.0089 95 THR A OG1 1181 C CG2 . THR A 87 ? 0.1679 0.2827 0.1635 -0.0091 0.0315 -0.0030 95 THR A CG2 1189 N N . PRO A 88 ? 0.1236 0.2050 0.1571 0.0088 0.0162 -0.0158 96 PRO A N 1190 C CA . PRO A 88 ? 0.1591 0.2002 0.1703 -0.0092 0.0027 -0.0185 96 PRO A CA 1191 C C . PRO A 88 ? 0.1238 0.2290 0.1712 0.0020 0.0121 -0.0112 96 PRO A C 1192 O O . PRO A 88 ? 0.1507 0.2108 0.1727 0.0015 0.0021 -0.0208 96 PRO A O 1193 C CB . PRO A 88 ? 0.1785 0.2151 0.2108 -0.0385 -0.0341 -0.0286 96 PRO A CB 1194 C CG . PRO A 88 ? 0.1451 0.2337 0.2074 0.0130 -0.0272 -0.0463 96 PRO A CG 1195 C CD . PRO A 88 ? 0.1156 0.2310 0.1586 -0.0014 0.0042 -0.0290 96 PRO A CD 1203 N N . HIS A 89 ? 0.1415 0.1979 0.1729 0.0111 0.0125 -0.0513 97 HIS A N 1204 C CA . HIS A 89 ? 0.1482 0.1930 0.1819 0.0097 0.0031 -0.0354 97 HIS A CA 1205 C C . HIS A 89 ? 0.1593 0.2107 0.2051 0.0100 0.0027 -0.0402 97 HIS A C 1206 O O . HIS A 89 ? 0.1604 0.2231 0.2226 0.0303 0.0205 -0.0346 97 HIS A O 1207 C CB . HIS A 89 ? 0.1691 0.1657 0.1738 0.0119 -0.0110 -0.0236 97 HIS A CB 1208 C CG . HIS A 89 ? 0.1399 0.1762 0.1756 0.0048 -0.0068 -0.0143 97 HIS A CG 1209 N ND1 . HIS A 89 ? 0.1384 0.1761 0.1729 0.0169 -0.0032 -0.0172 97 HIS A ND1 1210 C CD2 . HIS A 89 ? 0.1413 0.1659 0.1736 -0.0007 0.0102 -0.0160 97 HIS A CD2 1211 C CE1 . HIS A 89 ? 0.1475 0.1672 0.1760 0.0058 0.0058 -0.0064 97 HIS A CE1 1212 N NE2 . HIS A 89 ? 0.1403 0.1722 0.1698 -0.0169 0.0038 -0.0180 97 HIS A NE2 1220 N N . VAL A 90 ? 0.1769 0.1837 0.2083 0.0210 0.0282 -0.0352 98 VAL A N 1221 C CA . VAL A 90 ? 0.1627 0.2156 0.2119 0.0250 0.0397 -0.0533 98 VAL A CA 1222 C C . VAL A 90 ? 0.1873 0.2416 0.2209 0.0343 0.0327 -0.0853 98 VAL A C 1223 O O . VAL A 90 ? 0.1675 0.2772 0.2187 0.0353 0.0084 -0.0605 98 VAL A O 1224 C CB . VAL A 90 ? 0.1550 0.2459 0.2218 0.0086 0.0469 -0.0249 98 VAL A CB 1225 C CG1 . VAL A 90 ? 0.1420 0.2723 0.2367 0.0160 0.0174 -0.0397 98 VAL A CG1 1226 C CG2 . VAL A 90 ? 0.2027 0.2752 0.2205 -0.0194 0.0331 -0.0262 98 VAL A CG2 1236 N N . PRO A 91 ? 0.1954 0.2430 0.2292 0.0459 0.0208 -0.0678 99 PRO A N 1237 C CA . PRO A 91 ? 0.2412 0.2556 0.2416 0.0529 0.0311 -0.0858 99 PRO A CA 1238 C C . PRO A 91 ? 0.2076 0.2733 0.2353 0.0515 0.0063 -0.0740 99 PRO A C 1239 O O . PRO A 91 ? 0.2064 0.2908 0.2290 0.0359 0.0126 -0.0759 99 PRO A O 1240 C CB . PRO A 91 ? 0.2880 0.2624 0.2601 0.0536 0.0526 -0.0929 99 PRO A CB 1241 C CG . PRO A 91 ? 0.3029 0.2545 0.2667 0.0608 0.0477 -0.0724 99 PRO A CG 1242 C CD . PRO A 91 ? 0.2723 0.2430 0.2622 0.0611 0.0369 -0.0566 99 PRO A CD 1250 N N . ASN A 92 ? 0.2061 0.3196 0.2425 0.0493 -0.0087 -0.0544 100 ASN A N 1251 C CA . ASN A 92 ? 0.1978 0.3171 0.2410 0.0683 -0.0284 -0.0453 100 ASN A CA 1252 C C . ASN A 92 ? 0.2000 0.3322 0.2298 0.0442 -0.0074 -0.0537 100 ASN A C 1253 O O . ASN A 92 ? 0.2096 0.3509 0.2429 0.0579 0.0108 -0.0519 100 ASN A O 1254 C CB . ASN A 92 ? 0.2347 0.3470 0.2545 0.0630 -0.0450 -0.0488 100 ASN A CB 1255 C CG . ASN A 92 ? 0.2611 0.3405 0.2873 0.0843 -0.0486 -0.0512 100 ASN A CG 1256 O OD1 . ASN A 92 ? 0.2482 0.3108 0.3239 0.0718 -0.0559 -0.0298 100 ASN A OD1 1257 N ND2 . ASN A 92 ? 0.3091 0.3672 0.3075 0.0501 -0.0363 -0.0414 100 ASN A ND2 1264 N N . GLU A 93 ? 0.2166 0.3625 0.2276 0.0723 0.0178 -0.0440 101 GLU A N 1265 C CA . GLU A 93 ? 0.2329 0.3812 0.2829 0.0719 0.0341 -0.0577 101 GLU A CA 1266 C C . GLU A 93 ? 0.1834 0.3902 0.2706 0.0476 0.0164 -0.0471 101 GLU A C 1267 O O . GLU A 93 ? 0.2027 0.4570 0.2807 0.0350 0.0316 -0.0366 101 GLU A O 1268 C CB . GLU A 93 ? 0.2822 0.4155 0.3187 0.0991 0.0293 -0.0799 101 GLU A CB 1269 C CG . GLU A 93 ? 0.3944 0.4726 0.3552 0.1050 0.0367 -0.0943 101 GLU A CG 1270 C CD . GLU A 93 ? 0.4911 0.5216 0.3615 0.0736 0.0275 -0.1140 101 GLU A CD 1271 O OE1 . GLU A 93 ? 0.4752 0.4404 0.3453 0.0719 0.0152 -0.1524 101 GLU A OE1 1272 O OE2 . GLU A 93 ? 0.5731 0.5942 0.3891 0.0474 0.0238 -0.1012 101 GLU A OE2 1279 N N . SER A 94 ? 0.1953 0.3279 0.2644 0.0426 0.0140 -0.0575 102 SER A N 1280 C CA . SER A 94 ? 0.2196 0.3665 0.2601 -0.0031 -0.0113 -0.0279 102 SER A CA 1281 C C . SER A 94 ? 0.2729 0.3371 0.2353 -0.0142 -0.0147 -0.0131 102 SER A C 1282 O O . SER A 94 ? 0.2918 0.3700 0.2559 -0.0604 -0.0272 0.0006 102 SER A O 1283 C CB . SER A 94 ? 0.2686 0.3738 0.2629 0.0374 -0.0328 -0.0046 102 SER A CB 1284 O OG . SER A 94 ? 0.2905 0.4367 0.2979 0.0606 -0.0220 -0.0182 102 SER A OG 1290 N N . LEU A 95 ? 0.2619 0.3212 0.2042 -0.0082 -0.0109 -0.0263 103 LEU A N 1291 C CA . LEU A 95 ? 0.3475 0.3362 0.2314 -0.0327 0.0207 -0.0207 103 LEU A CA 1292 C C . LEU A 95 ? 0.3547 0.3226 0.2499 -0.0004 0.0252 -0.0231 103 LEU A C 1293 O O . LEU A 95 ? 0.3395 0.3681 0.2678 -0.0190 0.0267 -0.0438 103 LEU A O 1294 C CB . LEU A 95 ? 0.3529 0.3826 0.2961 -0.0116 0.0332 -0.0116 103 LEU A CB 1295 C CG . LEU A 95 ? 0.4043 0.4344 0.3250 -0.0916 0.0854 -0.0379 103 LEU A CG 1296 C CD1 . LEU A 95 ? 0.4238 0.3865 0.3361 -0.1372 0.1222 -0.0520 103 LEU A CD1 1297 C CD2 . LEU A 95 ? 0.3998 0.4618 0.3321 -0.1262 0.0794 -0.0224 103 LEU A CD2 1309 N N . GLY A 96 ? 0.3046 0.2774 0.2447 0.0085 0.0630 -0.0238 104 GLY A N 1310 C CA . GLY A 96 ? 0.2479 0.2504 0.2191 0.0001 0.0338 -0.0165 104 GLY A CA 1311 C C . GLY A 96 ? 0.1876 0.2587 0.1970 -0.0148 0.0086 -0.0196 104 GLY A C 1312 O O . GLY A 96 ? 0.1870 0.2481 0.2032 -0.0272 0.0435 -0.0182 104 GLY A O 1316 N N . GLU A 97 ? 0.1904 0.2640 0.1845 0.0027 0.0148 -0.0038 105 GLU A N 1317 C CA . GLU A 97 ? 0.1644 0.2723 0.1634 0.0041 0.0241 -0.0149 105 GLU A CA 1318 C C . GLU A 97 ? 0.1495 0.2844 0.1500 -0.0074 0.0261 -0.0015 105 GLU A C 1319 O O . GLU A 97 ? 0.1551 0.2779 0.1485 -0.0014 0.0134 0.0027 105 GLU A O 1320 C CB . GLU A 97 ? 0.2017 0.3340 0.1753 -0.0024 0.0255 -0.0083 105 GLU A CB 1321 C CG . GLU A 97 ? 0.2754 0.3667 0.2026 0.0251 0.0259 0.0410 105 GLU A CG 1322 C CD . GLU A 97 ? 0.3839 0.4468 0.2242 0.0228 0.0086 0.0468 105 GLU A CD 1323 O OE1 . GLU A 97 ? 0.4647 0.4992 0.2201 -0.0087 -0.0111 0.0448 105 GLU A OE1 1324 O OE2 . GLU A 97 ? 0.4319 0.4967 0.2213 0.0344 0.0367 0.0577 105 GLU A OE2 1331 N N . ALA A 98 ? 0.1496 0.2772 0.1715 0.0015 0.0283 -0.0005 106 ALA A N 1332 C CA . ALA A 98 ? 0.1389 0.2656 0.1730 0.0060 0.0420 0.0019 106 ALA A CA 1333 C C . ALA A 98 ? 0.1239 0.2619 0.1670 0.0158 0.0189 0.0012 106 ALA A C 1334 O O . ALA A 98 ? 0.1214 0.2662 0.1813 0.0178 0.0230 0.0068 106 ALA A O 1335 C CB . ALA A 98 ? 0.1498 0.3223 0.2124 0.0115 0.0355 -0.0148 106 ALA A CB 1341 N N . ALA A 99 ? 0.1228 0.2894 0.1699 -0.0019 0.0210 -0.0028 107 ALA A N 1342 C CA . ALA A 99 ? 0.1324 0.2766 0.1591 0.0202 0.0241 0.0141 107 ALA A CA 1343 C C . ALA A 99 ? 0.1341 0.2583 0.1468 0.0099 0.0297 -0.0118 107 ALA A C 1344 O O . ALA A 99 ? 0.1319 0.2549 0.1547 -0.0056 0.0061 0.0015 107 ALA A O 1345 C CB . ALA A 99 ? 0.1562 0.2831 0.1814 0.0421 0.0213 0.0105 107 ALA A CB 1351 N N . VAL A 100 ? 0.1362 0.2256 0.1542 -0.0033 0.0206 -0.0141 108 VAL A N 1352 C CA . VAL A 100 ? 0.1189 0.2504 0.1493 -0.0069 0.0093 -0.0046 108 VAL A CA 1353 C C . VAL A 100 ? 0.0979 0.2488 0.1564 -0.0076 0.0017 -0.0123 108 VAL A C 1354 O O . VAL A 100 ? 0.1115 0.2567 0.1468 -0.0033 0.0128 0.0088 108 VAL A O 1355 C CB . VAL A 100 ? 0.1457 0.2698 0.1685 -0.0170 0.0174 -0.0319 108 VAL A CB 1356 C CG1 . VAL A 100 ? 0.1305 0.2923 0.1722 -0.0156 0.0184 -0.0419 108 VAL A CG1 1357 C CG2 . VAL A 100 ? 0.1577 0.2918 0.1839 -0.0238 0.0258 -0.0221 108 VAL A CG2 1367 N N . LEU A 101 ? 0.1054 0.2715 0.1417 0.0046 0.0177 -0.0141 109 LEU A N 1368 C CA . LEU A 101 ? 0.1243 0.2551 0.1547 0.0003 0.0127 -0.0020 109 LEU A CA 1369 C C . LEU A 101 ? 0.1158 0.2366 0.1533 -0.0218 0.0206 0.0065 109 LEU A C 1370 O O . LEU A 101 ? 0.1251 0.2606 0.1595 -0.0068 -0.0037 -0.0045 109 LEU A O 1371 C CB . LEU A 101 ? 0.1380 0.2814 0.1462 -0.0049 0.0128 0.0011 109 LEU A CB 1372 C CG . LEU A 101 ? 0.1527 0.2653 0.1624 -0.0047 0.0079 0.0168 109 LEU A CG 1373 C CD1 . LEU A 101 ? 0.1706 0.3074 0.1542 -0.0011 0.0161 0.0335 109 LEU A CD1 1374 C CD2 . LEU A 101 ? 0.1738 0.3089 0.1816 -0.0199 -0.0180 0.0243 109 LEU A CD2 1386 N N . ALA A 102 ? 0.0897 0.2635 0.1596 0.0014 0.0143 0.0025 110 ALA A N 1387 C CA . ALA A 102 ? 0.0858 0.2781 0.1535 -0.0061 0.0179 0.0052 110 ALA A CA 1388 C C . ALA A 102 ? 0.0820 0.2418 0.1457 -0.0093 0.0050 -0.0104 110 ALA A C 1389 O O . ALA A 102 ? 0.1191 0.2416 0.1455 0.0000 0.0098 -0.0104 110 ALA A O 1390 C CB . ALA A 102 ? 0.1072 0.2781 0.1707 -0.0138 0.0142 -0.0226 110 ALA A CB 1396 N N . ILE A 103 ? 0.0901 0.2173 0.1563 -0.0194 0.0124 -0.0077 111 ILE A N 1397 C CA . ILE A 103 ? 0.1147 0.2174 0.1552 -0.0020 0.0126 -0.0034 111 ILE A CA 1398 C C . ILE A 103 ? 0.1053 0.2222 0.1544 -0.0223 0.0166 -0.0168 111 ILE A C 1399 O O . ILE A 103 ? 0.1057 0.2197 0.1640 -0.0136 0.0082 -0.0166 111 ILE A O 1400 C CB . ILE A 103 ? 0.1288 0.2240 0.1612 0.0075 0.0043 0.0028 111 ILE A CB 1401 C CG1 . ILE A 103 ? 0.1249 0.2415 0.1808 0.0052 0.0068 0.0072 111 ILE A CG1 1402 C CG2 . ILE A 103 ? 0.1337 0.2607 0.1564 -0.0122 0.0158 0.0049 111 ILE A CG2 1403 C CD1 . ILE A 103 ? 0.1685 0.2312 0.2063 0.0444 -0.0025 0.0097 111 ILE A CD1 1415 N N . VAL A 104 ? 0.0994 0.2326 0.1468 -0.0080 0.0076 -0.0097 112 VAL A N 1416 C CA . VAL A 104 ? 0.1134 0.2399 0.1428 0.0144 0.0093 -0.0207 112 VAL A CA 1417 C C . VAL A 104 ? 0.1017 0.2586 0.1433 0.0090 0.0055 -0.0123 112 VAL A C 1418 O O . VAL A 104 ? 0.1250 0.2677 0.1557 0.0012 0.0129 -0.0189 112 VAL A O 1419 C CB . VAL A 104 ? 0.1329 0.2345 0.1491 0.0317 -0.0031 -0.0052 112 VAL A CB 1420 C CG1 . VAL A 104 ? 0.1384 0.2530 0.1573 -0.0028 -0.0086 0.0108 112 VAL A CG1 1421 C CG2 . VAL A 104 ? 0.1397 0.2243 0.1793 0.0044 -0.0152 -0.0212 112 VAL A CG2 1431 N N . GLU A 105 ? 0.1192 0.2348 0.1560 -0.0064 0.0127 -0.0057 113 GLU A N 1432 C CA A GLU A 105 ? 0.1223 0.2411 0.1580 -0.0022 0.0195 0.0108 113 GLU A CA 1433 C CA B GLU A 105 ? 0.1322 0.2464 0.1618 -0.0116 0.0224 0.0086 113 GLU A CA 1434 C C . GLU A 105 ? 0.1106 0.2368 0.1611 -0.0082 0.0135 0.0067 113 GLU A C 1435 O O . GLU A 105 ? 0.1328 0.2201 0.1869 -0.0160 0.0062 0.0053 113 GLU A O 1436 C CB A GLU A 105 ? 0.1309 0.2836 0.1644 -0.0436 0.0079 0.0175 113 GLU A CB 1437 C CB B GLU A 105 ? 0.1620 0.2876 0.1736 -0.0509 0.0244 0.0163 113 GLU A CB 1438 C CG A GLU A 105 ? 0.1819 0.3328 0.1808 -0.0730 0.0123 0.0328 113 GLU A CG 1439 C CG B GLU A 105 ? 0.2214 0.3362 0.1919 -0.0803 0.0379 0.0324 113 GLU A CG 1440 C CD A GLU A 105 ? 0.2578 0.4157 0.2275 -0.1203 0.0384 0.0079 113 GLU A CD 1441 C CD B GLU A 105 ? 0.2967 0.4034 0.2229 -0.1073 0.0602 0.0335 113 GLU A CD 1442 O OE1 A GLU A 105 ? 0.2619 0.4479 0.2124 -0.1255 0.0375 0.0048 113 GLU A OE1 1443 O OE1 B GLU A 105 ? 0.3238 0.4272 0.2393 -0.1104 0.0606 0.0558 113 GLU A OE1 1444 O OE2 A GLU A 105 ? 0.3299 0.4585 0.2809 -0.1518 0.0567 -0.0140 113 GLU A OE2 1445 O OE2 B GLU A 105 ? 0.3249 0.4410 0.2184 -0.1082 0.0487 0.0292 113 GLU A OE2 1456 N N . ARG A 106 ? 0.1190 0.2658 0.1487 -0.0159 0.0098 0.0009 114 ARG A N 1457 C CA . ARG A 106 ? 0.1397 0.2482 0.1670 -0.0224 0.0039 -0.0123 114 ARG A CA 1458 C C . ARG A 106 ? 0.1276 0.2288 0.1544 -0.0310 0.0059 -0.0007 114 ARG A C 1459 O O . ARG A 106 ? 0.1243 0.2255 0.1693 -0.0222 -0.0061 -0.0103 114 ARG A O 1460 C CB . ARG A 106 ? 0.1505 0.2917 0.1505 0.0028 -0.0089 -0.0149 114 ARG A CB 1461 C CG . ARG A 106 ? 0.1640 0.3174 0.1599 -0.0035 -0.0215 -0.0110 114 ARG A CG 1462 C CD . ARG A 106 ? 0.1568 0.3318 0.1760 -0.0147 -0.0233 -0.0022 114 ARG A CD 1463 N NE . ARG A 106 ? 0.1303 0.3360 0.1817 -0.0197 -0.0207 -0.0041 114 ARG A NE 1464 C CZ . ARG A 106 ? 0.1266 0.3625 0.1898 -0.0173 0.0040 0.0022 114 ARG A CZ 1465 N NH1 . ARG A 106 ? 0.1102 0.3568 0.1831 0.0157 -0.0128 0.0100 114 ARG A NH1 1466 N NH2 . ARG A 106 ? 0.1401 0.3508 0.1713 -0.0244 0.0043 0.0116 114 ARG A NH2 1480 N N . LEU A 107 ? 0.1147 0.2191 0.1590 -0.0060 0.0012 -0.0117 115 LEU A N 1481 C CA A LEU A 107 ? 0.1291 0.2095 0.1642 -0.0072 0.0127 -0.0185 115 LEU A CA 1482 C CA B LEU A 107 ? 0.1285 0.2119 0.1696 -0.0054 0.0067 -0.0207 115 LEU A CA 1483 C C . LEU A 107 ? 0.1192 0.2163 0.1722 0.0056 0.0069 -0.0217 115 LEU A C 1484 O O . LEU A 107 ? 0.1207 0.2225 0.1760 -0.0037 0.0025 -0.0171 115 LEU A O 1485 C CB A LEU A 107 ? 0.1395 0.2083 0.1599 -0.0303 -0.0066 -0.0254 115 LEU A CB 1486 C CB B LEU A 107 ? 0.1448 0.2157 0.1786 -0.0198 -0.0134 -0.0286 115 LEU A CB 1487 C CG A LEU A 107 ? 0.1321 0.1893 0.1745 -0.0184 -0.0124 -0.0186 115 LEU A CG 1488 C CG B LEU A 107 ? 0.1909 0.2223 0.1913 -0.0374 -0.0077 -0.0338 115 LEU A CG 1489 C CD1 A LEU A 107 ? 0.1514 0.2172 0.1870 0.0003 0.0337 0.0102 115 LEU A CD1 1490 C CD1 B LEU A 107 ? 0.2170 0.2361 0.2149 -0.0389 -0.0107 -0.0241 115 LEU A CD1 1491 C CD2 A LEU A 107 ? 0.1951 0.2479 0.1544 -0.0059 0.0003 -0.0336 115 LEU A CD2 1492 C CD2 B LEU A 107 ? 0.2429 0.2238 0.1930 -0.0619 0.0274 -0.0120 115 LEU A CD2 1513 N N . THR A 108 ? 0.1341 0.2175 0.1601 -0.0154 0.0104 0.0033 116 THR A N 1514 C CA . THR A 108 ? 0.1456 0.2372 0.1623 -0.0039 0.0047 -0.0079 116 THR A CA 1515 C C . THR A 108 ? 0.1431 0.2141 0.1632 -0.0258 0.0127 -0.0019 116 THR A C 1516 O O . THR A 108 ? 0.1394 0.2185 0.1640 -0.0188 0.0071 -0.0044 116 THR A O 1517 C CB . THR A 108 ? 0.1441 0.2418 0.1650 -0.0174 -0.0032 -0.0008 116 THR A CB 1518 O OG1 . THR A 108 ? 0.1331 0.2069 0.1672 -0.0270 0.0007 0.0020 116 THR A OG1 1519 C CG2 . THR A 108 ? 0.1618 0.2543 0.1741 -0.0078 -0.0102 0.0081 116 THR A CG2 1527 N N . ASN A 109 ? 0.1384 0.2079 0.1700 -0.0286 0.0080 0.0080 117 ASN A N 1528 C CA . ASN A 109 ? 0.1386 0.2093 0.1791 -0.0399 0.0037 0.0081 117 ASN A CA 1529 C C . ASN A 109 ? 0.1467 0.2219 0.1704 -0.0324 0.0038 0.0079 117 ASN A C 1530 O O . ASN A 109 ? 0.1705 0.2303 0.1859 -0.0469 -0.0081 0.0000 117 ASN A O 1531 C CB . ASN A 109 ? 0.1511 0.2390 0.1856 -0.0417 0.0168 0.0067 117 ASN A CB 1532 C CG . ASN A 109 ? 0.1508 0.2748 0.2004 -0.0433 0.0251 0.0155 117 ASN A CG 1533 O OD1 . ASN A 109 ? 0.2141 0.3107 0.2010 -0.0495 0.0338 0.0397 117 ASN A OD1 1534 N ND2 . ASN A 109 ? 0.1958 0.3054 0.2156 -0.0547 0.0596 -0.0091 117 ASN A ND2 1541 N N . LEU A 110 ? 0.1357 0.2181 0.1761 -0.0326 0.0000 0.0092 118 LEU A N 1542 C CA . LEU A 110 ? 0.1532 0.2018 0.1772 -0.0436 0.0044 -0.0015 118 LEU A CA 1543 C C . LEU A 110 ? 0.1403 0.2095 0.1701 -0.0251 0.0062 0.0023 118 LEU A C 1544 O O . LEU A 110 ? 0.1602 0.1970 0.1774 -0.0266 0.0036 -0.0030 118 LEU A O 1545 C CB . LEU A 110 ? 0.1446 0.2092 0.1820 -0.0222 -0.0014 -0.0202 118 LEU A CB 1546 C CG . LEU A 110 ? 0.1839 0.1923 0.1908 0.0149 -0.0009 -0.0141 118 LEU A CG 1547 C CD1 . LEU A 110 ? 0.2347 0.2124 0.1854 0.0014 -0.0105 -0.0297 118 LEU A CD1 1548 C CD2 . LEU A 110 ? 0.2022 0.2065 0.2018 0.0229 0.0093 0.0066 118 LEU A CD2 1560 N N . ILE A 111 ? 0.1367 0.1816 0.1759 -0.0290 0.0079 0.0028 119 ILE A N 1561 C CA . ILE A 111 ? 0.1369 0.1924 0.1831 -0.0292 0.0069 0.0017 119 ILE A CA 1562 C C . ILE A 111 ? 0.1531 0.1887 0.2041 -0.0469 -0.0033 -0.0014 119 ILE A C 1563 O O . ILE A 111 ? 0.1898 0.1776 0.2107 -0.0314 -0.0084 -0.0245 119 ILE A O 1564 C CB . ILE A 111 ? 0.1337 0.2112 0.1809 -0.0344 0.0051 -0.0129 119 ILE A CB 1565 C CG1 . ILE A 111 ? 0.1614 0.2184 0.1726 -0.0522 0.0066 -0.0253 119 ILE A CG1 1566 C CG2 . ILE A 111 ? 0.1513 0.2536 0.1945 -0.0095 0.0124 0.0077 119 ILE A CG2 1567 C CD1 . ILE A 111 ? 0.1735 0.2168 0.1915 -0.0310 0.0034 -0.0201 119 ILE A CD1 1579 N N . LYS A 112 ? 0.1524 0.2010 0.1986 -0.0424 -0.0019 0.0105 120 LYS A N 1580 C CA . LYS A 112 ? 0.1970 0.1928 0.2199 -0.0520 0.0068 0.0109 120 LYS A CA 1581 C C . LYS A 112 ? 0.2231 0.1793 0.2399 -0.0373 0.0132 -0.0166 120 LYS A C 1582 O O . LYS A 112 ? 0.2658 0.2024 0.2596 -0.0588 0.0048 -0.0067 120 LYS A O 1583 C CB . LYS A 112 ? 0.2187 0.2069 0.2075 -0.0522 -0.0167 0.0229 120 LYS A CB 1584 C CG . LYS A 112 ? 0.1945 0.2128 0.2228 -0.0581 -0.0193 0.0263 120 LYS A CG 1585 C CD . LYS A 112 ? 0.2251 0.2626 0.2080 -0.0454 -0.0276 0.0250 120 LYS A CD 1586 C CE . LYS A 112 ? 0.2469 0.2798 0.2147 -0.0510 -0.0256 0.0469 120 LYS A CE 1587 N NZ . LYS A 112 ? 0.2427 0.3188 0.2303 -0.0904 -0.0373 0.0509 120 LYS A NZ 1601 N N . GLU A 113 ? 0.1755 0.2170 0.2216 -0.0536 0.0121 -0.0068 121 GLU A N 1602 C CA . GLU A 113 ? 0.2041 0.2418 0.2434 -0.0701 -0.0032 -0.0196 121 GLU A CA 1603 C C . GLU A 113 ? 0.2196 0.2101 0.2351 -0.0671 -0.0093 -0.0297 121 GLU A C 1604 O O . GLU A 113 ? 0.2544 0.2297 0.2731 -0.0885 0.0108 -0.0334 121 GLU A O 1605 C CB . GLU A 113 ? 0.2095 0.2808 0.2590 -0.0647 -0.0470 -0.0556 121 GLU A CB 1606 C CG . GLU A 113 ? 0.3000 0.3884 0.3220 -0.0243 -0.0461 -0.0737 121 GLU A CG 1607 C CD . GLU A 113 ? 0.3934 0.5128 0.3782 -0.0133 -0.0595 -0.0957 121 GLU A CD 1608 O OE1 . GLU A 113 ? 0.4231 0.5395 0.4023 0.0116 -0.0497 -0.1004 121 GLU A OE1 1609 O OE2 . GLU A 113 ? 0.4415 0.5598 0.4126 -0.0541 -0.0622 -0.0953 121 GLU A OE2 1616 N N . VAL A 114 ? 0.1905 0.2142 0.2100 -0.0588 -0.0080 -0.0175 122 VAL A N 1617 C CA . VAL A 114 ? 0.1883 0.2031 0.2129 -0.0458 -0.0068 -0.0338 122 VAL A CA 1618 C C . VAL A 114 ? 0.2122 0.1807 0.2288 -0.0352 0.0227 -0.0233 122 VAL A C 1619 O O . VAL A 114 ? 0.2093 0.1910 0.2488 -0.0390 0.0146 -0.0353 122 VAL A O 1620 C CB . VAL A 114 ? 0.2078 0.1933 0.2156 -0.0323 -0.0063 -0.0103 122 VAL A CB 1621 C CG1 . VAL A 114 ? 0.2679 0.2195 0.2174 -0.0235 0.0253 0.0012 122 VAL A CG1 1622 C CG2 . VAL A 114 ? 0.2190 0.2016 0.2198 -0.0412 0.0012 -0.0128 122 VAL A CG2 1632 N N . PHE A 115 ? 0.1811 0.1746 0.2196 -0.0336 0.0038 -0.0147 123 PHE A N 1633 C CA . PHE A 115 ? 0.2139 0.1916 0.2245 -0.0558 0.0217 -0.0089 123 PHE A CA 1634 C C . PHE A 115 ? 0.2296 0.1941 0.2449 -0.0500 0.0166 -0.0040 123 PHE A C 1635 O O . PHE A 115 ? 0.2182 0.2103 0.2308 -0.0537 0.0004 0.0185 123 PHE A O 1636 C CB . PHE A 115 ? 0.1788 0.1869 0.2199 -0.0228 -0.0039 0.0000 123 PHE A CB 1637 C CG . PHE A 115 ? 0.1895 0.1715 0.2224 -0.0349 -0.0027 -0.0115 123 PHE A CG 1638 C CD1 . PHE A 115 ? 0.1918 0.1567 0.2227 -0.0272 -0.0135 0.0050 123 PHE A CD1 1639 C CD2 . PHE A 115 ? 0.1884 0.1801 0.2313 -0.0183 0.0305 -0.0168 123 PHE A CD2 1640 C CE1 . PHE A 115 ? 0.1989 0.1361 0.2162 -0.0195 0.0016 -0.0170 123 PHE A CE1 1641 C CE2 . PHE A 115 ? 0.1824 0.1661 0.2366 -0.0092 0.0052 -0.0162 123 PHE A CE2 1642 C CZ . PHE A 115 ? 0.2058 0.1562 0.2234 -0.0235 -0.0062 -0.0260 123 PHE A CZ 1652 N N . PRO A 116 ? 0.2505 0.2049 0.2597 -0.0731 0.0229 -0.0105 124 PRO A N 1653 C CA . PRO A 116 ? 0.2702 0.1952 0.2924 -0.0781 0.0320 0.0206 124 PRO A CA 1654 C C . PRO A 116 ? 0.2933 0.2094 0.3197 -0.0779 0.0286 0.0395 124 PRO A C 1655 O O . PRO A 116 ? 0.3569 0.2599 0.3378 -0.0486 0.0254 0.0750 124 PRO A O 1656 C CB . PRO A 116 ? 0.2752 0.2215 0.3057 -0.0688 0.0285 0.0278 124 PRO A CB 1657 C CG . PRO A 116 ? 0.2796 0.2220 0.2978 -0.1135 0.0016 0.0335 124 PRO A CG 1658 C CD . PRO A 116 ? 0.2573 0.2186 0.2892 -0.0772 0.0067 0.0010 124 PRO A CD 1666 N N . ASP A 117 ? 0.2950 0.1622 0.3336 -0.0933 0.0218 0.0083 125 ASP A N 1667 C CA . ASP A 117 ? 0.3276 0.1765 0.3490 -0.0725 0.0042 0.0227 125 ASP A CA 1668 C C . ASP A 117 ? 0.3011 0.1849 0.3379 -0.0445 0.0056 0.0282 125 ASP A C 1669 O O . ASP A 117 ? 0.3109 0.2035 0.3881 -0.0559 0.0229 0.0155 125 ASP A O 1670 C CB . ASP A 117 ? 0.3646 0.2131 0.3976 -0.0662 -0.0069 0.0188 125 ASP A CB 1671 C CG . ASP A 117 ? 0.4440 0.3047 0.4414 -0.0647 0.0110 -0.0053 125 ASP A CG 1672 O OD1 . ASP A 117 ? 0.4660 0.2801 0.4619 -0.0915 0.0352 0.0104 125 ASP A OD1 1673 O OD2 . ASP A 117 ? 0.4914 0.3595 0.4715 -0.0812 0.0000 -0.0408 125 ASP A OD2 1678 N N . THR A 118 ? 0.2733 0.1848 0.2617 -0.0689 -0.0262 0.0152 126 THR A N 1679 C CA . THR A 118 ? 0.2584 0.1714 0.2328 -0.0577 -0.0182 -0.0108 126 THR A CA 1680 C C . THR A 118 ? 0.2785 0.1833 0.2281 -0.0781 -0.0047 0.0047 126 THR A C 1681 O O . THR A 118 ? 0.2998 0.2617 0.2395 -0.1092 0.0194 -0.0285 126 THR A O 1682 C CB . THR A 118 ? 0.2083 0.1640 0.2306 -0.0188 -0.0164 -0.0145 126 THR A CB 1683 O OG1 . THR A 118 ? 0.2247 0.1935 0.2218 -0.0276 -0.0041 -0.0218 126 THR A OG1 1684 C CG2 . THR A 118 ? 0.1906 0.2121 0.2275 -0.0220 -0.0146 -0.0050 126 THR A CG2 1692 N N . LYS A 119 ? 0.3069 0.1562 0.2221 -0.0695 -0.0215 0.0101 127 LYS A N 1693 C CA . LYS A 119 ? 0.3440 0.1588 0.2360 -0.0805 -0.0469 0.0178 127 LYS A CA 1694 C C . LYS A 119 ? 0.2454 0.1809 0.1980 -0.0637 -0.0288 0.0078 127 LYS A C 1695 O O . LYS A 119 ? 0.2233 0.1806 0.1967 -0.0419 -0.0099 0.0075 127 LYS A O 1696 C CB . LYS A 119 ? 0.4426 0.2306 0.2917 -0.0566 -0.0768 0.0222 127 LYS A CB 1697 C CG . LYS A 119 ? 0.4753 0.2925 0.3240 -0.0787 -0.0876 0.0027 127 LYS A CG 1698 C CD . LYS A 119 ? 0.5031 0.3964 0.3210 -0.0827 -0.0778 -0.0102 127 LYS A CD 1699 C CE . LYS A 119 ? 0.5306 0.4337 0.3322 -0.0794 -0.0790 -0.0185 127 LYS A CE 1700 N NZ . LYS A 119 ? 0.5725 0.4749 0.3681 -0.0532 -0.0606 0.0036 127 LYS A NZ 1714 N N . VAL A 120 ? 0.2325 0.1623 0.1739 -0.0723 -0.0120 -0.0026 128 VAL A N 1715 C CA . VAL A 120 ? 0.1665 0.1722 0.1705 -0.0475 -0.0086 -0.0123 128 VAL A CA 1716 C C . VAL A 120 ? 0.1558 0.1932 0.1704 -0.0427 0.0244 -0.0258 128 VAL A C 1717 O O . VAL A 120 ? 0.1860 0.2114 0.1757 -0.0538 0.0112 0.0118 128 VAL A O 1718 C CB . VAL A 120 ? 0.1580 0.2338 0.1717 -0.0301 0.0064 -0.0209 128 VAL A CB 1719 C CG1 . VAL A 120 ? 0.1749 0.2299 0.1867 -0.0037 -0.0022 -0.0175 128 VAL A CG1 1720 C CG2 . VAL A 120 ? 0.1548 0.2752 0.1843 -0.0482 -0.0005 -0.0136 128 VAL A CG2 1730 N N . TYR A 121 ? 0.1491 0.1628 0.1608 -0.0258 0.0023 -0.0117 129 TYR A N 1731 C CA . TYR A 121 ? 0.1331 0.1494 0.1629 -0.0357 -0.0093 -0.0023 129 TYR A CA 1732 C C . TYR A 121 ? 0.1474 0.1548 0.1457 -0.0128 -0.0082 -0.0124 129 TYR A C 1733 O O . TYR A 121 ? 0.1515 0.1721 0.1475 0.0061 0.0149 -0.0054 129 TYR A O 1734 C CB . TYR A 121 ? 0.1340 0.1771 0.1684 -0.0247 -0.0014 -0.0078 129 TYR A CB 1735 C CG . TYR A 121 ? 0.1854 0.1805 0.1881 0.0051 -0.0126 -0.0078 129 TYR A CG 1736 C CD1 . TYR A 121 ? 0.3663 0.1938 0.2003 0.0714 0.0218 -0.0133 129 TYR A CD1 1737 C CD2 . TYR A 121 ? 0.2121 0.1770 0.1902 0.0134 -0.0158 -0.0156 129 TYR A CD2 1738 C CE1 . TYR A 121 ? 0.4228 0.1906 0.2260 0.0637 0.0405 0.0187 129 TYR A CE1 1739 C CE2 . TYR A 121 ? 0.2600 0.1714 0.2058 0.0306 -0.0262 -0.0129 129 TYR A CE2 1740 C CZ . TYR A 121 ? 0.3451 0.1823 0.2330 0.0438 0.0009 -0.0020 129 TYR A CZ 1741 O OH . TYR A 121 ? 0.3653 0.1780 0.2559 0.0679 0.0146 0.0103 129 TYR A OH 1751 N N . ALA A 122 ? 0.1648 0.1660 0.1551 0.0100 0.0203 0.0154 130 ALA A N 1752 C CA . ALA A 122 ? 0.1389 0.1503 0.1598 0.0004 0.0084 -0.0135 130 ALA A CA 1753 C C . ALA A 122 ? 0.1323 0.1669 0.1542 -0.0123 0.0101 -0.0083 130 ALA A C 1754 O O . ALA A 122 ? 0.1357 0.1976 0.1476 -0.0122 -0.0006 0.0077 130 ALA A O 1755 C CB . ALA A 122 ? 0.1605 0.1528 0.1840 -0.0145 0.0016 -0.0344 130 ALA A CB 1761 N N . ALA A 123 ? 0.1505 0.1524 0.1479 -0.0023 0.0167 -0.0151 131 ALA A N 1762 C CA . ALA A 123 ? 0.1409 0.1806 0.1430 -0.0166 0.0159 -0.0101 131 ALA A CA 1763 C C . ALA A 123 ? 0.1293 0.1440 0.1473 -0.0084 -0.0010 -0.0137 131 ALA A C 1764 O O . ALA A 123 ? 0.1482 0.1825 0.1451 0.0019 -0.0167 -0.0180 131 ALA A O 1765 C CB . ALA A 123 ? 0.1539 0.1694 0.1510 -0.0028 0.0130 -0.0039 131 ALA A CB 1771 N N . LEU A 124 ? 0.1180 0.1781 0.1387 -0.0081 0.0087 -0.0078 132 LEU A N 1772 C CA . LEU A 124 ? 0.1093 0.1723 0.1475 0.0028 0.0164 -0.0168 132 LEU A CA 1773 C C . LEU A 124 ? 0.1237 0.1802 0.1424 -0.0125 0.0106 -0.0237 132 LEU A C 1774 O O . LEU A 124 ? 0.1173 0.1784 0.1387 -0.0080 0.0069 -0.0014 132 LEU A O 1775 C CB . LEU A 124 ? 0.1455 0.1733 0.1620 0.0019 0.0182 -0.0068 132 LEU A CB 1776 C CG . LEU A 124 ? 0.1529 0.2122 0.1600 -0.0019 0.0450 0.0232 132 LEU A CG 1777 C CD1 . LEU A 124 ? 0.1922 0.2453 0.1494 0.0226 0.0308 0.0306 132 LEU A CD1 1778 C CD2 . LEU A 124 ? 0.1352 0.2234 0.1891 -0.0155 0.0333 0.0202 132 LEU A CD2 1790 N N . GLY A 125 ? 0.1283 0.1733 0.1451 -0.0066 0.0067 -0.0153 133 GLY A N 1791 C CA . GLY A 125 ? 0.1203 0.1848 0.1518 0.0009 0.0209 -0.0135 133 GLY A CA 1792 C C . GLY A 125 ? 0.1017 0.1779 0.1393 -0.0078 0.0083 0.0059 133 GLY A C 1793 O O . GLY A 125 ? 0.1147 0.1696 0.1461 -0.0061 0.0134 -0.0059 133 GLY A O 1797 N N . ASN A 126 ? 0.1096 0.1699 0.1338 -0.0113 0.0215 -0.0052 134 ASN A N 1798 C CA . ASN A 126 ? 0.1175 0.1572 0.1467 0.0054 0.0131 -0.0133 134 ASN A CA 1799 C C . ASN A 126 ? 0.1161 0.1475 0.1536 0.0152 0.0199 -0.0042 134 ASN A C 1800 O O . ASN A 126 ? 0.1313 0.1786 0.1598 0.0081 0.0180 -0.0284 134 ASN A O 1801 C CB . ASN A 126 ? 0.1372 0.1629 0.1702 0.0095 0.0159 -0.0106 134 ASN A CB 1802 C CG . ASN A 126 ? 0.1096 0.1710 0.1650 0.0112 0.0134 -0.0323 134 ASN A CG 1803 O OD1 . ASN A 126 ? 0.1630 0.1747 0.1952 -0.0025 0.0752 -0.0349 134 ASN A OD1 1804 N ND2 . ASN A 126 ? 0.1268 0.1795 0.1670 0.0078 0.0005 -0.0219 134 ASN A ND2 1811 N N . HIS A 127 ? 0.1180 0.1796 0.1470 -0.0005 -0.0034 -0.0005 135 HIS A N 1812 C CA . HIS A 127 ? 0.1230 0.1987 0.1561 -0.0054 -0.0079 -0.0187 135 HIS A CA 1813 C C . HIS A 127 ? 0.1172 0.2084 0.1610 -0.0050 -0.0014 -0.0178 135 HIS A C 1814 O O . HIS A 127 ? 0.1318 0.2458 0.1657 0.0015 0.0101 -0.0015 135 HIS A O 1815 C CB . HIS A 127 ? 0.1164 0.2083 0.1611 0.0211 0.0014 -0.0083 135 HIS A CB 1816 C CG . HIS A 127 ? 0.1429 0.1991 0.1620 0.0277 -0.0104 -0.0091 135 HIS A CG 1817 N ND1 . HIS A 127 ? 0.1765 0.2291 0.1851 0.0260 -0.0059 -0.0011 135 HIS A ND1 1818 C CD2 . HIS A 127 ? 0.1386 0.1786 0.1791 0.0109 0.0008 0.0029 135 HIS A CD2 1819 C CE1 . HIS A 127 ? 0.1922 0.2024 0.1950 0.0184 0.0133 0.0099 135 HIS A CE1 1820 N NE2 . HIS A 127 ? 0.1641 0.1969 0.1778 0.0107 -0.0040 -0.0032 135 HIS A NE2 1828 N N . ASP A 128 ? 0.1141 0.2040 0.1640 0.0111 0.0054 -0.0061 136 ASP A N 1829 C CA . ASP A 128 ? 0.1249 0.1916 0.1475 -0.0028 0.0135 -0.0054 136 ASP A CA 1830 C C . ASP A 128 ? 0.1516 0.2177 0.1530 0.0039 0.0151 -0.0256 136 ASP A C 1831 O O . ASP A 128 ? 0.1653 0.2330 0.1511 -0.0080 0.0160 -0.0081 136 ASP A O 1832 C CB . ASP A 128 ? 0.1252 0.2157 0.1482 -0.0098 0.0107 0.0224 136 ASP A CB 1833 C CG . ASP A 128 ? 0.1214 0.2219 0.1416 -0.0066 0.0143 0.0077 136 ASP A CG 1834 O OD1 . ASP A 128 ? 0.1395 0.2317 0.1487 0.0042 0.0134 -0.0105 136 ASP A OD1 1835 O OD2 . ASP A 128 ? 0.1271 0.2110 0.1599 -0.0011 0.0084 -0.0064 136 ASP A OD2 1840 N N . PHE A 129 ? 0.1526 0.2021 0.1575 -0.0058 0.0154 -0.0217 137 PHE A N 1841 C CA . PHE A 129 ? 0.1454 0.2213 0.1501 -0.0032 0.0053 -0.0287 137 PHE A CA 1842 C C . PHE A 129 ? 0.1459 0.2244 0.1665 -0.0034 0.0191 -0.0410 137 PHE A C 1843 O O . PHE A 129 ? 0.1761 0.2573 0.1624 0.0335 0.0293 -0.0172 137 PHE A O 1844 C CB . PHE A 129 ? 0.1394 0.2381 0.1655 0.0012 0.0283 -0.0055 137 PHE A CB 1845 C CG . PHE A 129 ? 0.1480 0.2395 0.1734 0.0236 0.0162 -0.0264 137 PHE A CG 1846 C CD1 . PHE A 129 ? 0.1463 0.2635 0.1877 0.0015 -0.0017 -0.0204 137 PHE A CD1 1847 C CD2 . PHE A 129 ? 0.1576 0.2566 0.1697 0.0041 0.0148 -0.0150 137 PHE A CD2 1848 C CE1 . PHE A 129 ? 0.1635 0.2734 0.1848 0.0038 0.0053 0.0024 137 PHE A CE1 1849 C CE2 . PHE A 129 ? 0.1865 0.2897 0.1800 -0.0077 -0.0011 -0.0250 137 PHE A CE2 1850 C CZ . PHE A 129 ? 0.1790 0.2872 0.1822 -0.0069 -0.0124 -0.0140 137 PHE A CZ 1860 N N . HIS A 130 ? 0.1562 0.2454 0.1684 0.0380 0.0278 -0.0279 138 HIS A N 1861 C CA . HIS A 130 ? 0.1503 0.2601 0.1955 0.0016 0.0229 -0.0369 138 HIS A CA 1862 C C . HIS A 130 ? 0.1783 0.2676 0.2061 0.0148 0.0351 -0.0229 138 HIS A C 1863 O O . HIS A 130 ? 0.1928 0.3184 0.1993 0.0214 0.0574 -0.0137 138 HIS A O 1864 C CB . HIS A 130 ? 0.1402 0.2913 0.2401 0.0063 0.0130 -0.0378 138 HIS A CB 1865 C CG . HIS A 130 ? 0.1758 0.3073 0.2855 0.0210 0.0483 -0.0575 138 HIS A CG 1866 N ND1 . HIS A 130 ? 0.2318 0.3210 0.3406 0.0634 0.0991 -0.0631 138 HIS A ND1 1867 C CD2 . HIS A 130 ? 0.2055 0.3601 0.3277 -0.0043 0.0751 -0.0239 138 HIS A CD2 1868 C CE1 . HIS A 130 ? 0.2492 0.3619 0.3666 0.0560 0.0899 -0.0458 138 HIS A CE1 1869 N NE2 . HIS A 130 ? 0.2060 0.3592 0.3616 0.0652 0.0511 -0.0092 138 HIS A NE2 1877 N N . PRO A 131 ? 0.1697 0.3023 0.2100 0.0283 0.0150 -0.0644 139 PRO A N 1878 C CA . PRO A 131 ? 0.1530 0.2688 0.2342 0.0046 0.0067 -0.0642 139 PRO A CA 1879 C C . PRO A 131 ? 0.1600 0.2476 0.2075 -0.0105 -0.0078 -0.0476 139 PRO A C 1880 O O . PRO A 131 ? 0.1580 0.2390 0.1866 0.0213 0.0009 -0.0434 139 PRO A O 1881 C CB . PRO A 131 ? 0.2237 0.3001 0.2672 0.0326 0.0383 -0.0623 139 PRO A CB 1882 C CG . PRO A 131 ? 0.2725 0.3445 0.2384 0.0207 -0.0135 -0.0594 139 PRO A CG 1883 C CD . PRO A 131 ? 0.2415 0.3476 0.2134 0.0333 0.0042 -0.0732 139 PRO A CD 1891 N N . LYS A 132 ? 0.1798 0.2618 0.1997 0.0177 -0.0246 -0.0292 140 LYS A N 1892 C CA . LYS A 132 ? 0.2008 0.2316 0.2008 -0.0035 -0.0169 -0.0114 140 LYS A CA 1893 C C . LYS A 132 ? 0.1700 0.2261 0.1741 0.0067 0.0057 -0.0328 140 LYS A C 1894 O O . LYS A 132 ? 0.1620 0.2188 0.1789 0.0192 -0.0090 -0.0311 140 LYS A O 1895 C CB . LYS A 132 ? 0.2312 0.2677 0.2258 0.0191 -0.0666 -0.0201 140 LYS A CB 1896 C CG . LYS A 132 ? 0.3625 0.3896 0.2666 0.0312 -0.0487 0.0200 140 LYS A CG 1897 C CD . LYS A 132 ? 0.4473 0.4453 0.3121 -0.0129 -0.0139 0.0384 140 LYS A CD 1898 C CE . LYS A 132 ? 0.5108 0.4895 0.3563 -0.0074 0.0239 0.0572 140 LYS A CE 1899 N NZ . LYS A 132 ? 0.5535 0.5309 0.3802 0.0195 0.0376 0.0422 140 LYS A NZ 1913 N N . ASN A 133 ? 0.1804 0.2030 0.1661 0.0123 0.0055 -0.0192 141 ASN A N 1914 C CA . ASN A 133 ? 0.1747 0.1915 0.1727 0.0288 0.0145 -0.0241 141 ASN A CA 1915 C C . ASN A 133 ? 0.1722 0.2072 0.1734 0.0277 0.0137 -0.0302 141 ASN A C 1916 O O . ASN A 133 ? 0.1768 0.2152 0.1698 0.0215 0.0155 -0.0252 141 ASN A O 1917 C CB . ASN A 133 ? 0.1730 0.2017 0.1747 0.0278 -0.0020 -0.0308 141 ASN A CB 1918 C CG . ASN A 133 ? 0.2379 0.1848 0.1795 0.0196 -0.0025 -0.0271 141 ASN A CG 1919 O OD1 . ASN A 133 ? 0.2608 0.1820 0.1781 0.0024 0.0135 -0.0368 141 ASN A OD1 1920 N ND2 . ASN A 133 ? 0.3331 0.2210 0.2016 0.0559 -0.0058 -0.0264 141 ASN A ND2 1927 N N . GLN A 134 ? 0.1780 0.2277 0.1564 0.0215 0.0025 -0.0448 142 GLN A N 1928 C CA . GLN A 134 ? 0.1703 0.2440 0.1507 0.0240 0.0182 -0.0348 142 GLN A CA 1929 C C . GLN A 134 ? 0.1289 0.2699 0.1584 -0.0030 0.0330 -0.0250 142 GLN A C 1930 O O . GLN A 134 ? 0.1577 0.2687 0.1691 0.0296 0.0243 -0.0289 142 GLN A O 1931 C CB . GLN A 134 ? 0.1804 0.2361 0.1727 0.0483 0.0122 -0.0451 142 GLN A CB 1932 C CG . GLN A 134 ? 0.1921 0.2523 0.1742 0.0434 -0.0066 -0.0601 142 GLN A CG 1933 C CD . GLN A 134 ? 0.1943 0.2303 0.1909 0.0354 0.0062 -0.0391 142 GLN A CD 1934 O OE1 . GLN A 134 ? 0.1944 0.2411 0.2090 0.0384 0.0062 -0.0509 142 GLN A OE1 1935 N NE2 . GLN A 134 ? 0.2127 0.2675 0.1979 0.0505 0.0034 -0.0328 142 GLN A NE2 1944 N N . PHE A 135 ? 0.1329 0.2258 0.1652 0.0104 0.0403 -0.0302 143 PHE A N 1945 C CA . PHE A 135 ? 0.1415 0.2214 0.1694 0.0002 0.0151 -0.0049 143 PHE A CA 1946 C C . PHE A 135 ? 0.1450 0.2525 0.1643 -0.0046 0.0155 -0.0267 143 PHE A C 1947 O O . PHE A 135 ? 0.1518 0.2436 0.1663 0.0056 -0.0013 -0.0236 143 PHE A O 1948 C CB . PHE A 135 ? 0.1341 0.2041 0.1726 -0.0057 0.0199 -0.0164 143 PHE A CB 1949 C CG . PHE A 135 ? 0.1232 0.2103 0.1437 0.0026 0.0077 -0.0071 143 PHE A CG 1950 C CD1 . PHE A 135 ? 0.1383 0.2277 0.1645 0.0220 0.0196 -0.0207 143 PHE A CD1 1951 C CD2 . PHE A 135 ? 0.1381 0.2099 0.1451 0.0110 0.0088 -0.0122 143 PHE A CD2 1952 C CE1 . PHE A 135 ? 0.1464 0.2425 0.1529 0.0314 0.0220 -0.0081 143 PHE A CE1 1953 C CE2 . PHE A 135 ? 0.1544 0.2348 0.1337 0.0057 0.0222 -0.0112 143 PHE A CE2 1954 C CZ . PHE A 135 ? 0.1303 0.2635 0.1430 0.0234 0.0254 -0.0149 143 PHE A CZ 1964 N N . PRO A 136 ? 0.1393 0.2480 0.1703 0.0118 0.0131 -0.0100 144 PRO A N 1965 C CA . PRO A 136 ? 0.1779 0.2652 0.1514 0.0244 0.0215 0.0039 144 PRO A CA 1966 C C . PRO A 136 ? 0.1402 0.2602 0.1455 -0.0056 0.0217 -0.0097 144 PRO A C 1967 O O . PRO A 136 ? 0.1610 0.2669 0.1534 0.0040 0.0010 -0.0136 144 PRO A O 1968 C CB . PRO A 136 ? 0.1779 0.3266 0.1926 0.0557 0.0570 0.0110 144 PRO A CB 1969 C CG . PRO A 136 ? 0.2020 0.3088 0.2068 0.0018 0.0558 0.0043 144 PRO A CG 1970 C CD . PRO A 136 ? 0.1479 0.2409 0.1844 -0.0038 0.0267 -0.0014 144 PRO A CD 1978 N N . ALA A 137 ? 0.1470 0.2688 0.1764 0.0027 0.0065 -0.0062 145 ALA A N 1979 C CA . ALA A 137 ? 0.1461 0.2818 0.2012 -0.0240 -0.0002 0.0093 145 ALA A CA 1980 C C . ALA A 137 ? 0.1526 0.3209 0.1900 -0.0332 -0.0183 0.0251 145 ALA A C 1981 O O . ALA A 137 ? 0.2041 0.4133 0.2783 -0.0619 -0.0505 0.0826 145 ALA A O 1982 C CB . ALA A 137 ? 0.1554 0.3251 0.2396 -0.0326 0.0245 0.0295 145 ALA A CB 1988 N N . GLN A 138 ? 0.1417 0.3169 0.1709 -0.0385 0.0065 0.0118 146 GLN A N 1989 C CA . GLN A 138 ? 0.1762 0.3456 0.1586 -0.0293 -0.0059 -0.0017 146 GLN A CA 1990 C C . GLN A 138 ? 0.1733 0.2889 0.1463 0.0019 0.0185 -0.0189 146 GLN A C 1991 O O . GLN A 138 ? 0.1729 0.2795 0.1382 0.0024 0.0119 -0.0145 146 GLN A O 1992 C CB . GLN A 138 ? 0.1864 0.3900 0.1846 -0.0468 0.0079 -0.0338 146 GLN A CB 1993 C CG . GLN A 138 ? 0.1834 0.4301 0.2247 -0.0225 0.0574 -0.0618 146 GLN A CG 1994 C CD . GLN A 138 ? 0.2459 0.4881 0.2853 -0.0427 0.0330 -0.0645 146 GLN A CD 1995 O OE1 . GLN A 138 ? 0.2611 0.5526 0.2744 -0.0896 0.0400 -0.0802 146 GLN A OE1 1996 N NE2 . GLN A 138 ? 0.2933 0.4924 0.3269 -0.0322 0.0349 -0.0700 146 GLN A NE2 2005 N N . SER A 139 ? 0.1562 0.2884 0.1297 0.0093 0.0075 0.0031 147 SER A N 2006 C CA . SER A 139 ? 0.1432 0.2973 0.1423 -0.0052 0.0143 -0.0104 147 SER A CA 2007 C C . SER A 139 ? 0.1535 0.2787 0.1321 -0.0112 0.0195 -0.0181 147 SER A C 2008 O O . SER A 139 ? 0.1770 0.2929 0.1541 0.0052 0.0121 -0.0420 147 SER A O 2009 C CB . SER A 139 ? 0.1657 0.2784 0.1806 -0.0142 0.0171 -0.0100 147 SER A CB 2010 O OG . SER A 139 ? 0.2555 0.3219 0.2316 -0.0057 0.0224 -0.0037 147 SER A OG 2016 N N . ASN A 140 ? 0.1488 0.2641 0.1333 -0.0014 0.0150 -0.0099 148 ASN A N 2017 C CA . ASN A 140 ? 0.1309 0.2850 0.1365 -0.0139 0.0224 -0.0029 148 ASN A CA 2018 C C . ASN A 140 ? 0.1501 0.2539 0.1469 0.0178 0.0244 -0.0033 148 ASN A C 2019 O O . ASN A 140 ? 0.1512 0.2587 0.1621 0.0068 0.0281 -0.0179 148 ASN A O 2020 C CB . ASN A 140 ? 0.1334 0.2971 0.1483 0.0124 0.0389 -0.0270 148 ASN A CB 2021 C CG . ASN A 140 ? 0.1279 0.2696 0.1425 0.0259 0.0388 -0.0093 148 ASN A CG 2022 O OD1 . ASN A 140 ? 0.1514 0.2798 0.1354 0.0096 0.0111 -0.0139 148 ASN A OD1 2023 N ND2 . ASN A 140 ? 