data_2GAA # _entry.id 2GAA # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.281 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 2GAA RCSB RCSB036885 WWPDB D_1000036885 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 1UJ2 . unspecified PDB 2GA8 . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 2GAA _pdbx_database_status.recvd_initial_deposition_date 2006-03-08 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Chaptal, V.' 1 'Morera, S.' 2 # _citation.id primary _citation.title ;Crystal structure and functional analysis identify the P-loop containing protein YFH7 of Saccharomyces cerevisiae as an ATP-dependent kinase. ; _citation.journal_abbrev Proteins _citation.journal_volume 71 _citation.page_first 804 _citation.page_last 812 _citation.year 2007 _citation.journal_id_ASTM PSFGEY _citation.country US _citation.journal_id_ISSN 0887-3585 _citation.journal_id_CSD 0867 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 18004758 _citation.pdbx_database_id_DOI 10.1002/prot.21740 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Gueguen-Chaignon, V.' 1 primary 'Chaptal, V.' 2 primary 'Lariviere, L.' 3 primary 'Costa, N.' 4 primary 'Lopes, P.' 5 primary 'Morera, S.' 6 primary 'Nessler, S.' 7 # _cell.entry_id 2GAA _cell.length_a 134.756 _cell.length_b 134.756 _cell.length_c 48.679 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 9 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 2GAA _symmetry.space_group_name_H-M 'H 3' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 146 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man 'Hypothetical 39.9 kDa protein' 40996.633 1 ? ? ? ? 2 non-polymer syn 'SULFATE ION' 96.063 1 ? ? ? ? 3 water nat water 18.015 180 ? ? ? ? # _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 ;MVDTHKLADDVLQLLDNRIEDNYRVCVILVGSPGSGKSTIAEEL(CME)QIINEKYHTFLSEHPNVIEVNDRLKPMVNLV DSLKTLQPNKVAEMIENQGLFKDHVEDVNFQPVKYSALTSNNEE(CME)TAVVARGGTANAIRIAAVDNPVNVNKLAQDS INIAQIVPMDGFHLSRRCLDLFKDPQTAHKRRGSPSTFDSNNFLQLCKILAKTSL(CME)KVSSHHKFYSTSSVFEKLSK TFSQTIPDIFVPGFNHALKDPTPDQYCISKFTRIVILEGLYLLYDQENWKKIYKTLADTGALLVYKIDIDYEATEERVAK RHLQSGLVTTIAEGREKFRSNDLLNGRDIDNHLIKVDNIVHIRNDHHHHHH ; _entity_poly.pdbx_seq_one_letter_code_can ;MVDTHKLADDVLQLLDNRIEDNYRVCVILVGSPGSGKSTIAEELCQIINEKYHTFLSEHPNVIEVNDRLKPMVNLVDSLK TLQPNKVAEMIENQGLFKDHVEDVNFQPVKYSALTSNNEECTAVVARGGTANAIRIAAVDNPVNVNKLAQDSINIAQIVP MDGFHLSRRCLDLFKDPQTAHKRRGSPSTFDSNNFLQLCKILAKTSLCKVSSHHKFYSTSSVFEKLSKTFSQTIPDIFVP GFNHALKDPTPDQYCISKFTRIVILEGLYLLYDQENWKKIYKTLADTGALLVYKIDIDYEATEERVAKRHLQSGLVTTIA EGREKFRSNDLLNGRDIDNHLIKVDNIVHIRNDHHHHHH ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 MET n 1 2 VAL n 1 3 ASP n 1 4 THR n 1 5 HIS n 1 6 LYS n 1 7 LEU n 1 8 ALA n 1 9 ASP n 1 10 ASP n 1 11 VAL n 1 12 LEU n 1 13 GLN n 1 14 LEU n 1 15 LEU n 1 16 ASP n 1 17 ASN n 1 18 ARG n 1 19 ILE n 1 20 GLU n 1 21 ASP n 1 22 ASN n 1 23 TYR n 1 24 ARG n 1 25 VAL n 1 26 CYS n 1 27 VAL n 1 28 ILE n 1 29 LEU n 1 30 VAL n 1 31 GLY n 1 32 SER n 1 33 PRO n 1 34 GLY n 1 35 SER n 1 36 GLY n 1 37 LYS n 1 38 SER n 1 39 THR n 1 40 ILE n 1 41 ALA n 1 42 GLU n 1 43 GLU n 1 44 LEU n 1 45 CME n 1 46 GLN n 1 47 ILE n 1 48 ILE n 1 49 ASN n 1 50 GLU n 1 51 LYS n 1 52 TYR n 1 53 HIS n 1 54 THR n 1 55 PHE n 1 56 LEU n 1 57 SER n 1 58 GLU n 1 59 HIS n 1 60 PRO n 1 61 ASN n 1 62 VAL n 1 63 ILE n 1 64 GLU n 1 65 VAL n 1 66 ASN n 1 67 ASP n 1 68 ARG n 1 69 LEU n 1 70 LYS n 1 71 PRO n 1 72 MET n 1 73 VAL n 1 74 ASN n 1 75 LEU n 1 76 VAL n 1 77 ASP n 1 78 SER n 1 79 LEU n 1 80 LYS n 1 81 THR n 1 82 LEU n 1 83 GLN n 1 84 PRO n 1 85 ASN n 1 86 LYS n 1 87 VAL n 1 88 ALA n 1 89 GLU n 1 90 MET n 1 91 ILE n 1 92 GLU n 1 93 ASN n 1 94 GLN n 1 95 GLY n 1 96 LEU n 1 97 PHE n 1 98 LYS n 1 99 ASP n 1 100 HIS n 1 101 VAL n 1 102 GLU n 1 103 ASP n 1 104 VAL n 1 105 ASN n 1 106 PHE n 1 107 GLN n 1 108 PRO n 1 109 VAL n 1 110 LYS n 1 111 TYR n 1 112 SER n 1 113 ALA n 1 114 LEU n 1 115 THR n 1 116 SER n 1 117 ASN n 1 118 ASN n 1 119 GLU n 1 120 GLU n 1 121 CME n 1 122 THR n 1 123 ALA n 1 124 VAL n 1 125 VAL n 1 126 ALA n 1 127 ARG n 1 128 GLY n 1 129 GLY n 1 130 THR n 1 131 ALA n 1 132 ASN n 1 133 ALA n 1 134 ILE n 1 135 ARG n 1 136 ILE n 1 137 ALA n 1 138 ALA n 1 139 VAL n 1 140 ASP n 1 141 ASN n 1 142 PRO n 1 143 VAL n 1 144 ASN n 1 145 VAL n 1 146 ASN n 1 147 LYS n 1 148 LEU n 1 149 ALA n 1 150 GLN n 1 151 ASP n 1 152 SER n 1 153 ILE n 1 154 ASN n 1 155 ILE n 1 156 ALA n 1 157 GLN n 1 158 ILE n 1 159 VAL n 1 160 PRO n 1 161 MET n 1 162 ASP n 1 163 GLY n 1 164 PHE n 1 165 HIS n 1 166 LEU n 1 167 SER n 1 168 ARG n 1 169 ARG n 1 170 CYS n 1 171 LEU n 1 172 ASP n 1 173 LEU n 1 174 PHE n 1 175 LYS n 1 176 ASP n 1 177 PRO n 1 178 GLN n 1 179 THR n 1 180 ALA n 1 181 HIS n 1 182 LYS n 1 183 ARG n 1 184 ARG n 1 185 GLY n 1 186 SER n 1 187 PRO n 1 188 SER n 1 189 THR n 1 190 PHE n 1 191 ASP n 1 192 SER n 1 193 ASN n 1 194 ASN n 1 195 PHE n 1 196 LEU n 1 197 GLN n 1 198 LEU n 1 199 CYS n 1 200 LYS n 1 201 ILE n 1 202 LEU n 1 203 ALA n 1 204 LYS n 1 205 THR n 1 206 SER n 1 207 LEU n 1 208 CME n 1 209 LYS n 1 210 VAL n 1 211 SER n 1 212 SER n 1 213 HIS n 1 214 HIS n 1 215 LYS n 1 216 PHE n 1 217 TYR n 1 218 SER n 1 219 THR n 1 220 SER n 1 221 SER n 1 222 VAL n 1 223 PHE n 1 224 GLU n 1 225 LYS n 1 226 LEU n 1 227 SER n 1 228 LYS n 1 229 THR n 1 230 PHE n 1 231 SER n 1 232 GLN n 1 233 THR n 1 234 ILE n 1 235 PRO n 1 236 ASP n 1 237 ILE n 1 238 PHE n 1 239 VAL n 1 240 PRO n 1 241 GLY n 1 242 PHE n 1 243 ASN n 1 244 HIS n 1 245 ALA n 1 246 LEU n 1 247 LYS n 1 248 ASP n 1 249 PRO n 1 250 THR n 1 251 PRO n 1 252 ASP n 1 253 GLN n 1 254 TYR n 1 255 CYS n 1 256 ILE n 1 257 SER n 1 258 LYS n 1 259 PHE n 1 260 THR n 1 261 ARG n 1 262 ILE n 1 263 VAL n 1 264 ILE n 1 265 LEU n 1 266 GLU n 1 267 GLY n 1 268 LEU n 1 269 TYR n 1 270 LEU n 1 271 LEU n 1 272 TYR n 1 273 ASP n 1 274 GLN n 1 275 GLU n 1 276 ASN n 1 277 TRP n 1 278 LYS n 1 279 LYS n 1 280 ILE n 1 281 TYR n 1 282 LYS n 1 283 THR n 1 284 LEU n 1 285 ALA n 1 286 ASP n 1 287 THR n 1 288 GLY n 1 289 ALA n 1 290 LEU n 1 291 LEU n 1 292 VAL n 1 293 TYR n 1 294 LYS n 1 295 ILE n 1 296 ASP n 1 297 ILE n 1 298 ASP n 1 299 TYR n 1 300 GLU n 1 301 ALA n 1 302 THR n 1 303 GLU n 1 304 GLU n 1 305 ARG n 1 306 VAL n 1 307 ALA n 1 308 LYS n 1 309 ARG n 1 310 HIS n 1 311 LEU n 1 312 GLN n 1 313 SER n 1 314 GLY n 1 315 LEU n 1 316 VAL n 1 317 THR n 1 318 THR n 1 319 ILE n 1 320 ALA n 1 321 GLU n 1 322 GLY n 1 323 ARG n 1 324 GLU n 1 325 LYS n 1 326 PHE n 1 327 ARG n 1 328 SER n 1 329 ASN n 1 330 ASP n 1 331 LEU n 1 332 LEU n 1 333 ASN n 1 334 GLY n 1 335 ARG n 1 336 ASP n 1 337 ILE n 1 338 ASP n 1 339 ASN n 1 340 HIS n 1 341 LEU n 1 342 ILE n 1 343 LYS n 1 344 VAL n 1 345 ASP n 1 346 ASN n 1 347 ILE n 1 348 VAL n 1 349 HIS n 1 350 ILE n 1 351 ARG n 1 352 ASN n 1 353 ASP n 1 354 HIS n 1 355 HIS n 1 356 HIS n 1 357 HIS n 1 358 HIS n 1 359 HIS 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 ;baker's yeast ; _entity_src_gen.gene_src_genus Saccharomyces _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 'Saccharomyces cerevisiae' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 4932 _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 'Escherichia coli' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 562 _entity_src_gen.host_org_genus Escherichia _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 'BL21 Star' _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 YFH7_YEAST _struct_ref.pdbx_db_accession P43591 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;MVDTHKLADDVLQLLDNRIEDNYRVCVILVGSPGSGKSTIAEELCQIINEKYHTFLSEHPNVIEVNDRLKPMVNLVDSLK TLQPNKVAEMIENQGLFKDHVEDVNFQPVKYSALTSNNEECTAVVARGGTANAIRIAAVDNPVNVNKLAQDSINIAQIVP MDGFHLSRRCLDLFKDPQTAHKRRGSPSTFDSNNFLQLCKILAKTSLCKVSSHHKFYSTSSVFEKLSKTFSQTIPDIFVP GFNHALKDPTPDQYCISKFTRIVILEGLYLLYDQENWKKIYKTLADTGALLVYKIDIDYEATEERVAKRHLQSGLVTTIA EGREKFRSNDLLNGRDIDNHLIKVDNIVHIRND ; _struct_ref.pdbx_align_begin 1 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 2GAA _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 1 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 353 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession P43591 _struct_ref_seq.db_align_beg 1 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 353 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 1 _struct_ref_seq.pdbx_auth_seq_align_end 353 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 2GAA HIS A 354 ? UNP P43591 ? ? 'EXPRESSION TAG' 354 1 1 2GAA HIS A 355 ? UNP P43591 ? ? 'EXPRESSION TAG' 355 2 1 2GAA HIS A 356 ? UNP P43591 ? ? 'EXPRESSION TAG' 356 3 1 2GAA HIS A 357 ? UNP P43591 ? ? 'EXPRESSION TAG' 357 4 1 2GAA HIS A 358 ? UNP P43591 ? ? 'EXPRESSION TAG' 358 5 1 2GAA HIS A 359 ? UNP P43591 ? ? 'EXPRESSION TAG' 359 6 # 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 CME 'L-peptide linking' n 'S,S-(2-HYDROXYETHYL)THIOCYSTEINE' ? 'C5 H11 N O3 S2' 197.276 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 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 SO4 non-polymer . 'SULFATE ION' ? 'O4 S -2' 96.063 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 2GAA _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.07 _exptl_crystal.density_percent_sol 40.70 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 298 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 6.5 _exptl_crystal_grow.pdbx_details ;PEG 5000MME ammonium sulfate, pH 6.5,VAPOR DIFFUSION, HANGING DROP, temperature 298K ; _exptl_crystal_grow.pdbx_pH_range . # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type MARRESEARCH _diffrn_detector.pdbx_collection_date 2005-02-20 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.98 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ESRF BEAMLINE ID23-1' _diffrn_source.pdbx_synchrotron_site ESRF _diffrn_source.pdbx_synchrotron_beamline ID23-1 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 0.98 # _reflns.entry_id 2GAA _reflns.observed_criterion_sigma_I 1 _reflns.observed_criterion_sigma_F 1 _reflns.d_resolution_low 20 _reflns.d_resolution_high 1.95 _reflns.number_obs 23765 _reflns.number_all 23990 _reflns.percent_possible_obs 99.1 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value 0.059 _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 2.8 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 # _reflns_shell.d_res_high 1.95 _reflns_shell.d_res_low 2.06 _reflns_shell.percent_possible_all 99 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value 0.378 _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_redundancy 2.5 _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all 3436 _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_diffrn_id ? _reflns_shell.pdbx_ordinal 1 # _refine.entry_id 2GAA _refine.ls_number_reflns_obs 23765 _refine.ls_number_reflns_all 23990 _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 2 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 20 _refine.ls_d_res_high 1.95 _refine.ls_percent_reflns_obs ? _refine.ls_R_factor_obs ? _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.193 _refine.ls_R_factor_R_free 0.232 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free ? _refine.ls_number_reflns_R_free 1156 _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 ? _refine.details ? _refine.pdbx_starting_model 2GA8 _refine.pdbx_method_to_determine_struct 'FOURIER SYNTHESIS' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'Engh & Huber' _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.overall_SU_B ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_overall_phase_error ? _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _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 2625 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 5 _refine_hist.number_atoms_solvent 180 _refine_hist.number_atoms_total 2810 _refine_hist.d_res_high 1.95 _refine_hist.d_res_low 20 # 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 c_bond_d 0.0048 ? ? ? 'X-RAY DIFFRACTION' ? c_angle_deg 1.19 ? ? ? 'X-RAY DIFFRACTION' ? # _struct.entry_id 2GAA _struct.title 'Crystal structure of YFH7 from Saccharomyces cerevisiae: a putative P-loop containing kinase with a circular permutation.' _struct.pdbx_descriptor 'Hypothetical 39.9 kDa protein' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 2GAA _struct_keywords.pdbx_keywords 'UNKNOWN FUNCTION' _struct_keywords.text 'YFR007w, YFH7, UNKNOWN FUNCTION' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? # _struct_biol.id 1 _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 ASP A 3 ? ILE A 19 ? ASP A 3 ILE A 19 1 ? 17 HELX_P HELX_P2 2 GLY A 36 ? HIS A 59 ? GLY A 36 HIS A 59 1 ? 24 HELX_P HELX_P3 3 GLN A 83 ? ASN A 93 ? GLN A 83 ASN A 93 1 ? 11 HELX_P HELX_P4 4 PHE A 97 ? VAL A 101 ? PHE A 97 VAL A 101 5 ? 5 HELX_P HELX_P5 5 GLY A 128 ? ALA A 133 ? GLY A 128 ALA A 133 5 ? 6 HELX_P HELX_P6 6 ASP A 162 ? HIS A 165 ? ASP A 162 HIS A 165 5 ? 4 HELX_P HELX_P7 7 SER A 167 ? LEU A 173 ? SER A 167 LEU A 173 1 ? 7 HELX_P HELX_P8 8 ASP A 176 ? ARG A 183 ? ASP A 176 ARG A 183 1 ? 8 HELX_P HELX_P9 9 SER A 186 ? PHE A 190 ? SER A 186 PHE A 190 5 ? 5 HELX_P HELX_P10 10 ASP A 191 ? LEU A 207 ? ASP A 191 LEU A 207 1 ? 17 HELX_P HELX_P11 11 SER A 221 ? LYS A 228 ? SER A 221 LYS A 228 1 ? 8 HELX_P HELX_P12 12 GLN A 274 ? ASP A 286 ? GLN A 274 ASP A 286 1 ? 13 HELX_P HELX_P13 13 ASP A 298 ? SER A 313 ? ASP A 298 SER A 313 1 ? 16 HELX_P HELX_P14 14 THR A 318 ? ASN A 329 ? THR A 318 ASN A 329 1 ? 12 HELX_P HELX_P15 15 GLY A 334 ? HIS A 340 ? GLY A 334 HIS A 340 1 ? 7 # _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 covale1 covale ? ? A LEU 44 C ? ? ? 1_555 A CME 45 N ? ? A LEU 44 A CME 45 1_555 ? ? ? ? ? ? ? 1.325 ? covale2 covale ? ? A CME 45 C ? ? ? 1_555 A GLN 46 N ? ? A CME 45 A GLN 46 1_555 ? ? ? ? ? ? ? 1.464 ? covale3 covale ? ? A GLU 120 C ? ? ? 1_555 A CME 121 N ? ? A GLU 120 A CME 121 1_555 ? ? ? ? ? ? ? 1.215 ? covale4 covale ? ? A CME 121 C ? ? ? 1_555 A THR 122 N ? ? A CME 121 A THR 122 1_555 ? ? ? ? ? ? ? 1.551 ? covale5 covale ? ? A LEU 207 C ? ? ? 1_555 A CME 208 N ? ? A LEU 207 A CME 208 1_555 ? ? ? ? ? ? ? 1.138 ? covale6 covale ? ? A CME 208 C ? ? ? 1_555 A LYS 209 N ? ? A CME 208 A LYS 209 1_555 ? ? ? ? ? ? ? 1.452 ? # _struct_conn_type.id covale _struct_conn_type.criteria ? _struct_conn_type.reference ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 5 ? B ? 2 ? C ? 6 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? parallel A 2 3 ? parallel A 3 4 ? parallel A 4 5 ? parallel B 1 2 ? parallel C 1 2 ? parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel C 4 5 ? anti-parallel C 5 6 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 ALA A 156 ? PRO A 160 ? ALA A 156 PRO A 160 A 2 ILE A 262 ? GLY A 267 ? ILE A 262 GLY A 267 A 3 VAL A 25 ? VAL A 30 ? VAL A 25 VAL A 30 A 4 LEU A 290 ? ASP A 296 ? LEU A 290 ASP A 296 A 5 ILE A 347 ? ARG A 351 ? ILE A 347 ARG A 351 B 1 VAL A 65 ? ASN A 66 ? VAL A 65 ASN A 66 B 2 PHE A 230 ? SER A 231 ? PHE A 230 SER A 231 C 1 LYS A 80 ? THR A 81 ? LYS A 80 THR A 81 C 2 VAL A 109 ? ALA A 113 ? VAL A 109 ALA A 113 C 3 CME A 121 ? VAL A 125 ? CME A 121 VAL A 125 C 4 ILE A 134 ? ALA A 137 ? ILE A 134 ALA A 137 C 5 ILE A 237 ? ASN A 243 ? ILE A 237 ASN A 243 C 6 ASP A 248 ? ILE A 256 ? ASP A 248 ILE A 256 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 N VAL A 159 ? N VAL A 159 O ILE A 264 ? O ILE A 264 A 2 3 O LEU A 265 ? O LEU A 265 N VAL A 27 ? N VAL A 27 A 3 4 N VAL A 30 ? N VAL A 30 O ILE A 295 ? O ILE A 295 A 4 5 N ASP A 296 ? N ASP A 296 O ILE A 350 ? O ILE A 350 B 1 2 N ASN A 66 ? N ASN A 66 O PHE A 230 ? O PHE A 230 C 1 2 N LYS A 80 ? N LYS A 80 O LYS A 110 ? O LYS A 110 C 2 3 N VAL A 109 ? N VAL A 109 O VAL A 125 ? O VAL A 125 C 3 4 N VAL A 124 ? N VAL A 124 O ILE A 134 ? O ILE A 134 C 4 5 N ARG A 135 ? N ARG A 135 O PHE A 238 ? O PHE A 238 C 5 6 N GLY A 241 ? N GLY A 241 O THR A 250 ? O THR A 250 # _struct_site.id AC1 _struct_site.pdbx_evidence_code Software _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 9 _struct_site.details 'BINDING SITE FOR RESIDUE SO4 A 2847' # 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 9 SER A 32 ? SER A 32 . ? 1_555 ? 2 AC1 9 GLY A 34 ? GLY A 34 . ? 1_555 ? 3 AC1 9 SER A 35 ? SER A 35 . ? 1_555 ? 4 AC1 9 GLY A 36 ? GLY A 36 . ? 1_555 ? 5 AC1 9 LYS A 37 ? LYS A 37 . ? 1_555 ? 6 AC1 9 SER A 38 ? SER A 38 . ? 1_555 ? 7 AC1 9 ARG A 309 ? ARG A 309 . ? 1_555 ? 8 AC1 9 HOH C . ? HOH A 2857 . ? 1_555 ? 9 AC1 9 HOH C . ? HOH A 3005 . ? 1_555 ? # _database_PDB_matrix.entry_id 2GAA _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 2GAA _atom_sites.fract_transf_matrix[1][1] 0.007421 _atom_sites.fract_transf_matrix[1][2] 0.004284 _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] 0.008569 _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] 0.020543 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . VAL A 1 2 ? 20.864 -2.201 2.638 1.00 37.70 ? 2 VAL A N 1 ATOM 2 C CA . VAL A 1 2 ? 20.651 -2.256 4.114 1.00 36.53 ? 2 VAL A CA 1 ATOM 3 C C . VAL A 1 2 ? 19.173 -2.064 4.445 1.00 35.10 ? 2 VAL A C 1 ATOM 4 O O . VAL A 1 2 ? 18.454 -1.350 3.745 1.00 37.24 ? 2 VAL A O 1 ATOM 5 C CB . VAL A 1 2 ? 