data_4NN9 # _entry.id 4NN9 # _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 4NN9 WWPDB D_1000179375 # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4NN9 _pdbx_database_status.recvd_initial_deposition_date 1991-03-28 _pdbx_database_status.deposit_site ? _pdbx_database_status.process_site ? _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Tulip, W.R.' 1 'Varghese, J.N.' 2 'Baker, A.T.' 3 'Vandonkelaar, A.' 4 'Laver, W.G.' 5 'Webster, R.G.' 6 'Colman, P.M.' 7 # loop_ _citation.id _citation.title _citation.journal_abbrev _citation.journal_volume _citation.page_first _citation.page_last _citation.year _citation.journal_id_ASTM _citation.country _citation.journal_id_ISSN _citation.journal_id_CSD _citation.book_publisher _citation.pdbx_database_id_PubMed _citation.pdbx_database_id_DOI primary 'Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants.' J.Mol.Biol. 221 487 497 1991 JMOBAK UK 0022-2836 0070 ? 1920429 '10.1016/0022-2836(91)80069-7' 1 'Three-Dimensional Structure of the Neuraminidase of Influenza Virus A(Slash)Tokyo(Slash)3(Slash)67 at 2.2 Angstroms Resolution' J.Mol.Biol. 221 473 ? 1991 JMOBAK UK 0022-2836 0070 ? ? ? 2 'Three Dimensional Structure of Neuraminidase of Subtype N9 from an Avian Influenza Virus' Proteins 2 111 ? 1987 PSFGEY US 0887-3585 0867 ? ? ? 3 'Gene and Protein Sequence of an Influenza Virus Neuraminidase with Hemagglutinin Activity' Virology 145 117 ? 1985 VIRLAX US 0042-6822 0922 ? ? ? 4 'Influenza Virus Neuraminidase with Hemmagglutinin Activity' Virology 137 314 ? 1984 VIRLAX US 0042-6822 0922 ? ? ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Tulip, W.R.' 1 primary 'Varghese, J.N.' 2 primary 'Baker, A.T.' 3 primary 'van Donkelaar, A.' 4 primary 'Laver, W.G.' 5 primary 'Webster, R.G.' 6 primary 'Colman, P.M.' 7 1 'Varghese, J.N.' 8 1 'Colman, P.M.' 9 2 'Baker, A.T.' 10 2 'Varghese, J.N.' 11 2 'Laver, W.G.' 12 2 'Air, G.M.' 13 2 'Colman, P.M.' 14 3 'Air, G.M.' 15 3 'Ritchie, L.R.' 16 3 'Laver, W.G.' 17 3 'Colman, P.M.' 18 4 'Laver, W.G.' 19 4 'Colman, P.M.' 20 4 'Webster, R.G.' 21 4 'Hinshaw, V.S.' 22 4 'Air, G.M.' 23 # _cell.entry_id 4NN9 _cell.length_a 185.100 _cell.length_b 185.100 _cell.length_c 185.100 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 48 _cell.pdbx_unique_axis ? # _symmetry.entry_id 4NN9 _symmetry.space_group_name_H-M 'I 4 3 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 211 # 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 'NEURAMINIDASE N9' 43767.809 1 3.2.1.18 ? ? ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? 3 non-polymer man ALPHA-D-MANNOSE 180.156 5 ? ? ? ? 4 non-polymer syn 'CALCIUM ION' 40.078 1 ? ? ? ? 5 water nat water 18.015 89 ? ? ? ? # _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 ;RDFNNLTKGLCTINSWHIYGKDNAVRIGEDSDVLVTREPYVSCDPDECRFYALSQGTTIRGKHSNGTIHDRSQYRALISW PLSSPPTVYNSRVECIGWSSTSCHDGKTRMSICISGPNNNASAVIWYNRRPVTEINTWARNILRTQESECVCHNGVCPVV FTDGSATGPAETRIYYFKEGKILKWEPLAGTAKHIEECSCYGERAEITCTCRDNWQGSNRPVIRIDPVAMTHTSQYICSP VLTDNPRPNDPTVGKCNDPYPGNNNNGVKGFSYLDGVNTWLGRTISRASRSGYEMLKVPNALTDDKSKPTQGQTIVLNTD WSGYSGSFMDYWAEGECYRACFYVELIRGRPKEDKVWWTSNSIVSMCSSTEFLGQWDWPDGAKIEYFL ; _entity_poly.pdbx_seq_one_letter_code_can ;RDFNNLTKGLCTINSWHIYGKDNAVRIGEDSDVLVTREPYVSCDPDECRFYALSQGTTIRGKHSNGTIHDRSQYRALISW PLSSPPTVYNSRVECIGWSSTSCHDGKTRMSICISGPNNNASAVIWYNRRPVTEINTWARNILRTQESECVCHNGVCPVV FTDGSATGPAETRIYYFKEGKILKWEPLAGTAKHIEECSCYGERAEITCTCRDNWQGSNRPVIRIDPVAMTHTSQYICSP VLTDNPRPNDPTVGKCNDPYPGNNNNGVKGFSYLDGVNTWLGRTISRASRSGYEMLKVPNALTDDKSKPTQGQTIVLNTD WSGYSGSFMDYWAEGECYRACFYVELIRGRPKEDKVWWTSNSIVSMCSSTEFLGQWDWPDGAKIEYFL ; _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 ARG n 1 2 ASP n 1 3 PHE n 1 4 ASN n 1 5 ASN n 1 6 LEU n 1 7 THR n 1 8 LYS n 1 9 GLY n 1 10 LEU n 1 11 CYS n 1 12 THR n 1 13 ILE n 1 14 ASN n 1 15 SER n 1 16 TRP n 1 17 HIS n 1 18 ILE n 1 19 TYR n 1 20 GLY n 1 21 LYS n 1 22 ASP n 1 23 ASN n 1 24 ALA n 1 25 VAL n 1 26 ARG n 1 27 ILE n 1 28 GLY n 1 29 GLU n 1 30 ASP n 1 31 SER n 1 32 ASP n 1 33 VAL n 1 34 LEU n 1 35 VAL n 1 36 THR n 1 37 ARG n 1 38 GLU n 1 39 PRO n 1 40 TYR n 1 41 VAL n 1 42 SER n 1 43 CYS n 1 44 ASP n 1 45 PRO n 1 46 ASP n 1 47 GLU n 1 48 CYS n 1 49 ARG n 1 50 PHE n 1 51 TYR n 1 52 ALA n 1 53 LEU n 1 54 SER n 1 55 GLN n 1 56 GLY n 1 57 THR n 1 58 THR n 1 59 ILE n 1 60 ARG n 1 61 GLY n 1 62 LYS n 1 63 HIS n 1 64 SER n 1 65 ASN n 1 66 GLY n 1 67 THR n 1 68 ILE n 1 69 HIS n 1 70 ASP n 1 71 ARG n 1 72 SER n 1 73 GLN n 1 74 TYR n 1 75 ARG n 1 76 ALA n 1 77 LEU n 1 78 ILE n 1 79 SER n 1 80 TRP n 1 81 PRO n 1 82 LEU n 1 83 SER n 1 84 SER n 1 85 PRO n 1 86 PRO n 1 87 THR n 1 88 VAL n 1 89 TYR n 1 90 ASN n 1 91 SER n 1 92 ARG n 1 93 VAL n 1 94 GLU n 1 95 CYS n 1 96 ILE n 1 97 GLY n 1 98 TRP n 1 99 SER n 1 100 SER n 1 101 THR n 1 102 SER n 1 103 CYS n 1 104 HIS n 1 105 ASP n 1 106 GLY n 1 107 LYS n 1 108 THR n 1 109 ARG n 1 110 MET n 1 111 SER n 1 112 ILE n 1 113 CYS n 1 114 ILE n 1 115 SER n 1 116 GLY n 1 117 PRO n 1 118 ASN n 1 119 ASN n 1 120 ASN n 1 121 ALA n 1 122 SER n 1 123 ALA n 1 124 VAL n 1 125 ILE n 1 126 TRP n 1 127 TYR n 1 128 ASN n 1 129 ARG n 1 130 ARG n 1 131 PRO n 1 132 VAL n 1 133 THR n 1 134 GLU n 1 135 ILE n 1 136 ASN n 1 137 THR n 1 138 TRP n 1 139 ALA n 1 140 ARG n 1 141 ASN n 1 142 ILE n 1 143 LEU n 1 144 ARG n 1 145 THR n 1 146 GLN n 1 147 GLU n 1 148 SER n 1 149 GLU n 1 150 CYS n 1 151 VAL n 1 152 CYS n 1 153 HIS n 1 154 ASN n 1 155 GLY n 1 156 VAL n 1 157 CYS n 1 158 PRO n 1 159 VAL n 1 160 VAL n 1 161 PHE n 1 162 THR n 1 163 ASP n 1 164 GLY n 1 165 SER n 1 166 ALA n 1 167 THR n 1 168 GLY n 1 169 PRO n 1 170 ALA n 1 171 GLU n 1 172 THR n 1 173 ARG n 1 174 ILE n 1 175 TYR n 1 176 TYR n 1 177 PHE n 1 178 LYS n 1 179 GLU n 1 180 GLY n 1 181 LYS n 1 182 ILE n 1 183 LEU n 1 184 LYS n 1 185 TRP n 1 186 GLU n 1 187 PRO n 1 188 LEU n 1 189 ALA n 1 190 GLY n 1 191 THR n 1 192 ALA n 1 193 LYS n 1 194 HIS n 1 195 ILE n 1 196 GLU n 1 197 GLU n 1 198 CYS n 1 199 SER n 1 200 CYS n 1 201 TYR n 1 202 GLY n 1 203 GLU n 1 204 ARG n 1 205 ALA n 1 206 GLU n 1 207 ILE n 1 208 THR n 1 209 CYS n 1 210 THR n 1 211 CYS n 1 212 ARG n 1 213 ASP n 1 214 ASN n 1 215 TRP n 1 216 GLN n 1 217 GLY n 1 218 SER n 1 219 ASN n 1 220 ARG n 1 221 PRO n 1 222 VAL n 1 223 ILE n 1 224 ARG n 1 225 ILE n 1 226 ASP n 1 227 PRO n 1 228 VAL n 1 229 ALA n 1 230 MET n 1 231 THR n 1 232 HIS n 1 233 THR n 1 234 SER n 1 235 GLN n 1 236 TYR n 1 237 ILE n 1 238 CYS n 1 239 SER n 1 240 PRO n 1 241 VAL n 1 242 LEU n 1 243 THR n 1 244 ASP n 1 245 ASN n 1 246 PRO n 1 247 ARG n 1 248 PRO n 1 249 ASN n 1 250 ASP n 1 251 PRO n 1 252 THR n 1 253 VAL n 1 254 GLY n 1 255 LYS n 1 256 CYS n 1 257 ASN n 1 258 ASP n 1 259 PRO n 1 260 TYR n 1 261 PRO n 1 262 GLY n 1 263 ASN n 1 264 ASN n 1 265 ASN n 1 266 ASN n 1 267 GLY n 1 268 VAL n 1 269 LYS n 1 270 GLY n 1 271 PHE n 1 272 SER n 1 273 TYR n 1 274 LEU n 1 275 ASP n 1 276 GLY n 1 277 VAL n 1 278 ASN n 1 279 THR n 1 280 TRP n 1 281 LEU n 1 282 GLY n 1 283 ARG n 1 284 THR n 1 285 ILE n 1 286 SER n 1 287 ARG n 1 288 ALA n 1 289 SER n 1 290 ARG n 1 291 SER n 1 292 GLY n 1 293 TYR n 1 294 GLU n 1 295 MET n 1 296 LEU n 1 297 LYS n 1 298 VAL n 1 299 PRO n 1 300 ASN n 1 301 ALA n 1 302 LEU n 1 303 THR n 1 304 ASP n 1 305 ASP n 1 306 LYS n 1 307 SER n 1 308 LYS n 1 309 PRO n 1 310 THR n 1 311 GLN n 1 312 GLY n 1 313 GLN n 1 314 THR n 1 315 ILE n 1 316 VAL n 1 317 LEU n 1 318 ASN n 1 319 THR n 1 320 ASP n 1 321 TRP n 1 322 SER n 1 323 GLY n 1 324 TYR n 1 325 SER n 1 326 GLY n 1 327 SER n 1 328 PHE n 1 329 MET n 1 330 ASP n 1 331 TYR n 1 332 TRP n 1 333 ALA n 1 334 GLU n 1 335 GLY n 1 336 GLU n 1 337 CYS n 1 338 TYR n 1 339 ARG n 1 340 ALA n 1 341 CYS n 1 342 PHE n 1 343 TYR n 1 344 VAL n 1 345 GLU n 1 346 LEU n 1 347 ILE n 1 348 ARG n 1 349 GLY n 1 350 ARG n 1 351 PRO n 1 352 LYS n 1 353 GLU n 1 354 ASP n 1 355 LYS n 1 356 VAL n 1 357 TRP n 1 358 TRP n 1 359 THR n 1 360 SER n 1 361 ASN n 1 362 SER n 1 363 ILE n 1 364 VAL n 1 365 SER n 1 366 MET n 1 367 CYS n 1 368 SER n 1 369 SER n 1 370 THR n 1 371 GLU n 1 372 PHE n 1 373 LEU n 1 374 GLY n 1 375 GLN n 1 376 TRP n 1 377 ASP n 1 378 TRP n 1 379 PRO n 1 380 ASP n 1 381 GLY n 1 382 ALA n 1 383 LYS n 1 384 ILE n 1 385 GLU n 1 386 TYR n 1 387 PHE n 1 388 LEU 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 ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name ? _entity_src_gen.gene_src_genus 'Influenzavirus A' _entity_src_gen.pdbx_gene_src_gene ? _entity_src_gen.gene_src_species 'Influenza A virus' _entity_src_gen.gene_src_strain '(A/tern/Australia/G70C/1975(H11N9))' _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 'Influenza A virus' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 384509 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name ? _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id ? _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type ? _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code NRAM_IATRA _struct_ref.entity_id 1 _struct_ref.pdbx_db_accession P03472 _struct_ref.pdbx_align_begin 1 _struct_ref.pdbx_seq_one_letter_code ;MNPNQKILCTSATALVIGTIAVLIGITNLGLNIGLHLKPSCNCSHSQPEATNASQTIINNYYNDTNITQISNTNIQVEER AIRDFNNLTKGLCTINSWHIYGKDNAVRIGEDSDVLVTREPYVSCDPDECRFYALSQGTTIRGKHSNGTIHDRSQYRALI SWPLSSPPTVYNSRVECIGWSSTSCHDGKTRMSICISGPNNNASAVIWYNRRPVTEINTWARNILRTQESECVCHNGVCP VVFTDGSATGPAETRIYYFKEGKILKWEPLAGTAKHIEECSCYGERAEITCTCRDNWQGSNRPVIRIDPVAMTHTSQYIC SPVLTDNPRPNDPTVGKCNDPYPGNNNNGVKGFSYLDGVNTWLGRTISIASRSGYEMLKVPNALTDDKSKPTQGQTIVLN TDWSGYSGSFMDYWAEGECYRACFYVELIRGRPKEDKVWWTSNSIVSMCSSTEFLGQWDWPDGAKIEYFL ; _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 4NN9 _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 1 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 388 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession P03472 _struct_ref_seq.db_align_beg 83 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 470 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 82 _struct_ref_seq.pdbx_auth_seq_align_end 468 # _struct_ref_seq_dif.align_id 1 _struct_ref_seq_dif.pdbx_pdb_id_code 4NN9 _struct_ref_seq_dif.mon_id ARG _struct_ref_seq_dif.pdbx_pdb_strand_id A _struct_ref_seq_dif.seq_num 287 _struct_ref_seq_dif.pdbx_pdb_ins_code ? _struct_ref_seq_dif.pdbx_seq_db_name UNP _struct_ref_seq_dif.pdbx_seq_db_accession_code P03472 _struct_ref_seq_dif.db_mon_id ILE _struct_ref_seq_dif.pdbx_seq_db_seq_num 369 _struct_ref_seq_dif.details CONFLICT _struct_ref_seq_dif.pdbx_auth_seq_num 368 _struct_ref_seq_dif.pdbx_ordinal 1 # 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 CA non-polymer . 'CALCIUM ION' ? 'Ca 2' 40.078 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 4NN9 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number ? # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.02 _exptl_crystal.density_percent_sol 59.23 _exptl_crystal.description ? # _diffrn.id 1 _diffrn.crystal_id 1 _diffrn.ambient_temp ? _diffrn.ambient_temp_details ? # _refine.entry_id 4NN9 _refine.ls_number_reflns_obs ? _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 6.0 _refine.ls_d_res_high 2.3 _refine.ls_percent_reflns_obs ? _refine.ls_R_factor_obs ? _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.163 _refine.ls_R_factor_R_free ? _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free ? _refine.ls_number_reflns_R_free ? _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.B_iso_mean ? _refine.aniso_B[1][1] ? _refine.aniso_B[2][2] ? _refine.aniso_B[3][3] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][3] ? _refine.solvent_model_details ? _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_ls_cross_valid_method ? _refine.details ;SIDE CHAINS AND/OR WHOLE RESIDUES WERE OMITTED FROM THE CRYSTALLOGRAPHIC REFINEMENT BY ASSIGNING THEM OCCUPANCIES OF 0.02. BECAUSE AN ERROR IN THE REGISTRATION OF THE NEURAMINIDASE C-TERMINAL SEGMENT WAS DISCOVERED LATE IN THE REFINEMENT PROCESS, THE COORDINATES OF RESIDUES 458 - 468 IN THIS MUTANT WERE TAKEN DIRECTLY FROM THE REFINED COORDINATES OF S370L. THE OCCUPANCY AND B VALUE OF THE CALCIUM ION ARE TENTATIVE AND REQUIRE HIGH RESOLUTION DATA REFINEMENT. THE CALCIUM WAS REFINED AS A NON-BONDED ION. THE FIVE LIGANDS ARE O ASP 293, O GLY 297, OD2 ASP 324, O ASN 347, AND HOH 8. THEY ARE IN OCTAHEDRAL GEOMETRY (NO RESTRAINTS WERE IMPOSED) AND THE SIXTH LIGAND (PRESUMABLY ANOTHER WATER MOLECULE) IS NOT SEEN IN THE ELECTRON DENSITY MAPS. ; _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct ? _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ? _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML ? _refine.overall_SU_B ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.pdbx_overall_phase_error ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 3070 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 112 _refine_hist.number_atoms_solvent 89 _refine_hist.number_atoms_total 3271 _refine_hist.d_res_high 2.3 _refine_hist.d_res_low 6.0 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function x_bond_d 0.017 ? ? ? 'X-RAY DIFFRACTION' ? x_bond_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? x_bond_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? x_angle_d ? ? ? ? 'X-RAY DIFFRACTION' ? x_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? x_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? x_angle_deg 3.5 ? ? ? 'X-RAY DIFFRACTION' ? x_angle_deg_na ? ? ? ? 'X-RAY DIFFRACTION' ? x_angle_deg_prot ? ? ? ? 'X-RAY DIFFRACTION' ? x_dihedral_angle_d 27.9 ? ? ? 'X-RAY DIFFRACTION' ? x_dihedral_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? x_dihedral_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? x_improper_angle_d ? ? ? ? 'X-RAY DIFFRACTION' ? x_improper_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? x_improper_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? x_mcbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? x_mcangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? x_scbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? x_scangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? # _struct.entry_id 4NN9 _struct.title 'REFINED ATOMIC STRUCTURES OF N9 SUBTYPE INFLUENZA VIRUS NEURAMINIDASE AND ESCAPE MUTANTS' _struct.pdbx_descriptor 'NEURAMINIDASE N9 (E.C.3.2.1.18) (SIALIDASE) (MUTANT WITH ILE 368 REPLACED BY ARG) (I368R)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4NN9 _struct_keywords.pdbx_keywords 'HYDROLASE(O-GLYCOSYL)' _struct_keywords.text 'HYDROLASE(O-GLYCOSYL)' # 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 3 ? G N N 3 ? H N N 3 ? I N N 2 ? J N N 2 ? K N N 4 ? L N N 5 ? # _struct_biol.id 1 # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 ASN A 23 ? GLU A 29 ? ASN A 104 GLU A 110 1 ? 7 HELX_P HELX_P2 2 GLY A 61 ? ASN A 65 ? GLY A 142 ASN A 146 5 ? 5 HELX_P HELX_P3 3 LYS A 383 ? LEU A 388 ? LYS A 463 LEU A 468 5 ? 6 # _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 11 SG ? ? ? 1_555 A CYS 337 SG ? ? A CYS 92 A CYS 417 1_555 ? ? ? ? ? ? ? 2.006 ? disulf2 disulf ? ? A CYS 43 SG ? ? ? 1_555 A CYS 48 SG ? ? A CYS 124 A CYS 129 1_555 ? ? ? ? ? ? ? 2.023 ? disulf3 disulf ? ? A CYS 95 SG ? ? ? 1_555 A CYS 113 SG ? ? A CYS 175 A CYS 193 1_555 ? ? ? ? ? ? ? 2.057 ? disulf4 disulf ? ? A CYS 103 SG ? ? ? 1_555 A CYS 150 SG ? ? A CYS 183 A CYS 230 1_555 ? ? ? ? ? ? ? 2.058 ? disulf5 disulf ? ? A CYS 152 SG ? ? ? 1_555 A CYS 157 SG ? ? A CYS 232 A CYS 237 1_555 ? ? ? ? ? ? ? 1.989 ? disulf6 disulf ? ? A CYS 198 SG ? ? ? 1_555 A CYS 211 SG ? ? A CYS 278 A CYS 291 1_555 ? ? ? ? ? ? ? 2.120 ? disulf7 disulf ? ? A CYS 200 SG ? ? ? 1_555 A CYS 209 SG ? ? A CYS 280 A CYS 289 1_555 ? ? ? ? ? ? ? 1.962 ? disulf8 disulf ? ? A CYS 238 SG ? ? ? 1_555 A CYS 256 SG ? ? A CYS 318 A CYS 337 1_555 ? ? ? ? ? ? ? 2.005 ? disulf9 disulf ? ? A CYS 341 SG ? ? ? 1_555 A CYS 367 SG ? ? A CYS 421 A CYS 447 1_555 ? ? ? ? ? ? ? 2.033 ? covale1 covale ? ? A ASN 5 ND2 ? ? ? 1_555 J NAG . C1 ? A A ASN 86 A NAG 477 1_555 ? ? ? ? ? ? ? 1.460 ? covale2 covale ? ? A ASN 65 ND2 ? ? ? 1_555 I NAG . C1 ? A A ASN 146 A NAG 476 1_555 ? ? ? ? ? ? ? 1.462 ? covale3 covale ? ? A ASN 120 ND2 ? ? ? 1_555 B NAG . C1 ? A A ASN 200 A NAG 469 1_555 ? ? ? ? ? ? ? 1.456 ? covale4 covale ? ? B NAG . O4 ? A ? 1_555 C NAG . C1 ? B A NAG 469 A NAG 470 1_555 ? ? ? ? ? ? ? 1.461 ? covale5 covale ? ? C NAG . O4 ? B ? 1_555 D MAN . C1 ? C A NAG 470 A MAN 471 1_555 ? ? ? ? ? ? ? 1.419 ? covale6 covale ? ? D MAN . O3 ? C ? 1_555 E MAN . C1 ? D A MAN 471 A MAN 472 1_555 ? ? ? ? ? ? ? 1.407 ? covale7 covale ? ? D MAN . O6 ? C ? 1_555 H MAN . C1 ? G A MAN 471 A MAN 475 1_555 ? ? ? ? ? ? ? 1.469 ? covale8 covale ? ? E MAN . O2 ? D ? 1_555 F MAN . C1 ? E A MAN 472 A MAN 473 1_555 ? ? ? ? ? ? ? 1.428 ? covale9 covale ? ? F MAN . O2 ? E ? 1_555 G MAN . C1 ? F A MAN 473 A MAN 474 1_555 ? ? ? ? ? ? ? 1.421 ? metalc1 metalc ? ? K CA . CA ? ? ? 1_555 A ASP 244 OD2 ? ? A CA 18 A ASP 324 1_555 ? ? ? ? ? ? ? 2.880 ? metalc2 metalc ? ? K CA . CA ? ? ? 1_555 A GLY 217 O ? ? A CA 18 A GLY 297 1_555 ? ? ? ? ? ? ? 2.702 ? metalc3 metalc ? ? K CA . CA ? ? ? 1_555 A ASN 266 O ? ? A CA 18 A ASN 347 1_555 ? ? ? ? ? ? ? 3.127 ? metalc4 metalc ? ? K CA . CA ? ? ? 1_555 A ASP 213 O ? ? A CA 18 A ASP 293 1_555 ? ? ? ? ? ? ? 2.636 ? metalc5 metalc ? ? K CA . CA ? ? ? 1_555 L HOH . O ? ? A CA 18 A HOH 485 1_555 ? ? ? ? ? ? ? 2.974 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # 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 ASN 245 A . ? ASN 325 A PRO 246 A ? PRO 326 A 1 -1.02 2 ARG 350 A . ? ARG 430 A PRO 351 A ? PRO 431 A 1 2.10 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 4 ? B ? 4 ? C ? 4 ? D ? 4 ? E ? 4 ? F ? 4 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel D 3 4 ? anti-parallel E 1 2 ? anti-parallel E 2 3 ? anti-parallel E 3 4 ? anti-parallel F 1 2 ? anti-parallel F 2 3 ? anti-parallel F 3 4 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 SER A 15 ? LYS A 21 ? SER A 96 LYS A 102 A 2 THR A 359 ? SER A 369 ? THR A 439 SER A 449 A 3 CYS A 341 ? GLY A 349 ? CYS A 421 GLY A 429 A 4 SER A 325 ? PHE A 328 ? SER A 407 PHE A 410 B 1 LEU A 34 ? CYS A 43 ? LEU A 115 CYS A 124 B 2 CYS A 48 ? THR A 58 ? CYS A 129 THR A 139 B 3 ALA A 76 ? PRO A 81 ? ALA A 157 PRO A 162 B 4 ARG A 92 ? ILE A 96 ? ARG A 172 ILE A 176 C 1 SER A 100 ? HIS A 104 ? SER A 180 HIS A 184 C 2 ARG A 109 ? SER A 115 ? ARG A 189 SER A 195 C 3 SER A 122 ? TYR A 127 ? SER A 202 TYR A 207 C 4 ARG A 130 ? ASN A 136 ? ARG A 210 ASN A 216 D 1 ARG A 144 ? THR A 145 ? ARG A 224 THR A 225 D 2 VAL A 156 ? ASP A 163 ? VAL A 236 ASP A 243 D 3 GLU A 171 ? LYS A 178 ? GLU A 251 LYS A 258 D 4 LYS A 181 ? PRO A 187 ? LYS A 261 PRO A 267 E 1 SER A 199 ? GLU A 203 ? SER A 279 GLU A 283 E 2 GLU A 206 ? THR A 210 ? GLU A 286 THR A 290 E 3 PRO A 221 ? ASP A 226 ? PRO A 301 ASP A 306 E 4 THR A 231 ? TYR A 236 ? THR A 311 TYR A 316 F 1 SER A 272 ? TYR A 273 ? SER A 353 TYR A 354 F 2 TRP A 280 ? ARG A 283 ? TRP A 361 ARG A 364 F 3 SER A 291 ? LYS A 297 ? SER A 372 LYS A 378 F 4 GLN A 311 ? TRP A 321 ? GLN A 392 TRP A 403 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 N TYR A 19 ? N TYR A 100 O SER A 365 ? O SER A 445 A 2 3 O MET A 366 ? O MET A 446 N PHE A 342 ? N PHE A 422 A 3 4 N TYR A 343 ? N TYR A 423 O GLY A 326 ? O GLY A 408 B 1 2 O SER A 42 ? O SER A 123 N ARG A 49 ? N ARG A 130 B 2 3 N SER A 54 ? N SER A 135 O ALA A 76 ? O ALA A 157 B 3 4 O SER A 79 ? O SER A 160 N ARG A 92 ? N ARG A 172 C 1 2 O CYS A 103 ? O CYS A 183 N MET A 110 ? N MET A 190 C 2 3 O SER A 115 ? O SER A 195 N SER A 122 ? N SER A 202 C 3 4 N TYR A 127 ? N TYR A 207 O ARG A 130 ? O ARG A 210 D 1 2 N ARG A 144 ? N ARG A 224 O THR A 162 ? O THR A 242 D 2 3 O ASP A 163 ? O ASP A 243 N GLU A 171 ? N GLU A 251 D 3 4 N LYS A 178 ? N LYS A 258 O LYS A 181 ? O LYS A 261 E 1 2 N GLU A 203 ? N GLU A 283 O GLU A 206 ? O GLU A 286 E 2 3 N CYS A 209 ? N CYS A 289 O ILE A 223 ? O ILE A 303 E 3 4 N ASP A 226 ? N ASP A 306 O THR A 231 ? O THR A 311 F 1 2 N TYR A 273 ? N TYR A 354 O TRP A 280 ? O TRP A 361 F 2 3 O ARG A 283 ? O ARG A 364 N GLU A 294 ? N GLU A 375 F 3 4 N LYS A 297 ? N LYS A 378 O GLN A 311 ? O GLN A 392 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG A 469A' AC2 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 470B' AC3 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE MAN A 471C' AC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE MAN A 472D' AC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE MAN A 473E' AC6 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE MAN A 474F' AC7 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE MAN A 475G' AC8 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 476A' AC9 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 477A' BC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA A 18' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 7 ASN A 119 ? ASN A 199 . ? 1_555 ? 2 AC1 7 ASN A 120 ? ASN A 200 . ? 1_555 ? 3 AC1 7 ARG A 140 ? ARG A 220 . ? 1_555 ? 4 AC1 7 LEU A 373 ? LEU A 453 . ? 15_555 ? 5 AC1 7 GLY A 374 ? GLY A 454 . ? 15_555 ? 6 AC1 7 GLN A 375 ? GLN A 455 . ? 15_555 ? 7 AC1 7 NAG C . B NAG A 470 . ? 1_555 ? 8 AC2 6 GLN A 311 ? GLN A 392 . ? 15_555 ? 9 AC2 6 GLY A 312 ? GLY A 394 . ? 15_555 ? 10 AC2 6 PHE A 372 ? PHE A 452 . ? 15_555 ? 11 AC2 6 NAG B . A NAG A 469 . ? 1_555 ? 12 AC2 6 MAN D . C MAN A 471 . ? 1_555 ? 13 AC2 6 HOH L . ? HOH A 505 . ? 15_555 ? 14 AC3 6 LEU A 296 ? LEU A 377 . ? 15_555 ? 15 AC3 6 GLY A 312 ? GLY A 394 . ? 15_555 ? 16 AC3 6 NAG C . B NAG A 470 . ? 1_555 ? 17 AC3 6 MAN E . D MAN A 472 . ? 1_555 ? 18 AC3 6 MAN H . G MAN A 475 . ? 1_555 ? 19 AC3 6 HOH L . ? HOH A 558 . ? 15_555 ? 20 AC4 5 ARG A 283 ? ARG A 364 . ? 15_555 ? 21 AC4 5 GLU A 294 ? GLU A 375 . ? 15_555 ? 22 AC4 5 MAN D . C MAN A 471 . ? 1_555 ? 23 AC4 5 MAN F . E MAN A 473 . ? 1_555 ? 24 AC4 5 MAN G . F MAN A 474 . ? 1_555 ? 25 AC5 4 ASP A 250 ? ASP A 330 . ? 15_555 ? 26 AC5 4 ARG A 283 ? ARG A 364 . ? 15_555 ? 27 AC5 4 MAN E . D MAN A 472 . ? 1_555 ? 28 AC5 4 MAN G . F MAN A 474 . ? 1_555 ? 29 AC6 8 ARG A 247 ? ARG A 327 . ? 15_555 ? 30 AC6 8 ASN A 249 ? ASN A 329 . ? 15_555 ? 31 AC6 8 ASP A 250 ? ASP A 330 . ? 15_555 ? 32 AC6 8 ILE A 285 ? ILE A 366 . ? 15_555 ? 33 AC6 8 ARG A 287 ? ARG A 368 . ? 15_555 ? 34 AC6 8 MAN E . D MAN A 472 . ? 1_555 ? 35 AC6 8 MAN F . E MAN A 473 . ? 1_555 ? 36 AC6 8 HOH L . ? HOH A 556 . ? 15_555 ? 37 AC7 1 MAN D . C MAN A 471 . ? 1_555 ? 38 AC8 2 ASN A 65 ? ASN A 146 . ? 1_555 ? 39 AC8 2 TRP A 357 ? TRP A 437 . ? 1_555 ? 40 AC9 4 ASP A 2 ? ASP A 83 . ? 1_555 ? 41 AC9 4 PHE A 3 ? PHE A 84 . ? 1_555 ? 42 AC9 4 ASN A 5 ? ASN A 86 . ? 1_555 ? 43 AC9 4 ASN A 154 ? ASN A 234 . ? 1_555 ? 44 BC1 5 ASP A 213 ? ASP A 293 . ? 1_555 ? 45 BC1 5 GLY A 217 ? GLY A 297 . ? 1_555 ? 46 BC1 5 ASP A 244 ? ASP A 324 . ? 1_555 ? 47 BC1 5 ASN A 266 ? ASN A 347 . ? 1_555 ? 48 BC1 5 HOH L . ? HOH A 485 . ? 1_555 ? # _database_PDB_matrix.entry_id 4NN9 _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 4NN9 _atom_sites.fract_transf_matrix[1][1] 0.005402 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.005402 _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] 0.005402 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # _atom_sites_footnote.id 1 _atom_sites_footnote.text 'RESIDUES 326 AND 431 ARE CIS PROLINES.' # loop_ _atom_type.symbol C CA N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . ARG A 1 1 ? 10.639 10.430 33.059 1.00 31.98 ? 82 ARG A N 1 ATOM 2 C CA . ARG A 1 1 ? 11.492 9.505 32.371 1.00 30.78 ? 82 ARG A CA 1 ATOM 3 C C . ARG A 1 1 ? 12.562 10.210 31.543 1.00 28.55 ? 82 ARG A C 1 ATOM 4 O O . ARG A 1 1 ? 13.233 9.512 30.779 1.00 24.96 ? 82 ARG A O 1 ATOM 5 C CB . ARG A 1 1 ? 10.691 8.544 31.453 1.00 34.90 ? 82 ARG A CB 1 ATOM 6 C CG . ARG A 1 1 ? 9.866 9.054 30.270 1.00 39.95 ? 82 ARG A CG 1 ATOM 7 C CD . ARG A 1 1 ? 8.518 9.607 30.687 1.00 43.95 ? 82 ARG A CD 1 ATOM 8 N NE . ARG A 1 1 ? 7.706 8.552 31.274 1.00 48.82 ? 82 ARG A NE 1 ATOM 9 C CZ . ARG A 1 1 ? 6.361 8.616 31.332 1.00 52.69 ? 82 ARG A CZ 1 ATOM 10 N NH1 . ARG A 1 1 ? 5.640 9.631 30.813 1.00 53.23 ? 82 ARG A NH1 1 ATOM 11 N NH2 . ARG A 1 1 ? 5.689 7.609 31.894 1.00 54.70 ? 82 ARG A NH2 1 ATOM 12 N N . ASP A 1 2 ? 12.718 11.544 31.535 1.00 25.26 ? 83 ASP A N 1 ATOM 13 C CA . ASP A 1 2 ? 13.980 12.062 31.014 1.00 22.71 ? 83 ASP A CA 1 ATOM 14 C C . ASP A 1 2 ? 14.447 12.956 32.139 1.00 19.83 ? 83 ASP A C 1 ATOM 15 O O . ASP A 1 2 ? 13.587 13.323 32.950 1.00 20.62 ? 83 ASP A O 1 ATOM 16 C CB . ASP A 1 2 ? 13.875 12.914 29.749 1.00 26.52 ? 83 ASP A CB 1 ATOM 17 C CG . ASP A 1 2 ? 15.144 12.757 28.884 1.00 30.74 ? 83 ASP A CG 1 ATOM 18 O OD1 . ASP A 1 2 ? 16.278 12.776 29.401 1.00 32.59 ? 83 ASP A OD1 1 ATOM 19 O OD2 . ASP A 1 2 ? 15.000 12.599 27.664 1.00 34.32 ? 83 ASP A OD2 1 ATOM 20 N N . PHE A 1 3 ? 15.754 13.212 32.274 1.00 15.75 ? 84 PHE A N 1 ATOM 21 C CA . PHE A 1 3 ? 16.320 14.031 33.326 1.00 12.47 ? 84 PHE A CA 1 ATOM 22 C C . PHE A 1 3 ? 15.728 15.444 33.540 1.00 12.83 ? 84 PHE A C 1 ATOM 23 O O . PHE A 1 3 ? 15.349 16.129 32.593 1.00 13.28 ? 84 PHE A O 1 ATOM 24 C CB . PHE A 1 3 ? 17.797 14.095 33.037 1.00 13.01 ? 84 PHE A CB 1 ATOM 25 C CG . PHE A 1 3 ? 18.676 12.853 33.313 1.00 12.46 ? 84 PHE A CG 1 ATOM 26 C CD1 . PHE A 1 3 ? 18.607 12.135 34.512 1.00 10.72 ? 84 PHE A CD1 1 ATOM 27 C CD2 . PHE A 1 3 ? 19.614 12.473 32.361 1.00 10.18 ? 84 PHE A CD2 1 ATOM 28 C CE1 . PHE A 1 3 ? 19.455 11.063 34.756 1.00 9.43 ? 84 PHE A CE1 1 ATOM 29 C CE2 . PHE A 1 3 ? 20.438 11.388 32.644 1.00 9.87 ? 84 PHE A CE2 1 ATOM 30 C CZ . PHE A 1 3 ? 20.374 10.687 33.821 1.00 7.99 ? 84 PHE A CZ 1 ATOM 31 N N . ASN A 1 4 ? 15.558 15.967 34.741 1.00 10.30 ? 85 ASN A N 1 ATOM 32 C CA . ASN A 1 4 ? 14.969 17.294 34.936 1.00 12.23 ? 85 ASN A CA 1 ATOM 33 C C . ASN A 1 4 ? 15.980 18.387 34.610 1.00 12.03 ? 85 ASN A C 1 ATOM 34 O O . ASN A 1 4 ? 17.166 18.259 34.894 1.00 15.08 ? 85 ASN A O 1 ATOM 35 C CB . ASN A 1 4 ? 14.520 17.477 36.403 1.00 11.99 ? 85 ASN A CB 1 ATOM 36 C CG . ASN A 1 4 ? 14.035 18.866 36.771 1.00 12.69 ? 85 ASN A CG 1 ATOM 37 O OD1 . ASN A 1 4 ? 13.043 19.289 36.195 1.00 14.46 ? 85 ASN A OD1 1 ATOM 38 N ND2 . ASN A 1 4 ? 14.652 19.712 37.588 1.00 11.55 ? 85 ASN A ND2 1 ATOM 39 N N . ASN A 1 5 ? 15.586 19.548 34.116 1.00 15.33 ? 86 ASN A N 1 ATOM 40 C CA . ASN A 1 5 ? 16.520 20.600 33.811 1.00 16.53 ? 86 ASN A CA 1 ATOM 41 C C . ASN A 1 5 ? 15.959 21.830 34.429 1.00 15.06 ? 86 ASN A C 1 ATOM 42 O O . ASN A 1 5 ? 14.779 22.115 34.307 1.00 16.02 ? 86 ASN A O 1 ATOM 43 C CB . ASN A 1 5 ? 16.633 20.896 32.353 1.00 20.55 ? 86 ASN A CB 1 ATOM 44 C CG . ASN A 1 5 ? 17.178 19.707 31.600 1.00 24.87 ? 86 ASN A CG 1 ATOM 45 O OD1 . ASN A 1 5 ? 18.201 19.132 31.984 1.00 24.86 ? 86 ASN A OD1 1 ATOM 46 N ND2 . ASN A 1 5 ? 16.457 19.287 30.555 1.00 27.98 ? 86 ASN A ND2 1 ATOM 47 N N . LEU A 1 6 ? 16.784 22.539 35.158 1.00 14.70 ? 87 LEU A N 1 ATOM 48 C CA . LEU A 1 6 ? 16.462 23.799 35.786 1.00 12.49 ? 87 LEU A CA 1 ATOM 49 C C . LEU A 1 6 ? 16.264 24.922 34.786 1.00 12.29 ? 87 LEU A C 1 ATOM 50 O O . LEU A 1 6 ? 17.164 25.727 34.553 1.00 13.22 ? 87 LEU A O 1 ATOM 51 C CB . LEU A 1 6 ? 17.589 24.119 36.763 1.00 11.18 ? 87 LEU A CB 1 ATOM 52 C CG . LEU A 1 6 ? 18.010 23.080 37.795 1.00 9.68 ? 87 LEU A CG 1 ATOM 53 C CD1 . LEU A 1 6 ? 19.246 23.534 38.541 1.00 7.28 ? 87 LEU A CD1 1 ATOM 54 C CD2 . LEU A 1 6 ? 16.846 22.836 38.721 1.00 8.25 ? 87 LEU A CD2 1 ATOM 55 N N . THR A 1 7 ? 15.089 24.965 34.238 1.00 11.95 ? 88 THR A N 1 ATOM 56 C CA . THR A 1 7 ? 14.577 25.893 33.253 1.00 13.81 ? 88 THR A CA 1 ATOM 57 C C . THR A 1 7 ? 14.026 27.261 33.683 1.00 16.50 ? 88 THR A C 1 ATOM 58 O O . THR A 1 7 ? 14.173 28.255 32.978 1.00 16.23 ? 88 THR A O 1 ATOM 59 C CB . THR A 1 7 ? 13.623 24.998 32.515 1.00 12.80 ? 88 THR A CB 1 ATOM 60 O OG1 . THR A 1 7 ? 14.544 24.387 31.632 1.00 11.91 ? 88 THR A OG1 1 ATOM 61 C CG2 . THR A 1 7 ? 12.334 25.589 31.926 1.00 13.21 ? 88 THR A CG2 1 ATOM 62 N N . LYS A 1 8 ? 13.329 27.280 34.833 1.00 16.37 ? 89 LYS A N 1 ATOM 63 C CA . LYS A 1 8 ? 12.582 28.415 35.333 1.00 13.59 ? 89 LYS A CA 1 ATOM 64 C C . LYS A 1 8 ? 13.345 29.259 36.314 1.00 13.75 ? 89 LYS A C 1 ATOM 65 O O . LYS A 1 8 ? 14.423 28.877 36.772 1.00 13.28 ? 89 LYS A O 1 ATOM 66 C CB . LYS A 1 8 ? 11.345 27.887 35.989 1.00 14.66 ? 89 LYS A CB 1 ATOM 67 C CG . LYS A 1 8 ? 10.557 27.055 35.030 1.00 15.68 ? 89 LYS A CG 1 ATOM 68 C CD . LYS A 1 8 ? 9.385 26.546 35.766 1.00 17.20 ? 89 LYS A CD 1 ATOM 69 C CE . LYS A 1 8 ? 8.673 25.492 34.954 1.00 17.19 ? 89 LYS A CE 1 ATOM 70 N NZ . LYS A 1 8 ? 7.514 24.998 35.679 1.00 19.82 ? 89 LYS A NZ 1 ATOM 71 N N . GLY A 1 9 ? 12.786 30.427 36.606 1.00 9.40 ? 90 GLY A N 1 ATOM 72 C CA . GLY A 1 9 ? 13.330 31.361 37.595 1.00 5.50 ? 90 GLY A CA 1 ATOM 73 C C . GLY A 1 9 ? 12.393 31.308 38.795 1.00 6.20 ? 90 GLY A C 1 ATOM 74 O O . GLY A 1 9 ? 11.352 30.623 38.676 1.00 5.73 ? 90 GLY A O 1 ATOM 75 N N . LEU A 1 10 ? 12.695 31.933 39.936 1.00 5.96 ? 91 LEU A N 1 ATOM 76 C CA . LEU A 1 10 ? 11.831 31.783 41.103 1.00 8.03 ? 91 LEU A CA 1 ATOM 77 C C . LEU A 1 10 ? 10.654 32.715 40.954 1.00 9.05 ? 91 LEU A C 1 ATOM 78 O O . LEU A 1 10 ? 10.863 33.809 40.419 1.00 11.67 ? 91 LEU A O 1 ATOM 79 C CB . LEU A 1 10 ? 12.556 32.165 42.389 1.00 9.41 ? 91 LEU A CB 1 ATOM 80 C CG . LEU A 1 10 ? 13.853 31.486 42.783 1.00 10.69 ? 91 LEU A CG 1 ATOM 81 C CD1 . LEU A 1 10 ? 14.450 32.179 43.989 1.00 11.29 ? 91 LEU A CD1 1 ATOM 82 C CD2 . LEU A 1 10 ? 13.598 30.051 43.130 1.00 12.41 ? 91 LEU A CD2 1 ATOM 83 N N . CYS A 1 11 ? 9.449 32.361 41.375 1.00 11.20 ? 92 CYS A N 1 ATOM 84 C CA . CYS A 1 11 ? 8.330 33.289 41.389 1.00 15.71 ? 92 CYS A CA 1 ATOM 85 C C . CYS A 1 11 ? 8.638 34.396 42.427 1.00 17.07 ? 92 CYS A C 1 ATOM 86 O O . CYS A 1 11 ? 9.666 34.346 43.146 1.00 20.25 ? 92 CYS A O 1 ATOM 87 C CB . CYS A 1 11 ? 6.995 32.552 41.780 1.00 15.15 ? 92 CYS A CB 1 ATOM 88 S SG . CYS A 1 11 ? 6.625 30.948 41.013 1.00 13.88 ? 92 CYS A SG 1 ATOM 89 N N . THR A 1 12 ? 7.795 35.433 42.578 1.00 13.53 ? 93 THR A N 1 ATOM 90 C CA . THR A 1 12 ? 8.100 36.430 43.577 1.00 12.17 ? 93 THR A CA 1 ATOM 91 C C . THR A 1 12 ? 7.350 36.118 44.853 1.00 10.08 ? 93 THR A C 1 ATOM 92 O O . THR A 1 12 ? 6.207 35.650 44.896 1.00 9.00 ? 93 THR A O 1 ATOM 93 C CB . THR A 1 12 ? 7.752 37.795 43.001 1.00 12.33 ? 93 THR A CB 1 ATOM 94 O OG1 . THR A 1 12 ? 6.404 37.715 42.646 1.00 16.55 ? 93 THR A OG1 1 ATOM 95 C CG2 . THR A 1 12 ? 8.528 38.152 41.705 1.00 13.62 ? 93 THR A CG2 1 ATOM 96 N N . ILE A 1 13 ? 8.162 36.192 45.882 1.00 7.29 ? 94 ILE A N 1 ATOM 97 C CA . ILE A 1 13 ? 7.803 35.847 47.249 1.00 6.49 ? 94 ILE A CA 1 ATOM 98 C C . ILE A 1 13 ? 7.293 37.100 47.913 1.00 8.39 ? 94 ILE A C 1 ATOM 99 O O . ILE A 1 13 ? 8.121 37.944 48.309 1.00 7.78 ? 94 ILE A O 1 ATOM 100 C CB . ILE A 1 13 ? 9.062 35.307 47.929 1.00 4.68 ? 94 ILE A CB 1 ATOM 101 C CG1 . ILE A 1 13 ? 9.690 34.165 47.133 1.00 2.61 ? 94 ILE A CG1 1 ATOM 102 C CG2 . ILE A 1 13 ? 8.675 34.902 49.333 1.00 4.04 ? 94 ILE A CG2 1 ATOM 103 C CD1 . ILE A 1 13 ? 11.179 33.886 47.383 1.00 4.44 ? 94 ILE A CD1 1 ATOM 104 N N . ASN A 1 14 ? 5.973 37.296 47.960 1.00 8.84 ? 95 ASN A N 1 ATOM 105 C CA . ASN A 1 14 ? 5.409 38.410 48.707 1.00 7.43 ? 95 ASN A CA 1 ATOM 106 C C . ASN A 1 14 ? 4.974 38.032 50.121 1.00 8.84 ? 95 ASN A C 1 ATOM 107 O O . ASN A 1 14 ? 4.707 38.931 50.946 1.00 8.40 ? 95 ASN A O 1 ATOM 108 C CB . ASN A 1 14 ? 4.258 38.982 47.951 1.00 9.21 ? 95 ASN A CB 1 ATOM 109 C CG . ASN A 1 14 ? 4.761 39.938 46.871 1.00 11.63 ? 95 ASN A CG 1 ATOM 110 O OD1 . ASN A 1 14 ? 4.375 39.971 45.712 1.00 13.40 ? 95 ASN A OD1 1 ATOM 111 N ND2 . ASN A 1 14 ? 5.656 40.837 47.191 1.00 11.86 ? 95 ASN A ND2 1 ATOM 112 N N . SER A 1 15 ? 4.955 36.713 50.431 1.00 8.84 ? 96 SER A N 1 ATOM 113 C CA . SER A 1 15 ? 4.652 36.195 51.773 1.00 7.40 ? 96 SER A CA 1 ATOM 114 C C . SER A 1 15 ? 4.799 34.650 51.818 1.00 8.45 ? 96 SER A C 1 ATOM 115 O O . SER A 1 15 ? 5.077 34.001 50.793 1.00 8.93 ? 96 SER A O 1 ATOM 116 C CB . SER A 1 15 ? 3.209 36.615 52.191 1.00 5.97 ? 96 SER A CB 1 ATOM 117 O OG . SER A 1 15 ? 2.046 35.994 51.613 1.00 4.30 ? 96 SER A OG 1 ATOM 118 N N . TRP A 1 16 ? 4.588 33.964 52.940 1.00 8.25 ? 97 TRP A N 1 ATOM 119 C CA . TRP A 1 16 ? 4.697 32.512 52.993 1.00 10.66 ? 97 TRP A CA 1 ATOM 120 C C . TRP A 1 16 ? 3.407 31.860 53.480 1.00 9.95 ? 97 TRP A C 1 ATOM 121 O O . TRP A 1 16 ? 2.775 32.450 54.353 1.00 9.52 ? 97 TRP A O 1 ATOM 122 C CB . TRP A 1 16 ? 5.846 32.101 53.939 1.00 10.38 ? 97 TRP A CB 1 ATOM 123 C CG . TRP A 1 16 ? 7.195 32.642 53.521 1.00 11.28 ? 97 TRP A CG 1 ATOM 124 C CD1 . TRP A 1 16 ? 7.559 33.927 53.853 1.00 10.17 ? 97 TRP A CD1 1 ATOM 125 C CD2 . TRP A 1 16 ? 8.097 32.014 52.685 1.00 11.26 ? 97 TRP A CD2 1 ATOM 126 N NE1 . TRP A 1 16 ? 8.679 34.134 53.195 1.00 12.42 ? 97 TRP A NE1 1 ATOM 127 C CE2 . TRP A 1 16 ? 9.035 33.028 52.486 1.00 11.48 ? 97 TRP A CE2 1 ATOM 128 C CE3 . TRP A 1 16 ? 8.255 30.791 52.063 1.00 11.64 ? 97 TRP A CE3 1 ATOM 129 C CZ2 . TRP A 1 16 ? 10.117 32.799 51.659 1.00 9.76 ? 97 TRP A CZ2 1 ATOM 130 C CZ3 . TRP A 1 16 ? 9.336 30.589 51.234 1.00 11.78 ? 97 TRP A CZ3 1 ATOM 131 C CH2 . TRP A 1 16 ? 10.265 31.583 51.044 1.00 10.26 ? 97 TRP A CH2 1 ATOM 132 N N . HIS A 1 17 ? 2.990 30.655 53.009 1.00 8.34 ? 98 HIS A N 1 ATOM 133 C CA . HIS A 1 17 ? 1.774 29.939 53.445 1.00 9.18 ? 98 HIS A CA 1 ATOM 134 C C . HIS A 1 17 ? 2.112 28.578 54.044 1.00 11.22 ? 98 HIS A C 1 ATOM 135 O O . HIS A 1 17 ? 3.169 28.051 53.685 1.00 12.54 ? 98 HIS A O 1 ATOM 136 C CB . HIS A 1 17 ? 0.825 29.743 52.253 1.00 7.66 ? 98 HIS A CB 1 ATOM 137 C CG . HIS A 1 17 ? 1.194 28.778 51.128 1.00 5.26 ? 98 HIS A CG 1 ATOM 138 N ND1 . HIS A 1 17 ? 1.662 29.110 49.926 1.00 7.80 ? 98 HIS A ND1 1 ATOM 139 C CD2 . HIS A 1 17 ? 1.098 27.388 51.154 1.00 5.07 ? 98 HIS A CD2 1 ATOM 140 C CE1 . HIS A 1 17 ? 1.883 28.002 49.223 1.00 4.09 ? 98 HIS A CE1 1 ATOM 141 N NE2 . HIS A 1 17 ? 1.533 26.982 49.982 1.00 6.74 ? 98 HIS A NE2 1 ATOM 142 N N . ILE A 1 18 ? 1.342 27.908 54.957 1.00 10.93 ? 99 ILE A N 1 ATOM 143 C CA . ILE A 1 18 ? 1.722 26.558 55.430 1.00 9.28 ? 99 ILE A CA 1 ATOM 144 C C . ILE A 1 18 ? 1.670 25.542 54.315 1.00 10.32 ? 99 ILE A C 1 ATOM 145 O O . ILE A 1 18 ? 0.755 25.558 53.477 1.00 12.05 ? 99 ILE A O 1 ATOM 146 C CB . ILE A 1 18 ? 0.824 25.841 56.496 1.00 5.73 ? 99 ILE A CB 1 ATOM 147 C CG1 . ILE A 1 18 ? -0.277 26.752 56.852 1.00 6.88 ? 99 ILE A CG1 1 ATOM 148 C CG2 . ILE A 1 18 ? 1.640 25.417 57.723 1.00 2.73 ? 99 ILE A CG2 1 ATOM 149 C CD1 . ILE A 1 18 ? -1.537 26.344 56.108 1.00 6.73 ? 99 ILE A CD1 1 ATOM 150 N N . TYR A 1 19 ? 2.643 24.626 54.354 1.00 11.10 ? 100 TYR A N 1 ATOM 151 C CA . TYR A 1 19 ? 2.752 23.572 53.394 1.00 10.70 ? 100 TYR A CA 1 ATOM 152 C C . TYR A 1 19 ? 2.515 22.296 54.214 1.00 8.83 ? 100 TYR A C 1 ATOM 153 O O . TYR A 1 19 ? 1.447 21.709 54.100 1.00 10.74 ? 100 TYR A O 1 ATOM 154 C CB . TYR A 1 19 ? 4.133 23.700 52.772 1.00 8.57 ? 100 TYR A CB 1 ATOM 155 C CG . TYR A 1 19 ? 4.372 22.600 51.764 1.00 10.21 ? 100 TYR A CG 1 ATOM 156 C CD1 . TYR A 1 19 ? 3.689 22.672 50.576 1.00 11.61 ? 100 TYR A CD1 1 ATOM 157 C CD2 . TYR A 1 19 ? 5.201 21.529 52.060 1.00 12.08 ? 100 TYR A CD2 1 ATOM 158 C CE1 . TYR A 1 19 ? 3.826 21.683 49.666 1.00 11.47 ? 100 TYR A CE1 1 ATOM 159 C CE2 . TYR A 1 19 ? 5.346 20.525 51.149 1.00 11.36 ? 100 TYR A CE2 1 ATOM 160 C CZ . TYR A 1 19 ? 4.649 20.638 49.977 1.00 12.04 ? 100 TYR A CZ 1 ATOM 161 O OH . TYR A 1 19 ? 4.739 19.660 49.043 1.00 12.32 ? 100 TYR A OH 1 ATOM 162 N N . GLY A 1 20 ? 3.427 21.824 55.047 1.00 9.61 ? 101 GLY A N 1 ATOM 163 C CA . GLY A 1 20 ? 3.181 20.687 55.930 1.00 8.39 ? 101 GLY A CA 1 ATOM 164 C C . GLY A 1 20 ? 3.591 20.880 57.390 1.00 7.23 ? 101 GLY A C 1 ATOM 165 O O . GLY A 1 20 ? 4.426 21.688 57.725 1.00 9.71 ? 101 GLY A O 1 ATOM 166 N N . LYS A 1 21 ? 2.907 20.209 58.289 1.00 10.52 ? 102 LYS A N 1 ATOM 167 C CA . LYS A 1 21 ? 3.231 20.171 59.725 1.00 9.48 ? 102 LYS A CA 1 ATOM 168 C C . LYS A 1 21 ? 2.813 18.789 60.142 1.00 8.69 ? 102 LYS A C 1 ATOM 169 O O . LYS A 1 21 ? 1.693 18.388 59.820 1.00 8.01 ? 102 LYS A O 1 ATOM 170 C CB . LYS A 1 21 ? 2.417 21.150 60.569 1.00 8.96 ? 102 LYS A CB 1 ATOM 171 C CG . LYS A 1 21 ? 2.953 21.317 61.977 1.00 8.52 ? 102 LYS A CG 1 ATOM 172 C CD . LYS A 1 21 ? 2.108 22.333 62.745 1.00 7.35 ? 102 LYS A CD 1 ATOM 173 C CE . LYS A 1 21 ? 2.755 22.809 64.059 1.00 7.55 ? 102 LYS A CE 1 ATOM 174 N NZ . LYS A 1 21 ? 2.883 21.656 64.917 1.00 3.95 ? 102 LYS A NZ 1 ATOM 175 N N . ASP A 1 22 ? 3.680 18.048 60.824 1.00 11.40 ? 103 ASP A N 1 ATOM 176 C CA . ASP A 1 22 ? 3.300 16.713 61.264 1.00 12.27 ? 103 ASP A CA 1 ATOM 177 C C . ASP A 1 22 ? 2.943 16.522 62.730 1.00 13.38 ? 103 ASP A C 1 ATOM 178 O O . ASP A 1 22 ? 2.550 15.424 63.100 1.00 15.62 ? 103 ASP A O 1 ATOM 179 C CB . ASP A 1 22 ? 4.399 15.725 60.877 1.00 14.18 ? 103 ASP A CB 1 ATOM 180 C CG . ASP A 1 22 ? 5.759 15.835 61.558 1.00 10.89 ? 103 ASP A CG 1 ATOM 181 O OD1 . ASP A 1 22 ? 5.964 16.680 62.416 1.00 15.87 ? 103 ASP A OD1 1 ATOM 182 O OD2 . ASP A 1 22 ? 6.613 15.054 61.189 1.00 15.43 ? 103 ASP A OD2 1 ATOM 183 N N . ASN A 1 23 ? 3.128 17.460 63.664 1.00 13.73 ? 104 ASN A N 1 ATOM 184 C CA . ASN A 1 23 ? 2.737 17.336 65.083 1.00 10.81 ? 104 ASN A CA 1 ATOM 185 C C . ASN A 1 23 ? 3.277 16.017 65.653 1.00 9.98 ? 104 ASN A C 1 ATOM 186 O O . ASN A 1 23 ? 2.656 15.341 66.472 1.00 10.96 ? 104 ASN A O 1 ATOM 187 C CB . ASN A 1 23 ? 1.206 17.346 65.279 1.00 10.11 ? 104 ASN A CB 1 ATOM 188 C CG . ASN A 1 23 ? 0.524 18.560 64.689 1.00 10.44 ? 104 ASN A CG 1 ATOM 189 O OD1 . ASN A 1 23 ? 0.704 19.686 65.129 1.00 11.92 ? 104 ASN A OD1 1 ATOM 190 N ND2 . ASN A 1 23 ? -0.280 18.411 63.642 1.00 9.44 ? 104 ASN A ND2 1 ATOM 191 N N . ALA A 1 24 ? 4.498 15.640 65.300 1.00 9.41 ? 105 ALA A N 1 ATOM 192 C CA . ALA A 1 24 ? 5.102 14.348 65.697 1.00 8.02 ? 105 ALA A CA 1 ATOM 193 C C . ALA A 1 24 ? 5.270 13.972 67.182 1.00 7.24 ? 105 ALA A C 1 ATOM 194 O O . ALA A 1 24 ? 4.906 12.881 67.627 1.00 6.06 ? 105 ALA A O 1 ATOM 195 C CB . ALA A 1 24 ? 6.467 14.260 65.035 1.00 6.82 ? 105 ALA A CB 1 ATOM 196 N N . VAL A 1 25 ? 5.730 14.924 68.017 1.00 6.62 ? 106 VAL A N 1 ATOM 197 C CA . VAL A 1 25 ? 6.053 14.669 69.401 1.00 5.46 ? 106 VAL A CA 1 ATOM 198 C C . VAL A 1 25 ? 4.703 14.573 70.121 1.00 7.64 ? 106 VAL A C 1 ATOM 199 O O . VAL A 1 25 ? 4.609 13.731 71.023 1.00 6.80 ? 106 VAL A O 1 ATOM 200 C CB . VAL A 1 25 ? 6.918 15.823 69.951 1.00 7.09 ? 106 VAL A CB 1 ATOM 201 C CG1 . VAL A 1 25 ? 7.338 15.566 71.412 1.00 8.12 ? 