0.1292 0.2843 0.1481 0.0133 0.0227 -0.0166 148 ASN A ND2 2030 N N . ARG A 141 ? 0.1425 0.2557 0.1646 0.0233 0.0321 0.0077 149 ARG A N 2031 C CA . ARG A 141 ? 0.1342 0.2966 0.1586 0.0061 0.0126 -0.0170 149 ARG A CA 2032 C C . ARG A 141 ? 0.1438 0.2534 0.1647 -0.0066 0.0298 0.0032 149 ARG A C 2033 O O . ARG A 141 ? 0.1598 0.2874 0.1796 -0.0250 0.0320 -0.0213 149 ARG A O 2034 C CB . ARG A 141 ? 0.1437 0.3121 0.1613 0.0052 0.0312 -0.0133 149 ARG A CB 2035 C CG . ARG A 141 ? 0.1434 0.3136 0.1646 0.0130 0.0266 -0.0142 149 ARG A CG 2036 C CD . ARG A 141 ? 0.1761 0.3396 0.1770 0.0192 0.0282 0.0083 149 ARG A CD 2037 N NE . ARG A 141 ? 0.2068 0.3373 0.1863 0.0491 0.0456 0.0371 149 ARG A NE 2038 C CZ . ARG A 141 ? 0.2710 0.3108 0.2322 0.0069 0.1098 0.0566 149 ARG A CZ 2039 N NH1 . ARG A 141 ? 0.2806 0.2813 0.2247 0.0086 0.1055 0.0227 149 ARG A NH1 2040 N NH2 . ARG A 141 ? 0.3323 0.3313 0.2701 0.0111 0.1281 0.0734 149 ARG A NH2 2054 N N . ILE A 142 ? 0.1421 0.2388 0.1558 0.0135 0.0195 -0.0096 150 ILE A N 2055 C CA . ILE A 142 ? 0.1513 0.2483 0.1540 0.0128 0.0015 -0.0204 150 ILE A CA 2056 C C . ILE A 142 ? 0.1501 0.2389 0.1310 -0.0159 0.0181 0.0006 150 ILE A C 2057 O O . ILE A 142 ? 0.1432 0.2633 0.1277 -0.0086 0.0197 0.0016 150 ILE A O 2058 C CB . ILE A 142 ? 0.1753 0.2255 0.1812 0.0180 0.0104 -0.0176 150 ILE A CB 2059 C CG1 . ILE A 142 ? 0.2160 0.2629 0.2261 -0.0230 0.0201 0.0242 150 ILE A CG1 2060 C CG2 . ILE A 142 ? 0.1962 0.2444 0.1494 0.0115 0.0182 -0.0034 150 ILE A CG2 2061 C CD1 . ILE A 142 ? 0.2488 0.2628 0.2459 -0.0317 0.0432 0.0260 150 ILE A CD1 2073 N N . TYR A 143 ? 0.1275 0.2554 0.1282 0.0022 0.0048 -0.0117 151 TYR A N 2074 C CA . TYR A 143 ? 0.1189 0.2563 0.1394 0.0038 0.0278 -0.0026 151 TYR A CA 2075 C C . TYR A 143 ? 0.1149 0.2522 0.1476 -0.0215 0.0321 -0.0010 151 TYR A C 2076 O O . TYR A 143 ? 0.1445 0.2499 0.1586 -0.0092 0.0180 -0.0098 151 TYR A O 2077 C CB . TYR A 143 ? 0.1340 0.2437 0.1306 0.0176 0.0214 0.0019 151 TYR A CB 2078 C CG . TYR A 143 ? 0.1327 0.2545 0.1323 0.0020 0.0414 0.0098 151 TYR A CG 2079 C CD1 . TYR A 143 ? 0.1364 0.2342 0.1409 -0.0258 0.0359 -0.0039 151 TYR A CD1 2080 C CD2 . TYR A 143 ? 0.1219 0.2876 0.1319 -0.0050 0.0280 0.0148 151 TYR A CD2 2081 C CE1 . TYR A 143 ? 0.1318 0.2331 0.1270 0.0075 0.0124 0.0049 151 TYR A CE1 2082 C CE2 . TYR A 143 ? 0.1229 0.2708 0.1326 -0.0046 0.0321 -0.0007 151 TYR A CE2 2083 C CZ . TYR A 143 ? 0.1506 0.1905 0.1368 0.0011 0.0158 -0.0140 151 TYR A CZ 2084 O OH . TYR A 143 ? 0.1477 0.2382 0.1439 0.0030 0.0247 -0.0146 151 TYR A OH 2094 N N . ASN A 144 ? 0.1220 0.2542 0.1550 -0.0161 0.0235 0.0129 152 ASN A N 2095 C CA . ASN A 144 ? 0.1365 0.2971 0.1522 -0.0171 0.0287 0.0106 152 ASN A CA 2096 C C . ASN A 144 ? 0.1472 0.2747 0.1606 -0.0422 0.0264 0.0183 152 ASN A C 2097 O O . ASN A 144 ? 0.1583 0.2659 0.1917 -0.0178 0.0067 0.0234 152 ASN A O 2098 C CB . ASN A 144 ? 0.1644 0.3055 0.1505 -0.0111 0.0312 0.0209 152 ASN A CB 2099 C CG . ASN A 144 ? 0.2250 0.3742 0.1660 0.0682 0.0419 0.0069 152 ASN A CG 2100 O OD1 . ASN A 144 ? 0.2458 0.4269 0.1809 0.0728 0.0031 -0.0080 152 ASN A OD1 2101 N ND2 . ASN A 144 ? 0.3355 0.4435 0.1795 0.0936 -0.0040 -0.0049 152 ASN A ND2 2108 N N . GLN A 145 ? 0.1357 0.2837 0.1556 -0.0225 0.0304 0.0164 153 GLN A N 2109 C CA . GLN A 145 ? 0.1361 0.3159 0.1630 -0.0247 -0.0153 0.0129 153 GLN A CA 2110 C C . GLN A 145 ? 0.1700 0.2540 0.1606 -0.0143 0.0058 0.0090 153 GLN A C 2111 O O . GLN A 145 ? 0.1531 0.2488 0.1760 -0.0249 0.0043 0.0069 153 GLN A O 2112 C CB . GLN A 145 ? 0.1470 0.3406 0.1851 -0.0130 0.0014 0.0073 153 GLN A CB 2113 C CG . GLN A 145 ? 0.2035 0.4248 0.2381 -0.0370 0.0066 0.0305 153 GLN A CG 2114 C CD . GLN A 145 ? 0.2212 0.4870 0.2798 -0.1082 0.0237 0.0252 153 GLN A CD 2115 O OE1 . GLN A 145 ? 0.2577 0.4758 0.3306 -0.0801 0.0447 0.0513 153 GLN A OE1 2116 N NE2 . GLN A 145 ? 0.3025 0.5202 0.2955 -0.1853 0.0916 -0.0230 153 GLN A NE2 2125 N N . VAL A 146 ? 0.1561 0.2280 0.1451 -0.0153 0.0046 -0.0080 154 VAL A N 2126 C CA . VAL A 146 ? 0.1424 0.2246 0.1423 -0.0075 0.0181 -0.0008 154 VAL A CA 2127 C C . VAL A 146 ? 0.1408 0.2108 0.1563 -0.0126 0.0011 -0.0021 154 VAL A C 2128 O O . VAL A 146 ? 0.1589 0.2246 0.1737 -0.0237 0.0135 -0.0011 154 VAL A O 2129 C CB . VAL A 146 ? 0.1160 0.2381 0.1659 0.0046 0.0220 0.0108 154 VAL A CB 2130 C CG1 . VAL A 146 ? 0.1591 0.1926 0.1622 -0.0061 0.0367 0.0156 154 VAL A CG1 2131 C CG2 . VAL A 146 ? 0.1575 0.2726 0.1607 -0.0017 0.0058 0.0219 154 VAL A CG2 2141 N N . ALA A 147 ? 0.1466 0.2224 0.1568 -0.0138 0.0143 0.0012 155 ALA A N 2142 C CA . ALA A 147 ? 0.1646 0.2040 0.1604 -0.0136 0.0238 0.0097 155 ALA A CA 2143 C C . ALA A 147 ? 0.1602 0.2341 0.1748 -0.0232 0.0285 0.0127 155 ALA A C 2144 O O . ALA A 147 ? 0.1718 0.2441 0.2092 -0.0210 0.0092 0.0215 155 ALA A O 2145 C CB . ALA A 147 ? 0.1899 0.2405 0.1721 -0.0246 0.0029 0.0109 155 ALA A CB 2151 N N . GLU A 148 ? 0.1758 0.2401 0.1620 -0.0484 0.0235 0.0221 156 GLU A N 2152 C CA . GLU A 148 ? 0.2006 0.2384 0.1783 -0.0432 0.0249 0.0253 156 GLU A CA 2153 C C . GLU A 148 ? 0.1851 0.2345 0.1897 -0.0332 0.0200 0.0270 156 GLU A C 2154 O O . GLU A 148 ? 0.2425 0.2454 0.1935 -0.0524 0.0198 0.0347 156 GLU A O 2155 C CB . GLU A 148 ? 0.2295 0.2727 0.1842 -0.0730 0.0382 0.0150 156 GLU A CB 2156 C CG . GLU A 148 ? 0.2541 0.3291 0.2202 -0.0663 0.0393 0.0164 156 GLU A CG 2157 C CD . GLU A 148 ? 0.3188 0.4036 0.2353 -0.0942 0.0304 0.0295 156 GLU A CD 2158 O OE1 . GLU A 148 ? 0.4074 0.4395 0.2594 -0.0778 0.0467 0.0442 156 GLU A OE1 2159 O OE2 . GLU A 148 ? 0.3680 0.4754 0.2767 -0.0407 0.0103 0.0404 156 GLU A OE2 2166 N N . LEU A 149 ? 0.1673 0.2444 0.1818 -0.0377 0.0197 0.0197 157 LEU A N 2167 C CA . LEU A 149 ? 0.1741 0.2440 0.1759 -0.0685 0.0057 0.0112 157 LEU A CA 2168 C C . LEU A 149 ? 0.1894 0.2312 0.1565 -0.0419 -0.0104 0.0189 157 LEU A C 2169 O O . LEU A 149 ? 0.1665 0.2650 0.1760 -0.0550 -0.0165 0.0114 157 LEU A O 2170 C CB . LEU A 149 ? 0.1707 0.2440 0.1853 -0.0486 -0.0110 0.0112 157 LEU A CB 2171 C CG . LEU A 149 ? 0.1647 0.2680 0.1987 -0.0379 -0.0118 0.0182 157 LEU A CG 2172 C CD1 . LEU A 149 ? 0.1989 0.2590 0.2020 -0.0312 -0.0269 0.0108 157 LEU A CD1 2173 C CD2 . LEU A 149 ? 0.1886 0.3001 0.2193 -0.0277 -0.0023 0.0282 157 LEU A CD2 2185 N N . TRP A 150 ? 0.1906 0.2158 0.1456 -0.0322 0.0037 -0.0053 158 TRP A N 2186 C CA . TRP A 150 ? 0.1856 0.2050 0.1573 -0.0263 0.0183 0.0201 158 TRP A CA 2187 C C . TRP A 150 ? 0.1830 0.2094 0.1747 -0.0342 0.0200 -0.0009 158 TRP A C 2188 O O . TRP A 150 ? 0.1833 0.2335 0.1933 -0.0380 -0.0072 0.0197 158 TRP A O 2189 C CB . TRP A 150 ? 0.1600 0.2261 0.1535 -0.0344 0.0001 0.0137 158 TRP A CB 2190 C CG . TRP A 150 ? 0.1448 0.2009 0.1557 -0.0071 0.0074 0.0122 158 TRP A CG 2191 C CD1 . TRP A 150 ? 0.1570 0.2143 0.1548 -0.0222 0.0099 0.0096 158 TRP A CD1 2192 C CD2 . TRP A 150 ? 0.1373 0.1956 0.1402 -0.0042 -0.0051 0.0046 158 TRP A CD2 2193 N NE1 . TRP A 150 ? 0.1311 0.2210 0.1525 -0.0241 -0.0007 0.0075 158 TRP A NE1 2194 C CE2 . TRP A 150 ? 0.1199 0.1824 0.1464 -0.0037 0.0157 -0.0082 158 TRP A CE2 2195 C CE3 . TRP A 150 ? 0.1324 0.1966 0.1275 0.0023 -0.0054 -0.0040 158 TRP A CE3 2196 C CZ2 . TRP A 150 ? 0.1280 0.1661 0.1527 -0.0072 0.0159 -0.0058 158 TRP A CZ2 2197 C CZ3 . TRP A 150 ? 0.1513 0.1953 0.1292 -0.0218 0.0117 -0.0042 158 TRP A CZ3 2198 C CH2 . TRP A 150 ? 0.1327 0.1843 0.1442 -0.0237 0.0190 0.0103 158 TRP A CH2 2209 N N . ARG A 151 ? 0.2032 0.2240 0.1925 -0.0334 0.0024 0.0234 159 ARG A N 2210 C CA . ARG A 151 ? 0.2550 0.2166 0.2083 -0.0442 0.0062 0.0360 159 ARG A CA 2211 C C . ARG A 151 ? 0.2392 0.2190 0.2236 -0.0349 0.0171 0.0358 159 ARG A C 2212 O O . ARG A 151 ? 0.2427 0.2119 0.2372 -0.0254 0.0270 0.0288 159 ARG A O 2213 C CB . ARG A 151 ? 0.3530 0.2500 0.2198 -0.0732 0.0418 0.0198 159 ARG A CB 2214 C CG . ARG A 151 ? 0.4398 0.3356 0.2764 -0.0845 0.0254 0.0271 159 ARG A CG 2215 C CD . ARG A 151 ? 0.5245 0.4032 0.3180 -0.1040 0.0275 0.0168 159 ARG A CD 2216 N NE . ARG A 151 ? 0.5902 0.4480 0.3719 -0.0985 0.0413 0.0088 159 ARG A NE 2217 C CZ . ARG A 151 ? 0.6296 0.4787 0.3990 -0.0927 0.0494 0.0211 159 ARG A CZ 2218 N NH1 . ARG A 151 ? 0.6268 0.4550 0.4089 -0.1063 0.0534 0.0337 159 ARG A NH1 2219 N NH2 . ARG A 151 ? 0.6667 0.5309 0.4147 -0.0749 0.0395 -0.0057 159 ARG A NH2 2233 N N . PRO A 152 ? 0.2491 0.2087 0.2380 -0.0579 0.0177 0.0168 160 PRO A N 2234 C CA . PRO A 152 ? 0.2930 0.2295 0.2545 -0.0869 0.0347 0.0016 160 PRO A CA 2235 C C . PRO A 152 ? 0.3299 0.1967 0.2599 -0.0656 0.0585 0.0002 160 PRO A C 2236 O O . PRO A 152 ? 0.3668 0.2074 0.3087 -0.0718 0.0643 0.0045 160 PRO A O 2237 C CB . PRO A 152 ? 0.3058 0.3108 0.2695 -0.0862 0.0144 -0.0134 160 PRO A CB 2238 C CG . PRO A 152 ? 0.2961 0.3233 0.2721 -0.0620 -0.0443 0.0078 160 PRO A CG 2239 C CD . PRO A 152 ? 0.2728 0.2577 0.2484 -0.0756 -0.0114 0.0315 160 PRO A CD 2247 N N . TRP A 153 ? 0.3246 0.1903 0.2515 -0.0689 0.0843 0.0273 161 TRP A N 2248 C CA . TRP A 153 ? 0.3282 0.1938 0.2532 -0.0548 0.1008 0.0236 161 TRP A CA 2249 C C . TRP A 153 ? 0.2907 0.2302 0.2938 -0.0330 0.1016 0.0458 161 TRP A C 2250 O O . TRP A 153 ? 0.2899 0.2780 0.3153 0.0068 0.1100 0.0591 161 TRP A O 2251 C CB . TRP A 153 ? 0.3095 0.2423 0.2263 -0.0784 0.0717 0.0193 161 TRP A CB 2252 C CG . TRP A 153 ? 0.2909 0.2948 0.2330 -0.1116 0.0562 -0.0273 161 TRP A CG 2253 C CD1 . TRP A 153 ? 0.3320 0.3717 0.2628 -0.1504 0.0761 -0.0299 161 TRP A CD1 2254 C CD2 . TRP A 153 ? 0.2261 0.3474 0.2204 -0.1062 0.0408 -0.0303 161 TRP A CD2 2255 N NE1 . TRP A 153 ? 0.3031 0.3906 0.2572 -0.1564 0.0683 -0.0628 161 TRP A NE1 2256 C CE2 . TRP A 153 ? 0.2419 0.3931 0.2469 -0.1033 0.0553 -0.0501 161 TRP A CE2 2257 C CE3 . TRP A 153 ? 0.1576 0.3906 0.2194 -0.0233 0.0182 -0.0369 161 TRP A CE3 2258 C CZ2 . TRP A 153 ? 0.1972 0.4117 0.2347 -0.0858 0.0236 -0.0704 161 TRP A CZ2 2259 C CZ3 . TRP A 153 ? 0.1600 0.4163 0.2103 0.0170 0.0136 -0.0467 161 TRP A CZ3 2260 C CH2 . TRP A 153 ? 0.1810 0.4422 0.2308 0.0087 0.0269 -0.0267 161 TRP A CH2 2271 N N . LEU A 154 ? 0.2675 0.2371 0.3048 -0.0488 0.0667 0.0463 162 LEU A N 2272 C CA . LEU A 154 ? 0.2633 0.2399 0.3130 -0.0332 0.0430 0.0497 162 LEU A CA 2273 C C . LEU A 154 ? 0.2516 0.2384 0.3444 -0.0311 0.0547 0.0509 162 LEU A C 2274 O O . LEU A 154 ? 0.2352 0.2686 0.3650 -0.0268 0.0414 0.0614 162 LEU A O 2275 C CB . LEU A 154 ? 0.2053 0.2279 0.2896 -0.0240 0.0150 0.0695 162 LEU A CB 2276 C CG . LEU A 154 ? 0.1769 0.2428 0.2747 -0.0295 -0.0109 0.0685 162 LEU A CG 2277 C CD1 . LEU A 154 ? 0.2032 0.2492 0.2831 -0.0080 -0.0259 0.0442 162 LEU A CD1 2278 C CD2 . LEU A 154 ? 0.1896 0.2502 0.2810 -0.0203 -0.0132 0.0645 162 LEU A CD2 2290 N N . SER A 155 ? 0.2550 0.2196 0.3464 -0.0185 0.0433 0.0393 163 SER A N 2291 C CA . SER A 155 ? 0.2533 0.2360 0.3459 -0.0220 0.0255 0.0724 163 SER A CA 2292 C C . SER A 155 ? 0.2415 0.2222 0.3465 -0.0269 0.0371 0.0837 163 SER A C 2293 O O . SER A 155 ? 0.2170 0.2104 0.3438 -0.0030 0.0235 0.0818 163 SER A O 2294 C CB . SER A 155 ? 0.2495 0.2157 0.3547 -0.0198 0.0412 0.0653 163 SER A CB 2295 O OG . SER A 155 ? 0.2564 0.2078 0.3531 0.0050 0.0305 0.0648 163 SER A OG 2301 N N . ASN A 156 ? 0.2574 0.2459 0.3450 -0.0024 0.0116 0.0972 164 ASN A N 2302 C CA . ASN A 156 ? 0.2822 0.2618 0.3514 -0.0328 0.0221 0.1147 164 ASN A CA 2303 C C . ASN A 156 ? 0.2583 0.2425 0.3193 0.0023 0.0285 0.0983 164 ASN A C 2304 O O . ASN A 156 ? 0.2431 0.2825 0.3179 -0.0060 0.0025 0.1076 164 ASN A O 2305 C CB . ASN A 156 ? 0.3643 0.3108 0.3873 -0.0632 0.0300 0.1307 164 ASN A CB 2306 C CG . ASN A 156 ? 0.4378 0.3702 0.4132 -0.0838 0.0345 0.1346 164 ASN A CG 2307 O OD1 . ASN A 156 ? 0.4226 0.3884 0.4272 -0.1229 0.0365 0.1213 164 ASN A OD1 2308 N ND2 . ASN A 156 ? 0.5033 0.4162 0.4357 -0.0689 0.0329 0.1206 164 ASN A ND2 2315 N N . GLU A 157 ? 0.2411 0.2336 0.2946 0.0251 0.0237 0.0902 165 GLU A N 2316 C CA . GLU A 157 ? 0.2408 0.2606 0.2804 0.0169 0.0208 0.0747 165 GLU A CA 2317 C C . GLU A 157 ? 0.2450 0.2577 0.2377 0.0013 0.0275 0.0567 165 GLU A C 2318 O O . GLU A 157 ? 0.2314 0.2770 0.2112 0.0114 -0.0042 0.0505 165 GLU A O 2319 C CB . GLU A 157 ? 0.2513 0.3023 0.3046 0.0352 0.0170 0.0979 165 GLU A CB 2320 C CG . GLU A 157 ? 0.2467 0.3872 0.3436 0.0307 -0.0062 0.0561 165 GLU A CG 2321 C CD . GLU A 157 ? 0.2916 0.4605 0.3957 0.0190 0.0099 -0.0006 165 GLU A CD 2322 O OE1 . GLU A 157 ? 0.3263 0.4728 0.4510 0.0424 0.0316 -0.0178 165 GLU A OE1 2323 O OE2 . GLU A 157 ? 0.3509 0.5232 0.3864 0.0144 -0.0033 0.0213 165 GLU A OE2 2330 N N . SER A 158 ? 0.2152 0.2227 0.2310 0.0021 0.0294 0.0367 166 SER A N 2331 C CA . SER A 158 ? 0.1818 0.2164 0.2003 -0.0065 0.0004 0.0174 166 SER A CA 2332 C C . SER A 158 ? 0.1878 0.2457 0.1906 -0.0033 0.0236 0.0430 166 SER A C 2333 O O . SER A 158 ? 0.1802 0.2447 0.1896 0.0044 0.0273 0.0415 166 SER A O 2334 C CB . SER A 158 ? 0.1799 0.2197 0.2091 -0.0006 0.0156 0.0131 166 SER A CB 2335 O OG . SER A 158 ? 0.1908 0.2258 0.2141 0.0042 0.0287 0.0123 166 SER A OG 2341 N N . TYR A 159 ? 0.1989 0.2391 0.2004 -0.0015 0.0432 0.0640 167 TYR A N 2342 C CA . TYR A 159 ? 0.1905 0.2498 0.2249 -0.0273 0.0375 0.0755 167 TYR A CA 2343 C C . TYR A 159 ? 0.2147 0.2693 0.2149 -0.0168 0.0338 0.0715 167 TYR A C 2344 O O . TYR A 159 ? 0.2072 0.2683 0.2192 0.0071 0.0237 0.0482 167 TYR A O 2345 C CB . TYR A 159 ? 0.1988 0.2705 0.2820 0.0100 0.0648 0.0773 167 TYR A CB 2346 C CG . TYR A 159 ? 0.2060 0.2993 0.3119 -0.0044 0.0692 0.0752 167 TYR A CG 2347 C CD1 . TYR A 159 ? 0.2024 0.3012 0.3209 -0.0038 0.0643 0.0856 167 TYR A CD1 2348 C CD2 . TYR A 159 ? 0.2427 0.3585 0.3331 -0.0011 0.0894 0.0888 167 TYR A CD2 2349 C CE1 . TYR A 159 ? 0.2084 0.3261 0.3445 0.0050 0.0721 0.0927 167 TYR A CE1 2350 C CE2 . TYR A 159 ? 0.2629 0.3911 0.3486 0.0132 0.1100 0.1093 167 TYR A CE2 2351 C CZ . TYR A 159 ? 0.2487 0.3934 0.3665 0.0236 0.1118 0.1072 167 TYR A CZ 2352 O OH . TYR A 159 ? 0.3052 0.4507 0.3968 0.0529 0.1368 0.1446 167 TYR A OH 2362 N N . ALA A 160 ? 0.2338 0.2760 0.2234 0.0193 0.0274 0.0875 168 ALA A N 2363 C CA . ALA A 160 ? 0.2517 0.3053 0.2153 0.0389 0.0356 0.0784 168 ALA A CA 2364 C C . ALA A 160 ? 0.2211 0.2997 0.1901 0.0488 0.0017 0.0626 168 ALA A C 2365 O O . ALA A 160 ? 0.2325 0.3053 0.1990 0.0426 0.0238 0.0469 168 ALA A O 2366 C CB . ALA A 160 ? 0.2949 0.3353 0.2294 0.0479 0.0436 0.0963 168 ALA A CB 2372 N N . LEU A 161 ? 0.2096 0.2934 0.1849 0.0370 0.0044 0.0288 169 LEU A N 2373 C CA . LEU A 161 ? 0.2197 0.2887 0.1912 0.0214 0.0084 0.0126 169 LEU A CA 2374 C C . LEU A 161 ? 0.1711 0.2692 0.1885 0.0275 0.0072 0.0135 169 LEU A C 2375 O O . LEU A 161 ? 0.1679 0.2888 0.1787 0.0075 0.0054 0.0076 169 LEU A O 2376 C CB . LEU A 161 ? 0.2007 0.2865 0.1964 0.0244 -0.0100 0.0139 169 LEU A CB 2377 C CG . LEU A 161 ? 0.1937 0.3305 0.2198 0.0275 -0.0080 0.0171 169 LEU A CG 2378 C CD1 . LEU A 161 ? 0.1916 0.3455 0.2425 0.0415 0.0297 0.0299 169 LEU A CD1 2379 C CD2 . LEU A 161 ? 0.2435 0.3706 0.2375 0.0065 -0.0419 -0.0063 169 LEU A CD2 2391 N N . PHE A 162 ? 0.1623 0.2540 0.1774 0.0002 0.0193 0.0328 170 PHE A N 2392 C CA . PHE A 162 ? 0.1416 0.2343 0.1577 0.0004 -0.0023 -0.0026 170 PHE A CA 2393 C C . PHE A 162 ? 0.1428 0.2215 0.1545 -0.0064 -0.0046 0.0192 170 PHE A C 2394 O O . PHE A 162 ? 0.1446 0.1990 0.1559 -0.0050 0.0110 0.0109 170 PHE A O 2395 C CB . PHE A 162 ? 0.1719 0.2379 0.1512 -0.0061 0.0101 0.0107 170 PHE A CB 2396 C CG . PHE A 162 ? 0.1280 0.2092 0.1591 -0.0170 0.0111 0.0143 170 PHE A CG 2397 C CD1 . PHE A 162 ? 0.1298 0.2327 0.1558 0.0069 0.0070 -0.0022 170 PHE A CD1 2398 C CD2 . PHE A 162 ? 0.1409 0.2409 0.1394 0.0070 0.0085 0.0089 170 PHE A CD2 2399 C CE1 . PHE A 162 ? 0.1438 0.2328 0.1573 -0.0167 0.0156 -0.0184 170 PHE A CE1 2400 C CE2 . PHE A 162 ? 0.1282 0.2699 0.1486 -0.0118 0.0177 0.0093 170 PHE A CE2 2401 C CZ . PHE A 162 ? 0.1341 0.2222 0.1566 0.0041 -0.0001 0.0160 170 PHE A CZ 2411 N N . LYS A 163 ? 0.1442 0.2282 0.1603 -0.0060 0.0308 0.0314 171 LYS A N 2412 C CA . LYS A 163 ? 0.1560 0.2645 0.1692 -0.0189 0.0330 0.0124 171 LYS A CA 2413 C C . LYS A 163 ? 0.1520 0.2759 0.1602 -0.0098 0.0232 0.0021 171 LYS A C 2414 O O . LYS A 163 ? 0.1781 0.3127 0.1563 -0.0135 0.0288 -0.0080 171 LYS A O 2415 C CB . LYS A 163 ? 0.1621 0.2908 0.1761 -0.0153 0.0231 0.0299 171 LYS A CB 2416 C CG . LYS A 163 ? 0.1862 0.3044 0.2257 -0.0239 0.0136 0.0570 171 LYS A CG 2417 C CD . LYS A 163 ? 0.2966 0.4028 0.2834 -0.0842 0.0407 0.0334 171 LYS A CD 2418 C CE . LYS A 163 ? 0.3873 0.4762 0.3410 -0.0976 0.0768 0.0395 171 LYS A CE 2419 N NZ . LYS A 163 ? 0.4572 0.5227 0.3757 -0.1084 0.1119 0.0555 171 LYS A NZ 2433 N N . ARG A 164 ? 0.1888 0.2860 0.1495 -0.0023 0.0207 0.0060 172 ARG A N 2434 C CA . ARG A 164 ? 0.1794 0.3422 0.1602 -0.0312 0.0107 -0.0026 172 ARG A CA 2435 C C . ARG A 164 ? 0.1591 0.3220 0.1670 0.0023 -0.0019 -0.0367 172 ARG A C 2436 O O . ARG A 164 ? 0.2117 0.3134 0.1848 -0.0131 0.0296 -0.0553 172 ARG A O 2437 C CB . ARG A 164 ? 0.2235 0.3939 0.2055 -0.0263 -0.0042 0.0364 172 ARG A CB 2438 C CG . ARG A 164 ? 0.3162 0.5033 0.2680 0.0053 -0.0117 0.0500 172 ARG A CG 2439 C CD . ARG A 164 ? 0.4460 0.5986 0.3628 0.0403 0.0264 0.0416 172 ARG A CD 2440 N NE . ARG A 164 ? 0.5263 0.6726 0.4170 0.0666 0.0291 0.0254 172 ARG A NE 2441 C CZ . ARG A 164 ? 0.6206 0.7342 0.4548 0.0583 0.0584 0.0054 172 ARG A CZ 2442 N NH1 . ARG A 164 ? 0.6571 0.7547 0.4641 0.0695 0.0641 0.0158 172 ARG A NH1 2443 N NH2 . ARG A 164 ? 0.6454 0.7523 0.4660 0.0610 0.0722 -0.0047 172 ARG A NH2 2457 N N . GLY A 165 ? 0.1661 0.2780 0.1422 0.0192 0.0014 -0.0312 173 GLY A N 2458 C CA . GLY A 165 ? 0.1794 0.2279 0.1484 0.0124 0.0038 -0.0047 173 GLY A CA 2459 C C . GLY A 165 ? 0.1426 0.2046 0.1683 -0.0112 0.0147 -0.0182 173 GLY A C 2460 O O . GLY A 165 ? 0.1380 0.1984 0.1776 -0.0035 -0.0064 -0.0065 173 GLY A O 2464 N N . ALA A 166 ? 0.1459 0.2157 0.1499 -0.0181 0.0278 0.0134 174 ALA A N 2465 C CA . ALA A 166 ? 0.1357 0.2265 0.1431 -0.0197 0.0086 0.0279 174 ALA A CA 2466 C C . ALA A 166 ? 0.1475 0.2045 0.1352 -0.0376 0.0086 0.0184 174 ALA A C 2467 O O . ALA A 166 ? 0.1284 0.2037 0.1444 0.0033 0.0034 0.0210 174 ALA A O 2468 C CB . ALA A 166 ? 0.1277 0.2049 0.1704 -0.0126 0.0087 -0.0080 174 ALA A CB 2474 N N . PHE A 167 ? 0.1428 0.1946 0.1207 -0.0122 0.0128 0.0072 175 PHE A N 2475 C CA . PHE A 167 ? 0.1312 0.1790 0.1389 -0.0032 0.0107 0.0034 175 PHE A CA 2476 C C . PHE A 167 ? 0.1395 0.1805 0.1329 -0.0284 0.0029 -0.0084 175 PHE A C 2477 O O . PHE A 167 ? 0.1892 0.1997 0.1392 -0.0140 0.0226 0.0238 175 PHE A O 2478 C CB . PHE A 167 ? 0.1225 0.2172 0.1485 -0.0009 0.0142 -0.0111 175 PHE A CB 2479 C CG . PHE A 167 ? 0.1352 0.2023 0.1584 -0.0209 0.0274 -0.0058 175 PHE A CG 2480 C CD1 . PHE A 167 ? 0.1377 0.2760 0.1589 0.0101 -0.0015 -0.0189 175 PHE A CD1 2481 C CD2 . PHE A 167 ? 0.1332 0.2019 0.1621 -0.0081 0.0139 -0.0161 175 PHE A CD2 2482 C CE1 . PHE A 167 ? 0.1423 0.2671 0.1676 0.0156 0.0050 -0.0256 175 PHE A CE1 2483 C CE2 . PHE A 167 ? 0.1520 0.2350 0.1608 -0.0279 -0.0059 -0.0214 175 PHE A CE2 2484 C CZ . PHE A 167 ? 0.1513 0.2594 0.1581 -0.0045 -0.0118 -0.0174 175 PHE A CZ 2494 N N . TYR A 168 ? 0.1366 0.1903 0.1324 -0.0140 0.0142 -0.0044 176 TYR A N 2495 C CA . TYR A 168 ? 0.1386 0.1640 0.1478 -0.0175 0.0014 0.0116 176 TYR A CA 2496 C C . TYR A 168 ? 0.1345 0.1716 0.1530 -0.0105 -0.0192 0.0156 176 TYR A C 2497 O O . TYR A 168 ? 0.1529 0.1904 0.1461 -0.0120 0.0073 0.0170 176 TYR A O 2498 C CB . TYR A 168 ? 0.1317 0.2109 0.1645 -0.0123 -0.0032 0.0149 176 TYR A CB 2499 C CG . TYR A 168 ? 0.1240 0.1837 0.1705 -0.0103 0.0111 0.0105 176 TYR A CG 2500 C CD1 . TYR A 168 ? 0.1064 0.2302 0.1767 0.0001 0.0202 0.0254 176 TYR A CD1 2501 C CD2 . TYR A 168 ? 0.1433 0.2042 0.1655 -0.0022 0.0092 -0.0098 176 TYR A CD2 2502 C CE1 . TYR A 168 ? 0.1161 0.2773 0.1683 0.0105 0.0190 0.0324 176 TYR A CE1 2503 C CE2 . TYR A 168 ? 0.1292 0.2740 0.1727 -0.0072 0.0136 -0.0246 176 TYR A CE2 2504 C CZ . TYR A 168 ? 0.1158 0.3089 0.1534 -0.0062 -0.0022 0.0065 176 TYR A CZ 2505 O OH . TYR A 168 ? 0.1545 0.3667 0.1541 0.0185 -0.0078 0.0162 176 TYR A OH 2515 N N . SER A 169 ? 0.1676 0.1860 0.1647 0.0000 0.0017 0.0412 177 SER A N 2516 C CA A SER A 169 ? 0.1656 0.1978 0.1956 0.0193 0.0058 0.0077 177 SER A CA 2517 C CA B SER A 169 ? 0.1776 0.1873 0.1950 -0.0045 0.0081 0.0148 177 SER A CA 2518 C C . SER A 169 ? 0.1827 0.1699 0.2216 -0.0107 0.0255 0.0191 177 SER A C 2519 O O . SER A 169 ? 0.2667 0.1995 0.2512 -0.0248 0.0692 0.0167 177 SER A O 2520 C CB A SER A 169 ? 0.1801 0.2224 0.2074 0.0159 -0.0044 0.0239 177 SER A CB 2521 C CB B SER A 169 ? 0.1850 0.1976 0.2056 -0.0215 0.0019 0.0043 177 SER A CB 2522 O OG A SER A 169 ? 0.1987 0.2209 0.2350 0.0058 -0.0157 0.0502 177 SER A OG 2523 O OG B SER A 169 ? 0.1860 0.1851 0.2059 -0.0267 -0.0057 -0.0114 177 SER A OG 2532 N N . GLU A 170 ? 0.2107 0.1601 0.2261 -0.0124 0.0118 0.0036 178 GLU A N 2533 C CA . GLU A 170 ? 0.2519 0.2147 0.2462 -0.0427 -0.0166 0.0207 178 GLU A CA 2534 C C . GLU A 170 ? 0.3031 0.1729 0.2429 -0.0721 -0.0029 -0.0070 178 GLU A C 2535 O O . GLU A 170 ? 0.3466 0.1676 0.2591 -0.0683 0.0159 -0.0099 178 GLU A O 2536 C CB . GLU A 170 ? 0.2547 0.3074 0.2905 -0.0484 -0.0335 0.0077 178 GLU A CB 2537 C CG . GLU A 170 ? 0.2813 0.3029 0.3145 0.0266 -0.0170 -0.0043 178 GLU A CG 2538 C CD . GLU A 170 ? 0.2323 0.2977 0.3229 -0.0045 -0.0239 -0.0478 178 GLU A CD 2539 O OE1 . GLU A 170 ? 0.2997 0.3202 0.3358 0.0565 -0.0435 -0.0519 178 GLU A OE1 2540 O OE2 . GLU A 170 ? 0.2172 0.2994 0.3131 -0.0607 0.0345 -0.0405 178 GLU A OE2 2547 N N . LYS A 171 ? 0.3304 0.1855 0.2720 -0.0435 0.0242 -0.0048 179 LYS A N 2548 C CA . LYS A 171 ? 0.3699 0.2093 0.3234 -0.0667 0.0511 -0.0090 179 LYS A CA 2549 C C . LYS A 171 ? 0.3401 0.3246 0.3297 -0.1069 0.0303 -0.0560 179 LYS A C 2550 O O . LYS A 171 ? 0.3384 0.4718 0.3468 -0.1077 0.0576 -0.0898 179 LYS A O 2551 C CB . LYS A 171 ? 0.4449 0.1915 0.3850 -0.0324 0.1112 0.0249 179 LYS A CB 2552 C CG . LYS A 171 ? 0.5189 0.3274 0.4221 0.0080 0.1010 0.0488 179 LYS A CG 2553 C CD . LYS A 171 ? 0.5652 0.4201 0.4497 0.0356 0.1056 0.0461 179 LYS A CD 2554 C CE . LYS A 171 ? 0.5895 0.4747 0.4739 0.0226 0.1098 0.0703 179 LYS A CE 2555 N NZ . LYS A 171 ? 0.6074 0.4676 0.4799 0.0253 0.1102 0.0828 179 LYS A NZ 2569 N N . LEU A 172 ? 0.3173 0.2647 0.3045 -0.1047 0.0059 -0.0433 180 LEU A N 2570 C CA . LEU A 172 ? 0.3455 0.2941 0.3223 -0.0970 -0.0038 -0.0651 180 LEU A CA 2571 C C . LEU A 172 ? 0.4400 0.3508 0.3543 -0.1254 0.0136 -0.0830 180 LEU A C 2572 O O . LEU A 172 ? 0.5034 0.3244 0.3470 -0.1545 0.0380 -0.0405 180 LEU A O 2573 C CB . LEU A 172 ? 0.3020 0.2942 0.3050 -0.0214 -0.0631 -0.0371 180 LEU A CB 2574 C CG . LEU A 172 ? 0.2772 0.3116 0.3123 -0.0020 -0.0774 -0.0231 180 LEU A CG 2575 C CD1 . LEU A 172 ? 0.3039 0.2973 0.3186 0.0264 -0.0434 -0.0196 180 LEU A CD1 2576 C CD2 . LEU A 172 ? 0.2885 0.3681 0.3150 0.0703 -0.0977 -0.0103 180 LEU A CD2 2588 N N . PRO A 173 ? 0.5017 0.4080 0.4049 -0.1355 0.0381 -0.0911 181 PRO A N 2589 C CA . PRO A 173 ? 0.5280 0.4121 0.4210 -0.1666 0.0482 -0.0948 181 PRO A CA 2590 C C . PRO A 173 ? 0.5617 0.3697 0.4149 -0.1876 0.0553 -0.1178 181 PRO A C 2591 O O . PRO A 173 ? 0.5666 0.3158 0.4095 -0.1898 0.0555 -0.1188 181 PRO A O 2592 C CB . PRO A 173 ? 0.5120 0.4457 0.4253 -0.1537 0.0374 -0.0702 181 PRO A CB 2593 C CG . PRO A 173 ? 0.5040 0.4208 0.4294 -0.1503 0.0339 -0.0707 181 PRO A CG 2594 C CD . PRO A 173 ? 0.4960 0.4373 0.4132 -0.1190 0.0178 -0.0773 181 PRO A CD 2602 N N . GLY A 174 ? 0.5783 0.3826 0.4232 -0.1851 0.0620 -0.1021 182 GLY A N 2603 C CA . GLY A 174 ? 0.5604 0.3900 0.4244 -0.1808 0.0359 -0.0844 182 GLY A CA 2604 C C . GLY A 174 ? 0.5230 0.4159 0.4309 -0.1878 -0.0111 -0.1006 182 GLY A C 2605 O O . GLY A 174 ? 0.5188 0.4607 0.4636 -0.2186 -0.0149 -0.1172 182 GLY A O 2609 N N . PRO A 175 ? 0.4741 0.3711 0.3869 -0.2052 -0.0469 -0.0885 183 PRO A N 2610 C CA . PRO A 175 ? 0.5083 0.3454 0.3808 -0.1560 -0.0434 -0.0621 183 PRO A CA 2611 C C . PRO A 175 ? 0.5100 0.3027 0.3732 -0.1228 -0.0605 -0.0684 183 PRO A C 2612 O O . PRO A 175 ? 0.5753 0.3373 0.3758 -0.1152 -0.0230 -0.0680 183 PRO A O 2613 C CB . PRO A 175 ? 0.5078 0.3859 0.3822 -0.1306 -0.0445 -0.0391 183 PRO A CB 2614 C CG . PRO A 175 ? 0.4858 0.4058 0.3826 -0.1414 -0.0590 -0.0419 183 PRO A CG 2615 C CD . PRO A 175 ? 0.4852 0.3972 0.3819 -0.1672 -0.0568 -0.0750 183 PRO A CD 2623 N N . SER A 176 ? 0.4740 0.2432 0.3754 -0.0983 -0.0911 -0.0029 184 SER A N 2624 C CA . SER A 176 ? 0.4211 0.2728 0.3648 -0.0853 -0.1686 0.0113 184 SER A CA 2625 C C . SER A 176 ? 0.4418 0.2564 0.3523 -0.0701 -0.1459 -0.0002 184 SER A C 2626 O O . SER A 176 ? 0.4769 0.2671 0.3449 -0.0774 -0.0996 0.0243 184 SER A O 2627 C CB . SER A 176 ? 0.4422 0.2732 0.3788 -0.0727 -0.1843 0.0374 184 SER A CB 2628 O OG . SER A 176 ? 0.5108 0.2892 0.3998 -0.0574 -0.1545 0.0666 184 SER A OG 2634 N N . ARG A 177 ? 0.4367 0.2693 0.3630 -0.0403 -0.1367 -0.0086 185 ARG A N 2635 C CA . ARG A 177 ? 0.4874 0.2667 0.3868 0.0168 -0.1235 -0.0069 185 ARG A CA 2636 C C . ARG A 177 ? 0.4756 0.2700 0.3835 0.0243 -0.1208 -0.0258 185 ARG A C 2637 O O . ARG A 177 ? 0.5154 0.2870 0.3847 0.0207 -0.1209 -0.0023 185 ARG A O 2638 C CB . ARG A 177 ? 0.5005 0.3122 0.4151 0.0067 -0.1241 -0.0030 185 ARG A CB 2639 C CG . ARG A 177 ? 0.5223 0.3391 0.4407 0.0048 -0.1145 0.0168 185 ARG A CG 2640 C CD . ARG A 177 ? 0.5543 0.3893 0.4691 -0.0170 -0.0941 0.0065 185 ARG A CD 2641 N NE . ARG A 177 ? 0.5963 0.4269 0.4875 -0.0200 -0.0757 0.0018 185 ARG A NE 2642 C CZ . ARG A 177 ? 0.6347 0.4535 0.5044 -0.0194 -0.0420 -0.0105 185 ARG A CZ 2643 N NH1 . ARG A 177 ? 0.6370 0.4327 0.4960 0.0019 -0.0400 0.0051 185 ARG A NH1 2644 N NH2 . ARG A 177 ? 0.6539 0.4715 0.5228 -0.0228 -0.0169 -0.0061 185 ARG A NH2 2658 N N . ALA A 178 ? 0.3986 0.2388 0.3786 0.0208 -0.1295 -0.0818 186 ALA A N 2659 C CA . ALA A 178 ? 0.3794 0.2401 0.3527 0.0791 -0.0913 -0.0408 186 ALA A CA 2660 C C . ALA A 178 ? 0.3363 0.1904 0.3246 0.0440 -0.0685 -0.0201 186 ALA A C 2661 O O . ALA A 178 ? 0.2878 0.2061 0.3218 0.0406 -0.0719 -0.0326 186 ALA A O 2662 C CB . ALA A 178 ? 0.4077 0.2256 0.3626 0.0846 -0.0705 -0.0563 186 ALA A CB 2668 N N . GLY A 179 ? 0.2730 0.1695 0.3196 0.0381 -0.0412 -0.0308 187 GLY A N 2669 C CA . GLY A 179 ? 0.2565 0.1721 0.2836 0.0436 -0.0431 -0.0432 187 GLY A CA 2670 C C . GLY A 179 ? 0.2084 0.1597 0.2550 0.0131 -0.0459 -0.0232 187 GLY A C 2671 O O . GLY A 179 ? 0.2552 0.1691 0.2665 0.0019 -0.0254 -0.0180 187 GLY A O 2675 N N . ARG A 180 ? 0.2063 0.1620 0.2424 -0.0022 -0.0368 0.0053 188 ARG A N 2676 C CA . ARG A 180 ? 0.2056 0.1686 0.2057 -0.0172 -0.0321 0.0058 188 ARG A CA 2677 C C . ARG A 180 ? 0.1561 0.1692 0.2002 -0.0112 -0.0171 0.0028 188 ARG A C 2678 O O . ARG A 180 ? 0.1578 0.1719 0.2398 0.0151 -0.0080 0.0124 188 ARG A O 2679 C CB . ARG A 180 ? 0.2039 0.1953 0.2233 0.0104 -0.0324 0.0110 188 ARG A CB 2680 C CG . ARG A 180 ? 0.2227 0.1960 0.2153 0.0187 -0.0178 0.0044 188 ARG A CG 2681 C CD . ARG A 180 ? 0.2494 0.2128 0.2258 0.0108 -0.0398 0.0137 188 ARG A CD 2682 N NE . ARG A 180 ? 0.2278 0.2143 0.2420 -0.0030 -0.0537 0.0149 188 ARG A NE 2683 C CZ . ARG A 180 ? 0.2676 0.2356 0.2959 0.0158 -0.0325 0.0586 188 ARG A CZ 2684 N NH1 . ARG A 180 ? 0.2493 0.2900 0.3030 0.0506 -0.0001 0.0452 188 ARG A NH1 2685 N NH2 . ARG A 180 ? 0.3506 0.2513 0.3566 0.0519 -0.0062 0.0742 188 ARG A NH2 2699 N N . VAL A 181 ? 0.1624 0.1692 0.1691 -0.0152 -0.0038 0.0021 189 VAL A N 2700 C CA . VAL A 181 ? 0.1522 0.1642 0.1830 -0.0166 -0.0176 0.0002 189 VAL A CA 2701 C C . VAL A 181 ? 0.1616 0.1565 0.1818 -0.0207 -0.0090 0.0150 189 VAL A C 2702 O O . VAL A 181 ? 0.2275 0.1855 0.2119 -0.0591 0.0352 -0.0016 189 VAL A O 2703 C CB . VAL A 181 ? 0.1529 0.1807 0.2255 -0.0010 -0.0081 -0.0031 189 VAL A CB 2704 C CG1 . VAL A 181 ? 0.1470 0.1911 0.2104 -0.0023 -0.0223 -0.0029 189 VAL A CG1 2705 C CG2 . VAL A 181 ? 0.2130 0.2029 0.2519 -0.0114 -0.0387 0.0035 189 VAL A CG2 2715 N N . VAL A 182 ? 0.1322 0.1433 0.1634 0.0006 0.0030 0.0042 190 VAL A N 2716 C CA . VAL A 182 ? 0.1269 0.1707 0.1599 0.0100 -0.0023 0.0129 190 VAL A CA 2717 C C . VAL A 182 ? 0.1343 0.1492 0.1621 -0.0075 0.0060 0.0103 190 VAL A C 2718 O O . VAL A 182 ? 0.1660 0.1708 0.1793 0.0161 0.0368 0.0269 190 VAL A O 2719 C CB . VAL A 182 ? 0.1402 0.1795 0.1897 0.0017 -0.0216 -0.0073 190 VAL A CB 2720 C CG1 . VAL A 182 ? 0.1849 0.2473 0.2374 -0.0365 0.0062 -0.0232 190 VAL A CG1 2721 C CG2 . VAL A 182 ? 0.1555 0.2803 0.2105 -0.0209 -0.0367 0.0208 190 VAL A CG2 2731 N N . VAL A 183 ? 0.1324 0.1671 0.1441 -0.0058 0.0112 0.0000 191 VAL A N 2732 C CA . VAL A 183 ? 0.1252 0.1762 0.1426 0.0003 0.0028 0.0046 191 VAL A CA 2733 C C . VAL A 183 ? 0.1264 0.2065 0.1253 0.0136 0.0038 0.0009 191 VAL A C 2734 O O . VAL A 183 ? 0.1433 0.1784 0.1400 0.0007 0.0156 -0.0034 191 VAL A O 2735 C CB . VAL A 183 ? 0.1425 0.1827 0.1274 0.0012 -0.0118 0.0053 191 VAL A CB 2736 C CG1 . VAL A 183 ? 0.1413 0.2084 0.1673 -0.0183 0.0094 0.0121 191 VAL A CG1 2737 C CG2 . VAL A 183 ? 0.1639 0.2046 0.1479 -0.0261 -0.0064 -0.0074 191 VAL A CG2 2747 N N . LEU A 184 ? 0.1459 0.1667 0.1193 -0.0113 0.0039 0.0002 192 LEU A N 2748 C CA . LEU A 184 ? 0.1273 0.1703 0.1233 0.0081 -0.0036 0.0073 192 LEU A CA 2749 C C . LEU A 184 ? 0.1179 0.1619 0.1421 -0.0042 -0.0048 -0.0036 192 LEU A C 2750 O O . LEU A 184 ? 0.1069 0.1744 0.1394 0.0026 -0.0046 -0.0038 192 LEU A O 2751 C CB . LEU A 184 ? 0.1211 0.1733 0.1254 -0.0014 0.0082 0.0000 192 LEU A CB 2752 C CG . LEU A 184 ? 0.1166 0.1989 0.1431 0.0146 0.0028 -0.0170 192 LEU A CG 2753 C CD1 . LEU A 184 ? 0.1131 0.2262 0.1529 -0.0085 0.0158 -0.0090 192 LEU A CD1 2754 C CD2 . LEU A 184 ? 0.1419 0.2291 0.1782 0.0141 -0.0131 0.0145 192 LEU A CD2 2766 N N . ASN A 185 ? 0.1353 0.1598 0.1407 -0.0061 0.0045 -0.0180 193 ASN A N 2767 C CA . ASN A 185 ? 0.1260 0.1640 0.1232 -0.0010 0.0076 0.0053 193 ASN A CA 2768 C C . ASN A 185 ? 0.1003 0.1642 0.1457 -0.0081 0.0172 -0.0006 193 ASN A C 2769 O O . ASN A 185 ? 0.1258 0.1944 0.1372 -0.0053 -0.0057 -0.0150 193 ASN A O 2770 C CB . ASN A 185 ? 0.1199 0.1724 0.1457 -0.0004 0.0016 0.0159 193 ASN A CB 2771 C CG . ASN A 185 ? 0.1090 0.1987 0.1422 0.0003 0.0046 -0.0001 193 ASN A CG 2772 O OD1 . ASN A 185 ? 0.1273 0.1863 0.1444 0.0165 0.0079 0.0028 193 ASN A OD1 2773 N ND2 . ASN A 185 ? 0.1348 0.1980 0.1395 -0.0059 0.0227 -0.0153 193 ASN A ND2 2780 N N . THR A 186 ? 0.1156 0.1798 0.1336 -0.0126 0.0137 -0.0036 194 THR A N 2781 C CA . THR A 186 ? 0.1119 0.1486 0.1371 -0.0086 0.0118 -0.0021 194 THR A CA 2782 C C . THR A 186 ? 0.1192 0.1680 0.1316 -0.0053 0.0078 -0.0006 194 THR A C 2783 O O . THR A 186 ? 0.1196 0.1763 0.1554 0.0047 0.0090 -0.0064 194 THR A O 2784 C CB . THR A 186 ? 0.1016 0.1607 0.1527 -0.0058 0.0085 -0.0166 194 THR A CB 2785 O OG1 . THR A 186 ? 0.1101 0.1991 0.1363 -0.0026 0.0024 -0.0064 194 THR A OG1 2786 C CG2 . THR A 186 ? 0.1202 0.1568 0.1533 -0.0058 0.0125 -0.0237 194 THR A CG2 2794 N N . ASN A 187 ? 0.1074 0.1730 0.1343 -0.0057 0.0053 -0.0173 195 ASN A N 2795 C CA . ASN A 187 ? 0.1117 0.1706 0.1509 0.0077 0.0211 -0.0094 195 ASN A CA 2796 C C . ASN A 187 ? 0.1036 0.1664 0.1589 -0.0021 0.0217 -0.0146 195 ASN A C 2797 O O . ASN A 187 ? 0.1315 0.1759 0.1716 0.0011 0.0015 -0.0253 195 ASN A O 2798 C CB . ASN A 187 ? 0.1194 0.1911 0.1495 0.0038 0.0039 -0.0092 195 ASN A CB 2799 C CG . ASN A 187 ? 0.1256 0.1874 0.1464 -0.0037 0.0011 -0.0118 195 ASN A CG 2800 O OD1 . ASN A 187 ? 0.1572 0.2154 0.1510 -0.0029 -0.0143 0.0024 195 ASN A OD1 2801 N ND2 . ASN A 187 ? 0.1591 0.1956 0.1556 -0.0238 0.0087 -0.0144 195 ASN A ND2 2808 N N . LEU A 188 ? 0.1161 0.1769 0.1587 0.0126 0.0182 -0.0283 196 LEU A N 2809 C CA . LEU A 188 ? 0.1256 0.2030 0.1515 0.0009 0.0144 -0.0261 196 LEU A CA 2810 C C . LEU A 188 ? 0.1267 0.2012 0.1508 -0.0037 0.0209 -0.0267 196 LEU A C 2811 O O . LEU A 188 ? 0.1474 0.2407 0.1639 -0.0027 0.0045 -0.0408 196 LEU A O 2812 C CB . LEU A 188 ? 0.1370 0.2072 0.1529 0.0045 0.0163 -0.0384 196 LEU A CB 2813 C CG . LEU A 188 ? 0.1287 0.1879 0.1593 0.0015 0.0081 -0.0153 196 LEU A CG 2814 C CD1 . LEU A 188 ? 0.1746 0.2183 0.1614 -0.0075 0.0024 -0.0023 196 LEU A CD1 2815 C CD2 . LEU A 188 ? 0.1480 0.2321 0.1731 -0.0146 0.0112 -0.0138 196 LEU A CD2 2827 N N . TYR A 189 ? 0.1166 0.1848 0.1550 -0.0062 0.0086 -0.0244 197 TYR A N 2828 C CA . TYR A 189 ? 0.1164 0.1958 0.1743 -0.0141 0.0009 -0.0314 197 TYR A CA 2829 C C . TYR A 189 ? 0.1518 0.1609 0.1941 -0.0095 -0.0084 -0.0146 197 TYR A C 2830 O O . TYR A 189 ? 0.1538 0.1709 0.1758 0.0022 -0.0092 -0.0249 197 TYR A O 2831 C CB . TYR A 189 ? 0.1369 0.1985 0.1725 -0.0240 0.0005 -0.0208 197 TYR A CB 2832 C CG . TYR A 189 ? 0.1235 0.1863 0.1715 0.0017 -0.0030 0.0040 197 TYR A CG 2833 C CD1 . TYR A 189 ? 0.1257 0.1865 0.1705 0.0059 0.0032 -0.0122 197 TYR A CD1 2834 C CD2 . TYR A 189 ? 0.1086 0.2095 0.1532 0.0037 -0.0015 -0.0033 197 TYR A CD2 2835 C CE1 . TYR A 189 ? 0.1351 0.1806 0.1547 0.0036 -0.0187 -0.0155 197 TYR A CE1 2836 C CE2 . TYR A 189 ? 0.1417 0.2011 0.1565 0.0103 -0.0018 -0.0225 197 TYR A CE2 2837 C CZ . TYR A 189 ? 0.1390 0.1894 0.1611 -0.0091 -0.0144 -0.0163 197 TYR A CZ 2838 O OH . TYR A 189 ? 0.1561 0.1965 0.1680 -0.0101 -0.0417 -0.0057 197 TYR A OH 2848 N N . TYR A 190 ? 0.1607 0.1574 0.2222 -0.0108 -0.0303 -0.0166 198 TYR A N 2849 C CA . TYR A 190 ? 0.1486 0.1614 0.2359 0.0031 -0.0247 -0.0112 198 TYR A CA 2850 C C . TYR A 190 ? 0.1540 0.1858 0.2085 0.0290 -0.0001 -0.0018 198 TYR A C 2851 O O . TYR A 190 ? 0.2097 0.2314 0.2313 0.0476 0.0675 0.0040 198 TYR A O 2852 C CB . TYR A 190 ? 0.1733 0.2088 0.2741 -0.0198 -0.0490 -0.0006 198 TYR A CB 2853 C CG . TYR A 190 ? 0.1425 0.2582 0.2485 0.0135 -0.0261 -0.0136 198 TYR A CG 2854 C CD1 . TYR A 190 ? 0.2229 0.2838 0.2472 -0.0011 -0.0202 0.0184 198 TYR A CD1 2855 C CD2 . TYR A 190 ? 0.2155 0.3564 0.2598 0.0374 0.0092 0.0151 198 TYR A CD2 2856 C CE1 . TYR A 190 ? 0.2323 0.3416 0.2701 -0.0010 -0.0086 0.0268 198 TYR A CE1 2857 C CE2 . TYR A 190 ? 0.2529 0.3669 0.2630 0.0286 -0.0208 0.0560 198 TYR A CE2 2858 C CZ . TYR A 190 ? 0.2593 0.3874 0.2734 0.0005 -0.0434 0.0639 198 TYR A CZ 2859 O OH . TYR A 190 ? 0.2930 0.4165 0.3332 0.0089 -0.0209 0.0722 198 TYR A OH 2869 N N . SER A 191 ? 0.1685 0.1600 0.2116 0.0082 0.0177 -0.0186 199 SER A N 2870 C CA . SER A 191 ? 0.2385 0.1620 0.2550 0.0110 0.0292 -0.0127 199 SER A CA 2871 C C . SER A 191 ? 