21.478 -1.158 4.838 1.00 36.80 ? 2 VAL A CB 1 ATOM 6 C CG1 . VAL A 1 2 ? 21.004 0.222 4.407 1.00 34.55 ? 2 VAL A CG1 1 ATOM 7 C CG2 . VAL A 1 2 ? 21.363 -1.322 6.345 1.00 35.24 ? 2 VAL A CG2 1 ATOM 8 N N . ASP A 1 3 ? 18.725 -2.715 5.510 1.00 34.98 ? 3 ASP A N 1 ATOM 9 C CA . ASP A 1 3 ? 17.336 -2.615 5.945 1.00 34.72 ? 3 ASP A CA 1 ATOM 10 C C . ASP A 1 3 ? 17.249 -1.492 6.982 1.00 32.91 ? 3 ASP A C 1 ATOM 11 O O . ASP A 1 3 ? 17.628 -1.682 8.136 1.00 32.17 ? 3 ASP A O 1 ATOM 12 C CB . ASP A 1 3 ? 16.898 -3.936 6.575 1.00 36.71 ? 3 ASP A CB 1 ATOM 13 C CG . ASP A 1 3 ? 15.397 -4.038 6.731 1.00 38.31 ? 3 ASP A CG 1 ATOM 14 O OD1 . ASP A 1 3 ? 14.777 -3.088 7.247 1.00 42.22 ? 3 ASP A OD1 1 ATOM 15 O OD2 . ASP A 1 3 ? 14.838 -5.080 6.338 1.00 42.12 ? 3 ASP A OD2 1 ATOM 16 N N . THR A 1 4 ? 16.751 -0.330 6.572 1.00 31.80 ? 4 THR A N 1 ATOM 17 C CA . THR A 1 4 ? 16.655 0.811 7.477 1.00 31.89 ? 4 THR A CA 1 ATOM 18 C C . THR A 1 4 ? 15.604 0.650 8.573 1.00 30.07 ? 4 THR A C 1 ATOM 19 O O . THR A 1 4 ? 15.720 1.251 9.640 1.00 27.93 ? 4 THR A O 1 ATOM 20 C CB . THR A 1 4 ? 16.390 2.116 6.699 1.00 32.58 ? 4 THR A CB 1 ATOM 21 O OG1 . THR A 1 4 ? 15.129 2.032 6.025 1.00 34.67 ? 4 THR A OG1 1 ATOM 22 C CG2 . THR A 1 4 ? 17.489 2.347 5.673 1.00 33.72 ? 4 THR A CG2 1 ATOM 23 N N . HIS A 1 5 ? 14.578 -0.156 8.324 1.00 29.53 ? 5 HIS A N 1 ATOM 24 C CA . HIS A 1 5 ? 13.565 -0.362 9.350 1.00 29.09 ? 5 HIS A CA 1 ATOM 25 C C . HIS A 1 5 ? 14.157 -1.225 10.451 1.00 28.81 ? 5 HIS A C 1 ATOM 26 O O . HIS A 1 5 ? 13.807 -1.084 11.623 1.00 29.00 ? 5 HIS A O 1 ATOM 27 C CB . HIS A 1 5 ? 12.314 -1.022 8.768 1.00 29.80 ? 5 HIS A CB 1 ATOM 28 C CG . HIS A 1 5 ? 11.480 -0.096 7.942 1.00 30.10 ? 5 HIS A CG 1 ATOM 29 N ND1 . HIS A 1 5 ? 11.807 0.246 6.647 1.00 30.44 ? 5 HIS A ND1 1 ATOM 30 C CD2 . HIS A 1 5 ? 10.351 0.591 8.239 1.00 30.58 ? 5 HIS A CD2 1 ATOM 31 C CE1 . HIS A 1 5 ? 10.915 1.103 6.182 1.00 31.63 ? 5 HIS A CE1 1 ATOM 32 N NE2 . HIS A 1 5 ? 10.021 1.329 7.127 1.00 31.58 ? 5 HIS A NE2 1 ATOM 33 N N . LYS A 1 6 ? 15.064 -2.118 10.070 1.00 28.73 ? 6 LYS A N 1 ATOM 34 C CA . LYS A 1 6 ? 15.714 -2.982 11.045 1.00 27.94 ? 6 LYS A CA 1 ATOM 35 C C . LYS A 1 6 ? 16.684 -2.137 11.870 1.00 25.58 ? 6 LYS A C 1 ATOM 36 O O . LYS A 1 6 ? 16.854 -2.373 13.063 1.00 25.60 ? 6 LYS A O 1 ATOM 37 C CB . LYS A 1 6 ? 16.468 -4.116 10.347 1.00 30.10 ? 6 LYS A CB 1 ATOM 38 C CG . LYS A 1 6 ? 17.317 -4.969 11.288 1.00 34.68 ? 6 LYS A CG 1 ATOM 39 C CD . LYS A 1 6 ? 16.473 -5.607 12.387 1.00 38.77 ? 6 LYS A CD 1 ATOM 40 C CE . LYS A 1 6 ? 17.345 -6.313 13.420 1.00 39.55 ? 6 LYS A CE 1 ATOM 41 N NZ . LYS A 1 6 ? 18.167 -7.393 12.808 1.00 44.52 ? 6 LYS A NZ 1 ATOM 42 N N . LEU A 1 7 ? 17.327 -1.161 11.232 1.00 25.04 ? 7 LEU A N 1 ATOM 43 C CA . LEU A 1 7 ? 18.250 -0.290 11.956 1.00 23.60 ? 7 LEU A CA 1 ATOM 44 C C . LEU A 1 7 ? 17.419 0.486 12.962 1.00 21.28 ? 7 LEU A C 1 ATOM 45 O O . LEU A 1 7 ? 17.810 0.651 14.108 1.00 21.68 ? 7 LEU A O 1 ATOM 46 C CB . LEU A 1 7 ? 18.952 0.690 11.016 1.00 25.72 ? 7 LEU A CB 1 ATOM 47 C CG . LEU A 1 7 ? 20.021 0.137 10.072 1.00 26.98 ? 7 LEU A CG 1 ATOM 48 C CD1 . LEU A 1 7 ? 20.736 1.293 9.403 1.00 27.98 ? 7 LEU A CD1 1 ATOM 49 C CD2 . LEU A 1 7 ? 21.012 -0.708 10.847 1.00 29.12 ? 7 LEU A CD2 1 ATOM 50 N N . ALA A 1 8 ? 16.263 0.957 12.514 1.00 20.13 ? 8 ALA A N 1 ATOM 51 C CA . ALA A 1 8 ? 15.356 1.696 13.377 1.00 20.65 ? 8 ALA A CA 1 ATOM 52 C C . ALA A 1 8 ? 14.988 0.824 14.577 1.00 18.91 ? 8 ALA A C 1 ATOM 53 O O . ALA A 1 8 ? 14.958 1.298 15.706 1.00 17.30 ? 8 ALA A O 1 ATOM 54 C CB . ALA A 1 8 ? 14.101 2.092 12.604 1.00 18.12 ? 8 ALA A CB 1 ATOM 55 N N . ASP A 1 9 ? 14.718 -0.454 14.331 1.00 21.05 ? 9 ASP A N 1 ATOM 56 C CA . ASP A 1 9 ? 14.360 -1.368 15.415 1.00 22.26 ? 9 ASP A CA 1 ATOM 57 C C . ASP A 1 9 ? 15.513 -1.561 16.388 1.00 21.86 ? 9 ASP A C 1 ATOM 58 O O . ASP A 1 9 ? 15.302 -1.632 17.596 1.00 18.77 ? 9 ASP A O 1 ATOM 59 C CB . ASP A 1 9 ? 13.930 -2.735 14.872 1.00 26.17 ? 9 ASP A CB 1 ATOM 60 C CG . ASP A 1 9 ? 12.561 -2.701 14.205 1.00 28.74 ? 9 ASP A CG 1 ATOM 61 O OD1 . ASP A 1 9 ? 11.800 -1.728 14.410 1.00 27.75 ? 9 ASP A OD1 1 ATOM 62 O OD2 . ASP A 1 9 ? 12.246 -3.666 13.481 1.00 33.68 ? 9 ASP A OD2 1 ATOM 63 N N . ASP A 1 10 ? 16.732 -1.653 15.867 1.00 21.27 ? 10 ASP A N 1 ATOM 64 C CA . ASP A 1 10 ? 17.884 -1.826 16.739 1.00 21.60 ? 10 ASP A CA 1 ATOM 65 C C . ASP A 1 10 ? 18.143 -0.570 17.566 1.00 19.92 ? 10 ASP A C 1 ATOM 66 O O . ASP A 1 10 ? 18.533 -0.659 18.729 1.00 18.54 ? 10 ASP A O 1 ATOM 67 C CB . ASP A 1 10 ? 19.129 -2.200 15.926 1.00 25.15 ? 10 ASP A CB 1 ATOM 68 C CG . ASP A 1 10 ? 19.000 -3.566 15.259 1.00 28.76 ? 10 ASP A CG 1 ATOM 69 O OD1 . ASP A 1 10 ? 18.417 -4.482 15.875 1.00 31.77 ? 10 ASP A OD1 1 ATOM 70 O OD2 . ASP A 1 10 ? 19.487 -3.728 14.127 1.00 29.95 ? 10 ASP A OD2 1 ATOM 71 N N . VAL A 1 11 ? 17.910 0.598 16.971 1.00 19.02 ? 11 VAL A N 1 ATOM 72 C CA . VAL A 1 11 ? 18.113 1.864 17.675 1.00 18.55 ? 11 VAL A CA 1 ATOM 73 C C . VAL A 1 11 ? 17.117 2.007 18.824 1.00 18.28 ? 11 VAL A C 1 ATOM 74 O O . VAL A 1 11 ? 17.482 2.418 19.930 1.00 17.50 ? 11 VAL A O 1 ATOM 75 C CB . VAL A 1 11 ? 17.949 3.063 16.725 1.00 18.83 ? 11 VAL A CB 1 ATOM 76 C CG1 . VAL A 1 11 ? 18.005 4.364 17.514 1.00 19.55 ? 11 VAL A CG1 1 ATOM 77 C CG2 . VAL A 1 11 ? 19.045 3.041 15.675 1.00 19.35 ? 11 VAL A CG2 1 ATOM 78 N N . LEU A 1 12 ? 15.858 1.667 18.559 1.00 17.45 ? 12 LEU A N 1 ATOM 79 C CA . LEU A 1 12 ? 14.827 1.753 19.582 1.00 19.48 ? 12 LEU A CA 1 ATOM 80 C C . LEU A 1 12 ? 15.090 0.738 20.687 1.00 19.28 ? 12 LEU A C 1 ATOM 81 O O . LEU A 1 12 ? 14.778 0.984 21.848 1.00 19.80 ? 12 LEU A O 1 ATOM 82 C CB . LEU A 1 12 ? 13.443 1.526 18.969 1.00 19.04 ? 12 LEU A CB 1 ATOM 83 C CG . LEU A 1 12 ? 12.971 2.637 18.027 1.00 21.93 ? 12 LEU A CG 1 ATOM 84 C CD1 . LEU A 1 12 ? 11.597 2.296 17.485 1.00 21.73 ? 12 LEU A CD1 1 ATOM 85 C CD2 . LEU A 1 12 ? 12.935 3.966 18.769 1.00 21.79 ? 12 LEU A CD2 1 ATOM 86 N N . GLN A 1 13 ? 15.665 -0.405 20.326 1.00 20.68 ? 13 GLN A N 1 ATOM 87 C CA . GLN A 1 13 ? 15.963 -1.418 21.326 1.00 21.51 ? 13 GLN A CA 1 ATOM 88 C C . GLN A 1 13 ? 17.042 -0.923 22.286 1.00 20.94 ? 13 GLN A C 1 ATOM 89 O O . GLN A 1 13 ? 16.956 -1.150 23.492 1.00 19.81 ? 13 GLN A O 1 ATOM 90 C CB . GLN A 1 13 ? 16.414 -2.721 20.663 1.00 23.56 ? 13 GLN A CB 1 ATOM 91 C CG . GLN A 1 13 ? 16.854 -3.775 21.665 1.00 28.21 ? 13 GLN A CG 1 ATOM 92 C CD . GLN A 1 13 ? 16.979 -5.151 21.048 1.00 34.22 ? 13 GLN A CD 1 ATOM 93 O OE1 . GLN A 1 13 ? 17.726 -5.349 20.087 1.00 39.47 ? 13 GLN A OE1 1 ATOM 94 N NE2 . GLN A 1 13 ? 16.245 -6.113 21.597 1.00 36.88 ? 13 GLN A NE2 1 ATOM 95 N N . LEU A 1 14 ? 18.061 -0.250 21.756 1.00 20.43 ? 14 LEU A N 1 ATOM 96 C CA . LEU A 1 14 ? 19.118 0.274 22.616 1.00 19.68 ? 14 LEU A CA 1 ATOM 97 C C . LEU A 1 14 ? 18.561 1.390 23.485 1.00 17.56 ? 14 LEU A C 1 ATOM 98 O O . LEU A 1 14 ? 18.808 1.439 24.685 1.00 18.94 ? 14 LEU A O 1 ATOM 99 C CB . LEU A 1 14 ? 20.286 0.821 21.794 1.00 20.58 ? 14 LEU A CB 1 ATOM 100 C CG . LEU A 1 14 ? 21.439 1.360 22.660 1.00 22.39 ? 14 LEU A CG 1 ATOM 101 C CD1 . LEU A 1 14 ? 21.941 0.257 23.588 1.00 21.55 ? 14 LEU A CD1 1 ATOM 102 C CD2 . LEU A 1 14 ? 22.569 1.855 21.777 1.00 21.71 ? 14 LEU A CD2 1 ATOM 103 N N . LEU A 1 15 ? 17.809 2.296 22.873 1.00 16.34 ? 15 LEU A N 1 ATOM 104 C CA . LEU A 1 15 ? 17.223 3.400 23.619 1.00 16.37 ? 15 LEU A CA 1 ATOM 105 C C . LEU A 1 15 ? 16.365 2.870 24.764 1.00 15.78 ? 15 LEU A C 1 ATOM 106 O O . LEU A 1 15 ? 16.446 3.358 25.895 1.00 16.43 ? 15 LEU A O 1 ATOM 107 C CB . LEU A 1 15 ? 16.366 4.273 22.695 1.00 16.04 ? 15 LEU A CB 1 ATOM 108 C CG . LEU A 1 15 ? 15.657 5.460 23.350 1.00 18.52 ? 15 LEU A CG 1 ATOM 109 C CD1 . LEU A 1 15 ? 16.669 6.337 24.073 1.00 17.06 ? 15 LEU A CD1 1 ATOM 110 C CD2 . LEU A 1 15 ? 14.913 6.270 22.292 1.00 19.66 ? 15 LEU A CD2 1 ATOM 111 N N . ASP A 1 16 ? 15.539 1.872 24.465 1.00 15.59 ? 16 ASP A N 1 ATOM 112 C CA . ASP A 1 16 ? 14.674 1.288 25.484 1.00 17.68 ? 16 ASP A CA 1 ATOM 113 C C . ASP A 1 16 ? 15.506 0.674 26.602 1.00 18.44 ? 16 ASP A C 1 ATOM 114 O O . ASP A 1 16 ? 15.208 0.854 27.776 1.00 17.41 ? 16 ASP A O 1 ATOM 115 C CB . ASP A 1 16 ? 13.772 0.212 24.877 1.00 17.15 ? 16 ASP A CB 1 ATOM 116 C CG . ASP A 1 16 ? 12.776 -0.326 25.877 1.00 19.26 ? 16 ASP A CG 1 ATOM 117 O OD1 . ASP A 1 16 ? 11.881 0.437 26.291 1.00 16.49 ? 16 ASP A OD1 1 ATOM 118 O OD2 . ASP A 1 16 ? 12.898 -1.505 26.260 1.00 19.39 ? 16 ASP A OD2 1 ATOM 119 N N . ASN A 1 17 ? 16.551 -0.055 26.229 1.00 21.55 ? 17 ASN A N 1 ATOM 120 C CA . ASN A 1 17 ? 17.427 -0.687 27.209 1.00 24.82 ? 17 ASN A CA 1 ATOM 121 C C . ASN A 1 17 ? 18.173 0.333 28.075 1.00 24.18 ? 17 ASN A C 1 ATOM 122 O O . ASN A 1 17 ? 18.468 0.066 29.237 1.00 23.01 ? 17 ASN A O 1 ATOM 123 C CB . ASN A 1 17 ? 18.446 -1.585 26.498 1.00 29.08 ? 17 ASN A CB 1 ATOM 124 C CG . ASN A 1 17 ? 17.959 -3.019 26.337 1.00 36.29 ? 17 ASN A CG 1 ATOM 125 O OD1 . ASN A 1 17 ? 18.382 -3.731 25.419 1.00 38.41 ? 17 ASN A OD1 1 ATOM 126 N ND2 . ASN A 1 17 ? 17.079 -3.456 27.238 1.00 36.86 ? 17 ASN A ND2 1 ATOM 127 N N . ARG A 1 18 ? 18.458 1.503 27.512 1.00 22.14 ? 18 ARG A N 1 ATOM 128 C CA . ARG A 1 18 ? 19.204 2.538 28.225 1.00 21.11 ? 18 ARG A CA 1 ATOM 129 C C . ARG A 1 18 ? 18.347 3.695 28.725 1.00 20.28 ? 18 ARG A C 1 ATOM 130 O O . ARG A 1 18 ? 18.871 4.697 29.206 1.00 20.05 ? 18 ARG A O 1 ATOM 131 C CB . ARG A 1 18 ? 20.307 3.086 27.308 1.00 19.04 ? 18 ARG A CB 1 ATOM 132 C CG . ARG A 1 18 ? 21.289 2.029 26.802 1.00 20.86 ? 18 ARG A CG 1 ATOM 133 C CD . ARG A 1 18 ? 22.124 1.445 27.934 1.00 17.22 ? 18 ARG A CD 1 ATOM 134 N NE . ARG A 1 18 ? 22.896 2.489 28.598 1.00 21.54 ? 18 ARG A NE 1 ATOM 135 C CZ . ARG A 1 18 ? 23.779 2.280 29.570 1.00 22.00 ? 18 ARG A CZ 1 ATOM 136 N NH1 . ARG A 1 18 ? 24.015 1.051 30.006 1.00 25.82 ? 18 ARG A NH1 1 ATOM 137 N NH2 . ARG A 1 18 ? 24.432 3.306 30.105 1.00 23.48 ? 18 ARG A NH2 1 ATOM 138 N N . ILE A 1 19 ? 17.032 3.541 28.630 1.00 21.57 ? 19 ILE A N 1 ATOM 139 C CA . ILE A 1 19 ? 16.091 4.578 29.026 1.00 22.52 ? 19 ILE A CA 1 ATOM 140 C C . ILE A 1 19 ? 16.366 5.218 30.388 1.00 22.98 ? 19 ILE A C 1 ATOM 141 O O . ILE A 1 19 ? 16.158 6.416 30.569 1.00 22.41 ? 19 ILE A O 1 ATOM 142 C CB . ILE A 1 19 ? 14.643 4.028 28.998 1.00 24.32 ? 19 ILE A CB 1 ATOM 143 C CG1 . ILE A 1 19 ? 13.653 5.190 29.013 1.00 28.10 ? 19 ILE A CG1 1 ATOM 144 C CG2 . ILE A 1 19 ? 14.406 3.089 30.174 1.00 26.61 ? 19 ILE A CG2 1 ATOM 145 C CD1 . ILE A 1 19 ? 13.695 6.035 27.743 1.00 26.20 ? 19 ILE A CD1 1 ATOM 146 N N . GLU A 1 20 ? 16.840 4.423 31.341 1.00 22.29 ? 20 GLU A N 1 ATOM 147 C CA . GLU A 1 20 ? 17.124 4.933 32.679 1.00 25.26 ? 20 GLU A CA 1 ATOM 148 C C . GLU A 1 20 ? 18.565 5.398 32.884 1.00 24.46 ? 20 GLU A C 1 ATOM 149 O O . GLU A 1 20 ? 18.870 6.040 33.890 1.00 25.38 ? 20 GLU A O 1 ATOM 150 C CB . GLU A 1 20 ? 16.796 3.861 33.720 1.00 27.69 ? 20 GLU A CB 1 ATOM 151 C CG . GLU A 1 20 ? 15.312 3.627 33.940 1.00 35.06 ? 20 GLU A CG 1 ATOM 152 C CD . GLU A 1 20 ? 15.042 2.413 34.807 1.00 38.57 ? 20 GLU A CD 1 ATOM 153 O OE1 . GLU A 1 20 ? 15.602 2.333 35.922 1.00 40.85 ? 20 GLU A OE1 1 ATOM 154 O OE2 . GLU A 1 20 ? 14.269 1.537 34.372 1.00 42.53 ? 20 GLU A OE2 1 ATOM 155 N N . ASP A 1 21 ? 19.442 5.090 31.934 1.00 23.19 ? 21 ASP A N 1 ATOM 156 C CA . ASP A 1 21 ? 20.853 5.453 32.051 1.00 23.84 ? 21 ASP A CA 1 ATOM 157 C C . ASP A 1 21 ? 21.337 6.538 31.090 1.00 23.64 ? 21 ASP A C 1 ATOM 158 O O . ASP A 1 21 ? 22.361 7.185 31.336 1.00 23.85 ? 21 ASP A O 1 ATOM 159 C CB . ASP A 1 21 ? 21.718 4.210 31.850 1.00 25.50 ? 21 ASP A CB 1 ATOM 160 C CG . ASP A 1 21 ? 21.310 3.066 32.752 1.00 28.21 ? 21 ASP A CG 1 ATOM 161 O OD1 . ASP A 1 21 ? 21.288 3.264 33.984 1.00 30.65 ? 21 ASP A OD1 1 ATOM 162 O OD2 . ASP A 1 21 ? 21.012 1.973 32.229 1.00 30.29 ? 21 ASP A OD2 1 ATOM 163 N N . ASN A 1 22 ? 20.614 6.730 29.995 1.00 19.75 ? 22 ASN A N 1 ATOM 164 C CA . ASN A 1 22 ? 21.016 7.725 29.007 1.00 19.93 ? 22 ASN A CA 1 ATOM 165 C C . ASN A 1 22 ? 19.827 8.488 28.462 1.00 17.65 ? 22 ASN A C 1 ATOM 166 O O . ASN A 1 22 ? 18.840 7.893 28.027 1.00 18.55 ? 22 ASN A O 1 ATOM 167 C CB . ASN A 1 22 ? 21.758 7.061 27.836 1.00 17.06 ? 22 ASN A CB 1 ATOM 168 C CG . ASN A 1 22 ? 23.050 6.378 28.263 1.00 18.60 ? 22 ASN A CG 1 ATOM 169 O OD1 . ASN A 1 22 ? 23.065 5.185 28.575 1.00 17.12 ? 22 ASN A OD1 1 ATOM 170 N ND2 . ASN A 1 22 ? 24.143 7.137 28.279 1.00 16.68 ? 22 ASN A ND2 1 ATOM 171 N N . TYR A 1 23 ? 19.934 9.809 28.483 1.00 15.93 ? 23 TYR A N 1 ATOM 172 C CA . TYR A 1 23 ? 18.875 10.662 27.978 1.00 17.91 ? 23 TYR A CA 1 ATOM 173 C C . TYR A 1 23 ? 18.721 10.478 26.462 1.00 18.54 ? 23 TYR A C 1 ATOM 174 O O . TYR A 1 23 ? 17.630 10.613 25.916 1.00 16.88 ? 23 TYR A O 1 ATOM 175 C CB . TYR A 1 23 ? 19.184 12.121 28.290 1.00 16.61 ? 23 TYR A CB 1 ATOM 176 C CG . TYR A 1 23 ? 18.032 13.023 27.949 1.00 19.53 ? 23 TYR A CG 1 ATOM 177 C CD1 . TYR A 1 23 ? 16.885 13.040 28.746 1.00 13.88 ? 23 TYR A CD1 1 ATOM 178 C CD2 . TYR A 1 23 ? 18.062 13.827 26.810 1.00 15.42 ? 23 TYR A CD2 1 ATOM 179 C CE1 . TYR A 1 23 ? 15.806 13.829 28.418 1.00 16.07 ? 23 TYR A CE1 1 ATOM 180 C CE2 . TYR A 1 23 ? 16.975 14.628 26.472 1.00 16.75 ? 23 TYR A CE2 1 ATOM 181 C CZ . TYR A 1 23 ? 15.850 14.619 27.286 1.00 15.14 ? 23 TYR A CZ 1 ATOM 182 O OH . TYR A 1 23 ? 14.768 15.396 26.973 1.00 16.34 ? 23 TYR A OH 1 ATOM 183 N N . ARG A 1 24 ? 19.822 10.179 25.782 1.00 19.06 ? 24 ARG A N 1 ATOM 184 C CA . ARG A 1 24 ? 19.760 9.968 24.342 1.00 21.20 ? 24 ARG A CA 1 ATOM 185 C C . ARG A 1 24 ? 20.767 8.933 23.863 1.00 21.58 ? 24 ARG A C 1 ATOM 186 O O . ARG A 1 24 ? 21.793 8.702 24.503 1.00 22.28 ? 24 ARG A O 1 ATOM 187 C CB . ARG A 1 24 ? 19.956 11.295 23.589 1.00 24.70 ? 24 ARG A CB 1 ATOM 188 C CG . ARG A 1 24 ? 21.053 12.185 24.143 1.00 24.19 ? 24 ARG A CG 1 ATOM 189 C CD . ARG A 1 24 ? 21.242 13.453 23.324 1.00 25.16 ? 24 ARG A CD 1 ATOM 190 N NE . ARG A 1 24 ? 20.014 14.225 23.175 1.00 26.35 ? 24 ARG A NE 1 ATOM 191 C CZ . ARG A 1 24 ? 19.946 15.549 23.278 1.00 21.67 ? 24 ARG A CZ 1 ATOM 192 N NH1 . ARG A 1 24 ? 21.034 16.258 23.538 1.00 20.50 ? 24 ARG A NH1 1 ATOM 193 N NH2 . ARG A 1 24 ? 18.789 16.168 23.106 1.00 22.56 ? 24 ARG A NH2 1 ATOM 194 N N . VAL A 1 25 ? 20.438 8.273 22.757 1.00 20.47 ? 25 VAL A N 1 ATOM 195 C CA . VAL A 1 25 ? 21.323 7.281 22.178 1.00 19.25 ? 25 VAL A CA 1 ATOM 196 C C . VAL A 1 25 ? 21.928 7.915 20.940 1.00 17.53 ? 25 VAL A C 1 ATOM 197 O O . VAL A 1 25 ? 21.270 8.694 20.242 1.00 17.24 ? 25 VAL A O 1 ATOM 198 C CB . VAL A 1 25 ? 20.568 5.991 21.747 1.00 21.59 ? 25 VAL A CB 1 ATOM 199 C CG1 . VAL A 1 25 ? 19.876 5.361 22.946 1.00 26.23 ? 25 VAL A CG1 1 ATOM 200 C CG2 . VAL A 1 25 ? 19.561 6.313 20.662 1.00 25.38 ? 25 VAL A CG2 1 ATOM 201 N N . CYS A 1 26 ? 23.186 7.600 20.680 1.00 17.08 ? 26 CYS A N 1 ATOM 202 C CA . CYS A 1 26 ? 23.859 8.123 19.508 1.00 17.11 ? 26 CYS A CA 1 ATOM 203 C C . CYS A 1 26 ? 24.088 6.999 18.516 1.00 16.98 ? 26 CYS A C 1 ATOM 204 O O . CYS A 1 26 ? 24.270 5.841 18.896 1.00 15.61 ? 26 CYS A O 1 ATOM 205 C CB . CYS A 1 26 ? 25.201 8.745 19.882 1.00 18.74 ? 26 CYS A CB 1 ATOM 206 S SG . CYS A 1 26 ? 25.058 10.234 20.896 1.00 20.22 ? 26 CYS A SG 1 ATOM 207 N N . VAL A 1 27 ? 24.065 7.356 17.241 1.00 14.34 ? 27 VAL A N 1 ATOM 208 C CA . VAL A 1 27 ? 24.304 6.408 16.180 1.00 15.37 ? 27 VAL A CA 1 ATOM 209 C C . VAL A 1 27 ? 25.410 6.993 15.313 1.00 14.15 ? 27 VAL A C 1 ATOM 210 O O . VAL A 1 27 ? 25.340 8.149 14.908 1.00 15.50 ? 27 VAL A O 1 ATOM 211 C CB . VAL A 1 27 ? 23.049 6.194 15.306 1.00 16.88 ? 27 VAL A CB 1 ATOM 212 C CG1 . VAL A 1 27 ? 23.378 5.269 14.145 1.00 16.27 ? 27 VAL A CG1 1 ATOM 213 C CG2 . VAL A 1 27 ? 21.912 5.619 16.150 1.00 19.57 ? 27 VAL A CG2 1 ATOM 214 N N . ILE A 1 28 ? 26.450 6.209 15.071 1.00 14.23 ? 28 ILE A N 1 ATOM 215 C CA . ILE A 1 28 ? 27.534 6.656 14.205 1.00 15.29 ? 28 ILE A CA 1 ATOM 216 C C . ILE A 1 28 ? 27.353 5.894 12.899 1.00 16.05 ? 28 ILE A C 1 ATOM 217 O O . ILE A 1 28 ? 27.153 4.679 12.914 1.00 17.27 ? 28 ILE A O 1 ATOM 218 C CB . ILE A 1 28 ? 28.919 6.329 14.798 1.00 13.57 ? 28 ILE A CB 1 ATOM 219 C CG1 . ILE A 1 28 ? 29.276 7.359 15.872 1.00 13.94 ? 28 ILE A CG1 1 ATOM 220 C CG2 . ILE A 1 28 ? 29.976 6.313 13.687 1.00 15.01 ? 28 ILE A CG2 1 ATOM 221 C CD1 . ILE A 1 28 ? 30.620 7.098 16.539 1.00 16.90 ? 28 ILE A CD1 1 ATOM 222 N N . LEU A 1 29 ? 27.390 6.618 11.782 1.00 15.04 ? 29 LEU A N 1 ATOM 223 C CA . LEU A 1 29 ? 27.238 6.030 10.455 1.00 15.69 ? 29 LEU A CA 1 ATOM 224 C C . LEU A 1 29 ? 28.359 6.572 9.570 1.00 14.66 ? 29 LEU A C 1 ATOM 225 O O . LEU A 1 29 ? 28.380 7.757 9.232 1.00 16.14 ? 29 LEU A O 1 ATOM 226 C CB . LEU A 1 29 ? 25.881 6.407 9.852 1.00 17.33 ? 29 LEU A CB 1 ATOM 227 C CG . LEU A 1 29 ? 25.632 5.889 8.431 1.00 21.06 ? 29 LEU A CG 1 ATOM 228 C CD1 . LEU A 1 29 ? 25.682 4.361 8.424 1.00 21.03 ? 29 LEU A CD1 1 ATOM 229 C CD2 . LEU A 1 29 ? 24.284 6.385 7.927 1.00 22.62 ? 29 LEU A CD2 1 ATOM 230 N N . VAL A 1 30 ? 29.291 5.705 9.206 1.00 13.32 ? 30 VAL A N 1 ATOM 231 C CA . VAL A 1 30 ? 30.422 6.108 8.381 1.00 13.71 ? 30 VAL A CA 1 ATOM 232 C C . VAL A 1 30 ? 