106 VAL A CG1 1 ATOM 202 C CG2 . VAL A 1 25 ? 8.194 15.923 69.114 1.00 7.03 ? 106 VAL A CG2 1 ATOM 203 N N . ARG A 1 26 ? 3.664 15.404 69.797 1.00 8.48 ? 107 ARG A N 1 ATOM 204 C CA . ARG A 1 26 ? 2.288 15.317 70.352 1.00 9.88 ? 107 ARG A CA 1 ATOM 205 C C . ARG A 1 26 ? 1.688 13.947 70.223 1.00 10.74 ? 107 ARG A C 1 ATOM 206 O O . ARG A 1 26 ? 1.277 13.334 71.209 1.00 13.01 ? 107 ARG A O 1 ATOM 207 C CB . ARG A 1 26 ? 1.265 16.223 69.661 1.00 9.54 ? 107 ARG A CB 1 ATOM 208 C CG . ARG A 1 26 ? 1.312 17.674 70.054 1.00 11.73 ? 107 ARG A CG 1 ATOM 209 C CD . ARG A 1 26 ? 0.571 18.630 69.123 1.00 13.32 ? 107 ARG A CD 1 ATOM 210 N NE . ARG A 1 26 ? -0.883 18.511 69.154 1.00 14.44 ? 107 ARG A NE 1 ATOM 211 C CZ . ARG A 1 26 ? -1.662 18.992 70.141 1.00 15.30 ? 107 ARG A CZ 1 ATOM 212 N NH1 . ARG A 1 26 ? -1.177 19.716 71.149 1.00 14.75 ? 107 ARG A NH1 1 ATOM 213 N NH2 . ARG A 1 26 ? -2.984 18.809 70.068 1.00 15.65 ? 107 ARG A NH2 1 ATOM 214 N N . ILE A 1 27 ? 1.631 13.456 68.989 1.00 13.53 ? 108 ILE A N 1 ATOM 215 C CA . ILE A 1 27 ? 1.107 12.129 68.697 1.00 12.91 ? 108 ILE A CA 1 ATOM 216 C C . ILE A 1 27 ? 2.090 11.096 69.248 1.00 12.58 ? 108 ILE A C 1 ATOM 217 O O . ILE A 1 27 ? 1.665 10.034 69.710 1.00 14.83 ? 108 ILE A O 1 ATOM 218 C CB . ILE A 1 27 ? 0.913 12.030 67.159 1.00 12.30 ? 108 ILE A CB 1 ATOM 219 C CG1 . ILE A 1 27 ? -0.110 13.101 66.746 1.00 11.66 ? 108 ILE A CG1 1 ATOM 220 C CG2 . ILE A 1 27 ? 0.461 10.613 66.751 1.00 11.75 ? 108 ILE A CG2 1 ATOM 221 C CD1 . ILE A 1 27 ? -0.374 13.340 65.250 1.00 9.76 ? 108 ILE A CD1 1 ATOM 222 N N . GLY A 1 28 ? 3.393 11.336 69.307 1.00 9.71 ? 109 GLY A N 1 ATOM 223 C CA . GLY A 1 28 ? 4.327 10.396 69.893 1.00 8.44 ? 109 GLY A CA 1 ATOM 224 C C . GLY A 1 28 ? 4.123 10.093 71.376 1.00 8.06 ? 109 GLY A C 1 ATOM 225 O O . GLY A 1 28 ? 4.600 9.092 71.917 1.00 8.12 ? 109 GLY A O 1 ATOM 226 N N . GLU A 1 29 ? 3.365 10.909 72.101 1.00 9.30 ? 110 GLU A N 1 ATOM 227 C CA . GLU A 1 29 ? 3.102 10.642 73.513 1.00 8.25 ? 110 GLU A CA 1 ATOM 228 C C . GLU A 1 29 ? 2.227 9.402 73.603 1.00 9.53 ? 110 GLU A C 1 ATOM 229 O O . GLU A 1 29 ? 2.152 8.840 74.687 1.00 9.46 ? 110 GLU A O 1 ATOM 230 C CB . GLU A 1 29 ? 2.441 11.901 74.094 1.00 7.78 ? 110 GLU A CB 1 ATOM 231 C CG . GLU A 1 29 ? 2.217 11.999 75.583 1.00 9.55 ? 110 GLU A CG 1 ATOM 232 C CD . GLU A 1 29 ? 0.941 11.292 76.039 1.00 12.94 ? 110 GLU A CD 1 ATOM 233 O OE1 . GLU A 1 29 ? -0.134 11.543 75.466 1.00 12.60 ? 110 GLU A OE1 1 ATOM 234 O OE2 . GLU A 1 29 ? 1.011 10.440 76.937 1.00 13.77 ? 110 GLU A OE2 1 ATOM 235 N N . ASP A 1 30 ? 1.570 8.886 72.539 1.00 12.42 ? 111 ASP A N 1 ATOM 236 C CA . ASP A 1 30 ? 0.690 7.739 72.684 1.00 14.27 ? 111 ASP A CA 1 ATOM 237 C C . ASP A 1 30 ? 0.544 6.988 71.373 1.00 15.50 ? 111 ASP A C 1 ATOM 238 O O . ASP A 1 30 ? -0.542 6.538 70.971 1.00 19.07 ? 111 ASP A O 1 ATOM 239 C CB . ASP A 1 30 ? -0.631 8.273 73.186 1.00 15.93 ? 111 ASP A CB 1 ATOM 240 C CG . ASP A 1 30 ? -1.697 7.227 73.442 1.00 17.70 ? 111 ASP A CG 1 ATOM 241 O OD1 . ASP A 1 30 ? -1.402 6.216 74.080 1.00 18.94 ? 111 ASP A OD1 1 ATOM 242 O OD2 . ASP A 1 30 ? -2.822 7.435 72.990 1.00 20.22 ? 111 ASP A OD2 1 ATOM 243 N N . SER A 1 31 ? 1.667 6.850 70.666 1.00 13.85 ? 112 SER A N 1 ATOM 244 C CA . SER A 1 31 ? 1.724 6.189 69.370 1.00 11.19 ? 112 SER A CA 1 ATOM 245 C C . SER A 1 31 ? 3.123 5.656 69.125 1.00 10.13 ? 112 SER A C 1 ATOM 246 O O . SER A 1 31 ? 4.051 6.048 69.855 1.00 10.95 ? 112 SER A O 1 ATOM 247 C CB . SER A 1 31 ? 1.391 7.166 68.295 1.00 12.64 ? 112 SER A CB 1 ATOM 248 O OG . SER A 1 31 ? -0.008 7.395 68.348 1.00 15.66 ? 112 SER A OG 1 ATOM 249 N N . ASP A 1 32 ? 3.341 4.788 68.142 1.00 6.32 ? 113 ASP A N 1 ATOM 250 C CA . ASP A 1 32 ? 4.680 4.298 67.889 1.00 5.37 ? 113 ASP A CA 1 ATOM 251 C C . ASP A 1 32 ? 5.428 5.074 66.837 1.00 6.47 ? 113 ASP A C 1 ATOM 252 O O . ASP A 1 32 ? 5.588 4.683 65.678 1.00 6.95 ? 113 ASP A O 1 ATOM 253 C CB . ASP A 1 32 ? 4.560 2.834 67.528 1.00 6.40 ? 113 ASP A CB 1 ATOM 254 C CG . ASP A 1 32 ? 3.927 1.968 68.601 1.00 8.19 ? 113 ASP A CG 1 ATOM 255 O OD1 . ASP A 1 32 ? 4.136 2.193 69.781 1.00 9.42 ? 113 ASP A OD1 1 ATOM 256 O OD2 . ASP A 1 32 ? 3.187 1.063 68.261 1.00 10.88 ? 113 ASP A OD2 1 ATOM 257 N N . VAL A 1 33 ? 5.846 6.238 67.300 1.00 7.41 ? 114 VAL A N 1 ATOM 258 C CA . VAL A 1 33 ? 6.579 7.253 66.553 1.00 6.30 ? 114 VAL A CA 1 ATOM 259 C C . VAL A 1 33 ? 8.035 7.165 66.909 1.00 7.33 ? 114 VAL A C 1 ATOM 260 O O . VAL A 1 33 ? 8.396 7.059 68.081 1.00 8.84 ? 114 VAL A O 1 ATOM 261 C CB . VAL A 1 33 ? 6.011 8.648 66.909 1.00 8.27 ? 114 VAL A CB 1 ATOM 262 C CG1 . VAL A 1 33 ? 6.873 9.715 66.280 1.00 8.36 ? 114 VAL A CG1 1 ATOM 263 C CG2 . VAL A 1 33 ? 4.557 8.793 66.405 1.00 8.52 ? 114 VAL A CG2 1 ATOM 264 N N . LEU A 1 34 ? 8.877 7.207 65.904 1.00 8.31 ? 115 LEU A N 1 ATOM 265 C CA . LEU A 1 34 ? 10.324 7.104 65.996 1.00 9.10 ? 115 LEU A CA 1 ATOM 266 C C . LEU A 1 34 ? 10.967 8.370 66.539 1.00 9.92 ? 115 LEU A C 1 ATOM 267 O O . LEU A 1 34 ? 10.455 9.470 66.320 1.00 12.52 ? 115 LEU A O 1 ATOM 268 C CB . LEU A 1 34 ? 10.847 6.768 64.578 1.00 10.43 ? 115 LEU A CB 1 ATOM 269 C CG . LEU A 1 34 ? 10.634 5.318 64.089 1.00 10.10 ? 115 LEU A CG 1 ATOM 270 C CD1 . LEU A 1 34 ? 10.728 5.155 62.575 1.00 11.34 ? 115 LEU A CD1 1 ATOM 271 C CD2 . LEU A 1 34 ? 11.681 4.492 64.816 1.00 10.80 ? 115 LEU A CD2 1 ATOM 272 N N . VAL A 1 35 ? 12.133 8.298 67.220 1.00 9.95 ? 116 VAL A N 1 ATOM 273 C CA . VAL A 1 35 ? 12.816 9.493 67.751 1.00 6.74 ? 116 VAL A CA 1 ATOM 274 C C . VAL A 1 35 ? 13.648 9.989 66.559 1.00 5.59 ? 116 VAL A C 1 ATOM 275 O O . VAL A 1 35 ? 14.326 9.131 65.995 1.00 4.42 ? 116 VAL A O 1 ATOM 276 C CB . VAL A 1 35 ? 13.772 9.105 68.933 1.00 7.10 ? 116 VAL A CB 1 ATOM 277 C CG1 . VAL A 1 35 ? 14.856 10.170 69.169 1.00 2.32 ? 116 VAL A CG1 1 ATOM 278 C CG2 . VAL A 1 35 ? 12.968 9.039 70.236 1.00 5.33 ? 116 VAL A CG2 1 ATOM 279 N N . THR A 1 36 ? 13.656 11.256 66.121 1.00 6.43 ? 117 THR A N 1 ATOM 280 C CA . THR A 1 36 ? 14.522 11.673 65.016 1.00 7.46 ? 117 THR A CA 1 ATOM 281 C C . THR A 1 36 ? 15.317 12.933 65.373 1.00 8.45 ? 117 THR A C 1 ATOM 282 O O . THR A 1 36 ? 15.262 13.394 66.524 1.00 10.23 ? 117 THR A O 1 ATOM 283 C CB . THR A 1 36 ? 13.644 11.951 63.725 1.00 6.90 ? 117 THR A CB 1 ATOM 284 O OG1 . THR A 1 36 ? 12.563 12.826 64.083 1.00 7.03 ? 117 THR A OG1 1 ATOM 285 C CG2 . THR A 1 36 ? 13.137 10.675 63.104 1.00 6.85 ? 117 THR A CG2 1 ATOM 286 N N . ARG A 1 37 ? 16.045 13.432 64.382 1.00 9.01 ? 118 ARG A N 1 ATOM 287 C CA . ARG A 1 37 ? 16.529 14.802 64.328 1.00 9.00 ? 118 ARG A CA 1 ATOM 288 C C . ARG A 1 37 ? 17.089 14.936 62.903 1.00 9.11 ? 118 ARG A C 1 ATOM 289 O O . ARG A 1 37 ? 16.984 14.012 62.073 1.00 7.51 ? 118 ARG A O 1 ATOM 290 C CB . ARG A 1 37 ? 17.615 15.099 65.403 1.00 10.89 ? 118 ARG A CB 1 ATOM 291 C CG . ARG A 1 37 ? 17.215 16.071 66.543 1.00 10.75 ? 118 ARG A CG 1 ATOM 292 C CD . ARG A 1 37 ? 18.294 17.078 66.932 1.00 11.24 ? 118 ARG A CD 1 ATOM 293 N NE . ARG A 1 37 ? 18.639 17.932 65.801 1.00 10.82 ? 118 ARG A NE 1 ATOM 294 C CZ . ARG A 1 37 ? 19.690 18.765 65.777 1.00 9.61 ? 118 ARG A CZ 1 ATOM 295 N NH1 . ARG A 1 37 ? 20.616 18.737 66.697 1.00 10.44 ? 118 ARG A NH1 1 ATOM 296 N NH2 . ARG A 1 37 ? 19.878 19.571 64.753 1.00 9.14 ? 118 ARG A NH2 1 ATOM 297 N N . GLU A 1 38 ? 17.732 16.049 62.610 1.00 7.16 ? 119 GLU A N 1 ATOM 298 C CA . GLU A 1 38 ? 18.109 16.446 61.268 1.00 7.64 ? 119 GLU A CA 1 ATOM 299 C C . GLU A 1 38 ? 17.107 16.163 60.137 1.00 7.65 ? 119 GLU A C 1 ATOM 300 O O . GLU A 1 38 ? 17.444 15.539 59.128 1.00 6.76 ? 119 GLU A O 1 ATOM 301 C CB . GLU A 1 38 ? 19.466 15.835 60.905 1.00 7.59 ? 119 GLU A CB 1 ATOM 302 C CG . GLU A 1 38 ? 20.643 16.308 61.757 1.00 8.44 ? 119 GLU A CG 1 ATOM 303 C CD . GLU A 1 38 ? 20.723 15.597 63.108 1.00 13.09 ? 119 GLU A CD 1 ATOM 304 O OE1 . GLU A 1 38 ? 20.610 14.365 63.154 1.00 18.17 ? 119 GLU A OE1 1 ATOM 305 O OE2 . GLU A 1 38 ? 20.906 16.250 64.140 1.00 14.38 ? 119 GLU A OE2 1 ATOM 306 N N . PRO A 1 39 ? 15.852 16.660 60.259 1.00 8.67 ? 120 PRO A N 1 ATOM 307 C CA . PRO A 1 39 ? 14.789 16.530 59.277 1.00 9.92 ? 120 PRO A CA 1 ATOM 308 C C . PRO A 1 39 ? 15.017 17.321 57.995 1.00 9.39 ? 120 PRO A C 1 ATOM 309 O O . PRO A 1 39 ? 15.830 18.252 57.973 1.00 8.53 ? 120 PRO A O 1 ATOM 310 C CB . PRO A 1 39 ? 13.523 16.994 59.979 1.00 11.21 ? 120 PRO A CB 1 ATOM 311 C CG . PRO A 1 39 ? 14.085 18.152 60.736 1.00 10.76 ? 120 PRO A CG 1 ATOM 312 C CD . PRO A 1 39 ? 15.369 17.544 61.312 1.00 9.33 ? 120 PRO A CD 1 ATOM 313 N N . TYR A 1 40 ? 14.258 17.006 56.949 1.00 9.43 ? 121 TYR A N 1 ATOM 314 C CA . TYR A 1 40 ? 14.241 17.792 55.692 1.00 8.81 ? 121 TYR A CA 1 ATOM 315 C C . TYR A 1 40 ? 13.125 17.344 54.759 1.00 7.86 ? 121 TYR A C 1 ATOM 316 O O . TYR A 1 40 ? 12.409 16.408 55.114 1.00 11.15 ? 121 TYR A O 1 ATOM 317 C CB . TYR A 1 40 ? 15.608 17.705 54.940 1.00 5.50 ? 121 TYR A CB 1 ATOM 318 C CG . TYR A 1 40 ? 16.254 16.412 54.487 1.00 4.71 ? 121 TYR A CG 1 ATOM 319 C CD1 . TYR A 1 40 ? 16.957 15.603 55.363 1.00 2.79 ? 121 TYR A CD1 1 ATOM 320 C CD2 . TYR A 1 40 ? 16.215 16.152 53.118 1.00 4.19 ? 121 TYR A CD2 1 ATOM 321 C CE1 . TYR A 1 40 ? 17.657 14.517 54.873 1.00 4.55 ? 121 TYR A CE1 1 ATOM 322 C CE2 . TYR A 1 40 ? 16.915 15.072 52.608 1.00 4.98 ? 121 TYR A CE2 1 ATOM 323 C CZ . TYR A 1 40 ? 17.629 14.288 53.498 1.00 4.88 ? 121 TYR A CZ 1 ATOM 324 O OH . TYR A 1 40 ? 18.378 13.265 52.981 1.00 4.82 ? 121 TYR A OH 1 ATOM 325 N N . VAL A 1 41 ? 12.877 17.929 53.588 1.00 7.93 ? 122 VAL A N 1 ATOM 326 C CA . VAL A 1 41 ? 11.759 17.552 52.711 1.00 6.73 ? 122 VAL A CA 1 ATOM 327 C C . VAL A 1 41 ? 12.360 17.354 51.309 1.00 7.48 ? 122 VAL A C 1 ATOM 328 O O . VAL A 1 41 ? 13.325 18.028 50.953 1.00 4.36 ? 122 VAL A O 1 ATOM 329 C CB . VAL A 1 41 ? 10.708 18.694 52.724 1.00 3.55 ? 122 VAL A CB 1 ATOM 330 C CG1 . VAL A 1 41 ? 9.528 18.339 51.793 1.00 4.71 ? 122 VAL A CG1 1 ATOM 331 C CG2 . VAL A 1 41 ? 10.126 18.869 54.106 1.00 2.00 ? 122 VAL A CG2 1 ATOM 332 N N . SER A 1 42 ? 11.883 16.419 50.490 1.00 8.64 ? 123 SER A N 1 ATOM 333 C CA . SER A 1 42 ? 12.363 16.292 49.134 1.00 7.87 ? 123 SER A CA 1 ATOM 334 C C . SER A 1 42 ? 11.245 15.767 48.273 1.00 7.86 ? 123 SER A C 1 ATOM 335 O O . SER A 1 42 ? 10.392 15.083 48.813 1.00 6.97 ? 123 SER A O 1 ATOM 336 C CB . SER A 1 42 ? 13.537 15.360 49.109 1.00 6.90 ? 123 SER A CB 1 ATOM 337 O OG . SER A 1 42 ? 14.232 15.430 47.860 1.00 7.57 ? 123 SER A OG 1 ATOM 338 N N . CYS A 1 43 ? 11.157 16.224 47.015 1.00 10.46 ? 124 CYS A N 1 ATOM 339 C CA . CYS A 1 43 ? 10.124 15.790 46.109 1.00 12.29 ? 124 CYS A CA 1 ATOM 340 C C . CYS A 1 43 ? 10.627 14.922 44.962 1.00 13.02 ? 124 CYS A C 1 ATOM 341 O O . CYS A 1 43 ? 11.749 15.033 44.443 1.00 14.87 ? 124 CYS A O 1 ATOM 342 C CB . CYS A 1 43 ? 9.378 17.007 45.506 1.00 12.54 ? 124 CYS A CB 1 ATOM 343 S SG . CYS A 1 43 ? 8.559 18.206 46.609 1.00 12.44 ? 124 CYS A SG 1 ATOM 344 N N . ASP A 1 44 ? 9.695 14.017 44.660 1.00 13.36 ? 125 ASP A N 1 ATOM 345 C CA . ASP A 1 44 ? 9.716 13.139 43.519 1.00 11.83 ? 125 ASP A CA 1 ATOM 346 C C . ASP A 1 44 ? 8.880 13.721 42.382 1.00 10.54 ? 125 ASP A C 1 ATOM 347 O O . ASP A 1 44 ? 8.142 14.652 42.675 1.00 11.23 ? 125 ASP A O 1 ATOM 348 C CB . ASP A 1 44 ? 9.153 11.838 43.927 1.00 12.94 ? 125 ASP A CB 1 ATOM 349 C CG . ASP A 1 44 ? 10.161 10.973 44.652 1.00 16.24 ? 125 ASP A CG 1 ATOM 350 O OD1 . ASP A 1 44 ? 11.301 11.376 44.924 1.00 17.86 ? 125 ASP A OD1 1 ATOM 351 O OD2 . ASP A 1 44 ? 9.774 9.842 44.918 1.00 17.74 ? 125 ASP A OD2 1 ATOM 352 N N . PRO A 1 45 ? 8.872 13.268 41.111 1.00 10.30 ? 126 PRO A N 1 ATOM 353 C CA . PRO A 1 45 ? 7.936 13.703 40.067 1.00 12.10 ? 126 PRO A CA 1 ATOM 354 C C . PRO A 1 45 ? 6.454 13.651 40.451 1.00 13.29 ? 126 PRO A C 1 ATOM 355 O O . PRO A 1 45 ? 5.661 14.467 39.991 1.00 11.39 ? 126 PRO A O 1 ATOM 356 C CB . PRO A 1 45 ? 8.226 12.819 38.908 1.00 11.74 ? 126 PRO A CB 1 ATOM 357 C CG . PRO A 1 45 ? 9.686 12.617 39.079 1.00 12.19 ? 126 PRO A CG 1 ATOM 358 C CD . PRO A 1 45 ? 9.811 12.304 40.556 1.00 9.83 ? 126 PRO A CD 1 ATOM 359 N N . ASP A 1 46 ? 6.078 12.677 41.300 1.00 12.53 ? 127 ASP A N 1 ATOM 360 C CA . ASP A 1 46 ? 4.709 12.484 41.756 1.00 14.29 ? 127 ASP A CA 1 ATOM 361 C C . ASP A 1 46 ? 4.427 12.644 43.240 1.00 13.20 ? 127 ASP A C 1 ATOM 362 O O . ASP A 1 46 ? 3.245 12.652 43.578 1.00 13.01 ? 127 ASP A O 1 ATOM 363 C CB . ASP A 1 46 ? 4.191 11.120 41.399 1.00 17.48 ? 127 ASP A CB 1 ATOM 364 C CG . ASP A 1 46 ? 5.183 10.039 41.757 1.00 21.48 ? 127 ASP A CG 1 ATOM 365 O OD1 . ASP A 1 46 ? 5.686 9.948 42.890 1.00 22.89 ? 127 ASP A OD1 1 ATOM 366 O OD2 . ASP A 1 46 ? 5.475 9.287 40.839 1.00 24.46 ? 127 ASP A OD2 1 ATOM 367 N N . GLU A 1 47 ? 5.365 12.627 44.182 1.00 12.01 ? 128 GLU A N 1 ATOM 368 C CA . GLU A 1 47 ? 4.968 13.035 45.503 1.00 13.16 ? 128 GLU A CA 1 ATOM 369 C C . GLU A 1 47 ? 6.092 13.729 46.221 1.00 13.14 ? 128 GLU A C 1 ATOM 370 O O . GLU A 1 47 ? 7.234 13.631 45.781 1.00 16.27 ? 128 GLU A O 1 ATOM 371 C CB . GLU A 1 47 ? 4.493 11.849 46.320 1.00 12.36 ? 128 GLU A CB 1 ATOM 372 C CG . GLU A 1 47 ? 5.427 10.695 46.473 1.00 13.33 ? 128 GLU A CG 1 ATOM 373 C CD . GLU A 1 47 ? 5.204 9.809 47.692 1.00 14.98 ? 128 GLU A CD 1 ATOM 374 O OE1 . GLU A 1 47 ? 4.580 10.203 48.675 1.00 14.00 ? 128 GLU A OE1 1 ATOM 375 O OE2 . GLU A 1 47 ? 5.726 8.700 47.696 1.00 19.82 ? 128 GLU A OE2 1 ATOM 376 N N . CYS A 1 48 ? 5.766 14.567 47.208 1.00 13.41 ? 129 CYS A N 1 ATOM 377 C CA . CYS A 1 48 ? 6.778 15.189 48.080 1.00 11.89 ? 129 CYS A CA 1 ATOM 378 C C . CYS A 1 48 ? 6.771 14.385 49.394 1.00 10.98 ? 129 CYS A C 1 ATOM 379 O O . CYS A 1 48 ? 5.704 13.897 49.788 1.00 9.38 ? 129 CYS A O 1 ATOM 380 C CB . CYS A 1 48 ? 6.435 16.650 48.321 1.00 9.83 ? 129 CYS A CB 1 ATOM 381 S SG . CYS A 1 48 ? 6.650 17.565 46.797 1.00 7.84 ? 129 CYS A SG 1 ATOM 382 N N . ARG A 1 49 ? 7.903 14.149 50.068 1.00 8.68 ? 130 ARG A N 1 ATOM 383 C CA . ARG A 1 49 ? 8.013 13.359 51.305 1.00 8.24 ? 130 ARG A CA 1 ATOM 384 C C . ARG A 1 49 ? 8.881 14.038 52.358 1.00 9.39 ? 130 ARG A C 1 ATOM 385 O O . ARG A 1 49 ? 9.659 14.917 51.975 1.00 10.64 ? 130 ARG A O 1 ATOM 386 C CB . ARG A 1 49 ? 8.602 12.010 50.984 1.00 8.40 ? 130 ARG A CB 1 ATOM 387 C CG . ARG A 1 49 ? 7.649 11.033 50.317 1.00 8.75 ? 130 ARG A CG 1 ATOM 388 C CD . ARG A 1 49 ? 8.370 9.778 49.820 1.00 8.66 ? 130 ARG A CD 1 ATOM 389 N NE . ARG A 1 49 ? 8.600 8.764 50.839 1.00 6.14 ? 130 ARG A NE 1 ATOM 390 C CZ . ARG A 1 49 ? 7.650 7.888 51.197 1.00 3.73 ? 130 ARG A CZ 1 ATOM 391 N NH1 . ARG A 1 49 ? 6.428 7.989 50.726 1.00 2.41 ? 130 ARG A NH1 1 ATOM 392 N NH2 . ARG A 1 49 ? 7.979 6.932 52.053 1.00 2.52 ? 130 ARG A NH2 1 ATOM 393 N N . PHE A 1 50 ? 8.620 13.763 53.654 1.00 9.73 ? 131 PHE A N 1 ATOM 394 C CA . PHE A 1 50 ? 9.359 14.266 54.820 1.00 6.20 ? 131 PHE A CA 1 ATOM 395 C C . PHE A 1 50 ? 10.467 13.230 55.047 1.00 5.17 ? 131 PHE A C 1 ATOM 396 O O . PHE A 1 50 ? 10.266 12.041 54.725 1.00 3.70 ? 131 PHE A O 1 ATOM 397 C CB . PHE A 1 50 ? 8.493 14.317 56.101 1.00 7.10 ? 131 PHE A CB 1 ATOM 398 C CG . PHE A 1 50 ? 7.644 15.555 56.357 1.00 7.02 ? 131 PHE A CG 1 ATOM 399 C CD1 . PHE A 1 50 ? 7.741 16.670 55.576 1.00 7.82 ? 131 PHE A CD1 1 ATOM 400 C CD2 . PHE A 1 50 ? 6.724 15.575 57.383 1.00 8.11 ? 131 PHE A CD2 1 ATOM 401 C CE1 . PHE A 1 50 ? 6.936 17.779 55.791 1.00 7.82 ? 131 PHE A CE1 1 ATOM 402 C CE2 . PHE A 1 50 ? 5.921 16.693 57.582 1.00 6.75 ? 131 PHE A CE2 1 ATOM 403 C CZ . PHE A 1 50 ? 6.022 17.804 56.796 1.00 6.67 ? 131 PHE A CZ 1 ATOM 404 N N . TYR A 1 51 ? 11.635 13.654 55.569 1.00 6.34 ? 132 TYR A N 1 ATOM 405 C CA . TYR A 1 51 ? 12.827 12.834 55.717 1.00 5.81 ? 132 TYR A CA 1 ATOM 406 C C . TYR A 1 51 ? 13.477 13.117 57.075 1.00 6.96 ? 132 TYR A C 1 ATOM 407 O O . TYR A 1 51 ? 13.280 14.202 57.631 1.00 7.55 ? 132 TYR A O 1 ATOM 408 C CB . TYR A 1 51 ? 13.821 13.161 54.611 1.00 6.11 ? 132 TYR A CB 1 ATOM 409 C CG . TYR A 1 51 ? 13.517 12.679 53.190 1.00 7.00 ? 132 TYR A CG 1 ATOM 410 C CD1 . TYR A 1 51 ? 12.491 13.233 52.467 1.00 7.62 ? 132 TYR A CD1 1 ATOM 411 C CD2 . TYR A 1 51 ? 14.235 11.617 52.660 1.00 8.66 ? 132 TYR A CD2 1 ATOM 412 C CE1 . TYR A 1 51 ? 12.185 12.729 51.237 1.00 5.35 ? 132 TYR A CE1 1 ATOM 413 C CE2 . TYR A 1 51 ? 13.935 11.102 51.427 1.00 6.58 ? 132 TYR A CE2 1 ATOM 414 C CZ . TYR A 1 51 ? 12.905 11.679 50.725 1.00 6.66 ? 132 TYR A CZ 1 ATOM 415 O OH . TYR A 1 51 ? 12.462 11.135 49.505 1.00 11.11 ? 132 TYR A OH 1 ATOM 416 N N . ALA A 1 52 ? 14.231 12.188 57.670 1.00 6.80 ? 133 ALA A N 1 ATOM 417 C CA . ALA A 1 52 ? 14.989 12.404 58.879 1.00 5.20 ? 133 ALA A CA 1 ATOM 418 C C . ALA A 1 52 ? 15.902 11.235 59.150 1.00 5.89 ? 133 ALA A C 1 ATOM 419 O O . ALA A 1 52 ? 15.856 10.196 58.500 1.00 8.06 ? 133 ALA A O 1 ATOM 420 C CB . ALA A 1 52 ? 14.118 12.557 60.124 1.00 4.76 ? 133 ALA A CB 1 ATOM 421 N N . LEU A 1 53 ? 16.852 11.472 60.027 1.00 6.01 ? 134 LEU A N 1 ATOM 422 C CA . LEU A 1 53 ? 17.729 10.460 60.564 1.00 3.99 ? 134 LEU A CA 1 ATOM 423 C C . LEU A 1 53 ? 17.098 9.910 61.834 1.00 4.09 ? 134 LEU A C 1 ATOM 424 O O . LEU A 1 53 ? 16.909 10.593 62.820 1.00 4.61 ? 134 LEU A O 1 ATOM 425 C CB . LEU A 1 53 ? 19.056 11.144 60.799 1.00 4.72 ? 134 LEU A CB 1 ATOM 426 C CG . LEU A 1 53 ? 20.336 10.880 60.034 1.00 3.57 ? 134 LEU A CG 1 ATOM 427 C CD1 . LEU A 1 53 ? 20.107 10.460 58.598 1.00 4.69 ? 134 LEU A CD1 1 ATOM 428 C CD2 . LEU A 1 53 ? 21.110 12.155 60.091 1.00 2.17 ? 134 LEU A CD2 1 ATOM 429 N N . SER A 1 54 ? 16.750 8.641 61.807 1.00 5.73 ? 135 SER A N 1 ATOM 430 C CA . SER A 1 54 ? 16.101 7.961 62.891 1.00 5.70 ? 135 SER A CA 1 ATOM 431 C C . SER A 1 54 ? 17.090 7.756 64.028 1.00 8.69 ? 135 SER A C 1 ATOM 432 O O . SER A 1 54 ? 18.297 7.904 63.818 1.00 8.54 ? 135 SER A O 1 ATOM 433 C CB . SER A 1 54 ? 15.596 6.637 62.392 1.00 6.37 ? 135 SER A CB 1 ATOM 434 O OG . SER A 1 54 ? 15.137 5.818 63.440 1.00 8.90 ? 135 SER A OG 1 ATOM 435 N N . GLN A 1 55 ? 16.621 7.493 65.255 1.00 9.89 ? 136 GLN A N 1 ATOM 436 C CA . GLN A 1 55 ? 17.538 7.087 66.293 1.00 8.77 ? 136 GLN A CA 1 ATOM 437 C C . GLN A 1 55 ? 17.333 5.612 66.644 1.00 9.74 ? 136 GLN A C 1 ATOM 438 O O . GLN A 1 55 ? 18.000 5.084 67.528 1.00 9.15 ? 136 GLN A O 1 ATOM 439 C CB . GLN A 1 55 ? 17.312 7.993 67.490 1.00 7.69 ? 136 GLN A CB 1 ATOM 440 C CG . GLN A 1 55 ? 17.973 9.367 67.380 1.00 7.23 ? 136 GLN A CG 1 ATOM 441 C CD . GLN A 1 55 ? 19.467 9.418 67.718 1.00 7.92 ? 136 GLN A CD 1 ATOM 442 O OE1 . GLN A 1 55 ? 20.229 8.443 67.647 1.00 7.80 ? 136 GLN A OE1 1 ATOM 443 N NE2 . GLN A 1 55 ? 19.881 10.628 68.076 1.00 9.41 ? 136 GLN A NE2 1 ATOM 444 N N . GLY A 1 56 ? 16.413 4.875 66.013 1.00 10.54 ? 137 GLY A N 1 ATOM 445 C CA . GLY A 1 56 ? 16.221 3.439 66.258 1.00 8.87 ? 137 GLY A CA 1 ATOM 446 C C . GLY A 1 56 ? 15.496 3.130 67.565 1.00 11.52 ? 137 GLY A C 1 ATOM 447 O O . GLY A 1 56 ? 15.765 2.063 68.136 1.00 10.42 ? 137 GLY A O 1 ATOM 448 N N . THR A 1 57 ? 14.614 4.022 68.075 1.00 13.03 ? 138 THR A N 1 ATOM 449 C CA . THR A 1 57 ? 13.746 3.829 69.254 1.00 13.21 ? 138 THR A CA 1 ATOM 450 C C . THR A 1 57 ? 12.466 4.614 69.002 1.00 11.23 ? 138 THR A C 1 ATOM 451 O O . THR A 1 57 ? 12.472 5.482 68.111 1.00 8.30 ? 138 THR A O 1 ATOM 452 C CB . THR A 1 57 ? 14.100 4.477 70.597 1.00 14.66 ? 138 THR A CB 1 ATOM 453 O OG1 . THR A 1 57 ? 15.426 5.007 70.639 1.00 19.34 ? 138 THR A OG1 1 ATOM 454 C CG2 . THR A 1 57 ? 13.756 3.429 71.616 1.00 14.49 ? 138 THR A CG2 1 ATOM 455 N N . THR A 1 58 ? 11.405 4.361 69.773 1.00 9.21 ? 139 THR A N 1 ATOM 456 C CA . THR A 1 58 ? 10.260 5.242 69.788 1.00 10.29 ? 139 THR A CA 1 ATOM 457 C C . THR A 1 58 ? 10.422 6.260 70.938 1.00 10.01 ? 139 THR A C 1 ATOM 458 O O . THR A 1 58 ? 11.282 6.070 71.812 1.00 10.45 ? 139 THR A O 1 ATOM 459 C CB . THR A 1 58 ? 8.982 4.373 69.921 1.00 10.96 ? 139 THR A CB 1 ATOM 460 O OG1 . THR A 1 58 ? 9.198 3.441 70.983 1.00 13.13 ? 139 THR A OG1 1 ATOM 461 C CG2 . THR A 1 58 ? 8.640 3.644 68.614 1.00 9.70 ? 139 THR A CG2 1 ATOM 462 N N . ILE A 1 59 ? 9.663 7.374 70.956 1.00 9.98 ? 140 ILE A N 1 ATOM 463 C CA . ILE A 1 59 ? 9.783 8.362 72.027 1.00 8.70 ? 140 ILE A CA 1 ATOM 464 C C . ILE A 1 59 ? 9.480 7.777 73.397 1.00 7.68 ? 140 ILE A C 1 ATOM 465 O O . ILE A 1 59 ? 10.249 7.887 74.343 1.00 7.23 ? 140 ILE A O 1 ATOM 466 C CB . ILE A 1 59 ? 8.867 9.565 71.719 1.00 10.91 ? 140 ILE A CB 1 ATOM 467 C CG1 . ILE A 1 59 ? 9.162 10.192 70.337 1.00 12.12 ? 140 ILE A CG1 1 ATOM 468 C CG2 . ILE A 1 59 ? 9.142 10.620 72.774 1.00 10.42 ? 140 ILE A CG2 1 ATOM 469 C CD1 . ILE A 1 59 ? 8.337 11.402 69.907 1.00 12.47 ? 140 ILE A CD1 1 ATOM 470 N N . ARG A 1 60 ? 8.389 7.067 73.505 1.00 9.97 ? 141 ARG A N 1 ATOM 471 C CA . ARG A 1 60 ? 7.989 6.478 74.743 1.00 9.73 ? 141 ARG A CA 1 ATOM 472 C C . ARG A 1 60 ? 8.766 5.217 75.060 1.00 8.37 ? 141 ARG A C 1 ATOM 473 O O . ARG A 1 60 ? 8.734 4.772 76.217 1.00 7.70 ? 141 ARG A O 1 ATOM 474 C CB . ARG A 1 60 ? 6.513 6.270 74.605 1.00 14.44 ? 141 ARG A CB 1 ATOM 475 C CG . ARG A 1 60 ? 5.600 6.650 75.768 1.00 18.72 ? 141 ARG A CG 1 ATOM 476 C CD . ARG A 1 60 ? 5.419 8.147 75.892 1.00 21.90 ? 141 ARG A CD 1 ATOM 477 N NE . ARG A 1 60 ? 5.517 8.519 77.289 1.00 25.42 ? 141 ARG A NE 1 ATOM 478 C CZ . ARG A 1 60 ? 4.500 9.035 77.978 1.00 27.25 ? 141 ARG A CZ 1 ATOM 479 N NH1 . ARG A 1 60 ? 3.330 9.304 77.453 1.00 29.38 ? 141 ARG A NH1 1 ATOM 480 N NH2 . ARG A 1 60 ? 4.643 9.344 79.256 1.00 29.62 ? 141 ARG A NH2 1 ATOM 481 N N . GLY A 1 61 ? 9.545 4.646 74.156 1.00 7.71 ? 142 GLY A N 1 ATOM 482 C CA . GLY A 1 61 ? 10.328 3.487 74.509 1.00 10.49 ? 142 GLY A CA 1 ATOM 483 C C . GLY A 1 61 ? 11.541 3.854 75.375 1.00 11.62 ? 142 GLY A C 1 ATOM 484 O O . GLY A 1 61 ? 12.125 4.938 75.323 1.00 11.29 ? 142 GLY A O 1 ATOM 485 N N . LYS A 1 62 ? 12.013 2.895 76.143 1.00 12.74 ? 143 LYS A N 1 ATOM 486 C CA . LYS A 1 62 ? 13.117 3.036 77.070 1.00 15.38 ? 143 LYS A CA 1 ATOM 487 C C . LYS A 1 62 ? 14.445 3.307 76.404 1.00 16.71 ? 143 LYS A C 1 ATOM 488 O O . LYS A 1 62 ? 15.294 3.924 77.065 1.00 17.71 ? 143 LYS A O 1 ATOM 489 C CB . LYS A 1 62 ? 13.382 1.820 77.878 1.00 15.62 ? 143 LYS A CB 1 ATOM 490 C CG . LYS A 1 62 ? 12.173 1.384 78.654 1.00 16.58 ? 143 LYS A CG 1 ATOM 491 C CD . LYS A 1 62 ? 12.437 1.525 80.086 1.00 18.26 ? 143 LYS A CD 1 ATOM 492 C CE . LYS A 1 62 ? 11.398 0.659 80.702 1.00 22.09 ? 143 LYS A CE 1 ATOM 493 N NZ . LYS A 1 62 ? 11.686 -0.767 80.580 1.00 25.09 ? 143 LYS A NZ 1 ATOM 494 N N . HIS A 1 63 ? 14.709 2.897 75.137 1.00 16.41 ? 144 HIS A N 1 ATOM 495 C CA . HIS A 1 63 ? 16.047 3.143 74.636 1.00 11.35 ? 144 HIS A CA 1 ATOM 496 C C . HIS A 1 63 ? 16.061 4.578 74.111 1.00 11.56 ? 144 HIS A C 1 ATOM 497 O O . HIS A 1 63 ? 17.014 4.934 73.433 1.00 14.66 ? 144 HIS A O 1 ATOM 498 C CB . HIS A 1 63 ? 16.386 2.182 73.535 1.00 6.51 ? 144 HIS A CB 1 ATOM 499 C CG . HIS A 1 63 ? 16.194 0.696 73.856 1.00 3.08 ? 144 HIS A CG 1 ATOM 500 N ND1 . HIS A 1 63 ? 17.145 -0.157 74.271 1.00 3.84 ? 144 HIS A ND1 1 ATOM 501 C CD2 . HIS A 1 63 ? 15.042 -0.027 73.667 1.00 2.49 ? 144 HIS A CD2 1 ATOM 502 C CE1 . HIS A 1 63 ? 16.629 -1.383 74.315 1.00 2.33 ? 144 HIS A CE1 1 ATOM 503 N NE2 . HIS A 1 63 ? 15.348 -1.289 73.975 1.00 3.35 ? 144 HIS A NE2 1 ATOM 504 N N . SER A 1 64 ? 15.037 5.433 74.337 1.00 9.27 ? 145 SER A N 1 ATOM 505 C CA . SER A 1 64 ? 15.098 6.858 73.990 1.00 9.23 ? 145 SER A CA 1 ATOM 506 C C . SER A 1 64 ? 15.991 7.624 74.956 1.00 9.90 ? 145 SER A C 1 ATOM 507 O O . SER A 1 64 ? 16.348 8.781 74.706 1.00 9.62 ? 145 SER A O 1 ATOM 508 C CB . SER A 1 64 ? 13.692 7.559 74.009 1.00 9.40 ? 145 SER A CB 1 ATOM 509 O OG . SER A 1 64 ? 13.027 7.612 75.267 1.00 7.23 ? 145 SER A OG 1 ATOM 510 N N . ASN A 1 65 ? 16.354 7.011 76.093 1.00 15.64 ? 146 ASN A N 1 ATOM 511 C CA . ASN A 1 65 ? 17.204 7.670 77.060 1.00 17.22 ? 146 ASN A CA 1 ATOM 512 C C . ASN A 1 65 ? 18.572 7.629 76.449 1.00 15.86 ? 146 ASN A C 1 ATOM 513 O O . ASN A 1 65 ? 19.129 6.548 76.273 1.00 17.70 ? 146 ASN A O 1 ATOM 514 C CB . ASN A 1 65 ? 17.232 6.926 78.377 1.00 21.53 ? 146 ASN A CB 1 ATOM 515 C CG . ASN A 1 65 ? 18.262 7.425 79.403 1.00 25.36 ? 146 ASN A CG 1 ATOM 516 O OD1 . ASN A 1 65 ? 18.992 8.405 79.200 1.00 26.77 ? 146 ASN A OD1 1 ATOM 517 N ND2 . ASN A 1 65 ? 18.359 6.770 80.563 1.00 30.66 ? 146 ASN A ND2 1 ATOM 518 N N . GLY A 1 66 ? 19.102 8.778 76.091 1.00 14.11 ? 147 GLY A N 1 ATOM 519 C CA . GLY A 1 66 ? 20.413 8.809 75.465 1.00 13.28 ? 147 GLY A CA 1 ATOM 520 C C . GLY A 1 66 ? 20.473 9.347 74.042 1.00 13.41 ? 147 GLY A C 1 ATOM 521 O O . GLY A 1 66 ? 21.569 9.635 73.528 1.00 11.57 ? 147 GLY A O 1 ATOM 522 N N . THR A 1 67 ? 19.338 9.567 73.371 1.00 11.50 ? 148 THR A N 1 ATOM 523 C CA . THR A 1 67 ? 19.318 9.985 71.980 1.00 10.71 ? 148 THR A CA 1 ATOM 524 C C . THR A 1 67 ? 19.743 11.430 71.675 1.00 14.34 ? 148 THR A C 1 ATOM 525 O O . THR A 1 67 ? 19.530 11.934 70.544 1.00 14.08 ? 148 THR A O 1 ATOM 526 C CB . THR A 1 67 ? 17.897 9.644 71.437 1.00 10.91 ? 148 THR A CB 1 ATOM 527 O OG1 . THR A 1 67 ? 16.960 10.201 72.362 1.00 11.28 ? 148 THR A OG1 1 ATOM 528 C CG2 . THR A 1 67 ? 17.666 8.126 71.257 1.00 9.83 ? 148 THR A CG2 1 ATOM 529 N N . ILE A 1 68 ? 20.348 12.141 72.664 1.00 15.25 ? 149 ILE A N 1 ATOM 530 C CA . ILE A 1 68 ? 20.978 13.448 72.422 1.00 15.76 ? 149 ILE A CA 1 ATOM 531 C C . ILE A 1 68 ? 22.267 13.297 71.594 1.00 18.37 ? 149 ILE A C 1 ATOM 532 O O . ILE A 1 68 ? 22.699 14.230 70.913 1.00 19.11 ? 149 ILE A O 1 ATOM 533 C CB . ILE A 1 68 ? 21.325 14.171 73.770 1.00 15.68 ? 149 ILE A CB 1 ATOM 534 C CG1 . ILE A 1 68 ? 21.532 15.672 73.409 1.00 15.79 ? 149 ILE A CG1 1 ATOM 535 C CG2 . ILE A 1 68 ? 22.552 13.555 74.481 1.00 13.60 ? 149 ILE A CG2 1 ATOM 536 C CD1 . ILE A 1 68 ? 22.061 16.657 74.478 1.00 14.71 ? 149 ILE A CD1 1 ATOM 537 N N . HIS A 1 69 ? 22.895 12.116 71.689 1.00 20.65 ? 150 HIS A N 1 ATOM 538 C CA . HIS A 1 69 ? 24.131 11.793 71.000 1.00 22.40 ? 150 HIS A CA 1 ATOM 539 C C . HIS A 1 69 ? 23.887 11.744 69.512 1.00 21.19 ? 150 HIS A C 1 ATOM 540 O O . HIS A 1 69 ? 22.857 11.244 69.083 1.00 21.35 ? 150 HIS A O 1 ATOM 541 C CB . HIS A 1 69 ? 24.644 10.453 71.465 1.00 25.15 ? 150 HIS A CB 1 ATOM 542 C CG . HIS A 1 69 ? 24.947 10.565 72.940 1.00 28.24 ? 150 HIS A CG 1 ATOM 543 N ND1 . HIS A 1 69 ? 25.537 11.594 73.561 1.00 29.84 ? 150 HIS A ND1 1 ATOM 544 C CD2 . HIS A 1 69 ? 24.581 9.641 73.886 1.00 29.98 ? 150 HIS A CD2 1 ATOM 545 C CE1 . HIS A 1 69 ? 25.548 11.344 74.850 1.00 29.67 ? 150 HIS A CE1 1 ATOM 546 N NE2 . HIS A 1 69 ? 24.969 10.171 75.029 1.00 32.08 ? 150 HIS A NE2 1 ATOM 547 N N . ASP A 1 70 ? 24.856 12.240 68.757 1.00 21.12 ? 151 ASP A N 1 ATOM 548 C CA . ASP A 1 70 ? 24.650 12.361 67.333 1.00 22.65 ? 151 ASP A CA 1 ATOM 549 C C . ASP A 1 70 ? 24.991 11.256 66.388 1.00 19.62 ? 151 ASP A C 1 ATOM 550 O O . ASP A 1 70 ? 24.347 11.154 65.352 1.00 18.41 ? 151 ASP A O 1 ATOM 551 C CB . ASP A 1 70 ? 25.361 13.587 66.832 1.00 27.16 ? 151 ASP A CB 1 ATOM 552 C CG . ASP A 1 70 ? 24.448 14.808 66.900 1.00 31.20 ? 151 ASP A CG 1 ATOM 553 O OD1 . ASP A 1 70 ? 23.232 14.720 66.554 1.00 34.06 ? 151 ASP A OD1 1 ATOM 554 O OD2 . ASP A 1 70 ? 24.985 15.852 67.297 1.00 34.16 ? 151 ASP A OD2 1 ATOM 555 N N . ARG A 1 71 ? 25.942 10.404 66.739 1.00 16.44 ? 152 ARG A N 1 ATOM 556 C CA . ARG A 1 71 ? 26.401 9.376 65.839 1.00 14.53 ? 152 ARG A CA 1 ATOM 557 C C . ARG A 1 71 ? 26.296 8.037 66.522 1.00 12.25 ? 152 ARG A C 1 ATOM 558 O O . ARG A 1 71 ? 26.754 7.954 67.656 1.00 13.46 ? 152 ARG A O 1 ATOM 559 C CB . ARG A 1 71 ? 27.854 9.612 65.477 1.00 14.47 ? 152 ARG A CB 1 ATOM 560 C CG . ARG A 1 71 ? 28.113 10.791 64.584 1.00 16.33 ? 152 ARG A CG 1 ATOM 561 C CD . ARG A 1 71 ? 29.609 11.018 64.451 1.00 19.43 ? 152 ARG A CD 1 ATOM 562 N NE . ARG A 1 71 ? 29.777 12.423 64.751 1.00 23.96 ? 152 ARG A NE 1 ATOM 563 C CZ . ARG A 1 71 ? 30.172 12.840 65.954 1.00 25.80 ? 152 ARG A CZ 1 ATOM 564 N NH1 . ARG A 1 71 ? 30.773 12.042 66.842 1.00 27.43 ? 152 ARG A NH1 1 ATOM 565 N NH2 . ARG A 1 71 ? 30.125 14.129 66.240 1.00 26.04 ? 152 ARG A NH2 1 ATOM 566 N N . SER A 1 72 ? 25.834 6.961 65.902 1.00 11.56 ? 153 SER A N 1 ATOM 567 C CA . SER A 1 72 ? 25.661 5.639 66.547 1.00 10.92 ? 153 SER A CA 1 ATOM 568 C C . SER A 1 72 ? 25.328 4.615 65.487 1.00 11.39 ? 153 SER A C 1 ATOM 569 O O . SER A 1 72 ? 25.005 4.981 64.351 1.00 10.89 ? 153 SER A O 1 ATOM 570 C CB . SER A 1 72 ? 24.507 5.622 67.558 1.00 10.70 ? 153 SER A CB 1 ATOM 571 O OG . SER A 1 72 ? 23.248 5.077 67.147 1.00 8.48 ? 153 SER A OG 1 ATOM 572 N N . GLN A 1 73 ? 25.305 3.311 65.762 1.00 12.08 ? 154 GLN A N 1 ATOM 573 C CA . GLN A 1 73 ? 24.962 2.390 64.689 1.00 10.96 ? 154 GLN A CA 1 ATOM 574 C C . GLN A 1 73 ? 23.473 2.173 64.503 1.00 11.26 ? 154 GLN A C 1 ATOM 575 O O . GLN A 1 73 ? 23.060 1.467 63.571 1.00 14.89 ? 154 GLN A O 1 ATOM 576 C CB . GLN A 1 73 ? 25.569 1.040 64.918 1.00 12.25 ? 154 GLN A CB 1 ATOM 577 C CG . GLN A 1 73 ? 27.059 1.004 65.007 1.00 12.06 ? 154 GLN A CG 1 ATOM 578 C CD . GLN A 1 73 ? 27.609 1.195 66.413 1.00 13.53 ? 154 GLN A CD 1 ATOM 579 O OE1 . GLN A 1 73 ? 27.040 1.918 67.227 1.00 14.69 ? 154 GLN A OE1 1 ATOM 580 N NE2 . GLN A 1 73 ? 28.780 0.627 66.685 1.00 11.94 ? 154 GLN A NE2 1 ATOM 581 N N . TYR A 1 74 ? 22.640 2.741 65.369 1.00 10.28 ? 155 TYR A N 1 ATOM 582 C CA . TYR A 1 74 ? 21.202 2.514 65.359 1.00 7.30 ? 155 TYR A CA 1 ATOM 583 C C . TYR A 1 74 ? 20.473 3.589 64.580 1.00 9.99 ? 155 TYR A C 1 ATOM 584 O O . TYR A 1 74 ? 19.260 3.500 64.476 1.00 9.36 ? 155 TYR A O 1 ATOM 585 C CB . TYR A 1 74 ? 20.716 2.483 66.788 1.00 7.11 ? 155 TYR A CB 1 ATOM 586 C CG . TYR A 1 74 ? 21.725 1.678 67.648 1.00 4.68 ? 155 TYR A CG 1 ATOM 587 C CD1 . TYR A 1 74 ? 22.039 0.399 67.276 1.00 4.10 ? 155 TYR A CD1 1 ATOM 588 C CD2 . TYR A 1 74 ? 22.437 2.278 68.665 1.00 3.15 ? 155 TYR A CD2 1 ATOM 589 C CE1 . TYR A 1 74 ? 23.014 -0.323 67.933 1.00 3.19 ? 155 TYR A CE1 1 ATOM 590 C CE2 . TYR A 1 74 ? 23.411 1.555 69.352 1.00 2.11 ? 155 TYR A CE2 1 ATOM 591 C CZ . TYR A 1 74 ? 23.692 0.229 68.971 1.00 3.00 ? 155 TYR A CZ 1 ATOM 592 O OH . TYR A 1 74 ? 24.654 -0.537 69.593 1.00 5.53 ? 155 TYR A OH 1 ATOM 593 N N . ARG A 1 75 ? 21.092 4.658 64.033 1.00 10.18 ? 156 ARG A N 1 ATOM 594 C CA . ARG A 1 75 ? 20.445 5.649 63.160 1.00 8.38 ? 156 ARG A CA 1 ATOM 595 C C . ARG A 1 75 ? 20.310 5.306 61.667 1.00 6.89 ? 156 ARG A C 1 ATOM 596 O O . ARG A 1 75 ? 21.197 4.663 61.105 1.00 8.00 ? 156 ARG A O 1 ATOM 597 C CB . ARG A 1 75 ? 21.219 7.030 63.253 1.00 9.75 ? 156 ARG A CB 1 ATOM 598 C CG . ARG A 1 75 ? 21.452 7.622 64.622 1.00 10.60 ? 156 ARG A CG 1 ATOM 599 C CD . ARG A 1 75 ? 21.636 9.119 64.580 1.00 10.75 ? 156 ARG A CD 1 ATOM 600 N NE . ARG A 1 75 ? 20.380 9.827 64.415 1.00 12.56 ? 156 ARG A NE 1 ATOM 601 C CZ . ARG A 1 75 ? 20.222 11.153 64.552 1.00 13.18 ? 156 ARG A CZ 1 ATOM 602 N NH1 . ARG A 1 75 ? 21.212 11.983 64.813 1.00 14.75 ? 156 ARG A NH1 1 ATOM 603 N NH2 . ARG A 1 75 ? 19.003 11.713 64.453 1.00 14.46 ? 156 ARG A NH2 1 ATOM 604 N N . ALA A 1 76 ? 19.313 5.798 60.913 1.00 6.48 ? 157 ALA A N 1 ATOM 605 C CA . ALA A 1 76 ? 19.185 5.496 59.478 1.00 5.88 ? 157 ALA A CA 1 ATOM 606 C C . ALA A 1 76 ? 18.460 6.629 58.757 1.00 6.76 ? 157 ALA A C 1 ATOM 607 O O . ALA A 1 76 ? 17.749 7.367 59.464 1.00 7.94 ? 157 ALA A O 1 ATOM 608 C CB . ALA A 1 76 ? 18.366 4.266 59.238 1.00 4.05 ? 157 ALA A CB 1 ATOM 609 N N . LEU A 1 77 ? 18.553 6.792 57.421 1.00 4.73 ? 158 LEU A N 1 ATOM 610 C CA . LEU A 1 77 ? 17.747 7.817 56.768 1.00 4.04 ? 158 LEU A CA 1 ATOM 611 C C . LEU A 1 77 ? 16.450 7.105 56.435 1.00 5.71 ? 158 LEU A C 1 ATOM 612 O O . LEU A 1 77 ? 16.427 5.995 55.866 1.00 4.43 ? 158 LEU A O 1 ATOM 613 C CB . LEU A 1 77 ? 18.418 8.358 55.460 1.00 3.76 ? 158 LEU A CB 1 ATOM 614 C CG . LEU A 1 77 ? 17.689 9.410 54.614 1.00 3.81 ? 158 LEU A CG 1 ATOM 615 C CD1 . LEU A 1 77 ? 17.441 10.645 55.473 1.00 4.39 ? 158 LEU A CD1 1 ATOM 616 C CD2 . LEU A 1 77 ? 18.486 9.726 53.329 1.00 2.00 ? 158 LEU A CD2 1 ATOM 617 N N . ILE A 1 78 ? 15.373 7.695 56.930 1.00 5.63 ? 159 ILE A N 1 ATOM 618 C CA . ILE A 1 78 ? 14.006 7.218 56.632 1.00 5.74 ? 159 ILE A CA 1 ATOM 619 C C . ILE A 1 78 ? 13.155 8.320 55.958 1.00 5.46 ? 159 ILE A C 1 ATOM 620 O O . ILE A 1 78 ? 13.512 9.513 56.042 1.00 4.76 ? 159 ILE A O 1 ATOM 621 C CB . ILE A 1 78 ? 13.197 6.745 57.888 1.00 3.93 ? 159 ILE A CB 1 ATOM 622 C CG1 . ILE A 1 78 ? 13.339 7.643 59.092 1.00 6.65 ? 159 ILE A CG1 1 ATOM 623 C CG2 . ILE A 1 78 ? 13.683 5.375 58.261 1.00 3.74 ? 159 ILE A CG2 1 ATOM 624 C CD1 . ILE A 1 78 ? 12.085 7.643 60.027 1.00 7.03 ? 159 ILE A CD1 1 ATOM 625 N N . SER A 1 79 ? 12.057 7.980 55.278 1.00 4.58 ? 160 SER A N 1 ATOM 626 C CA . SER A 1 79 ? 11.131 8.958 54.715 1.00 4.75 ? 160 SER A CA 1 ATOM 627 C C . SER A 1 79 ? 9.720 8.512 55.048 1.00 5.87 ? 160 SER A C 1 ATOM 628 O O . SER A 1 79 ? 9.532 7.303 55.289 1.00 3.55 ? 160 SER A O 1 ATOM 629 C CB . SER A 1 79 ? 11.234 9.035 53.212 1.00 6.52 ? 160 SER A CB 1 ATOM 630 O OG . SER A 1 79 ? 10.905 7.840 52.502 1.00 6.50 ? 160 SER A OG 1 ATOM 631 N N . TRP A 1 80 ? 8.687 9.357 55.033 1.00 5.93 ? 161 TRP A N 1 ATOM 632 C CA . TRP A 1 80 ? 7.328 8.911 55.307 1.00 5.06 ? 161 TRP A CA 1 ATOM 633 C C . TRP A 1 80 ? 6.427 9.909 54.508 1.00 6.98 ? 161 TRP A C 1 ATOM 634 O O . TRP A 1 80 ? 6.900 10.933 53.957 1.00 7.84 ? 161 TRP A O 1 ATOM 635 C CB . TRP A 1 80 ? 7.139 8.890 56.904 1.00 5.46 ? 161 TRP A CB 1 ATOM 636 C CG . TRP A 1 80 ? 7.422 10.222 57.634 1.00 3.20 ? 161 TRP A CG 1 ATOM 637 C CD1 . TRP A 1 80 ? 6.367 11.066 57.896 1.00 4.20 ? 161 TRP A CD1 1 ATOM 638 C CD2 . TRP A 1 80 ? 8.634 10.748 58.120 1.00 4.95 ? 161 TRP A CD2 1 ATOM 639 N NE1 . TRP A 1 80 ? 6.872 12.106 58.539 1.00 5.20 ? 161 TRP A NE1 1 ATOM 640 C CE2 . TRP A 1 80 ? 8.215 11.961 58.685 1.00 7.09 ? 161 TRP A CE2 1 ATOM 641 C CE3 . TRP A 1 80 ? 9.970 10.416 58.180 1.00 3.95 ? 161 TRP A CE3 1 ATOM 642 C CZ2 . TRP A 1 80 ? 9.123 12.799 59.317 1.00 7.72 ? 161 TRP A CZ2 1 ATOM 643 C CZ3 . TRP A 1 80 ? 10.875 11.267 58.788 1.00 6.41 ? 161 TRP A CZ3 1 ATOM 644 C CH2 . TRP A 1 80 ? 10.458 12.446 59.366 1.00 6.83 ? 161 TRP A CH2 1 ATOM 645 N N . PRO A 1 81 ? 5.130 9.634 54.296 1.00 7.73 ? 162 PRO A N 1 ATOM 646 C CA . PRO A 1 81 ? 4.195 10.569 53.669 1.00 9.38 ? 162 PRO A CA 1 ATOM 647 C C . PRO A 1 81 ? 4.087 11.999 54.256 1.00 10.75 ? 162 PRO A C 1 ATOM 648 O O . PRO A 1 81 ? 4.208 12.213 55.467 1.00 10.74 ? 162 PRO A O 1 ATOM 649 C CB . PRO A 1 81 ? 2.894 9.835 53.697 1.00 7.98 ? 162 PRO A CB 1 ATOM 650 C CG . PRO A 1 81 ? 3.295 8.400 53.811 1.00 8.11 ? 162 PRO A CG 1 ATOM 651 C CD . PRO A 1 81 ? 4.413 8.476 54.782 1.00 8.08 ? 162 PRO A CD 1 ATOM 652 N N . LEU A 1 82 ? 3.871 13.003 53.379 1.00 11.26 ? 163 LEU A N 1 ATOM 653 C CA . LEU A 1 82 ? 3.809 14.418 53.758 1.00 13.14 ? 163 LEU A CA 1 ATOM 654 C C . LEU A 1 82 ? 2.743 14.653 54.835 1.00 13.66 ? 163 LEU A C 1 ATOM 655 O O . LEU A 1 82 ? 1.646 14.106 54.827 1.00 15.35 ? 163 LEU A O 1 ATOM 656 C CB . LEU A 1 82 ? 3.496 15.323 52.536 1.00 12.05 ? 163 LEU A CB 1 ATOM 657 C CG . LEU A 1 82 ? 3.583 16.845 52.708 1.00 12.65 ? 163 LEU A CG 1 ATOM 658 C CD1 . LEU A 1 82 ? 5.026 17.247 52.806 1.00 11.04 ? 163 LEU A CD1 1 ATOM 659 C CD2 . LEU A 1 82 ? 3.003 17.541 51.525 1.00 11.34 ? 163 LEU A CD2 1 ATOM 660 N N . SER A 1 83 ? 3.167 15.331 55.879 1.00 13.12 ? 164 SER A N 1 ATOM 661 C CA . SER A 1 83 ? 2.393 15.698 57.032 1.00 11.99 ? 164 SER A CA 1 ATOM 662 C C . SER A 1 83 ? 1.835 14.603 57.965 1.00 11.98 ? 164 SER A C 1 ATOM 663 O O . SER A 1 83 ? 0.948 14.873 58.785 1.00 11.45 ? 164 SER A O 1 ATOM 664 C CB . SER A 1 83 ? 1.259 16.666 56.546 1.00 11.88 ? 164 SER A CB 1 ATOM 665 O OG . SER A 1 83 ? 1.685 18.019 56.419 1.00 10.16 ? 164 SER A OG 1 ATOM 666 N N . SER A 1 84 ? 2.446 13.410 57.891 1.00 12.50 ? 165 SER A N 1 ATOM 667 C CA . SER A 1 84 ? 2.227 12.280 58.779 1.00 12.74 ? 165 SER A CA 1 ATOM 668 C C . SER A 1 84 ? 3.428 12.257 59.741 1.00 13.00 ? 165 SER A C 1 ATOM 669 O O . SER A 1 84 ? 4.435 12.905 59.441 1.00 12.87 ? 165 SER A O 1 ATOM 670 C CB . SER A 1 84 ? 2.224 10.965 58.026 1.00 13.50 ? 165 SER A CB 1 ATOM 671 O OG . SER A 1 84 ? 1.022 10.711 57.327 1.00 17.23 ? 165 SER A OG 1 ATOM 672 N N . PRO A 1 85 ? 3.446 11.576 60.902 1.00 13.25 ? 166 PRO A N 1 ATOM 673 C CA . PRO A 1 85 ? 4.595 11.474 61.779 1.00 13.75 ? 166 PRO A CA 1 ATOM 674 C C . PRO A 1 85 ? 5.462 10.270 61.403 1.00 13.20 ? 166 PRO A C 1 ATOM 675 O O . PRO A 1 85 ? 4.974 9.314 60.763 1.00 14.15 ? 166 PRO A O 1 ATOM 676 C CB . PRO A 1 85 ? 3.948 11.427 63.171 1.00 12.82 ? 166 PRO A CB 1 ATOM 677 C CG . PRO A 1 85 ? 2.604 10.782 63.006 1.00 10.49 ? 166 PRO A CG 1 ATOM 678 C CD . PRO A 1 85 ? 2.302 10.888 61.509 1.00 13.01 ? 166 PRO A CD 1 ATOM 679 N N . PRO A 1 86 ? 6.761 10.270 61.726 1.00 12.20 ? 167 PRO A N 1 ATOM 680 C CA . PRO A 1 86 ? 7.666 9.155 61.451 1.00 12.97 ? 167 PRO A CA 1 ATOM 681 C C . PRO A 1 86 ? 7.280 8.003 62.378 1.00 13.54 ? 167 PRO A C 1 ATOM 682 O O . PRO A 1 86 ? 7.795 7.871 63.497 1.00 18.57 ? 167 PRO A O 1 ATOM 683 C CB . PRO A 1 86 ? 9.024 9.732 61.711 1.00 10.12 ? 167 PRO A CB 1 ATOM 684 C CG . PRO A 1 86 ? 8.715 10.706 62.824 1.00 12.70 ? 167 PRO A CG 1 ATOM 685 C CD . PRO A 1 86 ? 7.462 11.382 62.352 1.00 12.43 ? 167 PRO A CD 1 ATOM 686 N N . THR A 1 87 ? 6.393 7.168 61.933 1.00 13.63 ? 168 THR A N 1 ATOM 687 C CA . THR A 1 87 ? 5.856 6.032 62.667 1.00 14.72 ? 168 THR A CA 1 ATOM 688 C C . THR A 1 87 ? 6.624 4.749 62.431 1.00 11.83 ? 168 THR A C 1 ATOM 689 O O . THR A 1 87 ? 7.038 4.583 61.298 1.00 12.07 ? 168 THR A O 1 ATOM 690 C CB . THR A 1 87 ? 4.411 6.001 62.219 1.00 16.05 ? 168 THR A CB 1 ATOM 691 O OG1 . THR A 1 87 ? 3.720 6.679 63.253 1.00 18.96 ? 168 THR A OG1 1 ATOM 692 C CG2 . THR A 1 87 ? 3.910 4.658 61.820 1.00 15.20 ? 168 THR A CG2 1 ATOM 693 N N . VAL A 1 88 ? 6.790 3.782 63.318 1.00 11.93 ? 169 VAL A N 1 ATOM 694 C CA . VAL A 1 88 ? 7.448 2.494 63.021 1.00 12.13 ? 169 VAL A CA 1 ATOM 695 C C . VAL A 1 88 ? 6.905 1.713 61.795 1.00 13.45 ? 169 VAL A C 1 ATOM 696 O O . VAL A 1 88 ? 7.636 1.054 61.071 1.00 14.71 ? 169 VAL A O 1 ATOM 697 C CB . VAL A 1 88 ? 7.388 1.575 64.270 1.00 12.63 ? 169 VAL A CB 1 ATOM 698 C CG1 . VAL A 1 88 ? 8.020 0.191 63.970 1.00 11.61 ? 169 VAL A CG1 1 ATOM 699 C CG2 . VAL A 1 88 ? 8.189 2.210 65.422 1.00 13.20 ? 169 VAL A CG2 1 ATOM 700 N N . TYR A 1 89 A 5.594 1.784 61.590 1.00 12.62 ? 169 TYR A N 1 ATOM 701 C CA . TYR A 1 89 A 4.802 1.076 60.600 1.00 11.91 ? 169 TYR A CA 1 ATOM 702 C C . TYR A 1 89 A 4.646 1.860 59.298 1.00 13.75 ? 169 TYR A C 1 ATOM 703 O O . TYR A 1 89 A 4.237 1.295 58.315 1.00 16.09 ? 