data_1H3J # _entry.id 1H3J # _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 1H3J WWPDB D_1290011360 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 1LY8 unspecified ;THE CRYSTAL STRUCTURE OF A MUTANT ENZYME OF COPRINUSCINEREUS PEROXIDASE PROVIDES AN UNDERSTANDING OF ITSINCREASED THERMOSTABILITY AND INSIGHT INTO MODELLING OFPROTEIN STRUCTURES ; PDB 1LY9 unspecified 'THE IMPACT OF THE PHYSICAL AND CHEMICAL ENVIRONMENT ON THEMOLECULAR STRUCTURE OF COPRINUS CINEREUS PEROXIDASE' PDB 1LYC unspecified 'THE IMPACT OF THE PHYSICAL AND CHEMICAL ENVIROMENT ON THEMOLECULAR STRUCTURE OF COPRINUS CINEREUS PEROXIDASE' PDB 1LYK unspecified 'THE IMPACT OF THE PHYSICAL AND CHEMICAL ENVIROMENT ON THEMOLECULAR STRUCTURE OF COPRINUS CINEREUS PEROXIDASE' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 1H3J _pdbx_database_status.recvd_initial_deposition_date 2002-09-05 _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Petersen, J.F.W.' 1 'Houborg, K.' 2 'Harris, P.' 3 'Larsen, S.' 4 # 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 'Impact of the Physical and Chemical Environment on the Molecular Structure of Coprinus Cinereus Peroxidase' 'Acta Crystallogr.,Sect.D' 59 989 ? 2003 ABCRE6 DK 0907-4449 0766 ? 12777760 10.1107/S0907444903006772 1 'Three-Dimensional Sturcture of a Recombinant Peroxidase from Coprinus Cinereus at 2.6 A' 'FEBS Lett.' 339 291 ? 1994 FEBLAL NE 0014-5793 0165 ? 8112469 '10.1016/0014-5793(94)80433-8' # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Houborg, K.' 1 primary 'Harris, P.' 2 primary 'Petersen, J.F.W.' 3 primary 'Rowland, P.' 4 primary 'Poulsen, J.' 5 primary 'Schneider, P.' 6 primary 'Vind, J.' 7 primary 'Larsen, S.' 8 1 'Petersen, J.F.W.' 9 1 'Kadziola, A.' 10 1 'Larsen, S.' 11 # _cell.entry_id 1H3J _cell.length_a 127.180 _cell.length_b 75.530 _cell.length_c 76.600 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1H3J _symmetry.space_group_name_H-M 'P 21 21 21' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 19 # 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 PEROXIDASE 35509.605 2 1.11.1.7 ? 'CATALYTIC DOMAIN, RESIDUES 22-363' 'N-LINKED GLYCOSYLATION SITE AT ASN142 O-LINKED GLYCOSYLATION SITE AT SER338' 2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487 2 ? ? ? ? 3 non-polymer syn 'CALCIUM ION' 40.078 4 ? ? ? ? 4 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? 5 non-polymer man BETA-D-MANNOSE 180.156 2 ? ? ? ? 6 non-polymer syn 'MAGNESIUM ION' 24.305 1 ? ? ? ? 7 water nat water 18.015 498 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name CIP1 # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer yes _entity_poly.pdbx_seq_one_letter_code ;GPGGGGSVTCPGGQSTSNSQCCVWFDVLDDLQTNFYQGSKCESPVRKILRIVFHDAIGFSPALTAAGQFGGGGADGSIIA HSNIELAFPANGGLTDTVEALRAVGINHGVSFGDLIQFATAVGMSNCPGSPRLEFLTGRSNSSQPSPPSLIPGPGNTVTA ILDRMGDAGFSPDEVVDLLAA(HSO)SLASQEGLNSAIFRSPLDSTPQVFDTQFYIETLLKGTTQPGPSLGFAEELSPFP GEFRMRSDALLARDSRTACRWQSMTSSNEVMGQRYRAAMAKMSVLGFDRNALTDCSDVIPSAVSNNAAPVIPGGLTVDDI EVSCPSEPFPEIATASGPLPSLAPAP ; _entity_poly.pdbx_seq_one_letter_code_can ;GPGGGGSVTCPGGQSTSNSQCCVWFDVLDDLQTNFYQGSKCESPVRKILRIVFHDAIGFSPALTAAGQFGGGGADGSIIA HSNIELAFPANGGLTDTVEALRAVGINHGVSFGDLIQFATAVGMSNCPGSPRLEFLTGRSNSSQPSPPSLIPGPGNTVTA ILDRMGDAGFSPDEVVDLLAAHSLASQEGLNSAIFRSPLDSTPQVFDTQFYIETLLKGTTQPGPSLGFAEELSPFPGEFR MRSDALLARDSRTACRWQSMTSSNEVMGQRYRAAMAKMSVLGFDRNALTDCSDVIPSAVSNNAAPVIPGGLTVDDIEVSC PSEPFPEIATASGPLPSLAPAP ; _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 GLY n 1 2 PRO n 1 3 GLY n 1 4 GLY n 1 5 GLY n 1 6 GLY n 1 7 SER n 1 8 VAL n 1 9 THR n 1 10 CYS n 1 11 PRO n 1 12 GLY n 1 13 GLY n 1 14 GLN n 1 15 SER n 1 16 THR n 1 17 SER n 1 18 ASN n 1 19 SER n 1 20 GLN n 1 21 CYS n 1 22 CYS n 1 23 VAL n 1 24 TRP n 1 25 PHE n 1 26 ASP n 1 27 VAL n 1 28 LEU n 1 29 ASP n 1 30 ASP n 1 31 LEU n 1 32 GLN n 1 33 THR n 1 34 ASN n 1 35 PHE n 1 36 TYR n 1 37 GLN n 1 38 GLY n 1 39 SER n 1 40 LYS n 1 41 CYS n 1 42 GLU n 1 43 SER n 1 44 PRO n 1 45 VAL n 1 46 ARG n 1 47 LYS n 1 48 ILE n 1 49 LEU n 1 50 ARG n 1 51 ILE n 1 52 VAL n 1 53 PHE n 1 54 HIS n 1 55 ASP n 1 56 ALA n 1 57 ILE n 1 58 GLY n 1 59 PHE n 1 60 SER n 1 61 PRO n 1 62 ALA n 1 63 LEU n 1 64 THR n 1 65 ALA n 1 66 ALA n 1 67 GLY n 1 68 GLN n 1 69 PHE n 1 70 GLY n 1 71 GLY n 1 72 GLY n 1 73 GLY n 1 74 ALA n 1 75 ASP n 1 76 GLY n 1 77 SER n 1 78 ILE n 1 79 ILE n 1 80 ALA n 1 81 HIS n 1 82 SER n 1 83 ASN n 1 84 ILE n 1 85 GLU n 1 86 LEU n 1 87 ALA n 1 88 PHE n 1 89 PRO n 1 90 ALA n 1 91 ASN n 1 92 GLY n 1 93 GLY n 1 94 LEU n 1 95 THR n 1 96 ASP n 1 97 THR n 1 98 VAL n 1 99 GLU n 1 100 ALA n 1 101 LEU n 1 102 ARG n 1 103 ALA n 1 104 VAL n 1 105 GLY n 1 106 ILE n 1 107 ASN n 1 108 HIS n 1 109 GLY n 1 110 VAL n 1 111 SER n 1 112 PHE n 1 113 GLY n 1 114 ASP n 1 115 LEU n 1 116 ILE n 1 117 GLN n 1 118 PHE n 1 119 ALA n 1 120 THR n 1 121 ALA n 1 122 VAL n 1 123 GLY n 1 124 MET n 1 125 SER n 1 126 ASN n 1 127 CYS n 1 128 PRO n 1 129 GLY n 1 130 SER n 1 131 PRO n 1 132 ARG n 1 133 LEU n 1 134 GLU n 1 135 PHE n 1 136 LEU n 1 137 THR n 1 138 GLY n 1 139 ARG n 1 140 SER n 1 141 ASN n 1 142 SER n 1 143 SER n 1 144 GLN n 1 145 PRO n 1 146 SER n 1 147 PRO n 1 148 PRO n 1 149 SER n 1 150 LEU n 1 151 ILE n 1 152 PRO n 1 153 GLY n 1 154 PRO n 1 155 GLY n 1 156 ASN n 1 157 THR n 1 158 VAL n 1 159 THR n 1 160 ALA n 1 161 ILE n 1 162 LEU n 1 163 ASP n 1 164 ARG n 1 165 MET n 1 166 GLY n 1 167 ASP n 1 168 ALA n 1 169 GLY n 1 170 PHE n 1 171 SER n 1 172 PRO n 1 173 ASP n 1 174 GLU n 1 175 VAL n 1 176 VAL n 1 177 ASP n 1 178 LEU n 1 179 LEU n 1 180 ALA n 1 181 ALA n 1 182 HSO n 1 183 SER n 1 184 LEU n 1 185 ALA n 1 186 SER n 1 187 GLN n 1 188 GLU n 1 189 GLY n 1 190 LEU n 1 191 ASN n 1 192 SER n 1 193 ALA n 1 194 ILE n 1 195 PHE n 1 196 ARG n 1 197 SER n 1 198 PRO n 1 199 LEU n 1 200 ASP n 1 201 SER n 1 202 THR n 1 203 PRO n 1 204 GLN n 1 205 VAL n 1 206 PHE n 1 207 ASP n 1 208 THR n 1 209 GLN n 1 210 PHE n 1 211 TYR n 1 212 ILE n 1 213 GLU n 1 214 THR n 1 215 LEU n 1 216 LEU n 1 217 LYS n 1 218 GLY n 1 219 THR n 1 220 THR n 1 221 GLN n 1 222 PRO n 1 223 GLY n 1 224 PRO n 1 225 SER n 1 226 LEU n 1 227 GLY n 1 228 PHE n 1 229 ALA n 1 230 GLU n 1 231 GLU n 1 232 LEU n 1 233 SER n 1 234 PRO n 1 235 PHE n 1 236 PRO n 1 237 GLY n 1 238 GLU n 1 239 PHE n 1 240 ARG n 1 241 MET n 1 242 ARG n 1 243 SER n 1 244 ASP n 1 245 ALA n 1 246 LEU n 1 247 LEU n 1 248 ALA n 1 249 ARG n 1 250 ASP n 1 251 SER n 1 252 ARG n 1 253 THR n 1 254 ALA n 1 255 CYS n 1 256 ARG n 1 257 TRP n 1 258 GLN n 1 259 SER n 1 260 MET n 1 261 THR n 1 262 SER n 1 263 SER n 1 264 ASN n 1 265 GLU n 1 266 VAL n 1 267 MET n 1 268 GLY n 1 269 GLN n 1 270 ARG n 1 271 TYR n 1 272 ARG n 1 273 ALA n 1 274 ALA n 1 275 MET n 1 276 ALA n 1 277 LYS n 1 278 MET n 1 279 SER n 1 280 VAL n 1 281 LEU n 1 282 GLY n 1 283 PHE n 1 284 ASP n 1 285 ARG n 1 286 ASN n 1 287 ALA n 1 288 LEU n 1 289 THR n 1 290 ASP n 1 291 CYS n 1 292 SER n 1 293 ASP n 1 294 VAL n 1 295 ILE n 1 296 PRO n 1 297 SER n 1 298 ALA n 1 299 VAL n 1 300 SER n 1 301 ASN n 1 302 ASN n 1 303 ALA n 1 304 ALA n 1 305 PRO n 1 306 VAL n 1 307 ILE n 1 308 PRO n 1 309 GLY n 1 310 GLY n 1 311 LEU n 1 312 THR n 1 313 VAL n 1 314 ASP n 1 315 ASP n 1 316 ILE n 1 317 GLU n 1 318 VAL n 1 319 SER n 1 320 CYS n 1 321 PRO n 1 322 SER n 1 323 GLU n 1 324 PRO n 1 325 PHE n 1 326 PRO n 1 327 GLU n 1 328 ILE n 1 329 ALA n 1 330 THR n 1 331 ALA n 1 332 SER n 1 333 GLY n 1 334 PRO n 1 335 LEU n 1 336 PRO n 1 337 SER n 1 338 LEU n 1 339 ALA n 1 340 PRO n 1 341 ALA n 1 342 PRO 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 'INKY CAP FUNGUS' _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene ? _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'COPRINUS CINEREUS' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 5346 _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 'ASPERGILLUS ORYZAE' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 5062 _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type ? _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code PER_COPCI _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? _struct_ref.pdbx_db_accession P28314 _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 1H3J A 1 ? 342 ? P28314 22 ? 363 ? 2 343 2 1 1H3J B 1 ? 342 ? P28314 22 ? 363 ? 2 343 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 CA non-polymer . 'CALCIUM ION' ? 'Ca 2' 40.078 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HEM non-polymer . 'PROTOPORPHYRIN IX CONTAINING FE' HEME 'C34 H32 Fe N4 O4' 616.487 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 HSO 'L-peptide linking' n L-histidinol ? 'C6 H12 N3 O 1' 142.179 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 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 MG non-polymer . 'MAGNESIUM ION' ? 'Mg 2' 24.305 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 1H3J _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.59 _exptl_crystal.density_percent_sol 52.52 _exptl_crystal.description ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 7.00 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '18% PEG6000, 0.35 M MGCL2, 0.1 M HEPES, PH 7.0' # _diffrn.id 1 _diffrn.ambient_temp 293.0 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector 'IMAGE PLATE' _diffrn_detector.type 'RIGAKU IMAGE PLATE' _diffrn_detector.pdbx_collection_date ? _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 'NI FILTER' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _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 'ROTATING ANODE' _diffrn_source.type RIGAKU _diffrn_source.pdbx_synchrotron_site ? _diffrn_source.pdbx_synchrotron_beamline ? _diffrn_source.pdbx_wavelength 1.5418 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 1H3J _reflns.observed_criterion_sigma_I ? _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 30.000 _reflns.d_resolution_high 2.000 _reflns.number_obs 50569 _reflns.number_all ? _reflns.percent_possible_obs 100.0 _reflns.pdbx_Rmerge_I_obs 0.07000 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 3.700 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.00 _reflns_shell.d_res_low 2.11 _reflns_shell.percent_possible_all 100.0 _reflns_shell.Rmerge_I_obs 0.20900 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_redundancy 2.90 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 1H3J _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 48695 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 2.0 _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 98 _refine.ls_R_factor_obs 0.186 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.186 _refine.ls_R_factor_R_free 0.256 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 10.0 _refine.ls_number_reflns_R_free ? _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean ? _refine.aniso_B[1][1] ? _refine.aniso_B[2][2] ? _refine.aniso_B[3][3] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][3] ? _refine.solvent_model_details ? _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.pdbx_ls_cross_valid_method THROUGOUT _refine.details ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ? _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML ? _refine.pdbx_overall_phase_error ? _refine.overall_SU_B ? _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 4924 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 169 _refine_hist.number_atoms_solvent 498 _refine_hist.number_atoms_total 5591 _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 0.02 ? ? ? '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 2.0 ? ? ? 'X-RAY DIFFRACTION' ? x_angle_deg_na ? ? ? ? 'X-RAY DIFFRACTION' ? x_angle_deg_prot ? ? ? ? 'X-RAY DIFFRACTION' ? x_dihedral_angle_d 24 ? ? ? 'X-RAY DIFFRACTION' ? x_dihedral_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? x_dihedral_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? x_improper_angle_d ? ? ? ? 'X-RAY DIFFRACTION' ? x_improper_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? x_improper_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? x_mcbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? x_mcangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? x_scbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? x_scangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? # _struct.entry_id 1H3J _struct.title 'STRUCTURE OF RECOMBINANT COPRINUS CINEREUS PEROXIDASE DETERMINED TO 2.0 A' _struct.pdbx_descriptor 'PEROXIDASE (E.C.1.11.1.7)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1H3J _struct_keywords.pdbx_keywords OXIDOREDUCTASE _struct_keywords.text 'OXIDOREDUCTASE, PEROXIDASE, HEME, CALCIUM-BINDING' # 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 3 ? E N N 3 ? F N N 4 ? G N N 4 ? H N N 5 ? I N N 6 ? J N N 2 ? K N N 3 ? L N N 3 ? M N N 4 ? N N N 4 ? O N N 5 ? P N N 7 ? Q N N 7 ? # _struct_biol.id 1 # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 AA1 ASN A 18 ? GLN A 20 ? ASN A 19 GLN A 21 5 ? 3 HELX_P HELX_P2 AA2 CYS A 21 ? ASN A 34 ? CYS A 22 ASN A 35 1 ? 14 HELX_P HELX_P3 AA3 GLU A 42 ? ILE A 57 ? GLU A 43 ILE A 58 1 ? 16 HELX_P HELX_P4 AA4 SER A 60 ? ALA A 66 ? SER A 61 ALA A 67 1 ? 7 HELX_P HELX_P5 AA5 GLY A 76 ? HIS A 81 ? GLY A 77 HIS A 82 1 ? 6 HELX_P HELX_P6 AA6 HIS A 81 ? LEU A 86 ? HIS A 82 LEU A 87 1 ? 6 HELX_P HELX_P7 AA7 ALA A 87 ? GLY A 92 ? ALA A 88 GLY A 93 5 ? 6 HELX_P HELX_P8 AA8 LEU A 94 ? GLY A 109 ? LEU A 95 GLY A 110 1 ? 16 HELX_P HELX_P9 AA9 SER A 111 ? ASN A 126 ? SER A 112 ASN A 127 1 ? 16 HELX_P HELX_P10 AB1 THR A 157 ? GLY A 169 ? THR A 158 GLY A 170 1 ? 13 HELX_P HELX_P11 AB2 SER A 171 ? LEU A 179 ? SER A 172 LEU A 180 1 ? 9 HELX_P HELX_P12 AB3 ALA A 180 ? LEU A 184 ? ALA A 181 LEU A 185 5 ? 5 HELX_P HELX_P13 AB4 ASN A 191 ? PHE A 195 ? ASN A 192 PHE A 196 5 ? 5 HELX_P HELX_P14 AB5 THR A 208 ? THR A 214 ? THR A 209 THR A 215 1 ? 7 HELX_P HELX_P15 AB6 ARG A 242 ? ASP A 250 ? ARG A 243 ASP A 251 1 ? 9 HELX_P HELX_P16 AB7 THR A 253 ? MET A 260 ? THR A 254 MET A 261 1 ? 8 HELX_P HELX_P17 AB8 SER A 263 ? SER A 279 ? SER A 264 SER A 280 1 ? 17 HELX_P HELX_P18 AB9 ASP A 284 ? LEU A 288 ? ASP A 285 LEU A 289 5 ? 5 HELX_P HELX_P19 AC1 SER A 292 ? ILE A 295 ? SER A 293 ILE A 296 5 ? 4 HELX_P HELX_P20 AC2 THR A 312 ? ILE A 316 ? THR A 313 ILE A 317 5 ? 5 HELX_P HELX_P21 AC3 ASN B 18 ? GLN B 20 ? ASN B 19 GLN B 21 5 ? 3 HELX_P HELX_P22 AC4 CYS B 21 ? ASN B 34 ? CYS B 22 ASN B 35 1 ? 14 HELX_P HELX_P23 AC5 GLU B 42 ? ILE B 57 ? GLU B 43 ILE B 58 1 ? 16 HELX_P HELX_P24 AC6 SER B 60 ? ALA B 65 ? SER B 61 ALA B 66 1 ? 6 HELX_P HELX_P25 AC7 GLY B 76 ? HIS B 81 ? GLY B 77 HIS B 82 1 ? 6 HELX_P HELX_P26 AC8 HIS B 81 ? LEU B 86 ? HIS B 82 LEU B 87 1 ? 6 HELX_P HELX_P27 AC9 ALA B 87 ? GLY B 92 ? ALA B 88 GLY B 93 5 ? 6 HELX_P HELX_P28 AD1 LEU B 94 ? GLY B 109 ? LEU B 95 GLY B 110 1 ? 16 HELX_P HELX_P29 AD2 SER B 111 ? SER B 125 ? SER B 112 SER B 126 1 ? 15 HELX_P HELX_P30 AD3 THR B 157 ? GLY B 169 ? THR B 158 GLY B 170 1 ? 13 HELX_P HELX_P31 AD4 SER B 171 ? LEU B 179 ? SER B 172 LEU B 180 1 ? 9 HELX_P HELX_P32 AD5 ALA B 180 ? LEU B 184 ? ALA B 181 LEU B 185 5 ? 5 HELX_P HELX_P33 AD6 ASN B 191 ? PHE B 195 ? ASN B 192 PHE B 196 5 ? 5 HELX_P HELX_P34 AD7 THR B 208 ? THR B 214 ? THR B 209 THR B 215 1 ? 7 HELX_P HELX_P35 AD8 ARG B 242 ? ASP B 250 ? ARG B 243 ASP B 251 1 ? 9 HELX_P HELX_P36 AD9 THR B 253 ? MET B 260 ? THR B 254 MET B 261 1 ? 8 HELX_P HELX_P37 AE1 SER B 263 ? SER B 279 ? SER B 264 SER B 280 1 ? 17 HELX_P HELX_P38 AE2 ASP B 284 ? LEU B 288 ? ASP B 285 LEU B 289 5 ? 5 HELX_P HELX_P39 AE3 SER B 292 ? ILE B 295 ? SER B 293 ILE B 296 5 ? 4 HELX_P HELX_P40 AE4 THR B 312 ? ILE B 316 ? THR B 313 ILE B 317 5 ? 5 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 10 SG ? ? ? 1_555 A CYS 22 SG ? ? A CYS 11 A CYS 23 1_555 ? ? ? ? ? ? ? 2.045 ? disulf2 disulf ? ? A CYS 21 SG ? ? ? 1_555 A CYS 291 SG ? ? A CYS 22 A CYS 292 1_555 ? ? ? ? ? ? ? 2.044 ? disulf3 disulf ? ? A CYS 41 SG ? ? ? 1_555 A CYS 127 SG ? ? A CYS 42 A CYS 128 1_555 ? ? ? ? ? ? ? 2.013 ? disulf4 disulf ? ? A CYS 255 SG ? ? ? 1_555 A CYS 320 SG ? ? A CYS 256 A CYS 321 1_555 ? ? ? ? ? ? ? 2.038 ? disulf5 disulf ? ? B CYS 10 SG ? ? ? 1_555 B CYS 22 SG ? ? B CYS 11 B CYS 23 1_555 ? ? ? ? ? ? ? 2.049 ? disulf6 disulf ? ? B CYS 21 SG ? ? ? 1_555 B CYS 291 SG ? ? B CYS 22 B CYS 292 1_555 ? ? ? ? ? ? ? 2.042 ? disulf7 disulf ? ? B CYS 41 SG ? ? ? 1_555 B CYS 127 SG ? ? B CYS 42 B CYS 128 1_555 ? ? ? ? ? ? ? 2.019 ? disulf8 disulf ? ? B CYS 255 SG ? ? ? 1_555 B CYS 320 SG ? ? B CYS 256 B CYS 321 1_555 ? ? ? ? ? ? ? 2.017 ? metalc1 metalc ? ? A ASP 55 O ? ? ? 1_555 D CA . CA ? ? A ASP 56 A CA 402 1_555 ? ? ? ? ? ? ? 2.406 ? metalc2 metalc ? ? A ASP 55 OD1 ? ? ? 1_555 D CA . CA ? ? A ASP 56 A CA 402 1_555 ? ? ? ? ? ? ? 2.324 ? metalc3 metalc ? ? A GLY 73 O ? ? ? 1_555 D CA . CA ? ? A GLY 74 A CA 402 1_555 ? ? ? ? ? ? ? 2.472 ? metalc4 metalc ? ? A ASP 75 OD2 ? ? ? 1_555 D CA . CA ? ? A ASP 76 A CA 402 1_555 ? ? ? ? ? ? ? 2.589 ? metalc5 metalc ? ? A SER 77 OG ? ? ? 1_555 D CA . CA ? ? A SER 78 A CA 402 1_555 ? ? ? ? ? ? ? 2.400 ? covale1 covale one ? A ASN 141 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 142 A NAG 404 1_555 ? ? ? ? ? ? ? 1.445 ? covale2 covale both ? A ALA 181 C ? ? ? 1_555 A HSO 182 N ? ? A ALA 182 A HSO 183 1_555 ? ? ? ? ? ? ? 1.336 ? metalc6 metalc ? ? A HSO 182 NE2 ? ? ? 1_555 C HEM . FE ? ? A HSO 183 A HEM 401 1_555 ? ? ? ? ? ? ? 2.195 ? covale3 covale one ? A HSO 182 C ? ? ? 1_555 A SER 183 N ? ? A HSO 183 A SER 184 1_555 ? ? ? ? ? ? ? 1.328 ? metalc7 metalc ? ? A SER 183 O ? ? ? 1_555 E CA . CA ? ? A SER 184 A CA 403 1_555 ? ? ? ? ? ? ? 2.408 ? metalc8 metalc ? ? A SER 183 OG ? ? ? 1_555 E CA . CA ? ? A SER 184 A CA 403 1_555 ? ? ? ? ? ? ? 2.624 ? metalc9 metalc ? ? A ASP 200 OD1 ? ? ? 1_555 E CA . CA ? ? A ASP 201 A CA 403 1_555 ? ? ? ? ? ? ? 2.799 ? metalc10 metalc ? ? A ASP 200 OD2 ? ? ? 1_555 E CA . CA ? ? A ASP 201 A CA 403 1_555 ? ? ? ? ? ? ? 2.561 ? metalc11 metalc ? ? A THR 202 O ? ? ? 1_555 E CA . CA ? ? A THR 203 A CA 403 1_555 ? ? ? ? ? ? ? 2.046 ? metalc12 metalc ? ? A THR 202 OG1 ? ? ? 1_555 E CA . CA ? ? A THR 203 A CA 403 1_555 ? ? ? ? ? ? ? 2.492 ? metalc13 metalc ? ? A VAL 205 O ? ? ? 1_555 E CA . CA ? ? A VAL 206 A CA 403 1_555 ? ? ? ? ? ? ? 2.388 ? metalc14 metalc ? ? A ASP 207 OD1 ? ? ? 1_555 E CA . CA ? ? A ASP 208 A CA 403 1_555 ? ? ? ? ? ? ? 2.547 ? covale4 covale one ? A SER 337 OG ? ? ? 1_555 H BMA . C1 ? ? A SER 338 A BMA 406 1_555 ? ? ? ? ? ? ? 1.363 ? metalc15 metalc ? ? B ASP 55 O ? ? ? 1_555 K CA . CA ? ? B ASP 56 B CA 402 1_555 ? ? ? ? ? ? ? 2.302 ? metalc16 metalc ? ? B ASP 55 OD2 ? ? ? 1_555 K CA . CA ? ? B ASP 56 B CA 402 1_555 ? ? ? ? ? ? ? 2.445 ? metalc17 metalc ? ? B GLY 73 O ? ? ? 1_555 K CA . CA ? ? B GLY 74 B CA 402 1_555 ? ? ? ? ? ? ? 2.545 ? metalc18 metalc ? ? B ASP 75 OD2 ? ? ? 1_555 K CA . CA ? ? B ASP 76 B CA 402 1_555 ? ? ? ? ? ? ? 2.651 ? metalc19 metalc ? ? B SER 77 OG ? ? ? 1_555 K CA . CA ? ? B SER 78 B CA 402 1_555 ? ? ? ? ? ? ? 2.456 ? covale5 covale one ? B ASN 141 ND2 ? ? ? 1_555 M NAG . C1 ? ? B ASN 142 B NAG 404 1_555 ? ? ? ? ? ? ? 1.425 ? covale6 covale both ? B ALA 181 C ? ? ? 1_555 B HSO 182 N ? ? B ALA 182 B HSO 183 1_555 ? ? ? ? ? ? ? 1.338 ? metalc20 metalc ? ? B HSO 182 NE2 ? ? ? 1_555 J HEM . FE ? ? B HSO 183 B HEM 401 1_555 ? ? ? ? ? ? ? 2.173 ? covale7 covale one ? B HSO 182 C ? ? ? 1_555 B SER 183 N ? ? B HSO 183 B SER 184 1_555 ? ? ? ? ? ? ? 1.333 ? metalc21 metalc ? ? B SER 183 O ? ? ? 1_555 L CA . CA ? ? B SER 184 B CA 403 1_555 ? ? ? ? ? ? ? 2.316 ? metalc22 metalc ? ? B SER 183 OG ? ? ? 1_555 L CA . CA ? ? B SER 184 B CA 403 1_555 ? ? ? ? ? ? ? 2.383 ? metalc23 metalc ? ? B ASP 200 OD1 ? ? ? 1_555 L CA . CA ? ? B ASP 201 B CA 403 1_555 ? ? ? ? ? ? ? 2.722 ? metalc24 metalc ? ? B ASP 200 OD2 ? ? ? 1_555 L CA . CA ? ? B ASP 201 B CA 403 1_555 ? ? ? ? ? ? ? 2.473 ? metalc25 metalc ? ? B THR 202 O ? ? ? 1_555 L CA . CA ? ? B THR 203 B CA 403 1_555 ? ? ? ? ? ? ? 2.227 ? metalc26 metalc ? ? B THR 202 OG1 ? ? ? 1_555 L CA . CA ? ? B THR 203 B CA 403 1_555 ? ? ? ? ? ? ? 2.597 ? metalc27 metalc ? ? B VAL 205 O ? ? ? 1_555 L CA . CA ? ? B VAL 206 B CA 403 1_555 ? ? ? ? ? ? ? 2.474 ? metalc28 metalc ? ? B ASP 207 OD1 ? ? ? 1_555 L CA . CA ? ? B ASP 208 B CA 403 1_555 ? ? ? ? ? ? ? 2.601 ? covale8 covale one ? B SER 337 OG ? ? ? 1_555 O BMA . C1 ? ? B SER 338 B BMA 406 1_555 ? ? ? ? ? ? ? 1.359 ? metalc29 metalc ? ? C HEM . FE ? ? ? 1_555 P HOH . O ? ? A HEM 401 A HOH 629 1_555 ? ? ? ? ? ? ? 2.449 ? metalc30 metalc ? ? D CA . CA ? ? ? 1_555 P HOH . O ? ? A CA 402 A HOH 563 1_555 ? ? ? ? ? ? ? 2.462 ? metalc31 metalc ? ? D CA . CA ? ? ? 1_555 P HOH . O ? ? A CA 402 A HOH 593 1_555 ? ? ? ? ? ? ? 2.214 ? covale9 covale both ? F NAG . O4 ? ? ? 1_555 G NAG . C1 ? ? A NAG 404 A NAG 405 1_555 ? ? ? ? ? ? ? 1.426 ? metalc32 metalc ? ? I MG . MG ? ? ? 1_555 P HOH . O ? ? A MG 407 A HOH 552 1_555 ? ? ? ? ? ? ? 2.102 ? metalc33 metalc ? ? I MG . MG ? ? ? 1_555 P HOH . O ? ? A MG 407 A HOH 610 1_555 ? ? ? ? ? ? ? 2.150 ? metalc34 metalc ? ? J HEM . FE ? ? ? 1_555 Q HOH . O ? ? B HEM 401 B HOH 629 1_555 ? ? ? ? ? ? ? 2.331 ? metalc35 metalc ? ? K CA . CA ? ? ? 1_555 Q HOH . O ? ? B CA 402 B HOH 554 1_555 ? ? ? ? ? ? ? 2.276 ? metalc36 metalc ? ? K CA . CA ? ? ? 1_555 Q HOH . O ? ? B CA 402 B HOH 587 1_555 ? ? ? ? ? ? ? 2.294 ? covale10 covale both ? M NAG . O4 ? ? ? 1_555 N NAG . C1 ? ? B NAG 404 B NAG 405 1_555 ? ? ? ? ? ? ? 1.390 ? metalc37 metalc ? ? I MG . MG ? ? ? 1_555 Q HOH . O ? ? A MG 407 B HOH 540 2_555 ? ? ? ? ? ? ? 2.080 ? metalc38 metalc ? ? I MG . MG ? ? ? 1_555 Q HOH . O ? ? A MG 407 B HOH 595 2_555 ? ? ? ? ? ? ? 2.148 ? metalc39 metalc ? ? I MG . MG ? ? ? 1_555 Q HOH . O ? ? A MG 407 B HOH 689 2_555 ? ? ? ? ? ? ? 1.951 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? metalc ? ? covale ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 GLY 333 A . ? GLY 334 A PRO 334 A ? PRO 335 A 1 -0.22 2 GLY 333 B . ? GLY 334 B PRO 334 B ? PRO 335 B 1 -0.09 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA1 ? 2 ? AA2 ? 2 ? AA3 ? 2 ? AA4 ? 2 ? AA5 ? 2 ? AA6 ? 2 ? AA7 ? 2 ? AA8 ? 2 ? AA9 ? 2 ? AB1 ? 2 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense AA1 1 2 ? anti-parallel AA2 1 2 ? anti-parallel AA3 1 2 ? anti-parallel AA4 1 2 ? anti-parallel AA5 1 2 ? parallel AA6 1 2 ? anti-parallel AA7 1 2 ? anti-parallel AA8 1 2 ? anti-parallel AA9 1 2 ? anti-parallel AB1 1 2 ? parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id AA1 1 VAL A 8 ? THR A 9 ? VAL A 9 THR A 10 AA1 2 SER A 15 ? THR A 16 ? SER A 16 THR A 17 AA2 1 LEU A 136 ? THR A 137 ? LEU A 137 THR A 138 AA2 2 THR A 289 ? ASP A 290 ? THR A 290 ASP A 291 AA3 1 SER A 186 ? GLN A 187 ? SER A 187 GLN A 188 AA3 2 SER A 197 ? PRO A 198 ? SER A 198 PRO A 199 AA4 1 GLU A 230 ? GLU A 231 ? GLU A 231 GLU A 232 AA4 2 ARG A 240 ? MET A 241 ? ARG A 241 MET A 242 AA5 1 VAL A 306 ? ILE A 307 ? VAL A 307 ILE A 308 AA5 2 ALA A 329 ? THR A 330 ? ALA A 330 THR A 331 AA6 1 VAL B 8 ? THR B 9 ? VAL B 9 THR B 10 AA6 2 SER B 15 ? THR B 16 ? SER B 16 THR B 17 AA7 1 LEU B 136 ? THR B 137 ? LEU B 137 THR B 138 AA7 2 THR B 289 ? ASP B 290 ? THR B 290 ASP B 291 AA8 1 SER B 186 ? GLN B 187 ? SER B 187 GLN B 188 AA8 2 SER B 197 ? PRO B 198 ? SER B 198 PRO B 199 AA9 1 GLU B 230 ? GLU B 231 ? GLU B 231 GLU B 232 AA9 2 ARG B 240 ? MET B 241 ? ARG B 241 MET B 242 AB1 1 VAL B 306 ? ILE B 307 ? VAL B 307 ILE B 308 AB1 2 ALA B 329 ? THR B 330 ? ALA B 330 THR B 331 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id AA1 1 2 N VAL A 8 ? N VAL A 9 O THR A 16 ? O THR A 17 AA2 1 2 N THR A 137 ? N THR A 138 O THR A 289 ? O THR A 290 AA3 1 2 N GLN A 187 ? N GLN A 188 O SER A 197 ? O SER A 198 AA4 1 2 N GLU A 231 ? N GLU A 232 O ARG A 240 ? O ARG A 241 AA5 1 2 N ILE A 307 ? N ILE A 308 O ALA A 329 ? O ALA A 330 AA6 1 2 N VAL B 8 ? N VAL B 9 O THR B 16 ? O THR B 17 AA7 1 2 N THR B 137 ? N THR B 138 O THR B 289 ? O THR B 290 AA8 1 2 N GLN B 187 ? N GLN B 188 O SER B 197 ? O SER B 198 AA9 1 2 N GLU B 231 ? N GLU B 232 O ARG B 240 ? O ARG B 241 AB1 1 2 N ILE B 307 ? N ILE B 308 O ALA B 329 ? O ALA B 330 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CA A1345' AC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA A1346' AC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE MG A1351' AC4 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CA B1345' AC5 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA B1346' AC6 Software ? ? ? ? 23 'BINDING SITE FOR RESIDUE HEM A1344' AC7 Software ? ? ? ? 25 'BINDING SITE FOR RESIDUE HEM B1344' AC8 Software ? ? ? ? 8 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 142 RESIDUES 1347 TO 1348' AC9 Software ? ? ? ? 5 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO SER A 338 RESIDUES 1349 TO 1349' BC1 Software ? ? ? ? 9 'BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B 142 RESIDUES 1347 TO 1348' BC2 Software ? ? ? ? 5 'BINDING SITE FOR CHAIN B OF SUGAR BOUND TO SER B 338 RESIDUES 1349 TO 1349' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 6 ASP A 55 ? ASP A 56 . ? 1_555 ? 2 AC1 6 GLY A 73 ? GLY A 74 . ? 1_555 ? 3 AC1 6 ASP A 75 ? ASP A 76 . ? 1_555 ? 4 AC1 6 SER A 77 ? SER A 78 . ? 1_555 ? 5 AC1 6 HOH P . ? HOH A 593 . ? 1_555 ? 6 AC1 6 HOH P . ? HOH A 563 . ? 1_555 ? 7 AC2 5 SER A 183 ? SER A 184 . ? 1_555 ? 8 AC2 5 ASP A 200 ? ASP A 201 . ? 1_555 ? 9 AC2 5 THR A 202 ? THR A 203 . ? 1_555 ? 10 AC2 5 VAL A 205 ? VAL A 206 . ? 1_555 ? 11 AC2 5 ASP A 207 ? ASP A 208 . ? 1_555 ? 12 AC3 5 HOH P . ? HOH A 552 . ? 1_555 ? 13 AC3 5 HOH P . ? HOH A 610 . ? 1_555 ? 14 AC3 5 HOH Q . ? HOH B 689 . ? 1_555 ? 15 AC3 5 HOH Q . ? HOH B 595 . ? 1_555 ? 16 AC3 5 HOH Q . ? HOH B 540 . ? 1_555 ? 17 AC4 6 ASP B 55 ? ASP B 56 . ? 1_555 ? 18 AC4 6 GLY B 73 ? GLY B 74 . ? 1_555 ? 19 AC4 6 ASP B 75 ? ASP B 76 . ? 1_555 ? 20 AC4 6 SER B 77 ? SER B 78 . ? 1_555 ? 21 AC4 6 HOH Q . ? HOH B 554 . ? 1_555 ? 22 AC4 6 HOH Q . ? HOH B 587 . ? 1_555 ? 23 AC5 5 SER B 183 ? SER B 184 . ? 1_555 ? 24 AC5 5 ASP B 200 ? ASP B 201 . ? 1_555 ? 25 AC5 5 THR B 202 ? THR B 203 . ? 1_555 ? 26 AC5 5 VAL B 205 ? VAL B 206 . ? 1_555 ? 27 AC5 5 ASP B 207 ? ASP B 208 . ? 1_555 ? 28 AC6 23 ARG A 46 ? ARG A 47 . ? 1_555 ? 29 AC6 23 LEU A 49 ? LEU A 50 . ? 1_555 ? 30 AC6 23 ARG A 50 ? ARG A 51 . ? 1_555 ? 31 AC6 23 PHE A 53 ? PHE A 54 . ? 1_555 ? 32 AC6 23 PRO A 152 ? PRO A 153 . ? 1_555 ? 33 AC6 23 GLY A 153 ? GLY A 154 . ? 1_555 ? 34 AC6 23 PRO A 154 ? PRO A 155 . ? 1_555 ? 35 AC6 23 LEU A 178 ? LEU A 179 . ? 1_555 ? 36 AC6 23 LEU A 179 ? LEU A 180 . ? 1_555 ? 37 AC6 23 ALA A 181 ? ALA A 182 . ? 1_555 ? 38 AC6 23 HSO A 182 ? HSO A 183 . ? 1_555 ? 39 AC6 23 LEU A 184 ? LEU A 185 . ? 1_555 ? 40 AC6 23 ALA A 185 ? ALA A 186 . ? 1_555 ? 41 AC6 23 SER A 186 ? SER A 187 . ? 1_555 ? 42 AC6 23 GLU A 188 ? GLU A 189 . ? 1_555 ? 43 AC6 23 GLY A 189 ? GLY A 190 . ? 1_555 ? 44 AC6 23 LEU A 190 ? LEU A 191 . ? 1_555 ? 45 AC6 23 MET A 241 ? MET A 242 . ? 1_555 ? 46 AC6 23 HOH P . ? HOH A 543 . ? 1_555 ? 47 AC6 23 HOH P . ? HOH A 572 . ? 1_555 ? 48 AC6 23 HOH P . ? HOH A 520 . ? 1_555 ? 49 AC6 23 HOH P . ? HOH A 629 . ? 1_555 ? 50 AC6 23 HOH P . ? HOH A 649 . ? 1_555 ? 51 AC7 25 ARG B 46 ? ARG B 47 . ? 1_555 ? 52 AC7 25 LEU B 49 ? LEU B 50 . ? 1_555 ? 53 AC7 25 ARG B 50 ? ARG B 51 . ? 1_555 ? 54 AC7 25 PHE B 53 ? PHE B 54 . ? 1_555 ? 55 AC7 25 PRO B 152 ? PRO B 153 . ? 1_555 ? 56 AC7 25 GLY B 153 ? GLY B 154 . ? 1_555 ? 57 AC7 25 PRO B 154 ? PRO B 155 . ? 1_555 ? 58 AC7 25 LEU B 178 ? LEU B 179 . ? 1_555 ? 59 AC7 25 LEU B 179 ? LEU B 180 . ? 1_555 ? 60 AC7 25 ALA B 181 ? ALA B 182 . ? 1_555 ? 61 AC7 25 HSO B 182 ? HSO B 183 . ? 1_555 ? 62 AC7 25 LEU B 184 ? LEU B 185 . ? 1_555 ? 63 AC7 25 ALA B 185 ? ALA B 186 . ? 1_555 ? 64 AC7 25 SER B 186 ? SER B 187 . ? 1_555 ? 65 AC7 25 GLN B 187 ? GLN B 188 . ? 1_555 ? 66 AC7 25 GLU B 188 ? GLU B 189 . ? 1_555 ? 67 AC7 25 GLY B 189 ? GLY B 190 . ? 1_555 ? 68 AC7 25 LEU B 190 ? LEU B 191 . ? 1_555 ? 69 AC7 25 MET B 241 ? MET B 242 . ? 1_555 ? 70 AC7 25 SER B 243 ? SER B 244 . ? 1_555 ? 71 AC7 25 HOH Q . ? HOH B 561 . ? 1_555 ? 72 AC7 25 HOH Q . ? HOH B 661 . ? 1_555 ? 73 AC7 25 HOH Q . ? HOH B 509 . ? 1_555 ? 74 AC7 25 HOH Q . ? HOH B 629 . ? 1_555 ? 75 AC7 25 HOH Q . ? HOH B 526 . ? 1_555 ? 76 AC8 8 ALA A 80 ? ALA A 81 . ? 1_555 ? 77 AC8 8 ARG A 102 ? ARG A 103 . ? 1_555 ? 78 AC8 8 GLY A 109 ? GLY A 110 . ? 1_555 ? 79 AC8 8 PHE A 112 ? PHE A 113 . ? 1_555 ? 80 AC8 8 ASN A 141 ? ASN A 142 . ? 1_555 ? 81 AC8 8 HOH P . ? HOH A 513 . ? 1_555 ? 82 AC8 8 HOH P . ? HOH A 663 . ? 1_555 ? 83 AC8 8 HOH P . ? HOH A 624 . ? 1_555 ? 84 AC9 5 GLY A 237 ? GLY A 238 . ? 1_555 ? 85 AC9 5 SER A 337 ? SER A 338 . ? 1_555 ? 86 AC9 5 LEU A 338 ? LEU A 339 . ? 1_555 ? 87 AC9 5 ALA A 339 ? ALA A 340 . ? 1_555 ? 88 AC9 5 HOH P . ? HOH A 518 . ? 1_555 ? 89 BC1 9 ALA B 80 ? ALA B 81 . ? 1_555 ? 90 BC1 9 ARG B 102 ? ARG B 103 . ? 1_555 ? 91 BC1 9 GLY B 109 ? GLY B 110 . ? 1_555 ? 92 BC1 9 VAL B 110 ? VAL B 111 . ? 1_555 ? 93 BC1 9 PHE B 112 ? PHE B 113 . ? 1_555 ? 94 BC1 9 ASN B 141 ? ASN B 142 . ? 1_555 ? 95 BC1 9 HOH Q . ? HOH B 532 . ? 1_555 ? 96 BC1 9 HOH Q . ? HOH B 584 . ? 1_555 ? 97 BC1 9 HOH Q . ? HOH B 618 . ? 1_555 ? 98 BC2 5 GLY B 237 ? GLY B 238 . ? 1_555 ? 99 BC2 5 SER B 337 ? SER B 338 . ? 1_555 ? 100 BC2 5 LEU B 338 ? LEU B 339 . ? 1_555 ? 101 BC2 5 HOH Q . ? HOH B 592 . ? 1_555 ? 102 BC2 5 HOH Q . ? HOH B 523 . ? 1_555 ? # _database_PDB_matrix.entry_id 1H3J _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 1H3J _atom_sites.fract_transf_matrix[1][1] 0.007863 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.013240 _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] 0.013055 _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 CA FE MG 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 . SER A 1 7 ? 80.079 23.729 51.291 1.00 41.88 ? 8 SER A N 1 ATOM 2 C CA . SER A 1 7 ? 79.751 23.172 52.629 1.00 42.93 ? 8 SER A CA 1 ATOM 3 C C . SER A 1 7 ? 80.154 24.130 53.754 1.00 40.56 ? 8 SER A C 1 ATOM 4 O O . SER A 1 7 ? 80.927 25.069 53.538 1.00 42.84 ? 8 SER A O 1 ATOM 5 C CB . SER A 1 7 ? 80.445 21.819 52.833 1.00 44.03 ? 8 SER A CB 1 ATOM 6 O OG . SER A 1 7 ? 80.113 21.261 54.101 1.00 47.04 ? 8 SER A OG 1 ATOM 7 N N . VAL A 1 8 ? 79.626 23.880 54.946 1.00 36.21 ? 9 VAL A N 1 ATOM 8 C CA . VAL A 1 8 ? 79.918 24.680 56.107 1.00 31.70 ? 9 VAL A CA 1 ATOM 9 C C . VAL A 1 8 ? 79.679 23.836 57.341 1.00 30.22 ? 9 VAL A C 1 ATOM 10 O O . VAL A 1 8 ? 78.831 22.956 57.345 1.00 32.28 ? 9 VAL A O 1 ATOM 11 C CB . VAL A 1 8 ? 79.063 25.989 56.129 1.00 31.75 ? 9 VAL A CB 1 ATOM 12 C CG1 . VAL A 1 8 ? 78.022 25.955 55.051 1.00 32.39 ? 9 VAL A CG1 1 ATOM 13 C CG2 . VAL A 1 8 ? 78.402 26.204 57.477 1.00 29.98 ? 9 VAL A CG2 1 ATOM 14 N N . THR A 1 9 ? 80.447 24.086 58.381 1.00 27.63 ? 10 THR A N 1 ATOM 15 C CA . THR A 1 9 ? 80.309 23.368 59.627 1.00 27.73 ? 10 THR A CA 1 ATOM 16 C C . THR A 1 9 ? 79.718 24.340 60.642 1.00 28.62 ? 10 THR A C 1 ATOM 17 O O . THR A 1 9 ? 80.347 25.325 61.023 1.00 29.43 ? 10 THR A O 1 ATOM 18 C CB . THR A 1 9 ? 81.693 22.881 60.118 1.00 28.59 ? 10 THR A CB 1 ATOM 19 O OG1 . THR A 1 9 ? 82.415 22.301 59.018 1.00 29.79 ? 10 THR A OG1 1 ATOM 20 C CG2 . THR A 1 9 ? 81.540 21.885 61.251 1.00 27.94 ? 10 THR A CG2 1 ATOM 21 N N . CYS A 1 10 ? 78.507 24.058 61.089 1.00 27.97 ? 11 CYS A N 1 ATOM 22 C CA . CYS A 1 10 ? 77.836 24.917 62.028 1.00 27.20 ? 11 CYS A CA 1 ATOM 23 C C . CYS A 1 10 ? 78.522 24.927 63.354 1.00 29.17 ? 11 CYS A C 1 ATOM 24 O O . CYS A 1 10 ? 79.286 24.028 63.680 1.00 30.52 ? 11 CYS A O 1 ATOM 25 C CB . CYS A 1 10 ? 76.363 24.515 62.156 1.00 25.16 ? 11 CYS A CB 1 ATOM 26 S SG . CYS A 1 10 ? 75.584 24.509 60.514 1.00 25.22 ? 11 CYS A SG 1 ATOM 27 N N . PRO A 1 11 ? 78.249 25.957 64.148 1.00 31.09 ? 12 PRO A N 1 ATOM 28 C CA . PRO A 1 11 ? 78.786 26.201 65.483 1.00 33.18 ? 12 PRO A CA 1 ATOM 29 C C . PRO A 1 11 ? 78.725 25.016 66.445 1.00 36.78 ? 12 PRO A C 1 ATOM 30 O O . PRO A 1 11 ? 79.386 25.024 67.485 1.00 39.77 ? 12 PRO A O 1 ATOM 31 C CB . PRO A 1 11 ? 77.919 27.340 65.976 1.00 33.72 ? 12 PRO A CB 1 ATOM 32 C CG . PRO A 1 11 ? 77.669 28.123 64.719 1.00 33.59 ? 12 PRO A CG 1 ATOM 33 C CD . PRO A 1 11 ? 77.357 27.051 63.729 1.00 30.72 ? 12 PRO A CD 1 ATOM 34 N N . GLY A 1 12 ? 77.899 24.021 66.146 1.00 37.94 ? 13 GLY A N 1 ATOM 35 C CA . GLY A 1 12 ? 77.800 22.866 67.028 1.00 37.93 ? 13 GLY A CA 1 ATOM 36 C C . GLY A 1 12 ? 78.385 21.600 66.422 1.00 37.68 ? 13 GLY A C 1 ATOM 37 O O . GLY A 1 12 ? 78.096 20.496 66.891 1.00 39.13 ? 13 GLY A O 1 ATOM 38 N N . GLY A 1 13 ? 79.158 21.748 65.348 1.00 36.84 ? 14 GLY A N 1 ATOM 39 C CA . GLY A 1 13 ? 79.779 20.600 64.710 1.00 34.68 ? 14 GLY A CA 1 ATOM 40 C C . GLY A 1 13 ? 79.020 20.036 63.535 1.00 33.62 ? 14 GLY A C 1 ATOM 41 O O . GLY A 1 13 ? 79.608 19.385 62.657 1.00 32.18 ? 14 GLY A O 1 ATOM 42 N N . GLN A 1 14 ? 77.724 20.330 63.480 1.00 32.69 ? 15 GLN A N 1 ATOM 43 C CA . GLN A 1 14 ? 76.892 19.822 62.406 1.00 31.36 ? 15 GLN A CA 1 ATOM 44 C C . GLN A 1 14 ? 77.364 20.366 61.090 1.00 30.45 ? 15 GLN A C 1 ATOM 45 O O . GLN A 1 14 ? 77.570 21.555 60.943 1.00 31.33 ? 15 GLN A O 1 ATOM 46 C CB . GLN A 1 14 ? 75.424 20.177 62.626 1.00 31.72 ? 15 GLN A CB 1 ATOM 47 C CG . GLN A 1 14 ? 74.872 19.795 63.992 1.00 32.44 ? 15 GLN A CG 1 ATOM 48 C CD . GLN A 1 14 ? 74.780 20.986 64.939 1.00 35.84 ? 15 GLN A CD 1 ATOM 49 O OE1 . GLN A 1 14 ? 75.254 22.085 64.627 1.00 37.36 ? 15 GLN A OE1 1 ATOM 50 N NE2 . GLN A 1 14 ? 74.161 20.779 66.098 1.00 36.80 ? 15 GLN A NE2 1 ATOM 51 N N . SER A 1 15 ? 77.603 19.476 60.148 1.00 29.86 ? 16 SER A N 1 ATOM 52 C CA . SER A 1 15 ? 78.038 19.862 58.829 1.00 29.39 ? 16 SER A CA 1 ATOM 53 C C . SER A 1 15 ? 76.799 20.039 57.937 1.00 30.11 ? 16 SER A C 1 ATOM 54 O O . SER A 1 15 ? 75.814 19.288 58.051 1.00 30.17 ? 16 SER A O 1 ATOM 55 C CB . SER A 1 15 ? 78.959 18.789 58.275 1.00 29.62 ? 16 SER A CB 1 ATOM 56 O OG . SER A 1 15 ? 79.436 19.155 56.992 1.00 35.54 ? 16 SER A OG 1 ATOM 57 N N . THR A 1 16 ? 76.847 21.010 57.031 1.00 29.06 ? 17 THR A N 1 ATOM 58 C CA . THR A 1 16 ? 75.714 21.271 56.172 1.00 27.42 ? 17 THR A CA 1 ATOM 59 C C . THR A 1 16 ? 76.132 21.979 54.900 1.00 26.92 ? 17 THR A C 1 ATOM 60 O O . THR A 1 16 ? 77.262 22.416 54.757 1.00 28.52 ? 17 THR A O 1 ATOM 61 C CB . THR A 1 16 ? 74.600 22.048 56.928 1.00 26.98 ? 17 THR A CB 1 ATOM 62 O OG1 . THR A 1 16 ? 73.522 22.306 56.026 1.00 27.56 ? 17 THR A OG1 1 ATOM 63 C CG2 . THR A 1 16 ? 75.126 23.378 57.491 1.00 26.79 ? 17 THR A CG2 1 ATOM 64 N N . SER A 1 17 ? 75.207 22.096 53.972 1.00 27.54 ? 18 SER A N 1 ATOM 65 C CA . SER A 1 17 ? 75.482 22.686 52.682 1.00 27.53 ? 18 SER A CA 1 ATOM 66 C C . SER A 1 17 ? 75.412 24.213 52.562 1.00 28.07 ? 18 SER A C 1 ATOM 67 O O . SER A 1 17 ? 75.930 24.765 51.590 1.00 29.81 ? 18 SER A O 1 ATOM 68 C CB . SER A 1 17 ? 74.542 22.053 51.665 1.00 29.59 ? 18 SER A CB 1 ATOM 69 O OG . SER A 1 17 ? 73.193 22.095 52.138 1.00 32.77 ? 18 SER A OG 1 ATOM 70 N N . ASN A 1 18 ? 74.782 24.906 53.512 1.00 27.05 ? 19 ASN A N 1 ATOM 71 C CA . ASN A 1 18 ? 74.685 26.369 53.406 1.00 24.28 ? 19 ASN A CA 1 ATOM 72 C C . ASN A 1 18 ? 74.607 26.907 54.807 1.00 22.88 ? 19 ASN A C 1 ATOM 73 O O . ASN A 1 18 ? 73.969 26.287 55.668 1.00 24.01 ? 19 ASN A O 1 ATOM 74 C CB . ASN A 1 18 ? 73.426 26.751 52.613 1.00 26.87 ? 19 ASN A CB 1 ATOM 75 C CG . ASN A 1 18 ? 73.370 28.227 52.266 1.00 28.80 ? 19 ASN A CG 1 ATOM 76 O OD1 . ASN A 1 18 ? 73.204 29.084 53.139 1.00 27.28 ? 19 ASN A OD1 1 ATOM 77 N ND2 . ASN A 1 18 ? 73.484 28.530 50.985 1.00 30.28 ? 19 ASN A ND2 1 ATOM 78 N N . SER A 1 19 ? 75.237 28.053 55.065 1.00 20.14 ? 20 SER A N 1 ATOM 79 C CA . SER A 1 19 ? 75.214 28.609 56.411 1.00 18.46 ? 20 SER A CA 1 ATOM 80 C C . SER A 1 19 ? 73.798 28.996 56.826 1.00 16.35 ? 20 SER A C 1 ATOM 81 O O . SER A 1 19 ? 73.540 29.198 57.996 1.00 17.34 ? 20 SER A O 1 ATOM 82 C CB . SER A 1 19 ? 76.122 29.813 56.504 1.00 20.35 ? 20 SER A CB 1 ATOM 83 O OG . SER A 1 19 ? 75.594 30.867 55.728 1.00 21.37 ? 20 SER A OG 1 ATOM 84 N N . GLN A 1 20 ? 72.880 29.136 55.877 1.00 18.04 ? 21 GLN A N 1 ATOM 85 C CA . GLN A 1 20 ? 71.482 29.462 56.215 1.00 20.56 ? 21 GLN A CA 1 ATOM 86 C C . GLN A 1 20 ? 70.802 28.334 56.993 1.00 21.87 ? 21 GLN A C 1 ATOM 87 O O . GLN A 1 20 ? 69.894 28.571 57.792 1.00 20.98 ? 21 GLN A O 1 ATOM 88 C CB . GLN A 1 20 ? 70.673 29.720 54.963 1.00 22.19 ? 21 GLN A CB 1 ATOM 89 C CG . GLN A 1 20 ? 71.025 30.997 54.248 1.00 26.21 ? 21 GLN A CG 1 ATOM 90 C CD . GLN A 1 20 ? 70.035 31.299 53.149 1.00 32.61 ? 21 GLN A CD 1 ATOM 91 O OE1 . GLN A 1 20 ? 70.406 31.428 51.976 1.00 36.20 ? 21 GLN A OE1 1 ATOM 92 N NE2 . GLN A 1 20 ? 68.755 31.379 53.507 1.00 34.28 ? 21 GLN A NE2 1 ATOM 93 N N . CYS A 1 21 ? 71.291 27.108 56.794 1.00 22.25 ? 22 CYS A N 1 ATOM 94 C CA . CYS A 1 21 ? 70.737 25.929 57.451 1.00 19.97 ? 22 CYS A CA 1 ATOM 95 C C . CYS A 1 21 ? 71.141 25.795 58.886 1.00 19.70 ? 22 CYS A C 1 ATOM 96 O O . CYS A 1 21 ? 70.460 25.120 59.653 1.00 22.59 ? 22 CYS A O 1 ATOM 97 C CB . CYS A 1 21 ? 71.157 24.661 56.722 1.00 17.41 ? 22 CYS A CB 1 ATOM 98 S SG . CYS A 1 21 ? 70.866 24.677 54.932 1.00 20.58 ? 22 CYS A SG 1 ATOM 99 N N . CYS A 1 22 ? 72.171 26.517 59.306 1.00 18.43 ? 23 CYS A N 1 ATOM 100 C CA . CYS A 1 22 ? 72.629 26.340 60.676 1.00 17.23 ? 23 CYS A CA 1 ATOM 101 C C . CYS A 1 22 ? 71.650 26.635 61.766 1.00 17.42 ? 23 CYS A C 1 ATOM 102 O O . CYS A 1 22 ? 71.622 25.919 62.779 1.00 18.01 ? 23 CYS A O 1 ATOM 103 C CB . CYS A 1 22 ? 73.953 27.084 60.948 1.00 21.01 ? 23 CYS A CB 1 ATOM 104 S SG . CYS A 1 22 ? 75.390 26.476 59.991 1.00 22.19 ? 23 CYS A SG 1 ATOM 105 N N . VAL A 1 23 ? 70.826 27.669 61.591 1.00 15.97 ? 24 VAL A N 1 ATOM 106 C CA . VAL A 1 23 ? 69.887 28.018 62.670 1.00 15.30 ? 24 VAL A CA 1 ATOM 107 C C . VAL A 1 23 ? 68.876 26.908 62.895 1.00 14.19 ? 24 VAL A C 1 ATOM 108 O O . VAL A 1 23 ? 68.463 26.630 64.017 1.00 13.69 ? 24 VAL A O 1 ATOM 109 C CB . VAL A 1 23 ? 69.160 29.378 62.398 1.00 14.76 ? 24 VAL A CB 1 ATOM 110 C CG1 . VAL A 1 23 ? 68.380 29.324 61.125 1.00 11.14 ? 24 VAL A CG1 1 ATOM 111 C CG2 . VAL A 1 23 ? 68.299 29.764 63.573 1.00 16.00 ? 24 VAL A CG2 1 ATOM 112 N N . TRP A 1 24 ? 68.631 26.172 61.831 1.00 14.65 ? 25 TRP A N 1 ATOM 113 C CA . TRP A 1 24 ? 67.657 25.103 61.846 1.00 15.81 ? 25 TRP A CA 1 ATOM 114 C C . TRP A 1 24 ? 68.030 23.922 62.732 1.00 18.53 ? 25 TRP A C 1 ATOM 115 O O . TRP A 1 24 ? 67.162 23.178 63.195 1.00 19.01 ? 25 TRP A O 1 ATOM 116 C CB . TRP A 1 24 ? 67.330 24.720 60.411 1.00 14.51 ? 25 TRP A CB 1 ATOM 117 C CG . TRP A 1 24 ? 66.660 25.867 59.664 1.00 16.60 ? 25 TRP A CG 1 ATOM 118 C CD1 . TRP A 1 24 ? 67.179 26.599 58.638 1.00 15.12 ? 25 TRP A CD1 1 ATOM 119 C CD2 . TRP A 1 24 ? 65.356 26.411 59.921 1.00 17.34 ? 25 TRP A CD2 1 ATOM 120 N NE1 . TRP A 1 24 ? 66.286 27.570 58.245 1.00 16.25 ? 25 TRP A NE1 1 ATOM 121 C CE2 . TRP A 1 24 ? 65.164 27.477 59.016 1.00 17.81 ? 25 TRP A CE2 1 ATOM 122 C CE3 . TRP A 1 24 ? 64.331 26.097 60.822 1.00 18.72 ? 25 TRP A CE3 1 ATOM 123 C CZ2 . TRP A 1 24 ? 63.977 28.236 58.991 1.00 19.13 ? 25 TRP A CZ2 1 ATOM 124 C CZ3 . TRP A 1 24 ? 63.145 26.857 60.794 1.00 18.61 ? 25 TRP A CZ3 1 ATOM 125 C CH2 . TRP A 1 24 ? 62.990 27.912 59.885 1.00 19.24 ? 25 TRP A CH2 1 ATOM 126 N N . PHE A 1 25 ? 69.304 23.802 63.070 1.00 19.69 ? 26 PHE A N 1 ATOM 127 C CA . PHE A 1 25 ? 69.713 22.732 63.957 1.00 19.96 ? 26 PHE A CA 1 ATOM 128 C C . PHE A 1 25 ? 69.284 23.069 65.356 1.00 19.94 ? 26 PHE A C 1 ATOM 129 O O . PHE A 1 25 ? 69.001 22.187 66.148 1.00 21.34 ? 26 PHE A O 1 ATOM 130 C CB . PHE A 1 25 ? 71.222 22.511 63.891 1.00 20.37 ? 26 PHE A CB 1 ATOM 131 C CG . PHE A 1 25 ? 71.656 21.836 62.645 1.00 23.46 ? 26 PHE A CG 1 ATOM 132 C CD1 . PHE A 1 25 ? 72.355 22.537 61.665 1.00 24.10 ? 26 PHE A CD1 1 ATOM 133 C CD2 . PHE A 1 25 ? 71.342 20.489 62.425 1.00 24.28 ? 26 PHE A CD2 1 ATOM 134 C CE1 . PHE A 1 25 ? 72.741 21.908 60.471 1.00 24.44 ? 26 PHE A CE1 1 ATOM 135 C CE2 . PHE A 1 25 ? 71.725 19.849 61.235 1.00 22.59 ? 26 PHE A CE2 1 ATOM 136 C CZ . PHE A 1 25 ? 72.423 20.559 60.260 1.00 23.49 ? 26 PHE A CZ 1 ATOM 137 N N . ASP A 1 26 ? 69.206 24.352 65.679 1.00 21.05 ? 27 ASP A N 1 ATOM 138 C CA . ASP A 1 26 ? 68.774 24.729 67.018 1.00 20.79 ? 27 ASP A CA 1 ATOM 139 C C . ASP A 1 26 ? 67.261 24.616 67.080 1.00 19.09 ? 27 ASP A C 1 ATOM 140 O O . ASP A 1 26 ? 66.701 24.233 68.105 1.00 19.71 ? 27 ASP A O 1 ATOM 141 C CB . ASP A 1 26 ? 69.195 26.156 67.343 1.00 26.49 ? 27 ASP A CB 1 ATOM 142 C CG . ASP A 1 26 ? 70.714 26.351 67.291 1.00 31.25 ? 27 ASP A CG 1 ATOM 143 O OD1 . ASP A 1 26 ? 71.471 25.389 67.600 1.00 35.21 ? 27 ASP A OD1 1 ATOM 144 O OD2 . ASP A 1 26 ? 71.141 27.463 66.921 1.00 32.16 ? 27 ASP A OD2 1 ATOM 145 N N . VAL A 1 27 ? 66.603 25.017 65.997 1.00 18.57 ? 28 VAL A N 1 ATOM 146 C CA . VAL A 1 27 ? 65.153 24.937 65.932 1.00 17.75 ? 28 VAL A CA 1 ATOM 147 C C . VAL A 1 27 ? 64.756 23.456 66.089 1.00 15.70 ? 28 VAL A C 1 ATOM 148 O O . VAL A 1 27 ? 63.891 23.127 66.894 1.00 16.87 ? 28 VAL A O 1 ATOM 149 C CB . VAL A 1 27 ? 64.623 25.556 64.608 1.00 18.09 ? 28 VAL A CB 1 ATOM 150 C CG1 . VAL A 1 27 ? 63.094 25.461 64.528 1.00 17.20 ? 28 VAL A CG1 1 ATOM 151 C CG2 . VAL A 1 27 ? 65.040 27.034 64.527 1.00 17.89 ? 28 VAL A CG2 1 ATOM 152 N N . LEU A 1 28 ? 65.470 22.564 65.419 1.00 16.33 ? 29 LEU A N 1 ATOM 153 C CA . LEU A 1 28 ? 65.179 21.133 65.524 1.00 20.31 ? 29 LEU A CA 1 ATOM 154 C C . LEU A 1 28 ? 65.255 20.659 66.965 1.00 21.91 ? 29 LEU A C 1 ATOM 155 O O . LEU A 1 28 ? 64.330 20.026 67.460 1.00 21.68 ? 29 LEU A O 1 ATOM 156 C CB . LEU A 1 28 ? 66.141 20.325 64.650 1.00 22.88 ? 29 LEU A CB 1 ATOM 157 C CG . LEU A 1 28 ? 66.226 18.795 64.724 1.00 25.00 ? 29 LEU A CG 1 ATOM 158 C CD1 . LEU A 1 28 ? 64.921 18.142 64.295 1.00 24.94 ? 29 LEU A CD1 1 ATOM 159 C CD2 . LEU A 1 28 ? 67.355 18.326 63.807 1.00 24.68 ? 29 LEU A CD2 1 ATOM 160 N N . ASP A 1 29 ? 66.349 20.989 67.650 1.00 24.18 ? 30 ASP A N 1 ATOM 161 C CA . ASP A 1 29 ? 66.535 20.585 69.043 1.00 25.59 ? 30 ASP A CA 1 ATOM 162 C C . ASP A 1 29 ? 65.440 21.147 69.945 1.00 24.47 ? 30 ASP A C 1 ATOM 163 O O . ASP A 1 29 ? 65.007 20.490 70.893 1.00 23.75 ? 30 ASP A O 1 ATOM 164 C CB . ASP A 1 29 ? 67.924 21.001 69.549 1.00 31.72 ? 30 ASP A CB 1 ATOM 165 C CG . ASP A 1 29 ? 68.060 20.891 71.081 1.00 38.27 ? 30 ASP A CG 1 ATOM 166 O OD1 . ASP A 1 29 ? 68.036 21.944 71.782 1.00 42.20 ? 30 ASP A OD1 1 ATOM 167 O OD2 . ASP A 1 29 ? 68.184 19.747 71.585 1.00 41.40 ? 30 ASP A OD2 1 ATOM 168 N N . ASP A 1 30 ? 65.008 22.370 69.674 1.00 22.66 ? 31 ASP A N 1 ATOM 169 C CA . ASP A 1 30 ? 63.945 22.973 70.464 1.00 21.75 ? 31 ASP A CA 1 ATOM 170 C C . ASP A 1 30 ? 62.610 22.245 70.199 1.00 19.37 ? 31 ASP A C 1 ATOM 171 O O . ASP A 1 30 ? 61.935 21.803 71.129 1.00 18.58 ? 31 ASP A O 1 ATOM 172 C CB . ASP A 1 30 ? 63.821 24.451 70.095 1.00 23.56 ? 31 ASP A CB 1 ATOM 173 C CG . ASP A 1 30 ? 62.911 25.222 71.035 1.00 25.71 ? 31 ASP A CG 1 ATOM 174 O OD1 . ASP A 1 30 ? 62.031 24.632 71.706 1.00 27.71 ? 31 ASP A OD1 1 ATOM 175 O OD2 . ASP A 1 30 ? 63.082 26.450 71.098 1.00 28.45 ? 31 ASP A OD2 1 ATOM 176 N N . LEU A 1 31 ? 62.257 22.097 68.929 1.00 18.12 ? 32 LEU A N 1 ATOM 177 C CA . LEU A 1 31 ? 61.012 21.434 68.568 1.00 19.02 ? 32 LEU A CA 1 ATOM 178 C C . LEU A 1 31 ? 60.917 20.020 69.122 1.00 20.10 ? 32 LEU A C 1 ATOM 179 O O . LEU A 1 31 ? 59.960 19.674 69.795 1.00 19.36 ? 32 LEU A O 1 ATOM 180 C CB . LEU A 1 31 ? 60.850 21.411 67.061 1.00 17.23 ? 32 LEU A CB 1 ATOM 181 C CG . LEU A 1 31 ? 60.430 22.748 66.443 1.00 15.97 ? 32 LEU A CG 1 ATOM 182 C CD1 . LEU A 1 31 ? 60.311 22.579 64.925 1.00 12.79 ? 32 LEU A CD1 1 ATOM 183 C CD2 . LEU A 1 31 ? 59.086 23.215 67.075 1.00 16.78 ? 32 LEU A CD2 1 ATOM 184 N N . GLN A 1 32 ? 61.936 19.218 68.876 1.00 20.80 ? 33 GLN A N 1 ATOM 185 C CA . GLN A 1 32 ? 61.953 17.845 69.359 1.00 21.56 ? 33 GLN A CA 1 ATOM 186 C C . GLN A 1 32 ? 61.852 17.700 70.861 1.00 21.32 ? 33 GLN A C 1 ATOM 187 O O . GLN A 1 32 ? 61.176 16.784 71.340 1.00 19.91 ? 33 GLN A O 1 ATOM 188 C CB . GLN A 1 32 ? 63.193 17.114 68.842 1.00 20.55 ? 33 GLN A CB 1 ATOM 189 C CG . GLN A 1 32 ? 63.199 16.901 67.340 1.00 19.83 ? 33 GLN A CG 1 ATOM 190 C CD . GLN A 1 32 ? 62.121 15.927 66.852 1.00 20.19 ? 33 GLN A CD 1 ATOM 191 O OE1 . GLN A 1 32 ? 62.386 15.075 66.003 1.00 23.14 ? 33 GLN A OE1 1 ATOM 192 N NE2 . GLN A 1 32 ? 60.914 16.061 67.362 1.00 15.75 ? 33 GLN A NE2 1 ATOM 193 N N . THR A 1 33 ? 62.447 18.638 71.595 1.00 21.64 ? 34 THR A N 1 ATOM 194 C CA . THR A 1 33 ? 62.447 18.601 73.055 1.00 22.61 ? 34 THR A CA 1 ATOM 195 C C . THR A 1 33 ? 61.180 19.144 73.709 1.00 24.01 ? 34 THR A C 1 ATOM 196 O O . THR A 1 33 ? 60.625 18.550 74.640 1.00 25.05 ? 34 THR A O 1 ATOM 197 C CB . THR A 1 33 ? 63.658 19.415 73.635 1.00 22.93 ? 34 THR A CB 1 ATOM 198 O OG1 . THR A 1 33 ? 64.880 18.942 73.057 1.00 25.18 ? 34 THR A OG1 1 ATOM 199 C CG2 . THR A 1 33 ? 63.755 19.236 75.127 1.00 25.02 ? 34 THR A CG2 1 ATOM 200 N N . ASN A 1 34 ? 60.697 20.257 73.188 1.00 24.37 ? 35 ASN A N 1 ATOM 201 C CA . ASN A 1 34 ? 59.558 20.908 73.779 1.00 23.64 ? 35 ASN A CA 1 ATOM 202 C C . ASN A 1 34 ? 58.234 20.755 73.056 1.00 24.68 ? 35 ASN A C 1 ATOM 203 O O . ASN A 1 34 ? 57.321 20.130 73.591 1.00 26.95 ? 35 ASN A O 1 ATOM 204 C CB . ASN A 1 34 ? 59.929 22.364 74.014 1.00 24.73 ? 35 ASN A CB 1 ATOM 205 C CG . ASN A 1 34 ? 61.285 22.484 74.706 1.00 24.85 ? 35 ASN A CG 1 ATOM 206 O OD1 . ASN A 1 34 ? 61.443 22.013 75.835 1.00 28.02 ? 35 ASN A OD1 1 ATOM 207 N ND2 . ASN A 1 34 ? 62.291 22.975 73.989 1.00 22.43 ? 35 ASN A ND2 1 ATOM 208 N N . PHE A 1 35 ? 58.124 21.274 71.845 1.00 22.70 ? 36 PHE A N 1 ATOM 209 C CA . PHE A 1 35 ? 56.869 21.147 71.123 1.00 21.77 ? 36 PHE A CA 1 ATOM 210 C C . PHE A 1 35 ? 56.458 19.672 70.964 1.00 20.74 ? 36 PHE A C 1 ATOM 211 O O . PHE A 1 35 ? 55.303 19.320 71.200 1.00 18.47 ? 36 PHE A O 1 ATOM 212 C CB . PHE A 1 35 ? 56.987 21.820 69.753 1.00 21.09 ? 36 PHE A CB 1 ATOM 213 C CG . PHE A 1 35 ? 55.701 21.833 68.960 1.00 22.16 ? 36 PHE A CG 1 ATOM 214 C CD1 . PHE A 1 35 ? 55.615 21.164 67.742 1.00 20.61 ? 36 PHE A CD1 1 ATOM 215 C CD2 . PHE A 1 35 ? 54.599 22.565 69.397 1.00 22.92 ? 36 PHE A CD2 1 ATOM 216 C CE1 . PHE A 1 35 ? 54.462 21.226 66.969 1.00 22.37 ? 36 PHE A CE1 1 ATOM 217 C CE2 . PHE A 1 35 ? 53.442 22.625 68.621 1.00 24.11 ? 36 PHE A CE2 1 ATOM 218 C CZ . PHE A 1 35 ? 53.383 21.953 67.406 1.00 22.63 ? 36 PHE A CZ 1 ATOM 219 N N . TYR A 1 36 ? 57.407 18.813 70.593 1.00 19.79 ? 37 TYR A N 1 ATOM 220 C CA . TYR A 1 36 ? 57.134 17.381 70.387 1.00 19.62 ? 37 TYR A CA 1 ATOM 221 C C . TYR A 1 36 ? 57.388 16.487 71.600 1.00 19.84 ? 37 TYR A C 1 ATOM 222 O O . TYR A 1 36 ? 57.412 15.271 71.471 1.00 19.65 ? 37 TYR A O 1 ATOM 223 C CB . TYR A 1 36 ? 57.893 16.853 69.167 1.00 14.94 ? 37 TYR A CB 1 ATOM 224 C CG . TYR A 1 36 ? 57.393 17.439 67.876 1.00 14.74 ? 37 TYR A CG 1 ATOM 225 C CD1 . TYR A 1 36 ? 58.260 18.070 66.982 1.00 14.45 ? 37 TYR A CD1 1 ATOM 226 C CD2 . TYR A 1 36 ? 56.043 17.388 67.556 1.00 15.53 ? 37 TYR A CD2 1 ATOM 227 C CE1 . TYR A 1 36 ? 57.790 18.642 65.792 1.00 14.96 ? 37 TYR A CE1 1 ATOM 228 C CE2 . TYR A 1 36 ? 55.559 17.956 66.378 1.00 15.77 ? 37 TYR A CE2 1 ATOM 229 C CZ . TYR A 1 36 ? 56.431 18.580 65.504 1.00 15.98 ? 37 TYR A CZ 1 ATOM 230 O OH . TYR A 1 36 ? 55.915 19.150 64.371 1.00 18.05 ? 37 TYR A OH 1 ATOM 231 N N . GLN A 1 37 ? 57.578 17.106 72.760 1.00 21.32 ? 38 GLN A N 1 ATOM 232 C CA . GLN A 1 37 ? 57.797 16.421 74.032 1.00 25.60 ? 38 GLN A CA 1 ATOM 233 C C . GLN A 1 37 ? 58.724 15.233 73.996 1.00 24.85 ? 38 GLN A C 1 ATOM 234 O O . GLN A 1 37 ? 58.443 14.195 74.592 1.00 25.41 ? 38 GLN A O 1 ATOM 235 C CB . GLN A 1 37 ? 56.455 15.990 74.613 1.00 30.34 ? 38 GLN A CB 1 ATOM 236 C CG . GLN A 1 37 ? 55.526 17.143 74.877 1.00 38.20 ? 38 GLN A CG 1 ATOM 237 C CD . GLN A 1 37 ? 54.100 16.815 74.510 1.00 43.61 ? 38 GLN A CD 1 ATOM 238 O OE1 . GLN A 1 37 ? 53.828 15.815 73.826 1.00 48.04 ? 38 GLN A OE1 1 ATOM 239 N NE2 . GLN A 1 37 ? 53.174 17.664 74.940 1.00 45.09 ? 38 GLN A NE2 1 ATOM 240 N N . GLY A 1 38 ? 59.834 15.366 73.300 1.00 24.52 ? 39 GLY A N 1 ATOM 241 C CA . GLY A 1 38 ? 60.752 14.248 73.240 1.00 23.62 ? 39 GLY A CA 1 ATOM 242 C C . GLY A 1 38 ? 60.632 13.432 71.979 1.00 23.71 ? 39 GLY A C 1 ATOM 243 O O . GLY A 1 38 ? 60.661 12.215 72.023 1.00 24.93 ? 39 GLY A O 1 ATOM 244 N N . SER A 1 39 ? 60.456 14.111 70.854 1.00 22.71 ? 40 SER A N 1 ATOM 245 C CA . SER A 1 39 ? 60.364 13.468 69.555 1.00 23.44 ? 40 SER A CA 1 ATOM 246 C C . SER A 1 39 ? 59.215 12.478 69.390 1.00 21.98 ? 40 SER A C 1 ATOM 247 O O . SER A 1 39 ? 59.357 11.469 68.709 1.00 23.60 ? 40 SER A O 1 ATOM 248 C CB . SER A 1 39 ? 61.699 12.804 69.225 1.00 25.33 ? 40 SER A CB 1 ATOM 249 O OG . SER A 1 39 ? 62.773 13.682 69.552 1.00 28.16 ? 40 SER A OG 1 ATOM 250 N N . LYS A 1 40 ? 58.069 12.802 69.973 1.00 21.69 ? 41 LYS A N 1 ATOM 251 C CA . LYS A 1 40 ? 56.887 11.946 69.880 1.00 21.17 ? 41 LYS A CA 1 ATOM 252 C C . LYS A 1 40 ? 56.002 12.238 68.655 1.00 20.17 ? 41 LYS A C 1 ATOM 253 O O . LYS A 1 40 ? 56.036 13.340 68.078 1.00 18.27 ? 41 LYS A O 1 ATOM 254 C CB . LYS A 1 40 ? 56.043 12.086 71.145 1.00 21.08 ? 41 LYS A CB 1 ATOM 255 C CG . LYS A 1 40 ? 56.733 11.652 72.413 1.00 26.00 ? 41 LYS A CG 1 ATOM 256 C CD . LYS A 1 40 ? 55.705 11.446 73.505 1.00 29.21 ? 41 LYS A CD 1 ATOM 257 C CE . LYS A 1 40 ? 56.332 11.066 74.845 1.00 33.93 ? 41 LYS A CE 1 ATOM 258 N NZ . LYS A 1 40 ? 56.935 12.237 75.590 1.00 36.17 ? 41 LYS A NZ 1 ATOM 259 N N . CYS A 1 41 ? 55.163 11.264 68.311 1.00 19.38 ? 42 CYS A N 1 ATOM 260 C CA . CYS A 1 41 ? 54.223 11.376 67.195 1.00 18.87 ? 42 CYS A CA 1 ATOM 261 C C . CYS A 1 41 ? 52.798 11.359 67.771 1.00 20.35 ? 42 CYS A C 1 ATOM 262 O O . CYS A 1 41 ? 52.058 10.373 67.663 1.00 20.58 ? 42 CYS A O 1 ATOM 263 C CB . CYS A 1 41 ? 54.403 10.217 66.241 1.00 17.38 ? 42 CYS A CB 1 ATOM 264 S SG . CYS A 1 41 ? 53.221 10.272 64.875 1.00 18.66 ? 42 CYS A SG 1 ATOM 265 N N . GLU A 1 42 ? 52.439 12.454 68.422 1.00 19.25 ? 43 GLU A N 1 ATOM 266 C CA . GLU A 1 42 ? 51.141 12.577 69.053 1.00 19.29 ? 43 GLU A CA 1 ATOM 267 C C . GLU A 1 42 ? 50.372 13.790 68.544 1.00 18.27 ? 43 GLU A C 1 ATOM 268 O O . GLU A 1 42 ? 50.631 14.271 67.429 1.00 16.83 ? 43 GLU A O 1 ATOM 269 C CB . GLU A 1 42 ? 51.305 12.565 70.575 1.00 20.54 ? 43 GLU A CB 1 ATOM 270 C CG . GLU A 1 42 ? 51.747 11.179 71.087 1.00 22.53 ? 43 GLU A CG 1 ATOM 271 C CD . GLU A 1 42 ? 52.047 11.153 72.581 1.00 25.67 ? 43 GLU A CD 1 ATOM 272 O OE1 . GLU A 1 42 ? 51.879 12.189 73.246 1.00 27.66 ? 43 GLU A OE1 1 ATOM 273 O OE2 . GLU A 1 42 ? 52.466 10.101 73.100 1.00 27.87 ? 43 GLU A OE2 1 ATOM 274 N N . SER A 1 43 ? 49.450 14.314 69.341 1.00 16.49 ? 44 SER A N 1 ATOM 275 C CA . SER A 1 43 ? 48.638 15.430 68.866 1.00 16.85 ? 44 SER A CA 1 ATOM 276 C C . SER A 1 43 ? 49.392 16.588 68.192 1.00 16.02 ? 44 SER A C 1 ATOM 277 O O . SER A 1 43 ? 49.017 16.998 67.094 1.00 14.16 ? 44 SER A O 1 ATOM 278 C CB . SER A 1 43 ? 47.740 15.945 69.966 1.00 17.24 ? 44 SER A CB 1 ATOM 279 O OG . SER A 1 43 ? 46.762 16.800 69.415 1.00 21.60 ? 44 SER A OG 1 ATOM 280 N N . PRO A 1 44 ? 50.485 17.105 68.814 1.00 15.10 ? 45 PRO A N 1 ATOM 281 C CA . PRO A 1 44 ? 51.205 18.218 68.169 1.00 13.56 ? 45 PRO A CA 1 ATOM 282 C C . PRO A 1 44 ? 51.536 18.013 66.690 1.00 12.96 ? 45 PRO A C 1 ATOM 283 O O . PRO A 1 44 ? 51.400 18.946 65.895 1.00 14.50 ? 45 PRO A O 1 ATOM 284 C CB . PRO A 1 44 ? 52.433 18.383 69.047 1.00 13.27 ? 45 PRO A CB 1 ATOM 285 C CG . PRO A 1 44 ? 51.876 18.115 70.424 1.00 14.31 ? 45 PRO A CG 1 ATOM 286 C CD . PRO A 1 44 ? 51.008 16.859 70.173 1.00 13.29 ? 45 PRO A CD 1 ATOM 287 N N . VAL A 1 45 ? 51.976 16.815 66.298 1.00 13.65 ? 46 VAL A N 1 ATOM 288 C CA . VAL A 1 45 ? 52.271 16.570 64.873 1.00 12.05 ? 46 VAL A CA 1 ATOM 289 C C . VAL A 1 45 ? 51.004 16.655 64.021 1.00 13.05 ? 46 VAL A C 1 ATOM 290 O O . VAL A 1 45 ? 51.032 17.143 62.899 1.00 9.66 ? 46 VAL A O 1 ATOM 291 C CB . VAL A 1 45 ? 52.871 15.162 64.608 1.00 13.19 ? 46 VAL A CB 1 ATOM 292 C CG1 . VAL A 1 45 ? 53.119 14.991 63.126 1.00 15.88 ? 46 VAL A CG1 1 ATOM 293 C CG2 . VAL A 1 45 ? 54.173 14.959 65.371 1.00 14.80 ? 46 VAL A CG2 1 ATOM 294 N N . ARG A 1 46 ? 49.902 16.138 64.564 1.00 12.48 ? 47 ARG A N 1 ATOM 295 C CA . ARG A 1 46 ? 48.625 16.118 63.856 1.00 12.97 ? 47 ARG A CA 1 ATOM 296 C C . ARG A 1 46 ? 48.082 17.543 63.656 1.00 11.84 ? 47 ARG A C 1 ATOM 297 O O . ARG A 1 46 ? 47.611 17.894 62.573 1.00 11.05 ? 47 ARG A O 1 ATOM 298 C CB . ARG A 1 46 ? 47.650 15.225 64.614 1.00 9.48 ? 47 ARG A CB 1 ATOM 299 C CG . ARG A 1 46 ? 48.183 13.793 64.765 1.00 11.43 ? 47 ARG A CG 1 ATOM 300 C CD . ARG A 1 46 ? 47.077 12.783 65.095 1.00 9.57 ? 47 ARG A CD 1 ATOM 301 N NE . ARG A 1 46 ? 46.277 13.181 66.258 1.00 12.40 ? 47 ARG A NE 1 ATOM 302 C CZ . ARG A 1 46 ? 46.469 12.747 67.503 1.00 13.76 ? 47 ARG A CZ 1 ATOM 303 N NH1 . ARG A 1 46 ? 47.440 11.879 67.784 1.00 13.29 ? 47 ARG A NH1 1 ATOM 304 N NH2 . ARG A 1 46 ? 45.692 13.185 68.474 1.00 11.06 ? 47 ARG A NH2 1 ATOM 305 N N . LYS A 1 47 ? 48.179 18.355 64.705 1.00 11.83 ? 48 LYS A N 1 ATOM 306 C CA . LYS A 1 47 ? 47.769 19.747 64.675 1.00 12.34 ? 48 LYS A CA 1 ATOM 307 C C . LYS A 1 47 ? 48.627 20.527 63.669 1.00 14.21 ? 48 LYS A C 1 ATOM 308 O O . LYS A 1 47 ? 48.104 21.345 62.886 1.00 13.80 ? 48 LYS A O 1 ATOM 309 C CB . LYS A 1 47 ? 47.942 20.367 66.052 1.00 11.71 ? 48 LYS A CB 1 ATOM 310 C CG . LYS A 1 47 ? 47.065 19.785 67.150 1.00 14.22 ? 48 LYS A CG 1 ATOM 311 C CD . LYS A 1 47 ? 45.609 20.075 66.887 1.00 14.30 ? 48 LYS A CD 1 ATOM 312 C CE . LYS A 1 47 ? 44.748 19.758 68.098 1.00 15.39 ? 48 LYS A CE 1 ATOM 313 N NZ . LYS A 1 47 ? 43.349 20.112 67.750 1.00 16.65 ? 48 LYS A NZ 1 ATOM 314 N N . ILE A 1 48 ? 49.938 20.253 63.674 1.00 12.76 ? 49 ILE A N 1 ATOM 315 C CA . ILE A 1 48 ? 50.849 20.952 62.789 1.00 10.95 ? 49 ILE A CA 1 ATOM 316 C C . ILE A 1 48 ? 50.566 20.641 61.337 1.00 11.94 ? 49 ILE A C 1 ATOM 317 O O . ILE A 1 48 ? 50.672 21.527 60.495 1.00 13.91 ? 49 ILE A O 1 ATOM 318 C CB . ILE A 1 48 ? 52.343 20.708 63.174 1.00 13.26 ? 49 ILE A CB 1 ATOM 319 C CG1 . ILE A 1 48 ? 53.053 22.053 63.388 1.00 12.69 ? 49 ILE A CG1 1 ATOM 320 C CG2 . ILE A 1 48 ? 53.077 19.918 62.083 1.00 11.65 ? 49 ILE A CG2 1 ATOM 321 C CD1 . ILE A 1 48 ? 53.257 22.862 62.078 1.00 10.29 ? 49 ILE A CD1 1 ATOM 322 N N . LEU A 1 49 ? 50.136 19.410 61.047 1.00 11.82 ? 50 LEU A N 1 ATOM 323 C CA . LEU A 1 49 ? 49.797 18.992 59.687 1.00 10.76 ? 50 LEU A CA 1 ATOM 324 C C . LEU A 1 49 ? 48.531 19.706 59.197 1.00 10.58 ? 50 LEU A C 1 ATOM 325 O O . LEU A 1 49 ? 48.415 20.020 58.000 1.00 11.13 ? 50 LEU A O 1 ATOM 326 C CB . LEU A 1 49 ? 49.640 17.464 59.599 1.00 13.73 ? 50 LEU A CB 1 ATOM 327 C CG . LEU A 1 49 ? 50.891 16.626 59.343 1.00 12.14 ? 50 LEU A CG 1 ATOM 328 C CD1 . LEU A 1 49 ? 50.569 15.167 59.495 1.00 15.56 ? 50 LEU A CD1 1 ATOM 329 C CD2 . LEU A 1 49 ? 51.393 16.877 57.973 1.00 13.20 ? 50 LEU A CD2 1 ATOM 330 N N . ARG A 1 50 ? 47.600 19.970 60.117 1.00 12.75 ? 51 ARG A N 1 ATOM 331 C CA . ARG A 1 50 ? 46.379 20.727 59.803 1.00 13.49 ? 51 ARG A CA 1 ATOM 332 C C . ARG A 1 50 ? 46.847 22.155 59.475 1.00 12.95 ? 51 ARG A C 1 ATOM 333 O O . ARG A 1 50 ? 46.419 22.782 58.503 1.00 13.01 ? 51 ARG A O 1 ATOM 334 C CB . ARG A 1 50 ? 45.453 20.804 61.022 1.00 12.59 ? 51 ARG A CB 1 ATOM 335 C CG . ARG A 1 50 ? 44.321 19.796 61.041 1.00 16.44 ? 51 ARG A CG 1 ATOM 336 C CD . ARG A 1 50 ? 43.337 20.076 62.203 1.00 16.70 ? 51 ARG A CD 1 ATOM 337 N NE . ARG A 1 50 ? 42.373 21.151 61.931 1.00 13.42 ? 51 ARG A NE 1 ATOM 338 C CZ . ARG A 1 50 ? 41.723 21.830 62.871 1.00 11.06 ? 51 ARG A CZ 1 ATOM 339 N NH1 . ARG A 1 50 ? 41.916 21.564 64.140 1.00 11.69 ? 51 ARG A NH1 1 ATOM 340 N NH2 . ARG A 1 50 ? 40.870 22.794 62.547 1.00 14.11 ? 51 ARG A NH2 1 ATOM 341 N N . ILE A 1 51 ? 47.728 22.663 60.322 1.00 13.97 ? 52 ILE A N 1 ATOM 342 C CA . ILE A 1 51 ? 48.259 24.012 60.160 1.00 12.67 ? 52 ILE A CA 1 ATOM 343 C C . ILE A 1 51 ? 48.982 24.224 58.842 1.00 11.89 ? 52 ILE A C 1 ATOM 344 O O . ILE A 1 51 ? 48.739 25.218 58.159 1.00 13.20 ? 52 ILE A O 1 ATOM 345 C CB . ILE A 1 51 ? 49.141 24.397 61.374 1.00 13.54 ? 52 ILE A CB 1 ATOM 346 C CG1 . ILE A 1 51 ? 48.253 24.529 62.611 1.00 12.81 ? 52 ILE A CG1 1 ATOM 347 C CG2 . ILE A 1 51 ? 49.902 25.690 61.125 1.00 11.35 ? 52 ILE A CG2 1 ATOM 348 C CD1 . ILE A 1 51 ? 48.980 24.830 63.887 1.00 11.26 ? 52 ILE A CD1 1 ATOM 349 N N . VAL A 1 52 ? 49.881 23.335 58.454 1.00 10.37 ? 53 VAL A N 1 ATOM 350 C CA . VAL A 1 52 ? 50.563 23.555 57.187 1.00 9.62 ? 53 VAL A CA 1 ATOM 351 C C . VAL A 1 52 ? 49.595 23.660 55.996 1.00 11.77 ? 53 VAL A C 1 ATOM 352 O O . VAL A 1 52 ? 49.744 24.546 55.141 1.00 10.88 ? 53 VAL A O 1 ATOM 353 C CB . VAL A 1 52 ? 51.697 22.503 56.942 1.00 11.00 ? 53 VAL A CB 1 ATOM 354 C CG1 . VAL A 1 52 ? 51.148 21.087 56.740 1.00 8.68 ? 53 VAL A CG1 1 ATOM 355 C CG2 . VAL A 1 52 ? 52.560 22.933 55.757 1.00 10.76 ? 53 VAL A CG2 1 ATOM 356 N N . PHE A 1 53 ? 48.619 22.752 55.925 1.00 10.56 ? 54 PHE A N 1 ATOM 357 C CA . PHE A 1 53 ? 47.619 22.761 54.851 1.00 10.93 ? 54 PHE A CA 1 ATOM 358 C C . PHE A 1 53 ? 46.773 24.054 54.890 1.00 9.64 ? 54 PHE A C 1 ATOM 359 O O . PHE A 1 53 ? 46.578 24.699 53.872 1.00 10.18 ? 54 PHE A O 1 ATOM 360 C CB . PHE A 1 53 ? 46.722 21.507 54.997 1.00 11.29 ? 54 PHE A CB 1 ATOM 361 C CG . PHE A 1 53 ? 45.548 21.465 54.048 1.00 12.69 ? 54 PHE A CG 1 ATOM 362 C CD1 . PHE A 1 53 ? 44.278 21.100 54.511 1.00 13.85 ? 54 PHE A CD1 1 ATOM 363 C CD2 . PHE A 1 53 ? 45.704 21.779 52.691 1.00 12.14 ? 54 PHE A CD2 1 ATOM 364 C CE1 . PHE A 1 53 ? 43.177 21.054 53.622 1.00 15.43 ? 54 PHE A CE1 1 ATOM 365 C CE2 . PHE A 1 53 ? 44.626 21.739 51.807 1.00 12.81 ? 54 PHE A CE2 1 ATOM 366 C CZ . PHE A 1 53 ? 43.365 21.382 52.262 1.00 13.70 ? 54 PHE A CZ 1 ATOM 367 N N . HIS A 1 54 ? 46.281 24.428 56.075 1.00 11.36 ? 55 HIS A N 1 ATOM 368 C CA . HIS A 1 54 ? 45.448 25.635 56.204 1.00 12.54 ? 55 HIS A CA 1 ATOM 369 C C . HIS A 1 54 ? 46.228 26.935 55.956 1.00 14.42 ? 55 HIS A C 1 ATOM 370 O O . HIS A 1 54 ? 45.652 27.916 55.473 1.00 14.75 ? 55 HIS A O 1 ATOM 371 C CB . HIS A 1 54 ? 44.692 25.665 57.538 1.00 11.36 ? 55 HIS A CB 1 ATOM 372 C CG . HIS A 1 54 ? 43.689 24.554 57.686 1.00 13.18 ? 55 HIS A CG 1 ATOM 373 N ND1 . HIS A 1 54 ? 42.756 24.522 58.702 1.00 13.37 ? 55 HIS A ND1 1 ATOM 374 C CD2 . HIS A 1 54 ? 43.530 23.390 57.005 1.00 14.75 ? 55 HIS A CD2 1 ATOM 375 C CE1 . HIS A 1 54 ? 42.079 23.391 58.648 1.00 15.79 ? 55 HIS A CE1 1 ATOM 376 N NE2 . HIS A 1 54 ? 42.526 22.683 57.632 1.00 17.22 ? 55 HIS A NE2 1 ATOM 377 N N . ASP A 1 55 ? 47.529 26.951 56.259 1.00 12.69 ? 56 ASP A N 1 ATOM 378 C CA . ASP A 1 55 ? 48.330 28.132 55.970 1.00 9.96 ? 56 ASP A CA 1 ATOM 379 C C . ASP A 1 55 ? 48.554 28.229 54.477 1.00 9.99 ? 56 ASP A C 1 ATOM 380 O O . ASP A 1 55 ? 48.303 29.274 53.872 1.00 12.21 ? 56 ASP A O 1 ATOM 381 C CB . ASP A 1 55 ? 49.700 28.084 56.646 1.00 11.78 ? 56 ASP A CB 1 ATOM 382 C CG . ASP A 1 55 ? 50.576 29.305 56.280 1.00 14.31 ? 56 ASP A CG 1 ATOM 383 O OD1 . ASP A 1 55 ? 50.020 30.424 56.175 1.00 15.09 ? 56 ASP A OD1 1 ATOM 384 O OD2 . ASP A 1 55 ? 51.804 29.140 56.075 1.00 12.28 ? 56 ASP A OD2 1 ATOM 385 N N . ALA A 1 56 ? 49.037 27.153 53.873 1.00 9.30 ? 57 ALA A N 1 ATOM 386 C CA . ALA A 1 56 ? 49.341 27.137 52.460 1.00 8.70 ? 57 ALA A CA 1 ATOM 387 C C . ALA A 1 56 ? 48.199 27.264 51.506 1.00 10.33 ? 57 ALA A C 1 ATOM 388 O O . ALA A 1 56 ? 48.347 27.894 50.476 1.00 10.17 ? 57 ALA A O 1 ATOM 389 C CB . ALA A 1 56 ? 50.115 25.887 52.117 1.00 10.27 ? 57 ALA A CB 1 ATOM 390 N N . ILE A 1 57 ? 47.047 26.715 51.857 1.00 10.16 ? 58 ILE A N 1 ATOM 391 C CA . ILE A 1 57 ? 45.918 26.730 50.938 1.00 11.55 ? 58 ILE A CA 1 ATOM 392 C C . ILE A 1 57 ? 45.221 28.104 50.738 1.00 12.06 ? 58 ILE A C 1 ATOM 393 O O . ILE A 1 57 ? 44.375 28.259 49.825 1.00 11.44 ? 58 ILE A O 1 ATOM 394 C CB . ILE A 1 57 ? 44.919 25.599 51.299 1.00 10.53 ? 58 ILE A CB 1 ATOM 395 C CG1 . ILE A 1 57 ? 44.135 25.188 50.064 1.00 10.30 ? 58 ILE A CG1 1 ATOM 396 C CG2 . ILE A 1 57 ? 44.013 26.022 52.439 1.00 8.54 ? 58 ILE A CG2 1 ATOM 397 C CD1 . ILE A 1 57 ? 45.000 24.687 48.927 1.00 12.07 ? 58 ILE A CD1 1 ATOM 398 N N . GLY A 1 58 ? 45.583 29.087 51.568 1.00 12.32 ? 59 GLY A N 1 ATOM 399 C CA . GLY A 1 58 ? 45.033 30.434 51.428 1.00 12.97 ? 59 GLY A CA 1 ATOM 400 C C . GLY A 1 58 ? 45.817 31.062 50.283 1.00 13.46 ? 59 GLY A C 1 ATOM 401 O O . GLY A 1 58 ? 46.677 31.937 50.488 1.00 13.97 ? 59 GLY A O 1 ATOM 402 N N . PHE A 1 59 ? 45.541 30.583 49.078 1.00 13.64 ? 60 PHE A N 1 ATOM 403 C CA . PHE A 1 59 ? 46.240 31.011 47.887 1.00 14.99 ? 60 PHE A CA 1 ATOM 404 C C . PHE A 1 59 ? 45.273 30.777 46.757 1.00 15.94 ? 60 PHE A C 1 ATOM 405 O O . PHE A 1 59 ? 44.774 29.675 46.607 1.00 18.19 ? 60 PHE A O 1 ATOM 406 C CB . PHE A 1 59 ? 47.492 30.143 47.708 1.00 13.69 ? 60 PHE A CB 1 ATOM 407 C CG . PHE A 1 59 ? 48.268 30.439 46.459 1.00 16.49 ? 60 PHE A CG 1 ATOM 408 C CD1 . PHE A 1 59 ? 49.047 31.589 46.369 1.00 15.90 ? 60 PHE A CD1 1 ATOM 409 C CD2 . PHE A 1 59 ? 48.206 29.575 45.367 1.00 15.89 ? 60 PHE A CD2 1 ATOM 410 C CE1 . PHE A 1 59 ? 49.749 31.880 45.210 1.00 16.52 ? 60 PHE A CE1 1 ATOM 411 C CE2 . PHE A 1 59 ? 48.905 29.851 44.200 1.00 17.33 ? 60 PHE A CE2 1 ATOM 412 C CZ . PHE A 1 59 ? 49.681 31.012 44.120 1.00 17.12 ? 60 PHE A CZ 1 ATOM 413 N N . SER A 1 60 ? 45.030 31.790 45.936 1.00 16.56 ? 61 SER A N 1 ATOM 414 C CA . SER A 1 60 ? 44.059 31.648 44.860 1.00 15.13 ? 61 SER A CA 1 ATOM 415 C C . SER A 1 60 ? 44.343 32.447 43.607 1.00 16.59 ? 61 SER A C 1 ATOM 416 O O . SER A 1 60 ? 44.040 33.642 43.528 1.00 16.22 ? 61 SER A O 1 ATOM 417 C CB . SER A 1 60 ? 42.661 32.011 45.369 1.00 14.94 ? 61 SER A CB 1 ATOM 418 O OG . SER A 1 60 ? 41.731 32.026 44.297 1.00 13.45 ? 61 SER A OG 1 ATOM 419 N N . PRO A 1 61 ? 44.937 31.797 42.606 1.00 17.07 ? 62 PRO A N 1 ATOM 420 C CA . PRO A 1 61 ? 45.248 32.463 41.351 1.00 17.98 ? 62 PRO A CA 1 ATOM 421 C C . PRO A 1 61 ? 43.988 33.065 40.743 1.00 19.10 ? 62 PRO A C 1 ATOM 422 O O . PRO A 1 61 ? 44.055 34.102 40.102 1.00 20.18 ? 62 PRO A O 1 ATOM 423 C CB . PRO A 1 61 ? 45.807 31.322 40.510 1.00 18.35 ? 62 PRO A CB 1 ATOM 424 C CG . PRO A 1 61 ? 46.580 30.529 41.539 1.00 18.01 ? 62 PRO A CG 1 ATOM 425 C CD . PRO A 1 61 ? 45.570 30.464 42.665 1.00 17.59 ? 62 PRO A CD 1 ATOM 426 N N . ALA A 1 62 ? 42.837 32.439 40.970 1.00 18.96 ? 63 ALA A N 1 ATOM 427 C CA . ALA A 1 62 ? 41.583 32.961 40.427 1.00 20.30 ? 63 ALA A CA 1 ATOM 428 C C . ALA A 1 62 ? 41.243 34.325 41.020 1.00 20.62 ? 63 ALA A C 1 ATOM 429 O O . ALA A 1 62 ? 40.809 35.228 40.309 1.00 22.81 ? 63 ALA A O 1 ATOM 430 C CB . ALA A 1 62 ? 40.434 31.990 40.670 1.00 20.21 ? 63 ALA A CB 1 ATOM 431 N N . LEU A 1 63 ? 41.396 34.485 42.324 1.00 20.43 ? 64 LEU A N 1 ATOM 432 C CA . LEU A 1 63 ? 41.093 35.771 42.913 1.00 20.28 ? 64 LEU A CA 1 ATOM 433 C C . LEU A 1 63 ? 42.075 36.816 42.383 1.00 22.56 ? 64 LEU A C 1 ATOM 434 O O . LEU A 1 63 ? 41.713 37.936 42.059 1.00 24.28 ? 64 LEU A O 1 ATOM 435 C CB . LEU A 1 63 ? 41.198 35.682 44.426 1.00 20.12 ? 64 LEU A CB 1 ATOM 436 C CG . LEU A 1 63 ? 40.122 34.871 45.135 1.00 20.38 ? 64 LEU A CG 1 ATOM 437 C CD1 . LEU A 1 63 ? 40.278 34.993 46.646 1.00 17.93 ? 64 LEU A CD1 1 ATOM 438 C CD2 . LEU A 1 63 ? 38.758 35.384 44.694 1.00 20.86 ? 64 LEU A CD2 1 ATOM 439 N N . THR A 1 64 ? 43.319 36.417 42.220 1.00 22.03 ? 65 THR A N 1 ATOM 440 C CA . THR A 1 64 ? 44.328 37.340 41.747 1.00 21.93 ? 65 THR A CA 1 ATOM 441 C C . THR A 1 64 ? 44.056 37.811 40.310 1.00 23.09 ? 65 THR A C 1 ATOM 442 O O . THR A 1 64 ? 44.136 38.991 40.032 1.00 22.67 ? 65 THR A O 1 ATOM 443 C CB . THR A 1 64 ? 45.738 36.709 41.903 1.00 20.90 ? 65 THR A CB 1 ATOM 444 O OG1 . THR A 1 64 ? 45.955 36.381 43.286 1.00 20.76 ? 65 THR A OG1 1 ATOM 445 C CG2 . THR A 1 64 ? 46.824 37.672 41.453 1.00 20.93 ? 65 THR A CG2 1 ATOM 446 N N . ALA A 1 65 ? 43.690 36.901 39.419 1.00 22.90 ? 66 ALA A N 1 ATOM 447 C CA . ALA A 1 65 ? 43.419 37.248 38.023 1.00 25.35 ? 66 ALA A CA 1 ATOM 448 C C . ALA A 1 65 ? 42.259 38.235 37.937 1.00 27.04 ? 66 ALA A C 1 ATOM 449 O O . ALA A 1 65 ? 42.127 38.999 36.966 1.00 29.14 ? 66 ALA A O 1 ATOM 450 C CB . ALA A 1 65 ? 43.093 35.979 37.214 1.00 22.07 ? 66 ALA A CB 1 ATOM 451 N N . ALA A 1 66 ? 41.405 38.191 38.948 1.00 28.13 ? 67 ALA A N 1 ATOM 452 C CA . ALA A 1 66 ? 40.250 39.072 39.003 1.00 31.02 ? 67 ALA A CA 1 ATOM 453 C C . ALA A 1 66 ? 40.556 40.419 39.692 1.00 32.78 ? 67 ALA A C 1 ATOM 454 O O . ALA A 1 66 ? 39.657 41.240 39.897 1.00 36.13 ? 67 ALA A O 1 ATOM 455 C CB . ALA A 1 66 ? 39.112 38.375 39.698 1.00 29.44 ? 67 ALA A CB 1 ATOM 456 N N . GLY A 1 67 ? 41.805 40.624 40.100 1.00 32.46 ? 68 GLY A N 1 ATOM 457 C CA . GLY A 1 67 ? 42.173 41.876 40.726 1.00 30.32 ? 68 GLY A CA 1 ATOM 458 C C . GLY A 1 67 ? 42.004 41.944 42.222 1.00 31.15 ? 68 GLY A C 1 ATOM 459 O O . GLY A 1 67 ? 42.157 43.006 42.814 1.00 32.68 ? 68 GLY A O 1 ATOM 460 N N . GLN A 1 68 ? 41.714 40.822 42.856 1.00 29.56 ? 69 GLN A N 1 ATOM 461 C CA . GLN A 1 68 ? 41.544 40.829 44.293 1.00 29.09 ? 69 GLN A CA 1 ATOM 462 C C . GLN A 1 68 ? 42.743 40.161 44.918 1.00 26.12 ? 69 GLN A C 1 ATOM 463 O O . GLN A 1 68 ? 43.544 39.552 44.222 1.00 26.60 ? 69 GLN A O 1 ATOM 464 C CB . GLN A 1 68 ? 40.257 40.099 44.661 1.00 33.80 ? 69 GLN A CB 1 ATOM 465 C CG . GLN A 1 68 ? 39.031 40.640 43.905 1.00 40.86 ? 69 GLN A CG 1 ATOM 466 C CD . GLN A 1 68 ? 37.705 40.125 44.453 1.00 44.93 ? 69 GLN A CD 1 ATOM 467 O OE1 . GLN A 1 68 ? 36.842 39.657 43.701 1.00 46.70 ? 69 GLN A OE1 1 ATOM 468 N NE2 . GLN A 1 68 ? 37.527 40.230 45.771 1.00 48.66 ? 69 GLN A NE2 1 ATOM 469 N N . PHE A 1 69 ? 42.901 40.311 46.221 1.00 22.55 ? 70 PHE A N 1 ATOM 470 C CA . PHE A 1 69 ? 44.025 39.667 46.901 1.00 22.61 ? 70 PHE A CA 1 ATOM 471 C C . PHE A 1 69 ? 43.641 38.197 47.026 1.00 20.94 ? 70 PHE A C 1 ATOM 472 O O . PHE A 1 69 ? 42.533 37.881 47.467 1.00 22.78 ? 70 PHE A O 1 ATOM 473 C CB . PHE A 1 69 ? 44.280 40.290 48.284 1.00 20.34 ? 70 PHE A CB 1 ATOM 474 C CG . PHE A 1 69 ? 45.383 39.614 49.078 1.00 20.43 ? 70 PHE A CG 1 ATOM 475 C CD1 . PHE A 1 69 ? 46.659 39.470 48.552 1.00 20.57 ? 70 PHE A CD1 1 ATOM 476 C CD2 . PHE A 1 69 ? 45.144 39.129 50.361 1.00 18.39 ? 70 PHE A CD2 1 ATOM 477 C CE1 . PHE A 1 69 ? 47.678 38.850 49.304 1.00 19.93 ? 70 PHE A CE1 1 ATOM 478 C CE2 . PHE A 1 69 ? 46.159 38.517 51.104 1.00 18.39 ? 70 PHE A CE2 1 ATOM 479 C CZ . PHE A 1 69 ? 