30.383 5.499 6.990 1.00 14.82 ? 30 VAL A C 1 ATOM 233 O O . VAL A 1 30 ? 30.011 4.337 6.811 1.00 15.45 ? 30 VAL A O 1 ATOM 234 C CB . VAL A 1 30 ? 31.766 5.715 9.048 1.00 15.18 ? 30 VAL A CB 1 ATOM 235 C CG1 . VAL A 1 30 ? 32.922 5.911 8.071 1.00 12.89 ? 30 VAL A CG1 1 ATOM 236 C CG2 . VAL A 1 30 ? 31.987 6.557 10.290 1.00 12.67 ? 30 VAL A CG2 1 ATOM 237 N N . GLY A 1 31 ? 30.783 6.304 6.010 1.00 16.91 ? 31 GLY A N 1 ATOM 238 C CA . GLY A 1 31 ? 30.829 5.855 4.632 1.00 16.27 ? 31 GLY A CA 1 ATOM 239 C C . GLY A 1 31 ? 31.756 6.755 3.837 1.00 16.39 ? 31 GLY A C 1 ATOM 240 O O . GLY A 1 31 ? 31.880 7.946 4.136 1.00 13.70 ? 31 GLY A O 1 ATOM 241 N N . SER A 1 32 ? 32.415 6.194 2.828 1.00 15.62 ? 32 SER A N 1 ATOM 242 C CA . SER A 1 32 ? 33.309 6.983 1.995 1.00 18.04 ? 32 SER A CA 1 ATOM 243 C C . SER A 1 32 ? 32.415 7.743 1.017 1.00 18.65 ? 32 SER A C 1 ATOM 244 O O . SER A 1 32 ? 31.203 7.517 0.984 1.00 18.67 ? 32 SER A O 1 ATOM 245 C CB . SER A 1 32 ? 34.290 6.068 1.251 1.00 18.07 ? 32 SER A CB 1 ATOM 246 O OG . SER A 1 32 ? 33.613 5.124 0.446 1.00 21.62 ? 32 SER A OG 1 ATOM 247 N N . PRO A 1 33 ? 32.991 8.662 0.224 1.00 18.64 ? 33 PRO A N 1 ATOM 248 C CA . PRO A 1 33 ? 32.189 9.428 -0.733 1.00 19.87 ? 33 PRO A CA 1 ATOM 249 C C . PRO A 1 33 ? 31.344 8.543 -1.654 1.00 21.79 ? 33 PRO A C 1 ATOM 250 O O . PRO A 1 33 ? 31.833 7.562 -2.213 1.00 22.60 ? 33 PRO A O 1 ATOM 251 C CB . PRO A 1 33 ? 33.242 10.230 -1.497 1.00 19.94 ? 33 PRO A CB 1 ATOM 252 C CG . PRO A 1 33 ? 34.297 10.463 -0.455 1.00 17.31 ? 33 PRO A CG 1 ATOM 253 C CD . PRO A 1 33 ? 34.401 9.100 0.191 1.00 18.51 ? 33 PRO A CD 1 ATOM 254 N N . GLY A 1 34 ? 30.067 8.892 -1.790 1.00 22.50 ? 34 GLY A N 1 ATOM 255 C CA . GLY A 1 34 ? 29.173 8.133 -2.644 1.00 21.59 ? 34 GLY A CA 1 ATOM 256 C C . GLY A 1 34 ? 28.627 6.853 -2.040 1.00 19.97 ? 34 GLY A C 1 ATOM 257 O O . GLY A 1 34 ? 27.990 6.071 -2.731 1.00 18.96 ? 34 GLY A O 1 ATOM 258 N N . SER A 1 35 ? 28.869 6.640 -0.751 1.00 18.91 ? 35 SER A N 1 ATOM 259 C CA . SER A 1 35 ? 28.397 5.438 -0.070 1.00 18.71 ? 35 SER A CA 1 ATOM 260 C C . SER A 1 35 ? 26.914 5.504 0.260 1.00 18.42 ? 35 SER A C 1 ATOM 261 O O . SER A 1 35 ? 26.293 4.482 0.537 1.00 19.98 ? 35 SER A O 1 ATOM 262 C CB . SER A 1 35 ? 29.175 5.236 1.229 1.00 20.23 ? 35 SER A CB 1 ATOM 263 O OG . SER A 1 35 ? 28.959 6.333 2.103 1.00 18.62 ? 35 SER A OG 1 ATOM 264 N N . GLY A 1 36 ? 26.346 6.706 0.243 1.00 19.97 ? 36 GLY A N 1 ATOM 265 C CA . GLY A 1 36 ? 24.934 6.852 0.555 1.00 21.57 ? 36 GLY A CA 1 ATOM 266 C C . GLY A 1 36 ? 24.624 6.987 2.044 1.00 22.20 ? 36 GLY A C 1 ATOM 267 O O . GLY A 1 36 ? 23.503 6.713 2.471 1.00 23.00 ? 36 GLY A O 1 ATOM 268 N N . LYS A 1 37 ? 25.605 7.405 2.840 1.00 22.08 ? 37 LYS A N 1 ATOM 269 C CA . LYS A 1 37 ? 25.396 7.574 4.279 1.00 22.08 ? 37 LYS A CA 1 ATOM 270 C C . LYS A 1 37 ? 24.376 8.678 4.557 1.00 20.82 ? 37 LYS A C 1 ATOM 271 O O . LYS A 1 37 ? 23.652 8.647 5.552 1.00 20.50 ? 37 LYS A O 1 ATOM 272 C CB . LYS A 1 37 ? 26.721 7.908 4.967 1.00 21.74 ? 37 LYS A CB 1 ATOM 273 C CG . LYS A 1 37 ? 27.467 9.069 4.339 1.00 20.55 ? 37 LYS A CG 1 ATOM 274 C CD . LYS A 1 37 ? 28.786 9.322 5.042 1.00 20.90 ? 37 LYS A CD 1 ATOM 275 C CE . LYS A 1 37 ? 29.577 10.418 4.342 1.00 20.33 ? 37 LYS A CE 1 ATOM 276 N NZ . LYS A 1 37 ? 30.007 9.991 2.978 1.00 20.59 ? 37 LYS A NZ 1 ATOM 277 N N . SER A 1 38 ? 24.318 9.648 3.660 1.00 22.34 ? 38 SER A N 1 ATOM 278 C CA . SER A 1 38 ? 23.395 10.764 3.796 1.00 25.21 ? 38 SER A CA 1 ATOM 279 C C . SER A 1 38 ? 21.938 10.293 3.719 1.00 25.32 ? 38 SER A C 1 ATOM 280 O O . SER A 1 38 ? 21.117 10.650 4.567 1.00 25.84 ? 38 SER A O 1 ATOM 281 C CB . SER A 1 38 ? 23.684 11.793 2.697 1.00 29.01 ? 38 SER A CB 1 ATOM 282 O OG . SER A 1 38 ? 22.962 12.992 2.907 1.00 35.07 ? 38 SER A OG 1 ATOM 283 N N . THR A 1 39 ? 21.625 9.478 2.714 1.00 25.21 ? 39 THR A N 1 ATOM 284 C CA . THR A 1 39 ? 20.267 8.973 2.530 1.00 26.66 ? 39 THR A CA 1 ATOM 285 C C . THR A 1 39 ? 19.875 7.922 3.567 1.00 25.12 ? 39 THR A C 1 ATOM 286 O O . THR A 1 39 ? 18.722 7.856 3.985 1.00 25.83 ? 39 THR A O 1 ATOM 287 C CB . THR A 1 39 ? 20.070 8.375 1.107 1.00 28.17 ? 39 THR A CB 1 ATOM 288 O OG1 . THR A 1 39 ? 20.914 7.232 0.934 1.00 31.97 ? 39 THR A OG1 1 ATOM 289 C CG2 . THR A 1 39 ? 20.423 9.404 0.049 1.00 29.49 ? 39 THR A CG2 1 ATOM 290 N N . ILE A 1 40 ? 20.826 7.091 3.974 1.00 23.16 ? 40 ILE A N 1 ATOM 291 C CA . ILE A 1 40 ? 20.535 6.077 4.974 1.00 21.97 ? 40 ILE A CA 1 ATOM 292 C C . ILE A 1 40 ? 20.187 6.781 6.285 1.00 22.37 ? 40 ILE A C 1 ATOM 293 O O . ILE A 1 40 ? 19.205 6.437 6.946 1.00 20.99 ? 40 ILE A O 1 ATOM 294 C CB . ILE A 1 40 ? 21.749 5.144 5.192 1.00 23.10 ? 40 ILE A CB 1 ATOM 295 C CG1 . ILE A 1 40 ? 22.022 4.344 3.912 1.00 24.13 ? 40 ILE A CG1 1 ATOM 296 C CG2 . ILE A 1 40 ? 21.479 4.185 6.349 1.00 22.58 ? 40 ILE A CG2 1 ATOM 297 C CD1 . ILE A 1 40 ? 23.245 3.445 3.997 1.00 23.01 ? 40 ILE A CD1 1 ATOM 298 N N . ALA A 1 41 ? 20.987 7.782 6.642 1.00 19.98 ? 41 ALA A N 1 ATOM 299 C CA . ALA A 1 41 ? 20.771 8.536 7.873 1.00 21.06 ? 41 ALA A CA 1 ATOM 300 C C . ALA A 1 41 ? 19.419 9.245 7.881 1.00 22.27 ? 41 ALA A C 1 ATOM 301 O O . ALA A 1 41 ? 18.692 9.208 8.875 1.00 22.40 ? 41 ALA A O 1 ATOM 302 C CB . ALA A 1 41 ? 21.898 9.556 8.059 1.00 17.59 ? 41 ALA A CB 1 ATOM 303 N N . GLU A 1 42 ? 19.080 9.887 6.768 1.00 23.90 ? 42 GLU A N 1 ATOM 304 C CA . GLU A 1 42 ? 17.816 10.608 6.671 1.00 24.36 ? 42 GLU A CA 1 ATOM 305 C C . GLU A 1 42 ? 16.639 9.653 6.728 1.00 23.63 ? 42 GLU A C 1 ATOM 306 O O . GLU A 1 42 ? 15.635 9.936 7.378 1.00 21.18 ? 42 GLU A O 1 ATOM 307 C CB . GLU A 1 42 ? 17.774 11.430 5.378 1.00 28.59 ? 42 GLU A CB 1 ATOM 308 C CG . GLU A 1 42 ? 18.896 12.456 5.288 1.00 35.56 ? 42 GLU A CG 1 ATOM 309 C CD . GLU A 1 42 ? 18.804 13.339 4.059 1.00 40.73 ? 42 GLU A CD 1 ATOM 310 O OE1 . GLU A 1 42 ? 18.796 12.801 2.931 1.00 44.65 ? 42 GLU A OE1 1 ATOM 311 O OE2 . GLU A 1 42 ? 18.746 14.577 4.223 1.00 44.49 ? 42 GLU A OE2 1 ATOM 312 N N . GLU A 1 43 ? 16.773 8.516 6.054 1.00 24.03 ? 43 GLU A N 1 ATOM 313 C CA . GLU A 1 43 ? 15.722 7.506 6.022 1.00 24.17 ? 43 GLU A CA 1 ATOM 314 C C . GLU A 1 43 ? 15.495 6.940 7.425 1.00 23.17 ? 43 GLU A C 1 ATOM 315 O O . GLU A 1 43 ? 14.357 6.832 7.895 1.00 20.45 ? 43 GLU A O 1 ATOM 316 C CB . GLU A 1 43 ? 16.116 6.391 5.051 1.00 26.67 ? 43 GLU A CB 1 ATOM 317 C CG . GLU A 1 43 ? 15.024 5.392 4.749 1.00 32.59 ? 43 GLU A CG 1 ATOM 318 C CD . GLU A 1 43 ? 15.375 4.499 3.572 1.00 37.76 ? 43 GLU A CD 1 ATOM 319 O OE1 . GLU A 1 43 ? 15.680 5.038 2.485 1.00 41.48 ? 43 GLU A OE1 1 ATOM 320 O OE2 . GLU A 1 43 ? 15.343 3.260 3.730 1.00 40.84 ? 43 GLU A OE2 1 ATOM 321 N N . LEU A 1 44 ? 16.584 6.586 8.095 1.00 20.53 ? 44 LEU A N 1 ATOM 322 C CA . LEU A 1 44 ? 16.506 6.047 9.448 1.00 19.58 ? 44 LEU A CA 1 ATOM 323 C C . LEU A 1 44 ? 15.817 7.033 10.395 1.00 19.61 ? 44 LEU A C 1 ATOM 324 O O . LEU A 1 44 ? 14.911 6.667 11.143 1.00 18.83 ? 44 LEU A O 1 ATOM 325 C CB . LEU A 1 44 ? 17.918 5.737 9.959 1.00 19.34 ? 44 LEU A CB 1 ATOM 326 C CG . LEU A 1 44 ? 18.087 5.336 11.430 1.00 18.80 ? 44 LEU A CG 1 ATOM 327 C CD1 . LEU A 1 44 ? 17.248 4.111 11.755 1.00 19.29 ? 44 LEU A CD1 1 ATOM 328 C CD2 . LEU A 1 44 ? 19.559 5.061 11.697 1.00 19.18 ? 44 LEU A CD2 1 HETATM 329 N N . CME A 1 45 ? 16.227 8.277 10.197 1.00 21.17 ? 45 CME A N 1 HETATM 330 C CA . CME A 1 45 ? 15.710 9.350 11.042 1.00 22.60 ? 45 CME A CA 1 HETATM 331 C CB . CME A 1 45 ? 16.478 10.629 10.733 1.00 26.47 ? 45 CME A CB 1 HETATM 332 S SG . CME A 1 45 ? 15.880 12.103 11.604 1.00 27.64 ? 45 CME A SG 1 HETATM 333 S SD . CME A 1 45 ? 14.641 12.986 10.255 1.00 40.89 ? 45 CME A SD 1 HETATM 334 C CE . CME A 1 45 ? 15.137 14.738 10.296 1.00 42.58 ? 45 CME A CE 1 HETATM 335 C CZ . CME A 1 45 ? 16.469 14.971 9.616 1.00 45.56 ? 45 CME A CZ 1 HETATM 336 O OH . CME A 1 45 ? 16.752 16.204 9.441 1.00 49.77 ? 45 CME A OH 1 HETATM 337 C C . CME A 1 45 ? 14.211 9.610 10.883 1.00 24.58 ? 45 CME A C 1 HETATM 338 O O . CME A 1 45 ? 13.414 9.447 11.809 1.00 22.88 ? 45 CME A O 1 ATOM 339 N N . GLN A 1 46 ? 14.041 9.307 9.461 1.00 32.96 ? 46 GLN A N 1 ATOM 340 C CA . GLN A 1 46 ? 12.615 9.538 9.305 1.00 30.18 ? 46 GLN A CA 1 ATOM 341 C C . GLN A 1 46 ? 11.801 8.387 9.879 1.00 27.07 ? 46 GLN A C 1 ATOM 342 O O . GLN A 1 46 ? 10.644 8.563 10.264 1.00 24.93 ? 46 GLN A O 1 ATOM 343 C CB . GLN A 1 46 ? 12.293 9.728 7.824 1.00 33.13 ? 46 GLN A CB 1 ATOM 344 C CG . GLN A 1 46 ? 12.739 11.072 7.297 1.00 38.36 ? 46 GLN A CG 1 ATOM 345 C CD . GLN A 1 46 ? 11.926 12.208 7.883 1.00 41.03 ? 46 GLN A CD 1 ATOM 346 O OE1 . GLN A 1 46 ? 12.312 13.374 7.798 1.00 43.44 ? 46 GLN A OE1 1 ATOM 347 N NE2 . GLN A 1 46 ? 10.782 11.872 8.475 1.00 43.87 ? 46 GLN A NE2 1 ATOM 348 N N . ILE A 1 47 ? 11.937 7.304 9.438 1.00 25.03 ? 47 ILE A N 1 ATOM 349 C CA . ILE A 1 47 ? 11.258 6.138 9.985 1.00 24.19 ? 47 ILE A CA 1 ATOM 350 C C . ILE A 1 47 ? 10.979 6.229 11.483 1.00 22.85 ? 47 ILE A C 1 ATOM 351 O O . ILE A 1 47 ? 9.853 6.004 11.927 1.00 20.38 ? 47 ILE A O 1 ATOM 352 C CB . ILE A 1 47 ? 12.066 4.861 9.702 1.00 23.46 ? 47 ILE A CB 1 ATOM 353 C CG1 . ILE A 1 47 ? 12.126 4.628 8.190 1.00 25.60 ? 47 ILE A CG1 1 ATOM 354 C CG2 . ILE A 1 47 ? 11.439 3.667 10.418 1.00 25.94 ? 47 ILE A CG2 1 ATOM 355 C CD1 . ILE A 1 47 ? 12.889 3.384 7.782 1.00 24.98 ? 47 ILE A CD1 1 ATOM 356 N N . ILE A 1 48 ? 12.003 6.555 12.263 1.00 22.27 ? 48 ILE A N 1 ATOM 357 C CA . ILE A 1 48 ? 11.833 6.660 13.707 1.00 20.44 ? 48 ILE A CA 1 ATOM 358 C C . ILE A 1 48 ? 10.824 7.740 14.080 1.00 21.22 ? 48 ILE A C 1 ATOM 359 O O . ILE A 1 48 ? 9.934 7.504 14.900 1.00 18.61 ? 48 ILE A O 1 ATOM 360 C CB . ILE A 1 48 ? 13.174 6.944 14.409 1.00 19.70 ? 48 ILE A CB 1 ATOM 361 C CG1 . ILE A 1 48 ? 14.076 5.709 14.292 1.00 20.29 ? 48 ILE A CG1 1 ATOM 362 C CG2 . ILE A 1 48 ? 12.929 7.321 15.881 1.00 16.36 ? 48 ILE A CG2 1 ATOM 363 C CD1 . ILE A 1 48 ? 15.540 5.954 14.654 1.00 20.27 ? 48 ILE A CD1 1 ATOM 364 N N . ASN A 1 49 ? 10.955 8.921 13.485 1.00 20.28 ? 49 ASN A N 1 ATOM 365 C CA . ASN A 1 49 ? 10.021 9.996 13.792 1.00 21.80 ? 49 ASN A CA 1 ATOM 366 C C . ASN A 1 49 ? 8.589 9.632 13.387 1.00 22.02 ? 49 ASN A C 1 ATOM 367 O O . ASN A 1 49 ? 7.643 9.932 14.113 1.00 21.23 ? 49 ASN A O 1 ATOM 368 C CB . ASN A 1 49 ? 10.452 11.302 13.120 1.00 19.06 ? 49 ASN A CB 1 ATOM 369 C CG . ASN A 1 49 ? 11.682 11.917 13.771 1.00 20.49 ? 49 ASN A CG 1 ATOM 370 O OD1 . ASN A 1 49 ? 11.847 11.863 14.991 1.00 20.96 ? 49 ASN A OD1 1 ATOM 371 N ND2 . ASN A 1 49 ? 12.542 12.521 12.959 1.00 20.81 ? 49 ASN A ND2 1 ATOM 372 N N . GLU A 1 50 ? 8.428 8.983 12.236 1.00 22.23 ? 50 GLU A N 1 ATOM 373 C CA . GLU A 1 50 ? 7.099 8.570 11.776 1.00 23.23 ? 50 GLU A CA 1 ATOM 374 C C . GLU A 1 50 ? 6.460 7.633 12.794 1.00 22.64 ? 50 GLU A C 1 ATOM 375 O O . GLU A 1 50 ? 5.274 7.750 13.111 1.00 23.35 ? 50 GLU A O 1 ATOM 376 C CB . GLU A 1 50 ? 7.193 7.845 10.430 1.00 24.50 ? 50 GLU A CB 1 ATOM 377 C CG . GLU A 1 50 ? 7.226 8.753 9.217 1.00 33.22 ? 50 GLU A CG 1 ATOM 378 C CD . GLU A 1 50 ? 7.555 7.995 7.936 1.00 37.95 ? 50 GLU A CD 1 ATOM 379 O OE1 . GLU A 1 50 ? 7.057 6.858 7.773 1.00 37.20 ? 50 GLU A OE1 1 ATOM 380 O OE2 . GLU A 1 50 ? 8.305 8.541 7.094 1.00 40.31 ? 50 GLU A OE2 1 ATOM 381 N N . LYS A 1 51 ? 7.250 6.683 13.284 1.00 21.70 ? 51 LYS A N 1 ATOM 382 C CA . LYS A 1 51 ? 6.777 5.732 14.273 1.00 19.43 ? 51 LYS A CA 1 ATOM 383 C C . LYS A 1 51 ? 6.290 6.467 15.517 1.00 20.37 ? 51 LYS A C 1 ATOM 384 O O . LYS A 1 51 ? 5.259 6.121 16.100 1.00 18.20 ? 51 LYS A O 1 ATOM 385 C CB . LYS A 1 51 ? 7.904 4.779 14.666 1.00 20.84 ? 51 LYS A CB 1 ATOM 386 C CG . LYS A 1 51 ? 8.139 3.629 13.706 1.00 24.17 ? 51 LYS A CG 1 ATOM 387 C CD . LYS A 1 51 ? 9.351 2.823 14.153 1.00 28.20 ? 51 LYS A CD 1 ATOM 388 C CE . LYS A 1 51 ? 9.410 1.457 13.487 1.00 29.98 ? 51 LYS A CE 1 ATOM 389 N NZ . LYS A 1 51 ? 8.282 0.579 13.934 1.00 32.17 ? 51 LYS A NZ 1 ATOM 390 N N . TYR A 1 52 ? 7.037 7.485 15.926 1.00 17.99 ? 52 TYR A N 1 ATOM 391 C CA . TYR A 1 52 ? 6.662 8.237 17.112 1.00 20.24 ? 52 TYR A CA 1 ATOM 392 C C . TYR A 1 52 ? 5.365 9.013 16.899 1.00 20.49 ? 52 TYR A C 1 ATOM 393 O O . TYR A 1 52 ? 4.505 9.049 17.777 1.00 20.46 ? 52 TYR A O 1 ATOM 394 C CB . TYR A 1 52 ? 7.787 9.195 17.519 1.00 19.56 ? 52 TYR A CB 1 ATOM 395 C CG . TYR A 1 52 ? 7.559 9.846 18.867 1.00 19.45 ? 52 TYR A CG 1 ATOM 396 C CD1 . TYR A 1 52 ? 7.395 9.073 20.021 1.00 19.20 ? 52 TYR A CD1 1 ATOM 397 C CD2 . TYR A 1 52 ? 7.479 11.231 18.987 1.00 19.72 ? 52 TYR A CD2 1 ATOM 398 C CE1 . TYR A 1 52 ? 7.151 9.668 21.261 1.00 14.92 ? 52 TYR A CE1 1 ATOM 399 C CE2 . TYR A 1 52 ? 7.237 11.832 20.221 1.00 19.30 ? 52 TYR A CE2 1 ATOM 400 C CZ . TYR A 1 52 ? 7.074 11.046 21.347 1.00 17.41 ? 52 TYR A CZ 1 ATOM 401 O OH . TYR A 1 52 ? 6.827 11.645 22.556 1.00 20.71 ? 52 TYR A OH 1 ATOM 402 N N . HIS A 1 53 ? 5.224 9.627 15.730 1.00 20.21 ? 53 HIS A N 1 ATOM 403 C CA . HIS A 1 53 ? 4.021 10.394 15.424 1.00 21.18 ? 53 HIS A CA 1 ATOM 404 C C . HIS A 1 53 ? 2.801 9.474 15.426 1.00 21.43 ? 53 HIS A C 1 ATOM 405 O O . HIS A 1 53 ? 1.734 9.843 15.915 1.00 22.55 ? 53 HIS A O 1 ATOM 406 C CB . HIS A 1 53 ? 4.184 11.084 14.069 1.00 19.26 ? 53 HIS A CB 1 ATOM 407 C CG . HIS A 1 53 ? 5.285 12.100 14.047 1.00 21.41 ? 53 HIS A CG 1 ATOM 408 N ND1 . HIS A 1 53 ? 5.959 12.446 12.896 1.00 21.78 ? 53 HIS A ND1 1 ATOM 409 C CD2 . HIS A 1 53 ? 5.841 12.834 15.041 1.00 19.13 ? 53 HIS A CD2 1 ATOM 410 C CE1 . HIS A 1 53 ? 6.885 13.344 13.181 1.00 20.79 ? 53 HIS A CE1 1 ATOM 411 N NE2 . HIS A 1 53 ? 6.834 13.597 14.477 1.00 20.93 ? 53 HIS A NE2 1 ATOM 412 N N . THR A 1 54 ? 2.973 8.271 14.892 1.00 22.47 ? 54 THR A N 1 ATOM 413 C CA . THR A 1 54 ? 1.898 7.292 14.847 1.00 23.08 ? 54 THR A CA 1 ATOM 414 C C . THR A 1 54 ? 1.511 6.905 16.276 1.00 23.32 ? 54 THR A C 1 ATOM 415 O O . THR A 1 54 ? 0.340 6.709 16.584 1.00 23.72 ? 54 THR A O 1 ATOM 416 C CB . THR A 1 54 ? 2.345 6.047 14.054 1.00 23.45 ? 54 THR A CB 1 ATOM 417 O OG1 . THR A 1 54 ? 2.676 6.443 12.719 1.00 22.69 ? 54 THR A OG1 1 ATOM 418 C CG2 . THR A 1 54 ? 1.232 4.994 14.002 1.00 24.95 ? 54 THR A CG2 1 ATOM 419 N N . PHE A 1 55 ? 2.506 6.803 17.151 1.00 24.05 ? 55 PHE A N 1 ATOM 420 C CA . PHE A 1 55 ? 2.257 6.468 18.545 1.00 22.71 ? 55 PHE A CA 1 ATOM 421 C C . PHE A 1 55 ? 1.497 7.610 19.217 1.00 22.89 ? 55 PHE A C 1 ATOM 422 O O . PHE A 1 55 ? 0.556 7.378 19.974 1.00 22.44 ? 55 PHE A O 1 ATOM 423 C CB . PHE A 1 55 ? 3.579 6.236 19.281 1.00 21.89 ? 55 PHE A CB 1 ATOM 424 C CG . PHE A 1 55 ? 3.453 6.281 20.779 1.00 21.22 ? 55 PHE A CG 1 ATOM 425 C CD1 . PHE A 1 55 ? 2.945 5.196 21.484 1.00 19.45 ? 55 PHE A CD1 1 ATOM 426 C CD2 . PHE A 1 55 ? 3.829 7.421 21.481 1.00 20.35 ? 55 PHE A CD2 1 ATOM 427 C CE1 . PHE A 1 55 ? 2.813 5.244 22.872 1.00 21.58 ? 55 PHE A CE1 1 ATOM 428 C CE2 . PHE A 1 55 ? 3.700 7.480 22.866 1.00 20.37 ? 55 PHE A CE2 1 ATOM 429 C CZ . PHE A 1 55 ? 3.191 6.389 23.562 1.00 20.77 ? 55 PHE A CZ 1 ATOM 430 N N . LEU A 1 56 ? 1.922 8.841 18.946 1.00 23.31 ? 56 LEU A N 1 ATOM 431 C CA . LEU A 1 56 ? 1.278 10.022 19.519 1.00 24.09 ? 56 LEU A CA 1 ATOM 432 C C . LEU A 1 56 ? -0.183 10.139 19.106 1.00 24.02 ? 56 LEU A C 1 ATOM 433 O O . LEU A 1 56 ? -1.007 10.644 19.867 1.00 24.08 ? 56 LEU A O 1 ATOM 434 C CB . LEU A 1 56 ? 2.007 11.293 19.092 1.00 23.21 ? 56 LEU A CB 1 ATOM 435 C CG . LEU A 1 56 ? 3.354 11.554 19.754 1.00 23.54 ? 56 LEU A CG 1 ATOM 436 C CD1 . LEU A 1 56 ? 3.944 12.840 19.195 1.00 20.42 ? 56 LEU A CD1 1 ATOM 437 C CD2 . LEU A 1 56 ? 3.172 11.645 21.273 1.00 23.81 ? 56 LEU A CD2 1 ATOM 438 N N . SER A 1 57 ? -0.490 9.687 17.894 1.00 21.99 ? 57 SER A N 1 ATOM 439 C CA . SER A 1 57 ? -1.853 9.737 17.379 1.00 24.53 ? 57 SER A CA 1 ATOM 440 C C . SER A 1 57 ? -2.864 9.167 18.377 1.00 23.60 ? 57 SER A C 1 ATOM 441 O O . SER A 1 57 ? -3.924 9.753 18.597 1.00 24.26 ? 57 SER A O 1 ATOM 442 C CB . SER A 1 57 ? -1.944 8.959 16.060 1.00 25.38 ? 57 SER A CB 1 ATOM 443 O OG . SER A 1 57 ? -3.294 8.819 15.653 1.00 29.75 ? 57 SER A OG 1 ATOM 444 N N . GLU A 1 58 ? -2.525 8.035 18.990 1.00 23.58 ? 58 GLU A N 1 ATOM 445 C CA . GLU A 1 58 ? -3.411 7.386 19.947 1.00 24.81 ? 58 GLU A CA 1 ATOM 446 C C . GLU A 1 58 ? -3.058 7.595 21.417 1.00 24.19 ? 58 GLU A C 1 ATOM 447 O O . GLU A 1 58 ? -3.733 7.075 22.308 1.00 23.68 ? 58 GLU A O 1 ATOM 448 C CB . GLU A 1 58 ? -3.510 5.894 19.613 1.00 28.87 ? 58 GLU A CB 1 ATOM 449 C CG . GLU A 1 58 ? -4.341 5.658 18.359 1.00 34.18 ? 58 GLU A CG 1 ATOM 450 C CD . GLU A 1 58 ? -4.364 4.210 17.906 1.00 38.43 ? 58 GLU A CD 1 ATOM 451 O OE1 . GLU A 1 58 ? -4.458 3.312 18.769 1.00 41.11 ? 58 GLU A OE1 1 ATOM 452 O OE2 . GLU A 1 58 ? -4.309 3.977 16.680 1.00 38.30 ? 58 GLU A OE2 1 ATOM 453 N N . HIS A 1 59 ? -1.994 8.354 21.661 1.00 22.91 ? 59 HIS A N 1 ATOM 454 C CA . HIS A 1 59 ? -1.554 8.695 23.012 1.00 21.63 ? 59 HIS A CA 1 ATOM 455 C C . HIS A 1 59 ? -1.302 10.193 22.931 1.00 22.50 ? 59 HIS A C 1 ATOM 456 O O . HIS A 1 59 ? -0.203 10.655 23.217 1.00 22.28 ? 59 HIS A O 1 ATOM 457 C CB . HIS A 1 59 ? -0.253 7.970 23.367 1.00 21.09 ? 59 HIS A CB 1 ATOM 458 C CG . HIS A 1 59 ? -0.349 6.483 23.279 1.00 19.75 ? 