data_1CB2 # _entry.id 1CB2 # _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 1CB2 WWPDB D_1000172204 # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 1CB2 _pdbx_database_status.recvd_initial_deposition_date 1995-11-25 _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 'Kleywegt, G.J.' 1 'Szardenings, M.' 2 'Jones, T.A.' 3 # 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 'The active site of Trichoderma reesei cellobiohydrolase II: the role of tyrosine 169.' 'Protein Eng.' 9 691 699 1996 PRENE9 UK 0269-2139 0859 ? 8875646 10.1093/protein/9.8.691 1 'Three-Dimensional Structure of Cellobiohydrolase II from Trichoderma Reesei' Science 249 380 ? 1990 SCIEAS US 0036-8075 0038 ? ? ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Koivula, A.' 1 primary 'Reinikainen, T.' 2 primary 'Ruohonen, L.' 3 primary 'Valkeajarvi, A.' 4 primary 'Claeyssens, M.' 5 primary 'Teleman, O.' 6 primary 'Kleywegt, G.J.' 7 primary 'Szardenings, M.' 8 primary 'Rouvinen, J.' 9 primary 'Jones, T.A.' 10 primary 'Teeri, T.T.' 11 1 'Rouvinen, J.' 12 1 'Bergfors, T.' 13 1 'Teeri, T.' 14 1 'Knowles, J.K.' 15 1 'Jones, T.A.' 16 # _cell.entry_id 1CB2 _cell.length_a 49.100 _cell.length_b 75.800 _cell.length_c 92.900 _cell.angle_alpha 90.00 _cell.angle_beta 103.20 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1CB2 _symmetry.space_group_name_H-M 'P 1 21 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 4 # 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 'CELLOBIOHYDROLASE II' 39039.297 2 3.2.1.91 Y169F CATALYTIC ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? 3 non-polymer man ALPHA-D-MANNOSE 180.156 14 ? ? ? ? 4 water nat water 18.015 392 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'CBH II (Y169F)' # _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 ;SGTATYSGNPFVGVTPWANAYYASEVSSLAIPSLTGAMATAAAAVAKVPSFMWLDTLDKTPLMEQTLADIRTANKNGGNY AGQFVVFDLPDRDCAALASNGEYSIADGGVAKYKNYIDTIRQIVVEYSDIRTLLVIEPDSLANLVTNLGTPKCANAQSAY LECINYAVTQLNLPNVAMYLDAGHAGWLGWPANQDPAAQLFANVYKNASSPRALRGLATNVANYNGWNITSPPSYTQGNA VYNEKLYIHAIGPLLANHGWSNAFFITDQGRSGKQPTGQQQWGDWCNVIGTGFGIRPSANTGDSLLDSFVWVKPGGECDG TSDSSAPRFDSHCALPDALQPAPQAGAWFQAYFVQLLTNANPSFL ; _entity_poly.pdbx_seq_one_letter_code_can ;SGTATYSGNPFVGVTPWANAYYASEVSSLAIPSLTGAMATAAAAVAKVPSFMWLDTLDKTPLMEQTLADIRTANKNGGNY AGQFVVFDLPDRDCAALASNGEYSIADGGVAKYKNYIDTIRQIVVEYSDIRTLLVIEPDSLANLVTNLGTPKCANAQSAY LECINYAVTQLNLPNVAMYLDAGHAGWLGWPANQDPAAQLFANVYKNASSPRALRGLATNVANYNGWNITSPPSYTQGNA VYNEKLYIHAIGPLLANHGWSNAFFITDQGRSGKQPTGQQQWGDWCNVIGTGFGIRPSANTGDSLLDSFVWVKPGGECDG TSDSSAPRFDSHCALPDALQPAPQAGAWFQAYFVQLLTNANPSFL ; _entity_poly.pdbx_strand_id A,B _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 SER n 1 2 GLY n 1 3 THR n 1 4 ALA n 1 5 THR n 1 6 TYR n 1 7 SER n 1 8 GLY n 1 9 ASN n 1 10 PRO n 1 11 PHE n 1 12 VAL n 1 13 GLY n 1 14 VAL n 1 15 THR n 1 16 PRO n 1 17 TRP n 1 18 ALA n 1 19 ASN n 1 20 ALA n 1 21 TYR n 1 22 TYR n 1 23 ALA n 1 24 SER n 1 25 GLU n 1 26 VAL n 1 27 SER n 1 28 SER n 1 29 LEU n 1 30 ALA n 1 31 ILE n 1 32 PRO n 1 33 SER n 1 34 LEU n 1 35 THR n 1 36 GLY n 1 37 ALA n 1 38 MET n 1 39 ALA n 1 40 THR n 1 41 ALA n 1 42 ALA n 1 43 ALA n 1 44 ALA n 1 45 VAL n 1 46 ALA n 1 47 LYS n 1 48 VAL n 1 49 PRO n 1 50 SER n 1 51 PHE n 1 52 MET n 1 53 TRP n 1 54 LEU n 1 55 ASP n 1 56 THR n 1 57 LEU n 1 58 ASP n 1 59 LYS n 1 60 THR n 1 61 PRO n 1 62 LEU n 1 63 MET n 1 64 GLU n 1 65 GLN n 1 66 THR n 1 67 LEU n 1 68 ALA n 1 69 ASP n 1 70 ILE n 1 71 ARG n 1 72 THR n 1 73 ALA n 1 74 ASN n 1 75 LYS n 1 76 ASN n 1 77 GLY n 1 78 GLY n 1 79 ASN n 1 80 TYR n 1 81 ALA n 1 82 GLY n 1 83 GLN n 1 84 PHE n 1 85 VAL n 1 86 VAL n 1 87 PHE n 1 88 ASP n 1 89 LEU n 1 90 PRO n 1 91 ASP n 1 92 ARG n 1 93 ASP n 1 94 CYS n 1 95 ALA n 1 96 ALA n 1 97 LEU n 1 98 ALA n 1 99 SER n 1 100 ASN n 1 101 GLY n 1 102 GLU n 1 103 TYR n 1 104 SER n 1 105 ILE n 1 106 ALA n 1 107 ASP n 1 108 GLY n 1 109 GLY n 1 110 VAL n 1 111 ALA n 1 112 LYS n 1 113 TYR n 1 114 LYS n 1 115 ASN n 1 116 TYR n 1 117 ILE n 1 118 ASP n 1 119 THR n 1 120 ILE n 1 121 ARG n 1 122 GLN n 1 123 ILE n 1 124 VAL n 1 125 VAL n 1 126 GLU n 1 127 TYR n 1 128 SER n 1 129 ASP n 1 130 ILE n 1 131 ARG n 1 132 THR n 1 133 LEU n 1 134 LEU n 1 135 VAL n 1 136 ILE n 1 137 GLU n 1 138 PRO n 1 139 ASP n 1 140 SER n 1 141 LEU n 1 142 ALA n 1 143 ASN n 1 144 LEU n 1 145 VAL n 1 146 THR n 1 147 ASN n 1 148 LEU n 1 149 GLY n 1 150 THR n 1 151 PRO n 1 152 LYS n 1 153 CYS n 1 154 ALA n 1 155 ASN n 1 156 ALA n 1 157 GLN n 1 158 SER n 1 159 ALA n 1 160 TYR n 1 161 LEU n 1 162 GLU n 1 163 CYS n 1 164 ILE n 1 165 ASN n 1 166 TYR n 1 167 ALA n 1 168 VAL n 1 169 THR n 1 170 GLN n 1 171 LEU n 1 172 ASN n 1 173 LEU n 1 174 PRO n 1 175 ASN n 1 176 VAL n 1 177 ALA n 1 178 MET n 1 179 TYR n 1 180 LEU n 1 181 ASP n 1 182 ALA n 1 183 GLY n 1 184 HIS n 1 185 ALA n 1 186 GLY n 1 187 TRP n 1 188 LEU n 1 189 GLY n 1 190 TRP n 1 191 PRO n 1 192 ALA n 1 193 ASN n 1 194 GLN n 1 195 ASP n 1 196 PRO n 1 197 ALA n 1 198 ALA n 1 199 GLN n 1 200 LEU n 1 201 PHE n 1 202 ALA n 1 203 ASN n 1 204 VAL n 1 205 TYR n 1 206 LYS n 1 207 ASN n 1 208 ALA n 1 209 SER n 1 210 SER n 1 211 PRO n 1 212 ARG n 1 213 ALA n 1 214 LEU n 1 215 ARG n 1 216 GLY n 1 217 LEU n 1 218 ALA n 1 219 THR n 1 220 ASN n 1 221 VAL n 1 222 ALA n 1 223 ASN n 1 224 TYR n 1 225 ASN n 1 226 GLY n 1 227 TRP n 1 228 ASN n 1 229 ILE n 1 230 THR n 1 231 SER n 1 232 PRO n 1 233 PRO n 1 234 SER n 1 235 TYR n 1 236 THR n 1 237 GLN n 1 238 GLY n 1 239 ASN n 1 240 ALA n 1 241 VAL n 1 242 TYR n 1 243 ASN n 1 244 GLU n 1 245 LYS n 1 246 LEU n 1 247 TYR n 1 248 ILE n 1 249 HIS n 1 250 ALA n 1 251 ILE n 1 252 GLY n 1 253 PRO n 1 254 LEU n 1 255 LEU n 1 256 ALA n 1 257 ASN n 1 258 HIS n 1 259 GLY n 1 260 TRP n 1 261 SER n 1 262 ASN n 1 263 ALA n 1 264 PHE n 1 265 PHE n 1 266 ILE n 1 267 THR n 1 268 ASP n 1 269 GLN n 1 270 GLY n 1 271 ARG n 1 272 SER n 1 273 GLY n 1 274 LYS n 1 275 GLN n 1 276 PRO n 1 277 THR n 1 278 GLY n 1 279 GLN n 1 280 GLN n 1 281 GLN n 1 282 TRP n 1 283 GLY n 1 284 ASP n 1 285 TRP n 1 286 CYS n 1 287 ASN n 1 288 VAL n 1 289 ILE n 1 290 GLY n 1 291 THR n 1 292 GLY n 1 293 PHE n 1 294 GLY n 1 295 ILE n 1 296 ARG n 1 297 PRO n 1 298 SER n 1 299 ALA n 1 300 ASN n 1 301 THR n 1 302 GLY n 1 303 ASP n 1 304 SER n 1 305 LEU n 1 306 LEU n 1 307 ASP n 1 308 SER n 1 309 PHE n 1 310 VAL n 1 311 TRP n 1 312 VAL n 1 313 LYS n 1 314 PRO n 1 315 GLY n 1 316 GLY n 1 317 GLU n 1 318 CYS n 1 319 ASP n 1 320 GLY n 1 321 THR n 1 322 SER n 1 323 ASP n 1 324 SER n 1 325 SER n 1 326 ALA n 1 327 PRO n 1 328 ARG n 1 329 PHE n 1 330 ASP n 1 331 SER n 1 332 HIS n 1 333 CYS n 1 334 ALA n 1 335 LEU n 1 336 PRO n 1 337 ASP n 1 338 ALA n 1 339 LEU n 1 340 GLN n 1 341 PRO n 1 342 ALA n 1 343 PRO n 1 344 GLN n 1 345 ALA n 1 346 GLY n 1 347 ALA n 1 348 TRP n 1 349 PHE n 1 350 GLN n 1 351 ALA n 1 352 TYR n 1 353 PHE n 1 354 VAL n 1 355 GLN n 1 356 LEU n 1 357 LEU n 1 358 THR n 1 359 ASN n 1 360 ALA n 1 361 ASN n 1 362 PRO n 1 363 SER n 1 364 PHE n 1 365 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 Hypocrea _entity_src_gen.pdbx_gene_src_gene 'CBH2 (Y169F)' _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'Hypocrea jecorina' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 51453 _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 'Hypocrea jecorina' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 51453 _entity_src_gen.host_org_genus Hypocrea _entity_src_gen.pdbx_host_org_gene 'CBH2 (Y169F)' _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 GUX2_TRIRE _struct_ref.entity_id 1 _struct_ref.pdbx_db_accession P07987 _struct_ref.pdbx_align_begin 1 _struct_ref.pdbx_seq_one_letter_code ;MIVGILTTLATLATLAASVPLEERQACSSVWGQCGGQNWSGPTCCASGSTCVYSNDYYSQCLPGAASSSSSTRAASTTSR VSPTTSRSSSATPPPGSTTTRVPPVGSGTATYSGNPFVGVTPWANAYYASEVSSLAIPSLTGAMATAAAAVAKVPSFMWL DTLDKTPLMEQTLADIRTANKNGGNYAGQFVVYDLPDRDCAALASNGEYSIADGGVAKYKNYIDTIRQIVVEYSDIRTLL VIEPDSLANLVTNLGTPKCANAQSAYLECINYAVTQLNLPNVAMYLDAGHAGWLGWPANQDPAAQLFANVYKNASSPRAL RGLATNVANYNGWNITSPPSYTQGNAVYNEKLYIHAIGPLLANHGWSNAFFITDQGRSGKQPTGQQQWGDWCNVIGTGFG IRPSANTGDSLLDSFVWVKPGGECDGTSDSSAPRFDSHCALPDALQPAPQAGAWFQAYFVQLLTNANPSFL ; _struct_ref.pdbx_db_isoform ? # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 1CB2 A 1 ? 365 ? P07987 107 ? 471 ? 83 447 2 1 1CB2 B 1 ? 365 ? P07987 107 ? 471 ? 83 447 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 1CB2 PHE A 87 ? UNP P07987 TYR 193 ENGINEERED 169 1 2 1CB2 PHE B 87 ? UNP P07987 TYR 193 ENGINEERED 169 2 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 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 1CB2 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number ? # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.15 _exptl_crystal.density_percent_sol 42.91 _exptl_crystal.description ? # _diffrn.id 1 _diffrn.ambient_temp ? _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector 'AREA DETECTOR' _diffrn_detector.type 'XUONG-HAMLIN MULTIWIRE' _diffrn_detector.pdbx_collection_date 1993-04-02 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol ? _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.5418 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source ? _diffrn_source.type ? _diffrn_source.pdbx_synchrotron_site ? _diffrn_source.pdbx_synchrotron_beamline ? _diffrn_source.pdbx_wavelength 1.5418 _diffrn_source.pdbx_wavelength_list ? # _reflns.entry_id 1CB2 _reflns.observed_criterion_sigma_I ? _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low ? _reflns.d_resolution_high ? _reflns.number_obs 46849 _reflns.number_all ? _reflns.percent_possible_obs 91.7 _reflns.pdbx_Rmerge_I_obs 0.068 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 4.3 _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _refine.entry_id 1CB2 _refine.ls_number_reflns_obs 40828 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0.0 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 8.0 _refine.ls_d_res_high 2.0 _refine.ls_percent_reflns_obs 91.7 _refine.ls_R_factor_obs 0.21 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.21 _refine.ls_R_factor_R_free 0.232 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 10. _refine.ls_number_reflns_R_free ? _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.B_iso_mean 15.8 _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 ? _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 5492 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 210 _refine_hist.number_atoms_solvent 392 _refine_hist.number_atoms_total 6094 _refine_hist.d_res_high 2.0 _refine_hist.d_res_low 8.0 # 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 0.005 ? ? ? '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 1.25 ? ? ? 'X-RAY DIFFRACTION' ? x_angle_deg_na ? ? ? ? 'X-RAY DIFFRACTION' ? x_angle_deg_prot ? ? ? ? 'X-RAY DIFFRACTION' ? x_dihedral_angle_d 24.0 ? ? ? 'X-RAY DIFFRACTION' ? x_dihedral_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? x_dihedral_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? x_improper_angle_d 1.11 ? ? ? '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_ncs_oper.id 1 _struct_ncs_oper.code given _struct_ncs_oper.details ? _struct_ncs_oper.matrix[1][1] 0.994635 _struct_ncs_oper.matrix[1][2] -0.096273 _struct_ncs_oper.matrix[1][3] -0.037846 _struct_ncs_oper.matrix[2][1] 0.097060 _struct_ncs_oper.matrix[2][2] 0.995086 _struct_ncs_oper.matrix[2][3] 0.019549 _struct_ncs_oper.matrix[3][1] 0.035779 _struct_ncs_oper.matrix[3][2] -0.023118 _struct_ncs_oper.matrix[3][3] 0.999092 _struct_ncs_oper.vector[1] 20.01249 _struct_ncs_oper.vector[2] 45.14702 _struct_ncs_oper.vector[3] 45.34660 # _struct.entry_id 1CB2 _struct.title 'CELLOBIOHYDROLASE II, CATALYTIC DOMAIN, MUTANT Y169F' _struct.pdbx_descriptor 'CELLOBIOHYDROLASE II' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1CB2 _struct_keywords.pdbx_keywords 'HYDROLASE (O-GLYCOSYL)' _struct_keywords.text 'HYDROLASE (O-GLYCOSYL), GLYCOSIDASE, GLYCOPROTEIN' # 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 1 ? C N N 2 ? D N N 2 ? E N N 3 ? F N N 3 ? G N N 3 ? H N N 3 ? I N N 3 ? J N N 3 ? K N N 3 ? L N N 2 ? M N N 2 ? N N N 3 ? O N N 3 ? P N N 3 ? Q N N 3 ? R N N 3 ? S N N 3 ? T N N 3 ? U N N 4 ? V N N 4 ? # loop_ _struct_biol.id 1 2 # 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 ALA A 20 ? LEU A 29 ? ALA A 102 LEU A 111 1 ? 10 HELX_P HELX_P2 2 ILE A 31 ? SER A 33 ? ILE A 113 SER A 115 5 ? 3 HELX_P HELX_P3 3 GLY A 36 ? LYS A 47 ? GLY A 118 LYS A 129 1 ? 12 HELX_P HELX_P4 4 LEU A 57 ? LYS A 75 ? LEU A 139 LYS A 157 5 ? 19 HELX_P HELX_P5 5 ILE A 105 ? ASP A 107 ? ILE A 187 ASP A 189 5 ? 3 HELX_P HELX_P6 6 GLY A 109 ? GLU A 126 ? GLY A 191 GLU A 208 1 ? 18 HELX_P HELX_P7 7 LEU A 141 ? THR A 146 ? LEU A 223 THR A 228 5 ? 6 HELX_P HELX_P8 8 PRO A 151 ? GLN A 170 ? PRO A 233 GLN A 252 1 ? 20 HELX_P HELX_P9 9 PRO A 191 ? ASN A 207 ? PRO A 273 ASN A 289 1 ? 17 HELX_P HELX_P10 10 SER A 234 ? THR A 236 ? SER A 316 THR A 318 5 ? 3 HELX_P HELX_P11 11 GLU A 244 ? HIS A 258 ? GLU A 326 HIS A 340 1 ? 15 HELX_P HELX_P12 12 SER A 331 ? ALA A 334 ? SER A 413 ALA A 416 5 ? 4 HELX_P HELX_P13 13 GLN A 350 ? THR A 358 ? GLN A 432 THR A 440 1 ? 9 HELX_P HELX_P14 14 ALA B 20 ? LEU B 29 ? ALA B 102 LEU B 111 1 ? 10 HELX_P HELX_P15 15 ILE B 31 ? SER B 33 ? ILE B 113 SER B 115 5 ? 3 HELX_P HELX_P16 16 GLY B 36 ? LYS B 47 ? GLY B 118 LYS B 129 1 ? 12 HELX_P HELX_P17 17 LEU B 57 ? LYS B 75 ? LEU B 139 LYS B 157 5 ? 19 HELX_P HELX_P18 18 ILE B 105 ? ASP B 107 ? ILE B 187 ASP B 189 5 ? 3 HELX_P HELX_P19 19 GLY B 109 ? GLU B 126 ? GLY B 191 GLU B 208 1 ? 18 HELX_P HELX_P20 20 LEU B 141 ? THR B 146 ? LEU B 223 THR B 228 5 ? 6 HELX_P HELX_P21 21 PRO B 151 ? GLN B 170 ? PRO B 233 GLN B 252 1 ? 20 HELX_P HELX_P22 22 PRO B 191 ? ASN B 207 ? PRO B 273 ASN B 289 1 ? 17 HELX_P HELX_P23 23 SER B 234 ? THR B 236 ? SER B 316 THR B 318 5 ? 3 HELX_P HELX_P24 24 GLU B 244 ? HIS B 258 ? GLU B 326 HIS B 340 1 ? 15 HELX_P HELX_P25 25 SER B 331 ? ALA B 334 ? SER B 413 ALA B 416 5 ? 4 HELX_P HELX_P26 26 GLN B 350 ? THR B 358 ? GLN B 432 THR B 440 1 ? 9 # _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 94 SG ? ? ? 1_555 A CYS 153 SG ? ? A CYS 176 A CYS 235 1_555 ? ? ? ? ? ? ? 2.029 ? disulf2 disulf ? ? A CYS 286 SG ? ? ? 1_555 A CYS 333 SG ? ? A CYS 368 A CYS 415 1_555 ? ? ? ? ? ? ? 2.030 ? disulf3 disulf ? ? B CYS 94 SG ? ? ? 1_555 B CYS 153 SG ? ? B CYS 176 B CYS 235 1_555 ? ? ? ? ? ? ? 2.029 ? disulf4 disulf ? ? B CYS 286 SG ? ? ? 1_555 B CYS 333 SG ? ? B CYS 368 B CYS 415 1_555 ? ? ? ? ? ? ? 2.030 ? covale1 covale ? ? C NAG . C1 ? ? ? 1_555 A ASN 207 ND2 ? ? A NAG 501 A ASN 289 1_555 ? ? ? ? ? ? ? 1.454 ? covale2 covale ? ? D NAG . C1 ? ? ? 1_555 A ASN 228 ND2 ? ? A NAG 502 A ASN 310 1_555 ? ? ? ? ? ? ? 1.448 ? covale3 covale ? ? E MAN . C1 ? ? ? 1_555 A THR 5 OG1 ? ? A MAN 503 A THR 87 1_555 ? ? ? ? ? ? ? 1.435 ? covale4 covale ? ? F MAN . C1 ? ? ? 1_555 A THR 15 OG1 ? ? A MAN 504 A THR 97 1_555 ? ? ? ? ? ? ? 1.434 ? covale5 covale ? ? G MAN . C1 ? ? ? 1_555 A SER 24 OG ? ? A MAN 505 A SER 106 1_555 ? ? ? ? ? ? ? 1.428 ? covale6 covale ? ? H MAN . C1 ? ? ? 1_555 A SER 27 OG ? ? A MAN 506 A SER 109 1_555 ? ? ? ? ? ? ? 1.425 ? covale7 covale ? ? I MAN . C1 ? ? ? 1_555 A SER 28 OG ? ? A MAN 507 A SER 110 1_555 ? ? ? ? ? ? ? 1.426 ? covale8 covale ? ? J MAN . C1 ? ? ? 1_555 A SER 33 OG ? ? A MAN 508 A SER 115 1_555 ? ? ? ? ? ? ? 1.426 ? covale9 covale ? ? K MAN . C1 ? ? ? 1_555 A THR 40 OG1 ? ? A MAN 509 A THR 122 1_555 ? ? ? ? ? ? ? 1.432 ? covale10 covale ? ? L NAG . C1 ? ? ? 1_555 B ASN 207 ND2 ? ? B NAG 501 B ASN 289 1_555 ? ? ? ? ? ? ? 1.454 ? covale11 covale ? ? M NAG . C1 ? ? ? 1_555 B ASN 228 ND2 ? ? B NAG 502 B ASN 310 1_555 ? ? ? ? ? ? ? 1.448 ? covale12 covale ? ? N MAN . C1 ? ? ? 1_555 B THR 5 OG1 ? ? B MAN 503 B THR 87 1_555 ? ? ? ? ? ? ? 1.434 ? covale13 covale ? ? O MAN . C1 ? ? ? 1_555 B THR 15 OG1 ? ? B MAN 504 B THR 97 1_555 ? ? ? ? ? ? ? 1.434 ? covale14 covale ? ? P MAN . C1 ? ? ? 1_555 B SER 24 OG ? ? B MAN 505 B SER 106 1_555 ? ? ? ? ? ? ? 1.429 ? covale15 covale ? ? Q MAN . C1 ? ? ? 1_555 B SER 27 OG ? ? B MAN 506 B SER 109 1_555 ? ? ? ? ? ? ? 1.425 ? covale16 covale ? ? R MAN . C1 ? ? ? 1_555 B SER 28 OG ? ? B MAN 507 B SER 110 1_555 ? ? ? ? ? ? ? 1.427 ? covale17 covale ? ? S MAN . C1 ? ? ? 1_555 B SER 33 OG ? ? B MAN 508 B SER 115 1_555 ? ? ? ? ? ? ? 1.426 ? covale18 covale ? ? T MAN . C1 ? ? ? 1_555 B THR 40 OG1 ? ? B MAN 509 B THR 122 1_555 ? ? ? ? ? ? ? 1.432 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 GLN 275 A . ? GLN 357 A PRO 276 A ? PRO 358 A 1 -0.67 2 GLN 340 A . ? GLN 422 A PRO 341 A ? PRO 423 A 1 -0.39 3 ASN 361 A . ? ASN 443 A PRO 362 A ? PRO 444 A 1 0.49 4 GLN 275 B . ? GLN 357 B PRO 276 B ? PRO 358 B 1 -0.65 5 GLN 340 B . ? GLN 422 B PRO 341 B ? PRO 423 B 1 -0.31 6 ASN 361 B . ? ASN 443 B PRO 362 B ? PRO 444 B 1 0.49 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 7 ? B ? 7 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? parallel A 2 3 ? parallel A 3 4 ? parallel A 4 5 ? parallel A 5 6 ? parallel A 6 7 ? parallel B 1 2 ? parallel B 2 3 ? parallel B 3 4 ? parallel B 4 5 ? parallel B 5 6 ? parallel B 6 7 ? 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 MET A 52 ? LEU A 54 ? MET A 134 LEU A 136 A 2 GLY A 82 ? VAL A 86 ? GLY A 164 VAL A 168 A 3 THR A 132 ? ILE A 136 ? THR A 214 ILE A 218 A 4 VAL A 176 ? ASP A 181 ? VAL A 258 ASP A 263 A 5 LEU A 214 ? THR A 219 ? LEU A 296 THR A 301 A 6 PHE A 264 ? ASP A 268 ? PHE A 346 ASP A 350 A 7 LEU A 306 ? VAL A 310 ? LEU A 388 VAL A 392 B 1 MET B 52 ? LEU B 54 ? MET B 134 LEU B 136 B 2 GLY B 82 ? VAL B 86 ? GLY B 164 VAL B 168 B 3 THR B 132 ? ILE B 136 ? THR B 214 ILE B 218 B 4 VAL B 176 ? ASP B 181 ? VAL B 258 ASP B 263 B 5 LEU B 214 ? THR B 219 ? LEU B 296 THR B 301 B 6 PHE B 264 ? ASP B 268 ? PHE B 346 ASP B 350 B 7 LEU B 306 ? VAL B 310 ? LEU B 388 VAL B 392 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 O MET A 52 ? O MET A 134 N VAL A 85 ? N VAL A 167 A 2 3 O GLY A 82 ? O GLY A 164 N LEU A 133 ? N LEU A 215 A 3 4 O THR A 132 ? O THR A 214 N ALA A 177 ? N ALA A 259 A 4 5 O MET A 178 ? O MET A 260 N ARG A 215 ? N ARG A 297 A 5 6 O LEU A 217 ? O LEU A 299 N PHE A 264 ? N PHE A 346 A 6 7 O PHE A 265 ? O PHE A 347 N ASP A 307 ? N ASP A 389 B 1 2 O MET B 52 ? O MET B 134 N VAL B 85 ? N VAL B 167 B 2 3 O GLY B 82 ? O GLY B 164 N LEU B 133 ? N LEU B 215 B 3 4 O THR B 132 ? O THR B 214 N ALA B 177 ? N ALA B 259 B 4 5 O MET B 178 ? O MET B 260 N ARG B 215 ? N ARG B 297 B 5 6 O LEU B 217 ? O LEU B 299 N PHE B 264 ? N PHE B 346 B 6 7 O PHE B 265 ? O PHE B 347 N ASP B 307 ? N ASP B 389 # 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 ST1 Unknown ? ? ? ? 3 'CATALYTIC SITE INCLUDING MUTATED TYR-> PHE.' ST2 Unknown ? ? ? ? 3 'CATALYTIC SITE INCLUDING MUTATED TYR-> PHE.' AC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 501' AC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 502' AC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE MAN A 503' AC4 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE MAN A 504' AC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE MAN A 505' AC6 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE MAN A 506' AC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE MAN A 507' AC8 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE MAN A 508' AC9 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE MAN A 509' BC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG B 501' BC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG B 502' BC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE MAN B 503' BC4 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE MAN B 504' BC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE MAN B 505' BC6 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE MAN B 506' BC7 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE MAN B 507' BC8 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE MAN B 508' BC9 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE MAN B 509' # 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 ST1 3 ASP A 93 ? ASP A 175 . ? 1_555 ? 2 ST1 3 ASP A 139 ? ASP A 221 . ? 1_555 ? 3 ST1 3 PHE A 87 ? PHE A 169 . ? 1_555 ? 4 ST2 3 ASP B 93 ? ASP B 175 . ? 1_555 ? 5 ST2 3 ASP B 139 ? ASP B 221 . ? 1_555 ? 6 ST2 3 PHE B 87 ? PHE B 169 . ? 1_555 ? 7 AC1 5 LEU A 161 ? LEU A 243 . ? 1_555 ? 8 AC1 5 ASN A 165 ? ASN A 247 . ? 1_555 ? 9 AC1 5 ASN A 207 ? ASN A 289 . ? 1_555 ? 10 AC1 5 HOH U . ? HOH A 624 . ? 1_555 ? 11 AC1 5 HOH U . ? HOH A 700 . ? 1_555 ? 12 AC2 5 TRP A 227 ? TRP A 309 . ? 1_555 ? 13 AC2 5 ASN A 228 ? ASN A 310 . ? 1_555 ? 14 AC2 5 THR A 230 ? THR A 312 . ? 1_555 ? 15 AC2 5 HOH U . ? HOH A 643 . ? 1_555 ? 16 AC2 5 HOH U . ? HOH A 795 . ? 1_555 ? 17 AC3 3 THR A 5 ? THR A 87 . ? 1_555 ? 18 AC3 3 LYS A 274 ? LYS A 356 . ? 1_455 ? 19 AC3 3 ASN A 359 ? ASN A 441 . ? 1_455 ? 20 AC4 2 THR A 15 ? THR A 97 . ? 1_555 ? 21 AC4 2 ASN A 79 ? ASN A 161 . ? 1_555 ? 22 AC5 4 TYR A 21 ? TYR A 103 . ? 1_555 ? 23 AC5 4 SER A 24 ? SER A 106 . ? 1_555 ? 24 AC5 4 LEU A 29 ? LEU A 111 . ? 1_555 ? 25 AC5 4 MAN I . ? MAN A 507 . ? 1_555 ? 26 AC6 5 ALA A 23 ? ALA A 105 . ? 1_555 ? 27 AC6 5 SER A 27 ? SER A 109 . ? 1_555 ? 28 AC6 5 ALA A 43 ? ALA A 125 . ? 1_555 ? 29 AC6 5 LYS A 47 ? LYS A 129 . ? 1_555 ? 30 AC6 5 HOH U . ? HOH A 764 . ? 1_555 ? 31 AC7 5 SER A 24 ? SER A 106 . ? 1_555 ? 32 AC7 5 SER A 28 ? SER A 110 . ? 1_555 ? 33 AC7 5 MAN G . ? MAN A 505 . ? 1_555 ? 34 AC7 5 GLN B 199 ? GLN B 281 . ? 1_545 ? 35 AC7 5 HIS B 258 ? HIS B 340 . ? 1_545 ? 36 AC8 3 LEU A 29 ? LEU A 111 . ? 1_555 ? 37 AC8 3 SER A 33 ? SER A 115 . ? 1_555 ? 38 AC8 3 GLN A 350 ? GLN A 432 . ? 1_555 ? 39 AC9 2 GLY A 36 ? GLY A 118 . ? 1_555 ? 40 AC9 2 THR A 40 ? THR A 122 . ? 1_555 ? 41 BC1 5 LEU B 161 ? LEU B 243 . ? 1_555 ? 42 BC1 5 ASN B 165 ? ASN B 247 . ? 1_555 ? 43 BC1 5 ASN B 207 ? ASN B 289 . ? 1_555 ? 44 BC1 5 HOH V . ? HOH B 624 . ? 1_555 ? 45 BC1 5 HOH V . ? HOH B 700 . ? 1_555 ? 46 BC2 5 TRP B 227 ? TRP B 309 . ? 1_555 ? 47 BC2 5 ASN B 228 ? ASN B 310 . ? 1_555 ? 48 BC2 5 THR B 230 ? THR B 312 . ? 1_555 ? 49 BC2 5 HOH V . ? HOH B 643 . ? 1_555 ? 50 BC2 5 HOH V . ? HOH B 795 . ? 1_555 ? 51 BC3 3 THR B 5 ? THR B 87 . ? 1_555 ? 52 BC3 3 GLY B 290 ? GLY B 372 . ? 1_455 ? 53 BC3 3 ASN B 359 ? ASN B 441 . ? 1_455 ? 54 BC4 2 THR B 15 ? THR B 97 . ? 1_555 ? 55 BC4 2 ASN B 79 ? ASN B 161 . ? 1_555 ? 56 BC5 4 TYR B 21 ? TYR B 103 . ? 1_555 ? 57 BC5 4 SER B 24 ? SER B 106 . ? 1_555 ? 58 BC5 4 LEU B 29 ? LEU B 111 . ? 1_555 ? 59 BC5 4 MAN R . ? MAN B 507 . ? 1_555 ? 60 BC6 5 ALA B 23 ? ALA B 105 . ? 1_555 ? 61 BC6 5 SER B 27 ? SER B 109 . ? 1_555 ? 62 BC6 5 ALA B 43 ? ALA B 125 . ? 1_555 ? 63 BC6 5 LYS B 47 ? LYS B 129 . ? 1_555 ? 64 BC6 5 HOH V . ? HOH B 764 . ? 1_555 ? 65 BC7 3 SER B 24 ? SER B 106 . ? 1_555 ? 66 BC7 3 SER B 28 ? SER B 110 . ? 1_555 ? 67 BC7 3 MAN P . ? MAN B 505 . ? 1_555 ? 68 BC8 3 LEU B 29 ? LEU B 111 . ? 1_555 ? 69 BC8 3 SER B 33 ? SER B 115 . ? 1_555 ? 70 BC8 3 GLN B 350 ? GLN B 432 . ? 1_555 ? 71 BC9 2 GLY B 36 ? GLY B 118 . ? 1_555 ? 72 BC9 2 THR B 40 ? THR B 122 . ? 1_555 ? # _database_PDB_matrix.entry_id 1CB2 _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 1CB2 _atom_sites.fract_transf_matrix[1][1] 0.020367 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.004777 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.013193 _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] 0.011056 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . THR A 1 3 ? 2.274 46.658 56.588 1.00 62.80 ? 85 THR A N 1 ATOM 2 C CA . THR A 1 3 ? 3.728 46.957 56.439 1.00 62.80 ? 85 THR A CA 1 ATOM 3 C C . THR A 1 3 ? 4.400 46.122 55.348 1.00 62.80 ? 85 THR A C 1 ATOM 4 O O . THR A 1 3 ? 5.518 46.426 54.935 1.00 62.80 ? 85 THR A O 1 ATOM 5 C CB . THR A 1 3 ? 4.485 46.758 57.771 1.00 91.15 ? 85 THR A CB 1 ATOM 6 O OG1 . THR A 1 3 ? 4.304 45.415 58.236 1.00 91.15 ? 85 THR A OG1 1 ATOM 7 C CG2 . THR A 1 3 ? 3.971 47.729 58.825 1.00 91.15 ? 85 THR A CG2 1 ATOM 8 N N . ALA A 1 4 ? 3.731 45.059 54.904 1.00 16.63 ? 86 ALA A N 1 ATOM 9 C CA . ALA A 1 4 ? 4.267 44.205 53.844 1.00 16.63 ? 86 ALA A CA 1 ATOM 10 C C . ALA A 1 4 ? 4.232 44.979 52.530 1.00 16.63 ? 86 ALA A C 1 ATOM 11 O O . ALA A 1 4 ? 5.195 44.968 51.771 1.00 16.63 ? 86 ALA A O 1 ATOM 12 C CB . ALA A 1 4 ? 3.455 42.933 53.724 1.00 19.12 ? 86 ALA A CB 1 ATOM 13 N N . THR A 1 5 ? 3.115 45.643 52.256 1.00 10.71 ? 87 THR A N 1 ATOM 14 C CA . THR A 1 5 ? 2.998 46.431 51.034 1.00 10.71 ? 87 THR A CA 1 ATOM 15 C C . THR A 1 5 ? 3.693 47.775 51.236 1.00 10.71 ? 87 THR A C 1 ATOM 16 O O . THR A 1 5 ? 3.930 48.193 52.371 1.00 10.71 ? 87 THR A O 1 ATOM 17 C CB . THR A 1 5 ? 1.538 46.644 50.632 1.00 21.46 ? 87 THR A CB 1 ATOM 18 O OG1 . THR A 1 5 ? 0.828 47.251 51.713 1.00 21.46 ? 87 THR A OG1 1 ATOM 19 C CG2 . THR A 1 5 ? 0.896 45.321 50.262 1.00 21.46 ? 87 THR A CG2 1 ATOM 20 N N . TYR A 1 6 ? 3.982 48.473 50.144 1.00 12.29 ? 88 TYR A N 1 ATOM 21 C CA . TYR A 1 6 ? 4.704 49.741 50.236 1.00 12.29 ? 88 TYR A CA 1 ATOM 22 C C . TYR A 1 6 ? 4.406 50.673 49.068 1.00 12.29 ? 88 TYR A C 1 ATOM 23 O O . TYR A 1 6 ? 3.777 50.287 48.083 1.00 12.29 ? 88 TYR A O 1 ATOM 24 C CB . TYR A 1 6 ? 6.214 49.456 50.230 1.00 6.55 ? 88 TYR A CB 1 ATOM 25 C CG . TYR A 1 6 ? 6.661 48.798 48.941 1.00 6.55 ? 88 TYR A CG 1 ATOM 26 C CD1 . TYR A 1 6 ? 6.506 47.424 48.752 1.00 6.55 ? 88 TYR A CD1 1 ATOM 27 C CD2 . TYR A 1 6 ? 7.136 49.560 47.870 1.00 6.55 ? 88 TYR A CD2 1 ATOM 28 C CE1 . TYR A 1 6 ? 6.796 46.826 47.525 1.00 6.55 ? 88 TYR A CE1 1 ATOM 29 C CE2 . TYR A 1 6 ? 7.428 48.974 46.641 1.00 6.55 ? 88 TYR A CE2 1 ATOM 30 C CZ . TYR A 1 6 ? 7.251 47.607 46.477 1.00 6.55 ? 88 TYR A CZ 1 ATOM 31 O OH . TYR A 1 6 ? 7.495 47.025 45.256 1.00 6.55 ? 88 TYR A OH 1 ATOM 32 N N . SER A 1 7 ? 4.910 51.894 49.182 1.00 24.43 ? 89 SER A N 1 ATOM 33 C CA . SER A 1 7 ? 4.785 52.899 48.141 1.00 24.43 ? 89 SER A CA 1 ATOM 34 C C . SER A 1 7 ? 6.173 53.531 48.084 1.00 24.43 ? 89 SER A C 1 ATOM 35 O O . SER A 1 7 ? 6.786 53.790 49.124 1.00 24.43 ? 89 SER A O 1 ATOM 36 C CB . SER A 1 7 ? 3.729 53.950 48.500 1.00 72.23 ? 89 SER A CB 1 ATOM 37 O OG . SER A 1 7 ? 4.132 54.751 49.598 1.00 72.23 ? 89 SER A OG 1 ATOM 38 N N . GLY A 1 8 ? 6.702 53.698 46.877 1.00 11.42 ? 90 GLY A N 1 ATOM 39 C CA . GLY A 1 8 ? 8.019 54.285 46.735 1.00 11.42 ? 90 GLY A CA 1 ATOM 40 C C . GLY A 1 8 ? 9.129 53.295 47.037 1.00 11.42 ? 90 GLY A C 1 ATOM 41 O O . GLY A 1 8 ? 9.002 52.107 46.744 1.00 11.42 ? 90 GLY A O 1 ATOM 42 N N . ASN A 1 9 ? 10.214 53.799 47.621 1.00 9.11 ? 91 ASN A N 1 ATOM 43 C CA . ASN A 1 9 ? 11.388 53.005 47.977 1.00 9.11 ? 91 ASN A CA 1 ATOM 44 C C . ASN A 1 9 ? 11.029 51.863 48.933 1.00 9.11 ? 91 ASN A C 1 ATOM 45 O O . ASN A 1 9 ? 10.717 52.096 50.097 1.00 9.11 ? 91 ASN A O 1 ATOM 46 C CB . ASN A 1 9 ? 12.440 53.926 48.615 1.00 3.56 ? 91 ASN A CB 1 ATOM 47 C CG . ASN A 1 9 ? 13.771 53.233 48.863 1.00 3.56 ? 91 ASN A CG 1 ATOM 48 O OD1 . ASN A 1 9 ? 13.875 52.008 48.800 1.00 3.56 ? 91 ASN A OD1 1 ATOM 49 N ND2 . ASN A 1 9 ? 14.794 54.020 49.160 1.00 3.56 ? 91 ASN A ND2 1 ATOM 50 N N . PRO A 1 10 ? 11.124 50.611 48.462 1.00 6.49 ? 92 PRO A N 1 ATOM 51 C CA . PRO A 1 10 ? 10.807 49.428 49.269 1.00 6.49 ? 92 PRO A CA 1 ATOM 52 C C . PRO A 1 10 ? 11.756 49.162 50.433 1.00 6.49 ? 92 PRO A C 1 ATOM 53 O O . PRO A 1 10 ? 11.474 48.323 51.291 1.00 6.49 ? 92 PRO A O 1 ATOM 54 C CB . PRO A 1 10 ? 10.829 48.297 48.245 1.00 10.03 ? 92 PRO A CB 1 ATOM 55 C CG . PRO A 1 10 ? 11.831 48.757 47.249 1.00 10.03 ? 92 PRO A CG 1 ATOM 56 C CD . PRO A 1 10 ? 11.531 50.225 47.101 1.00 10.03 ? 92 PRO A CD 1 ATOM 57 N N . PHE A 1 11 ? 12.883 49.868 50.455 1.00 13.59 ? 93 PHE A N 1 ATOM 58 C CA . PHE A 1 11 ? 13.857 49.709 51.526 1.00 13.59 ? 93 PHE A CA 1 ATOM 59 C C . PHE A 1 11 ? 13.516 50.597 52.715 1.00 13.59 ? 93 PHE A C 1 ATOM 60 O O . PHE A 1 11 ? 14.068 50.424 53.800 1.00 13.59 ? 93 PHE A O 1 ATOM 61 C CB . PHE A 1 11 ? 15.275 50.009 51.022 1.00 8.52 ? 93 PHE A CB 1 ATOM 62 C CG . PHE A 1 11 ? 15.856 48.911 50.168 1.00 8.52 ? 93 PHE A CG 1 ATOM 63 C CD1 . PHE A 1 11 ? 16.572 47.864 50.750 1.00 8.52 ? 93 PHE A CD1 1 ATOM 64 C CD2 . PHE A 1 11 ? 15.662 48.905 48.789 1.00 8.52 ? 93 PHE A CD2 1 ATOM 65 C CE1 . PHE A 1 11 ? 17.082 46.827 49.971 1.00 8.52 ? 93 PHE A CE1 1 ATOM 66 C CE2 . PHE A 1 11 ? 16.166 47.873 48.003 1.00 8.52 ? 93 PHE A CE2 1 ATOM 67 C CZ . PHE A 1 11 ? 16.878 46.831 48.594 1.00 8.52 ? 93 PHE A CZ 1 ATOM 68 N N . VAL A 1 12 ? 12.607 51.547 52.506 1.00 13.65 ? 94 VAL A N 1 ATOM 69 C CA . VAL A 1 12 ? 12.189 52.452 53.570 1.00 13.65 ? 94 VAL A CA 1 ATOM 70 C C . VAL A 1 12 ? 11.052 51.816 54.364 1.00 13.65 ? 94 VAL A C 1 ATOM 71 O O . VAL A 1 12 ? 10.064 51.364 53.784 1.00 13.65 ? 94 VAL A O 1 ATOM 72 C CB . VAL A 1 12 ? 11.718 53.813 53.004 1.00 19.12 ? 94 VAL A CB 1 ATOM 73 C CG1 . VAL A 1 12 ? 11.208 54.706 54.125 1.00 19.12 ? 94 VAL A CG1 1 ATOM 74 C CG2 . VAL A 1 12 ? 12.861 54.502 52.284 1.00 19.12 ? 94 VAL A CG2 1 ATOM 75 N N . GLY A 1 13 ? 11.209 51.759 55.685 1.00 20.83 ? 95 GLY A N 1 ATOM 76 C CA . GLY A 1 13 ? 10.178 51.181 56.531 1.00 20.83 ? 95 GLY A CA 1 ATOM 77 C C . GLY A 1 13 ? 10.440 49.764 57.010 1.00 20.83 ? 95 GLY A C 1 ATOM 78 O O . GLY A 1 13 ? 9.624 49.197 57.735 1.00 20.83 ? 95 GLY A O 1 ATOM 79 N N . VAL A 1 14 ? 11.558 49.180 56.587 1.00 11.89 ? 96 VAL A N 1 ATOM 80 C CA . VAL A 1 14 ? 11.926 47.824 56.992 1.00 11.89 ? 96 VAL A CA 1 ATOM 81 C C . VAL A 1 14 ? 13.425 47.724 57.203 1.00 11.89 ? 96 VAL A C 1 ATOM 82 O O . VAL A 1 14 ? 14.174 48.643 56.877 1.00 11.89 ? 96 VAL A O 1 ATOM 83 C CB . VAL A 1 14 ? 11.529 46.752 55.937 1.00 16.17 ? 96 VAL A CB 1 ATOM 84 C CG1 . VAL A 1 14 ? 10.027 46.559 55.901 1.00 16.17 ? 96 VAL A CG1 1 ATOM 85 C CG2 . VAL A 1 14 ? 12.065 47.132 54.561 1.00 16.17 ? 96 VAL A CG2 1 ATOM 86 N N . THR A 1 15 ? 13.850 46.589 57.744 1.00 9.64 ? 97 THR A N 1 ATOM 87 C CA . THR A 1 15 ? 15.257 46.319 57.994 1.00 9.64 ? 97 THR A CA 1 ATOM 88 C C . THR A 1 15 ? 15.547 44.999 57.297 1.00 9.64 ? 97 THR A C 1 ATOM 89 O O . THR A 1 15 ? 14.854 44.008 57.530 1.00 9.64 ? 97 THR A O 1 ATOM 90 C CB . THR A 1 15 ? 15.546 46.175 59.512 1.00 15.95 ? 97 THR A CB 1 ATOM 91 O OG1 . THR A 1 15 ? 15.202 47.397 60.179 1.00 15.95 ? 97 THR A OG1 1 ATOM 92 C CG2 . THR A 1 15 ? 17.018 45.866 59.755 1.00 15.95 ? 97 THR A CG2 1 ATOM 93 N N . PRO A 1 16 ? 16.522 44.988 56.370 1.00 9.18 ? 98 PRO A N 1 ATOM 94 C CA . PRO A 1 16 ? 16.862 43.755 55.657 1.00 9.18 ? 98 PRO A CA 1 ATOM 95 C C . PRO A 1 16 ? 17.356 42.685 56.634 1.00 9.18 ? 98 PRO A C 1 ATOM 96 O O . PRO A 1 16 ? 18.079 42.975 57.589 1.00 9.18 ? 98 PRO A O 1 ATOM 97 C CB . PRO A 1 16 ? 17.964 44.206 54.699 1.00 9.94 ? 98 PRO A CB 1 ATOM 98 C CG . PRO A 1 16 ? 17.639 45.644 54.458 1.00 9.94 ? 98 PRO A CG 1 ATOM 99 C CD . PRO A 1 16 ? 17.287 46.126 55.837 1.00 9.94 ? 98 PRO A CD 1 ATOM 100 N N . TRP A 1 17 ? 16.935 41.455 56.387 1.00 8.09 ? 99 TRP A N 1 ATOM 101 C CA . TRP A 1 17 ? 17.281 40.318 57.225 1.00 8.09 ? 99 TRP A CA 1 ATOM 102 C C . TRP A 1 17 ? 18.668 39.745 56.954 1.00 8.09 ? 99 TRP A C 1 ATOM 103 O O . TRP A 1 17 ? 19.064 39.579 55.802 1.00 8.09 ? 99 TRP A O 1 ATOM 104 C CB . TRP A 1 17 ? 16.221 39.234 57.008 1.00 8.12 ? 99 TRP A CB 1 ATOM 105 C CG . TRP A 1 17 ? 16.434 37.950 57.738 1.00 8.12 ? 99 TRP A CG 1 ATOM 106 C CD1 . TRP A 1 17 ? 16.788 36.749 57.193 1.00 8.12 ? 99 TRP A CD1 1 ATOM 107 C CD2 . TRP A 1 17 ? 16.233 37.714 59.134 1.00 8.12 ? 99 TRP A CD2 1 ATOM 108 N NE1 . TRP A 1 17 ? 16.809 35.777 58.161 1.00 8.12 ? 99 TRP A NE1 1 ATOM 109 C CE2 . TRP A 1 17 ? 16.472 36.340 59.363 1.00 8.12 ? 99 TRP A CE2 1 ATOM 110 C CE3 . TRP A 1 17 ? 15.863 38.527 60.213 1.00 8.12 ? 99 TRP A CE3 1 ATOM 111 C CZ2 . TRP A 1 17 ? 16.355 35.759 60.630 1.00 8.12 ? 99 TRP A CZ2 1 ATOM 112 C CZ3 . TRP A 1 17 ? 15.746 37.950 61.475 1.00 8.12 ? 99 TRP A CZ3 1 ATOM 113 C CH2 . TRP A 1 17 ? 15.991 36.576 61.671 1.00 8.12 ? 99 TRP A CH2 1 ATOM 114 N N . ALA A 1 18 ? 19.415 39.477 58.023 1.00 9.42 ? 100 ALA A N 1 ATOM 115 C CA . ALA A 1 18 ? 20.736 38.862 57.894 1.00 9.42 ? 100 ALA A CA 1 ATOM 116 C C . ALA A 1 18 ? 20.449 37.370 58.069 1.00 9.42 ? 100 ALA A C 1 ATOM 117 O O . ALA A 1 18 ? 20.193 36.905 59.183 1.00 9.42 ? 100 ALA A O 1 ATOM 118 C CB . ALA A 1 18 ? 21.676 39.364 58.984 1.00 10.51 ? 100 ALA A CB 1 ATOM 119 N N . ASN A 1 19 ? 20.456 36.631 56.964 1.00 8.54 ? 101 ASN A N 1 ATOM 120 C CA . ASN A 1 19 ? 20.134 35.206 56.991 1.00 8.54 ? 101 ASN A CA 1 ATOM 121 C C . ASN A 1 19 ? 21.049 34.282 57.791 1.00 8.54 ? 101 ASN A C 1 ATOM 122 O O . ASN A 1 19 ? 22.238 34.564 57.992 1.00 8.54 ? 101 ASN A O 1 ATOM 123 C CB . ASN A 1 19 ? 19.915 34.668 55.570 1.00 10.17 ? 101 ASN A CB 1 ATOM 124 C CG . ASN A 1 19 ? 21.190 34.611 54.750 1.00 10.17 ? 101 ASN A CG 1 ATOM 125 O OD1 . ASN A 1 19 ? 21.904 33.613 54.771 1.00 10.17 ? 101 ASN A OD1 1 ATOM 126 N ND2 . ASN A 1 19 ? 21.463 35.668 53.996 1.00 10.17 ? 101 ASN A ND2 1 ATOM 127 N N . ALA A 1 20 ? 20.477 33.162 58.228 1.00 12.05 ? 102 ALA A N 1 ATOM 128 C CA . ALA A 1 20 ? 21.183 32.166 59.027 1.00 12.05 ? 102 ALA A CA 1 ATOM 129 C C . ALA A 1 20 ? 22.178 31.340 58.224 1.00 12.05 ? 102 ALA A C 1 ATOM 130 O O . ALA A 1 20 ? 23.137 30.805 58.779 1.00 12.05 ? 102 ALA A O 1 ATOM 131 C CB . ALA A 1 20 ? 20.179 31.246 59.714 1.00 25.70 ? 102 ALA A CB 1 ATOM 132 N N . TYR A 1 21 ? 21.941 31.229 56.921 1.00 10.97 ? 103 TYR A N 1 ATOM 133 C CA . TYR A 1 21 ? 22.810 30.466 56.034 1.00 10.97 ? 103 TYR A CA 1 ATOM 134 C C . TYR A 1 21 ? 24.218 31.054 56.000 1.00 10.97 ? 103 TYR A C 1 ATOM 135 O O . TYR A 1 21 ? 25.204 30.347 56.213 1.00 10.97 ? 103 TYR A O 1 ATOM 136 C CB . TYR A 1 21 ? 22.222 30.449 54.621 1.00 23.99 ? 103 TYR A CB 1 ATOM 137 C CG . TYR A 1 21 ? 23.018 29.634 53.634 1.00 23.99 ? 103 TYR A CG 1 ATOM 138 C CD1 . TYR A 1 21 ? 22.767 28.276 53.471 1.00 23.99 ? 103 TYR A CD1 1 ATOM 139 C CD2 . TYR A 1 21 ? 24.026 30.219 52.863 1.00 23.99 ? 103 TYR A CD2 1 ATOM 140 C CE1 . TYR A 1 21 ? 23.496 27.513 52.564 1.00 23.99 ? 103 TYR A CE1 1 ATOM 141 C CE2 . TYR A 1 21 ? 24.764 29.465 51.955 1.00 23.99 ? 103 TYR A CE2 1 ATOM 142 C CZ . TYR A 1 21 ? 24.491 28.112 51.811 1.00 23.99 ? 103 TYR A CZ 1 ATOM 143 O OH . TYR A 1 21 ? 25.204 27.356 50.911 1.00 23.99 ? 103 TYR A OH 1 ATOM 144 N N . TYR A 1 22 ? 24.307 32.346 55.706 1.00 8.30 ? 104 TYR A N 1 ATOM 145 C CA . TYR A 1 22 ? 25.590 33.025 55.644 1.00 8.30 ? 104 TYR A CA 1 ATOM 146 C C . TYR A 1 22 ? 26.203 33.087 57.038 1.00 8.30 ? 104 TYR A C 1 ATOM 147 O O . TYR A 1 22 ? 27.404 32.882 57.204 1.00 8.30 ? 104 TYR A O 1 ATOM 148 C CB . TYR A 1 22 ? 25.419 34.432 55.065 1.00 9.59 ? 104 TYR A CB 1 ATOM 149 C CG . TYR A 1 22 ? 26.715 35.187 54.902 1.00 9.59 ? 104 TYR A CG 1 ATOM 150 C CD1 . TYR A 1 22 ? 27.658 34.801 53.949 1.00 9.59 ? 104 TYR A CD1 1 ATOM 151 C CD2 . TYR A 1 22 ? 27.008 36.277 55.715 1.00 9.59 ? 104 TYR A CD2 1 ATOM 152 C CE1 . TYR A 1 22 ? 28.867 35.487 53.814 1.00 9.59 ? 104 TYR A CE1 1 ATOM 153 C CE2 . TYR A 1 22 ? 28.208 36.967 55.591 1.00 9.59 ? 104 TYR A CE2 1 ATOM 154 C CZ . TYR A 1 22 ? 29.130 36.567 54.638 1.00 9.59 ? 104 TYR A CZ 1 ATOM 155 O OH . TYR A 1 22 ? 30.303 37.267 54.520 1.00 9.59 ? 104 TYR A OH 1 ATOM 156 N N . ALA A 1 23 ? 25.368 33.336 58.043 1.00 9.16 ? 105 ALA A N 1 ATOM 157 C CA . ALA A 1 23 ? 25.837 33.415 59.423 1.00 9.16 ? 105 ALA A CA 1 ATOM 158 C C . ALA A 1 23 ? 26.458 32.090 59.855 1.00 9.16 ? 105 ALA A C 1 ATOM 159 O O . ALA A 1 23 ? 27.435 32.074 60.600 1.00 9.16 ? 105 ALA A O 1 ATOM 160 C CB . ALA A 1 23 ? 24.702 33.800 60.350 1.00 8.78 ? 105 ALA A CB 1 ATOM 161 N N . SER A 1 24 ? 25.905 30.984 59.364 1.00 12.73 ? 106 SER A N 1 ATOM 162 C CA . SER A 1 24 ? 26.431 29.667 59.696 1.00 12.73 ? 106 SER A CA 1 ATOM 163 C C . SER A 1 24 ? 27.815 29.488 59.081 1.00 12.73 ? 106 SER A C 1 ATOM 164 O O . SER A 1 24 ? 28.732 28.994 59.741 1.00 12.73 ? 106 SER A O 1 ATOM 165 C CB . SER A 1 24 ? 25.498 28.550 59.216 1.00 13.82 ? 106 SER A CB 1 ATOM 166 O OG . SER A 1 24 ? 26.187 27.305 59.365 1.00 13.82 ? 106 SER A OG 1 ATOM 167 N N . GLU A 1 25 ? 27.965 29.896 57.822 1.00 10.73 ? 107 GLU A N 1 ATOM 168 C CA . GLU A 1 25 ? 29.254 29.799 57.134 1.00 10.73 ? 107 GLU A CA 1 ATOM 169 C C . GLU A 1 25 ? 30.343 30.556 57.887 1.00 10.73 ? 107 GLU A C 1 ATOM 170 O O . GLU A 1 25 ? 31.437 30.041 58.092 1.00 10.73 ? 107 GLU A O 1 ATOM 171 C CB . GLU A 1 25 ? 29.155 30.364 55.718 1.00 9.80 ? 107 GLU A CB 1 ATOM 172 C CG . GLU A 1 25 ? 28.228 29.603 54.795 1.00 9.80 ? 107 GLU A CG 1 ATOM 173 C CD . GLU A 1 25 ? 28.191 30.205 53.411 1.00 9.80 ? 107 GLU A CD 1 ATOM 174 O OE1 . GLU A 1 25 ? 27.797 31.383 53.287 1.00 9.80 ? 107 GLU A OE1 1 ATOM 175 O OE2 . GLU A 1 25 ? 28.566 29.504 52.450 1.00 9.80 ? 107 GLU A OE2 1 ATOM 176 N N . VAL A 1 26 ? 30.037 31.781 58.297 1.00 7.59 ? 108 VAL A N 1 ATOM 177 C CA . VAL A 1 26 ? 30.995 32.602 59.027 1.00 7.59 ? 108 VAL A CA 1 ATOM 178 C C . VAL A 1 26 ? 31.349 32.008 60.393 1.00 7.59 ? 108 VAL A C 1 ATOM 179 O O . VAL A 1 26 ? 32.522 31.809 60.704 1.00 7.59 ? 108 VAL A O 1 ATOM 180 C CB . VAL A 1 26 ? 30.464 34.042 59.221 1.00 11.96 ? 108 VAL A CB 1 ATOM 181 C CG1 . VAL A 1 26 ? 31.443 34.863 60.049 1.00 11.96 ? 108 VAL A CG1 1 ATOM 182 C CG2 . VAL A 1 26 ? 30.233 34.709 57.867 1.00 11.96 ? 108 VAL A CG2 1 ATOM 183 N N . SER A 1 27 ? 30.336 31.685 61.188 1.00 12.48 ? 109 SER A N 1 ATOM 184 C CA . SER A 1 27 ? 30.566 31.135 62.521 1.00 12.48 ? 109 SER A CA 1 ATOM 185 C C . SER A 1 27 ? 31.143 29.726 62.572 1.00 12.48 ? 109 SER A C 1 ATOM 186 O O . SER A 1 27 ? 31.971 29.429 63.432 1.00 12.48 ? 109 SER A O 1 ATOM 187 C CB . SER A 1 27 ? 29.282 31.200 63.343 1.00 12.37 ? 109 SER A CB 1 ATOM 188 O OG . SER A 1 27 ? 28.882 32.565 63.432 1.00 12.37 ? 109 SER A OG 1 ATOM 189 N N . SER A 1 28 ? 30.757 28.879 61.623 1.00 16.93 ? 110 SER A N 1 ATOM 190 C CA . SER A 1 28 ? 31.221 27.496 61.606 1.00 16.93 ? 110 SER A CA 1 ATOM 191 C C . SER A 1 28 ? 32.380 27.139 60.695 1.00 16.93 ? 110 SER A C 1 ATOM 192 O O . SER A 1 28 ? 33.049 26.128 60.915 1.00 16.93 ? 110 SER A O 1 ATOM 193 C CB . SER A 1 28 ? 30.044 26.562 61.352 1.00 15.02 ? 110 SER A CB 1 ATOM 194 O OG . SER A 1 28 ? 29.190 26.632 62.489 1.00 15.02 ? 110 SER A OG 1 ATOM 195 N N . LEU A 1 29 ? 32.625 27.956 59.679 1.00 17.67 ? 111 LEU A N 1 ATOM 196 C CA . LEU A 1 29 ? 33.710 27.684 58.753 1.00 17.67 ? 111 LEU A CA 1 ATOM 197 C C . LEU A 1 29 ? 34.845 28.697 58.843 1.00 17.67 ? 111 LEU A C 1 ATOM 198 O O . LEU A 1 29 ? 35.996 28.353 58.597 1.00 17.67 ? 111 LEU A O 1 ATOM 199 C CB . LEU A 1 29 ? 33.185 27.624 57.314 1.00 17.21 ? 111 LEU A CB 1 ATOM 200 C CG . LEU A 1 29 ? 32.010 26.691 57.005 1.00 17.21 ? 111 LEU A CG 1 ATOM 201 C CD1 . LEU A 1 29 ? 31.674 26.767 55.525 1.00 17.21 ? 111 LEU A CD1 1 ATOM 202 C CD2 . LEU A 1 29 ? 32.343 25.264 57.394 1.00 17.21 ? 111 LEU A CD2 1 ATOM 203 N N . ALA A 1 30 ? 34.527 29.936 59.205 1.00 12.14 ? 112 ALA A N 1 ATOM 204 C CA . ALA A 1 30 ? 35.535 30.986 59.290 1.00 12.14 ? 112 ALA A CA 1 ATOM 205 C C . ALA A 1 30 ? 36.090 31.233 60.689 1.00 12.14 ? 112 ALA A C 1 ATOM 206 O O . ALA A 1 30 ? 37.300 31.139 60.916 1.00 12.14 ? 112 ALA A O 1 ATOM 207 C CB . ALA A 1 30 ? 34.977 32.283 58.715 1.00 2.00 ? 112 ALA A CB 1 ATOM 208 N N . ILE A 1 31 ? 35.200 31.526 61.630 1.00 15.97 ? 113 ILE A N 1 ATOM 209 C CA . ILE A 1 31 ? 35.596 31.828 63.000 1.00 15.97 ? 113 ILE A CA 1 ATOM 210 C C . ILE A 1 31 ? 36.485 30.784 63.689 1.00 15.97 ? 113 ILE A C 1 ATOM 211 O O . ILE A 1 31 ? 37.471 31.148 64.332 1.00 15.97 ? 113 ILE A O 1 ATOM 212 C CB . ILE A 1 31 ? 34.369 32.227 63.861 1.00 8.57 ? 113 ILE A CB 1 ATOM 213 C CG1 . ILE A 1 31 ? 33.777 33.528 63.303 1.00 8.57 ? 113 ILE A CG1 1 ATOM 214 C CG2 . ILE A 1 31 ? 34.770 32.417 65.329 1.00 8.57 ? 113 ILE A CG2 1 ATOM 215 C CD1 . ILE A 1 31 ? 32.657 34.130 64.118 1.00 8.57 ? 113 ILE A CD1 1 ATOM 216 N N . PRO A 1 32 ? 36.191 29.480 63.523 1.00 21.74 ? 114 PRO A N 1 ATOM 217 C CA . PRO A 1 32 ? 37.034 28.466 64.170 1.00 21.74 ? 114 PRO A CA 1 ATOM 218 C C . PRO A 1 32 ? 38.506 28.518 63.743 1.00 21.74 ? 114 PRO A C 1 ATOM 219 O O . PRO A 1 32 ? 39.367 27.919 64.391 1.00 21.74 ? 114 PRO A O 1 ATOM 220 C CB . PRO A 1 32 ? 36.381 27.155 63.738 1.00 19.04 ? 114 PRO A CB 1 ATOM 221 C CG . PRO A 1 32 ? 34.942 27.527 63.589 1.00 19.04 ? 114 PRO A CG 1 ATOM 222 C CD . PRO A 1 32 ? 35.023 28.850 62.882 1.00 19.04 ? 114 PRO A CD 1 ATOM 223 N N . SER A 1 33 ? 38.783 29.244 62.660 1.00 20.81 ? 115 SER A N 1 ATOM 224 C CA . SER A 1 33 ? 40.134 29.379 62.135 1.00 20.81 ? 115 SER A CA 1 ATOM 225 C C . SER A 1 33 ? 40.746 30.748 62.374 1.00 20.81 ? 115 SER A C 1 ATOM 226 O O . SER A 1 33 ? 41.885 30.989 61.984 1.00 20.81 ? 115 SER A O 1 ATOM 227 C CB . SER A 1 33 ? 40.146 29.110 60.637 1.00 21.34 ? 115 SER A CB 1 ATOM 228 O OG . SER A 1 33 ? 39.684 27.788 60.393 1.00 21.34 ? 115 SER A OG 1 ATOM 229 N N . LEU A 1 34 ? 39.984 31.659 62.963 1.00 20.96 ? 116 LEU A N 1 ATOM 230 C CA . LEU A 1 34 ? 40.495 32.998 63.223 1.00 20.96 ? 116 LEU A CA 1 ATOM 231 C C . LEU A 1 34 ? 40.814 33.178 64.696 1.00 20.96 ? 116 LEU A C 1 ATOM 232 O O . LEU A 1 34 ? 40.382 32.384 65.520 1.00 20.96 ? 116 LEU A O 1 ATOM 233 C CB . LEU A 1 34 ? 39.494 34.046 62.749 1.00 14.81 ? 116 LEU A CB 1 ATOM 234 C CG . LEU A 1 34 ? 39.220 34.023 61.244 1.00 14.81 ? 116 LEU A CG 1 ATOM 235 C CD1 . LEU A 1 34 ? 38.162 35.054 60.906 1.00 14.81 ? 116 LEU A CD1 1 ATOM 236 C CD2 . LEU A 1 34 ? 40.509 34.293 60.475 1.00 14.81 ? 116 LEU A CD2 1 ATOM 237 N N . THR A 1 35 ? 41.564 34.225 65.027 1.00 30.06 ? 117 THR A N 1 ATOM 238 C CA . THR A 1 35 ? 41.937 34.465 66.414 1.00 30.06 ? 117 THR A CA 1 ATOM 239 C C . THR A 1 35 ? 41.799 35.929 66.829 1.00 30.06 ? 117 THR A C 1 ATOM 240 O O . THR A 1 35 ? 41.865 36.831 65.991 1.00 30.06 ? 117 THR A O 1 ATOM 241 C CB . THR A 1 35 ? 43.389 33.960 66.689 1.00 56.11 ? 117 THR A CB 1 ATOM 242 O OG1 . THR A 1 35 ? 43.527 33.618 68.072 1.00 56.11 ? 117 THR A OG1 1 ATOM 243 C CG2 . THR A 1 35 ? 44.427 35.026 66.337 1.00 56.11 ? 117 THR A CG2 1 ATOM 244 N N . GLY A 1 36 ? 41.563 36.140 68.123 1.00 34.58 ? 118 GLY A N 1 ATOM 245 C CA . GLY A 1 36 ? 41.432 37.479 68.676 1.00 34.58 ? 118 GLY A CA 1 ATOM 246 C C . GLY A 1 36 ? 40.614 38.483 67.883 1.00 34.58 ? 118 GLY A C 1 ATOM 247 O O . GLY A 1 36 ? 39.480 38.210 67.489 1.00 34.58 ? 118 GLY A O 1 ATOM 248 N N . ALA A 1 37 ? 41.220 39.639 67.622 1.00 18.26 ? 119 ALA A N 1 ATOM 249 C CA . ALA A 1 37 ? 40.577 40.728 66.895 1.00 18.26 ? 119 ALA A CA 1 ATOM 250 C C . ALA A 1 37 ? 39.937 40.304 65.582 1.00 18.26 ? 119 ALA A C 1 ATOM 251 O O . ALA A 1 37 ? 38.862 40.785 65.234 1.00 18.26 ? 119 ALA A O 1 ATOM 252 C CB . ALA A 1 37 ? 41.569 41.850 66.653 1.00 16.38 ? 119 ALA A CB 1 ATOM 253 N N . MET A 1 38 ? 40.590 39.398 64.863 1.00 21.92 ? 120 MET A N 1 ATOM 254 C CA . MET A 1 38 ? 40.071 38.926 63.586 1.00 21.92 ? 120 MET A CA 1 ATOM 255 C C . MET A 1 38 ? 38.750 38.170 63.685 1.00 21.92 ? 120 MET A C 1 ATOM 256 O O . MET A 1 38 ? 37.831 38.429 62.909 1.00 21.92 ? 120 MET A O 1 ATOM 257 C CB . MET A 1 38 ? 41.110 38.068 62.865 1.00 30.83 ? 120 MET A CB 1 ATOM 258 C CG . MET A 1 38 ? 42.204 38.877 62.197 1.00 30.83 ? 120 MET A CG 1 ATOM 259 S SD . MET A 1 38 ? 41.584 39.861 60.816 1.00 30.83 ? 120 MET A SD 1 ATOM 260 C CE . MET A 1 38 ? 41.715 38.695 59.497 1.00 30.83 ? 120 MET A CE 1 ATOM 261 N N . ALA A 1 39 ? 38.634 37.241 64.627 1.00 17.63 ? 121 ALA A N 1 ATOM 262 C CA . ALA A 1 39 ? 37.380 36.512 64.716 1.00 17.63 ? 121 ALA A CA 1 ATOM 263 C C . ALA A 1 39 ? 36.247 37.306 65.351 1.00 17.63 ? 121 ALA A C 1 ATOM 264 O O . ALA A 1 39 ? 35.080 36.991 65.131 1.00 17.63 ? 121 ALA A O 1 ATOM 265 C CB . ALA A 1 39 ? 37.563 35.198 65.367 1.00 37.09 ? 121 ALA A CB 1 ATOM 266 N N . THR A 1 40 ? 36.580 38.331 66.134 1.00 18.64 ? 122 THR A N 1 ATOM 267 C CA . THR A 1 40 ? 35.541 39.175 66.714 1.00 18.64 ? 122 THR A CA 1 ATOM 268 C C . THR A 1 40 ? 34.993 40.023 65.569 1.00 18.64 ? 122 THR A C 1 ATOM 269 O O . THR A 1 40 ? 33.785 40.250 65.468 1.00 18.64 ? 122 THR A O 1 ATOM 270 C CB . THR A 1 40 ? 36.076 40.069 67.856 1.00 24.96 ? 122 THR A CB 1 ATOM 271 O OG1 . THR A 1 40 ? 36.119 39.281 69.042 1.00 24.96 ? 122 THR A OG1 1 ATOM 272 C CG2 . THR A 1 40 ? 35.156 41.267 68.097 1.00 24.96 ? 122 THR A CG2 1 ATOM 273 N N . ALA A 1 41 ? 35.886 40.436 64.672 1.00 17.17 ? 123 ALA A N 1 ATOM 274 C CA . ALA A 1 41 ? 35.491 41.229 63.517 1.00 17.17 ? 123 ALA A CA 1 ATOM 275 C C . ALA A 1 41 ? 34.651 40.366 62.573 1.00 17.17 ? 123 ALA A C 1 ATOM 276 O O . ALA A 1 41 ? 33.684 40.848 61.984 1.00 17.17 ? 123 ALA A O 1 ATOM 277 C CB . ALA A 1 41 ? 36.718 41.760 62.795 1.00 17.51 ? 123 ALA A CB 1 ATOM 278 N N . ALA A 1 42 ? 35.009 39.086 62.453 1.00 11.83 ? 124 ALA A N 1 ATOM 279 C CA . ALA A 1 42 ? 34.276 38.158 61.588 1.00 11.83 ? 124 ALA A CA 1 ATOM 280 C C . ALA A 1 42 ? 32.846 37.946 62.088 1.00 11.83 ? 124 ALA A C 1 ATOM 281 O O . ALA A 1 42 ? 31.919 37.801 61.294 1.00 11.83 ? 124 ALA A O 1 ATOM 282 C CB . ALA A 1 42 ? 35.002 36.826 61.498 1.00 8.45 ? 124 ALA A CB 1 ATOM 283 N N . ALA A 1 43 ? 32.672 37.921 63.408 1.00 13.59 ? 125 ALA A N 1 ATOM 284 C CA . ALA A 1 43 ? 31.352 37.743 64.006 1.00 13.59 ? 125 ALA A CA 1 ATOM 285 C C . ALA A 1 43 ? 30.434 38.895 63.609 1.00 13.59 ? 125 ALA A C 1 ATOM 286 O O . ALA A 1 43 ? 29.241 38.698 63.397 1.00 13.59 ? 125 ALA A O 1 ATOM 287 C CB . ALA A 1 43 ? 31.464 37.660 65.537 1.00 2.00 ? 125 ALA A CB 1 ATOM 288 N N . ALA A 1 44 ? 31.009 40.091 63.499 1.00 9.60 ? 126 ALA A N 1 ATOM 289 C CA . ALA A 1 44 ? 30.262 41.285 63.131 1.00 9.60 ? 126 ALA A CA 1 ATOM 290 C C . ALA A 1 44 ? 29.794 41.246 61.672 1.00 9.60 ? 126 ALA A C 1 ATOM 291 O O . ALA A 1 44 ? 28.685 41.689 61.359 1.00 9.60 ? 126 ALA A O 1 ATOM 292 C CB . ALA A 1 44 ? 31.108 42.528 63.383 1.00 9.74 ? 126 ALA A CB 1 ATOM 293 N N . VAL A 1 45 ? 30.635 40.709 60.791 1.00 12.95 ? 127 VAL A N 1 ATOM 294 C CA . VAL A 1 45 ? 30.310 40.615 59.368 1.00 12.95 ? 127 VAL A CA 1 ATOM 295 C C . VAL A 1 45 ? 29.047 39.787 59.131 1.00 12.95 ? 127 VAL A C 1 ATOM 296 O O . VAL A 1 45 ? 28.239 40.102 58.249 1.00 12.95 ? 127 VAL A O 1 ATOM 297 C CB . VAL A 1 45 ? 31.469 39.980 58.553 1.00 10.95 ? 127 VAL A CB 1 ATOM 298 C CG1 . VAL A 1 45 ? 31.094 39.911 57.077 1.00 10.95 ? 127 VAL A CG1 1 ATOM 299 C CG2 . VAL A 1 45 ? 32.745 40.785 58.728 1.00 10.95 ? 127 VAL A CG2 1 ATOM 300 N N . ALA A 1 46 ? 28.876 38.737 59.933 1.00 11.12 ? 128 ALA A N 1 ATOM 301 C CA . ALA A 1 46 ? 27.717 37.859 59.806 1.00 11.12 ? 128 ALA A CA 1 ATOM 302 C C . ALA A 1 46 ? 26.397 38.566 60.116 1.00 11.12 ? 128 ALA A C 1 ATOM 303 O O . ALA A 1 46 ? 25.333 38.043 59.809 1.00 11.12 ? 128 ALA A O 1 ATOM 304 C CB . ALA A 1 46 ? 27.879 36.635 60.706 1.00 9.91 ? 128 ALA A CB 1 ATOM 305 N N . LYS A 1 47 ? 26.471 39.745 60.727 1.00 9.36 ? 129 LYS A N 1 ATOM 306 C CA . LYS A 1 47 ? 25.271 40.503 61.075 1.00 9.36 ? 129 LYS A CA 1 ATOM 307 C C . LYS A 1 47 ? 24.889 41.534 60.015 1.00 9.36 ? 129 LYS A C 1 ATOM 308 O O . LYS A 1 47 ? 23.876 42.228 60.141 1.00 9.36 ? 129 LYS A O 1 ATOM 309 C CB . LYS A 1 47 ? 25.442 41.166 62.443 1.00 34.55 ? 129 LYS A CB 1 ATOM 310 C CG . LYS A 1 47 ? 25.649 40.166 63.570 1.00 34.55 ? 129 LYS A CG 1 ATOM 311 C CD . LYS A 1 47 ? 25.705 40.848 64.922 1.00 34.55 ? 129 LYS A CD 1 ATOM 312 C CE . LYS A 1 47 ? 25.971 39.846 66.036 1.00 34.55 ? 129 LYS A CE 1 ATOM 313 N NZ . LYS A 1 47 ? 27.348 39.265 65.975 1.00 34.55 ? 129 LYS A NZ 1 ATOM 314 N N . VAL A 1 48 ? 25.714 41.644 58.978 1.00 5.91 ? 130 VAL A N 1 ATOM 315 C CA . VAL A 1 48 ? 25.444 42.575 57.892 1.00 5.91 ? 130 VAL A CA 1 ATOM 316 C C . VAL A 1 48 ? 24.541 41.824 56.914 1.00 5.91 ? 130 VAL A C 1 ATOM 317 O O . VAL A 1 48 ? 24.867 40.714 56.484 1.00 5.91 ? 130 VAL A O 1 ATOM 318 C CB . VAL A 1 48 ? 26.746 43.019 57.186 1.00 6.71 ? 130 VAL A CB 1 ATOM 319 C CG1 . VAL A 1 48 ? 26.435 44.020 56.085 1.00 6.71 ? 130 VAL A CG1 1 ATOM 320 C CG2 . VAL A 1 48 ? 27.709 43.634 58.193 1.00 6.71 ? 130 VAL A CG2 1 ATOM 321 N N . PRO A 1 49 ? 23.366 42.392 56.601 1.00 8.63 ? 131 PRO A N 1 ATOM 322 C CA . PRO A 1 49 ? 22.439 41.735 55.675 1.00 8.63 ? 131 PRO A CA 1 ATOM 323 C C . PRO A 1 49 ? 22.944 41.670 54.233 1.00 8.63 ? 131 PRO A C 1 ATOM 324 O O . PRO A 1 49 ? 23.488 42.640 53.701 1.00 8.63 ? 131 PRO A O 1 ATOM 325 C CB . PRO A 1 49 ? 21.164 42.571 55.809 1.00 7.06 ? 131 PRO A CB 1 ATOM 326 C CG . PRO A 1 49 ? 21.670 43.930 56.169 1.00 7.06 ? 131 PRO A CG 1 ATOM 327 C CD . PRO A 1 49 ? 22.812 43.658 57.113 1.00 7.06 ? 131 PRO A CD 1 ATOM 328 N N . SER A 1 50 ? 22.813 40.490 53.640 1.00 8.06 ? 132 SER A N 1 ATOM 329 C CA . SER A 1 50 ? 23.221 40.250 52.260 1.00 8.06 ? 132 SER A CA 1 ATOM 330 C C . SER A 1 50 ? 22.138 39.415 51.570 1.00 8.06 ? 132 SER A C 1 ATOM 331 O O . SER A 1 50 ? 21.222 38.914 52.225 1.00 8.06 ? 132 SER A O 1 ATOM 332 C CB . SER A 1 50 ? 24.582 39.541 52.207 1.00 6.64 ? 132 SER A CB 1 ATOM 333 O OG . SER A 1 50 ? 24.590 38.335 52.953 1.00 6.64 ? 132 SER A OG 1 ATOM 334 N N . PHE A 1 51 ? 22.211 39.307 50.249 1.00 5.54 ? 133 PHE A N 1 ATOM 335 C CA . PHE A 1 51 ? 21.220 38.544 49.499 1.00 5.54 ? 133 PHE A CA 1 ATOM 336 C C . PHE A 1 51 ? 21.500 37.047 49.481 1.00 5.54 ? 133 PHE A C 1 ATOM 337 O O . PHE A 1 51 ? 22.656 36.628 49.504 1.00 5.54 ? 133 PHE A O 1 ATOM 338 C CB . PHE A 1 51 ? 21.128 39.066 48.056 1.00 2.69 ? 133 PHE A CB 1 ATOM 339 C CG . PHE A 1 51 ? 20.295 40.318 47.909 1.00 2.69 ? 133 PHE A CG 1 ATOM 340 C CD1 . PHE A 1 51 ? 20.704 41.520 48.478 1.00 2.69 ? 133 PHE A CD1 1 ATOM 341 C CD2 . PHE A 1 51 ? 19.092 40.282 47.217 1.00 2.69 ? 133 PHE A CD2 1 ATOM 342 C CE1 . PHE A 1 51 ? 19.925 42.667 48.363 1.00 2.69 ? 133 PHE A CE1 1 ATOM 343 C CE2 . PHE A 1 51 ? 18.303 41.423 47.094 1.00 2.69 ? 133 PHE A CE2 1 ATOM 344 C CZ . PHE A 1 51 ? 18.720 42.620 47.670 1.00 2.69 ? 133 PHE A CZ 1 ATOM 345 N N . MET A 1 52 ? 20.432 36.250 49.491 1.00 5.01 ? 134 MET A N 1 ATOM 346 C CA . MET A 1 52 ? 20.546 34.797 49.425 1.00 5.01 ? 134 MET A CA 1 ATOM 347 C C . MET A 1 52 ? 20.258 34.416 47.979 1.00 5.01 ? 134 MET A C 1 ATOM 348 O O . MET A 1 52 ? 19.262 34.855 47.409 1.00 5.01 ? 134 MET A O 1 ATOM 349 C CB . MET A 1 52 ? 19.537 34.109 50.349 1.00 17.95 ? 134 MET A CB 1 ATOM 350 C CG . MET A 1 52 ? 19.530 32.586 50.195 1.00 17.95 ? 134 MET A CG 1 ATOM 351 S SD . MET A 1 52 ? 18.330 31.712 51.222 1.00 17.95 ? 134 MET A SD 1 ATOM 352 C CE . MET A 1 52 ? 19.261 31.561 52.735 1.00 17.95 ? 134 MET A CE 1 ATOM 353 N N . TRP A 1 53 ? 21.121 33.595 47.390 1.00 7.28 ? 135 TRP A N 1 ATOM 354 C CA . TRP A 1 53 ? 20.960 33.184 45.998 1.00 7.28 ? 135 TRP A CA 1 ATOM 355 C C . TRP A 1 53 ? 20.222 31.866 45.789 1.00 7.28 ? 135 TRP A C 1 ATOM 356 O O . TRP A 1 53 ? 20.601 30.836 46.340 1.00 7.28 ? 135 TRP A O 1 ATOM 357 C CB . TRP A 1 53 ? 22.327 33.121 45.298 1.00 5.57 ? 135 TRP A CB 1 ATOM 358 C CG . TRP A 1 53 ? 23.044 34.441 45.223 1.00 5.57 ? 135 TRP A CG 1 ATOM 359 C CD1 . TRP A 1 53 ? 23.344 35.272 46.264 1.00 5.57 ? 135 TRP A CD1 1 ATOM 360 C CD2 . TRP A 1 53 ? 23.553 35.075 44.044 1.00 5.57 ? 135 TRP A CD2 1 ATOM 361 N NE1 . TRP A 1 53 ? 24.003 36.383 45.806 1.00 5.57 ? 135 TRP A NE1 1 ATOM 362 C CE2 . TRP A 1 53 ? 24.147 36.292 44.445 1.00 5.57 ? 135 TRP A CE2 1 ATOM 363 C CE3 . TRP A 1 53 ? 23.563 34.739 42.681 1.00 5.57 ? 135 TRP A CE3 1 ATOM 364 C CZ2 . TRP A 1 53 ? 24.744 37.174 43.543 1.00 5.57 ? 135 TRP A CZ2 1 ATOM 365 C CZ3 . TRP A 1 53 ? 24.160 35.621 41.776 1.00 5.57 ? 135 TRP A CZ3 1 ATOM 366 C CH2 . TRP A 1 53 ? 24.742 36.824 42.216 1.00 5.57 ? 135 TRP A CH2 1 ATOM 367 N N . LEU A 1 54 ? 19.173 31.908 44.973 1.00 4.92 ? 136 LEU A N 1 ATOM 368 C CA . LEU A 1 54 ? 18.389 30.718 44.647 1.00 4.92 ? 136 LEU A CA 1 ATOM 369 C C . LEU A 1 54 ? 18.905 30.272 43.281 1.00 4.92 ? 136 LEU A C 1 ATOM 370 O O . LEU A 1 54 ? 18.261 30.480 42.260 1.00 4.92 ? 136 LEU A O 1 ATOM 371 C CB . LEU A 1 54 ? 16.901 31.075 44.568 1.00 9.81 ? 136 LEU A CB 1 ATOM 372 C CG . LEU A 1 54 ? 16.381 31.908 45.746 1.00 9.81 ? 136 LEU A CG 1 ATOM 373 C CD1 . LEU A 1 54 ? 14.909 32.214 45.570 1.00 9.81 ? 136 LEU A CD1 1 ATOM 374 C CD2 . LEU A 1 54 ? 16.619 31.168 47.049 1.00 9.81 ? 136 LEU A CD2 1 ATOM 375 N N . ASP A 1 55 ? 20.097 29.687 43.272 1.00 8.38 ? 137 ASP A N 1 ATOM 376 C CA . ASP A 1 55 ? 20.737 29.254 42.035 1.00 8.38 ? 137 ASP A CA 1 ATOM 377 C C . ASP A 1 55 ? 20.321 27.882 41.502 1.00 8.38 ? 137 ASP A C 1 ATOM 378 O O . ASP A 1 55 ? 20.733 27.478 40.414 1.00 8.38 ? 137 ASP A O 1 ATOM 379 C CB . ASP A 1 55 ? 22.265 29.354 42.166 1.00 19.79 ? 137 ASP A CB 1 ATOM 380 C CG . ASP A 1 55 ? 22.822 28.491 43.288 1.00 19.79 ? 137 ASP A CG 1 ATOM 381 O OD1 . ASP A 1 55 ? 22.418 28.664 44.457 1.00 19.79 ? 137 ASP A OD1 1 ATOM 382 O OD2 . ASP A 1 55 ? 23.678 27.637 42.995 1.00 19.79 ? 137 ASP A OD2 1 ATOM 383 N N . THR A 1 56 ? 19.514 27.162 42.272 1.00 7.47 ? 138 THR A N 1 ATOM 384 C CA . THR A 1 56 ? 19.009 25.850 41.863 1.00 7.47 ? 138 THR A CA 1 ATOM 385 C C . THR A 1 56 ? 17.603 25.704 42.427 1.00 7.47 ? 138 THR A C 1 ATOM 386 O O . THR A 1 56 ? 17.232 26.422 43.358 1.00 7.47 ? 138 THR A O 1 ATOM 387 C CB . THR A 1 56 ? 19.847 24.686 42.434 1.00 9.16 ? 138 THR A CB 1 ATOM 388 O OG1 . THR A 1 56 ? 19.930 24.818 43.858 1.00 9.16 ? 138 THR A OG1 1 ATOM 389 C CG2 . THR A 1 56 ? 21.243 24.662 41.839 1.00 9.16 ? 138 THR A CG2 1 ATOM 390 N N . LEU A 1 57 ? 16.841 24.757 41.889 1.00 8.32 ? 139 LEU A N 1 ATOM 391 C CA . LEU A 1 57 ? 15.491 24.529 42.373 1.00 8.32 ? 139 LEU A CA 1 ATOM 392 C C . LEU A 1 57 ? 15.539 24.027 43.815 1.00 8.32 ? 139 LEU A C 1 ATOM 393 O O . LEU A 1 57 ? 14.716 24.428 44.636 1.00 8.32 ? 139 LEU A O 1 ATOM 394 C CB . LEU A 1 57 ? 14.747 23.525 41.492 1.00 8.39 ? 139 LEU A CB 1 ATOM 395 C CG . LEU A 1 57 ? 13.292 23.247 41.903 1.00 8.39 ? 139 LEU A CG 1 ATOM 396 C CD1 . LEU A 1 57 ? 12.468 24.530 41.851 1.00 8.39 ? 139 LEU A CD1 1 ATOM 397 C CD2 . LEU A 1 57 ? 12.693 22.203 40.987 1.00 8.39 ? 139 LEU A CD2 1 ATOM 398 N N . ASP A 1 58 ? 16.535 23.198 44.131 1.00 9.25 ? 140 ASP A N 1 ATOM 399 C CA . ASP A 1 58 ? 16.654 22.676 45.490 1.00 9.25 ? 140 ASP A CA 1 ATOM 400 C C . ASP A 1 58 ? 17.015 23.724 46.540 1.00 9.25 ? 140 ASP A C 1 ATOM 401 O O . ASP A 1 58 ? 17.147 23.404 47.721 1.00 9.25 ? 140 ASP A O 1 ATOM 402 C CB . ASP A 1 58 ? 17.597 21.468 45.560 1.00 76.25 ? 140 ASP A CB 1 ATOM 403 C CG . ASP A 1 58 ? 18.910 21.704 44.853 1.00 76.25 ? 140 ASP A CG 1 ATOM 404 O OD1 . ASP A 1 58 ? 19.698 22.548 45.317 1.00 76.25 ? 140 ASP A OD1 1 ATOM 405 O OD2 . ASP A 1 58 ? 19.165 21.019 43.840 1.00 76.25 ? 140 ASP A OD2 1 ATOM 406 N N . LYS A 1 59 ? 17.173 24.972 46.106 1.00 8.17 ? 141 LYS A N 1 ATOM 407 C CA . LYS A 1 59 ? 17.462 26.074 47.016 1.00 8.17 ? 141 LYS A CA 1 ATOM 408 C C . LYS A 1 59 ? 16.145 26.691 47.500 1.00 8.17 ? 141 LYS A C 1 ATOM 409 O O . LYS A 1 59 ? 16.124 27.384 48.515 1.00 8.17 ? 141 LYS A O 1 ATOM 410 C CB . LYS A 1 59 ? 18.301 27.150 46.322 1.00 32.21 ? 141 LYS A CB 1 ATOM 411 C CG . LYS A 1 59 ? 19.802 26.926 46.390 1.00 32.21 ? 141 LYS A CG 1 ATOM 412 C CD . LYS A 1 59 ? 20.311 27.037 47.816 1.00 32.21 ? 141 LYS A CD 1 ATOM 413 C CE . LYS A 1 59 ? 21.839 27.056 47.873 1.00 32.21 ? 141 LYS A CE 1 ATOM 414 N NZ . LYS A 1 59 ? 22.434 28.355 47.418 1.00 32.21 ? 141 LYS A NZ 1 ATOM 415 N N . THR A 1 60 ? 15.047 26.421 46.793 1.00 7.63 ? 142 THR A N 1 ATOM 416 C CA . THR A 1 60 ? 13.745 26.979 47.178 1.00 7.63 ? 142 THR A CA 1 ATOM 417 C C . THR A 1 60 ? 13.283 26.653 48.605 1.00 7.63 ? 142 THR A C 1 ATOM 418 O O . THR A 1 60 ? 12.687 27.506 49.263 1.00 7.63 ? 142 THR A O 1 ATOM 419 C CB . THR A 1 60 ? 12.625 26.696 46.127 1.00 8.20 ? 142 THR A CB 1 ATOM 420 O OG1 . THR A 1 60 ? 12.557 25.296 45.836 1.00 8.20 ? 142 THR A OG1 1 ATOM 421 C CG2 . THR A 1 60 ? 12.901 27.472 44.839 1.00 8.20 ? 142 THR A CG2 1 ATOM 422 N N . PRO A 1 61 ? 13.524 25.418 49.098 1.00 11.58 ? 143 PRO A N 1 ATOM 423 C CA . PRO A 1 61 ? 13.101 25.105 50.471 1.00 11.58 ? 143 PRO A CA 1 ATOM 424 C C . PRO A 1 61 ? 13.826 26.027 51.459 1.00 11.58 ? 143 PRO A C 1 ATOM 425 O O . PRO A 1 61 ? 13.308 26.346 52.527 1.00 11.58 ? 143 PRO A O 1 ATOM 426 C CB . PRO A 1 61 ? 13.575 23.664 50.657 1.00 12.30 ? 143 PRO A CB 1 ATOM 427 C CG . PRO A 1 61 ? 13.504 23.091 49.290 1.00 12.30 ? 143 PRO A CG 1 ATOM 428 C CD . PRO A 1 61 ? 14.010 24.206 48.410 1.00 12.30 ? 143 PRO A CD 1 ATOM 429 N N . LEU A 1 62 ? 15.035 26.440 51.084 1.00 10.53 ? 144 LEU A N 1 ATOM 430 C CA . LEU A 1 62 ? 15.857 27.324 51.905 1.00 10.53 ? 144 LEU A CA 1 ATOM 431 C C . LEU A 1 62 ? 15.253 28.727 51.947 1.00 10.53 ? 144 LEU A C 1 ATOM 432 O O . LEU A 1 62 ? 15.408 29.450 52.931 1.00 10.53 ? 144 LEU A O 1 ATOM 433 C CB . LEU A 1 62 ? 17.281 27.369 51.350 1.00 26.30 ? 144 LEU A CB 1 ATOM 434 C CG . LEU A 1 62 ? 18.405 27.793 52.290 1.00 26.30 ? 144 LEU A CG 1 ATOM 435 C CD1 . LEU A 1 62 ? 18.423 26.885 53.505 1.00 26.30 ? 144 LEU A CD1 1 ATOM 436 C CD2 . LEU A 1 62 ? 19.730 27.717 51.551 1.00 26.30 ? 144 LEU A CD2 1 ATOM 437 N N . MET A 1 63 ? 14.591 29.118 50.860 1.00 7.23 ? 145 MET A N 1 ATOM 438 C CA . MET A 1 63 ? 13.932 30.421 50.796 1.00 7.23 ? 145 MET A CA 1 ATOM 439 C C . MET A 1 63 ? 12.743 30.428 51.758 1.00 7.23 ? 145 MET A C 1 ATOM 440 O O . MET A 1 63 ? 12.508 31.406 52.469 1.00 7.23 ? 145 MET A O 1 ATOM 441 C CB . MET A 1 63 ? 13.428 30.696 49.382 1.00 7.83 ? 145 MET A CB 1 ATOM 442 C CG . MET A 1 63 ? 12.639 31.983 49.271 1.00 7.83 ? 145 MET A CG 1 ATOM 443 S SD . MET A 1 63 ? 11.842 32.174 47.688 1.00 7.83 ? 145 MET A SD 1 ATOM 444 C CE . MET A 1 63 ? 11.311 33.868 47.812 1.00 7.83 ? 145 MET A CE 1 ATOM 445 N N . GLU A 1 64 ? 11.991 29.330 51.762 1.00 7.29 ? 146 GLU A N 1 ATOM 446 C CA . GLU A 1 64 ? 10.826 29.187 52.630 1.00 7.29 ? 146 GLU A CA 1 ATOM 447 C C . GLU A 1 64 ? 11.262 29.154 54.099 1.00 7.29 ? 146 GLU A C 1 ATOM 448 O O . GLU A 1 64 ? 10.608 29.722 54.975 1.00 7.29 ? 146 GLU A O 1 ATOM 449 C CB . GLU A 1 64 ? 10.074 27.907 52.266 1.00 27.88 ? 146 GLU A CB 1 ATOM 450 C CG . GLU A 1 64 ? 8.740 27.751 52.964 1.00 27.88 ? 146 GLU A CG 1 ATOM 451 C CD . GLU A 1 64 ? 7.920 26.587 52.430 1.00 27.88 ? 146 GLU A CD 1 ATOM 452 O OE1 . GLU A 1 64 ? 8.429 25.812 51.588 1.00 27.88 ? 146 GLU A OE1 1 ATOM 453 O OE2 . GLU A 1 64 ? 6.755 26.449 52.857 1.00 27.88 ? 146 GLU A OE2 1 ATOM 454 N N . GLN A 1 65 ? 12.392 28.505 54.347 1.00 12.87 ? 147 GLN A N 1 ATOM 455 C CA . GLN A 1 65 ? 12.960 28.380 55.684 1.00 12.87 ? 147 GLN A CA 1 ATOM 456 C C . GLN A 1 65 ? 13.369 29.763 56.210 1.00 12.87 ? 147 GLN A C 1 ATOM 457 O O . GLN A 1 65 ? 13.140 30.092 57.377 1.00 12.87 ? 147 GLN A O 1 ATOM 458 C CB . GLN A 1 65 ? 14.174 27.455 55.610 1.00 83.05 ? 147 GLN A CB 1 ATOM 459 C CG . GLN A 1 65 ? 14.788 27.050 56.932 1.00 83.05 ? 147 GLN A CG 1 ATOM 460 C CD . GLN A 1 65 ? 16.001 26.158 56.735 1.00 83.05 ? 147 GLN A CD 1 ATOM 461 O OE1 . GLN A 1 65 ? 17.089 26.447 57.238 1.00 83.05 ? 147 GLN A OE1 1 ATOM 462 N NE2 . GLN A 1 65 ? 15.826 25.080 55.973 1.00 83.05 ? 147 GLN A NE2 1 ATOM 463 N N . THR A 1 66 ? 13.957 30.573 55.331 1.00 11.02 ? 148 THR A N 1 ATOM 464 C CA . THR A 1 66 ? 14.405 31.922 55.672 1.00 11.02 ? 148 THR A CA 1 ATOM 465 C C . THR A 1 66 ? 13.219 32.822 55.995 1.00 11.02 ? 148 THR A C 1 ATOM 466 O O . THR A 1 66 ? 13.251 33.580 56.966 1.00 11.02 ? 148 THR A O 1 ATOM 467 C CB . THR A 1 66 ? 15.223 32.541 54.510 1.00 7.48 ? 148 THR A CB 1 ATOM 468 O OG1 . THR A 1 66 ? 16.363 31.717 54.242 1.00 7.48 ? 148 THR A OG1 1 ATOM 469 C CG2 . THR A 1 66 ? 15.694 33.947 54.857 1.00 7.48 ? 148 THR A CG2 1 ATOM 470 N N . LEU A 1 67 ? 12.172 32.731 55.178 1.00 7.90 ? 149 LEU A N 1 ATOM 471 C CA . LEU A 1 67 ? 10.969 33.528 55.379 1.00 7.90 ? 149 LEU A CA 1 ATOM 472 C C . LEU A 1 67 ? 10.261 33.126 56.670 1.00 7.90 ? 149 LEU A C 1 ATOM 473 O O . LEU A 1 67 ? 9.669 33.965 57.336 1.00 7.90 ? 149 LEU A O 1 ATOM 474 C CB . LEU A 1 67 ? 10.037 33.405 54.170 1.00 4.48 ? 149 LEU A CB 1 ATOM 475 C CG . LEU A 1 67 ? 10.563 34.099 52.906 1.00 4.48 ? 149 LEU A CG 1 ATOM 476 C CD1 . LEU A 1 67 ? 9.770 33.675 51.683 1.00 4.48 ? 149 LEU A CD1 1 ATOM 477 C CD2 . LEU A 1 67 ? 10.510 35.608 53.090 1.00 4.48 ? 149 LEU A CD2 1 ATOM 478 N N . ALA A 1 68 ? 10.350 31.851 57.037 1.00 12.57 ? 150 ALA A N 1 ATOM 479 C CA . ALA A 1 68 ? 9.744 31.375 58.278 1.00 12.57 ? 150 ALA A CA 1 ATOM 480 C C . ALA A 1 68 ? 10.454 32.051 59.455 1.00 12.57 ? 150 ALA A C 1 ATOM 481 O O . ALA A 1 68 ? 9.803 32.535 60.382 1.00 12.57 ? 150 ALA A O 1 ATOM 482 C CB . ALA A 1 68 ? 9.866 29.863 58.383 1.00 4.34 ? 150 ALA A CB 1 ATOM 483 N N . ASP A 1 69 ? 11.787 32.101 59.394 1.00 11.93 ? 151 ASP A N 1 ATOM 484 C CA . ASP A 1 69 ? 12.600 32.740 60.432 1.00 11.93 ? 151 ASP A CA 1 ATOM 485 C C . ASP A 1 69 ? 12.220 34.208 60.570 1.00 11.93 ? 151 ASP A C 1 ATOM 486 O O . ASP A 1 69 ? 12.155 34.742 61.677 1.00 11.93 ? 151 ASP A O 1 ATOM 487 C CB . ASP A 1 69 ? 14.092 32.670 60.089 1.00 22.41 ? 151 ASP A CB 1 ATOM 488 C CG . ASP A 1 69 ? 14.675 31.279 60.235 1.00 22.41 ? 151 ASP A CG 1 ATOM 489 O OD1 . ASP A 1 69 ? 13.982 30.367 60.734 1.00 22.41 ? 151 ASP A OD1 1 ATOM 490 O OD2 . ASP A 1 69 ? 15.851 31.105 59.852 1.00 22.41 ? 151 ASP A OD2 1 ATOM 491 N N . ILE A 1 70 ? 12.010 34.864 59.431 1.00 9.41 ? 152 ILE A N 1 ATOM 492 C CA . ILE A 1 70 ? 11.639 36.273 59.406 1.00 9.41 ? 152 ILE A CA 1 ATOM 493 C C . ILE A 1 70 ? 10.251 36.488 59.993 1.00 9.41 ? 152 ILE A C 1 ATOM 494 O O . ILE A 1 70 ? 10.037 37.441 60.739 1.00 9.41 ? 152 ILE A O 1 ATOM 495 C CB . ILE A 1 70 ? 11.686 36.840 57.973 1.00 7.61 ? 152 ILE A CB 1 ATOM 496 C CG1 . ILE A 1 70 ? 13.113 36.757 57.433 1.00 7.61 ? 152 ILE A CG1 1 ATOM 497 C CG2 . ILE A 1 70 ? 11.211 38.290 57.957 1.00 7.61 ? 152 ILE A CG2 1 ATOM 498 C CD1 . ILE A 1 70 ? 13.236 37.111 55.964 1.00 7.61 ? 152 ILE A CD1 1 ATOM 499 N N . ARG A 1 71 ? 9.311 35.607 59.660 1.00 12.30 ? 153 ARG A N 1 ATOM 500 C CA . ARG A 1 71 ? 7.953 35.728 60.183 1.00 12.30 ? 153 ARG A CA 1 ATOM 501 C C . ARG A 1 71 ? 8.004 35.666 61.702 1.00 12.30 ? 153 ARG A C 1 ATOM 502 O O . ARG A 1 71 ? 7.367 36.465 62.381 1.00 12.30 ? 153 ARG A O 1 ATOM 503 C CB . ARG A 1 71 ? 7.040 34.620 59.647 1.00 20.26 ? 153 ARG A CB 1 ATOM 504 C CG . ARG A 1 71 ? 5.643 34.657 60.254 1.00 20.26 ? 153 ARG A CG 1 ATOM 505 C CD . ARG A 1 71 ? 4.547 34.511 59.217 1.00 20.26 ? 153 ARG A CD 1 ATOM 506 N NE . ARG A 1 71 ? 4.327 33.134 58.800 1.00 20.26 ? 153 ARG A NE 1 ATOM 507 C CZ . ARG A 1 71 ? 3.692 32.779 57.687 1.00 20.26 ? 153 ARG A CZ 1 ATOM 508 N NH1 . ARG A 1 71 ? 3.214 33.695 56.856 1.00 20.26 ? 153 ARG A NH1 1 ATOM 509 N NH2 . ARG A 1 71 ? 3.506 31.494 57.423 1.00 20.26 ? 153 ARG A NH2 1 ATOM 510 N N . THR A 1 72 ? 8.799 34.743 62.230 1.00 13.15 ? 154 THR A N 1 ATOM 511 C CA . THR A 1 72 ? 8.928 34.605 63.672 1.00 13.15 ? 154 THR A CA 1 ATOM 512 C C . THR A 1 72 ? 9.583 35.827 64.277 1.00 13.15 ? 154 THR A C 1 ATOM 513 O O . THR A 1 72 ? 9.144 36.316 65.310 1.00 13.15 ? 154 THR A O 1 ATOM 514 C CB . THR A 1 72 ? 9.763 33.403 64.048 1.00 14.87 ? 154 THR A CB 1 ATOM 515 O OG1 . THR A 1 72 ? 9.089 32.209 63.632 1.00 14.87 ? 154 THR A OG1 1 ATOM 516 C CG2 . THR A 1 72 ? 9.990 33.384 65.554 1.00 14.87 ? 154 THR A CG2 1 ATOM 517 N N . ALA A 1 73 ? 10.651 36.297 63.638 1.00 12.79 ? 155 ALA A N 1 ATOM 518 C CA . ALA A 1 73 ? 11.375 37.475 64.098 1.00 12.79 ? 155 ALA A CA 1 ATOM 519 C C . ALA A 1 73 ? 10.428 38.665 64.169 1.00 12.79 ? 155 ALA A C 1 ATOM 520 O O . ALA A 1 73 ? 10.446 39.413 65.136 1.00 12.79 ? 155 ALA A O 1 ATOM 521 C CB . ALA A 1 73 ? 12.536 37.780 63.162 1.00 10.57 ? 155 ALA A CB 1 ATOM 522 N N . ASN A 1 74 ? 9.572 38.799 63.160 1.00 15.37 ? 156 ASN A N 1 ATOM 523 C CA . ASN A 1 74 ? 8.598 39.880 63.094 1.00 15.37 ? 156 ASN A CA 1 ATOM 524 C C . ASN A 1 74 ? 7.457 39.629 64.070 1.00 15.37 ? 156 ASN A C 1 ATOM 525 O O . ASN A 1 74 ? 6.859 40.570 64.591 1.00 15.37 ? 156 ASN A O 1 ATOM 526 C CB . ASN A 1 74 ? 8.046 40.017 61.677 1.00 13.29 ? 156 ASN A CB 1 ATOM 527 C CG . ASN A 1 74 ? 9.071 40.556 60.702 1.00 13.29 ? 156 ASN A CG 1 ATOM 528 O OD1 . ASN A 1 74 ? 10.212 40.839 61.076 1.00 13.29 ? 156 ASN A OD1 1 ATOM 529 N ND2 . ASN A 1 74 ? 8.670 40.703 59.441 1.00 13.29 ? 156 ASN A ND2 1 ATOM 530 N N . LYS A 1 75 ? 7.125 38.354 64.265 1.00 38.41 ? 157 LYS A N 1 ATOM 531 C CA . LYS A 1 75 ? 6.078 37.947 65.201 1.00 38.41 ? 157 LYS A CA 1 ATOM 532 C C . LYS A 1 75 ? 6.697 38.185 66.567 1.00 38.41 ? 157 LYS A C 1 ATOM 533 O O . LYS A 1 75 ? 6.003 38.287 67.566 1.00 38.41 ? 157 LYS A O 1 ATOM 534 C CB . LYS A 1 75 ? 5.736 36.465 65.012 1.00 69.82 ? 157 LYS A CB 1 ATOM 535 C CG . LYS A 1 75 ? 4.530 35.951 65.805 1.00 69.82 ? 157 LYS A CG 1 ATOM 536 C CD . LYS A 1 75 ? 4.892 35.556 67.233 1.00 69.82 ? 157 LYS A CD 1 ATOM 537 C CE . LYS A 1 75 ? 3.682 35.044 68.001 1.00 69.82 ? 157 LYS A CE 1 ATOM 538 N NZ . LYS A 1 75 ? 4.013 34.713 69.416 1.00 69.82 ? 157 LYS A NZ 1 ATOM 539 N N . ASN A 1 76 ? 8.023 38.261 66.582 1.00 61.63 ? 158 ASN A N 1 ATOM 540 C CA . ASN A 1 76 ? 8.781 38.502 67.787 1.00 61.63 ? 158 ASN A CA 1 ATOM 541 C C . ASN A 1 76 ? 9.329 39.918 67.790 1.00 61.63 ? 158 ASN A C 1 ATOM 542 O O . ASN A 1 76 ? 10.482 40.167 68.163 1.00 61.63 ? 158 ASN A O 1 ATOM 543 C CB . ASN A 1 76 ? 9.894 37.468 67.953 1.00 55.25 ? 158 ASN A CB 1 ATOM 544 C CG . ASN A 1 76 ? 9.375 36.145 68.481 1.00 55.25 ? 158 ASN A CG 1 ATOM 545 O OD1 . ASN A 1 76 ? 10.241 35.146 68.522 1.00 55.25 ? 158 ASN A OD1 1 ATOM 546 N ND2 . ASN A 1 76 ? 8.210 36.025 68.862 1.00 55.25 ? 158 ASN A ND2 1 ATOM 547 N N . GLY A 1 77 ? 8.493 40.836 67.316 1.00 44.94 ? 159 GLY A N 1 ATOM 548 C CA . GLY A 1 77 ? 8.830 42.247 67.267 1.00 44.94 ? 159 GLY A CA 1 ATOM 549 C C . GLY A 1 77 ? 9.706 42.830 66.177 1.00 44.94 ? 159 GLY A C 1 ATOM 550 O O . GLY A 1 77 ? 9.921 44.031 66.146 1.00 44.94 ? 159 GLY A O 1 ATOM 551 N N . GLY A 1 78 ? 10.202 41.991 65.282 1.00 26.25 ? 160 GLY A N 1 ATOM 552 C CA . GLY A 1 78 ? 11.049 42.491 64.221 1.00 26.25 ? 160 GLY A CA 1 ATOM 553 C C . GLY A 1 78 ? 10.251 43.186 63.139 1.00 26.25 ? 160 GLY A C 1 ATOM 554 O O . GLY A 1 78 ? 9.018 43.168 63.145 1.00 26.25 ? 160 GLY A O 1 ATOM 555 N N . ASN A 1 79 ? 10.967 43.808 62.213 1.00 19.55 ? 161 ASN A N 1 ATOM 556 C CA . ASN A 1 79 ? 10.370 44.516 61.088 1.00 19.55 ? 161 ASN A CA 1 ATOM 557 C C . ASN A 1 79 ? 11.359 44.271 59.949 1.00 19.55 ? 161 ASN A C 1 ATOM 558 O O . ASN A 1 79 ? 11.913 45.200 59.357 1.00 19.55 ? 161 ASN A O 1 ATOM 559 C CB . ASN A 1 79 ? 10.259 46.005 61.416 1.00 25.48 ? 161 ASN A CB 1 ATOM 560 C CG . ASN A 1 79 ? 9.541 46.787 60.344 1.00 25.48 ? 161 ASN A CG 1 ATOM 561 O OD1 . ASN A 1 79 ? 8.637 46.275 59.680 1.00 25.48 ? 161 ASN A OD1 1 ATOM 562 N ND2 . ASN A 1 79 ? 9.946 48.039 60.161 1.00 25.48 ? 161 ASN A ND2 1 ATOM 563 N N . TYR A 1 80 ? 11.587 42.988 59.681 1.00 11.12 ? 162 TYR A N 1 ATOM 564 C CA . TYR A 1 80 ? 12.530 42.546 58.667 1.00 11.12 ? 162 TYR A CA 1 ATOM 565 C C . TYR A 1 80 ? 11.920 42.194 57.326 1.00 11.12 ? 162 TYR A C 1 ATOM 566 O O . TYR A 1 80 ? 10.758 41.792 57.241 1.00 11.12 ? 162 TYR A O 1 ATOM 567 C CB . TYR A 1 80 ? 13.312 41.341 59.185 1.00 20.43 ? 162 TYR A CB 1 ATOM 568 C CG . TYR A 1 80 ? 14.093 41.625 60.442 1.00 20.43 ? 162 TYR A CG 1 ATOM 569 C CD1 . TYR A 1 80 ? 15.300 42.323 60.393 1.00 20.43 ? 162 TYR A CD1 1 ATOM 570 C CD2 . TYR A 1 80 ? 13.626 41.202 61.682 1.00 20.43 ? 162 TYR A CD2 1 ATOM 571 C CE1 . TYR A 1 80 ? 16.022 42.594 61.549 1.00 20.43 ? 162 TYR A CE1 1 ATOM 572 C CE2 . TYR A 1 80 ? 14.341 41.467 62.849 1.00 20.43 ? 162 TYR A CE2 1 ATOM 573 C CZ . TYR A 1 80 ? 15.538 42.163 62.775 1.00 20.43 ? 162 TYR A CZ 1 ATOM 574 O OH . TYR A 1 80 ? 16.246 42.429 63.924 1.00 20.43 ? 162 TYR A OH 1 ATOM 575 N N . ALA A 1 81 ? 12.750 42.302 56.290 1.00 11.72 ? 163 ALA A N 1 ATOM 576 C CA . ALA A 1 81 ? 12.368 41.993 54.919 1.00 11.72 ? 163 ALA A CA 1 ATOM 577 C C . ALA A 1 81 ? 13.344 40.962 54.354 1.00 11.72 ? 163 ALA A C 1 ATOM 578 O O . ALA A 1 81 ? 14.514 40.925 54.743 1.00 11.72 ? 163 ALA A O 1 ATOM 579 C CB . ALA A 1 81 ? 12.394 43.258 54.073 1.00 5.25 ? 163 ALA A CB 1 ATOM 580 N N . GLY A 1 82 ? 12.857 40.107 53.462 1.00 7.62 ? 164 GLY A N 1 ATOM 581 C CA . GLY A 1 82 ? 13.716 39.103 52.864 1.00 7.62 ? 164 GLY A CA 1 ATOM 582 C C . GLY A 1 82 ? 14.408 39.645 51.628 1.00 7.62 ? 164 GLY A C 1 ATOM 583 O O . GLY A 1 82 ? 13.894 40.555 50.972 1.00 7.62 ? 164 GLY A O 1 ATOM 584 N N . GLN A 1 83 ? 15.583 39.099 51.319 1.00 3.43 ? 165 GLN A N 1 ATOM 585 C CA . GLN A 1 83 ? 16.370 39.511 50.156 1.00 3.43 ? 165 GLN A CA 1 ATOM 586 C C . GLN A 1 83 ? 16.876 38.259 49.435 1.00 3.43 ? 165 GLN A C 1 ATOM 587 O O . GLN A 1 83 ? 17.683 37.504 49.985 1.00 3.43 ? 