0.2757 0.2147 0.2839 0.0429 0.0684 -0.0079 199 SER A C 2872 O O . SER A 191 ? 0.3925 0.2873 0.3267 0.0726 0.0964 -0.0340 199 SER A O 2873 C CB . SER A 191 ? 0.2973 0.2053 0.2909 0.0172 0.0578 -0.0140 199 SER A CB 2874 O OG . SER A 191 ? 0.3624 0.2017 0.2919 -0.0196 0.1033 0.0056 199 SER A OG 2880 N N . ASN A 192 ? 0.2233 0.2333 0.3301 0.0450 0.1015 0.0350 200 ASN A N 2881 C CA . ASN A 192 ? 0.2603 0.2783 0.3710 0.0642 0.0928 0.0525 200 ASN A CA 2882 C C . ASN A 192 ? 0.2178 0.2637 0.3810 0.0472 0.0909 0.0373 200 ASN A C 2883 O O . ASN A 192 ? 0.2246 0.2663 0.4148 0.0659 0.0679 0.0407 200 ASN A O 2884 C CB . ASN A 192 ? 0.3225 0.3631 0.3785 0.0743 0.0667 0.0755 200 ASN A CB 2885 C CG . ASN A 192 ? 0.4840 0.4408 0.4211 0.0642 0.0674 0.0676 200 ASN A CG 2886 O OD1 . ASN A 192 ? 0.5470 0.4986 0.4534 0.0712 0.0771 0.0926 200 ASN A OD1 2887 N ND2 . ASN A 192 ? 0.5504 0.4938 0.4410 0.0629 0.1035 0.0533 200 ASN A ND2 2894 N N . ASN A 193 ? 0.2038 0.1986 0.3468 0.0148 0.0871 0.0149 201 ASN A N 2895 C CA . ASN A 193 ? 0.1732 0.2021 0.2996 0.0070 0.0415 -0.0101 201 ASN A CA 2896 C C . ASN A 193 ? 0.1629 0.2181 0.3342 -0.0192 0.0233 -0.0313 201 ASN A C 2897 O O . ASN A 193 ? 0.1779 0.2478 0.3496 -0.0220 0.0043 -0.0743 201 ASN A O 2898 C CB . ASN A 193 ? 0.1600 0.1903 0.2299 0.0332 0.0209 -0.0257 201 ASN A CB 2899 C CG . ASN A 193 ? 0.1518 0.1961 0.2037 0.0120 0.0191 -0.0279 201 ASN A CG 2900 O OD1 . ASN A 193 ? 0.1852 0.2141 0.1952 0.0310 0.0273 -0.0405 201 ASN A OD1 2901 N ND2 . ASN A 193 ? 0.1431 0.1979 0.1857 0.0091 0.0123 -0.0198 201 ASN A ND2 2908 N N . GLU A 194 ? 0.2004 0.2251 0.3449 0.0154 0.0300 -0.0619 202 GLU A N 2909 C CA . GLU A 194 ? 0.2029 0.2584 0.3334 0.0579 0.0008 -0.0777 202 GLU A CA 2910 C C . GLU A 194 ? 0.2070 0.2827 0.2850 0.0476 -0.0105 -0.0882 202 GLU A C 2911 O O . GLU A 194 ? 0.2271 0.2935 0.2780 0.0279 -0.0461 -0.0906 202 GLU A O 2912 C CB . GLU A 194 ? 0.3106 0.2953 0.3672 0.0941 0.0058 -0.0691 202 GLU A CB 2913 C CG . GLU A 194 ? 0.4408 0.3882 0.4235 0.0894 0.0535 -0.0453 202 GLU A CG 2914 C CD . GLU A 194 ? 0.5690 0.5178 0.4742 0.0790 0.1034 -0.0047 202 GLU A CD 2915 O OE1 . GLU A 194 ? 0.6195 0.5640 0.4992 0.0699 0.1146 0.0060 202 GLU A OE1 2916 O OE2 . GLU A 194 ? 0.6199 0.5765 0.4885 0.0839 0.1181 0.0022 202 GLU A OE2 2923 N N . GLN A 195 ? 0.1948 0.2597 0.2548 0.0398 -0.0188 -0.0782 203 GLN A N 2924 C CA . GLN A 195 ? 0.1933 0.3099 0.2405 0.0337 -0.0167 -0.0859 203 GLN A CA 2925 C C . GLN A 195 ? 0.1958 0.3235 0.2385 0.0512 -0.0116 -0.0880 203 GLN A C 2926 O O . GLN A 195 ? 0.2291 0.3942 0.2303 0.0490 0.0008 -0.0721 203 GLN A O 2927 C CB . GLN A 195 ? 0.2101 0.3274 0.2443 0.0046 -0.0076 -0.0845 203 GLN A CB 2928 C CG . GLN A 195 ? 0.2080 0.3701 0.2777 -0.0147 -0.0274 -0.0690 203 GLN A CG 2929 C CD . GLN A 195 ? 0.2995 0.4530 0.3145 0.0069 0.0092 -0.0299 203 GLN A CD 2930 O OE1 . GLN A 195 ? 0.3453 0.4782 0.3195 0.0375 0.0404 -0.0291 203 GLN A OE1 2931 N NE2 . GLN A 195 ? 0.3458 0.5121 0.3396 -0.0157 0.0460 -0.0055 203 GLN A NE2 2940 N N . THR A 196 ? 0.1766 0.2442 0.2358 0.0375 -0.0169 -0.0774 204 THR A N 2941 C CA . THR A 196 ? 0.1745 0.2300 0.2486 0.0421 -0.0314 -0.0891 204 THR A CA 2942 C C . THR A 196 ? 0.2196 0.2391 0.3068 0.0284 -0.0470 -0.0879 204 THR A C 2943 O O . THR A 196 ? 0.1995 0.2752 0.3246 -0.0046 -0.0489 -0.0851 204 THR A O 2944 C CB . THR A 196 ? 0.2040 0.2446 0.2164 0.0421 -0.0196 -0.0682 204 THR A CB 2945 O OG1 . THR A 196 ? 0.2112 0.2918 0.2240 0.0333 0.0034 -0.0168 204 THR A OG1 2946 C CG2 . THR A 196 ? 0.2251 0.2588 0.2026 0.0416 -0.0077 -0.0785 204 THR A CG2 2954 N N . ALA A 197 ? 0.2572 0.2525 0.3581 0.0229 -0.0692 -0.1012 205 ALA A N 2955 C CA . ALA A 197 ? 0.2972 0.2499 0.3923 0.0130 -0.0941 -0.1027 205 ALA A CA 2956 C C . ALA A 197 ? 0.3090 0.2952 0.3944 0.0125 -0.0839 -0.1229 205 ALA A C 2957 O O . ALA A 197 ? 0.3017 0.3360 0.3955 0.0341 -0.0698 -0.1384 205 ALA A O 2958 C CB . ALA A 197 ? 0.3413 0.2416 0.4147 -0.0049 -0.0972 -0.0889 205 ALA A CB 2964 N N . GLY A 198 ? 0.3314 0.2957 0.4010 -0.0008 -0.0835 -0.1157 206 GLY A N 2965 C CA . GLY A 198 ? 0.3261 0.3236 0.3628 0.0074 -0.0843 -0.1159 206 GLY A CA 2966 C C . GLY A 198 ? 0.3105 0.3276 0.3248 0.0280 -0.0933 -0.1273 206 GLY A C 2967 O O . GLY A 198 ? 0.3607 0.3987 0.3297 0.0129 -0.1322 -0.1481 206 GLY A O 2971 N N . MET A 199 ? 0.2526 0.3111 0.2821 0.0279 -0.0585 -0.1156 207 MET A N 2972 C CA . MET A 199 ? 0.2220 0.3296 0.2445 0.0183 -0.0469 -0.0918 207 MET A CA 2973 C C . MET A 199 ? 0.2399 0.3245 0.2456 0.0086 -0.0273 -0.0969 207 MET A C 2974 O O . MET A 199 ? 0.2391 0.3521 0.2375 0.0104 -0.0235 -0.0920 207 MET A O 2975 C CB . MET A 199 ? 0.2018 0.3495 0.2189 0.0172 -0.0211 -0.1097 207 MET A CB 2976 C CG . MET A 199 ? 0.2152 0.3690 0.2387 0.0170 -0.0179 -0.1109 207 MET A CG 2977 S SD . MET A 199 ? 0.2351 0.3832 0.2566 -0.0050 -0.0059 -0.0442 207 MET A SD 2978 C CE . MET A 199 ? 0.2631 0.4391 0.2673 0.0216 -0.0141 -0.0251 207 MET A CE 2988 N N . ALA A 200 ? 0.2289 0.3005 0.2540 -0.0101 -0.0462 -0.0781 208 ALA A N 2989 C CA . ALA A 200 ? 0.2353 0.2719 0.2792 -0.0073 -0.0328 -0.0597 208 ALA A CA 2990 C C . ALA A 200 ? 0.2019 0.2676 0.2510 0.0187 -0.0247 -0.0489 208 ALA A C 2991 O O . ALA A 200 ? 0.2194 0.2649 0.2502 -0.0010 -0.0093 -0.0268 208 ALA A O 2992 C CB . ALA A 200 ? 0.2461 0.3235 0.3163 -0.0176 -0.0468 -0.0626 208 ALA A CB 2998 N N . ASP A 201 ? 0.1898 0.2417 0.2123 0.0200 -0.0247 -0.0449 209 ASP A N 2999 C CA . ASP A 201 ? 0.1720 0.2218 0.1973 0.0175 -0.0224 -0.0261 209 ASP A CA 3000 C C . ASP A 201 ? 0.1779 0.2354 0.1742 0.0250 -0.0306 -0.0329 209 ASP A C 3001 O O . ASP A 201 ? 0.1838 0.2525 0.1772 0.0350 -0.0328 -0.0167 209 ASP A O 3002 C CB . ASP A 201 ? 0.1705 0.2434 0.1987 -0.0017 -0.0349 -0.0196 209 ASP A CB 3003 C CG . ASP A 201 ? 0.2065 0.2116 0.1788 0.0030 -0.0152 -0.0052 209 ASP A CG 3004 O OD1 . ASP A 201 ? 0.2033 0.2429 0.1631 0.0210 -0.0243 -0.0290 209 ASP A OD1 3005 O OD2 . ASP A 201 ? 0.2330 0.2268 0.1926 0.0113 -0.0268 0.0013 209 ASP A OD2 3010 N N . PRO A 202 ? 0.1683 0.2326 0.1823 0.0176 -0.0031 -0.0382 210 PRO A N 3011 C CA . PRO A 202 ? 0.1774 0.2312 0.1716 0.0237 -0.0009 -0.0226 210 PRO A CA 3012 C C . PRO A 202 ? 0.1631 0.2261 0.1808 0.0242 0.0028 -0.0053 210 PRO A C 3013 O O . PRO A 202 ? 0.1616 0.2379 0.1676 0.0091 0.0043 -0.0071 210 PRO A O 3014 C CB . PRO A 202 ? 0.1709 0.2554 0.1863 0.0158 0.0066 0.0077 210 PRO A CB 3015 C CG . PRO A 202 ? 0.1695 0.2505 0.1861 0.0167 0.0110 -0.0016 210 PRO A CG 3016 C CD . PRO A 202 ? 0.1545 0.2270 0.1882 -0.0112 -0.0163 -0.0255 210 PRO A CD 3024 N N . GLY A 203 ? 0.1917 0.2310 0.2094 0.0171 0.0251 -0.0012 211 GLY A N 3025 C CA . GLY A 203 ? 0.1775 0.2526 0.1941 -0.0029 0.0466 -0.0168 211 GLY A CA 3026 C C . GLY A 203 ? 0.1862 0.2343 0.1572 0.0183 0.0348 -0.0058 211 GLY A C 3027 O O . GLY A 203 ? 0.2414 0.2330 0.1721 -0.0038 0.0336 0.0109 211 GLY A O 3031 N N . GLU A 204 ? 0.1709 0.2625 0.1452 0.0001 0.0048 -0.0144 212 GLU A N 3032 C CA . GLU A 204 ? 0.1853 0.2541 0.1448 0.0301 -0.0113 0.0039 212 GLU A CA 3033 C C . GLU A 204 ? 0.1619 0.2246 0.1482 0.0251 -0.0122 -0.0271 212 GLU A C 3034 O O . GLU A 204 ? 0.1801 0.2300 0.1527 0.0332 -0.0125 -0.0014 212 GLU A O 3035 C CB . GLU A 204 ? 0.2920 0.2994 0.1490 0.0577 0.0105 0.0094 212 GLU A CB 3036 C CG . GLU A 204 ? 0.4553 0.3972 0.1804 0.0653 0.0287 0.0182 212 GLU A CG 3037 C CD . GLU A 204 ? 0.5836 0.5108 0.2796 -0.0046 0.0272 0.0122 212 GLU A CD 3038 O OE1 . GLU A 204 ? 0.6312 0.5611 0.3169 -0.0640 0.0543 0.0459 212 GLU A OE1 3039 O OE2 . GLU A 204 ? 0.6483 0.5514 0.3261 0.0186 0.0289 -0.0088 212 GLU A OE2 3046 N N . GLN A 205 ? 0.1489 0.2027 0.1426 0.0135 -0.0240 -0.0215 213 GLN A N 3047 C CA . GLN A 205 ? 0.1329 0.1867 0.1576 0.0092 -0.0104 -0.0138 213 GLN A CA 3048 C C . GLN A 205 ? 0.1553 0.1974 0.1501 0.0067 -0.0345 -0.0146 213 GLN A C 3049 O O . GLN A 205 ? 0.1408 0.1916 0.1506 0.0090 -0.0196 -0.0229 213 GLN A O 3050 C CB . GLN A 205 ? 0.1433 0.1835 0.1511 0.0088 -0.0093 -0.0157 213 GLN A CB 3051 C CG . GLN A 205 ? 0.1293 0.1764 0.1606 0.0094 -0.0260 -0.0113 213 GLN A CG 3052 C CD . GLN A 205 ? 0.1287 0.1935 0.1502 -0.0010 -0.0066 0.0021 213 GLN A CD 3053 O OE1 . GLN A 205 ? 0.1403 0.2079 0.1448 -0.0073 -0.0245 -0.0162 213 GLN A OE1 3054 N NE2 . GLN A 205 ? 0.1464 0.1836 0.1568 -0.0174 -0.0244 -0.0029 213 GLN A NE2 3063 N N . PHE A 206 ? 0.1520 0.1715 0.1399 0.0121 -0.0144 -0.0208 214 PHE A N 3064 C CA . PHE A 206 ? 0.1344 0.1904 0.1552 0.0134 -0.0024 -0.0063 214 PHE A CA 3065 C C . PHE A 206 ? 0.1314 0.1960 0.1684 -0.0044 -0.0138 -0.0257 214 PHE A C 3066 O O . PHE A 206 ? 0.1403 0.2143 0.1768 0.0247 -0.0299 -0.0214 214 PHE A O 3067 C CB . PHE A 206 ? 0.1505 0.2094 0.1726 0.0151 -0.0228 -0.0141 214 PHE A CB 3068 C CG . PHE A 206 ? 0.1426 0.1990 0.2185 0.0100 -0.0026 -0.0019 214 PHE A CG 3069 C CD1 . PHE A 206 ? 0.1329 0.2321 0.2287 0.0046 0.0027 0.0282 214 PHE A CD1 3070 C CD2 . PHE A 206 ? 0.1666 0.2104 0.2564 -0.0227 -0.0070 0.0138 214 PHE A CD2 3071 C CE1 . PHE A 206 ? 0.1643 0.2427 0.2543 -0.0085 -0.0172 0.0494 214 PHE A CE1 3072 C CE2 . PHE A 206 ? 0.1752 0.2322 0.2797 -0.0100 -0.0064 0.0492 214 PHE A CE2 3073 C CZ . PHE A 206 ? 0.1636 0.2417 0.2623 -0.0070 -0.0257 0.0547 214 PHE A CZ 3083 N N . ARG A 207 ? 0.1367 0.2194 0.1536 0.0042 -0.0254 -0.0136 215 ARG A N 3084 C CA . ARG A 207 ? 0.1634 0.2213 0.1555 0.0044 -0.0265 0.0046 215 ARG A CA 3085 C C . ARG A 207 ? 0.1790 0.1933 0.1484 0.0178 -0.0326 0.0119 215 ARG A C 3086 O O . ARG A 207 ? 0.1563 0.1977 0.1610 0.0132 -0.0272 -0.0001 215 ARG A O 3087 C CB . ARG A 207 ? 0.1674 0.2204 0.1680 0.0309 -0.0366 0.0140 215 ARG A CB 3088 C CG . ARG A 207 ? 0.1795 0.2439 0.1646 0.0108 -0.0301 -0.0066 215 ARG A CG 3089 C CD . ARG A 207 ? 0.2334 0.2776 0.1697 0.0184 -0.0460 -0.0163 215 ARG A CD 3090 N NE . ARG A 207 ? 0.1942 0.2760 0.1910 0.0111 -0.0495 0.0046 215 ARG A NE 3091 C CZ . ARG A 207 ? 0.2416 0.2849 0.2012 0.0096 -0.0614 0.0088 215 ARG A CZ 3092 N NH1 . ARG A 207 ? 0.3342 0.2995 0.1935 0.0081 -0.0437 -0.0180 215 ARG A NH1 3093 N NH2 . ARG A 207 ? 0.2048 0.3001 0.1928 -0.0145 -0.0638 0.0160 215 ARG A NH2 3107 N N . TRP A 208 ? 0.1655 0.2197 0.1372 0.0148 -0.0313 -0.0084 216 TRP A N 3108 C CA . TRP A 208 ? 0.1649 0.1991 0.1477 0.0049 -0.0127 0.0029 216 TRP A CA 3109 C C . TRP A 208 ? 0.1174 0.1791 0.1588 0.0114 -0.0092 -0.0150 216 TRP A C 3110 O O . TRP A 208 ? 0.1412 0.1899 0.1579 0.0151 -0.0160 -0.0077 216 TRP A O 3111 C CB . TRP A 208 ? 0.1344 0.2144 0.1401 0.0178 -0.0015 0.0048 216 TRP A CB 3112 C CG . TRP A 208 ? 0.1446 0.1958 0.1488 0.0043 -0.0049 -0.0017 216 TRP A CG 3113 C CD1 . TRP A 208 ? 0.1541 0.2071 0.1540 0.0100 -0.0010 0.0083 216 TRP A CD1 3114 C CD2 . TRP A 208 ? 0.1558 0.1814 0.1657 0.0054 -0.0032 0.0010 216 TRP A CD2 3115 N NE1 . TRP A 208 ? 0.1673 0.2184 0.1854 -0.0133 0.0126 0.0096 216 TRP A NE1 3116 C CE2 . TRP A 208 ? 0.1488 0.2163 0.1735 -0.0111 0.0010 -0.0038 216 TRP A CE2 3117 C CE3 . TRP A 208 ? 0.1309 0.2471 0.1556 -0.0018 -0.0054 0.0149 216 TRP A CE3 3118 C CZ2 . TRP A 208 ? 0.1420 0.2259 0.1913 0.0024 -0.0161 -0.0335 216 TRP A CZ2 3119 C CZ3 . TRP A 208 ? 0.1359 0.2584 0.1657 -0.0131 -0.0130 0.0108 216 TRP A CZ3 3120 C CH2 . TRP A 208 ? 0.1338 0.2752 0.1812 -0.0019 -0.0234 -0.0311 216 TRP A CH2 3131 N N . LEU A 209 ? 0.1328 0.1763 0.1431 -0.0049 0.0016 -0.0129 217 LEU A N 3132 C CA . LEU A 209 ? 0.1286 0.1618 0.1552 -0.0014 -0.0056 -0.0097 217 LEU A CA 3133 C C . LEU A 209 ? 0.1254 0.1881 0.1525 0.0138 -0.0059 -0.0182 217 LEU A C 3134 O O . LEU A 209 ? 0.1504 0.1998 0.1426 0.0148 -0.0150 -0.0077 217 LEU A O 3135 C CB . LEU A 209 ? 0.1319 0.1991 0.1695 -0.0031 0.0061 -0.0063 217 LEU A CB 3136 C CG . LEU A 209 ? 0.1155 0.2294 0.1498 0.0000 -0.0129 -0.0037 217 LEU A CG 3137 C CD1 . LEU A 209 ? 0.1445 0.2319 0.1565 0.0034 -0.0108 -0.0012 217 LEU A CD1 3138 C CD2 . LEU A 209 ? 0.1612 0.2335 0.1655 -0.0015 -0.0004 0.0186 217 LEU A CD2 3150 N N . GLY A 210 ? 0.1514 0.1809 0.1650 0.0239 -0.0328 -0.0122 218 GLY A N 3151 C CA . GLY A 210 ? 0.1407 0.1906 0.1768 0.0078 -0.0207 0.0028 218 GLY A CA 3152 C C . GLY A 210 ? 0.1478 0.2048 0.1790 0.0089 -0.0219 -0.0150 218 GLY A C 3153 O O . GLY A 210 ? 0.1477 0.1981 0.1883 0.0067 -0.0167 -0.0051 218 GLY A O 3157 N N . ASP A 211 ? 0.1503 0.2097 0.1647 0.0162 -0.0234 0.0049 219 ASP A N 3158 C CA . ASP A 211 ? 0.1392 0.2049 0.1793 0.0149 -0.0169 0.0161 219 ASP A CA 3159 C C . ASP A 211 ? 0.1515 0.1776 0.1722 0.0000 -0.0189 0.0039 219 ASP A C 3160 O O . ASP A 211 ? 0.1855 0.2003 0.1636 0.0196 -0.0221 0.0131 219 ASP A O 3161 C CB . ASP A 211 ? 0.1747 0.2214 0.1794 0.0026 -0.0091 -0.0030 219 ASP A CB 3162 C CG . ASP A 211 ? 0.2164 0.2794 0.2056 0.0333 -0.0216 -0.0174 219 ASP A CG 3163 O OD1 . ASP A 211 ? 0.2538 0.2971 0.2077 0.0305 -0.0540 -0.0280 219 ASP A OD1 3164 O OD2 . ASP A 211 ? 0.2830 0.3608 0.2208 0.0278 -0.0304 -0.0406 219 ASP A OD2 3169 N N . VAL A 212 ? 0.1487 0.1913 0.1631 0.0160 -0.0248 0.0024 220 VAL A N 3170 C CA . VAL A 212 ? 0.1727 0.1552 0.1673 0.0051 -0.0218 -0.0027 220 VAL A CA 3171 C C . VAL A 212 ? 0.1716 0.1753 0.1577 0.0130 -0.0240 -0.0221 220 VAL A C 3172 O O . VAL A 212 ? 0.1735 0.1677 0.1720 0.0149 -0.0286 -0.0077 220 VAL A O 3173 C CB . VAL A 212 ? 0.1470 0.2014 0.1790 0.0007 -0.0295 -0.0160 220 VAL A CB 3174 C CG1 . VAL A 212 ? 0.1742 0.2206 0.1957 0.0087 -0.0243 -0.0123 220 VAL A CG1 3175 C CG2 . VAL A 212 ? 0.1505 0.2175 0.2072 0.0112 -0.0226 -0.0177 220 VAL A CG2 3185 N N . LEU A 213 ? 0.1504 0.1928 0.1640 0.0141 -0.0091 -0.0016 221 LEU A N 3186 C CA . LEU A 213 ? 0.1534 0.1823 0.1732 0.0299 -0.0127 0.0063 221 LEU A CA 3187 C C . LEU A 213 ? 0.1693 0.1935 0.1803 0.0179 -0.0078 -0.0087 221 LEU A C 3188 O O . LEU A 213 ? 0.1912 0.1878 0.1820 0.0397 -0.0061 -0.0115 221 LEU A O 3189 C CB . LEU A 213 ? 0.1525 0.1862 0.1674 -0.0020 -0.0026 -0.0023 221 LEU A CB 3190 C CG . LEU A 213 ? 0.1651 0.1785 0.1574 0.0021 -0.0173 0.0155 221 LEU A CG 3191 C CD1 . LEU A 213 ? 0.1541 0.2003 0.1926 0.0106 -0.0165 0.0295 221 LEU A CD1 3192 C CD2 . LEU A 213 ? 0.2029 0.2270 0.1662 0.0183 -0.0182 0.0077 221 LEU A CD2 3204 N N . SER A 214 ? 0.1699 0.2105 0.1744 0.0153 -0.0267 -0.0105 222 SER A N 3205 C CA . SER A 214 ? 0.1624 0.2111 0.1994 0.0331 -0.0187 -0.0125 222 SER A CA 3206 C C . SER A 214 ? 0.1797 0.1968 0.1746 0.0506 -0.0369 0.0069 222 SER A C 3207 O O . SER A 214 ? 0.1901 0.2214 0.1867 0.0459 -0.0178 0.0138 222 SER A O 3208 C CB . SER A 214 ? 0.1898 0.2341 0.2111 0.0295 -0.0490 -0.0006 222 SER A CB 3209 O OG . SER A 214 ? 0.2192 0.2663 0.2149 0.0074 -0.0391 0.0001 222 SER A OG 3215 N N . ASN A 215 ? 0.1897 0.1935 0.1814 0.0421 -0.0239 -0.0008 223 ASN A N 3216 C CA . ASN A 215 ? 0.2140 0.1824 0.1827 0.0420 -0.0219 0.0074 223 ASN A CA 3217 C C . ASN A 215 ? 0.2219 0.1877 0.1842 0.0454 -0.0275 0.0004 223 ASN A C 3218 O O . ASN A 215 ? 0.2273 0.2237 0.1832 0.0634 -0.0287 -0.0067 223 ASN A O 3219 C CB . ASN A 215 ? 0.2650 0.1794 0.1816 0.0557 -0.0232 0.0168 223 ASN A CB 3220 C CG . ASN A 215 ? 0.3615 0.2221 0.1604 0.0566 -0.0319 0.0477 223 ASN A CG 3221 O OD1 . ASN A 215 ? 0.3551 0.2651 0.1668 0.0663 -0.0681 0.0227 223 ASN A OD1 3222 N ND2 . ASN A 215 ? 0.3220 0.2517 0.1810 0.0243 -0.0195 0.0213 223 ASN A ND2 3228 N N . ALA A 216 ? 0.2375 0.1755 0.1710 0.0464 -0.0407 0.0069 224 ALA A N 3229 C CA . ALA A 216 ? 0.2585 0.1747 0.1797 0.0603 -0.0213 0.0062 224 ALA A CA 3230 C C . ALA A 216 ? 0.2682 0.1970 0.1841 0.0696 -0.0223 0.0100 224 ALA A C 3231 O O . ALA A 216 ? 0.3156 0.1767 0.1962 0.0855 -0.0166 0.0029 224 ALA A O 3232 C CB . ALA A 216 ? 0.2773 0.1775 0.1783 0.0503 -0.0174 0.0068 224 ALA A CB 3238 N N . SER A 217 ? 0.2463 0.2049 0.1764 0.0537 0.0171 0.0017 225 SER A N 3239 C CA . SER A 217 ? 0.2607 0.2384 0.2023 0.0666 0.0165 0.0231 225 SER A CA 3240 C C . SER A 217 ? 0.2760 0.2402 0.2116 0.0772 -0.0022 0.0018 225 SER A C 3241 O O . SER A 217 ? 0.2764 0.2282 0.2362 0.0755 0.0022 0.0152 225 SER A O 3242 C CB . SER A 217 ? 0.2173 0.3060 0.2608 0.0839 -0.0014 0.0379 225 SER A CB 3243 O OG . SER A 217 ? 0.2566 0.3571 0.3200 0.0609 0.0432 -0.0003 225 SER A OG 3249 N N . ARG A 218 ? 0.2529 0.2191 0.1985 0.0872 -0.0193 0.0095 226 ARG A N 3250 C CA . ARG A 218 ? 0.2277 0.2467 0.2110 0.0622 -0.0315 -0.0101 226 ARG A CA 3251 C C . ARG A 218 ? 0.2779 0.2102 0.2210 0.0753 -0.0245 0.0160 226 ARG A C 3252 O O . ARG A 218 ? 0.3185 0.2168 0.2453 0.0871 -0.0237 0.0101 226 ARG A O 3253 C CB . ARG A 218 ? 0.2180 0.2561 0.2041 0.0653 -0.0205 -0.0010 226 ARG A CB 3254 C CG . ARG A 218 ? 0.2587 0.2423 0.2123 0.0704 -0.0286 0.0081 226 ARG A CG 3255 C CD . ARG A 218 ? 0.2802 0.2572 0.2170 0.0457 -0.0183 0.0226 226 ARG A CD 3256 N NE . ARG A 218 ? 0.2949 0.2506 0.2293 0.0455 0.0015 0.0313 226 ARG A NE 3257 C CZ . ARG A 218 ? 0.2955 0.2669 0.2106 0.0332 -0.0014 0.0235 226 ARG A CZ 3258 N NH1 . ARG A 218 ? 0.2932 0.2970 0.1999 0.0591 0.0142 -0.0117 226 ARG A NH1 3259 N NH2 . ARG A 218 ? 0.3100 0.2635 0.2332 0.0151 -0.0089 0.0236 226 ARG A NH2 3273 N N . ASP A 219 ? 0.2810 0.2341 0.2178 0.0913 -0.0390 0.0124 227 ASP A N 3274 C CA . ASP A 219 ? 0.3105 0.2048 0.2479 0.0673 -0.0395 -0.0087 227 ASP A CA 3275 C C . ASP A 219 ? 0.3307 0.2069 0.2447 0.0528 -0.0510 0.0088 227 ASP A C 3276 O O . ASP A 219 ? 0.3980 0.2429 0.2779 0.0390 -0.0092 -0.0074 227 ASP A O 3277 C CB . ASP A 219 ? 0.3067 0.1934 0.2737 0.0493 -0.0265 -0.0168 227 ASP A CB 3278 C CG . ASP A 219 ? 0.3388 0.2350 0.2913 0.0280 -0.0111 -0.0044 227 ASP A CG 3279 O OD1 . ASP A 219 ? 0.3558 0.2273 0.2770 0.0191 -0.0086 0.0238 227 ASP A OD1 3280 O OD2 . ASP A 219 ? 0.3327 0.2461 0.3016 0.0123 -0.0116 0.0068 227 ASP A OD2 3285 N N . GLY A 220 ? 0.2803 0.2102 0.2354 0.0877 -0.0353 0.0108 228 GLY A N 3286 C CA . GLY A 220 ? 0.2945 0.2263 0.2289 0.0739 -0.0287 -0.0094 228 GLY A CA 3287 C C . GLY A 220 ? 0.2831 0.2161 0.2328 0.0817 -0.0386 -0.0092 228 GLY A C 3288 O O . GLY A 220 ? 0.3033 0.2797 0.2418 0.0695 -0.0538 -0.0377 228 GLY A O 3292 N N . GLU A 221 ? 0.2701 0.2025 0.2144 0.0692 -0.0495 -0.0271 229 GLU A N 3293 C CA . GLU A 221 ? 0.2167 0.1956 0.2205 0.0354 -0.0564 -0.0119 229 GLU A CA 3294 C C . GLU A 221 ? 0.2240 0.1894 0.2373 0.0257 -0.0527 -0.0109 229 GLU A C 3295 O O . GLU A 221 ? 0.2538 0.2508 0.2569 0.0095 -0.0803 0.0342 229 GLU A O 3296 C CB . GLU A 221 ? 0.2393 0.2080 0.2481 0.0328 -0.0525 0.0084 229 GLU A CB 3297 C CG . GLU A 221 ? 0.2687 0.2484 0.2825 0.0098 -0.0441 0.0155 229 GLU A CG 3298 C CD . GLU A 221 ? 0.3224 0.3204 0.3196 -0.0142 -0.0213 0.0528 229 GLU A CD 3299 O OE1 . GLU A 221 ? 0.3046 0.3863 0.3344 0.0577 -0.0035 0.0502 229 GLU A OE1 3300 O OE2 . GLU A 221 ? 0.4121 0.4024 0.3723 -0.0346 0.0297 0.0386 229 GLU A OE2 3307 N N . MET A 222 ? 0.2128 0.1814 0.2190 0.0498 -0.0369 0.0004 230 MET A N 3308 C CA A MET A 222 ? 0.1692 0.1710 0.2032 0.0469 -0.0243 -0.0233 230 MET A CA 3309 C CA B MET A 222 ? 0.1705 0.1799 0.2117 0.0431 -0.0208 -0.0169 230 MET A CA 3310 C C . MET A 222 ? 0.1446 0.1986 0.2048 0.0252 -0.0259 -0.0154 230 MET A C 3311 O O . MET A 222 ? 0.1773 0.1704 0.2264 0.0114 -0.0241 -0.0143 230 MET A O 3312 C CB A MET A 222 ? 0.1913 0.2071 0.2101 0.0505 -0.0242 -0.0348 230 MET A CB 3313 C CB B MET A 222 ? 0.1669 0.1902 0.2178 0.0486 -0.0046 -0.0297 230 MET A CB 3314 C CG A MET A 222 ? 0.2319 0.2434 0.2239 0.0583 -0.0302 -0.0201 230 MET A CG 3315 C CG B MET A 222 ? 0.1592 0.1987 0.2262 0.0582 0.0110 -0.0333 230 MET A CG 3316 S SD A MET A 222 ? 0.2420 0.2578 0.2253 0.0417 -0.0290 -0.0046 230 MET A SD 3317 S SD B MET A 222 ? 0.1096 0.1860 0.2268 0.0513 0.0278 -0.0384 230 MET A SD 3318 C CE A MET A 222 ? 0.2097 0.1976 0.2042 0.0340 -0.0120 -0.0219 230 MET A CE 3319 C CE B MET A 222 ? 0.0738 0.1421 0.2162 0.0327 0.0091 -0.0352 230 MET A CE 3336 N N . VAL A 223 ? 0.1560 0.1746 0.1871 0.0251 0.0010 -0.0104 231 VAL A N 3337 C CA . VAL A 223 ? 0.1507 0.1772 0.1645 0.0221 -0.0021 0.0003 231 VAL A CA 3338 C C . VAL A 223 ? 0.1505 0.1664 0.1645 0.0224 0.0064 -0.0018 231 VAL A C 3339 O O . VAL A 223 ? 0.1489 0.2025 0.1881 0.0163 -0.0076 0.0037 231 VAL A O 3340 C CB . VAL A 223 ? 0.2097 0.1884 0.1732 0.0381 -0.0178 -0.0076 231 VAL A CB 3341 C CG1 . VAL A 223 ? 0.2387 0.2343 0.1931 0.0166 -0.0184 -0.0223 231 VAL A CG1 3342 C CG2 . VAL A 223 ? 0.2368 0.1935 0.1747 0.0336 -0.0357 0.0015 231 VAL A CG2 3352 N N . TYR A 224 ? 0.1355 0.1658 0.1633 0.0245 -0.0093 -0.0089 232 TYR A N 3353 C CA . TYR A 224 ? 0.1550 0.1602 0.1435 0.0126 -0.0039 -0.0018 232 TYR A CA 3354 C C . TYR A 224 ? 0.1340 0.1537 0.1503 0.0019 -0.0009 0.0007 232 TYR A C 3355 O O . TYR A 224 ? 0.1555 0.1667 0.1731 -0.0078 0.0263 0.0077 232 TYR A O 3356 C CB . TYR A 224 ? 0.1349 0.1741 0.1550 0.0232 -0.0098 -0.0203 232 TYR A CB 3357 C CG . TYR A 224 ? 0.1364 0.1689 0.1613 0.0234 -0.0006 -0.0128 232 TYR A CG 3358 C CD1 . TYR A 224 ? 0.1596 0.1712 0.1672 0.0337 0.0060 -0.0094 232 TYR A CD1 3359 C CD2 . TYR A 224 ? 0.1364 0.1982 0.1687 0.0097 -0.0027 -0.0118 232 TYR A CD2 3360 C CE1 . TYR A 224 ? 0.1378 0.1616 0.1700 0.0189 -0.0028 -0.0096 232 TYR A CE1 3361 C CE2 . TYR A 224 ? 0.1427 0.1867 0.1639 0.0037 0.0006 -0.0259 232 TYR A CE2 3362 C CZ . TYR A 224 ? 0.1504 0.1698 0.1634 0.0263 -0.0163 -0.0114 232 TYR A CZ 3363 O OH . TYR A 224 ? 0.1670 0.1975 0.1585 0.0150 -0.0006 -0.0464 232 TYR A OH 3373 N N . VAL A 225 ? 0.1263 0.1607 0.1460 0.0193 0.0040 0.0055 233 VAL A N 3374 C CA . VAL A 225 ? 0.1223 0.1615 0.1445 0.0201 0.0143 0.0051 233 VAL A CA 3375 C C . VAL A 225 ? 0.1221 0.1648 0.1410 -0.0038 0.0099 0.0005 233 VAL A C 3376 O O . VAL A 225 ? 0.1427 0.1946 0.1426 0.0195 0.0119 0.0210 233 VAL A O 3377 C CB . VAL A 225 ? 0.1153 0.1946 0.1660 0.0054 0.0134 -0.0028 233 VAL A CB 3378 C CG1 . VAL A 225 ? 0.1478 0.2131 0.1543 0.0101 -0.0030 -0.0248 233 VAL A CG1 3379 C CG2 . VAL A 225 ? 0.1293 0.1936 0.1691 -0.0022 -0.0042 0.0069 233 VAL A CG2 3389 N N . ILE A 226 ? 0.1306 0.1574 0.1299 0.0013 0.0095 0.0035 234 ILE A N 3390 C CA . ILE A 226 ? 0.1198 0.1482 0.1386 0.0237 0.0076 0.0017 234 ILE A CA 3391 C C . ILE A 226 ? 0.1089 0.1607 0.1361 0.0051 -0.0096 -0.0070 234 ILE A C 3392 O O . ILE A 226 ? 0.1222 0.1599 0.1395 0.0097 0.0019 -0.0048 234 ILE A O 3393 C CB . ILE A 226 ? 0.1429 0.1661 0.1484 -0.0100 -0.0032 0.0026 234 ILE A CB 3394 C CG1 . ILE A 226 ? 0.1364 0.1596 0.1601 -0.0008 -0.0127 -0.0020 234 ILE A CG1 3395 C CG2 . ILE A 226 ? 0.1775 0.1830 0.1570 0.0018 0.0080 -0.0120 234 ILE A CG2 3396 C CD1 . ILE A 226 ? 0.1604 0.1691 0.1630 -0.0158 -0.0076 0.0031 234 ILE A CD1 3408 N N . GLY A 227 ? 0.1091 0.1558 0.1358 0.0247 0.0066 -0.0065 235 GLY A N 3409 C CA . GLY A 227 ? 0.1110 0.1774 0.1471 0.0024 -0.0062 -0.0195 235 GLY A CA 3410 C C . GLY A 227 ? 0.1180 0.1472 0.1400 0.0128 0.0026 -0.0153 235 GLY A C 3411 O O . GLY A 227 ? 0.1084 0.1697 0.1358 0.0073 0.0026 -0.0064 235 GLY A O 3415 N N . HIS A 228 ? 0.1190 0.1589 0.1253 -0.0082 -0.0042 -0.0106 236 HIS A N 3416 C CA . HIS A 228 ? 0.1145 0.1610 0.1336 0.0197 -0.0049 -0.0292 236 HIS A CA 3417 C C . HIS A 228 ? 0.1090 0.1568 0.1368 -0.0042 0.0097 -0.0005 236 HIS A C 3418 O O . HIS A 228 ? 0.1096 0.1586 0.1387 -0.0034 0.0128 -0.0011 236 HIS A O 3419 C CB . HIS A 228 ? 0.1133 0.1508 0.1362 0.0073 -0.0017 -0.0266 236 HIS A CB 3420 C CG . HIS A 228 ? 0.0716 0.1632 0.1456 -0.0130 -0.0001 -0.0024 236 HIS A CG 3421 N ND1 . HIS A 228 ? 0.0951 0.1667 0.1472 -0.0075 -0.0046 -0.0124 236 HIS A ND1 3422 C CD2 . HIS A 228 ? 0.1010 0.1546 0.1505 -0.0024 -0.0087 -0.0012 236 HIS A CD2 3423 C CE1 . HIS A 228 ? 0.0946 0.1659 0.1471 0.0049 -0.0071 0.0018 236 HIS A CE1 3424 N NE2 . HIS A 228 ? 0.1118 0.1352 0.1639 -0.0068 0.0046 -0.0055 236 HIS A NE2 3432 N N . VAL A 229 ? 0.1038 0.1634 0.1329 -0.0157 0.0155 -0.0114 237 VAL A N 3433 C CA . VAL A 229 ? 0.1158 0.1526 0.1312 -0.0187 0.0052 -0.0083 237 VAL A CA 3434 C C . VAL A 229 ? 0.1075 0.1559 0.1344 -0.0124 0.0003 -0.0244 237 VAL A C 3435 O O . VAL A 229 ? 0.1151 0.1598 0.1399 -0.0083 0.0004 -0.0131 237 VAL A O 3436 C CB . VAL A 229 ? 0.1177 0.1513 0.1472 -0.0060 -0.0014 -0.0037 237 VAL A CB 3437 C CG1 . VAL A 229 ? 0.1655 0.1334 0.1564 -0.0024 -0.0063 -0.0052 237 VAL A CG1 3438 C CG2 . VAL A 229 ? 0.1296 0.1482 0.1636 -0.0030 0.0023 -0.0169 237 VAL A CG2 3448 N N . PRO A 230 ? 0.1009 0.1763 0.1417 -0.0101 -0.0028 -0.0093 238 PRO A N 3449 C CA . PRO A 230 ? 0.0971 0.1693 0.1434 -0.0013 0.0074 -0.0109 238 PRO A CA 3450 C C . PRO A 230 ? 0.1208 0.1624 0.1419 -0.0166 0.0012 -0.0141 238 PRO A C 3451 O O . PRO A 230 ? 0.1009 0.1845 0.1458 -0.0097 0.0008 -0.0171 238 PRO A O 3452 C CB . PRO A 230 ? 0.1210 0.1770 0.1324 0.0010 -0.0215 -0.0081 238 PRO A CB 3453 C CG . PRO A 230 ? 0.1112 0.2025 0.1412 -0.0261 0.0128 0.0004 238 PRO A CG 3454 C CD . PRO A 230 ? 0.1115 0.1657 0.1460 -0.0143 -0.0024 0.0087 238 PRO A CD 3462 N N . PRO A 231 ? 0.1070 0.1611 0.1437 -0.0097 -0.0154 -0.0067 239 PRO A N 3463 C CA . PRO A 231 ? 0.1036 0.1858 0.1507 -0.0130 -0.0198 -0.0076 239 PRO A CA 3464 C C . PRO A 231 ? 0.1275 0.1508 0.1498 -0.0092 -0.0116 -0.0099 239 PRO A C 3465 O O . PRO A 231 ? 0.1248 0.1718 0.1448 -0.0123 -0.0022 -0.0096 239 PRO A O 3466 C CB . PRO A 231 ? 0.0982 0.2098 0.1541 -0.0051 -0.0020 -0.0189 239 PRO A CB 3467 C CG . PRO A 231 ? 0.1003 0.1908 0.1648 0.0053 -0.0206 0.0008 239 PRO A CG 3468 C CD . PRO A 231 ? 0.1221 0.1480 0.1547 0.0083 -0.0145 -0.0017 239 PRO A CD 3476 N N . GLY A 232 ? 0.1271 0.1652 0.1587 -0.0107 -0.0103 -0.0180 240 GLY A N 3477 C CA . GLY A 232 ? 0.1345 0.1796 0.1678 -0.0322 -0.0132 -0.0047 240 GLY A CA 3478 C C . GLY A 232 ? 0.1356 0.1630 0.1706 0.0018 -0.0145 -0.0182 240 GLY A C 3479 O O . GLY A 232 ? 0.1376 0.1729 0.1565 -0.0099 0.0005 -0.0092 240 GLY A O 3483 N N . PHE A 233 ? 0.1203 0.1477 0.1649 -0.0035 -0.0101 -0.0100 241 PHE A N 3484 C CA . PHE A 233 ? 0.1310 0.1633 0.1729 0.0015 -0.0077 0.0039 241 PHE A CA 3485 C C . PHE A 233 ? 0.1438 0.1381 0.1630 -0.0084 -0.0165 0.0017 241 PHE A C 3486 O O . PHE A 233 ? 0.1565 0.1399 0.1844 -0.0052 -0.0101 -0.0073 241 PHE A O 3487 C CB . PHE A 233 ? 0.1306 0.1781 0.1866 -0.0396 0.0024 0.0007 241 PHE A CB 3488 C CG . PHE A 233 ? 0.1416 0.1746 0.1904 -0.0301 -0.0087 -0.0145 241 PHE A CG 3489 C CD1 . PHE A 233 ? 0.1534 0.1683 0.2033 -0.0411 -0.0080 -0.0205 241 PHE A CD1 3490 C CD2 . PHE A 233 ? 0.1367 0.2008 0.2073 -0.0446 0.0031 -0.0044 241 PHE A CD2 3491 C CE1 . PHE A 233 ? 0.1469 0.1922 0.2315 -0.0205 -0.0073 -0.0189 241 PHE A CE1 3492 C CE2 . PHE A 233 ? 0.1520 0.2083 0.2368 -0.0358 -0.0123 -0.0210 241 PHE A CE2 3493 C CZ . PHE A 233 ? 0.1408 0.2067 0.2380 -0.0209 -0.0118 -0.0262 241 PHE A CZ 3503 N N . PHE A 234 ? 0.1405 0.1448 0.1784 -0.0177 -0.0162 -0.0024 242 PHE A N 3504 C CA . PHE A 234 ? 0.1318 0.1535 0.1853 -0.0223 -0.0265 0.0051 242 PHE A CA 3505 C C . PHE A 234 ? 0.1366 0.1200 0.1812 -0.0185 -0.0163 0.0064 242 PHE A C 3506 O O . PHE A 234 ? 0.1711 0.1550 0.1898 -0.0320 0.0063 -0.0110 242 PHE A O 3507 C CB . PHE A 234 ? 0.1234 0.1477 0.1705 -0.0070 -0.0108 0.0021 242 PHE A CB 3508 C CG . PHE A 234 ? 0.1336 0.1369 0.2010 -0.0043 -0.0100 0.0042 242 PHE A CG 3509 C CD1 . PHE A 234 ? 0.1442 0.1418 0.1965 -0.0048 -0.0239 0.0182 242 PHE A CD1 3510 C CD2 . PHE A 234 ? 0.1577 0.1492 0.2220 -0.0092 -0.0065 -0.0068 242 PHE A CD2 3511 C CE1 . PHE A 234 ? 0.1578 0.1518 0.2290 -0.0111 -0.0088 -0.0103 242 PHE A CE1 3512 C CE2 . PHE A 234 ? 0.1630 0.1864 0.2492 0.0162 -0.0383 0.0183 242 PHE A CE2 3513 C CZ . PHE A 234 ? 0.1673 0.1732 0.2478 -0.0125 -0.0317 0.0081 242 PHE A CZ 3523 N N . GLU A 235 ? 0.1264 0.1504 0.1761 -0.0179 0.0099 0.0036 243 GLU A N 3524 C CA . GLU A 235 ? 0.1450 0.1658 0.1713 -0.0195 0.0108 0.0044 243 GLU A CA 3525 C C . GLU A 235 ? 0.1656 0.1783 0.1780 -0.0324 0.0129 0.0040 243 GLU A C 3526 O O . GLU A 235 ? 0.1831 0.1865 0.1956 -0.0133 0.0204 0.0135 243 GLU A O 3527 C CB . GLU A 235 ? 0.1225 0.1789 0.1678 -0.0268 0.0172 0.0012 243 GLU A CB 3528 C CG . GLU A 235 ? 0.1394 0.1895 0.1576 -0.0062 0.0126 0.0155 243 GLU A CG 3529 C CD . GLU A 235 ? 0.1165 0.1803 0.1527 0.0283 -0.0171 -0.0010 243 GLU A CD 3530 O OE1 . GLU A 235 ? 0.1351 0.1505 0.1572 -0.0034 -0.0113 -0.0033 243 GLU A OE1 3531 O OE2 . GLU A 235 ? 0.1156 0.2001 0.1659 -0.0161 -0.0072 0.0053 243 GLU A OE2 3538 N N . LYS A 236 ? 0.1654 0.1841 0.1909 -0.0035 -0.0178 0.0180 244 LYS A N 3539 C CA . LYS A 236 ? 0.1908 0.1807 0.2161 0.0066 -0.0150 0.0042 244 LYS A CA 3540 C C . LYS A 236 ? 0.1577 0.1768 0.2330 -0.0027 0.0046 0.0261 244 LYS A C 3541 O O . LYS A 236 ? 0.2124 0.1653 0.2437 0.0057 -0.0208 0.0095 244 LYS A O 3542 C CB . LYS A 236 ? 0.2099 0.2184 0.2480 -0.0003 -0.0499 -0.0078 244 LYS A CB 3543 C CG . LYS A 236 ? 0.2333 0.2643 0.2913 0.0076 -0.0688 -0.0404 244 LYS A CG 3544 C CD . LYS A 236 ? 0.3066 0.2980 0.3275 0.0953 -0.0609 -0.0292 244 LYS A CD 3545 C CE . LYS A 236 ? 0.3419 0.3762 0.3465 0.0841 -0.0768 -0.0456 244 LYS A CE 3546 N NZ . LYS A 236 ? 0.3377 0.3903 0.3734 0.0591 -0.0689 -0.0357 244 LYS A NZ 3560 N N . THR A 237 ? 0.1659 0.1556 0.2353 -0.0217 -0.0038 0.0215 245 THR A N 3561 C CA . THR A 237 ? 0.1753 0.1506 0.2574 0.0015 -0.0034 0.0084 245 THR A CA 3562 C C . THR A 237 ? 0.1826 0.1262 0.2409 -0.0133 0.0136 0.0177 245 THR A C 3563 O O . THR A 237 ? 0.1749 0.1834 0.2270 -0.0065 0.0121 0.0046 245 THR A O 3564 C CB . THR A 237 ? 0.1992 0.1526 0.2772 0.0055 0.0044 -0.0088 245 THR A CB 3565 O OG1 . THR A 237 ? 0.2158 0.1593 0.3197 0.0065 0.0281 -0.0003 245 THR A OG1 3566 C CG2 . THR A 237 ? 0.2020 0.1807 0.2502 -0.0075 0.0088 -0.0163 245 THR A CG2 3574 N N . GLN A 238 ? 0.2008 0.1253 0.2425 -0.0158 -0.0149 0.0152 246 GLN A N 3575 C CA . GLN A 238 ? 0.2038 0.1516 0.2520 -0.0234 0.0031 0.0175 246 GLN A CA 3576 C C . GLN A 238 ? 0.2025 0.1642 0.2514 -0.0462 -0.0127 -0.0081 246 GLN A C 3577 O O . GLN A 238 ? 0.2204 0.1754 0.2655 -0.0217 0.0088 -0.0008 246 GLN A O 3578 C CB . GLN A 238 ? 0.2030 0.2031 0.2708 -0.0309 -0.0229 0.0142 246 GLN A CB 3579 C CG . GLN A 238 ? 0.2948 0.2549 0.3083 -0.0301 -0.0039 0.0295 246 GLN A CG 3580 C CD . GLN A 238 ? 0.3853 0.3367 0.3525 -0.0240 0.0195 0.0610 246 GLN A CD 3581 O OE1 . GLN A 238 ? 0.4551 0.3464 0.3828 0.0114 0.0551 0.0640 246 GLN A OE1 3582 N NE2 . GLN A 238 ? 0.4212 0.3423 0.3781 -0.0840 0.0441 0.0566 246 GLN A NE2 3591 N N . ASN A 239 ? 0.2309 0.1709 0.2482 -0.0581 -0.0165 -0.0040 247 ASN A N 3592 C CA . ASN A 239 ? 0.2471 0.1593 0.2502 -0.0207 -0.0238 -0.0279 247 ASN A CA 3593 C C . ASN A 239 ? 0.2302 0.1777 0.2367 -0.0112 -0.0075 -0.0222 247 ASN A C 3594 O O . ASN A 239 ? 0.2506 0.2018 0.2772 -0.0423 0.0168 -0.0558 247 ASN A O 3595 C CB . ASN A 239 ? 0.3477 0.2202 0.3063 -0.0877 -0.0025 -0.0532 247 ASN A CB 3596 C CG . ASN A 239 ? 0.4526 0.2992 0.3583 -0.1342 0.0292 -0.0757 247 ASN A CG 3597 O OD1 . ASN A 239 ? 0.4959 0.3467 0.4078 -0.1423 0.0665 -0.0909 247 ASN A OD1 3598 N ND2 . ASN A 239 ? 0.5190 0.3854 0.3403 -0.1616 0.0346 -0.0918 247 ASN A ND2 3605 N N . LYS A 240 ? 0.2245 0.1349 0.2013 -0.0258 0.0042 0.0123 248 LYS A N 3606 C CA . LYS A 240 ? 0.2120 0.1526 0.1993 -0.0078 0.0112 0.0006 248 LYS A CA 3607 C C . LYS A 240 ? 0.1714 0.1627 0.1893 -0.0340 -0.0070 -0.0093 248 LYS A C 3608 O O . LYS A 240 ? 0.1616 0.1814 0.1763 -0.0134 0.0019 -0.0185 248 LYS A O 3609 C CB . LYS A 240 ? 0.2070 0.1631 0.2285 -0.0041 -0.0026 0.0155 248 LYS A CB 3610 C CG . LYS A 240 ? 0.1978 0.1502 0.2574 -0.0291 0.0013 0.0086 248 LYS A CG 3611 C CD . LYS A 240 ? 0.2486 0.2350 0.2927 -0.0242 0.0195 -0.0284 248 LYS A CD 3612 C CE . LYS A 240 ? 0.3087 0.2941 0.3226 -0.0117 0.0254 -0.0448 248 LYS A CE 3613 N NZ . LYS A 240 ? 0.3474 0.3794 0.3519 0.0047 0.0341 -0.0588 248 LYS A NZ 3627 N N . ALA A 241 ? 0.1966 0.1363 0.1958 -0.0111 -0.0081 -0.0330 249 ALA A N 3628 C CA . ALA A 241 ? 0.1703 0.1471 0.1954 -0.0052 -0.0037 -0.0275 249 ALA A CA 3629 C C . ALA A 241 ? 0.1521 0.1746 0.2149 0.0129 -0.0076 -0.0175 249 ALA A C 3630 O O . ALA A 241 ? 0.2417 0.1986 0.2686 -0.0094 0.0526 -0.0253 249 ALA A O 3631 C CB . ALA A 241 ? 0.1730 0.1732 0.1996 -0.0257 -0.0179 -0.0030 249 ALA A CB 3637 N N . TRP A 242 ? 0.1501 0.1447 0.1886 0.0148 -0.0102 -0.0284 250 TRP A N 3638 C CA . TRP A 242 ? 0.1435 0.1704 0.1751 0.0082 -0.0046 -0.0263 250 TRP A CA 3639 C C . TRP A 242 ? 0.1470 0.1707 0.1574 0.0023 -0.0103 -0.0325 250 TRP A C 3640 O O . TRP A 242 ? 0.1617 0.1787 0.1795 0.0149 -0.0127 -0.0447 250 TRP A O 3641 C CB . TRP A 242 ? 0.1390 0.1720 0.1640 0.0065 -0.0096 -0.0105 250 TRP A CB 3642 C CG . TRP A 242 ? 0.1505 0.1645 0.1645 -0.0129 -0.0030 -0.0186 250 TRP A CG 3643 C CD1 . TRP A 242 ? 0.1479 0.1637 0.1618 -0.0254 -0.0184 -0.0276 250 TRP A CD1 3644 C CD2 . TRP A 242 ? 0.1396 0.1751 0.1686 -0.0185 -0.0023 -0.0331 250 TRP A CD2 3645 N NE1 . TRP A 242 ? 0.1324 0.1870 0.1728 -0.0202 -0.0028 -0.0122 250 TRP A NE1 3646 C CE2 . TRP A 242 ? 0.1281 0.1773 0.1715 -0.0083 -0.0109 -0.0149 250 TRP A CE2 3647 C CE3 . TRP A 242 ? 0.1551 0.1687 0.1957 0.0025 -0.0058 -0.0155 250 TRP A CE3 3648 C CZ2 . TRP A 242 ? 0.1337 0.2057 0.1876 -0.0204 -0.0244 -0.0020 250 TRP A CZ2 3649 C CZ3 . TRP A 242 ? 0.1639 0.1663 0.2250 0.0071 -0.0195 -0.0165 250 TRP A CZ3 3650 C CH2 . TRP A 242 ? 0.1712 0.2066 0.2069 -0.0043 -0.0216 -0.0056 250 TRP A CH2 3661 N N . PHE A 243 ? 0.1365 0.1843 0.1570 -0.0047 -0.0166 -0.0198 251 PHE A N 3662 C CA . PHE A 243 ? 0.1478 0.1759 0.1719 -0.0092 -0.0030 -0.0240 251 PHE A CA 3663 C C . PHE A 243 ? 0.1391 0.1723 0.1842 -0.0253 -0.0217 -0.0208 251 PHE A C 3664 O O . PHE A 243 ? 0.1609 0.1964 0.1869 -0.0262 -0.0121 -0.0337 251 PHE A O 3665 C CB . PHE A 243 ? 0.1384 0.1813 0.1618 0.0002 -0.0091 -0.0179 251 PHE A CB 3666 C CG . PHE A 243 ? 0.1425 0.1654 0.1552 -0.0205 -0.0013 -0.0105 251 PHE A CG 3667 C CD1 . PHE A 243 ? 0.1284 0.1865 0.1505 -0.0102 -0.0242 -0.0142 251 PHE A CD1 3668 C CD2 . PHE A 243 ? 0.1457 0.1884 0.1725 -0.0023 -0.0077 -0.0021 251 PHE A CD2 3669 C CE1 . PHE A 243 ? 0.1249 0.1960 0.1614 -0.0148 -0.0158 -0.0174 251 PHE A CE1 3670 C CE2 . PHE A 243 ? 0.1297 0.1719 0.1858 0.0183 0.0087 0.0110 251 PHE A CE2 3671 C CZ . PHE A 243 ? 0.1399 0.1834 0.1592 -0.0145 0.0032 -0.0233 251 PHE A CZ 3681 N N . ARG A 244 ? 0.1695 0.1786 0.1849 -0.0075 -0.0130 -0.0345 252 ARG A N 3682 C CA . ARG A 244 ? 