47.412 38.380 50.578 1.00 17.22 ? 70 PHE A CZ 1 ATOM 480 N N . GLY A 1 70 ? 44.503 37.310 46.547 1.00 20.48 ? 71 GLY A N 1 ATOM 481 C CA . GLY A 1 70 ? 44.215 35.890 46.628 1.00 16.24 ? 71 GLY A CA 1 ATOM 482 C C . GLY A 1 70 ? 44.880 35.153 47.783 1.00 16.37 ? 71 GLY A C 1 ATOM 483 O O . GLY A 1 70 ? 44.663 33.948 47.921 1.00 15.57 ? 71 GLY A O 1 ATOM 484 N N . GLY A 1 71 ? 45.652 35.845 48.621 1.00 13.49 ? 72 GLY A N 1 ATOM 485 C CA . GLY A 1 71 ? 46.326 35.174 49.722 1.00 13.90 ? 72 GLY A CA 1 ATOM 486 C C . GLY A 1 71 ? 47.768 34.890 49.331 1.00 14.49 ? 72 GLY A C 1 ATOM 487 O O . GLY A 1 71 ? 48.083 34.721 48.144 1.00 15.59 ? 72 GLY A O 1 ATOM 488 N N . GLY A 1 72 ? 48.664 34.868 50.312 1.00 15.12 ? 73 GLY A N 1 ATOM 489 C CA . GLY A 1 72 ? 50.071 34.619 50.027 1.00 16.39 ? 73 GLY A CA 1 ATOM 490 C C . GLY A 1 72 ? 50.588 33.186 50.130 1.00 16.96 ? 73 GLY A C 1 ATOM 491 O O . GLY A 1 72 ? 51.808 32.978 50.151 1.00 15.58 ? 73 GLY A O 1 ATOM 492 N N . GLY A 1 73 ? 49.679 32.215 50.261 1.00 16.71 ? 74 GLY A N 1 ATOM 493 C CA . GLY A 1 73 ? 50.071 30.822 50.347 1.00 15.83 ? 74 GLY A CA 1 ATOM 494 C C . GLY A 1 73 ? 50.772 30.452 51.630 1.00 14.77 ? 74 GLY A C 1 ATOM 495 O O . GLY A 1 73 ? 50.305 30.808 52.732 1.00 15.73 ? 74 GLY A O 1 ATOM 496 N N . ALA A 1 74 ? 51.885 29.732 51.483 1.00 15.41 ? 75 ALA A N 1 ATOM 497 C CA . ALA A 1 74 ? 52.697 29.248 52.598 1.00 14.99 ? 75 ALA A CA 1 ATOM 498 C C . ALA A 1 74 ? 53.573 30.341 53.237 1.00 16.50 ? 75 ALA A C 1 ATOM 499 O O . ALA A 1 74 ? 54.765 30.144 53.473 1.00 14.28 ? 75 ALA A O 1 ATOM 500 C CB . ALA A 1 74 ? 53.552 28.093 52.140 1.00 14.06 ? 75 ALA A CB 1 ATOM 501 N N . ASP A 1 75 ? 52.914 31.418 53.659 1.00 15.34 ? 76 ASP A N 1 ATOM 502 C CA . ASP A 1 75 ? 53.565 32.594 54.240 1.00 14.14 ? 76 ASP A CA 1 ATOM 503 C C . ASP A 1 75 ? 53.504 32.731 55.752 1.00 11.87 ? 76 ASP A C 1 ATOM 504 O O . ASP A 1 75 ? 53.869 33.754 56.285 1.00 14.94 ? 76 ASP A O 1 ATOM 505 C CB . ASP A 1 75 ? 52.948 33.842 53.585 1.00 14.87 ? 76 ASP A CB 1 ATOM 506 C CG . ASP A 1 75 ? 51.407 33.921 53.777 1.00 14.71 ? 76 ASP A CG 1 ATOM 507 O OD1 . ASP A 1 75 ? 50.747 34.838 53.244 1.00 15.64 ? 76 ASP A OD1 1 ATOM 508 O OD2 . ASP A 1 75 ? 50.856 33.089 54.518 1.00 13.23 ? 76 ASP A OD2 1 ATOM 509 N N . GLY A 1 76 ? 53.000 31.724 56.448 1.00 11.66 ? 77 GLY A N 1 ATOM 510 C CA . GLY A 1 76 ? 52.900 31.824 57.898 1.00 9.43 ? 77 GLY A CA 1 ATOM 511 C C . GLY A 1 76 ? 51.835 32.806 58.366 1.00 10.44 ? 77 GLY A C 1 ATOM 512 O O . GLY A 1 76 ? 51.781 33.126 59.544 1.00 9.65 ? 77 GLY A O 1 ATOM 513 N N . SER A 1 77 ? 50.956 33.256 57.464 1.00 11.81 ? 78 SER A N 1 ATOM 514 C CA . SER A 1 77 ? 49.878 34.204 57.811 1.00 10.02 ? 78 SER A CA 1 ATOM 515 C C . SER A 1 77 ? 48.979 33.696 58.915 1.00 12.96 ? 78 SER A C 1 ATOM 516 O O . SER A 1 77 ? 48.420 34.477 59.687 1.00 11.98 ? 78 SER A O 1 ATOM 517 C CB . SER A 1 77 ? 49.021 34.523 56.588 1.00 11.57 ? 78 SER A CB 1 ATOM 518 O OG . SER A 1 77 ? 48.397 33.375 56.032 1.00 12.28 ? 78 SER A OG 1 ATOM 519 N N . ILE A 1 78 ? 48.814 32.374 58.970 1.00 13.75 ? 79 ILE A N 1 ATOM 520 C CA . ILE A 1 78 ? 47.982 31.742 59.982 1.00 13.55 ? 79 ILE A CA 1 ATOM 521 C C . ILE A 1 78 ? 48.484 32.050 61.398 1.00 14.67 ? 79 ILE A C 1 ATOM 522 O O . ILE A 1 78 ? 47.707 32.029 62.367 1.00 16.16 ? 79 ILE A O 1 ATOM 523 C CB . ILE A 1 78 ? 47.832 30.204 59.698 1.00 13.88 ? 79 ILE A CB 1 ATOM 524 C CG1 . ILE A 1 78 ? 46.733 29.601 60.591 1.00 18.59 ? 79 ILE A CG1 1 ATOM 525 C CG2 . ILE A 1 78 ? 49.139 29.483 59.952 1.00 13.51 ? 79 ILE A CG2 1 ATOM 526 C CD1 . ILE A 1 78 ? 46.193 28.256 60.061 1.00 19.40 ? 79 ILE A CD1 1 ATOM 527 N N . ILE A 1 79 ? 49.780 32.356 61.518 1.00 15.72 ? 80 ILE A N 1 ATOM 528 C CA . ILE A 1 79 ? 50.376 32.719 62.811 1.00 15.03 ? 80 ILE A CA 1 ATOM 529 C C . ILE A 1 79 ? 50.443 34.256 62.908 1.00 15.15 ? 80 ILE A C 1 ATOM 530 O O . ILE A 1 79 ? 49.937 34.826 63.856 1.00 16.84 ? 80 ILE A O 1 ATOM 531 C CB . ILE A 1 79 ? 51.816 32.135 63.011 1.00 16.09 ? 80 ILE A CB 1 ATOM 532 C CG1 . ILE A 1 79 ? 51.773 30.608 63.055 1.00 16.23 ? 80 ILE A CG1 1 ATOM 533 C CG2 . ILE A 1 79 ? 52.418 32.632 64.315 1.00 13.68 ? 80 ILE A CG2 1 ATOM 534 C CD1 . ILE A 1 79 ? 53.149 29.966 63.130 1.00 16.00 ? 80 ILE A CD1 1 ATOM 535 N N . ALA A 1 80 ? 51.050 34.912 61.920 1.00 14.54 ? 81 ALA A N 1 ATOM 536 C CA . ALA A 1 80 ? 51.169 36.374 61.934 1.00 15.44 ? 81 ALA A CA 1 ATOM 537 C C . ALA A 1 80 ? 49.794 37.055 62.089 1.00 17.67 ? 81 ALA A C 1 ATOM 538 O O . ALA A 1 80 ? 49.664 38.039 62.818 1.00 16.53 ? 81 ALA A O 1 ATOM 539 C CB . ALA A 1 80 ? 51.845 36.865 60.677 1.00 11.29 ? 81 ALA A CB 1 ATOM 540 N N . HIS A 1 81 ? 48.772 36.508 61.427 1.00 16.88 ? 82 HIS A N 1 ATOM 541 C CA . HIS A 1 81 ? 47.422 37.069 61.469 1.00 16.78 ? 82 HIS A CA 1 ATOM 542 C C . HIS A 1 81 ? 46.393 36.113 62.031 1.00 17.49 ? 82 HIS A C 1 ATOM 543 O O . HIS A 1 81 ? 45.238 36.117 61.618 1.00 17.55 ? 82 HIS A O 1 ATOM 544 C CB . HIS A 1 81 ? 47.030 37.489 60.075 1.00 14.97 ? 82 HIS A CB 1 ATOM 545 C CG . HIS A 1 81 ? 47.985 38.463 59.474 1.00 19.36 ? 82 HIS A CG 1 ATOM 546 N ND1 . HIS A 1 81 ? 48.023 39.792 59.843 1.00 17.58 ? 82 HIS A ND1 1 ATOM 547 C CD2 . HIS A 1 81 ? 48.979 38.294 58.569 1.00 18.50 ? 82 HIS A CD2 1 ATOM 548 C CE1 . HIS A 1 81 ? 48.995 40.400 59.192 1.00 17.92 ? 82 HIS A CE1 1 ATOM 549 N NE2 . HIS A 1 81 ? 49.591 39.512 58.411 1.00 18.58 ? 82 HIS A NE2 1 ATOM 550 N N . SER A 1 82 ? 46.789 35.369 63.053 1.00 17.37 ? 83 SER A N 1 ATOM 551 C CA . SER A 1 82 ? 45.911 34.398 63.668 1.00 16.98 ? 83 SER A CA 1 ATOM 552 C C . SER A 1 82 ? 44.638 35.043 64.230 1.00 18.31 ? 83 SER A C 1 ATOM 553 O O . SER A 1 82 ? 43.591 34.400 64.338 1.00 16.55 ? 83 SER A O 1 ATOM 554 C CB . SER A 1 82 ? 46.675 33.708 64.770 1.00 16.69 ? 83 SER A CB 1 ATOM 555 O OG . SER A 1 82 ? 47.200 34.675 65.657 1.00 16.44 ? 83 SER A OG 1 ATOM 556 N N . ASN A 1 83 ? 44.736 36.320 64.579 1.00 18.57 ? 84 ASN A N 1 ATOM 557 C CA . ASN A 1 83 ? 43.612 37.047 65.125 1.00 18.16 ? 84 ASN A CA 1 ATOM 558 C C . ASN A 1 83 ? 42.452 37.005 64.126 1.00 17.45 ? 84 ASN A C 1 ATOM 559 O O . ASN A 1 83 ? 41.288 36.912 64.520 1.00 16.53 ? 84 ASN A O 1 ATOM 560 C CB . ASN A 1 83 ? 44.035 38.470 65.467 1.00 22.44 ? 84 ASN A CB 1 ATOM 561 C CG . ASN A 1 83 ? 44.360 39.308 64.235 1.00 27.34 ? 84 ASN A CG 1 ATOM 562 O OD1 . ASN A 1 83 ? 43.817 40.399 64.057 1.00 33.47 ? 84 ASN A OD1 1 ATOM 563 N ND2 . ASN A 1 83 ? 45.232 38.810 63.384 1.00 28.26 ? 84 ASN A ND2 1 ATOM 564 N N . ILE A 1 84 ? 42.783 37.023 62.843 1.00 14.33 ? 85 ILE A N 1 ATOM 565 C CA . ILE A 1 84 ? 41.790 36.938 61.779 1.00 15.41 ? 85 ILE A CA 1 ATOM 566 C C . ILE A 1 84 ? 41.536 35.479 61.368 1.00 15.54 ? 85 ILE A C 1 ATOM 567 O O . ILE A 1 84 ? 40.400 35.002 61.384 1.00 14.06 ? 85 ILE A O 1 ATOM 568 C CB . ILE A 1 84 ? 42.258 37.679 60.501 1.00 14.58 ? 85 ILE A CB 1 ATOM 569 C CG1 . ILE A 1 84 ? 42.262 39.194 60.727 1.00 18.85 ? 85 ILE A CG1 1 ATOM 570 C CG2 . ILE A 1 84 ? 41.386 37.305 59.283 1.00 14.26 ? 85 ILE A CG2 1 ATOM 571 C CD1 . ILE A 1 84 ? 40.876 39.817 60.980 1.00 19.92 ? 85 ILE A CD1 1 ATOM 572 N N . GLU A 1 85 ? 42.609 34.779 61.009 1.00 14.36 ? 86 GLU A N 1 ATOM 573 C CA . GLU A 1 85 ? 42.504 33.413 60.492 1.00 13.96 ? 86 GLU A CA 1 ATOM 574 C C . GLU A 1 85 ? 42.004 32.343 61.438 1.00 11.96 ? 86 GLU A C 1 ATOM 575 O O . GLU A 1 85 ? 41.282 31.432 61.042 1.00 13.56 ? 86 GLU A O 1 ATOM 576 C CB . GLU A 1 85 ? 43.836 32.994 59.844 1.00 13.81 ? 86 GLU A CB 1 ATOM 577 C CG . GLU A 1 85 ? 44.249 33.906 58.707 1.00 13.42 ? 86 GLU A CG 1 ATOM 578 C CD . GLU A 1 85 ? 45.309 33.298 57.794 1.00 15.89 ? 86 GLU A CD 1 ATOM 579 O OE1 . GLU A 1 85 ? 45.464 32.050 57.766 1.00 18.08 ? 86 GLU A OE1 1 ATOM 580 O OE2 . GLU A 1 85 ? 45.976 34.070 57.072 1.00 13.42 ? 86 GLU A OE2 1 ATOM 581 N N . LEU A 1 86 ? 42.322 32.466 62.706 1.00 12.59 ? 87 LEU A N 1 ATOM 582 C CA . LEU A 1 86 ? 41.872 31.447 63.625 1.00 16.38 ? 87 LEU A CA 1 ATOM 583 C C . LEU A 1 86 ? 40.371 31.493 63.939 1.00 17.64 ? 87 LEU A C 1 ATOM 584 O O . LEU A 1 86 ? 39.847 30.631 64.650 1.00 19.78 ? 87 LEU A O 1 ATOM 585 C CB . LEU A 1 86 ? 42.744 31.444 64.880 1.00 17.05 ? 87 LEU A CB 1 ATOM 586 C CG . LEU A 1 86 ? 43.825 30.348 64.987 1.00 16.94 ? 87 LEU A CG 1 ATOM 587 C CD1 . LEU A 1 86 ? 44.453 30.008 63.646 1.00 15.29 ? 87 LEU A CD1 1 ATOM 588 C CD2 . LEU A 1 86 ? 44.847 30.779 66.025 1.00 16.84 ? 87 LEU A CD2 1 ATOM 589 N N . ALA A 1 87 ? 39.687 32.500 63.400 1.00 17.38 ? 88 ALA A N 1 ATOM 590 C CA . ALA A 1 87 ? 38.233 32.648 63.580 1.00 15.87 ? 88 ALA A CA 1 ATOM 591 C C . ALA A 1 87 ? 37.513 32.014 62.380 1.00 15.86 ? 88 ALA A C 1 ATOM 592 O O . ALA A 1 87 ? 36.280 31.971 62.342 1.00 16.64 ? 88 ALA A O 1 ATOM 593 C CB . ALA A 1 87 ? 37.842 34.133 63.724 1.00 13.76 ? 88 ALA A CB 1 ATOM 594 N N . PHE A 1 88 ? 38.272 31.585 61.372 1.00 13.82 ? 89 PHE A N 1 ATOM 595 C CA . PHE A 1 88 ? 37.676 30.914 60.225 1.00 15.20 ? 89 PHE A CA 1 ATOM 596 C C . PHE A 1 88 ? 37.132 29.582 60.783 1.00 16.31 ? 89 PHE A C 1 ATOM 597 O O . PHE A 1 88 ? 37.791 28.937 61.599 1.00 16.78 ? 89 PHE A O 1 ATOM 598 C CB . PHE A 1 88 ? 38.750 30.580 59.184 1.00 15.10 ? 89 PHE A CB 1 ATOM 599 C CG . PHE A 1 88 ? 39.332 31.778 58.459 1.00 15.21 ? 89 PHE A CG 1 ATOM 600 C CD1 . PHE A 1 88 ? 38.823 33.071 58.654 1.00 14.90 ? 89 PHE A CD1 1 ATOM 601 C CD2 . PHE A 1 88 ? 40.358 31.597 57.526 1.00 14.87 ? 89 PHE A CD2 1 ATOM 602 C CE1 . PHE A 1 88 ? 39.331 34.168 57.921 1.00 13.98 ? 89 PHE A CE1 1 ATOM 603 C CE2 . PHE A 1 88 ? 40.873 32.701 56.790 1.00 13.94 ? 89 PHE A CE2 1 ATOM 604 C CZ . PHE A 1 88 ? 40.353 33.978 56.994 1.00 12.13 ? 89 PHE A CZ 1 ATOM 605 N N . PRO A 1 89 ? 35.918 29.166 60.375 1.00 16.75 ? 90 PRO A N 1 ATOM 606 C CA . PRO A 1 89 ? 35.296 27.914 60.822 1.00 16.39 ? 90 PRO A CA 1 ATOM 607 C C . PRO A 1 89 ? 36.230 26.681 60.751 1.00 15.15 ? 90 PRO A C 1 ATOM 608 O O . PRO A 1 89 ? 36.254 25.852 61.660 1.00 14.27 ? 90 PRO A O 1 ATOM 609 C CB . PRO A 1 89 ? 34.136 27.760 59.836 1.00 16.84 ? 90 PRO A CB 1 ATOM 610 C CG . PRO A 1 89 ? 33.693 29.187 59.652 1.00 18.55 ? 90 PRO A CG 1 ATOM 611 C CD . PRO A 1 89 ? 34.998 29.930 59.509 1.00 17.20 ? 90 PRO A CD 1 ATOM 612 N N . ALA A 1 90 ? 36.995 26.562 59.676 1.00 13.68 ? 91 ALA A N 1 ATOM 613 C CA . ALA A 1 90 ? 37.885 25.420 59.520 1.00 13.74 ? 91 ALA A CA 1 ATOM 614 C C . ALA A 1 90 ? 39.132 25.445 60.390 1.00 14.13 ? 91 ALA A C 1 ATOM 615 O O . ALA A 1 90 ? 39.877 24.450 60.404 1.00 13.45 ? 91 ALA A O 1 ATOM 616 C CB . ALA A 1 90 ? 38.300 25.272 58.058 1.00 15.38 ? 91 ALA A CB 1 ATOM 617 N N . ASN A 1 91 ? 39.335 26.520 61.155 1.00 13.29 ? 92 ASN A N 1 ATOM 618 C CA . ASN A 1 91 ? 40.571 26.659 61.957 1.00 12.92 ? 92 ASN A CA 1 ATOM 619 C C . ASN A 1 91 ? 40.441 26.536 63.427 1.00 13.65 ? 92 ASN A C 1 ATOM 620 O O . ASN A 1 91 ? 41.220 27.127 64.168 1.00 14.45 ? 92 ASN A O 1 ATOM 621 C CB . ASN A 1 91 ? 41.258 27.991 61.663 1.00 12.71 ? 92 ASN A CB 1 ATOM 622 C CG . ASN A 1 91 ? 42.012 27.971 60.356 1.00 13.61 ? 92 ASN A CG 1 ATOM 623 O OD1 . ASN A 1 91 ? 42.604 26.954 60.003 1.00 13.68 ? 92 ASN A OD1 1 ATOM 624 N ND2 . ASN A 1 91 ? 41.982 29.090 59.612 1.00 14.05 ? 92 ASN A ND2 1 ATOM 625 N N . GLY A 1 92 ? 39.445 25.787 63.863 1.00 14.76 ? 93 GLY A N 1 ATOM 626 C CA . GLY A 1 92 ? 39.235 25.599 65.296 1.00 15.46 ? 93 GLY A CA 1 ATOM 627 C C . GLY A 1 92 ? 40.184 24.572 65.888 1.00 15.10 ? 93 GLY A C 1 ATOM 628 O O . GLY A 1 92 ? 40.707 23.726 65.150 1.00 15.71 ? 93 GLY A O 1 ATOM 629 N N . GLY A 1 93 ? 40.418 24.678 67.197 1.00 14.56 ? 94 GLY A N 1 ATOM 630 C CA . GLY A 1 93 ? 41.305 23.765 67.911 1.00 17.16 ? 94 GLY A CA 1 ATOM 631 C C . GLY A 1 93 ? 42.785 23.894 67.567 1.00 17.22 ? 94 GLY A C 1 ATOM 632 O O . GLY A 1 93 ? 43.552 22.953 67.759 1.00 17.06 ? 94 GLY A O 1 ATOM 633 N N . LEU A 1 94 ? 43.190 25.095 67.149 1.00 16.99 ? 95 LEU A N 1 ATOM 634 C CA . LEU A 1 94 ? 44.557 25.384 66.735 1.00 16.84 ? 95 LEU A CA 1 ATOM 635 C C . LEU A 1 94 ? 45.271 26.460 67.539 1.00 18.13 ? 95 LEU A C 1 ATOM 636 O O . LEU A 1 94 ? 46.491 26.569 67.468 1.00 19.41 ? 95 LEU A O 1 ATOM 637 C CB . LEU A 1 94 ? 44.573 25.786 65.259 1.00 14.01 ? 95 LEU A CB 1 ATOM 638 C CG . LEU A 1 94 ? 44.125 24.689 64.288 1.00 15.86 ? 95 LEU A CG 1 ATOM 639 C CD1 . LEU A 1 94 ? 44.152 25.238 62.851 1.00 15.78 ? 95 LEU A CD1 1 ATOM 640 C CD2 . LEU A 1 94 ? 45.031 23.421 64.431 1.00 13.58 ? 95 LEU A CD2 1 ATOM 641 N N . THR A 1 95 ? 44.521 27.266 68.280 1.00 18.95 ? 96 THR A N 1 ATOM 642 C CA . THR A 1 95 ? 45.102 28.343 69.072 1.00 20.98 ? 96 THR A CA 1 ATOM 643 C C . THR A 1 95 ? 46.401 27.993 69.805 1.00 20.77 ? 96 THR A C 1 ATOM 644 O O . THR A 1 95 ? 47.427 28.604 69.564 1.00 20.72 ? 96 THR A O 1 ATOM 645 C CB . THR A 1 95 ? 44.074 28.848 70.103 1.00 24.49 ? 96 THR A CB 1 ATOM 646 O OG1 . THR A 1 95 ? 42.841 29.139 69.426 1.00 28.73 ? 96 THR A OG1 1 ATOM 647 C CG2 . THR A 1 95 ? 44.576 30.106 70.814 1.00 24.95 ? 96 THR A CG2 1 ATOM 648 N N . ASP A 1 96 ? 46.340 27.007 70.695 1.00 22.21 ? 97 ASP A N 1 ATOM 649 C CA . ASP A 1 96 ? 47.484 26.581 71.519 1.00 23.10 ? 97 ASP A CA 1 ATOM 650 C C . ASP A 1 96 ? 48.688 26.157 70.706 1.00 20.82 ? 97 ASP A C 1 ATOM 651 O O . ASP A 1 96 ? 49.824 26.391 71.103 1.00 21.65 ? 97 ASP A O 1 ATOM 652 C CB . ASP A 1 96 ? 47.091 25.410 72.443 1.00 27.89 ? 97 ASP A CB 1 ATOM 653 C CG . ASP A 1 96 ? 46.527 25.853 73.800 1.00 33.72 ? 97 ASP A CG 1 ATOM 654 O OD1 . ASP A 1 96 ? 45.999 26.990 73.947 1.00 35.69 ? 97 ASP A OD1 1 ATOM 655 O OD2 . ASP A 1 96 ? 46.621 25.023 74.746 1.00 39.06 ? 97 ASP A OD2 1 ATOM 656 N N . THR A 1 97 ? 48.445 25.490 69.593 1.00 18.91 ? 98 THR A N 1 ATOM 657 C CA . THR A 1 97 ? 49.551 25.055 68.759 1.00 17.38 ? 98 THR A CA 1 ATOM 658 C C . THR A 1 97 ? 50.169 26.286 68.101 1.00 17.71 ? 98 THR A C 1 ATOM 659 O O . THR A 1 97 ? 51.395 26.406 68.040 1.00 16.05 ? 98 THR A O 1 ATOM 660 C CB . THR A 1 97 ? 49.071 24.053 67.682 1.00 17.79 ? 98 THR A CB 1 ATOM 661 O OG1 . THR A 1 97 ? 48.507 22.915 68.333 1.00 16.32 ? 98 THR A OG1 1 ATOM 662 C CG2 . THR A 1 97 ? 50.214 23.613 66.785 1.00 14.59 ? 98 THR A CG2 1 ATOM 663 N N . VAL A 1 98 ? 49.326 27.178 67.582 1.00 16.49 ? 99 VAL A N 1 ATOM 664 C CA . VAL A 1 98 ? 49.800 28.411 66.944 1.00 15.42 ? 99 VAL A CA 1 ATOM 665 C C . VAL A 1 98 ? 50.601 29.283 67.919 1.00 15.84 ? 99 VAL A C 1 ATOM 666 O O . VAL A 1 98 ? 51.625 29.840 67.539 1.00 16.69 ? 99 VAL A O 1 ATOM 667 C CB . VAL A 1 98 ? 48.625 29.227 66.328 1.00 14.87 ? 99 VAL A CB 1 ATOM 668 C CG1 . VAL A 1 98 ? 49.043 30.692 66.063 1.00 13.11 ? 99 VAL A CG1 1 ATOM 669 C CG2 . VAL A 1 98 ? 48.194 28.573 65.028 1.00 12.08 ? 99 VAL A CG2 1 ATOM 670 N N . GLU A 1 99 ? 50.199 29.350 69.184 1.00 15.32 ? 100 GLU A N 1 ATOM 671 C CA . GLU A 1 99 ? 50.956 30.171 70.122 1.00 18.93 ? 100 GLU A CA 1 ATOM 672 C C . GLU A 1 99 ? 52.291 29.528 70.463 1.00 20.58 ? 100 GLU A C 1 ATOM 673 O O . GLU A 1 99 ? 53.293 30.223 70.676 1.00 20.47 ? 100 GLU A O 1 ATOM 674 C CB . GLU A 1 99 ? 50.159 30.460 71.380 1.00 21.24 ? 100 GLU A CB 1 ATOM 675 C CG . GLU A 1 99 ? 48.981 31.375 71.113 1.00 25.85 ? 100 GLU A CG 1 ATOM 676 C CD . GLU A 1 99 ? 49.386 32.638 70.389 1.00 29.21 ? 100 GLU A CD 1 ATOM 677 O OE1 . GLU A 1 99 ? 50.374 33.273 70.821 1.00 31.20 ? 100 GLU A OE1 1 ATOM 678 O OE2 . GLU A 1 99 ? 48.726 32.988 69.383 1.00 32.06 ? 100 GLU A OE2 1 ATOM 679 N N . ALA A 1 100 ? 52.300 28.202 70.526 1.00 19.55 ? 101 ALA A N 1 ATOM 680 C CA . ALA A 1 100 ? 53.530 27.473 70.774 1.00 19.39 ? 101 ALA A CA 1 ATOM 681 C C . ALA A 1 100 ? 54.501 27.756 69.626 1.00 19.45 ? 101 ALA A C 1 ATOM 682 O O . ALA A 1 100 ? 55.677 28.045 69.855 1.00 21.73 ? 101 ALA A O 1 ATOM 683 C CB . ALA A 1 100 ? 53.248 25.973 70.863 1.00 19.35 ? 101 ALA A CB 1 ATOM 684 N N . LEU A 1 101 ? 54.025 27.676 68.390 1.00 17.81 ? 102 LEU A N 1 ATOM 685 C CA . LEU A 1 101 ? 54.884 27.930 67.230 1.00 18.02 ? 102 LEU A CA 1 ATOM 686 C C . LEU A 1 101 ? 55.333 29.394 67.140 1.00 19.99 ? 102 LEU A C 1 ATOM 687 O O . LEU A 1 101 ? 56.462 29.679 66.714 1.00 19.30 ? 102 LEU A O 1 ATOM 688 C CB . LEU A 1 101 ? 54.172 27.517 65.933 1.00 16.48 ? 102 LEU A CB 1 ATOM 689 C CG . LEU A 1 101 ? 54.549 26.230 65.173 1.00 20.42 ? 102 LEU A CG 1 ATOM 690 C CD1 . LEU A 1 101 ? 55.118 25.167 66.051 1.00 15.66 ? 102 LEU A CD1 1 ATOM 691 C CD2 . LEU A 1 101 ? 53.339 25.728 64.390 1.00 18.75 ? 102 LEU A CD2 1 ATOM 692 N N . ARG A 1 102 ? 54.443 30.319 67.500 1.00 18.65 ? 103 ARG A N 1 ATOM 693 C CA . ARG A 1 102 ? 54.763 31.751 67.463 1.00 18.52 ? 103 ARG A CA 1 ATOM 694 C C . ARG A 1 102 ? 56.012 32.032 68.302 1.00 17.55 ? 103 ARG A C 1 ATOM 695 O O . ARG A 1 102 ? 56.914 32.767 67.873 1.00 17.03 ? 103 ARG A O 1 ATOM 696 C CB . ARG A 1 102 ? 53.589 32.584 68.009 1.00 18.63 ? 103 ARG A CB 1 ATOM 697 C CG . ARG A 1 102 ? 53.767 34.094 67.833 1.00 19.15 ? 103 ARG A CG 1 ATOM 698 C CD . ARG A 1 102 ? 52.826 34.882 68.750 1.00 19.91 ? 103 ARG A CD 1 ATOM 699 N NE . ARG A 1 102 ? 51.426 34.565 68.478 1.00 20.34 ? 103 ARG A NE 1 ATOM 700 C CZ . ARG A 1 102 ? 50.783 34.856 67.349 1.00 19.25 ? 103 ARG A CZ 1 ATOM 701 N NH1 . ARG A 1 102 ? 51.379 35.497 66.362 1.00 15.24 ? 103 ARG A NH1 1 ATOM 702 N NH2 . ARG A 1 102 ? 49.551 34.412 67.174 1.00 20.48 ? 103 ARG A NH2 1 ATOM 703 N N . ALA A 1 103 ? 56.066 31.417 69.480 1.00 17.23 ? 104 ALA A N 1 ATOM 704 C CA . ALA A 1 103 ? 57.187 31.597 70.386 1.00 17.88 ? 104 ALA A CA 1 ATOM 705 C C . ALA A 1 103 ? 58.491 31.024 69.849 1.00 17.72 ? 104 ALA A C 1 ATOM 706 O O . ALA A 1 103 ? 59.522 31.689 69.922 1.00 18.60 ? 104 ALA A O 1 ATOM 707 C CB . ALA A 1 103 ? 56.865 31.042 71.771 1.00 17.66 ? 104 ALA A CB 1 ATOM 708 N N . VAL A 1 104 ? 58.473 29.841 69.246 1.00 17.34 ? 105 VAL A N 1 ATOM 709 C CA . VAL A 1 104 ? 59.743 29.336 68.747 1.00 18.87 ? 105 VAL A CA 1 ATOM 710 C C . VAL A 1 104 ? 60.308 30.165 67.584 1.00 17.76 ? 105 VAL A C 1 ATOM 711 O O . VAL A 1 104 ? 61.511 30.443 67.541 1.00 17.44 ? 105 VAL A O 1 ATOM 712 C CB . VAL A 1 104 ? 59.790 27.767 68.500 1.00 19.08 ? 105 VAL A CB 1 ATOM 713 C CG1 . VAL A 1 104 ? 58.670 27.051 69.170 1.00 17.88 ? 105 VAL A CG1 1 ATOM 714 C CG2 . VAL A 1 104 ? 59.941 27.419 67.064 1.00 20.10 ? 105 VAL A CG2 1 ATOM 715 N N . GLY A 1 105 ? 59.451 30.614 66.678 1.00 17.82 ? 106 GLY A N 1 ATOM 716 C CA . GLY A 1 105 ? 59.920 31.417 65.558 1.00 20.31 ? 106 GLY A CA 1 ATOM 717 C C . GLY A 1 105 ? 60.515 32.751 66.000 1.00 22.44 ? 106 GLY A C 1 ATOM 718 O O . GLY A 1 105 ? 61.517 33.226 65.450 1.00 24.22 ? 106 GLY A O 1 ATOM 719 N N . ILE A 1 106 ? 59.855 33.381 66.958 1.00 23.02 ? 107 ILE A N 1 ATOM 720 C CA . ILE A 1 106 ? 60.297 34.646 67.512 1.00 25.03 ? 107 ILE A CA 1 ATOM 721 C C . ILE A 1 106 ? 61.652 34.450 68.205 1.00 27.15 ? 107 ILE A C 1 ATOM 722 O O . ILE A 1 106 ? 62.578 35.218 67.945 1.00 28.45 ? 107 ILE A O 1 ATOM 723 C CB . ILE A 1 106 ? 59.219 35.200 68.476 1.00 25.98 ? 107 ILE A CB 1 ATOM 724 C CG1 . ILE A 1 106 ? 58.093 35.812 67.658 1.00 24.89 ? 107 ILE A CG1 1 ATOM 725 C CG2 . ILE A 1 106 ? 59.777 36.238 69.446 1.00 27.74 ? 107 ILE A CG2 1 ATOM 726 C CD1 . ILE A 1 106 ? 56.952 36.262 68.496 1.00 26.12 ? 107 ILE A CD1 1 ATOM 727 N N . ASN A 1 107 ? 61.783 33.398 69.024 1.00 27.26 ? 108 ASN A N 1 ATOM 728 C CA . ASN A 1 107 ? 63.040 33.091 69.733 1.00 27.67 ? 108 ASN A CA 1 ATOM 729 C C . ASN A 1 107 ? 64.215 32.800 68.811 1.00 25.39 ? 108 ASN A C 1 ATOM 730 O O . ASN A 1 107 ? 65.333 33.192 69.098 1.00 25.73 ? 108 ASN A O 1 ATOM 731 C CB . ASN A 1 107 ? 62.895 31.885 70.677 1.00 32.85 ? 108 ASN A CB 1 ATOM 732 C CG . ASN A 1 107 ? 61.917 32.137 71.816 1.00 39.35 ? 108 ASN A CG 1 ATOM 733 O OD1 . ASN A 1 107 ? 61.953 33.194 72.466 1.00 42.23 ? 108 ASN A OD1 1 ATOM 734 N ND2 . ASN A 1 107 ? 61.001 31.188 72.037 1.00 42.13 ? 108 ASN A ND2 1 ATOM 735 N N . HIS A 1 108 ? 63.981 32.095 67.717 1.00 21.92 ? 109 HIS A N 1 ATOM 736 C CA . HIS A 1 108 ? 65.067 31.760 66.827 1.00 22.03 ? 109 HIS A CA 1 ATOM 737 C C . HIS A 1 108 ? 65.248 32.693 65.661 1.00 22.24 ? 109 HIS A C 1 ATOM 738 O O . HIS A 1 108 ? 66.186 32.540 64.888 1.00 22.03 ? 109 HIS A O 1 ATOM 739 C CB . HIS A 1 108 ? 64.938 30.316 66.355 1.00 22.63 ? 109 HIS A CB 1 ATOM 740 C CG . HIS A 1 108 ? 65.059 29.325 67.465 1.00 22.14 ? 109 HIS A CG 1 ATOM 741 N ND1 . HIS A 1 108 ? 66.262 28.797 67.858 1.00 23.43 ? 109 HIS A ND1 1 ATOM 742 C CD2 . HIS A 1 108 ? 64.132 28.821 68.315 1.00 24.50 ? 109 HIS A CD2 1 ATOM 743 C CE1 . HIS A 1 108 ? 66.083 28.018 68.909 1.00 24.14 ? 109 HIS A CE1 1 ATOM 744 N NE2 . HIS A 1 108 ? 64.797 28.014 69.205 1.00 23.53 ? 109 HIS A NE2 1 ATOM 745 N N . GLY A 1 109 ? 64.326 33.636 65.511 1.00 23.14 ? 110 GLY A N 1 ATOM 746 C CA . GLY A 1 109 ? 64.417 34.611 64.441 1.00 20.51 ? 110 GLY A CA 1 ATOM 747 C C . GLY A 1 109 ? 64.255 34.028 63.071 1.00 19.84 ? 110 GLY A C 1 ATOM 748 O O . GLY A 1 109 ? 64.937 34.435 62.122 1.00 22.75 ? 110 GLY A O 1 ATOM 749 N N . VAL A 1 110 ? 63.336 33.076 62.952 1.00 19.62 ? 111 VAL A N 1 ATOM 750 C CA . VAL A 1 110 ? 63.057 32.434 61.661 1.00 17.12 ? 111 VAL A CA 1 ATOM 751 C C . VAL A 1 110 ? 61.641 32.884 61.246 1.00 14.74 ? 111 VAL A C 1 ATOM 752 O O . VAL A 1 110 ? 60.810 33.154 62.109 1.00 14.42 ? 111 VAL A O 1 ATOM 753 C CB . VAL A 1 110 ? 63.181 30.830 61.759 1.00 15.06 ? 111 VAL A CB 1 ATOM 754 C CG1 . VAL A 1 110 ? 64.643 30.428 62.078 1.00 16.43 ? 111 VAL A CG1 1 ATOM 755 C CG2 . VAL A 1 110 ? 62.279 30.263 62.866 1.00 13.28 ? 111 VAL A CG2 1 ATOM 756 N N . SER A 1 111 ? 61.376 32.978 59.946 1.00 15.05 ? 112 SER A N 1 ATOM 757 C CA . SER A 1 111 ? 60.047 33.401 59.505 1.00 18.00 ? 112 SER A CA 1 ATOM 758 C C . SER A 1 111 ? 58.987 32.370 59.857 1.00 19.15 ? 112 SER A C 1 ATOM 759 O O . SER A 1 111 ? 59.276 31.166 59.885 1.00 19.72 ? 112 SER A O 1 ATOM 760 C CB . SER A 1 111 ? 59.991 33.693 58.012 1.00 14.59 ? 112 SER A CB 1 ATOM 761 O OG . SER A 1 111 ? 60.221 32.548 57.229 1.00 15.92 ? 112 SER A OG 1 ATOM 762 N N . PHE A 1 112 ? 57.774 32.844 60.145 1.00 17.15 ? 113 PHE A N 1 ATOM 763 C CA . PHE A 1 112 ? 56.657 31.969 60.479 1.00 16.41 ? 113 PHE A CA 1 ATOM 764 C C . PHE A 1 112 ? 56.369 30.966 59.346 1.00 14.72 ? 113 PHE A C 1 ATOM 765 O O . PHE A 1 112 ? 56.025 29.818 59.609 1.00 15.89 ? 113 PHE A O 1 ATOM 766 C CB . PHE A 1 112 ? 55.412 32.808 60.786 1.00 16.84 ? 113 PHE A CB 1 ATOM 767 C CG . PHE A 1 112 ? 55.508 33.637 62.054 1.00 16.18 ? 113 PHE A CG 1 ATOM 768 C CD1 . PHE A 1 112 ? 56.217 33.188 63.162 1.00 16.23 ? 113 PHE A CD1 1 ATOM 769 C CD2 . PHE A 1 112 ? 54.780 34.812 62.180 1.00 17.18 ? 113 PHE A CD2 1 ATOM 770 C CE1 . PHE A 1 112 ? 56.184 33.896 64.375 1.00 14.79 ? 113 PHE A CE1 1 ATOM 771 C CE2 . PHE A 1 112 ? 54.753 35.502 63.386 1.00 16.17 ? 113 PHE A CE2 1 ATOM 772 C CZ . PHE A 1 112 ? 55.456 35.035 64.478 1.00 13.57 ? 113 PHE A CZ 1 ATOM 773 N N . GLY A 1 113 ? 56.569 31.388 58.106 1.00 14.88 ? 114 GLY A N 1 ATOM 774 C CA . GLY A 1 113 ? 56.366 30.533 56.934 1.00 16.15 ? 114 GLY A CA 1 ATOM 775 C C . GLY A 1 113 ? 57.349 29.356 56.829 1.00 16.94 ? 114 GLY A C 1 ATOM 776 O O . GLY A 1 113 ? 56.943 28.227 56.537 1.00 14.21 ? 114 GLY A O 1 ATOM 777 N N . ASP A 1 114 ? 58.636 29.610 57.056 1.00 15.00 ? 115 ASP A N 1 ATOM 778 C CA . ASP A 1 114 ? 59.641 28.556 57.041 1.00 14.07 ? 115 ASP A CA 1 ATOM 779 C C . ASP A 1 114 ? 59.413 27.631 58.222 1.00 11.33 ? 115 ASP A C 1 ATOM 780 O O . ASP A 1 114 ? 59.583 26.427 58.117 1.00 12.66 ? 115 ASP A O 1 ATOM 781 C CB . ASP A 1 114 ? 61.043 29.147 57.256 1.00 14.56 ? 115 ASP A CB 1 ATOM 782 C CG . ASP A 1 114 ? 61.601 29.811 56.035 1.00 16.68 ? 115 ASP A CG 1 ATOM 783 O OD1 . ASP A 1 114 ? 60.988 29.740 54.973 1.00 17.75 ? 115 ASP A OD1 1 ATOM 784 O OD2 . ASP A 1 114 ? 62.697 30.386 56.120 1.00 21.60 ? 115 ASP A OD2 1 ATOM 785 N N . LEU A 1 115 ? 59.108 28.216 59.381 1.00 10.06 ? 116 LEU A N 1 ATOM 786 C CA . LEU A 1 115 ? 58.926 27.453 60.602 1.00 11.36 ? 116 LEU A CA 1 ATOM 787 C C . LEU A 1 115 ? 57.830 26.403 60.484 1.00 13.71 ? 116 LEU A C 1 ATOM 788 O O . LEU A 1 115 ? 57.965 25.304 61.020 1.00 11.91 ? 116 LEU A O 1 ATOM 789 C CB . LEU A 1 115 ? 58.640 28.365 61.791 1.00 10.28 ? 116 LEU A CB 1 ATOM 790 C CG . LEU A 1 115 ? 58.410 27.593 63.093 1.00 14.00 ? 116 LEU A CG 1 ATOM 791 C CD1 . LEU A 1 115 ? 59.646 26.772 63.472 1.00 14.44 ? 116 LEU A CD1 1 ATOM 792 C CD2 . LEU A 1 115 ? 57.986 28.534 64.206 1.00 13.33 ? 116 LEU A CD2 1 ATOM 793 N N . ILE A 1 116 ? 56.721 26.777 59.843 1.00 14.00 ? 117 ILE A N 1 ATOM 794 C CA . ILE A 1 116 ? 55.610 25.852 59.663 1.00 15.42 ? 117 ILE A CA 1 ATOM 795 C C . ILE A 1 116 ? 56.044 24.672 58.804 1.00 14.19 ? 117 ILE A C 1 ATOM 796 O O . ILE A 1 116 ? 55.735 23.525 59.131 1.00 15.68 ? 117 ILE A O 1 ATOM 797 C CB . ILE A 1 116 ? 54.342 26.576 59.073 1.00 15.04 ? 117 ILE A CB 1 ATOM 798 C CG1 . ILE A 1 116 ? 53.765 27.513 60.151 1.00 13.18 ? 117 ILE A CG1 1 ATOM 799 C CG2 . ILE A 1 116 ? 53.260 25.553 58.668 1.00 13.96 ? 117 ILE A CG2 1 ATOM 800 C CD1 . ILE A 1 116 ? 52.603 28.371 59.677 1.00 14.08 ? 117 ILE A CD1 1 ATOM 801 N N . GLN A 1 117 ? 56.782 24.933 57.727 1.00 13.11 ? 118 GLN A N 1 ATOM 802 C CA . GLN A 1 117 ? 57.250 23.858 56.851 1.00 12.46 ? 118 GLN A CA 1 ATOM 803 C C . GLN A 1 117 ? 58.259 22.978 57.573 1.00 11.93 ? 118 GLN A C 1 ATOM 804 O O . GLN A 1 117 ? 58.147 21.762 57.525 1.00 14.84 ? 118 GLN A O 1 ATOM 805 C CB . GLN A 1 117 ? 57.822 24.411 55.553 1.00 12.13 ? 118 GLN A CB 1 ATOM 806 C CG . GLN A 1 117 ? 56.799 25.231 54.783 1.00 18.63 ? 118 GLN A CG 1 ATOM 807 C CD . GLN A 1 117 ? 55.612 24.411 54.301 1.00 21.21 ? 118 GLN A CD 1 ATOM 808 O OE1 . GLN A 1 117 ? 55.730 23.214 54.076 1.00 24.98 ? 118 GLN A OE1 1 ATOM 809 N NE2 . GLN A 1 117 ? 54.486 25.063 54.090 1.00 21.30 ? 118 GLN A NE2 1 ATOM 810 N N . PHE A 1 118 ? 59.165 23.587 58.338 1.00 12.82 ? 119 PHE A N 1 ATOM 811 C CA . PHE A 1 118 ? 60.160 22.844 59.096 1.00 12.97 ? 119 PHE A CA 1 ATOM 812 C C . PHE A 1 118 ? 59.485 21.980 60.150 1.00 14.53 ? 119 PHE A C 1 ATOM 813 O O . PHE A 1 118 ? 59.810 20.804 60.262 1.00 13.98 ? 119 PHE A O 1 ATOM 814 C CB . PHE A 1 118 ? 61.135 23.796 59.793 1.00 12.05 ? 119 PHE A CB 1 ATOM 815 C CG . PHE A 1 118 ? 62.300 23.109 60.468 1.00 10.95 ? 119 PHE A CG 1 ATOM 816 C CD1 . PHE A 1 118 ? 62.373 23.030 61.849 1.00 10.59 ? 119 PHE A CD1 1 ATOM 817 C CD2 . PHE A 1 118 ? 63.347 22.588 59.710 1.00 11.26 ? 119 PHE A CD2 1 ATOM 818 C CE1 . PHE A 1 118 ? 63.482 22.438 62.475 1.00 13.00 ? 119 PHE A CE1 1 ATOM 819 C CE2 . PHE A 1 118 ? 64.456 21.993 60.317 1.00 10.02 ? 119 PHE A CE2 1 ATOM 820 C CZ . PHE A 1 118 ? 64.524 21.917 61.687 1.00 11.41 ? 119 PHE A CZ 1 ATOM 821 N N . ALA A 1 119 ? 58.591 22.558 60.962 1.00 12.99 ? 120 ALA A N 1 ATOM 822 C CA . ALA A 1 119 ? 57.922 21.784 61.997 1.00 12.43 ? 120 ALA A CA 1 ATOM 823 C C . ALA A 1 119 ? 57.150 20.589 61.421 1.00 12.41 ? 120 ALA A C 1 ATOM 824 O O . ALA A 1 119 ? 57.116 19.521 62.011 1.00 12.52 ? 120 ALA A O 1 ATOM 825 C CB . ALA A 1 119 ? 57.041 22.668 62.878 1.00 11.06 ? 120 ALA A CB 1 ATOM 826 N N . THR A 1 120 ? 56.616 20.750 60.219 1.00 14.12 ? 121 THR A N 1 ATOM 827 C CA . THR A 1 120 ? 55.887 19.684 59.527 1.00 13.36 ? 121 THR A CA 1 ATOM 828 C C . THR A 1 120 ? 56.851 18.498 59.189 1.00 14.85 ? 121 THR A C 1 ATOM 829 O O . THR A 1 120 ? 56.576 17.325 59.531 1.00 12.90 ? 121 THR A O 1 ATOM 830 C CB . THR A 1 120 ? 55.236 20.241 58.222 1.00 12.73 ? 121 THR A CB 1 ATOM 831 O OG1 . THR A 1 120 ? 54.207 21.188 58.560 1.00 12.76 ? 121 THR A OG1 1 ATOM 832 C CG2 . THR A 1 120 ? 54.643 19.116 57.390 1.00 14.09 ? 121 THR A CG2 1 ATOM 833 N N . ALA A 1 121 ? 57.973 18.827 58.538 1.00 13.90 ? 122 ALA A N 1 ATOM 834 C CA . ALA A 1 121 ? 58.992 17.842 58.148 1.00 14.29 ? 122 ALA A CA 1 ATOM 835 C C . ALA A 1 121 ? 59.592 17.163 59.376 1.00 15.60 ? 122 ALA A C 1 ATOM 836 O O . ALA A 1 121 ? 59.781 15.934 59.397 1.00 19.08 ? 122 ALA A O 1 ATOM 837 C CB . ALA A 1 121 ? 60.074 18.512 57.317 1.00 14.39 ? 122 ALA A CB 1 ATOM 838 N N . VAL A 1 122 ? 59.842 17.935 60.427 1.00 15.41 ? 123 VAL A N 1 ATOM 839 C CA . VAL A 1 122 ? 60.393 17.361 61.637 1.00 14.39 ? 123 VAL A CA 1 ATOM 840 C C . VAL A 1 122 ? 59.376 16.464 62.339 1.00 15.84 ? 123 VAL A C 1 ATOM 841 O O . VAL A 1 122 ? 59.703 15.364 62.745 1.00 15.44 ? 123 VAL A O 1 ATOM 842 C CB . VAL A 1 122 ? 60.851 18.441 62.611 1.00 14.84 ? 123 VAL A CB 1 ATOM 843 C CG1 . VAL A 1 122 ? 61.208 17.819 63.929 1.00 12.48 ? 123 VAL A CG1 1 ATOM 844 C CG2 . VAL A 1 122 ? 62.059 19.152 62.057 1.00 14.24 ? 123 VAL A CG2 1 ATOM 845 N N . GLY A 1 123 ? 58.170 16.969 62.537 1.00 13.03 ? 124 GLY A N 1 ATOM 846 C CA . GLY A 1 123 ? 57.133 16.209 63.198 1.00 12.45 ? 124 GLY A CA 1 ATOM 847 C C . GLY A 1 123 ? 56.886 14.892 62.502 1.00 12.69 ? 124 GLY A C 1 ATOM 848 O O . GLY A 1 123 ? 56.733 13.870 63.161 1.00 13.57 ? 124 GLY A O 1 ATOM 849 N N . MET A 1 124 ? 56.840 14.891 61.176 1.00 13.75 ? 125 MET A N 1 ATOM 850 C CA . MET A 1 124 ? 56.613 13.637 60.481 1.00 15.89 ? 125 MET A CA 1 ATOM 851 C C . MET A 1 124 ? 57.730 12.590 60.663 1.00 18.74 ? 125 MET A C 1 ATOM 852 O O . MET A 1 124 ? 57.467 11.375 60.618 1.00 16.58 ? 125 MET A O 1 ATOM 853 C CB . MET A 1 124 ? 56.339 13.881 59.015 1.00 14.79 ? 125 MET A CB 1 ATOM 854 C CG . MET A 1 124 ? 54.955 14.466 58.804 1.00 18.36 ? 125 MET A CG 1 ATOM 855 S SD . MET A 1 124 ? 54.423 14.103 57.204 1.00 23.22 ? 125 MET A SD 1 ATOM 856 C CE . MET A 1 124 ? 53.756 12.484 57.448 1.00 16.23 ? 125 MET A CE 1 ATOM 857 N N . SER A 1 125 ? 58.958 13.057 60.918 1.00 17.49 ? 126 SER A N 1 ATOM 858 C CA . SER A 1 125 ? 60.073 12.146 61.106 1.00 17.37 ? 126 SER A CA 1 ATOM 859 C C . SER A 1 125 ? 59.859 11.330 62.365 1.00 16.90 ? 126 SER A C 1 ATOM 860 O O . SER A 1 125 ? 60.455 10.263 62.517 1.00 18.72 ? 126 SER A O 1 ATOM 861 C CB . SER A 1 125 ? 61.406 12.911 61.167 1.00 16.70 ? 126 SER A CB 1 ATOM 862 O OG . SER A 1 125 ? 61.616 13.489 62.446 1.00 16.93 ? 126 SER A OG 1 ATOM 863 N N . ASN A 1 126 ? 58.997 11.808 63.265 1.00 17.05 ? 127 ASN A N 1 ATOM 864 C CA . ASN A 1 126 ? 58.705 11.104 64.519 1.00 16.17 ? 127 ASN A CA 1 ATOM 865 C C . ASN A 1 126 ? 57.681 9.979 64.384 1.00 16.89 ? 127 ASN A C 1 ATOM 866 O O . ASN A 1 126 ? 57.444 9.232 65.340 1.00 18.82 ? 127 ASN A O 1 ATOM 867 C CB . ASN A 1 126 ? 58.192 12.070 65.580 1.00 16.24 ? 127 ASN A CB 1 ATOM 868 C CG . ASN A 1 126 ? 59.174 13.170 65.892 1.00 20.01 ? 127 ASN A CG 1 ATOM 869 O OD1 . ASN A 1 126 ? 58.786 14.277 66.284 1.00 17.19 ? 127 ASN A OD1 1 ATOM 870 N ND2 . ASN A 1 126 ? 60.464 12.862 65.770 1.00 19.59 ? 127 ASN A ND2 1 ATOM 871 N N . CYS A 1 127 ? 57.066 9.878 63.213 1.00 15.87 ? 128 CYS A N 1 ATOM 872 C CA . CYS A 1 127 ? 56.057 8.856 62.955 1.00 14.56 ? 128 CYS A CA 1 ATOM 873 C C . CYS A 1 127 ? 56.585 7.779 62.001 1.00 14.66 ? 128 CYS A C 1 ATOM 874 O O . CYS A 1 127 ? 56.900 8.065 60.860 1.00 14.95 ? 128 CYS A O 1 ATOM 875 C CB . CYS A 1 127 ? 54.823 9.528 62.358 1.00 16.64 ? 128 CYS A CB 1 ATOM 876 S SG . CYS A 1 127 ? 54.248 10.990 63.299 1.00 16.28 ? 128 CYS A SG 1 ATOM 877 N N . PRO A 1 128 ? 56.676 6.515 62.460 1.00 14.17 ? 129 PRO A N 1 ATOM 878 C CA . PRO A 1 128 ? 57.170 5.415 61.635 1.00 14.02 ? 129 PRO A CA 1 ATOM 879 C C . PRO A 1 128 ? 56.484 5.384 60.295 1.00 13.28 ? 129 PRO A C 1 ATOM 880 O O . PRO A 1 128 ? 55.268 5.571 60.207 1.00 16.97 ? 129 PRO A O 1 ATOM 881 C CB . PRO A 1 128 ? 56.777 4.175 62.447 1.00 15.27 ? 129 PRO A CB 1 ATOM 882 C CG . PRO A 1 128 ? 56.875 4.625 63.826 1.00 14.56 ? 129 PRO A CG 1 ATOM 883 C CD . PRO A 1 128 ? 56.270 6.031 63.786 1.00 14.28 ? 129 PRO A CD 1 ATOM 884 N N . GLY A 1 129 ? 57.239 5.108 59.250 1.00 11.92 ? 130 GLY A N 1 ATOM 885 C CA . GLY A 1 129 ? 56.670 5.024 57.920 1.00 13.48 ? 130 GLY A CA 1 ATOM 886 C C . GLY A 1 129 ? 56.747 6.278 57.070 1.00 16.02 ? 130 GLY A C 1 ATOM 887 O O . GLY A 1 129 ? 56.656 6.195 55.847 1.00 16.24 ? 130 GLY A O 1 ATOM 888 N N . SER A 1 130 ? 56.935 7.438 57.697 1.00 18.48 ? 131 SER A N 1 ATOM 889 C CA . SER A 1 130 ? 56.977 8.705 56.968 1.00 17.42 ? 131 SER A CA 1 ATOM 890 C C . SER A 1 130 ? 58.155 8.907 56.049 1.00 16.49 ? 131 SER A C 1 ATOM 891 O O . SER A 1 130 ? 59.262 8.460 56.332 1.00 17.51 ? 131 SER A O 1 ATOM 892 C CB . SER A 1 130 ? 56.961 9.870 57.965 1.00 18.04 ? 131 SER A CB 1 ATOM 893 O OG . SER A 1 130 ? 55.892 9.739 58.891 1.00 20.67 ? 131 SER A OG 1 ATOM 894 N N . PRO A 1 131 ? 57.923 9.549 54.901 1.00 17.03 ? 132 PRO A N 1 ATOM 895 C CA . PRO A 1 131 ? 59.016 9.815 53.974 1.00 16.97 ? 132 PRO A CA 1 ATOM 896 C C . PRO A 1 131 ? 59.804 11.021 54.543 1.00 17.14 ? 132 PRO A C 1 ATOM 897 O O . PRO A 1 131 ? 59.412 11.624 55.533 1.00 16.18 ? 132 PRO A O 1 ATOM 898 C CB . PRO A 1 131 ? 58.284 10.183 52.680 1.00 18.09 ? 132 PRO A CB 1 ATOM 899 C CG . PRO A 1 131 ? 57.043 10.791 53.162 1.00 17.24 ? 132 PRO A CG 1 ATOM 900 C CD . PRO A 1 131 ? 56.628 9.904 54.298 1.00 15.99 ? 132 PRO A CD 1 ATOM 901 N N . ARG A 1 132 ? 60.911 11.389 53.917 1.00 18.21 ? 133 ARG A N 1 ATOM 902 C CA . ARG A 1 132 ? 61.690 12.504 54.428 1.00 20.03 ? 133 ARG A CA 1 ATOM 903 C C . ARG A 1 132 ? 61.309 13.689 53.583 1.00 16.76 ? 133 ARG A C 1 ATOM 904 O O . ARG A 1 132 ? 61.591 13.705 52.397 1.00 17.47 ? 133 ARG A O 1 ATOM 905 C CB . ARG A 1 132 ? 63.192 12.193 54.335 1.00 22.57 ? 133 ARG A CB 1 ATOM 906 C CG . ARG A 1 132 ? 63.961 12.566 55.604 1.00 28.00 ? 133 ARG A CG 1 ATOM 907 C CD . ARG A 1 132 ? 65.384 12.035 55.540 1.00 30.73 ? 133 ARG A CD 1 ATOM 908 N NE . ARG A 1 132 ? 66.028 12.440 54.302 1.00 32.82 ? 133 ARG A NE 1 ATOM 909 C CZ . ARG A 1 132 ? 66.913 13.420 54.233 1.00 35.09 ? 133 ARG A CZ 1 ATOM 910 N NH1 . ARG A 1 132 ? 67.259 14.076 55.332 1.00 35.29 ? 133 ARG A NH1 1 ATOM 911 N NH2 . ARG A 1 132 ? 67.405 13.783 53.061 1.00 36.86 ? 133 ARG A NH2 1 ATOM 912 N N . LEU A 1 133 ? 60.589 14.633 54.181 1.00 17.51 ? 134 LEU A N 1 ATOM 913 C CA . LEU A 1 133 ? 60.118 15.810 53.438 1.00 16.06 ? 134 LEU A CA 1 ATOM 914 C C . LEU A 1 133 ? 61.219 16.788 53.098 1.00 14.12 ? 134 LEU A C 1 ATOM 915 O O . LEU A 1 133 ? 62.122 17.027 53.893 1.00 15.04 ? 134 LEU A O 1 ATOM 916 C CB . LEU A 1 133 ? 58.994 16.560 54.201 1.00 16.32 ? 134 LEU A CB 1 ATOM 917 C CG . LEU A 1 133 ? 57.639 15.891 54.519 1.00 16.24 ? 134 LEU A CG 1 ATOM 918 C CD1 . LEU A 1 133 ? 56.583 16.928 54.968 1.00 13.23 ? 134 LEU A CD1 1 ATOM 919 C CD2 . LEU A 1 133 ? 57.169 15.142 53.275 1.00 15.63 ? 134 LEU A CD2 1 ATOM 920 N N . GLU A 1 134 ? 61.149 17.336 51.906 1.00 14.43 ? 135 GLU A N 1 ATOM 921 C CA . GLU A 1 134 ? 62.088 18.354 51.483 1.00 15.93 ? 135 GLU A CA 1 ATOM 922 C C . GLU A 1 134 ? 61.893 19.601 52.381 1.00 17.65 ? 135 GLU A C 1 ATOM 923 O O . GLU A 1 134 ? 60.786 19.875 52.877 1.00 15.07 ? 135 GLU A O 1 ATOM 924 C CB . GLU A 1 134 ? 61.787 18.701 50.021 1.00 16.94 ? 135 GLU A CB 1 ATOM 925 C CG . GLU A 1 134 ? 62.628 19.834 49.415 1.00 19.23 ? 135 GLU A CG 1 ATOM 926 C CD . GLU A 1 134 ? 62.098 20.293 48.076 1.00 19.92 ? 135 GLU A CD 1 ATOM 927 O OE1 . GLU A 1 134 ? 62.671 19.898 47.047 1.00 19.53 ? 135 GLU A OE1 1 ATOM 928 O OE2 . GLU A 1 134 ? 61.109 21.043 48.044 1.00 19.98 ? 135 GLU A OE2 1 ATOM 929 N N . PHE A 1 135 ? 62.974 20.336 52.637 1.00 19.11 ? 136 PHE A N 1 ATOM 930 C CA . PHE A 1 135 ? 62.888 21.562 53.452 1.00 19.80 ? 136 PHE A CA 1 ATOM 931 C C . PHE A 1 135 ? 63.675 22.731 52.831 1.00 20.68 ? 136 PHE A C 1 ATOM 932 O O . PHE A 1 135 ? 64.897 22.668 52.751 1.00 20.78 ? 136 PHE A O 1 ATOM 933 C CB . PHE A 1 135 ? 63.403 21.360 54.878 1.00 19.35 ? 136 PHE A CB 1 ATOM 934 C CG . PHE A 1 135 ? 63.382 22.640 55.708 1.00 19.00 ? 136 PHE A CG 1 ATOM 935 C CD1 . PHE A 1 135 ? 62.206 23.423 55.794 1.00 18.23 ? 136 PHE A CD1 1 ATOM 936 C CD2 . PHE A 1 135 ? 64.526 23.109 56.327 1.00 17.17 ? 136 PHE A CD2 1 ATOM 937 C CE1 . PHE A 1 135 ? 62.186 24.652 56.477 1.00 16.77 ? 136 PHE A CE1 1 ATOM 938 C CE2 . PHE A 1 135 ? 64.502 24.347 57.014 1.00 16.79 ? 136 PHE A CE2 1 ATOM 939 C CZ . PHE A 1 135 ? 63.332 25.110 57.082 1.00 16.40 ? 136 PHE A CZ 1 ATOM 940 N N . LEU A 1 136 ? 62.964 23.766 52.372 1.00 19.85 ? 137 LEU A N 1 ATOM 941 C CA . LEU A 1 136 ? 63.561 24.970 51.793 1.00 18.46 ? 137 LEU A CA 1 ATOM 942 C C . LEU A 1 136 ? 63.375 26.110 52.805 1.00 19.20 ? 137 LEU A C 1 ATOM 943 O O . LEU A 1 136 ? 62.381 26.141 53.527 1.00 20.18 ? 137 LEU A O 1 ATOM 944 C CB . LEU A 1 136 ? 62.853 25.327 50.505 1.00 18.78 ? 137 LEU A CB 1 ATOM 945 C CG . LEU A 1 136 ? 62.649 24.219 49.488 1.00 18.54 ? 137 LEU A CG 1 ATOM 946 C CD1 . LEU A 1 136 ? 61.983 24.821 48.273 1.00 19.67 ? 137 LEU A CD1 1 ATOM 947 C CD2 . LEU A 1 136 ? 63.980 23.615 49.103 1.00 20.97 ? 137 LEU A CD2 1 ATOM 948 N N . THR A 1 137 ? 64.349 27.015 52.899 1.00 18.01 ? 138 THR A N 1 ATOM 949 C CA . THR A 1 137 ? 64.291 28.138 53.826 1.00 18.39 ? 138 THR A CA 1 ATOM 950 C C . THR A 1 137 ? 64.436 29.466 53.049 1.00 21.04 ? 138 THR A C 1 ATOM 951 O O . THR A 1 137 ? 64.968 29.494 51.922 1.00 21.72 ? 138 THR A O 1 ATOM 952 C CB . THR A 1 137 ? 65.382 28.032 54.872 1.00 17.55 ? 138 THR A CB 1 ATOM 953 O OG1 . THR A 1 137 ? 65.247 29.097 55.817 1.00 19.66 ? 138 THR A OG1 1 ATOM 954 C CG2 . THR A 1 137 ? 66.753 28.093 54.212 1.00 18.02 ? 138 THR A CG2 1 ATOM 955 N N . GLY A 1 138 ? 63.926 30.555 53.619 1.00 20.51 ? 139 GLY A N 1 ATOM 956 C CA . GLY A 1 138 ? 64.022 31.823 52.928 1.00 21.35 ? 139 GLY A CA 1 ATOM 957 C C . GLY A 1 138 ? 62.722 32.582 52.692 1.00 22.44 ? 139 GLY A C 1 ATOM 958 O O . GLY A 1 138 ? 62.774 33.709 52.196 1.00 24.78 ? 139 GLY A O 1 ATOM 959 N N . ARG A 1 139 ? 61.562 31.991 53.005 1.00 18.94 ? 140 ARG A N 1 ATOM 960 C CA . ARG A 1 139 ? 60.299 32.693 52.811 1.00 16.36 ? 140 ARG A CA 1 ATOM 961 C C . ARG A 1 139 ? 60.288 33.941 53.694 1.00 16.89 ? 140 ARG A C 1 ATOM 962 O O . ARG A 1 139 ? 60.638 33.885 54.879 1.00 18.29 ? 140 ARG A O 1 ATOM 963 C CB . ARG A 1 139 ? 59.102 31.805 53.176 1.00 15.54 ? 140 ARG A CB 1 ATOM 964 C CG . ARG A 1 139 ? 58.876 30.617 52.230 1.00 13.61 ? 140 ARG A CG 1 ATOM 965 C CD . ARG A 1 139 ? 58.015 29.534 52.924 1.00 14.15 ? 140 ARG A CD 1 ATOM 966 N NE . ARG A 1 139 ? 58.026 28.268 52.195 1.00 13.55 ? 140 ARG A NE 1 ATOM 967 C CZ . ARG A 1 139 ? 58.924 27.314 52.396 1.00 13.72 ? 140 ARG A CZ 1 ATOM 968 N NH1 . ARG A 1 139 ? 59.878 27.491 53.296 1.00 13.61 ? 140 ARG A NH1 1 ATOM 969 N NH2 . ARG A 1 139 ? 58.837 26.162 51.748 1.00 10.71 ? 140 ARG A NH2 1 ATOM 970 N N . SER A 1 140 ? 59.884 35.063 53.106 1.00 18.71 ? 141 SER A N 1 ATOM 971 C CA . SER A 1 140 ? 59.796 36.325 53.830 1.00 19.14 ? 141 SER A CA 1 ATOM 972 C C . SER A 1 140 ? 58.916 36.155 55.055 1.00 18.52 ? 141 SER A C 1 ATOM 973 O O . SER A 1 140 ? 57.968 35.385 55.010 1.00 21.23 ? 141 SER A O 1 ATOM 974 C CB . SER A 1 140 ? 59.187 37.395 52.925 1.00 20.10 ? 141 SER A CB 1 ATOM 975 O OG . SER A 1 140 ? 58.689 38.469 53.724 1.00 25.12 ? 141 SER A OG 1 ATOM 976 N N . ASN A 1 141 ? 59.177 36.904 56.126 1.00 18.36 ? 142 ASN A N 1 ATOM 977 C CA . ASN A 1 141 ? 58.354 36.819 57.332 1.00 19.91 ? 142 ASN A CA 1 ATOM 978 C C . ASN A 1 141 ? 57.080 37.685 57.203 1.00 22.63 ? 142 ASN A C 1 ATOM 979 O O . ASN A 1 141 ? 56.154 37.548 58.005 1.00 22.69 ? 142 ASN A O 1 ATOM 980 C CB . ASN A 1 141 ? 59.141 37.280 58.553 1.00 18.94 ? 142 ASN A CB 1 ATOM 981 C CG . ASN A 1 141 ? 58.409 37.023 59.849 1.00 21.32 ? 142 ASN A CG 1 ATOM 982 O OD1 . ASN A 1 141 ? 57.927 35.920 60.101 1.00 19.56 ? 142 ASN A OD1 1 ATOM 983 N ND2 . ASN A 1 141 ? 58.308 38.049 60.685 1.00 23.63 ? 142 ASN A ND2 1 ATOM 984 N N . SER A 1 142 ? 57.031 38.556 56.194 1.00 22.16 ? 143 SER A N 1 ATOM 985 C CA . SER A 1 142 ? 55.864 39.422 56.021 1.00 25.07 ? 143 SER A CA 1 ATOM 986 C C . SER A 1 142 ? 54.748 38.705 55.273 1.00 22.96 ? 143 SER A C 1 ATOM 987 O O . SER A 1 142 ? 55.005 37.916 54.367 1.00 23.28 ? 143 SER A O 1 ATOM 988 C CB . SER A 1 142 ? 56.236 40.722 55.290 1.00 29.19 ? 143 SER A CB 1 ATOM 989 O OG . SER A 1 142 ? 56.570 40.475 53.925 1.00 36.44 ? 143 SER A OG 1 ATOM 990 N N . SER A 1 143 ? 53.509 38.985 55.661 1.00 21.49 ? 144 SER A N 1 ATOM 991 C CA . SER A 1 143 ? 52.344 38.366 55.033 1.00 21.09 ? 144 SER A CA 1 ATOM 992 C C . SER A 1 143 ? 51.082 39.183 55.341 1.00 20.87 ? 144 SER A C 1 ATOM 993 O O . SER A 1 143 ? 51.074 40.018 56.263 1.00 19.41 ? 144 SER A O 1 ATOM 994 C CB . SER A 1 143 ? 52.160 36.951 55.587 1.00 19.14 ? 144 SER A CB 1 ATOM 995 O OG . SER A 1 143 ? 51.881 37.027 56.974 1.00 20.11 ? 144 SER A OG 1 ATOM 996 N N . GLN A 1 144 ? 50.034 38.943 54.558 1.00 20.44 ? 145 GLN A N 1 ATOM 997 C CA . GLN A 1 144 ? 48.739 39.583 54.742 1.00 21.57 ? 145 GLN A CA 1 ATOM 998 C C . GLN A 1 144 ? 47.791 38.446 55.128 1.00 20.92 ? 145 GLN A C 1 ATOM 999 O O . GLN A 1 144 ? 48.037 37.275 54.784 1.00 20.54 ? 145 GLN A O 1 ATOM 1000 C CB . GLN A 1 144 ? 48.250 40.184 53.432 1.00 25.15 ? 145 GLN A CB 1 ATOM 1001 C CG . GLN A 1 144 ? 48.826 41.518 53.070 1.00 32.17 ? 145 GLN A CG 1 ATOM 1002 C CD . GLN A 1 144 ? 48.035 42.163 51.928 1.00 38.55 ? 145 GLN A CD 1 ATOM 1003 O OE1 . GLN A 1 144 ? 48.496 42.207 50.780 1.00 38.96 ? 145 GLN A OE1 1 ATOM 1004 N NE2 . GLN A 1 144 ? 46.814 42.623 52.232 1.00 40.62 ? 145 GLN A NE2 1 ATOM 1005 N N . PRO A 1 145 ? 46.704 38.767 55.850 1.00 18.83 ? 146 PRO A N 1 ATOM 1006 C CA . PRO A 1 145 ? 45.748 37.734 56.255 1.00 17.98 ? 146 PRO A CA 1 ATOM 1007 C C . PRO A 1 145 ? 45.209 37.069 54.997 1.00 17.28 ? 146 PRO A C 1 ATOM 1008 O O . PRO A 1 145 ? 45.118 37.692 53.931 1.00 16.60 ? 146 PRO A O 1 ATOM 1009 C CB . PRO A 1 145 ? 44.645 38.537 56.957 1.00 17.57 ? 146 PRO A CB 1 ATOM 1010 C CG . PRO A 1 145 ? 45.345 39.791 57.414 1.00 17.01 ? 146 PRO A CG 1 ATOM 1011 C CD . PRO A 1 145 ? 46.238 40.105 56.256 1.00 16.95 ? 146 PRO A CD 1 ATOM 1012 N N . SER A 1 146 ? 44.903 35.784 55.107 1.00 17.41 ? 147 SER A N 1 ATOM 1013 C CA . SER A 1 146 ? 44.350 35.032 53.978 1.00 16.15 ? 147 SER A CA 1 ATOM 1014 C C . SER A 1 146 ? 42.890 35.436 53.795 1.00 15.12 ? 147 SER A C 1 ATOM 1015 O O . SER A 1 146 ? 42.230 35.769 54.767 1.00 14.03 ? 147 SER A O 1 ATOM 1016 C CB . SER A 1 146 ? 44.340 33.543 54.328 1.00 16.75 ? 147 SER A CB 1 ATOM 1017 O OG . SER A 1 146 ? 43.557 32.798 53.412 1.00 16.73 ? 147 SER A OG 1 ATOM 1018 N N . PRO A 1 147 ? 42.402 35.497 52.544 1.00 14.61 ? 148 PRO A N 1 ATOM 1019 C CA . PRO A 1 147 ? 40.996 35.841 52.356 1.00 15.35 ? 148 PRO A CA 1 ATOM 1020 C C . PRO A 1 147 ? 40.213 34.657 52.983 1.00 16.37 ? 148 PRO A C 1 ATOM 1021 O O . PRO A 1 147 ? 40.771 33.537 53.140 1.00 15.38 ? 148 PRO A O 1 ATOM 1022 C CB . PRO A 1 147 ? 40.849 35.778 50.830 1.00 14.82 ? 148 PRO A CB 1 ATOM 1023 C CG . PRO A 1 147 ? 42.138 36.189 50.339 1.00 14.01 ? 148 PRO A CG 1 ATOM 1024 C CD . PRO A 1 147 ? 43.098 35.448 51.252 1.00 14.95 ? 148 PRO A CD 1 ATOM 1025 N N . PRO A 1 148 ? 38.951 34.876 53.387 1.00 15.08 ? 149 PRO A N 1 ATOM 1026 C CA . PRO A 1 148 ? 38.183 33.771 53.973 1.00 13.73 ? 149 PRO A CA 1 ATOM 1027 C C . PRO A 1 148 ? 37.663 32.830 52.882 1.00 13.30 ? 149 PRO A C 1 ATOM 1028 O O . PRO A 1 148 ? 37.780 33.123 51.695 1.00 12.04 ? 149 PRO A O 1 ATOM 1029 C CB . PRO A 1 148 ? 37.035 34.490 54.692 1.00 15.02 ? 149 PRO A CB 1 ATOM 1030 C CG . PRO A 1 148 ? 36.779 35.672 53.818 1.00 14.61 ? 149 PRO A CG 1 ATOM 1031 C CD . PRO A 1 148 ? 38.177 36.140 53.406 1.00 15.31 ? 149 PRO A CD 1 ATOM 1032 N N . SER A 1 149 ? 37.095 31.699 53.287 1.00 14.34 ? 150 SER A N 1 ATOM 1033 C CA . SER A 1 149 ? 36.514 30.717 52.358 1.00 15.69 ? 150 SER A CA 1 ATOM 1034 C C . SER A 1 149 ? 37.422 30.069 51.302 1.00 14.48 ? 150 SER A C 1 ATOM 1035 O O . SER A 1 149 ? 36.988 29.781 50.183 1.00 15.18 ? 150 SER A O 1 ATOM 1036 C CB . SER A 1 149 ? 35.231 31.280 51.709 1.00 17.55 ? 150 SER A CB 1 ATOM 1037 O OG . SER A 1 149 ? 34.191 31.467 52.687 1.00 22.22 ? 150 SER A OG 1 ATOM 1038 N N . LEU A 1 150 ? 38.669 29.797 51.680 1.00 13.28 ? 151 LEU A N 1 ATOM 1039 C CA . LEU A 1 150 ? 39.630 29.177 50.769 1.00 12.20 ? 151 LEU A CA 1 ATOM 1040 C C . LEU A 1 150 ? 40.045 27.753 51.199 1.00 12.55 ? 151 LEU A C 1 ATOM 1041 O O . LEU A 1 150 ? 40.682 27.037 50.435 1.00 12.04 ? 151 LEU A O 1 ATOM 1042 C CB . LEU A 1 150 ? 40.862 30.072 50.618 1.00 10.73 ? 151 LEU A CB 1 ATOM 1043 C CG . LEU A 1 150 ? 40.642 31.371 49.847 1.00 11.21 ? 151 LEU A CG 1 ATOM 1044 C CD1 . LEU A 1 150 ? 41.948 32.152 49.799 1.00 14.02 ? 151 LEU A CD1 1 ATOM 1045 C CD2 . LEU A 1 150 ? 40.122 31.116 48.440 1.00 11.83 ? 151 LEU A CD2 1 ATOM 1046 N N . ILE A 1 151 ? 39.615 27.339 52.386 1.00 13.31 ? 152 ILE A N 1 ATOM 1047 C CA . ILE A 1 151 ? 39.945 26.028 52.932 1.00 13.66 ? 152 ILE A CA 1 ATOM 1048 C C . ILE A 1 151 ? 38.792 25.048 52.715 1.00 13.23 ? 152 ILE A C 1 ATOM 1049 O O . ILE A 1 151 ? 37.700 25.277 53.205 1.00 12.82 ? 152 ILE A O 1 ATOM 1050 C CB . ILE A 1 151 ? 40.183 26.134 54.457 1.00 12.17 ? 152 ILE A CB 1 ATOM 1051 C CG1 . ILE A 1 151 ? 41.312 27.137 54.739 1.00 15.28 ? 152 ILE A CG1 1 ATOM 1052 C CG2 . ILE A 1 151 ? 40.540 24.763 55.041 1.00 12.66 ? 152 ILE A CG2 1 ATOM 1053 C CD1 . ILE A 1 151 ? 41.403 27.626 56.217 1.00 13.63 ? 152 ILE A CD1 1 ATOM 1054 N N . PRO A 1 152 ? 39.025 23.930 51.995 1.00 15.23 ? 153 PRO A N 1 ATOM 1055 C CA . PRO A 1 152 ? 37.946 22.945 51.770 1.00 15.12 ? 153 PRO A CA 1 ATOM 1056 C C . PRO A 1 152 ? 37.402 22.421 53.111 1.00 14.67 ? 153 PRO A C 1 ATOM 1057 O O . PRO A 1 152 ? 38.163 22.230 54.069 1.00 13.96 ? 153 PRO A O 1 ATOM 1058 C CB . PRO A 1 152 ? 38.663 21.819 51.018 1.00 14.37 ? 153 PRO A CB 1 ATOM 1059 C CG . PRO A 1 152 ? 39.772 22.509 50.279 1.00 16.31 ? 153 PRO A CG 1 ATOM 1060 C CD . PRO A 1 152 ? 40.261 23.564 51.274 1.00 14.96 ? 153 PRO A CD 1 ATOM 1061 N N . GLY A 1 153 ? 36.092 22.206 53.185 1.00 13.67 ? 154 GLY A N 1 ATOM 1062 C CA . GLY A 1 153 ? 35.493 21.708 54.414 1.00 13.34 ? 154 GLY A CA 1 ATOM 1063 C C . GLY A 1 153 ? 34.994 20.281 54.253 1.00 12.04 ? 154 GLY A C 1 ATOM 1064 O O . GLY A 1 153 ? 34.717 19.833 53.129 1.00 11.36 ? 154 GLY A O 1 ATOM 1065 N N . PRO A 1 154 ? 34.781 19.562 55.361 1.00 11.43 ? 155 PRO A N 1 ATOM 1066 C CA . PRO A 1 154 ? 34.306 18.170 55.310 1.00 11.30 ? 155 PRO A CA 1 ATOM 1067 C C . PRO A 1 154 ? 32.892 17.979 54.790 1.00 13.46 ? 155 PRO A C 1 ATOM 1068 O O . PRO A 1 154 ? 32.518 16.855 54.490 1.00 14.41 ? 155 PRO A O 1 ATOM 1069 C CB . PRO A 1 154 ? 34.449 17.706 56.752 1.00 10.28 ? 155 PRO A CB 1 ATOM 1070 C CG . PRO A 1 154 ? 34.140 18.982 57.525 1.00 10.91 ? 155 PRO A CG 1 ATOM 1071 C CD . PRO A 1 154 ? 34.932 20.029 56.743 1.00 9.83 ? 155 PRO A CD 1 ATOM 1072 N N . GLY A 1 155 ? 32.116 19.061 54.668 1.00 14.81 ? 156 GLY A N 1 ATOM 1073 C CA . GLY A 1 155 ? 30.754 18.960 54.163 1.00 13.13 ? 156 GLY A CA 1 ATOM 1074 C C . GLY A 1 155 ? 30.687 19.329 52.688 1.00 14.76 ? 156 GLY A C 1 ATOM 1075 O O . GLY A 1 155 ? 29.632 19.260 52.062 1.00 15.66 ? 156 GLY A O 1 ATOM 1076 N N . ASN A 1 156 ? 31.825 19.699 52.109 1.00 15.12 ? 157 ASN A N 1 ATOM 1077 C CA . ASN A 1 156 ? 31.871 20.077 50.695 1.00 15.75 ? 157 ASN A CA 1 ATOM 1078 C C . ASN A 1 156 ? 31.725 18.903 49.716 1.00 16.79 ? 157 ASN A C 1 ATOM 1079 O O . ASN A 1 156 ? 32.168 17.764 49.989 1.00 15.57 ? 157 ASN A O 1 ATOM 1080 C CB . ASN A 1 156 ? 33.203 20.792 50.350 1.00 18.51 ? 157 ASN A CB 1 ATOM 1081 C CG . ASN A 1 156 ? 33.428 22.091 51.135 1.00 20.47 ? 157 ASN A CG 1 ATOM 1082 O OD1 . ASN A 1 156 ? 34.412 22.789 50.905 1.00 23.40 ? 157 ASN A OD1 1 ATOM 1083 N ND2 . ASN A 1 156 ? 32.543 22.405 52.066 1.00 21.94 ? 157 ASN A ND2 1 ATOM 1084 N N . THR A 1 157 ? 31.194 19.207 48.533 1.00 16.24 ? 158 THR A N 1 ATOM 1085 C CA . THR A 1 157 ? 31.061 18.188 47.499 1.00 17.38 ? 158 THR A CA 1 ATOM 1086 C C . THR A 1 157 ? 32.438 17.937 46.873 1.00 15.36 ? 158 THR A C 1 ATOM 1087 O O . THR A 1 157 ? 33.312 18.791 46.929 1.00 13.53 ? 158 THR A O 1 ATOM 1088 C CB . THR A 1 157 ? 30.154 18.648 46.338 1.00 16.86 ? 158 THR A CB 1 ATOM 1089 O OG1 . THR A 1 157 ? 30.719 19.816 45.732 1.00 17.48 ? 158 THR A OG1 1 ATOM 1090 C CG2 . THR A 1 157 ? 28.748 18.924 46.813 1.00 16.30 ? 158 THR A CG2 1 ATOM 1091 N N . VAL A 1 158 ? 32.588 16.811 46.191 1.00 15.56 ? 159 VAL A N 1 ATOM 1092 C CA . VAL A 1 158 ? 33.837 16.502 45.531 1.00 15.00 ? 159 VAL A CA 1 ATOM 1093 C C . VAL A 1 158 ? 34.098 17.573 44.487 1.00 16.69 ? 159 VAL A C 1 ATOM 1094 O O . VAL A 1 158 ? 35.228 18.020 44.336 1.00 15.80 ? 159 VAL A O 1 ATOM 1095 C CB . VAL A 1 158 ? 33.806 15.092 44.891 1.00 14.42 ? 159 VAL A CB 1 ATOM 1096 C CG1 . VAL A 1 158 ? 34.954 14.916 43.854 1.00 11.79 ? 159 VAL A CG1 1 ATOM 1097 C CG2 . VAL A 1 158 ? 33.915 14.039 46.006 1.00 12.74 ? 159 VAL A CG2 1 ATOM 1098 N N . THR A 1 159 ? 33.058 18.021 43.788 1.00 15.97 ? 160 THR A N 1 ATOM 1099 C CA . THR A 1 159 ? 33.238 19.056 42.774 1.00 15.16 ? 160 THR A CA 1 ATOM 1100 C C . THR A 1 159 ? 33.818 20.299 43.427 1.00 15.47 ? 160 THR A C 1 ATOM 1101 O O . THR A 1 159 ? 34.752 20.881 42.926 1.00 14.44 ? 160 THR A O 1 ATOM 1102 C CB . THR A 1 159 ? 31.896 19.453 42.115 1.00 17.42 ? 160 THR A CB 1 ATOM 1103 O OG1 . THR A 1 159 ? 31.325 18.298 41.475 1.00 19.38 ? 160 THR A OG1 1 ATOM 1104 C CG2 . THR A 1 159 ? 32.104 20.582 41.061 1.00 13.85 ? 160 THR A CG2 1 ATOM 1105 N N . ALA A 1 160 ? 33.253 20.688 44.558 1.00 15.36 ? 161 ALA A N 1 ATOM 1106 C CA . ALA A 1 160 ? 33.715 21.860 45.262 1.00 14.36 ? 161 ALA A CA 1 ATOM 1107 C C . ALA A 1 160 ? 35.173 21.734 45.720 1.00 15.44 ? 161 ALA A C 1 ATOM 1108 O O . ALA A 1 160 ? 35.963 22.676 45.562 1.00 16.39 ? 161 ALA A O 1 ATOM 1109 C CB . ALA A 1 160 ? 32.835 22.102 46.424 1.00 14.22 ? 161 ALA A CB 1 ATOM 1110 N N . ILE A 1 161 ? 35.536 20.574 46.267 1.00 14.80 ? 162 ILE A N 1 ATOM 1111 C CA . ILE A 1 161 ? 36.900 20.329 46.762 1.00 12.21 ? 162 ILE A CA 1 ATOM 1112 C C . ILE A 1 161 ? 37.898 20.377 45.612 1.00 13.04 ? 162 ILE A C 1 ATOM 1113 O O . ILE A 1 161 ? 38.913 21.078 45.681 1.00 13.88 ? 162 ILE A O 1 ATOM 1114 C CB . ILE A 1 161 ? 36.985 18.946 47.505 1.00 12.84 ? 162 ILE A CB 1 ATOM 1115 C CG1 . ILE A 1 161 ? 36.146 18.995 48.783 1.00 11.19 ? 162 ILE A CG1 1 ATOM 1116 C CG2 . ILE A 1 161 ? 38.414 18.613 47.853 1.00 10.19 ? 162 ILE A CG2 1 ATOM 1117 C CD1 . ILE A 1 161 ? 35.861 17.667 49.431 1.00 9.73 ? 162 ILE A CD1 1 ATOM 1118 N N . LEU A 1 162 ? 37.554 19.721 44.514 1.00 12.98 ? 163 LEU A N 1 ATOM 1119 C CA . LEU A 1 162 ? 38.421 19.683 43.350 1.00 13.91 ? 163 LEU A CA 1 ATOM 1120 C C . LEU A 1 162 ? 38.582 21.045 42.719 1.00 15.42 ? 163 LEU A C 1 ATOM 1121 O O . LEU A 1 162 ? 39.672 21.367 42.284 1.00 18.19 ? 163 LEU A O 1 ATOM 1122 C CB . LEU A 1 162 ? 37.942 18.657 42.303 1.00 13.64 ? 163 LEU A CB 1 ATOM 1123 C CG . LEU A 1 162 ? 37.990 17.211 42.818 1.00 16.95 ? 163 LEU A CG 1 ATOM 1124 C CD1 . LEU A 1 162 ? 37.558 16.211 41.740 1.00 14.43 ? 163 LEU A CD1 1 ATOM 1125 C CD2 . LEU A 1 162 ? 39.396 16.887 43.328 1.00 17.41 ? 163 LEU A CD2 1 ATOM 1126 N N . ASP A 1 163 ? 37.526 21.848 42.654 1.00 15.22 ? 164 ASP A N 1 ATOM 1127 C CA . ASP A 1 163 ? 37.635 23.195 42.057 1.00 17.72 ? 164 ASP A CA 1 ATOM 1128 C C . ASP A 1 163 ? 38.570 24.104 42.882 1.00 15.40 ? 164 ASP A C 1 ATOM 1129 O O . ASP A 1 163 ? 39.423 24.821 42.343 1.00 15.93 ? 164 ASP A O 1 ATOM 1130 C CB . ASP A 1 163 ? 36.257 23.869 41.948 1.00 22.66 ? 164 ASP A CB 1 ATOM 1131 C CG . ASP A 1 163 ? 35.384 23.295 40.824 1.00 30.50 ? 164 ASP A CG 1 ATOM 1132 O OD1 . ASP A 1 163 ? 35.890 22.585 39.925 1.00 34.46 ? 164 ASP A OD1 1 ATOM 1133 O OD2 . ASP A 1 163 ? 34.159 23.565 40.836 1.00 35.98 ? 164 ASP A OD2 1 ATOM 1134 N N . ARG A 1 164 ? 38.380 24.092 44.193 1.00 13.83 ? 165 ARG A N 1 ATOM 1135 C CA . ARG A 1 164 ? 39.198 24.894 45.099 1.00 13.13 ? 165 ARG A CA 1 ATOM 1136 C C . ARG A 1 164 ? 40.670 24.443 44.993 1.00 14.42 ? 165 ARG A C 1 ATOM 1137 O O . ARG A 1 164 ? 41.563 25.235 44.685 1.00 13.19 ? 165 ARG A O 1 ATOM 1138 C CB . ARG A 1 164 ? 38.671 24.731 46.530 1.00 10.28 ? 165 ARG A CB 1 ATOM 1139 C CG . ARG A 1 164 ? 39.409 25.527 47.623 1.00 12.85 ? 165 ARG A CG 1 ATOM 1140 C CD . ARG A 1 164 ? 39.278 27.083 47.507 1.00 13.28 ? 165 ARG A CD 1 ATOM 1141 N NE . ARG A 1 164 ? 40.246 27.692 46.576 1.00 15.76 ? 165 ARG A NE 1 ATOM 1142 C CZ . ARG A 1 164 ? 41.544 27.925 46.831 1.00 13.03 ? 165 ARG A CZ 1 ATOM 1143 N NH1 . ARG A 1 164 ? 42.095 27.608 48.002 1.00 11.17 ? 165 ARG A NH1 1 ATOM 1144 N NH2 . ARG A 1 164 ? 42.291 28.496 45.902 1.00 10.74 ? 165 ARG A NH2 1 ATOM 1145 N N . MET A 1 165 ? 40.911 23.157 45.213 1.00 14.06 ? 166 MET A N 1 ATOM 1146 C CA . MET A 1 165 ? 42.270 22.630 45.139 1.00 15.25 ? 166 MET A CA 1 ATOM 1147 C C . MET A 1 165 ? 42.863 22.832 43.748 1.00 15.18 ? 166 MET A C 1 ATOM 1148 O O . MET A 1 165 ? 44.039 23.164 43.613 1.00 16.80 ? 166 MET A O 1 ATOM 1149 C CB . MET A 1 165 ? 42.287 21.147 45.525 1.00 16.76 ? 166 MET A CB 1 ATOM 1150 C CG . MET A 1 165 ? 41.819 20.850 46.966 1.00 16.17 ? 166 MET A CG 1 ATOM 1151 S SD . MET A 1 165 ? 42.921 21.478 48.204 1.00 20.49 ? 166 MET A SD 1 ATOM 1152 C CE . MET A 1 165 ? 44.172 20.206 48.185 1.00 20.21 ? 166 MET A CE 1 ATOM 1153 N N . GLY A 1 166 ? 42.024 22.700 42.723 1.00 16.08 ? 167 GLY A N 1 ATOM 1154 C CA . GLY A 1 166 ? 42.450 22.862 41.341 1.00 16.59 ? 167 GLY A CA 1 ATOM 1155 C C . GLY A 1 166 ? 42.917 24.290 41.102 1.00 17.24 ? 167 GLY A C 1 ATOM 1156 O O . GLY A 1 166 ? 43.902 24.518 40.390 1.00 15.54 ? 167 GLY A O 1 ATOM 1157 N N . ASP A 1 167 ? 42.205 25.244 41.696 1.00 16.15 ? 168 ASP A N 1 ATOM 1158 C CA . ASP A 1 167 ? 42.551 26.658 41.609 1.00 16.82 ? 168 ASP A CA 1 ATOM 1159 C C . ASP A 1 167 ? 43.934 26.907 42.233 1.00 17.75 ? 168 ASP A C 1 ATOM 1160 O O . ASP A 1 167 ? 44.742 27.645 41.662 1.00 19.10 ? 168 ASP A O 1 ATOM 1161 C CB . ASP A 1 167 ? 41.508 27.456 42.371 1.00 17.75 ? 168 ASP A CB 1 ATOM 1162 C CG . ASP A 1 167 ? 41.789 28.930 42.393 1.00 17.99 ? 168 ASP A CG 1 ATOM 1163 O OD1 . ASP A 1 167 ? 41.398 29.561 43.385 1.00 19.73 ? 168 ASP A OD1 1 ATOM 1164 O OD2 . ASP A 1 167 ? 42.366 29.465 41.427 1.00 21.09 ? 168 ASP A OD2 1 ATOM 1165 N N . ALA A 1 168 ? 44.188 26.309 43.404 1.00 16.22 ? 169 ALA A N 1 ATOM 1166 C CA . ALA A 1 168 ? 45.470 26.434 44.111 1.00 17.15 ? 169 ALA A CA 1 ATOM 1167 C C . ALA A 1 168 ? 46.607 25.845 43.286 1.00 18.53 ? 169 ALA A C 1 ATOM 1168 O O . ALA A 1 168 ? 47.778 26.161 43.514 1.00 17.35 ? 169 ALA A O 1 ATOM 1169 C CB . ALA A 1 168 ? 45.407 25.743 45.415 1.00 16.06 ? 169 ALA A CB 1 ATOM 1170 N N . GLY A 1 169 ? 46.239 24.922 42.397 1.00 19.01 ? 170 GLY A N 1 ATOM 1171 C CA . GLY A 1 169 ? 47.182 24.310 41.500 1.00 18.67 ? 170 GLY A CA 1 ATOM 1172 C C . GLY A 1 169 ? 47.327 22.817 41.607 1.00 20.80 ? 170 GLY A C 1 ATOM 1173 O O . GLY A 1 169 ? 48.301 22.298 41.078 1.00 21.79 ? 170 GLY A O 1 ATOM 1174 N N . PHE A 1 170 ? 46.395 22.116 42.255 1.00 20.06 ? 171 PHE A N 1 ATOM 1175 C CA . PHE A 1 170 ? 46.504 20.655 42.411 1.00 18.81 ? 171 PHE A CA 1 ATOM 1176 C C . PHE A 1 170 ? 45.524 19.883 41.565 1.00 19.19 ? 171 PHE A C 1 ATOM 1177 O O . PHE A 1 170 ? 44.360 20.267 41.468 1.00 20.51 ? 171 PHE A O 1 ATOM 1178 C CB . PHE A 1 170 ? 46.293 20.255 43.867 1.00 16.88 ? 171 PHE A CB 1 ATOM 1179 C CG . PHE A 1 170 ? 47.271 20.888 44.806 1.00 19.51 ? 171 PHE A CG 1 ATOM 1180 C CD1 . PHE A 1 170 ? 48.567 20.382 44.929 1.00 19.91 ? 171 PHE A CD1 1 ATOM 1181 C CD2 . PHE A 1 170 ? 46.923 22.008 45.538 1.00 16.77 ? 171 PHE A CD2 1 ATOM 1182 C CE1 . PHE A 1 170 ? 49.514 20.998 45.774 1.00 19.07 ? 171 PHE A CE1 1 ATOM 1183 C CE2 . PHE A 1 170 ? 47.857 22.625 46.379 1.00 19.03 ? 171 PHE A CE2 1 ATOM 1184 C CZ . PHE A 1 170 ? 49.154 22.116 46.493 1.00 17.32 ? 171 PHE A CZ 1 ATOM 1185 N N . SER A 1 171 ? 45.992 18.800 40.948 1.00 19.07 ? 172 SER A N 1 ATOM 1186 C CA . SER A 1 171 ? 45.132 17.928 40.125 1.00 18.24 ? 172 SER A CA 1 ATOM 1187 C C . SER A 1 171 ? 44.367 17.017 41.080 1.00 17.50 ? 172 SER A C 1 ATOM 1188 O O . SER A 1 171 ? 44.714 16.913 42.256 1.00 18.67 ? 172 SER A O 1 ATOM 1189 C CB . SER A 1 171 ? 45.984 17.013 39.249 1.00 19.23 ? 172 SER A CB 1 ATOM 1190 O OG . SER A 1 171 ? 46.668 16.081 40.075 1.00 19.13 ? 172 SER A OG 1 ATOM 1191 N N . PRO A 1 172 ? 43.350 16.304 40.575 1.00 16.60 ? 173 PRO A N 1 ATOM 1192 C CA . PRO A 1 172 ? 42.577 15.400 41.422 1.00 15.98 ? 173 PRO A CA 1 ATOM 1193 C C . PRO A 1 172 ? 43.491 14.347 42.043 1.00 15.37 ? 173 PRO A C 1 ATOM 1194 O O . PRO A 1 172 ? 43.290 13.952 43.209 1.00 14.64 ? 173 PRO A O 1 ATOM 1195 C CB . PRO A 1 172 ? 41.601 14.788 40.436 1.00 15.62 ? 173 PRO A CB 1 ATOM 1196 C CG . PRO A 1 172 ? 41.345 15.921 39.480 1.00 16.34 ? 173 PRO A CG 1 ATOM 1197 C CD . PRO A 1 172 ? 42.719 16.454 39.250 1.00 17.85 ? 173 PRO A CD 1 ATOM 1198 N N . ASP A 1 173 ? 44.471 13.869 41.263 1.00 14.91 ? 174 ASP A N 1 ATOM 1199 C CA . ASP A 1 173 ? 45.441 12.882 41.763 1.00 15.15 ? 174 ASP A CA 1 ATOM 1200 C C . ASP A 1 173 ? 46.203 13.422 42.956 1.00 13.87 ? 174 ASP A C 1 ATOM 1201 O O . ASP A 1 173 ? 46.384 12.726 43.953 1.00 12.32 ? 174 ASP A O 1 ATOM 1202 C CB . ASP A 1 173 ? 46.456 12.510 40.695 1.00 19.32 ? 174 ASP A CB 1 ATOM 1203 C CG . ASP A 1 173 ? 45.874 11.619 39.607 1.00 23.49 ? 174 ASP A CG 1 ATOM 1204 O OD1 . ASP A 1 173 ? 44.816 10.973 39.807 1.00 24.04 ? 174 ASP A OD1 1 ATOM 1205 O OD2 . ASP A 1 173 ? 46.497 11.562 38.527 1.00 28.52 ? 174 ASP A OD2 1 ATOM 1206 N N . GLU A 1 174 ? 46.695 14.650 42.828 1.00 14.32 ? 175 GLU A N 1 ATOM 1207 C CA . GLU A 1 174 ? 47.444 15.282 43.925 1.00 15.86 ? 175 GLU A CA 1 ATOM 1208 C C . GLU A 1 174 ? 46.589 15.517 45.171 1.00 14.16 ? 175 GLU A C 1 ATOM 1209 O O . GLU A 1 174 ? 47.089 15.517 46.296 1.00 14.44 ? 175 GLU A O 1 ATOM 1210 C CB . GLU A 1 174 ? 48.077 16.581 43.441 1.00 17.16 ? 175 GLU A CB 1 ATOM 1211 C CG . GLU A 1 174 ? 48.926 16.331 42.231 1.00 21.88 ? 175 GLU A CG 1 ATOM 1212 C CD . GLU A 1 174 ? 49.671 17.548 41.767 1.00 24.02 ? 175 GLU A CD 1 ATOM 1213 O OE1 . GLU A 1 174 ? 49.032 18.549 41.403 1.00 25.15 ? 175 GLU A OE1 1 ATOM 1214 O OE2 . GLU A 1 174 ? 50.910 17.492 41.767 1.00 27.62 ? 175 GLU A OE2 1 ATOM 1215 N N . VAL A 1 175 ? 45.301 15.767 44.962 1.00 13.67 ? 176 VAL A N 1 ATOM 1216 C CA . VAL A 1 175 ? 44.385 15.933 46.081 1.00 13.07 ? 176 VAL A CA 1 ATOM 1217 C C . VAL A 1 175 ? 44.342 14.625 46.892 1.00 11.99 ? 176 VAL A C 1 ATOM 1218 O O . VAL A 1 175 ? 44.430 14.641 48.129 1.00 11.72 ? 176 VAL A O 1 ATOM 1219 C CB . VAL A 1 175 ? 42.983 16.336 45.599 1.00 12.40 ? 176 VAL A CB 1 ATOM 1220 C CG1 . VAL A 1 175 ? 42.014 16.316 46.774 1.00 12.02 ? 176 VAL A CG1 1 ATOM 1221 C CG2 . VAL A 1 175 ? 43.049 17.730 44.956 1.00 10.69 ? 176 VAL A CG2 1 ATOM 1222 N N . VAL A 1 176 ? 44.208 13.504 46.189 1.00 10.93 ? 177 VAL A N 1 ATOM 1223 C CA . VAL A 1 176 ? 44.194 12.195 46.840 1.00 12.22 ? 177 VAL A CA 1 ATOM 1224 C C . VAL A 1 176 ? 45.564 11.943 47.532 1.00 12.19 ? 177 VAL A C 1 ATOM 1225 O O . VAL A 1 176 ? 45.606 11.514 48.678 1.00 13.15 ? 177 VAL A O 1 ATOM 1226 C CB . VAL A 1 176 ? 43.868 11.076 45.802 1.00 11.48 ? 177 VAL A CB 1 ATOM 1227 C CG1 . VAL A 1 176 ? 44.005 9.673 46.434 1.00 9.77 ? 177 VAL A CG1 1 ATOM 1228 C CG2 . VAL A 1 176 ? 42.447 11.298 45.248 1.00 12.79 ? 177 VAL A CG2 1 ATOM 1229 N N . ASP A 1 177 ? 46.669 12.304 46.878 1.00 12.31 ? 178 ASP A N 1 ATOM 1230 C CA . ASP A 1 177 ? 48.009 12.107 47.463 1.00 12.62 ? 178 ASP A CA 1 ATOM 1231 C C . ASP A 1 177 ? 48.223 12.914 48.740 1.00 14.14 ? 178 ASP A C 1 ATOM 1232 O O . ASP A 1 177 ? 48.835 12.432 49.701 1.00 14.85 ? 178 ASP A O 1 ATOM 1233 C CB . ASP A 1 177 ? 49.112 12.484 46.461 1.00 12.75 ? 178 ASP A CB 1 ATOM 1234 C CG . ASP A 1 177 ? 49.015 11.733 45.139 1.00 17.03 ? 178 ASP A CG 1 ATOM 1235 O OD1 . ASP A 1 177 ? 48.521 10.578 45.100 1.00 19.08 ? 178 ASP A OD1 1 ATOM 1236 O OD2 . ASP A 1 177 ? 49.453 12.313 44.129 1.00 17.00 ? 178 ASP A OD2 1 ATOM 1237 N N . LEU A 1 178 ? 47.767 14.167 48.726 1.00 14.12 ? 179 LEU A N 1 ATOM 1238 C CA . LEU A 1 178 ? 47.897 15.069 49.879 1.00 13.95 ? 179 LEU A CA 1 ATOM 1239 C C . LEU A 1 178 ? 47.103 14.542 51.079 1.00 15.07 ? 179 LEU A C 1 ATOM 1240 O O . LEU A 1 178 ? 47.479 14.753 52.244 1.00 14.47 ? 179 LEU A O 1 ATOM 1241 C CB . LEU A 1 178 ? 47.380 16.446 49.479 1.00 13.07 ? 179 LEU A CB 1 ATOM 1242 C CG . LEU A 1 178 ? 48.227 17.706 49.426 1.00 15.14 ? 179 LEU A CG 1 ATOM 1243 C CD1 . LEU A 1 178 ? 49.710 17.454 49.551 1.00 14.87 ? 179 LEU A CD1 1 ATOM 1244 C CD2 . LEU A 1 178 ? 47.866 18.454 48.179 1.00 14.08 ? 179 LEU A CD2 1 ATOM 1245 N N . LEU A 1 179 ? 46.009 13.836 50.793 1.00 13.58 ? 180 LEU A N 1 ATOM 1246 C CA . LEU A 1 179 ? 45.171 13.271 51.853 1.00 11.86 ? 180 LEU A CA 1 ATOM 1247 C C . LEU A 1 179 ? 45.810 12.115 52.618 1.00 10.82 ? 180 LEU A C 1 ATOM 1248 O O . LEU A 1 179 ? 45.241 11.638 53.590 1.00 10.76 ? 180 LEU A O 1 ATOM 1249 C CB . LEU A 1 179 ? 43.779 12.876 51.306 1.00 12.29 ? 180 LEU A CB 1 ATOM 1250 C CG . LEU A 1 179 ? 42.783 14.050 51.440 1.00 10.96 ? 180 LEU A CG 1 ATOM 1251 C CD1 . LEU A 1 179 ? 41.640 13.891 50.480 1.00 11.95 ? 180 LEU A CD1 1 ATOM 1252 C CD2 . LEU A 1 179 ? 42.321 14.197 52.873 1.00 8.22 ? 180 LEU A CD2 1 ATOM 1253 N N . ALA A 1 180 ? 47.033 11.727 52.259 1.00 11.45 ? 181 ALA A N 1 ATOM 1254 C CA . ALA A 1 180 ? 47.718 10.645 52.979 1.00 10.52 ? 181 ALA A CA 1 ATOM 1255 C C . ALA A 1 180 ? 47.943 11.119 54.416 1.00 10.21 ? 181 ALA A C 1 ATOM 1256 O O . ALA A 1 180 ? 48.072 10.301 55.362 1.00 10.30 ? 181 ALA A O 1 ATOM 1257 C CB . ALA A 1 180 ? 49.073 10.274 52.282 1.00 10.76 ? 181 ALA A CB 1 ATOM 1258 N N . ALA A 1 181 ? 47.916 12.446 54.619 1.00 9.21 ? 182 ALA A N 1 ATOM 1259 C CA . ALA A 1 181 ? 48.091 13.001 55.965 1.00 8.05 ? 182 ALA A CA 1 ATOM 1260 C C . ALA A 1 181 ? 47.016 12.518 56.946 1.00 8.12 ? 182 ALA A C 1 ATOM 1261 O O . ALA A 1 181 ? 47.220 12.549 58.157 1.00 9.03 ? 182 ALA A O 1 ATOM 1262 C CB . ALA A 1 181 ? 48.123 14.554 55.915 1.00 9.63 ? 182 ALA A CB 1 HETATM 1263 N N . HSO A 1 182 ? 45.858 12.088 56.437 1.00 9.91 ? 183 HSO A N 1 HETATM 1264 C CA . HSO A 1 182 ? 44.786 11.578 57.306 1.00 10.51 ? 183 HSO A CA 1 HETATM 1265 C CB . HSO A 1 182 ? 43.432 11.553 56.584 1.00 11.89 ? 183 HSO A CB 1 HETATM 1266 C CG . HSO A 1 182 ? 42.746 12.911 56.571 1.00 11.85 ? 183 HSO A CG 1 HETATM 1267 N ND1 . HSO A 1 182 ? 41.479 13.102 56.113 1.00 12.65 ? 183 HSO A ND1 1 HETATM 1268 C CD2 . HSO A 1 182 ? 43.260 14.127 57.019 1.00 12.50 ? 183 HSO A CD2 1 HETATM 1269 C CE1 . HSO A 1 182 ? 41.247 14.400 56.255 1.00 12.06 ? 183 HSO A CE1 1 HETATM 1270 N NE2 . HSO A 1 182 ? 42.246 15.067 56.755 1.00 9.61 ? 183 HSO A NE2 1 HETATM 1271 C C . HSO A 1 182 ? 45.129 10.190 57.868 1.00 12.07 ? 183 HSO A C 1 HETATM 1272 O O . HSO A 1 182 ? 44.370 9.607 58.632 1.00 11.16 ? 183 HSO A O 1 ATOM 1273 N N . SER A 1 183 ? 46.259 9.645 57.432 1.00 13.20 ? 184 SER A N 1 ATOM 1274 C CA . SER A 1 183 ? 46.742 8.393 57.966 1.00 11.00 ? 184 SER A CA 1 ATOM 1275 C C . SER A 1 183 ? 47.325 8.673 59.362 1.00 10.24 ? 184 SER A C 1 ATOM 1276 O O . SER A 1 183 ? 47.636 7.744 60.102 1.00 12.74 ? 184 SER A O 1 ATOM 1277 C CB . SER A 1 183 ? 47.797 7.816 57.035 1.00 12.20 ? 184 SER A CB 1 ATOM 1278 O OG . SER A 1 183 ? 48.283 6.566 57.525 1.00 17.12 ? 184 SER A OG 1 ATOM 1279 N N . LEU A 1 184 ? 47.488 9.948 59.729 1.00 10.57 ? 185 LEU A N 1 ATOM 1280 C CA . LEU A 1 184 ? 48.015 10.362 61.049 1.00 10.09 ? 185 LEU A CA 1 ATOM 1281 C C . LEU A 1 184 ? 47.007 11.402 61.531 1.00 12.68 ? 185 LEU A C 1 ATOM 1282 O O . LEU A 1 184 ? 47.355 12.570 61.728 1.00 14.04 ? 185 LEU A O 1 ATOM 1283 C CB . LEU A 1 184 ? 49.374 11.058 60.876 1.00 9.64 ? 185 LEU A CB 1 ATOM 1284 C CG . LEU A 1 184 ? 50.548 10.203 60.359 1.00 11.76 ? 185 LEU A CG 1 ATOM 1285 C CD1 . LEU A 1 184 ? 51.671 11.093 59.924 1.00 11.92 ? 185 LEU A CD1 1 ATOM 1286 C CD2 . LEU A 1 184 ? 51.030 9.257 61.472 1.00 11.09 ? 185 LEU A CD2 1 ATOM 1287 N N . ALA A 1 185 ? 45.768 10.980 61.759 1.00 13.71 ? 186 ALA A N 1 ATOM 1288 C CA . ALA A 1 185 ? 44.710 11.918 62.088 1.00 10.46 ? 186 ALA A CA 1 ATOM 1289 C C . ALA A 1 185 ? 43.606 11.406 62.982 1.00 12.38 ? 186 ALA A C 1 ATOM 1290 O O . ALA A 1 185 ? 43.293 10.206 62.994 1.00 12.97 ? 186 ALA A O 1 ATOM 1291 C CB . ALA A 1 185 ? 44.080 12.398 60.793 1.00 7.87 ? 186 ALA A CB 1 ATOM 1292 N N . SER A 1 186 ? 42.944 12.359 63.631 1.00 12.96 ? 187 SER A N 1 ATOM 1293 C CA . SER A 1 186 ? 41.812 12.118 64.503 1.00 13.71 ? 187 SER A CA 1 ATOM 1294 C C . SER A 1 186 ? 40.928 13.366 64.322 1.00 13.51 ? 187 SER A C 1 ATOM 1295 O O . SER A 1 186 ? 41.250 14.218 63.504 1.00 14.36 ? 187 SER A O 1 ATOM 1296 C CB . SER A 1 186 ? 42.276 11.988 65.961 1.00 13.82 ? 187 SER A CB 1 ATOM 1297 O OG . SER A 1 186 ? 42.523 13.238 66.587 1.00 13.65 ? 187 SER A OG 1 ATOM 1298 N N . GLN A 1 187 ? 39.790 13.435 65.004 1.00 13.03 ? 188 GLN A N 1 ATOM 1299 C CA . GLN A 1 187 ? 38.939 14.621 64.946 1.00 11.56 ? 188 GLN A CA 1 ATOM 1300 C C . GLN A 1 187 ? 38.643 14.971 66.371 1.00 12.04 ? 188 GLN A C 1 ATOM 1301 O O . GLN A 1 187 ? 38.518 14.093 67.214 1.00 12.75 ? 188 GLN A O 1 ATOM 1302 C CB . GLN A 1 187 ? 37.653 14.407 64.109 1.00 11.93 ? 188 GLN A CB 1 ATOM 1303 C CG . GLN A 1 187 ? 36.585 13.409 64.639 1.00 12.85 ? 188 GLN A CG 1 ATOM 1304 C CD . GLN A 1 187 ? 35.820 13.904 65.869 1.00 14.12 ? 188 GLN A CD 1 ATOM 1305 O OE1 . GLN A 1 187 ? 35.588 15.100 66.029 1.00 13.67 ? 188 GLN A OE1 1 ATOM 1306 N NE2 . GLN A 1 187 ? 35.508 12.991 66.782 1.00 15.17 ? 188 GLN A NE2 1 ATOM 1307 N N . GLU A 1 188 ? 38.615 16.251 66.689 1.00 13.04 ? 189 GLU A N 1 ATOM 1308 C CA . GLU A 1 188 ? 38.309 16.673 68.040 1.00 13.89 ? 189 GLU A CA 1 ATOM 1309 C C . GLU A 1 188 ? 37.065 17.538 67.986 1.00 16.29 ? 189 GLU A C 1 ATOM 1310 O O . GLU A 1 188 ? 36.303 17.594 68.944 1.00 18.38 ? 189 GLU A O 1 ATOM 1311 C CB . GLU A 1 188 ? 39.449 17.498 68.622 1.00 14.83 ? 189 GLU A CB 1 ATOM 1312 C CG . GLU A 1 188 ? 40.754 16.750 68.708 1.00 15.98 ? 189 GLU A CG 1 ATOM 1313 C CD . GLU A 1 188 ? 41.825 17.546 69.409 1.00 16.52 ? 189 GLU A CD 1 ATOM 1314 O OE1 . GLU A 1 188 ? 41.677 18.769 69.582 1.00 15.73 ? 189 GLU A OE1 1 ATOM 1315 O OE2 . GLU A 1 188 ? 42.831 16.935 69.795 1.00 19.11 ? 189 GLU A OE2 1 ATOM 1316 N N . GLY A 1 189 ? 36.855 18.191 66.854 1.00 16.41 ? 190 GLY A N 1 ATOM 1317 C CA . GLY A 1 189 ? 35.709 19.056 66.717 1.00 16.86 ? 190 GLY A CA 1 ATOM 1318 C C . GLY A 1 189 ? 34.483 18.590 65.947 1.00 18.43 ? 190 GLY A C 1 ATOM 1319 O O . GLY A 1 189 ? 33.466 19.278 66.013 1.00 18.00 ? 190 GLY A O 1 ATOM 1320 N N . LEU A 1 190 ? 34.537 17.498 65.190 1.00 16.48 ? 191 LEU A N 1 ATOM 1321 C CA . LEU A 1 190 ? 33.334 17.097 64.451 1.00 17.32 ? 191 LEU A CA 1 ATOM 1322 C C . LEU A 1 190 ? 