165 GLN A O 1 ATOM 588 C CB . GLN A 1 83 ? 17.571 40.357 50.594 1.00 7.95 ? 165 GLN A CB 1 ATOM 589 C CG . GLN A 1 83 ? 17.226 41.603 51.398 1.00 7.95 ? 165 GLN A CG 1 ATOM 590 C CD . GLN A 1 83 ? 18.413 42.526 51.574 1.00 7.95 ? 165 GLN A CD 1 ATOM 591 O OE1 . GLN A 1 83 ? 18.326 43.722 51.296 1.00 7.95 ? 165 GLN A OE1 1 ATOM 592 N NE2 . GLN A 1 83 ? 19.534 41.977 52.030 1.00 7.95 ? 165 GLN A NE2 1 ATOM 593 N N . PHE A 1 84 ? 16.418 38.050 48.204 1.00 2.00 ? 166 PHE A N 1 ATOM 594 C CA . PHE A 1 84 ? 16.823 36.874 47.440 1.00 2.00 ? 166 PHE A CA 1 ATOM 595 C C . PHE A 1 84 ? 17.219 37.212 46.001 1.00 2.00 ? 166 PHE A C 1 ATOM 596 O O . PHE A 1 84 ? 16.840 38.260 45.469 1.00 2.00 ? 166 PHE A O 1 ATOM 597 C CB . PHE A 1 84 ? 15.688 35.833 47.422 1.00 5.47 ? 166 PHE A CB 1 ATOM 598 C CG . PHE A 1 84 ? 15.170 35.472 48.785 1.00 5.47 ? 166 PHE A CG 1 ATOM 599 C CD1 . PHE A 1 84 ? 15.791 34.481 49.541 1.00 5.47 ? 166 PHE A CD1 1 ATOM 600 C CD2 . PHE A 1 84 ? 14.079 36.145 49.332 1.00 5.47 ? 166 PHE A CD2 1 ATOM 601 C CE1 . PHE A 1 84 ? 15.341 34.170 50.822 1.00 5.47 ? 166 PHE A CE1 1 ATOM 602 C CE2 . PHE A 1 84 ? 13.618 35.839 50.620 1.00 5.47 ? 166 PHE A CE2 1 ATOM 603 C CZ . PHE A 1 84 ? 14.255 34.849 51.362 1.00 5.47 ? 166 PHE A CZ 1 ATOM 604 N N . VAL A 1 85 ? 17.986 36.317 45.382 1.00 4.07 ? 167 VAL A N 1 ATOM 605 C CA . VAL A 1 85 ? 18.416 36.490 44.000 1.00 4.07 ? 167 VAL A CA 1 ATOM 606 C C . VAL A 1 85 ? 17.863 35.339 43.165 1.00 4.07 ? 167 VAL A C 1 ATOM 607 O O . VAL A 1 85 ? 18.094 34.174 43.493 1.00 4.07 ? 167 VAL A O 1 ATOM 608 C CB . VAL A 1 85 ? 19.965 36.485 43.861 1.00 2.00 ? 167 VAL A CB 1 ATOM 609 C CG1 . VAL A 1 85 ? 20.367 36.696 42.408 1.00 2.00 ? 167 VAL A CG1 1 ATOM 610 C CG2 . VAL A 1 85 ? 20.590 37.565 44.743 1.00 2.00 ? 167 VAL A CG2 1 ATOM 611 N N . VAL A 1 86 ? 17.088 35.664 42.130 1.00 2.00 ? 168 VAL A N 1 ATOM 612 C CA . VAL A 1 86 ? 16.530 34.652 41.224 1.00 2.00 ? 168 VAL A CA 1 ATOM 613 C C . VAL A 1 86 ? 17.623 34.425 40.183 1.00 2.00 ? 168 VAL A C 1 ATOM 614 O O . VAL A 1 86 ? 17.967 35.339 39.433 1.00 2.00 ? 168 VAL A O 1 ATOM 615 C CB . VAL A 1 86 ? 15.237 35.153 40.555 1.00 9.72 ? 168 VAL A CB 1 ATOM 616 C CG1 . VAL A 1 86 ? 14.677 34.091 39.626 1.00 9.72 ? 168 VAL A CG1 1 ATOM 617 C CG2 . VAL A 1 86 ? 14.212 35.518 41.626 1.00 9.72 ? 168 VAL A CG2 1 ATOM 618 N N . PHE A 1 87 ? 18.157 33.208 40.124 1.00 6.24 ? 169 PHE A N 1 ATOM 619 C CA . PHE A 1 87 ? 19.284 32.929 39.236 1.00 6.24 ? 169 PHE A CA 1 ATOM 620 C C . PHE A 1 87 ? 19.331 31.476 38.749 1.00 6.24 ? 169 PHE A C 1 ATOM 621 O O . PHE A 1 87 ? 20.145 30.682 39.223 1.00 6.24 ? 169 PHE A O 1 ATOM 622 C CB . PHE A 1 87 ? 20.555 33.279 40.030 1.00 6.53 ? 169 PHE A CB 1 ATOM 623 C CG . PHE A 1 87 ? 21.826 33.232 39.240 1.00 6.53 ? 169 PHE A CG 1 ATOM 624 C CD1 . PHE A 1 87 ? 21.963 33.947 38.058 1.00 6.53 ? 169 PHE A CD1 1 ATOM 625 C CD2 . PHE A 1 87 ? 22.919 32.526 39.726 1.00 6.53 ? 169 PHE A CD2 1 ATOM 626 C CE1 . PHE A 1 87 ? 23.175 33.964 37.375 1.00 6.53 ? 169 PHE A CE1 1 ATOM 627 C CE2 . PHE A 1 87 ? 24.134 32.537 39.052 1.00 6.53 ? 169 PHE A CE2 1 ATOM 628 C CZ . PHE A 1 87 ? 24.262 33.258 37.876 1.00 6.53 ? 169 PHE A CZ 1 ATOM 629 N N . ASP A 1 88 ? 18.496 31.141 37.767 1.00 7.74 ? 170 ASP A N 1 ATOM 630 C CA . ASP A 1 88 ? 18.466 29.772 37.253 1.00 7.74 ? 170 ASP A CA 1 ATOM 631 C C . ASP A 1 88 ? 17.945 29.669 35.820 1.00 7.74 ? 170 ASP A C 1 ATOM 632 O O . ASP A 1 88 ? 17.299 28.687 35.446 1.00 7.74 ? 170 ASP A O 1 ATOM 633 C CB . ASP A 1 88 ? 17.623 28.895 38.178 1.00 6.74 ? 170 ASP A CB 1 ATOM 634 C CG . ASP A 1 88 ? 18.018 27.434 38.128 1.00 6.74 ? 170 ASP A CG 1 ATOM 635 O OD1 . ASP A 1 88 ? 19.057 27.094 37.524 1.00 6.74 ? 170 ASP A OD1 1 ATOM 636 O OD2 . ASP A 1 88 ? 17.279 26.620 38.709 1.00 6.74 ? 170 ASP A OD2 1 ATOM 637 N N . LEU A 1 89 ? 18.265 30.677 35.019 1.00 8.70 ? 171 LEU A N 1 ATOM 638 C CA . LEU A 1 89 ? 17.856 30.751 33.623 1.00 8.70 ? 171 LEU A CA 1 ATOM 639 C C . LEU A 1 89 ? 18.457 29.591 32.818 1.00 8.70 ? 171 LEU A C 1 ATOM 640 O O . LEU A 1 89 ? 19.571 29.149 33.101 1.00 8.70 ? 171 LEU A O 1 ATOM 641 C CB . LEU A 1 89 ? 18.351 32.084 33.061 1.00 7.86 ? 171 LEU A CB 1 ATOM 642 C CG . LEU A 1 89 ? 17.513 32.962 32.141 1.00 7.86 ? 171 LEU A CG 1 ATOM 643 C CD1 . LEU A 1 89 ? 16.092 33.122 32.637 1.00 7.86 ? 171 LEU A CD1 1 ATOM 644 C CD2 . LEU A 1 89 ? 18.207 34.319 32.053 1.00 7.86 ? 171 LEU A CD2 1 ATOM 645 N N . PRO A 1 90 ? 17.700 29.038 31.849 1.00 9.87 ? 172 PRO A N 1 ATOM 646 C CA . PRO A 1 90 ? 18.229 27.931 31.040 1.00 9.87 ? 172 PRO A CA 1 ATOM 647 C C . PRO A 1 90 ? 19.383 28.472 30.193 1.00 9.87 ? 172 PRO A C 1 ATOM 648 O O . PRO A 1 90 ? 19.305 29.598 29.697 1.00 9.87 ? 172 PRO A O 1 ATOM 649 C CB . PRO A 1 90 ? 17.028 27.525 30.186 1.00 9.20 ? 172 PRO A CB 1 ATOM 650 C CG . PRO A 1 90 ? 16.227 28.786 30.078 1.00 9.20 ? 172 PRO A CG 1 ATOM 651 C CD . PRO A 1 90 ? 16.317 29.365 31.461 1.00 9.20 ? 172 PRO A CD 1 ATOM 652 N N . ASP A 1 91 ? 20.444 27.680 30.038 1.00 9.68 ? 173 ASP A N 1 ATOM 653 C CA . ASP A 1 91 ? 21.634 28.106 29.298 1.00 9.68 ? 173 ASP A CA 1 ATOM 654 C C . ASP A 1 91 ? 22.185 29.370 29.962 1.00 9.68 ? 173 ASP A C 1 ATOM 655 O O . ASP A 1 91 ? 22.619 30.309 29.289 1.00 9.68 ? 173 ASP A O 1 ATOM 656 C CB . ASP A 1 91 ? 21.317 28.368 27.816 1.00 15.40 ? 173 ASP A CB 1 ATOM 657 C CG . ASP A 1 91 ? 21.297 27.095 26.981 1.00 15.40 ? 173 ASP A CG 1 ATOM 658 O OD1 . ASP A 1 91 ? 21.092 26.001 27.545 1.00 15.40 ? 173 ASP A OD1 1 ATOM 659 O OD2 . ASP A 1 91 ? 21.488 27.190 25.750 1.00 15.40 ? 173 ASP A OD2 1 ATOM 660 N N . ARG A 1 92 ? 22.154 29.369 31.294 1.00 9.29 ? 174 ARG A N 1 ATOM 661 C CA . ARG A 1 92 ? 22.610 30.477 32.128 1.00 9.29 ? 174 ARG A CA 1 ATOM 662 C C . ARG A 1 92 ? 24.053 30.889 31.814 1.00 9.29 ? 174 ARG A C 1 ATOM 663 O O . ARG A 1 92 ? 24.893 30.040 31.507 1.00 9.29 ? 174 ARG A O 1 ATOM 664 C CB . ARG A 1 92 ? 22.498 30.064 33.600 1.00 8.10 ? 174 ARG A CB 1 ATOM 665 C CG . ARG A 1 92 ? 22.259 31.200 34.585 1.00 8.10 ? 174 ARG A CG 1 ATOM 666 C CD . ARG A 1 92 ? 22.102 30.659 36.014 1.00 8.10 ? 174 ARG A CD 1 ATOM 667 N NE . ARG A 1 92 ? 23.357 30.113 36.523 1.00 8.10 ? 174 ARG A NE 1 ATOM 668 C CZ . ARG A 1 92 ? 23.464 29.291 37.562 1.00 8.10 ? 174 ARG A CZ 1 ATOM 669 N NH1 . ARG A 1 92 ? 22.395 28.909 38.243 1.00 8.10 ? 174 ARG A NH1 1 ATOM 670 N NH2 . ARG A 1 92 ? 24.655 28.855 37.932 1.00 8.10 ? 174 ARG A NH2 1 ATOM 671 N N . ASP A 1 93 ? 24.334 32.188 31.911 1.00 4.64 ? 175 ASP A N 1 ATOM 672 C CA . ASP A 1 93 ? 25.670 32.735 31.650 1.00 4.64 ? 175 ASP A CA 1 ATOM 673 C C . ASP A 1 93 ? 26.166 32.301 30.268 1.00 4.64 ? 175 ASP A C 1 ATOM 674 O O . ASP A 1 93 ? 27.242 31.716 30.139 1.00 4.64 ? 175 ASP A O 1 ATOM 675 C CB . ASP A 1 93 ? 26.654 32.257 32.725 1.00 12.49 ? 175 ASP A CB 1 ATOM 676 C CG . ASP A 1 93 ? 26.108 32.412 34.136 1.00 12.49 ? 175 ASP A CG 1 ATOM 677 O OD1 . ASP A 1 93 ? 26.041 33.551 34.642 1.00 12.49 ? 175 ASP A OD1 1 ATOM 678 O OD2 . ASP A 1 93 ? 25.747 31.387 34.747 1.00 12.49 ? 175 ASP A OD2 1 ATOM 679 N N . CYS A 1 94 ? 25.396 32.624 29.236 1.00 7.75 ? 176 CYS A N 1 ATOM 680 C CA . CYS A 1 94 ? 25.721 32.233 27.864 1.00 7.75 ? 176 CYS A CA 1 ATOM 681 C C . CYS A 1 94 ? 27.125 32.568 27.343 1.00 7.75 ? 176 CYS A C 1 ATOM 682 O O . CYS A 1 94 ? 27.638 31.874 26.461 1.00 7.75 ? 176 CYS A O 1 ATOM 683 C CB . CYS A 1 94 ? 24.672 32.792 26.904 1.00 7.25 ? 176 CYS A CB 1 ATOM 684 S SG . CYS A 1 94 ? 24.607 34.613 26.845 1.00 7.25 ? 176 CYS A SG 1 ATOM 685 N N . ALA A 1 95 ? 27.738 33.628 27.865 1.00 15.00 ? 177 ALA A N 1 ATOM 686 C CA . ALA A 1 95 ? 29.068 34.029 27.408 1.00 15.00 ? 177 ALA A CA 1 ATOM 687 C C . ALA A 1 95 ? 30.231 33.446 28.214 1.00 15.00 ? 177 ALA A C 1 ATOM 688 O O . ALA A 1 95 ? 31.391 33.596 27.831 1.00 15.00 ? 177 ALA A O 1 ATOM 689 C CB . ALA A 1 95 ? 29.172 35.547 27.358 1.00 8.88 ? 177 ALA A CB 1 ATOM 690 N N . ALA A 1 96 ? 29.923 32.774 29.319 1.00 21.48 ? 178 ALA A N 1 ATOM 691 C CA . ALA A 1 96 ? 30.953 32.180 30.170 1.00 21.48 ? 178 ALA A CA 1 ATOM 692 C C . ALA A 1 96 ? 31.580 30.917 29.580 1.00 21.48 ? 178 ALA A C 1 ATOM 693 O O . ALA A 1 96 ? 30.942 30.187 28.817 1.00 21.48 ? 178 ALA A O 1 ATOM 694 C CB . ALA A 1 96 ? 30.385 31.884 31.550 1.00 9.41 ? 178 ALA A CB 1 ATOM 695 N N . LEU A 1 97 ? 32.833 30.665 29.954 1.00 29.21 ? 179 LEU A N 1 ATOM 696 C CA . LEU A 1 97 ? 33.571 29.492 29.489 1.00 29.21 ? 179 LEU A CA 1 ATOM 697 C C . LEU A 1 97 ? 33.051 28.229 30.167 1.00 29.21 ? 179 LEU A C 1 ATOM 698 O O . LEU A 1 97 ? 33.193 27.126 29.644 1.00 29.21 ? 179 LEU A O 1 ATOM 699 C CB . LEU A 1 97 ? 35.065 29.656 29.777 1.00 25.08 ? 179 LEU A CB 1 ATOM 700 C CG . LEU A 1 97 ? 35.765 30.792 29.030 1.00 25.08 ? 179 LEU A CG 1 ATOM 701 C CD1 . LEU A 1 97 ? 37.190 30.950 29.533 1.00 25.08 ? 179 LEU A CD1 1 ATOM 702 C CD2 . LEU A 1 97 ? 35.745 30.509 27.534 1.00 25.08 ? 179 LEU A CD2 1 ATOM 703 N N . ALA A 1 98 ? 32.455 28.405 31.342 1.00 25.51 ? 180 ALA A N 1 ATOM 704 C CA . ALA A 1 98 ? 31.898 27.298 32.105 1.00 25.51 ? 180 ALA A CA 1 ATOM 705 C C . ALA A 1 98 ? 30.697 27.792 32.907 1.00 25.51 ? 180 ALA A C 1 ATOM 706 O O . ALA A 1 98 ? 30.785 28.786 33.628 1.00 25.51 ? 180 ALA A O 1 ATOM 707 C CB . ALA A 1 98 ? 32.949 26.727 33.031 1.00 21.90 ? 180 ALA A CB 1 ATOM 708 N N . SER A 1 99 ? 29.566 27.113 32.755 1.00 26.90 ? 181 SER A N 1 ATOM 709 C CA . SER A 1 99 ? 28.355 27.491 33.472 1.00 26.90 ? 181 SER A CA 1 ATOM 710 C C . SER A 1 99 ? 27.880 26.367 34.382 1.00 26.90 ? 181 SER A C 1 ATOM 711 O O . SER A 1 99 ? 27.925 25.196 34.016 1.00 26.90 ? 181 SER A O 1 ATOM 712 C CB . SER A 1 99 ? 27.245 27.862 32.489 1.00 42.37 ? 181 SER A CB 1 ATOM 713 O OG . SER A 1 99 ? 26.044 28.168 33.179 1.00 42.37 ? 181 SER A OG 1 ATOM 714 N N . ASN A 1 100 ? 27.420 26.737 35.569 1.00 23.77 ? 182 ASN A N 1 ATOM 715 C CA . ASN A 1 100 ? 26.924 25.765 36.533 1.00 23.77 ? 182 ASN A CA 1 ATOM 716 C C . ASN A 1 100 ? 25.401 25.652 36.481 1.00 23.77 ? 182 ASN A C 1 ATOM 717 O O . ASN A 1 100 ? 24.799 24.972 37.312 1.00 23.77 ? 182 ASN A O 1 ATOM 718 C CB . ASN A 1 100 ? 27.382 26.140 37.946 1.00 39.31 ? 182 ASN A CB 1 ATOM 719 C CG . ASN A 1 100 ? 28.887 26.038 38.119 1.00 39.31 ? 182 ASN A CG 1 ATOM 720 O OD1 . ASN A 1 100 ? 29.435 24.941 38.217 1.00 39.31 ? 182 ASN A OD1 1 ATOM 721 N ND2 . ASN A 1 100 ? 29.563 27.181 38.162 1.00 39.31 ? 182 ASN A ND2 1 ATOM 722 N N . GLY A 1 101 ? 24.789 26.301 35.490 1.00 13.26 ? 183 GLY A N 1 ATOM 723 C CA . GLY A 1 101 ? 23.339 26.274 35.343 1.00 13.26 ? 183 GLY A CA 1 ATOM 724 C C . GLY A 1 101 ? 22.794 24.877 35.129 1.00 13.26 ? 183 GLY A C 1 ATOM 725 O O . GLY A 1 101 ? 23.241 24.168 34.231 1.00 13.26 ? 183 GLY A O 1 ATOM 726 N N . GLU A 1 102 ? 21.805 24.496 35.933 1.00 14.25 ? 184 GLU A N 1 ATOM 727 C CA . GLU A 1 102 ? 21.203 23.164 35.858 1.00 14.25 ? 184 GLU A CA 1 ATOM 728 C C . GLU A 1 102 ? 20.247 22.905 34.691 1.00 14.25 ? 184 GLU A C 1 ATOM 729 O O . GLU A 1 102 ? 19.997 21.748 34.345 1.00 14.25 ? 184 GLU A O 1 ATOM 730 C CB . GLU A 1 102 ? 20.494 22.832 37.174 1.00 10.70 ? 184 GLU A CB 1 ATOM 731 C CG . GLU A 1 102 ? 19.261 23.687 37.461 1.00 10.70 ? 184 GLU A CG 1 ATOM 732 C CD . GLU A 1 102 ? 18.581 23.331 38.770 1.00 10.70 ? 184 GLU A CD 1 ATOM 733 O OE1 . GLU A 1 102 ? 18.780 22.213 39.284 1.00 10.70 ? 184 GLU A OE1 1 ATOM 734 O OE2 . GLU A 1 102 ? 17.830 24.172 39.287 1.00 10.70 ? 184 GLU A OE2 1 ATOM 735 N N . TYR A 1 103 ? 19.703 23.965 34.097 1.00 11.19 ? 185 TYR A N 1 ATOM 736 C CA . TYR A 1 103 ? 18.768 23.811 32.985 1.00 11.19 ? 185 TYR A CA 1 ATOM 737 C C . TYR A 1 103 ? 19.366 24.188 31.636 1.00 11.19 ? 185 TYR A C 1 ATOM 738 O O . TYR A 1 103 ? 20.170 25.121 31.530 1.00 11.19 ? 185 TYR A O 1 ATOM 739 C CB . TYR A 1 103 ? 17.489 24.619 33.230 1.00 8.74 ? 185 TYR A CB 1 ATOM 740 C CG . TYR A 1 103 ? 16.745 24.228 34.490 1.00 8.74 ? 185 TYR A CG 1 ATOM 741 C CD1 . TYR A 1 103 ? 16.572 22.886 34.835 1.00 8.74 ? 185 TYR A CD1 1 ATOM 742 C CD2 . TYR A 1 103 ? 16.210 25.201 35.335 1.00 8.74 ? 185 TYR A CD2 1 ATOM 743 C CE1 . TYR A 1 103 ? 15.886 22.523 35.993 1.00 8.74 ? 185 TYR A CE1 1 ATOM 744 C CE2 . TYR A 1 103 ? 15.523 24.849 36.492 1.00 8.74 ? 185 TYR A CE2 1 ATOM 745 C CZ . TYR A 1 103 ? 15.365 23.511 36.814 1.00 8.74 ? 185 TYR A CZ 1 ATOM 746 O OH . TYR A 1 103 ? 14.702 23.165 37.966 1.00 8.74 ? 185 TYR A OH 1 ATOM 747 N N . SER A 1 104 ? 18.966 23.442 30.613 1.00 11.42 ? 186 SER A N 1 ATOM 748 C CA . SER A 1 104 ? 19.426 23.650 29.248 1.00 11.42 ? 186 SER A CA 1 ATOM 749 C C . SER A 1 104 ? 18.230 23.895 28.337 1.00 11.42 ? 186 SER A C 1 ATOM 750 O O . SER A 1 104 ? 17.225 23.188 28.422 1.00 11.42 ? 186 SER A O 1 ATOM 751 C CB . SER A 1 104 ? 20.185 22.416 28.758 1.00 52.50 ? 186 SER A CB 1 ATOM 752 O OG . SER A 1 104 ? 20.483 22.522 27.377 1.00 52.50 ? 186 SER A OG 1 ATOM 753 N N . ILE A 1 105 ? 18.339 24.895 27.469 1.00 13.19 ? 187 ILE A N 1 ATOM 754 C CA . ILE A 1 105 ? 17.263 25.219 26.539 1.00 13.19 ? 187 ILE A CA 1 ATOM 755 C C . ILE A 1 105 ? 16.917 24.004 25.679 1.00 13.19 ? 187 ILE A C 1 ATOM 756 O O . ILE A 1 105 ? 15.743 23.712 25.449 1.00 13.19 ? 187 ILE A O 1 ATOM 757 C CB . ILE A 1 105 ? 17.659 26.398 25.626 1.00 14.72 ? 187 ILE A CB 1 ATOM 758 C CG1 . ILE A 1 105 ? 17.852 27.665 26.460 1.00 14.72 ? 187 ILE A CG1 1 ATOM 759 C CG2 . ILE A 1 105 ? 16.602 26.624 24.554 1.00 14.72 ? 187 ILE A CG2 1 ATOM 760 C CD1 . ILE A 1 105 ? 18.372 28.847 25.672 1.00 14.72 ? 187 ILE A CD1 1 ATOM 761 N N . ALA A 1 106 ? 17.949 23.273 25.264 1.00 23.62 ? 188 ALA A N 1 ATOM 762 C CA . ALA A 1 106 ? 17.798 22.084 24.428 1.00 23.62 ? 188 ALA A CA 1 ATOM 763 C C . ALA A 1 106 ? 17.014 20.962 25.100 1.00 23.62 ? 188 ALA A C 1 ATOM 764 O O . ALA A 1 106 ? 16.335 20.184 24.429 1.00 23.62 ? 188 ALA A O 1 ATOM 765 C CB . ALA A 1 106 ? 19.165 21.572 24.005 1.00 31.43 ? 188 ALA A CB 1 ATOM 766 N N . ASP A 1 107 ? 17.116 20.874 26.421 1.00 17.14 ? 189 ASP A N 1 ATOM 767 C CA . ASP A 1 107 ? 16.420 19.836 27.165 1.00 17.14 ? 189 ASP A CA 1 ATOM 768 C C . ASP A 1 107 ? 15.269 20.408 27.993 1.00 17.14 ? 189 ASP A C 1 ATOM 769 O O . ASP A 1 107 ? 15.257 20.298 29.219 1.00 17.14 ? 189 ASP A O 1 ATOM 770 C CB . ASP A 1 107 ? 17.419 19.082 28.051 1.00 33.23 ? 189 ASP A CB 1 ATOM 771 C CG . ASP A 1 107 ? 16.846 17.796 28.631 1.00 33.23 ? 189 ASP A CG 1 ATOM 772 O OD1 . ASP A 1 107 ? 15.836 17.275 28.104 1.00 33.23 ? 189 ASP A OD1 1 ATOM 773 O OD2 . ASP A 1 107 ? 17.423 17.298 29.622 1.00 33.23 ? 189 ASP A OD2 1 ATOM 774 N N . GLY A 1 108 ? 14.324 21.047 27.305 1.00 17.00 ? 190 GLY A N 1 ATOM 775 C CA . GLY A 1 108 ? 13.156 21.629 27.950 1.00 17.00 ? 190 GLY A CA 1 ATOM 776 C C . GLY A 1 108 ? 13.442 22.596 29.087 1.00 17.00 ? 190 GLY A C 1 ATOM 777 O O . GLY A 1 108 ? 12.720 22.620 30.084 1.00 17.00 ? 190 GLY A O 1 ATOM 778 N N . GLY A 1 109 ? 14.472 23.418 28.919 1.00 10.23 ? 191 GLY A N 1 ATOM 779 C CA . GLY A 1 109 ? 14.849 24.368 29.947 1.00 10.23 ? 191 GLY A CA 1 ATOM 780 C C . GLY A 1 109 ? 13.848 25.469 30.226 1.00 10.23 ? 191 GLY A C 1 ATOM 781 O O . GLY A 1 109 ? 13.748 25.934 31.361 1.00 10.23 ? 191 GLY A O 1 ATOM 782 N N . VAL A 1 110 ? 13.126 25.909 29.200 1.00 10.21 ? 192 VAL A N 1 ATOM 783 C CA . VAL A 1 110 ? 12.142 26.971 29.376 1.00 10.21 ? 192 VAL A CA 1 ATOM 784 C C . VAL A 1 110 ? 10.997 26.511 30.281 1.00 10.21 ? 192 VAL A C 1 ATOM 785 O O . VAL A 1 110 ? 10.612 27.219 31.212 1.00 10.21 ? 192 VAL A O 1 ATOM 786 C CB . VAL A 1 110 ? 11.621 27.480 28.006 1.00 11.13 ? 192 VAL A CB 1 ATOM 787 C CG1 . VAL A 1 110 ? 10.434 28.418 28.183 1.00 11.13 ? 192 VAL A CG1 1 ATOM 788 C CG2 . VAL A 1 110 ? 12.744 28.211 27.280 1.00 11.13 ? 192 VAL A CG2 1 ATOM 789 N N . ALA A 1 111 ? 10.498 25.301 30.036 1.00 6.85 ? 193 ALA A N 1 ATOM 790 C CA . ALA A 1 111 ? 9.410 24.736 30.829 1.00 6.85 ? 193 ALA A CA 1 ATOM 791 C C . ALA A 1 111 ? 9.883 24.488 32.255 1.00 6.85 ? 193 ALA A C 1 ATOM 792 O O . ALA A 1 111 ? 9.139 24.689 33.208 1.00 6.85 ? 193 ALA A O 1 ATOM 793 C CB . ALA A 1 111 ? 8.913 23.434 30.203 1.00 8.76 ? 193 ALA A CB 1 ATOM 794 N N . LYS A 1 112 ? 11.128 24.045 32.394 1.00 5.28 ? 194 LYS A N 1 ATOM 795 C CA . LYS A 1 112 ? 11.704 23.793 33.711 1.00 5.28 ? 194 LYS A CA 1 ATOM 796 C C . LYS A 1 112 ? 11.851 25.101 34.481 1.00 5.28 ? 194 LYS A C 1 ATOM 797 O O . LYS A 1 112 ? 11.589 25.148 35.674 1.00 5.28 ? 194 LYS A O 1 ATOM 798 C CB . LYS A 1 112 ? 13.062 23.088 33.584 1.00 34.59 ? 194 LYS A CB 1 ATOM 799 C CG . LYS A 1 112 ? 12.974 21.618 33.165 1.00 34.59 ? 194 LYS A CG 1 ATOM 800 C CD . LYS A 1 112 ? 13.136 20.649 34.342 1.00 34.59 ? 194 LYS A CD 1 ATOM 801 C CE . LYS A 1 112 ? 12.255 21.025 35.537 1.00 34.59 ? 194 LYS A CE 1 ATOM 802 N NZ . LYS A 1 112 ? 12.127 19.950 36.565 1.00 34.59 ? 194 LYS A NZ 1 ATOM 803 N N . TYR A 1 113 ? 12.234 26.170 33.784 1.00 4.91 ? 195 TYR A N 1 ATOM 804 C CA . TYR A 1 113 ? 12.399 27.471 34.421 1.00 4.91 ? 195 TYR A CA 1 ATOM 805 C C . TYR A 1 113 ? 11.062 28.026 34.913 1.00 4.91 ? 195 TYR A C 1 ATOM 806 O O . TYR A 1 113 ? 11.001 28.657 35.965 1.00 4.91 ? 195 TYR A O 1 ATOM 807 C CB . TYR A 1 113 ? 13.055 28.473 33.468 1.00 7.31 ? 195 TYR A CB 1 ATOM 808 C CG . TYR A 1 113 ? 13.339 29.809 34.128 1.00 7.31 ? 195 TYR A CG 1 ATOM 809 C CD1 . TYR A 1 113 ? 14.434 29.965 34.975 1.00 7.31 ? 195 TYR A CD1 1 ATOM 810 C CD2 . TYR A 1 113 ? 12.500 30.908 33.928 1.00 7.31 ? 195 TYR A CD2 1 ATOM 811 C CE1 . TYR A 1 113 ? 14.690 31.180 35.611 1.00 7.31 ? 195 TYR A CE1 1 ATOM 812 C CE2 . TYR A 1 113 ? 12.748 32.129 34.559 1.00 7.31 ? 195 TYR A CE2 1 ATOM 813 C CZ . TYR A 1 113 ? 13.848 32.258 35.398 1.00 7.31 ? 195 TYR A CZ 1 ATOM 814 O OH . TYR A 1 113 ? 14.105 33.463 36.020 1.00 7.31 ? 195 TYR A OH 1 ATOM 815 N N . LYS A 1 114 ? 10.000 27.819 34.137 1.00 5.31 ? 196 LYS A N 1 ATOM 816 C CA . LYS A 1 114 ? 8.680 28.298 34.532 1.00 5.31 ? 196 LYS A CA 1 ATOM 817 C C . LYS A 1 114 ? 8.201 27.583 35.792 1.00 5.31 ? 196 LYS A C 1 ATOM 818 O O . LYS A 1 114 ? 7.542 28.188 36.637 1.00 5.31 ? 196 LYS A O 1 ATOM 819 C CB . LYS A 1 114 ? 7.679 28.136 33.389 1.00 17.39 ? 196 LYS A CB 1 ATOM 820 C CG . LYS A 1 114 ? 8.003 29.029 32.208 1.00 17.39 ? 196 LYS A CG 1 ATOM 821 C CD . LYS A 1 114 ? 6.929 28.978 31.143 1.00 17.39 ? 196 LYS A CD 1 ATOM 822 C CE . LYS A 1 114 ? 7.255 29.937 30.007 1.00 17.39 ? 196 LYS A CE 1 ATOM 823 N NZ . LYS A 1 114 ? 6.173 29.958 28.982 1.00 17.39 ? 196 LYS A NZ 1 ATOM 824 N N . ASN A 1 115 ? 8.560 26.308 35.929 1.00 6.21 ? 197 ASN A N 1 ATOM 825 C CA . ASN A 1 115 ? 8.186 25.528 37.110 1.00 6.21 ? 197 ASN A CA 1 ATOM 826 C C . ASN A 1 115 ? 8.928 26.094 38.319 1.00 6.21 ? 197 ASN A C 1 ATOM 827 O O . ASN A 1 115 ? 8.389 26.162 39.420 1.00 6.21 ? 197 ASN A O 1 ATOM 828 C CB . ASN A 1 115 ? 8.562 24.062 36.924 1.00 6.39 ? 197 ASN A CB 1 ATOM 829 C CG . ASN A 1 115 ? 8.248 23.233 38.144 1.00 6.39 ? 197 ASN A CG 1 ATOM 830 O OD1 . ASN A 1 115 ? 7.084 23.083 38.519 1.00 6.39 ? 197 ASN A OD1 1 ATOM 831 N ND2 . ASN A 1 115 ? 9.282 22.712 38.791 1.00 6.39 ? 197 ASN A ND2 1 ATOM 832 N N . TYR A 1 116 ? 10.186 26.463 38.096 1.00 5.70 ? 198 TYR A N 1 ATOM 833 C CA . TYR A 1 116 ? 11.039 27.053 39.119 1.00 5.70 ? 198 TYR A CA 1 ATOM 834 C C . TYR A 1 116 ? 10.405 28.369 39.598 1.00 5.70 ? 198 TYR A C 1 ATOM 835 O O . TYR A 1 116 ? 10.316 28.615 40.800 1.00 5.70 ? 198 TYR A O 1 ATOM 836 C CB . TYR A 1 116 ? 12.445 27.255 38.521 1.00 5.97 ? 198 TYR A CB 1 ATOM 837 C CG . TYR A 1 116 ? 13.363 28.235 39.220 1.00 5.97 ? 198 TYR A CG 1 ATOM 838 C CD1 . TYR A 1 116 ? 14.135 27.850 40.316 1.00 5.97 ? 198 TYR A CD1 1 ATOM 839 C CD2 . TYR A 1 116 ? 13.509 29.532 38.738 1.00 5.97 ? 198 TYR A CD2 1 ATOM 840 C CE1 . TYR A 1 116 ? 15.036 28.738 40.911 1.00 5.97 ? 198 TYR A CE1 1 ATOM 841 C CE2 . TYR A 1 116 ? 14.402 30.426 39.321 1.00 5.97 ? 198 TYR A CE2 1 ATOM 842 C CZ . TYR A 1 116 ? 15.161 30.024 40.403 1.00 5.97 ? 198 TYR A CZ 1 ATOM 843 O OH . TYR A 1 116 ? 16.039 30.920 40.968 1.00 5.97 ? 198 TYR A OH 1 ATOM 844 N N . ILE A 1 117 ? 9.907 29.177 38.663 1.00 6.48 ? 199 ILE A N 1 ATOM 845 C CA . ILE A 1 117 ? 9.264 30.453 39.002 1.00 6.48 ? 199 ILE A CA 1 ATOM 846 C C . ILE A 1 117 ? 7.920 30.215 39.699 1.00 6.48 ? 199 ILE A C 1 ATOM 847 O O . ILE A 1 117 ? 7.553 30.953 40.614 1.00 6.48 ? 199 ILE A O 1 ATOM 848 C CB . ILE A 1 117 ? 9.055 31.342 37.741 1.00 4.80 ? 199 ILE A CB 1 ATOM 849 C CG1 . ILE A 1 117 ? 10.410 31.789 37.176 1.00 4.80 ? 199 ILE A CG1 1 ATOM 850 C CG2 . ILE A 1 117 ? 8.226 32.575 38.075 1.00 4.80 ? 199 ILE A CG2 1 ATOM 851 C CD1 . ILE A 1 117 ? 11.213 32.706 38.101 1.00 4.80 ? 199 ILE A CD1 1 ATOM 852 N N . ASP A 1 118 ? 7.205 29.172 39.280 1.00 2.00 ? 200 ASP A N 1 ATOM 853 C CA . ASP A 1 118 ? 5.918 28.823 39.881 1.00 2.00 ? 200 ASP A CA 1 ATOM 854 C C . ASP A 1 118 ? 6.128 28.451 41.338 1.00 2.00 ? 200 ASP A C 1 ATOM 855 O O . ASP A 1 118 ? 5.306 28.771 42.200 1.00 2.00 ? 200 ASP A O 1 ATOM 856 C CB . ASP A 1 118 ? 5.284 27.625 39.161 1.00 10.64 ? 200 ASP A CB 1 ATOM 857 C CG . ASP A 1 118 ? 4.778 27.967 37.768 1.00 10.64 ? 200 ASP A CG 1 ATOM 858 O OD1 . ASP A 1 118 ? 4.648 29.165 37.452 1.00 10.64 ? 200 ASP A OD1 1 ATOM 859 O OD2 . ASP A 1 118 ? 4.505 27.027 36.992 1.00 10.64 ? 200 ASP A OD2 1 ATOM 860 N N . THR A 1 119 ? 7.232 27.754 41.592 1.00 7.81 ? 201 THR A N 1 ATOM 861 C CA . THR A 1 119 ? 7.587 27.313 42.933 1.00 7.81 ? 201 THR A CA 1 ATOM 862 C C . THR A 1 119 ? 7.881 28.510 43.833 1.00 7.81 ? 201 THR A C 1 ATOM 863 O O . THR A 1 119 ? 7.403 28.565 44.967 1.00 7.81 ? 201 THR A O 1 ATOM 864 C CB . THR A 1 119 ? 8.799 26.358 42.899 1.00 5.63 ? 201 THR A CB 1 ATOM 865 O OG1 . THR A 1 119 ? 8.492 25.226 42.068 1.00 5.63 ? 201 THR A OG1 1 ATOM 866 C CG2 . THR A 1 119 ? 9.140 25.880 44.294 1.00 5.63 ? 201 THR A CG2 1 ATOM 867 N N . ILE A 1 120 ? 8.647 29.472 43.319 1.00 9.79 ? 202 ILE A N 1 ATOM 868 C CA . ILE A 1 120 ? 8.981 30.678 44.078 1.00 9.79 ? 202 ILE A CA 1 ATOM 869 C C . ILE A 1 120 ? 7.726 31.516 44.342 1.00 9.79 ? 202 ILE A C 1 ATOM 870 O O . ILE A 1 120 ? 7.556 32.056 45.436 1.00 9.79 ? 202 ILE A O 1 ATOM 871 C CB . ILE A 1 120 ? 10.035 31.553 43.342 1.00 5.79 ? 202 ILE A CB 1 ATOM 872 C CG1 . ILE A 1 120 ? 11.373 30.814 43.267 1.00 5.79 ? 202 ILE A CG1 1 ATOM 873 C CG2 . ILE A 1 120 ? 10.233 32.885 44.064 1.00 5.79 ? 202 ILE A CG2 1 ATOM 874 C CD1 . ILE A 1 120 ? 12.458 31.580 42.525 1.00 5.79 ? 202 ILE A CD1 1 ATOM 875 N N . ARG A 1 121 ? 6.840 31.607 43.353 1.00 5.37 ? 203 ARG A N 1 ATOM 876 C CA . ARG A 1 121 ? 5.613 32.385 43.516 1.00 5.37 ? 203 ARG A CA 1 ATOM 877 C C . ARG A 1 121 ? 4.761 31.884 44.680 1.00 5.37 ? 203 ARG A C 1 ATOM 878 O O . ARG A 1 121 ? 4.275 32.683 45.481 1.00 5.37 ? 203 ARG A O 1 ATOM 879 C CB . ARG A 1 121 ? 4.781 32.392 42.229 1.00 14.42 ? 203 ARG A CB 1 ATOM 880 C CG . ARG A 1 121 ? 3.444 33.116 42.384 1.00 14.42 ? 203 ARG A CG 1 ATOM 881 C CD . ARG A 1 121 ? 2.626 33.099 41.104 1.00 14.42 ? 203 ARG A CD 1 ATOM 882 N NE . ARG A 1 121 ? 1.231 33.469 41.344 1.00 14.42 ? 203 ARG A NE 1 ATOM 883 C CZ . ARG A 1 121 ? 0.730 34.694 41.197 1.00 14.42 ? 203 ARG A CZ 1 ATOM 884 N NH1 . ARG A 1 121 ? 1.500 35.695 40.795 1.00 14.42 ? 203 ARG A NH1 1 ATOM 885 N NH2 . ARG A 1 121 ? -0.557 34.916 41.444 1.00 14.42 ? 203 ARG A NH2 1 ATOM 886 N N . GLN A 1 122 ? 4.593 30.564 44.776 1.00 11.15 ? 204 GLN A N 1 ATOM 887 C CA . GLN A 1 122 ? 3.799 29.961 45.849 1.00 11.15 ? 204 GLN A CA 1 ATOM 888 C C . GLN A 1 122 ? 4.335 30.314 47.227 1.00 11.15 ? 204 GLN A C 1 ATOM 889 O O . GLN A 1 122 ? 3.567 30.563 48.154 1.00 11.15 ? 204 GLN A O 1 ATOM 890 C CB . GLN A 1 122 ? 3.725 28.441 45.695 1.00 57.78 ? 204 GLN A CB 1 ATOM 891 C CG . GLN A 1 122 ? 2.567 27.970 44.837 1.00 57.78 ? 204 GLN A CG 1 ATOM 892 C CD . GLN A 1 122 ? 2.519 26.460 44.692 1.00 57.78 ? 204 GLN A CD 1 ATOM 893 O OE1 . GLN A 1 122 ? 2.917 25.715 45.597 1.00 57.78 ? 204 GLN A OE1 1 ATOM 894 N NE2 . GLN A 1 122 ? 2.019 25.998 43.551 1.00 57.78 ? 204 GLN A NE2 1 ATOM 895 N N . ILE A 1 123 ? 5.656 30.340 47.352 1.00 5.85 ? 205 ILE A N 1 ATOM 896 C CA . ILE A 1 123 ? 6.303 30.683 48.610 1.00 5.85 ? 205 ILE A CA 1 ATOM 897 C C . ILE A 1 123 ? 6.006 32.146 48.960 1.00 5.85 ? 205 ILE A C 1 ATOM 898 O O . ILE A 1 123 ? 5.601 32.459 50.080 1.00 5.85 ? 205 ILE A O 1 ATOM 899 C CB . ILE A 1 123 ? 7.830 30.437 48.512 1.00 5.46 ? 205 ILE A CB 1 ATOM 900 C CG1 . ILE A 1 123 ? 8.090 28.941 48.286 1.00 5.46 ? 205 ILE A CG1 1 ATOM 901 C CG2 . ILE A 1 123 ? 8.534 30.908 49.777 1.00 5.46 ? 205 ILE A CG2 1 ATOM 902 C CD1 . ILE A 1 123 ? 9.535 28.578 48.025 1.00 5.46 ? 205 ILE A CD1 1 ATOM 903 N N . VAL A 1 124 ? 6.157 33.030 47.977 1.00 9.21 ? 206 VAL A N 1 ATOM 904 C CA . VAL A 1 124 ? 5.907 34.453 48.178 1.00 9.21 ? 206 VAL A CA 1 ATOM 905 C C . VAL A 1 124 ? 4.437 34.730 48.505 1.00 9.21 ? 206 VAL A C 1 ATOM 906 O O . VAL A 1 124 ? 4.132 35.613 49.307 1.00 9.21 ? 206 VAL A O 1 ATOM 907 C CB . VAL A 1 124 ? 6.355 35.269 46.945 1.00 11.77 ? 206 VAL A CB 1 ATOM 908 C CG1 . VAL A 1 124 ? 6.050 36.744 47.138 1.00 11.77 ? 206 VAL A CG1 1 ATOM 909 C CG2 . VAL A 1 124 ? 7.847 35.074 46.715 1.00 11.77 ? 206 VAL A CG2 1 ATOM 910 N N . VAL A 1 125 ? 3.529 33.975 47.891 1.00 14.61 ? 207 VAL A N 1 ATOM 911 C CA . VAL A 1 125 ? 2.104 34.141 48.153 1.00 14.61 ? 207 VAL A CA 1 ATOM 912 C C . VAL A 1 125 ? 1.819 33.619 49.563 1.00 14.61 ? 207 VAL A C 1 ATOM 913 O O . VAL A 1 125 ? 0.993 34.175 50.287 1.00 14.61 ? 207 VAL A O 1 ATOM 914 C CB . VAL A 1 125 ? 1.240 33.389 47.104 1.00 9.62 ? 207 VAL A CB 1 ATOM 915 C CG1 . VAL A 1 125 ? -0.235 33.381 47.513 1.00 9.62 ? 207 VAL A CG1 1 ATOM 916 C CG2 . VAL A 1 125 ? 1.389 34.050 45.746 1.00 9.62 ? 207 VAL A CG2 1 ATOM 917 N N . GLU A 1 126 ? 2.544 32.579 49.964 1.00 13.65 ? 208 GLU A N 1 ATOM 918 C CA . GLU A 1 126 ? 2.376 32.001 51.293 1.00 13.65 ? 208 GLU A CA 1 ATOM 919 C C . GLU A 1 126 ? 2.836 32.998 52.359 1.00 13.65 ? 208 GLU A C 1 ATOM 920 O O . GLU A 1 126 ? 2.230 33.106 53.423 1.00 13.65 ? 208 GLU A O 1 ATOM 921 C CB . GLU A 1 126 ? 3.168 30.700 51.413 1.00 78.65 ? 208 GLU A CB 1 ATOM 922 C CG . GLU A 1 126 ? 2.892 29.919 52.684 1.00 78.65 ? 208 GLU A CG 1 ATOM 923 C CD . GLU A 1 126 ? 3.628 28.595 52.722 1.00 78.65 ? 208 GLU A CD 1 ATOM 924 O OE1 . GLU A 1 126 ? 3.467 27.790 51.778 1.00 78.65 ? 208 GLU A OE1 1 ATOM 925 O OE2 . GLU A 1 126 ? 4.369 28.358 53.700 1.00 78.65 ? 208 GLU A OE2 1 ATOM 926 N N . TYR A 1 127 ? 3.899 33.740 52.055 1.00 7.75 ? 209 TYR A N 1 ATOM 927 C CA . TYR A 1 127 ? 4.436 34.724 52.985 1.00 7.75 ? 209 TYR A CA 1 ATOM 928 C C . TYR A 1 127 ? 4.145 36.145 52.526 1.00 7.75 ? 209 TYR A C 1 ATOM 929 O O . TYR A 1 127 ? 5.039 36.993 52.462 1.00 7.75 ? 209 TYR A O 1 ATOM 930 C CB . TYR A 1 127 ? 5.937 34.501 53.186 1.00 11.39 ? 209 TYR A CB 1 ATOM 931 C CG . TYR A 1 127 ? 6.240 33.254 53.985 1.00 11.39 ? 209 TYR A CG 1 ATOM 932 C CD1 . TYR A 1 127 ? 6.341 32.008 53.367 1.00 11.39 ? 209 TYR A CD1 1 ATOM 933 C CD2 . TYR A 1 127 ? 6.373 33.313 55.368 1.00 11.39 ? 209 TYR A CD2 1 ATOM 934 C CE1 . TYR A 1 127 ? 6.560 30.848 54.111 1.00 11.39 ? 209 TYR A CE1 1 ATOM 935 C CE2 . TYR A 1 127 ? 6.591 32.165 56.122 1.00 11.39 ? 209 TYR A CE2 1 ATOM 936 C CZ . TYR A 1 127 ? 6.683 30.938 55.492 1.00 11.39 ? 209 TYR A CZ 1 ATOM 937 O OH . TYR A 1 127 ? 6.877 29.802 56.253 1.00 11.39 ? 209 TYR A OH 1 ATOM 938 N N . SER A 1 128 ? 2.877 36.397 52.219 1.00 10.94 ? 210 SER A N 1 ATOM 939 C CA . SER A 1 128 ? 2.426 37.706 51.760 1.00 10.94 ? 210 SER A CA 1 ATOM 940 C C . SER A 1 128 ? 2.652 38.775 52.817 1.00 10.94 ? 210 SER A C 1 ATOM 941 O O . SER A 1 128 ? 2.687 39.969 52.516 1.00 10.94 ? 210 SER A O 1 ATOM 942 C CB . SER A 1 128 ? 0.940 37.650 51.414 1.00 28.55 ? 210 SER A CB 1 ATOM 943 O OG . SER A 1 128 ? 0.698 36.691 50.405 1.00 28.55 ? 210 SER A OG 1 ATOM 944 N N . ASP A 1 129 ? 2.793 38.335 54.060 1.00 10.45 ? 211 ASP A N 1 ATOM 945 C CA . ASP A 1 129 ? 3.005 39.232 55.187 1.00 10.45 ? 211 ASP A CA 1 ATOM 946 C C . ASP A 1 129 ? 4.432 39.777 55.295 1.00 10.45 ? 211 ASP A C 1 ATOM 947 O O . ASP A 1 129 ? 4.705 40.660 56.111 1.00 10.45 ? 211 ASP A O 1 ATOM 948 C CB . ASP A 1 129 ? 2.605 38.528 56.490 1.00 14.02 ? 211 ASP A CB 1 ATOM 949 C CG . ASP A 1 129 ? 3.338 37.204 56.705 1.00 14.02 ? 211 ASP A CG 1 ATOM 950 O OD1 . ASP A 1 129 ? 3.376 36.358 55.789 1.00 14.02 ? 211 ASP A OD1 1 ATOM 951 O OD2 . ASP A 1 129 ? 3.863 37.003 57.814 1.00 14.02 ? 211 ASP A OD2 1 ATOM 952 N N . ILE A 1 130 ? 5.333 39.275 54.455 1.00 8.75 ? 212 ILE A N 1 ATOM 953 C CA . ILE A 1 130 ? 6.726 39.710 54.489 1.00 8.75 ? 212 ILE A CA 1 ATOM 954 C C . ILE A 1 130 ? 7.153 40.393 53.201 1.00 8.75 ? 212 ILE A C 1 ATOM 955 O O . ILE A 1 130 ? 6.961 39.854 52.110 1.00 8.75 ? 212 ILE A O 1 ATOM 956 C CB . ILE A 1 130 ? 7.677 38.514 54.749 1.00 9.44 ? 212 ILE A CB 1 ATOM 957 C CG1 . ILE A 1 130 ? 7.272 37.801 56.042 1.00 9.44 ? 212 ILE A CG1 1 ATOM 958 C CG2 . ILE A 1 130 ? 9.125 38.992 54.849 1.00 9.44 ? 212 ILE A CG2 1 ATOM 959 C CD1 . ILE A 1 130 ? 7.988 36.504 56.261 1.00 9.44 ? 212 ILE A CD1 1 ATOM 960 N N . ARG A 1 131 ? 7.732 41.581 53.339 1.00 8.98 ? 213 ARG A N 1 ATOM 961 C CA . ARG A 1 131 ? 8.223 42.337 52.192 1.00 8.98 ? 213 ARG A CA 1 ATOM 962 C C . ARG A 1 131 ? 9.434 41.577 51.651 1.00 8.98 ? 213 ARG A C 1 ATOM 963 O O . ARG A 1 131 ? 10.371 41.267 52.392 1.00 8.98 ? 213 ARG A O 1 ATOM 964 C CB . ARG A 1 131 ? 8.630 43.749 52.611 1.00 15.14 ? 213 ARG A CB 1 ATOM 965 C CG . ARG A 1 131 ? 8.759 44.711 51.449 1.00 15.14 ? 213 ARG A CG 1 ATOM 966 C CD . ARG A 1 131 ? 7.938 45.953 51.705 1.00 15.14 ? 213 ARG A CD 1 ATOM 967 N NE . ARG A 1 131 ? 8.770 47.081 52.093 1.00 15.14 ? 213 ARG A NE 1 ATOM 968 C CZ . ARG A 1 131 ? 8.392 48.047 52.923 1.00 15.14 ? 213 ARG A CZ 1 ATOM 969 N NH1 . ARG A 1 131 ? 7.194 48.026 53.488 1.00 15.14 ? 213 ARG A NH1 1 ATOM 970 N NH2 . ARG A 1 131 ? 9.229 49.031 53.200 1.00 15.14 ? 213 ARG A NH2 1 ATOM 971 N N . THR A 1 132 ? 9.398 41.260 50.362 1.00 8.27 ? 214 THR A N 1 ATOM 972 C CA . THR A 1 132 ? 10.473 40.506 49.738 1.00 8.27 ? 214 THR A CA 1 ATOM 973 C C . THR A 1 132 ? 11.135 41.264 48.600 1.00 8.27 ? 214 THR A C 1 ATOM 974 O O . THR A 1 132 ? 10.497 41.604 47.601 1.00 8.27 ? 214 THR A O 1 ATOM 975 C CB . THR A 1 132 ? 9.950 39.156 49.235 1.00 14.63 ? 214 THR A CB 1 ATOM 976 O OG1 . THR A 1 132 ? 9.363 38.450 50.333 1.00 14.63 ? 214 THR A OG1 1 ATOM 977 C CG2 . THR A 1 132 ? 11.078 38.319 48.656 1.00 14.63 ? 214 THR A CG2 1 ATOM 978 N N . LEU A 1 133 ? 12.427 41.517 48.774 1.00 9.19 ? 215 LEU A N 1 ATOM 979 C CA . LEU A 1 133 ? 13.240 42.241 47.802 1.00 9.19 ? 215 LEU A CA 1 ATOM 980 C C . LEU A 1 133 ? 13.976 41.228 46.921 1.00 9.19 ? 215 LEU A C 1 ATOM 981 O O . LEU A 1 133 ? 14.694 40.358 47.427 1.00 9.19 ? 215 LEU A O 1 ATOM 982 C CB . LEU A 1 133 ? 14.220 43.149 48.546 1.00 14.36 ? 215 LEU A CB 1 ATOM 983 C CG . LEU A 1 133 ? 13.531 43.966 49.647 1.00 14.36 ? 215 LEU A CG 1 ATOM 984 C CD1 . LEU A 1 133 ? 14.540 44.572 50.588 1.00 14.36 ? 215 LEU A CD1 1 ATOM 985 C CD2 . LEU A 1 133 ? 12.652 45.038 49.040 1.00 14.36 ? 215 LEU A CD2 1 ATOM 986 N N . LEU A 1 134 ? 13.811 41.356 45.605 1.00 5.88 ? 216 LEU A N 1 ATOM 987 C CA . LEU A 1 134 ? 14.416 40.424 44.660 1.00 5.88 ? 216 LEU A CA 1 ATOM 988 C C . LEU A 1 134 ? 15.277 41.047 43.568 1.00 5.88 ? 216 LEU A C 1 ATOM 989 O O . LEU A 1 134 ? 14.945 42.095 43.022 1.00 5.88 ? 216 LEU A O 1 ATOM 990 C CB . LEU A 1 134 ? 13.322 39.598 43.966 1.00 4.68 ? 216 LEU A CB 1 ATOM 991 C CG . LEU A 1 134 ? 12.329 38.749 44.766 1.00 4.68 ? 216 LEU A CG 1 ATOM 992 C CD1 . LEU A 1 134 ? 11.260 38.197 43.823 1.00 4.68 ? 216 LEU A CD1 1 ATOM 993 C CD2 . LEU A 1 134 ? 13.035 37.621 45.498 1.00 4.68 ? 216 LEU A CD2 1 ATOM 994 N N . VAL A 1 135 ? 16.396 40.392 43.274 1.00 3.73 ? 217 VAL A N 1 ATOM 995 C CA . VAL A 1 135 ? 17.281 40.809 42.196 1.00 3.73 ? 217 VAL A CA 1 ATOM 996 C C . VAL A 1 135 ? 17.009 39.750 41.137 1.00 3.73 ? 217 VAL A C 1 ATOM 997 O O . VAL A 1 135 ? 17.110 38.549 41.405 1.00 3.73 ? 217 VAL A O 1 ATOM 998 C CB . VAL A 1 135 ? 18.776 40.784 42.588 1.00 4.15 ? 217 VAL A CB 1 ATOM 999 C CG1 . VAL A 1 135 ? 19.651 40.979 41.340 1.00 4.15 ? 217 VAL A CG1 1 ATOM 1000 C CG2 . VAL A 1 135 ? 19.070 41.884 43.593 1.00 4.15 ? 217 VAL A CG2 1 ATOM 1001 N N . ILE A 1 136 ? 16.618 40.193 39.950 1.00 2.00 ? 218 ILE A N 1 ATOM 1002 C CA . ILE A 1 136 ? 16.285 39.268 38.878 1.00 2.00 ? 218 ILE A CA 1 ATOM 1003 C C . ILE A 1 136 ? 17.384 38.951 37.869 1.00 2.00 ? 218 ILE A C 1 ATOM 1004 O O . ILE A 1 136 ? 17.899 39.832 37.182 1.00 2.00 ? 218 ILE A O 1 ATOM 1005 C CB . ILE A 1 136 ? 15.028 39.742 38.106 1.00 4.84 ? 218 ILE A CB 1 ATOM 1006 C CG1 . ILE A 1 136 ? 13.870 40.011 39.079 1.00 4.84 ? 218 ILE A CG1 1 ATOM 1007 C CG2 . ILE A 1 136 ? 14.634 38.704 37.059 1.00 4.84 ? 218 ILE A CG2 1 ATOM 1008 C CD1 . ILE A 1 136 ? 13.425 38.799 39.876 1.00 4.84 ? 218 ILE A CD1 1 ATOM 1009 N N . GLU A 1 137 ? 17.750 37.676 37.841 1.00 5.14 ? 219 GLU A N 1 ATOM 1010 C CA . GLU A 1 137 ? 18.723 37.106 36.914 1.00 5.14 ? 219 GLU A CA 1 ATOM 1011 C C . GLU A 1 137 ? 20.005 37.846 36.523 1.00 5.14 ? 219 GLU A C 1 ATOM 1012 O O . GLU A 1 137 ? 20.088 38.431 35.440 1.00 5.14 ? 219 GLU A O 1 ATOM 1013 C CB . GLU A 1 137 ? 17.988 36.666 35.638 1.00 7.00 ? 219 GLU A CB 1 ATOM 1014 C CG . GLU A 1 137 ? 16.917 35.601 35.868 1.00 7.00 ? 219 GLU A CG 1 ATOM 1015 C CD . GLU A 1 137 ? 17.485 34.244 36.256 1.00 7.00 ? 219 GLU A CD 1 ATOM 1016 O OE1 . GLU A 1 137 ? 18.702 34.026 36.074 1.00 7.00 ? 219 GLU A OE1 1 ATOM 1017 O OE2 . GLU A 1 137 ? 16.714 33.386 36.739 1.00 7.00 ? 219 GLU A OE2 1 ATOM 1018 N N . PRO A 1 138 ? 21.028 37.826 37.397 1.00 9.76 ? 220 PRO A N 1 ATOM 1019 C CA . PRO A 1 138 ? 22.289 38.500 37.080 1.00 9.76 ? 220 PRO A CA 1 ATOM 1020 C C . PRO A 1 138 ? 22.922 37.844 35.852 1.00 9.76 ? 220 PRO A C 1 ATOM 1021 O O . PRO A 1 138 ? 22.673 36.667 35.571 1.00 9.76 ? 220 PRO A O 1 ATOM 1022 C CB . PRO A 1 138 ? 23.143 38.227 38.322 1.00 2.00 ? 220 PRO A CB 1 ATOM 1023 C CG . PRO A 1 138 ? 22.146 38.148 39.418 1.00 2.00 ? 220 PRO A CG 1 ATOM 1024 C CD . PRO A 1 138 ? 21.010 37.368 38.798 1.00 2.00 ? 220 PRO A CD 1 ATOM 1025 N N . ASP A 1 139 ? 23.721 38.613 35.117 1.00 8.20 ? 221 ASP A N 1 ATOM 1026 C CA . ASP A 1 139 ? 24.416 38.108 33.934 1.00 8.20 ? 221 ASP A CA 1 ATOM 1027 C C . ASP A 1 139 ? 23.492 37.481 32.886 1.00 8.20 ? 221 ASP A C 1 ATOM 1028 O O . ASP A 1 139 ? 23.790 36.421 32.326 1.00 8.20 ? 221 ASP A O 1 ATOM 1029 C CB . ASP A 1 139 ? 25.506 37.108 34.356 1.00 12.07 ? 221 ASP A CB 1 ATOM 1030 C CG . ASP A 1 139 ? 26.456 36.748 33.217 1.00 12.07 ? 221 ASP A CG 1 ATOM 1031 O OD1 . ASP A 1 139 ? 26.807 37.637 32.414 1.00 12.07 ? 221 ASP A OD1 1 ATOM 1032 O OD2 . ASP A 1 139 ? 26.858 35.574 33.129 1.00 12.07 ? 221 ASP A OD2 1 ATOM 1033 N N . SER A 1 140 ? 22.363 38.128 32.628 1.00 9.54 ? 222 SER A N 1 ATOM 1034 C CA . SER A 1 140 ? 21.439 37.619 31.625 1.00 9.54 ? 222 SER A CA 1 ATOM 1035 C C . SER A 1 140 ? 21.271 38.614 30.484 1.00 9.54 ? 222 SER A C 1 ATOM 1036 O O . SER A 1 140 ? 21.968 38.516 29.477 1.00 9.54 ? 222 SER A O 1 ATOM 1037 C CB . SER A 1 140 ? 20.084 37.251 32.241 1.00 3.81 ? 222 SER A CB 1 ATOM 1038 O OG . SER A 1 140 ? 19.479 38.351 32.892 1.00 3.81 ? 222 SER A OG 1 ATOM 1039 N N . LEU A 1 141 ? 20.422 39.620 30.682 1.00 8.04 ? 223 LEU A N 1 ATOM 1040 C CA . LEU A 1 141 ? 20.146 40.622 29.655 1.00 8.04 ? 223 LEU A CA 1 ATOM 1041 C C . LEU A 1 141 ? 21.345 41.445 29.194 1.00 8.04 ? 223 LEU A C 1 ATOM 1042 O O . LEU A 1 141 ? 21.362 41.919 28.060 1.00 8.04 ? 223 LEU A O 1 ATOM 1043 C CB . LEU A 1 141 ? 19.024 41.559 30.109 1.00 9.40 ? 223 LEU A CB 1 ATOM 1044 C CG . LEU A 1 141 ? 17.666 40.933 30.438 1.00 9.40 ? 223 LEU A CG 1 ATOM 1045 C CD1 . LEU A 1 141 ? 16.709 42.019 30.896 1.00 9.40 ? 223 LEU A CD1 1 ATOM 1046 C CD2 . LEU A 1 141 ? 17.113 40.199 29.230 1.00 9.40 ? 223 LEU A CD2 1 ATOM 1047 N N . ALA A 1 142 ? 22.343 41.624 30.058 1.00 7.77 ? 224 ALA A N 1 ATOM 1048 C CA . ALA A 1 142 ? 23.525 42.397 29.673 1.00 7.77 ? 224 ALA A CA 1 ATOM 1049 C C . ALA A 1 142 ? 24.265 41.735 28.504 1.00 7.77 ? 224 ALA A C 1 ATOM 1050 O O . ALA A 1 142 ? 24.841 42.422 27.654 1.00 7.77 ? 224 ALA A O 1 ATOM 1051 C CB . ALA A 1 142 ? 24.455 42.586 30.866 1.00 2.00 ? 224 ALA A CB 1 ATOM 1052 N N . ASN A 1 143 ? 24.216 40.403 28.449 1.00 8.87 ? 225 ASN A N 1 ATOM 1053 C CA . ASN A 1 143 ? 24.865 39.641 27.378 1.00 8.87 ? 225 ASN A CA 1 ATOM 1054 C C . ASN A 1 143 ? 24.184 39.859 26.033 1.00 8.87 ? 225 ASN A C 1 ATOM 1055 O O . ASN A 1 143 ? 24.792 39.655 24.985 1.00 8.87 ? 225 ASN A O 1 ATOM 1056 C CB . ASN A 1 143 ? 24.860 38.147 27.691 1.00 13.34 ? 225 ASN A CB 1 ATOM 1057 C CG . ASN A 1 143 ? 25.724 37.800 28.871 1.00 13.34 ? 225 ASN A CG 1 ATOM 1058 O OD1 . ASN A 1 143 ? 26.954 37.864 28.798 1.00 13.34 ? 225 ASN A OD1 1 ATOM 1059 N ND2 . ASN A 1 143 ? 25.088 37.413 29.971 1.00 13.34 ? 225 ASN A ND2 1 ATOM 1060 N N . LEU A 1 144 ? 22.911 40.242 26.073 1.00 10.78 ? 226 LEU A N 1 ATOM 1061 C CA . LEU A 1 144 ? 22.146 40.491 24.862 1.00 10.78 ? 226 LEU A CA 1 ATOM 1062 C C . LEU A 1 144 ? 22.486 41.849 24.275 1.00 10.78 ? 226 LEU A C 1 ATOM 1063 O O . LEU A 1 144 ? 22.086 42.162 23.157 1.00 10.78 ? 226 LEU A O 1 ATOM 1064 C CB . LEU A 1 144 ? 20.643 40.399 25.134 1.00 11.57 ? 226 LEU A CB 1 ATOM 1065 C CG . LEU A 1 144 ? 20.125 39.086 25.723 1.00 11.57 ? 226 LEU A CG 1 ATOM 1066 C CD1 . LEU A 1 144 ? 18.606 39.099 25.716 1.00 11.57 ? 226 LEU A CD1 1 ATOM 1067 C CD2 . LEU A 1 144 ? 20.655 37.902 24.930 1.00 11.57 ? 226 LEU A CD2 1 ATOM 1068 N N . VAL A 1 145 ? 23.204 42.662 25.043 1.00 11.35 ? 227 VAL A N 1 ATOM 1069 C CA . VAL A 1 145 ? 23.612 43.983 24.582 1.00 11.35 ? 227 VAL A CA 1 ATOM 1070 C C . VAL A 1 145 ? 24.980 43.926 23.890 1.00 11.35 ? 227 VAL A C 1 ATOM 1071 O O . VAL A 1 145 ? 25.163 44.527 22.829 1.00 11.35 ? 227 VAL A O 1 ATOM 1072 C CB . VAL A 1 145 ? 23.691 44.999 25.754 1.00 8.82 ? 227 VAL A CB 1 ATOM 1073 C CG1 . VAL A 1 145 ? 24.098 46.381 25.249 1.00 8.82 ? 227 VAL A CG1 1 ATOM 1074 C CG2 . VAL A 1 145 ? 22.361 45.077 26.480 1.00 8.82 ? 227 VAL A CG2 1 ATOM 1075 N N . THR A 1 146 ? 25.915 43.158 24.451 1.00 13.16 ? 228 THR A N 1 ATOM 1076 C CA . THR A 1 146 ? 27.265 43.086 23.889 1.00 13.16 ? 228 THR A CA 1 ATOM 1077 C C . THR A 1 146 ? 27.765 41.733 23.374 1.00 13.16 ? 228 THR A C 1 ATOM 1078 O O . THR A 1 146 ? 28.670 41.687 22.533 1.00 13.16 ? 228 THR A O 1 ATOM 1079 C CB . THR A 1 146 ? 28.310 43.568 24.916 1.00 8.54 ? 228 THR A CB 1 ATOM 1080 O OG1 . THR A 1 146 ? 28.319 42.670 26.030 1.00 8.54 ? 228 THR A OG1 1 ATOM 1081 C CG2 . THR A 1 146 ? 27.988 44.974 25.412 1.00 8.54 ? 228 THR A CG2 1 ATOM 1082 N N . ASN A 1 147 ? 27.192 40.640 23.870 1.00 9.31 ? 229 ASN A N 1 ATOM 1083 C CA . ASN A 1 147 ? 27.658 39.308 23.486 1.00 9.31 ? 229 ASN A CA 1 ATOM 1084 C C . ASN A 1 147 ? 26.864 38.509 22.464 1.00 9.31 ? 229 ASN A C 1 ATOM 1085 O O . ASN A 1 147 ? 26.959 37.280 22.438 1.00 9.31 ? 229 ASN A O 1 ATOM 1086 C CB . ASN A 1 147 ? 27.886 38.456 24.741 1.00 20.35 ? 229 ASN A CB 1 ATOM 1087 C CG . ASN A 1 147 ? 28.863 39.095 25.707 1.00 20.35 ? 229 ASN A CG 1 ATOM 1088 O OD1 . ASN A 1 147 ? 29.678 39.929 25.320 1.00 20.35 ? 229 ASN A OD1 1 ATOM 1089 N ND2 . ASN A 1 147 ? 28.778 38.716 26.971 1.00 20.35 ? 229 ASN A ND2 1 ATOM 1090 N N . LEU A 1 148 ? 26.105 39.181 21.605 1.00 11.22 ? 230 LEU A N 1 ATOM 1091 C CA . LEU A 1 148 ? 25.348 38.455 20.591 1.00 11.22 ? 230 LEU A CA 1 ATOM 1092 C C . LEU A 1 148 ? 26.289 37.848 19.549 1.00 11.22 ? 230 LEU A C 1 ATOM 1093 O O . LEU A 1 148 ? 25.867 37.045 18.718 1.00 11.22 ? 230 LEU A O 1 ATOM 1094 C CB . LEU A 1 148 ? 24.297 39.344 19.930 1.00 12.51 ? 230 LEU A CB 1 ATOM 1095 C CG . LEU A 1 148 ? 23.094 39.683 20.809 1.00 12.51 ? 230 LEU A CG 1 ATOM 1096 C CD1 . LEU A 1 148 ? 22.104 40.505 20.007 1.00 12.51 ? 230 LEU A CD1 1 ATOM 1097 C CD2 . LEU A 1 148 ? 22.444 38.398 21.317 1.00 12.51 ? 230 LEU A CD2 1 ATOM 1098 N N . GLY A 1 149 ? 27.565 38.230 19.620 1.00 18.93 ? 231 GLY A N 1 ATOM 1099 C CA . GLY A 1 149 ? 28.574 37.696 18.720 1.00 18.93 ? 231 GLY A CA 1 ATOM 1100 C C . GLY A 1 149 ? 28.947 36.281 19.138 1.00 18.93 ? 231 GLY A C 1 ATOM 1101 O O . GLY A 1 149 ? 29.577 35.545 18.378 1.00 18.93 ? 231 GLY A O 1 ATOM 1102 N N . THR A 1 150 ? 28.595 35.921 20.372 1.00 10.66 ? 232 THR A N 1 ATOM 1103 C CA . THR A 1 150 ? 28.844 34.586 20.911 1.00 10.66 ? 232 THR A CA 1 ATOM 1104 C C . THR A 1 150 ? 27.596 33.778 20.568 1.00 10.66 ? 232 THR A C 1 ATOM 1105 O O . THR A 1 150 ? 26.488 34.142 20.961 1.00 10.66 ? 232 THR A O 1 ATOM 1106 C CB . THR A 1 150 ? 29.020 34.623 22.448 1.00 12.83 ? 232 THR A CB 1 ATOM 1107 O OG1 . THR A 1 150 ? 30.170 35.409 22.781 1.00 12.83 ? 232 THR A OG1 1 ATOM 1108 C CG2 . THR A 1 150 ? 29.190 33.217 23.011 1.00 12.83 ? 232 THR A CG2 1 ATOM 1109 N N . PRO A 1 151 ? 27.763 32.676 19.815 1.00 14.35 ? 233 PRO A N 1 ATOM 1110 C CA . PRO A 1 151 ? 26.678 31.786 19.382 1.00 14.35 ? 233 PRO A CA 1 ATOM 1111 C C . PRO A 1 151 ? 25.735 31.324 20.484 1.00 14.35 ? 233 PRO A C 1 ATOM 1112 O O . PRO A 1 151 ? 24.521 31.307 20.289 1.00 14.35 ? 233 PRO A O 1 ATOM 1113 C CB . PRO A 1 151 ? 27.428 30.610 18.766 1.00 20.29 ? 233 PRO A CB 1 ATOM 1114 C CG . PRO A 1 151 ? 28.647 31.252 18.211 1.00 20.29 ? 233 PRO A CG 1 ATOM 1115 C CD . PRO A 1 151 ? 29.061 32.196 19.313 1.00 20.29 ? 233 PRO A CD 1 ATOM 1116 N N . LYS A 1 152 ? 26.284 30.949 21.634 1.00 12.51 ? 234 LYS A N 1 ATOM 1117 C CA . LYS A 1 152 ? 25.441 30.490 22.731 1.00 12.51 ? 234 LYS A CA 1 ATOM 1118 C C . LYS A 1 152 ? 24.479 31.578 23.197 1.00 12.51 ? 234 LYS A C 1 ATOM 1119 O O . LYS A 1 152 ? 23.340 31.280 23.535 1.00 12.51 ? 234 LYS A O 1 ATOM 1120 C CB . LYS A 1 152 ? 26.272 29.975 23.904 1.00 22.81 ? 234 LYS A CB 1 ATOM 1121 C CG . LYS A 1 152 ? 25.420 29.308 24.966 1.00 22.81 ? 234 LYS A CG 1 ATOM 1122 C CD . LYS A 1 152 ? 26.259 28.669 26.037 1.00 22.81 ? 234 LYS A CD 1 ATOM 1123 C CE . LYS A 1 152 ? 25.375 27.972 27.047 1.00 22.81 ? 234 LYS A CE 1 ATOM 1124 N NZ . LYS A 1 152 ? 26.185 27.246 28.056 1.00 22.81 ? 234 LYS A NZ 1 ATOM 1125 N N . CYS A 1 153 ? 24.938 32.830 23.210 1.00 11.05 ? 235 CYS A N 1 ATOM 1126 C CA . CYS A 1 153 ? 24.089 33.952 23.616 1.00 11.05 ? 235 CYS A CA 1 ATOM 1127 C C . CYS A 1 153 ? 23.041 34.265 22.551 1.00 11.05 ? 235 CYS A C 1 ATOM 1128 O O . CYS A 1 153 ? 21.876 34.514 22.868 1.00 11.05 ? 235 CYS A O 1 ATOM 1129 C CB . CYS A 1 153 ? 24.925 35.204 23.892 1.00 9.79 ? 235 CYS A CB 1 ATOM 1130 S SG . CYS A 1 153 ? 25.942 35.096 25.395 1.00 9.79 ? 235 CYS A SG 1 ATOM 1131 N N . ALA A 1 154 ? 23.461 34.258 21.288 1.00 10.67 ? 236 ALA A N 1 ATOM 1132 C CA . ALA A 1 154 ? 22.550 34.537 20.184 1.00 10.67 ? 236 ALA A CA 1 ATOM 1133 C C . ALA A 1 154 ? 21.395 33.537 20.181 1.00 10.67 ? 236 ALA A C 1 ATOM 1134 O O . ALA A 1 154 ? 20.235 33.912 20.013 1.00 10.67 ? 236 ALA A O 1 ATOM 1135 C CB . ALA A 1 154 ? 23.296 34.481 18.854 1.00 7.14 ? 236 ALA A CB 1 ATOM 1136 N N . ASN A 1 155 ? 21.716 32.269 20.417 1.00 15.18 ? 237 ASN A N 1 ATOM 1137 C CA . ASN A 1 155 ? 20.708 31.213 20.431 1.00 15.18 ? 237 ASN A CA 1 ATOM 1138 C C . ASN A 1 155 ? 19.832 31.195 21.683 1.00 15.18 ? 237 ASN A C 1 ATOM 1139 O O . ASN A 1 155 ? 18.739 30.634 21.666 1.00 15.18 ? 237 ASN A O 1 ATOM 1140 C CB . ASN A 1 155 ? 21.372 29.849 20.218 1.00 46.90 ? 237 ASN A CB 1 ATOM 1141 C CG . ASN A 1 155 ? 22.028 29.727 18.850 1.00 46.90 ? 237 ASN A CG 1 ATOM 1142 O OD1 . ASN A 1 155 ? 21.610 30.373 17.885 1.00 46.90 ? 237 ASN A OD1 1 ATOM 1143 N ND2 . ASN A 1 155 ? 23.065 28.906 18.764 1.00 46.90 ? 237 ASN A ND2 1 ATOM 1144 N N . ALA A 1 156 ? 20.300 31.844 22.746 1.00 15.88 ? 238 ALA A N 1 ATOM 1145 C CA . ALA A 1 156 ? 19.574 31.906 24.012 1.00 15.88 ? 238 ALA A CA 1 ATOM 1146 C C . ALA A 1 156 ? 18.731 33.173 24.174 1.00 15.88 ? 238 ALA A C 1 ATOM 1147 O O . ALA A 1 156 ? 18.016 33.322 25.162 1.00 15.88 ? 238 ALA A O 1 ATOM 1148 C CB . ALA A 1 156 ? 20.556 31.794 25.165 1.00 2.00 ? 238 ALA A CB 1 ATOM 1149 N N . GLN A 1 157 ? 18.801 34.068 23.194 1.00 8.98 ? 239 GLN A N 1 ATOM 1150 C CA . GLN A 1 157 ? 18.077 35.335 23.237 1.00 8.98 ? 239 GLN A CA 1 ATOM 1151 C C . GLN A 1 157 ? 16.569 35.229 23.467 1.00 8.98 ? 239 GLN A C 1 ATOM 1152 O O . GLN A 1 157 ? 16.023 35.854 24.388 1.00 8.98 ? 239 GLN A O 1 ATOM 1153 C CB . GLN A 1 157 ? 18.369 36.127 21.965 1.00 22.19 ? 239 GLN A CB 1 ATOM 1154 C CG . GLN A 1 157 ? 17.674 37.468 21.888 1.00 22.19 ? 239 GLN A CG 1 ATOM 1155 C CD . GLN A 1 157 ? 18.223 38.340 20.781 1.00 22.19 ? 239 GLN A CD 1 ATOM 1156 O OE1 . GLN A 1 157 ? 18.262 39.566 20.912 1.00 22.19 ? 239 GLN A OE1 1 ATOM 1157 N NE2 . GLN A 1 157 ? 18.668 37.716 19.688 1.00 22.19 ? 239 GLN A NE2 1 ATOM 1158 N N . SER A 1 158 ? 15.905 34.432 22.637 1.00 7.47 ? 240 SER A N 1 ATOM 1159 C CA . SER A 1 158 ? 14.463 34.247 22.743 1.00 7.47 ? 240 SER A CA 1 ATOM 1160 C C . SER A 1 158 ? 14.049 33.614 24.065 1.00 7.47 ? 240 SER A C 1 ATOM 1161 O O . SER A 1 158 ? 13.037 33.997 24.650 1.00 7.47 ? 240 SER A O 1 ATOM 1162 C CB . SER A 1 158 ? 13.953 33.395 21.584 1.00 30.96 ? 240 SER A CB 1 ATOM 1163 O OG . SER A 1 158 ? 14.177 34.050 20.351 1.00 30.96 ? 240 SER A OG 1 ATOM 1164 N N . ALA A 1 159 ? 14.826 32.636 24.522 1.00 8.69 ? 241 ALA A N 1 ATOM 1165 C CA . ALA A 1 159 ? 14.539 31.958 25.780 1.00 8.69 ? 241 ALA A CA 1 ATOM 1166 C C . ALA A 1 159 ? 14.719 32.920 26.946 1.00 8.69 ? 241 ALA A C 1 ATOM 1167 O O . ALA A 1 159 ? 13.865 32.985 27.826 1.00 8.69 ? 241 ALA A O 1 ATOM 1168 C CB . ALA A 1 159 ? 15.430 30.749 25.947 1.00 6.87 ? 241 ALA A CB 1 ATOM 1169 N N . TYR A 1 160 ? 15.814 33.682 26.936 1.00 8.54 ? 242 TYR A N 1 ATOM 1170 C CA . TYR A 1 160 ? 16.079 34.654 27.995 1.00 8.54 ? 242 TYR A CA 1 ATOM 1171 C C . TYR A 1 160 ? 14.919 35.635 28.137 1.00 8.54 ? 242 TYR A C 1 ATOM 1172 O O . TYR A 1 160 ? 14.404 35.842 29.236 1.00 8.54 ? 242 TYR A O 1 ATOM 1173 C CB . TYR A 1 160 ? 17.362 35.445 27.720 1.00 5.88 ? 242 TYR A CB 1 ATOM 1174 C CG . TYR A 1 160 ? 18.664 34.787 28.158 1.00 5.88 ? 242 TYR A CG 1 ATOM 1175 C CD1 . TYR A 1 160 ? 18.744 33.416 28.417 1.00 5.88 ? 242 TYR A CD1 1 ATOM 1176 C CD2 . TYR A 1 160 ? 19.832 35.545 28.276 1.00 5.88 ? 242 TYR A CD2 1 ATOM 1177 C CE1 . TYR A 1 160 ? 19.957 32.821 28.775 1.00 5.88 ? 242 TYR A CE1 1 ATOM 1178 C CE2 . TYR A 1 160 ? 21.046 34.960 28.633 1.00 5.88 ? 242 TYR A CE2 1 ATOM 1179 C CZ . TYR A 1 160 ? 21.103 33.603 28.879 1.00 5.88 ? 242 TYR A CZ 1 ATOM 1180 O OH . TYR A 1 160 ? 22.317 33.039 29.205 1.00 5.88 ? 242 TYR A OH 1 ATOM 1181 N N . LEU A 1 161 ? 14.497 36.224 27.021 1.00 7.74 ? 243 LEU A N 1 ATOM 1182 C CA . LEU A 1 161 ? 13.399 37.192 27.032 1.00 7.74 ? 243 LEU A CA 1 ATOM 1183 C C . LEU A 1 161 ? 12.062 36.592 27.451 1.00 7.74 ? 243 LEU A C 1 ATOM 1184 O O . LEU A 1 161 ? 11.284 37.240 28.149 1.00 7.74 ? 243 LEU A O 1 ATOM 1185 C CB . LEU A 1 161 ? 13.274 37.881 25.672 1.00 12.69 ? 243 LEU A CB 1 ATOM 1186 C CG . LEU A 1 161 ? 14.462 38.771 25.292 1.00 12.69 ? 243 LEU A CG 1 ATOM 1187 C CD1 . LEU A 1 161 ? 14.325 39.224 23.849 1.00 12.69 ? 243 LEU A CD1 1 ATOM 1188 C CD2 . LEU A 1 161 ? 14.548 39.969 26.224 1.00 12.69 ? 243 LEU A CD2 1 ATOM 1189 N N . GLU A 1 162 ? 11.806 35.350 27.048 1.00 8.83 ? 244 GLU A N 1 ATOM 1190 C CA . GLU A 1 162 ? 10.557 34.690 27.411 1.00 8.83 ? 244 GLU A CA 1 ATOM 1191 C C . GLU A 1 162 ? 10.514 34.384 28.904 1.00 8.83 ? 244 GLU A C 1 ATOM 1192 O O . GLU A 1 162 ? 9.507 34.628 29.575 1.00 8.83 ? 244 GLU A O 1 ATOM 1193 C CB . GLU A 1 162 ? 10.366 33.393 26.625 1.00 30.23 ? 244 GLU A CB 1 ATOM 1194 C CG . GLU A 1 162 ? 9.051 32.710 26.966 1.00 30.23 ? 244 GLU A CG 1 ATOM 1195 C CD . GLU A 1 162 ? 8.778 31.452 26.166 1.00 30.23 ? 244 GLU A CD 1 ATOM 1196 O OE1 . GLU A 1 162 ? 9.548 31.131 25.230 1.00 30.23 ? 244 GLU A OE1 1 ATOM 1197 O OE2 . GLU A 1 162 ? 7.770 30.781 26.480 1.00 30.23 ? 244 GLU A OE2 1 ATOM 1198 N N . CYS A 1 163 ? 11.623 33.858 29.412 1.00 5.48 ? 245 CYS A N 1 ATOM 1199 C CA . CYS A 1 163 ? 11.744 33.500 30.816 1.00 5.48 ? 245 CYS A CA 1 ATOM 1200 C C . CYS A 1 163 ? 11.709 34.707 31.749 1.00 5.48 ? 245 CYS A C 1 ATOM 1201 O O . CYS A 1 163 ? 11.081 34.647 32.803 1.00 5.48 ? 245 CYS A O 1 ATOM 1202 C CB . CYS A 1 163 ? 13.019 32.690 31.040 1.00 10.63 ? 245 CYS A CB 1 ATOM 1203 S SG . CYS A 1 163 ? 12.953 31.011 30.380 1.00 10.63 ? 245 CYS A SG 1 ATOM 1204 N N . ILE A 1 164 ? 12.373 35.796 31.365 1.00 5.70 ? 246 ILE A N 1 ATOM 1205 C CA . ILE A 1 164 ? 12.389 37.015 32.178 1.00 5.70 ? 246 ILE A CA 1 ATOM 1206 C C . ILE A 1 164 ? 10.986 37.619 32.229 1.00 5.70 ? 246 ILE A C 1 ATOM 1207 O O . ILE A 1 164 ? 10.572 38.165 33.253 1.00 5.70 ? 246 ILE A O 1 ATOM 1208 C CB . ILE A 1 164 ? 13.381 38.077 31.621 1.00 10.93 ? 246 ILE A CB 1 ATOM 1209 C CG1 . ILE A 1 164 ? 14.825 37.577 31.730 1.00 10.93 ? 246 ILE A CG1 1 ATOM 1210 C CG2 . ILE A 1 164 ? 13.235 39.399 32.379 1.00 10.93 ? 246 ILE A CG2 1 ATOM 1211 C CD1 . ILE A 1 164 ? 15.280 37.391 33.135 1.00 10.93 ? 246 ILE A CD1 1 ATOM 1212 N N . ASN A 1 165 ? 10.268 37.553 31.112 1.00 5.39 ? 247 ASN A N 1 ATOM 1213 C CA . ASN A 1 165 ? 8.906 38.070 31.060 1.00 5.39 ? 247 ASN A CA 1 ATOM 1214 C C . ASN A 1 165 ? 8.039 37.274 32.041 1.00 5.39 ? 247 ASN A C 1 ATOM 1215 O O . ASN A 1 165 ? 7.239 37.846 32.781 1.00 5.39 ? 247 ASN A O 1 ATOM 1216 C CB . ASN A 1 165 ? 8.344 37.953 29.638 1.00 11.42 ? 247 ASN A CB 1 ATOM 1217 C CG . ASN A 1 165 ? 6.887 38.375 29.549 1.00 11.42 ? 247 ASN A CG 1 ATOM 1218 O OD1 . ASN A 1 165 ? 5.990 37.548 29.653 1.00 11.42 ? 247 ASN A OD1 1 ATOM 1219 N ND2 . ASN A 1 165 ? 6.649 39.666 29.375 1.00 11.42 ? 247 ASN A ND2 1 ATOM 1220 N N . TYR A 1 166 ? 8.233 35.958 32.071 1.00 8.57 ? 248 TYR A N 1 ATOM 1221 C CA . TYR A 1 166 ? 7.471 35.095 32.963 1.00 8.57 ? 248 TYR A CA 1 ATOM 1222 C C . TYR A 1 166 ? 7.772 35.420 34.422 1.00 8.57 ? 248 TYR A C 1 ATOM 1223 O O . TYR A 1 166 ? 6.858 35.579 35.224 1.00 8.57 ? 248 TYR A O 1 ATOM 1224 C CB . TYR A 1 166 ? 7.785 33.621 32.686 1.00 5.65 ? 248 TYR A CB 1 ATOM 1225 C CG . TYR A 1 166 ? 6.796 32.660 33.316 1.00 5.65 ? 248 TYR A CG 1 ATOM 1226 C CD1 . TYR A 1 166 ? 5.546 32.441 32.742 1.00 5.65 ? 248 TYR A CD1 1 ATOM 1227 C CD2 . TYR A 1 166 ? 7.110 31.974 34.487 1.00 5.65 ? 248 TYR A CD2 1 ATOM 1228 C CE1 . TYR A 1 166 ? 4.634 31.558 33.318 1.00 5.65 ? 248 TYR A CE1 1 ATOM 1229 C CE2 . TYR A 1 166 ? 6.210 31.093 35.070 1.00 5.65 ? 248 TYR A CE2 1 ATOM 1230 C CZ . TYR A 1 166 ? 4.974 30.890 34.484 1.00 5.65 ? 248 TYR A CZ 1 ATOM 1231 O OH . TYR A 1 166 ? 4.073 30.028 35.060 1.00 5.65 ? 248 TYR A OH 1 ATOM 1232 N N . ALA A 1 167 ? 9.056 35.528 34.752 1.00 5.45 ? 249 ALA A N 1 ATOM 1233 C CA . ALA A 1 167 ? 9.495 35.828 36.114 1.00 5.45 ? 249 ALA A CA 1 ATOM 1234 C C . ALA A 1 167 ? 8.908 37.138 36.633 1.00 5.45 ? 249 ALA A C 1 ATOM 1235 O O . ALA A 1 167 ? 8.329 37.182 37.714 1.00 5.45 ? 249 ALA A O 1 ATOM 1236 C CB . ALA A 1 167 ? 11.023 35.885 36.172 1.00 6.14 ? 249 ALA A CB 1 ATOM 1237 N N . VAL A 1 168 ? 9.055 38.192 35.838 1.00 7.25 ? 250 VAL A N 1 ATOM 1238 C CA . VAL A 1 168 ? 8.572 39.527 36.175 1.00 7.25 ? 250 VAL A CA 1 ATOM 1239 C C . VAL A 1 168 ? 7.039 39.627 36.286 1.00 7.25 ? 250 VAL A C 1 ATOM 1240 O O . VAL A 1 168 ? 6.519 40.357 37.127 1.00 7.25 ? 250 VAL A O 1 ATOM 1241 C CB . VAL A 1 168 ? 9.143 40.562 35.160 1.00 12.96 ? 250 VAL A CB 1 ATOM 1242 C CG1 . VAL A 1 168 ? 8.447 41.898 35.278 1.00 12.96 ? 250 VAL A CG1 1 ATOM 1243 C CG2 . VAL A 1 168 ? 10.634 40.741 35.400 1.00 12.96 ? 250 VAL A CG2 1 ATOM 1244 N N . THR A 1 169 ? 6.311 38.896 35.452 1.00 10.34 ? 251 THR A N 1 ATOM 1245 C CA . THR A 1 169 ? 4.857 38.945 35.530 1.00 10.34 ? 251 THR A CA 1 ATOM 1246 C C . THR A 1 169 ? 4.319 38.059 36.664 1.00 10.34 ? 251 THR A C 1 ATOM 1247 O O . THR A 1 169 ? 3.420 38.467 37.395 1.00 10.34 ? 251 THR A O 1 ATOM 1248 C CB . THR A 1 169 ? 4.182 38.573 34.174 1.00 11.90 ? 251 THR A CB 1 ATOM 1249 O OG1 . THR A 1 169 ? 4.649 37.297 33.725 1.00 11.90 ? 251 THR A OG1 1 ATOM 1250 C CG2 . THR A 1 169 ? 4.511 39.602 33.117 1.00 11.90 ? 251 THR A CG2 1 ATOM 1251 N N . GLN A 1 170 ? 4.912 36.881 36.851 1.00 8.71 ? 252 GLN A N 1 ATOM 1252 C CA . GLN A 1 170 ? 4.470 35.954 37.894 1.00 8.71 ? 252 GLN A CA 1 ATOM 1253 C C . GLN A 1 170 ? 4.861 36.356 39.313 1.00 8.71 ? 252 GLN A C 1 ATOM 1254 O O . GLN A 1 170 ? 4.231 35.922 40.279 1.00 8.71 ? 252 GLN A O 1 ATOM 1255 C CB . GLN A 1 170 ? 4.965 34.536 37.604 1.00 15.01 ? 252 GLN A CB 1 ATOM 1256 C CG . GLN A 1 170 ? 4.399 33.928 36.329 1.00 15.01 ? 252 GLN A CG 1 ATOM 1257 C CD . GLN A 1 170 ? 2.892 33.782 36.364 1.00 15.01 ? 252 GLN A CD 1 ATOM 1258 O OE1 . GLN A 1 170 ? 2.315 33.409 37.385 1.00 15.01 ? 252 GLN A OE1 1 ATOM 1259 N NE2 . GLN A 1 170 ? 2.245 34.072 35.242 1.00 15.01 ? 252 GLN A NE2 1 ATOM 1260 N N . LEU A 1 171 ? 5.920 37.147 39.444 1.00 6.45 ? 253 LEU A N 1 ATOM 1261 C CA . LEU A 1 171 ? 6.357 37.599 40.756 1.00 6.45 ? 253 LEU A CA 1 ATOM 1262 C C . LEU A 1 171 ? 5.876 39.021 41.029 1.00 6.45 ? 253 LEU A C 1 ATOM 1263 O O . LEU A 1 171 ? 6.298 39.653 41.995 1.00 6.45 ? 253 LEU A O 1 ATOM 1264 C CB . LEU A 1 171 ? 7.881 37.492 40.889 1.00 8.43 ? 253 LEU A CB 1 ATOM 1265 C CG . LEU A 1 171 ? 8.430 36.073 40.724 1.00 8.43 ? 253 LEU A CG 1 ATOM 1266 C CD1 . LEU A 1 171 ? 9.942 36.055 40.903 1.00 8.43 ? 253 LEU A CD1 1 ATOM 1267 C CD2 . LEU A 1 171 ? 7.766 35.131 41.721 1.00 8.43 ? 253 LEU A CD2 1 ATOM 1268 N N . ASN A 1 172 ? 4.984 39.520 40.175 1.00 10.97 ? 254 ASN A N 1 ATOM 1269 C CA . ASN A 1 172 ? 4.430 40.864 40.335 1.00 10.97 ? 254 ASN A CA 1 ATOM 1270 C C . ASN A 1 172 ? 3.341 40.811 41.416 1.00 10.97 ? 254 ASN A C 1 ATOM 1271 O O . ASN A 1 172 ? 2.149 40.682 41.115 1.00 10.97 ? 254 ASN A O 1 ATOM 1272 C CB . ASN A 1 172 ? 3.859 41.355 38.996 1.00 5.19 ? 254 ASN A CB 1 ATOM 1273 C CG . ASN A 1 172 ? 3.296 42.765 39.072 1.00 5.19 ? 254 ASN A CG 1 ATOM 1274 O OD1 . ASN A 1 172 ? 3.682 43.559 39.924 1.00 5.19 ? 254 ASN A OD1 1 ATOM 1275 N ND2 . ASN A 1 172 ? 2.387 43.082 38.163 1.00 5.19 ? 254 ASN A ND2 1 ATOM 1276 N N . LEU A 1 173 ? 3.780 40.866 42.676 1.00 9.65 ? 255 LEU A N 1 ATOM 1277 C CA . LEU A 1 173 ? 2.898 40.812 43.841 1.00 9.65 ? 255 LEU A CA 1 ATOM 1278 C C . LEU A 1 173 ? 3.086 42.060 44.717 1.00 9.65 ? 255 LEU A C 1 ATOM 1279 O O . LEU A 1 173 ? 4.139 42.698 44.680 1.00 9.65 ? 255 LEU A O 1 ATOM 1280 C CB . LEU A 1 173 ? 3.182 39.525 44.632 1.00 11.07 ? 255 LEU A CB 1 ATOM 1281 C CG . LEU A 1 173 ? 2.862 38.226 43.876 1.00 11.07 ? 255 LEU A CG 1 ATOM 1282 C CD1 . LEU A 1 173 ? 3.551 37.030 44.490 1.00 11.07 ? 255 LEU A CD1 1 ATOM 1283 C CD2 . LEU A 1 173 ? 1.362 38.013 43.836 1.00 11.07 ? 255 LEU A CD2 1 ATOM 1284 N N . PRO A 1 174 ? 2.065 42.419 45.523 1.00 9.51 ? 256 PRO A N 1 ATOM 1285 C CA . PRO A 1 174 ? 2.072 43.585 46.417 1.00 9.51 ? 256 PRO A CA 1 ATOM 1286 C C . PRO A 1 174 ? 3.221 43.678 47.417 1.00 9.51 ? 256 PRO A C 1 ATOM 1287 O O . PRO A 1 174 ? 3.683 44.775 47.725 1.00 9.51 ? 256 PRO A O 1 ATOM 1288 C CB . PRO A 1 174 ? 0.729 43.475 47.146 1.00 19.63 ? 256 PRO A CB 1 ATOM 1289 C CG . PRO A 1 174 ? -0.133 42.768 46.189 1.00 19.63 ? 256 PRO A CG 1 ATOM 1290 C CD . PRO A 1 174 ? 0.775 41.711 45.613 1.00 19.63 ? 256 PRO A CD 1 ATOM 1291 N N . ASN A 1 175 ? 3.655 42.537 47.944 1.00 9.15 ? 257 ASN A N 1 ATOM 1292 C CA . ASN A 1 175 ? 4.744 42.507 48.927 1.00 9.15 ? 257 ASN A CA 1 ATOM 1293 C C . ASN A 1 175 ? 6.132 42.355 48.300 1.00 9.15 ? 257 ASN A C 1 ATOM 1294 O O . ASN A 1 175 ? 7.128 42.248 49.013 1.00 9.15 ? 257 ASN A O 1 ATOM 1295 C CB . ASN A 1 175 ? 4.510 41.376 49.943 1.00 8.27 ? 257 ASN A CB 1 ATOM 1296 C CG . ASN A 1 175 ? 4.519 39.996 49.300 1.00 8.27 ? 257 ASN A CG 1 ATOM 1297 O OD1 . ASN A 1 175 ? 3.955 39.792 48.222 1.00 8.27 ? 257 ASN A OD1 1 ATOM 1298 N ND2 . ASN A 1 175 ? 5.164 39.043 49.959 1.00 8.27 ? 257 ASN A ND2 1 ATOM 1299 N N . VAL A 1 176 ? 6.191 42.381 46.971 1.00 7.73 ? 258 VAL A N 1 ATOM 1300 C CA . VAL A 1 176 ? 7.442 42.206 46.240 1.00 7.73 ? 258 VAL A CA 1 ATOM 1301 C C . VAL A 1 176 ? 8.010 43.481 45.616 1.00 7.73 ? 258 VAL A C 1 ATOM 1302 O O . VAL A 1 176 ? 7.274 44.392 45.227 1.00 7.73 ? 258 VAL A O 1 ATOM 1303 C CB . VAL A 1 176 ? 7.262 41.144 45.120 1.00 5.79 ? 258 VAL A CB 1 ATOM 1304 C CG1 . VAL A 1 176 ? 8.502 41.055 44.230 1.00 5.79 ? 258 VAL A CG1 1 ATOM 1305 C CG2 . VAL A 1 176 ? 6.961 39.792 45.732 1.00 5.79 ? 258 VAL A CG2 1 ATOM 1306 N N . ALA A 1 177 ? 9.337 43.545 45.565 1.00 8.85 ? 259 ALA A N 1 ATOM 1307 C CA . ALA A 1 177 ? 10.053 44.650 44.942 1.00 8.85 ? 259 ALA A CA 1 ATOM 1308 C C . ALA A 1 177 ? 11.152 43.969 44.137 1.00 8.85 ? 259 ALA A C 1 ATOM 1309 O O . ALA A 1 177 ? 12.002 43.291 44.706 1.00 8.85 ? 259 ALA A O 1 ATOM 1310 C CB . ALA A 1 177 ? 10.653 45.564 45.981 1.00 10.43 ? 259 ALA A CB 1 ATOM 1311 N N . MET A 1 178 ? 11.083 44.089 42.813 1.00 5.01 ? 260 MET A N 1 ATOM 1312 C CA . MET A 1 178 ? 12.064 43.483 41.923 1.00 5.01 ? 260 MET A CA 1 ATOM 1313 C C . MET A 1 178 ? 12.991 44.508 41.297 1.00 5.01 ? 260 MET A C 1 ATOM 1314 O O . MET A 1 178 ? 12.600 45.646 41.029 1.00 5.01 ? 260 MET A O 1 ATOM 1315 C CB . MET A 1 178 ? 11.378 42.723 40.782 1.00 9.66 ? 260 MET A CB 1 ATOM 1316 C CG . MET A 1 178 ? 10.676 41.441 41.167 1.00 9.66 ? 260 MET A CG 1 ATOM 1317 S SD . MET A 1 178 ? 9.852 40.698 39.734 1.00 9.66 ? 260 MET A SD 1 ATOM 1318 C CE . MET A 1 178 ? 8.404 41.727 39.594 1.00 9.66 ? 260 MET A CE 1 ATOM 1319 N N . TYR A 1 179 ? 14.226 44.088 41.056 1.00 6.03 ? 261 TYR A N 1 ATOM 1320 C CA . TYR A 1 179 ? 15.221 44.929 40.412 1.00 6.03 ? 261 TYR A CA 1 ATOM 1321 C C . TYR A 1 179 ? 15.922 44.068 39.373 1.00 6.03 ? 261 TYR A C 1 ATOM 1322 O O . TYR A 1 179 ? 16.520 43.048 39.709 1.00 6.03 ? 261 TYR A O 1 ATOM 1323 C CB . TYR A 1 179 ? 16.248 45.446 41.416 1.00 2.00 ? 261 TYR A CB 1 ATOM 1324 C CG . TYR A 1 179 ? 15.718 46.449 42.414 1.00 2.00 ? 261 TYR A CG 1 ATOM 1325 C CD1 . TYR A 1 179 ? 15.153 46.031 43.617 1.00 2.00 ? 261 TYR A CD1 1 ATOM 1326 C CD2 . TYR A 1 179 ? 15.832 47.822 42.181 1.00 2.00 ? 261 TYR A CD2 1 ATOM 1327 C CE1 . TYR A 1 179 ? 14.718 46.957 44.570 1.00 2.00 ? 261 TYR A CE1 1 ATOM 1328 C CE2 . TYR A 1 179 ? 15.402 48.753 43.124 1.00 2.00 ? 261 TYR A CE2 1 ATOM 1329 C CZ . TYR A 1 179 ? 14.850 48.314 44.317 1.00 2.00 ? 261 TYR A CZ 1 ATOM 1330 O OH . TYR A 1 179 ? 14.451 49.224 45.273 1.00 2.00 ? 261 TYR A OH 1 ATOM 1331 N N . LEU A 1 180 ? 15.780 44.439 38.106 1.00 5.69 ? 262 LEU A N 1 ATOM 1332 C CA . LEU A 1 180 ? 16.416 43.717 37.006 1.00 5.69 ? 262 LEU A CA 1 ATOM 1333 C C . LEU A 1 180 ? 17.911 43.991 37.000 1.00 5.69 ? 262 LEU A C 1 ATOM 1334 O O . LEU A 1 180 ? 18.324 45.142 37.125 1.00 5.69 ? 262 LEU A O 1 ATOM 1335 C CB . LEU A 1 180 ? 15.856 44.197 35.665 1.00 18.07 ? 262 LEU A CB 1 ATOM 1336 C CG . LEU A 1 180 ? 14.762 43.426 34.936 1.00 18.07 ? 262 LEU A CG 1 ATOM 1337 C CD1 . LEU A 1 180 ? 14.428 44.188 33.667 1.00 18.07 ? 262 LEU A CD1 1 ATOM 1338 C CD2 . LEU A 1 180 ? 15.225 42.010 34.605 1.00 18.07 ? 262 LEU A CD2 1 ATOM 1339 N N . ASP A 1 181 ? 18.718 42.950 36.819 1.00 4.55 ? 263 ASP A N 1 ATOM 1340 C CA . ASP A 1 181 ? 20.162 43.129 36.768 1.00 4.55 ? 263 ASP A CA 1 ATOM 1341 C C . ASP A 1 181 ? 20.522 43.920 35.507 1.00 4.55 ? 263 ASP A C 1 ATOM 1342 O O . ASP A 1 181 ? 20.030 43.620 34.418 1.00 4.55 ? 263 ASP A O 1 ATOM 1343 C CB . ASP A 1 181 ? 20.875 41.781 36.750 1.00 8.44 ? 263 ASP A CB 1 ATOM 1344 C CG . ASP A 1 181 ? 22.383 41.931 36.725 1.00 8.44 ? 263 ASP A CG 1 ATOM 1345 O OD1 . ASP A 1 181 ? 22.984 42.011 37.812 1.00 8.44 ? 263 ASP A OD1 1 ATOM 1346 O OD2 . ASP A 1 181 ? 22.964 41.990 35.622 1.00 8.44 ? 263 ASP A OD2 1 ATOM 1347 N N . ALA A 1 182 ? 21.400 44.908 35.661 1.00 7.59 ? 264 ALA A N 1 ATOM 1348 C CA . ALA A 1 182 ? 21.811 45.746 34.543 1.00 7.59 ? 264 ALA A CA 1 ATOM 1349 C C . ALA A 1 182 ? 23.331 45.899 34.429 1.00 7.59 ? 264 ALA A C 1 ATOM 1350 O O . ALA A 1 182 ? 23.823 46.974 34.114 1.00 7.59 ? 264 ALA A O 1 ATOM 1351 C CB . ALA A 1 182 ? 21.144 47.113 34.659 1.00 7.78 ? 264 ALA A CB 1 ATOM 1352 N N . GLY A 1 183 ? 24.068 44.821 34.685 1.00 4.08 ? 265 GLY A N 1 ATOM 1353 C CA . GLY A 1 183 ? 25.519 44.862 34.590 1.00 4.08 ? 265 GLY A CA 1 ATOM 1354 C C . GLY A 1 183 ? 26.156 45.920 35.472 1.00 4.08 ? 265 GLY A C 1 ATOM 1355 O O . GLY A 1 183 ? 25.722 46.134 36.604 1.00 4.08 ? 265 GLY A O 1 ATOM 1356 N N . HIS A 1 184 ? 27.177 46.594 34.950 1.00 4.04 ? 266 HIS A N 1 ATOM 1357 C CA . HIS A 1 184 ? 27.874 47.636 35.698 1.00 4.04 ? 266 HIS A CA 1 ATOM 1358 C C . HIS A 1 184 ? 28.520 48.653 34.759 1.00 4.04 ? 266 HIS A C 1 ATOM 1359 O O . HIS A 1 184 ? 28.486 48.488 33.539 1.00 4.04 ? 266 HIS A O 1 ATOM 1360 C CB . HIS A 1 184 ? 28.925 47.021 36.637 1.00 5.77 ? 266 HIS A CB 1 ATOM 1361 C CG . HIS A 1 184 ? 29.934 46.160 35.943 1.00 5.77 ? 266 HIS A CG 1 ATOM 1362 N ND1 . HIS A 1 184 ? 31.135 46.646 35.472 1.00 5.77 ? 266 HIS A ND1 1 ATOM 1363 C CD2 . HIS A 1 184 ? 29.913 44.844 35.624 1.00 5.77 ? 266 HIS A CD2 1 ATOM 1364 C CE1 . HIS A 1 184 ? 31.809 45.670 34.892 1.00 5.77 ? 266 HIS A CE1 1 ATOM 1365 N NE2 . HIS A 1 184 ? 31.088 44.567 34.970 1.00 5.77 ? 266 HIS A NE2 1 ATOM 1366 N N . ALA A 1 185 ? 29.130 49.684 35.340 1.00 5.64 ? 267 ALA A N 1 ATOM 1367 C CA . ALA A 1 185 ? 29.781 50.756 34.585 1.00 5.64 ? 267 ALA A CA 1 ATOM 1368 C C . ALA A 1 185 ? 30.788 50.283 33.546 1.00 5.64 ? 267 ALA A C 1 ATOM 1369 O O . ALA A 1 185 ? 30.881 50.855 32.462 1.00 5.64 ? 267 ALA A O 1 ATOM 1370 C CB . ALA A 1 185 ? 30.453 51.732 35.541 1.00 4.30 ? 267 ALA A CB 1 ATOM 1371 N N . GLY A 1 186 ? 31.542 49.242 33.884 1.00 10.11 ? 268 GLY A N 1 ATOM 1372 C CA . GLY A 1 186 ? 32.551 48.728 32.972 1.00 10.11 ? 268 GLY A CA 1 ATOM 1373 C C . GLY A 1 186 ? 32.032 47.866 31.845 1.00 10.11 ? 268 GLY A C 1 ATOM 1374 O O . GLY A 1 186 ? 32.792 47.475 30.963 1.00 10.11 ? 268 GLY A O 1 ATOM 1375 N N . TRP A 1 187 ? 30.742 47.553 31.886 1.00 8.70 ? 269 TRP A N 1 ATOM 1376 C CA . TRP A 1 187 ? 30.121 46.730 30.863 1.00 8.70 ? 269 TRP A CA 1 ATOM 1377 C C . TRP A 1 187 ? 29.179 47.588 30.019 1.00 8.70 ? 269 TRP A C 1 ATOM 1378 O O . TRP A 1 187 ? 29.446 47.843 28.845 1.00 8.70 ? 269 TRP A O 1 ATOM 1379 C CB . TRP A 1 187 ? 29.352 45.574 31.523 1.00 13.19 ? 269 TRP A CB 1 ATOM 1380 C CG . TRP A 1 187 ? 28.871 44.489 30.581 1.00 13.19 ? 269 TRP A CG 1 ATOM 1381 C CD1 . TRP A 1 187 ? 28.865 44.522 29.210 1.00 13.19 ? 269 TRP A CD1 1 ATOM 1382 C CD2 . TRP A 1 187 ? 28.339 43.210 30.949 1.00 13.19 ? 269 TRP A CD2 1 ATOM 1383 N NE1 . TRP A 1 187 ? 28.363 43.346 28.711 1.00 13.19 ? 269 TRP A NE1 1 ATOM 1384 C CE2 . TRP A 1 187 ? 28.033 42.520 29.754 1.00 13.19 ? 269 TRP A CE2 1 ATOM 1385 C CE3 . TRP A 1 187 ? 28.089 42.577 32.174 1.00 13.19 ? 269 TRP A CE3 1 ATOM 1386 C CZ2 . TRP A 1 187 ? 27.493 41.226 29.746 1.00 13.19 ? 269 TRP A CZ2 1 ATOM 1387 C CZ3 . TRP A 1 187 ? 27.550 41.292 32.168 1.00 13.19 ? 269 TRP A CZ3 1 ATOM 1388 C CH2 . TRP A 1 187 ? 27.258 40.632 30.958 1.00 13.19 ? 269 TRP A CH2 1 ATOM 1389 N N . LEU A 1 188 ? 28.092 48.051 30.632 1.00 9.74 ? 270 LEU A N 1 ATOM 1390 C CA . LEU A 1 188 ? 27.093 48.856 29.933 1.00 9.74 ? 270 LEU A CA 1 ATOM 1391 C C . LEU A 1 188 ? 27.257 50.360 30.101 1.00 9.74 ? 270 LEU A C 1 ATOM 1392 O O . LEU A 1 188 ? 26.533 51.136 29.481 1.00 9.74 ? 270 LEU A O 1 ATOM 1393 C CB . LEU A 1 188 ? 25.685 48.425 30.360 1.00 5.89 ? 270 LEU A CB 1 ATOM 1394 C CG . LEU A 1 188 ? 25.399 46.927 30.203 1.00 5.89 ? 270 LEU A CG 1 ATOM 1395 C CD1 . LEU A 1 188 ? 23.987 46.619 30.639 1.00 5.89 ? 270 LEU A CD1 1 ATOM 1396 C CD2 . LEU A 1 188 ? 25.618 46.493 28.759 1.00 5.89 ? 270 LEU A CD2 1 ATOM 1397 N N . GLY A 1 189 ? 28.227 50.767 30.918 1.00 8.66 ? 271 GLY A N 1 ATOM 1398 C CA . GLY A 1 189 ? 28.471 52.181 31.146 1.00 8.66 ? 271 GLY A CA 1 ATOM 1399 C C . GLY A 1 189 ? 29.165 52.886 29.993 1.00 8.66 ? 271 GLY A C 1 ATOM 1400 O O . GLY A 1 189 ? 29.098 54.111 29.888 1.00 8.66 ? 271 GLY A O 1 ATOM 1401 N N . TRP A 1 190 ? 29.859 52.130 29.146 1.00 10.72 ? 272 TRP A N 1 ATOM 1402 C CA . TRP A 1 190 ? 30.546 52.710 27.996 1.00 10.72 ? 272 TRP A CA 1 ATOM 1403 C C . TRP A 1 190 ? 29.513 53.444 27.154 1.00 10.72 ? 272 TRP A C 1 ATOM 1404 O O . TRP A 1 190 ? 28.424 52.929 26.911 1.00 10.72 ? 272 TRP A O 1 ATOM 1405 C CB . TRP A 1 190 ? 31.218 51.619 27.159 1.00 13.00 ? 272 TRP A CB 1 ATOM 1406 C CG . TRP A 1 190 ? 32.368 50.973 27.856 1.00 13.00 ? 272 TRP A CG 1 ATOM 1407 C CD1 . TRP A 1 190 ? 32.315 49.909 28.709 1.00 13.00 ? 272 TRP A CD1 1 ATOM 1408 C CD2 . TRP A 1 190 ? 33.745 51.372 27.793 1.00 13.00 ? 272 TRP A CD2 1 ATOM 1409 N NE1 . TRP A 1 190 ? 33.572 49.626 29.186 1.00 13.00 ? 272 TRP A NE1 1 ATOM 1410 C CE2 . TRP A 1 190 ? 34.468 50.506 28.642 1.00 13.00 ? 272 TRP A CE2 1 ATOM 1411 C CE3 . TRP A 1 190 ? 34.438 52.378 27.102 1.00 13.00 ? 272 TRP A CE3 1 ATOM 1412 C CZ2 . TRP A 1 190 ? 35.853 50.616 28.822 1.00 13.00 ? 272 TRP A CZ2 1 ATOM 1413 C CZ3 . TRP A 1 190 ? 35.818 52.485 27.282 1.00 13.00 ? 272 TRP A CZ3 1 ATOM 1414 C CH2 . TRP A 1 190 ? 36.507 51.608 28.135 1.00 13.00 ? 272 TRP A CH2 1 ATOM 1415 N N . PRO A 1 191 ? 29.841 54.661 26.702 1.00 11.41 ? 273 PRO A N 1 ATOM 1416 C CA . PRO A 1 191 ? 28.947 55.488 25.887 1.00 11.41 ? 273 PRO A CA 1 ATOM 1417 C C . PRO A 1 191 ? 28.184 54.755 24.785 1.00 11.41 ? 273 PRO A C 1 ATOM 1418 O O . PRO A 1 191 ? 26.970 54.913 24.662 1.00 11.41 ? 273 PRO A O 1 ATOM 1419 C CB . PRO A 1 191 ? 29.887 56.546 25.322 1.00 14.64 ? 273 PRO A CB 1 ATOM 1420 C CG . PRO A 1 191 ? 30.843 56.756 26.458 1.00 14.64 ? 273 PRO A CG 1 ATOM 1421 C CD . PRO A 1 191 ? 31.126 55.345 26.936 1.00 14.64 ? 273 PRO A CD 1 ATOM 1422 N N . ALA A 1 192 ? 28.881 53.918 24.023 1.00 11.09 ? 274 ALA A N 1 ATOM 1423 C CA . ALA A 1 192 ? 28.262 53.177 22.921 1.00 11.09 ? 274 ALA A CA 1 ATOM 1424 C C . ALA A 1 192 ? 27.250 52.111 23.354 1.00 11.09 ? 274 ALA A C 1 ATOM 1425 O O . ALA A 1 192 ? 26.439 51.662 22.547 1.00 11.09 ? 274 ALA A O 1 ATOM 1426 C CB . ALA A 1 192 ? 29.340 52.547 22.048 1.00 15.96 ? 274 ALA A CB 1 ATOM 1427 N N . ASN A 1 193 ? 27.300 51.717 24.625 1.00 9.23 ? 275 ASN A N 1 ATOM 1428 C CA . ASN A 1 193 ? 26.404 50.692 25.159 1.00 9.23 ? 275 ASN A CA 1 ATOM 1429 C C . ASN A 1 193 ? 25.214 51.232 25.941 1.00 9.23 ? 275 ASN A C 1 ATOM 1430 O O . ASN A 1 193 ? 24.257 50.504 26.189 1.00 9.23 ? 275 ASN A O 1 ATOM 1431 C CB . ASN A 1 193 ? 27.183 49.728 26.065 1.00 11.92 ? 275 ASN A CB 1 ATOM 1432 C CG . ASN A 1 193 ? 28.188 48.887 25.304 1.00 11.92 ? 275 ASN A CG 1 ATOM 1433 O OD1 . ASN A 1 193 ? 28.065 48.691 24.096 1.00 11.92 ? 275 ASN A OD1 1 ATOM 1434 N ND2 . ASN A 1 193 ? 29.190 48.377 26.013 1.00 11.92 ? 275 ASN A ND2 1 ATOM 1435 N N . GLN A 1 194 ? 25.282 52.494 26.345 1.00 12.70 ? 276 GLN A N 1 ATOM 1436 C CA . GLN A 1 194 ? 24.219 53.106 27.137 1.00 12.70 ? 276 GLN A CA 1 ATOM 1437 C C . GLN A 1 194 ? 22.824 53.056 26.528 1.00 12.70 ? 276 GLN A C 1 ATOM 1438 O O . GLN A 1 194 ? 21.897 52.549 27.156 1.00 12.70 ? 276 GLN A O 1 ATOM 1439 C CB . GLN A 1 194 ? 24.569 54.549 27.479 1.00 13.84 ? 276 GLN A CB 1 ATOM 1440 C CG . GLN A 1 194 ? 25.755 54.691 28.398 1.00 13.84 ? 276 GLN A CG 1 ATOM 1441 C CD . GLN A 1 194 ? 26.011 56.131 28.783 1.00 13.84 ? 276 GLN A CD 1 ATOM 1442 O OE1 . GLN A 1 194 ? 25.185 57.007 28.536 1.00 13.84 ? 276 GLN A OE1 1 ATOM 1443 N NE2 . GLN A 1 194 ? 27.161 56.384 29.391 1.00 13.84 ? 276 GLN A NE2 1 ATOM 1444 N N . ASP A 1 195 ? 22.668 53.582 25.315 1.00 6.67 ? 277 ASP A N 1 ATOM 1445 C CA . ASP A 1 195 ? 21.359 53.585 24.677 1.00 6.67 ? 277 ASP A CA 1 ATOM 1446 C C . ASP A 1 195 ? 20.818 52.188 24.358 1.00 6.67 ? 277 ASP A C 1 ATOM 1447 O O . ASP A 1 195 ? 19.655 51.900 24.645 1.00 6.67 ? 277 ASP A O 1 ATOM 1448 C CB . ASP A 1 195 ? 21.348 54.463 23.426 1.00 21.49 ? 277 ASP A CB 1 ATOM 1449 C CG . ASP A 1 195 ? 19.948 54.846 23.014 1.00 21.49 ? 277 ASP A CG 1 ATOM 1450 O OD1 . ASP A 1 195 ? 19.252 55.476 23.837 1.00 21.49 ? 277 ASP A OD1 1 ATOM 1451 O OD2 . ASP A 1 195 ? 19.535 54.499 21.890 1.00 21.49 ? 277 ASP A OD2 1 ATOM 1452 N N . PRO A 1 196 ? 21.631 51.319 23.723 1.00 9.70 ? 278 PRO A N 1 ATOM 1453 C CA . PRO A 1 196 ? 21.155 49.967 23.405 1.00 9.70 ? 278 PRO A CA 1 ATOM 1454 C C . PRO A 1 196 ? 20.673 49.241 24.664 1.00 9.70 ? 278 PRO A C 1 ATOM 1455 O O . PRO A 1 196 ? 19.700 48.490 24.631 1.00 9.70 ? 278 PRO A O 1 ATOM 1456 C CB . PRO A 1 196 ? 22.400 49.300 22.828 1.00 9.68 ? 278 PRO A CB 1 ATOM 1457 C CG . PRO A 1 196 ? 23.099 50.418 22.157 1.00 9.68 ? 278 PRO A CG 1 ATOM 1458 C CD . PRO A 1 196 ? 22.968 51.548 23.145 1.00 9.68 ? 278 PRO A CD 1 ATOM 1459 N N . ALA A 1 197 ? 21.358 49.481 25.778 1.00 6.56 ? 279 ALA A N 1 ATOM 1460 C CA . ALA A 1 197 ? 