59 HIS A CG 1 ATOM 459 N ND1 . HIS A 1 59 ? -0.340 5.806 22.078 1.00 21.64 ? 59 HIS A ND1 1 ATOM 460 C CD2 . HIS A 1 59 ? -0.510 5.543 24.240 1.00 20.33 ? 59 HIS A CD2 1 ATOM 461 C CE1 . HIS A 1 59 ? -0.492 4.514 22.302 1.00 21.05 ? 59 HIS A CE1 1 ATOM 462 N NE2 . HIS A 1 59 ? -0.598 4.327 23.606 1.00 21.66 ? 59 HIS A NE2 1 ATOM 463 N N . PRO A 1 60 ? -2.342 10.968 22.549 1.00 22.91 ? 60 PRO A N 1 ATOM 464 C CA . PRO A 1 60 ? -2.401 12.425 22.360 1.00 23.54 ? 60 PRO A CA 1 ATOM 465 C C . PRO A 1 60 ? -1.764 13.345 23.391 1.00 24.12 ? 60 PRO A C 1 ATOM 466 O O . PRO A 1 60 ? -1.156 14.352 23.031 1.00 25.64 ? 60 PRO A O 1 ATOM 467 C CB . PRO A 1 60 ? -3.902 12.705 22.239 1.00 21.93 ? 60 PRO A CB 1 ATOM 468 C CG . PRO A 1 60 ? -4.472 11.420 21.771 1.00 21.78 ? 60 PRO A CG 1 ATOM 469 C CD . PRO A 1 60 ? -3.712 10.420 22.582 1.00 22.72 ? 60 PRO A CD 1 ATOM 470 N N . ASN A 1 61 ? -1.910 13.015 24.667 1.00 25.20 ? 61 ASN A N 1 ATOM 471 C CA . ASN A 1 61 ? -1.382 13.869 25.721 1.00 24.58 ? 61 ASN A CA 1 ATOM 472 C C . ASN A 1 61 ? -0.410 13.168 26.648 1.00 23.82 ? 61 ASN A C 1 ATOM 473 O O . ASN A 1 61 ? -0.330 13.484 27.833 1.00 22.45 ? 61 ASN A O 1 ATOM 474 C CB . ASN A 1 61 ? -2.556 14.428 26.517 1.00 26.35 ? 61 ASN A CB 1 ATOM 475 C CG . ASN A 1 61 ? -3.553 15.137 25.629 1.00 26.81 ? 61 ASN A CG 1 ATOM 476 O OD1 . ASN A 1 61 ? -3.237 16.165 25.036 1.00 26.67 ? 61 ASN A OD1 1 ATOM 477 N ND2 . ASN A 1 61 ? -4.757 14.581 25.514 1.00 25.05 ? 61 ASN A ND2 1 ATOM 478 N N . VAL A 1 62 ? 0.343 12.228 26.094 1.00 23.79 ? 62 VAL A N 1 ATOM 479 C CA . VAL A 1 62 ? 1.303 11.455 26.870 1.00 23.17 ? 62 VAL A CA 1 ATOM 480 C C . VAL A 1 62 ? 2.583 12.223 27.192 1.00 24.53 ? 62 VAL A C 1 ATOM 481 O O . VAL A 1 62 ? 3.248 11.937 28.191 1.00 24.00 ? 62 VAL A O 1 ATOM 482 C CB . VAL A 1 62 ? 1.683 10.168 26.118 1.00 22.67 ? 62 VAL A CB 1 ATOM 483 C CG1 . VAL A 1 62 ? 2.473 10.522 24.861 1.00 20.15 ? 62 VAL A CG1 1 ATOM 484 C CG2 . VAL A 1 62 ? 2.474 9.233 27.025 1.00 20.81 ? 62 VAL A CG2 1 ATOM 485 N N . ILE A 1 63 ? 2.927 13.199 26.356 1.00 24.86 ? 63 ILE A N 1 ATOM 486 C CA . ILE A 1 63 ? 4.152 13.952 26.575 1.00 27.00 ? 63 ILE A CA 1 ATOM 487 C C . ILE A 1 63 ? 4.131 14.837 27.808 1.00 29.12 ? 63 ILE A C 1 ATOM 488 O O . ILE A 1 63 ? 3.170 15.567 28.065 1.00 29.42 ? 63 ILE A O 1 ATOM 489 C CB . ILE A 1 63 ? 4.516 14.838 25.366 1.00 25.23 ? 63 ILE A CB 1 ATOM 490 C CG1 . ILE A 1 63 ? 4.784 13.968 24.139 1.00 24.39 ? 63 ILE A CG1 1 ATOM 491 C CG2 . ILE A 1 63 ? 5.755 15.663 25.690 1.00 24.46 ? 63 ILE A CG2 1 ATOM 492 C CD1 . ILE A 1 63 ? 5.091 14.767 22.880 1.00 21.65 ? 63 ILE A CD1 1 ATOM 493 N N . GLU A 1 64 ? 5.219 14.759 28.560 1.00 31.76 ? 64 GLU A N 1 ATOM 494 C CA . GLU A 1 64 ? 5.403 15.543 29.769 1.00 33.85 ? 64 GLU A CA 1 ATOM 495 C C . GLU A 1 64 ? 6.883 15.882 29.868 1.00 34.09 ? 64 GLU A C 1 ATOM 496 O O . GLU A 1 64 ? 7.741 15.054 29.543 1.00 34.43 ? 64 GLU A O 1 ATOM 497 C CB . GLU A 1 64 ? 4.985 14.743 30.999 1.00 36.86 ? 64 GLU A CB 1 ATOM 498 C CG . GLU A 1 64 ? 3.552 14.263 30.972 1.00 42.10 ? 64 GLU A CG 1 ATOM 499 C CD . GLU A 1 64 ? 3.102 13.739 32.316 1.00 45.48 ? 64 GLU A CD 1 ATOM 500 O OE1 . GLU A 1 64 ? 3.064 14.541 33.274 1.00 48.63 ? 64 GLU A OE1 1 ATOM 501 O OE2 . GLU A 1 64 ? 2.790 12.531 32.418 1.00 46.94 ? 64 GLU A OE2 1 ATOM 502 N N . VAL A 1 65 ? 7.180 17.102 30.296 1.00 32.53 ? 65 VAL A N 1 ATOM 503 C CA . VAL A 1 65 ? 8.559 17.531 30.447 1.00 32.11 ? 65 VAL A CA 1 ATOM 504 C C . VAL A 1 65 ? 8.857 17.609 31.938 1.00 32.46 ? 65 VAL A C 1 ATOM 505 O O . VAL A 1 65 ? 8.194 18.339 32.678 1.00 33.36 ? 65 VAL A O 1 ATOM 506 C CB . VAL A 1 65 ? 8.796 18.907 29.786 1.00 31.08 ? 65 VAL A CB 1 ATOM 507 C CG1 . VAL A 1 65 ? 10.252 19.310 29.932 1.00 31.12 ? 65 VAL A CG1 1 ATOM 508 C CG2 . VAL A 1 65 ? 8.418 18.844 28.315 1.00 29.86 ? 65 VAL A CG2 1 ATOM 509 N N . ASN A 1 66 ? 9.845 16.837 32.376 1.00 31.50 ? 66 ASN A N 1 ATOM 510 C CA . ASN A 1 66 ? 10.227 16.796 33.781 1.00 31.30 ? 66 ASN A CA 1 ATOM 511 C C . ASN A 1 66 ? 11.372 17.740 34.116 1.00 29.05 ? 66 ASN A C 1 ATOM 512 O O . ASN A 1 66 ? 11.747 18.593 33.312 1.00 26.31 ? 66 ASN A O 1 ATOM 513 C CB . ASN A 1 66 ? 10.642 15.379 34.163 1.00 35.66 ? 66 ASN A CB 1 ATOM 514 C CG . ASN A 1 66 ? 9.609 14.358 33.784 1.00 40.48 ? 66 ASN A CG 1 ATOM 515 O OD1 . ASN A 1 66 ? 8.513 14.324 34.349 1.00 45.24 ? 66 ASN A OD1 1 ATOM 516 N ND2 . ASN A 1 66 ? 9.944 13.518 32.814 1.00 42.90 ? 66 ASN A ND2 1 ATOM 517 N N . ASP A 1 67 ? 11.913 17.565 35.320 1.00 27.59 ? 67 ASP A N 1 ATOM 518 C CA . ASP A 1 67 ? 13.028 18.358 35.823 1.00 30.27 ? 67 ASP A CA 1 ATOM 519 C C . ASP A 1 67 ? 12.775 19.853 35.745 1.00 30.41 ? 67 ASP A C 1 ATOM 520 O O . ASP A 1 67 ? 13.701 20.642 35.568 1.00 30.70 ? 67 ASP A O 1 ATOM 521 C CB . ASP A 1 67 ? 14.299 18.005 35.051 1.00 30.58 ? 67 ASP A CB 1 ATOM 522 C CG . ASP A 1 67 ? 14.539 16.511 34.990 1.00 31.91 ? 67 ASP A CG 1 ATOM 523 O OD1 . ASP A 1 67 ? 14.366 15.841 36.030 1.00 31.36 ? 67 ASP A OD1 1 ATOM 524 O OD2 . ASP A 1 67 ? 14.902 16.009 33.906 1.00 33.53 ? 67 ASP A OD2 1 ATOM 525 N N . ARG A 1 68 ? 11.515 20.239 35.892 1.00 33.05 ? 68 ARG A N 1 ATOM 526 C CA . ARG A 1 68 ? 11.136 21.642 35.824 1.00 35.05 ? 68 ARG A CA 1 ATOM 527 C C . ARG A 1 68 ? 11.785 22.497 36.917 1.00 34.96 ? 68 ARG A C 1 ATOM 528 O O . ARG A 1 68 ? 12.000 23.691 36.719 1.00 36.75 ? 68 ARG A O 1 ATOM 529 C CB . ARG A 1 68 ? 9.612 21.769 35.899 1.00 37.39 ? 68 ARG A CB 1 ATOM 530 C CG . ARG A 1 68 ? 8.870 20.802 34.979 1.00 42.20 ? 68 ARG A CG 1 ATOM 531 C CD . ARG A 1 68 ? 8.302 19.618 35.759 1.00 46.76 ? 68 ARG A CD 1 ATOM 532 N NE . ARG A 1 68 ? 9.264 19.044 36.699 1.00 48.12 ? 68 ARG A NE 1 ATOM 533 C CZ . ARG A 1 68 ? 8.971 18.080 37.567 1.00 50.28 ? 68 ARG A CZ 1 ATOM 534 N NH1 . ARG A 1 68 ? 7.744 17.578 37.613 1.00 52.26 ? 68 ARG A NH1 1 ATOM 535 N NH2 . ARG A 1 68 ? 9.898 17.622 38.397 1.00 50.88 ? 68 ARG A NH2 1 ATOM 536 N N . LEU A 1 69 ? 12.102 21.890 38.058 1.00 34.11 ? 69 LEU A N 1 ATOM 537 C CA . LEU A 1 69 ? 12.716 22.628 39.166 1.00 34.93 ? 69 LEU A CA 1 ATOM 538 C C . LEU A 1 69 ? 14.227 22.435 39.259 1.00 34.98 ? 69 LEU A C 1 ATOM 539 O O . LEU A 1 69 ? 14.846 22.804 40.257 1.00 33.89 ? 69 LEU A O 1 ATOM 540 C CB . LEU A 1 69 ? 12.084 22.219 40.500 1.00 34.43 ? 69 LEU A CB 1 ATOM 541 C CG . LEU A 1 69 ? 10.556 22.256 40.609 1.00 35.56 ? 69 LEU A CG 1 ATOM 542 C CD1 . LEU A 1 69 ? 10.159 22.046 42.059 1.00 35.48 ? 69 LEU A CD1 1 ATOM 543 C CD2 . LEU A 1 69 ? 10.018 23.585 40.100 1.00 35.70 ? 69 LEU A CD2 1 ATOM 544 N N . LYS A 1 70 ? 14.819 21.854 38.222 1.00 34.15 ? 70 LYS A N 1 ATOM 545 C CA . LYS A 1 70 ? 16.257 21.629 38.209 1.00 34.26 ? 70 LYS A CA 1 ATOM 546 C C . LYS A 1 70 ? 16.943 22.657 37.325 1.00 32.74 ? 70 LYS A C 1 ATOM 547 O O . LYS A 1 70 ? 16.334 23.205 36.412 1.00 33.19 ? 70 LYS A O 1 ATOM 548 C CB . LYS A 1 70 ? 16.571 20.218 37.704 1.00 34.40 ? 70 LYS A CB 1 ATOM 549 C CG . LYS A 1 70 ? 16.138 19.118 38.643 1.00 36.36 ? 70 LYS A CG 1 ATOM 550 C CD . LYS A 1 70 ? 16.717 17.785 38.212 1.00 40.93 ? 70 LYS A CD 1 ATOM 551 C CE . LYS A 1 70 ? 16.439 16.701 39.241 1.00 42.14 ? 70 LYS A CE 1 ATOM 552 N NZ . LYS A 1 70 ? 17.051 15.400 38.844 1.00 45.36 ? 70 LYS A NZ 1 ATOM 553 N N . PRO A 1 71 ? 18.224 22.947 37.596 1.00 32.85 ? 71 PRO A N 1 ATOM 554 C CA . PRO A 1 71 ? 18.947 23.926 36.782 1.00 33.18 ? 71 PRO A CA 1 ATOM 555 C C . PRO A 1 71 ? 19.334 23.333 35.430 1.00 33.78 ? 71 PRO A C 1 ATOM 556 O O . PRO A 1 71 ? 19.417 22.114 35.278 1.00 33.96 ? 71 PRO A O 1 ATOM 557 C CB . PRO A 1 71 ? 20.161 24.248 37.642 1.00 32.60 ? 71 PRO A CB 1 ATOM 558 C CG . PRO A 1 71 ? 20.444 22.933 38.296 1.00 33.08 ? 71 PRO A CG 1 ATOM 559 C CD . PRO A 1 71 ? 19.065 22.460 38.704 1.00 32.39 ? 71 PRO A CD 1 ATOM 560 N N . MET A 1 72 ? 19.562 24.195 34.448 1.00 33.87 ? 72 MET A N 1 ATOM 561 C CA . MET A 1 72 ? 19.949 23.744 33.119 1.00 34.14 ? 72 MET A CA 1 ATOM 562 C C . MET A 1 72 ? 21.289 23.027 33.178 1.00 33.21 ? 72 MET A C 1 ATOM 563 O O . MET A 1 72 ? 22.140 23.357 34.000 1.00 32.59 ? 72 MET A O 1 ATOM 564 C CB . MET A 1 72 ? 20.070 24.935 32.168 1.00 35.63 ? 72 MET A CB 1 ATOM 565 C CG . MET A 1 72 ? 18.780 25.689 31.951 1.00 38.16 ? 72 MET A CG 1 ATOM 566 S SD . MET A 1 72 ? 17.520 24.641 31.201 1.00 41.27 ? 72 MET A SD 1 ATOM 567 C CE . MET A 1 72 ? 18.110 24.585 29.499 1.00 36.82 ? 72 MET A CE 1 ATOM 568 N N . VAL A 1 73 ? 21.470 22.038 32.311 1.00 31.50 ? 73 VAL A N 1 ATOM 569 C CA . VAL A 1 73 ? 22.731 21.313 32.255 1.00 31.00 ? 73 VAL A CA 1 ATOM 570 C C . VAL A 1 73 ? 23.732 22.304 31.666 1.00 31.94 ? 73 VAL A C 1 ATOM 571 O O . VAL A 1 73 ? 23.497 22.850 30.587 1.00 31.93 ? 73 VAL A O 1 ATOM 572 C CB . VAL A 1 73 ? 22.633 20.081 31.321 1.00 31.10 ? 73 VAL A CB 1 ATOM 573 C CG1 . VAL A 1 73 ? 23.979 19.374 31.241 1.00 32.53 ? 73 VAL A CG1 1 ATOM 574 C CG2 . VAL A 1 73 ? 21.563 19.125 31.827 1.00 31.15 ? 73 VAL A CG2 1 ATOM 575 N N . ASN A 1 74 ? 24.829 22.560 32.373 1.00 33.16 ? 74 ASN A N 1 ATOM 576 C CA . ASN A 1 74 ? 25.835 23.492 31.867 1.00 35.46 ? 74 ASN A CA 1 ATOM 577 C C . ASN A 1 74 ? 26.745 22.695 30.944 1.00 34.16 ? 74 ASN A C 1 ATOM 578 O O . ASN A 1 74 ? 27.442 21.787 31.382 1.00 33.87 ? 74 ASN A O 1 ATOM 579 C CB . ASN A 1 74 ? 26.653 24.097 33.012 1.00 37.35 ? 74 ASN A CB 1 ATOM 580 C CG . ASN A 1 74 ? 27.445 25.319 32.576 1.00 40.16 ? 74 ASN A CG 1 ATOM 581 O OD1 . ASN A 1 74 ? 28.071 25.321 31.515 1.00 40.85 ? 74 ASN A OD1 1 ATOM 582 N ND2 . ASN A 1 74 ? 27.424 26.362 33.396 1.00 40.40 ? 74 ASN A ND2 1 ATOM 583 N N . LEU A 1 75 ? 26.738 23.033 29.662 1.00 32.71 ? 75 LEU A N 1 ATOM 584 C CA . LEU A 1 75 ? 27.543 22.291 28.705 1.00 32.73 ? 75 LEU A CA 1 ATOM 585 C C . LEU A 1 75 ? 28.897 22.915 28.386 1.00 34.00 ? 75 LEU A C 1 ATOM 586 O O . LEU A 1 75 ? 29.820 22.219 27.964 1.00 36.05 ? 75 LEU A O 1 ATOM 587 C CB . LEU A 1 75 ? 26.736 22.109 27.417 1.00 30.12 ? 75 LEU A CB 1 ATOM 588 C CG . LEU A 1 75 ? 25.366 21.461 27.648 1.00 29.54 ? 75 LEU A CG 1 ATOM 589 C CD1 . LEU A 1 75 ? 24.559 21.444 26.359 1.00 27.79 ? 75 LEU A CD1 1 ATOM 590 C CD2 . LEU A 1 75 ? 25.568 20.050 28.192 1.00 26.88 ? 75 LEU A CD2 1 ATOM 591 N N . VAL A 1 76 ? 29.018 24.216 28.616 1.00 33.37 ? 76 VAL A N 1 ATOM 592 C CA . VAL A 1 76 ? 30.241 24.946 28.303 1.00 35.22 ? 76 VAL A CA 1 ATOM 593 C C . VAL A 1 76 ? 31.118 25.362 29.483 1.00 35.20 ? 76 VAL A C 1 ATOM 594 O O . VAL A 1 76 ? 32.191 25.928 29.284 1.00 34.73 ? 76 VAL A O 1 ATOM 595 C CB . VAL A 1 76 ? 29.896 26.211 27.500 1.00 35.90 ? 76 VAL A CB 1 ATOM 596 C CG1 . VAL A 1 76 ? 29.201 25.823 26.207 1.00 33.94 ? 76 VAL A CG1 1 ATOM 597 C CG2 . VAL A 1 76 ? 28.997 27.116 28.330 1.00 35.23 ? 76 VAL A CG2 1 ATOM 598 N N . ASP A 1 77 ? 30.670 25.078 30.702 1.00 35.36 ? 77 ASP A N 1 ATOM 599 C CA . ASP A 1 77 ? 31.416 25.441 31.908 1.00 37.08 ? 77 ASP A CA 1 ATOM 600 C C . ASP A 1 77 ? 32.903 25.067 31.881 1.00 35.10 ? 77 ASP A C 1 ATOM 601 O O . ASP A 1 77 ? 33.735 25.785 32.426 1.00 33.75 ? 77 ASP A O 1 ATOM 602 C CB . ASP A 1 77 ? 30.761 24.793 33.133 1.00 40.07 ? 77 ASP A CB 1 ATOM 603 C CG . ASP A 1 77 ? 30.764 23.272 33.060 1.00 44.13 ? 77 ASP A CG 1 ATOM 604 O OD1 . ASP A 1 77 ? 31.857 22.671 33.132 1.00 46.42 ? 77 ASP A OD1 1 ATOM 605 O OD2 . ASP A 1 77 ? 29.673 22.676 32.923 1.00 46.01 ? 77 ASP A OD2 1 ATOM 606 N N . SER A 1 78 ? 33.232 23.945 31.248 1.00 34.47 ? 78 SER A N 1 ATOM 607 C CA . SER A 1 78 ? 34.614 23.474 31.184 1.00 33.85 ? 78 SER A CA 1 ATOM 608 C C . SER A 1 78 ? 35.489 24.204 30.169 1.00 32.38 ? 78 SER A C 1 ATOM 609 O O . SER A 1 78 ? 36.707 24.017 30.152 1.00 30.89 ? 78 SER A O 1 ATOM 610 C CB . SER A 1 78 ? 34.639 21.974 30.871 1.00 37.28 ? 78 SER A CB 1 ATOM 611 O OG . SER A 1 78 ? 33.944 21.233 31.860 1.00 43.08 ? 78 SER A OG 1 ATOM 612 N N . LEU A 1 79 ? 34.879 25.030 29.323 1.00 28.80 ? 79 LEU A N 1 ATOM 613 C CA . LEU A 1 79 ? 35.640 25.754 28.314 1.00 27.23 ? 79 LEU A CA 1 ATOM 614 C C . LEU A 1 79 ? 36.025 27.152 28.768 1.00 26.06 ? 79 LEU A C 1 ATOM 615 O O . LEU A 1 79 ? 35.341 27.773 29.575 1.00 25.47 ? 79 LEU A O 1 ATOM 616 C CB . LEU A 1 79 ? 34.849 25.859 27.004 1.00 26.51 ? 79 LEU A CB 1 ATOM 617 C CG . LEU A 1 79 ? 34.420 24.560 26.315 1.00 25.14 ? 79 LEU A CG 1 ATOM 618 C CD1 . LEU A 1 79 ? 33.754 24.904 24.989 1.00 25.81 ? 79 LEU A CD1 1 ATOM 619 C CD2 . LEU A 1 79 ? 35.626 23.655 26.092 1.00 24.39 ? 79 LEU A CD2 1 ATOM 620 N N . LYS A 1 80 ? 37.139 27.629 28.239 1.00 26.45 ? 80 LYS A N 1 ATOM 621 C CA . LYS A 1 80 ? 37.639 28.959 28.536 1.00 26.81 ? 80 LYS A CA 1 ATOM 622 C C . LYS A 1 80 ? 36.783 29.950 27.753 1.00 26.52 ? 80 LYS A C 1 ATOM 623 O O . LYS A 1 80 ? 36.347 29.668 26.635 1.00 24.23 ? 80 LYS A O 1 ATOM 624 C CB . LYS A 1 80 ? 39.107 29.050 28.108 1.00 29.65 ? 80 LYS A CB 1 ATOM 625 C CG . LYS A 1 80 ? 39.588 30.435 27.722 1.00 34.28 ? 80 LYS A CG 1 ATOM 626 C CD . LYS A 1 80 ? 40.974 30.362 27.091 1.00 37.16 ? 80 LYS A CD 1 ATOM 627 C CE . LYS A 1 80 ? 41.337 31.665 26.406 1.00 38.86 ? 80 LYS A CE 1 ATOM 628 N NZ . LYS A 1 80 ? 41.268 32.806 27.358 1.00 40.94 ? 80 LYS A NZ 1 ATOM 629 N N . THR A 1 81 ? 36.523 31.105 28.347 1.00 26.15 ? 81 THR A N 1 ATOM 630 C CA . THR A 1 81 ? 35.718 32.114 27.684 1.00 26.58 ? 81 THR A CA 1 ATOM 631 C C . THR A 1 81 ? 36.600 32.999 26.819 1.00 27.45 ? 81 THR A C 1 ATOM 632 O O . THR A 1 81 ? 37.638 33.484 27.269 1.00 28.06 ? 81 THR A O 1 ATOM 633 C CB . THR A 1 81 ? 34.976 33.014 28.699 1.00 27.08 ? 81 THR A CB 1 ATOM 634 O OG1 . THR A 1 81 ? 34.081 32.220 29.483 1.00 28.84 ? 81 THR A OG1 1 ATOM 635 C CG2 . THR A 1 81 ? 34.183 34.089 27.977 1.00 27.76 ? 81 THR A CG2 1 ATOM 636 N N . LEU A 1 82 ? 36.190 33.194 25.571 1.00 26.37 ? 82 LEU A N 1 ATOM 637 C CA . LEU A 1 82 ? 36.933 34.056 24.669 1.00 29.27 ? 82 LEU A CA 1 ATOM 638 C C . LEU A 1 82 ? 36.571 35.452 25.154 1.00 29.62 ? 82 LEU A C 1 ATOM 639 O O . LEU A 1 82 ? 35.439 35.896 24.976 1.00 30.16 ? 82 LEU A O 1 ATOM 640 C CB . LEU A 1 82 ? 36.462 33.866 23.223 1.00 25.59 ? 82 LEU A CB 1 ATOM 641 C CG . LEU A 1 82 ? 37.238 34.656 22.164 1.00 25.99 ? 82 LEU A CG 1 ATOM 642 C CD1 . LEU A 1 82 ? 38.696 34.234 22.181 1.00 24.93 ? 82 LEU A CD1 1 ATOM 643 C CD2 . LEU A 1 82 ? 36.639 34.412 20.790 1.00 25.61 ? 82 LEU A CD2 1 ATOM 644 N N . GLN A 1 83 ? 37.520 36.131 25.787 1.00 32.82 ? 83 GLN A N 1 ATOM 645 C CA . GLN A 1 83 ? 37.261 37.468 26.311 1.00 35.12 ? 83 GLN A CA 1 ATOM 646 C C . GLN A 1 83 ? 36.736 38.410 25.228 1.00 34.53 ? 83 GLN A C 1 ATOM 647 O O . GLN A 1 83 ? 37.117 38.307 24.063 1.00 32.59 ? 83 GLN A O 1 ATOM 648 C CB . GLN A 1 83 ? 38.529 38.036 26.948 1.00 37.87 ? 83 GLN A CB 1 ATOM 649 C CG . GLN A 1 83 ? 39.064 37.197 28.107 1.00 40.59 ? 83 GLN A CG 1 ATOM 650 C CD . GLN A 1 83 ? 38.013 36.923 29.175 1.00 43.70 ? 83 GLN A CD 1 ATOM 651 O OE1 . GLN A 1 83 ? 37.327 37.836 29.641 1.00 44.30 ? 83 GLN A OE1 1 ATOM 652 N NE2 . GLN A 1 83 ? 37.892 35.660 29.575 1.00 43.50 ? 83 GLN A NE2 1 ATOM 653 N N . PRO A 1 84 ? 35.853 39.348 25.609 1.00 35.99 ? 84 PRO A N 1 ATOM 654 C CA . PRO A 1 84 ? 35.252 40.322 24.693 1.00 36.02 ? 84 PRO A CA 1 ATOM 655 C C . PRO A 1 84 ? 36.200 40.943 23.671 1.00 35.54 ? 84 PRO A C 1 ATOM 656 O O . PRO A 1 84 ? 35.831 41.128 22.514 1.00 35.57 ? 84 PRO A O 1 ATOM 657 C CB . PRO A 1 84 ? 34.655 41.351 25.645 1.00 36.33 ? 84 PRO A CB 1 ATOM 658 C CG . PRO A 1 84 ? 34.202 40.491 26.781 1.00 36.00 ? 84 PRO A CG 1 ATOM 659 C CD . PRO A 1 84 ? 35.410 39.606 26.992 1.00 35.88 ? 84 PRO A CD 1 ATOM 660 N N . ASN A 1 85 ? 37.421 41.260 24.088 1.00 36.95 ? 85 ASN A N 1 ATOM 661 C CA . ASN A 1 85 ? 38.375 41.860 23.166 1.00 38.01 ? 85 ASN A CA 1 ATOM 662 C C . ASN A 1 85 ? 38.786 40.888 22.064 1.00 37.94 ? 85 ASN A C 1 ATOM 663 O O . ASN A 1 85 ? 38.902 41.278 20.899 1.00 38.00 ? 85 ASN A O 1 ATOM 664 C CB . ASN A 1 85 ? 39.611 42.376 23.920 1.00 40.52 ? 85 ASN A CB 1 ATOM 665 C CG . ASN A 1 85 ? 40.321 41.291 24.708 1.00 42.99 ? 85 ASN A CG 1 ATOM 666 O OD1 . ASN A 1 85 ? 39.739 40.664 25.594 1.00 44.79 ? 85 ASN A OD1 1 ATOM 667 N ND2 . ASN A 1 85 ? 41.594 41.071 24.392 1.00 44.55 ? 85 ASN A ND2 1 ATOM 668 N N . LYS A 1 86 ? 38.998 39.626 22.430 1.00 35.43 ? 86 LYS A N 1 ATOM 669 C CA . LYS A 1 86 ? 39.386 38.609 21.455 1.00 34.59 ? 86 LYS A CA 1 ATOM 670 C C . LYS A 1 86 ? 38.224 38.278 20.518 1.00 32.49 ? 86 LYS A C 1 ATOM 671 O O . LYS A 1 86 ? 38.434 37.982 19.344 1.00 32.10 ? 86 LYS A O 1 ATOM 672 C CB . LYS A 1 86 ? 39.861 37.344 22.170 1.00 35.31 ? 86 LYS A CB 1 ATOM 673 C CG . LYS A 1 86 ? 41.134 37.535 22.988 1.00 38.83 ? 86 LYS A CG 1 ATOM 674 C CD . LYS A 1 86 ? 41.517 36.261 23.741 1.00 40.23 ? 86 LYS A CD 1 ATOM 675 C CE . LYS A 1 86 ? 40.427 35.842 24.725 1.00 41.58 ? 86 LYS A CE 1 ATOM 676 N NZ . LYS A 1 86 ? 40.759 34.582 25.447 1.00 38.67 ? 86 LYS A NZ 1 ATOM 677 N N . VAL A 1 87 ? 37.000 38.325 21.036 1.00 31.43 ? 87 VAL A N 1 ATOM 678 C CA . VAL A 1 87 ? 35.827 38.059 20.214 1.00 31.55 ? 87 VAL A CA 1 ATOM 679 C C . VAL A 1 87 ? 35.808 39.092 19.092 1.00 32.48 ? 87 VAL A C 1 ATOM 680 O O . VAL A 1 87 ? 35.587 38.764 17.925 1.00 30.53 ? 87 VAL A O 1 ATOM 681 C CB . VAL A 1 87 ? 34.510 38.182 21.030 1.00 31.10 ? 87 VAL A CB 1 ATOM 682 C CG1 . VAL A 1 87 ? 