169 TYR A O 1 ATOM 704 C CB . TYR A 1 89 A 3.404 0.770 61.242 1.00 9.82 ? 169 TYR A CB 1 ATOM 705 C CG . TYR A 1 89 A 3.456 0.286 62.708 1.00 6.90 ? 169 TYR A CG 1 ATOM 706 C CD1 . TYR A 1 89 A 4.133 -0.862 63.017 1.00 7.84 ? 169 TYR A CD1 1 ATOM 707 C CD2 . TYR A 1 89 A 2.927 1.027 63.728 1.00 7.77 ? 169 TYR A CD2 1 ATOM 708 C CE1 . TYR A 1 89 A 4.306 -1.312 64.301 1.00 6.83 ? 169 TYR A CE1 1 ATOM 709 C CE2 . TYR A 1 89 A 3.095 0.610 65.030 1.00 9.69 ? 169 TYR A CE2 1 ATOM 710 C CZ . TYR A 1 89 A 3.790 -0.554 65.299 1.00 8.18 ? 169 TYR A CZ 1 ATOM 711 O OH . TYR A 1 89 A 4.007 -0.987 66.575 1.00 8.77 ? 169 TYR A OH 1 ATOM 712 N N . ASN A 1 90 ? 5.007 3.125 59.146 1.00 16.40 ? 170 ASN A N 1 ATOM 713 C CA . ASN A 1 90 ? 4.692 3.870 57.943 1.00 17.62 ? 170 ASN A CA 1 ATOM 714 C C . ASN A 1 90 ? 5.895 4.498 57.231 1.00 15.57 ? 170 ASN A C 1 ATOM 715 O O . ASN A 1 90 ? 5.716 5.165 56.201 1.00 14.76 ? 170 ASN A O 1 ATOM 716 C CB . ASN A 1 90 ? 3.627 4.935 58.342 1.00 23.07 ? 170 ASN A CB 1 ATOM 717 C CG . ASN A 1 90 ? 4.075 6.352 58.783 1.00 27.98 ? 170 ASN A CG 1 ATOM 718 O OD1 . ASN A 1 90 ? 3.355 7.357 58.642 1.00 29.73 ? 170 ASN A OD1 1 ATOM 719 N ND2 . ASN A 1 90 ? 5.250 6.595 59.349 1.00 28.83 ? 170 ASN A ND2 1 ATOM 720 N N . SER A 1 91 ? 7.094 4.188 57.737 1.00 12.03 ? 171 SER A N 1 ATOM 721 C CA . SER A 1 91 ? 8.383 4.722 57.327 1.00 7.22 ? 171 SER A CA 1 ATOM 722 C C . SER A 1 91 ? 9.130 3.841 56.377 1.00 8.34 ? 171 SER A C 1 ATOM 723 O O . SER A 1 91 ? 9.076 2.634 56.565 1.00 7.51 ? 171 SER A O 1 ATOM 724 C CB . SER A 1 91 ? 9.282 4.866 58.491 1.00 6.65 ? 171 SER A CB 1 ATOM 725 O OG . SER A 1 91 ? 8.667 5.772 59.378 1.00 11.46 ? 171 SER A OG 1 ATOM 726 N N . ARG A 1 92 ? 9.952 4.383 55.483 1.00 7.73 ? 172 ARG A N 1 ATOM 727 C CA . ARG A 1 92 ? 10.648 3.594 54.487 1.00 5.76 ? 172 ARG A CA 1 ATOM 728 C C . ARG A 1 92 ? 12.118 3.861 54.767 1.00 5.56 ? 172 ARG A C 1 ATOM 729 O O . ARG A 1 92 ? 12.494 5.070 54.848 1.00 3.92 ? 172 ARG A O 1 ATOM 730 C CB . ARG A 1 92 ? 10.263 4.094 53.083 1.00 7.75 ? 172 ARG A CB 1 ATOM 731 C CG . ARG A 1 92 ? 10.750 3.194 51.970 1.00 9.39 ? 172 ARG A CG 1 ATOM 732 C CD . ARG A 1 92 ? 10.871 3.950 50.684 1.00 13.07 ? 172 ARG A CD 1 ATOM 733 N NE . ARG A 1 92 ? 9.608 4.289 50.001 1.00 16.93 ? 172 ARG A NE 1 ATOM 734 C CZ . ARG A 1 92 ? 9.571 5.315 49.129 1.00 18.63 ? 172 ARG A CZ 1 ATOM 735 N NH1 . ARG A 1 92 ? 10.619 6.145 48.930 1.00 24.41 ? 172 ARG A NH1 1 ATOM 736 N NH2 . ARG A 1 92 ? 8.469 5.556 48.443 1.00 19.96 ? 172 ARG A NH2 1 ATOM 737 N N . VAL A 1 93 ? 12.971 2.859 55.006 1.00 4.36 ? 173 VAL A N 1 ATOM 738 C CA . VAL A 1 93 ? 14.427 3.104 55.155 1.00 5.45 ? 173 VAL A CA 1 ATOM 739 C C . VAL A 1 93 ? 15.209 3.301 53.835 1.00 5.65 ? 173 VAL A C 1 ATOM 740 O O . VAL A 1 93 ? 15.294 2.414 52.967 1.00 3.80 ? 173 VAL A O 1 ATOM 741 C CB . VAL A 1 93 ? 15.081 2.003 55.957 1.00 2.20 ? 173 VAL A CB 1 ATOM 742 C CG1 . VAL A 1 93 ? 16.534 2.246 56.192 1.00 2.00 ? 173 VAL A CG1 1 ATOM 743 C CG2 . VAL A 1 93 ? 14.369 1.904 57.294 1.00 2.00 ? 173 VAL A CG2 1 ATOM 744 N N . GLU A 1 94 ? 15.803 4.471 53.611 1.00 7.35 ? 174 GLU A N 1 ATOM 745 C CA . GLU A 1 94 ? 16.614 4.740 52.443 1.00 7.93 ? 174 GLU A CA 1 ATOM 746 C C . GLU A 1 94 ? 18.064 4.150 52.419 1.00 10.93 ? 174 GLU A C 1 ATOM 747 O O . GLU A 1 94 ? 18.549 3.622 51.390 1.00 12.71 ? 174 GLU A O 1 ATOM 748 C CB . GLU A 1 94 ? 16.668 6.219 52.316 1.00 8.30 ? 174 GLU A CB 1 ATOM 749 C CG . GLU A 1 94 ? 15.305 6.891 52.205 1.00 11.42 ? 174 GLU A CG 1 ATOM 750 C CD . GLU A 1 94 ? 14.510 6.535 50.942 1.00 14.07 ? 174 GLU A CD 1 ATOM 751 O OE1 . GLU A 1 94 ? 15.158 6.490 49.876 1.00 16.23 ? 174 GLU A OE1 1 ATOM 752 O OE2 . GLU A 1 94 ? 13.274 6.325 51.017 1.00 11.98 ? 174 GLU A OE2 1 ATOM 753 N N . CYS A 1 95 ? 18.740 4.137 53.571 1.00 6.63 ? 175 CYS A N 1 ATOM 754 C CA . CYS A 1 95 ? 20.134 3.757 53.745 1.00 6.75 ? 175 CYS A CA 1 ATOM 755 C C . CYS A 1 95 ? 20.474 3.917 55.235 1.00 6.77 ? 175 CYS A C 1 ATOM 756 O O . CYS A 1 95 ? 19.748 4.554 56.006 1.00 6.62 ? 175 CYS A O 1 ATOM 757 C CB . CYS A 1 95 ? 21.094 4.659 52.821 1.00 7.27 ? 175 CYS A CB 1 ATOM 758 S SG . CYS A 1 95 ? 21.142 6.469 52.809 1.00 8.23 ? 175 CYS A SG 1 ATOM 759 N N . ILE A 1 96 ? 21.598 3.377 55.667 1.00 5.65 ? 176 ILE A N 1 ATOM 760 C CA . ILE A 1 96 ? 21.912 3.291 57.104 1.00 6.49 ? 176 ILE A CA 1 ATOM 761 C C . ILE A 1 96 ? 23.060 4.298 57.338 1.00 7.47 ? 176 ILE A C 1 ATOM 762 O O . ILE A 1 96 ? 23.979 4.384 56.503 1.00 6.14 ? 176 ILE A O 1 ATOM 763 C CB . ILE A 1 96 ? 22.364 1.847 57.472 1.00 6.12 ? 176 ILE A CB 1 ATOM 764 C CG1 . ILE A 1 96 ? 21.196 0.849 57.338 1.00 6.02 ? 176 ILE A CG1 1 ATOM 765 C CG2 . ILE A 1 96 ? 22.918 1.846 58.889 1.00 7.42 ? 176 ILE A CG2 1 ATOM 766 C CD1 . ILE A 1 96 ? 19.947 0.920 58.260 1.00 4.48 ? 176 ILE A CD1 1 ATOM 767 N N . GLY A 1 97 ? 23.008 5.096 58.395 1.00 7.71 ? 177 GLY A N 1 ATOM 768 C CA . GLY A 1 97 ? 23.974 6.150 58.537 1.00 9.69 ? 177 GLY A CA 1 ATOM 769 C C . GLY A 1 97 ? 23.488 7.326 59.358 1.00 9.40 ? 177 GLY A C 1 ATOM 770 O O . GLY A 1 97 ? 22.302 7.485 59.618 1.00 10.10 ? 177 GLY A O 1 ATOM 771 N N . TRP A 1 98 ? 24.450 8.116 59.800 1.00 8.98 ? 178 TRP A N 1 ATOM 772 C CA . TRP A 1 98 ? 24.196 9.249 60.698 1.00 9.50 ? 178 TRP A CA 1 ATOM 773 C C . TRP A 1 98 ? 24.411 10.681 60.174 1.00 8.87 ? 178 TRP A C 1 ATOM 774 O O . TRP A 1 98 ? 24.441 11.630 60.987 1.00 9.45 ? 178 TRP A O 1 ATOM 775 C CB . TRP A 1 98 ? 24.997 8.988 61.999 1.00 9.16 ? 178 TRP A CB 1 ATOM 776 C CG . TRP A 1 98 ? 26.477 8.537 61.911 1.00 11.20 ? 178 TRP A CG 1 ATOM 777 C CD1 . TRP A 1 98 ? 26.873 7.300 62.383 1.00 9.20 ? 178 TRP A CD1 1 ATOM 778 C CD2 . TRP A 1 98 ? 27.523 9.255 61.363 1.00 10.69 ? 178 TRP A CD2 1 ATOM 779 N NE1 . TRP A 1 98 ? 28.159 7.257 62.123 1.00 8.60 ? 178 TRP A NE1 1 ATOM 780 C CE2 . TRP A 1 98 ? 28.573 8.383 61.512 1.00 9.24 ? 178 TRP A CE2 1 ATOM 781 C CE3 . TRP A 1 98 ? 27.716 10.496 60.757 1.00 12.10 ? 178 TRP A CE3 1 ATOM 782 C CZ2 . TRP A 1 98 ? 29.819 8.765 61.055 1.00 10.95 ? 178 TRP A CZ2 1 ATOM 783 C CZ3 . TRP A 1 98 ? 28.969 10.862 60.293 1.00 12.00 ? 178 TRP A CZ3 1 ATOM 784 C CH2 . TRP A 1 98 ? 30.020 9.983 60.444 1.00 11.94 ? 178 TRP A CH2 1 ATOM 785 N N . SER A 1 99 ? 24.610 10.817 58.842 1.00 9.24 ? 179 SER A N 1 ATOM 786 C CA . SER A 1 99 ? 24.715 12.063 58.057 1.00 8.01 ? 179 SER A CA 1 ATOM 787 C C . SER A 1 99 ? 24.121 11.727 56.693 1.00 7.92 ? 179 SER A C 1 ATOM 788 O O . SER A 1 99 ? 24.300 10.592 56.269 1.00 9.64 ? 179 SER A O 1 ATOM 789 C CB . SER A 1 99 ? 26.168 12.519 57.830 1.00 6.51 ? 179 SER A CB 1 ATOM 790 O OG . SER A 1 99 ? 26.169 13.855 57.313 1.00 8.37 ? 179 SER A OG 1 ATOM 791 N N . SER A 1 100 ? 23.453 12.608 55.961 1.00 8.22 ? 180 SER A N 1 ATOM 792 C CA . SER A 1 100 ? 22.803 12.267 54.705 1.00 8.95 ? 180 SER A CA 1 ATOM 793 C C . SER A 1 100 ? 22.381 13.471 53.840 1.00 10.20 ? 180 SER A C 1 ATOM 794 O O . SER A 1 100 ? 22.435 14.654 54.252 1.00 10.53 ? 180 SER A O 1 ATOM 795 C CB . SER A 1 100 ? 21.553 11.432 54.981 1.00 7.41 ? 180 SER A CB 1 ATOM 796 O OG . SER A 1 100 ? 20.488 12.266 55.425 1.00 7.43 ? 180 SER A OG 1 ATOM 797 N N . THR A 1 101 ? 21.988 13.113 52.612 1.00 10.59 ? 181 THR A N 1 ATOM 798 C CA . THR A 1 101 ? 21.442 14.008 51.610 1.00 11.21 ? 181 THR A CA 1 ATOM 799 C C . THR A 1 101 ? 20.775 13.087 50.602 1.00 9.78 ? 181 THR A C 1 ATOM 800 O O . THR A 1 101 ? 21.087 11.903 50.545 1.00 8.25 ? 181 THR A O 1 ATOM 801 C CB . THR A 1 101 ? 22.562 14.872 50.945 1.00 11.92 ? 181 THR A CB 1 ATOM 802 O OG1 . THR A 1 101 ? 21.870 15.729 50.015 1.00 12.50 ? 181 THR A OG1 1 ATOM 803 C CG2 . THR A 1 101 ? 23.663 14.076 50.279 1.00 12.64 ? 181 THR A CG2 1 ATOM 804 N N . SER A 1 102 ? 19.773 13.615 49.902 1.00 11.56 ? 182 SER A N 1 ATOM 805 C CA . SER A 1 102 ? 18.982 12.944 48.844 1.00 10.17 ? 182 SER A CA 1 ATOM 806 C C . SER A 1 102 ? 18.274 13.859 47.815 1.00 9.89 ? 182 SER A C 1 ATOM 807 O O . SER A 1 102 ? 17.796 14.959 48.158 1.00 8.78 ? 182 SER A O 1 ATOM 808 C CB . SER A 1 102 ? 17.951 12.082 49.536 1.00 9.70 ? 182 SER A CB 1 ATOM 809 O OG . SER A 1 102 ? 17.352 11.070 48.742 1.00 8.85 ? 182 SER A OG 1 ATOM 810 N N . CYS A 1 103 ? 18.217 13.448 46.539 1.00 11.05 ? 183 CYS A N 1 ATOM 811 C CA . CYS A 1 103 ? 17.468 14.185 45.508 1.00 9.90 ? 183 CYS A CA 1 ATOM 812 C C . CYS A 1 103 ? 17.077 13.220 44.389 1.00 7.99 ? 183 CYS A C 1 ATOM 813 O O . CYS A 1 103 ? 17.693 12.172 44.193 1.00 8.07 ? 183 CYS A O 1 ATOM 814 C CB . CYS A 1 103 ? 18.364 15.323 44.944 1.00 10.41 ? 183 CYS A CB 1 ATOM 815 S SG . CYS A 1 103 ? 20.119 14.949 44.577 1.00 8.41 ? 183 CYS A SG 1 ATOM 816 N N . HIS A 1 104 ? 16.072 13.610 43.646 1.00 4.11 ? 184 HIS A N 1 ATOM 817 C CA . HIS A 1 104 ? 15.521 12.867 42.559 1.00 5.34 ? 184 HIS A CA 1 ATOM 818 C C . HIS A 1 104 ? 16.026 13.600 41.320 1.00 4.80 ? 184 HIS A C 1 ATOM 819 O O . HIS A 1 104 ? 16.106 14.842 41.219 1.00 3.37 ? 184 HIS A O 1 ATOM 820 C CB . HIS A 1 104 ? 13.992 12.900 42.711 1.00 5.75 ? 184 HIS A CB 1 ATOM 821 C CG . HIS A 1 104 ? 13.384 11.970 41.703 1.00 7.38 ? 184 HIS A CG 1 ATOM 822 N ND1 . HIS A 1 104 ? 13.338 12.038 40.383 1.00 7.99 ? 184 HIS A ND1 1 ATOM 823 C CD2 . HIS A 1 104 ? 12.844 10.781 42.077 1.00 8.53 ? 184 HIS A CD2 1 ATOM 824 C CE1 . HIS A 1 104 ? 12.799 10.945 39.925 1.00 8.07 ? 184 HIS A CE1 1 ATOM 825 N NE2 . HIS A 1 104 ? 12.508 10.196 40.958 1.00 7.32 ? 184 HIS A NE2 1 ATOM 826 N N . ASP A 1 105 ? 16.385 12.834 40.321 1.00 6.45 ? 185 ASP A N 1 ATOM 827 C CA . ASP A 1 105 ? 16.963 13.431 39.110 1.00 4.93 ? 185 ASP A CA 1 ATOM 828 C C . ASP A 1 105 ? 15.999 13.522 37.928 1.00 3.54 ? 185 ASP A C 1 ATOM 829 O O . ASP A 1 105 ? 16.351 13.970 36.839 1.00 6.42 ? 185 ASP A O 1 ATOM 830 C CB . ASP A 1 105 ? 18.233 12.671 38.690 1.00 3.84 ? 185 ASP A CB 1 ATOM 831 C CG . ASP A 1 105 ? 18.156 11.241 38.155 1.00 6.15 ? 185 ASP A CG 1 ATOM 832 O OD1 . ASP A 1 105 ? 17.077 10.647 38.010 1.00 7.07 ? 185 ASP A OD1 1 ATOM 833 O OD2 . ASP A 1 105 ? 19.233 10.764 37.853 1.00 4.05 ? 185 ASP A OD2 1 ATOM 834 N N . GLY A 1 106 ? 14.744 13.188 38.121 1.00 3.98 ? 186 GLY A N 1 ATOM 835 C CA . GLY A 1 106 ? 13.747 13.181 37.087 1.00 4.51 ? 186 GLY A CA 1 ATOM 836 C C . GLY A 1 106 ? 13.546 11.726 36.659 1.00 8.40 ? 186 GLY A C 1 ATOM 837 O O . GLY A 1 106 ? 12.425 11.289 36.330 1.00 8.32 ? 186 GLY A O 1 ATOM 838 N N . LYS A 1 107 ? 14.631 10.950 36.616 1.00 6.47 ? 187 LYS A N 1 ATOM 839 C CA . LYS A 1 107 ? 14.441 9.507 36.414 1.00 8.48 ? 187 LYS A CA 1 ATOM 840 C C . LYS A 1 107 ? 14.265 8.637 37.669 1.00 7.75 ? 187 LYS A C 1 ATOM 841 O O . LYS A 1 107 ? 13.307 7.850 37.705 1.00 6.74 ? 187 LYS A O 1 ATOM 842 C CB . LYS A 1 107 ? 15.601 8.972 35.581 1.00 10.91 ? 187 LYS A CB 1 ATOM 843 C CG . LYS A 1 107 ? 15.708 9.679 34.256 1.00 12.43 ? 187 LYS A CG 1 ATOM 844 C CD . LYS A 1 107 ? 16.735 8.934 33.470 1.00 13.79 ? 187 LYS A CD 1 ATOM 845 C CE . LYS A 1 107 ? 16.464 9.276 32.022 1.00 16.42 ? 187 LYS A CE 1 ATOM 846 N NZ . LYS A 1 107 ? 17.300 8.549 31.089 1.00 19.43 ? 187 LYS A NZ 1 ATOM 847 N N . THR A 1 108 ? 15.094 8.809 38.732 1.00 6.76 ? 188 THR A N 1 ATOM 848 C CA . THR A 1 108 ? 15.071 8.037 39.969 1.00 5.51 ? 188 THR A CA 1 ATOM 849 C C . THR A 1 108 ? 15.881 8.850 41.025 1.00 6.56 ? 188 THR A C 1 ATOM 850 O O . THR A 1 108 ? 16.318 9.993 40.761 1.00 5.97 ? 188 THR A O 1 ATOM 851 C CB . THR A 1 108 ? 15.599 6.572 39.624 1.00 3.52 ? 188 THR A CB 1 ATOM 852 O OG1 . THR A 1 108 ? 15.378 5.841 40.819 1.00 2.37 ? 188 THR A OG1 1 ATOM 853 C CG2 . THR A 1 108 ? 17.035 6.367 39.344 1.00 3.62 ? 188 THR A CG2 1 ATOM 854 N N . ARG A 1 109 ? 15.930 8.325 42.268 1.00 6.49 ? 189 ARG A N 1 ATOM 855 C CA . ARG A 1 109 ? 16.489 9.010 43.415 1.00 4.75 ? 189 ARG A CA 1 ATOM 856 C C . ARG A 1 109 ? 17.875 8.568 43.830 1.00 4.64 ? 189 ARG A C 1 ATOM 857 O O . ARG A 1 109 ? 18.138 7.365 43.735 1.00 5.98 ? 189 ARG A O 1 ATOM 858 C CB . ARG A 1 109 ? 15.533 8.797 44.579 1.00 3.23 ? 189 ARG A CB 1 ATOM 859 C CG . ARG A 1 109 ? 15.916 9.330 45.946 1.00 5.55 ? 189 ARG A CG 1 ATOM 860 C CD . ARG A 1 109 ? 14.704 9.623 46.796 1.00 7.64 ? 189 ARG A CD 1 ATOM 861 N NE . ARG A 1 109 ? 13.925 10.694 46.191 1.00 12.55 ? 189 ARG A NE 1 ATOM 862 C CZ . ARG A 1 109 ? 13.957 11.953 46.678 1.00 15.18 ? 189 ARG A CZ 1 ATOM 863 N NH1 . ARG A 1 109 ? 14.740 12.324 47.704 1.00 16.85 ? 189 ARG A NH1 1 ATOM 864 N NH2 . ARG A 1 109 ? 13.217 12.891 46.102 1.00 15.70 ? 189 ARG A NH2 1 ATOM 865 N N . MET A 1 110 ? 18.726 9.544 44.234 1.00 3.37 ? 190 MET A N 1 ATOM 866 C CA . MET A 1 110 ? 20.013 9.264 44.807 1.00 5.54 ? 190 MET A CA 1 ATOM 867 C C . MET A 1 110 ? 19.957 9.660 46.284 1.00 6.55 ? 190 MET A C 1 ATOM 868 O O . MET A 1 110 ? 19.376 10.715 46.597 1.00 9.22 ? 190 MET A O 1 ATOM 869 C CB . MET A 1 110 ? 21.014 10.062 44.082 1.00 7.80 ? 190 MET A CB 1 ATOM 870 C CG . MET A 1 110 ? 22.363 9.831 44.758 1.00 11.23 ? 190 MET A CG 1 ATOM 871 S SD . MET A 1 110 ? 23.763 10.731 44.072 1.00 14.39 ? 190 MET A SD 1 ATOM 872 C CE . MET A 1 110 ? 23.403 12.443 44.333 1.00 6.29 ? 190 MET A CE 1 ATOM 873 N N . SER A 1 111 ? 20.373 8.761 47.184 1.00 5.58 ? 191 SER A N 1 ATOM 874 C CA . SER A 1 111 ? 20.410 9.032 48.615 1.00 4.14 ? 191 SER A CA 1 ATOM 875 C C . SER A 1 111 ? 21.846 8.681 49.025 1.00 6.91 ? 191 SER A C 1 ATOM 876 O O . SER A 1 111 ? 22.497 7.834 48.388 1.00 10.17 ? 191 SER A O 1 ATOM 877 C CB . SER A 1 111 ? 19.411 8.133 49.412 1.00 2.47 ? 191 SER A CB 1 ATOM 878 O OG . SER A 1 111 ? 18.016 8.291 49.134 1.00 3.15 ? 191 SER A OG 1 ATOM 879 N N . ILE A 1 112 ? 22.412 9.360 50.028 1.00 7.89 ? 192 ILE A N 1 ATOM 880 C CA . ILE A 1 112 ? 23.770 9.130 50.404 1.00 8.61 ? 192 ILE A CA 1 ATOM 881 C C . ILE A 1 112 ? 23.740 9.050 51.883 1.00 7.26 ? 192 ILE A C 1 ATOM 882 O O . ILE A 1 112 ? 23.204 9.951 52.507 1.00 6.15 ? 192 ILE A O 1 ATOM 883 C CB . ILE A 1 112 ? 24.667 10.287 49.966 1.00 9.28 ? 192 ILE A CB 1 ATOM 884 C CG1 . ILE A 1 112 ? 24.578 10.415 48.431 1.00 7.72 ? 192 ILE A CG1 1 ATOM 885 C CG2 . ILE A 1 112 ? 26.083 10.060 50.487 1.00 10.41 ? 192 ILE A CG2 1 ATOM 886 C CD1 . ILE A 1 112 ? 25.482 11.428 47.737 1.00 3.72 ? 192 ILE A CD1 1 ATOM 887 N N . CYS A 1 113 ? 24.334 7.986 52.422 1.00 7.25 ? 193 CYS A N 1 ATOM 888 C CA . CYS A 1 113 ? 24.439 7.892 53.889 1.00 5.90 ? 193 CYS A CA 1 ATOM 889 C C . CYS A 1 113 ? 25.874 7.532 54.255 1.00 6.69 ? 193 CYS A C 1 ATOM 890 O O . CYS A 1 113 ? 26.638 6.847 53.553 1.00 9.18 ? 193 CYS A O 1 ATOM 891 C CB . CYS A 1 113 ? 23.539 6.826 54.560 1.00 5.27 ? 193 CYS A CB 1 ATOM 892 S SG . CYS A 1 113 ? 21.733 7.017 54.702 1.00 5.83 ? 193 CYS A SG 1 ATOM 893 N N . ILE A 1 114 ? 26.244 8.176 55.357 1.00 6.66 ? 194 ILE A N 1 ATOM 894 C CA . ILE A 1 114 ? 27.551 8.010 55.962 1.00 5.18 ? 194 ILE A CA 1 ATOM 895 C C . ILE A 1 114 ? 27.530 7.327 57.319 1.00 5.09 ? 194 ILE A C 1 ATOM 896 O O . ILE A 1 114 ? 26.738 7.729 58.181 1.00 3.81 ? 194 ILE A O 1 ATOM 897 C CB . ILE A 1 114 ? 28.206 9.429 56.077 1.00 5.13 ? 194 ILE A CB 1 ATOM 898 C CG1 . ILE A 1 114 ? 28.274 10.057 54.684 1.00 5.12 ? 194 ILE A CG1 1 ATOM 899 C CG2 . ILE A 1 114 ? 29.624 9.330 56.670 1.00 5.37 ? 194 ILE A CG2 1 ATOM 900 C CD1 . ILE A 1 114 ? 28.648 11.536 54.575 1.00 7.05 ? 194 ILE A CD1 1 ATOM 901 N N . SER A 1 115 ? 28.329 6.281 57.523 1.00 6.31 ? 195 SER A N 1 ATOM 902 C CA . SER A 1 115 ? 28.432 5.686 58.844 1.00 7.94 ? 195 SER A CA 1 ATOM 903 C C . SER A 1 115 ? 29.911 5.444 59.154 1.00 9.16 ? 195 SER A C 1 ATOM 904 O O . SER A 1 115 ? 30.747 5.716 58.280 1.00 10.32 ? 195 SER A O 1 ATOM 905 C CB . SER A 1 115 ? 27.619 4.382 58.883 1.00 8.65 ? 195 SER A CB 1 ATOM 906 O OG . SER A 1 115 ? 28.255 3.268 58.271 1.00 10.37 ? 195 SER A OG 1 ATOM 907 N N . GLY A 1 116 ? 30.327 4.967 60.336 1.00 8.46 ? 196 GLY A N 1 ATOM 908 C CA . GLY A 1 116 ? 31.739 4.772 60.611 1.00 10.78 ? 196 GLY A CA 1 ATOM 909 C C . GLY A 1 116 ? 32.069 5.225 62.031 1.00 13.04 ? 196 GLY A C 1 ATOM 910 O O . GLY A 1 116 ? 31.222 5.848 62.706 1.00 13.51 ? 196 GLY A O 1 ATOM 911 N N . PRO A 1 117 ? 33.257 4.937 62.559 1.00 11.27 ? 197 PRO A N 1 ATOM 912 C CA . PRO A 1 117 ? 33.804 5.725 63.637 1.00 11.87 ? 197 PRO A CA 1 ATOM 913 C C . PRO A 1 117 ? 34.305 7.057 63.090 1.00 14.14 ? 197 PRO A C 1 ATOM 914 O O . PRO A 1 117 ? 34.466 7.296 61.872 1.00 15.46 ? 197 PRO A O 1 ATOM 915 C CB . PRO A 1 117 ? 34.854 4.833 64.233 1.00 8.84 ? 197 PRO A CB 1 ATOM 916 C CG . PRO A 1 117 ? 35.263 3.909 63.158 1.00 8.94 ? 197 PRO A CG 1 ATOM 917 C CD . PRO A 1 117 ? 34.054 3.771 62.265 1.00 10.18 ? 197 PRO A CD 1 ATOM 918 N N . ASN A 1 118 ? 34.530 7.937 64.052 1.00 16.60 ? 198 ASN A N 1 ATOM 919 C CA . ASN A 1 118 ? 34.947 9.285 63.762 1.00 17.50 ? 198 ASN A CA 1 ATOM 920 C C . ASN A 1 118 ? 36.115 9.407 62.859 1.00 16.26 ? 198 ASN A C 1 ATOM 921 O O . ASN A 1 118 ? 36.109 10.251 61.975 1.00 17.05 ? 198 ASN A O 1 ATOM 922 C CB . ASN A 1 118 ? 35.205 10.012 65.078 1.00 19.62 ? 198 ASN A CB 1 ATOM 923 C CG . ASN A 1 118 ? 33.885 10.558 65.627 1.00 21.62 ? 198 ASN A CG 1 ATOM 924 O OD1 . ASN A 1 118 ? 32.811 10.125 65.209 1.00 23.35 ? 198 ASN A OD1 1 ATOM 925 N ND2 . ASN A 1 118 ? 33.790 11.542 66.521 1.00 23.27 ? 198 ASN A ND2 1 ATOM 926 N N . ASN A 1 119 ? 37.039 8.465 62.992 1.00 16.51 ? 199 ASN A N 1 ATOM 927 C CA . ASN A 1 119 ? 38.283 8.380 62.230 1.00 15.65 ? 199 ASN A CA 1 ATOM 928 C C . ASN A 1 119 ? 38.306 7.315 61.136 1.00 15.86 ? 199 ASN A C 1 ATOM 929 O O . ASN A 1 119 ? 39.378 6.999 60.625 1.00 17.28 ? 199 ASN A O 1 ATOM 930 C CB . ASN A 1 119 ? 39.464 8.098 63.177 1.00 17.48 ? 199 ASN A CB 1 ATOM 931 C CG . ASN A 1 119 ? 39.534 6.706 63.811 1.00 18.65 ? 199 ASN A CG 1 ATOM 932 O OD1 . ASN A 1 119 ? 38.554 5.949 63.912 1.00 20.18 ? 199 ASN A OD1 1 ATOM 933 N ND2 . ASN A 1 119 ? 40.708 6.322 64.280 1.00 16.57 ? 199 ASN A ND2 1 ATOM 934 N N . ASN A 1 120 ? 37.209 6.714 60.708 1.00 13.56 ? 200 ASN A N 1 ATOM 935 C CA . ASN A 1 120 ? 37.282 5.701 59.680 1.00 10.64 ? 200 ASN A CA 1 ATOM 936 C C . ASN A 1 120 ? 35.896 5.466 59.126 1.00 9.58 ? 200 ASN A C 1 ATOM 937 O O . ASN A 1 120 ? 35.435 4.335 58.908 1.00 10.76 ? 200 ASN A O 1 ATOM 938 C CB . ASN A 1 120 ? 37.830 4.423 60.254 1.00 10.46 ? 200 ASN A CB 1 ATOM 939 C CG . ASN A 1 120 ? 38.957 3.725 59.475 1.00 13.59 ? 200 ASN A CG 1 ATOM 940 O OD1 . ASN A 1 120 ? 39.411 4.061 58.384 1.00 11.73 ? 200 ASN A OD1 1 ATOM 941 N ND2 . ASN A 1 120 ? 39.380 2.653 60.153 1.00 15.68 ? 200 ASN A ND2 1 ATOM 942 N N . ALA A 1 121 ? 35.313 6.589 58.716 1.00 7.99 ? 201 ALA A N 1 ATOM 943 C CA . ALA A 1 121 ? 33.929 6.606 58.254 1.00 9.85 ? 201 ALA A CA 1 ATOM 944 C C . ALA A 1 121 ? 33.852 6.533 56.721 1.00 10.56 ? 201 ALA A C 1 ATOM 945 O O . ALA A 1 121 ? 34.850 6.805 56.007 1.00 10.01 ? 201 ALA A O 1 ATOM 946 C CB . ALA A 1 121 ? 33.232 7.891 58.724 1.00 10.94 ? 201 ALA A CB 1 ATOM 947 N N . SER A 1 122 ? 32.717 6.112 56.160 1.00 11.44 ? 202 SER A N 1 ATOM 948 C CA . SER A 1 122 ? 32.590 6.057 54.696 1.00 10.76 ? 202 SER A CA 1 ATOM 949 C C . SER A 1 122 ? 31.225 6.474 54.187 1.00 9.86 ? 202 SER A C 1 ATOM 950 O O . SER A 1 122 ? 30.254 6.246 54.906 1.00 9.92 ? 202 SER A O 1 ATOM 951 C CB . SER A 1 122 ? 32.922 4.607 54.256 1.00 11.44 ? 202 SER A CB 1 ATOM 952 O OG . SER A 1 122 ? 32.421 3.593 55.160 1.00 12.84 ? 202 SER A OG 1 ATOM 953 N N . ALA A 1 123 ? 31.100 6.990 52.961 1.00 8.05 ? 203 ALA A N 1 ATOM 954 C CA . ALA A 1 123 ? 29.809 7.258 52.348 1.00 8.55 ? 203 ALA A CA 1 ATOM 955 C C . ALA A 1 123 ? 29.475 6.147 51.337 1.00 8.76 ? 203 ALA A C 1 ATOM 956 O O . ALA A 1 123 ? 30.409 5.651 50.671 1.00 7.89 ? 203 ALA A O 1 ATOM 957 C CB . ALA A 1 123 ? 29.856 8.598 51.615 1.00 4.44 ? 203 ALA A CB 1 ATOM 958 N N . VAL A 1 124 ? 28.204 5.694 51.221 1.00 7.95 ? 204 VAL A N 1 ATOM 959 C CA . VAL A 1 124 ? 27.860 4.765 50.142 1.00 9.61 ? 204 VAL A CA 1 ATOM 960 C C . VAL A 1 124 ? 26.582 5.384 49.551 1.00 10.67 ? 204 VAL A C 1 ATOM 961 O O . VAL A 1 124 ? 25.729 5.930 50.260 1.00 13.43 ? 204 VAL A O 1 ATOM 962 C CB . VAL A 1 124 ? 27.748 3.248 50.676 1.00 9.89 ? 204 VAL A CB 1 ATOM 963 C CG1 . VAL A 1 124 ? 27.458 3.156 52.131 1.00 8.11 ? 204 VAL A CG1 1 ATOM 964 C CG2 . VAL A 1 124 ? 26.698 2.520 49.865 1.00 9.50 ? 204 VAL A CG2 1 ATOM 965 N N . ILE A 1 125 ? 26.616 5.491 48.202 1.00 11.66 ? 205 ILE A N 1 ATOM 966 C CA . ILE A 1 125 ? 25.717 6.272 47.317 1.00 10.81 ? 205 ILE A CA 1 ATOM 967 C C . ILE A 1 125 ? 24.804 5.234 46.738 1.00 8.94 ? 205 ILE A C 1 ATOM 968 O O . ILE A 1 125 ? 25.299 4.280 46.123 1.00 10.07 ? 205 ILE A O 1 ATOM 969 C CB . ILE A 1 125 ? 26.494 6.953 46.144 1.00 10.91 ? 205 ILE A CB 1 ATOM 970 C CG1 . ILE A 1 125 ? 27.395 8.084 46.625 1.00 10.85 ? 205 ILE A CG1 1 ATOM 971 C CG2 . ILE A 1 125 ? 25.515 7.516 45.158 1.00 6.69 ? 205 ILE A CG2 1 ATOM 972 C CD1 . ILE A 1 125 ? 28.595 7.727 47.521 1.00 9.85 ? 205 ILE A CD1 1 ATOM 973 N N . TRP A 1 126 ? 23.536 5.399 47.059 1.00 7.18 ? 206 TRP A N 1 ATOM 974 C CA . TRP A 1 126 ? 22.506 4.520 46.561 1.00 8.34 ? 206 TRP A CA 1 ATOM 975 C C . TRP A 1 126 ? 21.801 5.188 45.382 1.00 8.71 ? 206 TRP A C 1 ATOM 976 O O . TRP A 1 126 ? 21.489 6.372 45.518 1.00 11.96 ? 206 TRP A O 1 ATOM 977 C CB . TRP A 1 126 ? 21.552 4.303 47.717 1.00 10.41 ? 206 TRP A CB 1 ATOM 978 C CG . TRP A 1 126 ? 22.044 3.438 48.860 1.00 10.34 ? 206 TRP A CG 1 ATOM 979 C CD1 . TRP A 1 126 ? 23.042 3.810 49.720 1.00 11.55 ? 206 TRP A CD1 1 ATOM 980 C CD2 . TRP A 1 126 ? 21.537 2.206 49.146 1.00 9.64 ? 206 TRP A CD2 1 ATOM 981 N NE1 . TRP A 1 126 ? 23.166 2.794 50.557 1.00 11.31 ? 206 TRP A NE1 1 ATOM 982 C CE2 . TRP A 1 126 ? 22.274 1.816 50.251 1.00 10.57 ? 206 TRP A CE2 1 ATOM 983 C CE3 . TRP A 1 126 ? 20.552 1.448 48.582 1.00 8.41 ? 206 TRP A CE3 1 ATOM 984 C CZ2 . TRP A 1 126 ? 22.000 0.590 50.837 1.00 10.84 ? 206 TRP A CZ2 1 ATOM 985 C CZ3 . TRP A 1 126 ? 20.302 0.235 49.168 1.00 11.04 ? 206 TRP A CZ3 1 ATOM 986 C CH2 . TRP A 1 126 ? 21.002 -0.183 50.274 1.00 12.17 ? 206 TRP A CH2 1 ATOM 987 N N . TYR A 1 127 ? 21.555 4.569 44.235 1.00 6.79 ? 207 TYR A N 1 ATOM 988 C CA . TYR A 1 127 ? 20.829 5.172 43.115 1.00 6.47 ? 207 TYR A CA 1 ATOM 989 C C . TYR A 1 127 ? 19.797 4.110 42.732 1.00 8.39 ? 207 TYR A C 1 ATOM 990 O O . TYR A 1 127 ? 20.096 2.909 42.675 1.00 8.45 ? 207 TYR A O 1 ATOM 991 C CB . TYR A 1 127 ? 21.797 5.459 41.982 1.00 4.97 ? 207 TYR A CB 1 ATOM 992 C CG . TYR A 1 127 ? 21.153 6.166 40.795 1.00 4.31 ? 207 TYR A CG 1 ATOM 993 C CD1 . TYR A 1 127 ? 20.660 7.464 40.908 1.00 4.12 ? 207 TYR A CD1 1 ATOM 994 C CD2 . TYR A 1 127 ? 21.048 5.501 39.604 1.00 5.27 ? 207 TYR A CD2 1 ATOM 995 C CE1 . TYR A 1 127 ? 20.039 8.099 39.836 1.00 7.01 ? 207 TYR A CE1 1 ATOM 996 C CE2 . TYR A 1 127 ? 20.442 6.101 38.537 1.00 5.77 ? 207 TYR A CE2 1 ATOM 997 C CZ . TYR A 1 127 ? 19.947 7.394 38.642 1.00 7.96 ? 207 TYR A CZ 1 ATOM 998 O OH . TYR A 1 127 ? 19.285 7.939 37.543 1.00 8.78 ? 207 TYR A OH 1 ATOM 999 N N . ASN A 1 128 ? 18.513 4.487 42.586 1.00 10.07 ? 208 ASN A N 1 ATOM 1000 C CA . ASN A 1 128 ? 17.416 3.540 42.295 1.00 9.25 ? 208 ASN A CA 1 ATOM 1001 C C . ASN A 1 128 ? 17.286 2.340 43.268 1.00 10.82 ? 208 ASN A C 1 ATOM 1002 O O . ASN A 1 128 ? 17.203 1.174 42.898 1.00 10.45 ? 208 ASN A O 1 ATOM 1003 C CB . ASN A 1 128 ? 17.631 3.044 40.903 1.00 8.39 ? 208 ASN A CB 1 ATOM 1004 C CG . ASN A 1 128 ? 16.374 2.462 40.331 1.00 10.03 ? 208 ASN A CG 1 ATOM 1005 O OD1 . ASN A 1 128 ? 15.242 2.820 40.668 1.00 8.69 ? 208 ASN A OD1 1 ATOM 1006 N ND2 . ASN A 1 128 ? 16.628 1.486 39.478 1.00 10.63 ? 208 ASN A ND2 1 ATOM 1007 N N . ARG A 1 129 ? 17.219 2.615 44.581 1.00 12.35 ? 209 ARG A N 1 ATOM 1008 C CA . ARG A 1 129 ? 17.216 1.678 45.701 1.00 10.12 ? 209 ARG A CA 1 ATOM 1009 C C . ARG A 1 129 ? 18.413 0.702 45.741 1.00 9.34 ? 209 ARG A C 1 ATOM 1010 O O . ARG A 1 129 ? 18.387 -0.249 46.514 1.00 9.46 ? 209 ARG A O 1 ATOM 1011 C CB . ARG A 1 129 ? 15.934 0.844 45.724 0.02 10.87 ? 209 ARG A CB 1 ATOM 1012 C CG . ARG A 1 129 ? 14.636 1.600 46.007 0.02 11.43 ? 209 ARG A CG 1 ATOM 1013 C CD . ARG A 1 129 ? 13.792 0.838 47.027 0.02 12.06 ? 209 ARG A CD 1 ATOM 1014 N NE . ARG A 1 129 ? 14.405 0.916 48.347 0.02 12.39 ? 209 ARG A NE 1 ATOM 1015 C CZ . ARG A 1 129 ? 14.611 -0.151 49.132 0.02 12.67 ? 209 ARG A CZ 1 ATOM 1016 N NH1 . ARG A 1 129 ? 14.247 -1.377 48.760 0.02 12.85 ? 209 ARG A NH1 1 ATOM 1017 N NH2 . ARG A 1 129 ? 15.189 0.001 50.322 0.02 12.77 ? 209 ARG A NH2 1 ATOM 1018 N N . ARG A 1 130 ? 19.534 0.863 45.035 1.00 9.37 ? 210 ARG A N 1 ATOM 1019 C CA . ARG A 1 130 ? 20.656 -0.058 45.151 1.00 6.93 ? 210 ARG A CA 1 ATOM 1020 C C . ARG A 1 130 ? 21.967 0.702 45.455 1.00 8.34 ? 210 ARG A C 1 ATOM 1021 O O . ARG A 1 130 ? 22.140 1.847 45.008 1.00 8.61 ? 210 ARG A O 1 ATOM 1022 C CB . ARG A 1 130 ? 20.836 -0.806 43.852 1.00 6.11 ? 210 ARG A CB 1 ATOM 1023 C CG . ARG A 1 130 ? 19.751 -1.718 43.356 1.00 7.48 ? 210 ARG A CG 1 ATOM 1024 C CD . ARG A 1 130 ? 20.075 -2.261 41.983 1.00 6.26 ? 210 ARG A CD 1 ATOM 1025 N NE . ARG A 1 130 ? 19.035 -3.238 41.690 1.00 8.74 ? 210 ARG A NE 1 ATOM 1026 C CZ . ARG A 1 130 ? 18.050 -2.985 40.803 1.00 8.33 ? 210 ARG A CZ 1 ATOM 1027 N NH1 . ARG A 1 130 ? 17.978 -1.828 40.156 1.00 10.42 ? 210 ARG A NH1 1 ATOM 1028 N NH2 . ARG A 1 130 ? 17.040 -3.828 40.593 1.00 9.15 ? 210 ARG A NH2 1 ATOM 1029 N N . PRO A 1 131 ? 22.966 0.139 46.173 1.00 7.01 ? 211 PRO A N 1 ATOM 1030 C CA . PRO A 1 131 ? 24.334 0.679 46.259 1.00 5.28 ? 211 PRO A CA 1 ATOM 1031 C C . PRO A 1 131 ? 25.100 0.700 44.965 1.00 8.05 ? 211 PRO A C 1 ATOM 1032 O O . PRO A 1 131 ? 25.109 -0.313 44.276 1.00 10.75 ? 211 PRO A O 1 ATOM 1033 C CB . PRO A 1 131 ? 25.034 -0.166 47.292 1.00 5.44 ? 211 PRO A CB 1 ATOM 1034 C CG . PRO A 1 131 ? 24.252 -1.465 47.436 1.00 3.18 ? 211 PRO A CG 1 ATOM 1035 C CD . PRO A 1 131 ? 22.852 -1.105 46.927 1.00 5.29 ? 211 PRO A CD 1 ATOM 1036 N N . VAL A 1 132 ? 25.688 1.832 44.597 1.00 6.75 ? 212 VAL A N 1 ATOM 1037 C CA . VAL A 1 132 ? 26.502 1.886 43.397 1.00 5.62 ? 212 VAL A CA 1 ATOM 1038 C C . VAL A 1 132 ? 27.937 2.354 43.682 1.00 3.98 ? 212 VAL A C 1 ATOM 1039 O O . VAL A 1 132 ? 28.920 1.804 43.198 1.00 3.32 ? 212 VAL A O 1 ATOM 1040 C CB . VAL A 1 132 ? 25.729 2.793 42.453 1.00 6.12 ? 212 VAL A CB 1 ATOM 1041 C CG1 . VAL A 1 132 ? 26.424 2.925 41.170 1.00 6.76 ? 212 VAL A CG1 1 ATOM 1042 C CG2 . VAL A 1 132 ? 24.390 2.218 42.154 1.00 7.22 ? 212 VAL A CG2 1 ATOM 1043 N N . THR A 1 133 ? 28.132 3.394 44.481 1.00 4.86 ? 213 THR A N 1 ATOM 1044 C CA . THR A 1 133 ? 29.454 3.965 44.782 1.00 3.51 ? 213 THR A CA 1 ATOM 1045 C C . THR A 1 133 ? 29.713 4.160 46.284 1.00 6.27 ? 213 THR A C 1 ATOM 1046 O O . THR A 1 133 ? 28.764 4.383 47.053 1.00 6.60 ? 213 THR A O 1 ATOM 1047 C CB . THR A 1 133 ? 29.538 5.292 44.087 1.00 2.18 ? 213 THR A CB 1 ATOM 1048 O OG1 . THR A 1 133 ? 29.400 5.032 42.715 1.00 5.95 ? 213 THR A OG1 1 ATOM 1049 C CG2 . THR A 1 133 ? 30.851 5.957 44.308 1.00 2.30 ? 213 THR A CG2 1 ATOM 1050 N N . GLU A 1 134 ? 30.981 4.069 46.715 1.00 6.52 ? 214 GLU A N 1 ATOM 1051 C CA . GLU A 1 134 ? 31.407 4.214 48.124 1.00 11.21 ? 214 GLU A CA 1 ATOM 1052 C C . GLU A 1 134 ? 32.665 5.120 48.112 1.00 11.28 ? 214 GLU A C 1 ATOM 1053 O O . GLU A 1 134 ? 33.449 5.137 47.160 1.00 8.54 ? 214 GLU A O 1 ATOM 1054 C CB . GLU A 1 134 ? 31.812 2.872 48.792 1.00 11.68 ? 214 GLU A CB 1 ATOM 1055 C CG . GLU A 1 134 ? 30.939 1.613 48.692 1.00 13.76 ? 214 GLU A CG 1 ATOM 1056 C CD . GLU A 1 134 ? 30.803 1.056 47.270 1.00 16.31 ? 214 GLU A CD 1 ATOM 1057 O OE1 . GLU A 1 134 ? 31.773 0.665 46.636 1.00 15.78 ? 214 GLU A OE1 1 ATOM 1058 O OE2 . GLU A 1 134 ? 29.702 1.083 46.747 1.00 16.89 ? 214 GLU A OE2 1 ATOM 1059 N N . ILE A 1 135 ? 32.844 5.891 49.170 1.00 12.99 ? 215 ILE A N 1 ATOM 1060 C CA . ILE A 1 135 ? 33.903 6.893 49.263 1.00 14.29 ? 215 ILE A CA 1 ATOM 1061 C C . ILE A 1 135 ? 34.410 6.755 50.704 1.00 15.63 ? 215 ILE A C 1 ATOM 1062 O O . ILE A 1 135 ? 33.618 6.667 51.651 1.00 16.66 ? 215 ILE A O 1 ATOM 1063 C CB . ILE A 1 135 ? 33.311 8.328 48.992 1.00 14.77 ? 215 ILE A CB 1 ATOM 1064 C CG1 . ILE A 1 135 ? 32.612 8.424 47.610 1.00 13.61 ? 215 ILE A CG1 1 ATOM 1065 C CG2 . ILE A 1 135 ? 34.490 9.339 49.101 1.00 13.67 ? 215 ILE A CG2 1 ATOM 1066 C CD1 . ILE A 1 135 ? 31.917 9.772 47.202 1.00 12.67 ? 215 ILE A CD1 1 ATOM 1067 N N . ASN A 1 136 ? 35.714 6.641 50.921 1.00 16.18 ? 216 ASN A N 1 ATOM 1068 C CA . ASN A 1 136 ? 36.256 6.543 52.263 1.00 14.79 ? 216 ASN A CA 1 ATOM 1069 C C . ASN A 1 136 ? 36.741 7.937 52.668 1.00 14.13 ? 216 ASN A C 1 ATOM 1070 O O . ASN A 1 136 ? 36.878 8.853 51.851 1.00 14.70 ? 216 ASN A O 1 ATOM 1071 C CB . ASN A 1 136 ? 37.412 5.497 52.292 1.00 13.60 ? 216 ASN A CB 1 ATOM 1072 C CG . ASN A 1 136 ? 37.701 4.980 53.705 1.00 13.85 ? 216 ASN A CG 1 ATOM 1073 O OD1 . ASN A 1 136 ? 38.820 5.063 54.201 1.00 12.08 ? 216 ASN A OD1 1 ATOM 1074 N ND2 . ASN A 1 136 ? 36.732 4.420 54.443 1.00 12.78 ? 216 ASN A ND2 1 ATOM 1075 N N . THR A 1 137 ? 36.869 8.118 53.965 1.00 11.95 ? 217 THR A N 1 ATOM 1076 C CA . THR A 1 137 ? 37.301 9.345 54.579 1.00 12.24 ? 217 THR A CA 1 ATOM 1077 C C . THR A 1 137 ? 38.686 9.716 54.048 1.00 13.39 ? 217 THR A C 1 ATOM 1078 O O . THR A 1 137 ? 39.525 8.819 53.789 1.00 15.87 ? 217 THR A O 1 ATOM 1079 C CB . THR A 1 137 ? 37.201 9.048 56.118 1.00 10.77 ? 217 THR A CB 1 ATOM 1080 O OG1 . THR A 1 137 ? 37.479 10.251 56.818 1.00 10.88 ? 217 THR A OG1 1 ATOM 1081 C CG2 . THR A 1 137 ? 38.121 7.945 56.580 1.00 6.06 ? 217 THR A CG2 1 ATOM 1082 N N . TRP A 1 138 ? 38.801 11.023 53.732 1.00 13.98 ? 218 TRP A N 1 ATOM 1083 C CA . TRP A 1 138 ? 40.066 11.622 53.278 1.00 11.12 ? 218 TRP A CA 1 ATOM 1084 C C . TRP A 1 138 ? 40.836 12.385 54.335 1.00 8.93 ? 218 TRP A C 1 ATOM 1085 O O . TRP A 1 138 ? 42.045 12.439 54.227 1.00 9.27 ? 218 TRP A O 1 ATOM 1086 C CB . TRP A 1 138 ? 39.910 12.609 52.109 1.00 10.75 ? 218 TRP A CB 1 ATOM 1087 C CG . TRP A 1 138 ? 38.759 13.625 52.131 1.00 10.85 ? 218 TRP A CG 1 ATOM 1088 C CD1 . TRP A 1 138 ? 38.962 14.953 52.474 1.00 10.11 ? 218 TRP A CD1 1 ATOM 1089 C CD2 . TRP A 1 138 ? 37.456 13.378 51.750 1.00 9.43 ? 218 TRP A CD2 1 ATOM 1090 N NE1 . TRP A 1 138 ? 37.797 15.567 52.286 1.00 9.90 ? 218 TRP A NE1 1 ATOM 1091 C CE2 . TRP A 1 138 ? 36.886 14.669 51.856 1.00 10.55 ? 218 TRP A CE2 1 ATOM 1092 C CE3 . TRP A 1 138 ? 36.680 12.330 51.310 1.00 7.76 ? 218 TRP A CE3 1 ATOM 1093 C CZ2 . TRP A 1 138 ? 35.563 14.946 51.552 1.00 10.37 ? 218 TRP A CZ2 1 ATOM 1094 C CZ3 . TRP A 1 138 ? 35.346 12.613 50.998 1.00 9.42 ? 218 TRP A CZ3 1 ATOM 1095 C CH2 . TRP A 1 138 ? 34.798 13.886 51.120 1.00 10.34 ? 218 TRP A CH2 1 ATOM 1096 N N . ALA A 1 139 ? 40.250 13.019 55.338 1.00 9.36 ? 219 ALA A N 1 ATOM 1097 C CA . ALA A 1 139 ? 40.995 13.667 56.385 1.00 11.13 ? 219 ALA A CA 1 ATOM 1098 C C . ALA A 1 139 ? 40.797 12.997 57.741 1.00 14.11 ? 219 ALA A C 1 ATOM 1099 O O . ALA A 1 139 ? 41.279 13.491 58.749 1.00 16.95 ? 219 ALA A O 1 ATOM 1100 C CB . ALA A 1 139 ? 40.599 15.108 56.532 1.00 9.92 ? 219 ALA A CB 1 ATOM 1101 N N . ARG A 1 140 ? 40.047 11.897 57.834 1.00 16.19 ? 220 ARG A N 1 ATOM 1102 C CA . ARG A 1 140 ? 39.885 11.102 59.034 1.00 15.57 ? 220 ARG A CA 1 ATOM 1103 C C . ARG A 1 140 ? 39.333 11.695 60.326 1.00 15.98 ? 220 ARG A C 1 ATOM 1104 O O . ARG A 1 140 ? 39.654 11.258 61.438 1.00 14.27 ? 220 ARG A O 1 ATOM 1105 C CB . ARG A 1 140 ? 41.229 10.427 59.295 1.00 17.86 ? 220 ARG A CB 1 ATOM 1106 C CG . ARG A 1 140 ? 41.553 9.504 58.176 1.00 20.29 ? 220 ARG A CG 1 ATOM 1107 C CD . ARG A 1 140 ? 42.770 8.727 58.582 1.00 24.68 ? 220 ARG A CD 1 ATOM 1108 N NE . ARG A 1 140 ? 42.552 7.371 58.107 1.00 28.02 ? 220 ARG A NE 1 ATOM 1109 C CZ . ARG A 1 140 ? 42.085 6.364 58.874 1.00 28.61 ? 220 ARG A CZ 1 ATOM 1110 N NH1 . ARG A 1 140 ? 41.897 6.413 60.224 1.00 28.05 ? 220 ARG A NH1 1 ATOM 1111 N NH2 . ARG A 1 140 ? 41.850 5.246 58.204 1.00 30.48 ? 220 ARG A NH2 1 ATOM 1112 N N . ASN A 1 141 ? 38.370 12.622 60.178 1.00 16.60 ? 221 ASN A N 1 ATOM 1113 C CA . ASN A 1 141 ? 37.690 13.245 61.324 1.00 16.88 ? 221 ASN A CA 1 ATOM 1114 C C . ASN A 1 141 ? 36.297 13.717 60.894 1.00 16.24 ? 221 ASN A C 1 ATOM 1115 O O . ASN A 1 141 ? 36.128 14.720 60.206 1.00 16.69 ? 221 ASN A O 1 ATOM 1116 C CB . ASN A 1 141 ? 38.544 14.427 61.830 1.00 17.99 ? 221 ASN A CB 1 ATOM 1117 C CG . ASN A 1 141 ? 38.013 15.093 63.084 1.00 18.67 ? 221 ASN A CG 1 ATOM 1118 O OD1 . ASN A 1 141 ? 37.815 16.294 63.094 1.00 21.85 ? 221 ASN A OD1 1 ATOM 1119 N ND2 . ASN A 1 141 ? 37.838 14.448 64.227 1.00 20.90 ? 221 ASN A ND2 1 ATOM 1120 N N . ILE A 1 142 ? 35.325 12.855 61.211 1.00 14.91 ? 222 ILE A N 1 ATOM 1121 C CA . ILE A 1 142 ? 33.880 12.907 60.924 1.00 12.02 ? 222 ILE A CA 1 ATOM 1122 C C . ILE A 1 142 ? 33.509 13.458 59.522 1.00 13.40 ? 222 ILE A C 1 ATOM 1123 O O . ILE A 1 142 ? 33.225 14.658 59.324 1.00 12.63 ? 222 ILE A O 1 ATOM 1124 C CB . ILE A 1 142 ? 33.181 13.687 62.064 1.00 10.83 ? 222 ILE A CB 1 ATOM 1125 C CG1 . ILE A 1 142 ? 33.526 13.120 63.427 1.00 11.57 ? 222 ILE A CG1 1 ATOM 1126 C CG2 . ILE A 1 142 ? 31.677 13.485 61.986 1.00 10.00 ? 222 ILE A CG2 1 ATOM 1127 C CD1 . ILE A 1 142 ? 33.042 14.006 64.561 1.00 11.39 ? 222 ILE A CD1 1 ATOM 1128 N N . LEU A 1 143 ? 33.515 12.513 58.537 1.00 12.28 ? 223 LEU A N 1 ATOM 1129 C CA . LEU A 1 143 ? 33.171 12.805 57.153 1.00 11.86 ? 223 LEU A CA 1 ATOM 1130 C C . LEU A 1 143 ? 31.675 13.183 57.227 1.00 13.55 ? 223 LEU A C 1 ATOM 1131 O O . LEU A 1 143 ? 30.866 12.384 57.752 1.00 13.77 ? 223 LEU A O 1 ATOM 1132 C CB . LEU A 1 143 ? 33.436 11.540 56.268 1.00 9.60 ? 223 LEU A CB 1 ATOM 1133 C CG . LEU A 1 143 ? 33.019 11.416 54.755 1.00 8.30 ? 223 LEU A CG 1 ATOM 1134 C CD1 . LEU A 1 143 ? 33.592 12.566 53.980 1.00 2.08 ? 223 LEU A CD1 1 ATOM 1135 C CD2 . LEU A 1 143 ? 33.578 10.148 54.090 1.00 8.41 ? 223 LEU A CD2 1 ATOM 1136 N N . ARG A 1 144 ? 31.282 14.414 56.862 1.00 12.50 ? 224 ARG A N 1 ATOM 1137 C CA . ARG A 1 144 ? 29.854 14.737 56.885 1.00 12.42 ? 224 ARG A CA 1 ATOM 1138 C C . ARG A 1 144 ? 29.300 15.406 55.627 1.00 11.26 ? 224 ARG A C 1 ATOM 1139 O O . ARG A 1 144 ? 30.079 15.824 54.775 1.00 9.40 ? 224 ARG A O 1 ATOM 1140 C CB . ARG A 1 144 ? 29.472 15.665 58.032 1.00 12.64 ? 224 ARG A CB 1 ATOM 1141 C CG . ARG A 1 144 ? 30.506 16.069 59.063 1.00 14.25 ? 224 ARG A CG 1 ATOM 1142 C CD . ARG A 1 144 ? 31.331 17.175 58.504 1.00 13.28 ? 224 ARG A CD 1 ATOM 1143 N NE . ARG A 1 144 ? 31.805 18.099 59.537 1.00 12.98 ? 224 ARG A NE 1 ATOM 1144 C CZ . ARG A 1 144 ? 33.091 18.138 59.887 1.00 12.42 ? 224 ARG A CZ 1 ATOM 1145 N NH1 . ARG A 1 144 ? 33.966 17.229 59.464 1.00 14.00 ? 224 ARG A NH1 1 ATOM 1146 N NH2 . ARG A 1 144 ? 33.520 19.084 60.707 1.00 9.37 ? 224 ARG A NH2 1 ATOM 1147 N N . THR A 1 145 ? 27.958 15.445 55.426 1.00 10.37 ? 225 THR A N 1 ATOM 1148 C CA . THR A 1 145 ? 27.385 16.188 54.311 1.00 8.12 ? 225 THR A CA 1 ATOM 1149 C C . THR A 1 145 ? 26.210 17.125 54.666 1.00 8.88 ? 225 THR A C 1 ATOM 1150 O O . THR A 1 145 ? 26.061 17.556 55.820 1.00 10.35 ? 225 THR A O 1 ATOM 1151 C CB . THR A 1 145 ? 27.063 15.090 53.163 1.00 7.02 ? 225 THR A CB 1 ATOM 1152 O OG1 . THR A 1 145 ? 26.561 15.791 52.042 1.00 5.24 ? 225 THR A OG1 1 ATOM 1153 C CG2 . THR A 1 145 ? 26.055 14.052 53.523 1.00 2.62 ? 225 THR A CG2 1 ATOM 1154 N N . GLN A 1 146 ? 25.341 17.463 53.717 1.00 8.82 ? 226 GLN A N 1 ATOM 1155 C CA . GLN A 1 146 ? 24.400 18.569 53.801 1.00 8.01 ? 226 GLN A CA 1 ATOM 1156 C C . GLN A 1 146 ? 23.352 18.463 54.886 1.00 9.47 ? 226 GLN A C 1 ATOM 1157 O O . GLN A 1 146 ? 23.181 19.446 55.597 1.00 9.53 ? 226 GLN A O 1 ATOM 1158 C CB . GLN A 1 146 ? 23.699 18.758 52.412 1.00 6.42 ? 226 GLN A CB 1 ATOM 1159 C CG . GLN A 1 146 ? 24.700 18.920 51.257 1.00 3.30 ? 226 GLN A CG 1 ATOM 1160 C CD . GLN A 1 146 ? 24.183 19.370 49.884 1.00 4.39 ? 226 GLN A CD 1 ATOM 1161 O OE1 . GLN A 1 146 ? 24.979 19.552 48.962 1.00 3.71 ? 226 GLN A OE1 1 ATOM 1162 N NE2 . GLN A 1 146 ? 22.907 19.564 49.655 1.00 4.91 ? 226 GLN A NE2 1 ATOM 1163 N N . GLU A 1 147 ? 22.746 17.282 55.077 1.00 9.06 ? 227 GLU A N 1 ATOM 1164 C CA . GLU A 1 147 ? 21.583 16.994 55.919 1.00 9.17 ? 227 GLU A CA 1 ATOM 1165 C C . GLU A 1 147 ? 20.394 17.721 55.348 1.00 7.97 ? 227 GLU A C 1 ATOM 1166 O O . GLU A 1 147 ? 19.471 18.111 56.060 1.00 7.55 ? 227 GLU A O 1 ATOM 1167 C CB . GLU A 1 147 ? 21.620 17.451 57.396 1.00 10.47 ? 227 GLU A CB 1 ATOM 1168 C CG . GLU A 1 147 ? 22.887 17.281 58.201 1.00 11.75 ? 227 GLU A CG 1 ATOM 1169 C CD . GLU A 1 147 ? 23.505 15.913 58.301 1.00 12.02 ? 227 GLU A CD 1 ATOM 1170 O OE1 . GLU A 1 147 ? 22.912 14.924 57.907 1.00 16.01 ? 227 GLU A OE1 1 ATOM 1171 O OE2 . GLU A 1 147 ? 24.620 15.833 58.790 1.00 13.52 ? 227 GLU A OE2 1 ATOM 1172 N N . SER A 1 148 ? 20.382 17.968 54.047 1.00 5.60 ? 228 SER A N 1 ATOM 1173 C CA . SER A 1 148 ? 19.157 18.404 53.397 1.00 4.63 ? 228 SER A CA 1 ATOM 1174 C C . SER A 1 148 ? 19.259 18.007 51.944 1.00 5.01 ? 228 SER A C 1 ATOM 1175 O O . SER A 1 148 ? 20.309 17.423 51.576 1.00 4.88 ? 228 SER A O 1 ATOM 1176 C CB . SER A 1 148 ? 18.915 19.925 53.504 1.00 5.83 ? 228 SER A CB 1 ATOM 1177 O OG . SER A 1 148 ? 19.561 20.787 52.562 1.00 10.22 ? 228 SER A OG 1 ATOM 1178 N N . GLU A 1 149 ? 18.275 18.301 51.093 1.00 3.14 ? 229 GLU A N 1 ATOM 1179 C CA . GLU A 1 149 ? 18.338 17.746 49.765 1.00 5.35 ? 229 GLU A CA 1 ATOM 1180 C C . GLU A 1 149 ? 19.390 18.349 48.849 1.00 3.37 ? 229 GLU A C 1 ATOM 1181 O O . GLU A 1 149 ? 19.890 19.459 49.015 1.00 5.75 ? 229 GLU A O 1 ATOM 1182 C CB . GLU A 1 149 ? 16.963 17.833 49.093 1.00 9.09 ? 229 GLU A CB 1 ATOM 1183 C CG . GLU A 1 149 ? 16.625 19.080 48.250 1.00 10.08 ? 229 GLU A CG 1 ATOM 1184 C CD . GLU A 1 149 ? 15.308 19.078 47.484 1.00 11.85 ? 229 GLU A CD 1 ATOM 1185 O OE1 . GLU A 1 149 ? 14.629 18.062 47.449 1.00 11.06 ? 229 GLU A OE1 1 ATOM 1186 O OE2 . GLU A 1 149 ? 14.961 20.114 46.911 1.00 15.43 ? 229 GLU A OE2 1 ATOM 1187 N N . CYS A 1 150 ? 19.836 17.535 47.923 1.00 5.16 ? 230 CYS A N 1 ATOM 1188 C CA . CYS A 1 150 ? 20.732 18.021 46.881 1.00 6.09 ? 230 CYS A CA 1 ATOM 1189 C C . CYS A 1 150 ? 19.926 18.472 45.652 1.00 8.23 ? 230 CYS A C 1 ATOM 1190 O O . CYS A 1 150 ? 18.675 18.421 45.676 1.00 8.28 ? 230 CYS A O 1 ATOM 1191 C CB . CYS A 1 150 ? 21.736 16.879 46.522 1.00 7.89 ? 230 CYS A CB 1 ATOM 1192 S SG . CYS A 1 150 ? 21.090 15.204 46.373 1.00 11.21 ? 230 CYS A SG 1 ATOM 1193 N N . VAL A 1 151 ? 20.502 18.952 44.530 1.00 8.78 ? 231 VAL A N 1 ATOM 1194 C CA . VAL A 1 151 ? 19.714 19.386 43.354 1.00 5.92 ? 231 VAL A CA 1 ATOM 1195 C C . VAL A 1 151 ? 20.445 18.912 42.072 1.00 8.33 ? 231 VAL A C 1 ATOM 1196 O O . VAL A 1 151 ? 21.691 18.910 41.972 1.00 6.70 ? 