32.308 16.379 65.350 1.00 20.11 ? 191 LEU A C 1 ATOM 1323 O O . LEU A 1 190 ? 31.099 16.507 65.137 1.00 21.71 ? 191 LEU A O 1 ATOM 1324 C CB . LEU A 1 190 ? 33.682 16.254 63.230 1.00 14.45 ? 191 LEU A CB 1 ATOM 1325 C CG . LEU A 1 190 ? 34.615 16.895 62.205 1.00 12.42 ? 191 LEU A CG 1 ATOM 1326 C CD1 . LEU A 1 190 ? 34.860 15.909 61.075 1.00 12.04 ? 191 LEU A CD1 1 ATOM 1327 C CD2 . LEU A 1 190 ? 34.021 18.150 61.649 1.00 11.16 ? 191 LEU A CD2 1 ATOM 1328 N N . ASN A 1 191 ? 32.788 15.671 66.375 1.00 19.39 ? 192 ASN A N 1 ATOM 1329 C CA . ASN A 1 191 ? 31.934 14.930 67.315 1.00 20.01 ? 192 ASN A CA 1 ATOM 1330 C C . ASN A 1 191 ? 32.743 14.857 68.585 1.00 20.90 ? 192 ASN A C 1 ATOM 1331 O O . ASN A 1 191 ? 33.534 13.930 68.796 1.00 20.37 ? 192 ASN A O 1 ATOM 1332 C CB . ASN A 1 191 ? 31.618 13.512 66.800 1.00 17.66 ? 192 ASN A CB 1 ATOM 1333 C CG . ASN A 1 191 ? 30.597 12.787 67.662 1.00 16.26 ? 192 ASN A CG 1 ATOM 1334 O OD1 . ASN A 1 191 ? 30.438 13.091 68.829 1.00 17.87 ? 192 ASN A OD1 1 ATOM 1335 N ND2 . ASN A 1 191 ? 29.915 11.813 67.084 1.00 15.83 ? 192 ASN A ND2 1 ATOM 1336 N N . SER A 1 192 ? 32.582 15.882 69.402 1.00 22.18 ? 193 SER A N 1 ATOM 1337 C CA . SER A 1 192 ? 33.311 15.983 70.649 1.00 24.50 ? 193 SER A CA 1 ATOM 1338 C C . SER A 1 192 ? 33.044 14.822 71.612 1.00 25.24 ? 193 SER A C 1 ATOM 1339 O O . SER A 1 192 ? 33.812 14.610 72.559 1.00 26.66 ? 193 SER A O 1 ATOM 1340 C CB . SER A 1 192 ? 32.950 17.291 71.332 1.00 27.55 ? 193 SER A CB 1 ATOM 1341 O OG . SER A 1 192 ? 31.604 17.240 71.786 1.00 30.87 ? 193 SER A OG 1 ATOM 1342 N N . ALA A 1 193 ? 31.969 14.070 71.379 1.00 25.22 ? 194 ALA A N 1 ATOM 1343 C CA . ALA A 1 193 ? 31.647 12.942 72.257 1.00 24.41 ? 194 ALA A CA 1 ATOM 1344 C C . ALA A 1 193 ? 32.652 11.823 72.088 1.00 23.77 ? 194 ALA A C 1 ATOM 1345 O O . ALA A 1 193 ? 32.757 10.968 72.973 1.00 25.19 ? 194 ALA A O 1 ATOM 1346 C CB . ALA A 1 193 ? 30.243 12.421 71.993 1.00 27.93 ? 194 ALA A CB 1 ATOM 1347 N N . ILE A 1 194 ? 33.288 11.759 70.911 1.00 20.90 ? 195 ILE A N 1 ATOM 1348 C CA . ILE A 1 194 ? 34.347 10.768 70.629 1.00 20.10 ? 195 ILE A CA 1 ATOM 1349 C C . ILE A 1 194 ? 35.634 11.541 70.251 1.00 18.55 ? 195 ILE A C 1 ATOM 1350 O O . ILE A 1 194 ? 36.168 11.416 69.150 1.00 18.46 ? 195 ILE A O 1 ATOM 1351 C CB . ILE A 1 194 ? 33.936 9.726 69.550 1.00 18.62 ? 195 ILE A CB 1 ATOM 1352 C CG1 . ILE A 1 194 ? 33.255 10.374 68.358 1.00 17.61 ? 195 ILE A CG1 1 ATOM 1353 C CG2 . ILE A 1 194 ? 32.985 8.701 70.161 1.00 20.01 ? 195 ILE A CG2 1 ATOM 1354 C CD1 . ILE A 1 194 ? 33.021 9.391 67.231 1.00 13.99 ? 195 ILE A CD1 1 ATOM 1355 N N . PHE A 1 195 ? 36.069 12.374 71.196 1.00 17.43 ? 196 PHE A N 1 ATOM 1356 C CA . PHE A 1 195 ? 37.224 13.267 71.060 1.00 17.59 ? 196 PHE A CA 1 ATOM 1357 C C . PHE A 1 195 ? 38.445 12.449 70.717 1.00 17.90 ? 196 PHE A C 1 ATOM 1358 O O . PHE A 1 195 ? 38.746 11.476 71.408 1.00 16.72 ? 196 PHE A O 1 ATOM 1359 C CB . PHE A 1 195 ? 37.406 14.001 72.397 1.00 17.24 ? 196 PHE A CB 1 ATOM 1360 C CG . PHE A 1 195 ? 38.481 15.067 72.402 1.00 18.94 ? 196 PHE A CG 1 ATOM 1361 C CD1 . PHE A 1 195 ? 39.773 14.780 72.870 1.00 20.16 ? 196 PHE A CD1 1 ATOM 1362 C CD2 . PHE A 1 195 ? 38.173 16.383 72.056 1.00 20.45 ? 196 PHE A CD2 1 ATOM 1363 C CE1 . PHE A 1 195 ? 40.734 15.796 72.998 1.00 18.53 ? 196 PHE A CE1 1 ATOM 1364 C CE2 . PHE A 1 195 ? 39.120 17.404 72.180 1.00 20.86 ? 196 PHE A CE2 1 ATOM 1365 C CZ . PHE A 1 195 ? 40.400 17.113 72.653 1.00 18.84 ? 196 PHE A CZ 1 ATOM 1366 N N . ARG A 1 196 ? 39.105 12.824 69.627 1.00 17.64 ? 197 ARG A N 1 ATOM 1367 C CA . ARG A 1 196 ? 40.310 12.159 69.122 1.00 18.22 ? 197 ARG A CA 1 ATOM 1368 C C . ARG A 1 196 ? 40.150 10.754 68.548 1.00 18.73 ? 197 ARG A C 1 ATOM 1369 O O . ARG A 1 196 ? 41.108 9.967 68.518 1.00 19.64 ? 197 ARG A O 1 ATOM 1370 C CB . ARG A 1 196 ? 41.445 12.195 70.142 1.00 17.03 ? 197 ARG A CB 1 ATOM 1371 C CG . ARG A 1 196 ? 42.115 13.540 70.196 1.00 16.15 ? 197 ARG A CG 1 ATOM 1372 C CD . ARG A 1 196 ? 43.220 13.546 71.231 1.00 14.92 ? 197 ARG A CD 1 ATOM 1373 N NE . ARG A 1 196 ? 43.725 14.901 71.346 1.00 18.17 ? 197 ARG A NE 1 ATOM 1374 C CZ . ARG A 1 196 ? 44.582 15.323 72.261 1.00 19.05 ? 197 ARG A CZ 1 ATOM 1375 N NH1 . ARG A 1 196 ? 45.081 14.481 73.157 1.00 19.87 ? 197 ARG A NH1 1 ATOM 1376 N NH2 . ARG A 1 196 ? 44.843 16.617 72.344 1.00 20.89 ? 197 ARG A NH2 1 ATOM 1377 N N . SER A 1 197 ? 38.939 10.446 68.091 1.00 17.62 ? 198 SER A N 1 ATOM 1378 C CA . SER A 1 197 ? 38.666 9.180 67.442 1.00 16.00 ? 198 SER A CA 1 ATOM 1379 C C . SER A 1 197 ? 39.499 9.299 66.154 1.00 16.57 ? 198 SER A C 1 ATOM 1380 O O . SER A 1 197 ? 39.335 10.274 65.402 1.00 14.04 ? 198 SER A O 1 ATOM 1381 C CB . SER A 1 197 ? 37.188 9.089 67.068 1.00 16.53 ? 198 SER A CB 1 ATOM 1382 O OG . SER A 1 197 ? 36.846 10.172 66.215 1.00 17.00 ? 198 SER A OG 1 ATOM 1383 N N . PRO A 1 198 ? 40.377 8.304 65.874 1.00 16.74 ? 199 PRO A N 1 ATOM 1384 C CA . PRO A 1 198 ? 41.242 8.295 64.685 1.00 15.03 ? 199 PRO A CA 1 ATOM 1385 C C . PRO A 1 198 ? 40.523 8.049 63.377 1.00 15.19 ? 199 PRO A C 1 ATOM 1386 O O . PRO A 1 198 ? 39.460 7.413 63.339 1.00 15.82 ? 199 PRO A O 1 ATOM 1387 C CB . PRO A 1 198 ? 42.214 7.153 64.967 1.00 14.02 ? 199 PRO A CB 1 ATOM 1388 C CG . PRO A 1 198 ? 42.135 6.950 66.456 1.00 16.88 ? 199 PRO A CG 1 ATOM 1389 C CD . PRO A 1 198 ? 40.679 7.144 66.732 1.00 15.68 ? 199 PRO A CD 1 ATOM 1390 N N . LEU A 1 199 ? 41.164 8.482 62.302 1.00 12.05 ? 200 LEU A N 1 ATOM 1391 C CA . LEU A 1 199 ? 40.634 8.318 60.973 1.00 12.68 ? 200 LEU A CA 1 ATOM 1392 C C . LEU A 1 199 ? 41.082 6.972 60.378 1.00 13.29 ? 200 LEU A C 1 ATOM 1393 O O . LEU A 1 199 ? 40.619 6.577 59.300 1.00 13.03 ? 200 LEU A O 1 ATOM 1394 C CB . LEU A 1 199 ? 41.040 9.514 60.083 1.00 12.39 ? 200 LEU A CB 1 ATOM 1395 C CG . LEU A 1 199 ? 40.148 10.787 60.058 1.00 13.62 ? 200 LEU A CG 1 ATOM 1396 C CD1 . LEU A 1 199 ? 39.495 11.080 61.380 1.00 12.42 ? 200 LEU A CD1 1 ATOM 1397 C CD2 . LEU A 1 199 ? 40.915 11.994 59.558 1.00 10.46 ? 200 LEU A CD2 1 ATOM 1398 N N . ASP A 1 200 ? 42.049 6.316 61.015 1.00 14.01 ? 201 ASP A N 1 ATOM 1399 C CA . ASP A 1 200 ? 42.486 4.978 60.583 1.00 10.72 ? 201 ASP A CA 1 ATOM 1400 C C . ASP A 1 200 ? 42.959 4.187 61.798 1.00 12.06 ? 201 ASP A C 1 ATOM 1401 O O . ASP A 1 200 ? 43.061 4.750 62.888 1.00 9.68 ? 201 ASP A O 1 ATOM 1402 C CB . ASP A 1 200 ? 43.424 4.961 59.342 1.00 10.21 ? 201 ASP A CB 1 ATOM 1403 C CG . ASP A 1 200 ? 44.920 5.201 59.658 1.00 7.72 ? 201 ASP A CG 1 ATOM 1404 O OD1 . ASP A 1 200 ? 45.331 5.471 60.802 1.00 8.76 ? 201 ASP A OD1 1 ATOM 1405 O OD2 . ASP A 1 200 ? 45.684 5.099 58.692 1.00 6.31 ? 201 ASP A OD2 1 ATOM 1406 N N . SER A 1 201 ? 43.168 2.878 61.653 1.00 11.81 ? 202 SER A N 1 ATOM 1407 C CA . SER A 1 201 ? 43.556 2.082 62.809 1.00 14.06 ? 202 SER A CA 1 ATOM 1408 C C . SER A 1 201 ? 44.968 2.338 63.368 1.00 14.77 ? 202 SER A C 1 ATOM 1409 O O . SER A 1 201 ? 45.287 1.886 64.477 1.00 14.52 ? 202 SER A O 1 ATOM 1410 C CB . SER A 1 201 ? 43.346 0.582 62.526 1.00 16.03 ? 202 SER A CB 1 ATOM 1411 O OG . SER A 1 201 ? 43.968 0.211 61.299 1.00 15.95 ? 202 SER A OG 1 ATOM 1412 N N . THR A 1 202 ? 45.773 3.104 62.629 1.00 14.24 ? 203 THR A N 1 ATOM 1413 C CA . THR A 1 202 ? 47.157 3.417 63.007 1.00 13.02 ? 203 THR A CA 1 ATOM 1414 C C . THR A 1 202 ? 47.432 4.924 62.883 1.00 14.10 ? 203 THR A C 1 ATOM 1415 O O . THR A 1 202 ? 48.060 5.356 61.882 1.00 10.35 ? 203 THR A O 1 ATOM 1416 C CB . THR A 1 202 ? 48.113 2.707 62.058 1.00 11.76 ? 203 THR A CB 1 ATOM 1417 O OG1 . THR A 1 202 ? 47.773 3.045 60.711 1.00 12.17 ? 203 THR A OG1 1 ATOM 1418 C CG2 . THR A 1 202 ? 48.005 1.169 62.207 1.00 15.45 ? 203 THR A CG2 1 ATOM 1419 N N . PRO A 1 203 ? 46.890 5.742 63.819 1.00 16.51 ? 204 PRO A N 1 ATOM 1420 C CA . PRO A 1 203 ? 47.054 7.212 63.834 1.00 16.77 ? 204 PRO A CA 1 ATOM 1421 C C . PRO A 1 203 ? 48.484 7.643 64.132 1.00 17.75 ? 204 PRO A C 1 ATOM 1422 O O . PRO A 1 203 ? 48.784 8.828 64.045 1.00 17.91 ? 204 PRO A O 1 ATOM 1423 C CB . PRO A 1 203 ? 46.099 7.661 64.929 1.00 16.20 ? 204 PRO A CB 1 ATOM 1424 C CG . PRO A 1 203 ? 46.102 6.482 65.887 1.00 18.14 ? 204 PRO A CG 1 ATOM 1425 C CD . PRO A 1 203 ? 46.025 5.316 64.944 1.00 15.98 ? 204 PRO A CD 1 ATOM 1426 N N . GLN A 1 204 ? 49.339 6.690 64.534 1.00 18.04 ? 205 GLN A N 1 ATOM 1427 C CA . GLN A 1 204 ? 50.765 6.970 64.787 1.00 17.32 ? 205 GLN A CA 1 ATOM 1428 C C . GLN A 1 204 ? 51.677 6.295 63.730 1.00 16.74 ? 205 GLN A C 1 ATOM 1429 O O . GLN A 1 204 ? 52.899 6.252 63.888 1.00 18.69 ? 205 GLN A O 1 ATOM 1430 C CB . GLN A 1 204 ? 51.184 6.573 66.200 1.00 18.58 ? 205 GLN A CB 1 ATOM 1431 C CG . GLN A 1 204 ? 50.565 7.404 67.281 1.00 21.23 ? 205 GLN A CG 1 ATOM 1432 C CD . GLN A 1 204 ? 51.148 7.096 68.646 1.00 27.59 ? 205 GLN A CD 1 ATOM 1433 O OE1 . GLN A 1 204 ? 50.872 6.042 69.223 1.00 30.65 ? 205 GLN A OE1 1 ATOM 1434 N NE2 . GLN A 1 204 ? 51.958 8.016 69.177 1.00 28.38 ? 205 GLN A NE2 1 ATOM 1435 N N . VAL A 1 205 ? 51.090 5.824 62.631 1.00 14.20 ? 206 VAL A N 1 ATOM 1436 C CA . VAL A 1 205 ? 51.876 5.214 61.580 1.00 14.94 ? 206 VAL A CA 1 ATOM 1437 C C . VAL A 1 205 ? 51.479 5.755 60.211 1.00 16.05 ? 206 VAL A C 1 ATOM 1438 O O . VAL A 1 205 ? 50.332 5.609 59.781 1.00 16.93 ? 206 VAL A O 1 ATOM 1439 C CB . VAL A 1 205 ? 51.745 3.651 61.578 1.00 15.15 ? 206 VAL A CB 1 ATOM 1440 C CG1 . VAL A 1 205 ? 52.686 3.058 60.530 1.00 13.02 ? 206 VAL A CG1 1 ATOM 1441 C CG2 . VAL A 1 205 ? 52.055 3.079 62.962 1.00 13.97 ? 206 VAL A CG2 1 ATOM 1442 N N . PHE A 1 206 ? 52.437 6.317 59.488 1.00 14.40 ? 207 PHE A N 1 ATOM 1443 C CA . PHE A 1 206 ? 52.136 6.860 58.194 1.00 14.53 ? 207 PHE A CA 1 ATOM 1444 C C . PHE A 1 206 ? 52.112 5.651 57.259 1.00 17.05 ? 207 PHE A C 1 ATOM 1445 O O . PHE A 1 206 ? 53.131 5.202 56.730 1.00 16.88 ? 207 PHE A O 1 ATOM 1446 C CB . PHE A 1 206 ? 53.186 7.913 57.805 1.00 13.85 ? 207 PHE A CB 1 ATOM 1447 C CG . PHE A 1 206 ? 52.879 8.643 56.509 1.00 14.38 ? 207 PHE A CG 1 ATOM 1448 C CD1 . PHE A 1 206 ? 51.955 9.688 56.482 1.00 12.43 ? 207 PHE A CD1 1 ATOM 1449 C CD2 . PHE A 1 206 ? 53.501 8.270 55.321 1.00 13.14 ? 207 PHE A CD2 1 ATOM 1450 C CE1 . PHE A 1 206 ? 51.653 10.336 55.302 1.00 11.48 ? 207 PHE A CE1 1 ATOM 1451 C CE2 . PHE A 1 206 ? 53.209 8.920 54.109 1.00 14.07 ? 207 PHE A CE2 1 ATOM 1452 C CZ . PHE A 1 206 ? 52.285 9.950 54.099 1.00 12.61 ? 207 PHE A CZ 1 ATOM 1453 N N . ASP A 1 207 ? 50.907 5.138 57.052 1.00 18.24 ? 208 ASP A N 1 ATOM 1454 C CA . ASP A 1 207 ? 50.678 3.950 56.221 1.00 18.34 ? 208 ASP A CA 1 ATOM 1455 C C . ASP A 1 207 ? 49.395 4.040 55.363 1.00 16.62 ? 208 ASP A C 1 ATOM 1456 O O . ASP A 1 207 ? 48.599 4.970 55.512 1.00 14.68 ? 208 ASP A O 1 ATOM 1457 C CB . ASP A 1 207 ? 50.635 2.702 57.125 1.00 17.73 ? 208 ASP A CB 1 ATOM 1458 C CG . ASP A 1 207 ? 49.571 2.789 58.186 1.00 18.68 ? 208 ASP A CG 1 ATOM 1459 O OD1 . ASP A 1 207 ? 48.681 3.672 58.086 1.00 20.83 ? 208 ASP A OD1 1 ATOM 1460 O OD2 . ASP A 1 207 ? 49.601 1.965 59.125 1.00 17.68 ? 208 ASP A OD2 1 ATOM 1461 N N . THR A 1 208 ? 49.204 3.070 54.481 1.00 14.67 ? 209 THR A N 1 ATOM 1462 C CA . THR A 1 208 ? 48.043 3.041 53.592 1.00 15.51 ? 209 THR A CA 1 ATOM 1463 C C . THR A 1 208 ? 46.709 2.656 54.243 1.00 13.58 ? 209 THR A C 1 ATOM 1464 O O . THR A 1 208 ? 45.707 2.590 53.545 1.00 15.87 ? 209 THR A O 1 ATOM 1465 C CB . THR A 1 208 ? 48.277 2.075 52.424 1.00 16.30 ? 209 THR A CB 1 ATOM 1466 O OG1 . THR A 1 208 ? 48.402 0.726 52.930 1.00 17.90 ? 209 THR A OG1 1 ATOM 1467 C CG2 . THR A 1 208 ? 49.532 2.475 51.654 1.00 16.64 ? 209 THR A CG2 1 ATOM 1468 N N . GLN A 1 209 ? 46.699 2.362 55.540 1.00 12.24 ? 210 GLN A N 1 ATOM 1469 C CA . GLN A 1 209 ? 45.466 1.979 56.232 1.00 13.83 ? 210 GLN A CA 1 ATOM 1470 C C . GLN A 1 209 ? 44.260 2.916 55.983 1.00 15.69 ? 210 GLN A C 1 ATOM 1471 O O . GLN A 1 209 ? 43.139 2.461 55.800 1.00 16.02 ? 210 GLN A O 1 ATOM 1472 C CB . GLN A 1 209 ? 45.712 1.811 57.732 1.00 11.85 ? 210 GLN A CB 1 ATOM 1473 C CG . GLN A 1 209 ? 46.551 0.575 58.106 1.00 14.67 ? 210 GLN A CG 1 ATOM 1474 C CD . GLN A 1 209 ? 46.125 -0.732 57.381 1.00 16.49 ? 210 GLN A CD 1 ATOM 1475 O OE1 . GLN A 1 209 ? 46.945 -1.362 56.719 1.00 17.53 ? 210 GLN A OE1 1 ATOM 1476 N NE2 . GLN A 1 209 ? 44.860 -1.129 57.512 1.00 13.25 ? 210 GLN A NE2 1 ATOM 1477 N N . PHE A 1 210 ? 44.518 4.218 55.930 1.00 15.51 ? 211 PHE A N 1 ATOM 1478 C CA . PHE A 1 210 ? 43.486 5.225 55.692 1.00 14.04 ? 211 PHE A CA 1 ATOM 1479 C C . PHE A 1 210 ? 42.771 4.981 54.390 1.00 12.72 ? 211 PHE A C 1 ATOM 1480 O O . PHE A 1 210 ? 41.556 5.038 54.341 1.00 14.23 ? 211 PHE A O 1 ATOM 1481 C CB . PHE A 1 210 ? 44.106 6.651 55.704 1.00 14.08 ? 211 PHE A CB 1 ATOM 1482 C CG . PHE A 1 210 ? 43.175 7.729 55.211 1.00 13.32 ? 211 PHE A CG 1 ATOM 1483 C CD1 . PHE A 1 210 ? 42.098 8.150 55.989 1.00 11.59 ? 211 PHE A CD1 1 ATOM 1484 C CD2 . PHE A 1 210 ? 43.391 8.325 53.958 1.00 13.35 ? 211 PHE A CD2 1 ATOM 1485 C CE1 . PHE A 1 210 ? 41.232 9.168 55.524 1.00 10.11 ? 211 PHE A CE1 1 ATOM 1486 C CE2 . PHE A 1 210 ? 42.541 9.334 53.477 1.00 12.83 ? 211 PHE A CE2 1 ATOM 1487 C CZ . PHE A 1 210 ? 41.464 9.752 54.264 1.00 11.07 ? 211 PHE A CZ 1 ATOM 1488 N N . TYR A 1 211 ? 43.520 4.718 53.329 1.00 12.40 ? 212 TYR A N 1 ATOM 1489 C CA . TYR A 1 211 ? 42.912 4.489 52.033 1.00 14.96 ? 212 TYR A CA 1 ATOM 1490 C C . TYR A 1 211 ? 42.096 3.204 52.007 1.00 15.31 ? 212 TYR A C 1 ATOM 1491 O O . TYR A 1 211 ? 41.033 3.129 51.397 1.00 15.97 ? 212 TYR A O 1 ATOM 1492 C CB . TYR A 1 211 ? 43.984 4.486 50.933 1.00 14.72 ? 212 TYR A CB 1 ATOM 1493 C CG . TYR A 1 211 ? 44.660 5.837 50.774 1.00 16.35 ? 212 TYR A CG 1 ATOM 1494 C CD1 . TYR A 1 211 ? 44.047 6.871 50.046 1.00 16.29 ? 212 TYR A CD1 1 ATOM 1495 C CD2 . TYR A 1 211 ? 45.907 6.084 51.338 1.00 17.58 ? 212 TYR A CD2 1 ATOM 1496 C CE1 . TYR A 1 211 ? 44.668 8.110 49.877 1.00 13.97 ? 212 TYR A CE1 1 ATOM 1497 C CE2 . TYR A 1 211 ? 46.539 7.313 51.172 1.00 15.44 ? 212 TYR A CE2 1 ATOM 1498 C CZ . TYR A 1 211 ? 45.920 8.316 50.439 1.00 16.68 ? 212 TYR A CZ 1 ATOM 1499 O OH . TYR A 1 211 ? 46.602 9.490 50.225 1.00 15.59 ? 212 TYR A OH 1 ATOM 1500 N N . ILE A 1 212 ? 42.595 2.192 52.694 1.00 16.01 ? 213 ILE A N 1 ATOM 1501 C CA . ILE A 1 212 ? 41.916 0.894 52.748 1.00 15.23 ? 213 ILE A CA 1 ATOM 1502 C C . ILE A 1 212 ? 40.638 0.992 53.578 1.00 14.43 ? 213 ILE A C 1 ATOM 1503 O O . ILE A 1 212 ? 39.570 0.589 53.131 1.00 16.19 ? 213 ILE A O 1 ATOM 1504 C CB . ILE A 1 212 ? 42.834 -0.169 53.428 1.00 15.37 ? 213 ILE A CB 1 ATOM 1505 C CG1 . ILE A 1 212 ? 44.027 -0.499 52.521 1.00 14.13 ? 213 ILE A CG1 1 ATOM 1506 C CG2 . ILE A 1 212 ? 42.042 -1.403 53.835 1.00 13.60 ? 213 ILE A CG2 1 ATOM 1507 C CD1 . ILE A 1 212 ? 45.101 -1.348 53.233 1.00 12.51 ? 213 ILE A CD1 1 ATOM 1508 N N . GLU A 1 213 ? 40.776 1.473 54.803 1.00 11.92 ? 214 GLU A N 1 ATOM 1509 C CA . GLU A 1 213 ? 39.677 1.576 55.721 1.00 12.26 ? 214 GLU A CA 1 ATOM 1510 C C . GLU A 1 213 ? 38.514 2.475 55.325 1.00 14.64 ? 214 GLU A C 1 ATOM 1511 O O . GLU A 1 213 ? 37.372 2.155 55.660 1.00 14.01 ? 214 GLU A O 1 ATOM 1512 C CB . GLU A 1 213 ? 40.212 1.854 57.108 1.00 11.21 ? 214 GLU A CB 1 ATOM 1513 C CG . GLU A 1 213 ? 41.116 0.729 57.521 1.00 11.72 ? 214 GLU A CG 1 ATOM 1514 C CD . GLU A 1 213 ? 41.860 0.946 58.817 1.00 12.11 ? 214 GLU A CD 1 ATOM 1515 O OE1 . GLU A 1 213 ? 42.802 0.172 59.080 1.00 14.95 ? 214 GLU A OE1 1 ATOM 1516 O OE2 . GLU A 1 213 ? 41.522 1.845 59.593 1.00 13.00 ? 214 GLU A OE2 1 ATOM 1517 N N . THR A 1 214 ? 38.779 3.555 54.585 1.00 14.32 ? 215 THR A N 1 ATOM 1518 C CA . THR A 1 214 ? 37.708 4.446 54.140 1.00 15.28 ? 215 THR A CA 1 ATOM 1519 C C . THR A 1 214 ? 36.897 3.834 52.998 1.00 15.00 ? 215 THR A C 1 ATOM 1520 O O . THR A 1 214 ? 35.817 4.318 52.660 1.00 16.08 ? 215 THR A O 1 ATOM 1521 C CB . THR A 1 214 ? 38.233 5.830 53.683 1.00 14.25 ? 215 THR A CB 1 ATOM 1522 O OG1 . THR A 1 214 ? 39.260 5.638 52.725 1.00 18.63 ? 215 THR A OG1 1 ATOM 1523 C CG2 . THR A 1 214 ? 38.783 6.629 54.836 1.00 13.07 ? 215 THR A CG2 1 ATOM 1524 N N . LEU A 1 215 ? 37.440 2.802 52.370 1.00 14.37 ? 216 LEU A N 1 ATOM 1525 C CA . LEU A 1 215 ? 36.753 2.134 51.273 1.00 16.84 ? 216 LEU A CA 1 ATOM 1526 C C . LEU A 1 215 ? 35.875 0.969 51.738 1.00 17.00 ? 216 LEU A C 1 ATOM 1527 O O . LEU A 1 215 ? 35.170 0.380 50.947 1.00 19.11 ? 216 LEU A O 1 ATOM 1528 C CB . LEU A 1 215 ? 37.757 1.643 50.237 1.00 15.40 ? 216 LEU A CB 1 ATOM 1529 C CG . LEU A 1 215 ? 38.176 2.606 49.140 1.00 17.99 ? 216 LEU A CG 1 ATOM 1530 C CD1 . LEU A 1 215 ? 39.386 2.019 48.353 1.00 16.55 ? 216 LEU A CD1 1 ATOM 1531 C CD2 . LEU A 1 215 ? 36.984 2.871 48.215 1.00 18.47 ? 216 LEU A CD2 1 ATOM 1532 N N . LEU A 1 216 ? 35.959 0.605 53.003 1.00 17.78 ? 217 LEU A N 1 ATOM 1533 C CA . LEU A 1 216 ? 35.145 -0.472 53.526 1.00 18.98 ? 217 LEU A CA 1 ATOM 1534 C C . LEU A 1 216 ? 33.698 0.041 53.694 1.00 22.16 ? 217 LEU A C 1 ATOM 1535 O O . LEU A 1 216 ? 33.453 1.266 53.799 1.00 20.20 ? 217 LEU A O 1 ATOM 1536 C CB . LEU A 1 216 ? 35.690 -0.936 54.890 1.00 16.94 ? 217 LEU A CB 1 ATOM 1537 C CG . LEU A 1 216 ? 37.063 -1.642 54.977 1.00 18.00 ? 217 LEU A CG 1 ATOM 1538 C CD1 . LEU A 1 216 ? 37.546 -1.732 56.423 1.00 13.42 ? 217 LEU A CD1 1 ATOM 1539 C CD2 . LEU A 1 216 ? 36.959 -3.029 54.343 1.00 16.97 ? 217 LEU A CD2 1 ATOM 1540 N N . LYS A 1 217 ? 32.744 -0.891 53.707 1.00 20.83 ? 218 LYS A N 1 ATOM 1541 C CA . LYS A 1 217 ? 31.347 -0.534 53.898 1.00 19.85 ? 218 LYS A CA 1 ATOM 1542 C C . LYS A 1 217 ? 31.199 0.101 55.266 1.00 18.67 ? 218 LYS A C 1 ATOM 1543 O O . LYS A 1 217 ? 31.763 -0.405 56.253 1.00 17.39 ? 218 LYS A O 1 ATOM 1544 C CB . LYS A 1 217 ? 30.455 -1.782 53.832 1.00 20.71 ? 218 LYS A CB 1 ATOM 1545 C CG . LYS A 1 217 ? 30.389 -2.397 52.450 1.00 28.19 ? 218 LYS A CG 1 ATOM 1546 C CD . LYS A 1 217 ? 29.654 -3.736 52.494 1.00 33.48 ? 218 LYS A CD 1 ATOM 1547 C CE . LYS A 1 217 ? 29.538 -4.375 51.110 1.00 37.47 ? 218 LYS A CE 1 ATOM 1548 N NZ . LYS A 1 217 ? 29.042 -5.805 51.200 1.00 40.79 ? 218 LYS A NZ 1 ATOM 1549 N N . GLY A 1 218 ? 30.463 1.215 55.344 1.00 17.56 ? 219 GLY A N 1 ATOM 1550 C CA . GLY A 1 218 ? 30.257 1.846 56.637 1.00 16.74 ? 219 GLY A CA 1 ATOM 1551 C C . GLY A 1 218 ? 29.181 1.057 57.346 1.00 17.60 ? 219 GLY A C 1 ATOM 1552 O O . GLY A 1 218 ? 28.109 0.844 56.784 1.00 19.79 ? 219 GLY A O 1 ATOM 1553 N N . THR A 1 219 ? 29.439 0.619 58.567 1.00 18.62 ? 220 THR A N 1 ATOM 1554 C CA . THR A 1 219 ? 28.467 -0.202 59.300 1.00 19.65 ? 220 THR A CA 1 ATOM 1555 C C . THR A 1 219 ? 28.289 0.235 60.747 1.00 19.68 ? 220 THR A C 1 ATOM 1556 O O . THR A 1 219 ? 27.319 -0.138 61.401 1.00 21.78 ? 220 THR A O 1 ATOM 1557 C CB . THR A 1 219 ? 28.951 -1.716 59.378 1.00 20.02 ? 220 THR A CB 1 ATOM 1558 O OG1 . THR A 1 219 ? 30.188 -1.796 60.103 1.00 18.55 ? 220 THR A OG1 1 ATOM 1559 C CG2 . THR A 1 219 ? 29.152 -2.314 58.008 1.00 17.11 ? 220 THR A CG2 1 ATOM 1560 N N . THR A 1 220 ? 29.181 1.089 61.220 1.00 17.98 ? 221 THR A N 1 ATOM 1561 C CA . THR A 1 220 ? 29.175 1.455 62.611 1.00 18.91 ? 221 THR A CA 1 ATOM 1562 C C . THR A 1 220 ? 29.088 2.942 62.898 1.00 20.07 ? 221 THR A C 1 ATOM 1563 O O . THR A 1 220 ? 29.608 3.764 62.143 1.00 21.14 ? 221 THR A O 1 ATOM 1564 C CB . THR A 1 220 ? 30.469 0.880 63.239 1.00 19.70 ? 221 THR A CB 1 ATOM 1565 O OG1 . THR A 1 220 ? 30.581 -0.495 62.865 1.00 25.70 ? 221 THR A OG1 1 ATOM 1566 C CG2 . THR A 1 220 ? 30.489 0.999 64.727 1.00 16.81 ? 221 THR A CG2 1 ATOM 1567 N N . GLN A 1 221 ? 28.370 3.263 63.969 1.00 20.65 ? 222 GLN A N 1 ATOM 1568 C CA . GLN A 1 221 ? 28.220 4.627 64.471 1.00 22.53 ? 222 GLN A CA 1 ATOM 1569 C C . GLN A 1 221 ? 29.031 4.531 65.761 1.00 21.49 ? 222 GLN A C 1 ATOM 1570 O O . GLN A 1 221 ? 28.591 3.983 66.767 1.00 21.91 ? 222 GLN A O 1 ATOM 1571 C CB . GLN A 1 221 ? 26.758 4.951 64.789 1.00 24.79 ? 222 GLN A CB 1 ATOM 1572 C CG . GLN A 1 221 ? 26.595 6.348 65.348 1.00 28.39 ? 222 GLN A CG 1 ATOM 1573 C CD . GLN A 1 221 ? 25.195 6.646 65.837 1.00 30.18 ? 222 GLN A CD 1 ATOM 1574 O OE1 . GLN A 1 221 ? 24.240 6.649 65.063 1.00 32.81 ? 222 GLN A OE1 1 ATOM 1575 N NE2 . GLN A 1 221 ? 25.069 6.918 67.125 1.00 32.03 ? 222 GLN A NE2 1 ATOM 1576 N N . PRO A 1 222 ? 30.251 5.060 65.744 1.00 21.74 ? 223 PRO A N 1 ATOM 1577 C CA . PRO A 1 222 ? 31.116 4.992 66.923 1.00 20.94 ? 223 PRO A CA 1 ATOM 1578 C C . PRO A 1 222 ? 30.728 5.798 68.137 1.00 21.32 ? 223 PRO A C 1 ATOM 1579 O O . PRO A 1 222 ? 31.099 5.458 69.252 1.00 20.63 ? 223 PRO A O 1 ATOM 1580 C CB . PRO A 1 222 ? 32.467 5.424 66.365 1.00 21.10 ? 223 PRO A CB 1 ATOM 1581 C CG . PRO A 1 222 ? 32.071 6.424 65.294 1.00 21.20 ? 223 PRO A CG 1 ATOM 1582 C CD . PRO A 1 222 ? 30.915 5.736 64.612 1.00 21.66 ? 223 PRO A CD 1 ATOM 1583 N N . GLY A 1 223 ? 29.973 6.862 67.922 1.00 21.39 ? 224 GLY A N 1 ATOM 1584 C CA . GLY A 1 223 ? 29.605 7.712 69.024 1.00 22.33 ? 224 GLY A CA 1 ATOM 1585 C C . GLY A 1 223 ? 28.136 7.619 69.328 1.00 24.50 ? 224 GLY A C 1 ATOM 1586 O O . GLY A 1 223 ? 27.395 6.934 68.610 1.00 24.19 ? 224 GLY A O 1 ATOM 1587 N N . PRO A 1 224 ? 27.689 8.344 70.372 1.00 26.30 ? 225 PRO A N 1 ATOM 1588 C CA . PRO A 1 224 ? 26.316 8.434 70.887 1.00 26.35 ? 225 PRO A CA 1 ATOM 1589 C C . PRO A 1 224 ? 25.388 8.899 69.787 1.00 25.94 ? 225 PRO A C 1 ATOM 1590 O O . PRO A 1 224 ? 24.235 8.466 69.706 1.00 25.20 ? 225 PRO A O 1 ATOM 1591 C CB . PRO A 1 224 ? 26.439 9.474 71.997 1.00 26.49 ? 225 PRO A CB 1 ATOM 1592 C CG . PRO A 1 224 ? 27.845 9.286 72.484 1.00 26.78 ? 225 PRO A CG 1 ATOM 1593 C CD . PRO A 1 224 ? 28.598 9.181 71.181 1.00 25.49 ? 225 PRO A CD 1 ATOM 1594 N N . SER A 1 225 ? 25.935 9.728 68.904 1.00 24.99 ? 226 SER A N 1 ATOM 1595 C CA . SER A 1 225 ? 25.196 10.253 67.776 1.00 24.62 ? 226 SER A CA 1 ATOM 1596 C C . SER A 1 225 ? 26.168 10.590 66.654 1.00 23.51 ? 226 SER A C 1 ATOM 1597 O O . SER A 1 225 ? 27.379 10.478 66.829 1.00 21.99 ? 226 SER A O 1 ATOM 1598 C CB . SER A 1 225 ? 24.429 11.507 68.196 1.00 27.36 ? 226 SER A CB 1 ATOM 1599 O OG . SER A 1 225 ? 25.318 12.494 68.690 1.00 31.64 ? 226 SER A OG 1 ATOM 1600 N N . LEU A 1 226 ? 25.620 10.977 65.504 1.00 22.29 ? 227 LEU A N 1 ATOM 1601 C CA . LEU A 1 226 ? 26.400 11.345 64.334 1.00 20.90 ? 227 LEU A CA 1 ATOM 1602 C C . LEU A 1 226 ? 26.714 12.828 64.417 1.00 21.62 ? 227 LEU A C 1 ATOM 1603 O O . LEU A 1 226 ? 25.809 13.629 64.607 1.00 23.55 ? 227 LEU A O 1 ATOM 1604 C CB . LEU A 1 226 ? 25.578 11.080 63.091 1.00 21.08 ? 227 LEU A CB 1 ATOM 1605 C CG . LEU A 1 226 ? 25.976 9.910 62.197 1.00 23.66 ? 227 LEU A CG 1 ATOM 1606 C CD1 . LEU A 1 226 ? 26.973 9.011 62.881 1.00 25.25 ? 227 LEU A CD1 1 ATOM 1607 C CD2 . LEU A 1 226 ? 24.732 9.151 61.763 1.00 25.29 ? 227 LEU A CD2 1 ATOM 1608 N N . GLY A 1 227 ? 27.991 13.192 64.301 1.00 19.08 ? 228 GLY A N 1 ATOM 1609 C CA . GLY A 1 227 ? 28.389 14.583 64.378 1.00 15.12 ? 228 GLY A CA 1 ATOM 1610 C C . GLY A 1 227 ? 28.307 15.251 63.032 1.00 14.85 ? 228 GLY A C 1 ATOM 1611 O O . GLY A 1 227 ? 27.780 14.689 62.070 1.00 16.34 ? 228 GLY A O 1 ATOM 1612 N N . PHE A 1 228 ? 28.882 16.441 62.941 1.00 14.10 ? 229 PHE A N 1 ATOM 1613 C CA . PHE A 1 228 ? 28.874 17.176 61.697 1.00 13.12 ? 229 PHE A CA 1 ATOM 1614 C C . PHE A 1 228 ? 29.765 16.445 60.707 1.00 14.85 ? 229 PHE A C 1 ATOM 1615 O O . PHE A 1 228 ? 30.888 16.069 61.044 1.00 13.10 ? 229 PHE A O 1 ATOM 1616 C CB . PHE A 1 228 ? 29.429 18.593 61.911 1.00 12.73 ? 229 PHE A CB 1 ATOM 1617 C CG . PHE A 1 228 ? 29.551 19.379 60.644 1.00 15.33 ? 229 PHE A CG 1 ATOM 1618 C CD1 . PHE A 1 228 ? 28.489 19.427 59.735 1.00 13.45 ? 229 PHE A CD1 1 ATOM 1619 C CD2 . PHE A 1 228 ? 30.745 20.031 60.312 1.00 16.44 ? 229 PHE A CD2 1 ATOM 1620 C CE1 . PHE A 1 228 ? 28.609 20.100 58.509 1.00 15.66 ? 229 PHE A CE1 1 ATOM 1621 C CE2 . PHE A 1 228 ? 30.870 20.711 59.072 1.00 15.11 ? 229 PHE A CE2 1 ATOM 1622 C CZ . PHE A 1 228 ? 29.801 20.739 58.178 1.00 13.78 ? 229 PHE A CZ 1 ATOM 1623 N N . ALA A 1 229 ? 29.255 16.255 59.495 1.00 13.33 ? 230 ALA A N 1 ATOM 1624 C CA . ALA A 1 229 ? 29.992 15.591 58.422 1.00 16.51 ? 230 ALA A CA 1 ATOM 1625 C C . ALA A 1 229 ? 30.514 14.185 58.770 1.00 17.01 ? 230 ALA A C 1 ATOM 1626 O O . ALA A 1 229 ? 31.548 13.741 58.246 1.00 17.86 ? 230 ALA A O 1 ATOM 1627 C CB . ALA A 1 229 ? 31.148 16.506 57.910 1.00 15.06 ? 230 ALA A CB 1 ATOM 1628 N N . GLU A 1 230 ? 29.782 13.492 59.638 1.00 16.67 ? 231 GLU A N 1 ATOM 1629 C CA . GLU A 1 230 ? 30.148 12.146 60.028 1.00 16.85 ? 231 GLU A CA 1 ATOM 1630 C C . GLU A 1 230 ? 29.338 11.068 59.284 1.00 17.88 ? 231 GLU A C 1 ATOM 1631 O O . GLU A 1 230 ? 28.121 11.205 59.102 1.00 17.40 ? 231 GLU A O 1 ATOM 1632 C CB . GLU A 1 230 ? 29.973 11.959 61.524 1.00 14.13 ? 231 GLU A CB 1 ATOM 1633 C CG . GLU A 1 230 ? 30.331 10.575 61.953 1.00 11.88 ? 231 GLU A CG 1 ATOM 1634 C CD . GLU A 1 230 ? 30.348 10.377 63.434 1.00 15.12 ? 231 GLU A CD 1 ATOM 1635 O OE1 . GLU A 1 230 ? 30.117 11.315 64.214 1.00 17.89 ? 231 GLU A OE1 1 ATOM 1636 O OE2 . GLU A 1 230 ? 30.611 9.240 63.848 1.00 22.00 ? 231 GLU A OE2 1 ATOM 1637 N N . GLU A 1 231 ? 30.044 10.072 58.748 1.00 16.28 ? 232 GLU A N 1 ATOM 1638 C CA . GLU A 1 231 ? 29.435 8.929 58.070 1.00 17.36 ? 232 GLU A CA 1 ATOM 1639 C C . GLU A 1 231 ? 29.660 7.702 58.967 1.00 17.46 ? 232 GLU A C 1 ATOM 1640 O O . GLU A 1 231 ? 30.411 7.742 59.944 1.00 19.39 ? 232 GLU A O 1 ATOM 1641 C CB . GLU A 1 231 ? 30.107 8.675 56.727 1.00 19.67 ? 232 GLU A CB 1 ATOM 1642 C CG . GLU A 1 231 ? 30.013 9.808 55.738 1.00 25.40 ? 232 GLU A CG 1 ATOM 1643 C CD . GLU A 1 231 ? 28.597 10.014 55.217 1.00 29.25 ? 232 GLU A CD 1 ATOM 1644 O OE1 . GLU A 1 231 ? 28.092 9.143 54.493 1.00 33.93 ? 232 GLU A OE1 1 ATOM 1645 O OE2 . GLU A 1 231 ? 27.987 11.058 55.495 1.00 30.27 ? 232 GLU A OE2 1 ATOM 1646 N N . LEU A 1 232 ? 28.999 6.602 58.657 1.00 18.47 ? 233 LEU A N 1 ATOM 1647 C CA . LEU A 1 232 ? 29.173 5.378 59.436 1.00 18.33 ? 233 LEU A CA 1 ATOM 1648 C C . LEU A 1 232 ? 30.592 4.876 59.083 1.00 16.55 ? 233 LEU A C 1 ATOM 1649 O O . LEU A 1 232 ? 31.009 4.979 57.919 1.00 15.89 ? 233 LEU A O 1 ATOM 1650 C CB . LEU A 1 232 ? 28.123 4.354 58.981 1.00 18.31 ? 233 LEU A CB 1 ATOM 1651 C CG . LEU A 1 232 ? 26.836 4.018 59.757 1.00 18.60 ? 233 LEU A CG 1 ATOM 1652 C CD1 . LEU A 1 232 ? 26.431 5.013 60.787 1.00 16.72 ? 233 LEU A CD1 1 ATOM 1653 C CD2 . LEU A 1 232 ? 25.749 3.783 58.747 1.00 20.21 ? 233 LEU A CD2 1 ATOM 1654 N N . SER A 1 233 ? 31.328 4.348 60.059 1.00 17.77 ? 234 SER A N 1 ATOM 1655 C CA . SER A 1 233 ? 32.685 3.843 59.803 1.00 19.41 ? 234 SER A CA 1 ATOM 1656 C C . SER A 1 233 ? 32.669 2.306 59.795 1.00 21.33 ? 234 SER A C 1 ATOM 1657 O O . SER A 1 233 ? 31.600 1.691 59.972 1.00 20.45 ? 234 SER A O 1 ATOM 1658 C CB . SER A 1 233 ? 33.672 4.364 60.843 1.00 15.28 ? 234 SER A CB 1 ATOM 1659 O OG . SER A 1 233 ? 33.390 3.820 62.098 1.00 15.64 ? 234 SER A OG 1 ATOM 1660 N N . PRO A 1 234 ? 33.836 1.655 59.578 1.00 22.19 ? 235 PRO A N 1 ATOM 1661 C CA . PRO A 1 234 ? 33.821 0.181 59.560 1.00 22.35 ? 235 PRO A CA 1 ATOM 1662 C C . PRO A 1 234 ? 33.954 -0.569 60.887 1.00 21.96 ? 235 PRO A C 1 ATOM 1663 O O . PRO A 1 234 ? 33.744 -1.792 60.937 1.00 23.32 ? 235 PRO A O 1 ATOM 1664 C CB . PRO A 1 234 ? 34.929 -0.156 58.565 1.00 21.16 ? 235 PRO A CB 1 ATOM 1665 C CG . PRO A 1 234 ? 35.940 0.906 58.841 1.00 23.20 ? 235 PRO A CG 1 ATOM 1666 C CD . PRO A 1 234 ? 35.108 2.178 59.037 1.00 22.70 ? 235 PRO A CD 1 ATOM 1667 N N . PHE A 1 235 ? 34.301 0.142 61.955 1.00 21.25 ? 236 PHE A N 1 ATOM 1668 C CA . PHE A 1 235 ? 34.449 -0.477 63.260 1.00 20.63 ? 236 PHE A CA 1 ATOM 1669 C C . PHE A 1 235 ? 34.452 0.514 64.401 1.00 19.88 ? 236 PHE A C 1 ATOM 1670 O O . PHE A 1 235 ? 34.586 1.713 64.195 1.00 20.24 ? 236 PHE A O 1 ATOM 1671 C CB . PHE A 1 235 ? 35.653 -1.463 63.355 1.00 22.92 ? 236 PHE A CB 1 ATOM 1672 C CG . PHE A 1 235 ? 36.823 -1.187 62.409 1.00 22.19 ? 236 PHE A CG 1 ATOM 1673 C CD1 . PHE A 1 235 ? 36.978 -1.944 61.231 1.00 22.44 ? 236 PHE A CD1 1 ATOM 1674 C CD2 . PHE A 1 235 ? 37.795 -0.239 62.720 1.00 21.13 ? 236 PHE A CD2 1 ATOM 1675 C CE1 . PHE A 1 235 ? 38.061 -1.764 60.389 1.00 21.20 ? 236 PHE A CE1 1 ATOM 1676 C CE2 . PHE A 1 235 ? 38.900 -0.052 61.869 1.00 20.45 ? 236 PHE A CE2 1 ATOM 1677 C CZ . PHE A 1 235 ? 39.026 -0.812 60.707 1.00 20.82 ? 236 PHE A CZ 1 ATOM 1678 N N . PRO A 1 236 ? 34.194 0.037 65.620 1.00 20.48 ? 237 PRO A N 1 ATOM 1679 C CA . PRO A 1 236 ? 34.163 0.906 66.802 1.00 20.95 ? 237 PRO A CA 1 ATOM 1680 C C . PRO A 1 236 ? 35.421 1.751 66.957 1.00 21.20 ? 237 PRO A C 1 ATOM 1681 O O . PRO A 1 236 ? 36.522 1.308 66.610 1.00 21.39 ? 237 PRO A O 1 ATOM 1682 C CB . PRO A 1 236 ? 34.036 -0.097 67.950 1.00 20.15 ? 237 PRO A CB 1 ATOM 1683 C CG . PRO A 1 236 ? 33.284 -1.220 67.330 1.00 19.34 ? 237 PRO A CG 1 ATOM 1684 C CD . PRO A 1 236 ? 33.934 -1.367 65.991 1.00 20.14 ? 237 PRO A CD 1 ATOM 1685 N N . GLY A 1 237 ? 35.260 2.969 67.456 1.00 19.30 ? 238 GLY A N 1 ATOM 1686 C CA . GLY A 1 237 ? 36.404 3.840 67.646 1.00 18.40 ? 238 GLY A CA 1 ATOM 1687 C C . GLY A 1 237 ? 36.887 4.646 66.450 1.00 16.34 ? 238 GLY A C 1 ATOM 1688 O O . GLY A 1 237 ? 37.505 5.690 66.643 1.00 18.14 ? 238 GLY A O 1 ATOM 1689 N N . GLU A 1 238 ? 36.646 4.162 65.234 1.00 16.05 ? 239 GLU A N 1 ATOM 1690 C CA . GLU A 1 238 ? 37.048 4.853 64.007 1.00 15.35 ? 239 GLU A CA 1 ATOM 1691 C C . GLU A 1 238 ? 36.010 5.852 63.516 1.00 16.84 ? 239 GLU A C 1 ATOM 1692 O O . GLU A 1 238 ? 34.833 5.515 63.387 1.00 16.56 ? 239 GLU A O 1 ATOM 1693 C CB . GLU A 1 238 ? 37.329 3.866 62.877 1.00 12.17 ? 239 GLU A CB 1 ATOM 1694 C CG . GLU A 1 238 ? 37.792 4.542 61.581 1.00 9.91 ? 239 GLU A CG 1 ATOM 1695 C CD . GLU A 1 238 ? 38.536 3.643 60.645 1.00 10.66 ? 239 GLU A CD 1 ATOM 1696 O OE1 . GLU A 1 238 ? 38.061 3.409 59.523 1.00 10.75 ? 239 GLU A OE1 1 ATOM 1697 O OE2 . GLU A 1 238 ? 39.649 3.222 61.003 1.00 12.67 ? 239 GLU A OE2 1 ATOM 1698 N N . PHE A 1 239 ? 36.454 7.068 63.208 1.00 15.01 ? 240 PHE A N 1 ATOM 1699 C CA . PHE A 1 239 ? 35.549 8.089 62.707 1.00 13.70 ? 240 PHE A CA 1 ATOM 1700 C C . PHE A 1 239 ? 35.733 8.167 61.209 1.00 11.59 ? 240 PHE A C 1 ATOM 1701 O O . PHE A 1 239 ? 36.849 7.993 60.722 1.00 13.48 ? 240 PHE A O 1 ATOM 1702 C CB . PHE A 1 239 ? 35.903 9.426 63.350 1.00 16.30 ? 240 PHE A CB 1 ATOM 1703 C CG . PHE A 1 239 ? 35.052 10.595 62.881 1.00 16.12 ? 240 PHE A CG 1 ATOM 1704 C CD1 . PHE A 1 239 ? 35.318 11.234 61.678 1.00 15.00 ? 240 PHE A CD1 1 ATOM 1705 C CD2 . PHE A 1 239 ? 34.046 11.099 63.691 1.00 15.75 ? 240 PHE A CD2 1 ATOM 1706 C CE1 . PHE A 1 239 ? 34.600 12.363 61.285 1.00 16.29 ? 240 PHE A CE1 1 ATOM 1707 C CE2 . PHE A 1 239 ? 33.335 12.216 63.315 1.00 15.64 ? 240 PHE A CE2 1 ATOM 1708 C CZ . PHE A 1 239 ? 33.609 12.853 62.111 1.00 16.14 ? 240 PHE A CZ 1 ATOM 1709 N N . ARG A 1 240 ? 34.649 8.357 60.455 1.00 9.95 ? 241 ARG A N 1 ATOM 1710 C CA . ARG A 1 240 ? 34.774 8.512 59.007 1.00 11.00 ? 241 ARG A CA 1 ATOM 1711 C C . ARG A 1 240 ? 34.159 9.853 58.614 1.00 14.12 ? 241 ARG A C 1 ATOM 1712 O O . ARG A 1 240 ? 32.992 10.092 58.913 1.00 13.14 ? 241 ARG A O 1 ATOM 1713 C CB . ARG A 1 240 ? 34.056 7.398 58.260 1.00 10.36 ? 241 ARG A CB 1 ATOM 1714 C CG . ARG A 1 240 ? 34.150 7.563 56.760 1.00 10.13 ? 241 ARG A CG 1 ATOM 1715 C CD . ARG A 1 240 ? 33.429 6.433 56.018 1.00 16.21 ? 241 ARG A CD 1 ATOM 1716 N NE . ARG A 1 240 ? 34.135 5.151 56.177 1.00 16.87 ? 241 ARG A NE 1 ATOM 1717 C CZ . ARG A 1 240 ? 33.826 4.015 55.546 1.00 17.40 ? 241 ARG A CZ 1 ATOM 1718 N NH1 . ARG A 1 240 ? 32.799 3.951 54.688 1.00 12.39 ? 241 ARG A NH1 1 ATOM 1719 N NH2 . ARG A 1 240 ? 34.590 2.945 55.761 1.00 12.40 ? 241 ARG A NH2 1 ATOM 1720 N N . MET A 1 241 ? 34.914 10.741 57.968 1.00 13.72 ? 242 MET A N 1 ATOM 1721 C CA . MET A 1 241 ? 34.314 12.008 57.589 1.00 13.05 ? 242 MET A CA 1 ATOM 1722 C C . MET A 1 241 ? 33.782 11.931 56.164 1.00 13.67 ? 242 MET A C 1 ATOM 1723 O O . MET A 1 241 ? 34.300 11.196 55.311 1.00 12.32 ? 242 MET A O 1 ATOM 1724 C CB . MET A 1 241 ? 35.249 13.226 57.830 1.00 14.97 ? 242 MET A CB 1 ATOM 1725 C CG . MET A 1 241 ? 36.261 13.542 56.762 1.00 14.41 ? 242 MET A CG 1 ATOM 1726 S SD . MET A 1 241 ? 37.222 15.055 57.188 1.00 15.72 ? 242 MET A SD 1 ATOM 1727 C CE . MET A 1 241 ? 38.213 14.448 58.506 1.00 11.67 ? 242 MET A CE 1 ATOM 1728 N N . ARG A 1 242 ? 32.695 12.647 55.924 1.00 12.74 ? 243 ARG A N 1 ATOM 1729 C CA . ARG A 1 242 ? 32.038 12.659 54.642 1.00 11.00 ? 243 ARG A CA 1 ATOM 1730 C C . ARG A 1 242 ? 32.896 12.919 53.419 1.00 11.23 ? 243 ARG A C 1 ATOM 1731 O O . ARG A 1 242 ? 32.784 12.213 52.409 1.00 9.54 ? 243 ARG A O 1 ATOM 1732 C CB . ARG A 1 242 ? 30.885 13.654 54.708 1.00 11.60 ? 243 ARG A CB 1 ATOM 1733 C CG . ARG A 1 242 ? 29.850 13.490 53.643 1.00 13.07 ? 243 ARG A CG 1 ATOM 1734 C CD . ARG A 1 242 ? 28.824 14.600 53.863 1.00 18.63 ? 243 ARG A CD 1 ATOM 1735 N NE . ARG A 1 242 ? 27.674 14.507 52.979 1.00 20.01 ? 243 ARG A NE 1 ATOM 1736 C CZ . ARG A 1 242 ? 27.561 15.114 51.800 1.00 22.20 ? 243 ARG A CZ 1 ATOM 1737 N NH1 . ARG A 1 242 ? 28.532 15.869 51.303 1.00 22.93 ? 243 ARG A NH1 1 ATOM 1738 N NH2 . ARG A 1 242 ? 26.402 15.064 51.166 1.00 22.04 ? 243 ARG A NH2 1 ATOM 1739 N N . SER A 1 243 ? 33.721 13.965 53.468 1.00 11.25 ? 244 SER A N 1 ATOM 1740 C CA . SER A 1 243 ? 34.573 14.289 52.327 1.00 11.08 ? 244 SER A CA 1 ATOM 1741 C C . SER A 1 243 ? 35.472 13.096 51.960 1.00 11.53 ? 244 SER A C 1 ATOM 1742 O O . SER A 1 243 ? 35.653 12.811 50.779 1.00 13.29 ? 244 SER A O 1 ATOM 1743 C CB . SER A 1 243 ? 35.446 15.530 52.630 1.00 10.05 ? 244 SER A CB 1 ATOM 1744 O OG . SER A 1 243 ? 36.035 15.421 53.920 1.00 9.06 ? 244 SER A OG 1 ATOM 1745 N N . ASP A 1 244 ? 36.067 12.441 52.961 1.00 11.24 ? 245 ASP A N 1 ATOM 1746 C CA . ASP A 1 244 ? 36.940 11.299 52.710 1.00 12.15 ? 245 ASP A CA 1 ATOM 1747 C C . ASP A 1 244 ? 36.157 10.144 52.092 1.00 12.62 ? 245 ASP A C 1 ATOM 1748 O O . ASP A 1 244 ? 36.580 9.572 51.102 1.00 14.68 ? 245 ASP A O 1 ATOM 1749 C CB . ASP A 1 244 ? 37.637 10.837 53.994 1.00 10.14 ? 245 ASP A CB 1 ATOM 1750 C CG . ASP A 1 244 ? 38.714 11.817 54.485 1.00 9.32 ? 245 ASP A CG 1 ATOM 1751 O OD1 . ASP A 1 244 ? 39.077 11.786 55.678 1.00 11.72 ? 245 ASP A OD1 1 ATOM 1752 O OD2 . ASP A 1 244 ? 39.201 12.612 53.681 1.00 13.27 ? 245 ASP A OD2 1 ATOM 1753 N N . ALA A 1 245 ? 34.995 9.836 52.665 1.00 13.07 ? 246 ALA A N 1 ATOM 1754 C CA . ALA A 1 245 ? 34.154 8.762 52.138 1.00 13.37 ? 246 ALA A CA 1 ATOM 1755 C C . ALA A 1 245 ? 33.753 9.081 50.703 1.00 14.24 ? 246 ALA A C 1 ATOM 1756 O O . ALA A 1 245 ? 33.742 8.186 49.861 1.00 14.72 ? 246 ALA A O 1 ATOM 1757 C CB . ALA A 1 245 ? 32.919 8.538 53.023 1.00 12.47 ? 246 ALA A CB 1 ATOM 1758 N N . LEU A 1 246 ? 33.494 10.359 50.386 1.00 12.60 ? 247 LEU A N 1 ATOM 1759 C CA . LEU A 1 246 ? 33.103 10.722 49.019 1.00 13.33 ? 247 LEU A CA 1 ATOM 1760 C C . LEU A 1 246 ? 34.255 10.649 48.007 1.00 14.31 ? 247 LEU A C 1 ATOM 1761 O O . LEU A 1 246 ? 34.073 10.202 46.860 1.00 13.12 ? 247 LEU A O 1 ATOM 1762 C CB . LEU A 1 246 ? 32.467 12.122 48.978 1.00 15.07 ? 247 LEU A CB 1 ATOM 1763 C CG . LEU A 1 246 ? 31.102 12.351 49.635 1.00 18.12 ? 247 LEU A CG 1 ATOM 1764 C CD1 . LEU A 1 246 ? 30.728 13.830 49.572 1.00 19.04 ? 247 LEU A CD1 1 ATOM 1765 C CD2 . LEU A 1 246 ? 30.079 11.523 48.910 1.00 19.82 ? 247 LEU A CD2 1 ATOM 1766 N N . LEU A 1 247 ? 35.434 11.138 48.411 1.00 14.85 ? 248 LEU A N 1 ATOM 1767 C CA . LEU A 1 247 ? 36.617 11.121 47.530 1.00 14.06 ? 248 LEU A CA 1 ATOM 1768 C C . LEU A 1 247 ? 37.070 9.696 47.219 1.00 11.06 ? 248 LEU A C 1 ATOM 1769 O O . LEU A 1 247 ? 37.555 9.441 46.132 1.00 11.70 ? 248 LEU A O 1 ATOM 1770 C CB . LEU A 1 247 ? 37.777 11.945 48.121 1.00 12.52 ? 248 LEU A CB 1 ATOM 1771 C CG . LEU A 1 247 ? 37.547 13.465 48.097 1.00 11.89 ? 248 LEU A CG 1 ATOM 1772 C CD1 . LEU A 1 247 ? 38.438 14.143 49.117 1.00 10.86 ? 248 LEU A CD1 1 ATOM 1773 C CD2 . LEU A 1 247 ? 37.768 14.027 46.686 1.00 11.01 ? 248 LEU A CD2 1 ATOM 1774 N N . ALA A 1 248 ? 36.876 8.783 48.160 1.00 11.07 ? 249 ALA A N 1 ATOM 1775 C CA . ALA A 1 248 ? 37.240 7.372 47.982 1.00 14.33 ? 249 ALA A CA 1 ATOM 1776 C C . ALA A 1 248 ? 36.398 6.728 46.904 1.00 15.79 ? 249 ALA A C 1 ATOM 1777 O O . ALA A 1 248 ? 36.865 5.898 46.138 1.00 17.09 ? 249 ALA A O 1 ATOM 1778 C CB . ALA A 1 248 ? 37.020 6.603 49.302 1.00 11.74 ? 249 ALA A CB 1 ATOM 1779 N N . ARG A 1 249 ? 35.162 7.191 46.795 1.00 19.28 ? 250 ARG A N 1 ATOM 1780 C CA . ARG A 1 249 ? 34.201 6.607 45.874 1.00 18.54 ? 250 ARG A CA 1 ATOM 1781 C C . ARG A 1 249 ? 33.887 7.342 44.595 1.00 19.88 ? 250 ARG A C 1 ATOM 1782 O O . ARG A 1 249 ? 33.344 6.750 43.672 1.00 21.84 ? 250 ARG A O 1 ATOM 1783 C CB . ARG A 1 249 ? 32.920 6.312 46.651 1.00 17.39 ? 250 ARG A CB 1 ATOM 1784 C CG . ARG A 1 249 ? 33.166 5.405 47.848 1.00 14.12 ? 250 ARG A CG 1 ATOM 1785 C CD . ARG A 1 249 ? 32.018 5.404 48.829 1.00 15.20 ? 250 ARG A CD 1 ATOM 1786 N NE . ARG A 1 249 ? 32.200 4.367 49.842 1.00 14.97 ? 250 ARG A NE 1 ATOM 1787 C CZ . ARG A 1 249 ? 33.107 4.401 50.819 1.00 17.56 ? 250 ARG A CZ 1 ATOM 1788 N NH1 . ARG A 1 249 ? 33.929 5.432 50.942 1.00 15.96 ? 250 ARG A NH1 1 ATOM 1789 N NH2 . ARG A 1 249 ? 33.253 3.356 51.634 1.00 16.12 ? 250 ARG A NH2 1 ATOM 1790 N N . ASP A 1 250 ? 34.264 8.609 44.515 1.00 19.15 ? 251 ASP A N 1 ATOM 1791 C CA . ASP A 1 250 ? 33.987 9.396 43.338 1.00 17.66 ? 251 ASP A CA 1 ATOM 1792 C C . ASP A 1 250 ? 34.763 8.882 42.130 1.00 18.40 ? 251 ASP A C 1 ATOM 1793 O O . ASP A 1 250 ? 35.929 8.547 42.243 1.00 17.34 ? 251 ASP A O 1 ATOM 1794 C CB . ASP A 1 250 ? 34.337 10.854 43.623 1.00 16.88 ? 251 ASP A CB 1 ATOM 1795 C CG . ASP A 1 250 ? 33.761 11.770 42.614 1.00 18.57 ? 251 ASP A CG 1 ATOM 1796 O OD1 . ASP A 1 250 ? 34.335 11.873 41.534 1.00 20.99 ? 251 ASP A OD1 1 ATOM 1797 O OD2 . ASP A 1 250 ? 32.703 12.372 42.863 1.00 22.56 ? 251 ASP A OD2 1 ATOM 1798 N N . SER A 1 251 ? 34.155 8.929 40.953 1.00 18.45 ? 252 SER A N 1 ATOM 1799 C CA . SER A 1 251 ? 34.796 8.441 39.745 1.00 21.47 ? 252 SER A CA 1 ATOM 1800 C C . SER A 1 251 ? 36.029 9.212 39.288 1.00 23.22 ? 252 SER A C 1 ATOM 1801 O O . SER A 1 251 ? 36.813 8.692 38.482 1.00 24.11 ? 252 SER A O 1 ATOM 1802 C CB . SER A 1 251 ? 33.793 8.387 38.602 1.00 20.47 ? 252 SER A CB 1 ATOM 1803 O OG . SER A 1 251 ? 33.550 9.677 38.080 1.00 25.23 ? 252 SER A OG 1 ATOM 1804 N N . ARG A 1 252 ? 36.170 10.468 39.733 1.00 24.11 ? 253 ARG A N 1 ATOM 1805 C CA . ARG A 1 252 ? 37.327 11.300 39.366 1.00 21.09 ? 253 ARG A CA 1 ATOM 1806 C C . ARG A 1 252 ? 38.536 11.033 40.238 1.00 19.57 ? 253 ARG A C 1 ATOM 1807 O O . ARG A 1 252 ? 39.656 11.394 39.865 1.00 19.63 ? 253 ARG A O 1 ATOM 1808 C CB . ARG A 1 252 ? 37.028 12.793 39.508 1.00 22.53 ? 253 ARG A CB 1 ATOM 1809 C CG . ARG A 1 252 ? 35.986 13.339 38.576 1.00 24.50 ? 253 ARG A CG 1 ATOM 1810 C CD . ARG A 1 252 ? 34.759 13.657 39.378 1.00 25.87 ? 253 ARG A CD 1 ATOM 1811 N NE . ARG A 1 252 ? 34.541 15.075 39.489 1.00 27.86 ? 253 ARG A NE 1 ATOM 1812 C CZ . ARG A 1 252 ? 33.673 15.645 40.324 1.00 28.56 ? 253 ARG A CZ 1 ATOM 1813 N NH1 . ARG A 1 252 ? 32.941 14.922 41.166 1.00 27.40 ? 253 ARG A NH1 1 ATOM 1814 N NH2 . ARG A 1 252 ? 33.455 16.946 40.230 1.00 30.16 ? 253 ARG A NH2 1 ATOM 1815 N N . THR A 1 253 ? 38.308 10.464 41.414 1.00 16.17 ? 254 THR A N 1 ATOM 1816 C CA . THR A 1 253 ? 39.385 10.219 42.346 1.00 16.21 ? 254 THR A CA 1 ATOM 1817 C C . THR A 1 253 ? 39.508 8.769 42.857 1.00 17.70 ? 254 THR A C 1 ATOM 1818 O O . THR A 1 253 ? 40.504 8.413 43.499 1.00 17.37 ? 254 THR A O 1 ATOM 1819 C CB . THR A 1 253 ? 39.209 11.168 43.559 1.00 17.30 ? 254 THR A CB 1 ATOM 1820 O OG1 . THR A 1 253 ? 37.881 11.050 44.077 1.00 15.87 ? 254 THR A OG1 1 ATOM 1821 C CG2 . THR A 1 253 ? 39.420 12.628 43.142 1.00 17.19 ? 254 THR A CG2 1 ATOM 1822 N N . ALA A 1 254 ? 38.531 7.923 42.537 1.00 17.43 ? 255 ALA A N 1 ATOM 1823 C CA . ALA A 1 254 ? 38.519 6.553 43.042 1.00 18.11 ? 255 ALA A CA 1 ATOM 1824 C C . ALA A 1 254 ? 39.697 5.675 42.637 1.00 17.62 ? 255 ALA A C 1 ATOM 1825 O O . ALA A 1 254 ? 40.177 4.851 43.445 1.00 16.46 ? 255 ALA A O 1 ATOM 1826 C CB . ALA A 1 254 ? 37.223 5.877 42.682 1.00 17.58 ? 255 ALA A CB 1 ATOM 1827 N N . CYS A 1 255 ? 40.142 5.823 41.397 1.00 17.40 ? 256 CYS A N 1 ATOM 1828 C CA . CYS A 1 255 ? 41.246 5.012 40.922 1.00 20.12 ? 256 CYS A CA 1 ATOM 1829 C C . CYS A 1 255 ? 42.581 5.368 41.605 1.00 19.46 ? 256 CYS A C 1 ATOM 1830 O O . CYS A 1 255 ? 43.356 4.471 41.979 1.00 19.50 ? 256 CYS A O 1 ATOM 1831 C CB . CYS A 1 255 ? 41.334 5.063 39.398 1.00 22.81 ? 256 CYS A CB 1 ATOM 1832 S SG . CYS A 1 255 ? 39.884 4.312 38.578 1.00 23.77 ? 256 CYS A SG 1 ATOM 1833 N N . ARG A 1 256 ? 42.812 6.656 41.844 1.00 16.19 ? 257 ARG A N 1 ATOM 1834 C CA . ARG A 1 256 ? 44.033 7.072 42.534 1.00 16.07 ? 257 ARG A CA 1 ATOM 1835 C C . ARG A 1 256 ? 43.974 6.582 43.982 1.00 13.81 ? 257 ARG A C 1 ATOM 1836 O O . ARG A 1 256 ? 44.944 6.024 44.490 1.00 15.39 ? 257 ARG A O 1 ATOM 1837 C CB . ARG A 1 256 ? 44.181 8.601 42.519 1.00 18.38 ? 257 ARG A CB 1 ATOM 1838 C CG . ARG A 1 256 ? 45.465 9.132 43.146 1.00 17.98 ? 257 ARG A CG 1 ATOM 1839 C CD . ARG A 1 256 ? 46.691 8.701 42.342 1.00 19.10 ? 257 ARG A CD 1 ATOM 1840 N NE . ARG A 1 256 ? 47.853 9.545 42.629 1.00 17.60 ? 257 ARG A NE 1 ATOM 1841 C CZ . ARG A 1 256 ? 48.905 9.644 41.824 1.00 18.38 ? 257 ARG A CZ 1 ATOM 1842 N NH1 . ARG A 1 256 ? 48.934 8.952 40.692 1.00 17.66 ? 257 ARG A NH1 1 ATOM 1843 N NH2 . ARG A 1 256 ? 49.916 10.452 42.120 1.00 14.68 ? 257 ARG A NH2 1 ATOM 1844 N N . TRP A 1 257 ? 42.817 6.726 44.625 1.00 11.21 ? 258 TRP A N 1 ATOM 1845 C CA . TRP A 1 257 ? 42.635 6.308 46.013 1.00 10.86 ? 258 TRP A CA 1 ATOM 1846 C C . TRP A 1 257 ? 42.912 4.794 46.107 1.00 15.18 ? 258 TRP A C 1 ATOM 1847 O O . TRP A 1 257 ? 43.620 4.307 47.005 1.00 14.59 ? 258 TRP A O 1 ATOM 1848 C CB . TRP A 1 257 ? 41.183 6.616 46.440 1.00 9.50 ? 258 TRP A CB 1 ATOM 1849 C CG . TRP A 1 257 ? 40.899 6.627 47.939 1.00 9.14 ? 258 TRP A CG 1 ATOM 1850 C CD1 . TRP A 1 257 ? 40.704 5.550 48.744 1.00 11.32 ? 258 TRP A CD1 1 ATOM 1851 C CD2 . TRP A 1 257 ? 40.754 7.775 48.778 1.00 11.61 ? 258 TRP A CD2 1 ATOM 1852 N NE1 . TRP A 1 257 ? 40.453 5.946 50.032 1.00 10.88 ? 258 TRP A NE1 1 ATOM 1853 C CE2 . TRP A 1 257 ? 40.472 7.314 50.082 1.00 10.43 ? 258 TRP A CE2 1 ATOM 1854 C CE3 . TRP A 1 257 ? 40.835 9.162 48.558 1.00 11.49 ? 258 TRP A CE3 1 ATOM 1855 C CZ2 . TRP A 1 257 ? 40.264 8.176 51.159 1.00 12.22 ? 258 TRP A CZ2 1 ATOM 1856 C CZ3 . TRP A 1 257 ? 40.631 10.017 49.644 1.00 11.13 ? 258 TRP A CZ3 1 ATOM 1857 C CH2 . TRP A 1 257 ? 40.353 9.519 50.920 1.00 10.92 ? 258 TRP A CH2 1 ATOM 1858 N N . GLN A 1 258 ? 42.372 4.052 45.144 1.00 18.92 ? 259 GLN A N 1 ATOM 1859 C CA . GLN A 1 258 ? 42.536 2.599 45.128 1.00 20.77 ? 259 GLN A CA 1 ATOM 1860 C C . GLN A 1 258 ? 44.000 2.237 44.995 1.00 18.71 ? 259 GLN A C 1 ATOM 1861 O O . GLN A 1 258 ? 44.478 1.350 45.700 1.00 20.43 ? 259 GLN A O 1 ATOM 1862 C CB . GLN A 1 258 ? 41.726 1.976 43.987 1.00 20.02 ? 259 GLN A CB 1 ATOM 1863 C CG . GLN A 1 258 ? 41.670 0.464 44.016 1.00 23.80 ? 259 GLN A CG 1 ATOM 1864 C CD . GLN A 1 258 ? 40.736 -0.071 42.939 1.00 24.76 ? 259 GLN A CD 1 ATOM 1865 O OE1 . GLN A 1 258 ? 39.515 0.095 43.023 1.00 26.34 ? 259 GLN A OE1 1 ATOM 1866 N NE2 . GLN A 1 258 ? 41.303 -0.655 41.902 1.00 24.50 ? 259 GLN A NE2 1 ATOM 1867 N N . SER A 1 259 ? 44.721 2.942 44.130 1.00 18.73 ? 260 SER A N 1 ATOM 1868 C CA . SER A 1 259 ? 46.146 2.653 43.948 1.00 19.70 ? 260 SER A CA 1 ATOM 1869 C C . SER A 1 259 ? 47.026 2.941 45.166 1.00 20.85 ? 260 SER A C 1 ATOM 1870 O O . SER A 1 259 ? 48.192 2.535 45.192 1.00 23.34 ? 260 SER A O 1 ATOM 1871 C CB . SER A 1 259 ? 46.695 3.390 42.748 1.00 19.11 ? 260 SER A CB 1 ATOM 1872 O OG . SER A 1 259 ? 46.775 4.781 43.007 1.00 23.79 ? 260 SER A OG 1 ATOM 1873 N N . MET A 1 260 ? 46.486 3.649 46.159 1.00 21.04 ? 261 MET A N 1 ATOM 1874 C CA . MET A 1 260 ? 47.217 4.002 47.385 1.00 21.05 ? 261 MET A CA 1 ATOM 1875 C C . MET A 1 260 ? 47.104 2.941 48.470 1.00 22.18 ? 261 MET A C 1 ATOM 1876 O O . MET A 1 260 ? 47.786 3.012 49.495 1.00 24.97 ? 261 MET A O 1 ATOM 1877 C CB . MET A 1 260 ? 46.709 5.337 47.964 1.00 20.57 ? 261 MET A CB 1 ATOM 1878 C CG . MET A 1 260 ? 47.035 6.562 47.132 1.00 22.39 ? 261 MET A CG 1 ATOM 1879 S SD . MET A 1 260 ? 48.832 6.872 47.097 1.00 21.80 ? 261 MET A SD 1 ATOM 1880 C CE . MET A 1 260 ? 48.976 8.604 47.686 1.00 18.89 ? 261 MET A CE 1 ATOM 1881 N N . THR A 1 261 ? 46.255 1.949 48.248 1.00 18.58 ? 262 THR A N 1 ATOM 1882 C CA . THR A 1 261 ? 46.030 0.910 49.250 1.00 18.24 ? 262 THR A CA 1 ATOM 1883 C C . THR A 1 261 ? 47.133 -0.122 49.470 1.00 18.03 ? 262 THR A C 1 ATOM 1884 O O . THR A 1 261 ? 47.374 -0.549 50.595 1.00 16.60 ? 262 THR A O 1 ATOM 1885 C CB . THR A 1 261 ? 44.745 0.120 48.901 1.00 18.18 ? 262 THR A CB 1 ATOM 1886 O OG1 . THR A 1 261 ? 44.836 -0.330 47.538 1.00 17.70 ? 262 THR A OG1 1 ATOM 1887 C CG2 . THR A 1 261 ? 43.501 0.996 49.046 1.00 18.00 ? 262 THR A CG2 1 ATOM 1888 N N . SER A 1 262 ? 47.802 -0.505 48.392 1.00 20.40 ? 263 SER A N 1 ATOM 1889 C CA . SER A 1 262 ? 48.797 -1.581 48.429 1.00 24.10 ? 263 SER A CA 1 ATOM 1890 C C . SER A 1 262 ? 50.289 -1.364 48.763 1.00 25.11 ? 263 SER A C 1 ATOM 1891 O O . SER A 1 262 ? 50.973 -2.296 49.216 1.00 27.17 ? 263 SER A O 1 ATOM 1892 C CB . SER A 1 262 ? 48.711 -2.321 47.098 1.00 23.26 ? 263 SER A CB 1 ATOM 1893 O OG . SER A 1 262 ? 48.775 -1.379 46.038 1.00 31.05 ? 263 SER A OG 1 ATOM 1894 N N . SER A 1 263 ? 50.797 -0.158 48.574 1.00 23.47 ? 264 SER A N 1 ATOM 1895 C CA . SER A 1 263 ? 52.209 0.084 48.794 1.00 21.81 ? 264 SER A CA 1 ATOM 1896 C C . SER A 1 263 ? 52.480 1.340 49.587 1.00 21.57 ? 264 SER A C 1 ATOM 1897 O O . SER A 1 263 ? 52.211 2.458 49.137 1.00 19.65 ? 264 SER A O 1 ATOM 1898 C CB . SER A 1 263 ? 52.883 0.163 47.425 1.00 19.86 ? 264 SER A CB 1 ATOM 1899 O OG . SER A 1 263 ? 54.108 0.835 47.492 1.00 21.31 ? 264 SER A OG 1 ATOM 1900 N N . ASN A 1 264 ? 52.975 1.155 50.796 1.00 22.60 ? 265 ASN A N 1 ATOM 1901 C CA . ASN A 1 264 ? 53.330 2.294 51.625 1.00 25.18 ? 265 ASN A CA 1 ATOM 1902 C C . ASN A 1 264 ? 54.385 3.147 50.904 1.00 26.17 ? 265 ASN A C 1 ATOM 1903 O O . ASN A 1 264 ? 54.335 4.386 50.939 1.00 24.70 ? 265 ASN A O 1 ATOM 1904 C CB . ASN A 1 264 ? 53.890 1.805 52.952 1.00 24.92 ? 265 ASN A CB 1 ATOM 1905 C CG . ASN A 1 264 ? 52.825 1.273 53.851 1.00 25.46 ? 265 ASN A CG 1 ATOM 1906 O OD1 . ASN A 1 264 ? 51.792 1.909 54.024 1.00 22.43 ? 265 ASN A OD1 1 ATOM 1907 N ND2 . ASN A 1 264 ? 53.056 0.103 54.434 1.00 26.00 ? 265 ASN A ND2 1 ATOM 1908 N N . GLU A 1 265 ? 55.318 2.473 50.230 1.00 25.14 ? 266 GLU A N 1 ATOM 1909 C CA . GLU A 1 265 ? 56.395 3.142 49.514 1.00 28.22 ? 266 GLU A CA 1 ATOM 1910 C C . GLU A 1 265 ? 55.864 4.122 48.476 1.00 25.52 ? 266 GLU A C 1 ATOM 1911 O O . GLU A 1 265 ? 56.267 5.280 48.432 1.00 23.48 ? 266 GLU A O 1 ATOM 1912 C CB . GLU A 1 265 ? 57.289 2.105 48.836 1.00 33.83 ? 266 GLU A CB 1 ATOM 1913 C CG . GLU A 1 265 ? 58.400 2.719 48.019 1.00 43.94 ? 266 GLU A CG 1 ATOM 1914 C CD . GLU A 1 265 ? 58.884 1.797 46.914 1.00 51.06 ? 266 GLU A CD 1 ATOM 1915 O OE1 . GLU A 1 265 ? 59.885 1.067 47.149 1.00 56.19 ? 266 GLU A OE1 1 ATOM 1916 O OE2 . GLU A 1 265 ? 58.270 1.811 45.811 1.00 54.07 ? 266 GLU A OE2 1 ATOM 1917 N N . VAL A 1 266 ? 54.959 3.647 47.635 1.00 24.42 ? 267 VAL A N 1 ATOM 1918 C CA . VAL A 1 266 ? 54.369 4.473 46.596 1.00 24.24 ? 267 VAL A CA 1 ATOM 1919 C C . VAL A 1 266 ? 53.540 5.636 47.185 1.00 22.60 ? 267 VAL A C 1 ATOM 1920 O O . VAL A 1 266 ? 53.517 6.738 46.634 1.00 20.54 ? 267 VAL A O 1 ATOM 1921 C CB . VAL A 1 266 ? 53.507 3.606 45.674 1.00 26.27 ? 267 VAL A CB 1 ATOM 1922 C CG1 . VAL A 1 266 ? 52.437 4.441 44.978 1.00 29.15 ? 267 VAL A CG1 1 ATOM 1923 C CG2 . VAL A 1 266 ? 54.404 2.898 44.663 1.00 27.67 ? 267 VAL A CG2 1 ATOM 1924 N N . MET A 1 267 ? 52.881 5.383 48.309 1.00 20.96 ? 268 MET A N 1 ATOM 1925 C CA . MET A 1 267 ? 52.078 6.407 48.948 1.00 20.00 ? 268 MET A CA 1 ATOM 1926 C C . MET A 1 267 ? 53.017 7.554 49.351 1.00 20.80 ? 268 MET A C 1 ATOM 1927 O O . MET A 1 267 ? 52.800 8.731 48.966 1.00 20.27 ? 268 MET A O 1 ATOM 1928 C CB . MET A 1 267 ? 51.379 5.845 50.191 1.00 17.64 ? 268 MET A CB 1 ATOM 1929 C CG . MET A 1 267 ? 50.426 6.847 50.848 1.00 14.58 ? 268 MET A CG 1 ATOM 1930 S SD . MET A 1 267 ? 49.823 6.279 52.394 1.00 17.99 ? 268 MET A SD 1 ATOM 1931 C CE . MET A 1 267 ? 51.304 6.114 53.295 1.00 16.27 ? 268 MET A CE 1 ATOM 1932 N N . GLY A 1 268 ? 54.063 7.188 50.103 1.00 19.61 ? 269 GLY A N 1 ATOM 1933 C CA . GLY A 1 268 ? 55.060 8.138 50.581 1.00 17.03 ? 269 GLY A CA 1 ATOM 1934 C C . GLY A 1 268 ? 55.698 8.979 49.487 1.00 17.99 ? 269 GLY A C 1 ATOM 1935 O O . GLY A 1 268 ? 55.876 10.186 49.664 1.00 17.33 ? 269 GLY A O 1 ATOM 1936 N N . GLN A 1 269 ? 56.069 8.357 48.366 1.00 19.07 ? 270 GLN A N 1 ATOM 1937 C CA . GLN A 1 269 ? 56.675 9.083 47.261 1.00 21.19 ? 270 GLN A CA 1 ATOM 1938 C C . GLN A 1 269 ? 55.756 10.193 46.771 1.00 20.84 ? 270 GLN A C 1 ATOM 1939 O O . GLN A 1 269 ? 56.218 11.291 46.481 1.00 19.36 ? 270 GLN A O 1 ATOM 1940 C CB . GLN A 1 269 ? 56.896 8.196 46.035 1.00 25.71 ? 270 GLN A CB 1 ATOM 1941 C CG . GLN A 1 269 ? 57.788 6.991 46.153 1.00 34.13 ? 270 GLN A CG 1 ATOM 1942 C CD . GLN A 1 269 ? 57.613 6.047 44.946 1.00 37.22 ? 270 GLN A CD 1 ATOM 1943 O OE1 . GLN A 1 269 ? 58.238 4.991 44.881 1.00 41.49 ? 270 GLN A OE1 1 ATOM 1944 N NE2 . GLN A 1 269 ? 56.737 6.419 44.004 1.00 39.28 ? 270 GLN A NE2 1 ATOM 1945 N N . ARG A 1 270 ? 54.491 9.844 46.529 1.00 19.46 ? 271 ARG A N 1 ATOM 1946 C CA . ARG A 1 270 ? 53.478 10.785 46.005 1.00 17.37 ? 271 ARG A CA 1 ATOM 1947 C C . ARG A 1 270 ? 53.166 11.906 46.980 1.00 15.86 ? 271 ARG A C 1 ATOM 1948 O O . ARG A 1 270 ? 52.968 13.063 46.586 1.00 19.62 ? 271 ARG A O 1 ATOM 1949 C CB . ARG A 1 270 ? 52.185 10.038 45.681 1.00 15.64 ? 271 ARG A CB 1 ATOM 1950 C CG . ARG A 1 270 ? 52.321 9.028 44.572 1.00 15.63 ? 271 ARG A CG 1 ATOM 1951 C CD . ARG A 1 270 ? 51.181 8.055 44.616 1.00 18.51 ? 271 ARG A CD 1 ATOM 1952 N NE . ARG A 1 270 ? 51.096 7.310 43.374 1.00 21.02 ? 271 ARG A NE 1 ATOM 1953 C CZ . ARG A 1 270 ? 50.128 6.438 43.083 1.00 21.13 ? 271 ARG A CZ 1 ATOM 1954 N NH1 . ARG A 1 270 ? 49.148 6.184 43.950 1.00 19.17 ? 271 ARG A NH1 1 ATOM 1955 N NH2 . ARG A 1 270 ? 50.144 5.821 41.906 1.00 19.98 ? 271 ARG A NH2 1 ATOM 1956 N N . TYR A 1 271 ? 53.073 11.547 48.243 1.00 14.05 ? 272 TYR A N 1 ATOM 1957 C CA . TYR A 1 271 ? 52.771 12.519 49.262 1.00 15.44 ? 272 TYR A CA 1 ATOM 1958 C C . TYR A 1 271 ? 53.900 13.535 49.385 1.00 16.23 ? 272 TYR A C 1 ATOM 1959 O O . TYR A 1 271 ? 53.651 14.715 49.489 1.00 13.91 ? 272 TYR A O 1 ATOM 1960 C CB . TYR A 1 271 ? 52.545 11.805 50.586 1.00 13.53 ? 272 TYR A CB 1 ATOM 1961 C CG . TYR A 1 271 ? 52.363 12.747 51.761 1.00 12.27 ? 272 TYR A CG 1 ATOM 1962 C CD1 . TYR A 1 271 ? 53.357 12.848 52.735 1.00 12.39 ? 272 TYR A CD1 1 ATOM 1963 C CD2 . TYR A 1 271 ? 51.195 13.481 51.926 1.00 11.67 ? 272 TYR A CD2 1 ATOM 1964 C CE1 . TYR A 1 271 ? 53.208 13.621 53.827 1.00 12.23 ? 272 TYR A CE1 1 ATOM 1965 C CE2 . TYR A 1 271 ? 51.028 14.272 53.040 1.00 12.16 ? 272 TYR A CE2 1 ATOM 1966 C CZ . TYR A 1 271 ? 52.043 14.328 53.985 1.00 12.11 ? 272 TYR A CZ 1 ATOM 1967 O OH . TYR A 1 271 ? 51.909 15.054 55.133 1.00 11.23 ? 272 TYR A OH 1 ATOM 1968 N N . ARG A 1 272 ? 55.142 13.053 49.400 1.00 17.08 ? 273 ARG A N 1 ATOM 1969 C CA . ARG A 1 272 ? 56.311 13.928 49.505 1.00 18.09 ? 273 ARG A CA 1 ATOM 1970 C C . ARG A 1 272 ? 56.314 14.915 48.355 1.00 16.34 ? 273 ARG A C 1 ATOM 1971 O O . ARG A 1 272 ? 56.626 16.094 48.527 1.00 18.11 ? 273 ARG A O 1 ATOM 1972 C CB . ARG A 1 272 ? 57.613 13.114 49.450 1.00 21.69 ? 273 ARG A CB 1 ATOM 1973 C CG . ARG A 1 272 ? 58.875 13.965 49.683 1.00 21.69 ? 273 ARG A CG 1 ATOM 1974 C CD . ARG A 1 272 ? 60.146 13.239 49.293 1.00 26.03 ? 273 ARG A CD 1 ATOM 1975 N NE . ARG A 1 272 ? 61.354 13.926 49.758 1.00 27.54 ? 273 ARG A NE 1 ATOM 1976 C CZ . ARG A 1 272 ? 62.011 14.863 49.074 1.00 30.76 ? 273 ARG A CZ 1 ATOM 1977 N NH1 . ARG A 1 272 ? 61.587 15.243 47.871 1.00 30.01 ? 273 ARG A NH1 1 ATOM 1978 N NH2 . ARG A 1 272 ? 63.105 15.419 49.599 1.00 30.42 ? 273 ARG A NH2 1 ATOM 1979 N N . ALA A 1 273 ? 56.030 14.414 47.166 1.00 15.59 ? 274 ALA A N 1 ATOM 1980 C CA . ALA A 1 273 ? 55.988 15.260 45.992 1.00 16.44 ? 274 ALA A CA 1 ATOM 1981 C C . ALA A 1 273 ? 54.901 16.348 46.063 1.00 17.97 ? 274 ALA A C 1 ATOM 1982 O O . ALA A 1 273 ? 55.145 17.504 45.696 1.00 18.44 ? 274 ALA A O 1 ATOM 1983 C CB . ALA A 1 273 ? 55.806 14.409 44.756 1.00 16.65 ? 274 ALA A CB 1 ATOM 1984 N N . ALA A 1 274 ? 53.695 15.976 46.495 1.00 17.71 ? 275 ALA A N 1 ATOM 1985 C CA . ALA A 1 274 ? 52.591 16.942 46.585 1.00 16.88 ? 275 ALA A CA 1 ATOM 1986 C C . ALA A 1 274 ? 52.881 17.961 47.695 1.00 16.45 ? 275 ALA A C 1 ATOM 1987 O O . ALA A 1 274 ? 52.582 19.150 47.553 1.00 17.90 ? 275 ALA A O 1 ATOM 1988 C CB . ALA A 1 274 ? 51.243 16.221 46.821 1.00 15.39 ? 275 ALA A CB 1 ATOM 1989 N N . MET A 1 275 ? 53.451 17.506 48.803 1.00 15.43 ? 276 MET A N 1 ATOM 1990 C CA . MET A 1 275 ? 53.814 18.432 49.872 1.00 16.00 ? 276 MET A CA 1 ATOM 1991 C C . MET A 1 275 ? 54.892 19.458 49.392 1.00 17.22 ? 276 MET A C 1 ATOM 1992 O O . MET A 1 275 ? 54.813 20.653 49.742 1.00 13.93 ? 276 MET A O 1 ATOM 1993 C CB . MET A 1 275 ? 54.322 17.680 51.105 1.00 14.74 ? 276 MET A CB 1 ATOM 1994 C CG . MET A 1 275 ? 53.255 16.918 51.852 1.00 15.56 ? 276 MET A CG 1 ATOM 1995 S SD . MET A 1 275 ? 51.986 17.990 52.595 1.00 16.88 ? 276 MET A SD 1 ATOM 1996 C CE . MET A 1 275 ? 52.740 18.579 54.137 1.00 11.19 ? 276 MET A CE 1 ATOM 1997 N N . ALA A 1 276 ? 55.914 18.988 48.650 1.00 16.03 ? 277 ALA A N 1 ATOM 1998 C CA . ALA A 1 276 ? 56.981 19.884 48.146 1.00 16.42 ? 277 ALA A CA 1 ATOM 1999 C C . ALA A 1 276 ? 56.351 21.023 47.359 1.00 16.45 ? 277 ALA A C 1 ATOM 2000 O O . ALA A 1 276 ? 56.771 22.182 47.456 1.00 18.62 ? 277 ALA A O 1 ATOM 2001 C CB . ALA A 1 276 ? 57.968 19.119 47.263 1.00 13.06 ? 277 ALA A CB 1 ATOM 2002 N N . LYS A 1 277 ? 55.327 20.665 46.587 1.00 16.54 ? 278 LYS A N 1 ATOM 2003 C CA . LYS A 1 277 ? 54.571 21.580 45.756 1.00 16.27 ? 278 LYS A CA 1 ATOM 2004 C C . LYS A 1 277 ? 53.703 22.526 46.594 1.00 17.71 ? 278 LYS A C 1 ATOM 2005 O O . LYS A 1 277 ? 53.585 23.710 46.282 1.00 16.72 ? 278 LYS A O 1 ATOM 2006 C CB . LYS A 1 277 ? 53.725 20.764 44.785 1.00 18.42 ? 278 LYS A CB 1 ATOM 2007 C CG . LYS A 1 277 ? 52.840 21.563 43.889 1.00 21.74 ? 278 LYS A CG 1 ATOM 2008 C CD . LYS A 1 277 ? 52.313 20.711 42.768 1.00 22.31 ? 278 LYS A CD 1 ATOM 2009 C CE . LYS A 1 277 ? 51.423 21.545 41.895 1.00 24.79 ? 278 LYS A CE 1 ATOM 2010 N NZ . LYS A 1 277 ? 51.013 20.834 40.652 1.00 30.67 ? 278 LYS A NZ 1 ATOM 2011 N N . MET A 1 278 ? 53.134 22.017 47.683 1.00 17.15 ? 279 MET A N 1 ATOM 2012 C CA . MET A 1 278 ? 52.306 22.848 48.512 1.00 15.28 ? 279 MET A CA 1 ATOM 2013 C C . MET A 1 278 ? 53.151 23.762 49.362 1.00 15.79 ? 279 MET A C 1 ATOM 2014 O O . MET A 1 278 ? 52.710 24.849 49.732 1.00 15.44 ? 279 MET A O 1 ATOM 2015 C CB . MET A 1 278 ? 51.413 21.997 49.407 1.00 14.98 ? 279 MET A CB 1 ATOM 2016 C CG . MET A 1 278 ? 50.450 22.821 50.219 1.00 14.11 ? 279 MET A CG 1 ATOM 2017 S SD . MET A 1 278 ? 49.293 21.840 51.177 1.00 18.21 ? 279 MET A SD 1 ATOM 2018 C CE . MET A 1 278 ? 50.183 21.549 52.620 1.00 11.75 ? 279 MET A CE 1 ATOM 2019 N N . SER A 1 279 ? 54.391 23.361 49.631 1.00 16.54 ? 280 SER A N 1 ATOM 2020 C CA . SER A 1 279 ? 55.277 24.138 50.512 1.00 15.58 ? 280 SER A CA 1 ATOM 2021 C C . SER A 1 279 ? 55.732 25.462 49.919 1.00 15.19 ? 280 SER A C 1 ATOM 2022 O O . SER A 1 279 ? 56.227 26.320 50.636 1.00 15.88 ? 280 SER A O 1 ATOM 2023 C CB . SER A 1 279 ? 56.510 23.313 50.919 1.00 14.15 ? 280 SER A CB 1 ATOM 2024 O OG . SER A 1 279 ? 57.352 23.074 49.799 1.00 15.98 ? 280 SER A OG 1 ATOM 2025 N N . VAL A 1 280 ? 55.598 25.605 48.616 1.00 14.55 ? 281 VAL A N 1 ATOM 2026 C CA . VAL A 1 280 ? 56.032 26.814 47.962 1.00 16.77 ? 281 VAL A CA 1 ATOM 2027 C C . VAL A 1 280 ? 54.919 27.583 47.252 1.00 17.02 ? 281 VAL A C 1 ATOM 2028 O O . VAL A 1 280 ? 55.195 28.375 46.348 1.00 16.62 ? 281 VAL A O 1 ATOM 2029 C CB . VAL A 1 280 ? 57.216 26.530 46.974 1.00 18.00 ? 281 VAL A CB 1 ATOM 2030 C CG1 . VAL A 1 280 ? 58.456 26.046 47.742 1.00 16.86 ? 281 VAL A CG1 1 ATOM 2031 C CG2 . VAL A 1 280 ? 56.823 25.517 45.955 1.00 18.27 ? 281 VAL A CG2 1 ATOM 2032 N N . LEU A 1 281 ? 53.663 27.318 47.600 1.00 16.69 ? 282 LEU A N 1 ATOM 2033 C CA . LEU A 1 281 ? 52.564 28.090 46.996 1.00 16.39 ? 282 LEU A CA 1 ATOM 2034 C C . LEU A 1 281 ? 52.787 29.531 47.473 1.00 16.30 ? 282 LEU A C 1 ATOM 2035 O O . LEU A 1 281 ? 52.954 29.770 48.670 1.00 14.00 ? 282 LEU A O 1 ATOM 2036 C CB . LEU A 1 281 ? 51.200 27.603 47.502 1.00 16.31 ? 282 LEU A CB 1 ATOM 2037 C CG . LEU A 1 281 ? 50.655 26.270 46.994 1.00 12.95 ? 282 LEU A CG 1 ATOM 2038 C CD1 . LEU A 1 281 ? 49.301 26.023 47.637 1.00 14.21 ? 282 LEU A CD1 1 ATOM 2039 C CD2 . LEU A 1 281 ? 50.533 26.263 45.495 1.00 14.25 ? 282 LEU A CD2 1 ATOM 2040 N N . GLY A 1 282 ? 52.857 30.469 46.537 1.00 17.39 ? 283 GLY A N 1 ATOM 2041 C CA . GLY A 1 282 ? 53.094 31.854 46.896 1.00 17.49 ? 283 GLY A CA 1 ATOM 2042 C C . GLY A 1 282 ? 54.562 32.280 46.770 1.00 19.35 ? 283 GLY A C 1 ATOM 2043 O O . GLY A 1 282 ? 54.878 33.464 46.947 1.00 18.30 ? 283 GLY A O 1 ATOM 2044 N N . PHE A 1 283 ? 55.461 31.324 46.508 1.00 20.43 ? 284 PHE A N 1 ATOM 2045 C CA . PHE A 1 283 ? 56.892 31.613 46.374 1.00 21.16 ? 284 PHE A CA 1 ATOM 2046 C C . PHE A 1 283 ? 57.506 30.951 45.145 1.00 23.94 ? 284 PHE A C 1 ATOM 2047 O O . PHE A 1 283 ? 56.885 30.088 44.515 1.00 25.93 ? 284 PHE A O 1 ATOM 2048 C CB . PHE A 1 283 ? 57.650 31.150 47.624 1.00 17.11 ? 284 PHE A CB 1 ATOM 2049 C CG . PHE A 1 283 ? 57.095 31.693 48.886 1.00 18.20 ? 284 PHE A CG 1 ATOM 2050 C CD1 . PHE A 1 283 ? 57.633 32.825 49.466 1.00 16.06 ? 284 PHE A CD1 1 ATOM 2051 C CD2 . PHE A 1 283 ? 55.996 31.095 49.488 1.00 18.10 ? 284 PHE A CD2 1 ATOM 2052 C CE1 . PHE A 1 283 ? 57.091 33.371 50.636 1.00 18.10 ? 284 PHE A CE1 1 ATOM 2053 C CE2 . PHE A 1 283 ? 55.440 31.634 50.661 1.00 19.34 ? 284 PHE A CE2 1 ATOM 2054 C CZ . PHE A 1 283 ? 55.989 32.774 51.237 1.00 16.47 ? 284 PHE A CZ 1 ATOM 2055 N N . ASP A 1 284 ? 58.725 31.368 44.804 1.00 27.18 ? 285 ASP A N 1 ATOM 2056 C CA . ASP A 1 284 ? 59.473 30.802 43.678 1.00 29.41 ? 285 ASP A CA 1 ATOM 2057 C C . ASP A 1 284 ? 60.486 29.907 44.354 1.00 29.86 ? 285 ASP A C 1 ATOM 2058 O O . ASP A 1 284 ? 61.330 30.398 45.106 1.00 27.91 ? 285 ASP A O 1 ATOM 2059 C CB . ASP A 1 284 ? 60.224 31.897 42.926 1.00 34.70 ? 285 ASP A CB 1 ATOM 2060 C CG . ASP A 1 284 ? 60.993 31.367 41.712 1.00 38.62 ? 285 ASP A CG 1 ATOM 2061 O OD1 . ASP A 1 284 ? 61.159 30.132 41.586 1.00 38.73 ? 285 ASP A OD1 1 ATOM 2062 O OD2 . ASP A 1 284 ? 61.431 32.205 40.879 1.00 41.82 ? 285 ASP A OD2 1 ATOM 2063 N N . ARG A 1 285 ? 60.441 28.611 44.067 1.00 31.00 ? 286 ARG A N 1 ATOM 2064 C CA . ARG A 1 285 ? 61.361 27.700 44.730 1.00 33.85 ? 286 ARG A CA 1 ATOM 2065 C C . ARG A 1 285 ? 62.831 27.947 44.432 1.00 34.78 ? 286 ARG A C 1 ATOM 2066 O O . ARG A 1 285 ? 63.675 27.780 45.318 1.00 34.65 ? 286 ARG A O 1 ATOM 2067 C CB . ARG A 1 285 ? 60.983 26.233 44.510 1.00 33.70 ? 286 ARG A CB 1 ATOM 2068 C CG . ARG A 1 285 ? 60.930 25.793 43.084 1.00 33.65 ? 286 ARG A CG 1 ATOM 2069 C CD . ARG A 1 285 ? 60.721 24.287 43.032 1.00 35.84 ? 286 ARG A CD 1 ATOM 2070 N NE . ARG A 1 285 ? 61.800 23.584 43.723 1.00 36.38 ? 286 ARG A NE 1 ATOM 2071 C CZ . ARG A 1 285 ? 61.639 22.790 44.783 1.00 36.74 ? 286 ARG A CZ 1 ATOM 2072 N NH1 . ARG A 1 285 ? 60.430 22.567 45.303 1.00 36.55 ? 286 ARG A NH1 1 ATOM 2073 N NH2 . ARG A 1 285 ? 62.709 22.250 45.354 1.00 37.54 ? 286 ARG A NH2 1 ATOM 2074 N N . ASN A 1 286 ? 63.147 28.411 43.226 1.00 35.45 ? 287 ASN A N 1 ATOM 2075 C CA . ASN A 1 286 ? 64.544 28.675 42.928 1.00 36.62 ? 287 ASN A CA 1 ATOM 2076 C C . ASN A 1 286 ? 65.019 29.949 43.588 1.00 35.58 ? 287 ASN A C 1 ATOM 2077 O O . ASN A 1 286 ? 66.069 30.455 43.267 1.00 38.54 ? 287 ASN A O 1 ATOM 2078 C CB . ASN A 1 286 ? 64.844 28.683 41.425 1.00 40.89 ? 287 ASN A CB 1 ATOM 2079 C CG . ASN A 1 286 ? 63.929 29.588 40.648 1.00 44.13 ? 287 ASN A CG 1 ATOM 2080 O OD1 . ASN A 1 286 ? 62.972 29.123 40.020 1.00 47.75 ? 287 ASN A OD1 1 ATOM 2081 N ND2 . ASN A 1 286 ? 64.208 30.886 40.675 1.00 47.42 ? 287 ASN A ND2 1 ATOM 2082 N N . ALA A 1 287 ? 64.236 30.478 44.510 1.00 33.51 ? 288 ALA A N 1 ATOM 2083 C CA . ALA A 1 287 ? 64.628 31.668 45.226 1.00 30.51 ? 288 ALA A CA 1 ATOM 2084 C C . ALA A 1 287 ? 64.911 31.270 46.671 1.00 29.61 ? 288 ALA A C 1 ATOM 2085 O O . ALA A 1 287 ? 65.416 32.076 47.466 1.00 29.74 ? 288 ALA A O 1 ATOM 2086 C CB . ALA A 1 287 ? 63.508 32.679 45.182 1.00 31.88 ? 288 ALA A CB 1 ATOM 2087 N N . LEU A 1 288 ? 64.588 30.026 47.011 1.00 25.32 ? 289 LEU A N 1 ATOM 2088 C CA . LEU A 1 288 ? 64.764 29.540 48.384 1.00 23.91 ? 289 LEU A CA 1 ATOM 2089 C C . LEU A 1 288 ? 66.029 28.689 48.528 1.00 21.65 ? 289 LEU A C 1 ATOM 2090 O O . LEU A 1 288 ? 66.615 28.283 47.537 1.00 22.92 ? 289 LEU A O 1 ATOM 2091 C CB . LEU A 1 288 ? 63.498 28.755 48.830 1.00 21.26 ? 289 LEU A CB 1 ATOM 2092 C CG . LEU A 1 288 ? 62.146 29.509 48.736 1.00 19.32 ? 289 LEU A CG 1 ATOM 2093 C CD1 . LEU A 1 288 ? 60.977 28.574 48.918 1.00 16.19 ? 289 LEU A CD1 1 ATOM 2094 C CD2 . LEU A 1 288 ? 62.100 30.603 49.775 1.00 16.57 ? 289 LEU A CD2 1 ATOM 2095 N N . THR A 1 289 ? 66.465 28.446 49.757 1.00 21.24 ? 290 THR A N 1 ATOM 2096 C CA . THR A 1 289 ? 67.652 27.635 49.986 1.00 21.10 ? 290 THR A CA 1 ATOM 2097 C C . THR A 1 289 ? 67.241 26.269 50.509 1.00 21.51 ? 290 THR A C 1 ATOM 2098 O O . THR A 1 289 ? 66.400 26.154 51.392 1.00 19.77 ? 290 THR A O 1 ATOM 2099 C CB . THR A 1 289 ? 68.628 28.331 50.953 1.00 21.27 ? 290 THR A CB 1 ATOM 2100 O OG1 . THR A 1 289 ? 69.139 29.484 50.295 1.00 20.40 ? 290 THR A OG1 1 ATOM 2101 C CG2 . THR A 1 289 ? 69.807 27.418 51.355 1.00 20.76 ? 290 THR A CG2 1 ATOM 2102 N N . ASP A 1 290 ? 67.869 25.242 49.958 1.00 20.85 ? 291 ASP A N 1 ATOM 2103 C CA . ASP A 1 290 ? 67.589 23.872 50.333 1.00 20.95 ? 291 ASP A CA 1 ATOM 2104 C C . ASP A 1 290 ? 68.367 23.432 51.570 1.00 20.98 ? 291 ASP A C 1 ATOM 2105 O O . ASP A 1 290 ? 69.601 23.383 51.558 1.00 23.07 ? 291 ASP A O 1 ATOM 2106 C CB . ASP A 1 290 ? 67.903 22.954 49.151 1.00 21.64 ? 291 ASP A CB 1 ATOM 2107 C CG . ASP A 1 290 ? 67.305 21.571 49.312 1.00 22.01 ? 291 ASP A CG 1 ATOM 2108 O OD1 . ASP A 1 290 ? 66.925 21.190 50.431 1.00 22.39 ? 291 ASP A OD1 1 ATOM 2109 O OD2 . ASP A 1 290 ? 67.204 20.862 48.304 1.00 26.33 ? 291 ASP A OD2 1 ATOM 2110 N N . CYS A 1 291 ? 67.641 23.124 52.635 1.00 18.05 ? 292 CYS A N 1 ATOM 2111 C CA . CYS A 1 291 ? 68.234 22.659 53.861 1.00 16.45 ? 292 CYS A CA 1 ATOM 2112 C C . CYS A 1 291 ? 67.640 21.302 54.229 1.00 15.58 ? 292 CYS A C 1 ATOM 2113 O O . CYS A 1 291 ? 67.544 20.963 55.402 1.00 15.04 ? 292 CYS A O 1 ATOM 2114 C CB . CYS A 1 291 ? 67.985 23.667 54.978 1.00 17.37 ? 292 CYS A CB 1 ATOM 2115 S SG . CYS A 1 291 ? 68.903 25.214 54.738 1.00 20.55 ? 292 CYS A SG 1 ATOM 2116 N N . SER A 1 292 ? 67.276 20.515 53.222 1.00 16.82 ? 293 SER A N 1 ATOM 2117 C CA . SER A 1 292 ? 66.679 19.185 53.444 1.00 18.31 ? 293 SER A CA 1 ATOM 2118 C C . SER A 1 292 ? 67.570 18.293 54.285 1.00 19.06 ? 293 SER A C 1 ATOM 2119 O O . SER A 1 292 ? 67.078 17.442 55.032 1.00 17.84 ? 293 SER A O 1 ATOM 2120 C CB . SER A 1 292 ? 66.414 18.485 52.119 1.00 18.03 ? 293 SER A CB 1 ATOM 2121 O OG . SER A 1 292 ? 65.431 19.167 51.374 1.00 18.11 ? 293 SER A OG 1 ATOM 2122 N N . ASP A 1 293 ? 68.878 18.538 54.213 1.00 20.21 ? 294 ASP A N 1 ATOM 2123 C CA . ASP A 1 293 ? 69.858 17.752 54.959 1.00 21.31 ? 294 ASP A CA 1 ATOM 2124 C C . ASP A 1 293 ? 69.665 17.833 56.466 1.00 20.41 ? 294 ASP A C 1 ATOM 2125 O O . ASP A 1 293 ? 70.203 17.015 57.216 1.00 20.48 ? 294 ASP A O 1 ATOM 2126 C CB . ASP A 1 293 ? 71.281 18.190 54.590 1.00 26.60 ? 294 ASP A CB 1 ATOM 2127 C CG . ASP A 1 293 ? 71.514 19.688 54.823 1.00 31.05 ? 294 ASP A CG 1 ATOM 2128 O OD1 . ASP A 1 293 ? 71.054 20.513 53.991 1.00 34.21 ? 294 ASP A OD1 1 ATOM 2129 O OD2 . ASP A 1 293 ? 72.139 20.027 55.847 1.00 33.05 ? 294 ASP A OD2 1 ATOM 2130 N N . VAL A 1 294 ? 68.923 18.831 56.930 1.00 17.31 ? 295 VAL A N 1 ATOM 2131 C CA . VAL A 1 294 ? 68.706 18.946 58.367 1.00 17.15 ? 295 VAL A CA 1 ATOM 2132 C C . VAL A 1 294 ? 67.613 17.966 58.842 1.00 16.50 ? 295 VAL A C 1 ATOM 2133 O O . VAL A 1 294 ? 67.617 17.528 59.976 1.00 16.30 ? 295 VAL A O 1 ATOM 2134 C CB . VAL A 1 294 ? 68.290 20.414 58.757 1.00 16.54 ? 295 VAL A CB 1 ATOM 2135 C CG1 . VAL A 1 294 ? 68.123 20.559 60.272 1.00 15.79 ? 295 VAL A CG1 1 ATOM 2136 C CG2 . VAL A 1 294 ? 69.314 21.409 58.227 1.00 17.68 ? 295 VAL A CG2 1 ATOM 2137 N N . ILE A 1 295 ? 66.711 17.587 57.951 1.00 18.10 ? 296 ILE A N 1 ATOM 2138 C CA . ILE A 1 295 ? 65.584 16.736 58.335 1.00 18.96 ? 296 ILE A CA 1 ATOM 2139 C C . ILE A 1 295 ? 65.922 15.287 58.717 1.00 19.14 ? 296 ILE A C 1 ATOM 2140 O O . ILE A 1 295 ? 66.516 14.573 57.943 1.00 20.01 ? 296 ILE A O 1 ATOM 2141 C CB . ILE A 1 295 ? 64.521 16.732 57.206 1.00 18.69 ? 296 ILE A CB 1 ATOM 2142 C CG1 . ILE A 1 295 ? 64.137 18.173 56.837 1.00 17.97 ? 296 ILE A CG1 1 ATOM 2143 C CG2 . ILE A 1 295 ? 63.326 15.879 57.592 1.00 19.34 ? 296 ILE A CG2 1 ATOM 2144 C CD1 . ILE A 1 295 ? 63.800 19.052 58.026 1.00 16.21 ? 296 ILE A CD1 1 ATOM 2145 N N . PRO A 1 296 ? 65.587 14.870 59.946 1.00 19.65 ? 297 PRO A N 1 ATOM 2146 C CA . PRO A 1 296 ? 65.868 13.493 60.368 1.00 21.12 ? 297 PRO A CA 1 ATOM 2147 C C . PRO A 1 296 ? 65.033 12.466 59.620 1.00 21.47 ? 297 PRO A C 1 ATOM 2148 O O . PRO A 1 296 ? 64.054 12.823 58.960 1.00 20.66 ? 297 PRO A O 1 ATOM 2149 C CB . PRO A 1 296 ? 65.559 13.510 61.870 1.00 18.90 ? 297 PRO A CB 1 ATOM 2150 C CG . PRO A 1 296 ? 64.836 14.785 62.107 1.00 19.47 ? 297 PRO A CG 1 ATOM 2151 C CD . PRO A 1 296 ? 65.351 15.736 61.107 1.00 18.66 ? 297 PRO A CD 1 ATOM 2152 N N . SER A 1 297 ? 65.453 11.203 59.682 1.00 22.63 ? 298 SER A N 1 ATOM 2153 C CA . SER A 1 297 ? 64.749 10.119 58.997 1.00 24.32 ? 298 SER A CA 1 ATOM 2154 C C . SER A 1 297 ? 63.816 9.436 59.962 1.00 22.06 ? 298 SER A C 1 ATOM 2155 O O . SER A 1 297 ? 64.100 9.394 61.145 1.00 22.78 ? 298 SER A O 1 ATOM 2156 C CB . SER A 1 297 ? 65.745 9.094 58.460 1.00 27.43 ? 298 SER A CB 1 ATOM 2157 O OG . SER A 1 297 ? 66.630 9.681 57.515 1.00 33.84 ? 