20.996 48.862 27.049 1.00 6.56 ? 279 ALA A CA 1 ATOM 1461 C C . ALA A 1 197 ? 19.675 49.430 27.568 1.00 6.56 ? 279 ALA A C 1 ATOM 1462 O O . ALA A 1 197 ? 18.778 48.682 27.941 1.00 6.56 ? 279 ALA A O 1 ATOM 1463 C CB . ALA A 1 197 ? 22.104 49.081 28.069 1.00 4.26 ? 279 ALA A CB 1 ATOM 1464 N N . ALA A 1 198 ? 19.551 50.755 27.555 1.00 5.51 ? 280 ALA A N 1 ATOM 1465 C CA . ALA A 1 198 ? 18.341 51.423 28.027 1.00 5.51 ? 280 ALA A CA 1 ATOM 1466 C C . ALA A 1 198 ? 17.124 50.972 27.242 1.00 5.51 ? 280 ALA A C 1 ATOM 1467 O O . ALA A 1 198 ? 16.045 50.799 27.811 1.00 5.51 ? 280 ALA A O 1 ATOM 1468 C CB . ALA A 1 198 ? 18.490 52.930 27.925 1.00 2.00 ? 280 ALA A CB 1 ATOM 1469 N N . GLN A 1 199 ? 17.310 50.791 25.934 1.00 7.57 ? 281 GLN A N 1 ATOM 1470 C CA . GLN A 1 199 ? 16.243 50.354 25.032 1.00 7.57 ? 281 GLN A CA 1 ATOM 1471 C C . GLN A 1 199 ? 15.726 48.982 25.423 1.00 7.57 ? 281 GLN A C 1 ATOM 1472 O O . GLN A 1 199 ? 14.518 48.781 25.535 1.00 7.57 ? 281 GLN A O 1 ATOM 1473 C CB . GLN A 1 199 ? 16.734 50.298 23.582 1.00 56.15 ? 281 GLN A CB 1 ATOM 1474 C CG . GLN A 1 199 ? 17.061 51.645 22.980 1.00 56.15 ? 281 GLN A CG 1 ATOM 1475 C CD . GLN A 1 199 ? 17.293 51.579 21.483 1.00 56.15 ? 281 GLN A CD 1 ATOM 1476 O OE1 . GLN A 1 199 ? 16.420 51.153 20.727 1.00 56.15 ? 281 GLN A OE1 1 ATOM 1477 N NE2 . GLN A 1 199 ? 18.474 52.005 21.047 1.00 56.15 ? 281 GLN A NE2 1 ATOM 1478 N N . LEU A 1 200 ? 16.649 48.042 25.617 1.00 6.69 ? 282 LEU A N 1 ATOM 1479 C CA . LEU A 1 200 ? 16.310 46.676 25.996 1.00 6.69 ? 282 LEU A CA 1 ATOM 1480 C C . LEU A 1 200 ? 15.569 46.612 27.330 1.00 6.69 ? 282 LEU A C 1 ATOM 1481 O O . LEU A 1 200 ? 14.521 45.977 27.434 1.00 6.69 ? 282 LEU A O 1 ATOM 1482 C CB . LEU A 1 200 ? 17.574 45.815 26.066 1.00 15.17 ? 282 LEU A CB 1 ATOM 1483 C CG . LEU A 1 200 ? 17.364 44.354 26.469 1.00 15.17 ? 282 LEU A CG 1 ATOM 1484 C CD1 . LEU A 1 200 ? 16.457 43.654 25.472 1.00 15.17 ? 282 LEU A CD1 1 ATOM 1485 C CD2 . LEU A 1 200 ? 18.701 43.647 26.554 1.00 15.17 ? 282 LEU A CD2 1 ATOM 1486 N N . PHE A 1 201 ? 16.115 47.258 28.354 1.00 5.48 ? 283 PHE A N 1 ATOM 1487 C CA . PHE A 1 201 ? 15.472 47.247 29.664 1.00 5.48 ? 283 PHE A CA 1 ATOM 1488 C C . PHE A 1 201 ? 14.075 47.875 29.619 1.00 5.48 ? 283 PHE A C 1 ATOM 1489 O O . PHE A 1 201 ? 13.145 47.357 30.240 1.00 5.48 ? 283 PHE A O 1 ATOM 1490 C CB . PHE A 1 201 ? 16.354 47.937 30.709 1.00 12.77 ? 283 PHE A CB 1 ATOM 1491 C CG . PHE A 1 201 ? 17.653 47.224 30.962 1.00 12.77 ? 283 PHE A CG 1 ATOM 1492 C CD1 . PHE A 1 201 ? 17.676 45.850 31.183 1.00 12.77 ? 283 PHE A CD1 1 ATOM 1493 C CD2 . PHE A 1 201 ? 18.858 47.924 30.967 1.00 12.77 ? 283 PHE A CD2 1 ATOM 1494 C CE1 . PHE A 1 201 ? 18.881 45.182 31.402 1.00 12.77 ? 283 PHE A CE1 1 ATOM 1495 C CE2 . PHE A 1 201 ? 20.068 47.266 31.185 1.00 12.77 ? 283 PHE A CE2 1 ATOM 1496 C CZ . PHE A 1 201 ? 20.079 45.893 31.401 1.00 12.77 ? 283 PHE A CZ 1 ATOM 1497 N N . ALA A 1 202 ? 13.916 48.953 28.851 1.00 10.68 ? 284 ALA A N 1 ATOM 1498 C CA . ALA A 1 202 ? 12.614 49.612 28.731 1.00 10.68 ? 284 ALA A CA 1 ATOM 1499 C C . ALA A 1 202 ? 11.623 48.700 28.002 1.00 10.68 ? 284 ALA A C 1 ATOM 1500 O O . ALA A 1 202 ? 10.433 48.684 28.320 1.00 10.68 ? 284 ALA A O 1 ATOM 1501 C CB . ALA A 1 202 ? 12.747 50.935 28.003 1.00 4.00 ? 284 ALA A CB 1 ATOM 1502 N N . ASN A 1 203 ? 12.116 47.939 27.029 1.00 10.01 ? 285 ASN A N 1 ATOM 1503 C CA . ASN A 1 203 ? 11.268 47.019 26.276 1.00 10.01 ? 285 ASN A CA 1 ATOM 1504 C C . ASN A 1 203 ? 10.783 45.883 27.162 1.00 10.01 ? 285 ASN A C 1 ATOM 1505 O O . ASN A 1 203 ? 9.639 45.447 27.048 1.00 10.01 ? 285 ASN A O 1 ATOM 1506 C CB . ASN A 1 203 ? 12.016 46.442 25.072 1.00 28.10 ? 285 ASN A CB 1 ATOM 1507 C CG . ASN A 1 203 ? 12.126 47.425 23.926 1.00 28.10 ? 285 ASN A CG 1 ATOM 1508 O OD1 . ASN A 1 203 ? 11.369 48.394 23.843 1.00 28.10 ? 285 ASN A OD1 1 ATOM 1509 N ND2 . ASN A 1 203 ? 13.073 47.178 23.028 1.00 28.10 ? 285 ASN A ND2 1 ATOM 1510 N N . VAL A 1 204 ? 11.663 45.387 28.027 1.00 12.04 ? 286 VAL A N 1 ATOM 1511 C CA . VAL A 1 204 ? 11.311 44.303 28.938 1.00 12.04 ? 286 VAL A CA 1 ATOM 1512 C C . VAL A 1 204 ? 10.201 44.762 29.886 1.00 12.04 ? 286 VAL A C 1 ATOM 1513 O O . VAL A 1 204 ? 9.241 44.030 30.133 1.00 12.04 ? 286 VAL A O 1 ATOM 1514 C CB . VAL A 1 204 ? 12.551 43.831 29.746 1.00 5.57 ? 286 VAL A CB 1 ATOM 1515 C CG1 . VAL A 1 204 ? 12.141 42.847 30.841 1.00 5.57 ? 286 VAL A CG1 1 ATOM 1516 C CG2 . VAL A 1 204 ? 13.560 43.183 28.805 1.00 5.57 ? 286 VAL A CG2 1 ATOM 1517 N N . TYR A 1 205 ? 10.328 45.996 30.370 1.00 8.70 ? 287 TYR A N 1 ATOM 1518 C CA . TYR A 1 205 ? 9.370 46.611 31.283 1.00 8.70 ? 287 TYR A CA 1 ATOM 1519 C C . TYR A 1 205 ? 7.994 46.776 30.637 1.00 8.70 ? 287 TYR A C 1 ATOM 1520 O O . TYR A 1 205 ? 6.981 46.372 31.206 1.00 8.70 ? 287 TYR A O 1 ATOM 1521 C CB . TYR A 1 205 ? 9.905 47.975 31.719 1.00 13.74 ? 287 TYR A CB 1 ATOM 1522 C CG . TYR A 1 205 ? 8.997 48.767 32.627 1.00 13.74 ? 287 TYR A CG 1 ATOM 1523 C CD1 . TYR A 1 205 ? 8.847 48.422 33.971 1.00 13.74 ? 287 TYR A CD1 1 ATOM 1524 C CD2 . TYR A 1 205 ? 8.311 49.883 32.152 1.00 13.74 ? 287 TYR A CD2 1 ATOM 1525 C CE1 . TYR A 1 205 ? 8.036 49.170 34.818 1.00 13.74 ? 287 TYR A CE1 1 ATOM 1526 C CE2 . TYR A 1 205 ? 7.498 50.639 32.990 1.00 13.74 ? 287 TYR A CE2 1 ATOM 1527 C CZ . TYR A 1 205 ? 7.366 50.276 34.318 1.00 13.74 ? 287 TYR A CZ 1 ATOM 1528 O OH . TYR A 1 205 ? 6.560 51.020 35.142 1.00 13.74 ? 287 TYR A OH 1 ATOM 1529 N N . LYS A 1 206 ? 7.966 47.386 29.455 1.00 7.43 ? 288 LYS A N 1 ATOM 1530 C CA . LYS A 1 206 ? 6.723 47.617 28.725 1.00 7.43 ? 288 LYS A CA 1 ATOM 1531 C C . LYS A 1 206 ? 6.085 46.326 28.215 1.00 7.43 ? 288 LYS A C 1 ATOM 1532 O O . LYS A 1 206 ? 4.863 46.213 28.156 1.00 7.43 ? 288 LYS A O 1 ATOM 1533 C CB . LYS A 1 206 ? 6.969 48.575 27.560 1.00 21.16 ? 288 LYS A CB 1 ATOM 1534 C CG . LYS A 1 206 ? 7.406 49.957 27.998 1.00 21.16 ? 288 LYS A CG 1 ATOM 1535 C CD . LYS A 1 206 ? 7.720 50.849 26.813 1.00 21.16 ? 288 LYS A CD 1 ATOM 1536 C CE . LYS A 1 206 ? 8.876 50.297 25.999 1.00 21.16 ? 288 LYS A CE 1 ATOM 1537 N NZ . LYS A 1 206 ? 9.267 51.201 24.888 1.00 21.16 ? 288 LYS A NZ 1 ATOM 1538 N N . ASN A 1 207 ? 6.915 45.350 27.862 1.00 14.09 ? 289 ASN A N 1 ATOM 1539 C CA . ASN A 1 207 ? 6.429 44.068 27.368 1.00 14.09 ? 289 ASN A CA 1 ATOM 1540 C C . ASN A 1 207 ? 5.756 43.270 28.486 1.00 14.09 ? 289 ASN A C 1 ATOM 1541 O O . ASN A 1 207 ? 4.935 42.386 28.224 1.00 14.09 ? 289 ASN A O 1 ATOM 1542 C CB . ASN A 1 207 ? 7.580 43.271 26.754 1.00 17.14 ? 289 ASN A CB 1 ATOM 1543 C CG . ASN A 1 207 ? 7.109 42.040 26.007 1.00 17.14 ? 289 ASN A CG 1 ATOM 1544 O OD1 . ASN A 1 207 ? 6.236 42.126 25.139 1.00 17.14 ? 289 ASN A OD1 1 ATOM 1545 N ND2 . ASN A 1 207 ? 7.696 40.893 26.347 1.00 17.14 ? 289 ASN A ND2 1 ATOM 1546 N N . ALA A 1 208 ? 6.115 43.573 29.731 1.00 10.71 ? 290 ALA A N 1 ATOM 1547 C CA . ALA A 1 208 ? 5.524 42.905 30.882 1.00 10.71 ? 290 ALA A CA 1 ATOM 1548 C C . ALA A 1 208 ? 4.375 43.750 31.431 1.00 10.71 ? 290 ALA A C 1 ATOM 1549 O O . ALA A 1 208 ? 3.934 43.557 32.565 1.00 10.71 ? 290 ALA A O 1 ATOM 1550 C CB . ALA A 1 208 ? 6.579 42.672 31.955 1.00 9.65 ? 290 ALA A CB 1 ATOM 1551 N N . SER A 1 209 ? 3.900 44.688 30.615 1.00 13.72 ? 291 SER A N 1 ATOM 1552 C CA . SER A 1 209 ? 2.804 45.583 30.977 1.00 13.72 ? 291 SER A CA 1 ATOM 1553 C C . SER A 1 209 ? 3.113 46.504 32.152 1.00 13.72 ? 291 SER A C 1 ATOM 1554 O O . SER A 1 209 ? 2.262 46.729 33.016 1.00 13.72 ? 291 SER A O 1 ATOM 1555 C CB . SER A 1 209 ? 1.528 44.786 31.253 1.00 21.23 ? 291 SER A CB 1 ATOM 1556 O OG . SER A 1 209 ? 1.134 44.070 30.098 1.00 21.23 ? 291 SER A OG 1 ATOM 1557 N N . SER A 1 210 ? 4.343 47.007 32.198 1.00 10.98 ? 292 SER A N 1 ATOM 1558 C CA . SER A 1 210 ? 4.771 47.931 33.250 1.00 10.98 ? 292 SER A CA 1 ATOM 1559 C C . SER A 1 210 ? 4.409 47.459 34.664 1.00 10.98 ? 292 SER A C 1 ATOM 1560 O O . SER A 1 210 ? 3.686 48.145 35.391 1.00 10.98 ? 292 SER A O 1 ATOM 1561 C CB . SER A 1 210 ? 4.160 49.308 32.983 1.00 22.21 ? 292 SER A CB 1 ATOM 1562 O OG . SER A 1 210 ? 4.424 49.714 31.652 1.00 22.21 ? 292 SER A OG 1 ATOM 1563 N N . PRO A 1 211 ? 4.968 46.314 35.095 1.00 13.75 ? 293 PRO A N 1 ATOM 1564 C CA . PRO A 1 211 ? 4.698 45.748 36.421 1.00 13.75 ? 293 PRO A CA 1 ATOM 1565 C C . PRO A 1 211 ? 4.953 46.704 37.580 1.00 13.75 ? 293 PRO A C 1 ATOM 1566 O O . PRO A 1 211 ? 6.024 47.304 37.688 1.00 13.75 ? 293 PRO A O 1 ATOM 1567 C CB . PRO A 1 211 ? 5.645 44.547 36.488 1.00 13.04 ? 293 PRO A CB 1 ATOM 1568 C CG . PRO A 1 211 ? 5.891 44.203 35.064 1.00 13.04 ? 293 PRO A CG 1 ATOM 1569 C CD . PRO A 1 211 ? 6.010 45.537 34.402 1.00 13.04 ? 293 PRO A CD 1 ATOM 1570 N N . ARG A 1 212 ? 3.954 46.816 38.450 1.00 10.71 ? 294 ARG A N 1 ATOM 1571 C CA . ARG A 1 212 ? 4.009 47.660 39.640 1.00 10.71 ? 294 ARG A CA 1 ATOM 1572 C C . ARG A 1 212 ? 5.201 47.274 40.527 1.00 10.71 ? 294 ARG A C 1 ATOM 1573 O O . ARG A 1 212 ? 5.937 48.141 41.006 1.00 10.71 ? 294 ARG A O 1 ATOM 1574 C CB . ARG A 1 212 ? 2.685 47.501 40.400 1.00 124.15 ? 294 ARG A CB 1 ATOM 1575 C CG . ARG A 1 212 ? 2.679 47.867 41.874 1.00 124.15 ? 294 ARG A CG 1 ATOM 1576 C CD . ARG A 1 212 ? 1.330 47.477 42.476 1.00 124.15 ? 294 ARG A CD 1 ATOM 1577 N NE . ARG A 1 212 ? 1.269 47.619 43.930 1.00 124.15 ? 294 ARG A NE 1 ATOM 1578 C CZ . ARG A 1 212 ? 0.150 47.519 44.645 1.00 124.15 ? 294 ARG A CZ 1 ATOM 1579 N NH1 . ARG A 1 212 ? -1.010 47.279 44.043 1.00 124.15 ? 294 ARG A NH1 1 ATOM 1580 N NH2 . ARG A 1 212 ? 0.186 47.653 45.965 1.00 124.15 ? 294 ARG A NH2 1 ATOM 1581 N N . ALA A 1 213 ? 5.407 45.970 40.698 1.00 6.30 ? 295 ALA A N 1 ATOM 1582 C CA . ALA A 1 213 ? 6.496 45.441 41.526 1.00 6.30 ? 295 ALA A CA 1 ATOM 1583 C C . ALA A 1 213 ? 7.907 45.635 40.962 1.00 6.30 ? 295 ALA A C 1 ATOM 1584 O O . ALA A 1 213 ? 8.877 45.549 41.705 1.00 6.30 ? 295 ALA A O 1 ATOM 1585 C CB . ALA A 1 213 ? 6.254 43.964 41.825 1.00 2.00 ? 295 ALA A CB 1 ATOM 1586 N N . LEU A 1 214 ? 8.034 45.855 39.654 1.00 8.73 ? 296 LEU A N 1 ATOM 1587 C CA . LEU A 1 214 ? 9.351 46.063 39.051 1.00 8.73 ? 296 LEU A CA 1 ATOM 1588 C C . LEU A 1 214 ? 9.803 47.504 39.313 1.00 8.73 ? 296 LEU A C 1 ATOM 1589 O O . LEU A 1 214 ? 9.519 48.418 38.538 1.00 8.73 ? 296 LEU A O 1 ATOM 1590 C CB . LEU A 1 214 ? 9.307 45.757 37.549 1.00 6.73 ? 296 LEU A CB 1 ATOM 1591 C CG . LEU A 1 214 ? 10.633 45.757 36.782 1.00 6.73 ? 296 LEU A CG 1 ATOM 1592 C CD1 . LEU A 1 214 ? 11.663 44.870 37.475 1.00 6.73 ? 296 LEU A CD1 1 ATOM 1593 C CD2 . LEU A 1 214 ? 10.375 45.275 35.369 1.00 6.73 ? 296 LEU A CD2 1 ATOM 1594 N N . ARG A 1 215 ? 10.508 47.693 40.424 1.00 6.84 ? 297 ARG A N 1 ATOM 1595 C CA . ARG A 1 215 ? 10.982 49.012 40.836 1.00 6.84 ? 297 ARG A CA 1 ATOM 1596 C C . ARG A 1 215 ? 12.101 49.625 39.996 1.00 6.84 ? 297 ARG A C 1 ATOM 1597 O O . ARG A 1 215 ? 12.143 50.846 39.808 1.00 6.84 ? 297 ARG A O 1 ATOM 1598 C CB . ARG A 1 215 ? 11.398 48.977 42.312 1.00 13.01 ? 297 ARG A CB 1 ATOM 1599 C CG . ARG A 1 215 ? 12.295 50.130 42.723 1.00 13.01 ? 297 ARG A CG 1 ATOM 1600 C CD . ARG A 1 215 ? 11.735 50.935 43.855 1.00 13.01 ? 297 ARG A CD 1 ATOM 1601 N NE . ARG A 1 215 ? 10.845 52.004 43.429 1.00 13.01 ? 297 ARG A NE 1 ATOM 1602 C CZ . ARG A 1 215 ? 10.922 53.259 43.869 1.00 13.01 ? 297 ARG A CZ 1 ATOM 1603 N NH1 . ARG A 1 215 ? 11.855 53.613 44.740 1.00 13.01 ? 297 ARG A NH1 1 ATOM 1604 N NH2 . ARG A 1 215 ? 10.015 54.146 43.494 1.00 13.01 ? 297 ARG A NH2 1 ATOM 1605 N N . GLY A 1 216 ? 13.022 48.790 39.521 1.00 5.96 ? 298 GLY A N 1 ATOM 1606 C CA . GLY A 1 216 ? 14.122 49.311 38.735 1.00 5.96 ? 298 GLY A CA 1 ATOM 1607 C C . GLY A 1 216 ? 15.221 48.329 38.400 1.00 5.96 ? 298 GLY A C 1 ATOM 1608 O O . GLY A 1 216 ? 14.955 47.160 38.143 1.00 5.96 ? 298 GLY A O 1 ATOM 1609 N N . LEU A 1 217 ? 16.467 48.798 38.458 1.00 4.51 ? 299 LEU A N 1 ATOM 1610 C CA . LEU A 1 217 ? 17.624 47.982 38.100 1.00 4.51 ? 299 LEU A CA 1 ATOM 1611 C C . LEU A 1 217 ? 18.664 47.810 39.208 1.00 4.51 ? 299 LEU A C 1 ATOM 1612 O O . LEU A 1 217 ? 18.799 48.661 40.082 1.00 4.51 ? 299 LEU A O 1 ATOM 1613 C CB . LEU A 1 217 ? 18.307 48.596 36.872 1.00 6.07 ? 299 LEU A CB 1 ATOM 1614 C CG . LEU A 1 217 ? 17.426 48.846 35.638 1.00 6.07 ? 299 LEU A CG 1 ATOM 1615 C CD1 . LEU A 1 217 ? 18.201 49.619 34.589 1.00 6.07 ? 299 LEU A CD1 1 ATOM 1616 C CD2 . LEU A 1 217 ? 16.940 47.528 35.072 1.00 6.07 ? 299 LEU A CD2 1 ATOM 1617 N N . ALA A 1 218 ? 19.414 46.713 39.136 1.00 4.14 ? 300 ALA A N 1 ATOM 1618 C CA . ALA A 1 218 ? 20.465 46.409 40.101 1.00 4.14 ? 300 ALA A CA 1 ATOM 1619 C C . ALA A 1 218 ? 21.788 46.448 39.347 1.00 4.14 ? 300 ALA A C 1 ATOM 1620 O O . ALA A 1 218 ? 21.890 45.890 38.255 1.00 4.14 ? 300 ALA A O 1 ATOM 1621 C CB . ALA A 1 218 ? 20.241 45.028 40.695 1.00 2.00 ? 300 ALA A CB 1 ATOM 1622 N N . THR A 1 219 ? 22.787 47.139 39.895 1.00 2.76 ? 301 THR A N 1 ATOM 1623 C CA . THR A 1 219 ? 24.082 47.230 39.227 1.00 2.76 ? 301 THR A CA 1 ATOM 1624 C C . THR A 1 219 ? 25.217 46.716 40.105 1.00 2.76 ? 301 THR A C 1 ATOM 1625 O O . THR A 1 219 ? 25.072 46.591 41.324 1.00 2.76 ? 301 THR A O 1 ATOM 1626 C CB . THR A 1 219 ? 24.429 48.689 38.782 1.00 6.46 ? 301 THR A CB 1 ATOM 1627 O OG1 . THR A 1 219 ? 24.916 49.436 39.903 1.00 6.46 ? 301 THR A OG1 1 ATOM 1628 C CG2 . THR A 1 219 ? 23.210 49.409 38.211 1.00 6.46 ? 301 THR A CG2 1 ATOM 1629 N N . ASN A 1 220 ? 26.333 46.396 39.456 1.00 3.13 ? 302 ASN A N 1 ATOM 1630 C CA . ASN A 1 220 ? 27.545 45.913 40.114 1.00 3.13 ? 302 ASN A CA 1 ATOM 1631 C C . ASN A 1 220 ? 27.406 44.588 40.861 1.00 3.13 ? 302 ASN A C 1 ATOM 1632 O O . ASN A 1 220 ? 28.250 44.255 41.685 1.00 3.13 ? 302 ASN A O 1 ATOM 1633 C CB . ASN A 1 220 ? 28.098 46.995 41.055 1.00 5.02 ? 302 ASN A CB 1 ATOM 1634 C CG . ASN A 1 220 ? 29.598 46.879 41.264 1.00 5.02 ? 302 ASN A CG 1 ATOM 1635 O OD1 . ASN A 1 220 ? 30.354 46.662 40.315 1.00 5.02 ? 302 ASN A OD1 1 ATOM 1636 N ND2 . ASN A 1 220 ? 30.036 47.034 42.508 1.00 5.02 ? 302 ASN A ND2 1 ATOM 1637 N N . VAL A 1 221 ? 26.365 43.821 40.556 1.00 2.00 ? 303 VAL A N 1 ATOM 1638 C CA . VAL A 1 221 ? 26.147 42.540 41.218 1.00 2.00 ? 303 VAL A CA 1 ATOM 1639 C C . VAL A 1 221 ? 27.321 41.583 41.013 1.00 2.00 ? 303 VAL A C 1 ATOM 1640 O O . VAL A 1 221 ? 27.699 41.267 39.880 1.00 2.00 ? 303 VAL A O 1 ATOM 1641 C CB . VAL A 1 221 ? 24.835 41.872 40.751 1.00 5.14 ? 303 VAL A CB 1 ATOM 1642 C CG1 . VAL A 1 221 ? 24.670 40.508 41.411 1.00 5.14 ? 303 VAL A CG1 1 ATOM 1643 C CG2 . VAL A 1 221 ? 23.653 42.759 41.104 1.00 5.14 ? 303 VAL A CG2 1 ATOM 1644 N N . ALA A 1 222 ? 27.896 41.138 42.128 1.00 3.46 ? 304 ALA A N 1 ATOM 1645 C CA . ALA A 1 222 ? 29.039 40.227 42.133 1.00 3.46 ? 304 ALA A CA 1 ATOM 1646 C C . ALA A 1 222 ? 30.284 40.878 41.541 1.00 3.46 ? 304 ALA A C 1 ATOM 1647 O O . ALA A 1 222 ? 31.256 40.198 41.224 1.00 3.46 ? 304 ALA A O 1 ATOM 1648 C CB . ALA A 1 222 ? 28.705 38.918 41.395 1.00 2.58 ? 304 ALA A CB 1 ATOM 1649 N N . ASN A 1 223 ? 30.241 42.191 41.358 1.00 3.26 ? 305 ASN A N 1 ATOM 1650 C CA . ASN A 1 223 ? 31.390 42.904 40.832 1.00 3.26 ? 305 ASN A CA 1 ATOM 1651 C C . ASN A 1 223 ? 32.049 43.791 41.881 1.00 3.26 ? 305 ASN A C 1 ATOM 1652 O O . ASN A 1 223 ? 31.646 43.779 43.048 1.00 3.26 ? 305 ASN A O 1 ATOM 1653 C CB . ASN A 1 223 ? 31.073 43.635 39.534 1.00 18.80 ? 305 ASN A CB 1 ATOM 1654 C CG . ASN A 1 223 ? 31.564 42.868 38.326 1.00 18.80 ? 305 ASN A CG 1 ATOM 1655 O OD1 . ASN A 1 223 ? 32.730 42.972 37.949 1.00 18.80 ? 305 ASN A OD1 1 ATOM 1656 N ND2 . ASN A 1 223 ? 30.700 42.033 37.758 1.00 18.80 ? 305 ASN A ND2 1 ATOM 1657 N N . TYR A 1 224 ? 33.045 44.572 41.472 1.00 8.22 ? 306 TYR A N 1 ATOM 1658 C CA . TYR A 1 224 ? 33.827 45.362 42.423 1.00 8.22 ? 306 TYR A CA 1 ATOM 1659 C C . TYR A 1 224 ? 33.955 46.866 42.204 1.00 8.22 ? 306 TYR A C 1 ATOM 1660 O O . TYR A 1 224 ? 34.773 47.504 42.860 1.00 8.22 ? 306 TYR A O 1 ATOM 1661 C CB . TYR A 1 224 ? 35.241 44.773 42.477 1.00 4.48 ? 306 TYR A CB 1 ATOM 1662 C CG . TYR A 1 224 ? 35.302 43.261 42.406 1.00 4.48 ? 306 TYR A CG 1 ATOM 1663 C CD1 . TYR A 1 224 ? 35.222 42.592 41.181 1.00 4.48 ? 306 TYR A CD1 1 ATOM 1664 C CD2 . TYR A 1 224 ? 35.459 42.499 43.564 1.00 4.48 ? 306 TYR A CD2 1 ATOM 1665 C CE1 . TYR A 1 224 ? 35.300 41.195 41.116 1.00 4.48 ? 306 TYR A CE1 1 ATOM 1666 C CE2 . TYR A 1 224 ? 35.540 41.112 43.512 1.00 4.48 ? 306 TYR A CE2 1 ATOM 1667 C CZ . TYR A 1 224 ? 35.463 40.467 42.292 1.00 4.48 ? 306 TYR A CZ 1 ATOM 1668 O OH . TYR A 1 224 ? 35.580 39.096 42.258 1.00 4.48 ? 306 TYR A OH 1 ATOM 1669 N N . ASN A 1 225 ? 33.174 47.432 41.289 1.00 6.58 ? 307 ASN A N 1 ATOM 1670 C CA . ASN A 1 225 ? 33.260 48.861 41.012 1.00 6.58 ? 307 ASN A CA 1 ATOM 1671 C C . ASN A 1 225 ? 32.942 49.734 42.224 1.00 6.58 ? 307 ASN A C 1 ATOM 1672 O O . ASN A 1 225 ? 32.179 49.339 43.112 1.00 6.58 ? 307 ASN A O 1 ATOM 1673 C CB . ASN A 1 225 ? 32.333 49.244 39.861 1.00 8.46 ? 307 ASN A CB 1 ATOM 1674 C CG . ASN A 1 225 ? 32.696 48.555 38.564 1.00 8.46 ? 307 ASN A CG 1 ATOM 1675 O OD1 . ASN A 1 225 ? 33.754 47.936 38.445 1.00 8.46 ? 307 ASN A OD1 1 ATOM 1676 N ND2 . ASN A 1 225 ? 31.813 48.651 37.583 1.00 8.46 ? 307 ASN A ND2 1 ATOM 1677 N N . GLY A 1 226 ? 33.559 50.910 42.270 1.00 6.03 ? 308 GLY A N 1 ATOM 1678 C CA . GLY A 1 226 ? 33.303 51.832 43.356 1.00 6.03 ? 308 GLY A CA 1 ATOM 1679 C C . GLY A 1 226 ? 32.008 52.568 43.077 1.00 6.03 ? 308 GLY A C 1 ATOM 1680 O O . GLY A 1 226 ? 31.584 52.684 41.925 1.00 6.03 ? 308 GLY A O 1 ATOM 1681 N N . TRP A 1 227 ? 31.355 53.030 44.135 1.00 5.05 ? 309 TRP A N 1 ATOM 1682 C CA . TRP A 1 227 ? 30.108 53.764 44.001 1.00 5.05 ? 309 TRP A CA 1 ATOM 1683 C C . TRP A 1 227 ? 30.338 55.207 43.565 1.00 5.05 ? 309 TRP A C 1 ATOM 1684 O O . TRP A 1 227 ? 29.791 55.651 42.556 1.00 5.05 ? 309 TRP A O 1 ATOM 1685 C CB . TRP A 1 227 ? 29.340 53.725 45.334 1.00 5.90 ? 309 TRP A CB 1 ATOM 1686 C CG . TRP A 1 227 ? 28.361 54.859 45.550 1.00 5.90 ? 309 TRP A CG 1 ATOM 1687 C CD1 . TRP A 1 227 ? 28.427 55.823 46.522 1.00 5.90 ? 309 TRP A CD1 1 ATOM 1688 C CD2 . TRP A 1 227 ? 27.190 55.154 44.777 1.00 5.90 ? 309 TRP A CD2 1 ATOM 1689 N NE1 . TRP A 1 227 ? 27.375 56.698 46.395 1.00 5.90 ? 309 TRP A NE1 1 ATOM 1690 C CE2 . TRP A 1 227 ? 26.599 56.313 45.331 1.00 5.90 ? 309 TRP A CE2 1 ATOM 1691 C CE3 . TRP A 1 227 ? 26.581 54.552 43.665 1.00 5.90 ? 309 TRP A CE3 1 ATOM 1692 C CZ2 . TRP A 1 227 ? 25.431 56.887 44.815 1.00 5.90 ? 309 TRP A CZ2 1 ATOM 1693 C CZ3 . TRP A 1 227 ? 25.420 55.120 43.149 1.00 5.90 ? 309 TRP A CZ3 1 ATOM 1694 C CH2 . TRP A 1 227 ? 24.857 56.277 43.725 1.00 5.90 ? 309 TRP A CH2 1 ATOM 1695 N N . ASN A 1 228 ? 31.170 55.932 44.308 1.00 6.96 ? 310 ASN A N 1 ATOM 1696 C CA . ASN A 1 228 ? 31.411 57.340 44.008 1.00 6.96 ? 310 ASN A CA 1 ATOM 1697 C C . ASN A 1 228 ? 32.868 57.791 44.088 1.00 6.96 ? 310 ASN A C 1 ATOM 1698 O O . ASN A 1 228 ? 33.148 58.924 44.498 1.00 6.96 ? 310 ASN A O 1 ATOM 1699 C CB . ASN A 1 228 ? 30.565 58.195 44.951 1.00 12.84 ? 310 ASN A CB 1 ATOM 1700 C CG . ASN A 1 228 ? 30.898 57.950 46.414 1.00 12.84 ? 310 ASN A CG 1 ATOM 1701 O OD1 . ASN A 1 228 ? 31.653 57.029 46.746 1.00 12.84 ? 310 ASN A OD1 1 ATOM 1702 N ND2 . ASN A 1 228 ? 30.333 58.774 47.290 1.00 12.84 ? 310 ASN A ND2 1 ATOM 1703 N N . ILE A 1 229 ? 33.793 56.922 43.691 1.00 12.41 ? 311 ILE A N 1 ATOM 1704 C CA . ILE A 1 229 ? 35.212 57.269 43.721 1.00 12.41 ? 311 ILE A CA 1 ATOM 1705 C C . ILE A 1 229 ? 35.495 58.511 42.868 1.00 12.41 ? 311 ILE A C 1 ATOM 1706 O O . ILE A 1 229 ? 34.940 58.677 41.781 1.00 12.41 ? 311 ILE A O 1 ATOM 1707 C CB . ILE A 1 229 ? 36.114 56.072 43.318 1.00 13.37 ? 311 ILE A CB 1 ATOM 1708 C CG1 . ILE A 1 229 ? 35.656 55.455 41.994 1.00 13.37 ? 311 ILE A CG1 1 ATOM 1709 C CG2 . ILE A 1 229 ? 36.091 55.022 44.418 1.00 13.37 ? 311 ILE A CG2 1 ATOM 1710 C CD1 . ILE A 1 229 ? 36.482 54.255 41.566 1.00 13.37 ? 311 ILE A CD1 1 ATOM 1711 N N . THR A 1 230 ? 36.332 59.394 43.406 1.00 19.34 ? 312 THR A N 1 ATOM 1712 C CA . THR A 1 230 ? 36.687 60.662 42.774 1.00 19.34 ? 312 THR A CA 1 ATOM 1713 C C . THR A 1 230 ? 37.757 60.617 41.685 1.00 19.34 ? 312 THR A C 1 ATOM 1714 O O . THR A 1 230 ? 37.914 61.579 40.930 1.00 19.34 ? 312 THR A O 1 ATOM 1715 C CB . THR A 1 230 ? 37.110 61.682 43.840 1.00 13.91 ? 312 THR A CB 1 ATOM 1716 O OG1 . THR A 1 230 ? 38.181 61.135 44.621 1.00 13.91 ? 312 THR A OG1 1 ATOM 1717 C CG2 . THR A 1 230 ? 35.943 61.990 44.760 1.00 13.91 ? 312 THR A CG2 1 ATOM 1718 N N . SER A 1 231 ? 38.505 59.521 41.622 1.00 17.27 ? 313 SER A N 1 ATOM 1719 C CA . SER A 1 231 ? 39.549 59.363 40.616 1.00 17.27 ? 313 SER A CA 1 ATOM 1720 C C . SER A 1 231 ? 39.402 58.024 39.906 1.00 17.27 ? 313 SER A C 1 ATOM 1721 O O . SER A 1 231 ? 39.184 56.994 40.542 1.00 17.27 ? 313 SER A O 1 ATOM 1722 C CB . SER A 1 231 ? 40.935 59.474 41.250 1.00 38.78 ? 313 SER A CB 1 ATOM 1723 O OG . SER A 1 231 ? 41.179 60.796 41.697 1.00 38.78 ? 313 SER A OG 1 ATOM 1724 N N . PRO A 1 232 ? 39.506 58.030 38.571 1.00 13.95 ? 314 PRO A N 1 ATOM 1725 C CA . PRO A 1 232 ? 39.383 56.812 37.762 1.00 13.95 ? 314 PRO A CA 1 ATOM 1726 C C . PRO A 1 232 ? 40.563 55.849 37.851 1.00 13.95 ? 314 PRO A C 1 ATOM 1727 O O . PRO A 1 232 ? 41.713 56.242 37.662 1.00 13.95 ? 314 PRO A O 1 ATOM 1728 C CB . PRO A 1 232 ? 39.234 57.364 36.347 1.00 14.76 ? 314 PRO A CB 1 ATOM 1729 C CG . PRO A 1 232 ? 40.024 58.624 36.387 1.00 14.76 ? 314 PRO A CG 1 ATOM 1730 C CD . PRO A 1 232 ? 39.654 59.219 37.715 1.00 14.76 ? 314 PRO A CD 1 ATOM 1731 N N . PRO A 1 233 ? 40.291 54.575 38.182 1.00 11.71 ? 315 PRO A N 1 ATOM 1732 C CA . PRO A 1 233 ? 41.355 53.572 38.275 1.00 11.71 ? 315 PRO A CA 1 ATOM 1733 C C . PRO A 1 233 ? 41.970 53.389 36.881 1.00 11.71 ? 315 PRO A C 1 ATOM 1734 O O . PRO A 1 233 ? 41.308 53.638 35.867 1.00 11.71 ? 315 PRO A O 1 ATOM 1735 C CB . PRO A 1 233 ? 40.603 52.320 38.721 1.00 10.00 ? 315 PRO A CB 1 ATOM 1736 C CG . PRO A 1 233 ? 39.450 52.860 39.497 1.00 10.00 ? 315 PRO A CG 1 ATOM 1737 C CD . PRO A 1 233 ? 39.006 54.023 38.651 1.00 10.00 ? 315 PRO A CD 1 ATOM 1738 N N . SER A 1 234 ? 43.230 52.967 36.828 1.00 14.10 ? 316 SER A N 1 ATOM 1739 C CA . SER A 1 234 ? 43.924 52.778 35.553 1.00 14.10 ? 316 SER A CA 1 ATOM 1740 C C . SER A 1 234 ? 43.195 51.843 34.595 1.00 14.10 ? 316 SER A C 1 ATOM 1741 O O . SER A 1 234 ? 43.116 52.116 33.400 1.00 14.10 ? 316 SER A O 1 ATOM 1742 C CB . SER A 1 234 ? 45.353 52.275 35.777 1.00 16.74 ? 316 SER A CB 1 ATOM 1743 O OG . SER A 1 234 ? 45.358 50.989 36.374 1.00 16.74 ? 316 SER A OG 1 ATOM 1744 N N . TYR A 1 235 ? 42.641 50.756 35.125 1.00 9.29 ? 317 TYR A N 1 ATOM 1745 C CA . TYR A 1 235 ? 41.930 49.786 34.294 1.00 9.29 ? 317 TYR A CA 1 ATOM 1746 C C . TYR A 1 235 ? 40.607 50.276 33.684 1.00 9.29 ? 317 TYR A C 1 ATOM 1747 O O . TYR A 1 235 ? 40.013 49.576 32.868 1.00 9.29 ? 317 TYR A O 1 ATOM 1748 C CB . TYR A 1 235 ? 41.739 48.459 35.043 1.00 6.66 ? 317 TYR A CB 1 ATOM 1749 C CG . TYR A 1 235 ? 41.197 48.609 36.442 1.00 6.66 ? 317 TYR A CG 1 ATOM 1750 C CD1 . TYR A 1 235 ? 39.846 48.860 36.663 1.00 6.66 ? 317 TYR A CD1 1 ATOM 1751 C CD2 . TYR A 1 235 ? 42.048 48.547 37.546 1.00 6.66 ? 317 TYR A CD2 1 ATOM 1752 C CE1 . TYR A 1 235 ? 39.354 49.054 37.945 1.00 6.66 ? 317 TYR A CE1 1 ATOM 1753 C CE2 . TYR A 1 235 ? 41.564 48.739 38.836 1.00 6.66 ? 317 TYR A CE2 1 ATOM 1754 C CZ . TYR A 1 235 ? 40.216 48.995 39.025 1.00 6.66 ? 317 TYR A CZ 1 ATOM 1755 O OH . TYR A 1 235 ? 39.735 49.213 40.292 1.00 6.66 ? 317 TYR A OH 1 ATOM 1756 N N . THR A 1 236 ? 40.150 51.470 34.065 1.00 13.01 ? 318 THR A N 1 ATOM 1757 C CA . THR A 1 236 ? 38.906 52.019 33.506 1.00 13.01 ? 318 THR A CA 1 ATOM 1758 C C . THR A 1 236 ? 39.198 52.965 32.343 1.00 13.01 ? 318 THR A C 1 ATOM 1759 O O . THR A 1 236 ? 38.276 53.524 31.742 1.00 13.01 ? 318 THR A O 1 ATOM 1760 C CB . THR A 1 236 ? 38.072 52.814 34.546 1.00 8.52 ? 318 THR A CB 1 ATOM 1761 O OG1 . THR A 1 236 ? 38.764 54.015 34.908 1.00 8.52 ? 318 THR A OG1 1 ATOM 1762 C CG2 . THR A 1 236 ? 37.809 51.978 35.790 1.00 8.52 ? 318 THR A CG2 1 ATOM 1763 N N . GLN A 1 237 ? 40.484 53.137 32.041 1.00 18.92 ? 319 GLN A N 1 ATOM 1764 C CA . GLN A 1 237 ? 40.962 54.021 30.974 1.00 18.92 ? 319 GLN A CA 1 ATOM 1765 C C . GLN A 1 237 ? 40.116 54.002 29.706 1.00 18.92 ? 319 GLN A C 1 ATOM 1766 O O . GLN A 1 237 ? 39.857 52.944 29.134 1.00 18.92 ? 319 GLN A O 1 ATOM 1767 C CB . GLN A 1 237 ? 42.419 53.686 30.633 1.00 165.05 ? 319 GLN A CB 1 ATOM 1768 C CG . GLN A 1 237 ? 43.062 54.613 29.607 1.00 165.05 ? 319 GLN A CG 1 ATOM 1769 C CD . GLN A 1 237 ? 44.487 54.212 29.259 1.00 165.05 ? 319 GLN A CD 1 ATOM 1770 O OE1 . GLN A 1 237 ? 45.028 53.246 29.801 1.00 165.05 ? 319 GLN A OE1 1 ATOM 1771 N NE2 . GLN A 1 237 ? 45.102 54.958 28.344 1.00 165.05 ? 319 GLN A NE2 1 ATOM 1772 N N . GLY A 1 238 ? 39.668 55.185 29.298 1.00 21.43 ? 320 GLY A N 1 ATOM 1773 C CA . GLY A 1 238 ? 38.860 55.312 28.097 1.00 21.43 ? 320 GLY A CA 1 ATOM 1774 C C . GLY A 1 238 ? 37.369 55.441 28.348 1.00 21.43 ? 320 GLY A C 1 ATOM 1775 O O . GLY A 1 238 ? 36.604 55.740 27.428 1.00 21.43 ? 320 GLY A O 1 ATOM 1776 N N . ASN A 1 239 ? 36.954 55.221 29.592 1.00 8.80 ? 321 ASN A N 1 ATOM 1777 C CA . ASN A 1 239 ? 35.542 55.301 29.952 1.00 8.80 ? 321 ASN A CA 1 ATOM 1778 C C . ASN A 1 239 ? 35.295 56.434 30.943 1.00 8.80 ? 321 ASN A C 1 ATOM 1779 O O . ASN A 1 239 ? 35.817 56.421 32.055 1.00 8.80 ? 321 ASN A O 1 ATOM 1780 C CB . ASN A 1 239 ? 35.085 53.969 30.556 1.00 13.73 ? 321 ASN A CB 1 ATOM 1781 C CG . ASN A 1 239 ? 33.577 53.808 30.551 1.00 13.73 ? 321 ASN A CG 1 ATOM 1782 O OD1 . ASN A 1 239 ? 32.845 54.692 30.106 1.00 13.73 ? 321 ASN A OD1 1 ATOM 1783 N ND2 . ASN A 1 239 ? 33.106 52.663 31.029 1.00 13.73 ? 321 ASN A ND2 1 ATOM 1784 N N . ALA A 1 240 ? 34.496 57.415 30.532 1.00 14.57 ? 322 ALA A N 1 ATOM 1785 C CA . ALA A 1 240 ? 34.172 58.551 31.392 1.00 14.57 ? 322 ALA A CA 1 ATOM 1786 C C . ALA A 1 240 ? 33.300 58.093 32.561 1.00 14.57 ? 322 ALA A C 1 ATOM 1787 O O . ALA A 1 240 ? 33.307 58.702 33.625 1.00 14.57 ? 322 ALA A O 1 ATOM 1788 C CB . ALA A 1 240 ? 33.458 59.628 30.590 1.00 18.23 ? 322 ALA A CB 1 ATOM 1789 N N . VAL A 1 241 ? 32.534 57.028 32.340 1.00 12.31 ? 323 VAL A N 1 ATOM 1790 C CA . VAL A 1 241 ? 31.662 56.448 33.362 1.00 12.31 ? 323 VAL A CA 1 ATOM 1791 C C . VAL A 1 241 ? 32.491 55.367 34.061 1.00 12.31 ? 323 VAL A C 1 ATOM 1792 O O . VAL A 1 241 ? 32.439 54.195 33.687 1.00 12.31 ? 323 VAL A O 1 ATOM 1793 C CB . VAL A 1 241 ? 30.408 55.817 32.710 1.00 6.38 ? 323 VAL A CB 1 ATOM 1794 C CG1 . VAL A 1 241 ? 29.530 55.158 33.757 1.00 6.38 ? 323 VAL A CG1 1 ATOM 1795 C CG2 . VAL A 1 241 ? 29.621 56.881 31.966 1.00 6.38 ? 323 VAL A CG2 1 ATOM 1796 N N . TYR A 1 242 ? 33.254 55.769 35.075 1.00 10.88 ? 324 TYR A N 1 ATOM 1797 C CA . TYR A 1 242 ? 34.131 54.841 35.785 1.00 10.88 ? 324 TYR A CA 1 ATOM 1798 C C . TYR A 1 242 ? 33.664 54.357 37.163 1.00 10.88 ? 324 TYR A C 1 ATOM 1799 O O . TYR A 1 242 ? 34.394 53.633 37.849 1.00 10.88 ? 324 TYR A O 1 ATOM 1800 C CB . TYR A 1 242 ? 35.542 55.427 35.871 1.00 14.15 ? 324 TYR A CB 1 ATOM 1801 C CG . TYR A 1 242 ? 35.615 56.693 36.678 1.00 14.15 ? 324 TYR A CG 1 ATOM 1802 C CD1 . TYR A 1 242 ? 35.719 56.643 38.065 1.00 14.15 ? 324 TYR A CD1 1 ATOM 1803 C CD2 . TYR A 1 242 ? 35.562 57.941 36.062 1.00 14.15 ? 324 TYR A CD2 1 ATOM 1804 C CE1 . TYR A 1 242 ? 35.766 57.797 38.821 1.00 14.15 ? 324 TYR A CE1 1 ATOM 1805 C CE2 . TYR A 1 242 ? 35.609 59.111 36.812 1.00 14.15 ? 324 TYR A CE2 1 ATOM 1806 C CZ . TYR A 1 242 ? 35.711 59.025 38.193 1.00 14.15 ? 324 TYR A CZ 1 ATOM 1807 O OH . TYR A 1 242 ? 35.761 60.159 38.967 1.00 14.15 ? 324 TYR A OH 1 ATOM 1808 N N . ASN A 1 243 ? 32.509 54.839 37.611 1.00 3.85 ? 325 ASN A N 1 ATOM 1809 C CA . ASN A 1 243 ? 31.940 54.387 38.877 1.00 3.85 ? 325 ASN A CA 1 ATOM 1810 C C . ASN A 1 243 ? 30.437 54.162 38.703 1.00 3.85 ? 325 ASN A C 1 ATOM 1811 O O . ASN A 1 243 ? 29.864 54.532 37.676 1.00 3.85 ? 325 ASN A O 1 ATOM 1812 C CB . ASN A 1 243 ? 32.265 55.332 40.050 1.00 6.27 ? 325 ASN A CB 1 ATOM 1813 C CG . ASN A 1 243 ? 31.683 56.718 39.887 1.00 6.27 ? 325 ASN A CG 1 ATOM 1814 O OD1 . ASN A 1 243 ? 30.568 56.881 39.429 1.00 6.27 ? 325 ASN A OD1 1 ATOM 1815 N ND2 . ASN A 1 243 ? 32.432 57.725 40.309 1.00 6.27 ? 325 ASN A ND2 1 ATOM 1816 N N . GLU A 1 244 ? 29.808 53.529 39.687 1.00 7.65 ? 326 GLU A N 1 ATOM 1817 C CA . GLU A 1 244 ? 28.384 53.227 39.604 1.00 7.65 ? 326 GLU A CA 1 ATOM 1818 C C . GLU A 1 244 ? 27.434 54.425 39.644 1.00 7.65 ? 326 GLU A C 1 ATOM 1819 O O . GLU A 1 244 ? 26.376 54.396 39.011 1.00 7.65 ? 326 GLU A O 1 ATOM 1820 C CB . GLU A 1 244 ? 28.004 52.182 40.655 1.00 7.23 ? 326 GLU A CB 1 ATOM 1821 C CG . GLU A 1 244 ? 28.695 50.833 40.452 1.00 7.23 ? 326 GLU A CG 1 ATOM 1822 C CD . GLU A 1 244 ? 28.445 50.258 39.068 1.00 7.23 ? 326 GLU A CD 1 ATOM 1823 O OE1 . GLU A 1 244 ? 27.288 49.912 38.762 1.00 7.23 ? 326 GLU A OE1 1 ATOM 1824 O OE2 . GLU A 1 244 ? 29.403 50.163 38.274 1.00 7.23 ? 326 GLU A OE2 1 ATOM 1825 N N . LYS A 1 245 ? 27.805 55.471 40.377 1.00 4.37 ? 327 LYS A N 1 ATOM 1826 C CA . LYS A 1 245 ? 26.974 56.669 40.463 1.00 4.37 ? 327 LYS A CA 1 ATOM 1827 C C . LYS A 1 245 ? 26.833 57.303 39.080 1.00 4.37 ? 327 LYS A C 1 ATOM 1828 O O . LYS A 1 245 ? 25.729 57.636 38.650 1.00 4.37 ? 327 LYS A O 1 ATOM 1829 C CB . LYS A 1 245 ? 27.582 57.673 41.445 1.00 13.11 ? 327 LYS A CB 1 ATOM 1830 C CG . LYS A 1 245 ? 26.750 58.928 41.654 1.00 13.11 ? 327 LYS A CG 1 ATOM 1831 C CD . LYS A 1 245 ? 27.397 59.836 42.678 1.00 13.11 ? 327 LYS A CD 1 ATOM 1832 C CE . LYS A 1 245 ? 26.602 61.113 42.870 1.00 13.11 ? 327 LYS A CE 1 ATOM 1833 N NZ . LYS A 1 245 ? 27.231 61.992 43.900 1.00 13.11 ? 327 LYS A NZ 1 ATOM 1834 N N . LEU A 1 246 ? 27.959 57.451 38.385 1.00 7.78 ? 328 LEU A N 1 ATOM 1835 C CA . LEU A 1 246 ? 27.979 58.025 37.047 1.00 7.78 ? 328 LEU A CA 1 ATOM 1836 C C . LEU A 1 246 ? 27.188 57.148 36.085 1.00 7.78 ? 328 LEU A C 1 ATOM 1837 O O . LEU A 1 246 ? 26.554 57.648 35.156 1.00 7.78 ? 328 LEU A O 1 ATOM 1838 C CB . LEU A 1 246 ? 29.419 58.168 36.543 1.00 6.83 ? 328 LEU A CB 1 ATOM 1839 C CG . LEU A 1 246 ? 30.311 59.211 37.231 1.00 6.83 ? 328 LEU A CG 1 ATOM 1840 C CD1 . LEU A 1 246 ? 31.735 59.093 36.739 1.00 6.83 ? 328 LEU A CD1 1 ATOM 1841 C CD2 . LEU A 1 246 ? 29.772 60.610 36.981 1.00 6.83 ? 328 LEU A CD2 1 ATOM 1842 N N . TYR A 1 247 ? 27.244 55.838 36.302 1.00 7.56 ? 329 TYR A N 1 ATOM 1843 C CA . TYR A 1 247 ? 26.530 54.887 35.457 1.00 7.56 ? 329 TYR A CA 1 ATOM 1844 C C . TYR A 1 247 ? 25.004 55.030 35.562 1.00 7.56 ? 329 TYR A C 1 ATOM 1845 O O . TYR A 1 247 ? 24.324 55.190 34.544 1.00 7.56 ? 329 TYR A O 1 ATOM 1846 C CB . TYR A 1 247 ? 26.961 53.453 35.800 1.00 6.18 ? 329 TYR A CB 1 ATOM 1847 C CG . TYR A 1 247 ? 26.210 52.373 35.051 1.00 6.18 ? 329 TYR A CG 1 ATOM 1848 C CD1 . TYR A 1 247 ? 25.905 52.517 33.699 1.00 6.18 ? 329 TYR A CD1 1 ATOM 1849 C CD2 . TYR A 1 247 ? 25.773 51.224 35.703 1.00 6.18 ? 329 TYR A CD2 1 ATOM 1850 C CE1 . TYR A 1 247 ? 25.179 51.552 33.019 1.00 6.18 ? 329 TYR A CE1 1 ATOM 1851 C CE2 . TYR A 1 247 ? 25.043 50.247 35.030 1.00 6.18 ? 329 TYR A CE2 1 ATOM 1852 C CZ . TYR A 1 247 ? 24.751 50.418 33.690 1.00 6.18 ? 329 TYR A CZ 1 ATOM 1853 O OH . TYR A 1 247 ? 24.030 49.461 33.004 1.00 6.18 ? 329 TYR A OH 1 ATOM 1854 N N . ILE A 1 248 ? 24.467 54.981 36.781 1.00 9.78 ? 330 ILE A N 1 ATOM 1855 C CA . ILE A 1 248 ? 23.019 55.085 36.966 1.00 9.78 ? 330 ILE A CA 1 ATOM 1856 C C . ILE A 1 248 ? 22.451 56.443 36.550 1.00 9.78 ? 330 ILE A C 1 ATOM 1857 O O . ILE A 1 248 ? 21.325 56.522 36.060 1.00 9.78 ? 330 ILE A O 1 ATOM 1858 C CB . ILE A 1 248 ? 22.558 54.719 38.413 1.00 6.06 ? 330 ILE A CB 1 ATOM 1859 C CG1 . ILE A 1 248 ? 22.960 55.798 39.420 1.00 6.06 ? 330 ILE A CG1 1 ATOM 1860 C CG2 . ILE A 1 248 ? 23.139 53.374 38.820 1.00 6.06 ? 330 ILE A CG2 1 ATOM 1861 C CD1 . ILE A 1 248 ? 22.335 55.602 40.803 1.00 6.06 ? 330 ILE A CD1 1 ATOM 1862 N N . HIS A 1 249 ? 23.234 57.502 36.719 1.00 5.99 ? 331 HIS A N 1 ATOM 1863 C CA . HIS A 1 249 ? 22.781 58.830 36.329 1.00 5.99 ? 331 HIS A CA 1 ATOM 1864 C C . HIS A 1 249 ? 22.833 59.040 34.824 1.00 5.99 ? 331 HIS A C 1 ATOM 1865 O O . HIS A 1 249 ? 22.200 59.950 34.298 1.00 5.99 ? 331 HIS A O 1 ATOM 1866 C CB . HIS A 1 249 ? 23.565 59.914 37.060 1.00 7.13 ? 331 HIS A CB 1 ATOM 1867 C CG . HIS A 1 249 ? 23.135 60.088 38.480 1.00 7.13 ? 331 HIS A CG 1 ATOM 1868 N ND1 . HIS A 1 249 ? 22.120 60.943 38.846 1.00 7.13 ? 331 HIS A ND1 1 ATOM 1869 C CD2 . HIS A 1 249 ? 23.532 59.467 39.613 1.00 7.13 ? 331 HIS A CD2 1 ATOM 1870 C CE1 . HIS A 1 249 ? 21.903 60.837 40.145 1.00 7.13 ? 331 HIS A CE1 1 ATOM 1871 N NE2 . HIS A 1 249 ? 22.748 59.946 40.633 1.00 7.13 ? 331 HIS A NE2 1 ATOM 1872 N N . ALA A 1 250 ? 23.581 58.187 34.134 1.00 9.94 ? 332 ALA A N 1 ATOM 1873 C CA . ALA A 1 250 ? 23.687 58.268 32.686 1.00 9.94 ? 332 ALA A CA 1 ATOM 1874 C C . ALA A 1 250 ? 22.554 57.467 32.047 1.00 9.94 ? 332 ALA A C 1 ATOM 1875 O O . ALA A 1 250 ? 21.894 57.941 31.131 1.00 9.94 ? 332 ALA A O 1 ATOM 1876 C CB . ALA A 1 250 ? 25.037 57.727 32.220 1.00 5.98 ? 332 ALA A CB 1 ATOM 1877 N N . ILE A 1 251 ? 22.306 56.265 32.561 1.00 9.10 ? 333 ILE A N 1 ATOM 1878 C CA . ILE A 1 251 ? 21.274 55.406 32.005 1.00 9.10 ? 333 ILE A CA 1 ATOM 1879 C C . ILE A 1 251 ? 19.854 55.734 32.481 1.00 9.10 ? 333 ILE A C 1 ATOM 1880 O O . ILE A 1 251 ? 18.884 55.468 31.771 1.00 9.10 ? 333 ILE A O 1 ATOM 1881 C CB . ILE A 1 251 ? 21.628 53.905 32.221 1.00 18.77 ? 333 ILE A CB 1 ATOM 1882 C CG1 . ILE A 1 251 ? 20.819 53.024 31.270 1.00 18.77 ? 333 ILE A CG1 1 ATOM 1883 C CG2 . ILE A 1 251 ? 21.395 53.491 33.661 1.00 18.77 ? 333 ILE A CG2 1 ATOM 1884 C CD1 . ILE A 1 251 ? 21.221 51.560 31.280 1.00 18.77 ? 333 ILE A CD1 1 ATOM 1885 N N . GLY A 1 252 ? 19.743 56.381 33.639 1.00 8.23 ? 334 GLY A N 1 ATOM 1886 C CA . GLY A 1 252 ? 18.442 56.735 34.183 1.00 8.23 ? 334 GLY A CA 1 ATOM 1887 C C . GLY A 1 252 ? 17.572 57.520 33.214 1.00 8.23 ? 334 GLY A C 1 ATOM 1888 O O . GLY A 1 252 ? 16.459 57.094 32.888 1.00 8.23 ? 334 GLY A O 1 ATOM 1889 N N . PRO A 1 253 ? 18.029 58.706 32.780 1.00 12.52 ? 335 PRO A N 1 ATOM 1890 C CA . PRO A 1 253 ? 17.256 59.524 31.841 1.00 12.52 ? 335 PRO A CA 1 ATOM 1891 C C . PRO A 1 253 ? 16.994 58.834 30.499 1.00 12.52 ? 335 PRO A C 1 ATOM 1892 O O . PRO A 1 253 ? 15.976 59.096 29.854 1.00 12.52 ? 335 PRO A O 1 ATOM 1893 C CB . PRO A 1 253 ? 18.113 60.784 31.684 1.00 10.20 ? 335 PRO A CB 1 ATOM 1894 C CG . PRO A 1 253 ? 19.469 60.397 32.211 1.00 10.20 ? 335 PRO A CG 1 ATOM 1895 C CD . PRO A 1 253 ? 19.167 59.459 33.324 1.00 10.20 ? 335 PRO A CD 1 ATOM 1896 N N . LEU A 1 254 ? 17.896 57.943 30.090 1.00 9.05 ? 336 LEU A N 1 ATOM 1897 C CA . LEU A 1 254 ? 17.730 57.223 28.829 1.00 9.05 ? 336 LEU A CA 1 ATOM 1898 C C . LEU A 1 254 ? 16.565 56.239 28.925 1.00 9.05 ? 336 LEU A C 1 ATOM 1899 O O . LEU A 1 254 ? 15.834 56.039 27.952 1.00 9.05 ? 336 LEU A O 1 ATOM 1900 C CB . LEU A 1 254 ? 19.017 56.491 28.433 1.00 8.49 ? 336 LEU A CB 1 ATOM 1901 C CG . LEU A 1 254 ? 20.271 57.353 28.227 1.00 8.49 ? 336 LEU A CG 1 ATOM 1902 C CD1 . LEU A 1 254 ? 21.423 56.466 27.790 1.00 8.49 ? 336 LEU A CD1 1 ATOM 1903 C CD2 . LEU A 1 254 ? 20.015 58.447 27.190 1.00 8.49 ? 336 LEU A CD2 1 ATOM 1904 N N . LEU A 1 255 ? 16.388 55.629 30.095 1.00 7.84 ? 337 LEU A N 1 ATOM 1905 C CA . LEU A 1 255 ? 15.281 54.695 30.302 1.00 7.84 ? 337 LEU A CA 1 ATOM 1906 C C . LEU A 1 255 ? 13.976 55.475 30.150 1.00 7.84 ? 337 LEU A C 1 ATOM 1907 O O . LEU A 1 255 ? 13.029 55.008 29.511 1.00 7.84 ? 337 LEU A O 1 ATOM 1908 C CB . LEU A 1 255 ? 15.348 54.064 31.697 1.00 9.01 ? 337 LEU A CB 1 ATOM 1909 C CG . LEU A 1 255 ? 16.435 53.020 31.983 1.00 9.01 ? 337 LEU A CG 1 ATOM 1910 C CD1 . LEU A 1 255 ? 16.565 52.826 33.483 1.00 9.01 ? 337 LEU A CD1 1 ATOM 1911 C CD2 . LEU A 1 255 ? 16.106 51.700 31.295 1.00 9.01 ? 337 LEU A CD2 1 ATOM 1912 N N . ALA A 1 256 ? 13.952 56.682 30.715 1.00 13.62 ? 338 ALA A N 1 ATOM 1913 C CA . ALA A 1 256 ? 12.785 57.555 30.644 1.00 13.62 ? 338 ALA A CA 1 ATOM 1914 C C . ALA A 1 256 ? 12.471 57.880 29.188 1.00 13.62 ? 338 ALA A C 1 ATOM 1915 O O . ALA A 1 256 ? 11.309 57.871 28.781 1.00 13.62 ? 338 ALA A O 1 ATOM 1916 C CB . ALA A 1 256 ? 13.036 58.829 31.427 1.00 6.14 ? 338 ALA A CB 1 ATOM 1917 N N . ASN A 1 257 ? 13.514 58.131 28.400 1.00 15.09 ? 339 ASN A N 1 ATOM 1918 C CA . ASN A 1 257 ? 13.347 58.434 26.982 1.00 15.09 ? 339 ASN A CA 1 ATOM 1919 C C . ASN A 1 257 ? 12.748 57.257 26.229 1.00 15.09 ? 339 ASN A C 1 ATOM 1920 O O . ASN A 1 257 ? 12.094 57.441 25.205 1.00 15.09 ? 339 ASN A O 1 ATOM 1921 C CB . ASN A 1 257 ? 14.686 58.794 26.332 1.00 23.89 ? 339 ASN A CB 1 ATOM 1922 C CG . ASN A 1 257 ? 15.197 60.158 26.750 1.00 23.89 ? 339 ASN A CG 1 ATOM 1923 O OD1 . ASN A 1 257 ? 16.395 60.434 26.650 1.00 23.89 ? 339 ASN A OD1 1 ATOM 1924 N ND2 . ASN A 1 257 ? 14.295 61.027 27.201 1.00 23.89 ? 339 ASN A ND2 1 ATOM 1925 N N . HIS A 1 258 ? 12.959 56.050 26.746 1.00 13.74 ? 340 HIS A N 1 ATOM 1926 C CA . HIS A 1 258 ? 12.455 54.846 26.102 1.00 13.74 ? 340 HIS A CA 1 ATOM 1927 C C . HIS A 1 258 ? 11.174 54.246 26.669 1.00 13.74 ? 340 HIS A C 1 ATOM 1928 O O . HIS A 1 258 ? 10.833 53.106 26.355 1.00 13.74 ? 340 HIS A O 1 ATOM 1929 C CB . HIS A 1 258 ? 13.559 53.796 26.036 1.00 12.76 ? 340 HIS A CB 1 ATOM 1930 C CG . HIS A 1 258 ? 14.661 54.154 25.095 1.00 12.76 ? 340 HIS A CG 1 ATOM 1931 N ND1 . HIS A 1 258 ? 14.479 54.210 23.730 1.00 12.76 ? 340 HIS A ND1 1 ATOM 1932 C CD2 . HIS A 1 258 ? 15.951 54.501 25.318 1.00 12.76 ? 340 HIS A CD2 1 ATOM 1933 C CE1 . HIS A 1 258 ? 15.609 54.578 23.151 1.00 12.76 ? 340 HIS A CE1 1 ATOM 1934 N NE2 . HIS A 1 258 ? 16.517 54.760 24.092 1.00 12.76 ? 340 HIS A NE2 1 ATOM 1935 N N . GLY A 1 259 ? 10.471 54.995 27.512 1.00 12.56 ? 341 GLY A N 1 ATOM 1936 C CA . GLY A 1 259 ? 9.221 54.490 28.052 1.00 12.56 ? 341 GLY A CA 1 ATOM 1937 C C . GLY A 1 259 ? 9.184 54.035 29.497 1.00 12.56 ? 341 GLY A C 1 ATOM 1938 O O . GLY A 1 259 ? 8.103 53.766 30.023 1.00 12.56 ? 341 GLY A O 1 ATOM 1939 N N . TRP A 1 260 ? 10.346 53.903 30.134 1.00 14.47 ? 342 TRP A N 1 ATOM 1940 C CA . TRP A 1 260 ? 10.387 53.485 31.529 1.00 14.47 ? 342 TRP A CA 1 ATOM 1941 C C . TRP A 1 260 ? 10.762 54.666 32.419 1.00 14.47 ? 342 TRP A C 1 ATOM 1942 O O . TRP A 1 260 ? 11.941 54.932 32.664 1.00 14.47 ? 342 TRP A O 1 ATOM 1943 C CB . TRP A 1 260 ? 11.371 52.324 31.735 1.00 6.17 ? 342 TRP A CB 1 ATOM 1944 C CG . TRP A 1 260 ? 11.331 51.709 33.130 1.00 6.17 ? 342 TRP A CG 1 ATOM 1945 C CD1 . TRP A 1 260 ? 10.622 52.159 34.213 1.00 6.17 ? 342 TRP A CD1 1 ATOM 1946 C CD2 . TRP A 1 260 ? 12.015 50.526 33.569 1.00 6.17 ? 342 TRP A CD2 1 ATOM 1947 N NE1 . TRP A 1 260 ? 10.822 51.329 35.292 1.00 6.17 ? 342 TRP A NE1 1 ATOM 1948 C CE2 . TRP A 1 260 ? 11.671 50.319 34.925 1.00 6.17 ? 342 TRP A CE2 1 ATOM 1949 C CE3 . TRP A 1 260 ? 12.884 49.620 32.946 1.00 6.17 ? 342 TRP A CE3 1 ATOM 1950 C CZ2 . TRP A 1 260 ? 12.164 49.243 35.670 1.00 6.17 ? 342 TRP A CZ2 1 ATOM 1951 C CZ3 . TRP A 1 260 ? 13.374 48.550 33.688 1.00 6.17 ? 342 TRP A CZ3 1 ATOM 1952 C CH2 . TRP A 1 260 ? 13.011 48.373 35.036 1.00 6.17 ? 342 TRP A CH2 1 ATOM 1953 N N . SER A 1 261 ? 9.748 55.389 32.873 1.00 17.28 ? 343 SER A N 1 ATOM 1954 C CA . SER A 1 261 ? 9.958 56.524 33.755 1.00 17.28 ? 343 SER A CA 1 ATOM 1955 C C . SER A 1 261 ? 9.911 56.023 35.193 1.00 17.28 ? 343 SER A C 1 ATOM 1956 O O . SER A 1 261 ? 9.330 54.969 35.477 1.00 17.28 ? 343 SER A O 1 ATOM 1957 C CB . SER A 1 261 ? 8.871 57.580 33.545 1.00 35.11 ? 343 SER A CB 1 ATOM 1958 O OG . SER A 1 261 ? 8.969 58.161 32.259 1.00 35.11 ? 343 SER A OG 1 ATOM 1959 N N . ASN A 1 262 ? 10.550 56.764 36.091 1.00 10.26 ? 344 ASN A N 1 ATOM 1960 C CA . ASN A 1 262 ? 10.562 56.420 37.512 1.00 10.26 ? 344 ASN A CA 1 ATOM 1961 C C . ASN A 1 262 ? 11.262 55.110 37.847 1.00 10.26 ? 344 ASN A C 1 ATOM 1962 O O . ASN A 1 262 ? 10.806 54.353 38.708 1.00 10.26 ? 344 ASN A O 1 ATOM 1963 C CB . ASN A 1 262 ? 9.139 56.413 38.077 1.00 56.90 ? 344 ASN A CB 1 ATOM 1964 C CG . ASN A 1 262 ? 8.485 57.772 38.005 1.00 56.90 ? 344 ASN A CG 1 ATOM 1965 O OD1 . ASN A 1 262 ? 8.972 58.737 38.598 1.00 56.90 ? 344 ASN A OD1 1 ATOM 1966 N ND2 . ASN A 1 262 ? 7.384 57.864 37.263 1.00 56.90 ? 344 ASN A ND2 1 ATOM 1967 N N . ALA A 1 263 ? 12.351 54.830 37.141 1.00 7.63 ? 345 ALA A N 1 ATOM 1968 C CA . ALA A 1 263 ? 13.132 53.629 37.408 1.00 7.63 ? 345 ALA A CA 1 ATOM 1969 C C . ALA A 1 263 ? 14.173 54.014 38.458 1.00 7.63 ? 345 ALA A C 1 ATOM 1970 O O . ALA A 1 263 ? 14.800 55.070 38.359 1.00 7.63 ? 345 ALA A O 1 ATOM 1971 C CB . ALA A 1 263 ? 13.818 53.148 36.139 1.00 3.79 ? 345 ALA A CB 1 ATOM 1972 N N . PHE A 1 264 ? 14.296 53.194 39.497 1.00 6.60 ? 346 PHE A N 1 ATOM 1973 C CA . PHE A 1 264 ? 15.264 53.434 40.551 1.00 6.60 ? 346 PHE A CA 1 ATOM 1974 C C . PHE A 1 264 ? 16.287 52.312 40.575 1.00 6.60 ? 346 PHE A C 1 ATOM 1975 O O . PHE A 1 264 ? 16.116 51.302 39.896 1.00 6.60 ? 346 PHE A O 1 ATOM 1976 C CB . PHE A 1 264 ? 14.573 53.622 41.895 1.00 7.91 ? 346 PHE A CB 1 ATOM 1977 C CG . PHE A 1 264 ? 13.818 54.914 41.994 1.00 7.91 ? 346 PHE A CG 1 ATOM 1978 C CD1 . PHE A 1 264 ? 12.496 54.996 41.564 1.00 7.91 ? 346 PHE A CD1 1 ATOM 1979 C CD2 . PHE A 1 264 ? 14.441 56.065 42.473 1.00 7.91 ? 346 PHE A CD2 1 ATOM 1980 C CE1 . PHE A 1 264 ? 11.803 56.206 41.607 1.00 7.91 ? 346 PHE A CE1 1 ATOM 1981 C CE2 . PHE A 1 264 ? 13.756 57.279 42.522 1.00 7.91 ? 346 PHE A CE2 1 ATOM 1982 C CZ . PHE A 1 264 ? 12.434 57.349 42.084 1.00 7.91 ? 346 PHE A CZ 1 ATOM 1983 N N . PHE A 1 265 ? 17.344 52.481 41.368 1.00 6.41 ? 347 PHE A N 1 ATOM 1984 C CA . PHE A 1 265 ? 18.423 51.503 41.398 1.00 6.41 ? 347 PHE A CA 1 ATOM 1985 C C . PHE A 1 265 ? 18.924 51.080 42.771 1.00 6.41 ? 347 PHE A C 1 ATOM 1986 O O . PHE A 1 265 ? 18.675 51.745 43.772 1.00 6.41 ? 347 PHE A O 1 ATOM 1987 C CB . PHE A 1 265 ? 19.642 52.088 40.664 1.00 5.39 ? 347 PHE A CB 1 ATOM 1988 C CG . PHE A 1 265 ? 19.351 52.602 39.281 1.00 5.39 ? 347 PHE A CG 1 ATOM 1989 C CD1 . PHE A 1 265 ? 18.681 53.811 39.094 1.00 5.39 ? 347 PHE A CD1 1 ATOM 1990 C CD2 . PHE A 1 265 ? 19.780 51.897 38.164 1.00 5.39 ? 347 PHE A CD2 1 ATOM 1991 C CE1 . PHE A 1 265 ? 18.443 54.307 37.813 1.00 5.39 ? 347 PHE A CE1 1 ATOM 1992 C CE2 . PHE A 1 265 ? 19.548 52.386 36.878 1.00 5.39 ? 347 PHE A CE2 1 ATOM 1993 C CZ . PHE A 1 265 ? 18.879 53.593 36.705 1.00 5.39 ? 347 PHE A CZ 1 ATOM 1994 N N . ILE A 1 266 ? 19.625 49.945 42.792 1.00 4.23 ? 348 ILE A N 1 ATOM 1995 C CA . ILE A 1 266 ? 20.307 49.435 43.985 1.00 4.23 ? 348 ILE A CA 1 ATOM 1996 C C . ILE A 1 266 ? 21.670 49.025 43.440 1.00 4.23 ? 348 ILE A C 1 ATOM 1997 O O . ILE A 1 266 ? 21.787 48.651 42.267 1.00 4.23 ? 348 ILE A O 1 ATOM 1998 C CB . ILE A 1 266 ? 19.619 48.246 44.698 1.00 2.00 ? 348 ILE A CB 1 ATOM 1999 C CG1 . ILE A 1 266 ? 19.399 47.068 43.753 1.00 2.00 ? 348 ILE A CG1 1 ATOM 2000 C CG2 . ILE A 1 266 ? 18.349 48.706 45.373 1.00 2.00 ? 348 ILE A CG2 1 ATOM 2001 C CD1 . ILE A 1 266 ? 18.872 45.829 44.467 1.00 2.00 ? 348 ILE A CD1 1 ATOM 2002 N N . THR A 1 267 ? 22.707 49.164 44.257 1.00 4.23 ? 349 THR A N 1 ATOM 2003 C CA . THR A 1 267 ? 24.060 48.846 43.818 1.00 4.23 ? 349 THR A CA 1 ATOM 2004 C C . THR A 1 267 ? 24.821 47.993 44.815 1.00 4.23 ? 349 THR A C 1 ATOM 2005 O O . THR A 1 267 ? 24.856 48.300 46.002 1.00 4.23 ? 349 THR A O 1 ATOM 2006 C CB . THR A 1 267 ? 24.862 50.141 43.558 1.00 18.85 ? 349 THR A CB 1 ATOM 2007 O OG1 . THR A 1 267 ? 24.190 50.919 42.562 1.00 18.85 ? 349 THR A OG1 1 ATOM 2008 C CG2 . THR A 1 267 ? 26.256 49.831 43.063 1.00 18.85 ? 349 THR A CG2 1 ATOM 2009 N N . ASP A 1 268 ? 25.443 46.931 44.315 1.00 2.00 ? 350 ASP A N 1 ATOM 2010 C CA . ASP A 1 268 ? 26.227 46.023 45.146 1.00 2.00 ? 350 ASP A CA 1 ATOM 2011 C C . ASP A 1 268 ? 27.546 46.710 45.539 1.00 2.00 ? 350 ASP A C 1 ATOM 2012 O O . ASP A 1 268 ? 28.246 47.259 44.687 1.00 2.00 ? 350 ASP A O 1 ATOM 2013 C CB . ASP A 1 268 ? 26.512 44.728 44.363 1.00 2.00 ? 350 ASP A CB 1 ATOM 2014 C CG . ASP A 1 268 ? 26.937 43.561 45.256 1.00 2.00 ? 350 ASP A CG 1 ATOM 2015 O OD1 . ASP A 1 268 ? 27.210 43.768 46.455 1.00 2.00 ? 350 ASP A OD1 1 ATOM 2016 O OD2 . ASP A 1 268 ? 26.994 42.419 44.750 1.00 2.00 ? 350 ASP A OD2 1 ATOM 2017 N N . GLN A 1 269 ? 27.858 46.712 46.832 1.00 2.00 ? 351 GLN A N 1 ATOM 2018 C CA . GLN A 1 269 ? 29.101 47.307 47.328 1.00 2.00 ? 351 GLN A CA 1 ATOM 2019 C C . GLN A 1 269 ? 29.810 46.347 48.281 1.00 2.00 ? 351 GLN A C 1 ATOM 2020 O O . GLN A 1 269 ? 30.786 46.720 48.926 1.00 2.00 ? 351 GLN A O 1 ATOM 2021 C CB . GLN A 1 269 ? 28.842 48.644 48.045 1.00 6.72 ? 351 GLN A CB 1 ATOM 2022 C CG . GLN A 1 269 ? 28.506 49.825 47.133 1.00 6.72 ? 351 GLN A CG 1 ATOM 2023 C CD . GLN A 1 269 ? 29.651 50.215 46.202 1.00 6.72 ? 351 GLN A CD 1 ATOM 2024 O OE1 . GLN A 1 269 ? 30.578 50.918 46.602 1.00 6.72 ? 351 GLN A OE1 1 ATOM 2025 N NE2 . GLN A 1 269 ? 29.579 49.771 44.951 1.00 6.72 ? 351 GLN A NE2 1 ATOM 2026 N N . GLY A 1 270 ? 29.330 45.105 48.332 1.00 4.35 ? 352 GLY A N 1 ATOM 2027 C CA . GLY A 1 270 ? 29.897 44.090 49.205 1.00 4.35 ? 352 GLY A CA 1 ATOM 2028 C C . GLY A 1 270 ? 31.381 43.810 49.059 1.00 4.35 ? 352 GLY A C 1 ATOM 2029 O O . GLY A 1 270 ? 32.023 43.378 50.015 1.00 4.35 ? 352 GLY A O 1 ATOM 2030 N N . ARG A 1 271 ? 31.932 44.035 47.869 1.00 5.02 ? 353 ARG A N 1 ATOM 2031 C CA . ARG A 1 271 ? 33.356 43.804 47.639 1.00 5.02 ? 353 ARG A CA 1 ATOM 2032 C C . ARG A 1 271 ? 33.994 45.014 46.953 1.00 5.02 ? 353 ARG A C 1 ATOM 2033 O O . ARG A 1 271 ? 34.947 44.873 46.190 1.00 5.02 ? 353 ARG A O 1 ATOM 2034 C CB . ARG A 1 271 ? 33.563 42.524 46.808 1.00 7.04 ? 353 ARG A CB 1 ATOM 2035 C CG . ARG A 1 271 ? 32.997 41.261 47.475 1.00 7.04 ? 353 ARG A CG 1 ATOM 2036 C CD . ARG A 1 271 ? 33.421 39.973 46.785 1.00 7.04 ? 353 ARG A CD 1 ATOM 2037 N NE . ARG A 1 271 ? 32.863 39.828 45.441 1.00 7.04 ? 353 ARG A NE 1 ATOM 2038 C CZ . ARG A 1 271 ? 33.075 38.779 44.653 1.00 7.04 ? 353 ARG A CZ 1 ATOM 2039 N NH1 . ARG A 1 271 ? 33.832 37.773 45.067 1.00 7.04 ? 353 ARG A NH1 1 ATOM 2040 N NH2 . ARG A 1 271 ? 32.533 38.732 43.448 1.00 7.04 ? 353 ARG A NH2 1 ATOM 2041 N N . SER A 1 272 ? 33.506 46.207 47.291 1.00 3.23 ? 354 SER A N 1 ATOM 2042 C CA . SER A 1 272 ? 33.990 47.452 46.691 1.00 3.23 ? 354 SER A CA 1 ATOM 2043 C C . SER A 1 272 ? 34.749 48.407 47.616 1.00 3.23 ? 354 SER A C 1 ATOM 2044 O O . SER A 1 272 ? 35.169 49.478 47.177 1.00 3.23 ? 354 SER A O 1 ATOM 2045 C CB . SER A 1 272 ? 32.817 48.213 46.065 1.00 3.09 ? 354 SER A CB 1 ATOM 2046 O OG . SER A 1 272 ? 32.142 47.427 45.104 1.00 3.09 ? 354 SER A OG 1 ATOM 2047 N N . GLY A 1 273 ? 34.957 48.001 48.868 1.00 7.81 ? 355 GLY A N 1 ATOM 2048 C CA . GLY A 1 273 ? 35.636 48.838 49.850 1.00 7.81 ? 355 GLY A CA 1 ATOM 2049 C C . GLY A 1 273 ? 37.036 49.333 49.541 1.00 7.81 ? 355 GLY A C 1 ATOM 2050 O O . GLY A 1 273 ? 37.411 50.435 49.955 1.00 7.81 ? 355 GLY A O 1 ATOM 2051 N N . LYS A 1 274 ? 37.822 48.533 48.828 1.00 6.97 ? 356 LYS A N 1 ATOM 2052 C CA . LYS A 1 274 ? 39.180 48.942 48.492 1.00 6.97 ? 356 LYS A CA 1 ATOM 2053 C C . LYS A 1 274 ? 39.261 49.358 47.034 1.00 6.97 ? 356 LYS A C 1 ATOM 2054 O O . LYS A 1 274 ? 39.016 48.556 46.133 1.00 6.97 ? 356 LYS A O 1 ATOM 2055 C CB . LYS A 1 274 ? 40.171 47.815 48.776 1.00 19.76 ? 356 LYS A CB 1 ATOM 2056 C CG . LYS A 1 274 ? 41.611 48.276 48.816 1.00 19.76 ? 356 LYS A CG 1 ATOM 2057 C CD . LYS A 1 274 ? 42.534 47.122 49.110 1.00 19.76 ? 356 LYS A CD 1 ATOM 2058 C CE . LYS A 1 274 ? 43.912 47.610 49.516 1.00 19.76 ? 356 LYS A CE 1 ATOM 2059 N NZ . LYS A 1 274 ? 44.572 48.413 48.453 1.00 19.76 ? 356 LYS A NZ 1 ATOM 2060 N N . GLN A 1 275 ? 39.605 50.622 46.816 1.00 11.15 ? 357 GLN A N 1 ATOM 2061 C CA . GLN A 1 275 ? 39.715 51.182 45.476 1.00 11.15 ? 357 GLN A CA 1 ATOM 2062 C C . GLN A 1 275 ? 41.038 51.927 45.310 1.00 11.15 ? 357 GLN A C 1 ATOM 2063 O O . GLN A 1 275 ? 41.441 52.689 46.188 1.00 11.15 ? 357 GLN A O 1 ATOM 2064 C CB . GLN A 1 275 ? 38.558 52.147 45.216 1.00 6.24 ? 357 GLN A CB 1 ATOM 2065 C CG . GLN A 1 275 ? 37.172 51.524 45.315 1.00 6.24 ? 357 GLN A CG 1 ATOM 2066 C CD . GLN A 1 275 ? 36.880 50.552 44.186 1.00 6.24 ? 357 GLN A CD 1 ATOM 2067 O OE1 . GLN A 1 275 ? 37.473 50.632 43.108 1.00 6.24 ? 357 GLN A OE1 1 ATOM 2068 N NE2 . GLN A 1 275 ? 35.949 49.641 44.422 1.00 6.24 ? 357 GLN A NE2 1 ATOM 2069 N N . PRO A 1 276 ? 41.754 51.677 44.203 1.00 11.32 ? 358 PRO A N 1 ATOM 2070 C CA . PRO A 1 276 ? 41.367 50.734 43.152 1.00 11.32 ? 358 PRO A CA 1 ATOM 2071 C C . PRO A 1 276 ? 41.593 49.308 43.619 1.00 11.32 ? 358 PRO A C 1 ATOM 2072 O O . PRO A 1 276 ? 42.290 49.073 44.604 1.00 11.32 ? 358 PRO A O 1 ATOM 2073 C CB . PRO A 1 276 ? 42.310 51.097 42.006 1.00 14.81 ? 358 PRO A CB 1 ATOM 2074 C CG . PRO A 1 276 ? 43.529 51.571 42.707 1.00 14.81 ? 358 PRO A CG 1 ATOM 2075 C CD . PRO A 1 276 ? 42.975 52.412 43.824 1.00 14.81 ? 358 PRO A CD 1 ATOM 2076 N N . THR A 1 277 ? 40.974 48.357 42.933 1.00 14.08 ? 359 THR A N 1 ATOM 2077 C CA . THR A 1 277 ? 41.129 46.955 43.288 1.00 14.08 ? 359 THR A CA 1 ATOM 2078 C C . THR A 1 277 ? 42.435 46.418 42.689 1.00 14.08 ? 359 THR A C 1 ATOM 2079 O O . THR A 1 277 ? 43.237 47.184 42.152 1.00 14.08 ? 359 THR A O 1 ATOM 2080 C CB . THR A 1 277 ? 39.956 46.128 42.739 1.00 5.87 ? 359 THR A CB 1 ATOM 2081 O OG1 . THR A 1 277 ? 40.069 46.048 41.314 1.00 5.87 ? 359 THR A OG1 1 ATOM 2082 C CG2 . THR A 1 277 ? 38.624 46.786 43.091 1.00 5.87 ? 359 THR A CG2 1 ATOM 2083 N N . GLY A 1 278 ? 42.635 45.105 42.781 1.00 10.52 ? 360 GLY A N 1 ATOM 2084 C CA . GLY A 1 278 ? 43.825 44.491 42.220 1.00 10.52 ? 360 GLY A CA 1 ATOM 2085 C C . GLY A 1 278 ? 43.608 44.005 40.796 1.00 10.52 ? 360 GLY A C 1 ATOM 2086 O O . GLY A 1 278 ? 44.418 43.241 40.266 1.00 10.52 ? 360 GLY A O 1 ATOM 2087 N N . GLN A 1 279 ? 42.516 44.444 40.173 1.00 6.51 ? 361 GLN A N 1 ATOM 2088 C CA . GLN A 1 279 ? 42.197 44.052 38.799 1.00 6.51 ? 361 GLN A CA 1 ATOM 2089 C C . GLN A 1 279 ? 43.232 44.578 37.816 1.00 6.51 ? 361 GLN A C 1 ATOM 2090 O O . GLN A 1 279 ? 43.551 45.763 37.816 1.00 6.51 ? 361 GLN A O 1 ATOM 2091 C CB . GLN A 1 279 ? 40.819 44.582 38.384 1.00 10.95 ? 361 GLN A CB 1 ATOM 2092 C CG . GLN A 1 279 ? 39.646 43.767 38.890 1.00 10.95 ? 361 GLN A CG 1 ATOM 2093 C CD . GLN A 1 279 ? 38.313 44.471 38.699 1.00 10.95 ? 361 GLN A CD 1 ATOM 2094 O OE1 . GLN A 1 279 ? 37.408 43.950 38.043 1.00 10.95 ? 361 GLN A OE1 1 ATOM 2095 N NE2 . GLN A 1 279 ? 38.184 45.659 39.277 1.00 10.95 ? 361 GLN A NE2 1 ATOM 2096 N N . GLN A 1 280 ? 43.788 43.684 37.010 1.00 16.70 ? 362 GLN A N 1 ATOM 2097 C CA . GLN A 1 280 ? 44.760 44.080 36.005 1.00 16.70 ? 362 GLN A CA 1 ATOM 2098 C C . GLN A 1 280 ? 43.984 44.565 34.783 1.00 16.70 ? 362 GLN A C 1 ATOM 2099 O O . GLN A 1 280 ? 44.443 45.427 34.037 1.00 16.70 ? 362 GLN A O 1 ATOM 2100 C CB . GLN A 1 280 ? 45.710 42.921 35.691 1.00 44.99 ? 362 GLN A CB 1 ATOM 2101 C CG . GLN A 1 280 ? 46.837 42.812 36.728 1.00 44.99 ? 362 GLN A CG 1 ATOM 2102 C CD . GLN A 1 280 ? 47.449 41.424 36.841 1.00 44.99 ? 362 GLN A CD 1 ATOM 2103 O OE1 . GLN A 1 280 ? 47.536 40.681 35.859 1.00 44.99 ? 362 GLN A OE1 1 ATOM 2104 N NE2 . GLN A 1 280 ? 47.881 41.070 38.052 1.00 44.99 ? 362 GLN A NE2 1 ATOM 2105 N N . GLN A 1 281 ? 42.765 44.053 34.640 1.00 10.54 ? 363 GLN A N 1 ATOM 2106 C CA . GLN A 1 281 ? 41.865 44.435 33.557 1.00 10.54 ? 363 GLN A CA 1 ATOM 2107 C C . GLN A 1 281 ? 40.456 44.506 34.133 1.00 10.54 ? 363 GLN A C 1 ATOM 2108 O O . GLN A 1 281 ? 40.101 43.715 35.001 1.00 10.54 ? 363 GLN A O 1 ATOM 2109 C CB . GLN A 1 281 ? 41.944 43.443 32.395 1.00 110.20 ? 363 GLN A CB 1 ATOM 2110 C CG . GLN A 1 281 ? 43.240 43.565 31.609 1.00 110.20 ? 363 GLN A CG 1 ATOM 2111 C CD . GLN A 1 281 ? 43.320 42.630 30.424 1.00 110.20 ? 363 GLN A CD 1 ATOM 2112 O OE1 . GLN A 1 281 ? 42.328 42.021 30.021 1.00 110.20 ? 363 GLN A OE1 1 ATOM 2113 N NE2 . GLN A 1 281 ? 44.513 42.514 29.852 1.00 110.20 ? 363 GLN A NE2 1 ATOM 2114 N N . TRP A 1 282 ? 39.673 45.476 33.670 1.00 8.92 ? 364 TRP A N 1 ATOM 2115 C CA . TRP A 1 282 ? 38.304 45.678 34.150 1.00 8.92 ? 364 TRP A CA 1 ATOM 2116 C C . TRP A 1 282 ? 37.414 44.445 33.982 1.00 8.92 ? 364 TRP A C 1 ATOM 2117 O O . TRP A 1 282 ? 36.524 44.198 34.794 1.00 8.92 ? 364 TRP A O 1 ATOM 2118 C CB . TRP A 1 282 ? 37.670 46.874 33.429 1.00 6.90 ? 364 TRP A CB 1 ATOM 2119 C CG . TRP A 1 282 ? 36.693 47.673 34.256 1.00 6.90 ? 364 TRP A CG 1 ATOM 2120 C CD1 . TRP A 1 282 ? 36.228 47.377 35.516 1.00 6.90 ? 364 TRP A CD1 1 ATOM 2121 C CD2 . TRP A 1 282 ? 36.098 48.926 33.895 1.00 6.90 ? 364 TRP A CD2 1 ATOM 2122 N NE1 . TRP A 1 282 ? 35.392 48.375 35.957 1.00 6.90 ? 364 TRP A NE1 1 ATOM 2123 C CE2 . TRP A 1 282 ? 35.291 49.337 34.985 1.00 6.90 ? 364 TRP A CE2 1 ATOM 2124 C CE3 . TRP A 1 282 ? 36.171 49.745 32.759 1.00 6.90 ? 364 TRP A CE3 1 ATOM 2125 C CZ2 . TRP A 1 282 ? 34.564 50.536 34.969 1.00 6.90 ? 364 TRP A CZ2 1 ATOM 2126 C CZ3 . TRP A 1 282 ? 35.446 50.938 32.743 1.00 6.90 ? 364 TRP A CZ3 1 ATOM 2127 C CH2 . TRP A 1 282 ? 34.653 51.320 33.844 1.00 6.90 ? 364 TRP A CH2 1 ATOM 2128 N N . GLY A 1 283 ? 37.677 43.664 32.941 1.00 11.48 ? 365 GLY A N 1 ATOM 2129 C CA . GLY A 1 283 ? 36.886 42.475 32.677 1.00 11.48 ? 365 GLY A CA 1 ATOM 2130 C C . GLY A 1 283 ? 37.136 41.286 33.587 1.00 11.48 ? 365 GLY A C 1 ATOM 2131 O O . GLY A 1 283 ? 36.420 40.289 33.498 1.00 11.48 ? 365 GLY A O 1 ATOM 2132 N N . ASP A 1 284 ? 38.159 41.370 34.435 1.00 16.97 ? 366 ASP A N 1 ATOM 2133 C CA . ASP A 1 284 ? 38.491 40.292 35.369 1.00 16.97 ? 366 ASP A CA 1 ATOM 2134 C C . ASP A 1 284 ? 37.494 40.297 36.534 1.00 16.97 ? 366 ASP A C 1 ATOM 2135 O O . ASP A 1 284 ? 37.438 41.247 37.315 1.00 16.97 ? 366 ASP A O 1 ATOM 2136 C CB . ASP A 1 284 ? 39.935 40.456 35.856 1.00 12.95 ? 366 ASP A CB 1 ATOM 2137 C CG . ASP A 1 284 ? 40.953 40.374 34.714 1.00 12.95 ? 366 ASP A CG 1 ATOM 2138 O OD1 . ASP A 1 284 ? 40.586 39.926 33.607 1.00 12.95 ? 366 ASP A OD1 1 ATOM 2139 O OD2 . ASP A 1 284 ? 42.126 40.750 34.918 1.00 12.95 ? 366 ASP A OD2 1 ATOM 2140 N N . TRP A 1 285 ? 36.737 39.209 36.660 1.00 7.55 ? 367 TRP A N 1 ATOM 2141 C CA . TRP A 1 285 ? 35.687 39.090 37.674 1.00 7.55 ? 367 TRP A CA 1 ATOM 2142 C C . TRP A 1 285 ? 35.829 37.984 38.722 1.00 7.55 ? 367 TRP A C 1 ATOM 2143 O O . TRP A 1 285 ? 35.142 38.012 39.749 1.00 7.55 ? 367 TRP A O 1 ATOM 2144 C CB . TRP A 1 285 ? 34.351 38.871 36.958 1.00 12.79 ? 367 TRP A CB 1 ATOM 2145 C CG . TRP A 1 285 ? 34.395 37.659 36.050 1.00 12.79 ? 367 TRP A CG 1 ATOM 2146 C CD1 . TRP A 1 285 ? 34.737 37.644 34.729 1.00 12.79 ? 367 TRP A CD1 1 ATOM 2147 C CD2 . TRP A 1 285 ? 34.166 36.283 36.422 1.00 12.79 ? 367 TRP A CD2 1 ATOM 2148 N NE1 . TRP A 1 285 ? 34.746 36.353 34.256 1.00 12.79 ? 367 TRP A NE1 1 ATOM 2149 C CE2 . TRP A 1 285 ? 34.400 35.499 35.267 1.00 12.79 ? 367 TRP A CE2 1 ATOM 2150 C CE3 . TRP A 1 285 ? 33.792 35.640 37.612 1.00 12.79 ? 367 TRP A CE3 1 ATOM 2151 C CZ2 . TRP A 1 285 ? 34.275 34.100 35.270 1.00 12.79 ? 367 TRP A CZ2 1 ATOM 2152 C CZ3 . TRP A 1 285 ? 33.667 34.246 37.614 1.00 12.79 ? 367 TRP A CZ3 1 ATOM 2153 C CH2 . TRP A 1 285 ? 33.909 33.495 36.446 1.00 12.79 ? 367 TRP A CH2 1 ATOM 2154 N N . CYS A 1 286 ? 36.669 36.991 38.453 1.00 8.50 ? 368 CYS A N 1 ATOM 2155 C CA . CYS A 1 286 ? 36.814 35.863 39.373 1.00 8.50 ? 368 CYS A CA 1 ATOM 2156 C C . CYS A 1 286 ? 37.768 36.022 40.548 1.00 8.50 ? 368 CYS A C 1 ATOM 2157 O O . CYS A 1 286 ? 38.975 36.169 40.358 1.00 8.50 ? 368 CYS A O 1 ATOM 2158 C CB . CYS A 1 286 ? 37.170 34.592 38.605 1.00 10.00 ? 368 CYS A CB 1 ATOM 2159 S SG . CYS A 1 286 ? 36.912 33.093 39.591 1.00 10.00 ? 368 CYS A SG 1 ATOM 2160 N N . ASN A 1 287 ? 37.207 35.944 41.758 1.00 8.16 ? 369 ASN A N 1 ATOM 2161 C CA . ASN A 1 287 ? 37.950 36.045 43.021 1.00 8.16 ? 369 ASN A CA 1 ATOM 2162 C C . ASN A 1 287 ? 39.081 37.067 42.961 1.00 8.16 ? 369 ASN A C 1 ATOM 2163 O O . ASN A 1 287 ? 40.219 36.765 43.325 1.00 8.16 ? 369 ASN A O 1 ATOM 2164 C CB . ASN A 1 287 ? 38.532 34.676 43.410 1.00 8.86 ? 369 ASN A CB 1 ATOM 2165 C CG . ASN A 1 287 ? 37.501 33.553 43.360 1.00 8.86 ? 369 ASN A CG 1 ATOM 2166 O OD1 . ASN A 1 287 ? 36.402 33.674 43.896 1.00 8.86 ? 369 ASN A OD1 1 ATOM 2167 N ND2 . ASN A 1 287 ? 37.868 32.445 42.734 1.00 8.86 ? 369 ASN A ND2 1 ATOM 2168 N N . VAL A 1 288 ? 38.755 38.281 42.531 1.00 8.74 ? 370 VAL A N 1 ATOM 2169 C CA . VAL A 1 288 ? 39.740 39.350 42.394 1.00 8.74 ? 370 VAL A CA 1 ATOM 2170 C C . VAL A 1 288 ? 40.485 39.704 43.677 1.00 8.74 ? 370 VAL A C 1 ATOM 2171 O O . VAL A 1 288 ? 39.885 39.862 44.736 1.00 8.74 ? 370 VAL A O 1 ATOM 2172 C CB . VAL A 1 288 ? 39.098 40.609 41.772 1.00 4.03 ? 370 VAL A CB 1 ATOM 2173 C CG1 . VAL A 1 288 ? 40.084 41.763 41.745 1.00 4.03 ? 370 VAL A CG1 1 ATOM 2174 C CG2 . VAL A 1 288 ? 38.629 40.293 40.357 1.00 4.03 ? 370 VAL A CG2 1 ATOM 2175 N N . ILE A 1 289 ? 41.807 39.806 43.567 1.00 6.40 ? 371 ILE A N 1 ATOM 2176 C CA . ILE A 1 289 ? 42.664 40.137 44.701 1.00 6.40 ? 371 ILE A CA 1 ATOM 2177 C C . ILE A 1 289 ? 42.625 41.632 45.004 1.00 6.40 ? 371 ILE A C 1 ATOM 2178 O O . ILE A 1 289 ? 42.293 42.434 44.138 1.00 6.40 ? 371 ILE A O 1 ATOM 2179 C CB . ILE A 1 289 ? 44.141 39.748 44.424 1.00 22.22 ? 371 ILE A CB 1 ATOM 2180 C CG1 . ILE A 1 289 ? 44.663 40.501 43.194 1.00 22.22 ? 371 ILE A CG1 1 ATOM 2181 C CG2 . ILE A 1 289 ? 44.270 38.240 44.237 1.00 22.22 ? 371 ILE A CG2 1 ATOM 2182 C CD1 . ILE A 1 289 ? 46.139 40.307 42.915 1.00 22.22 ? 371 ILE A CD1 1 ATOM 2183 N N . GLY A 1 290 ? 42.982 41.998 46.231 1.00 5.61 ? 372 GLY A N 1 ATOM 2184 C CA . GLY A 1 290 ? 43.009 43.397 46.618 1.00 5.61 ? 372 GLY A CA 1 ATOM 2185 C C . GLY A 1 290 ? 41.658 44.059 46.793 1.00 5.61 ? 372 GLY A C 1 ATOM 2186 O O . GLY A 1 290 ? 41.500 45.251 46.505 1.00 5.61 ? 372 GLY A O 1 ATOM 2187 N N . THR A 1 291 ? 40.684 43.291 47.273 1.00 5.09 ? 373 THR A N 1 ATOM 2188 C CA . THR A 1 291 ? 39.341 43.813 47.500 1.00 5.09 ? 373 THR A CA 1 ATOM 2189 C C . THR A 1 291 ? 38.984 43.756 48.982 1.00 5.09 ? 373 THR A C 1 ATOM 2190 O O . THR A 1 291 ? 39.654 43.092 49.769 1.00 5.09 ? 373 THR A O 1 ATOM 2191 C CB . THR A 1 291 ? 38.288 43.021 46.702 1.00 4.17 ? 373 THR A CB 1 ATOM 2192 O OG1 . THR A 1 291 ? 38.283 41.655 47.140 1.00 4.17 ? 373 THR A OG1 1 ATOM 2193 C CG2 . THR A 1 291 ? 38.599 43.076 45.208 1.00 4.17 ? 373 THR A CG2 1 ATOM 2194 N N . GLY A 1 292 ? 37.929 44.467 49.357 1.00 7.05 ? 374 GLY A N 1 ATOM 2195 C CA . GLY A 1 292 ? 37.494 44.469 50.741 1.00 7.05 ? 374 GLY A CA 1 ATOM 2196 C C . GLY A 1 292 ? 36.010 44.766 50.836 1.00 7.05 ? 374 GLY A C 1 ATOM 2197 O O . GLY A 1 292 ? 35.396 45.206 49.856 1.00 7.05 ? 374 GLY A O 1 ATOM 2198 N N . PHE A 1 293 ? 35.420 44.467 51.990 1.00 6.28 ? 375 PHE A N 1 ATOM 2199 C CA . PHE A 1 293 ? 34.007 44.741 52.209 1.00 6.28 ? 375 PHE A CA 1 ATOM 2200 C C . PHE A 1 293 ? 33.831 46.252 52.051 1.00 6.28 ? 375 PHE A C 1 ATOM 2201 O O . PHE A 1 293 ? 34.697 47.031 52.468 1.00 6.28 ? 375 PHE A O 1 ATOM 2202 C CB . PHE A 1 293 ? 33.589 44.307 53.616 1.00 3.91 ? 375 PHE A CB 1 ATOM 2203 C CG . PHE A 1 293 ? 33.477 42.812 53.792 1.00 3.91 ? 375 PHE A CG 1 ATOM 2204 C CD1 . PHE A 1 293 ? 32.538 42.081 53.071 1.00 3.91 ? 375 PHE A CD1 1 ATOM 2205 C CD2 . PHE A 1 293 ? 34.283 42.145 54.709 1.00 3.91 ? 375 PHE A CD2 1 ATOM 2206 C CE1 . PHE A 1 293 ? 32.397 40.709 53.259 1.00 3.91 ? 375 PHE A CE1 1 ATOM 2207 C CE2 . PHE A 1 293 ? 34.150 40.757 54.911 1.00 3.91 ? 375 PHE A CE2 1 ATOM 2208 C CZ . PHE A 1 293 ? 33.204 40.042 54.182 1.00 3.91 ? 375 PHE A CZ 1 ATOM 2209 N N . GLY A 1 294 ? 32.723 46.665 51.443 1.00 5.89 ? 376 GLY A N 1 ATOM 2210 C CA . GLY A 1 294 ? 32.505 48.084 51.230 1.00 5.89 ? 376 GLY A CA 1 ATOM 2211 C C . GLY A 1 294 ? 31.396 48.743 52.023 1.00 5.89 ? 376 GLY A C 1 ATOM 2212 O O . GLY A 1 294 ? 31.061 48.311 53.129 1.00 5.89 ? 376 GLY A O 1 ATOM 2213 N N . ILE A 1 295 ? 30.834 49.805 51.441 1.00 9.60 ? 377 ILE A N 1 ATOM 2214 C CA . ILE A 1 295 ? 29.751 50.572 52.054 1.00 9.60 ? 377 ILE A CA 1 ATOM 2215 C C . ILE A 1 295 ? 28.652 49.624 52.529 1.00 9.60 ? 377 ILE A C 1 ATOM 2216 O O . ILE A 1 295 ? 28.198 48.768 51.771 1.00 9.60 ? 377 ILE A O 1 ATOM 2217 C CB . ILE A 1 295 ? 29.175 51.626 51.063 1.00 10.70 ? 377 ILE A CB 1 ATOM 2218 C CG1 . ILE A 1 295 ? 30.266 52.633 50.678 1.00 10.70 ? 377 ILE A CG1 1 ATOM 2219 C CG2 . ILE A 1 295 ? 28.009 52.373 51.697 1.00 10.70 ? 377 ILE A CG2 1 ATOM 2220 C CD1 . ILE A 1 295 ? 29.850 53.644 49.618 1.00 10.70 ? 377 ILE A CD1 1 ATOM 2221 N N . ARG A 1 296 ? 28.278 49.761 53.800 1.00 6.06 ? 378 ARG A N 1 ATOM 2222 C CA . ARG A 1 296 ? 27.257 48.922 54.431 1.00 6.06 ? 378 ARG A CA 1 ATOM 2223 C C . ARG A 1 296 ? 25.865 49.218 53.885 1.00 6.06 ? 378 ARG A C 1 ATOM 2224 O O . ARG A 1 296 ? 25.535 50.367 53.607 1.00 6.06 ? 378 ARG A O 1 ATOM 2225 C CB . ARG A 1 296 ? 27.243 49.149 55.950 1.00 15.97 ? 378 ARG A CB 1 ATOM 2226 C CG . ARG A 1 296 ? 28.607 49.128 56.628 1.00 15.97 ? 378 ARG A CG 1 ATOM 2227 C CD . ARG A 1 296 ? 29.161 47.724 56.802 1.00 15.97 ? 378 ARG A CD 1 ATOM 2228 N NE . ARG A 1 296 ? 30.550 47.758 57.261 1.00 15.97 ? 378 ARG A NE 1 ATOM 2229 C CZ . ARG A 1 296 ? 30.932 47.950 58.521 1.00 15.97 ? 378 ARG A CZ 1 ATOM 2230 N NH1 . ARG A 1 296 ? 30.033 48.090 59.487 1.00 15.97 ? 378 ARG A NH1 1 ATOM 2231 N NH2 . ARG A 1 296 ? 32.223 47.969 58.823 1.00 15.97 ? 378 ARG A NH2 1 ATOM 2232 N N . PRO A 1 297 ? 25.015 48.181 53.771 1.00 9.03 ? 379 PRO A N 1 ATOM 2233 C CA . PRO A 1 297 ? 23.646 48.314 53.265 1.00 9.03 ? 379 PRO A CA 1 ATOM 2234 C C . PRO A 1 297 ? 22.891 49.436 53.982 1.00 9.03 ? 379 PRO A C 1 ATOM 2235 O O . PRO A 1 297 ? 22.869 49.487 55.212 1.00 9.03 ? 379 PRO A O 1 ATOM 2236 C CB . PRO A 1 297 ? 23.038 46.948 53.577 1.00 4.61 ? 379 PRO A CB 1 ATOM 2237 C CG . PRO A 1 297 ? 24.198 46.028 53.440 1.00 4.61 ? 379 PRO A CG 1 ATOM 2238 C CD . PRO A 1 297 ? 25.311 46.780 54.120 1.00 4.61 ? 379 PRO A CD 1 ATOM 2239 N N . SER A 1 298 ? 22.306 50.345 53.208 1.00 8.46 ? 380 SER A N 1 ATOM 2240 C CA . SER A 1 298 ? 21.559 51.469 53.770 1.00 8.46 ? 380 SER A CA 1 ATOM 2241 C C . SER A 1 298 ? 20.742 52.204 52.718 1.00 8.46 ? 380 SER A C 1 ATOM 2242 O O . SER A 1 298 ? 21.181 52.364 51.579 1.00 8.46 ? 380 SER A O 1 ATOM 2243 C CB . SER A 1 298 ? 22.511 52.463 54.440 1.00 12.62 ? 380 SER A CB 1 ATOM 2244 O OG . SER A 1 298 ? 21.823 53.636 54.845 1.00 12.62 ? 380 SER A OG 1 ATOM 2245 N N . ALA A 1 299 ? 19.562 52.665 53.124 1.00 7.38 ? 381 ALA A N 1 ATOM 2246 C CA . ALA A 1 299 ? 18.663 53.405 52.244 1.00 7.38 ? 381 ALA A CA 1 ATOM 2247 C C . ALA A 1 299 ? 18.987 54.904 52.238 1.00 7.38 ? 381 ALA A C 1 ATOM 2248 O O . ALA A 1 299 ? 18.468 55.655 51.412 1.00 7.38 ? 381 ALA A O 1 ATOM 2249 C CB . ALA A 1 299 ? 17.212 53.172 52.657 1.00 9.25 ? 381 ALA A CB 1 ATOM 2250 N N . ASN A 1 300 ? 19.815 55.342 53.184 1.00 12.49 ? 382 ASN A N 1 ATOM 2251 C CA . ASN A 1 300 ? 20.221 56.745 53.255 1.00 12.49 ? 382 ASN A CA 1 ATOM 2252 C C . ASN A 1 300 ? 21.429 56.864 52.342 1.00 12.49 ? 382 ASN A C 1 ATOM 2253 O O . ASN A 1 300 ? 22.575 56.890 52.790 1.00 12.49 ? 382 ASN A O 1 ATOM 2254 C CB . ASN A 1 300 ? 20.582 57.135 54.690 1.00 34.09 ? 382 ASN A CB 1 ATOM 2255 C CG . ASN A 1 300 ? 19.383 57.100 55.621 1.00 34.09 ? 382 ASN A CG 1 ATOM 2256 O OD1 . ASN A 1 300 ? 19.387 56.405 56.634 1.00 34.09 ? 382 ASN A OD1 1 ATOM 2257 N ND2 . ASN A 1 300 ? 18.347 57.847 55.276 1.00 34.09 ? 382 ASN A ND2 1 ATOM 2258 N N . THR A 1 301 ? 21.148 56.931 51.048 1.00 10.39 ? 383 THR A N 1 ATOM 2259 C CA . THR A 1 301 ? 22.181 56.983 50.025 1.00 10.39 ? 383 THR A CA 1 ATOM 2260 C C . THR A 1 301 ? 22.664 58.364 49.599 1.00 10.39 ? 383 THR A C 1 ATOM 2261 O O . THR A 1 301 ? 23.660 58.472 48.889 1.00 10.39 ? 383 THR A O 1 ATOM 2262 C CB . THR A 1 301 ? 21.690 56.255 48.769 1.00 5.84 ? 383 THR A CB 1 ATOM 2263 O OG1 . THR A 1 301 ? 20.534 56.932 48.262 1.00 5.84 ? 383 THR A OG1 1 ATOM 2264 C CG2 . THR A 1 301 ? 21.303 54.821 49.100 1.00 5.84 ? 383 THR A CG2 1 ATOM 2265 N N . GLY A 1 302 ? 21.942 59.410 49.985 1.00 7.60 ? 384 GLY A N 1 ATOM 2266 C CA . GLY A 1 302 ? 22.332 60.754 49.588 1.00 7.60 ? 384 GLY A CA 1 ATOM 2267 C C . GLY A 1 302 ? 22.308 60.916 48.079 1.00 7.60 ? 384 GLY A C 1 ATOM 2268 O O . GLY A 1 302 ? 23.004 61.767 47.522 1.00 7.60 ? 384 GLY A O 1 ATOM 2269 N N . ASP A 1 303 ? 21.479 60.115 47.416 1.00 7.89 ? 385 ASP A N 1 ATOM 2270 C CA . ASP A 1 303 ? 21.375 60.137 45.963 1.00 7.89 ? 385 ASP A CA 1 ATOM 2271 C C . ASP A 1 303 ? 19.912 60.013 45.532 1.00 7.89 ? 385 ASP A C 1 ATOM 2272 O O . ASP A 1 303 ? 19.160 59.218 46.086 1.00 7.89 ? 385 ASP A O 1 ATOM 2273 C CB . ASP A 1 303 ? 22.198 58.982 45.389 1.00 10.40 ? 385 ASP A CB 1 ATOM 2274 C CG . ASP A 1 303 ? 22.317 59.039 43.886 1.00 10.40 ? 385 ASP A CG 1 ATOM 2275 O OD1 . ASP A 1 303 ? 23.266 59.680 43.388 1.00 10.40 ? 385 ASP A OD1 1 ATOM 2276 O OD2 . ASP A 1 303 ? 21.467 58.431 43.202 1.00 10.40 ? 385 ASP A OD2 1 ATOM 2277 N N . SER A 1 304 ? 19.535 60.776 44.510 1.00 9.65 ? 386 SER A N 1 ATOM 2278 C CA . SER A 1 304 ? 18.167 60.795 43.994 1.00 9.65 ? 386 SER A CA 1 ATOM 2279 C C . SER A 1 304 ? 17.670 59.517 43.321 1.00 9.65 ? 386 SER A C 1 ATOM 2280 O O . SER A 1 304 ? 16.469 59.247 43.320 1.00 9.65 ? 386 SER A O 1 ATOM 2281 C CB . SER A 1 304 ? 18.016 61.949 43.011 1.00 12.36 ? 386 SER A CB 1 ATOM 2282 O OG . SER A 1 304 ? 18.941 61.814 41.947 1.00 12.36 ? 386 SER A OG 1 ATOM 2283 N N . LEU A 1 305 ? 18.584 58.753 42.730 1.00 7.82 ? 387 LEU A N 1 ATOM 2284 C CA . LEU A 1 305 ? 18.226 57.529 42.018 1.00 7.82 ? 387 LEU A CA 1 ATOM 2285 C C . LEU A 1 305 ? 18.501 56.215 42.743 1.00 7.82 ? 387 LEU A C 1 ATOM 2286 O O . LEU A 1 305 ? 17.907 55.189 42.411 1.00 7.82 ? 387 LEU A O 1 ATOM 2287 C CB . LEU A 1 305 ? 18.919 57.500 40.654 1.00 9.54 ? 387 LEU A CB 1 ATOM 2288 C CG . LEU A 1 305 ? 18.546 58.586 39.644 1.00 9.54 ? 387 LEU A CG 1 ATOM 2289 C CD1 . LEU A 1 305 ? 19.374 58.410 38.387 1.00 9.54 ? 387 LEU A CD1 1 ATOM 2290 C CD2 . LEU A 1 305 ? 17.064 58.509 39.308 1.00 9.54 ? 387 LEU A CD2 1 ATOM 2291 N N . LEU A 1 306 ? 19.403 56.230 43.721 1.00 6.49 ? 388 LEU A N 1 ATOM 2292 C CA . LEU A 1 306 ? 19.733 55.003 44.438 1.00 6.49 ? 388 LEU A CA 1 ATOM 2293 C C . LEU A 1 306 ? 18.836 54.739 45.648 1.00 6.49 ? 388 LEU A C 1 ATOM 2294 O O . LEU A 1 306 ? 18.864 55.484 46.632 1.00 6.49 ? 388 LEU A O 1 ATOM 2295 C CB . LEU A 1 306 ? 21.202 55.010 44.871 1.00 2.47 ? 388 LEU A CB 1 ATOM 2296 C CG . LEU A 1 306 ? 21.790 53.636 45.207 1.00 2.47 ? 388 LEU A CG 1 ATOM 2297 C CD1 . LEU A 1 306 ? 22.007 52.863 43.916 1.00 2.47 ? 388 LEU A CD1 1 ATOM 2298 C CD2 . LEU A 1 306 ? 23.104 53.793 45.950 1.00 2.47 ? 388 LEU A CD2 1 ATOM 2299 N N . ASP A 1 307 ? 18.038 53.678 45.567 1.00 5.65 ? 389 ASP A N 1 ATOM 2300 C CA . ASP A 1 307 ? 17.148 53.299 46.658 1.00 5.65 ? 389 ASP A CA 1 ATOM 2301 C C . ASP A 1 307 ? 17.945 52.803 47.850 1.00 5.65 ? 389 ASP A C 1 ATOM 2302 O O . ASP A 1 307 ? 17.569 53.049 49.002 1.00 5.65 ? 389 ASP A O 1 ATOM 2303 C CB . ASP A 1 307 ? 16.196 52.180 46.228 1.00 3.66 ? 389 ASP A CB 1 ATOM 2304 C CG . ASP A 1 307 ? 14.989 52.679 45.464 1.00 3.66 ? 389 ASP A CG 1 ATOM 2305 O OD1 . ASP A 1 307 ? 14.685 53.888 45.471 1.00 3.66 ? 389 ASP A OD1 1 ATOM 2306 O OD2 . ASP A 1 307 ? 14.320 51.829 44.861 1.00 3.66 ? 389 ASP A OD2 1 ATOM 2307 N N . SER A 1 308 ? 19.051 52.110 47.573 1.00 5.43 ? 390 SER A N 1 ATOM 2308 C CA . SER A 1 308 ? 19.869 51.560 48.643 1.00 5.43 ? 390 SER A CA 1 ATOM 2309 C C . SER A 1 308 ? 21.180 50.918 48.209 1.00 5.43 ? 390 SER A C 1 ATOM 2310 O O . SER A 1 308 ? 21.321 50.460 47.074 1.00 5.43 ? 390 SER A O 1 ATOM 2311 C CB . SER A 1 308 ? 19.045 50.512 49.401 1.00 8.49 ? 390 SER A CB 1 ATOM 2312 O OG . SER A 1 308 ? 19.818 49.810 50.353 1.00 8.49 ? 390 SER A OG 1 ATOM 2313 N N . PHE A 1 309 ? 22.155 50.949 49.119 1.00 7.71 ? 391 PHE A N 1 ATOM 2314 C CA . PHE A 1 309 ? 23.434 50.277 48.914 1.00 7.71 ? 391 PHE A CA 1 ATOM 2315 C C . PHE A 1 309 ? 23.083 48.880 49.422 1.00 7.71 ? 391 PHE A C 1 ATOM 2316 O O . PHE A 1 309 ? 22.385 48.749 50.432 1.00 7.71 ? 391 PHE A O 1 ATOM 2317 C CB . PHE A 1 309 ? 24.530 50.837 49.836 1.00 7.71 ? 391 PHE A CB 1 ATOM 2318 C CG . PHE A 1 309 ? 24.943 52.247 49.523 1.00 7.71 ? 391 PHE A CG 1 ATOM 2319 C CD1 . PHE A 1 309 ? 25.628 52.542 48.349 1.00 7.71 ? 391 PHE A CD1 1 ATOM 2320 C CD2 . PHE A 1 309 ? 24.669 53.276 50.420 1.00 7.71 ? 391 PHE A CD2 1 ATOM 2321 C CE1 . PHE A 1 309 ? 26.034 53.843 48.074 1.00 7.71 ? 391 PHE A CE1 1 ATOM 2322 C CE2 . PHE A 1 309 ? 25.073 54.580 50.153 1.00 7.71 ? 391 PHE A CE2 1 ATOM 2323 C CZ . PHE A 1 309 ? 25.757 54.864 48.977 1.00 7.71 ? 391 PHE A CZ 1 ATOM 2324 N N . VAL A 1 310 ? 