231 VAL A O 1 ATOM 1197 C CB . VAL A 1 151 ? 19.540 20.958 43.312 1.00 6.89 ? 231 VAL A CB 1 ATOM 1198 C CG1 . VAL A 1 151 ? 18.525 21.330 42.235 1.00 6.25 ? 231 VAL A CG1 1 ATOM 1199 C CG2 . VAL A 1 151 ? 18.980 21.504 44.597 1.00 4.66 ? 231 VAL A CG2 1 ATOM 1200 N N . CYS A 1 152 ? 19.645 18.477 41.080 1.00 5.87 ? 232 CYS A N 1 ATOM 1201 C CA . CYS A 1 152 ? 20.217 17.987 39.843 1.00 8.31 ? 232 CYS A CA 1 ATOM 1202 C C . CYS A 1 152 ? 19.842 18.781 38.620 1.00 7.99 ? 232 CYS A C 1 ATOM 1203 O O . CYS A 1 152 ? 18.775 19.380 38.572 1.00 7.93 ? 232 CYS A O 1 ATOM 1204 C CB . CYS A 1 152 ? 19.798 16.547 39.574 1.00 9.34 ? 232 CYS A CB 1 ATOM 1205 S SG . CYS A 1 152 ? 19.904 15.537 41.043 1.00 9.03 ? 232 CYS A SG 1 ATOM 1206 N N . HIS A 1 153 ? 20.692 18.821 37.601 1.00 9.75 ? 233 HIS A N 1 ATOM 1207 C CA . HIS A 1 153 ? 20.324 19.440 36.304 1.00 12.07 ? 233 HIS A CA 1 ATOM 1208 C C . HIS A 1 153 ? 20.812 18.521 35.182 1.00 12.42 ? 233 HIS A C 1 ATOM 1209 O O . HIS A 1 153 ? 21.997 18.203 35.162 1.00 14.48 ? 233 HIS A O 1 ATOM 1210 C CB . HIS A 1 153 ? 21.014 20.788 36.208 1.00 9.85 ? 233 HIS A CB 1 ATOM 1211 C CG . HIS A 1 153 ? 20.905 21.429 34.861 1.00 9.70 ? 233 HIS A CG 1 ATOM 1212 N ND1 . HIS A 1 153 ? 21.810 21.421 33.892 1.00 10.00 ? 233 HIS A ND1 1 ATOM 1213 C CD2 . HIS A 1 153 ? 19.859 22.236 34.524 1.00 9.59 ? 233 HIS A CD2 1 ATOM 1214 C CE1 . HIS A 1 153 ? 21.331 22.195 32.953 1.00 8.16 ? 233 HIS A CE1 1 ATOM 1215 N NE2 . HIS A 1 153 ? 20.166 22.684 33.346 1.00 10.65 ? 233 HIS A NE2 1 ATOM 1216 N N . ASN A 1 154 ? 19.947 18.016 34.322 1.00 11.62 ? 234 ASN A N 1 ATOM 1217 C CA . ASN A 1 154 ? 20.277 17.062 33.280 1.00 13.78 ? 234 ASN A CA 1 ATOM 1218 C C . ASN A 1 154 ? 21.228 15.923 33.665 1.00 13.87 ? 234 ASN A C 1 ATOM 1219 O O . ASN A 1 154 ? 22.196 15.566 32.979 1.00 15.96 ? 234 ASN A O 1 ATOM 1220 C CB . ASN A 1 154 ? 20.852 17.789 32.067 1.00 12.54 ? 234 ASN A CB 1 ATOM 1221 C CG . ASN A 1 154 ? 20.978 16.888 30.848 1.00 12.60 ? 234 ASN A CG 1 ATOM 1222 O OD1 . ASN A 1 154 ? 20.132 16.049 30.509 1.00 12.33 ? 234 ASN A OD1 1 ATOM 1223 N ND2 . ASN A 1 154 ? 22.104 17.028 30.168 1.00 13.46 ? 234 ASN A ND2 1 ATOM 1224 N N . GLY A 1 155 ? 20.974 15.323 34.814 1.00 15.07 ? 235 GLY A N 1 ATOM 1225 C CA . GLY A 1 155 ? 21.697 14.140 35.222 1.00 13.85 ? 235 GLY A CA 1 ATOM 1226 C C . GLY A 1 155 ? 22.735 14.317 36.279 1.00 13.92 ? 235 GLY A C 1 ATOM 1227 O O . GLY A 1 155 ? 22.909 13.370 37.036 1.00 15.00 ? 235 GLY A O 1 ATOM 1228 N N . VAL A 1 156 ? 23.391 15.468 36.330 1.00 11.57 ? 236 VAL A N 1 ATOM 1229 C CA . VAL A 1 156 ? 24.493 15.738 37.238 1.00 8.57 ? 236 VAL A CA 1 ATOM 1230 C C . VAL A 1 156 ? 23.908 16.360 38.470 1.00 6.32 ? 236 VAL A C 1 ATOM 1231 O O . VAL A 1 156 ? 23.289 17.417 38.319 1.00 5.04 ? 236 VAL A O 1 ATOM 1232 C CB . VAL A 1 156 ? 25.523 16.750 36.601 1.00 9.73 ? 236 VAL A CB 1 ATOM 1233 C CG1 . VAL A 1 156 ? 26.734 17.074 37.458 1.00 8.26 ? 236 VAL A CG1 1 ATOM 1234 C CG2 . VAL A 1 156 ? 25.969 16.105 35.306 1.00 8.19 ? 236 VAL A CG2 1 ATOM 1235 N N . CYS A 1 157 ? 24.106 15.716 39.624 1.00 7.21 ? 237 CYS A N 1 ATOM 1236 C CA . CYS A 1 157 ? 23.705 16.164 40.949 1.00 8.36 ? 237 CYS A CA 1 ATOM 1237 C C . CYS A 1 157 ? 24.909 16.459 41.870 1.00 9.70 ? 237 CYS A C 1 ATOM 1238 O O . CYS A 1 157 ? 25.508 15.508 42.384 1.00 8.14 ? 237 CYS A O 1 ATOM 1239 C CB . CYS A 1 157 ? 22.866 15.090 41.608 1.00 9.36 ? 237 CYS A CB 1 ATOM 1240 S SG . CYS A 1 157 ? 21.479 14.362 40.735 1.00 12.05 ? 237 CYS A SG 1 ATOM 1241 N N . PRO A 1 158 ? 25.378 17.709 42.089 1.00 11.62 ? 238 PRO A N 1 ATOM 1242 C CA . PRO A 1 158 ? 26.507 18.086 42.963 1.00 12.32 ? 238 PRO A CA 1 ATOM 1243 C C . PRO A 1 158 ? 26.239 17.963 44.483 1.00 11.99 ? 238 PRO A C 1 ATOM 1244 O O . PRO A 1 158 ? 25.155 18.351 44.938 1.00 12.85 ? 238 PRO A O 1 ATOM 1245 C CB . PRO A 1 158 ? 26.823 19.513 42.584 1.00 11.54 ? 238 PRO A CB 1 ATOM 1246 C CG . PRO A 1 158 ? 26.017 19.761 41.347 1.00 11.57 ? 238 PRO A CG 1 ATOM 1247 C CD . PRO A 1 158 ? 24.767 18.911 41.552 1.00 10.14 ? 238 PRO A CD 1 ATOM 1248 N N . VAL A 1 159 ? 27.131 17.448 45.317 1.00 9.72 ? 239 VAL A N 1 ATOM 1249 C CA . VAL A 1 159 ? 26.925 17.302 46.749 1.00 6.96 ? 239 VAL A CA 1 ATOM 1250 C C . VAL A 1 159 ? 28.188 17.883 47.395 1.00 7.30 ? 239 VAL A C 1 ATOM 1251 O O . VAL A 1 159 ? 29.306 17.605 46.947 1.00 8.61 ? 239 VAL A O 1 ATOM 1252 C CB . VAL A 1 159 ? 26.772 15.771 47.179 1.00 6.00 ? 239 VAL A CB 1 ATOM 1253 C CG1 . VAL A 1 159 ? 26.476 15.639 48.681 1.00 2.12 ? 239 VAL A CG1 1 ATOM 1254 C CG2 . VAL A 1 159 ? 25.647 15.126 46.409 1.00 3.49 ? 239 VAL A CG2 1 ATOM 1255 N N . VAL A 1 160 ? 28.069 18.613 48.504 1.00 7.38 ? 240 VAL A N 1 ATOM 1256 C CA . VAL A 1 160 ? 29.194 19.154 49.209 1.00 5.89 ? 240 VAL A CA 1 ATOM 1257 C C . VAL A 1 160 ? 29.404 18.223 50.386 1.00 6.28 ? 240 VAL A C 1 ATOM 1258 O O . VAL A 1 160 ? 28.420 17.803 51.014 1.00 5.44 ? 240 VAL A O 1 ATOM 1259 C CB . VAL A 1 160 ? 28.814 20.572 49.676 1.00 7.28 ? 240 VAL A CB 1 ATOM 1260 C CG1 . VAL A 1 160 ? 30.060 21.187 50.277 1.00 6.99 ? 240 VAL A CG1 1 ATOM 1261 C CG2 . VAL A 1 160 ? 28.234 21.412 48.504 1.00 6.50 ? 240 VAL A CG2 1 ATOM 1262 N N . PHE A 1 161 ? 30.651 17.965 50.804 1.00 5.93 ? 241 PHE A N 1 ATOM 1263 C CA . PHE A 1 161 ? 31.022 17.072 51.870 1.00 8.14 ? 241 PHE A CA 1 ATOM 1264 C C . PHE A 1 161 ? 32.146 17.827 52.582 1.00 7.67 ? 241 PHE A C 1 ATOM 1265 O O . PHE A 1 161 ? 32.932 18.500 51.901 1.00 6.84 ? 241 PHE A O 1 ATOM 1266 C CB . PHE A 1 161 ? 31.654 15.757 51.394 1.00 6.96 ? 241 PHE A CB 1 ATOM 1267 C CG . PHE A 1 161 ? 30.772 14.715 50.752 1.00 6.25 ? 241 PHE A CG 1 ATOM 1268 C CD1 . PHE A 1 161 ? 30.078 13.836 51.546 1.00 6.37 ? 241 PHE A CD1 1 ATOM 1269 C CD2 . PHE A 1 161 ? 30.691 14.629 49.373 1.00 6.11 ? 241 PHE A CD2 1 ATOM 1270 C CE1 . PHE A 1 161 ? 29.301 12.875 50.937 1.00 7.01 ? 241 PHE A CE1 1 ATOM 1271 C CE2 . PHE A 1 161 ? 29.907 13.666 48.774 1.00 6.57 ? 241 PHE A CE2 1 ATOM 1272 C CZ . PHE A 1 161 ? 29.192 12.802 49.560 1.00 6.62 ? 241 PHE A CZ 1 ATOM 1273 N N . THR A 1 162 ? 32.179 17.795 53.906 1.00 6.55 ? 242 THR A N 1 ATOM 1274 C CA . THR A 1 162 ? 33.354 18.302 54.621 1.00 9.61 ? 242 THR A CA 1 ATOM 1275 C C . THR A 1 162 ? 34.054 17.153 55.367 1.00 10.07 ? 242 THR A C 1 ATOM 1276 O O . THR A 1 162 ? 33.391 16.193 55.750 1.00 13.23 ? 242 THR A O 1 ATOM 1277 C CB . THR A 1 162 ? 32.845 19.406 55.563 1.00 9.12 ? 242 THR A CB 1 ATOM 1278 O OG1 . THR A 1 162 ? 32.412 20.450 54.697 1.00 9.91 ? 242 THR A OG1 1 ATOM 1279 C CG2 . THR A 1 162 ? 33.867 19.995 56.515 1.00 10.48 ? 242 THR A CG2 1 ATOM 1280 N N . ASP A 1 163 ? 35.374 17.107 55.534 1.00 13.64 ? 243 ASP A N 1 ATOM 1281 C CA . ASP A 1 163 ? 35.974 16.077 56.371 1.00 15.05 ? 243 ASP A CA 1 ATOM 1282 C C . ASP A 1 163 ? 37.090 16.832 57.089 1.00 17.58 ? 243 ASP A C 1 ATOM 1283 O O . ASP A 1 163 ? 37.870 17.567 56.454 1.00 17.36 ? 243 ASP A O 1 ATOM 1284 C CB . ASP A 1 163 ? 36.579 14.937 55.554 1.00 12.84 ? 243 ASP A CB 1 ATOM 1285 C CG . ASP A 1 163 ? 36.962 13.693 56.361 1.00 12.21 ? 243 ASP A CG 1 ATOM 1286 O OD1 . ASP A 1 163 ? 37.197 13.747 57.557 1.00 11.79 ? 243 ASP A OD1 1 ATOM 1287 O OD2 . ASP A 1 163 ? 37.046 12.634 55.766 1.00 9.99 ? 243 ASP A OD2 1 ATOM 1288 N N . GLY A 1 164 ? 37.105 16.679 58.414 1.00 18.05 ? 244 GLY A N 1 ATOM 1289 C CA . GLY A 1 164 ? 38.094 17.332 59.256 1.00 18.90 ? 244 GLY A CA 1 ATOM 1290 C C . GLY A 1 164 ? 37.538 18.173 60.410 1.00 19.23 ? 244 GLY A C 1 ATOM 1291 O O . GLY A 1 164 ? 36.374 18.100 60.775 1.00 18.71 ? 244 GLY A O 1 ATOM 1292 N N . SER A 1 165 ? 38.385 18.976 61.031 1.00 19.85 ? 245 SER A N 1 ATOM 1293 C CA . SER A 1 165 ? 38.004 19.866 62.102 1.00 21.09 ? 245 SER A CA 1 ATOM 1294 C C . SER A 1 165 ? 36.827 20.781 61.844 1.00 22.21 ? 245 SER A C 1 ATOM 1295 O O . SER A 1 165 ? 36.713 21.560 60.902 1.00 24.49 ? 245 SER A O 1 ATOM 1296 C CB . SER A 1 165 ? 39.210 20.740 62.491 1.00 23.70 ? 245 SER A CB 1 ATOM 1297 O OG . SER A 1 165 ? 39.038 21.623 63.616 1.00 26.37 ? 245 SER A OG 1 ATOM 1298 N N . ALA A 1 166 ? 35.987 20.733 62.859 1.00 24.48 ? 246 ALA A N 1 ATOM 1299 C CA . ALA A 1 166 ? 34.830 21.613 62.978 1.00 24.64 ? 246 ALA A CA 1 ATOM 1300 C C . ALA A 1 166 ? 35.256 22.909 63.651 1.00 25.14 ? 246 ALA A C 1 ATOM 1301 O O . ALA A 1 166 ? 34.452 23.791 63.956 1.00 25.50 ? 246 ALA A O 1 ATOM 1302 C CB . ALA A 1 166 ? 33.782 21.010 63.871 1.00 24.45 ? 246 ALA A CB 1 ATOM 1303 N N . THR A 1 167 ? 36.532 23.075 63.969 1.00 24.86 ? 247 THR A N 1 ATOM 1304 C CA . THR A 1 167 ? 36.908 24.188 64.797 1.00 25.40 ? 247 THR A CA 1 ATOM 1305 C C . THR A 1 167 ? 38.140 24.924 64.325 1.00 26.16 ? 247 THR A C 1 ATOM 1306 O O . THR A 1 167 ? 38.671 25.832 64.973 1.00 27.51 ? 247 THR A O 1 ATOM 1307 C CB . THR A 1 167 ? 36.904 23.441 66.167 1.00 24.39 ? 247 THR A CB 1 ATOM 1308 O OG1 . THR A 1 167 ? 35.639 23.903 66.677 1.00 25.16 ? 247 THR A OG1 1 ATOM 1309 C CG2 . THR A 1 167 ? 38.090 23.574 67.086 1.00 23.72 ? 247 THR A CG2 1 ATOM 1310 N N . GLY A 1 168 ? 38.471 24.624 63.085 1.00 26.09 ? 248 GLY A N 1 ATOM 1311 C CA . GLY A 1 168 ? 39.682 25.126 62.478 1.00 26.49 ? 248 GLY A CA 1 ATOM 1312 C C . GLY A 1 168 ? 39.472 25.002 60.994 1.00 27.09 ? 248 GLY A C 1 ATOM 1313 O O . GLY A 1 168 ? 38.324 24.814 60.594 1.00 28.14 ? 248 GLY A O 1 ATOM 1314 N N . PRO A 1 169 ? 40.472 25.131 60.121 1.00 28.02 ? 249 PRO A N 1 ATOM 1315 C CA . PRO A 1 169 ? 40.423 24.641 58.749 1.00 26.92 ? 249 PRO A CA 1 ATOM 1316 C C . PRO A 1 169 ? 40.041 23.170 58.623 1.00 26.55 ? 249 PRO A C 1 ATOM 1317 O O . PRO A 1 169 ? 40.486 22.287 59.386 1.00 27.55 ? 249 PRO A O 1 ATOM 1318 C CB . PRO A 1 169 ? 41.786 24.921 58.224 1.00 27.79 ? 249 PRO A CB 1 ATOM 1319 C CG . PRO A 1 169 ? 42.116 26.199 58.933 1.00 26.46 ? 249 PRO A CG 1 ATOM 1320 C CD . PRO A 1 169 ? 41.681 25.896 60.345 1.00 27.44 ? 249 PRO A CD 1 ATOM 1321 N N . ALA A 1 170 ? 39.235 22.905 57.598 1.00 25.03 ? 250 ALA A N 1 ATOM 1322 C CA . ALA A 1 170 ? 38.786 21.547 57.309 1.00 22.33 ? 250 ALA A CA 1 ATOM 1323 C C . ALA A 1 170 ? 39.011 21.237 55.850 1.00 20.05 ? 250 ALA A C 1 ATOM 1324 O O . ALA A 1 170 ? 39.390 22.115 55.081 1.00 19.04 ? 250 ALA A O 1 ATOM 1325 C CB . ALA A 1 170 ? 37.296 21.391 57.579 1.00 22.05 ? 250 ALA A CB 1 ATOM 1326 N N . GLU A 1 171 ? 38.778 20.033 55.374 1.00 16.56 ? 251 GLU A N 1 ATOM 1327 C CA . GLU A 1 171 ? 38.811 19.806 53.940 1.00 14.82 ? 251 GLU A CA 1 ATOM 1328 C C . GLU A 1 171 ? 37.463 19.515 53.319 1.00 13.78 ? 251 GLU A C 1 ATOM 1329 O O . GLU A 1 171 ? 36.925 18.433 53.543 1.00 11.27 ? 251 GLU A O 1 ATOM 1330 C CB . GLU A 1 171 ? 39.744 18.677 53.668 1.00 16.12 ? 251 GLU A CB 1 ATOM 1331 C CG . GLU A 1 171 ? 41.182 18.933 54.090 1.00 19.00 ? 251 GLU A CG 1 ATOM 1332 C CD . GLU A 1 171 ? 42.092 17.710 53.971 1.00 25.01 ? 251 GLU A CD 1 ATOM 1333 O OE1 . GLU A 1 171 ? 41.935 16.916 53.010 1.00 26.89 ? 251 GLU A OE1 1 ATOM 1334 O OE2 . GLU A 1 171 ? 42.970 17.570 54.849 1.00 28.52 ? 251 GLU A OE2 1 ATOM 1335 N N . THR A 1 172 ? 36.931 20.474 52.562 1.00 14.16 ? 252 THR A N 1 ATOM 1336 C CA . THR A 1 172 ? 35.663 20.418 51.812 1.00 15.71 ? 252 THR A CA 1 ATOM 1337 C C . THR A 1 172 ? 35.823 20.182 50.293 1.00 16.29 ? 252 THR A C 1 ATOM 1338 O O . THR A 1 172 ? 36.653 20.854 49.656 1.00 18.56 ? 252 THR A O 1 ATOM 1339 C CB . THR A 1 172 ? 34.920 21.781 52.060 1.00 16.33 ? 252 THR A CB 1 ATOM 1340 O OG1 . THR A 1 172 ? 34.721 21.866 53.472 1.00 16.12 ? 252 THR A OG1 1 ATOM 1341 C CG2 . THR A 1 172 ? 33.620 21.935 51.300 1.00 13.97 ? 252 THR A CG2 1 ATOM 1342 N N . ARG A 1 173 ? 34.994 19.330 49.671 1.00 13.96 ? 253 ARG A N 1 ATOM 1343 C CA . ARG A 1 173 ? 35.039 18.987 48.242 1.00 11.37 ? 253 ARG A CA 1 ATOM 1344 C C . ARG A 1 173 ? 33.633 19.042 47.664 1.00 11.29 ? 253 ARG A C 1 ATOM 1345 O O . ARG A 1 173 ? 32.683 18.747 48.405 1.00 10.56 ? 253 ARG A O 1 ATOM 1346 C CB . ARG A 1 173 ? 35.532 17.552 47.997 1.00 12.59 ? 253 ARG A CB 1 ATOM 1347 C CG . ARG A 1 173 ? 36.944 17.196 48.442 1.00 8.73 ? 253 ARG A CG 1 ATOM 1348 C CD . ARG A 1 173 ? 37.214 15.671 48.427 1.00 6.30 ? 253 ARG A CD 1 ATOM 1349 N NE . ARG A 1 173 ? 38.620 15.373 48.766 1.00 5.79 ? 253 ARG A NE 1 ATOM 1350 C CZ . ARG A 1 173 ? 39.154 14.146 48.624 1.00 2.43 ? 253 ARG A CZ 1 ATOM 1351 N NH1 . ARG A 1 173 ? 38.438 13.068 48.304 1.00 2.89 ? 253 ARG A NH1 1 ATOM 1352 N NH2 . ARG A 1 173 ? 40.432 13.989 48.850 1.00 5.50 ? 253 ARG A NH2 1 ATOM 1353 N N . ILE A 1 174 ? 33.436 19.425 46.395 1.00 12.33 ? 254 ILE A N 1 ATOM 1354 C CA . ILE A 1 174 ? 32.089 19.315 45.777 1.00 12.48 ? 254 ILE A CA 1 ATOM 1355 C C . ILE A 1 174 ? 32.207 18.098 44.838 1.00 14.00 ? 254 ILE A C 1 ATOM 1356 O O . ILE A 1 174 ? 33.128 18.146 43.977 1.00 11.85 ? 254 ILE A O 1 ATOM 1357 C CB . ILE A 1 174 ? 31.703 20.603 44.933 1.00 13.41 ? 254 ILE A CB 1 ATOM 1358 C CG1 . ILE A 1 174 ? 31.234 21.762 45.812 1.00 13.42 ? 254 ILE A CG1 1 ATOM 1359 C CG2 . ILE A 1 174 ? 30.447 20.335 44.054 1.00 13.62 ? 254 ILE A CG2 1 ATOM 1360 C CD1 . ILE A 1 174 ? 32.286 22.412 46.717 1.00 14.56 ? 254 ILE A CD1 1 ATOM 1361 N N . TYR A 1 175 ? 31.405 16.982 45.040 1.00 12.99 ? 255 TYR A N 1 ATOM 1362 C CA . TYR A 1 175 ? 31.409 15.821 44.140 1.00 9.19 ? 255 TYR A CA 1 ATOM 1363 C C . TYR A 1 175 ? 30.312 15.987 43.107 1.00 8.57 ? 255 TYR A C 1 ATOM 1364 O O . TYR A 1 175 ? 29.203 16.380 43.464 1.00 5.61 ? 255 TYR A O 1 ATOM 1365 C CB . TYR A 1 175 ? 31.154 14.519 44.900 1.00 10.04 ? 255 TYR A CB 1 ATOM 1366 C CG . TYR A 1 175 ? 32.412 13.869 45.452 1.00 11.50 ? 255 TYR A CG 1 ATOM 1367 C CD1 . TYR A 1 175 ? 32.954 14.357 46.635 1.00 12.27 ? 255 TYR A CD1 1 ATOM 1368 C CD2 . TYR A 1 175 ? 33.010 12.806 44.770 1.00 11.90 ? 255 TYR A CD2 1 ATOM 1369 C CE1 . TYR A 1 175 ? 34.099 13.810 47.148 1.00 12.33 ? 255 TYR A CE1 1 ATOM 1370 C CE2 . TYR A 1 175 ? 34.165 12.263 45.292 1.00 12.37 ? 255 TYR A CE2 1 ATOM 1371 C CZ . TYR A 1 175 ? 34.697 12.785 46.467 1.00 12.56 ? 255 TYR A CZ 1 ATOM 1372 O OH . TYR A 1 175 ? 35.874 12.318 47.023 1.00 13.04 ? 255 TYR A OH 1 ATOM 1373 N N . TYR A 1 176 ? 30.519 15.711 41.824 1.00 9.54 ? 256 TYR A N 1 ATOM 1374 C CA . TYR A 1 176 ? 29.462 15.831 40.813 1.00 9.14 ? 256 TYR A CA 1 ATOM 1375 C C . TYR A 1 176 ? 29.101 14.393 40.458 1.00 10.54 ? 256 TYR A C 1 ATOM 1376 O O . TYR A 1 176 ? 29.967 13.656 39.986 1.00 11.12 ? 256 TYR A O 1 ATOM 1377 C CB . TYR A 1 176 ? 30.006 16.591 39.587 1.00 8.44 ? 256 TYR A CB 1 ATOM 1378 C CG . TYR A 1 176 ? 30.419 18.044 39.900 1.00 6.17 ? 256 TYR A CG 1 ATOM 1379 C CD1 . TYR A 1 176 ? 31.695 18.400 40.339 1.00 6.29 ? 256 TYR A CD1 1 ATOM 1380 C CD2 . TYR A 1 176 ? 29.457 19.033 39.768 1.00 6.19 ? 256 TYR A CD2 1 ATOM 1381 C CE1 . TYR A 1 176 ? 31.994 19.739 40.627 1.00 6.64 ? 256 TYR A CE1 1 ATOM 1382 C CE2 . TYR A 1 176 ? 29.728 20.366 40.051 1.00 5.01 ? 256 TYR A CE2 1 ATOM 1383 C CZ . TYR A 1 176 ? 31.004 20.708 40.465 1.00 7.09 ? 256 TYR A CZ 1 ATOM 1384 O OH . TYR A 1 176 ? 31.275 22.026 40.724 1.00 4.24 ? 256 TYR A OH 1 ATOM 1385 N N . PHE A 1 177 ? 27.879 13.914 40.685 1.00 10.24 ? 257 PHE A N 1 ATOM 1386 C CA . PHE A 1 177 ? 27.513 12.536 40.377 1.00 9.51 ? 257 PHE A CA 1 ATOM 1387 C C . PHE A 1 177 ? 26.563 12.485 39.198 1.00 9.66 ? 257 PHE A C 1 ATOM 1388 O O . PHE A 1 177 ? 25.783 13.421 39.005 1.00 6.67 ? 257 PHE A O 1 ATOM 1389 C CB . PHE A 1 177 ? 26.777 11.885 41.531 1.00 7.81 ? 257 PHE A CB 1 ATOM 1390 C CG . PHE A 1 177 ? 27.553 11.753 42.825 1.00 8.27 ? 257 PHE A CG 1 ATOM 1391 C CD1 . PHE A 1 177 ? 28.349 10.636 43.010 1.00 6.96 ? 257 PHE A CD1 1 ATOM 1392 C CD2 . PHE A 1 177 ? 27.442 12.736 43.816 1.00 7.08 ? 257 PHE A CD2 1 ATOM 1393 C CE1 . PHE A 1 177 ? 29.023 10.530 44.208 1.00 7.21 ? 257 PHE A CE1 1 ATOM 1394 C CE2 . PHE A 1 177 ? 28.131 12.603 45.012 1.00 7.98 ? 257 PHE A CE2 1 ATOM 1395 C CZ . PHE A 1 177 ? 28.922 11.481 45.211 1.00 7.72 ? 257 PHE A CZ 1 ATOM 1396 N N . LYS A 1 178 ? 26.601 11.394 38.443 1.00 9.52 ? 258 LYS A N 1 ATOM 1397 C CA . LYS A 1 178 ? 25.570 11.177 37.435 1.00 14.18 ? 258 LYS A CA 1 ATOM 1398 C C . LYS A 1 178 ? 25.262 9.684 37.375 1.00 16.34 ? 258 LYS A C 1 ATOM 1399 O O . LYS A 1 178 ? 26.144 8.848 37.206 1.00 16.57 ? 258 LYS A O 1 ATOM 1400 C CB . LYS A 1 178 ? 25.989 11.672 36.058 1.00 17.03 ? 258 LYS A CB 1 ATOM 1401 C CG . LYS A 1 178 ? 24.779 11.557 35.103 1.00 18.66 ? 258 LYS A CG 1 ATOM 1402 C CD . LYS A 1 178 ? 25.134 12.223 33.789 1.00 22.48 ? 258 LYS A CD 1 ATOM 1403 C CE . LYS A 1 178 ? 24.000 12.070 32.809 1.00 23.39 ? 258 LYS A CE 1 ATOM 1404 N NZ . LYS A 1 178 ? 24.122 13.163 31.876 1.00 28.78 ? 258 LYS A NZ 1 ATOM 1405 N N . GLU A 1 179 ? 23.970 9.381 37.643 1.00 16.78 ? 259 GLU A N 1 ATOM 1406 C CA . GLU A 1 179 ? 23.442 8.051 37.931 1.00 18.08 ? 259 GLU A CA 1 ATOM 1407 C C . GLU A 1 179 ? 24.220 7.314 39.035 1.00 17.01 ? 259 GLU A C 1 ATOM 1408 O O . GLU A 1 179 ? 24.464 6.112 38.936 1.00 16.59 ? 259 GLU A O 1 ATOM 1409 C CB . GLU A 1 179 ? 23.433 7.186 36.694 1.00 20.61 ? 259 GLU A CB 1 ATOM 1410 C CG . GLU A 1 179 ? 22.451 7.627 35.619 1.00 25.75 ? 259 GLU A CG 1 ATOM 1411 C CD . GLU A 1 179 ? 22.741 6.968 34.266 1.00 27.46 ? 259 GLU A CD 1 ATOM 1412 O OE1 . GLU A 1 179 ? 23.394 5.923 34.182 1.00 29.27 ? 259 GLU A OE1 1 ATOM 1413 O OE2 . GLU A 1 179 ? 22.301 7.509 33.255 1.00 28.78 ? 259 GLU A OE2 1 ATOM 1414 N N . GLY A 1 180 ? 24.596 7.973 40.125 1.00 13.66 ? 260 GLY A N 1 ATOM 1415 C CA . GLY A 1 180 ? 25.304 7.304 41.197 1.00 11.93 ? 260 GLY A CA 1 ATOM 1416 C C . GLY A 1 180 ? 26.807 7.223 41.004 1.00 12.17 ? 260 GLY A C 1 ATOM 1417 O O . GLY A 1 180 ? 27.480 6.913 41.981 1.00 11.50 ? 260 GLY A O 1 ATOM 1418 N N . LYS A 1 181 ? 27.411 7.517 39.842 1.00 13.07 ? 261 LYS A N 1 ATOM 1419 C CA . LYS A 1 181 ? 28.844 7.357 39.572 1.00 11.38 ? 261 LYS A CA 1 ATOM 1420 C C . LYS A 1 181 ? 29.498 8.747 39.667 1.00 9.47 ? 261 LYS A C 1 ATOM 1421 O O . LYS A 1 181 ? 28.838 9.765 39.390 1.00 9.18 ? 261 LYS A O 1 ATOM 1422 C CB . LYS A 1 181 ? 28.999 6.760 38.173 0.02 11.78 ? 261 LYS A CB 1 ATOM 1423 C CG . LYS A 1 181 ? 30.428 6.767 37.651 0.02 11.63 ? 261 LYS A CG 1 ATOM 1424 C CD . LYS A 1 181 ? 30.434 6.327 36.209 0.02 11.51 ? 261 LYS A CD 1 ATOM 1425 C CE . LYS A 1 181 ? 31.811 6.419 35.584 0.02 11.47 ? 261 LYS A CE 1 ATOM 1426 N NZ . LYS A 1 181 ? 31.698 5.924 34.227 0.02 11.62 ? 261 LYS A NZ 1 ATOM 1427 N N . ILE A 1 182 ? 30.771 8.869 40.064 1.00 8.97 ? 262 ILE A N 1 ATOM 1428 C CA . ILE A 1 182 ? 31.430 10.164 40.260 1.00 7.81 ? 262 ILE A CA 1 ATOM 1429 C C . ILE A 1 182 ? 31.877 10.625 38.892 1.00 8.94 ? 262 ILE A C 1 ATOM 1430 O O . ILE A 1 182 ? 32.412 9.819 38.144 1.00 11.56 ? 262 ILE A O 1 ATOM 1431 C CB . ILE A 1 182 ? 32.653 10.010 41.149 1.00 6.63 ? 262 ILE A CB 1 ATOM 1432 C CG1 . ILE A 1 182 ? 32.180 9.510 42.496 1.00 8.31 ? 262 ILE A CG1 1 ATOM 1433 C CG2 . ILE A 1 182 ? 33.426 11.314 41.230 1.00 4.31 ? 262 ILE A CG2 1 ATOM 1434 C CD1 . ILE A 1 182 ? 33.331 9.101 43.400 1.00 9.26 ? 262 ILE A CD1 1 ATOM 1435 N N . LEU A 1 183 ? 31.699 11.876 38.542 1.00 8.82 ? 263 LEU A N 1 ATOM 1436 C CA . LEU A 1 183 ? 32.118 12.339 37.253 1.00 7.18 ? 263 LEU A CA 1 ATOM 1437 C C . LEU A 1 183 ? 33.386 13.129 37.421 1.00 9.45 ? 263 LEU A C 1 ATOM 1438 O O . LEU A 1 183 ? 34.247 13.150 36.526 1.00 12.48 ? 263 LEU A O 1 ATOM 1439 C CB . LEU A 1 183 ? 31.107 13.241 36.680 1.00 7.10 ? 263 LEU A CB 1 ATOM 1440 C CG . LEU A 1 183 ? 29.826 12.716 36.206 1.00 6.83 ? 263 LEU A CG 1 ATOM 1441 C CD1 . LEU A 1 183 ? 28.810 13.857 36.057 1.00 6.00 ? 263 LEU A CD1 1 ATOM 1442 C CD2 . LEU A 1 183 ? 30.102 12.010 34.889 1.00 7.91 ? 263 LEU A CD2 1 ATOM 1443 N N . LYS A 1 184 ? 33.479 13.781 38.604 1.00 10.38 ? 264 LYS A N 1 ATOM 1444 C CA . LYS A 1 184 ? 34.521 14.730 38.954 1.00 8.78 ? 264 LYS A CA 1 ATOM 1445 C C . LYS A 1 184 ? 34.403 15.206 40.413 1.00 6.93 ? 264 LYS A C 1 ATOM 1446 O O . LYS A 1 184 ? 33.294 15.118 40.948 1.00 6.26 ? 264 LYS A O 1 ATOM 1447 C CB . LYS A 1 184 ? 34.373 15.881 37.987 1.00 8.07 ? 264 LYS A CB 1 ATOM 1448 C CG . LYS A 1 184 ? 35.329 17.026 38.220 1.00 9.06 ? 264 LYS A CG 1 ATOM 1449 C CD . LYS A 1 184 ? 34.844 18.183 37.431 1.00 9.97 ? 264 LYS A CD 1 ATOM 1450 C CE . LYS A 1 184 ? 35.677 19.405 37.575 1.00 13.07 ? 264 LYS A CE 1 ATOM 1451 N NZ . LYS A 1 184 ? 35.178 20.298 36.537 1.00 17.80 ? 264 LYS A NZ 1 ATOM 1452 N N . TRP A 1 185 ? 35.462 15.643 41.095 1.00 3.90 ? 265 TRP A N 1 ATOM 1453 C CA . TRP A 1 185 ? 35.303 16.315 42.367 1.00 7.52 ? 265 TRP A CA 1 ATOM 1454 C C . TRP A 1 185 ? 36.371 17.418 42.401 1.00 8.24 ? 265 TRP A C 1 ATOM 1455 O O . TRP A 1 185 ? 37.391 17.332 41.700 1.00 9.45 ? 265 TRP A O 1 ATOM 1456 C CB . TRP A 1 185 ? 35.505 15.389 43.614 1.00 7.89 ? 265 TRP A CB 1 ATOM 1457 C CG . TRP A 1 185 ? 36.852 14.739 43.910 1.00 8.51 ? 265 TRP A CG 1 ATOM 1458 C CD1 . TRP A 1 185 ? 37.069 13.420 43.569 1.00 9.74 ? 265 TRP A CD1 1 ATOM 1459 C CD2 . TRP A 1 185 ? 37.943 15.307 44.523 1.00 7.65 ? 265 TRP A CD2 1 ATOM 1460 N NE1 . TRP A 1 185 ? 38.314 13.165 43.958 1.00 8.82 ? 265 TRP A NE1 1 ATOM 1461 C CE2 . TRP A 1 185 ? 38.843 14.255 44.514 1.00 9.16 ? 265 TRP A CE2 1 ATOM 1462 C CE3 . TRP A 1 185 ? 38.363 16.480 45.068 1.00 9.38 ? 265 TRP A CE3 1 ATOM 1463 C CZ2 . TRP A 1 185 ? 40.116 14.328 45.008 1.00 9.41 ? 265 TRP A CZ2 1 ATOM 1464 C CZ3 . TRP A 1 185 ? 39.649 16.561 45.573 1.00 9.28 ? 265 TRP A CZ3 1 ATOM 1465 C CH2 . TRP A 1 185 ? 40.521 15.507 45.546 1.00 9.22 ? 265 TRP A CH2 1 ATOM 1466 N N . GLU A 1 186 ? 36.128 18.438 43.219 1.00 8.93 ? 266 GLU A N 1 ATOM 1467 C CA . GLU A 1 186 ? 36.991 19.577 43.317 1.00 6.11 ? 266 GLU A CA 1 ATOM 1468 C C . GLU A 1 186 ? 37.065 19.937 44.787 1.00 5.11 ? 266 GLU A C 1 ATOM 1469 O O . GLU A 1 186 ? 36.085 19.728 45.521 1.00 3.51 ? 266 GLU A O 1 ATOM 1470 C CB . GLU A 1 186 ? 36.432 20.801 42.636 1.00 10.45 ? 266 GLU A CB 1 ATOM 1471 C CG . GLU A 1 186 ? 35.806 20.858 41.253 1.00 12.06 ? 266 GLU A CG 1 ATOM 1472 C CD . GLU A 1 186 ? 35.298 22.273 41.015 1.00 14.80 ? 266 GLU A CD 1 ATOM 1473 O OE1 . GLU A 1 186 ? 36.149 23.115 40.707 1.00 18.22 ? 266 GLU A OE1 1 ATOM 1474 O OE2 . GLU A 1 186 ? 34.085 22.521 41.135 1.00 14.99 ? 266 GLU A OE2 1 ATOM 1475 N N . PRO A 1 187 ? 38.152 20.520 45.274 1.00 5.76 ? 267 PRO A N 1 ATOM 1476 C CA . PRO A 1 187 ? 38.187 21.092 46.594 1.00 6.13 ? 267 PRO A CA 1 ATOM 1477 C C . PRO A 1 187 ? 37.583 22.505 46.666 1.00 7.71 ? 267 PRO A C 1 ATOM 1478 O O . PRO A 1 187 ? 37.443 23.170 45.646 1.00 7.70 ? 267 PRO A O 1 ATOM 1479 C CB . PRO A 1 187 ? 39.655 20.970 46.920 1.00 7.36 ? 267 PRO A CB 1 ATOM 1480 C CG . PRO A 1 187 ? 40.394 21.132 45.627 1.00 5.56 ? 267 PRO A CG 1 ATOM 1481 C CD . PRO A 1 187 ? 39.451 20.597 44.585 1.00 7.73 ? 267 PRO A CD 1 ATOM 1482 N N . LEU A 1 188 ? 37.220 23.010 47.844 1.00 8.39 ? 268 LEU A N 1 ATOM 1483 C CA . LEU A 1 188 ? 36.564 24.297 47.944 1.00 11.87 ? 268 LEU A CA 1 ATOM 1484 C C . LEU A 1 188 ? 37.410 25.439 47.391 1.00 13.16 ? 268 LEU A C 1 ATOM 1485 O O . LEU A 1 188 ? 38.619 25.489 47.583 1.00 16.59 ? 268 LEU A O 1 ATOM 1486 C CB . LEU A 1 188 ? 36.212 24.632 49.400 1.00 11.01 ? 268 LEU A CB 1 ATOM 1487 C CG . LEU A 1 188 ? 34.896 25.298 49.895 1.00 11.29 ? 268 LEU A CG 1 ATOM 1488 C CD1 . LEU A 1 188 ? 35.288 26.223 51.010 1.00 11.45 ? 268 LEU A CD1 1 ATOM 1489 C CD2 . LEU A 1 188 ? 34.181 26.153 48.888 1.00 10.34 ? 268 LEU A CD2 1 ATOM 1490 N N . ALA A 1 189 ? 36.796 26.376 46.709 1.00 13.11 ? 269 ALA A N 1 ATOM 1491 C CA . ALA A 1 189 ? 37.495 27.532 46.217 1.00 13.72 ? 269 ALA A CA 1 ATOM 1492 C C . ALA A 1 189 ? 36.762 28.819 46.597 1.00 14.78 ? 269 ALA A C 1 ATOM 1493 O O . ALA A 1 189 ? 35.615 28.750 47.020 1.00 16.74 ? 269 ALA A O 1 ATOM 1494 C CB . ALA A 1 189 ? 37.584 27.472 44.716 1.00 14.98 ? 269 ALA A CB 1 ATOM 1495 N N . GLY A 1 190 ? 37.369 29.995 46.420 1.00 14.16 ? 270 GLY A N 1 ATOM 1496 C CA . GLY A 1 190 ? 36.746 31.291 46.634 1.00 15.42 ? 270 GLY A CA 1 ATOM 1497 C C . GLY A 1 190 ? 37.115 31.783 48.010 1.00 16.37 ? 270 GLY A C 1 ATOM 1498 O O . GLY A 1 190 ? 38.131 31.315 48.544 1.00 15.54 ? 270 GLY A O 1 ATOM 1499 N N . THR A 1 191 ? 36.301 32.665 48.619 1.00 16.08 ? 271 THR A N 1 ATOM 1500 C CA . THR A 1 191 ? 36.677 33.216 49.889 1.00 14.94 ? 271 THR A CA 1 ATOM 1501 C C . THR A 1 191 ? 36.051 32.628 51.122 1.00 17.72 ? 271 THR A C 1 ATOM 1502 O O . THR A 1 191 ? 36.351 33.175 52.179 1.00 21.38 ? 271 THR A O 1 ATOM 1503 C CB . THR A 1 191 ? 36.399 34.696 49.849 1.00 13.41 ? 271 THR A CB 1 ATOM 1504 O OG1 . THR A 1 191 ? 35.056 34.870 49.446 1.00 12.84 ? 271 THR A OG1 1 ATOM 1505 C CG2 . THR A 1 191 ? 37.291 35.409 48.894 1.00 12.11 ? 271 THR A CG2 1 ATOM 1506 N N . ALA A 1 192 ? 35.204 31.567 51.101 1.00 19.35 ? 272 ALA A N 1 ATOM 1507 C CA . ALA A 1 192 ? 34.549 31.059 52.321 1.00 19.25 ? 272 ALA A CA 1 ATOM 1508 C C . ALA A 1 192 ? 35.588 30.272 53.094 1.00 19.02 ? 272 ALA A C 1 ATOM 1509 O O . ALA A 1 192 ? 36.374 29.511 52.526 1.00 22.76 ? 272 ALA A O 1 ATOM 1510 C CB . ALA A 1 192 ? 33.411 30.110 52.017 1.00 17.19 ? 272 ALA A CB 1 ATOM 1511 N N . LYS A 1 193 ? 35.618 30.484 54.403 1.00 19.46 ? 273 LYS A N 1 ATOM 1512 C CA . LYS A 1 193 ? 36.661 29.909 55.252 1.00 17.96 ? 273 LYS A CA 1 ATOM 1513 C C . LYS A 1 193 ? 36.400 28.528 55.843 1.00 19.68 ? 273 LYS A C 1 ATOM 1514 O O . LYS A 1 193 ? 37.334 27.801 56.217 1.00 20.52 ? 273 LYS A O 1 ATOM 1515 C CB . LYS A 1 193 ? 36.961 30.842 56.417 0.02 18.91 ? 273 LYS A CB 1 ATOM 1516 C CG . LYS A 1 193 ? 37.929 31.938 56.034 0.02 18.88 ? 273 LYS A CG 1 ATOM 1517 C CD . LYS A 1 193 ? 38.362 32.686 57.276 0.02 19.23 ? 273 LYS A CD 1 ATOM 1518 C CE . LYS A 1 193 ? 39.357 33.744 56.834 0.02 19.56 ? 273 LYS A CE 1 ATOM 1519 N NZ . LYS A 1 193 ? 39.877 34.509 57.950 0.02 19.83 ? 273 LYS A NZ 1 ATOM 1520 N N . HIS A 1 194 ? 35.129 28.134 56.013 1.00 18.90 ? 274 HIS A N 1 ATOM 1521 C CA . HIS A 1 194 ? 34.753 26.888 56.672 1.00 18.26 ? 274 HIS A CA 1 ATOM 1522 C C . HIS A 1 194 ? 33.352 26.546 56.161 1.00 18.75 ? 274 HIS A C 1 ATOM 1523 O O . HIS A 1 194 ? 32.531 27.468 56.086 1.00 19.58 ? 274 HIS A O 1 ATOM 1524 C CB . HIS A 1 194 ? 34.752 27.129 58.188 1.00 16.90 ? 274 HIS A CB 1 ATOM 1525 C CG . HIS A 1 194 ? 34.439 25.879 58.958 1.00 16.79 ? 274 HIS A CG 1 ATOM 1526 N ND1 . HIS A 1 194 ? 33.262 25.339 59.283 1.00 15.83 ? 274 HIS A ND1 1 ATOM 1527 C CD2 . HIS A 1 194 ? 35.436 25.042 59.373 1.00 16.40 ? 274 HIS A CD2 1 ATOM 1528 C CE1 . HIS A 1 194 ? 33.513 24.201 59.889 1.00 14.81 ? 274 HIS A CE1 1 ATOM 1529 N NE2 . HIS A 1 194 ? 34.821 24.044 59.936 1.00 16.44 ? 274 HIS A NE2 1 ATOM 1530 N N . ILE A 1 195 ? 33.035 25.293 55.818 1.00 18.04 ? 275 ILE A N 1 ATOM 1531 C CA . ILE A 1 195 ? 31.734 24.876 55.265 1.00 15.79 ? 275 ILE A CA 1 ATOM 1532 C C . ILE A 1 195 ? 31.222 23.684 56.079 1.00 13.96 ? 275 ILE A C 1 ATOM 1533 O O . ILE A 1 195 ? 31.957 22.754 56.425 1.00 12.67 ? 275 ILE A O 1 ATOM 1534 C CB . ILE A 1 195 ? 31.844 24.436 53.772 1.00 15.50 ? 275 ILE A CB 1 ATOM 1535 C CG1 . ILE A 1 195 ? 32.148 25.631 52.899 1.00 17.00 ? 275 ILE A CG1 1 ATOM 1536 C CG2 . ILE A 1 195 ? 30.563 23.746 53.314 1.00 17.45 ? 275 ILE A CG2 1 ATOM 1537 C CD1 . ILE A 1 195 ? 31.147 26.830 52.804 1.00 17.72 ? 275 ILE A CD1 1 ATOM 1538 N N . GLU A 1 196 ? 29.922 23.657 56.282 1.00 12.26 ? 276 GLU A N 1 ATOM 1539 C CA . GLU A 1 196 ? 29.273 22.700 57.139 1.00 13.40 ? 276 GLU A CA 1 ATOM 1540 C C . GLU A 1 196 ? 27.831 22.758 56.657 1.00 13.51 ? 276 GLU A C 1 ATOM 1541 O O . GLU A 1 196 ? 27.404 23.845 56.279 1.00 12.13 ? 276 GLU A O 1 ATOM 1542 C CB . GLU A 1 196 ? 29.425 23.194 58.575 1.00 16.17 ? 276 GLU A CB 1 ATOM 1543 C CG . GLU A 1 196 ? 29.396 22.262 59.782 1.00 21.18 ? 276 GLU A CG 1 ATOM 1544 C CD . GLU A 1 196 ? 30.679 21.491 60.045 1.00 25.96 ? 276 GLU A CD 1 ATOM 1545 O OE1 . GLU A 1 196 ? 31.708 21.770 59.427 1.00 27.21 ? 276 GLU A OE1 1 ATOM 1546 O OE2 . GLU A 1 196 ? 30.637 20.598 60.900 1.00 29.99 ? 276 GLU A OE2 1 ATOM 1547 N N . GLU A 1 197 ? 27.085 21.663 56.545 1.00 12.94 ? 277 GLU A N 1 ATOM 1548 C CA . GLU A 1 197 ? 25.643 21.676 56.273 1.00 13.06 ? 277 GLU A CA 1 ATOM 1549 C C . GLU A 1 197 ? 25.005 22.604 55.207 1.00 12.76 ? 277 GLU A C 1 ATOM 1550 O O . GLU A 1 197 ? 24.163 23.430 55.562 1.00 14.12 ? 277 GLU A O 1 ATOM 1551 C CB . GLU A 1 197 ? 24.973 21.922 57.634 1.00 11.05 ? 277 GLU A CB 1 ATOM 1552 C CG . GLU A 1 197 ? 25.205 20.830 58.616 1.00 9.68 ? 277 GLU A CG 1 ATOM 1553 C CD . GLU A 1 197 ? 24.895 21.139 60.073 1.00 10.12 ? 277 GLU A CD 1 ATOM 1554 O OE1 . GLU A 1 197 ? 24.581 22.262 60.463 1.00 10.79 ? 277 GLU A OE1 1 ATOM 1555 O OE2 . GLU A 1 197 ? 24.976 20.208 60.865 1.00 11.27 ? 277 GLU A OE2 1 ATOM 1556 N N . CYS A 1 198 ? 25.327 22.583 53.911 1.00 11.19 ? 278 CYS A N 1 ATOM 1557 C CA . CYS A 1 198 ? 24.716 23.460 52.943 1.00 8.90 ? 278 CYS A CA 1 ATOM 1558 C C . CYS A 1 198 ? 23.295 23.106 52.589 1.00 8.24 ? 278 CYS A C 1 ATOM 1559 O O . CYS A 1 198 ? 22.904 21.946 52.491 1.00 7.99 ? 278 CYS A O 1 ATOM 1560 C CB . CYS A 1 198 ? 25.557 23.466 51.681 1.00 8.81 ? 278 CYS A CB 1 ATOM 1561 S SG . CYS A 1 198 ? 27.250 23.977 51.867 1.00 10.55 ? 278 CYS A SG 1 ATOM 1562 N N . SER A 1 199 ? 22.499 24.170 52.619 1.00 8.36 ? 279 SER A N 1 ATOM 1563 C CA . SER A 1 199 ? 21.142 24.130 52.091 1.00 9.67 ? 279 SER A CA 1 ATOM 1564 C C . SER A 1 199 ? 21.043 24.646 50.678 1.00 10.91 ? 279 SER A C 1 ATOM 1565 O O . SER A 1 199 ? 21.411 25.804 50.453 1.00 8.98 ? 279 SER A O 1 ATOM 1566 C CB . SER A 1 199 ? 20.265 24.968 52.982 1.00 9.28 ? 279 SER A CB 1 ATOM 1567 O OG . SER A 1 199 ? 20.098 24.427 54.311 1.00 7.23 ? 279 SER A OG 1 ATOM 1568 N N . CYS A 1 200 ? 20.638 23.823 49.682 1.00 13.28 ? 280 CYS A N 1 ATOM 1569 C CA . CYS A 1 200 ? 20.649 24.282 48.303 1.00 9.88 ? 280 CYS A CA 1 ATOM 1570 C C . CYS A 1 200 ? 19.318 24.386 47.563 1.00 9.66 ? 280 CYS A C 1 ATOM 1571 O O . CYS A 1 200 ? 18.322 23.781 48.011 1.00 8.06 ? 280 CYS A O 1 ATOM 1572 C CB . CYS A 1 200 ? 21.543 23.364 47.499 1.00 8.94 ? 280 CYS A CB 1 ATOM 1573 S SG . CYS A 1 200 ? 23.157 22.973 48.266 1.00 10.48 ? 280 CYS A SG 1 ATOM 1574 N N . TYR A 1 201 ? 19.277 25.170 46.454 1.00 11.94 ? 281 TYR A N 1 ATOM 1575 C CA . TYR A 1 201 ? 18.167 25.262 45.528 1.00 11.55 ? 281 TYR A CA 1 ATOM 1576 C C . TYR A 1 201 ? 18.817 25.553 44.185 1.00 12.73 ? 281 TYR A C 1 ATOM 1577 O O . TYR A 1 201 ? 20.009 25.893 44.104 1.00 13.54 ? 281 TYR A O 1 ATOM 1578 C CB . TYR A 1 201 ? 17.174 26.410 45.798 1.00 11.63 ? 281 TYR A CB 1 ATOM 1579 C CG . TYR A 1 201 ? 17.653 27.857 45.762 1.00 10.55 ? 281 TYR A CG 1 ATOM 1580 C CD1 . TYR A 1 201 ? 18.235 28.390 46.899 1.00 11.28 ? 281 TYR A CD1 1 ATOM 1581 C CD2 . TYR A 1 201 ? 17.497 28.644 44.627 1.00 10.90 ? 281 TYR A CD2 1 ATOM 1582 C CE1 . TYR A 1 201 ? 18.665 29.702 46.886 1.00 9.57 ? 281 TYR A CE1 1 ATOM 1583 C CE2 . TYR A 1 201 ? 17.924 29.943 44.600 1.00 9.84 ? 281 TYR A CE2 1 ATOM 1584 C CZ . TYR A 1 201 ? 18.522 30.434 45.736 1.00 10.33 ? 281 TYR A CZ 1 ATOM 1585 O OH . TYR A 1 201 ? 18.981 31.711 45.780 1.00 11.58 ? 281 TYR A OH 1 ATOM 1586 N N . GLY A 1 202 ? 18.024 25.393 43.124 1.00 14.42 ? 282 GLY A N 1 ATOM 1587 C CA . GLY A 1 202 ? 18.463 25.683 41.771 1.00 15.50 ? 282 GLY A CA 1 ATOM 1588 C C . GLY A 1 202 ? 17.387 26.415 40.954 1.00 16.69 ? 282 GLY A C 1 ATOM 1589 O O . GLY A 1 202 ? 16.172 26.271 41.179 1.00 16.05 ? 282 GLY A O 1 ATOM 1590 N N . GLU A 1 203 ? 17.819 27.288 40.026 1.00 17.21 ? 283 GLU A N 1 ATOM 1591 C CA . GLU A 1 203 ? 16.922 27.955 39.087 1.00 16.97 ? 283 GLU A CA 1 ATOM 1592 C C . GLU A 1 203 ? 17.844 28.407 37.968 1.00 16.18 ? 283 GLU A C 1 ATOM 1593 O O . GLU A 1 203 ? 19.049 28.530 38.188 1.00 15.36 ? 283 GLU A O 1 ATOM 1594 C CB . GLU A 1 203 ? 16.159 29.130 39.759 1.00 17.23 ? 283 GLU A CB 1 ATOM 1595 C CG . GLU A 1 203 ? 16.829 30.067 40.733 1.00 21.05 ? 283 GLU A CG 1 ATOM 1596 C CD . GLU A 1 203 ? 17.835 30.985 40.073 1.00 23.68 ? 283 GLU A CD 1 ATOM 1597 O OE1 . GLU A 1 203 ? 17.437 31.625 39.095 1.00 25.58 ? 283 GLU A OE1 1 ATOM 1598 O OE2 . GLU A 1 203 ? 19.001 31.045 40.520 1.00 24.68 ? 283 GLU A OE2 1 ATOM 1599 N N . ARG A 1 204 ? 17.302 28.546 36.754 1.00 15.81 ? 284 ARG A N 1 ATOM 1600 C CA . ARG A 1 204 ? 18.004 28.867 35.504 1.00 15.44 ? 284 ARG A CA 1 ATOM 1601 C C . ARG A 1 204 ? 19.463 28.376 35.418 1.00 15.30 ? 284 ARG A C 1 ATOM 1602 O O . ARG A 1 204 ? 20.443 29.111 35.294 1.00 17.96 ? 284 ARG A O 1 ATOM 1603 C CB . ARG A 1 204 ? 17.929 30.371 35.278 1.00 16.13 ? 284 ARG A CB 1 ATOM 1604 C CG . ARG A 1 204 ? 16.541 30.893 34.968 1.00 18.73 ? 284 ARG A CG 1 ATOM 1605 C CD . ARG A 1 204 ? 16.610 32.415 34.923 1.00 19.29 ? 284 ARG A CD 1 ATOM 1606 N NE . ARG A 1 204 ? 15.357 33.169 34.890 1.00 20.16 ? 284 ARG A NE 1 ATOM 1607 C CZ . ARG A 1 204 ? 14.425 33.003 33.956 1.00 22.92 ? 284 ARG A CZ 1 ATOM 1608 N NH1 . ARG A 1 204 ? 14.523 32.140 32.932 1.00 23.81 ? 284 ARG A NH1 1 ATOM 1609 N NH2 . ARG A 1 204 ? 13.327 33.736 34.076 1.00 24.10 ? 284 ARG A NH2 1 ATOM 1610 N N . ALA A 1 205 ? 19.535 27.056 35.513 1.00 13.28 ? 285 ALA A N 1 ATOM 1611 C CA . ALA A 1 205 ? 20.722 26.242 35.371 1.00 13.55 ? 285 ALA A CA 1 ATOM 1612 C C . ALA A 1 205 ? 21.941 26.546 36.228 1.00 14.88 ? 285 ALA A C 1 ATOM 1613 O O . ALA A 1 205 ? 23.072 26.231 35.851 1.00 17.17 ? 285 ALA A O 1 ATOM 1614 C CB . ALA A 1 205 ? 21.104 26.241 33.893 1.00 11.62 ? 285 ALA A CB 1 ATOM 1615 N N . GLU A 1 206 ? 21.716 27.026 37.440 1.00 15.38 ? 286 GLU A N 1 ATOM 1616 C CA . GLU A 1 206 ? 22.748 27.339 38.392 1.00 16.90 ? 286 GLU A CA 1 ATOM 1617 C C . GLU A 1 206 ? 22.208 26.850 39.757 1.00 14.09 ? 286 GLU A C 1 ATOM 1618 O O . GLU A 1 206 ? 20.978 26.836 39.977 1.00 12.19 ? 286 GLU A O 1 ATOM 1619 C CB . GLU A 1 206 ? 22.962 28.848 38.358 1.00 22.37 ? 286 GLU A CB 1 ATOM 1620 C CG . GLU A 1 206 ? 23.971 29.275 39.372 1.00 29.36 ? 286 GLU A CG 1 ATOM 1621 C CD . GLU A 1 206 ? 24.060 30.773 39.462 1.00 33.12 ? 286 GLU A CD 1 ATOM 1622 O OE1 . GLU A 1 206 ? 23.196 31.374 40.114 1.00 35.88 ? 286 GLU A OE1 1 ATOM 1623 O OE2 . GLU A 1 206 ? 25.005 31.312 38.882 1.00 36.20 ? 286 GLU A OE2 1 ATOM 1624 N N . ILE A 1 207 ? 23.074 26.448 40.692 1.00 10.24 ? 287 ILE A N 1 ATOM 1625 C CA . ILE A 1 207 ? 22.683 25.930 42.013 1.00 8.40 ? 287 ILE A CA 1 ATOM 1626 C C . ILE A 1 207 ? 23.353 26.811 43.098 1.00 6.61 ? 287 ILE A C 1 ATOM 1627 O O . ILE A 1 207 ? 24.564 27.036 43.085 1.00 6.31 ? 287 ILE A O 1 ATOM 1628 C CB . ILE A 1 207 ? 23.132 24.426 42.133 1.00 6.20 ? 287 ILE A CB 1 ATOM 1629 C CG1 . ILE A 1 207 ? 22.359 23.493 41.215 1.00 2.55 ? 287 ILE A CG1 1 ATOM 1630 C CG2 . ILE A 1 207 ? 22.951 23.987 43.573 1.00 6.16 ? 287 ILE A CG2 1 ATOM 1631 C CD1 . ILE A 1 207 ? 22.996 22.129 41.023 1.00 2.33 ? 287 ILE A CD1 1 ATOM 1632 N N . THR A 1 208 ? 22.589 27.248 44.084 1.00 6.37 ? 288 THR A N 1 ATOM 1633 C CA . THR A 1 208 ? 23.000 28.132 45.174 1.00 9.44 ? 288 THR A CA 1 ATOM 1634 C C . THR A 1 208 ? 22.795 27.395 46.480 1.00 9.24 ? 288 THR A C 1 ATOM 1635 O O . THR A 1 208 ? 21.685 26.915 46.740 1.00 12.94 ? 288 THR A O 1 ATOM 1636 C CB . THR A 1 208 ? 22.113 29.431 45.170 1.00 9.79 ? 288 THR A CB 1 ATOM 1637 O OG1 . THR A 1 208 ? 22.267 29.911 43.844 1.00 9.72 ? 288 THR A OG1 1 ATOM 1638 C CG2 . THR A 1 208 ? 22.492 30.566 46.113 1.00 11.03 ? 288 THR A CG2 1 ATOM 1639 N N . CYS A 1 209 ? 23.899 27.186 47.170 1.00 7.62 ? 289 CYS A N 1 ATOM 1640 C CA . CYS A 1 209 ? 23.874 26.709 48.553 1.00 9.14 ? 289 CYS A CA 1 ATOM 1641 C C . CYS A 1 209 ? 24.292 27.799 49.576 1.00 9.58 ? 289 CYS A C 1 ATOM 1642 O O . CYS A 1 209 ? 25.230 28.578 49.302 1.00 11.26 ? 289 CYS A O 1 ATOM 1643 C CB . CYS A 1 209 ? 24.812 25.512 48.660 1.00 8.23 ? 289 CYS A CB 1 ATOM 1644 S SG . CYS A 1 209 ? 24.536 24.125 47.479 1.00 10.24 ? 289 CYS A SG 1 ATOM 1645 N N . THR A 1 210 ? 23.667 27.814 50.771 1.00 8.29 ? 290 THR A N 1 ATOM 1646 C CA . THR A 1 210 ? 23.893 28.757 51.869 1.00 5.80 ? 290 THR A CA 1 ATOM 1647 C C . THR A 1 210 ? 24.255 27.743 52.933 1.00 5.66 ? 290 THR A C 1 ATOM 1648 O O . THR A 1 210 ? 23.417 26.891 53.256 1.00 8.11 ? 290 THR A O 1 ATOM 1649 C CB . THR A 1 210 ? 22.592 29.503 52.367 1.00 4.84 ? 290 THR A CB 1 ATOM 1650 O OG1 . THR A 1 210 ? 21.973 30.188 51.266 1.00 3.26 ? 290 THR A OG1 1 ATOM 1651 C CG2 . THR A 1 210 ? 22.889 30.429 53.504 1.00 2.66 ? 290 THR A CG2 1 ATOM 1652 N N . CYS A 1 211 ? 25.491 27.818 53.431 1.00 5.93 ? 291 CYS A N 1 ATOM 1653 C CA . CYS A 1 211 ? 26.046 26.878 54.374 1.00 5.16 ? 291 CYS A CA 1 ATOM 1654 C C . CYS A 1 211 ? 26.285 27.498 55.759 1.00 3.42 ? 291 CYS A C 1 ATOM 1655 O O . CYS A 1 211 ? 25.720 28.554 56.066 1.00 2.74 ? 291 CYS A O 1 ATOM 1656 C CB . CYS A 1 211 ? 27.312 26.361 53.745 1.00 4.88 ? 291 CYS A CB 1 ATOM 1657 S SG . CYS A 1 211 ? 27.156 26.089 52.030 1.00 4.08 ? 291 CYS A SG 1 ATOM 1658 N N . ARG A 1 212 ? 27.064 26.827 56.614 1.00 2.76 ? 292 ARG A N 1 ATOM 1659 C CA . ARG A 1 212 ? 27.273 27.276 57.963 1.00 4.01 ? 292 ARG A CA 1 ATOM 1660 C C . ARG A 1 212 ? 28.782 27.298 58.149 1.00 5.95 ? 292 ARG A C 1 ATOM 1661 O O . ARG A 1 212 ? 29.445 26.268 57.926 1.00 2.00 ? 292 ARG A O 1 ATOM 1662 C CB . ARG A 1 212 ? 26.620 26.257 58.911 1.00 4.36 ? 292 ARG A CB 1 ATOM 1663 C CG . ARG A 1 212 ? 27.127 26.318 60.380 1.00 5.82 ? 292 ARG A CG 1 ATOM 1664 C CD . ARG A 1 212 ? 26.777 25.004 60.990 1.00 6.58 ? 292 ARG A CD 1 ATOM 1665 N NE . ARG A 1 212 ? 27.362 24.815 62.297 1.00 7.53 ? 292 ARG A NE 1 ATOM 1666 C CZ . ARG A 1 212 ? 26.775 23.967 63.154 1.00 7.71 ? 292 ARG A CZ 1 ATOM 1667 N NH1 . ARG A 1 212 ? 25.639 23.356 62.815 1.00 10.21 ? 292 ARG A NH1 1 ATOM 1668 N NH2 . ARG A 1 212 ? 27.324 23.737 64.338 1.00 6.15 ? 292 ARG A NH2 1 ATOM 1669 N N . ASP A 1 213 ? 29.357 28.453 58.509 1.00 7.25 ? 293 ASP A N 1 ATOM 1670 C CA . ASP A 1 213 ? 30.779 28.448 58.813 1.00 9.74 ? 293 ASP A CA 1 ATOM 1671 C C . ASP A 1 213 ? 30.892 27.994 60.289 1.00 11.56 ? 293 ASP A C 1 ATOM 1672 O O . ASP A 1 213 ? 30.620 28.798 61.166 1.00 10.97 ? 293 ASP A O 1 ATOM 1673 C CB . ASP A 1 213 ? 31.303 29.883 58.574 1.00 11.76 ? 293 ASP A CB 1 ATOM 1674 C CG . ASP A 1 213 ? 32.763 30.148 58.944 1.00 13.36 ? 293 ASP A CG 1 ATOM 1675 O OD1 . ASP A 1 213 ? 33.168 29.824 60.041 1.00 15.60 ? 293 ASP A OD1 1 ATOM 1676 O OD2 . ASP A 1 213 ? 33.506 30.651 58.118 1.00 15.95 ? 293 ASP A OD2 1 ATOM 1677 N N . ASN A 1 214 ? 31.229 26.800 60.759 1.00 12.54 ? 294 ASN A N 1 ATOM 1678 C CA . ASN A 1 214 ? 31.304 26.594 62.193 1.00 13.73 ? 294 ASN A CA 1 ATOM 1679 C C . ASN A 1 214 ? 32.487 27.269 62.901 1.00 18.16 ? 294 ASN A C 1 ATOM 1680 O O . ASN A 1 214 ? 