298 SER A OG 1 ATOM 2158 N N . ALA A 1 298 ? 62.688 8.929 59.484 1.00 22.19 ? 299 ALA A N 1 ATOM 2159 C CA . ALA A 1 298 ? 61.770 8.240 60.389 1.00 22.97 ? 299 ALA A CA 1 ATOM 2160 C C . ALA A 1 298 ? 62.109 6.752 60.391 1.00 22.28 ? 299 ALA A C 1 ATOM 2161 O O . ALA A 1 298 ? 62.677 6.231 59.420 1.00 23.58 ? 299 ALA A O 1 ATOM 2162 C CB . ALA A 1 298 ? 60.317 8.439 59.947 1.00 21.18 ? 299 ALA A CB 1 ATOM 2163 N N . VAL A 1 299 ? 61.734 6.063 61.461 1.00 22.58 ? 300 VAL A N 1 ATOM 2164 C CA . VAL A 1 299 ? 61.968 4.630 61.554 1.00 23.03 ? 300 VAL A CA 1 ATOM 2165 C C . VAL A 1 299 ? 61.065 4.003 60.497 1.00 23.79 ? 300 VAL A C 1 ATOM 2166 O O . VAL A 1 299 ? 60.057 4.599 60.108 1.00 22.16 ? 300 VAL A O 1 ATOM 2167 C CB . VAL A 1 299 ? 61.674 4.065 62.980 1.00 23.94 ? 300 VAL A CB 1 ATOM 2168 C CG1 . VAL A 1 299 ? 62.626 4.688 64.012 1.00 24.26 ? 300 VAL A CG1 1 ATOM 2169 C CG2 . VAL A 1 299 ? 60.269 4.323 63.385 1.00 25.92 ? 300 VAL A CG2 1 ATOM 2170 N N . SER A 1 300 ? 61.460 2.856 59.958 1.00 23.85 ? 301 SER A N 1 ATOM 2171 C CA . SER A 1 300 ? 60.657 2.227 58.927 1.00 23.77 ? 301 SER A CA 1 ATOM 2172 C C . SER A 1 300 ? 59.438 1.460 59.488 1.00 21.39 ? 301 SER A C 1 ATOM 2173 O O . SER A 1 300 ? 59.415 1.041 60.653 1.00 17.80 ? 301 SER A O 1 ATOM 2174 C CB . SER A 1 300 ? 61.525 1.304 58.084 1.00 24.69 ? 301 SER A CB 1 ATOM 2175 O OG . SER A 1 300 ? 61.799 0.130 58.814 1.00 29.39 ? 301 SER A OG 1 ATOM 2176 N N . ASN A 1 301 ? 58.388 1.385 58.683 1.00 20.14 ? 302 ASN A N 1 ATOM 2177 C CA . ASN A 1 301 ? 57.198 0.641 59.076 1.00 20.32 ? 302 ASN A CA 1 ATOM 2178 C C . ASN A 1 301 ? 57.338 -0.657 58.306 1.00 19.21 ? 302 ASN A C 1 ATOM 2179 O O . ASN A 1 301 ? 57.410 -0.639 57.080 1.00 17.64 ? 302 ASN A O 1 ATOM 2180 C CB . ASN A 1 301 ? 55.926 1.372 58.616 1.00 20.54 ? 302 ASN A CB 1 ATOM 2181 C CG . ASN A 1 301 ? 54.661 0.502 58.711 1.00 20.35 ? 302 ASN A CG 1 ATOM 2182 O OD1 . ASN A 1 301 ? 53.716 0.687 57.937 1.00 20.94 ? 302 ASN A OD1 1 ATOM 2183 N ND2 . ASN A 1 301 ? 54.619 -0.401 59.696 1.00 18.78 ? 302 ASN A ND2 1 ATOM 2184 N N . ASN A 1 302 ? 57.385 -1.782 59.005 1.00 21.08 ? 303 ASN A N 1 ATOM 2185 C CA . ASN A 1 302 ? 57.514 -3.073 58.315 1.00 23.45 ? 303 ASN A CA 1 ATOM 2186 C C . ASN A 1 302 ? 56.211 -3.851 58.163 1.00 23.03 ? 303 ASN A C 1 ATOM 2187 O O . ASN A 1 302 ? 56.172 -4.823 57.422 1.00 23.60 ? 303 ASN A O 1 ATOM 2188 C CB . ASN A 1 302 ? 58.562 -3.953 59.006 1.00 23.41 ? 303 ASN A CB 1 ATOM 2189 C CG . ASN A 1 302 ? 59.939 -3.321 58.992 1.00 26.26 ? 303 ASN A CG 1 ATOM 2190 O OD1 . ASN A 1 302 ? 60.407 -2.902 57.937 1.00 27.03 ? 303 ASN A OD1 1 ATOM 2191 N ND2 . ASN A 1 302 ? 60.562 -3.183 60.165 1.00 25.85 ? 303 ASN A ND2 1 ATOM 2192 N N . ALA A 1 303 ? 55.156 -3.426 58.855 1.00 22.91 ? 304 ALA A N 1 ATOM 2193 C CA . ALA A 1 303 ? 53.861 -4.103 58.766 1.00 20.32 ? 304 ALA A CA 1 ATOM 2194 C C . ALA A 1 303 ? 53.344 -4.028 57.344 1.00 20.86 ? 304 ALA A C 1 ATOM 2195 O O . ALA A 1 303 ? 53.688 -3.114 56.603 1.00 23.64 ? 304 ALA A O 1 ATOM 2196 C CB . ALA A 1 303 ? 52.892 -3.483 59.705 1.00 20.22 ? 304 ALA A CB 1 ATOM 2197 N N . ALA A 1 304 ? 52.586 -5.030 56.920 1.00 20.95 ? 305 ALA A N 1 ATOM 2198 C CA . ALA A 1 304 ? 52.036 -5.021 55.567 1.00 21.20 ? 305 ALA A CA 1 ATOM 2199 C C . ALA A 1 304 ? 50.639 -4.402 55.586 1.00 18.81 ? 305 ALA A C 1 ATOM 2200 O O . ALA A 1 304 ? 49.965 -4.413 56.615 1.00 20.34 ? 305 ALA A O 1 ATOM 2201 C CB . ALA A 1 304 ? 51.947 -6.457 55.006 1.00 19.91 ? 305 ALA A CB 1 ATOM 2202 N N . PRO A 1 305 ? 50.226 -3.771 54.475 1.00 19.97 ? 306 PRO A N 1 ATOM 2203 C CA . PRO A 1 305 ? 48.881 -3.180 54.429 1.00 19.19 ? 306 PRO A CA 1 ATOM 2204 C C . PRO A 1 305 ? 47.917 -4.354 54.607 1.00 20.76 ? 306 PRO A C 1 ATOM 2205 O O . PRO A 1 305 ? 48.098 -5.411 53.974 1.00 20.08 ? 306 PRO A O 1 ATOM 2206 C CB . PRO A 1 305 ? 48.799 -2.648 53.002 1.00 17.59 ? 306 PRO A CB 1 ATOM 2207 C CG . PRO A 1 305 ? 50.211 -2.211 52.724 1.00 19.70 ? 306 PRO A CG 1 ATOM 2208 C CD . PRO A 1 305 ? 51.006 -3.399 53.281 1.00 20.30 ? 306 PRO A CD 1 ATOM 2209 N N . VAL A 1 306 ? 46.946 -4.205 55.496 1.00 21.46 ? 307 VAL A N 1 ATOM 2210 C CA . VAL A 1 306 ? 45.982 -5.280 55.742 1.00 22.04 ? 307 VAL A CA 1 ATOM 2211 C C . VAL A 1 306 ? 44.530 -4.809 55.831 1.00 23.58 ? 307 VAL A C 1 ATOM 2212 O O . VAL A 1 306 ? 44.267 -3.644 56.167 1.00 22.28 ? 307 VAL A O 1 ATOM 2213 C CB . VAL A 1 306 ? 46.229 -6.001 57.102 1.00 21.60 ? 307 VAL A CB 1 ATOM 2214 C CG1 . VAL A 1 306 ? 47.556 -6.696 57.116 1.00 23.26 ? 307 VAL A CG1 1 ATOM 2215 C CG2 . VAL A 1 306 ? 46.111 -5.000 58.261 1.00 21.58 ? 307 VAL A CG2 1 ATOM 2216 N N . ILE A 1 307 ? 43.606 -5.720 55.499 1.00 23.06 ? 308 ILE A N 1 ATOM 2217 C CA . ILE A 1 307 ? 42.175 -5.491 55.653 1.00 23.15 ? 308 ILE A CA 1 ATOM 2218 C C . ILE A 1 307 ? 42.033 -6.128 57.031 1.00 22.37 ? 308 ILE A C 1 ATOM 2219 O O . ILE A 1 307 ? 42.181 -7.343 57.205 1.00 25.24 ? 308 ILE A O 1 ATOM 2220 C CB . ILE A 1 307 ? 41.323 -6.216 54.614 1.00 22.82 ? 308 ILE A CB 1 ATOM 2221 C CG1 . ILE A 1 307 ? 41.666 -5.715 53.221 1.00 21.78 ? 308 ILE A CG1 1 ATOM 2222 C CG2 . ILE A 1 307 ? 39.872 -5.978 54.920 1.00 25.25 ? 308 ILE A CG2 1 ATOM 2223 C CD1 . ILE A 1 307 ? 40.806 -6.294 52.138 1.00 24.19 ? 308 ILE A CD1 1 ATOM 2224 N N . PRO A 1 308 ? 41.793 -5.305 58.048 1.00 22.97 ? 309 PRO A N 1 ATOM 2225 C CA . PRO A 1 308 ? 41.665 -5.765 59.420 1.00 24.41 ? 309 PRO A CA 1 ATOM 2226 C C . PRO A 1 308 ? 40.413 -6.534 59.861 1.00 25.96 ? 309 PRO A C 1 ATOM 2227 O O . PRO A 1 308 ? 39.422 -6.624 59.144 1.00 26.04 ? 309 PRO A O 1 ATOM 2228 C CB . PRO A 1 308 ? 41.801 -4.458 60.192 1.00 23.13 ? 309 PRO A CB 1 ATOM 2229 C CG . PRO A 1 308 ? 41.012 -3.532 59.354 1.00 22.04 ? 309 PRO A CG 1 ATOM 2230 C CD . PRO A 1 308 ? 41.388 -3.889 57.934 1.00 20.83 ? 309 PRO A CD 1 ATOM 2231 N N . GLY A 1 309 ? 40.511 -7.042 61.086 1.00 26.76 ? 310 GLY A N 1 ATOM 2232 C CA . GLY A 1 309 ? 39.451 -7.751 61.773 1.00 29.05 ? 310 GLY A CA 1 ATOM 2233 C C . GLY A 1 309 ? 38.474 -8.679 61.092 1.00 29.53 ? 310 GLY A C 1 ATOM 2234 O O . GLY A 1 309 ? 37.324 -8.720 61.508 1.00 32.62 ? 310 GLY A O 1 ATOM 2235 N N . GLY A 1 310 ? 38.920 -9.460 60.114 1.00 30.00 ? 311 GLY A N 1 ATOM 2236 C CA . GLY A 1 310 ? 38.024 -10.383 59.440 1.00 29.15 ? 311 GLY A CA 1 ATOM 2237 C C . GLY A 1 310 ? 37.345 -9.879 58.175 1.00 30.52 ? 311 GLY A C 1 ATOM 2238 O O . GLY A 1 310 ? 36.669 -10.653 57.493 1.00 30.90 ? 311 GLY A O 1 ATOM 2239 N N . LEU A 1 311 ? 37.457 -8.595 57.852 1.00 28.11 ? 312 LEU A N 1 ATOM 2240 C CA . LEU A 1 311 ? 36.812 -8.118 56.626 1.00 28.39 ? 312 LEU A CA 1 ATOM 2241 C C . LEU A 1 311 ? 37.607 -8.607 55.397 1.00 28.20 ? 312 LEU A C 1 ATOM 2242 O O . LEU A 1 311 ? 38.792 -8.950 55.509 1.00 30.81 ? 312 LEU A O 1 ATOM 2243 C CB . LEU A 1 311 ? 36.642 -6.590 56.652 1.00 27.40 ? 312 LEU A CB 1 ATOM 2244 C CG . LEU A 1 311 ? 35.860 -6.078 57.873 1.00 27.15 ? 312 LEU A CG 1 ATOM 2245 C CD1 . LEU A 1 311 ? 35.839 -4.567 57.892 1.00 23.80 ? 312 LEU A CD1 1 ATOM 2246 C CD2 . LEU A 1 311 ? 34.448 -6.627 57.834 1.00 27.28 ? 312 LEU A CD2 1 ATOM 2247 N N . THR A 1 312 ? 36.973 -8.634 54.233 1.00 25.55 ? 313 THR A N 1 ATOM 2248 C CA . THR A 1 312 ? 37.627 -9.121 53.038 1.00 25.13 ? 313 THR A CA 1 ATOM 2249 C C . THR A 1 312 ? 37.416 -8.121 51.939 1.00 23.55 ? 313 THR A C 1 ATOM 2250 O O . THR A 1 312 ? 36.785 -7.091 52.155 1.00 23.75 ? 313 THR A O 1 ATOM 2251 C CB . THR A 1 312 ? 37.018 -10.483 52.585 1.00 28.65 ? 313 THR A CB 1 ATOM 2252 O OG1 . THR A 1 312 ? 35.611 -10.331 52.360 1.00 32.80 ? 313 THR A OG1 1 ATOM 2253 C CG2 . THR A 1 312 ? 37.217 -11.552 53.646 1.00 28.09 ? 313 THR A CG2 1 ATOM 2254 N N . VAL A 1 313 ? 37.916 -8.437 50.751 1.00 21.50 ? 314 VAL A N 1 ATOM 2255 C CA . VAL A 1 313 ? 37.742 -7.554 49.613 1.00 23.20 ? 314 VAL A CA 1 ATOM 2256 C C . VAL A 1 313 ? 36.243 -7.403 49.326 1.00 22.65 ? 314 VAL A C 1 ATOM 2257 O O . VAL A 1 313 ? 35.821 -6.496 48.604 1.00 23.29 ? 314 VAL A O 1 ATOM 2258 C CB . VAL A 1 313 ? 38.506 -8.087 48.344 1.00 24.32 ? 314 VAL A CB 1 ATOM 2259 C CG1 . VAL A 1 313 ? 37.776 -9.287 47.746 1.00 26.04 ? 314 VAL A CG1 1 ATOM 2260 C CG2 . VAL A 1 313 ? 38.658 -6.988 47.274 1.00 24.04 ? 314 VAL A CG2 1 ATOM 2261 N N . ASP A 1 314 ? 35.457 -8.343 49.851 1.00 22.56 ? 315 ASP A N 1 ATOM 2262 C CA . ASP A 1 314 ? 34.007 -8.341 49.690 1.00 22.90 ? 315 ASP A CA 1 ATOM 2263 C C . ASP A 1 314 ? 33.417 -7.166 50.447 1.00 22.27 ? 315 ASP A C 1 ATOM 2264 O O . ASP A 1 314 ? 32.336 -6.704 50.108 1.00 22.42 ? 315 ASP A O 1 ATOM 2265 C CB . ASP A 1 314 ? 33.381 -9.623 50.256 1.00 21.89 ? 315 ASP A CB 1 ATOM 2266 C CG . ASP A 1 314 ? 33.712 -10.854 49.445 1.00 21.17 ? 315 ASP A CG 1 ATOM 2267 O OD1 . ASP A 1 314 ? 33.847 -10.766 48.213 1.00 21.82 ? 315 ASP A OD1 1 ATOM 2268 O OD2 . ASP A 1 314 ? 33.817 -11.926 50.067 1.00 26.26 ? 315 ASP A OD2 1 ATOM 2269 N N . ASP A 1 315 ? 34.086 -6.745 51.516 1.00 22.06 ? 316 ASP A N 1 ATOM 2270 C CA . ASP A 1 315 ? 33.625 -5.622 52.319 1.00 21.03 ? 316 ASP A CA 1 ATOM 2271 C C . ASP A 1 315 ? 34.144 -4.276 51.854 1.00 21.58 ? 316 ASP A C 1 ATOM 2272 O O . ASP A 1 315 ? 33.887 -3.261 52.501 1.00 23.24 ? 316 ASP A O 1 ATOM 2273 C CB . ASP A 1 315 ? 33.988 -5.843 53.767 1.00 21.78 ? 316 ASP A CB 1 ATOM 2274 C CG . ASP A 1 315 ? 33.395 -7.104 54.291 1.00 24.27 ? 316 ASP A CG 1 ATOM 2275 O OD1 . ASP A 1 315 ? 34.153 -8.042 54.565 1.00 22.60 ? 316 ASP A OD1 1 ATOM 2276 O OD2 . ASP A 1 315 ? 32.148 -7.173 54.395 1.00 28.52 ? 316 ASP A OD2 1 ATOM 2277 N N . ILE A 1 316 ? 34.818 -4.277 50.710 1.00 20.12 ? 317 ILE A N 1 ATOM 2278 C CA . ILE A 1 316 ? 35.389 -3.097 50.117 1.00 20.08 ? 317 ILE A CA 1 ATOM 2279 C C . ILE A 1 316 ? 34.445 -2.651 49.025 1.00 21.84 ? 317 ILE A C 1 ATOM 2280 O O . ILE A 1 316 ? 34.070 -3.448 48.160 1.00 21.98 ? 317 ILE A O 1 ATOM 2281 C CB . ILE A 1 316 ? 36.775 -3.423 49.461 1.00 19.56 ? 317 ILE A CB 1 ATOM 2282 C CG1 . ILE A 1 316 ? 37.794 -3.801 50.528 1.00 19.76 ? 317 ILE A CG1 1 ATOM 2283 C CG2 . ILE A 1 316 ? 37.285 -2.259 48.597 1.00 18.08 ? 317 ILE A CG2 1 ATOM 2284 C CD1 . ILE A 1 316 ? 38.373 -2.624 51.282 1.00 20.80 ? 317 ILE A CD1 1 ATOM 2285 N N . GLU A 1 317 ? 34.072 -1.377 49.047 1.00 20.49 ? 318 GLU A N 1 ATOM 2286 C CA . GLU A 1 317 ? 33.197 -0.831 48.019 1.00 22.60 ? 318 GLU A CA 1 ATOM 2287 C C . GLU A 1 317 ? 34.054 -0.364 46.853 1.00 24.14 ? 318 GLU A C 1 ATOM 2288 O O . GLU A 1 317 ? 34.341 0.828 46.698 1.00 24.45 ? 318 GLU A O 1 ATOM 2289 C CB . GLU A 1 317 ? 32.362 0.309 48.587 1.00 21.58 ? 318 GLU A CB 1 ATOM 2290 C CG . GLU A 1 317 ? 31.714 -0.070 49.894 1.00 24.88 ? 318 GLU A CG 1 ATOM 2291 C CD . GLU A 1 317 ? 30.593 0.871 50.304 1.00 27.98 ? 318 GLU A CD 1 ATOM 2292 O OE1 . GLU A 1 317 ? 30.878 1.990 50.769 1.00 22.85 ? 318 GLU A OE1 1 ATOM 2293 O OE2 . GLU A 1 317 ? 29.416 0.470 50.175 1.00 30.61 ? 318 GLU A OE2 1 ATOM 2294 N N . VAL A 1 318 ? 34.526 -1.336 46.079 1.00 25.75 ? 319 VAL A N 1 ATOM 2295 C CA . VAL A 1 318 ? 35.391 -1.082 44.928 1.00 26.85 ? 319 VAL A CA 1 ATOM 2296 C C . VAL A 1 318 ? 34.767 -0.034 44.031 1.00 27.40 ? 319 VAL A C 1 ATOM 2297 O O . VAL A 1 318 ? 33.701 -0.263 43.478 1.00 30.12 ? 319 VAL A O 1 ATOM 2298 C CB . VAL A 1 318 ? 35.659 -2.393 44.137 1.00 26.11 ? 319 VAL A CB 1 ATOM 2299 C CG1 . VAL A 1 318 ? 36.559 -2.123 42.926 1.00 29.36 ? 319 VAL A CG1 1 ATOM 2300 C CG2 . VAL A 1 318 ? 36.299 -3.425 45.060 1.00 26.55 ? 319 VAL A CG2 1 ATOM 2301 N N . SER A 1 319 ? 35.463 1.083 43.843 1.00 28.05 ? 320 SER A N 1 ATOM 2302 C CA . SER A 1 319 ? 34.947 2.183 43.063 1.00 26.31 ? 320 SER A CA 1 ATOM 2303 C C . SER A 1 319 ? 35.732 2.524 41.829 1.00 28.28 ? 320 SER A C 1 ATOM 2304 O O . SER A 1 319 ? 35.407 3.496 41.140 1.00 26.08 ? 320 SER A O 1 ATOM 2305 C CB . SER A 1 319 ? 34.810 3.400 43.949 1.00 25.30 ? 320 SER A CB 1 ATOM 2306 O OG . SER A 1 319 ? 34.117 3.044 45.131 1.00 26.12 ? 320 SER A OG 1 ATOM 2307 N N . CYS A 1 320 ? 36.825 1.806 41.595 1.00 29.85 ? 321 CYS A N 1 ATOM 2308 C CA . CYS A 1 320 ? 37.586 2.036 40.371 1.00 32.73 ? 321 CYS A CA 1 ATOM 2309 C C . CYS A 1 320 ? 37.280 0.872 39.427 1.00 37.07 ? 321 CYS A C 1 ATOM 2310 O O . CYS A 1 320 ? 37.607 -0.280 39.724 1.00 38.63 ? 321 CYS A O 1 ATOM 2311 C CB . CYS A 1 320 ? 39.086 2.118 40.612 1.00 30.08 ? 321 CYS A CB 1 ATOM 2312 S SG . CYS A 1 320 ? 39.976 2.329 39.039 1.00 26.18 ? 321 CYS A SG 1 ATOM 2313 N N . PRO A 1 321 ? 36.575 1.151 38.313 1.00 40.43 ? 322 PRO A N 1 ATOM 2314 C CA . PRO A 1 321 ? 36.242 0.079 37.374 1.00 41.75 ? 322 PRO A CA 1 ATOM 2315 C C . PRO A 1 321 ? 37.430 -0.365 36.539 1.00 42.86 ? 322 PRO A C 1 ATOM 2316 O O . PRO A 1 321 ? 37.760 -1.553 36.488 1.00 45.52 ? 322 PRO A O 1 ATOM 2317 C CB . PRO A 1 321 ? 35.139 0.712 36.521 1.00 42.25 ? 322 PRO A CB 1 ATOM 2318 C CG . PRO A 1 321 ? 35.518 2.178 36.482 1.00 41.13 ? 322 PRO A CG 1 ATOM 2319 C CD . PRO A 1 321 ? 35.949 2.434 37.912 1.00 41.35 ? 322 PRO A CD 1 ATOM 2320 N N . SER A 1 322 ? 38.130 0.603 35.969 1.00 42.79 ? 323 SER A N 1 ATOM 2321 C CA . SER A 1 322 ? 39.260 0.321 35.110 1.00 43.71 ? 323 SER A CA 1 ATOM 2322 C C . SER A 1 322 ? 40.348 -0.521 35.745 1.00 43.03 ? 323 SER A C 1 ATOM 2323 O O . SER A 1 322 ? 41.143 -1.130 35.050 1.00 43.39 ? 323 SER A O 1 ATOM 2324 C CB . SER A 1 322 ? 39.857 1.632 34.607 1.00 45.45 ? 323 SER A CB 1 ATOM 2325 O OG . SER A 1 322 ? 40.138 2.492 35.704 1.00 49.58 ? 323 SER A OG 1 ATOM 2326 N N . GLU A 1 323 ? 40.419 -0.538 37.060 1.00 42.86 ? 324 GLU A N 1 ATOM 2327 C CA . GLU A 1 323 ? 41.468 -1.305 37.684 1.00 43.13 ? 324 GLU A CA 1 ATOM 2328 C C . GLU A 1 323 ? 40.950 -2.164 38.815 1.00 41.55 ? 324 GLU A C 1 ATOM 2329 O O . GLU A 1 323 ? 40.146 -1.746 39.644 1.00 39.62 ? 324 GLU A O 1 ATOM 2330 C CB . GLU A 1 323 ? 42.608 -0.389 38.159 1.00 46.63 ? 324 GLU A CB 1 ATOM 2331 C CG . GLU A 1 323 ? 43.426 0.257 37.035 1.00 52.45 ? 324 GLU A CG 1 ATOM 2332 C CD . GLU A 1 323 ? 43.626 1.779 37.213 1.00 57.58 ? 324 GLU A CD 1 ATOM 2333 O OE1 . GLU A 1 323 ? 43.128 2.568 36.364 1.00 58.27 ? 324 GLU A OE1 1 ATOM 2334 O OE2 . GLU A 1 323 ? 44.295 2.195 38.196 1.00 60.87 ? 324 GLU A OE2 1 ATOM 2335 N N . PRO A 1 324 ? 41.370 -3.423 38.822 1.00 40.97 ? 325 PRO A N 1 ATOM 2336 C CA . PRO A 1 324 ? 40.970 -4.386 39.845 1.00 38.61 ? 325 PRO A CA 1 ATOM 2337 C C . PRO A 1 324 ? 41.602 -4.052 41.176 1.00 36.07 ? 325 PRO A C 1 ATOM 2338 O O . PRO A 1 324 ? 42.729 -3.552 41.244 1.00 35.32 ? 325 PRO A O 1 ATOM 2339 C CB . PRO A 1 324 ? 41.492 -5.714 39.290 1.00 40.82 ? 325 PRO A CB 1 ATOM 2340 C CG . PRO A 1 324 ? 42.704 -5.298 38.451 1.00 42.49 ? 325 PRO A CG 1 ATOM 2341 C CD . PRO A 1 324 ? 42.195 -4.047 37.769 1.00 42.47 ? 325 PRO A CD 1 ATOM 2342 N N . PHE A 1 325 ? 40.875 -4.332 42.242 1.00 33.27 ? 326 PHE A N 1 ATOM 2343 C CA . PHE A 1 325 ? 41.393 -4.052 43.561 1.00 32.42 ? 326 PHE A CA 1 ATOM 2344 C C . PHE A 1 325 ? 42.594 -4.958 43.840 1.00 33.28 ? 326 PHE A C 1 ATOM 2345 O O . PHE A 1 325 ? 42.525 -6.182 43.686 1.00 34.14 ? 326 PHE A O 1 ATOM 2346 C CB . PHE A 1 325 ? 40.304 -4.248 44.617 1.00 29.49 ? 326 PHE A CB 1 ATOM 2347 C CG . PHE A 1 325 ? 40.631 -3.628 45.926 1.00 25.83 ? 326 PHE A CG 1 ATOM 2348 C CD1 . PHE A 1 325 ? 40.490 -2.265 46.108 1.00 25.24 ? 326 PHE A CD1 1 ATOM 2349 C CD2 . PHE A 1 325 ? 41.142 -4.396 46.960 1.00 25.22 ? 326 PHE A CD2 1 ATOM 2350 C CE1 . PHE A 1 325 ? 40.857 -1.674 47.297 1.00 25.20 ? 326 PHE A CE1 1 ATOM 2351 C CE2 . PHE A 1 325 ? 41.516 -3.810 48.167 1.00 24.84 ? 326 PHE A CE2 1 ATOM 2352 C CZ . PHE A 1 325 ? 41.372 -2.443 48.334 1.00 24.24 ? 326 PHE A CZ 1 ATOM 2353 N N . PRO A 1 326 ? 43.721 -4.359 44.239 1.00 33.77 ? 327 PRO A N 1 ATOM 2354 C CA . PRO A 1 326 ? 44.947 -5.112 44.540 1.00 33.61 ? 327 PRO A CA 1 ATOM 2355 C C . PRO A 1 326 ? 44.812 -6.218 45.588 1.00 33.68 ? 327 PRO A C 1 ATOM 2356 O O . PRO A 1 326 ? 43.886 -6.224 46.402 1.00 32.79 ? 327 PRO A O 1 ATOM 2357 C CB . PRO A 1 326 ? 45.915 -4.012 45.008 1.00 32.65 ? 327 PRO A CB 1 ATOM 2358 C CG . PRO A 1 326 ? 45.015 -2.887 45.453 1.00 32.44 ? 327 PRO A CG 1 ATOM 2359 C CD . PRO A 1 326 ? 43.947 -2.910 44.398 1.00 31.99 ? 327 PRO A CD 1 ATOM 2360 N N . GLU A 1 327 ? 45.744 -7.164 45.548 1.00 33.84 ? 328 GLU A N 1 ATOM 2361 C CA . GLU A 1 327 ? 45.764 -8.254 46.515 1.00 33.69 ? 328 GLU A CA 1 ATOM 2362 C C . GLU A 1 327 ? 46.393 -7.697 47.777 1.00 30.99 ? 328 GLU A C 1 ATOM 2363 O O . GLU A 1 327 ? 47.535 -7.261 47.762 1.00 31.79 ? 328 GLU A O 1 ATOM 2364 C CB . GLU A 1 327 ? 46.600 -9.423 45.986 1.00 38.45 ? 328 GLU A CB 1 ATOM 2365 C CG . GLU A 1 327 ? 45.812 -10.711 45.786 1.00 45.63 ? 328 GLU A CG 1 ATOM 2366 C CD . GLU A 1 327 ? 44.693 -10.570 44.752 1.00 50.61 ? 328 GLU A CD 1 ATOM 2367 O OE1 . GLU A 1 327 ? 45.027 -10.464 43.542 1.00 54.61 ? 328 GLU A OE1 1 ATOM 2368 O OE2 . GLU A 1 327 ? 43.490 -10.571 45.143 1.00 50.60 ? 328 GLU A OE2 1 ATOM 2369 N N . ILE A 1 328 ? 45.655 -7.712 48.871 1.00 28.93 ? 329 ILE A N 1 ATOM 2370 C CA . ILE A 1 328 ? 46.148 -7.171 50.130 1.00 27.79 ? 329 ILE A CA 1 ATOM 2371 C C . ILE A 1 328 ? 46.069 -8.300 51.132 1.00 26.33 ? 329 ILE A C 1 ATOM 2372 O O . ILE A 1 328 ? 45.321 -9.230 50.919 1.00 28.72 ? 329 ILE A O 1 ATOM 2373 C CB . ILE A 1 328 ? 45.220 -5.968 50.597 1.00 27.11 ? 329 ILE A CB 1 ATOM 2374 C CG1 . ILE A 1 328 ? 45.179 -4.882 49.530 1.00 27.97 ? 329 ILE A CG1 1 ATOM 2375 C CG2 . ILE A 1 328 ? 45.731 -5.322 51.863 1.00 25.14 ? 329 ILE A CG2 1 ATOM 2376 C CD1 . ILE A 1 328 ? 46.519 -4.287 49.265 1.00 28.10 ? 329 ILE A CD1 1 ATOM 2377 N N . ALA A 1 329 ? 46.828 -8.226 52.217 1.00 27.06 ? 330 ALA A N 1 ATOM 2378 C CA . ALA A 1 329 ? 46.796 -9.240 53.261 1.00 26.82 ? 330 ALA A CA 1 ATOM 2379 C C . ALA A 1 329 ? 45.501 -9.076 54.063 1.00 29.16 ? 330 ALA A C 1 ATOM 2380 O O . ALA A 1 329 ? 45.019 -7.958 54.253 1.00 27.12 ? 330 ALA A O 1 ATOM 2381 C CB . ALA A 1 329 ? 48.004 -9.092 54.180 1.00 25.54 ? 330 ALA A CB 1 ATOM 2382 N N . THR A 1 330 ? 44.932 -10.190 54.516 1.00 30.73 ? 331 THR A N 1 ATOM 2383 C CA . THR A 1 330 ? 43.698 -10.190 55.298 1.00 34.31 ? 331 THR A CA 1 ATOM 2384 C C . THR A 1 330 ? 44.020 -10.629 56.711 1.00 35.48 ? 331 THR A C 1 ATOM 2385 O O . THR A 1 330 ? 44.706 -11.621 56.914 1.00 36.72 ? 331 THR A O 1 ATOM 2386 C CB . THR A 1 330 ? 42.658 -11.197 54.776 1.00 35.10 ? 331 THR A CB 1 ATOM 2387 O OG1 . THR A 1 330 ? 42.396 -10.995 53.380 1.00 36.62 ? 331 THR A OG1 1 ATOM 2388 C CG2 . THR A 1 330 ? 41.374 -11.052 55.577 1.00 40.58 ? 331 THR A CG2 1 ATOM 2389 N N . ALA A 1 331 ? 43.537 -9.889 57.691 1.00 37.42 ? 332 ALA A N 1 ATOM 2390 C CA . ALA A 1 331 ? 43.781 -10.240 59.071 1.00 40.10 ? 332 ALA A CA 1 ATOM 2391 C C . ALA A 1 331 ? 42.555 -11.014 59.564 1.00 42.48 ? 332 ALA A C 1 ATOM 2392 O O . ALA A 1 331 ? 41.488 -10.968 58.935 1.00 45.23 ? 332 ALA A O 1 ATOM 2393 C CB . ALA A 1 331 ? 43.997 -8.982 59.886 1.00 38.85 ? 332 ALA A CB 1 ATOM 2394 N N . SER A 1 332 ? 42.716 -11.745 60.663 1.00 44.20 ? 333 SER A N 1 ATOM 2395 C CA . SER A 1 332 ? 41.617 -12.514 61.225 1.00 44.63 ? 333 SER A CA 1 ATOM 2396 C C . SER A 1 332 ? 40.848 -11.671 62.220 1.00 44.83 ? 333 SER A C 1 ATOM 2397 O O . SER A 1 332 ? 41.387 -10.696 62.761 1.00 45.18 ? 333 SER A O 1 ATOM 2398 N N . GLY A 1 333 ? 39.585 -12.030 62.439 1.00 44.24 ? 334 GLY A N 1 ATOM 2399 C CA . GLY A 1 333 ? 38.725 -11.301 63.368 1.00 41.73 ? 334 GLY A CA 1 ATOM 2400 C C . GLY A 1 333 ? 39.137 -11.350 64.833 1.00 40.64 ? 334 GLY A C 1 ATOM 2401 O O . GLY A 1 333 ? 40.179 -11.901 65.173 1.00 42.67 ? 334 GLY A O 1 ATOM 2402 N N . PRO A 1 334 ? 38.366 -10.728 65.726 1.00 38.68 ? 335 PRO A N 1 ATOM 2403 C CA . PRO A 1 334 ? 37.152 -10.001 65.364 1.00 37.39 ? 335 PRO A CA 1 ATOM 2404 C C . PRO A 1 334 ? 37.489 -8.560 64.945 1.00 35.27 ? 335 PRO A C 1 ATOM 2405 O O . PRO A 1 334 ? 38.663 -8.181 64.823 1.00 34.61 ? 335 PRO A O 1 ATOM 2406 C CB . PRO A 1 334 ? 36.359 -10.021 66.669 1.00 37.75 ? 335 PRO A CB 1 ATOM 2407 C CG . PRO A 1 334 ? 37.455 -9.821 67.705 1.00 37.92 ? 335 PRO A CG 1 ATOM 2408 C CD . PRO A 1 334 ? 38.593 -10.710 67.185 1.00 38.37 ? 335 PRO A CD 1 ATOM 2409 N N . LEU A 1 335 ? 36.433 -7.772 64.761 1.00 33.53 ? 336 LEU A N 1 ATOM 2410 C CA . LEU A 1 335 ? 36.506 -6.366 64.384 1.00 29.84 ? 336 LEU A CA 1 ATOM 2411 C C . LEU A 1 335 ? 37.215 -5.619 65.516 1.00 28.31 ? 336 LEU A C 1 ATOM 2412 O O . LEU A 1 335 ? 36.926 -5.854 66.703 1.00 26.97 ? 336 LEU A O 1 ATOM 2413 C CB . LEU A 1 335 ? 35.077 -5.836 64.241 1.00 28.79 ? 336 LEU A CB 1 ATOM 2414 C CG . LEU A 1 335 ? 34.634 -5.153 62.961 1.00 28.34 ? 336 LEU A CG 1 ATOM 2415 C CD1 . LEU A 1 335 ? 35.154 -5.878 61.746 1.00 28.96 ? 336 LEU A CD1 1 ATOM 2416 C CD2 . LEU A 1 335 ? 33.117 -5.084 62.949 1.00 30.81 ? 336 LEU A CD2 1 ATOM 2417 N N . PRO A 1 336 ? 38.220 -4.781 65.174 1.00 26.71 ? 337 PRO A N 1 ATOM 2418 C CA . PRO A 1 336 ? 38.925 -4.033 66.231 1.00 24.55 ? 337 PRO A CA 1 ATOM 2419 C C . PRO A 1 336 ? 38.085 -2.899 66.813 1.00 22.37 ? 337 PRO A C 1 ATOM 2420 O O . PRO A 1 336 ? 37.038 -2.555 66.294 1.00 21.70 ? 337 PRO A O 1 ATOM 2421 C CB . PRO A 1 336 ? 40.175 -3.504 65.518 1.00 24.12 ? 337 PRO A CB 1 ATOM 2422 C CG . PRO A 1 336 ? 39.757 -3.395 64.076 1.00 24.86 ? 337 PRO A CG 1 ATOM 2423 C CD . PRO A 1 336 ? 38.860 -4.605 63.853 1.00 25.42 ? 337 PRO A CD 1 ATOM 2424 N N . SER A 1 337 ? 38.484 -2.409 67.963 1.00 23.32 ? 338 SER A N 1 ATOM 2425 C CA . SER A 1 337 ? 37.792 -1.294 68.575 1.00 26.79 ? 338 SER A CA 1 ATOM 2426 C C . SER A 1 337 ? 38.915 -0.313 68.874 1.00 25.52 ? 338 SER A C 1 ATOM 2427 O O . SER A 1 337 ? 39.702 -0.541 69.792 1.00 25.72 ? 338 SER A O 1 ATOM 2428 C CB . SER A 1 337 ? 37.125 -1.713 69.877 1.00 30.45 ? 338 SER A CB 1 ATOM 2429 O OG . SER A 1 337 ? 36.095 -0.825 70.371 1.00 34.43 ? 338 SER A OG 1 ATOM 2430 N N . LEU A 1 338 ? 38.972 0.777 68.113 1.00 24.32 ? 339 LEU A N 1 ATOM 2431 C CA . LEU A 1 338 ? 40.035 1.776 68.262 1.00 23.59 ? 339 LEU A CA 1 ATOM 2432 C C . LEU A 1 338 ? 39.942 2.643 69.486 1.00 23.82 ? 339 LEU A C 1 ATOM 2433 O O . LEU A 1 338 ? 38.850 3.119 69.871 1.00 23.60 ? 339 LEU A O 1 ATOM 2434 C CB . LEU A 1 338 ? 40.123 2.705 67.047 1.00 20.69 ? 339 LEU A CB 1 ATOM 2435 C CG . LEU A 1 338 ? 40.164 2.066 65.683 1.00 21.99 ? 339 LEU A CG 1 ATOM 2436 C CD1 . LEU A 1 338 ? 40.627 3.151 64.749 1.00 22.00 ? 339 LEU A CD1 1 ATOM 2437 C CD2 . LEU A 1 338 ? 41.095 0.837 65.648 1.00 23.39 ? 339 LEU A CD2 1 ATOM 2438 N N . ALA A 1 339 ? 41.121 2.872 70.054 1.00 22.76 ? 340 ALA A N 1 ATOM 2439 C CA . ALA A 1 339 ? 41.301 3.723 71.217 1.00 23.14 ? 340 ALA A CA 1 ATOM 2440 C C . ALA A 1 339 ? 41.553 5.135 70.659 1.00 22.99 ? 340 ALA A C 1 ATOM 2441 O O . ALA A 1 339 ? 41.912 5.303 69.483 1.00 21.69 ? 340 ALA A O 1 ATOM 2442 C CB . ALA A 1 339 ? 42.520 3.254 72.042 1.00 22.29 ? 340 ALA A CB 1 ATOM 2443 N N . PRO A 1 340 ? 41.334 6.165 71.493 1.00 23.43 ? 341 PRO A N 1 ATOM 2444 C CA . PRO A 1 340 ? 41.546 7.552 71.071 1.00 22.60 ? 341 PRO A CA 1 ATOM 2445 C C . PRO A 1 340 ? 43.005 7.722 70.686 1.00 23.32 ? 341 PRO A C 1 ATOM 2446 O O . PRO A 1 340 ? 43.862 7.048 71.257 1.00 22.51 ? 341 PRO A O 1 ATOM 2447 C CB . PRO A 1 340 ? 41.253 8.339 72.349 1.00 22.66 ? 341 PRO A CB 1 ATOM 2448 C CG . PRO A 1 340 ? 40.261 7.484 73.059 1.00 23.37 ? 341 PRO A CG 1 ATOM 2449 C CD . PRO A 1 340 ? 40.820 6.103 72.874 1.00 22.13 ? 341 PRO A CD 1 ATOM 2450 N N . ALA A 1 341 ? 43.275 8.566 69.689 1.00 21.67 ? 342 ALA A N 1 ATOM 2451 C CA . ALA A 1 341 ? 44.642 8.848 69.270 1.00 20.15 ? 342 ALA A CA 1 ATOM 2452 C C . ALA A 1 341 ? 45.298 9.619 70.443 1.00 19.93 ? 342 ALA A C 1 ATOM 2453 O O . ALA A 1 341 ? 44.626 10.347 71.188 1.00 19.41 ? 342 ALA A O 1 ATOM 2454 C CB . ALA A 1 341 ? 44.637 9.665 68.009 1.00 19.26 ? 342 ALA A CB 1 ATOM 2455 N N . PRO A 1 342 ? 46.598 9.409 70.665 1.00 19.67 ? 343 PRO A N 1 ATOM 2456 C CA . PRO A 1 342 ? 47.333 10.067 71.754 1.00 21.70 ? 343 PRO A CA 1 ATOM 2457 C C . PRO A 1 342 ? 47.531 11.589 71.598 1.00 23.54 ? 343 PRO A C 1 ATOM 2458 O O . PRO A 1 342 ? 47.586 12.277 72.634 1.00 26.95 ? 343 PRO A O 1 ATOM 2459 C CB . PRO A 1 342 ? 48.660 9.317 71.759 1.00 19.87 ? 343 PRO A CB 1 ATOM 2460 C CG . PRO A 1 342 ? 48.868 9.009 70.302 1.00 21.45 ? 343 PRO A CG 1 ATOM 2461 C CD . PRO A 1 342 ? 47.500 8.622 69.799 1.00 21.20 ? 343 PRO A CD 1 ATOM 2462 O OXT . PRO A 1 342 ? 47.615 12.089 70.461 1.00 24.23 ? 343 PRO A OXT 1 ATOM 2463 N N . SER B 1 7 ? 80.076 45.445 13.547 1.00 40.25 ? 8 SER B N 1 ATOM 2464 C CA . SER B 1 7 ? 79.799 44.774 14.843 1.00 39.78 ? 8 SER B CA 1 ATOM 2465 C C . SER B 1 7 ? 80.209 45.691 16.000 1.00 37.51 ? 8 SER B C 1 ATOM 2466 O O . SER B 1 7 ? 81.188 46.436 15.888 1.00 39.22 ? 8 SER B O 1 ATOM 2467 C CB . SER B 1 7 ? 80.546 43.447 14.920 1.00 41.06 ? 8 SER B CB 1 ATOM 2468 O OG . SER B 1 7 ? 80.152 42.719 16.067 1.00 43.85 ? 8 SER B OG 1 ATOM 2469 N N . VAL B 1 8 ? 79.471 45.608 17.102 1.00 31.97 ? 9 VAL B N 1 ATOM 2470 C CA . VAL B 1 8 ? 79.698 46.432 18.267 1.00 27.02 ? 9 VAL B CA 1 ATOM 2471 C C . VAL B 1 8 ? 79.530 45.597 19.514 1.00 25.05 ? 9 VAL B C 1 ATOM 2472 O O . VAL B 1 8 ? 78.665 44.734 19.570 1.00 24.95 ? 9 VAL B O 1 ATOM 2473 C CB . VAL B 1 8 ? 78.609 47.515 18.327 1.00 25.36 ? 9 VAL B CB 1 ATOM 2474 C CG1 . VAL B 1 8 ? 78.689 48.310 19.595 1.00 24.93 ? 9 VAL B CG1 1 ATOM 2475 C CG2 . VAL B 1 8 ? 78.701 48.398 17.132 1.00 27.59 ? 9 VAL B CG2 1 ATOM 2476 N N . THR B 1 9 ? 80.304 45.898 20.542 1.00 23.03 ? 10 THR B N 1 ATOM 2477 C CA . THR B 1 9 ? 80.191 45.198 21.809 1.00 21.66 ? 10 THR B CA 1 ATOM 2478 C C . THR B 1 9 ? 79.609 46.207 22.788 1.00 21.98 ? 10 THR B C 1 ATOM 2479 O O . THR B 1 9 ? 80.238 47.210 23.087 1.00 21.30 ? 10 THR B O 1 ATOM 2480 C CB . THR B 1 9 ? 81.573 44.689 22.279 1.00 21.07 ? 10 THR B CB 1 ATOM 2481 O OG1 . THR B 1 9 ? 82.131 43.892 21.232 1.00 18.82 ? 10 THR B OG1 1 ATOM 2482 C CG2 . THR B 1 9 ? 81.467 43.853 23.524 1.00 19.91 ? 10 THR B CG2 1 ATOM 2483 N N . CYS B 1 10 ? 78.381 45.964 23.230 1.00 21.60 ? 11 CYS B N 1 ATOM 2484 C CA . CYS B 1 10 ? 77.706 46.855 24.138 1.00 22.84 ? 11 CYS B CA 1 ATOM 2485 C C . CYS B 1 10 ? 78.344 46.742 25.479 1.00 25.43 ? 11 CYS B C 1 ATOM 2486 O O . CYS B 1 10 ? 79.013 45.753 25.779 1.00 27.81 ? 11 CYS B O 1 ATOM 2487 C CB . CYS B 1 10 ? 76.210 46.516 24.220 1.00 20.42 ? 11 CYS B CB 1 ATOM 2488 S SG . CYS B 1 10 ? 75.446 46.536 22.569 1.00 21.80 ? 11 CYS B SG 1 ATOM 2489 N N . PRO B 1 11 ? 78.119 47.745 26.326 1.00 27.22 ? 12 PRO B N 1 ATOM 2490 C CA . PRO B 1 11 ? 78.638 47.855 27.692 1.00 30.11 ? 12 PRO B CA 1 ATOM 2491 C C . PRO B 1 11 ? 78.610 46.569 28.530 1.00 33.08 ? 12 PRO B C 1 ATOM 2492 O O . PRO B 1 11 ? 79.534 46.328 29.321 1.00 35.68 ? 12 PRO B O 1 ATOM 2493 C CB . PRO B 1 11 ? 77.737 48.928 28.297 1.00 28.53 ? 12 PRO B CB 1 ATOM 2494 C CG . PRO B 1 11 ? 77.550 49.855 27.151 1.00 28.49 ? 12 PRO B CG 1 ATOM 2495 C CD . PRO B 1 11 ? 77.321 48.933 25.972 1.00 27.35 ? 12 PRO B CD 1 ATOM 2496 N N . GLY B 1 12 ? 77.555 45.762 28.366 1.00 33.73 ? 13 GLY B N 1 ATOM 2497 C CA . GLY B 1 12 ? 77.421 44.534 29.133 1.00 33.80 ? 13 GLY B CA 1 ATOM 2498 C C . GLY B 1 12 ? 78.044 43.281 28.538 1.00 34.12 ? 13 GLY B C 1 ATOM 2499 O O . GLY B 1 12 ? 77.753 42.178 28.997 1.00 34.40 ? 13 GLY B O 1 ATOM 2500 N N . GLY B 1 13 ? 78.843 43.441 27.485 1.00 33.72 ? 14 GLY B N 1 ATOM 2501 C CA . GLY B 1 13 ? 79.503 42.312 26.848 1.00 31.72 ? 14 GLY B CA 1 ATOM 2502 C C . GLY B 1 13 ? 78.817 41.787 25.611 1.00 30.89 ? 14 GLY B C 1 ATOM 2503 O O . GLY B 1 13 ? 79.441 41.135 24.770 1.00 31.81 ? 14 GLY B O 1 ATOM 2504 N N . GLN B 1 14 ? 77.527 42.074 25.491 1.00 30.86 ? 15 GLN B N 1 ATOM 2505 C CA . GLN B 1 14 ? 76.747 41.619 24.353 1.00 29.36 ? 15 GLN B CA 1 ATOM 2506 C C . GLN B 1 14 ? 77.189 42.246 23.057 1.00 28.71 ? 15 GLN B C 1 ATOM 2507 O O . GLN B 1 14 ? 77.297 43.460 22.931 1.00 28.76 ? 15 GLN B O 1 ATOM 2508 C CB . GLN B 1 14 ? 75.252 41.892 24.547 1.00 31.32 ? 15 GLN B CB 1 ATOM 2509 C CG . GLN B 1 14 ? 74.708 41.551 25.921 1.00 32.41 ? 15 GLN B CG 1 ATOM 2510 C CD . GLN B 1 14 ? 74.626 42.759 26.857 1.00 35.52 ? 15 GLN B CD 1 ATOM 2511 O OE1 . GLN B 1 14 ? 74.083 42.658 27.968 1.00 36.48 ? 15 GLN B OE1 1 ATOM 2512 N NE2 . GLN B 1 14 ? 75.151 43.912 26.414 1.00 35.91 ? 15 GLN B NE2 1 ATOM 2513 N N . SER B 1 15 ? 77.359 41.394 22.067 1.00 28.22 ? 16 SER B N 1 ATOM 2514 C CA . SER B 1 15 ? 77.759 41.804 20.739 1.00 28.54 ? 16 SER B CA 1 ATOM 2515 C C . SER B 1 15 ? 76.513 41.981 19.860 1.00 28.50 ? 16 SER B C 1 ATOM 2516 O O . SER B 1 15 ? 75.518 41.267 20.017 1.00 28.79 ? 16 SER B O 1 ATOM 2517 C CB . SER B 1 15 ? 78.689 40.748 20.163 1.00 29.28 ? 16 SER B CB 1 ATOM 2518 O OG . SER B 1 15 ? 78.736 40.857 18.763 1.00 37.04 ? 16 SER B OG 1 ATOM 2519 N N . THR B 1 16 ? 76.576 42.904 18.912 1.00 26.64 ? 17 THR B N 1 ATOM 2520 C CA . THR B 1 16 ? 75.437 43.168 18.057 1.00 24.81 ? 17 THR B CA 1 ATOM 2521 C C . THR B 1 16 ? 75.875 43.807 16.743 1.00 24.32 ? 17 THR B C 1 ATOM 2522 O O . THR B 1 16 ? 77.053 44.055 16.524 1.00 24.71 ? 17 THR B O 1 ATOM 2523 C CB . THR B 1 16 ? 74.383 44.050 18.794 1.00 24.33 ? 17 THR B CB 1 ATOM 2524 O OG1 . THR B 1 16 ? 73.217 44.130 17.982 1.00 24.71 ? 17 THR B OG1 1 ATOM 2525 C CG2 . THR B 1 16 ? 74.897 45.481 19.032 1.00 21.45 ? 17 THR B CG2 1 ATOM 2526 N N . SER B 1 17 ? 74.920 44.105 15.879 1.00 24.81 ? 18 SER B N 1 ATOM 2527 C CA . SER B 1 17 ? 75.228 44.674 14.573 1.00 25.38 ? 18 SER B CA 1 ATOM 2528 C C . SER B 1 17 ? 75.252 46.196 14.509 1.00 24.81 ? 18 SER B C 1 ATOM 2529 O O . SER B 1 17 ? 75.854 46.761 13.592 1.00 24.61 ? 18 SER B O 1 ATOM 2530 C CB . SER B 1 17 ? 74.198 44.181 13.541 1.00 28.12 ? 18 SER B CB 1 ATOM 2531 O OG . SER B 1 17 ? 72.870 44.288 14.069 1.00 31.90 ? 18 SER B OG 1 ATOM 2532 N N . ASN B 1 18 ? 74.635 46.862 15.475 1.00 22.50 ? 19 ASN B N 1 ATOM 2533 C CA . ASN B 1 18 ? 74.563 48.315 15.406 1.00 21.27 ? 19 ASN B CA 1 ATOM 2534 C C . ASN B 1 18 ? 74.468 48.853 16.816 1.00 19.83 ? 19 ASN B C 1 ATOM 2535 O O . ASN B 1 18 ? 73.856 48.212 17.676 1.00 19.95 ? 19 ASN B O 1 ATOM 2536 C CB . ASN B 1 18 ? 73.327 48.672 14.586 1.00 23.54 ? 19 ASN B CB 1 ATOM 2537 C CG . ASN B 1 18 ? 73.271 50.120 14.209 1.00 27.60 ? 19 ASN B CG 1 ATOM 2538 O OD1 . ASN B 1 18 ? 73.120 50.999 15.065 1.00 29.98 ? 19 ASN B OD1 1 ATOM 2539 N ND2 . ASN B 1 18 ? 73.353 50.386 12.917 1.00 28.38 ? 19 ASN B ND2 1 ATOM 2540 N N . SER B 1 19 ? 75.090 50.004 17.076 1.00 18.37 ? 20 SER B N 1 ATOM 2541 C CA . SER B 1 19 ? 75.067 50.591 18.418 1.00 17.98 ? 20 SER B CA 1 ATOM 2542 C C . SER B 1 19 ? 73.659 50.999 18.858 1.00 16.96 ? 20 SER B C 1 ATOM 2543 O O . SER B 1 19 ? 73.415 51.214 20.046 1.00 18.13 ? 20 SER B O 1 ATOM 2544 C CB . SER B 1 19 ? 76.002 51.786 18.510 1.00 15.37 ? 20 SER B CB 1 ATOM 2545 O OG . SER B 1 19 ? 75.508 52.848 17.735 1.00 18.51 ? 20 SER B OG 1 ATOM 2546 N N . GLN B 1 20 ? 72.746 51.137 17.902 1.00 17.15 ? 21 GLN B N 1 ATOM 2547 C CA . GLN B 1 20 ? 71.355 51.467 18.210 1.00 17.30 ? 21 GLN B CA 1 ATOM 2548 C C . GLN B 1 20 ? 70.679 50.305 18.931 1.00 19.23 ? 21 GLN B C 1 ATOM 2549 O O . GLN B 1 20 ? 69.706 50.499 19.678 1.00 18.52 ? 21 GLN B O 1 ATOM 2550 C CB . GLN B 1 20 ? 70.604 51.773 16.933 1.00 19.55 ? 21 GLN B CB 1 ATOM 2551 C CG . GLN B 1 20 ? 71.123 52.979 16.219 1.00 25.17 ? 21 GLN B CG 1 ATOM 2552 C CD . GLN B 1 20 ? 70.254 53.341 15.062 1.00 29.94 ? 21 GLN B CD 1 ATOM 2553 O OE1 . GLN B 1 20 ? 69.024 53.394 15.191 1.00 34.18 ? 21 GLN B OE1 1 ATOM 2554 N NE2 . GLN B 1 20 ? 70.865 53.568 13.909 1.00 32.68 ? 21 GLN B NE2 1 ATOM 2555 N N . CYS B 1 21 ? 71.235 49.093 18.776 1.00 18.20 ? 22 CYS B N 1 ATOM 2556 C CA . CYS B 1 21 ? 70.648 47.922 19.420 1.00 17.82 ? 22 CYS B CA 1 ATOM 2557 C C . CYS B 1 21 ? 71.007 47.771 20.878 1.00 16.25 ? 22 CYS B C 1 ATOM 2558 O O . CYS B 1 21 ? 70.328 47.031 21.588 1.00 17.76 ? 22 CYS B O 1 ATOM 2559 C CB . CYS B 1 21 ? 71.042 46.620 18.710 1.00 14.52 ? 22 CYS B CB 1 ATOM 2560 S SG . CYS B 1 21 ? 70.757 46.549 16.941 1.00 16.30 ? 22 CYS B SG 1 ATOM 2561 N N . CYS B 1 22 ? 72.046 48.467 21.346 1.00 16.46 ? 23 CYS B N 1 ATOM 2562 C CA . CYS B 1 22 ? 72.485 48.299 22.742 1.00 15.55 ? 23 CYS B CA 1 ATOM 2563 C C . CYS B 1 22 ? 71.466 48.577 23.819 1.00 15.97 ? 23 CYS B C 1 ATOM 2564 O O . CYS B 1 22 ? 71.381 47.818 24.783 1.00 15.71 ? 23 CYS B O 1 ATOM 2565 C CB . CYS B 1 22 ? 73.785 49.068 23.062 1.00 16.32 ? 23 CYS B CB 1 ATOM 2566 S SG . CYS B 1 22 ? 75.259 48.527 22.121 1.00 19.48 ? 23 CYS B SG 1 ATOM 2567 N N . VAL B 1 23 ? 70.706 49.664 23.697 1.00 15.52 ? 24 VAL B N 1 ATOM 2568 C CA . VAL B 1 23 ? 69.713 49.968 24.737 1.00 13.51 ? 24 VAL B CA 1 ATOM 2569 C C . VAL B 1 23 ? 68.724 48.803 24.890 1.00 10.18 ? 24 VAL B C 1 ATOM 2570 O O . VAL B 1 23 ? 68.294 48.477 25.987 1.00 10.75 ? 24 VAL B O 1 ATOM 2571 C CB . VAL B 1 23 ? 68.941 51.331 24.473 1.00 13.46 ? 24 VAL B CB 1 ATOM 2572 C CG1 . VAL B 1 23 ? 68.203 51.323 23.164 1.00 10.68 ? 24 VAL B CG1 1 ATOM 2573 C CG2 . VAL B 1 23 ? 67.986 51.627 25.607 1.00 11.99 ? 24 VAL B CG2 1 ATOM 2574 N N . TRP B 1 24 ? 68.483 48.115 23.791 1.00 11.34 ? 25 TRP B N 1 ATOM 2575 C CA . TRP B 1 24 ? 67.536 47.015 23.790 1.00 13.51 ? 25 TRP B CA 1 ATOM 2576 C C . TRP B 1 24 ? 67.890 45.831 24.677 1.00 14.85 ? 25 TRP B C 1 ATOM 2577 O O . TRP B 1 24 ? 67.011 45.119 25.125 1.00 16.30 ? 25 TRP B O 1 ATOM 2578 C CB . TRP B 1 24 ? 67.223 46.629 22.355 1.00 12.70 ? 25 TRP B CB 1 ATOM 2579 C CG . TRP B 1 24 ? 66.536 47.769 21.635 1.00 14.06 ? 25 TRP B CG 1 ATOM 2580 C CD1 . TRP B 1 24 ? 67.060 48.533 20.638 1.00 12.84 ? 25 TRP B CD1 1 ATOM 2581 C CD2 . TRP B 1 24 ? 65.220 48.308 21.907 1.00 14.71 ? 25 TRP B CD2 1 ATOM 2582 N NE1 . TRP B 1 24 ? 66.166 49.513 20.277 1.00 15.62 ? 25 TRP B NE1 1 ATOM 2583 C CE2 . TRP B 1 24 ? 65.028 49.402 21.037 1.00 15.37 ? 25 TRP B CE2 1 ATOM 2584 C CE3 . TRP B 1 24 ? 64.183 47.968 22.801 1.00 15.06 ? 25 TRP B CE3 1 ATOM 2585 C CZ2 . TRP B 1 24 ? 63.843 50.175 21.026 1.00 13.46 ? 25 TRP B CZ2 1 ATOM 2586 C CZ3 . TRP B 1 24 ? 62.996 48.738 22.794 1.00 14.11 ? 25 TRP B CZ3 1 ATOM 2587 C CH2 . TRP B 1 24 ? 62.848 49.829 21.909 1.00 13.94 ? 25 TRP B CH2 1 ATOM 2588 N N . PHE B 1 25 ? 69.168 45.633 24.981 1.00 15.11 ? 26 PHE B N 1 ATOM 2589 C CA . PHE B 1 25 ? 69.531 44.553 25.888 1.00 14.98 ? 26 PHE B CA 1 ATOM 2590 C C . PHE B 1 25 ? 69.078 44.919 27.289 1.00 15.03 ? 26 PHE B C 1 ATOM 2591 O O . PHE B 1 25 ? 68.707 44.044 28.070 1.00 15.69 ? 26 PHE B O 1 ATOM 2592 C CB . PHE B 1 25 ? 71.050 44.300 25.894 1.00 17.56 ? 26 PHE B CB 1 ATOM 2593 C CG . PHE B 1 25 ? 71.546 43.665 24.658 1.00 19.12 ? 26 PHE B CG 1 ATOM 2594 C CD1 . PHE B 1 25 ? 72.251 44.410 23.728 1.00 19.31 ? 26 PHE B CD1 1 ATOM 2595 C CD2 . PHE B 1 25 ? 71.213 42.331 24.368 1.00 20.08 ? 26 PHE B CD2 1 ATOM 2596 C CE1 . PHE B 1 25 ? 72.607 43.842 22.511 1.00 21.81 ? 26 PHE B CE1 1 ATOM 2597 C CE2 . PHE B 1 25 ? 71.569 41.760 23.158 1.00 19.77 ? 26 PHE B CE2 1 ATOM 2598 C CZ . PHE B 1 25 ? 72.263 42.514 22.223 1.00 21.40 ? 26 PHE B CZ 1 ATOM 2599 N N . ASP B 1 26 ? 69.126 46.202 27.639 1.00 15.47 ? 27 ASP B N 1 ATOM 2600 C CA . ASP B 1 26 ? 68.680 46.581 28.975 1.00 15.58 ? 27 ASP B CA 1 ATOM 2601 C C . ASP B 1 26 ? 67.171 46.478 29.019 1.00 14.14 ? 27 ASP B C 1 ATOM 2602 O O . ASP B 1 26 ? 66.611 46.195 30.065 1.00 15.21 ? 27 ASP B O 1 ATOM 2603 C CB . ASP B 1 26 ? 69.070 48.012 29.340 1.00 21.72 ? 27 ASP B CB 1 ATOM 2604 C CG . ASP B 1 26 ? 70.600 48.230 29.388 1.00 28.19 ? 27 ASP B CG 1 ATOM 2605 O OD1 . ASP B 1 26 ? 71.373 47.248 29.590 1.00 32.47 ? 27 ASP B OD1 1 ATOM 2606 O OD2 . ASP B 1 26 ? 71.014 49.406 29.221 1.00 30.07 ? 27 ASP B OD2 1 ATOM 2607 N N . VAL B 1 27 ? 66.508 46.840 27.925 1.00 14.14 ? 28 VAL B N 1 ATOM 2608 C CA . VAL B 1 27 ? 65.046 46.731 27.893 1.00 15.87 ? 28 VAL B CA 1 ATOM 2609 C C . VAL B 1 27 ? 64.655 45.245 28.055 1.00 15.11 ? 28 VAL B C 1 ATOM 2610 O O . VAL B 1 27 ? 63.756 44.913 28.834 1.00 17.08 ? 28 VAL B O 1 ATOM 2611 C CB . VAL B 1 27 ? 64.437 47.296 26.578 1.00 14.30 ? 28 VAL B CB 1 ATOM 2612 C CG1 . VAL B 1 27 ? 62.889 47.197 26.611 1.00 12.70 ? 28 VAL B CG1 1 ATOM 2613 C CG2 . VAL B 1 27 ? 64.866 48.758 26.397 1.00 13.85 ? 28 VAL B CG2 1 ATOM 2614 N N . LEU B 1 28 ? 65.357 44.354 27.367 1.00 15.63 ? 29 LEU B N 1 ATOM 2615 C CA . LEU B 1 28 ? 65.054 42.925 27.443 1.00 17.27 ? 29 LEU B CA 1 ATOM 2616 C C . LEU B 1 28 ? 65.071 42.374 28.870 1.00 19.04 ? 29 LEU B C 1 ATOM 2617 O O . LEU B 1 28 ? 64.111 41.755 29.344 1.00 17.65 ? 29 LEU B O 1 ATOM 2618 C CB . LEU B 1 28 ? 66.035 42.150 26.569 1.00 17.30 ? 29 LEU B CB 1 ATOM 2619 C CG . LEU B 1 28 ? 65.964 40.621 26.646 1.00 20.39 ? 29 LEU B CG 1 ATOM 2620 C CD1 . LEU B 1 28 ? 64.776 40.094 25.886 1.00 18.59 ? 29 LEU B CD1 1 ATOM 2621 C CD2 . LEU B 1 28 ? 67.243 40.057 26.035 1.00 22.47 ? 29 LEU B CD2 1 ATOM 2622 N N . ASP B 1 29 ? 66.148 42.658 29.583 1.00 20.51 ? 30 ASP B N 1 ATOM 2623 C CA . ASP B 1 29 ? 66.291 42.180 30.940 1.00 22.77 ? 30 ASP B CA 1 ATOM 2624 C C . ASP B 1 29 ? 65.204 42.698 31.855 1.00 22.42 ? 30 ASP B C 1 ATOM 2625 O O . ASP B 1 29 ? 64.770 41.998 32.774 1.00 24.00 ? 30 ASP B O 1 ATOM 2626 C CB . ASP B 1 29 ? 67.669 42.546 31.492 1.00 29.72 ? 30 ASP B CB 1 ATOM 2627 C CG . ASP B 1 29 ? 67.888 42.014 32.903 1.00 37.88 ? 30 ASP B CG 1 ATOM 2628 O OD1 . ASP B 1 29 ? 67.707 42.787 33.878 1.00 43.35 ? 30 ASP B OD1 1 ATOM 2629 O OD2 . ASP B 1 29 ? 68.237 40.816 33.040 1.00 41.78 ? 30 ASP B OD2 1 ATOM 2630 N N . ASP B 1 30 ? 64.819 43.951 31.657 1.00 19.95 ? 31 ASP B N 1 ATOM 2631 C CA . ASP B 1 30 ? 63.769 44.549 32.460 1.00 18.26 ? 31 ASP B CA 1 ATOM 2632 C C . ASP B 1 30 ? 62.433 43.834 32.190 1.00 15.94 ? 31 ASP B C 1 ATOM 2633 O O . ASP B 1 30 ? 61.783 43.357 33.110 1.00 16.71 ? 31 ASP B O 1 ATOM 2634 C CB . ASP B 1 30 ? 63.650 46.025 32.088 1.00 19.36 ? 31 ASP B CB 1 ATOM 2635 C CG . ASP B 1 30 ? 62.654 46.776 32.956 1.00 23.91 ? 31 ASP B CG 1 ATOM 2636 O OD1 . ASP B 1 30 ? 61.820 46.159 33.658 1.00 23.57 ? 31 ASP B OD1 1 ATOM 2637 O OD2 . ASP B 1 30 ? 62.722 48.020 32.934 1.00 26.50 ? 31 ASP B OD2 1 ATOM 2638 N N . LEU B 1 31 ? 62.047 43.781 30.920 1.00 15.92 ? 32 LEU B N 1 ATOM 2639 C CA . LEU B 1 31 ? 60.800 43.152 30.493 1.00 16.00 ? 32 LEU B CA 1 ATOM 2640 C C . LEU B 1 31 ? 60.735 41.736 31.002 1.00 16.38 ? 32 LEU B C 1 ATOM 2641 O O . LEU B 1 31 ? 59.764 41.349 31.627 1.00 16.78 ? 32 LEU B O 1 ATOM 2642 C CB . LEU B 1 31 ? 60.673 43.151 28.965 1.00 13.24 ? 32 LEU B CB 1 ATOM 2643 C CG . LEU B 1 31 ? 60.344 44.487 28.282 1.00 16.06 ? 32 LEU B CG 1 ATOM 2644 C CD1 . LEU B 1 31 ? 60.196 44.315 26.749 1.00 12.96 ? 32 LEU B CD1 1 ATOM 2645 C CD2 . LEU B 1 31 ? 59.048 45.027 28.869 1.00 17.50 ? 32 LEU B CD2 1 ATOM 2646 N N . GLN B 1 32 ? 61.788 40.967 30.758 1.00 16.75 ? 33 GLN B N 1 ATOM 2647 C CA . GLN B 1 32 ? 61.831 39.575 31.194 1.00 17.03 ? 33 GLN B CA 1 ATOM 2648 C C . GLN B 1 32 ? 61.720 39.372 32.689 1.00 17.87 ? 33 GLN B C 1 ATOM 2649 O O . GLN B 1 32 ? 61.010 38.471 33.142 1.00 21.02 ? 33 GLN B O 1 ATOM 2650 C CB . GLN B 1 32 ? 63.078 38.858 30.641 1.00 16.38 ? 33 GLN B CB 1 ATOM 2651 C CG . GLN B 1 32 ? 63.062 38.621 29.130 1.00 16.27 ? 33 GLN B CG 1 ATOM 2652 C CD . GLN B 1 32 ? 61.989 37.622 28.669 1.00 15.34 ? 33 GLN B CD 1 ATOM 2653 O OE1 . GLN B 1 32 ? 62.259 36.739 27.863 1.00 17.84 ? 33 GLN B OE1 1 ATOM 2654 N NE2 . GLN B 1 32 ? 60.777 37.808 29.117 1.00 12.64 ? 33 GLN B NE2 1 ATOM 2655 N N . THR B 1 33 ? 62.347 40.253 33.456 1.00 19.93 ? 34 THR B N 1 ATOM 2656 C CA . THR B 1 33 ? 62.331 40.134 34.897 1.00 19.58 ? 34 THR B CA 1 ATOM 2657 C C . THR B 1 33 ? 61.063 40.668 35.551 1.00 19.67 ? 34 THR B C 1 ATOM 2658 O O . THR B 1 33 ? 60.529 40.049 36.458 1.00 19.80 ? 34 THR B O 1 ATOM 2659 C CB . THR B 1 33 ? 63.577 40.835 35.517 1.00 21.11 ? 34 THR B CB 1 ATOM 2660 O OG1 . THR B 1 33 ? 64.782 40.242 34.994 1.00 22.29 ? 34 THR B OG1 1 ATOM 2661 C CG2 . THR B 1 33 ? 63.570 40.680 37.004 1.00 21.08 ? 34 THR B CG2 1 ATOM 2662 N N . ASN B 1 34 ? 60.547 41.780 35.042 1.00 18.73 ? 35 ASN B N 1 ATOM 2663 C CA . ASN B 1 34 ? 59.375 42.421 35.629 1.00 19.26 ? 35 ASN B CA 1 ATOM 2664 C C . ASN B 1 34 ? 58.043 42.262 34.901 1.00 19.63 ? 35 ASN B C 1 ATOM 2665 O O . ASN B 1 34 ? 57.115 41.668 35.433 1.00 20.65 ? 35 ASN B O 1 ATOM 2666 C CB . ASN B 1 34 ? 59.696 43.898 35.867 1.00 20.55 ? 35 ASN B CB 1 ATOM 2667 C CG . ASN B 1 34 ? 61.011 44.072 36.643 1.00 23.61 ? 35 ASN B CG 1 ATOM 2668 O OD1 . ASN B 1 34 ? 61.096 43.668 37.797 1.00 24.62 ? 35 ASN B OD1 1 ATOM 2669 N ND2 . ASN B 1 34 ? 62.055 44.568 35.980 1.00 21.72 ? 35 ASN B ND2 1 ATOM 2670 N N . PHE B 1 35 ? 57.934 42.785 33.695 1.00 18.72 ? 36 PHE B N 1 ATOM 2671 C CA . PHE B 1 35 ? 56.684 42.672 32.970 1.00 18.84 ? 36 PHE B CA 1 ATOM 2672 C C . PHE B 1 35 ? 56.278 41.200 32.769 1.00 20.08 ? 36 PHE B C 1 ATOM 2673 O O . PHE B 1 35 ? 55.133 40.828 33.048 1.00 18.30 ? 36 PHE B O 1 ATOM 2674 C CB . PHE B 1 35 ? 56.805 43.401 31.629 1.00 19.96 ? 36 PHE B CB 1 ATOM 2675 C CG . PHE B 1 35 ? 55.509 43.504 30.850 1.00 18.64 ? 36 PHE B CG 1 ATOM 2676 C CD1 . PHE B 1 35 ? 54.414 44.194 31.361 1.00 20.00 ? 36 PHE B CD1 1 ATOM 2677 C CD2 . PHE B 1 35 ? 55.406 42.935 29.592 1.00 17.36 ? 36 PHE B CD2 1 ATOM 2678 C CE1 . PHE B 1 35 ? 53.247 44.304 30.620 1.00 19.12 ? 36 PHE B CE1 1 ATOM 2679 C CE2 . PHE B 1 35 ? 54.236 43.043 28.842 1.00 19.19 ? 36 PHE B CE2 1 ATOM 2680 C CZ . PHE B 1 35 ? 53.165 43.722 29.355 1.00 18.22 ? 36 PHE B CZ 1 ATOM 2681 N N . TYR B 1 36 ? 57.223 40.353 32.351 1.00 19.30 ? 37 TYR B N 1 ATOM 2682 C CA . TYR B 1 36 ? 56.927 38.947 32.086 1.00 17.69 ? 37 TYR B CA 1 ATOM 2683 C C . TYR B 1 36 ? 57.165 38.066 33.274 1.00 19.01 ? 37 TYR B C 1 ATOM 2684 O O . TYR B 1 36 ? 57.175 36.844 33.157 1.00 20.93 ? 37 TYR B O 1 ATOM 2685 C CB . TYR B 1 36 ? 57.669 38.441 30.846 1.00 15.33 ? 37 TYR B CB 1 ATOM 2686 C CG . TYR B 1 36 ? 57.169 39.075 29.558 1.00 12.20 ? 37 TYR B CG 1 ATOM 2687 C CD1 . TYR B 1 36 ? 58.053 39.674 28.654 1.00 11.52 ? 37 TYR B CD1 1 ATOM 2688 C CD2 . TYR B 1 36 ? 55.804 39.102 29.259 1.00 11.52 ? 37 TYR B CD2 1 ATOM 2689 C CE1 . TYR B 1 36 ? 57.583 40.303 27.480 1.00 12.36 ? 37 TYR B CE1 1 ATOM 2690 C CE2 . TYR B 1 36 ? 55.329 39.715 28.099 1.00 11.30 ? 37 TYR B CE2 1 ATOM 2691 C CZ . TYR B 1 36 ? 56.211 40.314 27.216 1.00 12.47 ? 37 TYR B CZ 1 ATOM 2692 O OH . TYR B 1 36 ? 55.721 40.951 26.102 1.00 13.09 ? 37 TYR B OH 1 ATOM 2693 N N . GLN B 1 37 ? 57.414 38.713 34.403 1.00 19.41 ? 38 GLN B N 1 ATOM 2694 C CA . GLN B 1 37 ? 57.590 38.049 35.679 1.00 20.99 ? 38 GLN B CA 1 ATOM 2695 C C . GLN B 1 37 ? 58.518 36.848 35.644 1.00 19.84 ? 38 GLN B C 1 ATOM 2696 O O . GLN B 1 37 ? 58.188 35.788 36.165 1.00 19.05 ? 38 GLN B O 1 ATOM 2697 C CB . GLN B 1 37 ? 56.206 37.615 36.190 1.00 25.65 ? 38 GLN B CB 1 ATOM 2698 C CG . GLN B 1 37 ? 55.179 38.753 36.247 1.00 32.55 ? 38 GLN B CG 1 ATOM 2699 C CD . GLN B 1 37 ? 53.769 38.273 36.554 1.00 38.37 ? 38 GLN B CD 1 ATOM 2700 O OE1 . GLN B 1 37 ? 53.579 37.254 37.218 1.00 42.19 ? 38 GLN B OE1 1 ATOM 2701 N NE2 . GLN B 1 37 ? 52.769 39.009 36.075 1.00 43.00 ? 38 GLN B NE2 1 ATOM 2702 N N . GLY B 1 38 ? 59.678 36.990 35.038 1.00 18.76 ? 39 GLY B N 1 ATOM 2703 C CA . GLY B 1 38 ? 60.556 35.837 34.989 1.00 17.40 ? 39 GLY B CA 1 ATOM 2704 C C . GLY B 1 38 ? 60.447 35.079 33.680 1.00 17.62 ? 39 GLY B C 1 ATOM 2705 O O . GLY B 1 38 ? 60.477 33.855 33.657 1.00 17.29 ? 39 GLY B O 1 ATOM 2706 N N . SER B 1 39 ? 60.288 35.801 32.581 1.00 16.57 ? 40 SER B N 1 ATOM 2707 C CA . SER B 1 39 ? 60.236 35.183 31.276 1.00 16.66 ? 40 SER B CA 1 ATOM 2708 C C . SER B 1 39 ? 59.084 34.215 31.112 1.00 16.82 ? 40 SER B C 1 ATOM 2709 O O . SER B 1 39 ? 59.249 33.165 30.518 1.00 17.92 ? 40 SER B O 1 ATOM 2710 C CB . SER B 1 39 ? 61.550 34.436 31.000 1.00 18.45 ? 40 SER B CB 1 ATOM 2711 O OG . SER B 1 39 ? 62.681 35.304 31.022 1.00 18.90 ? 40 SER B OG 1 ATOM 2712 N N . LYS B 1 40 ? 57.912 34.556 31.620 1.00 17.06 ? 41 LYS B N 1 ATOM 2713 C CA . LYS B 1 40 ? 56.785 33.656 31.486 1.00 16.14 ? 41 LYS B CA 1 ATOM 2714 C C . LYS B 1 40 ? 55.933 33.933 30.248 1.00 15.26 ? 41 LYS B C 1 ATOM 2715 O O . LYS B 1 40 ? 56.026 34.994 29.643 1.00 14.43 ? 41 LYS B O 1 ATOM 2716 C CB . LYS B 1 40 ? 55.921 33.758 32.719 1.00 16.40 ? 41 LYS B CB 1 ATOM 2717 C CG . LYS B 1 40 ? 56.694 33.708 33.957 1.00 21.67 ? 41 LYS B CG 1 ATOM 2718 C CD . LYS B 1 40 ? 56.740 32.334 34.466 1.00 27.53 ? 41 LYS B CD 1 ATOM 2719 C CE . LYS B 1 40 ? 56.454 32.387 35.951 1.00 33.84 ? 41 LYS B CE 1 ATOM 2720 N NZ . LYS B 1 40 ? 55.176 33.125 36.249 1.00 37.15 ? 41 LYS B NZ 1 ATOM 2721 N N . CYS B 1 41 ? 55.100 32.954 29.898 1.00 15.43 ? 42 CYS B N 1 ATOM 2722 C CA . CYS B 1 41 ? 54.166 33.035 28.777 1.00 15.09 ? 42 CYS B CA 1 ATOM 2723 C C . CYS B 1 41 ? 52.734 33.020 29.352 1.00 15.87 ? 42 CYS B C 1 ATOM 2724 O O . CYS B 1 41 ? 52.002 32.039 29.218 1.00 16.68 ? 42 CYS B O 1 ATOM 2725 C CB . CYS B 1 41 ? 54.358 31.851 27.834 1.00 12.83 ? 42 CYS B CB 1 ATOM 2726 S SG . CYS B 1 41 ? 53.186 31.880 26.450 1.00 15.59 ? 42 CYS B SG 1 ATOM 2727 N N . GLU B 1 42 ? 52.389 34.062 30.098 1.00 14.89 ? 43 GLU B N 1 ATOM 2728 C CA . GLU B 1 42 ? 51.060 34.162 30.692 1.00 14.77 ? 43 GLU B CA 1 ATOM 2729 C C . GLU B 1 42 ? 50.265 35.378 30.158 1.00 13.98 ? 43 GLU B C 1 ATOM 2730 O O . GLU B 1 42 ? 50.542 35.866 29.049 1.00 12.45 ? 43 GLU B O 1 ATOM 2731 C CB . GLU B 1 42 ? 51.175 34.176 32.209 1.00 14.97 ? 43 GLU B CB 1 ATOM 2732 C CG . GLU B 1 42 ? 51.820 32.924 32.741 1.00 20.40 ? 43 GLU B CG 1 ATOM 2733 C CD . GLU B 1 42 ? 52.114 32.995 34.223 1.00 23.74 ? 43 GLU B CD 1 ATOM 2734 O OE1 . GLU B 1 42 ? 52.047 34.091 34.805 1.00 27.72 ? 43 GLU B OE1 1 ATOM 2735 O OE2 . GLU B 1 42 ? 52.427 31.954 34.811 1.00 26.64 ? 43 GLU B OE2 1 ATOM 2736 N N . SER B 1 43 ? 49.294 35.876 30.927 1.00 13.65 ? 44 SER B N 1 ATOM 2737 C CA . SER B 1 43 ? 48.464 36.992 30.480 1.00 13.73 ? 44 SER B CA 1 ATOM 2738 C C . SER B 1 43 ? 49.199 38.190 29.857 1.00 13.65 ? 44 SER B C 1 ATOM 2739 O O . SER B 1 43 ? 48.734 38.729 28.840 1.00 11.56 ? 44 SER B O 1 ATOM 2740 C CB . SER B 1 43 ? 47.582 37.486 31.619 1.00 14.43 ? 44 SER B CB 1 ATOM 2741 O OG . SER B 1 43 ? 46.633 38.409 31.120 1.00 20.03 ? 44 SER B OG 1 ATOM 2742 N N . PRO B 1 44 ? 50.357 38.622 30.438 1.00 13.00 ? 45 PRO B N 1 ATOM 2743 C CA . PRO B 1 44 ? 51.052 39.783 29.833 1.00 11.97 ? 45 PRO B CA 1 ATOM 2744 C C . PRO B 1 44 ? 51.453 39.607 28.373 1.00 11.73 ? 45 PRO B C 1 ATOM 2745 O O . PRO B 1 44 ? 51.392 40.559 27.604 1.00 13.39 ? 45 PRO B O 1 ATOM 2746 C CB . PRO B 1 44 ? 52.241 40.013 30.764 1.00 12.53 ? 45 PRO B CB 1 ATOM 2747 C CG . PRO B 1 44 ? 51.649 39.630 32.122 1.00 11.80 ? 45 PRO B CG 1 ATOM 2748 C CD . PRO B 1 44 ? 50.904 38.329 31.777 1.00 9.66 ? 45 PRO B CD 1 ATOM 2749 N N . VAL B 1 45 ? 51.781 38.387 27.967 1.00 12.00 ? 46 VAL B N 1 ATOM 2750 C CA . VAL B 1 45 ? 52.159 38.160 26.580 1.00 11.42 ? 46 VAL B CA 1 ATOM 2751 C C . VAL B 1 45 ? 50.911 38.291 25.731 1.00 12.62 ? 46 VAL B C 1 ATOM 2752 O O . VAL B 1 45 ? 50.922 38.913 24.649 1.00 11.11 ? 46 VAL B O 1 ATOM 2753 C CB . VAL B 1 45 ? 52.759 36.727 26.343 1.00 11.85 ? 46 VAL B CB 1 ATOM 2754 C CG1 . VAL B 1 45 ? 52.977 36.511 24.871 1.00 11.66 ? 46 VAL B CG1 1 ATOM 2755 C CG2 . VAL B 1 45 ? 54.083 36.576 27.061 1.00 12.54 ? 46 VAL B CG2 1 ATOM 2756 N N . ARG B 1 46 ? 49.822 37.721 26.239 1.00 11.63 ? 47 ARG B N 1 ATOM 2757 C CA . ARG B 1 46 ? 48.558 37.773 25.516 1.00 12.57 ? 47 ARG B CA 1 ATOM 2758 C C . ARG B 1 46 ? 48.032 39.220 25.382 1.00 10.47 ? 47 ARG B C 1 ATOM 2759 O O . ARG B 1 46 ? 47.590 39.628 24.318 1.00 10.19 ? 47 ARG B O 1 ATOM 2760 C CB . ARG B 1 46 ? 47.554 36.850 26.206 1.00 10.26 ? 47 ARG B CB 1 ATOM 2761 C CG . ARG B 1 46 ? 48.132 35.441 26.443 1.00 7.62 ? 47 ARG B CG 1 ATOM 2762 C CD . ARG B 1 46 ? 47.039 34.406 26.761 1.00 6.10 ? 47 ARG B CD 1 ATOM 2763 N NE . ARG B 1 46 ? 46.243 34.787 27.927 1.00 9.36 ? 47 ARG B NE 1 ATOM 2764 C CZ . ARG B 1 46 ? 46.444 34.360 29.165 1.00 7.51 ? 47 ARG B CZ 1 ATOM 2765 N NH1 . ARG B 1 46 ? 47.436 33.514 29.429 1.00 9.07 ? 47 ARG B NH1 1 ATOM 2766 N NH2 . ARG B 1 46 ? 45.667 34.803 30.140 1.00 8.02 ? 47 ARG B NH2 1 ATOM 2767 N N . LYS B 1 47 ? 48.134 39.992 26.449 1.00 9.25 ? 48 LYS B N 1 ATOM 2768 C CA . LYS B 1 47 ? 47.696 41.394 26.413 1.00 11.29 ? 48 LYS B CA 1 ATOM 2769 C C . LYS B 1 47 ? 48.550 42.227 25.438 1.00 12.38 ? 48 LYS B C 1 ATOM 2770 O O . LYS B 1 47 ? 48.031 43.073 24.687 1.00 11.97 ? 48 LYS B O 1 ATOM 2771 C CB . LYS B 1 47 ? 47.763 42.016 27.808 1.00 10.36 ? 48 LYS B CB 1 ATOM 2772 C CG . LYS B 1 47 ? 46.829 41.380 28.851 1.00 12.30 ? 48 LYS B CG 1 ATOM 2773 C CD . LYS B 1 47 ? 45.370 41.768 28.610 1.00 11.76 ? 48 LYS B CD 1 ATOM 2774 C CE . LYS B 1 47 ? 44.507 41.492 29.839 1.00 14.59 ? 48 LYS B CE 1 ATOM 2775 N NZ . LYS B 1 47 ? 43.042 41.644 29.533 1.00 14.63 ? 48 LYS B NZ 1 ATOM 2776 N N . ILE B 1 48 ? 49.858 41.967 25.429 1.00 11.41 ? 49 ILE B N 1 ATOM 2777 C CA . ILE B 1 48 ? 50.766 42.692 24.547 1.00 10.22 ? 49 ILE B CA 1 ATOM 2778 C C . ILE B 1 48 ? 50.463 42.387 23.084 1.00 9.83 ? 49 ILE B C 1 ATOM 2779 O O . ILE B 1 48 ? 50.575 43.275 22.251 1.00 11.73 ? 49 ILE B O 1 ATOM 2780 C CB . ILE B 1 48 ? 52.272 42.433 24.921 1.00 11.31 ? 49 ILE B CB 1 ATOM 2781 C CG1 . ILE B 1 48 ? 52.995 43.774 25.174 1.00 9.68 ? 49 ILE B CG1 1 ATOM 2782 C CG2 . ILE B 1 48 ? 52.992 41.694 23.813 1.00 7.64 ? 49 ILE B CG2 1 ATOM 2783 C CD1 . ILE B 1 48 ? 53.184 44.605 23.903 1.00 10.13 ? 49 ILE B CD1 1 ATOM 2784 N N . LEU B 1 49 ? 50.081 41.138 22.771 1.00 10.12 ? 50 LEU B N 1 ATOM 2785 C CA . LEU B 1 49 ? 49.739 40.772 21.397 1.00 8.48 ? 50 LEU B CA 1 ATOM 2786 C C . LEU B 1 49 ? 48.463 41.519 20.936 1.00 8.14 ? 50 LEU B C 1 ATOM 2787 O O . LEU B 1 49 ? 48.366 41.878 19.762 1.00 7.20 ? 50 LEU B O 1 ATOM 2788 C CB . LEU B 1 49 ? 49.577 39.255 21.261 1.00 10.88 ? 50 LEU B CB 1 ATOM 2789 C CG . LEU B 1 49 ? 50.835 38.429 20.993 1.00 11.09 ? 50 LEU B CG 1 ATOM 2790 C CD1 . LEU B 1 49 ? 50.536 36.982 21.147 1.00 12.16 ? 50 LEU B CD1 1 ATOM 2791 C CD2 . LEU B 1 49 ? 51.293 38.689 19.565 1.00 14.91 ? 50 LEU B CD2 1 ATOM 2792 N N . ARG B 1 50 ? 47.480 41.698 21.826 1.00 8.20 ? 51 ARG B N 1 ATOM 2793 C CA . ARG B 1 50 ? 46.256 42.467 21.504 1.00 9.97 ? 51 ARG B CA 1 ATOM 2794 C C . ARG B 1 50 ? 46.714 43.906 21.263 1.00 9.21 ? 51 ARG B C 1 ATOM 2795 O O . ARG B 1 50 ? 46.319 44.539 20.322 1.00 9.99 ? 51 ARG B O 1 ATOM 2796 C CB . ARG B 1 50 ? 45.286 42.476 22.696 1.00 8.68 ? 51 ARG B CB 1 ATOM 2797 C CG . ARG B 1 50 ? 44.201 41.424 22.629 1.00 14.00 ? 51 ARG B CG 1 ATOM 2798 C CD . ARG B 1 50 ? 43.165 41.587 23.760 1.00 13.68 ? 51 ARG B CD 1 ATOM 2799 N NE . ARG B 1 50 ? 42.220 42.680 23.543 1.00 11.09 ? 51 ARG B NE 1 ATOM 2800 C CZ . ARG B 1 50 ? 41.603 43.326 24.522 1.00 10.61 ? 51 ARG B CZ 1 ATOM 2801 N NH1 . ARG B 1 50 ? 41.819 42.990 25.766 1.00 9.35 ? 51 ARG B NH1 1 ATOM 2802 N NH2 . ARG B 1 50 ? 40.826 44.365 24.260 1.00 10.71 ? 51 ARG B NH2 1 ATOM 2803 N N . ILE B 1 51 ? 47.579 44.405 22.132 1.00 9.70 ? 52 ILE B N 1 ATOM 2804 C CA . ILE B 1 51 ? 48.085 45.774 21.994 1.00 8.95 ? 52 ILE B CA 1 ATOM 2805 C C . ILE B 1 51 ? 48.833 46.019 20.689 1.00 9.10 ? 52 ILE B C 1 ATOM 2806 O O . ILE B 1 51 ? 48.600 47.046 20.041 1.00 9.54 ? 52 ILE B O 1 ATOM 2807 C CB . ILE B 1 51 ? 48.929 46.181 23.209 1.00 10.53 ? 52 ILE B CB 1 ATOM 2808 C CG1 . ILE B 1 51 ? 48.015 46.415 24.413 1.00 10.03 ? 52 ILE B CG1 1 ATOM 2809 C CG2 . ILE B 1 51 ? 49.701 47.490 22.939 1.00 11.32 ? 52 ILE B CG2 1 ATOM 2810 C CD1 . ILE B 1 51 ? 48.729 46.404 25.736 1.00 9.87 ? 52 ILE B CD1 1 ATOM 2811 N N . VAL B 1 52 ? 49.751 45.133 20.280 1.00 8.05 ? 53 VAL B N 1 ATOM 2812 C CA . VAL B 1 52 ? 50.470 45.383 19.043 1.00 8.02 ? 53 VAL B CA 1 ATOM 2813 C C . VAL B 1 52 ? 49.543 45.453 17.820 1.00 8.78 ? 53 VAL B C 1 ATOM 2814 O O . VAL B 1 52 ? 49.724 46.302 16.928 1.00 8.66 ? 53 VAL B O 1 ATOM 2815 C CB . VAL B 1 52 ? 51.677 44.413 18.829 1.00 9.31 ? 53 VAL B CB 1 ATOM 2816 C CG1 . VAL B 1 52 ? 51.228 42.941 18.722 1.00 8.16 ? 53 VAL B CG1 1 ATOM 2817 C CG2 . VAL B 1 52 ? 52.512 44.870 17.597 1.00 7.30 ? 53 VAL B CG2 1 ATOM 2818 N N . PHE B 1 53 ? 48.497 44.620 17.804 1.00 7.94 ? 54 PHE B N 1 ATOM 2819 C CA . PHE B 1 53 ? 47.536 44.611 16.708 1.00 7.43 ? 54 PHE B CA 1 ATOM 2820 C C . PHE B 1 53 ? 46.698 45.903 16.771 1.00 7.54 ? 54 PHE B C 1 ATOM 2821 O O . PHE B 1 53 ? 46.500 46.536 15.746 1.00 7.46 ? 54 PHE B O 1 ATOM 2822 C CB . PHE B 1 53 ? 46.621 43.356 16.814 1.00 8.33 ? 54 PHE B CB 1 ATOM 2823 C CG . PHE B 1 53 ? 45.466 43.342 15.846 1.00 7.80 ? 54 PHE B CG 1 ATOM 2824 C CD1 . PHE B 1 53 ? 44.192 43.049 16.291 1.00 10.39 ? 54 PHE B CD1 1 ATOM 2825 C CD2 . PHE B 1 53 ? 45.649 43.605 14.492 1.00 8.26 ? 54 PHE B CD2 1 ATOM 2826 C CE1 . PHE B 1 53 ? 43.100 43.014 15.392 1.00 9.28 ? 54 PHE B CE1 1 ATOM 2827 C CE2 . PHE B 1 53 ? 44.584 43.575 13.596 1.00 9.52 ? 54 PHE B CE2 1 ATOM 2828 C CZ . PHE B 1 53 ? 43.313 43.281 14.037 1.00 8.47 ? 54 PHE B CZ 1 ATOM 2829 N N . HIS B 1 54 ? 46.222 46.279 17.961 1.00 7.68 ? 55 HIS B N 1 ATOM 2830 C CA . HIS B 1 54 ? 45.380 47.485 18.081 1.00 10.79 ? 55 HIS B CA 1 ATOM 2831 C C . HIS B 1 54 ? 46.124 48.795 17.844 1.00 11.68 ? 55 HIS B C 1 ATOM 2832 O O . HIS B 1 54 ? 45.548 49.764 17.376 1.00 12.32 ? 55 HIS B O 1 ATOM 2833 C CB . HIS B 1 54 ? 44.580 47.508 19.374 1.00 9.10 ? 55 HIS B CB 1 ATOM 2834 C CG . HIS B 1 54 ? 43.587 46.378 19.477 1.00 12.87 ? 55 HIS B CG 1 ATOM 2835 N ND1 . HIS B 1 54 ? 42.689 46.255 20.512 1.00 11.23 ? 55 HIS B ND1 1 ATOM 2836 C CD2 . HIS B 1 54 ? 43.395 45.304 18.681 1.00 12.13 ? 55 HIS B CD2 1 ATOM 2837 C CE1 . HIS B 1 54 ? 41.979 45.153 20.353 1.00 12.54 ? 55 HIS B CE1 1 ATOM 2838 N NE2 . HIS B 1 54 ? 42.388 44.554 19.248 1.00 14.70 ? 55 HIS B NE2 1 ATOM 2839 N N . ASP B 1 55 ? 47.408 48.832 18.144 1.00 11.53 ? 56 ASP B N 1 ATOM 2840 C CA . ASP B 1 55 ? 48.178 50.024 17.857 1.00 10.83 ? 56 ASP B CA 1 ATOM 2841 C C . ASP B 1 55 ? 48.418 50.152 16.357 1.00 10.80 ? 56 ASP B C 1 ATOM 2842 O O . ASP B 1 55 ? 48.176 51.225 15.772 1.00 10.43 ? 56 ASP B O 1 ATOM 2843 C CB . ASP B 1 55 ? 49.537 49.972 18.540 1.00 12.65 ? 56 ASP B CB 1 ATOM 2844 C CG . ASP B 1 55 ? 50.358 51.240 18.290 1.00 14.30 ? 56 ASP B CG 1 ATOM 2845 O OD1 . ASP B 1 55 ? 51.555 51.119 18.016 1.00 14.72 ? 56 ASP B OD1 1 ATOM 2846 O OD2 . ASP B 1 55 ? 49.801 52.352 18.358 1.00 15.70 ? 56 ASP B OD2 1 ATOM 2847 N N . ALA B 1 56 ? 48.894 49.073 15.739 1.00 10.58 ? 57 ALA B N 1 ATOM 2848 C CA . ALA B 1 56 ? 49.239 49.075 14.327 1.00 11.29 ? 57 ALA B CA 1 ATOM 2849 C C . ALA B 1 56 ? 48.117 49.215 13.314 1.00 12.06 ? 57 ALA B C 1 ATOM 2850 O O . ALA B 1 56 ? 48.281 49.868 12.281 1.00 11.68 ? 57 ALA B O 1 ATOM 2851 C CB . ALA B 1 56 ? 50.068 47.836 13.994 1.00 11.14 ? 57 ALA B CB 1 ATOM 2852 N N . ILE B 1 57 ? 46.979 48.608 13.614 1.00 12.42 ? 58 ILE B N 1 ATOM 2853 C CA . ILE B 1 57 ? 45.841 48.613 12.706 1.00 12.29 ? 58 ILE B CA 1 ATOM 2854 C C . ILE B 1 57 ? 45.162 49.989 12.551 1.00 13.37 ? 58 ILE B C 1 ATOM 2855 O O . ILE B 1 57 ? 44.317 50.185 11.646 1.00 14.46 ? 58 ILE B O 1 ATOM 2856 C CB . ILE B 1 57 ? 44.821 47.505 13.071 1.00 10.96 ? 58 ILE B CB 1 ATOM 2857 C CG1 . ILE B 1 57 ? 44.032 47.156 11.832 1.00 12.71 ? 58 ILE B CG1 1 ATOM 2858 C CG2 . ILE B 1 57 ? 43.925 47.911 14.242 1.00 6.51 ? 58 ILE B CG2 1 ATOM 2859 C CD1 . ILE B 1 57 ? 44.913 46.516 10.779 1.00 14.17 ? 58 ILE B CD1 1 ATOM 2860 N N . GLY B 1 58 ? 45.512 50.919 13.441 1.00 13.30 ? 59 GLY B N 1 ATOM 2861 C CA . GLY B 1 58 ? 44.982 52.273 13.354 1.00 13.56 ? 59 GLY B CA 1 ATOM 2862 C C . GLY B 1 58 ? 45.762 52.984 12.250 1.00 13.15 ? 59 GLY B C 1 ATOM 2863 O O . GLY B 1 58 ? 46.595 53.861 12.519 1.00 13.17 ? 59 GLY B O 1 ATOM 2864 N N . PHE B 1 59 ? 45.488 52.581 11.020 1.00 13.12 ? 60 PHE B N 1 ATOM 2865 C CA . PHE B 1 59 ? 46.151 53.088 9.842 1.00 14.37 ? 60 PHE B CA 1 ATOM 2866 C C . PHE B 1 59 ? 45.176 52.902 8.680 1.00 16.12 ? 60 PHE B C 1 ATOM 2867 O O . PHE B 1 59 ? 44.727 51.782 8.413 1.00 15.81 ? 60 PHE B O 1 ATOM 2868 C CB . PHE B 1 59 ? 47.433 52.278 9.609 1.00 14.06 ? 60 PHE B CB 1 ATOM 2869 C CG . PHE B 1 59 ? 48.187 52.671 8.355 1.00 15.55 ? 60 PHE B CG 1 ATOM 2870 C CD1 . PHE B 1 59 ? 48.979 53.820 8.334 1.00 17.59 ? 60 PHE B CD1 1 ATOM 2871 C CD2 . PHE B 1 59 ? 48.109 51.884 7.213 1.00 14.87 ? 60 PHE B CD2 1 ATOM 2872 C CE1 . PHE B 1 59 ? 49.688 54.181 7.204 1.00 16.55 ? 60 PHE B CE1 1 ATOM 2873 C CE2 . PHE B 1 59 ? 48.805 52.227 6.075 1.00 18.41 ? 60 PHE B CE2 1 ATOM 2874 C CZ . PHE B 1 59 ? 49.606 53.387 6.074 1.00 17.81 ? 60 PHE B CZ 1 ATOM 2875 N N . SER B 1 60 ? 44.867 53.978 7.962 1.00 15.93 ? 61 SER B N 1 ATOM 2876 C CA . SER B 1 60 ? 43.901 53.860 6.889 1.00 16.15 ? 61 SER B CA 1 ATOM 2877 C C . SER B 1 60 ? 44.148 54.680 5.644 1.00 17.90 ? 61 SER B C 1 ATOM 2878 O O . SER B 1 60 ? 43.834 55.878 5.604 1.00 16.22 ? 61 SER B O 1 ATOM 2879 C CB . SER B 1 60 ? 42.503 54.202 7.408 1.00 15.41 ? 61 SER B CB 1 ATOM 2880 O OG . SER B 1 60 ? 41.573 54.115 6.344 1.00 14.72 ? 61 SER B OG 1 ATOM 2881 N N . PRO B 1 61 ? 44.703 54.046 4.608 1.00 20.19 ? 62 PRO B N 1 ATOM 2882 C CA . PRO B 1 61 ? 44.974 54.733 3.344 1.00 23.79 ? 62 PRO B CA 1 ATOM 2883 C C . PRO B 1 61 ? 43.667 55.316 2.769 1.00 24.68 ? 62 PRO B C 1 ATOM 2884 O O . PRO B 1 61 ? 43.662 56.401 2.170 1.00 24.80 ? 62 PRO B O 1 ATOM 2885 C CB . PRO B 1 61 ? 45.550 53.614 2.474 1.00 21.73 ? 62 PRO B CB 1 ATOM 2886 C CG . PRO B 1 61 ? 46.343 52.810 3.483 1.00 21.08 ? 62 PRO B CG 1 ATOM 2887 C CD . PRO B 1 61 ? 45.351 52.718 4.632 1.00 22.04 ? 62 PRO B CD 1 ATOM 2888 N N . ALA B 1 62 ? 42.562 54.610 2.985 1.00 24.66 ? 63 ALA B N 1 ATOM 2889 C CA . ALA B 1 62 ? 41.257 55.083 2.531 1.00 25.02 ? 63 ALA B CA 1 ATOM 2890 C C . ALA B 1 62 ? 40.876 56.468 3.125 1.00 26.15 ? 63 ALA B C 1 ATOM 2891 O O . ALA B 1 62 ? 40.416 57.354 2.387 1.00 28.36 ? 63 ALA B O 1 ATOM 2892 C CB . ALA B 1 62 ? 40.167 54.041 2.846 1.00 22.98 ? 63 ALA B CB 1 ATOM 2893 N N . LEU B 1 63 ? 41.055 56.673 4.430 1.00 25.28 ? 64 LEU B N 1 ATOM 2894 C CA . LEU B 1 63 ? 40.716 57.965 5.027 1.00 27.05 ? 64 LEU B CA 1 ATOM 2895 C C . LEU B 1 63 ? 41.655 59.066 4.522 1.00 30.18 ? 64 LEU B C 1 ATOM 2896 O O . LEU B 1 63 ? 41.243 60.221 4.322 1.00 30.10 ? 64 LEU B O 1 ATOM 2897 C CB . LEU B 1 63 ? 40.802 57.907 6.544 1.00 25.68 ? 64 LEU B CB 1 ATOM 2898 C CG . LEU B 1 63 ? 39.828 57.024 7.310 1.00 27.50 ? 64 LEU B CG 1 ATOM 2899 C CD1 . LEU B 1 63 ? 40.186 57.101 8.782 1.00 26.58 ? 64 LEU B CD1 1 ATOM 2900 C CD2 . LEU B 1 63 ? 38.407 57.490 7.094 1.00 28.58 ? 64 LEU B CD2 1 ATOM 2901 N N . THR B 1 64 ? 42.924 58.701 4.341 1.00 31.47 ? 65 THR B N 1 ATOM 2902 C CA . THR B 1 64 ? 43.941 59.622 3.864 1.00 31.64 ? 65 THR B CA 1 ATOM 2903 C C . THR B 1 64 ? 43.575 60.081 2.460 1.00 34.19 ? 65 THR B C 1 ATOM 2904 O O . THR B 1 64 ? 43.845 61.213 2.086 1.00 36.26 ? 65 THR B O 1 ATOM 2905 C CB . THR B 1 64 ? 45.322 58.949 3.845 1.00 30.78 ? 65 THR B CB 1 ATOM 2906 O OG1 . THR B 1 64 ? 45.666 58.547 5.174 1.00 29.77 ? 65 THR B OG1 1 ATOM 2907 C CG2 . THR B 1 64 ? 46.387 59.904 3.343 1.00 31.66 ? 65 THR B CG2 1 ATOM 2908 N N . ALA B 1 65 ? 42.958 59.196 1.684 1.00 35.05 ? 66 ALA B N 1 ATOM 2909 C CA . ALA B 1 65 ? 42.532 59.515 0.320 1.00 36.18 ? 66 ALA B CA 1 ATOM 2910 C C . ALA B 1 65 ? 41.281 60.380 0.343 1.00 36.60 ? 66 ALA B C 1 ATOM 2911 O O . ALA B 1 65 ? 40.840 60.858 -0.689 1.00 39.53 ? 66 ALA B O 1 ATOM 2912 C CB . ALA B 1 65 ? 42.260 58.229 -0.480 1.00 35.69 ? 66 ALA B CB 1 ATOM 2913 N N . ALA B 1 66 ? 40.670 60.508 1.513 1.00 38.04 ? 67 ALA B N 1 ATOM 2914 C CA . ALA B 1 66 ? 39.484 61.329 1.679 1.00 39.64 ? 67 ALA B CA 1 ATOM 2915 C C . ALA B 1 66 ? 39.924 62.640 2.333 1.00 40.90 ? 67 ALA B C 1 ATOM 2916 O O . ALA B 1 66 ? 39.104 63.419 2.833 1.00 41.10 ? 67 ALA B O 1 ATOM 2917 C CB . ALA B 1 66 ? 38.477 60.613 2.563 1.00 39.40 ? 67 ALA B CB 1 ATOM 2918 N N . GLY B 1 67 ? 41.235 62.848 2.368 1.00 41.30 ? 68 GLY B N 1 ATOM 2919 C CA . GLY B 1 67 ? 41.780 64.043 2.970 1.00 41.13 ? 68 GLY B CA 1 ATOM 2920 C C . GLY B 1 67 ? 41.625 64.095 4.479 1.00 41.68 ? 68 GLY B C 1 ATOM 2921 O O . GLY B 1 67 ? 41.583 65.181 5.064 1.00 43.40 ? 68 GLY B O 1 ATOM 2922 N N . GLN B 1 68 ? 41.503 62.945 5.127 1.00 38.30 ? 69 GLN B N 1 ATOM 2923 C CA . GLN B 1 68 ? 41.390 62.952 6.572 1.00 35.37 ? 69 GLN B CA 1 ATOM 2924 C C . GLN B 1 68 ? 42.615 62.236 7.135 1.00 32.39 ? 69 GLN B C 1 ATOM 2925 O O . GLN B 1 68 ? 43.396 61.665 6.383 1.00 31.47 ? 69 GLN B O 1 ATOM 2926 C CB . GLN B 1 68 ? 40.101 62.269 7.002 1.00 38.76 ? 69 GLN B CB 1 ATOM 2927 C CG . GLN B 1 68 ? 38.839 62.821 6.329 1.00 41.77 ? 69 GLN B CG 1 ATOM 2928 C CD . GLN B 1 68 ? 37.570 62.080 6.768 1.00 44.98 ? 69 GLN B CD 1 ATOM 2929 O OE1 . GLN B 1 68 ? 36.950 61.346 5.985 1.00 44.38 ? 69 GLN B OE1 1 ATOM 2930 N NE2 . GLN B 1 68 ? 37.180 62.273 8.028 1.00 46.17 ? 69 GLN B NE2 1 ATOM 2931 N N . PHE B 1 69 ? 42.844 62.358 8.437 1.00 29.25 ? 70 PHE B N 1 ATOM 2932 C CA . PHE B 1 69 ? 43.975 61.684 9.091 1.00 25.85 ? 70 PHE B CA 1 ATOM 2933 C C . PHE B 1 69 ? 43.578 60.204 9.165 1.00 24.63 ? 70 PHE B C 1 ATOM 2934 O O . PHE B 1 69 ? 42.511 59.890 9.701 1.00 26.04 ? 70 PHE B O 1 ATOM 2935 C CB . PHE B 1 69 ? 44.177 62.227 10.511 1.00 23.11 ? 70 PHE B CB 1 ATOM 2936 C CG . PHE B 1 69 ? 45.272 61.542 11.278 1.00 22.76 ? 70 PHE B CG 1 ATOM 2937 C CD1 . PHE B 1 69 ? 46.574 61.504 10.778 1.00 21.62 ? 70 PHE B CD1 1 ATOM 2938 C CD2 . PHE B 1 69 ? 45.013 60.941 12.502 1.00 20.87 ? 70 PHE B CD2 1 ATOM 2939 C CE1 . PHE B 1 69 ? 47.590 60.875 11.494 1.00 19.44 ? 70 PHE B CE1 1 ATOM 2940 C CE2 . PHE B 1 69 ? 46.025 60.314 13.224 1.00 21.10 ? 70 PHE B CE2 1 ATOM 2941 C CZ . PHE B 1 69 ? 47.308 60.280 12.720 1.00 19.05 ? 70 PHE B CZ 1 ATOM 2942 N N . GLY B 1 70 ? 44.401 59.323 8.588 1.00 24.27 ? 71 GLY B N 1 ATOM 2943 C CA . GLY B 1 70 ? 44.130 57.892 8.596 1.00 20.61 ? 71 GLY B CA 1 ATOM 2944 C C . GLY B 1 70 ? 44.795 57.115 9.718 1.00 19.78 ? 71 GLY B C 1 ATOM 2945 O O . GLY B 1 70 ? 44.668 55.893 9.759 1.00 21.36 ? 71 GLY B O 1 ATOM 2946 N N . GLY B 1 71 ? 45.470 57.796 10.641 1.00 18.30 ? 72 GLY B N 1 ATOM 2947 C CA . GLY B 1 71 ? 46.148 57.109 11.729 1.00 17.33 ? 72 GLY B CA 1 ATOM 2948 C C . GLY B 1 71 ? 47.607 56.890 11.360 1.00 16.10 ? 72 GLY B C 1 ATOM 2949 O O . GLY B 1 71 ? 47.940 56.829 10.181 1.00 17.25 ? 72 GLY B O 1 ATOM 2950 N N . GLY B 1 72 ? 48.484 56.799 12.361 1.00 17.27 ? 73 GLY B N 1 ATOM 2951 C CA . GLY B 1 72 ? 49.921 56.595 12.126 1.00 15.68 ? 73 GLY B CA 1 ATOM 2952 C C . GLY B 1 72 ? 50.482 55.163 12.135 1.00 15.72 ? 73 GLY B C 1 ATOM 2953 O O . GLY B 1 72 ? 51.696 54.975 12.031 1.00 13.51 ? 73 GLY B O 1 ATOM 2954 N N . GLY B 1 73 ? 49.621 54.159 12.285 1.00 14.65 ? 74 GLY B N 1 ATOM 2955 C CA . GLY B 1 73 ? 50.080 52.776 12.274 1.00 13.13 ? 74 GLY B CA 1 ATOM 2956 C C . GLY B 1 73 ? 50.757 52.324 13.552 1.00 13.56 ? 74 GLY B C 1 ATOM 2957 O O . GLY B 1 73 ? 50.272 52.617 14.674 1.00 12.27 ? 74 GLY B O 1 ATOM 2958 N N . ALA B 1 74 ? 51.865 51.599 13.392 1.00 13.73 ? 75 ALA B N 1 ATOM 2959 C CA . ALA B 1 74 ? 52.634 51.070 14.521 1.00 14.26 ? 75 ALA B CA 1 ATOM 2960 C C . ALA B 1 74 ? 53.446 52.159 15.244 1.00 15.60 ? 75 ALA B C 1 ATOM 2961 O O . ALA B 1 74 ? 54.637 51.998 15.496 1.00 16.45 ? 75 ALA B O 1 ATOM 2962 C CB . ALA B 1 74 ? 53.544 49.948 14.026 1.00 12.99 ? 75 ALA B CB 1 ATOM 2963 N N . ASP B 1 75 ? 52.757 53.200 15.694 1.00 15.64 ? 76 ASP B N 1 ATOM 2964 C CA . ASP B 1 75 ? 53.387 54.351 16.346 1.00 13.67 ? 76 ASP B CA 1 ATOM 2965 C C . ASP B 1 75 ? 53.336 54.500 17.847 1.00 12.04 ? 76 ASP B C 1 ATOM 2966 O O . ASP B 1 75 ? 53.747 55.516 18.366 1.00 14.78 ? 76 ASP B O 1 ATOM 2967 C CB . ASP B 1 75 ? 52.842 55.626 15.719 1.00 15.84 ? 76 ASP B CB 1 ATOM 2968 C CG . ASP B 1 75 ? 51.325 55.764 15.882 1.00 19.20 ? 76 ASP B CG 1 ATOM 2969 O OD1 . ASP B 1 75 ? 50.731 56.650 15.235 1.00 18.75 ? 76 ASP B OD1 1 ATOM 2970 O OD2 . ASP B 1 75 ? 50.720 54.993 16.658 1.00 18.95 ? 76 ASP B OD2 1 ATOM 2971 N N . GLY B 1 76 ? 52.768 53.540 18.563 1.00 11.62 ? 77 GLY B N 1 ATOM 2972 C CA . GLY B 1 76 ? 52.703 53.650 20.013 1.00 9.95 ? 77 GLY B CA 1 ATOM 2973 C C . GLY B 1 76 ? 51.635 54.624 20.474 1.00 11.04 ? 77 GLY B C 1 ATOM 2974 O O . GLY B 1 76 ? 51.594 54.996 21.655 1.00 11.16 ? 77 GLY B O 1 ATOM 2975 N N . SER B 1 77 ? 50.773 55.053 19.545 1.00 11.93 ? 78 SER B N 1 ATOM 2976 C CA . SER B 1 77 ? 49.678 55.983 19.874 1.00 12.09 ? 78 SER B CA 1 ATOM 2977 C C . SER B 1 77 ? 48.762 55.432 20.957 1.00 12.97 ? 78 SER B C 1 ATOM 2978 O O . SER B 1 77 ? 48.267 56.184 21.791 1.00 11.49 ? 78 SER B O 1 ATOM 2979 C CB . SER B 1 77 ? 48.850 56.367 18.619 1.00 12.35 ? 78 SER B CB 1 ATOM 2980 O OG . SER B 1 77 ? 48.204 55.266 17.970 1.00 12.18 ? 78 SER B OG 1 ATOM 2981 N N . ILE B 1 78 ? 48.616 54.106 21.017 1.00 13.90 ? 79 ILE B N 1 ATOM 2982 C CA . ILE B 1 78 ? 47.744 53.480 22.018 1.00 12.63 ? 79 ILE B CA 1 ATOM 2983 C C . ILE B 1 78 ? 48.267 53.757 23.439 1.00 13.19 ? 79 ILE B C 1 ATOM 2984 O O . ILE B 1 78 ? 47.523 53.645 24.436 1.00 12.87 ? 79 ILE B O 1 ATOM 2985 C CB . ILE B 1 78 ? 47.578 51.943 21.727 1.00 13.37 ? 79 ILE B CB 1 ATOM 2986 C CG1 . ILE B 1 78 ? 46.477 51.332 22.589 1.00 14.71 ? 79 ILE B CG1 1 ATOM 2987 C CG2 . ILE B 1 78 ? 48.868 51.200 22.006 1.00 10.67 ? 79 ILE B CG2 1 ATOM 2988 C CD1 . ILE B 1 78 ? 46.013 49.937 22.055 1.00 18.07 ? 79 ILE B CD1 1 ATOM 2989 N N . ILE B 1 79 ? 49.558 54.095 23.532 1.00 13.32 ? 80 ILE B N 1 ATOM 2990 C CA . ILE B 1 79 ? 50.170 54.425 24.823 1.00 12.99 ? 80 ILE B CA 1 ATOM 2991 C C . ILE B 1 79 ? 50.256 55.963 24.948 1.00 14.44 ? 80 ILE B C 1 ATOM 2992 O O . ILE B 1 79 ? 49.723 56.533 25.905 1.00 14.27 ? 80 ILE B O 1 ATOM 2993 C CB . ILE B 1 79 ? 51.595 53.836 24.985 1.00 15.07 ? 80 ILE B CB 1 ATOM 2994 C CG1 . ILE B 1 79 ? 51.572 52.317 24.851 1.00 14.35 ? 80 ILE B CG1 1 ATOM 2995 C CG2 . ILE B 1 79 ? 52.160 54.232 26.337 1.00 12.46 ? 80 ILE B CG2 1 ATOM 2996 C CD1 . ILE B 1 79 ? 52.955 51.708 24.924 1.00 17.44 ? 80 ILE B CD1 1 ATOM 2997 N N . ALA B 1 80 ? 50.798 56.622 23.916 1.00 11.98 ? 81 ALA B N 1 ATOM 2998 C CA . ALA B 1 80 ? 50.944 58.079 23.945 1.00 16.03 ? 81 ALA B CA 1 ATOM 2999 C C . ALA B 1 80 ? 49.572 58.731 24.169 1.00 17.08 ? 81 ALA B C 1 ATOM 3000 O O . ALA B 1 80 ? 49.446 59.587 25.033 1.00 17.70 ? 81 ALA B O 1 ATOM 3001 C CB . ALA B 1 80 ? 51.611 58.606 22.663 1.00 11.59 ? 81 ALA B CB 1 ATOM 3002 N N . HIS B 1 81 ? 48.540 58.220 23.491 1.00 17.48 ? 82 HIS B N 1 ATOM 3003 C CA . HIS B 1 81 ? 47.186 58.748 23.607 1.00 16.92 ? 82 HIS B CA 1 ATOM 3004 C C . HIS B 1 81 ? 46.165 57.757 24.142 1.00 17.48 ? 82 HIS B C 1 ATOM 3005 O O . HIS B 1 81 ? 