23.536 47.842 48.731 1.00 5.65 ? 392 VAL A N 1 ATOM 2325 C CA . VAL A 1 310 ? 23.248 46.479 49.158 1.00 5.65 ? 392 VAL A CA 1 ATOM 2326 C C . VAL A 1 310 ? 24.478 45.591 49.000 1.00 5.65 ? 392 VAL A C 1 ATOM 2327 O O . VAL A 1 310 ? 25.473 45.997 48.404 1.00 5.65 ? 392 VAL A O 1 ATOM 2328 C CB . VAL A 1 310 ? 22.075 45.846 48.330 1.00 2.00 ? 392 VAL A CB 1 ATOM 2329 C CG1 . VAL A 1 310 ? 20.760 46.553 48.627 1.00 2.00 ? 392 VAL A CG1 1 ATOM 2330 C CG2 . VAL A 1 310 ? 22.370 45.908 46.835 1.00 2.00 ? 392 VAL A CG2 1 ATOM 2331 N N . TRP A 1 311 ? 24.421 44.411 49.611 1.00 5.57 ? 393 TRP A N 1 ATOM 2332 C CA . TRP A 1 311 ? 25.478 43.408 49.508 1.00 5.57 ? 393 TRP A CA 1 ATOM 2333 C C . TRP A 1 311 ? 24.771 42.206 48.889 1.00 5.57 ? 393 TRP A C 1 ATOM 2334 O O . TRP A 1 311 ? 24.099 41.450 49.581 1.00 5.57 ? 393 TRP A O 1 ATOM 2335 C CB . TRP A 1 311 ? 26.040 43.036 50.889 1.00 5.41 ? 393 TRP A CB 1 ATOM 2336 C CG . TRP A 1 311 ? 27.034 44.027 51.448 1.00 5.41 ? 393 TRP A CG 1 ATOM 2337 C CD1 . TRP A 1 311 ? 27.221 45.322 51.047 1.00 5.41 ? 393 TRP A CD1 1 ATOM 2338 C CD2 . TRP A 1 311 ? 27.973 43.797 52.509 1.00 5.41 ? 393 TRP A CD2 1 ATOM 2339 N NE1 . TRP A 1 311 ? 28.212 45.910 51.793 1.00 5.41 ? 393 TRP A NE1 1 ATOM 2340 C CE2 . TRP A 1 311 ? 28.692 45.002 52.698 1.00 5.41 ? 393 TRP A CE2 1 ATOM 2341 C CE3 . TRP A 1 311 ? 28.277 42.696 53.320 1.00 5.41 ? 393 TRP A CE3 1 ATOM 2342 C CZ2 . TRP A 1 311 ? 29.698 45.134 53.665 1.00 5.41 ? 393 TRP A CZ2 1 ATOM 2343 C CZ3 . TRP A 1 311 ? 29.280 42.829 54.285 1.00 5.41 ? 393 TRP A CZ3 1 ATOM 2344 C CH2 . TRP A 1 311 ? 29.974 44.039 54.446 1.00 5.41 ? 393 TRP A CH2 1 ATOM 2345 N N . VAL A 1 312 ? 24.850 42.078 47.572 1.00 5.13 ? 394 VAL A N 1 ATOM 2346 C CA . VAL A 1 312 ? 24.186 40.979 46.889 1.00 5.13 ? 394 VAL A CA 1 ATOM 2347 C C . VAL A 1 312 ? 25.029 39.706 46.926 1.00 5.13 ? 394 VAL A C 1 ATOM 2348 O O . VAL A 1 312 ? 24.599 38.683 47.465 1.00 5.13 ? 394 VAL A O 1 ATOM 2349 C CB . VAL A 1 312 ? 23.817 41.378 45.435 1.00 2.00 ? 394 VAL A CB 1 ATOM 2350 C CG1 . VAL A 1 312 ? 22.961 40.305 44.789 1.00 2.00 ? 394 VAL A CG1 1 ATOM 2351 C CG2 . VAL A 1 312 ? 23.070 42.707 45.440 1.00 2.00 ? 394 VAL A CG2 1 ATOM 2352 N N . LYS A 1 313 ? 26.221 39.767 46.343 1.00 6.87 ? 395 LYS A N 1 ATOM 2353 C CA . LYS A 1 313 ? 27.139 38.631 46.343 1.00 6.87 ? 395 LYS A CA 1 ATOM 2354 C C . LYS A 1 313 ? 27.736 38.558 47.752 1.00 6.87 ? 395 LYS A C 1 ATOM 2355 O O . LYS A 1 313 ? 28.357 39.516 48.219 1.00 6.87 ? 395 LYS A O 1 ATOM 2356 C CB . LYS A 1 313 ? 28.237 38.842 45.296 1.00 8.32 ? 395 LYS A CB 1 ATOM 2357 C CG . LYS A 1 313 ? 29.430 37.900 45.410 1.00 8.32 ? 395 LYS A CG 1 ATOM 2358 C CD . LYS A 1 313 ? 29.098 36.459 45.065 1.00 8.32 ? 395 LYS A CD 1 ATOM 2359 C CE . LYS A 1 313 ? 30.341 35.607 45.268 1.00 8.32 ? 395 LYS A CE 1 ATOM 2360 N NZ . LYS A 1 313 ? 30.168 34.193 44.846 1.00 8.32 ? 395 LYS A NZ 1 ATOM 2361 N N . PRO A 1 314 ? 27.501 37.444 48.468 1.00 9.02 ? 396 PRO A N 1 ATOM 2362 C CA . PRO A 1 314 ? 28.021 37.271 49.833 1.00 9.02 ? 396 PRO A CA 1 ATOM 2363 C C . PRO A 1 314 ? 29.534 37.088 49.827 1.00 9.02 ? 396 PRO A C 1 ATOM 2364 O O . PRO A 1 314 ? 30.048 36.167 49.198 1.00 9.02 ? 396 PRO A O 1 ATOM 2365 C CB . PRO A 1 314 ? 27.311 36.003 50.322 1.00 8.20 ? 396 PRO A CB 1 ATOM 2366 C CG . PRO A 1 314 ? 26.116 35.853 49.382 1.00 8.20 ? 396 PRO A CG 1 ATOM 2367 C CD . PRO A 1 314 ? 26.682 36.288 48.070 1.00 8.20 ? 396 PRO A CD 1 ATOM 2368 N N . GLY A 1 315 ? 30.235 37.981 50.520 1.00 8.89 ? 397 GLY A N 1 ATOM 2369 C CA . GLY A 1 315 ? 31.685 37.919 50.582 1.00 8.89 ? 397 GLY A CA 1 ATOM 2370 C C . GLY A 1 315 ? 32.186 36.680 51.291 1.00 8.89 ? 397 GLY A C 1 ATOM 2371 O O . GLY A 1 315 ? 31.834 36.444 52.440 1.00 8.89 ? 397 GLY A O 1 ATOM 2372 N N . GLY A 1 316 ? 33.035 35.907 50.622 1.00 6.98 ? 398 GLY A N 1 ATOM 2373 C CA . GLY A 1 316 ? 33.546 34.685 51.215 1.00 6.98 ? 398 GLY A CA 1 ATOM 2374 C C . GLY A 1 316 ? 33.142 33.483 50.382 1.00 6.98 ? 398 GLY A C 1 ATOM 2375 O O . GLY A 1 316 ? 33.827 32.465 50.374 1.00 6.98 ? 398 GLY A O 1 ATOM 2376 N N . GLU A 1 317 ? 31.998 33.584 49.710 1.00 5.74 ? 399 GLU A N 1 ATOM 2377 C CA . GLU A 1 317 ? 31.516 32.510 48.847 1.00 5.74 ? 399 GLU A CA 1 ATOM 2378 C C . GLU A 1 317 ? 32.217 32.647 47.496 1.00 5.74 ? 399 GLU A C 1 ATOM 2379 O O . GLU A 1 317 ? 32.136 33.691 46.843 1.00 5.74 ? 399 GLU A O 1 ATOM 2380 C CB . GLU A 1 317 ? 29.997 32.592 48.699 1.00 9.49 ? 399 GLU A CB 1 ATOM 2381 C CG . GLU A 1 317 ? 29.269 32.376 50.020 1.00 9.49 ? 399 GLU A CG 1 ATOM 2382 C CD . GLU A 1 317 ? 27.759 32.388 49.884 1.00 9.49 ? 399 GLU A CD 1 ATOM 2383 O OE1 . GLU A 1 317 ? 27.257 32.512 48.749 1.00 9.49 ? 399 GLU A OE1 1 ATOM 2384 O OE2 . GLU A 1 317 ? 27.066 32.278 50.916 1.00 9.49 ? 399 GLU A OE2 1 ATOM 2385 N N . CYS A 1 318 ? 32.885 31.576 47.084 1.00 5.43 ? 400 CYS A N 1 ATOM 2386 C CA . CYS A 1 318 ? 33.667 31.536 45.851 1.00 5.43 ? 400 CYS A CA 1 ATOM 2387 C C . CYS A 1 318 ? 32.955 31.854 44.533 1.00 5.43 ? 400 CYS A C 1 ATOM 2388 O O . CYS A 1 318 ? 31.774 31.561 44.367 1.00 5.43 ? 400 CYS A O 1 ATOM 2389 C CB . CYS A 1 318 ? 34.369 30.183 45.745 1.00 11.26 ? 400 CYS A CB 1 ATOM 2390 S SG . CYS A 1 318 ? 35.812 30.185 44.667 1.00 11.26 ? 400 CYS A SG 1 ATOM 2391 N N . ASP A 1 319 ? 33.693 32.463 43.603 1.00 4.79 ? 401 ASP A N 1 ATOM 2392 C CA . ASP A 1 319 ? 33.169 32.813 42.276 1.00 4.79 ? 401 ASP A CA 1 ATOM 2393 C C . ASP A 1 319 ? 33.384 31.662 41.295 1.00 4.79 ? 401 ASP A C 1 ATOM 2394 O O . ASP A 1 319 ? 32.721 31.579 40.265 1.00 4.79 ? 401 ASP A O 1 ATOM 2395 C CB . ASP A 1 319 ? 33.879 34.052 41.716 1.00 9.63 ? 401 ASP A CB 1 ATOM 2396 C CG . ASP A 1 319 ? 33.545 35.325 42.472 1.00 9.63 ? 401 ASP A CG 1 ATOM 2397 O OD1 . ASP A 1 319 ? 32.393 35.488 42.916 1.00 9.63 ? 401 ASP A OD1 1 ATOM 2398 O OD2 . ASP A 1 319 ? 34.438 36.186 42.599 1.00 9.63 ? 401 ASP A OD2 1 ATOM 2399 N N . GLY A 1 320 ? 34.355 30.810 41.594 1.00 8.41 ? 402 GLY A N 1 ATOM 2400 C CA . GLY A 1 320 ? 34.656 29.687 40.724 1.00 8.41 ? 402 GLY A CA 1 ATOM 2401 C C . GLY A 1 320 ? 35.974 29.053 41.128 1.00 8.41 ? 402 GLY A C 1 ATOM 2402 O O . GLY A 1 320 ? 36.782 29.681 41.822 1.00 8.41 ? 402 GLY A O 1 ATOM 2403 N N . THR A 1 321 ? 36.208 27.826 40.673 1.00 11.57 ? 403 THR A N 1 ATOM 2404 C CA . THR A 1 321 ? 37.429 27.096 41.015 1.00 11.57 ? 403 THR A CA 1 ATOM 2405 C C . THR A 1 321 ? 38.635 27.385 40.117 1.00 11.57 ? 403 THR A C 1 ATOM 2406 O O . THR A 1 321 ? 38.489 27.657 38.925 1.00 11.57 ? 403 THR A O 1 ATOM 2407 C CB . THR A 1 321 ? 37.168 25.569 41.043 1.00 17.26 ? 403 THR A CB 1 ATOM 2408 O OG1 . THR A 1 321 ? 38.322 24.893 41.554 1.00 17.26 ? 403 THR A OG1 1 ATOM 2409 C CG2 . THR A 1 321 ? 36.857 25.045 39.648 1.00 17.26 ? 403 THR A CG2 1 ATOM 2410 N N . SER A 1 322 ? 39.828 27.319 40.701 1.00 14.90 ? 404 SER A N 1 ATOM 2411 C CA . SER A 1 322 ? 41.058 27.537 39.947 1.00 14.90 ? 404 SER A CA 1 ATOM 2412 C C . SER A 1 322 ? 41.687 26.191 39.562 1.00 14.90 ? 404 SER A C 1 ATOM 2413 O O . SER A 1 322 ? 42.744 26.154 38.935 1.00 14.90 ? 404 SER A O 1 ATOM 2414 C CB . SER A 1 322 ? 42.051 28.376 40.756 1.00 12.69 ? 404 SER A CB 1 ATOM 2415 O OG . SER A 1 322 ? 42.416 27.734 41.967 1.00 12.69 ? 404 SER A OG 1 ATOM 2416 N N . ASP A 1 323 ? 41.012 25.097 39.922 1.00 10.45 ? 405 ASP A N 1 ATOM 2417 C CA . ASP A 1 323 ? 41.479 23.743 39.639 1.00 10.45 ? 405 ASP A CA 1 ATOM 2418 C C . ASP A 1 323 ? 41.210 23.354 38.185 1.00 10.45 ? 405 ASP A C 1 ATOM 2419 O O . ASP A 1 323 ? 40.061 23.166 37.787 1.00 10.45 ? 405 ASP A O 1 ATOM 2420 C CB . ASP A 1 323 ? 40.789 22.763 40.588 1.00 15.85 ? 405 ASP A CB 1 ATOM 2421 C CG . ASP A 1 323 ? 41.355 21.351 40.507 1.00 15.85 ? 405 ASP A CG 1 ATOM 2422 O OD1 . ASP A 1 323 ? 42.303 21.100 39.731 1.00 15.85 ? 405 ASP A OD1 1 ATOM 2423 O OD2 . ASP A 1 323 ? 40.839 20.481 41.237 1.00 15.85 ? 405 ASP A OD2 1 ATOM 2424 N N . SER A 1 324 ? 42.280 23.165 37.417 1.00 24.19 ? 406 SER A N 1 ATOM 2425 C CA . SER A 1 324 ? 42.165 22.811 36.003 1.00 24.19 ? 406 SER A CA 1 ATOM 2426 C C . SER A 1 324 ? 41.620 21.412 35.724 1.00 24.19 ? 406 SER A C 1 ATOM 2427 O O . SER A 1 324 ? 41.039 21.176 34.665 1.00 24.19 ? 406 SER A O 1 ATOM 2428 C CB . SER A 1 324 ? 43.512 22.997 35.297 1.00 35.77 ? 406 SER A CB 1 ATOM 2429 O OG . SER A 1 324 ? 44.528 22.225 35.914 1.00 35.77 ? 406 SER A OG 1 ATOM 2430 N N . SER A 1 325 ? 41.803 20.487 36.664 1.00 45.83 ? 407 SER A N 1 ATOM 2431 C CA . SER A 1 325 ? 41.315 19.122 36.484 1.00 45.83 ? 407 SER A CA 1 ATOM 2432 C C . SER A 1 325 ? 39.887 18.969 36.996 1.00 45.83 ? 407 SER A C 1 ATOM 2433 O O . SER A 1 325 ? 39.337 17.866 37.019 1.00 45.83 ? 407 SER A O 1 ATOM 2434 C CB . SER A 1 325 ? 42.233 18.120 37.195 1.00 46.70 ? 407 SER A CB 1 ATOM 2435 O OG . SER A 1 325 ? 42.184 18.282 38.602 1.00 46.70 ? 407 SER A OG 1 ATOM 2436 N N . ALA A 1 326 ? 39.288 20.084 37.401 1.00 27.55 ? 408 ALA A N 1 ATOM 2437 C CA . ALA A 1 326 ? 37.930 20.081 37.922 1.00 27.55 ? 408 ALA A CA 1 ATOM 2438 C C . ALA A 1 326 ? 36.907 20.474 36.865 1.00 27.55 ? 408 ALA A C 1 ATOM 2439 O O . ALA A 1 326 ? 37.206 21.252 35.955 1.00 27.55 ? 408 ALA A O 1 ATOM 2440 C CB . ALA A 1 326 ? 37.833 21.022 39.112 1.00 23.87 ? 408 ALA A CB 1 ATOM 2441 N N . PRO A 1 327 ? 35.695 19.893 36.939 1.00 55.29 ? 409 PRO A N 1 ATOM 2442 C CA . PRO A 1 327 ? 34.642 20.216 35.975 1.00 55.29 ? 409 PRO A CA 1 ATOM 2443 C C . PRO A 1 327 ? 34.199 21.649 36.254 1.00 55.29 ? 409 PRO A C 1 ATOM 2444 O O . PRO A 1 327 ? 34.360 22.143 37.375 1.00 55.29 ? 409 PRO A O 1 ATOM 2445 C CB . PRO A 1 327 ? 33.530 19.225 36.330 1.00 54.07 ? 409 PRO A CB 1 ATOM 2446 C CG . PRO A 1 327 ? 34.251 18.094 36.989 1.00 54.07 ? 409 PRO A CG 1 ATOM 2447 C CD . PRO A 1 327 ? 35.273 18.799 37.828 1.00 54.07 ? 409 PRO A CD 1 ATOM 2448 N N . ARG A 1 328 ? 33.651 22.312 35.241 1.00 28.17 ? 410 ARG A N 1 ATOM 2449 C CA . ARG A 1 328 ? 33.185 23.695 35.369 1.00 28.17 ? 410 ARG A CA 1 ATOM 2450 C C . ARG A 1 328 ? 34.343 24.681 35.570 1.00 28.17 ? 410 ARG A C 1 ATOM 2451 O O . ARG A 1 328 ? 34.121 25.834 35.938 1.00 28.17 ? 410 ARG A O 1 ATOM 2452 C CB . ARG A 1 328 ? 32.185 23.839 36.526 1.00 78.50 ? 410 ARG A CB 1 ATOM 2453 C CG . ARG A 1 328 ? 31.091 22.781 36.584 1.00 78.50 ? 410 ARG A CG 1 ATOM 2454 C CD . ARG A 1 328 ? 30.130 22.869 35.418 1.00 78.50 ? 410 ARG A CD 1 ATOM 2455 N NE . ARG A 1 328 ? 29.049 21.895 35.550 1.00 78.50 ? 410 ARG A NE 1 ATOM 2456 C CZ . ARG A 1 328 ? 28.496 21.243 34.532 1.00 78.50 ? 410 ARG A CZ 1 ATOM 2457 N NH1 . ARG A 1 328 ? 28.916 21.456 33.291 1.00 78.50 ? 410 ARG A NH1 1 ATOM 2458 N NH2 . ARG A 1 328 ? 27.526 20.366 34.756 1.00 78.50 ? 410 ARG A NH2 1 ATOM 2459 N N . PHE A 1 329 ? 35.574 24.229 35.331 1.00 17.38 ? 411 PHE A N 1 ATOM 2460 C CA . PHE A 1 329 ? 36.743 25.095 35.474 1.00 17.38 ? 411 PHE A CA 1 ATOM 2461 C C . PHE A 1 329 ? 36.700 26.236 34.458 1.00 17.38 ? 411 PHE A C 1 ATOM 2462 O O . PHE A 1 329 ? 36.511 26.016 33.263 1.00 17.38 ? 411 PHE A O 1 ATOM 2463 C CB . PHE A 1 329 ? 38.048 24.299 35.304 1.00 18.39 ? 411 PHE A CB 1 ATOM 2464 C CG . PHE A 1 329 ? 39.274 25.164 35.187 1.00 18.39 ? 411 PHE A CG 1 ATOM 2465 C CD1 . PHE A 1 329 ? 39.672 25.977 36.243 1.00 18.39 ? 411 PHE A CD1 1 ATOM 2466 C CD2 . PHE A 1 329 ? 40.006 25.199 34.006 1.00 18.39 ? 411 PHE A CD2 1 ATOM 2467 C CE1 . PHE A 1 329 ? 40.777 26.816 36.128 1.00 18.39 ? 411 PHE A CE1 1 ATOM 2468 C CE2 . PHE A 1 329 ? 41.116 26.037 33.876 1.00 18.39 ? 411 PHE A CE2 1 ATOM 2469 C CZ . PHE A 1 329 ? 41.501 26.849 34.943 1.00 18.39 ? 411 PHE A CZ 1 ATOM 2470 N N . ASP A 1 330 ? 36.857 27.457 34.955 1.00 14.96 ? 412 ASP A N 1 ATOM 2471 C CA . ASP A 1 330 ? 36.848 28.647 34.112 1.00 14.96 ? 412 ASP A CA 1 ATOM 2472 C C . ASP A 1 330 ? 38.247 29.245 34.209 1.00 14.96 ? 412 ASP A C 1 ATOM 2473 O O . ASP A 1 330 ? 38.730 29.520 35.309 1.00 14.96 ? 412 ASP A O 1 ATOM 2474 C CB . ASP A 1 330 ? 35.803 29.643 34.630 1.00 18.01 ? 412 ASP A CB 1 ATOM 2475 C CG . ASP A 1 330 ? 35.500 30.750 33.637 1.00 18.01 ? 412 ASP A CG 1 ATOM 2476 O OD1 . ASP A 1 330 ? 36.440 31.421 33.172 1.00 18.01 ? 412 ASP A OD1 1 ATOM 2477 O OD2 . ASP A 1 330 ? 34.314 30.951 33.323 1.00 18.01 ? 412 ASP A OD2 1 ATOM 2478 N N . SER A 1 331 ? 38.897 29.439 33.062 1.00 12.59 ? 413 SER A N 1 ATOM 2479 C CA . SER A 1 331 ? 40.254 29.990 33.031 1.00 12.59 ? 413 SER A CA 1 ATOM 2480 C C . SER A 1 331 ? 40.412 31.395 33.623 1.00 12.59 ? 413 SER A C 1 ATOM 2481 O O . SER A 1 331 ? 41.517 31.789 33.994 1.00 12.59 ? 413 SER A O 1 ATOM 2482 C CB . SER A 1 331 ? 40.836 29.925 31.614 1.00 38.45 ? 413 SER A CB 1 ATOM 2483 O OG . SER A 1 331 ? 39.962 30.499 30.662 1.00 38.45 ? 413 SER A OG 1 ATOM 2484 N N . HIS A 1 332 ? 39.311 32.138 33.726 1.00 11.99 ? 414 HIS A N 1 ATOM 2485 C CA . HIS A 1 332 ? 39.338 33.483 34.306 1.00 11.99 ? 414 HIS A CA 1 ATOM 2486 C C . HIS A 1 332 ? 39.691 33.425 35.793 1.00 11.99 ? 414 HIS A C 1 ATOM 2487 O O . HIS A 1 332 ? 40.152 34.411 36.380 1.00 11.99 ? 414 HIS A O 1 ATOM 2488 C CB . HIS A 1 332 ? 37.979 34.162 34.148 1.00 30.83 ? 414 HIS A CB 1 ATOM 2489 C CG . HIS A 1 332 ? 37.705 34.649 32.760 1.00 30.83 ? 414 HIS A CG 1 ATOM 2490 N ND1 . HIS A 1 332 ? 37.116 33.864 31.797 1.00 30.83 ? 414 HIS A ND1 1 ATOM 2491 C CD2 . HIS A 1 332 ? 37.946 35.846 32.179 1.00 30.83 ? 414 HIS A CD2 1 ATOM 2492 C CE1 . HIS A 1 332 ? 37.003 34.553 30.675 1.00 30.83 ? 414 HIS A CE1 1 ATOM 2493 N NE2 . HIS A 1 332 ? 37.502 35.763 30.883 1.00 30.83 ? 414 HIS A NE2 1 ATOM 2494 N N . CYS A 1 333 ? 39.444 32.268 36.401 1.00 11.00 ? 415 CYS A N 1 ATOM 2495 C CA . CYS A 1 333 ? 39.728 32.055 37.816 1.00 11.00 ? 415 CYS A CA 1 ATOM 2496 C C . CYS A 1 333 ? 41.172 31.620 38.066 1.00 11.00 ? 415 CYS A C 1 ATOM 2497 O O . CYS A 1 333 ? 41.574 31.399 39.209 1.00 11.00 ? 415 CYS A O 1 ATOM 2498 C CB . CYS A 1 333 ? 38.746 31.033 38.385 1.00 7.33 ? 415 CYS A CB 1 ATOM 2499 S SG . CYS A 1 333 ? 37.017 31.582 38.240 1.00 7.33 ? 415 CYS A SG 1 ATOM 2500 N N . ALA A 1 334 ? 41.954 31.542 36.990 1.00 17.58 ? 416 ALA A N 1 ATOM 2501 C CA . ALA A 1 334 ? 43.359 31.144 37.063 1.00 17.58 ? 416 ALA A CA 1 ATOM 2502 C C . ALA A 1 334 ? 44.307 32.298 36.725 1.00 17.58 ? 416 ALA A C 1 ATOM 2503 O O . ALA A 1 334 ? 45.522 32.115 36.689 1.00 17.58 ? 416 ALA A O 1 ATOM 2504 C CB . ALA A 1 334 ? 43.619 29.965 36.130 1.00 14.36 ? 416 ALA A CB 1 ATOM 2505 N N . LEU A 1 335 ? 43.742 33.478 36.480 1.00 9.80 ? 417 LEU A N 1 ATOM 2506 C CA . LEU A 1 335 ? 44.512 34.676 36.147 1.00 9.80 ? 417 LEU A CA 1 ATOM 2507 C C . LEU A 1 335 ? 45.345 35.170 37.329 1.00 9.80 ? 417 LEU A C 1 ATOM 2508 O O . LEU A 1 335 ? 45.038 34.871 38.486 1.00 9.80 ? 417 LEU A O 1 ATOM 2509 C CB . LEU A 1 335 ? 43.571 35.788 35.674 1.00 17.20 ? 417 LEU A CB 1 ATOM 2510 C CG . LEU A 1 335 ? 42.846 35.547 34.349 1.00 17.20 ? 417 LEU A CG 1 ATOM 2511 C CD1 . LEU A 1 335 ? 41.882 36.691 34.072 1.00 17.20 ? 417 LEU A CD1 1 ATOM 2512 C CD2 . LEU A 1 335 ? 43.857 35.414 33.219 1.00 17.20 ? 417 LEU A CD2 1 ATOM 2513 N N . PRO A 1 336 ? 46.414 35.941 37.051 1.00 16.82 ? 418 PRO A N 1 ATOM 2514 C CA . PRO A 1 336 ? 47.309 36.486 38.080 1.00 16.82 ? 418 PRO A CA 1 ATOM 2515 C C . PRO A 1 336 ? 46.613 37.346 39.137 1.00 16.82 ? 418 PRO A C 1 ATOM 2516 O O . PRO A 1 336 ? 47.119 37.494 40.251 1.00 16.82 ? 418 PRO A O 1 ATOM 2517 C CB . PRO A 1 336 ? 48.309 37.314 37.267 1.00 14.52 ? 418 PRO A CB 1 ATOM 2518 C CG . PRO A 1 336 ? 48.343 36.616 35.953 1.00 14.52 ? 418 PRO A CG 1 ATOM 2519 C CD . PRO A 1 336 ? 46.890 36.302 35.703 1.00 14.52 ? 418 PRO A CD 1 ATOM 2520 N N . ASP A 1 337 ? 45.465 37.923 38.786 1.00 13.91 ? 419 ASP A N 1 ATOM 2521 C CA . ASP A 1 337 ? 44.737 38.756 39.736 1.00 13.91 ? 419 ASP A CA 1 ATOM 2522 C C . ASP A 1 337 ? 43.554 38.055 40.399 1.00 13.91 ? 419 ASP A C 1 ATOM 2523 O O . ASP A 1 337 ? 42.671 38.703 40.971 1.00 13.91 ? 419 ASP A O 1 ATOM 2524 C CB . ASP A 1 337 ? 44.320 40.090 39.106 1.00 14.42 ? 419 ASP A CB 1 ATOM 2525 C CG . ASP A 1 337 ? 43.390 39.930 37.917 1.00 14.42 ? 419 ASP A CG 1 ATOM 2526 O OD1 . ASP A 1 337 ? 43.134 38.790 37.467 1.00 14.42 ? 419 ASP A OD1 1 ATOM 2527 O OD2 . ASP A 1 337 ? 42.907 40.970 37.429 1.00 14.42 ? 419 ASP A OD2 1 ATOM 2528 N N . ALA A 1 338 ? 43.533 36.729 40.291 1.00 11.21 ? 420 ALA A N 1 ATOM 2529 C CA . ALA A 1 338 ? 42.495 35.915 40.910 1.00 11.21 ? 420 ALA A CA 1 ATOM 2530 C C . ALA A 1 338 ? 43.181 35.163 42.052 1.00 11.21 ? 420 ALA A C 1 ATOM 2531 O O . ALA A 1 338 ? 44.257 34.590 41.856 1.00 11.21 ? 420 ALA A O 1 ATOM 2532 C CB . ALA A 1 338 ? 41.913 34.939 39.901 1.00 11.47 ? 420 ALA A CB 1 ATOM 2533 N N . LEU A 1 339 ? 42.586 35.203 43.246 1.00 9.97 ? 421 LEU A N 1 ATOM 2534 C CA . LEU A 1 339 ? 43.150 34.530 44.415 1.00 9.97 ? 421 LEU A CA 1 ATOM 2535 C C . LEU A 1 339 ? 43.076 33.011 44.248 1.00 9.97 ? 421 LEU A C 1 ATOM 2536 O O . LEU A 1 339 ? 42.036 32.467 43.864 1.00 9.97 ? 421 LEU A O 1 ATOM 2537 C CB . LEU A 1 339 ? 42.423 34.968 45.696 1.00 9.49 ? 421 LEU A CB 1 ATOM 2538 C CG . LEU A 1 339 ? 43.091 34.607 47.034 1.00 9.49 ? 421 LEU A CG 1 ATOM 2539 C CD1 . LEU A 1 339 ? 44.509 35.177 47.102 1.00 9.49 ? 421 LEU A CD1 1 ATOM 2540 C CD2 . LEU A 1 339 ? 42.253 35.134 48.192 1.00 9.49 ? 421 LEU A CD2 1 ATOM 2541 N N . GLN A 1 340 ? 44.189 32.339 44.535 1.00 11.23 ? 422 GLN A N 1 ATOM 2542 C CA . GLN A 1 340 ? 44.289 30.886 44.395 1.00 11.23 ? 422 GLN A CA 1 ATOM 2543 C C . GLN A 1 340 ? 45.010 30.243 45.577 1.00 11.23 ? 422 GLN A C 1 ATOM 2544 O O . GLN A 1 340 ? 45.832 30.884 46.236 1.00 11.23 ? 422 GLN A O 1 ATOM 2545 C CB . GLN A 1 340 ? 45.029 30.550 43.097 1.00 28.19 ? 422 GLN A CB 1 ATOM 2546 C CG . GLN A 1 340 ? 44.333 31.081 41.851 1.00 28.19 ? 422 GLN A CG 1 ATOM 2547 C CD . GLN A 1 340 ? 45.175 30.956 40.608 1.00 28.19 ? 422 GLN A CD 1 ATOM 2548 O OE1 . GLN A 1 340 ? 45.444 29.850 40.135 1.00 28.19 ? 422 GLN A OE1 1 ATOM 2549 N NE2 . GLN A 1 340 ? 45.595 32.092 40.061 1.00 28.19 ? 422 GLN A NE2 1 ATOM 2550 N N . PRO A 1 341 ? 44.702 28.965 45.870 1.00 15.99 ? 423 PRO A N 1 ATOM 2551 C CA . PRO A 1 341 ? 43.728 28.118 45.168 1.00 15.99 ? 423 PRO A CA 1 ATOM 2552 C C . PRO A 1 341 ? 42.279 28.401 45.581 1.00 15.99 ? 423 PRO A C 1 ATOM 2553 O O . PRO A 1 341 ? 42.000 28.666 46.752 1.00 15.99 ? 423 PRO A O 1 ATOM 2554 C CB . PRO A 1 341 ? 44.165 26.707 45.554 1.00 15.38 ? 423 PRO A CB 1 ATOM 2555 C CG . PRO A 1 341 ? 44.719 26.885 46.925 1.00 15.38 ? 423 PRO A CG 1 ATOM 2556 C CD . PRO A 1 341 ? 45.474 28.185 46.854 1.00 15.38 ? 423 PRO A CD 1 ATOM 2557 N N . ALA A 1 342 ? 41.368 28.335 44.612 1.00 9.04 ? 424 ALA A N 1 ATOM 2558 C CA . ALA A 1 342 ? 39.953 28.608 44.846 1.00 9.04 ? 424 ALA A CA 1 ATOM 2559 C C . ALA A 1 342 ? 39.079 27.372 44.672 1.00 9.04 ? 424 ALA A C 1 ATOM 2560 O O . ALA A 1 342 ? 39.254 26.610 43.724 1.00 9.04 ? 424 ALA A O 1 ATOM 2561 C CB . ALA A 1 342 ? 39.479 29.709 43.903 1.00 11.03 ? 424 ALA A CB 1 ATOM 2562 N N . PRO A 1 343 ? 38.125 27.157 45.597 1.00 13.15 ? 425 PRO A N 1 ATOM 2563 C CA . PRO A 1 343 ? 37.212 26.011 45.551 1.00 13.15 ? 425 PRO A CA 1 ATOM 2564 C C . PRO A 1 343 ? 36.090 26.207 44.532 1.00 13.15 ? 425 PRO A C 1 ATOM 2565 O O . PRO A 1 343 ? 36.089 27.176 43.770 1.00 13.15 ? 425 PRO A O 1 ATOM 2566 C CB . PRO A 1 343 ? 36.665 25.957 46.977 1.00 12.22 ? 425 PRO A CB 1 ATOM 2567 C CG . PRO A 1 343 ? 36.611 27.396 47.366 1.00 12.22 ? 425 PRO A CG 1 ATOM 2568 C CD . PRO A 1 343 ? 37.916 27.949 46.824 1.00 12.22 ? 425 PRO A CD 1 ATOM 2569 N N . GLN A 1 344 ? 35.147 25.270 44.519 1.00 14.00 ? 426 GLN A N 1 ATOM 2570 C CA . GLN A 1 344 ? 34.009 25.313 43.609 1.00 14.00 ? 426 GLN A CA 1 ATOM 2571 C C . GLN A 1 344 ? 33.197 26.588 43.839 1.00 14.00 ? 426 GLN A C 1 ATOM 2572 O O . GLN A 1 344 ? 33.198 27.145 44.938 1.00 14.00 ? 426 GLN A O 1 ATOM 2573 C CB . GLN A 1 344 ? 33.128 24.084 43.845 1.00 121.03 ? 426 GLN A CB 1 ATOM 2574 C CG . GLN A 1 344 ? 31.924 23.961 42.926 1.00 121.03 ? 426 GLN A CG 1 ATOM 2575 C CD . GLN A 1 344 ? 31.024 22.796 43.300 1.00 121.03 ? 426 GLN A CD 1 ATOM 2576 O OE1 . GLN A 1 344 ? 31.313 22.044 44.233 1.00 121.03 ? 426 GLN A OE1 1 ATOM 2577 N NE2 . GLN A 1 344 ? 29.922 22.645 42.575 1.00 121.03 ? 426 GLN A NE2 1 ATOM 2578 N N . ALA A 1 345 ? 32.528 27.059 42.791 1.00 11.24 ? 427 ALA A N 1 ATOM 2579 C CA . ALA A 1 345 ? 31.699 28.255 42.883 1.00 11.24 ? 427 ALA A CA 1 ATOM 2580 C C . ALA A 1 345 ? 30.663 28.087 43.994 1.00 11.24 ? 427 ALA A C 1 ATOM 2581 O O . ALA A 1 345 ? 30.067 27.018 44.145 1.00 11.24 ? 427 ALA A O 1 ATOM 2582 C CB . ALA A 1 345 ? 31.003 28.515 41.551 1.00 16.41 ? 427 ALA A CB 1 ATOM 2583 N N . GLY A 1 346 ? 30.508 29.121 44.813 1.00 9.56 ? 428 GLY A N 1 ATOM 2584 C CA . GLY A 1 346 ? 29.541 29.069 45.892 1.00 9.56 ? 428 GLY A CA 1 ATOM 2585 C C . GLY A 1 346 ? 30.072 28.457 47.172 1.00 9.56 ? 428 GLY A C 1 ATOM 2586 O O . GLY A 1 346 ? 29.474 28.640 48.228 1.00 9.56 ? 428 GLY A O 1 ATOM 2587 N N . ALA A 1 347 ? 31.179 27.722 47.086 1.00 9.30 ? 429 ALA A N 1 ATOM 2588 C CA . ALA A 1 347 ? 31.778 27.095 48.263 1.00 9.30 ? 429 ALA A CA 1 ATOM 2589 C C . ALA A 1 347 ? 32.507 28.140 49.107 1.00 9.30 ? 429 ALA A C 1 ATOM 2590 O O . ALA A 1 347 ? 32.906 29.182 48.596 1.00 9.30 ? 429 ALA A O 1 ATOM 2591 C CB . ALA A 1 347 ? 32.740 25.993 47.838 1.00 3.88 ? 429 ALA A CB 1 ATOM 2592 N N . TRP A 1 348 ? 32.685 27.869 50.397 1.00 7.68 ? 430 TRP A N 1 ATOM 2593 C CA . TRP A 1 348 ? 33.377 28.823 51.257 1.00 7.68 ? 430 TRP A CA 1 ATOM 2594 C C . TRP A 1 348 ? 34.849 28.925 50.850 1.00 7.68 ? 430 TRP A C 1 ATOM 2595 O O . TRP A 1 348 ? 35.518 27.914 50.637 1.00 7.68 ? 430 TRP A O 1 ATOM 2596 C CB . TRP A 1 348 ? 33.249 28.439 52.737 1.00 6.72 ? 430 TRP A CB 1 ATOM 2597 C CG . TRP A 1 348 ? 33.674 29.551 53.668 1.00 6.72 ? 430 TRP A CG 1 ATOM 2598 C CD1 . TRP A 1 348 ? 34.813 29.600 54.427 1.00 6.72 ? 430 TRP A CD1 1 ATOM 2599 C CD2 . TRP A 1 348 ? 32.993 30.790 53.890 1.00 6.72 ? 430 TRP A CD2 1 ATOM 2600 N NE1 . TRP A 1 348 ? 34.884 30.797 55.098 1.00 6.72 ? 430 TRP A NE1 1 ATOM 2601 C CE2 . TRP A 1 348 ? 33.780 31.548 54.786 1.00 6.72 ? 430 TRP A CE2 1 ATOM 2602 C CE3 . TRP A 1 348 ? 31.793 31.339 53.412 1.00 6.72 ? 430 TRP A CE3 1 ATOM 2603 C CZ2 . TRP A 1 348 ? 33.408 32.828 55.217 1.00 6.72 ? 430 TRP A CZ2 1 ATOM 2604 C CZ3 . TRP A 1 348 ? 31.423 32.610 53.838 1.00 6.72 ? 430 TRP A CZ3 1 ATOM 2605 C CH2 . TRP A 1 348 ? 32.230 33.340 54.732 1.00 6.72 ? 430 TRP A CH2 1 ATOM 2606 N N . PHE A 1 349 ? 35.334 30.157 50.739 1.00 9.57 ? 431 PHE A N 1 ATOM 2607 C CA . PHE A 1 349 ? 36.713 30.443 50.343 1.00 9.57 ? 431 PHE A CA 1 ATOM 2608 C C . PHE A 1 349 ? 37.339 31.299 51.456 1.00 9.57 ? 431 PHE A C 1 ATOM 2609 O O . PHE A 1 349 ? 37.386 32.524 51.367 1.00 9.57 ? 431 PHE A O 1 ATOM 2610 C CB . PHE A 1 349 ? 36.692 31.179 48.995 1.00 9.92 ? 431 PHE A CB 1 ATOM 2611 C CG . PHE A 1 349 ? 38.038 31.312 48.326 1.00 9.92 ? 431 PHE A CG 1 ATOM 2612 C CD1 . PHE A 1 349 ? 39.209 30.873 48.942 1.00 9.92 ? 431 PHE A CD1 1 ATOM 2613 C CD2 . PHE A 1 349 ? 38.130 31.915 47.072 1.00 9.92 ? 431 PHE A CD2 1 ATOM 2614 C CE1 . PHE A 1 349 ? 40.448 31.034 48.320 1.00 9.92 ? 431 PHE A CE1 1 ATOM 2615 C CE2 . PHE A 1 349 ? 39.364 32.080 46.446 1.00 9.92 ? 431 PHE A CE2 1 ATOM 2616 C CZ . PHE A 1 349 ? 40.524 31.640 47.072 1.00 9.92 ? 431 PHE A CZ 1 ATOM 2617 N N . GLN A 1 350 ? 37.835 30.617 52.488 1.00 9.00 ? 432 GLN A N 1 ATOM 2618 C CA . GLN A 1 350 ? 38.429 31.233 53.679 1.00 9.00 ? 432 GLN A CA 1 ATOM 2619 C C . GLN A 1 350 ? 39.457 32.331 53.438 1.00 9.00 ? 432 GLN A C 1 ATOM 2620 O O . GLN A 1 350 ? 39.356 33.411 54.014 1.00 9.00 ? 432 GLN A O 1 ATOM 2621 C CB . GLN A 1 350 ? 39.031 30.149 54.586 1.00 11.29 ? 432 GLN A CB 1 ATOM 2622 C CG . GLN A 1 350 ? 39.621 30.655 55.902 1.00 11.29 ? 432 GLN A CG 1 ATOM 2623 C CD . GLN A 1 350 ? 38.575 31.203 56.854 1.00 11.29 ? 432 GLN A CD 1 ATOM 2624 O OE1 . GLN A 1 350 ? 37.384 31.270 56.530 1.00 11.29 ? 432 GLN A OE1 1 ATOM 2625 N NE2 . GLN A 1 350 ? 39.018 31.608 58.041 1.00 11.29 ? 432 GLN A NE2 1 ATOM 2626 N N . ALA A 1 351 ? 40.459 32.045 52.615 1.00 7.45 ? 433 ALA A N 1 ATOM 2627 C CA . ALA A 1 351 ? 41.491 33.033 52.323 1.00 7.45 ? 433 ALA A CA 1 ATOM 2628 C C . ALA A 1 351 ? 40.881 34.295 51.713 1.00 7.45 ? 433 ALA A C 1 ATOM 2629 O O . ALA A 1 351 ? 41.344 35.400 51.986 1.00 7.45 ? 433 ALA A O 1 ATOM 2630 C CB . ALA A 1 351 ? 42.553 32.443 51.393 1.00 4.06 ? 433 ALA A CB 1 ATOM 2631 N N . TYR A 1 352 ? 39.825 34.136 50.916 1.00 4.96 ? 434 TYR A N 1 ATOM 2632 C CA . TYR A 1 352 ? 39.185 35.298 50.298 1.00 4.96 ? 434 TYR A CA 1 ATOM 2633 C C . TYR A 1 352 ? 38.408 36.116 51.324 1.00 4.96 ? 434 TYR A C 1 ATOM 2634 O O . TYR A 1 352 ? 38.414 37.348 51.276 1.00 4.96 ? 434 TYR A O 1 ATOM 2635 C CB . TYR A 1 352 ? 38.282 34.896 49.133 1.00 4.13 ? 434 TYR A CB 1 ATOM 2636 C CG . TYR A 1 352 ? 38.040 36.052 48.188 1.00 4.13 ? 434 TYR A CG 1 ATOM 2637 C CD1 . TYR A 1 352 ? 38.946 36.344 47.169 1.00 4.13 ? 434 TYR A CD1 1 ATOM 2638 C CD2 . TYR A 1 352 ? 36.944 36.893 48.352 1.00 4.13 ? 434 TYR A CD2 1 ATOM 2639 C CE1 . TYR A 1 352 ? 38.765 37.448 46.343 1.00 4.13 ? 434 TYR A CE1 1 ATOM 2640 C CE2 . TYR A 1 352 ? 36.754 37.998 47.533 1.00 4.13 ? 434 TYR A CE2 1 ATOM 2641 C CZ . TYR A 1 352 ? 37.666 38.272 46.532 1.00 4.13 ? 434 TYR A CZ 1 ATOM 2642 O OH . TYR A 1 352 ? 37.474 39.373 45.728 1.00 4.13 ? 434 TYR A OH 1 ATOM 2643 N N . PHE A 1 353 ? 37.758 35.425 52.260 1.00 7.79 ? 435 PHE A N 1 ATOM 2644 C CA . PHE A 1 353 ? 37.005 36.081 53.326 1.00 7.79 ? 435 PHE A CA 1 ATOM 2645 C C . PHE A 1 353 ? 37.951 36.921 54.185 1.00 7.79 ? 435 PHE A C 1 ATOM 2646 O O . PHE A 1 353 ? 37.652 38.077 54.503 1.00 7.79 ? 435 PHE A O 1 ATOM 2647 C CB . PHE A 1 353 ? 36.301 35.043 54.207 1.00 12.02 ? 435 PHE A CB 1 ATOM 2648 C CG . PHE A 1 353 ? 35.599 35.634 55.405 1.00 12.02 ? 435 PHE A CG 1 ATOM 2649 C CD1 . PHE A 1 353 ? 34.366 36.271 55.267 1.00 12.02 ? 435 PHE A CD1 1 ATOM 2650 C CD2 . PHE A 1 353 ? 36.169 35.554 56.673 1.00 12.02 ? 435 PHE A CD2 1 ATOM 2651 C CE1 . PHE A 1 353 ? 33.713 36.821 56.378 1.00 12.02 ? 435 PHE A CE1 1 ATOM 2652 C CE2 . PHE A 1 353 ? 35.527 36.098 57.784 1.00 12.02 ? 435 PHE A CE2 1 ATOM 2653 C CZ . PHE A 1 353 ? 34.297 36.733 57.636 1.00 12.02 ? 435 PHE A CZ 1 ATOM 2654 N N . VAL A 1 354 ? 39.087 36.334 54.565 1.00 10.14 ? 436 VAL A N 1 ATOM 2655 C CA . VAL A 1 354 ? 40.075 37.034 55.384 1.00 10.14 ? 436 VAL A CA 1 ATOM 2656 C C . VAL A 1 354 ? 40.583 38.281 54.656 1.00 10.14 ? 436 VAL A C 1 ATOM 2657 O O . VAL A 1 354 ? 40.786 39.329 55.273 1.00 10.14 ? 436 VAL A O 1 ATOM 2658 C CB . VAL A 1 354 ? 41.263 36.116 55.748 1.00 13.06 ? 436 VAL A CB 1 ATOM 2659 C CG1 . VAL A 1 354 ? 42.296 36.886 56.540 1.00 13.06 ? 436 VAL A CG1 1 ATOM 2660 C CG2 . VAL A 1 354 ? 40.774 34.915 56.551 1.00 13.06 ? 436 VAL A CG2 1 ATOM 2661 N N . GLN A 1 355 ? 40.765 38.168 53.341 1.00 9.84 ? 437 GLN A N 1 ATOM 2662 C CA . GLN A 1 355 ? 41.215 39.297 52.525 1.00 9.84 ? 437 GLN A CA 1 ATOM 2663 C C . GLN A 1 355 ? 40.209 40.444 52.615 1.00 9.84 ? 437 GLN A C 1 ATOM 2664 O O . GLN A 1 355 ? 40.582 41.589 52.886 1.00 9.84 ? 437 GLN A O 1 ATOM 2665 C CB . GLN A 1 355 ? 41.361 38.882 51.055 1.00 14.28 ? 437 GLN A CB 1 ATOM 2666 C CG . GLN A 1 355 ? 41.647 40.054 50.115 1.00 14.28 ? 437 GLN A CG 1 ATOM 2667 C CD . GLN A 1 355 ? 41.617 39.668 48.650 1.00 14.28 ? 437 GLN A CD 1 ATOM 2668 O OE1 . GLN A 1 355 ? 42.572 39.096 48.126 1.00 14.28 ? 437 GLN A OE1 1 ATOM 2669 N NE2 . GLN A 1 355 ? 40.525 40.006 47.973 1.00 14.28 ? 437 GLN A NE2 1 ATOM 2670 N N . LEU A 1 356 ? 38.936 40.127 52.380 1.00 4.65 ? 438 LEU A N 1 ATOM 2671 C CA . LEU A 1 356 ? 37.858 41.121 52.424 1.00 4.65 ? 438 LEU A CA 1 ATOM 2672 C C . LEU A 1 356 ? 37.769 41.789 53.789 1.00 4.65 ? 438 LEU A C 1 ATOM 2673 O O . LEU A 1 356 ? 37.589 43.005 53.885 1.00 4.65 ? 438 LEU A O 1 ATOM 2674 C CB . LEU A 1 356 ? 36.513 40.464 52.096 1.00 3.69 ? 438 LEU A CB 1 ATOM 2675 C CG . LEU A 1 356 ? 36.246 39.997 50.669 1.00 3.69 ? 438 LEU A CG 1 ATOM 2676 C CD1 . LEU A 1 356 ? 34.941 39.230 50.636 1.00 3.69 ? 438 LEU A CD1 1 ATOM 2677 C CD2 . LEU A 1 356 ? 36.183 41.180 49.739 1.00 3.69 ? 438 LEU A CD2 1 ATOM 2678 N N . LEU A 1 357 ? 37.909 40.981 54.837 1.00 9.74 ? 439 LEU A N 1 ATOM 2679 C CA . LEU A 1 357 ? 37.846 41.457 56.214 1.00 9.74 ? 439 LEU A CA 1 ATOM 2680 C C . LEU A 1 357 ? 39.011 42.401 56.518 1.00 9.74 ? 439 LEU A C 1 ATOM 2681 O O . LEU A 1 357 ? 38.833 43.440 57.148 1.00 9.74 ? 439 LEU A O 1 ATOM 2682 C CB . LEU A 1 357 ? 37.872 40.259 57.171 1.00 16.05 ? 439 LEU A CB 1 ATOM 2683 C CG . LEU A 1 357 ? 37.704 40.500 58.672 1.00 16.05 ? 439 LEU A CG 1 ATOM 2684 C CD1 . LEU A 1 357 ? 36.357 41.156 58.950 1.00 16.05 ? 439 LEU A CD1 1 ATOM 2685 C CD2 . LEU A 1 357 ? 37.813 39.181 59.416 1.00 16.05 ? 439 LEU A CD2 1 ATOM 2686 N N . THR A 1 358 ? 40.195 42.045 56.035 1.00 13.22 ? 440 THR A N 1 ATOM 2687 C CA . THR A 1 358 ? 41.394 42.841 56.254 1.00 13.22 ? 440 THR A CA 1 ATOM 2688 C C . THR A 1 358 ? 41.376 44.179 55.518 1.00 13.22 ? 440 THR A C 1 ATOM 2689 O O . THR A 1 358 ? 41.826 45.190 56.058 1.00 13.22 ? 440 THR A O 1 ATOM 2690 C CB . THR A 1 358 ? 42.659 42.046 55.845 1.00 20.52 ? 440 THR A CB 1 ATOM 2691 O OG1 . THR A 1 358 ? 42.781 40.883 56.677 1.00 20.52 ? 440 THR A OG1 1 ATOM 2692 C CG2 . THR A 1 358 ? 43.910 42.902 55.996 1.00 20.52 ? 440 THR A CG2 1 ATOM 2693 N N . ASN A 1 359 ? 40.844 44.177 54.297 1.00 9.16 ? 441 ASN A N 1 ATOM 2694 C CA . ASN A 1 359 ? 40.779 45.381 53.462 1.00 9.16 ? 441 ASN A CA 1 ATOM 2695 C C . ASN A 1 359 ? 39.463 46.154 53.568 1.00 9.16 ? 441 ASN A C 1 ATOM 2696 O O . ASN A 1 359 ? 39.240 47.098 52.799 1.00 9.16 ? 441 ASN A O 1 ATOM 2697 C CB . ASN A 1 359 ? 40.992 45.006 51.991 1.00 13.07 ? 441 ASN A CB 1 ATOM 2698 C CG . ASN A 1 359 ? 42.381 44.474 51.711 1.00 13.07 ? 441 ASN A CG 1 ATOM 2699 O OD1 . ASN A 1 359 ? 43.356 44.898 52.326 1.00 13.07 ? 441 ASN A OD1 1 ATOM 2700 N ND2 . ASN A 1 359 ? 42.481 43.561 50.755 1.00 13.07 ? 441 ASN A ND2 1 ATOM 2701 N N . ALA A 1 360 ? 38.595 45.755 54.497 1.00 7.74 ? 442 ALA A N 1 ATOM 2702 C CA . ALA A 1 360 ? 37.290 46.394 54.666 1.00 7.74 ? 442 ALA A CA 1 ATOM 2703 C C . ALA A 1 360 ? 37.327 47.904 54.900 1.00 7.74 ? 442 ALA A C 1 ATOM 2704 O O . ALA A 1 360 ? 38.218 48.423 55.580 1.00 7.74 ? 442 ALA A O 1 ATOM 2705 C CB . ALA A 1 360 ? 36.516 45.713 55.783 1.00 10.99 ? 442 ALA A CB 1 ATOM 2706 N N . ASN A 1 361 ? 36.347 48.597 54.322 1.00 10.44 ? 443 ASN A N 1 ATOM 2707 C CA . ASN A 1 361 ? 36.209 50.048 54.457 1.00 10.44 ? 443 ASN A CA 1 ATOM 2708 C C . ASN A 1 361 ? 34.749 50.428 54.186 1.00 10.44 ? 443 ASN A C 1 ATOM 2709 O O . ASN A 1 361 ? 34.296 50.383 53.043 1.00 10.44 ? 443 ASN A O 1 ATOM 2710 C CB . ASN A 1 361 ? 37.132 50.779 53.478 1.00 22.05 ? 443 ASN A CB 1 ATOM 2711 C CG . ASN A 1 361 ? 37.006 52.291 53.571 1.00 22.05 ? 443 ASN A CG 1 ATOM 2712 O OD1 . ASN A 1 361 ? 36.585 52.831 54.593 1.00 22.05 ? 443 ASN A OD1 1 ATOM 2713 N ND2 . ASN A 1 361 ? 37.365 52.980 52.494 1.00 22.05 ? 443 ASN A ND2 1 ATOM 2714 N N . PRO A 1 362 ? 33.990 50.806 55.236 1.00 10.06 ? 444 PRO A N 1 ATOM 2715 C CA . PRO A 1 362 ? 34.345 50.929 56.657 1.00 10.06 ? 444 PRO A CA 1 ATOM 2716 C C . PRO A 1 362 ? 34.972 49.667 57.243 1.00 10.06 ? 444 PRO A C 1 ATOM 2717 O O . PRO A 1 362 ? 34.609 48.549 56.877 1.00 10.06 ? 444 PRO A O 1 ATOM 2718 C CB . PRO A 1 362 ? 32.999 51.217 57.329 1.00 11.88 ? 444 PRO A CB 1 ATOM 2719 C CG . PRO A 1 362 ? 32.201 51.855 56.269 1.00 11.88 ? 444 PRO A CG 1 ATOM 2720 C CD . PRO A 1 362 ? 32.559 51.086 55.033 1.00 11.88 ? 444 PRO A CD 1 ATOM 2721 N N . SER A 1 363 ? 35.916 49.863 58.153 1.00 9.80 ? 445 SER A N 1 ATOM 2722 C CA . SER A 1 363 ? 36.610 48.757 58.797 1.00 9.80 ? 445 SER A CA 1 ATOM 2723 C C . SER A 1 363 ? 35.763 48.044 59.850 1.00 9.80 ? 445 SER A C 1 ATOM 2724 O O . SER A 1 363 ? 34.865 48.632 60.447 1.00 9.80 ? 445 SER A O 1 ATOM 2725 C CB . SER A 1 363 ? 37.901 49.273 59.446 1.00 16.31 ? 445 SER A CB 1 ATOM 2726 O OG . SER A 1 363 ? 38.599 48.231 60.107 1.00 16.31 ? 445 SER A OG 1 ATOM 2727 N N . PHE A 1 364 ? 36.028 46.756 60.030 1.00 12.74 ? 446 PHE A N 1 ATOM 2728 C CA . PHE A 1 364 ? 35.345 45.956 61.037 1.00 12.74 ? 446 PHE A CA 1 ATOM 2729 C C . PHE A 1 364 ? 36.293 45.817 62.224 1.00 12.74 ? 446 PHE A C 1 ATOM 2730 O O . PHE A 1 364 ? 35.862 45.614 63.360 1.00 12.74 ? 446 PHE A O 1 ATOM 2731 C CB . PHE A 1 364 ? 35.003 44.572 60.490 1.00 14.15 ? 446 PHE A CB 1 ATOM 2732 C CG . PHE A 1 364 ? 33.807 44.556 59.593 1.00 14.15 ? 446 PHE A CG 1 ATOM 2733 C CD1 . PHE A 1 364 ? 32.523 44.510 60.132 1.00 14.15 ? 446 PHE A CD1 1 ATOM 2734 C CD2 . PHE A 1 364 ? 33.956 44.588 58.211 1.00 14.15 ? 446 PHE A CD2 1 ATOM 2735 C CE1 . PHE A 1 364 ? 31.404 44.498 59.301 1.00 14.15 ? 446 PHE A CE1 1 ATOM 2736 C CE2 . PHE A 1 364 ? 32.846 44.576 57.377 1.00 14.15 ? 446 PHE A CE2 1 ATOM 2737 C CZ . PHE A 1 364 ? 31.569 44.529 57.923 1.00 14.15 ? 446 PHE A CZ 1 ATOM 2738 N N . LEU A 1 365 ? 37.587 45.913 61.938 1.00 32.79 ? 447 LEU A N 1 ATOM 2739 C CA . LEU A 1 365 ? 38.629 45.810 62.948 1.00 32.79 ? 447 LEU A CA 1 ATOM 2740 C C . LEU A 1 365 ? 38.840 47.142 63.660 1.00 32.79 ? 447 LEU A C 1 ATOM 2741 O O . LEU A 1 365 ? 38.784 48.194 62.987 1.00 32.79 ? 447 LEU A O 1 ATOM 2742 C CB . LEU A 1 365 ? 39.936 45.344 62.299 1.00 20.50 ? 447 LEU A CB 1 ATOM 2743 C CG . LEU A 1 365 ? 39.949 43.897 61.797 1.00 20.50 ? 447 LEU A CG 1 ATOM 2744 C CD1 . LEU A 1 365 ? 41.053 43.698 60.774 1.00 20.50 ? 447 LEU A CD1 1 ATOM 2745 C CD2 . LEU A 1 365 ? 40.120 42.954 62.972 1.00 20.50 ? 447 LEU A CD2 1 ATOM 2746 O OXT . LEU A 1 365 ? 39.053 47.119 64.890 1.00 32.79 ? 447 LEU A OXT 1 ATOM 2747 N N . THR B 1 3 ? 15.641 92.903 100.886 1.00 62.80 ? 85 THR B N 1 ATOM 2748 C CA . THR B 1 3 ? 17.064 93.338 100.782 1.00 62.80 ? 85 THR B CA 1 ATOM 2749 C C . THR B 1 3 ? 17.854 92.551 99.736 1.00 62.80 ? 85 THR B C 1 ATOM 2750 O O . THR B 1 3 ? 18.952 92.954 99.356 1.00 62.80 ? 85 THR B O 1 ATOM 2751 C CB . THR B 1 3 ? 17.785 93.240 102.145 1.00 91.15 ? 85 THR B CB 1 ATOM 2752 O OG1 . THR B 1 3 ? 17.717 91.895 102.634 1.00 91.15 ? 85 THR B OG1 1 ATOM 2753 C CG2 . THR B 1 3 ? 17.141 94.177 103.157 1.00 91.15 ? 85 THR B CG2 1 ATOM 2754 N N . ALA B 1 4 ? 17.308 91.420 99.293 1.00 16.63 ? 86 ALA B N 1 ATOM 2755 C CA . ALA B 1 4 ? 17.963 90.602 98.272 1.00 16.63 ? 86 ALA B CA 1 ATOM 2756 C C . ALA B 1 4 ? 17.903 91.343 96.941 1.00 16.63 ? 86 ALA B C 1 ATOM 2757 O O . ALA B 1 4 ? 18.891 91.410 96.217 1.00 16.63 ? 86 ALA B O 1 ATOM 2758 C CB . ALA B 1 4 ? 17.282 89.255 98.153 1.00 19.12 ? 86 ALA B CB 1 ATOM 2759 N N . THR B 1 5 ? 16.739 91.890 96.611 1.00 10.71 ? 87 THR B N 1 ATOM 2760 C CA . THR B 1 5 ? 16.593 92.639 95.368 1.00 10.71 ? 87 THR B CA 1 ATOM 2761 C C . THR B 1 5 ? 17.147 94.047 95.564 1.00 10.71 ? 87 THR B C 1 ATOM 2762 O O . THR B 1 5 ? 17.300 94.508 96.697 1.00 10.71 ? 87 THR B O 1 ATOM 2763 C CB . THR B 1 5 ? 15.135 92.701 94.909 1.00 21.46 ? 87 THR B CB 1 ATOM 2764 O OG1 . THR B 1 5 ? 14.330 93.257 95.950 1.00 21.46 ? 87 THR B OG1 1 ATOM 2765 C CG2 . THR B 1 5 ? 14.638 91.315 94.547 1.00 21.46 ? 87 THR B CG2 1 ATOM 2766 N N . TYR B 1 6 ? 17.409 94.749 94.467 1.00 12.29 ? 88 TYR B N 1 ATOM 2767 C CA . TYR B 1 6 ? 18.001 96.082 94.555 1.00 12.29 ? 88 TYR B CA 1 ATOM 2768 C C . TYR B 1 6 ? 17.659 96.958 93.356 1.00 12.29 ? 88 TYR B C 1 ATOM 2769 O O . TYR B 1 6 ? 17.108 96.494 92.359 1.00 12.29 ? 88 TYR B O 1 ATOM 2770 C CB . TYR B 1 6 ? 19.531 95.945 94.610 1.00 6.55 ? 88 TYR B CB 1 ATOM 2771 C CG . TYR B 1 6 ? 20.088 95.309 93.353 1.00 6.55 ? 88 TYR B CG 1 ATOM 2772 C CD1 . TYR B 1 6 ? 20.073 93.923 93.191 1.00 6.55 ? 88 TYR B CD1 1 ATOM 2773 C CD2 . TYR B 1 6 ? 20.527 96.092 92.283 1.00 6.55 ? 88 TYR B CD2 1 ATOM 2774 C CE1 . TYR B 1 6 ? 20.465 93.332 91.989 1.00 6.55 ? 88 TYR B CE1 1 ATOM 2775 C CE2 . TYR B 1 6 ? 20.921 95.513 91.079 1.00 6.55 ? 88 TYR B CE2 1 ATOM 2776 C CZ . TYR B 1 6 ? 20.882 94.132 90.940 1.00 6.55 ? 88 TYR B CZ 1 ATOM 2777 O OH . TYR B 1 6 ? 21.227 93.553 89.743 1.00 6.55 ? 88 TYR B OH 1 ATOM 2778 N N . SER B 1 7 ? 18.039 98.224 93.460 1.00 24.43 ? 89 SER B N 1 ATOM 2779 C CA . SER B 1 7 ? 17.857 99.192 92.392 1.00 24.43 ? 89 SER B CA 1 ATOM 2780 C C . SER B 1 7 ? 19.179 99.954 92.370 1.00 24.43 ? 89 SER B C 1 ATOM 2781 O O . SER B 1 7 ? 19.724 100.292 93.425 1.00 24.43 ? 89 SER B O 1 ATOM 2782 C CB . SER B 1 7 ? 16.692 100.142 92.689 1.00 72.23 ? 89 SER B CB 1 ATOM 2783 O OG . SER B 1 7 ? 16.974 101.000 93.782 1.00 72.23 ? 89 SER B OG 1 ATOM 2784 N N . GLY B 1 8 ? 19.735 100.148 91.179 1.00 11.42 ? 90 GLY B N 1 ATOM 2785 C CA . GLY B 1 8 ? 20.994 100.857 91.071 1.00 11.42 ? 90 GLY B CA 1 ATOM 2786 C C . GLY B 1 8 ? 22.181 99.986 91.435 1.00 11.42 ? 90 GLY B C 1 ATOM 2787 O O . GLY B 1 8 ? 22.181 98.786 91.166 1.00 11.42 ? 90 GLY B O 1 ATOM 2788 N N . ASN B 1 9 ? 23.190 100.604 92.046 1.00 9.11 ? 91 ASN B N 1 ATOM 2789 C CA . ASN B 1 9 ? 24.421 99.935 92.462 1.00 9.11 ? 91 ASN B CA 1 ATOM 2790 C C . ASN B 1 9 ? 24.137 98.782 93.431 1.00 9.11 ? 91 ASN B C 1 ATOM 2791 O O . ASN B 1 9 ? 23.761 99.007 94.577 1.00 9.11 ? 91 ASN B O 1 ATOM 2792 C CB . ASN B 1 9 ? 25.354 100.966 93.116 1.00 3.56 ? 91 ASN B CB 1 ATOM 2793 C CG . ASN B 1 9 ? 26.735 100.410 93.427 1.00 3.56 ? 91 ASN B CG 1 ATOM 2794 O OD1 . ASN B 1 9 ? 26.959 99.200 93.396 1.00 3.56 ? 91 ASN B OD1 1 ATOM 2795 N ND2 . ASN B 1 9 ? 27.666 101.299 93.742 1.00 3.56 ? 91 ASN B ND2 1 ATOM 2796 N N . PRO B 1 10 ? 24.370 97.536 92.993 1.00 6.49 ? 92 PRO B N 1 ATOM 2797 C CA . PRO B 1 10 ? 24.138 96.344 93.815 1.00 6.49 ? 92 PRO B CA 1 ATOM 2798 C C . PRO B 1 10 ? 25.064 96.194 95.018 1.00 6.49 ? 92 PRO B C 1 ATOM 2799 O O . PRO B 1 10 ? 24.832 95.349 95.884 1.00 6.49 ? 92 PRO B O 1 ATOM 2800 C CB . PRO B 1 10 ? 24.308 95.201 92.819 1.00 10.03 ? 92 PRO B CB 1 ATOM 2801 C CG . PRO B 1 10 ? 25.298 95.736 91.849 1.00 10.03 ? 92 PRO B CG 1 ATOM 2802 C CD . PRO B 1 10 ? 24.864 97.165 91.656 1.00 10.03 ? 92 PRO B CD 1 ATOM 2803 N N . PHE B 1 11 ? 26.116 97.007 95.064 1.00 13.59 ? 93 PHE B N 1 ATOM 2804 C CA . PHE B 1 11 ? 27.059 96.964 96.172 1.00 13.59 ? 93 PHE B CA 1 ATOM 2805 C C . PHE B 1 11 ? 26.590 97.838 97.328 1.00 13.59 ? 93 PHE B C 1 ATOM 2806 O O . PHE B 1 11 ? 27.114 97.740 98.435 1.00 13.59 ? 93 PHE B O 1 ATOM 2807 C CB . PHE B 1 11 ? 28.460 97.390 95.713 1.00 8.52 ? 93 PHE B CB 1 ATOM 2808 C CG . PHE B 1 11 ? 29.176 96.337 94.906 1.00 8.52 ? 93 PHE B CG 1 ATOM 2809 C CD1 . PHE B 1 11 ? 29.967 95.376 95.537 1.00 8.52 ? 93 PHE B CD1 1 ATOM 2810 C CD2 . PHE B 1 11 ? 29.036 96.286 93.521 1.00 8.52 ? 93 PHE B CD2 1 ATOM 2811 C CE1 . PHE B 1 11 ? 30.603 94.379 94.801 1.00 8.52 ? 93 PHE B CE1 1 ATOM 2812 C CE2 . PHE B 1 11 ? 29.666 95.292 92.778 1.00 8.52 ? 93 PHE B CE2 1 ATOM 2813 C CZ . PHE B 1 11 ? 30.452 94.336 93.418 1.00 8.52 ? 93 PHE B CZ 1 ATOM 2814 N N . VAL B 1 12 ? 25.602 98.691 97.064 1.00 13.65 ? 94 VAL B N 1 ATOM 2815 C CA . VAL B 1 12 ? 25.059 99.572 98.092 1.00 13.65 ? 94 VAL B CA 1 ATOM 2816 C C . VAL B 1 12 ? 23.959 98.844 98.859 1.00 13.65 ? 94 VAL B C 1 ATOM 2817 O O . VAL B 1 12 ? 23.042 98.287 98.254 1.00 13.65 ? 94 VAL B O 1 ATOM 2818 C CB . VAL B 1 12 ? 24.481 100.869 97.478 1.00 19.12 ? 94 VAL B CB 1 ATOM 2819 C CG1 . VAL B 1 12 ? 23.845 101.730 98.559 1.00 19.12 ? 94 VAL B CG1 1 ATOM 2820 C CG2 . VAL B 1 12 ? 25.579 101.652 96.783 1.00 19.12 ? 94 VAL B CG2 1 ATOM 2821 N N . GLY B 1 13 ? 24.071 98.828 100.186 1.00 20.83 ? 95 GLY B N 1 ATOM 2822 C CA . GLY B 1 13 ? 23.069 98.170 101.007 1.00 20.83 ? 95 GLY B CA 1 ATOM 2823 C C . GLY B 1 13 ? 23.448 96.794 101.528 1.00 20.83 ? 95 GLY B C 1 ATOM 2824 O O . GLY B 1 13 ? 22.663 96.165 102.236 1.00 20.83 ? 95 GLY B O 1 ATOM 2825 N N . VAL B 1 14 ? 24.632 96.313 101.159 1.00 11.89 ? 96 VAL B N 1 ATOM 2826 C CA . VAL B 1 14 ? 25.113 95.008 101.608 1.00 11.89 ? 96 VAL B CA 1 ATOM 2827 C C . VAL B 1 14 ? 26.606 95.058 101.875 1.00 11.89 ? 96 VAL B C 1 ATOM 2828 O O . VAL B 1 14 ? 27.275 96.039 101.555 1.00 11.89 ? 96 VAL B O 1 ATOM 2829 C CB . VAL B 1 14 ? 24.862 93.882 100.565 1.00 16.17 ? 96 VAL B CB 1 ATOM 2830 C CG1 . VAL B 1 14 ? 23.388 93.543 100.479 1.00 16.17 ? 96 VAL B CG1 1 ATOM 2831 C CG2 . VAL B 1 14 ? 25.410 94.285 99.200 1.00 16.17 ? 96 VAL B CG2 1 ATOM 2832 N N . THR B 1 15 ? 27.118 93.980 102.457 1.00 9.64 ? 97 THR B N 1 ATOM 2833 C CA . THR B 1 15 ? 28.534 93.853 102.763 1.00 9.64 ? 97 THR B CA 1 ATOM 2834 C C . THR B 1 15 ? 28.975 92.554 102.108 1.00 9.64 ? 97 THR B C 1 ATOM 2835 O O . THR B 1 15 ? 28.373 91.505 102.338 1.00 9.64 ? 97 THR B O 1 ATOM 2836 C CB . THR B 1 15 ? 28.777 93.767 104.293 1.00 15.95 ? 97 THR B CB 1 ATOM 2837 O OG1 . THR B 1 15 ? 28.292 94.963 104.919 1.00 15.95 ? 97 THR B OG1 1 ATOM 2838 C CG2 . THR B 1 15 ? 30.262 93.608 104.596 1.00 15.95 ? 97 THR B CG2 1 ATOM 2839 N N . PRO B 1 16 ? 29.981 92.620 101.217 1.00 9.18 ? 98 PRO B N 1 ATOM 2840 C CA . PRO B 1 16 ? 30.465 91.412 100.545 1.00 9.18 ? 98 PRO B CA 1 ATOM 2841 C C . PRO B 1 16 ? 31.023 90.414 101.563 1.00 9.18 ? 98 PRO B C 1 ATOM 2842 O O . PRO B 1 16 ? 31.678 90.791 102.537 1.00 9.18 ? 98 PRO B O 1 ATOM 2843 C CB . PRO B 1 16 ? 31.554 91.949 99.617 1.00 9.94 ? 98 PRO B CB 1 ATOM 2844 C CG . PRO B 1 16 ? 31.102 93.343 99.331 1.00 9.94 ? 98 PRO B CG 1 ATOM 2845 C CD . PRO B 1 16 ? 30.653 93.816 100.685 1.00 9.94 ? 98 PRO B CD 1 ATOM 2846 N N . TRP B 1 17 ? 30.732 89.144 101.330 1.00 8.09 ? 99 TRP B N 1 ATOM 2847 C CA . TRP B 1 17 ? 31.153 88.063 102.206 1.00 8.09 ? 99 TRP B CA 1 ATOM 2848 C C . TRP B 1 17 ? 32.598 87.622 101.998 1.00 8.09 ? 99 TRP B C 1 ATOM 2849 O O . TRP B 1 17 ? 33.052 87.473 100.865 1.00 8.09 ? 99 TRP B O 1 ATOM 2850 C CB . TRP B 1 17 ? 30.212 86.877 101.976 1.00 8.12 ? 99 TRP B CB 1 ATOM 2851 C CG . TRP B 1 17 ? 30.520 85.634 102.743 1.00 8.12 ? 99 TRP B CG 1 ATOM 2852 C CD1 . TRP B 1 17 ? 31.008 84.463 102.239 1.00 8.12 ? 99 TRP B CD1 1 ATOM 2853 C CD2 . TRP B 1 17 ? 30.290 85.407 104.136 1.00 8.12 ? 99 TRP B CD2 1 ATOM 2854 N NE1 . TRP B 1 17 ? 31.086 83.517 103.229 1.00 8.12 ? 99 TRP B NE1 1 ATOM 2855 C CE2 . TRP B 1 17 ? 30.651 84.068 104.405 1.00 8.12 ? 99 TRP B CE2 1 ATOM 2856 C CE3 . TRP B 1 17 ? 29.802 86.201 105.182 1.00 8.12 ? 99 TRP B CE3 1 ATOM 2857 C CZ2 . TRP B 1 17 ? 30.542 83.503 105.680 1.00 8.12 ? 99 TRP B CZ2 1 ATOM 2858 C CZ3 . TRP B 1 17 ? 29.694 85.641 106.452 1.00 8.12 ? 99 TRP B CZ3 1 ATOM 2859 C CH2 . TRP B 1 17 ? 30.062 84.301 106.688 1.00 8.12 ? 99 TRP B CH2 1 ATOM 2860 N N . ALA B 1 18 ? 33.327 87.449 103.099 1.00 9.42 ? 100 ALA B N 1 ATOM 2861 C CA . ALA B 1 18 ? 34.705 86.962 103.032 1.00 9.42 ? 100 ALA B CA 1 ATOM 2862 C C . ALA B 1 18 ? 34.556 85.453 103.231 1.00 9.42 ? 100 ALA B C 1 ATOM 2863 O O . ALA B 1 18 ? 34.304 84.988 104.345 1.00 9.42 ? 100 ALA B O 1 ATOM 2864 C CB . ALA B 1 18 ? 35.550 87.575 104.143 1.00 10.51 ? 100 ALA B CB 1 ATOM 2865 N N . ASN B 1 19 ? 34.676 84.697 102.144 1.00 8.54 ? 101 ASN B N 1 ATOM 2866 C CA . ASN B 1 19 ? 34.492 83.248 102.192 1.00 8.54 ? 101 ASN B CA 1 ATOM 2867 C C . ASN B 1 19 ? 35.461 82.433 103.046 1.00 8.54 ? 101 ASN B C 1 ATOM 2868 O O . ASN B 1 19 ? 36.609 82.833 103.283 1.00 8.54 ? 101 ASN B O 1 ATOM 2869 C CB . ASN B 1 19 ? 34.380 82.664 100.777 1.00 10.17 ? 101 ASN B CB 1 ATOM 2870 C CG . ASN B 1 19 ? 35.685 82.715 100.005 1.00 10.17 ? 101 ASN B CG 1 ATOM 2871 O OD1 . ASN B 1 19 ? 36.490 81.792 100.075 1.00 10.17 ? 101 ASN B OD1 1 ATOM 2872 N ND2 . ASN B 1 19 ? 35.883 83.779 99.237 1.00 10.17 ? 101 ASN B ND2 1 ATOM 2873 N N . ALA B 1 20 ? 34.983 81.272 103.488 1.00 12.05 ? 102 ALA B N 1 ATOM 2874 C CA . ALA B 1 20 ? 35.751 80.365 104.334 1.00 12.05 ? 102 ALA B CA 1 ATOM 2875 C C . ALA B 1 20 ? 36.851 79.624 103.587 1.00 12.05 ? 102 ALA B C 1 ATOM 2876 O O . ALA B 1 20 ? 37.835 79.195 104.188 1.00 12.05 ? 102 ALA B O 1 ATOM 2877 C CB . ALA B 1 20 ? 34.815 79.365 105.006 1.00 25.70 ? 102 ALA B CB 1 ATOM 2878 N N . TYR B 1 21 ? 36.675 79.465 102.279 1.00 10.97 ? 103 TYR B N 1 ATOM 2879 C CA . TYR B 1 21 ? 37.646 78.773 101.442 1.00 10.97 ? 103 TYR B CA 1 ATOM 2880 C C . TYR B 1 21 ? 38.992 79.494 101.444 1.00 10.97 ? 103 TYR B C 1 ATOM 2881 O O . TYR B 1 21 ? 40.032 78.890 101.709 1.00 10.97 ? 103 TYR B O 1 ATOM 2882 C CB . TYR B 1 21 ? 37.117 78.671 100.009 1.00 23.99 ? 103 TYR B CB 1 ATOM 2883 C CG . TYR B 1 21 ? 38.024 77.918 99.070 1.00 23.99 ? 103 TYR B CG 1 ATOM 2884 C CD1 . TYR B 1 21 ? 37.911 76.539 98.930 1.00 23.99 ? 103 TYR B CD1 1 ATOM 2885 C CD2 . TYR B 1 21 ? 39.000 78.583 98.323 1.00 23.99 ? 103 TYR B CD2 1 ATOM 2886 C CE1 . TYR B 1 21 ? 38.744 75.833 98.067 1.00 23.99 ? 103 TYR B CE1 1 ATOM 2887 C CE2 . TYR B 1 21 ? 39.841 77.887 97.459 1.00 23.99 ? 103 TYR B CE2 1 ATOM 2888 C CZ . TYR B 1 21 ? 39.705 76.511 97.337 1.00 23.99 ? 103 TYR B CZ 1 ATOM 2889 O OH . TYR B 1 21 ? 40.521 75.810 96.481 1.00 23.99 ? 103 TYR B OH 1 ATOM 2890 N N . TYR B 1 22 ? 38.967 80.782 101.124 1.00 8.30 ? 104 TYR B N 1 ATOM 2891 C CA . TYR B 1 22 ? 40.180 81.581 101.092 1.00 8.30 ? 104 TYR B CA 1 ATOM 2892 C C . TYR B 1 22 ? 40.731 81.730 102.505 1.00 8.30 ? 104 TYR B C 1 ATOM 2893 O O . TYR B 1 22 ? 41.939 81.646 102.719 1.00 8.30 ? 104 TYR B O 1 ATOM 2894 C CB . TYR B 1 22 ? 39.896 82.953 100.475 1.00 9.59 ? 104 TYR B CB 1 ATOM 2895 C CG . TYR B 1 22 ? 41.119 83.827 100.341 1.00 9.59 ? 104 TYR B CG 1 ATOM 2896 C CD1 . TYR B 1 22 ? 42.130 83.516 99.432 1.00 9.59 ? 104 TYR B CD1 1 ATOM 2897 C CD2 . TYR B 1 22 ? 41.274 84.956 101.139 1.00 9.59 ? 104 TYR B CD2 1 ATOM 2898 C CE1 . TYR B 1 22 ? 43.272 84.314 99.324 1.00 9.59 ? 104 TYR B CE1 1 ATOM 2899 C CE2 . TYR B 1 22 ? 42.406 85.757 101.042 1.00 9.59 ? 104 TYR B CE2 1 ATOM 2900 C CZ . TYR B 1 22 ? 43.398 85.430 100.132 1.00 9.59 ? 104 TYR B CZ 1 ATOM 2901 O OH . TYR B 1 22 ? 44.502 86.238 100.040 1.00 9.59 ? 104 TYR B OH 1 ATOM 2902 N N . ALA B 1 23 ? 39.838 81.916 103.474 1.00 9.16 ? 105 ALA B N 1 ATOM 2903 C CA . ALA B 1 23 ? 40.245 82.067 104.868 1.00 9.16 ? 105 ALA B CA 1 ATOM 2904 C C . ALA B 1 23 ? 40.974 80.817 105.352 1.00 9.16 ? 105 ALA B C 1 ATOM 2905 O O . ALA B 1 23 ? 41.919 80.911 106.132 1.00 9.16 ? 105 ALA B O 1 ATOM 2906 C CB . ALA B 1 23 ? 39.044 82.358 105.744 1.00 8.78 ? 105 ALA B CB 1 ATOM 2907 N N . SER B 1 24 ? 40.549 79.654 104.867 1.00 12.73 ? 106 SER B N 1 ATOM 2908 C CA . SER B 1 24 ? 41.186 78.401 105.248 1.00 12.73 ? 106 SER B CA 1 ATOM 2909 C C . SER B 1 24 ? 42.603 78.345 104.687 1.00 12.73 ? 106 SER B C 1 ATOM 2910 O O . SER B 1 24 ? 43.538 77.955 105.391 1.00 12.73 ? 106 SER B O 1 ATOM 2911 C CB . SER B 1 24 ? 40.384 77.189 104.761 1.00 13.82 ? 106 SER B CB 1 ATOM 2912 O OG . SER B 1 24 ? 41.184 76.020 104.963 1.00 13.82 ? 106 SER B OG 1 ATOM 2913 N N . GLU B 1 25 ? 42.761 78.741 103.426 1.00 10.73 ? 107 GLU B N 1 ATOM 2914 C CA . GLU B 1 25 ? 44.078 78.756 102.787 1.00 10.73 ? 107 GLU B CA 1 ATOM 2915 C C . GLU B 1 25 ? 45.060 79.630 103.560 1.00 10.73 ? 107 GLU B C 1 ATOM 2916 O O . GLU B 1 25 ? 46.190 79.227 103.816 1.00 10.73 ? 107 GLU B O 1 ATOM 2917 C CB . GLU B 1 25 ? 43.979 79.281 101.355 1.00 9.80 ? 107 GLU B CB 1 ATOM 2918 C CG . GLU B 1 25 ? 43.165 78.416 100.417 1.00 9.80 ? 107 GLU B CG 1 ATOM 2919 C CD . GLU B 1 25 ? 43.123 78.984 99.019 1.00 9.80 ? 107 GLU B CD 1 ATOM 2920 O OE1 . GLU B 1 25 ? 42.622 80.116 98.854 1.00 9.80 ? 107 GLU B OE1 1 ATOM 2921 O OE2 . GLU B 1 25 ? 43.600 78.304 98.089 1.00 9.80 ? 107 GLU B OE2 1 ATOM 2922 N N . VAL B 1 26 ? 44.622 80.827 103.931 1.00 7.59 ? 108 VAL B N 1 ATOM 2923 C CA . VAL B 1 26 ? 45.469 81.751 104.675 1.00 7.59 ? 108 VAL B CA 1 ATOM 2924 C C . VAL B 1 26 ? 45.826 81.221 106.066 1.00 7.59 ? 108 VAL B C 1 ATOM 2925 O O . VAL B 1 26 ? 47.000 81.143 106.424 1.00 7.59 ? 108 VAL B O 1 ATOM 2926 C CB . VAL B 1 26 ? 44.794 83.136 104.817 1.00 11.96 ? 108 VAL B CB 1 ATOM 2927 C CG1 . VAL B 1 26 ? 45.658 84.064 105.660 1.00 11.96 ? 108 VAL B CG1 1 ATOM 2928 C CG2 . VAL B 1 26 ? 44.552 83.751 103.440 1.00 11.96 ? 108 VAL B CG2 1 ATOM 2929 N N . SER B 1 27 ? 44.820 80.817 106.832 1.00 12.48 ? 109 SER B N 1 ATOM 2930 C CA . SER B 1 27 ? 45.051 80.318 108.185 1.00 12.48 ? 109 SER B CA 1 ATOM 2931 C C . SER B 1 27 ? 45.758 78.973 108.289 1.00 12.48 ? 109 SER B C 1 ATOM 2932 O O . SER B 1 27 ? 46.578 78.775 109.185 1.00 12.48 ? 109 SER B O 1 ATOM 2933 C CB . SER B 1 27 ? 43.736 80.274 108.958 1.00 12.37 ? 109 SER B CB 1 ATOM 2934 O OG . SER B 1 27 ? 43.204 81.595 109.002 1.00 12.37 ? 109 SER B OG 1 ATOM 2935 N N . SER B 1 28 ? 45.492 78.074 107.346 1.00 16.93 ? 110 SER B N 1 ATOM 2936 C CA . SER B 1 28 ? 46.087 76.743 107.378 1.00 16.93 ? 110 SER B CA 1 ATOM 2937 C C . SER B 1 28 ? 47.309 76.482 106.518 1.00 16.93 ? 110 SER B C 1 ATOM 2938 O O . SER B 1 28 ? 48.063 75.545 106.785 1.00 16.93 ? 110 SER B O 1 ATOM 2939 C CB . SER B 1 28 ? 45.016 75.694 107.104 1.00 15.02 ? 110 SER B CB 1 ATOM 2940 O OG . SER B 1 28 ? 44.117 75.703 108.208 1.00 15.02 ? 110 SER B OG 1 ATOM 2941 N N . LEU B 1 29 ? 47.512 77.299 105.492 1.00 17.67 ? 111 LEU B N 1 ATOM 2942 C CA . LEU B 1 29 ? 48.653 77.115 104.612 1.00 17.67 ? 111 LEU B CA 1 ATOM 2943 C C . LEU B 1 29 ? 49.681 78.235 104.719 1.00 17.67 ? 111 LEU B C 1 ATOM 2944 O O . LEU B 1 29 ? 50.868 78.000 104.523 1.00 17.67 ? 111 LEU B O 1 ATOM 2945 C CB . LEU B 1 29 ? 48.191 76.977 103.157 1.00 17.21 ? 111 LEU B CB 1 ATOM 2946 C CG . LEU B 1 29 ? 47.124 75.928 102.828 1.00 17.21 ? 111 LEU B CG 1 ATOM 2947 C CD1 . LEU B 1 29 ? 46.838 75.942 101.336 1.00 17.21 ? 111 LEU B CD1 1 ATOM 2948 C CD2 . LEU B 1 29 ? 47.578 74.548 103.262 1.00 17.21 ? 111 LEU B CD2 1 ATOM 2949 N N . ALA B 1 30 ? 49.232 79.445 105.041 1.00 12.14 ? 112 ALA B N 1 ATOM 2950 C CA . ALA B 1 30 ? 50.130 80.589 105.138 1.00 12.14 ? 112 ALA B CA 1 ATOM 2951 C C . ALA B 1 30 ? 50.605 80.916 106.550 1.00 12.14 ? 112 ALA B C 1 ATOM 2952 O O . ALA B 1 30 ? 51.809 80.944 106.822 1.00 12.14 ? 112 ALA B O 1 ATOM 2953 C CB . ALA B 1 30 ? 49.472 81.814 104.513 1.00 2.00 ? 112 ALA B CB 1 ATOM 2954 N N . ILE B 1 31 ? 49.656 81.139 107.451 1.00 15.97 ? 113 ILE B N 1 ATOM 2955 C CA . ILE B 1 31 ? 49.969 81.505 108.827 1.00 15.97 ? 113 ILE B CA 1 ATOM 2956 C C . ILE B 1 31 ? 50.928 80.566 109.572 1.00 15.97 ? 113 ILE B C 1 ATOM 2957 O O . ILE B 1 31 ? 51.849 81.037 110.241 1.00 15.97 ? 113 ILE B O 1 ATOM 2958 C CB . ILE B 1 31 ? 48.678 81.800 109.634 1.00 8.57 ? 113 ILE B CB 1 ATOM 2959 C CG1 . ILE B 1 31 ? 47.985 83.026 109.026 1.00 8.57 ? 113 ILE B CG1 1 ATOM 2960 C CG2 . ILE B 1 31 ? 49.003 82.057 111.111 1.00 8.57 ? 113 ILE B CG2 1 ATOM 2961 C CD1 . ILE B 1 31 ? 46.782 83.532 109.786 1.00 8.57 ? 113 ILE B CD1 1 ATOM 2962 N N . PRO B 1 32 ? 50.767 79.237 109.425 1.00 21.74 ? 114 PRO B N 1 ATOM 2963 C CA . PRO B 1 32 ? 51.679 78.322 110.125 1.00 21.74 ? 114 PRO B CA 1 ATOM 2964 C C . PRO B 1 32 ? 53.154 78.508 109.750 1.00 21.74 ? 114 PRO B C 1 ATOM 2965 O O . PRO B 1 32 ? 54.043 78.009 110.442 1.00 21.74 ? 114 PRO B O 1 ATOM 2966 C CB . PRO B 1 32 ? 51.172 76.946 109.701 1.00 19.04 ? 114 PRO B CB 1 ATOM 2967 C CG . PRO B 1 32 ? 49.710 77.173 109.492 1.00 19.04 ? 114 PRO B CG 1 ATOM 2968 C CD . PRO B 1 32 ? 49.690 78.484 108.758 1.00 19.04 ? 114 PRO B CD 1 ATOM 2969 N N . SER B 1 33 ? 53.401 79.237 108.661 1.00 20.81 ? 115 SER B N 1 ATOM 2970 C CA . SER B 1 33 ? 54.751 79.492 108.182 1.00 20.81 ? 115 SER B CA 1 ATOM 2971 C C . SER B 1 33 ? 55.219 80.918 108.411 1.00 20.81 ? 115 SER B C 1 ATOM 2972 O O . SER B 1 33 ? 56.344 81.261 108.057 1.00 20.81 ? 115 SER B O 1 ATOM 2973 C CB . SER B 1 33 ? 54.846 79.196 106.692 1.00 21.34 ? 115 SER B CB 1 ATOM 2974 O OG . SER B 1 33 ? 54.523 77.831 106.462 1.00 21.34 ? 115 SER B OG 1 ATOM 2975 N N . LEU B 1 34 ? 54.351 81.762 108.951 1.00 20.96 ? 116 LEU B N 1 ATOM 2976 C CA . LEU B 1 34 ? 54.721 83.149 109.198 1.00 20.96 ? 116 LEU B CA 1 ATOM 2977 C C . LEU B 1 34 ? 54.965 83.388 110.677 1.00 20.96 ? 116 LEU B C 1 ATOM 2978 O O . LEU B 1 34 ? 54.580 82.572 111.503 1.00 20.96 ? 116 LEU B O 1 ATOM 2979 C CB . LEU B 1 34 ? 53.642 84.086 108.665 1.00 14.81 ? 116 LEU B CB 1 ATOM 2980 C CG . LEU B 1 34 ? 53.429 84.007 107.152 1.00 14.81 ? 116 LEU B CG 1 ATOM 2981 C CD1 . LEU B 1 34 ? 52.290 84.923 106.752 1.00 14.81 ? 116 LEU B CD1 1 ATOM 2982 C CD2 . LEU B 1 34 ? 54.714 84.386 106.423 1.00 14.81 ? 116 LEU B CD2 1 ATOM 2983 N N . THR B 1 35 ? 55.598 84.509 111.010 1.00 30.06 ? 117 THR B N 1 ATOM 2984 C CA . THR B 1 35 ? 55.893 84.811 112.404 1.00 30.06 ? 117 THR B CA 1 ATOM 2985 C C . THR B 1 35 ? 55.599 86.263 112.780 1.00 30.06 ? 117 THR B C 1 ATOM 2986 O O . THR B 1 35 ? 55.610 87.151 111.924 1.00 30.06 ? 117 THR B O 1 ATOM 2987 C CB . THR B 1 35 ? 57.375 84.455 112.742 1.00 56.11 ? 117 THR B CB 1 ATOM 2988 O OG1 . THR B 1 35 ? 57.493 84.155 114.137 1.00 56.11 ? 117 THR B OG1 1 ATOM 2989 C CG2 . THR B 1 35 ? 58.318 85.610 112.403 1.00 56.11 ? 117 THR B CG2 1 ATOM 2990 N N . GLY B 1 36 ? 55.295 86.475 114.059 1.00 34.58 ? 118 GLY B N 1 ATOM 2991 C CA . GLY B 1 36 ? 55.015 87.806 114.576 1.00 34.58 ? 118 GLY B CA 1 ATOM 2992 C C . GLY B 1 36 ? 54.135 88.710 113.731 1.00 34.58 ? 118 GLY B C 1 ATOM 2993 O O . GLY B 1 36 ? 53.048 88.321 113.304 1.00 34.58 ? 118 GLY B O 1 ATOM 2994 N N . ALA B 1 37 ? 54.636 89.914 113.466 1.00 18.26 ? 119 ALA B N 1 ATOM 2995 C CA . ALA B 1 37 ? 53.919 90.921 112.691 1.00 18.26 ? 119 ALA B CA 1 ATOM 2996 C C . ALA B 1 37 ? 53.373 90.411 111.366 1.00 18.26 ? 119 ALA B C 1 ATOM 2997 O O . ALA B 1 37 ? 52.271 90.779 110.969 1.00 18.26 ? 119 ALA B O 1 ATOM 2998 C CB . ALA B 1 37 ? 54.807 92.129 112.459 1.00 16.38 ? 119 ALA B CB 1 ATOM 2999 N N . MET B 1 38 ? 54.137 89.559 110.692 1.00 21.92 ? 120 MET B N 1 ATOM 3000 C CA . MET B 1 38 ? 53.714 89.014 109.409 1.00 21.92 ? 120 MET B CA 1 ATOM 3001 C C . MET B 1 38 ? 52.470 88.136 109.478 1.00 21.92 ? 120 MET B C 1 ATOM 3002 O O . MET B 1 38 ? 51.560 88.289 108.664 1.00 21.92 ? 120 MET B O 1 ATOM 3003 C CB . MET B 1 38 ? 54.858 88.247 108.745 1.00 30.83 ? 120 MET B CB 1 ATOM 3004 C CG . MET B 1 38 ? 55.893 89.145 108.098 1.00 30.83 ? 120 MET B CG 1 ATOM 3005 S SD . MET B 1 38 ? 55.234 90.037 106.674 1.00 30.83 ? 120 MET B SD 1 ATOM 3006 C CE . MET B 1 38 ? 55.527 88.864 105.388 1.00 30.83 ? 120 MET B CE 1 ATOM 3007 N N . ALA B 1 39 ? 52.408 87.218 110.436 1.00 17.63 ? 121 ALA B N 1 ATOM 3008 C CA . ALA B 1 39 ? 51.228 86.373 110.497 1.00 17.63 ? 121 ALA B CA 1 ATOM 3009 C C . ALA B 1 39 ? 50.000 87.065 111.073 1.00 17.63 ? 121 ALA B C 1 ATOM 3010 O O . ALA B 1 39 ? 48.878 86.634 110.818 1.00 17.63 ? 121 ALA B O 1 ATOM 3011 C CB . ALA B 1 39 ? 51.511 85.096 111.185 1.00 37.09 ? 121 ALA B CB 1 ATOM 3012 N N . THR B 1 40 ? 50.203 88.133 111.843 1.00 18.64 ? 122 THR B N 1 ATOM 3013 C CA . THR B 1 40 ? 49.066 88.883 112.366 1.00 18.64 ? 122 THR B CA 1 ATOM 3014 C C . THR B 1 40 ? 48.483 89.652 111.183 1.00 18.64 ? 122 THR B C 1 ATOM 3015 O O . THR B 1 40 ? 47.264 89.758 111.033 1.00 18.64 ? 122 THR B O 1 ATOM 3016 C CB . THR B 1 40 ? 49.469 89.847 113.505 1.00 24.96 ? 122 THR B CB 1 ATOM 3017 O OG1 . THR B 1 40 ? 49.543 89.090 114.710 1.00 24.96 ? 122 THR B OG1 1 ATOM 3018 C CG2 . THR B 1 40 ? 48.430 90.955 113.686 1.00 24.96 ? 122 THR B CG2 1 ATOM 3019 N N . ALA B 1 41 ? 49.365 90.132 110.309 1.00 17.17 ? 123 ALA B N 1 ATOM 3020 C CA . ALA B 1 41 ? 48.940 90.860 109.123 1.00 17.17 ? 123 ALA B CA 1 ATOM 3021 C C . ALA B 1 41 ? 48.223 89.901 108.169 1.00 17.17 ? 123 ALA B C 1 ATOM 3022 O O . ALA B 1 41 ? 47.237 90.275 107.535 1.00 17.17 ? 123 ALA B O 1 ATOM 3023 C CB . ALA B 1 41 ? 50.137 91.493 108.433 1.00 17.51 ? 123 ALA B CB 1 ATOM 3024 N N . ALA B 1 42 ? 48.707 88.660 108.092 1.00 11.83 ? 124 ALA B N 1 ATOM 3025 C CA . ALA B 1 42 ? 48.100 87.648 107.223 1.00 11.83 ? 124 ALA B CA 1 ATOM 3026 C C . ALA B 1 42 ? 46.679 87.308 107.676 1.00 11.83 ? 124 ALA B C 1 ATOM 3027 O O . ALA B 1 42 ? 45.801 87.059 106.853 1.00 11.83 ? 124 ALA B O 1 ATOM 3028 C CB . ALA B 1 42 ? 48.954 86.392 107.190 1.00 8.45 ? 124 ALA B CB 1 ATOM 3029 N N . ALA B 1 43 ? 46.459 87.292 108.989 1.00 13.59 ? 125 ALA B N 1 ATOM 3030 C CA . ALA B 1 43 ? 45.140 86.999 109.544 1.00 13.59 ? 125 ALA B CA 1 ATOM 3031 C C . ALA B 1 43 ? 44.131 88.048 109.088 1.00 13.59 ? 125 ALA B C 1 ATOM 3032 O O . ALA B 1 43 ? 42.972 87.732 108.838 1.00 13.59 ? 125 ALA B O 1 ATOM 3033 C CB . ALA B 1 43 ? 45.202 86.957 111.079 1.00 2.00 ? 125 ALA B CB 1 ATOM 3034 N N . ALA B 1 44 ? 44.592 89.292 108.971 1.00 9.60 ? 126 ALA B N 1 ATOM 3035 C CA . ALA B 1 44 ? 43.748 90.401 108.549 1.00 9.60 ? 126 ALA B CA 1 ATOM 3036 C C . ALA B 1 44 ? 43.342 90.288 107.075 1.00 9.60 ? 126 ALA B C 1 ATOM 3037 O O . ALA B 1 44 ? 42.208 90.615 106.712 1.00 9.60 ? 126 ALA B O 1 ATOM 3038 C CB . ALA B 1 44 ? 44.460 91.725 108.802 1.00 9.74 ? 126 ALA B CB 1 ATOM 3039 N N . VAL B 1 45 ? 44.263 89.818 106.237 1.00 12.95 ? 127 VAL B N 1 ATOM 3040 C CA . VAL B 1 45 ? 44.003 89.665 104.806 1.00 12.95 ? 127 VAL B CA 1 ATOM 3041 C C . VAL B 1 45 ? 42.835 88.714 104.543 1.00 12.95 ? 127 VAL B C 1 ATOM 3042 O O . VAL B 1 45 ? 42.035 88.932 103.626 1.00 12.95 ? 127 VAL B O 1 ATOM 3043 C CB . VAL B 1 45 ? 45.248 89.130 104.048 1.00 10.95 ? 127 VAL B CB 1 ATOM 3044 C CG1 . VAL B 1 45 ? 44.937 88.996 102.562 1.00 10.95 ? 127 VAL B CG1 1 ATOM 3045 C CG2 . VAL B 1 45 ? 46.433 90.058 104.250 1.00 10.95 ? 127 VAL B CG2 1 ATOM 3046 N N . ALA B 1 46 ? 42.736 87.668 105.363 1.00 11.12 ? 128 ALA B N 1 ATOM 3047 C CA . ALA B 1 46 ? 41.673 86.679 105.215 1.00 11.12 ? 128 ALA B CA 1 ATOM 3048 C C . ALA B 1 46 ? 40.280 87.261 105.461 1.00 11.12 ? 128 ALA B C 1 ATOM 3049 O O . ALA B 1 46 ? 39.284 86.631 105.128 1.00 11.12 ? 128 ALA B O 1 ATOM 3050 C CB . ALA B 1 46 ? 41.917 85.495 106.148 1.00 9.91 ? 128 ALA B CB 1 ATOM 3051 N N . LYS B 1 47 ? 40.217 88.453 106.047 1.00 9.36 ? 129 LYS B N 1 ATOM 3052 C CA . LYS B 1 47 ? 38.937 89.098 106.334 1.00 9.36 ? 129 LYS B CA 1 ATOM 3053 C C . LYS B 1 47 ? 38.498 90.066 105.237 1.00 9.36 ? 129 LYS B C 1 ATOM 3054 O O . LYS B 1 47 ? 37.419 90.661 105.311 1.00 9.36 ? 129 LYS B O 1 ATOM 3055 C CB . LYS B 1 47 ? 38.992 89.801 107.692 1.00 34.55 ? 129 LYS B CB 1 ATOM 3056 C CG . LYS B 1 47 ? 39.251 88.848 108.848 1.00 34.55 ? 129 LYS B CG 1 ATOM 3057 C CD . LYS B 1 47 ? 39.190 89.558 110.185 1.00 34.55 ? 129 LYS B CD 1 ATOM 3058 C CE . LYS B 1 47 ? 39.509 88.609 111.331 1.00 34.55 ? 129 LYS B CE 1 ATOM 3059 N NZ . LYS B 1 47 ? 40.937 88.163 111.332 1.00 34.55 ? 129 LYS B NZ 1 ATOM 3060 N N . VAL B 1 48 ? 39.347 90.235 104.228 1.00 5.91 ? 130 VAL B N 1 ATOM 3061 C CA . VAL B 1 48 ? 39.030 91.114 103.112 1.00 5.91 ? 130 VAL B CA 1 ATOM 3062 C C . VAL B 1 48 ? 38.241 90.260 102.120 1.00 5.91 ? 130 VAL B C 1 ATOM 3063 O O . VAL B 1 48 ? 38.689 89.179 101.728 1.00 5.91 ? 130 VAL B O 1 ATOM 3064 C CB . VAL B 1 48 ? 40.309 91.669 102.443 1.00 6.71 ? 130 VAL B CB 1 ATOM 3065 C CG1 . VAL B 1 48 ? 39.945 92.613 101.309 1.00 6.71 ? 130 VAL B CG1 1 ATOM 3066 C CG2 . VAL B 1 48 ? 41.170 92.394 103.469 1.00 6.71 ? 130 VAL B CG2 1 ATOM 3067 N N . PRO B 1 49 ? 37.030 90.705 101.752 1.00 8.63 ? 131 PRO B N 1 ATOM 3068 C CA . PRO B 1 49 ? 36.206 89.943 100.809 1.00 8.63 ? 131 PRO B CA 1 ATOM 3069 C C . PRO B 1 49 ? 36.769 89.899 99.388 1.00 8.63 ? 131 PRO B C 1 ATOM 3070 O O . PRO B 1 49 ? 37.237 90.907 98.853 1.00 8.63 ? 131 PRO B O 1 ATOM 3071 C CB . PRO B 1 49 ? 34.852 90.654 100.878 1.00 7.06 ? 131 PRO B CB 1 ATOM 3072 C CG . PRO B 1 49 ? 35.211 92.063 101.224 1.00 7.06 ? 131 PRO B CG 1 ATOM 3073 C CD . PRO B 1 49 ? 36.338 91.921 102.215 1.00 7.06 ? 131 PRO B CD 1 ATOM 3074 N N . SER B 1 50 ? 36.775 88.701 98.818 1.00 8.06 ? 132 SER B N 1 ATOM 3075 C CA . SER B 1 50 ? 37.256 88.475 97.459 1.00 8.06 ? 132 SER B CA 1 ATOM 3076 C C . SER B 1 50 ? 36.285 87.525 96.751 1.00 8.06 ? 132 SER B C 1 ATOM 3077 O O . SER B 1 50 ? 35.398 86.951 97.384 1.00 8.06 ? 132 SER B O 1 ATOM 3078 C CB . SER B 1 50 ? 38.680 87.900 97.472 1.00 6.64 ? 132 SER B CB 1 ATOM 3079 O OG . SER B 1 50 ? 38.776 86.716 98.245 1.00 6.64 ? 132 SER B OG 1 ATOM 3080 N N . PHE B 1 51 ? 36.418 87.399 95.436 1.00 5.54 ? 133 PHE B N 1 ATOM 3081 C CA . PHE B 1 51 ? 35.535 86.529 94.669 1.00 5.54 ? 133 PHE B CA 1 ATOM 3082 C C . PHE B 1 51 ? 35.958 85.066 94.695 1.00 5.54 ? 133 PHE B C 1 ATOM 3083 O O . PHE B 1 51 ? 37.147 84.762 94.770 1.00 5.54 ? 133 PHE B O 1 ATOM 3084 C CB . PHE B 1 51 ? 35.447 87.011 93.212 1.00 2.69 ? 133 PHE B CB 1 ATOM 3085 C CG . PHE B 1 51 ? 34.504 88.173 93.006 1.00 2.69 ? 133 PHE B CG 1 ATOM 3086 C CD1 . PHE B 1 51 ? 34.773 89.420 93.562 1.00 2.69 ? 133 PHE B CD1 1 ATOM 3087 C CD2 . PHE B 1 51 ? 33.337 88.007 92.273 1.00 2.69 ? 133 PHE B CD2 1 ATOM 3088 C CE1 . PHE B 1 51 ? 33.893 90.484 93.392 1.00 2.69 ? 133 PHE B CE1 1 ATOM 3089 C CE2 . PHE B 1 51 ? 32.447 89.064 92.095 1.00 2.69 ? 133 PHE B CE2 1 ATOM 3090 C CZ . PHE B 1 51 ? 32.725 90.306 92.658 1.00 2.69 ? 133 PHE B CZ 1 ATOM 3091 N N . MET B 1 52 ? 34.972 84.170 94.686 1.00 5.01 ? 134 MET B N 1 ATOM 3092 C CA . MET B 1 52 ? 35.228 82.733 94.657 1.00 5.01 ? 134 MET B CA 1 ATOM 3093 C C . MET B 1 52 ? 35.033 82.298 93.211 1.00 5.01 ? 134 MET B C 1 ATOM 3094 O O . MET B 1 52 ? 34.021 82.627 92.596 1.00 5.01 ? 134 MET B O 1 ATOM 3095 C CB . MET B 1 52 ? 34.255 81.969 95.560 1.00 17.95 ? 134 MET B CB 1 ATOM 3096 C CG . MET B 1 52 ? 34.401 80.450 95.441 1.00 17.95 ? 134 MET B CG 1 ATOM 3097 S SD . MET B 1 52 ? 33.253 79.484 96.445 1.00 17.95 ? 134 MET B SD 1 ATOM 3098 C CE . MET B 1 52 ? 34.136 79.453 97.993 1.00 17.95 ? 134 MET B CE 1 ATOM 3099 N N . TRP B 1 53 ? 35.992 81.553 92.673 1.00 7.28 ? 135 TRP B N 1 ATOM 3100 C CA . TRP B 1 53 ? 35.924 81.102 91.286 1.00 7.28 ? 135 TRP B CA 1 ATOM 3101 C C . TRP B 1 53 ? 35.325 79.714 91.081 1.00 7.28 ? 135 TRP B C 1 ATOM 3102 O O . TRP B 1 53 ? 35.780 78.737 91.669 1.00 7.28 ? 135 TRP B O 1 ATOM 3103 C CB . TRP B 1 53 ? 37.317 81.158 90.637 1.00 5.57 ? 135 TRP B CB 1 ATOM 3104 C CG . TRP B 1 53 ? 37.906 82.540 90.557 1.00 5.57 ? 135 TRP B CG 1 ATOM 3105 C CD1 . TRP B 1 53 ? 38.085 83.416 91.588 1.00 5.57 ? 135 TRP B CD1 1 ATOM 3106 C CD2 . TRP B 1 53 ? 38.395 83.197 89.382 1.00 5.57 ? 135 TRP B CD2 1 ATOM 3107 N NE1 . TRP B 1 53 ? 38.650 84.576 91.129 1.00 5.57 ? 135 TRP B NE1 1 ATOM 3108 C CE2 . TRP B 1 53 ? 38.854 84.473 89.776 1.00 5.57 ? 135 TRP B CE2 1 ATOM 3109 C CE3 . TRP B 1 53 ? 38.489 82.837 88.029 1.00 5.57 ? 135 TRP B CE3 1 ATOM 3110 C CZ2 . TRP B 1 53 ? 39.397 85.391 88.876 1.00 5.57 ? 135 TRP B CZ2 1 ATOM 3111 C CZ3 . TRP B 1 53 ? 39.032 83.755 87.126 1.00 5.57 ? 135 TRP B CZ3 1 ATOM 3112 C CH2 . TRP B 1 53 ? 39.479 85.017 87.558 1.00 5.57 ? 135 TRP B CH2 1 ATOM 3113 N N . LEU B 1 54 ? 34.309 79.638 90.227 1.00 4.92 ? 136 LEU B N 1 ATOM 3114 C CA . LEU B 1 54 ? 33.656 78.372 89.901 1.00 4.92 ? 136 LEU B CA 1 ATOM 3115 C C . LEU B 1 54 ? 34.264 77.951 88.565 1.00 4.92 ? 136 LEU B C 1 ATOM 3116 O O . LEU B 1 54 ? 33.642 78.076 87.517 1.00 4.92 ? 136 LEU B O 1 ATOM 3117 C CB . LEU B 1 54 ? 32.144 78.581 89.760 1.00 9.81 ? 136 LEU B CB 1 ATOM 3118 C CG . LEU B 1 54 ? 31.502 79.382 90.900 1.00 9.81 ? 136 LEU B CG 1 ATOM 3119 C CD1 . LEU B 1 54 ? 30.016 79.541 90.664 1.00 9.81 ? 136 LEU B CD1 1 ATOM 3120 C CD2 . LEU B 1 54 ? 31.761 78.695 92.227 1.00 9.81 ? 136 LEU B CD2 1 ATOM 3121 N N . ASP B 1 55 ? 35.506 77.485 88.612 1.00 8.38 ? 137 ASP B N 1 ATOM 3122 C CA . ASP B 1 55 ? 36.231 77.092 87.409 1.00 8.38 ? 137 ASP B CA 1 ATOM 3123 C C . ASP B 1 55 ? 35.969 75.676 86.893 1.00 8.38 ? 137 ASP B C 1 ATOM 3124 O O . ASP B 1 55 ? 36.459 75.292 85.830 1.00 8.38 ? 137 ASP B O 1 ATOM 3125 C CB . ASP B 1 55 ? 37.736 77.342 87.592 1.00 19.79 ? 137 ASP B CB 1 ATOM 3126 C CG . ASP B 1 55 ? 38.331 76.559 88.753 1.00 19.79 ? 137 ASP B CG 1 ATOM 3127 O OD1 . ASP B 1 55 ? 37.868 76.715 89.903 1.00 19.79 ? 137 ASP B OD1 1 ATOM 3128 O OD2 . ASP B 1 55 ? 39.276 75.787 88.511 1.00 19.79 ? 137 ASP B OD2 1 ATOM 3129 N N . THR B 1 56 ? 35.207 74.896 87.650 1.00 7.47 ? 138 THR B N 1 ATOM 3130 C CA . THR B 1 56 ? 34.846 73.533 87.254 1.00 7.47 ? 138 THR B CA 1 ATOM 3131 C C . THR B 1 56 ? 33.441 73.263 87.771 1.00 7.47 ? 138 THR B C 1 ATOM 3132 O O . THR B 1 56 ? 32.967 73.959 88.671 1.00 7.47 ? 138 THR B O 1 ATOM 3133 C CB . THR B 1 56 ? 35.770 72.468 87.881 1.00 9.16 ? 138 THR B CB 1 ATOM 3134 O OG1 . THR B 1 56 ? 35.786 72.635 89.304 1.00 9.16 ? 138 THR B OG1 1 ATOM 3135 C CG2 . THR B 1 56 ? 37.184 72.568 87.338 1.00 9.16 ? 138 THR B CG2 1 ATOM 3136 N N . LEU B 1 57 ? 32.794 72.236 87.228 1.00 8.32 ? 139 LEU B N 1 ATOM 3137 C CA . LEU B 1 57 ? 31.455 71.887 87.668 1.00 8.32 ? 139 LEU B CA 1 ATOM 3138 C C . LEU B 1 57 ? 31.497 71.421 89.122 1.00 8.32 ? 139 LEU B C 1 ATOM 3139 O O . LEU B 1 57 ? 30.608 71.756 89.904 1.00 8.32 ? 139 LEU B O 1 ATOM 3140 C CB . LEU B 1 57 ? 30.845 70.799 86.785 1.00 8.39 ? 139 LEU B CB 1 ATOM 3141 C CG . LEU B 1 57 ? 29.409 70.389 87.150 1.00 8.39 ? 139 LEU B CG 1 ATOM 3142 C CD1 . LEU B 1 57 ? 28.468 71.585 87.039 1.00 8.39 ? 139 LEU B CD1 1 ATOM 3143 C CD2 . LEU B 1 57 ? 28.949 69.274 86.237 1.00 8.39 ? 139 LEU B CD2 1 ATOM 3144 N N . ASP B 1 58 ? 32.555 70.699 89.493 1.00 9.25 ? 140 ASP B N 1 ATOM 3145 C CA . ASP B 1 58 ? 32.672 70.217 90.867 1.00 9.25 ? 140 ASP B CA 1 ATOM 3146 C C . ASP B 1 58 ? 32.891 71.316 91.905 1.00 9.25 ? 140 ASP B C 1 ATOM 3147 O O . ASP B 1 58 ? 33.008 71.033 93.097 1.00 9.25 ? 140 ASP B O 1 ATOM 3148 C CB . ASP B 1 58 ? 33.724 69.108 90.999 1.00 76.25 ? 140 ASP B CB 1 ATOM 3149 C CG . ASP B 1 58 ? 35.034 69.457 90.334 1.00 76.25 ? 140 ASP B CG 1 ATOM 3150 O OD1 . ASP B 1 58 ? 35.719 70.382 90.806 1.00 76.25 ? 140 ASP B OD1 1 ATOM 3151 O OD2 . ASP B 1 58 ? 35.392 68.780 89.347 1.00 76.25 ? 140 ASP B OD2 1 ATOM 3152 N N . LYS B 1 59 ? 32.944 72.564 91.448 1.00 8.17 ? 141 LYS B N 1 ATOM 3153 C CA . LYS B 1 59 ? 33.091 73.707 92.342 1.00 8.17 ? 141 LYS B CA 1 ATOM 3154 C C . LYS B 1 59 ? 31.704 74.202 92.764 1.00 8.17 ? 141 LYS B C 1 ATOM 3155 O O . LYS B 1 59 ? 31.578 74.910 93.761 1.00 8.17 ? 141 LYS B O 1 ATOM 3156 C CB . LYS B 1 59 ? 33.848 74.845 91.654 1.00 32.21 ? 141 LYS B CB 1 ATOM 3157 C CG . LYS B 1 59 ? 35.360 74.770 91.781 1.00 32.21 ? 141 LYS B CG 1 ATOM 3158 C CD . LYS B 1 59 ? 35.802 74.957 93.221 1.00 32.21 ? 141 LYS B CD 1 ATOM 3159 C CE . LYS B 1 59 ? 37.318 75.126 93.332 1.00 32.21 ? 141 LYS B CE 1 ATOM 3160 N NZ . LYS B 1 59 ? 37.802 76.467 92.869 1.00 32.21 ? 141 LYS B NZ 1 ATOM 3161 N N . THR B 1 60 ? 30.664 73.813 92.025 1.00 7.63 ? 142 THR B N 1 ATOM 3162 C CA . THR B 1 60 ? 29.301 74.250 92.350 1.00 7.63 ? 142 THR B CA 1 ATOM 3163 C C . THR B 1 60 ? 28.819 73.909 93.767 1.00 7.63 ? 142 THR B C 1 ATOM 3164 O O . THR B 1 60 ? 28.119 74.712 94.383 1.00 7.63 ? 142 THR B O 1 ATOM 3165 C CB . THR B 1 60 ? 28.254 73.839 91.266 1.00 8.20 ? 142 THR B CB 1 ATOM 3166 O OG1 . THR B 1 60 ? 28.332 72.434 91.005 1.00 8.20 ? 142 THR B OG1 1 ATOM 3167 C CG2 . THR B 1 60 ? 28.502 74.613 89.971 1.00 8.20 ? 142 THR B CG2 1 ATOM 3168 N N . PRO B 1 61 ? 29.159 72.713 94.296 1.00 11.58 ? 143 PRO B N 1 ATOM 3169 C CA . PRO B 1 61 ? 28.716 72.387 95.660 1.00 11.58 ? 143 PRO B CA 1 ATOM 3170 C C . PRO B 1 61 ? 29.311 73.394 96.652 1.00 11.58 ? 143 PRO B C 1 ATOM 3171 O O . PRO B 1 61 ? 28.725 73.682 97.693 1.00 11.58 ? 143 PRO B O 1 ATOM 3172 C CB . PRO B 1 61 ? 29.319 71.003 95.896 1.00 12.30 ? 143 PRO B CB 1 ATOM 3173 C CG . PRO B 1 61 ? 29.356 70.399 94.541 1.00 12.30 ? 143 PRO B CG 1 ATOM 3174 C CD . PRO B 1 61 ? 29.785 71.540 93.654 1.00 12.30 ? 143 PRO B CD 1 ATOM 3175 N N . LEU B 1 62 ? 30.488 73.915 96.311 1.00 10.53 ? 144 LEU B N 1 ATOM 3176 C CA . LEU B 1 62 ? 31.189 74.891 97.140 1.00 10.53 ? 144 LEU B CA 1 ATOM 3177 C C . LEU B 1 62 ? 30.452 76.229 97.128 1.00 10.53 ? 144 LEU B C 1 ATOM 3178 O O . LEU B 1 62 ? 30.499 76.983 98.100 1.00 10.53 ? 144 LEU B O 1 ATOM 3179 C CB . LEU B 1 62 ? 32.622 75.063 96.636 1.00 26.30 ? 144 LEU B CB 1 ATOM 3180 C CG . LEU B 1 62 ? 33.664 75.612 97.605 1.00 26.30 ? 144 LEU B CG 1 ATOM 3181 C CD1 . LEU B 1 62 ? 33.723 74.734 98.841 1.00 26.30 ? 144 LEU B CD1 1 ATOM 3182 C CD2 . LEU B 1 62 ? 35.017 75.651 96.916 1.00 26.30 ? 144 LEU B CD2 1 ATOM 3183 N N . MET B 1 63 ? 29.797 76.532 96.009 1.00 7.23 ? 145 MET B N 1 ATOM 3184 C CA . MET B 1 63 ? 29.019 77.764 95.892 1.00 7.23 ? 145 MET B CA 1 ATOM 3185 C C . MET B 1 63 ? 27.799 77.674 96.810 1.00 7.23 ? 145 MET B C 1 ATOM 3186 O O . MET B 1 63 ? 27.444 78.638 97.489 1.00 7.23 ? 145 MET B O 1 ATOM 3187 C CB . MET B 1 63 ? 28.544 77.961 94.455 1.00 7.83 ? 145 MET B CB 1 ATOM 3188 C CG . MET B 1 63 ? 27.640 79.163 94.286 1.00 7.83 ? 145 MET B CG 1 ATOM 3189 S SD . MET B 1 63 ? 26.889 79.245 92.671 1.00 7.83 ? 145 MET B SD 1 ATOM 3190 C CE . MET B 1 63 ? 26.193 80.881 92.737 1.00 7.83 ? 145 MET B CE 1 ATOM 3191 N N . GLU B 1 64 ? 