33.312 37.965 20.120 1.00 28.76 ? 87 VAL A CG1 1 ATOM 683 C CG2 . VAL A 1 87 ? 34.496 37.169 22.160 1.00 31.45 ? 87 VAL A CG2 1 ATOM 684 N N . ALA A 1 88 ? 36.056 40.346 19.456 1.00 33.41 ? 88 ALA A N 1 ATOM 685 C CA . ALA A 1 88 ? 36.075 41.435 18.489 1.00 32.82 ? 88 ALA A CA 1 ATOM 686 C C . ALA A 1 88 ? 37.178 41.212 17.454 1.00 33.20 ? 88 ALA A C 1 ATOM 687 O O . ALA A 1 88 ? 36.959 41.375 16.255 1.00 32.59 ? 88 ALA A O 1 ATOM 688 C CB . ALA A 1 88 ? 36.285 42.767 19.213 1.00 33.98 ? 88 ALA A CB 1 ATOM 689 N N . GLU A 1 89 ? 38.364 40.839 17.923 1.00 33.50 ? 89 GLU A N 1 ATOM 690 C CA . GLU A 1 89 ? 39.490 40.588 17.029 1.00 35.73 ? 89 GLU A CA 1 ATOM 691 C C . GLU A 1 89 ? 39.119 39.495 16.021 1.00 36.18 ? 89 GLU A C 1 ATOM 692 O O . GLU A 1 89 ? 39.332 39.650 14.819 1.00 34.97 ? 89 GLU A O 1 ATOM 693 C CB . GLU A 1 89 ? 40.717 40.148 17.835 1.00 37.91 ? 89 GLU A CB 1 ATOM 694 C CG . GLU A 1 89 ? 41.992 40.037 17.012 1.00 41.83 ? 89 GLU A CG 1 ATOM 695 C CD . GLU A 1 89 ? 43.132 39.397 17.781 1.00 44.86 ? 89 GLU A CD 1 ATOM 696 O OE1 . GLU A 1 89 ? 43.399 39.827 18.924 1.00 46.54 ? 89 GLU A OE1 1 ATOM 697 O OE2 . GLU A 1 89 ? 43.769 38.467 17.239 1.00 47.86 ? 89 GLU A OE2 1 ATOM 698 N N . MET A 1 90 ? 38.567 38.391 16.523 1.00 35.57 ? 90 MET A N 1 ATOM 699 C CA . MET A 1 90 ? 38.159 37.273 15.672 1.00 34.09 ? 90 MET A CA 1 ATOM 700 C C . MET A 1 90 ? 37.141 37.727 14.639 1.00 33.35 ? 90 MET A C 1 ATOM 701 O O . MET A 1 90 ? 37.290 37.459 13.445 1.00 32.50 ? 90 MET A O 1 ATOM 702 C CB . MET A 1 90 ? 37.544 36.152 16.516 1.00 34.09 ? 90 MET A CB 1 ATOM 703 C CG . MET A 1 90 ? 36.837 35.072 15.695 1.00 32.88 ? 90 MET A CG 1 ATOM 704 S SD . MET A 1 90 ? 35.856 33.977 16.734 1.00 35.50 ? 90 MET A SD 1 ATOM 705 C CE . MET A 1 90 ? 34.384 34.984 16.986 1.00 36.25 ? 90 MET A CE 1 ATOM 706 N N . ILE A 1 91 ? 36.096 38.399 15.109 1.00 33.11 ? 91 ILE A N 1 ATOM 707 C CA . ILE A 1 91 ? 35.052 38.898 14.226 1.00 35.23 ? 91 ILE A CA 1 ATOM 708 C C . ILE A 1 91 ? 35.677 39.806 13.179 1.00 35.48 ? 91 ILE A C 1 ATOM 709 O O . ILE A 1 91 ? 35.290 39.786 12.012 1.00 35.65 ? 91 ILE A O 1 ATOM 710 C CB . ILE A 1 91 ? 33.986 39.709 14.998 1.00 35.73 ? 91 ILE A CB 1 ATOM 711 C CG1 . ILE A 1 91 ? 33.237 38.798 15.975 1.00 36.61 ? 91 ILE A CG1 1 ATOM 712 C CG2 . ILE A 1 91 ? 33.022 40.370 14.015 1.00 35.48 ? 91 ILE A CG2 1 ATOM 713 C CD1 . ILE A 1 91 ? 32.534 37.627 15.313 1.00 36.88 ? 91 ILE A CD1 1 ATOM 714 N N . GLU A 1 92 ? 36.651 40.598 13.610 1.00 37.20 ? 92 GLU A N 1 ATOM 715 C CA . GLU A 1 92 ? 37.337 41.521 12.718 1.00 38.83 ? 92 GLU A CA 1 ATOM 716 C C . GLU A 1 92 ? 38.112 40.758 11.649 1.00 36.82 ? 92 GLU A C 1 ATOM 717 O O . GLU A 1 92 ? 38.160 41.171 10.492 1.00 35.81 ? 92 GLU A O 1 ATOM 718 C CB . GLU A 1 92 ? 38.278 42.413 13.528 1.00 41.97 ? 92 GLU A CB 1 ATOM 719 C CG . GLU A 1 92 ? 38.928 43.529 12.735 1.00 47.41 ? 92 GLU A CG 1 ATOM 720 C CD . GLU A 1 92 ? 39.451 44.634 13.629 1.00 49.78 ? 92 GLU A CD 1 ATOM 721 O OE1 . GLU A 1 92 ? 38.625 45.279 14.310 1.00 51.73 ? 92 GLU A OE1 1 ATOM 722 O OE2 . GLU A 1 92 ? 40.680 44.858 13.657 1.00 51.90 ? 92 GLU A OE2 1 ATOM 723 N N . ASN A 1 93 ? 38.713 39.638 12.039 1.00 35.34 ? 93 ASN A N 1 ATOM 724 C CA . ASN A 1 93 ? 39.466 38.819 11.096 1.00 32.90 ? 93 ASN A CA 1 ATOM 725 C C . ASN A 1 93 ? 38.558 37.825 10.381 1.00 32.00 ? 93 ASN A C 1 ATOM 726 O O . ASN A 1 93 ? 38.918 36.662 10.204 1.00 30.21 ? 93 ASN A O 1 ATOM 727 C CB . ASN A 1 93 ? 40.586 38.064 11.814 1.00 33.71 ? 93 ASN A CB 1 ATOM 728 C CG . ASN A 1 93 ? 41.631 38.990 12.389 1.00 35.22 ? 93 ASN A CG 1 ATOM 729 O OD1 . ASN A 1 93 ? 42.101 39.905 11.715 1.00 35.94 ? 93 ASN A OD1 1 ATOM 730 N ND2 . ASN A 1 93 ? 42.011 38.753 13.634 1.00 35.10 ? 93 ASN A ND2 1 ATOM 731 N N . GLN A 1 94 ? 37.376 38.291 9.986 1.00 29.98 ? 94 GLN A N 1 ATOM 732 C CA . GLN A 1 94 ? 36.407 37.467 9.268 1.00 31.57 ? 94 GLN A CA 1 ATOM 733 C C . GLN A 1 94 ? 35.957 36.206 10.022 1.00 31.08 ? 94 GLN A C 1 ATOM 734 O O . GLN A 1 94 ? 35.611 35.197 9.400 1.00 30.74 ? 94 GLN A O 1 ATOM 735 C CB . GLN A 1 94 ? 36.983 37.058 7.908 1.00 33.39 ? 94 GLN A CB 1 ATOM 736 C CG . GLN A 1 94 ? 37.626 38.191 7.115 1.00 34.60 ? 94 GLN A CG 1 ATOM 737 C CD . GLN A 1 94 ? 36.721 39.401 6.961 1.00 36.43 ? 94 GLN A CD 1 ATOM 738 O OE1 . GLN A 1 94 ? 36.576 40.205 7.879 1.00 38.50 ? 94 GLN A OE1 1 ATOM 739 N NE2 . GLN A 1 94 ? 36.103 39.529 5.798 1.00 38.88 ? 94 GLN A NE2 1 ATOM 740 N N . GLY A 1 95 ? 35.962 36.270 11.350 1.00 29.81 ? 95 GLY A N 1 ATOM 741 C CA . GLY A 1 95 ? 35.553 35.135 12.163 1.00 28.83 ? 95 GLY A CA 1 ATOM 742 C C . GLY A 1 95 ? 36.567 34.003 12.144 1.00 29.50 ? 95 GLY A C 1 ATOM 743 O O . GLY A 1 95 ? 36.199 32.830 12.237 1.00 29.44 ? 95 GLY A O 1 ATOM 744 N N . LEU A 1 96 ? 37.846 34.358 12.044 1.00 28.23 ? 96 LEU A N 1 ATOM 745 C CA . LEU A 1 96 ? 38.919 33.375 11.988 1.00 28.43 ? 96 LEU A CA 1 ATOM 746 C C . LEU A 1 96 ? 40.031 33.575 13.013 1.00 28.91 ? 96 LEU A C 1 ATOM 747 O O . LEU A 1 96 ? 40.226 34.676 13.530 1.00 26.11 ? 96 LEU A O 1 ATOM 748 C CB . LEU A 1 96 ? 39.532 33.387 10.592 1.00 30.37 ? 96 LEU A CB 1 ATOM 749 C CG . LEU A 1 96 ? 38.589 32.962 9.469 1.00 30.84 ? 96 LEU A CG 1 ATOM 750 C CD1 . LEU A 1 96 ? 39.194 33.311 8.127 1.00 34.72 ? 96 LEU A CD1 1 ATOM 751 C CD2 . LEU A 1 96 ? 38.324 31.473 9.577 1.00 32.43 ? 96 LEU A CD2 1 ATOM 752 N N . PHE A 1 97 ? 40.747 32.488 13.298 1.00 30.72 ? 97 PHE A N 1 ATOM 753 C CA . PHE A 1 97 ? 41.887 32.488 14.218 1.00 30.84 ? 97 PHE A CA 1 ATOM 754 C C . PHE A 1 97 ? 43.086 32.194 13.321 1.00 32.15 ? 97 PHE A C 1 ATOM 755 O O . PHE A 1 97 ? 43.454 31.037 13.121 1.00 32.83 ? 97 PHE A O 1 ATOM 756 C CB . PHE A 1 97 ? 41.764 31.373 15.260 1.00 30.14 ? 97 PHE A CB 1 ATOM 757 C CG . PHE A 1 97 ? 40.611 31.536 16.205 1.00 29.22 ? 97 PHE A CG 1 ATOM 758 C CD1 . PHE A 1 97 ? 40.536 32.636 17.053 1.00 30.29 ? 97 PHE A CD1 1 ATOM 759 C CD2 . PHE A 1 97 ? 39.611 30.571 16.269 1.00 28.85 ? 97 PHE A CD2 1 ATOM 760 C CE1 . PHE A 1 97 ? 39.479 32.773 17.957 1.00 30.19 ? 97 PHE A CE1 1 ATOM 761 C CE2 . PHE A 1 97 ? 38.552 30.695 17.166 1.00 30.52 ? 97 PHE A CE2 1 ATOM 762 C CZ . PHE A 1 97 ? 38.487 31.802 18.015 1.00 29.36 ? 97 PHE A CZ 1 ATOM 763 N N . LYS A 1 98 ? 43.689 33.249 12.788 1.00 33.47 ? 98 LYS A N 1 ATOM 764 C CA . LYS A 1 98 ? 44.815 33.127 11.869 1.00 35.64 ? 98 LYS A CA 1 ATOM 765 C C . LYS A 1 98 ? 45.921 32.131 12.207 1.00 34.96 ? 98 LYS A C 1 ATOM 766 O O . LYS A 1 98 ? 46.340 31.358 11.349 1.00 35.84 ? 98 LYS A O 1 ATOM 767 C CB . LYS A 1 98 ? 45.448 34.502 11.641 1.00 39.05 ? 98 LYS A CB 1 ATOM 768 C CG . LYS A 1 98 ? 46.556 34.498 10.597 1.00 42.98 ? 98 LYS A CG 1 ATOM 769 C CD . LYS A 1 98 ? 47.094 35.900 10.347 1.00 46.11 ? 98 LYS A CD 1 ATOM 770 C CE . LYS A 1 98 ? 48.195 35.887 9.299 1.00 47.14 ? 98 LYS A CE 1 ATOM 771 N NZ . LYS A 1 98 ? 49.329 35.015 9.715 1.00 49.65 ? 98 LYS A NZ 1 ATOM 772 N N . ASP A 1 99 ? 46.387 32.137 13.450 1.00 33.88 ? 99 ASP A N 1 ATOM 773 C CA . ASP A 1 99 ? 47.488 31.263 13.839 1.00 33.51 ? 99 ASP A CA 1 ATOM 774 C C . ASP A 1 99 ? 47.164 29.835 14.266 1.00 31.63 ? 99 ASP A C 1 ATOM 775 O O . ASP A 1 99 ? 48.068 29.096 14.656 1.00 31.33 ? 99 ASP A O 1 ATOM 776 C CB . ASP A 1 99 ? 48.301 31.936 14.950 1.00 37.13 ? 99 ASP A CB 1 ATOM 777 C CG . ASP A 1 99 ? 48.777 33.327 14.563 1.00 40.45 ? 99 ASP A CG 1 ATOM 778 O OD1 . ASP A 1 99 ? 49.335 33.482 13.452 1.00 42.89 ? 99 ASP A OD1 1 ATOM 779 O OD2 . ASP A 1 99 ? 48.597 34.262 15.371 1.00 41.62 ? 99 ASP A OD2 1 ATOM 780 N N . HIS A 1 100 ? 45.901 29.430 14.183 1.00 29.10 ? 100 HIS A N 1 ATOM 781 C CA . HIS A 1 100 ? 45.536 28.083 14.609 1.00 27.59 ? 100 HIS A CA 1 ATOM 782 C C . HIS A 1 100 ? 44.725 27.244 13.623 1.00 25.40 ? 100 HIS A C 1 ATOM 783 O O . HIS A 1 100 ? 44.268 26.160 13.975 1.00 25.10 ? 100 HIS A O 1 ATOM 784 C CB . HIS A 1 100 ? 44.768 28.160 15.933 1.00 28.68 ? 100 HIS A CB 1 ATOM 785 C CG . HIS A 1 100 ? 45.576 28.695 17.075 1.00 29.13 ? 100 HIS A CG 1 ATOM 786 N ND1 . HIS A 1 100 ? 46.619 27.995 17.641 1.00 30.28 ? 100 HIS A ND1 1 ATOM 787 C CD2 . HIS A 1 100 ? 45.496 29.864 17.753 1.00 29.69 ? 100 HIS A CD2 1 ATOM 788 C CE1 . HIS A 1 100 ? 47.147 28.709 18.619 1.00 30.63 ? 100 HIS A CE1 1 ATOM 789 N NE2 . HIS A 1 100 ? 46.484 29.848 18.709 1.00 31.30 ? 100 HIS A NE2 1 ATOM 790 N N . VAL A 1 101 ? 44.558 27.713 12.393 1.00 23.98 ? 101 VAL A N 1 ATOM 791 C CA . VAL A 1 101 ? 43.759 26.971 11.424 1.00 22.42 ? 101 VAL A CA 1 ATOM 792 C C . VAL A 1 101 ? 44.153 25.512 11.177 1.00 22.44 ? 101 VAL A C 1 ATOM 793 O O . VAL A 1 101 ? 43.325 24.719 10.742 1.00 21.97 ? 101 VAL A O 1 ATOM 794 C CB . VAL A 1 101 ? 43.686 27.720 10.070 1.00 22.08 ? 101 VAL A CB 1 ATOM 795 C CG1 . VAL A 1 101 ? 43.038 29.082 10.281 1.00 22.18 ? 101 VAL A CG1 1 ATOM 796 C CG2 . VAL A 1 101 ? 45.077 27.862 9.456 1.00 22.17 ? 101 VAL A CG2 1 ATOM 797 N N . GLU A 1 102 ? 45.403 25.150 11.456 1.00 24.23 ? 102 GLU A N 1 ATOM 798 C CA . GLU A 1 102 ? 45.859 23.772 11.258 1.00 22.58 ? 102 GLU A CA 1 ATOM 799 C C . GLU A 1 102 ? 46.260 23.137 12.593 1.00 24.22 ? 102 GLU A C 1 ATOM 800 O O . GLU A 1 102 ? 46.838 22.050 12.633 1.00 24.09 ? 102 GLU A O 1 ATOM 801 C CB . GLU A 1 102 ? 47.051 23.738 10.293 1.00 24.97 ? 102 GLU A CB 1 ATOM 802 C CG . GLU A 1 102 ? 46.770 24.352 8.927 1.00 24.06 ? 102 GLU A CG 1 ATOM 803 C CD . GLU A 1 102 ? 47.999 24.377 8.031 1.00 24.50 ? 102 GLU A CD 1 ATOM 804 O OE1 . GLU A 1 102 ? 48.427 23.304 7.560 1.00 27.94 ? 102 GLU A OE1 1 ATOM 805 O OE2 . GLU A 1 102 ? 48.544 25.473 7.803 1.00 24.45 ? 102 GLU A OE2 1 ATOM 806 N N . ASP A 1 103 ? 45.943 23.821 13.685 1.00 21.79 ? 103 ASP A N 1 ATOM 807 C CA . ASP A 1 103 ? 46.272 23.335 15.019 1.00 20.95 ? 103 ASP A CA 1 ATOM 808 C C . ASP A 1 103 ? 45.168 22.438 15.580 1.00 20.87 ? 103 ASP A C 1 ATOM 809 O O . ASP A 1 103 ? 44.147 22.923 16.076 1.00 21.27 ? 103 ASP A O 1 ATOM 810 C CB . ASP A 1 103 ? 46.501 24.529 15.943 1.00 21.06 ? 103 ASP A CB 1 ATOM 811 C CG . ASP A 1 103 ? 46.908 24.118 17.336 1.00 21.76 ? 103 ASP A CG 1 ATOM 812 O OD1 . ASP A 1 103 ? 47.244 22.933 17.538 1.00 24.64 ? 103 ASP A OD1 1 ATOM 813 O OD2 . ASP A 1 103 ? 46.899 24.990 18.227 1.00 26.32 ? 103 ASP A OD2 1 ATOM 814 N N . VAL A 1 104 ? 45.382 21.128 15.517 1.00 19.37 ? 104 VAL A N 1 ATOM 815 C CA . VAL A 1 104 ? 44.389 20.182 16.002 1.00 19.56 ? 104 VAL A CA 1 ATOM 816 C C . VAL A 1 104 ? 44.254 20.174 17.520 1.00 19.84 ? 104 VAL A C 1 ATOM 817 O O . VAL A 1 104 ? 43.287 19.634 18.059 1.00 21.38 ? 104 VAL A O 1 ATOM 818 C CB . VAL A 1 104 ? 44.684 18.747 15.478 1.00 19.70 ? 104 VAL A CB 1 ATOM 819 C CG1 . VAL A 1 104 ? 44.787 18.776 13.946 1.00 20.04 ? 104 VAL A CG1 1 ATOM 820 C CG2 . VAL A 1 104 ? 45.980 18.201 16.081 1.00 19.55 ? 104 VAL A CG2 1 ATOM 821 N N . ASN A 1 105 ? 45.210 20.791 18.209 1.00 21.01 ? 105 ASN A N 1 ATOM 822 C CA . ASN A 1 105 ? 45.174 20.852 19.671 1.00 21.91 ? 105 ASN A CA 1 ATOM 823 C C . ASN A 1 105 ? 44.602 22.162 20.213 1.00 21.54 ? 105 ASN A C 1 ATOM 824 O O . ASN A 1 105 ? 44.542 22.367 21.425 1.00 20.77 ? 105 ASN A O 1 ATOM 825 C CB . ASN A 1 105 ? 46.572 20.618 20.264 1.00 24.93 ? 105 ASN A CB 1 ATOM 826 C CG . ASN A 1 105 ? 46.852 19.149 20.544 1.00 28.10 ? 105 ASN A CG 1 ATOM 827 O OD1 . ASN A 1 105 ? 47.814 18.811 21.235 1.00 33.27 ? 105 ASN A OD1 1 ATOM 828 N ND2 . ASN A 1 105 ? 46.016 18.271 20.006 1.00 29.03 ? 105 ASN A ND2 1 ATOM 829 N N . PHE A 1 106 ? 44.190 23.055 19.320 1.00 20.08 ? 106 PHE A N 1 ATOM 830 C CA . PHE A 1 106 ? 43.591 24.309 19.744 1.00 21.01 ? 106 PHE A CA 1 ATOM 831 C C . PHE A 1 106 ? 42.290 23.935 20.442 1.00 21.12 ? 106 PHE A C 1 ATOM 832 O O . PHE A 1 106 ? 41.438 23.274 19.854 1.00 23.05 ? 106 PHE A O 1 ATOM 833 C CB . PHE A 1 106 ? 43.297 25.192 18.530 1.00 23.03 ? 106 PHE A CB 1 ATOM 834 C CG . PHE A 1 106 ? 42.666 26.512 18.872 1.00 24.63 ? 106 PHE A CG 1 ATOM 835 C CD1 . PHE A 1 106 ? 43.357 27.454 19.629 1.00 25.69 ? 106 PHE A CD1 1 ATOM 836 C CD2 . PHE A 1 106 ? 41.386 26.821 18.425 1.00 25.56 ? 106 PHE A CD2 1 ATOM 837 C CE1 . PHE A 1 106 ? 42.784 28.683 19.932 1.00 28.52 ? 106 PHE A CE1 1 ATOM 838 C CE2 . PHE A 1 106 ? 40.802 28.047 18.722 1.00 28.13 ? 106 PHE A CE2 1 ATOM 839 C CZ . PHE A 1 106 ? 41.502 28.982 19.477 1.00 28.84 ? 106 PHE A CZ 1 ATOM 840 N N . GLN A 1 107 ? 42.135 24.342 21.697 1.00 21.88 ? 107 GLN A N 1 ATOM 841 C CA . GLN A 1 107 ? 40.928 24.014 22.445 1.00 21.85 ? 107 GLN A CA 1 ATOM 842 C C . GLN A 1 107 ? 39.778 24.952 22.115 1.00 21.69 ? 107 GLN A C 1 ATOM 843 O O . GLN A 1 107 ? 39.983 26.138 21.888 1.00 20.72 ? 107 GLN A O 1 ATOM 844 C CB . GLN A 1 107 ? 41.201 24.054 23.953 1.00 25.83 ? 107 GLN A CB 1 ATOM 845 C CG . GLN A 1 107 ? 42.185 22.997 24.445 1.00 28.15 ? 107 GLN A CG 1 ATOM 846 C CD . GLN A 1 107 ? 41.755 21.589 24.079 1.00 31.56 ? 107 GLN A CD 1 ATOM 847 O OE1 . GLN A 1 107 ? 40.644 21.162 24.400 1.00 33.35 ? 107 GLN A OE1 1 ATOM 848 N NE2 . GLN A 1 107 ? 42.636 20.859 23.404 1.00 32.61 ? 107 GLN A NE2 1 ATOM 849 N N . PRO A 1 108 ? 38.544 24.422 22.079 1.00 21.54 ? 108 PRO A N 1 ATOM 850 C CA . PRO A 1 108 ? 37.365 25.234 21.775 1.00 22.05 ? 108 PRO A CA 1 ATOM 851 C C . PRO A 1 108 ? 37.168 26.290 22.856 1.00 21.38 ? 108 PRO A C 1 ATOM 852 O O . PRO A 1 108 ? 37.507 26.071 24.015 1.00 21.34 ? 108 PRO A O 1 ATOM 853 C CB . PRO A 1 108 ? 36.226 24.213 21.780 1.00 20.00 ? 108 PRO A CB 1 ATOM 854 C CG . PRO A 1 108 ? 36.905 22.927 21.442 1.00 22.30 ? 108 PRO A CG 1 ATOM 855 C CD . PRO A 1 108 ? 38.169 23.010 22.250 1.00 22.74 ? 108 PRO A CD 1 ATOM 856 N N . VAL A 1 109 ? 36.626 27.434 22.471 1.00 22.12 ? 109 VAL A N 1 ATOM 857 C CA . VAL A 1 109 ? 36.368 28.503 23.421 1.00 22.47 ? 109 VAL A CA 1 ATOM 858 C C . VAL A 1 109 ? 34.920 28.950 23.251 1.00 24.24 ? 109 VAL A C 1 ATOM 859 O O . VAL A 1 109 ? 34.312 28.720 22.206 1.00 23.32 ? 109 VAL A O 1 ATOM 860 C CB . VAL A 1 109 ? 37.321 29.692 23.196 1.00 21.32 ? 109 VAL A CB 1 ATOM 861 C CG1 . VAL A 1 109 ? 38.758 29.260 23.488 1.00 19.10 ? 109 VAL A CG1 1 ATOM 862 C CG2 . VAL A 1 109 ? 37.200 30.197 21.766 1.00 18.68 ? 109 VAL A CG2 1 ATOM 863 N N . LYS A 1 110 ? 34.367 29.572 24.286 1.00 24.75 ? 110 LYS A N 1 ATOM 864 C CA . LYS A 1 110 ? 32.984 30.027 24.254 1.00 26.28 ? 110 LYS A CA 1 ATOM 865 C C . LYS A 1 110 ? 32.881 31.534 24.457 1.00 26.55 ? 110 LYS A C 1 ATOM 866 O O . LYS A 1 110 ? 33.825 32.175 24.917 1.00 24.64 ? 110 LYS A O 1 ATOM 867 C CB . LYS A 1 110 ? 32.187 29.337 25.359 1.00 27.41 ? 110 LYS A CB 1 ATOM 868 C CG . LYS A 1 110 ? 32.618 29.772 26.753 1.00 27.80 ? 110 LYS A CG 1 ATOM 869 C CD . LYS A 1 110 ? 31.844 29.058 27.832 1.00 31.68 ? 110 LYS A CD 1 ATOM 870 C CE . LYS A 1 110 ? 32.383 29.413 29.205 1.00 33.95 ? 110 LYS A CE 1 ATOM 871 N NZ . LYS A 1 110 ? 31.791 28.544 30.258 1.00 39.09 ? 110 LYS A NZ 1 ATOM 872 N N . TYR A 1 111 ? 31.719 32.081 24.114 1.00 28.40 ? 111 TYR A N 1 ATOM 873 C CA . TYR A 1 111 ? 31.438 33.505 24.271 1.00 31.13 ? 111 TYR A CA 1 ATOM 874 C C . TYR A 1 111 ? 29.960 33.764 23.994 1.00 33.79 ? 111 TYR A C 1 ATOM 875 O O . TYR A 1 111 ? 29.332 33.051 23.211 1.00 31.85 ? 111 TYR A O 1 ATOM 876 C CB . TYR A 1 111 ? 32.324 34.346 23.338 1.00 29.13 ? 111 TYR A CB 1 ATOM 877 C CG . TYR A 1 111 ? 32.050 34.192 21.855 1.00 28.50 ? 111 TYR A CG 1 ATOM 878 C CD1 . TYR A 1 111 ? 31.041 34.922 21.228 1.00 27.03 ? 111 TYR A CD1 1 ATOM 879 C CD2 . TYR A 1 111 ? 32.814 33.326 21.076 1.00 28.38 ? 111 TYR A CD2 1 ATOM 880 C CE1 . TYR A 1 111 ? 30.802 34.794 19.864 1.00 26.14 ? 111 TYR A CE1 1 ATOM 881 C CE2 . TYR A 1 111 ? 32.583 33.187 19.714 1.00 26.85 ? 111 TYR A CE2 1 ATOM 882 C CZ . TYR A 1 111 ? 31.578 33.922 19.114 1.00 27.64 ? 111 TYR A CZ 1 ATOM 883 O OH . TYR A 1 111 ? 31.342 33.766 17.769 1.00 27.72 ? 111 TYR A OH 1 ATOM 884 N N . SER A 1 112 ? 29.408 34.775 24.656 1.00 38.13 ? 112 SER A N 1 ATOM 885 C CA . SER A 1 112 ? 28.004 35.130 24.492 1.00 42.77 ? 112 SER A CA 1 ATOM 886 C C . SER A 1 112 ? 27.781 35.946 23.230 1.00 45.36 ? 112 SER A C 1 ATOM 887 O O . SER A 1 112 ? 28.313 37.047 23.090 1.00 47.50 ? 112 SER A O 1 ATOM 888 C CB . SER A 1 112 ? 27.514 35.921 25.705 1.00 42.81 ? 112 SER A CB 1 ATOM 889 O OG . SER A 1 112 ? 27.537 35.116 26.871 1.00 45.90 ? 112 SER A OG 1 ATOM 890 N N . ALA A 1 113 ? 26.987 35.399 22.316 1.00 47.86 ? 113 ALA A N 1 ATOM 891 C CA . ALA A 1 113 ? 26.688 36.069 21.058 1.00 49.45 ? 113 ALA A CA 1 ATOM 892 C C . ALA A 1 113 ? 25.368 36.826 21.155 1.00 50.27 ? 113 ALA A C 1 ATOM 893 O O . ALA A 1 113 ? 24.705 36.808 22.193 1.00 51.68 ? 113 ALA A O 1 ATOM 894 C CB . ALA A 1 113 ? 26.629 35.043 19.922 1.00 49.49 ? 113 ALA A CB 1 ATOM 895 N N . GLU A 1 119 ? 17.059 36.895 23.201 1.00 62.70 ? 119 GLU A N 1 ATOM 896 C CA . GLU A 1 119 ? 17.567 35.980 24.217 1.00 61.88 ? 119 GLU A CA 1 ATOM 897 C C . GLU A 1 119 ? 19.054 35.712 24.007 1.00 60.47 ? 119 GLU A C 1 ATOM 898 O O . GLU A 1 119 ? 19.566 35.849 22.897 1.00 59.89 ? 119 GLU A O 1 ATOM 899 C CB . GLU A 1 119 ? 16.778 34.666 24.193 1.00 63.98 ? 119 GLU A CB 1 ATOM 900 C CG . GLU A 1 119 ? 16.030 34.392 22.894 1.00 65.78 ? 119 GLU A CG 1 ATOM 901 C CD . GLU A 1 119 ? 16.933 34.426 21.677 1.00 67.92 ? 