0.1687 0.1660 0.1718 -0.0126 -0.0186 -0.0397 252 ARG A CA 3683 C C . ARG A 244 ? 0.1657 0.1752 0.1840 -0.0016 -0.0255 -0.0316 252 ARG A C 3684 O O . ARG A 244 ? 0.1633 0.1745 0.1928 -0.0051 -0.0308 -0.0378 252 ARG A O 3685 C CB . ARG A 244 ? 0.1891 0.2031 0.1769 0.0062 -0.0063 -0.0522 252 ARG A CB 3686 C CG . ARG A 244 ? 0.1924 0.2343 0.2341 -0.0118 0.0194 -0.0502 252 ARG A CG 3687 C CD . ARG A 244 ? 0.2482 0.2370 0.2797 -0.0131 0.0082 -0.0942 252 ARG A CD 3688 N NE . ARG A 244 ? 0.2976 0.3095 0.3025 0.0544 -0.0079 -0.1198 252 ARG A NE 3689 C CZ . ARG A 244 ? 0.3398 0.4169 0.3623 -0.0301 0.0128 -0.0724 252 ARG A CZ 3690 N NH1 . ARG A 244 ? 0.3860 0.4499 0.3952 -0.0207 0.0405 -0.0559 252 ARG A NH1 3691 N NH2 . ARG A 244 ? 0.2739 0.4727 0.3684 -0.0386 -0.0254 -0.0344 252 ARG A NH2 3705 N N . GLU A 245 ? 0.1792 0.2001 0.2021 -0.0238 -0.0226 -0.0470 253 GLU A N 3706 C CA . GLU A 245 ? 0.1676 0.2057 0.2216 -0.0049 -0.0173 -0.0442 253 GLU A CA 3707 C C . GLU A 245 ? 0.1711 0.2035 0.2037 -0.0271 -0.0207 -0.0614 253 GLU A C 3708 O O . GLU A 245 ? 0.1658 0.2213 0.1870 -0.0200 -0.0173 -0.0399 253 GLU A O 3709 C CB . GLU A 245 ? 0.2044 0.2151 0.2577 -0.0581 -0.0011 -0.0629 253 GLU A CB 3710 C CG . GLU A 245 ? 0.2135 0.2361 0.3141 -0.0627 0.0174 -0.0527 253 GLU A CG 3711 C CD . GLU A 245 ? 0.2492 0.2757 0.3697 -0.0381 0.0341 -0.0646 253 GLU A CD 3712 O OE1 . GLU A 245 ? 0.3213 0.2862 0.4281 -0.0527 0.0672 -0.0553 253 GLU A OE1 3713 O OE2 . GLU A 245 ? 0.2602 0.3243 0.3770 -0.0389 -0.0009 -0.0358 253 GLU A OE2 3720 N N . SER A 246 ? 0.1672 0.1890 0.2150 -0.0095 -0.0164 -0.0485 254 SER A N 3721 C CA . SER A 246 ? 0.1780 0.2189 0.2044 -0.0306 -0.0117 -0.0259 254 SER A CA 3722 C C . SER A 246 ? 0.1733 0.1972 0.1830 -0.0072 -0.0116 -0.0127 254 SER A C 3723 O O . SER A 246 ? 0.1647 0.2337 0.1818 -0.0215 -0.0399 -0.0205 254 SER A O 3724 C CB . SER A 246 ? 0.2525 0.2784 0.2138 -0.0678 0.0121 -0.0516 254 SER A CB 3725 O OG . SER A 246 ? 0.3132 0.3274 0.2116 -0.0395 0.0468 -0.0585 254 SER A OG 3731 N N . PHE A 247 ? 0.1454 0.1999 0.1672 -0.0065 -0.0191 -0.0297 255 PHE A N 3732 C CA . PHE A 247 ? 0.1367 0.1989 0.1686 -0.0115 0.0083 -0.0318 255 PHE A CA 3733 C C . PHE A 247 ? 0.1076 0.2011 0.1724 0.0040 -0.0205 -0.0141 255 PHE A C 3734 O O . PHE A 247 ? 0.1281 0.2033 0.1823 -0.0098 -0.0183 -0.0110 255 PHE A O 3735 C CB . PHE A 247 ? 0.1268 0.2196 0.1683 -0.0095 -0.0143 -0.0187 255 PHE A CB 3736 C CG . PHE A 247 ? 0.1303 0.2127 0.1664 -0.0093 -0.0215 -0.0309 255 PHE A CG 3737 C CD1 . PHE A 247 ? 0.1274 0.2240 0.1869 0.0037 0.0003 -0.0319 255 PHE A CD1 3738 C CD2 . PHE A 247 ? 0.1415 0.1836 0.1763 -0.0042 -0.0073 -0.0195 255 PHE A CD2 3739 C CE1 . PHE A 247 ? 0.1491 0.2428 0.1833 0.0047 0.0078 -0.0259 255 PHE A CE1 3740 C CE2 . PHE A 247 ? 0.1385 0.1692 0.2133 -0.0025 0.0098 -0.0327 255 PHE A CE2 3741 C CZ . PHE A 247 ? 0.1701 0.2053 0.1985 -0.0173 0.0236 -0.0524 255 PHE A CZ 3751 N N . ASN A 248 ? 0.1257 0.2048 0.1639 -0.0031 -0.0206 -0.0210 256 ASN A N 3752 C CA . ASN A 248 ? 0.1224 0.1701 0.1714 -0.0053 -0.0170 -0.0209 256 ASN A CA 3753 C C . ASN A 248 ? 0.1250 0.1894 0.1632 -0.0295 -0.0017 -0.0180 256 ASN A C 3754 O O . ASN A 248 ? 0.1384 0.2044 0.1628 -0.0057 -0.0086 -0.0295 256 ASN A O 3755 C CB . ASN A 248 ? 0.1288 0.1752 0.1703 -0.0102 -0.0288 -0.0203 256 ASN A CB 3756 C CG . ASN A 248 ? 0.1552 0.1749 0.1727 -0.0205 -0.0114 -0.0221 256 ASN A CG 3757 O OD1 . ASN A 248 ? 0.1562 0.1851 0.1708 -0.0383 -0.0376 -0.0171 256 ASN A OD1 3758 N ND2 . ASN A 248 ? 0.1645 0.2134 0.1679 -0.0270 -0.0085 -0.0329 256 ASN A ND2 3765 N N . GLU A 249 ? 0.1262 0.1839 0.1876 -0.0121 -0.0279 -0.0379 257 GLU A N 3766 C CA . GLU A 249 ? 0.1364 0.2038 0.2091 -0.0337 -0.0213 -0.0482 257 GLU A CA 3767 C C . GLU A 249 ? 0.1484 0.2242 0.1926 -0.0348 -0.0183 -0.0346 257 GLU A C 3768 O O . GLU A 249 ? 0.1682 0.2246 0.2041 -0.0049 -0.0245 -0.0305 257 GLU A O 3769 C CB . GLU A 249 ? 0.1703 0.2248 0.2270 -0.0170 -0.0378 -0.0171 257 GLU A CB 3770 C CG . GLU A 249 ? 0.2390 0.2375 0.2392 -0.0567 -0.0457 -0.0268 257 GLU A CG 3771 C CD . GLU A 249 ? 0.3636 0.3179 0.2780 -0.0708 -0.0487 -0.0140 257 GLU A CD 3772 O OE1 . GLU A 249 ? 0.4259 0.3060 0.3029 -0.0668 -0.0334 -0.0359 257 GLU A OE1 3773 O OE2 . GLU A 249 ? 0.3721 0.3471 0.2875 -0.0914 -0.0938 -0.0134 257 GLU A OE2 3780 N N . GLU A 250 ? 0.1472 0.2118 0.1772 0.0006 -0.0281 -0.0166 258 GLU A N 3781 C CA . GLU A 250 ? 0.1694 0.2324 0.1695 0.0081 -0.0151 -0.0002 258 GLU A CA 3782 C C . GLU A 250 ? 0.1394 0.2219 0.1886 0.0062 -0.0097 -0.0098 258 GLU A C 3783 O O . GLU A 250 ? 0.1525 0.2054 0.1814 0.0040 -0.0326 0.0042 258 GLU A O 3784 C CB . GLU A 250 ? 0.2415 0.2723 0.1758 -0.0067 -0.0136 -0.0120 258 GLU A CB 3785 C CG . GLU A 250 ? 0.3257 0.3762 0.2364 -0.0027 -0.0250 0.0007 258 GLU A CG 3786 C CD . GLU A 250 ? 0.4329 0.4747 0.3349 0.0131 -0.0408 0.0147 258 GLU A CD 3787 O OE1 . GLU A 250 ? 0.3980 0.5186 0.3158 0.0000 -0.1388 0.0141 258 GLU A OE1 3788 O OE2 . GLU A 250 ? 0.5104 0.5384 0.4021 0.0425 -0.0081 0.0149 258 GLU A OE2 3795 N N . TYR A 251 ? 0.1473 0.1849 0.1831 0.0013 -0.0254 -0.0192 259 TYR A N 3796 C CA . TYR A 251 ? 0.1419 0.2069 0.1890 -0.0132 -0.0185 -0.0194 259 TYR A CA 3797 C C . TYR A 251 ? 0.1141 0.1870 0.1789 0.0172 -0.0386 -0.0298 259 TYR A C 3798 O O . TYR A 251 ? 0.1376 0.1914 0.1942 0.0127 -0.0289 -0.0273 259 TYR A O 3799 C CB . TYR A 251 ? 0.1462 0.1850 0.1861 -0.0149 -0.0396 -0.0032 259 TYR A CB 3800 C CG . TYR A 251 ? 0.1359 0.1935 0.1748 -0.0073 -0.0137 -0.0174 259 TYR A CG 3801 C CD1 . TYR A 251 ? 0.1325 0.2268 0.1752 -0.0258 -0.0142 -0.0175 259 TYR A CD1 3802 C CD2 . TYR A 251 ? 0.1204 0.2063 0.1670 -0.0099 -0.0249 -0.0046 259 TYR A CD2 3803 C CE1 . TYR A 251 ? 0.1277 0.2324 0.1809 -0.0155 -0.0075 -0.0266 259 TYR A CE1 3804 C CE2 . TYR A 251 ? 0.1328 0.1982 0.1591 0.0022 -0.0082 0.0099 259 TYR A CE2 3805 C CZ . TYR A 251 ? 0.1127 0.2175 0.1690 -0.0131 -0.0155 -0.0019 259 TYR A CZ 3806 O OH . TYR A 251 ? 0.1360 0.2285 0.1932 -0.0171 -0.0186 -0.0328 259 TYR A OH 3816 N N . LEU A 252 ? 0.1347 0.1850 0.1825 -0.0100 -0.0241 -0.0251 260 LEU A N 3817 C CA . LEU A 252 ? 0.1550 0.1831 0.1873 0.0081 0.0072 -0.0206 260 LEU A CA 3818 C C . LEU A 252 ? 0.1436 0.2027 0.1927 0.0046 -0.0076 -0.0004 260 LEU A C 3819 O O . LEU A 252 ? 0.1452 0.1959 0.2151 -0.0017 -0.0090 0.0001 260 LEU A O 3820 C CB . LEU A 252 ? 0.1742 0.1883 0.2009 0.0209 0.0055 0.0005 260 LEU A CB 3821 C CG . LEU A 252 ? 0.1768 0.2095 0.2128 0.0018 -0.0119 -0.0193 260 LEU A CG 3822 C CD1 . LEU A 252 ? 0.2237 0.2008 0.2225 0.0036 0.0159 -0.0198 260 LEU A CD1 3823 C CD2 . LEU A 252 ? 0.2412 0.2642 0.2267 0.0100 0.0031 -0.0324 260 LEU A CD2 3835 N N . LYS A 253 ? 0.1380 0.2040 0.1965 -0.0072 -0.0165 -0.0065 261 LYS A N 3836 C CA . LYS A 253 ? 0.1357 0.2219 0.2159 -0.0060 -0.0220 -0.0015 261 LYS A CA 3837 C C . LYS A 253 ? 0.1547 0.2041 0.1902 0.0192 -0.0311 0.0022 261 LYS A C 3838 O O . LYS A 253 ? 0.1725 0.2150 0.2040 0.0027 -0.0281 -0.0038 261 LYS A O 3839 C CB . LYS A 253 ? 0.1807 0.2537 0.2356 0.0201 -0.0481 0.0061 261 LYS A CB 3840 C CG . LYS A 253 ? 0.2811 0.3747 0.2779 0.0129 -0.0540 -0.0266 261 LYS A CG 3841 C CD . LYS A 253 ? 0.3559 0.5180 0.3011 0.0355 -0.0982 -0.0251 261 LYS A CD 3842 C CE . LYS A 253 ? 0.4808 0.5930 0.3568 0.0167 -0.0465 -0.0385 261 LYS A CE 3843 N NZ . LYS A 253 ? 0.5438 0.6359 0.3831 -0.0150 -0.0258 -0.0582 261 LYS A NZ 3857 N N . VAL A 254 ? 0.1468 0.2066 0.2015 0.0093 -0.0274 -0.0099 262 VAL A N 3858 C CA . VAL A 254 ? 0.1567 0.2145 0.2146 0.0326 -0.0095 0.0024 262 VAL A CA 3859 C C . VAL A 254 ? 0.1351 0.1930 0.2035 -0.0023 -0.0035 0.0046 262 VAL A C 3860 O O . VAL A 254 ? 0.1431 0.1865 0.1976 0.0175 -0.0153 -0.0015 262 VAL A O 3861 C CB . VAL A 254 ? 0.1411 0.2090 0.2542 0.0192 0.0354 0.0082 262 VAL A CB 3862 C CG1 . VAL A 254 ? 0.1399 0.1903 0.2839 0.0205 0.0366 0.0303 262 VAL A CG1 3863 C CG2 . VAL A 254 ? 0.1742 0.2241 0.2686 0.0141 0.0400 0.0008 262 VAL A CG2 3873 N N . ILE A 255 ? 0.1274 0.1987 0.2025 -0.0008 -0.0222 -0.0067 263 ILE A N 3874 C CA . ILE A 255 ? 0.1526 0.1803 0.1920 0.0050 -0.0267 -0.0009 263 ILE A CA 3875 C C . ILE A 255 ? 0.1483 0.1846 0.1848 0.0051 -0.0205 0.0218 263 ILE A C 3876 O O . ILE A 255 ? 0.1500 0.2083 0.2113 0.0051 -0.0160 -0.0074 263 ILE A O 3877 C CB . ILE A 255 ? 0.1423 0.1831 0.2002 0.0064 -0.0306 0.0095 263 ILE A CB 3878 C CG1 . ILE A 255 ? 0.1382 0.1877 0.1928 -0.0101 -0.0245 0.0107 263 ILE A CG1 3879 C CG2 . ILE A 255 ? 0.1822 0.1930 0.1881 0.0241 -0.0271 0.0090 263 ILE A CG2 3880 C CD1 . ILE A 255 ? 0.1492 0.2286 0.1973 -0.0034 -0.0246 0.0280 263 ILE A CD1 3892 N N . GLN A 256 ? 0.1301 0.2194 0.1956 0.0227 0.0057 0.0125 264 GLN A N 3893 C CA . GLN A 256 ? 0.1263 0.2402 0.2133 0.0055 -0.0077 0.0095 264 GLN A CA 3894 C C . GLN A 256 ? 0.1252 0.2718 0.2007 0.0145 -0.0145 -0.0134 264 GLN A C 3895 O O . GLN A 256 ? 0.1743 0.2923 0.2264 0.0496 -0.0196 -0.0146 264 GLN A O 3896 C CB . GLN A 256 ? 0.1483 0.2585 0.2412 0.0147 -0.0328 -0.0244 264 GLN A CB 3897 C CG . GLN A 256 ? 0.2082 0.2891 0.2861 0.0292 -0.0245 -0.0110 264 GLN A CG 3898 C CD . GLN A 256 ? 0.2815 0.3274 0.3028 -0.0028 -0.0593 -0.0216 264 GLN A CD 3899 O OE1 . GLN A 256 ? 0.3044 0.3470 0.3128 -0.0185 -0.0463 -0.0372 264 GLN A OE1 3900 N NE2 . GLN A 256 ? 0.3054 0.3227 0.3054 -0.0274 -0.0583 -0.0072 264 GLN A NE2 3909 N N . LYS A 257 ? 0.1255 0.2236 0.2059 0.0221 -0.0158 -0.0056 265 LYS A N 3910 C CA . LYS A 257 ? 0.1383 0.2434 0.2145 0.0130 -0.0270 -0.0193 265 LYS A CA 3911 C C . LYS A 257 ? 0.1503 0.2280 0.2175 0.0318 -0.0290 0.0016 265 LYS A C 3912 O O . LYS A 257 ? 0.1603 0.2692 0.2340 0.0206 -0.0380 0.0041 265 LYS A O 3913 C CB . LYS A 257 ? 0.1697 0.2316 0.2125 0.0070 -0.0285 -0.0167 265 LYS A CB 3914 C CG . LYS A 257 ? 0.1953 0.2688 0.2284 0.0229 -0.0297 0.0271 265 LYS A CG 3915 C CD . LYS A 257 ? 0.2643 0.3563 0.2440 0.0356 -0.0331 0.0267 265 LYS A CD 3916 C CE . LYS A 257 ? 0.3462 0.4383 0.2494 0.0166 -0.0089 0.0243 265 LYS A CE 3917 N NZ . LYS A 257 ? 0.4289 0.5031 0.2734 0.0191 0.0137 0.0218 265 LYS A NZ 3931 N N . HIS A 258 ? 0.1265 0.2037 0.2106 -0.0020 -0.0231 0.0238 266 HIS A N 3932 C CA . HIS A 258 ? 0.1399 0.1923 0.2014 0.0203 -0.0020 0.0155 266 HIS A CA 3933 C C . HIS A 258 ? 0.1235 0.2010 0.2039 0.0151 -0.0144 0.0070 266 HIS A C 3934 O O . HIS A 258 ? 0.1383 0.1956 0.1974 0.0052 0.0004 0.0002 266 HIS A O 3935 C CB . HIS A 258 ? 0.1497 0.1869 0.1834 0.0014 -0.0054 0.0067 266 HIS A CB 3936 C CG . HIS A 258 ? 0.1420 0.2092 0.1882 0.0190 0.0073 0.0117 266 HIS A CG 3937 N ND1 . HIS A 258 ? 0.1730 0.2252 0.1937 0.0002 0.0013 0.0180 266 HIS A ND1 3938 C CD2 . HIS A 258 ? 0.1441 0.2549 0.2020 0.0019 0.0307 0.0007 266 HIS A CD2 3939 C CE1 . HIS A 258 ? 0.1851 0.2684 0.1898 0.0044 -0.0078 0.0195 266 HIS A CE1 3940 N NE2 . HIS A 258 ? 0.1737 0.2873 0.1961 -0.0036 0.0010 -0.0114 266 HIS A NE2 3948 N N . HIS A 259 ? 0.1189 0.2058 0.1956 0.0009 -0.0074 0.0120 267 HIS A N 3949 C CA . HIS A 259 ? 0.1295 0.2149 0.1808 0.0078 0.0034 0.0095 267 HIS A CA 3950 C C . HIS A 259 ? 0.1078 0.2106 0.1813 0.0193 0.0007 0.0217 267 HIS A C 3951 O O . HIS A 259 ? 0.1532 0.2219 0.1622 0.0064 -0.0062 0.0182 267 HIS A O 3952 C CB . HIS A 259 ? 0.1415 0.2296 0.1854 -0.0043 0.0206 -0.0042 267 HIS A CB 3953 C CG . HIS A 259 ? 0.1465 0.2388 0.2243 -0.0010 0.0190 0.0008 267 HIS A CG 3954 N ND1 . HIS A 259 ? 0.1498 0.2239 0.2522 -0.0166 0.0276 -0.0095 267 HIS A ND1 3955 C CD2 . HIS A 259 ? 0.1308 0.3024 0.2500 -0.0243 0.0039 -0.0271 267 HIS A CD2 3956 C CE1 . HIS A 259 ? 0.1537 0.2734 0.2635 -0.0082 0.0373 -0.0136 267 HIS A CE1 3957 N NE2 . HIS A 259 ? 0.1578 0.3185 0.2703 -0.0020 0.0165 -0.0187 267 HIS A NE2 3965 N N . ARG A 260 ? 0.1247 0.2165 0.1778 -0.0012 -0.0005 -0.0071 268 ARG A N 3966 C CA . ARG A 260 ? 0.1463 0.2129 0.2052 0.0027 -0.0017 0.0133 268 ARG A CA 3967 C C . ARG A 260 ? 0.1457 0.1860 0.2130 0.0439 -0.0139 -0.0176 268 ARG A C 3968 O O . ARG A 260 ? 0.1876 0.2219 0.2518 0.0113 0.0190 -0.0430 268 ARG A O 3969 C CB . ARG A 260 ? 0.1457 0.2537 0.2355 0.0309 -0.0002 0.0065 268 ARG A CB 3970 C CG . ARG A 260 ? 0.1800 0.3605 0.3219 0.0626 -0.0024 0.0033 268 ARG A CG 3971 C CD . ARG A 260 ? 0.2195 0.4649 0.3765 0.0070 0.0054 -0.0138 268 ARG A CD 3972 N NE . ARG A 260 ? 0.3152 0.5517 0.4061 -0.0264 0.0265 -0.0388 268 ARG A NE 3973 C CZ . ARG A 260 ? 0.3544 0.6024 0.4099 -0.0627 0.0294 -0.0663 268 ARG A CZ 3974 N NH1 . ARG A 260 ? 0.2973 0.6007 0.3933 -0.0866 -0.0265 -0.0881 268 ARG A NH1 3975 N NH2 . ARG A 260 ? 0.4037 0.6496 0.4283 -0.0542 0.0589 -0.0592 268 ARG A NH2 3989 N N . VAL A 261 ? 0.1593 0.1946 0.1840 0.0330 -0.0221 -0.0112 269 VAL A N 3990 C CA . VAL A 261 ? 0.1578 0.2002 0.1801 0.0098 -0.0124 -0.0143 269 VAL A CA 3991 C C . VAL A 261 ? 0.1486 0.1870 0.1914 -0.0025 -0.0210 -0.0128 269 VAL A C 3992 O O . VAL A 261 ? 0.1644 0.1847 0.2334 -0.0107 -0.0319 0.0301 269 VAL A O 3993 C CB . VAL A 261 ? 0.1867 0.2045 0.1922 0.0302 -0.0057 0.0141 269 VAL A CB 3994 C CG1 . VAL A 261 ? 0.2602 0.2901 0.2305 0.0252 0.0154 0.0339 269 VAL A CG1 3995 C CG2 . VAL A 261 ? 0.2029 0.1971 0.1935 0.0106 0.0067 0.0027 269 VAL A CG2 4005 N N . ILE A 262 ? 0.1307 0.1813 0.1818 0.0044 -0.0093 0.0082 270 ILE A N 4006 C CA . ILE A 262 ? 0.1359 0.1998 0.1714 -0.0154 0.0039 0.0126 270 ILE A CA 4007 C C . ILE A 262 ? 0.1186 0.1950 0.1705 0.0137 0.0047 0.0080 270 ILE A C 4008 O O . ILE A 262 ? 0.1510 0.1913 0.1612 0.0003 0.0130 -0.0004 270 ILE A O 4009 C CB . ILE A 262 ? 0.1279 0.1961 0.1676 0.0185 -0.0002 0.0261 270 ILE A CB 4010 C CG1 . ILE A 262 ? 0.1391 0.1817 0.1767 0.0029 0.0218 0.0047 270 ILE A CG1 4011 C CG2 . ILE A 262 ? 0.1627 0.1907 0.1656 0.0313 0.0091 -0.0009 270 ILE A CG2 4012 C CD1 . ILE A 262 ? 0.1838 0.2006 0.1707 0.0178 0.0076 -0.0053 270 ILE A CD1 4024 N N . ALA A 263 ? 0.1367 0.1669 0.1913 0.0165 -0.0030 -0.0151 271 ALA A N 4025 C CA . ALA A 263 ? 0.1741 0.1568 0.1954 0.0188 -0.0011 -0.0125 271 ALA A CA 4026 C C . ALA A 263 ? 0.1845 0.2119 0.1990 0.0644 0.0026 -0.0300 271 ALA A C 4027 O O . ALA A 263 ? 0.2450 0.2306 0.1959 0.0959 0.0124 -0.0213 271 ALA A O 4028 C CB . ALA A 263 ? 0.1727 0.2097 0.2095 0.0411 -0.0236 -0.0035 271 ALA A CB 4034 N N . GLY A 264 ? 0.1683 0.1901 0.1831 0.0598 -0.0107 -0.0292 272 GLY A N 4035 C CA . GLY A 264 ? 0.2202 0.2165 0.1748 0.1024 0.0105 -0.0095 272 GLY A CA 4036 C C . GLY A 264 ? 0.1519 0.1842 0.1536 0.0496 -0.0053 -0.0071 272 GLY A C 4037 O O . GLY A 264 ? 0.1391 0.1599 0.1646 0.0209 -0.0124 -0.0052 272 GLY A O 4041 N N . GLN A 265 ? 0.1406 0.1810 0.1399 0.0344 0.0086 0.0046 273 GLN A N 4042 C CA . GLN A 265 ? 0.1206 0.1671 0.1351 0.0169 -0.0051 -0.0046 273 GLN A CA 4043 C C . GLN A 265 ? 0.1115 0.1624 0.1357 -0.0005 0.0144 -0.0097 273 GLN A C 4044 O O . GLN A 265 ? 0.1132 0.1729 0.1374 0.0133 0.0147 0.0131 273 GLN A O 4045 C CB . GLN A 265 ? 0.1131 0.1670 0.1408 0.0195 0.0113 0.0095 273 GLN A CB 4046 C CG . GLN A 265 ? 0.1163 0.2041 0.1535 0.0100 0.0116 0.0183 273 GLN A CG 4047 C CD . GLN A 265 ? 0.1186 0.2248 0.1792 0.0304 -0.0193 -0.0115 273 GLN A CD 4048 O OE1 . GLN A 265 ? 0.1698 0.2696 0.2042 0.0510 -0.0222 -0.0504 273 GLN A OE1 4049 N NE2 . GLN A 265 ? 0.1300 0.2086 0.2330 -0.0002 -0.0200 -0.0206 273 GLN A NE2 4058 N N . PHE A 266 ? 0.1096 0.1546 0.1355 0.0102 0.0171 -0.0092 274 PHE A N 4059 C CA . PHE A 266 ? 0.1056 0.1647 0.1398 0.0071 -0.0060 -0.0026 274 PHE A CA 4060 C C . PHE A 266 ? 0.1002 0.1436 0.1472 0.0114 0.0084 -0.0151 274 PHE A C 4061 O O . PHE A 266 ? 0.1243 0.1744 0.1425 0.0095 0.0007 0.0020 274 PHE A O 4062 C CB . PHE A 266 ? 0.1352 0.1583 0.1494 0.0104 0.0025 -0.0074 274 PHE A CB 4063 C CG . PHE A 266 ? 0.1377 0.1589 0.1529 0.0118 0.0043 0.0003 274 PHE A CG 4064 C CD1 . PHE A 266 ? 0.1624 0.1563 0.1502 0.0182 0.0020 0.0066 274 PHE A CD1 4065 C CD2 . PHE A 266 ? 0.1535 0.1494 0.1475 0.0163 -0.0199 -0.0152 274 PHE A CD2 4066 C CE1 . PHE A 266 ? 0.1865 0.1668 0.1632 0.0436 0.0033 -0.0027 274 PHE A CE1 4067 C CE2 . PHE A 266 ? 0.1850 0.1816 0.1525 0.0333 -0.0065 -0.0315 274 PHE A CE2 4068 C CZ . PHE A 266 ? 0.1734 0.1875 0.1605 0.0296 -0.0117 -0.0075 274 PHE A CZ 4078 N N . PHE A 267 ? 0.1030 0.1477 0.1386 -0.0098 0.0030 -0.0091 275 PHE A N 4079 C CA . PHE A 267 ? 0.1188 0.1306 0.1269 0.0072 0.0020 -0.0163 275 PHE A CA 4080 C C . PHE A 267 ? 0.1073 0.1341 0.1268 -0.0038 -0.0011 -0.0096 275 PHE A C 4081 O O . PHE A 267 ? 0.1216 0.1755 0.1286 0.0001 -0.0030 -0.0039 275 PHE A O 4082 C CB . PHE A 267 ? 0.1139 0.1357 0.1378 -0.0147 -0.0097 -0.0219 275 PHE A CB 4083 C CG . PHE A 267 ? 0.1013 0.1586 0.1504 -0.0007 -0.0190 -0.0262 275 PHE A CG 4084 C CD1 . PHE A 267 ? 0.1110 0.1913 0.1582 -0.0105 -0.0256 -0.0253 275 PHE A CD1 4085 C CD2 . PHE A 267 ? 0.1392 0.1806 0.1431 -0.0012 -0.0293 -0.0416 275 PHE A CD2 4086 C CE1 . PHE A 267 ? 0.1330 0.2227 0.1398 0.0073 -0.0232 -0.0324 275 PHE A CE1 4087 C CE2 . PHE A 267 ? 0.1465 0.2069 0.1432 0.0104 -0.0154 -0.0248 275 PHE A CE2 4088 C CZ . PHE A 267 ? 0.1368 0.2133 0.1451 0.0026 -0.0246 -0.0364 275 PHE A CZ 4098 N N . GLY A 268 ? 0.1091 0.1619 0.1413 0.0002 0.0040 -0.0215 276 GLY A N 4099 C CA . GLY A 268 ? 0.1067 0.1738 0.1575 0.0076 -0.0136 0.0045 276 GLY A CA 4100 C C . GLY A 268 ? 0.1084 0.1794 0.1254 -0.0134 -0.0214 0.0071 276 GLY A C 4101 O O . GLY A 268 ? 0.1018 0.1649 0.1524 0.0011 0.0087 -0.0087 276 GLY A O 4105 N N . HIS A 269 ? 0.1020 0.1602 0.1293 -0.0061 0.0000 0.0027 277 HIS A N 4106 C CA . HIS A 269 ? 0.1061 0.1257 0.1281 0.0054 -0.0048 -0.0040 277 HIS A CA 4107 C C . HIS A 269 ? 0.1211 0.1598 0.1278 0.0189 0.0071 -0.0072 277 HIS A C 4108 O O . HIS A 269 ? 0.1297 0.1775 0.1406 0.0158 0.0088 0.0087 277 HIS A O 4109 C CB . HIS A 269 ? 0.1103 0.1457 0.1438 -0.0007 0.0031 -0.0170 277 HIS A CB 4110 C CG . HIS A 269 ? 0.0881 0.1700 0.1439 0.0016 0.0046 -0.0036 277 HIS A CG 4111 N ND1 . HIS A 269 ? 0.1190 0.1642 0.1446 0.0183 -0.0128 -0.0227 277 HIS A ND1 4112 C CD2 . HIS A 269 ? 0.1079 0.2034 0.1383 -0.0183 0.0037 -0.0107 277 HIS A CD2 4113 C CE1 . HIS A 269 ? 0.1292 0.1526 0.1689 0.0112 0.0085 -0.0222 277 HIS A CE1 4114 N NE2 . HIS A 269 ? 0.1248 0.1713 0.1642 -0.0005 0.0023 -0.0309 277 HIS A NE2 4122 N N . HIS A 270 ? 0.1038 0.1428 0.1446 -0.0072 0.0120 -0.0057 278 HIS A N 4123 C CA . HIS A 270 ? 0.0842 0.1658 0.1485 -0.0139 0.0191 -0.0102 278 HIS A CA 4124 C C . HIS A 270 ? 0.1064 0.1559 0.1485 0.0024 0.0141 0.0018 278 HIS A C 4125 O O . HIS A 270 ? 0.1446 0.1728 0.1648 0.0095 -0.0199 -0.0003 278 HIS A O 4126 C CB . HIS A 270 ? 0.0997 0.1729 0.1456 -0.0253 0.0045 0.0182 278 HIS A CB 4127 C CG . HIS A 270 ? 0.1213 0.1630 0.1467 -0.0087 0.0030 0.0164 278 HIS A CG 4128 N ND1 . HIS A 270 ? 0.1136 0.1684 0.1566 -0.0092 0.0125 -0.0034 278 HIS A ND1 4129 C CD2 . HIS A 270 ? 0.1292 0.1969 0.1523 -0.0117 0.0124 -0.0045 278 HIS A CD2 4130 C CE1 . HIS A 270 ? 0.1000 0.1797 0.1654 -0.0111 0.0192 -0.0155 278 HIS A CE1 4131 N NE2 . HIS A 270 ? 0.1166 0.1884 0.1713 -0.0193 -0.0024 -0.0005 278 HIS A NE2 4139 N N . HIS A 271 ? 0.0902 0.1701 0.1300 -0.0108 0.0057 0.0034 279 HIS A N 4140 C CA . HIS A 271 ? 0.0800 0.1881 0.1398 0.0077 0.0233 -0.0036 279 HIS A CA 4141 C C . HIS A 271 ? 0.1012 0.1675 0.1484 -0.0204 0.0136 0.0058 279 HIS A C 4142 O O . HIS A 271 ? 0.1335 0.2201 0.1499 -0.0276 0.0101 -0.0101 279 HIS A O 4143 C CB . HIS A 271 ? 0.0949 0.1748 0.1444 0.0026 -0.0069 -0.0128 279 HIS A CB 4144 C CG . HIS A 271 ? 0.0956 0.1754 0.1371 0.0017 0.0236 0.0007 279 HIS A CG 4145 N ND1 . HIS A 271 ? 0.1026 0.1764 0.1487 0.0199 0.0077 0.0080 279 HIS A ND1 4146 C CD2 . HIS A 271 ? 0.0978 0.1656 0.1441 0.0020 0.0212 0.0020 279 HIS A CD2 4147 C CE1 . HIS A 271 ? 0.1325 0.1685 0.1402 0.0143 0.0077 0.0023 279 HIS A CE1 4148 N NE2 . HIS A 271 ? 0.1161 0.1655 0.1500 -0.0221 0.0149 0.0013 279 HIS A NE2 4156 N N . THR A 272 ? 0.1077 0.1909 0.1529 -0.0235 0.0184 -0.0140 280 THR A N 4157 C CA . THR A 272 ? 0.1039 0.1981 0.1498 -0.0226 0.0349 0.0029 280 THR A CA 4158 C C . THR A 272 ? 0.1155 0.2076 0.1401 0.0004 0.0141 -0.0084 280 THR A C 4159 O O . THR A 272 ? 0.1671 0.2148 0.1423 0.0099 0.0193 -0.0018 280 THR A O 4160 C CB . THR A 272 ? 0.1511 0.2109 0.1604 -0.0066 0.0116 -0.0047 280 THR A CB 4161 O OG1 . THR A 272 ? 0.1623 0.2305 0.1746 -0.0379 0.0135 -0.0114 280 THR A OG1 4162 C CG2 . THR A 272 ? 0.1930 0.2394 0.1912 0.0176 -0.0043 -0.0188 280 THR A CG2 4170 N N . ASP A 273 ? 0.1023 0.1665 0.1344 -0.0040 0.0094 0.0013 281 ASP A N 4171 C CA . ASP A 273 ? 0.1079 0.1647 0.1423 -0.0003 0.0237 0.0077 281 ASP A CA 4172 C C . ASP A 273 ? 0.0876 0.1680 0.1280 -0.0087 0.0270 -0.0083 281 ASP A C 4173 O O . ASP A 273 ? 0.1058 0.1804 0.1330 -0.0166 0.0063 0.0088 281 ASP A O 4174 C CB . ASP A 273 ? 0.1355 0.1734 0.1327 -0.0050 -0.0007 -0.0122 281 ASP A CB 4175 C CG . ASP A 273 ? 0.1372 0.1678 0.1429 -0.0134 0.0122 -0.0037 281 ASP A CG 4176 O OD1 . ASP A 273 ? 0.1192 0.1820 0.1583 0.0053 -0.0075 0.0011 281 ASP A OD1 4177 O OD2 . ASP A 273 ? 0.1374 0.1717 0.1429 0.0149 -0.0037 -0.0109 281 ASP A OD2 4182 N N . SER A 274 ? 0.0971 0.1751 0.1270 0.0089 0.0041 0.0069 282 SER A N 4183 C CA . SER A 274 ? 0.0981 0.1578 0.1394 0.0125 0.0095 0.0064 282 SER A CA 4184 C C . SER A 274 ? 0.0992 0.1878 0.1255 -0.0162 0.0212 -0.0132 282 SER A C 4185 O O . SER A 274 ? 0.0953 0.1749 0.1441 -0.0032 0.0111 0.0076 282 SER A O 4186 C CB . SER A 274 ? 0.0992 0.1671 0.1538 -0.0159 0.0082 0.0166 282 SER A CB 4187 O OG . SER A 274 ? 0.1295 0.1682 0.1432 -0.0063 0.0054 0.0044 282 SER A OG 4193 N N . PHE A 275 ? 0.0967 0.1793 0.1311 0.0055 -0.0015 0.0058 283 PHE A N 4194 C CA . PHE A 275 ? 0.1152 0.1707 0.1308 -0.0145 -0.0077 0.0012 283 PHE A CA 4195 C C . PHE A 275 ? 0.0977 0.1627 0.1339 0.0094 0.0060 0.0186 283 PHE A C 4196 O O . PHE A 275 ? 0.1167 0.1557 0.1462 -0.0008 0.0016 0.0151 283 PHE A O 4197 C CB . PHE A 275 ? 0.1243 0.1630 0.1449 -0.0176 0.0017 -0.0109 283 PHE A CB 4198 C CG . PHE A 275 ? 0.1169 0.1691 0.1478 0.0090 0.0043 -0.0209 283 PHE A CG 4199 C CD1 . PHE A 275 ? 0.0876 0.1978 0.1668 0.0145 0.0224 -0.0132 283 PHE A CD1 4200 C CD2 . PHE A 275 ? 0.1062 0.1688 0.1578 -0.0029 0.0133 -0.0066 283 PHE A CD2 4201 C CE1 . PHE A 275 ? 0.0879 0.2478 0.1645 0.0043 0.0157 0.0022 283 PHE A CE1 4202 C CE2 . PHE A 275 ? 0.1164 0.1948 0.1589 -0.0141 0.0079 -0.0114 283 PHE A CE2 4203 C CZ . PHE A 275 ? 0.1430 0.2027 0.1556 -0.0048 0.0234 -0.0144 283 PHE A CZ 4213 N N . ARG A 276 ? 0.1036 0.1376 0.1524 -0.0065 -0.0103 -0.0048 284 ARG A N 4214 C CA . ARG A 276 ? 0.1139 0.1640 0.1602 -0.0019 -0.0087 0.0053 284 ARG A CA 4215 C C . ARG A 276 ? 0.1035 0.1652 0.1642 -0.0081 -0.0165 0.0063 284 ARG A C 4216 O O . ARG A 276 ? 0.1212 0.1747 0.1823 -0.0035 -0.0141 0.0184 284 ARG A O 4217 C CB . ARG A 276 ? 0.1157 0.1743 0.1703 -0.0156 -0.0032 0.0040 284 ARG A CB 4218 C CG . ARG A 276 ? 0.1034 0.1649 0.1734 -0.0027 -0.0040 0.0045 284 ARG A CG 4219 C CD . ARG A 276 ? 0.1358 0.1453 0.1716 -0.0359 0.0041 -0.0004 284 ARG A CD 4220 N NE . ARG A 276 ? 0.1171 0.1552 0.1614 0.0108 -0.0161 -0.0040 284 ARG A NE 4221 C CZ . ARG A 276 ? 0.1362 0.1503 0.1654 -0.0175 -0.0079 -0.0057 284 ARG A CZ 4222 N NH1 . ARG A 276 ? 0.1241 0.1530 0.1745 -0.0069 -0.0072 -0.0056 284 ARG A NH1 4223 N NH2 . ARG A 276 ? 0.1353 0.1726 0.1622 0.0109 -0.0082 -0.0050 284 ARG A NH2 4237 N N . MET A 277 ? 0.0922 0.1690 0.1780 -0.0099 -0.0034 0.0201 285 MET A N 4238 C CA . MET A 277 ? 0.1002 0.1767 0.1760 -0.0121 -0.0031 -0.0028 285 MET A CA 4239 C C . MET A 277 ? 0.1064 0.1824 0.1722 -0.0036 0.0080 0.0062 285 MET A C 4240 O O . MET A 277 ? 0.1493 0.1911 0.1987 0.0062 -0.0364 -0.0077 285 MET A O 4241 C CB . MET A 277 ? 0.1047 0.1884 0.1918 0.0060 -0.0114 -0.0029 285 MET A CB 4242 C CG . MET A 277 ? 0.1433 0.2099 0.1640 0.0308 -0.0097 0.0167 285 MET A CG 4243 S SD . MET A 277 ? 0.1541 0.2487 0.1806 0.0117 -0.0137 -0.0127 285 MET A SD 4244 C CE . MET A 277 ? 0.1775 0.2545 0.2131 0.0335 0.0050 -0.0262 285 MET A CE 4254 N N . PHE A 278 ? 0.1035 0.1837 0.1700 0.0044 -0.0060 0.0143 286 PHE A N 4255 C CA . PHE A 278 ? 0.0772 0.1922 0.1658 0.0033 0.0056 0.0097 286 PHE A CA 4256 C C . PHE A 278 ? 0.1033 0.2034 0.1532 -0.0070 0.0090 0.0166 286 PHE A C 4257 O O . PHE A 278 ? 0.0990 0.2153 0.1671 0.0175 0.0010 -0.0026 286 PHE A O 4258 C CB . PHE A 278 ? 0.0964 0.2129 0.1639 -0.0001 0.0156 0.0027 286 PHE A CB 4259 C CG . PHE A 278 ? 0.0871 0.2016 0.1747 0.0070 0.0059 0.0025 286 PHE A CG 4260 C CD1 . PHE A 278 ? 0.0989 0.1992 0.1800 -0.0230 0.0036 0.0171 286 PHE A CD1 4261 C CD2 . PHE A 278 ? 0.1106 0.1996 0.1846 0.0004 0.0250 -0.0082 286 PHE A CD2 4262 C CE1 . PHE A 278 ? 0.1087 0.2190 0.1919 -0.0370 0.0077 0.0201 286 PHE A CE1 4263 C CE2 . PHE A 278 ? 0.1283 0.2138 0.1946 -0.0140 0.0406 -0.0303 286 PHE A CE2 4264 C CZ . PHE A 278 ? 0.1120 0.2068 0.2216 0.0042 0.0263 0.0150 286 PHE A CZ 4274 N N . TYR A 279 ? 0.1095 0.2143 0.1698 -0.0184 0.0016 0.0128 287 TYR A N 4275 C CA . TYR A 279 ? 0.0898 0.2406 0.1699 0.0103 0.0018 0.0145 287 TYR A CA 4276 C C . TYR A 279 ? 0.1022 0.2600 0.1717 0.0323 0.0089 -0.0022 287 TYR A C 4277 O O . TYR A 279 ? 0.1223 0.2626 0.1794 0.0232 -0.0123 -0.0279 287 TYR A O 4278 C CB . TYR A 279 ? 0.1143 0.2785 0.1965 -0.0280 0.0000 0.0287 287 TYR A CB 4279 C CG . TYR A 279 ? 0.1132 0.2641 0.1994 -0.0228 -0.0063 0.0408 287 TYR A CG 4280 C CD1 . TYR A 279 ? 0.1155 0.3022 0.2078 0.0144 0.0078 0.0486 287 TYR A CD1 4281 C CD2 . TYR A 279 ? 0.1080 0.2267 0.2011 0.0044 0.0006 0.0307 287 TYR A CD2 4282 C CE1 . TYR A 279 ? 0.1388 0.2730 0.2085 0.0215 0.0159 0.0322 287 TYR A CE1 4283 C CE2 . TYR A 279 ? 0.1347 0.2355 0.2110 -0.0101 -0.0058 0.0362 287 TYR A CE2 4284 C CZ . TYR A 279 ? 0.1593 0.2679 0.2087 0.0146 0.0185 0.0630 287 TYR A CZ 4285 O OH . TYR A 279 ? 0.1882 0.3166 0.2085 0.0199 0.0016 0.0541 287 TYR A OH 4295 N N . ASP A 280 ? 0.1038 0.2462 0.1786 -0.0028 -0.0058 0.0000 288 ASP A N 4296 C CA . ASP A 280 ? 0.1127 0.2600 0.1855 0.0089 -0.0213 0.0197 288 ASP A CA 4297 C C . ASP A 280 ? 0.1271 0.2597 0.1731 0.0069 0.0037 -0.0003 288 ASP A C 4298 O O . ASP A 280 ? 0.1188 0.2717 0.1907 -0.0001 -0.0189 0.0089 288 ASP A O 4299 C CB . ASP A 280 ? 0.1283 0.2666 0.2116 -0.0143 -0.0137 0.0255 288 ASP A CB 4300 C CG . ASP A 280 ? 0.1326 0.2552 0.2520 -0.0096 -0.0159 0.0521 288 ASP A CG 4301 O OD1 . ASP A 280 ? 0.1145 0.2647 0.2301 -0.0091 -0.0129 0.0345 288 ASP A OD1 4302 O OD2 . ASP A 280 ? 0.1541 0.2770 0.3004 -0.0044 -0.0095 0.0551 288 ASP A OD2 4307 N N . ASN A 281 ? 0.1172 0.2764 0.1826 -0.0116 -0.0187 -0.0028 289 ASN A N 4308 C CA . ASN A 281 ? 0.1468 0.2621 0.1941 0.0002 -0.0130 -0.0062 289 ASN A CA 4309 C C . ASN A 281 ? 0.1243 0.2497 0.2068 -0.0142 -0.0053 -0.0198 289 ASN A C 4310 O O . ASN A 281 ? 0.1600 0.3228 0.2536 -0.0396 0.0018 -0.0391 289 ASN A O 4311 C CB . ASN A 281 ? 0.1469 0.3031 0.1945 0.0092 -0.0152 -0.0313 289 ASN A CB 4312 C CG . ASN A 281 ? 0.1271 0.2981 0.1958 0.0098 -0.0246 -0.0287 289 ASN A CG 4313 O OD1 . ASN A 281 ? 0.1453 0.3352 0.2085 0.0408 -0.0258 -0.0142 289 ASN A OD1 4314 N ND2 . ASN A 281 ? 0.1652 0.3193 0.2051 -0.0084 -0.0175 -0.0232 289 ASN A ND2 4321 N N . THR A 282 ? 0.1176 0.2432 0.1914 -0.0100 0.0011 0.0012 290 THR A N 4322 C CA . THR A 282 ? 0.1104 0.2607 0.2032 -0.0208 0.0190 -0.0023 290 THR A CA 4323 C C . THR A 282 ? 0.0990 0.2635 0.2052 -0.0221 0.0255 0.0042 290 THR A C 4324 O O . THR A 282 ? 0.1127 0.3225 0.2066 -0.0215 0.0214 -0.0027 290 THR A O 4325 C CB . THR A 282 ? 0.1160 0.3051 0.1980 0.0025 -0.0182 -0.0084 290 THR A CB 4326 O OG1 . THR A 282 ? 0.1359 0.2833 0.2122 0.0004 -0.0137 -0.0064 290 THR A OG1 4327 C CG2 . THR A 282 ? 0.1252 0.3123 0.2047 0.0253 -0.0120 -0.0236 290 THR A CG2 4335 N N . GLY A 283 ? 0.1219 0.2630 0.1963 -0.0238 0.0162 0.0151 291 GLY A N 4336 C CA . GLY A 283 ? 0.1299 0.2538 0.1873 -0.0186 0.0082 0.0300 291 GLY A CA 4337 C C . GLY A 283 ? 0.1034 0.2532 0.1784 0.0033 0.0315 0.0225 291 GLY A C 4338 O O . GLY A 283 ? 0.1294 0.3171 0.1823 0.0007 -0.0027 0.0253 291 GLY A O 4342 N N . ALA A 284 ? 0.1136 0.2739 0.1776 -0.0167 -0.0041 0.0168 292 ALA A N 4343 C CA . ALA A 284 ? 0.1141 0.2864 0.1870 -0.0134 0.0156 -0.0027 292 ALA A CA 4344 C C . ALA A 284 ? 0.1268 0.2429 0.1609 -0.0107 0.0099 0.0077 292 ALA A C 4345 O O . ALA A 284 ? 0.1007 0.2595 0.1563 -0.0064 0.0185 0.0029 292 ALA A O 4346 C CB . ALA A 284 ? 0.1101 0.2876 0.2032 0.0171 0.0207 -0.0014 292 ALA A CB 4352 N N . PRO A 285 ? 0.1314 0.2685 0.1659 -0.0150 0.0193 -0.0118 293 PRO A N 4353 C CA . PRO A 285 ? 0.1149 0.2453 0.1604 -0.0146 -0.0061 0.0069 293 PRO A CA 4354 C C . PRO A 285 ? 0.1175 0.2108 0.1866 -0.0094 0.0086 -0.0208 293 PRO A C 4355 O O . PRO A 285 ? 0.1757 0.2551 0.2236 0.0089 0.0410 -0.0222 293 PRO A O 4356 C CB . PRO A 285 ? 0.1662 0.3027 0.1779 -0.0205 0.0057 0.0163 293 PRO A CB 4357 C CG . PRO A 285 ? 0.1932 0.3549 0.1978 0.0152 0.0129 -0.0187 293 PRO A CG 4358 C CD . PRO A 285 ? 0.1533 0.2927 0.1789 -0.0139 0.0173 -0.0052 293 PRO A CD 4366 N N . ILE A 286 ? 0.0856 0.2387 0.1829 -0.0013 -0.0015 -0.0079 294 ILE A N 4367 C CA . ILE A 286 ? 0.1128 0.2307 0.1786 0.0006 0.0111 0.0202 294 ILE A CA 4368 C C . ILE A 286 ? 0.1149 0.2111 0.1786 -0.0010 0.0007 0.0172 294 ILE A C 4369 O O . ILE A 286 ? 0.1106 0.2138 0.2072 0.0083 0.0091 0.0153 294 ILE A O 4370 C CB . ILE A 286 ? 0.1298 0.2405 0.1962 0.0023 0.0026 0.0266 294 ILE A CB 4371 C CG1 . ILE A 286 ? 0.1443 0.2162 0.1763 -0.0060 -0.0233 0.0195 294 ILE A CG1 4372 C CG2 . ILE A 286 ? 0.1041 0.2897 0.2069 0.0090 0.0066 0.0347 294 ILE A CG2 4373 C CD1 . ILE A 286 ? 0.1705 0.2192 0.1954 0.0136 -0.0025 0.0141 294 ILE A CD1 4385 N N . ASN A 287 ? 0.1154 0.1861 0.1623 0.0057 0.0065 0.0178 295 ASN A N 4386 C CA . ASN A 287 ? 0.0936 0.2016 0.1600 0.0068 0.0030 0.0059 295 ASN A CA 4387 C C . ASN A 287 ? 0.0876 0.1763 0.1686 0.0112 0.0231 0.0100 295 ASN A C 4388 O O . ASN A 287 ? 0.1188 0.1941 0.1719 -0.0050 -0.0080 -0.0076 295 ASN A O 4389 C CB . ASN A 287 ? 0.1365 0.1831 0.1781 0.0024 0.0026 0.0124 295 ASN A CB 4390 C CG . ASN A 287 ? 0.1235 0.1828 0.2088 0.0000 -0.0036 0.0255 295 ASN A CG 4391 O OD1 . ASN A 287 ? 0.1345 0.2004 0.2719 0.0035 0.0264 0.0206 295 ASN A OD1 4392 N ND2 . ASN A 287 ? 0.1479 0.1979 0.2154 -0.0073 0.0075 0.0263 295 ASN A ND2 4399 N N . VAL A 288 ? 0.0883 0.1715 0.1780 0.0023 -0.0012 0.0170 296 VAL A N 4400 C CA . VAL A 288 ? 0.1303 0.1568 0.1744 0.0105 -0.0024 -0.0089 296 VAL A CA 4401 C C . VAL A 288 ? 0.1193 0.1476 0.1593 -0.0105 -0.0077 -0.0004 296 VAL A C 4402 O O . VAL A 288 ? 0.1314 0.1573 0.2121 -0.0030 -0.0165 0.0171 296 VAL A O 4403 C CB . VAL A 288 ? 0.2103 0.2260 0.1865 0.0660 -0.0212 -0.0183 296 VAL A CB 4404 C CG1 . VAL A 288 ? 0.2449 0.2704 0.2248 0.0651 -0.0468 -0.0047 296 VAL A CG1 4405 C CG2 . VAL A 288 ? 0.2099 0.2526 0.1633 0.0677 -0.0169 -0.0099 296 VAL A CG2 4415 N N . MET A 289 ? 0.1013 0.1608 0.1699 0.0043 0.0057 -0.0081 297 MET A N 4416 C CA . MET A 289 ? 0.0898 0.1717 0.1576 0.0007 0.0157 0.0013 297 MET A CA 4417 C C . MET A 289 ? 0.0707 0.1697 0.1494 -0.0018 -0.0029 0.0193 297 MET A C 4418 O O . MET A 289 ? 0.1172 0.1656 0.1551 -0.0273 -0.0089 0.0152 297 MET A O 4419 C CB . MET A 289 ? 0.1089 0.1513 0.1445 0.0012 0.0178 -0.0027 297 MET A CB 4420 C CG . MET A 289 ? 0.1153 0.1749 0.1646 0.0116 0.0088 -0.0191 297 MET A CG 4421 S SD . MET A 289 ? 0.1460 0.1942 0.1915 0.0041 0.0085 -0.0246 297 MET A SD 4422 C CE . MET A 289 ? 0.1685 0.2134 0.1675 0.0096 -0.0172 -0.0043 297 MET A CE 4432 N N . PHE A 290 ? 0.1099 0.1552 0.1371 -0.0055 0.0025 0.0042 298 PHE A N 4433 C CA . PHE A 290 ? 0.0914 0.1507 0.1358 0.0014 0.0035 -0.0083 298 PHE A CA 4434 C C . PHE A 290 ? 0.1075 0.1956 0.1337 -0.0024 0.0187 0.0096 298 PHE A C 4435 O O . PHE A 290 ? 0.1125 0.1798 0.1539 0.0114 0.0149 0.0245 298 PHE A O 4436 C CB . PHE A 290 ? 0.1078 0.1856 0.1514 0.0057 0.0069 -0.0202 298 PHE A CB 4437 C CG . PHE A 290 ? 0.1276 0.1815 0.1600 -0.0017 -0.0050 -0.0055 298 PHE A CG 4438 C CD1 . PHE A 290 ? 0.1322 0.1963 0.1794 -0.0137 0.0104 -0.0312 298 PHE A CD1 4439 C CD2 . PHE A 290 ? 0.1445 0.1926 0.1813 0.0092 0.0086 -0.0143 298 PHE A CD2 4440 C CE1 . PHE A 290 ? 0.1387 0.2361 0.1985 -0.0058 0.0139 -0.0295 298 PHE A CE1 4441 C CE2 . PHE A 290 ? 0.1678 0.1966 0.2127 0.0105 0.0068 0.0039 298 PHE A CE2 4442 C CZ . PHE A 290 ? 0.1483 0.1975 0.2169 0.0021 0.0160 -0.0309 298 PHE A CZ 4452 N N . LEU A 291 ? 0.0985 0.1549 0.1302 -0.0020 0.0125 0.0021 299 LEU A N 4453 C CA . LEU A 291 ? 0.0938 0.1507 0.1308 0.0060 0.0057 0.0042 299 LEU A CA 4454 C C . LEU A 291 ? 0.1143 0.1707 0.1359 -0.0011 0.0095 0.0086 299 LEU A C 4455 O O . LEU A 291 ? 0.1125 0.1745 0.1542 -0.0162 0.0030 0.0102 299 LEU A O 4456 C CB . LEU A 291 ? 0.1112 0.1596 0.1385 0.0147 -0.0095 0.0032 299 LEU A CB 4457 C CG . LEU A 291 ? 0.1271 0.1498 0.1626 0.0018 0.0274 0.0108 299 LEU A CG 4458 C CD1 . LEU A 291 ? 0.1604 0.2093 0.1712 -0.0129 -0.0218 -0.0084 299 LEU A CD1 4459 C CD2 . LEU A 291 ? 0.2278 0.2475 0.1763 -0.1105 0.0206 -0.0052 299 LEU A CD2 4471 N N . THR A 292 ? 0.1049 0.1641 0.1265 -0.0155 0.0074 0.0071 300 THR A N 4472 C CA . THR A 292 ? 0.1135 0.1603 0.1438 -0.0138 0.0023 0.0047 300 THR A CA 4473 C C . THR A 292 ? 0.0986 0.1838 0.1453 -0.0006 0.0096 -0.0095 300 THR A C 4474 O O . THR A 292 ? 0.1009 0.2005 0.1541 0.0174 0.0063 -0.0194 300 THR A O 4475 C CB . THR A 292 ? 0.1257 0.1807 0.1610 -0.0103 0.0009 -0.0055 300 THR A CB 4476 O OG1 . THR A 292 ? 0.1933 0.2002 0.2029 -0.0109 -0.0206 -0.0330 300 THR A OG1 4477 C CG2 . THR A 292 ? 0.1633 0.1774 0.1589 -0.0278 -0.0046 0.0066 300 THR A CG2 4485 N N . PRO A 293 ? 0.1141 0.1978 0.1327 0.0065 0.0024 0.0024 301 PRO A N 4486 C CA . PRO A 293 ? 0.1197 0.1693 0.1556 -0.0119 0.0059 0.0165 301 PRO A CA 4487 C C . PRO A 293 ? 0.1177 0.1746 0.1570 -0.0138 -0.0016 -0.0088 301 PRO A C 4488 O O . PRO A 293 ? 0.1161 0.2048 0.1863 -0.0217 0.0091 0.0114 301 PRO A O 4489 C CB . PRO A 293 ? 0.1831 0.2153 0.1454 0.0197 -0.0038 0.0185 301 PRO A CB 4490 C CG . PRO A 293 ? 0.1823 0.2221 0.1251 -0.0075 -0.0125 -0.0062 301 PRO A CG 4491 C CD . PRO A 293 ? 0.1450 0.2053 0.1276 -0.0114 0.0176 -0.0059 301 PRO A CD 4499 N N . GLY A 294 ? 0.1294 0.1771 0.1389 -0.0168 0.0078 -0.0131 302 GLY A N 4500 C CA . GLY A 294 ? 0.1201 0.2005 0.1527 -0.0091 0.0198 -0.0008 302 GLY A CA 4501 C C . GLY A 294 ? 