45.007 57.722 23.708 1.00 16.48 ? 82 HIS B O 1 ATOM 3006 C CB . HIS B 1 81 ? 46.750 59.242 22.262 1.00 16.63 ? 82 HIS B CB 1 ATOM 3007 C CG . HIS B 1 81 ? 47.756 60.132 21.627 1.00 20.36 ? 82 HIS B CG 1 ATOM 3008 N ND1 . HIS B 1 81 ? 47.853 61.475 21.935 1.00 19.14 ? 82 HIS B ND1 1 ATOM 3009 C CD2 . HIS B 1 81 ? 48.735 59.877 20.722 1.00 20.64 ? 82 HIS B CD2 1 ATOM 3010 C CE1 . HIS B 1 81 ? 48.845 62.009 21.241 1.00 19.21 ? 82 HIS B CE1 1 ATOM 3011 N NE2 . HIS B 1 81 ? 49.396 61.064 20.501 1.00 22.68 ? 82 HIS B NE2 1 ATOM 3012 N N . SER B 1 82 ? 46.583 56.972 25.119 1.00 18.41 ? 83 SER B N 1 ATOM 3013 C CA . SER B 1 82 ? 45.712 55.971 25.717 1.00 18.46 ? 83 SER B CA 1 ATOM 3014 C C . SER B 1 82 ? 44.415 56.586 26.260 1.00 19.54 ? 83 SER B C 1 ATOM 3015 O O . SER B 1 82 ? 43.384 55.942 26.286 1.00 16.43 ? 83 SER B O 1 ATOM 3016 C CB . SER B 1 82 ? 46.455 55.260 26.839 1.00 18.62 ? 83 SER B CB 1 ATOM 3017 O OG . SER B 1 82 ? 46.989 56.194 27.768 1.00 20.43 ? 83 SER B OG 1 ATOM 3018 N N . ASN B 1 83 ? 44.478 57.842 26.679 1.00 20.24 ? 84 ASN B N 1 ATOM 3019 C CA . ASN B 1 83 ? 43.314 58.528 27.223 1.00 21.96 ? 84 ASN B CA 1 ATOM 3020 C C . ASN B 1 83 ? 42.175 58.507 26.195 1.00 19.43 ? 84 ASN B C 1 ATOM 3021 O O . ASN B 1 83 ? 41.000 58.413 26.556 1.00 19.26 ? 84 ASN B O 1 ATOM 3022 C CB . ASN B 1 83 ? 43.683 59.978 27.587 1.00 25.22 ? 84 ASN B CB 1 ATOM 3023 C CG . ASN B 1 83 ? 44.042 60.820 26.367 1.00 29.89 ? 84 ASN B CG 1 ATOM 3024 O OD1 . ASN B 1 83 ? 44.998 60.526 25.641 1.00 32.00 ? 84 ASN B OD1 1 ATOM 3025 N ND2 . ASN B 1 83 ? 43.248 61.852 26.114 1.00 34.86 ? 84 ASN B ND2 1 ATOM 3026 N N . ILE B 1 84 ? 42.541 58.586 24.922 1.00 17.92 ? 85 ILE B N 1 ATOM 3027 C CA . ILE B 1 84 ? 41.569 58.555 23.842 1.00 17.01 ? 85 ILE B CA 1 ATOM 3028 C C . ILE B 1 84 ? 41.370 57.114 23.387 1.00 18.37 ? 85 ILE B C 1 ATOM 3029 O O . ILE B 1 84 ? 40.239 56.601 23.419 1.00 16.20 ? 85 ILE B O 1 ATOM 3030 C CB . ILE B 1 84 ? 42.065 59.355 22.613 1.00 17.19 ? 85 ILE B CB 1 ATOM 3031 C CG1 . ILE B 1 84 ? 42.187 60.848 22.950 1.00 20.16 ? 85 ILE B CG1 1 ATOM 3032 C CG2 . ILE B 1 84 ? 41.173 59.123 21.406 1.00 14.66 ? 85 ILE B CG2 1 ATOM 3033 C CD1 . ILE B 1 84 ? 40.877 61.533 23.264 1.00 20.27 ? 85 ILE B CD1 1 ATOM 3034 N N . GLU B 1 85 ? 42.475 56.427 23.073 1.00 16.67 ? 86 GLU B N 1 ATOM 3035 C CA . GLU B 1 85 ? 42.372 55.082 22.508 1.00 16.01 ? 86 GLU B CA 1 ATOM 3036 C C . GLU B 1 85 ? 41.834 54.015 23.418 1.00 15.10 ? 86 GLU B C 1 ATOM 3037 O O . GLU B 1 85 ? 41.065 53.148 23.008 1.00 15.95 ? 86 GLU B O 1 ATOM 3038 C CB . GLU B 1 85 ? 43.687 54.660 21.847 1.00 16.68 ? 86 GLU B CB 1 ATOM 3039 C CG . GLU B 1 85 ? 44.129 55.616 20.756 1.00 15.86 ? 86 GLU B CG 1 ATOM 3040 C CD . GLU B 1 85 ? 45.155 55.027 19.800 1.00 17.56 ? 86 GLU B CD 1 ATOM 3041 O OE1 . GLU B 1 85 ? 45.278 53.787 19.711 1.00 18.68 ? 86 GLU B OE1 1 ATOM 3042 O OE2 . GLU B 1 85 ? 45.826 55.807 19.095 1.00 17.06 ? 86 GLU B OE2 1 ATOM 3043 N N . LEU B 1 86 ? 42.139 54.117 24.687 1.00 14.13 ? 87 LEU B N 1 ATOM 3044 C CA . LEU B 1 86 ? 41.640 53.105 25.559 1.00 15.60 ? 87 LEU B CA 1 ATOM 3045 C C . LEU B 1 86 ? 40.146 53.193 25.847 1.00 15.64 ? 87 LEU B C 1 ATOM 3046 O O . LEU B 1 86 ? 39.612 52.352 26.564 1.00 17.73 ? 87 LEU B O 1 ATOM 3047 C CB . LEU B 1 86 ? 42.488 53.009 26.823 1.00 18.15 ? 87 LEU B CB 1 ATOM 3048 C CG . LEU B 1 86 ? 43.529 51.876 26.820 1.00 18.70 ? 87 LEU B CG 1 ATOM 3049 C CD1 . LEU B 1 86 ? 44.228 51.723 25.476 1.00 16.94 ? 87 LEU B CD1 1 ATOM 3050 C CD2 . LEU B 1 86 ? 44.483 52.103 27.970 1.00 18.45 ? 87 LEU B CD2 1 ATOM 3051 N N . ALA B 1 87 ? 39.473 54.207 25.309 1.00 15.89 ? 88 ALA B N 1 ATOM 3052 C CA . ALA B 1 87 ? 38.012 54.330 25.471 1.00 16.11 ? 88 ALA B CA 1 ATOM 3053 C C . ALA B 1 87 ? 37.327 53.695 24.240 1.00 15.73 ? 88 ALA B C 1 ATOM 3054 O O . ALA B 1 87 ? 36.102 53.660 24.154 1.00 17.92 ? 88 ALA B O 1 ATOM 3055 C CB . ALA B 1 87 ? 37.562 55.799 25.665 1.00 14.82 ? 88 ALA B CB 1 ATOM 3056 N N . PHE B 1 88 ? 38.116 53.235 23.268 1.00 14.16 ? 89 PHE B N 1 ATOM 3057 C CA . PHE B 1 88 ? 37.558 52.563 22.102 1.00 14.97 ? 89 PHE B CA 1 ATOM 3058 C C . PHE B 1 88 ? 36.989 51.235 22.627 1.00 16.14 ? 89 PHE B C 1 ATOM 3059 O O . PHE B 1 88 ? 37.612 50.556 23.428 1.00 16.06 ? 89 PHE B O 1 ATOM 3060 C CB . PHE B 1 88 ? 38.634 52.279 21.054 1.00 13.58 ? 89 PHE B CB 1 ATOM 3061 C CG . PHE B 1 88 ? 39.176 53.519 20.356 1.00 15.30 ? 89 PHE B CG 1 ATOM 3062 C CD1 . PHE B 1 88 ? 38.646 54.786 20.608 1.00 14.28 ? 89 PHE B CD1 1 ATOM 3063 C CD2 . PHE B 1 88 ? 40.220 53.411 19.436 1.00 11.90 ? 89 PHE B CD2 1 ATOM 3064 C CE1 . PHE B 1 88 ? 39.159 55.910 19.947 1.00 13.23 ? 89 PHE B CE1 1 ATOM 3065 C CE2 . PHE B 1 88 ? 40.726 54.527 18.782 1.00 12.01 ? 89 PHE B CE2 1 ATOM 3066 C CZ . PHE B 1 88 ? 40.199 55.772 19.035 1.00 12.11 ? 89 PHE B CZ 1 ATOM 3067 N N . PRO B 1 89 ? 35.786 50.850 22.193 1.00 16.35 ? 90 PRO B N 1 ATOM 3068 C CA . PRO B 1 89 ? 35.187 49.597 22.668 1.00 16.77 ? 90 PRO B CA 1 ATOM 3069 C C . PRO B 1 89 ? 36.071 48.357 22.519 1.00 15.44 ? 90 PRO B C 1 ATOM 3070 O O . PRO B 1 89 ? 36.000 47.446 23.334 1.00 13.91 ? 90 PRO B O 1 ATOM 3071 C CB . PRO B 1 89 ? 33.911 49.504 21.828 1.00 19.70 ? 90 PRO B CB 1 ATOM 3072 C CG . PRO B 1 89 ? 33.537 50.972 21.645 1.00 18.37 ? 90 PRO B CG 1 ATOM 3073 C CD . PRO B 1 89 ? 34.877 51.551 21.269 1.00 16.53 ? 90 PRO B CD 1 ATOM 3074 N N . ALA B 1 90 ? 36.920 48.339 21.498 1.00 14.25 ? 91 ALA B N 1 ATOM 3075 C CA . ALA B 1 90 ? 37.824 47.209 21.283 1.00 14.55 ? 91 ALA B CA 1 ATOM 3076 C C . ALA B 1 90 ? 39.086 47.175 22.192 1.00 14.53 ? 91 ALA B C 1 ATOM 3077 O O . ALA B 1 90 ? 39.805 46.163 22.203 1.00 15.24 ? 91 ALA B O 1 ATOM 3078 C CB . ALA B 1 90 ? 38.239 47.154 19.831 1.00 14.08 ? 91 ALA B CB 1 ATOM 3079 N N . ASN B 1 91 ? 39.280 48.196 23.031 1.00 13.54 ? 92 ASN B N 1 ATOM 3080 C CA . ASN B 1 91 ? 40.482 48.293 23.893 1.00 12.75 ? 92 ASN B CA 1 ATOM 3081 C C . ASN B 1 91 ? 40.277 48.154 25.357 1.00 11.89 ? 92 ASN B C 1 ATOM 3082 O O . ASN B 1 91 ? 40.999 48.748 26.146 1.00 11.37 ? 92 ASN B O 1 ATOM 3083 C CB . ASN B 1 91 ? 41.221 49.608 23.652 1.00 13.92 ? 92 ASN B CB 1 ATOM 3084 C CG . ASN B 1 91 ? 41.938 49.597 22.358 1.00 16.48 ? 92 ASN B CG 1 ATOM 3085 O OD1 . ASN B 1 91 ? 42.317 48.531 21.896 1.00 18.40 ? 92 ASN B OD1 1 ATOM 3086 N ND2 . ASN B 1 91 ? 42.069 50.750 21.710 1.00 17.14 ? 92 ASN B ND2 1 ATOM 3087 N N . GLY B 1 92 ? 39.263 47.400 25.745 1.00 12.89 ? 93 GLY B N 1 ATOM 3088 C CA . GLY B 1 92 ? 39.025 47.198 27.165 1.00 14.14 ? 93 GLY B CA 1 ATOM 3089 C C . GLY B 1 92 ? 39.978 46.154 27.726 1.00 12.62 ? 93 GLY B C 1 ATOM 3090 O O . GLY B 1 92 ? 40.484 45.309 26.974 1.00 13.40 ? 93 GLY B O 1 ATOM 3091 N N . GLY B 1 93 ? 40.237 46.243 29.027 1.00 12.12 ? 94 GLY B N 1 ATOM 3092 C CA . GLY B 1 93 ? 41.129 45.314 29.707 1.00 13.38 ? 94 GLY B CA 1 ATOM 3093 C C . GLY B 1 93 ? 42.609 45.480 29.413 1.00 14.86 ? 94 GLY B C 1 ATOM 3094 O O . GLY B 1 93 ? 43.414 44.583 29.675 1.00 15.13 ? 94 GLY B O 1 ATOM 3095 N N . LEU B 1 94 ? 42.988 46.642 28.894 1.00 15.93 ? 95 LEU B N 1 ATOM 3096 C CA . LEU B 1 94 ? 44.376 46.904 28.568 1.00 14.40 ? 95 LEU B CA 1 ATOM 3097 C C . LEU B 1 94 ? 45.035 47.984 29.402 1.00 16.29 ? 95 LEU B C 1 ATOM 3098 O O . LEU B 1 94 ? 46.249 48.124 29.350 1.00 17.07 ? 95 LEU B O 1 ATOM 3099 C CB . LEU B 1 94 ? 44.494 47.284 27.100 1.00 13.34 ? 95 LEU B CB 1 ATOM 3100 C CG . LEU B 1 94 ? 44.008 46.239 26.090 1.00 13.35 ? 95 LEU B CG 1 ATOM 3101 C CD1 . LEU B 1 94 ? 43.960 46.868 24.700 1.00 10.92 ? 95 LEU B CD1 1 ATOM 3102 C CD2 . LEU B 1 94 ? 44.882 44.959 26.143 1.00 12.33 ? 95 LEU B CD2 1 ATOM 3103 N N . THR B 1 95 ? 44.277 48.708 30.218 1.00 15.68 ? 96 THR B N 1 ATOM 3104 C CA . THR B 1 95 ? 44.861 49.822 30.997 1.00 18.22 ? 96 THR B CA 1 ATOM 3105 C C . THR B 1 95 ? 46.145 49.515 31.753 1.00 17.10 ? 96 THR B C 1 ATOM 3106 O O . THR B 1 95 ? 47.142 50.229 31.632 1.00 16.00 ? 96 THR B O 1 ATOM 3107 C CB . THR B 1 95 ? 43.842 50.426 31.993 1.00 20.21 ? 96 THR B CB 1 ATOM 3108 O OG1 . THR B 1 95 ? 42.652 50.795 31.283 1.00 24.20 ? 96 THR B OG1 1 ATOM 3109 C CG2 . THR B 1 95 ? 44.420 51.676 32.649 1.00 22.36 ? 96 THR B CG2 1 ATOM 3110 N N . ASP B 1 96 ? 46.093 48.460 32.549 1.00 16.43 ? 97 ASP B N 1 ATOM 3111 C CA . ASP B 1 96 ? 47.227 48.026 33.343 1.00 20.68 ? 97 ASP B CA 1 ATOM 3112 C C . ASP B 1 96 ? 48.458 47.652 32.533 1.00 17.60 ? 97 ASP B C 1 ATOM 3113 O O . ASP B 1 96 ? 49.582 47.952 32.916 1.00 18.74 ? 97 ASP B O 1 ATOM 3114 C CB . ASP B 1 96 ? 46.809 46.859 34.244 1.00 23.18 ? 97 ASP B CB 1 ATOM 3115 C CG . ASP B 1 96 ? 45.855 47.293 35.338 1.00 28.73 ? 97 ASP B CG 1 ATOM 3116 O OD1 . ASP B 1 96 ? 45.855 48.500 35.695 1.00 31.40 ? 97 ASP B OD1 1 ATOM 3117 O OD2 . ASP B 1 96 ? 45.108 46.433 35.842 1.00 32.15 ? 97 ASP B OD2 1 ATOM 3118 N N . THR B 1 97 ? 48.241 46.939 31.447 1.00 16.03 ? 98 THR B N 1 ATOM 3119 C CA . THR B 1 97 ? 49.333 46.559 30.595 1.00 14.95 ? 98 THR B CA 1 ATOM 3120 C C . THR B 1 97 ? 49.958 47.830 30.011 1.00 16.38 ? 98 THR B C 1 ATOM 3121 O O . THR B 1 97 ? 51.169 47.976 30.021 1.00 18.07 ? 98 THR B O 1 ATOM 3122 C CB . THR B 1 97 ? 48.830 45.625 29.465 1.00 15.44 ? 98 THR B CB 1 ATOM 3123 O OG1 . THR B 1 97 ? 48.161 44.505 30.046 1.00 16.16 ? 98 THR B OG1 1 ATOM 3124 C CG2 . THR B 1 97 ? 49.992 45.145 28.576 1.00 13.84 ? 98 THR B CG2 1 ATOM 3125 N N . VAL B 1 98 ? 49.138 48.732 29.471 1.00 14.53 ? 99 VAL B N 1 ATOM 3126 C CA . VAL B 1 98 ? 49.629 49.989 28.882 1.00 15.56 ? 99 VAL B CA 1 ATOM 3127 C C . VAL B 1 98 ? 50.462 50.850 29.862 1.00 15.55 ? 99 VAL B C 1 ATOM 3128 O O . VAL B 1 98 ? 51.479 51.414 29.472 1.00 14.91 ? 99 VAL B O 1 ATOM 3129 C CB . VAL B 1 98 ? 48.446 50.831 28.275 1.00 16.02 ? 99 VAL B CB 1 ATOM 3130 C CG1 . VAL B 1 98 ? 48.896 52.247 27.914 1.00 13.72 ? 99 VAL B CG1 1 ATOM 3131 C CG2 . VAL B 1 98 ? 47.931 50.140 27.031 1.00 13.43 ? 99 VAL B CG2 1 ATOM 3132 N N . GLU B 1 99 ? 50.051 50.932 31.124 1.00 14.92 ? 100 GLU B N 1 ATOM 3133 C CA . GLU B 1 99 ? 50.799 51.731 32.081 1.00 17.23 ? 100 GLU B CA 1 ATOM 3134 C C . GLU B 1 99 ? 52.127 51.102 32.379 1.00 18.19 ? 100 GLU B C 1 ATOM 3135 O O . GLU B 1 99 ? 53.142 51.790 32.514 1.00 19.52 ? 100 GLU B O 1 ATOM 3136 C CB . GLU B 1 99 ? 50.014 51.928 33.365 1.00 19.86 ? 100 GLU B CB 1 ATOM 3137 C CG . GLU B 1 99 ? 48.797 52.823 33.168 1.00 22.05 ? 100 GLU B CG 1 ATOM 3138 C CD . GLU B 1 99 ? 49.135 54.130 32.465 1.00 22.79 ? 100 GLU B CD 1 ATOM 3139 O OE1 . GLU B 1 99 ? 50.145 54.771 32.820 1.00 24.15 ? 100 GLU B OE1 1 ATOM 3140 O OE2 . GLU B 1 99 ? 48.396 54.508 31.532 1.00 27.58 ? 100 GLU B OE2 1 ATOM 3141 N N . ALA B 1 100 ? 52.128 49.782 32.464 1.00 18.36 ? 101 ALA B N 1 ATOM 3142 C CA . ALA B 1 100 ? 53.354 49.064 32.720 1.00 17.09 ? 101 ALA B CA 1 ATOM 3143 C C . ALA B 1 100 ? 54.330 49.389 31.607 1.00 16.11 ? 101 ALA B C 1 ATOM 3144 O O . ALA B 1 100 ? 55.487 49.709 31.886 1.00 16.63 ? 101 ALA B O 1 ATOM 3145 C CB . ALA B 1 100 ? 53.091 47.572 32.789 1.00 17.81 ? 101 ALA B CB 1 ATOM 3146 N N . LEU B 1 101 ? 53.879 49.326 30.357 1.00 14.34 ? 102 LEU B N 1 ATOM 3147 C CA . LEU B 1 101 ? 54.744 49.606 29.208 1.00 15.70 ? 102 LEU B CA 1 ATOM 3148 C C . LEU B 1 101 ? 55.160 51.066 29.122 1.00 17.34 ? 102 LEU B C 1 ATOM 3149 O O . LEU B 1 101 ? 56.244 51.387 28.642 1.00 17.06 ? 102 LEU B O 1 ATOM 3150 C CB . LEU B 1 101 ? 54.077 49.183 27.901 1.00 15.31 ? 102 LEU B CB 1 ATOM 3151 C CG . LEU B 1 101 ? 53.940 47.665 27.668 1.00 18.26 ? 102 LEU B CG 1 ATOM 3152 C CD1 . LEU B 1 101 ? 53.143 47.398 26.389 1.00 19.06 ? 102 LEU B CD1 1 ATOM 3153 C CD2 . LEU B 1 101 ? 55.307 47.012 27.577 1.00 16.99 ? 102 LEU B CD2 1 ATOM 3154 N N . ARG B 1 102 ? 54.270 51.956 29.527 1.00 16.84 ? 103 ARG B N 1 ATOM 3155 C CA . ARG B 1 102 ? 54.588 53.373 29.521 1.00 18.61 ? 103 ARG B CA 1 ATOM 3156 C C . ARG B 1 102 ? 55.849 53.640 30.359 1.00 18.52 ? 103 ARG B C 1 ATOM 3157 O O . ARG B 1 102 ? 56.778 54.348 29.918 1.00 20.26 ? 103 ARG B O 1 ATOM 3158 C CB . ARG B 1 102 ? 53.423 54.143 30.120 1.00 18.63 ? 103 ARG B CB 1 ATOM 3159 C CG . ARG B 1 102 ? 53.705 55.601 30.390 1.00 20.82 ? 103 ARG B CG 1 ATOM 3160 C CD . ARG B 1 102 ? 52.413 56.288 30.820 1.00 21.51 ? 103 ARG B CD 1 ATOM 3161 N NE . ARG B 1 102 ? 51.879 56.873 29.614 1.00 24.47 ? 103 ARG B NE 1 ATOM 3162 C CZ . ARG B 1 102 ? 50.682 56.664 29.130 1.00 22.05 ? 103 ARG B CZ 1 ATOM 3163 N NH1 . ARG B 1 102 ? 49.822 55.869 29.739 1.00 23.80 ? 103 ARG B NH1 1 ATOM 3164 N NH2 . ARG B 1 102 ? 50.377 57.243 28.003 1.00 26.26 ? 103 ARG B NH2 1 ATOM 3165 N N . ALA B 1 103 ? 55.871 53.056 31.558 1.00 18.89 ? 104 ALA B N 1 ATOM 3166 C CA . ALA B 1 103 ? 56.983 53.204 32.489 1.00 18.09 ? 104 ALA B CA 1 ATOM 3167 C C . ALA B 1 103 ? 58.302 52.701 31.898 1.00 18.63 ? 104 ALA B C 1 ATOM 3168 O O . ALA B 1 103 ? 59.331 53.372 31.981 1.00 21.32 ? 104 ALA B O 1 ATOM 3169 C CB . ALA B 1 103 ? 56.666 52.495 33.784 1.00 16.52 ? 104 ALA B CB 1 ATOM 3170 N N . VAL B 1 104 ? 58.269 51.558 31.238 1.00 15.70 ? 105 VAL B N 1 ATOM 3171 C CA . VAL B 1 104 ? 59.476 51.009 30.647 1.00 14.99 ? 105 VAL B CA 1 ATOM 3172 C C . VAL B 1 104 ? 60.031 51.917 29.538 1.00 15.99 ? 105 VAL B C 1 ATOM 3173 O O . VAL B 1 104 ? 61.244 52.168 29.464 1.00 16.06 ? 105 VAL B O 1 ATOM 3174 C CB . VAL B 1 104 ? 59.202 49.577 30.106 1.00 14.12 ? 105 VAL B CB 1 ATOM 3175 C CG1 . VAL B 1 104 ? 60.402 49.038 29.385 1.00 13.49 ? 105 VAL B CG1 1 ATOM 3176 C CG2 . VAL B 1 104 ? 58.843 48.653 31.246 1.00 11.13 ? 105 VAL B CG2 1 ATOM 3177 N N . GLY B 1 105 ? 59.146 52.416 28.675 1.00 16.06 ? 106 GLY B N 1 ATOM 3178 C CA . GLY B 1 105 ? 59.583 53.276 27.579 1.00 17.63 ? 106 GLY B CA 1 ATOM 3179 C C . GLY B 1 105 ? 60.188 54.594 28.055 1.00 19.56 ? 106 GLY B C 1 ATOM 3180 O O . GLY B 1 105 ? 61.179 55.089 27.499 1.00 19.34 ? 106 GLY B O 1 ATOM 3181 N N . ILE B 1 106 ? 59.556 55.174 29.066 1.00 20.38 ? 107 ILE B N 1 ATOM 3182 C CA . ILE B 1 106 ? 60.023 56.411 29.634 1.00 21.95 ? 107 ILE B CA 1 ATOM 3183 C C . ILE B 1 106 ? 61.356 56.194 30.341 1.00 24.57 ? 107 ILE B C 1 ATOM 3184 O O . ILE B 1 106 ? 62.284 56.962 30.101 1.00 26.34 ? 107 ILE B O 1 ATOM 3185 C CB . ILE B 1 106 ? 58.954 57.030 30.555 1.00 21.14 ? 107 ILE B CB 1 ATOM 3186 C CG1 . ILE B 1 106 ? 57.803 57.540 29.702 1.00 17.77 ? 107 ILE B CG1 1 ATOM 3187 C CG2 . ILE B 1 106 ? 59.504 58.210 31.329 1.00 21.49 ? 107 ILE B CG2 1 ATOM 3188 C CD1 . ILE B 1 106 ? 56.706 58.097 30.519 1.00 20.05 ? 107 ILE B CD1 1 ATOM 3189 N N . ASN B 1 107 ? 61.492 55.121 31.131 1.00 25.90 ? 108 ASN B N 1 ATOM 3190 C CA . ASN B 1 107 ? 62.762 54.836 31.844 1.00 27.63 ? 108 ASN B CA 1 ATOM 3191 C C . ASN B 1 107 ? 63.968 54.532 30.941 1.00 27.02 ? 108 ASN B C 1 ATOM 3192 O O . ASN B 1 107 ? 65.099 54.830 31.302 1.00 28.07 ? 108 ASN B O 1 ATOM 3193 C CB . ASN B 1 107 ? 62.642 53.667 32.841 1.00 31.87 ? 108 ASN B CB 1 ATOM 3194 C CG . ASN B 1 107 ? 61.514 53.846 33.855 1.00 37.94 ? 108 ASN B CG 1 ATOM 3195 O OD1 . ASN B 1 107 ? 60.844 52.871 34.231 1.00 41.18 ? 108 ASN B OD1 1 ATOM 3196 N ND2 . ASN B 1 107 ? 61.305 55.077 34.319 1.00 40.62 ? 108 ASN B ND2 1 ATOM 3197 N N . HIS B 1 108 ? 63.754 53.881 29.804 1.00 24.38 ? 109 HIS B N 1 ATOM 3198 C CA . HIS B 1 108 ? 64.870 53.551 28.932 1.00 21.30 ? 109 HIS B CA 1 ATOM 3199 C C . HIS B 1 108 ? 64.985 54.512 27.799 1.00 20.49 ? 109 HIS B C 1 ATOM 3200 O O . HIS B 1 108 ? 65.862 54.391 26.952 1.00 21.38 ? 109 HIS B O 1 ATOM 3201 C CB . HIS B 1 108 ? 64.725 52.133 28.398 1.00 21.52 ? 109 HIS B CB 1 ATOM 3202 C CG . HIS B 1 108 ? 64.824 51.093 29.464 1.00 22.54 ? 109 HIS B CG 1 ATOM 3203 N ND1 . HIS B 1 108 ? 66.031 50.660 29.963 1.00 21.95 ? 109 HIS B ND1 1 ATOM 3204 C CD2 . HIS B 1 108 ? 63.872 50.435 30.162 1.00 23.59 ? 109 HIS B CD2 1 ATOM 3205 C CE1 . HIS B 1 108 ? 65.821 49.782 30.926 1.00 23.30 ? 109 HIS B CE1 1 ATOM 3206 N NE2 . HIS B 1 108 ? 64.519 49.626 31.066 1.00 24.52 ? 109 HIS B NE2 1 ATOM 3207 N N . GLY B 1 109 ? 64.067 55.462 27.755 1.00 20.71 ? 110 GLY B N 1 ATOM 3208 C CA . GLY B 1 109 ? 64.103 56.429 26.691 1.00 19.46 ? 110 GLY B CA 1 ATOM 3209 C C . GLY B 1 109 ? 63.995 55.859 25.299 1.00 19.39 ? 110 GLY B C 1 ATOM 3210 O O . GLY B 1 109 ? 64.746 56.282 24.417 1.00 21.82 ? 110 GLY B O 1 ATOM 3211 N N . VAL B 1 110 ? 63.065 54.924 25.087 1.00 18.66 ? 111 VAL B N 1 ATOM 3212 C CA . VAL B 1 110 ? 62.831 54.320 23.759 1.00 15.36 ? 111 VAL B CA 1 ATOM 3213 C C . VAL B 1 110 ? 61.448 54.771 23.239 1.00 13.28 ? 111 VAL B C 1 ATOM 3214 O O . VAL B 1 110 ? 60.580 55.106 24.038 1.00 13.72 ? 111 VAL B O 1 ATOM 3215 C CB . VAL B 1 110 ? 62.910 52.767 23.818 1.00 15.93 ? 111 VAL B CB 1 ATOM 3216 C CG1 . VAL B 1 110 ? 64.385 52.332 24.090 1.00 14.10 ? 111 VAL B CG1 1 ATOM 3217 C CG2 . VAL B 1 110 ? 61.956 52.217 24.928 1.00 11.35 ? 111 VAL B CG2 1 ATOM 3218 N N . SER B 1 111 ? 61.237 54.817 21.930 1.00 11.72 ? 112 SER B N 1 ATOM 3219 C CA . SER B 1 111 ? 59.921 55.257 21.463 1.00 15.72 ? 112 SER B CA 1 ATOM 3220 C C . SER B 1 111 ? 58.853 54.228 21.858 1.00 16.82 ? 112 SER B C 1 ATOM 3221 O O . SER B 1 111 ? 59.164 53.036 22.007 1.00 16.68 ? 112 SER B O 1 ATOM 3222 C CB . SER B 1 111 ? 59.895 55.525 19.954 1.00 12.97 ? 112 SER B CB 1 ATOM 3223 O OG . SER B 1 111 ? 60.094 54.366 19.176 1.00 16.87 ? 112 SER B OG 1 ATOM 3224 N N . PHE B 1 112 ? 57.614 54.691 22.044 1.00 15.36 ? 113 PHE B N 1 ATOM 3225 C CA . PHE B 1 112 ? 56.499 53.830 22.448 1.00 15.12 ? 113 PHE B CA 1 ATOM 3226 C C . PHE B 1 112 ? 56.208 52.801 21.351 1.00 13.42 ? 113 PHE B C 1 ATOM 3227 O O . PHE B 1 112 ? 55.851 51.671 21.639 1.00 15.06 ? 113 PHE B O 1 ATOM 3228 C CB . PHE B 1 112 ? 55.228 54.660 22.739 1.00 14.13 ? 113 PHE B CB 1 ATOM 3229 C CG . PHE B 1 112 ? 55.248 55.430 24.049 1.00 14.25 ? 113 PHE B CG 1 ATOM 3230 C CD1 . PHE B 1 112 ? 56.015 55.021 25.130 1.00 15.15 ? 113 PHE B CD1 1 ATOM 3231 C CD2 . PHE B 1 112 ? 54.428 56.571 24.208 1.00 16.86 ? 113 PHE B CD2 1 ATOM 3232 C CE1 . PHE B 1 112 ? 55.978 55.727 26.357 1.00 13.80 ? 113 PHE B CE1 1 ATOM 3233 C CE2 . PHE B 1 112 ? 54.385 57.279 25.432 1.00 15.66 ? 113 PHE B CE2 1 ATOM 3234 C CZ . PHE B 1 112 ? 55.172 56.843 26.505 1.00 14.47 ? 113 PHE B CZ 1 ATOM 3235 N N . GLY B 1 113 ? 56.367 53.203 20.102 1.00 12.06 ? 114 GLY B N 1 ATOM 3236 C CA . GLY B 1 113 ? 56.146 52.306 18.980 1.00 13.32 ? 114 GLY B CA 1 ATOM 3237 C C . GLY B 1 113 ? 57.164 51.164 18.881 1.00 16.62 ? 114 GLY B C 1 ATOM 3238 O O . GLY B 1 113 ? 56.792 50.008 18.619 1.00 13.49 ? 114 GLY B O 1 ATOM 3239 N N . ASP B 1 114 ? 58.449 51.479 19.021 1.00 13.51 ? 115 ASP B N 1 ATOM 3240 C CA . ASP B 1 114 ? 59.503 50.458 18.986 1.00 13.75 ? 115 ASP B CA 1 ATOM 3241 C C . ASP B 1 114 ? 59.284 49.493 20.148 1.00 12.00 ? 115 ASP B C 1 ATOM 3242 O O . ASP B 1 114 ? 59.446 48.298 19.998 1.00 13.06 ? 115 ASP B O 1 ATOM 3243 C CB . ASP B 1 114 ? 60.876 51.107 19.213 1.00 12.85 ? 115 ASP B CB 1 ATOM 3244 C CG . ASP B 1 114 ? 61.460 51.718 17.975 1.00 16.03 ? 115 ASP B CG 1 ATOM 3245 O OD1 . ASP B 1 114 ? 60.831 51.712 16.893 1.00 16.87 ? 115 ASP B OD1 1 ATOM 3246 O OD2 . ASP B 1 114 ? 62.606 52.194 18.087 1.00 19.86 ? 115 ASP B OD2 1 ATOM 3247 N N . LEU B 1 115 ? 59.038 50.060 21.327 1.00 10.66 ? 116 LEU B N 1 ATOM 3248 C CA . LEU B 1 115 ? 58.811 49.293 22.551 1.00 11.84 ? 116 LEU B CA 1 ATOM 3249 C C . LEU B 1 115 ? 57.718 48.245 22.417 1.00 13.26 ? 116 LEU B C 1 ATOM 3250 O O . LEU B 1 115 ? 57.866 47.136 22.929 1.00 11.35 ? 116 LEU B O 1 ATOM 3251 C CB . LEU B 1 115 ? 58.459 50.212 23.706 1.00 10.08 ? 116 LEU B CB 1 ATOM 3252 C CG . LEU B 1 115 ? 58.145 49.460 24.995 1.00 11.89 ? 116 LEU B CG 1 ATOM 3253 C CD1 . LEU B 1 115 ? 59.360 48.585 25.426 1.00 11.97 ? 116 LEU B CD1 1 ATOM 3254 C CD2 . LEU B 1 115 ? 57.769 50.477 26.058 1.00 10.95 ? 116 LEU B CD2 1 ATOM 3255 N N . ILE B 1 116 ? 56.607 48.608 21.778 1.00 12.90 ? 117 ILE B N 1 ATOM 3256 C CA . ILE B 1 116 ? 55.517 47.661 21.585 1.00 13.25 ? 117 ILE B CA 1 ATOM 3257 C C . ILE B 1 116 ? 55.980 46.489 20.669 1.00 14.51 ? 117 ILE B C 1 ATOM 3258 O O . ILE B 1 116 ? 55.722 45.305 20.974 1.00 14.16 ? 117 ILE B O 1 ATOM 3259 C CB . ILE B 1 116 ? 54.208 48.392 21.031 1.00 16.04 ? 117 ILE B CB 1 ATOM 3260 C CG1 . ILE B 1 116 ? 53.601 49.302 22.125 1.00 12.15 ? 117 ILE B CG1 1 ATOM 3261 C CG2 . ILE B 1 116 ? 53.133 47.351 20.611 1.00 12.68 ? 117 ILE B CG2 1 ATOM 3262 C CD1 . ILE B 1 116 ? 52.498 50.222 21.605 1.00 13.02 ? 117 ILE B CD1 1 ATOM 3263 N N . GLN B 1 117 ? 56.681 46.810 19.576 1.00 14.11 ? 118 GLN B N 1 ATOM 3264 C CA . GLN B 1 117 ? 57.211 45.793 18.659 1.00 13.62 ? 118 GLN B CA 1 ATOM 3265 C C . GLN B 1 117 ? 58.222 44.903 19.378 1.00 12.19 ? 118 GLN B C 1 ATOM 3266 O O . GLN B 1 117 ? 58.197 43.675 19.241 1.00 12.45 ? 118 GLN B O 1 ATOM 3267 C CB . GLN B 1 117 ? 57.844 46.452 17.448 1.00 12.74 ? 118 GLN B CB 1 ATOM 3268 C CG . GLN B 1 117 ? 56.815 47.245 16.701 1.00 19.50 ? 118 GLN B CG 1 ATOM 3269 C CD . GLN B 1 117 ? 55.641 46.390 16.228 1.00 22.33 ? 118 GLN B CD 1 ATOM 3270 O OE1 . GLN B 1 117 ? 55.786 45.188 15.967 1.00 24.49 ? 118 GLN B OE1 1 ATOM 3271 N NE2 . GLN B 1 117 ? 54.482 47.008 16.092 1.00 24.24 ? 118 GLN B NE2 1 ATOM 3272 N N . PHE B 1 118 ? 59.065 45.516 20.199 1.00 11.60 ? 119 PHE B N 1 ATOM 3273 C CA . PHE B 1 118 ? 60.057 44.763 20.945 1.00 11.97 ? 119 PHE B CA 1 ATOM 3274 C C . PHE B 1 118 ? 59.415 43.835 21.982 1.00 13.34 ? 119 PHE B C 1 ATOM 3275 O O . PHE B 1 118 ? 59.778 42.671 22.079 1.00 13.63 ? 119 PHE B O 1 ATOM 3276 C CB . PHE B 1 118 ? 61.028 45.707 21.648 1.00 11.49 ? 119 PHE B CB 1 ATOM 3277 C CG . PHE B 1 118 ? 62.183 45.005 22.291 1.00 8.14 ? 119 PHE B CG 1 ATOM 3278 C CD1 . PHE B 1 118 ? 62.287 44.935 23.670 1.00 8.45 ? 119 PHE B CD1 1 ATOM 3279 C CD2 . PHE B 1 118 ? 63.164 44.421 21.504 1.00 7.77 ? 119 PHE B CD2 1 ATOM 3280 C CE1 . PHE B 1 118 ? 63.353 44.285 24.258 1.00 11.28 ? 119 PHE B CE1 1 ATOM 3281 C CE2 . PHE B 1 118 ? 64.234 43.765 22.080 1.00 6.08 ? 119 PHE B CE2 1 ATOM 3282 C CZ . PHE B 1 118 ? 64.330 43.696 23.447 1.00 9.32 ? 119 PHE B CZ 1 ATOM 3283 N N . ALA B 1 119 ? 58.520 44.366 22.811 1.00 11.35 ? 120 ALA B N 1 ATOM 3284 C CA . ALA B 1 119 ? 57.849 43.552 23.807 1.00 10.82 ? 120 ALA B CA 1 ATOM 3285 C C . ALA B 1 119 ? 57.062 42.375 23.183 1.00 9.77 ? 120 ALA B C 1 ATOM 3286 O O . ALA B 1 119 ? 56.952 41.324 23.779 1.00 12.46 ? 120 ALA B O 1 ATOM 3287 C CB . ALA B 1 119 ? 56.951 44.421 24.694 1.00 13.06 ? 120 ALA B CB 1 ATOM 3288 N N . THR B 1 120 ? 56.550 42.536 21.976 1.00 10.57 ? 121 THR B N 1 ATOM 3289 C CA . THR B 1 120 ? 55.818 41.466 21.307 1.00 11.50 ? 121 THR B CA 1 ATOM 3290 C C . THR B 1 120 ? 56.791 40.325 20.922 1.00 12.12 ? 121 THR B C 1 ATOM 3291 O O . THR B 1 120 ? 56.524 39.154 21.196 1.00 11.18 ? 121 THR B O 1 ATOM 3292 C CB . THR B 1 120 ? 55.111 42.020 20.048 1.00 10.19 ? 121 THR B CB 1 ATOM 3293 O OG1 . THR B 1 120 ? 54.094 42.962 20.442 1.00 10.72 ? 121 THR B OG1 1 ATOM 3294 C CG2 . THR B 1 120 ? 54.500 40.907 19.235 1.00 8.80 ? 121 THR B CG2 1 ATOM 3295 N N . ALA B 1 121 ? 57.955 40.690 20.375 1.00 12.35 ? 122 ALA B N 1 ATOM 3296 C CA . ALA B 1 121 ? 58.961 39.710 19.951 1.00 11.68 ? 122 ALA B CA 1 ATOM 3297 C C . ALA B 1 121 ? 59.556 38.978 21.142 1.00 13.38 ? 122 ALA B C 1 ATOM 3298 O O . ALA B 1 121 ? 59.739 37.757 21.118 1.00 14.27 ? 122 ALA B O 1 ATOM 3299 C CB . ALA B 1 121 ? 60.053 40.385 19.151 1.00 9.90 ? 122 ALA B CB 1 ATOM 3300 N N . VAL B 1 122 ? 59.803 39.706 22.214 1.00 12.81 ? 123 VAL B N 1 ATOM 3301 C CA . VAL B 1 122 ? 60.365 39.100 23.393 1.00 13.17 ? 123 VAL B CA 1 ATOM 3302 C C . VAL B 1 122 ? 59.316 38.248 24.096 1.00 12.73 ? 123 VAL B C 1 ATOM 3303 O O . VAL B 1 122 ? 59.617 37.196 24.656 1.00 12.64 ? 123 VAL B O 1 ATOM 3304 C CB . VAL B 1 122 ? 60.903 40.201 24.338 1.00 13.19 ? 123 VAL B CB 1 ATOM 3305 C CG1 . VAL B 1 122 ? 61.220 39.648 25.704 1.00 13.91 ? 123 VAL B CG1 1 ATOM 3306 C CG2 . VAL B 1 122 ? 62.132 40.831 23.728 1.00 14.65 ? 123 VAL B CG2 1 ATOM 3307 N N . GLY B 1 123 ? 58.091 38.745 24.142 1.00 11.06 ? 124 GLY B N 1 ATOM 3308 C CA . GLY B 1 123 ? 57.035 38.005 24.810 1.00 10.93 ? 124 GLY B CA 1 ATOM 3309 C C . GLY B 1 123 ? 56.833 36.661 24.148 1.00 13.55 ? 124 GLY B C 1 ATOM 3310 O O . GLY B 1 123 ? 56.735 35.639 24.824 1.00 15.03 ? 124 GLY B O 1 ATOM 3311 N N . MET B 1 124 ? 56.782 36.647 22.821 1.00 13.60 ? 125 MET B N 1 ATOM 3312 C CA . MET B 1 124 ? 56.583 35.391 22.121 1.00 15.96 ? 125 MET B CA 1 ATOM 3313 C C . MET B 1 124 ? 57.689 34.356 22.306 1.00 17.04 ? 125 MET B C 1 ATOM 3314 O O . MET B 1 124 ? 57.415 33.151 22.319 1.00 14.19 ? 125 MET B O 1 ATOM 3315 C CB . MET B 1 124 ? 56.322 35.652 20.653 1.00 15.69 ? 125 MET B CB 1 ATOM 3316 C CG . MET B 1 124 ? 54.968 36.338 20.483 1.00 19.59 ? 125 MET B CG 1 ATOM 3317 S SD . MET B 1 124 ? 54.315 36.005 18.929 1.00 19.74 ? 125 MET B SD 1 ATOM 3318 C CE . MET B 1 124 ? 53.820 34.302 19.162 1.00 18.84 ? 125 MET B CE 1 ATOM 3319 N N . SER B 1 125 ? 58.920 34.833 22.521 1.00 17.47 ? 126 SER B N 1 ATOM 3320 C CA . SER B 1 125 ? 60.057 33.946 22.713 1.00 16.01 ? 126 SER B CA 1 ATOM 3321 C C . SER B 1 125 ? 59.896 33.137 23.990 1.00 15.99 ? 126 SER B C 1 ATOM 3322 O O . SER B 1 125 ? 60.608 32.146 24.178 1.00 16.69 ? 126 SER B O 1 ATOM 3323 C CB . SER B 1 125 ? 61.380 34.743 22.743 1.00 14.48 ? 126 SER B CB 1 ATOM 3324 O OG . SER B 1 125 ? 61.553 35.396 23.990 1.00 12.11 ? 126 SER B OG 1 ATOM 3325 N N . ASN B 1 126 ? 58.995 33.567 24.890 1.00 15.34 ? 127 ASN B N 1 ATOM 3326 C CA . ASN B 1 126 ? 58.750 32.834 26.138 1.00 15.13 ? 127 ASN B CA 1 ATOM 3327 C C . ASN B 1 126 ? 57.682 31.755 25.984 1.00 14.97 ? 127 ASN B C 1 ATOM 3328 O O . ASN B 1 126 ? 57.382 31.039 26.930 1.00 16.22 ? 127 ASN B O 1 ATOM 3329 C CB . ASN B 1 126 ? 58.302 33.761 27.246 1.00 15.28 ? 127 ASN B CB 1 ATOM 3330 C CG . ASN B 1 126 ? 59.293 34.845 27.518 1.00 18.19 ? 127 ASN B CG 1 ATOM 3331 O OD1 . ASN B 1 126 ? 60.506 34.661 27.348 1.00 18.63 ? 127 ASN B OD1 1 ATOM 3332 N ND2 . ASN B 1 126 ? 58.792 35.986 27.971 1.00 17.91 ? 127 ASN B ND2 1 ATOM 3333 N N . CYS B 1 127 ? 57.076 31.673 24.807 1.00 14.09 ? 128 CYS B N 1 ATOM 3334 C CA . CYS B 1 127 ? 56.040 30.695 24.559 1.00 13.72 ? 128 CYS B CA 1 ATOM 3335 C C . CYS B 1 127 ? 56.580 29.638 23.619 1.00 11.40 ? 128 CYS B C 1 ATOM 3336 O O . CYS B 1 127 ? 56.879 29.938 22.479 1.00 11.73 ? 128 CYS B O 1 ATOM 3337 C CB . CYS B 1 127 ? 54.856 31.412 23.908 1.00 14.25 ? 128 CYS B CB 1 ATOM 3338 S SG . CYS B 1 127 ? 54.188 32.766 24.938 1.00 12.69 ? 128 CYS B SG 1 ATOM 3339 N N . PRO B 1 128 ? 56.647 28.370 24.047 1.00 11.07 ? 129 PRO B N 1 ATOM 3340 C CA . PRO B 1 128 ? 57.164 27.290 23.200 1.00 11.83 ? 129 PRO B CA 1 ATOM 3341 C C . PRO B 1 128 ? 56.478 27.227 21.845 1.00 12.20 ? 129 PRO B C 1 ATOM 3342 O O . PRO B 1 128 ? 55.263 27.405 21.753 1.00 12.89 ? 129 PRO B O 1 ATOM 3343 C CB . PRO B 1 128 ? 56.870 26.029 24.005 1.00 12.79 ? 129 PRO B CB 1 ATOM 3344 C CG . PRO B 1 128 ? 56.881 26.514 25.422 1.00 13.58 ? 129 PRO B CG 1 ATOM 3345 C CD . PRO B 1 128 ? 56.174 27.856 25.347 1.00 11.74 ? 129 PRO B CD 1 ATOM 3346 N N . GLY B 1 129 ? 57.262 26.998 20.796 1.00 12.04 ? 130 GLY B N 1 ATOM 3347 C CA . GLY B 1 129 ? 56.704 26.899 19.452 1.00 13.34 ? 130 GLY B CA 1 ATOM 3348 C C . GLY B 1 129 ? 56.764 28.178 18.633 1.00 14.01 ? 130 GLY B C 1 ATOM 3349 O O . GLY B 1 129 ? 56.611 28.133 17.410 1.00 14.86 ? 130 GLY B O 1 ATOM 3350 N N . SER B 1 130 ? 56.995 29.314 19.294 1.00 14.90 ? 131 SER B N 1 ATOM 3351 C CA . SER B 1 130 ? 57.041 30.609 18.611 1.00 13.66 ? 131 SER B CA 1 ATOM 3352 C C . SER B 1 130 ? 58.202 30.798 17.696 1.00 14.01 ? 131 SER B C 1 ATOM 3353 O O . SER B 1 130 ? 59.292 30.303 17.953 1.00 14.24 ? 131 SER B O 1 ATOM 3354 C CB . SER B 1 130 ? 57.101 31.751 19.626 1.00 13.45 ? 131 SER B CB 1 ATOM 3355 O OG . SER B 1 130 ? 55.982 31.748 20.477 1.00 15.30 ? 131 SER B OG 1 ATOM 3356 N N . PRO B 1 131 ? 57.972 31.466 16.567 1.00 15.47 ? 132 PRO B N 1 ATOM 3357 C CA . PRO B 1 131 ? 59.081 31.704 15.636 1.00 16.17 ? 132 PRO B CA 1 ATOM 3358 C C . PRO B 1 131 ? 59.839 32.942 16.196 1.00 16.04 ? 132 PRO B C 1 ATOM 3359 O O . PRO B 1 131 ? 59.400 33.541 17.189 1.00 14.33 ? 132 PRO B O 1 ATOM 3360 C CB . PRO B 1 131 ? 58.370 32.008 14.316 1.00 16.55 ? 132 PRO B CB 1 ATOM 3361 C CG . PRO B 1 131 ? 57.092 32.631 14.764 1.00 16.03 ? 132 PRO B CG 1 ATOM 3362 C CD . PRO B 1 131 ? 56.674 31.809 15.956 1.00 15.69 ? 132 PRO B CD 1 ATOM 3363 N N . ARG B 1 132 ? 60.980 33.297 15.612 1.00 15.86 ? 133 ARG B N 1 ATOM 3364 C CA . ARG B 1 132 ? 61.716 34.461 16.102 1.00 16.38 ? 133 ARG B CA 1 ATOM 3365 C C . ARG B 1 132 ? 61.297 35.643 15.237 1.00 12.83 ? 133 ARG B C 1 ATOM 3366 O O . ARG B 1 132 ? 61.532 35.661 14.039 1.00 13.22 ? 133 ARG B O 1 ATOM 3367 C CB . ARG B 1 132 ? 63.237 34.208 16.059 1.00 20.94 ? 133 ARG B CB 1 ATOM 3368 C CG . ARG B 1 132 ? 63.938 34.436 17.433 1.00 26.47 ? 133 ARG B CG 1 ATOM 3369 C CD . ARG B 1 132 ? 65.426 34.022 17.434 1.00 31.58 ? 133 ARG B CD 1 ATOM 3370 N NE . ARG B 1 132 ? 66.079 34.391 16.183 1.00 33.78 ? 133 ARG B NE 1 ATOM 3371 C CZ . ARG B 1 132 ? 66.841 35.466 16.032 1.00 35.27 ? 133 ARG B CZ 1 ATOM 3372 N NH1 . ARG B 1 132 ? 67.071 36.285 17.054 1.00 36.22 ? 133 ARG B NH1 1 ATOM 3373 N NH2 . ARG B 1 132 ? 67.310 35.763 14.835 1.00 38.12 ? 133 ARG B NH2 1 ATOM 3374 N N . LEU B 1 133 ? 60.613 36.602 15.846 1.00 13.01 ? 134 LEU B N 1 ATOM 3375 C CA . LEU B 1 133 ? 60.108 37.751 15.112 1.00 13.04 ? 134 LEU B CA 1 ATOM 3376 C C . LEU B 1 133 ? 61.201 38.752 14.817 1.00 12.32 ? 134 LEU B C 1 ATOM 3377 O O . LEU B 1 133 ? 62.115 38.939 15.605 1.00 10.83 ? 134 LEU B O 1 ATOM 3378 C CB . LEU B 1 133 ? 58.982 38.452 15.912 1.00 14.05 ? 134 LEU B CB 1 ATOM 3379 C CG . LEU B 1 133 ? 57.680 37.727 16.308 1.00 16.37 ? 134 LEU B CG 1 ATOM 3380 C CD1 . LEU B 1 133 ? 56.616 38.711 16.767 1.00 17.57 ? 134 LEU B CD1 1 ATOM 3381 C CD2 . LEU B 1 133 ? 57.185 36.952 15.111 1.00 10.62 ? 134 LEU B CD2 1 ATOM 3382 N N . GLU B 1 134 ? 61.095 39.387 13.672 1.00 13.43 ? 135 GLU B N 1 ATOM 3383 C CA . GLU B 1 134 ? 62.019 40.435 13.275 1.00 14.36 ? 135 GLU B CA 1 ATOM 3384 C C . GLU B 1 134 ? 61.779 41.621 14.210 1.00 15.18 ? 135 GLU B C 1 ATOM 3385 O O . GLU B 1 134 ? 60.643 41.832 14.674 1.00 14.51 ? 135 GLU B O 1 ATOM 3386 C CB . GLU B 1 134 ? 61.680 40.873 11.852 1.00 15.68 ? 135 GLU B CB 1 ATOM 3387 C CG . GLU B 1 134 ? 62.392 42.133 11.349 1.00 15.49 ? 135 GLU B CG 1 ATOM 3388 C CD . GLU B 1 134 ? 61.950 42.538 9.956 1.00 14.61 ? 135 GLU B CD 1 ATOM 3389 O OE1 . GLU B 1 134 ? 60.945 43.263 9.829 1.00 16.21 ? 135 GLU B OE1 1 ATOM 3390 O OE2 . GLU B 1 134 ? 62.618 42.156 8.978 1.00 16.17 ? 135 GLU B OE2 1 ATOM 3391 N N . PHE B 1 135 ? 62.844 42.370 14.519 1.00 15.65 ? 136 PHE B N 1 ATOM 3392 C CA . PHE B 1 135 ? 62.745 43.562 15.368 1.00 14.82 ? 136 PHE B CA 1 ATOM 3393 C C . PHE B 1 135 ? 63.554 44.701 14.761 1.00 16.24 ? 136 PHE B C 1 ATOM 3394 O O . PHE B 1 135 ? 64.767 44.622 14.663 1.00 14.70 ? 136 PHE B O 1 ATOM 3395 C CB . PHE B 1 135 ? 63.215 43.336 16.803 1.00 13.95 ? 136 PHE B CB 1 ATOM 3396 C CG . PHE B 1 135 ? 63.205 44.603 17.622 1.00 14.53 ? 136 PHE B CG 1 ATOM 3397 C CD1 . PHE B 1 135 ? 62.024 45.368 17.742 1.00 14.16 ? 136 PHE B CD1 1 ATOM 3398 C CD2 . PHE B 1 135 ? 64.376 45.094 18.181 1.00 13.27 ? 136 PHE B CD2 1 ATOM 3399 C CE1 . PHE B 1 135 ? 62.016 46.596 18.394 1.00 14.74 ? 136 PHE B CE1 1 ATOM 3400 C CE2 . PHE B 1 135 ? 64.383 46.335 18.848 1.00 13.57 ? 136 PHE B CE2 1 ATOM 3401 C CZ . PHE B 1 135 ? 63.201 47.088 18.952 1.00 15.06 ? 136 PHE B CZ 1 ATOM 3402 N N . LEU B 1 136 ? 62.841 45.722 14.318 1.00 17.02 ? 137 LEU B N 1 ATOM 3403 C CA . LEU B 1 136 ? 63.395 46.920 13.704 1.00 17.83 ? 137 LEU B CA 1 ATOM 3404 C C . LEU B 1 136 ? 63.218 48.061 14.713 1.00 17.81 ? 137 LEU B C 1 ATOM 3405 O O . LEU B 1 136 ? 62.208 48.121 15.412 1.00 16.77 ? 137 LEU B O 1 ATOM 3406 C CB . LEU B 1 136 ? 62.614 47.226 12.419 1.00 18.54 ? 137 LEU B CB 1 ATOM 3407 C CG . LEU B 1 136 ? 63.123 46.768 11.050 1.00 20.55 ? 137 LEU B CG 1 ATOM 3408 C CD1 . LEU B 1 136 ? 63.883 45.480 11.132 1.00 21.95 ? 137 LEU B CD1 1 ATOM 3409 C CD2 . LEU B 1 136 ? 61.975 46.661 10.090 1.00 20.70 ? 137 LEU B CD2 1 ATOM 3410 N N . THR B 1 137 ? 64.211 48.938 14.822 1.00 18.18 ? 138 THR B N 1 ATOM 3411 C CA . THR B 1 137 ? 64.140 50.058 15.755 1.00 18.02 ? 138 THR B CA 1 ATOM 3412 C C . THR B 1 137 ? 64.285 51.383 15.015 1.00 18.46 ? 138 THR B C 1 ATOM 3413 O O . THR B 1 137 ? 64.797 51.419 13.904 1.00 18.83 ? 138 THR B O 1 ATOM 3414 C CB . THR B 1 137 ? 65.228 49.961 16.837 1.00 17.72 ? 138 THR B CB 1 ATOM 3415 O OG1 . THR B 1 137 ? 65.025 50.988 17.808 1.00 17.33 ? 138 THR B OG1 1 ATOM 3416 C CG2 . THR B 1 137 ? 66.609 50.116 16.233 1.00 16.67 ? 138 THR B CG2 1 ATOM 3417 N N . GLY B 1 138 ? 63.793 52.463 15.611 1.00 17.96 ? 139 GLY B N 1 ATOM 3418 C CA . GLY B 1 138 ? 63.917 53.760 14.985 1.00 19.22 ? 139 GLY B CA 1 ATOM 3419 C C . GLY B 1 138 ? 62.633 54.527 14.712 1.00 20.34 ? 139 GLY B C 1 ATOM 3420 O O . GLY B 1 138 ? 62.685 55.577 14.058 1.00 19.39 ? 139 GLY B O 1 ATOM 3421 N N . ARG B 1 139 ? 61.485 54.016 15.169 1.00 18.83 ? 140 ARG B N 1 ATOM 3422 C CA . ARG B 1 139 ? 60.214 54.708 14.927 1.00 17.32 ? 140 ARG B CA 1 ATOM 3423 C C . ARG B 1 139 ? 60.164 55.951 15.789 1.00 16.86 ? 140 ARG B C 1 ATOM 3424 O O . ARG B 1 139 ? 60.437 55.885 16.987 1.00 16.13 ? 140 ARG B O 1 ATOM 3425 C CB . ARG B 1 139 ? 59.017 53.815 15.286 1.00 16.26 ? 140 ARG B CB 1 ATOM 3426 C CG . ARG B 1 139 ? 58.897 52.563 14.422 1.00 16.12 ? 140 ARG B CG 1 ATOM 3427 C CD . ARG B 1 139 ? 57.952 51.506 15.041 1.00 15.69 ? 140 ARG B CD 1 ATOM 3428 N NE . ARG B 1 139 ? 57.980 50.280 14.251 1.00 15.06 ? 140 ARG B NE 1 ATOM 3429 C CZ . ARG B 1 139 ? 58.853 49.300 14.445 1.00 14.72 ? 140 ARG B CZ 1 ATOM 3430 N NH1 . ARG B 1 139 ? 59.747 49.409 15.410 1.00 15.49 ? 140 ARG B NH1 1 ATOM 3431 N NH2 . ARG B 1 139 ? 58.858 48.225 13.664 1.00 11.32 ? 140 ARG B NH2 1 ATOM 3432 N N . SER B 1 140 ? 59.737 57.063 15.196 1.00 19.69 ? 141 SER B N 1 ATOM 3433 C CA . SER B 1 140 ? 59.626 58.314 15.937 1.00 18.96 ? 141 SER B CA 1 ATOM 3434 C C . SER B 1 140 ? 58.722 58.087 17.120 1.00 17.82 ? 141 SER B C 1 ATOM 3435 O O . SER B 1 140 ? 57.823 57.267 17.040 1.00 18.33 ? 141 SER B O 1 ATOM 3436 C CB . SER B 1 140 ? 59.023 59.413 15.043 1.00 22.46 ? 141 SER B CB 1 ATOM 3437 O OG . SER B 1 140 ? 58.654 60.564 15.815 1.00 23.57 ? 141 SER B OG 1 ATOM 3438 N N . ASN B 1 141 ? 58.946 58.818 18.206 1.00 17.81 ? 142 ASN B N 1 ATOM 3439 C CA . ASN B 1 141 ? 58.124 58.709 19.412 1.00 19.35 ? 142 ASN B CA 1 ATOM 3440 C C . ASN B 1 141 ? 56.883 59.600 19.350 1.00 21.10 ? 142 ASN B C 1 ATOM 3441 O O . ASN B 1 141 ? 55.984 59.490 20.181 1.00 19.79 ? 142 ASN B O 1 ATOM 3442 C CB . ASN B 1 141 ? 58.933 59.066 20.647 1.00 18.78 ? 142 ASN B CB 1 ATOM 3443 C CG . ASN B 1 141 ? 58.175 58.838 21.926 1.00 20.55 ? 142 ASN B CG 1 ATOM 3444 O OD1 . ASN B 1 141 ? 57.678 57.734 22.175 1.00 18.68 ? 142 ASN B OD1 1 ATOM 3445 N ND2 . ASN B 1 141 ? 58.084 59.881 22.747 1.00 18.78 ? 142 ASN B ND2 1 ATOM 3446 N N . SER B 1 142 ? 56.813 60.441 18.325 1.00 23.08 ? 143 SER B N 1 ATOM 3447 C CA . SER B 1 142 ? 55.678 61.345 18.146 1.00 24.99 ? 143 SER B CA 1 ATOM 3448 C C . SER B 1 142 ? 54.538 60.652 17.439 1.00 23.12 ? 143 SER B C 1 ATOM 3449 O O . SER B 1 142 ? 54.744 59.945 16.440 1.00 22.68 ? 143 SER B O 1 ATOM 3450 C CB . SER B 1 142 ? 56.081 62.572 17.317 1.00 27.13 ? 143 SER B CB 1 ATOM 3451 O OG . SER B 1 142 ? 57.118 63.289 17.967 1.00 32.85 ? 143 SER B OG 1 ATOM 3452 N N . SER B 1 143 ? 53.334 60.888 17.945 1.00 23.35 ? 144 SER B N 1 ATOM 3453 C CA . SER B 1 143 ? 52.132 60.303 17.350 1.00 23.33 ? 144 SER B CA 1 ATOM 3454 C C . SER B 1 143 ? 50.862 61.146 17.636 1.00 23.01 ? 144 SER B C 1 ATOM 3455 O O . SER B 1 143 ? 50.821 61.941 18.601 1.00 20.49 ? 144 SER B O 1 ATOM 3456 C CB . SER B 1 143 ? 51.948 58.895 17.917 1.00 20.25 ? 144 SER B CB 1 ATOM 3457 O OG . SER B 1 143 ? 51.773 58.983 19.333 1.00 22.02 ? 144 SER B OG 1 ATOM 3458 N N . GLN B 1 144 ? 49.852 60.959 16.783 1.00 22.05 ? 145 GLN B N 1 ATOM 3459 C CA . GLN B 1 144 ? 48.537 61.571 16.928 1.00 22.02 ? 145 GLN B CA 1 ATOM 3460 C C . GLN B 1 144 ? 47.597 60.387 17.293 1.00 21.12 ? 145 GLN B C 1 ATOM 3461 O O . GLN B 1 144 ? 47.823 59.245 16.882 1.00 18.96 ? 145 GLN B O 1 ATOM 3462 C CB . GLN B 1 144 ? 48.047 62.128 15.589 1.00 27.31 ? 145 GLN B CB 1 ATOM 3463 C CG . GLN B 1 144 ? 48.679 63.409 15.053 1.00 36.07 ? 145 GLN B CG 1 ATOM 3464 C CD . GLN B 1 144 ? 47.835 64.003 13.899 1.00 41.25 ? 145 GLN B CD 1 ATOM 3465 O OE1 . GLN B 1 144 ? 48.289 64.100 12.750 1.00 45.32 ? 145 GLN B OE1 1 ATOM 3466 N NE2 . GLN B 1 144 ? 46.584 64.363 14.204 1.00 44.67 ? 145 GLN B NE2 1 ATOM 3467 N N . PRO B 1 145 ? 46.502 60.656 18.007 1.00 20.44 ? 146 PRO B N 1 ATOM 3468 C CA . PRO B 1 145 ? 45.563 59.594 18.387 1.00 19.09 ? 146 PRO B CA 1 ATOM 3469 C C . PRO B 1 145 ? 44.978 58.918 17.138 1.00 17.66 ? 146 PRO B C 1 ATOM 3470 O O . PRO B 1 145 ? 44.753 59.564 16.113 1.00 15.85 ? 146 PRO B O 1 ATOM 3471 C CB . PRO B 1 145 ? 44.471 60.360 19.144 1.00 20.81 ? 146 PRO B CB 1 ATOM 3472 C CG . PRO B 1 145 ? 45.163 61.611 19.629 1.00 20.49 ? 146 PRO B CG 1 ATOM 3473 C CD . PRO B 1 145 ? 46.015 61.973 18.445 1.00 20.82 ? 146 PRO B CD 1 ATOM 3474 N N . SER B 1 146 ? 44.839 57.603 17.186 1.00 16.77 ? 147 SER B N 1 ATOM 3475 C CA . SER B 1 146 ? 44.266 56.880 16.064 1.00 15.19 ? 147 SER B CA 1 ATOM 3476 C C . SER B 1 146 ? 42.802 57.284 15.928 1.00 13.29 ? 147 SER B C 1 ATOM 3477 O O . SER B 1 146 ? 42.186 57.671 16.919 1.00 13.90 ? 147 SER B O 1 ATOM 3478 C CB . SER B 1 146 ? 44.273 55.378 16.380 1.00 15.35 ? 147 SER B CB 1 ATOM 3479 O OG . SER B 1 146 ? 43.593 54.610 15.392 1.00 13.05 ? 147 SER B OG 1 ATOM 3480 N N . PRO B 1 147 ? 42.263 57.299 14.694 1.00 13.17 ? 148 PRO B N 1 ATOM 3481 C CA . PRO B 1 147 ? 40.849 57.630 14.480 1.00 13.81 ? 148 PRO B CA 1 ATOM 3482 C C . PRO B 1 147 ? 40.086 56.428 15.081 1.00 16.47 ? 148 PRO B C 1 ATOM 3483 O O . PRO B 1 147 ? 40.659 55.323 15.244 1.00 15.49 ? 148 PRO B O 1 ATOM 3484 C CB . PRO B 1 147 ? 40.711 57.590 12.968 1.00 12.91 ? 148 PRO B CB 1 ATOM 3485 C CG . PRO B 1 147 ? 42.022 58.072 12.492 1.00 13.65 ? 148 PRO B CG 1 ATOM 3486 C CD . PRO B 1 147 ? 42.988 57.306 13.409 1.00 12.28 ? 148 PRO B CD 1 ATOM 3487 N N . PRO B 1 148 ? 38.796 56.617 15.429 1.00 16.77 ? 149 PRO B N 1 ATOM 3488 C CA . PRO B 1 148 ? 38.067 55.483 15.991 1.00 14.43 ? 149 PRO B CA 1 ATOM 3489 C C . PRO B 1 148 ? 37.548 54.562 14.897 1.00 14.72 ? 149 PRO B C 1 ATOM 3490 O O . PRO B 1 148 ? 37.661 54.850 13.699 1.00 12.49 ? 149 PRO B O 1 ATOM 3491 C CB . PRO B 1 148 ? 36.923 56.166 16.729 1.00 17.16 ? 149 PRO B CB 1 ATOM 3492 C CG . PRO B 1 148 ? 36.606 57.313 15.833 1.00 17.15 ? 149 PRO B CG 1 ATOM 3493 C CD . PRO B 1 148 ? 37.962 57.827 15.385 1.00 15.09 ? 149 PRO B CD 1 ATOM 3494 N N . SER B 1 149 ? 36.987 53.428 15.309 1.00 15.98 ? 150 SER B N 1 ATOM 3495 C CA . SER B 1 149 ? 36.418 52.475 14.362 1.00 17.01 ? 150 SER B CA 1 ATOM 3496 C C . SER B 1 149 ? 37.364 51.889 13.275 1.00 15.95 ? 150 SER B C 1 ATOM 3497 O O . SER B 1 149 ? 36.927 51.638 12.149 1.00 15.75 ? 150 SER B O 1 ATOM 3498 C CB . SER B 1 149 ? 35.142 53.093 13.725 1.00 22.44 ? 150 SER B CB 1 ATOM 3499 O OG . SER B 1 149 ? 34.094 53.251 14.701 1.00 24.49 ? 150 SER B OG 1 ATOM 3500 N N . LEU B 1 150 ? 38.637 51.638 13.620 1.00 13.68 ? 151 LEU B N 1 ATOM 3501 C CA . LEU B 1 150 ? 39.605 51.056 12.674 1.00 12.32 ? 151 LEU B CA 1 ATOM 3502 C C . LEU B 1 150 ? 39.994 49.619 13.064 1.00 12.43 ? 151 LEU B C 1 ATOM 3503 O O . LEU B 1 150 ? 40.638 48.906 12.297 1.00 15.37 ? 151 LEU B O 1 ATOM 3504 C CB . LEU B 1 150 ? 40.875 51.917 12.563 1.00 10.76 ? 151 LEU B CB 1 ATOM 3505 C CG . LEU B 1 150 ? 40.708 53.295 11.911 1.00 11.18 ? 151 LEU B CG 1 ATOM 3506 C CD1 . LEU B 1 150 ? 42.059 53.925 11.687 1.00 12.29 ? 151 LEU B CD1 1 ATOM 3507 C CD2 . LEU B 1 150 ? 39.986 53.137 10.559 1.00 11.03 ? 151 LEU B CD2 1 ATOM 3508 N N . ILE B 1 151 ? 39.569 49.192 14.242 1.00 11.82 ? 152 ILE B N 1 ATOM 3509 C CA . ILE B 1 151 ? 39.880 47.854 14.761 1.00 13.73 ? 152 ILE B CA 1 ATOM 3510 C C . ILE B 1 151 ? 38.727 46.885 14.512 1.00 14.33 ? 152 ILE B C 1 ATOM 3511 O O . ILE B 1 151 ? 37.597 47.162 14.905 1.00 14.24 ? 152 ILE B O 1 ATOM 3512 C CB . ILE B 1 151 ? 40.075 47.899 16.292 1.00 11.23 ? 152 ILE B CB 1 ATOM 3513 C CG1 . ILE B 1 151 ? 41.192 48.903 16.656 1.00 13.12 ? 152 ILE B CG1 1 ATOM 3514 C CG2 . ILE B 1 151 ? 40.377 46.505 16.834 1.00 11.17 ? 152 ILE B CG2 1 ATOM 3515 C CD1 . ILE B 1 151 ? 41.233 49.251 18.131 1.00 10.46 ? 152 ILE B CD1 1 ATOM 3516 N N . PRO B 1 152 ? 38.996 45.750 13.853 1.00 15.25 ? 153 PRO B N 1 ATOM 3517 C CA . PRO B 1 152 ? 37.969 44.746 13.575 1.00 15.29 ? 153 PRO B CA 1 ATOM 3518 C C . PRO B 1 152 ? 37.394 44.191 14.889 1.00 13.21 ? 153 PRO B C 1 ATOM 3519 O O . PRO B 1 152 ? 38.127 43.994 15.871 1.00 11.65 ? 153 PRO B O 1 ATOM 3520 C CB . PRO B 1 152 ? 38.759 43.675 12.827 1.00 15.23 ? 153 PRO B CB 1 ATOM 3521 C CG . PRO B 1 152 ? 39.735 44.481 12.055 1.00 17.38 ? 153 PRO B CG 1 ATOM 3522 C CD . PRO B 1 152 ? 40.237 45.432 13.115 1.00 16.25 ? 153 PRO B CD 1 ATOM 3523 N N . GLY B 1 153 ? 36.079 43.984 14.912 1.00 12.50 ? 154 GLY B N 1 ATOM 3524 C CA . GLY B 1 153 ? 35.424 43.458 16.099 1.00 12.74 ? 154 GLY B CA 1 ATOM 3525 C C . GLY B 1 153 ? 34.941 42.025 15.894 1.00 10.79 ? 154 GLY B C 1 ATOM 3526 O O . GLY B 1 153 ? 34.683 41.601 14.754 1.00 10.31 ? 154 GLY B O 1 ATOM 3527 N N . PRO B 1 154 ? 34.689 41.295 16.987 1.00 9.76 ? 155 PRO B N 1 ATOM 3528 C CA . PRO B 1 154 ? 34.233 39.902 16.884 1.00 10.55 ? 155 PRO B CA 1 ATOM 3529 C C . PRO B 1 154 ? 32.840 39.671 16.289 1.00 12.50 ? 155 PRO B C 1 ATOM 3530 O O . PRO B 1 154 ? 32.514 38.542 15.915 1.00 13.22 ? 155 PRO B O 1 ATOM 3531 C CB . PRO B 1 154 ? 34.346 39.391 18.325 1.00 9.74 ? 155 PRO B CB 1 ATOM 3532 C CG . PRO B 1 154 ? 34.047 40.616 19.170 1.00 8.51 ? 155 PRO B CG 1 ATOM 3533 C CD . PRO B 1 154 ? 34.730 41.758 18.397 1.00 7.48 ? 155 PRO B CD 1 ATOM 3534 N N . GLY B 1 155 ? 32.022 40.733 16.229 1.00 13.70 ? 156 GLY B N 1 ATOM 3535 C CA . GLY B 1 155 ? 30.676 40.635 15.677 1.00 12.39 ? 156 GLY B CA 1 ATOM 3536 C C . GLY B 1 155 ? 30.571 41.101 14.234 1.00 13.31 ? 156 GLY B C 1 ATOM 3537 O O . GLY B 1 155 ? 29.492 41.125 13.657 1.00 13.42 ? 156 GLY B O 1 ATOM 3538 N N . ASN B 1 156 ? 31.700 41.464 13.642 1.00 13.95 ? 157 ASN B N 1 ATOM 3539 C CA . ASN B 1 156 ? 31.721 41.934 12.255 1.00 13.95 ? 157 ASN B CA 1 ATOM 3540 C C . ASN B 1 156 ? 31.626 40.787 11.265 1.00 13.51 ? 157 ASN B C 1 ATOM 3541 O O . ASN B 1 156 ? 32.156 39.695 11.506 1.00 14.04 ? 157 ASN B O 1 ATOM 3542 C CB . ASN B 1 156 ? 33.055 42.639 11.945 1.00 16.40 ? 157 ASN B CB 1 ATOM 3543 C CG . ASN B 1 156 ? 33.312 43.914 12.778 1.00 20.05 ? 157 ASN B CG 1 ATOM 3544 O OD1 . ASN B 1 156 ? 34.335 44.555 12.578 1.00 21.84 ? 157 ASN B OD1 1 ATOM 3545 N ND2 . ASN B 1 156 ? 32.430 44.252 13.720 1.00 22.07 ? 157 ASN B ND2 1 ATOM 3546 N N . THR B 1 157 ? 31.088 41.067 10.091 1.00 12.47 ? 158 THR B N 1 ATOM 3547 C CA . THR B 1 157 ? 31.021 40.042 9.057 1.00 15.15 ? 158 THR B CA 1 ATOM 3548 C C . THR B 1 157 ? 32.420 39.832 8.435 1.00 14.44 ? 158 THR B C 1 ATOM 3549 O O . THR B 1 157 ? 33.291 40.703 8.499 1.00 13.09 ? 158 THR B O 1 ATOM 3550 C CB . THR B 1 157 ? 30.112 40.446 7.881 1.00 14.71 ? 158 THR B CB 1 ATOM 3551 O OG1 . THR B 1 157 ? 30.708 41.561 7.210 1.00 13.48 ? 158 THR B OG1 1 ATOM 3552 C CG2 . THR B 1 157 ? 28.688 40.785 8.345 1.00 16.70 ? 158 THR B CG2 1 ATOM 3553 N N . VAL B 1 158 ? 32.611 38.694 7.783 1.00 13.43 ? 159 VAL B N 1 ATOM 3554 C CA . VAL B 1 158 ? 33.879 38.411 7.135 1.00 12.92 ? 159 VAL B CA 1 ATOM 3555 C C . VAL B 1 158 ? 34.144 39.515 6.107 1.00 13.54 ? 159 VAL B C 1 ATOM 3556 O O . VAL B 1 158 ? 35.273 39.989 5.962 1.00 12.87 ? 159 VAL B O 1 ATOM 3557 C CB . VAL B 1 158 ? 33.884 36.982 6.471 1.00 12.50 ? 159 VAL B CB 1 ATOM 3558 C CG1 . VAL B 1 158 ? 35.036 36.826 5.459 1.00 9.50 ? 159 VAL B CG1 1 ATOM 3559 C CG2 . VAL B 1 158 ? 33.996 35.902 7.574 1.00 9.71 ? 159 VAL B CG2 1 ATOM 3560 N N . THR B 1 159 ? 33.109 39.957 5.412 1.00 14.26 ? 160 THR B N 1 ATOM 3561 C CA . THR B 1 159 ? 33.307 41.008 4.413 1.00 13.83 ? 160 THR B CA 1 ATOM 3562 C C . THR B 1 159 ? 33.879 42.263 5.049 1.00 12.91 ? 160 THR B C 1 ATOM 3563 O O . THR B 1 159 ? 34.890 42.784 4.582 1.00 11.78 ? 160 THR B O 1 ATOM 3564 C CB . THR B 1 159 ? 31.995 41.347 3.691 1.00 16.96 ? 160 THR B CB 1 ATOM 3565 O OG1 . THR B 1 159 ? 31.583 40.199 2.940 1.00 20.32 ? 160 THR B OG1 1 ATOM 3566 C CG2 . THR B 1 159 ? 32.196 42.524 2.723 1.00 15.44 ? 160 THR B CG2 1 ATOM 3567 N N . ALA B 1 160 ? 33.305 42.673 6.172 1.00 12.10 ? 161 ALA B N 1 ATOM 3568 C CA . ALA B 1 160 ? 33.772 43.887 6.833 1.00 13.22 ? 161 ALA B CA 1 ATOM 3569 C C . ALA B 1 160 ? 35.188 43.726 7.363 1.00 13.57 ? 161 ALA B C 1 ATOM 3570 O O . ALA B 1 160 ? 35.989 44.648 7.278 1.00 13.05 ? 161 ALA B O 1 ATOM 3571 C CB . ALA B 1 160 ? 32.840 44.291 7.947 1.00 12.78 ? 161 ALA B CB 1 ATOM 3572 N N . ILE B 1 161 ? 35.513 42.537 7.853 1.00 12.70 ? 162 ILE B N 1 ATOM 3573 C CA . ILE B 1 161 ? 36.847 42.298 8.380 1.00 12.78 ? 162 ILE B CA 1 ATOM 3574 C C . ILE B 1 161 ? 37.887 42.333 7.275 1.00 12.83 ? 162 ILE B C 1 ATOM 3575 O O . ILE B 1 161 ? 38.956 42.949 7.433 1.00 13.73 ? 162 ILE B O 1 ATOM 3576 C CB . ILE B 1 161 ? 36.934 40.943 9.134 1.00 12.91 ? 162 ILE B CB 1 ATOM 3577 C CG1 . ILE B 1 161 ? 36.215 41.060 10.481 1.00 11.62 ? 162 ILE B CG1 1 ATOM 3578 C CG2 . ILE B 1 161 ? 38.380 40.564 9.386 1.00 11.34 ? 162 ILE B CG2 1 ATOM 3579 C CD1 . ILE B 1 161 ? 36.015 39.767 11.166 1.00 10.62 ? 162 ILE B CD1 1 ATOM 3580 N N . LEU B 1 162 ? 37.553 41.756 6.127 1.00 11.34 ? 163 LEU B N 1 ATOM 3581 C CA . LEU B 1 162 ? 38.505 41.690 5.035 1.00 12.30 ? 163 LEU B CA 1 ATOM 3582 C C . LEU B 1 162 ? 38.715 43.030 4.407 1.00 15.28 ? 163 LEU B C 1 ATOM 3583 O O . LEU B 1 162 ? 39.820 43.327 3.922 1.00 14.77 ? 163 LEU B O 1 ATOM 3584 C CB . LEU B 1 162 ? 38.071 40.689 3.972 1.00 12.33 ? 163 LEU B CB 1 ATOM 3585 C CG . LEU B 1 162 ? 37.956 39.230 4.406 1.00 13.51 ? 163 LEU B CG 1 ATOM 3586 C CD1 . LEU B 1 162 ? 37.672 38.372 3.186 1.00 12.06 ? 163 LEU B CD1 1 ATOM 3587 C CD2 . LEU B 1 162 ? 39.216 38.749 5.110 1.00 14.62 ? 163 LEU B CD2 1 ATOM 3588 N N . ASP B 1 163 ? 37.648 43.829 4.388 1.00 16.21 ? 164 ASP B N 1 ATOM 3589 C CA . ASP B 1 163 ? 37.712 45.176 3.821 1.00 18.39 ? 164 ASP B CA 1 ATOM 3590 C C . ASP B 1 163 ? 38.562 46.128 4.693 1.00 15.87 ? 164 ASP B C 1 ATOM 3591 O O . ASP B 1 163 ? 39.365 46.918 4.177 1.00 16.68 ? 164 ASP B O 1 ATOM 3592 C CB . ASP B 1 163 ? 36.298 45.736 3.602 1.00 21.04 ? 164 ASP B CB 1 ATOM 3593 C CG . ASP B 1 163 ? 35.588 45.114 2.384 1.00 27.48 ? 164 ASP B CG 1 ATOM 3594 O OD1 . ASP B 1 163 ? 34.377 45.403 2.211 1.00 32.54 ? 164 ASP B OD1 1 ATOM 3595 O OD2 . ASP B 1 163 ? 36.221 44.349 1.593 1.00 32.32 ? 164 ASP B OD2 1 ATOM 3596 N N . ARG B 1 164 ? 38.400 46.032 6.007 1.00 13.01 ? 165 ARG B N 1 ATOM 3597 C CA . ARG B 1 164 ? 39.164 46.857 6.919 1.00 12.61 ? 165 ARG B CA 1 ATOM 3598 C C . ARG B 1 164 ? 40.649 46.449 6.835 1.00 14.49 ? 165 ARG B C 1 ATOM 3599 O O . ARG B 1 164 ? 41.533 47.289 6.595 1.00 13.86 ? 165 ARG B O 1 ATOM 3600 C CB . ARG B 1 164 ? 38.629 46.681 8.339 1.00 9.87 ? 165 ARG B CB 1 ATOM 3601 C CG . ARG B 1 164 ? 39.375 47.489 9.444 1.00 12.98 ? 165 ARG B CG 1 ATOM 3602 C CD . ARG B 1 164 ? 39.220 49.044 9.303 1.00 12.21 ? 165 ARG B CD 1 ATOM 3603 N NE . ARG B 1 164 ? 40.240 49.638 8.418 1.00 14.78 ? 165 ARG B NE 1 ATOM 3604 C CZ . ARG B 1 164 ? 41.531 49.815 8.737 1.00 11.68 ? 165 ARG B CZ 1 ATOM 3605 N NH1 . ARG B 1 164 ? 42.001 49.453 9.929 1.00 10.00 ? 165 ARG B NH1 1 ATOM 3606 N NH2 . ARG B 1 164 ? 42.354 50.331 7.843 1.00 11.68 ? 165 ARG B NH2 1 ATOM 3607 N N . MET B 1 165 ? 40.919 45.151 7.005 1.00 12.46 ? 166 MET B N 1 ATOM 3608 C CA . MET B 1 165 ? 42.302 44.641 6.935 1.00 13.35 ? 166 MET B CA 1 ATOM 3609 C C . MET B 1 165 ? 42.906 44.881 5.555 1.00 14.19 ? 166 MET B C 1 ATOM 3610 O O . MET B 1 165 ? 44.095 45.180 5.434 1.00 15.84 ? 166 MET B O 1 ATOM 3611 C CB . MET B 1 165 ? 42.352 43.139 7.263 1.00 14.83 ? 166 MET B CB 1 ATOM 3612 C CG . MET B 1 165 ? 41.932 42.786 8.723 1.00 15.86 ? 166 MET B CG 1 ATOM 3613 S SD . MET B 1 165 ? 43.052 43.400 10.013 1.00 18.69 ? 166 MET B SD 1 ATOM 3614 C CE . MET B 1 165 ? 44.390 42.197 9.796 1.00 15.98 ? 166 MET B CE 1 ATOM 3615 N N . GLY B 1 166 ? 42.075 44.748 4.521 1.00 13.68 ? 167 GLY B N 1 ATOM 3616 C CA . GLY B 1 166 ? 42.515 44.959 3.157 1.00 14.03 ? 167 GLY B CA 1 ATOM 3617 C C . GLY B 1 166 ? 42.933 46.399 2.971 1.00 15.52 ? 167 GLY B C 1 ATOM 3618 O O . GLY B 1 166 ? 43.898 46.673 2.265 1.00 17.65 ? 167 GLY B O 1 ATOM 3619 N N . ASP B 1 167 ? 42.184 47.312 3.576 1.00 15.69 ? 168 ASP B N 1 ATOM 3620 C CA . ASP B 1 167 ? 42.479 48.737 3.521 1.00 16.69 ? 168 ASP B CA 1 ATOM 3621 C C . ASP B 1 167 ? 43.863 48.989 4.137 1.00 17.08 ? 168 ASP B C 1 ATOM 3622 O O . ASP B 1 167 ? 44.687 49.724 3.563 1.00 17.47 ? 168 ASP B O 1 ATOM 3623 C CB . ASP B 1 167 ? 41.392 49.510 4.286 1.00 17.25 ? 168 ASP B CB 1 ATOM 3624 C CG . ASP B 1 167 ? 41.689 51.008 4.398 1.00 20.49 ? 168 ASP B CG 1 ATOM 3625 O OD1 . ASP B 1 167 ? 41.373 51.580 5.461 1.00 20.25 ? 168 ASP B OD1 1 ATOM 3626 O OD2 . ASP B 1 167 ? 42.236 51.617 3.432 1.00 22.16 ? 168 ASP B OD2 1 ATOM 3627 N N . ALA B 1 168 ? 44.122 48.373 5.288 1.00 17.28 ? 169 ALA B N 1 ATOM 3628 C CA . ALA B 1 168 ? 45.413 48.512 5.972 1.00 17.13 ? 169 ALA B CA 1 ATOM 3629 C C . ALA B 1 168 ? 46.539 47.884 5.164 1.00 17.95 ? 169 ALA B C 1 ATOM 3630 O O . ALA B 1 168 ? 47.711 48.120 5.431 1.00 19.41 ? 169 ALA B O 1 ATOM 3631 C CB . ALA B 1 168 ? 45.360 47.887 7.375 1.00 16.11 ? 169 ALA B CB 1 ATOM 3632 N N . GLY B 1 169 ? 46.179 47.008 4.238 1.00 18.11 ? 170 GLY B N 1 ATOM 3633 C CA . GLY B 1 169 ? 47.162 46.383 3.379 1.00 18.21 ? 170 GLY B CA 1 ATOM 3634 C C . GLY B 1 169 ? 47.297 44.875 3.408 1.00 20.10 ? 170 GLY B C 1 ATOM 3635 O O . GLY B 1 169 ? 48.168 44.330 2.723 1.00 22.25 ? 170 GLY B O 1 ATOM 3636 N N . PHE B 1 170 ? 46.453 44.182 4.162 1.00 19.08 ? 171 PHE B N 1 ATOM 3637 C CA . PHE B 1 170 ? 46.566 42.729 4.233 1.00 16.39 ? 171 PHE B CA 1 ATOM 3638 C C . PHE B 1 170 ? 45.603 42.033 3.325 1.00 16.49 ? 171 PHE B C 1 ATOM 3639 O O . PHE B 1 170 ? 44.457 42.475 3.194 1.00 18.11 ? 171 PHE B O 1 ATOM 3640 C CB . PHE B 1 170 ? 46.329 42.255 5.654 1.00 14.55 ? 171 PHE B CB 1 ATOM 3641 C CG . PHE B 1 170 ? 47.249 42.878 6.644 1.00 17.17 ? 171 PHE B CG 1 ATOM 3642 C CD1 . PHE B 1 170 ? 48.570 42.461 6.729 1.00 17.60 ? 171 PHE B CD1 1 ATOM 3643 C CD2 . PHE B 1 170 ? 46.821 43.932 7.448 1.00 17.28 ? 171 PHE B CD2 1 ATOM 3644 C CE1 . PHE B 1 170 ? 49.468 43.089 7.596 1.00 17.81 ? 171 PHE B CE1 1 ATOM 3645 C CE2 . PHE B 1 170 ? 47.714 44.571 8.324 1.00 18.85 ? 171 PHE B CE2 1 ATOM 3646 C CZ . PHE B 1 170 ? 49.031 44.148 8.393 1.00 18.77 ? 171 PHE B CZ 1 ATOM 3647 N N . SER B 1 171 ? 46.077 40.969 2.678 1.00 15.82 ? 172 SER B N 1 ATOM 3648 C CA . SER B 1 171 ? 45.243 40.133 1.799 1.00 17.03 ? 172 SER B CA 1 ATOM 3649 C C . SER B 1 171 ? 44.435 39.154 2.689 1.00 16.24 ? 172 SER B C 1 ATOM 3650 O O . SER B 1 171 ? 44.727 39.016 3.876 1.00 17.33 ? 172 SER B O 1 ATOM 3651 C CB . SER B 1 171 ? 46.128 39.307 0.847 1.00 18.67 ? 172 SER B CB 1 ATOM 3652 O OG . SER B 1 171 ? 46.918 38.336 1.542 1.00 20.17 ? 172 SER B OG 1 ATOM 3653 N N . PRO B 1 172 ? 43.404 38.481 2.135 1.00 15.16 ? 173 PRO B N 1 ATOM 3654 C CA . PRO B 1 172 ? 42.655 37.547 2.985 1.00 13.91 ? 173 PRO B CA 1 ATOM 3655 C C . PRO B 1 172 ? 43.579 36.464 3.582 1.00 12.50 ? 173 PRO B C 1 ATOM 3656 O O . PRO B 1 172 ? 43.394 36.063 4.730 1.00 11.78 ? 173 PRO B O 1 ATOM 3657 C CB . PRO B 1 172 ? 41.629 36.948 2.024 1.00 12.98 ? 173 PRO B CB 1 ATOM 3658 C CG . PRO B 1 172 ? 41.389 38.041 1.042 1.00 14.21 ? 173 PRO B CG 1 ATOM 3659 C CD . PRO B 1 172 ? 42.765 38.633 0.814 1.00 14.82 ? 173 PRO B CD 1 ATOM 3660 N N . ASP B 1 173 ? 44.589 36.012 2.829 1.00 14.42 ? 174 ASP B N 1 ATOM 3661 C CA . ASP B 1 173 ? 45.515 35.000 3.360 1.00 14.11 ? 174 ASP B CA 1 ATOM 3662 C C . ASP B 1 173 ? 46.233 35.521 4.566 1.00 12.07 ? 174 ASP B C 1 ATOM 3663 O O . ASP B 1 173 ? 46.445 34.798 5.528 1.00 11.01 ? 174 ASP B O 1 ATOM 3664 C CB . ASP B 1 173 ? 46.591 34.644 2.358 1.00 17.57 ? 174 ASP B CB 1 ATOM 3665 C CG . ASP B 1 173 ? 46.102 33.721 1.269 1.00 22.56 ? 174 ASP B CG 1 ATOM 3666 O OD1 . ASP B 1 173 ? 45.041 33.076 1.419 1.00 21.25 ? 174 ASP B OD1 1 ATOM 3667 O OD2 . ASP B 1 173 ? 46.801 33.636 0.239 1.00 26.46 ? 174 ASP B OD2 1 ATOM 3668 N N . GLU B 1 174 ? 46.654 36.779 4.484 1.00 12.56 ? 175 GLU B N 1 ATOM 3669 C CA . GLU B 1 174 ? 47.393 37.407 5.581 1.00 13.13 ? 175 GLU B CA 1 ATOM 3670 C C . GLU B 1 174 ? 46.578 37.621 6.828 1.00 12.28 ? 175 GLU B C 1 ATOM 3671 O O . GLU B 1 174 ? 47.116 37.610 7.937 1.00 13.07 ? 175 GLU B O 1 ATOM 3672 C CB . GLU B 1 174 ? 48.026 38.721 5.128 1.00 14.00 ? 175 GLU B CB 1 ATOM 3673 C CG . GLU B 1 174 ? 49.178 38.482 4.159 1.00 17.25 ? 175 GLU B CG 1 ATOM 3674 C CD . GLU B 1 174 ? 49.743 39.775 3.575 1.00 19.25 ? 175 GLU B CD 1 ATOM 3675 O OE1 . GLU B 1 174 ? 50.951 39.835 3.297 1.00 21.64 ? 175 GLU B OE1 1 ATOM 3676 O OE2 . GLU B 1 174 ? 48.975 40.729 3.380 1.00 19.64 ? 175 GLU B OE2 1 ATOM 3677 N N . VAL B 1 175 ? 45.272 37.818 6.655 1.00 12.97 ? 176 VAL B N 1 ATOM 3678 C CA . VAL B 1 175 ? 44.398 37.998 7.800 1.00 10.81 ? 176 VAL B CA 1 ATOM 3679 C C . VAL B 1 175 ? 44.379 36.677 8.568 1.00 10.86 ? 176 VAL B C 1 ATOM 3680 O O . VAL B 1 175 ? 44.525 36.660 9.790 1.00 12.22 ? 176 VAL B O 1 ATOM 3681 C CB . VAL B 1 175 ? 42.971 38.397 7.373 1.00 11.74 ? 176 VAL B CB 1 ATOM 3682 C CG1 . VAL B 1 175 ? 42.052 38.411 8.595 1.00 11.77 ? 176 VAL B CG1 1 ATOM 3683 C CG2 . VAL B 1 175 ? 42.986 39.793 6.722 1.00 9.69 ? 176 VAL B CG2 1 ATOM 3684 N N . VAL B 1 176 ? 44.233 35.572 7.843 1.00 11.60 ? 177 VAL B N 1 ATOM 3685 C CA . VAL B 1 176 ? 44.238 34.249 8.454 1.00 11.23 ? 177 VAL B CA 1 ATOM 3686 C C . VAL B 1 176 ? 45.622 34.028 9.129 1.00 12.14 ? 177 VAL B C 1 ATOM 3687 O O . VAL B 1 176 ? 45.697 33.595 10.270 1.00 11.09 ? 177 VAL B O 1 ATOM 3688 C CB . VAL B 1 176 ? 43.964 33.165 7.369 1.00 13.40 ? 177 VAL B CB 1 ATOM 3689 C CG1 . VAL B 1 176 ? 44.144 31.734 7.936 1.00 10.21 ? 177 VAL B CG1 1 ATOM 3690 C CG2 . VAL B 1 176 ? 42.555 33.378 6.754 1.00 11.18 ? 177 VAL B CG2 1 ATOM 3691 N N . ASP B 1 177 ? 46.709 34.362 8.440 1.00 13.04 ? 178 ASP B N 1 ATOM 3692 C CA . ASP B 1 177 ? 48.049 34.206 9.020 1.00 12.07 ? 178 ASP B CA 1 ATOM 3693 C C . ASP B 1 177 ? 48.213 34.969 10.340 1.00 12.54 ? 178 ASP B C 1 ATOM 3694 O O . ASP B 1 177 ? 48.738 34.429 11.313 1.00 13.32 ? 178 ASP B O 1 ATOM 3695 C CB . ASP B 1 177 ? 49.127 34.682 8.040 1.00 11.69 ? 178 ASP B CB 1 ATOM 3696 C CG . ASP B 1 177 ? 49.113 33.923 6.720 1.00 15.63 ? 178 ASP B CG 1 ATOM 3697 O OD1 . ASP B 1 177 ? 48.528 32.804 6.684 1.00 13.52 ? 178 ASP B OD1 1 ATOM 3698 O OD2 . ASP B 1 177 ? 49.692 34.453 5.727 1.00 13.35 ? 178 ASP B OD2 1 ATOM 3699 N N . LEU B 1 178 ? 47.776 36.229 10.373 1.00 12.22 ? 179 LEU B N 1 ATOM 3700 C CA . LEU B 1 178 ? 47.881 37.059 11.583 1.00 10.40 ? 179 LEU B CA 1 ATOM 3701 C C . LEU B 1 178 ? 47.128 36.517 12.775 1.00 12.24 ? 179 LEU B C 1 ATOM 3702 O O . LEU B 1 178 ? 47.510 36.782 13.924 1.00 10.25 ? 179 LEU B O 1 ATOM 3703 C CB . LEU B 1 178 ? 47.396 38.473 11.304 1.00 9.86 ? 179 LEU B CB 1 ATOM 3704 C CG . LEU B 1 178 ? 48.437 39.379 10.638 1.00 9.94 ? 179 LEU B CG 1 ATOM 3705 C CD1 . LEU B 1 178 ? 47.801 40.667 10.118 1.00 9.39 ? 179 LEU B CD1 1 ATOM 3706 C CD2 . LEU B 1 178 ? 49.543 39.654 11.652 1.00 10.39 ? 179 LEU B CD2 1 ATOM 3707 N N . LEU B 1 179 ? 46.053 35.769 12.507 1.00 11.65 ? 180 LEU B N 1 ATOM 3708 C CA . LEU B 1 179 ? 45.213 35.194 13.559 1.00 11.32 ? 180 LEU B CA 1 ATOM 3709 C C . LEU B 1 179 ? 45.835 33.989 14.281 1.00 9.52 ? 180 LEU B C 1 ATOM 3710 O O . LEU B 1 179 ? 45.261 33.471 15.219 1.00 8.29 ? 180 LEU B O 1 ATOM 3711 C CB . LEU B 1 179 ? 43.811 34.865 12.997 1.00 10.97 ? 180 LEU B CB 1 ATOM 3712 C CG . LEU B 1 179 ? 42.847 36.053 13.137 1.00 12.52 ? 180 LEU B CG 1 ATOM 3713 C CD1 . LEU B 1 179 ? 41.761 35.955 12.097 1.00 12.36 ? 180 LEU B CD1 1 ATOM 3714 C CD2 . LEU B 1 179 ? 42.260 36.073 14.554 1.00 8.45 ? 180 LEU B CD2 1 ATOM 3715 N N . ALA B 1 180 ? 47.030 33.574 13.868 1.00 8.76 ? 181 ALA B N 1 ATOM 3716 C CA . ALA B 1 180 ? 47.718 32.471 14.554 1.00 7.54 ? 181 ALA B CA 1 ATOM 3717 C C . ALA B 1 180 ? 47.951 32.930 16.005 1.00 9.12 ? 181 ALA B C 1 ATOM 3718 O O . ALA B 1 180 ? 48.160 32.102 16.908 1.00 7.89 ? 181 ALA B O 1 ATOM 3719 C CB . ALA B 1 180 ? 49.077 32.170 13.867 1.00 6.77 ? 181 ALA B CB 1 ATOM 3720 N N . ALA B 1 181 ? 47.936 34.254 16.244 1.00 7.50 ? 182 ALA B N 1 ATOM 3721 C CA . ALA B 1 181 ? 48.119 34.783 17.593 1.00 6.09 ? 182 ALA B CA 1 ATOM 3722 C C . ALA B 1 181 ? 47.018 34.279 18.522 1.00 6.50 ? 182 ALA B C 1 ATOM 3723 O O . ALA B 1 181 ? 47.194 34.241 19.734 1.00 5.46 ? 182 ALA B O 1 ATOM 3724 C CB . ALA B 1 181 ? 48.171 36.335 17.582 1.00 7.14 ? 182 ALA B CB 1 HETATM 3725 N N . HSO B 1 182 ? 45.881 33.869 17.949 1.00 7.03 ? 183 HSO B N 1 HETATM 3726 C CA . HSO B 1 182 ? 44.777 33.341 18.761 1.00 7.01 ? 183 HSO B CA 1 HETATM 3727 C CB . HSO B 1 182 ? 43.410 33.404 18.045 1.00 6.73 ? 183 HSO B CB 1 HETATM 3728 C CG . HSO B 1 182 ? 42.741 34.752 18.208 1.00 8.16 ? 183 HSO B CG 1 HETATM 3729 N ND1 . HSO B 1 182 ? 41.437 35.011 17.794 1.00 10.57 ? 183 HSO B ND1 1 HETATM 3730 C CD2 . HSO B 1 182 ? 43.328 35.951 18.659 1.00 9.13 ? 183 HSO B CD2 1 HETATM 3731 C CE1 . HSO B 1 182 ? 41.268 36.325 17.986 1.00 9.75 ? 183 HSO B CE1 1 HETATM 3732 N NE2 . HSO B 1 182 ? 42.344 36.873 18.459 1.00 8.18 ? 183 HSO B NE2 1 HETATM 3733 C C . HSO B 1 182 ? 45.073 31.950 19.325 1.00 8.27 ? 183 HSO B C 1 HETATM 3734 O O . HSO B 1 182 ? 44.288 31.383 20.092 1.00 10.01 ? 183 HSO B O 1 ATOM 3735 N N . SER B 1 183 ? 46.244 31.413 18.982 1.00 9.38 ? 184 SER B N 1 ATOM 3736 C CA . SER B 1 183 ? 46.704 30.150 19.536 1.00 8.57 ? 184 SER B CA 1 ATOM 3737 C C . SER B 1 183 ? 47.329 30.387 20.941 1.00 8.98 ? 184 SER B C 1 ATOM 3738 O O . SER B 1 183 ? 47.696 29.434 21.631 1.00 10.13 ? 184 SER B O 1 ATOM 3739 C CB . SER B 1 183 ? 47.726 29.494 18.606 1.00 9.94 ? 184 SER B CB 1 ATOM 3740 O OG . SER B 1 183 ? 48.219 28.287 19.199 1.00 11.81 ? 184 SER B OG 1 ATOM 3741 N N . LEU B 1 184 ? 47.491 31.652 21.330 1.00 7.95 ? 185 LEU B N 1 ATOM 3742 C CA . LEU B 1 184 ? 48.041 32.043 22.643 1.00 8.78 ? 185 LEU B CA 1 ATOM 3743 C C . LEU B 1 184 ? 47.004 33.052 23.176 1.00 12.17 ? 185 LEU B C 1 ATOM 3744 O O . LEU B 1 184 ? 47.347 34.199 23.476 1.00 12.08 ? 185 LEU B O 1 ATOM 3745 C CB . LEU B 1 184 ? 49.391 32.769 22.423 1.00 6.80 ? 185 LEU B CB 1 ATOM 3746 C CG . LEU B 1 184 ? 50.549 31.922 21.870 1.00 9.48 ? 185 LEU B CG 1 ATOM 3747 C CD1 . LEU B 1 184 ? 51.773 32.792 21.635 1.00 14.03 ? 185 LEU B CD1 1 ATOM 3748 C CD2 . LEU B 1 184 ? 50.915 30.857 22.890 1.00 8.27 ? 185 LEU B CD2 1 ATOM 3749 N N . ALA B 1 185 ? 45.754 32.617 23.338 1.00 11.32 ? 186 ALA B N 1 ATOM 3750 C CA . ALA B 1 185 ? 44.697 33.571 23.674 1.00 11.03 ? 186 ALA B CA 1 ATOM 3751 C C . ALA B 1 185 ? 43.576 33.096 24.560 1.00 11.99 ? 186 ALA B C 1 ATOM 3752 O O . ALA B 1 185 ? 43.306 31.885 24.659 1.00 12.66 ? 186 ALA B O 1 ATOM 3753 C CB . ALA B 1 185 ? 44.082 34.123 22.354 1.00 5.31 ? 186 ALA B CB 1 ATOM 3754 N N . SER B 1 186 ? 42.908 34.065 25.179 1.00 11.78 ? 187 SER B N 1 ATOM 3755 C CA . SER B 1 186 ? 41.728 33.804 26.000 1.00 12.06 ? 187 SER B CA 1 ATOM 3756 C C . SER B 1 186 ? 40.839 35.041 25.815 1.00 11.96 ? 187 SER B C 1 ATOM 3757 O O . SER B 1 186 ? 41.119 35.871 24.938 1.00 11.57 ? 187 SER B O 1 ATOM 3758 C CB . SER B 1 186 ? 42.108 33.572 27.474 1.00 11.60 ? 187 SER B CB 1 ATOM 3759 O OG . SER B 1 186 ? 42.489 34.760 28.159 1.00 13.41 ? 187 SER B OG 1 ATOM 3760 N N . GLN B 1 187 ? 39.696 35.078 26.494 1.00 11.91 ? 188 GLN B N 1 ATOM 3761 C CA . GLN B 1 187 ? 38.812 36.242 26.474 1.00 11.44 ? 188 GLN B CA 1 ATOM 3762 C C . GLN B 1 187 ? 38.480 36.528 27.924 1.00 11.01 ? 188 GLN B C 1 ATOM 3763 O O . GLN B 1 187 ? 38.388 35.604 28.739 1.00 10.71 ? 188 GLN B O 1 ATOM 3764 C CB . GLN B 1 187 ? 37.529 36.008 25.645 1.00 12.61 ? 188 GLN B CB 1 ATOM 3765 C CG . GLN B 1 187 ? 36.499 34.958 26.176 1.00 14.78 ? 188 GLN B CG 1 ATOM 3766 C CD . GLN B 1 187 ? 35.663 35.433 27.377 1.00 15.19 ? 188 GLN B CD 1 ATOM 3767 O OE1 . GLN B 1 187 ? 35.345 36.631 27.510 1.00 12.73 ? 188 GLN B OE1 1 ATOM 3768 N NE2 . GLN B 1 187 ? 35.373 34.503 28.293 1.00 13.47 ? 188 GLN B NE2 1 ATOM 3769 N N . GLU B 1 188 ? 38.410 37.808 28.269 1.00 11.85 ? 189 GLU B N 1 ATOM 3770 C CA . GLU B 1 188 ? 38.067 38.222 29.623 1.00 12.83 ? 189 GLU B CA 1 ATOM 3771 C C . GLU B 1 188 ? 36.770 39.033 29.599 1.00 13.96 ? 189 GLU B C 1 ATOM 3772 O O . GLU B 1 188 ? 35.982 38.999 30.550 1.00 15.28 ? 189 GLU B O 1 ATOM 3773 C CB . GLU B 1 188 ? 39.162 39.108 30.227 1.00 11.45 ? 189 GLU B CB 1 ATOM 3774 C CG . GLU B 1 188 ? 40.455 38.351 30.497 1.00 16.14 ? 189 GLU B CG 1 ATOM 3775 C CD . GLU B 1 188 ? 41.564 39.209 31.091 1.00 15.33 ? 189 GLU B CD 1 ATOM 3776 O OE1 . GLU B 1 188 ? 42.623 38.624 31.416 1.00 15.38 ? 189 GLU B OE1 1 ATOM 3777 O OE2 . GLU B 1 188 ? 41.390 40.439 31.223 1.00 14.66 ? 189 GLU B OE2 1 ATOM 3778 N N . GLY B 1 189 ? 36.538 39.720 28.490 1.00 13.75 ? 190 GLY B N 1 ATOM 3779 C CA . GLY B 1 189 ? 35.365 40.564 28.397 1.00 16.36 ? 190 GLY B CA 1 ATOM 3780 C C . GLY B 1 189 ? 34.172 40.161 27.556 1.00 15.43 ? 190 GLY B C 1 ATOM 3781 O O . GLY B 1 189 ? 33.206 40.909 27.557 1.00 17.63 ? 190 GLY B O 1 ATOM 3782 N N . LEU B 1 190 ? 34.233 39.063 26.808 1.00 14.60 ? 191 LEU B N 1 ATOM 3783 C CA . LEU B 1 190 ? 33.091 38.637 25.994 1.00 12.59 ? 191 LEU B CA 1 ATOM 3784 C C . LEU B 1 190 ? 32.072 37.839 26.824 1.00 14.07 ? 191 LEU B C 1 ATOM 3785 O O . LEU B 1 190 ? 30.863 37.900 26.567 1.00 15.80 ? 191 LEU B O 1 ATOM 3786 C CB . LEU B 1 190 ? 33.550 37.846 24.772 1.00 11.32 ? 191 LEU B CB 1 ATOM 3787 C CG . LEU B 1 190 ? 34.469 38.584 23.772 1.00 10.97 ? 191 LEU B CG 1 ATOM 3788 C CD1 . LEU B 1 190 ? 34.833 37.623 22.658 1.00 11.76 ? 191 LEU B CD1 1 ATOM 3789 C CD2 . LEU B 1 190 ? 33.800 39.828 23.189 1.00 9.18 ? 191 LEU B CD2 1 ATOM 3790 N N . ASN B 1 191 ? 32.561 37.108 27.827 1.00 13.67 ? 192 ASN B N 1 ATOM 3791 C CA . ASN B 1 191 ? 31.738 36.313 28.732 1.00 15.19 ? 192 ASN B CA 1 ATOM 3792 C C . ASN B 1 191 ? 32.519 36.272 30.017 1.00 17.53 ? 192 ASN B C 1 ATOM 3793 O O . ASN B 1 191 ? 33.350 35.380 30.223 1.00 15.63 ? 192 ASN B O 1 ATOM 3794 C CB . ASN B 1 191 ? 31.513 34.882 28.223 1.00 15.78 ? 192 ASN B CB 1 ATOM 3795 C CG . ASN B 1 191 ? 30.460 34.137 29.040 1.00 15.33 ? 192 ASN B CG 1 ATOM 3796 O OD1 . ASN B 1 191 ? 30.239 34.444 30.221 1.00 15.22 ? 192 ASN B OD1 1 ATOM 3797 N ND2 . ASN B 1 191 ? 29.789 33.174 28.411 1.00 11.23 ? 192 ASN B ND2 1 ATOM 3798 N N . SER B 1 192 ? 32.278 37.260 30.874 1.00 19.31 ? 193 SER B N 1 ATOM 3799 C CA . SER B 1 192 ? 32.996 37.360 32.136 1.00 22.31 ? 193 SER B CA 1 ATOM 3800 C C . SER B 1 192 ? 32.742 36.196 33.101 1.00 22.53 ? 193 SER B C 1 ATOM 3801 O O . SER B 1 192 ? 33.522 35.978 34.043 1.00 22.99 ? 193 SER B O 1 ATOM 3802 C CB . SER B 1 192 ? 32.690 38.699 32.816 1.00 24.79 ? 193 SER B CB 1 ATOM 3803 O OG . SER B 1 192 ? 31.326 38.783 33.199 1.00 28.82 ? 193 SER B OG 1 ATOM 3804 N N . ALA B 1 193 ? 31.676 35.438 32.849 1.00 21.20 ? 194 ALA B N 1 ATOM 3805 C CA . ALA B 1 193 ? 31.326 34.287 33.689 1.00 19.92 ? 194 ALA B CA 1 ATOM 3806 C C . ALA B 1 193 ? 32.386 33.216 33.544 1.00 18.88 ? 194 ALA B C 1 ATOM 3807 O O . ALA B 1 193 ? 32.586 32.437 34.463 1.00 17.90 ? 194 ALA B O 1 ATOM 3808 C CB . ALA B 1 193 ? 29.958 33.727 33.304 1.00 20.05 ? 194 ALA B CB 1 ATOM 3809 N N . ILE B 1 194 ? 33.012 33.132 32.360 1.00 18.14 ? 195 ILE B N 1 ATOM 3810 C CA . ILE B 1 194 ? 34.088 32.174 32.129 1.00 15.46 ? 195 ILE B CA 1 ATOM 3811 C C . ILE B 1 194 ? 35.354 32.958 31.791 1.00 15.78 ? 195 ILE B C 1 ATOM 3812 O O . ILE B 1 194 ? 35.969 32.772 30.755 1.00 16.22 ? 195 ILE B O 1 ATOM 3813 C CB . ILE B 1 194 ? 33.751 31.148 31.048 1.00 14.58 ? 195 ILE B CB 1 ATOM 3814 C CG1 . ILE B 1 194 ? 33.159 31.829 29.819 1.00 14.23 ? 195 ILE B CG1 1 ATOM 3815 C CG2 . ILE B 1 194 ? 32.815 30.097 31.620 1.00 14.33 ? 195 ILE B CG2 1 ATOM 3816 C CD1 . ILE B 1 194 ? 32.966 30.898 28.626 1.00 13.07 ? 195 ILE B CD1 1 ATOM 3817 N N . PHE B 1 195 ? 35.738 33.818 32.722 1.00 15.99 ? 196 PHE B N 1 ATOM 3818 C CA . PHE B 1 195 ? 36.906 34.682 32.611 1.00 17.03 ? 196 PHE B CA 1 ATOM 3819 C C . PHE B 1 195 ? 38.158 33.845 32.244 1.00 17.35 ? 196 PHE B C 1 ATOM 3820 O O . PHE B 1 195 ? 38.442 32.821 32.873 1.00 16.49 ? 196 PHE B O 1 ATOM 3821 C CB . PHE B 1 195 ? 37.050 35.399 33.959 1.00 16.67 ? 196 PHE B CB 1 ATOM 3822 C CG . PHE B 1 195 ? 38.155 36.414 34.023 1.00 18.29 ? 196 PHE B CG 1 ATOM 3823 C CD1 . PHE B 1 195 ? 39.342 36.122 34.697 1.00 17.77 ? 196 PHE B CD1 1 ATOM 3824 C CD2 . PHE B 1 195 ? 37.989 37.689 33.495 1.00 18.86 ? 196 PHE B CD2 1 ATOM 3825 C CE1 . PHE B 1 195 ? 40.361 37.092 34.851 1.00 19.24 ? 196 PHE B CE1 1 ATOM 3826 C CE2 . PHE B 1 195 ? 38.991 38.662 33.644 1.00 18.56 ? 196 PHE B CE2 1 ATOM 3827 C CZ . PHE B 1 195 ? 40.181 38.358 34.327 1.00 18.07 ? 196 PHE B CZ 1 ATOM 3828 N N . ARG B 1 196 ? 38.850 34.263 31.178 1.00 16.65 ? 197 ARG B N 1 ATOM 3829 C CA . ARG B 1 196 ? 40.076 33.612 30.668 1.00 16.78 ? 197 ARG B CA 1 ATOM 3830 C C . ARG B 1 196 ? 39.958 32.214 30.064 1.00 16.10 ? 197 ARG B C 1 ATOM 3831 O O . ARG B 1 196 ? 40.945 31.469 30.004 1.00 15.23 ? 197 ARG B O 1 ATOM 3832 C CB . ARG B 1 196 ? 41.250 33.684 31.663 1.00 17.82 ? 197 ARG B CB 1 ATOM 3833 C CG . ARG B 1 196 ? 41.493 35.105 32.141 1.00 19.23 ? 197 ARG B CG 1 ATOM 3834 C CD . ARG B 1 196 ? 42.888 35.622 31.999 1.00 21.46 ? 197 ARG B CD 1 ATOM 3835 N NE . ARG B 1 196 ? 43.664 35.437 33.203 1.00 22.13 ? 197 ARG B NE 1 ATOM 3836 C CZ . ARG B 1 196 ? 44.368 36.386 33.832 1.00 21.53 ? 197 ARG B CZ 1 ATOM 3837 N NH1 . ARG B 1 196 ? 44.407 37.642 33.431 1.00 21.58 ? 197 ARG B NH1 1 ATOM 3838 N NH2 . ARG B 1 196 ? 45.180 36.028 34.796 1.00 21.58 ? 197 ARG B NH2 1 ATOM 3839 N N . SER B 1 197 ? 38.763 31.902 29.568 1.00 15.91 ? 198 SER B N 1 ATOM 3840 C CA . SER B 1 197 ? 38.488 30.650 28.875 1.00 13.71 ? 198 SER B CA 1 ATOM 3841 C C . SER B 1 197 ? 39.358 30.794 27.617 1.00 15.43 ? 