32.457 27.513 64.122 1.00 18.67 ? 294 ASN A O 1 ATOM 1681 C CB . ASN A 1 214 ? 31.335 25.108 62.437 1.00 12.67 ? 294 ASN A CB 1 ATOM 1682 C CG . ASN A 1 214 ? 30.928 24.797 63.858 1.00 13.55 ? 294 ASN A CG 1 ATOM 1683 O OD1 . ASN A 1 214 ? 31.659 24.336 64.724 1.00 16.61 ? 294 ASN A OD1 1 ATOM 1684 N ND2 . ASN A 1 214 ? 29.684 25.097 64.143 1.00 16.10 ? 294 ASN A ND2 1 ATOM 1685 N N . TRP A 1 215 ? 33.557 27.581 62.155 1.00 19.27 ? 295 TRP A N 1 ATOM 1686 C CA . TRP A 1 215 ? 34.759 28.138 62.745 1.00 21.05 ? 295 TRP A CA 1 ATOM 1687 C C . TRP A 1 215 ? 34.595 29.573 63.297 1.00 22.86 ? 295 TRP A C 1 ATOM 1688 O O . TRP A 1 215 ? 34.750 29.804 64.517 1.00 24.15 ? 295 TRP A O 1 ATOM 1689 C CB . TRP A 1 215 ? 35.840 28.013 61.662 1.00 20.74 ? 295 TRP A CB 1 ATOM 1690 C CG . TRP A 1 215 ? 37.264 28.399 62.047 1.00 20.63 ? 295 TRP A CG 1 ATOM 1691 C CD1 . TRP A 1 215 ? 37.630 28.624 63.343 1.00 20.95 ? 295 TRP A CD1 1 ATOM 1692 C CD2 . TRP A 1 215 ? 38.300 28.638 61.185 1.00 21.06 ? 295 TRP A CD2 1 ATOM 1693 N NE1 . TRP A 1 215 ? 38.873 29.026 63.301 1.00 20.69 ? 295 TRP A NE1 1 ATOM 1694 C CE2 . TRP A 1 215 ? 39.303 29.041 62.050 1.00 20.71 ? 295 TRP A CE2 1 ATOM 1695 C CE3 . TRP A 1 215 ? 38.519 28.575 59.825 1.00 22.95 ? 295 TRP A CE3 1 ATOM 1696 C CZ2 . TRP A 1 215 ? 40.543 29.391 61.598 1.00 21.97 ? 295 TRP A CZ2 1 ATOM 1697 C CZ3 . TRP A 1 215 ? 39.765 28.922 59.364 1.00 22.90 ? 295 TRP A CZ3 1 ATOM 1698 C CH2 . TRP A 1 215 ? 40.763 29.334 60.240 1.00 22.67 ? 295 TRP A CH2 1 ATOM 1699 N N . GLN A 1 216 ? 34.323 30.562 62.441 1.00 21.38 ? 296 GLN A N 1 ATOM 1700 C CA . GLN A 1 216 ? 34.227 31.929 62.887 1.00 22.71 ? 296 GLN A CA 1 ATOM 1701 C C . GLN A 1 216 ? 33.246 32.930 62.294 1.00 21.59 ? 296 GLN A C 1 ATOM 1702 O O . GLN A 1 216 ? 33.294 34.046 62.793 1.00 23.82 ? 296 GLN A O 1 ATOM 1703 C CB . GLN A 1 216 ? 35.641 32.520 62.822 1.00 25.55 ? 296 GLN A CB 1 ATOM 1704 C CG . GLN A 1 216 ? 36.473 32.460 61.549 1.00 30.06 ? 296 GLN A CG 1 ATOM 1705 C CD . GLN A 1 216 ? 37.949 32.791 61.803 1.00 32.10 ? 296 GLN A CD 1 ATOM 1706 O OE1 . GLN A 1 216 ? 38.455 32.813 62.923 1.00 34.62 ? 296 GLN A OE1 1 ATOM 1707 N NE2 . GLN A 1 216 ? 38.681 33.057 60.732 1.00 32.76 ? 296 GLN A NE2 1 ATOM 1708 N N . GLY A 1 217 ? 32.351 32.711 61.318 1.00 18.48 ? 297 GLY A N 1 ATOM 1709 C CA . GLY A 1 217 ? 31.514 33.814 60.874 1.00 17.99 ? 297 GLY A CA 1 ATOM 1710 C C . GLY A 1 217 ? 30.108 33.717 61.475 1.00 16.15 ? 297 GLY A C 1 ATOM 1711 O O . GLY A 1 217 ? 29.607 32.636 61.774 1.00 17.15 ? 297 GLY A O 1 ATOM 1712 N N . SER A 1 218 ? 29.440 34.833 61.704 1.00 15.64 ? 298 SER A N 1 ATOM 1713 C CA . SER A 1 218 ? 28.037 34.827 62.095 1.00 15.87 ? 298 SER A CA 1 ATOM 1714 C C . SER A 1 218 ? 27.111 35.223 60.928 1.00 15.22 ? 298 SER A C 1 ATOM 1715 O O . SER A 1 218 ? 25.880 35.103 60.933 1.00 12.89 ? 298 SER A O 1 ATOM 1716 C CB . SER A 1 218 ? 27.961 35.751 63.312 1.00 17.57 ? 298 SER A CB 1 ATOM 1717 O OG . SER A 1 218 ? 28.907 35.346 64.329 1.00 19.40 ? 298 SER A OG 1 ATOM 1718 N N . ASN A 1 219 ? 27.787 35.668 59.864 1.00 14.63 ? 299 ASN A N 1 ATOM 1719 C CA . ASN A 1 219 ? 27.189 35.874 58.544 1.00 15.96 ? 299 ASN A CA 1 ATOM 1720 C C . ASN A 1 219 ? 27.338 34.516 57.840 1.00 14.54 ? 299 ASN A C 1 ATOM 1721 O O . ASN A 1 219 ? 28.188 33.758 58.287 1.00 13.30 ? 299 ASN A O 1 ATOM 1722 C CB . ASN A 1 219 ? 27.951 36.955 57.748 1.00 17.51 ? 299 ASN A CB 1 ATOM 1723 C CG . ASN A 1 219 ? 29.471 36.814 57.697 1.00 18.45 ? 299 ASN A CG 1 ATOM 1724 O OD1 . ASN A 1 219 ? 30.093 36.128 58.527 1.00 18.99 ? 299 ASN A OD1 1 ATOM 1725 N ND2 . ASN A 1 219 ? 30.149 37.451 56.751 1.00 17.38 ? 299 ASN A ND2 1 ATOM 1726 N N . ARG A 1 220 ? 26.565 34.095 56.832 1.00 14.37 ? 300 ARG A N 1 ATOM 1727 C CA . ARG A 1 220 ? 26.724 32.783 56.169 1.00 13.55 ? 300 ARG A CA 1 ATOM 1728 C C . ARG A 1 220 ? 27.455 32.728 54.831 1.00 10.32 ? 300 ARG A C 1 ATOM 1729 O O . ARG A 1 220 ? 27.272 33.595 53.981 1.00 9.66 ? 300 ARG A O 1 ATOM 1730 C CB . ARG A 1 220 ? 25.357 32.116 55.913 1.00 13.99 ? 300 ARG A CB 1 ATOM 1731 C CG . ARG A 1 220 ? 24.691 31.648 57.201 1.00 12.63 ? 300 ARG A CG 1 ATOM 1732 C CD . ARG A 1 220 ? 23.387 30.953 56.936 1.00 11.30 ? 300 ARG A CD 1 ATOM 1733 N NE . ARG A 1 220 ? 22.719 30.751 58.212 1.00 11.10 ? 300 ARG A NE 1 ATOM 1734 C CZ . ARG A 1 220 ? 22.828 29.634 58.930 1.00 7.12 ? 300 ARG A CZ 1 ATOM 1735 N NH1 . ARG A 1 220 ? 23.647 28.686 58.549 1.00 7.14 ? 300 ARG A NH1 1 ATOM 1736 N NH2 . ARG A 1 220 ? 22.150 29.458 60.059 1.00 7.66 ? 300 ARG A NH2 1 ATOM 1737 N N . PRO A 1 221 ? 28.264 31.695 54.592 1.00 11.40 ? 301 PRO A N 1 ATOM 1738 C CA . PRO A 1 221 ? 28.885 31.423 53.293 1.00 11.40 ? 301 PRO A CA 1 ATOM 1739 C C . PRO A 1 221 ? 27.989 30.909 52.178 1.00 13.15 ? 301 PRO A C 1 ATOM 1740 O O . PRO A 1 221 ? 27.015 30.211 52.463 1.00 13.83 ? 301 PRO A O 1 ATOM 1741 C CB . PRO A 1 221 ? 29.990 30.449 53.626 1.00 11.89 ? 301 PRO A CB 1 ATOM 1742 C CG . PRO A 1 221 ? 29.537 29.737 54.861 1.00 9.22 ? 301 PRO A CG 1 ATOM 1743 C CD . PRO A 1 221 ? 28.755 30.792 55.620 1.00 10.24 ? 301 PRO A CD 1 ATOM 1744 N N . VAL A 1 222 ? 28.304 31.238 50.927 1.00 12.67 ? 302 VAL A N 1 ATOM 1745 C CA . VAL A 1 222 ? 27.465 30.861 49.809 1.00 14.18 ? 302 VAL A CA 1 ATOM 1746 C C . VAL A 1 222 ? 28.420 30.268 48.802 1.00 14.47 ? 302 VAL A C 1 ATOM 1747 O O . VAL A 1 222 ? 29.496 30.823 48.538 1.00 14.46 ? 302 VAL A O 1 ATOM 1748 C CB . VAL A 1 222 ? 26.732 32.073 49.148 1.00 15.96 ? 302 VAL A CB 1 ATOM 1749 C CG1 . VAL A 1 222 ? 25.884 31.609 47.955 1.00 17.55 ? 302 VAL A CG1 1 ATOM 1750 C CG2 . VAL A 1 222 ? 25.790 32.723 50.161 1.00 15.68 ? 302 VAL A CG2 1 ATOM 1751 N N . ILE A 1 223 ? 28.034 29.078 48.356 1.00 13.53 ? 303 ILE A N 1 ATOM 1752 C CA . ILE A 1 223 ? 28.714 28.393 47.290 1.00 12.95 ? 303 ILE A CA 1 ATOM 1753 C C . ILE A 1 223 ? 27.789 28.495 46.085 1.00 12.00 ? 303 ILE A C 1 ATOM 1754 O O . ILE A 1 223 ? 26.645 28.138 46.292 1.00 12.68 ? 303 ILE A O 1 ATOM 1755 C CB . ILE A 1 223 ? 28.977 26.935 47.684 1.00 11.76 ? 303 ILE A CB 1 ATOM 1756 C CG1 . ILE A 1 223 ? 29.862 26.900 48.918 1.00 12.27 ? 303 ILE A CG1 1 ATOM 1757 C CG2 . ILE A 1 223 ? 29.734 26.226 46.564 1.00 9.71 ? 303 ILE A CG2 1 ATOM 1758 C CD1 . ILE A 1 223 ? 30.100 25.519 49.484 1.00 13.88 ? 303 ILE A CD1 1 ATOM 1759 N N . ARG A 1 224 ? 28.162 29.000 44.891 1.00 12.42 ? 304 ARG A N 1 ATOM 1760 C CA . ARG A 1 224 ? 27.348 29.012 43.680 1.00 11.81 ? 304 ARG A CA 1 ATOM 1761 C C . ARG A 1 224 ? 27.997 27.950 42.771 1.00 13.96 ? 304 ARG A C 1 ATOM 1762 O O . ARG A 1 224 ? 29.234 27.970 42.591 1.00 14.54 ? 304 ARG A O 1 ATOM 1763 C CB . ARG A 1 224 ? 27.382 30.408 43.042 0.02 12.90 ? 304 ARG A CB 1 ATOM 1764 C CG . ARG A 1 224 ? 26.334 31.298 43.702 0.02 13.54 ? 304 ARG A CG 1 ATOM 1765 C CD . ARG A 1 224 ? 26.181 32.653 43.029 0.02 14.49 ? 304 ARG A CD 1 ATOM 1766 N NE . ARG A 1 224 ? 25.063 33.366 43.628 0.02 15.28 ? 304 ARG A NE 1 ATOM 1767 C CZ . ARG A 1 224 ? 24.080 33.907 42.905 0.02 15.73 ? 304 ARG A CZ 1 ATOM 1768 N NH1 . ARG A 1 224 ? 24.069 33.867 41.573 0.02 16.06 ? 304 ARG A NH1 1 ATOM 1769 N NH2 . ARG A 1 224 ? 23.093 34.522 43.550 0.02 15.97 ? 304 ARG A NH2 1 ATOM 1770 N N . ILE A 1 225 ? 27.185 26.993 42.236 1.00 13.76 ? 305 ILE A N 1 ATOM 1771 C CA . ILE A 1 225 ? 27.645 25.866 41.449 1.00 10.94 ? 305 ILE A CA 1 ATOM 1772 C C . ILE A 1 225 ? 27.054 25.957 40.064 1.00 13.87 ? 305 ILE A C 1 ATOM 1773 O O . ILE A 1 225 ? 25.876 26.300 39.931 1.00 15.70 ? 305 ILE A O 1 ATOM 1774 C CB . ILE A 1 225 ? 27.227 24.526 42.085 1.00 9.30 ? 305 ILE A CB 1 ATOM 1775 C CG1 . ILE A 1 225 ? 27.729 24.384 43.512 1.00 6.27 ? 305 ILE A CG1 1 ATOM 1776 C CG2 . ILE A 1 225 ? 27.889 23.402 41.322 1.00 7.65 ? 305 ILE A CG2 1 ATOM 1777 C CD1 . ILE A 1 225 ? 27.102 23.297 44.364 1.00 5.05 ? 305 ILE A CD1 1 ATOM 1778 N N . ASP A 1 226 ? 27.867 25.661 39.042 1.00 14.98 ? 306 ASP A N 1 ATOM 1779 C CA . ASP A 1 226 ? 27.408 25.595 37.649 1.00 15.73 ? 306 ASP A CA 1 ATOM 1780 C C . ASP A 1 226 ? 27.440 24.096 37.382 1.00 15.39 ? 306 ASP A C 1 ATOM 1781 O O . ASP A 1 226 ? 28.544 23.506 37.310 1.00 17.47 ? 306 ASP A O 1 ATOM 1782 C CB . ASP A 1 226 ? 28.383 26.265 36.662 1.00 18.33 ? 306 ASP A CB 1 ATOM 1783 C CG . ASP A 1 226 ? 28.047 26.185 35.166 1.00 20.34 ? 306 ASP A CG 1 ATOM 1784 O OD1 . ASP A 1 226 ? 27.124 25.502 34.730 1.00 20.87 ? 306 ASP A OD1 1 ATOM 1785 O OD2 . ASP A 1 226 ? 28.744 26.801 34.378 1.00 23.84 ? 306 ASP A OD2 1 ATOM 1786 N N . PRO A 1 227 ? 26.301 23.431 37.199 1.00 12.32 ? 307 PRO A N 1 ATOM 1787 C CA . PRO A 1 227 ? 26.253 22.011 36.934 1.00 8.51 ? 307 PRO A CA 1 ATOM 1788 C C . PRO A 1 227 ? 26.661 21.693 35.487 1.00 8.32 ? 307 PRO A C 1 ATOM 1789 O O . PRO A 1 227 ? 27.041 20.552 35.299 1.00 7.44 ? 307 PRO A O 1 ATOM 1790 C CB . PRO A 1 227 ? 24.830 21.649 37.321 1.00 6.26 ? 307 PRO A CB 1 ATOM 1791 C CG . PRO A 1 227 ? 24.080 22.859 36.823 1.00 7.05 ? 307 PRO A CG 1 ATOM 1792 C CD . PRO A 1 227 ? 24.944 23.946 37.410 1.00 10.55 ? 307 PRO A CD 1 ATOM 1793 N N . VAL A 1 228 ? 26.707 22.548 34.449 1.00 7.48 ? 308 VAL A N 1 ATOM 1794 C CA . VAL A 1 228 ? 27.120 22.106 33.107 1.00 8.20 ? 308 VAL A CA 1 ATOM 1795 C C . VAL A 1 228 ? 28.661 22.122 33.029 1.00 8.45 ? 308 VAL A C 1 ATOM 1796 O O . VAL A 1 228 ? 29.321 21.142 32.706 1.00 8.84 ? 308 VAL A O 1 ATOM 1797 C CB . VAL A 1 228 ? 26.469 23.054 32.096 1.00 8.33 ? 308 VAL A CB 1 ATOM 1798 C CG1 . VAL A 1 228 ? 26.797 22.605 30.654 1.00 7.06 ? 308 VAL A CG1 1 ATOM 1799 C CG2 . VAL A 1 228 ? 24.944 23.049 32.329 1.00 8.16 ? 308 VAL A CG2 1 ATOM 1800 N N . ALA A 1 229 ? 29.282 23.256 33.385 1.00 10.93 ? 309 ALA A N 1 ATOM 1801 C CA . ALA A 1 229 ? 30.724 23.372 33.467 1.00 11.04 ? 309 ALA A CA 1 ATOM 1802 C C . ALA A 1 229 ? 31.272 22.639 34.661 1.00 14.07 ? 309 ALA A C 1 ATOM 1803 O O . ALA A 1 229 ? 32.487 22.459 34.738 1.00 17.50 ? 309 ALA A O 1 ATOM 1804 C CB . ALA A 1 229 ? 31.152 24.782 33.655 1.00 10.66 ? 309 ALA A CB 1 ATOM 1805 N N . MET A 1 230 ? 30.478 22.247 35.661 1.00 15.19 ? 310 MET A N 1 ATOM 1806 C CA . MET A 1 230 ? 31.005 21.609 36.862 1.00 15.62 ? 310 MET A CA 1 ATOM 1807 C C . MET A 1 230 ? 32.110 22.450 37.529 1.00 14.19 ? 310 MET A C 1 ATOM 1808 O O . MET A 1 230 ? 33.276 22.099 37.620 1.00 14.90 ? 310 MET A O 1 ATOM 1809 C CB . MET A 1 230 ? 31.480 20.150 36.498 1.00 14.76 ? 310 MET A CB 1 ATOM 1810 C CG . MET A 1 230 ? 30.343 19.293 35.919 1.00 13.86 ? 310 MET A CG 1 ATOM 1811 S SD . MET A 1 230 ? 30.856 17.553 35.748 1.00 19.49 ? 310 MET A SD 1 ATOM 1812 C CE . MET A 1 230 ? 29.996 17.125 34.279 1.00 14.97 ? 310 MET A CE 1 ATOM 1813 N N . THR A 1 231 ? 31.764 23.650 37.961 1.00 17.11 ? 311 THR A N 1 ATOM 1814 C CA . THR A 1 231 ? 32.687 24.489 38.759 1.00 16.98 ? 311 THR A CA 1 ATOM 1815 C C . THR A 1 231 ? 31.898 25.229 39.830 1.00 15.97 ? 311 THR A C 1 ATOM 1816 O O . THR A 1 231 ? 30.660 25.122 39.851 1.00 17.83 ? 311 THR A O 1 ATOM 1817 C CB . THR A 1 231 ? 33.425 25.570 37.965 1.00 17.24 ? 311 THR A CB 1 ATOM 1818 O OG1 . THR A 1 231 ? 32.863 25.703 36.673 1.00 17.68 ? 311 THR A OG1 1 ATOM 1819 C CG2 . THR A 1 231 ? 34.908 25.204 37.907 1.00 18.13 ? 311 THR A CG2 1 ATOM 1820 N N . HIS A 1 232 ? 32.506 26.003 40.738 1.00 16.71 ? 312 HIS A N 1 ATOM 1821 C CA . HIS A 1 232 ? 31.766 26.711 41.787 1.00 16.68 ? 312 HIS A CA 1 ATOM 1822 C C . HIS A 1 232 ? 32.522 27.951 42.265 1.00 17.60 ? 312 HIS A C 1 ATOM 1823 O O . HIS A 1 232 ? 33.651 28.187 41.838 1.00 21.11 ? 312 HIS A O 1 ATOM 1824 C CB . HIS A 1 232 ? 31.567 25.800 43.000 1.00 13.69 ? 312 HIS A CB 1 ATOM 1825 C CG . HIS A 1 232 ? 32.883 25.507 43.711 1.00 10.75 ? 312 HIS A CG 1 ATOM 1826 N ND1 . HIS A 1 232 ? 33.782 24.584 43.380 1.00 9.94 ? 312 HIS A ND1 1 ATOM 1827 C CD2 . HIS A 1 232 ? 33.348 26.126 44.858 1.00 10.45 ? 312 HIS A CD2 1 ATOM 1828 C CE1 . HIS A 1 232 ? 34.739 24.590 44.274 1.00 8.29 ? 312 HIS A CE1 1 ATOM 1829 N NE2 . HIS A 1 232 ? 34.466 25.526 45.151 1.00 8.53 ? 312 HIS A NE2 1 ATOM 1830 N N . THR A 1 233 ? 31.996 28.723 43.201 1.00 16.45 ? 313 THR A N 1 ATOM 1831 C CA . THR A 1 233 ? 32.719 29.790 43.883 1.00 19.14 ? 313 THR A CA 1 ATOM 1832 C C . THR A 1 233 ? 32.060 29.953 45.237 1.00 18.42 ? 313 THR A C 1 ATOM 1833 O O . THR A 1 233 ? 30.924 29.473 45.397 1.00 19.04 ? 313 THR A O 1 ATOM 1834 C CB . THR A 1 233 ? 32.619 31.173 43.236 1.00 21.50 ? 313 THR A CB 1 ATOM 1835 O OG1 . THR A 1 233 ? 31.594 31.201 42.238 1.00 23.90 ? 313 THR A OG1 1 ATOM 1836 C CG2 . THR A 1 233 ? 34.035 31.558 42.839 1.00 25.00 ? 313 THR A CG2 1 ATOM 1837 N N . SER A 1 234 ? 32.754 30.570 46.196 1.00 17.19 ? 314 SER A N 1 ATOM 1838 C CA . SER A 1 234 ? 32.201 30.883 47.489 1.00 15.54 ? 314 SER A CA 1 ATOM 1839 C C . SER A 1 234 ? 32.574 32.321 47.825 1.00 17.83 ? 314 SER A C 1 ATOM 1840 O O . SER A 1 234 ? 33.619 32.809 47.355 1.00 15.75 ? 314 SER A O 1 ATOM 1841 C CB . SER A 1 234 ? 32.740 29.995 48.537 1.00 11.62 ? 314 SER A CB 1 ATOM 1842 O OG . SER A 1 234 ? 34.136 30.148 48.677 1.00 10.35 ? 314 SER A OG 1 ATOM 1843 N N . GLN A 1 235 ? 31.773 32.907 48.741 1.00 18.10 ? 315 GLN A N 1 ATOM 1844 C CA . GLN A 1 235 ? 31.717 34.295 49.171 1.00 16.36 ? 315 GLN A CA 1 ATOM 1845 C C . GLN A 1 235 ? 30.963 34.168 50.488 1.00 16.74 ? 315 GLN A C 1 ATOM 1846 O O . GLN A 1 235 ? 30.559 33.051 50.870 1.00 16.97 ? 315 GLN A O 1 ATOM 1847 C CB . GLN A 1 235 ? 30.866 35.100 48.241 1.00 17.79 ? 315 GLN A CB 1 ATOM 1848 C CG . GLN A 1 235 ? 30.880 36.618 48.419 1.00 20.77 ? 315 GLN A CG 1 ATOM 1849 C CD . GLN A 1 235 ? 29.748 37.309 47.657 1.00 20.78 ? 315 GLN A CD 1 ATOM 1850 O OE1 . GLN A 1 235 ? 29.178 36.744 46.718 1.00 21.30 ? 315 GLN A OE1 1 ATOM 1851 N NE2 . GLN A 1 235 ? 29.418 38.542 48.048 1.00 20.84 ? 315 GLN A NE2 1 ATOM 1852 N N . TYR A 1 236 ? 30.758 35.282 51.203 1.00 13.41 ? 316 TYR A N 1 ATOM 1853 C CA . TYR A 1 236 ? 29.861 35.283 52.343 1.00 11.46 ? 316 TYR A CA 1 ATOM 1854 C C . TYR A 1 236 ? 28.719 36.224 51.917 1.00 11.56 ? 316 TYR A C 1 ATOM 1855 O O . TYR A 1 236 ? 28.896 37.003 50.971 1.00 11.61 ? 316 TYR A O 1 ATOM 1856 C CB . TYR A 1 236 ? 30.482 35.857 53.567 1.00 8.08 ? 316 TYR A CB 1 ATOM 1857 C CG . TYR A 1 236 ? 31.387 34.875 54.250 1.00 6.25 ? 316 TYR A CG 1 ATOM 1858 C CD1 . TYR A 1 236 ? 32.710 34.782 53.874 1.00 8.16 ? 316 TYR A CD1 1 ATOM 1859 C CD2 . TYR A 1 236 ? 30.911 34.148 55.301 1.00 8.12 ? 316 TYR A CD2 1 ATOM 1860 C CE1 . TYR A 1 236 ? 33.592 33.976 54.546 1.00 8.31 ? 316 TYR A CE1 1 ATOM 1861 C CE2 . TYR A 1 236 ? 31.773 33.334 55.991 1.00 8.31 ? 316 TYR A CE2 1 ATOM 1862 C CZ . TYR A 1 236 ? 33.098 33.266 55.612 1.00 8.44 ? 316 TYR A CZ 1 ATOM 1863 O OH . TYR A 1 236 ? 33.951 32.481 56.344 1.00 7.46 ? 316 TYR A OH 1 ATOM 1864 N N . ILE A 1 237 ? 27.542 36.159 52.546 1.00 11.54 ? 317 ILE A N 1 ATOM 1865 C CA . ILE A 1 237 ? 26.444 37.088 52.279 1.00 13.20 ? 317 ILE A CA 1 ATOM 1866 C C . ILE A 1 237 ? 26.929 38.411 52.866 1.00 13.20 ? 317 ILE A C 1 ATOM 1867 O O . ILE A 1 237 ? 27.256 38.520 54.055 1.00 14.90 ? 317 ILE A O 1 ATOM 1868 C CB . ILE A 1 237 ? 25.083 36.609 53.000 1.00 14.07 ? 317 ILE A CB 1 ATOM 1869 C CG1 . ILE A 1 237 ? 24.602 35.286 52.427 1.00 14.11 ? 317 ILE A CG1 1 ATOM 1870 C CG2 . ILE A 1 237 ? 23.942 37.634 52.804 1.00 12.60 ? 317 ILE A CG2 1 ATOM 1871 C CD1 . ILE A 1 237 ? 23.442 34.628 53.204 1.00 13.95 ? 317 ILE A CD1 1 ATOM 1872 N N . CYS A 1 238 ? 27.031 39.436 52.024 1.00 14.81 ? 318 CYS A N 1 ATOM 1873 C CA . CYS A 1 238 ? 27.354 40.797 52.406 1.00 14.84 ? 318 CYS A CA 1 ATOM 1874 C C . CYS A 1 238 ? 26.548 41.471 53.509 1.00 14.34 ? 318 CYS A C 1 ATOM 1875 O O . CYS A 1 238 ? 27.124 42.181 54.351 1.00 13.93 ? 318 CYS A O 1 ATOM 1876 C CB . CYS A 1 238 ? 27.268 41.705 51.217 1.00 14.61 ? 318 CYS A CB 1 ATOM 1877 S SG . CYS A 1 238 ? 28.480 41.379 49.906 1.00 21.12 ? 318 CYS A SG 1 ATOM 1878 N N . SER A 1 239 ? 25.217 41.271 53.532 1.00 12.11 ? 319 SER A N 1 ATOM 1879 C CA . SER A 1 239 ? 24.308 41.993 54.407 1.00 11.60 ? 319 SER A CA 1 ATOM 1880 C C . SER A 1 239 ? 24.663 42.039 55.891 1.00 13.56 ? 319 SER A C 1 ATOM 1881 O O . SER A 1 239 ? 25.087 41.008 56.419 1.00 16.23 ? 319 SER A O 1 ATOM 1882 C CB . SER A 1 239 ? 22.931 41.392 54.279 1.00 9.32 ? 319 SER A CB 1 ATOM 1883 O OG . SER A 1 239 ? 22.030 42.170 55.050 1.00 9.27 ? 319 SER A OG 1 ATOM 1884 N N . PRO A 1 240 ? 24.495 43.146 56.643 1.00 14.07 ? 320 PRO A N 1 ATOM 1885 C CA . PRO A 1 240 ? 24.723 43.158 58.090 1.00 12.00 ? 320 PRO A CA 1 ATOM 1886 C C . PRO A 1 240 ? 23.623 42.412 58.868 1.00 13.88 ? 320 PRO A C 1 ATOM 1887 O O . PRO A 1 240 ? 23.744 42.269 60.101 1.00 14.73 ? 320 PRO A O 1 ATOM 1888 C CB . PRO A 1 240 ? 24.830 44.638 58.399 1.00 11.33 ? 320 PRO A CB 1 ATOM 1889 C CG . PRO A 1 240 ? 23.827 45.251 57.440 1.00 11.46 ? 320 PRO A CG 1 ATOM 1890 C CD . PRO A 1 240 ? 24.051 44.455 56.151 1.00 12.60 ? 320 PRO A CD 1 ATOM 1891 N N . VAL A 1 241 ? 22.518 41.935 58.252 1.00 12.19 ? 321 VAL A N 1 ATOM 1892 C CA . VAL A 1 241 ? 21.452 41.190 58.966 1.00 8.03 ? 321 VAL A CA 1 ATOM 1893 C C . VAL A 1 241 ? 22.081 39.812 59.146 1.00 9.61 ? 321 VAL A C 1 ATOM 1894 O O . VAL A 1 241 ? 22.195 39.057 58.174 1.00 8.78 ? 321 VAL A O 1 ATOM 1895 C CB . VAL A 1 241 ? 20.157 41.076 58.113 1.00 6.24 ? 321 VAL A CB 1 ATOM 1896 C CG1 . VAL A 1 241 ? 19.166 40.276 58.868 1.00 4.08 ? 321 VAL A CG1 1 ATOM 1897 C CG2 . VAL A 1 241 ? 19.519 42.413 57.841 1.00 7.16 ? 321 VAL A CG2 1 ATOM 1898 N N . LEU A 1 242 ? 22.600 39.503 60.328 1.00 9.69 ? 322 LEU A N 1 ATOM 1899 C CA . LEU A 1 242 ? 23.286 38.246 60.581 1.00 9.45 ? 322 LEU A CA 1 ATOM 1900 C C . LEU A 1 242 ? 22.367 37.067 60.846 1.00 8.19 ? 322 LEU A C 1 ATOM 1901 O O . LEU A 1 242 ? 21.371 37.158 61.556 1.00 10.45 ? 322 LEU A O 1 ATOM 1902 C CB . LEU A 1 242 ? 24.218 38.470 61.764 1.00 10.28 ? 322 LEU A CB 1 ATOM 1903 C CG . LEU A 1 242 ? 25.235 39.595 61.658 1.00 11.29 ? 322 LEU A CG 1 ATOM 1904 C CD1 . LEU A 1 242 ? 25.972 39.701 62.977 1.00 13.20 ? 322 LEU A CD1 1 ATOM 1905 C CD2 . LEU A 1 242 ? 26.176 39.355 60.488 1.00 11.09 ? 322 LEU A CD2 1 ATOM 1906 N N . THR A 1 243 ? 22.592 35.921 60.224 1.00 7.71 ? 323 THR A N 1 ATOM 1907 C CA . THR A 1 243 ? 21.653 34.849 60.403 1.00 6.22 ? 323 THR A CA 1 ATOM 1908 C C . THR A 1 243 ? 22.261 33.581 60.972 1.00 6.34 ? 323 THR A C 1 ATOM 1909 O O . THR A 1 243 ? 21.546 32.587 60.954 1.00 10.18 ? 323 THR A O 1 ATOM 1910 C CB . THR A 1 243 ? 20.996 34.578 59.032 1.00 3.73 ? 323 THR A CB 1 ATOM 1911 O OG1 . THR A 1 243 ? 22.022 34.608 58.088 1.00 3.66 ? 323 THR A OG1 1 ATOM 1912 C CG2 . THR A 1 243 ? 20.004 35.632 58.643 1.00 5.21 ? 323 THR A CG2 1 ATOM 1913 N N . ASP A 1 244 ? 23.514 33.463 61.448 1.00 6.76 ? 324 ASP A N 1 ATOM 1914 C CA . ASP A 1 244 ? 23.820 32.260 62.208 1.00 8.32 ? 324 ASP A CA 1 ATOM 1915 C C . ASP A 1 244 ? 23.335 32.389 63.667 1.00 9.14 ? 324 ASP A C 1 ATOM 1916 O O . ASP A 1 244 ? 22.614 33.312 64.046 1.00 8.15 ? 324 ASP A O 1 ATOM 1917 C CB . ASP A 1 244 ? 25.309 31.956 62.173 1.00 7.60 ? 324 ASP A CB 1 ATOM 1918 C CG . ASP A 1 244 ? 25.576 30.452 62.191 1.00 8.89 ? 324 ASP A CG 1 ATOM 1919 O OD1 . ASP A 1 244 ? 24.725 29.667 62.624 1.00 10.57 ? 324 ASP A OD1 1 ATOM 1920 O OD2 . ASP A 1 244 ? 26.641 30.062 61.749 1.00 10.35 ? 324 ASP A OD2 1 ATOM 1921 N N . ASN A 1 245 ? 23.624 31.446 64.552 1.00 10.46 ? 325 ASN A N 1 ATOM 1922 C CA . ASN A 1 245 ? 23.145 31.466 65.911 1.00 12.38 ? 325 ASN A CA 1 ATOM 1923 C C . ASN A 1 245 ? 24.060 30.509 66.660 1.00 14.36 ? 325 ASN A C 1 ATOM 1924 O O . ASN A 1 245 ? 24.249 29.396 66.164 1.00 15.16 ? 325 ASN A O 1 ATOM 1925 C CB . ASN A 1 245 ? 21.707 30.978 65.957 1.00 11.96 ? 325 ASN A CB 1 ATOM 1926 C CG . ASN A 1 245 ? 21.227 30.829 67.379 1.00 12.27 ? 325 ASN A CG 1 ATOM 1927 O OD1 . ASN A 1 245 ? 21.567 29.826 67.992 1.00 12.37 ? 325 ASN A OD1 1 ATOM 1928 N ND2 . ASN A 1 245 ? 20.530 31.775 67.993 1.00 10.51 ? 325 ASN A ND2 1 ATOM 1929 N N . PRO A 1 246 ? 24.706 30.901 67.768 1.00 15.34 ? 326 PRO A N 1 ATOM 1930 C CA . PRO A 1 246 ? 24.632 32.239 68.353 1.00 16.45 ? 326 PRO A CA 1 ATOM 1931 C C . PRO A 1 246 ? 25.259 33.371 67.499 1.00 18.42 ? 326 PRO A C 1 ATOM 1932 O O . PRO A 1 246 ? 25.975 33.085 66.526 1.00 20.69 ? 326 PRO A O 1 ATOM 1933 C CB . PRO A 1 246 ? 25.288 32.026 69.691 1.00 15.28 ? 326 PRO A CB 1 ATOM 1934 C CG . PRO A 1 246 ? 25.657 30.577 69.771 1.00 14.74 ? 326 PRO A CG 1 ATOM 1935 C CD . PRO A 1 246 ? 25.817 30.192 68.341 1.00 14.10 ? 326 PRO A CD 1 ATOM 1936 N N . ARG A 1 247 ? 25.054 34.654 67.758 1.00 17.07 ? 327 ARG A N 1 ATOM 1937 C CA . ARG A 1 247 ? 25.575 35.701 66.880 1.00 16.47 ? 327 ARG A CA 1 ATOM 1938 C C . ARG A 1 247 ? 25.592 37.005 67.690 1.00 16.87 ? 327 ARG A C 1 ATOM 1939 O O . ARG A 1 247 ? 24.782 37.195 68.609 1.00 18.09 ? 327 ARG A O 1 ATOM 1940 C CB . ARG A 1 247 ? 24.654 35.857 65.649 1.00 15.34 ? 327 ARG A CB 1 ATOM 1941 C CG . ARG A 1 247 ? 23.259 36.419 65.979 1.00 11.59 ? 327 ARG A CG 1 ATOM 1942 C CD . ARG A 1 247 ? 22.382 36.399 64.743 1.00 11.57 ? 327 ARG A CD 1 ATOM 1943 N NE . ARG A 1 247 ? 21.046 36.823 65.150 1.00 11.77 ? 327 ARG A NE 1 ATOM 1944 C CZ . ARG A 1 247 ? 20.009 35.973 65.206 1.00 11.31 ? 327 ARG A CZ 1 ATOM 1945 N NH1 . ARG A 1 247 ? 20.121 34.674 64.930 1.00 11.90 ? 327 ARG A NH1 1 ATOM 1946 N NH2 . ARG A 1 247 ? 18.861 36.442 65.654 1.00 10.91 ? 327 ARG A NH2 1 ATOM 1947 N N . PRO A 1 248 ? 26.467 37.954 67.386 1.00 15.25 ? 328 PRO A N 1 ATOM 1948 C CA . PRO A 1 248 ? 26.388 39.288 67.945 1.00 16.41 ? 328 PRO A CA 1 ATOM 1949 C C . PRO A 1 248 ? 25.261 40.091 67.363 1.00 17.43 ? 328 PRO A C 1 ATOM 1950 O O . PRO A 1 248 ? 24.607 39.631 66.430 1.00 18.58 ? 328 PRO A O 1 ATOM 1951 C CB . PRO A 1 248 ? 27.751 39.832 67.671 1.00 15.23 ? 328 PRO A CB 1 ATOM 1952 C CG . PRO A 1 248 ? 28.203 39.170 66.390 1.00 14.75 ? 328 PRO A CG 1 ATOM 1953 C CD . PRO A 1 248 ? 27.685 37.766 66.586 1.00 16.56 ? 328 PRO A CD 1 ATOM 1954 N N . ASN A 1 249 ? 25.016 41.269 67.916 1.00 19.66 ? 329 ASN A N 1 ATOM 1955 C CA . ASN A 1 249 ? 24.043 42.199 67.350 1.00 23.42 ? 329 ASN A CA 1 ATOM 1956 C C . ASN A 1 249 ? 24.280 42.496 65.876 1.00 19.20 ? 329 ASN A C 1 ATOM 1957 O O . ASN A 1 249 ? 25.443 42.453 65.430 1.00 17.41 ? 329 ASN A O 1 ATOM 1958 C CB . ASN A 1 249 ? 24.080 43.540 68.050 1.00 31.94 ? 329 ASN A CB 1 ATOM 1959 C CG . ASN A 1 249 ? 23.468 43.549 69.426 1.00 41.28 ? 329 ASN A CG 1 ATOM 1960 O OD1 . ASN A 1 249 ? 23.359 42.527 70.074 1.00 46.85 ? 329 ASN A OD1 1 ATOM 1961 N ND2 . ASN A 1 249 ? 23.079 44.678 69.977 1.00 46.14 ? 329 ASN A ND2 1 ATOM 1962 N N . ASP A 1 250 ? 23.249 42.820 65.097 1.00 15.94 ? 330 ASP A N 1 ATOM 1963 C CA . ASP A 1 250 ? 23.495 43.119 63.684 1.00 17.34 ? 330 ASP A CA 1 ATOM 1964 C C . ASP A 1 250 ? 24.232 44.439 63.546 1.00 17.25 ? 330 ASP A C 1 ATOM 1965 O O . ASP A 1 250 ? 23.858 45.365 64.279 1.00 19.94 ? 330 ASP A O 1 ATOM 1966 C CB . ASP A 1 250 ? 22.209 43.244 62.887 1.00 16.03 ? 330 ASP A CB 1 ATOM 1967 C CG . ASP A 1 250 ? 21.334 42.010 62.854 1.00 15.99 ? 330 ASP A CG 1 ATOM 1968 O OD1 . ASP A 1 250 ? 21.842 40.883 62.766 1.00 14.60 ? 330 ASP A OD1 1 ATOM 1969 O OD2 . ASP A 1 250 ? 20.128 42.210 62.926 1.00 15.09 ? 330 ASP A OD2 1 ATOM 1970 N N . PRO A 1 251 ? 25.291 44.583 62.734 1.00 16.70 ? 331 PRO A N 1 ATOM 1971 C CA . PRO A 1 251 ? 26.039 45.837 62.624 1.00 17.18 ? 331 PRO A CA 1 ATOM 1972 C C . PRO A 1 251 ? 25.400 46.840 61.685 1.00 16.63 ? 331 PRO A C 1 ATOM 1973 O O . PRO A 1 251 ? 24.245 46.696 61.330 1.00 19.28 ? 331 PRO A O 1 ATOM 1974 C CB . PRO A 1 251 ? 27.415 45.408 62.175 1.00 15.14 ? 331 PRO A CB 1 ATOM 1975 C CG . PRO A 1 251 ? 27.134 44.185 61.352 1.00 13.88 ? 331 PRO A CG 1 ATOM 1976 C CD . PRO A 1 251 ? 26.078 43.476 62.191 1.00 16.33 ? 331 PRO A CD 1 ATOM 1977 N N . THR A 1 252 ? 26.075 47.894 61.280 1.00 15.87 ? 332 THR A N 1 ATOM 1978 C CA . THR A 1 252 ? 25.500 48.808 60.318 1.00 14.15 ? 332 THR A CA 1 ATOM 1979 C C . THR A 1 252 ? 25.996 48.440 58.938 1.00 14.71 ? 332 THR A C 1 ATOM 1980 O O . THR A 1 252 ? 25.311 48.703 57.953 1.00 13.13 ? 332 THR A O 1 ATOM 1981 C CB . THR A 1 252 ? 25.902 50.234 60.722 1.00 16.61 ? 332 THR A CB 1 ATOM 1982 O OG1 . THR A 1 252 ? 25.146 50.573 61.869 1.00 17.88 ? 332 THR A OG1 1 ATOM 1983 C CG2 . THR A 1 252 ? 25.496 51.290 59.747 1.00 18.32 ? 332 THR A CG2 1 ATOM 1984 N N . VAL A 1 253 ? 27.194 47.824 58.882 1.00 16.99 ? 333 VAL A N 1 ATOM 1985 C CA . VAL A 1 253 ? 27.868 47.449 57.642 1.00 18.84 ? 333 VAL A CA 1 ATOM 1986 C C . VAL A 1 253 ? 28.208 45.953 57.797 1.00 20.62 ? 333 VAL A C 1 ATOM 1987 O O . VAL A 1 253 ? 28.517 45.513 58.925 1.00 20.65 ? 333 VAL A O 1 ATOM 1988 C CB . VAL A 1 253 ? 29.226 48.199 57.414 1.00 19.71 ? 333 VAL A CB 1 ATOM 1989 C CG1 . VAL A 1 253 ? 29.503 48.152 55.926 1.00 21.65 ? 333 VAL A CG1 1 ATOM 1990 C CG2 . VAL A 1 253 ? 29.212 49.647 57.844 1.00 20.06 ? 333 VAL A CG2 1 ATOM 1991 N N . GLY A 1 254 ? 28.253 45.171 56.715 1.00 19.92 ? 335 GLY A N 1 ATOM 1992 C CA . GLY A 1 254 ? 28.527 43.740 56.810 1.00 19.71 ? 335 GLY A CA 1 ATOM 1993 C C . GLY A 1 254 ? 29.799 43.323 56.102 1.00 19.54 ? 335 GLY A C 1 ATOM 1994 O O . GLY A 1 254 ? 30.581 44.188 55.727 1.00 21.45 ? 335 GLY A O 1 ATOM 1995 N N . LYS A 1 255 ? 30.075 42.036 55.867 1.00 20.61 ? 336 LYS A N 1 ATOM 1996 C CA . LYS A 1 255 ? 31.283 41.590 55.172 1.00 19.69 ? 336 LYS A CA 1 ATOM 1997 C C . LYS A 1 255 ? 30.947 40.578 54.095 1.00 19.14 ? 336 LYS A C 1 ATOM 1998 O O . LYS A 1 255 ? 30.255 39.580 54.327 1.00 19.14 ? 336 LYS A O 1 ATOM 1999 C CB . LYS A 1 255 ? 32.267 40.938 56.118 1.00 21.56 ? 336 LYS A CB 1 ATOM 2000 C CG . LYS A 1 255 ? 32.977 41.941 56.989 1.00 24.22 ? 336 LYS A CG 1 ATOM 2001 C CD . LYS A 1 255 ? 33.756 41.192 58.064 1.00 26.85 ? 336 LYS A CD 1 ATOM 2002 C CE . LYS A 1 255 ? 34.569 42.145 58.936 1.00 29.68 ? 336 LYS A CE 1 ATOM 2003 N NZ . LYS A 1 255 ? 35.482 42.996 58.175 1.00 33.74 ? 336 LYS A NZ 1 ATOM 2004 N N . CYS A 1 256 ? 31.523 40.878 52.920 1.00 18.25 ? 337 CYS A N 1 ATOM 2005 C CA . CYS A 1 256 ? 31.319 40.089 51.731 1.00 18.09 ? 337 CYS A CA 1 ATOM 2006 C C . CYS A 1 256 ? 32.326 39.001 51.583 1.00 18.67 ? 337 CYS A C 1 ATOM 2007 O O . CYS A 1 256 ? 32.005 37.970 51.009 1.00 17.57 ? 337 CYS A O 1 ATOM 2008 C CB . CYS A 1 256 ? 31.413 40.913 50.495 1.00 18.40 ? 337 CYS A CB 1 ATOM 2009 S SG . CYS A 1 256 ? 30.219 42.276 50.343 1.00 20.74 ? 337 CYS A SG 1 ATOM 2010 N N . ASN A 1 257 ? 33.553 39.108 52.076 1.00 20.11 ? 338 ASN A N 1 ATOM 2011 C CA . ASN A 1 257 ? 34.534 38.048 51.814 1.00 20.55 ? 338 ASN A CA 1 ATOM 2012 C C . ASN A 1 257 ? 35.339 37.672 53.034 1.00 22.41 ? 338 ASN A C 1 ATOM 2013 O O . ASN A 1 257 ? 36.403 37.067 52.937 1.00 24.97 ? 338 ASN A O 1 ATOM 2014 C CB . ASN A 1 257 ? 35.520 38.463 50.705 1.00 20.13 ? 338 ASN A CB 1 ATOM 2015 C CG . ASN A 1 257 ? 34.847 38.842 49.387 1.00 20.49 ? 338 ASN A CG 1 ATOM 2016 O OD1 . ASN A 1 257 ? 34.684 40.037 49.115 1.00 21.18 ? 338 ASN A OD1 1 ATOM 2017 N ND2 . ASN A 1 257 ? 34.372 37.918 48.552 1.00 19.42 ? 338 ASN A ND2 1 ATOM 2018 N N . ASP A 1 258 ? 34.801 37.971 54.210 1.00 22.25 ? 339 ASP A N 1 ATOM 2019 C CA . ASP A 1 258 ? 35.482 37.604 55.432 1.00 22.64 ? 339 ASP A CA 1 ATOM 2020 C C . ASP A 1 258 ? 34.441 37.219 56.446 1.00 21.11 ? 339 ASP A C 1 ATOM 2021 O O . ASP A 1 258 ? 33.317 37.681 56.311 1.00 20.94 ? 339 ASP A O 1 ATOM 2022 C CB . ASP A 1 258 ? 36.278 38.753 55.957 1.00 28.49 ? 339 ASP A CB 1 ATOM 2023 C CG . ASP A 1 258 ? 37.679 38.841 55.339 1.00 33.31 ? 339 ASP A CG 1 ATOM 2024 O OD1 . ASP A 1 258 ? 38.474 37.920 55.572 1.00 35.62 ? 339 ASP A OD1 1 ATOM 2025 O OD2 . ASP A 1 258 ? 37.979 39.827 54.640 1.00 34.63 ? 339 ASP A OD2 1 ATOM 2026 N N . PRO A 1 259 ? 34.688 36.351 57.425 1.00 19.31 ? 340 PRO A N 1 ATOM 2027 C CA . PRO A 1 259 ? 33.763 36.052 58.516 1.00 19.52 ? 340 PRO A CA 1 ATOM 2028 C C . PRO A 1 259 ? 33.455 37.266 59.376 1.00 18.81 ? 340 PRO A C 1 ATOM 2029 O O . PRO A 1 259 ? 34.294 38.149 59.540 1.00 19.76 ? 340 PRO A O 1 ATOM 2030 C CB . PRO A 1 259 ? 34.433 34.941 59.303 1.00 17.27 ? 340 PRO A CB 1 ATOM 2031 C CG . PRO A 1 259 ? 35.878 35.195 59.042 1.00 15.97 ? 340 PRO A CG 1 ATOM 2032 C CD . PRO A 1 259 ? 35.862 35.510 57.549 1.00 18.68 ? 340 PRO A CD 1 ATOM 2033 N N . TYR A 1 260 ? 32.246 37.358 59.866 1.00 19.02 ? 341 TYR A N 1 ATOM 2034 C CA . TYR A 1 260 ? 31.987 38.400 60.816 1.00 20.35 ? 341 TYR A CA 1 ATOM 2035 C C . TYR A 1 260 ? 32.303 37.814 62.191 1.00 20.00 ? 341 TYR A C 1 ATOM 2036 O O . TYR A 1 260 ? 31.655 36.820 62.547 1.00 20.06 ? 341 TYR A O 1 ATOM 2037 C CB . TYR A 1 260 ? 30.533 38.832 60.776 1.00 19.97 ? 341 TYR A CB 1 ATOM 2038 C CG . TYR A 1 260 ? 30.328 40.157 61.501 1.00 19.34 ? 341 TYR A CG 1 ATOM 2039 C CD1 . TYR A 1 260 ? 30.734 41.342 60.898 1.00 20.63 ? 341 TYR A CD1 1 ATOM 2040 C CD2 . TYR A 1 260 ? 29.767 40.172 62.763 1.00 19.19 ? 341 TYR A CD2 1 ATOM 2041 C CE1 . TYR A 1 260 ? 30.578 42.551 61.549 1.00 21.30 ? 341 TYR A CE1 1 ATOM 2042 C CE2 . TYR A 1 260 ? 29.609 41.377 63.416 1.00 21.10 ? 341 TYR A CE2 1 ATOM 2043 C CZ . TYR A 1 260 ? 30.012 42.552 62.809 1.00 21.68 ? 341 TYR A CZ 1 ATOM 2044 O OH . TYR A 1 260 ? 29.844 43.747 63.482 1.00 21.34 ? 341 TYR A OH 1 ATOM 2045 N N . PRO A 1 261 ? 33.235 38.379 62.973 1.00 20.07 ? 342 PRO A N 1 ATOM 2046 C CA . PRO A 1 261 ? 33.676 37.850 64.256 1.00 19.69 ? 342 PRO A CA 1 ATOM 2047 C C . PRO A 1 261 ? 32.684 38.123 65.389 1.00 20.40 ? 342 PRO A C 1 ATOM 2048 O O . PRO A 1 261 ? 31.764 38.950 65.263 1.00 19.17 ? 342 PRO A O 1 ATOM 2049 C CB . PRO A 1 261 ? 35.038 38.511 64.411 1.00 19.99 ? 342 PRO A CB 1 ATOM 2050 C CG . PRO A 1 261 ? 34.703 39.944 64.019 1.00 19.02 ? 342 PRO A CG 1 ATOM 2051 C CD . PRO A 1 261 ? 33.834 39.703 62.763 1.00 19.96 ? 342 PRO A CD 1 ATOM 2052 N N . GLY A 1 262 ? 32.852 37.466 66.531 1.00 20.71 ? 343 GLY A N 1 ATOM 2053 C CA . GLY A 1 262 ? 31.922 37.705 67.617 1.00 23.24 ? 343 GLY A CA 1 ATOM 2054 C C . GLY A 1 262 ? 31.625 36.409 68.323 1.00 25.75 ? 343 GLY A C 1 ATOM 2055 O O . GLY A 1 262 ? 31.673 36.380 69.552 1.00 28.28 ? 343 GLY A O 1 ATOM 2056 N N . ASN A 1 263 ? 31.227 35.339 67.624 1.00 26.37 ? 344 ASN A N 1 ATOM 2057 C CA . ASN A 1 263 ? 31.076 34.021 68.232 1.00 25.34 ? 344 ASN A CA 1 ATOM 2058 C C . ASN A 1 263 ? 32.051 33.130 67.447 1.00 25.92 ? 344 ASN A C 1 ATOM 2059 O O . ASN A 1 263 ? 32.254 33.360 66.240 1.00 28.26 ? 344 ASN A O 1 ATOM 2060 C CB . ASN A 1 263 ? 29.665 33.476 68.067 0.02 23.06 ? 344 ASN A CB 1 ATOM 2061 C CG . ASN A 1 263 ? 29.528 32.099 68.701 0.02 21.35 ? 344 ASN A CG 1 ATOM 2062 O OD1 . ASN A 1 263 ? 29.132 31.139 68.052 0.02 20.37 ? 344 ASN A OD1 1 ATOM 2063 N ND2 . ASN A 1 263 ? 29.832 31.910 69.978 0.02 20.43 ? 344 ASN A ND2 1 ATOM 2064 N N . ASN A 1 264 ? 32.715 32.177 68.123 1.00 23.73 ? 345 ASN A N 1 ATOM 2065 C CA . ASN A 1 264 ? 33.560 31.160 67.499 1.00 21.85 ? 345 ASN A CA 1 ATOM 2066 C C . ASN A 1 264 ? 33.065 29.782 67.920 1.00 21.52 ? 345 ASN A C 1 ATOM 2067 O O . ASN A 1 264 ? 32.439 29.564 68.962 1.00 20.87 ? 345 ASN A O 1 ATOM 2068 C CB . ASN A 1 264 ? 35.010 31.287 67.934 0.02 21.08 ? 345 ASN A CB 1 ATOM 2069 C CG . ASN A 1 264 ? 35.695 32.512 67.360 0.02 20.43 ? 345 ASN A CG 1 ATOM 2070 O OD1 . ASN A 1 264 ? 35.757 33.566 67.990 0.02 20.11 ? 345 ASN A OD1 1 ATOM 2071 N ND2 . ASN A 1 264 ? 36.210 32.421 66.145 0.02 20.17 ? 345 ASN A ND2 1 ATOM 2072 N N . ASN A 1 265 ? 33.251 28.840 67.010 1.00 21.90 ? 346 ASN A N 1 ATOM 2073 C CA . ASN A 1 265 ? 33.021 27.425 67.238 1.00 21.46 ? 346 ASN A CA 1 ATOM 2074 C C . ASN A 1 265 ? 31.639 26.934 67.620 1.00 20.60 ? 346 ASN A C 1 ATOM 2075 O O . ASN A 1 265 ? 31.432 26.183 68.572 1.00 18.70 ? 346 ASN A O 1 ATOM 2076 C CB . ASN A 1 265 ? 34.044 26.956 68.258 1.00 23.31 ? 346 ASN A CB 1 ATOM 2077 C CG . ASN A 1 265 ? 35.450 27.024 67.698 1.00 26.29 ? 346 ASN A CG 1 ATOM 2078 O OD1 . ASN A 1 265 ? 36.390 27.398 68.408 1.00 27.36 ? 346 ASN A OD1 1 ATOM 2079 N ND2 . ASN A 1 265 ? 35.670 26.703 66.426 1.00 26.11 ? 346 ASN A ND2 1 ATOM 2080 N N . ASN A 1 266 ? 30.633 27.314 66.851 1.00 21.73 ? 347 ASN A N 1 ATOM 2081 C CA . ASN A 1 266 ? 29.267 26.863 67.106 1.00 22.23 ? 347 ASN A CA 1 ATOM 2082 C C . ASN A 1 266 ? 28.300 27.358 66.037 1.00 21.86 ? 347 ASN A C 1 ATOM 2083 O O . ASN A 1 266 ? 28.624 28.324 65.333 1.00 22.66 ? 347 ASN A O 1 ATOM 2084 C CB . ASN A 1 266 ? 28.787 27.365 68.444 1.00 24.04 ? 347 ASN A CB 1 ATOM 2085 C CG . ASN A 1 266 ? 27.523 26.656 68.884 1.00 24.99 ? 347 ASN A CG 1 ATOM 2086 O OD1 . ASN A 1 266 ? 27.035 25.669 68.321 1.00 26.96 ? 347 ASN A OD1 1 ATOM 2087 N ND2 . ASN A 1 266 ? 27.022 27.223 69.974 1.00 27.38 ? 347 ASN A ND2 1 ATOM 2088 N N . GLY A 1 267 ? 27.121 26.768 65.798 1.00 20.09 ? 348 GLY A N 1 ATOM 2089 C CA . GLY A 1 267 ? 26.256 27.400 64.824 1.00 19.29 ? 348 GLY A CA 1 ATOM 2090 C C . GLY A 1 267 ? 24.990 26.637 64.602 1.00 18.77 ? 348 GLY A C 1 ATOM 2091 O O . GLY A 1 267 ? 24.670 25.802 65.458 1.00 17.96 ? 348 GLY A O 1 ATOM 2092 N N . VAL A 1 268 ? 24.352 26.873 63.425 1.00 14.09 ? 349 VAL A N 1 ATOM 2093 C CA . VAL A 1 268 ? 23.162 26.149 63.072 1.00 11.61 ? 349 VAL A CA 1 ATOM 2094 C C . VAL A 1 268 ? 23.010 26.146 61.547 1.00 13.87 ? 349 VAL A C 1 ATOM 2095 O O . VAL A 1 268 ? 23.581 26.968 60.814 1.00 13.23 ? 349 VAL A O 1 ATOM 2096 C CB . VAL A 1 268 ? 21.958 26.793 63.830 1.00 11.18 ? 349 VAL A CB 1 ATOM 2097 C CG1 . VAL A 1 268 ? 21.448 28.100 63.257 1.00 10.43 ? 349 VAL A CG1 1 ATOM 2098 C CG2 . VAL A 1 268 ? 20.901 25.744 63.843 1.00 9.31 ? 349 VAL A CG2 1 ATOM 2099 N N . LYS A 1 269 ? 22.353 25.096 61.055 1.00 11.03 ? 350 LYS A N 1 ATOM 2100 C CA . LYS A 1 269 ? 22.055 24.977 59.643 1.00 7.82 ? 350 LYS A CA 1 ATOM 2101 C C . LYS A 1 269 ? 20.980 25.984 59.246 1.00 5.87 ? 350 LYS A C 1 ATOM 2102 O O . LYS A 1 269 ? 19.989 26.084 59.972 1.00 5.57 ? 350 LYS A O 1 ATOM 2103 C CB . LYS A 1 269 ? 21.631 23.511 59.412 1.00 5.17 ? 350 LYS A CB 1 ATOM 2104 C CG . LYS A 1 269 ? 21.201 23.291 57.985 1.00 4.42 ? 350 LYS A CG 1 ATOM 2105 C CD . LYS A 1 269 ? 20.958 21.835 57.593 1.00 4.91 ? 350 LYS A CD 1 ATOM 2106 C CE . LYS A 1 269 ? 20.302 21.746 56.226 1.00 2.37 ? 350 LYS A CE 1 ATOM 2107 N NZ . LYS A 1 269 ? 21.202 22.187 55.187 1.00 2.39 ? 350 LYS A NZ 1 ATOM 2108 N N . GLY A 1 270 ? 21.105 26.733 58.153 1.00 5.01 ? 351 GLY A N 1 ATOM 2109 C CA . GLY A 1 270 ? 20.095 27.705 57.821 1.00 3.74 ? 351 GLY A CA 1 ATOM 2110 C C . GLY A 1 270 ? 20.016 27.782 56.308 1.00 5.99 ? 351 GLY A C 1 ATOM 2111 O O . GLY A 1 270 ? 20.487 26.888 55.591 1.00 7.45 ? 351 GLY A O 1 ATOM 2112 N N . PHE A 1 271 ? 19.363 28.794 55.733 1.00 7.19 ? 352 PHE A N 1 ATOM 2113 C CA . PHE A 1 271 ? 19.275 28.871 54.295 1.00 7.04 ? 352 PHE A CA 1 ATOM 2114 C C . PHE A 1 271 ? 18.919 30.296 53.949 1.00 7.12 ? 352 PHE A C 1 ATOM 2115 O O . PHE A 1 271 ? 18.635 31.072 54.854 1.00 6.62 ? 352 PHE A O 1 ATOM 2116 C CB . PHE A 1 271 ? 18.177 27.887 53.753 1.00 7.57 ? 352 PHE A CB 1 ATOM 2117 C CG . PHE A 1 271 ? 16.775 28.434 54.058 1.00 7.14 ? 352 PHE A CG 1 ATOM 2118 C CD1 . PHE A 1 271 ? 16.288 28.321 55.337 1.00 7.20 ? 352 PHE A CD1 1 ATOM 2119 C CD2 . PHE A 1 271 ? 16.050 29.091 53.067 1.00 5.36 ? 352 PHE A CD2 1 ATOM 2120 C CE1 . PHE A 1 271 ? 15.089 28.885 55.635 1.00 5.80 ? 352 PHE A CE1 1 ATOM 2121 C CE2 . PHE A 1 271 ? 14.839 29.664 53.379 1.00 6.38 ? 352 PHE A CE2 1 ATOM 2122 C CZ . PHE A 1 271 ? 14.381 29.545 54.678 1.00 6.74 ? 352 PHE A CZ 1 ATOM 2123 N N . SER A 1 272 ? 18.936 30.647 52.650 1.00 7.37 ? 353 SER A N 1 ATOM 2124 C CA . SER A 1 272 ? 18.355 31.898 52.177 1.00 8.18 ? 353 SER A CA 1 ATOM 2125 C C . SER A 1 272 ? 17.969 31.762 50.701 1.00 7.06 ? 353 SER A C 1 ATOM 2126 O O . SER A 1 272 ? 18.545 30.910 50.043 1.00 7.79 ? 353 SER A O 1 ATOM 2127 C CB . SER A 1 272 ? 19.372 33.025 52.403 1.00 8.41 ? 353 SER A CB 1 ATOM 2128 O OG . SER A 1 272 ? 20.603 32.813 51.767 1.00 13.55 ? 353 SER A OG 1 ATOM 2129 N N . TYR A 1 273 ? 16.957 32.425 50.144 1.00 7.29 ? 354 TYR A N 1 ATOM 2130 C CA . TYR A 1 273 ? 16.713 32.446 48.697 1.00 7.66 ? 354 TYR A CA 1 ATOM 2131 C C . TYR A 1 273 ? 17.265 33.750 48.168 1.00 7.00 ? 354 TYR A C 1 ATOM 2132 O O . TYR A 1 273 ? 16.717 34.796 48.478 1.00 6.98 ? 354 TYR A O 1 ATOM 2133 C CB . TYR A 1 273 ? 15.226 32.378 48.371 1.00 7.03 ? 354 TYR A CB 1 ATOM 2134 C CG . TYR A 1 273 ? 14.830 30.925 48.495 1.00 9.40 ? 354 TYR A CG 1 ATOM 2135 C CD1 . TYR A 1 273 ? 14.434 30.381 49.706 1.00 10.84 ? 354 TYR A CD1 1 ATOM 2136 C CD2 . TYR A 1 273 ? 14.899 30.134 47.344 1.00 10.70 ? 354 TYR A CD2 1 ATOM 2137 C CE1 . TYR A 1 273 ? 14.100 29.028 49.753 1.00 12.20 ? 354 TYR A CE1 1 ATOM 2138 C CE2 . TYR A 1 273 ? 14.577 28.796 47.386 1.00 10.69 ? 354 TYR A CE2 1 ATOM 2139 C CZ . TYR A 1 273 ? 14.179 28.240 48.589 1.00 11.94 ? 354 TYR A CZ 1 ATOM 2140 O OH . TYR A 1 273 ? 13.896 26.873 48.585 1.00 12.95 ? 354 TYR A OH 1 ATOM 2141 N N . LEU A 1 274 ? 18.410 33.722 47.499 1.00 8.64 ? 355 LEU A N 1 ATOM 2142 C CA . LEU A 1 274 ? 19.077 34.901 46.984 1.00 9.38 ? 355 LEU A CA 1 ATOM 2143 C C . LEU A 1 274 ? 18.680 35.331 45.567 1.00 10.55 ? 355 LEU A C 1 ATOM 2144 O O . LEU A 1 274 ? 19.272 34.927 44.577 1.00 11.15 ? 355 LEU A O 1 ATOM 2145 C CB . LEU A 1 274 ? 20.569 34.596 47.098 1.00 8.50 ? 355 LEU A CB 1 ATOM 2146 C CG . LEU A 1 274 ? 21.067 34.383 48.542 1.00 8.89 ? 355 LEU A CG 1 ATOM 2147 C CD1 . LEU A 1 274 ? 22.525 33.918 48.482 1.00 7.16 ? 355 LEU A CD1 1 ATOM 2148 C CD2 . LEU A 1 274 ? 20.850 35.649 49.381 1.00 6.09 ? 355 LEU A CD2 1 ATOM 2149 N N . ASP A 1 275 ? 17.697 36.201 45.359 1.00 12.36 ? 356 ASP A N 1 ATOM 2150 C CA . ASP A 1 275 ? 17.272 36.567 44.029 1.00 12.21 ? 356 ASP A CA 1 ATOM 2151 C C . ASP A 1 275 ? 17.080 38.083 43.803 1.00 12.25 ? 356 ASP A C 1 ATOM 2152 O O . ASP A 1 275 ? 15.961 38.594 43.619 1.00 9.90 ? 356 ASP A O 1 ATOM 2153 C CB . ASP A 1 275 ? 15.974 35.746 43.768 1.00 12.56 ? 356 ASP A CB 1 ATOM 2154 C CG . ASP A 1 275 ? 15.609 35.798 42.295 1.00 15.35 ? 356 ASP A CG 1 ATOM 2155 O OD1 . ASP A 1 275 ? 16.516 35.663 41.472 1.00 18.08 ? 356 ASP A OD1 1 ATOM 2156 O OD2 . ASP A 1 275 ? 14.443 35.980 41.967 1.00 15.41 ? 356 ASP A OD2 1 ATOM 2157 N N . GLY A 1 276 ? 18.163 38.877 43.786 1.00 12.40 ? 357 GLY A N 1 ATOM 2158 C CA . GLY A 1 276 ? 18.120 40.329 43.572 1.00 10.97 ? 357 GLY A CA 1 ATOM 2159 C C . GLY A 1 276 ? 17.207 41.044 44.563 1.00 11.83 ? 357 GLY A C 1 ATOM 2160 O O . GLY A 1 276 ? 17.436 40.993 45.767 1.00 13.08 ? 357 GLY A O 1 ATOM 2161 N N . VAL A 1 277 ? 16.128 41.660 44.099 1.00 11.82 ? 358 VAL A N 1 ATOM 2162 C CA . VAL A 1 277 ? 15.260 42.396 45.003 1.00 14.70 ? 