0.1128 0.1696 0.1317 -0.0063 0.0139 -0.0253 302 GLY A C 4502 O O . GLY A 294 ? 0.1022 0.1984 0.1396 -0.0091 0.0102 -0.0154 302 GLY A O 4506 N N . VAL A 295 ? 0.1145 0.1741 0.1235 -0.0061 0.0076 -0.0021 303 VAL A N 4507 C CA . VAL A 295 ? 0.1023 0.1579 0.1392 0.0000 0.0079 -0.0191 303 VAL A CA 4508 C C . VAL A 295 ? 0.0905 0.1432 0.1575 -0.0119 0.0184 -0.0108 303 VAL A C 4509 O O . VAL A 295 ? 0.1113 0.1842 0.1533 -0.0018 -0.0024 -0.0009 303 VAL A O 4510 C CB . VAL A 295 ? 0.1174 0.1603 0.1527 -0.0157 0.0181 -0.0052 303 VAL A CB 4511 C CG1 . VAL A 295 ? 0.1207 0.1912 0.1636 -0.0371 0.0261 -0.0126 303 VAL A CG1 4512 C CG2 . VAL A 295 ? 0.1401 0.1688 0.1872 -0.0027 0.0412 -0.0033 303 VAL A CG2 4522 N N . THR A 296 ? 0.1067 0.1344 0.1513 0.0115 0.0133 -0.0246 304 THR A N 4523 C CA . THR A 296 ? 0.0943 0.1689 0.1547 -0.0015 0.0228 -0.0195 304 THR A CA 4524 C C . THR A 296 ? 0.0972 0.1462 0.1492 -0.0116 0.0063 -0.0135 304 THR A C 4525 O O . THR A 296 ? 0.1073 0.1785 0.1443 -0.0093 0.0002 -0.0009 304 THR A O 4526 C CB . THR A 296 ? 0.1177 0.1610 0.1491 0.0100 0.0219 -0.0286 304 THR A CB 4527 O OG1 . THR A 296 ? 0.1271 0.2015 0.1660 0.0376 -0.0037 -0.0335 304 THR A OG1 4528 C CG2 . THR A 296 ? 0.1307 0.1559 0.1558 0.0063 0.0053 -0.0050 304 THR A CG2 4536 N N . PRO A 297 ? 0.1000 0.1620 0.1445 0.0064 0.0047 -0.0018 305 PRO A N 4537 C CA . PRO A 297 ? 0.0983 0.1576 0.1505 -0.0022 0.0088 0.0029 305 PRO A CA 4538 C C . PRO A 297 ? 0.1107 0.1610 0.1617 -0.0056 0.0031 0.0029 305 PRO A C 4539 O O . PRO A 297 ? 0.1356 0.1723 0.1752 -0.0140 0.0298 0.0012 305 PRO A O 4540 C CB . PRO A 297 ? 0.1207 0.1666 0.1477 0.0137 0.0055 0.0061 305 PRO A CB 4541 C CG . PRO A 297 ? 0.1222 0.1678 0.1499 -0.0041 0.0159 0.0056 305 PRO A CG 4542 C CD . PRO A 297 ? 0.1045 0.1650 0.1504 -0.0166 -0.0015 -0.0069 305 PRO A CD 4550 N N . TRP A 298 ? 0.1131 0.1616 0.1427 0.0043 0.0095 -0.0081 306 TRP A N 4551 C CA . TRP A 298 ? 0.1357 0.1537 0.1700 0.0037 0.0163 -0.0115 306 TRP A CA 4552 C C . TRP A 298 ? 0.1138 0.1461 0.1613 -0.0064 -0.0108 0.0107 306 TRP A C 4553 O O . TRP A 298 ? 0.1237 0.1623 0.1856 -0.0089 -0.0035 -0.0066 306 TRP A O 4554 C CB . TRP A 298 ? 0.1161 0.1570 0.1860 0.0009 0.0223 -0.0175 306 TRP A CB 4555 C CG . TRP A 298 ? 0.1267 0.1640 0.1899 0.0071 0.0127 -0.0048 306 TRP A CG 4556 C CD1 . TRP A 298 ? 0.1412 0.1679 0.2013 0.0068 0.0019 -0.0132 306 TRP A CD1 4557 C CD2 . TRP A 298 ? 0.1325 0.1708 0.1928 0.0039 0.0081 -0.0248 306 TRP A CD2 4558 N NE1 . TRP A 298 ? 0.1667 0.1676 0.2247 0.0169 0.0285 -0.0392 306 TRP A NE1 4559 C CE2 . TRP A 298 ? 0.1637 0.1731 0.1989 -0.0066 0.0042 -0.0190 306 TRP A CE2 4560 C CE3 . TRP A 298 ? 0.1775 0.1695 0.1943 -0.0143 0.0113 -0.0119 306 TRP A CE3 4561 C CZ2 . TRP A 298 ? 0.2015 0.1810 0.2056 -0.0379 0.0247 -0.0324 306 TRP A CZ2 4562 C CZ3 . TRP A 298 ? 0.2085 0.1777 0.1919 -0.0342 -0.0045 0.0109 306 TRP A CZ3 4563 C CH2 . TRP A 298 ? 0.2091 0.1790 0.1886 -0.0379 -0.0061 -0.0156 306 TRP A CH2 4574 N N . LYS A 299 ? 0.1167 0.1578 0.1751 -0.0110 -0.0012 0.0097 307 LYS A N 4575 C CA . LYS A 299 ? 0.1400 0.1481 0.2030 -0.0018 0.0008 -0.0017 307 LYS A CA 4576 C C . LYS A 299 ? 0.1399 0.1523 0.2075 -0.0063 0.0008 0.0040 307 LYS A C 4577 O O . LYS A 299 ? 0.1417 0.1795 0.2316 -0.0079 -0.0056 -0.0351 307 LYS A O 4578 C CB . LYS A 299 ? 0.1603 0.1649 0.2085 -0.0043 0.0255 0.0113 307 LYS A CB 4579 C CG . LYS A 299 ? 0.1803 0.2204 0.2299 -0.0064 0.0048 0.0507 307 LYS A CG 4580 C CD . LYS A 299 ? 0.2623 0.2541 0.2793 -0.0265 0.0154 0.0769 307 LYS A CD 4581 C CE . LYS A 299 ? 0.3706 0.3572 0.3176 0.0517 0.0353 0.0922 307 LYS A CE 4582 N NZ . LYS A 299 ? 0.4596 0.4436 0.3436 0.0865 0.0625 0.0778 307 LYS A NZ 4596 N N . THR A 300 ? 0.1358 0.1527 0.1958 -0.0107 -0.0029 -0.0169 308 THR A N 4597 C CA . THR A 300 ? 0.1446 0.1549 0.1985 -0.0249 0.0049 -0.0036 308 THR A CA 4598 C C . THR A 300 ? 0.1364 0.1636 0.2047 -0.0200 -0.0108 0.0010 308 THR A C 4599 O O . THR A 300 ? 0.1750 0.1450 0.2223 -0.0259 -0.0043 0.0017 308 THR A O 4600 C CB . THR A 300 ? 0.1417 0.1790 0.2051 -0.0184 -0.0167 -0.0040 308 THR A CB 4601 O OG1 . THR A 300 ? 0.1740 0.2116 0.2067 -0.0213 -0.0274 -0.0020 308 THR A OG1 4602 C CG2 . THR A 300 ? 0.1438 0.2334 0.2165 -0.0047 -0.0029 -0.0043 308 THR A CG2 4610 N N . THR A 301 ? 0.1468 0.1714 0.2018 0.0036 0.0070 -0.0288 309 THR A N 4611 C CA . THR A 301 ? 0.1812 0.1645 0.2332 0.0076 0.0192 -0.0464 309 THR A CA 4612 C C . THR A 301 ? 0.2056 0.1811 0.2400 0.0060 0.0084 -0.0310 309 THR A C 4613 O O . THR A 301 ? 0.2188 0.1835 0.2906 0.0042 0.0068 -0.0697 309 THR A O 4614 C CB . THR A 301 ? 0.2160 0.2045 0.2620 -0.0111 0.0221 -0.0457 309 THR A CB 4615 O OG1 . THR A 301 ? 0.2582 0.2516 0.2496 -0.0341 0.0582 -0.0140 309 THR A OG1 4616 C CG2 . THR A 301 ? 0.2138 0.2241 0.3049 0.0075 0.0198 -0.0363 309 THR A CG2 4624 N N . LEU A 302 ? 0.1743 0.1951 0.2225 -0.0343 -0.0052 -0.0201 310 LEU A N 4625 C CA . LEU A 302 ? 0.1564 0.1994 0.2448 -0.0266 -0.0101 -0.0257 310 LEU A CA 4626 C C . LEU A 302 ? 0.1769 0.1913 0.2841 -0.0427 0.0185 -0.0387 310 LEU A C 4627 O O . LEU A 302 ? 0.1745 0.1622 0.2827 -0.0205 0.0070 -0.0146 310 LEU A O 4628 C CB . LEU A 302 ? 0.1714 0.2288 0.2501 -0.0014 -0.0293 -0.0244 310 LEU A CB 4629 C CG . LEU A 302 ? 0.1969 0.2583 0.2682 -0.0039 -0.0173 -0.0349 310 LEU A CG 4630 C CD1 . LEU A 302 ? 0.2342 0.3467 0.2790 0.0087 -0.0116 -0.0339 310 LEU A CD1 4631 C CD2 . LEU A 302 ? 0.2083 0.2537 0.2784 -0.0094 -0.0483 -0.0100 310 LEU A CD2 4643 N N . PRO A 303 ? 0.2498 0.1900 0.3160 -0.0417 0.0401 -0.0623 311 PRO A N 4644 C CA . PRO A 303 ? 0.2603 0.2025 0.3452 -0.0632 0.0454 -0.0736 311 PRO A CA 4645 C C . PRO A 303 ? 0.2377 0.2346 0.3569 -0.0738 0.0288 -0.0674 311 PRO A C 4646 O O . PRO A 303 ? 0.2344 0.2931 0.3877 -0.0674 0.0142 -0.0702 311 PRO A O 4647 C CB . PRO A 303 ? 0.3338 0.2537 0.3721 -0.0961 0.0992 -0.0955 311 PRO A CB 4648 C CG . PRO A 303 ? 0.3745 0.2789 0.3656 -0.0779 0.0978 -0.1047 311 PRO A CG 4649 C CD . PRO A 303 ? 0.3200 0.2290 0.3359 -0.0631 0.0598 -0.0999 311 PRO A CD 4657 N N . GLY A 304 ? 0.2852 0.2425 0.3437 -0.0887 0.0367 -0.0699 312 GLY A N 4658 C CA . GLY A 304 ? 0.3259 0.3067 0.3542 -0.1066 0.0729 -0.0675 312 GLY A CA 4659 C C . GLY A 304 ? 0.3142 0.3093 0.3477 -0.1482 0.0946 -0.0797 312 GLY A C 4660 O O . GLY A 304 ? 0.3964 0.3568 0.3733 -0.1844 0.1482 -0.1121 312 GLY A O 4664 N N . VAL A 305 ? 0.2176 0.2788 0.3079 -0.0840 0.0124 -0.0502 313 VAL A N 4665 C CA . VAL A 305 ? 0.1797 0.2223 0.2811 -0.0441 0.0096 -0.0254 313 VAL A CA 4666 C C . VAL A 305 ? 0.2032 0.2059 0.2896 -0.0581 0.0042 -0.0129 313 VAL A C 4667 O O . VAL A 305 ? 0.2257 0.2222 0.2836 -0.0394 0.0064 0.0019 313 VAL A O 4668 C CB . VAL A 305 ? 0.1783 0.2089 0.2770 -0.0166 -0.0070 -0.0183 313 VAL A CB 4669 C CG1 . VAL A 305 ? 0.2009 0.2179 0.2754 -0.0138 0.0033 -0.0225 313 VAL A CG1 4670 C CG2 . VAL A 305 ? 0.1703 0.2372 0.2849 0.0000 -0.0059 -0.0290 313 VAL A CG2 4680 N N . VAL A 306 ? 0.2228 0.2021 0.2979 -0.0465 0.0050 -0.0129 314 VAL A N 4681 C CA . VAL A 306 ? 0.2479 0.1791 0.2832 -0.0699 -0.0055 0.0108 314 VAL A CA 4682 C C . VAL A 306 ? 0.2244 0.1774 0.2533 -0.0571 0.0106 0.0258 314 VAL A C 4683 O O . VAL A 306 ? 0.2365 0.2434 0.2552 -0.0511 0.0512 -0.0036 314 VAL A O 4684 C CB . VAL A 306 ? 0.3183 0.2423 0.3060 -0.0964 -0.0269 0.0201 314 VAL A CB 4685 C CG1 . VAL A 306 ? 0.3692 0.2631 0.2991 -0.0981 -0.0099 0.0617 314 VAL A CG1 4686 C CG2 . VAL A 306 ? 0.3781 0.2606 0.3389 -0.1039 -0.0137 0.0060 314 VAL A CG2 4696 N N . ASP A 307 ? 0.2467 0.2128 0.2685 -0.0647 -0.0021 0.0361 315 ASP A N 4697 C CA . ASP A 307 ? 0.2737 0.2267 0.2880 -0.0616 -0.0006 0.0237 315 ASP A CA 4698 C C . ASP A 307 ? 0.2046 0.2168 0.2528 -0.0494 -0.0025 0.0207 315 ASP A C 4699 O O . ASP A 307 ? 0.2415 0.2438 0.2370 -0.0423 -0.0063 -0.0070 315 ASP A O 4700 C CB . ASP A 307 ? 0.3327 0.2581 0.3114 -0.0387 -0.0118 0.0050 315 ASP A CB 4701 C CG . ASP A 307 ? 0.3969 0.2741 0.3228 -0.0313 -0.0172 -0.0185 315 ASP A CG 4702 O OD1 . ASP A 307 ? 0.3710 0.2781 0.3204 0.0245 -0.0681 0.0117 315 ASP A OD1 4703 O OD2 . ASP A 307 ? 0.4620 0.3356 0.3294 -0.0410 0.0065 -0.0269 315 ASP A OD2 4708 N N . GLY A 308 ? 0.2212 0.1820 0.2382 -0.0605 0.0111 0.0208 316 GLY A N 4709 C CA . GLY A 308 ? 0.1832 0.1907 0.2133 -0.0305 -0.0044 0.0197 316 GLY A CA 4710 C C . GLY A 308 ? 0.1430 0.1726 0.2009 -0.0095 -0.0027 0.0272 316 GLY A C 4711 O O . GLY A 308 ? 0.1413 0.1643 0.2028 -0.0208 -0.0084 0.0148 316 GLY A O 4715 N N . ALA A 309 ? 0.1556 0.1708 0.1817 -0.0149 0.0007 0.0112 317 ALA A N 4716 C CA . ALA A 309 ? 0.1509 0.1806 0.1838 -0.0230 0.0000 -0.0057 317 ALA A CA 4717 C C . ALA A 309 ? 0.1446 0.1610 0.1698 -0.0217 -0.0188 0.0029 317 ALA A C 4718 O O . ALA A 309 ? 0.1409 0.1788 0.2011 -0.0295 0.0038 0.0047 317 ALA A O 4719 C CB . ALA A 309 ? 0.1709 0.1448 0.2023 -0.0007 -0.0220 0.0024 317 ALA A CB 4725 N N . ASN A 310 ? 0.1209 0.1608 0.1619 -0.0098 0.0091 0.0034 318 ASN A N 4726 C CA . ASN A 310 ? 0.1089 0.1666 0.1357 -0.0160 0.0033 -0.0085 318 ASN A CA 4727 C C . ASN A 310 ? 0.0977 0.1767 0.1434 -0.0058 0.0147 -0.0005 318 ASN A C 4728 O O . ASN A 310 ? 0.1101 0.1913 0.1572 -0.0042 0.0063 -0.0084 318 ASN A O 4729 C CB . ASN A 310 ? 0.1027 0.1825 0.1454 -0.0183 -0.0012 -0.0022 318 ASN A CB 4730 C CG . ASN A 310 ? 0.1257 0.1793 0.1475 -0.0201 -0.0126 0.0001 318 ASN A CG 4731 O OD1 . ASN A 310 ? 0.1407 0.1891 0.1575 -0.0035 -0.0020 -0.0046 318 ASN A OD1 4732 N ND2 . ASN A 310 ? 0.1315 0.1839 0.1330 -0.0010 0.0095 -0.0214 318 ASN A ND2 4739 N N . ASN A 311 ? 0.1093 0.1608 0.1477 -0.0202 0.0151 0.0103 319 ASN A N 4740 C CA . ASN A 311 ? 0.1102 0.1712 0.1524 -0.0162 0.0209 -0.0050 319 ASN A CA 4741 C C . ASN A 311 ? 0.1041 0.1614 0.1562 -0.0021 0.0161 0.0049 319 ASN A C 4742 O O . ASN A 311 ? 0.0965 0.1744 0.1560 0.0008 0.0007 -0.0029 319 ASN A O 4743 C CB . ASN A 311 ? 0.1210 0.1712 0.1370 -0.0129 0.0062 -0.0022 319 ASN A CB 4744 C CG . ASN A 311 ? 0.1224 0.2030 0.1493 -0.0008 0.0038 0.0055 319 ASN A CG 4745 O OD1 . ASN A 311 ? 0.1132 0.2061 0.1509 0.0057 -0.0063 -0.0108 319 ASN A OD1 4746 N ND2 . ASN A 311 ? 0.1333 0.2116 0.1495 -0.0125 -0.0070 0.0180 319 ASN A ND2 4753 N N . PRO A 312 ? 0.0996 0.1805 0.1396 -0.0005 0.0041 -0.0040 320 PRO A N 4754 C CA . PRO A 312 ? 0.1168 0.1554 0.1354 -0.0022 0.0101 -0.0046 320 PRO A CA 4755 C C . PRO A 312 ? 0.1128 0.1495 0.1500 0.0025 0.0195 -0.0198 320 PRO A C 4756 O O . PRO A 312 ? 0.1171 0.1701 0.1503 0.0019 0.0074 -0.0183 320 PRO A O 4757 C CB . PRO A 312 ? 0.0863 0.1691 0.1535 -0.0015 0.0132 -0.0147 320 PRO A CB 4758 C CG . PRO A 312 ? 0.1071 0.1746 0.1550 -0.0019 -0.0063 -0.0150 320 PRO A CG 4759 C CD . PRO A 312 ? 0.1064 0.1670 0.1581 -0.0069 0.0026 -0.0079 320 PRO A CD 4767 N N . GLY A 313 ? 0.0982 0.1816 0.1361 -0.0004 0.0098 -0.0024 321 GLY A N 4768 C CA . GLY A 313 ? 0.1052 0.1656 0.1591 -0.0077 0.0301 0.0004 321 GLY A CA 4769 C C . GLY A 313 ? 0.1173 0.1633 0.1448 -0.0192 -0.0005 -0.0286 321 GLY A C 4770 O O . GLY A 313 ? 0.1313 0.1743 0.1461 0.0085 -0.0050 -0.0151 321 GLY A O 4774 N N . ILE A 314 ? 0.1257 0.1595 0.1540 0.0021 0.0053 -0.0126 322 ILE A N 4775 C CA . ILE A 314 ? 0.1157 0.1678 0.1582 0.0028 0.0122 0.0079 322 ILE A CA 4776 C C . ILE A 314 ? 0.1191 0.1622 0.1525 -0.0138 0.0201 -0.0064 322 ILE A C 4777 O O . ILE A 314 ? 0.1371 0.1875 0.1481 0.0154 0.0242 0.0110 322 ILE A O 4778 C CB . ILE A 314 ? 0.1169 0.1738 0.1889 -0.0110 0.0169 0.0053 322 ILE A CB 4779 C CG1 . ILE A 314 ? 0.1291 0.1808 0.2064 -0.0132 0.0010 0.0016 322 ILE A CG1 4780 C CG2 . ILE A 314 ? 0.1290 0.1897 0.2011 -0.0108 0.0301 0.0042 322 ILE A CG2 4781 C CD1 . ILE A 314 ? 0.1387 0.1964 0.2146 -0.0118 -0.0019 -0.0086 322 ILE A CD1 4793 N N . ARG A 315 ? 0.1222 0.1608 0.1536 -0.0059 0.0210 -0.0046 323 ARG A N 4794 C CA . ARG A 315 ? 0.1138 0.1448 0.1601 -0.0139 0.0047 0.0016 323 ARG A CA 4795 C C . ARG A 315 ? 0.1195 0.1781 0.1401 -0.0117 -0.0010 -0.0243 323 ARG A C 4796 O O . ARG A 315 ? 0.1369 0.1814 0.1362 -0.0056 0.0045 -0.0132 323 ARG A O 4797 C CB . ARG A 315 ? 0.1270 0.1556 0.1734 -0.0167 0.0048 0.0015 323 ARG A CB 4798 C CG . ARG A 315 ? 0.1169 0.1869 0.1867 -0.0063 0.0101 -0.0151 323 ARG A CG 4799 C CD . ARG A 315 ? 0.1410 0.1645 0.1814 -0.0140 0.0027 0.0081 323 ARG A CD 4800 N NE . ARG A 315 ? 0.1492 0.1722 0.1731 0.0058 -0.0043 0.0193 323 ARG A NE 4801 C CZ . ARG A 315 ? 0.1336 0.1567 0.1936 -0.0047 -0.0146 -0.0116 323 ARG A CZ 4802 N NH1 . ARG A 315 ? 0.1275 0.1607 0.1863 0.0102 0.0016 -0.0124 323 ARG A NH1 4803 N NH2 . ARG A 315 ? 0.1417 0.1676 0.2078 -0.0106 -0.0148 0.0271 323 ARG A NH2 4817 N N . ILE A 316 ? 0.1229 0.1469 0.1481 -0.0026 0.0102 -0.0148 324 ILE A N 4818 C CA . ILE A 316 ? 0.1382 0.1654 0.1669 -0.0178 0.0106 -0.0128 324 ILE A CA 4819 C C . ILE A 316 ? 0.1325 0.1763 0.1582 -0.0009 0.0276 -0.0034 324 ILE A C 4820 O O . ILE A 316 ? 0.1364 0.2131 0.1733 0.0190 0.0139 0.0084 324 ILE A O 4821 C CB . ILE A 316 ? 0.2553 0.1578 0.2171 0.0236 -0.0032 0.0027 324 ILE A CB 4822 C CG1 . ILE A 316 ? 0.2936 0.1714 0.2429 0.0088 -0.0439 -0.0236 324 ILE A CG1 4823 C CG2 . ILE A 316 ? 0.2627 0.1992 0.2546 -0.0195 0.0257 -0.0246 324 ILE A CG2 4824 C CD1 . ILE A 316 ? 0.3023 0.1943 0.2871 0.0045 -0.0460 0.0022 324 ILE A CD1 4836 N N . PHE A 317 ? 0.1313 0.1692 0.1415 0.0063 0.0082 -0.0146 325 PHE A N 4837 C CA . PHE A 317 ? 0.1359 0.1488 0.1585 0.0147 0.0086 -0.0100 325 PHE A CA 4838 C C . PHE A 317 ? 0.1604 0.1502 0.1829 0.0112 0.0036 -0.0060 325 PHE A C 4839 O O . PHE A 317 ? 0.1684 0.1825 0.1822 0.0157 0.0152 -0.0270 325 PHE A O 4840 C CB . PHE A 317 ? 0.1403 0.1623 0.1749 0.0195 0.0035 -0.0199 325 PHE A CB 4841 C CG . PHE A 317 ? 0.1601 0.1619 0.1748 0.0306 -0.0211 -0.0193 325 PHE A CG 4842 C CD1 . PHE A 317 ? 0.1495 0.1853 0.1710 -0.0110 -0.0157 -0.0080 325 PHE A CD1 4843 C CD2 . PHE A 317 ? 0.1780 0.1441 0.1621 0.0058 -0.0107 -0.0034 325 PHE A CD2 4844 C CE1 . PHE A 317 ? 0.1727 0.1747 0.1584 0.0116 -0.0156 -0.0115 325 PHE A CE1 4845 C CE2 . PHE A 317 ? 0.1620 0.1737 0.1501 0.0166 -0.0058 0.0072 325 PHE A CE2 4846 C CZ . PHE A 317 ? 0.1607 0.1632 0.1460 -0.0058 -0.0178 -0.0126 325 PHE A CZ 4856 N N . GLU A 318 ? 0.1559 0.1430 0.1963 0.0123 0.0131 -0.0073 326 GLU A N 4857 C CA . GLU A 318 ? 0.1445 0.1521 0.2072 0.0052 0.0100 -0.0264 326 GLU A CA 4858 C C . GLU A 318 ? 0.1499 0.1420 0.2157 0.0062 0.0372 -0.0319 326 GLU A C 4859 O O . GLU A 318 ? 0.1604 0.1735 0.2158 0.0098 0.0067 -0.0118 326 GLU A O 4860 C CB . GLU A 318 ? 0.1870 0.1768 0.2095 0.0326 -0.0027 -0.0248 326 GLU A CB 4861 C CG . GLU A 318 ? 0.2152 0.2429 0.2170 -0.0025 0.0088 -0.0324 326 GLU A CG 4862 C CD . GLU A 318 ? 0.2484 0.2608 0.2338 0.0090 -0.0066 -0.0449 326 GLU A CD 4863 O OE1 . GLU A 318 ? 0.2825 0.2644 0.2374 0.0223 0.0163 -0.0476 326 GLU A OE1 4864 O OE2 . GLU A 318 ? 0.2939 0.3125 0.2462 0.0205 -0.0299 -0.0320 326 GLU A OE2 4871 N N . TYR A 319 ? 0.1728 0.1494 0.2078 -0.0005 0.0203 -0.0244 327 TYR A N 4872 C CA . TYR A 319 ? 0.1743 0.1543 0.2070 0.0058 -0.0135 -0.0244 327 TYR A CA 4873 C C . TYR A 319 ? 0.1872 0.1728 0.2111 0.0031 -0.0074 -0.0315 327 TYR A C 4874 O O . TYR A 319 ? 0.2082 0.1412 0.2230 0.0289 -0.0169 -0.0181 327 TYR A O 4875 C CB . TYR A 319 ? 0.2007 0.1594 0.1958 0.0151 -0.0293 -0.0355 327 TYR A CB 4876 C CG . TYR A 319 ? 0.1947 0.1546 0.2038 0.0070 -0.0272 -0.0228 327 TYR A CG 4877 C CD1 . TYR A 319 ? 0.1921 0.1810 0.1962 0.0306 -0.0104 -0.0028 327 TYR A CD1 4878 C CD2 . TYR A 319 ? 0.2408 0.1673 0.2162 0.0076 -0.0123 -0.0134 327 TYR A CD2 4879 C CE1 . TYR A 319 ? 0.2183 0.2270 0.2203 0.0328 0.0041 -0.0369 327 TYR A CE1 4880 C CE2 . TYR A 319 ? 0.2252 0.1948 0.2083 0.0340 -0.0258 -0.0192 327 TYR A CE2 4881 C CZ . TYR A 319 ? 0.1868 0.1678 0.2197 0.0163 0.0066 -0.0243 327 TYR A CZ 4882 O OH . TYR A 319 ? 0.2224 0.2158 0.2392 0.0044 0.0058 -0.0017 327 TYR A OH 4892 N N . ASP A 320 ? 0.1806 0.1774 0.2136 0.0189 -0.0032 -0.0173 328 ASP A N 4893 C CA . ASP A 320 ? 0.2228 0.1571 0.2455 0.0515 -0.0112 -0.0298 328 ASP A CA 4894 C C . ASP A 320 ? 0.2208 0.1779 0.2419 0.0444 -0.0217 -0.0195 328 ASP A C 4895 O O . ASP A 320 ? 0.2300 0.1974 0.2299 0.0185 -0.0359 -0.0287 328 ASP A O 4896 C CB . ASP A 320 ? 0.2341 0.2111 0.3046 0.0770 -0.0317 -0.0555 328 ASP A CB 4897 C CG . ASP A 320 ? 0.2731 0.2842 0.3891 0.0556 -0.0466 -0.0944 328 ASP A CG 4898 O OD1 . ASP A 320 ? 0.3035 0.3345 0.4463 0.0760 -0.0355 -0.0668 328 ASP A OD1 4899 O OD2 . ASP A 320 ? 0.3605 0.3478 0.4131 0.0746 -0.0756 -0.0777 328 ASP A OD2 4904 N N . ARG A 321 ? 0.2308 0.2030 0.2515 0.0500 -0.0185 -0.0213 329 ARG A N 4905 C CA . ARG A 321 ? 0.2256 0.1872 0.2862 0.0328 -0.0271 -0.0247 329 ARG A CA 4906 C C . ARG A 321 ? 0.2678 0.1975 0.2983 0.0140 -0.0518 -0.0133 329 ARG A C 4907 O O . ARG A 321 ? 0.3243 0.2587 0.2926 0.0063 -0.0622 -0.0033 329 ARG A O 4908 C CB . ARG A 321 ? 0.2463 0.1752 0.2805 0.0031 -0.0488 -0.0043 329 ARG A CB 4909 C CG . ARG A 321 ? 0.2552 0.1544 0.2951 0.0061 -0.0362 0.0097 329 ARG A CG 4910 C CD . ARG A 321 ? 0.2378 0.1875 0.3188 0.0151 -0.0322 -0.0117 329 ARG A CD 4911 N NE . ARG A 321 ? 0.2330 0.1766 0.3235 0.0010 -0.0195 -0.0068 329 ARG A NE 4912 C CZ . ARG A 321 ? 0.2492 0.1564 0.3275 0.0107 -0.0257 0.0068 329 ARG A CZ 4913 N NH1 . ARG A 321 ? 0.2473 0.1836 0.3389 0.0144 -0.0172 -0.0137 329 ARG A NH1 4914 N NH2 . ARG A 321 ? 0.2108 0.1625 0.3186 -0.0153 0.0012 -0.0190 329 ARG A NH2 4928 N N . ALA A 322 ? 0.3031 0.1893 0.3102 0.0415 -0.0866 -0.0029 330 ALA A N 4929 C CA . ALA A 322 ? 0.3222 0.2659 0.3394 0.0518 -0.1053 -0.0225 330 ALA A CA 4930 C C . ALA A 322 ? 0.2913 0.2766 0.3268 0.0346 -0.1186 -0.0104 330 ALA A C 4931 O O . ALA A 322 ? 0.3469 0.3178 0.3646 0.0222 -0.1223 0.0323 330 ALA A O 4932 C CB . ALA A 322 ? 0.3679 0.3009 0.3751 0.0827 -0.0991 -0.0403 330 ALA A CB 4938 N N . THR A 323 ? 0.2504 0.2142 0.3033 0.0792 -0.0668 -0.0331 331 THR A N 4939 C CA . THR A 323 ? 0.2430 0.2371 0.2814 0.0586 -0.0363 -0.0033 331 THR A CA 4940 C C . THR A 323 ? 0.2305 0.1950 0.2348 0.0255 -0.0327 -0.0138 331 THR A C 4941 O O . THR A 323 ? 0.2200 0.2197 0.2239 0.0417 -0.0390 -0.0176 331 THR A O 4942 C CB . THR A 323 ? 0.2497 0.2528 0.2975 0.0976 -0.0391 -0.0124 331 THR A CB 4943 O OG1 . THR A 323 ? 0.2592 0.2327 0.3123 0.0769 -0.0222 -0.0247 331 THR A OG1 4944 C CG2 . THR A 323 ? 0.2619 0.2845 0.3217 0.1038 -0.0570 -0.0225 331 THR A CG2 4952 N N . LEU A 324 ? 0.1787 0.1721 0.2315 0.0281 -0.0275 -0.0080 332 LEU A N 4953 C CA . LEU A 324 ? 0.1726 0.1874 0.2011 0.0419 0.0076 -0.0174 332 LEU A CA 4954 C C . LEU A 324 ? 0.1805 0.1974 0.1795 0.0412 0.0133 -0.0237 332 LEU A C 4955 O O . LEU A 324 ? 0.2015 0.1857 0.1816 0.0432 0.0098 -0.0260 332 LEU A O 4956 C CB . LEU A 324 ? 0.1599 0.2165 0.2112 0.0101 0.0076 -0.0249 332 LEU A CB 4957 C CG . LEU A 324 ? 0.2274 0.2437 0.2494 -0.0186 0.0307 -0.0237 332 LEU A CG 4958 C CD1 . LEU A 324 ? 0.2191 0.2412 0.2030 0.0158 0.0088 -0.0423 332 LEU A CD1 4959 C CD2 . LEU A 324 ? 0.2476 0.3074 0.2666 -0.0319 0.0286 -0.0004 332 LEU A CD2 4971 N N . ASN A 325 ? 0.2066 0.2044 0.1973 0.0424 0.0084 -0.0234 333 ASN A N 4972 C CA . ASN A 325 ? 0.1664 0.2085 0.2003 0.0341 -0.0098 -0.0207 333 ASN A CA 4973 C C . ASN A 325 ? 0.1743 0.1938 0.1987 -0.0080 0.0096 -0.0360 333 ASN A C 4974 O O . ASN A 325 ? 0.1855 0.2063 0.2002 0.0412 -0.0064 -0.0208 333 ASN A O 4975 C CB . ASN A 325 ? 0.1752 0.2454 0.2396 0.0539 -0.0009 -0.0183 333 ASN A CB 4976 C CG . ASN A 325 ? 0.2227 0.3212 0.2936 0.0567 -0.0008 -0.0451 333 ASN A CG 4977 O OD1 . ASN A 325 ? 0.2262 0.4142 0.3068 0.0619 -0.0405 -0.0602 333 ASN A OD1 4978 N ND2 . ASN A 325 ? 0.2562 0.3442 0.3335 0.0624 -0.0127 -0.0126 333 ASN A ND2 4985 N N . LEU A 326 ? 0.1691 0.1697 0.1958 0.0217 -0.0019 -0.0332 334 LEU A N 4986 C CA . LEU A 326 ? 0.1667 0.1680 0.1894 0.0088 0.0018 -0.0207 334 LEU A CA 4987 C C . LEU A 326 ? 0.1455 0.1828 0.1891 0.0103 0.0087 -0.0028 334 LEU A C 4988 O O . LEU A 326 ? 0.1569 0.2114 0.1950 0.0096 0.0266 -0.0264 334 LEU A O 4989 C CB . LEU A 326 ? 0.1332 0.1566 0.2121 0.0132 0.0092 -0.0286 334 LEU A CB 4990 C CG . LEU A 326 ? 0.1577 0.1771 0.2057 0.0286 0.0174 -0.0216 334 LEU A CG 4991 C CD1 . LEU A 326 ? 0.1997 0.1834 0.2488 0.0288 0.0268 -0.0305 334 LEU A CD1 4992 C CD2 . LEU A 326 ? 0.1767 0.1945 0.1862 0.0183 0.0191 -0.0077 334 LEU A CD2 5004 N N . LYS A 327 ? 0.1356 0.1876 0.2028 0.0436 0.0096 -0.0277 335 LYS A N 5005 C CA . LYS A 327 ? 0.1689 0.1770 0.2012 0.0241 0.0224 -0.0356 335 LYS A CA 5006 C C . LYS A 327 ? 0.1458 0.1888 0.1868 0.0224 0.0213 -0.0145 335 LYS A C 5007 O O . LYS A 327 ? 0.1561 0.2352 0.1897 0.0362 0.0144 -0.0241 335 LYS A O 5008 C CB . LYS A 327 ? 0.2167 0.1907 0.2089 0.0374 0.0023 -0.0412 335 LYS A CB 5009 C CG . LYS A 327 ? 0.2331 0.2141 0.2595 0.0601 -0.0031 -0.0403 335 LYS A CG 5010 C CD . LYS A 327 ? 0.2773 0.2665 0.3403 0.1193 0.0025 0.0045 335 LYS A CD 5011 C CE . LYS A 327 ? 0.3106 0.3592 0.3863 0.1113 0.0100 -0.0046 335 LYS A CE 5012 N NZ . LYS A 327 ? 0.3403 0.4029 0.4184 0.0915 0.0232 -0.0073 335 LYS A NZ 5026 N N . ASP A 328 ? 0.1533 0.1695 0.1668 0.0117 0.0142 -0.0271 336 ASP A N 5027 C CA . ASP A 328 ? 0.1644 0.1669 0.1657 0.0060 0.0045 -0.0061 336 ASP A CA 5028 C C . ASP A 328 ? 0.1554 0.1668 0.1782 0.0100 0.0015 -0.0133 336 ASP A C 5029 O O . ASP A 328 ? 0.1509 0.1872 0.1756 0.0076 -0.0014 -0.0197 336 ASP A O 5030 C CB . ASP A 328 ? 0.1892 0.1853 0.1696 0.0226 -0.0040 -0.0226 336 ASP A CB 5031 C CG . ASP A 328 ? 0.1750 0.2047 0.1805 0.0372 -0.0104 -0.0091 336 ASP A CG 5032 O OD1 . ASP A 328 ? 0.1652 0.1981 0.1762 0.0217 0.0224 -0.0168 336 ASP A OD1 5033 O OD2 . ASP A 328 ? 0.2002 0.2405 0.1780 0.0375 0.0185 -0.0413 336 ASP A OD2 5038 N N . LEU A 329 ? 0.1474 0.1761 0.1734 0.0168 0.0081 -0.0071 337 LEU A N 5039 C CA . LEU A 329 ? 0.1432 0.1830 0.1703 0.0304 0.0003 -0.0366 337 LEU A CA 5040 C C . LEU A 329 ? 0.1265 0.1746 0.1669 0.0322 0.0113 -0.0138 337 LEU A C 5041 O O . LEU A 329 ? 0.1277 0.2217 0.1752 -0.0005 0.0148 0.0001 337 LEU A O 5042 C CB . LEU A 329 ? 0.1774 0.1973 0.1815 0.0272 0.0060 0.0026 337 LEU A CB 5043 C CG . LEU A 329 ? 0.2009 0.2089 0.1829 -0.0123 0.0146 0.0178 337 LEU A CG 5044 C CD1 . LEU A 329 ? 0.1858 0.2330 0.1869 0.0086 0.0002 -0.0203 337 LEU A CD1 5045 C CD2 . LEU A 329 ? 0.2019 0.2377 0.1763 -0.0180 0.0166 -0.0165 337 LEU A CD2 5057 N N . VAL A 330 ? 0.1468 0.1507 0.1543 0.0213 0.0051 -0.0073 338 VAL A N 5058 C CA . VAL A 330 ? 0.1556 0.1787 0.1550 -0.0155 0.0063 -0.0122 338 VAL A CA 5059 C C . VAL A 330 ? 0.1234 0.1607 0.1624 0.0071 0.0140 -0.0159 338 VAL A C 5060 O O . VAL A 330 ? 0.1329 0.2025 0.1509 0.0029 0.0219 0.0057 338 VAL A O 5061 C CB . VAL A 330 ? 0.1807 0.1885 0.1664 -0.0145 0.0246 -0.0317 338 VAL A CB 5062 C CG1 . VAL A 330 ? 0.1930 0.2292 0.1569 -0.0300 0.0056 -0.0341 338 VAL A CG1 5063 C CG2 . VAL A 330 ? 0.2078 0.1947 0.1952 0.0217 0.0269 -0.0445 338 VAL A CG2 5073 N N . THR A 331 ? 0.1294 0.1733 0.1473 -0.0016 0.0117 -0.0208 339 THR A N 5074 C CA . THR A 331 ? 0.1487 0.1595 0.1436 0.0230 0.0093 -0.0104 339 THR A CA 5075 C C . THR A 331 ? 0.1547 0.1682 0.1353 0.0196 0.0099 -0.0154 339 THR A C 5076 O O . THR A 331 ? 0.1323 0.1935 0.1459 0.0058 0.0027 -0.0094 339 THR A O 5077 C CB . THR A 331 ? 0.1411 0.1813 0.1384 0.0173 0.0115 -0.0156 339 THR A CB 5078 O OG1 . THR A 331 ? 0.1457 0.1819 0.1588 -0.0159 -0.0095 -0.0049 339 THR A OG1 5079 C CG2 . THR A 331 ? 0.1755 0.1693 0.1538 -0.0114 0.0062 0.0114 339 THR A CG2 5087 N N . TYR A 332 ? 0.1298 0.1858 0.1531 0.0077 0.0018 -0.0238 340 TYR A N 5088 C CA . TYR A 332 ? 0.1482 0.1728 0.1598 -0.0062 0.0061 -0.0144 340 TYR A CA 5089 C C . TYR A 332 ? 0.1343 0.1664 0.1574 -0.0003 0.0178 -0.0198 340 TYR A C 5090 O O . TYR A 332 ? 0.1477 0.1660 0.1557 0.0033 0.0031 -0.0202 340 TYR A O 5091 C CB . TYR A 332 ? 0.1549 0.1592 0.1876 0.0053 0.0036 -0.0049 340 TYR A CB 5092 C CG . TYR A 332 ? 0.1538 0.1787 0.2169 -0.0161 0.0129 -0.0195 340 TYR A CG 5093 C CD1 . TYR A 332 ? 0.1497 0.1690 0.2829 -0.0156 0.0283 0.0192 340 TYR A CD1 5094 C CD2 . TYR A 332 ? 0.2082 0.1734 0.2555 -0.0106 0.0583 -0.0200 340 TYR A CD2 5095 C CE1 . TYR A 332 ? 0.1844 0.1925 0.3330 0.0335 0.0501 0.0287 340 TYR A CE1 5096 C CE2 . TYR A 332 ? 0.2488 0.1531 0.3077 -0.0220 0.1005 -0.0339 340 TYR A CE2 5097 C CZ . TYR A 332 ? 0.2328 0.1590 0.3735 0.0401 0.0935 -0.0332 340 TYR A CZ 5098 O OH . TYR A 332 ? 0.2810 0.1872 0.4630 0.0392 0.1281 -0.0212 340 TYR A OH 5108 N N . PHE A 333 ? 0.1138 0.1885 0.1613 0.0189 0.0062 -0.0198 341 PHE A N 5109 C CA . PHE A 333 ? 0.1031 0.1951 0.1589 0.0026 -0.0049 -0.0079 341 PHE A CA 5110 C C . PHE A 333 ? 0.1320 0.1922 0.1714 0.0027 0.0174 -0.0242 341 PHE A C 5111 O O . PHE A 333 ? 0.1411 0.2031 0.1863 0.0125 -0.0092 -0.0483 341 PHE A O 5112 C CB . PHE A 333 ? 0.1234 0.2019 0.1667 -0.0184 -0.0120 -0.0135 341 PHE A CB 5113 C CG . PHE A 333 ? 0.1267 0.2153 0.1731 -0.0056 0.0029 -0.0106 341 PHE A CG 5114 C CD1 . PHE A 333 ? 0.1337 0.2269 0.1571 0.0150 0.0148 0.0005 341 PHE A CD1 5115 C CD2 . PHE A 333 ? 0.1598 0.2027 0.1627 -0.0126 0.0163 -0.0097 341 PHE A CD2 5116 C CE1 . PHE A 333 ? 0.1680 0.2370 0.1802 0.0047 0.0017 -0.0055 341 PHE A CE1 5117 C CE2 . PHE A 333 ? 0.1891 0.2152 0.1742 -0.0053 0.0090 0.0082 341 PHE A CE2 5118 C CZ . PHE A 333 ? 0.1776 0.2377 0.1719 0.0172 0.0128 0.0040 341 PHE A CZ 5128 N N . LEU A 334 ? 0.1330 0.1836 0.1615 -0.0079 -0.0119 -0.0200 342 LEU A N 5129 C CA . LEU A 334 ? 0.1196 0.1850 0.1657 0.0082 -0.0253 -0.0205 342 LEU A CA 5130 C C . LEU A 334 ? 0.1322 0.2292 0.1522 0.0220 -0.0211 -0.0119 342 LEU A C 5131 O O . LEU A 334 ? 0.1723 0.2168 0.1465 -0.0138 -0.0157 -0.0069 342 LEU A O 5132 C CB . LEU A 334 ? 0.1268 0.1878 0.1621 -0.0025 -0.0031 -0.0259 342 LEU A CB 5133 C CG . LEU A 334 ? 0.1213 0.2255 0.1568 -0.0081 -0.0029 0.0088 342 LEU A CG 5134 C CD1 . LEU A 334 ? 0.1622 0.2123 0.1835 -0.0086 -0.0222 -0.0077 342 LEU A CD1 5135 C CD2 . LEU A 334 ? 0.1329 0.2987 0.1747 0.0115 -0.0163 -0.0026 342 LEU A CD2 5147 N N . ASN A 335 ? 0.1408 0.2100 0.1552 0.0049 -0.0103 -0.0098 343 ASN A N 5148 C CA . ASN A 335 ? 0.1546 0.2315 0.1385 -0.0018 -0.0077 -0.0141 343 ASN A CA 5149 C C . ASN A 335 ? 0.1309 0.2066 0.1606 -0.0035 0.0019 -0.0115 343 ASN A C 5150 O O . ASN A 335 ? 0.1349 0.2280 0.1820 -0.0090 -0.0291 -0.0182 343 ASN A O 5151 C CB . ASN A 335 ? 0.1504 0.2813 0.1465 -0.0101 -0.0091 -0.0040 343 ASN A CB 5152 C CG . ASN A 335 ? 0.1913 0.3416 0.1796 -0.0325 -0.0043 0.0275 343 ASN A CG 5153 O OD1 . ASN A 335 ? 0.2142 0.3291 0.2107 -0.0179 0.0129 0.0589 343 ASN A OD1 5154 N ND2 . ASN A 335 ? 0.2914 0.4042 0.2146 -0.0288 0.0620 0.0405 343 ASN A ND2 5161 N N . LEU A 336 ? 0.1156 0.2047 0.1694 -0.0118 -0.0011 -0.0292 344 LEU A N 5162 C CA . LEU A 336 ? 0.1453 0.2263 0.2004 -0.0161 0.0004 -0.0242 344 LEU A CA 5163 C C . LEU A 336 ? 0.1382 0.2275 0.2123 -0.0045 -0.0219 -0.0374 344 LEU A C 5164 O O . LEU A 336 ? 0.1571 0.2890 0.2173 0.0181 -0.0338 -0.0649 344 LEU A O 5165 C CB . LEU A 336 ? 0.1432 0.2718 0.2145 -0.0258 0.0210 -0.0591 344 LEU A CB 5166 C CG . LEU A 336 ? 0.1542 0.2826 0.1992 -0.0192 -0.0013 -0.0446 344 LEU A CG 5167 C CD1 . LEU A 336 ? 0.1743 0.3339 0.2123 -0.0534 0.0375 -0.0291 344 LEU A CD1 5168 C CD2 . LEU A 336 ? 0.1857 0.2947 0.1968 0.0027 -0.0033 -0.0568 344 LEU A CD2 5180 N N . ARG A 337 ? 0.1480 0.2173 0.2434 0.0001 -0.0237 0.0209 345 ARG A N 5181 C CA . ARG A 337 ? 0.2237 0.2961 0.2698 0.0169 -0.0438 0.0302 345 ARG A CA 5182 C C . ARG A 337 ? 0.1879 0.2730 0.2387 0.0210 -0.0680 0.0114 345 ARG A C 5183 O O . ARG A 337 ? 0.2179 0.3122 0.2730 0.0439 -0.0810 -0.0077 345 ARG A O 5184 C CB . ARG A 337 ? 0.3417 0.3375 0.3021 0.0023 -0.0646 0.0885 345 ARG A CB 5185 C CG . ARG A 337 ? 0.4355 0.4409 0.3206 -0.0359 -0.0838 0.0707 345 ARG A CG 5186 C CD . ARG A 337 ? 0.5167 0.5165 0.3384 -0.0896 -0.0948 0.0720 345 ARG A CD 5187 N NE . ARG A 337 ? 0.6098 0.5988 0.3781 -0.1050 -0.0621 0.0395 345 ARG A NE 5188 C CZ . ARG A 337 ? 0.6577 0.6443 0.4114 -0.1096 -0.0518 0.0297 345 ARG A CZ 5189 N NH1 . ARG A 337 ? 0.6808 0.6368 0.4369 -0.1135 -0.0374 0.0242 345 ARG A NH1 5190 N NH2 . ARG A 337 ? 0.6731 0.6930 0.4150 -0.1028 -0.0518 0.0297 345 ARG A NH2 5204 N N . GLN A 338 ? 0.1787 0.2575 0.2011 -0.0004 -0.0386 0.0150 346 GLN A N 5205 C CA . GLN A 338 ? 0.1910 0.2871 0.1680 0.0021 -0.0073 0.0124 346 GLN A CA 5206 C C . GLN A 338 ? 0.1593 0.2753 0.1632 0.0138 -0.0237 0.0033 346 GLN A C 5207 O O . GLN A 338 ? 0.1600 0.3129 0.1679 -0.0057 -0.0354 -0.0119 346 GLN A O 5208 C CB . GLN A 338 ? 0.2406 0.2588 0.1608 0.0330 -0.0167 0.0206 346 GLN A CB 5209 C CG . GLN A 338 ? 0.2816 0.2613 0.1671 0.0270 -0.0021 -0.0083 346 GLN A CG 5210 C CD . GLN A 338 ? 0.3053 0.2801 0.1687 -0.0069 -0.0229 0.0055 346 GLN A CD 5211 O OE1 . GLN A 338 ? 0.3822 0.3067 0.1716 0.0137 -0.0153 0.0139 346 GLN A OE1 5212 N NE2 . GLN A 338 ? 0.2618 0.3269 0.1578 -0.0360 -0.0088 0.0088 346 GLN A NE2 5221 N N . ALA A 339 ? 0.1610 0.2597 0.1478 -0.0244 -0.0337 0.0107 347 ALA A N 5222 C CA . ALA A 339 ? 0.1730 0.2694 0.1596 -0.0310 -0.0178 -0.0072 347 ALA A CA 5223 C C . ALA A 339 ? 0.1560 0.2432 0.1510 -0.0235 -0.0241 -0.0254 347 ALA A C 5224 O O . ALA A 339 ? 0.1655 0.2530 0.1527 -0.0316 -0.0120 -0.0130 347 ALA A O 5225 C CB . ALA A 339 ? 0.1837 0.3220 0.1858 -0.0554 -0.0425 0.0276 347 ALA A CB 5231 N N . ASN A 340 ? 0.1654 0.2467 0.1547 -0.0203 -0.0217 -0.0172 348 ASN A N 5232 C CA . ASN A 340 ? 0.2022 0.2400 0.1539 0.0009 -0.0114 0.0025 348 ASN A CA 5233 C C . ASN A 340 ? 0.1638 0.2909 0.1760 0.0044 -0.0175 -0.0010 348 ASN A C 5234 O O . ASN A 340 ? 0.1686 0.3600 0.2118 -0.0066 -0.0081 -0.0325 348 ASN A O 5235 C CB . ASN A 340 ? 0.2272 0.1976 0.1808 0.0023 -0.0006 0.0185 348 ASN A CB 5236 C CG . ASN A 340 ? 0.1877 0.2406 0.1828 -0.0040 -0.0155 0.0261 348 ASN A CG 5237 O OD1 . ASN A 340 ? 0.2806 0.2364 0.1690 -0.0227 0.0007 0.0099 348 ASN A OD1 5238 N ND2 . ASN A 340 ? 0.1910 0.2902 0.1842 -0.0227 -0.0123 -0.0030 348 ASN A ND2 5245 N N . VAL A 341 ? 0.1523 0.3020 0.1580 -0.0046 -0.0187 0.0084 349 VAL A N 5246 C CA . VAL A 341 ? 0.1516 0.3365 0.1664 -0.0165 -0.0379 0.0031 349 VAL A CA 5247 C C . VAL A 341 ? 0.1740 0.3186 0.1845 -0.0103 -0.0478 -0.0028 349 VAL A C 5248 O O . VAL A 341 ? 0.1990 0.3594 0.1945 -0.0588 -0.0708 0.0060 349 VAL A O 5249 C CB . VAL A 341 ? 0.1652 0.3842 0.1966 -0.0473 -0.0269 0.0430 349 VAL A CB 5250 C CG1 . VAL A 341 ? 0.2055 0.3908 0.2084 -0.0303 -0.0022 0.0687 349 VAL A CG1 5251 C CG2 . VAL A 341 ? 0.1680 0.4008 0.2334 -0.0012 0.0088 0.0556 349 VAL A CG2 5261 N N . GLN A 342 ? 0.1899 0.2801 0.2002 0.0013 -0.0309 -0.0236 350 GLN A N 5262 C CA . GLN A 342 ? 0.1953 0.2866 0.2198 0.0034 -0.0206 -0.0320 350 GLN A CA 5263 C C . GLN A 342 ? 0.1811 0.2946 0.2405 -0.0352 -0.0242 -0.0483 350 GLN A C 5264 O O . GLN A 342 ? 0.2016 0.3189 0.2466 -0.0529 0.0062 -0.0349 350 GLN A O 5265 C CB . GLN A 342 ? 0.1998 0.2896 0.2253 -0.0277 -0.0199 -0.0192 350 GLN A CB 5266 C CG . GLN A 342 ? 0.2250 0.2889 0.2314 -0.0069 -0.0063 0.0039 350 GLN A CG 5267 C CD . GLN A 342 ? 0.2609 0.3532 0.2535 0.0107 -0.0077 0.0103 350 GLN A CD 5268 O OE1 . GLN A 342 ? 0.2576 0.4425 0.3033 0.0525 -0.0207 0.0366 350 GLN A OE1 5269 N NE2 . GLN A 342 ? 0.3103 0.3848 0.2649 0.0251 0.0492 0.0333 350 GLN A NE2 5278 N N . GLU A 343 ? 0.2087 0.3267 0.2896 -0.0424 -0.0262 -0.0313 351 GLU A N 5279 C CA . GLU A 343 ? 0.2241 0.3514 0.3134 -0.0757 -0.0506 -0.0465 351 GLU A CA 5280 C C . GLU A 343 ? 0.2257 0.3444 0.3535 -0.1002 -0.0621 -0.0176 351 GLU A C 5281 O O . GLU A 343 ? 0.2922 0.3819 0.3725 -0.1193 -0.0387 -0.0182 351 GLU A O 5282 C CB . GLU A 343 ? 0.2884 0.4301 0.2936 -0.0560 -0.0635 -0.0180 351 GLU A CB 5283 C CG . GLU A 343 ? 0.3128 0.5051 0.3051 -0.0557 -0.0283 0.0379 351 GLU A CG 5284 C CD . GLU A 343 ? 0.3232 0.5506 0.3272 -0.0647 0.0257 0.0883 351 GLU A CD 5285 O OE1 . GLU A 343 ? 0.3646 0.5876 0.3388 -0.0374 0.0354 0.1122 351 GLU A OE1 5286 O OE2 . GLU A 343 ? 0.3238 0.5571 0.3256 -0.0950 0.0453 0.0968 351 GLU A OE2 5293 N N . THR A 344 ? 0.2459 0.3844 0.3952 -0.0615 -0.0816 0.0442 352 THR A N 5294 C CA . THR A 344 ? 0.2880 0.4015 0.4470 -0.0912 -0.0999 0.0449 352 THR A CA 5295 C C . THR A 344 ? 0.2330 0.4301 0.4542 -0.0914 -0.0953 0.0707 352 THR A C 5296 O O . THR A 344 ? 0.2070 0.4421 0.4353 -0.0910 -0.0796 0.0979 352 THR A O 5297 C CB . THR A 344 ? 0.3558 0.4060 0.4962 -0.1371 -0.1150 0.0503 352 THR A CB 5298 O OG1 . THR A 344 ? 0.4213 0.4225 0.5321 -0.1262 -0.0860 0.0465 352 THR A OG1 5299 C CG2 . THR A 344 ? 0.4049 0.4421 0.4992 -0.1118 -0.1366 0.0416 352 THR A CG2 5307 N N . PRO A 345 ? 0.2381 0.4210 0.4754 -0.0954 -0.0584 0.0539 353 PRO A N 5308 C CA . PRO A 345 ? 0.2536 0.4203 0.4899 -0.0926 -0.0534 0.0183 353 PRO A CA 5309 C C . PRO A 345 ? 0.2795 0.4192 0.5217 -0.0283 -0.0195 0.0548 353 PRO A C 5310 O O . PRO A 345 ? 0.3151 0.4243 0.5703 -0.0079 0.0076 0.0755 353 PRO A O 5311 C CB . PRO A 345 ? 0.3104 0.4799 0.5027 -0.0878 -0.0303 0.0136 353 PRO A CB 5312 C CG . PRO A 345 ? 0.2984 0.4862 0.4984 -0.0687 -0.0375 0.0075 353 PRO A CG 5313 C CD . PRO A 345 ? 0.2541 0.4559 0.4775 -0.0706 -0.0750 0.0273 353 PRO A CD 5321 N N . ARG A 346 ? 0.2466 0.3652 0.4849 0.0131 -0.0567 0.0275 354 ARG A N 5322 C CA . ARG A 346 ? 0.2500 0.3520 0.4334 -0.0560 -0.0626 -0.0289 354 ARG A CA 5323 C C . ARG A 346 ? 0.2113 0.2707 0.3363 -0.0490 -0.0625 -0.0503 354 ARG A C 5324 O O . ARG A 346 ? 0.2018 0.2719 0.2833 0.0010 -0.0625 -0.0443 354 ARG A O 5325 C CB . ARG A 346 ? 0.3438 0.4941 0.4583 -0.1055 -0.0698 -0.0465 354 ARG A CB 5326 C CG . ARG A 346 ? 0.4242 0.5769 0.4762 -0.1335 -0.0733 -0.0716 354 ARG A CG 5327 C CD . ARG A 346 ? 0.5270 0.6684 0.5042 -0.1236 -0.0335 -0.0693 354 ARG A CD 5328 N NE . ARG A 346 ? 0.5929 0.7395 0.5247 -0.1111 -0.0198 -0.0640 354 ARG A NE 5329 C CZ . ARG A 346 ? 0.6446 0.7935 0.5433 -0.0882 -0.0034 -0.0587 354 ARG A CZ 5330 N NH1 . ARG A 346 ? 0.6549 0.8049 0.5496 -0.0857 0.0126 -0.0493 354 ARG A NH1 5331 N NH2 . ARG A 346 ? 0.6586 0.8160 0.5492 -0.0786 -0.0013 -0.0553 354 ARG A NH2 5345 N N . TRP A 347 ? 0.1828 0.2346 0.3103 -0.0396 -0.0510 -0.0341 355 TRP A N 5346 C CA . TRP A 347 ? 0.1634 0.1842 0.2715 -0.0032 -0.0362 -0.0243 355 TRP A CA 5347 C C . TRP A 347 ? 0.1827 0.2182 0.2449 0.0138 -0.0462 -0.0448 355 TRP A C 5348 O O . TRP A 347 ? 