119 GLU A CD 1 ATOM 902 O OE1 . GLU A 1 119 ? 17.946 33.693 21.662 1.00 70.21 ? 119 GLU A OE1 1 ATOM 903 O OE2 . GLU A 1 119 ? 16.627 35.184 20.732 1.00 68.60 ? 119 GLU A OE2 1 ATOM 904 N N . GLU A 1 120 ? 19.742 35.325 25.077 1.00 59.33 ? 120 GLU A N 1 ATOM 905 C CA . GLU A 1 120 ? 21.178 35.072 25.010 1.00 58.67 ? 120 GLU A CA 1 ATOM 906 C C . GLU A 1 120 ? 21.569 33.858 24.174 1.00 56.73 ? 120 GLU A C 1 ATOM 907 O O . GLU A 1 120 ? 20.845 32.864 24.108 1.00 56.81 ? 120 GLU A O 1 ATOM 908 C CB . GLU A 1 120 ? 21.760 34.915 26.417 1.00 59.87 ? 120 GLU A CB 1 ATOM 909 C CG . GLU A 1 120 ? 21.475 33.570 27.067 1.00 62.50 ? 120 GLU A CG 1 ATOM 910 C CD . GLU A 1 120 ? 22.159 33.424 28.412 1.00 64.50 ? 120 GLU A CD 1 ATOM 911 O OE1 . GLU A 1 120 ? 23.390 33.637 28.475 1.00 65.37 ? 120 GLU A OE1 1 ATOM 912 O OE2 . GLU A 1 120 ? 21.470 33.093 29.403 1.00 65.57 ? 120 GLU A OE2 1 HETATM 913 N N . CME A 1 121 ? 22.681 33.432 23.934 1.00 53.95 ? 121 CME A N 1 HETATM 914 C CA . CME A 1 121 ? 23.138 32.366 23.055 1.00 50.85 ? 121 CME A CA 1 HETATM 915 C CB . CME A 1 121 ? 22.518 32.503 21.668 1.00 49.18 ? 121 CME A CB 1 HETATM 916 S SG . CME A 1 121 ? 23.094 31.225 20.506 1.00 45.22 ? 121 CME A SG 1 HETATM 917 S SD . CME A 1 121 ? 21.606 29.848 20.552 1.00 45.67 ? 121 CME A SD 1 HETATM 918 C CE . CME A 1 121 ? 20.406 30.456 19.325 1.00 46.46 ? 121 CME A CE 1 HETATM 919 C CZ . CME A 1 121 ? 20.908 30.297 17.904 1.00 48.56 ? 121 CME A CZ 1 HETATM 920 O OH . CME A 1 121 ? 20.186 30.881 17.031 1.00 49.17 ? 121 CME A OH 1 HETATM 921 C C . CME A 1 121 ? 24.653 32.431 22.930 1.00 50.21 ? 121 CME A C 1 HETATM 922 O O . CME A 1 121 ? 25.260 33.455 23.226 1.00 48.74 ? 121 CME A O 1 ATOM 923 N N . THR A 1 122 ? 24.983 30.976 23.355 1.00 25.24 ? 122 THR A N 1 ATOM 924 C CA . THR A 1 122 ? 26.408 30.759 23.623 1.00 25.22 ? 122 THR A CA 1 ATOM 925 C C . THR A 1 122 ? 27.044 30.122 22.400 1.00 25.36 ? 122 THR A C 1 ATOM 926 O O . THR A 1 122 ? 26.585 29.126 21.868 1.00 25.93 ? 122 THR A O 1 ATOM 927 C CB . THR A 1 122 ? 26.586 29.833 24.822 1.00 26.13 ? 122 THR A CB 1 ATOM 928 O OG1 . THR A 1 122 ? 25.914 30.377 25.958 1.00 28.26 ? 122 THR A OG1 1 ATOM 929 C CG2 . THR A 1 122 ? 28.061 29.644 25.175 1.00 25.41 ? 122 THR A CG2 1 ATOM 930 N N . ALA A 1 123 ? 28.080 30.673 21.929 1.00 24.88 ? 123 ALA A N 1 ATOM 931 C CA . ALA A 1 123 ? 28.729 30.131 20.746 1.00 24.45 ? 123 ALA A CA 1 ATOM 932 C C . ALA A 1 123 ? 30.019 29.431 21.142 1.00 23.77 ? 123 ALA A C 1 ATOM 933 O O . ALA A 1 123 ? 30.781 29.930 21.976 1.00 23.99 ? 123 ALA A O 1 ATOM 934 C CB . ALA A 1 123 ? 29.032 31.257 19.769 1.00 24.95 ? 123 ALA A CB 1 ATOM 935 N N . VAL A 1 124 ? 30.236 28.254 20.571 1.00 21.68 ? 124 VAL A N 1 ATOM 936 C CA . VAL A 1 124 ? 31.440 27.495 20.854 1.00 19.61 ? 124 VAL A CA 1 ATOM 937 C C . VAL A 1 124 ? 32.189 27.336 19.543 1.00 18.74 ? 124 VAL A C 1 ATOM 938 O O . VAL A 1 124 ? 31.662 26.774 18.584 1.00 17.73 ? 124 VAL A O 1 ATOM 939 C CB . VAL A 1 124 ? 31.109 26.108 21.430 1.00 19.97 ? 124 VAL A CB 1 ATOM 940 C CG1 . VAL A 1 124 ? 32.395 25.326 21.672 1.00 20.60 ? 124 VAL A CG1 1 ATOM 941 C CG2 . VAL A 1 124 ? 30.320 26.258 22.722 1.00 21.13 ? 124 VAL A CG2 1 ATOM 942 N N . VAL A 1 125 ? 33.418 27.839 19.505 1.00 17.99 ? 125 VAL A N 1 ATOM 943 C CA . VAL A 1 125 ? 34.227 27.763 18.300 1.00 18.43 ? 125 VAL A CA 1 ATOM 944 C C . VAL A 1 125 ? 35.603 27.175 18.566 1.00 19.12 ? 125 VAL A C 1 ATOM 945 O O . VAL A 1 125 ? 36.102 27.213 19.692 1.00 18.99 ? 125 VAL A O 1 ATOM 946 C CB . VAL A 1 125 ? 34.409 29.162 17.654 1.00 19.68 ? 125 VAL A CB 1 ATOM 947 C CG1 . VAL A 1 125 ? 33.093 29.660 17.099 1.00 16.83 ? 125 VAL A CG1 1 ATOM 948 C CG2 . VAL A 1 125 ? 34.932 30.147 18.685 1.00 18.42 ? 125 VAL A CG2 1 ATOM 949 N N . ALA A 1 126 ? 36.201 26.617 17.517 1.00 19.07 ? 126 ALA A N 1 ATOM 950 C CA . ALA A 1 126 ? 37.529 26.036 17.606 1.00 19.45 ? 126 ALA A CA 1 ATOM 951 C C . ALA A 1 126 ? 38.370 26.561 16.440 1.00 20.32 ? 126 ALA A C 1 ATOM 952 O O . ALA A 1 126 ? 38.141 27.674 15.968 1.00 20.32 ? 126 ALA A O 1 ATOM 953 C CB . ALA A 1 126 ? 37.448 24.519 17.591 1.00 19.13 ? 126 ALA A CB 1 ATOM 954 N N . ARG A 1 127 ? 39.321 25.770 15.955 1.00 19.72 ? 127 ARG A N 1 ATOM 955 C CA . ARG A 1 127 ? 40.199 26.245 14.890 1.00 20.55 ? 127 ARG A CA 1 ATOM 956 C C . ARG A 1 127 ? 39.552 26.748 13.595 1.00 19.36 ? 127 ARG A C 1 ATOM 957 O O . ARG A 1 127 ? 40.183 27.480 12.841 1.00 23.51 ? 127 ARG A O 1 ATOM 958 C CB . ARG A 1 127 ? 41.276 25.195 14.584 1.00 18.75 ? 127 ARG A CB 1 ATOM 959 C CG . ARG A 1 127 ? 40.903 24.038 13.664 1.00 15.59 ? 127 ARG A CG 1 ATOM 960 C CD . ARG A 1 127 ? 42.126 23.119 13.563 1.00 17.15 ? 127 ARG A CD 1 ATOM 961 N NE . ARG A 1 127 ? 42.295 22.455 12.270 1.00 16.85 ? 127 ARG A NE 1 ATOM 962 C CZ . ARG A 1 127 ? 41.918 21.210 12.006 1.00 16.12 ? 127 ARG A CZ 1 ATOM 963 N NH1 . ARG A 1 127 ? 41.335 20.473 12.943 1.00 17.75 ? 127 ARG A NH1 1 ATOM 964 N NH2 . ARG A 1 127 ? 42.145 20.694 10.808 1.00 16.11 ? 127 ARG A NH2 1 ATOM 965 N N . GLY A 1 128 ? 38.302 26.379 13.346 1.00 19.80 ? 128 GLY A N 1 ATOM 966 C CA . GLY A 1 128 ? 37.625 26.832 12.142 1.00 18.10 ? 128 GLY A CA 1 ATOM 967 C C . GLY A 1 128 ? 36.935 28.180 12.300 1.00 20.02 ? 128 GLY A C 1 ATOM 968 O O . GLY A 1 128 ? 36.433 28.755 11.331 1.00 19.46 ? 128 GLY A O 1 ATOM 969 N N . GLY A 1 129 ? 36.903 28.693 13.524 1.00 19.53 ? 129 GLY A N 1 ATOM 970 C CA . GLY A 1 129 ? 36.270 29.977 13.756 1.00 19.31 ? 129 GLY A CA 1 ATOM 971 C C . GLY A 1 129 ? 34.753 29.928 13.709 1.00 18.25 ? 129 GLY A C 1 ATOM 972 O O . GLY A 1 129 ? 34.147 28.856 13.797 1.00 17.58 ? 129 GLY A O 1 ATOM 973 N N . THR A 1 130 ? 34.137 31.095 13.544 1.00 19.08 ? 130 THR A N 1 ATOM 974 C CA . THR A 1 130 ? 32.681 31.202 13.523 1.00 20.39 ? 130 THR A CA 1 ATOM 975 C C . THR A 1 130 ? 31.962 30.329 12.507 1.00 19.67 ? 130 THR A C 1 ATOM 976 O O . THR A 1 130 ? 30.827 29.930 12.735 1.00 20.62 ? 130 THR A O 1 ATOM 977 C CB . THR A 1 130 ? 32.228 32.658 13.294 1.00 19.47 ? 130 THR A CB 1 ATOM 978 O OG1 . THR A 1 130 ? 32.785 33.145 12.066 1.00 21.34 ? 130 THR A OG1 1 ATOM 979 C CG2 . THR A 1 130 ? 32.678 33.539 14.444 1.00 20.90 ? 130 THR A CG2 1 ATOM 980 N N . ALA A 1 131 ? 32.611 30.030 11.390 1.00 19.13 ? 131 ALA A N 1 ATOM 981 C CA . ALA A 1 131 ? 31.968 29.222 10.354 1.00 18.58 ? 131 ALA A CA 1 ATOM 982 C C . ALA A 1 131 ? 31.545 27.821 10.811 1.00 18.42 ? 131 ALA A C 1 ATOM 983 O O . ALA A 1 131 ? 30.598 27.254 10.270 1.00 17.41 ? 131 ALA A O 1 ATOM 984 C CB . ALA A 1 131 ? 32.886 29.123 9.132 1.00 19.73 ? 131 ALA A CB 1 ATOM 985 N N . ASN A 1 132 ? 32.238 27.258 11.799 1.00 17.79 ? 132 ASN A N 1 ATOM 986 C CA . ASN A 1 132 ? 31.900 25.922 12.289 1.00 17.13 ? 132 ASN A CA 1 ATOM 987 C C . ASN A 1 132 ? 31.388 25.969 13.726 1.00 18.59 ? 132 ASN A C 1 ATOM 988 O O . ASN A 1 132 ? 31.398 24.966 14.439 1.00 17.70 ? 132 ASN A O 1 ATOM 989 C CB . ASN A 1 132 ? 33.129 25.013 12.218 1.00 17.92 ? 132 ASN A CB 1 ATOM 990 C CG . ASN A 1 132 ? 33.737 24.964 10.834 1.00 17.42 ? 132 ASN A CG 1 ATOM 991 O OD1 . ASN A 1 132 ? 34.919 25.257 10.655 1.00 18.58 ? 132 ASN A OD1 1 ATOM 992 N ND2 . ASN A 1 132 ? 32.933 24.590 9.845 1.00 15.67 ? 132 ASN A ND2 1 ATOM 993 N N . ALA A 1 133 ? 30.925 27.139 14.141 1.00 18.58 ? 133 ALA A N 1 ATOM 994 C CA . ALA A 1 133 ? 30.440 27.322 15.498 1.00 18.88 ? 133 ALA A CA 1 ATOM 995 C C . ALA A 1 133 ? 29.239 26.457 15.864 1.00 17.68 ? 133 ALA A C 1 ATOM 996 O O . ALA A 1 133 ? 28.389 26.149 15.032 1.00 19.22 ? 133 ALA A O 1 ATOM 997 C CB . ALA A 1 133 ? 30.106 28.805 15.730 1.00 18.10 ? 133 ALA A CB 1 ATOM 998 N N . ILE A 1 134 ? 29.200 26.058 17.128 1.00 19.15 ? 134 ILE A N 1 ATOM 999 C CA . ILE A 1 134 ? 28.101 25.279 17.686 1.00 19.18 ? 134 ILE A CA 1 ATOM 1000 C C . ILE A 1 134 ? 27.415 26.330 18.540 1.00 19.81 ? 134 ILE A C 1 ATOM 1001 O O . ILE A 1 134 ? 28.096 27.098 19.214 1.00 18.94 ? 134 ILE A O 1 ATOM 1002 C CB . ILE A 1 134 ? 28.617 24.157 18.609 1.00 17.51 ? 134 ILE A CB 1 ATOM 1003 C CG1 . ILE A 1 134 ? 29.398 23.124 17.788 1.00 17.61 ? 134 ILE A CG1 1 ATOM 1004 C CG2 . ILE A 1 134 ? 27.447 23.509 19.351 1.00 19.49 ? 134 ILE A CG2 1 ATOM 1005 C CD1 . ILE A 1 134 ? 30.148 22.114 18.641 1.00 12.41 ? 134 ILE A CD1 1 ATOM 1006 N N . ARG A 1 135 ? 26.086 26.387 18.512 1.00 21.73 ? 135 ARG A N 1 ATOM 1007 C CA . ARG A 1 135 ? 25.378 27.387 19.305 1.00 21.76 ? 135 ARG A CA 1 ATOM 1008 C C . ARG A 1 135 ? 24.417 26.776 20.308 1.00 21.65 ? 135 ARG A C 1 ATOM 1009 O O . ARG A 1 135 ? 23.626 25.903 19.970 1.00 20.79 ? 135 ARG A O 1 ATOM 1010 C CB . ARG A 1 135 ? 24.639 28.371 18.384 1.00 24.84 ? 135 ARG A CB 1 ATOM 1011 C CG . ARG A 1 135 ? 25.594 29.258 17.593 1.00 28.56 ? 135 ARG A CG 1 ATOM 1012 C CD . ARG A 1 135 ? 24.896 30.443 16.945 1.00 35.00 ? 135 ARG A CD 1 ATOM 1013 N NE . ARG A 1 135 ? 25.874 31.376 16.386 1.00 38.87 ? 135 ARG A NE 1 ATOM 1014 C CZ . ARG A 1 135 ? 26.670 31.097 15.358 1.00 40.50 ? 135 ARG A CZ 1 ATOM 1015 N NH1 . ARG A 1 135 ? 26.600 29.912 14.764 1.00 41.91 ? 135 ARG A NH1 1 ATOM 1016 N NH2 . ARG A 1 135 ? 27.555 31.993 14.938 1.00 40.31 ? 135 ARG A NH2 1 ATOM 1017 N N . ILE A 1 136 ? 24.499 27.245 21.548 1.00 21.59 ? 136 ILE A N 1 ATOM 1018 C CA . ILE A 1 136 ? 23.651 26.740 22.619 1.00 24.43 ? 136 ILE A CA 1 ATOM 1019 C C . ILE A 1 136 ? 22.742 27.845 23.159 1.00 27.29 ? 136 ILE A C 1 ATOM 1020 O O . ILE A 1 136 ? 23.202 28.936 23.483 1.00 25.11 ? 136 ILE A O 1 ATOM 1021 C CB . ILE A 1 136 ? 24.517 26.170 23.760 1.00 24.71 ? 136 ILE A CB 1 ATOM 1022 C CG1 . ILE A 1 136 ? 25.550 25.200 23.176 1.00 23.08 ? 136 ILE A CG1 1 ATOM 1023 C CG2 . ILE A 1 136 ? 23.636 25.455 24.781 1.00 26.24 ? 136 ILE A CG2 1 ATOM 1024 C CD1 . ILE A 1 136 ? 26.556 24.681 24.178 1.00 24.74 ? 136 ILE A CD1 1 ATOM 1025 N N . ALA A 1 137 ? 21.448 27.553 23.249 1.00 30.12 ? 137 ALA A N 1 ATOM 1026 C CA . ALA A 1 137 ? 20.470 28.522 23.732 1.00 34.76 ? 137 ALA A CA 1 ATOM 1027 C C . ALA A 1 137 ? 20.306 28.513 25.252 1.00 38.65 ? 137 ALA A C 1 ATOM 1028 O O . ALA A 1 137 ? 20.808 27.626 25.941 1.00 40.53 ? 137 ALA A O 1 ATOM 1029 C CB . ALA A 1 137 ? 19.128 28.270 23.059 1.00 34.19 ? 137 ALA A CB 1 ATOM 1030 N N . ALA A 1 138 ? 19.598 29.514 25.768 1.00 42.99 ? 138 ALA A N 1 ATOM 1031 C CA . ALA A 1 138 ? 19.356 29.638 27.204 1.00 44.62 ? 138 ALA A CA 1 ATOM 1032 C C . ALA A 1 138 ? 18.719 28.374 27.773 1.00 45.98 ? 138 ALA A C 1 ATOM 1033 O O . ALA A 1 138 ? 17.501 28.303 27.946 1.00 46.09 ? 138 ALA A O 1 ATOM 1034 C CB . ALA A 1 138 ? 18.458 30.839 27.476 1.00 44.84 ? 138 ALA A CB 1 ATOM 1035 N N . SER A 1 152 ? 5.387 17.451 14.429 1.00 44.08 ? 152 SER A N 1 ATOM 1036 C CA . SER A 1 152 ? 6.024 18.604 15.061 1.00 43.77 ? 152 SER A CA 1 ATOM 1037 C C . SER A 1 152 ? 7.084 18.179 16.074 1.00 41.25 ? 152 SER A C 1 ATOM 1038 O O . SER A 1 152 ? 8.180 18.742 16.111 1.00 42.29 ? 152 SER A O 1 ATOM 1039 C CB . SER A 1 152 ? 4.978 19.475 15.757 1.00 44.61 ? 152 SER A CB 1 ATOM 1040 O OG . SER A 1 152 ? 5.603 20.547 16.443 1.00 48.48 ? 152 SER A OG 1 ATOM 1041 N N . ILE A 1 153 ? 6.752 17.197 16.907 1.00 37.74 ? 153 ILE A N 1 ATOM 1042 C CA . ILE A 1 153 ? 7.702 16.710 17.898 1.00 33.92 ? 153 ILE A CA 1 ATOM 1043 C C . ILE A 1 153 ? 8.481 15.550 17.302 1.00 29.76 ? 153 ILE A C 1 ATOM 1044 O O . ILE A 1 153 ? 7.922 14.487 17.042 1.00 29.22 ? 153 ILE A O 1 ATOM 1045 C CB . ILE A 1 153 ? 6.999 16.214 19.183 1.00 34.71 ? 153 ILE A CB 1 ATOM 1046 C CG1 . ILE A 1 153 ? 6.265 17.373 19.864 1.00 35.80 ? 153 ILE A CG1 1 ATOM 1047 C CG2 . ILE A 1 153 ? 8.027 15.617 20.143 1.00 34.54 ? 153 ILE A CG2 1 ATOM 1048 C CD1 . ILE A 1 153 ? 7.176 18.479 20.372 1.00 34.61 ? 153 ILE A CD1 1 ATOM 1049 N N . ASN A 1 154 ? 9.769 15.762 17.071 1.00 25.95 ? 154 ASN A N 1 ATOM 1050 C CA . ASN A 1 154 ? 10.616 14.720 16.512 1.00 24.16 ? 154 ASN A CA 1 ATOM 1051 C C . ASN A 1 154 ? 11.634 14.277 17.548 1.00 21.47 ? 154 ASN A C 1 ATOM 1052 O O . ASN A 1 154 ? 12.224 15.109 18.238 1.00 19.28 ? 154 ASN A O 1 ATOM 1053 C CB . ASN A 1 154 ? 11.326 15.229 15.259 1.00 26.60 ? 154 ASN A CB 1 ATOM 1054 C CG . ASN A 1 154 ? 10.356 15.591 14.159 1.00 27.62 ? 154 ASN A CG 1 ATOM 1055 O OD1 . ASN A 1 154 ? 9.521 14.781 13.769 1.00 28.71 ? 154 ASN A OD1 1 ATOM 1056 N ND2 . ASN A 1 154 ? 10.457 16.810 13.656 1.00 32.27 ? 154 ASN A ND2 1 ATOM 1057 N N . ILE A 1 155 ? 11.833 12.967 17.654 1.00 17.89 ? 155 ILE A N 1 ATOM 1058 C CA . ILE A 1 155 ? 12.770 12.426 18.623 1.00 16.79 ? 155 ILE A CA 1 ATOM 1059 C C . ILE A 1 155 ? 14.117 12.036 18.010 1.00 16.33 ? 155 ILE A C 1 ATOM 1060 O O . ILE A 1 155 ? 15.065 11.727 18.731 1.00 15.72 ? 155 ILE A O 1 ATOM 1061 C CB . ILE A 1 155 ? 12.170 11.200 19.339 1.00 15.97 ? 155 ILE A CB 1 ATOM 1062 C CG1 . ILE A 1 155 ? 11.754 10.149 18.302 1.00 15.90 ? 155 ILE A CG1 1 ATOM 1063 C CG2 . ILE A 1 155 ? 10.974 11.633 20.208 1.00 15.32 ? 155 ILE A CG2 1 ATOM 1064 C CD1 . ILE A 1 155 ? 11.307 8.829 18.899 1.00 16.79 ? 155 ILE A CD1 1 ATOM 1065 N N . ALA A 1 156 ? 14.192 12.046 16.684 1.00 16.56 ? 156 ALA A N 1 ATOM 1066 C CA . ALA A 1 156 ? 15.425 11.697 15.988 1.00 15.35 ? 156 ALA A CA 1 ATOM 1067 C C . ALA A 1 156 ? 15.877 12.855 15.128 1.00 15.81 ? 156 ALA A C 1 ATOM 1068 O O . ALA A 1 156 ? 15.069 13.508 14.466 1.00 17.00 ? 156 ALA A O 1 ATOM 1069 C CB . ALA A 1 156 ? 15.219 10.453 15.122 1.00 14.71 ? 156 ALA A CB 1 ATOM 1070 N N . GLN A 1 157 ? 17.178 13.109 15.144 1.00 15.28 ? 157 GLN A N 1 ATOM 1071 C CA . GLN A 1 157 ? 17.763 14.188 14.365 1.00 16.47 ? 157 GLN A CA 1 ATOM 1072 C C . GLN A 1 157 ? 19.105 13.698 13.823 1.00 17.18 ? 157 GLN A C 1 ATOM 1073 O O . GLN A 1 157 ? 19.739 12.819 14.414 1.00 14.87 ? 157 GLN A O 1 ATOM 1074 C CB . GLN A 1 157 ? 17.966 15.416 15.261 1.00 16.11 ? 157 GLN A CB 1 ATOM 1075 C CG . GLN A 1 157 ? 18.640 16.607 14.606 1.00 18.31 ? 157 GLN A CG 1 ATOM 1076 C CD . GLN A 1 157 ? 17.867 17.146 13.412 1.00 21.45 ? 157 GLN A CD 1 ATOM 1077 O OE1 . GLN A 1 157 ? 17.791 16.504 12.359 1.00 22.30 ? 157 GLN A OE1 1 ATOM 1078 N NE2 . GLN A 1 157 ? 17.286 18.332 13.573 1.00 20.89 ? 157 GLN A NE2 1 ATOM 1079 N N . ILE A 1 158 ? 19.524 14.247 12.690 1.00 16.80 ? 158 ILE A N 1 ATOM 1080 C CA . ILE A 1 158 ? 20.803 13.860 12.102 1.00 20.04 ? 158 ILE A CA 1 ATOM 1081 C C . ILE A 1 158 ? 21.829 14.962 12.291 1.00 20.55 ? 158 ILE A C 1 ATOM 1082 O O . ILE A 1 158 ? 21.491 16.145 12.298 1.00 20.83 ? 158 ILE A O 1 ATOM 1083 C CB . ILE A 1 158 ? 20.700 13.602 10.579 1.00 20.82 ? 158 ILE A CB 1 ATOM 1084 C CG1 . ILE A 1 158 ? 20.261 14.883 9.864 1.00 24.24 ? 158 ILE A CG1 1 ATOM 1085 C CG2 . ILE A 1 158 ? 19.724 12.472 10.299 1.00 19.47 ? 158 ILE A CG2 1 ATOM 1086 C CD1 . ILE A 1 158 ? 20.329 14.792 8.339 1.00 26.06 ? 158 ILE A CD1 1 ATOM 1087 N N . VAL A 1 159 ? 23.086 14.568 12.456 1.00 20.97 ? 159 VAL A N 1 ATOM 1088 C CA . VAL A 1 159 ? 24.170 15.528 12.594 1.00 20.47 ? 159 VAL A CA 1 ATOM 1089 C C . VAL A 1 159 ? 25.195 15.219 11.507 1.00 19.92 ? 159 VAL A C 1 ATOM 1090 O O . VAL A 1 159 ? 25.974 14.285 11.634 1.00 18.51 ? 159 VAL A O 1 ATOM 1091 C CB . VAL A 1 159 ? 24.869 15.433 13.968 1.00 22.06 ? 159 VAL A CB 1 ATOM 1092 C CG1 . VAL A 1 159 ? 26.123 16.305 13.970 1.00 22.66 ? 159 VAL A CG1 1 ATOM 1093 C CG2 . VAL A 1 159 ? 23.925 15.872 15.069 1.00 21.64 ? 159 VAL A CG2 1 ATOM 1094 N N . PRO A 1 160 ? 25.175 15.977 10.403 1.00 19.65 ? 160 PRO A N 1 ATOM 1095 C CA . PRO A 1 160 ? 26.136 15.740 9.320 1.00 20.72 ? 160 PRO A CA 1 ATOM 1096 C C . PRO A 1 160 ? 27.497 16.310 9.706 1.00 21.58 ? 160 PRO A C 1 ATOM 1097 O O . PRO A 1 160 ? 27.585 17.358 10.345 1.00 21.72 ? 160 PRO A O 1 ATOM 1098 C CB . PRO A 1 160 ? 25.530 16.500 8.135 1.00 22.38 ? 160 PRO A CB 1 ATOM 1099 C CG . PRO A 1 160 ? 24.068 16.618 8.486 1.00 22.20 ? 160 PRO A CG 1 ATOM 1100 C CD . PRO A 1 160 ? 24.120 16.901 9.963 1.00 22.06 ? 160 PRO A CD 1 ATOM 1101 N N . MET A 1 161 ? 28.558 15.618 9.320 1.00 21.61 ? 161 MET A N 1 ATOM 1102 C CA . MET A 1 161 ? 29.905 16.083 9.615 1.00 22.41 ? 161 MET A CA 1 ATOM 1103 C C . MET A 1 161 ? 30.247 17.222 8.639 1.00 22.46 ? 161 MET A C 1 ATOM 1104 O O . MET A 1 161 ? 31.104 18.065 8.916 1.00 19.53 ? 161 MET A O 1 ATOM 1105 C CB . MET A 1 161 ? 30.881 14.920 9.445 1.00 21.01 ? 161 MET A CB 1 ATOM 1106 C CG . MET A 1 161 ? 32.219 15.104 10.106 1.00 24.62 ? 161 MET A CG 1 ATOM 1107 S SD . MET A 1 161 ? 33.309 13.734 9.696 1.00 22.52 ? 161 MET A SD 1 ATOM 1108 C CE . MET A 1 161 ? 33.971 14.321 8.175 1.00 21.03 ? 161 MET A CE 1 ATOM 1109 N N . ASP A 1 162 ? 29.554 17.244 7.502 1.00 22.90 ? 162 ASP A N 1 ATOM 1110 C CA . ASP A 1 162 ? 29.767 18.253 6.458 1.00 24.93 ? 162 ASP A CA 1 ATOM 1111 C C . ASP A 1 162 ? 29.806 19.692 6.964 1.00 22.86 ? 162 ASP A C 1 ATOM 1112 O O . ASP A 1 162 ? 30.544 20.521 6.433 1.00 20.69 ? 162 ASP A O 1 ATOM 1113 C CB . ASP A 1 162 ? 28.665 18.165 5.397 1.00 29.29 ? 162 ASP A CB 1 ATOM 1114 C CG . ASP A 1 162 ? 28.732 16.896 4.584 1.00 33.72 ? 162 ASP A CG 1 ATOM 1115 O OD1 . ASP A 1 162 ? 29.707 16.721 3.825 1.00 36.08 ? 162 ASP A OD1 1 ATOM 1116 O OD2 . ASP A 1 162 ? 27.803 16.070 4.703 1.00 36.92 ? 162 ASP A OD2 1 ATOM 1117 N N . GLY A 1 163 ? 