358 VAL A CA 1 ATOM 2163 C C . VAL A 1 277 ? 14.397 41.386 45.795 1.00 14.75 ? 358 VAL A C 1 ATOM 2164 O O . VAL A 1 277 ? 14.164 41.556 46.996 1.00 15.41 ? 358 VAL A O 1 ATOM 2165 C CB . VAL A 1 277 ? 14.495 43.416 44.068 1.00 15.01 ? 358 VAL A CB 1 ATOM 2166 C CG1 . VAL A 1 277 ? 13.217 43.982 44.619 1.00 15.52 ? 358 VAL A CG1 1 ATOM 2167 C CG2 . VAL A 1 277 ? 15.376 44.640 43.995 1.00 14.02 ? 358 VAL A CG2 1 ATOM 2168 N N . ASN A 1 278 ? 14.110 40.219 45.180 1.00 16.36 ? 359 ASN A N 1 ATOM 2169 C CA . ASN A 1 278 ? 13.222 39.142 45.668 1.00 16.62 ? 359 ASN A CA 1 ATOM 2170 C C . ASN A 1 278 ? 14.027 38.246 46.608 1.00 16.20 ? 359 ASN A C 1 ATOM 2171 O O . ASN A 1 278 ? 14.066 37.031 46.383 1.00 18.80 ? 359 ASN A O 1 ATOM 2172 C CB . ASN A 1 278 ? 12.762 38.354 44.445 1.00 17.02 ? 359 ASN A CB 1 ATOM 2173 C CG . ASN A 1 278 ? 11.694 37.304 44.625 1.00 19.32 ? 359 ASN A CG 1 ATOM 2174 O OD1 . ASN A 1 278 ? 10.823 37.380 45.483 1.00 20.17 ? 359 ASN A OD1 1 ATOM 2175 N ND2 . ASN A 1 278 ? 11.624 36.346 43.729 1.00 19.21 ? 359 ASN A ND2 1 ATOM 2176 N N . THR A 1 279 ? 14.748 38.794 47.610 1.00 13.38 ? 360 THR A N 1 ATOM 2177 C CA . THR A 1 279 ? 15.608 37.986 48.454 1.00 10.43 ? 360 THR A CA 1 ATOM 2178 C C . THR A 1 279 ? 15.108 37.974 49.853 1.00 12.62 ? 360 THR A C 1 ATOM 2179 O O . THR A 1 279 ? 14.949 39.056 50.430 1.00 15.64 ? 360 THR A O 1 ATOM 2180 C CB . THR A 1 279 ? 17.025 38.526 48.489 1.00 10.35 ? 360 THR A CB 1 ATOM 2181 O OG1 . THR A 1 279 ? 17.579 38.353 47.176 1.00 9.81 ? 360 THR A OG1 1 ATOM 2182 C CG2 . THR A 1 279 ? 17.905 37.802 49.497 1.00 9.43 ? 360 THR A CG2 1 ATOM 2183 N N . TRP A 1 280 ? 14.964 36.761 50.398 1.00 13.56 ? 361 TRP A N 1 ATOM 2184 C CA . TRP A 1 280 ? 14.478 36.559 51.745 1.00 13.10 ? 361 TRP A CA 1 ATOM 2185 C C . TRP A 1 280 ? 15.468 35.691 52.553 1.00 13.06 ? 361 TRP A C 1 ATOM 2186 O O . TRP A 1 280 ? 15.961 34.670 52.032 1.00 12.43 ? 361 TRP A O 1 ATOM 2187 C CB . TRP A 1 280 ? 13.112 35.893 51.655 1.00 10.58 ? 361 TRP A CB 1 ATOM 2188 C CG . TRP A 1 280 ? 11.909 36.770 51.293 1.00 10.21 ? 361 TRP A CG 1 ATOM 2189 C CD1 . TRP A 1 280 ? 11.622 37.040 49.984 1.00 10.38 ? 361 TRP A CD1 1 ATOM 2190 C CD2 . TRP A 1 280 ? 10.935 37.251 52.161 1.00 10.77 ? 361 TRP A CD2 1 ATOM 2191 N NE1 . TRP A 1 280 ? 10.468 37.648 50.009 1.00 11.42 ? 361 TRP A NE1 1 ATOM 2192 C CE2 . TRP A 1 280 ? 10.037 37.791 51.255 1.00 9.33 ? 361 TRP A CE2 1 ATOM 2193 C CE3 . TRP A 1 280 ? 10.617 37.340 53.531 1.00 9.75 ? 361 TRP A CE3 1 ATOM 2194 C CZ2 . TRP A 1 280 ? 8.868 38.381 51.646 1.00 7.88 ? 361 TRP A CZ2 1 ATOM 2195 C CZ3 . TRP A 1 280 ? 9.436 37.944 53.943 1.00 6.39 ? 361 TRP A CZ3 1 ATOM 2196 C CH2 . TRP A 1 280 ? 8.581 38.451 53.002 1.00 7.22 ? 361 TRP A CH2 1 ATOM 2197 N N . LEU A 1 281 ? 15.801 36.092 53.794 1.00 12.90 ? 362 LEU A N 1 ATOM 2198 C CA . LEU A 1 281 ? 16.717 35.398 54.700 1.00 12.34 ? 362 LEU A CA 1 ATOM 2199 C C . LEU A 1 281 ? 15.930 34.890 55.895 1.00 12.38 ? 362 LEU A C 1 ATOM 2200 O O . LEU A 1 281 ? 15.102 35.614 56.469 1.00 11.96 ? 362 LEU A O 1 ATOM 2201 C CB . LEU A 1 281 ? 17.819 36.291 55.285 1.00 13.97 ? 362 LEU A CB 1 ATOM 2202 C CG . LEU A 1 281 ? 18.613 37.213 54.383 1.00 14.32 ? 362 LEU A CG 1 ATOM 2203 C CD1 . LEU A 1 281 ? 19.640 37.951 55.137 1.00 12.94 ? 362 LEU A CD1 1 ATOM 2204 C CD2 . LEU A 1 281 ? 19.349 36.390 53.378 1.00 17.22 ? 362 LEU A CD2 1 ATOM 2205 N N . GLY A 1 282 ? 16.161 33.630 56.270 1.00 11.13 ? 363 GLY A N 1 ATOM 2206 C CA . GLY A 1 282 ? 15.538 33.044 57.438 1.00 8.60 ? 363 GLY A CA 1 ATOM 2207 C C . GLY A 1 282 ? 16.505 33.081 58.618 1.00 7.77 ? 363 GLY A C 1 ATOM 2208 O O . GLY A 1 282 ? 17.718 33.028 58.419 1.00 6.07 ? 363 GLY A O 1 ATOM 2209 N N . ARG A 1 283 ? 16.100 33.213 59.878 1.00 9.08 ? 364 ARG A N 1 ATOM 2210 C CA . ARG A 1 283 ? 16.992 33.147 61.061 1.00 9.34 ? 364 ARG A CA 1 ATOM 2211 C C . ARG A 1 283 ? 16.271 32.884 62.411 1.00 11.33 ? 364 ARG A C 1 ATOM 2212 O O . ARG A 1 283 ? 15.048 33.059 62.522 1.00 9.13 ? 364 ARG A O 1 ATOM 2213 C CB . ARG A 1 283 ? 17.795 34.445 61.263 1.00 10.83 ? 364 ARG A CB 1 ATOM 2214 C CG . ARG A 1 283 ? 16.944 35.709 61.138 1.00 13.26 ? 364 ARG A CG 1 ATOM 2215 C CD . ARG A 1 283 ? 17.125 36.927 62.121 1.00 15.94 ? 364 ARG A CD 1 ATOM 2216 N NE . ARG A 1 283 ? 18.318 37.721 61.942 1.00 17.40 ? 364 ARG A NE 1 ATOM 2217 C CZ . ARG A 1 283 ? 18.431 39.036 62.190 1.00 17.86 ? 364 ARG A CZ 1 ATOM 2218 N NH1 . ARG A 1 283 ? 17.444 39.884 62.531 1.00 19.52 ? 364 ARG A NH1 1 ATOM 2219 N NH2 . ARG A 1 283 ? 19.635 39.539 62.020 1.00 16.04 ? 364 ARG A NH2 1 ATOM 2220 N N . THR A 1 284 ? 16.940 32.441 63.486 1.00 11.63 ? 365 THR A N 1 ATOM 2221 C CA . THR A 1 284 ? 16.349 32.318 64.818 1.00 12.56 ? 365 THR A CA 1 ATOM 2222 C C . THR A 1 284 ? 16.107 33.755 65.321 1.00 14.06 ? 365 THR A C 1 ATOM 2223 O O . THR A 1 284 ? 16.839 34.670 64.903 1.00 13.46 ? 365 THR A O 1 ATOM 2224 C CB . THR A 1 284 ? 17.339 31.551 65.746 1.00 11.12 ? 365 THR A CB 1 ATOM 2225 O OG1 . THR A 1 284 ? 18.574 32.228 65.626 1.00 14.46 ? 365 THR A OG1 1 ATOM 2226 C CG2 . THR A 1 284 ? 17.624 30.094 65.357 1.00 9.50 ? 365 THR A CG2 1 ATOM 2227 N N . ILE A 1 285 ? 15.092 34.018 66.164 1.00 14.29 ? 366 ILE A N 1 ATOM 2228 C CA . ILE A 1 285 ? 14.871 35.327 66.792 1.00 13.75 ? 366 ILE A CA 1 ATOM 2229 C C . ILE A 1 285 ? 15.872 35.451 67.949 1.00 12.21 ? 366 ILE A C 1 ATOM 2230 O O . ILE A 1 285 ? 16.560 36.458 68.056 1.00 13.15 ? 366 ILE A O 1 ATOM 2231 C CB . ILE A 1 285 ? 13.400 35.388 67.271 1.00 13.81 ? 366 ILE A CB 1 ATOM 2232 C CG1 . ILE A 1 285 ? 12.526 35.600 66.052 1.00 13.18 ? 366 ILE A CG1 1 ATOM 2233 C CG2 . ILE A 1 285 ? 13.177 36.513 68.300 1.00 15.90 ? 366 ILE A CG2 1 ATOM 2234 C CD1 . ILE A 1 285 ? 11.033 35.435 66.442 1.00 14.41 ? 366 ILE A CD1 1 ATOM 2235 N N . SER A 1 286 ? 15.975 34.467 68.836 1.00 11.69 ? 367 SER A N 1 ATOM 2236 C CA . SER A 1 286 ? 17.006 34.517 69.829 1.00 13.74 ? 367 SER A CA 1 ATOM 2237 C C . SER A 1 286 ? 18.424 34.644 69.250 1.00 13.12 ? 367 SER A C 1 ATOM 2238 O O . SER A 1 286 ? 18.873 33.783 68.509 1.00 15.00 ? 367 SER A O 1 ATOM 2239 C CB . SER A 1 286 ? 16.938 33.266 70.659 1.00 11.74 ? 367 SER A CB 1 ATOM 2240 O OG . SER A 1 286 ? 17.990 33.175 71.627 1.00 13.04 ? 367 SER A OG 1 ATOM 2241 N N . ARG A 1 287 ? 19.213 35.651 69.608 1.00 16.10 ? 368 ARG A N 1 ATOM 2242 C CA . ARG A 1 287 ? 20.638 35.710 69.243 1.00 20.02 ? 368 ARG A CA 1 ATOM 2243 C C . ARG A 1 287 ? 21.478 34.693 70.032 1.00 18.58 ? 368 ARG A C 1 ATOM 2244 O O . ARG A 1 287 ? 22.669 34.520 69.758 1.00 21.21 ? 368 ARG A O 1 ATOM 2245 C CB . ARG A 1 287 ? 21.266 37.059 69.552 1.00 23.40 ? 368 ARG A CB 1 ATOM 2246 C CG . ARG A 1 287 ? 20.753 38.310 68.857 1.00 27.52 ? 368 ARG A CG 1 ATOM 2247 C CD . ARG A 1 287 ? 21.266 39.570 69.590 1.00 29.83 ? 368 ARG A CD 1 ATOM 2248 N NE . ARG A 1 287 ? 22.689 39.437 69.887 1.00 32.87 ? 368 ARG A NE 1 ATOM 2249 C CZ . ARG A 1 287 ? 23.231 39.777 71.064 1.00 33.15 ? 368 ARG A CZ 1 ATOM 2250 N NH1 . ARG A 1 287 ? 22.529 40.386 72.032 1.00 33.83 ? 368 ARG A NH1 1 ATOM 2251 N NH2 . ARG A 1 287 ? 24.530 39.512 71.245 1.00 34.20 ? 368 ARG A NH2 1 ATOM 2252 N N . ALA A 1 288 ? 20.944 33.986 71.032 1.00 16.30 ? 369 ALA A N 1 ATOM 2253 C CA . ALA A 1 288 ? 21.771 33.124 71.867 1.00 15.12 ? 369 ALA A CA 1 ATOM 2254 C C . ALA A 1 288 ? 21.395 31.657 71.887 1.00 15.53 ? 369 ALA A C 1 ATOM 2255 O O . ALA A 1 288 ? 22.208 30.779 72.152 1.00 16.88 ? 369 ALA A O 1 ATOM 2256 C CB . ALA A 1 288 ? 21.738 33.634 73.300 1.00 12.61 ? 369 ALA A CB 1 ATOM 2257 N N . SER A 1 289 ? 20.172 31.379 71.535 1.00 17.99 ? 370 SER A N 1 ATOM 2258 C CA . SER A 1 289 ? 19.648 30.061 71.619 1.00 18.70 ? 370 SER A CA 1 ATOM 2259 C C . SER A 1 289 ? 18.923 29.786 70.319 1.00 17.74 ? 370 SER A C 1 ATOM 2260 O O . SER A 1 289 ? 18.539 30.729 69.635 1.00 17.52 ? 370 SER A O 1 ATOM 2261 C CB . SER A 1 289 ? 18.723 30.064 72.785 1.00 21.74 ? 370 SER A CB 1 ATOM 2262 O OG . SER A 1 289 ? 18.537 28.729 73.183 1.00 28.86 ? 370 SER A OG 1 ATOM 2263 N N . ARG A 1 290 ? 18.641 28.525 69.978 1.00 16.10 ? 371 ARG A N 1 ATOM 2264 C CA . ARG A 1 290 ? 17.894 28.166 68.789 1.00 14.83 ? 371 ARG A CA 1 ATOM 2265 C C . ARG A 1 290 ? 16.440 28.259 69.237 1.00 15.65 ? 371 ARG A C 1 ATOM 2266 O O . ARG A 1 290 ? 15.777 27.254 69.555 1.00 17.76 ? 371 ARG A O 1 ATOM 2267 C CB . ARG A 1 290 ? 18.179 26.706 68.315 1.00 13.96 ? 371 ARG A CB 1 ATOM 2268 C CG . ARG A 1 290 ? 19.649 26.435 68.041 1.00 14.87 ? 371 ARG A CG 1 ATOM 2269 C CD . ARG A 1 290 ? 19.897 24.978 67.741 1.00 15.61 ? 371 ARG A CD 1 ATOM 2270 N NE . ARG A 1 290 ? 21.226 24.765 67.162 1.00 16.38 ? 371 ARG A NE 1 ATOM 2271 C CZ . ARG A 1 290 ? 21.826 23.556 67.152 1.00 15.48 ? 371 ARG A CZ 1 ATOM 2272 N NH1 . ARG A 1 290 ? 21.182 22.501 67.644 1.00 12.41 ? 371 ARG A NH1 1 ATOM 2273 N NH2 . ARG A 1 290 ? 23.034 23.389 66.595 1.00 14.36 ? 371 ARG A NH2 1 ATOM 2274 N N . SER A 1 291 ? 15.948 29.502 69.279 1.00 15.00 ? 372 SER A N 1 ATOM 2275 C CA . SER A 1 291 ? 14.565 29.711 69.627 1.00 14.38 ? 372 SER A CA 1 ATOM 2276 C C . SER A 1 291 ? 13.943 30.815 68.780 1.00 10.74 ? 372 SER A C 1 ATOM 2277 O O . SER A 1 291 ? 14.596 31.827 68.430 1.00 7.15 ? 372 SER A O 1 ATOM 2278 C CB . SER A 1 291 ? 14.507 30.008 71.136 1.00 16.21 ? 372 SER A CB 1 ATOM 2279 O OG . SER A 1 291 ? 14.857 31.323 71.520 1.00 18.83 ? 372 SER A OG 1 ATOM 2280 N N . GLY A 1 292 ? 12.661 30.576 68.426 1.00 7.21 ? 373 GLY A N 1 ATOM 2281 C CA . GLY A 1 292 ? 11.972 31.477 67.548 1.00 7.86 ? 373 GLY A CA 1 ATOM 2282 C C . GLY A 1 292 ? 12.451 31.292 66.105 1.00 8.73 ? 373 GLY A C 1 ATOM 2283 O O . GLY A 1 292 ? 13.489 30.671 65.843 1.00 12.78 ? 373 GLY A O 1 ATOM 2284 N N . TYR A 1 293 ? 11.736 31.808 65.115 1.00 5.52 ? 374 TYR A N 1 ATOM 2285 C CA . TYR A 1 293 ? 12.166 31.758 63.734 1.00 5.17 ? 374 TYR A CA 1 ATOM 2286 C C . TYR A 1 293 ? 11.441 32.841 62.922 1.00 5.68 ? 374 TYR A C 1 ATOM 2287 O O . TYR A 1 293 ? 10.219 33.069 62.982 1.00 4.93 ? 374 TYR A O 1 ATOM 2288 C CB . TYR A 1 293 ? 11.885 30.382 63.086 1.00 3.22 ? 374 TYR A CB 1 ATOM 2289 C CG . TYR A 1 293 ? 12.832 30.107 61.920 1.00 2.47 ? 374 TYR A CG 1 ATOM 2290 C CD1 . TYR A 1 293 ? 14.112 29.680 62.192 1.00 3.04 ? 374 TYR A CD1 1 ATOM 2291 C CD2 . TYR A 1 293 ? 12.433 30.372 60.601 1.00 3.40 ? 374 TYR A CD2 1 ATOM 2292 C CE1 . TYR A 1 293 ? 14.928 29.559 61.101 1.00 3.86 ? 374 TYR A CE1 1 ATOM 2293 C CE2 . TYR A 1 293 ? 13.252 30.235 59.501 1.00 2.26 ? 374 TYR A CE2 1 ATOM 2294 C CZ . TYR A 1 293 ? 14.519 29.837 59.780 1.00 3.35 ? 374 TYR A CZ 1 ATOM 2295 O OH . TYR A 1 293 ? 15.426 29.675 58.746 1.00 2.66 ? 374 TYR A OH 1 ATOM 2296 N N . GLU A 1 294 ? 12.223 33.545 62.149 1.00 4.85 ? 375 GLU A N 1 ATOM 2297 C CA . GLU A 1 294 ? 11.669 34.557 61.292 1.00 6.49 ? 375 GLU A CA 1 ATOM 2298 C C . GLU A 1 294 ? 12.266 34.595 59.919 1.00 7.52 ? 375 GLU A C 1 ATOM 2299 O O . GLU A 1 294 ? 13.452 34.247 59.747 1.00 8.46 ? 375 GLU A O 1 ATOM 2300 C CB . GLU A 1 294 ? 11.867 35.864 61.953 1.00 9.08 ? 375 GLU A CB 1 ATOM 2301 C CG . GLU A 1 294 ? 13.304 36.309 62.187 1.00 10.57 ? 375 GLU A CG 1 ATOM 2302 C CD . GLU A 1 294 ? 13.395 37.639 62.906 1.00 13.16 ? 375 GLU A CD 1 ATOM 2303 O OE1 . GLU A 1 294 ? 12.360 38.254 63.208 1.00 13.56 ? 375 GLU A OE1 1 ATOM 2304 O OE2 . GLU A 1 294 ? 14.523 38.043 63.172 1.00 15.05 ? 375 GLU A OE2 1 ATOM 2305 N N . MET A 1 295 ? 11.395 35.040 59.025 1.00 8.87 ? 376 MET A N 1 ATOM 2306 C CA . MET A 1 295 ? 11.786 35.265 57.647 1.00 11.48 ? 376 MET A CA 1 ATOM 2307 C C . MET A 1 295 ? 11.837 36.797 57.447 1.00 12.69 ? 376 MET A C 1 ATOM 2308 O O . MET A 1 295 ? 10.953 37.536 57.886 1.00 13.03 ? 376 MET A O 1 ATOM 2309 C CB . MET A 1 295 ? 10.774 34.642 56.667 1.00 13.42 ? 376 MET A CB 1 ATOM 2310 C CG . MET A 1 295 ? 10.828 33.105 56.555 1.00 14.06 ? 376 MET A CG 1 ATOM 2311 S SD . MET A 1 295 ? 12.461 32.516 56.066 1.00 16.33 ? 376 MET A SD 1 ATOM 2312 C CE . MET A 1 295 ? 12.548 33.107 54.397 1.00 13.02 ? 376 MET A CE 1 ATOM 2313 N N . LEU A 1 296 ? 12.897 37.318 56.835 1.00 13.49 ? 377 LEU A N 1 ATOM 2314 C CA . LEU A 1 296 ? 13.124 38.749 56.600 1.00 12.65 ? 377 LEU A CA 1 ATOM 2315 C C . LEU A 1 296 ? 13.486 39.021 55.144 1.00 9.67 ? 377 LEU A C 1 ATOM 2316 O O . LEU A 1 296 ? 14.359 38.353 54.586 1.00 7.94 ? 377 LEU A O 1 ATOM 2317 C CB . LEU A 1 296 ? 14.264 39.235 57.516 1.00 12.11 ? 377 LEU A CB 1 ATOM 2318 C CG . LEU A 1 296 ? 13.998 39.287 58.998 1.00 12.53 ? 377 LEU A CG 1 ATOM 2319 C CD1 . LEU A 1 296 ? 15.285 39.578 59.754 1.00 11.12 ? 377 LEU A CD1 1 ATOM 2320 C CD2 . LEU A 1 296 ? 13.031 40.396 59.283 1.00 12.80 ? 377 LEU A CD2 1 ATOM 2321 N N . LYS A 1 297 ? 12.809 39.929 54.462 1.00 10.65 ? 378 LYS A N 1 ATOM 2322 C CA . LYS A 1 297 ? 13.154 40.261 53.069 1.00 12.62 ? 378 LYS A CA 1 ATOM 2323 C C . LYS A 1 297 ? 14.249 41.342 53.119 1.00 15.37 ? 378 LYS A C 1 ATOM 2324 O O . LYS A 1 297 ? 14.043 42.404 53.729 1.00 18.47 ? 378 LYS A O 1 ATOM 2325 C CB . LYS A 1 297 ? 11.910 40.778 52.353 1.00 8.20 ? 378 LYS A CB 1 ATOM 2326 C CG . LYS A 1 297 ? 12.184 41.107 50.930 1.00 7.95 ? 378 LYS A CG 1 ATOM 2327 C CD . LYS A 1 297 ? 10.969 41.819 50.371 1.00 9.92 ? 378 LYS A CD 1 ATOM 2328 C CE . LYS A 1 297 ? 11.263 42.142 48.895 1.00 13.51 ? 378 LYS A CE 1 ATOM 2329 N NZ . LYS A 1 297 ? 10.164 42.803 48.179 1.00 15.72 ? 378 LYS A NZ 1 ATOM 2330 N N . VAL A 1 298 ? 15.430 41.106 52.553 1.00 15.21 ? 379 VAL A N 1 ATOM 2331 C CA . VAL A 1 298 ? 16.563 42.014 52.642 1.00 14.70 ? 379 VAL A CA 1 ATOM 2332 C C . VAL A 1 298 ? 16.976 42.046 51.196 1.00 14.71 ? 379 VAL A C 1 ATOM 2333 O O . VAL A 1 298 ? 17.674 41.123 50.737 1.00 14.83 ? 379 VAL A O 1 ATOM 2334 C CB . VAL A 1 298 ? 17.675 41.392 53.527 1.00 13.98 ? 379 VAL A CB 1 ATOM 2335 C CG1 . VAL A 1 298 ? 18.800 42.382 53.643 1.00 13.89 ? 379 VAL A CG1 1 ATOM 2336 C CG2 . VAL A 1 298 ? 17.149 41.022 54.921 1.00 14.65 ? 379 VAL A CG2 1 ATOM 2337 N N . PRO A 1 299 ? 16.531 43.062 50.435 1.00 13.78 ? 380 PRO A N 1 ATOM 2338 C CA . PRO A 1 299 ? 16.842 43.207 49.014 1.00 14.09 ? 380 PRO A CA 1 ATOM 2339 C C . PRO A 1 299 ? 18.380 43.200 48.764 1.00 14.05 ? 380 PRO A C 1 ATOM 2340 O O . PRO A 1 299 ? 19.154 43.890 49.447 1.00 16.30 ? 380 PRO A O 1 ATOM 2341 C CB . PRO A 1 299 ? 16.114 44.518 48.635 1.00 12.99 ? 380 PRO A CB 1 ATOM 2342 C CG . PRO A 1 299 ? 14.960 44.529 49.569 1.00 10.74 ? 380 PRO A CG 1 ATOM 2343 C CD . PRO A 1 299 ? 15.607 44.109 50.871 1.00 12.79 ? 380 PRO A CD 1 ATOM 2344 N N . ASN A 1 300 ? 18.857 42.362 47.848 1.00 11.70 ? 381 ASN A N 1 ATOM 2345 C CA . ASN A 1 300 ? 20.260 42.292 47.448 1.00 10.40 ? 381 ASN A CA 1 ATOM 2346 C C . ASN A 1 300 ? 21.265 41.955 48.541 1.00 8.71 ? 381 ASN A C 1 ATOM 2347 O O . ASN A 1 300 ? 22.450 42.282 48.443 1.00 10.71 ? 381 ASN A O 1 ATOM 2348 C CB . ASN A 1 300 ? 20.692 43.598 46.822 1.00 11.34 ? 381 ASN A CB 1 ATOM 2349 C CG . ASN A 1 300 ? 20.002 43.876 45.517 1.00 13.14 ? 381 ASN A CG 1 ATOM 2350 O OD1 . ASN A 1 300 ? 19.994 43.086 44.573 1.00 16.48 ? 381 ASN A OD1 1 ATOM 2351 N ND2 . ASN A 1 300 ? 19.427 45.071 45.461 1.00 15.04 ? 381 ASN A ND2 1 ATOM 2352 N N . ALA A 1 301 ? 20.864 41.118 49.501 1.00 11.13 ? 382 ALA A N 1 ATOM 2353 C CA . ALA A 1 301 ? 21.635 40.772 50.672 1.00 11.34 ? 382 ALA A CA 1 ATOM 2354 C C . ALA A 1 301 ? 23.040 40.278 50.382 1.00 13.43 ? 382 ALA A C 1 ATOM 2355 O O . ALA A 1 301 ? 23.977 40.525 51.136 1.00 11.90 ? 382 ALA A O 1 ATOM 2356 C CB . ALA A 1 301 ? 20.886 39.704 51.433 1.00 11.18 ? 382 ALA A CB 1 ATOM 2357 N N . LEU A 1 302 ? 23.171 39.577 49.265 1.00 15.27 ? 383 LEU A N 1 ATOM 2358 C CA . LEU A 1 302 ? 24.428 38.960 48.876 1.00 15.81 ? 383 LEU A CA 1 ATOM 2359 C C . LEU A 1 302 ? 25.526 39.961 48.502 1.00 16.38 ? 383 LEU A C 1 ATOM 2360 O O . LEU A 1 302 ? 26.699 39.682 48.721 1.00 15.13 ? 383 LEU A O 1 ATOM 2361 C CB . LEU A 1 302 ? 24.208 38.002 47.663 1.00 12.25 ? 383 LEU A CB 1 ATOM 2362 C CG . LEU A 1 302 ? 25.434 37.379 46.975 1.00 12.47 ? 383 LEU A CG 1 ATOM 2363 C CD1 . LEU A 1 302 ? 26.113 36.387 47.904 1.00 10.77 ? 383 LEU A CD1 1 ATOM 2364 C CD2 . LEU A 1 302 ? 24.997 36.656 45.706 1.00 12.75 ? 383 LEU A CD2 1 ATOM 2365 N N . THR A 1 303 ? 25.138 41.090 47.917 1.00 16.21 ? 384 THR A N 1 ATOM 2366 C CA . THR A 1 303 ? 26.061 42.067 47.359 1.00 15.55 ? 384 THR A CA 1 ATOM 2367 C C . THR A 1 303 ? 26.111 43.391 48.090 1.00 16.22 ? 384 THR A C 1 ATOM 2368 O O . THR A 1 303 ? 27.154 43.992 48.296 1.00 17.58 ? 384 THR A O 1 ATOM 2369 C CB . THR A 1 303 ? 25.656 42.208 45.882 1.00 14.21 ? 384 THR A CB 1 ATOM 2370 O OG1 . THR A 1 303 ? 24.249 42.357 45.734 1.00 14.91 ? 384 THR A OG1 1 ATOM 2371 C CG2 . THR A 1 303 ? 26.022 40.932 45.158 1.00 15.37 ? 384 THR A CG2 1 ATOM 2372 N N . ASP A 1 304 ? 24.968 43.881 48.540 1.00 18.44 ? 385 ASP A N 1 ATOM 2373 C CA . ASP A 1 304 ? 24.906 45.145 49.227 1.00 18.49 ? 385 ASP A CA 1 ATOM 2374 C C . ASP A 1 304 ? 25.287 44.956 50.682 1.00 18.21 ? 385 ASP A C 1 ATOM 2375 O O . ASP A 1 304 ? 24.480 44.499 51.483 1.00 17.53 ? 385 ASP A O 1 ATOM 2376 C CB . ASP A 1 304 ? 23.497 45.631 49.029 1.00 20.90 ? 385 ASP A CB 1 ATOM 2377 C CG . ASP A 1 304 ? 23.121 46.992 49.621 1.00 23.62 ? 385 ASP A CG 1 ATOM 2378 O OD1 . ASP A 1 304 ? 23.675 47.442 50.633 1.00 24.91 ? 385 ASP A OD1 1 ATOM 2379 O OD2 . ASP A 1 304 ? 22.187 47.601 49.090 1.00 23.48 ? 385 ASP A OD2 1 ATOM 2380 N N . ASP A 1 305 ? 26.453 45.427 51.103 1.00 17.61 ? 386 ASP A N 1 ATOM 2381 C CA . ASP A 1 305 ? 26.878 45.244 52.467 1.00 18.51 ? 386 ASP A CA 1 ATOM 2382 C C . ASP A 1 305 ? 26.260 46.211 53.499 1.00 18.05 ? 386 ASP A C 1 ATOM 2383 O O . ASP A 1 305 ? 26.640 46.256 54.669 1.00 17.50 ? 386 ASP A O 1 ATOM 2384 C CB . ASP A 1 305 ? 28.405 45.301 52.457 1.00 18.88 ? 386 ASP A CB 1 ATOM 2385 C CG . ASP A 1 305 ? 29.072 46.658 52.278 1.00 20.78 ? 386 ASP A CG 1 ATOM 2386 O OD1 . ASP A 1 305 ? 28.479 47.606 51.761 1.00 19.99 ? 386 ASP A OD1 1 ATOM 2387 O OD2 . ASP A 1 305 ? 30.234 46.753 52.669 1.00 24.26 ? 386 ASP A OD2 1 ATOM 2388 N N . LYS A 1 306 ? 25.298 47.028 53.123 1.00 18.41 ? 387 LYS A N 1 ATOM 2389 C CA . LYS A 1 306 ? 24.599 47.870 54.068 1.00 20.30 ? 387 LYS A CA 1 ATOM 2390 C C . LYS A 1 306 ? 23.061 47.672 54.044 1.00 21.14 ? 387 LYS A C 1 ATOM 2391 O O . LYS A 1 306 ? 22.297 48.524 54.515 1.00 20.56 ? 387 LYS A O 1 ATOM 2392 C CB . LYS A 1 306 ? 24.973 49.300 53.748 1.00 23.63 ? 387 LYS A CB 1 ATOM 2393 C CG . LYS A 1 306 ? 26.299 49.720 54.351 1.00 28.56 ? 387 LYS A CG 1 ATOM 2394 C CD . LYS A 1 306 ? 26.695 51.173 54.085 1.00 34.04 ? 387 LYS A CD 1 ATOM 2395 C CE . LYS A 1 306 ? 27.280 51.302 52.680 1.00 37.37 ? 387 LYS A CE 1 ATOM 2396 N NZ . LYS A 1 306 ? 27.944 52.590 52.548 1.00 41.03 ? 387 LYS A NZ 1 ATOM 2397 N N . SER A 1 307 ? 22.550 46.554 53.483 1.00 19.76 ? 388 SER A N 1 ATOM 2398 C CA . SER A 1 307 ? 21.129 46.204 53.323 1.00 18.10 ? 388 SER A CA 1 ATOM 2399 C C . SER A 1 307 ? 20.385 45.767 54.615 1.00 17.24 ? 388 SER A C 1 ATOM 2400 O O . SER A 1 307 ? 20.822 44.877 55.355 1.00 15.83 ? 388 SER A O 1 ATOM 2401 C CB . SER A 1 307 ? 21.102 45.103 52.272 1.00 17.58 ? 388 SER A CB 1 ATOM 2402 O OG . SER A 1 307 ? 22.116 44.177 52.680 1.00 18.31 ? 388 SER A OG 1 ATOM 2403 N N . LYS A 1 308 ? 19.252 46.414 54.883 1.00 15.80 ? 389 LYS A N 1 ATOM 2404 C CA . LYS A 1 308 ? 18.406 46.260 56.055 1.00 16.58 ? 389 LYS A CA 1 ATOM 2405 C C . LYS A 1 308 ? 17.035 45.694 55.615 1.00 16.72 ? 389 LYS A C 1 ATOM 2406 O O . LYS A 1 308 ? 16.699 45.797 54.431 1.00 16.58 ? 389 LYS A O 1 ATOM 2407 C CB . LYS A 1 308 ? 18.200 47.620 56.733 0.02 15.72 ? 389 LYS A CB 1 ATOM 2408 C CG . LYS A 1 308 ? 19.444 48.355 57.210 0.02 15.27 ? 389 LYS A CG 1 ATOM 2409 C CD . LYS A 1 308 ? 20.278 47.540 58.191 0.02 14.87 ? 389 LYS A CD 1 ATOM 2410 C CE . LYS A 1 308 ? 21.488 48.343 58.656 0.02 14.60 ? 389 LYS A CE 1 ATOM 2411 N NZ . LYS A 1 308 ? 22.399 48.652 57.568 0.02 14.37 ? 389 LYS A NZ 1 ATOM 2412 N N . PRO A 1 309 ? 16.192 45.047 56.449 1.00 15.17 ? 390 PRO A N 1 ATOM 2413 C CA . PRO A 1 309 ? 14.986 44.372 56.006 1.00 12.79 ? 390 PRO A CA 1 ATOM 2414 C C . PRO A 1 309 ? 13.909 45.306 55.471 1.00 15.11 ? 390 PRO A C 1 ATOM 2415 O O . PRO A 1 309 ? 13.817 46.458 55.878 1.00 16.48 ? 390 PRO A O 1 ATOM 2416 C CB . PRO A 1 309 ? 14.546 43.620 57.232 1.00 13.44 ? 390 PRO A CB 1 ATOM 2417 C CG . PRO A 1 309 ? 15.758 43.494 58.120 1.00 11.07 ? 390 PRO A CG 1 ATOM 2418 C CD . PRO A 1 309 ? 16.387 44.836 57.897 1.00 11.49 ? 390 PRO A CD 1 ATOM 2419 N N . THR A 1 310 ? 12.977 44.812 54.677 1.00 13.70 ? 391 THR A N 1 ATOM 2420 C CA . THR A 1 310 ? 11.975 45.644 54.104 1.00 12.03 ? 391 THR A CA 1 ATOM 2421 C C . THR A 1 310 ? 10.566 45.158 54.421 1.00 11.35 ? 391 THR A C 1 ATOM 2422 O O . THR A 1 310 ? 9.611 45.911 54.264 1.00 9.73 ? 391 THR A O 1 ATOM 2423 C CB . THR A 1 310 ? 12.403 45.622 52.649 1.00 12.46 ? 391 THR A CB 1 ATOM 2424 O OG1 . THR A 1 310 ? 12.937 46.931 52.428 1.00 16.61 ? 391 THR A OG1 1 ATOM 2425 C CG2 . THR A 1 310 ? 11.333 45.267 51.662 1.00 10.91 ? 391 THR A CG2 1 ATOM 2426 N N . GLN A 1 311 ? 10.421 43.913 54.910 1.00 10.89 ? 392 GLN A N 1 ATOM 2427 C CA . GLN A 1 311 ? 9.140 43.205 55.092 1.00 9.14 ? 392 GLN A CA 1 ATOM 2428 C C . GLN A 1 311 ? 9.566 41.998 55.936 1.00 7.80 ? 392 GLN A C 1 ATOM 2429 O O . GLN A 1 311 ? 10.755 41.633 55.894 1.00 7.41 ? 392 GLN A O 1 ATOM 2430 C CB . GLN A 1 311 ? 8.607 42.738 53.705 1.00 9.97 ? 392 GLN A CB 1 ATOM 2431 C CG . GLN A 1 311 ? 7.087 42.500 53.700 1.00 11.80 ? 392 GLN A CG 1 ATOM 2432 C CD . GLN A 1 311 ? 6.465 41.631 52.597 1.00 12.81 ? 392 GLN A CD 1 ATOM 2433 O OE1 . GLN A 1 311 ? 5.956 40.580 52.974 1.00 13.75 ? 392 GLN A OE1 1 ATOM 2434 N NE2 . GLN A 1 311 ? 6.310 41.919 51.301 1.00 12.59 ? 392 GLN A NE2 1 ATOM 2435 N N . GLY A 1 312 ? 8.718 41.330 56.705 1.00 10.02 ? 394 GLY A N 1 ATOM 2436 C CA . GLY A 1 312 ? 9.107 40.141 57.458 1.00 9.53 ? 394 GLY A CA 1 ATOM 2437 C C . GLY A 1 312 ? 7.899 39.233 57.681 1.00 11.65 ? 394 GLY A C 1 ATOM 2438 O O . GLY A 1 312 ? 6.801 39.616 57.258 1.00 11.14 ? 394 GLY A O 1 ATOM 2439 N N . GLN A 1 313 ? 8.076 38.046 58.260 1.00 12.45 ? 395 GLN A N 1 ATOM 2440 C CA . GLN A 1 313 ? 7.018 37.139 58.629 1.00 14.81 ? 395 GLN A CA 1 ATOM 2441 C C . GLN A 1 313 ? 7.590 36.229 59.702 1.00 16.03 ? 395 GLN A C 1 ATOM 2442 O O . GLN A 1 313 ? 8.695 35.675 59.512 1.00 15.62 ? 395 GLN A O 1 ATOM 2443 C CB . GLN A 1 313 ? 6.613 36.284 57.461 1.00 16.21 ? 395 GLN A CB 1 ATOM 2444 C CG . GLN A 1 313 ? 5.170 35.881 57.670 1.00 18.40 ? 395 GLN A CG 1 ATOM 2445 C CD . GLN A 1 313 ? 4.438 35.547 56.377 1.00 19.25 ? 395 GLN A CD 1 ATOM 2446 O OE1 . GLN A 1 313 ? 4.610 34.437 55.884 1.00 19.11 ? 395 GLN A OE1 1 ATOM 2447 N NE2 . GLN A 1 313 ? 3.630 36.469 55.774 1.00 21.22 ? 395 GLN A NE2 1 ATOM 2448 N N . THR A 1 314 ? 6.857 36.121 60.820 1.00 15.73 ? 396 THR A N 1 ATOM 2449 C CA . THR A 1 314 ? 7.254 35.310 61.971 1.00 14.83 ? 396 THR A CA 1 ATOM 2450 C C . THR A 1 314 ? 6.714 33.910 61.787 1.00 13.99 ? 396 THR A C 1 ATOM 2451 O O . THR A 1 314 ? 5.531 33.707 61.522 1.00 13.51 ? 396 THR A O 1 ATOM 2452 C CB . THR A 1 314 ? 6.677 35.900 63.258 1.00 15.25 ? 396 THR A CB 1 ATOM 2453 O OG1 . THR A 1 314 ? 7.110 37.242 63.213 1.00 17.44 ? 396 THR A OG1 1 ATOM 2454 C CG2 . THR A 1 314 ? 7.136 35.259 64.551 1.00 13.39 ? 396 THR A CG2 1 ATOM 2455 N N . ILE A 1 315 ? 7.600 32.940 61.891 1.00 14.08 ? 397 ILE A N 1 ATOM 2456 C CA . ILE A 1 315 ? 7.220 31.550 61.677 1.00 12.28 ? 397 ILE A CA 1 ATOM 2457 C C . ILE A 1 315 ? 6.991 30.819 63.003 1.00 11.32 ? 397 ILE A C 1 ATOM 2458 O O . ILE A 1 315 ? 5.986 30.135 63.217 1.00 12.06 ? 397 ILE A O 1 ATOM 2459 C CB . ILE A 1 315 ? 8.364 30.908 60.843 1.00 11.28 ? 397 ILE A CB 1 ATOM 2460 C CG1 . ILE A 1 315 ? 8.709 31.669 59.579 1.00 8.86 ? 397 ILE A CG1 1 ATOM 2461 C CG2 . ILE A 1 315 ? 7.903 29.545 60.471 1.00 11.52 ? 397 ILE A CG2 1 ATOM 2462 C CD1 . ILE A 1 315 ? 7.558 32.168 58.675 1.00 7.70 ? 397 ILE A CD1 1 ATOM 2463 N N . VAL A 1 316 ? 7.854 31.032 63.992 1.00 8.10 ? 398 VAL A N 1 ATOM 2464 C CA . VAL A 1 316 ? 7.803 30.386 65.309 1.00 7.21 ? 398 VAL A CA 1 ATOM 2465 C C . VAL A 1 316 ? 8.151 31.530 66.256 1.00 9.75 ? 398 VAL A C 1 ATOM 2466 O O . VAL A 1 316 ? 9.074 32.301 65.953 1.00 13.07 ? 398 VAL A O 1 ATOM 2467 C CB . VAL A 1 316 ? 8.869 29.189 65.421 1.00 6.61 ? 398 VAL A CB 1 ATOM 2468 C CG1 . VAL A 1 316 ? 8.872 28.470 66.791 1.00 2.72 ? 398 VAL A CG1 1 ATOM 2469 C CG2 . VAL A 1 316 ? 8.476 28.104 64.412 1.00 2.85 ? 398 VAL A CG2 1 ATOM 2470 N N . LEU A 1 317 ? 7.464 31.708 67.401 1.00 12.67 ? 399 LEU A N 1 ATOM 2471 C CA . LEU A 1 317 ? 7.686 32.859 68.299 1.00 11.32 ? 399 LEU A CA 1 ATOM 2472 C C . LEU A 1 317 ? 8.900 32.538 69.150 1.00 11.83 ? 399 LEU A C 1 ATOM 2473 O O . LEU A 1 317 ? 9.240 31.356 69.343 1.00 10.66 ? 399 LEU A O 1 ATOM 2474 C CB . LEU A 1 317 ? 6.493 33.111 69.251 1.00 9.15 ? 399 LEU A CB 1 ATOM 2475 C CG . LEU A 1 317 ? 5.155 33.507 68.625 1.00 10.24 ? 399 LEU A CG 1 ATOM 2476 C CD1 . LEU A 1 317 ? 4.167 33.671 69.751 1.00 10.69 ? 399 LEU A CD1 1 ATOM 2477 C CD2 . LEU A 1 317 ? 5.236 34.810 67.828 1.00 9.36 ? 399 LEU A CD2 1 ATOM 2478 N N . ASN A 1 318 ? 9.466 33.544 69.812 1.00 14.80 ? 400 ASN A N 1 ATOM 2479 C CA . ASN A 1 318 ? 10.706 33.362 70.564 1.00 15.72 ? 400 ASN A CA 1 ATOM 2480 C C . ASN A 1 318 ? 10.624 32.510 71.810 1.00 15.63 ? 400 ASN A C 1 ATOM 2481 O O . ASN A 1 318 ? 11.648 32.101 72.349 1.00 17.15 ? 400 ASN A O 1 ATOM 2482 C CB . ASN A 1 318 ? 11.282 34.688 70.978 1.00 18.48 ? 400 ASN A CB 1 ATOM 2483 C CG . ASN A 1 318 ? 12.774 34.610 71.271 1.00 21.91 ? 400 ASN A CG 1 ATOM 2484 O OD1 . ASN A 1 318 ? 13.327 35.531 71.874 1.00 25.08 ? 400 ASN A OD1 1 ATOM 2485 N ND2 . ASN A 1 318 ? 13.556 33.623 70.816 1.00 21.13 ? 400 ASN A ND2 1 ATOM 2486 N N . THR A 1 319 ? 9.430 32.169 72.226 1.00 15.81 ? 401 THR A N 1 ATOM 2487 C CA . THR A 1 319 ? 9.253 31.383 73.401 1.00 16.47 ? 401 THR A CA 1 ATOM 2488 C C . THR A 1 319 ? 9.221 29.907 73.051 1.00 17.72 ? 401 THR A C 1 ATOM 2489 O O . THR A 1 319 ? 9.108 29.056 73.956 1.00 18.41 ? 401 THR A O 1 ATOM 2490 C CB . THR A 1 319 ? 7.959 31.830 74.067 1.00 16.56 ? 401 THR A CB 1 ATOM 2491 O OG1 . THR A 1 319 ? 7.026 32.237 73.070 1.00 17.63 ? 401 THR A OG1 1 ATOM 2492 C CG2 . THR A 1 319 ? 8.208 33.025 74.967 1.00 16.29 ? 401 THR A CG2 1 ATOM 2493 N N . ASP A 1 320 ? 9.275 29.557 71.762 1.00 16.55 ? 402 ASP A N 1 ATOM 2494 C CA . ASP A 1 320 ? 9.247 28.147 71.431 1.00 16.12 ? 402 ASP A CA 1 ATOM 2495 C C . ASP A 1 320 ? 10.487 27.941 70.626 1.00 15.18 ? 402 ASP A C 1 ATOM 2496 O O . ASP A 1 320 ? 11.077 28.852 70.041 1.00 14.84 ? 402 ASP A O 1 ATOM 2497 C CB . ASP A 1 320 ? 8.043 27.724 70.594 1.00 18.34 ? 402 ASP A CB 1 ATOM 2498 C CG . ASP A 1 320 ? 6.691 28.145 71.153 1.00 20.15 ? 402 ASP A CG 1 ATOM 2499 O OD1 . ASP A 1 320 ? 6.295 27.724 72.229 1.00 19.74 ? 402 ASP A OD1 1 ATOM 2500 O OD2 . ASP A 1 320 ? 6.010 28.917 70.480 1.00 22.01 ? 402 ASP A OD2 1 ATOM 2501 N N . TRP A 1 321 ? 10.927 26.716 70.796 1.00 15.94 ? 403 TRP A N 1 ATOM 2502 C CA . TRP A 1 321 ? 12.084 26.120 70.174 1.00 14.53 ? 403 TRP A CA 1 ATOM 2503 C C . TRP A 1 321 ? 11.968 25.879 68.671 1.00 13.31 ? 403 TRP A C 1 ATOM 2504 O O . TRP A 1 321 ? 10.901 25.579 68.107 1.00 12.33 ? 403 TRP A O 1 ATOM 2505 C CB . TRP A 1 321 ? 12.338 24.809 70.911 1.00 15.56 ? 403 TRP A CB 1 ATOM 2506 C CG . TRP A 1 321 ? 12.490 24.996 72.416 1.00 16.53 ? 403 TRP A CG 1 ATOM 2507 C CD1 . TRP A 1 321 ? 11.595 24.402 73.273 1.00 17.11 ? 403 TRP A CD1 1 ATOM 2508 C CD2 . TRP A 1 321 ? 13.470 25.736 73.057 1.00 18.13 ? 403 TRP A CD2 1 ATOM 2509 N NE1 . TRP A 1 321 ? 12.000 24.759 74.466 1.00 18.46 ? 403 TRP A NE1 1 ATOM 2510 C CE2 . TRP A 1 321 ? 13.105 25.548 74.387 1.00 18.25 ? 403 TRP A CE2 1 ATOM 2511 C CE3 . TRP A 1 321 ? 14.567 26.516 72.713 1.00 16.87 ? 403 TRP A CE3 1 ATOM 2512 C CZ2 . TRP A 1 321 ? 13.840 26.149 75.390 1.00 18.91 ? 403 TRP A CZ2 1 ATOM 2513 C CZ3 . TRP A 1 321 ? 15.291 27.105 73.715 1.00 17.27 ? 403 TRP A CZ3 1 ATOM 2514 C CH2 . TRP A 1 321 ? 14.925 26.921 75.032 1.00 16.97 ? 403 TRP A CH2 1 ATOM 2515 N N . SER A 1 322 ? 13.109 26.085 68.034 1.00 12.57 ? 404 SER A N 1 ATOM 2516 C CA . SER A 1 322 ? 13.256 25.767 66.646 1.00 9.87 ? 404 SER A CA 1 ATOM 2517 C C . SER A 1 322 ? 14.489 24.888 66.419 1.00 9.64 ? 404 SER A C 1 ATOM 2518 O O . SER A 1 322 ? 14.631 23.877 67.106 1.00 13.49 ? 404 SER A O 1 ATOM 2519 C CB . SER A 1 322 ? 13.307 27.084 65.878 1.00 8.45 ? 404 SER A CB 1 ATOM 2520 O OG . SER A 1 322 ? 14.483 27.820 66.153 1.00 9.38 ? 404 SER A OG 1 ATOM 2521 N N . GLY A 1 323 ? 15.442 25.160 65.553 1.00 9.05 ? 405 GLY A N 1 ATOM 2522 C CA . GLY A 1 323 ? 16.481 24.198 65.240 1.00 9.23 ? 405 GLY A CA 1 ATOM 2523 C C . GLY A 1 323 ? 16.923 24.426 63.805 1.00 10.78 ? 405 GLY A C 1 ATOM 2524 O O . GLY A 1 323 ? 16.914 25.578 63.335 1.00 11.87 ? 405 GLY A O 1 ATOM 2525 N N . TYR A 1 324 ? 17.189 23.323 63.091 1.00 7.55 ? 406 TYR A N 1 ATOM 2526 C CA . TYR A 1 324 ? 17.754 23.360 61.752 1.00 8.42 ? 406 TYR A CA 1 ATOM 2527 C C . TYR A 1 324 ? 16.693 23.757 60.712 1.00 7.06 ? 406 TYR A C 1 ATOM 2528 O O . TYR A 1 324 ? 15.504 23.522 60.866 1.00 8.67 ? 406 TYR A O 1 ATOM 2529 C CB . TYR A 1 324 ? 18.318 21.974 61.495 1.00 8.19 ? 406 TYR A CB 1 ATOM 2530 C CG . TYR A 1 324 ? 19.718 21.623 61.974 1.00 7.83 ? 406 TYR A CG 1 ATOM 2531 C CD1 . TYR A 1 324 ? 20.436 22.340 62.933 1.00 10.32 ? 406 TYR A CD1 1 ATOM 2532 C CD2 . TYR A 1 324 ? 20.281 20.522 61.381 1.00 6.84 ? 406 TYR A CD2 1 ATOM 2533 C CE1 . TYR A 1 324 ? 21.711 21.923 63.274 1.00 9.20 ? 406 TYR A CE1 1 ATOM 2534 C CE2 . TYR A 1 324 ? 21.551 20.117 61.718 1.00 9.42 ? 406 TYR A CE2 1 ATOM 2535 C CZ . TYR A 1 324 ? 22.268 20.817 62.656 1.00 11.60 ? 406 TYR A CZ 1 ATOM 2536 O OH . TYR A 1 324 ? 23.558 20.391 63.000 1.00 15.22 ? 406 TYR A OH 1 ATOM 2537 N N . SER A 1 325 ? 17.012 24.440 59.655 1.00 7.60 ? 407 SER A N 1 ATOM 2538 C CA . SER A 1 325 ? 16.054 24.762 58.618 1.00 5.16 ? 407 SER A CA 1 ATOM 2539 C C . SER A 1 325 ? 16.771 24.551 57.314 1.00 4.99 ? 407 SER A C 1 ATOM 2540 O O . SER A 1 325 ? 17.991 24.588 57.313 1.00 4.80 ? 407 SER A O 1 ATOM 2541 C CB . SER A 1 325 ? 15.618 26.197 58.775 1.00 8.52 ? 407 SER A CB 1 ATOM 2542 O OG . SER A 1 325 ? 16.684 27.104 59.093 1.00 12.45 ? 407 SER A OG 1 ATOM 2543 N N . GLY A 1 326 ? 16.077 24.300 56.216 1.00 4.41 ? 408 GLY A N 1 ATOM 2544 C CA . GLY A 1 326 ? 16.653 24.028 54.892 1.00 2.58 ? 408 GLY A CA 1 ATOM 2545 C C . GLY A 1 326 ? 15.684 24.403 53.766 1.00 6.65 ? 408 GLY A C 1 ATOM 2546 O O . GLY A 1 326 ? 14.522 24.736 54.026 1.00 9.12 ? 408 GLY A O 1 ATOM 2547 N N . SER A 1 327 ? 16.135 24.304 52.514 1.00 6.32 ? 409 SER A N 1 ATOM 2548 C CA . SER A 1 327 ? 15.443 24.739 51.334 1.00 3.94 ? 409 SER A CA 1 ATOM 2549 C C . SER A 1 327 ? 15.069 23.571 50.449 1.00 5.14 ? 409 SER A C 1 ATOM 2550 O O . SER A 1 327 ? 15.805 22.580 50.395 1.00 5.67 ? 409 SER A O 1 ATOM 2551 C CB . SER A 1 327 ? 16.335 25.734 50.572 1.00 3.65 ? 409 SER A CB 1 ATOM 2552 O OG . SER A 1 327 ? 17.713 25.379 50.367 1.00 5.12 ? 409 SER A OG 1 ATOM 2553 N N . PHE A 1 328 ? 13.896 23.591 49.823 1.00 5.41 ? 410 PHE A N 1 ATOM 2554 C CA . PHE A 1 328 ? 13.519 22.595 48.825 1.00 6.18 ? 410 PHE A CA 1 ATOM 2555 C C . PHE A 1 328 ? 12.549 23.358 47.974 1.00 5.51 ? 410 PHE A C 1 ATOM 2556 O O . PHE A 1 328 ? 12.097 24.419 48.357 1.00 3.08 ? 410 PHE A O 1 ATOM 2557 C CB . PHE A 1 328 ? 12.808 21.318 49.410 1.00 5.40 ? 410 PHE A CB 1 ATOM 2558 C CG . PHE A 1 328 ? 11.424 21.524 50.036 1.00 6.38 ? 410 PHE A CG 1 ATOM 2559 C CD1 . PHE A 1 328 ? 11.317 22.060 51.325 1.00 4.38 ? 410 PHE A CD1 1 ATOM 2560 C CD2 . PHE A 1 328 ? 10.281 21.224 49.294 1.00 4.24 ? 410 PHE A CD2 1 ATOM 2561 C CE1 . PHE A 1 328 ? 10.045 22.314 51.829 1.00 5.03 ? 410 PHE A CE1 1 ATOM 2562 C CE2 . PHE A 1 328 ? 9.035 21.482 49.840 1.00 5.34 ? 410 PHE A CE2 1 ATOM 2563 C CZ . PHE A 1 328 ? 8.903 22.018 51.110 1.00 2.70 ? 410 PHE A CZ 1 ATOM 2564 N N . MET A 1 329 ? 12.319 22.867 46.771 1.00 7.53 ? 411 MET A N 1 ATOM 2565 C CA . MET A 1 329 ? 11.292 23.296 45.851 1.00 8.38 ? 411 MET A CA 1 ATOM 2566 C C . MET A 1 329 ? 10.782 22.040 45.109 1.00 9.97 ? 411 MET A C 1 ATOM 2567 O O . MET A 1 329 ? 11.482 21.047 44.867 1.00 8.03 ? 411 MET A O 1 ATOM 2568 C CB . MET A 1 329 ? 11.861 24.294 44.842 1.00 8.23 ? 411 MET A CB 1 ATOM 2569 C CG . MET A 1 329 ? 12.349 25.591 45.477 1.00 8.45 ? 411 MET A CG 1 ATOM 2570 S SD . MET A 1 329 ? 12.564 27.011 44.396 1.00 7.83 ? 411 MET A SD 1 ATOM 2571 C CE . MET A 1 329 ? 13.810 26.446 43.299 1.00 7.07 ? 411 MET A CE 1 ATOM 2572 N N . ASP A 1 330 ? 9.556 22.066 44.632 1.00 10.41 ? 412 ASP A N 1 ATOM 2573 C CA . ASP A 1 330 ? 9.024 20.967 43.858 1.00 12.01 ? 412 ASP A CA 1 ATOM 2574 C C . ASP A 1 330 ? 9.193 21.365 42.401 1.00 12.57 ? 412 ASP A C 1 ATOM 2575 O O . ASP A 1 330 ? 8.383 22.036 41.748 1.00 12.95 ? 412 ASP A O 1 ATOM 2576 C CB . ASP A 1 330 ? 7.531 20.744 44.188 1.00 13.23 ? 412 ASP A CB 1 ATOM 2577 C CG . ASP A 1 330 ? 6.720 19.805 43.323 1.00 12.93 ? 412 ASP A CG 1 ATOM 2578 O OD1 . ASP A 1 330 ? 7.259 19.027 42.552 1.00 12.02 ? 412 ASP A OD1 1 ATOM 2579 O OD2 . ASP A 1 330 ? 5.507 19.861 43.465 1.00 14.88 ? 412 ASP A OD2 1 ATOM 2580 N N . TYR A 1 331 A 10.275 20.816 41.871 1.00 11.22 ? 412 TYR A N 1 ATOM 2581 C CA . TYR A 1 331 A 10.645 21.108 40.512 1.00 9.38 ? 412 TYR A CA 1 ATOM 2582 C C . TYR A 1 331 A 9.681 20.509 39.526 1.00 10.00 ? 412 TYR A C 1 ATOM 2583 O O . TYR A 1 331 A 9.811 20.822 38.366 1.00 9.59 ? 412 TYR A O 1 ATOM 2584 C CB . TYR A 1 331 A 12.037 20.571 40.238 1.00 8.24 ? 412 TYR A CB 1 ATOM 2585 C CG . TYR A 1 331 A 13.049 21.232 41.152 1.00 8.20 ? 412 TYR A CG 1 ATOM 2586 C CD1 . TYR A 1 331 A 13.459 22.515 40.896 1.00 10.68 ? 412 TYR A CD1 1 ATOM 2587 C CD2 . TYR A 1 331 A 13.579 20.557 42.225 1.00 8.51 ? 412 TYR A CD2 1 ATOM 2588 C CE1 . TYR A 1 331 A 14.370 23.132 41.714 1.00 9.86 ? 412 TYR A CE1 1 ATOM 2589 C CE2 . TYR A 1 331 A 14.471 21.172 43.055 1.00 6.91 ? 412 TYR A CE2 1 ATOM 2590 C CZ . TYR A 1 331 A 14.862 22.471 42.829 1.00 8.81 ? 412 TYR A CZ 1 ATOM 2591 O OH . TYR A 1 331 A 15.773 23.125 43.691 1.00 4.68 ? 412 TYR A OH 1 ATOM 2592 N N . TRP A 1 332 B 8.685 19.706 39.906 1.00 11.16 ? 412 TRP A N 1 ATOM 2593 C CA . TRP A 1 332 B 7.768 19.094 38.984 1.00 10.94 ? 412 TRP A CA 1 ATOM 2594 C C . TRP A 1 332 B 6.332 19.659 39.176 1.00 12.27 ? 412 TRP A C 1 ATOM 2595 O O . TRP A 1 332 B 5.333 19.015 38.853 1.00 15.46 ? 412 TRP A O 1 ATOM 2596 C CB . TRP A 1 332 B 7.886 17.560 39.226 1.00 10.73 ? 412 TRP A CB 1 ATOM 2597 C CG . TRP A 1 332 B 9.283 16.979 38.955 1.00 10.08 ? 412 TRP A CG 1 ATOM 2598 C CD1 . TRP A 1 332 B 9.675 16.547 37.710 1.00 7.35 ? 412 TRP A CD1 1 ATOM 2599 C CD2 . TRP A 1 332 B 10.324 16.819 39.870 1.00 9.96 ? 412 TRP A CD2 1 ATOM 2600 N NE1 . TRP A 1 332 B 10.923 16.155 37.819 1.00 5.34 ? 412 TRP A NE1 1 ATOM 2601 C CE2 . TRP A 1 332 B 11.341 16.292 39.066 1.00 8.20 ? 412 TRP A CE2 1 ATOM 2602 C CE3 . TRP A 1 332 B 10.602 17.058 41.203 1.00 7.37 ? 412 TRP A CE3 1 ATOM 2603 C CZ2 . TRP A 1 332 B 12.595 15.995 39.532 1.00 7.58 ? 412 TRP A CZ2 1 ATOM 2604 C CZ3 . TRP A 1 332 B 11.870 16.749 41.658 1.00 6.51 ? 412 TRP A CZ3 1 ATOM 2605 C CH2 . TRP A 1 332 B 12.854 16.227 40.852 1.00 6.21 ? 412 TRP A CH2 1 ATOM 2606 N N . ALA A 1 333 ? 6.136 20.875 39.707 1.00 13.01 ? 413 ALA A N 1 ATOM 2607 C CA . ALA A 1 333 ? 4.846 21.508 39.874 1.00 11.41 ? 413 ALA A CA 1 ATOM 2608 C C . ALA A 1 333 ? 4.445 22.211 38.554 1.00 13.66 ? 413 ALA A C 1 ATOM 2609 O O . ALA A 1 333 ? 5.349 22.688 37.848 1.00 12.80 ? 413 ALA A O 1 ATOM 2610 C CB . ALA A 1 333 ? 4.980 22.502 40.988 1.00 11.20 ? 413 ALA A CB 1 ATOM 2611 N N . GLU A 1 334 ? 3.178 22.324 38.080 1.00 14.13 ? 414 GLU A N 1 ATOM 2612 C CA . GLU A 1 334 ? 2.847 23.025 36.831 1.00 17.26 ? 414 GLU A CA 1 ATOM 2613 C C . GLU A 1 334 ? 3.047 24.525 37.003 1.00 17.27 ? 414 GLU A C 1 ATOM 2614 O O . GLU A 1 334 ? 2.970 25.001 38.126 1.00 19.52 ? 414 GLU A O 1 ATOM 2615 C CB . GLU A 1 334 ? 1.389 22.758 36.443 0.02 18.68 ? 414 GLU A CB 1 ATOM 2616 C CG . GLU A 1 334 ? 1.218 21.324 35.963 0.02 20.96 ? 414 GLU A CG 1 ATOM 2617 C CD . GLU A 1 334 ? -0.175 20.916 35.500 0.02 22.08 ? 414 GLU A CD 1 ATOM 2618 O OE1 . GLU A 1 334 ? -0.619 21.373 34.447 0.02 22.72 ? 414 GLU A OE1 1 ATOM 2619 O OE2 . GLU A 1 334 ? -0.803 20.099 36.172 0.02 22.83 ? 414 GLU A OE2 1 ATOM 2620 N N . GLY A 1 335 ? 3.320 25.372 36.030 1.00 17.85 ? 415 GLY A N 1 ATOM 2621 C CA . GLY A 1 335 ? 3.572 26.761 36.342 1.00 17.45 ? 415 GLY A CA 1 ATOM 2622 C C . GLY A 1 335 ? 4.727 27.323 35.536 1.00 18.32 ? 415 GLY A C 1 ATOM 2623 O O . GLY A 1 335 ? 5.400 26.598 34.790 1.00 16.56 ? 415 GLY A O 1 ATOM 2624 N N . GLU A 1 336 ? 4.878 28.655 35.658 1.00 18.42 ? 416 GLU A N 1 ATOM 2625 C CA . GLU A 1 336 ? 5.845 29.389 34.871 1.00 19.25 ? 416 GLU A CA 1 ATOM 2626 C C . GLU A 1 336 ? 7.163 29.556 35.624 1.00 20.50 ? 416 GLU A C 1 ATOM 2627 O O . GLU A 1 336 ? 8.212 29.749 34.989 1.00 21.31 ? 416 GLU A O 1 ATOM 2628 C CB . GLU A 1 336 ? 5.322 30.774 34.497 0.02 20.28 ? 416 GLU A CB 1 ATOM 2629 C CG . GLU A 1 336 ? 5.081 31.770 35.622 0.02 20.69 ? 416 GLU A CG 1 ATOM 2630 C CD . GLU A 1 336 ? 5.561 33.161 35.243 0.02 20.86 ? 416 GLU A CD 1 ATOM 2631 O OE1 . GLU A 1 336 ? 6.736 33.457 35.471 0.02 21.01 ? 416 GLU A OE1 1 ATOM 2632 O OE2 . GLU A 1 336 ? 4.755 33.929 34.721 0.02 20.90 ? 416 GLU A OE2 1 ATOM 2633 N N . CYS A 1 337 ? 7.187 29.414 36.967 1.00 17.96 ? 417 CYS A N 1 ATOM 2634 C CA . CYS A 1 337 ? 8.376 29.691 37.802 1.00 13.97 ? 417 CYS A CA 1 ATOM 2635 C C . CYS A 1 337 ? 8.448 28.712 39.002 1.00 13.06 ? 417 CYS A C 1 ATOM 2636 O O . CYS A 1 337 ? 7.436 28.061 39.314 1.00 13.36 ? 417 CYS A O 1 ATOM 2637 C CB . CYS A 1 337 ? 8.318 31.138 38.329 1.00 12.29 ? 417 CYS A CB 1 ATOM 2638 S SG . CYS A 1 337 ? 6.676 31.309 39.040 1.00 14.20 ? 417 CYS A SG 1 ATOM 2639 N N . TYR A 1 338 ? 9.564 28.473 39.711 1.00 9.89 ? 418 TYR A N 1 ATOM 2640 C CA . TYR A 1 338 ? 9.626 27.622 40.871 1.00 6.58 ? 418 TYR A CA 1 ATOM 2641 C C . TYR A 1 338 ? 9.163 28.358 42.134 1.00 6.23 ? 418 TYR A C 1 ATOM 2642 O O . TYR A 1 338 ? 9.569 29.486 42.457 1.00 7.24 ? 418 TYR A O 1 ATOM 2643 C CB . TYR A 1 338 ? 11.089 27.154 40.990 1.00 7.95 ? 418 TYR A CB 1 ATOM 2644 C CG . TYR A 1 338 ? 11.649 26.288 39.878 1.00 7.44 ? 418 TYR A CG 1 ATOM 2645 C CD1 . TYR A 1 338 ? 10.870 25.334 39.274 1.00 6.41 ? 418 TYR A CD1 1 ATOM 2646 C CD2 . TYR A 1 338 ? 12.948 26.448 39.471 1.00 8.86 ? 