0.2318 0.2271 0.2746 -0.0190 -0.0233 -0.0524 355 TRP A O 5349 C CB . TRP A 347 ? 0.1793 0.1842 0.2451 0.0182 -0.0008 0.0009 355 TRP A CB 5350 C CG . TRP A 347 ? 0.1190 0.1856 0.2425 0.0011 0.0022 0.0236 355 TRP A CG 5351 C CD1 . TRP A 347 ? 0.1551 0.2579 0.2532 0.0034 0.0007 0.0499 355 TRP A CD1 5352 C CD2 . TRP A 347 ? 0.1356 0.1905 0.2290 0.0023 0.0144 0.0272 355 TRP A CD2 5353 N NE1 . TRP A 347 ? 0.1369 0.2420 0.2637 0.0089 0.0207 0.0685 355 TRP A NE1 5354 C CE2 . TRP A 347 ? 0.1548 0.2232 0.2413 0.0026 0.0180 0.0346 355 TRP A CE2 5355 C CE3 . TRP A 347 ? 0.1454 0.2053 0.2203 -0.0102 0.0202 0.0171 355 TRP A CE3 5356 C CZ2 . TRP A 347 ? 0.1958 0.1936 0.2539 0.0310 0.0432 0.0416 355 TRP A CZ2 5357 C CZ3 . TRP A 347 ? 0.2099 0.1609 0.2264 0.0045 0.0449 0.0086 355 TRP A CZ3 5358 C CH2 . TRP A 347 ? 0.2253 0.1782 0.2309 0.0176 0.0413 0.0256 355 TRP A CH2 5369 N N . GLU A 348 ? 0.1496 0.2291 0.2230 0.0101 -0.0456 -0.0563 356 GLU A N 5370 C CA . GLU A 348 ? 0.1544 0.2395 0.2193 0.0247 -0.0373 -0.0308 356 GLU A CA 5371 C C . GLU A 348 ? 0.1863 0.2182 0.1859 -0.0038 0.0049 -0.0413 356 GLU A C 5372 O O . GLU A 348 ? 0.1636 0.2308 0.1770 0.0181 -0.0047 -0.0522 356 GLU A O 5373 C CB . GLU A 348 ? 0.2219 0.3769 0.2255 0.0602 -0.0425 -0.0171 356 GLU A CB 5374 C CG . GLU A 348 ? 0.3112 0.5057 0.2432 0.0528 -0.0072 0.0047 356 GLU A CG 5375 C CD . GLU A 348 ? 0.3858 0.6108 0.2598 0.1128 0.0206 0.0208 356 GLU A CD 5376 O OE1 . GLU A 348 ? 0.4486 0.6822 0.2689 0.1076 0.0503 0.0234 356 GLU A OE1 5377 O OE2 . GLU A 348 ? 0.3864 0.6506 0.2660 0.1402 0.0282 0.0293 356 GLU A OE2 5384 N N . GLN A 349 ? 0.1672 0.2192 0.1635 0.0104 -0.0090 -0.0489 357 GLN A N 5385 C CA . GLN A 349 ? 0.1547 0.2072 0.1679 0.0166 -0.0033 -0.0236 357 GLN A CA 5386 C C . GLN A 349 ? 0.1605 0.2163 0.1602 0.0224 -0.0023 -0.0116 357 GLN A C 5387 O O . GLN A 349 ? 0.2322 0.2243 0.1589 0.0045 -0.0185 -0.0300 357 GLN A O 5388 C CB . GLN A 349 ? 0.1688 0.2273 0.1760 0.0088 -0.0122 -0.0416 357 GLN A CB 5389 C CG . GLN A 349 ? 0.1827 0.2494 0.1992 0.0523 0.0032 -0.0795 357 GLN A CG 5390 C CD . GLN A 349 ? 0.2253 0.2862 0.2325 0.0282 -0.0203 -0.0942 357 GLN A CD 5391 O OE1 . GLN A 349 ? 0.3030 0.2979 0.2362 0.0736 -0.0387 -0.0811 357 GLN A OE1 5392 N NE2 . GLN A 349 ? 0.2430 0.3759 0.2976 0.0276 0.0037 -0.1164 357 GLN A NE2 5401 N N . GLU A 350 ? 0.1220 0.2286 0.1590 0.0010 -0.0091 -0.0282 358 GLU A N 5402 C CA . GLU A 350 ? 0.1277 0.2058 0.1463 0.0021 0.0070 -0.0278 358 GLU A CA 5403 C C . GLU A 350 ? 0.1330 0.2159 0.1420 -0.0046 0.0273 -0.0279 358 GLU A C 5404 O O . GLU A 350 ? 0.1632 0.2669 0.1395 -0.0110 0.0168 0.0127 358 GLU A O 5405 C CB . GLU A 350 ? 0.1454 0.2011 0.1580 0.0150 -0.0090 -0.0120 358 GLU A CB 5406 C CG . GLU A 350 ? 0.1493 0.2088 0.1571 0.0126 -0.0031 -0.0054 358 GLU A CG 5407 C CD . GLU A 350 ? 0.1354 0.1971 0.1484 0.0146 0.0039 -0.0182 358 GLU A CD 5408 O OE1 . GLU A 350 ? 0.1440 0.2138 0.1342 0.0053 0.0002 0.0040 358 GLU A OE1 5409 O OE2 . GLU A 350 ? 0.1275 0.2104 0.1386 0.0063 0.0056 -0.0092 358 GLU A OE2 5416 N N . TYR A 351 ? 0.1383 0.2092 0.1371 0.0116 0.0138 0.0034 359 TYR A N 5417 C CA . TYR A 351 ? 0.1264 0.2038 0.1363 -0.0041 0.0174 -0.0180 359 TYR A CA 5418 C C . TYR A 351 ? 0.1184 0.2113 0.1388 -0.0157 0.0110 -0.0037 359 TYR A C 5419 O O . TYR A 351 ? 0.1355 0.1966 0.1549 -0.0092 0.0211 0.0047 359 TYR A O 5420 C CB . TYR A 351 ? 0.1548 0.2294 0.1442 -0.0094 0.0310 -0.0260 359 TYR A CB 5421 C CG . TYR A 351 ? 0.1303 0.2059 0.1493 0.0033 0.0279 -0.0105 359 TYR A CG 5422 C CD1 . TYR A 351 ? 0.1384 0.1751 0.1590 -0.0051 0.0209 -0.0150 359 TYR A CD1 5423 C CD2 . TYR A 351 ? 0.1520 0.2162 0.1773 0.0087 0.0194 -0.0238 359 TYR A CD2 5424 C CE1 . TYR A 351 ? 0.1239 0.1462 0.1663 0.0042 0.0189 -0.0276 359 TYR A CE1 5425 C CE2 . TYR A 351 ? 0.1618 0.1983 0.1730 0.0128 -0.0004 -0.0337 359 TYR A CE2 5426 C CZ . TYR A 351 ? 0.1374 0.2022 0.1718 -0.0102 -0.0001 -0.0257 359 TYR A CZ 5427 O OH . TYR A 351 ? 0.1458 0.2104 0.1828 0.0304 -0.0021 -0.0463 359 TYR A OH 5437 N N . ARG A 352 ? 0.1403 0.2131 0.1493 0.0192 0.0029 -0.0339 360 ARG A N 5438 C CA . ARG A 352 ? 0.1387 0.2023 0.1579 0.0156 0.0068 -0.0189 360 ARG A CA 5439 C C . ARG A 352 ? 0.1424 0.1837 0.1544 0.0070 0.0165 0.0010 360 ARG A C 5440 O O . ARG A 352 ? 0.1395 0.2179 0.1523 0.0059 0.0241 -0.0071 360 ARG A O 5441 C CB . ARG A 352 ? 0.1434 0.2206 0.1668 -0.0035 0.0067 -0.0265 360 ARG A CB 5442 C CG . ARG A 352 ? 0.1621 0.1881 0.1800 0.0011 0.0025 -0.0217 360 ARG A CG 5443 C CD . ARG A 352 ? 0.1968 0.1783 0.1861 0.0011 0.0255 -0.0284 360 ARG A CD 5444 N NE . ARG A 352 ? 0.2322 0.1858 0.2110 -0.0025 0.0196 -0.0572 360 ARG A NE 5445 C CZ . ARG A 352 ? 0.2119 0.1991 0.2221 -0.0142 0.0312 -0.0563 360 ARG A CZ 5446 N NH1 . ARG A 352 ? 0.2595 0.2075 0.2185 -0.0033 0.0389 -0.0453 360 ARG A NH1 5447 N NH2 . ARG A 352 ? 0.2509 0.1998 0.2570 -0.0109 0.0580 -0.0506 360 ARG A NH2 5461 N N . LEU A 353 ? 0.1392 0.1896 0.1504 0.0179 0.0220 -0.0021 361 LEU A N 5462 C CA A LEU A 353 ? 0.1328 0.2031 0.1668 -0.0042 0.0239 -0.0040 361 LEU A CA 5463 C CA B LEU A 353 ? 0.1458 0.2161 0.1645 0.0055 0.0180 -0.0052 361 LEU A CA 5464 C C . LEU A 353 ? 0.1453 0.2169 0.1622 0.0027 0.0068 -0.0077 361 LEU A C 5465 O O . LEU A 353 ? 0.1277 0.2245 0.1728 0.0162 0.0286 -0.0076 361 LEU A O 5466 C CB A LEU A 353 ? 0.1606 0.2114 0.1609 -0.0160 0.0107 -0.0199 361 LEU A CB 5467 C CB B LEU A 353 ? 0.1608 0.2468 0.1706 0.0008 0.0160 -0.0093 361 LEU A CB 5468 C CG A LEU A 353 ? 0.1518 0.2846 0.1652 -0.0159 0.0038 -0.0029 361 LEU A CG 5469 C CG B LEU A 353 ? 0.1650 0.2763 0.1816 -0.0010 0.0178 -0.0001 361 LEU A CG 5470 C CD1 A LEU A 353 ? 0.2024 0.3469 0.1982 -0.0461 0.0081 -0.0784 361 LEU A CD1 5471 C CD1 B LEU A 353 ? 0.1946 0.3121 0.1981 -0.0130 0.0360 -0.0122 361 LEU A CD1 5472 C CD2 A LEU A 353 ? 0.1856 0.3597 0.2203 0.0071 0.0175 -0.0313 361 LEU A CD2 5473 C CD2 B LEU A 353 ? 0.1371 0.2465 0.1677 -0.0258 0.0077 0.0345 361 LEU A CD2 5494 N N . THR A 354 ? 0.1377 0.2198 0.1646 0.0135 0.0183 -0.0253 362 THR A N 5495 C CA . THR A 354 ? 0.1555 0.2348 0.1890 0.0132 0.0536 -0.0157 362 THR A CA 5496 C C . THR A 354 ? 0.1490 0.2358 0.1865 0.0170 0.0445 -0.0347 362 THR A C 5497 O O . THR A 354 ? 0.1569 0.2647 0.2021 0.0261 0.0401 0.0089 362 THR A O 5498 C CB . THR A 354 ? 0.1590 0.2323 0.2022 0.0289 0.0303 -0.0006 362 THR A CB 5499 O OG1 . THR A 354 ? 0.1814 0.2337 0.2042 0.0338 0.0356 -0.0161 362 THR A OG1 5500 C CG2 . THR A 354 ? 0.1790 0.2395 0.2061 0.0340 0.0399 -0.0144 362 THR A CG2 5508 N N . GLU A 355 ? 0.1699 0.2543 0.1725 0.0251 0.0324 -0.0311 363 GLU A N 5509 C CA . GLU A 355 ? 0.1743 0.2938 0.1817 0.0044 0.0288 -0.0108 363 GLU A CA 5510 C C . GLU A 355 ? 0.1430 0.2521 0.1796 -0.0121 0.0080 0.0032 363 GLU A C 5511 O O . GLU A 355 ? 0.1872 0.3047 0.2028 -0.0074 0.0451 0.0204 363 GLU A O 5512 C CB . GLU A 355 ? 0.2200 0.3050 0.2053 0.0074 0.0232 -0.0071 363 GLU A CB 5513 C CG . GLU A 355 ? 0.2983 0.3495 0.2479 0.0212 0.0328 -0.0104 363 GLU A CG 5514 C CD . GLU A 355 ? 0.3640 0.3726 0.2776 -0.0003 0.0086 -0.0520 363 GLU A CD 5515 O OE1 . GLU A 355 ? 0.3339 0.4123 0.2626 -0.0097 -0.0114 -0.0943 363 GLU A OE1 5516 O OE2 . GLU A 355 ? 0.4337 0.4196 0.3099 -0.0381 0.0231 -0.0527 363 GLU A OE2 5523 N N . ALA A 356 ? 0.1553 0.2393 0.1806 0.0144 0.0143 -0.0079 364 ALA A N 5524 C CA . ALA A 356 ? 0.1266 0.2642 0.2035 0.0216 0.0264 0.0079 364 ALA A CA 5525 C C . ALA A 356 ? 0.1243 0.2679 0.1894 0.0047 0.0182 0.0153 364 ALA A C 5526 O O . ALA A 356 ? 0.1374 0.3113 0.1964 -0.0108 0.0227 0.0285 364 ALA A O 5527 C CB . ALA A 356 ? 0.1283 0.2586 0.1996 0.0311 0.0323 0.0128 364 ALA A CB 5533 N N . TYR A 357 ? 0.1316 0.2481 0.1858 0.0152 0.0174 0.0100 365 TYR A N 5534 C CA . TYR A 357 ? 0.1470 0.2289 0.1935 0.0308 0.0283 -0.0086 365 TYR A CA 5535 C C . TYR A 357 ? 0.1511 0.2653 0.2007 0.0153 0.0165 -0.0089 365 TYR A C 5536 O O . TYR A 357 ? 0.1540 0.2659 0.2170 -0.0041 0.0166 -0.0184 365 TYR A O 5537 C CB . TYR A 357 ? 0.1484 0.2403 0.1927 0.0167 0.0385 -0.0105 365 TYR A CB 5538 C CG . TYR A 357 ? 0.1482 0.2263 0.2016 0.0090 0.0084 -0.0076 365 TYR A CG 5539 C CD1 . TYR A 357 ? 0.1844 0.2078 0.2294 0.0164 0.0629 -0.0002 365 TYR A CD1 5540 C CD2 . TYR A 357 ? 0.1631 0.2169 0.2158 0.0114 0.0456 -0.0107 365 TYR A CD2 5541 C CE1 . TYR A 357 ? 0.2064 0.2014 0.2365 0.0060 0.0827 -0.0040 365 TYR A CE1 5542 C CE2 . TYR A 357 ? 0.1820 0.1993 0.2154 -0.0199 0.0590 -0.0225 365 TYR A CE2 5543 C CZ . TYR A 357 ? 0.1870 0.1861 0.2237 -0.0078 0.0572 -0.0296 365 TYR A CZ 5544 O OH . TYR A 357 ? 0.2262 0.1858 0.2574 0.0074 0.0717 0.0025 365 TYR A OH 5554 N N . GLN A 358 ? 0.1411 0.2722 0.1935 0.0114 0.0399 -0.0150 366 GLN A N 5555 C CA . GLN A 358 ? 0.1564 0.2843 0.1899 0.0276 0.0385 -0.0178 366 GLN A CA 5556 C C . GLN A 358 ? 0.1428 0.3040 0.2042 0.0242 0.0413 -0.0065 366 GLN A C 5557 O O . GLN A 358 ? 0.1555 0.3351 0.2202 0.0171 0.0581 -0.0025 366 GLN A O 5558 C CB . GLN A 358 ? 0.1999 0.3260 0.2123 0.0632 0.0329 0.0103 366 GLN A CB 5559 C CG . GLN A 358 ? 0.2672 0.3529 0.2355 0.0585 0.0532 0.0034 366 GLN A CG 5560 C CD . GLN A 358 ? 0.2607 0.4322 0.2603 0.0703 0.0565 -0.0262 366 GLN A CD 5561 O OE1 . GLN A 358 ? 0.3035 0.5124 0.3006 0.0732 0.0801 -0.0714 366 GLN A OE1 5562 N NE2 . GLN A 358 ? 0.2595 0.4516 0.2659 0.0329 0.0425 -0.0219 366 GLN A NE2 5571 N N . VAL A 359 ? 0.1461 0.3003 0.1995 0.0281 0.0353 -0.0057 367 VAL A N 5572 C CA . VAL A 359 ? 0.1445 0.2842 0.1859 0.0604 0.0197 0.0017 367 VAL A CA 5573 C C . VAL A 359 ? 0.1619 0.2707 0.2170 0.0639 0.0383 -0.0115 367 VAL A C 5574 O O . VAL A 359 ? 0.1603 0.2764 0.2243 0.0478 0.0268 -0.0261 367 VAL A O 5575 C CB . VAL A 359 ? 0.1692 0.2826 0.1922 0.0385 0.0178 -0.0254 367 VAL A CB 5576 C CG1 . VAL A 359 ? 0.1939 0.2986 0.1897 -0.0025 0.0166 -0.0226 367 VAL A CG1 5577 C CG2 . VAL A 359 ? 0.1580 0.2612 0.2122 0.0274 0.0249 -0.0213 367 VAL A CG2 5587 N N . PRO A 360 ? 0.1746 0.2666 0.2285 0.0666 0.0413 -0.0222 368 PRO A N 5588 C CA . PRO A 360 ? 0.1667 0.2431 0.2337 0.0566 0.0251 -0.0474 368 PRO A CA 5589 C C . PRO A 360 ? 0.1621 0.2476 0.2389 0.0455 0.0055 -0.0427 368 PRO A C 5590 O O . PRO A 360 ? 0.2144 0.2649 0.2485 0.0214 0.0132 -0.0627 368 PRO A O 5591 C CB . PRO A 360 ? 0.2072 0.2660 0.2526 0.0675 0.0398 -0.0287 368 PRO A CB 5592 C CG . PRO A 360 ? 0.1894 0.2765 0.2492 0.0596 0.0114 -0.0251 368 PRO A CG 5593 C CD . PRO A 360 ? 0.1472 0.2770 0.2308 0.0623 0.0140 -0.0347 368 PRO A CD 5601 N N . ASP A 361 ? 0.1414 0.2497 0.2296 0.0569 0.0135 -0.0223 369 ASP A N 5602 C CA . ASP A 361 ? 0.1604 0.2065 0.2154 0.0214 0.0070 -0.0181 369 ASP A CA 5603 C C . ASP A 361 ? 0.1402 0.1862 0.2080 0.0279 0.0045 -0.0202 369 ASP A C 5604 O O . ASP A 361 ? 0.1541 0.2139 0.2076 0.0184 0.0049 -0.0166 369 ASP A O 5605 C CB . ASP A 361 ? 0.1886 0.2207 0.2243 0.0393 -0.0004 -0.0446 369 ASP A CB 5606 C CG . ASP A 361 ? 0.1951 0.2440 0.2584 0.0759 -0.0042 -0.0297 369 ASP A CG 5607 O OD1 . ASP A 361 ? 0.1533 0.2420 0.2462 0.0458 0.0160 -0.0498 369 ASP A OD1 5608 O OD2 . ASP A 361 ? 0.2302 0.2766 0.3117 0.0714 -0.0235 -0.0375 369 ASP A OD2 5613 N N . ALA A 362 ? 0.1504 0.1985 0.2136 0.0189 0.0299 -0.0310 370 ALA A N 5614 C CA . ALA A 362 ? 0.1491 0.1815 0.2067 0.0311 -0.0021 -0.0146 370 ALA A CA 5615 C C . ALA A 362 ? 0.1573 0.1961 0.1988 0.0480 0.0153 -0.0226 370 ALA A C 5616 O O . ALA A 362 ? 0.1711 0.2352 0.1989 0.0465 0.0209 -0.0442 370 ALA A O 5617 C CB . ALA A 362 ? 0.1409 0.2153 0.2153 0.0227 0.0256 -0.0182 370 ALA A CB 5623 N N . SER A 363 ? 0.1625 0.1911 0.2067 0.0237 0.0056 -0.0301 371 SER A N 5624 C CA . SER A 363 ? 0.1599 0.1848 0.2209 0.0235 -0.0103 -0.0108 371 SER A CA 5625 C C . SER A 363 ? 0.1702 0.1908 0.1998 0.0269 0.0196 -0.0050 371 SER A C 5626 O O . SER A 363 ? 0.1582 0.2022 0.1840 0.0024 0.0187 -0.0100 371 SER A O 5627 C CB . SER A 363 ? 0.1604 0.2106 0.2248 0.0227 -0.0045 -0.0166 371 SER A CB 5628 O OG . SER A 363 ? 0.1688 0.2235 0.2350 0.0463 0.0029 -0.0065 371 SER A OG 5634 N N . VAL A 364 ? 0.1810 0.2045 0.1943 0.0160 0.0105 0.0027 372 VAL A N 5635 C CA . VAL A 364 ? 0.2047 0.2178 0.1977 -0.0179 0.0040 -0.0043 372 VAL A CA 5636 C C . VAL A 364 ? 0.1701 0.2074 0.1944 0.0189 -0.0070 0.0086 372 VAL A C 5637 O O . VAL A 364 ? 0.1857 0.2059 0.2013 0.0194 -0.0054 -0.0076 372 VAL A O 5638 C CB . VAL A 364 ? 0.2233 0.2690 0.2115 -0.0382 0.0092 0.0097 372 VAL A CB 5639 C CG1 . VAL A 364 ? 0.3125 0.3422 0.2185 -0.1279 -0.0261 0.0195 372 VAL A CG1 5640 C CG2 . VAL A 364 ? 0.2476 0.2650 0.2299 -0.0188 0.0052 0.0146 372 VAL A CG2 5650 N N . SER A 365 ? 0.1624 0.2215 0.2048 0.0137 -0.0040 -0.0078 373 SER A N 5651 C CA A SER A 365 ? 0.1577 0.2236 0.2139 0.0219 0.0096 -0.0165 373 SER A CA 5652 C CA B SER A 365 ? 0.1641 0.2277 0.2127 0.0236 0.0050 -0.0114 373 SER A CA 5653 C CA C SER A 365 ? 0.1602 0.2303 0.2026 0.0196 -0.0047 -0.0102 373 SER A CA 5654 C C . SER A 365 ? 0.1374 0.2443 0.2096 0.0219 0.0100 -0.0060 373 SER A C 5655 O O . SER A 365 ? 0.1587 0.2608 0.2195 -0.0040 0.0103 -0.0031 373 SER A O 5656 C CB A SER A 365 ? 0.1827 0.2825 0.2324 0.0482 0.0259 -0.0037 373 SER A CB 5657 C CB B SER A 365 ? 0.2010 0.2842 0.2286 0.0491 0.0114 0.0034 373 SER A CB 5658 C CB C SER A 365 ? 0.1789 0.2592 0.1927 0.0288 -0.0212 -0.0056 373 SER A CB 5659 O OG A SER A 365 ? 0.2027 0.2820 0.2383 0.0449 0.0278 -0.0117 373 SER A OG 5660 O OG B SER A 365 ? 0.2517 0.3058 0.2352 0.0648 0.0162 0.0088 373 SER A OG 5661 O OG C SER A 365 ? 0.1854 0.2562 0.1736 0.0226 -0.0516 -0.0087 373 SER A OG 5673 N N . SER A 366 ? 0.1319 0.2112 0.1852 0.0125 0.0075 -0.0008 374 SER A N 5674 C CA . SER A 366 ? 0.1612 0.2186 0.1944 0.0168 0.0286 -0.0231 374 SER A CA 5675 C C . SER A 366 ? 0.1491 0.2063 0.1920 0.0224 0.0235 -0.0089 374 SER A C 5676 O O . SER A 366 ? 0.1619 0.2144 0.1940 0.0058 0.0351 -0.0112 374 SER A O 5677 C CB . SER A 366 ? 0.1724 0.1898 0.2104 0.0253 0.0108 -0.0152 374 SER A CB 5678 O OG . SER A 366 ? 0.1942 0.2118 0.2125 0.0345 0.0116 -0.0323 374 SER A OG 5684 N N . MET A 367 ? 0.1380 0.2123 0.1700 0.0262 0.0123 -0.0175 375 MET A N 5685 C CA . MET A 367 ? 0.1339 0.1920 0.1605 0.0146 0.0251 -0.0204 375 MET A CA 5686 C C . MET A 367 ? 0.1548 0.2005 0.1808 -0.0026 0.0072 -0.0114 375 MET A C 5687 O O . MET A 367 ? 0.1303 0.2192 0.1800 0.0129 0.0149 0.0052 375 MET A O 5688 C CB . MET A 367 ? 0.1249 0.2108 0.1618 0.0107 -0.0028 -0.0157 375 MET A CB 5689 C CG . MET A 367 ? 0.1574 0.1914 0.1650 0.0117 -0.0070 -0.0243 375 MET A CG 5690 S SD . MET A 367 ? 0.1727 0.2080 0.1993 -0.0034 -0.0123 -0.0289 375 MET A SD 5691 C CE . MET A 367 ? 0.1801 0.2366 0.2158 -0.0099 -0.0445 -0.0176 375 MET A CE 5701 N N . HIS A 368 ? 0.1287 0.2282 0.1847 0.0087 0.0000 0.0064 376 HIS A N 5702 C CA . HIS A 368 ? 0.1408 0.2266 0.1961 0.0017 -0.0024 -0.0015 376 HIS A CA 5703 C C . HIS A 368 ? 0.1142 0.2099 0.2078 -0.0020 -0.0083 0.0075 376 HIS A C 5704 O O . HIS A 368 ? 0.1284 0.2347 0.2034 -0.0080 0.0089 0.0107 376 HIS A O 5705 C CB . HIS A 368 ? 0.1702 0.2174 0.2103 0.0049 0.0060 0.0002 376 HIS A CB 5706 C CG . HIS A 368 ? 0.1679 0.2953 0.2468 0.0186 -0.0170 -0.0025 376 HIS A CG 5707 N ND1 . HIS A 368 ? 0.2039 0.3383 0.2786 -0.0151 0.0131 0.0092 376 HIS A ND1 5708 C CD2 . HIS A 368 ? 0.1845 0.3579 0.3035 -0.0235 0.0190 -0.0416 376 HIS A CD2 5709 C CE1 . HIS A 368 ? 0.1753 0.3299 0.3025 -0.0586 0.0199 -0.0294 376 HIS A CE1 5710 N NE2 . HIS A 368 ? 0.2480 0.3914 0.3427 -0.0376 0.0326 -0.0096 376 HIS A NE2 5718 N N . THR A 369 ? 0.1407 0.2241 0.2041 0.0097 0.0149 -0.0077 377 THR A N 5719 C CA . THR A 369 ? 0.1558 0.2612 0.2066 -0.0014 0.0155 -0.0105 377 THR A CA 5720 C C . THR A 369 ? 0.1448 0.2551 0.1835 -0.0053 0.0184 -0.0011 377 THR A C 5721 O O . THR A 369 ? 0.1779 0.2532 0.1810 0.0013 0.0236 0.0029 377 THR A O 5722 C CB . THR A 369 ? 0.1960 0.2720 0.2188 0.0335 0.0311 0.0065 377 THR A CB 5723 O OG1 . THR A 369 ? 0.2103 0.3077 0.2538 0.0332 0.0715 -0.0001 377 THR A OG1 5724 C CG2 . THR A 369 ? 0.2801 0.2696 0.2045 0.0290 0.0488 -0.0049 377 THR A CG2 5732 N N . ALA A 370 ? 0.1367 0.2563 0.1832 -0.0075 0.0099 -0.0171 378 ALA A N 5733 C CA . ALA A 370 ? 0.1392 0.2402 0.1818 -0.0229 0.0050 -0.0075 378 ALA A CA 5734 C C . ALA A 370 ? 0.1181 0.2249 0.1752 0.0007 0.0110 0.0089 378 ALA A C 5735 O O . ALA A 370 ? 0.1324 0.2213 0.1835 -0.0126 0.0060 0.0230 378 ALA A O 5736 C CB . ALA A 370 ? 0.1531 0.2255 0.1708 -0.0238 -0.0065 -0.0130 378 ALA A CB 5742 N N . LEU A 371 ? 0.1254 0.2209 0.1759 -0.0075 0.0067 -0.0050 379 LEU A N 5743 C CA . LEU A 371 ? 0.1283 0.2173 0.1760 -0.0095 0.0096 0.0115 379 LEU A CA 5744 C C . LEU A 371 ? 0.1152 0.2396 0.1799 0.0022 0.0018 -0.0105 379 LEU A C 5745 O O . LEU A 371 ? 0.1271 0.2281 0.1949 -0.0181 0.0043 0.0203 379 LEU A O 5746 C CB . LEU A 371 ? 0.1428 0.2145 0.1626 -0.0308 0.0114 0.0086 379 LEU A CB 5747 C CG . LEU A 371 ? 0.1820 0.2532 0.1656 -0.0226 0.0099 0.0393 379 LEU A CG 5748 C CD1 . LEU A 371 ? 0.2325 0.3315 0.2207 -0.0108 0.0134 0.0432 379 LEU A CD1 5749 C CD2 . LEU A 371 ? 0.1962 0.2272 0.1976 0.0009 0.0417 0.0170 379 LEU A CD2 5761 N N . THR A 372 ? 0.1202 0.2269 0.2029 -0.0058 0.0172 0.0069 380 THR A N 5762 C CA A THR A 372 ? 0.1143 0.2694 0.2004 -0.0056 0.0204 0.0086 380 THR A CA 5763 C CA B THR A 372 ? 0.1207 0.2600 0.2030 -0.0002 0.0132 0.0081 380 THR A CA 5764 C C . THR A 372 ? 0.1085 0.2630 0.1897 -0.0215 0.0183 0.0192 380 THR A C 5765 O O . THR A 372 ? 0.1329 0.3016 0.2107 -0.0297 0.0180 0.0169 380 THR A O 5766 C CB A THR A 372 ? 0.1340 0.3189 0.2201 -0.0089 0.0280 0.0253 380 THR A CB 5767 C CB B THR A 372 ? 0.1642 0.2939 0.2298 0.0063 0.0066 0.0297 380 THR A CB 5768 O OG1 A THR A 372 ? 0.1376 0.3461 0.2129 0.0162 0.0194 0.0446 380 THR A OG1 5769 O OG1 B THR A 372 ? 0.1764 0.2996 0.2479 -0.0047 0.0041 0.0184 380 THR A OG1 5770 C CG2 A THR A 372 ? 0.1337 0.3216 0.2443 -0.0322 0.0624 0.0159 380 THR A CG2 5771 C CG2 B THR A 372 ? 0.1682 0.2926 0.2281 0.0214 0.0033 0.0412 380 THR A CG2 5784 N N . ARG A 373 ? 0.1185 0.2744 0.1959 -0.0077 0.0203 0.0037 381 ARG A N 5785 C CA . ARG A 373 ? 0.1361 0.2685 0.1907 -0.0123 0.0032 -0.0046 381 ARG A CA 5786 C C . ARG A 373 ? 0.1125 0.2582 0.1761 -0.0316 0.0133 0.0070 381 ARG A C 5787 O O . ARG A 373 ? 0.1481 0.2835 0.1797 -0.0234 0.0191 0.0229 381 ARG A O 5788 C CB . ARG A 373 ? 0.1809 0.2886 0.1897 0.0163 0.0192 -0.0113 381 ARG A CB 5789 C CG . ARG A 373 ? 0.2119 0.3289 0.1941 0.0449 0.0092 -0.0154 381 ARG A CG 5790 C CD . ARG A 373 ? 0.2727 0.3891 0.2202 0.0110 0.0588 -0.0461 381 ARG A CD 5791 N NE . ARG A 373 ? 0.2898 0.4122 0.2443 -0.0127 0.0568 -0.0453 381 ARG A NE 5792 C CZ . ARG A 373 ? 0.2885 0.4108 0.2548 -0.0140 0.0598 -0.0509 381 ARG A CZ 5793 N NH1 . ARG A 373 ? 0.3011 0.4472 0.2564 -0.0267 0.0580 -0.0436 381 ARG A NH1 5794 N NH2 . ARG A 373 ? 0.2811 0.4522 0.2703 0.0019 0.0696 -0.0683 381 ARG A NH2 5808 N N . ILE A 374 ? 0.0996 0.2711 0.1613 -0.0056 0.0239 0.0159 382 ILE A N 5809 C CA . ILE A 374 ? 0.1232 0.2209 0.1728 -0.0130 0.0151 0.0027 382 ILE A CA 5810 C C . ILE A 374 ? 0.1216 0.2410 0.2051 -0.0114 0.0059 0.0482 382 ILE A C 5811 O O . ILE A 374 ? 0.1505 0.2300 0.2107 -0.0142 -0.0076 0.0334 382 ILE A O 5812 C CB . ILE A 374 ? 0.1294 0.2255 0.1806 -0.0113 0.0176 0.0121 382 ILE A CB 5813 C CG1 . ILE A 374 ? 0.1185 0.2214 0.1874 -0.0098 0.0066 0.0152 382 ILE A CG1 5814 C CG2 . ILE A 374 ? 0.1468 0.2310 0.1756 -0.0253 0.0124 0.0259 382 ILE A CG2 5815 C CD1 . ILE A 374 ? 0.1172 0.2573 0.1767 -0.0095 0.0156 0.0275 382 ILE A CD1 5827 N N . ALA A 375 ? 0.1346 0.2303 0.2091 -0.0094 -0.0100 0.0322 383 ALA A N 5828 C CA . ALA A 375 ? 0.1590 0.2476 0.2122 -0.0417 -0.0107 0.0136 383 ALA A CA 5829 C C . ALA A 375 ? 0.1894 0.2568 0.2306 -0.0769 0.0049 -0.0007 383 ALA A C 5830 O O . ALA A 375 ? 0.2545 0.2915 0.2710 -0.0735 0.0534 0.0145 383 ALA A O 5831 C CB . ALA A 375 ? 0.1591 0.2540 0.2364 -0.0477 -0.0023 0.0106 383 ALA A CB 5837 N N . SER A 376 ? 0.1627 0.2913 0.2069 -0.0586 -0.0159 0.0156 384 SER A N 5838 C CA . SER A 376 ? 0.1620 0.3385 0.2280 -0.0645 0.0314 0.0239 384 SER A CA 5839 C C . SER A 376 ? 0.1765 0.3792 0.2288 -0.0980 0.0087 0.0310 384 SER A C 5840 O O . SER A 376 ? 0.2209 0.4600 0.2356 -0.1285 0.0018 0.0645 384 SER A O 5841 C CB . SER A 376 ? 0.2000 0.3387 0.2491 -0.0962 0.0340 0.0213 384 SER A CB 5842 O OG . SER A 376 ? 0.2033 0.3702 0.2681 -0.0479 0.0068 0.0211 384 SER A OG 5848 N N . GLU A 377 ? 0.1480 0.3252 0.2170 -0.0420 0.0080 0.0231 385 GLU A N 5849 C CA . GLU A 377 ? 0.1489 0.3417 0.2030 -0.0539 0.0128 0.0189 385 GLU A CA 5850 C C . GLU A 377 ? 0.1423 0.3434 0.2104 -0.0600 0.0162 0.0429 385 GLU A C 5851 O O . GLU A 377 ? 0.1449 0.3553 0.1962 -0.0702 0.0162 0.0552 385 GLU A O 5852 C CB . GLU A 377 ? 0.1684 0.3788 0.1932 -0.0137 0.0026 -0.0015 385 GLU A CB 5853 C CG . GLU A 377 ? 0.1778 0.4000 0.2174 -0.0089 0.0358 -0.0305 385 GLU A CG 5854 C CD . GLU A 377 ? 0.2852 0.4326 0.2623 0.0081 0.0084 -0.0491 385 GLU A CD 5855 O OE1 . GLU A 377 ? 0.3167 0.4834 0.3125 0.0022 -0.0094 -0.0454 385 GLU A OE1 5856 O OE2 . GLU A 377 ? 0.4112 0.4565 0.3009 0.0061 0.0195 -0.0359 385 GLU A OE2 5863 N N . PRO A 378 ? 0.1354 0.3542 0.2345 -0.0488 -0.0032 0.0858 386 PRO A N 5864 C CA . PRO A 378 ? 0.1789 0.3260 0.2360 -0.0447 0.0174 0.0885 386 PRO A CA 5865 C C . PRO A 378 ? 0.1459 0.3089 0.1908 -0.0873 0.0129 0.0662 386 PRO A C 5866 O O . PRO A 378 ? 0.1455 0.3448 0.2056 -0.0516 0.0181 0.0839 386 PRO A O 5867 C CB . PRO A 378 ? 0.2102 0.3366 0.2853 -0.0622 0.0199 0.0934 386 PRO A CB 5868 C CG . PRO A 378 ? 0.2283 0.3776 0.3153 -0.0563 0.0709 0.0859 386 PRO A CG 5869 C CD . PRO A 378 ? 0.1682 0.3649 0.2737 -0.0288 0.0274 0.0874 386 PRO A CD 5877 N N . HIS A 379 ? 0.1786 0.3479 0.1752 -0.0645 -0.0122 0.0482 387 HIS A N 5878 C CA . HIS A 379 ? 0.1813 0.3604 0.1719 -0.0376 0.0121 0.0246 387 HIS A CA 5879 C C . HIS A 379 ? 0.1455 0.3148 0.1628 -0.0278 0.0309 0.0349 387 HIS A C 5880 O O . HIS A 379 ? 0.1489 0.3296 0.1643 -0.0383 0.0199 0.0241 387 HIS A O 5881 C CB . HIS A 379 ? 0.2846 0.4059 0.2106 -0.0525 0.0442 0.0191 387 HIS A CB 5882 C CG . HIS A 379 ? 0.3868 0.4389 0.2741 -0.0654 0.0533 0.0158 387 HIS A CG 5883 N ND1 . HIS A 379 ? 0.4537 0.4756 0.3117 -0.0343 0.0987 0.0247 387 HIS A ND1 5884 C CD2 . HIS A 379 ? 0.4377 0.4691 0.3102 -0.0229 0.0706 0.0109 387 HIS A CD2 5885 C CE1 . HIS A 379 ? 0.4615 0.4706 0.3286 -0.0196 0.1079 0.0242 387 HIS A CE1 5886 N NE2 . HIS A 379 ? 0.4669 0.4771 0.3318 -0.0149 0.0890 0.0200 387 HIS A NE2 5894 N N . ILE A 380 ? 0.1339 0.2971 0.1503 -0.0106 0.0171 0.0233 388 ILE A N 5895 C CA . ILE A 380 ? 0.1271 0.2711 0.1605 0.0024 0.0022 0.0228 388 ILE A CA 5896 C C . ILE A 380 ? 0.1420 0.2503 0.1661 -0.0339 0.0103 0.0104 388 ILE A C 5897 O O . ILE A 380 ? 0.1274 0.2332 0.1788 -0.0229 0.0099 0.0078 388 ILE A O 5898 C CB . ILE A 380 ? 0.1445 0.2710 0.1829 -0.0091 0.0134 0.0140 388 ILE A CB 5899 C CG1 . ILE A 380 ? 0.1564 0.2863 0.1930 0.0002 0.0128 -0.0305 388 ILE A CG1 5900 C CG2 . ILE A 380 ? 0.1619 0.2296 0.1859 -0.0175 0.0139 0.0098 388 ILE A CG2 5901 C CD1 . ILE A 380 ? 0.1968 0.3229 0.2031 0.0220 0.0100 -0.0637 388 ILE A CD1 5913 N N . LEU A 381 ? 0.1202 0.2578 0.1651 -0.0147 0.0161 0.0171 389 LEU A N 5914 C CA . LEU A 381 ? 0.1383 0.2195 0.1768 -0.0109 0.0201 0.0180 389 LEU A CA 5915 C C . LEU A 381 ? 0.1178 0.2168 0.1762 -0.0119 0.0278 0.0092 389 LEU A C 5916 O O . LEU A 381 ? 0.1105 0.2193 0.1728 -0.0142 0.0137 0.0084 389 LEU A O 5917 C CB . LEU A 381 ? 0.1501 0.2243 0.1941 -0.0230 -0.0060 0.0318 389 LEU A CB 5918 C CG . LEU A 381 ? 0.1624 0.2305 0.2116 -0.0491 -0.0312 0.0256 389 LEU A CG 5919 C CD1 . LEU A 381 ? 0.1883 0.2611 0.2155 -0.0263 -0.0327 0.0196 389 LEU A CD1 5920 C CD2 . LEU A 381 ? 0.1873 0.2634 0.2292 -0.0541 -0.0252 0.0285 389 LEU A CD2 5932 N N . GLN A 382 ? 0.1459 0.2210 0.1719 -0.0246 0.0042 0.0155 390 GLN A N 5933 C CA . GLN A 382 ? 0.1389 0.2365 0.1702 -0.0150 0.0084 0.0386 390 GLN A CA 5934 C C . GLN A 382 ? 0.1070 0.2167 0.1400 0.0000 0.0334 0.0230 390 GLN A C 5935 O O . GLN A 382 ? 0.1169 0.2075 0.1497 -0.0052 0.0248 0.0231 390 GLN A O 5936 C CB . GLN A 382 ? 0.1653 0.2641 0.1843 -0.0513 0.0096 0.0569 390 GLN A CB 5937 C CG . GLN A 382 ? 0.1635 0.2661 0.1941 -0.0343 0.0054 0.0451 390 GLN A CG 5938 C CD . GLN A 382 ? 0.1717 0.2573 0.2156 -0.0246 -0.0165 0.0491 390 GLN A CD 5939 O OE1 . GLN A 382 ? 0.2042 0.2575 0.2481 -0.0175 -0.0122 0.0370 390 GLN A OE1 5940 N NE2 . GLN A 382 ? 0.1559 0.2491 0.2265 -0.0247 0.0013 0.0367 390 GLN A NE2 5949 N N . ARG A 383 ? 0.1299 0.2151 0.1446 0.0018 0.0164 0.0041 391 ARG A N 5950 C CA . ARG A 383 ? 0.1100 0.2440 0.1554 0.0053 0.0272 0.0098 391 ARG A CA 5951 C C . ARG A 383 ? 0.1066 0.1843 0.1566 -0.0053 0.0466 0.0156 391 ARG A C 5952 O O . ARG A 383 ? 0.1275 0.1959 0.1548 0.0070 0.0198 0.0157 391 ARG A O 5953 C CB . ARG A 383 ? 0.1443 0.2353 0.1316 -0.0046 0.0060 0.0029 391 ARG A CB 5954 C CG . ARG A 383 ? 0.1494 0.2621 0.1496 -0.0106 -0.0102 -0.0040 391 ARG A CG 5955 C CD . ARG A 383 ? 0.1523 0.2922 0.1347 0.0097 -0.0064 0.0027 391 ARG A CD 5956 N NE . ARG A 383 ? 0.1512 0.2880 0.1459 0.0071 -0.0055 0.0037 391 ARG A NE 5957 C CZ . ARG A 383 ? 0.1475 0.3187 0.1457 0.0075 -0.0040 -0.0013 391 ARG A CZ 5958 N NH1 . ARG A 383 ? 0.1390 0.3379 0.1816 0.0341 0.0074 -0.0140 391 ARG A NH1 5959 N NH2 . ARG A 383 ? 0.2033 0.3661 0.1451 0.0258 -0.0019 0.0002 391 ARG A NH2 5973 N N . TYR A 384 ? 0.1121 0.2049 0.1477 -0.0090 0.0026 0.0174 392 TYR A N 5974 C CA . TYR A 384 ? 0.1018 0.1943 0.1622 0.0033 0.0265 0.0162 392 TYR A CA 5975 C C . TYR A 384 ? 0.0960 0.1924 0.1491 -0.0229 0.0092 0.0180 392 TYR A C 5976 O O . TYR A 384 ? 0.1064 0.1962 0.1534 -0.0084 0.0073 0.0124 392 TYR A O 5977 C CB . TYR A 384 ? 0.1034 0.1951 0.1588 -0.0176 0.0168 0.0169 392 TYR A CB 5978 C CG . TYR A 384 ? 0.1044 0.1952 0.1540 -0.0179 0.0017 0.0120 392 TYR A CG 5979 C CD1 . TYR A 384 ? 0.0996 0.2211 0.1513 -0.0117 -0.0081 0.0187 392 TYR A CD1 5980 C CD2 . TYR A 384 ? 0.1163 0.1854 0.1538 -0.0213 -0.0027 0.0197 392 TYR A CD2 5981 C CE1 . TYR A 384 ? 0.1083 0.1921 0.1540 -0.0073 -0.0055 0.0036 392 TYR A CE1 5982 C CE2 . TYR A 384 ? 0.1282 0.2016 0.1556 -0.0183 0.0040 -0.0129 392 TYR A CE2 5983 C CZ . TYR A 384 ? 0.1260 0.1998 0.1496 -0.0063 0.0071 0.0050 392 TYR A CZ 5984 O OH . TYR A 384 ? 0.1467 0.1939 0.1539 -0.0093 0.0017 0.0049 392 TYR A OH 5994 N N . TYR A 385 ? 0.1269 0.2018 0.1472 -0.0213 0.0083 0.0150 393 TYR A N 5995 C CA . TYR A 385 ? 0.1134 0.1903 0.1562 -0.0144 0.0262 0.0169 393 TYR A CA 5996 C C . TYR A 385 ? 0.1106 0.1986 0.1630 -0.0181 0.0194 0.0289 393 TYR A C 5997 O O . TYR A 385 ? 0.1190 0.1959 0.1611 -0.0121 0.0038 0.0236 393 TYR A O 5998 C CB . TYR A 385 ? 0.1153 0.2020 0.1649 -0.0219 0.0043 0.0249 393 TYR A CB 5999 C CG . TYR A 385 ? 0.1403 0.2087 0.1923 -0.0093 0.0010 0.0240 393 TYR A CG 6000 C CD1 . TYR A 385 ? 0.1745 0.2059 0.2125 0.0294 -0.0058 0.0161 393 TYR A CD1 6001 C CD2 . TYR A 385 ? 0.1669 0.2517 0.2193 0.0283 -0.0055 0.0641 393 TYR A CD2 6002 C CE1 . TYR A 385 ? 0.2123 0.2383 0.2558 -0.0097 0.0229 -0.0164 393 TYR A CE1 6003 C CE2 . TYR A 385 ? 0.2257 0.2667 0.2689 0.0505 0.0367 0.0707 393 TYR A CE2 6004 C CZ . TYR A 385 ? 0.2310 0.2659 0.3063 0.0504 0.0550 0.0237 393 TYR A CZ 6005 O OH . TYR A 385 ? 0.3235 0.3106 0.3691 0.1029 0.0735 0.0032 393 TYR A OH 6015 N N . VAL A 386 ? 0.0967 0.2154 0.1562 -0.0137 0.0139 0.0148 394 VAL A N 6016 C CA . VAL A 386 ? 0.1297 0.2002 0.1461 0.0055 0.0123 0.0235 394 VAL A CA 6017 C C . VAL A 386 ? 0.0903 0.2204 0.1282 -0.0171 0.0001 0.0018 394 VAL A C 6018 O O . VAL A 386 ? 0.1119 0.2103 0.1400 -0.0048 -0.0001 0.0082 394 VAL A O 6019 C CB . VAL A 386 ? 0.1374 0.1981 0.1510 -0.0058 0.0120 0.0339 394 VAL A CB 6020 C CG1 . VAL A 386 ? 0.1145 0.2471 0.1527 -0.0141 0.0161 0.0372 394 VAL A CG1 6021 C CG2 . VAL A 386 ? 0.1438 0.2449 0.1742 -0.0254 0.0090 0.0376 394 VAL A CG2 6031 N N . TYR A 387 ? 0.1058 0.1947 0.1401 -0.0061 0.0023 0.0172 395 TYR A N 6032 C CA . TYR A 387 ? 0.1065 0.1733 0.1440 -0.0113 0.0070 -0.0034 395 TYR A CA 6033 C C . TYR A 387 ? 0.1097 0.1635 0.1370 -0.0080 0.0080 0.0090 395 TYR A C 6034 O O . TYR A 387 ? 0.1082 0.1818 0.1349 -0.0127 0.0106 0.0036 395 TYR A O 6035 C CB . TYR A 387 ? 0.1234 0.1811 0.1433 -0.0083 0.0076 0.0002 395 TYR A CB 6036 C CG . TYR A 387 ? 0.1283 0.1923 0.1328 -0.0028 0.0214 0.0104 395 TYR A CG 6037 C CD1 . TYR A 387 ? 0.1412 0.2227 0.1404 0.0096 0.0156 0.0025 395 TYR A CD1 6038 C CD2 . TYR A 387 ? 0.1229 0.2046 0.1568 0.0048 0.0269 0.0076 395 TYR A CD2 6039 C CE1 . TYR A 387 ? 0.1749 0.2528 0.1466 0.0008 0.0306 0.0107 395 TYR A CE1 6040 C CE2 . TYR A 387 ? 0.1308 0.1973 0.1753 -0.0045 0.0433 0.0010 395 TYR A CE2 6041 C CZ . TYR A 387 ? 0.1748 0.2355 0.1562 -0.0092 0.0350 -0.0095 395 TYR A CZ 6042 O OH . TYR A 387 ? 0.2251 0.2770 0.1451 0.0223 0.0335 -0.0178 395 TYR A OH 6052 N N . ASN A 388 ? 0.1102 0.1636 0.1351 -0.0048 0.0106 0.0048 396 ASN A N 6053 C CA . ASN A 388 ? 0.1070 0.1745 0.1377 -0.0096 0.0030 0.0050 396 ASN A CA 6054 C C . ASN A 388 ? 0.1135 0.1673 0.1350 -0.0182 -0.0118 0.0258 396 ASN A C 6055 O O . ASN A 388 ? 0.1228 0.1752 0.1442 -0.0028 0.0108 0.0087 396 ASN A O 6056 C CB . ASN A 388 ? 0.1120 0.1753 0.1642 -0.0245 0.0189 -0.0064 396 ASN A CB 6057 C CG . ASN A 388 ? 0.1297 0.1679 0.1656 -0.0068 0.0104 -0.0106 396 ASN A CG 6058 O OD1 . ASN A 388 ? 0.1638 0.1876 0.1692 0.0084 -0.0021 -0.0025 396 ASN A OD1 6059 N ND2 . ASN A 388 ? 0.1255 0.1910 0.1502 0.0093 -0.0012 0.0058 396 ASN A ND2 6066 N N . SER A 389 ? 0.1261 0.1681 0.1423 -0.0017 0.0219 0.0150 397 SER A N 6067 C CA . SER A 389 ? 0.1109 0.1705 0.1640 0.0101 0.0033 0.0174 397 SER A CA 6068 C C . SER A 389 ? 0.1262 0.1716 0.1333 -0.0155 -0.0233 0.0097 397 SER A C 6069 O O . SER A 389 ? 0.1104 0.2026 0.1407 0.0003 -0.0085 0.0141 397 SER A O 6070 C CB . SER A 389 ? 0.1115 0.1987 0.1905 -0.0067 -0.0002 0.0195 397 SER A CB 6071 O OG . SER A 389 ? 0.1337 0.2219 0.1958 -0.0057 0.0008 0.0395 397 SER A OG 6077 N N . VAL A 390 ? 0.1247 0.1744 0.1445 0.0167 -0.0050 0.0076 398 VAL A N 6078 C CA . VAL A 390 ? 0.1225 0.1781 0.1386 -0.0056 0.0061 -0.0134 398 VAL A CA 6079 C C . VAL A 390 ? 0.1172 0.1706 0.1421 0.0027 0.0012 -0.0081 398 VAL A C 6080 O O . VAL A 390 ? 0.1092 0.2017 0.1501 -0.0069 -0.0041 0.0022 398 VAL A O 6081 C CB . VAL A 390 ? 0.1257 0.1689 0.1367 0.0049 0.0171 0.0123 398 VAL A CB 6082 C CG1 . VAL A 390 ? 0.1388 0.1507 0.1450 -0.0129 0.0076 0.0065 398 VAL A CG1 6083 C CG2 . VAL A 390 ? 0.1172 0.1957 0.1404 0.0108 -0.0021 0.0112 398 VAL A CG2 6093 N N . SER A 391 ? 0.1128 0.2274 0.1416 -0.0201 0.0155 0.0309 399 SER A N 6094 C CA . SER A 391 ? 0.1384 0.2374 0.1427 -0.0097 0.0062 0.0286 399 SER A CA 6095 C C . SER A 391 ? 0.1585 0.2400 0.1551 -0.0111 0.0002 0.0333 399 SER A C 6096 O O . SER A 391 ? 0.1933 0.3070 0.1504 -0.0128 -0.0230 0.0382 399 SER A O 6097 C CB . SER A 391 ? 0.1519 0.2637 0.1365 -0.0013 -0.0014 0.0230 399 SER A CB 6098 O OG . SER A 391 ? 0.1535 0.2519 0.1507 0.0044 0.0100 0.0065 399 SER A OG 6104 N N . TYR A 392 ? 0.1373 0.2316 0.1651 0.0066 -0.0023 0.0532 400 TYR A N 6105 C CA . TYR A 392 ? 0.1488 0.2237 0.1907 0.0235 0.0123 0.0500 400 TYR A CA 6106 C C . TYR A 392 ? 0.1383 0.2604 0.2231 0.0269 0.0128 0.0820 400 TYR A C 6107 O O . TYR A 392 ? 0.2081 0.2674 0.2246 0.0285 -0.0138 0.0921 400 TYR A O 6108 C CB . TYR A 392 ? 0.1462 0.2256 0.1950 0.0057 0.0027 0.0521 400 TYR A CB 6109 C CG . TYR A 392 ? 0.1431 0.1945 0.2146 0.0082 0.0002 0.0527 400 TYR A CG 6110 C CD1 . TYR A 392 ? 0.1532 0.2118 0.2273 -0.0016 -0.0006 0.0388 400 TYR A CD1 6111 C CD2 . TYR A 392 ? 0.1773 0.2245 0.2131 0.0141 0.0084 0.0441 400 TYR A CD2 6112 C CE1 . TYR A 392 ? 0.1781 0.2023 0.2413 0.0099 -0.0078 -0.0070 400 TYR A CE1 6113 C CE2 . TYR A 392 ? 0.2103 0.2250 0.2344 0.0142 0.0034 0.0035 400 TYR A CE2 6114 C CZ . TYR A 392 ? 0.2139 0.1963 0.2452 0.0300 -0.0190 0.0271 400 TYR A CZ 6115 O OH . TYR A 392 ? 0.2665 0.2436 0.2834 0.0612 -0.0070 -0.0056 400 TYR A OH 6125 N N . ASN A 393 ? 0.1409 0.2606 0.2681 0.0100 0.0014 0.1097 401 ASN A N 6126 C CA . ASN A 393 ? 0.1652 0.2787 0.3099 -0.0203 0.0178 0.1352 401 ASN A CA 6127 C C . ASN A 393 ? 0.1538 0.3133 0.3067 -0.0147 0.0188 0.1453 401 ASN A C 6128 O O . ASN A 393 ? 0.1764 0.3341 0.3276 0.0189 0.0228 0.1751 401 ASN A O 6129 C CB . ASN A 393 ? 0.2144 0.3136 0.3388 -0.0064 0.0224 0.1140 401 ASN A CB 6130 C CG . ASN A 393 ? 0.2960 0.3531 0.3560 -0.0011 -0.0108 0.0887 401 ASN A CG 6131 O OD1 . ASN A 393 ? 0.3109 0.3545 0.3857 -0.0081 0.0332 0.0859 401 ASN A OD1 6132 N ND2 . ASN A 393 ? 0.3425 0.4110 0.3846 -0.0424 -0.0228 0.0445 401 ASN A ND2 6139 N N . HIS A 394 ? 0.1673 0.3024 0.2996 0.0248 0.0095 0.1378 402 HIS A N 6140 C CA . HIS A 394 ? 0.1661 0.2938 0.2848 -0.0045 0.0019 0.1143 402 HIS A CA 6141 C C . HIS A 394 ? 0.1949 0.2954 0.2866 -0.0073 -0.0120 0.1097 402 HIS A C 6142 O O . HIS A 394 ? 0.2475 0.3112 0.2816 -0.0395 0.0041 0.0947 402 HIS A O 6143 C CB . HIS A 394 ? 0.2310 0.3175 0.2720 -0.0334 -0.0143 0.1335 402 HIS A CB 6144 C CG . HIS A 394 ? 0.2690 0.3639 0.2691 -0.0499 -0.0354 0.1415 402 HIS A CG 6145 N ND1 . HIS A 394 ? 0.2471 0.4325 0.2470 -0.0786 -0.0710 0.1218 402 HIS A ND1 6146 C CD2 . HIS A 394 ? 0.2974 0.3940 0.3060 -0.1124 -0.0047 0.1237 402 HIS A CD2 6147 C CE1 . HIS A 394 ? 0.2384 0.4202 0.2492 -0.0958 -0.0814 0.1341 402 HIS A CE1 6148 N NE2 . HIS A 394 ? 0.3208 0.4117 0.2990 -0.1190 -0.0313 0.1064 402 HIS A NE2 6156 N N . LEU A 395 ? 0.2056 0.2790 0.2930 0.0019 -0.0097 0.1058 403 LEU A N 6157 C CA . LEU A 395 ? 0.2170 0.2760 0.3099 -0.0161 -0.0222 0.0957 403 LEU A CA 6158 C C . LEU A 395 ? 0.2122 0.2743 0.2917 -0.0057 -0.0195 0.0963 403 LEU A C 6159 O O . LEU A 395 ? 0.2322 0.2586 0.2593 -0.0018 -0.0031 0.0749 403 LEU A O 6160 C CB . LEU A 395 ? 0.2545 0.2672 0.3589 -0.0263 -0.0010 0.0561 403 LEU A CB 6161 C CG . LEU A 395 ? 0.2793 0.2992 0.3921 0.0039 0.0250 0.0475 403 LEU A CG 6162 C CD1 . LEU A 395 ? 0.3023 0.3150 0.4108 0.0042 0.0413 0.0559 403 LEU A CD1 6163 C CD2 . LEU A 395 ? 0.3054 0.3179 0.4165 0.0254 0.0161 0.0510 403 LEU A CD2 6175 N N . THR A 396 ? 0.2181 0.2936 0.2779 -0.0298 -0.0207 0.1208 404 THR A N 6176 C CA . THR A 396 ? 0.2131 0.2613 0.2839 -0.0655 -0.0398 0.0789 404 THR A CA 6177 C C . THR A 396 ? 