28.993 19.989 7.974 1.00 20.28 ? 163 GLY A N 1 ATOM 1118 C CA . GLY A 1 163 ? 28.938 21.336 8.504 1.00 17.65 ? 163 GLY A CA 1 ATOM 1119 C C . GLY A 1 163 ? 30.235 21.794 9.130 1.00 18.50 ? 163 GLY A C 1 ATOM 1120 O O . GLY A 1 163 ? 30.431 22.988 9.374 1.00 16.61 ? 163 GLY A O 1 ATOM 1121 N N . PHE A 1 164 ? 31.134 20.853 9.392 1.00 16.79 ? 164 PHE A N 1 ATOM 1122 C CA . PHE A 1 164 ? 32.400 21.208 10.005 1.00 17.47 ? 164 PHE A CA 1 ATOM 1123 C C . PHE A 1 164 ? 33.562 21.350 9.024 1.00 17.66 ? 164 PHE A C 1 ATOM 1124 O O . PHE A 1 164 ? 34.719 21.384 9.433 1.00 18.44 ? 164 PHE A O 1 ATOM 1125 C CB . PHE A 1 164 ? 32.720 20.221 11.127 1.00 15.15 ? 164 PHE A CB 1 ATOM 1126 C CG . PHE A 1 164 ? 31.788 20.349 12.307 1.00 15.72 ? 164 PHE A CG 1 ATOM 1127 C CD1 . PHE A 1 164 ? 32.186 21.024 13.458 1.00 14.88 ? 164 PHE A CD1 1 ATOM 1128 C CD2 . PHE A 1 164 ? 30.481 19.866 12.230 1.00 14.40 ? 164 PHE A CD2 1 ATOM 1129 C CE1 . PHE A 1 164 ? 31.293 21.224 14.521 1.00 14.25 ? 164 PHE A CE1 1 ATOM 1130 C CE2 . PHE A 1 164 ? 29.580 20.060 13.290 1.00 14.94 ? 164 PHE A CE2 1 ATOM 1131 C CZ . PHE A 1 164 ? 29.992 20.741 14.432 1.00 13.33 ? 164 PHE A CZ 1 ATOM 1132 N N . HIS A 1 165 ? 33.249 21.432 7.730 1.00 18.65 ? 165 HIS A N 1 ATOM 1133 C CA . HIS A 1 165 ? 34.282 21.655 6.714 1.00 16.99 ? 165 HIS A CA 1 ATOM 1134 C C . HIS A 1 165 ? 34.876 23.000 7.085 1.00 17.96 ? 165 HIS A C 1 ATOM 1135 O O . HIS A 1 165 ? 34.133 23.925 7.401 1.00 17.81 ? 165 HIS A O 1 ATOM 1136 C CB . HIS A 1 165 ? 33.688 21.856 5.312 1.00 18.37 ? 165 HIS A CB 1 ATOM 1137 C CG . HIS A 1 165 ? 33.593 20.614 4.486 1.00 20.22 ? 165 HIS A CG 1 ATOM 1138 N ND1 . HIS A 1 165 ? 32.478 19.803 4.486 1.00 21.21 ? 165 HIS A ND1 1 ATOM 1139 C CD2 . HIS A 1 165 ? 34.453 20.071 3.592 1.00 21.27 ? 165 HIS A CD2 1 ATOM 1140 C CE1 . HIS A 1 165 ? 32.654 18.816 3.625 1.00 21.13 ? 165 HIS A CE1 1 ATOM 1141 N NE2 . HIS A 1 165 ? 33.844 18.955 3.070 1.00 21.25 ? 165 HIS A NE2 1 ATOM 1142 N N . LEU A 1 166 ? 36.194 23.133 7.050 1.00 17.82 ? 166 LEU A N 1 ATOM 1143 C CA . LEU A 1 166 ? 36.773 24.436 7.326 1.00 18.85 ? 166 LEU A CA 1 ATOM 1144 C C . LEU A 1 166 ? 36.333 25.284 6.126 1.00 19.24 ? 166 LEU A C 1 ATOM 1145 O O . LEU A 1 166 ? 36.206 24.771 5.013 1.00 20.20 ? 166 LEU A O 1 ATOM 1146 C CB . LEU A 1 166 ? 38.301 24.347 7.397 1.00 18.55 ? 166 LEU A CB 1 ATOM 1147 C CG . LEU A 1 166 ? 38.846 23.510 8.560 1.00 17.39 ? 166 LEU A CG 1 ATOM 1148 C CD1 . LEU A 1 166 ? 40.359 23.378 8.453 1.00 13.24 ? 166 LEU A CD1 1 ATOM 1149 C CD2 . LEU A 1 166 ? 38.452 24.156 9.873 1.00 17.63 ? 166 LEU A CD2 1 ATOM 1150 N N . SER A 1 167 ? 36.073 26.566 6.345 1.00 19.70 ? 167 SER A N 1 ATOM 1151 C CA . SER A 1 167 ? 35.641 27.422 5.250 1.00 20.38 ? 167 SER A CA 1 ATOM 1152 C C . SER A 1 167 ? 36.771 27.569 4.238 1.00 21.04 ? 167 SER A C 1 ATOM 1153 O O . SER A 1 167 ? 37.935 27.318 4.555 1.00 21.86 ? 167 SER A O 1 ATOM 1154 C CB . SER A 1 167 ? 35.228 28.800 5.778 1.00 18.97 ? 167 SER A CB 1 ATOM 1155 O OG . SER A 1 167 ? 36.346 29.521 6.258 1.00 19.99 ? 167 SER A OG 1 ATOM 1156 N N . ARG A 1 168 ? 36.428 27.964 3.018 1.00 21.81 ? 168 ARG A N 1 ATOM 1157 C CA . ARG A 1 168 ? 37.436 28.145 1.981 1.00 23.42 ? 168 ARG A CA 1 ATOM 1158 C C . ARG A 1 168 ? 38.392 29.258 2.390 1.00 23.49 ? 168 ARG A C 1 ATOM 1159 O O . ARG A 1 168 ? 39.579 29.215 2.074 1.00 24.06 ? 168 ARG A O 1 ATOM 1160 C CB . ARG A 1 168 ? 36.773 28.485 0.647 1.00 24.79 ? 168 ARG A CB 1 ATOM 1161 C CG . ARG A 1 168 ? 35.924 27.365 0.059 1.00 29.52 ? 168 ARG A CG 1 ATOM 1162 C CD . ARG A 1 168 ? 35.218 27.848 -1.202 1.00 33.66 ? 168 ARG A CD 1 ATOM 1163 N NE . ARG A 1 168 ? 34.394 29.018 -0.920 1.00 37.23 ? 168 ARG A NE 1 ATOM 1164 C CZ . ARG A 1 168 ? 33.940 29.858 -1.844 1.00 40.85 ? 168 ARG A CZ 1 ATOM 1165 N NH1 . ARG A 1 168 ? 33.196 30.896 -1.487 1.00 42.81 ? 168 ARG A NH1 1 ATOM 1166 N NH2 . ARG A 1 168 ? 34.234 29.666 -3.124 1.00 43.69 ? 168 ARG A NH2 1 ATOM 1167 N N . ARG A 1 169 ? 37.876 30.265 3.086 1.00 24.58 ? 169 ARG A N 1 ATOM 1168 C CA . ARG A 1 169 ? 38.732 31.356 3.533 1.00 26.53 ? 169 ARG A CA 1 ATOM 1169 C C . ARG A 1 169 ? 39.684 30.815 4.596 1.00 25.65 ? 169 ARG A C 1 ATOM 1170 O O . ARG A 1 169 ? 40.828 31.246 4.701 1.00 25.97 ? 169 ARG A O 1 ATOM 1171 C CB . ARG A 1 169 ? 37.899 32.507 4.101 1.00 29.26 ? 169 ARG A CB 1 ATOM 1172 C CG . ARG A 1 169 ? 38.742 33.578 4.776 1.00 36.70 ? 169 ARG A CG 1 ATOM 1173 C CD . ARG A 1 169 ? 37.977 34.875 5.031 1.00 42.10 ? 169 ARG A CD 1 ATOM 1174 N NE . ARG A 1 169 ? 37.758 35.648 3.810 1.00 47.01 ? 169 ARG A NE 1 ATOM 1175 C CZ . ARG A 1 169 ? 36.790 35.410 2.930 1.00 49.45 ? 169 ARG A CZ 1 ATOM 1176 N NH1 . ARG A 1 169 ? 35.933 34.417 3.129 1.00 50.28 ? 169 ARG A NH1 1 ATOM 1177 N NH2 . ARG A 1 169 ? 36.680 36.166 1.844 1.00 51.15 ? 169 ARG A NH2 1 ATOM 1178 N N . CYS A 1 170 ? 39.206 29.858 5.381 1.00 24.73 ? 170 CYS A N 1 ATOM 1179 C CA . CYS A 1 170 ? 40.030 29.251 6.414 1.00 25.18 ? 170 CYS A CA 1 ATOM 1180 C C . CYS A 1 170 ? 41.148 28.461 5.727 1.00 24.94 ? 170 CYS A C 1 ATOM 1181 O O . CYS A 1 170 ? 42.290 28.450 6.181 1.00 24.16 ? 170 CYS A O 1 ATOM 1182 C CB . CYS A 1 170 ? 39.172 28.323 7.279 1.00 26.84 ? 170 CYS A CB 1 ATOM 1183 S SG . CYS A 1 170 ? 39.959 27.752 8.786 1.00 30.55 ? 170 CYS A SG 1 ATOM 1184 N N . LEU A 1 171 ? 40.815 27.807 4.620 1.00 24.27 ? 171 LEU A N 1 ATOM 1185 C CA . LEU A 1 171 ? 41.803 27.028 3.888 1.00 24.69 ? 171 LEU A CA 1 ATOM 1186 C C . LEU A 1 171 ? 42.879 27.925 3.264 1.00 25.58 ? 171 LEU A C 1 ATOM 1187 O O . LEU A 1 171 ? 44.009 27.489 3.061 1.00 26.72 ? 171 LEU A O 1 ATOM 1188 C CB . LEU A 1 171 ? 41.118 26.178 2.806 1.00 21.45 ? 171 LEU A CB 1 ATOM 1189 C CG . LEU A 1 171 ? 40.168 25.063 3.278 1.00 21.57 ? 171 LEU A CG 1 ATOM 1190 C CD1 . LEU A 1 171 ? 39.633 24.300 2.072 1.00 22.36 ? 171 LEU A CD1 1 ATOM 1191 C CD2 . LEU A 1 171 ? 40.898 24.100 4.212 1.00 21.61 ? 171 LEU A CD2 1 ATOM 1192 N N . ASP A 1 172 ? 42.533 29.177 2.972 1.00 26.93 ? 172 ASP A N 1 ATOM 1193 C CA . ASP A 1 172 ? 43.491 30.110 2.380 1.00 29.31 ? 172 ASP A CA 1 ATOM 1194 C C . ASP A 1 172 ? 44.609 30.443 3.356 1.00 29.43 ? 172 ASP A C 1 ATOM 1195 O O . ASP A 1 172 ? 45.693 30.869 2.956 1.00 31.18 ? 172 ASP A O 1 ATOM 1196 C CB . ASP A 1 172 ? 42.814 31.424 1.965 1.00 29.64 ? 172 ASP A CB 1 ATOM 1197 C CG . ASP A 1 172 ? 41.895 31.266 0.766 1.00 32.06 ? 172 ASP A CG 1 ATOM 1198 O OD1 . ASP A 1 172 ? 42.211 30.464 -0.135 1.00 34.07 ? 172 ASP A OD1 1 ATOM 1199 O OD2 . ASP A 1 172 ? 40.860 31.965 0.715 1.00 34.67 ? 172 ASP A OD2 1 ATOM 1200 N N . LEU A 1 173 ? 44.340 30.254 4.641 1.00 28.49 ? 173 LEU A N 1 ATOM 1201 C CA . LEU A 1 173 ? 45.323 30.552 5.669 1.00 28.44 ? 173 LEU A CA 1 ATOM 1202 C C . LEU A 1 173 ? 46.237 29.377 5.974 1.00 28.34 ? 173 LEU A C 1 ATOM 1203 O O . LEU A 1 173 ? 47.124 29.487 6.815 1.00 27.90 ? 173 LEU A O 1 ATOM 1204 C CB . LEU A 1 173 ? 44.620 31.011 6.949 1.00 28.11 ? 173 LEU A CB 1 ATOM 1205 C CG . LEU A 1 173 ? 43.718 32.236 6.771 1.00 29.71 ? 173 LEU A CG 1 ATOM 1206 C CD1 . LEU A 1 173 ? 42.974 32.521 8.072 1.00 30.41 ? 173 LEU A CD1 1 ATOM 1207 C CD2 . LEU A 1 173 ? 44.553 33.436 6.346 1.00 28.12 ? 173 LEU A CD2 1 ATOM 1208 N N . PHE A 1 174 ? 46.016 28.250 5.306 1.00 28.35 ? 174 PHE A N 1 ATOM 1209 C CA . PHE A 1 174 ? 46.866 27.082 5.515 1.00 31.00 ? 174 PHE A CA 1 ATOM 1210 C C . PHE A 1 174 ? 48.256 27.426 4.998 1.00 33.70 ? 174 PHE A C 1 ATOM 1211 O O . PHE A 1 174 ? 48.393 28.213 4.060 1.00 32.58 ? 174 PHE A O 1 ATOM 1212 C CB . PHE A 1 174 ? 46.314 25.870 4.758 1.00 29.61 ? 174 PHE A CB 1 ATOM 1213 C CG . PHE A 1 174 ? 45.334 25.048 5.554 1.00 30.66 ? 174 PHE A CG 1 ATOM 1214 C CD1 . PHE A 1 174 ? 44.268 25.651 6.212 1.00 31.41 ? 174 PHE A CD1 1 ATOM 1215 C CD2 . PHE A 1 174 ? 45.471 23.667 5.631 1.00 30.28 ? 174 PHE A CD2 1 ATOM 1216 C CE1 . PHE A 1 174 ? 43.347 24.886 6.938 1.00 32.10 ? 174 PHE A CE1 1 ATOM 1217 C CE2 . PHE A 1 174 ? 44.559 22.895 6.351 1.00 31.44 ? 174 PHE A CE2 1 ATOM 1218 C CZ . PHE A 1 174 ? 43.495 23.506 7.006 1.00 30.21 ? 174 PHE A CZ 1 ATOM 1219 N N . LYS A 1 175 ? 49.285 26.845 5.606 1.00 36.19 ? 175 LYS A N 1 ATOM 1220 C CA . LYS A 1 175 ? 50.653 27.121 5.180 1.00 39.66 ? 175 LYS A CA 1 ATOM 1221 C C . LYS A 1 175 ? 50.780 26.844 3.685 1.00 40.22 ? 175 LYS A C 1 ATOM 1222 O O . LYS A 1 175 ? 51.528 27.515 2.978 1.00 41.77 ? 175 LYS A O 1 ATOM 1223 C CB . LYS A 1 175 ? 51.644 26.264 5.971 1.00 42.68 ? 175 LYS A CB 1 ATOM 1224 C CG . LYS A 1 175 ? 53.057 26.836 5.995 1.00 48.11 ? 175 LYS A CG 1 ATOM 1225 C CD . LYS A 1 175 ? 53.067 28.243 6.601 1.00 51.21 ? 175 LYS A CD 1 ATOM 1226 C CE . LYS A 1 175 ? 54.436 28.908 6.476 1.00 53.33 ? 175 LYS A CE 1 ATOM 1227 N NZ . LYS A 1 175 ? 54.434 30.307 7.000 1.00 53.83 ? 175 LYS A NZ 1 ATOM 1228 N N . ASP A 1 176 ? 50.035 25.854 3.209 1.00 39.80 ? 176 ASP A N 1 ATOM 1229 C CA . ASP A 1 176 ? 50.035 25.504 1.794 1.00 40.02 ? 176 ASP A CA 1 ATOM 1230 C C . ASP A 1 176 ? 48.587 25.431 1.312 1.00 38.95 ? 176 ASP A C 1 ATOM 1231 O O . ASP A 1 176 ? 48.005 24.350 1.212 1.00 37.36 ? 176 ASP A O 1 ATOM 1232 C CB . ASP A 1 176 ? 50.735 24.164 1.569 1.00 40.57 ? 176 ASP A CB 1 ATOM 1233 C CG . ASP A 1 176 ? 50.658 23.712 0.130 1.00 42.58 ? 176 ASP A CG 1 ATOM 1234 O OD1 . ASP A 1 176 ? 50.724 24.583 -0.762 1.00 42.61 ? 176 ASP A OD1 1 ATOM 1235 O OD2 . ASP A 1 176 ? 50.541 22.493 -0.112 1.00 43.52 ? 176 ASP A OD2 1 ATOM 1236 N N . PRO A 1 177 ? 47.990 26.594 1.006 1.00 38.94 ? 177 PRO A N 1 ATOM 1237 C CA . PRO A 1 177 ? 46.605 26.706 0.536 1.00 39.28 ? 177 PRO A CA 1 ATOM 1238 C C . PRO A 1 177 ? 46.278 25.845 -0.678 1.00 39.58 ? 177 PRO A C 1 ATOM 1239 O O . PRO A 1 177 ? 45.212 25.230 -0.737 1.00 38.02 ? 177 PRO A O 1 ATOM 1240 C CB . PRO A 1 177 ? 46.464 28.194 0.228 1.00 37.91 ? 177 PRO A CB 1 ATOM 1241 C CG . PRO A 1 177 ? 47.430 28.830 1.164 1.00 39.82 ? 177 PRO A CG 1 ATOM 1242 C CD . PRO A 1 177 ? 48.625 27.921 1.056 1.00 38.16 ? 177 PRO A CD 1 ATOM 1243 N N . GLN A 1 178 ? 47.200 25.810 -1.639 1.00 40.10 ? 178 GLN A N 1 ATOM 1244 C CA . GLN A 1 178 ? 47.012 25.050 -2.873 1.00 41.67 ? 178 GLN A CA 1 ATOM 1245 C C . GLN A 1 178 ? 46.590 23.610 -2.610 1.00 40.51 ? 178 GLN A C 1 ATOM 1246 O O . GLN A 1 178 ? 45.574 23.148 -3.128 1.00 40.66 ? 178 GLN A O 1 ATOM 1247 C CB . GLN A 1 178 ? 48.298 25.071 -3.718 1.00 44.90 ? 178 GLN A CB 1 ATOM 1248 C CG . GLN A 1 178 ? 49.430 24.193 -3.187 1.00 49.23 ? 178 GLN A CG 1 ATOM 1249 C CD . GLN A 1 178 ? 50.694 24.260 -4.034 1.00 52.47 ? 178 GLN A CD 1 ATOM 1250 O OE1 . GLN A 1 178 ? 50.651 24.105 -5.258 1.00 54.58 ? 178 GLN A OE1 1 ATOM 1251 N NE2 . GLN A 1 178 ? 51.831 24.478 -3.380 1.00 53.34 ? 178 GLN A NE2 1 ATOM 1252 N N . THR A 1 179 ? 47.373 22.903 -1.804 1.00 39.74 ? 179 THR A N 1 ATOM 1253 C CA . THR A 1 179 ? 47.073 21.518 -1.480 1.00 39.11 ? 179 THR A CA 1 ATOM 1254 C C . THR A 1 179 ? 45.839 21.456 -0.583 1.00 37.29 ? 179 THR A C 1 ATOM 1255 O O . THR A 1 179 ? 45.041 20.524 -0.675 1.00 37.08 ? 179 THR A O 1 ATOM 1256 C CB . THR A 1 179 ? 48.277 20.850 -0.773 1.00 40.55 ? 179 THR A CB 1 ATOM 1257 O OG1 . THR A 1 179 ? 49.400 20.838 -1.664 1.00 43.22 ? 179 THR A OG1 1 ATOM 1258 C CG2 . THR A 1 179 ? 47.950 19.420 -0.370 1.00 41.03 ? 179 THR A CG2 1 ATOM 1259 N N . ALA A 1 180 ? 45.681 22.459 0.275 1.00 34.96 ? 180 ALA A N 1 ATOM 1260 C CA . ALA A 1 180 ? 44.536 22.504 1.177 1.00 34.53 ? 180 ALA A CA 1 ATOM 1261 C C . ALA A 1 180 ? 43.239 22.450 0.375 1.00 33.74 ? 180 ALA A C 1 ATOM 1262 O O . ALA A 1 180 ? 42.346 21.657 0.673 1.00 34.47 ? 180 ALA A O 1 ATOM 1263 C CB . ALA A 1 180 ? 44.583 23.775 2.026 1.00 31.88 ? 180 ALA A CB 1 ATOM 1264 N N . HIS A 1 181 ? 43.144 23.291 -0.651 1.00 33.57 ? 181 HIS A N 1 ATOM 1265 C CA . HIS A 1 181 ? 41.953 23.329 -1.492 1.00 32.70 ? 181 HIS A CA 1 ATOM 1266 C C . HIS A 1 181 ? 41.820 22.099 -2.381 1.00 32.85 ? 181 HIS A C 1 ATOM 1267 O O . HIS A 1 181 ? 40.757 21.487 -2.456 1.00 32.84 ? 181 HIS A O 1 ATOM 1268 C CB . HIS A 1 181 ? 41.955 24.582 -2.370 1.00 30.57 ? 181 HIS A CB 1 ATOM 1269 C CG . HIS A 1 181 ? 41.613 25.837 -1.632 1.00 29.75 ? 181 HIS A CG 1 ATOM 1270 N ND1 . HIS A 1 181 ? 42.569 26.670 -1.093 1.00 30.51 ? 181 HIS A ND1 1 ATOM 1271 C CD2 . HIS A 1 181 ? 40.416 26.394 -1.332 1.00 30.06 ? 181 HIS A CD2 1 ATOM 1272 C CE1 . HIS A 1 181 ? 41.976 27.689 -0.496 1.00 28.59 ? 181 HIS A CE1 1 ATOM 1273 N NE2 . HIS A 1 181 ? 40.670 27.545 -0.626 1.00 30.87 ? 181 HIS A NE2 1 ATOM 1274 N N . LYS A 1 182 ? 42.903 21.742 -3.059 1.00 33.91 ? 182 LYS A N 1 ATOM 1275 C CA . LYS A 1 182 ? 42.893 20.591 -3.949 1.00 35.19 ? 182 LYS A CA 1 ATOM 1276 C C . LYS A 1 182 ? 42.517 19.324 -3.185 1.00 34.78 ? 182 LYS A C 1 ATOM 1277 O O . LYS A 1 182 ? 41.895 18.416 -3.735 1.00 34.82 ? 182 LYS A O 1 ATOM 1278 C CB . LYS A 1 182 ? 44.271 20.437 -4.601 1.00 36.29 ? 182 LYS A CB 1 ATOM 1279 C CG . LYS A 1 182 ? 44.335 19.445 -5.754 1.00 41.12 ? 182 LYS A CG 1 ATOM 1280 C CD . LYS A 1 182 ? 44.447 18.007 -5.274 1.00 43.72 ? 182 LYS A CD 1 ATOM 1281 C CE . LYS A 1 182 ? 44.519 17.039 -6.449 1.00 45.97 ? 182 LYS A CE 1 ATOM 1282 N NZ . LYS A 1 182 ? 45.683 17.316 -7.341 1.00 47.41 ? 182 LYS A NZ 1 ATOM 1283 N N . ARG A 1 183 ? 42.881 19.276 -1.909 1.00 34.06 ? 183 ARG A N 1 ATOM 1284 C CA . ARG A 1 183 ? 42.591 18.112 -1.084 1.00 34.08 ? 183 ARG A CA 1 ATOM 1285 C C . ARG A 1 183 ? 41.423 18.350 -0.130 1.00 31.07 ? 183 ARG A C 1 ATOM 1286 O O . ARG A 1 183 ? 41.284 17.644 0.866 1.00 30.06 ? 183 ARG A O 1 ATOM 1287 C CB . ARG A 1 183 ? 43.836 17.735 -0.285 1.00 37.19 ? 183 ARG A CB 1 ATOM 1288 C CG . ARG A 1 183 ? 43.863 16.302 0.196 1.00 44.99 ? 183 ARG A CG 1 ATOM 1289 C CD . ARG A 1 183 ? 45.195 15.992 0.858 1.00 49.02 ? 183 ARG A CD 1 ATOM 1290 N NE . ARG A 1 183 ? 45.353 14.571 1.145 1.00 52.53 ? 183 ARG A NE 1 ATOM 1291 C CZ . ARG A 1 183 ? 46.421 14.048 1.736 1.00 54.74 ? 183 ARG A CZ 1 ATOM 1292 N NH1 . ARG A 1 183 ? 47.426 14.834 2.106 1.00 55.14 ? 183 ARG A NH1 1 ATOM 1293 N NH2 . ARG A 1 183 ? 46.488 12.740 1.952 1.00 55.91 ? 183 ARG A NH2 1 ATOM 1294 N N . ARG A 1 184 ? 40.585 19.338 -0.432 1.00 27.74 ? 184 ARG A N 1 ATOM 1295 C CA . ARG A 1 184 ? 39.449 19.634 0.433 1.00 26.61 ? 184 ARG A CA 1 ATOM 1296 C C . ARG A 1 184 ? 38.582 18.392 0.589 1.00 26.14 ? 184 ARG A C 1 ATOM 1297 O O . ARG A 1 184 ? 38.160 17.785 -0.394 1.00 25.40 ? 184 ARG A O 1 ATOM 1298 C CB . ARG A 1 184 ? 38.606 20.787 -0.126 1.00 26.57 ? 184 ARG A CB 1 ATOM 1299 C CG . ARG A 1 184 ? 37.560 21.286 0.874 1.00 25.00 ? 184 ARG A CG 1 ATOM 1300 C CD . ARG A 1 184 ? 36.740 22.460 0.357 1.00 25.97 ? 184 ARG A CD 1 ATOM 1301 N NE . ARG A 1 184 ? 36.155 23.206 1.472 1.00 25.59 ? 184 ARG A NE 1 ATOM 1302 C CZ . ARG A 1 184 ? 35.196 24.120 1.352 1.00 27.34 ? 184 ARG A CZ 1 ATOM 1303 N NH1 . ARG A 1 184 ? 34.696 24.415 0.156 1.00 23.01 ? 184 ARG A NH1 1 ATOM 1304 N NH2 . ARG A 1 184 ? 34.734 24.734 2.433 1.00 23.06 ? 184 ARG A NH2 1 ATOM 1305 N N . GLY A 1 185 ? 38.315 18.022 1.833 1.00 24.68 ? 185 GLY A N 1 ATOM 1306 C CA . GLY A 1 185 ? 37.519 16.842 2.093 1.00 22.54 ? 185 GLY A CA 1 ATOM 1307 C C . GLY A 1 185 ? 38.371 15.845 2.857 1.00 23.27 ? 185 GLY A C 1 ATOM 1308 O O . GLY A 1 185 ? 37.871 14.845 3.368 1.00 21.76 ? 185 GLY A O 1 ATOM 1309 N N . SER A 1 186 ? 39.671 16.117 2.925 1.00 21.58 ? 186 SER A N 1 ATOM 1310 C CA . SER A 1 186 ? 40.586 15.247 3.656 1.00 20.98 ? 186 SER A CA 1 ATOM 1311 C C . SER A 1 186 ? 40.320 15.504 5.138 1.00 19.69 ? 186 SER A C 1 ATOM 1312 O O . SER A 1 186 ? 39.743 16.533 5.493 1.00 17.18 ? 186 SER A O 1 ATOM 1313 C CB . SER A 1 186 ? 42.039 15.596 3.327 1.00 22.61 ? 186 SER A CB 1 ATOM 1314 O OG . SER A 1 186 ? 42.407 16.838 3.904 1.00 27.30 ? 186 SER A OG 1 ATOM 1315 N N . PRO A 1 187 ? 40.750 14.582 6.018 1.00 17.80 ? 187 PRO A N 1 ATOM 1316 C CA . PRO A 1 187 ? 40.551 14.713 7.464 1.00 17.84 ? 187 PRO A CA 1 ATOM 1317 C C . PRO A 1 187 ? 41.078 16.028 8.035 1.00 18.51 ? 187 PRO A C 1 ATOM 1318 O O . PRO A 1 187 ? 40.549 16.546 9.019 1.00 18.56 ? 187 PRO A O 1 ATOM 1319 C CB . PRO A 1 187 ? 41.321 13.517 8.032 1.00 17.44 ? 187 PRO A CB 1 ATOM 1320 C CG . PRO A 1 187 ? 41.306 12.534 6.928 1.00 20.26 ? 187 PRO A CG 1 ATOM 1321 C CD . PRO A 1 187 ? 41.536 13.374 5.711 1.00 17.95 ? 187 PRO A CD 1 ATOM 1322 N N . SER A 1 188 ? 42.129 16.562 7.424 1.00 16.85 ? 188 SER A N 1 ATOM 1323 C CA . SER A 1 188 ? 42.723 17.800 7.911 1.00 17.68 ? 188 SER A CA 1 ATOM 1324 C C . SER A 1 188 ? 42.015 19.070 7.442 1.00 17.03 ? 188 SER A C 1 ATOM 1325 O O . SER A 1 188 ? 42.437 20.174 7.790 1.00 17.97 ? 188 SER A O 1 ATOM 1326 C CB . SER A 1 188 ? 44.206 17.859 7.521 1.00 19.66 ? 188 SER A CB 1 ATOM 1327 O OG . SER A 1 188 ? 44.354 17.989 6.118 1.00 23.45 ? 188 SER A OG 1 ATOM 1328 N N . THR A 1 189 ? 40.945 18.933 6.661 1.00 16.39 ? 189 THR A N 1 ATOM 1329 C CA . THR A 1 189 ? 40.231 20.117 6.196 1.00 14.69 ? 189 THR A CA 1 ATOM 1330 C C . THR A 1 189 ? 38.873 20.293 6.874 1.00 15.86 ? 189 THR A C 1 ATOM 1331 O O . THR A 1 189 ? 37.970 20.935 6.334 1.00 14.18 ? 189 THR A O 1 ATOM 1332 C CB . THR A 1 189 ? 40.051 20.120 4.650 1.00 17.13 ? 189 THR A CB 1 ATOM 1333 O OG1 . THR A 1 189 ? 39.383 18.927 4.230 1.00 18.08 ? 