418 TYR A CD2 1 ATOM 2647 C CE1 . TYR A 1 338 ? 11.405 24.544 38.281 1.00 6.66 ? 418 TYR A CE1 1 ATOM 2648 C CE2 . TYR A 1 338 ? 13.495 25.656 38.473 1.00 7.60 ? 418 TYR A CE2 1 ATOM 2649 C CZ . TYR A 1 338 ? 12.720 24.683 37.867 1.00 7.33 ? 418 TYR A CZ 1 ATOM 2650 O OH . TYR A 1 338 ? 13.224 23.853 36.840 1.00 10.64 ? 418 TYR A OH 1 ATOM 2651 N N . ARG A 1 339 ? 8.323 27.712 42.915 1.00 4.73 ? 419 ARG A N 1 ATOM 2652 C CA . ARG A 1 339 ? 7.827 28.292 44.159 1.00 4.55 ? 419 ARG A CA 1 ATOM 2653 C C . ARG A 1 339 ? 8.837 27.921 45.238 1.00 4.73 ? 419 ARG A C 1 ATOM 2654 O O . ARG A 1 339 ? 9.079 26.735 45.467 1.00 7.63 ? 419 ARG A O 1 ATOM 2655 C CB . ARG A 1 339 ? 6.465 27.690 44.391 1.00 3.91 ? 419 ARG A CB 1 ATOM 2656 C CG . ARG A 1 339 ? 5.600 28.345 45.415 1.00 6.86 ? 419 ARG A CG 1 ATOM 2657 C CD . ARG A 1 339 ? 4.475 27.372 45.485 1.00 9.44 ? 419 ARG A CD 1 ATOM 2658 N NE . ARG A 1 339 ? 3.369 27.977 46.119 1.00 13.28 ? 419 ARG A NE 1 ATOM 2659 C CZ . ARG A 1 339 ? 2.213 28.220 45.480 1.00 11.66 ? 419 ARG A CZ 1 ATOM 2660 N NH1 . ARG A 1 339 ? 1.892 27.865 44.251 1.00 8.11 ? 419 ARG A NH1 1 ATOM 2661 N NH2 . ARG A 1 339 ? 1.294 28.821 46.168 1.00 12.65 ? 419 ARG A NH2 1 ATOM 2662 N N . ALA A 1 340 ? 9.392 28.882 45.955 1.00 4.78 ? 420 ALA A N 1 ATOM 2663 C CA . ALA A 1 340 ? 10.418 28.673 46.970 1.00 6.25 ? 420 ALA A CA 1 ATOM 2664 C C . ALA A 1 340 ? 9.834 28.048 48.238 1.00 6.94 ? 420 ALA A C 1 ATOM 2665 O O . ALA A 1 340 ? 8.785 28.554 48.691 1.00 4.41 ? 420 ALA A O 1 ATOM 2666 C CB . ALA A 1 340 ? 11.041 30.027 47.301 1.00 4.97 ? 420 ALA A CB 1 ATOM 2667 N N . CYS A 1 341 ? 10.405 27.000 48.860 1.00 7.33 ? 421 CYS A N 1 ATOM 2668 C CA . CYS A 1 341 ? 9.849 26.468 50.093 1.00 7.89 ? 421 CYS A CA 1 ATOM 2669 C C . CYS A 1 341 ? 10.938 26.234 51.148 1.00 6.76 ? 421 CYS A C 1 ATOM 2670 O O . CYS A 1 341 ? 12.128 26.309 50.816 1.00 7.09 ? 421 CYS A O 1 ATOM 2671 C CB . CYS A 1 341 ? 9.141 25.150 49.821 1.00 9.34 ? 421 CYS A CB 1 ATOM 2672 S SG . CYS A 1 341 ? 7.812 24.824 48.620 1.00 12.60 ? 421 CYS A SG 1 ATOM 2673 N N . PHE A 1 342 ? 10.627 25.991 52.420 1.00 5.59 ? 422 PHE A N 1 ATOM 2674 C CA . PHE A 1 342 ? 11.626 25.724 53.423 1.00 4.57 ? 422 PHE A CA 1 ATOM 2675 C C . PHE A 1 342 ? 10.986 24.895 54.542 1.00 3.72 ? 422 PHE A C 1 ATOM 2676 O O . PHE A 1 342 ? 9.750 24.744 54.573 1.00 4.47 ? 422 PHE A O 1 ATOM 2677 C CB . PHE A 1 342 ? 12.150 27.064 53.928 1.00 4.94 ? 422 PHE A CB 1 ATOM 2678 C CG . PHE A 1 342 ? 11.232 27.938 54.811 1.00 6.51 ? 422 PHE A CG 1 ATOM 2679 C CD1 . PHE A 1 342 ? 11.212 27.681 56.187 1.00 5.44 ? 422 PHE A CD1 1 ATOM 2680 C CD2 . PHE A 1 342 ? 10.417 28.943 54.271 1.00 3.11 ? 422 PHE A CD2 1 ATOM 2681 C CE1 . PHE A 1 342 ? 10.386 28.431 56.987 1.00 5.47 ? 422 PHE A CE1 1 ATOM 2682 C CE2 . PHE A 1 342 ? 9.596 29.690 55.093 1.00 2.54 ? 422 PHE A CE2 1 ATOM 2683 C CZ . PHE A 1 342 ? 9.592 29.429 56.440 1.00 2.68 ? 422 PHE A CZ 1 ATOM 2684 N N . TYR A 1 343 ? 11.773 24.319 55.455 1.00 4.92 ? 423 TYR A N 1 ATOM 2685 C CA . TYR A 1 343 ? 11.253 23.619 56.648 1.00 4.50 ? 423 TYR A CA 1 ATOM 2686 C C . TYR A 1 343 ? 12.075 24.169 57.819 1.00 4.51 ? 423 TYR A C 1 ATOM 2687 O O . TYR A 1 343 ? 13.129 24.767 57.581 1.00 4.12 ? 423 TYR A O 1 ATOM 2688 C CB . TYR A 1 343 ? 11.417 22.061 56.535 1.00 2.16 ? 423 TYR A CB 1 ATOM 2689 C CG . TYR A 1 343 ? 12.867 21.575 56.558 1.00 2.90 ? 423 TYR A CG 1 ATOM 2690 C CD1 . TYR A 1 343 ? 13.561 21.442 57.750 1.00 3.79 ? 423 TYR A CD1 1 ATOM 2691 C CD2 . TYR A 1 343 ? 13.571 21.396 55.374 1.00 3.37 ? 423 TYR A CD2 1 ATOM 2692 C CE1 . TYR A 1 343 ? 14.936 21.236 57.760 1.00 3.48 ? 423 TYR A CE1 1 ATOM 2693 C CE2 . TYR A 1 343 ? 14.932 21.182 55.383 1.00 2.00 ? 423 TYR A CE2 1 ATOM 2694 C CZ . TYR A 1 343 ? 15.616 21.137 56.567 1.00 3.84 ? 423 TYR A CZ 1 ATOM 2695 O OH . TYR A 1 343 ? 16.966 20.971 56.576 1.00 5.81 ? 423 TYR A OH 1 ATOM 2696 N N . VAL A 1 344 ? 11.643 24.011 59.093 1.00 6.99 ? 424 VAL A N 1 ATOM 2697 C CA . VAL A 1 344 ? 12.308 24.402 60.346 1.00 4.44 ? 424 VAL A CA 1 ATOM 2698 C C . VAL A 1 344 ? 12.032 23.141 61.190 1.00 5.34 ? 424 VAL A C 1 ATOM 2699 O O . VAL A 1 344 ? 10.903 22.627 61.233 1.00 2.61 ? 424 VAL A O 1 ATOM 2700 C CB . VAL A 1 344 ? 11.615 25.631 61.080 1.00 6.49 ? 424 VAL A CB 1 ATOM 2701 C CG1 . VAL A 1 344 ? 12.469 26.112 62.291 1.00 4.44 ? 424 VAL A CG1 1 ATOM 2702 C CG2 . VAL A 1 344 ? 11.350 26.763 60.073 1.00 4.68 ? 424 VAL A CG2 1 ATOM 2703 N N . GLU A 1 345 ? 13.083 22.639 61.839 1.00 4.45 ? 425 GLU A N 1 ATOM 2704 C CA . GLU A 1 345 ? 13.101 21.572 62.834 1.00 4.76 ? 425 GLU A CA 1 ATOM 2705 C C . GLU A 1 345 ? 12.679 22.211 64.150 1.00 5.61 ? 425 GLU A C 1 ATOM 2706 O O . GLU A 1 345 ? 13.052 23.346 64.443 1.00 6.96 ? 425 GLU A O 1 ATOM 2707 C CB . GLU A 1 345 ? 14.523 21.058 62.867 1.00 5.04 ? 425 GLU A CB 1 ATOM 2708 C CG . GLU A 1 345 ? 14.803 20.042 63.942 1.00 7.30 ? 425 GLU A CG 1 ATOM 2709 C CD . GLU A 1 345 ? 16.231 19.518 64.048 1.00 8.30 ? 425 GLU A CD 1 ATOM 2710 O OE1 . GLU A 1 345 ? 17.185 20.277 64.032 1.00 9.35 ? 425 GLU A OE1 1 ATOM 2711 O OE2 . GLU A 1 345 ? 16.377 18.326 64.215 1.00 7.84 ? 425 GLU A OE2 1 ATOM 2712 N N . LEU A 1 346 ? 11.861 21.557 64.955 1.00 7.35 ? 426 LEU A N 1 ATOM 2713 C CA . LEU A 1 346 ? 11.367 22.120 66.202 1.00 7.04 ? 426 LEU A CA 1 ATOM 2714 C C . LEU A 1 346 ? 11.862 21.072 67.169 1.00 8.79 ? 426 LEU A C 1 ATOM 2715 O O . LEU A 1 346 ? 11.241 19.999 67.227 1.00 10.92 ? 426 LEU A O 1 ATOM 2716 C CB . LEU A 1 346 ? 9.835 22.186 66.132 1.00 7.30 ? 426 LEU A CB 1 ATOM 2717 C CG . LEU A 1 346 ? 9.274 23.044 64.995 1.00 7.16 ? 426 LEU A CG 1 ATOM 2718 C CD1 . LEU A 1 346 ? 7.767 22.858 64.926 1.00 7.08 ? 426 LEU A CD1 1 ATOM 2719 C CD2 . LEU A 1 346 ? 9.677 24.506 65.203 1.00 7.52 ? 426 LEU A CD2 1 ATOM 2720 N N . ILE A 1 347 ? 12.989 21.316 67.848 1.00 8.65 ? 427 ILE A N 1 ATOM 2721 C CA . ILE A 1 347 ? 13.613 20.345 68.764 1.00 9.10 ? 427 ILE A CA 1 ATOM 2722 C C . ILE A 1 347 ? 12.947 20.440 70.146 1.00 10.00 ? 427 ILE A C 1 ATOM 2723 O O . ILE A 1 347 ? 12.721 21.550 70.651 1.00 9.36 ? 427 ILE A O 1 ATOM 2724 C CB . ILE A 1 347 ? 15.171 20.597 68.964 1.00 7.90 ? 427 ILE A CB 1 ATOM 2725 C CG1 . ILE A 1 347 ? 15.914 20.701 67.642 1.00 6.17 ? 427 ILE A CG1 1 ATOM 2726 C CG2 . ILE A 1 347 ? 15.769 19.415 69.761 1.00 3.84 ? 427 ILE A CG2 1 ATOM 2727 C CD1 . ILE A 1 347 ? 17.289 21.400 67.713 1.00 3.66 ? 427 ILE A CD1 1 ATOM 2728 N N . ARG A 1 348 ? 12.699 19.285 70.775 1.00 8.95 ? 428 ARG A N 1 ATOM 2729 C CA . ARG A 1 348 ? 12.108 19.149 72.087 1.00 10.94 ? 428 ARG A CA 1 ATOM 2730 C C . ARG A 1 348 ? 12.982 18.139 72.859 1.00 13.33 ? 428 ARG A C 1 ATOM 2731 O O . ARG A 1 348 ? 13.491 17.158 72.267 1.00 12.37 ? 428 ARG A O 1 ATOM 2732 C CB . ARG A 1 348 ? 10.696 18.573 72.022 1.00 9.83 ? 428 ARG A CB 1 ATOM 2733 C CG . ARG A 1 348 ? 9.643 19.325 71.252 1.00 7.04 ? 428 ARG A CG 1 ATOM 2734 C CD . ARG A 1 348 ? 9.529 20.766 71.759 1.00 7.92 ? 428 ARG A CD 1 ATOM 2735 N NE . ARG A 1 348 ? 9.209 20.809 73.173 1.00 7.04 ? 428 ARG A NE 1 ATOM 2736 C CZ . ARG A 1 348 ? 7.987 21.080 73.638 1.00 8.99 ? 428 ARG A CZ 1 ATOM 2737 N NH1 . ARG A 1 348 ? 6.921 21.182 72.871 1.00 8.55 ? 428 ARG A NH1 1 ATOM 2738 N NH2 . ARG A 1 348 ? 7.788 21.150 74.930 1.00 10.09 ? 428 ARG A NH2 1 ATOM 2739 N N . GLY A 1 349 ? 13.072 18.285 74.188 1.00 13.19 ? 429 GLY A N 1 ATOM 2740 C CA . GLY A 1 349 ? 13.903 17.416 75.027 1.00 14.63 ? 429 GLY A CA 1 ATOM 2741 C C . GLY A 1 349 ? 15.311 17.983 75.295 1.00 14.10 ? 429 GLY A C 1 ATOM 2742 O O . GLY A 1 349 ? 15.562 19.196 75.180 1.00 12.40 ? 429 GLY A O 1 ATOM 2743 N N . ARG A 1 350 ? 16.310 17.181 75.665 1.00 18.67 ? 430 ARG A N 1 ATOM 2744 C CA . ARG A 1 350 ? 17.647 17.717 75.965 1.00 19.98 ? 430 ARG A CA 1 ATOM 2745 C C . ARG A 1 350 ? 18.335 18.404 74.782 1.00 20.56 ? 430 ARG A C 1 ATOM 2746 O O . ARG A 1 350 ? 18.104 18.000 73.633 1.00 22.44 ? 430 ARG A O 1 ATOM 2747 C CB . ARG A 1 350 ? 18.550 16.622 76.485 1.00 18.12 ? 430 ARG A CB 1 ATOM 2748 C CG . ARG A 1 350 ? 18.037 16.168 77.827 1.00 21.86 ? 430 ARG A CG 1 ATOM 2749 C CD . ARG A 1 350 ? 18.980 15.267 78.661 1.00 23.36 ? 430 ARG A CD 1 ATOM 2750 N NE . ARG A 1 350 ? 18.280 14.884 79.882 1.00 25.92 ? 430 ARG A NE 1 ATOM 2751 C CZ . ARG A 1 350 ? 18.867 14.721 81.068 1.00 27.31 ? 430 ARG A CZ 1 ATOM 2752 N NH1 . ARG A 1 350 ? 20.198 14.710 81.165 1.00 28.32 ? 430 ARG A NH1 1 ATOM 2753 N NH2 . ARG A 1 350 ? 18.111 14.477 82.164 1.00 27.61 ? 430 ARG A NH2 1 ATOM 2754 N N . PRO A 1 351 ? 19.199 19.421 74.953 1.00 20.14 ? 431 PRO A N 1 ATOM 2755 C CA . PRO A 1 351 ? 19.660 20.008 76.223 1.00 19.69 ? 431 PRO A CA 1 ATOM 2756 C C . PRO A 1 351 ? 18.769 20.953 76.998 1.00 19.16 ? 431 PRO A C 1 ATOM 2757 O O . PRO A 1 351 ? 18.903 21.014 78.207 1.00 19.82 ? 431 PRO A O 1 ATOM 2758 C CB . PRO A 1 351 ? 20.936 20.687 75.880 1.00 20.08 ? 431 PRO A CB 1 ATOM 2759 C CG . PRO A 1 351 ? 20.574 21.214 74.503 1.00 20.21 ? 431 PRO A CG 1 ATOM 2760 C CD . PRO A 1 351 ? 19.989 19.988 73.859 1.00 19.83 ? 431 PRO A CD 1 ATOM 2761 N N . LYS A 1 352 ? 17.893 21.716 76.362 1.00 19.06 ? 432 LYS A N 1 ATOM 2762 C CA . LYS A 1 352 ? 17.151 22.726 77.091 1.00 18.96 ? 432 LYS A CA 1 ATOM 2763 C C . LYS A 1 352 ? 16.044 22.177 77.959 1.00 18.27 ? 432 LYS A C 1 ATOM 2764 O O . LYS A 1 352 ? 15.828 22.709 79.052 1.00 19.00 ? 432 LYS A O 1 ATOM 2765 C CB . LYS A 1 352 ? 16.548 23.733 76.124 1.00 21.51 ? 432 LYS A CB 1 ATOM 2766 C CG . LYS A 1 352 ? 17.573 24.491 75.305 1.00 27.76 ? 432 LYS A CG 1 ATOM 2767 C CD . LYS A 1 352 ? 18.338 25.448 76.193 1.00 31.13 ? 432 LYS A CD 1 ATOM 2768 C CE . LYS A 1 352 ? 19.412 26.186 75.422 1.00 33.44 ? 432 LYS A CE 1 ATOM 2769 N NZ . LYS A 1 352 ? 19.909 27.309 76.198 1.00 36.19 ? 432 LYS A NZ 1 ATOM 2770 N N . GLU A 1 353 ? 15.334 21.120 77.542 1.00 16.41 ? 433 GLU A N 1 ATOM 2771 C CA . GLU A 1 353 ? 14.241 20.614 78.327 1.00 16.96 ? 433 GLU A CA 1 ATOM 2772 C C . GLU A 1 353 ? 14.802 19.349 78.900 1.00 18.37 ? 433 GLU A C 1 ATOM 2773 O O . GLU A 1 353 ? 14.417 18.240 78.550 1.00 19.95 ? 433 GLU A O 1 ATOM 2774 C CB . GLU A 1 353 ? 13.058 20.338 77.456 1.00 13.97 ? 433 GLU A CB 1 ATOM 2775 C CG . GLU A 1 353 ? 12.368 21.582 77.027 1.00 13.86 ? 433 GLU A CG 1 ATOM 2776 C CD . GLU A 1 353 ? 11.234 21.361 76.052 1.00 16.11 ? 433 GLU A CD 1 ATOM 2777 O OE1 . GLU A 1 353 ? 11.375 20.548 75.146 1.00 18.11 ? 433 GLU A OE1 1 ATOM 2778 O OE2 . GLU A 1 353 ? 10.207 22.020 76.178 1.00 18.59 ? 433 GLU A OE2 1 ATOM 2779 N N . ASP A 1 354 ? 15.716 19.529 79.856 1.00 21.17 ? 434 ASP A N 1 ATOM 2780 C CA . ASP A 1 354 ? 16.414 18.389 80.462 1.00 21.49 ? 434 ASP A CA 1 ATOM 2781 C C . ASP A 1 354 ? 15.590 17.611 81.501 1.00 21.91 ? 434 ASP A C 1 ATOM 2782 O O . ASP A 1 354 ? 16.096 16.779 82.265 1.00 22.61 ? 434 ASP A O 1 ATOM 2783 C CB . ASP A 1 354 ? 17.728 18.900 81.078 0.02 21.20 ? 434 ASP A CB 1 ATOM 2784 C CG . ASP A 1 354 ? 17.566 19.988 82.125 0.02 21.18 ? 434 ASP A CG 1 ATOM 2785 O OD1 . ASP A 1 354 ? 17.467 21.157 81.754 0.02 21.22 ? 434 ASP A OD1 1 ATOM 2786 O OD2 . ASP A 1 354 ? 17.534 19.664 83.312 0.02 21.24 ? 434 ASP A OD2 1 ATOM 2787 N N . LYS A 1 355 ? 14.266 17.805 81.499 1.00 20.69 ? 435 LYS A N 1 ATOM 2788 C CA . LYS A 1 355 ? 13.485 17.161 82.519 1.00 22.49 ? 435 LYS A CA 1 ATOM 2789 C C . LYS A 1 355 ? 13.081 15.792 81.999 1.00 22.50 ? 435 LYS A C 1 ATOM 2790 O O . LYS A 1 355 ? 12.484 15.023 82.767 1.00 24.42 ? 435 LYS A O 1 ATOM 2791 C CB . LYS A 1 355 ? 12.308 18.062 82.817 1.00 27.35 ? 435 LYS A CB 1 ATOM 2792 C CG . LYS A 1 355 ? 11.848 17.969 84.263 1.00 31.81 ? 435 LYS A CG 1 ATOM 2793 C CD . LYS A 1 355 ? 12.826 18.610 85.237 1.00 37.06 ? 435 LYS A CD 1 ATOM 2794 C CE . LYS A 1 355 ? 12.421 18.196 86.655 1.00 40.74 ? 435 LYS A CE 1 ATOM 2795 N NZ . LYS A 1 355 ? 13.112 19.075 87.582 1.00 43.02 ? 435 LYS A NZ 1 ATOM 2796 N N . VAL A 1 356 ? 13.281 15.555 80.670 1.00 18.35 ? 436 VAL A N 1 ATOM 2797 C CA . VAL A 1 356 ? 13.190 14.237 80.047 1.00 15.11 ? 436 VAL A CA 1 ATOM 2798 C C . VAL A 1 356 ? 14.603 13.769 79.667 1.00 13.14 ? 436 VAL A C 1 ATOM 2799 O O . VAL A 1 356 ? 15.519 14.563 79.586 1.00 10.48 ? 436 VAL A O 1 ATOM 2800 C CB . VAL A 1 356 ? 12.346 14.270 78.762 1.00 14.09 ? 436 VAL A CB 1 ATOM 2801 C CG1 . VAL A 1 356 ? 10.949 14.753 79.060 1.00 11.48 ? 436 VAL A CG1 1 ATOM 2802 C CG2 . VAL A 1 356 ? 13.034 15.173 77.738 1.00 13.22 ? 436 VAL A CG2 1 ATOM 2803 N N . TRP A 1 357 ? 14.780 12.522 79.274 1.00 12.87 ? 437 TRP A N 1 ATOM 2804 C CA . TRP A 1 357 ? 16.067 11.962 78.930 1.00 13.43 ? 437 TRP A CA 1 ATOM 2805 C C . TRP A 1 357 ? 16.230 11.830 77.422 1.00 11.30 ? 437 TRP A C 1 ATOM 2806 O O . TRP A 1 357 ? 17.223 11.248 77.034 1.00 11.15 ? 437 TRP A O 1 ATOM 2807 C CB . TRP A 1 357 ? 16.201 10.589 79.615 1.00 17.37 ? 437 TRP A CB 1 ATOM 2808 C CG . TRP A 1 357 ? 16.464 10.760 81.104 1.00 22.56 ? 437 TRP A CG 1 ATOM 2809 C CD1 . TRP A 1 357 ? 15.416 10.848 81.984 1.00 23.89 ? 437 TRP A CD1 1 ATOM 2810 C CD2 . TRP A 1 357 ? 17.680 10.957 81.723 1.00 24.78 ? 437 TRP A CD2 1 ATOM 2811 N NE1 . TRP A 1 357 ? 15.963 11.120 83.146 1.00 25.20 ? 437 TRP A NE1 1 ATOM 2812 C CE2 . TRP A 1 357 ? 17.291 11.190 83.031 1.00 24.54 ? 437 TRP A CE2 1 ATOM 2813 C CE3 . TRP A 1 357 ? 19.022 10.993 81.396 1.00 25.26 ? 437 TRP A CE3 1 ATOM 2814 C CZ2 . TRP A 1 357 ? 18.210 11.448 84.019 1.00 23.20 ? 437 TRP A CZ2 1 ATOM 2815 C CZ3 . TRP A 1 357 ? 19.953 11.262 82.382 1.00 24.40 ? 437 TRP A CZ3 1 ATOM 2816 C CH2 . TRP A 1 357 ? 19.549 11.483 83.680 1.00 23.64 ? 437 TRP A CH2 1 ATOM 2817 N N . TRP A 1 358 ? 15.367 12.383 76.537 1.00 11.92 ? 438 TRP A N 1 ATOM 2818 C CA . TRP A 1 358 ? 15.456 12.092 75.114 1.00 9.93 ? 438 TRP A CA 1 ATOM 2819 C C . TRP A 1 358 ? 15.578 13.379 74.329 1.00 8.77 ? 438 TRP A C 1 ATOM 2820 O O . TRP A 1 358 ? 15.357 14.443 74.915 1.00 10.63 ? 438 TRP A O 1 ATOM 2821 C CB . TRP A 1 358 ? 14.229 11.340 74.593 1.00 9.47 ? 438 TRP A CB 1 ATOM 2822 C CG . TRP A 1 358 ? 12.865 11.920 74.943 1.00 10.25 ? 438 TRP A CG 1 ATOM 2823 C CD1 . TRP A 1 358 ? 12.139 11.303 75.931 1.00 10.50 ? 438 TRP A CD1 1 ATOM 2824 C CD2 . TRP A 1 358 ? 12.199 12.995 74.371 1.00 10.42 ? 438 TRP A CD2 1 ATOM 2825 N NE1 . TRP A 1 358 ? 11.015 11.961 75.971 1.00 10.13 ? 438 TRP A NE1 1 ATOM 2826 C CE2 . TRP A 1 358 ? 11.018 12.944 75.076 1.00 9.91 ? 438 TRP A CE2 1 ATOM 2827 C CE3 . TRP A 1 358 ? 12.321 13.991 73.418 1.00 9.61 ? 438 TRP A CE3 1 ATOM 2828 C CZ2 . TRP A 1 358 ? 9.975 13.820 74.868 1.00 11.62 ? 438 TRP A CZ2 1 ATOM 2829 C CZ3 . TRP A 1 358 ? 11.298 14.883 73.197 1.00 8.78 ? 438 TRP A CZ3 1 ATOM 2830 C CH2 . TRP A 1 358 ? 10.125 14.804 73.916 1.00 9.51 ? 438 TRP A CH2 1 ATOM 2831 N N . THR A 1 359 ? 16.008 13.347 73.065 1.00 7.61 ? 439 THR A N 1 ATOM 2832 C CA . THR A 1 359 ? 15.915 14.510 72.188 1.00 8.78 ? 439 THR A CA 1 ATOM 2833 C C . THR A 1 359 ? 15.154 14.198 70.890 1.00 7.26 ? 439 THR A C 1 ATOM 2834 O O . THR A 1 359 ? 15.587 13.334 70.130 1.00 7.39 ? 439 THR A O 1 ATOM 2835 C CB . THR A 1 359 ? 17.302 15.019 71.827 1.00 9.46 ? 439 THR A CB 1 ATOM 2836 O OG1 . THR A 1 359 ? 17.980 15.239 73.060 1.00 11.27 ? 439 THR A OG1 1 ATOM 2837 C CG2 . THR A 1 359 ? 17.267 16.320 71.050 1.00 10.36 ? 439 THR A CG2 1 ATOM 2838 N N . SER A 1 360 ? 14.025 14.816 70.557 1.00 5.80 ? 440 SER A N 1 ATOM 2839 C CA . SER A 1 360 ? 13.360 14.510 69.315 1.00 6.71 ? 440 SER A CA 1 ATOM 2840 C C . SER A 1 360 ? 12.857 15.795 68.656 1.00 6.82 ? 440 SER A C 1 ATOM 2841 O O . SER A 1 360 ? 13.329 16.868 69.055 1.00 9.11 ? 440 SER A O 1 ATOM 2842 C CB . SER A 1 360 ? 12.237 13.518 69.582 1.00 4.35 ? 440 SER A CB 1 ATOM 2843 O OG . SER A 1 360 ? 12.132 12.803 68.349 1.00 3.69 ? 440 SER A OG 1 ATOM 2844 N N . ASN A 1 361 ? 11.989 15.772 67.642 1.00 8.70 ? 441 ASN A N 1 ATOM 2845 C CA . ASN A 1 361 ? 11.520 16.993 66.979 1.00 10.94 ? 441 ASN A CA 1 ATOM 2846 C C . ASN A 1 361 ? 10.228 16.824 66.160 1.00 9.81 ? 441 ASN A C 1 ATOM 2847 O O . ASN A 1 361 ? 9.778 15.697 65.871 1.00 6.20 ? 441 ASN A O 1 ATOM 2848 C CB . ASN A 1 361 ? 12.560 17.517 66.019 1.00 12.16 ? 441 ASN A CB 1 ATOM 2849 C CG . ASN A 1 361 ? 12.651 16.700 64.734 1.00 15.68 ? 441 ASN A CG 1 ATOM 2850 O OD1 . ASN A 1 361 ? 13.319 15.673 64.756 1.00 18.82 ? 441 ASN A OD1 1 ATOM 2851 N ND2 . ASN A 1 361 ? 12.084 17.044 63.582 1.00 14.19 ? 441 ASN A ND2 1 ATOM 2852 N N . SER A 1 362 ? 9.585 17.944 65.814 1.00 8.42 ? 442 SER A N 1 ATOM 2853 C CA . SER A 1 362 ? 8.622 17.813 64.731 1.00 6.14 ? 442 SER A CA 1 ATOM 2854 C C . SER A 1 362 ? 9.013 18.701 63.576 1.00 7.40 ? 442 SER A C 1 ATOM 2855 O O . SER A 1 362 ? 10.129 19.252 63.571 1.00 10.37 ? 442 SER A O 1 ATOM 2856 C CB . SER A 1 362 ? 7.271 18.118 65.283 1.00 8.46 ? 442 SER A CB 1 ATOM 2857 O OG . SER A 1 362 ? 6.993 19.443 65.718 1.00 9.56 ? 442 SER A OG 1 ATOM 2858 N N . ILE A 1 363 ? 8.168 18.870 62.561 1.00 8.36 ? 443 ILE A N 1 ATOM 2859 C CA . ILE A 1 363 ? 8.535 19.667 61.385 1.00 6.34 ? 443 ILE A CA 1 ATOM 2860 C C . ILE A 1 363 ? 7.390 20.632 61.100 1.00 7.34 ? 443 ILE A C 1 ATOM 2861 O O . ILE A 1 363 ? 6.216 20.321 61.349 1.00 4.14 ? 443 ILE A O 1 ATOM 2862 C CB . ILE A 1 363 ? 8.709 18.777 60.054 1.00 3.88 ? 443 ILE A CB 1 ATOM 2863 C CG1 . ILE A 1 363 ? 9.784 17.730 60.260 1.00 2.17 ? 443 ILE A CG1 1 ATOM 2864 C CG2 . ILE A 1 363 ? 9.155 19.612 58.852 1.00 3.39 ? 443 ILE A CG2 1 ATOM 2865 C CD1 . ILE A 1 363 ? 9.849 16.683 59.179 1.00 2.10 ? 443 ILE A CD1 1 ATOM 2866 N N . VAL A 1 364 ? 7.780 21.813 60.594 1.00 8.23 ? 444 VAL A N 1 ATOM 2867 C CA . VAL A 1 364 ? 6.843 22.711 59.898 1.00 7.28 ? 444 VAL A CA 1 ATOM 2868 C C . VAL A 1 364 ? 7.536 23.118 58.569 1.00 7.34 ? 444 VAL A C 1 ATOM 2869 O O . VAL A 1 364 ? 8.785 23.205 58.540 1.00 3.18 ? 444 VAL A O 1 ATOM 2870 C CB . VAL A 1 364 ? 6.493 23.918 60.906 1.00 6.70 ? 444 VAL A CB 1 ATOM 2871 C CG1 . VAL A 1 364 ? 7.545 24.971 61.077 1.00 5.89 ? 444 VAL A CG1 1 ATOM 2872 C CG2 . VAL A 1 364 ? 5.279 24.594 60.334 1.00 4.09 ? 444 VAL A CG2 1 ATOM 2873 N N . SER A 1 365 ? 6.797 23.192 57.449 1.00 8.31 ? 445 SER A N 1 ATOM 2874 C CA . SER A 1 365 ? 7.272 23.717 56.175 1.00 11.17 ? 445 SER A CA 1 ATOM 2875 C C . SER A 1 365 ? 6.213 24.687 55.677 1.00 11.44 ? 445 SER A C 1 ATOM 2876 O O . SER A 1 365 ? 5.008 24.609 56.006 1.00 6.17 ? 445 SER A O 1 ATOM 2877 C CB . SER A 1 365 ? 7.512 22.649 55.035 1.00 12.02 ? 445 SER A CB 1 ATOM 2878 O OG . SER A 1 365 ? 6.708 21.509 55.176 1.00 14.21 ? 445 SER A OG 1 ATOM 2879 N N . MET A 1 366 ? 6.763 25.533 54.811 1.00 10.73 ? 446 MET A N 1 ATOM 2880 C CA . MET A 1 366 ? 6.138 26.708 54.231 1.00 10.36 ? 446 MET A CA 1 ATOM 2881 C C . MET A 1 366 ? 6.495 26.946 52.767 1.00 10.02 ? 446 MET A C 1 ATOM 2882 O O . MET A 1 366 ? 7.658 26.708 52.435 1.00 9.88 ? 446 MET A O 1 ATOM 2883 C CB . MET A 1 366 ? 6.616 27.859 55.021 1.00 10.50 ? 446 MET A CB 1 ATOM 2884 C CG . MET A 1 366 ? 5.558 28.749 55.511 1.00 14.54 ? 446 MET A CG 1 ATOM 2885 S SD . MET A 1 366 ? 5.149 28.511 57.247 1.00 20.45 ? 446 MET A SD 1 ATOM 2886 C CE . MET A 1 366 ? 4.375 30.092 57.222 1.00 15.69 ? 446 MET A CE 1 ATOM 2887 N N . CYS A 1 367 ? 5.625 27.397 51.851 1.00 10.79 ? 447 CYS A N 1 ATOM 2888 C CA . CYS A 1 367 ? 6.072 27.739 50.514 1.00 12.69 ? 447 CYS A CA 1 ATOM 2889 C C . CYS A 1 367 ? 5.678 29.194 50.265 1.00 13.64 ? 447 CYS A C 1 ATOM 2890 O O . CYS A 1 367 ? 5.019 29.806 51.127 1.00 14.35 ? 447 CYS A O 1 ATOM 2891 C CB . CYS A 1 367 ? 5.434 26.788 49.496 1.00 12.55 ? 447 CYS A CB 1 ATOM 2892 S SG . CYS A 1 367 ? 6.082 25.099 49.652 1.00 12.92 ? 447 CYS A SG 1 ATOM 2893 N N . SER A 1 368 ? 6.038 29.826 49.168 1.00 13.98 ? 448 SER A N 1 ATOM 2894 C CA . SER A 1 368 ? 5.749 31.239 49.037 1.00 14.01 ? 448 SER A CA 1 ATOM 2895 C C . SER A 1 368 ? 4.452 31.544 48.314 1.00 15.15 ? 448 SER A C 1 ATOM 2896 O O . SER A 1 368 ? 3.910 30.652 47.639 1.00 16.18 ? 448 SER A O 1 ATOM 2897 C CB . SER A 1 368 ? 6.896 31.905 48.318 1.00 15.04 ? 448 SER A CB 1 ATOM 2898 O OG . SER A 1 368 ? 7.379 31.183 47.200 1.00 16.00 ? 448 SER A OG 1 ATOM 2899 N N . SER A 1 369 ? 4.011 32.804 48.432 1.00 12.76 ? 449 SER A N 1 ATOM 2900 C CA . SER A 1 369 ? 2.811 33.217 47.785 1.00 11.29 ? 449 SER A CA 1 ATOM 2901 C C . SER A 1 369 ? 3.114 34.594 47.215 1.00 13.26 ? 449 SER A C 1 ATOM 2902 O O . SER A 1 369 ? 3.956 35.328 47.770 1.00 13.37 ? 449 SER A O 1 ATOM 2903 C CB . SER A 1 369 ? 1.672 33.251 48.815 1.00 9.35 ? 449 SER A CB 1 ATOM 2904 O OG . SER A 1 369 ? 0.536 33.823 48.150 1.00 8.44 ? 449 SER A OG 1 ATOM 2905 N N . THR A 1 370 ? 2.467 34.903 46.074 1.00 15.67 ? 450 THR A N 1 ATOM 2906 C CA . THR A 1 370 ? 2.525 36.208 45.420 1.00 15.43 ? 450 THR A CA 1 ATOM 2907 C C . THR A 1 370 ? 1.549 37.220 46.032 1.00 17.94 ? 450 THR A C 1 ATOM 2908 O O . THR A 1 370 ? 1.511 38.425 45.734 1.00 19.00 ? 450 THR A O 1 ATOM 2909 C CB . THR A 1 370 ? 2.211 36.080 43.937 1.00 14.68 ? 450 THR A CB 1 ATOM 2910 O OG1 . THR A 1 370 ? 0.940 35.462 43.732 1.00 12.93 ? 450 THR A OG1 1 ATOM 2911 C CG2 . THR A 1 370 ? 3.310 35.280 43.306 1.00 14.23 ? 450 THR A CG2 1 ATOM 2912 N N . GLU A 1 371 ? 0.725 36.670 46.906 1.00 20.19 ? 451 GLU A N 1 ATOM 2913 C CA . GLU A 1 371 ? -0.237 37.398 47.680 1.00 19.42 ? 451 GLU A CA 1 ATOM 2914 C C . GLU A 1 371 ? 0.468 37.884 48.924 1.00 18.38 ? 451 GLU A C 1 ATOM 2915 O O . GLU A 1 371 ? 1.575 37.412 49.205 1.00 18.76 ? 451 GLU A O 1 ATOM 2916 C CB . GLU A 1 371 ? -1.360 36.467 48.076 1.00 19.83 ? 451 GLU A CB 1 ATOM 2917 C CG . GLU A 1 371 ? -2.004 35.838 46.868 1.00 22.18 ? 451 GLU A CG 1 ATOM 2918 C CD . GLU A 1 371 ? -2.591 36.833 45.852 1.00 24.89 ? 451 GLU A CD 1 ATOM 2919 O OE1 . GLU A 1 371 ? -3.398 37.691 46.236 1.00 26.40 ? 451 GLU A OE1 1 ATOM 2920 O OE2 . GLU A 1 371 ? -2.257 36.733 44.663 1.00 26.17 ? 451 GLU A OE2 1 ATOM 2921 N N . PHE A 1 372 ? -0.152 38.791 49.685 1.00 16.92 ? 452 PHE A N 1 ATOM 2922 C CA . PHE A 1 372 ? 0.358 39.151 51.005 1.00 15.66 ? 452 PHE A CA 1 ATOM 2923 C C . PHE A 1 372 ? -0.533 38.508 52.066 1.00 14.14 ? 452 PHE A C 1 ATOM 2924 O O . PHE A 1 372 ? -1.500 39.108 52.502 1.00 15.92 ? 452 PHE A O 1 ATOM 2925 C CB . PHE A 1 372 ? 0.359 40.669 51.226 1.00 14.02 ? 452 PHE A CB 1 ATOM 2926 C CG . PHE A 1 372 ? 1.478 41.322 50.415 1.00 13.70 ? 452 PHE A CG 1 ATOM 2927 C CD1 . PHE A 1 372 ? 1.236 41.648 49.078 1.00 12.39 ? 452 PHE A CD1 1 ATOM 2928 C CD2 . PHE A 1 372 ? 2.699 41.586 50.990 1.00 12.45 ? 452 PHE A CD2 1 ATOM 2929 C CE1 . PHE A 1 372 ? 2.175 42.246 48.271 1.00 9.69 ? 452 PHE A CE1 1 ATOM 2930 C CE2 . PHE A 1 372 ? 3.624 42.198 50.172 1.00 12.17 ? 452 PHE A CE2 1 ATOM 2931 C CZ . PHE A 1 372 ? 3.387 42.522 48.849 1.00 10.64 ? 452 PHE A CZ 1 ATOM 2932 N N . LEU A 1 373 ? -0.288 37.254 52.450 1.00 11.00 ? 453 LEU A N 1 ATOM 2933 C CA . LEU A 1 373 ? -1.107 36.595 53.419 1.00 10.42 ? 453 LEU A CA 1 ATOM 2934 C C . LEU A 1 373 ? -0.664 36.967 54.834 1.00 10.86 ? 453 LEU A C 1 ATOM 2935 O O . LEU A 1 373 ? 0.501 37.276 55.135 1.00 9.67 ? 453 LEU A O 1 ATOM 2936 C CB . LEU A 1 373 ? -1.015 35.070 53.148 1.00 6.38 ? 453 LEU A CB 1 ATOM 2937 C CG . LEU A 1 373 ? -1.241 34.562 51.731 1.00 4.71 ? 453 LEU A CG 1 ATOM 2938 C CD1 . LEU A 1 373 ? -0.978 33.077 51.786 1.00 2.00 ? 453 LEU A CD1 1 ATOM 2939 C CD2 . LEU A 1 373 ? -2.625 34.936 51.193 1.00 4.84 ? 453 LEU A CD2 1 ATOM 2940 N N . GLY A 1 374 ? -1.699 37.014 55.665 1.00 10.76 ? 454 GLY A N 1 ATOM 2941 C CA . GLY A 1 374 ? -1.542 37.175 57.105 1.00 12.95 ? 454 GLY A CA 1 ATOM 2942 C C . GLY A 1 374 ? -0.791 35.969 57.646 1.00 14.15 ? 454 GLY A C 1 ATOM 2943 O O . GLY A 1 374 ? -0.804 34.892 57.037 1.00 16.14 ? 454 GLY A O 1 ATOM 2944 N N . GLN A 1 375 ? -0.169 36.147 58.797 1.00 13.97 ? 455 GLN A N 1 ATOM 2945 C CA . GLN A 1 375 ? 0.643 35.151 59.469 1.00 12.76 ? 455 GLN A CA 1 ATOM 2946 C C . GLN A 1 375 ? 0.030 34.562 60.736 1.00 14.71 ? 455 GLN A C 1 ATOM 2947 O O . GLN A 1 375 ? -0.805 35.170 61.438 1.00 15.38 ? 455 GLN A O 1 ATOM 2948 C CB . GLN A 1 375 ? 2.005 35.789 59.814 1.00 12.81 ? 455 GLN A CB 1 ATOM 2949 C CG . GLN A 1 375 ? 1.932 37.092 60.615 1.00 13.55 ? 455 GLN A CG 1 ATOM 2950 C CD . GLN A 1 375 ? 3.211 37.888 60.864 1.00 15.31 ? 455 GLN A CD 1 ATOM 2951 O OE1 . GLN A 1 375 ? 4.304 37.702 60.322 1.00 15.94 ? 455 GLN A OE1 1 ATOM 2952 N NE2 . GLN A 1 375 ? 3.112 38.896 61.723 1.00 17.40 ? 455 GLN A NE2 1 ATOM 2953 N N . TRP A 1 376 ? 0.514 33.361 61.053 1.00 14.71 ? 456 TRP A N 1 ATOM 2954 C CA . TRP A 1 376 ? 0.240 32.688 62.314 1.00 13.16 ? 456 TRP A CA 1 ATOM 2955 C C . TRP A 1 376 ? 1.617 32.125 62.652 1.00 13.24 ? 456 TRP A C 1 ATOM 2956 O O . TRP A 1 376 ? 2.505 32.069 61.798 1.00 12.54 ? 456 TRP A O 1 ATOM 2957 C CB . TRP A 1 376 ? -0.740 31.535 62.161 1.00 12.42 ? 456 TRP A CB 1 ATOM 2958 C CG . TRP A 1 376 ? -1.635 31.254 63.354 1.00 11.09 ? 456 TRP A CG 1 ATOM 2959 C CD1 . TRP A 1 376 ? -1.691 32.052 64.484 1.00 9.42 ? 456 TRP A CD1 1 ATOM 2960 C CD2 . TRP A 1 376 ? -2.521 30.225 63.420 1.00 9.97 ? 456 TRP A CD2 1 ATOM 2961 N NE1 . TRP A 1 376 ? -2.611 31.525 65.252 1.00 9.66 ? 456 TRP A NE1 1 ATOM 2962 C CE2 . TRP A 1 376 ? -3.131 30.442 64.662 1.00 9.48 ? 456 TRP A CE2 1 ATOM 2963 C CE3 . TRP A 1 376 ? -2.886 29.185 62.610 1.00 8.44 ? 456 TRP A CE3 1 ATOM 2964 C CZ2 . TRP A 1 376 ? -4.120 29.605 65.103 1.00 7.90 ? 456 TRP A CZ2 1 ATOM 2965 C CZ3 . TRP A 1 376 ? -3.887 28.346 63.073 1.00 10.03 ? 456 TRP A CZ3 1 ATOM 2966 C CH2 . TRP A 1 376 ? -4.501 28.559 64.292 1.00 7.34 ? 456 TRP A CH2 1 ATOM 2967 N N . ASP A 1 377 ? 1.804 31.803 63.931 1.00 12.61 ? 457 ASP A N 1 ATOM 2968 C CA . ASP A 1 377 ? 3.015 31.174 64.409 1.00 14.70 ? 457 ASP A CA 1 ATOM 2969 C C . ASP A 1 377 ? 2.699 29.695 64.556 1.00 14.65 ? 457 ASP A C 1 ATOM 2970 O O . ASP A 1 377 ? 1.551 29.349 64.857 1.00 13.00 ? 457 ASP A O 1 ATOM 2971 C CB . ASP A 1 377 ? 3.445 31.746 65.754 1.00 16.68 ? 457 ASP A CB 1 ATOM 2972 C CG . ASP A 1 377 ? 2.560 31.537 66.987 1.00 17.88 ? 457 ASP A CG 1 ATOM 2973 O OD1 . ASP A 1 377 ? 1.510 32.177 67.115 1.00 18.39 ? 457 ASP A OD1 1 ATOM 2974 O OD2 . ASP A 1 377 ? 2.974 30.751 67.836 1.00 21.05 ? 457 ASP A OD2 1 ATOM 2975 N N . TRP A 1 378 ? 3.769 28.819 64.359 1.00 13.05 ? 458 TRP A N 1 ATOM 2976 C CA . TRP A 1 378 ? 3.570 27.377 64.270 1.00 12.07 ? 458 TRP A CA 1 ATOM 2977 C C . TRP A 1 378 ? 4.491 26.661 65.232 1.00 13.28 ? 458 TRP A C 1 ATOM 2978 O O . TRP A 1 378 ? 5.557 26.187 64.877 1.00 10.80 ? 458 TRP A O 1 ATOM 2979 C CB . TRP A 1 378 ? 3.859 26.928 62.793 1.00 10.56 ? 458 TRP A CB 1 ATOM 2980 C CG . TRP A 1 378 ? 2.862 27.591 61.821 1.00 11.69 ? 458 TRP A CG 1 ATOM 2981 C CD1 . TRP A 1 378 ? 3.151 28.804 61.246 1.00 10.57 ? 458 TRP A CD1 1 ATOM 2982 C CD2 . TRP A 1 378 ? 1.617 27.168 61.502 1.00 9.96 ? 458 TRP A CD2 1 ATOM 2983 N NE1 . TRP A 1 378 ? 2.075 29.155 60.577 1.00 6.45 ? 458 TRP A NE1 1 ATOM 2984 C CE2 . TRP A 1 378 ? 1.128 28.183 60.712 1.00 9.20 ? 458 TRP A CE2 1 ATOM 2985 C CE3 . TRP A 1 378 ? 0.831 26.073 61.783 1.00 10.72 ? 458 TRP A CE3 1 ATOM 2986 C CZ2 . TRP A 1 378 ? -0.149 28.071 60.201 1.00 8.83 ? 458 TRP A CZ2 1 ATOM 2987 C CZ3 . TRP A 1 378 ? -0.445 25.970 61.272 1.00 10.03 ? 458 TRP A CZ3 1 ATOM 2988 C CH2 . TRP A 1 378 ? -0.929 26.959 60.482 1.00 7.67 ? 458 TRP A CH2 1 ATOM 2989 N N . PRO A 1 379 ? 4.149 26.573 66.533 1.00 16.08 ? 459 PRO A N 1 ATOM 2990 C CA . PRO A 1 379 ? 5.021 25.976 67.539 1.00 18.25 ? 459 PRO A CA 1 ATOM 2991 C C . PRO A 1 379 ? 4.997 24.426 67.538 1.00 19.58 ? 459 PRO A C 1 ATOM 2992 O O . PRO A 1 379 ? 4.091 23.924 66.912 1.00 25.91 ? 459 PRO A O 1 ATOM 2993 C CB . PRO A 1 379 ? 4.514 26.637 68.812 1.00 17.89 ? 459 PRO A CB 1 ATOM 2994 C CG . PRO A 1 379 ? 3.021 26.625 68.564 1.00 17.90 ? 459 PRO A CG 1 ATOM 2995 C CD . PRO A 1 379 ? 2.872 26.990 67.090 1.00 17.41 ? 459 PRO A CD 1 ATOM 2996 N N . ASP A 1 380 ? 5.843 23.570 68.126 1.00 20.95 ? 460 ASP A N 1 ATOM 2997 C CA . ASP A 1 380 ? 5.646 22.102 68.148 1.00 22.21 ? 460 ASP A CA 1 ATOM 2998 C C . ASP A 1 380 ? 4.304 21.647 68.680 1.00 22.26 ? 460 ASP A C 1 ATOM 2999 O O . ASP A 1 380 ? 3.720 20.660 68.246 1.00 26.10 ? 460 ASP A O 1 ATOM 3000 C CB . ASP A 1 380 ? 6.718 21.400 69.012 1.00 19.19 ? 460 ASP A CB 1 ATOM 3001 C CG . ASP A 1 380 ? 6.533 19.884 69.359 1.00 19.13 ? 460 ASP A CG 1 ATOM 3002 O OD1 . ASP A 1 380 ? 6.481 19.023 68.457 1.00 18.42 ? 460 ASP A OD1 1 ATOM 3003 O OD2 . ASP A 1 380 ? 6.454 19.518 70.560 1.00 14.85 ? 460 ASP A OD2 1 ATOM 3004 N N . GLY A 1 381 ? 4.018 22.243 69.839 1.00 22.95 ? 461 GLY A N 1 ATOM 3005 C CA . GLY A 1 381 ? 2.753 22.043 70.531 1.00 22.70 ? 461 GLY A CA 1 ATOM 3006 C C . GLY A 1 381 ? 2.701 20.930 71.590 1.00 24.20 ? 461 GLY A C 1 ATOM 3007 O O . GLY A 1 381 ? 1.655 20.797 72.217 1.00 26.35 ? 461 GLY A O 1 ATOM 3008 N N . ALA A 1 382 ? 3.694 20.082 71.885 1.00 25.26 ? 462 ALA A N 1 ATOM 3009 C CA . ALA A 1 382 ? 3.592 19.094 72.961 1.00 23.70 ? 462 ALA A CA 1 ATOM 3010 C C . ALA A 1 382 ? 3.818 19.806 74.268 1.00 24.13 ? 462 ALA A C 1 ATOM 3011 O O . ALA A 1 382 ? 4.488 20.825 74.277 1.00 23.43 ? 462 ALA A O 1 ATOM 3012 C CB . ALA A 1 382 ? 4.694 18.045 72.915 1.00 23.42 ? 462 ALA A CB 1 ATOM 3013 N N . LYS A 1 383 ? 3.393 19.176 75.340 1.00 26.15 ? 463 LYS A N 1 ATOM 3014 C CA . LYS A 1 383 ? 3.625 19.650 76.696 1.00 26.83 ? 463 LYS A CA 1 ATOM 3015 C C . LYS A 1 383 ? 4.621 18.655 77.266 1.00 24.06 ? 463 LYS A C 1 ATOM 3016 O O . LYS A 1 383 ? 4.190 17.532 77.537 1.00 24.26 ? 463 LYS A O 1 ATOM 3017 C CB . LYS A 1 383 ? 2.334 19.630 77.537 1.00 30.18 ? 463 LYS A CB 1 ATOM 3018 C CG . LYS A 1 383 ? 1.192 20.274 76.815 1.00 34.18 ? 463 LYS A CG 1 ATOM 3019 C CD . LYS A 1 383 ? 0.037 20.681 77.688 1.00 38.45 ? 463 LYS A CD 1 ATOM 3020 C CE . LYS A 1 383 ? -0.821 21.192 76.545 1.00 42.13 ? 463 LYS A CE 1 ATOM 3021 N NZ . LYS A 1 383 ? -2.041 21.870 76.912 1.00 42.54 ? 463 LYS A NZ 1 ATOM 3022 N N . ILE A 1 384 ? 5.888 18.990 77.560 1.00 22.82 ? 464 ILE A N 1 ATOM 3023 C CA . ILE A 1 384 ? 6.832 18.015 78.089 1.00 24.12 ? 464 ILE A CA 1 ATOM 3024 C C . ILE A 1 384 ? 6.327 17.285 79.324 1.00 23.48 ? 464 ILE A C 1 ATOM 3025 O O . ILE A 1 384 ? 6.534 16.087 79.432 1.00 27.96 ? 464 ILE A O 1 ATOM 3026 C CB . ILE A 1 384 ? 8.207 18.807 78.300 1.00 23.84 ? 464 ILE A CB 1 ATOM 3027 C CG1 . ILE A 1 384 ? 9.047 18.666 77.014 1.00 23.31 ? 464 ILE A CG1 1 ATOM 3028 C CG2 . ILE A 1 384 ? 8.998 18.289 79.519 1.00 24.77 ? 464 ILE A CG2 1 ATOM 3029 C CD1 . ILE A 1 384 ? 9.555 17.251 76.658 1.00 22.09 ? 464 ILE A CD1 1 ATOM 3030 N N . GLU A 1 385 ? 5.511 17.991 80.144 1.00 22.98 ? 465 GLU A N 1 ATOM 3031 C CA . GLU A 1 385 ? 5.044 17.418 81.394 1.00 23.09 ? 465 GLU A CA 1 ATOM 3032 C C . GLU A 1 385 ? 4.188 16.167 81.267 1.00 23.42 ? 465 GLU A C 1 ATOM 3033 O O . GLU A 1 385 ? 4.086 15.416 82.233 1.00 23.81 ? 465 GLU A O 1 ATOM 3034 C CB . GLU A 1 385 ? 4.275 18.485 82.182 1.00 22.73 ? 465 GLU A CB 1 ATOM 3035 C CG . GLU A 1 385 ? 5.333 19.319 82.862 1.00 22.57 ? 465 GLU A CG 1 ATOM 3036 C CD . GLU A 1 385 ? 4.940 20.372 83.892 1.00 22.54 ? 465 GLU A CD 1 ATOM 3037 O OE1 . GLU A 1 385 ? 3.744 20.628 84.107 1.00 22.52 ? 465 GLU A OE1 1 ATOM 3038 O OE2 . GLU A 1 385 ? 5.844 20.967 84.509 1.00 22.52 ? 465 GLU A OE2 1 ATOM 3039 N N . TYR A 1 386 ? 3.652 15.871 80.091 1.00 23.86 ? 466 TYR A N 1 ATOM 3040 C CA . TYR A 1 386 ? 2.881 14.659 79.912 1.00 23.07 ? 466 TYR A CA 1 ATOM 3041 C C . TYR A 1 386 ? 3.809 13.447 79.779 1.00 22.81 ? 466 TYR A C 1 ATOM 3042 O O . TYR A 1 386 ? 3.343 12.316 79.757 1.00 25.19 ? 466 TYR A O 1 ATOM 3043 C CB . TYR A 1 386 ? 2.058 14.834 78.646 1.00 21.40 ? 466 TYR A CB 1 ATOM 3044 C CG . TYR A 1 386 ? 0.894 15.834 78.711 1.00 21.08 ? 466 TYR A CG 1 ATOM 3045 C CD1 . TYR A 1 386 ? 0.353 16.189 79.916 1.00 18.92 ? 466 TYR A CD1 1 ATOM 3046 C CD2 . TYR A 1 386 ? 0.318 16.312 77.556 1.00 21.10 ? 466 TYR A CD2 1 ATOM 3047 C CE1 . TYR A 1 386 ? -0.753 16.976 79.960 1.00 21.17 ? 466 TYR A CE1 1 ATOM 3048 C CE2 . TYR A 1 386 ? -0.800 17.113 77.597 1.00 21.93 ? 466 TYR A CE2 1 ATOM 3049 C CZ . TYR A 1 386 ? -1.336 17.439 78.806 1.00 22.87 ? 466 TYR A CZ 1 ATOM 3050 O OH . TYR A 1 386 ? -2.476 18.193 78.859 1.00 26.74 ? 466 TYR A OH 1 ATOM 3051 N N . PHE A 1 387 ? 5.097 13.653 79.625 1.00 21.72 ? 467 PHE A N 1 ATOM 3052 C CA . PHE A 1 387 ? 6.019 12.574 79.376 1.00 23.16 ? 467 PHE A CA 1 ATOM 3053 C C . PHE A 1 387 ? 6.712 12.134 80.669 1.00 24.20 ? 467 PHE A C 1 ATOM 3054 O O . PHE A 1 387 ? 7.617 11.272 80.605 1.00 24.50 ? 467 PHE A O 1 ATOM 3055 C CB . PHE A 1 387 ? 7.037 13.062 78.306 1.00 21.26 ? 467 PHE A CB 1 ATOM 3056 C CG . PHE A 1 387 ? 6.493 13.249 76.890 1.00 19.83 ? 467 PHE A CG 1 ATOM 3057 C CD1 . PHE A 1 387 ? 6.511 12.204 75.990 1.00 19.60 ? 467 PHE A CD1 1 ATOM 3058 C CD2 . PHE A 1 387 ? 6.036 14.482 76.488 1.00 20.23 ? 467 PHE A CD2 1 ATOM 3059 C CE1 . PHE A 1 387 ? 6.070 12.388 74.696 1.00 17.84 ? 467 PHE A CE1 1 ATOM 3060 C CE2 . PHE A 1 387 ? 5.592 14.672 75.197 1.00 20.20 ? 467 PHE A CE2 1 ATOM 3061 C CZ . PHE A 1 387 ? 5.614 13.626 74.297 1.00 19.24 ? 467 PHE A CZ 1 ATOM 3062 N N . LEU A 1 388 ? 6.288 12.765 81.767 1.00 24.68 ? 468 LEU A N 1 ATOM 3063 C CA . LEU A 1 388 ? 6.871 12.551 83.077 1.00 25.15 ? 468 LEU A CA 1 ATOM 3064 C C . LEU A 1 388 ? 5.865 11.616 83.724 1.00 25.42 ? 468 LEU A C 1 ATOM 3065 O O . LEU A 1 388 ? 6.277 10.612 84.256 1.00 30.43 ? 468 LEU A O 1 ATOM 3066 C CB . LEU A 1 388 ? 6.951 13.840 83.839 1.00 24.97 ? 468 LEU A CB 1 ATOM 3067 C CG . LEU A 1 388 ? 7.805 14.938 83.190 1.00 26.95 ? 468 LEU A CG 1 ATOM 3068 C CD1 . LEU A 1 388 ? 7.658 16.176 84.056 1.00 26.67 ? 468 LEU A CD1 1 ATOM 3069 C CD2 . LEU A 1 388 ? 9.287 14.552 83.046 1.00 27.97 ? 468 LEU A CD2 1 ATOM 3070 O OXT . LEU A 1 388 ? 4.671 11.836 83.675 1.00 24.26 ? 468 LEU A OXT 1 HETATM 3071 C C1 . NAG B 2 . A 40.422 1.748 59.690 1.00 17.69 ? 469 NAG A C1 1 HETATM 3072 C C2 . NAG B 2 . A 41.046 1.074 60.946 1.00 19.70 ? 469 NAG A C2 1 HETATM 3073 C C3 . NAG B 2 . A 42.167 0.050 60.403 1.00 19.28 ? 469 NAG A C3 1 HETATM 3074 C C4 . NAG B 2 . A 41.517 -0.947 59.424 1.00 18.61 ? 469 NAG A C4 1 HETATM 3075 C C5 . NAG B 2 . A 40.751 -0.201 58.312 1.00 17.02 ? 469 NAG A C5 1 HETATM 3076 C C6 . NAG B 2 . A 39.965 -1.196 57.490 1.00 17.77 ? 469 NAG A C6 1 HETATM 3077 C C7 . NAG B 2 . A 42.152 3.175 61.676 1.00 26.27 ? 469 NAG A C7 1 HETATM 3078 C C8 . NAG B 2 . A 42.359 4.080 62.854 1.00 25.48 ? 469 NAG A C8 1 HETATM 3079 N N2 . NAG B 2 . A 41.492 2.056 61.936 1.00 23.43 ? 469 NAG A N2 1 HETATM 3080 O O3 . NAG B 2 . A 42.802 -0.715 61.440 1.00 18.43 ? 469 NAG A O3 1 HETATM 3081 O O4 . NAG B 2 . A 42.482 -1.865 58.788 1.00 18.50 ? 469 NAG A O4 1 HETATM 3082 O O5 . NAG B 2 . A 39.827 0.718 58.882 1.00 17.74 ? 469 NAG A O5 1 HETATM 3083 O O6 . NAG B 2 . A 39.180 -2.041 58.309 1.00 19.36 ? 469 NAG A O6 1 HETATM 3084 O O7 . NAG B 2 . A 42.597 3.480 60.579 1.00 30.46 ? 469 NAG A O7 1 HETATM 3085 C C1 . NAG C 2 . B 42.236 -3.297 58.941 1.00 19.39 ? 470 NAG A C1 1 HETATM 3086 C C2 . NAG C 2 . B 42.965 -4.161 57.897 1.00 18.78 ? 470 NAG A C2 1 HETATM 3087 C C3 . NAG C 2 . B 42.652 -5.623 58.171 1.00 19.62 ? 470 NAG A C3 1 HETATM 3088 C C4 . NAG C 2 . B 42.970 -5.936 59.628 1.00 20.79 ? 470 NAG A C4 1 HETATM 3089 C C5 . NAG C 2 . B 42.265 -5.007 60.639 1.00 20.92 ? 470 NAG A C5 1 HETATM 3090 C C6 . NAG C 2 . B 42.677 -5.293 62.086 1.00 22.99 ? 470 NAG A C6 1 HETATM 3091 C C7 . NAG C 2 . B 43.211 -3.144 55.648 1.00 21.50 ? 470 NAG A C7 1 HETATM 3092 C C8 . NAG C 2 . B 42.629 -2.904 54.256 1.00 19.40 ? 470 NAG A C8 1 HETATM 3093 N N2 . NAG C 2 . B 42.501 -3.801 56.561 1.00 20.41 ? 470 NAG A N2 1 HETATM 3094 O O3 . NAG C 2 . B 43.279 -6.559 57.314 1.00 19.49 ? 470 NAG A O3 1 HETATM 3095 O O4 . NAG C 2 . B 42.503 -7.247 59.939 1.00 22.27 ? 470 NAG A O4 1 HETATM 3096 O O5 . NAG C 2 . B 42.609 -3.657 60.297 1.00 20.33 ? 470 NAG A O5 1 HETATM 3097 O O6 . NAG C 2 . B 44.092 -5.237 62.183 1.00 26.44 ? 470 NAG A O6 1 HETATM 3098 O O7 . NAG C 2 . B 44.319 -2.707 55.934 1.00 24.22 ? 470 NAG A O7 1 HETATM 3099 C C1 . MAN D 3 . C 43.440 -8.219 60.376 1.00 22.41 ? 471 MAN A C1 1 HETATM 3100 C C2 . MAN D 3 . C 42.677 -9.414 60.968 1.00 21.77 ? 471 MAN A C2 1 HETATM 3101 C C3 . MAN D 3 . C 43.637 -10.524 61.285 1.00 22.57 ? 471 MAN A C3 1 HETATM 3102 C C4 . MAN D 3 . C 44.494 -10.872 60.042 1.00 22.70 ? 471 MAN A C4 1 HETATM 3103 C C5 . MAN D 3 . C 45.161 -9.640 59.440 1.00 23.21 ? 471 MAN A C5 1 HETATM 3104 C C6 . MAN D 3 . C 45.866 -9.910 58.140 1.00 26.23 ? 471 MAN A C6 1 HETATM 3105 O O2 . MAN D 3 . C 41.754 -9.851 60.004 1.00 20.70 ? 471 MAN A O2 1 HETATM 3106 O O3 . MAN D 3 . C 42.904 -11.691 61.687 1.00 22.62 ? 471 MAN A O3 1 HETATM 3107 O O4 . MAN D 3 . C 45.507 -11.759 60.453 1.00 23.06 ? 471 MAN A O4 1 HETATM 3108 O O5 . MAN D 3 . C 44.160 -8.644 59.204 1.00 23.18 ? 471 MAN A O5 1 HETATM 3109 O O6 . MAN D 3 . C 46.978 -9.000 57.954 1.00 32.00 ? 471 MAN A O6 1 HETATM 3110 C C1 . MAN E 3 . D 43.415 -12.414 62.781 1.00 22.29 ? 472 MAN A C1 1 HETATM 3111 C C2 . MAN E 3 . D 42.763 -13.771 62.900 1.00 23.25 ? 472 MAN A C2 1 HETATM 3112 C C3 . MAN E 3 . D 41.335 -13.618 63.460 1.00 23.78 ? 472 MAN A C3 1 HETATM 3113 C C4 . MAN E 3 . D 41.437 -12.874 64.791 1.00 24.14 ? 472 MAN A C4 1 HETATM 3114 C C5 . MAN E 3 . D 41.970 -11.482 64.517 1.00 25.00 ? 472 MAN A C5 1 HETATM 3115 C C6 . MAN E 3 . D 42.015 -10.585 65.794 1.00 26.32 ? 472 MAN A C6 1 HETATM 3116 O O2 . MAN E 3 . D 43.628 -14.437 63.809 1.00 24.37 ? 472 MAN A O2 1 HETATM 3117 O O3 . MAN E 3 . D 40.659 -14.862 63.631 1.00 23.96 ? 472 MAN A O3 1 HETATM 3118 O O4 . MAN E 3 . D 40.179 -12.804 65.433 1.00 24.55 ? 472 MAN A O4 1 HETATM 3119 O O5 . MAN E 3 . D 43.292 -11.605 63.963 1.00 24.14 ? 472 MAN A O5 1 HETATM 3120 O O6 . MAN E 3 . D 43.110 -9.671 65.833 1.00 28.23 ? 472 MAN A O6 1 HETATM 3121 C C1 . MAN F 3 . E 43.384 -15.784 64.217 1.00 27.44 ? 473 MAN A C1 1 HETATM 3122 C C2 . MAN F 3 . E 44.470 -16.118 65.223 1.00 27.29 ? 473 MAN A C2 1 HETATM 3123 C C3 . MAN F 3 . E 45.809 -16.212 64.509 1.00 26.54 ? 473 MAN A C3 1 HETATM 3124 C C4 . MAN F 3 . E 45.699 -17.270 63.407 1.00 25.91 ? 473 MAN A C4 1 HETATM 3125 C C5 . MAN F 3 . E 44.611 -16.883 62.410 1.00 26.36 ? 473 MAN A C5 1 HETATM 3126 C C6 . MAN F 3 . E 44.409 -17.911 61.303 1.00 26.73 ? 473 MAN A C6 1 HETATM 3127 O O2 . MAN F 3 . E 44.145 -17.385 65.811 1.00 28.37 ? 473 MAN A O2 1 HETATM 3128 O O3 . MAN F 3 . E 46.815 -16.561 65.446 1.00 27.47 ? 473 MAN A O3 1 HETATM 3129 O O4 . MAN F 3 . E 46.949 -17.335 62.769 1.00 27.34 ? 473 MAN A O4 1 HETATM 3130 O O5 . MAN F 3 . E 43.375 -16.732 63.116 1.00 27.70 ? 