0.2403 0.2251 0.2864 -0.0729 -0.0338 0.0534 404 THR A C 6178 O O . THR A 396 ? 0.2733 0.2486 0.3032 -0.0320 -0.0308 0.0556 404 THR A O 6179 C CB . THR A 396 ? 0.2338 0.3531 0.2854 -0.0355 -0.0183 0.0720 404 THR A CB 6180 O OG1 . THR A 396 ? 0.2892 0.3947 0.2699 -0.0564 -0.0221 0.0738 404 THR A OG1 6181 C CG2 . THR A 396 ? 0.2203 0.3580 0.2784 -0.0488 0.0051 0.0781 404 THR A CG2 6189 N N . CYS A 397 ? 0.2373 0.2220 0.2617 -0.0150 -0.0256 0.0710 405 CYS A N 6190 C CA . CYS A 397 ? 0.2299 0.2628 0.2685 -0.0517 -0.0342 0.0697 405 CYS A CA 6191 C C . CYS A 397 ? 0.2760 0.3078 0.2754 -0.0842 -0.0586 0.0788 405 CYS A C 6192 O O . CYS A 397 ? 0.2883 0.2861 0.2897 -0.0939 -0.0591 0.0981 405 CYS A O 6193 C CB . CYS A 397 ? 0.2014 0.2428 0.2732 -0.0395 -0.0316 0.0615 405 CYS A CB 6194 S SG . CYS A 397 ? 0.2012 0.2570 0.2801 -0.0417 -0.0303 0.0659 405 CYS A SG 6199 N N . GLU A 398 ? 0.2881 0.2989 0.2891 -0.1038 -0.0753 0.1052 406 GLU A N 6200 C CA . GLU A 398 ? 0.3485 0.3267 0.3225 -0.1030 -0.0942 0.1047 406 GLU A CA 6201 C C . GLU A 398 ? 0.3169 0.3070 0.3176 -0.1145 -0.0707 0.1142 406 GLU A C 6202 O O . GLU A 398 ? 0.3001 0.2715 0.3036 -0.0913 -0.0756 0.1244 406 GLU A O 6203 C CB . GLU A 398 ? 0.4349 0.3960 0.3643 -0.0906 -0.1045 0.1090 406 GLU A CB 6204 C CG . GLU A 398 ? 0.4958 0.4492 0.3961 -0.0524 -0.1001 0.1561 406 GLU A CG 6205 C CD . GLU A 398 ? 0.5679 0.5670 0.4424 -0.0108 -0.0811 0.1308 406 GLU A CD 6206 O OE1 . GLU A 398 ? 0.5965 0.6001 0.4598 -0.0016 -0.0693 0.1188 406 GLU A OE1 6207 O OE2 . GLU A 398 ? 0.6110 0.6074 0.4583 0.0006 -0.0667 0.1428 406 GLU A OE2 6214 N N . ASP A 399 ? 0.3165 0.3179 0.3243 -0.1121 -0.0623 0.1109 407 ASP A N 6215 C CA . ASP A 399 ? 0.3395 0.3108 0.3554 -0.1547 -0.0524 0.0900 407 ASP A CA 6216 C C . ASP A 399 ? 0.3236 0.2514 0.3480 -0.1255 -0.0347 0.0865 407 ASP A C 6217 O O . ASP A 399 ? 0.2906 0.2678 0.3345 -0.1094 -0.0298 0.0991 407 ASP A O 6218 C CB . ASP A 399 ? 0.4159 0.4063 0.4075 -0.1636 -0.0057 0.0696 407 ASP A CB 6219 C CG . ASP A 399 ? 0.5038 0.5156 0.4578 -0.1459 0.0359 0.0653 407 ASP A CG 6220 O OD1 . ASP A 399 ? 0.5507 0.5804 0.4795 -0.1121 0.0548 0.0534 407 ASP A OD1 6221 O OD2 . ASP A 399 ? 0.5461 0.5922 0.4786 -0.1179 0.0415 0.0727 407 ASP A OD2 6226 N N . SER A 400 ? 0.3473 0.2516 0.3480 -0.0950 -0.0597 0.0778 408 SER A N 6227 C CA . SER A 400 ? 0.3446 0.2667 0.3557 -0.0567 -0.0274 0.0468 408 SER A CA 6228 C C . SER A 400 ? 0.2821 0.2454 0.3146 -0.0449 -0.0310 0.0545 408 SER A C 6229 O O . SER A 400 ? 0.2762 0.2327 0.2912 -0.0676 -0.0023 0.0388 408 SER A O 6230 C CB . SER A 400 ? 0.4106 0.2988 0.4017 -0.0381 -0.0183 0.0362 408 SER A CB 6231 O OG . SER A 400 ? 0.4858 0.3649 0.4317 -0.0250 0.0113 0.0234 408 SER A OG 6237 N N . CYS A 401 ? 0.2396 0.2394 0.3072 -0.0336 -0.0371 0.0602 409 CYS A N 6238 C CA . CYS A 401 ? 0.2168 0.2186 0.2736 -0.0204 -0.0420 0.0665 409 CYS A CA 6239 C C . CYS A 401 ? 0.2049 0.2175 0.2497 -0.0573 -0.0166 0.0483 409 CYS A C 6240 O O . CYS A 401 ? 0.1719 0.2238 0.2405 -0.0385 -0.0133 0.0598 409 CYS A O 6241 C CB . CYS A 401 ? 0.2334 0.2594 0.2812 -0.0375 -0.0253 0.0338 409 CYS A CB 6242 S SG . CYS A 401 ? 0.2142 0.2666 0.2886 -0.0318 -0.0280 0.0628 409 CYS A SG 6247 N N . ARG A 402 ? 0.2016 0.2146 0.2325 -0.0575 -0.0031 0.0495 410 ARG A N 6248 C CA . ARG A 402 ? 0.1983 0.2377 0.2204 -0.0551 0.0117 0.0466 410 ARG A CA 6249 C C . ARG A 402 ? 0.1835 0.2052 0.2130 -0.0494 -0.0038 0.0477 410 ARG A C 6250 O O . ARG A 402 ? 0.1812 0.2282 0.2062 -0.0189 0.0054 0.0307 410 ARG A O 6251 C CB . ARG A 402 ? 0.2082 0.2542 0.2209 -0.0836 -0.0051 0.0499 410 ARG A CB 6252 C CG . ARG A 402 ? 0.2070 0.2933 0.2152 -0.0572 0.0148 0.0479 410 ARG A CG 6253 C CD . ARG A 402 ? 0.2043 0.3045 0.2297 -0.0601 0.0040 0.0427 410 ARG A CD 6254 N NE . ARG A 402 ? 0.2111 0.3693 0.2674 -0.0426 0.0016 0.0183 410 ARG A NE 6255 C CZ . ARG A 402 ? 0.2472 0.3735 0.3026 -0.0647 0.0169 -0.0188 410 ARG A CZ 6256 N NH1 . ARG A 402 ? 0.2528 0.3989 0.3239 -0.0510 0.0143 -0.0235 410 ARG A NH1 6257 N NH2 . ARG A 402 ? 0.2582 0.3488 0.3262 -0.0555 -0.0073 -0.0168 410 ARG A NH2 6271 N N . ILE A 403 ? 0.1921 0.2214 0.2153 -0.0574 -0.0167 0.0479 411 ILE A N 6272 C CA A ILE A 403 ? 0.2008 0.2267 0.2273 -0.0632 -0.0268 0.0452 411 ILE A CA 6273 C CA B ILE A 403 ? 0.1856 0.2202 0.2291 -0.0698 -0.0219 0.0541 411 ILE A CA 6274 C C . ILE A 403 ? 0.1752 0.1812 0.2211 -0.0510 -0.0205 0.0111 411 ILE A C 6275 O O . ILE A 403 ? 0.1725 0.1918 0.2291 -0.0327 -0.0180 0.0284 411 ILE A O 6276 C CB A ILE A 403 ? 0.2826 0.2900 0.2467 -0.0952 -0.0400 0.0359 411 ILE A CB 6277 C CB B ILE A 403 ? 0.2499 0.2718 0.2546 -0.1150 -0.0303 0.0515 411 ILE A CB 6278 C CG1 A ILE A 403 ? 0.3441 0.3355 0.2624 -0.1142 -0.0294 0.0266 411 ILE A CG1 6279 C CG1 B ILE A 403 ? 0.3002 0.2809 0.2704 -0.1230 -0.0227 0.0372 411 ILE A CG1 6280 C CG2 A ILE A 403 ? 0.2975 0.2738 0.2435 -0.1151 -0.0562 0.0200 411 ILE A CG2 6281 C CG2 B ILE A 403 ? 0.2684 0.2612 0.2623 -0.1551 -0.0328 0.0435 411 ILE A CG2 6282 C CD1 A ILE A 403 ? 0.3882 0.3529 0.2692 -0.1034 -0.0312 0.0198 411 ILE A CD1 6283 C CD1 B ILE A 403 ? 0.3457 0.2964 0.2839 -0.1235 -0.0095 0.0280 411 ILE A CD1 6303 N N . GLU A 404 ? 0.1588 0.1776 0.2194 -0.0238 -0.0076 0.0126 412 GLU A N 6304 C CA . GLU A 404 ? 0.1869 0.1745 0.2087 -0.0194 0.0136 0.0015 412 GLU A CA 6305 C C . GLU A 404 ? 0.1701 0.1641 0.1997 -0.0217 -0.0001 0.0098 412 GLU A C 6306 O O . GLU A 404 ? 0.1790 0.1887 0.1928 -0.0022 0.0143 -0.0065 412 GLU A O 6307 C CB . GLU A 404 ? 0.2063 0.1583 0.2370 -0.0002 0.0108 0.0016 412 GLU A CB 6308 C CG . GLU A 404 ? 0.2465 0.1963 0.2687 0.0122 0.0051 0.0309 412 GLU A CG 6309 C CD . GLU A 404 ? 0.3200 0.2231 0.3179 0.0032 -0.0212 -0.0042 412 GLU A CD 6310 O OE1 . GLU A 404 ? 0.3458 0.2083 0.3582 0.0336 -0.0449 0.0023 412 GLU A OE1 6311 O OE2 . GLU A 404 ? 0.3587 0.2663 0.3497 0.0232 -0.0192 -0.0241 412 GLU A OE2 6318 N N . HIS A 405 ? 0.1420 0.1718 0.1975 -0.0175 -0.0081 0.0170 413 HIS A N 6319 C CA . HIS A 405 ? 0.1237 0.1872 0.1852 -0.0113 -0.0067 0.0045 413 HIS A CA 6320 C C . HIS A 405 ? 0.1342 0.1713 0.1854 -0.0269 0.0014 0.0165 413 HIS A C 6321 O O . HIS A 405 ? 0.1386 0.1766 0.1894 -0.0279 0.0018 0.0238 413 HIS A O 6322 C CB . HIS A 405 ? 0.1198 0.1961 0.1905 -0.0389 0.0101 0.0087 413 HIS A CB 6323 C CG . HIS A 405 ? 0.1418 0.1914 0.1859 -0.0227 -0.0057 0.0041 413 HIS A CG 6324 N ND1 . HIS A 405 ? 0.1365 0.1954 0.1656 -0.0239 0.0043 -0.0032 413 HIS A ND1 6325 C CD2 . HIS A 405 ? 0.1740 0.1981 0.2111 -0.0187 -0.0084 0.0095 413 HIS A CD2 6326 C CE1 . HIS A 405 ? 0.1355 0.1907 0.1911 -0.0321 -0.0152 0.0168 413 HIS A CE1 6327 N NE2 . HIS A 405 ? 0.1613 0.2162 0.2067 -0.0219 -0.0244 0.0186 413 HIS A NE2 6335 N N . VAL A 406 ? 0.1266 0.1710 0.1993 -0.0225 0.0010 0.0127 414 VAL A N 6336 C CA . VAL A 406 ? 0.1176 0.1971 0.2125 -0.0185 0.0027 0.0161 414 VAL A CA 6337 C C . VAL A 406 ? 0.1368 0.1541 0.2141 -0.0342 0.0157 0.0236 414 VAL A C 6338 O O . VAL A 406 ? 0.1264 0.1901 0.2051 -0.0298 0.0160 0.0244 414 VAL A O 6339 C CB . VAL A 406 ? 0.1213 0.2355 0.2173 -0.0287 0.0172 -0.0078 414 VAL A CB 6340 C CG1 . VAL A 406 ? 0.1441 0.2597 0.2389 -0.0246 0.0543 0.0086 414 VAL A CG1 6341 C CG2 . VAL A 406 ? 0.1957 0.2306 0.2185 0.0020 0.0418 0.0037 414 VAL A CG2 6351 N N . CYS A 407 ? 0.1248 0.1637 0.2036 -0.0371 -0.0075 0.0184 415 CYS A N 6352 C CA . CYS A 407 ? 0.1477 0.1617 0.2079 -0.0331 -0.0044 0.0289 415 CYS A CA 6353 C C . CYS A 407 ? 0.1536 0.1588 0.2016 -0.0375 0.0008 0.0101 415 CYS A C 6354 O O . CYS A 407 ? 0.1503 0.1785 0.1906 -0.0177 -0.0048 0.0024 415 CYS A O 6355 C CB . CYS A 407 ? 0.1526 0.1621 0.2210 -0.0293 0.0001 0.0145 415 CYS A CB 6356 S SG . CYS A 407 ? 0.1728 0.2147 0.2540 -0.0471 -0.0023 0.0168 415 CYS A SG 6361 N N . ALA A 408 ? 0.1344 0.1728 0.1757 -0.0347 -0.0073 0.0117 416 ALA A N 6362 C CA . ALA A 408 ? 0.1246 0.1436 0.1919 -0.0197 0.0030 -0.0130 416 ALA A CA 6363 C C . ALA A 408 ? 0.1059 0.1462 0.1885 -0.0001 -0.0016 -0.0275 416 ALA A C 6364 O O . ALA A 408 ? 0.1398 0.1800 0.1671 -0.0292 0.0037 0.0195 416 ALA A O 6365 C CB . ALA A 408 ? 0.1514 0.1579 0.1964 0.0065 -0.0066 -0.0052 416 ALA A CB 6371 N N . ILE A 409 ? 0.1348 0.1430 0.1768 -0.0178 0.0065 -0.0050 417 ILE A N 6372 C CA . ILE A 409 ? 0.1256 0.1575 0.1727 -0.0267 -0.0018 0.0116 417 ILE A CA 6373 C C . ILE A 409 ? 0.1357 0.1707 0.1647 -0.0281 0.0005 0.0180 417 ILE A C 6374 O O . ILE A 409 ? 0.1331 0.1861 0.1802 -0.0041 -0.0099 0.0189 417 ILE A O 6375 C CB . ILE A 409 ? 0.1194 0.1541 0.1725 -0.0137 0.0203 -0.0030 417 ILE A CB 6376 C CG1 . ILE A 409 ? 0.1189 0.1522 0.1724 -0.0178 -0.0041 0.0069 417 ILE A CG1 6377 C CG2 . ILE A 409 ? 0.1122 0.2105 0.1817 -0.0322 0.0179 -0.0064 417 ILE A CG2 6378 C CD1 . ILE A 409 ? 0.1439 0.2079 0.1790 -0.0112 -0.0002 0.0023 417 ILE A CD1 6390 N N . GLN A 410 ? 0.1377 0.1737 0.1879 -0.0213 -0.0011 0.0180 418 GLN A N 6391 C CA A GLN A 410 ? 0.1293 0.2007 0.2025 -0.0150 0.0029 -0.0024 418 GLN A CA 6392 C CA B GLN A 410 ? 0.1162 0.1940 0.1995 -0.0129 0.0000 0.0077 418 GLN A CA 6393 C C . GLN A 410 ? 0.1299 0.2105 0.2122 0.0013 0.0132 0.0167 418 GLN A C 6394 O O . GLN A 410 ? 0.1465 0.2470 0.2086 0.0120 -0.0069 0.0215 418 GLN A O 6395 C CB A GLN A 410 ? 0.1597 0.2599 0.2211 -0.0273 0.0130 -0.0183 418 GLN A CB 6396 C CB B GLN A 410 ? 0.1113 0.2283 0.2106 -0.0226 -0.0011 0.0074 418 GLN A CB 6397 C CG A GLN A 410 ? 0.2092 0.3284 0.2191 -0.0411 0.0075 -0.0245 418 GLN A CG 6398 C CG B GLN A 410 ? 0.1082 0.2604 0.1917 -0.0233 -0.0369 0.0285 418 GLN A CG 6399 C CD A GLN A 410 ? 0.2756 0.3857 0.2418 -0.0555 0.0236 -0.0031 418 GLN A CD 6400 C CD B GLN A 410 ? 0.1231 0.3201 0.2020 -0.0171 -0.0495 0.0099 418 GLN A CD 6401 O OE1 A GLN A 410 ? 0.3226 0.3841 0.2471 -0.0368 0.0345 -0.0052 418 GLN A OE1 6402 O OE1 B GLN A 410 ? 0.1723 0.3492 0.1988 0.0296 -0.0543 0.0182 418 GLN A OE1 6403 N NE2 A GLN A 410 ? 0.2897 0.4035 0.2456 -0.0639 0.0158 0.0072 418 GLN A NE2 6404 N NE2 B GLN A 410 ? 0.1292 0.3463 0.2217 0.0107 -0.0138 0.0104 418 GLN A NE2 6419 N N . HIS A 411 ? 0.1144 0.2183 0.1911 -0.0014 -0.0099 -0.0026 419 HIS A N 6420 C CA . HIS A 411 ? 0.1394 0.1911 0.1947 -0.0288 0.0004 0.0032 419 HIS A CA 6421 C C . HIS A 411 ? 0.1377 0.1835 0.1920 -0.0071 -0.0236 0.0143 419 HIS A C 6422 O O . HIS A 411 ? 0.1336 0.1895 0.2186 -0.0170 0.0019 0.0163 419 HIS A O 6423 C CB . HIS A 411 ? 0.1584 0.2181 0.2092 -0.0117 -0.0024 0.0143 419 HIS A CB 6424 C CG . HIS A 411 ? 0.1477 0.2840 0.2263 -0.0269 -0.0258 0.0059 419 HIS A CG 6425 N ND1 . HIS A 411 ? 0.1277 0.4066 0.2779 -0.0635 0.0081 0.0232 419 HIS A ND1 6426 C CD2 . HIS A 411 ? 0.1815 0.2593 0.2293 -0.0536 0.0085 -0.0267 419 HIS A CD2 6427 C CE1 . HIS A 411 ? 0.1550 0.3950 0.2869 -0.0730 0.0338 0.0168 419 HIS A CE1 6428 N NE2 . HIS A 411 ? 0.1677 0.3270 0.2595 -0.0829 0.0251 -0.0185 419 HIS A NE2 6436 N N . VAL A 412 ? 0.1190 0.1784 0.2004 -0.0149 -0.0225 0.0123 420 VAL A N 6437 C CA . VAL A 412 ? 0.1267 0.1841 0.1932 -0.0097 -0.0066 0.0015 420 VAL A CA 6438 C C . VAL A 412 ? 0.1252 0.2041 0.1932 -0.0137 -0.0001 -0.0136 420 VAL A C 6439 O O . VAL A 412 ? 0.1461 0.2254 0.1784 -0.0071 -0.0021 -0.0192 420 VAL A O 6440 C CB . VAL A 412 ? 0.1460 0.1824 0.1954 -0.0030 -0.0204 -0.0009 420 VAL A CB 6441 C CG1 . VAL A 412 ? 0.1767 0.2130 0.2158 -0.0209 0.0075 0.0133 420 VAL A CG1 6442 C CG2 . VAL A 412 ? 0.1902 0.2057 0.2113 -0.0225 -0.0355 -0.0130 420 VAL A CG2 6452 N N . ALA A 413 ? 0.1261 0.1996 0.2065 -0.0171 -0.0013 -0.0162 421 ALA A N 6453 C CA . ALA A 413 ? 0.1587 0.1838 0.2165 -0.0333 -0.0051 -0.0084 421 ALA A CA 6454 C C . ALA A 413 ? 0.1432 0.1964 0.2185 -0.0514 -0.0250 -0.0295 421 ALA A C 6455 O O . ALA A 413 ? 0.1769 0.2059 0.2243 -0.0341 -0.0044 -0.0180 421 ALA A O 6456 C CB . ALA A 413 ? 0.1322 0.2301 0.2387 -0.0264 -0.0268 -0.0002 421 ALA A CB 6462 N N . PHE A 414 ? 0.1692 0.1973 0.2165 -0.0234 -0.0291 -0.0333 422 PHE A N 6463 C CA . PHE A 414 ? 0.1924 0.1818 0.2368 -0.0350 -0.0238 -0.0485 422 PHE A CA 6464 C C . PHE A 414 ? 0.2184 0.2174 0.2477 -0.0634 -0.0297 -0.0286 422 PHE A C 6465 O O . PHE A 414 ? 0.2335 0.2173 0.2195 -0.0595 -0.0282 0.0092 422 PHE A O 6466 C CB . PHE A 414 ? 0.2031 0.1777 0.2336 -0.0182 -0.0253 -0.0551 422 PHE A CB 6467 C CG . PHE A 414 ? 0.1777 0.2030 0.2289 0.0098 -0.0169 -0.0076 422 PHE A CG 6468 C CD1 . PHE A 414 ? 0.1781 0.1960 0.2541 -0.0060 0.0014 0.0094 422 PHE A CD1 6469 C CD2 . PHE A 414 ? 0.2004 0.2649 0.2527 0.0300 -0.0132 -0.0426 422 PHE A CD2 6470 C CE1 . PHE A 414 ? 0.1869 0.1847 0.2464 -0.0034 0.0022 0.0183 422 PHE A CE1 6471 C CE2 . PHE A 414 ? 0.2156 0.2885 0.2511 0.0189 0.0115 -0.0240 422 PHE A CE2 6472 C CZ . PHE A 414 ? 0.2185 0.2477 0.2356 0.0024 0.0065 0.0074 422 PHE A CZ 6482 N N . ASN A 415 ? 0.2429 0.2440 0.2458 -0.0928 -0.0395 -0.0410 423 ASN A N 6483 C CA . ASN A 415 ? 0.2465 0.3053 0.2795 -0.1352 -0.0436 -0.0394 423 ASN A CA 6484 C C . ASN A 415 ? 0.1888 0.2813 0.2720 -0.0820 -0.0395 -0.0010 423 ASN A C 6485 O O . ASN A 415 ? 0.2333 0.2373 0.2971 -0.0820 0.0016 -0.0352 423 ASN A O 6486 C CB . ASN A 415 ? 0.2972 0.4108 0.3200 -0.1501 -0.0794 -0.0603 423 ASN A CB 6487 C CG . ASN A 415 ? 0.4090 0.4900 0.3696 -0.1274 -0.0697 -0.0798 423 ASN A CG 6488 O OD1 . ASN A 415 ? 0.4522 0.4977 0.3914 -0.1102 -0.0353 -0.1162 423 ASN A OD1 6489 N ND2 . ASN A 415 ? 0.4820 0.5376 0.3789 -0.1084 -0.0584 -0.0661 423 ASN A ND2 6496 N N . THR A 416 ? 0.1773 0.2726 0.2435 -0.0563 -0.0445 0.0058 424 THR A N 6497 C CA . THR A 416 ? 0.1945 0.2758 0.2537 -0.0340 -0.0501 -0.0124 424 THR A CA 6498 C C . THR A 416 ? 0.1634 0.2233 0.2506 -0.0686 -0.0170 -0.0013 424 THR A C 6499 O O . THR A 416 ? 0.1653 0.2407 0.2596 -0.0546 -0.0132 0.0052 424 THR A O 6500 C CB . THR A 416 ? 0.2693 0.3447 0.2652 0.0211 -0.0789 0.0073 424 THR A CB 6501 O OG1 . THR A 416 ? 0.3369 0.3729 0.2600 0.0101 -0.0208 0.0012 424 THR A OG1 6502 C CG2 . THR A 416 ? 0.3498 0.3898 0.2863 0.0516 -0.1050 -0.0167 424 THR A CG2 6510 N N . TYR A 417 ? 0.1373 0.2040 0.2353 -0.0536 -0.0050 -0.0147 425 TYR A N 6511 C CA . TYR A 417 ? 0.1406 0.1872 0.2394 -0.0398 -0.0062 0.0021 425 TYR A CA 6512 C C . TYR A 417 ? 0.1599 0.1969 0.2574 -0.0497 0.0036 0.0044 425 TYR A C 6513 O O . TYR A 417 ? 0.1659 0.1830 0.2616 -0.0282 0.0193 -0.0018 425 TYR A O 6514 C CB . TYR A 417 ? 0.1579 0.1787 0.2291 -0.0518 -0.0049 0.0032 425 TYR A CB 6515 C CG . TYR A 417 ? 0.1406 0.1814 0.2166 -0.0402 0.0134 -0.0218 425 TYR A CG 6516 C CD1 . TYR A 417 ? 0.1680 0.1594 0.2311 -0.0193 0.0061 -0.0166 425 TYR A CD1 6517 C CD2 . TYR A 417 ? 0.1499 0.1590 0.2202 -0.0263 0.0184 -0.0305 425 TYR A CD2 6518 C CE1 . TYR A 417 ? 0.1862 0.1801 0.2410 -0.0120 -0.0026 -0.0164 425 TYR A CE1 6519 C CE2 . TYR A 417 ? 0.1398 0.1892 0.2129 -0.0362 0.0033 -0.0061 425 TYR A CE2 6520 C CZ . TYR A 417 ? 0.1618 0.1779 0.2178 -0.0229 -0.0080 -0.0011 425 TYR A CZ 6521 O OH . TYR A 417 ? 0.1787 0.1908 0.2255 -0.0121 -0.0256 -0.0142 425 TYR A OH 6531 N N . ALA A 418 ? 0.2020 0.2133 0.2537 -0.0496 -0.0013 -0.0197 426 ALA A N 6532 C CA . ALA A 418 ? 0.2180 0.2231 0.2795 -0.0485 0.0021 -0.0084 426 ALA A CA 6533 C C . ALA A 418 ? 0.2379 0.2233 0.3069 -0.0542 0.0151 -0.0099 426 ALA A C 6534 O O . ALA A 418 ? 0.2385 0.2045 0.3204 -0.0677 0.0311 -0.0138 426 ALA A O 6535 C CB . ALA A 418 ? 0.2695 0.2432 0.3004 -0.0719 0.0201 -0.0253 426 ALA A CB 6541 N N . THR A 419 ? 0.2148 0.2276 0.3165 -0.0708 0.0081 -0.0288 427 THR A N 6542 C CA . THR A 419 ? 0.2101 0.2661 0.3220 -0.0871 0.0071 -0.0181 427 THR A CA 6543 C C . THR A 419 ? 0.1869 0.2432 0.3122 -0.0900 0.0232 0.0032 427 THR A C 6544 O O . THR A 419 ? 0.1773 0.2214 0.3238 -0.0684 0.0330 -0.0132 427 THR A O 6545 C CB . THR A 419 ? 0.1850 0.3990 0.3279 -0.0647 -0.0226 -0.0373 427 THR A CB 6546 O OG1 . THR A 419 ? 0.2675 0.4454 0.3534 -0.0944 -0.0159 -0.0599 427 THR A OG1 6547 C CG2 . THR A 419 ? 0.2296 0.4309 0.3530 -0.0515 -0.0030 0.0049 427 THR A CG2 6555 N N . CYS A 420 ? 0.1872 0.2087 0.2874 -0.0610 0.0133 -0.0046 428 CYS A N 6556 C CA . CYS A 420 ? 0.1726 0.2027 0.2679 -0.0422 0.0120 0.0300 428 CYS A CA 6557 C C . CYS A 420 ? 0.1841 0.1832 0.2953 -0.0505 -0.0001 0.0224 428 CYS A C 6558 O O . CYS A 420 ? 0.1939 0.1978 0.2984 -0.0475 0.0295 0.0325 428 CYS A O 6559 C CB . CYS A 420 ? 0.1848 0.1963 0.2495 -0.0213 0.0080 0.0035 428 CYS A CB 6560 S SG . CYS A 420 ? 0.1628 0.2354 0.2558 -0.0385 0.0020 0.0091 428 CYS A SG 6565 N N . LEU A 421 ? 0.1911 0.2411 0.3314 -0.0304 -0.0203 0.0095 429 LEU A N 6566 C CA . LEU A 421 ? 0.2108 0.3213 0.4039 0.0220 -0.0052 0.0281 429 LEU A CA 6567 C C . LEU A 421 ? 0.3135 0.3109 0.4803 0.0194 -0.0211 0.0584 429 LEU A C 6568 O O . LEU A 421 ? 0.3153 0.3596 0.4941 0.0067 -0.0168 0.0906 429 LEU A O 6569 C CB . LEU A 421 ? 0.2269 0.3579 0.4084 0.0370 0.0088 0.0446 429 LEU A CB 6570 C CG . LEU A 421 ? 0.2921 0.3263 0.4218 -0.0001 0.0446 0.0443 429 LEU A CG 6571 C CD1 . LEU A 421 ? 0.3038 0.3010 0.4357 0.0469 0.0662 0.0513 429 LEU A CD1 6572 C CD2 . LEU A 421 ? 0.2975 0.3845 0.4276 0.0057 0.0332 0.0358 429 LEU A CD2 6584 N N . HIS A 422 ? 0.4085 0.2566 0.5237 -0.0598 -0.0389 0.0318 430 HIS A N 6585 C CA . HIS A 422 ? 0.4933 0.3934 0.5620 -0.0655 -0.0179 0.0431 430 HIS A CA 6586 C C . HIS A 422 ? 0.5115 0.4476 0.5762 -0.0598 -0.0064 0.0632 430 HIS A C 6587 O O . HIS A 422 ? 0.5124 0.4654 0.5839 -0.0725 -0.0157 0.0638 430 HIS A O 6588 C CB . HIS A 422 ? 0.5788 0.4370 0.5821 -0.0351 -0.0096 0.0341 430 HIS A CB 6589 C CG . HIS A 422 ? 0.6408 0.4838 0.6103 -0.0193 -0.0009 0.0060 430 HIS A CG 6590 N ND1 . HIS A 422 ? 0.6679 0.5008 0.6227 -0.0260 -0.0029 -0.0147 430 HIS A ND1 6591 C CD2 . HIS A 422 ? 0.6614 0.5090 0.6245 -0.0063 0.0017 -0.0035 430 HIS A CD2 6592 C CE1 . HIS A 422 ? 0.6777 0.5178 0.6304 -0.0179 0.0024 -0.0171 430 HIS A CE1 6593 N NE2 . HIS A 422 ? 0.6733 0.5233 0.6324 -0.0114 0.0069 -0.0137 430 HIS A NE2 6601 N N . GLY A 423 ? 0.5213 0.4652 0.5822 -0.0326 0.0067 0.0768 431 GLY A N 6602 C CA . GLY A 423 ? 0.5099 0.4934 0.5929 0.0117 -0.0038 0.0888 431 GLY A CA 6603 C C . GLY A 423 ? 0.5039 0.5065 0.5989 0.0170 -0.0233 0.1009 431 GLY A C 6604 O O . GLY A 423 ? 0.5229 0.5013 0.6075 0.0098 -0.0269 0.1115 431 GLY A O 6608 ZN ZN . ZN B . ? 0.1090 0.1834 0.1755 0.0038 0.0103 0.0065 501 ZN A ZN 6609 ZN ZN . ZN C . ? 0.1005 0.1982 0.1487 -0.0045 0.0025 -0.0071 502 ZN A ZN 6610 C C1 . NAG D . ? 0.2209 0.2689 0.3306 -0.0592 -0.0745 -0.0232 503 NAG A C1 6611 C C2 . NAG D . ? 0.2541 0.3469 0.3639 -0.1101 -0.0558 -0.0339 503 NAG A C2 6612 C C3 . NAG D . ? 0.2969 0.3802 0.3804 -0.1417 -0.1047 -0.0474 503 NAG A C3 6613 C C4 . NAG D . ? 0.3221 0.3238 0.3978 -0.1027 -0.1320 -0.0601 503 NAG A C4 6614 C C5 . NAG D . ? 0.3013 0.2596 0.3735 -0.0516 -0.1215 -0.0611 503 NAG A C5 6615 C C6 . NAG D . ? 0.3259 0.2591 0.3969 -0.0080 -0.1092 -0.0727 503 NAG A C6 6616 C C7 . NAG D . ? 0.2521 0.4330 0.4102 -0.0771 0.0452 -0.0118 503 NAG A C7 6617 C C8 . NAG D . ? 0.3098 0.4703 0.4116 -0.0739 0.0537 0.0004 503 NAG A C8 6618 N N2 . NAG D . ? 0.2403 0.4044 0.3857 -0.1136 0.0089 -0.0306 503 NAG A N2 6619 O O3 . NAG D . ? 0.3420 0.4775 0.3832 -0.1380 -0.0846 -0.0224 503 NAG A O3 6620 O O4 . NAG D . ? 0.4369 0.3562 0.4393 -0.1025 -0.1387 -0.0722 503 NAG A O4 6621 O O5 . NAG D . ? 0.2458 0.2166 0.3538 -0.0429 -0.0858 -0.0497 503 NAG A O5 6622 O O6 . NAG D . ? 0.3298 0.3094 0.4066 -0.0113 -0.1013 -0.0956 503 NAG A O6 6623 O O7 . NAG D . ? 0.2977 0.4340 0.4170 -0.0169 0.0549 -0.0100 503 NAG A O7 6637 C C1 . NAG E . ? 0.4920 0.4237 0.4834 -0.0761 -0.1560 -0.1059 504 NAG A C1 6638 C C2 . NAG E . ? 0.5296 0.4087 0.5080 -0.0930 -0.1487 -0.1479 504 NAG A C2 6639 C C3 . NAG E . ? 0.5865 0.4632 0.5282 -0.0485 -0.1208 -0.1377 504 NAG A C3 6640 C C4 . NAG E . ? 0.5975 0.5214 0.5311 -0.0069 -0.1198 -0.1024 504 NAG A C4 6641 C C5 . NAG E . ? 0.5671 0.5411 0.5195 -0.0150 -0.1484 -0.0910 504 NAG A C5 6642 C C6 . NAG E . ? 0.5906 0.6022 0.5353 0.0080 -0.1228 -0.0655 504 NAG A C6 6643 C C7 . NAG E . ? 0.5919 0.3817 0.5651 -0.0794 -0.0564 -0.1356 504 NAG A C7 6644 C C8 . NAG E . ? 0.5832 0.3904 0.5737 -0.0607 -0.0568 -0.1297 504 NAG A C8 6645 N N2 . NAG E . ? 0.5740 0.3967 0.5361 -0.0730 -0.0997 -0.1353 504 NAG A N2 6646 O O3 . NAG E . ? 0.6262 0.4733 0.5538 -0.0287 -0.0867 -0.1323 504 NAG A O3 6647 O O4 . NAG E . ? 0.6356 0.5502 0.5429 0.0015 -0.0923 -0.1053 504 NAG A O4 6648 O O5 . NAG E . ? 0.5059 0.4910 0.4894 -0.0705 -0.2033 -0.1162 504 NAG A O5 6649 O O6 . NAG E . ? 0.5987 0.6377 0.5420 0.0128 -0.1140 -0.0573 504 NAG A O6 6650 O O7 . NAG E . ? 0.6364 0.3636 0.5808 -0.1101 -0.0223 -0.1321 504 NAG A O7 6665 C C1 . BMA F . ? 0.4169 0.5865 0.4032 -0.0915 0.0147 0.1152 505 BMA A C1 6666 C C2 . BMA F . ? 0.4379 0.6009 0.4191 -0.0915 0.0065 0.0977 505 BMA A C2 6667 C C3 . BMA F . ? 0.4507 0.6021 0.4346 -0.0679 0.0243 0.0867 505 BMA A C3 6668 C C4 . BMA F . ? 0.4639 0.6483 0.4375 -0.0573 0.0346 0.0878 505 BMA A C4 6669 C C5 . BMA F . ? 0.4604 0.6288 0.4284 -0.0579 0.0270 0.1023 505 BMA A C5 6670 C C6 . BMA F . ? 0.4738 0.5898 0.4387 -0.0403 0.0196 0.1005 505 BMA A C6 6671 O O2 . BMA F . ? 0.4270 0.5953 0.4152 -0.1032 -0.0363 0.0899 505 BMA A O2 6672 O O3 . BMA F . ? 0.4374 0.5391 0.4419 -0.0653 0.0314 0.0851 505 BMA A O3 6673 O O4 . BMA F . ? 0.4828 0.6851 0.4421 -0.0426 0.0454 0.0861 505 BMA A O4 6674 O O5 . BMA F . ? 0.4325 0.6083 0.4122 -0.0607 0.0293 0.1295 505 BMA A O5 6675 O O6 . BMA F . ? 0.4677 0.5340 0.4464 -0.0172 0.0100 0.0990 505 BMA A O6 6685 C C1 . MAN G . ? 0.4303 0.4812 0.4607 -0.0457 0.0271 0.0269 506 MAN A C1 6686 C C2 . MAN G . ? 0.4468 0.4538 0.4783 -0.0129 0.0210 0.0090 506 MAN A C2 6687 C C3 . MAN G . ? 0.4122 0.4352 0.4775 -0.0185 0.0392 0.0231 506 MAN A C3 6688 C C4 . MAN G . ? 0.4141 0.4130 0.4800 -0.0470 0.0465 0.0181 506 MAN A C4 6689 C C5 . MAN G . ? 0.3966 0.4136 0.4760 -0.0366 0.0342 0.0060 506 MAN A C5 6690 C C6 . MAN G . ? 0.4071 0.3764 0.4690 0.0224 0.0280 0.0363 506 MAN A C6 6691 O O2 . MAN G . ? 0.5119 0.5041 0.5045 0.0078 0.0369 -0.0038 506 MAN A O2 6692 O O3 . MAN G . ? 0.4279 0.4847 0.4860 0.0263 0.0224 0.0547 506 MAN A O3 6693 O O4 . MAN G . ? 0.4578 0.4355 0.4836 -0.0421 0.0235 0.0303 506 MAN A O4 6694 O O5 . MAN G . ? 0.4251 0.4669 0.4664 -0.0461 0.0328 0.0380 506 MAN A O5 6695 O O6 . MAN G . ? 0.4605 0.4357 0.5004 0.0132 0.0332 0.0338 506 MAN A O6 6707 C C1 . NAG H . ? 0.2610 0.2284 0.2042 0.0130 -0.0320 0.0234 507 NAG A C1 6708 C C2 . NAG H . ? 0.2097 0.2411 0.2187 0.0153 -0.0289 0.0019 507 NAG A C2 6709 C C3 . NAG H . ? 0.2050 0.2861 0.2518 0.0236 -0.0037 0.0507 507 NAG A C3 6710 C C4 . NAG H . ? 0.2336 0.3077 0.2363 -0.0061 -0.0066 0.0545 507 NAG A C4 6711 C C5 . NAG H . ? 0.2429 0.2786 0.2268 0.0052 -0.0233 0.0448 507 NAG A C5 6712 C C6 . NAG H . ? 0.2757 0.2754 0.2791 0.0141 -0.0136 0.0496 507 NAG A C6 6713 C C7 . NAG H . ? 0.1894 0.2719 0.2564 -0.0059 -0.0396 0.0195 507 NAG A C7 6714 C C8 . NAG H . ? 0.2336 0.2563 0.2457 -0.0019 -0.0438 -0.0062 507 NAG A C8 6715 N N2 . NAG H . ? 0.1833 0.2359 0.2339 -0.0145 -0.0165 -0.0155 507 NAG A N2 6716 O O3 . NAG H . ? 0.2295 0.3088 0.3008 0.0446 0.0209 0.0645 507 NAG A O3 6717 O O4 . NAG H . ? 0.2635 0.3565 0.2424 -0.0351 -0.0032 0.0679 507 NAG A O4 6718 O O5 . NAG H . ? 0.2601 0.2619 0.2110 0.0227 -0.0055 0.0252 507 NAG A O5 6719 O O6 . NAG H . ? 0.3464 0.3191 0.3089 0.0304 -0.0174 0.0397 507 NAG A O6 6720 O O7 . NAG H . ? 0.2321 0.2767 0.2818 0.0138 -0.0535 0.0129 507 NAG A O7 6734 C C1 . MAN I . ? 0.4691 0.4758 0.4557 0.0005 0.0308 0.0502 508 MAN A C1 6735 C C2 . MAN I . ? 0.4633 0.4545 0.4673 -0.0069 0.0255 0.0483 508 MAN A C2 6736 C C3 . MAN I . ? 0.4497 0.4353 0.4754 -0.0104 0.0226 0.0236 508 MAN A C3 6737 C C4 . MAN I . ? 0.4222 0.4408 0.4752 -0.0014 0.0111 0.0115 508 MAN A C4 6738 C C5 . MAN I . ? 0.4281 0.4414 0.4641 -0.0059 0.0157 0.0035 508 MAN A C5 6739 C C6 . MAN I . ? 0.4260 0.4479 0.4572 -0.0083 -0.0045 0.0012 508 MAN A C6 6740 O O2 . MAN I . ? 0.5084 0.4759 0.4830 0.0208 0.0411 0.0654 508 MAN A O2 6741 O O3 . MAN I . ? 0.4906 0.4738 0.4913 -0.0237 0.0403 0.0233 508 MAN A O3 6742 O O4 . MAN I . ? 0.4492 0.5091 0.4940 -0.0031 0.0197 0.0272 508 MAN A O4 6743 O O5 . MAN I . ? 0.4659 0.4871 0.4644 0.0103 0.0328 0.0273 508 MAN A O5 6744 O O6 . MAN I . ? 0.4564 0.4812 0.4681 -0.0129 -0.0134 0.0259 508 MAN A O6 6756 C C1 . NAG J . ? 0.3206 0.3768 0.2717 -0.0508 -0.0109 0.0930 509 NAG A C1 6757 C C2 . NAG J . ? 0.3482 0.3763 0.2785 -0.0690 -0.0014 0.1065 509 NAG A C2 6758 C C3 . NAG J . ? 0.3507 0.4194 0.3238 -0.0710 0.0034 0.1359 509 NAG A C3 6759 C C4 . NAG J . ? 0.3383 0.4605 0.3545 -0.0827 0.0025 0.1309 509 NAG A C4 6760 C C5 . NAG J . ? 0.3316 0.4518 0.3517 -0.0659 0.0016 0.1142 509 NAG A C5 6761 C C6 . NAG J . ? 0.3745 0.4742 0.3780 -0.0494 0.0258 0.0998 509 NAG A C6 6762 C C7 . NAG J . ? 0.3364 0.2770 0.2334 -0.0293 -0.0399 0.0671 509 NAG A C7 6763 C C8 . NAG J . ? 0.3732 0.2916 0.2414 -0.0041 -0.0379 0.0412 509 NAG A C8 6764 N N2 . NAG J . ? 0.3522 0.3260 0.2511 -0.0560 -0.0344 0.0692 509 NAG A N2 6765 O O3 . NAG J . ? 0.3845 0.4430 0.3401 -0.0612 0.0098 0.1256 509 NAG A O3 6766 O O4 . NAG J . ? 0.3575 0.5293 0.3835 -0.1230 0.0110 0.1194 509 NAG A O4 6767 O O5 . NAG J . ? 0.3016 0.4231 0.3166 -0.0684 -0.0225 0.1039 509 NAG A O5 6768 O O6 . NAG J . ? 0.3984 0.5042 0.4045 -0.0062 0.0326 0.1043 509 NAG A O6 6769 O O7 . NAG J . ? 0.3653 0.3362 0.2193 -0.0640 -0.0279 0.0068 509 NAG A O7 6783 C C1 . FUC K . ? 0.4232 0.4187 0.4392 -0.0239 -0.0158 -0.0480 510 FUC A C1 6784 C C2 . FUC K . ? 0.4516 0.4065 0.4494 -0.0330 -0.0720 -0.0209 510 FUC A C2 6785 C C3 . FUC K . ? 0.4191 0.3681 0.4453 -0.0347 -0.1031 -0.0359 510 FUC A C3 6786 C C4 . FUC K . ? 0.4061 0.3485 0.4557 -0.0365 -0.0547 -0.0390 510 FUC A C4 6787 C C5 . FUC K . ? 0.4189 0.3588 0.4504 0.0304 -0.0340 -0.0245 510 FUC A C5 6788 C C6 . FUC K . ? 0.4374 0.3411 0.4672 0.0698 -0.0079 0.0001 510 FUC A C6 6789 O O2 . FUC K . ? 0.5097 0.4324 0.4799 -0.0162 -0.0613 0.0025 510 FUC A O2 6790 O O3 . FUC K . ? 0.4368 0.3757 0.4487 -0.0488 -0.1345 -0.0501 510 FUC A O3 6791 O O4 . FUC K . ? 0.3807 0.3913 0.4741 -0.0455 -0.0241 -0.0155 510 FUC A O4 6792 O O5 . FUC K . ? 0.4076 0.3620 0.4403 0.0466 -0.0104 -0.0240 510 FUC A O5 6804 C C1 . NAG L . ? 0.1716 0.4424 0.3206 0.0043 0.0013 -0.1189 511 NAG A C1 6805 C C2 . NAG L . ? 0.1847 0.4655 0.3267 -0.0151 0.0037 -0.1406 511 NAG A C2 6806 C C3 . NAG L . ? 0.1802 0.4431 0.3435 -0.0446 0.0113 -0.1390 511 NAG A C3 6807 C C4 . NAG L . ? 0.2562 0.4739 0.3790 -0.0674 -0.0021 -0.1192 511 NAG A C4 6808 C C5 . NAG L . ? 0.2555 0.4681 0.3740 -0.0154 0.0059 -0.1144 511 NAG A C5 6809 C C6 . NAG L . ? 0.3160 0.4671 0.3986 -0.0448 -0.0095 -0.1128 511 NAG A C6 6810 C C7 . NAG L . ? 0.2312 0.5137 0.3510 0.0124 -0.0164 -0.1235 511 NAG A C7 6811 C C8 . NAG L . ? 0.1773 0.5095 0.3689 0.0258 -0.0345 -0.1119 511 NAG A C8 6812 N N2 . NAG L . ? 0.1721 0.5347 0.3343 -0.0011 -0.0150 -0.1252 511 NAG A N2 6813 O O3 . NAG L . ? 0.2420 0.4495 0.3300 -0.0488 0.0231 -0.1425 511 NAG A O3 6814 O O4 . NAG L . ? 0.3643 0.4932 0.4416 -0.0702 0.0414 -0.1240 511 NAG A O4 6815 O O5 . NAG L . ? 0.2171 0.4860 0.3509 0.0368 -0.0173 -0.1018 511 NAG A O5 6816 O O6 . NAG L . ? 0.3816 0.4371 0.4168 -0.0480 0.0175 -0.0946 511 NAG A O6 6817 O O7 . NAG L . ? 0.3029 0.5095 0.3625 0.0120 -0.0074 -0.1125 511 NAG A O7 6830 C C1 . NAG M . ? 0.4886 0.5152 0.4982 -0.0735 0.0548 -0.0873 512 NAG A C1 6831 C C2 . NAG M . ? 0.5506 0.5468 0.5344 -0.0618 0.0519 -0.0448 512 NAG A C2 6832 C C3 . NAG M . ? 0.5852 0.5590 0.5534 -0.0499 0.0699 -0.0284 512 NAG A C3 6833 C C4 . NAG M . ? 0.5991 0.5522 0.5643 -0.0304 0.0865 -0.0261 512 NAG A C4 6834 C C5 . NAG M . ? 0.5729 0.5379 0.5469 -0.0379 0.0747 -0.0386 512 NAG A C5 6835 C C6 . NAG M . ? 0.6111 0.5489 0.5599 -0.0277 0.0786 -0.0162 512 NAG A C6 6836 C C7 . NAG M . ? 0.5858 0.6177 0.5698 -0.0268 0.0055 0.0122 512 NAG A C7 6837 C C8 . NAG M . ? 0.5886 0.6217 0.5744 -0.0186 -0.0040 0.0132 512 NAG A C8 6838 N N2 . NAG M . ? 0.5720 0.5748 0.5525 -0.0533 0.0395 -0.0159 512 NAG A N2 6839 O O3 . NAG M . ? 0.6012 0.5934 0.5612 -0.0498 0.0746 -0.0205 512 NAG A O3 6840 O O4 . NAG M . ? 0.6239 0.5589 0.5837 -0.0167 0.1014 -0.0291 512 NAG A O4 6841 O O5 . NAG M . ? 0.5200 0.5331 0.5164 -0.0591 0.0598 -0.0769 512 NAG A O5 6842 O O6 . NAG M . ? 0.6407 0.5807 0.5738 -0.0348 0.0769 -0.0113 512 NAG A O6 6843 O O7 . NAG M . ? 0.6175 0.6681 0.5861 -0.0222 0.0073 0.0234 512 NAG A O7 6858 N N . NO3 N . ? 0.3325 0.4332 0.4025 -0.0155 -0.1614 -0.0253 513 NO3 A N 6859 O O1 . NO3 N . ? 0.2960 0.3951 0.3905 0.0208 -0.1178 -0.0203 513 NO3 A O1 6860 O O2 . NO3 N . ? 0.3787 0.4622 0.4223 0.0029 -0.1338 0.0279 513 NO3 A O2 6861 O O3 . NO3 N . ? 0.4402 0.4665 0.4445 0.0367 -0.0447 -0.0330 513 NO3 A O3 6862 N N . NO3 O . ? 0.4657 0.5824 0.4310 0.1203 0.0854 -0.0413 514 NO3 A N 6863 O O1 . NO3 O . ? 0.4063 0.4619 0.3949 0.1341 0.0674 -0.0535 514 NO3 A O1 6864 O O2 . NO3 O . ? 0.5182 0.6193 0.4643 0.0770 0.0960 -0.0553 514 NO3 A O2 6865 O O3 . NO3 O . ? 0.4641 0.6206 0.4318 0.0885 0.0683 -0.0160 514 NO3 A O3 6866 C C1 . GOL P . ? 0.3904 0.3527 0.4471 -0.0174 -0.0115 -0.0242 515 GOL A C1 6867 O O1 . GOL P . ? 0.3919 0.4298 0.4479 -0.0065 -0.0105 -0.0357 515 GOL A O1 6868 C C2 . GOL P . ? 0.3885 0.3428 0.4533 0.0152 -0.0153 -0.0111 515 GOL A C2 6869 O O2 . GOL P . ? 0.3496 0.3374 0.4441 0.0436 -0.0602 0.0012 515 GOL A O2 6870 C C3 . GOL P . ? 0.4186 0.3578 0.4648 0.0212 0.0114 -0.0240 515 GOL A C3 6871 O O3 . GOL P . ? 