27.156 76.509 96.813 1.00 7.29 ? 146 GLU B N 1 ATOM 3192 C CA . GLU B 1 64 ? 25.979 76.270 97.641 1.00 7.29 ? 146 GLU B CA 1 ATOM 3193 C C . GLU B 1 64 ? 26.360 76.308 99.125 1.00 7.29 ? 146 GLU B C 1 ATOM 3194 O O . GLU B 1 64 ? 25.622 76.827 99.964 1.00 7.29 ? 146 GLU B O 1 ATOM 3195 C CB . GLU B 1 64 ? 25.368 74.916 97.280 1.00 27.88 ? 146 GLU B CB 1 ATOM 3196 C CG . GLU B 1 64 ? 24.029 74.645 97.934 1.00 27.88 ? 146 GLU B CG 1 ATOM 3197 C CD . GLU B 1 64 ? 23.346 73.397 97.398 1.00 27.88 ? 146 GLU B CD 1 ATOM 3198 O OE1 . GLU B 1 64 ? 23.959 72.659 96.593 1.00 27.88 ? 146 GLU B OE1 1 ATOM 3199 O OE2 . GLU B 1 64 ? 22.184 73.155 97.786 1.00 27.88 ? 146 GLU B OE2 1 ATOM 3200 N N . GLN B 1 65 ? 27.537 75.777 99.429 1.00 12.87 ? 147 GLN B N 1 ATOM 3201 C CA . GLN B 1 65 ? 28.063 75.734 100.788 1.00 12.87 ? 147 GLN B CA 1 ATOM 3202 C C . GLN B 1 65 ? 28.317 77.160 101.296 1.00 12.87 ? 147 GLN B C 1 ATOM 3203 O O . GLN B 1 65 ? 28.013 77.488 102.446 1.00 12.87 ? 147 GLN B O 1 ATOM 3204 C CB . GLN B 1 65 ? 29.363 74.930 100.779 1.00 83.05 ? 147 GLN B CB 1 ATOM 3205 C CG . GLN B 1 65 ? 29.962 74.612 102.131 1.00 83.05 ? 147 GLN B CG 1 ATOM 3206 C CD . GLN B 1 65 ? 31.262 73.839 101.998 1.00 83.05 ? 147 GLN B CD 1 ATOM 3207 O OE1 . GLN B 1 65 ? 32.297 74.242 102.533 1.00 83.05 ? 147 GLN B OE1 1 ATOM 3208 N NE2 . GLN B 1 65 ? 31.221 72.734 101.255 1.00 83.05 ? 147 GLN B NE2 1 ATOM 3209 N N . THR B 1 66 ? 28.857 78.006 100.420 1.00 11.02 ? 148 THR B N 1 ATOM 3210 C CA . THR B 1 66 ? 29.160 79.399 100.745 1.00 11.02 ? 148 THR B CA 1 ATOM 3211 C C . THR B 1 66 ? 27.881 80.185 101.005 1.00 11.02 ? 148 THR B C 1 ATOM 3212 O O . THR B 1 66 ? 27.804 80.962 101.959 1.00 11.02 ? 148 THR B O 1 ATOM 3213 C CB . THR B 1 66 ? 29.958 80.071 99.599 1.00 7.48 ? 148 THR B CB 1 ATOM 3214 O OG1 . THR B 1 66 ? 31.181 79.357 99.392 1.00 7.48 ? 148 THR B OG1 1 ATOM 3215 C CG2 . THR B 1 66 ? 30.278 81.523 99.931 1.00 7.48 ? 148 THR B CG2 1 ATOM 3216 N N . LEU B 1 67 ? 26.880 79.977 100.153 1.00 7.90 ? 149 LEU B N 1 ATOM 3217 C CA . LEU B 1 67 ? 25.599 80.658 100.293 1.00 7.90 ? 149 LEU B CA 1 ATOM 3218 C C . LEU B 1 67 ? 24.885 80.214 101.566 1.00 7.90 ? 149 LEU B C 1 ATOM 3219 O O . LEU B 1 67 ? 24.190 81.004 102.191 1.00 7.90 ? 149 LEU B O 1 ATOM 3220 C CB . LEU B 1 67 ? 24.730 80.421 99.054 1.00 4.48 ? 149 LEU B CB 1 ATOM 3221 C CG . LEU B 1 67 ? 25.234 81.138 97.794 1.00 4.48 ? 149 LEU B CG 1 ATOM 3222 C CD1 . LEU B 1 67 ? 24.532 80.615 96.554 1.00 4.48 ? 149 LEU B CD1 1 ATOM 3223 C CD2 . LEU B 1 67 ? 25.029 82.638 97.941 1.00 4.48 ? 149 LEU B CD2 1 ATOM 3224 N N . ALA B 1 68 ? 25.082 78.961 101.966 1.00 12.57 ? 150 ALA B N 1 ATOM 3225 C CA . ALA B 1 68 ? 24.478 78.453 103.195 1.00 12.57 ? 150 ALA B CA 1 ATOM 3226 C C . ALA B 1 68 ? 25.075 79.217 104.381 1.00 12.57 ? 150 ALA B C 1 ATOM 3227 O O . ALA B 1 68 ? 24.345 79.654 105.272 1.00 12.57 ? 150 ALA B O 1 ATOM 3228 C CB . ALA B 1 68 ? 24.741 76.962 103.339 1.00 4.34 ? 150 ALA B CB 1 ATOM 3229 N N . ASP B 1 69 ? 26.398 79.395 104.366 1.00 11.93 ? 151 ASP B N 1 ATOM 3230 C CA . ASP B 1 69 ? 27.106 80.131 105.418 1.00 11.93 ? 151 ASP B CA 1 ATOM 3231 C C . ASP B 1 69 ? 26.581 81.557 105.508 1.00 11.93 ? 151 ASP B C 1 ATOM 3232 O O . ASP B 1 69 ? 26.423 82.104 106.599 1.00 11.93 ? 151 ASP B O 1 ATOM 3233 C CB . ASP B 1 69 ? 28.609 80.199 105.130 1.00 22.41 ? 151 ASP B CB 1 ATOM 3234 C CG . ASP B 1 69 ? 29.318 78.874 105.329 1.00 22.41 ? 151 ASP B CG 1 ATOM 3235 O OD1 . ASP B 1 69 ? 28.697 77.909 105.824 1.00 22.41 ? 151 ASP B OD1 1 ATOM 3236 O OD2 . ASP B 1 69 ? 30.519 78.808 104.992 1.00 22.41 ? 151 ASP B OD2 1 ATOM 3237 N N . ILE B 1 70 ? 26.352 82.167 104.347 1.00 9.41 ? 152 ILE B N 1 ATOM 3238 C CA . ILE B 1 70 ? 25.849 83.533 104.277 1.00 9.41 ? 152 ILE B CA 1 ATOM 3239 C C . ILE B 1 70 ? 24.425 83.624 104.808 1.00 9.41 ? 152 ILE B C 1 ATOM 3240 O O . ILE B 1 70 ? 24.092 84.566 105.524 1.00 9.41 ? 152 ILE B O 1 ATOM 3241 C CB . ILE B 1 70 ? 25.895 84.074 102.833 1.00 7.61 ? 152 ILE B CB 1 ATOM 3242 C CG1 . ILE B 1 70 ? 27.343 84.119 102.347 1.00 7.61 ? 152 ILE B CG1 1 ATOM 3243 C CG2 . ILE B 1 70 ? 25.284 85.470 102.767 1.00 7.61 ? 152 ILE B CG2 1 ATOM 3244 C CD1 . ILE B 1 70 ? 27.487 84.454 100.875 1.00 7.61 ? 152 ILE B CD1 1 ATOM 3245 N N . ARG B 1 71 ? 23.588 82.649 104.462 1.00 12.30 ? 153 ARG B N 1 ATOM 3246 C CA . ARG B 1 71 ? 22.205 82.648 104.934 1.00 12.30 ? 153 ARG B CA 1 ATOM 3247 C C . ARG B 1 71 ? 22.205 82.621 106.454 1.00 12.30 ? 153 ARG B C 1 ATOM 3248 O O . ARG B 1 71 ? 21.468 83.367 107.092 1.00 12.30 ? 153 ARG B O 1 ATOM 3249 C CB . ARG B 1 71 ? 21.424 81.446 104.391 1.00 20.26 ? 153 ARG B CB 1 ATOM 3250 C CG . ARG B 1 71 ? 20.008 81.359 104.947 1.00 20.26 ? 153 ARG B CG 1 ATOM 3251 C CD . ARG B 1 71 ? 18.971 81.087 103.875 1.00 20.26 ? 153 ARG B CD 1 ATOM 3252 N NE . ARG B 1 71 ? 18.901 79.688 103.482 1.00 20.26 ? 153 ARG B NE 1 ATOM 3253 C CZ . ARG B 1 71 ? 18.346 79.251 102.356 1.00 20.26 ? 153 ARG B CZ 1 ATOM 3254 N NH1 . ARG B 1 71 ? 17.814 80.100 101.487 1.00 20.26 ? 153 ARG B NH1 1 ATOM 3255 N NH2 . ARG B 1 71 ? 18.294 77.949 102.115 1.00 20.26 ? 153 ARG B NH2 1 ATOM 3256 N N . THR B 1 72 ? 23.064 81.790 107.032 1.00 13.15 ? 154 THR B N 1 ATOM 3257 C CA . THR B 1 72 ? 23.151 81.693 108.480 1.00 13.15 ? 154 THR B CA 1 ATOM 3258 C C . THR B 1 72 ? 23.662 82.985 109.080 1.00 13.15 ? 154 THR B C 1 ATOM 3259 O O . THR B 1 72 ? 23.139 83.449 110.085 1.00 13.15 ? 154 THR B O 1 ATOM 3260 C CB . THR B 1 72 ? 24.083 80.586 108.914 1.00 14.87 ? 154 THR B CB 1 ATOM 3261 O OG1 . THR B 1 72 ? 23.544 79.324 108.501 1.00 14.87 ? 154 THR B OG1 1 ATOM 3262 C CG2 . THR B 1 72 ? 24.254 80.618 110.427 1.00 14.87 ? 154 THR B CG2 1 ATOM 3263 N N . ALA B 1 73 ? 24.703 83.544 108.469 1.00 12.79 ? 155 ALA B N 1 ATOM 3264 C CA . ALA B 1 73 ? 25.293 84.795 108.927 1.00 12.79 ? 155 ALA B CA 1 ATOM 3265 C C . ALA B 1 73 ? 24.234 85.889 108.937 1.00 12.79 ? 155 ALA B C 1 ATOM 3266 O O . ALA B 1 73 ? 24.143 86.654 109.886 1.00 12.79 ? 155 ALA B O 1 ATOM 3267 C CB . ALA B 1 73 ? 26.454 85.193 108.026 1.00 10.57 ? 155 ALA B CB 1 ATOM 3268 N N . ASN B 1 74 ? 23.407 85.919 107.895 1.00 15.37 ? 156 ASN B N 1 ATOM 3269 C CA . ASN B 1 74 ? 22.337 86.899 107.769 1.00 15.37 ? 156 ASN B CA 1 ATOM 3270 C C . ASN B 1 74 ? 21.189 86.558 108.709 1.00 15.37 ? 156 ASN B C 1 ATOM 3271 O O . ASN B 1 74 ? 20.484 87.446 109.186 1.00 15.37 ? 156 ASN B O 1 ATOM 3272 C CB . ASN B 1 74 ? 21.829 86.954 106.330 1.00 13.29 ? 156 ASN B CB 1 ATOM 3273 C CG . ASN B 1 74 ? 22.833 87.571 105.380 1.00 13.29 ? 156 ASN B CG 1 ATOM 3274 O OD1 . ASN B 1 74 ? 23.927 87.971 105.788 1.00 13.29 ? 156 ASN B OD1 1 ATOM 3275 N ND2 . ASN B 1 74 ? 22.468 87.654 104.103 1.00 13.29 ? 156 ASN B ND2 1 ATOM 3276 N N . LYS B 1 75 ? 20.975 85.260 108.922 1.00 38.41 ? 157 LYS B N 1 ATOM 3277 C CA . LYS B 1 75 ? 19.937 84.772 109.829 1.00 38.41 ? 157 LYS B CA 1 ATOM 3278 C C . LYS B 1 75 ? 20.478 85.096 111.210 1.00 38.41 ? 157 LYS B C 1 ATOM 3279 O O . LYS B 1 75 ? 19.740 85.149 112.181 1.00 38.41 ? 157 LYS B O 1 ATOM 3280 C CB . LYS B 1 75 ? 19.747 83.261 109.662 1.00 69.82 ? 157 LYS B CB 1 ATOM 3281 C CG . LYS B 1 75 ? 18.567 82.647 110.423 1.00 69.82 ? 157 LYS B CG 1 ATOM 3282 C CD . LYS B 1 75 ? 18.911 82.317 111.872 1.00 69.82 ? 157 LYS B CD 1 ATOM 3283 C CE . LYS B 1 75 ? 17.727 81.706 112.607 1.00 69.82 ? 157 LYS B CE 1 ATOM 3284 N NZ . LYS B 1 75 ? 18.035 81.436 114.041 1.00 69.82 ? 157 LYS B NZ 1 ATOM 3285 N N . ASN B 1 76 ? 21.789 85.300 111.271 1.00 61.63 ? 158 ASN B N 1 ATOM 3286 C CA . ASN B 1 76 ? 22.474 85.637 112.496 1.00 61.63 ? 158 ASN B CA 1 ATOM 3287 C C . ASN B 1 76 ? 22.883 87.100 112.486 1.00 61.63 ? 158 ASN B C 1 ATOM 3288 O O . ASN B 1 76 ? 23.992 87.467 112.894 1.00 61.63 ? 158 ASN B O 1 ATOM 3289 C CB . ASN B 1 76 ? 23.674 84.720 112.726 1.00 55.25 ? 158 ASN B CB 1 ATOM 3290 C CG . ASN B 1 76 ? 23.266 83.363 113.265 1.00 55.25 ? 158 ASN B CG 1 ATOM 3291 O OD1 . ASN B 1 76 ? 24.222 82.454 113.360 1.00 55.25 ? 158 ASN B OD1 1 ATOM 3292 N ND2 . ASN B 1 76 ? 22.104 83.138 113.607 1.00 55.25 ? 158 ASN B ND2 1 ATOM 3293 N N . GLY B 1 77 ? 21.981 87.923 111.961 1.00 44.94 ? 159 GLY B N 1 ATOM 3294 C CA . GLY B 1 77 ? 22.182 89.359 111.892 1.00 44.94 ? 159 GLY B CA 1 ATOM 3295 C C . GLY B 1 77 ? 23.038 90.002 110.821 1.00 44.94 ? 159 GLY B C 1 ATOM 3296 O O . GLY B 1 77 ? 23.138 91.218 110.770 1.00 44.94 ? 159 GLY B O 1 ATOM 3297 N N . GLY B 1 78 ? 23.646 89.198 109.964 1.00 26.25 ? 160 GLY B N 1 ATOM 3298 C CA . GLY B 1 78 ? 24.481 89.757 108.922 1.00 26.25 ? 160 GLY B CA 1 ATOM 3299 C C . GLY B 1 78 ? 23.661 90.350 107.797 1.00 26.25 ? 160 GLY B C 1 ATOM 3300 O O . GLY B 1 78 ? 22.436 90.213 107.759 1.00 26.25 ? 160 GLY B O 1 ATOM 3301 N N . ASN B 1 79 ? 24.349 91.020 106.883 1.00 19.55 ? 161 ASN B N 1 ATOM 3302 C CA . ASN B 1 79 ? 23.729 91.645 105.721 1.00 19.55 ? 161 ASN B CA 1 ATOM 3303 C C . ASN B 1 79 ? 24.780 91.475 104.624 1.00 19.55 ? 161 ASN B C 1 ATOM 3304 O O . ASN B 1 79 ? 25.264 92.442 104.031 1.00 19.55 ? 161 ASN B O 1 ATOM 3305 C CB . ASN B 1 79 ? 23.463 93.122 106.010 1.00 25.48 ? 161 ASN B CB 1 ATOM 3306 C CG . ASN B 1 79 ? 22.714 93.810 104.896 1.00 25.48 ? 161 ASN B CG 1 ATOM 3307 O OD1 . ASN B 1 79 ? 21.889 93.200 104.212 1.00 25.48 ? 161 ASN B OD1 1 ATOM 3308 N ND2 . ASN B 1 79 ? 23.003 95.091 104.698 1.00 25.48 ? 161 ASN B ND2 1 ATOM 3309 N N . TYR B 1 80 ? 25.140 90.215 104.394 1.00 11.12 ? 162 TYR B N 1 ATOM 3310 C CA . TYR B 1 80 ? 26.159 89.847 103.425 1.00 11.12 ? 162 TYR B CA 1 ATOM 3311 C C . TYR B 1 80 ? 25.637 89.411 102.072 1.00 11.12 ? 162 TYR B C 1 ATOM 3312 O O . TYR B 1 80 ? 24.523 88.897 101.954 1.00 11.12 ? 162 TYR B O 1 ATOM 3313 C CB . TYR B 1 80 ? 27.033 88.734 103.998 1.00 20.43 ? 162 TYR B CB 1 ATOM 3314 C CG . TYR B 1 80 ? 27.735 89.117 105.276 1.00 20.43 ? 162 TYR B CG 1 ATOM 3315 C CD1 . TYR B 1 80 ? 28.870 89.928 105.254 1.00 20.43 ? 162 TYR B CD1 1 ATOM 3316 C CD2 . TYR B 1 80 ? 27.264 88.675 106.508 1.00 20.43 ? 162 TYR B CD2 1 ATOM 3317 C CE1 . TYR B 1 80 ? 29.518 90.290 106.428 1.00 20.43 ? 162 TYR B CE1 1 ATOM 3318 C CE2 . TYR B 1 80 ? 27.906 89.031 107.693 1.00 20.43 ? 162 TYR B CE2 1 ATOM 3319 C CZ . TYR B 1 80 ? 29.032 89.838 107.646 1.00 20.43 ? 162 TYR B CZ 1 ATOM 3320 O OH . TYR B 1 80 ? 29.667 90.194 108.813 1.00 20.43 ? 162 TYR B OH 1 ATOM 3321 N N . ALA B 1 81 ? 26.491 89.579 101.064 1.00 11.72 ? 163 ALA B N 1 ATOM 3322 C CA . ALA B 1 81 ? 26.193 89.208 99.687 1.00 11.72 ? 163 ALA B CA 1 ATOM 3323 C C . ALA B 1 81 ? 27.284 88.266 99.182 1.00 11.72 ? 163 ALA B C 1 ATOM 3324 O O . ALA B 1 81 ? 28.437 88.350 99.613 1.00 11.72 ? 163 ALA B O 1 ATOM 3325 C CB . ALA B 1 81 ? 26.129 90.453 98.814 1.00 5.25 ? 163 ALA B CB 1 ATOM 3326 N N . GLY B 1 82 ? 26.916 87.350 98.293 1.00 7.62 ? 164 GLY B N 1 ATOM 3327 C CA . GLY B 1 82 ? 27.890 86.423 97.749 1.00 7.62 ? 164 GLY B CA 1 ATOM 3328 C C . GLY B 1 82 ? 28.573 87.005 96.527 1.00 7.62 ? 164 GLY B C 1 ATOM 3329 O O . GLY B 1 82 ? 27.998 87.848 95.832 1.00 7.62 ? 164 GLY B O 1 ATOM 3330 N N . GLN B 1 83 ? 29.805 86.570 96.273 1.00 3.43 ? 165 GLN B N 1 ATOM 3331 C CA . GLN B 1 83 ? 30.593 87.033 95.129 1.00 3.43 ? 165 GLN B CA 1 ATOM 3332 C C . GLN B 1 83 ? 31.244 85.822 94.456 1.00 3.43 ? 165 GLN B C 1 ATOM 3333 O O . GLN B 1 83 ? 32.098 85.160 95.052 1.00 3.43 ? 165 GLN B O 1 ATOM 3334 C CB . GLN B 1 83 ? 31.689 88.000 95.590 1.00 7.95 ? 165 GLN B CB 1 ATOM 3335 C CG . GLN B 1 83 ? 31.196 89.222 96.352 1.00 7.95 ? 165 GLN B CG 1 ATOM 3336 C CD . GLN B 1 83 ? 32.281 90.259 96.549 1.00 7.95 ? 165 GLN B CD 1 ATOM 3337 O OE1 . GLN B 1 83 ? 32.090 91.436 96.241 1.00 7.95 ? 165 GLN B OE1 1 ATOM 3338 N NE2 . GLN B 1 83 ? 33.431 89.831 97.058 1.00 7.95 ? 165 GLN B NE2 1 ATOM 3339 N N . PHE B 1 84 ? 30.855 85.546 93.215 1.00 2.00 ? 166 PHE B N 1 ATOM 3340 C CA . PHE B 1 84 ? 31.400 84.400 92.493 1.00 2.00 ? 166 PHE B CA 1 ATOM 3341 C C . PHE B 1 84 ? 31.816 84.747 91.062 1.00 2.00 ? 166 PHE B C 1 ATOM 3342 O O . PHE B 1 84 ? 31.358 85.742 90.492 1.00 2.00 ? 166 PHE B O 1 ATOM 3343 C CB . PHE B 1 84 ? 30.372 83.254 92.458 1.00 5.47 ? 166 PHE B CB 1 ATOM 3344 C CG . PHE B 1 84 ? 29.840 82.871 93.810 1.00 5.47 ? 166 PHE B CG 1 ATOM 3345 C CD1 . PHE B 1 84 ? 30.524 81.960 94.610 1.00 5.47 ? 166 PHE B CD1 1 ATOM 3346 C CD2 . PHE B 1 84 ? 28.669 83.445 94.302 1.00 5.47 ? 166 PHE B CD2 1 ATOM 3347 C CE1 . PHE B 1 84 ? 30.058 81.632 95.881 1.00 5.47 ? 166 PHE B CE1 1 ATOM 3348 C CE2 . PHE B 1 84 ? 28.191 83.121 95.579 1.00 5.47 ? 166 PHE B CE2 1 ATOM 3349 C CZ . PHE B 1 84 ? 28.892 82.212 96.366 1.00 5.47 ? 166 PHE B CZ 1 ATOM 3350 N N . VAL B 1 85 ? 32.688 83.918 90.491 1.00 4.07 ? 167 VAL B N 1 ATOM 3351 C CA . VAL B 1 85 ? 33.151 84.105 89.122 1.00 4.07 ? 167 VAL B CA 1 ATOM 3352 C C . VAL B 1 85 ? 32.744 82.890 88.295 1.00 4.07 ? 167 VAL B C 1 ATOM 3353 O O . VAL B 1 85 ? 33.073 81.760 88.657 1.00 4.07 ? 167 VAL B O 1 ATOM 3354 C CB . VAL B 1 85 ? 34.698 84.248 89.039 1.00 2.00 ? 167 VAL B CB 1 ATOM 3355 C CG1 . VAL B 1 85 ? 35.132 84.469 87.596 1.00 2.00 ? 167 VAL B CG1 1 ATOM 3356 C CG2 . VAL B 1 85 ? 35.182 85.401 89.917 1.00 2.00 ? 167 VAL B CG2 1 ATOM 3357 N N . VAL B 1 86 ? 31.981 83.118 87.225 1.00 2.00 ? 168 VAL B N 1 ATOM 3358 C CA . VAL B 1 86 ? 31.558 82.039 86.324 1.00 2.00 ? 168 VAL B CA 1 ATOM 3359 C C . VAL B 1 86 ? 32.706 81.899 85.328 1.00 2.00 ? 168 VAL B C 1 ATOM 3360 O O . VAL B 1 86 ? 32.989 82.827 84.570 1.00 2.00 ? 168 VAL B O 1 ATOM 3361 C CB . VAL B 1 86 ? 30.249 82.399 85.597 1.00 9.72 ? 168 VAL B CB 1 ATOM 3362 C CG1 . VAL B 1 86 ? 29.829 81.270 84.674 1.00 9.72 ? 168 VAL B CG1 1 ATOM 3363 C CG2 . VAL B 1 86 ? 29.153 82.684 86.622 1.00 9.72 ? 168 VAL B CG2 1 ATOM 3364 N N . PHE B 1 87 ? 33.356 80.739 85.316 1.00 6.24 ? 169 PHE B N 1 ATOM 3365 C CA . PHE B 1 87 ? 34.538 80.553 84.476 1.00 6.24 ? 169 PHE B CA 1 ATOM 3366 C C . PHE B 1 87 ? 34.743 79.102 84.024 1.00 6.24 ? 169 PHE B C 1 ATOM 3367 O O . PHE B 1 87 ? 35.611 78.400 84.545 1.00 6.24 ? 169 PHE B O 1 ATOM 3368 C CB . PHE B 1 87 ? 35.738 81.040 85.306 1.00 6.53 ? 169 PHE B CB 1 ATOM 3369 C CG . PHE B 1 87 ? 37.037 81.101 84.564 1.00 6.53 ? 169 PHE B CG 1 ATOM 3370 C CD1 . PHE B 1 87 ? 37.149 81.803 83.371 1.00 6.53 ? 169 PHE B CD1 1 ATOM 3371 C CD2 . PHE B 1 87 ? 38.174 80.514 85.105 1.00 6.53 ? 169 PHE B CD2 1 ATOM 3372 C CE1 . PHE B 1 87 ? 38.379 81.924 82.732 1.00 6.53 ? 169 PHE B CE1 1 ATOM 3373 C CE2 . PHE B 1 87 ? 39.407 80.630 84.474 1.00 6.53 ? 169 PHE B CE2 1 ATOM 3374 C CZ . PHE B 1 87 ? 39.509 81.337 83.287 1.00 6.53 ? 169 PHE B CZ 1 ATOM 3375 N N . ASP B 1 88 ? 33.982 78.669 83.021 1.00 7.74 ? 170 ASP B N 1 ATOM 3376 C CA . ASP B 1 88 ? 34.103 77.293 82.538 1.00 7.74 ? 170 ASP B CA 1 ATOM 3377 C C . ASP B 1 88 ? 33.649 77.112 81.090 1.00 7.74 ? 170 ASP B C 1 ATOM 3378 O O . ASP B 1 88 ? 33.115 76.065 80.716 1.00 7.74 ? 170 ASP B O 1 ATOM 3379 C CB . ASP B 1 88 ? 33.314 76.357 83.452 1.00 6.74 ? 170 ASP B CB 1 ATOM 3380 C CG . ASP B 1 88 ? 33.850 74.940 83.450 1.00 6.74 ? 170 ASP B CG 1 ATOM 3381 O OD1 . ASP B 1 88 ? 34.939 74.691 82.892 1.00 6.74 ? 170 ASP B OD1 1 ATOM 3382 O OD2 . ASP B 1 88 ? 33.171 74.070 84.023 1.00 6.74 ? 170 ASP B OD2 1 ATOM 3383 N N . LEU B 1 89 ? 33.901 78.131 80.278 1.00 8.70 ? 171 LEU B N 1 ATOM 3384 C CA . LEU B 1 89 ? 33.540 78.137 78.867 1.00 8.70 ? 171 LEU B CA 1 ATOM 3385 C C . LEU B 1 89 ? 34.280 77.026 78.111 1.00 8.70 ? 171 LEU B C 1 ATOM 3386 O O . LEU B 1 89 ? 35.419 76.699 78.444 1.00 8.70 ? 171 LEU B O 1 ATOM 3387 C CB . LEU B 1 89 ? 33.925 79.501 78.292 1.00 7.86 ? 171 LEU B CB 1 ATOM 3388 C CG . LEU B 1 89 ? 33.042 80.275 77.323 1.00 7.86 ? 171 LEU B CG 1 ATOM 3389 C CD1 . LEU B 1 89 ? 31.594 80.306 77.764 1.00 7.86 ? 171 LEU B CD1 1 ATOM 3390 C CD2 . LEU B 1 89 ? 33.605 81.691 77.229 1.00 7.86 ? 171 LEU B CD2 1 ATOM 3391 N N . PRO B 1 90 ? 33.617 76.383 77.129 1.00 9.87 ? 172 PRO B N 1 ATOM 3392 C CA . PRO B 1 90 ? 34.280 75.317 76.365 1.00 9.87 ? 172 PRO B CA 1 ATOM 3393 C C . PRO B 1 90 ? 35.408 75.951 75.547 1.00 9.87 ? 172 PRO B C 1 ATOM 3394 O O . PRO B 1 90 ? 35.241 77.054 75.023 1.00 9.87 ? 172 PRO B O 1 ATOM 3395 C CB . PRO B 1 90 ? 33.157 74.780 75.478 1.00 9.20 ? 172 PRO B CB 1 ATOM 3396 C CG . PRO B 1 90 ? 32.243 75.955 75.312 1.00 9.20 ? 172 PRO B CG 1 ATOM 3397 C CD . PRO B 1 90 ? 32.224 76.567 76.684 1.00 9.20 ? 172 PRO B CD 1 ATOM 3398 N N . ASP B 1 91 ? 36.545 75.263 75.449 1.00 9.68 ? 173 ASP B N 1 ATOM 3399 C CA . ASP B 1 91 ? 37.716 75.787 74.742 1.00 9.68 ? 173 ASP B CA 1 ATOM 3400 C C . ASP B 1 91 ? 38.117 77.112 75.396 1.00 9.68 ? 173 ASP B C 1 ATOM 3401 O O . ASP B 1 91 ? 38.484 78.075 74.718 1.00 9.68 ? 173 ASP B O 1 ATOM 3402 C CB . ASP B 1 91 ? 37.431 75.988 73.244 1.00 15.40 ? 173 ASP B CB 1 ATOM 3403 C CG . ASP B 1 91 ? 37.566 74.703 72.439 1.00 15.40 ? 173 ASP B CG 1 ATOM 3404 O OD1 . ASP B 1 91 ? 37.446 73.606 73.020 1.00 15.40 ? 173 ASP B OD1 1 ATOM 3405 O OD2 . ASP B 1 91 ? 37.793 74.792 71.213 1.00 15.40 ? 173 ASP B OD2 1 ATOM 3406 N N . ARG B 1 92 ? 38.036 77.134 76.726 1.00 9.29 ? 174 ARG B N 1 ATOM 3407 C CA . ARG B 1 92 ? 38.351 78.297 77.550 1.00 9.29 ? 174 ARG B CA 1 ATOM 3408 C C . ARG B 1 92 ? 39.759 78.841 77.278 1.00 9.29 ? 174 ARG B C 1 ATOM 3409 O O . ARG B 1 92 ? 40.687 78.071 77.021 1.00 9.29 ? 174 ARG B O 1 ATOM 3410 C CB . ARG B 1 92 ? 38.224 77.904 79.026 1.00 8.10 ? 174 ARG B CB 1 ATOM 3411 C CG . ARG B 1 92 ? 37.839 79.030 79.975 1.00 8.10 ? 174 ARG B CG 1 ATOM 3412 C CD . ARG B 1 92 ? 37.681 78.505 81.410 1.00 8.10 ? 174 ARG B CD 1 ATOM 3413 N NE . ARG B 1 92 ? 38.963 78.093 81.976 1.00 8.10 ? 174 ARG B NE 1 ATOM 3414 C CZ . ARG B 1 92 ? 39.109 77.306 83.037 1.00 8.10 ? 174 ARG B CZ 1 ATOM 3415 N NH1 . ARG B 1 92 ? 38.057 76.835 83.688 1.00 8.10 ? 174 ARG B NH1 1 ATOM 3416 N NH2 . ARG B 1 92 ? 40.322 76.995 83.459 1.00 8.10 ? 174 ARG B NH2 1 ATOM 3417 N N . ASP B 1 93 ? 39.909 80.163 77.355 1.00 4.64 ? 175 ASP B N 1 ATOM 3418 C CA . ASP B 1 93 ? 41.195 80.831 77.130 1.00 4.64 ? 175 ASP B CA 1 ATOM 3419 C C . ASP B 1 93 ? 41.783 80.421 75.777 1.00 4.64 ? 175 ASP B C 1 ATOM 3420 O O . ASP B 1 93 ? 42.914 79.940 75.700 1.00 4.64 ? 175 ASP B O 1 ATOM 3421 C CB . ASP B 1 93 ? 42.179 80.472 78.250 1.00 12.49 ? 175 ASP B CB 1 ATOM 3422 C CG . ASP B 1 93 ? 41.568 80.601 79.636 1.00 12.49 ? 175 ASP B CG 1 ATOM 3423 O OD1 . ASP B 1 93 ? 41.373 81.738 80.113 1.00 12.49 ? 175 ASP B OD1 1 ATOM 3424 O OD2 . ASP B 1 93 ? 41.285 79.558 80.258 1.00 12.49 ? 175 ASP B OD2 1 ATOM 3425 N N . CYS B 1 94 ? 41.025 80.647 74.710 1.00 7.75 ? 176 CYS B N 1 ATOM 3426 C CA . CYS B 1 94 ? 41.438 80.263 73.360 1.00 7.75 ? 176 CYS B CA 1 ATOM 3427 C C . CYS B 1 94 ? 42.822 80.722 72.882 1.00 7.75 ? 176 CYS B C 1 ATOM 3428 O O . CYS B 1 94 ? 43.432 80.064 72.036 1.00 7.75 ? 176 CYS B O 1 ATOM 3429 C CB . CYS B 1 94 ? 40.377 80.699 72.351 1.00 7.25 ? 176 CYS B CB 1 ATOM 3430 S SG . CYS B 1 94 ? 40.139 82.503 72.247 1.00 7.25 ? 176 CYS B SG 1 ATOM 3431 N N . ALA B 1 95 ? 43.310 81.847 73.401 1.00 15.00 ? 177 ALA B N 1 ATOM 3432 C CA . ALA B 1 95 ? 44.611 82.366 72.983 1.00 15.00 ? 177 ALA B CA 1 ATOM 3433 C C . ALA B 1 95 ? 45.794 81.914 73.843 1.00 15.00 ? 177 ALA B C 1 ATOM 3434 O O . ALA B 1 95 ? 46.947 82.169 73.499 1.00 15.00 ? 177 ALA B O 1 ATOM 3435 C CB . ALA B 1 95 ? 44.570 83.886 72.902 1.00 8.88 ? 177 ALA B CB 1 ATOM 3436 N N . ALA B 1 96 ? 45.510 81.237 74.952 1.00 21.48 ? 178 ALA B N 1 ATOM 3437 C CA . ALA B 1 96 ? 46.560 80.763 75.853 1.00 21.48 ? 178 ALA B CA 1 ATOM 3438 C C . ALA B 1 96 ? 47.327 79.556 75.315 1.00 21.48 ? 178 ALA B C 1 ATOM 3439 O O . ALA B 1 96 ? 46.792 78.752 74.547 1.00 21.48 ? 178 ALA B O 1 ATOM 3440 C CB . ALA B 1 96 ? 45.971 80.440 77.218 1.00 9.41 ? 178 ALA B CB 1 ATOM 3441 N N . LEU B 1 97 ? 48.583 79.434 75.739 1.00 29.21 ? 179 LEU B N 1 ATOM 3442 C CA . LEU B 1 97 ? 49.448 78.329 75.328 1.00 29.21 ? 179 LEU B CA 1 ATOM 3443 C C . LEU B 1 97 ? 49.027 77.035 76.016 1.00 29.21 ? 179 LEU B C 1 ATOM 3444 O O . LEU B 1 97 ? 49.294 75.941 75.524 1.00 29.21 ? 179 LEU B O 1 ATOM 3445 C CB . LEU B 1 97 ? 50.907 78.643 75.666 1.00 25.08 ? 179 LEU B CB 1 ATOM 3446 C CG . LEU B 1 97 ? 51.522 79.827 74.918 1.00 25.08 ? 179 LEU B CG 1 ATOM 3447 C CD1 . LEU B 1 97 ? 52.906 80.132 75.468 1.00 25.08 ? 179 LEU B CD1 1 ATOM 3448 C CD2 . LEU B 1 97 ? 51.586 79.514 73.429 1.00 25.08 ? 179 LEU B CD2 1 ATOM 3449 N N . ALA B 1 98 ? 48.373 77.175 77.165 1.00 25.51 ? 180 ALA B N 1 ATOM 3450 C CA . ALA B 1 98 ? 47.896 76.035 77.933 1.00 25.51 ? 180 ALA B CA 1 ATOM 3451 C C . ALA B 1 98 ? 46.624 76.425 78.680 1.00 25.51 ? 180 ALA B C 1 ATOM 3452 O O . ALA B 1 98 ? 46.588 77.437 79.380 1.00 25.51 ? 180 ALA B O 1 ATOM 3453 C CB . ALA B 1 98 ? 48.962 75.586 78.909 1.00 21.90 ? 180 ALA B CB 1 ATOM 3454 N N . SER B 1 99 ? 45.570 75.637 78.503 1.00 26.90 ? 181 SER B N 1 ATOM 3455 C CA . SER B 1 99 ? 44.302 75.909 79.167 1.00 26.90 ? 181 SER B CA 1 ATOM 3456 C C . SER B 1 99 ? 43.903 74.763 80.085 1.00 26.90 ? 181 SER B C 1 ATOM 3457 O O . SER B 1 99 ? 44.075 73.595 79.748 1.00 26.90 ? 181 SER B O 1 ATOM 3458 C CB . SER B 1 99 ? 43.199 76.152 78.137 1.00 42.37 ? 181 SER B CB 1 ATOM 3459 O OG . SER B 1 99 ? 41.949 76.353 78.776 1.00 42.37 ? 181 SER B OG 1 ATOM 3460 N N . ASN B 1 100 ? 43.365 75.109 81.246 1.00 23.77 ? 182 ASN B N 1 ATOM 3461 C CA . ASN B 1 100 ? 42.929 74.113 82.214 1.00 23.77 ? 182 ASN B CA 1 ATOM 3462 C C . ASN B 1 100 ? 41.427 73.852 82.110 1.00 23.77 ? 182 ASN B C 1 ATOM 3463 O O . ASN B 1 100 ? 40.862 73.133 82.935 1.00 23.77 ? 182 ASN B O 1 ATOM 3464 C CB . ASN B 1 100 ? 43.295 74.558 83.634 1.00 39.31 ? 182 ASN B CB 1 ATOM 3465 C CG . ASN B 1 100 ? 44.795 74.606 83.863 1.00 39.31 ? 182 ASN B CG 1 ATOM 3466 O OD1 . ASN B 1 100 ? 45.442 73.570 84.005 1.00 39.31 ? 182 ASN B OD1 1 ATOM 3467 N ND2 . ASN B 1 100 ? 45.356 75.810 83.903 1.00 39.31 ? 182 ASN B ND2 1 ATOM 3468 N N . GLY B 1 101 ? 40.793 74.419 81.083 1.00 13.26 ? 183 GLY B N 1 ATOM 3469 C CA . GLY B 1 101 ? 39.359 74.248 80.885 1.00 13.26 ? 183 GLY B CA 1 ATOM 3470 C C . GLY B 1 101 ? 38.960 72.801 80.684 1.00 13.26 ? 183 GLY B C 1 ATOM 3471 O O . GLY B 1 101 ? 39.507 72.121 79.819 1.00 13.26 ? 183 GLY B O 1 ATOM 3472 N N . GLU B 1 102 ? 37.982 72.342 81.461 1.00 14.25 ? 184 GLU B N 1 ATOM 3473 C CA . GLU B 1 102 ? 37.515 70.956 81.395 1.00 14.25 ? 184 GLU B CA 1 ATOM 3474 C C . GLU B 1 102 ? 36.633 70.583 80.201 1.00 14.25 ? 184 GLU B C 1 ATOM 3475 O O . GLU B 1 102 ? 36.509 69.400 79.873 1.00 14.25 ? 184 GLU B O 1 ATOM 3476 C CB . GLU B 1 102 ? 36.792 70.583 82.692 1.00 10.70 ? 184 GLU B CB 1 ATOM 3477 C CG . GLU B 1 102 ? 35.472 71.319 82.915 1.00 10.70 ? 184 GLU B CG 1 ATOM 3478 C CD . GLU B 1 102 ? 34.780 70.925 84.207 1.00 10.70 ? 184 GLU B CD 1 ATOM 3479 O OE1 . GLU B 1 102 ? 35.066 69.842 84.753 1.00 10.70 ? 184 GLU B OE1 1 ATOM 3480 O OE2 . GLU B 1 102 ? 33.933 71.699 84.677 1.00 10.70 ? 184 GLU B OE2 1 ATOM 3481 N N . TYR B 1 103 ? 36.012 71.573 79.564 1.00 11.19 ? 185 TYR B N 1 ATOM 3482 C CA . TYR B 1 103 ? 35.139 71.307 78.423 1.00 11.19 ? 185 TYR B CA 1 ATOM 3483 C C . TYR B 1 103 ? 35.749 71.714 77.088 1.00 11.19 ? 185 TYR B C 1 ATOM 3484 O O . TYR B 1 103 ? 36.463 72.719 76.989 1.00 11.19 ? 185 TYR B O 1 ATOM 3485 C CB . TYR B 1 103 ? 33.780 71.992 78.603 1.00 8.74 ? 185 TYR B CB 1 ATOM 3486 C CG . TYR B 1 103 ? 33.030 71.556 79.844 1.00 8.74 ? 185 TYR B CG 1 ATOM 3487 C CD1 . TYR B 1 103 ? 32.974 70.210 80.214 1.00 8.74 ? 185 TYR B CD1 1 ATOM 3488 C CD2 . TYR B 1 103 ? 32.372 72.488 80.647 1.00 8.74 ? 185 TYR B CD2 1 ATOM 3489 C CE1 . TYR B 1 103 ? 32.283 69.805 81.355 1.00 8.74 ? 185 TYR B CE1 1 ATOM 3490 C CE2 . TYR B 1 103 ? 31.679 72.094 81.786 1.00 8.74 ? 185 TYR B CE2 1 ATOM 3491 C CZ . TYR B 1 103 ? 31.638 70.754 82.133 1.00 8.74 ? 185 TYR B CZ 1 ATOM 3492 O OH . TYR B 1 103 ? 30.969 70.367 83.269 1.00 8.74 ? 185 TYR B OH 1 ATOM 3493 N N . SER B 1 104 ? 35.461 70.913 76.068 1.00 11.42 ? 186 SER B N 1 ATOM 3494 C CA . SER B 1 104 ? 35.950 71.138 74.716 1.00 11.42 ? 186 SER B CA 1 ATOM 3495 C C . SER B 1 104 ? 34.772 71.248 73.758 1.00 11.42 ? 186 SER B C 1 ATOM 3496 O O . SER B 1 104 ? 33.837 70.449 73.823 1.00 11.42 ? 186 SER B O 1 ATOM 3497 C CB . SER B 1 104 ? 36.843 69.974 74.282 1.00 52.50 ? 186 SER B CB 1 ATOM 3498 O OG . SER B 1 104 ? 37.181 70.082 72.911 1.00 52.50 ? 186 SER B OG 1 ATOM 3499 N N . ILE B 1 105 ? 34.817 72.237 72.871 1.00 13.19 ? 187 ILE B N 1 ATOM 3500 C CA . ILE B 1 105 ? 33.751 72.436 71.896 1.00 13.19 ? 187 ILE B CA 1 ATOM 3501 C C . ILE B 1 105 ? 33.556 71.177 71.053 1.00 13.19 ? 187 ILE B C 1 ATOM 3502 O O . ILE B 1 105 ? 32.425 70.768 70.788 1.00 13.19 ? 187 ILE B O 1 ATOM 3503 C CB . ILE B 1 105 ? 34.065 73.630 70.971 1.00 14.72 ? 187 ILE B CB 1 ATOM 3504 C CG1 . ILE B 1 105 ? 34.104 74.926 71.782 1.00 14.72 ? 187 ILE B CG1 1 ATOM 3505 C CG2 . ILE B 1 105 ? 33.033 73.732 69.857 1.00 14.72 ? 187 ILE B CG2 1 ATOM 3506 C CD1 . ILE B 1 105 ? 34.537 76.137 70.986 1.00 14.72 ? 187 ILE B CD1 1 ATOM 3507 N N . ALA B 1 106 ? 34.668 70.542 70.692 1.00 23.62 ? 188 ALA B N 1 ATOM 3508 C CA . ALA B 1 106 ? 34.664 69.328 69.879 1.00 23.62 ? 188 ALA B CA 1 ATOM 3509 C C . ALA B 1 106 ? 33.967 68.148 70.548 1.00 23.62 ? 188 ALA B C 1 ATOM 3510 O O . ALA B 1 106 ? 33.392 67.295 69.871 1.00 23.62 ? 188 ALA B O 1 ATOM 3511 C CB . ALA B 1 106 ? 36.089 68.942 69.517 1.00 31.43 ? 188 ALA B CB 1 ATOM 3512 N N . ASP B 1 107 ? 34.027 68.096 71.873 1.00 17.14 ? 189 ASP B N 1 ATOM 3513 C CA . ASP B 1 107 ? 33.407 67.010 72.616 1.00 17.14 ? 189 ASP B CA 1 ATOM 3514 C C . ASP B 1 107 ? 32.175 67.484 73.389 1.00 17.14 ? 189 ASP B C 1 ATOM 3515 O O . ASP B 1 107 ? 32.128 67.397 74.616 1.00 17.14 ? 189 ASP B O 1 ATOM 3516 C CB . ASP B 1 107 ? 34.439 66.374 73.554 1.00 33.23 ? 189 ASP B CB 1 ATOM 3517 C CG . ASP B 1 107 ? 33.971 65.050 74.143 1.00 33.23 ? 189 ASP B CG 1 ATOM 3518 O OD1 . ASP B 1 107 ? 33.037 64.424 73.592 1.00 33.23 ? 189 ASP B OD1 1 ATOM 3519 O OD2 . ASP B 1 107 ? 34.556 64.630 75.165 1.00 33.23 ? 189 ASP B OD2 1 ATOM 3520 N N . GLY B 1 108 ? 31.200 68.015 72.653 1.00 17.00 ? 190 GLY B N 1 ATOM 3521 C CA . GLY B 1 108 ? 29.958 68.493 73.242 1.00 17.00 ? 190 GLY B CA 1 ATOM 3522 C C . GLY B 1 108 ? 30.106 69.505 74.366 1.00 17.00 ? 190 GLY B C 1 ATOM 3523 O O . GLY B 1 108 ? 29.348 69.479 75.335 1.00 17.00 ? 190 GLY B O 1 ATOM 3524 N N . GLY B 1 109 ? 31.058 70.420 74.216 1.00 10.23 ? 191 GLY B N 1 ATOM 3525 C CA . GLY B 1 109 ? 31.302 71.422 75.234 1.00 10.23 ? 191 GLY B CA 1 ATOM 3526 C C . GLY B 1 109 ? 30.190 72.426 75.452 1.00 10.23 ? 191 GLY B C 1 ATOM 3527 O O . GLY B 1 109 ? 30.003 72.901 76.571 1.00 10.23 ? 191 GLY B O 1 ATOM 3528 N N . VAL B 1 110 ? 29.469 72.774 74.391 1.00 10.21 ? 192 VAL B N 1 ATOM 3529 C CA . VAL B 1 110 ? 28.381 73.738 74.507 1.00 10.21 ? 192 VAL B CA 1 ATOM 3530 C C . VAL B 1 110 ? 27.252 73.187 75.381 1.00 10.21 ? 192 VAL B C 1 ATOM 3531 O O . VAL B 1 110 ? 26.766 73.872 76.281 1.00 10.21 ? 192 VAL B O 1 ATOM 3532 C CB . VAL B 1 110 ? 27.866 74.167 73.108 1.00 11.13 ? 192 VAL B CB 1 ATOM 3533 C CG1 . VAL B 1 110 ? 26.588 74.989 73.220 1.00 11.13 ? 192 VAL B CG1 1 ATOM 3534 C CG2 . VAL B 1 110 ? 28.940 74.990 72.406 1.00 11.13 ? 192 VAL B CG2 1 ATOM 3535 N N . ALA B 1 111 ? 26.882 71.930 75.146 1.00 6.85 ? 193 ALA B N 1 ATOM 3536 C CA . ALA B 1 111 ? 25.824 71.277 75.912 1.00 6.85 ? 193 ALA B CA 1 ATOM 3537 C C . ALA B 1 111 ? 26.264 71.105 77.360 1.00 6.85 ? 193 ALA B C 1 ATOM 3538 O O . ALA B 1 111 ? 25.469 71.251 78.281 1.00 6.85 ? 193 ALA B O 1 ATOM 3539 C CB . ALA B 1 111 ? 25.479 69.921 75.299 1.00 8.76 ? 193 ALA B CB 1 ATOM 3540 N N . LYS B 1 112 ? 27.540 70.787 77.553 1.00 5.28 ? 194 LYS B N 1 ATOM 3541 C CA . LYS B 1 112 ? 28.087 70.618 78.896 1.00 5.28 ? 194 LYS B CA 1 ATOM 3542 C C . LYS B 1 112 ? 28.078 71.949 79.640 1.00 5.28 ? 194 LYS B C 1 ATOM 3543 O O . LYS B 1 112 ? 27.768 71.994 80.821 1.00 5.28 ? 194 LYS B O 1 ATOM 3544 C CB . LYS B 1 112 ? 29.511 70.046 78.834 1.00 34.59 ? 194 LYS B CB 1 ATOM 3545 C CG . LYS B 1 112 ? 29.580 68.566 78.446 1.00 34.59 ? 194 LYS B CG 1 ATOM 3546 C CD . LYS B 1 112 ? 29.790 67.641 79.650 1.00 34.59 ? 194 LYS B CD 1 ATOM 3547 C CE . LYS B 1 112 ? 28.833 67.953 80.804 1.00 34.59 ? 194 LYS B CE 1 ATOM 3548 N NZ . LYS B 1 112 ? 28.770 66.891 81.851 1.00 34.59 ? 194 LYS B NZ 1 ATOM 3549 N N . TYR B 1 113 ? 28.383 73.036 78.933 1.00 4.91 ? 195 TYR B N 1 ATOM 3550 C CA . TYR B 1 113 ? 28.398 74.359 79.545 1.00 4.91 ? 195 TYR B CA 1 ATOM 3551 C C . TYR B 1 113 ? 26.996 74.792 79.976 1.00 4.91 ? 195 TYR B C 1 ATOM 3552 O O . TYR B 1 113 ? 26.834 75.434 81.010 1.00 4.91 ? 195 TYR B O 1 ATOM 3553 C CB . TYR B 1 113 ? 28.990 75.402 78.593 1.00 7.31 ? 195 TYR B CB 1 ATOM 3554 C CG . TYR B 1 113 ? 29.119 76.771 79.232 1.00 7.31 ? 195 TYR B CG 1 ATOM 3555 C CD1 . TYR B 1 113 ? 30.161 77.049 80.114 1.00 7.31 ? 195 TYR B CD1 1 ATOM 3556 C CD2 . TYR B 1 113 ? 28.186 77.780 78.977 1.00 7.31 ? 195 TYR B CD2 1 ATOM 3557 C CE1 . TYR B 1 113 ? 30.274 78.296 80.730 1.00 7.31 ? 195 TYR B CE1 1 ATOM 3558 C CE2 . TYR B 1 113 ? 28.291 79.031 79.588 1.00 7.31 ? 195 TYR B CE2 1 ATOM 3559 C CZ . TYR B 1 113 ? 29.341 79.283 80.462 1.00 7.31 ? 195 TYR B CZ 1 ATOM 3560 O OH . TYR B 1 113 ? 29.457 80.519 81.065 1.00 7.31 ? 195 TYR B OH 1 ATOM 3561 N N . LYS B 1 114 ? 25.989 74.467 79.167 1.00 5.31 ? 196 LYS B N 1 ATOM 3562 C CA . LYS B 1 114 ? 24.615 74.824 79.504 1.00 5.31 ? 196 LYS B CA 1 ATOM 3563 C C . LYS B 1 114 ? 24.159 74.090 80.762 1.00 5.31 ? 196 LYS B C 1 ATOM 3564 O O . LYS B 1 114 ? 23.414 74.645 81.569 1.00 5.31 ? 196 LYS B O 1 ATOM 3565 C CB . LYS B 1 114 ? 23.678 74.543 78.330 1.00 17.39 ? 196 LYS B CB 1 ATOM 3566 C CG . LYS B 1 114 ? 23.959 75.440 77.141 1.00 17.39 ? 196 LYS B CG 1 ATOM 3567 C CD . LYS B 1 114 ? 22.936 75.264 76.039 1.00 17.39 ? 196 LYS B CD 1 ATOM 3568 C CE . LYS B 1 114 ? 23.211 76.228 74.894 1.00 17.39 ? 196 LYS B CE 1 ATOM 3569 N NZ . LYS B 1 114 ? 22.171 76.124 73.831 1.00 17.39 ? 196 LYS B NZ 1 ATOM 3570 N N . ASN B 1 115 ? 24.634 72.859 80.941 1.00 6.21 ? 197 ASN B N 1 ATOM 3571 C CA . ASN B 1 115 ? 24.292 72.070 82.126 1.00 6.21 ? 197 ASN B CA 1 ATOM 3572 C C . ASN B 1 115 ? 24.930 72.728 83.347 1.00 6.21 ? 197 ASN B C 1 ATOM 3573 O O . ASN B 1 115 ? 24.346 72.765 84.426 1.00 6.21 ? 197 ASN B O 1 ATOM 3574 C CB . ASN B 1 115 ? 24.815 70.644 81.987 1.00 6.39 ? 197 ASN B CB 1 ATOM 3575 C CG . ASN B 1 115 ? 24.536 69.812 83.214 1.00 6.39 ? 197 ASN B CG 1 ATOM 3576 O OD1 . ASN B 1 115 ? 23.378 69.557 83.550 1.00 6.39 ? 197 ASN B OD1 1 ATOM 3577 N ND2 . ASN B 1 115 ? 25.590 69.407 83.909 1.00 6.39 ? 197 ASN B ND2 1 ATOM 3578 N N . TYR B 1 116 ? 26.154 73.213 83.161 1.00 5.70 ? 198 TYR B N 1 ATOM 3579 C CA . TYR B 1 116 ? 26.907 73.903 84.200 1.00 5.70 ? 198 TYR B CA 1 ATOM 3580 C C . TYR B 1 116 ? 26.132 75.161 84.625 1.00 5.70 ? 198 TYR B C 1 ATOM 3581 O O . TYR B 1 116 ? 25.974 75.420 85.817 1.00 5.70 ? 198 TYR B O 1 ATOM 3582 C CB . TYR B 1 116 ? 28.309 74.229 83.648 1.00 5.97 ? 198 TYR B CB 1 ATOM 3583 C CG . TYR B 1 116 ? 29.101 75.307 84.356 1.00 5.97 ? 198 TYR B CG 1 ATOM 3584 C CD1 . TYR B 1 116 ? 29.865 75.020 85.488 1.00 5.97 ? 198 TYR B CD1 1 ATOM 3585 C CD2 . TYR B 1 116 ? 29.140 76.602 83.850 1.00 5.97 ? 198 TYR B CD2 1 ATOM 3586 C CE1 . TYR B 1 116 ? 30.653 76.003 86.094 1.00 5.97 ? 198 TYR B CE1 1 ATOM 3587 C CE2 . TYR B 1 116 ? 29.920 77.590 84.444 1.00 5.97 ? 198 TYR B CE2 1 ATOM 3588 C CZ . TYR B 1 116 ? 30.673 77.285 85.561 1.00 5.97 ? 198 TYR B CZ 1 ATOM 3589 O OH . TYR B 1 116 ? 31.438 78.273 86.136 1.00 5.97 ? 198 TYR B OH 1 ATOM 3590 N N . ILE B 1 117 ? 25.594 75.898 83.654 1.00 6.48 ? 199 ILE B N 1 ATOM 3591 C CA . ILE B 1 117 ? 24.819 77.112 83.941 1.00 6.48 ? 199 ILE B CA 1 ATOM 3592 C C . ILE B 1 117 ? 23.479 76.758 84.594 1.00 6.48 ? 199 ILE B C 1 ATOM 3593 O O . ILE B 1 117 ? 23.008 77.475 85.478 1.00 6.48 ? 199 ILE B O 1 ATOM 3594 C CB . ILE B 1 117 ? 24.573 77.952 82.653 1.00 4.80 ? 199 ILE B CB 1 ATOM 3595 C CG1 . ILE B 1 117 ? 25.899 78.517 82.126 1.00 4.80 ? 199 ILE B CG1 1 ATOM 3596 C CG2 . ILE B 1 117 ? 23.617 79.105 82.928 1.00 4.80 ? 199 ILE B CG2 1 ATOM 3597 C CD1 . ILE B 1 117 ? 26.575 79.525 83.058 1.00 4.80 ? 199 ILE B CD1 1 ATOM 3598 N N . ASP B 1 118 ? 22.884 75.643 84.174 1.00 2.00 ? 200 ASP B N 1 ATOM 3599 C CA . ASP B 1 118 ? 21.615 75.182 84.737 1.00 2.00 ? 200 ASP B CA 1 ATOM 3600 C C . ASP B 1 118 ? 21.804 74.861 86.209 1.00 2.00 ? 200 ASP B C 1 ATOM 3601 O O . ASP B 1 118 ? 20.923 75.117 87.033 1.00 2.00 ? 200 ASP B O 1 ATOM 3602 C CB . ASP B 1 118 ? 21.126 73.915 84.022 1.00 10.64 ? 200 ASP B CB 1 ATOM 3603 C CG . ASP B 1 118 ? 20.643 74.179 82.605 1.00 10.64 ? 200 ASP B CG 1 ATOM 3604 O OD1 . ASP B 1 118 ? 20.410 75.352 82.257 1.00 10.64 ? 200 ASP B OD1 1 ATOM 3605 O OD2 . ASP B 1 118 ? 20.491 73.202 81.841 1.00 10.64 ? 200 ASP B OD2 1 ATOM 3606 N N . THR B 1 119 ? 22.960 74.280 86.518 1.00 7.81 ? 201 THR B N 1 ATOM 3607 C CA . THR B 1 119 ? 23.304 73.902 87.881 1.00 7.81 ? 201 THR B CA 1 ATOM 3608 C C . THR B 1 119 ? 23.448 75.139 88.763 1.00 7.81 ? 201 THR B C 1 ATOM 3609 O O . THR B 1 119 ? 22.924 75.169 89.877 1.00 7.81 ? 201 THR B O 1 ATOM 3610 C CB . THR B 1 119 ? 24.603 73.068 87.912 1.00 5.63 ? 201 THR B CB 1 ATOM 3611 O OG1 . THR B 1 119 ? 24.438 71.896 87.097 1.00 5.63 ? 201 THR B OG1 1 ATOM 3612 C CG2 . THR B 1 119 ? 24.936 72.653 89.329 1.00 5.63 ? 201 THR B CG2 1 ATOM 3613 N N . ILE B 1 120 ? 24.136 76.160 88.254 1.00 9.79 ? 202 ILE B N 1 ATOM 3614 C CA . ILE B 1 120 ? 24.324 77.408 88.997 1.00 9.79 ? 202 ILE B CA 1 ATOM 3615 C C . ILE B 1 120 ? 22.985 78.125 89.196 1.00 9.79 ? 202 ILE B C 1 ATOM 3616 O O . ILE B 1 120 ? 22.722 78.667 90.271 1.00 9.79 ? 202 ILE B O 1 ATOM 3617 C CB . ILE B 1 120 ? 25.316 78.366 88.279 1.00 5.79 ? 202 ILE B CB 1 ATOM 3618 C CG1 . ILE B 1 120 ? 26.720 77.759 88.269 1.00 5.79 ? 202 ILE B CG1 1 ATOM 3619 C CG2 . ILE B 1 120 ? 25.357 79.725 88.976 1.00 5.79 ? 202 ILE B CG2 1 ATOM 3620 C CD1 . ILE B 1 120 ? 27.754 78.612 87.549 1.00 5.79 ? 202 ILE B CD1 1 ATOM 3621 N N . ARG B 1 121 ? 22.132 78.110 88.174 1.00 5.37 ? 203 ARG B N 1 ATOM 3622 C CA . ARG B 1 121 ? 20.831 78.768 88.275 1.00 5.37 ? 203 ARG B CA 1 ATOM 3623 C C . ARG B 1 121 ? 19.987 78.210 89.419 1.00 5.37 ? 203 ARG B C 1 ATOM 3624 O O . ARG B 1 121 ? 19.397 78.973 90.184 1.00 5.37 ? 203 ARG B O 1 ATOM 3625 C CB . ARG B 1 121 ? 20.051 78.669 86.959 1.00 14.42 ? 203 ARG B CB 1 ATOM 3626 C CG . ARG B 1 121 ? 18.646 79.263 87.050 1.00 14.42 ? 203 ARG B CG 1 ATOM 3627 C CD . ARG B 1 121 ? 17.882 79.142 85.742 1.00 14.42 ? 203 ARG B CD 1 ATOM 3628 N NE . ARG B 1 121 ? 16.450 79.379 85.923 1.00 14.42 ? 203 ARG B NE 1 ATOM 3629 C CZ . ARG B 1 121 ? 15.839 80.547 85.730 1.00 14.42 ? 203 ARG B CZ 1 ATOM 3630 N NH1 . ARG B 1 121 ? 16.524 81.610 85.333 1.00 14.42 ? 203 ARG B NH1 1 ATOM 3631 N NH2 . ARG B 1 121 ? 14.529 80.648 85.926 1.00 14.42 ? 203 ARG B NH2 1 ATOM 3632 N N . GLN B 1 122 ? 19.944 76.882 89.540 1.00 11.15 ? 204 GLN B N 1 ATOM 3633 C CA . GLN B 1 122 ? 19.171 76.226 90.597 1.00 11.15 ? 204 GLN B CA 1 ATOM 3634 C C . GLN B 1 122 ? 19.618 76.656 91.985 1.00 11.15 ? 204 GLN B C 1 ATOM 3635 O O . GLN B 1 122 ? 18.796 76.847 92.878 1.00 11.15 ? 204 GLN B O 1 ATOM 3636 C CB . GLN B 1 122 ? 19.250 74.703 90.476 1.00 57.78 ? 204 GLN B CB 1 ATOM 3637 C CG . GLN B 1 122 ? 18.176 74.105 89.588 1.00 57.78 ? 204 GLN B CG 1 ATOM 3638 C CD . GLN B 1 122 ? 18.279 72.595 89.476 1.00 57.78 ? 204 GLN B CD 1 ATOM 3639 O OE1 . GLN B 1 122 ? 18.712 71.910 90.412 1.00 57.78 ? 204 GLN B OE1 1 ATOM 3640 N NE2 . GLN B 1 122 ? 17.870 72.065 88.329 1.00 57.78 ? 204 GLN B NE2 1 ATOM 3641 N N . ILE B 1 123 ? 20.925 76.813 92.157 1.00 5.85 ? 205 ILE B N 1 ATOM 3642 C CA . ILE B 1 123 ? 21.488 77.241 93.429 1.00 5.85 ? 205 ILE B CA 1 ATOM 3643 C C . ILE B 1 123 ? 21.039 78.675 93.734 1.00 5.85 ? 205 ILE B C 1 ATOM 3644 O O . ILE B 1 123 ? 20.563 78.969 94.831 1.00 5.85 ? 205 ILE B O 1 ATOM 3645 C CB . ILE B 1 123 ? 23.034 77.143 93.391 1.00 5.46 ? 205 ILE B CB 1 ATOM 3646 C CG1 . ILE B 1 123 ? 23.445 75.675 93.209 1.00 5.46 ? 205 ILE B CG1 1 ATOM 3647 C CG2 . ILE B 1 123 ? 23.641 77.705 94.669 1.00 5.46 ? 205 ILE B CG2 1 ATOM 3648 C CD1 . ILE B 1 123 ? 24.927 75.449 93.008 1.00 5.46 ? 205 ILE B CD1 1 ATOM 3649 N N . VAL B 1 124 ? 21.141 79.550 92.737 1.00 9.21 ? 206 VAL B N 1 ATOM 3650 C CA . VAL B 1 124 ? 20.748 80.946 92.896 1.00 9.21 ? 206 VAL B CA 1 ATOM 3651 C C . VAL B 1 124 ? 19.246 81.085 93.163 1.00 9.21 ? 206 VAL B C 1 ATOM 3652 O O . VAL B 1 124 ? 18.828 81.950 93.933 1.00 9.21 ? 206 VAL B O 1 ATOM 3653 C CB . VAL B 1 124 ? 21.161 81.777 91.661 1.00 11.77 ? 206 VAL B CB 1 ATOM 3654 C CG1 . VAL B 1 124 ? 20.709 83.219 91.809 1.00 11.77 ? 206 VAL B CG1 1 ATOM 3655 C CG2 . VAL B 1 124 ? 22.673 81.724 91.489 1.00 11.77 ? 206 VAL B CG2 1 ATOM 3656 N N . VAL B 1 125 ? 18.439 80.234 92.535 1.00 14.61 ? 207 VAL B N 1 ATOM 3657 C CA . VAL B 1 125 ? 16.996 80.266 92.742 1.00 14.61 ? 207 VAL B CA 1 ATOM 3658 C C . VAL B 1 125 ? 16.709 79.746 94.152 1.00 14.61 ? 207 VAL B C 1 ATOM 3659 O O . VAL B 1 125 ? 15.807 80.234 94.833 1.00 14.61 ? 207 VAL B O 1 ATOM 3660 C CB . VAL B 1 125 ? 16.249 79.413 91.680 1.00 9.62 ? 207 VAL B CB 1 ATOM 3661 C CG1 . VAL B 1 125 ? 14.767 79.270 92.036 1.00 9.62 ? 207 VAL B CG1 1 ATOM 3662 C CG2 . VAL B 1 125 ? 16.385 80.059 90.314 1.00 9.62 ? 207 VAL B CG2 1 ATOM 3663 N N . GLU B 1 126 ? 17.515 78.790 94.603 1.00 13.65 ? 208 GLU B N 1 ATOM 3664 C CA . GLU B 1 126 ? 17.354 78.224 95.938 1.00 13.65 ? 208 GLU B CA 1 ATOM 3665 C C . GLU B 1 126 ? 17.675 79.282 96.997 1.00 13.65 ? 208 GLU B C 1 ATOM 3666 O O . GLU B 1 126 ? 17.021 79.351 98.036 1.00 13.65 ? 208 GLU B O 1 ATOM 3667 C CB . GLU B 1 126 ? 18.262 77.009 96.117 1.00 78.65 ? 208 GLU B CB 1 ATOM 3668 C CG . GLU B 1 126 ? 18.015 76.230 97.395 1.00 78.65 ? 208 GLU B CG 1 ATOM 3669 C CD . GLU B 1 126 ? 18.873 74.984 97.489 1.00 78.65 ? 208 GLU B CD 1 ATOM 3670 O OE1 . GLU B 1 126 ? 18.826 74.149 96.559 1.00 78.65 ? 208 GLU B OE1 1 ATOM 3671 O OE2 . GLU B 1 126 ? 19.596 74.840 98.499 1.00 78.65 ? 208 GLU B OE2 1 ATOM 3672 N N . TYR B 1 127 ? 18.672 80.117 96.714 1.00 7.75 ? 209 TYR B N 1 ATOM 3673 C CA . TYR B 1 127 ? 19.076 81.167 97.639 1.00 7.75 ? 209 TYR B CA 1 ATOM 3674 C C . TYR B 1 127 ? 18.668 82.544 97.138 1.00 7.75 ? 209 TYR B C 1 ATOM 3675 O O . TYR B 1 127 ? 19.478 83.473 97.086 1.00 7.75 ? 209 TYR B O 1 ATOM 3676 C CB . TYR B 1 127 ? 20.583 81.094 97.899 1.00 11.39 ? 209 TYR B CB 1 ATOM 3677 C CG . TYR B 1 127 ? 20.974 79.899 98.737 1.00 11.39 ? 209 TYR B CG 1 ATOM 3678 C CD1 . TYR B 1 127 ? 21.218 78.656 98.152 1.00 11.39 ? 209 TYR B CD1 1 ATOM 3679 C CD2 . TYR B 1 127 ? 21.049 79.997 100.122 1.00 11.39 ? 209 TYR B CD2 1 ATOM 3680 C CE1 . TYR B 1 127 ? 21.520 77.538 98.930 1.00 11.39 ? 209 TYR B CE1 1 ATOM 3681 C CE2 . TYR B 1 127 ? 21.347 78.891 100.910 1.00 11.39 ? 209 TYR B CE2 1 ATOM 3682 C CZ . TYR B 1 127 ? 21.581 77.666 100.312 1.00 11.39 ? 209 TYR B CZ 1 ATOM 3683 O OH . TYR B 1 127 ? 21.854 76.570 101.106 1.00 11.39 ? 209 TYR B OH 1 ATOM 3684 N N . SER B 1 128 ? 17.394 82.665 96.780 1.00 10.94 ? 210 SER B N 1 ATOM 3685 C CA . SER B 1 128 ? 16.836 83.915 96.275 1.00 10.94 ? 210 SER B CA 1 ATOM 3686 C C . SER B 1 128 ? 16.918 85.021 97.314 1.00 10.94 ? 210 SER B C 1 ATOM 3687 O O . SER B 1 128 ? 16.850 86.207 96.987 1.00 10.94 ? 210 SER B O 1 ATOM 3688 C CB . SER B 1 128 ? 15.377 83.708 95.877 1.00 28.55 ? 210 SER B CB 1 ATOM 3689 O OG . SER B 1 128 ? 15.267 82.711 94.883 1.00 28.55 ? 210 SER B OG 1 ATOM 3690 N N . ASP B 1 129 ? 17.054 84.622 98.571 1.00 10.45 ? 211 ASP B N 1 ATOM 3691 C CA . ASP B 1 129 ? 17.136 85.557 99.684 1.00 10.45 ? 211 ASP B CA 1 ATOM 3692 C C . ASP B 1 129 ? 18.499 86.240 99.830 1.00 10.45 ? 211 ASP B C 1 ATOM 3693 O O . ASP B 1 129 ? 18.654 87.161 100.635 1.00 10.45 ? 211 ASP B O 1 ATOM 3694 C CB . ASP B 1 129 ? 16.756 84.843 100.988 1.00 14.02 ? 211 ASP B CB 1 ATOM 3695 C CG . ASP B 1 129 ? 17.605 83.601 101.259 1.00 14.02 ? 211 ASP B CG 1 ATOM 3696 O OD1 . ASP B 1 129 ? 17.759 82.745 100.365 1.00 14.02 ? 211 ASP B OD1 1 ATOM 3697 O OD2 . ASP B 1 129 ? 18.104 83.473 102.391 1.00 14.02 ? 211 ASP B OD2 1 ATOM 3698 N N . ILE B 1 130 ? 19.475 85.811 99.035 1.00 8.75 ? 212 ILE B N 1 ATOM 3699 C CA . ILE B 1 130 ? 20.817 86.380 99.109 1.00 8.75 ? 212 ILE B CA 1 ATOM 3700 C C . ILE B 1 130 ? 21.225 87.076 97.821 1.00 8.75 ? 212 ILE B C 1 ATOM 3701 O O . ILE B 1 130 ? 21.127 86.500 96.737 1.00 8.75 ? 212 ILE B O 1 ATOM 3702 C CB . ILE B 1 130 ? 21.868 85.287 99.430 1.00 9.44 ? 212 ILE B CB 1 ATOM 3703 C CG1 . ILE B 1 130 ? 21.485 84.564 100.724 1.00 9.44 ? 212 ILE B CG1 1 ATOM 3704 C CG2 . ILE B 1 130 ? 23.259 85.905 99.571 1.00 9.44 ? 212 ILE B CG2 1 ATOM 3705 C CD1 . ILE B 1 130 ? 22.314 83.347 100.998 1.00 9.44 ? 212 ILE B CD1 1 ATOM 3706 N N . ARG B 1 131 ? 21.681 88.317 97.953 1.00 8.98 ? 213 ARG B N 1 ATOM 3707 C CA . ARG B 1 131 ? 22.140 89.094 96.807 1.00 8.98 ? 213 ARG B CA 1 ATOM 3708 C C . ARG B 1 131 ? 23.438 88.445 96.327 1.00 8.98 ? 213 ARG B C 1 ATOM 3709 O O . ARG B 1 131 ? 24.372 88.242 97.108 1.00 8.98 ? 213 ARG B O 1 ATOM 3710 C CB . ARG B 1 131 ? 22.393 90.547 97.207 1.00 15.14 ? 213 ARG B CB 1 ATOM 3711 C CG . ARG B 1 131 ? 22.473 91.494 96.029 1.00 15.14 ? 213 ARG B CG 1 ATOM 3712 C CD . ARG B 1 131 ? 21.527 92.655 96.226 1.00 15.14 ? 213 ARG B CD 1 ATOM 3713 N NE . ARG B 1 131 ? 22.231 93.866 96.618 1.00 15.14 ? 213 ARG B NE 1 ATOM 3714 C CZ . ARG B 1 131 ? 21.731 94.807 97.411 1.00 15.14 ? 213 ARG B CZ 1 ATOM 3715 N NH1 . ARG B 1 131 ? 20.520 94.681 97.933 1.00 15.14 ? 213 ARG B NH1 1 ATOM 3716 N NH2 . ARG B 1 131 ? 22.458 95.873 97.695 1.00 15.14 ? 213 ARG B NH2 1 ATOM 3717 N N . THR B 1 132 ? 23.482 88.101 95.045 1.00 8.27 ? 214 THR B N 1 ATOM 3718 C CA . THR B 1 132 ? 24.647 87.443 94.478 1.00 8.27 ? 214 THR B CA 1 ATOM 3719 C C . THR B 1 132 ? 25.276 88.239 93.347 1.00 8.27 ? 214 THR B C 1 ATOM 3720 O O . THR B 1 132 ? 24.646 88.496 92.318 1.00 8.27 ? 214 THR B O 1 ATOM 3721 C CB . THR B 1 132 ? 24.276 86.039 93.988 1.00 14.63 ? 214 THR B CB 1 ATOM 3722 O OG1 . THR B 1 132 ? 23.719 85.301 95.080 1.00 14.63 ? 214 THR B OG1 1 ATOM 3723 C CG2 . THR B 1 132 ? 25.501 85.304 93.469 1.00 14.63 ? 214 THR B CG2 1 ATOM 3724 N N . LEU B 1 133 ? 26.530 88.620 93.561 1.00 9.19 ? 215 LEU B N 1 ATOM 3725 C CA . LEU B 1 133 ? 27.306 89.400 92.602 1.00 9.19 ? 215 LEU B CA 1 ATOM 3726 C C . LEU B 1 133 ? 28.169 88.446 91.772 1.00 9.19 ? 215 LEU B C 1 ATOM 3727 O O . LEU B 1 133 ? 28.947 87.660 92.323 1.00 9.19 ? 215 LEU B O 1 ATOM 3728 C CB . LEU B 1 133 ? 28.165 90.413 93.360 1.00 14.36 ? 215 LEU B CB 1 ATOM 3729 C CG . LEU B 1 133 ? 27.359 91.181 94.416 1.00 14.36 ? 215 LEU B CG 1 ATOM 3730 C CD1 . LEU B 1 133 ? 28.269 91.900 95.378 1.00 14.36 ? 215 LEU B CD1 1 ATOM 3731 C CD2 . LEU B 1 133 ? 26.405 92.150 93.754 1.00 14.36 ? 215 LEU B CD2 1 ATOM 3732 N N . LEU B 1 134 ? 28.042 88.532 90.448 1.00 5.88 ? 216 LEU B N 1 ATOM 3733 C CA . LEU B 1 134 ? 28.769 87.645 89.547 1.00 5.88 ? 216 LEU B CA 1 ATOM 3734 C C . LEU B 1 134 ? 29.607 88.327 88.473 1.00 5.88 ? 216 LEU B C 1 ATOM 3735 O O . LEU B 1 134 ? 29.196 89.327 87.891 1.00 5.88 ? 216 LEU B O 1 ATOM 3736 C CB . LEU B 1 134 ? 27.787 86.703 88.834 1.00 4.68 ? 216 LEU B CB 1 ATOM 3737 C CG . LEU B 1 134 ? 26.851 85.777 89.617 1.00 4.68 ? 216 LEU B CG 1 ATOM 3738 C CD1 . LEU B 1 134 ? 25.876 85.106 88.650 1.00 4.68 ? 216 LEU B CD1 1 ATOM 3739 C CD2 . LEU B 1 134 ? 27.634 84.738 90.400 1.00 4.68 ? 216 LEU B CD2 1 ATOM 3740 N N . VAL B 1 135 ? 30.794 87.778 88.234 1.00 3.73 ? 217 VAL B N 1 ATOM 3741 C CA . VAL B 1 135 ? 31.675 88.258 87.179 1.00 3.73 ? 217 VAL B CA 1 ATOM 3742 C C . VAL B 1 135 ? 31.547 87.157 86.136 1.00 3.73 ? 217 VAL B C 1 ATOM 3743 O O . VAL B 1 135 ? 31.752 85.977 86.435 1.00 3.73 ? 217 VAL B O 1 ATOM 3744 C CB . VAL B 1 135 ? 33.150 88.386 87.625 1.00 4.15 ? 217 VAL B CB 1 ATOM 3745 C CG1 . VAL B 1 135 ? 34.048 88.640 86.405 1.00 4.15 ? 217 VAL B CG1 1 ATOM 3746 C CG2 . VAL B 1 135 ? 33.298 89.528 88.614 1.00 4.15 ? 217 VAL B CG2 1 ATOM 3747 N N . ILE B 1 136 ? 31.160 87.536 84.926 1.00 2.00 ? 218 ILE B N 1 ATOM 3748 C CA . ILE B 1 136 ? 30.958 86.563 83.864 1.00 2.00 ? 218 ILE B CA 1 ATOM 3749 C C . ILE B 1 136 ? 32.120 86.334 82.903 1.00 2.00 ? 218 ILE B C 1 ATOM 3750 O O . ILE B 1 136 ? 32.574 87.247 82.214 1.00 2.00 ? 218 ILE B O 1 ATOM 3751 C CB . ILE B 1 136 ? 29.692 86.897 83.037 1.00 4.84 ? 218 ILE B CB 1 ATOM 3752 C CG1 . ILE B 1 136 ? 28.477 87.072 83.961 1.00 4.84 ? 218 ILE B CG1 1 ATOM 3753 C CG2 . ILE B 1 136 ? 29.439 85.806 82.001 1.00 4.84 ? 218 ILE B CG2 1 ATOM 3754 C CD1 . ILE B 1 136 ? 28.121 85.838 84.770 1.00 4.84 ? 218 ILE B CD1 1 ATOM 3755 N N . GLU B 1 137 ? 32.608 85.100 82.917 1.00 5.14 ? 219 GLU B N 1 ATOM 3756 C CA . GLU B 1 137 ? 33.666 84.610 82.039 1.00 5.14 ? 219 GLU B CA 1 ATOM 3757 C C . GLU B 1 137 ? 34.884 85.463 81.677 1.00 5.14 ? 219 GLU B C 1 ATOM 3758 O O . GLU B 1 137 ? 34.952 86.032 80.585 1.00 5.14 ? 219 GLU B O 1 ATOM 3759 C CB . GLU B 1 137 ? 33.025 84.075 80.748 1.00 7.00 ? 219 GLU B CB 1 ATOM 3760 C CG . GLU B 1 137 ? 32.054 82.916 80.964 1.00 7.00 ? 219 GLU B CG 1 ATOM 3761 C CD . GLU B 1 137 ? 32.735 81.629 81.404 1.00 7.00 ? 219 GLU B CD 1 ATOM 3762 O OE1 . GLU B 1 137 ? 33.973 81.526 81.270 1.00 7.00 ? 219 GLU B OE1 1 ATOM 3763 O OE2 . GLU B 1 137 ? 32.032 80.709 81.878 1.00 7.00 ? 219 GLU B OE2 1 ATOM 3764 N N . PRO B 1 138 ? 35.871 85.559 82.588 1.00 9.76 ? 220 PRO B N 1 ATOM 3765 C CA . PRO B 1 138 ? 37.072 86.346 82.300 1.00 9.76 ? 220 PRO B CA 1 ATOM 3766 C C . PRO B 1 138 ? 37.811 85.731 81.111 1.00 9.76 ? 220 PRO B C 1 ATOM 3767 O O . PRO B 1 138 ? 37.688 84.530 80.849 1.00 9.76 ? 220 PRO B O 1 ATOM 3768 C CB . PRO B 1 138 ? 37.901 86.182 83.578 1.00 2.00 ? 220 PRO B CB 1 ATOM 3769 C CG . PRO B 1 138 ? 36.875 86.028 84.639 1.00 2.00 ? 220 PRO B CG 1 ATOM 3770 C CD . PRO B 1 138 ? 35.844 85.129 83.997 1.00 2.00 ? 220 PRO B CD 1 ATOM 3771 N N . ASP B 1 139 ? 38.560 86.559 80.388 1.00 8.20 ? 221 ASP B N 1 ATOM 3772 C CA . ASP B 1 139 ? 39.344 86.101 79.242 1.00 8.20 ? 221 ASP B CA 1 ATOM 3773 C C . ASP B 1 139 ? 38.525 85.367 78.177 1.00 8.20 ? 221 ASP B C 1 ATOM 3774 O O . ASP B 1 139 ? 38.945 84.330 77.652 1.00 8.20 ? 221 ASP B O 1 ATOM 3775 C CB . ASP B 1 139 ? 40.509 85.220 79.726 1.00 12.07 ? 221 ASP B CB 1 ATOM 3776 C CG . ASP B 1 139 ? 41.532 84.932 78.630 1.00 12.07 ? 221 ASP B CG 1 ATOM 3777 O OD1 . ASP B 1 139 ? 41.825 85.835 77.820 1.00 12.07 ? 221 ASP B OD1 1 ATOM 3778 O OD2 . ASP B 1 139 ? 42.048 83.801 78.584 1.00 12.07 ? 221 ASP B OD2 1 ATOM 3779 N N . SER B 1 140 ? 37.350 85.896 77.864 1.00 9.54 ? 222 SER B N 1 ATOM 3780 C CA . SER B 1 140 ? 36.518 85.280 76.840 1.00 9.54 ? 222 SER B CA 1 ATOM 3781 C C . SER B 1 140 ? 36.298 86.232 75.671 1.00 9.54 ? 222 SER B C 1 ATOM 3782 O O . SER B 1 140 ? 37.039 86.182 74.692 1.00 9.54 ? 222 SER B O 1 ATOM 3783 C CB . SER B 1 140 ? 35.182 84.795 77.416 1.00 3.81 ? 222 SER B CB 1 ATOM 3784 O OG . SER B 1 140 ? 34.450 85.843 78.019 1.00 3.81 ? 222 SER B OG 1 ATOM 3785 N N . LEU B 1 141 ? 35.349 87.154 75.815 1.00 8.04 ? 223 LEU B N 1 ATOM 3786 C CA . LEU B 1 141 ? 35.017 88.105 74.756 1.00 8.04 ? 223 LEU B CA 1 ATOM 3787 C C . LEU B 1 141 ? 36.148 89.031 74.320 1.00 8.04 ? 223 LEU B C 1 ATOM 3788 O O . LEU B 1 141 ? 36.162 89.482 73.176 1.00 8.04 ? 223 LEU B O 1 ATOM 3789 C CB . LEU B 1 141 ? 33.794 88.937 75.148 1.00 9.40 ? 223 LEU B CB 1 ATOM 3790 C CG . LEU B 1 141 ? 32.491 88.189 75.443 1.00 9.40 ? 223 LEU B CG 1 ATOM 3791 C CD1 . LEU B 1 141 ? 31.417 89.185 75.841 1.00 9.40 ? 223 LEU B CD1 1 ATOM 3792 C CD2 . LEU B 1 141 ? 32.057 87.381 74.233 1.00 9.40 ? 223 LEU B CD2 1 ATOM 3793 N N . ALA B 1 142 ? 37.091 89.323 75.214 1.00 7.77 ? 224 ALA B N 1 ATOM 3794 C CA . ALA B 1 142 ? 38.207 90.199 74.854 1.00 7.77 ? 224 ALA B CA 1 ATOM 3795 C C . ALA B 1 142 ? 39.051 89.589 73.728 1.00 7.77 ? 224 ALA B C 1 ATOM 3796 O O . ALA B 1 142 ? 39.590 90.312 72.884 1.00 7.77 ? 224 ALA B O 1 ATOM 3797 C CB . ALA B 1 142 ? 39.068 90.501 76.075 1.00 2.00 ? 224 ALA B CB 1 ATOM 3798 N N . ASN B 1 143 ? 39.132 88.258 73.702 1.00 8.87 ? 225 ASN B N 1 ATOM 3799 C CA . ASN B 1 143 ? 39.892 87.542 72.673 1.00 8.87 ? 225 ASN B CA 1 ATOM 3800 C C . ASN B 1 143 ? 39.244 87.666 71.300 1.00 8.87 ? 225 ASN B C 1 ATOM 3801 O O . ASN B 1 143 ? 39.908 87.502 70.279 1.00 8.87 ? 225 ASN B O 1 ATOM 3802 C CB . ASN B 1 143 ? 40.019 86.061 73.020 1.00 13.34 ? 225 ASN B CB 1 ATOM 3803 C CG . ASN B 1 143 ? 40.867 85.822 74.238 1.00 13.34 ? 225 ASN B CG 1 ATOM 3804 O OD1 . ASN B 1 143 ? 42.087 86.004 74.208 1.00 13.34 ? 225 ASN B OD1 1 ATOM 3805 N ND2 . ASN B 1 143 ? 40.230 85.397 75.323 1.00 13.34 ? 225 ASN B ND2 1 ATOM 3806 N N . LEU B 1 144 ? 37.940 87.925 71.285 1.00 10.78 ? 226 LEU B N 1 ATOM 3807 C CA . LEU B 1 144 ? 37.201 88.075 70.042 1.00 10.78 ? 226 LEU B CA 1 ATOM 3808 C C . LEU B 1 144 ? 37.430 89.447 69.437 1.00 10.78 ? 226 LEU B C 1 ATOM 3809 O O . LEU B 1 144 ? 37.045 89.698 68.298 1.00 10.78 ? 226 LEU B O 1 ATOM 3810 C CB . LEU B 1 144 ? 35.704 87.842 70.262 1.00 11.57 ? 226 LEU B CB 1 ATOM 3811 C CG . LEU B 1 144 ? 35.293 86.497 70.863 1.00 11.57 ? 226 LEU B CG 1 ATOM 3812 C CD1 . LEU B 1 144 ? 33.781 86.363 70.801 1.00 11.57 ? 226 LEU B CD1 1 ATOM 3813 C CD2 . LEU B 1 144 ? 35.964 85.355 70.117 1.00 11.57 ? 226 LEU B CD2 1 ATOM 3814 N N . VAL B 1 145 ? 38.037 90.341 70.211 1.00 11.35 ? 227 VAL B N 1 ATOM 3815 C CA . VAL B 1 145 ? 38.333 91.686 69.734 1.00 11.35 ? 227 VAL B CA 1 ATOM 3816 C C . VAL B 1 145 ? 39.725 91.749 69.093 1.00 11.35 ? 227 VAL B C 1 ATOM 3817 O O . VAL B 1 145 ? 39.890 92.344 68.026 1.00 11.35 ? 227 VAL B O 1 ATOM 3818 C CB . VAL B 1 145 ? 38.270 92.728 70.885 1.00 8.82 ? 227 VAL B CB 1 ATOM 3819 C CG1 . VAL B 1 145 ? 38.560 94.133 70.363 1.00 8.82 ? 227 VAL B CG1 1 ATOM 3820 C CG2 . VAL B 1 145 ? 36.912 92.691 71.561 1.00 8.82 ? 227 VAL B CG2 1 ATOM 3821 N N . THR B 1 146 ? 40.708 91.086 69.705 1.00 13.16 ? 228 THR B N 1 ATOM 3822 C CA . THR B 1 146 ? 42.079 91.135 69.193 1.00 13.16 ? 228 THR B CA 1 ATOM 3823 C C . THR B 1 146 ? 42.726 89.827 68.728 1.00 13.16 ? 228 THR B C 1 ATOM 3824 O O . THR B 1 146 ? 43.663 89.852 67.921 1.00 13.16 ? 228 THR B O 1 ATOM 3825 C CB . THR B 1 146 ? 43.033 91.736 70.246 1.00 8.54 ? 228 THR B CB 1 ATOM 3826 O OG1 . THR B 1 146 ? 43.086 90.865 71.380 1.00 8.54 ? 228 THR B OG1 1 ATOM 3827 C CG2 . THR B 1 146 ? 42.559 93.113 70.697 1.00 8.54 ? 228 THR B CG2 1 ATOM 3828 N N . ASN B 1 147 ? 42.243 88.693 69.228 1.00 9.31 ? 229 ASN B N 1 ATOM 3829 C CA . ASN B 1 147 ? 42.849 87.406 68.892 1.00 9.31 ? 229 ASN B CA 1 ATOM 3830 C C . ASN B 1 147 ? 42.175 86.513 67.861 1.00 9.31 ? 229 ASN B C 1 ATOM 3831 O O . ASN B 1 147 ? 42.389 85.299 67.867 1.00 9.31 ? 229 ASN B O 1 ATOM 3832 C CB . ASN B 1 147 ? 43.110 86.604 70.174 1.00 20.35 ? 229 ASN B CB 1 ATOM 3833 C CG . ASN B 1 147 ? 43.984 87.354 71.159 1.00 20.35 ? 229 ASN B CG 1 ATOM 3834 O OD1 . ASN B 1 147 ? 44.729 88.255 70.782 1.00 20.35 ? 229 ASN B OD1 1 ATOM 3835 N ND2 . ASN B 1 147 ? 43.888 86.993 72.428 1.00 20.35 ? 229 ASN B ND2 1 ATOM 3836 N N . LEU B 1 148 ? 41.388 87.092 66.960 1.00 11.22 ? 230 LEU B N 1 ATOM 3837 C CA . LEU B 1 148 ? 40.743 86.276 65.937 1.00 11.22 ? 230 LEU B CA 1 ATOM 3838 C C . LEU B 1 148 ? 41.777 85.743 64.943 1.00 11.22 ? 230 LEU B C 1 ATOM 3839 O O . LEU B 1 148 ? 41.466 84.887 64.117 1.00 11.22 ? 230 LEU B O 1 ATOM 3840 C CB . LEU B 1 148 ? 39.637 87.046 65.218 1.00 12.51 ? 230 LEU B CB 1 ATOM 3841 C CG . LEU B 1 148 ? 38.375 87.283 66.046 1.00 12.51 ? 230 LEU B CG 1 ATOM 3842 C CD1 . LEU B 1 148 ? 37.341 87.990 65.190 1.00 12.51 ? 230 LEU B CD1 1 ATOM 3843 C CD2 . LEU B 1 148 ? 37.833 85.952 66.560 1.00 12.51 ? 230 LEU B CD2 1 ATOM 3844 N N . GLY B 1 149 ? 43.007 86.248 65.051 1.00 18.93 ? 231 GLY B N 1 ATOM 3845 C CA . GLY B 1 149 ? 44.096 85.797 64.200 1.00 18.93 ? 231 GLY B CA 1 ATOM 3846 C C . GLY B 1 149 ? 44.587 84.433 64.664 1.00 18.93 ? 231 GLY B C 1 ATOM 3847 O O . GLY B 1 149 ? 45.313 83.747 63.944 1.00 18.93 ? 231 GLY B O 1 ATOM 3848 N N . THR B 1 150 ? 44.225 84.065 65.893 1.00 10.66 ? 232 THR B N 1 ATOM 3849 C CA . THR B 1 150 ? 44.581 82.771 66.471 1.00 10.66 ? 232 THR B CA 1 ATOM 3850 C C . THR B 1 150 ? 43.430 81.840 66.102 1.00 10.66 ? 232 THR B C 1 ATOM 3851 O O . THR B 1 150 ? 42.278 82.102 66.447 1.00 10.66 ? 232 THR B O 1 ATOM 3852 C CB . THR B 1 150 ? 44.694 82.855 68.012 1.00 12.83 ? 232 THR B CB 1 ATOM 3853 O OG1 . THR B 1 150 ? 45.750 83.756 68.368 1.00 12.83 ? 232 THR B OG1 1 ATOM 3854 C CG2 . THR B 1 150 ? 44.977 81.484 68.613 1.00 12.83 ? 232 THR B CG2 1 ATOM 3855 N N . PRO B 1 151 ? 43.731 80.745 65.382 1.00 14.35 ? 233 PRO B N 1 ATOM 3856 C CA . PRO B 1 151 ? 42.754 79.745 64.931 1.00 14.35 ? 233 PRO B CA 1 ATOM 3857 C C . PRO B 1 151 ? 41.819 79.215 66.009 1.00 14.35 ? 233 PRO B C 1 ATOM 3858 O O . PRO B 1 151 ? 40.620 79.077 65.771 1.00 14.35 ? 233 PRO B O 1 ATOM 3859 C CB . PRO B 1 151 ? 43.636 78.636 64.369 1.00 20.29 ? 233 PRO B CB 1 ATOM 3860 C CG . PRO B 1 151 ? 44.808 79.382 63.844 1.00 20.29 ? 233 PRO B CG 1 ATOM 3861 C CD . PRO B 1 151 ? 45.087 80.383 64.938 1.00 20.29 ? 233 PRO B CD 1 ATOM 3862 N N . LYS B 1 152 ? 42.357 78.918 67.186 1.00 12.51 ? 234 LYS B N 1 ATOM 3863 C CA . LYS B 1 152 ? 41.521 78.401 68.262 1.00 12.51 ? 234 LYS B CA 1 ATOM 3864 C C . LYS B 1 152 ? 40.442 79.399 68.668 1.00 12.51 ? 234 LYS B C 1 ATOM 3865 O O . LYS B 1 152 ? 39.325 78.999 68.972 1.00 12.51 ? 234 LYS B O 1 ATOM 3866 C CB . LYS B 1 152 ? 42.353 77.992 69.476 1.00 22.81 ? 234 LYS B CB 1 ATOM 3867 C CG . LYS B 1 152 ? 41.530 77.266 70.522 1.00 22.81 ? 234 LYS B CG 1 ATOM 3868 C CD . LYS B 1 152 ? 42.385 76.733 71.637 1.00 22.81 ? 234 LYS B CD 1 ATOM 3869 C CE . LYS B 1 152 ? 41.535 75.973 72.630 1.00 22.81 ? 234 LYS B CE 1 ATOM 3870 N NZ . LYS B 1 152 ? 42.372 75.349 73.684 1.00 22.81 ? 234 LYS B NZ 1 ATOM 3871 N N . CYS B 1 153 ? 40.778 80.690 68.669 1.00 11.05 ? 235 CYS B N 1 ATOM 3872 C CA . CYS B 1 153 ? 39.810 81.732 69.018 1.00 11.05 ? 235 CYS B CA 1 ATOM 3873 C C . CYS B 1 153 ? 38.778 81.921 67.909 1.00 11.05 ? 235 CYS B C 1 ATOM 3874 O O . CYS B 1 153 ? 37.583 82.062 68.179 1.00 11.05 ? 235 CYS B O 1 ATOM 3875 C CB . CYS B 1 153 ? 40.510 83.064 69.295 1.00 9.79 ? 235 CYS B CB 1 ATOM 3876 S SG . CYS B 1 153 ? 41.475 83.085 70.835 1.00 9.79 ? 235 CYS B SG 1 ATOM 3877 N N . ALA B 1 154 ? 39.244 81.930 66.663 1.00 10.67 ? 236 ALA B N 1 ATOM 3878 C CA . ALA B 1 154 ? 38.353 82.098 65.521 1.00 10.67 ? 236 ALA B CA 1 ATOM 3879 C C . ALA B 1 154 ? 37.300 80.990 65.499 1.00 10.67 ? 236 ALA B C 1 ATOM 3880 O O . ALA B 1 154 ? 36.117 81.248 65.281 1.00 10.67 ? 236 ALA B O 1 ATOM 3881 C CB . ALA B 1 154 ? 39.150 82.088 64.220 1.00 7.14 ? 236 ALA B CB 1 ATOM 3882 N N . ASN B 1 155 ? 37.733 79.764 65.776 1.00 15.18 ? 237 ASN B N 1 ATOM 3883 C CA . ASN B 1 155 ? 36.831 78.616 65.778 1.00 15.18 ? 237 ASN B CA 1 ATOM 3884 C C . ASN B 1 155 ? 35.914 78.538 66.998 1.00 15.18 ? 237 ASN B C 1 ATOM 3885 O O . ASN B 1 155 ? 34.882 77.873 66.955 1.00 15.18 ? 237 ASN B O 1 ATOM 3886 C CB . ASN B 1 155 ? 37.631 77.319 65.621 1.00 46.90 ? 237 ASN B CB 1 ATOM 3887 C CG . ASN B 1 155 ? 38.347 77.234 64.280 1.00 46.90 ? 237 ASN B CG 1 ATOM 3888 O OD1 . ASN B 1 155 ? 37.906 77.818 63.286 1.00 46.90 ? 237 ASN B OD1 1 ATOM 3889 N ND2 . ASN B 1 155 ? 39.461 76.517 64.251 1.00 46.90 ? 237 ASN B ND2 1 ATOM 3890 N N . ALA B 1 156 ? 36.277 79.250 68.062 1.00 15.88 ? 238 ALA B N 1 ATOM 3891 C CA . ALA B 1 156 ? 35.501 79.266 69.300 1.00 15.88 ? 238 ALA B CA 1 ATOM 3892 C C . ALA B 1 156 ? 34.534 80.448 69.402 1.00 15.88 ? 238 ALA B C 1 ATOM 3893 O O . ALA B 1 156 ? 33.772 80.546 70.360 1.00 15.88 ? 238 ALA B O 1 ATOM 3894 C CB . ALA B 1 156 ? 36.445 79.272 70.489 1.00 2.00 ? 238 ALA B CB 1 ATOM 3895 N N . GLN B 1 157 ? 34.555 81.326 68.405 1.00 8.98 ? 239 GLN B N 1 ATOM 3896 C CA . GLN B 1 157 ? 33.711 82.517 68.392 1.00 8.98 ? 239 GLN B CA 1 ATOM 3897 C C . GLN B 1 157 ? 32.213 82.270 68.571 1.00 8.98 ? 239 GLN B C 1 ATOM 3898 O O . GLN B 1 157 ? 31.575 82.857 69.457 1.00 8.98 ? 239 GLN B O 1 ATOM 3899 C CB . GLN B 1 157 ? 33.974 83.309 67.114 1.00 22.19 ? 239 GLN B CB 1 ATOM 3900 C CG . GLN B 1 157 ? 33.156 84.574 66.981 1.00 22.19 ? 239 GLN B CG 1 ATOM 3901 C CD . GLN B 1 157 ? 33.660 85.474 65.874 1.00 22.19 ? 239 GLN B CD 1 ATOM 3902 O OE1 . GLN B 1 157 ? 33.576 86.700 65.978 1.00 22.19 ? 239 GLN B OE1 1 ATOM 3903 N NE2 . GLN B 1 157 ? 34.204 84.875 64.813 1.00 22.19 ? 239 GLN B NE2 1 ATOM 3904 N N . SER B 1 158 ? 31.661 81.396 67.736 1.00 7.47 ? 240 SER B N 1 ATOM 3905 C CA . SER B 1 158 ? 30.240 81.074 67.795 1.00 7.47 ? 240 SER B CA 1 ATOM 3906 C C . SER B 1 158 ? 29.839 80.430 69.115 1.00 7.47 ? 240 SER B C 1 ATOM 3907 O O . SER B 1 158 ? 28.774 80.724 69.655 1.00 7.47 ? 240 SER B O 1 ATOM 3908 C CB . SER B 1 158 ? 29.859 80.154 66.638 1.00 30.96 ? 240 SER B CB 1 ATOM 3909 O OG . SER B 1 158 ? 30.065 80.804 65.399 1.00 30.96 ? 240 SER B OG 1 ATOM 3910 N N . ALA B 1 159 ? 30.689 79.541 69.622 1.00 8.69 ? 241 ALA B N 1 ATOM 3911 C CA . ALA B 1 159 ? 30.421 78.863 70.885 1.00 8.69 ? 241 ALA B CA 1 ATOM 3912 C C . ALA B 1 159 ? 30.463 79.861 72.034 1.00 8.69 ? 241 ALA B C 1 ATOM 3913 O O . ALA B 1 159 ? 29.574 79.860 72.881 1.00 8.69 ? 241 ALA B O 1 ATOM 3914 C CB . ALA B 1 159 ? 31.417 77.750 71.111 1.00 6.87 ? 241 ALA B CB 1 ATOM 3915 N N . TYR B 1 160 ? 31.480 80.725 72.045 1.00 8.54 ? 242 TYR B N 1 ATOM 3916 C CA . TYR B 1 160 ? 31.609 81.739 73.090 1.00 8.54 ? 242 TYR B CA 1 ATOM 3917 C C . TYR B 1 160 ? 30.356 82.605 73.168 1.00 8.54 ? 242 TYR B C 1 ATOM 3918 O O . TYR B 1 160 ? 29.782 82.783 74.243 1.00 8.54 ? 242 TYR B O 1 ATOM 3919 C CB . TYR B 1 160 ? 32.820 82.645 72.843 1.00 5.88 ? 242 TYR B CB 1 ATOM 3920 C CG . TYR B 1 160 ? 34.162 82.125 73.343 1.00 5.88 ? 242 TYR B CG 1 ATOM 3921 C CD1 . TYR B 1 160 ? 34.363 80.774 73.636 1.00 5.88 ? 242 TYR B CD1 1 ATOM 3922 C CD2 . TYR B 1 160 ? 35.246 82.995 73.485 1.00 5.88 ? 242 TYR B CD2 1 ATOM 3923 C CE1 . TYR B 1 160 ? 35.614 80.306 74.051 1.00 5.88 ? 242 TYR B CE1 1 ATOM 3924 C CE2 . TYR B 1 160 ? 36.496 82.538 73.898 1.00 5.88 ? 242 TYR B CE2 1 ATOM 3925 C CZ . TYR B 1 160 ? 36.674 81.198 74.178 1.00 5.88 ? 242 TYR B CZ 1 ATOM 3926 O OH . TYR B 1 160 ? 37.924 80.761 74.560 1.00 5.88 ? 242 TYR B OH 1 ATOM 3927 N N . LEU B 1 161 ? 29.922 83.128 72.024 1.00 7.74 ? 243 LEU B N 1 ATOM 3928 C CA . LEU B 1 161 ? 28.736 83.985 71.974 1.00 7.74 ? 243 LEU B CA 1 ATOM 3929 C C . LEU B 1 161 ? 27.448 83.267 72.358 1.00 7.74 ? 243 LEU B C 1 ATOM 3930 O O . LEU B 1 161 ? 26.585 83.850 73.013 1.00 7.74 ? 243 LEU B O 1 ATOM 3931 C CB . LEU B 1 161 ? 28.597 84.632 70.594 1.00 12.69 ? 243 LEU B CB 1 ATOM 3932 C CG . LEU B 1 161 ? 29.707 85.626 70.237 1.00 12.69 ? 243 LEU B CG 1 ATOM 3933 C CD1 . LEU B 1 161 ? 29.582 86.035 68.780 1.00 12.69 ? 243 LEU B CD1 1 ATOM 3934 C CD2 . LEU B 1 161 ? 29.642 86.844 71.143 1.00 12.69 ? 243 LEU B CD2 1 ATOM 3935 N N . GLU B 1 162 ? 27.328 81.998 71.975 1.00 8.83 ? 244 GLU B N 1 ATOM 3936 C CA . GLU B 1 162 ? 26.136 81.227 72.308 1.00 8.83 ? 244 GLU B CA 1 ATOM 3937 C C . GLU B 1 162 ? 26.066 80.948 73.806 1.00 8.83 ? 244 GLU B C 1 ATOM 3938 O O . GLU B 1 162 ? 25.015 81.106 74.434 1.00 8.83 ? 244 GLU B O 1 ATOM 3939 C CB . GLU B 1 162 ? 26.100 79.903 71.546 1.00 30.23 ? 244 GLU B CB 1 ATOM 3940 C CG . GLU B 1 162 ? 24.845 79.102 71.856 1.00 30.23 ? 244 GLU B CG 1 ATOM 3941 C CD . GLU B 1 162 ? 24.725 77.808 71.076 1.00 30.23 ? 244 GLU B CD 1 ATOM 3942 O OE1 . GLU B 1 162 ? 25.557 77.545 70.176 1.00 30.23 ? 244 GLU B OE1 1 ATOM 3943 O OE2 . GLU B 1 162 ? 23.775 77.049 71.369 1.00 30.23 ? 244 GLU B OE2 1 ATOM 3944 N N . CYS B 1 163 ? 27.200 80.542 74.365 1.00 5.48 ? 245 CYS B N 1 ATOM 3945 C CA . CYS B 1 163 ? 27.302 80.225 75.780 1.00 5.48 ? 245 CYS B CA 1 ATOM 3946 C C . CYS B 1 163 ? 27.116 81.441 76.683 1.00 5.48 ? 245 CYS B C 1 ATOM 3947 O O . CYS B 1 163 ? 26.457 81.341 77.715 1.00 5.48 ? 245 CYS B O 1 ATOM 3948 C CB . CYS B 1 163 ? 28.640 79.547 76.069 1.00 10.63 ? 245 CYS B CB 1 ATOM 3949 S SG . CYS B 1 163 ? 28.761 77.857 75.446 1.00 10.63 ? 245 CYS B SG 1 ATOM 3950 N N . ILE B 1 164 ? 27.686 82.581 76.298 1.00 5.70 ? 246 ILE B N 1 ATOM 3951 C CA . ILE B 1 164 ? 27.554 83.812 77.083 1.00 5.70 ? 246 ILE B CA 1 ATOM 3952 C C . ILE B 1 164 ? 26.098 84.278 77.070 1.00 5.70 ? 246 ILE B C 1 ATOM 3953 O O . ILE B 1 164 ? 25.595 84.801 78.065 1.00 5.70 ? 246 ILE B O 1 ATOM 3954 C CB . ILE B 1 164 ? 28.459 84.954 76.537 1.00 10.93 ? 246 ILE B CB 1 ATOM 3955 C CG1 . ILE B 1 164 ? 29.939 84.599 76.710 1.00 10.93 ? 246 ILE B CG1 1 ATOM 3956 C CG2 . ILE B 1 164 ? 28.158 86.270 77.259 1.00 10.93 ? 246 ILE B CG2 1 ATOM 3957 C CD1 . ILE B 1 164 ? 30.357 84.485 78.134 1.00 10.93 ? 246 ILE B CD1 1 ATOM 3958 N N . ASN B 1 165 ? 25.433 84.120 75.930 1.00 5.39 ? 247 ASN B N 1 ATOM 3959 C CA . ASN B 1 165 ? 24.030 84.502 75.817 1.00 5.39 ? 247 ASN B CA 1 ATOM 3960 C C . ASN B 1 165 ? 23.207 83.645 76.784 1.00 5.39 ? 247 ASN B C 1 ATOM 3961 O O . ASN B 1 165 ? 22.328 84.151 77.482 1.00 5.39 ? 247 ASN B O 1 ATOM 3962 C CB . ASN B 1 165 ? 23.536 84.303 74.379 1.00 11.42 ? 247 ASN B CB 1 ATOM 3963 C CG . ASN B 1 165 ? 22.050 84.580 74.228 1.00 11.42 ? 247 ASN B CG 1 ATOM 3964 O OD1 . ASN B 1 165 ? 21.233 83.672 74.319 1.00 11.42 ? 247 ASN B OD1 1 ATOM 3965 N ND2 . ASN B 1 165 ? 21.695 85.838 74.016 1.00 11.42 ? 247 ASN B ND2 1 ATOM 3966 N N . TYR B 1 166 ? 23.526 82.354 76.852 1.00 8.57 ? 248 TYR B N 1 ATOM 3967 C CA . TYR B 1 166 ? 22.817 81.439 77.736 1.00 8.57 ? 248 TYR B CA 1 ATOM 3968 C C . TYR B 1 166 ? 23.030 81.820 79.197 1.00 8.57 ? 248 TYR B C 1 ATOM 3969 O O . TYR B 1 166 ? 22.075 81.905 79.961 1.00 8.57 ? 248 TYR B O 1 ATOM 3970 C CB . TYR B 1 166 ? 23.282 79.997 77.504 1.00 5.65 ? 248 TYR B CB 1 ATOM 3971 C CG . TYR B 1 166 ? 22.367 78.957 78.120 1.00 5.65 ? 248 TYR B CG 1 ATOM 3972 C CD1 . TYR B 1 166 ? 21.166 78.607 77.507 1.00 5.65 ? 248 TYR B CD1 1 ATOM 3973 C CD2 . TYR B 1 166 ? 22.701 78.328 79.318 1.00 5.65 ? 248 TYR B CD2 1 ATOM 3974 C CE1 . TYR B 1 166 ? 20.322 77.651 78.071 1.00 5.65 ? 248 TYR B CE1 1 ATOM 3975 C CE2 . TYR B 1 166 ? 21.868 77.376 79.888 1.00 5.65 ? 248 TYR B CE2 1 ATOM 3976 C CZ . TYR B 1 166 ? 20.681 77.042 79.263 1.00 5.65 ? 248 TYR B CZ 1 ATOM 3977 O OH . TYR B 1 166 ? 19.846 76.108 79.826 1.00 5.65 ? 248 TYR B OH 1 ATOM 3978 N N . ALA B 1 167 ? 24.284 82.059 79.570 1.00 5.45 ? 249 ALA B N 1 ATOM 3979 C CA . ALA B 1 167 ? 24.640 82.427 80.939 1.00 5.45 ? 249 ALA B CA 1 ATOM 3980 C C . ALA B 1 167 ? 23.911 83.683 81.407 1.00 5.45 ? 249 ALA B C 1 ATOM 3981 O O . ALA B 1 167 ? 23.290 83.692 82.465 1.00 5.45 ? 249 ALA B O 1 ATOM 3982 C CB . ALA B 1 167 ? 26.153 82.633 81.051 1.00 6.14 ? 249 ALA B CB 1 ATOM 3983 N N . VAL B 1 168 ? 23.986 84.731 80.593 1.00 7.25 ? 250 VAL B N 1 ATOM 3984 C CA . VAL B 1 168 ? 23.364 86.019 80.882 1.00 7.25 ? 250 VAL B CA 1 ATOM 3985 C C . VAL B 1 168 ? 21.825 85.972 80.935 1.00 7.25 ? 250 VAL B C 1 ATOM 3986 O O . VAL B 1 168 ? 21.206 86.664 81.740 1.00 7.25 ? 250 VAL B O 1 ATOM 3987 C CB . VAL B 1 168 ? 23.871 87.084 79.864 1.00 12.96 ? 250 VAL B CB 1 ATOM 3988 C CG1 . VAL B 1 168 ? 23.045 88.349 79.926 1.00 12.96 ? 250 VAL B CG1 1 ATOM 3989 C CG2 . VAL B 1 168 ? 25.327 87.412 80.153 1.00 12.96 ? 250 VAL B CG2 1 ATOM 3990 N N . THR B 1 169 ? 21.203 85.158 80.093 1.00 10.34 ? 251 THR B N 1 ATOM 3991 C CA . THR B 1 169 ? 19.749 85.067 80.118 1.00 10.34 ? 251 THR B CA 1 ATOM 3992 C C . THR B 1 169 ? 19.257 84.155 81.252 1.00 10.34 ? 251 THR B C 1 ATOM 3993 O O . THR B 1 169 ? 18.296 84.488 81.941 1.00 10.34 ? 251 THR B O 1 ATOM 3994 C CB . THR B 1 169 ? 19.165 84.604 78.747 1.00 11.90 ? 251 THR B CB 1 ATOM 3995 O OG1 . THR B 1 169 ? 19.769 83.371 78.345 1.00 11.90 ? 251 THR B OG1 1 ATOM 3996 C CG2 . THR B 1 169 ? 19.433 85.640 77.679 1.00 11.90 ? 251 THR B CG2 1 ATOM 3997 N N . GLN B 1 170 ? 19.953 83.044 81.487 1.00 8.71 ? 252 GLN B N 1 ATOM 3998 C CA . GLN B 1 170 ? 19.563 82.099 82.535 1.00 8.71 ? 252 GLN B CA 1 ATOM 3999 C C . GLN B 1 170 ? 19.859 82.565 83.957 1.00 8.71 ? 252 GLN B C 1 ATOM 4000 O O . GLN B 1 170 ? 19.238 82.091 84.910 1.00 8.71 ? 252 GLN B O 1 ATOM 4001 C CB . GLN B 1 170 ? 20.203 80.730 82.296 1.00 15.01 ? 252 GLN B CB 1 ATOM 4002 C CG . GLN B 1 170 ? 19.747 80.045 81.016 1.00 15.01 ? 252 GLN B CG 1 ATOM 4003 C CD . GLN B 1 170 ? 18.260 79.755 81.000 1.00 15.01 ? 252 GLN B CD 1 ATOM 4004 O OE1 . GLN B 1 170 ? 17.684 79.347 82.008 1.00 15.01 ? 252 GLN B OE1 1 ATOM 4005 N NE2 . GLN B 1 170 ? 17.631 79.958 79.849 1.00 15.01 ? 252 GLN B NE2 1 ATOM 4006 N N . LEU B 1 171 ? 20.832 83.457 84.108 1.00 6.45 ? 253 LEU B N 1 ATOM 4007 C CA . LEU B 1 171 ? 21.173 83.975 85.424 1.00 6.45 ? 253 LEU B CA 1 ATOM 4008 C C . LEU B 1 171 ? 20.547 85.349 85.647 1.00 6.45 ? 253 LEU B C 1 ATOM 4009 O O . LEU B 1 171 ? 20.870 86.037 86.612 1.00 6.45 ? 253 LEU B O 1 ATOM 4010 C CB . LEU B 1 171 ? 22.694 84.019 85.614 1.00 8.43 ? 253 LEU B CB 1 ATOM 4011 C CG . LEU B 1 171 ? 23.383 82.657 85.501 1.00 8.43 ? 253 LEU B CG 1 ATOM 4012 C CD1 . LEU B 1 171 ? 24.882 82.789 85.735 1.00 8.43 ? 253 LEU B CD1 1 ATOM 4013 C CD2 . LEU B 1 171 ? 22.776 81.675 86.495 1.00 8.43 ? 253 LEU B CD2 1 ATOM 4014 N N . ASN B 1 172 ? 19.645 85.742 84.750 1.00 10.97 ? 254 ASN B N 1 ATOM 4015 C CA . ASN B 1 172 ? 18.958 87.029 84.859 1.00 10.97 ? 254 ASN B CA 1 ATOM 4016 C C . ASN B 1 172 ? 17.839 86.891 85.901 1.00 10.97 ? 254 ASN B C 1 ATOM 4017 O O . ASN B 1 172 ? 16.677 86.641 85.561 1.00 10.97 ? 254 ASN B O 1 ATOM 4018 C CB . ASN B 1 172 ? 18.394 87.436 83.489 1.00 5.19 ? 254 ASN B CB 1 ATOM 4019 C CG . ASN B 1 172 ? 17.695 88.786 83.512 1.00 5.19 ? 254 ASN B CG 1 ATOM 4020 O OD1 . ASN B 1 172 ? 17.970 89.630 84.359 1.00 5.19 ? 254 ASN B OD1 1 ATOM 4021 N ND2 . ASN B 1 172 ? 16.795 88.995 82.564 1.00 5.19 ? 254 ASN B ND2 1 ATOM 4022 N N . LEU B 1 173 ? 18.223 87.013 87.174 1.00 9.65 ? 255 LEU B N 1 ATOM 4023 C CA . LEU B 1 173 ? 17.307 86.897 88.308 1.00 9.65 ? 255 LEU B CA 1 ATOM 4024 C C . LEU B 1 173 ? 17.340 88.174 89.161 1.00 9.65 ? 255 LEU B C 1 ATOM 4025 O O . LEU B 1 173 ? 18.328 88.910 89.147 1.00 9.65 ? 255 LEU B O 1 ATOM 4026 C CB . LEU B 1 173 ? 17.683 85.659 89.138 1.00 11.07 ? 255 LEU B CB 1 ATOM 4027 C CG . LEU B 1 173 ? 17.518 84.321 88.401 1.00 11.07 ? 255 LEU B CG 1 ATOM 4028 C CD1 . LEU B 1 173 ? 18.296 83.209 89.067 1.00 11.07 ? 255 LEU B CD1 1 ATOM 4029 C CD2 . LEU B 1 173 ? 16.049 83.962 88.313 1.00 11.07 ? 255 LEU B CD2 1 ATOM 4030 N N . PRO B 1 174 ? 16.260 88.448 89.922 1.00 9.51 ? 256 PRO B N 1 ATOM 4031 C CA . PRO B 1 174 ? 16.121 89.626 90.788 1.00 9.51 ? 256 PRO B CA 1 ATOM 4032 C C . PRO B 1 174 ? 17.217 89.850 91.826 1.00 9.51 ? 256 PRO B C 1 ATOM 4033 O O . PRO B 1 174 ? 17.559 90.992 92.125 1.00 9.51 ? 256 PRO B O 1 ATOM 4034 C CB . PRO B 1 174 ? 14.768 89.401 91.471 1.00 19.63 ? 256 PRO B CB 1 ATOM 4035 C CG . PRO B 1 174 ? 14.015 88.595 90.500 1.00 19.63 ? 256 PRO B CG 1 ATOM 4036 C CD . PRO B 1 174 ? 15.041 87.620 89.982 1.00 19.63 ? 256 PRO B CD 1 ATOM 4037 N N . ASN B 1 175 ? 17.738 88.767 92.394 1.00 9.15 ? 257 ASN B N 1 ATOM 4038 C CA . ASN B 1 175 ? 18.787 88.862 93.416 1.00 9.15 ? 257 ASN B CA 1 ATOM 4039 C C . ASN B 1 175 ? 20.206 88.833 92.843 1.00 9.15 ? 257 ASN B C 1 ATOM 4040 O O . ASN B 1 175 ? 21.180 88.837 93.593 1.00 9.15 ? 257 ASN B O 1 ATOM 4041 C CB . ASN B 1 175 ? 18.625 87.734 94.449 1.00 8.27 ? 257 ASN B CB 1 ATOM 4042 C CG . ASN B 1 175 ? 18.791 86.349 93.839 1.00 8.27 ? 257 ASN B CG 1 ATOM 4043 O OD1 . ASN B 1 175 ? 18.290 86.070 92.746 1.00 8.27 ? 257 ASN B OD1 1 ATOM 4044 N ND2 . ASN B 1 175 ? 19.499 85.476 94.542 1.00 8.27 ? 257 ASN B ND2 1 ATOM 4045 N N . VAL B 1 176 ? 20.312 88.839 91.517 1.00 7.73 ? 258 VAL B N 1 ATOM 4046 C CA . VAL B 1 176 ? 21.601 88.772 90.835 1.00 7.73 ? 258 VAL B CA 1 ATOM 4047 C C . VAL B 1 176 ? 22.067 90.084 90.203 1.00 7.73 ? 258 VAL B C 1 ATOM 4048 O O . VAL B 1 176 ? 21.262 90.911 89.767 1.00 7.73 ? 258 VAL B O 1 ATOM 4049 C CB . VAL B 1 176 ? 21.567 87.676 89.734 1.00 5.79 ? 258 VAL B CB 1 ATOM 4050 C CG1 . VAL B 1 176 ? 22.842 87.690 88.892 1.00 5.79 ? 258 VAL B CG1 1 ATOM 4051 C CG2 . VAL B 1 176 ? 21.374 86.313 90.366 1.00 5.79 ? 258 VAL B CG2 1 ATOM 4052 N N . ALA B 1 177 ? 23.383 90.275 90.198 1.00 8.85 ? 259 ALA B N 1 ATOM 4053 C CA . ALA B 1 177 ? 24.012 91.432 89.575 1.00 8.85 ? 259 ALA B CA 1 ATOM 4054 C C . ALA B 1 177 ? 25.201 90.845 88.826 1.00 8.85 ? 259 ALA B C 1 ATOM 4055 O O . ALA B 1 177 ? 26.090 90.264 89.441 1.00 8.85 ? 