198 SER B C 1 ATOM 3842 O O . SER B 1 197 ? 39.267 31.818 26.918 1.00 14.74 ? 198 SER B O 1 ATOM 3843 C CB . SER B 1 197 ? 37.029 30.617 28.457 1.00 15.21 ? 198 SER B CB 1 ATOM 3844 O OG . SER B 1 197 ? 36.697 31.763 27.673 1.00 13.43 ? 198 SER B OG 1 ATOM 3845 N N . PRO B 1 198 ? 40.237 29.801 27.329 1.00 14.14 ? 199 PRO B N 1 ATOM 3846 C CA . PRO B 1 198 ? 41.138 29.812 26.167 1.00 11.57 ? 199 PRO B CA 1 ATOM 3847 C C . PRO B 1 198 ? 40.458 29.689 24.829 1.00 10.81 ? 199 PRO B C 1 ATOM 3848 O O . PRO B 1 198 ? 39.388 29.084 24.713 1.00 12.51 ? 199 PRO B O 1 ATOM 3849 C CB . PRO B 1 198 ? 42.001 28.571 26.381 1.00 11.63 ? 199 PRO B CB 1 ATOM 3850 C CG . PRO B 1 198 ? 41.886 28.264 27.819 1.00 13.53 ? 199 PRO B CG 1 ATOM 3851 C CD . PRO B 1 198 ? 40.475 28.615 28.169 1.00 12.31 ? 199 PRO B CD 1 ATOM 3852 N N . LEU B 1 199 ? 41.126 30.193 23.812 1.00 8.87 ? 200 LEU B N 1 ATOM 3853 C CA . LEU B 1 199 ? 40.618 30.083 22.470 1.00 8.37 ? 200 LEU B CA 1 ATOM 3854 C C . LEU B 1 199 ? 41.052 28.748 21.856 1.00 10.24 ? 200 LEU B C 1 ATOM 3855 O O . LEU B 1 199 ? 40.493 28.315 20.842 1.00 11.63 ? 200 LEU B O 1 ATOM 3856 C CB . LEU B 1 199 ? 41.063 31.271 21.619 1.00 8.23 ? 200 LEU B CB 1 ATOM 3857 C CG . LEU B 1 199 ? 40.583 32.663 22.101 1.00 7.28 ? 200 LEU B CG 1 ATOM 3858 C CD1 . LEU B 1 199 ? 40.717 33.615 20.918 1.00 4.75 ? 200 LEU B CD1 1 ATOM 3859 C CD2 . LEU B 1 199 ? 39.112 32.630 22.556 1.00 7.50 ? 200 LEU B CD2 1 ATOM 3860 N N . ASP B 1 200 ? 42.105 28.137 22.395 1.00 9.88 ? 201 ASP B N 1 ATOM 3861 C CA . ASP B 1 200 ? 42.501 26.797 21.921 1.00 7.30 ? 201 ASP B CA 1 ATOM 3862 C C . ASP B 1 200 ? 42.941 25.977 23.106 1.00 6.87 ? 201 ASP B C 1 ATOM 3863 O O . ASP B 1 200 ? 43.064 26.529 24.197 1.00 6.18 ? 201 ASP B O 1 ATOM 3864 C CB . ASP B 1 200 ? 43.461 26.821 20.714 1.00 6.13 ? 201 ASP B CB 1 ATOM 3865 C CG . ASP B 1 200 ? 44.927 26.935 21.077 1.00 4.99 ? 201 ASP B CG 1 ATOM 3866 O OD1 . ASP B 1 200 ? 45.332 27.117 22.226 1.00 5.50 ? 201 ASP B OD1 1 ATOM 3867 O OD2 . ASP B 1 200 ? 45.703 26.842 20.137 1.00 6.00 ? 201 ASP B OD2 1 ATOM 3868 N N . SER B 1 201 ? 43.180 24.675 22.941 1.00 7.32 ? 202 SER B N 1 ATOM 3869 C CA . SER B 1 201 ? 43.526 23.865 24.110 1.00 9.90 ? 202 SER B CA 1 ATOM 3870 C C . SER B 1 201 ? 44.925 24.084 24.681 1.00 11.55 ? 202 SER B C 1 ATOM 3871 O O . SER B 1 201 ? 45.205 23.631 25.794 1.00 12.24 ? 202 SER B O 1 ATOM 3872 C CB . SER B 1 201 ? 43.288 22.362 23.829 1.00 9.24 ? 202 SER B CB 1 ATOM 3873 O OG . SER B 1 201 ? 43.996 21.955 22.661 1.00 11.49 ? 202 SER B OG 1 ATOM 3874 N N . THR B 1 202 ? 45.763 24.846 23.973 1.00 9.57 ? 203 THR B N 1 ATOM 3875 C CA . THR B 1 202 ? 47.138 25.103 24.398 1.00 9.63 ? 203 THR B CA 1 ATOM 3876 C C . THR B 1 202 ? 47.438 26.617 24.374 1.00 9.77 ? 203 THR B C 1 ATOM 3877 O O . THR B 1 202 ? 48.134 27.105 23.480 1.00 9.75 ? 203 THR B O 1 ATOM 3878 C CB . THR B 1 202 ? 48.094 24.377 23.432 1.00 9.82 ? 203 THR B CB 1 ATOM 3879 O OG1 . THR B 1 202 ? 47.725 24.696 22.091 1.00 12.47 ? 203 THR B OG1 1 ATOM 3880 C CG2 . THR B 1 202 ? 47.975 22.853 23.583 1.00 11.77 ? 203 THR B CG2 1 ATOM 3881 N N . PRO B 1 203 ? 46.871 27.379 25.318 1.00 10.44 ? 204 PRO B N 1 ATOM 3882 C CA . PRO B 1 203 ? 47.073 28.826 25.384 1.00 11.91 ? 204 PRO B CA 1 ATOM 3883 C C . PRO B 1 203 ? 48.512 29.282 25.672 1.00 13.48 ? 204 PRO B C 1 ATOM 3884 O O . PRO B 1 203 ? 48.808 30.468 25.582 1.00 12.20 ? 204 PRO B O 1 ATOM 3885 C CB . PRO B 1 203 ? 46.101 29.244 26.479 1.00 11.49 ? 204 PRO B CB 1 ATOM 3886 C CG . PRO B 1 203 ? 46.058 28.044 27.366 1.00 11.54 ? 204 PRO B CG 1 ATOM 3887 C CD . PRO B 1 203 ? 45.991 26.927 26.408 1.00 9.81 ? 204 PRO B CD 1 ATOM 3888 N N . GLN B 1 204 ? 49.362 28.349 26.115 1.00 15.59 ? 205 GLN B N 1 ATOM 3889 C CA . GLN B 1 204 ? 50.780 28.649 26.372 1.00 14.63 ? 205 GLN B CA 1 ATOM 3890 C C . GLN B 1 204 ? 51.708 28.034 25.308 1.00 15.12 ? 205 GLN B C 1 ATOM 3891 O O . GLN B 1 204 ? 52.937 28.066 25.460 1.00 16.48 ? 205 GLN B O 1 ATOM 3892 C CB . GLN B 1 204 ? 51.198 28.211 27.782 1.00 15.57 ? 205 GLN B CB 1 ATOM 3893 C CG . GLN B 1 204 ? 50.490 28.970 28.890 1.00 14.95 ? 205 GLN B CG 1 ATOM 3894 C CD . GLN B 1 204 ? 51.054 28.658 30.263 1.00 19.08 ? 205 GLN B CD 1 ATOM 3895 O OE1 . GLN B 1 204 ? 51.805 29.451 30.835 1.00 20.58 ? 205 GLN B OE1 1 ATOM 3896 N NE2 . GLN B 1 204 ? 50.666 27.517 30.822 1.00 18.72 ? 205 GLN B NE2 1 ATOM 3897 N N . VAL B 1 205 ? 51.126 27.491 24.228 1.00 12.24 ? 206 VAL B N 1 ATOM 3898 C CA . VAL B 1 205 ? 51.914 26.900 23.148 1.00 10.96 ? 206 VAL B CA 1 ATOM 3899 C C . VAL B 1 205 ? 51.509 27.509 21.825 1.00 11.37 ? 206 VAL B C 1 ATOM 3900 O O . VAL B 1 205 ? 50.323 27.490 21.464 1.00 9.89 ? 206 VAL B O 1 ATOM 3901 C CB . VAL B 1 205 ? 51.730 25.341 23.058 1.00 10.07 ? 206 VAL B CB 1 ATOM 3902 C CG1 . VAL B 1 205 ? 52.663 24.737 22.014 1.00 8.36 ? 206 VAL B CG1 1 ATOM 3903 C CG2 . VAL B 1 205 ? 52.028 24.715 24.373 1.00 9.60 ? 206 VAL B CG2 1 ATOM 3904 N N . PHE B 1 206 ? 52.485 28.031 21.080 1.00 9.46 ? 207 PHE B N 1 ATOM 3905 C CA . PHE B 1 206 ? 52.191 28.625 19.806 1.00 9.72 ? 207 PHE B CA 1 ATOM 3906 C C . PHE B 1 206 ? 52.176 27.458 18.828 1.00 12.21 ? 207 PHE B C 1 ATOM 3907 O O . PHE B 1 206 ? 53.215 27.024 18.344 1.00 13.24 ? 207 PHE B O 1 ATOM 3908 C CB . PHE B 1 206 ? 53.241 29.677 19.436 1.00 9.40 ? 207 PHE B CB 1 ATOM 3909 C CG . PHE B 1 206 ? 52.946 30.395 18.146 1.00 11.75 ? 207 PHE B CG 1 ATOM 3910 C CD1 . PHE B 1 206 ? 52.113 31.502 18.132 1.00 10.04 ? 207 PHE B CD1 1 ATOM 3911 C CD2 . PHE B 1 206 ? 53.474 29.951 16.956 1.00 10.24 ? 207 PHE B CD2 1 ATOM 3912 C CE1 . PHE B 1 206 ? 51.822 32.142 16.955 1.00 9.22 ? 207 PHE B CE1 1 ATOM 3913 C CE2 . PHE B 1 206 ? 53.185 30.595 15.750 1.00 11.94 ? 207 PHE B CE2 1 ATOM 3914 C CZ . PHE B 1 206 ? 52.353 31.693 15.756 1.00 9.09 ? 207 PHE B CZ 1 ATOM 3915 N N . ASP B 1 207 ? 50.973 26.991 18.499 1.00 12.28 ? 208 ASP B N 1 ATOM 3916 C CA . ASP B 1 207 ? 50.781 25.813 17.638 1.00 12.73 ? 208 ASP B CA 1 ATOM 3917 C C . ASP B 1 207 ? 49.501 25.920 16.771 1.00 11.17 ? 208 ASP B C 1 ATOM 3918 O O . ASP B 1 207 ? 48.729 26.879 16.896 1.00 11.20 ? 208 ASP B O 1 ATOM 3919 C CB . ASP B 1 207 ? 50.718 24.536 18.514 1.00 10.38 ? 208 ASP B CB 1 ATOM 3920 C CG . ASP B 1 207 ? 49.623 24.600 19.557 1.00 10.36 ? 208 ASP B CG 1 ATOM 3921 O OD1 . ASP B 1 207 ? 48.738 25.472 19.479 1.00 12.52 ? 208 ASP B OD1 1 ATOM 3922 O OD2 . ASP B 1 207 ? 49.620 23.768 20.479 1.00 13.18 ? 208 ASP B OD2 1 ATOM 3923 N N . THR B 1 208 ? 49.281 24.913 15.935 1.00 9.91 ? 209 THR B N 1 ATOM 3924 C CA . THR B 1 208 ? 48.138 24.891 15.046 1.00 9.80 ? 209 THR B CA 1 ATOM 3925 C C . THR B 1 208 ? 46.825 24.514 15.707 1.00 9.58 ? 209 THR B C 1 ATOM 3926 O O . THR B 1 208 ? 45.819 24.505 15.024 1.00 12.03 ? 209 THR B O 1 ATOM 3927 C CB . THR B 1 208 ? 48.340 23.922 13.841 1.00 10.77 ? 209 THR B CB 1 ATOM 3928 O OG1 . THR B 1 208 ? 48.437 22.568 14.319 1.00 13.08 ? 209 THR B OG1 1 ATOM 3929 C CG2 . THR B 1 208 ? 49.591 24.313 13.038 1.00 10.27 ? 209 THR B CG2 1 ATOM 3930 N N . GLN B 1 209 ? 46.806 24.200 17.001 1.00 9.58 ? 210 GLN B N 1 ATOM 3931 C CA . GLN B 1 209 ? 45.536 23.803 17.627 1.00 10.29 ? 210 GLN B CA 1 ATOM 3932 C C . GLN B 1 209 ? 44.344 24.745 17.377 1.00 10.93 ? 210 GLN B C 1 ATOM 3933 O O . GLN B 1 209 ? 43.229 24.291 17.193 1.00 10.64 ? 210 GLN B O 1 ATOM 3934 C CB . GLN B 1 209 ? 45.689 23.560 19.119 1.00 9.05 ? 210 GLN B CB 1 ATOM 3935 C CG . GLN B 1 209 ? 46.496 22.314 19.522 1.00 11.18 ? 210 GLN B CG 1 ATOM 3936 C CD . GLN B 1 209 ? 46.136 21.061 18.718 1.00 12.34 ? 210 GLN B CD 1 ATOM 3937 O OE1 . GLN B 1 209 ? 46.988 20.519 18.017 1.00 13.69 ? 210 GLN B OE1 1 ATOM 3938 N NE2 . GLN B 1 209 ? 44.873 20.629 18.781 1.00 9.82 ? 210 GLN B NE2 1 ATOM 3939 N N . PHE B 1 210 ? 44.601 26.052 17.365 1.00 10.53 ? 211 PHE B N 1 ATOM 3940 C CA . PHE B 1 210 ? 43.575 27.077 17.142 1.00 10.11 ? 211 PHE B CA 1 ATOM 3941 C C . PHE B 1 210 ? 42.823 26.822 15.838 1.00 10.14 ? 211 PHE B C 1 ATOM 3942 O O . PHE B 1 210 ? 41.606 26.773 15.832 1.00 12.86 ? 211 PHE B O 1 ATOM 3943 C CB . PHE B 1 210 ? 44.229 28.484 17.113 1.00 8.86 ? 211 PHE B CB 1 ATOM 3944 C CG . PHE B 1 210 ? 43.296 29.570 16.678 1.00 10.00 ? 211 PHE B CG 1 ATOM 3945 C CD1 . PHE B 1 210 ? 42.187 29.912 17.465 1.00 7.47 ? 211 PHE B CD1 1 ATOM 3946 C CD2 . PHE B 1 210 ? 43.505 30.231 15.443 1.00 9.00 ? 211 PHE B CD2 1 ATOM 3947 C CE1 . PHE B 1 210 ? 41.291 30.907 17.031 1.00 5.72 ? 211 PHE B CE1 1 ATOM 3948 C CE2 . PHE B 1 210 ? 42.622 31.221 14.998 1.00 7.46 ? 211 PHE B CE2 1 ATOM 3949 C CZ . PHE B 1 210 ? 41.522 31.558 15.788 1.00 6.86 ? 211 PHE B CZ 1 ATOM 3950 N N . TYR B 1 211 ? 43.570 26.630 14.750 1.00 9.00 ? 212 TYR B N 1 ATOM 3951 C CA . TYR B 1 211 ? 43.012 26.377 13.422 1.00 10.00 ? 212 TYR B CA 1 ATOM 3952 C C . TYR B 1 211 ? 42.198 25.076 13.346 1.00 11.40 ? 212 TYR B C 1 ATOM 3953 O O . TYR B 1 211 ? 41.136 25.037 12.713 1.00 13.21 ? 212 TYR B O 1 ATOM 3954 C CB . TYR B 1 211 ? 44.140 26.371 12.376 1.00 9.54 ? 212 TYR B CB 1 ATOM 3955 C CG . TYR B 1 211 ? 44.794 27.730 12.225 1.00 11.81 ? 212 TYR B CG 1 ATOM 3956 C CD1 . TYR B 1 211 ? 44.145 28.765 11.538 1.00 11.78 ? 212 TYR B CD1 1 ATOM 3957 C CD2 . TYR B 1 211 ? 46.047 27.990 12.781 1.00 10.77 ? 212 TYR B CD2 1 ATOM 3958 C CE1 . TYR B 1 211 ? 44.721 30.008 11.399 1.00 10.87 ? 212 TYR B CE1 1 ATOM 3959 C CE2 . TYR B 1 211 ? 46.637 29.231 12.646 1.00 12.14 ? 212 TYR B CE2 1 ATOM 3960 C CZ . TYR B 1 211 ? 45.972 30.232 11.957 1.00 12.66 ? 212 TYR B CZ 1 ATOM 3961 O OH . TYR B 1 211 ? 46.599 31.444 11.766 1.00 15.00 ? 212 TYR B OH 1 ATOM 3962 N N . ILE B 1 212 ? 42.694 24.016 13.996 1.00 10.34 ? 213 ILE B N 1 ATOM 3963 C CA . ILE B 1 212 ? 42.005 22.714 14.014 1.00 8.21 ? 213 ILE B CA 1 ATOM 3964 C C . ILE B 1 212 ? 40.730 22.817 14.849 1.00 10.91 ? 213 ILE B C 1 ATOM 3965 O O . ILE B 1 212 ? 39.659 22.482 14.376 1.00 11.50 ? 213 ILE B O 1 ATOM 3966 C CB . ILE B 1 212 ? 42.885 21.626 14.685 1.00 9.48 ? 213 ILE B CB 1 ATOM 3967 C CG1 . ILE B 1 212 ? 44.189 21.399 13.886 1.00 8.13 ? 213 ILE B CG1 1 ATOM 3968 C CG2 . ILE B 1 212 ? 42.059 20.336 14.953 1.00 7.46 ? 213 ILE B CG2 1 ATOM 3969 C CD1 . ILE B 1 212 ? 45.247 20.636 14.701 1.00 6.95 ? 213 ILE B CD1 1 ATOM 3970 N N . GLU B 1 213 ? 40.858 23.284 16.087 1.00 10.18 ? 214 GLU B N 1 ATOM 3971 C CA . GLU B 1 213 ? 39.756 23.394 17.012 1.00 9.97 ? 214 GLU B CA 1 ATOM 3972 C C . GLU B 1 213 ? 38.598 24.328 16.656 1.00 13.55 ? 214 GLU B C 1 ATOM 3973 O O . GLU B 1 213 ? 37.444 24.033 17.025 1.00 14.44 ? 214 GLU B O 1 ATOM 3974 C CB . GLU B 1 213 ? 40.285 23.597 18.424 1.00 8.62 ? 214 GLU B CB 1 ATOM 3975 C CG . GLU B 1 213 ? 41.256 22.452 18.825 1.00 8.95 ? 214 GLU B CG 1 ATOM 3976 C CD . GLU B 1 213 ? 41.950 22.648 20.171 1.00 7.65 ? 214 GLU B CD 1 ATOM 3977 O OE1 . GLU B 1 213 ? 42.938 21.945 20.456 1.00 10.63 ? 214 GLU B OE1 1 ATOM 3978 O OE2 . GLU B 1 213 ? 41.520 23.482 20.986 1.00 10.27 ? 214 GLU B OE2 1 ATOM 3979 N N . THR B 1 214 ? 38.860 25.427 15.944 1.00 11.21 ? 215 THR B N 1 ATOM 3980 C CA . THR B 1 214 ? 37.771 26.298 15.526 1.00 12.08 ? 215 THR B CA 1 ATOM 3981 C C . THR B 1 214 ? 36.988 25.642 14.380 1.00 11.77 ? 215 THR B C 1 ATOM 3982 O O . THR B 1 214 ? 35.931 26.136 13.992 1.00 13.11 ? 215 THR B O 1 ATOM 3983 C CB . THR B 1 214 ? 38.277 27.689 15.020 1.00 12.39 ? 215 THR B CB 1 ATOM 3984 O OG1 . THR B 1 214 ? 39.390 27.496 14.154 1.00 15.28 ? 215 THR B OG1 1 ATOM 3985 C CG2 . THR B 1 214 ? 38.689 28.561 16.150 1.00 9.82 ? 215 THR B CG2 1 ATOM 3986 N N . LEU B 1 215 ? 37.565 24.624 13.747 1.00 8.70 ? 216 LEU B N 1 ATOM 3987 C CA . LEU B 1 215 ? 36.896 23.929 12.641 1.00 10.46 ? 216 LEU B CA 1 ATOM 3988 C C . LEU B 1 215 ? 36.004 22.761 13.052 1.00 9.84 ? 216 LEU B C 1 ATOM 3989 O O . LEU B 1 215 ? 35.259 22.224 12.241 1.00 9.87 ? 216 LEU B O 1 ATOM 3990 C CB . LEU B 1 215 ? 37.910 23.446 11.609 1.00 11.26 ? 216 LEU B CB 1 ATOM 3991 C CG . LEU B 1 215 ? 38.403 24.464 10.580 1.00 14.51 ? 216 LEU B CG 1 ATOM 3992 C CD1 . LEU B 1 215 ? 39.589 23.874 9.766 1.00 11.76 ? 216 LEU B CD1 1 ATOM 3993 C CD2 . LEU B 1 215 ? 37.246 24.861 9.672 1.00 12.77 ? 216 LEU B CD2 1 ATOM 3994 N N . LEU B 1 216 ? 36.086 22.348 14.301 1.00 9.83 ? 217 LEU B N 1 ATOM 3995 C CA . LEU B 1 216 ? 35.266 21.255 14.773 1.00 9.64 ? 217 LEU B CA 1 ATOM 3996 C C . LEU B 1 216 ? 33.831 21.764 14.939 1.00 12.09 ? 217 LEU B C 1 ATOM 3997 O O . LEU B 1 216 ? 33.601 22.958 15.172 1.00 11.54 ? 217 LEU B O 1 ATOM 3998 C CB . LEU B 1 216 ? 35.757 20.793 16.141 1.00 8.77 ? 217 LEU B CB 1 ATOM 3999 C CG . LEU B 1 216 ? 37.099 20.077 16.238 1.00 8.71 ? 217 LEU B CG 1 ATOM 4000 C CD1 . LEU B 1 216 ? 37.530 20.077 17.685 1.00 8.07 ? 217 LEU B CD1 1 ATOM 4001 C CD2 . LEU B 1 216 ? 36.981 18.625 15.672 1.00 9.57 ? 217 LEU B CD2 1 ATOM 4002 N N . LYS B 1 217 ? 32.871 20.853 14.844 1.00 11.91 ? 218 LYS B N 1 ATOM 4003 C CA . LYS B 1 217 ? 31.484 21.213 15.045 1.00 13.65 ? 218 LYS B CA 1 ATOM 4004 C C . LYS B 1 217 ? 31.282 21.794 16.456 1.00 12.53 ? 218 LYS B C 1 ATOM 4005 O O . LYS B 1 217 ? 31.763 21.231 17.454 1.00 11.87 ? 218 LYS B O 1 ATOM 4006 C CB . LYS B 1 217 ? 30.615 19.974 14.891 1.00 13.68 ? 218 LYS B CB 1 ATOM 4007 C CG . LYS B 1 217 ? 30.641 19.394 13.526 1.00 22.34 ? 218 LYS B CG 1 ATOM 4008 C CD . LYS B 1 217 ? 29.760 18.141 13.467 1.00 27.79 ? 218 LYS B CD 1 ATOM 4009 C CE . LYS B 1 217 ? 29.912 17.402 12.119 1.00 32.44 ? 218 LYS B CE 1 ATOM 4010 N NZ . LYS B 1 217 ? 29.160 16.088 12.070 1.00 32.60 ? 218 LYS B NZ 1 ATOM 4011 N N . GLY B 1 218 ? 30.528 22.893 16.543 1.00 12.23 ? 219 GLY B N 1 ATOM 4012 C CA . GLY B 1 218 ? 30.256 23.498 17.835 1.00 13.55 ? 219 GLY B CA 1 ATOM 4013 C C . GLY B 1 218 ? 29.169 22.703 18.535 1.00 15.52 ? 219 GLY B C 1 ATOM 4014 O O . GLY B 1 218 ? 28.069 22.545 18.015 1.00 16.70 ? 219 GLY B O 1 ATOM 4015 N N . THR B 1 219 ? 29.446 22.208 19.720 1.00 15.28 ? 220 THR B N 1 ATOM 4016 C CA . THR B 1 219 ? 28.438 21.399 20.411 1.00 15.80 ? 220 THR B CA 1 ATOM 4017 C C . THR B 1 219 ? 28.228 21.822 21.853 1.00 16.65 ? 220 THR B C 1 ATOM 4018 O O . THR B 1 219 ? 27.227 21.453 22.459 1.00 17.90 ? 220 THR B O 1 ATOM 4019 C CB . THR B 1 219 ? 28.879 19.891 20.464 1.00 15.41 ? 220 THR B CB 1 ATOM 4020 O OG1 . THR B 1 219 ? 30.097 19.768 21.209 1.00 16.62 ? 220 THR B OG1 1 ATOM 4021 C CG2 . THR B 1 219 ? 29.136 19.339 19.087 1.00 13.02 ? 220 THR B CG2 1 ATOM 4022 N N . THR B 1 220 ? 29.152 22.627 22.378 1.00 15.43 ? 221 THR B N 1 ATOM 4023 C CA . THR B 1 220 ? 29.157 22.972 23.782 1.00 15.45 ? 221 THR B CA 1 ATOM 4024 C C . THR B 1 220 ? 29.027 24.452 24.047 1.00 16.47 ? 221 THR B C 1 ATOM 4025 O O . THR B 1 220 ? 29.436 25.270 23.239 1.00 19.19 ? 221 THR B O 1 ATOM 4026 C CB . THR B 1 220 ? 30.509 22.475 24.419 1.00 16.42 ? 221 THR B CB 1 ATOM 4027 O OG1 . THR B 1 220 ? 30.685 21.066 24.180 1.00 18.89 ? 221 THR B OG1 1 ATOM 4028 C CG2 . THR B 1 220 ? 30.584 22.749 25.904 1.00 15.57 ? 221 THR B CG2 1 ATOM 4029 N N . GLN B 1 221 ? 28.337 24.768 25.135 1.00 17.50 ? 222 GLN B N 1 ATOM 4030 C CA . GLN B 1 221 ? 28.176 26.132 25.616 1.00 19.70 ? 222 GLN B CA 1 ATOM 4031 C C . GLN B 1 221 ? 29.022 26.059 26.911 1.00 18.48 ? 222 GLN B C 1 ATOM 4032 O O . GLN B 1 221 ? 28.589 25.529 27.949 1.00 17.98 ? 222 GLN B O 1 ATOM 4033 C CB . GLN B 1 221 ? 26.708 26.430 25.907 1.00 20.21 ? 222 GLN B CB 1 ATOM 4034 C CG . GLN B 1 221 ? 26.512 27.758 26.592 1.00 21.61 ? 222 GLN B CG 1 ATOM 4035 C CD . GLN B 1 221 ? 25.050 28.059 26.907 1.00 22.66 ? 222 GLN B CD 1 ATOM 4036 O OE1 . GLN B 1 221 ? 24.198 28.043 26.016 1.00 22.45 ? 222 GLN B OE1 1 ATOM 4037 N NE2 . GLN B 1 221 ? 24.764 28.358 28.168 1.00 22.18 ? 222 GLN B NE2 1 ATOM 4038 N N . PRO B 1 222 ? 30.258 26.583 26.861 1.00 17.75 ? 223 PRO B N 1 ATOM 4039 C CA . PRO B 1 222 ? 31.125 26.521 28.045 1.00 17.33 ? 223 PRO B CA 1 ATOM 4040 C C . PRO B 1 222 ? 30.700 27.266 29.286 1.00 18.06 ? 223 PRO B C 1 ATOM 4041 O O . PRO B 1 222 ? 31.077 26.873 30.400 1.00 17.31 ? 223 PRO B O 1 ATOM 4042 C CB . PRO B 1 222 ? 32.467 27.025 27.513 1.00 16.37 ? 223 PRO B CB 1 ATOM 4043 C CG . PRO B 1 222 ? 32.056 27.997 26.471 1.00 13.44 ? 223 PRO B CG 1 ATOM 4044 C CD . PRO B 1 222 ? 30.916 27.311 25.759 1.00 14.73 ? 223 PRO B CD 1 ATOM 4045 N N . GLY B 1 223 ? 29.909 28.322 29.117 1.00 18.22 ? 224 GLY B N 1 ATOM 4046 C CA . GLY B 1 223 ? 29.512 29.104 30.268 1.00 18.60 ? 224 GLY B CA 1 ATOM 4047 C C . GLY B 1 223 ? 28.034 29.014 30.589 1.00 19.88 ? 224 GLY B C 1 ATOM 4048 O O . GLY B 1 223 ? 27.289 28.358 29.855 1.00 19.29 ? 224 GLY B O 1 ATOM 4049 N N . PRO B 1 224 ? 27.578 29.729 31.637 1.00 19.64 ? 225 PRO B N 1 ATOM 4050 C CA . PRO B 1 224 ? 26.191 29.775 32.109 1.00 21.51 ? 225 PRO B CA 1 ATOM 4051 C C . PRO B 1 224 ? 25.272 30.298 31.022 1.00 22.41 ? 225 PRO B C 1 ATOM 4052 O O . PRO B 1 224 ? 24.102 29.922 30.962 1.00 22.90 ? 225 PRO B O 1 ATOM 4053 C CB . PRO B 1 224 ? 26.260 30.748 33.289 1.00 23.24 ? 225 PRO B CB 1 ATOM 4054 C CG . PRO B 1 224 ? 27.663 30.638 33.764 1.00 22.13 ? 225 PRO B CG 1 ATOM 4055 C CD . PRO B 1 224 ? 28.422 30.616 32.451 1.00 19.03 ? 225 PRO B CD 1 ATOM 4056 N N . SER B 1 225 ? 25.800 31.183 30.181 1.00 20.85 ? 226 SER B N 1 ATOM 4057 C CA . SER B 1 225 ? 25.054 31.714 29.070 1.00 20.13 ? 226 SER B CA 1 ATOM 4058 C C . SER B 1 225 ? 26.031 32.053 27.965 1.00 18.67 ? 226 SER B C 1 ATOM 4059 O O . SER B 1 225 ? 27.242 31.908 28.127 1.00 16.59 ? 226 SER B O 1 ATOM 4060 C CB . SER B 1 225 ? 24.306 32.969 29.497 1.00 24.29 ? 226 SER B CB 1 ATOM 4061 O OG . SER B 1 225 ? 25.213 34.012 29.813 1.00 29.63 ? 226 SER B OG 1 ATOM 4062 N N . LEU B 1 226 ? 25.502 32.474 26.822 1.00 17.83 ? 227 LEU B N 1 ATOM 4063 C CA . LEU B 1 226 ? 26.357 32.862 25.706 1.00 17.85 ? 227 LEU B CA 1 ATOM 4064 C C . LEU B 1 226 ? 26.619 34.358 25.808 1.00 17.32 ? 227 LEU B C 1 ATOM 4065 O O . LEU B 1 226 ? 25.681 35.126 26.007 1.00 20.07 ? 227 LEU B O 1 ATOM 4066 C CB . LEU B 1 226 ? 25.673 32.589 24.377 1.00 16.93 ? 227 LEU B CB 1 ATOM 4067 C CG . LEU B 1 226 ? 25.528 31.146 23.980 1.00 18.62 ? 227 LEU B CG 1 ATOM 4068 C CD1 . LEU B 1 226 ? 24.580 31.052 22.767 1.00 20.58 ? 227 LEU B CD1 1 ATOM 4069 C CD2 . LEU B 1 226 ? 26.899 30.583 23.693 1.00 19.24 ? 227 LEU B CD2 1 ATOM 4070 N N . GLY B 1 227 ? 27.889 34.758 25.741 1.00 16.49 ? 228 GLY B N 1 ATOM 4071 C CA . GLY B 1 227 ? 28.274 36.160 25.802 1.00 13.11 ? 228 GLY B CA 1 ATOM 4072 C C . GLY B 1 227 ? 28.222 36.832 24.436 1.00 13.23 ? 228 GLY B C 1 ATOM 4073 O O . GLY B 1 227 ? 27.736 36.259 23.439 1.00 12.46 ? 228 GLY B O 1 ATOM 4074 N N . PHE B 1 228 ? 28.744 38.053 24.368 1.00 12.19 ? 229 PHE B N 1 ATOM 4075 C CA . PHE B 1 228 ? 28.726 38.789 23.126 1.00 10.62 ? 229 PHE B CA 1 ATOM 4076 C C . PHE B 1 228 ? 29.619 38.085 22.120 1.00 10.85 ? 229 PHE B C 1 ATOM 4077 O O . PHE B 1 228 ? 30.756 37.726 22.450 1.00 9.75 ? 229 PHE B O 1 ATOM 4078 C CB . PHE B 1 228 ? 29.203 40.235 23.353 1.00 11.89 ? 229 PHE B CB 1 ATOM 4079 C CG . PHE B 1 228 ? 29.324 41.046 22.077 1.00 13.46 ? 229 PHE B CG 1 ATOM 4080 C CD1 . PHE B 1 228 ? 28.232 41.213 21.227 1.00 11.67 ? 229 PHE B CD1 1 ATOM 4081 C CD2 . PHE B 1 228 ? 30.562 41.580 21.684 1.00 13.53 ? 229 PHE B CD2 1 ATOM 4082 C CE1 . PHE B 1 228 ? 28.358 41.892 19.998 1.00 14.00 ? 229 PHE B CE1 1 ATOM 4083 C CE2 . PHE B 1 228 ? 30.699 42.265 20.451 1.00 12.11 ? 229 PHE B CE2 1 ATOM 4084 C CZ . PHE B 1 228 ? 29.594 42.419 19.609 1.00 13.42 ? 229 PHE B CZ 1 ATOM 4085 N N . ALA B 1 229 ? 29.074 37.849 20.926 1.00 10.55 ? 230 ALA B N 1 ATOM 4086 C CA . ALA B 1 229 ? 29.766 37.211 19.792 1.00 13.58 ? 230 ALA B CA 1 ATOM 4087 C C . ALA B 1 229 ? 30.374 35.841 20.110 1.00 13.52 ? 230 ALA B C 1 ATOM 4088 O O . ALA B 1 229 ? 31.464 35.488 19.626 1.00 14.60 ? 230 ALA B O 1 ATOM 4089 C CB . ALA B 1 229 ? 30.833 38.141 19.232 1.00 12.77 ? 230 ALA B CB 1 ATOM 4090 N N . GLU B 1 230 ? 29.697 35.118 20.990 1.00 13.50 ? 231 GLU B N 1 ATOM 4091 C CA . GLU B 1 230 ? 30.128 33.797 21.394 1.00 13.77 ? 231 GLU B CA 1 ATOM 4092 C C . GLU B 1 230 ? 29.314 32.737 20.660 1.00 16.22 ? 231 GLU B C 1 ATOM 4093 O O . GLU B 1 230 ? 28.086 32.882 20.544 1.00 15.53 ? 231 GLU B O 1 ATOM 4094 C CB . GLU B 1 230 ? 29.916 33.627 22.880 1.00 12.68 ? 231 GLU B CB 1 ATOM 4095 C CG . GLU B 1 230 ? 30.325 32.272 23.299 1.00 14.78 ? 231 GLU B CG 1 ATOM 4096 C CD . GLU B 1 230 ? 30.313 32.052 24.774 1.00 15.38 ? 231 GLU B CD 1 ATOM 4097 O OE1 . GLU B 1 230 ? 29.995 32.982 25.532 1.00 17.55 ? 231 GLU B OE1 1 ATOM 4098 O OE2 . GLU B 1 230 ? 30.645 30.921 25.193 1.00 17.91 ? 231 GLU B OE2 1 ATOM 4099 N N . GLU B 1 231 ? 30.010 31.756 20.075 1.00 15.21 ? 232 GLU B N 1 ATOM 4100 C CA . GLU B 1 231 ? 29.404 30.621 19.363 1.00 15.26 ? 232 GLU B CA 1 ATOM 4101 C C . GLU B 1 231 ? 29.637 29.362 20.205 1.00 13.54 ? 232 GLU B C 1 ATOM 4102 O O . GLU B 1 231 ? 30.383 29.390 21.194 1.00 13.18 ? 232 GLU B O 1 ATOM 4103 C CB . GLU B 1 231 ? 30.070 30.415 18.000 1.00 16.68 ? 232 GLU B CB 1 ATOM 4104 C CG . GLU B 1 231 ? 29.862 31.574 17.051 1.00 22.86 ? 232 GLU B CG 1 ATOM 4105 C CD . GLU B 1 231 ? 28.407 31.709 16.649 1.00 25.94 ? 232 GLU B CD 1 ATOM 4106 O OE1 . GLU B 1 231 ? 27.868 32.828 16.620 1.00 27.15 ? 232 GLU B OE1 1 ATOM 4107 O OE2 . GLU B 1 231 ? 27.791 30.672 16.355 1.00 28.31 ? 232 GLU B OE2 1 ATOM 4108 N N . LEU B 1 232 ? 28.961 28.268 19.867 1.00 13.81 ? 233 LEU B N 1 ATOM 4109 C CA . LEU B 1 232 ? 29.177 27.026 20.616 1.00 13.52 ? 233 LEU B CA 1 ATOM 4110 C C . LEU B 1 232 ? 30.594 26.552 20.277 1.00 11.31 ? 233 LEU B C 1 ATOM 4111 O O . LEU B 1 232 ? 31.057 26.719 19.137 1.00 9.53 ? 233 LEU B O 1 ATOM 4112 C CB . LEU B 1 232 ? 28.165 25.955 20.212 1.00 11.91 ? 233 LEU B CB 1 ATOM 4113 C CG . LEU B 1 232 ? 26.721 26.230 20.614 1.00 11.62 ? 233 LEU B CG 1 ATOM 4114 C CD1 . LEU B 1 232 ? 25.891 25.182 20.001 1.00 14.52 ? 233 LEU B CD1 1 ATOM 4115 C CD2 . LEU B 1 232 ? 26.576 26.196 22.091 1.00 9.47 ? 233 LEU B CD2 1 ATOM 4116 N N . SER B 1 233 ? 31.296 26.025 21.272 1.00 13.11 ? 234 SER B N 1 ATOM 4117 C CA . SER B 1 233 ? 32.660 25.539 21.055 1.00 14.19 ? 234 SER B CA 1 ATOM 4118 C C . SER B 1 233 ? 32.638 23.999 21.002 1.00 15.34 ? 234 SER B C 1 ATOM 4119 O O . SER B 1 233 ? 31.571 23.402 21.133 1.00 16.84 ? 234 SER B O 1 ATOM 4120 C CB . SER B 1 233 ? 33.576 26.061 22.150 1.00 11.53 ? 234 SER B CB 1 ATOM 4121 O OG . SER B 1 233 ? 33.310 25.375 23.339 1.00 12.54 ? 234 SER B OG 1 ATOM 4122 N N . PRO B 1 234 ? 33.803 23.340 20.838 1.00 16.26 ? 235 PRO B N 1 ATOM 4123 C CA . PRO B 1 234 ? 33.796 21.874 20.769 1.00 16.58 ? 235 PRO B CA 1 ATOM 4124 C C . PRO B 1 234 ? 33.950 21.132 22.084 1.00 16.95 ? 235 PRO B C 1 ATOM 4125 O O . PRO B 1 234 ? 33.805 19.910 22.127 1.00 18.12 ? 235 PRO B O 1 ATOM 4126 C CB . PRO B 1 234 ? 34.952 21.586 19.823 1.00 15.63 ? 235 PRO B CB 1 ATOM 4127 C CG . PRO B 1 234 ? 35.940 22.583 20.253 1.00 17.38 ? 235 PRO B CG 1 ATOM 4128 C CD . PRO B 1 234 ? 35.141 23.863 20.514 1.00 15.85 ? 235 PRO B CD 1 ATOM 4129 N N . PHE B 1 235 ? 34.280 21.845 23.154 1.00 16.71 ? 236 PHE B N 1 ATOM 4130 C CA . PHE B 1 235 ? 34.440 21.206 24.451 1.00 15.23 ? 236 PHE B CA 1 ATOM 4131 C C . PHE B 1 235 ? 34.418 22.155 25.625 1.00 13.30 ? 236 PHE B C 1 ATOM 4132 O O . PHE B 1 235 ? 34.565 23.363 25.475 1.00 14.22 ? 236 PHE B O 1 ATOM 4133 C CB . PHE B 1 235 ? 35.632 20.203 24.487 1.00 17.05 ? 236 PHE B CB 1 ATOM 4134 C CG . PHE B 1 235 ? 36.864 20.609 23.685 1.00 15.23 ? 236 PHE B CG 1 ATOM 4135 C CD1 . PHE B 1 235 ? 37.182 19.948 22.493 1.00 15.05 ? 236 PHE B CD1 1 ATOM 4136 C CD2 . PHE B 1 235 ? 37.735 21.575 24.156 1.00 16.65 ? 236 PHE B CD2 1 ATOM 4137 C CE1 . PHE B 1 235 ? 38.345 20.241 21.778 1.00 15.26 ? 236 PHE B CE1 1 ATOM 4138 C CE2 . PHE B 1 235 ? 38.925 21.879 23.440 1.00 16.58 ? 236 PHE B CE2 1 ATOM 4139 C CZ . PHE B 1 235 ? 39.223 21.212 22.253 1.00 15.25 ? 236 PHE B CZ 1 ATOM 4140 N N . PRO B 1 236 ? 34.141 21.630 26.813 1.00 12.93 ? 237 PRO B N 1 ATOM 4141 C CA . PRO B 1 236 ? 34.094 22.479 27.996 1.00 13.54 ? 237 PRO B CA 1 ATOM 4142 C C . PRO B 1 236 ? 35.352 23.295 28.161 1.00 14.36 ? 237 PRO B C 1 ATOM 4143 O O . PRO B 1 236 ? 36.454 22.825 27.837 1.00 14.19 ? 237 PRO B O 1 ATOM 4144 C CB . PRO B 1 236 ? 33.948 21.469 29.148 1.00 12.89 ? 237 PRO B CB 1 ATOM 4145 C CG . PRO B 1 236 ? 33.212 20.356 28.538 1.00 13.32 ? 237 PRO B CG 1 ATOM 4146 C CD . PRO B 1 236 ? 33.861 20.224 27.167 1.00 15.74 ? 237 PRO B CD 1 ATOM 4147 N N . GLY B 1 237 ? 35.185 24.503 28.686 1.00 13.91 ? 238 GLY B N 1 ATOM 4148 C CA . GLY B 1 237 ? 36.312 25.376 28.921 1.00 13.62 ? 238 GLY B CA 1 ATOM 4149 C C . GLY B 1 237 ? 36.807 26.200 27.748 1.00 13.30 ? 238 GLY B C 1 ATOM 4150 O O . GLY B 1 237 ? 37.430 27.235 27.985 1.00 15.00 ? 238 GLY B O 1 ATOM 4151 N N . GLU B 1 238 ? 36.563 25.760 26.508 1.00 12.03 ? 239 GLU B N 1 ATOM 4152 C CA . GLU B 1 238 ? 36.994 26.484 25.314 1.00 12.08 ? 239 GLU B CA 1 ATOM 4153 C C . GLU B 1 238 ? 35.949 27.483 24.837 1.00 11.99 ? 239 GLU B C 1 ATOM 4154 O O . GLU B 1 238 ? 34.753 27.153 24.737 1.00 11.63 ? 239 GLU B O 1 ATOM 4155 C CB . GLU B 1 238 ? 37.353 25.535 24.171 1.00 10.28 ? 239 GLU B CB 1 ATOM 4156 C CG . GLU B 1 238 ? 37.941 26.266 22.957 1.00 7.74 ? 239 GLU B CG 1 ATOM 4157 C CD . GLU B 1 238 ? 38.641 25.349 21.991 1.00 9.63 ? 239 GLU B CD 1 ATOM 4158 O OE1 . GLU B 1 238 ? 38.127 25.158 20.885 1.00 9.49 ? 239 GLU B OE1 1 ATOM 4159 O OE2 . GLU B 1 238 ? 39.732 24.853 22.320 1.00 10.35 ? 239 GLU B OE2 1 ATOM 4160 N N . PHE B 1 239 ? 36.398 28.705 24.546 1.00 10.62 ? 240 PHE B N 1 ATOM 4161 C CA . PHE B 1 239 ? 35.501 29.763 24.065 1.00 9.71 ? 240 PHE B CA 1 ATOM 4162 C C . PHE B 1 239 ? 35.689 29.878 22.581 1.00 9.59 ? 240 PHE B C 1 ATOM 4163 O O . PHE B 1 239 ? 36.830 29.796 22.114 1.00 12.51 ? 240 PHE B O 1 ATOM 4164 C CB . PHE B 1 239 ? 35.865 31.103 24.705 1.00 11.54 ? 240 PHE B CB 1 ATOM 4165 C CG . PHE B 1 239 ? 34.979 32.254 24.287 1.00 11.02 ? 240 PHE B CG 1 ATOM 4166 C CD1 . PHE B 1 239 ? 35.206 32.942 23.100 1.00 11.42 ? 240 PHE B CD1 1 ATOM 4167 C CD2 . PHE B 1 239 ? 33.942 32.674 25.119 1.00 11.13 ? 240 PHE B CD2 1 ATOM 4168 C CE1 . PHE B 1 239 ? 34.417 34.041 22.738 1.00 11.47 ? 240 PHE B CE1 1 ATOM 4169 C CE2 . PHE B 1 239 ? 33.149 33.790 24.758 1.00 13.05 ? 240 PHE B CE2 1 ATOM 4170 C CZ . PHE B 1 239 ? 33.392 34.459 23.571 1.00 11.25 ? 240 PHE B CZ 1 ATOM 4171 N N . ARG B 1 240 ? 34.617 30.085 21.823 1.00 7.16 ? 241 ARG B N 1 ATOM 4172 C CA . ARG B 1 240 ? 34.745 30.235 20.377 1.00 10.08 ? 241 ARG B CA 1 ATOM 4173 C C . ARG B 1 240 ? 34.128 31.558 19.981 1.00 11.62 ? 241 ARG B C 1 ATOM 4174 O O . ARG B 1 240 ? 32.954 31.776 20.229 1.00 13.95 ? 241 ARG B O 1 ATOM 4175 C CB . ARG B 1 240 ? 34.033 29.123 19.622 1.00 9.39 ? 241 ARG B CB 1 ATOM 4176 C CG . ARG B 1 240 ? 34.126 29.304 18.135 1.00 10.30 ? 241 ARG B CG 1 ATOM 4177 C CD . ARG B 1 240 ? 33.487 28.157 17.398 1.00 13.07 ? 241 ARG B CD 1 ATOM 4178 N NE . ARG B 1 240 ? 34.190 26.898 17.626 1.00 14.04 ? 241 ARG B NE 1 ATOM 4179 C CZ . ARG B 1 240 ? 33.884 25.741 17.030 1.00 13.59 ? 241 ARG B CZ 1 ATOM 4180 N NH1 . ARG B 1 240 ? 32.875 25.679 16.173 1.00 7.99 ? 241 ARG B NH1 1 ATOM 4181 N NH2 . ARG B 1 240 ? 34.653 24.650 17.222 1.00 11.88 ? 241 ARG B NH2 1 ATOM 4182 N N . MET B 1 241 ? 34.893 32.436 19.350 1.00 12.38 ? 242 MET B N 1 ATOM 4183 C CA . MET B 1 241 ? 34.311 33.703 18.958 1.00 11.61 ? 242 MET B CA 1 ATOM 4184 C C . MET B 1 241 ? 33.778 33.641 17.536 1.00 11.44 ? 242 MET B C 1 ATOM 4185 O O . MET B 1 241 ? 34.284 32.914 16.683 1.00 9.15 ? 242 MET B O 1 ATOM 4186 C CB . MET B 1 241 ? 35.241 34.905 19.229 1.00 13.88 ? 242 MET B CB 1 ATOM 4187 C CG . MET B 1 241 ? 36.213 35.306 18.135 1.00 15.65 ? 242 MET B CG 1 ATOM 4188 S SD . MET B 1 241 ? 37.194 36.761 18.630 1.00 14.21 ? 242 MET B SD 1 ATOM 4189 C CE . MET B 1 241 ? 37.879 36.222 20.151 1.00 13.22 ? 242 MET B CE 1 ATOM 4190 N N . ARG B 1 242 ? 32.694 34.371 17.315 1.00 10.96 ? 243 ARG B N 1 ATOM 4191 C CA . ARG B 1 242 ? 32.000 34.387 16.045 1.00 10.70 ? 243 ARG B CA 1 ATOM 4192 C C . ARG B 1 242 ? 32.866 34.717 14.832 1.00 8.67 ? 243 ARG B C 1 ATOM 4193 O O . ARG B 1 242 ? 32.771 34.030 13.830 1.00 9.40 ? 243 ARG B O 1 ATOM 4194 C CB . ARG B 1 242 ? 30.783 35.330 16.188 1.00 14.33 ? 243 ARG B CB 1 ATOM 4195 C CG . ARG B 1 242 ? 29.804 35.373 15.024 1.00 17.28 ? 243 ARG B CG 1 ATOM 4196 C CD . ARG B 1 242 ? 28.723 36.428 15.311 1.00 19.73 ? 243 ARG B CD 1 ATOM 4197 N NE . ARG B 1 242 ? 27.620 36.395 14.353 1.00 22.27 ? 243 ARG B NE 1 ATOM 4198 C CZ . ARG B 1 242 ? 27.611 37.006 13.168 1.00 22.09 ? 243 ARG B CZ 1 ATOM 4199 N NH1 . ARG B 1 242 ? 28.646 37.719 12.743 1.00 22.61 ? 243 ARG B NH1 1 ATOM 4200 N NH2 . ARG B 1 242 ? 26.528 36.933 12.418 1.00 22.33 ? 243 ARG B NH2 1 ATOM 4201 N N . SER B 1 243 ? 33.728 35.740 14.903 1.00 9.13 ? 244 SER B N 1 ATOM 4202 C CA . SER B 1 243 ? 34.553 36.093 13.739 1.00 9.10 ? 244 SER B CA 1 ATOM 4203 C C . SER B 1 243 ? 35.510 34.945 13.343 1.00 8.87 ? 244 SER B C 1 ATOM 4204 O O . SER B 1 243 ? 35.642 34.638 12.161 1.00 11.35 ? 244 SER B O 1 ATOM 4205 C CB . SER B 1 243 ? 35.309 37.417 13.981 1.00 7.41 ? 244 SER B CB 1 ATOM 4206 O OG . SER B 1 243 ? 35.914 37.417 15.260 1.00 8.01 ? 244 SER B OG 1 ATOM 4207 N N . ASP B 1 244 ? 36.138 34.303 14.333 1.00 8.97 ? 245 ASP B N 1 ATOM 4208 C CA . ASP B 1 244 ? 37.042 33.176 14.083 1.00 9.46 ? 245 ASP B CA 1 ATOM 4209 C C . ASP B 1 244 ? 36.274 32.018 13.453 1.00 10.70 ? 245 ASP B C 1 ATOM 4210 O O . ASP B 1 244 ? 36.728 31.418 12.479 1.00 12.19 ? 245 ASP B O 1 ATOM 4211 C CB . ASP B 1 244 ? 37.645 32.667 15.379 1.00 8.75 ? 245 ASP B CB 1 ATOM 4212 C CG . ASP B 1 244 ? 38.693 33.588 15.939 1.00 9.94 ? 245 ASP B CG 1 ATOM 4213 O OD1 . ASP B 1 244 ? 38.984 33.478 17.152 1.00 9.77 ? 245 ASP B OD1 1 ATOM 4214 O OD2 . ASP B 1 244 ? 39.252 34.408 15.170 1.00 12.57 ? 245 ASP B OD2 1 ATOM 4215 N N . ALA B 1 245 ? 35.086 31.731 13.998 1.00 12.06 ? 246 ALA B N 1 ATOM 4216 C CA . ALA B 1 245 ? 34.264 30.640 13.487 1.00 11.40 ? 246 ALA B CA 1 ATOM 4217 C C . ALA B 1 245 ? 33.854 30.911 12.048 1.00 12.03 ? 246 ALA B C 1 ATOM 4218 O O . ALA B 1 245 ? 33.850 30.007 11.227 1.00 11.86 ? 246 ALA B O 1 ATOM 4219 C CB . ALA B 1 245 ? 33.062 30.427 14.364 1.00 10.97 ? 246 ALA B CB 1 ATOM 4220 N N . LEU B 1 246 ? 33.552 32.165 11.720 1.00 12.41 ? 247 LEU B N 1 ATOM 4221 C CA . LEU B 1 246 ? 33.133 32.494 10.362 1.00 11.89 ? 247 LEU B CA 1 ATOM 4222 C C . LEU B 1 246 ? 34.316 32.485 9.416 1.00 12.49 ? 247 LEU B C 1 ATOM 4223 O O . LEU B 1 246 ? 34.189 32.007 8.271 1.00 12.00 ? 247 LEU B O 1 ATOM 4224 C CB . LEU B 1 246 ? 32.460 33.863 10.309 1.00 12.29 ? 247 LEU B CB 1 ATOM 4225 C CG . LEU B 1 246 ? 31.091 34.083 10.952 1.00 15.28 ? 247 LEU B CG 1 ATOM 4226 C CD1 . LEU B 1 246 ? 30.754 35.565 10.838 1.00 15.27 ? 247 LEU B CD1 1 ATOM 4227 C CD2 . LEU B 1 246 ? 30.026 33.265 10.221 1.00 16.62 ? 247 LEU B CD2 1 ATOM 4228 N N . LEU B 1 247 ? 35.463 33.027 9.875 1.00 12.85 ? 248 LEU B N 1 ATOM 4229 C CA . LEU B 1 247 ? 36.659 33.059 9.023 1.00 10.57 ? 248 LEU B CA 1 ATOM 4230 C C . LEU B 1 247 ? 37.119 31.637 8.682 1.00 8.25 ? 248 LEU B C 1 ATOM 4231 O O . LEU B 1 247 ? 37.592 31.385 7.590 1.00 9.44 ? 248 LEU B O 1 ATOM 4232 C CB . LEU B 1 247 ? 37.780 33.890 9.659 1.00 10.49 ? 248 LEU B CB 1 ATOM 4233 C CG . LEU B 1 247 ? 37.556 35.407 9.663 1.00 9.69 ? 248 LEU B CG 1 ATOM 4234 C CD1 . LEU B 1 247 ? 38.462 36.075 10.711 1.00 7.83 ? 248 LEU B CD1 1 ATOM 4235 C CD2 . LEU B 1 247 ? 37.826 35.961 8.261 1.00 8.66 ? 248 LEU B CD2 1 ATOM 4236 N N . ALA B 1 248 ? 36.969 30.715 9.619 1.00 8.99 ? 249 ALA B N 1 ATOM 4237 C CA . ALA B 1 248 ? 37.315 29.302 9.376 1.00 11.10 ? 249 ALA B CA 1 ATOM 4238 C C . ALA B 1 248 ? 36.491 28.668 8.252 1.00 12.07 ? 249 ALA B C 1 ATOM 4239 O O . ALA B 1 248 ? 36.973 27.819 7.510 1.00 12.86 ? 249 ALA B O 1 ATOM 4240 C CB . ALA B 1 248 ? 37.072 28.489 10.657 1.00 10.50 ? 249 ALA B CB 1 ATOM 4241 N N . ARG B 1 249 ? 35.229 29.072 8.164 1.00 13.97 ? 250 ARG B N 1 ATOM 4242 C CA . ARG B 1 249 ? 34.281 28.515 7.208 1.00 12.90 ? 250 ARG B CA 1 ATOM 4243 C C . ARG B 1 249 ? 33.966 29.268 5.929 1.00 15.43 ? 250 ARG B C 1 ATOM 4244 O O . ARG B 1 249 ? 33.450 28.679 4.979 1.00 15.53 ? 250 ARG B O 1 ATOM 4245 C CB . ARG B 1 249 ? 33.010 28.223 7.956 1.00 10.89 ? 250 ARG B CB 1 ATOM 4246 C CG . ARG B 1 249 ? 33.240 27.196 9.010 1.00 9.51 ? 250 ARG B CG 1 ATOM 4247 C CD . ARG B 1 249 ? 32.150 27.237 10.048 1.00 10.23 ? 250 ARG B CD 1 ATOM 4248 N NE . ARG B 1 249 ? 32.329 26.156 11.015 1.00 11.42 ? 250 ARG B NE 1 ATOM 4249 C CZ . ARG B 1 249 ? 33.159 26.196 12.063 1.00 12.61 ? 250 ARG B CZ 1 ATOM 4250 N NH1 . ARG B 1 249 ? 33.905 27.276 12.301 1.00 10.06 ? 250 ARG B NH1 1 ATOM 4251 N NH2 . ARG B 1 249 ? 33.265 25.141 12.874 1.00 11.74 ? 250 ARG B NH2 1 ATOM 4252 N N . ASP B 1 250 ? 34.325 30.549 5.878 1.00 16.24 ? 251 ASP B N 1 ATOM 4253 C CA . ASP B 1 250 ? 34.080 31.397 4.706 1.00 15.58 ? 251 ASP B CA 1 ATOM 4254 C C . ASP B 1 250 ? 34.873 30.965 3.466 1.00 15.30 ? 251 ASP B C 1 ATOM 4255 O O . ASP B 1 250 ? 36.069 30.802 3.529 1.00 13.97 ? 251 ASP B O 1 ATOM 4256 C CB . ASP B 1 250 ? 34.429 32.842 5.054 1.00 13.91 ? 251 ASP B CB 1 ATOM 4257 C CG . ASP B 1 250 ? 33.872 33.811 4.063 1.00 16.01 ? 251 ASP B CG 1 ATOM 4258 O OD1 . ASP B 1 250 ? 34.548 34.047 3.056 1.00 17.05 ? 251 ASP B OD1 1 ATOM 4259 O OD2 . ASP B 1 250 ? 32.743 34.306 4.273 1.00 15.97 ? 251 ASP B OD2 1 ATOM 4260 N N . SER B 1 251 ? 34.231 30.890 2.307 1.00 15.12 ? 252 SER B N 1 ATOM 4261 C CA . SER B 1 251 ? 34.942 30.472 1.105 1.00 15.78 ? 252 SER B CA 1 ATOM 4262 C C . SER B 1 251 ? 36.194 31.298 0.756 1.00 17.48 ? 252 SER B C 1 ATOM 4263 O O . SER B 1 251 ? 37.131 30.790 0.110 1.00 18.10 ? 252 SER B O 1 ATOM 4264 C CB . SER B 1 251 ? 34.004 30.454 -0.097 1.00 18.20 ? 252 SER B CB 1 ATOM 4265 O OG . SER B 1 251 ? 33.461 31.741 -0.313 1.00 21.27 ? 252 SER B OG 1 ATOM 4266 N N . ARG B 1 252 ? 36.233 32.558 1.184 1.00 17.03 ? 253 ARG B N 1 ATOM 4267 C CA . ARG B 1 252 ? 37.365 33.409 0.870 1.00 13.68 ? 253 ARG B CA 1 ATOM 4268 C C . ARG B 1 252 ? 38.588 33.098 1.712 1.00 15.47 ? 253 ARG B C 1 ATOM 4269 O O . ARG B 1 252 ? 39.712 33.364 1.292 1.00 16.26 ? 253 ARG B O 1 ATOM 4270 C CB . ARG B 1 252 ? 36.986 34.861 1.079 1.00 15.07 ? 253 ARG B CB 1 ATOM 4271 C CG . ARG B 1 252 ? 36.112 35.428 0.002 1.00 14.43 ? 253 ARG B CG 1 ATOM 4272 C CD . ARG B 1 252 ? 35.502 36.692 0.486 1.00 15.00 ? 253 ARG B CD 1 ATOM 4273 N NE . ARG B 1 252 ? 34.608 36.481 1.621 1.00 15.85 ? 253 ARG B NE 1 ATOM 4274 C CZ . ARG B 1 252 ? 33.711 37.388 2.016 1.00 19.48 ? 253 ARG B CZ 1 ATOM 4275 N NH1 . ARG B 1 252 ? 33.630 38.539 1.368 1.00 19.79 ? 253 ARG B NH1 1 ATOM 4276 N NH2 . ARG B 1 252 ? 32.860 37.149 3.017 1.00 16.74 ? 253 ARG B NH2 1 ATOM 4277 N N . THR B 1 253 ? 38.365 32.547 2.900 1.00 14.41 ? 254 THR B N 1 ATOM 4278 C CA . THR B 1 253 ? 39.449 32.260 3.828 1.00 13.19 ? 254 THR B CA 1 ATOM 4279 C C . THR B 1 253 ? 39.635 30.790 4.276 1.00 12.67 ? 254 THR B C 1 ATOM 4280 O O . THR B 1 253 ? 40.656 30.441 4.851 1.00 10.59 ? 254 THR B O 1 ATOM 4281 C CB . THR B 1 253 ? 39.258 33.157 5.078 1.00 14.01 ? 254 THR B CB 1 ATOM 4282 O OG1 . THR B 1 253 ? 37.909 33.030 5.536 1.00 14.11 ? 254 THR B OG1 1 ATOM 4283 C CG2 . THR B 1 253 ? 39.516 34.641 4.725 1.00 11.21 ? 254 THR B CG2 1 ATOM 4284 N N . ALA B 1 254 ? 38.688 29.917 3.953 1.00 12.34 ? 255 ALA B N 1 ATOM 4285 C CA . ALA B 1 254 ? 38.732 28.523 4.402 1.00 12.51 ? 255 ALA B CA 1 ATOM 4286 C C . ALA B 1 254 ? 39.928 27.684 3.976 1.00 11.59 ? 255 ALA B C 1 ATOM 4287 O O . ALA B 1 254 ? 40.404 26.843 4.745 1.00 11.63 ? 255 ALA B O 1 ATOM 4288 C CB . ALA B 1 254 ? 37.432 27.805 4.015 1.00 11.45 ? 255 ALA B CB 1 ATOM 4289 N N . CYS B 1 255 ? 40.373 27.843 2.743 1.00 12.12 ? 256 CYS B N 1 ATOM 4290 C CA . CYS B 1 255 ? 41.487 27.044 2.291 1.00 13.32 ? 256 CYS B CA 1 ATOM 4291 C C . CYS B 1 255 ? 42.779 27.431 3.019 1.00 12.82 ? 256 CYS B C 1 ATOM 4292 O O . CYS B 1 255 ? 43.541 26.557 3.433 1.00 13.03 ? 256 CYS B O 1 ATOM 4293 C CB . CYS B 1 255 ? 41.597 27.099 0.770 1.00 14.00 ? 256 CYS B CB 1 ATOM 4294 S SG . CYS B 1 255 ? 40.108 26.381 -0.016 1.00 19.05 ? 256 CYS B SG 1 ATOM 4295 N N . ARG B 1 256 ? 42.988 28.721 3.251 1.00 11.92 ? 257 ARG B N 1 ATOM 4296 C CA . ARG B 1 256 ? 44.173 29.160 3.975 1.00 13.01 ? 257 ARG B CA 1 ATOM 4297 C C . ARG B 1 256 ? 44.077 28.637 5.393 1.00 12.98 ? 257 ARG B C 1 ATOM 4298 O O . ARG B 1 256 ? 45.051 28.104 5.907 1.00 12.57 ? 257 ARG B O 1 ATOM 4299 C CB . ARG B 1 256 ? 44.292 30.691 4.008 1.00 13.56 ? 257 ARG B CB 1 ATOM 4300 C CG . ARG B 1 256 ? 45.615 31.232 4.619 1.00 17.77 ? 257 ARG B CG 1 ATOM 4301 C CD . ARG B 1 256 ? 46.896 30.779 3.854 1.00 16.56 ? 257 ARG B CD 1 ATOM 4302 N NE . ARG B 1 256 ? 48.069 31.606 4.185 1.00 17.36 ? 257 ARG B NE 1 ATOM 4303 C CZ . ARG B 1 256 ? 49.113 31.809 3.370 1.00 17.24 ? 257 ARG B CZ 1 ATOM 4304 N NH1 . ARG B 1 256 ? 49.164 31.237 2.165 1.00 18.46 ? 257 ARG B NH1 1 ATOM 4305 N NH2 . ARG B 1 256 ? 50.085 32.648 3.706 1.00 16.20 ? 257 ARG B NH2 1 ATOM 4306 N N . TRP B 1 257 ? 42.910 28.778 6.027 1.00 11.24 ? 258 TRP B N 1 ATOM 4307 C CA . TRP B 1 257 ? 42.712 28.324 7.423 1.00 10.93 ? 258 TRP B CA 1 ATOM 4308 C C . TRP B 1 257 ? 43.041 26.833 7.575 1.00 11.86 ? 258 TRP B C 1 ATOM 4309 O O . TRP B 1 257 ? 43.688 26.398 8.552 1.00 11.17 ? 258 TRP B O 1 ATOM 4310 C CB . TRP B 1 257 ? 41.247 28.557 7.837 1.00 8.66 ? 258 TRP B CB 1 ATOM 4311 C CG . TRP B 1 257 ? 40.981 28.573 9.317 1.00 9.09 ? 258 TRP B CG 1 ATOM 4312 C CD1 . TRP B 1 257 ? 40.807 27.506 10.141 1.00 8.74 ? 258 TRP B CD1 1 ATOM 4313 C CD2 . TRP B 1 257 ? 40.824 29.738 10.130 1.00 10.48 ? 258 TRP B CD2 1 ATOM 4314 N NE1 . TRP B 1 257 ? 40.550 27.927 11.429 1.00 7.51 ? 258 TRP B NE1 1 ATOM 4315 C CE2 . TRP B 1 257 ? 40.555 29.294 11.453 1.00 6.83 ? 258 TRP B CE2 1 ATOM 4316 C CE3 . TRP B 1 257 ? 40.881 31.112 9.873 1.00 8.20 ? 258 TRP B CE3 1 ATOM 4317 C CZ2 . TRP B 1 257 ? 40.343 30.169 12.508 1.00 8.26 ? 258 TRP B CZ2 1 ATOM 4318 C CZ3 . TRP B 1 257 ? 40.668 31.992 10.932 1.00 10.79 ? 258 TRP B CZ3 1 ATOM 4319 C CH2 . TRP B 1 257 ? 40.398 31.513 12.236 1.00 9.79 ? 258 TRP B CH2 1 ATOM 4320 N N . GLN B 1 258 ? 42.564 26.066 6.599 1.00 14.46 ? 259 GLN B N 1 ATOM 4321 C CA . GLN B 1 258 ? 42.733 24.611 6.544 1.00 15.10 ? 259 GLN B CA 1 ATOM 4322 C C . GLN B 1 258 ? 44.197 24.223 6.361 1.00 14.06 ? 259 GLN B C 1 ATOM 4323 O O . GLN B 1 258 ? 44.684 23.278 7.026 1.00 15.90 ? 259 GLN B O 1 ATOM 4324 C CB . GLN B 1 258 ? 41.873 24.007 5.415 1.00 14.55 ? 259 GLN B CB 1 ATOM 4325 C CG . GLN B 1 258 ? 41.978 22.489 5.316 1.00 15.64 ? 259 GLN B CG 1 ATOM 4326 C CD . GLN B 1 258 ? 40.990 21.914 4.322 1.00 16.41 ? 259 GLN B CD 1 ATOM 4327 O OE1 . GLN B 1 258 ? 39.795 21.944 4.559 1.00 18.78 ? 259 GLN B OE1 1 ATOM 4328 N NE2 . GLN B 1 258 ? 41.485 21.396 3.208 1.00 16.63 ? 259 GLN B NE2 1 ATOM 4329 N N . SER B 1 259 ? 44.910 24.954 5.497 1.00 14.96 ? 260 SER B N 1 ATOM 4330 C CA . SER B 1 259 ? 46.332 24.666 5.284 1.00 14.89 ? 260 SER B CA 1 ATOM 4331 C C . SER B 1 259 ? 47.190 25.004 6.507 1.00 15.90 ? 260 SER B C 1 ATOM 4332 O O . SER B 1 259 ? 48.336 24.604 6.590 1.00 17.21 ? 260 SER B O 1 ATOM 4333 C CB . SER B 1 259 ? 46.864 25.383 4.060 1.00 16.91 ? 260 SER B CB 1 ATOM 4334 O OG . SER B 1 259 ? 47.006 26.757 4.313 1.00 18.16 ? 260 SER B OG 1 ATOM 4335 N N . MET B 1 260 ? 46.620 25.699 7.483 1.00 16.03 ? 261 MET B N 1 ATOM 4336 C CA . MET B 1 260 ? 47.352 26.055 8.704 1.00 16.24 ? 261 MET B CA 1 ATOM 4337 C C . MET B 1 260 ? 47.215 24.972 9.760 1.00 16.10 ? 261 MET B C 1 ATOM 4338 O O . MET B 1 260 ? 47.814 25.084 10.817 1.00 19.82 ? 261 MET B O 1 ATOM 4339 C CB . MET B 1 260 ? 46.819 27.375 9.329 1.00 14.69 ? 261 MET B CB 1 ATOM 4340 C CG . MET B 1 260 ? 47.161 28.660 8.595 1.00 16.01 ? 261 MET B CG 1 ATOM 4341 S SD . MET B 1 260 ? 48.949 28.884 8.552 1.00 15.89 ? 261 MET B SD 1 ATOM 4342 C CE . MET B 1 260 ? 49.117 30.661 8.943 1.00 14.12 ? 261 MET B CE 1 ATOM 4343 N N . THR B 1 261 ? 46.467 23.906 9.497 1.00 13.86 ? 262 THR B N 1 ATOM 4344 C CA . THR B 1 261 ? 46.264 22.918 10.558 1.00 12.13 ? 262 THR B CA 1 ATOM 4345 C C . THR B 1 261 ? 47.359 21.897 10.770 1.00 12.99 ? 262 THR B C 1 ATOM 4346 O O . THR B 1 261 ? 47.596 21.468 11.909 1.00 14.47 ? 262 THR B O 1 ATOM 4347 C CB . THR B 1 261 ? 44.942 22.108 10.332 1.00 11.79 ? 262 THR B CB 1 ATOM 4348 O OG1 . THR B 1 261 ? 44.988 21.486 9.037 1.00 11.34 ? 262 THR B OG1 1 ATOM 4349 C CG2 . THR B 1 261 ? 43.715 23.015 10.406 1.00 11.77 ? 262 THR B CG2 1 ATOM 4350 N N . SER B 1 262 ? 48.009 21.508 9.676 1.00 13.85 ? 263 SER B N 1 ATOM 4351 C CA . SER B 1 262 ? 48.988 20.427 9.698 1.00 17.83 ? 263 SER B CA 1 ATOM 4352 C C . SER B 1 262 ? 50.460 20.691 10.032 1.00 17.84 ? 263 SER B C 1 ATOM 4353 O O . SER B 1 262 ? 51.177 19.761 10.422 1.00 20.89 ? 263 SER B O 1 ATOM 4354 C CB . SER B 1 262 ? 48.893 19.652 8.372 1.00 16.92 ? 263 SER B CB 1 ATOM 4355 O OG . SER B 1 262 ? 48.883 20.559 7.274 1.00 23.79 ? 263 SER B OG 1 ATOM 4356 N N . SER B 1 263 ? 50.927 21.922 9.918 1.00 16.37 ? 264 SER B N 1 ATOM 4357 C CA . SER B 1 263 ? 52.340 22.160 10.190 1.00 14.97 ? 264 SER B CA 1 ATOM 4358 C C . SER B 1 263 ? 52.590 23.407 11.009 1.00 13.68 ? 264 SER B C 1 ATOM 4359 O O . SER B 1 263 ? 52.267 24.513 10.582 1.00 12.02 ? 264 SER B O 1 ATOM 4360 C CB . SER B 1 263 ? 53.087 22.237 8.847 1.00 15.37 ? 264 SER B CB 1 ATOM 4361 O OG . SER B 1 263 ? 54.323 22.927 8.960 1.00 19.42 ? 264 SER B OG 1 ATOM 4362 N N . ASN B 1 264 ? 53.117 23.212 12.207 1.00 12.52 ? 265 ASN B N 1 ATOM 4363 C CA . ASN B 1 264 ? 53.459 24.326 13.079 1.00 16.08 ? 265 ASN B CA 1 ATOM 4364 C C . ASN B 1 264 ? 54.526 25.207 12.420 1.00 18.30 ? 265 ASN B C 1 ATOM 4365 O O . ASN B 1 264 ? 54.575 26.430 12.633 1.00 17.79 ? 265 ASN B O 1 ATOM 4366 C CB . ASN B 1 264 ? 54.005 23.805 14.406 1.00 15.91 ? 265 ASN B CB 1 ATOM 4367 C CG . ASN B 1 264 ? 52.948 23.124 15.251 1.00 17.88 ? 265 ASN B CG 1 ATOM 4368 O OD1 . ASN B 1 264 ? 51.861 23.647 15.444 1.00 17.63 ? 265 ASN B OD1 1 ATOM 4369 N ND2 . ASN B 1 264 ? 53.267 21.958 15.758 1.00 17.77 ? 265 ASN B ND2 1 ATOM 4370 N N . GLU B 1 265 ? 55.387 24.570 11.626 1.00 19.98 ? 266 GLU B N 1 ATOM 4371 C CA . GLU B 1 265 ? 56.475 25.261 10.950 1.00 22.03 ? 266 GLU B CA 1 ATOM 4372 C C . GLU B 1 265 ? 55.944 26.228 9.913 1.00 18.45 ? 266 GLU B C 1 ATOM 4373 O O . GLU B 1 265 ? 56.334 27.390 9.885 1.00 16.01 ? 266 GLU B O 1 ATOM 4374 C CB . GLU B 1 265 ? 57.406 24.231 10.312 1.00 27.35 ? 266 GLU B CB 1 ATOM 4375 C CG . GLU B 1 265 ? 58.353 24.757 9.272 1.00 36.99 ? 266 GLU B CG 1 ATOM 4376 C CD . GLU B 1 265 ? 58.600 23.709 8.195 1.00 44.41 ? 266 GLU B CD 1 ATOM 4377 O OE1 . GLU B 1 265 ? 59.433 22.789 8.422 1.00 47.81 ? 266 GLU B OE1 1 ATOM 4378 O OE2 . GLU B 1 265 ? 57.922 23.778 7.134 1.00 47.21 ? 266 GLU B OE2 1 ATOM 4379 N N . VAL B 1 266 ? 55.067 25.748 9.051 1.00 16.85 ? 267 VAL B N 1 ATOM 4380 C CA . VAL B 1 266 ? 54.480 26.606 8.029 1.00 17.93 ? 267 VAL B CA 1 ATOM 4381 C C . VAL B 1 266 ? 53.632 27.730 8.647 1.00 16.00 ? 267 VAL B C 1 ATOM 4382 O O . VAL B 1 266 ? 53.627 28.856 8.152 1.00 15.59 ? 267 VAL B O 1 ATOM 4383 C CB . VAL B 1 266 ? 53.629 25.784 7.060 1.00 21.51 ? 267 VAL B CB 1 ATOM 4384 C CG1 . VAL B 1 266 ? 52.786 26.710 6.178 1.00 25.08 ? 267 VAL B CG1 1 ATOM 4385 C CG2 . VAL B 1 266 ? 54.540 24.870 6.209 1.00 22.00 ? 267 VAL B CG2 1 ATOM 4386 N N . MET B 1 267 ? 52.925 27.432 9.725 1.00 14.68 ? 268 MET B N 1 ATOM 4387 C CA . MET B 1 267 ? 52.120 28.454 10.396 1.00 14.71 ? 268 MET B CA 1 ATOM 4388 C C . MET B 1 267 ? 53.072 29.551 10.920 1.00 14.95 ? 268 MET B C 1 ATOM 4389 O O . MET B 1 267 ? 52.845 30.751 10.709 1.00 12.60 ? 268 MET B O 1 ATOM 4390 C CB . MET B 1 267 ? 51.357 27.832 11.578 1.00 14.66 ? 268 MET B CB 1 ATOM 4391 C CG . MET B 1 267 ? 50.593 28.861 12.444 1.00 12.14 ? 268 MET B CG 1 ATOM 4392 S SD . MET B 1 267 ? 49.942 28.249 13.975 1.00 14.62 ? 268 MET B SD 1 ATOM 4393 C CE . MET B 1 267 ? 51.392 27.942 14.844 1.00 15.92 ? 268 MET B CE 1 ATOM 4394 N N . GLY B 1 268 ? 54.128 29.120 11.615 1.00 14.87 ? 269 GLY B N 1 ATOM 4395 C CA . GLY B 1 268 ? 55.108 30.052 12.167 1.00 14.47 ? 269 GLY B CA 1 ATOM 4396 C C . GLY B 1 268 ? 55.749 30.946 11.115 1.00 14.77 ? 269 GLY B C 1 ATOM 4397 O O . GLY B 1 268 ? 55.919 32.148 11.340 1.00 15.75 ? 269 GLY B O 1 ATOM 4398 N N . GLN B 1 269 ? 56.123 30.363 9.978 1.00 16.23 ? 270 GLN B N 1 ATOM 4399 C CA . GLN B 1 269 ? 56.712 31.114 8.890 1.00 16.61 ? 270 GLN B CA 1 ATOM 4400 C C . GLN B 1 269 ? 55.773 32.216 8.452 1.00 15.24 ? 270 GLN B C 1 ATOM 4401 O O . GLN B 1 269 ? 56.178 33.360 8.308 1.00 15.50 ? 270 GLN B O 1 ATOM 4402 C CB . GLN B 1 269 ? 56.897 30.243 7.660 1.00 21.61 ? 270 GLN B CB 1 ATOM 4403 C CG . GLN B 1 269 ? 58.119 29.367 7.588 1.00 32.79 ? 270 GLN B CG 1 ATOM 4404 C CD . GLN B 1 269 ? 58.134 28.570 6.263 1.00 37.88 ? 270 GLN B CD 1 ATOM 4405 O OE1 . GLN B 1 269 ? 58.412 29.118 5.182 1.00 42.44 ? 270 GLN B OE1 1 ATOM 4406 N NE2 . GLN B 1 269 ? 57.781 27.293 6.339 1.00 40.49 ? 270 GLN B NE2 1 ATOM 4407 N N . ARG B 1 270 ? 54.530 31.847 8.158 1.00 14.35 ? 271 ARG B N 1 ATOM 4408 C CA . ARG B 1 270 ? 53.521 32.796 7.671 1.00 12.73 ? 271 ARG B CA 1 ATOM 4409 C C . ARG B 1 270 ? 53.206 33.884 8.685 1.00 10.49 ? 271 ARG B C 1 ATOM 4410 O O . ARG B 1 270 ? 53.108 35.049 8.337 1.00 13.92 ? 271 ARG B O 1 ATOM 4411 C CB . ARG B 1 270 ? 52.260 32.052 7.188 1.00 12.29 ? 271 ARG B CB 1 ATOM 4412 C CG . ARG B 1 270 ? 52.653 30.903 6.286 1.00 16.11 ? 271 ARG B CG 1 ATOM 4413 C CD . ARG B 1 270 ? 51.702 30.512 5.183 1.00 22.20 ? 271 ARG B CD 1 ATOM 4414 N NE . ARG B 1 270 ? 50.636 29.612 5.589 1.00 26.12 ? 271 ARG B NE 1 ATOM 4415 C CZ . ARG B 1 270 ? 50.185 28.560 4.887 1.00 26.86 ? 271 ARG B CZ 1 ATOM 4416 N NH1 . ARG B 1 270 ? 50.703 28.204 3.715 1.00 25.12 ? 271 ARG B NH1 1 ATOM 4417 N NH2 . ARG B 1 270 ? 49.135 27.901 5.344 1.00 26.75 ? 271 ARG B NH2 1 ATOM 4418 N N . TYR B 1 271 ? 53.101 33.526 9.947 1.00 10.00 ? 272 TYR B N 1 ATOM 4419 C CA . TYR B 1 271 ? 52.828 34.521 10.962 1.00 12.11 ? 272 TYR B CA 1 ATOM 4420 C C . TYR B 1 271 ? 53.944 35.548 11.074 1.00 13.34 ? 272 TYR B C 1 ATOM 4421 O O . TYR B 1 271 ? 53.678 36.732 11.252 1.00 13.21 ? 272 TYR B O 1 ATOM 4422 C CB . TYR B 1 271 ? 52.661 33.845 12.307 1.00 11.66 ? 272 TYR B CB 1 ATOM 4423 C CG . TYR B 1 271 ? 52.464 34.803 13.458 1.00 10.81 ? 272 TYR B CG 1 ATOM 4424 C CD1 . TYR B 1 271 ? 53.430 34.901 14.473 1.00 10.10 ? 272 TYR B CD1 1 ATOM 4425 C CD2 . TYR B 1 271 ? 51.268 35.515 13.595 1.00 10.24 ? 272 TYR B CD2 1 ATOM 4426 C CE1 . TYR B 1 271 ? 53.204 35.661 15.602 1.00 10.02 ? 272 TYR B CE1 1 ATOM 4427 C CE2 . TYR B 1 271 ? 51.029 36.275 14.709 1.00 9.75 ? 272 TYR B CE2 1 ATOM 4428 C CZ . TYR B 1 271 ? 51.992 36.339 15.716 1.00 10.61 ? 272 TYR B CZ 1 ATOM 4429 O OH . TYR B 1 271 ? 51.729 37.009 16.877 1.00 13.26 ? 272 TYR B OH 1 ATOM 4430 N N . ARG B 1 272 ? 55.189 35.078 11.039 1.00 14.53 ? 273 ARG B N 1 ATOM 4431 C CA . ARG B 1 272 ? 56.340 35.965 11.156 1.00 15.61 ? 273 ARG B CA 1 ATOM 4432 C C . ARG B 1 272 ? 56.358 36.987 10.043 1.00 13.75 ? 273 ARG B C 1 ATOM 4433 O O . ARG B 1 272 ? 56.637 38.162 10.278 1.00 16.12 ? 273 ARG B O 1 ATOM 4434 C CB . ARG B 1 272 ? 57.652 35.168 11.153 1.00 17.87 ? 273 ARG B CB 1 ATOM 4435 C CG . ARG B 1 272 ? 58.924 36.023 11.241 1.00 19.05 ? 273 ARG B CG 1 ATOM 4436 C CD . ARG B 1 272 ? 60.166 35.184 11.042 1.00 22.13 ? 273 ARG B CD 1 ATOM 4437 N NE . ARG B 1 272 ? 61.395 35.908 11.367 1.00 24.50 ? 273 ARG B NE 1 ATOM 4438 C CZ . ARG B 1 272 ? 61.956 36.838 10.591 1.00 24.27 ? 273 ARG B CZ 1 ATOM 4439 N NH1 . ARG B 1 272 ? 61.421 37.171 9.435 1.00 26.19 ? 273 ARG B NH1 1 ATOM 4440 N NH2 . ARG B 1 272 ? 63.024 37.486 11.001 1.00 26.15 ? 273 ARG B NH2 1 ATOM 4441 N N . ALA B 1 273 ? 56.058 36.544 8.828 1.00 14.85 ? 274 ALA B N 1 ATOM 4442 C CA . ALA B 1 273 ? 56.049 37.440 7.673 1.00 13.64 ? 274 ALA B CA 1 ATOM 4443 C C . ALA B 1 273 ? 54.957 38.511 7.773 1.00 14.80 ? 274 ALA B C 1 ATOM 4444 O O . ALA B 1 273 ? 55.206 39.691 7.512 1.00 14.11 ? 274 ALA B O 1 ATOM 4445 C CB . ALA B 1 273 ? 55.916 36.650 6.371 1.00 12.88 ? 274 ALA B CB 1 ATOM 4446 N N . ALA B 1 274 ? 53.751 38.103 8.171 1.00 14.34 ? 275 ALA B N 1 ATOM 4447 C CA . ALA B 1 274 ? 52.643 39.055 8.298 1.00 13.56 ? 275 ALA B CA 1 ATOM 4448 C C . ALA B 1 274 ? 52.924 40.012 9.454 1.00 12.30 ? 275 ALA B C 1 ATOM 4449 O O . ALA B 1 274 ? 52.611 41.204 9.373 1.00 13.88 ? 275 ALA B O 1 ATOM 4450 C CB . ALA B 1 274 ? 51.295 38.317 8.490 1.00 10.51 ? 275 ALA B CB 1 ATOM 4451 N N . MET B 1 275 ? 53.504 39.507 10.533 1.00 12.45 ? 276 MET B N 1 ATOM 4452 C CA . MET B 1 275 ? 53.823 40.389 11.664 1.00 13.76 ? 276 MET B CA 1 ATOM 4453 C C . MET B 1 275 ? 54.881 41.440 11.250 1.00 14.37 ? 276 MET B C 1 ATOM 4454 O O . MET B 1 275 ? 54.792 42.597 11.663 1.00 13.67 ? 276 MET B O 1 ATOM 4455 C CB . MET B 1 275 ? 54.323 39.599 12.893 1.00 12.52 ? 276 MET B CB 1 ATOM 4456 C CG . MET B 1 275 ? 53.257 38.807 13.641 1.00 15.51 ? 276 MET B CG 1 ATOM 4457 S SD . MET B 1 275 ? 51.955 39.852 14.349 1.00 14.67 ? 276 MET B SD 1 ATOM 4458 C CE . MET B 1 275 ? 52.687 40.383 15.845 1.00 11.93 ? 276 MET B CE 1 ATOM 4459 N N . ALA B 1 276 ? 55.880 41.037 10.449 1.00 13.92 ? 277 ALA B N 1 ATOM 4460 C CA . ALA B 1 276 ? 56.938 41.959 9.997 1.00 13.73 ? 277 ALA B CA 1 ATOM 4461 C C . ALA B 1 276 ? 56.287 43.070 9.208 1.00 15.29 ? 277 ALA B C 1 ATOM 4462 O O . ALA B 1 276 ? 56.639 44.240 9.338 1.00 17.50 ? 277 ALA B O 1 ATOM 4463 C CB . ALA B 1 276 ? 57.953 41.237 9.149 1.00 11.07 ? 277 ALA B CB 1 ATOM 4464 N N . LYS B 1 277 ? 55.298 42.698 8.415 1.00 16.25 ? 278 LYS B N 1 ATOM 4465 C CA . LYS B 1 277 ? 54.554 43.640 7.591 1.00 16.37 ? 278 LYS B CA 1 ATOM 4466 C C . LYS B 1 277 ? 53.738 44.608 8.447 1.00 16.70 ? 278 LYS B C 1 ATOM 4467 O O . LYS B 1 277 ? 53.759 45.811 8.213 1.00 15.92 ? 278 LYS B O 1 ATOM 4468 C CB . LYS B 1 277 ? 53.668 42.836 6.647 1.00 19.27 ? 278 LYS B CB 1 ATOM 4469 C CG . LYS B 1 277 ? 52.761 43.624 5.783 1.00 20.86 ? 278 LYS B CG 1 ATOM 4470 C CD . LYS B 1 277 ? 52.362 42.785 4.585 1.00 20.45 ? 278 LYS B CD 1 ATOM 4471 C CE . LYS B 1 277 ? 51.307 43.515 3.817 1.00 21.09 ? 278 LYS B CE 1 ATOM 4472 N NZ . LYS B 1 277 ? 50.973 42.829 2.560 1.00 26.48 ? 278 LYS B NZ 1 ATOM 4473 N N . MET B 1 278 ? 53.057 44.078 9.458 1.00 14.32 ? 279 MET B N 1 ATOM 4474 C CA . MET B 1 278 ? 52.244 44.872 10.354 1.00 14.27 ? 279 MET B CA 1 ATOM 4475 C C . MET B 1 278 ? 53.102 45.794 11.211 1.00 16.84 ? 279 MET B C 1 ATOM 4476 O O . MET B 1 278 ? 52.676 46.906 11.548 1.00 16.11 ? 279 MET B O 1 ATOM 4477 C CB . MET B 1 278 ? 51.408 43.962 11.262 1.00 13.15 ? 279 MET B CB 1 ATOM 4478 C CG . MET B 1 278 ? 50.531 44.699 12.264 1.00 14.32 ? 279 MET B CG 1 ATOM 4479 S SD . MET B 1 278 ? 49.199 43.693 12.986 1.00 16.43 ? 279 MET B SD 1 ATOM 4480 C CE . MET B 1 278 ? 49.958 43.229 14.451 1.00 10.86 ? 279 MET B CE 1 ATOM 4481 N N . SER B 1 279 ? 54.320 45.354 11.532 1.00 17.34 ? 280 SER B N 1 ATOM 4482 C CA . SER B 1 279 ? 55.240 46.124 12.381 1.00 16.03 ? 280 SER B CA 1 ATOM 4483 C C . SER B 1 279 ? 55.652 47.472 11.789 1.00 14.70 ? 280 SER B C 1 ATOM 4484 O O . SER B 1 279 ? 56.112 48.344 12.507 1.00 16.53 ? 280 SER B O 1 ATOM 4485 C CB . SER B 1 279 ? 56.526 45.330 12.686 1.00 15.35 ? 280 SER B CB 1 ATOM 4486 O OG . SER B 1 279 ? 57.333 45.191 11.506 1.00 14.38 ? 280 SER B OG 1 ATOM 4487 N N . VAL B 1 280 ? 55.536 47.632 10.487 1.00 13.93 ? 281 VAL B N 1 ATOM 4488 C CA . VAL B 1 280 ? 55.947 48.886 9.894 1.00 16.23 ? 281 VAL B CA 1 ATOM 4489 C C . VAL B 1 280 ? 54.819 49.645 9.201 1.00 17.07 ? 281 VAL B C 1 ATOM 4490 O O . VAL B 1 280 ? 55.080 50.416 8.275 1.00 16.64 ? 281 VAL B O 1 ATOM 4491 C CB . VAL B 1 280 ? 57.122 48.669 8.909 1.00 17.17 ? 281 VAL B CB 1 ATOM 4492 C CG1 . VAL B 1 280 ? 58.346 48.131 9.658 1.00 17.31 ? 281 VAL B CG1 1 ATOM 4493 C CG2 . VAL B 1 280 ? 56.704 47.715 7.807 1.00 16.03 ? 281 VAL B CG2 1 ATOM 4494 N N . LEU B 1 281 ? 53.570 49.417 9.604 1.00 16.37 ? 282 LEU B N 1 ATOM 4495 C CA . LEU B 1 281 ? 52.462 50.165 8.993 1.00 16.74 ? 282 LEU B CA 1 ATOM 4496 C C . LEU B 1 281 ? 52.653 51.600 9.469 1.00 16.65 ? 282 LEU B C 1 ATOM 4497 O O . LEU B 1 281 ? 52.832 51.847 10.670 1.00 15.24 ? 282 LEU B O 1 ATOM 4498 C CB . LEU B 1 281 ? 51.105 49.651 9.463 1.00 16.96 ? 282 LEU B CB 1 ATOM 4499 C CG . LEU B 1 281 ? 50.595 48.300 8.933 1.00 17.94 ? 282 LEU B CG 1 ATOM 4500 C CD1 . LEU B 1 281 ? 49.319 47.902 9.678 1.00 18.05 ? 282 LEU B CD1 1 ATOM 4501 C CD2 . LEU B 1 281 ? 50.342 48.361 7.445 1.00 16.19 ? 282 LEU B CD2 1 ATOM 4502 N N . GLY B 1 282 ? 52.690 52.526 8.511 1.00 18.83 ? 283 GLY B N 1 ATOM 4503 C CA . GLY B 1 282 ? 52.902 53.925 8.819 1.00 19.30 ? 283 GLY B CA 1 ATOM 4504 C C . GLY B 1 282 ? 54.375 54.316 8.828 1.00 21.69 ? 283 GLY B C 1 ATOM 4505 O O . GLY B 1 282 ? 54.707 55.456 9.223 1.00 22.01 ? 283 GLY B O 1 ATOM 4506 N N . PHE B 1 283 ? 55.254 53.396 8.409 1.00 20.16 ? 284 PHE B N 1 ATOM 4507 C CA . PHE B 1 283 ? 56.699 53.635 8.373 1.00 20.31 ? 284 PHE B CA 1 ATOM 4508 C C . PHE B 1 283 ? 57.354 53.067 7.112 1.00 23.13 ? 284 PHE B C 1 ATOM 4509 O O . PHE B 1 283 ? 56.732 52.313 6.346 1.00 23.52 ? 284 PHE B O 1 ATOM 4510 C CB . PHE B 1 283 ? 57.391 53.064 9.621 1.00 16.94 ? 284 PHE B CB 1 ATOM 4511 C CG . PHE B 1 283 ? 56.924 53.689 10.888 1.00 16.91 ? 284 PHE B CG 1 ATOM 4512 C CD1 . PHE B 1 283 ? 57.565 54.802 11.407 1.00 15.33 ? 284 PHE B CD1 1 ATOM 4513 C CD2 . PHE B 1 283 ? 55.786 53.214 11.533 1.00 15.69 ? 284 PHE B CD2 1 ATOM 4514 C CE1 . PHE B 1 283 ? 57.071 55.450 12.562 1.00 15.26 ? 284 PHE B CE1 1 ATOM 4515 C CE2 . PHE B 1 283 ? 55.291 53.850 12.674 1.00 16.52 ? 284 PHE B CE2 1 ATOM 4516 C CZ . PHE B 1 283 ? 55.929 54.967 13.192 1.00 16.38 ? 284 PHE B CZ 1 ATOM 4517 N N . ASP B 1 284 ? 58.601 53.488 6.885 1.00 25.42 ? 285 ASP B N 1 ATOM 4518 C CA . ASP B 1 284 ? 59.421 53.050 5.758 1.00 26.40 ? 285 ASP B CA 1 ATOM 4519 C C . ASP B 1 284 ? 60.435 52.132 6.423 1.00 26.25 ? 285 ASP B C 1 ATOM 4520 O O . ASP B 1 284 ? 61.279 52.600 7.183 1.00 23.09 ? 285 ASP B O 1 ATOM 4521 C CB . ASP B 1 284 ? 60.136 54.267 5.172 1.00 31.33 ? 285 ASP B CB 1 ATOM 4522 C CG . ASP B 1 284 ? 60.988 53.941 3.949 1.00 36.30 ? 285 ASP B CG 1 ATOM 4523 O OD1 . ASP B 1 284 ? 61.451 54.926 3.322 1.00 40.50 ? 285 ASP B OD1 1 ATOM 4524 O OD2 . ASP B 1 284 ? 61.189 52.745 3.610 1.00 35.45 ? 285 ASP B OD2 1 ATOM 4525 N N . ARG B 1 285 ? 60.347 50.826 6.186 1.00 27.02 ? 286 ARG B N 1 ATOM 4526 C CA . ARG B 1 285 ? 61.296 49.933 6.855 1.00 29.17 ? 286 ARG B CA 1 ATOM 4527 C C . ARG B 1 285 ? 62.745 50.216 6.501 1.00 29.70 ? 286 ARG B C 1 ATOM 4528 O O . ARG B 1 285 ? 63.632 49.941 7.295 1.00 31.28 ? 286 ARG B O 1 ATOM 4529 C CB . ARG B 1 285 ? 60.958 48.451 6.662 1.00 29.43 ? 286 ARG B CB 1 ATOM 4530 C CG . ARG B 1 285 ? 60.863 48.000 5.252 1.00 29.89 ? 286 ARG B CG 1 ATOM 4531 C CD . ARG B 1 285 ? 60.634 46.514 5.234 1.00 31.99 ? 286 ARG B CD 1 ATOM 4532 N NE . ARG B 1 285 ? 61.791 45.768 5.737 1.00 34.34 ? 286 ARG B NE 1 ATOM 4533 C CZ . ARG B 1 285 ? 61.757 44.847 6.707 1.00 34.07 ? 286 ARG B CZ 1 ATOM 4534 N NH1 . ARG B 1 285 ? 60.621 44.537 7.320 1.00 33.17 ? 286 ARG B NH1 1 ATOM 4535 N NH2 . ARG B 1 285 ? 62.875 44.206 7.045 1.00 36.12 ? 286 ARG B NH2 1 ATOM 4536 N N . ASN B 1 286 ? 62.979 50.822 5.343 1.00 30.92 ? 287 ASN B N 1 ATOM 4537 C CA . ASN B 1 286 ? 64.342 51.159 4.934 1.00 32.21 ? 287 ASN B CA 1 ATOM 4538 C C . ASN B 1 286 ? 64.912 52.274 5.816 1.00 30.28 ? 287 ASN B C 1 ATOM 4539 O O . ASN B 1 286 ? 66.106 52.512 5.821 1.00 32.04 ? 287 ASN B O 1 ATOM 4540 C CB . ASN B 1 286 ? 64.378 51.587 3.456 1.00 36.48 ? 287 ASN B CB 1 ATOM 4541 C CG . ASN B 1 286 ? 63.773 50.536 2.529 1.00 41.33 ? 287 ASN B CG 1 ATOM 4542 O OD1 . ASN B 1 286 ? 64.170 49.365 2.555 1.00 44.01 ? 287 ASN B OD1 1 ATOM 4543 N ND2 . ASN B 1 286 ? 62.770 50.937 1.744 1.00 42.84 ? 287 ASN B ND2 1 ATOM 4544 N N . ALA B 1 287 ? 64.057 52.956 6.566 1.00 27.46 ? 288 ALA B N 1 ATOM 4545 C CA . ALA B 1 287 ? 64.518 54.032 7.442 1.00 26.78 ? 288 ALA B CA 1 ATOM 4546 C C . ALA B 1 287 ? 64.880 53.531 8.835 1.00 25.99 ? 288 ALA B C 1 ATOM 4547 O O . ALA B 1 287 ? 65.504 54.254 9.625 1.00 23.84 ? 288 ALA B O 1 ATOM 4548 C CB . ALA B 1 287 ? 63.447 55.102 7.553 1.00 27.42 ? 288 ALA B CB 1 ATOM 4549 N N . LEU B 1 288 ? 64.502 52.283 9.113 1.00 23.78 ? 289 LEU B N 1 ATOM 4550 C CA . LEU B 1 288 ? 64.716 51.663 10.410 1.00 20.50 ? 289 LEU B CA 1 ATOM 4551 C C . LEU B 1 288 ? 65.964 50.804 10.447 1.00 18.80 ? 289 LEU B C 1 ATOM 4552 O O . LEU B 1 288 ? 66.464 50.401 9.417 1.00 20.09 ? 289 LEU B O 1 ATOM 4553 C CB . LEU B 1 288 ? 63.495 50.819 10.736 1.00 18.21 ? 289 LEU B CB 1 ATOM 4554 C CG . LEU B 1 288 ? 62.207 51.630 10.627 1.00 17.65 ? 289 LEU B CG 1 ATOM 4555 C CD1 . LEU B 1 288 ? 61.015 50.710 10.720 1.00 17.19 ? 289 LEU B CD1 1 ATOM 4556 C CD2 . LEU B 1 288 ? 62.140 52.630 11.747 1.00 14.28 ? 289 LEU B CD2 1 ATOM 4557 N N . THR B 1 289 ? 66.428 50.490 11.648 1.00 18.52 ? 290 THR B N 1 ATOM 4558 C CA . THR B 1 289 ? 67.621 49.679 11.842 1.00 18.98 ? 290 THR B CA 1 ATOM 4559 C C . THR B 1 289 ? 67.247 48.331 12.417 1.00 18.14 ? 290 THR B C 1 ATOM 4560 O O . THR B 1 289 ? 66.517 48.259 13.391 1.00 17.80 ? 290 THR B O 1 ATOM 4561 C CB . THR B 1 289 ? 68.565 50.390 12.791 1.00 19.61 ? 290 THR B CB 1 ATOM 4562 O OG1 . THR B 1 289 ? 69.055 51.559 12.132 1.00 22.30 ? 290 THR B OG1 1 ATOM 4563 C CG2 . THR B 1 289 ? 69.736 49.488 13.231 1.00 19.84 ? 290 THR B CG2 1 ATOM 4564 N N . ASP B 1 290 ? 67.804 47.275 11.835 1.00 19.26 ? 291 ASP B N 1 ATOM 4565 C CA . ASP B 1 290 ? 67.544 45.892 12.234 1.00 19.12 ? 291 ASP B CA 1 ATOM 4566 C C . ASP B 1 290 ? 68.309 45.445 13.477 1.00 18.65 ? 291 ASP B C 1 ATOM 4567 O O . ASP B 1 290 ? 69.548 45.333 13.468 1.00 20.20 ? 291 ASP B O 1 ATOM 4568 C CB . ASP B 1 290 ? 67.856 44.945 11.054 1.00 20.17 ? 291 ASP B CB 1 ATOM 4569 C CG . ASP B 1 290 ? 67.325 43.513 11.262 1.00 20.49 ? 291 ASP B CG 1 ATOM 4570 O OD1 . ASP B 1 290 ? 67.316 42.743 10.293 1.00 24.68 ? 291 ASP B OD1 1 ATOM 4571 O OD2 . ASP B 1 290 ? 66.907 43.143 12.362 1.00 19.25 ? 291 ASP B OD2 1 ATOM 4572 N N . CYS B 1 291 ? 67.562 45.176 14.541 1.00 14.55 ? 292 CYS B N 1 ATOM 4573 C CA . CYS B 1 291 ? 68.137 44.689 15.782 1.00 13.69 ? 292 CYS B CA 1 ATOM 4574 C C . CYS B 1 291 ? 67.536 43.318 16.114 1.00 12.80 ? 292 CYS B C 1 ATOM 4575 O O . CYS B 1 291 ? 67.395 42.961 17.280 1.00 12.18 ? 292 CYS B O 1 ATOM 4576 C CB . CYS B 1 291 ? 67.861 45.701 16.905 1.00 15.67 ? 292 CYS B CB 1 ATOM 4577 S SG . CYS B 1 291 ? 68.842 47.224 16.720 1.00 16.74 ? 292 CYS B SG 1 ATOM 4578 N N . SER B 1 292 ? 67.199 42.539 15.092 1.00 13.09 ? 293 SER B N 1 ATOM 4579 C CA . SER B 1 292 ? 66.596 41.225 15.317 1.00 13.28 ? 293 SER B CA 1 ATOM 4580 C C . SER B 1 292 ? 67.475 40.312 16.138 1.00 16.98 ? 293 SER B C 1 ATOM 4581 O O . SER B 1 292 ? 66.970 39.392 16.801 1.00 16.89 ? 293 SER B O 1 ATOM 4582 C CB . SER B 1 292 ? 66.295 40.557 14.005 1.00 12.98 ? 293 SER B CB 1 ATOM 4583 O OG . SER B 1 292 ? 65.376 41.334 13.270 1.00 10.42 ? 293 SER B OG 1 ATOM 4584 N N . ASP B 1 293 ? 68.781 40.590 16.162 1.00 19.35 ? 294 ASP B N 1 ATOM 4585 C CA . ASP B 1 293 ? 69.702 39.745 16.933 1.00 19.58 ? 294 ASP B CA 1 ATOM 4586 C C . ASP B 1 293 ? 69.517 39.815 18.441 1.00 19.46 ? 294 ASP B C 1 ATOM 4587 O O . ASP B 1 293 ? 69.975 38.941 19.169 1.00 19.41 ? 294 ASP B O 1 ATOM 4588 C CB . ASP B 1 293 ? 71.186 39.960 16.528 1.00 21.91 ? 294 ASP B CB 1 ATOM 4589 C CG . ASP B 1 293 ? 71.736 41.364 16.875 1.00 26.45 ? 294 ASP B CG 1 ATOM 4590 O OD1 . ASP B 1 293 ? 71.475 41.910 17.965 1.00 26.36 ? 294 ASP B OD1 1 ATOM 4591 O OD2 . ASP B 1 293 ? 72.522 41.898 16.072 1.00 31.45 ? 294 ASP B OD2 1 ATOM 4592 N N . VAL B 1 294 ? 68.809 40.818 18.931 1.00 18.05 ? 295 VAL B N 1 ATOM 4593 C CA . VAL B 1 294 ? 68.630 40.904 20.370 1.00 16.70 ? 295 VAL B CA 1 ATOM 4594 C C . VAL B 1 294 ? 67.559 39.918 20.838 1.00 16.67 ? 295 VAL B C 1 ATOM 4595 O O . VAL B 1 294 ? 67.505 39.544 22.013 1.00 15.57 ? 295 VAL B O 1 ATOM 4596 C CB . VAL B 1 294 ? 68.191 42.336 20.801 1.00 16.27 ? 295 VAL B CB 1 ATOM 4597 C CG1 . VAL B 1 294 ? 68.057 42.419 22.320 1.00 15.64 ? 295 VAL B CG1 1 ATOM 4598 C CG2 . VAL B 1 294 ? 69.180 43.382 20.276 1.00 17.00 ? 295 VAL B CG2 1 ATOM 4599 N N . ILE B 1 295 ? 66.727 39.468 19.909 1.00 16.18 ? 296 ILE B N 1 ATOM 4600 C CA . ILE B 1 295 ? 65.613 38.603 20.279 1.00 15.50 ? 296 ILE B CA 1 ATOM 4601 C C . ILE B 1 295 ? 66.000 37.136 20.574 1.00 14.88 ? 296 ILE B C 1 ATOM 4602 O O . ILE B 1 295 ? 66.623 36.491 19.757 1.00 13.46 ? 296 ILE B O 1 ATOM 4603 C CB . ILE B 1 295 ? 64.511 38.640 19.147 1.00 15.23 ? 296 ILE B CB 1 ATOM 4604 C CG1 . ILE B 1 295 ? 64.208 40.083 18.693 1.00 14.41 ? 296 ILE B CG1 1 ATOM 4605 C CG2 . ILE B 1 295 ? 63.251 37.906 19.606 1.00 16.74 ? 296 ILE B CG2 1 ATOM 4606 C CD1 . ILE B 1 295 ? 63.736 41.004 19.814 1.00 8.69 ? 296 ILE B CD1 1 ATOM 4607 N N . PRO B 1 296 ? 65.626 36.612 21.755 1.00 15.79 ? 297 PRO B N 1 ATOM 4608 C CA . PRO B 1 296 ? 65.903 35.235 22.166 1.00 17.66 ? 297 PRO B CA 1 ATOM 4609 C C . PRO B 1 296 ? 65.077 34.265 21.322 1.00 20.63 ? 297 PRO B C 1 ATOM 4610 O O . PRO B 1 296 ? 64.097 34.656 20.678 1.00 21.02 ? 297 PRO B O 1 ATOM 4611 C CB . PRO B 1 296 ? 65.390 35.197 23.600 1.00 16.82 ? 297 PRO B CB 1 ATOM 4612 C CG . PRO B 1 296 ? 65.475 36.587 24.054 1.00 17.62 ? 297 PRO B CG 1 ATOM 4613 C CD . PRO B 1 296 ? 65.037 37.370 22.869 1.00 16.66 ? 297 PRO B CD 1 ATOM 4614 N N . SER B 1 297 ? 65.462 32.992 21.352 1.00 21.51 ? 298 SER B N 1 ATOM 4615 C CA . SER B 1 297 ? 64.760 31.938 20.619 1.00 20.91 ? 298 SER B CA 1 ATOM 4616 C C . SER B 1 297 ? 63.830 31.263 21.600 1.00 17.93 ? 298 SER B C 1 ATOM 4617 O O . SER B 1 297 ? 64.122 31.214 22.789 1.00 17.76 ? 298 SER B O 1 ATOM 4618 C CB . SER B 1 297 ? 65.755 30.907 20.097 1.00 24.72 ? 298 SER B CB 1 ATOM 4619 O OG . SER B 1 297 ? 66.184 31.228 18.786 1.00 30.62 ? 298 SER B OG 1 ATOM 4620 N N . ALA B 1 298 ? 62.698 30.768 21.125 1.00 18.85 ? 299 ALA B N 1 ATOM 4621 C CA . ALA B 1 298 ? 61.744 30.090 22.014 1.00 17.82 ? 299 ALA B CA 1 ATOM 4622 C C . ALA B 1 298 ? 62.101 28.604 22.070 1.00 18.07 ? 299 ALA B C 1 ATOM 4623 O O . ALA B 1 298 ? 62.769 28.091 21.170 1.00 17.94 ? 299 ALA B O 1 ATOM 4624 C CB . ALA B 1 298 ? 60.326 30.243 21.470 1.00 18.10 ? 299 ALA B CB 1 ATOM 4625 N N . VAL B 1 299 ? 61.655 27.900 23.098 1.00 17.78 ? 300 VAL B N 1 ATOM 4626 C CA . VAL B 1 299 ? 61.932 26.478 23.128 1.00 19.89 ? 300 VAL B CA 1 ATOM 4627 C C . VAL B 1 299 ? 61.016 25.819 22.103 1.00 19.49 ? 300 VAL B C 1 ATOM 4628 O O . VAL B 1 299 ? 59.941 26.344 21.811 1.00 18.83 ? 300 VAL B O 1 ATOM 4629 C CB . VAL B 1 299 ? 61.723 25.859 24.522 1.00 20.50 ? 300 VAL B CB 1 ATOM 4630 C CG1 . VAL B 1 299 ? 62.597 26.561 25.540 1.00 20.95 ? 300 VAL B CG1 1 ATOM 4631 C CG2 . VAL B 1 299 ? 60.292 25.930 24.930 1.00 23.40 ? 300 VAL B CG2 1 ATOM 4632 N N . SER B 1 300 ? 61.469 24.712 21.516 1.00 20.20 ? 301 SER B N 1 ATOM 4633 C CA . SER B 1 300 ? 60.689 23.976 20.521 1.00 21.04 ? 301 SER B CA 1 ATOM 4634 C C . SER B 1 300 ? 59.456 23.285 21.084 1.00 19.44 ? 301 SER B C 1 ATOM 4635 O O . SER B 1 300 ? 59.428 22.846 22.232 1.00 19.75 ? 301 SER B O 1 ATOM 4636 C CB . SER B 1 300 ? 61.531 22.891 19.856 1.00 23.13 ? 301 SER B CB 1 ATOM 4637 O OG . SER B 1 300 ? 62.616 23.474 19.169 1.00 29.43 ? 301 SER B OG 1 ATOM 4638 N N . ASN B 1 301 ? 58.450 23.168 20.237 1.00 17.44 ? 302 ASN B N 1 ATOM 4639 C CA . ASN B 1 301 ? 57.246 22.485 20.605 1.00 16.26 ? 302 ASN B CA 1 ATOM 4640 C C . ASN B 1 301 ? 57.351 21.261 19.721 1.00 16.39 ? 302 ASN B C 1 ATOM 4641 O O . ASN B 1 301 ? 57.393 21.388 18.492 1.00 15.89 ? 302 ASN B O 1 ATOM 4642 C CB . ASN B 1 301 ? 56.005 23.315 20.235 1.00 15.28 ? 302 ASN B CB 1 ATOM 4643 C CG . ASN B 1 301 ? 54.750 22.456 20.064 1.00 15.42 ? 302 ASN B CG 1 ATOM 4644 O OD1 . ASN B 1 301 ? 53.963 22.669 19.148 1.00 18.29 ? 302 ASN B OD1 1 ATOM 4645 N ND2 . ASN B 1 301 ? 54.573 21.478 20.935 1.00 14.16 ? 302 ASN B ND2 1 ATOM 4646 N N . ASN B 1 302 ? 57.469 20.090 20.340 1.00 18.78 ? 303 ASN B N 1 ATOM 4647 C CA . ASN B 1 302 ? 57.567 18.837 19.584 1.00 19.99 ? 303 ASN B CA 1 ATOM 4648 C C . ASN B 1 302 ? 56.290 18.020 19.490 1.00 18.91 ? 303 ASN B C 1 ATOM 4649 O O . ASN B 1 302 ? 56.283 16.980 18.842 1.00 20.84 ? 303 ASN B O 1 ATOM 4650 C CB . ASN B 1 302 ? 58.691 17.961 20.121 1.00 21.84 ? 303 ASN B CB 1 ATOM 4651 C CG . ASN B 1 302 ? 60.045 18.553 19.851 1.00 24.04 ? 303 ASN B CG 1 ATOM 4652 O OD1 . ASN B 1 302 ? 60.319 19.010 18.733 1.00 26.02 ? 303 ASN B OD1 1 ATOM 4653 N ND2 . ASN B 1 302 ? 60.884 18.611 20.883 1.00 22.94 ? 303 ASN B ND2 1 ATOM 4654 N N . ALA B 1 303 ? 55.216 18.490 20.114 1.00 19.20 ? 304 ALA B N 1 ATOM 4655 C CA . ALA B 1 303 ? 53.944 17.794 20.049 1.00 17.76 ? 304 ALA B CA 1 ATOM 4656 C C . ALA B 1 303 ? 53.430 17.906 18.608 1.00 18.78 ? 304 ALA B C 1 ATOM 4657 O O . ALA B 1 303 ? 53.707 18.889 17.914 1.00 21.89 ? 304 ALA B O 1 ATOM 4658 C CB . ALA B 1 303 ? 52.967 18.423 21.008 1.00 17.26 ? 304 ALA B CB 1 ATOM 4659 N N . ALA B 1 304 ? 52.745 16.882 18.115 1.00 16.51 ? 305 ALA B N 1 ATOM 4660 C CA . ALA B 1 304 ? 52.223 16.945 16.757 1.00 16.33 ? 305 ALA B CA 1 ATOM 4661 C C . ALA B 1 304 ? 50.808 17.502 16.804 1.00 13.94 ? 305 ALA B C 1 ATOM 4662 O O . ALA B 1 304 ? 50.168 17.461 17.845 1.00 13.52 ? 305 ALA B O 1 ATOM 4663 C CB . ALA B 1 304 ? 52.171 15.540 16.139 1.00 15.57 ? 305 ALA B CB 1 ATOM 4664 N N . PRO B 1 305 ? 50.353 18.115 15.707 1.00 14.15 ? 306 PRO B N 1 ATOM 4665 C CA . PRO B 1 305 ? 48.985 18.646 15.666 1.00 14.36 ? 306 PRO B CA 1 ATOM 4666 C C . PRO B 1 305 ? 48.046 17.426 15.859 1.00 15.62 ? 306 PRO B C 1 ATOM 4667 O O . PRO B 1 305 ? 48.315 16.353 15.316 1.00 15.68 ? 306 PRO B O 1 ATOM 4668 C CB . PRO B 1 305 ? 48.886 19.191 14.241 1.00 13.53 ? 306 PRO B CB 1 ATOM 4669 C CG . PRO B 1 305 ? 50.274 19.747 13.999 1.00 14.11 ? 306 PRO B CG 1 ATOM 4670 C CD . PRO B 1 305 ? 51.132 18.590 14.542 1.00 14.68 ? 306 PRO B CD 1 ATOM 4671 N N . VAL B 1 306 ? 47.019 17.552 16.698 1.00 16.92 ? 307 VAL B N 1 ATOM 4672 C CA . VAL B 1 306 ? 46.073 16.447 16.933 1.00 18.99 ? 307 VAL B CA 1 ATOM 4673 C C . VAL B 1 306 ? 44.613 16.935 17.046 1.00 19.27 ? 307 VAL B C 1 ATOM 4674 O O . VAL B 1 306 ? 44.367 18.101 17.382 1.00 17.84 ? 307 VAL B O 1 ATOM 4675 C CB . VAL B 1 306 ? 46.353 15.718 18.280 1.00 19.00 ? 307 VAL B CB 1 ATOM 4676 C CG1 . VAL B 1 306 ? 47.699 15.034 18.248 1.00 23.63 ? 