0.4606 0.3206 0.4775 0.0023 0.0510 -0.0509 515 GOL A O3 # 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 ASP 1 9 ? ? ? A . n A 1 2 ARG 2 10 ? ? ? A . n A 1 3 HIS 3 11 ? ? ? A . n A 1 4 HIS 4 12 ? ? ? A . n A 1 5 HIS 5 13 ? ? ? A . n A 1 6 HIS 6 14 ? ? ? A . n A 1 7 HIS 7 15 ? ? ? A . n A 1 8 HIS 8 16 ? ? ? A . n A 1 9 LYS 9 17 ? ? ? A . n A 1 10 LEU 10 18 ? ? ? A . n A 1 11 GLN 11 19 ? ? ? A . n A 1 12 LEU 12 20 20 LEU LEU A . n A 1 13 GLY 13 21 21 GLY GLY A . n A 1 14 ARG 14 22 22 ARG ARG A . n A 1 15 PHE 15 23 23 PHE PHE A . n A 1 16 TRP 16 24 24 TRP TRP A . n A 1 17 HIS 17 25 25 HIS HIS A . n A 1 18 ILE 18 26 26 ILE ILE A . n A 1 19 SER 19 27 27 SER SER A . n A 1 20 ASP 20 28 28 ASP ASP A . n A 1 21 LEU 21 29 29 LEU LEU A . n A 1 22 HIS 22 30 30 HIS HIS A . n A 1 23 LEU 23 31 31 LEU LEU A . n A 1 24 ASP 24 32 32 ASP ASP A . n A 1 25 PRO 25 33 33 PRO PRO A . n A 1 26 ASN 26 34 34 ASN ASN A . n A 1 27 TYR 27 35 35 TYR TYR A . n A 1 28 THR 28 36 36 THR THR A . n A 1 29 VAL 29 37 37 VAL VAL A . n A 1 30 SER 30 38 38 SER SER A . n A 1 31 LYS 31 39 39 LYS LYS A . n A 1 32 ASP 32 40 40 ASP ASP A . n A 1 33 PRO 33 41 41 PRO PRO A . n A 1 34 LEU 34 42 42 LEU LEU A . n A 1 35 GLN 35 43 43 GLN GLN A . n A 1 36 VAL 36 44 44 VAL VAL A . n A 1 37 CYS 37 45 45 CYS CYS A . n A 1 38 PRO 38 46 46 PRO PRO A . n A 1 39 SER 39 47 47 SER SER A . n A 1 40 ALA 40 48 48 ALA ALA A . n A 1 41 GLY 41 49 49 GLY GLY A . n A 1 42 SER 42 50 50 SER SER A . n A 1 43 GLN 43 51 51 GLN GLN A . n A 1 44 PRO 44 52 52 PRO PRO A . n A 1 45 VAL 45 53 53 VAL VAL A . n A 1 46 LEU 46 54 54 LEU LEU A . n A 1 47 ASN 47 55 55 ASN ASN A . n A 1 48 ALA 48 56 56 ALA ALA A . n A 1 49 GLY 49 57 57 GLY GLY A . n A 1 50 PRO 50 58 58 PRO PRO A . n A 1 51 TRP 51 59 59 TRP TRP A . n A 1 52 GLY 52 60 60 GLY GLY A . n A 1 53 ASP 53 61 61 ASP ASP A . n A 1 54 TYR 54 62 62 TYR TYR A . n A 1 55 LEU 55 63 63 LEU LEU A . n A 1 56 CYS 56 64 64 CYS CYS A . n A 1 57 ASP 57 65 65 ASP ASP A . n A 1 58 SER 58 66 66 SER SER A . n A 1 59 PRO 59 67 67 PRO PRO A . n A 1 60 TRP 60 68 68 TRP TRP A . n A 1 61 ALA 61 69 69 ALA ALA A . n A 1 62 LEU 62 70 70 LEU LEU A . n A 1 63 ILE 63 71 71 ILE ILE A . n A 1 64 ASN 64 72 72 ASN ASN A . n A 1 65 SER 65 73 73 SER SER A . n A 1 66 SER 66 74 74 SER SER A . n A 1 67 LEU 67 75 75 LEU LEU A . n A 1 68 TYR 68 76 76 TYR TYR A . n A 1 69 ALA 69 77 77 ALA ALA A . n A 1 70 MET 70 78 78 MET MET A . n A 1 71 LYS 71 79 79 LYS LYS A . n A 1 72 GLU 72 80 80 GLU GLU A . n A 1 73 ILE 73 81 81 ILE ILE A . n A 1 74 GLU 74 82 82 GLU GLU A . n A 1 75 PRO 75 83 83 PRO PRO A . n A 1 76 LYS 76 84 84 LYS LYS A . n A 1 77 PRO 77 85 85 PRO PRO A . n A 1 78 ASP 78 86 86 ASP ASP A . n A 1 79 PHE 79 87 87 PHE PHE A . n A 1 80 ILE 80 88 88 ILE ILE A . n A 1 81 LEU 81 89 89 LEU LEU A . n A 1 82 TRP 82 90 90 TRP TRP A . n A 1 83 THR 83 91 91 THR THR A . n A 1 84 GLY 84 92 92 GLY GLY A . n A 1 85 ASP 85 93 93 ASP ASP A . n A 1 86 ASP 86 94 94 ASP ASP A . n A 1 87 THR 87 95 95 THR THR A . n A 1 88 PRO 88 96 96 PRO PRO A . n A 1 89 HIS 89 97 97 HIS HIS A . n A 1 90 VAL 90 98 98 VAL VAL A . n A 1 91 PRO 91 99 99 PRO PRO A . n A 1 92 ASN 92 100 100 ASN ASN A . n A 1 93 GLU 93 101 101 GLU GLU A . n A 1 94 SER 94 102 102 SER SER A . n A 1 95 LEU 95 103 103 LEU LEU A . n A 1 96 GLY 96 104 104 GLY GLY A . n A 1 97 GLU 97 105 105 GLU GLU A . n A 1 98 ALA 98 106 106 ALA ALA A . n A 1 99 ALA 99 107 107 ALA ALA A . n A 1 100 VAL 100 108 108 VAL VAL A . n A 1 101 LEU 101 109 109 LEU LEU A . n A 1 102 ALA 102 110 110 ALA ALA A . n A 1 103 ILE 103 111 111 ILE ILE A . n A 1 104 VAL 104 112 112 VAL VAL A . n A 1 105 GLU 105 113 113 GLU GLU A . n A 1 106 ARG 106 114 114 ARG ARG A . n A 1 107 LEU 107 115 115 LEU LEU A . n A 1 108 THR 108 116 116 THR THR A . n A 1 109 ASN 109 117 117 ASN ASN A . n A 1 110 LEU 110 118 118 LEU LEU A . n A 1 111 ILE 111 119 119 ILE ILE A . n A 1 112 LYS 112 120 120 LYS LYS A . n A 1 113 GLU 113 121 121 GLU GLU A . n A 1 114 VAL 114 122 122 VAL VAL A . n A 1 115 PHE 115 123 123 PHE PHE A . n A 1 116 PRO 116 124 124 PRO PRO A . n A 1 117 ASP 117 125 125 ASP ASP A . n A 1 118 THR 118 126 126 THR THR A . n A 1 119 LYS 119 127 127 LYS LYS A . n A 1 120 VAL 120 128 128 VAL VAL A . n A 1 121 TYR 121 129 129 TYR TYR A . n A 1 122 ALA 122 130 130 ALA ALA A . n A 1 123 ALA 123 131 131 ALA ALA A . n A 1 124 LEU 124 132 132 LEU LEU A . n A 1 125 GLY 125 133 133 GLY GLY A . n A 1 126 ASN 126 134 134 ASN ASN A . n A 1 127 HIS 127 135 135 HIS HIS A . n A 1 128 ASP 128 136 136 ASP ASP A . n A 1 129 PHE 129 137 137 PHE PHE A . n A 1 130 HIS 130 138 138 HIS HIS A . n A 1 131 PRO 131 139 139 PRO PRO A . n A 1 132 LYS 132 140 140 LYS LYS A . n A 1 133 ASN 133 141 141 ASN ASN A . n A 1 134 GLN 134 142 142 GLN GLN A . n A 1 135 PHE 135 143 143 PHE PHE A . n A 1 136 PRO 136 144 144 PRO PRO A . n A 1 137 ALA 137 145 145 ALA ALA A . n A 1 138 GLN 138 146 146 GLN GLN A . n A 1 139 SER 139 147 147 SER SER A . n A 1 140 ASN 140 148 148 ASN ASN A . n A 1 141 ARG 141 149 149 ARG ARG A . n A 1 142 ILE 142 150 150 ILE ILE A . n A 1 143 TYR 143 151 151 TYR TYR A . n A 1 144 ASN 144 152 152 ASN ASN A . n A 1 145 GLN 145 153 153 GLN GLN A . n A 1 146 VAL 146 154 154 VAL VAL A . n A 1 147 ALA 147 155 155 ALA ALA A . n A 1 148 GLU 148 156 156 GLU GLU A . n A 1 149 LEU 149 157 157 LEU LEU A . n A 1 150 TRP 150 158 158 TRP TRP A . n A 1 151 ARG 151 159 159 ARG ARG A . n A 1 152 PRO 152 160 160 PRO PRO A . n A 1 153 TRP 153 161 161 TRP TRP A . n A 1 154 LEU 154 162 162 LEU LEU A . n A 1 155 SER 155 163 163 SER SER A . n A 1 156 ASN 156 164 164 ASN ASN A . n A 1 157 GLU 157 165 165 GLU GLU A . n A 1 158 SER 158 166 166 SER SER A . n A 1 159 TYR 159 167 167 TYR TYR A . n A 1 160 ALA 160 168 168 ALA ALA A . n A 1 161 LEU 161 169 169 LEU LEU A . n A 1 162 PHE 162 170 170 PHE PHE A . n A 1 163 LYS 163 171 171 LYS LYS A . n A 1 164 ARG 164 172 172 ARG ARG A . n A 1 165 GLY 165 173 173 GLY GLY A . n A 1 166 ALA 166 174 174 ALA ALA A . n A 1 167 PHE 167 175 175 PHE PHE A . n A 1 168 TYR 168 176 176 TYR TYR A . n A 1 169 SER 169 177 177 SER SER A . n A 1 170 GLU 170 178 178 GLU GLU A . n A 1 171 LYS 171 179 179 LYS LYS A . n A 1 172 LEU 172 180 180 LEU LEU A . n A 1 173 PRO 173 181 181 PRO PRO A . n A 1 174 GLY 174 182 182 GLY GLY A . n A 1 175 PRO 175 183 183 PRO PRO A . n A 1 176 SER 176 184 184 SER SER A . n A 1 177 ARG 177 185 185 ARG ARG A . n A 1 178 ALA 178 186 186 ALA ALA A . n A 1 179 GLY 179 187 187 GLY GLY A . n A 1 180 ARG 180 188 188 ARG ARG A . n A 1 181 VAL 181 189 189 VAL VAL A . n A 1 182 VAL 182 190 190 VAL VAL A . n A 1 183 VAL 183 191 191 VAL VAL A . n A 1 184 LEU 184 192 192 LEU LEU A . n A 1 185 ASN 185 193 193 ASN ASN A . n A 1 186 THR 186 194 194 THR THR A . n A 1 187 ASN 187 195 195 ASN ASN A . n A 1 188 LEU 188 196 196 LEU LEU A . n A 1 189 TYR 189 197 197 TYR TYR A . n A 1 190 TYR 190 198 198 TYR TYR A . n A 1 191 SER 191 199 199 SER SER A . n A 1 192 ASN 192 200 200 ASN ASN A . n A 1 193 ASN 193 201 201 ASN ASN A . n A 1 194 GLU 194 202 202 GLU GLU A . n A 1 195 GLN 195 203 203 GLN GLN A . n A 1 196 THR 196 204 204 THR THR A . n A 1 197 ALA 197 205 205 ALA ALA A . n A 1 198 GLY 198 206 206 GLY GLY A . n A 1 199 MET 199 207 207 MET MET A . n A 1 200 ALA 200 208 208 ALA ALA A . n A 1 201 ASP 201 209 209 ASP ASP A . n A 1 202 PRO 202 210 210 PRO PRO A . n A 1 203 GLY 203 211 211 GLY GLY A . n A 1 204 GLU 204 212 212 GLU GLU A . n A 1 205 GLN 205 213 213 GLN GLN A . n A 1 206 PHE 206 214 214 PHE PHE A . n A 1 207 ARG 207 215 215 ARG ARG A . n A 1 208 TRP 208 216 216 TRP TRP A . n A 1 209 LEU 209 217 217 LEU LEU A . n A 1 210 GLY 210 218 218 GLY GLY A . n A 1 211 ASP 211 219 219 ASP ASP A . n A 1 212 VAL 212 220 220 VAL VAL A . n A 1 213 LEU 213 221 221 LEU LEU A . n A 1 214 SER 214 222 222 SER SER A . n A 1 215 ASN 215 223 223 ASN ASN A . n A 1 216 ALA 216 224 224 ALA ALA A . n A 1 217 SER 217 225 225 SER SER A . n A 1 218 ARG 218 226 226 ARG ARG A . n A 1 219 ASP 219 227 227 ASP ASP A . n A 1 220 GLY 220 228 228 GLY GLY A . n A 1 221 GLU 221 229 229 GLU GLU A . n A 1 222 MET 222 230 230 MET MET A . n A 1 223 VAL 223 231 231 VAL VAL A . n A 1 224 TYR 224 232 232 TYR TYR A . n A 1 225 VAL 225 233 233 VAL VAL A . n A 1 226 ILE 226 234 234 ILE ILE A . n A 1 227 GLY 227 235 235 GLY GLY A . n A 1 228 HIS 228 236 236 HIS HIS A . n A 1 229 VAL 229 237 237 VAL VAL A . n A 1 230 PRO 230 238 238 PRO PRO A . n A 1 231 PRO 231 239 239 PRO PRO A . n A 1 232 GLY 232 240 240 GLY GLY A . n A 1 233 PHE 233 241 241 PHE PHE A . n A 1 234 PHE 234 242 242 PHE PHE A . n A 1 235 GLU 235 243 243 GLU GLU A . n A 1 236 LYS 236 244 244 LYS LYS A . n A 1 237 THR 237 245 245 THR THR A . n A 1 238 GLN 238 246 246 GLN GLN A . n A 1 239 ASN 239 247 247 ASN ASN A . n A 1 240 LYS 240 248 248 LYS LYS A . n A 1 241 ALA 241 249 249 ALA ALA A . n A 1 242 TRP 242 250 250 TRP TRP A . n A 1 243 PHE 243 251 251 PHE PHE A . n A 1 244 ARG 244 252 252 ARG ARG A . n A 1 245 GLU 245 253 253 GLU GLU A . n A 1 246 SER 246 254 254 SER SER A . n A 1 247 PHE 247 255 255 PHE PHE A . n A 1 248 ASN 248 256 256 ASN ASN A . n A 1 249 GLU 249 257 257 GLU GLU A . n A 1 250 GLU 250 258 258 GLU GLU A . n A 1 251 TYR 251 259 259 TYR TYR A . n A 1 252 LEU 252 260 260 LEU LEU A . n A 1 253 LYS 253 261 261 LYS LYS A . n A 1 254 VAL 254 262 262 VAL VAL A . n A 1 255 ILE 255 263 263 ILE ILE A . n A 1 256 GLN 256 264 264 GLN GLN A . n A 1 257 LYS 257 265 265 LYS LYS A . n A 1 258 HIS 258 266 266 HIS HIS A . n A 1 259 HIS 259 267 267 HIS HIS A . n A 1 260 ARG 260 268 268 ARG ARG A . n A 1 261 VAL 261 269 269 VAL VAL A . n A 1 262 ILE 262 270 270 ILE ILE A . n A 1 263 ALA 263 271 271 ALA ALA A . n A 1 264 GLY 264 272 272 GLY GLY A . n A 1 265 GLN 265 273 273 GLN GLN A . n A 1 266 PHE 266 274 274 PHE PHE A . n A 1 267 PHE 267 275 275 PHE PHE A . n A 1 268 GLY 268 276 276 GLY GLY A . n A 1 269 HIS 269 277 277 HIS HIS A . n A 1 270 HIS 270 278 278 HIS HIS A . n A 1 271 HIS 271 279 279 HIS HIS A . n A 1 272 THR 272 280 280 THR THR A . n A 1 273 ASP 273 281 281 ASP ASP A . n A 1 274 SER 274 282 282 SER SER A . n A 1 275 PHE 275 283 283 PHE PHE A . n A 1 276 ARG 276 284 284 ARG ARG A . n A 1 277 MET 277 285 285 MET MET A . n A 1 278 PHE 278 286 286 PHE PHE A . n A 1 279 TYR 279 287 287 TYR TYR A . n A 1 280 ASP 280 288 288 ASP ASP A . n A 1 281 ASN 281 289 289 ASN ASN A . n A 1 282 THR 282 290 290 THR THR A . n A 1 283 GLY 283 291 291 GLY GLY A . n A 1 284 ALA 284 292 292 ALA ALA A . n A 1 285 PRO 285 293 293 PRO PRO A . n A 1 286 ILE 286 294 294 ILE ILE A . n A 1 287 ASN 287 295 295 ASN ASN A . n A 1 288 VAL 288 296 296 VAL VAL A . n A 1 289 MET 289 297 297 MET MET A . n A 1 290 PHE 290 298 298 PHE PHE A . n A 1 291 LEU 291 299 299 LEU LEU A . n A 1 292 THR 292 300 300 THR THR A . n A 1 293 PRO 293 301 301 PRO PRO A . n A 1 294 GLY 294 302 302 GLY GLY A . n A 1 295 VAL 295 303 303 VAL VAL A . n A 1 296 THR 296 304 304 THR THR A . n A 1 297 PRO 297 305 305 PRO PRO A . n A 1 298 TRP 298 306 306 TRP TRP A . n A 1 299 LYS 299 307 307 LYS LYS A . n A 1 300 THR 300 308 308 THR THR A . n A 1 301 THR 301 309 309 THR THR A . n A 1 302 LEU 302 310 310 LEU LEU A . n A 1 303 PRO 303 311 311 PRO PRO A . n A 1 304 GLY 304 312 312 GLY GLY A . n A 1 305 VAL 305 313 313 VAL VAL A . n A 1 306 VAL 306 314 314 VAL VAL A . n A 1 307 ASP 307 315 315 ASP ASP A . n A 1 308 GLY 308 316 316 GLY GLY A . n A 1 309 ALA 309 317 317 ALA ALA A . n A 1 310 ASN 310 318 318 ASN ASN A . n A 1 311 ASN 311 319 319 ASN ASN A . n A 1 312 PRO 312 320 320 PRO PRO A . n A 1 313 GLY 313 321 321 GLY GLY A . n A 1 314 ILE 314 322 322 ILE ILE A . n A 1 315 ARG 315 323 323 ARG ARG A . n A 1 316 ILE 316 324 324 ILE ILE A . n A 1 317 PHE 317 325 325 PHE PHE A . n A 1 318 GLU 318 326 326 GLU GLU A . n A 1 319 TYR 319 327 327 TYR TYR A . n A 1 320 ASP 320 328 328 ASP ASP A . n A 1 321 ARG 321 329 329 ARG ARG A . n A 1 322 ALA 322 330 330 ALA ALA A . n A 1 323 THR 323 331 331 THR THR A . n A 1 324 LEU 324 332 332 LEU LEU A . n A 1 325 ASN 325 333 333 ASN ASN A . n A 1 326 LEU 326 334 334 LEU LEU A . n A 1 327 LYS 327 335 335 LYS LYS A . n A 1 328 ASP 328 336 336 ASP ASP A . n A 1 329 LEU 329 337 337 LEU LEU A . n A 1 330 VAL 330 338 338 VAL VAL A . n A 1 331 THR 331 339 339 THR THR A . n A 1 332 TYR 332 340 340 TYR TYR A . n A 1 333 PHE 333 341 341 PHE PHE A . n A 1 334 LEU 334 342 342 LEU LEU A . n A 1 335 ASN 335 343 343 ASN ASN A . n A 1 336 LEU 336 344 344 LEU LEU A . n A 1 337 ARG 337 345 345 ARG ARG A . n A 1 338 GLN 338 346 346 GLN GLN A . n A 1 339 ALA 339 347 347 ALA ALA A . n A 1 340 ASN 340 348 348 ASN ASN A . n A 1 341 VAL 341 349 349 VAL VAL A . n A 1 342 GLN 342 350 350 GLN GLN A . n A 1 343 GLU 343 351 351 GLU GLU A . n A 1 344 THR 344 352 352 THR THR A . n A 1 345 PRO 345 353 353 PRO PRO A . n A 1 346 ARG 346 354 354 ARG ARG A . n A 1 347 TRP 347 355 355 TRP TRP A . n A 1 348 GLU 348 356 356 GLU GLU A . n A 1 349 GLN 349 357 357 GLN GLN A . n A 1 350 GLU 350 358 358 GLU GLU A . n A 1 351 TYR 351 359 359 TYR TYR A . n A 1 352 ARG 352 360 360 ARG ARG A . n A 1 353 LEU 353 361 361 LEU LEU A . n A 1 354 THR 354 362 362 THR THR A . n A 1 355 GLU 355 363 363 GLU GLU A . n A 1 356 ALA 356 364 364 ALA ALA A . n A 1 357 TYR 357 365 365 TYR TYR A . n A 1 358 GLN 358 366 366 GLN GLN A . n A 1 359 VAL 359 367 367 VAL VAL A . n A 1 360 PRO 360 368 368 PRO PRO A . n A 1 361 ASP 361 369 369 ASP ASP A . n A 1 362 ALA 362 370 370 ALA ALA A . n A 1 363 SER 363 371 371 SER SER A . n A 1 364 VAL 364 372 372 VAL VAL A . n A 1 365 SER 365 373 373 SER SER A . n A 1 366 SER 366 374 374 SER SER A . n A 1 367 MET 367 375 375 MET MET A . n A 1 368 HIS 368 376 376 HIS HIS A . n A 1 369 THR 369 377 377 THR THR A . n A 1 370 ALA 370 378 378 ALA ALA A . n A 1 371 LEU 371 379 379 LEU LEU A . n A 1 372 THR 372 380 380 THR THR A . n A 1 373 ARG 373 381 381 ARG ARG A . n A 1 374 ILE 374 382 382 ILE ILE A . n A 1 375 ALA 375 383 383 ALA ALA A . n A 1 376 SER 376 384 384 SER SER A . n A 1 377 GLU 377 385 385 GLU GLU A . n A 1 378 PRO 378 386 386 PRO PRO A . n A 1 379 HIS 379 387 387 HIS HIS A . n A 1 380 ILE 380 388 388 ILE ILE A . n A 1 381 LEU 381 389 389 LEU LEU A . n A 1 382 GLN 382 390 390 GLN GLN A . n A 1 383 ARG 383 391 391 ARG ARG A . n A 1 384 TYR 384 392 392 TYR TYR A . n A 1 385 TYR 385 393 393 TYR TYR A . n A 1 386 VAL 386 394 394 VAL VAL A . n A 1 387 TYR 387 395 395 TYR TYR A . n A 1 388 ASN 388 396 396 ASN ASN A . n A 1 389 SER 389 397 397 SER SER A . n A 1 390 VAL 390 398 398 VAL VAL A . n A 1 391 SER 391 399 399 SER SER A . n A 1 392 TYR 392 400 400 TYR TYR A . n A 1 393 ASN 393 401 401 ASN ASN A . n A 1 394 HIS 394 402 402 HIS HIS A . n A 1 395 LEU 395 403 403 LEU LEU A . n A 1 396 THR 396 404 404 THR THR A . n A 1 397 CYS 397 405 405 CYS CYS A . n A 1 398 GLU 398 406 406 GLU GLU A . n A 1 399 ASP 399 407 407 ASP ASP A . n A 1 400 SER 400 408 408 SER SER A . n A 1 401 CYS 401 409 409 CYS CYS A . n A 1 402 ARG 402 410 410 ARG ARG A . n A 1 403 ILE 403 411 411 ILE ILE A . n A 1 404 GLU 404 412 412 GLU GLU A . n A 1 405 HIS 405 413 413 HIS HIS A . n A 1 406 VAL 406 414 414 VAL VAL A . n A 1 407 CYS 407 415 415 CYS CYS A . n A 1 408 ALA 408 416 416 ALA ALA A . n A 1 409 ILE 409 417 417 ILE ILE A . n A 1 410 GLN 410 418 418 GLN GLN A . n A 1 411 HIS 411 419 419 HIS HIS A . n A 1 412 VAL 412 420 420 VAL VAL A . n A 1 413 ALA 413 421 421 ALA ALA A . n A 1 414 PHE 414 422 422 PHE PHE A . n A 1 415 ASN 415 423 423 ASN ASN A . n A 1 416 THR 416 424 424 THR THR A . n A 1 417 TYR 417 425 425 TYR TYR A . n A 1 418 ALA 418 426 426 ALA ALA A . n A 1 419 THR 419 427 427 THR THR A . n A 1 420 CYS 420 428 428 CYS CYS A . n A 1 421 LEU 421 429 429 LEU LEU A . n A 1 422 HIS 422 430 430 HIS HIS A . n A 1 423 GLY 423 431 431 GLY GLY A . n A 1 424 LEU 424 432 ? ? ? A . n A 1 425 GLY 425 433 ? ? ? A . n A 1 426 ALA 426 434 ? ? ? A . n A 1 427 LYS 427 435 ? ? ? 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 ZN 1 501 1 ZN ZN A . C 2 ZN 1 502 2 ZN ZN A . D 3 NAG 1 503 1 NAG NAG A . E 3 NAG 2 504 5 NAG NAG A . F 4 BMA 1 505 1 BMA BMA A . G 5 MAN 2 506 1 MAN MAN A . H 3 NAG 3 507 2 NAG NAG A . I 5 MAN 4 508 2 MAN MAN A . J 3 NAG 5 509 3 NAG NAG A . K 6 FUC 1 510 1 FUC FUC A . L 3 NAG 2 511 4 NAG NAG A . M 3 NAG 3 512 6 NAG NAG A . N 7 NO3 1 513 1 NO3 NO3 A . O 7 NO3 1 514 2 NO3 NO3 A . P 8 GOL 1 515 1 GOL GOL A . Q 9 HOH 1 601 322 HOH HOH A . Q 9 HOH 2 602 401 HOH HOH A . Q 9 HOH 3 603 178 HOH HOH A . Q 9 HOH 4 604 286 HOH HOH A . Q 9 HOH 5 605 275 HOH HOH A . Q 9 HOH 6 606 411 HOH HOH A . Q 9 HOH 7 607 263 HOH HOH A . Q 9 HOH 8 608 219 HOH HOH A . Q 9 HOH 9 609 259 HOH HOH A . Q 9 HOH 10 610 464 HOH HOH A . Q 9 HOH 11 611 162 HOH HOH A . Q 9 HOH 12 612 208 HOH HOH A . Q 9 HOH 13 613 1 HOH HOH A . Q 9 HOH 14 614 242 HOH HOH A . Q 9 HOH 15 615 349 HOH HOH A . Q 9 HOH 16 616 155 HOH HOH A . Q 9 HOH 17 617 317 HOH HOH A . Q 9 HOH 18 618 161 HOH HOH A . Q 9 HOH 19 619 402 HOH HOH A . Q 9 HOH 20 620 489 HOH HOH A . Q 9 HOH 21 621 470 HOH HOH A . Q 9 HOH 22 622 340 HOH HOH A . Q 9 HOH 23 623 234 HOH HOH A . Q 9 HOH 24 624 410 HOH HOH A . Q 9 HOH 25 625 114 HOH HOH A . Q 9 HOH 26 626 433 HOH HOH A . Q 9 HOH 27 627 348 HOH HOH A . Q 9 HOH 28 628 475 HOH HOH A . Q 9 HOH 29 629 292 HOH HOH A . Q 9 HOH 30 630 55 HOH HOH A . Q 9 HOH 31 631 413 HOH HOH A . Q 9 HOH 32 632 30 HOH HOH A . Q 9 HOH 33 633 404 HOH HOH A . Q 9 HOH 34 634 197 HOH HOH A . Q 9 HOH 35 635 371 HOH HOH A . Q 9 HOH 36 636 332 HOH HOH A . Q 9 HOH 37 637 352 HOH HOH A . Q 9 HOH 38 638 460 HOH HOH A . Q 9 HOH 39 639 100 HOH HOH A . Q 9 HOH 40 640 478 HOH HOH A . Q 9 HOH 41 641 363 HOH HOH A . Q 9 HOH 42 642 118 HOH HOH A . Q 9 HOH 43 643 339 HOH HOH A . Q 9 HOH 44 644 326 HOH HOH A . Q 9 HOH 45 645 418 HOH HOH A . Q 9 HOH 46 646 450 HOH HOH A . Q 9 HOH 47 647 474 HOH HOH A . Q 9 HOH 48 648 172 HOH HOH A . Q 9 HOH 49 649 485 HOH HOH A . Q 9 HOH 50 650 366 HOH HOH A . Q 9 HOH 51 651 151 HOH HOH A . Q 9 HOH 52 652 12 HOH HOH A . Q 9 HOH 53 653 403 HOH HOH A . Q 9 HOH 54 654 24 HOH HOH A . Q 9 HOH 55 655 150 HOH HOH A . Q 9 HOH 56 656 394 HOH HOH A . Q 9 HOH 57 657 358 HOH HOH A . Q 9 HOH 58 658 196 HOH HOH A . Q 9 HOH 59 659 337 HOH HOH A . Q 9 HOH 60 660 265 HOH HOH A . Q 9 HOH 61 661 169 HOH HOH A . Q 9 HOH 62 662 373 HOH HOH A . Q 9 HOH 63 663 261 HOH HOH A . Q 9 HOH 64 664 15 HOH HOH A . Q 9 HOH 65 665 177 HOH HOH A . Q 9 HOH 66 666 447 HOH HOH A . Q 9 HOH 67 667 294 HOH HOH A . Q 9 HOH 68 668 228 HOH HOH A . Q 9 HOH 69 669 468 HOH HOH A . Q 9 HOH 70 670 147 HOH HOH A . Q 9 HOH 71 671 63 HOH HOH A . Q 9 HOH 72 672 190 HOH HOH A . Q 9 HOH 73 673 68 HOH HOH A . Q 9 HOH 74 674 199 HOH HOH A . Q 9 HOH 75 675 33 HOH HOH A . Q 9 HOH 76 676 107 HOH HOH A . Q 9 HOH 77 677 167 HOH HOH A . Q 9 HOH 78 678 59 HOH HOH A . Q 9 HOH 79 679 115 HOH HOH A . Q 9 HOH 80 680 10 HOH HOH A . Q 9 HOH 81 681 76 HOH HOH A . Q 9 HOH 82 682 27 HOH HOH A . Q 9 HOH 83 683 351 HOH HOH A . Q 9 HOH 84 684 183 HOH HOH A . Q 9 HOH 85 685 138 HOH HOH A . Q 9 HOH 86 686 93 HOH HOH A . Q 9 HOH 87 687 18 HOH HOH A . Q 9 HOH 88 688 256 HOH HOH A . Q 9 HOH 89 689 143 HOH HOH A . Q 9 HOH 90 690 171 HOH HOH A . Q 9 HOH 91 691 84 HOH HOH A . Q 9 HOH 92 692 299 HOH HOH A . Q 9 HOH 93 693 221 HOH HOH A . Q 9 HOH 94 694 108 HOH HOH A . Q 9 HOH 95 695 230 HOH HOH A . Q 9 HOH 96 696 251 HOH HOH A . Q 9 HOH 97 697 22 HOH HOH A . Q 9 HOH 98 698 209 HOH HOH A . Q 9 HOH 99 699 193 HOH HOH A . Q 9 HOH 100 700 370 HOH HOH A . Q 9 HOH 101 701 43 HOH HOH A . Q 9 HOH 102 702 456 HOH HOH A . Q 9 HOH 103 703 335 HOH HOH A . Q 9 HOH 104 704 86 HOH HOH A . Q 9 HOH 105 705 53 HOH HOH A . Q 9 HOH 106 706 216 HOH HOH A . Q 9 HOH 107 707 35 HOH HOH A . Q 9 HOH 108 708 272 HOH HOH A . Q 9 HOH 109 709 483 HOH HOH A . Q 9 HOH 110 710 384 HOH HOH A . Q 9 HOH 111 711 293 HOH HOH A . Q 9 HOH 112 712 127 HOH HOH A . Q 9 HOH 113 713 156 HOH HOH A . Q 9 HOH 114 714 102 HOH HOH A . Q 9 HOH 115 715 146 HOH HOH A . Q 9 HOH 116 716 91 HOH HOH A . Q 9 HOH 117 717 163 HOH HOH A . Q 9 HOH 118 718 3 HOH HOH A . Q 9 HOH 119 719 325 HOH HOH A . Q 9 HOH 120 720 149 HOH HOH A . Q 9 HOH 121 721 135 HOH HOH A . Q 9 HOH 122 722 77 HOH HOH A . Q 9 HOH 123 723 38 HOH HOH A . Q 9 HOH 124 724 235 HOH HOH A . Q 9 HOH 125 725 295 HOH HOH A . Q 9 HOH 126 726 302 HOH HOH A . Q 9 HOH 127 727 41 HOH HOH A . Q 9 HOH 128 728 52 HOH HOH A . Q 9 HOH 129 729 334 HOH HOH A . Q 9 HOH 130 730 195 HOH HOH A . Q 9 HOH 131 731 424 HOH HOH A . Q 9 HOH 132 732 123 HOH HOH A . Q 9 HOH 133 733 355 HOH HOH A . Q 9 HOH 134 734 95 HOH HOH A . Q 9 HOH 135 735 7 HOH HOH A . Q 9 HOH 136 736 281 HOH HOH A . Q 9 HOH 137 737 204 HOH HOH A . Q 9 HOH 138 738 94 HOH HOH A . Q 9 HOH 139 739 284 HOH HOH A . Q 9 HOH 140 740 17 HOH HOH A . Q 9 HOH 141 741 305 HOH HOH A . Q 9 HOH 142 742 89 HOH HOH A . Q 9 HOH 143 743 179 HOH HOH A . Q 9 HOH 144 744 6 HOH HOH A . Q 9 HOH 145 745 51 HOH HOH A . Q 9 HOH 146 746 70 HOH HOH A . Q 9 HOH 147 747 48 HOH HOH A . Q 9 HOH 148 748 26 HOH HOH A . Q 9 HOH 149 749 409 HOH HOH A . Q 9 HOH 150 750 297 HOH HOH A . Q 9 HOH 151 751 122 HOH HOH A . Q 9 HOH 152 752 389 HOH HOH A . Q 9 HOH 153 753 186 HOH HOH A . Q 9 HOH 154 754 260 HOH HOH A . Q 9 HOH 155 755 21 HOH HOH A . Q 9 HOH 156 756 248 HOH HOH A . Q 9 HOH 157 757 264 HOH HOH A . Q 9 HOH 158 758 47 HOH HOH A . Q 9 HOH 159 759 343 HOH HOH A . Q 9 HOH 160 760 20 HOH HOH A . Q 9 HOH 161 761 67 HOH HOH A . Q 9 HOH 162 762 381 HOH HOH A . Q 9 HOH 163 763 440 HOH HOH A . Q 9 HOH 164 764 69 HOH HOH A . Q 9 HOH 165 765 194 HOH HOH A . Q 9 HOH 166 766 372 HOH HOH A . Q 9 HOH 167 767 139 HOH HOH A . Q 9 HOH 168 768 189 HOH HOH A . Q 9 HOH 169 769 116 HOH HOH A . Q 9 HOH 170 770 213 HOH HOH A . Q 9 HOH 171 771 14 HOH HOH A . Q 9 HOH 172 772 25 HOH HOH A . Q 9 HOH 173 773 54 HOH HOH A . Q 9 HOH 174 774 8 HOH HOH A . Q 9 HOH 175 775 207 HOH HOH A . Q 9 HOH 176 776 111 HOH HOH A . Q 9 HOH 177 777 50 HOH HOH A . Q 9 HOH 178 778 112 HOH HOH A . Q 9 HOH 179 779 11 HOH HOH A . Q 9 HOH 180 780 82 HOH HOH A . Q 9 HOH 181 781 211 HOH HOH A . Q 9 HOH 182 782 5 HOH HOH A . Q 9 HOH 183 783 131 HOH HOH A . Q 9 HOH 184 784 99 HOH HOH A . Q 9 HOH 185 785 203 HOH HOH A . Q 9 HOH 186 786 428 HOH HOH A . Q 9 HOH 187 787 87 HOH HOH A . Q 9 HOH 188 788 342 HOH HOH A . Q 9 HOH 189 789 23 HOH HOH A . Q 9 HOH 190 790 105 HOH HOH A . Q 9 HOH 191 791 56 HOH HOH A . Q 9 HOH 192 792 229 HOH HOH A . Q 9 HOH 193 793 106 HOH HOH A . Q 9 HOH 194 794 31 HOH HOH A . Q 9 HOH 195 795 49 HOH HOH A . Q 9 HOH 196 796 19 HOH HOH A . Q 9 HOH 197 797 2 HOH HOH A . Q 9 HOH 198 798 400 HOH HOH A . Q 9 HOH 199 799 220 HOH HOH A . Q 9 HOH 200 800 362 HOH HOH A . Q 9 HOH 201 801 273 HOH HOH A . Q 9 HOH 202 802 165 HOH HOH A . Q 9 HOH 203 803 81 HOH HOH A . Q 9 HOH 204 804 145 HOH HOH A . Q 9 HOH 205 805 252 HOH HOH A . Q 9 HOH 206 806 438 HOH HOH A . Q 9 HOH 207 807 380 HOH HOH A . Q 9 HOH 208 808 78 HOH HOH A . Q 9 HOH 209 809 29 HOH HOH A . Q 9 HOH 210 810 426 HOH HOH A . Q 9 HOH 211 811 176 HOH HOH A . Q 9 HOH 212 812 192 HOH HOH A . Q 9 HOH 213 813 274 HOH HOH A . Q 9 HOH 214 814 290 HOH HOH A . Q 9 HOH 215 815 113 HOH HOH A . Q 9 HOH 216 816 223 HOH HOH A . Q 9 HOH 217 817 109 HOH HOH A . Q 9 HOH 218 818 57 HOH HOH A . Q 9 HOH 219 819 168 HOH HOH A . Q 9 HOH 220 820 39 HOH HOH A . Q 9 HOH 221 821 365 HOH HOH A . Q 9 HOH 222 822 79 HOH HOH A . Q 9 HOH 223 823 98 HOH HOH A . Q 9 HOH 224 824 344 HOH HOH A . Q 9 HOH 225 825 157 HOH HOH A . Q 9 HOH 226 826 83 HOH HOH A . Q 9 HOH 227 827 97 HOH HOH A . Q 9 HOH 228 828 62 HOH HOH A . Q 9 HOH 229 829 73 HOH HOH A . Q 9 HOH 230 830 430 HOH HOH A . Q 9 HOH 231 831 88 HOH HOH A . Q 9 HOH 232 832 429 HOH HOH A . Q 9 HOH 233 833 121 HOH HOH A . Q 9 HOH 234 834 369 HOH HOH A . Q 9 HOH 235 835 185 HOH HOH A . Q 9 HOH 236 836 34 HOH HOH A . Q 9 HOH 237 837 454 HOH HOH A . Q 9 HOH 238 838 276 HOH HOH A . Q 9 HOH 239 839 9 HOH HOH A . Q 9 HOH 240 840 13 HOH HOH A . Q 9 HOH 241 841 306 HOH HOH A . Q 9 HOH 242 842 159 HOH HOH A . Q 9 HOH 243 843 350 HOH HOH A . Q 9 HOH 244 844 436 HOH HOH A . Q 9 HOH 245 845 495 HOH HOH A . Q 9 HOH 246 846 486 HOH HOH A . Q 9 HOH 247 847 245 HOH HOH A . Q 9 HOH 248 848 236 HOH HOH A . Q 9 HOH 249 849 132 HOH HOH A . Q 9 HOH 250 850 46 HOH HOH A . Q 9 HOH 251 851 307 HOH HOH A . Q 9 HOH 252 852 291 HOH HOH A . Q 9 HOH 253 853 32 HOH HOH A . Q 9 HOH 254 854 201 HOH HOH A . Q 9 HOH 255 855 200 HOH HOH A . Q 9 HOH 256 856 258 HOH HOH A . Q 9 HOH 257 857 71 HOH HOH A . Q 9 HOH 258 858 368 HOH HOH A . Q 9 HOH 259 859 188 HOH HOH A . Q 9 HOH 260 860 174 HOH HOH A . Q 9 HOH 261 861 65 HOH HOH A . Q 9 HOH 262 862 225 HOH HOH A . Q 9 HOH 263 863 4 HOH HOH A . Q 9 HOH 264 864 311 HOH HOH A . Q 9 HOH 265 865 96 HOH HOH A . Q 9 HOH 266 866 16 HOH HOH A . Q 9 HOH 267 867 187 HOH HOH A . Q 9 HOH 268 868 184 HOH HOH A . Q 9 HOH 269 869 110 HOH HOH A . Q 9 HOH 270 870 247 HOH HOH A . Q 9 HOH 271 871 37 HOH HOH A . Q 9 HOH 272 872 92 HOH HOH A . Q 9 HOH 273 873 44 HOH HOH A . Q 9 HOH 274 874 36 HOH HOH A . Q 9 HOH 275 875 119 HOH HOH A . Q 9 HOH 276 876 58 HOH HOH A . Q 9 HOH 277 877 72 HOH HOH A . Q 9 HOH 278 878 74 HOH HOH A . Q 9 HOH 279 879 45 HOH HOH A . Q 9 HOH 280 880 120 HOH HOH A . Q 9 HOH 281 881 182 HOH HOH A . Q 9 HOH 282 882 226 HOH HOH A . Q 9 HOH 283 883 437 HOH HOH A . Q 9 HOH 284 884 379 HOH HOH A . Q 9 HOH 285 885 244 HOH HOH A . Q 9 HOH 286 886 202 HOH HOH A . Q 9 HOH 287 887 126 HOH HOH A . Q 9 HOH 288 888 477 HOH HOH A . Q 9 HOH 289 889 140 HOH HOH A . Q 9 HOH 290 890 191 HOH HOH A . Q 9 HOH 291 891 61 HOH HOH A . Q 9 HOH 292 892 125 HOH HOH A . Q 9 HOH 293 893 255 HOH HOH A . Q 9 HOH 294 894 181 HOH HOH A . Q 9 HOH 295 895 298 HOH HOH A . Q 9 HOH 296 896 136 HOH HOH A . Q 9 HOH 297 897 465 HOH HOH A . Q 9 HOH 298 898 393 HOH HOH A . Q 9 HOH 299 899 75 HOH HOH A . Q 9 HOH 300 900 249 HOH HOH A . Q 9 HOH 301 901 101 HOH HOH A . Q 9 HOH 302 902 198 HOH HOH A . Q 9 HOH 303 903 414 HOH HOH A . Q 9 HOH 304 904 206 HOH HOH A . Q 9 HOH 305 905 130 HOH HOH A . Q 9 HOH 306 906 66 HOH HOH A . Q 9 HOH 307 907 158 HOH HOH A . Q 9 HOH 308 908 341 HOH HOH A . Q 9 HOH 309 909 240 HOH HOH A . Q 9 HOH 310 910 141 HOH HOH A . Q 9 HOH 311 911 246 HOH HOH A . Q 9 HOH 312 912 134 HOH HOH A . Q 9 HOH 313 913 487 HOH HOH A . Q 9 HOH 314 914 407 HOH HOH A . Q 9 HOH 315 915 124 HOH HOH A . Q 9 HOH 316 916 278 HOH HOH A . Q 9 HOH 317 917 233 HOH HOH A . Q 9 HOH 318 918 356 HOH HOH A . Q 9 HOH 319 919 296 HOH HOH A . Q 9 HOH 320 920 303 HOH HOH A . Q 9 HOH 321 921 282 HOH HOH A . Q 9 HOH 322 922 254 HOH HOH A . Q 9 HOH 323 923 173 HOH HOH A . Q 9 HOH 324 924 142 HOH HOH A . Q 9 HOH 325 925 445 HOH HOH A . Q 9 HOH 326 926 391 HOH HOH A . Q 9 HOH 327 927 308 HOH HOH A . Q 9 HOH 328 928 28 HOH HOH A . Q 9 HOH 329 929 90 HOH HOH A . Q 9 HOH 330 930 85 HOH HOH A . Q 9 HOH 331 931 224 HOH HOH A . Q 9 HOH 332 932 154 HOH HOH A . Q 9 HOH 333 933 42 HOH HOH A . Q 9 HOH 334 934 269 HOH HOH A . Q 9 HOH 335 935 318 HOH HOH A . Q 9 HOH 336 936 472 HOH HOH A . Q 9 HOH 337 937 60 HOH HOH A . Q 9 HOH 338 938 170 HOH HOH A . Q 9 HOH 339 939 104 HOH HOH A . Q 9 HOH 340 940 388 HOH HOH A . Q 9 HOH 341 941 40 HOH HOH A . Q 9 HOH 342 942 425 HOH HOH A . Q 9 HOH 343 943 321 HOH HOH A . Q 9 HOH 344 944 309 HOH HOH A . Q 9 HOH 345 945 215 HOH HOH A . Q 9 HOH 346 946 153 HOH HOH A . Q 9 HOH 347 947 382 HOH HOH A . Q 9 HOH 348 948 144 HOH HOH A . Q 9 HOH 349 949 463 HOH HOH A . Q 9 HOH 350 950 166 HOH HOH A . Q 9 HOH 351 951 133 HOH HOH A . Q 9 HOH 352 952 455 HOH HOH A . Q 9 HOH 353 953 492 HOH HOH A . Q 9 HOH 354 954 301 HOH HOH A . Q 9 HOH 355 955 324 HOH HOH A . Q 9 HOH 356 956 345 HOH HOH A . Q 9 HOH 357 957 488 HOH HOH A . Q 9 HOH 358 958 390 HOH HOH A . Q 9 HOH 359 959 446 HOH HOH A . Q 9 HOH 360 960 164 HOH HOH A . Q 9 HOH 361 961 117 HOH HOH A . Q 9 HOH 362 962 239 HOH HOH A . Q 9 HOH 363 963 160 HOH HOH A . Q 9 HOH 364 964 482 HOH HOH A . Q 9 HOH 365 965 180 HOH HOH A . Q 9 HOH 366 966 398 HOH HOH A . Q 9 HOH 367 967 137 HOH HOH A . Q 9 HOH 368 968 64 HOH HOH A . Q 9 HOH 369 969 319 HOH HOH A . Q 9 HOH 370 970 268 HOH HOH A . Q 9 HOH 371 971 320 HOH HOH A . Q 9 HOH 372 972 434 HOH HOH A . Q 9 HOH 373 973 222 HOH HOH A . Q 9 HOH 374 974 364 HOH HOH A . Q 9 HOH 375 975 387 HOH HOH A . Q 9 HOH 376 976 493 HOH HOH A . Q 9 HOH 377 977 346 HOH HOH A . Q 9 HOH 378 978 128 HOH HOH A . Q 9 HOH 379 979 417 HOH HOH A . Q 9 HOH 380 980 473 HOH HOH A . Q 9 HOH 381 981 314 HOH HOH A . Q 9 HOH 382 982 484 HOH HOH A . Q 9 HOH 383 983 481 HOH HOH A . Q 9 HOH 384 984 451 HOH HOH A . Q 9 HOH 385 985 408 HOH HOH A . Q 9 HOH 386 986 469 HOH HOH A . Q 9 HOH 387 987 448 HOH HOH A . Q 9 HOH 388 988 396 HOH HOH A . Q 9 HOH 389 989 374 HOH HOH A . Q 9 HOH 390 990 496 HOH HOH A . Q 9 HOH 391 991 205 HOH HOH A . Q 9 HOH 392 992 283 HOH HOH A . Q 9 HOH 393 993 227 HOH HOH A . Q 9 HOH 394 994 257 HOH HOH A . Q 9 HOH 395 995 376 HOH HOH A . Q 9 HOH 396 996 304 HOH HOH A . Q 9 HOH 397 997 420 HOH HOH A . Q 9 HOH 398 998 479 HOH HOH A . Q 9 HOH 399 999 129 HOH HOH A . Q 9 HOH 400 1000 175 HOH HOH A . Q 9 HOH 401 1001 338 HOH HOH A . Q 9 HOH 402 1002 461 HOH HOH A . Q 9 HOH 403 1003 397 HOH HOH A . Q 9 HOH 404 1004 347 HOH HOH A . Q 9 HOH 405 1005 262 HOH HOH A . Q 9 HOH 406 1006 243 HOH HOH A . Q 9 HOH 407 1007 431 HOH HOH A . Q 9 HOH 408 1008 287 HOH HOH A . Q 9 HOH 409 1009 421 HOH HOH A . Q 9 HOH 410 1010 103 HOH HOH A . Q 9 HOH 411 1011 336 HOH HOH A . Q 9 HOH 412 1012 300 HOH HOH A . Q 9 HOH 413 1013 267 HOH HOH A . Q 9 HOH 414 1014 237 HOH HOH A . Q 9 HOH 415 1015 241 HOH HOH A . Q 9 HOH 416 1016 443 HOH HOH A . Q 9 HOH 417 1017 491 HOH HOH A . Q 9 HOH 418 1018 354 HOH HOH A . Q 9 HOH 419 1019 280 HOH HOH A . Q 9 HOH 420 1020 378 HOH HOH A . Q 9 HOH 421 1021 439 HOH HOH A . Q 9 HOH 422 1022 367 HOH HOH A . Q 9 HOH 423 1023 452 HOH HOH A . Q 9 HOH 424 1024 327 HOH HOH A . Q 9 HOH 425 1025 214 HOH HOH A . Q 9 HOH 426 1026 210 HOH HOH A . Q 9 HOH 427 1027 218 HOH HOH A . Q 9 HOH 428 1028 313 HOH HOH A . Q 9 HOH 429 1029 312 HOH HOH A . Q 9 HOH 430 1030 453 HOH HOH A . Q 9 HOH 431 1031 422 HOH HOH A . Q 9 HOH 432 1032 231 HOH HOH A . Q 9 HOH 433 1033 423 HOH HOH A . Q 9 HOH 434 1034 148 HOH HOH A . Q 9 HOH 435 1035 377 HOH HOH A . Q 9 HOH 436 1036 328 HOH HOH A . Q 9 HOH 437 1037 361 HOH HOH A . Q 9 HOH 438 1038 152 HOH HOH A . Q 9 HOH 439 1039 412 HOH HOH A . Q 9 HOH 440 1040 357 HOH HOH A . Q 9 HOH 441 1041 288 HOH HOH A . Q 9 HOH 442 1042 406 HOH HOH A . Q 9 HOH 443 1043 217 HOH HOH A . Q 9 HOH 444 1044 405 HOH HOH A . Q 9 HOH 445 1045 279 HOH HOH A . Q 9 HOH 446 1046 471 HOH HOH A . Q 9 HOH 447 1047 271 HOH HOH A . Q 9 HOH 448 1048 442 HOH HOH A . Q 9 HOH 449 1049 289 HOH HOH A . Q 9 HOH 450 1050 476 HOH HOH A . Q 9 HOH 451 1051 330 HOH HOH A . Q 9 HOH 452 1052 316 HOH HOH A . Q 9 HOH 453 1053 212 HOH HOH A . Q 9 HOH 454 1054 458 HOH HOH A . Q 9 HOH 455 1055 399 HOH HOH A . Q 9 HOH 456 1056 457 HOH HOH A . Q 9 HOH 457 1057 360 HOH HOH A . Q 9 HOH 458 1058 466 HOH HOH A . Q 9 HOH 459 1059 467 HOH HOH A . Q 9 HOH 460 1060 238 HOH HOH A . Q 9 HOH 461 1061 315 HOH HOH A . Q 9 HOH 462 1062 383 HOH HOH A . Q 9 HOH 463 1063 444 HOH HOH A . Q 9 HOH 464 1064 333 HOH HOH A . Q 9 HOH 465 1065 441 HOH HOH A . Q 9 HOH 466 1066 323 HOH HOH A . Q 9 HOH 467 1067 392 HOH HOH A . Q 9 HOH 468 1068 232 HOH HOH A . Q 9 HOH 469 1069 427 HOH HOH A . Q 9 HOH 470 1070 266 HOH HOH A . Q 9 HOH 471 1071 375 HOH HOH A . Q 9 HOH 472 1072 385 HOH HOH A . Q 9 HOH 473 1073 432 HOH HOH A . Q 9 HOH 474 1074 462 HOH HOH A . Q 9 HOH 475 1075 270 HOH HOH A . Q 9 HOH 476 1076 395 HOH HOH A . Q 9 HOH 477 1077 415 HOH HOH A . Q 9 HOH 478 1078 490 HOH HOH A . Q 9 HOH 479 1079 480 HOH HOH A . Q 9 HOH 480 1080 253 HOH HOH A . Q 9 HOH 481 1081 459 HOH HOH A . Q 9 HOH 482 1082 329 HOH HOH A . Q 9 HOH 483 1083 285 HOH HOH A . Q 9 HOH 484 1084 277 HOH HOH A . Q 9 HOH 485 1085 250 HOH HOH A . Q 9 HOH 486 1086 386 HOH HOH A . Q 9 HOH 487 1087 310 HOH HOH A . Q 9 HOH 488 1088 449 HOH HOH A . Q 9 HOH 489 1089 494 HOH HOH A . Q 9 HOH 490 1090 80 HOH HOH A . Q 9 HOH 491 1091 435 HOH HOH A . Q 9 HOH 492 1092 353 HOH HOH A . Q 9 HOH 493 1093 419 HOH HOH A . Q 9 HOH 494 1094 416 HOH HOH A . Q 9 HOH 495 1095 331 HOH HOH A . Q 9 HOH 496 1096 359 HOH HOH A . # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details 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 # _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_struct_special_symmetry.id _pdbx_struct_special_symmetry.PDB_model_num _pdbx_struct_special_symmetry.auth_asym_id _pdbx_struct_special_symmetry.auth_comp_id _pdbx_struct_special_symmetry.auth_seq_id _pdbx_struct_special_symmetry.PDB_ins_code _pdbx_struct_special_symmetry.label_asym_id _pdbx_struct_special_symmetry.label_comp_id _pdbx_struct_special_symmetry.label_seq_id 1 1 A HOH 743 ? Q HOH . 2 1 A HOH 909 ? Q HOH . 3 1 A HOH 994 ? Q HOH . 4 1 A HOH 1014 ? Q HOH . 5 1 A HOH 1060 ? Q HOH . 6 1 A HOH 1063 ? Q HOH . # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 OD1 ? A ASP 20 ? A ASP 28 ? 1_555 ZN ? C ZN . ? A ZN 502 ? 1_555 NE2 ? A HIS 22 ? A HIS 30 ? 1_555 113.2 ? 2 OD1 ? A ASP 20 ? A ASP 28 ? 1_555 ZN ? C ZN . ? A ZN 502 ? 1_555 OD2 ? A ASP 85 ? A ASP 93 ? 1_555 85.9 ? 3 NE2 ? A HIS 22 ? A HIS 30 ? 1_555 ZN ? C ZN . ? A ZN 502 ? 1_555 OD2 ? A ASP 85 ? A ASP 93 ? 1_555 88.6 ? 4 OD1 ? A ASP 20 ? A ASP 28 ? 1_555 ZN ? C ZN . ? A ZN 502 ? 1_555 NE2 ? A HIS 271 ? A HIS 279 ? 1_555 93.2 ? 5 NE2 ? A HIS 22 ? A HIS 30 ? 1_555 ZN ? C ZN . ? A ZN 502 ? 1_555 NE2 ? A HIS 271 ? A HIS 279 ? 1_555 99.2 ? 6 OD2 ? A ASP 85 ? A ASP 93 ? 1_555 ZN ? C ZN . ? A ZN 502 ? 1_555 NE2 ? A HIS 271 ? A HIS 279 ? 1_555 171.8 ? 7 OD1 ? A ASP 20 ? A ASP 28 ? 1_555 ZN ? C ZN . ? A ZN 502 ? 1_555 O ? Q HOH . ? A HOH 613 ? 1_555 101.0 ? 8 NE2 ? A HIS 22 ? A HIS 30 ? 1_555 ZN ? C ZN . ? A ZN 502 ? 1_555 O ? Q HOH . ? A HOH 613 ? 1_555 138.2 ? 9 OD2 ? A ASP 85 ? A ASP 93 ? 1_555 ZN ? C ZN . ? A ZN 502 ? 1_555 O ? Q HOH . ? A HOH 613 ? 1_555 70.0 ? 10 NE2 ? A HIS 271 ? A HIS 279 ? 1_555 ZN ? C ZN . ? A ZN 502 ? 1_555 O ? Q HOH . ? A HOH 613 ? 1_555 102.2 ? 11 OD2 ? A ASP 85 ? A ASP 93 ? 1_555 ZN ? B ZN . ? A ZN 501 ? 1_555 OD1 ? A ASN 126 ? A ASN 134 ? 1_555 102.6 ? 12 OD2 ? A ASP 85 ? A ASP 93 ? 1_555 ZN ? B ZN . ? A ZN 501 ? 1_555 NE2 ? A HIS 228 ? A HIS 236 ? 1_555 86.7 ? 13 OD1 ? A ASN 126 ? A ASN 134 ? 1_555 ZN ? B ZN . ? A ZN 501 ? 1_555 NE2 ? A HIS 228 ? A HIS 236 ? 1_555 89.7 ? 14 OD2 ? A ASP 85 ? A ASP 93 ? 1_555 ZN ? B ZN . ? A ZN 501 ? 1_555 ND1 ? A HIS 269 ? A HIS 277 ? 1_555 161.8 ? 15 OD1 ? A ASN 126 ? A ASN 134 ? 1_555 ZN ? B ZN . ? A ZN 501 ? 1_555 ND1 ? A HIS 269 ? A HIS 277 ? 1_555 95.1 ? 16 NE2 ? A HIS 228 ? A HIS 236 ? 1_555 ZN ? B ZN . ? A ZN 501 ? 1_555 ND1 ? A HIS 269 ? A HIS 277 ? 1_555 97.9 ? 17 OD2 ? A ASP 85 ? A ASP 93 ? 1_555 ZN ? B ZN . ? A ZN 501 ? 1_555 O ? Q HOH . ? A HOH 613 ? 1_555 72.0 ? 18 OD1 ? A ASN 126 ? A ASN 134 ? 1_555 ZN ? B ZN . ? A ZN 501 ? 1_555 O ? Q HOH . ? A HOH 613 ? 1_555 146.8 ? 19 NE2 ? A HIS 228 ? A HIS 236 ? 1_555 ZN ? B ZN . ? A ZN 501 ? 1_555 O ? Q HOH . ? A HOH 613 ? 1_555 121.8 ? 20 ND1 ? A HIS 269 ? A HIS 277 ? 1_555 ZN ? B ZN . ? A ZN 501 ? 1_555 O ? Q HOH . ? A HOH 613 ? 1_555 90.8 ? # 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 2016-10-05 2 'Structure model' 1 1 2016-10-12 3 'Structure model' 1 2 2016-11-23 # _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' 'Database references' 2 3 'Structure model' 'Database references' # loop_ _software.citation_id _software.classification _software.compiler_name _software.compiler_version _software.contact_author _software.contact_author_email _software.date _software.description _software.dependencies _software.hardware _software.language _software.location _software.mods _software.name _software.os _software.os_version _software.type _software.version _software.pdbx_ordinal ? refinement ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.10.1_2155 1 ? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? . 2 ? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? . 3 ? phasing ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? . 4 # 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 O3 A NO3 513 ? ? O A HOH 601 ? ? 2.12 2 1 O A HOH 657 ? ? O A HOH 988 ? ? 2.16 3 1 OD1 A ASP 328 ? ? O A HOH 602 ? ? 2.17 4 1 O A HOH 942 ? ? O A HOH 1086 ? ? 2.19 # _pdbx_validate_symm_contact.id 1 _pdbx_validate_symm_contact.PDB_model_num 1 _pdbx_validate_symm_contact.auth_atom_id_1 O _pdbx_validate_symm_contact.auth_asym_id_1 A _pdbx_validate_symm_contact.auth_comp_id_1 HOH _pdbx_validate_symm_contact.auth_seq_id_1 1012 _pdbx_validate_symm_contact.PDB_ins_code_1 ? _pdbx_validate_symm_contact.label_alt_id_1 ? _pdbx_validate_symm_contact.site_symmetry_1 1_555 _pdbx_validate_symm_contact.auth_atom_id_2 O _pdbx_validate_symm_contact.auth_asym_id_2 A _pdbx_validate_symm_contact.auth_comp_id_2 HOH _pdbx_validate_symm_contact.auth_seq_id_2 1036 _pdbx_validate_symm_contact.PDB_ins_code_2 ? _pdbx_validate_symm_contact.label_alt_id_2 ? _pdbx_validate_symm_contact.site_symmetry_2 2_555 _pdbx_validate_symm_contact.dist 2.07 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 HIS A 30 ? ? 39.25 71.70 2 1 ASN A 55 ? ? 39.73 59.68 3 1 ASP A 93 ? ? 76.71 82.32 4 1 LEU A 103 ? ? -153.60 82.71 5 1 ASP A 136 ? ? -88.96 49.74 6 1 ASN A 141 ? ? 74.84 -9.43 7 1 ALA A 145 ? ? -86.92 36.36 8 1 ALA A 186 ? ? -158.05 68.61 9 1 HIS A 236 ? ? -94.25 -69.35 10 1 HIS A 277 ? ? 75.64 -38.67 11 1 HIS A 279 ? ? 78.23 -8.83 12 1 TRP A 306 ? ? -39.85 125.13 13 1 ASP A 369 ? ? -166.59 -169.29 # _pdbx_distant_solvent_atoms.id 1 _pdbx_distant_solvent_atoms.PDB_model_num 1 _pdbx_distant_solvent_atoms.auth_atom_id O _pdbx_distant_solvent_atoms.label_alt_id ? _pdbx_distant_solvent_atoms.auth_asym_id A _pdbx_distant_solvent_atoms.auth_comp_id HOH _pdbx_distant_solvent_atoms.auth_seq_id 1096 _pdbx_distant_solvent_atoms.PDB_ins_code ? _pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 7.72 _pdbx_distant_solvent_atoms.neighbor_ligand_distance . # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A ASP 9 ? A ASP 1 2 1 Y 1 A ARG 10 ? A ARG 2 3 1 Y 1 A HIS 11 ? A HIS 3 4 1 Y 1 A HIS 12 ? A HIS 4 5 1 Y 1 A HIS 13 ? A HIS 5 6 1 Y 1 A HIS 14 ? A HIS 6 7 1 Y 1 A HIS 15 ? A HIS 7 8 1 Y 1 A HIS 16 ? A HIS 8 9 1 Y 1 A LYS 17 ? A LYS 9 10 1 Y 1 A LEU 18 ? A LEU 10 11 1 Y 1 A GLN 19 ? A GLN 11 12 1 Y 1 A LEU 432 ? A LEU 424 13 1 Y 1 A GLY 433 ? A GLY 425 14 1 Y 1 A ALA 434 ? A ALA 426 15 1 Y 1 A LYS 435 ? A LYS 427 # _pdbx_audit_support.funding_organization 'Canadian Institutes of Health Research' _pdbx_audit_support.country Canada _pdbx_audit_support.grant_number MOP-133535 _pdbx_audit_support.ordinal 1 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 'ZINC ION' ZN 3 N-ACETYL-D-GLUCOSAMINE NAG 4 BETA-D-MANNOSE BMA 5 ALPHA-D-MANNOSE MAN 6 ALPHA-L-FUCOSE FUC 7 'NITRATE ION' NO3 8 GLYCEROL GOL 9 water HOH #