259 ALA B O 1 ATOM 4056 C CB . ALA B 1 177 ? 24.482 92.420 90.614 1.00 10.43 ? 259 ALA B CB 1 ATOM 4057 N N . MET B 1 178 ? 25.171 90.932 87.498 1.00 5.01 ? 260 MET B N 1 ATOM 4058 C CA . MET B 1 178 ? 26.239 90.407 86.658 1.00 5.01 ? 260 MET B CA 1 ATOM 4059 C C . MET B 1 178 ? 27.086 91.505 86.042 1.00 5.01 ? 260 MET B C 1 ATOM 4060 O O . MET B 1 178 ? 26.598 92.594 85.734 1.00 5.01 ? 260 MET B O 1 ATOM 4061 C CB . MET B 1 178 ? 25.673 89.562 85.511 1.00 9.66 ? 260 MET B CB 1 ATOM 4062 C CG . MET B 1 178 ? 25.084 88.225 85.900 1.00 9.66 ? 260 MET B CG 1 ATOM 4063 S SD . MET B 1 178 ? 24.390 87.378 84.456 1.00 9.66 ? 260 MET B SD 1 ATOM 4064 C CE . MET B 1 178 ? 22.856 88.259 84.241 1.00 9.66 ? 260 MET B CE 1 ATOM 4065 N N . TYR B 1 179 ? 28.364 91.202 85.855 1.00 6.03 ? 261 TYR B N 1 ATOM 4066 C CA . TYR B 1 179 ? 29.297 92.123 85.228 1.00 6.03 ? 261 TYR B CA 1 ATOM 4067 C C . TYR B 1 179 ? 30.116 91.314 84.235 1.00 6.03 ? 261 TYR B C 1 ATOM 4068 O O . TYR B 1 179 ? 30.797 90.363 84.615 1.00 6.03 ? 261 TYR B O 1 ATOM 4069 C CB . TYR B 1 179 ? 30.231 92.756 86.256 1.00 2.00 ? 261 TYR B CB 1 ATOM 4070 C CG . TYR B 1 179 ? 29.569 93.723 87.211 1.00 2.00 ? 261 TYR B CG 1 ATOM 4071 C CD1 . TYR B 1 179 ? 29.002 93.275 88.402 1.00 2.00 ? 261 TYR B CD1 1 ATOM 4072 C CD2 . TYR B 1 179 ? 29.559 95.095 86.950 1.00 2.00 ? 261 TYR B CD2 1 ATOM 4073 C CE1 . TYR B 1 179 ? 28.444 94.173 89.317 1.00 2.00 ? 261 TYR B CE1 1 ATOM 4074 C CE2 . TYR B 1 179 ? 29.006 95.998 87.855 1.00 2.00 ? 261 TYR B CE2 1 ATOM 4075 C CZ . TYR B 1 179 ? 28.454 95.531 89.038 1.00 2.00 ? 261 TYR B CZ 1 ATOM 4076 O OH . TYR B 1 179 ? 27.934 96.417 89.958 1.00 2.00 ? 261 TYR B OH 1 ATOM 4077 N N . LEU B 1 180 ? 29.987 91.644 82.955 1.00 5.69 ? 262 LEU B N 1 ATOM 4078 C CA . LEU B 1 180 ? 30.731 90.966 81.896 1.00 5.69 ? 262 LEU B CA 1 ATOM 4079 C C . LEU B 1 180 ? 32.192 91.384 81.937 1.00 5.69 ? 262 LEU B C 1 ATOM 4080 O O . LEU B 1 180 ? 32.487 92.572 82.050 1.00 5.69 ? 262 LEU B O 1 ATOM 4081 C CB . LEU B 1 180 ? 30.179 91.363 80.525 1.00 18.07 ? 262 LEU B CB 1 ATOM 4082 C CG . LEU B 1 180 ? 29.192 90.475 79.775 1.00 18.07 ? 262 LEU B CG 1 ATOM 4083 C CD1 . LEU B 1 180 ? 28.835 91.176 78.478 1.00 18.07 ? 262 LEU B CD1 1 ATOM 4084 C CD2 . LEU B 1 180 ? 29.802 89.105 79.494 1.00 18.07 ? 262 LEU B CD2 1 ATOM 4085 N N . ASP B 1 181 ? 33.102 90.423 81.809 1.00 4.55 ? 263 ASP B N 1 ATOM 4086 C CA . ASP B 1 181 ? 34.523 90.740 81.806 1.00 4.55 ? 263 ASP B CA 1 ATOM 4087 C C . ASP B 1 181 ? 34.852 91.537 80.540 1.00 4.55 ? 263 ASP B C 1 ATOM 4088 O O . ASP B 1 181 ? 34.433 91.170 79.442 1.00 4.55 ? 263 ASP B O 1 ATOM 4089 C CB . ASP B 1 181 ? 35.362 89.467 81.844 1.00 8.44 ? 263 ASP B CB 1 ATOM 4090 C CG . ASP B 1 181 ? 36.849 89.762 81.870 1.00 8.44 ? 263 ASP B CG 1 ATOM 4091 O OD1 . ASP B 1 181 ? 37.398 89.922 82.975 1.00 8.44 ? 263 ASP B OD1 1 ATOM 4092 O OD2 . ASP B 1 181 ? 37.463 89.856 80.787 1.00 8.44 ? 263 ASP B OD2 1 ATOM 4093 N N . ALA B 1 182 ? 35.625 92.609 80.703 1.00 7.59 ? 264 ALA B N 1 ATOM 4094 C CA . ALA B 1 182 ? 35.995 93.461 79.581 1.00 7.59 ? 264 ALA B CA 1 ATOM 4095 C C . ALA B 1 182 ? 37.496 93.758 79.518 1.00 7.59 ? 264 ALA B C 1 ATOM 4096 O O . ALA B 1 182 ? 37.894 94.869 79.196 1.00 7.59 ? 264 ALA B O 1 ATOM 4097 C CB . ALA B 1 182 ? 35.196 94.758 79.641 1.00 7.78 ? 264 ALA B CB 1 ATOM 4098 N N . GLY B 1 183 ? 38.324 92.762 79.825 1.00 4.08 ? 265 GLY B N 1 ATOM 4099 C CA . GLY B 1 183 ? 39.766 92.942 79.781 1.00 4.08 ? 265 GLY B CA 1 ATOM 4100 C C . GLY B 1 183 ? 40.265 94.074 80.661 1.00 4.08 ? 265 GLY B C 1 ATOM 4101 O O . GLY B 1 183 ? 39.770 94.267 81.771 1.00 4.08 ? 265 GLY B O 1 ATOM 4102 N N . HIS B 1 184 ? 41.235 94.833 80.160 1.00 4.04 ? 266 HIS B N 1 ATOM 4103 C CA . HIS B 1 184 ? 41.800 95.952 80.908 1.00 4.04 ? 266 HIS B CA 1 ATOM 4104 C C . HIS B 1 184 ? 42.380 97.009 79.970 1.00 4.04 ? 266 HIS B C 1 ATOM 4105 O O . HIS B 1 184 ? 42.408 96.817 78.753 1.00 4.04 ? 266 HIS B O 1 ATOM 4106 C CB . HIS B 1 184 ? 42.869 95.461 81.898 1.00 5.77 ? 266 HIS B CB 1 ATOM 4107 C CG . HIS B 1 184 ? 43.982 94.688 81.261 1.00 5.77 ? 266 HIS B CG 1 ATOM 4108 N ND1 . HIS B 1 184 ? 45.147 95.279 80.822 1.00 5.77 ? 266 HIS B ND1 1 ATOM 4109 C CD2 . HIS B 1 184 ? 44.100 93.370 80.972 1.00 5.77 ? 266 HIS B CD2 1 ATOM 4110 C CE1 . HIS B 1 184 ? 45.934 94.362 80.289 1.00 5.77 ? 266 HIS B CE1 1 ATOM 4111 N NE2 . HIS B 1 184 ? 45.320 93.196 80.367 1.00 5.77 ? 266 HIS B NE2 1 ATOM 4112 N N . ALA B 1 185 ? 42.865 98.105 80.548 1.00 5.64 ? 267 ALA B N 1 ATOM 4113 C CA . ALA B 1 185 ? 43.438 99.220 79.792 1.00 5.64 ? 267 ALA B CA 1 ATOM 4114 C C . ALA B 1 185 ? 44.525 98.827 78.801 1.00 5.64 ? 267 ALA B C 1 ATOM 4115 O O . ALA B 1 185 ? 44.603 99.384 77.708 1.00 5.64 ? 267 ALA B O 1 ATOM 4116 C CB . ALA B 1 185 ? 43.977 100.275 80.749 1.00 4.30 ? 267 ALA B CB 1 ATOM 4117 N N . GLY B 1 186 ? 45.362 97.871 79.190 1.00 10.11 ? 268 GLY B N 1 ATOM 4118 C CA . GLY B 1 186 ? 46.450 97.440 78.327 1.00 10.11 ? 268 GLY B CA 1 ATOM 4119 C C . GLY B 1 186 ? 46.059 96.509 77.202 1.00 10.11 ? 268 GLY B C 1 ATOM 4120 O O . GLY B 1 186 ? 46.886 96.177 76.357 1.00 10.11 ? 268 GLY B O 1 ATOM 4121 N N . TRP B 1 187 ? 44.805 96.074 77.204 1.00 8.70 ? 269 TRP B N 1 ATOM 4122 C CA . TRP B 1 187 ? 44.305 95.174 76.179 1.00 8.70 ? 269 TRP B CA 1 ATOM 4123 C C . TRP B 1 187 ? 43.317 95.920 75.282 1.00 8.70 ? 269 TRP B C 1 ATOM 4124 O O . TRP B 1 187 ? 43.603 96.177 74.113 1.00 8.70 ? 269 TRP B O 1 ATOM 4125 C CB . TRP B 1 187 ? 43.626 93.962 76.838 1.00 13.19 ? 269 TRP B CB 1 ATOM 4126 C CG . TRP B 1 187 ? 43.288 92.817 75.904 1.00 13.19 ? 269 TRP B CG 1 ATOM 4127 C CD1 . TRP B 1 187 ? 43.331 92.823 74.534 1.00 13.19 ? 269 TRP B CD1 1 ATOM 4128 C CD2 . TRP B 1 187 ? 42.868 91.500 76.283 1.00 13.19 ? 269 TRP B CD2 1 ATOM 4129 N NE1 . TRP B 1 187 ? 42.964 91.594 74.044 1.00 13.19 ? 269 TRP B NE1 1 ATOM 4130 C CE2 . TRP B 1 187 ? 42.675 90.761 75.094 1.00 13.19 ? 269 TRP B CE2 1 ATOM 4131 C CE3 . TRP B 1 187 ? 42.634 90.870 77.512 1.00 13.19 ? 269 TRP B CE3 1 ATOM 4132 C CZ2 . TRP B 1 187 ? 42.263 89.420 75.096 1.00 13.19 ? 269 TRP B CZ2 1 ATOM 4133 C CZ3 . TRP B 1 187 ? 42.222 89.539 77.517 1.00 13.19 ? 269 TRP B CZ3 1 ATOM 4134 C CH2 . TRP B 1 187 ? 42.041 88.830 76.312 1.00 13.19 ? 269 TRP B CH2 1 ATOM 4135 N N . LEU B 1 188 ? 42.168 96.287 75.845 1.00 9.74 ? 270 LEU B N 1 ATOM 4136 C CA . LEU B 1 188 ? 41.124 96.978 75.092 1.00 9.74 ? 270 LEU B CA 1 ATOM 4137 C C . LEU B 1 188 ? 41.136 98.494 75.231 1.00 9.74 ? 270 LEU B C 1 ATOM 4138 O O . LEU B 1 188 ? 40.364 99.183 74.568 1.00 9.74 ? 270 LEU B O 1 ATOM 4139 C CB . LEU B 1 188 ? 39.749 96.421 75.479 1.00 5.89 ? 270 LEU B CB 1 ATOM 4140 C CG . LEU B 1 188 ? 39.614 94.899 75.346 1.00 5.89 ? 270 LEU B CG 1 ATOM 4141 C CD1 . LEU B 1 188 ? 38.223 94.464 75.738 1.00 5.89 ? 270 LEU B CD1 1 ATOM 4142 C CD2 . LEU B 1 188 ? 39.929 94.460 73.921 1.00 5.89 ? 270 LEU B CD2 1 ATOM 4143 N N . GLY B 1 189 ? 42.030 99.009 76.073 1.00 8.66 ? 271 GLY B N 1 ATOM 4144 C CA . GLY B 1 189 ? 42.128 100.444 76.277 1.00 8.66 ? 271 GLY B CA 1 ATOM 4145 C C . GLY B 1 189 ? 42.794 101.190 75.133 1.00 8.66 ? 271 GLY B C 1 ATOM 4146 O O . GLY B 1 189 ? 42.614 102.401 74.998 1.00 8.66 ? 271 GLY B O 1 ATOM 4147 N N . TRP B 1 190 ? 43.590 100.489 74.329 1.00 10.72 ? 272 TRP B N 1 ATOM 4148 C CA . TRP B 1 190 ? 44.261 101.110 73.192 1.00 10.72 ? 272 TRP B CA 1 ATOM 4149 C C . TRP B 1 190 ? 43.194 101.724 72.296 1.00 10.72 ? 272 TRP B C 1 ATOM 4150 O O . TRP B 1 190 ? 42.170 101.101 72.027 1.00 10.72 ? 272 TRP B O 1 ATOM 4151 C CB . TRP B 1 190 ? 45.066 100.073 72.405 1.00 13.00 ? 272 TRP B CB 1 ATOM 4152 C CG . TRP B 1 190 ? 46.245 99.556 73.157 1.00 13.00 ? 272 TRP B CG 1 ATOM 4153 C CD1 . TRP B 1 190 ? 46.263 98.509 74.032 1.00 13.00 ? 272 TRP B CD1 1 ATOM 4154 C CD2 . TRP B 1 190 ? 47.579 100.085 73.134 1.00 13.00 ? 272 TRP B CD2 1 ATOM 4155 N NE1 . TRP B 1 190 ? 47.522 98.358 74.560 1.00 13.00 ? 272 TRP B NE1 1 ATOM 4156 C CE2 . TRP B 1 190 ? 48.349 99.310 74.028 1.00 13.00 ? 272 TRP B CE2 1 ATOM 4157 C CE3 . TRP B 1 190 ? 48.197 101.140 72.445 1.00 13.00 ? 272 TRP B CE3 1 ATOM 4158 C CZ2 . TRP B 1 190 ? 49.709 99.558 74.255 1.00 13.00 ? 272 TRP B CZ2 1 ATOM 4159 C CZ3 . TRP B 1 190 ? 49.553 101.384 72.672 1.00 13.00 ? 272 TRP B CZ3 1 ATOM 4160 C CH2 . TRP B 1 190 ? 50.290 100.595 73.569 1.00 13.00 ? 272 TRP B CH2 1 ATOM 4161 N N . PRO B 1 191 ? 43.420 102.958 71.828 1.00 11.41 ? 273 PRO B N 1 ATOM 4162 C CA . PRO B 1 191 ? 42.482 103.678 70.963 1.00 11.41 ? 273 PRO B CA 1 ATOM 4163 C C . PRO B 1 191 ? 41.836 102.853 69.852 1.00 11.41 ? 273 PRO B C 1 ATOM 4164 O O . PRO B 1 191 ? 40.618 102.890 69.682 1.00 11.41 ? 273 PRO B O 1 ATOM 4165 C CB . PRO B 1 191 ? 43.337 104.811 70.408 1.00 14.64 ? 273 PRO B CB 1 ATOM 4166 C CG . PRO B 1 191 ? 44.225 105.135 71.572 1.00 14.64 ? 273 PRO B CG 1 ATOM 4167 C CD . PRO B 1 191 ? 44.624 103.768 72.092 1.00 14.64 ? 273 PRO B CD 1 ATOM 4168 N N . ALA B 1 192 ? 42.639 102.073 69.135 1.00 11.09 ? 274 ALA B N 1 ATOM 4169 C CA . ALA B 1 192 ? 42.136 101.254 68.029 1.00 11.09 ? 274 ALA B CA 1 ATOM 4170 C C . ALA B 1 192 ? 41.216 100.103 68.450 1.00 11.09 ? 274 ALA B C 1 ATOM 4171 O O . ALA B 1 192 ? 40.483 99.562 67.625 1.00 11.09 ? 274 ALA B O 1 ATOM 4172 C CB . ALA B 1 192 ? 43.302 100.715 67.210 1.00 15.96 ? 274 ALA B CB 1 ATOM 4173 N N . ASN B 1 193 ? 41.255 99.741 69.730 1.00 9.23 ? 275 ASN B N 1 ATOM 4174 C CA . ASN B 1 193 ? 40.442 98.645 70.256 1.00 9.23 ? 275 ASN B CA 1 ATOM 4175 C C . ASN B 1 193 ? 39.177 99.082 70.982 1.00 9.23 ? 275 ASN B C 1 ATOM 4176 O O . ASN B 1 193 ? 38.286 98.269 71.212 1.00 9.23 ? 275 ASN B O 1 ATOM 4177 C CB . ASN B 1 193 ? 41.276 97.779 71.211 1.00 11.92 ? 275 ASN B CB 1 ATOM 4178 C CG . ASN B 1 193 ? 42.385 97.024 70.506 1.00 11.92 ? 275 ASN B CG 1 ATOM 4179 O OD1 . ASN B 1 193 ? 42.327 96.794 69.299 1.00 11.92 ? 275 ASN B OD1 1 ATOM 4180 N ND2 . ASN B 1 193 ? 43.404 96.628 71.262 1.00 11.92 ? 275 ASN B ND2 1 ATOM 4181 N N . GLN B 1 194 ? 39.108 100.352 71.359 1.00 12.70 ? 276 GLN B N 1 ATOM 4182 C CA . GLN B 1 194 ? 37.962 100.873 72.098 1.00 12.70 ? 276 GLN B CA 1 ATOM 4183 C C . GLN B 1 194 ? 36.602 100.676 71.441 1.00 12.70 ? 276 GLN B C 1 ATOM 4184 O O . GLN B 1 194 ? 35.705 100.094 72.047 1.00 12.70 ? 276 GLN B O 1 ATOM 4185 C CB . GLN B 1 194 ? 38.158 102.350 72.419 1.00 13.84 ? 276 GLN B CB 1 ATOM 4186 C CG . GLN B 1 194 ? 39.289 102.624 73.376 1.00 13.84 ? 276 GLN B CG 1 ATOM 4187 C CD . GLN B 1 194 ? 39.391 104.090 73.736 1.00 13.84 ? 276 GLN B CD 1 ATOM 4188 O OE1 . GLN B 1 194 ? 38.494 104.876 73.440 1.00 13.84 ? 276 GLN B OE1 1 ATOM 4189 N NE2 . GLN B 1 194 ? 40.487 104.465 74.379 1.00 13.84 ? 276 GLN B NE2 1 ATOM 4190 N N . ASP B 1 195 ? 36.442 101.161 70.211 1.00 6.67 ? 277 ASP B N 1 ATOM 4191 C CA . ASP B 1 195 ? 35.164 101.024 69.527 1.00 6.67 ? 277 ASP B CA 1 ATOM 4192 C C . ASP B 1 195 ? 34.773 99.575 69.221 1.00 6.67 ? 277 ASP B C 1 ATOM 4193 O O . ASP B 1 195 ? 33.633 99.182 69.473 1.00 6.67 ? 277 ASP B O 1 ATOM 4194 C CB . ASP B 1 195 ? 35.116 101.872 68.256 1.00 21.49 ? 277 ASP B CB 1 ATOM 4195 C CG . ASP B 1 195 ? 33.702 102.110 67.785 1.00 21.49 ? 277 ASP B CG 1 ATOM 4196 O OD1 . ASP B 1 195 ? 32.918 102.685 68.568 1.00 21.49 ? 277 ASP B OD1 1 ATOM 4197 O OD2 . ASP B 1 195 ? 33.367 101.702 66.656 1.00 21.49 ? 277 ASP B OD2 1 ATOM 4198 N N . PRO B 1 196 ? 35.689 98.777 68.636 1.00 9.70 ? 278 PRO B N 1 ATOM 4199 C CA . PRO B 1 196 ? 35.358 97.379 68.332 1.00 9.70 ? 278 PRO B CA 1 ATOM 4200 C C . PRO B 1 196 ? 34.901 96.635 69.590 1.00 9.70 ? 278 PRO B C 1 ATOM 4201 O O . PRO B 1 196 ? 34.006 95.792 69.539 1.00 9.70 ? 278 PRO B O 1 ATOM 4202 C CB . PRO B 1 196 ? 36.682 96.825 67.816 1.00 9.68 ? 278 PRO B CB 1 ATOM 4203 C CG . PRO B 1 196 ? 37.295 97.992 67.144 1.00 9.68 ? 278 PRO B CG 1 ATOM 4204 C CD . PRO B 1 196 ? 37.019 99.123 68.101 1.00 9.68 ? 278 PRO B CD 1 ATOM 4205 N N . ALA B 1 197 ? 35.517 96.962 70.721 1.00 6.56 ? 279 ALA B N 1 ATOM 4206 C CA . ALA B 1 197 ? 35.168 96.336 71.993 1.00 6.56 ? 279 ALA B CA 1 ATOM 4207 C C . ALA B 1 197 ? 33.780 96.783 72.451 1.00 6.56 ? 279 ALA B C 1 ATOM 4208 O O . ALA B 1 197 ? 32.946 95.959 72.809 1.00 6.56 ? 279 ALA B O 1 ATOM 4209 C CB . ALA B 1 197 ? 36.210 96.681 73.046 1.00 4.26 ? 279 ALA B CB 1 ATOM 4210 N N . ALA B 1 198 ? 33.529 98.089 72.403 1.00 5.51 ? 280 ALA B N 1 ATOM 4211 C CA . ALA B 1 198 ? 32.244 98.645 72.816 1.00 5.51 ? 280 ALA B CA 1 ATOM 4212 C C . ALA B 1 198 ? 31.106 98.063 71.998 1.00 5.51 ? 280 ALA B C 1 ATOM 4213 O O . ALA B 1 198 ? 30.028 97.797 72.532 1.00 5.51 ? 280 ALA B O 1 ATOM 4214 C CB . ALA B 1 198 ? 32.251 100.158 72.684 1.00 2.00 ? 280 ALA B CB 1 ATOM 4215 N N . GLN B 1 199 ? 31.358 97.876 70.702 1.00 7.57 ? 281 GLN B N 1 ATOM 4216 C CA . GLN B 1 199 ? 30.373 97.320 69.773 1.00 7.57 ? 281 GLN B CA 1 ATOM 4217 C C . GLN B 1 199 ? 29.976 95.912 70.177 1.00 7.57 ? 281 GLN B C 1 ATOM 4218 O O . GLN B 1 199 ? 28.790 95.597 70.250 1.00 7.57 ? 281 GLN B O 1 ATOM 4219 C CB . GLN B 1 199 ? 30.922 97.283 68.343 1.00 56.15 ? 281 GLN B CB 1 ATOM 4220 C CG . GLN B 1 199 ? 31.140 98.643 67.722 1.00 56.15 ? 281 GLN B CG 1 ATOM 4221 C CD . GLN B 1 199 ? 31.434 98.571 66.236 1.00 56.15 ? 281 GLN B CD 1 ATOM 4222 O OE1 . GLN B 1 199 ? 30.635 98.048 65.460 1.00 56.15 ? 281 GLN B OE1 1 ATOM 4223 N NE2 . GLN B 1 199 ? 32.584 99.101 65.833 1.00 56.15 ? 281 GLN B NE2 1 ATOM 4224 N N . LEU B 1 200 ? 30.978 95.070 70.425 1.00 6.69 ? 282 LEU B N 1 ATOM 4225 C CA . LEU B 1 200 ? 30.757 93.685 70.824 1.00 6.69 ? 282 LEU B CA 1 ATOM 4226 C C . LEU B 1 200 ? 29.976 93.575 72.131 1.00 6.69 ? 282 LEU B C 1 ATOM 4227 O O . LEU B 1 200 ? 28.991 92.844 72.212 1.00 6.69 ? 282 LEU B O 1 ATOM 4228 C CB . LEU B 1 200 ? 32.095 92.952 70.959 1.00 15.17 ? 282 LEU B CB 1 ATOM 4229 C CG . LEU B 1 200 ? 32.011 91.486 71.387 1.00 15.17 ? 282 LEU B CG 1 ATOM 4230 C CD1 . LEU B 1 200 ? 31.214 90.682 70.375 1.00 15.17 ? 282 LEU B CD1 1 ATOM 4231 C CD2 . LEU B 1 200 ? 33.406 90.914 71.537 1.00 15.17 ? 282 LEU B CD2 1 ATOM 4232 N N . PHE B 1 201 ? 30.418 94.291 73.159 1.00 5.48 ? 283 PHE B N 1 ATOM 4233 C CA . PHE B 1 201 ? 29.730 94.243 74.445 1.00 5.48 ? 283 PHE B CA 1 ATOM 4234 C C . PHE B 1 201 ? 28.282 94.732 74.336 1.00 5.48 ? 283 PHE B C 1 ATOM 4235 O O . PHE B 1 201 ? 27.383 94.138 74.935 1.00 5.48 ? 283 PHE B O 1 ATOM 4236 C CB . PHE B 1 201 ? 30.501 95.036 75.505 1.00 12.77 ? 283 PHE B CB 1 ATOM 4237 C CG . PHE B 1 201 ? 31.853 94.458 75.820 1.00 12.77 ? 283 PHE B CG 1 ATOM 4238 C CD1 . PHE B 1 201 ? 31.999 93.097 76.074 1.00 12.77 ? 283 PHE B CD1 1 ATOM 4239 C CD2 . PHE B 1 201 ? 32.984 95.271 75.852 1.00 12.77 ? 283 PHE B CD2 1 ATOM 4240 C CE1 . PHE B 1 201 ? 33.254 92.553 76.351 1.00 12.77 ? 283 PHE B CE1 1 ATOM 4241 C CE2 . PHE B 1 201 ? 34.242 94.738 76.129 1.00 12.77 ? 283 PHE B CE2 1 ATOM 4242 C CZ . PHE B 1 201 ? 34.377 93.377 76.377 1.00 12.77 ? 283 PHE B CZ 1 ATOM 4243 N N . ALA B 1 202 ? 28.049 95.774 73.538 1.00 10.68 ? 284 ALA B N 1 ATOM 4244 C CA . ALA B 1 202 ? 26.695 96.301 73.356 1.00 10.68 ? 284 ALA B CA 1 ATOM 4245 C C . ALA B 1 202 ? 25.825 95.283 72.613 1.00 10.68 ? 284 ALA B C 1 ATOM 4246 O O . ALA B 1 202 ? 24.631 95.158 72.889 1.00 10.68 ? 284 ALA B O 1 ATOM 4247 C CB . ALA B 1 202 ? 26.728 97.616 72.603 1.00 4.00 ? 284 ALA B CB 1 ATOM 4248 N N . ASN B 1 203 ? 26.425 94.555 71.676 1.00 10.01 ? 285 ASN B N 1 ATOM 4249 C CA . ASN B 1 203 ? 25.699 93.542 70.915 1.00 10.01 ? 285 ASN B CA 1 ATOM 4250 C C . ASN B 1 203 ? 25.292 92.382 71.809 1.00 10.01 ? 285 ASN B C 1 ATOM 4251 O O . ASN B 1 203 ? 24.201 91.835 71.664 1.00 10.01 ? 285 ASN B O 1 ATOM 4252 C CB . ASN B 1 203 ? 26.544 93.017 69.752 1.00 28.10 ? 285 ASN B CB 1 ATOM 4253 C CG . ASN B 1 203 ? 26.602 93.984 68.588 1.00 28.10 ? 285 ASN B CG 1 ATOM 4254 O OD1 . ASN B 1 203 ? 25.759 94.873 68.456 1.00 28.10 ? 285 ASN B OD1 1 ATOM 4255 N ND2 . ASN B 1 203 ? 27.602 93.812 67.731 1.00 28.10 ? 285 ASN B ND2 1 ATOM 4256 N N . VAL B 1 204 ? 26.183 91.991 72.716 1.00 12.04 ? 286 VAL B N 1 ATOM 4257 C CA . VAL B 1 204 ? 25.902 90.896 73.639 1.00 12.04 ? 286 VAL B CA 1 ATOM 4258 C C . VAL B 1 204 ? 24.718 91.263 74.536 1.00 12.04 ? 286 VAL B C 1 ATOM 4259 O O . VAL B 1 204 ? 23.825 90.447 74.765 1.00 12.04 ? 286 VAL B O 1 ATOM 4260 C CB . VAL B 1 204 ? 27.151 90.562 74.501 1.00 5.57 ? 286 VAL B CB 1 ATOM 4261 C CG1 . VAL B 1 204 ? 26.796 89.565 75.603 1.00 5.57 ? 286 VAL B CG1 1 ATOM 4262 C CG2 . VAL B 1 204 ? 28.252 89.997 73.612 1.00 5.57 ? 286 VAL B CG2 1 ATOM 4263 N N . TYR B 1 205 ? 24.708 92.513 74.995 1.00 8.70 ? 287 TYR B N 1 ATOM 4264 C CA . TYR B 1 205 ? 23.661 93.050 75.859 1.00 8.70 ? 287 TYR B CA 1 ATOM 4265 C C . TYR B 1 205 ? 22.301 93.068 75.160 1.00 8.70 ? 287 TYR B C 1 ATOM 4266 O O . TYR B 1 205 ? 21.311 92.579 75.702 1.00 8.70 ? 287 TYR B O 1 ATOM 4267 C CB . TYR B 1 205 ? 24.045 94.468 76.282 1.00 13.74 ? 287 TYR B CB 1 ATOM 4268 C CG . TYR B 1 205 ? 23.031 95.185 77.138 1.00 13.74 ? 287 TYR B CG 1 ATOM 4269 C CD1 . TYR B 1 205 ? 22.865 94.854 78.484 1.00 13.74 ? 287 TYR B CD1 1 ATOM 4270 C CD2 . TYR B 1 205 ? 22.260 96.220 76.614 1.00 13.74 ? 287 TYR B CD2 1 ATOM 4271 C CE1 . TYR B 1 205 ? 21.954 95.536 79.284 1.00 13.74 ? 287 TYR B CE1 1 ATOM 4272 C CE2 . TYR B 1 205 ? 21.347 96.910 77.404 1.00 13.74 ? 287 TYR B CE2 1 ATOM 4273 C CZ . TYR B 1 205 ? 21.200 96.562 78.735 1.00 13.74 ? 287 TYR B CZ 1 ATOM 4274 O OH . TYR B 1 205 ? 20.295 97.240 79.512 1.00 13.74 ? 287 TYR B OH 1 ATOM 4275 N N . LYS B 1 206 ? 22.259 93.649 73.964 1.00 7.43 ? 288 LYS B N 1 ATOM 4276 C CA . LYS B 1 206 ? 21.028 93.744 73.185 1.00 7.43 ? 288 LYS B CA 1 ATOM 4277 C C . LYS B 1 206 ? 20.537 92.388 72.683 1.00 7.43 ? 288 LYS B C 1 ATOM 4278 O O . LYS B 1 206 ? 19.335 92.155 72.583 1.00 7.43 ? 288 LYS B O 1 ATOM 4279 C CB . LYS B 1 206 ? 21.225 94.699 72.008 1.00 21.16 ? 288 LYS B CB 1 ATOM 4280 C CG . LYS B 1 206 ? 21.510 96.125 72.429 1.00 21.16 ? 288 LYS B CG 1 ATOM 4281 C CD . LYS B 1 206 ? 21.781 97.020 71.236 1.00 21.16 ? 288 LYS B CD 1 ATOM 4282 C CE . LYS B 1 206 ? 23.015 96.567 70.477 1.00 21.16 ? 288 LYS B CE 1 ATOM 4283 N NZ . LYS B 1 206 ? 23.359 97.482 69.360 1.00 21.16 ? 288 LYS B NZ 1 ATOM 4284 N N . ASN B 1 207 ? 21.470 91.490 72.382 1.00 14.09 ? 289 ASN B N 1 ATOM 4285 C CA . ASN B 1 207 ? 21.129 90.158 71.901 1.00 14.09 ? 289 ASN B CA 1 ATOM 4286 C C . ASN B 1 207 ? 20.494 89.320 73.012 1.00 14.09 ? 289 ASN B C 1 ATOM 4287 O O . ASN B 1 207 ? 19.772 88.356 72.742 1.00 14.09 ? 289 ASN B O 1 ATOM 4288 C CB . ASN B 1 207 ? 22.373 89.464 71.347 1.00 17.14 ? 289 ASN B CB 1 ATOM 4289 C CG . ASN B 1 207 ? 22.052 88.179 70.612 1.00 17.14 ? 289 ASN B CG 1 ATOM 4290 O OD1 . ASN B 1 207 ? 21.208 88.163 69.712 1.00 17.14 ? 289 ASN B OD1 1 ATOM 4291 N ND2 . ASN B 1 207 ? 22.733 87.101 71.000 1.00 17.14 ? 289 ASN B ND2 1 ATOM 4292 N N . ALA B 1 208 ? 20.775 89.681 74.262 1.00 10.71 ? 290 ALA B N 1 ATOM 4293 C CA . ALA B 1 208 ? 20.207 88.981 75.406 1.00 10.71 ? 290 ALA B CA 1 ATOM 4294 C C . ALA B 1 208 ? 18.963 89.721 75.894 1.00 10.71 ? 290 ALA B C 1 ATOM 4295 O O . ALA B 1 208 ? 18.500 89.508 77.016 1.00 10.71 ? 290 ALA B O 1 ATOM 4296 C CB . ALA B 1 208 ? 21.239 88.873 76.521 1.00 9.65 ? 290 ALA B CB 1 ATOM 4297 N N . SER B 1 209 ? 18.431 90.592 75.040 1.00 13.72 ? 291 SER B N 1 ATOM 4298 C CA . SER B 1 209 ? 17.241 91.384 75.342 1.00 13.72 ? 291 SER B CA 1 ATOM 4299 C C . SER B 1 209 ? 17.415 92.353 76.506 1.00 13.72 ? 291 SER B C 1 ATOM 4300 O O . SER B 1 209 ? 16.514 92.511 77.333 1.00 13.72 ? 291 SER B O 1 ATOM 4301 C CB . SER B 1 209 ? 16.038 90.472 75.591 1.00 21.23 ? 291 SER B CB 1 ATOM 4302 O OG . SER B 1 209 ? 15.759 89.699 74.439 1.00 21.23 ? 291 SER B OG 1 ATOM 4303 N N . SER B 1 210 ? 18.588 92.974 76.584 1.00 10.98 ? 292 SER B N 1 ATOM 4304 C CA . SER B 1 210 ? 18.885 93.956 77.629 1.00 10.98 ? 292 SER B CA 1 ATOM 4305 C C . SER B 1 210 ? 18.517 93.478 79.040 1.00 10.98 ? 292 SER B C 1 ATOM 4306 O O . SER B 1 210 ? 17.704 94.105 79.724 1.00 10.98 ? 292 SER B O 1 ATOM 4307 C CB . SER B 1 210 ? 18.155 95.261 77.309 1.00 22.21 ? 292 SER B CB 1 ATOM 4308 O OG . SER B 1 210 ? 18.429 95.665 75.979 1.00 22.21 ? 292 SER B OG 1 ATOM 4309 N N . PRO B 1 211 ? 19.167 92.402 79.517 1.00 13.75 ? 293 PRO B N 1 ATOM 4310 C CA . PRO B 1 211 ? 18.903 91.838 80.845 1.00 13.75 ? 293 PRO B CA 1 ATOM 4311 C C . PRO B 1 211 ? 19.020 92.837 81.990 1.00 13.75 ? 293 PRO B C 1 ATOM 4312 O O . PRO B 1 211 ? 20.024 93.540 82.122 1.00 13.75 ? 293 PRO B O 1 ATOM 4313 C CB . PRO B 1 211 ? 19.958 90.736 80.974 1.00 13.04 ? 293 PRO B CB 1 ATOM 4314 C CG . PRO B 1 211 ? 20.289 90.390 79.568 1.00 13.04 ? 293 PRO B CG 1 ATOM 4315 C CD . PRO B 1 211 ? 20.304 91.716 78.880 1.00 13.04 ? 293 PRO B CD 1 ATOM 4316 N N . ARG B 1 212 ? 17.983 92.868 82.821 1.00 10.71 ? 294 ARG B N 1 ATOM 4317 C CA . ARG B 1 212 ? 17.911 93.737 83.992 1.00 10.71 ? 294 ARG B CA 1 ATOM 4318 C C . ARG B 1 212 ? 19.101 93.486 84.930 1.00 10.71 ? 294 ARG B C 1 ATOM 4319 O O . ARG B 1 212 ? 19.731 94.429 85.415 1.00 10.71 ? 294 ARG B O 1 ATOM 4320 C CB . ARG B 1 212 ? 16.581 93.465 84.708 1.00 124.15 ? 294 ARG B CB 1 ATOM 4321 C CG . ARG B 1 212 ? 16.484 93.857 86.172 1.00 124.15 ? 294 ARG B CG 1 ATOM 4322 C CD . ARG B 1 212 ? 15.157 93.350 86.734 1.00 124.15 ? 294 ARG B CD 1 ATOM 4323 N NE . ARG B 1 212 ? 15.028 93.514 88.181 1.00 124.15 ? 294 ARG B NE 1 ATOM 4324 C CZ . ARG B 1 212 ? 13.897 93.320 88.858 1.00 124.15 ? 294 ARG B CZ 1 ATOM 4325 N NH1 . ARG B 1 212 ? 12.789 92.957 88.220 1.00 124.15 ? 294 ARG B NH1 1 ATOM 4326 N NH2 . ARG B 1 212 ? 13.870 93.483 90.175 1.00 124.15 ? 294 ARG B NH2 1 ATOM 4327 N N . ALA B 1 213 ? 19.425 92.212 85.138 1.00 6.30 ? 295 ALA B N 1 ATOM 4328 C CA . ALA B 1 213 ? 20.527 91.807 86.017 1.00 6.30 ? 295 ALA B CA 1 ATOM 4329 C C . ALA B 1 213 ? 21.933 92.126 85.499 1.00 6.30 ? 295 ALA B C 1 ATOM 4330 O O . ALA B 1 213 ? 22.878 92.149 86.278 1.00 6.30 ? 295 ALA B O 1 ATOM 4331 C CB . ALA B 1 213 ? 20.417 90.320 86.341 1.00 2.00 ? 295 ALA B CB 1 ATOM 4332 N N . LEU B 1 214 ? 22.088 92.332 84.192 1.00 8.73 ? 296 LEU B N 1 ATOM 4333 C CA . LEU B 1 214 ? 23.401 92.655 83.632 1.00 8.73 ? 296 LEU B CA 1 ATOM 4334 C C . LEU B 1 214 ? 23.702 94.138 83.876 1.00 8.73 ? 296 LEU B C 1 ATOM 4335 O O . LEU B 1 214 ? 23.361 95.004 83.071 1.00 8.73 ? 296 LEU B O 1 ATOM 4336 C CB . LEU B 1 214 ? 23.443 92.317 82.137 1.00 6.73 ? 296 LEU B CB 1 ATOM 4337 C CG . LEU B 1 214 ? 24.791 92.430 81.418 1.00 6.73 ? 296 LEU B CG 1 ATOM 4338 C CD1 . LEU B 1 214 ? 25.875 91.661 82.168 1.00 6.73 ? 296 LEU B CD1 1 ATOM 4339 C CD2 . LEU B 1 214 ? 24.634 91.898 80.008 1.00 6.73 ? 296 LEU B CD2 1 ATOM 4340 N N . ARG B 1 215 ? 24.343 94.416 85.007 1.00 6.84 ? 297 ARG B N 1 ATOM 4341 C CA . ARG B 1 215 ? 24.672 95.782 85.405 1.00 6.84 ? 297 ARG B CA 1 ATOM 4342 C C . ARG B 1 215 ? 25.757 96.485 84.592 1.00 6.84 ? 297 ARG B C 1 ATOM 4343 O O . ARG B 1 215 ? 25.689 97.700 84.377 1.00 6.84 ? 297 ARG B O 1 ATOM 4344 C CB . ARG B 1 215 ? 25.033 95.817 86.896 1.00 13.01 ? 297 ARG B CB 1 ATOM 4345 C CG . ARG B 1 215 ? 25.798 97.059 87.312 1.00 13.01 ? 297 ARG B CG 1 ATOM 4346 C CD . ARG B 1 215 ? 25.121 97.828 88.404 1.00 13.01 ? 297 ARG B CD 1 ATOM 4347 N NE . ARG B 1 215 ? 24.149 98.797 87.922 1.00 13.01 ? 297 ARG B NE 1 ATOM 4348 C CZ . ARG B 1 215 ? 24.088 100.062 88.335 1.00 13.01 ? 297 ARG B CZ 1 ATOM 4349 N NH1 . ARG B 1 215 ? 24.949 100.522 89.231 1.00 13.01 ? 297 ARG B NH1 1 ATOM 4350 N NH2 . ARG B 1 215 ? 23.115 100.849 87.908 1.00 13.01 ? 297 ARG B NH2 1 ATOM 4351 N N . GLY B 1 216 ? 26.772 95.734 84.170 1.00 5.96 ? 298 GLY B N 1 ATOM 4352 C CA . GLY B 1 216 ? 27.845 96.344 83.412 1.00 5.96 ? 298 GLY B CA 1 ATOM 4353 C C . GLY B 1 216 ? 29.046 95.467 83.139 1.00 5.96 ? 298 GLY B C 1 ATOM 4354 O O . GLY B 1 216 ? 28.903 94.273 82.900 1.00 5.96 ? 298 GLY B O 1 ATOM 4355 N N . LEU B 1 217 ? 30.238 96.055 83.231 1.00 4.51 ? 299 LEU B N 1 ATOM 4356 C CA . LEU B 1 217 ? 31.481 95.349 82.933 1.00 4.51 ? 299 LEU B CA 1 ATOM 4357 C C . LEU B 1 217 ? 32.490 95.300 84.082 1.00 4.51 ? 299 LEU B C 1 ATOM 4358 O O . LEU B 1 217 ? 32.509 96.177 84.940 1.00 4.51 ? 299 LEU B O 1 ATOM 4359 C CB . LEU B 1 217 ? 32.147 96.002 81.717 1.00 6.07 ? 299 LEU B CB 1 ATOM 4360 C CG . LEU B 1 217 ? 31.294 96.141 80.447 1.00 6.07 ? 299 LEU B CG 1 ATOM 4361 C CD1 . LEU B 1 217 ? 32.030 96.965 79.408 1.00 6.07 ? 299 LEU B CD1 1 ATOM 4362 C CD2 . LEU B 1 217 ? 30.959 94.771 79.894 1.00 6.07 ? 299 LEU B CD2 1 ATOM 4363 N N . ALA B 1 218 ? 33.344 94.280 84.062 1.00 4.14 ? 300 ALA B N 1 ATOM 4364 C CA . ALA B 1 218 ? 34.382 94.098 85.071 1.00 4.14 ? 300 ALA B CA 1 ATOM 4365 C C . ALA B 1 218 ? 35.723 94.251 84.364 1.00 4.14 ? 300 ALA B C 1 ATOM 4366 O O . ALA B 1 218 ? 35.919 93.684 83.289 1.00 4.14 ? 300 ALA B O 1 ATOM 4367 C CB . ALA B 1 218 ? 34.270 92.714 85.688 1.00 2.00 ? 300 ALA B CB 1 ATOM 4368 N N . THR B 1 219 ? 36.629 95.046 84.931 1.00 2.76 ? 301 THR B N 1 ATOM 4369 C CA . THR B 1 219 ? 37.934 95.249 84.308 1.00 2.76 ? 301 THR B CA 1 ATOM 4370 C C . THR B 1 219 ? 39.079 94.865 85.237 1.00 2.76 ? 301 THR B C 1 ATOM 4371 O O . THR B 1 219 ? 38.901 94.750 86.453 1.00 2.76 ? 301 THR B O 1 ATOM 4372 C CB . THR B 1 219 ? 38.155 96.726 83.842 1.00 6.46 ? 301 THR B CB 1 ATOM 4373 O OG1 . THR B 1 219 ? 38.525 97.539 84.962 1.00 6.46 ? 301 THR B OG1 1 ATOM 4374 C CG2 . THR B 1 219 ? 36.895 97.313 83.211 1.00 6.46 ? 301 THR B CG2 1 ATOM 4375 N N . ASN B 1 220 ? 40.244 94.642 84.636 1.00 3.13 ? 302 ASN B N 1 ATOM 4376 C CA . ASN B 1 220 ? 41.471 94.292 85.348 1.00 3.13 ? 302 ASN B CA 1 ATOM 4377 C C . ASN B 1 220 ? 41.432 92.975 86.120 1.00 3.13 ? 302 ASN B C 1 ATOM 4378 O O . ASN B 1 220 ? 42.273 92.741 86.981 1.00 3.13 ? 302 ASN B O 1 ATOM 4379 C CB . ASN B 1 220 ? 41.882 95.441 86.283 1.00 5.02 ? 302 ASN B CB 1 ATOM 4380 C CG . ASN B 1 220 ? 43.377 95.475 86.548 1.00 5.02 ? 302 ASN B CG 1 ATOM 4381 O OD1 . ASN B 1 220 ? 44.186 95.314 85.632 1.00 5.02 ? 302 ASN B OD1 1 ATOM 4382 N ND2 . ASN B 1 220 ? 43.750 95.696 87.803 1.00 5.02 ? 302 ASN B ND2 1 ATOM 4383 N N . VAL B 1 221 ? 40.482 92.105 85.796 1.00 2.00 ? 303 VAL B N 1 ATOM 4384 C CA . VAL B 1 221 ? 40.364 90.822 86.479 1.00 2.00 ? 303 VAL B CA 1 ATOM 4385 C C . VAL B 1 221 ? 41.631 89.979 86.339 1.00 2.00 ? 303 VAL B C 1 ATOM 4386 O O . VAL B 1 221 ? 42.081 89.679 85.227 1.00 2.00 ? 303 VAL B O 1 ATOM 4387 C CB . VAL B 1 221 ? 39.141 90.020 85.981 1.00 5.14 ? 303 VAL B CB 1 ATOM 4388 C CG1 . VAL B 1 221 ? 39.083 88.660 86.666 1.00 5.14 ? 303 VAL B CG1 1 ATOM 4389 C CG2 . VAL B 1 221 ? 37.866 90.795 86.271 1.00 5.14 ? 303 VAL B CG2 1 ATOM 4390 N N . ALA B 1 222 ? 42.204 89.614 87.483 1.00 3.46 ? 304 ALA B N 1 ATOM 4391 C CA . ALA B 1 222 ? 43.428 88.819 87.550 1.00 3.46 ? 304 ALA B CA 1 ATOM 4392 C C . ALA B 1 222 ? 44.626 89.576 86.988 1.00 3.46 ? 304 ALA B C 1 ATOM 4393 O O . ALA B 1 222 ? 45.671 88.987 86.722 1.00 3.46 ? 304 ALA B O 1 ATOM 4394 C CB . ALA B 1 222 ? 43.250 87.469 86.831 1.00 2.58 ? 304 ALA B CB 1 ATOM 4395 N N . ASN B 1 223 ? 44.464 90.874 86.774 1.00 3.26 ? 305 ASN B N 1 ATOM 4396 C CA . ASN B 1 223 ? 45.558 91.685 86.273 1.00 3.26 ? 305 ASN B CA 1 ATOM 4397 C C . ASN B 1 223 ? 46.089 92.652 87.324 1.00 3.26 ? 305 ASN B C 1 ATOM 4398 O O . ASN B 1 223 ? 45.645 92.624 88.476 1.00 3.26 ? 305 ASN B O 1 ATOM 4399 C CB . ASN B 1 223 ? 45.222 92.356 84.948 1.00 18.80 ? 305 ASN B CB 1 ATOM 4400 C CG . ASN B 1 223 ? 45.830 91.617 83.776 1.00 18.80 ? 305 ASN B CG 1 ATOM 4401 O OD1 . ASN B 1 223 ? 46.994 91.827 83.439 1.00 18.80 ? 305 ASN B OD1 1 ATOM 4402 N ND2 . ASN B 1 223 ? 45.072 90.691 83.197 1.00 18.80 ? 305 ASN B ND2 1 ATOM 4403 N N . TYR B 1 224 ? 47.020 93.518 86.933 1.00 8.22 ? 306 TYR B N 1 ATOM 4404 C CA . TYR B 1 224 ? 47.685 94.399 87.893 1.00 8.22 ? 306 TYR B CA 1 ATOM 4405 C C . TYR B 1 224 ? 47.676 95.903 87.644 1.00 8.22 ? 306 TYR B C 1 ATOM 4406 O O . TYR B 1 224 ? 48.403 96.631 88.314 1.00 8.22 ? 306 TYR B O 1 ATOM 4407 C CB . TYR B 1 224 ? 49.146 93.951 88.011 1.00 4.48 ? 306 TYR B CB 1 ATOM 4408 C CG . TYR B 1 224 ? 49.355 92.451 87.977 1.00 4.48 ? 306 TYR B CG 1 ATOM 4409 C CD1 . TYR B 1 224 ? 49.387 91.753 86.766 1.00 4.48 ? 306 TYR B CD1 1 ATOM 4410 C CD2 . TYR B 1 224 ? 49.541 91.731 89.157 1.00 4.48 ? 306 TYR B CD2 1 ATOM 4411 C CE1 . TYR B 1 224 ? 49.601 90.370 86.736 1.00 4.48 ? 306 TYR B CE1 1 ATOM 4412 C CE2 . TYR B 1 224 ? 49.757 90.357 89.140 1.00 4.48 ? 306 TYR B CE2 1 ATOM 4413 C CZ . TYR B 1 224 ? 49.789 89.684 87.934 1.00 4.48 ? 306 TYR B CZ 1 ATOM 4414 O OH . TYR B 1 224 ? 50.038 88.330 87.935 1.00 4.48 ? 306 TYR B OH 1 ATOM 4415 N N . ASN B 1 225 ? 46.879 96.373 86.689 1.00 6.58 ? 307 ASN B N 1 ATOM 4416 C CA . ASN B 1 225 ? 46.838 97.798 86.382 1.00 6.58 ? 307 ASN B CA 1 ATOM 4417 C C . ASN B 1 225 ? 46.392 98.659 87.561 1.00 6.58 ? 307 ASN B C 1 ATOM 4418 O O . ASN B 1 225 ? 45.637 98.210 88.430 1.00 6.58 ? 307 ASN B O 1 ATOM 4419 C CB . ASN B 1 225 ? 45.923 98.067 85.190 1.00 8.46 ? 307 ASN B CB 1 ATOM 4420 C CG . ASN B 1 225 ? 46.399 97.391 83.923 1.00 8.46 ? 307 ASN B CG 1 ATOM 4421 O OD1 . ASN B 1 225 ? 47.515 96.875 83.856 1.00 8.46 ? 307 ASN B OD1 1 ATOM 4422 N ND2 . ASN B 1 225 ? 45.549 97.381 82.909 1.00 8.46 ? 307 ASN B ND2 1 ATOM 4423 N N . GLY B 1 226 ? 46.890 99.890 87.602 1.00 6.03 ? 308 GLY B N 1 ATOM 4424 C CA . GLY B 1 226 ? 46.506 100.804 88.657 1.00 6.03 ? 308 GLY B CA 1 ATOM 4425 C C . GLY B 1 226 ? 45.158 101.406 88.314 1.00 6.03 ? 308 GLY B C 1 ATOM 4426 O O . GLY B 1 226 ? 44.768 101.457 87.146 1.00 6.03 ? 308 GLY B O 1 ATOM 4427 N N . TRP B 1 227 ? 44.424 101.823 89.337 1.00 5.05 ? 309 TRP B N 1 ATOM 4428 C CA . TRP B 1 227 ? 43.118 102.429 89.142 1.00 5.05 ? 309 TRP B CA 1 ATOM 4429 C C . TRP B 1 227 ? 43.224 103.879 88.681 1.00 5.05 ? 309 TRP B C 1 ATOM 4430 O O . TRP B 1 227 ? 42.675 104.248 87.643 1.00 5.05 ? 309 TRP B O 1 ATOM 4431 C CB . TRP B 1 227 ? 42.307 102.342 90.447 1.00 5.90 ? 309 TRP B CB 1 ATOM 4432 C CG . TRP B 1 227 ? 41.216 103.380 90.602 1.00 5.90 ? 309 TRP B CG 1 ATOM 4433 C CD1 . TRP B 1 227 ? 41.152 104.364 91.553 1.00 5.90 ? 309 TRP B CD1 1 ATOM 4434 C CD2 . TRP B 1 227 ? 40.052 103.544 89.781 1.00 5.90 ? 309 TRP B CD2 1 ATOM 4435 N NE1 . TRP B 1 227 ? 40.026 105.130 91.368 1.00 5.90 ? 309 TRP B NE1 1 ATOM 4436 C CE2 . TRP B 1 227 ? 39.332 104.651 90.286 1.00 5.90 ? 309 TRP B CE2 1 ATOM 4437 C CE3 . TRP B 1 227 ? 39.546 102.865 88.662 1.00 5.90 ? 309 TRP B CE3 1 ATOM 4438 C CZ2 . TRP B 1 227 ? 38.134 105.099 89.716 1.00 5.90 ? 309 TRP B CZ2 1 ATOM 4439 C CZ3 . TRP B 1 227 ? 38.357 103.307 88.092 1.00 5.90 ? 309 TRP B CZ3 1 ATOM 4440 C CH2 . TRP B 1 227 ? 37.663 104.415 88.620 1.00 5.90 ? 309 TRP B CH2 1 ATOM 4441 N N . ASN B 1 228 ? 43.954 104.696 89.437 1.00 6.96 ? 310 ASN B N 1 ATOM 4442 C CA . ASN B 1 228 ? 44.069 106.114 89.113 1.00 6.96 ? 310 ASN B CA 1 ATOM 4443 C C . ASN B 1 228 ? 45.472 106.706 89.235 1.00 6.96 ? 310 ASN B C 1 ATOM 4444 O O . ASN B 1 228 ? 45.626 107.869 89.628 1.00 6.96 ? 310 ASN B O 1 ATOM 4445 C CB . ASN B 1 228 ? 43.110 106.901 90.005 1.00 12.84 ? 310 ASN B CB 1 ATOM 4446 C CG . ASN B 1 228 ? 43.409 106.719 91.484 1.00 12.84 ? 310 ASN B CG 1 ATOM 4447 O OD1 . ASN B 1 228 ? 44.236 105.882 91.864 1.00 12.84 ? 310 ASN B OD1 1 ATOM 4448 N ND2 . ASN B 1 228 ? 42.735 107.501 92.320 1.00 12.84 ? 310 ASN B ND2 1 ATOM 4449 N N . ILE B 1 229 ? 46.491 105.923 88.891 1.00 12.41 ? 311 ILE B N 1 ATOM 4450 C CA . ILE B 1 229 ? 47.867 106.407 88.964 1.00 12.41 ? 311 ILE B CA 1 ATOM 4451 C C . ILE B 1 229 ? 48.062 107.654 88.093 1.00 12.41 ? 311 ILE B C 1 ATOM 4452 O O . ILE B 1 229 ? 47.535 107.744 86.983 1.00 12.41 ? 311 ILE B O 1 ATOM 4453 C CB . ILE B 1 229 ? 48.895 105.296 88.621 1.00 13.37 ? 311 ILE B CB 1 ATOM 4454 C CG1 . ILE B 1 229 ? 48.549 104.611 87.296 1.00 13.37 ? 311 ILE B CG1 1 ATOM 4455 C CG2 . ILE B 1 229 ? 48.932 104.270 89.744 1.00 13.37 ? 311 ILE B CG2 1 ATOM 4456 C CD1 . ILE B 1 229 ? 49.502 103.489 86.926 1.00 13.37 ? 311 ILE B CD1 1 ATOM 4457 N N . THR B 1 230 ? 48.789 108.624 88.640 1.00 19.34 ? 312 THR B N 1 ATOM 4458 C CA . THR B 1 230 ? 49.044 109.908 87.992 1.00 19.34 ? 312 THR B CA 1 ATOM 4459 C C . THR B 1 230 ? 50.154 109.946 86.943 1.00 19.34 ? 312 THR B C 1 ATOM 4460 O O . THR B 1 230 ? 50.246 110.904 86.172 1.00 19.34 ? 312 THR B O 1 ATOM 4461 C CB . THR B 1 230 ? 49.326 110.985 89.049 1.00 13.91 ? 312 THR B CB 1 ATOM 4462 O OG1 . THR B 1 230 ? 50.414 110.560 89.880 1.00 13.91 ? 312 THR B OG1 1 ATOM 4463 C CG2 . THR B 1 230 ? 48.101 111.196 89.919 1.00 13.91 ? 312 THR B CG2 1 ATOM 4464 N N . SER B 1 231 ? 51.005 108.927 86.932 1.00 17.27 ? 313 SER B N 1 ATOM 4465 C CA . SER B 1 231 ? 52.097 108.851 85.968 1.00 17.27 ? 313 SER B CA 1 ATOM 4466 C C . SER B 1 231 ? 52.107 107.490 85.285 1.00 17.27 ? 313 SER B C 1 ATOM 4467 O O . SER B 1 231 ? 51.965 106.457 85.936 1.00 17.27 ? 313 SER B O 1 ATOM 4468 C CB . SER B 1 231 ? 53.441 109.108 86.649 1.00 38.78 ? 313 SER B CB 1 ATOM 4469 O OG . SER B 1 231 ? 53.539 110.456 87.074 1.00 38.78 ? 313 SER B OG 1 ATOM 4470 N N . PRO B 1 232 ? 52.260 107.480 83.955 1.00 13.95 ? 314 PRO B N 1 ATOM 4471 C CA . PRO B 1 232 ? 52.286 106.241 83.170 1.00 13.95 ? 314 PRO B CA 1 ATOM 4472 C C . PRO B 1 232 ? 53.549 105.399 83.323 1.00 13.95 ? 314 PRO B C 1 ATOM 4473 O O . PRO B 1 232 ? 54.662 105.898 83.167 1.00 13.95 ? 314 PRO B O 1 ATOM 4474 C CB . PRO B 1 232 ? 52.138 106.748 81.738 1.00 14.76 ? 314 PRO B CB 1 ATOM 4475 C CG . PRO B 1 232 ? 52.801 108.079 81.777 1.00 14.76 ? 314 PRO B CG 1 ATOM 4476 C CD . PRO B 1 232 ? 52.325 108.661 83.077 1.00 14.76 ? 314 PRO B CD 1 ATOM 4477 N N . PRO B 1 233 ? 53.388 104.111 83.674 1.00 11.71 ? 315 PRO B N 1 ATOM 4478 C CA . PRO B 1 233 ? 54.540 103.218 83.828 1.00 11.71 ? 315 PRO B CA 1 ATOM 4479 C C . PRO B 1 233 ? 55.222 103.068 82.462 1.00 11.71 ? 315 PRO B C 1 ATOM 4480 O O . PRO B 1 233 ? 54.578 103.232 81.419 1.00 11.71 ? 315 PRO B O 1 ATOM 4481 C CB . PRO B 1 233 ? 53.895 101.908 84.276 1.00 10.00 ? 315 PRO B CB 1 ATOM 4482 C CG . PRO B 1 233 ? 52.667 102.348 84.997 1.00 10.00 ? 315 PRO B CG 1 ATOM 4483 C CD . PRO B 1 233 ? 52.145 103.446 84.109 1.00 10.00 ? 315 PRO B CD 1 ATOM 4484 N N . SER B 1 234 ? 56.517 102.770 82.463 1.00 14.10 ? 316 SER B N 1 ATOM 4485 C CA . SER B 1 234 ? 57.274 102.624 81.219 1.00 14.10 ? 316 SER B CA 1 ATOM 4486 C C . SER B 1 234 ? 56.675 101.604 80.257 1.00 14.10 ? 316 SER B C 1 ATOM 4487 O O . SER B 1 234 ? 56.616 101.845 79.054 1.00 14.10 ? 316 SER B O 1 ATOM 4488 C CB . SER B 1 234 ? 58.735 102.267 81.505 1.00 16.74 ? 316 SER B CB 1 ATOM 4489 O OG . SER B 1 234 ? 58.842 100.999 82.132 1.00 16.74 ? 316 SER B OG 1 ATOM 4490 N N . TYR B 1 235 ? 56.209 100.479 80.792 1.00 9.29 ? 317 TYR B N 1 ATOM 4491 C CA . TYR B 1 235 ? 55.627 99.429 79.959 1.00 9.29 ? 317 TYR B CA 1 ATOM 4492 C C . TYR B 1 235 ? 54.287 99.776 79.291 1.00 9.29 ? 317 TYR B C 1 ATOM 4493 O O . TYR B 1 235 ? 53.794 99.006 78.470 1.00 9.29 ? 317 TYR B O 1 ATOM 4494 C CB . TYR B 1 235 ? 55.536 98.104 80.731 1.00 6.66 ? 317 TYR B CB 1 ATOM 4495 C CG . TYR B 1 235 ? 54.930 98.228 82.106 1.00 6.66 ? 317 TYR B CG 1 ATOM 4496 C CD1 . TYR B 1 235 ? 53.553 98.351 82.272 1.00 6.66 ? 317 TYR B CD1 1 ATOM 4497 C CD2 . TYR B 1 235 ? 55.740 98.271 83.241 1.00 6.66 ? 317 TYR B CD2 1 ATOM 4498 C CE1 . TYR B 1 235 ? 52.997 98.521 83.531 1.00 6.66 ? 317 TYR B CE1 1 ATOM 4499 C CE2 . TYR B 1 235 ? 55.191 98.440 84.508 1.00 6.66 ? 317 TYR B CE2 1 ATOM 4500 C CZ . TYR B 1 235 ? 53.819 98.568 84.642 1.00 6.66 ? 317 TYR B CZ 1 ATOM 4501 O OH . TYR B 1 235 ? 53.272 98.763 85.886 1.00 6.66 ? 317 TYR B OH 1 ATOM 4502 N N . THR B 1 236 ? 53.703 100.927 79.627 1.00 13.01 ? 318 THR B N 1 ATOM 4503 C CA . THR B 1 236 ? 52.434 101.342 79.012 1.00 13.01 ? 318 THR B CA 1 ATOM 4504 C C . THR B 1 236 ? 52.677 102.289 77.838 1.00 13.01 ? 318 THR B C 1 ATOM 4505 O O . THR B 1 236 ? 51.729 102.744 77.192 1.00 13.01 ? 318 THR B O 1 ATOM 4506 C CB . THR B 1 236 ? 51.488 102.072 80.002 1.00 8.52 ? 318 THR B CB 1 ATOM 4507 O OG1 . THR B 1 236 ? 52.047 103.341 80.361 1.00 8.52 ? 318 THR B OG1 1 ATOM 4508 C CG2 . THR B 1 236 ? 51.260 101.239 81.255 1.00 8.52 ? 318 THR B CG2 1 ATOM 4509 N N . GLN B 1 237 ? 53.951 102.579 77.579 1.00 18.92 ? 319 GLN B N 1 ATOM 4510 C CA . GLN B 1 237 ? 54.382 103.484 76.509 1.00 18.92 ? 319 GLN B CA 1 ATOM 4511 C C . GLN B 1 237 ? 53.590 103.358 75.213 1.00 18.92 ? 319 GLN B C 1 ATOM 4512 O O . GLN B 1 237 ? 53.456 102.269 74.656 1.00 18.92 ? 319 GLN B O 1 ATOM 4513 C CB . GLN B 1 237 ? 55.876 103.285 76.228 1.00 165.05 ? 319 GLN B CB 1 ATOM 4514 C CG . GLN B 1 237 ? 56.465 104.250 75.205 1.00 165.05 ? 319 GLN B CG 1 ATOM 4515 C CD . GLN B 1 237 ? 57.934 103.983 74.917 1.00 165.05 ? 319 GLN B CD 1 ATOM 4516 O OE1 . GLN B 1 237 ? 58.545 103.084 75.501 1.00 165.05 ? 319 GLN B OE1 1 ATOM 4517 N NE2 . GLN B 1 237 ? 58.509 104.767 74.008 1.00 165.05 ? 319 GLN B NE2 1 ATOM 4518 N N . GLY B 1 238 ? 53.046 104.484 74.762 1.00 21.43 ? 320 GLY B N 1 ATOM 4519 C CA . GLY B 1 238 ? 52.276 104.508 73.530 1.00 21.43 ? 320 GLY B CA 1 ATOM 4520 C C . GLY B 1 238 ? 50.771 104.497 73.724 1.00 21.43 ? 320 GLY B C 1 ATOM 4521 O O . GLY B 1 238 ? 50.016 104.702 72.771 1.00 21.43 ? 320 GLY B O 1 ATOM 4522 N N . ASN B 1 239 ? 50.332 104.262 74.957 1.00 8.80 ? 321 ASN B N 1 ATOM 4523 C CA . ASN B 1 239 ? 48.906 104.212 75.265 1.00 8.80 ? 321 ASN B CA 1 ATOM 4524 C C . ASN B 1 239 ? 48.514 105.334 76.220 1.00 8.80 ? 321 ASN B C 1 ATOM 4525 O O . ASN B 1 239 ? 48.992 105.394 77.350 1.00 8.80 ? 321 ASN B O 1 ATOM 4526 C CB . ASN B 1 239 ? 48.557 102.854 75.883 1.00 13.73 ? 321 ASN B CB 1 ATOM 4527 C CG . ASN B 1 239 ? 47.073 102.547 75.827 1.00 13.73 ? 321 ASN B CG 1 ATOM 4528 O OD1 . ASN B 1 239 ? 46.277 103.347 75.336 1.00 13.73 ? 321 ASN B OD1 1 ATOM 4529 N ND2 . ASN B 1 239 ? 46.697 101.371 76.314 1.00 13.73 ? 321 ASN B ND2 1 ATOM 4530 N N . ALA B 1 240 ? 47.640 106.225 75.758 1.00 14.57 ? 322 ALA B N 1 ATOM 4531 C CA . ALA B 1 240 ? 47.176 107.341 76.579 1.00 14.57 ? 322 ALA B CA 1 ATOM 4532 C C . ALA B 1 240 ? 46.309 106.823 77.726 1.00 14.57 ? 322 ALA B C 1 ATOM 4533 O O . ALA B 1 240 ? 46.217 107.451 78.776 1.00 14.57 ? 322 ALA B O 1 ATOM 4534 C CB . ALA B 1 240 ? 46.393 108.327 75.727 1.00 18.23 ? 322 ALA B CB 1 ATOM 4535 N N . VAL B 1 241 ? 45.658 105.685 77.503 1.00 12.31 ? 323 VAL B N 1 ATOM 4536 C CA . VAL B 1 241 ? 44.808 105.043 78.506 1.00 12.31 ? 323 VAL B CA 1 ATOM 4537 C C . VAL B 1 241 ? 45.710 104.061 79.259 1.00 12.31 ? 323 VAL B C 1 ATOM 4538 O O . VAL B 1 241 ? 45.785 102.883 78.911 1.00 12.31 ? 323 VAL B O 1 ATOM 4539 C CB . VAL B 1 241 ? 43.646 104.281 77.824 1.00 6.38 ? 323 VAL B CB 1 ATOM 4540 C CG1 . VAL B 1 241 ? 42.796 103.560 78.854 1.00 6.38 ? 323 VAL B CG1 1 ATOM 4541 C CG2 . VAL B 1 241 ? 42.789 105.248 77.028 1.00 6.38 ? 323 VAL B CG2 1 ATOM 4542 N N . TYR B 1 242 ? 46.392 104.555 80.290 1.00 10.88 ? 324 TYR B N 1 ATOM 4543 C CA . TYR B 1 242 ? 47.326 103.731 81.052 1.00 10.88 ? 324 TYR B CA 1 ATOM 4544 C C . TYR B 1 242 ? 46.856 103.231 82.424 1.00 10.88 ? 324 TYR B C 1 ATOM 4545 O O . TYR B 1 242 ? 47.626 102.595 83.152 1.00 10.88 ? 324 TYR B O 1 ATOM 4546 C CB . TYR B 1 242 ? 48.670 104.453 81.175 1.00 14.15 ? 324 TYR B CB 1 ATOM 4547 C CG . TYR B 1 242 ? 48.590 105.735 81.955 1.00 14.15 ? 324 TYR B CG 1 ATOM 4548 C CD1 . TYR B 1 242 ? 48.646 105.723 83.346 1.00 14.15 ? 324 TYR B CD1 1 ATOM 4549 C CD2 . TYR B 1 242 ? 48.441 106.960 81.309 1.00 14.15 ? 324 TYR B CD2 1 ATOM 4550 C CE1 . TYR B 1 242 ? 48.553 106.890 84.076 1.00 14.15 ? 324 TYR B CE1 1 ATOM 4551 C CE2 . TYR B 1 242 ? 48.346 108.143 82.033 1.00 14.15 ? 324 TYR B CE2 1 ATOM 4552 C CZ . TYR B 1 242 ? 48.404 108.095 83.418 1.00 14.15 ? 324 TYR B CZ 1 ATOM 4553 O OH . TYR B 1 242 ? 48.315 109.243 84.167 1.00 14.15 ? 324 TYR B OH 1 ATOM 4554 N N . ASN B 1 243 ? 45.644 103.607 82.819 1.00 3.85 ? 325 ASN B N 1 ATOM 4555 C CA . ASN B 1 243 ? 45.074 103.127 84.074 1.00 3.85 ? 325 ASN B CA 1 ATOM 4556 C C . ASN B 1 243 ? 43.607 102.754 83.851 1.00 3.85 ? 325 ASN B C 1 ATOM 4557 O O . ASN B 1 243 ? 43.040 103.046 82.796 1.00 3.85 ? 325 ASN B O 1 ATOM 4558 C CB . ASN B 1 243 ? 45.262 104.122 85.235 1.00 6.27 ? 325 ASN B CB 1 ATOM 4559 C CG . ASN B 1 243 ? 44.556 105.441 85.020 1.00 6.27 ? 325 ASN B CG 1 ATOM 4560 O OD1 . ASN B 1 243 ? 43.448 105.486 84.519 1.00 6.27 ? 325 ASN B OD1 1 ATOM 4561 N ND2 . ASN B 1 243 ? 45.188 106.524 85.445 1.00 6.27 ? 325 ASN B ND2 1 ATOM 4562 N N . GLU B 1 244 ? 43.005 102.082 84.827 1.00 7.65 ? 326 GLU B N 1 ATOM 4563 C CA . GLU B 1 244 ? 41.621 101.642 84.700 1.00 7.65 ? 326 GLU B CA 1 ATOM 4564 C C . GLU B 1 244 ? 40.559 102.742 84.678 1.00 7.65 ? 326 GLU B C 1 ATOM 4565 O O . GLU B 1 244 ? 39.534 102.598 84.008 1.00 7.65 ? 326 GLU B O 1 ATOM 4566 C CB . GLU B 1 244 ? 41.304 100.585 85.760 1.00 7.23 ? 326 GLU B CB 1 ATOM 4567 C CG . GLU B 1 244 ? 42.129 99.306 85.613 1.00 7.23 ? 326 GLU B CG 1 ATOM 4568 C CD . GLU B 1 244 ? 41.988 98.683 84.235 1.00 7.23 ? 326 GLU B CD 1 ATOM 4569 O OE1 . GLU B 1 244 ? 40.882 98.220 83.896 1.00 7.23 ? 326 GLU B OE1 1 ATOM 4570 O OE2 . GLU B 1 244 ? 42.980 98.666 83.478 1.00 7.23 ? 326 GLU B OE2 1 ATOM 4571 N N . LYS B 1 245 ? 40.800 103.834 85.399 1.00 4.37 ? 327 LYS B N 1 ATOM 4572 C CA . LYS B 1 245 ? 39.855 104.947 85.428 1.00 4.37 ? 327 LYS B CA 1 ATOM 4573 C C . LYS B 1 245 ? 39.706 105.537 84.026 1.00 4.37 ? 327 LYS B C 1 ATOM 4574 O O . LYS B 1 245 ? 38.592 105.753 83.550 1.00 4.37 ? 327 LYS B O 1 ATOM 4575 C CB . LYS B 1 245 ? 40.326 106.024 86.408 1.00 13.11 ? 327 LYS B CB 1 ATOM 4576 C CG . LYS B 1 245 ? 39.369 107.196 86.558 1.00 13.11 ? 327 LYS B CG 1 ATOM 4577 C CD . LYS B 1 245 ? 39.887 108.182 87.583 1.00 13.11 ? 327 LYS B CD 1 ATOM 4578 C CE . LYS B 1 245 ? 38.966 109.380 87.717 1.00 13.11 ? 327 LYS B CE 1 ATOM 4579 N NZ . LYS B 1 245 ? 39.468 110.336 88.748 1.00 13.11 ? 327 LYS B NZ 1 ATOM 4580 N N . LEU B 1 246 ? 40.838 105.780 83.369 1.00 7.78 ? 328 LEU B N 1 ATOM 4581 C CA . LEU B 1 246 ? 40.853 106.327 82.020 1.00 7.78 ? 328 LEU B CA 1 ATOM 4582 C C . LEU B 1 246 ? 40.187 105.359 81.050 1.00 7.78 ? 328 LEU B C 1 ATOM 4583 O O . LEU B 1 246 ? 39.544 105.776 80.088 1.00 7.78 ? 328 LEU B O 1 ATOM 4584 C CB . LEU B 1 246 ? 42.291 106.599 81.564 1.00 6.83 ? 328 LEU B CB 1 ATOM 4585 C CG . LEU B 1 246 ? 43.051 107.737 82.259 1.00 6.83 ? 328 LEU B CG 1 ATOM 4586 C CD1 . LEU B 1 246 ? 44.498 107.748 81.822 1.00 6.83 ? 328 LEU B CD1 1 ATOM 4587 C CD2 . LEU B 1 246 ? 42.390 109.072 81.958 1.00 6.83 ? 328 LEU B CD2 1 ATOM 4588 N N . TYR B 1 247 ? 40.361 104.065 81.300 1.00 7.56 ? 329 TYR B N 1 ATOM 4589 C CA . TYR B 1 247 ? 39.774 103.033 80.452 1.00 7.56 ? 329 TYR B CA 1 ATOM 4590 C C . TYR B 1 247 ? 38.239 103.029 80.499 1.00 7.56 ? 329 TYR B C 1 ATOM 4591 O O . TYR B 1 247 ? 37.585 103.102 79.454 1.00 7.56 ? 329 TYR B O 1 ATOM 4592 C CB . TYR B 1 247 ? 40.328 101.654 80.843 1.00 6.18 ? 329 TYR B CB 1 ATOM 4593 C CG . TYR B 1 247 ? 39.713 100.492 80.093 1.00 6.18 ? 329 TYR B CG 1 ATOM 4594 C CD1 . TYR B 1 247 ? 39.447 100.579 78.728 1.00 6.18 ? 329 TYR B CD1 1 ATOM 4595 C CD2 . TYR B 1 247 ? 39.365 99.319 80.755 1.00 6.18 ? 329 TYR B CD2 1 ATOM 4596 C CE1 . TYR B 1 247 ? 38.844 99.535 78.045 1.00 6.18 ? 329 TYR B CE1 1 ATOM 4597 C CE2 . TYR B 1 247 ? 38.758 98.263 80.079 1.00 6.18 ? 329 TYR B CE2 1 ATOM 4598 C CZ . TYR B 1 247 ? 38.502 98.378 78.726 1.00 6.18 ? 329 TYR B CZ 1 ATOM 4599 O OH . TYR B 1 247 ? 37.903 97.343 78.037 1.00 6.18 ? 329 TYR B OH 1 ATOM 4600 N N . ILE B 1 248 ? 37.663 102.952 81.699 1.00 9.78 ? 330 ILE B N 1 ATOM 4601 C CA . ILE B 1 248 ? 36.206 102.918 81.829 1.00 9.78 ? 330 ILE B CA 1 ATOM 4602 C C . ILE B 1 248 ? 35.526 104.206 81.362 1.00 9.78 ? 330 ILE B C 1 ATOM 4603 O O . ILE B 1 248 ? 34.417 104.166 80.830 1.00 9.78 ? 330 ILE B O 1 ATOM 4604 C CB . ILE B 1 248 ? 35.728 102.538 83.267 1.00 6.06 ? 330 ILE B CB 1 ATOM 4605 C CG1 . ILE B 1 248 ? 35.986 103.670 84.262 1.00 6.06 ? 330 ILE B CG1 1 ATOM 4606 C CG2 . ILE B 1 248 ? 36.420 101.264 83.725 1.00 6.06 ? 330 ILE B CG2 1 ATOM 4607 C CD1 . ILE B 1 248 ? 35.330 103.441 85.626 1.00 6.06 ? 330 ILE B CD1 1 ATOM 4608 N N . HIS B 1 249 ? 36.196 105.339 81.534 1.00 5.99 ? 331 HIS B N 1 ATOM 4609 C CA . HIS B 1 249 ? 35.633 106.609 81.098 1.00 5.99 ? 331 HIS B CA 1 ATOM 4610 C C . HIS B 1 249 ? 35.721 106.794 79.591 1.00 5.99 ? 331 HIS B C 1 ATOM 4611 O O . HIS B 1 249 ? 35.024 107.628 79.022 1.00 5.99 ? 331 HIS B O 1 ATOM 4612 C CB . HIS B 1 249 ? 36.280 107.778 81.831 1.00 7.13 ? 331 HIS B CB 1 ATOM 4613 C CG . HIS B 1 249 ? 35.782 107.938 83.230 1.00 7.13 ? 331 HIS B CG 1 ATOM 4614 N ND1 . HIS B 1 249 ? 34.676 108.697 83.540 1.00 7.13 ? 331 HIS B ND1 1 ATOM 4615 C CD2 . HIS B 1 249 ? 36.194 107.380 84.391 1.00 7.13 ? 331 HIS B CD2 1 ATOM 4616 C CE1 . HIS B 1 249 ? 34.422 108.596 84.832 1.00 7.13 ? 331 HIS B CE1 1 ATOM 4617 N NE2 . HIS B 1 249 ? 35.329 107.801 85.371 1.00 7.13 ? 331 HIS B NE2 1 ATOM 4618 N N . ALA B 1 250 ? 36.573 106.004 78.948 1.00 9.94 ? 332 ALA B N 1 ATOM 4619 C CA . ALA B 1 250 ? 36.726 106.067 77.503 1.00 9.94 ? 332 ALA B CA 1 ATOM 4620 C C . ALA B 1 250 ? 35.700 105.147 76.843 1.00 9.94 ? 332 ALA B C 1 ATOM 4621 O O . ALA B 1 250 ? 35.033 105.537 75.893 1.00 9.94 ? 332 ALA B O 1 ATOM 4622 C CB . ALA B 1 250 ? 38.138 105.650 77.099 1.00 5.98 ? 332 ALA B CB 1 ATOM 4623 N N . ILE B 1 251 ? 35.550 103.937 77.375 1.00 9.10 ? 333 ILE B N 1 ATOM 4624 C CA . ILE B 1 251 ? 34.627 102.971 76.803 1.00 9.10 ? 333 ILE B CA 1 ATOM 4625 C C . ILE B 1 251 ? 33.165 103.169 77.220 1.00 9.10 ? 333 ILE B C 1 ATOM 4626 O O . ILE B 1 251 ? 32.253 102.796 76.482 1.00 9.10 ? 333 ILE B O 1 ATOM 4627 C CB . ILE B 1 251 ? 35.115 101.516 77.066 1.00 18.77 ? 333 ILE B CB 1 ATOM 4628 C CG1 . ILE B 1 251 ? 34.432 100.542 76.107 1.00 18.77 ? 333 ILE B CG1 1 ATOM 4629 C CG2 . ILE B 1 251 ? 34.869 101.110 78.506 1.00 18.77 ? 333 ILE B CG2 1 ATOM 4630 C CD1 . ILE B 1 251 ? 34.972 99.125 76.166 1.00 18.77 ? 333 ILE B CD1 1 ATOM 4631 N N . GLY B 1 252 ? 32.948 103.825 78.358 1.00 8.23 ? 334 GLY B N 1 ATOM 4632 C CA . GLY B 1 252 ? 31.600 104.061 78.847 1.00 8.23 ? 334 GLY B CA 1 ATOM 4633 C C . GLY B 1 252 ? 30.696 104.739 77.829 1.00 8.23 ? 334 GLY B C 1 ATOM 4634 O O . GLY B 1 252 ? 29.642 104.201 77.474 1.00 8.23 ? 334 GLY B O 1 ATOM 4635 N N . PRO B 1 253 ? 31.052 105.955 77.385 1.00 12.52 ? 335 PRO B N 1 ATOM 4636 C CA . PRO B 1 253 ? 30.240 106.676 76.400 1.00 12.52 ? 335 PRO B CA 1 ATOM 4637 C C . PRO B 1 253 ? 30.097 105.938 75.066 1.00 12.52 ? 335 PRO B C 1 ATOM 4638 O O . PRO B 1 253 ? 29.084 106.087 74.379 1.00 12.52 ? 335 PRO B O 1 ATOM 4639 C CB . PRO B 1 253 ? 30.977 108.010 76.245 1.00 10.20 ? 335 PRO B CB 1 ATOM 4640 C CG . PRO B 1 253 ? 32.343 107.767 76.829 1.00 10.20 ? 335 PRO B CG 1 ATOM 4641 C CD . PRO B 1 253 ? 32.091 106.826 77.952 1.00 10.20 ? 335 PRO B CD 1 ATOM 4642 N N . LEU B 1 254 ? 31.095 105.131 74.710 1.00 9.05 ? 336 LEU B N 1 ATOM 4643 C CA . LEU B 1 254 ? 31.047 104.373 73.461 1.00 9.05 ? 336 LEU B CA 1 ATOM 4644 C C . LEU B 1 254 ? 29.980 103.283 73.538 1.00 9.05 ? 336 LEU B C 1 ATOM 4645 O O . LEU B 1 254 ? 29.309 102.994 72.544 1.00 9.05 ? 336 LEU B O 1 ATOM 4646 C CB . LEU B 1 254 ? 32.413 103.762 73.128 1.00 8.49 ? 336 LEU B CB 1 ATOM 4647 C CG . LEU B 1 254 ? 33.585 104.738 72.947 1.00 8.49 ? 336 LEU B CG 1 ATOM 4648 C CD1 . LEU B 1 254 ? 34.833 103.958 72.572 1.00 8.49 ? 336 LEU B CD1 1 ATOM 4649 C CD2 . LEU B 1 254 ? 33.264 105.781 71.877 1.00 8.49 ? 336 LEU B CD2 1 ATOM 4650 N N . LEU B 1 255 ? 29.818 102.682 74.715 1.00 7.84 ? 337 LEU B N 1 ATOM 4651 C CA . LEU B 1 255 ? 28.799 101.649 74.903 1.00 7.84 ? 337 LEU B CA 1 ATOM 4652 C C . LEU B 1 255 ? 27.432 102.295 74.687 1.00 7.84 ? 337 LEU B C 1 ATOM 4653 O O . LEU B 1 255 ? 26.559 101.726 74.025 1.00 7.84 ? 337 LEU B O 1 ATOM 4654 C CB . LEU B 1 255 ? 28.874 101.055 76.314 1.00 9.01 ? 337 LEU B CB 1 ATOM 4655 C CG . LEU B 1 255 ? 30.044 100.127 76.663 1.00 9.01 ? 337 LEU B CG 1 ATOM 4656 C CD1 . LEU B 1 255 ? 30.136 99.976 78.171 1.00 9.01 ? 337 LEU B CD1 1 ATOM 4657 C CD2 . LEU B 1 255 ? 29.870 98.768 75.994 1.00 9.01 ? 337 LEU B CD2 1 ATOM 4658 N N . ALA B 1 256 ? 27.270 103.505 75.223 1.00 13.62 ? 338 ALA B N 1 ATOM 4659 C CA . ALA B 1 256 ? 26.028 104.259 75.090 1.00 13.62 ? 338 ALA B CA 1 ATOM 4660 C C . ALA B 1 256 ? 25.740 104.524 73.616 1.00 13.62 ? 338 ALA B C 1 ATOM 4661 O O . ALA B 1 256 ? 24.600 104.394 73.168 1.00 13.62 ? 338 ALA B O 1 ATOM 4662 C CB . ALA B 1 256 ? 26.126 105.567 75.851 1.00 6.14 ? 338 ALA B CB 1 ATOM 4663 N N . ASN B 1 257 ? 26.783 104.859 72.860 1.00 15.09 ? 339 ASN B N 1 ATOM 4664 C CA . ASN B 1 257 ? 26.641 105.117 71.431 1.00 15.09 ? 339 ASN B CA 1 ATOM 4665 C C . ASN B 1 257 ? 26.187 103.873 70.684 1.00 15.09 ? 339 ASN B C 1 ATOM 4666 O O . ASN B 1 257 ? 25.558 103.972 69.634 1.00 15.09 ? 339 ASN B O 1 ATOM 4667 C CB . ASN B 1 257 ? 27.963 105.592 70.821 1.00 23.89 ? 339 ASN B CB 1 ATOM 4668 C CG . ASN B 1 257 ? 28.324 107.007 71.225 1.00 23.89 ? 339 ASN B CG 1 ATOM 4669 O OD1 . ASN B 1 257 ? 29.493 107.396 71.162 1.00 23.89 ? 339 ASN B OD1 1 ATOM 4670 N ND2 . ASN B 1 257 ? 27.326 107.793 71.624 1.00 23.89 ? 339 ASN B ND2 1 ATOM 4671 N N . HIS B 1 258 ? 26.494 102.702 71.236 1.00 13.74 ? 340 HIS B N 1 ATOM 4672 C CA . HIS B 1 258 ? 26.133 101.443 70.603 1.00 13.74 ? 340 HIS B CA 1 ATOM 4673 C C . HIS B 1 258 ? 24.895 100.732 71.137 1.00 13.74 ? 340 HIS B C 1 ATOM 4674 O O . HIS B 1 258 ? 24.677 99.559 70.838 1.00 13.74 ? 340 HIS B O 1 ATOM 4675 C CB . HIS B 1 258 ? 27.334 100.504 70.600 1.00 12.76 ? 340 HIS B CB 1 ATOM 4676 C CG . HIS B 1 258 ? 28.432 100.949 69.691 1.00 12.76 ? 340 HIS B CG 1 ATOM 4677 N ND1 . HIS B 1 258 ? 28.297 100.960 68.320 1.00 12.76 ? 340 HIS B ND1 1 ATOM 4678 C CD2 . HIS B 1 258 ? 29.673 101.423 69.952 1.00 12.76 ? 340 HIS B CD2 1 ATOM 4679 C CE1 . HIS B 1 258 ? 29.407 101.424 67.773 1.00 12.76 ? 340 HIS B CE1 1 ATOM 4680 N NE2 . HIS B 1 258 ? 30.257 101.712 68.742 1.00 12.76 ? 340 HIS B NE2 1 ATOM 4681 N N . GLY B 1 259 ? 24.092 101.426 71.937 1.00 12.56 ? 341 GLY B N 1 ATOM 4682 C CA . GLY B 1 259 ? 22.876 100.813 72.443 1.00 12.56 ? 341 GLY B CA 1 ATOM 4683 C C . GLY B 1 259 ? 22.829 100.385 73.896 1.00 12.56 ? 341 GLY B C 1 ATOM 4684 O O . GLY B 1 259 ? 21.760 100.022 74.389 1.00 12.56 ? 341 GLY B O 1 ATOM 4685 N N . TRP B 1 260 ? 23.973 100.378 74.577 1.00 14.47 ? 342 TRP B N 1 ATOM 4686 C CA . TRP B 1 260 ? 24.001 99.994 75.982 1.00 14.47 ? 342 TRP B CA 1 ATOM 4687 C C . TRP B 1 260 ? 24.227 101.223 76.857 1.00 14.47 ? 342 TRP B C 1 ATOM 4688 O O . TRP B 1 260 ? 25.365 101.607 77.138 1.00 14.47 ? 342 TRP B O 1 ATOM 4689 C CB . TRP B 1 260 ? 25.084 98.938 76.250 1.00 6.17 ? 342 TRP B CB 1 ATOM 4690 C CG . TRP B 1 260 ? 25.051 98.349 77.657 1.00 6.17 ? 342 TRP B CG 1 ATOM 4691 C CD1 . TRP B 1 260 ? 24.261 98.750 78.703 1.00 6.17 ? 342 TRP B CD1 1 ATOM 4692 C CD2 . TRP B 1 260 ? 25.828 97.247 78.147 1.00 6.17 ? 342 TRP B CD2 1 ATOM 4693 N NE1 . TRP B 1 260 ? 24.499 97.964 79.807 1.00 6.17 ? 342 TRP B NE1 1 ATOM 4694 C CE2 . TRP B 1 260 ? 25.455 97.034 79.494 1.00 6.17 ? 342 TRP B CE2 1 ATOM 4695 C CE3 . TRP B 1 260 ? 26.803 96.418 77.577 1.00 6.17 ? 342 TRP B CE3 1 ATOM 4696 C CZ2 . TRP B 1 260 ? 26.020 96.026 80.281 1.00 6.17 ? 342 TRP B CZ2 1 ATOM 4697 C CZ3 . TRP B 1 260 ? 27.366 95.415 78.360 1.00 6.17 ? 342 TRP B CZ3 1 ATOM 4698 C CH2 . TRP B 1 260 ? 26.971 95.230 79.698 1.00 6.17 ? 342 TRP B CH2 1 ATOM 4699 N N . SER B 1 261 ? 23.132 101.853 77.258 1.00 17.28 ? 343 SER B N 1 ATOM 4700 C CA . SER B 1 261 ? 23.198 103.020 78.121 1.00 17.28 ? 343 SER B CA 1 ATOM 4701 C C . SER B 1 261 ? 23.145 102.545 79.567 1.00 17.28 ? 343 SER B C 1 ATOM 4702 O O . SER B 1 261 ? 22.658 101.445 79.854 1.00 17.28 ? 343 SER B O 1 ATOM 4703 C CB . SER B 1 261 ? 22.023 103.961 77.847 1.00 35.11 ? 343 SER B CB 1 ATOM 4704 O OG . SER B 1 261 ? 22.113 104.523 76.553 1.00 35.11 ? 343 SER B OG 1 ATOM 4705 N N . ASN B 1 262 ? 23.675 103.362 80.470 1.00 10.26 ? 344 ASN B N 1 ATOM 4706 C CA . ASN B 1 262 ? 23.666 103.048 81.898 1.00 10.26 ? 344 ASN B CA 1 ATOM 4707 C C . ASN B 1 262 ? 24.476 101.819 82.288 1.00 10.26 ? 344 ASN B C 1 ATOM 4708 O O . ASN B 1 262 ? 24.063 101.038 83.150 1.00 10.26 ? 344 ASN B O 1 ATOM 4709 C CB . ASN B 1 262 ? 22.230 102.914 82.412 1.00 56.90 ? 344 ASN B CB 1 ATOM 4710 C CG . ASN B 1 262 ? 21.452 104.202 82.285 1.00 56.90 ? 344 ASN B CG 1 ATOM 4711 O OD1 . ASN B 1 262 ? 21.821 105.221 82.873 1.00 56.90 ? 344 ASN B OD1 1 ATOM 4712 N ND2 . ASN B 1 262 ? 20.376 104.172 81.502 1.00 56.90 ? 344 ASN B ND2 1 ATOM 4713 N N . ALA B 1 263 ? 25.613 101.632 81.628 1.00 7.63 ? 345 ALA B N 1 ATOM 4714 C CA . ALA B 1 263 ? 26.495 100.518 81.951 1.00 7.63 ? 345 ALA B CA 1 ATOM 4715 C C . ALA B 1 263 ? 27.454 101.023 83.028 1.00 7.63 ? 345 ALA B C 1 ATOM 4716 O O . ALA B 1 263 ? 27.980 102.133 82.927 1.00 7.63 ? 345 ALA B O 1 ATOM 4717 C CB . ALA B 1 263 ? 27.272 100.082 80.719 1.00 3.79 ? 345 ALA B CB 1 ATOM 4718 N N . PHE B 1 264 ? 27.616 100.239 84.090 1.00 6.60 ? 346 PHE B N 1 ATOM 4719 C CA . PHE B 1 264 ? 28.516 100.593 85.172 1.00 6.60 ? 346 PHE B CA 1 ATOM 4720 C C . PHE B 1 264 ? 29.640 99.576 85.258 1.00 6.60 ? 346 PHE B C 1 ATOM 4721 O O . PHE B 1 264 ? 29.593 98.541 84.597 1.00 6.60 ? 346 PHE B O 1 ATOM 4722 C CB . PHE B 1 264 ? 27.759 100.739 86.485 1.00 7.91 ? 346 PHE B CB 1 ATOM 4723 C CG . PHE B 1 264 ? 26.880 101.953 86.527 1.00 7.91 ? 346 PHE B CG 1 ATOM 4724 C CD1 . PHE B 1 264 ? 25.574 101.898 86.049 1.00 7.91 ? 346 PHE B CD1 1 ATOM 4725 C CD2 . PHE B 1 264 ? 27.371 103.169 87.002 1.00 7.91 ? 346 PHE B CD2 1 ATOM 4726 C CE1 . PHE B 1 264 ? 24.766 103.036 86.039 1.00 7.91 ? 346 PHE B CE1 1 ATOM 4727 C CE2 . PHE B 1 264 ? 26.571 104.311 86.998 1.00 7.91 ? 346 PHE B CE2 1 ATOM 4728 C CZ . PHE B 1 264 ? 25.266 104.244 86.511 1.00 7.91 ? 346 PHE B CZ 1 ATOM 4729 N N . PHE B 1 265 ? 30.645 99.862 86.084 1.00 6.41 ? 347 PHE B N 1 ATOM 4730 C CA . PHE B 1 265 ? 31.812 98.994 86.176 1.00 6.41 ? 347 PHE B CA 1 ATOM 4731 C C . PHE B 1 265 ? 32.299 98.649 87.575 1.00 6.41 ? 347 PHE B C 1 ATOM 4732 O O . PHE B 1 265 ? 31.949 99.306 88.551 1.00 6.41 ? 347 PHE B O 1 ATOM 4733 C CB . PHE B 1 265 ? 32.995 99.680 85.472 1.00 5.39 ? 347 PHE B CB 1 ATOM 4734 C CG . PHE B 1 265 ? 32.709 100.137 84.068 1.00 5.39 ? 347 PHE B CG 1 ATOM 4735 C CD1 . PHE B 1 265 ? 31.933 101.271 83.829 1.00 5.39 ? 347 PHE B CD1 1 ATOM 4736 C CD2 . PHE B 1 265 ? 33.246 99.455 82.984 1.00 5.39 ? 347 PHE B CD2 1 ATOM 4737 C CE1 . PHE B 1 265 ? 31.697 101.716 82.530 1.00 5.39 ? 347 PHE B CE1 1 ATOM 4738 C CE2 . PHE B 1 265 ? 33.017 99.894 81.679 1.00 5.39 ? 347 PHE B CE2 1 ATOM 4739 C CZ . PHE B 1 265 ? 32.242 101.027 81.455 1.00 5.39 ? 347 PHE B CZ 1 ATOM 4740 N N . ILE B 1 266 ? 33.104 97.588 87.647 1.00 4.23 ? 348 ILE B N 1 ATOM 4741 C CA . ILE B 1 266 ? 33.787 97.170 88.875 1.00 4.23 ? 348 ILE B CA 1 ATOM 4742 C C . ILE B 1 266 ? 35.202 96.884 88.389 1.00 4.23 ? 348 ILE B C 1 ATOM 4743 O O . ILE B 1 266 ? 35.399 96.500 87.230 1.00 4.23 ? 348 ILE B O 1 ATOM 4744 C CB . ILE B 1 266 ? 33.190 95.934 89.591 1.00 2.00 ? 348 ILE B CB 1 ATOM 4745 C CG1 . ILE B 1 266 ? 33.120 94.722 88.666 1.00 2.00 ? 348 ILE B CG1 1 ATOM 4746 C CG2 . ILE B 1 266 ? 31.857 96.282 90.209 1.00 2.00 ? 348 ILE B CG2 1 ATOM 4747 C CD1 . ILE B 1 266 ? 32.688 93.452 89.389 1.00 2.00 ? 348 ILE B CD1 1 ATOM 4748 N N . THR B 1 267 ? 36.190 97.139 89.239 1.00 4.23 ? 349 THR B N 1 ATOM 4749 C CA . THR B 1 267 ? 37.583 96.945 88.856 1.00 4.23 ? 349 THR B CA 1 ATOM 4750 C C . THR B 1 267 ? 38.384 96.189 89.899 1.00 4.23 ? 349 THR B C 1 ATOM 4751 O O . THR B 1 267 ? 38.344 96.522 91.080 1.00 4.23 ? 349 THR B O 1 ATOM 4752 C CB . THR B 1 267 ? 38.265 98.306 88.595 1.00 18.85 ? 349 THR B CB 1 ATOM 4753 O OG1 . THR B 1 267 ? 37.560 98.996 87.558 1.00 18.85 ? 349 THR B OG1 1 ATOM 4754 C CG2 . THR B 1 267 ? 39.700 98.123 88.158 1.00 18.85 ? 349 THR B CG2 1 ATOM 4755 N N . ASP B 1 268 ? 39.124 95.183 89.447 1.00 2.00 ? 350 ASP B N 1 ATOM 4756 C CA . ASP B 1 268 ? 39.959 94.372 90.326 1.00 2.00 ? 350 ASP B CA 1 ATOM 4757 C C . ASP B 1 268 ? 41.190 95.191 90.750 1.00 2.00 ? 350 ASP B C 1 ATOM 4758 O O . ASP B 1 268 ? 41.866 95.789 89.911 1.00 2.00 ? 350 ASP B O 1 ATOM 4759 C CB . ASP B 1 268 ? 40.397 93.096 89.584 1.00 2.00 ? 350 ASP B CB 1 ATOM 4760 C CG . ASP B 1 268 ? 40.898 91.993 90.518 1.00 2.00 ? 350 ASP B CG 1 ATOM 4761 O OD1 . ASP B 1 268 ? 41.105 92.249 91.721 1.00 2.00 ? 350 ASP B OD1 1 ATOM 4762 O OD2 . ASP B 1 268 ? 41.084 90.852 90.041 1.00 2.00 ? 350 ASP B OD2 1 ATOM 4763 N N . GLN B 1 269 ? 41.452 95.249 92.053 1.00 2.00 ? 351 GLN B N 1 ATOM 4764 C CA . GLN B 1 269 ? 42.612 95.971 92.579 1.00 2.00 ? 351 GLN B CA 1 ATOM 4765 C C . GLN B 1 269 ? 43.373 95.104 93.579 1.00 2.00 ? 351 GLN B C 1 ATOM 4766 O O . GLN B 1 269 ? 44.284 95.582 94.250 1.00 2.00 ? 351 GLN B O 1 ATOM 4767 C CB . GLN B 1 269 ? 42.198 97.291 93.255 1.00 6.72 ? 351 GLN B CB 1 ATOM 4768 C CG . GLN B 1 269 ? 41.785 98.415 92.305 1.00 6.72 ? 351 GLN B CG 1 ATOM 4769 C CD . GLN B 1 269 ? 42.921 98.896 91.407 1.00 6.72 ? 351 GLN B CD 1 ATOM 4770 O OE1 . GLN B 1 269 ? 43.761 99.694 91.823 1.00 6.72 ? 351 GLN B OE1 1 ATOM 4771 N NE2 . GLN B 1 269 ? 42.940 98.423 90.164 1.00 6.72 ? 351 GLN B NE2 1 ATOM 4772 N N . GLY B 1 270 ? 43.014 93.822 93.641 1.00 4.35 ? 352 GLY B N 1 ATOM 4773 C CA . GLY B 1 270 ? 43.642 92.884 94.557 1.00 4.35 ? 352 GLY B CA 1 ATOM 4774 C C . GLY B 1 270 ? 45.151 92.747 94.471 1.00 4.35 ? 352 GLY B C 1 ATOM 4775 O O . GLY B 1 270 ? 45.795 92.398 95.459 1.00 4.35 ? 352 GLY B O 1 ATOM 4776 N N . ARG B 1 271 ? 45.722 93.001 93.297 1.00 5.02 ? 353 ARG B N 1 ATOM 4777 C CA . ARG B 1 271 ? 47.169 92.905 93.123 1.00 5.02 ? 353 ARG B CA 1 ATOM 4778 C C . ARG B 1 271 ? 47.713 94.157 92.433 1.00 5.02 ? 353 ARG B C 1 ATOM 4779 O O . ARG B 1 271 ? 48.704 94.094 91.708 1.00 5.02 ? 353 ARG B O 1 ATOM 4780 C CB . ARG B 1 271 ? 47.530 91.635 92.330 1.00 7.04 ? 353 ARG B CB 1 ATOM 4781 C CG . ARG B 1 271 ? 47.063 90.336 93.005 1.00 7.04 ? 353 ARG B CG 1 ATOM 4782 C CD . ARG B 1 271 ? 47.635 89.082 92.361 1.00 7.04 ? 353 ARG B CD 1 ATOM 4783 N NE . ARG B 1 271 ? 47.145 88.857 91.001 1.00 7.04 ? 353 ARG B NE 1 ATOM 4784 C CZ . ARG B 1 271 ? 47.487 87.819 90.246 1.00 7.04 ? 353 ARG B CZ 1 ATOM 4785 N NH1 . ARG B 1 271 ? 48.321 86.899 90.710 1.00 7.04 ? 353 ARG B NH1 1 ATOM 4786 N NH2 . ARG B 1 271 ? 46.998 87.696 89.024 1.00 7.04 ? 353 ARG B NH2 1 ATOM 4787 N N . SER B 1 272 ? 47.100 95.304 92.725 1.00 3.23 ? 354 SER B N 1 ATOM 4788 C CA . SER B 1 272 ? 47.485 96.578 92.114 1.00 3.23 ? 354 SER B CA 1 ATOM 4789 C C . SER B 1 272 ? 48.113 97.620 93.044 1.00 3.23 ? 354 SER B C 1 ATOM 4790 O O . SER B 1 272 ? 48.444 98.718 92.595 1.00 3.23 ? 354 SER B O 1 ATOM 4791 C CB . SER B 1 272 ? 46.268 97.209 91.429 1.00 3.09 ? 354 SER B CB 1 ATOM 4792 O OG . SER B 1 272 ? 45.709 96.342 90.463 1.00 3.09 ? 354 SER B OG 1 ATOM 4793 N N . GLY B 1 273 ? 48.311 97.260 94.311 1.00 7.81 ? 355 GLY B N 1 ATOM 4794 C CA . GLY B 1 273 ? 48.869 98.178 95.297 1.00 7.81 ? 355 GLY B CA 1 ATOM 4795 C C . GLY B 1 273 ? 50.225 98.801 95.027 1.00 7.81 ? 355 GLY B C 1 ATOM 4796 O O . GLY B 1 273 ? 50.477 99.942 95.429 1.00 7.81 ? 355 GLY B O 1 ATOM 4797 N N . LYS B 1 274 ? 51.111 98.067 94.362 1.00 6.97 ? 356 LYS B N 1 ATOM 4798 C CA . LYS B 1 274 ? 52.435 98.599 94.065 1.00 6.97 ? 356 LYS B CA 1 ATOM 4799 C C . LYS B 1 274 ? 52.531 98.993 92.602 1.00 6.97 ? 356 LYS B C 1 ATOM 4800 O O . LYS B 1 274 ? 52.399 98.153 91.711 1.00 6.97 ? 356 LYS B O 1 ATOM 4801 C CB . LYS B 1 274 ? 53.519 97.580 94.410 1.00 19.76 ? 356 LYS B CB 1 ATOM 4802 C CG . LYS B 1 274 ? 54.905 98.179 94.491 1.00 19.76 ? 356 LYS B CG 1 ATOM 4803 C CD . LYS B 1 274 ? 55.923 97.126 94.844 1.00 19.76 ? 356 LYS B CD 1 ATOM 4804 C CE . LYS B 1 274 ? 57.231 97.753 95.288 1.00 19.76 ? 356 LYS B CE 1 ATOM 4805 N NZ . LYS B 1 274 ? 57.851 98.596 94.231 1.00 19.76 ? 356 LYS B NZ 1 ATOM 4806 N N . GLN B 1 275 ? 52.760 100.280 92.367 1.00 11.15 ? 357 GLN B N 1 ATOM 4807 C CA . GLN B 1 275 ? 52.866 100.821 91.019 1.00 11.15 ? 357 GLN B CA 1 ATOM 4808 C C . GLN B 1 275 ? 54.116 101.688 90.883 1.00 11.15 ? 357 GLN B C 1 ATOM 4809 O O . GLN B 1 275 ? 54.411 102.502 91.757 1.00 11.15 ? 357 GLN B O 1 ATOM 4810 C CB . GLN B 1 275 ? 51.632 101.664 90.696 1.00 6.24 ? 357 GLN B CB 1 ATOM 4811 C CG . GLN B 1 275 ? 50.310 100.912 90.759 1.00 6.24 ? 357 GLN B CG 1 ATOM 4812 C CD . GLN B 1 275 ? 50.156 99.894 89.643 1.00 6.24 ? 357 GLN B CD 1 ATOM 4813 O OE1 . GLN B 1 275 ? 50.778 100.010 88.586 1.00 6.24 ? 357 GLN B OE1 1 ATOM 4814 N NE2 . GLN B 1 275 ? 49.308 98.902 89.867 1.00 6.24 ? 357 GLN B NE2 1 ATOM 4815 N N . PRO B 1 276 ? 54.894 101.487 89.809 1.00 11.32 ? 358 PRO B N 1 ATOM 4816 C CA . PRO B 1 276 ? 54.640 100.490 88.767 1.00 11.32 ? 358 PRO B CA 1 ATOM 4817 C C . PRO B 1 276 ? 54.985 99.102 89.274 1.00 11.32 ? 358 PRO B C 1 ATOM 4818 O O . PRO B 1 276 ? 55.663 98.956 90.289 1.00 11.32 ? 358 PRO B O 1 ATOM 4819 C CB . PRO B 1 276 ? 55.586 100.921 87.647 1.00 14.81 ? 358 PRO B CB 1 ATOM 4820 C CG . PRO B 1 276 ? 56.727 101.524 88.380 1.00 14.81 ? 358 PRO B CG 1 ATOM 4821 C CD . PRO B 1 276 ? 56.052 102.329 89.457 1.00 14.81 ? 358 PRO B CD 1 ATOM 4822 N N . THR B 1 277 ? 54.486 98.083 88.589 1.00 14.08 ? 359 THR B N 1 ATOM 4823 C CA . THR B 1 277 ? 54.762 96.710 88.981 1.00 14.08 ? 359 THR B CA 1 ATOM 4824 C C . THR B 1 277 ? 56.135 96.290 88.442 1.00 14.08 ? 359 THR B C 1 ATOM 4825 O O . THR B 1 277 ? 56.880 97.120 87.917 1.00 14.08 ? 359 THR B O 1 ATOM 4826 C CB . THR B 1 277 ? 53.696 95.762 88.410 1.00 5.87 ? 359 THR B CB 1 ATOM 4827 O OG1 . THR B 1 277 ? 53.870 95.666 86.992 1.00 5.87 ? 359 THR B OG1 1 ATOM 4828 C CG2 . THR B 1 277 ? 52.294 96.294 88.699 1.00 5.87 ? 359 THR B CG2 1 ATOM 4829 N N . GLY B 1 278 ? 56.457 95.005 88.571 1.00 10.52 ? 360 GLY B N 1 ATOM 4830 C CA . GLY B 1 278 ? 57.721 94.498 88.068 1.00 10.52 ? 360 GLY B CA 1 ATOM 4831 C C . GLY B 1 278 ? 57.606 93.966 86.648 1.00 10.52 ? 360 GLY B C 1 ATOM 4832 O O . GLY B 1 278 ? 58.505 93.274 86.166 1.00 10.52 ? 360 GLY B O 1 ATOM 4833 N N . GLN B 1 279 ? 56.501 94.285 85.977 1.00 6.51 ? 361 GLN B N 1 ATOM 4834 C CA . GLN B 1 279 ? 56.274 93.837 84.602 1.00 6.51 ? 361 GLN B CA 1 ATOM 4835 C C . GLN B 1 279 ? 57.290 94.441 83.645 1.00 6.51 ? 361 GLN B C 1 ATOM 4836 O O . GLN B 1 279 ? 57.493 95.652 83.629 1.00 6.51 ? 361 GLN B O 1 ATOM 4837 C CB . GLN B 1 279 ? 54.868 94.222 84.126 1.00 10.95 ? 361 GLN B CB 1 ATOM 4838 C CG . GLN B 1 279 ? 53.760 93.307 84.608 1.00 10.95 ? 361 GLN B CG 1 ATOM 4839 C CD . GLN B 1 279 ? 52.374 93.875 84.353 1.00 10.95 ? 361 GLN B CD 1 ATOM 4840 O OE1 . GLN B 1 279 ? 51.549 93.256 83.677 1.00 10.95 ? 361 GLN B OE1 1 ATOM 4841 N NE2 . GLN B 1 279 ? 52.109 95.056 84.899 1.00 10.95 ? 361 GLN B NE2 1 ATOM 4842 N N . GLN B 1 280 ? 57.959 93.590 82.880 1.00 16.70 ? 362 GLN B N 1 ATOM 4843 C CA . GLN B 1 280 ? 58.926 94.059 81.901 1.00 16.70 ? 362 GLN B CA 1 ATOM 4844 C C . GLN B 1 280 ? 58.154 94.442 80.641 1.00 16.70 ? 362 GLN B C 1 ATOM 4845 O O . GLN B 1 280 ? 58.555 95.330 79.893 1.00 16.70 ? 362 GLN B O 1 ATOM 4846 C CB . GLN B 1 280 ? 59.994 92.991 81.648 1.00 44.99 ? 362 GLN B CB 1 ATOM 4847 C CG . GLN B 1 280 ? 61.087 93.013 82.727 1.00 44.99 ? 362 GLN B CG 1 ATOM 4848 C CD . GLN B 1 280 ? 61.825 91.693 82.894 1.00 44.99 ? 362 GLN B CD 1 ATOM 4849 O OE1 . GLN B 1 280 ? 62.020 90.943 81.933 1.00 44.99 ? 362 GLN B OE1 1 ATOM 4850 N NE2 . GLN B 1 280 ? 62.243 91.406 84.128 1.00 44.99 ? 362 GLN B NE2 1 ATOM 4851 N N . GLN B 1 281 ? 56.996 93.812 80.467 1.00 10.54 ? 363 GLN B N 1 ATOM 4852 C CA . GLN B 1 281 ? 56.105 94.083 79.344 1.00 10.54 ? 363 GLN B CA 1 ATOM 4853 C C . GLN B 1 281 ? 54.675 94.028 79.867 1.00 10.54 ? 363 GLN B C 1 ATOM 4854 O O . GLN B 1 281 ? 54.365 93.224 80.740 1.00 10.54 ? 363 GLN B O 1 ATOM 4855 C CB . GLN B 1 281 ? 56.323 93.081 78.209 1.00 110.20 ? 363 GLN B CB 1 ATOM 4856 C CG . GLN B 1 281 ? 57.630 93.313 77.467 1.00 110.20 ? 363 GLN B CG 1 ATOM 4857 C CD . GLN B 1 281 ? 57.845 92.367 76.307 1.00 110.20 ? 363 GLN B CD 1 ATOM 4858 O OE1 . GLN B 1 281 ? 56.932 91.657 75.883 1.00 110.20 ? 363 GLN B OE1 1 ATOM 4859 N NE2 . GLN B 1 281 ? 59.064 92.356 75.781 1.00 110.20 ? 363 GLN B NE2 1 ATOM 4860 N N . TRP B 1 282 ? 53.820 94.908 79.354 1.00 8.92 ? 364 TRP B N 1 ATOM 4861 C CA . TRP B 1 282 ? 52.421 94.986 79.780 1.00 8.92 ? 364 TRP B CA 1 ATOM 4862 C C . TRP B 1 282 ? 51.661 93.669 79.609 1.00 8.92 ? 364 TRP B C 1 ATOM 4863 O O . TRP B 1 282 ? 50.769 93.353 80.394 1.00 8.92 ? 364 TRP B O 1 ATOM 4864 C CB . TRP B 1 282 ? 51.703 96.100 79.009 1.00 6.90 ? 364 TRP B CB 1 ATOM 4865 C CG . TRP B 1 282 ? 50.623 96.817 79.782 1.00 6.90 ? 364 TRP B CG 1 ATOM 4866 C CD1 . TRP B 1 282 ? 50.141 96.502 81.031 1.00 6.90 ? 364 TRP B CD1 1 ATOM 4867 C CD2 . TRP B 1 282 ? 49.924 97.999 79.371 1.00 6.90 ? 364 TRP B CD2 1 ATOM 4868 N NE1 . TRP B 1 282 ? 49.197 97.422 81.419 1.00 6.90 ? 364 TRP B NE1 1 ATOM 4869 C CE2 . TRP B 1 282 ? 49.040 98.351 80.422 1.00 6.90 ? 364 TRP B CE2 1 ATOM 4870 C CE3 . TRP B 1 282 ? 49.961 98.799 78.220 1.00 6.90 ? 364 TRP B CE3 1 ATOM 4871 C CZ2 . TRP B 1 282 ? 48.202 99.473 80.352 1.00 6.90 ? 364 TRP B CZ2 1 ATOM 4872 C CZ3 . TRP B 1 282 ? 49.125 99.915 78.151 1.00 6.90 ? 364 TRP B CZ3 1 ATOM 4873 C CH2 . TRP B 1 282 ? 48.258 100.240 79.213 1.00 6.90 ? 364 TRP B CH2 1 ATOM 4874 N N . GLY B 1 283 ? 52.037 92.897 78.596 1.00 11.48 ? 365 GLY B N 1 ATOM 4875 C CA . GLY B 1 283 ? 51.375 91.632 78.332 1.00 11.48 ? 365 GLY B CA 1 ATOM 4876 C C . GLY B 1 283 ? 51.703 90.491 79.277 1.00 11.48 ? 365 GLY B C 1 ATOM 4877 O O . GLY B 1 283 ? 51.091 89.428 79.186 1.00 11.48 ? 365 GLY B O 1 ATOM 4878 N N . ASP B 1 284 ? 52.681 90.691 80.159 1.00 16.97 ? 366 ASP B N 1 ATOM 4879 C CA . ASP B 1 284 ? 53.079 89.668 81.129 1.00 16.97 ? 366 ASP B CA 1 ATOM 4880 C C . ASP B 1 284 ? 52.043 89.599 82.257 1.00 16.97 ? 366 ASP B C 1 ATOM 4881 O O . ASP B 1 284 ? 51.866 90.555 83.014 1.00 16.97 ? 366 ASP B O 1 ATOM 4882 C CB . ASP B 1 284 ? 54.481 89.981 81.664 1.00 12.95 ? 366 ASP B CB 1 ATOM 4883 C CG . ASP B 1 284 ? 55.545 89.976 80.561 1.00 12.95 ? 366 ASP B CG 1 ATOM 4884 O OD1 . ASP B 1 284 ? 55.265 89.473 79.452 1.00 12.95 ? 366 ASP B OD1 1 ATOM 4885 O OD2 . ASP B 1 284 ? 56.668 90.468 80.798 1.00 12.95 ? 366 ASP B OD2 1 ATOM 4886 N N . TRP B 1 285 ? 51.390 88.446 82.381 1.00 7.55 ? 367 TRP B N 1 ATOM 4887 C CA . TRP B 1 285 ? 50.319 88.245 83.360 1.00 7.55 ? 367 TRP B CA 1 ATOM 4888 C C . TRP B 1 285 ? 50.527 87.179 84.437 1.00 7.55 ? 367 TRP B C 1 ATOM 4889 O O . TRP B 1 285 ? 49.802 87.160 85.438 1.00 7.55 ? 367 TRP B O 1 ATOM 4890 C CB . TRP B 1 285 ? 49.038 87.884 82.601 1.00 12.79 ? 367 TRP B CB 1 ATOM 4891 C CG . TRP B 1 285 ? 49.233 86.664 81.724 1.00 12.79 ? 367 TRP B CG 1 ATOM 4892 C CD1 . TRP B 1 285 ? 49.625 86.657 80.417 1.00 12.79 ? 367 TRP B CD1 1 ATOM 4893 C CD2 . TRP B 1 285 ? 49.124 85.280 82.119 1.00 12.79 ? 367 TRP B CD2 1 ATOM 4894 N NE1 . TRP B 1 285 ? 49.776 85.364 79.974 1.00 12.79 ? 367 TRP B NE1 1 ATOM 4895 C CE2 . TRP B 1 285 ? 49.476 84.500 80.992 1.00 12.79 ? 367 TRP B CE2 1 ATOM 4896 C CE3 . TRP B 1 285 ? 48.769 84.627 83.310 1.00 12.79 ? 367 TRP B CE3 1 ATOM 4897 C CZ2 . TRP B 1 285 ? 49.486 83.096 81.023 1.00 12.79 ? 367 TRP B CZ2 1 ATOM 4898 C CZ3 . TRP B 1 285 ? 48.778 83.228 83.339 1.00 12.79 ? 367 TRP B CZ3 1 ATOM 4899 C CH2 . TRP B 1 285 ? 49.136 82.481 82.198 1.00 12.79 ? 367 TRP B CH2 1 ATOM 4900 N N . CYS B 1 286 ? 51.468 86.267 84.222 1.00 8.50 ? 368 CYS B N 1 ATOM 4901 C CA . CYS B 1 286 ? 51.686 85.177 85.172 1.00 8.50 ? 368 CYS B CA 1 ATOM 4902 C C . CYS B 1 286 ? 52.575 85.450 86.376 1.00 8.50 ? 368 CYS B C 1 ATOM 4903 O O . CYS B 1 286 ? 53.769 85.710 86.226 1.00 8.50 ? 368 CYS B O 1 ATOM 4904 C CB . CYS B 1 286 ? 52.192 83.931 84.447 1.00 10.00 ? 368 CYS B CB 1 ATOM 4905 S SG . CYS B 1 286 ? 52.042 82.434 85.457 1.00 10.00 ? 368 CYS B SG 1 ATOM 4906 N N . ASN B 1 287 ? 51.979 85.342 87.567 1.00 8.16 ? 369 ASN B N 1 ATOM 4907 C CA . ASN B 1 287 ? 52.661 85.539 88.853 1.00 8.16 ? 369 ASN B CA 1 ATOM 4908 C C . ASN B 1 287 ? 53.689 86.665 88.810 1.00 8.16 ? 369 ASN B C 1 ATOM 4909 O O . ASN B 1 287 ? 54.837 86.482 89.221 1.00 8.16 ? 369 ASN B O 1 ATOM 4910 C CB . ASN B 1 287 ? 53.356 84.241 89.294 1.00 8.86 ? 369 ASN B CB 1 ATOM 4911 C CG . ASN B 1 287 ? 52.441 83.023 89.233 1.00 8.86 ? 369 ASN B CG 1 ATOM 4912 O OD1 . ASN B 1 287 ? 51.316 83.047 89.727 1.00 8.86 ? 369 ASN B OD1 1 ATOM 4913 N ND2 . ASN B 1 287 ? 52.936 81.943 88.647 1.00 8.86 ? 