307 VAL B CG1 1 ATOM 4677 C CG2 . VAL B 1 306 ? 46.287 16.708 19.442 1.00 20.17 ? 307 VAL B CG2 1 ATOM 4678 N N . ILE B 1 307 ? 43.665 16.066 16.703 1.00 17.85 ? 308 ILE B N 1 ATOM 4679 C CA . ILE B 1 307 ? 42.247 16.373 16.865 1.00 17.14 ? 308 ILE B CA 1 ATOM 4680 C C . ILE B 1 307 ? 42.077 15.797 18.258 1.00 16.63 ? 308 ILE B C 1 ATOM 4681 O O . ILE B 1 307 ? 42.240 14.604 18.465 1.00 20.62 ? 308 ILE B O 1 ATOM 4682 C CB . ILE B 1 307 ? 41.379 15.657 15.829 1.00 16.46 ? 308 ILE B CB 1 ATOM 4683 C CG1 . ILE B 1 307 ? 41.769 16.156 14.446 1.00 15.30 ? 308 ILE B CG1 1 ATOM 4684 C CG2 . ILE B 1 307 ? 39.882 15.932 16.119 1.00 16.59 ? 308 ILE B CG2 1 ATOM 4685 C CD1 . ILE B 1 307 ? 40.918 15.652 13.317 1.00 19.12 ? 308 ILE B CD1 1 ATOM 4686 N N . PRO B 1 308 ? 41.809 16.642 19.248 1.00 18.57 ? 309 PRO B N 1 ATOM 4687 C CA . PRO B 1 308 ? 41.676 16.106 20.596 1.00 19.59 ? 309 PRO B CA 1 ATOM 4688 C C . PRO B 1 308 ? 40.407 15.420 21.090 1.00 21.38 ? 309 PRO B C 1 ATOM 4689 O O . PRO B 1 308 ? 39.372 15.427 20.443 1.00 22.08 ? 309 PRO B O 1 ATOM 4690 C CB . PRO B 1 308 ? 41.993 17.326 21.445 1.00 18.82 ? 309 PRO B CB 1 ATOM 4691 C CG . PRO B 1 308 ? 41.367 18.397 20.710 1.00 18.00 ? 309 PRO B CG 1 ATOM 4692 C CD . PRO B 1 308 ? 41.629 18.103 19.251 1.00 17.58 ? 309 PRO B CD 1 ATOM 4693 N N . GLY B 1 309 ? 40.567 14.749 22.226 1.00 22.11 ? 310 GLY B N 1 ATOM 4694 C CA . GLY B 1 309 ? 39.474 14.127 22.943 1.00 23.67 ? 310 GLY B CA 1 ATOM 4695 C C . GLY B 1 309 ? 38.476 13.206 22.314 1.00 24.38 ? 310 GLY B C 1 ATOM 4696 O O . GLY B 1 309 ? 37.312 13.229 22.677 1.00 24.84 ? 310 GLY B O 1 ATOM 4697 N N . GLY B 1 310 ? 38.921 12.371 21.396 1.00 25.13 ? 311 GLY B N 1 ATOM 4698 C CA . GLY B 1 310 ? 38.011 11.419 20.797 1.00 24.21 ? 311 GLY B CA 1 ATOM 4699 C C . GLY B 1 310 ? 37.303 11.913 19.565 1.00 25.35 ? 311 GLY B C 1 ATOM 4700 O O . GLY B 1 310 ? 36.495 11.182 18.992 1.00 26.87 ? 311 GLY B O 1 ATOM 4701 N N . LEU B 1 311 ? 37.577 13.141 19.149 1.00 21.65 ? 312 LEU B N 1 ATOM 4702 C CA . LEU B 1 311 ? 36.924 13.647 17.962 1.00 19.26 ? 312 LEU B CA 1 ATOM 4703 C C . LEU B 1 311 ? 37.769 13.213 16.773 1.00 18.30 ? 312 LEU B C 1 ATOM 4704 O O . LEU B 1 311 ? 38.963 12.886 16.916 1.00 19.45 ? 312 LEU B O 1 ATOM 4705 C CB . LEU B 1 311 ? 36.720 15.167 18.072 1.00 17.67 ? 312 LEU B CB 1 ATOM 4706 C CG . LEU B 1 311 ? 35.961 15.561 19.360 1.00 18.05 ? 312 LEU B CG 1 ATOM 4707 C CD1 . LEU B 1 311 ? 35.928 17.068 19.571 1.00 17.26 ? 312 LEU B CD1 1 ATOM 4708 C CD2 . LEU B 1 311 ? 34.532 15.017 19.296 1.00 15.92 ? 312 LEU B CD2 1 ATOM 4709 N N . THR B 1 312 ? 37.158 13.179 15.598 1.00 16.00 ? 313 THR B N 1 ATOM 4710 C CA . THR B 1 312 ? 37.858 12.740 14.400 1.00 14.44 ? 313 THR B CA 1 ATOM 4711 C C . THR B 1 312 ? 37.590 13.738 13.304 1.00 13.77 ? 313 THR B C 1 ATOM 4712 O O . THR B 1 312 ? 36.906 14.746 13.511 1.00 14.36 ? 313 THR B O 1 ATOM 4713 C CB . THR B 1 312 ? 37.316 11.362 13.912 1.00 15.31 ? 313 THR B CB 1 ATOM 4714 O OG1 . THR B 1 312 ? 36.014 11.547 13.369 1.00 16.97 ? 313 THR B OG1 1 ATOM 4715 C CG2 . THR B 1 312 ? 37.166 10.390 15.060 1.00 11.51 ? 313 THR B CG2 1 ATOM 4716 N N . VAL B 1 313 ? 38.063 13.418 12.110 1.00 14.21 ? 314 VAL B N 1 ATOM 4717 C CA . VAL B 1 313 ? 37.855 14.291 10.975 1.00 16.51 ? 314 VAL B CA 1 ATOM 4718 C C . VAL B 1 313 ? 36.372 14.395 10.620 1.00 16.53 ? 314 VAL B C 1 ATOM 4719 O O . VAL B 1 313 ? 35.986 15.287 9.873 1.00 15.56 ? 314 VAL B O 1 ATOM 4720 C CB . VAL B 1 313 ? 38.707 13.827 9.746 1.00 17.83 ? 314 VAL B CB 1 ATOM 4721 C CG1 . VAL B 1 313 ? 38.276 12.434 9.297 1.00 20.34 ? 314 VAL B CG1 1 ATOM 4722 C CG2 . VAL B 1 313 ? 38.608 14.840 8.582 1.00 18.32 ? 314 VAL B CG2 1 ATOM 4723 N N . ASP B 1 314 ? 35.548 13.470 11.134 1.00 16.20 ? 315 ASP B N 1 ATOM 4724 C CA . ASP B 1 314 ? 34.125 13.513 10.838 1.00 17.54 ? 315 ASP B CA 1 ATOM 4725 C C . ASP B 1 314 ? 33.525 14.669 11.595 1.00 17.90 ? 315 ASP B C 1 ATOM 4726 O O . ASP B 1 314 ? 32.430 15.121 11.262 1.00 17.53 ? 315 ASP B O 1 ATOM 4727 C CB . ASP B 1 314 ? 33.396 12.240 11.283 1.00 17.58 ? 315 ASP B CB 1 ATOM 4728 C CG . ASP B 1 314 ? 33.830 11.016 10.525 1.00 18.42 ? 315 ASP B CG 1 ATOM 4729 O OD1 . ASP B 1 314 ? 33.922 11.082 9.280 1.00 17.99 ? 315 ASP B OD1 1 ATOM 4730 O OD2 . ASP B 1 314 ? 34.083 9.989 11.193 1.00 20.86 ? 315 ASP B OD2 1 ATOM 4731 N N . ASP B 1 315 ? 34.214 15.091 12.658 1.00 17.84 ? 316 ASP B N 1 ATOM 4732 C CA . ASP B 1 315 ? 33.765 16.191 13.494 1.00 15.11 ? 316 ASP B CA 1 ATOM 4733 C C . ASP B 1 315 ? 34.262 17.529 12.983 1.00 14.93 ? 316 ASP B C 1 ATOM 4734 O O . ASP B 1 315 ? 33.889 18.569 13.494 1.00 16.32 ? 316 ASP B O 1 ATOM 4735 C CB . ASP B 1 315 ? 34.218 15.968 14.927 1.00 15.46 ? 316 ASP B CB 1 ATOM 4736 C CG . ASP B 1 315 ? 33.627 14.716 15.518 1.00 16.10 ? 316 ASP B CG 1 ATOM 4737 O OD1 . ASP B 1 315 ? 34.359 13.758 15.769 1.00 14.82 ? 316 ASP B OD1 1 ATOM 4738 O OD2 . ASP B 1 315 ? 32.409 14.671 15.707 1.00 17.17 ? 316 ASP B OD2 1 ATOM 4739 N N . ILE B 1 316 ? 35.003 17.497 11.893 1.00 13.41 ? 317 ILE B N 1 ATOM 4740 C CA . ILE B 1 316 ? 35.561 18.697 11.303 1.00 15.53 ? 317 ILE B CA 1 ATOM 4741 C C . ILE B 1 316 ? 34.603 19.189 10.201 1.00 16.90 ? 317 ILE B C 1 ATOM 4742 O O . ILE B 1 316 ? 34.205 18.409 9.310 1.00 16.68 ? 317 ILE B O 1 ATOM 4743 C CB . ILE B 1 316 ? 37.006 18.382 10.709 1.00 12.25 ? 317 ILE B CB 1 ATOM 4744 C CG1 . ILE B 1 316 ? 38.032 18.197 11.822 1.00 15.47 ? 317 ILE B CG1 1 ATOM 4745 C CG2 . ILE B 1 316 ? 37.497 19.480 9.781 1.00 13.56 ? 317 ILE B CG2 1 ATOM 4746 C CD1 . ILE B 1 316 ? 38.467 19.485 12.522 1.00 12.34 ? 317 ILE B CD1 1 ATOM 4747 N N . GLU B 1 317 ? 34.226 20.471 10.254 1.00 16.83 ? 318 GLU B N 1 ATOM 4748 C CA . GLU B 1 317 ? 33.345 21.035 9.241 1.00 16.27 ? 318 GLU B CA 1 ATOM 4749 C C . GLU B 1 317 ? 34.191 21.520 8.102 1.00 16.88 ? 318 GLU B C 1 ATOM 4750 O O . GLU B 1 317 ? 34.403 22.725 7.957 1.00 16.40 ? 318 GLU B O 1 ATOM 4751 C CB . GLU B 1 317 ? 32.512 22.167 9.816 1.00 16.32 ? 318 GLU B CB 1 ATOM 4752 C CG . GLU B 1 317 ? 31.683 21.716 10.959 1.00 19.30 ? 318 GLU B CG 1 ATOM 4753 C CD . GLU B 1 317 ? 30.594 22.707 11.329 1.00 23.58 ? 318 GLU B CD 1 ATOM 4754 O OE1 . GLU B 1 317 ? 29.439 22.490 10.896 1.00 24.32 ? 318 GLU B OE1 1 ATOM 4755 O OE2 . GLU B 1 317 ? 30.886 23.685 12.064 1.00 20.60 ? 318 GLU B OE2 1 ATOM 4756 N N . VAL B 1 318 ? 34.690 20.567 7.309 1.00 17.73 ? 319 VAL B N 1 ATOM 4757 C CA . VAL B 1 318 ? 35.557 20.857 6.164 1.00 19.51 ? 319 VAL B CA 1 ATOM 4758 C C . VAL B 1 318 ? 34.934 21.937 5.276 1.00 20.13 ? 319 VAL B C 1 ATOM 4759 O O . VAL B 1 318 ? 33.830 21.763 4.783 1.00 21.15 ? 319 VAL B O 1 ATOM 4760 C CB . VAL B 1 318 ? 35.888 19.554 5.320 1.00 19.86 ? 319 VAL B CB 1 ATOM 4761 C CG1 . VAL B 1 318 ? 36.869 19.876 4.170 1.00 22.64 ? 319 VAL B CG1 1 ATOM 4762 C CG2 . VAL B 1 318 ? 36.520 18.509 6.210 1.00 17.83 ? 319 VAL B CG2 1 ATOM 4763 N N . SER B 1 319 ? 35.668 23.027 5.044 1.00 20.12 ? 320 SER B N 1 ATOM 4764 C CA . SER B 1 319 ? 35.178 24.153 4.250 1.00 19.63 ? 320 SER B CA 1 ATOM 4765 C C . SER B 1 319 ? 35.978 24.523 3.008 1.00 20.64 ? 320 SER B C 1 ATOM 4766 O O . SER B 1 319 ? 35.634 25.485 2.311 1.00 20.94 ? 320 SER B O 1 ATOM 4767 C CB . SER B 1 319 ? 35.028 25.370 5.139 1.00 15.75 ? 320 SER B CB 1 ATOM 4768 O OG . SER B 1 319 ? 34.272 25.018 6.274 1.00 18.69 ? 320 SER B OG 1 ATOM 4769 N N . CYS B 1 320 ? 37.048 23.783 2.727 1.00 21.63 ? 321 CYS B N 1 ATOM 4770 C CA . CYS B 1 320 ? 37.861 24.034 1.543 1.00 23.41 ? 321 CYS B CA 1 ATOM 4771 C C . CYS B 1 320 ? 37.699 22.895 0.526 1.00 26.43 ? 321 CYS B C 1 ATOM 4772 O O . CYS B 1 320 ? 38.439 21.908 0.534 1.00 27.68 ? 321 CYS B O 1 ATOM 4773 C CB . CYS B 1 320 ? 39.331 24.189 1.904 1.00 20.99 ? 321 CYS B CB 1 ATOM 4774 S SG . CYS B 1 320 ? 40.326 24.421 0.408 1.00 19.95 ? 321 CYS B SG 1 ATOM 4775 N N . PRO B 1 321 ? 36.778 23.068 -0.424 1.00 30.24 ? 322 PRO B N 1 ATOM 4776 C CA . PRO B 1 321 ? 36.498 22.072 -1.468 1.00 31.80 ? 322 PRO B CA 1 ATOM 4777 C C . PRO B 1 321 ? 37.690 21.647 -2.350 1.00 32.40 ? 322 PRO B C 1 ATOM 4778 O O . PRO B 1 321 ? 37.847 20.463 -2.670 1.00 33.10 ? 322 PRO B O 1 ATOM 4779 C CB . PRO B 1 321 ? 35.390 22.748 -2.284 1.00 32.62 ? 322 PRO B CB 1 ATOM 4780 C CG . PRO B 1 321 ? 35.689 24.240 -2.118 1.00 32.87 ? 322 PRO B CG 1 ATOM 4781 C CD . PRO B 1 321 ? 36.017 24.317 -0.645 1.00 32.12 ? 322 PRO B CD 1 ATOM 4782 N N . SER B 1 322 ? 38.536 22.601 -2.715 1.00 32.37 ? 323 SER B N 1 ATOM 4783 C CA . SER B 1 322 ? 39.684 22.337 -3.571 1.00 32.02 ? 323 SER B CA 1 ATOM 4784 C C . SER B 1 322 ? 40.813 21.506 -2.972 1.00 31.09 ? 323 SER B C 1 ATOM 4785 O O . SER B 1 322 ? 41.685 21.030 -3.689 1.00 30.86 ? 323 SER B O 1 ATOM 4786 C CB . SER B 1 322 ? 40.232 23.667 -4.108 1.00 32.24 ? 323 SER B CB 1 ATOM 4787 O OG . SER B 1 322 ? 40.127 24.703 -3.136 1.00 32.73 ? 323 SER B OG 1 ATOM 4788 N N . GLU B 1 323 ? 40.808 21.315 -1.669 1.00 31.24 ? 324 GLU B N 1 ATOM 4789 C CA . GLU B 1 323 ? 41.890 20.565 -1.064 1.00 32.72 ? 324 GLU B CA 1 ATOM 4790 C C . GLU B 1 323 ? 41.384 19.646 0.038 1.00 31.94 ? 324 GLU B C 1 ATOM 4791 O O . GLU B 1 323 ? 40.610 20.060 0.906 1.00 31.04 ? 324 GLU B O 1 ATOM 4792 C CB . GLU B 1 323 ? 42.958 21.520 -0.479 1.00 37.36 ? 324 GLU B CB 1 ATOM 4793 C CG . GLU B 1 323 ? 43.850 22.245 -1.499 1.00 44.29 ? 324 GLU B CG 1 ATOM 4794 C CD . GLU B 1 323 ? 43.528 23.757 -1.664 1.00 48.10 ? 324 GLU B CD 1 ATOM 4795 O OE1 . GLU B 1 323 ? 43.177 24.187 -2.793 1.00 49.93 ? 324 GLU B OE1 1 ATOM 4796 O OE2 . GLU B 1 323 ? 43.662 24.528 -0.682 1.00 47.55 ? 324 GLU B OE2 1 ATOM 4797 N N . PRO B 1 324 ? 41.803 18.372 0.007 1.00 31.25 ? 325 PRO B N 1 ATOM 4798 C CA . PRO B 1 324 ? 41.401 17.383 1.015 1.00 29.12 ? 325 PRO B CA 1 ATOM 4799 C C . PRO B 1 324 ? 41.956 17.744 2.415 1.00 27.22 ? 325 PRO B C 1 ATOM 4800 O O . PRO B 1 324 ? 43.080 18.262 2.551 1.00 25.69 ? 325 PRO B O 1 ATOM 4801 C CB . PRO B 1 324 ? 42.004 16.088 0.472 1.00 30.39 ? 325 PRO B CB 1 ATOM 4802 C CG . PRO B 1 324 ? 43.203 16.565 -0.318 1.00 32.03 ? 325 PRO B CG 1 ATOM 4803 C CD . PRO B 1 324 ? 42.644 17.755 -1.033 1.00 31.32 ? 325 PRO B CD 1 ATOM 4804 N N . PHE B 1 325 ? 41.151 17.530 3.449 1.00 24.13 ? 326 PHE B N 1 ATOM 4805 C CA . PHE B 1 325 ? 41.604 17.863 4.782 1.00 23.30 ? 326 PHE B CA 1 ATOM 4806 C C . PHE B 1 325 ? 42.848 17.053 5.093 1.00 23.96 ? 326 PHE B C 1 ATOM 4807 O O . PHE B 1 325 ? 42.903 15.848 4.831 1.00 23.20 ? 326 PHE B O 1 ATOM 4808 C CB . PHE B 1 325 ? 40.523 17.625 5.822 1.00 20.85 ? 326 PHE B CB 1 ATOM 4809 C CG . PHE B 1 325 ? 40.821 18.262 7.123 1.00 19.28 ? 326 PHE B CG 1 ATOM 4810 C CD1 . PHE B 1 325 ? 40.558 19.613 7.317 1.00 19.10 ? 326 PHE B CD1 1 ATOM 4811 C CD2 . PHE B 1 325 ? 41.397 17.530 8.147 1.00 18.93 ? 326 PHE B CD2 1 ATOM 4812 C CE1 . PHE B 1 325 ? 40.864 20.229 8.523 1.00 17.96 ? 326 PHE B CE1 1 ATOM 4813 C CE2 . PHE B 1 325 ? 41.712 18.126 9.358 1.00 20.89 ? 326 PHE B CE2 1 ATOM 4814 C CZ . PHE B 1 325 ? 41.445 19.482 9.551 1.00 18.40 ? 326 PHE B CZ 1 ATOM 4815 N N . PRO B 1 326 ? 43.891 17.720 5.598 1.00 24.00 ? 327 PRO B N 1 ATOM 4816 C CA . PRO B 1 326 ? 45.120 16.988 5.909 1.00 23.73 ? 327 PRO B CA 1 ATOM 4817 C C . PRO B 1 326 ? 44.966 15.882 6.958 1.00 23.82 ? 327 PRO B C 1 ATOM 4818 O O . PRO B 1 326 ? 44.117 15.951 7.846 1.00 22.97 ? 327 PRO B O 1 ATOM 4819 C CB . PRO B 1 326 ? 46.089 18.107 6.325 1.00 24.97 ? 327 PRO B CB 1 ATOM 4820 C CG . PRO B 1 326 ? 45.191 19.248 6.747 1.00 22.92 ? 327 PRO B CG 1 ATOM 4821 C CD . PRO B 1 326 ? 44.056 19.175 5.783 1.00 22.27 ? 327 PRO B CD 1 ATOM 4822 N N . GLU B 1 327 ? 45.793 14.852 6.838 1.00 25.11 ? 328 GLU B N 1 ATOM 4823 C CA . GLU B 1 327 ? 45.749 13.725 7.764 1.00 26.77 ? 328 GLU B CA 1 ATOM 4824 C C . GLU B 1 327 ? 46.491 14.135 9.007 1.00 24.99 ? 328 GLU B C 1 ATOM 4825 O O . GLU B 1 327 ? 47.673 14.436 8.929 1.00 26.90 ? 328 GLU B O 1 ATOM 4826 C CB . GLU B 1 327 ? 46.479 12.501 7.171 1.00 30.64 ? 328 GLU B CB 1 ATOM 4827 C CG . GLU B 1 327 ? 45.896 11.898 5.877 1.00 40.70 ? 328 GLU B CG 1 ATOM 4828 C CD . GLU B 1 327 ? 44.734 10.897 6.117 1.00 46.67 ? 328 GLU B CD 1 ATOM 4829 O OE1 . GLU B 1 327 ? 43.584 11.172 5.665 1.00 48.52 ? 328 GLU B OE1 1 ATOM 4830 O OE2 . GLU B 1 327 ? 44.986 9.821 6.735 1.00 49.53 ? 328 GLU B OE2 1 ATOM 4831 N N . ILE B 1 328 ? 45.830 14.213 10.150 1.00 22.86 ? 329 ILE B N 1 ATOM 4832 C CA . ILE B 1 328 ? 46.588 14.552 11.345 1.00 22.11 ? 329 ILE B CA 1 ATOM 4833 C C . ILE B 1 328 ? 46.287 13.553 12.423 1.00 19.89 ? 329 ILE B C 1 ATOM 4834 O O . ILE B 1 328 ? 45.395 12.762 12.279 1.00 19.62 ? 329 ILE B O 1 ATOM 4835 C CB . ILE B 1 328 ? 46.388 16.024 11.869 1.00 23.75 ? 329 ILE B CB 1 ATOM 4836 C CG1 . ILE B 1 328 ? 45.106 16.181 12.658 1.00 24.38 ? 329 ILE B CG1 1 ATOM 4837 C CG2 . ILE B 1 328 ? 46.474 17.037 10.736 1.00 23.77 ? 329 ILE B CG2 1 ATOM 4838 C CD1 . ILE B 1 328 ? 45.097 17.460 13.432 1.00 27.41 ? 329 ILE B CD1 1 ATOM 4839 N N . ALA B 1 329 ? 47.080 13.552 13.473 1.00 20.04 ? 330 ALA B N 1 ATOM 4840 C CA . ALA B 1 329 ? 46.892 12.639 14.584 1.00 19.29 ? 330 ALA B CA 1 ATOM 4841 C C . ALA B 1 329 ? 45.583 12.904 15.348 1.00 21.12 ? 330 ALA B C 1 ATOM 4842 O O . ALA B 1 329 ? 45.152 14.053 15.500 1.00 18.87 ? 330 ALA B O 1 ATOM 4843 C CB . ALA B 1 329 ? 48.074 12.756 15.522 1.00 17.63 ? 330 ALA B CB 1 ATOM 4844 N N . THR B 1 330 ? 44.959 11.841 15.841 1.00 22.83 ? 331 THR B N 1 ATOM 4845 C CA . THR B 1 330 ? 43.727 11.977 16.611 1.00 27.48 ? 331 THR B CA 1 ATOM 4846 C C . THR B 1 330 ? 43.927 11.287 17.952 1.00 30.11 ? 331 THR B C 1 ATOM 4847 O O . THR B 1 330 ? 44.505 10.217 18.029 1.00 29.79 ? 331 THR B O 1 ATOM 4848 C CB . THR B 1 330 ? 42.443 11.480 15.840 1.00 26.77 ? 331 THR B CB 1 ATOM 4849 O OG1 . THR B 1 330 ? 42.552 10.101 15.479 1.00 31.96 ? 331 THR B OG1 1 ATOM 4850 C CG2 . THR B 1 330 ? 42.251 12.265 14.558 1.00 26.63 ? 331 THR B CG2 1 ATOM 4851 N N . ALA B 1 331 ? 43.621 12.002 19.022 1.00 33.69 ? 332 ALA B N 1 ATOM 4852 C CA . ALA B 1 331 ? 43.794 11.467 20.358 1.00 36.66 ? 332 ALA B CA 1 ATOM 4853 C C . ALA B 1 331 ? 42.566 10.659 20.729 1.00 39.73 ? 332 ALA B C 1 ATOM 4854 O O . ALA B 1 331 ? 41.564 10.683 20.009 1.00 42.99 ? 332 ALA B O 1 ATOM 4855 C CB . ALA B 1 331 ? 44.004 12.601 21.335 1.00 36.43 ? 332 ALA B CB 1 ATOM 4856 N N . SER B 1 332 ? 42.666 9.910 21.825 1.00 41.13 ? 333 SER B N 1 ATOM 4857 C CA . SER B 1 332 ? 41.558 9.105 22.308 1.00 40.79 ? 333 SER B CA 1 ATOM 4858 C C . SER B 1 332 ? 40.806 9.954 23.312 1.00 40.81 ? 333 SER B C 1 ATOM 4859 O O . SER B 1 332 ? 41.393 10.855 23.923 1.00 42.92 ? 333 SER B O 1 ATOM 4860 N N . GLY B 1 333 ? 39.506 9.717 23.447 1.00 40.06 ? 334 GLY B N 1 ATOM 4861 C CA . GLY B 1 333 ? 38.694 10.495 24.375 1.00 37.41 ? 334 GLY B CA 1 ATOM 4862 C C . GLY B 1 333 ? 39.084 10.260 25.826 1.00 36.25 ? 334 GLY B C 1 ATOM 4863 O O . GLY B 1 333 ? 40.069 9.564 26.097 1.00 38.65 ? 334 GLY B O 1 ATOM 4864 N N . PRO B 1 334 ? 38.345 10.827 26.790 1.00 33.22 ? 335 PRO B N 1 ATOM 4865 C CA . PRO B 1 334 ? 37.177 11.668 26.557 1.00 31.06 ? 335 PRO B CA 1 ATOM 4866 C C . PRO B 1 334 ? 37.536 13.122 26.172 1.00 28.23 ? 335 PRO B C 1 ATOM 4867 O O . PRO B 1 334 ? 38.711 13.493 26.055 1.00 26.75 ? 335 PRO B O 1 ATOM 4868 C CB . PRO B 1 334 ? 36.465 11.600 27.903 1.00 30.83 ? 335 PRO B CB 1 ATOM 4869 C CG . PRO B 1 334 ? 37.617 11.636 28.867 1.00 32.10 ? 335 PRO B CG 1 ATOM 4870 C CD . PRO B 1 334 ? 38.606 10.672 28.235 1.00 32.86 ? 335 PRO B CD 1 ATOM 4871 N N . LEU B 1 335 ? 36.500 13.926 25.972 1.00 26.21 ? 336 LEU B N 1 ATOM 4872 C CA . LEU B 1 335 ? 36.671 15.313 25.613 1.00 23.44 ? 336 LEU B CA 1 ATOM 4873 C C . LEU B 1 335 ? 37.390 15.985 26.756 1.00 21.34 ? 336 LEU B C 1 ATOM 4874 O O . LEU B 1 335 ? 37.171 15.638 27.913 1.00 20.91 ? 336 LEU B O 1 ATOM 4875 C CB . LEU B 1 335 ? 35.314 16.005 25.419 1.00 21.62 ? 336 LEU B CB 1 ATOM 4876 C CG . LEU B 1 335 ? 34.445 15.762 24.190 1.00 22.78 ? 336 LEU B CG 1 ATOM 4877 C CD1 . LEU B 1 335 ? 33.270 16.693 24.340 1.00 23.73 ? 336 LEU B CD1 1 ATOM 4878 C CD2 . LEU B 1 335 ? 35.158 16.028 22.893 1.00 18.47 ? 336 LEU B CD2 1 ATOM 4879 N N . PRO B 1 336 ? 38.308 16.917 26.445 1.00 21.68 ? 337 PRO B N 1 ATOM 4880 C CA . PRO B 1 336 ? 39.031 17.615 27.519 1.00 20.20 ? 337 PRO B CA 1 ATOM 4881 C C . PRO B 1 336 ? 38.158 18.708 28.134 1.00 19.60 ? 337 PRO B C 1 ATOM 4882 O O . PRO B 1 336 ? 37.066 18.990 27.643 1.00 19.64 ? 337 PRO B O 1 ATOM 4883 C CB . PRO B 1 336 ? 40.243 18.198 26.795 1.00 21.73 ? 337 PRO B CB 1 ATOM 4884 C CG . PRO B 1 336 ? 39.741 18.421 25.394 1.00 21.47 ? 337 PRO B CG 1 ATOM 4885 C CD . PRO B 1 336 ? 38.853 17.241 25.111 1.00 20.37 ? 337 PRO B CD 1 ATOM 4886 N N . SER B 1 337 ? 38.561 19.211 29.285 1.00 19.12 ? 338 SER B N 1 ATOM 4887 C CA . SER B 1 337 ? 37.840 20.303 29.913 1.00 19.81 ? 338 SER B CA 1 ATOM 4888 C C . SER B 1 337 ? 38.959 21.289 30.227 1.00 18.92 ? 338 SER B C 1 ATOM 4889 O O . SER B 1 337 ? 39.830 21.026 31.064 1.00 17.34 ? 338 SER B O 1 ATOM 4890 C CB . SER B 1 337 ? 37.147 19.862 31.188 1.00 25.28 ? 338 SER B CB 1 ATOM 4891 O OG . SER B 1 337 ? 36.038 20.728 31.501 1.00 32.41 ? 338 SER B OG 1 ATOM 4892 N N . LEU B 1 338 ? 38.936 22.417 29.532 1.00 16.34 ? 339 LEU B N 1 ATOM 4893 C CA . LEU B 1 338 ? 39.993 23.405 29.680 1.00 16.33 ? 339 LEU B CA 1 ATOM 4894 C C . LEU B 1 338 ? 39.949 24.254 30.906 1.00 15.97 ? 339 LEU B C 1 ATOM 4895 O O . LEU B 1 338 ? 38.896 24.767 31.307 1.00 17.78 ? 339 LEU B O 1 ATOM 4896 C CB . LEU B 1 338 ? 40.057 24.331 28.457 1.00 14.23 ? 339 LEU B CB 1 ATOM 4897 C CG . LEU B 1 338 ? 40.816 23.941 27.203 1.00 17.11 ? 339 LEU B CG 1 ATOM 4898 C CD1 . LEU B 1 338 ? 40.706 22.490 26.865 1.00 16.10 ? 339 LEU B CD1 1 ATOM 4899 C CD2 . LEU B 1 338 ? 40.309 24.847 26.091 1.00 15.39 ? 339 LEU B CD2 1 ATOM 4900 N N . ALA B 1 339 ? 41.125 24.404 31.490 1.00 14.91 ? 340 ALA B N 1 ATOM 4901 C CA . ALA B 1 339 ? 41.313 25.264 32.635 1.00 15.92 ? 340 ALA B CA 1 ATOM 4902 C C . ALA B 1 339 ? 41.499 26.657 32.027 1.00 14.63 ? 340 ALA B C 1 ATOM 4903 O O . ALA B 1 339 ? 41.851 26.803 30.844 1.00 13.24 ? 340 ALA B O 1 ATOM 4904 C CB . ALA B 1 339 ? 42.597 24.878 33.390 1.00 15.22 ? 340 ALA B CB 1 ATOM 4905 N N . PRO B 1 340 ? 41.245 27.695 32.826 1.00 17.46 ? 341 PRO B N 1 ATOM 4906 C CA . PRO B 1 340 ? 41.416 29.058 32.319 1.00 16.87 ? 341 PRO B CA 1 ATOM 4907 C C . PRO B 1 340 ? 42.913 29.243 32.057 1.00 16.82 ? 341 PRO B C 1 ATOM 4908 O O . PRO B 1 340 ? 43.742 28.587 32.704 1.00 15.55 ? 341 PRO B O 1 ATOM 4909 C CB . PRO B 1 340 ? 40.992 29.938 33.504 1.00 16.67 ? 341 PRO B CB 1 ATOM 4910 C CG . PRO B 1 340 ? 40.180 29.040 34.379 1.00 18.40 ? 341 PRO B CG 1 ATOM 4911 C CD . PRO B 1 340 ? 40.835 27.690 34.241 1.00 17.69 ? 341 PRO B CD 1 ATOM 4912 N N . ALA B 1 341 ? 43.239 30.093 31.082 1.00 16.59 ? 342 ALA B N 1 ATOM 4913 C CA . ALA B 1 341 ? 44.607 30.438 30.720 1.00 14.77 ? 342 ALA B CA 1 ATOM 4914 C C . ALA B 1 341 ? 45.228 31.168 31.924 1.00 16.15 ? 342 ALA B C 1 ATOM 4915 O O . ALA B 1 341 ? 44.522 31.869 32.684 1.00 17.34 ? 342 ALA B O 1 ATOM 4916 C CB . ALA B 1 341 ? 44.590 31.330 29.491 1.00 13.11 ? 342 ALA B CB 1 ATOM 4917 N N . PRO B 1 342 ? 46.539 30.974 32.156 1.00 16.84 ? 343 PRO B N 1 ATOM 4918 C CA . PRO B 1 342 ? 47.306 31.571 33.260 1.00 17.57 ? 343 PRO B CA 1 ATOM 4919 C C . PRO B 1 342 ? 47.474 33.087 33.205 1.00 18.51 ? 343 PRO B C 1 ATOM 4920 O O . PRO B 1 342 ? 47.430 33.688 32.109 1.00 16.37 ? 343 PRO B O 1 ATOM 4921 C CB . PRO B 1 342 ? 48.674 30.898 33.132 1.00 19.25 ? 343 PRO B CB 1 ATOM 4922 C CG . PRO B 1 342 ? 48.393 29.662 32.373 1.00 19.70 ? 343 PRO B CG 1 ATOM 4923 C CD . PRO B 1 342 ? 47.397 30.093 31.357 1.00 17.54 ? 343 PRO B CD 1 ATOM 4924 O OXT . PRO B 1 342 ? 47.706 33.646 34.295 1.00 18.78 ? 343 PRO B OXT 1 HETATM 4925 C CHA . HEM C 2 . ? 41.862 16.414 60.574 1.00 13.38 ? 401 HEM A CHA 1 HETATM 4926 C CHB . HEM C 2 . ? 39.173 18.006 56.819 1.00 8.68 ? 401 HEM A CHB 1 HETATM 4927 C CHC . HEM C 2 . ? 42.933 17.669 53.724 1.00 7.39 ? 401 HEM A CHC 1 HETATM 4928 C CHD . HEM C 2 . ? 45.772 16.992 57.606 1.00 8.92 ? 401 HEM A CHD 1 HETATM 4929 C C1A . HEM C 2 . ? 40.860 17.063 59.870 1.00 11.86 ? 401 HEM A C1A 1 HETATM 4930 C C2A . HEM C 2 . ? 39.563 17.373 60.348 1.00 11.72 ? 401 HEM A C2A 1 HETATM 4931 C C3A . HEM C 2 . ? 38.843 17.876 59.293 1.00 11.22 ? 401 HEM A C3A 1 HETATM 4932 C C4A . HEM C 2 . ? 39.640 17.773 58.136 1.00 10.40 ? 401 HEM A C4A 1 HETATM 4933 C CMA . HEM C 2 . ? 37.441 18.455 59.330 1.00 9.77 ? 401 HEM A CMA 1 HETATM 4934 C CAA . HEM C 2 . ? 39.048 17.120 61.742 1.00 10.67 ? 401 HEM A CAA 1 HETATM 4935 C CBA . HEM C 2 . ? 39.681 18.163 62.635 1.00 11.33 ? 401 HEM A CBA 1 HETATM 4936 C CGA . HEM C 2 . ? 39.037 18.244 64.008 1.00 13.18 ? 401 HEM A CGA 1 HETATM 4937 O O1A . HEM C 2 . ? 37.804 18.290 64.094 1.00 13.73 ? 401 HEM A O1A 1 HETATM 4938 O O2A . HEM C 2 . ? 39.761 18.251 65.017 1.00 13.33 ? 401 HEM A O2A 1 HETATM 4939 C C1B . HEM C 2 . ? 39.925 17.955 55.630 1.00 7.00 ? 401 HEM A C1B 1 HETATM 4940 C C2B . HEM C 2 . ? 39.420 18.236 54.377 1.00 8.11 ? 401 HEM A C2B 1 HETATM 4941 C C3B . HEM C 2 . ? 40.467 18.043 53.506 1.00 9.25 ? 401 HEM A C3B 1 HETATM 4942 C C4B . HEM C 2 . ? 41.619 17.692 54.252 1.00 7.73 ? 401 HEM A C4B 1 HETATM 4943 C CMB . HEM C 2 . ? 38.010 18.656 53.929 1.00 8.18 ? 401 HEM A CMB 1 HETATM 4944 C CAB . HEM C 2 . ? 40.495 18.350 52.133 1.00 10.81 ? 401 HEM A CAB 1 HETATM 4945 C CBB . HEM C 2 . ? 40.240 17.584 50.979 1.00 12.35 ? 401 HEM A CBB 1 HETATM 4946 C C1C . HEM C 2 . ? 44.089 17.578 54.548 1.00 7.63 ? 401 HEM A C1C 1 HETATM 4947 C C2C . HEM C 2 . ? 45.483 17.805 54.143 1.00 9.00 ? 401 HEM A C2C 1 HETATM 4948 C C3C . HEM C 2 . ? 46.272 17.705 55.229 1.00 6.46 ? 401 HEM A C3C 1 HETATM 4949 C C4C . HEM C 2 . ? 45.355 17.334 56.316 1.00 6.99 ? 401 HEM A C4C 1 HETATM 4950 C CMC . HEM C 2 . ? 45.869 18.050 52.668 1.00 7.81 ? 401 HEM A CMC 1 HETATM 4951 C CAC . HEM C 2 . ? 47.679 17.914 55.448 1.00 9.47 ? 401 HEM A CAC 1 HETATM 4952 C CBC . HEM C 2 . ? 48.668 17.621 54.545 1.00 8.57 ? 401 HEM A CBC 1 HETATM 4953 C C1D . HEM C 2 . ? 44.972 16.694 58.716 1.00 9.49 ? 401 HEM A C1D 1 HETATM 4954 C C2D . HEM C 2 . ? 45.452 16.098 59.940 1.00 9.97 ? 401 HEM A C2D 1 HETATM 4955 C C3D . HEM C 2 . ? 44.370 16.006 60.768 1.00 10.97 ? 401 HEM A C3D 1 HETATM 4956 C C4D . HEM C 2 . ? 43.198 16.452 60.040 1.00 13.24 ? 401 HEM A C4D 1 HETATM 4957 C CMD . HEM C 2 . ? 46.835 15.498 60.253 1.00 7.85 ? 401 HEM A CMD 1 HETATM 4958 C CAD . HEM C 2 . ? 44.369 15.447 62.191 1.00 9.94 ? 401 HEM A CAD 1 HETATM 4959 C CBD . HEM C 2 . ? 44.221 16.501 63.260 1.00 8.93 ? 401 HEM A CBD 1 HETATM 4960 C CGD . HEM C 2 . ? 44.187 15.910 64.644 1.00 12.70 ? 401 HEM A CGD 1 HETATM 4961 O O1D . HEM C 2 . ? 44.165 16.668 65.638 1.00 13.30 ? 401 HEM A O1D 1 HETATM 4962 O O2D . HEM C 2 . ? 44.193 14.667 64.762 1.00 12.25 ? 401 HEM A O2D 1 HETATM 4963 N NA . HEM C 2 . ? 40.941 17.307 58.518 1.00 12.05 ? 401 HEM A NA 1 HETATM 4964 N NB . HEM C 2 . ? 41.296 17.662 55.574 1.00 7.41 ? 401 HEM A NB 1 HETATM 4965 N NC . HEM C 2 . ? 44.033 17.353 55.907 1.00 9.60 ? 401 HEM A NC 1 HETATM 4966 N ND . HEM C 2 . ? 43.575 16.880 58.761 1.00 12.81 ? 401 HEM A ND 1 HETATM 4967 FE FE . HEM C 2 . ? 42.418 17.207 57.212 1.00 13.52 ? 401 HEM A FE 1 HETATM 4968 CA CA . CA D 3 . ? 48.788 31.532 54.545 1.00 14.54 ? 402 CA A CA 1 HETATM 4969 CA CA . CA E 3 . ? 47.957 5.372 59.839 1.00 14.11 ? 403 CA A CA 1 HETATM 4970 C C1 . NAG F 4 . ? 57.783 37.906 62.024 1.00 25.76 ? 404 NAG A C1 1 HETATM 4971 C C2 . NAG F 4 . ? 58.822 38.375 63.012 1.00 27.22 ? 404 NAG A C2 1 HETATM 4972 C C3 . NAG F 4 . ? 58.189 38.378 64.428 1.00 28.15 ? 404 NAG A C3 1 HETATM 4973 C C4 . NAG F 4 . ? 56.923 39.245 64.407 1.00 26.60 ? 404 NAG A C4 1 HETATM 4974 C C5 . NAG F 4 . ? 55.996 38.800 63.423 1.00 26.91 ? 404 NAG A C5 1 HETATM 4975 C C6 . NAG F 4 . ? 54.689 39.614 63.349 1.00 26.88 ? 404 NAG A C6 1 HETATM 4976 C C7 . NAG F 4 . ? 61.157 37.854 62.317 1.00 33.42 ? 404 NAG A C7 1 HETATM 4977 C C8 . NAG F 4 . ? 62.300 36.870 62.456 1.00 34.41 ? 404 NAG A C8 1 HETATM 4978 N N2 . NAG F 4 . ? 60.038 37.569 62.989 1.00 30.98 ? 404 NAG A N2 1 HETATM 4979 O O3 . NAG F 4 . ? 59.034 38.808 65.452 1.00 27.32 ? 404 NAG A O3 1 HETATM 4980 O O4 . NAG F 4 . ? 56.227 39.093 65.594 1.00 31.90 ? 404 NAG A O4 1 HETATM 4981 O O5 . NAG F 4 . ? 56.656 38.778 62.103 1.00 24.97 ? 404 NAG A O5 1 HETATM 4982 O O6 . NAG F 4 . ? 54.052 39.397 62.104 1.00 28.74 ? 404 NAG A O6 1 HETATM 4983 O O7 . NAG F 4 . ? 61.289 38.854 61.587 1.00 34.61 ? 404 NAG A O7 1 HETATM 4984 C C1 . NAG G 4 . ? 56.200 40.038 66.662 1.00 37.33 ? 405 NAG A C1 1 HETATM 4985 C C2 . NAG G 4 . ? 55.098 39.574 67.594 1.00 38.00 ? 405 NAG A C2 1 HETATM 4986 C C3 . NAG G 4 . ? 55.132 40.411 68.876 1.00 40.51 ? 405 NAG A C3 1 HETATM 4987 C C4 . NAG G 4 . ? 56.559 40.427 69.619 1.00 41.60 ? 405 NAG A C4 1 HETATM 4988 C C5 . NAG G 4 . ? 57.557 40.856 68.506 1.00 40.87 ? 405 NAG A C5 1 HETATM 4989 C C6 . NAG G 4 . ? 58.995 40.764 69.002 1.00 42.47 ? 405 NAG A C6 1 HETATM 4990 C C7 . NAG G 4 . ? 53.094 38.665 66.460 1.00 39.30 ? 405 NAG A C7 1 HETATM 4991 C C8 . NAG G 4 . ? 51.760 38.874 65.715 1.00 39.81 ? 405 NAG A C8 1 HETATM 4992 N N2 . NAG G 4 . ? 53.814 39.698 66.903 1.00 38.27 ? 405 NAG A N2 1 HETATM 4993 O O3 . NAG G 4 . ? 54.174 39.841 69.759 1.00 41.64 ? 405 NAG A O3 1 HETATM 4994 O O4 . NAG G 4 . ? 56.632 41.283 70.850 1.00 40.26 ? 405 NAG A O4 1 HETATM 4995 O O5 . NAG G 4 . ? 57.423 39.972 67.363 1.00 38.84 ? 405 NAG A O5 1 HETATM 4996 O O6 . NAG G 4 . ? 59.890 40.805 67.898 1.00 44.95 ? 405 NAG A O6 1 HETATM 4997 O O7 . NAG G 4 . ? 53.437 37.499 66.615 1.00 38.05 ? 405 NAG A O7 1 HETATM 4998 C C1 . BMA H 5 . ? 36.445 0.224 71.168 1.00 37.43 ? 406 BMA A C1 1 HETATM 4999 C C2 . BMA H 5 . ? 35.271 1.094 71.314 1.00 39.32 ? 406 BMA A C2 1 HETATM 5000 C C3 . BMA H 5 . ? 35.921 2.439 71.150 1.00 40.40 ? 406 BMA A C3 1 HETATM 5001 C C4 . BMA H 5 . ? 36.938 2.512 72.387 1.00 39.15 ? 406 BMA A C4 1 HETATM 5002 C C5 . BMA H 5 . ? 37.825 1.247 72.749 1.00 40.44 ? 406 BMA A C5 1 HETATM 5003 C C6 . BMA H 5 . ? 38.252 1.320 74.247 1.00 42.79 ? 406 BMA A C6 1 HETATM 5004 O O2 . BMA H 5 . ? 34.633 0.840 72.589 1.00 39.69 ? 406 BMA A O2 1 HETATM 5005 O O3 . BMA H 5 . ? 34.871 3.423 71.101 1.00 40.73 ? 406 BMA A O3 1 HETATM 5006 O O4 . BMA H 5 . ? 37.873 3.468 72.099 1.00 38.94 ? 406 BMA A O4 1 HETATM 5007 O O5 . BMA H 5 . ? 37.009 0.056 72.466 1.00 37.55 ? 406 BMA A O5 1 HETATM 5008 O O6 . BMA H 5 . ? 39.363 0.508 74.605 1.00 48.14 ? 406 BMA A O6 1 HETATM 5009 MG MG . MG I 6 . ? 31.653 -11.072 56.070 1.00 44.20 ? 407 MG A MG 1 HETATM 5010 C CHA . HEM J 2 . ? 41.771 38.210 22.211 1.00 9.22 ? 401 HEM B CHA 1 HETATM 5011 C CHB . HEM J 2 . ? 39.168 39.857 18.495 1.00 6.34 ? 401 HEM B CHB 1 HETATM 5012 C CHC . HEM J 2 . ? 42.835 39.515 15.415 1.00 7.66 ? 401 HEM B CHC 1 HETATM 5013 C CHD . HEM J 2 . ? 45.667 38.819 19.337 1.00 7.42 ? 401 HEM B CHD 1 HETATM 5014 C C1A . HEM J 2 . ? 40.718 38.733 21.481 1.00 10.18 ? 401 HEM B C1A 1 HETATM 5015 C C2A . HEM J 2 . ? 39.370 39.027 21.950 1.00 9.99 ? 401 HEM B C2A 1 HETATM 5016 C C3A . HEM J 2 . ? 38.674 39.605 20.912 1.00 7.53 ? 401 HEM B C3A 1 HETATM 5017 C C4A . HEM J 2 . ? 39.574 39.631 19.783 1.00 8.78 ? 401 HEM B C4A 1 HETATM 5018 C CMA . HEM J 2 . ? 37.324 40.307 20.988 1.00 7.40 ? 401 HEM B CMA 1 HETATM 5019 C CAA . HEM J 2 . ? 38.857 38.830 23.359 1.00 8.54 ? 401 HEM B CAA 1 HETATM 5020 C CBA . HEM J 2 . ? 39.484 39.825 24.303 1.00 8.92 ? 401 HEM B CBA 1 HETATM 5021 C CGA . HEM J 2 . ? 38.818 39.853 25.680 1.00 11.56 ? 401 HEM B CGA 1 HETATM 5022 O O1A . HEM J 2 . ? 37.581 39.990 25.777 1.00 12.94 ? 401 HEM B O1A 1 HETATM 5023 O O2A . HEM J 2 . ? 39.541 39.803 26.685 1.00 13.05 ? 401 HEM B O2A 1 HETATM 5024 C C1B . HEM J 2 . ? 39.877 39.740 17.278 1.00 6.85 ? 401 HEM B C1B 1 HETATM 5025 C C2B . HEM J 2 . ? 39.346 40.017 16.022 1.00 8.18 ? 401 HEM B C2B 1 HETATM 5026 C C3B . HEM J 2 . ? 40.356 39.887 15.165 1.00 6.94 ? 401 HEM B C3B 1 HETATM 5027 C C4B . HEM J 2 . ? 41.509 39.534 15.902 1.00 8.05 ? 401 HEM B C4B 1 HETATM 5028 C CMB . HEM J 2 . ? 37.880 40.421 15.686 1.00 10.19 ? 401 HEM B CMB 1 HETATM 5029 C CAB . HEM J 2 . ? 40.387 40.237 13.853 1.00 9.57 ? 401 HEM B CAB 1 HETATM 5030 C CBB . HEM J 2 . ? 40.149 39.513 12.687 1.00 13.49 ? 401 HEM B CBB 1 HETATM 5031 C C1C . HEM J 2 . ? 43.981 39.383 16.260 1.00 8.44 ? 401 HEM B C1C 1 HETATM 5032 C C2C . HEM J 2 . ? 45.365 39.613 15.835 1.00 6.35 ? 401 HEM B C2C 1 HETATM 5033 C C3C . HEM J 2 . ? 46.160 39.498 16.936 1.00 7.41 ? 401 HEM B C3C 1 HETATM 5034 C C4C . HEM J 2 . ? 45.245 39.173 18.047 1.00 6.81 ? 401 HEM B C4C 1 HETATM 5035 C CMC . HEM J 2 . ? 45.707 39.944 14.378 1.00 5.47 ? 401 HEM B CMC 1 HETATM 5036 C CAC . HEM J 2 . ? 47.561 39.612 17.123 1.00 9.05 ? 401 HEM B CAC 1 HETATM 5037 C CBC . HEM J 2 . ? 48.498 39.564 16.150 1.00 9.32 ? 401 HEM B CBC 1 HETATM 5038 C C1D . HEM J 2 . ? 44.861 38.426 20.357 1.00 9.75 ? 401 HEM B C1D 1 HETATM 5039 C C2D . HEM J 2 . ? 45.320 37.849 21.592 1.00 10.04 ? 401 HEM B C2D 1 HETATM 5040 C C3D . HEM J 2 . ? 44.225 37.745 22.412 1.00 10.01 ? 401 HEM B C3D 1 HETATM 5041 C C4D . HEM J 2 . ? 43.085 38.180 21.662 1.00 10.84 ? 401 HEM B C4D 1 HETATM 5042 C CMD . HEM J 2 . ? 46.751 37.342 21.897 1.00 9.00 ? 401 HEM B CMD 1 HETATM 5043 C CAD . HEM J 2 . ? 44.119 37.197 23.841 1.00 9.14 ? 401 HEM B CAD 1 HETATM 5044 C CBD . HEM J 2 . ? 44.053 38.207 24.944 1.00 7.88 ? 401 HEM B CBD 1 HETATM 5045 C CGD . HEM J 2 . ? 44.020 37.573 26.322 1.00 10.62 ? 401 HEM B CGD 1 HETATM 5046 O O1D . HEM J 2 . ? 43.911 38.312 27.319 1.00 11.15 ? 401 HEM B O1D 1 HETATM 5047 O O2D . HEM J 2 . ? 44.113 36.331 26.442 1.00 10.58 ? 401 HEM B O2D 1 HETATM 5048 N NA . HEM J 2 . ? 40.874 39.134 20.158 1.00 11.31 ? 401 HEM B NA 1 HETATM 5049 N NB . HEM J 2 . ? 41.214 39.427 17.203 1.00 6.21 ? 401 HEM B NB 1 HETATM 5050 N NC . HEM J 2 . ? 43.908 39.132 17.605 1.00 9.09 ? 401 HEM B NC 1 HETATM 5051 N ND . HEM J 2 . ? 43.460 38.589 20.370 1.00 11.53 ? 401 HEM B ND 1 HETATM 5052 FE FE . HEM J 2 . ? 42.338 39.012 18.842 1.00 12.90 ? 401 HEM B FE 1 HETATM 5053 CA CA . CA K 3 . ? 48.632 53.371 16.468 1.00 14.98 ? 402 CA B CA 1 HETATM 5054 CA CA . CA L 3 . ? 47.880 27.154 21.268 1.00 10.97 ? 403 CA B CA 1 HETATM 5055 C C1 . NAG M 4 . ? 57.547 59.784 24.063 1.00 21.40 ? 404 NAG B C1 1 HETATM 5056 C C2 . NAG M 4 . ? 58.536 60.210 25.099 1.00 23.58 ? 404 NAG B C2 1 HETATM 5057 C C3 . NAG M 4 . ? 57.941 60.170 26.464 1.00 24.15 ? 404 NAG B C3 1 HETATM 5058 C C4 . NAG M 4 . ? 56.637 60.983 26.553 1.00 24.55 ? 404 NAG B C4 1 HETATM 5059 C C5 . NAG M 4 . ? 55.752 60.552 25.491 1.00 23.62 ? 404 NAG B C5 1 HETATM 5060 C C6 . NAG M 4 . ? 54.551 61.374 25.405 1.00 26.37 ? 404 NAG B C6 1 HETATM 5061 C C7 . NAG M 4 . ? 60.827 59.477 24.500 1.00 30.44 ? 404 NAG B C7 1 HETATM 5062 C C8 . NAG M 4 . ? 61.803 58.358 24.839 1.00 31.56 ? 404 NAG B C8 1 HETATM 5063 N N2 . NAG M 4 . ? 59.689 59.318 25.163 1.00 27.96 ? 404 NAG B N2 1 HETATM 5064 O O3 . NAG M 4 . ? 58.799 60.616 27.439 1.00 21.62 ? 404 NAG B O3 1 HETATM 5065 O O4 . NAG M 4 . ? 56.036 60.660 27.815 1.00 24.60 ? 404 NAG B O4 1 HETATM 5066 O O5 . NAG M 4 . ? 56.390 60.595 24.175 1.00 23.33 ? 404 NAG B O5 1 HETATM 5067 O O6 . NAG M 4 . ? 53.763 60.799 24.343 1.00 30.04 ? 404 NAG B O6 1 HETATM 5068 O O7 . NAG M 4 . ? 61.012 60.395 23.695 1.00 31.67 ? 404 NAG B O7 1 HETATM 5069 C C1 . NAG N 4 . ? 55.945 61.647 28.789 1.00 27.21 ? 405 NAG B C1 1 HETATM 5070 C C2 . NAG N 4 . ? 54.847 61.209 29.731 1.00 28.89 ? 405 NAG B C2 1 HETATM 5071 C C3 . NAG N 4 . ? 54.813 62.117 30.965 1.00 30.18 ? 405 NAG B C3 1 HETATM 5072 C C4 . NAG N 4 . ? 56.211 62.216 31.726 1.00 30.46 ? 405 NAG B C4 1 HETATM 5073 C C5 . NAG N 4 . ? 57.274 62.545 30.607 1.00 29.52 ? 405 NAG B C5 1 HETATM 5074 C C6 . NAG N 4 . ? 58.680 62.254 31.153 1.00 27.61 ? 405 NAG B C6 1 HETATM 5075 C C7 . NAG N 4 . ? 52.813 60.327 28.536 1.00 30.38 ? 405 NAG B C7 1 HETATM 5076 C C8 . NAG N 4 . ? 51.503 60.593 27.779 1.00 31.26 ? 405 NAG B C8 1 HETATM 5077 N N2 . NAG N 4 . ? 53.578 61.313 29.012 1.00 29.54 ? 405 NAG B N2 1 HETATM 5078 O O3 . NAG N 4 . ? 53.861 61.546 31.878 1.00 31.27 ? 405 NAG B O3 1 HETATM 5079 O O4 . NAG N 4 . ? 56.226 63.183 32.894 1.00 33.52 ? 405 NAG B O4 1 HETATM 5080 O O5 . NAG N 4 . ? 57.168 61.706 29.423 1.00 26.63 ? 405 NAG B O5 1 HETATM 5081 O O6 . NAG N 4 . ? 59.516 62.552 30.084 1.00 31.15 ? 405 NAG B O6 1 HETATM 5082 O O7 . NAG N 4 . ? 53.090 59.141 28.667 1.00 29.64 ? 405 NAG B O7 1 HETATM 5083 C C1 . BMA O 5 . ? 36.257 21.841 32.249 1.00 38.28 ? 406 BMA B C1 1 HETATM 5084 C C2 . BMA O 5 . ? 35.056 22.725 32.467 1.00 39.60 ? 406 BMA B C2 1 HETATM 5085 C C3 . BMA O 5 . ? 35.744 24.105 32.379 1.00 41.43 ? 406 BMA B C3 1 HETATM 5086 C C4 . BMA O 5 . ? 36.774 24.114 33.649 1.00 40.13 ? 406 BMA B C4 1 HETATM 5087 C C5 . BMA O 5 . ? 37.755 22.849 33.736 1.00 41.30 ? 406 BMA B C5 1 HETATM 5088 C C6 . BMA O 5 . ? 38.640 22.598 34.946 1.00 42.90 ? 406 BMA B C6 1 HETATM 5089 O O2 . BMA O 5 . ? 34.535 22.332 33.753 1.00 39.71 ? 406 BMA B O2 1 HETATM 5090 O O3 . BMA O 5 . ? 34.834 25.214 32.303 1.00 42.56 ? 406 BMA B O3 1 HETATM 5091 O O4 . BMA O 5 . ? 37.574 25.264 33.501 1.00 40.32 ? 406 BMA B O4 1 HETATM 5092 O O5 . BMA O 5 . ? 36.935 21.646 33.523 1.00 39.84 ? 406 BMA B O5 1 HETATM 5093 O O6 . BMA O 5 . ? 37.801 22.433 36.064 1.00 49.06 ? 406 BMA B O6 1 HETATM 5094 O O . HOH P 7 . ? 38.157 1.135 44.762 1.00 25.91 ? 501 HOH A O 1 HETATM 5095 O O . HOH P 7 . ? 50.010 2.018 46.772 1.00 28.97 ? 502 HOH A O 1 HETATM 5096 O O . HOH P 7 . ? 58.135 0.543 62.699 1.00 33.81 ? 503 HOH A O 1 HETATM 5097 O O . HOH P 7 . ? 35.996 19.119 70.912 1.00 35.79 ? 504 HOH A O 1 HETATM 5098 O O . HOH P 7 . ? 59.596 21.949 50.009 1.00 15.71 ? 505 HOH A O 1 HETATM 5099 O O . HOH P 7 . ? 53.221 34.847 49.214 1.00 18.46 ? 506 HOH A O 1 HETATM 5100 O O . HOH P 7 . ? 55.807 35.802 53.239 1.00 24.04 ? 507 HOH A O 1 HETATM 5101 O O . HOH P 7 . ? 44.046 4.701 68.250 1.00 27.66 ? 508 HOH A O 1 HETATM 5102 O O . HOH P 7 . ? 71.807 29.855 59.746 1.00 17.00 ? 509 HOH A O 1 HETATM 5103 O O . HOH P 7 . ? 57.092 -5.666 55.197 1.00 31.37 ? 510 HOH A O 1 HETATM 5104 O O . HOH P 7 . ? 44.959 6.600 73.523 1.00 15.00 ? 511 HOH A O 1 HETATM 5105 O O . HOH P 7 . ? 29.867 5.272 55.643 1.00 22.10 ? 512 HOH A O 1 HETATM 5106 O O . HOH P 7 . ? 59.579 34.712 63.734 1.00 36.26 ? 513 HOH A O 1 HETATM 5107 O O . HOH P 7 . ? 36.288 31.708 48.631 1.00 35.35 ? 514 HOH A O 1 HETATM 5108 O O . HOH P 7 . ? 37.165 34.606 49.686 1.00 29.72 ? 515 HOH A O 1 HETATM 5109 O O . HOH P 7 . ? 49.438 -6.532 52.082 1.00 25.66 ? 516 HOH A O 1 HETATM 5110 O O . HOH P 7 . ? 61.801 28.771 71.614 1.00 29.13 ? 517 HOH A O 1 HETATM 5111 O O . HOH P 7 . ? 33.131 3.273 69.192 1.00 30.17 ? 518 HOH A O 1 HETATM 5112 O O . HOH P 7 . ? 39.040 21.499 56.392 1.00 26.99 ? 519 HOH A O 1 HETATM 5113 O O . HOH P 7 . ? 44.691 15.754 68.006 1.00 15.53 ? 520 HOH A O 1 HETATM 5114 O O . HOH P 7 . ? 48.163 35.369 53.026 1.00 18.09 ? 521 HOH A O 1 HETATM 5115 O O . HOH P 7 . ? 38.478 15.092 53.104 1.00 10.60 ? 522 HOH A O 1 HETATM 5116 O O . HOH P 7 . ? 66.820 31.094 55.277 1.00 34.86 ? 523 HOH A O 1 HETATM 5117 O O . HOH P 7 . ? 56.731 33.645 56.492 1.00 18.85 ? 524 HOH A O 1 HETATM 5118 O O . HOH P 7 . ? 43.815 11.030 73.575 1.00 37.02 ? 525 HOH A O 1 HETATM 5119 O O . HOH P 7 . ? 53.415 8.038 71.805 1.00 15.00 ? 526 HOH A O 1 HETATM 5120 O O . HOH P 7 . ? 47.046 37.914 45.108 1.00 16.78 ? 527 HOH A O 1 HETATM 5121 O O . HOH P 7 . ? 34.728 10.744 35.998 1.00 32.04 ? 528 HOH A O 1 HETATM 5122 O O . HOH P 7 . ? 59.318 21.522 54.292 1.00 30.95 ? 529 HOH A O 1 HETATM 5123 O O . HOH P 7 . ? 42.480 11.218 40.974 1.00 26.20 ? 530 HOH A O 1 HETATM 5124 O O . HOH P 7 . ? 54.244 14.976 71.376 1.00 31.99 ? 531 HOH A O 1 HETATM 5125 O O . HOH P 7 . ? 60.212 7.729 63.182 1.00 32.41 ? 532 HOH A O 1 HETATM 5126 O O . HOH P 7 . ? 38.370 6.108 69.094 1.00 24.57 ? 533 HOH A O 1 HETATM 5127 O O . HOH P 7 . ? 68.688 29.825 67.786 1.00 15.00 ? 534 HOH A O 1 HETATM 5128 O O . HOH P 7 . ? 52.743 16.015 42.959 1.00 22.01 ? 535 HOH A O 1 HETATM 5129 O O . HOH P 7 . ? 31.369 16.189 51.952 1.00 14.89 ? 536 HOH A O 1 HETATM 5130 O O . HOH P 7 . ? 29.030 8.452 65.811 1.00 14.31 ? 537 HOH A O 1 HETATM 5131 O O . HOH P 7 . ? 57.064 -2.308 61.574 1.00 35.11 ? 538 HOH A O 1 HETATM 5132 O O . HOH P 7 . ? 56.942 18.112 43.848 1.00 22.48 ? 539 HOH A O 1 HETATM 5133 O O . HOH P 7 . ? 40.242 38.793 48.449 1.00 31.61 ? 540 HOH A O 1 HETATM 5134 O O . HOH P 7 . ? 38.703 3.870 45.425 1.00 19.05 ? 541 HOH A O 1 HETATM 5135 O O . HOH P 7 . ? 53.686 20.461 72.974 1.00 28.75 ? 542 HOH A O 1 HETATM 5136 O O . HOH P 7 . ? 36.578 20.347 62.930 1.00 20.34 ? 543 HOH A O 1 HETATM 5137 O O . HOH P 7 . ? 32.430 -3.368 59.239 1.00 21.29 ? 544 HOH A O 1 HETATM 5138 O O . HOH P 7 . ? 32.940 5.454 41.380 1.00 42.10 ? 545 HOH A O 1 HETATM 5139 O O . HOH P 7 . ? 64.932 14.838 51.455 1.00 32.30 ? 546 HOH A O 1 HETATM 5140 O O . HOH P 7 . ? 45.829 27.514 39.227 1.00 30.04 ? 547 HOH A O 1 HETATM 5141 O O . HOH P 7 . ? 52.050 13.673 44.151 1.00 20.84 ? 548 HOH A O 1 HETATM 5142 O O . HOH P 7 . ? 64.552 15.914 53.819 1.00 16.40 ? 549 HOH A O 1 HETATM 5143 O O . HOH P 7 . ? 38.169 36.435 61.023 1.00 16.10 ? 550 HOH A O 1 HETATM 5144 O O . HOH P 7 . ? 44.637 2.420 67.023 1.00 38.87 ? 551 HOH A O 1 HETATM 5145 O O . HOH P 7 . ? 33.202 -10.544 54.751 1.00 33.10 ? 552 HOH A O 1 HETATM 5146 O O . HOH P 7 . ? 32.747 -2.863 56.731 1.00 23.98 ? 553 HOH A O 1 HETATM 5147 O O . HOH P 7 . ? 49.022 -0.044 55.629 1.00 17.61 ? 554 HOH A O 1 HETATM 5148 O O . HOH P 7 . ? 73.604 26.275 64.567 1.00 32.67 ? 555 HOH A O 1 HETATM 5149 O O . HOH P 7 . ? 33.926 32.340 63.599 1.00 36.73 ? 556 HOH A O 1 HETATM 5150 O O . HOH P 7 . ? 49.953 21.215 69.847 1.00 28.08 ? 557 HOH A O 1 HETATM 5151 O O . HOH P 7 . ? 73.467 18.056 57.533 1.00 34.09 ? 558 HOH A O 1 HETATM 5152 O O . HOH P 7 . ? 35.225 25.239 45.128 1.00 25.15 ? 559 HOH A O 1 HETATM 5153 O O . HOH P 7 . ? 30.862 12.275 44.844 1.00 19.61 ? 560 HOH A O 1 HETATM 5154 O O . HOH P 7 . ? 56.524 20.637 53.801 1.00 46.47 ? 561 HOH A O 1 HETATM 5155 O O . HOH P 7 . ? 41.693 27.682 66.780 1.00 21.93 ? 562 HOH A O 1 HETATM 5156 O O . HOH P 7 . ? 46.729 30.831 55.699 1.00 10.54 ? 563 HOH A O 1 HETATM 5157 O O . HOH P 7 . ? 69.424 16.474 61.703 1.00 38.87 ? 564 HOH A O 1 HETATM 5158 O O . HOH P 7 . ? 27.905 12.477 69.590 1.00 40.07 ? 565 HOH A O 1 HETATM 5159 O O . HOH P 7 . ? 25.168 16.100 63.679 1.00 23.67 ? 566 HOH A O 1 HETATM 5160 O O . HOH P 7 . ? 37.391 23.714 62.891 1.00 20.98 ? 567 HOH A O 1 HETATM 5161 O O . HOH P 7 . ? 53.951 14.945 68.788 1.00 16.16 ? 568 HOH A O 1 HETATM 5162 O O . HOH P 7 . ? 50.764 -0.499 59.252 1.00 19.29 ? 569 HOH A O 1 HETATM 5163 O O . HOH P 7 . ? 58.753 11.974 45.733 1.00 38.43 ? 570 HOH A O 1 HETATM 5164 O O . HOH P 7 . ? 32.296 7.806 61.926 1.00 9.35 ? 571 HOH A O 1 HETATM 5165 O O . HOH P 7 . ? 42.547 18.858 65.354 1.00 12.10 ? 572 HOH A O 1 HETATM 5166 O O . HOH P 7 . ? 63.553 32.281 57.902 1.00 12.91 ? 573 HOH A O 1 HETATM 5167 O O . HOH P 7 . ? 59.778 14.231 57.251 1.00 19.11 ? 574 HOH A O 1 HETATM 5168 O O . HOH P 7 . ? 29.775 2.811 53.151 1.00 37.14 ? 575 HOH A O 1 HETATM 5169 O O . HOH P 7 . ? 38.145 7.290 58.320 1.00 16.14 ? 576 HOH A O 1 HETATM 5170 O O . HOH P 7 . ? 53.871 25.274 44.032 1.00 22.10 ? 577 HOH A O 1 HETATM 5171 O O . HOH P 7 . ? 44.061 29.699 57.407 1.00 15.27 ? 578 HOH A O 1 HETATM 5172 O O . HOH P 7 . ? 54.000 35.807 58.265 1.00 14.92 ? 579 HOH A O 1 HETATM 5173 O O . HOH P 7 . ? 60.001 35.495 50.376 1.00 22.44 ? 580 HOH A O 1 HETATM 5174 O O . HOH P 7 . ? 36.797 5.061 57.695 1.00 15.73 ? 581 HOH A O 1 HETATM 5175 O O . HOH P 7 . ? 39.053 31.412 44.673 1.00 27.31 ? 582 HOH A O 1 HETATM 5176 O O . HOH P 7 . ? 48.043 6.969 38.963 1.00 43.55 ? 583 HOH A O 1 HETATM 5177 O O . HOH P 7 . ? 76.839 29.064 53.029 1.00 44.51 ? 584 HOH A O 1 HETATM 5178 O O . HOH P 7 . ? 45.474 -2.073 61.806 1.00 38.46 ? 585 HOH A O 1 HETATM 5179 O O . HOH P 7 . ? 26.286 13.380 60.120 1.00 18.13 ? 586 HOH A O 1 HETATM 5180 O O . HOH P 7 . ? 39.270 7.545 39.122 1.00 25.35 ? 587 HOH A O 1 HETATM 5181 O O . HOH P 7 . ? 50.574 27.095 73.694 1.00 33.92 ? 588 HOH A O 1 HETATM 5182 O O . HOH P 7 . ? 25.955 16.755 48.995 1.00 58.60 ? 589 HOH A O 1 HETATM 5183 O O . HOH P 7 . ? 26.966 6.799 56.755 1.00 38.36 ? 590 HOH A O 1 HETATM 5184 O O . HOH P 7 . ? 50.030 26.934 42.047 1.00 38.78 ? 591 HOH A O 1 HETATM 5185 O O . HOH P 7 . ? 51.217 37.411 52.242 1.00 22.81 ? 592 HOH A O 1 HETATM 5186 O O . HOH P 7 . ? 47.508 32.592 53.082 1.00 10.49 ? 593 HOH A O 1 HETATM 5187 O O . HOH P 7 . ? 45.969 23.579 69.318 1.00 18.67 ? 594 HOH A O 1 HETATM 5188 O O . HOH P 7 . ? 41.688 19.402 41.554 1.00 21.95 ? 595 HOH A O 1 HETATM 5189 O O . HOH P 7 . ? 62.838 11.761 64.302 1.00 33.45 ? 596 HOH A O 1 HETATM 5190 O O . HOH P 7 . ? 67.986 30.623 57.453 1.00 22.62 ? 597 HOH A O 1 HETATM 5191 O O . HOH P 7 . ? 68.164 10.581 60.165 1.00 58.69 ? 598 HOH A O 1 HETATM 5192 O O . HOH P 7 . ? 54.511 2.810 56.097 1.00 28.22 ? 599 HOH A O 1 HETATM 5193 O O . HOH P 7 . ? 35.909 25.253 55.410 1.00 28.64 ? 600 HOH A O 1 HETATM 5194 O O . HOH P 7 . ? 26.449 16.276 59.045 1.00 19.52 ? 601 HOH A O 1 HETATM 5195 O O . HOH P 7 . ? 46.327 34.557 38.454 1.00 32.38 ? 602 HOH A O 1 HETATM 5196 O O . HOH P 7 . ? 37.646 10.085 57.453 1.00 10.99 ? 603 HOH A O 1 HETATM 5197 O O . HOH P 7 . ? 54.081 27.419 55.633 1.00 31.96 ? 604 HOH A O 1 HETATM 5198 O O . HOH P 7 . ? 61.927 9.385 56.717 1.00 15.53 ? 605 HOH A O 1 HETATM 5199 O O . HOH P 7 . ? 77.724 32.714 55.316 1.00 37.64 ? 606 HOH A O 1 HETATM 5200 O O . HOH P 7 . ? 41.642 8.635 40.158 1.00 24.46 ? 607 HOH A O 1 HETATM 5201 O O . HOH P 7 . ? 27.772 13.404 57.108 1.00 30.79 ? 608 HOH A O 1 HETATM 5202 O O . HOH P 7 . ? 44.787 8.247 61.218 1.00 15.68 ? 609 HOH A O 1 HETATM 5203 O O . HOH P 7 . ? 31.030 -9.024 56.268 1.00 32.83 ? 610 HOH A O 1 HETATM 5204 O O . HOH P 7 . ? 61.141 18.514 45.059 1.00 37.97 ? 611 HOH A O 1 HETATM 5205 O O . HOH P 7 . ? 63.578 21.677 77.716 1.00 40.21 ? 612 HOH A O 1 HETATM 5206 O O . HOH P 7 . ? 49.637 10.775 66.184 1.00 15.23 ? 613 HOH A O 1 HETATM 5207 O O . HOH P 7 . ? 61.462 12.060 58.003 1.00 19.89 ? 614 HOH A O 1 HETATM 5208 O O . HOH P 7 . ? 56.670 27.425 72.473 1.00 35.17 ? 615 HOH A O 1 HETATM 5209 O O . HOH P 7 . ? 37.129 28.545 64.362 1.00 28.79 ? 616 HOH A O 1 HETATM 5210 O O . HOH P 7 . ? 44.151 -0.402 41.654 1.00 36.20 ? 617 HOH A O 1 HETATM 5211 O O . HOH P 7 . ? 63.329 34.435 55.735 1.00 25.52 ? 618 HOH A O 1 HETATM 5212 O O . HOH P 7 . ? 40.282 30.815 53.942 1.00 12.78 ? 619 HOH A O 1 HETATM 5213 O O . HOH P 7 . ? 61.329 38.749 56.637 1.00 31.08 ? 620 HOH A O 1 HETATM 5214 O O . HOH P 7 . ? 53.287 32.862 71.834 1.00 15.00 ? 621 HOH A O 1 HETATM 5215 O O . HOH P 7 . ? 50.942 19.282 74.096 1.00 15.00 ? 622 HOH A O 1 HETATM 5216 O O . HOH P 7 . ? 46.006 40.965 61.538 1.00 41.51 ? 623 HOH A O 1 HETATM 5217 O O . HOH P 7 . ? 54.541 37.257 70.986 1.00 39.69 ? 624 HOH A O 1 HETATM 5218 O O . HOH P 7 . ? 38.755 28.598 44.276 1.00 18.41 ? 625 HOH A O 1 HETATM 5219 O O . HOH P 7 . ? 54.628 27.811 43.571 1.00 28.08 ? 626 HOH A O 1 HETATM 5220 O O . HOH P 7 . ? 35.638 38.568 47.193 1.00 35.32 ? 627 HOH A O 1 HETATM 5221 O O . HOH P 7 . ? 39.716 20.890 69.447 1.00 32.69 ? 628 HOH A O 1 HETATM 5222 O O . HOH P 7 . ? 42.450 19.653 57.330 1.00 7.30 ? 629 HOH A O 1 HETATM 5223 O O . HOH P 7 . ? 36.590 30.950 56.045 1.00 26.00 ? 630 HOH A O 1 HETATM 5224 O O . HOH P 7 . ? 29.179 18.543 65.929 1.00 32.10 ? 631 HOH A O 1 HETATM 5225 O O . HOH P 7 . ? 31.403 9.896 45.748 1.00 16.45 ? 632 HOH A O 1 HETATM 5226 O O . HOH P 7 . ? 40.651 38.088 55.542 1.00 21.20 ? 633 HOH A O 1 HETATM 5227 O O . HOH P 7 . ? 59.599 14.537 45.862 1.00 37.36 ? 634 HOH A O 1 HETATM 5228 O O . HOH P 7 . ? 28.825 21.982 45.260 1.00 36.11 ? 635 HOH A O 1 HETATM 5229 O O . HOH P 7 . ? 35.848 24.463 48.992 1.00 40.10 ? 636 HOH A O 1 HETATM 5230 O O . HOH P 7 . ? 43.217 39.779 53.182 1.00 50.68 ? 637 HOH A O 1 HETATM 5231 O O . HOH P 7 . ? 58.422 17.254 50.528 1.00 16.35 ? 638 HOH A O 1 HETATM 5232 O O . HOH P 7 . ? 48.356 4.794 68.387 1.00 36.53 ? 639 HOH A O 1 HETATM 5233 O O . HOH P 7 . ? 51.371 -0.736 56.689 1.00 23.29 ? 640 HOH A O 1 HETATM 5234 O O . HOH P 7 . ? 69.606 25.742 47.640 1.00 39.96 ? 641 HOH A O 1 HETATM 5235 O O . HOH P 7 . ? 43.456 30.016 54.358 1.00 28.05 ? 642 HOH A O 1 HETATM 5236 O O . HOH P 7 . ? 59.222 23.824 70.861 1.00 21.08 ? 643 HOH A O 1 HETATM 5237 O O . HOH P 7 . ? 48.870 -2.495 58.641 1.00 15.00 ? 644 HOH A O 1 HETATM 5238 O O . HOH P 7 . ? 53.793 21.581 52.567 1.00 24.68 ? 645 HOH A O 1 HETATM 5239 O O . HOH P 7 . ? 55.080 8.597 69.568 1.00 27.56 ? 646 HOH A O 1 HETATM 5240 O O . HOH P 7 . ? 48.990 15.156 38.493 1.00 34.39 ? 647 HOH A O 1 HETATM 5241 O O . HOH P 7 . ? 55.647 6.176 53.066 1.00 38.91 ? 648 HOH A O 1 HETATM 5242 O O . HOH P 7 . ? 39.728 20.842 66.446 1.00 19.08 ? 649 HOH A O 1 HETATM 5243 O O . HOH P 7 . ? 59.981 5.590 56.617 1.00 21.95 ? 650 HOH A O 1 HETATM 5244 O O . HOH P 7 . ? 32.204 21.969 55.294 1.00 15.09 ? 651 HOH A O 1 HETATM 5245 O O . HOH P 7 . ? 69.572 15.503 51.938 1.00 40.73 ? 652 HOH A O 1 HETATM 5246 O O . HOH P 7 . ? 58.903 2.673 56.034 1.00 22.44 ? 653 HOH A O 1 HETATM 5247 O O . HOH P 7 . ? 50.157 -5.045 50.065 1.00 37.73 ? 654 HOH A O 1 HETATM 5248 O O . HOH P 7 . ? 56.005 -0.472 45.582 1.00 29.49 ? 655 HOH A O 1 HETATM 5249 O O . HOH P 7 . ? 59.863 33.826 46.077 1.00 25.92 ? 656 HOH A O 1 HETATM 5250 O O . HOH P 7 . ? 43.416 1.249 69.025 1.00 27.19 ? 657 HOH A O 1 HETATM 5251 O O . HOH P 7 . ? 48.077 19.285 70.479 1.00 45.52 ? 658 HOH A O 1 HETATM 5252 O O . HOH P 7 . ? 53.148 29.912 43.595 1.00 36.26 ? 659 HOH A O 1 HETATM 5253 O O . HOH P 7 . ? 55.926 -0.470 49.987 1.00 15.00 ? 660 HOH A O 1 HETATM 5254 O O . HOH P 7 . ? 38.414 28.958 54.629 1.00 30.80 ? 661 HOH A O 1 HETATM 5255 O O . HOH P 7 . ? 59.963 23.411 52.447 1.00 15.93 ? 662 HOH A O 1 HETATM 5256 O O . HOH P 7 . ? 51.322 40.678 61.884 1.00 42.54 ? 663 HOH A O 1 HETATM 5257 O O . HOH P 7 . ? 61.685 9.749 51.491 1.00 22.13 ? 664 HOH A O 1 HETATM 5258 O O . HOH P 7 . ? 39.078 34.537 37.919 1.00 38.65 ? 665 HOH A O 1 HETATM 5259 O O . HOH P 7 . ? 45.378 34.367 68.105 1.00 33.43 ? 666 HOH A O 1 HETATM 5260 O O . HOH P 7 . ? 59.012 40.961 59.996 1.00 38.69 ? 667 HOH A O 1 HETATM 5261 O O . HOH P 7 . ? 31.015 -4.721 55.868 1.00 25.05 ? 668 HOH A O 1 HETATM 5262 O O . HOH P 7 . ? 26.779 11.929 51.558 1.00 40.97 ? 669 HOH A O 1 HETATM 5263 O O . HOH P 7 . ? 41.829 29.156 38.409 1.00 31.34 ? 670 HOH A O 1 HETATM 5264 O O . HOH P 7 . ? 33.717 0.016 40.407 1.00 39.32 ? 671 HOH A O 1 HETATM 5265 O O . HOH P 7 . ? 57.074 35.551 46.334 1.00 38.16 ? 672 HOH A O 1 HETATM 5266 O O . HOH P 7 . ? 57.951 19.726 51.620 1.00 16.34 ? 673 HOH A O 1 HETATM 5267 O O . HOH P 7 . ? 30.165 14.869 46.016 1.00 12.83 ? 674 HOH A O 1 HETATM 5268 O O . HOH P 7 . ? 40.449 20.976 59.490 1.00 12.13 ? 675 HOH A O 1 HETATM 5269 O O . HOH P 7 . ? 31.079 9.217 40.568 1.00 37.14 ? 676 HOH A O 1 HETATM 5270 O O . HOH P 7 . ? 35.211 26.810 52.118 1.00 37.51 ? 677 HOH A O 1 HETATM 5271 O O . HOH P 7 . ? 41.694 26.336 70.276 1.00 15.00 ? 678 HOH A O 1 HETATM 5272 O O . HOH P 7 . ? 54.026 -1.748 51.408 1.00 34.16 ? 679 HOH A O 1 HETATM 5273 O O . HOH P 7 . ? 30.303 22.242 48.532 1.00 18.75 ? 680 HOH A O 1 HETATM 5274 O O . HOH P 7 . ? 30.481 16.172 43.663 1.00 18.99 ? 681 HOH A O 1 HETATM 5275 O O . HOH P 7 . ? 49.174 3.714 65.601 1.00 11.77 ? 682 HOH A O 1 HETATM 5276 O O . HOH P 7 . ? 35.748 18.161 38.409 1.00 38.87 ? 683 HOH A O 1 HETATM 5277 O O . HOH P 7 . ? 77.164 16.333 60.119 1.00 51.14 ? 684 HOH A O 1 HETATM 5278 O O . HOH P 7 . ? 44.632 14.068 37.925 1.00 32.32 ? 685 HOH A O 1 HETATM 5279 O O . HOH P 7 . ? 67.747 33.905 60.709 1.00 44.63 ? 686 HOH A O 1 HETATM 5280 O O . HOH P 7 . ? 64.313 1.532 60.612 1.00 28.18 ? 687 HOH A O 1 HETATM 5281 O O . HOH P 7 . ? 22.464 10.537 64.944 1.00 37.84 ? 688 HOH A O 1 HETATM 5282 O O . HOH P 7 . ? 31.446 20.771 63.972 1.00 15.00 ? 689 HOH A O 1 HETATM 5283 O O . HOH P 7 . ? 36.733 28.183 56.871 1.00 7.54 ? 690 HOH A O 1 HETATM 5284 O O . HOH P 7 . ? 63.517 36.578 53.570 1.00 15.00 ? 691 HOH A O 1 HETATM 5285 O O . HOH P 7 . ? 45.969 -1.282 64.891 1.00 31.70 ? 692 HOH A O 1 HETATM 5286 O O . HOH P 7 . ? 66.852 32.466 51.075 1.00 36.67 ? 693 HOH A O 1 HETATM 5287 O O . HOH P 7 . ? 45.397 28.410 76.870 1.00 41.66 ? 694 HOH A O 1 HETATM 5288 O O . HOH P 7 . ? 37.970 21.750 60.813 1.00 22.39 ? 695 HOH A O 1 HETATM 5289 O O . HOH P 7 . ? 26.109 1.330 65.496 1.00 49.81 ? 696 HOH A O 1 HETATM 5290 O O . HOH P 7 . ? 53.373 7.361 40.843 1.00 34.82 ? 697 HOH A O 1 HETATM 5291 O O . HOH P 7 . ? 62.207 15.769 75.924 1.00 38.90 ? 698 HOH A O 1 HETATM 5292 O O . HOH P 7 . ? 60.086 7.119 66.026 1.00 47.07 ? 699 HOH A O 1 HETATM 5293 O O . HOH P 7 . ? 46.162 4.874 69.776 1.00 15.00 ? 700 HOH A O 1 HETATM 5294 O O . HOH P 7 . ? 59.271 28.391 73.274 1.00 29.85 ? 701 HOH A O 1 HETATM 5295 O O . HOH P 7 . ? 24.659 1.640 62.866 1.00 47.67 ? 702 HOH A O 1 HETATM 5296 O O . HOH P 7 . ? 57.916 20.949 43.435 1.00 40.88 ? 703 HOH A O 1 HETATM 5297 O O . HOH P 7 . ? 38.856 -13.501 57.476 1.00 34.31 ? 704 HOH A O 1 HETATM 5298 O O . HOH P 7 . ? 72.882 30.652 62.125 1.00 51.86 ? 705 HOH A O 1 HETATM 5299 O O . HOH P 7 . ? 46.526 21.211 38.028 1.00 45.86 ? 706 HOH A O 1 HETATM 5300 O O . HOH P 7 . ? 57.344 24.846 72.549 1.00 42.52 ? 707 HOH A O 1 HETATM 5301 O O . HOH P 7 . ? 61.198 -5.993 56.002 1.00 28.51 ? 708 HOH A O 1 HETATM 5302 O O . HOH P 7 . ? 37.867 28.175 41.769 1.00 44.77 ? 709 HOH A O 1 HETATM 5303 O O . HOH P 7 . ? 55.414 36.589 50.857 1.00 31.50 ? 710 HOH A O 1 HETATM 5304 O O . HOH P 7 . ? 64.550 -1.283 56.628 1.00 26.27 ? 711 HOH A O 1 HETATM 5305 O O . HOH P 7 . ? 37.112 22.232 65.161 1.00 31.50 ? 712 HOH A O 1 HETATM 5306 O O . HOH P 7 . ? 79.029 30.788 53.874 1.00 36.94 ? 713 HOH A O 1 HETATM 5307 O O . HOH P 7 . ? 30.005 6.082 52.954 1.00 36.82 ? 714 HOH A O 1 HETATM 5308 O O . HOH P 7 . ? 24.258 12.005 58.828 1.00 41.37 ? 715 HOH A O 1 HETATM 5309 O O . HOH P 7 . ? 40.585 19.876 38.592 1.00 15.00 ? 716 HOH A O 1 HETATM 5310 O O . HOH P 7 . ? 51.453 24.720 42.455 1.00 39.69 ? 717 HOH A O 1 HETATM 5311 O O . HOH P 7 . ? 41.455 39.614 51.020 1.00 36.07 ? 718 HOH A O 1 HETATM 5312 O O . HOH P 7 . ? 61.103 0.897 54.845 1.00 41.67 ? 719 HOH A O 1 HETATM 5313 O O . HOH P 7 . ? 43.775 -3.273 63.471 1.00 15.00 ? 720 HOH A O 1 HETATM 5314 O O . HOH P 7 . ? 37.122 22.171 58.370 1.00 31.52 ? 721 HOH A O 1 HETATM 5315 O O . HOH P 7 . ? 22.437 13.939 51.810 1.00 34.65 ? 722 HOH A O 1 HETATM 5316 O O . HOH P 7 . ? 27.053 17.091 66.645 1.00 38.67 ? 723 HOH A O 1 HETATM 5317 O O . HOH P 7 . ? 53.657 12.449 42.284 1.00 37.65 ? 724 HOH A O 1 HETATM 5318 O O . HOH P 7 . ? 56.490 42.258 58.224 1.00 35.17 ? 725 HOH A O 1 HETATM 5319 O O . HOH P 7 . ? 30.967 -5.923 59.230 1.00 46.48 ? 726 HOH A O 1 HETATM 5320 O O . HOH P 7 . ? 25.597 15.493 56.642 1.00 41.26 ? 727 HOH A O 1 HETATM 5321 O O . HOH P 7 . ? 34.104 23.546 58.177 1.00 49.43 ? 728 HOH A O 1 HETATM 5322 O O . HOH P 7 . ? 36.774 31.726 46.149 1.00 31.73 ? 729 HOH A O 1 HETATM 5323 O O . HOH P 7 . ? 59.307 16.609 44.152 1.00 38.60 ? 730 HOH A O 1 HETATM 5324 O O . HOH P 7 . ? 60.702 10.288 46.802 1.00 32.43 ? 731 HOH A O 1 HETATM 5325 O O . HOH P 7 . ? 47.907 -2.579 61.182 1.00 42.58 ? 732 HOH A O 1 HETATM 5326 O O . HOH P 7 . ? 29.640 8.189 47.007 1.00 36.04 ? 733 HOH A O 1 HETATM 5327 O O . HOH P 7 . ? 75.403 29.780 63.031 1.00 33.94 ? 734 HOH A O 1 HETATM 5328 O O . HOH P 7 . ? 41.347 40.337 57.373 1.00 51.08 ? 735 HOH A O 1 HETATM 5329 O O . HOH P 7 . ? 51.743 29.220 41.277 1.00 34.59 ? 736 HOH A O 1 HETATM 5330 O O . HOH Q 7 . ? 45.608 62.236 24.038 1.00 15.00 ? 501 HOH B O 1 HETATM 5331 O O . HOH Q 7 . ? 53.282 56.759 11.237 1.00 19.50 ? 502 HOH B O 1 HETATM 5332 O O . HOH Q 7 . ? 58.035 22.427 24.315 1.00 42.45 ? 503 HOH B O 1 HETATM 5333 O O . HOH Q 7 . ? 41.592 49.244 28.567 1.00 17.82 ? 504 HOH B O 1 HETATM 5334 O O . HOH Q 7 . ? 38.213 23.215 6.091 1.00 20.10 ? 505 HOH B O 1 HETATM 5335 O O . HOH Q 7 . ? 27.466 33.640 30.938 1.00 39.77 ? 506 HOH B O 1 HETATM 5336 O O . HOH Q 7 . ? 53.378 41.867 34.572 1.00 27.10 ? 507 HOH B O 1 HETATM 5337 O O . HOH Q 7 . ? 59.495 43.917 11.996 1.00 23.02 ? 508 HOH B O 1 HETATM 5338 O O . HOH Q 7 . ? 44.493 37.489 29.676 1.00 9.70 ? 509 HOH B O 1 HETATM 5339 O O . HOH Q 7 . ? 38.944 25.733 6.546 1.00 10.83 ? 510 HOH B O 1 HETATM 5340 O O . HOH Q 7 . ? 59.258 43.294 16.287 1.00 29.85 ? 511 HOH B O 1 HETATM 5341 O O . HOH Q 7 . ? 35.633 40.856 32.310 1.00 33.95 ? 512 HOH B O 1 HETATM 5342 O O . HOH Q 7 . ? 43.345 61.654 15.540 1.00 37.73 ? 513 HOH B O 1 HETATM 5343 O O . HOH Q 7 . ? 53.932 47.196 6.036 1.00 23.37 ? 514 HOH B O 1 HETATM 5344 O O . HOH Q 7 . ? 44.857 23.923 28.342 1.00 15.00 ? 515 HOH B O 1 HETATM 5345 O O . HOH Q 7 . ? 40.520 61.057 10.891 1.00 40.13 ? 516 HOH B O 1 HETATM 5346 O O . HOH Q 7 . ? 56.491 49.008 34.176 1.00 21.69 ? 517 HOH B O 1 HETATM 5347 O O . HOH Q 7 . ? 56.559 55.664 18.647 1.00 33.60 ? 518 HOH B O 1 HETATM 5348 O O . HOH Q 7 . ? 49.666 15.353 13.334 1.00 13.44 ? 519 HOH B O 1 HETATM 5349 O O . HOH Q 7 . ? 39.403 29.585 0.504 1.00 17.70 ? 520 HOH B O 1 HETATM 5350 O O . HOH Q 7 . ? 57.018 16.615 16.371 1.00 26.25 ? 521 HOH B O 1 HETATM 5351 O O . HOH Q 7 . ? 29.770 27.038 16.893 1.00 29.07 ? 522 HOH B O 1 HETATM 5352 O O . HOH Q 7 . ? 33.053 24.948 30.410 1.00 24.64 ? 523 HOH B O 1 HETATM 5353 O O . HOH Q 7 . ? 36.877 56.518 11.843 1.00 34.78 ? 524 HOH B O 1 HETATM 5354 O O . HOH Q 7 . ? 49.061 21.795 17.055 1.00 8.67 ? 525 HOH B O 1 HETATM 5355 O O . HOH Q 7 . ? 42.429 40.454 27.060 1.00 10.49 ? 526 HOH B O 1 HETATM 5356 O O . HOH Q 7 . ? 54.465 24.833 17.611 1.00 21.55 ? 527 HOH B O 1 HETATM 5357 O O . HOH Q 7 . ? 44.164 26.187 29.755 1.00 25.40 ? 528 HOH B O 1 HETATM 5358 O O . HOH Q 7 . ? 61.763 50.465 33.695 1.00 29.86 ? 529 HOH B O 1 HETATM 5359 O O . HOH Q 7 . ? 56.230 21.151 8.596 1.00 37.21 ? 530 HOH B O 1 HETATM 5360 O O . HOH Q 7 . ? 29.123 30.028 27.145 1.00 16.37 ? 531 HOH B O 1 HETATM 5361 O O . HOH Q 7 . ? 59.227 56.522 25.796 1.00 24.17 ? 532 HOH B O 1 HETATM 5362 O O . HOH Q 7 . ? 32.733 18.816 17.847 1.00 15.45 ? 533 HOH B O 1 HETATM 5363 O O . HOH Q 7 . ? 53.103 53.763 34.256 1.00 39.83 ? 534 HOH B O 1 HETATM 5364 O O . HOH Q 7 . ? 54.367 21.387 23.558 1.00 32.41 ? 535 HOH B O 1 HETATM 5365 O O . HOH Q 7 . ? 44.570 24.482 1.790 1.00 39.92 ? 536 HOH B O 1 HETATM 5366 O O . HOH Q 7 . ? 47.981 57.251 15.166 1.00 12.15 ? 537 HOH B O 1 HETATM 5367 O O . HOH Q 7 . ? 34.949 12.177 22.163 1.00 32.46 ? 538 HOH B O 1 HETATM 5368 O O . HOH Q 7 . ? 32.394 18.413 20.472 1.00 12.61 ? 539 HOH B O 1 HETATM 5369 O O . HOH Q 7 . ? 31.356 13.052 17.508 1.00 25.70 ? 540 HOH B O 1 HETATM 5370 O O . HOH Q 7 . ? 42.693 33.337 2.600 1.00 26.63 ? 541 HOH B O 1 HETATM 5371 O O . HOH Q 7 . ? 62.139 19.583 16.903 1.00 39.80 ? 542 HOH B O 1 HETATM 5372 O O . HOH Q 7 . ? 65.007 34.837 29.854 1.00 37.96 ? 543 HOH B O 1 HETATM 5373 O O . HOH Q 7 . ? 71.618 51.779 21.904 1.00 16.86 ? 544 HOH B O 1 HETATM 5374 O O . HOH Q 7 . ? 59.840 36.235 18.956 1.00 15.43 ? 545 HOH B O 1 HETATM 5375 O O . HOH Q 7 . ? 38.356 43.182 18.379 1.00 15.00 ? 546 HOH B O 1 HETATM 5376 O O . HOH Q 7 . ? 50.310 48.461 35.409 1.00 27.40 ? 547 HOH B O 1 HETATM 5377 O O . HOH Q 7 . ? 56.831 40.308 5.514 1.00 27.14 ? 548 HOH B O 1 HETATM 5378 O O . HOH Q 7 . ? 38.441 36.912 14.649 1.00 12.90 ? 549 HOH B O 1 HETATM 5379 O O . HOH Q 7 . ? 45.788 44.812 31.182 1.00 14.31 ? 550 HOH B O 1 HETATM 5380 O O . HOH Q 7 . ? 55.507 57.619 15.420 1.00 22.92 ? 551 HOH B O 1 HETATM 5381 O O . HOH Q 7 . ? 50.754 21.402 20.896 1.00 19.56 ? 552 HOH B O 1 HETATM 5382 O O . HOH Q 7 . ? 52.029 35.720 5.759 1.00 15.97 ? 553 HOH B O 1 HETATM 5383 O O . HOH Q 7 . ? 47.372 54.536 14.973 1.00 10.85 ? 554 HOH B O 1 HETATM 5384 O O . HOH Q 7 . ? 66.835 54.194 11.935 1.00 47.21 ? 555 HOH B O 1 HETATM 5385 O O . HOH Q 7 . ? 56.330 42.587 15.717 1.00 28.08 ? 556 HOH B O 1 HETATM 5386 O O . HOH Q 7 . ? 30.076 24.632 14.431 1.00 22.53 ? 557 HOH B O 1 HETATM 5387 O O . HOH Q 7 . ? 54.845 50.041 5.634 1.00 30.78 ? 558 HOH B O 1 HETATM 5388 O O . HOH Q 7 . ? 32.085 33.874 0.541 1.00 41.84 ? 559 HOH B O 1 HETATM 5389 O O . HOH Q 7 . ? 59.375 36.737 7.757 1.00 29.37 ? 560 HOH B O 1 HETATM 5390 O O . HOH Q 7 . ? 36.364 41.987 24.443 1.00 17.34 ? 561 HOH B O 1 HETATM 5391 O O . HOH Q 7 . ? 64.661 38.039 15.603 1.00 17.15 ? 562 HOH B O 1 HETATM 5392 O O . HOH Q 7 . ? 57.366 19.261 22.910 1.00 32.37 ? 563 HOH B O 1 HETATM 5393 O O . HOH Q 7 . ? 49.011 36.017 34.412 1.00 21.25 ? 564 HOH B O 1 HETATM 5394 O O . HOH Q 7 . ? 63.339 54.018 19.952 1.00 12.53 ? 565 HOH B O 1 HETATM 5395 O O . HOH Q 7 . ? 57.985 44.566 6.689 1.00 15.00 ? 566 HOH B O 1 HETATM 5396 O O . HOH Q 7 . ? 73.216 40.060 19.247 1.00 30.51 ? 567 HOH B O 1 HETATM 5397 O O . HOH Q 7 . ? 83.452 45.227 19.276 1.00 30.94 ? 568 HOH B O 1 HETATM 5398 O O . HOH Q 7 . ? 30.965 34.178 6.317 1.00 20.29 ? 569 HOH B O 1 HETATM 5399 O O . HOH Q 7 . ? 41.760 41.583 3.170 1.00 15.99 ? 570 HOH B O 1 HETATM 5400 O O . HOH Q 7 . ? 53.838 57.705 20.550 1.00 17.14 ? 571 HOH B O 1 HETATM 5401 O O . HOH Q 7 . ? 44.886 28.486 35.167 1.00 15.00 ? 572 HOH B O 1 HETATM 5402 O O . HOH Q 7 . ? 43.861 51.507 19.274 1.00 17.95 ? 573 HOH B O 1 HETATM 5403 O O . HOH Q 7 . ? 33.612 9.775 13.864 1.00 27.15 ? 574 HOH B O 1 HETATM 5404 O O . HOH Q 7 . ? 37.591 31.763 18.741 1.00 11.42 ? 575 HOH B O 1 HETATM 5405 O O . HOH Q 7 . ? 62.720 33.803 26.015 1.00 30.69 ? 576 HOH B O 1 HETATM 5406 O O . HOH Q 7 . ? 26.215 35.041 21.535 1.00 14.89 ? 577 HOH B O 1 HETATM 5407 O O . HOH Q 7 . ? 41.862 51.319 0.748 1.00 37.36 ? 578 HOH B O 1 HETATM 5408 O O . HOH Q 7 . ? 55.712 28.177 14.836 1.00 36.64 ? 579 HOH B O 1 HETATM 5409 O O . HOH Q 7 . ? 38.210 29.082 19.563 1.00 9.47 ? 580 HOH B O 1 HETATM 5410 O O . HOH Q 7 . ? 67.728 52.366 19.430 1.00 22.13 ? 581 HOH B O 1 HETATM 5411 O O . HOH Q 7 . ? 30.494 14.003 9.690 1.00 32.84 ? 582 HOH B O 1 HETATM 5412 O O . HOH Q 7 . ? 69.445 38.400 23.563 1.00 35.73 ? 583 HOH B O 1 HETATM 5413 O O . HOH Q 7 . ? 54.586 61.262 21.730 1.00 38.61 ? 584 HOH B O 1 HETATM 5414 O O . HOH Q 7 . ? 32.180 29.448 23.262 1.00 12.82 ? 585 HOH B O 1 HETATM 5415 O O . HOH Q 7 . ? 62.550 59.098 28.405 1.00 43.02 ? 586 HOH B O 1 HETATM 5416 O O . HOH Q 7 . ? 46.682 52.838 17.552 1.00 13.67 ? 587 HOH B O 1 HETATM 5417 O O . HOH Q 7 . ? 50.220 24.379 8.586 1.00 35.93 ? 588 HOH B O 1 HETATM 5418 O O . HOH Q 7 . ? 46.460 32.783 36.595 1.00 30.49 ? 589 HOH B O 1 HETATM 5419 O O . HOH Q 7 . ? 68.569 51.701 29.700 1.00 25.61 ? 590 HOH B O 1 HETATM 5420 O O . HOH Q 7 . ? 40.632 42.961 17.840 1.00 26.16 ? 591 HOH B O 1 HETATM 5421 O O . HOH Q 7 . ? 37.716 21.045 38.446 1.00 32.16 ? 592 HOH B O 1 HETATM 5422 O O . HOH Q 7 . ? 35.110 47.259 7.111 1.00 46.53 ? 593 HOH B O 1 HETATM 5423 O O . HOH Q 7 . ? 43.521 19.293 -4.813 1.00 34.00 ? 594 HOH B O 1 HETATM 5424 O O . HOH Q 7 . ? 33.222 11.251 16.058 1.00 27.82 ? 595 HOH B O 1 HETATM 5425 O O . HOH Q 7 . ? 27.559 34.953 18.373 1.00 28.76 ? 596 HOH B O 1 HETATM 5426 O O . HOH Q 7 . ? 46.684 51.117 36.096 1.00 34.45 ? 597 HOH B O 1 HETATM 5427 O O . HOH Q 7 . ? 38.883 53.520 6.673 1.00 33.11 ? 598 HOH B O 1 HETATM 5428 O O . HOH Q 7 . ? 31.377 37.760 13.507 1.00 13.75 ? 599 HOH B O 1 HETATM 5429 O O . HOH Q 7 . ? 52.780 38.169 4.560 1.00 20.86 ? 600 HOH B O 1 HETATM 5430 O O . HOH Q 7 . ? 29.098 39.956 27.179 1.00 42.74 ? 601 HOH B O 1 HETATM 5431 O O . HOH Q 7 . ? 76.746 51.124 15.146 1.00 40.28 ? 602 HOH B O 1 HETATM 5432 O O . HOH Q 7 . ? 40.116 52.669 15.873 1.00 19.17 ? 603 HOH B O 1 HETATM 5433 O O . HOH Q 7 . ? 37.300 45.282 24.518 1.00 20.09 ? 604 HOH B O 1 HETATM 5434 O O . HOH Q 7 . ? 35.615 60.425 9.414 1.00 35.73 ? 605 HOH B O 1 HETATM 5435 O O . HOH Q 7 . ? 25.884 38.418 10.142 1.00 28.03 ? 606 HOH B O 1 HETATM 5436 O O . HOH Q 7 . ? 47.223 40.804 32.438 1.00 41.34 ? 607 HOH B O 1 HETATM 5437 O O . HOH Q 7 . ? 70.500 42.820 14.310 1.00 30.86 ? 608 HOH B O 1 HETATM 5438 O O . HOH Q 7 . ? 58.361 39.241 12.203 1.00 11.37 ? 609 HOH B O 1 HETATM 5439 O O . HOH Q 7 . ? 61.583 33.930 19.667 1.00 19.04 ? 610 HOH B O 1 HETATM 5440 O O . HOH Q 7 . ? 43.052 52.045 16.397 1.00 34.32 ? 611 HOH B O 1 HETATM 5441 O O . HOH Q 7 . ? 43.845 24.944 -5.414 1.00 38.00 ? 612 HOH B O 1 HETATM 5442 O O . HOH Q 7 . ? 64.610 36.991 13.266 1.00 31.32 ? 613 HOH B O 1 HETATM 5443 O O . HOH Q 7 . ? 49.529 42.609 31.605 1.00 21.79 ? 614 HOH B O 1 HETATM 5444 O O . HOH Q 7 . ? 37.942 58.156 22.965 1.00 19.64 ? 615 HOH B O 1 HETATM 5445 O O . HOH Q 7 . ? 47.090 59.898 7.190 1.00 41.50 ? 616 HOH B O 1 HETATM 5446 O O . HOH Q 7 . ? 26.989 28.328 17.699 1.00 29.79 ? 617 HOH B O 1 HETATM 5447 O O . HOH Q 7 . ? 51.315 62.181 24.107 1.00 15.00 ? 618 HOH B O 1 HETATM 5448 O O . HOH Q 7 . ? 60.386 29.475 25.076 1.00 26.68 ? 619 HOH B O 1 HETATM 5449 O O . HOH Q 7 . ? 49.463 32.274 27.658 1.00 13.19 ? 620 HOH B O 1 HETATM 5450 O O . HOH Q 7 . ? 31.150 16.852 16.995 1.00 19.08 ? 621 HOH B O 1 HETATM 5451 O O . HOH Q 7 . ? 66.722 53.177 17.207 1.00 33.44 ? 622 HOH B O 1 HETATM 5452 O O . HOH Q 7 . ? 38.276 27.648 30.659 1.00 15.47 ? 623 HOH B O 1 HETATM 5453 O O . HOH Q 7 . ? 36.744 26.836 19.062 1.00 10.34 ? 624 HOH B O 1 HETATM 5454 O O . HOH Q 7 . ? 40.564 59.941 17.437 1.00 25.76 ? 625 HOH B O 1 HETATM 5455 O O . HOH Q 7 . ? 26.286 38.214 20.535 1.00 22.77 ? 626 HOH B O 1 HETATM 5456 O O . HOH Q 7 . ? 45.788 19.792 23.081 1.00 30.28 ? 627 HOH B O 1 HETATM 5457 O O . HOH Q 7 . ? 64.483 56.021 11.900 1.00 34.59 ? 628 HOH B O 1 HETATM 5458 O O . HOH Q 7 . ? 42.366 41.326 19.119 1.00 7.83 ? 629 HOH B O 1 HETATM 5459 O O . HOH Q 7 . ? 62.026 31.004 18.334 1.00 20.10 ? 630 HOH B O 1 HETATM 5460 O O . HOH Q 7 . ? 50.831 59.384 14.416 1.00 25.05 ? 631 HOH B O 1 HETATM 5461 O O . HOH Q 7 . ? 74.808 40.301 15.456 1.00 34.50 ? 632 HOH B O 1 HETATM 5462 O O . HOH Q 7 . ? 31.421 24.858 6.137 1.00 30.79 ? 633 HOH B O 1 HETATM 5463 O O . HOH Q 7 . ? 28.782 43.094 5.756 1.00 34.72 ? 634 HOH B O 1 HETATM 5464 O O . HOH Q 7 . ? 37.253 50.162 26.237 1.00 29.41 ? 635 HOH B O 1 HETATM 5465 O O . HOH Q 7 . ? 59.083 45.252 32.794 1.00 16.47 ? 636 HOH B O 1 HETATM 5466 O O . HOH Q 7 . ? 40.363 42.708 21.351 1.00 13.43 ? 637 HOH B O 1 HETATM 5467 O O . HOH Q 7 . ? 53.280 29.528 33.514 1.00 37.26 ? 638 HOH B O 1 HETATM 5468 O O . HOH Q 7 . ? 65.098 45.996 6.643 1.00 15.00 ? 639 HOH B O 1 HETATM 5469 O O . HOH Q 7 . ? 59.902 27.538 18.538 1.00 19.45 ? 640 HOH B O 1 HETATM 5470 O O . HOH Q 7 . ? 36.337 52.608 18.007 1.00 30.04 ? 641 HOH B O 1 HETATM 5471 O O . HOH Q 7 . ? 42.832 15.028 24.016 1.00 15.00 ? 642 HOH B O 1 HETATM 5472 O O . HOH Q 7 . ? 44.730 29.920 22.676 1.00 7.84 ? 643 HOH B O 1 HETATM 5473 O O . HOH Q 7 . ? 63.182 19.961 22.032 1.00 47.86 ? 644 HOH B O 1 HETATM 5474 O O . HOH Q 7 . ? 53.802 36.508 30.775 1.00 17.94 ? 645 HOH B O 1 HETATM 5475 O O . HOH Q 7 . ? 52.728 51.979 5.656 1.00 37.01 ? 646 HOH B O 1 HETATM 5476 O O . HOH Q 7 . ? 59.879 57.597 12.341 1.00 23.53 ? 647 HOH B O 1 HETATM 5477 O O . HOH Q 7 . ? 35.847 47.126 17.232 1.00 26.82 ? 648 HOH B O 1 HETATM 5478 O O . HOH Q 7 . ? 31.495 31.731 7.200 1.00 12.85 ? 649 HOH B O 1 HETATM 5479 O O . HOH Q 7 . ? 73.029 39.941 27.898 1.00 49.55 ? 650 HOH B O 1 HETATM 5480 O O . HOH Q 7 . ? 45.206 56.233 30.079 1.00 38.58 ? 651 HOH B O 1 HETATM 5481 O O . HOH Q 7 . ? 47.708 56.459 5.068 1.00 15.00 ? 652 HOH B O 1 HETATM 5482 O O . HOH Q 7 . ? 57.995 41.848 13.417 1.00 12.61 ? 653 HOH B O 1 HETATM 5483 O O . HOH Q 7 . ? 55.160 19.229 15.386 1.00 34.07 ? 654 HOH B O 1 HETATM 5484 O O . HOH Q 7 . ? 61.798 31.820 13.207 1.00 23.36 ? 655 HOH B O 1 HETATM 5485 O O . HOH Q 7 . ? 54.007 49.383 17.910 1.00 27.47 ? 656 HOH B O 1 HETATM 5486 O O . HOH Q 7 . ? 38.624 50.704 6.202 1.00 21.09 ? 657 HOH B O 1 HETATM 5487 O O . HOH Q 7 . ? 30.065 43.831 10.102 1.00 17.15 ? 658 HOH B O 1 HETATM 5488 O O . HOH Q 7 . ? 58.394 28.604 11.644 1.00 30.17 ? 659 HOH B O 1 HETATM 5489 O O . HOH Q 7 . ? 43.692 32.890 35.345 1.00 30.09 ? 660 HOH B O 1 HETATM 5490 O O . HOH Q 7 . ? 39.660 42.389 28.157 1.00 17.90 ? 661 HOH B O 1 HETATM 5491 O O . HOH Q 7 . ? 59.885 45.367 14.224 1.00 14.35 ? 662 HOH B O 1 HETATM 5492 O O . HOH Q 7 . ? 25.039 37.894 25.105 1.00 26.19 ? 663 HOH B O 1 HETATM 5493 O O . HOH Q 7 . ? 36.212 45.385 10.411 1.00 22.76 ? 664 HOH B O 1 HETATM 5494 O O . HOH Q 7 . ? 41.901 30.855 1.446 1.00 16.06 ? 665 HOH B O 1 HETATM 5495 O O . HOH Q 7 . ? 59.052 34.148 7.850 1.00 36.88 ? 666 HOH B O 1 HETATM 5496 O O . HOH Q 7 . ? 73.833 47.871 26.543 1.00 37.78 ? 667 HOH B O 1 HETATM 5497 O O . HOH Q 7 . ? 38.509 16.100 3.089 1.00 32.57 ? 668 HOH B O 1 HETATM 5498 O O . HOH Q 7 . ? 58.866 24.879 17.776 1.00 28.24 ? 669 HOH B O 1 HETATM 5499 O O . HOH Q 7 . ? 61.485 60.451 18.582 1.00 33.88 ? 670 HOH B O 1 HETATM 5500 O O . HOH Q 7 . ? 55.163 30.202 31.207 1.00 22.37 ? 671 HOH B O 1 HETATM 5501 O O . HOH Q 7 . ? 31.185 30.803 2.417 1.00 29.42 ? 672 HOH B O 1 HETATM 5502 O O . HOH Q 7 . ? 63.065 56.578 18.371 1.00 38.96 ? 673 HOH B O 1 HETATM 5503 O O . HOH Q 7 . ? 47.009 37.199 36.941 1.00 26.36 ? 674 HOH B O 1 HETATM 5504 O O . HOH Q 7 . ? 43.496 22.823 30.388 1.00 20.76 ? 675 HOH B O 1 HETATM 5505 O O . HOH Q 7 . ? 77.352 40.266 16.101 1.00 45.41 ? 676 HOH B O 1 HETATM 5506 O O . HOH Q 7 . ? 43.505 46.842 32.864 1.00 27.38 ? 677 HOH B O 1 HETATM 5507 O O . HOH Q 7 . ? 30.372 39.514 30.027 1.00 25.38 ? 678 HOH B O 1 HETATM 5508 O O . HOH Q 7 . ? 61.949 32.041 28.074 1.00 35.63 ? 679 HOH B O 1 HETATM 5509 O O . HOH Q 7 . ? 38.173 50.863 16.565 1.00 24.69 ? 680 HOH B O 1 HETATM 5510 O O . HOH Q 7 . ? 53.919 20.340 12.987 1.00 42.02 ? 681 HOH B O 1 HETATM 5511 O O . HOH Q 7 . ? 68.253 32.489 22.573 1.00 15.00 ? 682 HOH B O 1 HETATM 5512 O O . HOH Q 7 . ? 31.993 43.729 16.982 1.00 15.33 ? 683 HOH B O 1 HETATM 5513 O O . HOH Q 7 . ? 30.667 38.043 5.005 1.00 16.21 ? 684 HOH B O 1 HETATM 5514 O O . HOH Q 7 . ? 51.378 21.055 18.038 1.00 12.77 ? 685 HOH B O 1 HETATM 5515 O O . HOH Q 7 . ? 73.336 50.541 27.497 1.00 37.94 ? 