473 MAN A O5 1 HETATM 3131 O O6 . MAN F 3 . E 44.301 -19.215 61.808 1.00 26.77 ? 473 MAN A O6 1 HETATM 3132 C C1 . MAN G 3 . F 43.420 -17.390 67.033 1.00 28.57 ? 474 MAN A C1 1 HETATM 3133 C C2 . MAN G 3 . F 43.308 -18.831 67.484 1.00 28.83 ? 474 MAN A C2 1 HETATM 3134 C C3 . MAN G 3 . F 42.283 -19.616 66.622 1.00 29.94 ? 474 MAN A C3 1 HETATM 3135 C C4 . MAN G 3 . F 40.893 -18.893 66.735 1.00 30.47 ? 474 MAN A C4 1 HETATM 3136 C C5 . MAN G 3 . F 41.065 -17.477 66.201 1.00 30.85 ? 474 MAN A C5 1 HETATM 3137 C C6 . MAN G 3 . F 39.760 -16.677 66.345 1.00 30.75 ? 474 MAN A C6 1 HETATM 3138 O O2 . MAN G 3 . F 42.891 -18.845 68.845 1.00 29.78 ? 474 MAN A O2 1 HETATM 3139 O O3 . MAN G 3 . F 42.250 -20.937 67.121 1.00 30.53 ? 474 MAN A O3 1 HETATM 3140 O O4 . MAN G 3 . F 39.848 -19.551 66.050 1.00 28.91 ? 474 MAN A O4 1 HETATM 3141 O O5 . MAN G 3 . F 42.122 -16.768 66.936 1.00 30.02 ? 474 MAN A O5 1 HETATM 3142 O O6 . MAN G 3 . F 39.613 -16.186 67.681 1.00 32.40 ? 474 MAN A O6 1 HETATM 3143 C C1 . MAN H 3 . G 48.330 -9.574 57.971 1.00 38.50 ? 475 MAN A C1 1 HETATM 3144 C C2 . MAN H 3 . G 49.140 -9.207 59.257 1.00 40.14 ? 475 MAN A C2 1 HETATM 3145 C C3 . MAN H 3 . G 50.124 -8.015 59.067 1.00 43.13 ? 475 MAN A C3 1 HETATM 3146 C C4 . MAN H 3 . G 50.655 -7.825 57.649 1.00 44.47 ? 475 MAN A C4 1 HETATM 3147 C C5 . MAN H 3 . G 49.487 -7.939 56.656 1.00 43.95 ? 475 MAN A C5 1 HETATM 3148 C C6 . MAN H 3 . G 49.783 -7.647 55.170 1.00 45.43 ? 475 MAN A C6 1 HETATM 3149 O O2 . MAN H 3 . G 49.911 -10.282 59.755 1.00 40.55 ? 475 MAN A O2 1 HETATM 3150 O O3 . MAN H 3 . G 51.317 -8.184 59.851 1.00 43.57 ? 475 MAN A O3 1 HETATM 3151 O O4 . MAN H 3 . G 51.272 -6.548 57.644 1.00 49.27 ? 475 MAN A O4 1 HETATM 3152 O O5 . MAN H 3 . G 49.000 -9.273 56.767 1.00 41.61 ? 475 MAN A O5 1 HETATM 3153 O O6 . MAN H 3 . G 49.789 -8.878 54.464 1.00 48.69 ? 475 MAN A O6 1 HETATM 3154 C C1 . NAG I 2 . A 18.987 7.321 81.763 1.00 36.58 ? 476 NAG A C1 1 HETATM 3155 C C2 . NAG I 2 . A 18.132 7.049 82.975 1.00 38.39 ? 476 NAG A C2 1 HETATM 3156 C C3 . NAG I 2 . A 18.838 7.555 84.216 1.00 41.36 ? 476 NAG A C3 1 HETATM 3157 C C4 . NAG I 2 . A 20.209 6.890 84.328 1.00 42.72 ? 476 NAG A C4 1 HETATM 3158 C C5 . NAG I 2 . A 21.029 7.308 83.081 1.00 42.84 ? 476 NAG A C5 1 HETATM 3159 C C6 . NAG I 2 . A 22.480 6.825 83.053 1.00 43.96 ? 476 NAG A C6 1 HETATM 3160 C C7 . NAG I 2 . A 15.711 7.064 82.898 1.00 40.73 ? 476 NAG A C7 1 HETATM 3161 C C8 . NAG I 2 . A 14.395 7.812 82.917 1.00 41.20 ? 476 NAG A C8 1 HETATM 3162 N N2 . NAG I 2 . A 16.852 7.734 82.865 1.00 39.23 ? 476 NAG A N2 1 HETATM 3163 O O3 . NAG I 2 . A 18.118 7.347 85.418 1.00 43.38 ? 476 NAG A O3 1 HETATM 3164 O O4 . NAG I 2 . A 20.764 7.339 85.543 1.00 46.40 ? 476 NAG A O4 1 HETATM 3165 O O5 . NAG I 2 . A 20.318 6.797 81.927 1.00 40.05 ? 476 NAG A O5 1 HETATM 3166 O O6 . NAG I 2 . A 22.907 6.781 81.708 1.00 45.51 ? 476 NAG A O6 1 HETATM 3167 O O7 . NAG I 2 . A 15.720 5.841 82.849 1.00 42.86 ? 476 NAG A O7 1 HETATM 3168 C C1 . NAG J 2 . A 16.880 18.146 29.748 1.00 30.85 ? 477 NAG A C1 1 HETATM 3169 C C2 . NAG J 2 . A 15.717 17.511 29.061 1.00 32.40 ? 477 NAG A C2 1 HETATM 3170 C C3 . NAG J 2 . A 16.232 16.295 28.334 1.00 34.86 ? 477 NAG A C3 1 HETATM 3171 C C4 . NAG J 2 . A 17.301 16.700 27.310 1.00 35.51 ? 477 NAG A C4 1 HETATM 3172 C C5 . NAG J 2 . A 18.439 17.424 28.086 1.00 35.64 ? 477 NAG A C5 1 HETATM 3173 C C6 . NAG J 2 . A 19.598 17.983 27.237 1.00 36.82 ? 477 NAG A C6 1 HETATM 3174 C C7 . NAG J 2 . A 13.468 17.125 29.931 1.00 35.23 ? 477 NAG A C7 1 HETATM 3175 C C8 . NAG J 2 . A 12.577 16.632 31.051 1.00 33.63 ? 477 NAG A C8 1 HETATM 3176 N N2 . NAG J 2 . A 14.787 17.126 30.098 1.00 33.86 ? 477 NAG A N2 1 HETATM 3177 O O3 . NAG J 2 . A 15.202 15.601 27.668 1.00 35.48 ? 477 NAG A O3 1 HETATM 3178 O O4 . NAG J 2 . A 17.730 15.505 26.645 1.00 36.33 ? 477 NAG A O4 1 HETATM 3179 O O5 . NAG J 2 . A 17.871 18.541 28.810 1.00 32.38 ? 477 NAG A O5 1 HETATM 3180 O O6 . NAG J 2 . A 19.145 19.185 26.629 1.00 39.74 ? 477 NAG A O6 1 HETATM 3181 O O7 . NAG J 2 . A 12.967 17.587 28.916 1.00 35.45 ? 477 NAG A O7 1 HETATM 3182 CA CA . CA K 4 . ? 29.264 30.216 62.927 1.00 2.93 ? 18 CA A CA 1 HETATM 3183 O O . HOH L 5 . ? 4.983 14.588 37.218 1.00 29.89 ? 478 HOH A O 1 HETATM 3184 O O . HOH L 5 . ? 20.608 38.860 47.136 1.00 6.25 ? 479 HOH A O 1 HETATM 3185 O O . HOH L 5 . ? -1.412 10.592 59.410 1.00 18.88 ? 480 HOH A O 1 HETATM 3186 O O . HOH L 5 . ? -1.600 12.485 61.576 1.00 41.48 ? 481 HOH A O 1 HETATM 3187 O O . HOH L 5 . ? 6.529 7.183 71.266 1.00 29.06 ? 482 HOH A O 1 HETATM 3188 O O . HOH L 5 . ? 27.655 30.926 59.013 1.00 7.77 ? 483 HOH A O 1 HETATM 3189 O O . HOH L 5 . ? -4.001 17.395 79.551 1.00 49.35 ? 484 HOH A O 1 HETATM 3190 O O . HOH L 5 . ? 27.927 32.086 64.814 1.00 31.01 ? 485 HOH A O 1 HETATM 3191 O O . HOH L 5 . ? 29.856 5.213 68.055 1.00 45.89 ? 486 HOH A O 1 HETATM 3192 O O . HOH L 5 . ? 24.481 16.665 63.609 1.00 35.38 ? 487 HOH A O 1 HETATM 3193 O O . HOH L 5 . ? 20.923 5.639 68.323 1.00 44.01 ? 488 HOH A O 1 HETATM 3194 O O . HOH L 5 . ? 11.391 7.626 45.986 1.00 35.63 ? 489 HOH A O 1 HETATM 3195 O O . HOH L 5 . ? 36.163 9.803 59.316 1.00 4.78 ? 490 HOH A O 1 HETATM 3196 O O . HOH L 5 . ? 40.965 2.962 55.766 1.00 39.98 ? 491 HOH A O 1 HETATM 3197 O O . HOH L 5 . ? 10.333 31.624 35.341 1.00 17.87 ? 492 HOH A O 1 HETATM 3198 O O . HOH L 5 . ? 10.358 33.611 37.318 1.00 31.43 ? 493 HOH A O 1 HETATM 3199 O O . HOH L 5 . ? 40.757 16.160 42.328 1.00 23.81 ? 494 HOH A O 1 HETATM 3200 O O . HOH L 5 . ? 7.386 25.226 41.728 1.00 33.56 ? 495 HOH A O 1 HETATM 3201 O O . HOH L 5 . ? 9.949 12.295 66.840 1.00 9.16 ? 496 HOH A O 1 HETATM 3202 O O . HOH L 5 . ? 2.003 32.435 44.633 1.00 28.71 ? 497 HOH A O 1 HETATM 3203 O O . HOH L 5 . ? 4.982 32.164 44.683 1.00 25.28 ? 498 HOH A O 1 HETATM 3204 O O . HOH L 5 . ? 18.317 19.238 58.484 1.00 16.88 ? 499 HOH A O 1 HETATM 3205 O O . HOH L 5 . ? 23.125 26.844 68.101 1.00 25.78 ? 500 HOH A O 1 HETATM 3206 O O . HOH L 5 . ? 15.391 19.556 51.753 1.00 2.46 ? 501 HOH A O 1 HETATM 3207 O O . HOH L 5 . ? 20.887 38.757 44.482 1.00 19.15 ? 502 HOH A O 1 HETATM 3208 O O . HOH L 5 . ? 22.303 40.943 43.889 1.00 24.77 ? 503 HOH A O 1 HETATM 3209 O O . HOH L 5 . ? 14.421 15.881 44.533 1.00 18.17 ? 504 HOH A O 1 HETATM 3210 O O . HOH L 5 . ? 4.575 39.813 55.525 1.00 36.70 ? 505 HOH A O 1 HETATM 3211 O O . HOH L 5 . ? 20.082 14.091 57.624 1.00 20.40 ? 506 HOH A O 1 HETATM 3212 O O . HOH L 5 . ? 4.115 17.451 37.153 1.00 41.21 ? 507 HOH A O 1 HETATM 3213 O O . HOH L 5 . ? 28.341 19.169 57.124 1.00 22.51 ? 508 HOH A O 1 HETATM 3214 O O . HOH L 5 . ? 23.253 19.894 66.440 1.00 30.04 ? 509 HOH A O 1 HETATM 3215 O O . HOH L 5 . ? 3.733 12.190 50.619 1.00 16.94 ? 510 HOH A O 1 HETATM 3216 O O . HOH L 5 . ? 24.326 14.399 61.745 1.00 29.95 ? 511 HOH A O 1 HETATM 3217 O O . HOH L 5 . ? 17.105 0.739 60.735 1.00 10.98 ? 512 HOH A O 1 HETATM 3218 O O . HOH L 5 . ? 16.731 2.392 62.829 1.00 33.80 ? 513 HOH A O 1 HETATM 3219 O O . HOH L 5 . ? 14.326 3.396 62.684 1.00 22.58 ? 514 HOH A O 1 HETATM 3220 O O . HOH L 5 . ? 12.211 0.180 54.995 1.00 9.79 ? 515 HOH A O 1 HETATM 3221 O O . HOH L 5 . ? -0.574 17.758 52.083 1.00 23.56 ? 516 HOH A O 1 HETATM 3222 O O . HOH L 5 . ? 6.289 4.918 53.486 1.00 22.40 ? 517 HOH A O 1 HETATM 3223 O O . HOH L 5 . ? 0.274 18.969 54.332 1.00 8.87 ? 518 HOH A O 1 HETATM 3224 O O . HOH L 5 . ? -1.308 12.561 73.240 1.00 13.95 ? 519 HOH A O 1 HETATM 3225 O O . HOH L 5 . ? -1.078 10.967 70.903 1.00 24.90 ? 520 HOH A O 1 HETATM 3226 O O . HOH L 5 . ? 17.316 12.684 68.270 1.00 11.17 ? 521 HOH A O 1 HETATM 3227 O O . HOH L 5 . ? 21.334 16.596 69.868 1.00 47.54 ? 522 HOH A O 1 HETATM 3228 O O . HOH L 5 . ? 19.449 19.122 70.951 1.00 50.28 ? 523 HOH A O 1 HETATM 3229 O O . HOH L 5 . ? 20.222 13.912 68.409 1.00 26.65 ? 524 HOH A O 1 HETATM 3230 O O . HOH L 5 . ? 24.262 4.427 61.538 1.00 5.94 ? 525 HOH A O 1 HETATM 3231 O O . HOH L 5 . ? 20.932 1.433 62.052 1.00 6.06 ? 526 HOH A O 1 HETATM 3232 O O . HOH L 5 . ? 26.278 4.265 54.708 1.00 14.63 ? 527 HOH A O 1 HETATM 3233 O O . HOH L 5 . ? 28.853 3.800 55.479 1.00 34.35 ? 528 HOH A O 1 HETATM 3234 O O . HOH L 5 . ? 24.214 1.758 53.025 1.00 53.18 ? 529 HOH A O 1 HETATM 3235 O O . HOH L 5 . ? 31.684 -0.709 58.733 1.00 38.36 ? 530 HOH A O 1 HETATM 3236 O O . HOH L 5 . ? 12.498 29.178 31.032 1.00 61.25 ? 531 HOH A O 1 HETATM 3237 O O . HOH L 5 . ? 30.761 2.016 58.792 1.00 6.58 ? 532 HOH A O 1 HETATM 3238 O O . HOH L 5 . ? 32.725 -0.772 56.170 1.00 24.41 ? 533 HOH A O 1 HETATM 3239 O O . HOH L 5 . ? 33.264 2.886 57.550 1.00 3.42 ? 534 HOH A O 1 HETATM 3240 O O . HOH L 5 . ? 38.057 25.097 56.377 1.00 36.59 ? 535 HOH A O 1 HETATM 3241 O O . HOH L 5 . ? 35.607 23.666 55.284 1.00 24.07 ? 536 HOH A O 1 HETATM 3242 O O . HOH L 5 . ? 11.627 14.697 62.114 1.00 23.62 ? 537 HOH A O 1 HETATM 3243 O O . HOH L 5 . ? 1.383 6.818 76.584 1.00 35.66 ? 538 HOH A O 1 HETATM 3244 O O . HOH L 5 . ? -0.748 3.960 72.163 1.00 21.07 ? 539 HOH A O 1 HETATM 3245 O O . HOH L 5 . ? 13.709 8.390 77.991 1.00 13.63 ? 540 HOH A O 1 HETATM 3246 O O . HOH L 5 . ? 16.323 17.572 41.665 1.00 14.52 ? 541 HOH A O 1 HETATM 3247 O O . HOH L 5 . ? 16.220 18.242 44.370 1.00 8.39 ? 542 HOH A O 1 HETATM 3248 O O . HOH L 5 . ? 16.081 18.430 39.268 1.00 20.26 ? 543 HOH A O 1 HETATM 3249 O O . HOH L 5 . ? 37.170 10.328 45.832 1.00 29.11 ? 544 HOH A O 1 HETATM 3250 O O . HOH L 5 . ? 23.268 20.025 46.017 1.00 12.37 ? 545 HOH A O 1 HETATM 3251 O O . HOH L 5 . ? 16.098 22.686 46.204 1.00 6.41 ? 546 HOH A O 1 HETATM 3252 O O . HOH L 5 . ? 21.917 11.299 38.423 1.00 7.84 ? 547 HOH A O 1 HETATM 3253 O O . HOH L 5 . ? 29.739 19.820 54.782 1.00 12.10 ? 548 HOH A O 1 HETATM 3254 O O . HOH L 5 . ? 38.232 24.133 42.867 1.00 27.77 ? 549 HOH A O 1 HETATM 3255 O O . HOH L 5 . ? 19.986 28.290 50.589 1.00 15.83 ? 550 HOH A O 1 HETATM 3256 O O . HOH L 5 . ? 24.304 35.790 57.276 1.00 16.25 ? 551 HOH A O 1 HETATM 3257 O O . HOH L 5 . ? 24.353 38.291 56.468 1.00 17.17 ? 552 HOH A O 1 HETATM 3258 O O . HOH L 5 . ? 19.705 31.958 62.883 1.00 15.63 ? 553 HOH A O 1 HETATM 3259 O O . HOH L 5 . ? 18.654 30.461 58.471 1.00 4.84 ? 554 HOH A O 1 HETATM 3260 O O . HOH L 5 . ? 17.603 23.270 71.145 1.00 19.89 ? 555 HOH A O 1 HETATM 3261 O O . HOH L 5 . ? 22.184 39.763 65.360 1.00 22.51 ? 556 HOH A O 1 HETATM 3262 O O . HOH L 5 . ? 31.036 45.488 60.520 1.00 53.68 ? 557 HOH A O 1 HETATM 3263 O O . HOH L 5 . ? 10.059 39.638 61.502 1.00 18.20 ? 558 HOH A O 1 HETATM 3264 O O . HOH L 5 . ? 3.869 33.254 58.388 1.00 36.82 ? 559 HOH A O 1 HETATM 3265 O O . HOH L 5 . ? 8.463 24.435 69.118 1.00 22.61 ? 560 HOH A O 1 HETATM 3266 O O . HOH L 5 . ? 17.076 21.451 73.333 1.00 16.24 ? 561 HOH A O 1 HETATM 3267 O O . HOH L 5 . ? 13.941 22.053 73.335 1.00 21.97 ? 562 HOH A O 1 HETATM 3268 O O . HOH L 5 . ? 20.025 21.721 70.421 1.00 23.11 ? 563 HOH A O 1 HETATM 3269 O O . HOH L 5 . ? 8.942 15.101 62.861 1.00 28.20 ? 564 HOH A O 1 HETATM 3270 O O . HOH L 5 . ? 5.107 19.778 63.777 1.00 17.93 ? 565 HOH A O 1 HETATM 3271 O O . HOH L 5 . ? -2.990 18.655 77.342 1.00 29.86 ? 566 HOH A O 1 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ARG 1 82 82 ARG ARG A . n A 1 2 ASP 2 83 83 ASP ASP A . n A 1 3 PHE 3 84 84 PHE PHE A . n A 1 4 ASN 4 85 85 ASN ASN A . n A 1 5 ASN 5 86 86 ASN ASN A . n A 1 6 LEU 6 87 87 LEU LEU A . n A 1 7 THR 7 88 88 THR THR A . n A 1 8 LYS 8 89 89 LYS LYS A . n A 1 9 GLY 9 90 90 GLY GLY A . n A 1 10 LEU 10 91 91 LEU LEU A . n A 1 11 CYS 11 92 92 CYS CYS A . n A 1 12 THR 12 93 93 THR THR A . n A 1 13 ILE 13 94 94 ILE ILE A . n A 1 14 ASN 14 95 95 ASN ASN A . n A 1 15 SER 15 96 96 SER SER A . n A 1 16 TRP 16 97 97 TRP TRP A . n A 1 17 HIS 17 98 98 HIS HIS A . n A 1 18 ILE 18 99 99 ILE ILE A . n A 1 19 TYR 19 100 100 TYR TYR A . n A 1 20 GLY 20 101 101 GLY GLY A . n A 1 21 LYS 21 102 102 LYS LYS A . n A 1 22 ASP 22 103 103 ASP ASP A . n A 1 23 ASN 23 104 104 ASN ASN A . n A 1 24 ALA 24 105 105 ALA ALA A . n A 1 25 VAL 25 106 106 VAL VAL A . n A 1 26 ARG 26 107 107 ARG ARG A . n A 1 27 ILE 27 108 108 ILE ILE A . n A 1 28 GLY 28 109 109 GLY GLY A . n A 1 29 GLU 29 110 110 GLU GLU A . n A 1 30 ASP 30 111 111 ASP ASP A . n A 1 31 SER 31 112 112 SER SER A . n A 1 32 ASP 32 113 113 ASP ASP A . n A 1 33 VAL 33 114 114 VAL VAL A . n A 1 34 LEU 34 115 115 LEU LEU A . n A 1 35 VAL 35 116 116 VAL VAL A . n A 1 36 THR 36 117 117 THR THR A . n A 1 37 ARG 37 118 118 ARG ARG A . n A 1 38 GLU 38 119 119 GLU GLU A . n A 1 39 PRO 39 120 120 PRO PRO A . n A 1 40 TYR 40 121 121 TYR TYR A . n A 1 41 VAL 41 122 122 VAL VAL A . n A 1 42 SER 42 123 123 SER SER A . n A 1 43 CYS 43 124 124 CYS CYS A . n A 1 44 ASP 44 125 125 ASP ASP A . n A 1 45 PRO 45 126 126 PRO PRO A . n A 1 46 ASP 46 127 127 ASP ASP A . n A 1 47 GLU 47 128 128 GLU GLU A . n A 1 48 CYS 48 129 129 CYS CYS A . n A 1 49 ARG 49 130 130 ARG ARG A . n A 1 50 PHE 50 131 131 PHE PHE A . n A 1 51 TYR 51 132 132 TYR TYR A . n A 1 52 ALA 52 133 133 ALA ALA A . n A 1 53 LEU 53 134 134 LEU LEU A . n A 1 54 SER 54 135 135 SER SER A . n A 1 55 GLN 55 136 136 GLN GLN A . n A 1 56 GLY 56 137 137 GLY GLY A . n A 1 57 THR 57 138 138 THR THR A . n A 1 58 THR 58 139 139 THR THR A . n A 1 59 ILE 59 140 140 ILE ILE A . n A 1 60 ARG 60 141 141 ARG ARG A . n A 1 61 GLY 61 142 142 GLY GLY A . n A 1 62 LYS 62 143 143 LYS LYS A . n A 1 63 HIS 63 144 144 HIS HIS A . n A 1 64 SER 64 145 145 SER SER A . n A 1 65 ASN 65 146 146 ASN ASN A . n A 1 66 GLY 66 147 147 GLY GLY A . n A 1 67 THR 67 148 148 THR THR A . n A 1 68 ILE 68 149 149 ILE ILE A . n A 1 69 HIS 69 150 150 HIS HIS A . n A 1 70 ASP 70 151 151 ASP ASP A . n A 1 71 ARG 71 152 152 ARG ARG A . n A 1 72 SER 72 153 153 SER SER A . n A 1 73 GLN 73 154 154 GLN GLN A . n A 1 74 TYR 74 155 155 TYR TYR A . n A 1 75 ARG 75 156 156 ARG ARG A . n A 1 76 ALA 76 157 157 ALA ALA A . n A 1 77 LEU 77 158 158 LEU LEU A . n A 1 78 ILE 78 159 159 ILE ILE A . n A 1 79 SER 79 160 160 SER SER A . n A 1 80 TRP 80 161 161 TRP TRP A . n A 1 81 PRO 81 162 162 PRO PRO A . n A 1 82 LEU 82 163 163 LEU LEU A . n A 1 83 SER 83 164 164 SER SER A . n A 1 84 SER 84 165 165 SER SER A . n A 1 85 PRO 85 166 166 PRO PRO A . n A 1 86 PRO 86 167 167 PRO PRO A . n A 1 87 THR 87 168 168 THR THR A . n A 1 88 VAL 88 169 169 VAL VAL A . n A 1 89 TYR 89 169 169 TYR TYR A A n A 1 90 ASN 90 170 170 ASN ASN A . n A 1 91 SER 91 171 171 SER SER A . n A 1 92 ARG 92 172 172 ARG ARG A . n A 1 93 VAL 93 173 173 VAL VAL A . n A 1 94 GLU 94 174 174 GLU GLU A . n A 1 95 CYS 95 175 175 CYS CYS A . n A 1 96 ILE 96 176 176 ILE ILE A . n A 1 97 GLY 97 177 177 GLY GLY A . n A 1 98 TRP 98 178 178 TRP TRP A . n A 1 99 SER 99 179 179 SER SER A . n A 1 100 SER 100 180 180 SER SER A . n A 1 101 THR 101 181 181 THR THR A . n A 1 102 SER 102 182 182 SER SER A . n A 1 103 CYS 103 183 183 CYS CYS A . n A 1 104 HIS 104 184 184 HIS HIS A . n A 1 105 ASP 105 185 185 ASP ASP A . n A 1 106 GLY 106 186 186 GLY GLY A . n A 1 107 LYS 107 187 187 LYS LYS A . n A 1 108 THR 108 188 188 THR THR A . n A 1 109 ARG 109 189 189 ARG ARG A . n A 1 110 MET 110 190 190 MET MET A . n A 1 111 SER 111 191 191 SER SER A . n A 1 112 ILE 112 192 192 ILE ILE A . n A 1 113 CYS 113 193 193 CYS CYS A . n A 1 114 ILE 114 194 194 ILE ILE A . n A 1 115 SER 115 195 195 SER SER A . n A 1 116 GLY 116 196 196 GLY GLY A . n A 1 117 PRO 117 197 197 PRO PRO A . n A 1 118 ASN 118 198 198 ASN ASN A . n A 1 119 ASN 119 199 199 ASN ASN A . n A 1 120 ASN 120 200 200 ASN ASN A . n A 1 121 ALA 121 201 201 ALA ALA A . n A 1 122 SER 122 202 202 SER SER A . n A 1 123 ALA 123 203 203 ALA ALA A . n A 1 124 VAL 124 204 204 VAL VAL A . n A 1 125 ILE 125 205 205 ILE ILE A . n A 1 126 TRP 126 206 206 TRP TRP A . n A 1 127 TYR 127 207 207 TYR TYR A . n A 1 128 ASN 128 208 208 ASN ASN A . n A 1 129 ARG 129 209 209 ARG ARG A . n A 1 130 ARG 130 210 210 ARG ARG A . n A 1 131 PRO 131 211 211 PRO PRO A . n A 1 132 VAL 132 212 212 VAL VAL A . n A 1 133 THR 133 213 213 THR THR A . n A 1 134 GLU 134 214 214 GLU GLU A . n A 1 135 ILE 135 215 215 ILE ILE A . n A 1 136 ASN 136 216 216 ASN ASN A . n A 1 137 THR 137 217 217 THR THR A . n A 1 138 TRP 138 218 218 TRP TRP A . n A 1 139 ALA 139 219 219 ALA ALA A . n A 1 140 ARG 140 220 220 ARG ARG A . n A 1 141 ASN 141 221 221 ASN ASN A . n A 1 142 ILE 142 222 222 ILE ILE A . n A 1 143 LEU 143 223 223 LEU LEU A . n A 1 144 ARG 144 224 224 ARG ARG A . n A 1 145 THR 145 225 225 THR THR A . n A 1 146 GLN 146 226 226 GLN GLN A . n A 1 147 GLU 147 227 227 GLU GLU A . n A 1 148 SER 148 228 228 SER SER A . n A 1 149 GLU 149 229 229 GLU GLU A . n A 1 150 CYS 150 230 230 CYS CYS A . n A 1 151 VAL 151 231 231 VAL VAL A . n A 1 152 CYS 152 232 232 CYS CYS A . n A 1 153 HIS 153 233 233 HIS HIS A . n A 1 154 ASN 154 234 234 ASN ASN A . n A 1 155 GLY 155 235 235 GLY GLY A . n A 1 156 VAL 156 236 236 VAL VAL A . n A 1 157 CYS 157 237 237 CYS CYS A . n A 1 158 PRO 158 238 238 PRO PRO A . n A 1 159 VAL 159 239 239 VAL VAL A . n A 1 160 VAL 160 240 240 VAL VAL A . n A 1 161 PHE 161 241 241 PHE PHE A . n A 1 162 THR 162 242 242 THR THR A . n A 1 163 ASP 163 243 243 ASP ASP A . n A 1 164 GLY 164 244 244 GLY GLY A . n A 1 165 SER 165 245 245 SER SER A . n A 1 166 ALA 166 246 246 ALA ALA A . n A 1 167 THR 167 247 247 THR THR A . n A 1 168 GLY 168 248 248 GLY GLY A . n A 1 169 PRO 169 249 249 PRO PRO A . n A 1 170 ALA 170 250 250 ALA ALA A . n A 1 171 GLU 171 251 251 GLU GLU A . n A 1 172 THR 172 252 252 THR THR A . n A 1 173 ARG 173 253 253 ARG ARG A . n A 1 174 ILE 174 254 254 ILE ILE A . n A 1 175 TYR 175 255 255 TYR TYR A . n A 1 176 TYR 176 256 256 TYR TYR A . n A 1 177 PHE 177 257 257 PHE PHE A . n A 1 178 LYS 178 258 258 LYS LYS A . n A 1 179 GLU 179 259 259 GLU GLU A . n A 1 180 GLY 180 260 260 GLY GLY A . n A 1 181 LYS 181 261 261 LYS LYS A . n A 1 182 ILE 182 262 262 ILE ILE A . n A 1 183 LEU 183 263 263 LEU LEU A . n A 1 184 LYS 184 264 264 LYS LYS A . n A 1 185 TRP 185 265 265 TRP TRP A . n A 1 186 GLU 186 266 266 GLU GLU A . n A 1 187 PRO 187 267 267 PRO PRO A . n A 1 188 LEU 188 268 268 LEU LEU A . n A 1 189 ALA 189 269 269 ALA ALA A . n A 1 190 GLY 190 270 270 GLY GLY A . n A 1 191 THR 191 271 271 THR THR A . n A 1 192 ALA 192 272 272 ALA ALA A . n A 1 193 LYS 193 273 273 LYS LYS A . n A 1 194 HIS 194 274 274 HIS HIS A . n A 1 195 ILE 195 275 275 ILE ILE A . n A 1 196 GLU 196 276 276 GLU GLU A . n A 1 197 GLU 197 277 277 GLU GLU A . n A 1 198 CYS 198 278 278 CYS CYS A . n A 1 199 SER 199 279 279 SER SER A . n A 1 200 CYS 200 280 280 CYS CYS A . n A 1 201 TYR 201 281 281 TYR TYR A . n A 1 202 GLY 202 282 282 GLY GLY A . n A 1 203 GLU 203 283 283 GLU GLU A . n A 1 204 ARG 204 284 284 ARG ARG A . n A 1 205 ALA 205 285 285 ALA ALA A . n A 1 206 GLU 206 286 286 GLU GLU A . n A 1 207 ILE 207 287 287 ILE ILE A . n A 1 208 THR 208 288 288 THR THR A . n A 1 209 CYS 209 289 289 CYS CYS A . n A 1 210 THR 210 290 290 THR THR A . n A 1 211 CYS 211 291 291 CYS CYS A . n A 1 212 ARG 212 292 292 ARG ARG A . n A 1 213 ASP 213 293 293 ASP ASP A . n A 1 214 ASN 214 294 294 ASN ASN A . n A 1 215 TRP 215 295 295 TRP TRP A . n A 1 216 GLN 216 296 296 GLN GLN A . n A 1 217 GLY 217 297 297 GLY GLY A . n A 1 218 SER 218 298 298 SER SER A . n A 1 219 ASN 219 299 299 ASN ASN A . n A 1 220 ARG 220 300 300 ARG ARG A . n A 1 221 PRO 221 301 301 PRO PRO A . n A 1 222 VAL 222 302 302 VAL VAL A . n A 1 223 ILE 223 303 303 ILE ILE A . n A 1 224 ARG 224 304 304 ARG ARG A . n A 1 225 ILE 225 305 305 ILE ILE A . n A 1 226 ASP 226 306 306 ASP ASP A . n A 1 227 PRO 227 307 307 PRO PRO A . n A 1 228 VAL 228 308 308 VAL VAL A . n A 1 229 ALA 229 309 309 ALA ALA A . n A 1 230 MET 230 310 310 MET MET A . n A 1 231 THR 231 311 311 THR THR A . n A 1 232 HIS 232 312 312 HIS HIS A . n A 1 233 THR 233 313 313 THR THR A . n A 1 234 SER 234 314 314 SER SER A . n A 1 235 GLN 235 315 315 GLN GLN A . n A 1 236 TYR 236 316 316 TYR TYR A . n A 1 237 ILE 237 317 317 ILE ILE A . n A 1 238 CYS 238 318 318 CYS CYS A . n A 1 239 SER 239 319 319 SER SER A . n A 1 240 PRO 240 320 320 PRO PRO A . n A 1 241 VAL 241 321 321 VAL VAL A . n A 1 242 LEU 242 322 322 LEU LEU A . n A 1 243 THR 243 323 323 THR THR A . n A 1 244 ASP 244 324 324 ASP ASP A . n A 1 245 ASN 245 325 325 ASN ASN A . n A 1 246 PRO 246 326 326 PRO PRO A . n A 1 247 ARG 247 327 327 ARG ARG A . n A 1 248 PRO 248 328 328 PRO PRO A . n A 1 249 ASN 249 329 329 ASN ASN A . n A 1 250 ASP 250 330 330 ASP ASP A . n A 1 251 PRO 251 331 331 PRO PRO A . n A 1 252 THR 252 332 332 THR THR A . n A 1 253 VAL 253 333 333 VAL VAL A . n A 1 254 GLY 254 335 335 GLY GLY A . n A 1 255 LYS 255 336 336 LYS LYS A . n A 1 256 CYS 256 337 337 CYS CYS A . n A 1 257 ASN 257 338 338 ASN ASN A . n A 1 258 ASP 258 339 339 ASP ASP A . n A 1 259 PRO 259 340 340 PRO PRO A . n A 1 260 TYR 260 341 341 TYR TYR A . n A 1 261 PRO 261 342 342 PRO PRO A . n A 1 262 GLY 262 343 343 GLY GLY A . n A 1 263 ASN 263 344 344 ASN ASN A . n A 1 264 ASN 264 345 345 ASN ASN A . n A 1 265 ASN 265 346 346 ASN ASN A . n A 1 266 ASN 266 347 347 ASN ASN A . n A 1 267 GLY 267 348 348 GLY GLY A . n A 1 268 VAL 268 349 349 VAL VAL A . n A 1 269 LYS 269 350 350 LYS LYS A . n A 1 270 GLY 270 351 351 GLY GLY A . n A 1 271 PHE 271 352 352 PHE PHE A . n A 1 272 SER 272 353 353 SER SER A . n A 1 273 TYR 273 354 354 TYR TYR A . n A 1 274 LEU 274 355 355 LEU LEU A . n A 1 275 ASP 275 356 356 ASP ASP A . n A 1 276 GLY 276 357 357 GLY GLY A . n A 1 277 VAL 277 358 358 VAL VAL A . n A 1 278 ASN 278 359 359 ASN ASN A . n A 1 279 THR 279 360 360 THR THR A . n A 1 280 TRP 280 361 361 TRP TRP A . n A 1 281 LEU 281 362 362 LEU LEU A . n A 1 282 GLY 282 363 363 GLY GLY A . n A 1 283 ARG 283 364 364 ARG ARG A . n A 1 284 THR 284 365 365 THR THR A . n A 1 285 ILE 285 366 366 ILE ILE A . n A 1 286 SER 286 367 367 SER SER A . n A 1 287 ARG 287 368 368 ARG ARG A . n A 1 288 ALA 288 369 369 ALA ALA A . n A 1 289 SER 289 370 370 SER SER A . n A 1 290 ARG 290 371 371 ARG ARG A . n A 1 291 SER 291 372 372 SER SER A . n A 1 292 GLY 292 373 373 GLY GLY A . n A 1 293 TYR 293 374 374 TYR TYR A . n A 1 294 GLU 294 375 375 GLU GLU A . n A 1 295 MET 295 376 376 MET MET A . n A 1 296 LEU 296 377 377 LEU LEU A . n A 1 297 LYS 297 378 378 LYS LYS A . n A 1 298 VAL 298 379 379 VAL VAL A . n A 1 299 PRO 299 380 380 PRO PRO A . n A 1 300 ASN 300 381 381 ASN ASN A . n A 1 301 ALA 301 382 382 ALA ALA A . n A 1 302 LEU 302 383 383 LEU LEU A . n A 1 303 THR 303 384 384 THR THR A . n A 1 304 ASP 304 385 385 ASP ASP A . n A 1 305 ASP 305 386 386 ASP ASP A . n A 1 306 LYS 306 387 387 LYS LYS A . n A 1 307 SER 307 388 388 SER SER A . n A 1 308 LYS 308 389 389 LYS LYS A . n A 1 309 PRO 309 390 390 PRO PRO A . n A 1 310 THR 310 391 391 THR THR A . n A 1 311 GLN 311 392 392 GLN GLN A . n A 1 312 GLY 312 394 394 GLY GLY A . n A 1 313 GLN 313 395 395 GLN GLN A . n A 1 314 THR 314 396 396 THR THR A . n A 1 315 ILE 315 397 397 ILE ILE A . n A 1 316 VAL 316 398 398 VAL VAL A . n A 1 317 LEU 317 399 399 LEU LEU A . n A 1 318 ASN 318 400 400 ASN ASN A . n A 1 319 THR 319 401 401 THR THR A . n A 1 320 ASP 320 402 402 ASP ASP A . n A 1 321 TRP 321 403 403 TRP TRP A . n A 1 322 SER 322 404 404 SER SER A . n A 1 323 GLY 323 405 405 GLY GLY A . n A 1 324 TYR 324 406 406 TYR TYR A . n A 1 325 SER 325 407 407 SER SER A . n A 1 326 GLY 326 408 408 GLY GLY A . n A 1 327 SER 327 409 409 SER SER A . n A 1 328 PHE 328 410 410 PHE PHE A . n A 1 329 MET 329 411 411 MET MET A . n A 1 330 ASP 330 412 412 ASP ASP A . n A 1 331 TYR 331 412 412 TYR TYR A A n A 1 332 TRP 332 412 412 TRP TRP A B n A 1 333 ALA 333 413 413 ALA ALA A . n A 1 334 GLU 334 414 414 GLU GLU A . n A 1 335 GLY 335 415 415 GLY GLY A . n A 1 336 GLU 336 416 416 GLU GLU A . n A 1 337 CYS 337 417 417 CYS CYS A . n A 1 338 TYR 338 418 418 TYR TYR A . n A 1 339 ARG 339 419 419 ARG ARG A . n A 1 340 ALA 340 420 420 ALA ALA A . n A 1 341 CYS 341 421 421 CYS CYS A . n A 1 342 PHE 342 422 422 PHE PHE A . n A 1 343 TYR 343 423 423 TYR TYR A . n A 1 344 VAL 344 424 424 VAL VAL A . n A 1 345 GLU 345 425 425 GLU GLU A . n A 1 346 LEU 346 426 426 LEU LEU A . n A 1 347 ILE 347 427 427 ILE ILE A . n A 1 348 ARG 348 428 428 ARG ARG A . n A 1 349 GLY 349 429 429 GLY GLY A . n A 1 350 ARG 350 430 430 ARG ARG A . n A 1 351 PRO 351 431 431 PRO PRO A . n A 1 352 LYS 352 432 432 LYS LYS A . n A 1 353 GLU 353 433 433 GLU GLU A . n A 1 354 ASP 354 434 434 ASP ASP A . n A 1 355 LYS 355 435 435 LYS LYS A . n A 1 356 VAL 356 436 436 VAL VAL A . n A 1 357 TRP 357 437 437 TRP TRP A . n A 1 358 TRP 358 438 438 TRP TRP A . n A 1 359 THR 359 439 439 THR THR A . n A 1 360 SER 360 440 440 SER SER A . n A 1 361 ASN 361 441 441 ASN ASN A . n A 1 362 SER 362 442 442 SER SER A . n A 1 363 ILE 363 443 443 ILE ILE A . n A 1 364 VAL 364 444 444 VAL VAL A . n A 1 365 SER 365 445 445 SER SER A . n A 1 366 MET 366 446 446 MET MET A . n A 1 367 CYS 367 447 447 CYS CYS A . n A 1 368 SER 368 448 448 SER SER A . n A 1 369 SER 369 449 449 SER SER A . n A 1 370 THR 370 450 450 THR THR A . n A 1 371 GLU 371 451 451 GLU GLU A . n A 1 372 PHE 372 452 452 PHE PHE A . n A 1 373 LEU 373 453 453 LEU LEU A . n A 1 374 GLY 374 454 454 GLY GLY A . n A 1 375 GLN 375 455 455 GLN GLN A . n A 1 376 TRP 376 456 456 TRP TRP A . n A 1 377 ASP 377 457 457 ASP ASP A . n A 1 378 TRP 378 458 458 TRP TRP A . n A 1 379 PRO 379 459 459 PRO PRO A . n A 1 380 ASP 380 460 460 ASP ASP A . n A 1 381 GLY 381 461 461 GLY GLY A . n A 1 382 ALA 382 462 462 ALA ALA A . n A 1 383 LYS 383 463 463 LYS LYS A . n A 1 384 ILE 384 464 464 ILE ILE A . n A 1 385 GLU 385 465 465 GLU GLU A . n A 1 386 TYR 386 466 466 TYR TYR A . n A 1 387 PHE 387 467 467 PHE PHE A . n A 1 388 LEU 388 468 468 LEU LEU A . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 NAG 1 469 200 NAG NAG A A C 2 NAG 2 470 200 NAG NAG A B D 3 MAN 3 471 200 MAN MAN A C E 3 MAN 4 472 200 MAN MAN A D F 3 MAN 5 473 200 MAN MAN A E G 3 MAN 6 474 200 MAN MAN A F H 3 MAN 7 475 200 MAN MAN A G I 2 NAG 1 476 146 NAG NAG A A J 2 NAG 1 477 86 NAG NAG A A K 4 CA 1 18 18 CA CA A . L 5 HOH 1 478 1 HOH HOH A . L 5 HOH 2 479 2 HOH HOH A . L 5 HOH 3 480 3 HOH HOH A . L 5 HOH 4 481 4 HOH HOH A . L 5 HOH 5 482 5 HOH HOH A . L 5 HOH 6 483 6 HOH HOH A . L 5 HOH 7 484 7 HOH HOH A . L 5 HOH 8 485 8 HOH HOH A . L 5 HOH 9 486 9 HOH HOH A . L 5 HOH 10 487 10 HOH HOH A . L 5 HOH 11 488 11 HOH HOH A . L 5 HOH 12 489 12 HOH HOH A . L 5 HOH 13 490 13 HOH HOH A . L 5 HOH 14 491 14 HOH HOH A . L 5 HOH 15 492 15 HOH HOH A . L 5 HOH 16 493 16 HOH HOH A . L 5 HOH 17 494 17 HOH HOH A . L 5 HOH 18 495 19 HOH HOH A . L 5 HOH 19 496 20 HOH HOH A . L 5 HOH 20 497 21 HOH HOH A . L 5 HOH 21 498 22 HOH HOH A . L 5 HOH 22 499 23 HOH HOH A . L 5 HOH 23 500 24 HOH HOH A . L 5 HOH 24 501 25 HOH HOH A . L 5 HOH 25 502 26 HOH HOH A . L 5 HOH 26 503 27 HOH HOH A . L 5 HOH 27 504 28 HOH HOH A . L 5 HOH 28 505 29 HOH HOH A . L 5 HOH 29 506 30 HOH HOH A . L 5 HOH 30 507 31 HOH HOH A . L 5 HOH 31 508 32 HOH HOH A . L 5 HOH 32 509 33 HOH HOH A . L 5 HOH 33 510 34 HOH HOH A . L 5 HOH 34 511 35 HOH HOH A . L 5 HOH 35 512 36 HOH HOH A . L 5 HOH 36 513 37 HOH HOH A . L 5 HOH 37 514 38 HOH HOH A . L 5 HOH 38 515 39 HOH HOH A . L 5 HOH 39 516 40 HOH HOH A . L 5 HOH 40 517 41 HOH HOH A . L 5 HOH 41 518 42 HOH HOH A . L 5 HOH 42 519 43 HOH HOH A . L 5 HOH 43 520 44 HOH HOH A . L 5 HOH 44 521 45 HOH HOH A . L 5 HOH 45 522 46 HOH HOH A . L 5 HOH 46 523 47 HOH HOH A . L 5 HOH 47 524 48 HOH HOH A . L 5 HOH 48 525 49 HOH HOH A . L 5 HOH 49 526 50 HOH HOH A . L 5 HOH 50 527 51 HOH HOH A . L 5 HOH 51 528 52 HOH HOH A . L 5 HOH 52 529 53 HOH HOH A . L 5 HOH 53 530 54 HOH HOH A . L 5 HOH 54 531 55 HOH HOH A . L 5 HOH 55 532 56 HOH HOH A . L 5 HOH 56 533 57 HOH HOH A . L 5 HOH 57 534 58 HOH HOH A . L 5 HOH 58 535 59 HOH HOH A . L 5 HOH 59 536 60 HOH HOH A . L 5 HOH 60 537 61 HOH HOH A . L 5 HOH 61 538 62 HOH HOH A . L 5 HOH 62 539 63 HOH HOH A . L 5 HOH 63 540 64 HOH HOH A . L 5 HOH 64 541 65 HOH HOH A . L 5 HOH 65 542 66 HOH HOH A . L 5 HOH 66 543 67 HOH HOH A . L 5 HOH 67 544 68 HOH HOH A . L 5 HOH 68 545 69 HOH HOH A . L 5 HOH 69 546 70 HOH HOH A . L 5 HOH 70 547 71 HOH HOH A . L 5 HOH 71 548 72 HOH HOH A . L 5 HOH 72 549 73 HOH HOH A . L 5 HOH 73 550 74 HOH HOH A . L 5 HOH 74 551 75 HOH HOH A . L 5 HOH 75 552 76 HOH HOH A . L 5 HOH 76 553 77 HOH HOH A . L 5 HOH 77 554 78 HOH HOH A . L 5 HOH 78 555 79 HOH HOH A . L 5 HOH 79 556 80 HOH HOH A . L 5 HOH 80 557 81 HOH HOH A . L 5 HOH 81 558 82 HOH HOH A . L 5 HOH 82 559 83 HOH HOH A . L 5 HOH 83 560 84 HOH HOH A . L 5 HOH 84 561 85 HOH HOH A . L 5 HOH 85 562 86 HOH HOH A . L 5 HOH 86 563 87 HOH HOH A . L 5 HOH 87 564 88 HOH HOH A . L 5 HOH 88 565 89 HOH HOH A . L 5 HOH 89 566 90 HOH HOH A . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 5 A ASN 86 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 65 A ASN 146 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 120 A ASN 200 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_defined_assembly _pdbx_struct_assembly.method_details ? _pdbx_struct_assembly.oligomeric_details tetrameric _pdbx_struct_assembly.oligomeric_count 4 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2,3,4 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 15_555 y,-x,z 0.0000000000 1.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 3 'crystal symmetry operation' 16_555 -y,x,z 0.0000000000 -1.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 4 'crystal symmetry operation' 2_555 -x,-y,z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 # 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 OD2 ? A ASP 244 ? A ASP 324 ? 1_555 CA ? K CA . ? A CA 18 ? 1_555 O ? A GLY 217 ? A GLY 297 ? 1_555 89.4 ? 2 OD2 ? A ASP 244 ? A ASP 324 ? 1_555 CA ? K CA . ? A CA 18 ? 1_555 O ? A ASN 266 ? A ASN 347 ? 1_555 95.5 ? 3 O ? A GLY 217 ? A GLY 297 ? 1_555 CA ? K CA . ? A CA 18 ? 1_555 O ? A ASN 266 ? A ASN 347 ? 1_555 153.6 ? 4 OD2 ? A ASP 244 ? A ASP 324 ? 1_555 CA ? K CA . ? A CA 18 ? 1_555 O ? A ASP 213 ? A ASP 293 ? 1_555 99.6 ? 5 O ? A GLY 217 ? A GLY 297 ? 1_555 CA ? K CA . ? A CA 18 ? 1_555 O ? A ASP 213 ? A ASP 293 ? 1_555 97.5 ? 6 O ? A ASN 266 ? A ASN 347 ? 1_555 CA ? K CA . ? A CA 18 ? 1_555 O ? A ASP 213 ? A ASP 293 ? 1_555 107.1 ? 7 OD2 ? A ASP 244 ? A ASP 324 ? 1_555 CA ? K CA . ? A CA 18 ? 1_555 O ? L HOH . ? A HOH 485 ? 1_555 83.3 ? 8 O ? A GLY 217 ? A GLY 297 ? 1_555 CA ? K CA . ? A CA 18 ? 1_555 O ? L HOH . ? A HOH 485 ? 1_555 76.4 ? 9 O ? A ASN 266 ? A ASN 347 ? 1_555 CA ? K CA . ? A CA 18 ? 1_555 O ? L HOH . ? A HOH 485 ? 1_555 78.5 ? 10 O ? A ASP 213 ? A ASP 293 ? 1_555 CA ? K CA . ? A CA 18 ? 1_555 O ? L HOH . ? A HOH 485 ? 1_555 173.3 ? # 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 1992-07-15 2 'Structure model' 1 1 2008-03-25 3 'Structure model' 1 2 2011-07-13 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Source and taxonomy' 3 3 'Structure model' 'Version format compliance' # _software.name X-PLOR _software.classification refinement _software.version . _software.citation_id ? _software.pdbx_ordinal 1 # 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 OH A TYR 466 ? ? O A HOH 566 ? ? 1.67 2 1 OH A TYR 466 ? ? O A HOH 484 ? ? 1.86 # _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_1 557 _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_2 557 _pdbx_validate_symm_contact.PDB_ins_code_2 ? _pdbx_validate_symm_contact.label_alt_id_2 ? _pdbx_validate_symm_contact.site_symmetry_2 48_555 _pdbx_validate_symm_contact.dist 2.11 # loop_ _pdbx_validate_rmsd_bond.id _pdbx_validate_rmsd_bond.PDB_model_num _pdbx_validate_rmsd_bond.auth_atom_id_1 _pdbx_validate_rmsd_bond.auth_asym_id_1 _pdbx_validate_rmsd_bond.auth_comp_id_1 _pdbx_validate_rmsd_bond.auth_seq_id_1 _pdbx_validate_rmsd_bond.PDB_ins_code_1 _pdbx_validate_rmsd_bond.label_alt_id_1 _pdbx_validate_rmsd_bond.auth_atom_id_2 _pdbx_validate_rmsd_bond.auth_asym_id_2 _pdbx_validate_rmsd_bond.auth_comp_id_2 _pdbx_validate_rmsd_bond.auth_seq_id_2 _pdbx_validate_rmsd_bond.PDB_ins_code_2 _pdbx_validate_rmsd_bond.label_alt_id_2 _pdbx_validate_rmsd_bond.bond_value _pdbx_validate_rmsd_bond.bond_target_value _pdbx_validate_rmsd_bond.bond_deviation _pdbx_validate_rmsd_bond.bond_standard_deviation _pdbx_validate_rmsd_bond.linker_flag 1 1 NE2 A HIS 184 ? ? CD2 A HIS 184 ? ? 1.307 1.373 -0.066 0.011 N 2 1 NE2 A HIS 233 ? ? CD2 A HIS 233 ? ? 1.297 1.373 -0.076 0.011 N 3 1 NE2 A HIS 274 ? ? CD2 A HIS 274 ? ? 1.300 1.373 -0.073 0.011 N 4 1 NE2 A HIS 312 ? ? CD2 A HIS 312 ? ? 1.302 1.373 -0.071 0.011 N # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 NE A ARG 82 ? ? CZ A ARG 82 ? ? NH1 A ARG 82 ? ? 123.55 120.30 3.25 0.50 N 2 1 CD1 A TRP 97 ? ? CG A TRP 97 ? ? CD2 A TRP 97 ? ? 113.45 106.30 7.15 0.80 N 3 1 CE2 A TRP 97 ? ? CD2 A TRP 97 ? ? CG A TRP 97 ? ? 101.24 107.30 -6.06 0.80 N 4 1 CB A TYR 121 ? ? CG A TYR 121 ? ? CD2 A TYR 121 ? ? 116.17 121.00 -4.83 0.60 N 5 1 NE A ARG 141 ? ? CZ A ARG 141 ? ? NH1 A ARG 141 ? ? 123.63 120.30 3.33 0.50 N 6 1 NE A ARG 156 ? ? CZ A ARG 156 ? ? NH1 A ARG 156 ? ? 123.63 120.30 3.33 0.50 N 7 1 CD1 A TRP 161 ? ? CG A TRP 161 ? ? CD2 A TRP 161 ? ? 111.41 106.30 5.11 0.80 N 8 1 CB A TRP 161 ? ? CG A TRP 161 ? ? CD1 A TRP 161 ? ? 118.57 127.00 -8.43 1.30 N 9 1 CE2 A TRP 161 ? ? CD2 A TRP 161 ? ? CG A TRP 161 ? ? 101.83 107.30 -5.47 0.80 N 10 1 CG A TRP 161 ? ? CD2 A TRP 161 ? ? CE3 A TRP 161 ? ? 139.44 133.90 5.54 0.90 N 11 1 CA A CYS 175 ? ? CB A CYS 175 ? ? SG A CYS 175 ? ? 125.45 114.20 11.25 1.10 N 12 1 CD1 A TRP 178 ? ? CG A TRP 178 ? ? CD2 A TRP 178 ? ? 112.56 106.30 6.26 0.80 N 13 1 CG A TRP 178 ? ? CD1 A TRP 178 ? ? NE1 A TRP 178 ? ? 104.03 110.10 -6.07 1.00 N 14 1 CE2 A TRP 178 ? ? CD2 A TRP 178 ? ? CG A TRP 178 ? ? 101.88 107.30 -5.42 0.80 N 15 1 CA A CYS 193 ? ? CB A CYS 193 ? ? SG A CYS 193 ? ? 122.55 114.20 8.35 1.10 N 16 1 CD1 A TRP 206 ? ? CG A TRP 206 ? ? CD2 A TRP 206 ? ? 112.65 106.30 6.35 0.80 N 17 1 CD1 A TRP 218 ? ? CG A TRP 218 ? ? CD2 A TRP 218 ? ? 112.21 106.30 5.91 0.80 N 18 1 CE2 A TRP 218 ? ? CD2 A TRP 218 ? ? CG A TRP 218 ? ? 101.32 107.30 -5.98 0.80 N 19 1 NE A ARG 220 ? ? CZ A ARG 220 ? ? NH1 A ARG 220 ? ? 125.70 120.30 5.40 0.50 N 20 1 NE A ARG 220 ? ? CZ A ARG 220 ? ? NH2 A ARG 220 ? ? 113.82 120.30 -6.48 0.50 N 21 1 N A THR 247 ? ? CA A THR 247 ? ? CB A THR 247 ? ? 97.72 110.30 -12.58 1.90 N 22 1 NE A ARG 253 ? ? CZ A ARG 253 ? ? NH1 A ARG 253 ? ? 123.33 120.30 3.03 0.50 N 23 1 CD1 A TRP 265 ? ? CG A TRP 265 ? ? CD2 A TRP 265 ? ? 112.37 106.30 6.07 0.80 N 24 1 CE2 A TRP 265 ? ? CD2 A TRP 265 ? ? CG A TRP 265 ? ? 101.49 107.30 -5.81 0.80 N 25 1 CG A TRP 265 ? ? CD2 A TRP 265 ? ? CE3 A TRP 265 ? ? 141.30 133.90 7.40 0.90 N 26 1 NE A ARG 284 ? ? CZ A ARG 284 ? ? NH1 A ARG 284 ? ? 124.38 120.30 4.08 0.50 N 27 1 NE A ARG 284 ? ? CZ A ARG 284 ? ? NH2 A ARG 284 ? ? 116.61 120.30 -3.69 0.50 N 28 1 CD1 A TRP 295 ? ? CG A TRP 295 ? ? CD2 A TRP 295 ? ? 111.48 106.30 5.18 0.80 N 29 1 CE2 A TRP 295 ? ? CD2 A TRP 295 ? ? CG A TRP 295 ? ? 101.87 107.30 -5.43 0.80 N 30 1 CD1 A TRP 361 ? ? CG A TRP 361 ? ? CD2 A TRP 361 ? ? 112.48 106.30 6.18 0.80 N 31 1 CE2 A TRP 361 ? ? CD2 A TRP 361 ? ? CG A TRP 361 ? ? 100.41 107.30 -6.89 0.80 N 32 1 CG A TRP 361 ? ? CD2 A TRP 361 ? ? CE3 A TRP 361 ? ? 141.88 133.90 7.98 0.90 N 33 1 NE A ARG 364 ? ? CZ A ARG 364 ? ? NH1 A ARG 364 ? ? 127.04 120.30 6.74 0.50 N 34 1 NE A ARG 364 ? ? CZ A ARG 364 ? ? NH2 A ARG 364 ? ? 115.30 120.30 -5.00 0.50 N 35 1 CG A TYR 374 ? ? CD1 A TYR 374 ? ? CE1 A TYR 374 ? ? 115.13 121.30 -6.17 0.80 N 36 1 CD1 A TRP 403 ? ? CG A TRP 403 ? ? CD2 A TRP 403 ? ? 113.77 106.30 7.47 0.80 N 37 1 CE2 A TRP 403 ? ? CD2 A TRP 403 ? ? CG A TRP 403 ? ? 100.63 107.30 -6.67 0.80 N 38 1 CB A TYR 406 ? ? CG A TYR 406 ? ? CD2 A TYR 406 ? ? 115.28 121.00 -5.72 0.60 N 39 1 CB A TYR 406 ? ? CG A TYR 406 ? ? CD1 A TYR 406 ? ? 124.84 121.00 3.84 0.60 N 40 1 CE2 A TRP 412 B ? CD2 A TRP 412 B ? CG A TRP 412 B ? 102.04 107.30 -5.26 0.80 N 41 1 CG A TRP 412 B ? CD2 A TRP 412 B ? CE3 A TRP 412 B ? 139.69 133.90 5.79 0.90 N 42 1 NE A ARG 419 ? ? CZ A ARG 419 ? ? NH1 A ARG 419 ? ? 127.17 120.30 6.87 0.50 N 43 1 NE A ARG 419 ? ? CZ A ARG 419 ? ? NH2 A ARG 419 ? ? 116.22 120.30 -4.08 0.50 N 44 1 CA A CYS 421 ? ? CB A CYS 421 ? ? SG A CYS 421 ? ? 127.81 114.20 13.61 1.10 N 45 1 NE A ARG 428 ? ? CZ A ARG 428 ? ? NH1 A ARG 428 ? ? 123.61 120.30 3.31 0.50 N 46 1 CD1 A TRP 437 ? ? CG A TRP 437 ? ? CD2 A TRP 437 ? ? 112.13 106.30 5.83 0.80 N 47 1 CE2 A TRP 437 ? ? CD2 A TRP 437 ? ? CG A TRP 437 ? ? 101.56 107.30 -5.74 0.80 N 48 1 CD1 A TRP 438 ? ? CG A TRP 438 ? ? CD2 A TRP 438 ? ? 113.02 106.30 6.72 0.80 N 49 1 CB A TRP 438 ? ? CG A TRP 438 ? ? CD1 A TRP 438 ? ? 117.90 127.00 -9.10 1.30 N 50 1 CE2 A TRP 438 ? ? CD2 A TRP 438 ? ? CG A TRP 438 ? ? 99.90 107.30 -7.40 0.80 N 51 1 CG A TRP 438 ? ? CD2 A TRP 438 ? ? CE3 A TRP 438 ? ? 143.03 133.90 9.13 0.90 N 52 1 CG A MET 446 ? ? SD A MET 446 ? ? CE A MET 446 ? ? 88.13 100.20 -12.07 1.60 N 53 1 CD1 A TRP 456 ? ? CG A TRP 456 ? ? CD2 A TRP 456 ? ? 111.73 106.30 5.43 0.80 N 54 1 CE2 A TRP 456 ? ? CD2 A TRP 456 ? ? CG A TRP 456 ? ? 102.10 107.30 -5.20 0.80 N 55 1 CD1 A TRP 458 ? ? CG A TRP 458 ? ? CD2 A TRP 458 ? ? 111.78 106.30 5.48 0.80 N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 LEU A 87 ? ? -68.92 81.99 2 1 TYR A 100 ? ? -114.75 -73.45 3 1 ASP A 111 ? ? -155.73 40.95 4 1 ARG A 118 ? ? -170.54 -172.98 5 1 GLU A 119 ? ? 38.95 55.78 6 1 CYS A 175 ? ? 179.24 166.69 7 1 ASN A 200 ? ? -164.66 53.57 8 1 ARG A 209 ? ? 55.35 15.55 9 1 ILE A 222 ? ? 38.67 85.88 10 1 THR A 225 ? ? -131.56 -156.38 11 1 ARG A 284 ? ? 29.93 60.85 12 1 CYS A 291 ? ? -112.00 -165.19 13 1 SER A 404 ? ? -128.06 -127.18 14 1 GLU A 433 ? ? -106.33 72.32 # _pdbx_validate_planes.id 1 _pdbx_validate_planes.PDB_model_num 1 _pdbx_validate_planes.auth_comp_id TYR _pdbx_validate_planes.auth_asym_id A _pdbx_validate_planes.auth_seq_id 423 _pdbx_validate_planes.PDB_ins_code ? _pdbx_validate_planes.label_alt_id ? _pdbx_validate_planes.rmsd 0.082 _pdbx_validate_planes.type 'SIDE CHAIN' # _pdbx_validate_chiral.id 1 _pdbx_validate_chiral.PDB_model_num 1 _pdbx_validate_chiral.auth_atom_id C1 _pdbx_validate_chiral.label_alt_id ? _pdbx_validate_chiral.auth_asym_id A _pdbx_validate_chiral.auth_comp_id MAN _pdbx_validate_chiral.auth_seq_id 471 _pdbx_validate_chiral.PDB_ins_code C _pdbx_validate_chiral.details 'WRONG HAND' _pdbx_validate_chiral.omega . # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 ALPHA-D-MANNOSE MAN 4 'CALCIUM ION' CA 5 water HOH #