369 ASN B ND2 1 ATOM 4914 N N . VAL B 1 288 ? 53.265 87.833 88.341 1.00 8.74 ? 370 VAL B N 1 ATOM 4915 C CA . VAL B 1 288 ? 54.146 88.990 88.214 1.00 8.74 ? 370 VAL B CA 1 ATOM 4916 C C . VAL B 1 288 ? 54.805 89.439 89.515 1.00 8.74 ? 370 VAL B C 1 ATOM 4917 O O . VAL B 1 288 ? 54.153 89.559 90.548 1.00 8.74 ? 370 VAL B O 1 ATOM 4918 C CB . VAL B 1 288 ? 53.410 90.168 87.541 1.00 4.03 ? 370 VAL B CB 1 ATOM 4919 C CG1 . VAL B 1 288 ? 54.281 91.411 87.522 1.00 4.03 ? 370 VAL B CG1 1 ATOM 4920 C CG2 . VAL B 1 288 ? 53.028 89.780 86.118 1.00 4.03 ? 370 VAL B CG2 1 ATOM 4921 N N . ILE B 1 289 ? 56.114 89.667 89.450 1.00 6.40 ? 371 ILE B N 1 ATOM 4922 C CA . ILE B 1 289 ? 56.892 90.102 90.606 1.00 6.40 ? 371 ILE B CA 1 ATOM 4923 C C . ILE B 1 289 ? 56.698 91.591 90.872 1.00 6.40 ? 371 ILE B C 1 ATOM 4924 O O . ILE B 1 289 ? 56.323 92.340 89.977 1.00 6.40 ? 371 ILE B O 1 ATOM 4925 C CB . ILE B 1 289 ? 58.409 89.853 90.391 1.00 22.22 ? 371 ILE B CB 1 ATOM 4926 C CG1 . ILE B 1 289 ? 58.902 90.628 89.163 1.00 22.22 ? 371 ILE B CG1 1 ATOM 4927 C CG2 . ILE B 1 289 ? 58.689 88.361 90.243 1.00 22.22 ? 371 ILE B CG2 1 ATOM 4928 C CD1 . ILE B 1 289 ? 60.399 90.573 88.942 1.00 22.22 ? 371 ILE B CD1 1 ATOM 4929 N N . GLY B 1 290 ? 56.971 92.014 92.103 1.00 5.61 ? 372 GLY B N 1 ATOM 4930 C CA . GLY B 1 290 ? 56.848 93.417 92.458 1.00 5.61 ? 372 GLY B CA 1 ATOM 4931 C C . GLY B 1 290 ? 55.434 93.948 92.569 1.00 5.61 ? 372 GLY B C 1 ATOM 4932 O O . GLY B 1 290 ? 55.173 95.113 92.248 1.00 5.61 ? 372 GLY B O 1 ATOM 4933 N N . THR B 1 291 ? 54.521 93.098 93.032 1.00 5.09 ? 373 THR B N 1 ATOM 4934 C CA . THR B 1 291 ? 53.127 93.492 93.198 1.00 5.09 ? 373 THR B CA 1 ATOM 4935 C C . THR B 1 291 ? 52.721 93.429 94.667 1.00 5.09 ? 373 THR B C 1 ATOM 4936 O O . THR B 1 291 ? 53.422 92.849 95.493 1.00 5.09 ? 373 THR B O 1 ATOM 4937 C CB . THR B 1 291 ? 52.186 92.586 92.382 1.00 4.17 ? 373 THR B CB 1 ATOM 4938 O OG1 . THR B 1 291 ? 52.296 91.235 92.851 1.00 4.17 ? 373 THR B OG1 1 ATOM 4939 C CG2 . THR B 1 291 ? 52.546 92.642 90.899 1.00 4.17 ? 373 THR B CG2 1 ATOM 4940 N N . GLY B 1 292 ? 51.589 94.042 94.988 1.00 7.05 ? 374 GLY B N 1 ATOM 4941 C CA . GLY B 1 292 ? 51.104 94.029 96.355 1.00 7.05 ? 374 GLY B CA 1 ATOM 4942 C C . GLY B 1 292 ? 49.596 94.182 96.390 1.00 7.05 ? 374 GLY B C 1 ATOM 4943 O O . GLY B 1 292 ? 48.980 94.541 95.379 1.00 7.05 ? 374 GLY B O 1 ATOM 4944 N N . PHE B 1 293 ? 48.994 93.850 97.529 1.00 6.28 ? 375 PHE B N 1 ATOM 4945 C CA . PHE B 1 293 ? 47.554 93.990 97.691 1.00 6.28 ? 375 PHE B CA 1 ATOM 4946 C C . PHE B 1 293 ? 47.239 95.473 97.492 1.00 6.28 ? 375 PHE B C 1 ATOM 4947 O O . PHE B 1 293 ? 48.010 96.340 97.921 1.00 6.28 ? 375 PHE B O 1 ATOM 4948 C CB . PHE B 1 293 ? 47.127 93.545 99.091 1.00 3.91 ? 375 PHE B CB 1 ATOM 4949 C CG . PHE B 1 293 ? 47.152 92.050 99.298 1.00 3.91 ? 375 PHE B CG 1 ATOM 4950 C CD1 . PHE B 1 293 ? 46.316 91.217 98.561 1.00 3.91 ? 375 PHE B CD1 1 ATOM 4951 C CD2 . PHE B 1 293 ? 47.984 91.482 100.258 1.00 3.91 ? 375 PHE B CD2 1 ATOM 4952 C CE1 . PHE B 1 293 ? 46.301 89.842 98.775 1.00 3.91 ? 375 PHE B CE1 1 ATOM 4953 C CE2 . PHE B 1 293 ? 47.977 90.092 100.487 1.00 3.91 ? 375 PHE B CE2 1 ATOM 4954 C CZ . PHE B 1 293 ? 47.133 89.274 99.742 1.00 3.91 ? 375 PHE B CZ 1 ATOM 4955 N N . GLY B 1 294 ? 46.120 95.765 96.835 1.00 5.89 ? 376 GLY B N 1 ATOM 4956 C CA . GLY B 1 294 ? 45.775 97.151 96.581 1.00 5.89 ? 376 GLY B CA 1 ATOM 4957 C C . GLY B 1 294 ? 44.579 97.715 97.319 1.00 5.89 ? 376 GLY B C 1 ATOM 4958 O O . GLY B 1 294 ? 44.245 97.274 98.422 1.00 5.89 ? 376 GLY B O 1 ATOM 4959 N N . ILE B 1 295 ? 43.939 98.706 96.693 1.00 9.60 ? 377 ILE B N 1 ATOM 4960 C CA . ILE B 1 295 ? 42.765 99.376 97.249 1.00 9.60 ? 377 ILE B CA 1 ATOM 4961 C C . ILE B 1 295 ? 41.745 98.335 97.706 1.00 9.60 ? 377 ILE B C 1 ATOM 4962 O O . ILE B 1 295 ? 41.405 97.424 96.952 1.00 9.60 ? 377 ILE B O 1 ATOM 4963 C CB . ILE B 1 295 ? 42.128 100.349 96.214 1.00 10.70 ? 377 ILE B CB 1 ATOM 4964 C CG1 . ILE B 1 295 ? 43.131 101.450 95.845 1.00 10.70 ? 377 ILE B CG1 1 ATOM 4965 C CG2 . ILE B 1 295 ? 40.873 100.992 96.788 1.00 10.70 ? 377 ILE B CG2 1 ATOM 4966 C CD1 . ILE B 1 295 ? 42.660 102.395 94.747 1.00 10.70 ? 377 ILE B CD1 1 ATOM 4967 N N . ARG B 1 296 ? 41.312 98.460 98.959 1.00 6.06 ? 378 ARG B N 1 ATOM 4968 C CA . ARG B 1 296 ? 40.353 97.538 99.572 1.00 6.06 ? 378 ARG B CA 1 ATOM 4969 C C . ARG B 1 296 ? 38.961 97.687 98.970 1.00 6.06 ? 378 ARG B C 1 ATOM 4970 O O . ARG B 1 296 ? 38.533 98.793 98.654 1.00 6.06 ? 378 ARG B O 1 ATOM 4971 C CB . ARG B 1 296 ? 40.260 97.793 101.084 1.00 15.97 ? 378 ARG B CB 1 ATOM 4972 C CG . ARG B 1 296 ? 41.593 97.917 101.811 1.00 15.97 ? 378 ARG B CG 1 ATOM 4973 C CD . ARG B 1 296 ? 42.273 96.577 102.037 1.00 15.97 ? 378 ARG B CD 1 ATOM 4974 N NE . ARG B 1 296 ? 43.634 96.755 102.545 1.00 15.97 ? 378 ARG B NE 1 ATOM 4975 C CZ . ARG B 1 296 ? 43.947 97.008 103.813 1.00 15.97 ? 378 ARG B CZ 1 ATOM 4976 N NH1 . ARG B 1 296 ? 43.003 97.079 104.742 1.00 15.97 ? 378 ARG B NH1 1 ATOM 4977 N NH2 . ARG B 1 296 ? 45.218 97.158 104.160 1.00 15.97 ? 378 ARG B NH2 1 ATOM 4978 N N . PRO B 1 297 ? 38.220 96.570 98.850 1.00 9.03 ? 379 PRO B N 1 ATOM 4979 C CA . PRO B 1 297 ? 36.864 96.560 98.292 1.00 9.03 ? 379 PRO B CA 1 ATOM 4980 C C . PRO B 1 297 ? 35.978 97.617 98.956 1.00 9.03 ? 379 PRO B C 1 ATOM 4981 O O . PRO B 1 297 ? 35.905 97.690 100.183 1.00 9.03 ? 379 PRO B O 1 ATOM 4982 C CB . PRO B 1 297 ? 36.379 95.148 98.614 1.00 4.61 ? 379 PRO B CB 1 ATOM 4983 C CG . PRO B 1 297 ? 37.627 94.342 98.540 1.00 4.61 ? 379 PRO B CG 1 ATOM 4984 C CD . PRO B 1 297 ? 38.636 95.212 99.242 1.00 4.61 ? 379 PRO B CD 1 ATOM 4985 N N . SER B 1 298 ? 35.338 98.450 98.141 1.00 8.46 ? 380 SER B N 1 ATOM 4986 C CA . SER B 1 298 ? 34.466 99.507 98.649 1.00 8.46 ? 380 SER B CA 1 ATOM 4987 C C . SER B 1 298 ? 33.622 100.138 97.552 1.00 8.46 ? 380 SER B C 1 ATOM 4988 O O . SER B 1 298 ? 34.087 100.318 96.426 1.00 8.46 ? 380 SER B O 1 ATOM 4989 C CB . SER B 1 298 ? 35.292 100.601 99.330 1.00 12.62 ? 380 SER B CB 1 ATOM 4990 O OG . SER B 1 298 ? 34.479 101.710 99.683 1.00 12.62 ? 380 SER B OG 1 ATOM 4991 N N . ALA B 1 299 ? 32.389 100.490 97.905 1.00 7.38 ? 381 ALA B N 1 ATOM 4992 C CA . ALA B 1 299 ? 31.457 101.122 96.976 1.00 7.38 ? 381 ALA B CA 1 ATOM 4993 C C . ALA B 1 299 ? 31.635 102.645 96.947 1.00 7.38 ? 381 ALA B C 1 ATOM 4994 O O . ALA B 1 299 ? 31.078 103.326 96.086 1.00 7.38 ? 381 ALA B O 1 ATOM 4995 C CB . ALA B 1 299 ? 30.020 100.758 97.342 1.00 9.25 ? 381 ALA B CB 1 ATOM 4996 N N . ASN B 1 300 ? 32.380 103.180 97.912 1.00 12.49 ? 382 ASN B N 1 ATOM 4997 C CA . ASN B 1 300 ? 32.646 104.617 97.965 1.00 12.49 ? 382 ASN B CA 1 ATOM 4998 C C . ASN B 1 300 ? 33.871 104.835 97.093 1.00 12.49 ? 382 ASN B C 1 ATOM 4999 O O . ASN B 1 300 ? 34.992 104.981 97.581 1.00 12.49 ? 382 ASN B O 1 ATOM 5000 C CB . ASN B 1 300 ? 32.914 105.068 99.403 1.00 34.09 ? 382 ASN B CB 1 ATOM 5001 C CG . ASN B 1 300 ? 31.689 104.935 100.291 1.00 34.09 ? 382 ASN B CG 1 ATOM 5002 O OD1 . ASN B 1 300 ? 31.722 104.264 101.319 1.00 34.09 ? 382 ASN B OD1 1 ATOM 5003 N ND2 . ASN B 1 300 ? 30.600 105.571 99.892 1.00 34.09 ? 382 ASN B ND2 1 ATOM 5004 N N . THR B 1 301 ? 33.634 104.849 95.789 1.00 10.39 ? 383 THR B N 1 ATOM 5005 C CA . THR B 1 301 ? 34.695 104.981 94.802 1.00 10.39 ? 383 THR B CA 1 ATOM 5006 C C . THR B 1 301 ? 35.059 106.394 94.362 1.00 10.39 ? 383 THR B C 1 ATOM 5007 O O . THR B 1 301 ? 36.066 106.584 93.686 1.00 10.39 ? 383 THR B O 1 ATOM 5008 C CB . THR B 1 301 ? 34.325 104.184 93.547 1.00 5.84 ? 383 THR B CB 1 ATOM 5009 O OG1 . THR B 1 301 ? 33.129 104.736 92.983 1.00 5.84 ? 383 THR B OG1 1 ATOM 5010 C CG2 . THR B 1 301 ? 34.065 102.726 93.897 1.00 5.84 ? 383 THR B CG2 1 ATOM 5011 N N . GLY B 1 302 ? 34.225 107.372 94.698 1.00 7.60 ? 384 GLY B N 1 ATOM 5012 C CA . GLY B 1 302 ? 34.499 108.739 94.284 1.00 7.60 ? 384 GLY B CA 1 ATOM 5013 C C . GLY B 1 302 ? 34.517 108.869 92.772 1.00 7.60 ? 384 GLY B C 1 ATOM 5014 O O . GLY B 1 302 ? 35.148 109.772 92.221 1.00 7.60 ? 384 GLY B O 1 ATOM 5015 N N . ASP B 1 303 ? 33.794 107.978 92.098 1.00 7.89 ? 385 ASP B N 1 ATOM 5016 C CA . ASP B 1 303 ? 33.744 107.962 90.642 1.00 7.89 ? 385 ASP B CA 1 ATOM 5017 C C . ASP B 1 303 ? 32.317 107.688 90.162 1.00 7.89 ? 385 ASP B C 1 ATOM 5018 O O . ASP B 1 303 ? 31.624 106.835 90.707 1.00 7.89 ? 385 ASP B O 1 ATOM 5019 C CB . ASP B 1 303 ? 34.695 106.881 90.125 1.00 10.40 ? 385 ASP B CB 1 ATOM 5020 C CG . ASP B 1 303 ? 34.865 106.920 88.626 1.00 10.40 ? 385 ASP B CG 1 ATOM 5021 O OD1 . ASP B 1 303 ? 35.766 107.640 88.148 1.00 10.40 ? 385 ASP B OD1 1 ATOM 5022 O OD2 . ASP B 1 303 ? 34.104 106.219 87.927 1.00 10.40 ? 385 ASP B OD2 1 ATOM 5023 N N . SER B 1 304 ? 31.907 108.391 89.110 1.00 9.65 ? 386 SER B N 1 ATOM 5024 C CA . SER B 1 304 ? 30.564 108.267 88.545 1.00 9.65 ? 386 SER B CA 1 ATOM 5025 C C . SER B 1 304 ? 30.218 106.934 87.885 1.00 9.65 ? 386 SER B C 1 ATOM 5026 O O . SER B 1 304 ? 29.050 106.548 87.847 1.00 9.65 ? 386 SER B O 1 ATOM 5027 C CB . SER B 1 304 ? 30.340 109.381 87.531 1.00 12.36 ? 386 SER B CB 1 ATOM 5028 O OG . SER B 1 304 ? 31.313 109.316 86.504 1.00 12.36 ? 386 SER B OG 1 ATOM 5029 N N . LEU B 1 305 ? 31.223 106.250 87.344 1.00 7.82 ? 387 LEU B N 1 ATOM 5030 C CA . LEU B 1 305 ? 31.012 104.984 86.649 1.00 7.82 ? 387 LEU B CA 1 ATOM 5031 C C . LEU B 1 305 ? 31.385 103.717 87.413 1.00 7.82 ? 387 LEU B C 1 ATOM 5032 O O . LEU B 1 305 ? 30.905 102.632 87.084 1.00 7.82 ? 387 LEU B O 1 ATOM 5033 C CB . LEU B 1 305 ? 31.756 104.996 85.311 1.00 9.54 ? 387 LEU B CB 1 ATOM 5034 C CG . LEU B 1 305 ? 31.318 106.020 84.264 1.00 9.54 ? 387 LEU B CG 1 ATOM 5035 C CD1 . LEU B 1 305 ? 32.206 105.901 83.042 1.00 9.54 ? 387 LEU B CD1 1 ATOM 5036 C CD2 . LEU B 1 305 ? 29.864 105.793 83.877 1.00 9.54 ? 387 LEU B CD2 1 ATOM 5037 N N . LEU B 1 306 ? 32.243 103.839 88.422 1.00 6.49 ? 388 LEU B N 1 ATOM 5038 C CA . LEU B 1 306 ? 32.663 102.664 89.179 1.00 6.49 ? 388 LEU B CA 1 ATOM 5039 C C . LEU B 1 306 ? 31.750 102.338 90.362 1.00 6.49 ? 388 LEU B C 1 ATOM 5040 O O . LEU B 1 306 ? 31.669 103.101 91.329 1.00 6.49 ? 388 LEU B O 1 ATOM 5041 C CB . LEU B 1 306 ? 34.107 102.822 89.664 1.00 2.47 ? 388 LEU B CB 1 ATOM 5042 C CG . LEU B 1 306 ? 34.811 101.518 90.052 1.00 2.47 ? 388 LEU B CG 1 ATOM 5043 C CD1 . LEU B 1 306 ? 35.150 100.745 88.788 1.00 2.47 ? 388 LEU B CD1 1 ATOM 5044 C CD2 . LEU B 1 306 ? 36.075 101.816 90.838 1.00 2.47 ? 388 LEU B CD2 1 ATOM 5045 N N . ASP B 1 307 ? 31.061 101.203 90.277 1.00 5.65 ? 389 ASP B N 1 ATOM 5046 C CA . ASP B 1 307 ? 30.171 100.761 91.344 1.00 5.65 ? 389 ASP B CA 1 ATOM 5047 C C . ASP B 1 307 ? 30.967 100.368 92.575 1.00 5.65 ? 389 ASP B C 1 ATOM 5048 O O . ASP B 1 307 ? 30.526 100.599 93.706 1.00 5.65 ? 389 ASP B O 1 ATOM 5049 C CB . ASP B 1 307 ? 29.349 99.546 90.906 1.00 3.66 ? 389 ASP B CB 1 ATOM 5050 C CG . ASP B 1 307 ? 28.129 99.911 90.088 1.00 3.66 ? 389 ASP B CG 1 ATOM 5051 O OD1 . ASP B 1 307 ? 27.710 101.084 90.056 1.00 3.66 ? 389 ASP B OD1 1 ATOM 5052 O OD2 . ASP B 1 307 ? 27.568 98.988 89.481 1.00 3.66 ? 389 ASP B OD2 1 ATOM 5053 N N . SER B 1 308 ? 32.144 99.780 92.353 1.00 5.43 ? 390 SER B N 1 ATOM 5054 C CA . SER B 1 308 ? 32.970 99.333 93.464 1.00 5.43 ? 390 SER B CA 1 ATOM 5055 C C . SER B 1 308 ? 34.352 98.813 93.093 1.00 5.43 ? 390 SER B C 1 ATOM 5056 O O . SER B 1 308 ? 34.580 98.349 91.974 1.00 5.43 ? 390 SER B O 1 ATOM 5057 C CB . SER B 1 308 ? 32.223 98.225 94.216 1.00 8.49 ? 390 SER B CB 1 ATOM 5058 O OG . SER B 1 308 ? 33.023 97.620 95.211 1.00 8.49 ? 390 SER B OG 1 ATOM 5059 N N . PHE B 1 309 ? 35.285 98.956 94.036 1.00 7.71 ? 391 PHE B N 1 ATOM 5060 C CA . PHE B 1 309 ? 36.629 98.408 93.892 1.00 7.71 ? 391 PHE B CA 1 ATOM 5061 C C . PHE B 1 309 ? 36.395 96.993 94.420 1.00 7.71 ? 391 PHE B C 1 ATOM 5062 O O . PHE B 1 309 ? 35.676 96.815 95.407 1.00 7.71 ? 391 PHE B O 1 ATOM 5063 C CB . PHE B 1 309 ? 37.631 99.089 94.840 1.00 7.71 ? 391 PHE B CB 1 ATOM 5064 C CG . PHE B 1 309 ? 37.917 100.526 94.509 1.00 7.71 ? 391 PHE B CG 1 ATOM 5065 C CD1 . PHE B 1 309 ? 38.615 100.863 93.354 1.00 7.71 ? 391 PHE B CD1 1 ATOM 5066 C CD2 . PHE B 1 309 ? 37.512 101.541 95.372 1.00 7.71 ? 391 PHE B CD2 1 ATOM 5067 C CE1 . PHE B 1 309 ? 38.904 102.192 93.064 1.00 7.71 ? 391 PHE B CE1 1 ATOM 5068 C CE2 . PHE B 1 309 ? 37.798 102.873 95.089 1.00 7.71 ? 391 PHE B CE2 1 ATOM 5069 C CZ . PHE B 1 309 ? 38.496 103.199 93.932 1.00 7.71 ? 391 PHE B CZ 1 ATOM 5070 N N . VAL B 1 310 ? 36.972 95.991 93.769 1.00 5.65 ? 392 VAL B N 1 ATOM 5071 C CA . VAL B 1 310 ? 36.801 94.615 94.217 1.00 5.65 ? 392 VAL B CA 1 ATOM 5072 C C . VAL B 1 310 ? 38.116 93.848 94.124 1.00 5.65 ? 392 VAL B C 1 ATOM 5073 O O . VAL B 1 310 ? 39.089 94.337 93.555 1.00 5.65 ? 392 VAL B O 1 ATOM 5074 C CB . VAL B 1 310 ? 35.726 93.855 93.363 1.00 2.00 ? 392 VAL B CB 1 ATOM 5075 C CG1 . VAL B 1 310 ? 34.339 94.437 93.596 1.00 2.00 ? 392 VAL B CG1 1 ATOM 5076 C CG2 . VAL B 1 310 ? 36.070 93.916 91.878 1.00 2.00 ? 392 VAL B CG2 1 ATOM 5077 N N . TRP B 1 311 ? 38.149 92.680 94.760 1.00 5.57 ? 393 TRP B N 1 ATOM 5078 C CA . TRP B 1 311 ? 39.301 91.782 94.718 1.00 5.57 ? 393 TRP B CA 1 ATOM 5079 C C . TRP B 1 311 ? 38.737 90.506 94.102 1.00 5.57 ? 393 TRP B C 1 ATOM 5080 O O . TRP B 1 311 ? 38.115 89.702 94.787 1.00 5.57 ? 393 TRP B O 1 ATOM 5081 C CB . TRP B 1 311 ? 39.844 91.494 96.126 1.00 5.41 ? 393 TRP B CB 1 ATOM 5082 C CG . TRP B 1 311 ? 40.716 92.587 96.697 1.00 5.41 ? 393 TRP B CG 1 ATOM 5083 C CD1 . TRP B 1 311 ? 40.792 93.886 96.273 1.00 5.41 ? 393 TRP B CD1 1 ATOM 5084 C CD2 . TRP B 1 311 ? 41.632 92.470 97.796 1.00 5.41 ? 393 TRP B CD2 1 ATOM 5085 N NE1 . TRP B 1 311 ? 41.693 94.582 97.041 1.00 5.41 ? 393 TRP B NE1 1 ATOM 5086 C CE2 . TRP B 1 311 ? 42.224 93.743 97.983 1.00 5.41 ? 393 TRP B CE2 1 ATOM 5087 C CE3 . TRP B 1 311 ? 42.009 91.420 98.643 1.00 5.41 ? 393 TRP B CE3 1 ATOM 5088 C CZ2 . TRP B 1 311 ? 43.175 93.991 98.982 1.00 5.41 ? 393 TRP B CZ2 1 ATOM 5089 C CZ3 . TRP B 1 311 ? 42.958 91.669 99.640 1.00 5.41 ? 393 TRP B CZ3 1 ATOM 5090 C CH2 . TRP B 1 311 ? 43.525 92.943 99.798 1.00 5.41 ? 393 TRP B CH2 1 ATOM 5091 N N . VAL B 1 312 ? 38.878 90.360 92.792 1.00 5.13 ? 394 VAL B N 1 ATOM 5092 C CA . VAL B 1 312 ? 38.349 89.189 92.111 1.00 5.13 ? 394 VAL B CA 1 ATOM 5093 C C . VAL B 1 312 ? 39.309 88.005 92.208 1.00 5.13 ? 394 VAL B C 1 ATOM 5094 O O . VAL B 1 312 ? 38.959 86.955 92.754 1.00 5.13 ? 394 VAL B O 1 ATOM 5095 C CB . VAL B 1 312 ? 37.999 89.522 90.636 1.00 2.00 ? 394 VAL B CB 1 ATOM 5096 C CG1 . VAL B 1 312 ? 37.275 88.358 89.985 1.00 2.00 ? 394 VAL B CG1 1 ATOM 5097 C CG2 . VAL B 1 312 ? 37.127 90.772 90.583 1.00 2.00 ? 394 VAL B CG2 1 ATOM 5098 N N . LYS B 1 313 ? 40.510 88.170 91.666 1.00 6.87 ? 395 LYS B N 1 ATOM 5099 C CA . LYS B 1 313 ? 41.533 87.128 91.725 1.00 6.87 ? 395 LYS B CA 1 ATOM 5100 C C . LYS B 1 313 ? 42.080 87.141 93.156 1.00 6.87 ? 395 LYS B C 1 ATOM 5101 O O . LYS B 1 313 ? 42.588 88.164 93.623 1.00 6.87 ? 395 LYS B O 1 ATOM 5102 C CB . LYS B 1 313 ? 42.644 87.424 90.714 1.00 8.32 ? 395 LYS B CB 1 ATOM 5103 C CG . LYS B 1 313 ? 43.917 86.605 90.892 1.00 8.32 ? 395 LYS B CG 1 ATOM 5104 C CD . LYS B 1 313 ? 43.739 85.132 90.569 1.00 8.32 ? 395 LYS B CD 1 ATOM 5105 C CE . LYS B 1 313 ? 45.049 84.409 90.836 1.00 8.32 ? 395 LYS B CE 1 ATOM 5106 N NZ . LYS B 1 313 ? 45.030 82.977 90.441 1.00 8.32 ? 395 LYS B NZ 1 ATOM 5107 N N . PRO B 1 314 ? 41.927 86.024 93.889 1.00 9.02 ? 396 PRO B N 1 ATOM 5108 C CA . PRO B 1 314 ? 42.409 85.929 95.275 1.00 9.02 ? 396 PRO B CA 1 ATOM 5109 C C . PRO B 1 314 ? 43.932 85.893 95.328 1.00 9.02 ? 396 PRO B C 1 ATOM 5110 O O . PRO B 1 314 ? 44.555 85.015 94.739 1.00 9.02 ? 396 PRO B O 1 ATOM 5111 C CB . PRO B 1 314 ? 41.806 84.608 95.768 1.00 8.20 ? 396 PRO B CB 1 ATOM 5112 C CG . PRO B 1 314 ? 40.668 84.324 94.789 1.00 8.20 ? 396 PRO B CG 1 ATOM 5113 C CD . PRO B 1 314 ? 41.239 84.786 93.489 1.00 8.20 ? 396 PRO B CD 1 ATOM 5114 N N . GLY B 1 315 ? 44.517 86.864 96.024 1.00 8.89 ? 397 GLY B N 1 ATOM 5115 C CA . GLY B 1 315 ? 45.963 86.944 96.140 1.00 8.89 ? 397 GLY B CA 1 ATOM 5116 C C . GLY B 1 315 ? 46.553 85.773 96.895 1.00 8.89 ? 397 GLY B C 1 ATOM 5117 O O . GLY B 1 315 ? 46.182 85.527 98.035 1.00 8.89 ? 397 GLY B O 1 ATOM 5118 N N . GLY B 1 316 ? 47.498 85.074 96.275 1.00 6.98 ? 398 GLY B N 1 ATOM 5119 C CA . GLY B 1 316 ? 48.101 83.919 96.913 1.00 6.98 ? 398 GLY B CA 1 ATOM 5120 C C . GLY B 1 316 ? 47.846 82.667 96.095 1.00 6.98 ? 398 GLY B C 1 ATOM 5121 O O . GLY B 1 316 ? 48.626 81.721 96.135 1.00 6.98 ? 398 GLY B O 1 ATOM 5122 N N . GLU B 1 317 ? 46.724 82.644 95.380 1.00 5.74 ? 399 GLU B N 1 ATOM 5123 C CA . GLU B 1 317 ? 46.381 81.511 94.525 1.00 5.74 ? 399 GLU B CA 1 ATOM 5124 C C . GLU B 1 317 ? 47.116 81.689 93.197 1.00 5.74 ? 399 GLU B C 1 ATOM 5125 O O . GLU B 1 317 ? 46.960 82.707 92.518 1.00 5.74 ? 399 GLU B O 1 ATOM 5126 C CB . GLU B 1 317 ? 44.868 81.442 94.321 1.00 9.49 ? 399 GLU B CB 1 ATOM 5127 C CG . GLU B 1 317 ? 44.114 81.183 95.620 1.00 9.49 ? 399 GLU B CG 1 ATOM 5128 C CD . GLU B 1 317 ? 42.617 81.045 95.430 1.00 9.49 ? 399 GLU B CD 1 ATOM 5129 O OE1 . GLU B 1 317 ? 42.148 81.098 94.275 1.00 9.49 ? 399 GLU B OE1 1 ATOM 5130 O OE2 . GLU B 1 317 ? 41.899 80.889 96.439 1.00 9.49 ? 399 GLU B OE2 1 ATOM 5131 N N . CYS B 1 318 ? 47.899 80.680 92.834 1.00 5.43 ? 400 CYS B N 1 ATOM 5132 C CA . CYS B 1 318 ? 48.728 80.692 91.631 1.00 5.43 ? 400 CYS B CA 1 ATOM 5133 C C . CYS B 1 318 ? 48.039 80.914 90.282 1.00 5.43 ? 400 CYS B C 1 ATOM 5134 O O . CYS B 1 318 ? 46.898 80.504 90.081 1.00 5.43 ? 400 CYS B O 1 ATOM 5135 C CB . CYS B 1 318 ? 49.560 79.412 91.582 1.00 11.26 ? 400 CYS B CB 1 ATOM 5136 S SG . CYS B 1 318 ? 51.036 79.533 90.557 1.00 11.26 ? 400 CYS B SG 1 ATOM 5137 N N . ASP B 1 319 ? 48.749 81.573 89.365 1.00 4.79 ? 401 ASP B N 1 ATOM 5138 C CA . ASP B 1 319 ? 48.245 81.845 88.012 1.00 4.79 ? 401 ASP B CA 1 ATOM 5139 C C . ASP B 1 319 ? 48.606 80.701 87.067 1.00 4.79 ? 401 ASP B C 1 ATOM 5140 O O . ASP B 1 319 ? 47.994 80.534 86.016 1.00 4.79 ? 401 ASP B O 1 ATOM 5141 C CB . ASP B 1 319 ? 48.853 83.136 87.450 1.00 9.63 ? 401 ASP B CB 1 ATOM 5142 C CG . ASP B 1 319 ? 48.369 84.385 88.164 1.00 9.63 ? 401 ASP B CG 1 ATOM 5143 O OD1 . ASP B 1 319 ? 47.191 84.444 88.562 1.00 9.63 ? 401 ASP B OD1 1 ATOM 5144 O OD2 . ASP B 1 319 ? 49.170 85.331 88.303 1.00 9.63 ? 401 ASP B OD2 1 ATOM 5145 N N . GLY B 1 320 ? 49.643 79.953 87.420 1.00 8.41 ? 402 GLY B N 1 ATOM 5146 C CA . GLY B 1 320 ? 50.083 78.848 86.587 1.00 8.41 ? 402 GLY B CA 1 ATOM 5147 C C . GLY B 1 320 ? 51.440 78.353 87.053 1.00 8.41 ? 402 GLY B C 1 ATOM 5148 O O . GLY B 1 320 ? 52.157 79.070 87.760 1.00 8.41 ? 402 GLY B O 1 ATOM 5149 N N . THR B 1 321 ? 51.808 77.146 86.635 1.00 11.57 ? 403 THR B N 1 ATOM 5150 C CA . THR B 1 321 ? 53.080 76.545 87.037 1.00 11.57 ? 403 THR B CA 1 ATOM 5151 C C . THR B 1 321 ? 54.285 76.932 86.176 1.00 11.57 ? 403 THR B C 1 ATOM 5152 O O . THR B 1 321 ? 54.159 77.165 84.974 1.00 11.57 ? 403 THR B O 1 ATOM 5153 C CB . THR B 1 321 ? 52.966 75.000 87.091 1.00 17.26 ? 403 THR B CB 1 ATOM 5154 O OG1 . THR B 1 321 ? 54.160 74.450 87.659 1.00 17.26 ? 403 THR B OG1 1 ATOM 5155 C CG2 . THR B 1 321 ? 52.760 74.421 85.698 1.00 17.26 ? 403 THR B CG2 1 ATOM 5156 N N . SER B 1 322 ? 55.456 76.993 86.804 1.00 14.90 ? 404 SER B N 1 ATOM 5157 C CA . SER B 1 322 ? 56.687 77.315 86.090 1.00 14.90 ? 404 SER B CA 1 ATOM 5158 C C . SER B 1 322 ? 57.457 76.029 85.759 1.00 14.90 ? 404 SER B C 1 ATOM 5159 O O . SER B 1 322 ? 58.536 76.082 85.171 1.00 14.90 ? 404 SER B O 1 ATOM 5160 C CB . SER B 1 322 ? 57.564 78.262 86.914 1.00 12.69 ? 404 SER B CB 1 ATOM 5161 O OG . SER B 1 322 ? 57.943 77.682 88.152 1.00 12.69 ? 404 SER B OG 1 ATOM 5162 N N . ASP B 1 323 ? 56.877 74.882 86.120 1.00 10.45 ? 405 ASP B N 1 ATOM 5163 C CA . ASP B 1 323 ? 57.483 73.574 85.885 1.00 10.45 ? 405 ASP B CA 1 ATOM 5164 C C . ASP B 1 323 ? 57.308 73.133 84.431 1.00 10.45 ? 405 ASP B C 1 ATOM 5165 O O . ASP B 1 323 ? 56.198 72.826 83.997 1.00 10.45 ? 405 ASP B O 1 ATOM 5166 C CB . ASP B 1 323 ? 56.855 72.551 86.831 1.00 15.85 ? 405 ASP B CB 1 ATOM 5167 C CG . ASP B 1 323 ? 57.557 71.199 86.803 1.00 15.85 ? 405 ASP B CG 1 ATOM 5168 O OD1 . ASP B 1 323 ? 58.554 71.026 86.067 1.00 15.85 ? 405 ASP B OD1 1 ATOM 5169 O OD2 . ASP B 1 323 ? 57.100 70.297 87.534 1.00 15.85 ? 405 ASP B OD2 1 ATOM 5170 N N . SER B 1 324 ? 58.419 73.033 83.707 1.00 24.19 ? 406 SER B N 1 ATOM 5171 C CA . SER B 1 324 ? 58.393 72.642 82.298 1.00 24.19 ? 406 SER B CA 1 ATOM 5172 C C . SER B 1 324 ? 57.996 71.192 82.032 1.00 24.19 ? 406 SER B C 1 ATOM 5173 O O . SER B 1 324 ? 57.481 70.880 80.959 1.00 24.19 ? 406 SER B O 1 ATOM 5174 C CB . SER B 1 324 ? 59.741 72.944 81.637 1.00 35.77 ? 406 SER B CB 1 ATOM 5175 O OG . SER B 1 324 ? 60.803 72.287 82.307 1.00 35.77 ? 406 SER B OG 1 ATOM 5176 N N . SER B 1 325 ? 58.231 70.308 82.999 1.00 45.83 ? 407 SER B N 1 ATOM 5177 C CA . SER B 1 325 ? 57.884 68.898 82.834 1.00 45.83 ? 407 SER B CA 1 ATOM 5178 C C . SER B 1 325 ? 56.459 68.618 83.298 1.00 45.83 ? 407 SER B C 1 ATOM 5179 O O . SER B 1 325 ? 56.017 67.467 83.326 1.00 45.83 ? 407 SER B O 1 ATOM 5180 C CB . SER B 1 325 ? 58.867 68.004 83.600 1.00 46.70 ? 407 SER B CB 1 ATOM 5181 O OG . SER B 1 325 ? 58.749 68.188 85.000 1.00 46.70 ? 407 SER B OG 1 ATOM 5182 N N . ALA B 1 326 ? 55.741 69.677 83.655 1.00 27.55 ? 408 ALA B N 1 ATOM 5183 C CA . ALA B 1 326 ? 54.371 69.552 84.127 1.00 27.55 ? 408 ALA B CA 1 ATOM 5184 C C . ALA B 1 326 ? 53.355 69.823 83.025 1.00 27.55 ? 408 ALA B C 1 ATOM 5185 O O . ALA B 1 326 ? 53.612 70.609 82.109 1.00 27.55 ? 408 ALA B O 1 ATOM 5186 C CB . ALA B 1 326 ? 54.138 70.502 85.291 1.00 23.87 ? 408 ALA B CB 1 ATOM 5187 N N . PRO B 1 327 ? 52.203 69.129 83.069 1.00 55.29 ? 409 PRO B N 1 ATOM 5188 C CA . PRO B 1 327 ? 51.161 69.329 82.061 1.00 55.29 ? 409 PRO B CA 1 ATOM 5189 C C . PRO B 1 327 ? 50.572 70.718 82.291 1.00 55.29 ? 409 PRO B C 1 ATOM 5190 O O . PRO B 1 327 ? 50.642 71.247 83.405 1.00 55.29 ? 409 PRO B O 1 ATOM 5191 C CB . PRO B 1 327 ? 50.137 68.242 82.399 1.00 54.07 ? 409 PRO B CB 1 ATOM 5192 C CG . PRO B 1 327 ? 50.938 67.200 83.109 1.00 54.07 ? 409 PRO B CG 1 ATOM 5193 C CD . PRO B 1 327 ? 51.855 68.017 83.968 1.00 54.07 ? 409 PRO B CD 1 ATOM 5194 N N . ARG B 1 328 ? 50.001 71.305 81.244 1.00 28.17 ? 410 ARG B N 1 ATOM 5195 C CA . ARG B 1 328 ? 49.400 72.638 81.323 1.00 28.17 ? 410 ARG B CA 1 ATOM 5196 C C . ARG B 1 328 ? 50.449 73.735 81.542 1.00 28.17 ? 410 ARG B C 1 ATOM 5197 O O . ARG B 1 328 ? 50.103 74.868 81.876 1.00 28.17 ? 410 ARG B O 1 ATOM 5198 C CB . ARG B 1 328 ? 48.347 72.707 82.440 1.00 78.50 ? 410 ARG B CB 1 ATOM 5199 C CG . ARG B 1 328 ? 47.359 71.549 82.483 1.00 78.50 ? 410 ARG B CG 1 ATOM 5200 C CD . ARG B 1 328 ? 46.439 71.520 81.282 1.00 78.50 ? 410 ARG B CD 1 ATOM 5201 N NE . ARG B 1 328 ? 45.452 70.449 81.397 1.00 78.50 ? 410 ARG B NE 1 ATOM 5202 C CZ . ARG B 1 328 ? 45.004 69.727 80.376 1.00 78.50 ? 410 ARG B CZ 1 ATOM 5203 N NH1 . ARG B 1 328 ? 45.448 69.955 79.146 1.00 78.50 ? 410 ARG B NH1 1 ATOM 5204 N NH2 . ARG B 1 328 ? 44.115 68.764 80.585 1.00 78.50 ? 410 ARG B NH2 1 ATOM 5205 N N . PHE B 1 329 ? 51.726 73.400 81.358 1.00 17.38 ? 411 PHE B N 1 ATOM 5206 C CA . PHE B 1 329 ? 52.800 74.378 81.523 1.00 17.38 ? 411 PHE B CA 1 ATOM 5207 C C . PHE B 1 329 ? 52.686 75.490 80.480 1.00 17.38 ? 411 PHE B C 1 ATOM 5208 O O . PHE B 1 329 ? 52.564 75.229 79.284 1.00 17.38 ? 411 PHE B O 1 ATOM 5209 C CB . PHE B 1 329 ? 54.181 73.710 81.418 1.00 18.39 ? 411 PHE B CB 1 ATOM 5210 C CG . PHE B 1 329 ? 55.321 74.687 81.325 1.00 18.39 ? 411 PHE B CG 1 ATOM 5211 C CD1 . PHE B 1 329 ? 55.599 75.555 82.376 1.00 18.39 ? 411 PHE B CD1 1 ATOM 5212 C CD2 . PHE B 1 329 ? 56.091 74.770 80.171 1.00 18.39 ? 411 PHE B CD2 1 ATOM 5213 C CE1 . PHE B 1 329 ? 56.622 76.495 82.281 1.00 18.39 ? 411 PHE B CE1 1 ATOM 5214 C CE2 . PHE B 1 329 ? 57.119 75.709 80.061 1.00 18.39 ? 411 PHE B CE2 1 ATOM 5215 C CZ . PHE B 1 329 ? 57.384 76.575 81.122 1.00 18.39 ? 411 PHE B CZ 1 ATOM 5216 N N . ASP B 1 330 ? 52.705 76.730 80.954 1.00 14.96 ? 412 ASP B N 1 ATOM 5217 C CA . ASP B 1 330 ? 52.614 77.897 80.084 1.00 14.96 ? 412 ASP B CA 1 ATOM 5218 C C . ASP B 1 330 ? 53.944 78.629 80.217 1.00 14.96 ? 412 ASP B C 1 ATOM 5219 O O . ASP B 1 330 ? 54.356 78.971 81.327 1.00 14.96 ? 412 ASP B O 1 ATOM 5220 C CB . ASP B 1 330 ? 51.459 78.796 80.541 1.00 18.01 ? 412 ASP B CB 1 ATOM 5221 C CG . ASP B 1 330 ? 51.089 79.849 79.512 1.00 18.01 ? 412 ASP B CG 1 ATOM 5222 O OD1 . ASP B 1 330 ? 51.977 80.599 79.066 1.00 18.01 ? 412 ASP B OD1 1 ATOM 5223 O OD2 . ASP B 1 330 ? 49.902 79.928 79.152 1.00 18.01 ? 412 ASP B OD2 1 ATOM 5224 N N . SER B 1 331 ? 54.615 78.863 79.090 1.00 12.59 ? 413 SER B N 1 ATOM 5225 C CA . SER B 1 331 ? 55.913 79.542 79.095 1.00 12.59 ? 413 SER B CA 1 ATOM 5226 C C . SER B 1 331 ? 55.913 80.967 79.659 1.00 12.59 ? 413 SER B C 1 ATOM 5227 O O . SER B 1 331 ? 56.960 81.474 80.060 1.00 12.59 ? 413 SER B O 1 ATOM 5228 C CB . SER B 1 331 ? 56.552 79.507 77.701 1.00 38.45 ? 413 SER B CB 1 ATOM 5229 O OG . SER B 1 331 ? 55.663 79.974 76.705 1.00 38.45 ? 413 SER B OG 1 ATOM 5230 N N . HIS B 1 332 ? 54.742 81.602 79.706 1.00 11.99 ? 414 HIS B N 1 ATOM 5231 C CA . HIS B 1 332 ? 54.618 82.954 80.255 1.00 11.99 ? 414 HIS B CA 1 ATOM 5232 C C . HIS B 1 332 ? 54.918 82.960 81.754 1.00 11.99 ? 414 HIS B C 1 ATOM 5233 O O . HIS B 1 332 ? 55.259 83.997 82.335 1.00 11.99 ? 414 HIS B O 1 ATOM 5234 C CB . HIS B 1 332 ? 53.206 83.495 80.033 1.00 30.83 ? 414 HIS B CB 1 ATOM 5235 C CG . HIS B 1 332 ? 52.940 83.926 78.625 1.00 30.83 ? 414 HIS B CG 1 ATOM 5236 N ND1 . HIS B 1 332 ? 52.466 83.069 77.660 1.00 30.83 ? 414 HIS B ND1 1 ATOM 5237 C CD2 . HIS B 1 332 ? 53.086 85.129 78.025 1.00 30.83 ? 414 HIS B CD2 1 ATOM 5238 C CE1 . HIS B 1 332 ? 52.330 83.721 76.519 1.00 30.83 ? 414 HIS B CE1 1 ATOM 5239 N NE2 . HIS B 1 332 ? 52.701 84.978 76.717 1.00 30.83 ? 414 HIS B NE2 1 ATOM 5240 N N . CYS B 1 333 ? 54.761 81.797 82.380 1.00 11.00 ? 415 CYS B N 1 ATOM 5241 C CA . CYS B 1 333 ? 55.010 81.640 83.809 1.00 11.00 ? 415 CYS B CA 1 ATOM 5242 C C . CYS B 1 333 ? 56.479 81.352 84.120 1.00 11.00 ? 415 CYS B C 1 ATOM 5243 O O . CYS B 1 333 ? 56.857 81.193 85.282 1.00 11.00 ? 415 CYS B O 1 ATOM 5244 C CB . CYS B 1 333 ? 54.110 80.539 84.366 1.00 7.33 ? 415 CYS B CB 1 ATOM 5245 S SG . CYS B 1 333 ? 52.343 80.914 84.146 1.00 7.33 ? 415 CYS B SG 1 ATOM 5246 N N . ALA B 1 334 ? 57.305 81.329 83.075 1.00 17.58 ? 416 ALA B N 1 ATOM 5247 C CA . ALA B 1 334 ? 58.738 81.071 83.207 1.00 17.58 ? 416 ALA B CA 1 ATOM 5248 C C . ALA B 1 334 ? 59.582 82.305 82.877 1.00 17.58 ? 416 ALA B C 1 ATOM 5249 O O . ALA B 1 334 ? 60.810 82.240 82.889 1.00 17.58 ? 416 ALA B O 1 ATOM 5250 C CB . ALA B 1 334 ? 59.145 79.905 82.312 1.00 14.36 ? 416 ALA B CB 1 ATOM 5251 N N . LEU B 1 335 ? 58.916 83.419 82.585 1.00 9.80 ? 417 LEU B N 1 ATOM 5252 C CA . LEU B 1 335 ? 59.579 84.680 82.252 1.00 9.80 ? 417 LEU B CA 1 ATOM 5253 C C . LEU B 1 335 ? 60.316 85.275 83.451 1.00 9.80 ? 417 LEU B C 1 ATOM 5254 O O . LEU B 1 335 ? 59.995 84.970 84.603 1.00 9.80 ? 417 LEU B O 1 ATOM 5255 C CB . LEU B 1 335 ? 58.554 85.686 81.720 1.00 17.20 ? 417 LEU B CB 1 ATOM 5256 C CG . LEU B 1 335 ? 57.906 85.350 80.376 1.00 17.20 ? 417 LEU B CG 1 ATOM 5257 C CD1 . LEU B 1 335 ? 56.848 86.389 80.038 1.00 17.20 ? 417 LEU B CD1 1 ATOM 5258 C CD2 . LEU B 1 335 ? 58.968 85.293 79.286 1.00 17.20 ? 417 LEU B CD2 1 ATOM 5259 N N . PRO B 1 336 ? 61.315 86.141 83.194 1.00 16.82 ? 418 PRO B N 1 ATOM 5260 C CA . PRO B 1 336 ? 62.114 86.790 84.241 1.00 16.82 ? 418 PRO B CA 1 ATOM 5261 C C . PRO B 1 336 ? 61.299 87.599 85.252 1.00 16.82 ? 418 PRO B C 1 ATOM 5262 O O . PRO B 1 336 ? 61.746 87.817 86.380 1.00 16.82 ? 418 PRO B O 1 ATOM 5263 C CB . PRO B 1 336 ? 63.060 87.695 83.446 1.00 14.52 ? 418 PRO B CB 1 ATOM 5264 C CG . PRO B 1 336 ? 63.210 86.978 82.150 1.00 14.52 ? 418 PRO B CG 1 ATOM 5265 C CD . PRO B 1 336 ? 61.805 86.520 81.856 1.00 14.52 ? 418 PRO B CD 1 ATOM 5266 N N . ASP B 1 337 ? 60.115 88.055 84.847 1.00 13.91 ? 419 ASP B N 1 ATOM 5267 C CA . ASP B 1 337 ? 59.274 88.832 85.751 1.00 13.91 ? 419 ASP B CA 1 ATOM 5268 C C . ASP B 1 337 ? 58.140 88.032 86.387 1.00 13.91 ? 419 ASP B C 1 ATOM 5269 O O . ASP B 1 337 ? 57.178 88.602 86.912 1.00 13.91 ? 419 ASP B O 1 ATOM 5270 C CB . ASP B 1 337 ? 58.755 90.106 85.076 1.00 14.42 ? 419 ASP B CB 1 ATOM 5271 C CG . ASP B 1 337 ? 57.891 89.834 83.859 1.00 14.42 ? 419 ASP B CG 1 ATOM 5272 O OD1 . ASP B 1 337 ? 57.763 88.665 83.426 1.00 14.42 ? 419 ASP B OD1 1 ATOM 5273 O OD2 . ASP B 1 337 ? 57.328 90.812 83.330 1.00 14.42 ? 419 ASP B OD2 1 ATOM 5274 N N . ALA B 1 338 ? 58.251 86.709 86.309 1.00 11.21 ? 420 ALA B N 1 ATOM 5275 C CA . ALA B 1 338 ? 57.274 85.810 86.910 1.00 11.21 ? 420 ALA B CA 1 ATOM 5276 C C . ALA B 1 338 ? 57.985 85.150 88.092 1.00 11.21 ? 420 ALA B C 1 ATOM 5277 O O . ALA B 1 338 ? 59.118 84.681 87.948 1.00 11.21 ? 420 ALA B O 1 ATOM 5278 C CB . ALA B 1 338 ? 56.827 84.762 85.903 1.00 11.47 ? 420 ALA B CB 1 ATOM 5279 N N . LEU B 1 339 ? 57.344 85.156 89.263 1.00 9.97 ? 421 LEU B N 1 ATOM 5280 C CA . LEU B 1 339 ? 57.926 84.564 90.467 1.00 9.97 ? 421 LEU B CA 1 ATOM 5281 C C . LEU B 1 339 ? 58.005 83.042 90.332 1.00 9.97 ? 421 LEU B C 1 ATOM 5282 O O . LEU B 1 339 ? 57.037 82.392 89.924 1.00 9.97 ? 421 LEU B O 1 ATOM 5283 C CB . LEU B 1 339 ? 57.112 84.954 91.711 1.00 9.49 ? 421 LEU B CB 1 ATOM 5284 C CG . LEU B 1 339 ? 57.761 84.686 93.080 1.00 9.49 ? 421 LEU B CG 1 ATOM 5285 C CD1 . LEU B 1 339 ? 59.113 85.392 93.185 1.00 9.49 ? 421 LEU B CD1 1 ATOM 5286 C CD2 . LEU B 1 339 ? 56.832 85.152 94.194 1.00 9.49 ? 421 LEU B CD2 1 ATOM 5287 N N . GLN B 1 340 ? 59.166 82.487 90.675 1.00 11.23 ? 422 GLN B N 1 ATOM 5288 C CA . GLN B 1 340 ? 59.410 81.048 90.572 1.00 11.23 ? 422 GLN B CA 1 ATOM 5289 C C . GLN B 1 340 ? 60.145 80.501 91.793 1.00 11.23 ? 422 GLN B C 1 ATOM 5290 O O . GLN B 1 340 ? 60.875 81.232 92.466 1.00 11.23 ? 422 GLN B O 1 ATOM 5291 C CB . GLN B 1 340 ? 60.228 80.760 89.309 1.00 28.19 ? 422 GLN B CB 1 ATOM 5292 C CG . GLN B 1 340 ? 59.531 81.196 88.027 1.00 28.19 ? 422 GLN B CG 1 ATOM 5293 C CD . GLN B 1 340 ? 60.428 81.129 86.818 1.00 28.19 ? 422 GLN B CD 1 ATOM 5294 O OE1 . GLN B 1 340 ? 60.820 80.046 86.381 1.00 28.19 ? 422 GLN B OE1 1 ATOM 5295 N NE2 . GLN B 1 340 ? 60.757 82.290 86.261 1.00 28.19 ? 422 GLN B NE2 1 ATOM 5296 N N . PRO B 1 341 ? 59.950 79.205 92.105 1.00 15.99 ? 423 PRO B N 1 ATOM 5297 C CA . PRO B 1 341 ? 59.089 78.254 91.388 1.00 15.99 ? 423 PRO B CA 1 ATOM 5298 C C . PRO B 1 341 ? 57.605 78.403 91.742 1.00 15.99 ? 423 PRO B C 1 ATOM 5299 O O . PRO B 1 341 ? 57.258 78.663 92.896 1.00 15.99 ? 423 PRO B O 1 ATOM 5300 C CB . PRO B 1 341 ? 59.645 76.900 91.822 1.00 15.38 ? 423 PRO B CB 1 ATOM 5301 C CG . PRO B 1 341 ? 60.127 77.158 93.207 1.00 15.38 ? 423 PRO B CG 1 ATOM 5302 C CD . PRO B 1 341 ? 60.756 78.523 93.133 1.00 15.38 ? 423 PRO B CD 1 ATOM 5303 N N . ALA B 1 342 ? 56.742 78.230 90.743 1.00 9.04 ? 424 ALA B N 1 ATOM 5304 C CA . ALA B 1 342 ? 55.300 78.369 90.920 1.00 9.04 ? 424 ALA B CA 1 ATOM 5305 C C . ALA B 1 342 ? 54.556 77.051 90.743 1.00 9.04 ? 424 ALA B C 1 ATOM 5306 O O . ALA B 1 342 ? 54.839 76.291 89.820 1.00 9.04 ? 424 ALA B O 1 ATOM 5307 C CB . ALA B 1 342 ? 54.758 79.400 89.935 1.00 11.03 ? 424 ALA B CB 1 ATOM 5308 N N . PRO B 1 343 ? 53.593 76.762 91.638 1.00 13.15 ? 425 PRO B N 1 ATOM 5309 C CA . PRO B 1 343 ? 52.797 75.533 91.586 1.00 13.15 ? 425 PRO B CA 1 ATOM 5310 C C . PRO B 1 343 ? 51.700 75.599 90.524 1.00 13.15 ? 425 PRO B C 1 ATOM 5311 O O . PRO B 1 343 ? 51.635 76.548 89.740 1.00 13.15 ? 425 PRO B O 1 ATOM 5312 C CB . PRO B 1 343 ? 52.204 75.454 92.993 1.00 12.22 ? 425 PRO B CB 1 ATOM 5313 C CG . PRO B 1 343 ? 51.997 76.888 93.346 1.00 12.22 ? 425 PRO B CG 1 ATOM 5314 C CD . PRO B 1 343 ? 53.262 77.554 92.839 1.00 12.22 ? 425 PRO B CD 1 ATOM 5315 N N . GLN B 1 344 ? 50.853 74.575 90.499 1.00 14.00 ? 426 GLN B N 1 ATOM 5316 C CA . GLN B 1 344 ? 49.752 74.489 89.548 1.00 14.00 ? 426 GLN B CA 1 ATOM 5317 C C . GLN B 1 344 ? 48.813 75.684 89.719 1.00 14.00 ? 426 GLN B C 1 ATOM 5318 O O . GLN B 1 344 ? 48.718 76.259 90.804 1.00 14.00 ? 426 GLN B O 1 ATOM 5319 C CB . GLN B 1 344 ? 48.985 73.185 89.780 1.00 121.03 ? 426 GLN B CB 1 ATOM 5320 C CG . GLN B 1 344 ? 47.834 72.928 88.822 1.00 121.03 ? 426 GLN B CG 1 ATOM 5321 C CD . GLN B 1 344 ? 47.037 71.689 89.190 1.00 121.03 ? 426 GLN B CD 1 ATOM 5322 O OE1 . GLN B 1 344 ? 47.361 70.987 90.150 1.00 121.03 ? 426 GLN B OE1 1 ATOM 5323 N NE2 . GLN B 1 344 ? 45.983 71.417 88.430 1.00 121.03 ? 426 GLN B NE2 1 ATOM 5324 N N . ALA B 1 345 ? 48.141 76.067 88.637 1.00 11.24 ? 427 ALA B N 1 ATOM 5325 C CA . ALA B 1 345 ? 47.198 77.178 88.672 1.00 11.24 ? 427 ALA B CA 1 ATOM 5326 C C . ALA B 1 345 ? 46.142 76.932 89.748 1.00 11.24 ? 427 ALA B C 1 ATOM 5327 O O . ALA B 1 345 ? 45.646 75.814 89.903 1.00 11.24 ? 427 ALA B O 1 ATOM 5328 C CB . ALA B 1 345 ? 46.531 77.343 87.310 1.00 16.41 ? 427 ALA B CB 1 ATOM 5329 N N . GLY B 1 346 ? 45.857 77.962 90.537 1.00 9.56 ? 428 GLY B N 1 ATOM 5330 C CA . GLY B 1 346 ? 44.860 77.838 91.582 1.00 9.56 ? 428 GLY B CA 1 ATOM 5331 C C . GLY B 1 346 ? 45.398 77.305 92.894 1.00 9.56 ? 428 GLY B C 1 ATOM 5332 O O . GLY B 1 346 ? 44.746 77.450 93.923 1.00 9.56 ? 428 GLY B O 1 ATOM 5333 N N . ALA B 1 347 ? 46.573 76.680 92.865 1.00 9.30 ? 429 ALA B N 1 ATOM 5334 C CA . ALA B 1 347 ? 47.185 76.137 94.076 1.00 9.30 ? 429 ALA B CA 1 ATOM 5335 C C . ALA B 1 347 ? 47.777 77.264 94.922 1.00 9.30 ? 429 ALA B C 1 ATOM 5336 O O . ALA B 1 347 ? 48.093 78.330 94.401 1.00 9.30 ? 429 ALA B O 1 ATOM 5337 C CB . ALA B 1 347 ? 48.264 75.125 93.712 1.00 3.88 ? 429 ALA B CB 1 ATOM 5338 N N . TRP B 1 348 ? 47.932 77.037 96.223 1.00 7.68 ? 430 TRP B N 1 ATOM 5339 C CA . TRP B 1 348 ? 48.496 78.070 97.085 1.00 7.68 ? 430 TRP B CA 1 ATOM 5340 C C . TRP B 1 348 ? 49.965 78.306 96.729 1.00 7.68 ? 430 TRP B C 1 ATOM 5341 O O . TRP B 1 348 ? 50.736 77.361 96.563 1.00 7.68 ? 430 TRP B O 1 ATOM 5342 C CB . TRP B 1 348 ? 48.349 77.704 98.568 1.00 6.72 ? 430 TRP B CB 1 ATOM 5343 C CG . TRP B 1 348 ? 48.630 78.870 99.488 1.00 6.72 ? 430 TRP B CG 1 ATOM 5344 C CD1 . TRP B 1 348 ? 49.729 79.045 100.285 1.00 6.72 ? 430 TRP B CD1 1 ATOM 5345 C CD2 . TRP B 1 348 ? 47.825 80.042 99.656 1.00 6.72 ? 430 TRP B CD2 1 ATOM 5346 N NE1 . TRP B 1 348 ? 49.659 80.256 100.931 1.00 6.72 ? 430 TRP B NE1 1 ATOM 5347 C CE2 . TRP B 1 348 ? 48.501 80.890 100.562 1.00 6.72 ? 430 TRP B CE2 1 ATOM 5348 C CE3 . TRP B 1 348 ? 46.596 80.462 99.123 1.00 6.72 ? 430 TRP B CE3 1 ATOM 5349 C CZ2 . TRP B 1 348 ? 47.991 82.136 100.950 1.00 6.72 ? 430 TRP B CZ2 1 ATOM 5350 C CZ3 . TRP B 1 348 ? 46.090 81.699 99.506 1.00 6.72 ? 430 TRP B CZ3 1 ATOM 5351 C CH2 . TRP B 1 348 ? 46.788 82.521 100.411 1.00 6.72 ? 430 TRP B CH2 1 ATOM 5352 N N . PHE B 1 349 ? 50.333 79.577 96.607 1.00 9.57 ? 431 PHE B N 1 ATOM 5353 C CA . PHE B 1 349 ? 51.692 79.988 96.254 1.00 9.57 ? 431 PHE B CA 1 ATOM 5354 C C . PHE B 1 349 ? 52.191 80.922 97.368 1.00 9.57 ? 431 PHE B C 1 ATOM 5355 O O . PHE B 1 349 ? 52.123 82.144 97.253 1.00 9.57 ? 431 PHE B O 1 ATOM 5356 C CB . PHE B 1 349 ? 51.652 80.692 94.889 1.00 9.92 ? 431 PHE B CB 1 ATOM 5357 C CG . PHE B 1 349 ? 53.003 80.942 94.266 1.00 9.92 ? 431 PHE B CG 1 ATOM 5358 C CD1 . PHE B 1 349 ? 54.187 80.631 94.933 1.00 9.92 ? 431 PHE B CD1 1 ATOM 5359 C CD2 . PHE B 1 349 ? 53.084 81.526 93.002 1.00 9.92 ? 431 PHE B CD2 1 ATOM 5360 C CE1 . PHE B 1 349 ? 55.427 80.899 94.352 1.00 9.92 ? 431 PHE B CE1 1 ATOM 5361 C CE2 . PHE B 1 349 ? 54.319 81.798 92.417 1.00 9.92 ? 431 PHE B CE2 1 ATOM 5362 C CZ . PHE B 1 349 ? 55.492 81.485 93.094 1.00 9.92 ? 431 PHE B CZ 1 ATOM 5363 N N . GLN B 1 350 ? 52.710 80.312 98.433 1.00 9.00 ? 432 GLN B N 1 ATOM 5364 C CA . GLN B 1 350 ? 53.197 81.006 99.630 1.00 9.00 ? 432 GLN B CA 1 ATOM 5365 C C . GLN B 1 350 ? 54.123 82.194 99.400 1.00 9.00 ? 432 GLN B C 1 ATOM 5366 O O . GLN B 1 350 ? 53.897 83.270 99.947 1.00 9.00 ? 432 GLN B O 1 ATOM 5367 C CB . GLN B 1 350 ? 53.866 80.003 100.583 1.00 11.29 ? 432 GLN B CB 1 ATOM 5368 C CG . GLN B 1 350 ? 54.354 80.590 101.907 1.00 11.29 ? 432 GLN B CG 1 ATOM 5369 C CD . GLN B 1 350 ? 53.225 81.052 102.808 1.00 11.29 ? 432 GLN B CD 1 ATOM 5370 O OE1 . GLN B 1 350 ? 52.046 80.997 102.440 1.00 11.29 ? 432 GLN B OE1 1 ATOM 5371 N NE2 . GLN B 1 350 ? 53.582 81.521 104.000 1.00 11.29 ? 432 GLN B NE2 1 ATOM 5372 N N . ALA B 1 351 ? 55.178 81.990 98.621 1.00 7.45 ? 433 ALA B N 1 ATOM 5373 C CA . ALA B 1 351 ? 56.120 83.068 98.343 1.00 7.45 ? 433 ALA B CA 1 ATOM 5374 C C . ALA B 1 351 ? 55.415 84.252 97.682 1.00 7.45 ? 433 ALA B C 1 ATOM 5375 O O . ALA B 1 351 ? 55.759 85.402 97.946 1.00 7.45 ? 433 ALA B O 1 ATOM 5376 C CB . ALA B 1 351 ? 57.269 82.566 97.465 1.00 4.06 ? 433 ALA B CB 1 ATOM 5377 N N . TYR B 1 352 ? 54.410 83.976 96.852 1.00 4.96 ? 434 TYR B N 1 ATOM 5378 C CA . TYR B 1 352 ? 53.685 85.058 96.185 1.00 4.96 ? 434 TYR B CA 1 ATOM 5379 C C . TYR B 1 352 ? 52.795 85.817 97.163 1.00 4.96 ? 434 TYR B C 1 ATOM 5380 O O . TYR B 1 352 ? 52.684 87.042 97.087 1.00 4.96 ? 434 TYR B O 1 ATOM 5381 C CB . TYR B 1 352 ? 52.870 84.548 94.998 1.00 4.13 ? 434 TYR B CB 1 ATOM 5382 C CG . TYR B 1 352 ? 52.554 85.656 94.018 1.00 4.13 ? 434 TYR B CG 1 ATOM 5383 C CD1 . TYR B 1 352 ? 53.465 86.015 93.026 1.00 4.13 ? 434 TYR B CD1 1 ATOM 5384 C CD2 . TYR B 1 352 ? 51.377 86.390 94.124 1.00 4.13 ? 434 TYR B CD2 1 ATOM 5385 C CE1 . TYR B 1 352 ? 53.210 87.080 92.169 1.00 4.13 ? 434 TYR B CE1 1 ATOM 5386 C CE2 . TYR B 1 352 ? 51.112 87.455 93.273 1.00 4.13 ? 434 TYR B CE2 1 ATOM 5387 C CZ . TYR B 1 352 ? 52.031 87.797 92.299 1.00 4.13 ? 434 TYR B CZ 1 ATOM 5388 O OH . TYR B 1 352 ? 51.764 88.858 91.464 1.00 4.13 ? 434 TYR B OH 1 ATOM 5389 N N . PHE B 1 353 ? 52.180 85.084 98.091 1.00 7.79 ? 435 PHE B N 1 ATOM 5390 C CA . PHE B 1 353 ? 51.327 85.685 99.114 1.00 7.79 ? 435 PHE B CA 1 ATOM 5391 C C . PHE B 1 353 ? 52.155 86.629 99.987 1.00 7.79 ? 435 PHE B C 1 ATOM 5392 O O . PHE B 1 353 ? 51.734 87.757 100.267 1.00 7.79 ? 435 PHE B O 1 ATOM 5393 C CB . PHE B 1 353 ? 50.694 84.601 99.993 1.00 12.02 ? 435 PHE B CB 1 ATOM 5394 C CG . PHE B 1 353 ? 49.893 85.144 101.151 1.00 12.02 ? 435 PHE B CG 1 ATOM 5395 C CD1 . PHE B 1 353 ? 48.611 85.656 100.954 1.00 12.02 ? 435 PHE B CD1 1 ATOM 5396 C CD2 . PHE B 1 353 ? 50.420 85.145 102.440 1.00 12.02 ? 435 PHE B CD2 1 ATOM 5397 C CE1 . PHE B 1 353 ? 47.866 86.161 102.028 1.00 12.02 ? 435 PHE B CE1 1 ATOM 5398 C CE2 . PHE B 1 353 ? 49.687 85.646 103.515 1.00 12.02 ? 435 PHE B CE2 1 ATOM 5399 C CZ . PHE B 1 353 ? 48.408 86.155 103.308 1.00 12.02 ? 435 PHE B CZ 1 ATOM 5400 N N . VAL B 1 354 ? 53.327 86.163 100.421 1.00 10.14 ? 436 VAL B N 1 ATOM 5401 C CA . VAL B 1 354 ? 54.211 86.971 101.258 1.00 10.14 ? 436 VAL B CA 1 ATOM 5402 C C . VAL B 1 354 ? 54.624 88.247 100.520 1.00 10.14 ? 436 VAL B C 1 ATOM 5403 O O . VAL B 1 354 ? 54.701 89.322 101.119 1.00 10.14 ? 436 VAL B O 1 ATOM 5404 C CB . VAL B 1 354 ? 55.467 86.180 101.685 1.00 13.06 ? 436 VAL B CB 1 ATOM 5405 C CG1 . VAL B 1 354 ? 56.391 87.062 102.496 1.00 13.06 ? 436 VAL B CG1 1 ATOM 5406 C CG2 . VAL B 1 354 ? 55.066 84.954 102.498 1.00 13.06 ? 436 VAL B CG2 1 ATOM 5407 N N . GLN B 1 355 ? 54.865 88.127 99.215 1.00 9.84 ? 437 GLN B N 1 ATOM 5408 C CA . GLN B 1 355 ? 55.235 89.278 98.390 1.00 9.84 ? 437 GLN B CA 1 ATOM 5409 C C . GLN B 1 355 ? 54.121 90.324 98.417 1.00 9.84 ? 437 GLN B C 1 ATOM 5410 O O . GLN B 1 355 ? 54.371 91.504 98.675 1.00 9.84 ? 437 GLN B O 1 ATOM 5411 C CB . GLN B 1 355 ? 55.476 88.851 96.936 1.00 14.28 ? 437 GLN B CB 1 ATOM 5412 C CG . GLN B 1 355 ? 55.683 90.026 95.980 1.00 14.28 ? 437 GLN B CG 1 ATOM 5413 C CD . GLN B 1 355 ? 55.746 89.611 94.524 1.00 14.28 ? 437 GLN B CD 1 ATOM 5414 O OE1 . GLN B 1 355 ? 56.771 89.124 94.048 1.00 14.28 ? 437 GLN B OE1 1 ATOM 5415 N NE2 . GLN B 1 355 ? 54.653 89.828 93.801 1.00 14.28 ? 437 GLN B NE2 1 ATOM 5416 N N . LEU B 1 356 ? 52.894 89.880 98.144 1.00 4.65 ? 438 LEU B N 1 ATOM 5417 C CA . LEU B 1 356 ? 51.724 90.765 98.127 1.00 4.65 ? 438 LEU B CA 1 ATOM 5418 C C . LEU B 1 356 ? 51.520 91.448 99.472 1.00 4.65 ? 438 LEU B C 1 ATOM 5419 O O . LEU B 1 356 ? 51.220 92.643 99.533 1.00 4.65 ? 438 LEU B O 1 ATOM 5420 C CB . LEU B 1 356 ? 50.462 89.975 97.766 1.00 3.69 ? 438 LEU B CB 1 ATOM 5421 C CG . LEU B 1 356 ? 50.296 89.456 96.342 1.00 3.69 ? 438 LEU B CG 1 ATOM 5422 C CD1 . LEU B 1 356 ? 49.073 88.566 96.280 1.00 3.69 ? 438 LEU B CD1 1 ATOM 5423 C CD2 . LEU B 1 356 ? 50.154 90.609 95.383 1.00 3.69 ? 438 LEU B CD2 1 ATOM 5424 N N . LEU B 1 357 ? 51.697 90.678 100.543 1.00 9.74 ? 439 LEU B N 1 ATOM 5425 C CA . LEU B 1 357 ? 51.537 91.173 101.905 1.00 9.74 ? 439 LEU B CA 1 ATOM 5426 C C . LEU B 1 357 ? 52.593 92.231 102.229 1.00 9.74 ? 439 LEU B C 1 ATOM 5427 O O . LEU B 1 357 ? 52.292 93.260 102.828 1.00 9.74 ? 439 LEU B O 1 ATOM 5428 C CB . LEU B 1 357 ? 51.642 90.002 102.890 1.00 16.05 ? 439 LEU B CB 1 ATOM 5429 C CG . LEU B 1 357 ? 51.395 90.255 104.378 1.00 16.05 ? 439 LEU B CG 1 ATOM 5430 C CD1 . LEU B 1 357 ? 49.981 90.782 104.592 1.00 16.05 ? 439 LEU B CD1 1 ATOM 5431 C CD2 . LEU B 1 357 ? 51.602 88.967 105.156 1.00 16.05 ? 439 LEU B CD2 1 ATOM 5432 N N . THR B 1 358 ? 53.823 91.982 101.797 1.00 13.22 ? 440 THR B N 1 ATOM 5433 C CA . THR B 1 358 ? 54.931 92.895 102.040 1.00 13.22 ? 440 THR B CA 1 ATOM 5434 C C . THR B 1 358 ? 54.812 94.210 101.273 1.00 13.22 ? 440 THR B C 1 ATOM 5435 O O . THR B 1 358 ? 55.142 95.271 101.805 1.00 13.22 ? 440 THR B O 1 ATOM 5436 C CB . THR B 1 358 ? 56.281 92.219 101.695 1.00 20.52 ? 440 THR B CB 1 ATOM 5437 O OG1 . THR B 1 358 ? 56.483 91.089 102.558 1.00 20.52 ? 440 THR B OG1 1 ATOM 5438 C CG2 . THR B 1 358 ? 57.437 93.195 101.871 1.00 20.52 ? 440 THR B CG2 1 ATOM 5439 N N . ASN B 1 359 ? 54.329 94.133 100.034 1.00 9.16 ? 441 ASN B N 1 ATOM 5440 C CA . ASN B 1 359 ? 54.180 95.308 99.170 1.00 9.16 ? 441 ASN B CA 1 ATOM 5441 C C . ASN B 1 359 ? 52.793 95.952 99.211 1.00 9.16 ? 441 ASN B C 1 ATOM 5442 O O . ASN B 1 359 ? 52.509 96.854 98.413 1.00 9.16 ? 441 ASN B O 1 ATOM 5443 C CB . ASN B 1 359 ? 54.484 94.927 97.717 1.00 13.07 ? 441 ASN B CB 1 ATOM 5444 C CG . ASN B 1 359 ? 55.927 94.527 97.499 1.00 13.07 ? 441 ASN B CG 1 ATOM 5445 O OD1 . ASN B 1 359 ? 56.833 95.055 98.138 1.00 13.07 ? 441 ASN B OD1 1 ATOM 5446 N ND2 . ASN B 1 359 ? 56.151 93.609 96.568 1.00 13.07 ? 441 ASN B ND2 1 ATOM 5447 N N . ALA B 1 360 ? 51.933 95.489 100.117 1.00 7.74 ? 442 ALA B N 1 ATOM 5448 C CA . ALA B 1 360 ? 50.567 96.001 100.225 1.00 7.74 ? 442 ALA B CA 1 ATOM 5449 C C . ALA B 1 360 ? 50.450 97.512 100.425 1.00 7.74 ? 442 ALA B C 1 ATOM 5450 O O . ALA B 1 360 ? 51.260 98.128 101.124 1.00 7.74 ? 442 ALA B O 1 ATOM 5451 C CB . ALA B 1 360 ? 49.820 95.270 101.329 1.00 10.99 ? 442 ALA B CB 1 ATOM 5452 N N . ASN B 1 361 ? 49.430 98.095 99.796 1.00 10.44 ? 443 ASN B N 1 ATOM 5453 C CA . ASN B 1 361 ? 49.148 99.528 99.893 1.00 10.44 ? 443 ASN B CA 1 ATOM 5454 C C . ASN B 1 361 ? 47.669 99.759 99.561 1.00 10.44 ? 443 ASN B C 1 ATOM 5455 O O . ASN B 1 361 ? 47.266 99.648 98.404 1.00 10.44 ? 443 ASN B O 1 ATOM 5456 C CB . ASN B 1 361 ? 50.033 100.326 98.931 1.00 22.05 ? 443 ASN B CB 1 ATOM 5457 C CG . ASN B 1 361 ? 49.758 101.820 98.984 1.00 22.05 ? 443 ASN B CG 1 ATOM 5458 O OD1 . ASN B 1 361 ? 49.249 102.337 99.978 1.00 22.05 ? 443 ASN B OD1 1 ATOM 5459 N ND2 . ASN B 1 361 ? 50.090 102.520 97.905 1.00 22.05 ? 443 ASN B ND2 1 ATOM 5460 N N . PRO B 1 362 ? 46.838 100.082 100.574 1.00 10.06 ? 444 PRO B N 1 ATOM 5461 C CA . PRO B 1 362 ? 47.126 100.267 102.004 1.00 10.06 ? 444 PRO B CA 1 ATOM 5462 C C . PRO B 1 362 ? 47.849 99.083 102.641 1.00 10.06 ? 444 PRO B C 1 ATOM 5463 O O . PRO B 1 362 ? 47.609 97.929 102.288 1.00 10.06 ? 444 PRO B O 1 ATOM 5464 C CB . PRO B 1 362 ? 45.734 100.436 102.620 1.00 11.88 ? 444 PRO B CB 1 ATOM 5465 C CG . PRO B 1 362 ? 44.919 100.973 101.518 1.00 11.88 ? 444 PRO B CG 1 ATOM 5466 C CD . PRO B 1 362 ? 45.396 100.218 100.314 1.00 11.88 ? 444 PRO B CD 1 ATOM 5467 N N . SER B 1 363 ? 48.734 99.388 103.579 1.00 9.80 ? 445 SER B N 1 ATOM 5468 C CA . SER B 1 363 ? 49.507 98.367 104.273 1.00 9.80 ? 445 SER B CA 1 ATOM 5469 C C . SER B 1 363 ? 48.693 97.596 105.311 1.00 9.80 ? 445 SER B C 1 ATOM 5470 O O . SER B 1 363 ? 47.721 98.106 105.862 1.00 9.80 ? 445 SER B O 1 ATOM 5471 C CB . SER B 1 363 ? 50.717 99.019 104.956 1.00 16.31 ? 445 SER B CB 1 ATOM 5472 O OG . SER B 1 363 ? 51.486 98.063 105.665 1.00 16.31 ? 445 SER B OG 1 ATOM 5473 N N . PHE B 1 364 ? 49.074 96.344 105.530 1.00 12.74 ? 446 PHE B N 1 ATOM 5474 C CA . PHE B 1 364 ? 48.434 95.501 106.530 1.00 12.74 ? 446 PHE B CA 1 ATOM 5475 C C . PHE B 1 364 ? 49.345 95.478 107.753 1.00 12.74 ? 446 PHE B C 1 ATOM 5476 O O . PHE B 1 364 ? 48.893 95.256 108.878 1.00 12.74 ? 446 PHE B O 1 ATOM 5477 C CB . PHE B 1 364 ? 48.247 94.080 106.004 1.00 14.15 ? 446 PHE B CB 1 ATOM 5478 C CG . PHE B 1 364 ? 47.093 93.930 105.065 1.00 14.15 ? 446 PHE B CG 1 ATOM 5479 C CD1 . PHE B 1 364 ? 45.800 93.771 105.559 1.00 14.15 ? 446 PHE B CD1 1 ATOM 5480 C CD2 . PHE B 1 364 ? 47.291 93.950 103.689 1.00 14.15 ? 446 PHE B CD2 1 ATOM 5481 C CE1 . PHE B 1 364 ? 44.720 93.634 104.689 1.00 14.15 ? 446 PHE B CE1 1 ATOM 5482 C CE2 . PHE B 1 364 ? 46.219 93.814 102.816 1.00 14.15 ? 446 PHE B CE2 1 ATOM 5483 C CZ . PHE B 1 364 ? 44.933 93.654 103.317 1.00 14.15 ? 446 PHE B CZ 1 ATOM 5484 N N . LEU B 1 365 ? 50.634 95.693 107.512 1.00 32.79 ? 447 LEU B N 1 ATOM 5485 C CA . LEU B 1 365 ? 51.642 95.712 108.561 1.00 32.79 ? 447 LEU B CA 1 ATOM 5486 C C . LEU B 1 365 ? 51.696 97.072 109.249 1.00 32.79 ? 447 LEU B C 1 ATOM 5487 O O . LEU B 1 365 ? 51.565 98.100 108.550 1.00 32.79 ? 447 LEU B O 1 ATOM 5488 C CB . LEU B 1 365 ? 53.011 95.362 107.970 1.00 20.50 ? 447 LEU B CB 1 ATOM 5489 C CG . LEU B 1 365 ? 53.182 93.914 107.502 1.00 20.50 ? 447 LEU B CG 1 ATOM 5490 C CD1 . LEU B 1 365 ? 54.338 93.803 106.524 1.00 20.50 ? 447 LEU B CD1 1 ATOM 5491 C CD2 . LEU B 1 365 ? 53.399 93.015 108.704 1.00 20.50 ? 447 LEU B CD2 1 ATOM 5492 O OXT . LEU B 1 365 ? 51.864 97.094 110.486 1.00 32.79 ? 447 LEU B OXT 1 HETATM 5493 C C1 . NAG C 2 . ? 7.665 39.740 25.462 1.00 23.57 ? 501 NAG A C1 1 HETATM 5494 C C2 . NAG C 2 . ? 9.095 39.310 25.128 1.00 23.57 ? 501 NAG A C2 1 HETATM 5495 C C3 . NAG C 2 . ? 9.076 38.026 24.309 1.00 23.57 ? 501 NAG A C3 1 HETATM 5496 C C4 . NAG C 2 . ? 8.290 36.955 25.047 1.00 23.57 ? 501 NAG A C4 1 HETATM 5497 C C5 . NAG C 2 . ? 6.884 37.459 25.338 1.00 23.57 ? 501 NAG A C5 1 HETATM 5498 C C6 . NAG C 2 . ? 6.085 36.426 26.123 1.00 23.57 ? 501 NAG A C6 1 HETATM 5499 C C7 . NAG C 2 . ? 10.609 41.198 24.983 1.00 23.57 ? 501 NAG A C7 1 HETATM 5500 C C8 . NAG C 2 . ? 11.276 42.246 24.108 1.00 23.57 ? 501 NAG A C8 1 HETATM 5501 N N2 . NAG C 2 . ? 9.779 40.352 24.376 1.00 23.57 ? 501 NAG A N2 1 HETATM 5502 O O3 . NAG C 2 . ? 10.390 37.581 24.064 1.00 23.57 ? 501 NAG A O3 1 HETATM 5503 O O4 . NAG C 2 . ? 8.229 35.776 24.275 1.00 23.57 ? 501 NAG A O4 1 HETATM 5504 O O5 . NAG C 2 . ? 6.968 38.668 26.105 1.00 23.57 ? 501 NAG A O5 1 HETATM 5505 O O6 . NAG C 2 . ? 4.778 36.907 26.361 1.00 23.57 ? 501 NAG A O6 1 HETATM 5506 O O7 . NAG C 2 . ? 10.827 41.160 26.194 1.00 23.57 ? 501 NAG A O7 1 HETATM 5507 C C1 . NAG D 2 . ? 30.539 58.596 48.712 1.00 20.85 ? 502 NAG A C1 1 HETATM 5508 C C2 . NAG D 2 . ? 30.809 59.950 49.345 1.00 20.85 ? 502 NAG A C2 1 HETATM 5509 C C3 . NAG D 2 . ? 30.957 59.806 50.852 1.00 20.85 ? 502 NAG A C3 1 HETATM 5510 C C4 . NAG D 2 . ? 29.749 59.078 51.439 1.00 20.85 ? 502 NAG A C4 1 HETATM 5511 C C5 . NAG D 2 . ? 29.516 57.753 50.709 1.00 20.85 ? 502 NAG A C5 1 HETATM 5512 C C6 . NAG D 2 . ? 28.252 57.061 51.212 1.00 20.85 ? 502 NAG A C6 1 HETATM 5513 C C7 . NAG D 2 . ? 31.992 61.441 47.842 1.00 20.85 ? 502 NAG A C7 1 HETATM 5514 C C8 . NAG D 2 . ? 33.333 61.954 47.344 1.00 20.85 ? 502 NAG A C8 1 HETATM 5515 N N2 . NAG D 2 . ? 32.031 60.514 48.796 1.00 20.85 ? 502 NAG A N2 1 HETATM 5516 O O3 . NAG D 2 . ? 31.084 61.082 51.439 1.00 20.85 ? 502 NAG A O3 1 HETATM 5517 O O4 . NAG D 2 . ? 29.964 58.836 52.812 1.00 20.85 ? 502 NAG A O4 1 HETATM 5518 O O5 . NAG D 2 . ? 29.383 58.004 49.305 1.00 20.85 ? 502 NAG A O5 1 HETATM 5519 O O6 . NAG D 2 . ? 27.108 57.791 50.826 1.00 20.85 ? 502 NAG A O6 1 HETATM 5520 O O7 . NAG D 2 . ? 30.935 61.866 47.364 1.00 20.85 ? 502 NAG A O7 1 HETATM 5521 C C1 . MAN E 3 . ? -0.041 48.314 51.297 1.00 97.46 ? 503 MAN A C1 1 HETATM 5522 C C2 . MAN E 3 . ? -0.688 48.942 52.525 1.00 97.46 ? 503 MAN A C2 1 HETATM 5523 C C3 . MAN E 3 . ? -1.689 47.975 53.150 1.00 97.46 ? 503 MAN A C3 1 HETATM 5524 C C4 . MAN E 3 . ? -2.700 47.509 52.106 1.00 97.46 ? 503 MAN A C4 1 HETATM 5525 C C5 . MAN E 3 . ? -1.979 46.908 50.901 1.00 97.46 ? 503 MAN A C5 1 HETATM 5526 C C6 . MAN E 3 . ? -2.966 46.527 49.799 1.00 97.46 ? 503 MAN A C6 1 HETATM 5527 O O2 . MAN E 3 . ? -1.335 50.144 52.168 1.00 97.46 ? 503 MAN A O2 1 HETATM 5528 O O3 . MAN E 3 . ? -2.358 48.597 54.224 1.00 97.46 ? 503 MAN A O3 1 HETATM 5529 O O4 . MAN E 3 . ? -3.563 46.548 52.673 1.00 97.46 ? 503 MAN A O4 1 HETATM 5530 O O5 . MAN E 3 . ? -1.043 47.861 50.374 1.00 97.46 ? 503 MAN A O5 1 HETATM 5531 O O6 . MAN E 3 . ? -2.285 46.326 48.577 1.00 97.46 ? 503 MAN A O6 1 HETATM 5532 C C1 . MAN F 3 . ? 14.600 47.235 61.470 1.00 77.07 ? 504 MAN A C1 1 HETATM 5533 C C2 . MAN F 3 . ? 13.251 47.944 61.485 1.00 77.07 ? 504 MAN A C2 1 HETATM 5534 C C3 . MAN F 3 . ? 13.428 49.456 61.379 1.00 77.07 ? 504 MAN A C3 1 HETATM 5535 C C4 . MAN F 3 . ? 14.409 49.953 62.435 1.00 77.07 ? 504 MAN A C4 1 HETATM 5536 C C5 . MAN F 3 . ? 15.721 49.175 62.348 1.00 77.07 ? 504 MAN A C5 1 HETATM 5537 C C6 . MAN F 3 . ? 16.696 49.610 63.443 1.00 77.07 ? 504 MAN A C6 1 HETATM 5538 O O2 . MAN F 3 . ? 12.562 47.633 62.675 1.00 77.07 ? 504 MAN A O2 1 HETATM 5539 O O3 . MAN F 3 . ? 12.181 50.098 61.545 1.00 77.07 ? 504 MAN A O3 1 HETATM 5540 O O4 . MAN F 3 . ? 14.652 51.332 62.250 1.00 77.07 ? 504 MAN A O4 1 HETATM 5541 O O5 . MAN F 3 . ? 15.447 47.774 62.489 1.00 77.07 ? 504 MAN A O5 1 HETATM 5542 O O6 . MAN F 3 . ? 17.900 50.073 62.869 1.00 77.07 ? 504 MAN A O6 1 HETATM 5543 C C1 . MAN G 3 . ? 25.519 26.162 58.830 1.00 40.38 ? 505 MAN A C1 1 HETATM 5544 C C2 . MAN G 3 . ? 26.440 24.953 58.953 1.00 40.38 ? 505 MAN A C2 1 HETATM 5545 C C3 . MAN G 3 . ? 27.644 25.102 58.025 1.00 40.38 ? 505 MAN A C3 1 HETATM 5546 C C4 . MAN G 3 . ? 27.184 25.377 56.600 1.00 40.38 ? 505 MAN A C4 1 HETATM 5547 C C5 . MAN G 3 . ? 26.251 26.586 56.564 1.00 40.38 ? 505 MAN A C5 1 HETATM 5548 C C6 . MAN G 3 . ? 25.704 26.808 55.158 1.00 40.38 ? 505 MAN A C6 1 HETATM 5549 O O2 . MAN G 3 . ? 25.737 23.768 58.651 1.00 40.38 ? 505 MAN A O2 1 HETATM 5550 O O3 . MAN G 3 . ? 28.429 23.931 58.055 1.00 40.38 ? 505 MAN A O3 1 HETATM 5551 O O4 . MAN G 3 . ? 28.301 25.610 55.770 1.00 40.38 ? 505 MAN A O4 1 HETATM 5552 O O5 . MAN G 3 . ? 25.153 26.368 57.460 1.00 40.38 ? 505 MAN A O5 1 HETATM 5553 O O6 . MAN G 3 . ? 25.128 25.616 54.661 1.00 40.38 ? 505 MAN A O6 1 HETATM 5554 C C1 . MAN H 3 . ? 27.563 32.774 63.930 1.00 20.45 ? 506 MAN A C1 1 HETATM 5555 C C2 . MAN H 3 . ? 27.198 34.237 63.722 1.00 20.45 ? 506 MAN A C2 1 HETATM 5556 C C3 . MAN H 3 . ? 28.086 35.135 64.585 1.00 20.45 ? 506 MAN A C3 1 HETATM 5557 C C4 . MAN H 3 . ? 28.050 34.682 66.044 1.00 20.45 ? 506 MAN A C4 1 HETATM 5558 C C5 . MAN H 3 . ? 28.395 33.200 66.144 1.00 20.45 ? 506 MAN A C5 1 HETATM 5559 C C6 . MAN H 3 . ? 28.298 32.703 67.582 1.00 20.45 ? 506 MAN A C6 1 HETATM 5560 O O2 . MAN H 3 . ? 25.845 34.441 64.052 1.00 20.45 ? 506 MAN A O2 1 HETATM 5561 O O3 . MAN H 3 . ? 27.662 36.478 64.493 1.00 20.45 ? 506 MAN A O3 1 HETATM 5562 O O4 . MAN H 3 . ? 28.966 35.438 66.806 1.00 20.45 ? 506 MAN A O4 1 HETATM 5563 O O5 . MAN H 3 . ? 27.492 32.452 65.324 1.00 20.45 ? 506 MAN A O5 1 HETATM 5564 O O6 . MAN H 3 . ? 26.948 32.621 67.982 1.00 20.45 ? 506 MAN A O6 1 HETATM 5565 C C1 . MAN I 3 . ? 27.801 26.446 62.225 1.00 37.66 ? 507 MAN A C1 1 HETATM 5566 C C2 . MAN I 3 . ? 27.009 27.009 63.395 1.00 37.66 ? 507 MAN A C2 1 HETATM 5567 C C3 . MAN I 3 . ? 27.342 26.238 64.666 1.00 37.66 ? 507 MAN A C3 1 HETATM 5568 C C4 . MAN I 3 . ? 27.118 24.740 64.452 1.00 37.66 ? 507 MAN A C4 1 HETATM 5569 C C5 . MAN I 3 . ? 27.868 24.253 63.206 1.00 37.66 ? 507 MAN A C5 1 HETATM 5570 C C6 . MAN I 3 . ? 27.526 22.802 62.894 1.00 37.66 ? 507 MAN A C6 1 HETATM 5571 O O2 . MAN I 3 . ? 25.627 26.919 63.129 1.00 37.66 ? 507 MAN A O2 1 HETATM 5572 O O3 . MAN I 3 . ? 26.546 26.697 65.735 1.00 37.66 ? 507 MAN A O3 1 HETATM 5573 O O4 . MAN I 3 . ? 27.560 24.023 65.588 1.00 37.66 ? 507 MAN A O4 1 HETATM 5574 O O5 . MAN I 3 . ? 27.505 25.058 62.078 1.00 37.66 ? 507 MAN A O5 1 HETATM 5575 O O6 . MAN I 3 . ? 28.308 22.347 61.811 1.00 37.66 ? 507 MAN A O6 1 HETATM 5576 C C1 . MAN J 3 . ? 39.157 27.596 59.082 1.00 75.63 ? 508 MAN A C1 1 HETATM 5577 C C2 . MAN J 3 . ? 38.706 26.151 58.933 1.00 75.63 ? 508 MAN A C2 1 HETATM 5578 C C3 . MAN J 3 . ? 39.906 25.214 59.029 1.00 75.63 ? 508 MAN A C3 1 HETATM 5579 C C4 . MAN J 3 . ? 40.996 25.633 58.044 1.00 75.63 ? 508 MAN A C4 1 HETATM 5580 C C5 . MAN J 3 . ? 41.338 27.114 58.213 1.00 75.63 ? 508 MAN A C5 1 HETATM 5581 C C6 . MAN J 3 . ? 42.334 27.578 57.155 1.00 75.63 ? 508 MAN A C6 1 HETATM 5582 O O2 . MAN J 3 . ? 38.056 25.975 57.692 1.00 75.63 ? 508 MAN A O2 1 HETATM 5583 O O3 . MAN J 3 . ? 39.507 23.888 58.763 1.00 75.63 ? 508 MAN A O3 1 HETATM 5584 O O4 . MAN J 3 . ? 42.153 24.852 58.256 1.00 75.63 ? 508 MAN A O4 1 HETATM 5585 O O5 . MAN J 3 . ? 40.144 27.892 58.095 1.00 75.63 ? 508 MAN A O5 1 HETATM 5586 O O6 . MAN J 3 . ? 43.034 28.716 57.615 1.00 75.63 ? 508 MAN A O6 1 HETATM 5587 C C1 . MAN K 3 . ? 37.211 39.549 69.928 1.00 64.09 ? 509 MAN A C1 1 HETATM 5588 C C2 . MAN K 3 . ? 37.850 38.233 70.353 1.00 64.09 ? 509 MAN A C2 1 HETATM 5589 C C3 . MAN K 3 . ? 36.863 37.386 71.157 1.00 64.09 ? 509 MAN A C3 1 HETATM 5590 C C4 . MAN K 3 . ? 36.228 38.200 72.288 1.00 64.09 ? 509 MAN A C4 1 HETATM 5591 C C5 . MAN K 3 . ? 35.681 39.525 71.763 1.00 64.09 ? 509 MAN A C5 1 HETATM 5592 C C6 . MAN K 3 . ? 35.158 40.397 72.899 1.00 64.09 ? 509 MAN A C6 1 HETATM 5593 O O2 . MAN K 3 . ? 39.003 38.489 71.129 1.00 64.09 ? 509 MAN A O2 1 HETATM 5594 O O3 . MAN K 3 . ? 37.528 36.267 71.700 1.00 64.09 ? 509 MAN A O3 1 HETATM 5595 O O4 . MAN K 3 . ? 35.182 37.462 72.882 1.00 64.09 ? 509 MAN A O4 1 HETATM 5596 O O5 . MAN K 3 . ? 36.726 40.220 71.084 1.00 64.09 ? 509 MAN A O5 1 HETATM 5597 O O6 . MAN K 3 . ? 36.128 40.509 73.915 1.00 64.09 ? 509 MAN A O6 1 HETATM 5598 C C1 . NAG L 2 . ? 22.847 85.933 70.141 1.00 23.57 ? 501 NAG B C1 1 HETATM 5599 C C2 . NAG L 2 . ? 24.323 85.638 69.868 1.00 23.57 ? 501 NAG B C2 1 HETATM 5600 C C3 . NAG L 2 . ? 24.459 84.342 69.079 1.00 23.57 ? 501 NAG B C3 1 HETATM 5601 C C4 . NAG L 2 . ? 23.752 83.215 69.813 1.00 23.57 ? 501 NAG B C4 1 HETATM 5602 C C5 . NAG L 2 . ? 22.294 83.585 70.042 1.00 23.57 ? 501 NAG B C5 1 HETATM 5603 C C6 . NAG L 2 . ? 21.569 82.495 70.822 1.00 23.57 ? 501 NAG B C6 1 HETATM 5604 C C7 . NAG L 2 . ? 25.653 87.661 69.734 1.00 23.57 ? 501 NAG B C7 1 HETATM 5605 C C8 . NAG L 2 . ? 26.248 88.751 68.860 1.00 23.57 ? 501 NAG B C8 1 HETATM 5606 N N2 . NAG L 2 . ? 24.932 86.726 69.118 1.00 23.57 ? 501 NAG B N2 1 HETATM 5607 O O3 . NAG L 2 . ? 25.818 84.022 68.892 1.00 23.57 ? 501 NAG B O3 1 HETATM 5608 O O4 . NAG L 2 . ? 23.834 82.021 69.067 1.00 23.57 ? 501 NAG B O4 1 HETATM 5609 O O5 . NAG L 2 . ? 22.232 84.812 70.783 1.00 23.57 ? 501 NAG B O5 1 HETATM 5610 O O6 . NAG L 2 . ? 20.214 82.852 71.001 1.00 23.57 ? 501 NAG B O6 1 HETATM 5611 O O7 . NAG L 2 . ? 25.827 87.668 70.953 1.00 23.57 ? 501 NAG B O7 1 HETATM 5612 C C1 . NAG M 2 . ? 42.903 107.372 93.752 1.00 20.85 ? 502 NAG B C1 1 HETATM 5613 C C2 . NAG M 2 . ? 43.017 108.757 94.363 1.00 20.85 ? 502 NAG B C2 1 HETATM 5614 C C3 . NAG M 2 . ? 43.121 108.658 95.877 1.00 20.85 ? 502 NAG B C3 1 HETATM 5615 C C4 . NAG M 2 . ? 41.967 107.828 96.438 1.00 20.85 ? 502 NAG B C4 1 HETATM 5616 C C5 . NAG M 2 . ? 41.891 106.472 95.730 1.00 20.85 ? 502 NAG B C5 1 HETATM 5617 C C6 . NAG M 2 . ? 40.681 105.671 96.204 1.00 20.85 ? 502 NAG B C6 1 HETATM 5618 C C7 . NAG M 2 . ? 44.107 110.327 92.869 1.00 20.85 ? 502 NAG B C7 1 HETATM 5619 C C8 . NAG M 2 . ? 45.410 110.957 92.408 1.00 20.85 ? 502 NAG B C8 1 HETATM 5620 N N2 . NAG M 2 . ? 44.199 109.427 93.845 1.00 20.85 ? 502 NAG B N2 1 HETATM 5621 O O3 . NAG M 2 . ? 43.102 109.952 96.439 1.00 20.85 ? 502 NAG B O3 1 HETATM 5622 O O4 . NAG M 2 . ? 42.153 107.635 97.823 1.00 20.85 ? 502 NAG B O4 1 HETATM 5623 O O5 . NAG M 2 . ? 41.788 106.682 94.317 1.00 20.85 ? 502 NAG B O5 1 HETATM 5624 O O6 . NAG M 2 . ? 39.488 106.279 95.760 1.00 20.85 ? 502 NAG B O6 1 HETATM 5625 O O7 . NAG M 2 . ? 43.033 110.638 92.344 1.00 20.85 ? 502 NAG B O7 1 HETATM 5626 C C1 . MAN N 3 . ? 13.379 94.222 95.479 1.00 97.46 ? 503 MAN B C1 1 HETATM 5627 C C2 . MAN N 3 . ? 12.629 94.809 96.668 1.00 97.46 ? 503 MAN B C2 1 HETATM 5628 C C3 . MAN N 3 . ? 11.702 93.761 97.279 1.00 97.46 ? 503 MAN B C3 1 HETATM 5629 C C4 . MAN N 3 . ? 10.781 93.179 96.210 1.00 97.46 ? 503 MAN B C4 1 HETATM 5630 C C5 . MAN N 3 . ? 11.602 92.628 95.046 1.00 97.46 ? 503 MAN B C5 1 HETATM 5631 C C6 . MAN N 3 . ? 10.698 92.131 93.919 1.00 97.46 ? 503 MAN B C6 1 HETATM 5632 O O2 . MAN N 3 . ? 11.883 95.935 96.260 1.00 97.46 ? 503 MAN B O2 1 HETATM 5633 O O3 . MAN N 3 . ? 10.936 94.336 98.314 1.00 97.46 ? 503 MAN B O3 1 HETATM 5634 O O4 . MAN N 3 . ? 9.994 92.150 96.768 1.00 97.46 ? 503 MAN B O4 1 HETATM 5635 O O5 . MAN N 3 . ? 12.461 93.656 94.531 1.00 97.46 ? 503 MAN B O5 1 HETATM 5636 O O6 . MAN N 3 . ? 11.441 91.973 92.727 1.00 97.46 ? 503 MAN B O6 1 HETATM 5637 C C1 . MAN O 3 . ? 27.660 94.769 106.191 1.00 77.07 ? 504 MAN B C1 1 HETATM 5638 C C2 . MAN O 3 . ? 26.250 95.344 106.142 1.00 77.07 ? 504 MAN B C2 1 HETATM 5639 C C3 . MAN O 3 . ? 26.284 96.863 106.007 1.00 77.07 ? 504 MAN B C3 1 HETATM 5640 C C4 . MAN O 3 . ? 27.172 97.474 107.086 1.00 77.07 ? 504 MAN B C4 1 HETATM 5641 C C5 . MAN O 3 . ? 28.555 96.825 107.064 1.00 77.07 ? 504 MAN B C5 1 HETATM 5642 C C6 . MAN O 3 . ? 29.442 97.374 108.182 1.00 77.07 ? 504 MAN B C6 1 HETATM 5643 O O2 . MAN O 3 . ? 25.549 94.990 107.313 1.00 77.07 ? 504 MAN B O2 1 HETATM 5644 O O3 . MAN O 3 . ? 24.976 97.384 106.113 1.00 77.07 ? 504 MAN B O3 1 HETATM 5645 O O4 . MAN O 3 . ? 27.288 98.866 106.878 1.00 77.07 ? 504 MAN B O4 1 HETATM 5646 O O5 . MAN O 3 . ? 28.412 95.407 107.227 1.00 77.07 ? 504 MAN B O5 1 HETATM 5647 O O6 . MAN O 3 . ? 30.616 97.940 107.641 1.00 77.07 ? 504 MAN B O6 1 HETATM 5648 C C1 . MAN P 3 . ? 40.649 74.807 104.431 1.00 40.38 ? 505 MAN B C1 1 HETATM 5649 C C2 . MAN P 3 . ? 41.677 73.696 104.615 1.00 40.38 ? 505 MAN B C2 1 HETATM 5650 C C3 . MAN P 3 . ? 42.896 73.943 103.728 1.00 40.38 ? 505 MAN B C3 1 HETATM 5651 C C4 . MAN P 3 . ? 42.465 74.144 102.281 1.00 40.38 ? 505 MAN B C4 1 HETATM 5652 C C5 . MAN P 3 . ? 41.422 75.256 102.184 1.00 40.38 ? 505 MAN B C5 1 HETATM 5653 C C6 . MAN P 3 . ? 40.910 75.396 100.754 1.00 40.38 ? 505 MAN B C6 1 HETATM 5654 O O2 . MAN P 3 . ? 41.103 72.443 104.316 1.00 40.38 ? 505 MAN B O2 1 HETATM 5655 O O3 . MAN P 3 . ? 43.788 72.855 103.813 1.00 40.38 ? 505 MAN B O3 1 HETATM 5656 O O4 . MAN P 3 . ? 43.585 74.468 101.486 1.00 40.38 ? 505 MAN B O4 1 HETATM 5657 O O5 . MAN P 3 . ? 40.317 74.950 103.045 1.00 40.38 ? 505 MAN B O5 1 HETATM 5658 O O6 . MAN P 3 . ? 40.471 74.145 100.265 1.00 40.38 ? 505 MAN B O6 1 HETATM 5659 C C1 . MAN Q 3 . ? 41.853 81.685 109.447 1.00 20.45 ? 506 MAN B C1 1 HETATM 5660 C C2 . MAN Q 3 . ? 41.357 83.101 109.192 1.00 20.45 ? 506 MAN B C2 1 HETATM 5661 C C3 . MAN Q 3 . ? 42.121 84.098 110.066 1.00 20.45 ? 506 MAN B C3 1 HETATM 5662 C C4 . MAN Q 3 . ? 42.074 83.672 111.532 1.00 20.45 ? 506 MAN B C4 1 HETATM 5663 C C5 . MAN Q 3 . ? 42.556 82.233 111.679 1.00 20.45 ? 506 MAN B C5 1 HETATM 5664 C C6 . MAN Q 3 . ? 42.453 81.757 113.124 1.00 20.45 ? 506 MAN B C6 1 HETATM 5665 O O2 . MAN Q 3 . ? 39.979 83.179 109.469 1.00 20.45 ? 506 MAN B O2 1 HETATM 5666 O O3 . MAN Q 3 . ? 41.573 85.391 109.927 1.00 20.45 ? 506 MAN B O3 1 HETATM 5667 O O4 . MAN Q 3 . ? 42.883 84.528 112.309 1.00 20.45 ? 506 MAN B O4 1 HETATM 5668 O O5 . MAN Q 3 . ? 41.760 81.385 110.845 1.00 20.45 ? 506 MAN B O5 1 HETATM 5669 O O6 . MAN Q 3 . ? 41.103 81.552 113.477 1.00 20.45 ? 506 MAN B O6 1 HETATM 5670 C C1 . MAN R 3 . ? 42.763 75.378 107.898 1.00 37.66 ? 507 MAN B C1 1 HETATM 5671 C C2 . MAN R 3 . ? 41.877 75.884 109.026 1.00 37.66 ? 507 MAN B C2 1 HETATM 5672 C C3 . MAN R 3 . ? 42.234 75.174 110.326 1.00 37.66 ? 507 MAN B C3 1 HETATM 5673 C C4 . MAN R 3 . ? 42.164 73.658 110.138 1.00 37.66 ? 507 MAN B C4 1 HETATM 5674 C C5 . MAN R 3 . ? 43.004 73.221 108.932 1.00 37.66 ? 507 MAN B C5 1 HETATM 5675 C C6 . MAN R 3 . ? 42.815 71.738 108.641 1.00 37.66 ? 507 MAN B C6 1 HETATM 5676 O O2 . MAN R 3 . ? 40.521 75.655 108.713 1.00 37.66 ? 507 MAN B O2 1 HETATM 5677 O O3 . MAN R 3 . ? 41.358 75.574 111.355 1.00 37.66 ? 507 MAN B O3 1 HETATM 5678 O O4 . MAN R 3 . ? 42.630 73.009 111.306 1.00 37.66 ? 507 MAN B O4 1 HETATM 5679 O O5 . MAN R 3 . ? 42.608 73.965 107.773 1.00 37.66 ? 507 MAN B O5 1 HETATM 5680 O O6 . MAN R 3 . ? 43.678 71.340 107.598 1.00 37.66 ? 507 MAN B O6 1 HETATM 5681 C C1 . MAN S 3 . ? 54.067 77.563 105.138 1.00 75.63 ? 508 MAN B C1 1 HETATM 5682 C C2 . MAN S 3 . ? 53.763 76.078 105.006 1.00 75.63 ? 508 MAN B C2 1 HETATM 5683 C C3 . MAN S 3 . ? 55.043 75.264 105.167 1.00 75.63 ? 508 MAN B C3 1 HETATM 5684 C C4 . MAN S 3 . ? 56.124 75.768 104.212 1.00 75.63 ? 508 MAN B C4 1 HETATM 5685 C C5 . MAN S 3 . ? 56.315 77.278 104.359 1.00 75.63 ? 508 MAN B C5 1 HETATM 5686 C C6 . MAN S 3 . ? 57.301 77.816 103.327 1.00 75.63 ? 508 MAN B C6 1 HETATM 5687 O O2 . MAN S 3 . ? 53.180 75.816 103.747 1.00 75.63 ? 508 MAN B O2 1 HETATM 5688 O O3 . MAN S 3 . ? 54.784 73.901 104.918 1.00 75.63 ? 508 MAN B O3 1 HETATM 5689 O O4 . MAN S 3 . ? 57.342 75.107 104.483 1.00 75.63 ? 508 MAN B O4 1 HETATM 5690 O O5 . MAN S 3 . ? 55.057 77.934 104.180 1.00 75.63 ? 508 MAN B O5 1 HETATM 5691 O O6 . MAN S 3 . ? 57.871 79.025 103.785 1.00 75.63 ? 508 MAN B O6 1 HETATM 5692 C C1 . MAN T 3 . ? 50.570 89.480 115.628 1.00 64.09 ? 509 MAN B C1 1 HETATM 5693 C C2 . MAN T 3 . ? 51.316 88.241 116.106 1.00 64.09 ? 509 MAN B C2 1 HETATM 5694 C C3 . MAN T 3 . ? 50.385 87.318 116.894 1.00 64.09 ? 509 MAN B C3 1 HETATM 5695 C C4 . MAN T 3 . ? 49.633 88.089 117.982 1.00 64.09 ? 509 MAN B C4 1 HETATM 5696 C C5 . MAN T 3 . ? 48.981 89.344 117.407 1.00 64.09 ? 509 MAN B C5 1 HETATM 5697 C C6 . MAN T 3 . ? 48.334 90.183 118.503 1.00 64.09 ? 509 MAN B C6 1 HETATM 5698 O O2 . MAN T 3 . ? 52.409 88.623 116.917 1.00 64.09 ? 509 MAN B O2 1 HETATM 5699 O O3 . MAN T 3 . ? 51.134 86.280 117.486 1.00 64.09 ? 509 MAN B O3 1 HETATM 5700 O O4 . MAN T 3 . ? 48.641 87.265 118.555 1.00 64.09 ? 509 MAN B O4 1 HETATM 5701 O O5 . MAN T 3 . ? 49.979 90.124 116.750 1.00 64.09 ? 509 MAN B O5 1 HETATM 5702 O O6 . MAN T 3 . ? 49.249 90.409 119.551 1.00 64.09 ? 509 MAN B O6 1 HETATM 5703 O O . HOH U 4 . ? 29.290 41.798 47.062 1.00 2.00 ? 601 HOH A O 1 HETATM 5704 O O . HOH U 4 . ? 30.852 45.024 45.302 1.00 4.50 ? 602 HOH A O 1 HETATM 5705 O O . HOH U 4 . ? 22.322 43.755 51.559 1.00 2.00 ? 603 HOH A O 1 HETATM 5706 O O . HOH U 4 . ? 24.898 43.782 38.025 1.00 3.33 ? 604 HOH A O 1 HETATM 5707 O O . HOH U 4 . ? 37.292 46.405 46.843 1.00 2.00 ? 605 HOH A O 1 HETATM 5708 O O . HOH U 4 . ? 30.757 41.532 44.706 1.00 6.89 ? 606 HOH A O 1 HETATM 5709 O O . HOH U 4 . ? 20.034 26.912 34.791 1.00 11.88 ? 607 HOH A O 1 HETATM 5710 O O . HOH U 4 . ? 24.488 33.138 51.332 1.00 6.07 ? 608 HOH A O 1 HETATM 5711 O O . HOH U 4 . ? 21.995 41.141 33.128 1.00 6.03 ? 609 HOH A O 1 HETATM 5712 O O . HOH U 4 . ? 33.520 36.199 47.807 1.00 8.57 ? 610 HOH A O 1 HETATM 5713 O O . HOH U 4 . ? 23.864 35.857 51.989 1.00 7.19 ? 611 HOH A O 1 HETATM 5714 O O . HOH U 4 . ? 22.266 34.061 32.279 1.00 9.24 ? 612 HOH A O 1 HETATM 5715 O O . HOH U 4 . ? 40.516 32.101 41.712 1.00 8.32 ? 613 HOH A O 1 HETATM 5716 O O . HOH U 4 . ? 20.150 45.427 52.143 1.00 10.00 ? 614 HOH A O 1 HETATM 5717 O O . HOH U 4 . ? 19.441 48.259 52.897 1.00 13.46 ? 615 HOH A O 1 HETATM 5718 O O . HOH U 4 . ? 21.065 34.639 34.751 1.00 11.05 ? 616 HOH A O 1 HETATM 5719 O O . HOH U 4 . ? 37.162 49.948 40.565 1.00 7.81 ? 617 HOH A O 1 HETATM 5720 O O . HOH U 4 . ? 17.540 32.884 58.125 1.00 7.49 ? 618 HOH A O 1 HETATM 5721 O O . HOH U 4 . ? 36.187 47.473 39.796 1.00 9.58 ? 619 HOH A O 1 HETATM 5722 O O . HOH U 4 . ? 34.927 51.691 39.780 1.00 11.06 ? 620 HOH A O 1 HETATM 5723 O O . HOH U 4 . ? 8.903 41.407 29.376 1.00 10.40 ? 621 HOH A O 1 HETATM 5724 O O . HOH U 4 . ? 8.371 42.781 55.966 1.00 11.28 ? 622 HOH A O 1 HETATM 5725 O O . HOH U 4 . ? 32.609 47.315 55.347 1.00 11.10 ? 623 HOH A O 1 HETATM 5726 O O . HOH U 4 . ? 11.171 39.917 28.494 1.00 8.62 ? 624 HOH A O 1 HETATM 5727 O O . HOH U 4 . ? 32.301 38.082 39.787 1.00 9.55 ? 625 HOH A O 1 HETATM 5728 O O . HOH U 4 . ? 22.050 28.763 23.587 1.00 14.27 ? 626 HOH A O 1 HETATM 5729 O O . HOH U 4 . ? 32.212 50.441 48.881 1.00 7.94 ? 627 HOH A O 1 HETATM 5730 O O . HOH U 4 . ? 38.854 36.847 36.367 1.00 12.30 ? 628 HOH A O 1 HETATM 5731 O O . HOH U 4 . ? 41.232 29.189 51.698 1.00 18.64 ? 629 HOH A O 1 HETATM 5732 O O . HOH U 4 . ? 28.925 52.487 55.318 1.00 10.72 ? 630 HOH A O 1 HETATM 5733 O O . HOH U 4 . ? 23.223 32.439 48.934 1.00 17.97 ? 631 HOH A O 1 HETATM 5734 O O . HOH U 4 . ? 18.729 59.194 49.227 1.00 13.65 ? 632 HOH A O 1 HETATM 5735 O O . HOH U 4 . ? 21.741 25.846 38.520 1.00 12.92 ? 633 HOH A O 1 HETATM 5736 O O . HOH U 4 . ? 18.923 41.164 33.366 1.00 13.72 ? 634 HOH A O 1 HETATM 5737 O O . HOH U 4 . ? 29.481 39.960 20.523 1.00 10.72 ? 635 HOH A O 1 HETATM 5738 O O . HOH U 4 . ? 9.638 51.375 38.151 1.00 13.47 ? 636 HOH A O 1 HETATM 5739 O O . HOH U 4 . ? 35.585 35.068 46.066 1.00 11.66 ? 637 HOH A O 1 HETATM 5740 O O . HOH U 4 . ? 17.738 21.848 41.750 1.00 17.01 ? 638 HOH A O 1 HETATM 5741 O O . HOH U 4 . ? 40.402 37.852 38.503 1.00 17.11 ? 639 HOH A O 1 HETATM 5742 O O . HOH U 4 . ? 27.807 35.209 30.376 1.00 16.33 ? 640 HOH A O 1 HETATM 5743 O O . HOH U 4 . ? 24.167 36.708 57.677 1.00 11.23 ? 641 HOH A O 1 HETATM 5744 O O . HOH U 4 . ? 40.755 47.049 31.499 1.00 13.59 ? 642 HOH A O 1 HETATM 5745 O O . HOH U 4 . ? 26.316 58.716 48.353 1.00 24.24 ? 643 HOH A O 1 HETATM 5746 O O . HOH U 4 . ? 38.257 45.473 58.883 1.00 13.04 ? 644 HOH A O 1 HETATM 5747 O O . HOH U 4 . ? 26.058 52.840 54.660 1.00 12.03 ? 645 HOH A O 1 HETATM 5748 O O . HOH U 4 . ? 24.505 55.119 23.627 1.00 10.77 ? 646 HOH A O 1 HETATM 5749 O O . HOH U 4 . ? 17.049 21.359 31.215 1.00 13.73 ? 647 HOH A O 1 HETATM 5750 O O . HOH U 4 . ? 15.747 56.658 36.330 1.00 17.83 ? 648 HOH A O 1 HETATM 5751 O O . HOH U 4 . ? 2.892 47.276 47.433 1.00 14.30 ? 649 HOH A O 1 HETATM 5752 O O . HOH U 4 . ? 27.867 32.836 45.998 1.00 20.83 ? 650 HOH A O 1 HETATM 5753 O O . HOH U 4 . ? 23.323 38.236 55.503 1.00 14.40 ? 651 HOH A O 1 HETATM 5754 O O . HOH U 4 . ? 27.601 42.847 37.368 1.00 16.81 ? 652 HOH A O 1 HETATM 5755 O O . HOH U 4 . ? 11.958 23.374 37.509 1.00 14.47 ? 653 HOH A O 1 HETATM 5756 O O . HOH U 4 . ? 34.088 45.104 38.479 1.00 15.88 ? 654 HOH A O 1 HETATM 5757 O O . HOH U 4 . ? 13.484 56.295 34.581 1.00 16.50 ? 655 HOH A O 1 HETATM 5758 O O . HOH U 4 . ? 6.671 50.105 37.992 1.00 22.10 ? 656 HOH A O 1 HETATM 5759 O O . HOH U 4 . ? 14.618 56.332 46.585 1.00 24.88 ? 657 HOH A O 1 HETATM 5760 O O . HOH U 4 . ? 44.868 47.567 39.655 1.00 24.12 ? 658 HOH A O 1 HETATM 5761 O O . HOH U 4 . ? 16.796 37.021 53.134 1.00 13.93 ? 659 HOH A O 1 HETATM 5762 O O . HOH U 4 . ? 30.098 40.986 50.751 1.00 18.34 ? 660 HOH A O 1 HETATM 5763 O O . HOH U 4 . ? 32.787 54.028 46.503 1.00 23.18 ? 661 HOH A O 1 HETATM 5764 O O . HOH U 4 . ? 16.482 59.539 35.653 1.00 22.40 ? 662 HOH A O 1 HETATM 5765 O O . HOH U 4 . ? 24.358 26.885 40.308 1.00 29.63 ? 663 HOH A O 1 HETATM 5766 O O . HOH U 4 . ? 33.930 52.104 50.889 1.00 17.94 ? 664 HOH A O 1 HETATM 5767 O O . HOH U 4 . ? 26.877 39.683 54.915 1.00 20.71 ? 665 HOH A O 1 HETATM 5768 O O . HOH U 4 . ? 34.059 32.993 31.563 1.00 20.42 ? 666 HOH A O 1 HETATM 5769 O O . HOH U 4 . ? 7.345 36.740 50.454 1.00 19.55 ? 667 HOH A O 1 HETATM 5770 O O . HOH U 4 . ? 34.448 42.633 35.883 1.00 15.67 ? 668 HOH A O 1 HETATM 5771 O O . HOH U 4 . ? 1.149 45.813 37.845 1.00 20.65 ? 669 HOH A O 1 HETATM 5772 O O . HOH U 4 . ? 4.369 45.630 44.298 1.00 18.38 ? 