686 HOH B O 1 HETATM 5516 O O . HOH Q 7 . ? 22.424 32.362 26.326 1.00 32.50 ? 687 HOH B O 1 HETATM 5517 O O . HOH Q 7 . ? 70.052 47.929 9.770 1.00 30.47 ? 688 HOH B O 1 HETATM 5518 O O . HOH Q 7 . ? 33.380 11.501 19.011 1.00 25.80 ? 689 HOH B O 1 HETATM 5519 O O . HOH Q 7 . ? 30.209 36.713 7.392 1.00 13.63 ? 690 HOH B O 1 HETATM 5520 O O . HOH Q 7 . ? 53.799 36.361 33.502 1.00 29.71 ? 691 HOH B O 1 HETATM 5521 O O . HOH Q 7 . ? 36.592 28.131 -1.492 1.00 33.66 ? 692 HOH B O 1 HETATM 5522 O O . HOH Q 7 . ? 56.297 21.574 11.246 1.00 34.05 ? 693 HOH B O 1 HETATM 5523 O O . HOH Q 7 . ? 59.319 62.640 21.833 1.00 30.70 ? 694 HOH B O 1 HETATM 5524 O O . HOH Q 7 . ? 47.811 26.410 30.048 1.00 30.80 ? 695 HOH B O 1 HETATM 5525 O O . HOH Q 7 . ? 63.659 33.888 12.260 1.00 40.47 ? 696 HOH B O 1 HETATM 5526 O O . HOH Q 7 . ? 59.531 28.801 27.559 1.00 41.23 ? 697 HOH B O 1 HETATM 5527 O O . HOH Q 7 . ? 49.254 25.318 27.052 1.00 6.33 ? 698 HOH B O 1 HETATM 5528 O O . HOH Q 7 . ? 54.256 26.490 27.897 1.00 47.31 ? 699 HOH B O 1 HETATM 5529 O O . HOH Q 7 . ? 37.219 29.889 32.570 1.00 33.93 ? 700 HOH B O 1 HETATM 5530 O O . HOH Q 7 . ? 50.634 16.750 11.348 1.00 37.51 ? 701 HOH B O 1 HETATM 5531 O O . HOH Q 7 . ? 44.732 36.327 -0.366 1.00 30.07 ? 702 HOH B O 1 HETATM 5532 O O . HOH Q 7 . ? 28.943 26.445 32.780 1.00 53.57 ? 703 HOH B O 1 HETATM 5533 O O . HOH Q 7 . ? 36.390 49.923 18.735 1.00 10.17 ? 704 HOH B O 1 HETATM 5534 O O . HOH Q 7 . ? 26.355 22.643 26.556 1.00 36.81 ? 705 HOH B O 1 HETATM 5535 O O . HOH Q 7 . ? 60.175 55.685 8.668 1.00 37.00 ? 706 HOH B O 1 HETATM 5536 O O . HOH Q 7 . ? 48.969 19.390 20.334 1.00 35.32 ? 707 HOH B O 1 HETATM 5537 O O . HOH Q 7 . ? 45.833 26.301 31.714 1.00 35.68 ? 708 HOH B O 1 HETATM 5538 O O . HOH Q 7 . ? 57.115 57.659 9.060 1.00 35.71 ? 709 HOH B O 1 HETATM 5539 O O . HOH Q 7 . ? 36.023 40.523 0.328 1.00 38.84 ? 710 HOH B O 1 HETATM 5540 O O . HOH Q 7 . ? 52.706 64.392 28.299 1.00 36.41 ? 711 HOH B O 1 HETATM 5541 O O . HOH Q 7 . ? 64.403 23.433 22.240 1.00 24.19 ? 712 HOH B O 1 HETATM 5542 O O . HOH Q 7 . ? 64.949 46.129 36.051 1.00 46.47 ? 713 HOH B O 1 HETATM 5543 O O . HOH Q 7 . ? 69.528 38.025 13.936 1.00 35.37 ? 714 HOH B O 1 HETATM 5544 O O . HOH Q 7 . ? 44.738 21.977 3.331 1.00 27.94 ? 715 HOH B O 1 HETATM 5545 O O . HOH Q 7 . ? 50.247 23.410 4.157 1.00 51.67 ? 716 HOH B O 1 HETATM 5546 O O . HOH Q 7 . ? 64.234 36.180 33.824 1.00 27.79 ? 717 HOH B O 1 HETATM 5547 O O . HOH Q 7 . ? 45.641 44.147 0.486 1.00 42.01 ? 718 HOH B O 1 HETATM 5548 O O . HOH Q 7 . ? 61.284 16.138 17.230 1.00 22.64 ? 719 HOH B O 1 HETATM 5549 O O . HOH Q 7 . ? 30.542 27.548 14.364 1.00 36.65 ? 720 HOH B O 1 HETATM 5550 O O . HOH Q 7 . ? 65.723 36.434 27.508 1.00 38.02 ? 721 HOH B O 1 HETATM 5551 O O . HOH Q 7 . ? 51.612 63.477 21.846 1.00 42.44 ? 722 HOH B O 1 HETATM 5552 O O . HOH Q 7 . ? 40.926 42.197 0.723 1.00 28.16 ? 723 HOH B O 1 HETATM 5553 O O . HOH Q 7 . ? 37.700 43.289 22.548 1.00 26.30 ? 724 HOH B O 1 HETATM 5554 O O . HOH Q 7 . ? 42.589 44.192 33.223 1.00 43.22 ? 725 HOH B O 1 HETATM 5555 O O . HOH Q 7 . ? 57.041 46.312 34.152 1.00 30.74 ? 726 HOH B O 1 HETATM 5556 O O . HOH Q 7 . ? 55.107 58.495 13.078 1.00 39.32 ? 727 HOH B O 1 HETATM 5557 O O . HOH Q 7 . ? 55.014 44.700 35.573 1.00 39.78 ? 728 HOH B O 1 HETATM 5558 O O . HOH Q 7 . ? 55.802 33.474 4.524 1.00 36.72 ? 729 HOH B O 1 HETATM 5559 O O . HOH Q 7 . ? 53.996 30.032 3.172 1.00 42.03 ? 730 HOH B O 1 HETATM 5560 O O . HOH Q 7 . ? 59.755 31.062 10.899 1.00 39.74 ? 731 HOH B O 1 HETATM 5561 O O . HOH Q 7 . ? 57.295 42.840 5.106 1.00 29.43 ? 732 HOH B O 1 HETATM 5562 O O . HOH Q 7 . ? 53.476 54.735 5.239 1.00 35.60 ? 733 HOH B O 1 HETATM 5563 O O . HOH Q 7 . ? 33.658 43.394 24.616 1.00 15.00 ? 734 HOH B O 1 HETATM 5564 O O . HOH Q 7 . ? 31.358 16.079 21.215 1.00 28.34 ? 735 HOH B O 1 HETATM 5565 O O . HOH Q 7 . ? 36.835 43.732 26.828 1.00 32.65 ? 736 HOH B O 1 HETATM 5566 O O . HOH Q 7 . ? 37.756 43.021 30.303 1.00 15.00 ? 737 HOH B O 1 HETATM 5567 O O . HOH Q 7 . ? 24.202 33.589 20.210 1.00 52.16 ? 738 HOH B O 1 HETATM 5568 O O . HOH Q 7 . ? 35.090 45.637 19.233 1.00 15.00 ? 739 HOH B O 1 HETATM 5569 O O . HOH Q 7 . ? 30.065 15.081 18.931 1.00 40.92 ? 740 HOH B O 1 HETATM 5570 O O . HOH Q 7 . ? 45.346 43.414 33.198 1.00 39.10 ? 741 HOH B O 1 HETATM 5571 O O . HOH Q 7 . ? 72.851 38.270 21.940 1.00 15.00 ? 742 HOH B O 1 HETATM 5572 O O . HOH Q 7 . ? 31.026 46.630 10.692 1.00 42.02 ? 743 HOH B O 1 HETATM 5573 O O . HOH Q 7 . ? 55.157 38.951 3.470 1.00 32.55 ? 744 HOH B O 1 HETATM 5574 O O . HOH Q 7 . ? 51.296 20.805 23.365 1.00 33.32 ? 745 HOH B O 1 HETATM 5575 O O . HOH Q 7 . ? 59.436 39.264 6.461 1.00 40.90 ? 746 HOH B O 1 HETATM 5576 O O . HOH Q 7 . ? 45.610 21.743 -5.177 1.00 44.92 ? 747 HOH B O 1 HETATM 5577 O O . HOH Q 7 . ? 36.940 53.787 8.459 1.00 34.37 ? 748 HOH B O 1 HETATM 5578 O O . HOH Q 7 . ? 36.812 43.873 20.176 1.00 26.93 ? 749 HOH B O 1 HETATM 5579 O O . HOH Q 7 . ? 25.665 37.512 18.001 1.00 32.17 ? 750 HOH B O 1 HETATM 5580 O O . HOH Q 7 . ? 56.409 45.727 4.667 1.00 39.95 ? 751 HOH B O 1 HETATM 5581 O O . HOH Q 7 . ? 60.831 32.249 8.790 1.00 31.27 ? 752 HOH B O 1 HETATM 5582 O O . HOH Q 7 . ? 57.257 59.206 11.500 1.00 43.08 ? 753 HOH B O 1 HETATM 5583 O O . HOH Q 7 . ? 29.063 26.914 7.629 1.00 36.09 ? 754 HOH B O 1 HETATM 5584 O O . HOH Q 7 . ? 48.875 55.999 2.690 1.00 15.00 ? 755 HOH B O 1 HETATM 5585 O O . HOH Q 7 . ? 29.206 19.877 28.607 1.00 41.60 ? 756 HOH B O 1 HETATM 5586 O O . HOH Q 7 . ? 32.500 12.958 21.063 1.00 42.69 ? 757 HOH B O 1 HETATM 5587 O O . HOH Q 7 . ? 29.772 29.985 8.556 1.00 28.76 ? 758 HOH B O 1 HETATM 5588 O O . HOH Q 7 . ? 51.954 14.047 13.008 1.00 34.20 ? 759 HOH B O 1 HETATM 5589 O O . HOH Q 7 . ? 38.903 30.598 37.442 1.00 47.54 ? 760 HOH B O 1 HETATM 5590 O O . HOH Q 7 . ? 38.415 39.258 -0.512 1.00 39.13 ? 761 HOH B O 1 HETATM 5591 O O . HOH Q 7 . ? 68.512 36.345 26.278 1.00 37.16 ? 762 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 GLY 1 2 ? ? ? A . n A 1 2 PRO 2 3 ? ? ? A . n A 1 3 GLY 3 4 ? ? ? A . n A 1 4 GLY 4 5 ? ? ? A . n A 1 5 GLY 5 6 ? ? ? A . n A 1 6 GLY 6 7 ? ? ? A . n A 1 7 SER 7 8 8 SER SER A . n A 1 8 VAL 8 9 9 VAL VAL A . n A 1 9 THR 9 10 10 THR THR A . n A 1 10 CYS 10 11 11 CYS CYS A . n A 1 11 PRO 11 12 12 PRO PRO A . n A 1 12 GLY 12 13 13 GLY GLY A . n A 1 13 GLY 13 14 14 GLY GLY A . n A 1 14 GLN 14 15 15 GLN GLN A . n A 1 15 SER 15 16 16 SER SER A . n A 1 16 THR 16 17 17 THR THR A . n A 1 17 SER 17 18 18 SER SER A . n A 1 18 ASN 18 19 19 ASN ASN A . n A 1 19 SER 19 20 20 SER SER A . n A 1 20 GLN 20 21 21 GLN GLN A . n A 1 21 CYS 21 22 22 CYS CYS A . n A 1 22 CYS 22 23 23 CYS CYS A . n A 1 23 VAL 23 24 24 VAL VAL A . n A 1 24 TRP 24 25 25 TRP TRP A . n A 1 25 PHE 25 26 26 PHE PHE A . n A 1 26 ASP 26 27 27 ASP ASP A . n A 1 27 VAL 27 28 28 VAL VAL A . n A 1 28 LEU 28 29 29 LEU LEU A . n A 1 29 ASP 29 30 30 ASP ASP A . n A 1 30 ASP 30 31 31 ASP ASP A . n A 1 31 LEU 31 32 32 LEU LEU A . n A 1 32 GLN 32 33 33 GLN GLN A . n A 1 33 THR 33 34 34 THR THR A . n A 1 34 ASN 34 35 35 ASN ASN A . n A 1 35 PHE 35 36 36 PHE PHE A . n A 1 36 TYR 36 37 37 TYR TYR A . n A 1 37 GLN 37 38 38 GLN GLN A . n A 1 38 GLY 38 39 39 GLY GLY A . n A 1 39 SER 39 40 40 SER SER A . n A 1 40 LYS 40 41 41 LYS LYS A . n A 1 41 CYS 41 42 42 CYS CYS A . n A 1 42 GLU 42 43 43 GLU GLU A . n A 1 43 SER 43 44 44 SER SER A . n A 1 44 PRO 44 45 45 PRO PRO A . n A 1 45 VAL 45 46 46 VAL VAL A . n A 1 46 ARG 46 47 47 ARG ARG A . n A 1 47 LYS 47 48 48 LYS LYS A . n A 1 48 ILE 48 49 49 ILE ILE A . n A 1 49 LEU 49 50 50 LEU LEU A . n A 1 50 ARG 50 51 51 ARG ARG A . n A 1 51 ILE 51 52 52 ILE ILE A . n A 1 52 VAL 52 53 53 VAL VAL A . n A 1 53 PHE 53 54 54 PHE PHE A . n A 1 54 HIS 54 55 55 HIS HIS A . n A 1 55 ASP 55 56 56 ASP ASP A . n A 1 56 ALA 56 57 57 ALA ALA A . n A 1 57 ILE 57 58 58 ILE ILE A . n A 1 58 GLY 58 59 59 GLY GLY A . n A 1 59 PHE 59 60 60 PHE PHE A . n A 1 60 SER 60 61 61 SER SER A . n A 1 61 PRO 61 62 62 PRO PRO A . n A 1 62 ALA 62 63 63 ALA ALA A . n A 1 63 LEU 63 64 64 LEU LEU A . n A 1 64 THR 64 65 65 THR THR A . n A 1 65 ALA 65 66 66 ALA ALA A . n A 1 66 ALA 66 67 67 ALA ALA A . n A 1 67 GLY 67 68 68 GLY GLY A . n A 1 68 GLN 68 69 69 GLN GLN A . n A 1 69 PHE 69 70 70 PHE PHE A . n A 1 70 GLY 70 71 71 GLY GLY A . n A 1 71 GLY 71 72 72 GLY GLY A . n A 1 72 GLY 72 73 73 GLY GLY A . n A 1 73 GLY 73 74 74 GLY GLY A . n A 1 74 ALA 74 75 75 ALA ALA A . n A 1 75 ASP 75 76 76 ASP ASP A . n A 1 76 GLY 76 77 77 GLY GLY A . n A 1 77 SER 77 78 78 SER SER A . n A 1 78 ILE 78 79 79 ILE ILE A . n A 1 79 ILE 79 80 80 ILE ILE A . n A 1 80 ALA 80 81 81 ALA ALA A . n A 1 81 HIS 81 82 82 HIS HIS A . n A 1 82 SER 82 83 83 SER SER A . n A 1 83 ASN 83 84 84 ASN ASN A . n A 1 84 ILE 84 85 85 ILE ILE A . n A 1 85 GLU 85 86 86 GLU GLU A . n A 1 86 LEU 86 87 87 LEU LEU A . n A 1 87 ALA 87 88 88 ALA ALA A . n A 1 88 PHE 88 89 89 PHE PHE A . n A 1 89 PRO 89 90 90 PRO PRO A . n A 1 90 ALA 90 91 91 ALA ALA A . n A 1 91 ASN 91 92 92 ASN ASN A . n A 1 92 GLY 92 93 93 GLY GLY A . n A 1 93 GLY 93 94 94 GLY GLY A . n A 1 94 LEU 94 95 95 LEU LEU A . n A 1 95 THR 95 96 96 THR THR A . n A 1 96 ASP 96 97 97 ASP ASP A . n A 1 97 THR 97 98 98 THR THR A . n A 1 98 VAL 98 99 99 VAL VAL A . n A 1 99 GLU 99 100 100 GLU GLU A . n A 1 100 ALA 100 101 101 ALA ALA A . n A 1 101 LEU 101 102 102 LEU LEU A . n A 1 102 ARG 102 103 103 ARG ARG A . n A 1 103 ALA 103 104 104 ALA ALA A . n A 1 104 VAL 104 105 105 VAL VAL A . n A 1 105 GLY 105 106 106 GLY GLY A . n A 1 106 ILE 106 107 107 ILE ILE A . n A 1 107 ASN 107 108 108 ASN ASN A . n A 1 108 HIS 108 109 109 HIS HIS A . n A 1 109 GLY 109 110 110 GLY GLY A . n A 1 110 VAL 110 111 111 VAL VAL A . n A 1 111 SER 111 112 112 SER SER A . n A 1 112 PHE 112 113 113 PHE PHE A . n A 1 113 GLY 113 114 114 GLY GLY A . n A 1 114 ASP 114 115 115 ASP ASP A . n A 1 115 LEU 115 116 116 LEU LEU A . n A 1 116 ILE 116 117 117 ILE ILE A . n A 1 117 GLN 117 118 118 GLN GLN A . n A 1 118 PHE 118 119 119 PHE PHE A . n A 1 119 ALA 119 120 120 ALA ALA A . n A 1 120 THR 120 121 121 THR THR A . n A 1 121 ALA 121 122 122 ALA ALA A . n A 1 122 VAL 122 123 123 VAL VAL A . n A 1 123 GLY 123 124 124 GLY GLY A . n A 1 124 MET 124 125 125 MET MET A . n A 1 125 SER 125 126 126 SER SER A . n A 1 126 ASN 126 127 127 ASN ASN A . n A 1 127 CYS 127 128 128 CYS CYS A . n A 1 128 PRO 128 129 129 PRO PRO A . n A 1 129 GLY 129 130 130 GLY GLY A . n A 1 130 SER 130 131 131 SER SER A . n A 1 131 PRO 131 132 132 PRO PRO A . n A 1 132 ARG 132 133 133 ARG ARG A . n A 1 133 LEU 133 134 134 LEU LEU A . n A 1 134 GLU 134 135 135 GLU GLU A . n A 1 135 PHE 135 136 136 PHE PHE A . n A 1 136 LEU 136 137 137 LEU LEU A . n A 1 137 THR 137 138 138 THR THR A . n A 1 138 GLY 138 139 139 GLY GLY A . n A 1 139 ARG 139 140 140 ARG ARG A . n A 1 140 SER 140 141 141 SER SER A . n A 1 141 ASN 141 142 142 ASN ASN A . n A 1 142 SER 142 143 143 SER SER A . n A 1 143 SER 143 144 144 SER SER A . n A 1 144 GLN 144 145 145 GLN GLN A . n A 1 145 PRO 145 146 146 PRO PRO A . n A 1 146 SER 146 147 147 SER SER A . n A 1 147 PRO 147 148 148 PRO PRO A . n A 1 148 PRO 148 149 149 PRO PRO A . n A 1 149 SER 149 150 150 SER SER A . n A 1 150 LEU 150 151 151 LEU LEU A . n A 1 151 ILE 151 152 152 ILE ILE A . n A 1 152 PRO 152 153 153 PRO PRO A . n A 1 153 GLY 153 154 154 GLY GLY A . n A 1 154 PRO 154 155 155 PRO PRO A . n A 1 155 GLY 155 156 156 GLY GLY A . n A 1 156 ASN 156 157 157 ASN ASN A . n A 1 157 THR 157 158 158 THR THR A . n A 1 158 VAL 158 159 159 VAL VAL A . n A 1 159 THR 159 160 160 THR THR A . n A 1 160 ALA 160 161 161 ALA ALA A . n A 1 161 ILE 161 162 162 ILE ILE A . n A 1 162 LEU 162 163 163 LEU LEU A . n A 1 163 ASP 163 164 164 ASP ASP A . n A 1 164 ARG 164 165 165 ARG ARG A . n A 1 165 MET 165 166 166 MET MET A . n A 1 166 GLY 166 167 167 GLY GLY A . n A 1 167 ASP 167 168 168 ASP ASP A . n A 1 168 ALA 168 169 169 ALA ALA A . n A 1 169 GLY 169 170 170 GLY GLY A . n A 1 170 PHE 170 171 171 PHE PHE A . n A 1 171 SER 171 172 172 SER SER A . n A 1 172 PRO 172 173 173 PRO PRO A . n A 1 173 ASP 173 174 174 ASP ASP A . n A 1 174 GLU 174 175 175 GLU GLU A . n A 1 175 VAL 175 176 176 VAL VAL A . n A 1 176 VAL 176 177 177 VAL VAL A . n A 1 177 ASP 177 178 178 ASP ASP A . n A 1 178 LEU 178 179 179 LEU LEU A . n A 1 179 LEU 179 180 180 LEU LEU A . n A 1 180 ALA 180 181 181 ALA ALA A . n A 1 181 ALA 181 182 182 ALA ALA A . n A 1 182 HSO 182 183 183 HSO HSO A . n A 1 183 SER 183 184 184 SER SER A . n A 1 184 LEU 184 185 185 LEU LEU A . n A 1 185 ALA 185 186 186 ALA ALA A . n A 1 186 SER 186 187 187 SER SER A . n A 1 187 GLN 187 188 188 GLN GLN A . n A 1 188 GLU 188 189 189 GLU GLU A . n A 1 189 GLY 189 190 190 GLY GLY A . n A 1 190 LEU 190 191 191 LEU LEU A . n A 1 191 ASN 191 192 192 ASN ASN A . n A 1 192 SER 192 193 193 SER SER A . n A 1 193 ALA 193 194 194 ALA ALA A . n A 1 194 ILE 194 195 195 ILE ILE A . n A 1 195 PHE 195 196 196 PHE PHE A . n A 1 196 ARG 196 197 197 ARG ARG A . n A 1 197 SER 197 198 198 SER SER A . n A 1 198 PRO 198 199 199 PRO PRO A . n A 1 199 LEU 199 200 200 LEU LEU A . n A 1 200 ASP 200 201 201 ASP ASP A . n A 1 201 SER 201 202 202 SER SER A . n A 1 202 THR 202 203 203 THR THR A . n A 1 203 PRO 203 204 204 PRO PRO A . n A 1 204 GLN 204 205 205 GLN GLN A . n A 1 205 VAL 205 206 206 VAL VAL A . n A 1 206 PHE 206 207 207 PHE PHE A . n A 1 207 ASP 207 208 208 ASP ASP A . n A 1 208 THR 208 209 209 THR THR A . n A 1 209 GLN 209 210 210 GLN GLN A . n A 1 210 PHE 210 211 211 PHE PHE A . n A 1 211 TYR 211 212 212 TYR TYR A . n A 1 212 ILE 212 213 213 ILE ILE A . n A 1 213 GLU 213 214 214 GLU GLU A . n A 1 214 THR 214 215 215 THR THR A . n A 1 215 LEU 215 216 216 LEU LEU A . n A 1 216 LEU 216 217 217 LEU LEU A . n A 1 217 LYS 217 218 218 LYS LYS A . n A 1 218 GLY 218 219 219 GLY GLY A . n A 1 219 THR 219 220 220 THR THR A . n A 1 220 THR 220 221 221 THR THR A . n A 1 221 GLN 221 222 222 GLN GLN A . n A 1 222 PRO 222 223 223 PRO PRO A . n A 1 223 GLY 223 224 224 GLY GLY A . n A 1 224 PRO 224 225 225 PRO PRO A . n A 1 225 SER 225 226 226 SER SER A . n A 1 226 LEU 226 227 227 LEU LEU A . n A 1 227 GLY 227 228 228 GLY GLY A . n A 1 228 PHE 228 229 229 PHE PHE A . n A 1 229 ALA 229 230 230 ALA ALA A . n A 1 230 GLU 230 231 231 GLU GLU A . n A 1 231 GLU 231 232 232 GLU GLU A . n A 1 232 LEU 232 233 233 LEU LEU A . n A 1 233 SER 233 234 234 SER SER A . n A 1 234 PRO 234 235 235 PRO PRO A . n A 1 235 PHE 235 236 236 PHE PHE A . n A 1 236 PRO 236 237 237 PRO PRO A . n A 1 237 GLY 237 238 238 GLY GLY A . n A 1 238 GLU 238 239 239 GLU GLU A . n A 1 239 PHE 239 240 240 PHE PHE A . n A 1 240 ARG 240 241 241 ARG ARG A . n A 1 241 MET 241 242 242 MET MET A . n A 1 242 ARG 242 243 243 ARG ARG A . n A 1 243 SER 243 244 244 SER SER A . n A 1 244 ASP 244 245 245 ASP ASP A . n A 1 245 ALA 245 246 246 ALA ALA A . n A 1 246 LEU 246 247 247 LEU LEU A . n A 1 247 LEU 247 248 248 LEU LEU A . n A 1 248 ALA 248 249 249 ALA ALA A . n A 1 249 ARG 249 250 250 ARG ARG A . n A 1 250 ASP 250 251 251 ASP ASP A . n A 1 251 SER 251 252 252 SER SER A . n A 1 252 ARG 252 253 253 ARG ARG A . n A 1 253 THR 253 254 254 THR THR A . n A 1 254 ALA 254 255 255 ALA ALA A . n A 1 255 CYS 255 256 256 CYS CYS A . n A 1 256 ARG 256 257 257 ARG ARG A . n A 1 257 TRP 257 258 258 TRP TRP A . n A 1 258 GLN 258 259 259 GLN GLN A . n A 1 259 SER 259 260 260 SER SER A . n A 1 260 MET 260 261 261 MET MET A . n A 1 261 THR 261 262 262 THR THR A . n A 1 262 SER 262 263 263 SER SER A . n A 1 263 SER 263 264 264 SER SER A . n A 1 264 ASN 264 265 265 ASN ASN A . n A 1 265 GLU 265 266 266 GLU GLU A . n A 1 266 VAL 266 267 267 VAL VAL A . n A 1 267 MET 267 268 268 MET MET A . n A 1 268 GLY 268 269 269 GLY GLY A . n A 1 269 GLN 269 270 270 GLN GLN A . n A 1 270 ARG 270 271 271 ARG ARG A . n A 1 271 TYR 271 272 272 TYR TYR A . n A 1 272 ARG 272 273 273 ARG ARG A . n A 1 273 ALA 273 274 274 ALA ALA A . n A 1 274 ALA 274 275 275 ALA ALA A . n A 1 275 MET 275 276 276 MET MET A . n A 1 276 ALA 276 277 277 ALA ALA A . n A 1 277 LYS 277 278 278 LYS LYS A . n A 1 278 MET 278 279 279 MET MET A . n A 1 279 SER 279 280 280 SER SER A . n A 1 280 VAL 280 281 281 VAL VAL A . n A 1 281 LEU 281 282 282 LEU LEU A . n A 1 282 GLY 282 283 283 GLY GLY A . n A 1 283 PHE 283 284 284 PHE PHE A . n A 1 284 ASP 284 285 285 ASP ASP A . n A 1 285 ARG 285 286 286 ARG ARG A . n A 1 286 ASN 286 287 287 ASN ASN A . n A 1 287 ALA 287 288 288 ALA ALA A . n A 1 288 LEU 288 289 289 LEU LEU A . n A 1 289 THR 289 290 290 THR THR A . n A 1 290 ASP 290 291 291 ASP ASP A . n A 1 291 CYS 291 292 292 CYS CYS A . n A 1 292 SER 292 293 293 SER SER A . n A 1 293 ASP 293 294 294 ASP ASP A . n A 1 294 VAL 294 295 295 VAL VAL A . n A 1 295 ILE 295 296 296 ILE ILE A . n A 1 296 PRO 296 297 297 PRO PRO A . n A 1 297 SER 297 298 298 SER SER A . n A 1 298 ALA 298 299 299 ALA ALA A . n A 1 299 VAL 299 300 300 VAL VAL A . n A 1 300 SER 300 301 301 SER SER A . n A 1 301 ASN 301 302 302 ASN ASN A . n A 1 302 ASN 302 303 303 ASN ASN A . n A 1 303 ALA 303 304 304 ALA ALA A . n A 1 304 ALA 304 305 305 ALA ALA A . n A 1 305 PRO 305 306 306 PRO PRO A . n A 1 306 VAL 306 307 307 VAL VAL A . n A 1 307 ILE 307 308 308 ILE ILE A . n A 1 308 PRO 308 309 309 PRO PRO A . n A 1 309 GLY 309 310 310 GLY GLY A . n A 1 310 GLY 310 311 311 GLY GLY A . n A 1 311 LEU 311 312 312 LEU LEU A . n A 1 312 THR 312 313 313 THR THR A . n A 1 313 VAL 313 314 314 VAL VAL A . n A 1 314 ASP 314 315 315 ASP ASP A . n A 1 315 ASP 315 316 316 ASP ASP A . n A 1 316 ILE 316 317 317 ILE ILE A . n A 1 317 GLU 317 318 318 GLU GLU A . n A 1 318 VAL 318 319 319 VAL VAL A . n A 1 319 SER 319 320 320 SER SER A . n A 1 320 CYS 320 321 321 CYS CYS A . n A 1 321 PRO 321 322 322 PRO PRO A . n A 1 322 SER 322 323 323 SER SER A . n A 1 323 GLU 323 324 324 GLU GLU A . n A 1 324 PRO 324 325 325 PRO PRO A . n A 1 325 PHE 325 326 326 PHE PHE A . n A 1 326 PRO 326 327 327 PRO PRO A . n A 1 327 GLU 327 328 328 GLU GLU A . n A 1 328 ILE 328 329 329 ILE ILE A . n A 1 329 ALA 329 330 330 ALA ALA A . n A 1 330 THR 330 331 331 THR THR A . n A 1 331 ALA 331 332 332 ALA ALA A . n A 1 332 SER 332 333 333 SER SER A . n A 1 333 GLY 333 334 334 GLY GLY A . n A 1 334 PRO 334 335 335 PRO PRO A . n A 1 335 LEU 335 336 336 LEU LEU A . n A 1 336 PRO 336 337 337 PRO PRO A . n A 1 337 SER 337 338 338 SER SER A . n A 1 338 LEU 338 339 339 LEU LEU A . n A 1 339 ALA 339 340 340 ALA ALA A . n A 1 340 PRO 340 341 341 PRO PRO A . n A 1 341 ALA 341 342 342 ALA ALA A . n A 1 342 PRO 342 343 343 PRO PRO A . n B 1 1 GLY 1 2 ? ? ? B . n B 1 2 PRO 2 3 ? ? ? B . n B 1 3 GLY 3 4 ? ? ? B . n B 1 4 GLY 4 5 ? ? ? B . n B 1 5 GLY 5 6 ? ? ? B . n B 1 6 GLY 6 7 ? ? ? B . n B 1 7 SER 7 8 8 SER SER B . n B 1 8 VAL 8 9 9 VAL VAL B . n B 1 9 THR 9 10 10 THR THR B . n B 1 10 CYS 10 11 11 CYS CYS B . n B 1 11 PRO 11 12 12 PRO PRO B . n B 1 12 GLY 12 13 13 GLY GLY B . n B 1 13 GLY 13 14 14 GLY GLY B . n B 1 14 GLN 14 15 15 GLN GLN B . n B 1 15 SER 15 16 16 SER SER B . n B 1 16 THR 16 17 17 THR THR B . n B 1 17 SER 17 18 18 SER SER B . n B 1 18 ASN 18 19 19 ASN ASN B . n B 1 19 SER 19 20 20 SER SER B . n B 1 20 GLN 20 21 21 GLN GLN B . n B 1 21 CYS 21 22 22 CYS CYS B . n B 1 22 CYS 22 23 23 CYS CYS B . n B 1 23 VAL 23 24 24 VAL VAL B . n B 1 24 TRP 24 25 25 TRP TRP B . n B 1 25 PHE 25 26 26 PHE PHE B . n B 1 26 ASP 26 27 27 ASP ASP B . n B 1 27 VAL 27 28 28 VAL VAL B . n B 1 28 LEU 28 29 29 LEU LEU B . n B 1 29 ASP 29 30 30 ASP ASP B . n B 1 30 ASP 30 31 31 ASP ASP B . n B 1 31 LEU 31 32 32 LEU LEU B . n B 1 32 GLN 32 33 33 GLN GLN B . n B 1 33 THR 33 34 34 THR THR B . n B 1 34 ASN 34 35 35 ASN ASN B . n B 1 35 PHE 35 36 36 PHE PHE B . n B 1 36 TYR 36 37 37 TYR TYR B . n B 1 37 GLN 37 38 38 GLN GLN B . n B 1 38 GLY 38 39 39 GLY GLY B . n B 1 39 SER 39 40 40 SER SER B . n B 1 40 LYS 40 41 41 LYS LYS B . n B 1 41 CYS 41 42 42 CYS CYS B . n B 1 42 GLU 42 43 43 GLU GLU B . n B 1 43 SER 43 44 44 SER SER B . n B 1 44 PRO 44 45 45 PRO PRO B . n B 1 45 VAL 45 46 46 VAL VAL B . n B 1 46 ARG 46 47 47 ARG ARG B . n B 1 47 LYS 47 48 48 LYS LYS B . n B 1 48 ILE 48 49 49 ILE ILE B . n B 1 49 LEU 49 50 50 LEU LEU B . n B 1 50 ARG 50 51 51 ARG ARG B . n B 1 51 ILE 51 52 52 ILE ILE B . n B 1 52 VAL 52 53 53 VAL VAL B . n B 1 53 PHE 53 54 54 PHE PHE B . n B 1 54 HIS 54 55 55 HIS HIS B . n B 1 55 ASP 55 56 56 ASP ASP B . n B 1 56 ALA 56 57 57 ALA ALA B . n B 1 57 ILE 57 58 58 ILE ILE B . n B 1 58 GLY 58 59 59 GLY GLY B . n B 1 59 PHE 59 60 60 PHE PHE B . n B 1 60 SER 60 61 61 SER SER B . n B 1 61 PRO 61 62 62 PRO PRO B . n B 1 62 ALA 62 63 63 ALA ALA B . n B 1 63 LEU 63 64 64 LEU LEU B . n B 1 64 THR 64 65 65 THR THR B . n B 1 65 ALA 65 66 66 ALA ALA B . n B 1 66 ALA 66 67 67 ALA ALA B . n B 1 67 GLY 67 68 68 GLY GLY B . n B 1 68 GLN 68 69 69 GLN GLN B . n B 1 69 PHE 69 70 70 PHE PHE B . n B 1 70 GLY 70 71 71 GLY GLY B . n B 1 71 GLY 71 72 72 GLY GLY B . n B 1 72 GLY 72 73 73 GLY GLY B . n B 1 73 GLY 73 74 74 GLY GLY B . n B 1 74 ALA 74 75 75 ALA ALA B . n B 1 75 ASP 75 76 76 ASP ASP B . n B 1 76 GLY 76 77 77 GLY GLY B . n B 1 77 SER 77 78 78 SER SER B . n B 1 78 ILE 78 79 79 ILE ILE B . n B 1 79 ILE 79 80 80 ILE ILE B . n B 1 80 ALA 80 81 81 ALA ALA B . n B 1 81 HIS 81 82 82 HIS HIS B . n B 1 82 SER 82 83 83 SER SER B . n B 1 83 ASN 83 84 84 ASN ASN B . n B 1 84 ILE 84 85 85 ILE ILE B . n B 1 85 GLU 85 86 86 GLU GLU B . n B 1 86 LEU 86 87 87 LEU LEU B . n B 1 87 ALA 87 88 88 ALA ALA B . n B 1 88 PHE 88 89 89 PHE PHE B . n B 1 89 PRO 89 90 90 PRO PRO B . n B 1 90 ALA 90 91 91 ALA ALA B . n B 1 91 ASN 91 92 92 ASN ASN B . n B 1 92 GLY 92 93 93 GLY GLY B . n B 1 93 GLY 93 94 94 GLY GLY B . n B 1 94 LEU 94 95 95 LEU LEU B . n B 1 95 THR 95 96 96 THR THR B . n B 1 96 ASP 96 97 97 ASP ASP B . n B 1 97 THR 97 98 98 THR THR B . n B 1 98 VAL 98 99 99 VAL VAL B . n B 1 99 GLU 99 100 100 GLU GLU B . n B 1 100 ALA 100 101 101 ALA ALA B . n B 1 101 LEU 101 102 102 LEU LEU B . n B 1 102 ARG 102 103 103 ARG ARG B . n B 1 103 ALA 103 104 104 ALA ALA B . n B 1 104 VAL 104 105 105 VAL VAL B . n B 1 105 GLY 105 106 106 GLY GLY B . n B 1 106 ILE 106 107 107 ILE ILE B . n B 1 107 ASN 107 108 108 ASN ASN B . n B 1 108 HIS 108 109 109 HIS HIS B . n B 1 109 GLY 109 110 110 GLY GLY B . n B 1 110 VAL 110 111 111 VAL VAL B . n B 1 111 SER 111 112 112 SER SER B . n B 1 112 PHE 112 113 113 PHE PHE B . n B 1 113 GLY 113 114 114 GLY GLY B . n B 1 114 ASP 114 115 115 ASP ASP B . n B 1 115 LEU 115 116 116 LEU LEU B . n B 1 116 ILE 116 117 117 ILE ILE B . n B 1 117 GLN 117 118 118 GLN GLN B . n B 1 118 PHE 118 119 119 PHE PHE B . n B 1 119 ALA 119 120 120 ALA ALA B . n B 1 120 THR 120 121 121 THR THR B . n B 1 121 ALA 121 122 122 ALA ALA B . n B 1 122 VAL 122 123 123 VAL VAL B . n B 1 123 GLY 123 124 124 GLY GLY B . n B 1 124 MET 124 125 125 MET MET B . n B 1 125 SER 125 126 126 SER SER B . n B 1 126 ASN 126 127 127 ASN ASN B . n B 1 127 CYS 127 128 128 CYS CYS B . n B 1 128 PRO 128 129 129 PRO PRO B . n B 1 129 GLY 129 130 130 GLY GLY B . n B 1 130 SER 130 131 131 SER SER B . n B 1 131 PRO 131 132 132 PRO PRO B . n B 1 132 ARG 132 133 133 ARG ARG B . n B 1 133 LEU 133 134 134 LEU LEU B . n B 1 134 GLU 134 135 135 GLU GLU B . n B 1 135 PHE 135 136 136 PHE PHE B . n B 1 136 LEU 136 137 137 LEU LEU B . n B 1 137 THR 137 138 138 THR THR B . n B 1 138 GLY 138 139 139 GLY GLY B . n B 1 139 ARG 139 140 140 ARG ARG B . n B 1 140 SER 140 141 141 SER SER B . n B 1 141 ASN 141 142 142 ASN ASN B . n B 1 142 SER 142 143 143 SER SER B . n B 1 143 SER 143 144 144 SER SER B . n B 1 144 GLN 144 145 145 GLN GLN B . n B 1 145 PRO 145 146 146 PRO PRO B . n B 1 146 SER 146 147 147 SER SER B . n B 1 147 PRO 147 148 148 PRO PRO B . n B 1 148 PRO 148 149 149 PRO PRO B . n B 1 149 SER 149 150 150 SER SER B . n B 1 150 LEU 150 151 151 LEU LEU B . n B 1 151 ILE 151 152 152 ILE ILE B . n B 1 152 PRO 152 153 153 PRO PRO B . n B 1 153 GLY 153 154 154 GLY GLY B . n B 1 154 PRO 154 155 155 PRO PRO B . n B 1 155 GLY 155 156 156 GLY GLY B . n B 1 156 ASN 156 157 157 ASN ASN B . n B 1 157 THR 157 158 158 THR THR B . n B 1 158 VAL 158 159 159 VAL VAL B . n B 1 159 THR 159 160 160 THR THR B . n B 1 160 ALA 160 161 161 ALA ALA B . n B 1 161 ILE 161 162 162 ILE ILE B . n B 1 162 LEU 162 163 163 LEU LEU B . n B 1 163 ASP 163 164 164 ASP ASP B . n B 1 164 ARG 164 165 165 ARG ARG B . n B 1 165 MET 165 166 166 MET MET B . n B 1 166 GLY 166 167 167 GLY GLY B . n B 1 167 ASP 167 168 168 ASP ASP B . n B 1 168 ALA 168 169 169 ALA ALA B . n B 1 169 GLY 169 170 170 GLY GLY B . n B 1 170 PHE 170 171 171 PHE PHE B . n B 1 171 SER 171 172 172 SER SER B . n B 1 172 PRO 172 173 173 PRO PRO B . n B 1 173 ASP 173 174 174 ASP ASP B . n B 1 174 GLU 174 175 175 GLU GLU B . n B 1 175 VAL 175 176 176 VAL VAL B . n B 1 176 VAL 176 177 177 VAL VAL B . n B 1 177 ASP 177 178 178 ASP ASP B . n B 1 178 LEU 178 179 179 LEU LEU B . n B 1 179 LEU 179 180 180 LEU LEU B . n B 1 180 ALA 180 181 181 ALA ALA B . n B 1 181 ALA 181 182 182 ALA ALA B . n B 1 182 HSO 182 183 183 HSO HSO B . n B 1 183 SER 183 184 184 SER SER B . n B 1 184 LEU 184 185 185 LEU LEU B . n B 1 185 ALA 185 186 186 ALA ALA B . n B 1 186 SER 186 187 187 SER SER B . n B 1 187 GLN 187 188 188 GLN GLN B . n B 1 188 GLU 188 189 189 GLU GLU B . n B 1 189 GLY 189 190 190 GLY GLY B . n B 1 190 LEU 190 191 191 LEU LEU B . n B 1 191 ASN 191 192 192 ASN ASN B . n B 1 192 SER 192 193 193 SER SER B . n B 1 193 ALA 193 194 194 ALA ALA B . n B 1 194 ILE 194 195 195 ILE ILE B . n B 1 195 PHE 195 196 196 PHE PHE B . n B 1 196 ARG 196 197 197 ARG ARG B . n B 1 197 SER 197 198 198 SER SER B . n B 1 198 PRO 198 199 199 PRO PRO B . n B 1 199 LEU 199 200 200 LEU LEU B . n B 1 200 ASP 200 201 201 ASP ASP B . n B 1 201 SER 201 202 202 SER SER B . n B 1 202 THR 202 203 203 THR THR B . n B 1 203 PRO 203 204 204 PRO PRO B . n B 1 204 GLN 204 205 205 GLN GLN B . n B 1 205 VAL 205 206 206 VAL VAL B . n B 1 206 PHE 206 207 207 PHE PHE B . n B 1 207 ASP 207 208 208 ASP ASP B . n B 1 208 THR 208 209 209 THR THR B . n B 1 209 GLN 209 210 210 GLN GLN B . n B 1 210 PHE 210 211 211 PHE PHE B . n B 1 211 TYR 211 212 212 TYR TYR B . n B 1 212 ILE 212 213 213 ILE ILE B . n B 1 213 GLU 213 214 214 GLU GLU B . n B 1 214 THR 214 215 215 THR THR B . n B 1 215 LEU 215 216 216 LEU LEU B . n B 1 216 LEU 216 217 217 LEU LEU B . n B 1 217 LYS 217 218 218 LYS LYS B . n B 1 218 GLY 218 219 219 GLY GLY B . n B 1 219 THR 219 220 220 THR THR B . n B 1 220 THR 220 221 221 THR THR B . n B 1 221 GLN 221 222 222 GLN GLN B . n B 1 222 PRO 222 223 223 PRO PRO B . n B 1 223 GLY 223 224 224 GLY GLY B . n B 1 224 PRO 224 225 225 PRO PRO B . n B 1 225 SER 225 226 226 SER SER B . n B 1 226 LEU 226 227 227 LEU LEU B . n B 1 227 GLY 227 228 228 GLY GLY B . n B 1 228 PHE 228 229 229 PHE PHE B . n B 1 229 ALA 229 230 230 ALA ALA B . n B 1 230 GLU 230 231 231 GLU GLU B . n B 1 231 GLU 231 232 232 GLU GLU B . n B 1 232 LEU 232 233 233 LEU LEU B . n B 1 233 SER 233 234 234 SER SER B . n B 1 234 PRO 234 235 235 PRO PRO B . n B 1 235 PHE 235 236 236 PHE PHE B . n B 1 236 PRO 236 237 237 PRO PRO B . n B 1 237 GLY 237 238 238 GLY GLY B . n B 1 238 GLU 238 239 239 GLU GLU B . n B 1 239 PHE 239 240 240 PHE PHE B . n B 1 240 ARG 240 241 241 ARG ARG B . n B 1 241 MET 241 242 242 MET MET B . n B 1 242 ARG 242 243 243 ARG ARG B . n B 1 243 SER 243 244 244 SER SER B . n B 1 244 ASP 244 245 245 ASP ASP B . n B 1 245 ALA 245 246 246 ALA ALA B . n B 1 246 LEU 246 247 247 LEU LEU B . n B 1 247 LEU 247 248 248 LEU LEU B . n B 1 248 ALA 248 249 249 ALA ALA B . n B 1 249 ARG 249 250 250 ARG ARG B . n B 1 250 ASP 250 251 251 ASP ASP B . n B 1 251 SER 251 252 252 SER SER B . n B 1 252 ARG 252 253 253 ARG ARG B . n B 1 253 THR 253 254 254 THR THR B . n B 1 254 ALA 254 255 255 ALA ALA B . n B 1 255 CYS 255 256 256 CYS CYS B . n B 1 256 ARG 256 257 257 ARG ARG B . n B 1 257 TRP 257 258 258 TRP TRP B . n B 1 258 GLN 258 259 259 GLN GLN B . n B 1 259 SER 259 260 260 SER SER B . n B 1 260 MET 260 261 261 MET MET B . n B 1 261 THR 261 262 262 THR THR B . n B 1 262 SER 262 263 263 SER SER B . n B 1 263 SER 263 264 264 SER SER B . n B 1 264 ASN 264 265 265 ASN ASN B . n B 1 265 GLU 265 266 266 GLU GLU B . n B 1 266 VAL 266 267 267 VAL VAL B . n B 1 267 MET 267 268 268 MET MET B . n B 1 268 GLY 268 269 269 GLY GLY B . n B 1 269 GLN 269 270 270 GLN GLN B . n B 1 270 ARG 270 271 271 ARG ARG B . n B 1 271 TYR 271 272 272 TYR TYR B . n B 1 272 ARG 272 273 273 ARG ARG B . n B 1 273 ALA 273 274 274 ALA ALA B . n B 1 274 ALA 274 275 275 ALA ALA B . n B 1 275 MET 275 276 276 MET MET B . n B 1 276 ALA 276 277 277 ALA ALA B . n B 1 277 LYS 277 278 278 LYS LYS B . n B 1 278 MET 278 279 279 MET MET B . n B 1 279 SER 279 280 280 SER SER B . n B 1 280 VAL 280 281 281 VAL VAL B . n B 1 281 LEU 281 282 282 LEU LEU B . n B 1 282 GLY 282 283 283 GLY GLY B . n B 1 283 PHE 283 284 284 PHE PHE B . n B 1 284 ASP 284 285 285 ASP ASP B . n B 1 285 ARG 285 286 286 ARG ARG B . n B 1 286 ASN 286 287 287 ASN ASN B . n B 1 287 ALA 287 288 288 ALA ALA B . n B 1 288 LEU 288 289 289 LEU LEU B . n B 1 289 THR 289 290 290 THR THR B . n B 1 290 ASP 290 291 291 ASP ASP B . n B 1 291 CYS 291 292 292 CYS CYS B . n B 1 292 SER 292 293 293 SER SER B . n B 1 293 ASP 293 294 294 ASP ASP B . n B 1 294 VAL 294 295 295 VAL VAL B . n B 1 295 ILE 295 296 296 ILE ILE B . n B 1 296 PRO 296 297 297 PRO PRO B . n B 1 297 SER 297 298 298 SER SER B . n B 1 298 ALA 298 299 299 ALA ALA B . n B 1 299 VAL 299 300 300 VAL VAL B . n B 1 300 SER 300 301 301 SER SER B . n B 1 301 ASN 301 302 302 ASN ASN B . n B 1 302 ASN 302 303 303 ASN ASN B . n B 1 303 ALA 303 304 304 ALA ALA B . n B 1 304 ALA 304 305 305 ALA ALA B . n B 1 305 PRO 305 306 306 PRO PRO B . n B 1 306 VAL 306 307 307 VAL VAL B . n B 1 307 ILE 307 308 308 ILE ILE B . n B 1 308 PRO 308 309 309 PRO PRO B . n B 1 309 GLY 309 310 310 GLY GLY B . n B 1 310 GLY 310 311 311 GLY GLY B . n B 1 311 LEU 311 312 312 LEU LEU B . n B 1 312 THR 312 313 313 THR THR B . n B 1 313 VAL 313 314 314 VAL VAL B . n B 1 314 ASP 314 315 315 ASP ASP B . n B 1 315 ASP 315 316 316 ASP ASP B . n B 1 316 ILE 316 317 317 ILE ILE B . n B 1 317 GLU 317 318 318 GLU GLU B . n B 1 318 VAL 318 319 319 VAL VAL B . n B 1 319 SER 319 320 320 SER SER B . n B 1 320 CYS 320 321 321 CYS CYS B . n B 1 321 PRO 321 322 322 PRO PRO B . n B 1 322 SER 322 323 323 SER SER B . n B 1 323 GLU 323 324 324 GLU GLU B . n B 1 324 PRO 324 325 325 PRO PRO B . n B 1 325 PHE 325 326 326 PHE PHE B . n B 1 326 PRO 326 327 327 PRO PRO B . n B 1 327 GLU 327 328 328 GLU GLU B . n B 1 328 ILE 328 329 329 ILE ILE B . n B 1 329 ALA 329 330 330 ALA ALA B . n B 1 330 THR 330 331 331 THR THR B . n B 1 331 ALA 331 332 332 ALA ALA B . n B 1 332 SER 332 333 333 SER SER B . n B 1 333 GLY 333 334 334 GLY GLY B . n B 1 334 PRO 334 335 335 PRO PRO B . n B 1 335 LEU 335 336 336 LEU LEU B . n B 1 336 PRO 336 337 337 PRO PRO B . n B 1 337 SER 337 338 338 SER SER B . n B 1 338 LEU 338 339 339 LEU LEU B . n B 1 339 ALA 339 340 340 ALA ALA B . n B 1 340 PRO 340 341 341 PRO PRO B . n B 1 341 ALA 341 342 342 ALA ALA B . n B 1 342 PRO 342 343 343 PRO PRO 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 HEM 1 401 1344 HEM HEM A . D 3 CA 1 402 1345 CA CA A . E 3 CA 1 403 1346 CA CA A . F 4 NAG 1 404 1347 NAG NAG A . G 4 NAG 2 405 1348 NAG NAG A . H 5 BMA 1 406 1349 BMA BMA A . I 6 MG 1 407 1351 MG MG A . J 2 HEM 1 401 1344 HEM HEM B . K 3 CA 1 402 1345 CA CA B . L 3 CA 1 403 1346 CA CA B . M 4 NAG 1 404 1347 NAG NAG B . N 4 NAG 2 405 1348 NAG NAG B . O 5 BMA 1 406 1349 BMA BMA B . P 7 HOH 1 501 2187 HOH HOH A . P 7 HOH 2 502 2188 HOH HOH A . P 7 HOH 3 503 2213 HOH HOH A . P 7 HOH 4 504 2141 HOH HOH A . P 7 HOH 5 505 2202 HOH HOH A . P 7 HOH 6 506 2048 HOH HOH A . P 7 HOH 7 507 2109 HOH HOH A . P 7 HOH 8 508 2225 HOH HOH A . P 7 HOH 9 509 2008 HOH HOH A . P 7 HOH 10 510 2215 HOH HOH A . P 7 HOH 11 511 2227 HOH HOH A . P 7 HOH 12 512 2167 HOH HOH A . P 7 HOH 13 513 2081 HOH HOH A . P 7 HOH 14 514 2117 HOH HOH A . P 7 HOH 15 515 2116 HOH HOH A . P 7 HOH 16 516 2217 HOH HOH A . P 7 HOH 17 517 2076 HOH HOH A . P 7 HOH 18 518 2236 HOH HOH A . P 7 HOH 19 519 2122 HOH HOH A . P 7 HOH 20 520 2231 HOH HOH A . P 7 HOH 21 521 2111 HOH HOH A . P 7 HOH 22 522 2174 HOH HOH A . P 7 HOH 23 523 2102 HOH HOH A . P 7 HOH 24 524 2105 HOH HOH A . P 7 HOH 25 525 2228 HOH HOH A . P 7 HOH 26 526 2029 HOH HOH A . P 7 HOH 27 527 2041 HOH HOH A . P 7 HOH 28 528 2180 HOH HOH A . P 7 HOH 29 529 2100 HOH HOH A . P 7 HOH 30 530 2139 HOH HOH A . P 7 HOH 31 531 2023 HOH HOH A . P 7 HOH 32 532 2090 HOH HOH A . P 7 HOH 33 533 2170 HOH HOH A . P 7 HOH 34 534 2079 HOH HOH A . P 7 HOH 35 535 2140 HOH HOH A . P 7 HOH 36 536 2125 HOH HOH A . P 7 HOH 37 537 2164 HOH HOH A . P 7 HOH 38 538 2216 HOH HOH A . P 7 HOH 39 539 2200 HOH HOH A . P 7 HOH 40 540 2047 HOH HOH A . P 7 HOH 41 541 2183 HOH HOH A . P 7 HOH 42 542 2020 HOH HOH A . P 7 HOH 43 543 2229 HOH HOH A . P 7 HOH 44 544 2169 HOH HOH A . P 7 HOH 45 545 2177 HOH HOH A . P 7 HOH 46 546 2199 HOH HOH A . P 7 HOH 47 547 2132 HOH HOH A . P 7 HOH 48 548 2195 HOH HOH A . P 7 HOH 49 549 2097 HOH HOH A . P 7 HOH 50 550 2055 HOH HOH A . P 7 HOH 51 551 2149 HOH HOH A . P 7 HOH 52 552 2220 HOH HOH A . P 7 HOH 53 553 2157 HOH HOH A . P 7 HOH 54 554 2156 HOH HOH A . P 7 HOH 55 555 2013 HOH HOH A . P 7 HOH 56 556 2058 HOH HOH A . P 7 HOH 57 557 2071 HOH HOH A . P 7 HOH 58 558 2004 HOH HOH A . P 7 HOH 59 559 2130 HOH HOH A . P 7 HOH 60 560 2178 HOH HOH A . P 7 HOH 61 561 2084 HOH HOH A . P 7 HOH 62 562 2063 HOH HOH A . P 7 HOH 63 563 2056 HOH HOH A . P 7 HOH 64 564 2209 HOH HOH A . P 7 HOH 65 565 2145 HOH HOH A . P 7 HOH 66 566 2160 HOH HOH A . P 7 HOH 67 567 2060 HOH HOH A . P 7 HOH 68 568 2026 HOH HOH A . P 7 HOH 69 569 2154 HOH HOH A . P 7 HOH 70 570 2194 HOH HOH A . P 7 HOH 71 571 2166 HOH HOH A . P 7 HOH 72 572 2230 HOH HOH A . P 7 HOH 73 573 2082 HOH HOH A . P 7 HOH 74 574 2088 HOH HOH A . P 7 HOH 75 575 2222 HOH HOH A . P 7 HOH 76 576 2146 HOH HOH A . P 7 HOH 77 577 2201 HOH HOH A . P 7 HOH 78 578 2057 HOH HOH A . P 7 HOH 79 579 2110 HOH HOH A . P 7 HOH 80 580 2106 HOH HOH A . P 7 HOH 81 581 2171 HOH HOH A . P 7 HOH 82 582 2038 HOH HOH A . P 7 HOH 83 583 2184 HOH HOH A . P 7 HOH 84 584 2006 HOH HOH A . P 7 HOH 85 585 2150 HOH HOH A . P 7 HOH 86 586 2162 HOH HOH A . P 7 HOH 87 587 2181 HOH HOH A . P 7 HOH 88 588 2069 HOH HOH A . P 7 HOH 89 589 2172 HOH HOH A . P 7 HOH 90 590 2168 HOH HOH A . P 7 HOH 91 591 2134 HOH HOH A . P 7 HOH 92 592 2049 HOH HOH A . P 7 HOH 93 593 2035 HOH HOH A . P 7 HOH 94 594 2070 HOH HOH A . P 7 HOH 95 595 2136 HOH HOH A . P 7 HOH 96 596 2089 HOH HOH A . P 7 HOH 97 597 2011 HOH HOH A . P 7 HOH 98 598 2211 HOH HOH A . P 7 HOH 99 599 2153 HOH HOH A . P 7 HOH 100 600 2119 HOH HOH A . P 7 HOH 101 601 2163 HOH HOH A . P 7 HOH 102 602 2039 HOH HOH A . P 7 HOH 103 603 2175 HOH HOH A . P 7 HOH 104 604 2085 HOH HOH A . P 7 HOH 105 605 2094 HOH HOH A . P 7 HOH 106 606 2007 HOH HOH A . P 7 HOH 107 607 2185 HOH HOH A . P 7 HOH 108 608 2165 HOH HOH A . P 7 HOH 109 609 2147 HOH HOH A . P 7 HOH 110 610 2221 HOH HOH A . P 7 HOH 111 611 2098 HOH HOH A . P 7 HOH 112 612 2019 HOH HOH A . P 7 HOH 113 613 2027 HOH HOH A . P 7 HOH 114 614 2210 HOH HOH A . P 7 HOH 115 615 2074 HOH HOH A . P 7 HOH 116 616 2059 HOH HOH A . P 7 HOH 117 617 2186 HOH HOH A . P 7 HOH 118 618 2104 HOH HOH A . P 7 HOH 119 619 2115 HOH HOH A . P 7 HOH 120 620 2108 HOH HOH A . P 7 HOH 121 621 2073 HOH HOH A . P 7 HOH 122 622 2022 HOH HOH A . P 7 HOH 123 623 2051 HOH HOH A . P 7 HOH 124 624 2235 HOH HOH A . P 7 HOH 125 625 2131 HOH HOH A . P 7 HOH 126 626 2203 HOH HOH A . P 7 HOH 127 627 2043 HOH HOH A . P 7 HOH 128 628 2142 HOH HOH A . P 7 HOH 129 629 2232 HOH HOH A . P 7 HOH 130 630 2118 HOH HOH A . P 7 HOH 131 631 2144 HOH HOH A . P 7 HOH 132 632 2176 HOH HOH A . P 7 HOH 133 633 2114 HOH HOH A . P 7 HOH 134 634 2197 HOH HOH A . P 7 HOH 135 635 2126 HOH HOH A . P 7 HOH 136 636 2124 HOH HOH A . P 7 HOH 137 637 2112 HOH HOH A . P 7 HOH 138 638 2198 HOH HOH A . P 7 HOH 139 639 2151 HOH HOH A . P 7 HOH 140 640 2191 HOH HOH A . P 7 HOH 141 641 2208 HOH HOH A . P 7 HOH 142 642 2113 HOH HOH A . P 7 HOH 143 643 2021 HOH HOH A . P 7 HOH 144 644 2155 HOH HOH A . P 7 HOH 145 645 2083 HOH HOH A . P 7 HOH 146 646 2028 HOH HOH A . P 7 HOH 147 647 2137 HOH HOH A . P 7 HOH 148 648 2092 HOH HOH A . P 7 HOH 149 649 2233 HOH HOH A . P 7 HOH 150 650 2093 HOH HOH A . P 7 HOH 151 651 2123 HOH HOH A . P 7 HOH 152 652 2095 HOH HOH A . P 7 HOH 153 653 2214 HOH HOH A . P 7 HOH 154 654 2189 HOH HOH A . P 7 HOH 155 655 2190 HOH HOH A . P 7 HOH 156 656 2206 HOH HOH A . P 7 HOH 157 657 2224 HOH HOH A . P 7 HOH 158 658 2030 HOH HOH A . P 7 HOH 159 659 2204 HOH HOH A . P 7 HOH 160 660 2193 HOH HOH A . P 7 HOH 161 661 2120 HOH HOH A . P 7 HOH 162 662 2101 HOH HOH A . P 7 HOH 163 663 2234 HOH HOH A . P 7 HOH 164 664 2096 HOH HOH A . P 7 HOH 165 665 2040 HOH HOH A . P 7 HOH 166 666 2054 HOH HOH A . P 7 HOH 167 667 2107 HOH HOH A . P 7 HOH 168 668 2219 HOH HOH A . P 7 HOH 169 669 2173 HOH HOH A . P 7 HOH 170 670 2133 HOH HOH A . P 7 HOH 171 671 2223 HOH HOH A . P 7 HOH 172 672 2205 HOH HOH A . P 7 HOH 173 673 2099 HOH HOH A . P 7 HOH 174 674 2128 HOH HOH A . P 7 HOH 175 675 2031 HOH HOH A . P 7 HOH 176 676 2179 HOH HOH A . P 7 HOH 177 677 2121 HOH HOH A . P 7 HOH 178 678 2067 HOH HOH A . P 7 HOH 179 679 2192 HOH HOH A . P 7 HOH 180 680 2127 HOH HOH A . P 7 HOH 181 681 2129 HOH HOH A . P 7 HOH 182 682 2152 HOH HOH A . P 7 HOH 183 683 2182 HOH HOH A . P 7 HOH 184 684 2003 HOH HOH A . P 7 HOH 185 685 2138 HOH HOH A . P 7 HOH 186 686 2080 HOH HOH A . P 7 HOH 187 687 2212 HOH HOH A . P 7 HOH 188 688 2161 HOH HOH A . P 7 HOH 189 689 2143 HOH HOH A . P 7 HOH 190 690 2061 HOH HOH A . P 7 HOH 191 691 2103 HOH HOH A . P 7 HOH 192 692 2148 HOH HOH A . P 7 HOH 193 693 2010 HOH HOH A . P 7 HOH 194 694 2068 HOH HOH A . P 7 HOH 195 695 2062 HOH HOH A . P 7 HOH 196 696 2159 HOH HOH A . P 7 HOH 197 697 2196 HOH HOH A . P 7 HOH 198 698 2018 HOH HOH A . P 7 HOH 199 699 2091 HOH HOH A . P 7 HOH 200 700 2226 HOH HOH A . P 7 HOH 201 701 2075 HOH HOH A . P 7 HOH 202 702 2158 HOH HOH A . P 7 HOH 203 703 2207 HOH HOH A . P 7 HOH 204 704 2218 HOH HOH A . P 7 HOH 205 705 2002 HOH HOH A . P 7 HOH 206 706 2135 HOH HOH A . P 7 HOH 207 707 2009 HOH HOH A . P 7 HOH 208 708 2005 HOH HOH A . P 7 HOH 209 709 2042 HOH HOH A . P 7 HOH 210 710 2017 HOH HOH A . P 7 HOH 211 711 2033 HOH HOH A . P 7 HOH 212 712 2024 HOH HOH A . P 7 HOH 213 713 2001 HOH HOH A . P 7 HOH 214 714 2065 HOH HOH A . P 7 HOH 215 715 2064 HOH HOH A . P 7 HOH 216 716 2137 HOH HOH A . P 7 HOH 217 717 2045 HOH HOH A . P 7 HOH 218 718 2016 HOH HOH A . P 7 HOH 219 719 2086 HOH HOH A . P 7 HOH 220 720 2052 HOH HOH A . P 7 HOH 221 721 2025 HOH HOH A . P 7 HOH 222 722 2019 HOH HOH A . P 7 HOH 223 723 2050 HOH HOH A . P 7 HOH 224 724 2078 HOH HOH A . P 7 HOH 225 725 2034 HOH HOH A . P 7 HOH 226 726 2066 HOH HOH A . P 7 HOH 227 727 2039 HOH HOH A . P 7 HOH 228 728 2012 HOH HOH A . P 7 HOH 229 729 2015 HOH HOH A . P 7 HOH 230 730 2032 HOH HOH A . P 7 HOH 231 731 2077 HOH HOH A . P 7 HOH 232 732 2053 HOH HOH A . P 7 HOH 233 733 2072 HOH HOH A . P 7 HOH 234 734 2087 HOH HOH A . P 7 HOH 235 735 2037 HOH HOH A . P 7 HOH 236 736 2046 HOH HOH A . Q 7 HOH 1 501 2053 HOH HOH B . Q 7 HOH 2 502 2048 HOH HOH B . Q 7 HOH 3 503 2223 HOH HOH B . Q 7 HOH 4 504 2062 HOH HOH B . Q 7 HOH 5 505 2191 HOH HOH B . Q 7 HOH 6 506 2163 HOH HOH B . Q 7 HOH 7 507 2022 HOH HOH B . Q 7 HOH 8 508 2209 HOH HOH B . Q 7 HOH 9 509 2256 HOH HOH B . Q 7 HOH 10 510 2188 HOH HOH B . Q 7 HOH 11 511 2101 HOH HOH B . Q 7 HOH 12 512 2142 HOH HOH B . Q 7 HOH 13 513 2115 HOH HOH B . Q 7 HOH 14 514 2208 HOH HOH B . Q 7 HOH 15 515 2150 HOH HOH B . Q 7 HOH 16 516 2046 HOH HOH B . Q 7 HOH 17 517 2072 HOH HOH B . Q 7 HOH 18 518 2108 HOH HOH B . Q 7 HOH 19 519 2232 HOH HOH B . Q 7 HOH 20 520 2184 HOH HOH B . Q 7 HOH 21 521 2226 HOH HOH B . Q 7 HOH 22 522 2172 HOH HOH B . Q 7 HOH 23 523 2262 HOH HOH B . Q 7 HOH 24 524 2119 HOH HOH B . Q 7 HOH 25 525 2158 HOH HOH B . Q 7 HOH 26 526 2258 HOH HOH B . Q 7 HOH 27 527 2155 HOH HOH B . Q 7 HOH 28 528 2248 HOH HOH B . Q 7 HOH 29 529 2076 HOH HOH B . Q 7 HOH 30 530 2195 HOH HOH B . Q 7 HOH 31 531 2168 HOH HOH B . Q 7 HOH 32 532 2082 HOH HOH B . Q 7 HOH 33 533 2159 HOH HOH B . Q 7 HOH 34 534 2071 HOH HOH B . Q 7 HOH 35 535 2224 HOH HOH B . Q 7 HOH 36 536 2245 HOH HOH B . Q 7 HOH 37 537 2114 HOH HOH B . Q 7 HOH 38 538 2234 HOH HOH B . Q 7 HOH 39 539 2173 HOH HOH B . Q 7 HOH 40 540 2239 HOH HOH B . Q 7 HOH 41 541 2139 HOH HOH B . Q 7 HOH 42 542 2227 HOH HOH B . Q 7 HOH 43 543 2026 HOH HOH B . Q 7 HOH 44 544 2008 HOH HOH B . Q 7 HOH 45 545 2087 HOH HOH B . Q 7 HOH 46 546 2123 HOH HOH B . Q 7 HOH 47 547 2065 HOH HOH B . Q 7 HOH 48 548 2207 HOH HOH B . Q 7 HOH 49 549 2178 HOH HOH B . Q 7 HOH 50 550 2069 HOH HOH B . Q 7 HOH 51 551 2112 HOH HOH B . Q 7 HOH 52 552 2156 HOH HOH B . Q 7 HOH 53 553 2141 HOH HOH B . Q 7 HOH 54 554 2038 HOH HOH B . Q 7 HOH 55 555 2216 HOH HOH B . Q 7 HOH 56 556 2086 HOH HOH B . Q 7 HOH 57 557 2241 HOH HOH B . Q 7 HOH 58 558 2210 HOH HOH B . Q 7 HOH 59 559 2183 HOH HOH B . Q 7 HOH 60 560 2206 HOH HOH B . Q 7 HOH 61 561 2254 HOH HOH B . Q 7 HOH 62 562 2100 HOH HOH B . Q 7 HOH 63 563 2230 HOH HOH B . Q 7 HOH 64 564 2253 HOH HOH B . Q 7 HOH 65 565 2085 HOH HOH B . Q 7 HOH 66 566 2215 HOH HOH B . Q 7 HOH 67 567 2004 HOH HOH B . Q 7 HOH 68 568 2001 HOH HOH B . Q 7 HOH 69 569 2181 HOH HOH B . Q 7 HOH 70 570 2132 HOH HOH B . Q 7 HOH 71 571 2113 HOH HOH B . Q 7 HOH 72 572 2250 HOH HOH B . Q 7 HOH 73 573 2057 HOH HOH B . Q 7 HOH 74 574 2236 HOH HOH B . Q 7 HOH 75 575 2179 HOH HOH B . Q 7 HOH 76 576 2093 HOH HOH B . Q 7 HOH 77 577 2166 HOH HOH B . Q 7 HOH 78 578 2134 HOH HOH B . Q 7 HOH 79 579 2095 HOH HOH B . Q 7 HOH 80 580 2147 HOH HOH B . Q 7 HOH 81 581 2012 HOH HOH B . Q 7 HOH 82 582 2237 HOH HOH B . Q 7 HOH 83 583 2219 HOH HOH B . Q 7 HOH 84 584 2111 HOH HOH B . Q 7 HOH 85 585 2170 HOH HOH B . Q 7 HOH 86 586 2075 HOH HOH B . Q 7 HOH 87 587 2056 HOH HOH B . Q 7 HOH 88 588 2193 HOH HOH B . Q 7 HOH 89 589 2252 HOH HOH B . Q 7 HOH 90 590 2078 HOH HOH B . Q 7 HOH 91 591 2036 HOH HOH B . Q 7 HOH 92 592 2261 HOH HOH B . Q 7 HOH 93 593 2130 HOH HOH B . Q 7 HOH 94 594 2243 HOH HOH B . Q 7 HOH 95 595 2238 HOH HOH B . Q 7 HOH 96 596 2169 HOH HOH B . Q 7 HOH 97 597 2067 HOH HOH B . Q 7 HOH 98 598 2040 HOH HOH B . Q 7 HOH 99 599 2124 HOH HOH B . Q 7 HOH 100 600 2140 HOH HOH B . Q 7 HOH 101 601 2143 HOH HOH B . Q 7 HOH 102 602 2009 HOH HOH B . Q 7 HOH 103 603 2118 HOH HOH B . Q 7 HOH 104 604 2059 HOH HOH B . Q 7 HOH 105 605 2045 HOH HOH B . Q 7 HOH 106 606 2177 HOH HOH B . Q 7 HOH 107 607 2033 HOH HOH B . Q 7 HOH 108 608 2006 HOH HOH B . Q 7 HOH 109 609 2205 HOH HOH B . Q 7 HOH 110 610 2220 HOH HOH B . Q 7 HOH 111 611 2117 HOH HOH B . Q 7 HOH 112 612 2244 HOH HOH B . Q 7 HOH 113 613 2204 HOH HOH B . Q 7 HOH 114 614 2068 HOH HOH B . Q 7 HOH 115 615 2055 HOH HOH B . Q 7 HOH 116 616 2044 HOH HOH B . Q 7 HOH 117 617 2171 HOH HOH B . Q 7 HOH 118 618 2259 HOH HOH B . Q 7 HOH 119 619 2089 HOH HOH B . Q 7 HOH 120 620 2151 HOH HOH B . Q 7 HOH 121 621 2240 HOH HOH B . Q 7 HOH 122 622 2104 HOH HOH B . Q 7 HOH 123 623 2174 HOH HOH B . Q 7 HOH 124 624 2175 HOH HOH B . Q 7 HOH 125 625 2116 HOH HOH B . Q 7 HOH 126 626 2167 HOH HOH B . Q 7 HOH 127 627 2149 HOH HOH B . Q 7 HOH 128 628 2105 HOH HOH B . Q 7 HOH 129 629 2257 HOH HOH B . Q 7 HOH 130 630 2097 HOH HOH B . Q 7 HOH 131 631 2049 HOH HOH B . Q 7 HOH 132 632 2218 HOH HOH B . Q 7 HOH 133 633 2242 HOH HOH B . Q 7 HOH 134 634 2127 HOH HOH B . Q 7 HOH 135 635 2058 HOH HOH B . Q 7 HOH 136 636 2023 HOH HOH B . Q 7 HOH 137 637 2034 HOH HOH B . Q 7 HOH 138 638 2030 HOH HOH B . Q 7 HOH 139 639 2214 HOH HOH B . Q 7 HOH 140 640 2096 HOH HOH B . Q 7 HOH 141 641 2120 HOH HOH B . Q 7 HOH 142 642 2233 HOH HOH B . Q 7 HOH 143 643 2148 HOH HOH B . Q 7 HOH 144 644 2229 HOH HOH B . Q 7 HOH 145 645 2032 HOH HOH B . Q 7 HOH 146 646 2211 HOH HOH B . Q 7 HOH 147 647 2107 HOH HOH B . Q 7 HOH 148 648 2122 HOH HOH B . Q 7 HOH 149 649 2180 HOH HOH B . Q 7 HOH 150 650 2003 HOH HOH B . Q 7 HOH 151 651 2052 HOH HOH B . Q 7 HOH 152 652 2043 HOH HOH B . Q 7 HOH 153 653 2102 HOH HOH B . Q 7 HOH 154 654 2231 HOH HOH B . Q 7 HOH 155 655 2099 HOH HOH B . Q 7 HOH 156 656 2084 HOH HOH B . Q 7 HOH 157 657 2133 HOH HOH B . Q 7 HOH 158 658 2128 HOH HOH B . Q 7 HOH 159 659 2198 HOH HOH B . Q 7 HOH 160 660 2251 HOH HOH B . Q 7 HOH 161 661 2255 HOH HOH B . Q 7 HOH 162 662 2103 HOH HOH B . Q 7 HOH 163 663 2164 HOH HOH B . Q 7 HOH 164 664 2126 HOH HOH B . Q 7 HOH 165 665 2189 HOH HOH B . Q 7 HOH 166 666 2200 HOH HOH B . Q 7 HOH 167 667 2013 HOH HOH B . Q 7 HOH 168 668 2246 HOH HOH B . Q 7 HOH 169 669 2225 HOH HOH B . Q 7 HOH 170 670 2110 HOH HOH B . Q 7 HOH 171 671 2029 HOH HOH B . Q 7 HOH 172 672 2185 HOH HOH B . Q 7 HOH 173 673 2106 HOH HOH B . Q 7 HOH 174 674 2146 HOH HOH B . Q 7 HOH 175 675 2247 HOH HOH B . Q 7 HOH 176 676 2005 HOH HOH B . Q 7 HOH 177 677 2066 HOH HOH B . Q 7 HOH 178 678 2144 HOH HOH B . Q 7 HOH 179 679 2091 HOH HOH B . Q 7 HOH 180 680 2121 HOH HOH B . Q 7 HOH 181 681 2197 HOH HOH B . Q 7 HOH 182 682 2221 HOH HOH B . Q 7 HOH 183 683 2125 HOH HOH B . Q 7 HOH 184 684 2186 HOH HOH B . Q 7 HOH 185 685 2196 HOH HOH B . Q 7 HOH 186 686 2015 HOH HOH B . Q 7 HOH 187 687 2165 HOH HOH B . Q 7 HOH 188 688 2217 HOH HOH B . Q 7 HOH 189 689 2235 HOH HOH B . Q 7 HOH 190 690 2129 HOH HOH B . Q 7 HOH 191 691 2031 HOH HOH B . Q 7 HOH 192 692 2182 HOH HOH B . Q 7 HOH 193 693 2199 HOH HOH B . Q 7 HOH 194 694 2109 HOH HOH B . Q 7 HOH 195 695 2154 HOH HOH B . Q 7 HOH 196 696 2203 HOH HOH B . Q 7 HOH 197 697 2092 HOH HOH B . Q 7 HOH 198 698 2153 HOH HOH B . Q 7 HOH 199 699 2152 HOH HOH B . Q 7 HOH 200 700 2145 HOH HOH B . Q 7 HOH 201 701 2194 HOH HOH B . Q 7 HOH 202 702 2138 HOH HOH B . Q 7 HOH 203 703 2162 HOH HOH B . Q 7 HOH 204 704 2060 HOH HOH B . Q 7 HOH 205 705 2161 HOH HOH B . Q 7 HOH 206 706 2213 HOH HOH B . Q 7 HOH 207 707 2157 HOH HOH B . Q 7 HOH 208 708 2249 HOH HOH B . Q 7 HOH 209 709 2212 HOH HOH B . Q 7 HOH 210 710 2187 HOH HOH B . Q 7 HOH 211 711 2260 HOH HOH B . Q 7 HOH 212 712 2222 HOH HOH B . Q 7 HOH 213 713 2021 HOH HOH B . Q 7 HOH 214 714 2098 HOH HOH B . Q 7 HOH 215 715 2190 HOH HOH B . Q 7 HOH 216 716 2192 HOH HOH B . Q 7 HOH 217 717 2027 HOH HOH B . Q 7 HOH 218 718 2136 HOH HOH B . Q 7 HOH 219 719 2228 HOH HOH B . Q 7 HOH 220 720 2176 HOH HOH B . Q 7 HOH 221 721 2018 HOH HOH B . Q 7 HOH 222 722 2051 HOH HOH B . Q 7 HOH 223 723 2131 HOH HOH B . Q 7 HOH 224 724 2061 HOH HOH B . Q 7 HOH 225 725 2028 HOH HOH B . Q 7 HOH 226 726 2010 HOH HOH B . Q 7 HOH 227 727 2020 HOH HOH B . Q 7 HOH 228 728 2011 HOH HOH B . Q 7 HOH 229 729 2201 HOH HOH B . Q 7 HOH 230 730 2202 HOH HOH B . Q 7 HOH 231 731 2035 HOH HOH B . Q 7 HOH 232 732 2080 HOH HOH B . Q 7 HOH 233 733 2083 HOH HOH B . Q 7 HOH 234 734 2135 HOH HOH B . Q 7 HOH 235 735 2064 HOH HOH B . Q 7 HOH 236 736 2024 HOH HOH B . Q 7 HOH 237 737 2050 HOH HOH B . Q 7 HOH 238 738 2063 HOH HOH B . Q 7 HOH 239 739 2041 HOH HOH B . Q 7 HOH 240 740 2090 HOH HOH B . Q 7 HOH 241 741 2014 HOH HOH B . Q 7 HOH 242 742 2002 HOH HOH B . Q 7 HOH 243 743 2042 HOH HOH B . Q 7 HOH 244 744 2047 HOH HOH B . Q 7 HOH 245 745 2054 HOH HOH B . Q 7 HOH 246 746 2079 HOH HOH B . Q 7 HOH 247 747 2014 HOH HOH B . Q 7 HOH 248 748 2016 HOH HOH B . Q 7 HOH 249 749 2025 HOH HOH B . Q 7 HOH 250 750 2036 HOH HOH B . Q 7 HOH 251 751 2081 HOH HOH B . Q 7 HOH 252 752 2077 HOH HOH B . Q 7 HOH 253 753 2037 HOH HOH B . Q 7 HOH 254 754 2094 HOH HOH B . Q 7 HOH 255 755 2017 HOH HOH B . Q 7 HOH 256 756 2160 HOH HOH B . Q 7 HOH 257 757 2088 HOH HOH B . Q 7 HOH 258 758 2070 HOH HOH B . Q 7 HOH 259 759 2074 HOH HOH B . Q 7 HOH 260 760 2044 HOH HOH B . Q 7 HOH 261 761 2073 HOH HOH B . Q 7 HOH 262 762 2007 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 141 A ASN 142 ? ASN 'GLYCOSYLATION SITE' 2 A SER 337 A SER 338 ? SER 'GLYCOSYLATION SITE' 3 B ASN 141 B ASN 142 ? ASN 'GLYCOSYLATION SITE' 4 B SER 337 B SER 338 ? SER 'GLYCOSYLATION SITE' 5 A HSO 182 A HSO 183 ? HIS L-HISTIDINOL 6 B HSO 182 B HSO 183 ? HIS L-HISTIDINOL # 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_and_software_defined_assembly PISA monomeric 1 2 author_and_software_defined_assembly PISA 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,P 2 1 B,J,K,L,M,N,O,Q # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 O ? A ASP 55 ? A ASP 56 ? 1_555 CA ? D CA . ? A CA 402 ? 1_555 OD1 ? A ASP 55 ? A ASP 56 ? 1_555 81.7 ? 2 O ? A ASP 55 ? A ASP 56 ? 1_555 CA ? D CA . ? A CA 402 ? 1_555 O ? A GLY 73 ? A GLY 74 ? 1_555 69.1 ? 3 OD1 ? A ASP 55 ? A ASP 56 ? 1_555 CA ? D CA . ? A CA 402 ? 1_555 O ? A GLY 73 ? A GLY 74 ? 1_555 92.8 ? 4 O ? A ASP 55 ? A ASP 56 ? 1_555 CA ? D CA . ? A CA 402 ? 1_555 OD2 ? A ASP 75 ? A ASP 76 ? 1_555 136.3 ? 5 OD1 ? A ASP 55 ? A ASP 56 ? 1_555 CA ? D CA . ? A CA 402 ? 1_555 OD2 ? A ASP 75 ? A ASP 76 ? 1_555 82.6 ? 6 O ? A GLY 73 ? A GLY 74 ? 1_555 CA ? D CA . ? A CA 402 ? 1_555 OD2 ? A ASP 75 ? A ASP 76 ? 1_555 71.2 ? 7 O ? A ASP 55 ? A ASP 56 ? 1_555 CA ? D CA . ? A CA 402 ? 1_555 OG ? A SER 77 ? A SER 78 ? 1_555 149.5 ? 8 OD1 ? A ASP 55 ? A ASP 56 ? 1_555 CA ? D CA . ? A CA 402 ? 1_555 OG ? A SER 77 ? A SER 78 ? 1_555 91.0 ? 9 O ? A GLY 73 ? A GLY 74 ? 1_555 CA ? D CA . ? A CA 402 ? 1_555 OG ? A SER 77 ? A SER 78 ? 1_555 141.2 ? 10 OD2 ? A ASP 75 ? A ASP 76 ? 1_555 CA ? D CA . ? A CA 402 ? 1_555 OG ? A SER 77 ? A SER 78 ? 1_555 71.0 ? 11 O ? A ASP 55 ? A ASP 56 ? 1_555 CA ? D CA . ? A CA 402 ? 1_555 O ? P HOH . ? A HOH 563 ? 1_555 72.3 ? 12 OD1 ? A ASP 55 ? A ASP 56 ? 1_555 CA ? D CA . ? A CA 402 ? 1_555 O ? P HOH . ? A HOH 563 ? 1_555 88.8 ? 13 O ? A GLY 73 ? A GLY 74 ? 1_555 CA ? D CA . ? A CA 402 ? 1_555 O ? P HOH . ? A HOH 563 ? 1_555 140.7 ? 14 OD2 ? A ASP 75 ? A ASP 76 ? 1_555 CA ? D CA . ? A CA 402 ? 1_555 O ? P HOH . ? A HOH 563 ? 1_555 147.6 ? 15 OG ? A SER 77 ? A SER 78 ? 1_555 CA ? D CA . ? A CA 402 ? 1_555 O ? P HOH . ? A HOH 563 ? 1_555 78.0 ? 16 O ? A ASP 55 ? A ASP 56 ? 1_555 CA ? D CA . ? A CA 402 ? 1_555 O ? P HOH . ? A HOH 593 ? 1_555 98.5 ? 17 OD1 ? A ASP 55 ? A ASP 56 ? 1_555 CA ? D CA . ? A CA 402 ? 1_555 O ? P HOH . ? A HOH 593 ? 1_555 176.4 ? 18 O ? A GLY 73 ? A GLY 74 ? 1_555 CA ? D CA . ? A CA 402 ? 1_555 O ? P HOH . ? A HOH 593 ? 1_555 90.6 ? 19 OD2 ? A ASP 75 ? A ASP 76 ? 1_555 CA ? D CA . ? A CA 402 ? 1_555 O ? P HOH . ? A HOH 593 ? 1_555 99.6 ? 20 OG ? A SER 77 ? A SER 78 ? 1_555 CA ? D CA . ? A CA 402 ? 1_555 O ? P HOH . ? A HOH 593 ? 1_555 87.0 ? 21 O ? P HOH . ? A HOH 563 ? 1_555 CA ? D CA . ? A CA 402 ? 1_555 O ? P HOH . ? A HOH 593 ? 1_555 87.9 ? 22 NE2 ? A HSO 182 ? A HSO 183 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 NA ? C HEM . ? A HEM 401 ? 1_555 97.4 ? 23 NE2 ? A HSO 182 ? A HSO 183 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 NB ? C HEM . ? A HEM 401 ? 1_555 90.4 ? 24 NA ? C HEM . ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 NB ? C HEM . ? A HEM 401 ? 1_555 96.2 ? 25 NE2 ? A HSO 182 ? A HSO 183 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 NC ? C HEM . ? A HEM 401 ? 1_555 89.9 ? 26 NA ? C HEM . ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 NC ? C HEM . ? A HEM 401 ? 1_555 172.6 ? 27 NB ? C HEM . ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 NC ? C HEM . ? A HEM 401 ? 1_555 84.7 ? 28 NE2 ? A HSO 182 ? A HSO 183 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 ND ? C HEM . ? A HEM 401 ? 1_555 92.8 ? 29 NA ? C HEM . ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 ND ? C HEM . ? A HEM 401 ? 1_555 85.8 ? 30 NB ? C HEM . ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 ND ? C HEM . ? A HEM 401 ? 1_555 176.0 ? 31 NC ? C HEM . ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 ND ? C HEM . ? A HEM 401 ? 1_555 92.8 ? 32 NE2 ? A HSO 182 ? A HSO 183 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 O ? P HOH . ? A HOH 629 ? 1_555 170.0 ? 33 NA ? C HEM . ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 O ? P HOH . ? A HOH 629 ? 1_555 85.8 ? 34 NB ? C HEM . ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 O ? P HOH . ? A HOH 629 ? 1_555 79.8 ? 35 NC ? C HEM . ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 O ? P HOH . ? A HOH 629 ? 1_555 87.1 ? 36 ND ? C HEM . ? A HEM 401 ? 1_555 FE ? C HEM . ? A HEM 401 ? 1_555 O ? P HOH . ? A HOH 629 ? 1_555 96.9 ? 37 O ? A SER 183 ? A SER 184 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 OG ? A SER 183 ? A SER 184 ? 1_555 70.4 ? 38 O ? A SER 183 ? A SER 184 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 OD1 ? A ASP 200 ? A ASP 201 ? 1_555 78.6 ? 39 OG ? A SER 183 ? A SER 184 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 OD1 ? A ASP 200 ? A ASP 201 ? 1_555 113.8 ? 40 O ? A SER 183 ? A SER 184 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 OD2 ? A ASP 200 ? A ASP 201 ? 1_555 92.0 ? 41 OG ? A SER 183 ? A SER 184 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 OD2 ? A ASP 200 ? A ASP 201 ? 1_555 76.3 ? 42 OD1 ? A ASP 200 ? A ASP 201 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 OD2 ? A ASP 200 ? A ASP 201 ? 1_555 47.5 ? 43 O ? A SER 183 ? A SER 184 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 O ? A THR 202 ? A THR 203 ? 1_555 84.6 ? 44 OG ? A SER 183 ? A SER 184 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 O ? A THR 202 ? A THR 203 ? 1_555 151.4 ? 45 OD1 ? A ASP 200 ? A ASP 201 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 O ? A THR 202 ? A THR 203 ? 1_555 72.8 ? 46 OD2 ? A ASP 200 ? A ASP 201 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 O ? A THR 202 ? A THR 203 ? 1_555 119.4 ? 47 O ? A SER 183 ? A SER 184 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 OG1 ? A THR 202 ? A THR 203 ? 1_555 150.7 ? 48 OG ? A SER 183 ? A SER 184 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 OG1 ? A THR 202 ? A THR 203 ? 1_555 138.0 ? 49 OD1 ? A ASP 200 ? A ASP 201 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 OG1 ? A THR 202 ? A THR 203 ? 1_555 81.0 ? 50 OD2 ? A ASP 200 ? A ASP 201 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 OG1 ? A THR 202 ? A THR 203 ? 1_555 89.5 ? 51 O ? A THR 202 ? A THR 203 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 OG1 ? A THR 202 ? A THR 203 ? 1_555 69.3 ? 52 O ? A SER 183 ? A SER 184 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 O ? A VAL 205 ? A VAL 206 ? 1_555 92.1 ? 53 OG ? A SER 183 ? A SER 184 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 O ? A VAL 205 ? A VAL 206 ? 1_555 79.0 ? 54 OD1 ? A ASP 200 ? A ASP 201 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 O ? A VAL 205 ? A VAL 206 ? 1_555 159.8 ? 55 OD2 ? A ASP 200 ? A ASP 201 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 O ? A VAL 205 ? A VAL 206 ? 1_555 152.0 ? 56 O ? A THR 202 ? A THR 203 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 O ? A VAL 205 ? A VAL 206 ? 1_555 88.6 ? 57 OG1 ? A THR 202 ? A THR 203 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 O ? A VAL 205 ? A VAL 206 ? 1_555 100.1 ? 58 O ? A SER 183 ? A SER 184 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 OD1 ? A ASP 207 ? A ASP 208 ? 1_555 140.4 ? 59 OG ? A SER 183 ? A SER 184 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 OD1 ? A ASP 207 ? A ASP 208 ? 1_555 70.2 ? 60 OD1 ? A ASP 200 ? A ASP 201 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 OD1 ? A ASP 207 ? A ASP 208 ? 1_555 121.8 ? 61 OD2 ? A ASP 200 ? A ASP 201 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 OD1 ? A ASP 207 ? A ASP 208 ? 1_555 82.7 ? 62 O ? A THR 202 ? A THR 203 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 OD1 ? A ASP 207 ? A ASP 208 ? 1_555 131.9 ? 63 OG1 ? A THR 202 ? A THR 203 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 OD1 ? A ASP 207 ? A ASP 208 ? 1_555 68.8 ? 64 O ? A VAL 205 ? A VAL 206 ? 1_555 CA ? E CA . ? A CA 403 ? 1_555 OD1 ? A ASP 207 ? A ASP 208 ? 1_555 76.5 ? 65 O ? B ASP 55 ? B ASP 56 ? 1_555 CA ? K CA . ? B CA 402 ? 1_555 OD2 ? B ASP 55 ? B ASP 56 ? 1_555 86.6 ? 66 O ? B ASP 55 ? B ASP 56 ? 1_555 CA ? K CA . ? B CA 402 ? 1_555 O ? B GLY 73 ? B GLY 74 ? 1_555 68.8 ? 67 OD2 ? B ASP 55 ? B ASP 56 ? 1_555 CA ? K CA . ? B CA 402 ? 1_555 O ? B GLY 73 ? B GLY 74 ? 1_555 96.5 ? 68 O ? B ASP 55 ? B ASP 56 ? 1_555 CA ? K CA . ? B CA 402 ? 1_555 OD2 ? B ASP 75 ? B ASP 76 ? 1_555 138.4 ? 69 OD2 ? B ASP 55 ? B ASP 56 ? 1_555 CA ? K CA . ? B CA 402 ? 1_555 OD2 ? B ASP 75 ? B ASP 76 ? 1_555 79.8 ? 70 O ? B GLY 73 ? B GLY 74 ? 1_555 CA ? K CA . ? B CA 402 ? 1_555 OD2 ? B ASP 75 ? B ASP 76 ? 1_555 74.0 ? 71 O ? B ASP 55 ? B ASP 56 ? 1_555 CA ? K CA . ? B CA 402 ? 1_555 OG ? B SER 77 ? B SER 78 ? 1_555 150.5 ? 72 OD2 ? B ASP 55 ? B ASP 56 ? 1_555 CA ? K CA . ? B CA 402 ? 1_555 OG ? B SER 77 ? B SER 78 ? 1_555 86.1 ? 73 O ? B GLY 73 ? B GLY 74 ? 1_555 CA ? K CA . ? B CA 402 ? 1_555 OG ? B SER 77 ? B SER 78 ? 1_555 140.5 ? 74 OD2 ? B ASP 75 ? B ASP 76 ? 1_555 CA ? K CA . ? B CA 402 ? 1_555 OG ? B SER 77 ? B SER 78 ? 1_555 67.7 ? 75 O ? B ASP 55 ? B ASP 56 ? 1_555 CA ? K CA . ? B CA 402 ? 1_555 O ? Q HOH . ? B HOH 554 ? 1_555 99.7 ? 76 OD2 ? B ASP 55 ? B ASP 56 ? 1_555 CA ? K CA . ? B CA 402 ? 1_555 O ? Q HOH . ? B HOH 554 ? 1_555 170.4 ? 77 O ? B GLY 73 ? B GLY 74 ? 1_555 CA ? K CA . ? B CA 402 ? 1_555 O ? Q HOH . ? B HOH 554 ? 1_555 92.6 ? 78 OD2 ? B ASP 75 ? B ASP 76 ? 1_555 CA ? K CA . ? B CA 402 ? 1_555 O ? Q HOH . ? B HOH 554 ? 1_555 99.8 ? 79 OG ? B SER 77 ? B SER 78 ? 1_555 CA ? K CA . ? B CA 402 ? 1_555 O ? Q HOH . ? B HOH 554 ? 1_555 84.9 ? 80 O ? B ASP 55 ? B ASP 56 ? 1_555 CA ? K CA . ? B CA 402 ? 1_555 O ? Q HOH . ? B HOH 587 ? 1_555 76.0 ? 81 OD2 ? B ASP 55 ? B ASP 56 ? 1_555 CA ? K CA . ? B CA 402 ? 1_555 O ? Q HOH . ? B HOH 587 ? 1_555 86.8 ? 82 O ? B GLY 73 ? B GLY 74 ? 1_555 CA ? K CA . ? B CA 402 ? 1_555 O ? Q HOH . ? B HOH 587 ? 1_555 144.3 ? 83 OD2 ? B ASP 75 ? B ASP 76 ? 1_555 CA ? K CA . ? B CA 402 ? 1_555 O ? Q HOH . ? B HOH 587 ? 1_555 141.1 ? 84 OG ? B SER 77 ? B SER 78 ? 1_555 CA ? K CA . ? B CA 402 ? 1_555 O ? Q HOH . ? B HOH 587 ? 1_555 75.1 ? 85 O ? Q HOH . ? B HOH 554 ? 1_555 CA ? K CA . ? B CA 402 ? 1_555 O ? Q HOH . ? B HOH 587 ? 1_555 87.6 ? 86 NE2 ? B HSO 182 ? B HSO 183 ? 1_555 FE ? J HEM . ? B HEM 401 ? 1_555 NA ? J HEM . ? B HEM 401 ? 1_555 100.4 ? 87 NE2 ? B HSO 182 ? B HSO 183 ? 1_555 FE ? J HEM . ? B HEM 401 ? 1_555 NB ? J HEM . ? B HEM 401 ? 1_555 93.5 ? 88 NA ? J HEM . ? B HEM 401 ? 1_555 FE ? J HEM . ? B HEM 401 ? 1_555 NB ? J HEM . ? B HEM 401 ? 1_555 96.6 ? 89 NE2 ? B HSO 182 ? B HSO 183 ? 1_555 FE ? J HEM . ? B HEM 401 ? 1_555 NC ? J HEM . ? B HEM 401 ? 1_555 87.0 ? 90 NA ? J HEM . ? B HEM 401 ? 1_555 FE ? J HEM . ? B HEM 401 ? 1_555 NC ? J HEM . ? B HEM 401 ? 1_555 172.1 ? 91 NB ? J HEM . ? B HEM 401 ? 1_555 FE ? J HEM . ? B HEM 401 ? 1_555 NC ? J HEM . ? B HEM 401 ? 1_555 85.6 ? 92 NE2 ? B HSO 182 ? B HSO 183 ? 1_555 FE ? J HEM . ? B HEM 401 ? 1_555 ND ? J HEM . ? B HEM 401 ? 1_555 85.6 ? 93 NA ? J HEM . ? B HEM 401 ? 1_555 FE ? J HEM . ? B HEM 401 ? 1_555 ND ? J HEM . ? B HEM 401 ? 1_555 85.3 ? 94 NB ? J HEM . ? B HEM 401 ? 1_555 FE ? J HEM . ? B HEM 401 ? 1_555 ND ? J HEM . ? B HEM 401 ? 1_555 178.0 ? 95 NC ? J HEM . ? B HEM 401 ? 1_555 FE ? J HEM . ? B HEM 401 ? 1_555 ND ? J HEM . ? B HEM 401 ? 1_555 92.6 ? 96 NE2 ? B HSO 182 ? B HSO 183 ? 1_555 FE ? J HEM . ? B HEM 401 ? 1_555 O ? Q HOH . ? B HOH 629 ? 1_555 176.6 ? 97 NA ? J HEM . ? B HEM 401 ? 1_555 FE ? J HEM . ? B HEM 401 ? 1_555 O ? Q HOH . ? B HOH 629 ? 1_555 82.4 ? 98 NB ? J HEM . ? B HEM 401 ? 1_555 FE ? J HEM . ? B HEM 401 ? 1_555 O ? Q HOH . ? B HOH 629 ? 1_555 84.2 ? 99 NC ? J HEM . ? B HEM 401 ? 1_555 FE ? J HEM . ? B HEM 401 ? 1_555 O ? Q HOH . ? B HOH 629 ? 1_555 90.3 ? 100 ND ? J HEM . ? B HEM 401 ? 1_555 FE ? J HEM . ? B HEM 401 ? 1_555 O ? Q HOH . ? B HOH 629 ? 1_555 96.6 ? 101 O ? B SER 183 ? B SER 184 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 OG ? B SER 183 ? B SER 184 ? 1_555 71.3 ? 102 O ? B SER 183 ? B SER 184 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 OD1 ? B ASP 200 ? B ASP 201 ? 1_555 83.3 ? 103 OG ? B SER 183 ? B SER 184 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 OD1 ? B ASP 200 ? B ASP 201 ? 1_555 116.4 ? 104 O ? B SER 183 ? B SER 184 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 OD2 ? B ASP 200 ? B ASP 201 ? 1_555 97.2 ? 105 OG ? B SER 183 ? B SER 184 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 OD2 ? B ASP 200 ? B ASP 201 ? 1_555 77.8 ? 106 OD1 ? B ASP 200 ? B ASP 201 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 OD2 ? B ASP 200 ? B ASP 201 ? 1_555 48.3 ? 107 O ? B SER 183 ? B SER 184 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 O ? B THR 202 ? B THR 203 ? 1_555 82.8 ? 108 OG ? B SER 183 ? B SER 184 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 O ? B THR 202 ? B THR 203 ? 1_555 148.9 ? 109 OD1 ? B ASP 200 ? B ASP 201 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 O ? B THR 202 ? B THR 203 ? 1_555 75.9 ? 110 OD2 ? B ASP 200 ? B ASP 201 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 O ? B THR 202 ? B THR 203 ? 1_555 123.5 ? 111 O ? B SER 183 ? B SER 184 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 OG1 ? B THR 202 ? B THR 203 ? 1_555 151.3 ? 112 OG ? B SER 183 ? B SER 184 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 OG1 ? B THR 202 ? B THR 203 ? 1_555 137.2 ? 113 OD1 ? B ASP 200 ? B ASP 201 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 OG1 ? B THR 202 ? B THR 203 ? 1_555 79.6 ? 114 OD2 ? B ASP 200 ? B ASP 201 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 OG1 ? B THR 202 ? B THR 203 ? 1_555 88.5 ? 115 O ? B THR 202 ? B THR 203 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 OG1 ? B THR 202 ? B THR 203 ? 1_555 70.8 ? 116 O ? B SER 183 ? B SER 184 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 O ? B VAL 205 ? B VAL 206 ? 1_555 86.1 ? 117 OG ? B SER 183 ? B SER 184 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 O ? B VAL 205 ? B VAL 206 ? 1_555 82.2 ? 118 OD1 ? B ASP 200 ? B ASP 201 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 O ? B VAL 205 ? B VAL 206 ? 1_555 153.9 ? 119 OD2 ? B ASP 200 ? B ASP 201 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 O ? B VAL 205 ? B VAL 206 ? 1_555 157.3 ? 120 O ? B THR 202 ? B THR 203 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 O ? B VAL 205 ? B VAL 206 ? 1_555 79.1 ? 121 OG1 ? B THR 202 ? B THR 203 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 O ? B VAL 205 ? B VAL 206 ? 1_555 99.3 ? 122 O ? B SER 183 ? B SER 184 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 OD1 ? B ASP 207 ? B ASP 208 ? 1_555 140.4 ? 123 OG ? B SER 183 ? B SER 184 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 OD1 ? B ASP 207 ? B ASP 208 ? 1_555 70.3 ? 124 OD1 ? B ASP 200 ? B ASP 201 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 OD1 ? B ASP 207 ? B ASP 208 ? 1_555 122.8 ? 125 OD2 ? B ASP 200 ? B ASP 201 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 OD1 ? B ASP 207 ? B ASP 208 ? 1_555 83.9 ? 126 O ? B THR 202 ? B THR 203 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 OD1 ? B ASP 207 ? B ASP 208 ? 1_555 129.1 ? 127 OG1 ? B THR 202 ? B THR 203 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 OD1 ? B ASP 207 ? B ASP 208 ? 1_555 68.0 ? 128 O ? B VAL 205 ? B VAL 206 ? 1_555 CA ? L CA . ? B CA 403 ? 1_555 OD1 ? B ASP 207 ? B ASP 208 ? 1_555 79.4 ? 129 O ? P HOH . ? A HOH 552 ? 1_555 MG ? I MG . ? A MG 407 ? 1_555 O ? P HOH . ? A HOH 610 ? 1_555 91.8 ? 130 O ? P HOH . ? A HOH 552 ? 1_555 MG ? I MG . ? A MG 407 ? 1_555 O ? Q HOH . ? B HOH 540 ? 2_555 87.4 ? 131 O ? P HOH . ? A HOH 610 ? 1_555 MG ? I MG . ? A MG 407 ? 1_555 O ? Q HOH . ? B HOH 540 ? 2_555 178.0 ? 132 O ? P HOH . ? A HOH 552 ? 1_555 MG ? I MG . ? A MG 407 ? 1_555 O ? Q HOH . ? B HOH 595 ? 2_555 87.8 ? 133 O ? P HOH . ? A HOH 610 ? 1_555 MG ? I MG . ? A MG 407 ? 1_555 O ? Q HOH . ? B HOH 595 ? 2_555 88.8 ? 134 O ? Q HOH . ? B HOH 540 ? 2_555 MG ? I MG . ? A MG 407 ? 1_555 O ? Q HOH . ? B HOH 595 ? 2_555 89.3 ? 135 O ? P HOH . ? A HOH 552 ? 1_555 MG ? I MG . ? A MG 407 ? 1_555 O ? Q HOH . ? B HOH 689 ? 2_555 178.1 ? 136 O ? P HOH . ? A HOH 610 ? 1_555 MG ? I MG . ? A MG 407 ? 1_555 O ? Q HOH . ? B HOH 689 ? 2_555 86.4 ? 137 O ? Q HOH . ? B HOH 540 ? 2_555 MG ? I MG . ? A MG 407 ? 1_555 O ? Q HOH . ? B HOH 689 ? 2_555 94.4 ? 138 O ? Q HOH . ? B HOH 595 ? 2_555 MG ? I MG . ? A MG 407 ? 1_555 O ? Q HOH . ? B HOH 689 ? 2_555 92.6 ? # 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 2003-06-12 2 'Structure model' 1 1 2011-10-19 # _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' 'Derived calculations' 2 2 'Structure model' 'Non-polymer description' 3 2 'Structure model' Other 4 2 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal X-PLOR refinement . ? 1 DENZO 'data reduction' . ? 2 SCALA 'data scaling' . ? 3 # _pdbx_entry_details.entry_id 1H3J _pdbx_entry_details.compound_details ;ACTIVITY INVOLVES DONOR + H(2)O(2) = OXIDIZED DONOR + 2 H(2)O. USALLY OCCURS BOUND TO PROTOHEME IX, IRON(III) ION AND 2 CALCIUM IONS PER SUBUNIT. N-LINKED GLYCOSYLATION SITE AT ASN142 O-LINKED GLYCOSYLATION SITE AT SER338 ; _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 PRO A 12 ? ? -48.70 -17.73 2 1 ASN A 35 ? ? -104.59 -64.13 3 1 CYS A 42 ? ? -114.23 71.75 4 1 GLU A 43 ? ? -123.41 -154.99 5 1 ASN A 192 ? ? -154.07 88.05 6 1 ASN B 35 ? ? -104.69 -63.99 7 1 CYS B 42 ? ? -113.76 65.24 8 1 GLU B 43 ? ? -116.98 -155.62 9 1 ASN B 192 ? ? -151.70 89.16 10 1 ILE B 195 ? ? -118.61 58.35 # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 A SER 333 ? CB ? A SER 332 CB 2 1 Y 1 A SER 333 ? OG ? A SER 332 OG 3 1 Y 1 B SER 333 ? CB ? B SER 332 CB 4 1 Y 1 B SER 333 ? OG ? B SER 332 OG # 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 GLY 2 ? A GLY 1 2 1 Y 1 A PRO 3 ? A PRO 2 3 1 Y 1 A GLY 4 ? A GLY 3 4 1 Y 1 A GLY 5 ? A GLY 4 5 1 Y 1 A GLY 6 ? A GLY 5 6 1 Y 1 A GLY 7 ? A GLY 6 7 1 Y 1 B GLY 2 ? B GLY 1 8 1 Y 1 B PRO 3 ? B PRO 2 9 1 Y 1 B GLY 4 ? B GLY 3 10 1 Y 1 B GLY 5 ? B GLY 4 11 1 Y 1 B GLY 6 ? B GLY 5 12 1 Y 1 B GLY 7 ? B GLY 6 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 'PROTOPORPHYRIN IX CONTAINING FE' HEM 3 'CALCIUM ION' CA 4 N-ACETYL-D-GLUCOSAMINE NAG 5 BETA-D-MANNOSE BMA 6 'MAGNESIUM ION' MG 7 water HOH #