670 HOH A O 1 HETATM 5773 O O . HOH U 4 . ? 16.151 30.767 22.615 1.00 18.31 ? 671 HOH A O 1 HETATM 5774 O O . HOH U 4 . ? 14.982 20.564 38.492 1.00 22.33 ? 672 HOH A O 1 HETATM 5775 O O . HOH U 4 . ? 2.017 37.841 48.018 1.00 27.49 ? 673 HOH A O 1 HETATM 5776 O O . HOH U 4 . ? 10.725 23.992 27.142 1.00 18.04 ? 674 HOH A O 1 HETATM 5777 O O . HOH U 4 . ? 25.547 40.969 35.529 1.00 28.47 ? 675 HOH A O 1 HETATM 5778 O O . HOH U 4 . ? 42.007 31.582 58.261 1.00 20.23 ? 676 HOH A O 1 HETATM 5779 O O . HOH U 4 . ? 20.712 24.362 24.913 1.00 20.40 ? 677 HOH A O 1 HETATM 5780 O O . HOH U 4 . ? 32.033 30.158 38.097 1.00 29.86 ? 678 HOH A O 1 HETATM 5781 O O . HOH U 4 . ? 30.844 37.829 21.734 1.00 20.16 ? 679 HOH A O 1 HETATM 5782 O O . HOH U 4 . ? 26.384 39.607 37.987 1.00 17.45 ? 680 HOH A O 1 HETATM 5783 O O . HOH U 4 . ? 7.377 51.770 44.152 1.00 30.21 ? 681 HOH A O 1 HETATM 5784 O O . HOH U 4 . ? 33.493 26.139 40.037 1.00 22.63 ? 682 HOH A O 1 HETATM 5785 O O . HOH U 4 . ? 43.711 47.058 45.804 1.00 23.33 ? 683 HOH A O 1 HETATM 5786 O O . HOH U 4 . ? 13.414 24.855 26.230 1.00 17.17 ? 684 HOH A O 1 HETATM 5787 O O . HOH U 4 . ? 19.325 37.849 53.729 1.00 20.06 ? 685 HOH A O 1 HETATM 5788 O O . HOH U 4 . ? 44.340 50.291 46.604 1.00 33.50 ? 686 HOH A O 1 HETATM 5789 O O . HOH U 4 . ? 22.448 60.323 29.705 1.00 22.29 ? 687 HOH A O 1 HETATM 5790 O O . HOH U 4 . ? 4.603 24.024 37.574 1.00 18.86 ? 688 HOH A O 1 HETATM 5791 O O . HOH U 4 . ? 18.870 40.417 61.027 1.00 21.56 ? 689 HOH A O 1 HETATM 5792 O O . HOH U 4 . ? 6.460 26.152 46.882 1.00 21.91 ? 690 HOH A O 1 HETATM 5793 O O . HOH U 4 . ? 3.172 30.867 38.757 1.00 19.05 ? 691 HOH A O 1 HETATM 5794 O O . HOH U 4 . ? 7.918 49.016 43.032 1.00 22.35 ? 692 HOH A O 1 HETATM 5795 O O . HOH U 4 . ? 17.923 19.640 38.128 1.00 17.88 ? 693 HOH A O 1 HETATM 5796 O O . HOH U 4 . ? 28.056 60.679 46.525 1.00 23.63 ? 694 HOH A O 1 HETATM 5797 O O . HOH U 4 . ? 38.154 56.684 33.470 1.00 20.42 ? 695 HOH A O 1 HETATM 5798 O O . HOH U 4 . ? 40.602 49.647 52.476 1.00 25.97 ? 696 HOH A O 1 HETATM 5799 O O . HOH U 4 . ? 7.293 44.621 57.944 1.00 34.71 ? 697 HOH A O 1 HETATM 5800 O O . HOH U 4 . ? 16.725 56.317 49.237 1.00 24.25 ? 698 HOH A O 1 HETATM 5801 O O . HOH U 4 . ? 31.908 53.934 23.961 1.00 18.16 ? 699 HOH A O 1 HETATM 5802 O O . HOH U 4 . ? 10.946 35.125 23.326 1.00 29.62 ? 700 HOH A O 1 HETATM 5803 O O . HOH U 4 . ? 13.724 33.847 64.015 1.00 32.36 ? 701 HOH A O 1 HETATM 5804 O O . HOH U 4 . ? 26.727 60.290 34.568 1.00 23.47 ? 702 HOH A O 1 HETATM 5805 O O . HOH U 4 . ? 28.576 39.295 52.601 1.00 19.53 ? 703 HOH A O 1 HETATM 5806 O O . HOH U 4 . ? 4.951 32.986 28.230 1.00 57.28 ? 704 HOH A O 1 HETATM 5807 O O . HOH U 4 . ? 9.817 56.185 49.109 1.00 31.58 ? 705 HOH A O 1 HETATM 5808 O O . HOH U 4 . ? 38.296 27.707 52.503 1.00 25.38 ? 706 HOH A O 1 HETATM 5809 O O . HOH U 4 . ? 31.331 25.438 51.654 1.00 25.38 ? 707 HOH A O 1 HETATM 5810 O O . HOH U 4 . ? 13.614 58.051 38.982 1.00 25.86 ? 708 HOH A O 1 HETATM 5811 O O . HOH U 4 . ? 44.559 52.711 39.427 1.00 26.34 ? 709 HOH A O 1 HETATM 5812 O O . HOH U 4 . ? 25.902 42.097 21.009 1.00 25.99 ? 710 HOH A O 1 HETATM 5813 O O . HOH U 4 . ? 35.750 28.188 37.723 1.00 35.74 ? 711 HOH A O 1 HETATM 5814 O O . HOH U 4 . ? 32.178 30.638 35.258 1.00 22.91 ? 712 HOH A O 1 HETATM 5815 O O . HOH U 4 . ? 30.303 32.591 39.870 1.00 28.66 ? 713 HOH A O 1 HETATM 5816 O O . HOH U 4 . ? 29.094 29.779 21.633 1.00 32.79 ? 714 HOH A O 1 HETATM 5817 O O . HOH U 4 . ? 31.544 41.158 67.017 1.00 26.72 ? 715 HOH A O 1 HETATM 5818 O O . HOH U 4 . ? 5.981 29.503 58.875 1.00 23.57 ? 716 HOH A O 1 HETATM 5819 O O . HOH U 4 . ? 34.295 57.655 27.572 1.00 29.10 ? 717 HOH A O 1 HETATM 5820 O O . HOH U 4 . ? 34.703 52.180 47.818 1.00 26.46 ? 718 HOH A O 1 HETATM 5821 O O . HOH U 4 . ? 8.326 52.938 51.324 1.00 35.56 ? 719 HOH A O 1 HETATM 5822 O O . HOH U 4 . ? 40.942 60.246 44.377 1.00 31.71 ? 720 HOH A O 1 HETATM 5823 O O . HOH U 4 . ? 2.344 29.201 41.165 1.00 28.08 ? 721 HOH A O 1 HETATM 5824 O O . HOH U 4 . ? 43.614 29.222 49.820 1.00 36.89 ? 722 HOH A O 1 HETATM 5825 O O . HOH U 4 . ? 18.173 52.208 55.821 1.00 34.23 ? 723 HOH A O 1 HETATM 5826 O O . HOH U 4 . ? 40.378 47.500 57.260 1.00 26.35 ? 724 HOH A O 1 HETATM 5827 O O . HOH U 4 . ? 19.295 46.371 22.461 1.00 52.25 ? 725 HOH A O 1 HETATM 5828 O O . HOH U 4 . ? 35.290 24.950 51.040 1.00 28.89 ? 726 HOH A O 1 HETATM 5829 O O . HOH U 4 . ? 21.299 41.737 62.190 1.00 36.20 ? 727 HOH A O 1 HETATM 5830 O O . HOH U 4 . ? 32.199 61.271 42.865 1.00 39.26 ? 728 HOH A O 1 HETATM 5831 O O . HOH U 4 . ? 39.931 52.358 49.374 1.00 37.07 ? 729 HOH A O 1 HETATM 5832 O O . HOH U 4 . ? 29.745 30.168 26.264 1.00 37.50 ? 730 HOH A O 1 HETATM 5833 O O . HOH U 4 . ? 17.190 33.292 19.771 1.00 23.98 ? 731 HOH A O 1 HETATM 5834 O O . HOH U 4 . ? 4.430 48.832 45.020 1.00 30.92 ? 732 HOH A O 1 HETATM 5835 O O . HOH U 4 . ? 32.546 27.341 37.391 1.00 47.07 ? 733 HOH A O 1 HETATM 5836 O O . HOH U 4 . ? 25.267 30.972 47.476 1.00 39.52 ? 734 HOH A O 1 HETATM 5837 O O . HOH U 4 . ? 4.024 50.221 54.190 1.00 36.15 ? 735 HOH A O 1 HETATM 5838 O O . HOH U 4 . ? 27.870 59.593 29.922 1.00 38.57 ? 736 HOH A O 1 HETATM 5839 O O . HOH U 4 . ? 31.044 60.305 40.369 1.00 31.55 ? 737 HOH A O 1 HETATM 5840 O O . HOH U 4 . ? 30.573 36.086 39.235 1.00 38.06 ? 738 HOH A O 1 HETATM 5841 O O . HOH U 4 . ? 10.023 26.122 56.505 1.00 27.70 ? 739 HOH A O 1 HETATM 5842 O O . HOH U 4 . ? 13.215 39.843 66.553 1.00 39.82 ? 740 HOH A O 1 HETATM 5843 O O . HOH U 4 . ? 27.757 44.250 62.292 1.00 30.17 ? 741 HOH A O 1 HETATM 5844 O O . HOH U 4 . ? 0.973 29.188 48.412 1.00 44.64 ? 742 HOH A O 1 HETATM 5845 O O . HOH U 4 . ? 44.048 36.146 52.729 1.00 23.63 ? 743 HOH A O 1 HETATM 5846 O O . HOH U 4 . ? 33.201 61.657 34.134 1.00 46.49 ? 744 HOH A O 1 HETATM 5847 O O . HOH U 4 . ? 6.318 24.437 33.136 1.00 20.59 ? 745 HOH A O 1 HETATM 5848 O O . HOH U 4 . ? 24.783 51.817 57.444 1.00 45.21 ? 746 HOH A O 1 HETATM 5849 O O . HOH U 4 . ? 43.336 31.850 55.390 1.00 36.62 ? 747 HOH A O 1 HETATM 5850 O O . HOH U 4 . ? 38.673 43.903 30.194 1.00 22.40 ? 748 HOH A O 1 HETATM 5851 O O . HOH U 4 . ? 7.371 23.835 54.752 1.00 34.48 ? 749 HOH A O 1 HETATM 5852 O O . HOH U 4 . ? 2.901 35.189 32.590 1.00 35.44 ? 750 HOH A O 1 HETATM 5853 O O . HOH U 4 . ? 4.794 37.891 62.329 1.00 35.70 ? 751 HOH A O 1 HETATM 5854 O O . HOH U 4 . ? 29.642 34.659 41.923 1.00 50.62 ? 752 HOH A O 1 HETATM 5855 O O . HOH U 4 . ? 37.049 52.613 58.789 1.00 41.54 ? 753 HOH A O 1 HETATM 5856 O O . HOH U 4 . ? 27.265 29.537 36.483 1.00 45.02 ? 754 HOH A O 1 HETATM 5857 O O . HOH U 4 . ? 23.331 37.209 61.727 1.00 28.46 ? 755 HOH A O 1 HETATM 5858 O O . HOH U 4 . ? 33.777 36.100 31.497 1.00 41.58 ? 756 HOH A O 1 HETATM 5859 O O . HOH U 4 . ? 12.613 27.072 23.813 1.00 40.43 ? 757 HOH A O 1 HETATM 5860 O O . HOH U 4 . ? 4.448 38.809 59.747 1.00 44.02 ? 758 HOH A O 1 HETATM 5861 O O . HOH U 4 . ? 16.828 58.173 46.802 1.00 37.35 ? 759 HOH A O 1 HETATM 5862 O O . HOH U 4 . ? 6.502 26.328 28.410 1.00 42.24 ? 760 HOH A O 1 HETATM 5863 O O . HOH U 4 . ? 37.708 31.823 67.479 1.00 46.71 ? 761 HOH A O 1 HETATM 5864 O O . HOH U 4 . ? 23.085 30.346 61.668 1.00 26.97 ? 762 HOH A O 1 HETATM 5865 O O . HOH U 4 . ? 29.945 61.893 44.421 1.00 31.32 ? 763 HOH A O 1 HETATM 5866 O O . HOH U 4 . ? 24.617 36.887 64.212 1.00 42.51 ? 764 HOH A O 1 HETATM 5867 O O . HOH U 4 . ? 8.679 26.669 60.217 1.00 52.44 ? 765 HOH A O 1 HETATM 5868 O O . HOH U 4 . ? 44.317 31.673 32.464 1.00 38.36 ? 766 HOH A O 1 HETATM 5869 O O . HOH U 4 . ? 43.579 58.280 38.410 1.00 56.78 ? 767 HOH A O 1 HETATM 5870 O O . HOH U 4 . ? 30.906 39.743 29.460 1.00 55.36 ? 768 HOH A O 1 HETATM 5871 O O . HOH U 4 . ? 43.861 47.818 32.077 1.00 37.92 ? 769 HOH A O 1 HETATM 5872 O O . HOH U 4 . ? 2.226 42.541 34.848 1.00 31.21 ? 770 HOH A O 1 HETATM 5873 O O . HOH U 4 . ? -0.584 29.930 45.582 1.00 29.05 ? 771 HOH A O 1 HETATM 5874 O O . HOH U 4 . ? 26.873 33.795 42.771 1.00 47.96 ? 772 HOH A O 1 HETATM 5875 O O . HOH U 4 . ? 27.265 27.310 41.323 1.00 49.77 ? 773 HOH A O 1 HETATM 5876 O O . HOH U 4 . ? 2.238 25.386 40.319 1.00 43.74 ? 774 HOH A O 1 HETATM 5877 O O . HOH U 4 . ? 14.707 61.190 33.939 1.00 46.18 ? 775 HOH A O 1 HETATM 5878 O O . HOH U 4 . ? 8.800 53.650 40.755 1.00 37.25 ? 776 HOH A O 1 HETATM 5879 O O . HOH U 4 . ? 27.332 28.419 49.769 1.00 38.45 ? 777 HOH A O 1 HETATM 5880 O O . HOH U 4 . ? -0.603 33.677 53.801 1.00 45.28 ? 778 HOH A O 1 HETATM 5881 O O . HOH U 4 . ? 3.374 39.710 29.653 1.00 43.70 ? 779 HOH A O 1 HETATM 5882 O O . HOH U 4 . ? 18.257 30.720 56.350 1.00 33.05 ? 780 HOH A O 1 HETATM 5883 O O . HOH U 4 . ? 31.976 42.090 33.655 1.00 58.20 ? 781 HOH A O 1 HETATM 5884 O O . HOH U 4 . ? 19.827 44.015 59.799 1.00 36.85 ? 782 HOH A O 1 HETATM 5885 O O . HOH U 4 . ? 7.282 51.070 40.855 1.00 47.85 ? 783 HOH A O 1 HETATM 5886 O O . HOH U 4 . ? 37.884 59.668 33.578 1.00 50.56 ? 784 HOH A O 1 HETATM 5887 O O . HOH U 4 . ? 23.829 25.748 24.201 1.00 53.36 ? 785 HOH A O 1 HETATM 5888 O O . HOH U 4 . ? 15.424 19.775 41.310 1.00 31.42 ? 786 HOH A O 1 HETATM 5889 O O . HOH U 4 . ? 11.828 25.714 58.795 1.00 35.58 ? 787 HOH A O 1 HETATM 5890 O O . HOH U 4 . ? 4.216 26.472 34.325 1.00 27.08 ? 788 HOH A O 1 HETATM 5891 O O . HOH U 4 . ? 46.952 33.503 44.056 1.00 22.99 ? 789 HOH A O 1 HETATM 5892 O O . HOH U 4 . ? 6.777 34.907 29.237 1.00 36.80 ? 790 HOH A O 1 HETATM 5893 O O . HOH U 4 . ? 1.653 40.369 36.692 1.00 38.94 ? 791 HOH A O 1 HETATM 5894 O O . HOH U 4 . ? 6.019 40.911 58.504 1.00 32.64 ? 792 HOH A O 1 HETATM 5895 O O . HOH U 4 . ? 34.193 56.524 47.952 1.00 28.58 ? 793 HOH A O 1 HETATM 5896 O O . HOH U 4 . ? 8.864 56.559 43.903 1.00 27.40 ? 794 HOH A O 1 HETATM 5897 O O . HOH U 4 . ? 24.997 58.134 52.635 1.00 31.53 ? 795 HOH A O 1 HETATM 5898 O O . HOH U 4 . ? 37.097 58.817 46.004 1.00 41.19 ? 796 HOH A O 1 HETATM 5899 O O . HOH V 4 . ? 43.340 90.503 92.448 1.00 2.00 ? 601 HOH B O 1 HETATM 5900 O O . HOH V 4 . ? 44.650 93.830 90.670 1.00 4.50 ? 602 HOH B O 1 HETATM 5901 O O . HOH V 4 . ? 36.051 91.862 96.646 1.00 2.00 ? 603 HOH B O 1 HETATM 5902 O O . HOH V 4 . ? 39.123 91.874 83.216 1.00 3.33 ? 604 HOH B O 1 HETATM 5903 O O . HOH V 4 . ? 50.864 95.859 92.409 1.00 2.00 ? 605 HOH B O 1 HETATM 5904 O O . HOH V 4 . ? 44.914 90.334 90.152 1.00 6.89 ? 606 HOH B O 1 HETATM 5905 O O . HOH V 4 . ? 36.031 74.551 80.201 1.00 11.88 ? 607 HOH B O 1 HETATM 5906 O O . HOH V 4 . ? 39.236 81.503 96.742 1.00 6.07 ? 608 HOH B O 1 HETATM 5907 O O . HOH V 4 . ? 36.675 88.868 78.280 1.00 6.03 ? 609 HOH B O 1 HETATM 5908 O O . HOH V 4 . ? 48.058 85.356 93.473 1.00 8.57 ? 610 HOH B O 1 HETATM 5909 O O . HOH V 4 . ? 38.329 84.160 97.313 1.00 7.19 ? 611 HOH B O 1 HETATM 5910 O O . HOH V 4 . ? 37.658 81.833 77.606 1.00 9.24 ? 612 HOH B O 1 HETATM 5911 O O . HOH V 4 . ? 55.642 81.838 87.728 1.00 8.32 ? 613 HOH B O 1 HETATM 5912 O O . HOH V 4 . ? 33.708 93.326 97.113 1.00 10.00 ? 614 HOH B O 1 HETATM 5913 O O . HOH V 4 . ? 32.701 96.090 97.776 1.00 13.46 ? 615 HOH B O 1 HETATM 5914 O O . HOH V 4 . ? 36.314 82.340 80.019 1.00 11.05 ? 616 HOH B O 1 HETATM 5915 O O . HOH V 4 . ? 50.631 99.250 86.050 1.00 7.81 ? 617 HOH B O 1 HETATM 5916 O O . HOH V 4 . ? 32.093 80.708 103.286 1.00 7.49 ? 618 HOH B O 1 HETATM 5917 O O . HOH V 4 . ? 49.929 96.677 85.304 1.00 9.58 ? 619 HOH B O 1 HETATM 5918 O O . HOH V 4 . ? 48.270 100.752 85.145 1.00 11.06 ? 620 HOH B O 1 HETATM 5919 O O . HOH V 4 . ? 23.770 87.789 74.057 1.00 10.40 ? 621 HOH B O 1 HETATM 5920 O O . HOH V 4 . ? 22.102 89.624 100.572 1.00 11.28 ? 622 HOH B O 1 HETATM 5921 O O . HOH V 4 . ? 45.797 96.477 100.716 1.00 11.10 ? 623 HOH B O 1 HETATM 5922 O O . HOH V 4 . ? 26.202 86.509 73.292 1.00 8.62 ? 624 HOH B O 1 HETATM 5923 O O . HOH V 4 . ? 46.968 86.955 85.373 1.00 9.55 ? 625 HOH B O 1 HETATM 5924 O O . HOH V 4 . ? 38.282 76.370 69.036 1.00 14.27 ? 626 HOH B O 1 HETATM 5925 O O . HOH V 4 . ? 45.346 99.422 94.170 1.00 7.94 ? 627 HOH B O 1 HETATM 5926 O O . HOH V 4 . ? 53.734 86.295 82.219 1.00 12.30 ? 628 HOH B O 1 HETATM 5927 O O . HOH V 4 . ? 56.257 79.205 97.798 1.00 18.64 ? 629 HOH B O 1 HETATM 5928 O O . HOH V 4 . ? 41.636 101.265 100.436 1.00 10.72 ? 630 HOH B O 1 HETATM 5929 O O . HOH V 4 . ? 38.136 80.637 94.317 1.00 17.97 ? 631 HOH B O 1 HETATM 5930 O O . HOH V 4 . ? 31.079 106.830 93.831 1.00 13.65 ? 632 HOH B O 1 HETATM 5931 O O . HOH V 4 . ? 37.691 73.729 84.012 1.00 12.92 ? 633 HOH B O 1 HETATM 5932 O O . HOH V 4 . ? 33.608 88.598 78.408 1.00 13.72 ? 634 HOH B O 1 HETATM 5933 O O . HOH V 4 . ? 44.712 88.173 65.982 1.00 10.72 ? 635 HOH B O 1 HETATM 5934 O O . HOH V 4 . ? 23.209 97.951 82.620 1.00 13.47 ? 636 HOH B O 1 HETATM 5935 O O . HOH V 4 . ? 50.287 84.397 91.833 1.00 11.66 ? 637 HOH B O 1 HETATM 5936 O O . HOH V 4 . ? 33.972 69.426 87.188 1.00 17.01 ? 638 HOH B O 1 HETATM 5937 O O . HOH V 4 . ? 55.096 87.487 84.385 1.00 17.11 ? 639 HOH B O 1 HETATM 5938 O O . HOH V 4 . ? 43.131 83.476 75.876 1.00 16.33 ? 640 HOH B O 1 HETATM 5939 O O . HOH V 4 . ? 38.333 85.148 102.987 1.00 11.23 ? 641 HOH B O 1 HETATM 5940 O O . HOH V 4 . ? 54.827 96.536 77.187 1.00 13.59 ? 642 HOH B O 1 HETATM 5941 O O . HOH V 4 . ? 38.705 107.074 93.240 1.00 24.24 ? 643 HOH B O 1 HETATM 5942 O O . HOH V 4 . ? 51.458 95.261 104.494 1.00 13.04 ? 644 HOH B O 1 HETATM 5943 O O . HOH V 4 . ? 38.775 101.325 99.668 1.00 12.03 ? 645 HOH B O 1 HETATM 5944 O O . HOH V 4 . ? 38.185 102.836 68.555 1.00 10.77 ? 646 HOH B O 1 HETATM 5945 O O . HOH V 4 . ? 33.732 68.666 76.649 1.00 13.73 ? 647 HOH B O 1 HETATM 5946 O O . HOH V 4 . ? 28.845 103.765 80.897 1.00 17.83 ? 648 HOH B O 1 HETATM 5947 O O . HOH V 4 . ? 16.542 93.399 91.747 1.00 14.30 ? 649 HOH B O 1 HETATM 5948 O O . HOH V 4 . ? 42.828 81.426 91.541 1.00 20.83 ? 650 HOH B O 1 HETATM 5949 O O . HOH V 4 . ? 37.429 86.544 100.750 1.00 14.40 ? 651 HOH B O 1 HETATM 5950 O O . HOH V 4 . ? 41.926 91.193 82.678 1.00 16.81 ? 652 HOH B O 1 HETATM 5951 O O . HOH V 4 . ? 28.236 70.300 82.709 1.00 14.47 ? 653 HOH B O 1 HETATM 5952 O O . HOH V 4 . ? 48.119 94.090 83.968 1.00 15.88 ? 654 HOH B O 1 HETATM 5953 O O . HOH V 4 . ? 26.696 103.150 79.077 1.00 16.50 ? 655 HOH B O 1 HETATM 5954 O O . HOH V 4 . ? 20.386 96.396 82.384 1.00 22.10 ? 656 HOH B O 1 HETATM 5955 O O . HOH V 4 . ? 27.366 103.532 91.110 1.00 24.88 ? 657 HOH B O 1 HETATM 5956 O O . HOH V 4 . ? 58.560 97.610 85.471 1.00 24.12 ? 658 HOH B O 1 HETATM 5957 O O . HOH V 4 . ? 31.143 84.655 98.177 1.00 13.93 ? 659 HOH B O 1 HETATM 5958 O O . HOH V 4 . ? 44.082 89.845 96.181 1.00 18.34 ? 660 HOH B O 1 HETATM 5959 O O . HOH V 4 . ? 45.662 103.001 91.731 1.00 23.18 ? 661 HOH B O 1 HETATM 5960 O O . HOH V 4 . ? 29.325 106.690 80.181 1.00 22.40 ? 662 HOH B O 1 HETATM 5961 O O . HOH V 4 . ? 40.126 75.052 85.868 1.00 29.63 ? 663 HOH B O 1 HETATM 5962 O O . HOH V 4 . ? 46.818 101.283 96.199 1.00 17.94 ? 664 HOH B O 1 HETATM 5963 O O . HOH V 4 . ? 40.847 88.317 100.256 1.00 20.71 ? 665 HOH B O 1 HETATM 5964 O O . HOH V 4 . ? 49.518 81.901 77.337 1.00 20.42 ? 666 HOH B O 1 HETATM 5965 O O . HOH V 4 . ? 21.872 83.406 95.168 1.00 19.55 ? 667 HOH B O 1 HETATM 5966 O O . HOH V 4 . ? 48.813 91.616 81.444 1.00 15.67 ? 668 HOH B O 1 HETATM 5967 O O . HOH V 4 . ? 15.312 91.586 82.139 1.00 20.65 ? 669 HOH B O 1 HETATM 5968 O O . HOH V 4 . ? 18.289 91.843 88.706 1.00 18.38 ? 670 HOH B O 1 HETATM 5969 O O . HOH V 4 . ? 32.259 77.773 67.808 1.00 18.31 ? 671 HOH B O 1 HETATM 5970 O O . HOH V 4 . ? 31.478 67.817 83.864 1.00 22.33 ? 672 HOH B O 1 HETATM 5971 O O . HOH V 4 . ? 16.558 83.937 92.518 1.00 27.49 ? 673 HOH B O 1 HETATM 5972 O O . HOH V 4 . ? 27.343 70.593 72.293 1.00 18.04 ? 674 HOH B O 1 HETATM 5973 O O . HOH V 4 . ? 40.134 89.089 80.810 1.00 28.47 ? 675 HOH B O 1 HETATM 5974 O O . HOH V 4 . ? 56.549 81.790 104.328 1.00 20.23 ? 676 HOH B O 1 HETATM 5975 O O . HOH V 4 . ? 37.325 71.887 70.415 1.00 20.40 ? 677 HOH B O 1 HETATM 5976 O O . HOH V 4 . ? 47.528 79.011 83.858 1.00 29.86 ? 678 HOH B O 1 HETATM 5977 O O . HOH V 4 . ? 46.227 86.209 67.290 1.00 20.16 ? 679 HOH B O 1 HETATM 5978 O O . HOH V 4 . ? 41.004 87.863 83.327 1.00 17.45 ? 680 HOH B O 1 HETATM 5979 O O . HOH V 4 . ? 20.695 98.242 88.526 1.00 30.21 ? 681 HOH B O 1 HETATM 5980 O O . HOH V 4 . ? 49.294 75.191 85.941 1.00 22.63 ? 682 HOH B O 1 HETATM 5981 O O . HOH V 4 . ? 57.225 97.112 91.585 1.00 23.33 ? 683 HOH B O 1 HETATM 5982 O O . HOH V 4 . ? 29.969 71.695 71.458 1.00 17.17 ? 684 HOH B O 1 HETATM 5983 O O . HOH V 4 . ? 33.557 85.736 98.843 1.00 20.06 ? 685 HOH B O 1 HETATM 5984 O O . HOH V 4 . ? 57.509 100.406 92.332 1.00 33.50 ? 686 HOH B O 1 HETATM 5985 O O . HOH V 4 . ? 35.408 107.933 74.433 1.00 22.29 ? 687 HOH B O 1 HETATM 5986 O O . HOH V 4 . ? 20.856 70.234 82.496 1.00 18.86 ? 688 HOH B O 1 HETATM 5987 O O . HOH V 4 . ? 32.581 88.390 106.059 1.00 21.56 ? 689 HOH B O 1 HETATM 5988 O O . HOH V 4 . ? 22.146 72.714 91.813 1.00 21.91 ? 690 HOH B O 1 HETATM 5989 O O . HOH V 4 . ? 18.729 76.928 83.468 1.00 19.05 ? 691 HOH B O 1 HETATM 5990 O O . HOH V 4 . ? 21.540 95.532 87.490 1.00 22.35 ? 692 HOH B O 1 HETATM 5991 O O . HOH V 4 . ? 34.506 67.176 83.627 1.00 17.88 ? 693 HOH B O 1 HETATM 5992 O O . HOH V 4 . ? 40.315 109.161 91.430 1.00 23.63 ? 694 HOH B O 1 HETATM 5993 O O . HOH V 4 . ? 51.238 105.910 78.841 1.00 20.42 ? 695 HOH B O 1 HETATM 5994 O O . HOH V 4 . ? 53.631 99.517 98.080 1.00 25.97 ? 696 HOH B O 1 HETATM 5995 O O . HOH V 4 . ? 20.778 91.389 102.467 1.00 34.71 ? 697 HOH B O 1 HETATM 5996 O O . HOH V 4 . ? 29.363 103.773 93.835 1.00 24.25 ? 698 HOH B O 1 HETATM 5997 O O . HOH V 4 . ? 45.650 102.381 69.181 1.00 18.16 ? 699 HOH B O 1 HETATM 5998 O O . HOH V 4 . ? 26.635 81.618 68.231 1.00 29.62 ? 700 HOH B O 1 HETATM 5999 O O . HOH V 4 . ? 27.982 81.411 109.012 1.00 32.36 ? 701 HOH B O 1 HETATM 6000 O O . HOH V 4 . ? 39.484 108.411 79.446 1.00 23.47 ? 702 HOH B O 1 HETATM 6001 O O . HOH V 4 . ? 42.661 88.051 98.014 1.00 19.53 ? 703 HOH B O 1 HETATM 6002 O O . HOH V 4 . ? 20.693 79.003 72.966 1.00 57.28 ? 704 HOH B O 1 HETATM 6003 O O . HOH V 4 . ? 22.509 102.969 93.463 1.00 31.58 ? 705 HOH B O 1 HETATM 6004 O O . HOH V 4 . ? 53.449 77.461 98.532 1.00 25.38 ? 706 HOH B O 1 HETATM 6005 O O . HOH V 4 . ? 46.771 74.511 97.487 1.00 25.38 ? 707 HOH B O 1 HETATM 6006 O O . HOH V 4 . ? 26.489 104.996 83.438 1.00 25.86 ? 708 HOH B O 1 HETATM 6007 O O . HOH V 4 . ? 57.766 102.695 85.114 1.00 26.34 ? 709 HOH B O 1 HETATM 6008 O O . HOH V 4 . ? 40.928 89.962 66.290 1.00 25.99 ? 710 HOH B O 1 HETATM 6009 O O . HOH V 4 . ? 51.429 77.404 83.663 1.00 35.74 ? 711 HOH B O 1 HETATM 6010 O O . HOH V 4 . ? 47.734 79.447 81.016 1.00 22.91 ? 712 HOH B O 1 HETATM 6011 O O . HOH V 4 . ? 45.506 81.299 85.511 1.00 28.66 ? 713 HOH B O 1 HETATM 6012 O O . HOH V 4 . ? 45.265 78.026 67.312 1.00 32.79 ? 714 HOH B O 1 HETATM 6013 O O . HOH V 4 . ? 44.889 90.475 112.480 1.00 26.72 ? 715 HOH B O 1 HETATM 6014 O O . HOH V 4 . ? 20.893 76.237 103.700 1.00 23.57 ? 716 HOH B O 1 HETATM 6015 O O . HOH V 4 . ? 47.529 106.386 72.788 1.00 29.10 ? 717 HOH B O 1 HETATM 6016 O O . HOH V 4 . ? 47.696 101.374 93.157 1.00 26.46 ? 718 HOH B O 1 HETATM 6017 O O . HOH V 4 . ? 21.255 99.636 95.698 1.00 35.56 ? 719 HOH B O 1 HETATM 6018 O O . HOH V 4 . ? 53.255 109.938 89.755 1.00 31.71 ? 720 HOH B O 1 HETATM 6019 O O . HOH V 4 . ? 17.975 75.237 85.883 1.00 28.08 ? 721 HOH B O 1 HETATM 6020 O O . HOH V 4 . ? 58.694 79.433 96.006 1.00 36.89 ? 722 HOH B O 1 HETATM 6021 O O . HOH V 4 . ? 30.949 99.954 100.560 1.00 34.23 ? 723 HOH B O 1 HETATM 6022 O O . HOH V 4 . ? 53.434 97.452 102.901 1.00 26.35 ? 724 HOH B O 1 HETATM 6023 O O . HOH V 4 . ? 33.890 93.602 67.406 1.00 52.25 ? 725 HOH B O 1 HETATM 6024 O O . HOH V 4 . ? 50.779 74.397 97.026 1.00 28.89 ? 726 HOH B O 1 HETATM 6025 O O . HOH V 4 . ? 34.825 89.962 107.277 1.00 36.20 ? 727 HOH B O 1 HETATM 6026 O O . HOH V 4 . ? 44.518 110.080 87.908 1.00 39.26 ? 728 HOH B O 1 HETATM 6027 O O . HOH V 4 . ? 52.820 102.089 94.894 1.00 37.07 ? 729 HOH B O 1 HETATM 6028 O O . HOH V 4 . ? 45.700 78.567 71.954 1.00 37.50 ? 730 HOH B O 1 HETATM 6029 O O . HOH V 4 . ? 33.157 80.330 64.945 1.00 23.98 ? 731 HOH B O 1 HETATM 6030 O O . HOH V 4 . ? 18.014 95.049 89.355 1.00 30.92 ? 732 HOH B O 1 HETATM 6031 O O . HOH V 4 . ? 48.337 76.244 83.236 1.00 47.07 ? 733 HOH B O 1 HETATM 6032 O O . HOH V 4 . ? 40.365 79.347 92.968 1.00 39.52 ? 734 HOH B O 1 HETATM 6033 O O . HOH V 4 . ? 17.129 96.571 98.470 1.00 36.15 ? 735 HOH B O 1 HETATM 6034 O O . HOH V 4 . ? 40.863 107.737 74.861 1.00 38.57 ? 736 HOH B O 1 HETATM 6035 O O . HOH V 4 . ? 43.556 108.958 85.396 1.00 31.55 ? 737 HOH B O 1 HETATM 6036 O O . HOH V 4 . ? 45.462 84.790 84.806 1.00 38.06 ? 738 HOH B O 1 HETATM 6037 O O . HOH V 4 . ? 25.328 73.218 101.555 1.00 27.70 ? 739 HOH B O 1 HETATM 6038 O O . HOH V 4 . ? 26.802 87.378 111.391 1.00 39.82 ? 740 HOH B O 1 HETATM 6039 O O . HOH V 4 . ? 41.003 93.091 107.552 1.00 30.17 ? 741 HOH B O 1 HETATM 6040 O O . HOH V 4 . ? 16.338 75.232 93.075 1.00 44.64 ? 742 HOH B O 1 HETATM 6041 O O . HOH V 4 . ? 58.349 86.422 98.768 1.00 23.63 ? 743 HOH B O 1 HETATM 6042 O O . HOH V 4 . ? 45.808 110.391 79.212 1.00 46.49 ? 744 HOH B O 1 HETATM 6043 O O . HOH V 4 . ? 22.690 70.725 78.114 1.00 20.59 ? 745 HOH B O 1 HETATM 6044 O O . HOH V 4 . ? 37.500 100.238 102.427 1.00 45.21 ? 746 HOH B O 1 HETATM 6045 O O . HOH V 4 . ? 57.953 82.130 101.501 1.00 36.62 ? 747 HOH B O 1 HETATM 6046 O O . HOH V 4 . ? 53.109 93.178 75.882 1.00 22.40 ? 748 HOH B O 1 HETATM 6047 O O . HOH V 4 . ? 22.977 70.651 99.762 1.00 34.48 ? 749 HOH B O 1 HETATM 6048 O O . HOH V 4 . ? 18.277 81.082 77.197 1.00 35.44 ? 750 HOH B O 1 HETATM 6049 O O . HOH V 4 . ? 18.774 84.536 106.915 1.00 35.70 ? 751 HOH B O 1 HETATM 6050 O O . HOH V 4 . ? 44.572 83.332 87.491 1.00 50.62 ? 752 HOH B O 1 HETATM 6051 O O . HOH V 4 . ? 49.573 102.247 104.191 1.00 41.54 ? 753 HOH B O 1 HETATM 6052 O O . HOH V 4 . ? 42.907 77.898 82.089 1.00 45.02 ? 754 HOH B O 1 HETATM 6053 O O . HOH V 4 . ? 37.300 85.644 106.992 1.00 28.46 ? 755 HOH B O 1 HETATM 6054 O O . HOH V 4 . ? 48.941 84.964 77.189 1.00 41.58 ? 756 HOH B O 1 HETATM 6055 O O . HOH V 4 . ? 29.050 73.776 68.963 1.00 40.43 ? 757 HOH B O 1 HETATM 6056 O O . HOH V 4 . ? 18.439 85.365 104.301 1.00 44.02 ? 758 HOH B O 1 HETATM 6057 O O . HOH V 4 . ? 29.378 105.582 91.363 1.00 37.35 ? 759 HOH B O 1 HETATM 6058 O O . HOH V 4 . ? 22.870 72.532 73.355 1.00 42.24 ? 760 HOH B O 1 HETATM 6059 O O . HOH V 4 . ? 51.901 81.793 113.378 1.00 46.71 ? 761 HOH B O 1 HETATM 6060 O O . HOH V 4 . ? 37.718 78.790 107.083 1.00 26.97 ? 762 HOH B O 1 HETATM 6061 O O . HOH V 4 . ? 42.157 110.511 89.368 1.00 31.32 ? 763 HOH B O 1 HETATM 6062 O O . HOH V 4 . ? 38.516 85.497 109.528 1.00 42.51 ? 764 HOH B O 1 HETATM 6063 O O . HOH V 4 . ? 23.798 73.705 105.203 1.00 52.44 ? 765 HOH B O 1 HETATM 6064 O O . HOH V 4 . ? 59.814 81.600 78.635 1.00 38.36 ? 766 HOH B O 1 HETATM 6065 O O . HOH V 4 . ? 56.293 108.121 83.934 1.00 56.78 ? 767 HOH B O 1 HETATM 6066 O O . HOH V 4 . ? 45.812 88.270 74.967 1.00 55.36 ? 768 HOH B O 1 HETATM 6067 O O . HOH V 4 . ? 57.821 97.614 77.858 1.00 37.92 ? 769 HOH B O 1 HETATM 6068 O O . HOH V 4 . ? 16.812 88.376 79.259 1.00 31.21 ? 770 HOH B O 1 HETATM 6069 O O . HOH V 4 . ? 14.825 75.764 90.174 1.00 29.05 ? 771 HOH B O 1 HETATM 6070 O O . HOH V 4 . ? 41.869 82.220 88.259 1.00 47.96 ? 772 HOH B O 1 HETATM 6071 O O . HOH V 4 . ? 42.938 75.777 86.976 1.00 49.77 ? 773 HOH B O 1 HETATM 6072 O O . HOH V 4 . ? 18.269 71.414 85.122 1.00 43.74 ? 774 HOH B O 1 HETATM 6073 O O . HOH V 4 . ? 27.465 108.127 78.366 1.00 46.18 ? 775 HOH B O 1 HETATM 6074 O O . HOH V 4 . ? 22.058 100.184 85.139 1.00 37.25 ? 776 HOH B O 1 HETATM 6075 O O . HOH V 4 . ? 42.578 77.052 95.391 1.00 38.45 ? 777 HOH B O 1 HETATM 6076 O O . HOH V 4 . ? 14.134 79.652 98.299 1.00 45.28 ? 778 HOH B O 1 HETATM 6077 O O . HOH V 4 . ? 18.423 85.569 74.175 1.00 43.70 ? 779 HOH B O 1 HETATM 6078 O O . HOH V 4 . ? 33.081 78.590 101.588 1.00 33.05 ? 780 HOH B O 1 HETATM 6079 O O . HOH V 4 . ? 46.491 90.792 79.142 1.00 58.20 ? 781 HOH B O 1 HETATM 6080 O O . HOH V 4 . ? 33.232 92.039 104.783 1.00 36.85 ? 782 HOH B O 1 HETATM 6081 O O . HOH V 4 . ? 20.793 97.472 85.244 1.00 47.85 ? 783 HOH B O 1 HETATM 6082 O O . HOH V 4 . ? 50.678 108.855 78.870 1.00 50.56 ? 784 HOH B O 1 HETATM 6083 O O . HOH V 4 . ? 40.319 73.554 69.783 1.00 53.36 ? 785 HOH B O 1 HETATM 6084 O O . HOH V 4 . ? 31.887 67.129 86.714 1.00 31.42 ? 786 HOH B O 1 HETATM 6085 O O . HOH V 4 . ? 27.076 73.032 103.917 1.00 35.58 ? 787 HOH B O 1 HETATM 6086 O O . HOH V 4 . ? 20.358 72.569 79.179 1.00 27.08 ? 788 HOH B O 1 HETATM 6087 O O . HOH V 4 . ? 61.820 83.904 90.268 1.00 22.99 ? 789 HOH B O 1 HETATM 6088 O O . HOH V 4 . ? 22.286 81.112 73.993 1.00 36.80 ? 790 HOH B O 1 HETATM 6089 O O . HOH V 4 . ? 16.382 86.195 81.131 1.00 38.94 ? 791 HOH B O 1 HETATM 6090 O O . HOH V 4 . ? 19.846 87.585 103.067 1.00 32.64 ? 792 HOH B O 1 HETATM 6091 O O . HOH V 4 . ? 46.766 105.649 93.172 1.00 28.58 ? 793 HOH B O 1 HETATM 6092 O O . HOH V 4 . ? 21.722 103.147 88.219 1.00 27.40 ? 794 HOH B O 1 HETATM 6093 O O . HOH V 4 . ? 37.287 106.451 97.484 1.00 31.53 ? 795 HOH B O 1 HETATM 6094 O O . HOH V 4 . ? 49.507 108.175 91.276 1.00 41.19 ? 796 HOH B 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 SER 1 83 ? ? ? A . n A 1 2 GLY 2 84 ? ? ? A . n A 1 3 THR 3 85 85 THR THR A . n A 1 4 ALA 4 86 86 ALA ALA A . n A 1 5 THR 5 87 87 THR THR A . n A 1 6 TYR 6 88 88 TYR TYR A . n A 1 7 SER 7 89 89 SER SER A . n A 1 8 GLY 8 90 90 GLY GLY A . n A 1 9 ASN 9 91 91 ASN ASN A . n A 1 10 PRO 10 92 92 PRO PRO A . n A 1 11 PHE 11 93 93 PHE PHE A . n A 1 12 VAL 12 94 94 VAL VAL A . n A 1 13 GLY 13 95 95 GLY GLY A . n A 1 14 VAL 14 96 96 VAL VAL A . n A 1 15 THR 15 97 97 THR THR A . n A 1 16 PRO 16 98 98 PRO PRO A . n A 1 17 TRP 17 99 99 TRP TRP A . n A 1 18 ALA 18 100 100 ALA ALA A . n A 1 19 ASN 19 101 101 ASN ASN A . n A 1 20 ALA 20 102 102 ALA ALA A . n A 1 21 TYR 21 103 103 TYR TYR A . n A 1 22 TYR 22 104 104 TYR TYR A . n A 1 23 ALA 23 105 105 ALA ALA A . n A 1 24 SER 24 106 106 SER SER A . n A 1 25 GLU 25 107 107 GLU GLU A . n A 1 26 VAL 26 108 108 VAL VAL A . n A 1 27 SER 27 109 109 SER SER A . n A 1 28 SER 28 110 110 SER SER A . n A 1 29 LEU 29 111 111 LEU LEU A . n A 1 30 ALA 30 112 112 ALA ALA A . n A 1 31 ILE 31 113 113 ILE ILE A . n A 1 32 PRO 32 114 114 PRO PRO A . n A 1 33 SER 33 115 115 SER SER A . n A 1 34 LEU 34 116 116 LEU LEU A . n A 1 35 THR 35 117 117 THR THR A . n A 1 36 GLY 36 118 118 GLY GLY A . n A 1 37 ALA 37 119 119 ALA ALA A . n A 1 38 MET 38 120 120 MET MET A . n A 1 39 ALA 39 121 121 ALA ALA A . n A 1 40 THR 40 122 122 THR THR A . n A 1 41 ALA 41 123 123 ALA ALA A . n A 1 42 ALA 42 124 124 ALA ALA A . n A 1 43 ALA 43 125 125 ALA ALA A . n A 1 44 ALA 44 126 126 ALA ALA A . n A 1 45 VAL 45 127 127 VAL VAL A . n A 1 46 ALA 46 128 128 ALA ALA A . n A 1 47 LYS 47 129 129 LYS LYS A . n A 1 48 VAL 48 130 130 VAL VAL A . n A 1 49 PRO 49 131 131 PRO PRO A . n A 1 50 SER 50 132 132 SER SER A . n A 1 51 PHE 51 133 133 PHE PHE A . n A 1 52 MET 52 134 134 MET MET A . n A 1 53 TRP 53 135 135 TRP TRP A . n A 1 54 LEU 54 136 136 LEU LEU A . n A 1 55 ASP 55 137 137 ASP ASP A . n A 1 56 THR 56 138 138 THR THR A . n A 1 57 LEU 57 139 139 LEU LEU A . n A 1 58 ASP 58 140 140 ASP ASP A . n A 1 59 LYS 59 141 141 LYS LYS A . n A 1 60 THR 60 142 142 THR THR A . n A 1 61 PRO 61 143 143 PRO PRO A . n A 1 62 LEU 62 144 144 LEU LEU A . n A 1 63 MET 63 145 145 MET MET A . n A 1 64 GLU 64 146 146 GLU GLU A . n A 1 65 GLN 65 147 147 GLN GLN A . n A 1 66 THR 66 148 148 THR THR A . n A 1 67 LEU 67 149 149 LEU LEU A . n A 1 68 ALA 68 150 150 ALA ALA A . n A 1 69 ASP 69 151 151 ASP ASP A . n A 1 70 ILE 70 152 152 ILE ILE A . n A 1 71 ARG 71 153 153 ARG ARG A . n A 1 72 THR 72 154 154 THR THR A . n A 1 73 ALA 73 155 155 ALA ALA A . n A 1 74 ASN 74 156 156 ASN ASN A . n A 1 75 LYS 75 157 157 LYS LYS A . n A 1 76 ASN 76 158 158 ASN ASN A . n A 1 77 GLY 77 159 159 GLY GLY A . n A 1 78 GLY 78 160 160 GLY GLY A . n A 1 79 ASN 79 161 161 ASN ASN A . n A 1 80 TYR 80 162 162 TYR TYR A . n A 1 81 ALA 81 163 163 ALA ALA A . n A 1 82 GLY 82 164 164 GLY GLY A . n A 1 83 GLN 83 165 165 GLN GLN A . n A 1 84 PHE 84 166 166 PHE PHE A . n A 1 85 VAL 85 167 167 VAL VAL A . n A 1 86 VAL 86 168 168 VAL VAL A . n A 1 87 PHE 87 169 169 PHE PHE A . n A 1 88 ASP 88 170 170 ASP ASP A . n A 1 89 LEU 89 171 171 LEU LEU A . n A 1 90 PRO 90 172 172 PRO PRO A . n A 1 91 ASP 91 173 173 ASP ASP A . n A 1 92 ARG 92 174 174 ARG ARG A . n A 1 93 ASP 93 175 175 ASP ASP A . n A 1 94 CYS 94 176 176 CYS CYS A . n A 1 95 ALA 95 177 177 ALA ALA A . n A 1 96 ALA 96 178 178 ALA ALA A . n A 1 97 LEU 97 179 179 LEU LEU A . n A 1 98 ALA 98 180 180 ALA ALA A . n A 1 99 SER 99 181 181 SER SER A . n A 1 100 ASN 100 182 182 ASN ASN A . n A 1 101 GLY 101 183 183 GLY GLY A . n A 1 102 GLU 102 184 184 GLU GLU A . n A 1 103 TYR 103 185 185 TYR TYR A . n A 1 104 SER 104 186 186 SER SER A . n A 1 105 ILE 105 187 187 ILE ILE A . n A 1 106 ALA 106 188 188 ALA ALA A . n A 1 107 ASP 107 189 189 ASP ASP A . n A 1 108 GLY 108 190 190 GLY GLY A . n A 1 109 GLY 109 191 191 GLY GLY A . n A 1 110 VAL 110 192 192 VAL VAL A . n A 1 111 ALA 111 193 193 ALA ALA A . n A 1 112 LYS 112 194 194 LYS LYS A . n A 1 113 TYR 113 195 195 TYR TYR A . n A 1 114 LYS 114 196 196 LYS LYS A . n A 1 115 ASN 115 197 197 ASN ASN A . n A 1 116 TYR 116 198 198 TYR TYR A . n A 1 117 ILE 117 199 199 ILE ILE A . n A 1 118 ASP 118 200 200 ASP ASP A . n A 1 119 THR 119 201 201 THR THR A . n A 1 120 ILE 120 202 202 ILE ILE A . n A 1 121 ARG 121 203 203 ARG ARG A . n A 1 122 GLN 122 204 204 GLN GLN A . n A 1 123 ILE 123 205 205 ILE ILE A . n A 1 124 VAL 124 206 206 VAL VAL A . n A 1 125 VAL 125 207 207 VAL VAL A . n A 1 126 GLU 126 208 208 GLU GLU A . n A 1 127 TYR 127 209 209 TYR TYR A . n A 1 128 SER 128 210 210 SER SER A . n A 1 129 ASP 129 211 211 ASP ASP A . n A 1 130 ILE 130 212 212 ILE ILE A . n A 1 131 ARG 131 213 213 ARG ARG A . n A 1 132 THR 132 214 214 THR THR A . n A 1 133 LEU 133 215 215 LEU LEU A . n A 1 134 LEU 134 216 216 LEU LEU A . n A 1 135 VAL 135 217 217 VAL VAL A . n A 1 136 ILE 136 218 218 ILE ILE A . n A 1 137 GLU 137 219 219 GLU GLU A . n A 1 138 PRO 138 220 220 PRO PRO A . n A 1 139 ASP 139 221 221 ASP ASP A . n A 1 140 SER 140 222 222 SER SER A . n A 1 141 LEU 141 223 223 LEU LEU A . n A 1 142 ALA 142 224 224 ALA ALA A . n A 1 143 ASN 143 225 225 ASN ASN A . n A 1 144 LEU 144 226 226 LEU LEU A . n A 1 145 VAL 145 227 227 VAL VAL A . n A 1 146 THR 146 228 228 THR THR A . n A 1 147 ASN 147 229 229 ASN ASN A . n A 1 148 LEU 148 230 230 LEU LEU A . n A 1 149 GLY 149 231 231 GLY GLY A . n A 1 150 THR 150 232 232 THR THR A . n A 1 151 PRO 151 233 233 PRO PRO A . n A 1 152 LYS 152 234 234 LYS LYS A . n A 1 153 CYS 153 235 235 CYS CYS A . n A 1 154 ALA 154 236 236 ALA ALA A . n A 1 155 ASN 155 237 237 ASN ASN A . n A 1 156 ALA 156 238 238 ALA ALA A . n A 1 157 GLN 157 239 239 GLN GLN A . n A 1 158 SER 158 240 240 SER SER A . n A 1 159 ALA 159 241 241 ALA ALA A . n A 1 160 TYR 160 242 242 TYR TYR A . n A 1 161 LEU 161 243 243 LEU LEU A . n A 1 162 GLU 162 244 244 GLU GLU A . n A 1 163 CYS 163 245 245 CYS CYS A . n A 1 164 ILE 164 246 246 ILE ILE A . n A 1 165 ASN 165 247 247 ASN ASN A . n A 1 166 TYR 166 248 248 TYR TYR A . n A 1 167 ALA 167 249 249 ALA ALA A . n A 1 168 VAL 168 250 250 VAL VAL A . n A 1 169 THR 169 251 251 THR THR A . n A 1 170 GLN 170 252 252 GLN GLN A . n A 1 171 LEU 171 253 253 LEU LEU A . n A 1 172 ASN 172 254 254 ASN ASN A . n A 1 173 LEU 173 255 255 LEU LEU A . n A 1 174 PRO 174 256 256 PRO PRO A . n A 1 175 ASN 175 257 257 ASN ASN A . n A 1 176 VAL 176 258 258 VAL VAL A . n A 1 177 ALA 177 259 259 ALA ALA A . n A 1 178 MET 178 260 260 MET MET A . n A 1 179 TYR 179 261 261 TYR TYR A . n A 1 180 LEU 180 262 262 LEU LEU A . n A 1 181 ASP 181 263 263 ASP ASP A . n A 1 182 ALA 182 264 264 ALA ALA A . n A 1 183 GLY 183 265 265 GLY GLY A . n A 1 184 HIS 184 266 266 HIS HIS A . n A 1 185 ALA 185 267 267 ALA ALA A . n A 1 186 GLY 186 268 268 GLY GLY A . n A 1 187 TRP 187 269 269 TRP TRP A . n A 1 188 LEU 188 270 270 LEU LEU A . n A 1 189 GLY 189 271 271 GLY GLY A . n A 1 190 TRP 190 272 272 TRP TRP A . n A 1 191 PRO 191 273 273 PRO PRO A . n A 1 192 ALA 192 274 274 ALA ALA A . n A 1 193 ASN 193 275 275 ASN ASN A . n A 1 194 GLN 194 276 276 GLN GLN A . n A 1 195 ASP 195 277 277 ASP ASP A . n A 1 196 PRO 196 278 278 PRO PRO A . n A 1 197 ALA 197 279 279 ALA ALA A . n A 1 198 ALA 198 280 280 ALA ALA A . n A 1 199 GLN 199 281 281 GLN GLN A . n A 1 200 LEU 200 282 282 LEU LEU A . n A 1 201 PHE 201 283 283 PHE PHE A . n A 1 202 ALA 202 284 284 ALA ALA A . n A 1 203 ASN 203 285 285 ASN ASN A . n A 1 204 VAL 204 286 286 VAL VAL A . n A 1 205 TYR 205 287 287 TYR TYR A . n A 1 206 LYS 206 288 288 LYS LYS A . n A 1 207 ASN 207 289 289 ASN ASN A . n A 1 208 ALA 208 290 290 ALA ALA A . n A 1 209 SER 209 291 291 SER SER A . n A 1 210 SER 210 292 292 SER SER A . n A 1 211 PRO 211 293 293 PRO PRO A . n A 1 212 ARG 212 294 294 ARG ARG A . n A 1 213 ALA 213 295 295 ALA ALA A . n A 1 214 LEU 214 296 296 LEU LEU A . n A 1 215 ARG 215 297 297 ARG ARG A . n A 1 216 GLY 216 298 298 GLY GLY A . n A 1 217 LEU 217 299 299 LEU LEU A . n A 1 218 ALA 218 300 300 ALA ALA A . n A 1 219 THR 219 301 301 THR THR A . n A 1 220 ASN 220 302 302 ASN ASN A . n A 1 221 VAL 221 303 303 VAL VAL A . n A 1 222 ALA 222 304 304 ALA ALA A . n A 1 223 ASN 223 305 305 ASN ASN A . n A 1 224 TYR 224 306 306 TYR TYR A . n A 1 225 ASN 225 307 307 ASN ASN A . n A 1 226 GLY 226 308 308 GLY GLY A . n A 1 227 TRP 227 309 309 TRP TRP A . n A 1 228 ASN 228 310 310 ASN ASN A . n A 1 229 ILE 229 311 311 ILE ILE A . n A 1 230 THR 230 312 312 THR THR A . n A 1 231 SER 231 313 313 SER SER A . n A 1 232 PRO 232 314 314 PRO PRO A . n A 1 233 PRO 233 315 315 PRO PRO A . n A 1 234 SER 234 316 316 SER SER A . n A 1 235 TYR 235 317 317 TYR TYR A . n A 1 236 THR 236 318 318 THR THR A . n A 1 237 GLN 237 319 319 GLN GLN A . n A 1 238 GLY 238 320 320 GLY GLY A . n A 1 239 ASN 239 321 321 ASN ASN A . n A 1 240 ALA 240 322 322 ALA ALA A . n A 1 241 VAL 241 323 323 VAL VAL A . n A 1 242 TYR 242 324 324 TYR TYR A . n A 1 243 ASN 243 325 325 ASN ASN A . n A 1 244 GLU 244 326 326 GLU GLU A . n A 1 245 LYS 245 327 327 LYS LYS A . n A 1 246 LEU 246 328 328 LEU LEU A . n A 1 247 TYR 247 329 329 TYR TYR A . n A 1 248 ILE 248 330 330 ILE ILE A . n A 1 249 HIS 249 331 331 HIS HIS A . n A 1 250 ALA 250 332 332 ALA ALA A . n A 1 251 ILE 251 333 333 ILE ILE A . n A 1 252 GLY 252 334 334 GLY GLY A . n A 1 253 PRO 253 335 335 PRO PRO A . n A 1 254 LEU 254 336 336 LEU LEU A . n A 1 255 LEU 255 337 337 LEU LEU A . n A 1 256 ALA 256 338 338 ALA ALA A . n A 1 257 ASN 257 339 339 ASN ASN A . n A 1 258 HIS 258 340 340 HIS HIS A . n A 1 259 GLY 259 341 341 GLY GLY A . n A 1 260 TRP 260 342 342 TRP TRP A . n A 1 261 SER 261 343 343 SER SER A . n A 1 262 ASN 262 344 344 ASN ASN A . n A 1 263 ALA 263 345 345 ALA ALA A . n A 1 264 PHE 264 346 346 PHE PHE A . n A 1 265 PHE 265 347 347 PHE PHE A . n A 1 266 ILE 266 348 348 ILE ILE A . n A 1 267 THR 267 349 349 THR THR A . n A 1 268 ASP 268 350 350 ASP ASP A . n A 1 269 GLN 269 351 351 GLN GLN A . n A 1 270 GLY 270 352 352 GLY GLY A . n A 1 271 ARG 271 353 353 ARG ARG A . n A 1 272 SER 272 354 354 SER SER A . n A 1 273 GLY 273 355 355 GLY GLY A . n A 1 274 LYS 274 356 356 LYS LYS A . n A 1 275 GLN 275 357 357 GLN GLN A . n A 1 276 PRO 276 358 358 PRO PRO A . n A 1 277 THR 277 359 359 THR THR A . n A 1 278 GLY 278 360 360 GLY GLY A . n A 1 279 GLN 279 361 361 GLN GLN A . n A 1 280 GLN 280 362 362 GLN GLN A . n A 1 281 GLN 281 363 363 GLN GLN A . n A 1 282 TRP 282 364 364 TRP TRP A . n A 1 283 GLY 283 365 365 GLY GLY A . n A 1 284 ASP 284 366 366 ASP ASP A . n A 1 285 TRP 285 367 367 TRP TRP A . n A 1 286 CYS 286 368 368 CYS CYS A . n A 1 287 ASN 287 369 369 ASN ASN A . n A 1 288 VAL 288 370 370 VAL VAL A . n A 1 289 ILE 289 371 371 ILE ILE A . n A 1 290 GLY 290 372 372 GLY GLY A . n A 1 291 THR 291 373 373 THR THR A . n A 1 292 GLY 292 374 374 GLY GLY A . n A 1 293 PHE 293 375 375 PHE PHE A . n A 1 294 GLY 294 376 376 GLY GLY A . n A 1 295 ILE 295 377 377 ILE ILE A . n A 1 296 ARG 296 378 378 ARG ARG A . n A 1 297 PRO 297 379 379 PRO PRO A . n A 1 298 SER 298 380 380 SER SER A . n A 1 299 ALA 299 381 381 ALA ALA A . n A 1 300 ASN 300 382 382 ASN ASN A . n A 1 301 THR 301 383 383 THR THR A . n A 1 302 GLY 302 384 384 GLY GLY A . n A 1 303 ASP 303 385 385 ASP ASP A . n A 1 304 SER 304 386 386 SER SER A . n A 1 305 LEU 305 387 387 LEU LEU A . n A 1 306 LEU 306 388 388 LEU LEU A . n A 1 307 ASP 307 389 389 ASP ASP A . n A 1 308 SER 308 390 390 SER SER A . n A 1 309 PHE 309 391 391 PHE PHE A . n A 1 310 VAL 310 392 392 VAL VAL A . n A 1 311 TRP 311 393 393 TRP TRP A . n A 1 312 VAL 312 394 394 VAL VAL A . n A 1 313 LYS 313 395 395 LYS LYS A . n A 1 314 PRO 314 396 396 PRO PRO A . n A 1 315 GLY 315 397 397 GLY GLY A . n A 1 316 GLY 316 398 398 GLY GLY A . n A 1 317 GLU 317 399 399 GLU GLU A . n A 1 318 CYS 318 400 400 CYS CYS A . n A 1 319 ASP 319 401 401 ASP ASP A . n A 1 320 GLY 320 402 402 GLY GLY A . n A 1 321 THR 321 403 403 THR THR A . n A 1 322 SER 322 404 404 SER SER A . n A 1 323 ASP 323 405 405 ASP ASP A . n A 1 324 SER 324 406 406 SER SER A . n A 1 325 SER 325 407 407 SER SER A . n A 1 326 ALA 326 408 408 ALA ALA A . n A 1 327 PRO 327 409 409 PRO PRO A . n A 1 328 ARG 328 410 410 ARG ARG A . n A 1 329 PHE 329 411 411 PHE PHE A . n A 1 330 ASP 330 412 412 ASP ASP A . n A 1 331 SER 331 413 413 SER SER A . n A 1 332 HIS 332 414 414 HIS HIS A . n A 1 333 CYS 333 415 415 CYS CYS A . n A 1 334 ALA 334 416 416 ALA ALA A . n A 1 335 LEU 335 417 417 LEU LEU A . n A 1 336 PRO 336 418 418 PRO PRO A . n A 1 337 ASP 337 419 419 ASP ASP A . n A 1 338 ALA 338 420 420 ALA ALA A . n A 1 339 LEU 339 421 421 LEU LEU A . n A 1 340 GLN 340 422 422 GLN GLN A . n A 1 341 PRO 341 423 423 PRO PRO A . n A 1 342 ALA 342 424 424 ALA ALA A . n A 1 343 PRO 343 425 425 PRO PRO A . n A 1 344 GLN 344 426 426 GLN GLN A . n A 1 345 ALA 345 427 427 ALA ALA A . n A 1 346 GLY 346 428 428 GLY GLY A . n A 1 347 ALA 347 429 429 ALA ALA A . n A 1 348 TRP 348 430 430 TRP TRP A . n A 1 349 PHE 349 431 431 PHE PHE A . n A 1 350 GLN 350 432 432 GLN GLN A . n A 1 351 ALA 351 433 433 ALA ALA A . n A 1 352 TYR 352 434 434 TYR TYR A . n A 1 353 PHE 353 435 435 PHE PHE A . n A 1 354 VAL 354 436 436 VAL VAL A . n A 1 355 GLN 355 437 437 GLN GLN A . n A 1 356 LEU 356 438 438 LEU LEU A . n A 1 357 LEU 357 439 439 LEU LEU A . n A 1 358 THR 358 440 440 THR THR A . n A 1 359 ASN 359 441 441 ASN ASN A . n A 1 360 ALA 360 442 442 ALA ALA A . n A 1 361 ASN 361 443 443 ASN ASN A . n A 1 362 PRO 362 444 444 PRO PRO A . n A 1 363 SER 363 445 445 SER SER A . n A 1 364 PHE 364 446 446 PHE PHE A . n A 1 365 LEU 365 447 447 LEU LEU A . n B 1 1 SER 1 83 ? ? ? B . n B 1 2 GLY 2 84 ? ? ? B . n B 1 3 THR 3 85 85 THR THR B . n B 1 4 ALA 4 86 86 ALA ALA B . n B 1 5 THR 5 87 87 THR THR B . n B 1 6 TYR 6 88 88 TYR TYR B . n B 1 7 SER 7 89 89 SER SER B . n B 1 8 GLY 8 90 90 GLY GLY B . n B 1 9 ASN 9 91 91 ASN ASN B . n B 1 10 PRO 10 92 92 PRO PRO B . n B 1 11 PHE 11 93 93 PHE PHE B . n B 1 12 VAL 12 94 94 VAL VAL B . n B 1 13 GLY 13 95 95 GLY GLY B . n B 1 14 VAL 14 96 96 VAL VAL B . n B 1 15 THR 15 97 97 THR THR B . n B 1 16 PRO 16 98 98 PRO PRO B . n B 1 17 TRP 17 99 99 TRP TRP B . n B 1 18 ALA 18 100 100 ALA ALA B . n B 1 19 ASN 19 101 101 ASN ASN B . n B 1 20 ALA 20 102 102 ALA ALA B . n B 1 21 TYR 21 103 103 TYR TYR B . n B 1 22 TYR 22 104 104 TYR TYR B . n B 1 23 ALA 23 105 105 ALA ALA B . n B 1 24 SER 24 106 106 SER SER B . n B 1 25 GLU 25 107 107 GLU GLU B . n B 1 26 VAL 26 108 108 VAL VAL B . n B 1 27 SER 27 109 109 SER SER B . n B 1 28 SER 28 110 110 SER SER B . n B 1 29 LEU 29 111 111 LEU LEU B . n B 1 30 ALA 30 112 112 ALA ALA B . n B 1 31 ILE 31 113 113 ILE ILE B . n B 1 32 PRO 32 114 114 PRO PRO B . n B 1 33 SER 33 115 115 SER SER B . n B 1 34 LEU 34 116 116 LEU LEU B . n B 1 35 THR 35 117 117 THR THR B . n B 1 36 GLY 36 118 118 GLY GLY B . n B 1 37 ALA 37 119 119 ALA ALA B . n B 1 38 MET 38 120 120 MET MET B . n B 1 39 ALA 39 121 121 ALA ALA B . n B 1 40 THR 40 122 122 THR THR B . n B 1 41 ALA 41 123 123 ALA ALA B . n B 1 42 ALA 42 124 124 ALA ALA B . n B 1 43 ALA 43 125 125 ALA ALA B . n B 1 44 ALA 44 126 126 ALA ALA B . n B 1 45 VAL 45 127 127 VAL VAL B . n B 1 46 ALA 46 128 128 ALA ALA B . n B 1 47 LYS 47 129 129 LYS LYS B . n B 1 48 VAL 48 130 130 VAL VAL B . n B 1 49 PRO 49 131 131 PRO PRO B . n B 1 50 SER 50 132 132 SER SER B . n B 1 51 PHE 51 133 133 PHE PHE B . n B 1 52 MET 52 134 134 MET MET B . n B 1 53 TRP 53 135 135 TRP TRP B . n B 1 54 LEU 54 136 136 LEU LEU B . n B 1 55 ASP 55 137 137 ASP ASP B . n B 1 56 THR 56 138 138 THR THR B . n B 1 57 LEU 57 139 139 LEU LEU B . n B 1 58 ASP 58 140 140 ASP ASP B . n B 1 59 LYS 59 141 141 LYS LYS B . n B 1 60 THR 60 142 142 THR THR B . n B 1 61 PRO 61 143 143 PRO PRO B . n B 1 62 LEU 62 144 144 LEU LEU B . n B 1 63 MET 63 145 145 MET MET B . n B 1 64 GLU 64 146 146 GLU GLU B . n B 1 65 GLN 65 147 147 GLN GLN B . n B 1 66 THR 66 148 148 THR THR B . n B 1 67 LEU 67 149 149 LEU LEU B . n B 1 68 ALA 68 150 150 ALA ALA B . n B 1 69 ASP 69 151 151 ASP ASP B . n B 1 70 ILE 70 152 152 ILE ILE B . n B 1 71 ARG 71 153 153 ARG ARG B . n B 1 72 THR 72 154 154 THR THR B . n B 1 73 ALA 73 155 155 ALA ALA B . n B 1 74 ASN 74 156 156 ASN ASN B . n B 1 75 LYS 75 157 157 LYS LYS B . n B 1 76 ASN 76 158 158 ASN ASN B . n B 1 77 GLY 77 159 159 GLY GLY B . n B 1 78 GLY 78 160 160 GLY GLY B . n B 1 79 ASN 79 161 161 ASN ASN B . n B 1 80 TYR 80 162 162 TYR TYR B . n B 1 81 ALA 81 163 163 ALA ALA B . n B 1 82 GLY 82 164 164 GLY GLY B . n B 1 83 GLN 83 165 165 GLN GLN B . n B 1 84 PHE 84 166 166 PHE PHE B . n B 1 85 VAL 85 167 167 VAL VAL B . n B 1 86 VAL 86 168 168 VAL VAL B . n B 1 87 PHE 87 169 169 PHE PHE B . n B 1 88 ASP 88 170 170 ASP ASP B . n B 1 89 LEU 89 171 171 LEU LEU B . n B 1 90 PRO 90 172 172 PRO PRO B . n B 1 91 ASP 91 173 173 ASP ASP B . n B 1 92 ARG 92 174 174 ARG ARG B . n B 1 93 ASP 93 175 175 ASP ASP B . n B 1 94 CYS 94 176 176 CYS CYS B . n B 1 95 ALA 95 177 177 ALA ALA B . n B 1 96 ALA 96 178 178 ALA ALA B . n B 1 97 LEU 97 179 179 LEU LEU B . n B 1 98 ALA 98 180 180 ALA ALA B . n B 1 99 SER 99 181 181 SER SER B . n B 1 100 ASN 100 182 182 ASN ASN B . n B 1 101 GLY 101 183 183 GLY GLY B . n B 1 102 GLU 102 184 184 GLU GLU B . n B 1 103 TYR 103 185 185 TYR TYR B . n B 1 104 SER 104 186 186 SER SER B . n B 1 105 ILE 105 187 187 ILE ILE B . n B 1 106 ALA 106 188 188 ALA ALA B . n B 1 107 ASP 107 189 189 ASP ASP B . n B 1 108 GLY 108 190 190 GLY GLY B . n B 1 109 GLY 109 191 191 GLY GLY B . n B 1 110 VAL 110 192 192 VAL VAL B . n B 1 111 ALA 111 193 193 ALA ALA B . n B 1 112 LYS 112 194 194 LYS LYS B . n B 1 113 TYR 113 195 195 TYR TYR B . n B 1 114 LYS 114 196 196 LYS LYS B . n B 1 115 ASN 115 197 197 ASN ASN B . n B 1 116 TYR 116 198 198 TYR TYR B . n B 1 117 ILE 117 199 199 ILE ILE B . n B 1 118 ASP 118 200 200 ASP ASP B . n B 1 119 THR 119 201 201 THR THR B . n B 1 120 ILE 120 202 202 ILE ILE B . n B 1 121 ARG 121 203 203 ARG ARG B . n B 1 122 GLN 122 204 204 GLN GLN B . n B 1 123 ILE 123 205 205 ILE ILE B . n B 1 124 VAL 124 206 206 VAL VAL B . n B 1 125 VAL 125 207 207 VAL VAL B . n B 1 126 GLU 126 208 208 GLU GLU B . n B 1 127 TYR 127 209 209 TYR TYR B . n B 1 128 SER 128 210 210 SER SER B . n B 1 129 ASP 129 211 211 ASP ASP B . n B 1 130 ILE 130 212 212 ILE ILE B . n B 1 131 ARG 131 213 213 ARG ARG B . n B 1 132 THR 132 214 214 THR THR B . n B 1 133 LEU 133 215 215 LEU LEU B . n B 1 134 LEU 134 216 216 LEU LEU B . n B 1 135 VAL 135 217 217 VAL VAL B . n B 1 136 ILE 136 218 218 ILE ILE B . n B 1 137 GLU 137 219 219 GLU GLU B . n B 1 138 PRO 138 220 220 PRO PRO B . n B 1 139 ASP 139 221 221 ASP ASP B . n B 1 140 SER 140 222 222 SER SER B . n B 1 141 LEU 141 223 223 LEU LEU B . n B 1 142 ALA 142 224 224 ALA ALA B . n B 1 143 ASN 143 225 225 ASN ASN B . n B 1 144 LEU 144 226 226 LEU LEU B . n B 1 145 VAL 145 227 227 VAL VAL B . n B 1 146 THR 146 228 228 THR THR B . n B 1 147 ASN 147 229 229 ASN ASN B . n B 1 148 LEU 148 230 230 LEU LEU B . n B 1 149 GLY 149 231 231 GLY GLY B . n B 1 150 THR 150 232 232 THR THR B . n B 1 151 PRO 151 233 233 PRO PRO B . n B 1 152 LYS 152 234 234 LYS LYS B . n B 1 153 CYS 153 235 235 CYS CYS B . n B 1 154 ALA 154 236 236 ALA ALA B . n B 1 155 ASN 155 237 237 ASN ASN B . n B 1 156 ALA 156 238 238 ALA ALA B . n B 1 157 GLN 157 239 239 GLN GLN B . n B 1 158 SER 158 240 240 SER SER B . n B 1 159 ALA 159 241 241 ALA ALA B . n B 1 160 TYR 160 242 242 TYR TYR B . n B 1 161 LEU 161 243 243 LEU LEU B . n B 1 162 GLU 162 244 244 GLU GLU B . n B 1 163 CYS 163 245 245 CYS CYS B . n B 1 164 ILE 164 246 246 ILE ILE B . n B 1 165 ASN 165 247 247 ASN ASN B . n B 1 166 TYR 166 248 248 TYR TYR B . n B 1 167 ALA 167 249 249 ALA ALA B . n B 1 168 VAL 168 250 250 VAL VAL B . n B 1 169 THR 169 251 251 THR THR B . n B 1 170 GLN 170 252 252 GLN GLN B . n B 1 171 LEU 171 253 253 LEU LEU B . n B 1 172 ASN 172 254 254 ASN ASN B . n B 1 173 LEU 173 255 255 LEU LEU B . n B 1 174 PRO 174 256 256 PRO PRO B . n B 1 175 ASN 175 257 257 ASN ASN B . n B 1 176 VAL 176 258 258 VAL VAL B . n B 1 177 ALA 177 259 259 ALA ALA B . n B 1 178 MET 178 260 260 MET MET B . n B 1 179 TYR 179 261 261 TYR TYR B . n B 1 180 LEU 180 262 262 LEU LEU B . n B 1 181 ASP 181 263 263 ASP ASP B . n B 1 182 ALA 182 264 264 ALA ALA B . n B 1 183 GLY 183 265 265 GLY GLY B . n B 1 184 HIS 184 266 266 HIS HIS B . n B 1 185 ALA 185 267 267 ALA ALA B . n B 1 186 GLY 186 268 268 GLY GLY B . n B 1 187 TRP 187 269 269 TRP TRP B . n B 1 188 LEU 188 270 270 LEU LEU B . n B 1 189 GLY 189 271 271 GLY GLY B . n B 1 190 TRP 190 272 272 TRP TRP B . n B 1 191 PRO 191 273 273 PRO PRO B . n B 1 192 ALA 192 274 274 ALA ALA B . n B 1 193 ASN 193 275 275 ASN ASN B . n B 1 194 GLN 194 276 276 GLN GLN B . n B 1 195 ASP 195 277 277 ASP ASP B . n B 1 196 PRO 196 278 278 PRO PRO B . n B 1 197 ALA 197 279 279 ALA ALA B . n B 1 198 ALA 198 280 280 ALA ALA B . n B 1 199 GLN 199 281 281 GLN GLN B . n B 1 200 LEU 200 282 282 LEU LEU B . n B 1 201 PHE 201 283 283 PHE PHE B . n B 1 202 ALA 202 284 284 ALA ALA B . n B 1 203 ASN 203 285 285 ASN ASN B . n B 1 204 VAL 204 286 286 VAL VAL B . n B 1 205 TYR 205 287 287 TYR TYR B . n B 1 206 LYS 206 288 288 LYS LYS B . n B 1 207 ASN 207 289 289 ASN ASN B . n B 1 208 ALA 208 290 290 ALA ALA B . n B 1 209 SER 209 291 291 SER SER B . n B 1 210 SER 210 292 292 SER SER B . n B 1 211 PRO 211 293 293 PRO PRO B . n B 1 212 ARG 212 294 294 ARG ARG B . n B 1 213 ALA 213 295 295 ALA ALA B . n B 1 214 LEU 214 296 296 LEU LEU B . n B 1 215 ARG 215 297 297 ARG ARG B . n B 1 216 GLY 216 298 298 GLY GLY B . n B 1 217 LEU 217 299 299 LEU LEU B . n B 1 218 ALA 218 300 300 ALA ALA B . n B 1 219 THR 219 301 301 THR THR B . n B 1 220 ASN 220 302 302 ASN ASN B . n B 1 221 VAL 221 303 303 VAL VAL B . n B 1 222 ALA 222 304 304 ALA ALA B . n B 1 223 ASN 223 305 305 ASN ASN B . n B 1 224 TYR 224 306 306 TYR TYR B . n B 1 225 ASN 225 307 307 ASN ASN B . n B 1 226 GLY 226 308 308 GLY GLY B . n B 1 227 TRP 227 309 309 TRP TRP B . n B 1 228 ASN 228 310 310 ASN ASN B . n B 1 229 ILE 229 311 311 ILE ILE B . n B 1 230 THR 230 312 312 THR THR B . n B 1 231 SER 231 313 313 SER SER B . n B 1 232 PRO 232 314 314 PRO PRO B . n B 1 233 PRO 233 315 315 PRO PRO B . n B 1 234 SER 234 316 316 SER SER B . n B 1 235 TYR 235 317 317 TYR TYR B . n B 1 236 THR 236 318 318 THR THR B . n B 1 237 GLN 237 319 319 GLN GLN B . n B 1 238 GLY 238 320 320 GLY GLY B . n B 1 239 ASN 239 321 321 ASN ASN B . n B 1 240 ALA 240 322 322 ALA ALA B . n B 1 241 VAL 241 323 323 VAL VAL B . n B 1 242 TYR 242 324 324 TYR TYR B . n B 1 243 ASN 243 325 325 ASN ASN B . n B 1 244 GLU 244 326 326 GLU GLU B . n B 1 245 LYS 245 327 327 LYS LYS B . n B 1 246 LEU 246 328 328 LEU LEU B . n B 1 247 TYR 247 329 329 TYR TYR B . n B 1 248 ILE 248 330 330 ILE ILE B . n B 1 249 HIS 249 331 331 HIS HIS B . n B 1 250 ALA 250 332 332 ALA ALA B . n B 1 251 ILE 251 333 333 ILE ILE B . n B 1 252 GLY 252 334 334 GLY GLY B . n B 1 253 PRO 253 335 335 PRO PRO B . n B 1 254 LEU 254 336 336 LEU LEU B . n B 1 255 LEU 255 337 337 LEU LEU B . n B 1 256 ALA 256 338 338 ALA ALA B . n B 1 257 ASN 257 339 339 ASN ASN B . n B 1 258 HIS 258 340 340 HIS HIS B . n B 1 259 GLY 259 341 341 GLY GLY B . n B 1 260 TRP 260 342 342 TRP TRP B . n B 1 261 SER 261 343 343 SER SER B . n B 1 262 ASN 262 344 344 ASN ASN B . n B 1 263 ALA 263 345 345 ALA ALA B . n B 1 264 PHE 264 346 346 PHE PHE B . n B 1 265 PHE 265 347 347 PHE PHE B . n B 1 266 ILE 266 348 348 ILE ILE B . n B 1 267 THR 267 349 349 THR THR B . n B 1 268 ASP 268 350 350 ASP ASP B . n B 1 269 GLN 269 351 351 GLN GLN B . n B 1 270 GLY 270 352 352 GLY GLY B . n B 1 271 ARG 271 353 353 ARG ARG B . n B 1 272 SER 272 354 354 SER SER B . n B 1 273 GLY 273 355 355 GLY GLY B . n B 1 274 LYS 274 356 356 LYS LYS B . n B 1 275 GLN 275 357 357 GLN GLN B . n B 1 276 PRO 276 358 358 PRO PRO B . n B 1 277 THR 277 359 359 THR THR B . n B 1 278 GLY 278 360 360 GLY GLY B . n B 1 279 GLN 279 361 361 GLN GLN B . n B 1 280 GLN 280 362 362 GLN GLN B . n B 1 281 GLN 281 363 363 GLN GLN B . n B 1 282 TRP 282 364 364 TRP TRP B . n B 1 283 GLY 283 365 365 GLY GLY B . n B 1 284 ASP 284 366 366 ASP ASP B . n B 1 285 TRP 285 367 367 TRP TRP B . n B 1 286 CYS 286 368 368 CYS CYS B . n B 1 287 ASN 287 369 369 ASN ASN B . n B 1 288 VAL 288 370 370 VAL VAL B . n B 1 289 ILE 289 371 371 ILE ILE B . n B 1 290 GLY 290 372 372 GLY GLY B . n B 1 291 THR 291 373 373 THR THR B . n B 1 292 GLY 292 374 374 GLY GLY B . n B 1 293 PHE 293 375 375 PHE PHE B . n B 1 294 GLY 294 376 376 GLY GLY B . n B 1 295 ILE 295 377 377 ILE ILE B . n B 1 296 ARG 296 378 378 ARG ARG B . n B 1 297 PRO 297 379 379 PRO PRO B . n B 1 298 SER 298 380 380 SER SER B . n B 1 299 ALA 299 381 381 ALA ALA B . n B 1 300 ASN 300 382 382 ASN ASN B . n B 1 301 THR 301 383 383 THR THR B . n B 1 302 GLY 302 384 384 GLY GLY B . n B 1 303 ASP 303 385 385 ASP ASP B . n B 1 304 SER 304 386 386 SER SER B . n B 1 305 LEU 305 387 387 LEU LEU B . n B 1 306 LEU 306 388 388 LEU LEU B . n B 1 307 ASP 307 389 389 ASP ASP B . n B 1 308 SER 308 390 390 SER SER B . n B 1 309 PHE 309 391 391 PHE PHE B . n B 1 310 VAL 310 392 392 VAL VAL B . n B 1 311 TRP 311 393 393 TRP TRP B . n B 1 312 VAL 312 394 394 VAL VAL B . n B 1 313 LYS 313 395 395 LYS LYS B . n B 1 314 PRO 314 396 396 PRO PRO B . n B 1 315 GLY 315 397 397 GLY GLY B . n B 1 316 GLY 316 398 398 GLY GLY B . n B 1 317 GLU 317 399 399 GLU GLU B . n B 1 318 CYS 318 400 400 CYS CYS B . n B 1 319 ASP 319 401 401 ASP ASP B . n B 1 320 GLY 320 402 402 GLY GLY B . n B 1 321 THR 321 403 403 THR THR B . n B 1 322 SER 322 404 404 SER SER B . n B 1 323 ASP 323 405 405 ASP ASP B . n B 1 324 SER 324 406 406 SER SER B . n B 1 325 SER 325 407 407 SER SER B . n B 1 326 ALA 326 408 408 ALA ALA B . n B 1 327 PRO 327 409 409 PRO PRO B . n B 1 328 ARG 328 410 410 ARG ARG B . n B 1 329 PHE 329 411 411 PHE PHE B . n B 1 330 ASP 330 412 412 ASP ASP B . n B 1 331 SER 331 413 413 SER SER B . n B 1 332 HIS 332 414 414 HIS HIS B . n B 1 333 CYS 333 415 415 CYS CYS B . n B 1 334 ALA 334 416 416 ALA ALA B . n B 1 335 LEU 335 417 417 LEU LEU B . n B 1 336 PRO 336 418 418 PRO PRO B . n B 1 337 ASP 337 419 419 ASP ASP B . n B 1 338 ALA 338 420 420 ALA ALA B . n B 1 339 LEU 339 421 421 LEU LEU B . n B 1 340 GLN 340 422 422 GLN GLN B . n B 1 341 PRO 341 423 423 PRO PRO B . n B 1 342 ALA 342 424 424 ALA ALA B . n B 1 343 PRO 343 425 425 PRO PRO B . n B 1 344 GLN 344 426 426 GLN GLN B . n B 1 345 ALA 345 427 427 ALA ALA B . n B 1 346 GLY 346 428 428 GLY GLY B . n B 1 347 ALA 347 429 429 ALA ALA B . n B 1 348 TRP 348 430 430 TRP TRP B . n B 1 349 PHE 349 431 431 PHE PHE B . n B 1 350 GLN 350 432 432 GLN GLN B . n B 1 351 ALA 351 433 433 ALA ALA B . n B 1 352 TYR 352 434 434 TYR TYR B . n B 1 353 PHE 353 435 435 PHE PHE B . n B 1 354 VAL 354 436 436 VAL VAL B . n B 1 355 GLN 355 437 437 GLN GLN B . n B 1 356 LEU 356 438 438 LEU LEU B . n B 1 357 LEU 357 439 439 LEU LEU B . n B 1 358 THR 358 440 440 THR THR B . n B 1 359 ASN 359 441 441 ASN ASN B . n B 1 360 ALA 360 442 442 ALA ALA B . n B 1 361 ASN 361 443 443 ASN ASN B . n B 1 362 PRO 362 444 444 PRO PRO B . n B 1 363 SER 363 445 445 SER SER B . n B 1 364 PHE 364 446 446 PHE PHE B . n B 1 365 LEU 365 447 447 LEU LEU B . 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 C 2 NAG 1 501 501 NAG NAG A . D 2 NAG 1 502 502 NAG NAG A . E 3 MAN 1 503 503 MAN MAN A . F 3 MAN 1 504 504 MAN MAN A . G 3 MAN 1 505 505 MAN MAN A . H 3 MAN 1 506 506 MAN MAN A . I 3 MAN 1 507 507 MAN MAN A . J 3 MAN 1 508 508 MAN MAN A . K 3 MAN 1 509 509 MAN MAN A . L 2 NAG 1 501 501 NAG NAG B . M 2 NAG 1 502 502 NAG NAG B . N 3 MAN 1 503 503 MAN MAN B . O 3 MAN 1 504 504 MAN MAN B . P 3 MAN 1 505 505 MAN MAN B . Q 3 MAN 1 506 506 MAN MAN B . R 3 MAN 1 507 507 MAN MAN B . S 3 MAN 1 508 508 MAN MAN B . T 3 MAN 1 509 509 MAN MAN B . U 4 HOH 1 601 601 HOH HOH A . U 4 HOH 2 602 602 HOH HOH A . U 4 HOH 3 603 603 HOH HOH A . U 4 HOH 4 604 604 HOH HOH A . U 4 HOH 5 605 605 HOH HOH A . U 4 HOH 6 606 606 HOH HOH A . U 4 HOH 7 607 607 HOH HOH A . U 4 HOH 8 608 608 HOH HOH A . U 4 HOH 9 609 609 HOH HOH A . U 4 HOH 10 610 610 HOH HOH A . U 4 HOH 11 611 611 HOH HOH A . U 4 HOH 12 612 612 HOH HOH A . U 4 HOH 13 613 613 HOH HOH A . U 4 HOH 14 614 614 HOH HOH A . U 4 HOH 15 615 615 HOH HOH A . U 4 HOH 16 616 616 HOH HOH A . U 4 HOH 17 617 617 HOH HOH A . U 4 HOH 18 618 618 HOH HOH A . U 4 HOH 19 619 619 HOH HOH A . U 4 HOH 20 620 620 HOH HOH A . U 4 HOH 21 621 621 HOH HOH A . U 4 HOH 22 622 622 HOH HOH A . U 4 HOH 23 623 623 HOH HOH A . U 4 HOH 24 624 624 HOH HOH A . U 4 HOH 25 625 625 HOH HOH A . U 4 HOH 26 626 626 HOH HOH A . U 4 HOH 27 627 627 HOH HOH A . U 4 HOH 28 628 628 HOH HOH A . U 4 HOH 29 629 629 HOH HOH A . U 4 HOH 30 630 630 HOH HOH A . U 4 HOH 31 631 631 HOH HOH A . U 4 HOH 32 632 632 HOH HOH A . U 4 HOH 33 633 633 HOH HOH A . U 4 HOH 34 634 634 HOH HOH A . U 4 HOH 35 635 635 HOH HOH A . U 4 HOH 36 636 636 HOH HOH A . U 4 HOH 37 637 637 HOH HOH A . U 4 HOH 38 638 638 HOH HOH A . U 4 HOH 39 639 639 HOH HOH A . U 4 HOH 40 640 640 HOH HOH A . U 4 HOH 41 641 641 HOH HOH A . U 4 HOH 42 642 642 HOH HOH A . U 4 HOH 43 643 643 HOH HOH A . U 4 HOH 44 644 644 HOH HOH A . U 4 HOH 45 645 645 HOH HOH A . U 4 HOH 46 646 646 HOH HOH A . U 4 HOH 47 647 647 HOH HOH A . U 4 HOH 48 648 648 HOH HOH A . U 4 HOH 49 649 649 HOH HOH A . U 4 HOH 50 650 650 HOH HOH A . U 4 HOH 51 651 651 HOH HOH A . U 4 HOH 52 652 652 HOH HOH A . U 4 HOH 53 653 653 HOH HOH A . U 4 HOH 54 654 654 HOH HOH A . U 4 HOH 55 655 655 HOH HOH A . U 4 HOH 56 656 656 HOH HOH A . U 4 HOH 57 657 657 HOH HOH A . U 4 HOH 58 658 658 HOH HOH A . U 4 HOH 59 659 659 HOH HOH A . U 4 HOH 60 660 660 HOH HOH A . U 4 HOH 61 661 661 HOH HOH A . U 4 HOH 62 662 662 HOH HOH A . U 4 HOH 63 663 663 HOH HOH A . U 4 HOH 64 664 664 HOH HOH A . U 4 HOH 65 665 665 HOH HOH A . U 4 HOH 66 666 666 HOH HOH A . U 4 HOH 67 667 667 HOH HOH A . U 4 HOH 68 668 668 HOH HOH A . U 4 HOH 69 669 669 HOH HOH A . U 4 HOH 70 670 670 HOH HOH A . U 4 HOH 71 671 671 HOH HOH A . U 4 HOH 72 672 672 HOH HOH A . U 4 HOH 73 673 673 HOH HOH A . U 4 HOH 74 674 674 HOH HOH A . U 4 HOH 75 675 675 HOH HOH A . U 4 HOH 76 676 676 HOH HOH A . U 4 HOH 77 677 677 HOH HOH A . U 4 HOH 78 678 678 HOH HOH A . U 4 HOH 79 679 679 HOH HOH A . U 4 HOH 80 680 680 HOH HOH A . U 4 HOH 81 681 681 HOH HOH A . U 4 HOH 82 682 682 HOH HOH A . U 4 HOH 83 683 683 HOH HOH A . U 4 HOH 84 684 684 HOH HOH A . U 4 HOH 85 685 685 HOH HOH A . U 4 HOH 86 686 686 HOH HOH A . U 4 HOH 87 687 687 HOH HOH A . U 4 HOH 88 688 688 HOH HOH A . U 4 HOH 89 689 689 HOH HOH A . U 4 HOH 90 690 690 HOH HOH A . U 4 HOH 91 691 691 HOH HOH A . U 4 HOH 92 692 692 HOH HOH A . U 4 HOH 93 693 693 HOH HOH A . U 4 HOH 94 694 694 HOH HOH A . U 4 HOH 95 695 695 HOH HOH A . U 4 HOH 96 696 696 HOH HOH A . U 4 HOH 97 697 697 HOH HOH A . U 4 HOH 98 698 698 HOH HOH A . U 4 HOH 99 699 699 HOH HOH A . U 4 HOH 100 700 700 HOH HOH A . U 4 HOH 101 701 701 HOH HOH A . U 4 HOH 102 702 702 HOH HOH A . U 4 HOH 103 703 703 HOH HOH A . U 4 HOH 104 704 704 HOH HOH A . U 4 HOH 105 705 705 HOH HOH A . U 4 HOH 106 706 706 HOH HOH A . U 4 HOH 107 707 707 HOH HOH A . U 4 HOH 108 708 708 HOH HOH A . U 4 HOH 109 709 709 HOH HOH A . U 4 HOH 110 710 710 HOH HOH A . U 4 HOH 111 711 711 HOH HOH A . U 4 HOH 112 712 712 HOH HOH A . U 4 HOH 113 713 713 HOH HOH A . U 4 HOH 114 714 714 HOH HOH A . U 4 HOH 115 715 715 HOH HOH A . U 4 HOH 116 716 716 HOH HOH A . U 4 HOH 117 717 717 HOH HOH A . U 4 HOH 118 718 718 HOH HOH A . U 4 HOH 119 719 719 HOH HOH A . U 4 HOH 120 720 720 HOH HOH A . U 4 HOH 121 721 721 HOH HOH A . U 4 HOH 122 722 722 HOH HOH A . U 4 HOH 123 723 723 HOH HOH A . U 4 HOH 124 724 724 HOH HOH A . U 4 HOH 125 725 725 HOH HOH A . U 4 HOH 126 726 726 HOH HOH A . U 4 HOH 127 727 727 HOH HOH A . U 4 HOH 128 728 728 HOH HOH A . U 4 HOH 129 729 729 HOH HOH A . U 4 HOH 130 730 730 HOH HOH A . U 4 HOH 131 731 731 HOH HOH A . U 4 HOH 132 732 732 HOH HOH A . U 4 HOH 133 733 733 HOH HOH A . U 4 HOH 134 734 734 HOH HOH A . U 4 HOH 135 735 735 HOH HOH A . U 4 HOH 136 736 736 HOH HOH A . U 4 HOH 137 737 737 HOH HOH A . U 4 HOH 138 738 738 HOH HOH A . U 4 HOH 139 739 739 HOH HOH A . U 4 HOH 140 740 740 HOH HOH A . U 4 HOH 141 741 741 HOH HOH A . U 4 HOH 142 742 742 HOH HOH A . U 4 HOH 143 743 743 HOH HOH A . U 4 HOH 144 744 744 HOH HOH A . U 4 HOH 145 745 745 HOH HOH A . U 4 HOH 146 746 746 HOH HOH A . U 4 HOH 147 747 747 HOH HOH A . U 4 HOH 148 748 748 HOH HOH A . U 4 HOH 149 749 749 HOH HOH A . U 4 HOH 150 750 750 HOH HOH A . U 4 HOH 151 751 751 HOH HOH A . U 4 HOH 152 752 752 HOH HOH A . U 4 HOH 153 753 753 HOH HOH A . U 4 HOH 154 754 754 HOH HOH A . U 4 HOH 155 755 755 HOH HOH A . U 4 HOH 156 756 756 HOH HOH A . U 4 HOH 157 757 757 HOH HOH A . U 4 HOH 158 758 758 HOH HOH A . U 4 HOH 159 759 759 HOH HOH A . U 4 HOH 160 760 760 HOH HOH A . U 4 HOH 161 761 761 HOH HOH A . U 4 HOH 162 762 762 HOH HOH A . U 4 HOH 163 763 763 HOH HOH A . U 4 HOH 164 764 764 HOH HOH A . U 4 HOH 165 765 765 HOH HOH A . U 4 HOH 166 766 766 HOH HOH A . U 4 HOH 167 767 767 HOH HOH A . U 4 HOH 168 768 768 HOH HOH A . U 4 HOH 169 769 769 HOH HOH A . U 4 HOH 170 770 770 HOH HOH A . U 4 HOH 171 771 771 HOH HOH A . U 4 HOH 172 772 772 HOH HOH A . U 4 HOH 173 773 773 HOH HOH A . U 4 HOH 174 774 774 HOH HOH A . U 4 HOH 175 775 775 HOH HOH A . U 4 HOH 176 776 776 HOH HOH A . U 4 HOH 177 777 777 HOH HOH A . U 4 HOH 178 778 778 HOH HOH A . U 4 HOH 179 779 779 HOH HOH A . U 4 HOH 180 780 780 HOH HOH A . U 4 HOH 181 781 781 HOH HOH A . U 4 HOH 182 782 782 HOH HOH A . U 4 HOH 183 783 783 HOH HOH A . U 4 HOH 184 784 784 HOH HOH A . U 4 HOH 185 785 785 HOH HOH A . U 4 HOH 186 786 786 HOH HOH A . U 4 HOH 187 787 787 HOH HOH A . U 4 HOH 188 788 788 HOH HOH A . U 4 HOH 189 789 789 HOH HOH A . U 4 HOH 190 790 790 HOH HOH A . U 4 HOH 191 791 791 HOH HOH A . U 4 HOH 192 792 792 HOH HOH A . U 4 HOH 193 793 793 HOH HOH A . U 4 HOH 194 794 794 HOH HOH A . U 4 HOH 195 795 795 HOH HOH A . U 4 HOH 196 796 796 HOH HOH A . V 4 HOH 1 601 601 HOH HOH B . V 4 HOH 2 602 602 HOH HOH B . V 4 HOH 3 603 603 HOH HOH B . V 4 HOH 4 604 604 HOH HOH B . V 4 HOH 5 605 605 HOH HOH B . V 4 HOH 6 606 606 HOH HOH B . V 4 HOH 7 607 607 HOH HOH B . V 4 HOH 8 608 608 HOH HOH B . V 4 HOH 9 609 609 HOH HOH B . V 4 HOH 10 610 610 HOH HOH B . V 4 HOH 11 611 611 HOH HOH B . V 4 HOH 12 612 612 HOH HOH B . V 4 HOH 13 613 613 HOH HOH B . V 4 HOH 14 614 614 HOH HOH B . V 4 HOH 15 615 615 HOH HOH B . V 4 HOH 16 616 616 HOH HOH B . V 4 HOH 17 617 617 HOH HOH B . V 4 HOH 18 618 618 HOH HOH B . V 4 HOH 19 619 619 HOH HOH B . V 4 HOH 20 620 620 HOH HOH B . V 4 HOH 21 621 621 HOH HOH B . V 4 HOH 22 622 622 HOH HOH B . V 4 HOH 23 623 623 HOH HOH B . V 4 HOH 24 624 624 HOH HOH B . V 4 HOH 25 625 625 HOH HOH B . V 4 HOH 26 626 626 HOH HOH B . V 4 HOH 27 627 627 HOH HOH B . V 4 HOH 28 628 628 HOH HOH B . V 4 HOH 29 629 629 HOH HOH B . V 4 HOH 30 630 630 HOH HOH B . V 4 HOH 31 631 631 HOH HOH B . V 4 HOH 32 632 632 HOH HOH B . V 4 HOH 33 633 633 HOH HOH B . V 4 HOH 34 634 634 HOH HOH B . V 4 HOH 35 635 635 HOH HOH B . V 4 HOH 36 636 636 HOH HOH B . V 4 HOH 37 637 637 HOH HOH B . V 4 HOH 38 638 638 HOH HOH B . V 4 HOH 39 639 639 HOH HOH B . V 4 HOH 40 640 640 HOH HOH B . V 4 HOH 41 641 641 HOH HOH B . V 4 HOH 42 642 642 HOH HOH B . V 4 HOH 43 643 643 HOH HOH B . V 4 HOH 44 644 644 HOH HOH B . V 4 HOH 45 645 645 HOH HOH B . V 4 HOH 46 646 646 HOH HOH B . V 4 HOH 47 647 647 HOH HOH B . V 4 HOH 48 648 648 HOH HOH B . V 4 HOH 49 649 649 HOH HOH B . V 4 HOH 50 650 650 HOH HOH B . V 4 HOH 51 651 651 HOH HOH B . V 4 HOH 52 652 652 HOH HOH B . V 4 HOH 53 653 653 HOH HOH B . V 4 HOH 54 654 654 HOH HOH B . V 4 HOH 55 655 655 HOH HOH B . V 4 HOH 56 656 656 HOH HOH B . V 4 HOH 57 657 657 HOH HOH B . V 4 HOH 58 658 658 HOH HOH B . V 4 HOH 59 659 659 HOH HOH B . V 4 HOH 60 660 660 HOH HOH B . V 4 HOH 61 661 661 HOH HOH B . V 4 HOH 62 662 662 HOH HOH B . V 4 HOH 63 663 663 HOH HOH B . V 4 HOH 64 664 664 HOH HOH B . V 4 HOH 65 665 665 HOH HOH B . V 4 HOH 66 666 666 HOH HOH B . V 4 HOH 67 667 667 HOH HOH B . V 4 HOH 68 668 668 HOH HOH B . V 4 HOH 69 669 669 HOH HOH B . V 4 HOH 70 670 670 HOH HOH B . V 4 HOH 71 671 671 HOH HOH B . V 4 HOH 72 672 672 HOH HOH B . V 4 HOH 73 673 673 HOH HOH B . V 4 HOH 74 674 674 HOH HOH B . V 4 HOH 75 675 675 HOH HOH B . V 4 HOH 76 676 676 HOH HOH B . V 4 HOH 77 677 677 HOH HOH B . V 4 HOH 78 678 678 HOH HOH B . V 4 HOH 79 679 679 HOH HOH B . V 4 HOH 80 680 680 HOH HOH B . V 4 HOH 81 681 681 HOH HOH B . V 4 HOH 82 682 682 HOH HOH B . V 4 HOH 83 683 683 HOH HOH B . V 4 HOH 84 684 684 HOH HOH B . V 4 HOH 85 685 685 HOH HOH B . V 4 HOH 86 686 686 HOH HOH B . V 4 HOH 87 687 687 HOH HOH B . V 4 HOH 88 688 688 HOH HOH B . V 4 HOH 89 689 689 HOH HOH B . V 4 HOH 90 690 690 HOH HOH B . V 4 HOH 91 691 691 HOH HOH B . V 4 HOH 92 692 692 HOH HOH B . V 4 HOH 93 693 693 HOH HOH B . V 4 HOH 94 694 694 HOH HOH B . V 4 HOH 95 695 695 HOH HOH B . V 4 HOH 96 696 696 HOH HOH B . V 4 HOH 97 697 697 HOH HOH B . V 4 HOH 98 698 698 HOH HOH B . V 4 HOH 99 699 699 HOH HOH B . V 4 HOH 100 700 700 HOH HOH B . V 4 HOH 101 701 701 HOH HOH B . V 4 HOH 102 702 702 HOH HOH B . V 4 HOH 103 703 703 HOH HOH B . V 4 HOH 104 704 704 HOH HOH B . V 4 HOH 105 705 705 HOH HOH B . V 4 HOH 106 706 706 HOH HOH B . V 4 HOH 107 707 707 HOH HOH B . V 4 HOH 108 708 708 HOH HOH B . V 4 HOH 109 709 709 HOH HOH B . V 4 HOH 110 710 710 HOH HOH B . V 4 HOH 111 711 711 HOH HOH B . V 4 HOH 112 712 712 HOH HOH B . V 4 HOH 113 713 713 HOH HOH B . V 4 HOH 114 714 714 HOH HOH B . V 4 HOH 115 715 715 HOH HOH B . V 4 HOH 116 716 716 HOH HOH B . V 4 HOH 117 717 717 HOH HOH B . V 4 HOH 118 718 718 HOH HOH B . V 4 HOH 119 719 719 HOH HOH B . V 4 HOH 120 720 720 HOH HOH B . V 4 HOH 121 721 721 HOH HOH B . V 4 HOH 122 722 722 HOH HOH B . V 4 HOH 123 723 723 HOH HOH B . V 4 HOH 124 724 724 HOH HOH B . V 4 HOH 125 725 725 HOH HOH B . V 4 HOH 126 726 726 HOH HOH B . V 4 HOH 127 727 727 HOH HOH B . V 4 HOH 128 728 728 HOH HOH B . V 4 HOH 129 729 729 HOH HOH B . V 4 HOH 130 730 730 HOH HOH B . V 4 HOH 131 731 731 HOH HOH B . V 4 HOH 132 732 732 HOH HOH B . V 4 HOH 133 733 733 HOH HOH B . V 4 HOH 134 734 734 HOH HOH B . V 4 HOH 135 735 735 HOH HOH B . V 4 HOH 136 736 736 HOH HOH B . V 4 HOH 137 737 737 HOH HOH B . V 4 HOH 138 738 738 HOH HOH B . V 4 HOH 139 739 739 HOH HOH B . V 4 HOH 140 740 740 HOH HOH B . V 4 HOH 141 741 741 HOH HOH B . V 4 HOH 142 742 742 HOH HOH B . V 4 HOH 143 743 743 HOH HOH B . V 4 HOH 144 744 744 HOH HOH B . V 4 HOH 145 745 745 HOH HOH B . V 4 HOH 146 746 746 HOH HOH B . V 4 HOH 147 747 747 HOH HOH B . V 4 HOH 148 748 748 HOH HOH B . V 4 HOH 149 749 749 HOH HOH B . V 4 HOH 150 750 750 HOH HOH B . V 4 HOH 151 751 751 HOH HOH B . V 4 HOH 152 752 752 HOH HOH B . V 4 HOH 153 753 753 HOH HOH B . V 4 HOH 154 754 754 HOH HOH B . V 4 HOH 155 755 755 HOH HOH B . V 4 HOH 156 756 756 HOH HOH B . V 4 HOH 157 757 757 HOH HOH B . V 4 HOH 158 758 758 HOH HOH B . V 4 HOH 159 759 759 HOH HOH B . V 4 HOH 160 760 760 HOH HOH B . V 4 HOH 161 761 761 HOH HOH B . V 4 HOH 162 762 762 HOH HOH B . V 4 HOH 163 763 763 HOH HOH B . V 4 HOH 164 764 764 HOH HOH B . V 4 HOH 165 765 765 HOH HOH B . V 4 HOH 166 766 766 HOH HOH B . V 4 HOH 167 767 767 HOH HOH B . V 4 HOH 168 768 768 HOH HOH B . V 4 HOH 169 769 769 HOH HOH B . V 4 HOH 170 770 770 HOH HOH B . V 4 HOH 171 771 771 HOH HOH B . V 4 HOH 172 772 772 HOH HOH B . V 4 HOH 173 773 773 HOH HOH B . V 4 HOH 174 774 774 HOH HOH B . V 4 HOH 175 775 775 HOH HOH B . V 4 HOH 176 776 776 HOH HOH B . V 4 HOH 177 777 777 HOH HOH B . V 4 HOH 178 778 778 HOH HOH B . V 4 HOH 179 779 779 HOH HOH B . V 4 HOH 180 780 780 HOH HOH B . V 4 HOH 181 781 781 HOH HOH B . V 4 HOH 182 782 782 HOH HOH B . V 4 HOH 183 783 783 HOH HOH B . V 4 HOH 184 784 784 HOH HOH B . V 4 HOH 185 785 785 HOH HOH B . V 4 HOH 186 786 786 HOH HOH B . V 4 HOH 187 787 787 HOH HOH B . V 4 HOH 188 788 788 HOH HOH B . V 4 HOH 189 789 789 HOH HOH B . V 4 HOH 190 790 790 HOH HOH B . V 4 HOH 191 791 791 HOH HOH B . V 4 HOH 192 792 792 HOH HOH B . V 4 HOH 193 793 793 HOH HOH B . V 4 HOH 194 794 794 HOH HOH B . V 4 HOH 195 795 795 HOH HOH B . V 4 HOH 196 796 796 HOH HOH B . # 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 207 A ASN 289 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 228 A ASN 310 ? ASN 'GLYCOSYLATION SITE' 3 A THR 5 A THR 87 ? THR 'GLYCOSYLATION SITE' 4 A THR 15 A THR 97 ? THR 'GLYCOSYLATION SITE' 5 A SER 24 A SER 106 ? SER 'GLYCOSYLATION SITE' 6 A SER 27 A SER 109 ? SER 'GLYCOSYLATION SITE' 7 A SER 28 A SER 110 ? SER 'GLYCOSYLATION SITE' 8 A SER 33 A SER 115 ? SER 'GLYCOSYLATION SITE' 9 A THR 40 A THR 122 ? THR 'GLYCOSYLATION SITE' 10 B ASN 207 B ASN 289 ? ASN 'GLYCOSYLATION SITE' 11 B ASN 228 B ASN 310 ? ASN 'GLYCOSYLATION SITE' 12 B THR 5 B THR 87 ? THR 'GLYCOSYLATION SITE' 13 B THR 15 B THR 97 ? THR 'GLYCOSYLATION SITE' 14 B SER 24 B SER 106 ? SER 'GLYCOSYLATION SITE' 15 B SER 27 B SER 109 ? SER 'GLYCOSYLATION SITE' 16 B SER 28 B SER 110 ? SER 'GLYCOSYLATION SITE' 17 B SER 33 B SER 115 ? SER 'GLYCOSYLATION SITE' 18 B THR 40 B THR 122 ? THR 'GLYCOSYLATION SITE' # loop_ _pdbx_struct_assembly.id _pdbx_struct_assembly.details _pdbx_struct_assembly.method_details _pdbx_struct_assembly.oligomeric_details _pdbx_struct_assembly.oligomeric_count 1 author_defined_assembly ? monomeric 1 2 author_defined_assembly ? monomeric 1 # loop_ _pdbx_struct_assembly_gen.assembly_id _pdbx_struct_assembly_gen.oper_expression _pdbx_struct_assembly_gen.asym_id_list 1 1 A,C,D,E,F,G,H,I,J,K,U 2 1 B,L,M,N,O,P,Q,R,S,T,V # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 1996-10-14 2 'Structure model' 1 1 2008-03-24 3 'Structure model' 1 2 2011-07-13 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Non-polymer description' 3 3 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal HAMLIN 'data collection' . ? 1 X-PLOR refinement . ? 2 HAMLIN 'data reduction' . ? 3 # _pdbx_entry_details.entry_id 1CB2 _pdbx_entry_details.compound_details 'THE CATALYTIC CORE STARTS AT RESIDUE 83.' _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details ? # 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 ASP A 140 ? ? -67.94 0.21 2 1 ASN A 161 ? ? -145.08 57.15 3 1 PHE A 169 ? ? -151.06 78.17 4 1 ASP A 170 ? ? -155.59 35.02 5 1 ASP A 189 ? ? -109.41 59.27 6 1 TYR A 209 ? ? -107.92 50.94 7 1 GLU A 219 ? ? 39.94 78.76 8 1 SER A 222 ? ? -117.94 -81.45 9 1 TRP A 269 ? ? -109.94 -67.66 10 1 GLN A 319 ? ? -39.59 125.01 11 1 ASN A 369 ? ? 37.62 51.80 12 1 ASP B 140 ? ? -67.98 0.25 13 1 ASN B 161 ? ? -145.12 57.18 14 1 PHE B 169 ? ? -151.06 78.13 15 1 ASP B 170 ? ? -155.59 35.00 16 1 ASP B 189 ? ? -109.39 59.22 17 1 TYR B 209 ? ? -107.91 50.92 18 1 GLU B 219 ? ? 39.90 78.78 19 1 SER B 222 ? ? -117.95 -81.45 20 1 TRP B 269 ? ? -109.98 -67.69 21 1 GLN B 319 ? ? -39.54 125.00 22 1 ASN B 369 ? ? 37.70 51.76 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A SER 83 ? A SER 1 2 1 Y 1 A GLY 84 ? A GLY 2 3 1 Y 1 B SER 83 ? B SER 1 4 1 Y 1 B GLY 84 ? B GLY 2 # 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 water HOH #