189 THR A OG1 1 ATOM 1334 C CG2 . THR A 1 189 ? 41.414 20.210 3.961 1.00 17.81 ? 189 THR A CG2 1 ATOM 1335 N N . PHE A 1 190 ? 38.749 19.726 8.070 1.00 13.96 ? 190 PHE A N 1 ATOM 1336 C CA . PHE A 1 190 ? 37.535 19.825 8.874 1.00 17.29 ? 190 PHE A CA 1 ATOM 1337 C C . PHE A 1 190 ? 37.954 20.343 10.249 1.00 17.66 ? 190 PHE A C 1 ATOM 1338 O O . PHE A 1 190 ? 39.099 20.151 10.666 1.00 16.48 ? 190 PHE A O 1 ATOM 1339 C CB . PHE A 1 190 ? 36.884 18.450 9.052 1.00 16.50 ? 190 PHE A CB 1 ATOM 1340 C CG . PHE A 1 190 ? 36.161 17.939 7.829 1.00 20.89 ? 190 PHE A CG 1 ATOM 1341 C CD1 . PHE A 1 190 ? 34.793 18.157 7.668 1.00 19.20 ? 190 PHE A CD1 1 ATOM 1342 C CD2 . PHE A 1 190 ? 36.844 17.227 6.848 1.00 20.06 ? 190 PHE A CD2 1 ATOM 1343 C CE1 . PHE A 1 190 ? 34.118 17.669 6.550 1.00 22.36 ? 190 PHE A CE1 1 ATOM 1344 C CE2 . PHE A 1 190 ? 36.177 16.736 5.725 1.00 20.79 ? 190 PHE A CE2 1 ATOM 1345 C CZ . PHE A 1 190 ? 34.812 16.956 5.575 1.00 20.78 ? 190 PHE A CZ 1 ATOM 1346 N N . ASP A 1 191 ? 37.036 21.000 10.949 1.00 15.78 ? 191 ASP A N 1 ATOM 1347 C CA . ASP A 1 191 ? 37.335 21.484 12.288 1.00 17.13 ? 191 ASP A CA 1 ATOM 1348 C C . ASP A 1 191 ? 37.081 20.288 13.207 1.00 17.33 ? 191 ASP A C 1 ATOM 1349 O O . ASP A 1 191 ? 36.042 20.199 13.879 1.00 16.00 ? 191 ASP A O 1 ATOM 1350 C CB . ASP A 1 191 ? 36.410 22.644 12.675 1.00 16.91 ? 191 ASP A CB 1 ATOM 1351 C CG . ASP A 1 191 ? 36.838 23.326 13.967 1.00 16.84 ? 191 ASP A CG 1 ATOM 1352 O OD1 . ASP A 1 191 ? 37.560 22.695 14.770 1.00 16.51 ? 191 ASP A OD1 1 ATOM 1353 O OD2 . ASP A 1 191 ? 36.446 24.487 14.183 1.00 14.73 ? 191 ASP A OD2 1 ATOM 1354 N N . SER A 1 192 ? 38.029 19.358 13.212 1.00 16.37 ? 192 SER A N 1 ATOM 1355 C CA . SER A 1 192 ? 37.916 18.160 14.028 1.00 15.95 ? 192 SER A CA 1 ATOM 1356 C C . SER A 1 192 ? 37.801 18.524 15.503 1.00 16.29 ? 192 SER A C 1 ATOM 1357 O O . SER A 1 192 ? 37.148 17.808 16.271 1.00 15.20 ? 192 SER A O 1 ATOM 1358 C CB . SER A 1 192 ? 39.135 17.254 13.800 1.00 15.27 ? 192 SER A CB 1 ATOM 1359 O OG . SER A 1 192 ? 40.323 17.894 14.230 1.00 14.97 ? 192 SER A OG 1 ATOM 1360 N N . ASN A 1 193 ? 38.430 19.637 15.886 1.00 12.85 ? 193 ASN A N 1 ATOM 1361 C CA . ASN A 1 193 ? 38.423 20.123 17.272 1.00 14.99 ? 193 ASN A CA 1 ATOM 1362 C C . ASN A 1 193 ? 36.993 20.353 17.755 1.00 15.38 ? 193 ASN A C 1 ATOM 1363 O O . ASN A 1 193 ? 36.581 19.861 18.808 1.00 14.72 ? 193 ASN A O 1 ATOM 1364 C CB . ASN A 1 193 ? 39.159 21.474 17.397 1.00 14.31 ? 193 ASN A CB 1 ATOM 1365 C CG . ASN A 1 193 ? 40.537 21.481 16.741 1.00 19.66 ? 193 ASN A CG 1 ATOM 1366 O OD1 . ASN A 1 193 ? 40.747 20.882 15.683 1.00 17.84 ? 193 ASN A OD1 1 ATOM 1367 N ND2 . ASN A 1 193 ? 41.478 22.197 17.361 1.00 18.12 ? 193 ASN A ND2 1 ATOM 1368 N N . ASN A 1 194 ? 36.243 21.137 16.988 1.00 15.61 ? 194 ASN A N 1 ATOM 1369 C CA . ASN A 1 194 ? 34.874 21.449 17.363 1.00 15.04 ? 194 ASN A CA 1 ATOM 1370 C C . ASN A 1 194 ? 33.912 20.283 17.182 1.00 15.64 ? 194 ASN A C 1 ATOM 1371 O O . ASN A 1 194 ? 32.923 20.187 17.908 1.00 15.13 ? 194 ASN A O 1 ATOM 1372 C CB . ASN A 1 194 ? 34.366 22.674 16.592 1.00 16.26 ? 194 ASN A CB 1 ATOM 1373 C CG . ASN A 1 194 ? 33.647 23.666 17.496 1.00 15.75 ? 194 ASN A CG 1 ATOM 1374 O OD1 . ASN A 1 194 ? 32.772 24.412 17.055 1.00 16.91 ? 194 ASN A OD1 1 ATOM 1375 N ND2 . ASN A 1 194 ? 34.026 23.684 18.765 1.00 11.34 ? 194 ASN A ND2 1 ATOM 1376 N N . PHE A 1 195 ? 34.169 19.397 16.222 1.00 13.92 ? 195 PHE A N 1 ATOM 1377 C CA . PHE A 1 195 ? 33.263 18.265 16.079 1.00 14.22 ? 195 PHE A CA 1 ATOM 1378 C C . PHE A 1 195 ? 33.418 17.399 17.338 1.00 14.29 ? 195 PHE A C 1 ATOM 1379 O O . PHE A 1 195 ? 32.431 16.934 17.915 1.00 11.70 ? 195 PHE A O 1 ATOM 1380 C CB . PHE A 1 195 ? 33.568 17.421 14.839 1.00 14.20 ? 195 PHE A CB 1 ATOM 1381 C CG . PHE A 1 195 ? 32.466 16.446 14.509 1.00 16.51 ? 195 PHE A CG 1 ATOM 1382 C CD1 . PHE A 1 195 ? 31.332 16.868 13.821 1.00 14.41 ? 195 PHE A CD1 1 ATOM 1383 C CD2 . PHE A 1 195 ? 32.520 15.130 14.964 1.00 16.57 ? 195 PHE A CD2 1 ATOM 1384 C CE1 . PHE A 1 195 ? 30.273 15.991 13.597 1.00 14.39 ? 195 PHE A CE1 1 ATOM 1385 C CE2 . PHE A 1 195 ? 31.465 14.257 14.744 1.00 11.85 ? 195 PHE A CE2 1 ATOM 1386 C CZ . PHE A 1 195 ? 30.344 14.690 14.061 1.00 15.02 ? 195 PHE A CZ 1 ATOM 1387 N N . LEU A 1 196 ? 34.659 17.177 17.760 1.00 14.04 ? 196 LEU A N 1 ATOM 1388 C CA . LEU A 1 196 ? 34.898 16.408 18.978 1.00 15.34 ? 196 LEU A CA 1 ATOM 1389 C C . LEU A 1 196 ? 34.168 17.094 20.132 1.00 15.64 ? 196 LEU A C 1 ATOM 1390 O O . LEU A 1 196 ? 33.538 16.436 20.958 1.00 16.99 ? 196 LEU A O 1 ATOM 1391 C CB . LEU A 1 196 ? 36.400 16.336 19.282 1.00 16.92 ? 196 LEU A CB 1 ATOM 1392 C CG . LEU A 1 196 ? 36.806 15.765 20.648 1.00 17.69 ? 196 LEU A CG 1 ATOM 1393 C CD1 . LEU A 1 196 ? 36.226 14.370 20.830 1.00 16.94 ? 196 LEU A CD1 1 ATOM 1394 C CD2 . LEU A 1 196 ? 38.330 15.730 20.752 1.00 18.16 ? 196 LEU A CD2 1 ATOM 1395 N N . GLN A 1 197 ? 34.243 18.422 20.177 1.00 16.57 ? 197 GLN A N 1 ATOM 1396 C CA . GLN A 1 197 ? 33.584 19.191 21.228 1.00 16.73 ? 197 GLN A CA 1 ATOM 1397 C C . GLN A 1 197 ? 32.078 18.974 21.157 1.00 16.53 ? 197 GLN A C 1 ATOM 1398 O O . GLN A 1 197 ? 31.418 18.893 22.184 1.00 18.15 ? 197 GLN A O 1 ATOM 1399 C CB . GLN A 1 197 ? 33.909 20.680 21.093 1.00 16.87 ? 197 GLN A CB 1 ATOM 1400 C CG . GLN A 1 197 ? 33.365 21.554 22.226 1.00 18.89 ? 197 GLN A CG 1 ATOM 1401 C CD . GLN A 1 197 ? 33.817 21.081 23.599 1.00 21.20 ? 197 GLN A CD 1 ATOM 1402 O OE1 . GLN A 1 197 ? 34.990 20.774 23.807 1.00 20.27 ? 197 GLN A OE1 1 ATOM 1403 N NE2 . GLN A 1 197 ? 32.886 21.026 24.545 1.00 21.40 ? 197 GLN A NE2 1 ATOM 1404 N N . LEU A 1 198 ? 31.527 18.891 19.949 1.00 17.23 ? 198 LEU A N 1 ATOM 1405 C CA . LEU A 1 198 ? 30.095 18.635 19.819 1.00 16.26 ? 198 LEU A CA 1 ATOM 1406 C C . LEU A 1 198 ? 29.802 17.274 20.446 1.00 14.22 ? 198 LEU A C 1 ATOM 1407 O O . LEU A 1 198 ? 28.814 17.114 21.159 1.00 14.38 ? 198 LEU A O 1 ATOM 1408 C CB . LEU A 1 198 ? 29.659 18.624 18.350 1.00 14.79 ? 198 LEU A CB 1 ATOM 1409 C CG . LEU A 1 198 ? 28.219 18.161 18.060 1.00 13.90 ? 198 LEU A CG 1 ATOM 1410 C CD1 . LEU A 1 198 ? 27.217 18.979 18.854 1.00 13.94 ? 198 LEU A CD1 1 ATOM 1411 C CD2 . LEU A 1 198 ? 27.939 18.278 16.556 1.00 13.30 ? 198 LEU A CD2 1 ATOM 1412 N N . CYS A 1 199 ? 30.665 16.296 20.185 1.00 11.73 ? 199 CYS A N 1 ATOM 1413 C CA . CYS A 1 199 ? 30.467 14.957 20.744 1.00 15.25 ? 199 CYS A CA 1 ATOM 1414 C C . CYS A 1 199 ? 30.533 14.982 22.267 1.00 14.62 ? 199 CYS A C 1 ATOM 1415 O O . CYS A 1 199 ? 29.758 14.299 22.934 1.00 15.27 ? 199 CYS A O 1 ATOM 1416 C CB . CYS A 1 199 ? 31.493 13.977 20.181 1.00 13.66 ? 199 CYS A CB 1 ATOM 1417 S SG . CYS A 1 199 ? 31.240 13.642 18.424 1.00 15.41 ? 199 CYS A SG 1 ATOM 1418 N N . LYS A 1 200 ? 31.432 15.790 22.818 1.00 14.97 ? 200 LYS A N 1 ATOM 1419 C CA . LYS A 1 200 ? 31.540 15.898 24.275 1.00 16.34 ? 200 LYS A CA 1 ATOM 1420 C C . LYS A 1 200 ? 30.261 16.491 24.870 1.00 17.13 ? 200 LYS A C 1 ATOM 1421 O O . LYS A 1 200 ? 29.830 16.108 25.959 1.00 17.60 ? 200 LYS A O 1 ATOM 1422 C CB . LYS A 1 200 ? 32.733 16.774 24.662 1.00 16.63 ? 200 LYS A CB 1 ATOM 1423 C CG . LYS A 1 200 ? 34.084 16.113 24.459 1.00 17.87 ? 200 LYS A CG 1 ATOM 1424 C CD . LYS A 1 200 ? 35.205 17.025 24.938 1.00 20.47 ? 200 LYS A CD 1 ATOM 1425 C CE . LYS A 1 200 ? 36.564 16.364 24.776 1.00 22.54 ? 200 LYS A CE 1 ATOM 1426 N NZ . LYS A 1 200 ? 37.660 17.264 25.226 1.00 25.14 ? 200 LYS A NZ 1 ATOM 1427 N N . ILE A 1 201 ? 29.670 17.442 24.153 1.00 16.37 ? 201 ILE A N 1 ATOM 1428 C CA . ILE A 1 201 ? 28.445 18.082 24.588 1.00 14.57 ? 201 ILE A CA 1 ATOM 1429 C C . ILE A 1 201 ? 27.308 17.063 24.533 1.00 15.15 ? 201 ILE A C 1 ATOM 1430 O O . ILE A 1 201 ? 26.496 16.971 25.455 1.00 14.12 ? 201 ILE A O 1 ATOM 1431 C CB . ILE A 1 201 ? 28.130 19.309 23.696 1.00 15.86 ? 201 ILE A CB 1 ATOM 1432 C CG1 . ILE A 1 201 ? 29.054 20.472 24.086 1.00 16.04 ? 201 ILE A CG1 1 ATOM 1433 C CG2 . ILE A 1 201 ? 26.670 19.710 23.831 1.00 17.16 ? 201 ILE A CG2 1 ATOM 1434 C CD1 . ILE A 1 201 ? 28.993 21.646 23.144 1.00 20.39 ? 201 ILE A CD1 1 ATOM 1435 N N . LEU A 1 202 ? 27.255 16.288 23.454 1.00 13.54 ? 202 LEU A N 1 ATOM 1436 C CA . LEU A 1 202 ? 26.223 15.266 23.323 1.00 14.65 ? 202 LEU A CA 1 ATOM 1437 C C . LEU A 1 202 ? 26.334 14.212 24.421 1.00 15.38 ? 202 LEU A C 1 ATOM 1438 O O . LEU A 1 202 ? 25.326 13.794 24.994 1.00 15.86 ? 202 LEU A O 1 ATOM 1439 C CB . LEU A 1 202 ? 26.314 14.590 21.953 1.00 14.41 ? 202 LEU A CB 1 ATOM 1440 C CG . LEU A 1 202 ? 25.963 15.484 20.761 1.00 14.47 ? 202 LEU A CG 1 ATOM 1441 C CD1 . LEU A 1 202 ? 26.198 14.724 19.466 1.00 16.84 ? 202 LEU A CD1 1 ATOM 1442 C CD2 . LEU A 1 202 ? 24.515 15.934 20.870 1.00 14.94 ? 202 LEU A CD2 1 ATOM 1443 N N . ALA A 1 203 ? 27.554 13.780 24.719 1.00 15.98 ? 203 ALA A N 1 ATOM 1444 C CA . ALA A 1 203 ? 27.757 12.762 25.751 1.00 15.43 ? 203 ALA A CA 1 ATOM 1445 C C . ALA A 1 203 ? 27.293 13.273 27.107 1.00 17.27 ? 203 ALA A C 1 ATOM 1446 O O . ALA A 1 203 ? 26.724 12.526 27.915 1.00 14.27 ? 203 ALA A O 1 ATOM 1447 C CB . ALA A 1 203 ? 29.229 12.364 25.813 1.00 14.96 ? 203 ALA A CB 1 ATOM 1448 N N . LYS A 1 204 ? 27.542 14.554 27.352 1.00 17.40 ? 204 LYS A N 1 ATOM 1449 C CA . LYS A 1 204 ? 27.145 15.173 28.604 1.00 18.78 ? 204 LYS A CA 1 ATOM 1450 C C . LYS A 1 204 ? 25.620 15.270 28.681 1.00 19.99 ? 204 LYS A C 1 ATOM 1451 O O . LYS A 1 204 ? 25.032 15.077 29.746 1.00 18.31 ? 204 LYS A O 1 ATOM 1452 C CB . LYS A 1 204 ? 27.784 16.557 28.718 1.00 19.99 ? 204 LYS A CB 1 ATOM 1453 C CG . LYS A 1 204 ? 27.625 17.194 30.080 1.00 27.56 ? 204 LYS A CG 1 ATOM 1454 C CD . LYS A 1 204 ? 28.494 18.435 30.226 1.00 30.52 ? 204 LYS A CD 1 ATOM 1455 C CE . LYS A 1 204 ? 28.333 19.027 31.619 1.00 33.59 ? 204 LYS A CE 1 ATOM 1456 N NZ . LYS A 1 204 ? 29.223 20.202 31.835 1.00 36.42 ? 204 LYS A NZ 1 ATOM 1457 N N . THR A 1 205 ? 24.973 15.562 27.552 1.00 19.36 ? 205 THR A N 1 ATOM 1458 C CA . THR A 1 205 ? 23.518 15.655 27.549 1.00 20.33 ? 205 THR A CA 1 ATOM 1459 C C . THR A 1 205 ? 22.911 14.262 27.626 1.00 20.50 ? 205 THR A C 1 ATOM 1460 O O . THR A 1 205 ? 21.718 14.113 27.869 1.00 23.58 ? 205 THR A O 1 ATOM 1461 C CB . THR A 1 205 ? 22.967 16.357 26.277 1.00 20.46 ? 205 THR A CB 1 ATOM 1462 O OG1 . THR A 1 205 ? 23.398 15.653 25.101 1.00 19.10 ? 205 THR A OG1 1 ATOM 1463 C CG2 . THR A 1 205 ? 23.427 17.790 26.223 1.00 20.27 ? 205 THR A CG2 1 ATOM 1464 N N . SER A 1 206 ? 23.736 13.243 27.416 1.00 19.45 ? 206 SER A N 1 ATOM 1465 C CA . SER A 1 206 ? 23.275 11.861 27.469 1.00 19.26 ? 206 SER A CA 1 ATOM 1466 C C . SER A 1 206 ? 23.480 11.264 28.856 1.00 21.34 ? 206 SER A C 1 ATOM 1467 O O . SER A 1 206 ? 22.640 10.510 29.353 1.00 21.24 ? 206 SER A O 1 ATOM 1468 C CB . SER A 1 206 ? 24.028 11.011 26.448 1.00 19.61 ? 206 SER A CB 1 ATOM 1469 O OG . SER A 1 206 ? 23.695 9.643 26.606 1.00 21.18 ? 206 SER A OG 1 ATOM 1470 N N . LEU A 1 207 ? 24.594 11.620 29.486 1.00 21.72 ? 207 LEU A N 1 ATOM 1471 C CA . LEU A 1 207 ? 24.930 11.097 30.810 1.00 22.27 ? 207 LEU A CA 1 ATOM 1472 C C . LEU A 1 207 ? 24.384 11.902 31.981 1.00 24.42 ? 207 LEU A C 1 ATOM 1473 O O . LEU A 1 207 ? 24.687 11.603 33.136 1.00 27.29 ? 207 LEU A O 1 ATOM 1474 C CB . LEU A 1 207 ? 26.449 10.968 30.934 1.00 20.59 ? 207 LEU A CB 1 ATOM 1475 C CG . LEU A 1 207 ? 27.015 9.908 29.982 1.00 19.56 ? 207 LEU A CG 1 ATOM 1476 C CD1 . LEU A 1 207 ? 28.522 10.036 29.852 1.00 20.62 ? 207 LEU A CD1 1 ATOM 1477 C CD2 . LEU A 1 207 ? 26.622 8.533 30.491 1.00 20.14 ? 207 LEU A CD2 1 HETATM 1478 N N . CME A 1 208 ? 23.549 12.667 31.865 0.50 21.71 ? 208 CME A N 1 HETATM 1479 C CA . CME A 1 208 ? 22.971 13.489 32.913 0.50 23.80 ? 208 CME A CA 1 HETATM 1480 C CB . CME A 1 208 ? 22.178 14.640 32.296 0.50 24.08 ? 208 CME A CB 1 HETATM 1481 S SG . CME A 1 208 ? 21.058 14.105 30.969 0.70 27.36 ? 208 CME A SG 1 HETATM 1482 S SD . CME A 1 208 ? 19.549 13.160 31.942 0.70 30.06 ? 208 CME A SD 1 HETATM 1483 C CE . CME A 1 208 ? 18.186 14.351 31.890 0.70 28.20 ? 208 CME A CE 1 HETATM 1484 C CZ . CME A 1 208 ? 18.647 15.721 32.312 0.70 30.71 ? 208 CME A CZ 1 HETATM 1485 O OH . CME A 1 208 ? 19.191 15.757 33.463 0.75 32.13 ? 208 CME A OH 1 HETATM 1486 C C . CME A 1 208 ? 22.063 12.639 33.790 0.50 23.27 ? 208 CME A C 1 HETATM 1487 O O . CME A 1 208 ? 21.652 11.543 33.400 0.50 23.65 ? 208 CME A O 1 ATOM 1488 N N . LYS A 1 209 ? 21.088 13.142 34.741 1.00 48.67 ? 209 LYS A N 1 ATOM 1489 C CA . LYS A 1 209 ? 20.383 12.044 35.394 1.00 51.51 ? 209 LYS A CA 1 ATOM 1490 C C . LYS A 1 209 ? 18.876 12.171 35.211 1.00 47.31 ? 209 LYS A C 1 ATOM 1491 O O . LYS A 1 209 ? 18.339 13.276 35.075 1.00 46.21 ? 209 LYS A O 1 ATOM 1492 C CB . LYS A 1 209 ? 20.728 12.042 36.896 1.00 50.51 ? 209 LYS A CB 1 ATOM 1493 C CG . LYS A 1 209 ? 19.658 11.382 37.755 1.00 50.44 ? 209 LYS A CG 1 ATOM 1494 C CD . LYS A 1 209 ? 19.866 11.614 39.251 1.00 48.86 ? 209 LYS A CD 1 ATOM 1495 C CE . LYS A 1 209 ? 21.036 12.547 39.548 1.00 48.27 ? 209 LYS A CE 1 ATOM 1496 N NZ . LYS A 1 209 ? 21.885 12.070 40.647 1.00 47.61 ? 209 LYS A NZ 1 ATOM 1497 N N . VAL A 1 210 ? 18.452 10.871 34.526 1.00 49.44 ? 210 VAL A N 1 ATOM 1498 C CA . VAL A 1 210 ? 17.159 10.728 33.863 1.00 49.55 ? 210 VAL A CA 1 ATOM 1499 C C . VAL A 1 210 ? 16.125 10.361 34.915 1.00 50.82 ? 210 VAL A C 1 ATOM 1500 O O . VAL A 1 210 ? 16.387 9.533 35.786 1.00 50.74 ? 210 VAL A O 1 ATOM 1501 C CB . VAL A 1 210 ? 17.193 9.613 32.787 1.00 48.21 ? 210 VAL A CB 1 ATOM 1502 C CG1 . VAL A 1 210 ? 15.817 9.461 32.152 1.00 46.66 ? 210 VAL A CG1 1 ATOM 1503 C CG2 . VAL A 1 210 ? 18.229 9.924 31.730 1.00 45.54 ? 210 VAL A CG2 1 ATOM 1504 N N . SER A 1 211 ? 14.993 11.019 34.806 1.00 51.80 ? 211 SER A N 1 ATOM 1505 C CA . SER A 1 211 ? 13.885 10.727 35.714 1.00 53.70 ? 211 SER A CA 1 ATOM 1506 C C . SER A 1 211 ? 14.287 10.899 37.175 1.00 54.60 ? 211 SER A C 1 ATOM 1507 O O . SER A 1 211 ? 13.809 10.175 38.052 1.00 55.75 ? 211 SER A O 1 ATOM 1508 C CB . SER A 1 211 ? 13.386 9.295 35.483 1.00 53.15 ? 211 SER A CB 1 ATOM 1509 O OG . SER A 1 211 ? 12.313 8.976 36.352 1.00 55.79 ? 211 SER A OG 1 ATOM 1510 N N . SER A 1 218 ? 6.162 0.964 34.697 1.00 49.91 ? 218 SER A N 1 ATOM 1511 C CA . SER A 1 218 ? 5.704 -0.416 34.559 1.00 48.82 ? 218 SER A CA 1 ATOM 1512 C C . SER A 1 218 ? 5.392 -0.743 33.103 1.00 47.13 ? 218 SER A C 1 ATOM 1513 O O . SER A 1 218 ? 5.134 -1.897 32.759 1.00 47.70 ? 218 SER A O 1 ATOM 1514 C CB . SER A 1 218 ? 4.452 -0.648 35.408 1.00 49.12 ? 218 SER A CB 1 ATOM 1515 O OG . SER A 1 218 ? 3.373 0.150 34.954 1.00 50.63 ? 218 SER A OG 1 ATOM 1516 N N . THR A 1 219 ? 5.412 0.277 32.251 1.00 44.13 ? 219 THR A N 1 ATOM 1517 C CA . THR A 1 219 ? 5.127 0.083 30.835 1.00 40.38 ? 219 THR A CA 1 ATOM 1518 C C . THR A 1 219 ? 6.272 -0.641 30.141 1.00 38.36 ? 219 THR A C 1 ATOM 1519 O O . THR A 1 219 ? 7.322 -0.882 30.742 1.00 37.52 ? 219 THR A O 1 ATOM 1520 C CB . THR A 1 219 ? 4.906 1.424 30.117 1.00 39.67 ? 219 THR A CB 1 ATOM 1521 O OG1 . THR A 1 219 ? 4.657 1.184 28.726 1.00 40.41 ? 219 THR A OG1 1 ATOM 1522 C CG2 . THR A 1 219 ? 6.130 2.311 30.260 1.00 39.50 ? 219 THR A CG2 1 ATOM 1523 N N . SER A 1 220 ? 6.057 -0.987 28.875 1.00 33.56 ? 220 SER A N 1 ATOM 1524 C CA . SER A 1 220 ? 7.070 -1.672 28.083 1.00 32.47 ? 220 SER A CA 1 ATOM 1525 C C . SER A 1 220 ? 7.308 -0.918 26.775 1.00 27.89 ? 220 SER A C 1 ATOM 1526 O O . SER A 1 220 ? 8.276 -1.184 26.061 1.00 32.04 ? 220 SER A O 1 ATOM 1527 C CB . SER A 1 220 ? 6.626 -3.109 27.789 1.00 33.35 ? 220 SER A CB 1 ATOM 1528 O OG . SER A 1 220 ? 5.357 -3.122 27.159 1.00 34.14 ? 220 SER A OG 1 ATOM 1529 N N . SER A 1 221 ? 6.423 0.025 26.470 1.00 24.41 ? 221 SER A N 1 ATOM 1530 C CA . SER A 1 221 ? 6.536 0.815 25.254 1.00 22.19 ? 221 SER A CA 1 ATOM 1531 C C . SER A 1 221 ? 7.679 1.821 25.348 1.00 21.11 ? 221 SER A C 1 ATOM 1532 O O . SER A 1 221 ? 7.699 2.662 26.247 1.00 19.54 ? 221 SER A O 1 ATOM 1533 C CB . SER A 1 221 ? 5.237 1.571 24.989 1.00 25.31 ? 221 SER A CB 1 ATOM 1534 O OG . SER A 1 221 ? 5.419 2.502 23.934 1.00 28.26 ? 221 SER A OG 1 ATOM 1535 N N . VAL A 1 222 ? 8.626 1.742 24.419 1.00 19.35 ? 222 VAL A N 1 ATOM 1536 C CA . VAL A 1 222 ? 9.741 2.671 24.441 1.00 18.20 ? 222 VAL A CA 1 ATOM 1537 C C . VAL A 1 222 ? 9.216 4.098 24.247 1.00 18.04 ? 222 VAL A C 1 ATOM 1538 O O . VAL A 1 222 ? 9.676 5.032 24.901 1.00 17.73 ? 222 VAL A O 1 ATOM 1539 C CB . VAL A 1 222 ? 10.797 2.328 23.353 1.00 17.90 ? 222 VAL A CB 1 ATOM 1540 C CG1 . VAL A 1 222 ? 10.184 2.416 21.954 1.00 17.00 ? 222 VAL A CG1 1 ATOM 1541 C CG2 . VAL A 1 222 ? 11.991 3.271 23.488 1.00 17.24 ? 222 VAL A CG2 1 ATOM 1542 N N . PHE A 1 223 ? 8.223 4.269 23.383 1.00 17.54 ? 223 PHE A N 1 ATOM 1543 C CA . PHE A 1 223 ? 7.685 5.611 23.164 1.00 17.79 ? 223 PHE A CA 1 ATOM 1544 C C . PHE A 1 223 ? 6.990 6.171 24.402 1.00 18.81 ? 223 PHE A C 1 ATOM 1545 O O . PHE A 1 223 ? 7.062 7.371 24.678 1.00 18.81 ? 223 PHE A O 1 ATOM 1546 C CB . PHE A 1 223 ? 6.749 5.621 21.958 1.00 17.02 ? 223 PHE A CB 1 ATOM 1547 C CG . PHE A 1 223 ? 7.443 5.305 20.662 1.00 16.80 ? 223 PHE A CG 1 ATOM 1548 C CD1 . PHE A 1 223 ? 8.718 5.805 20.404 1.00 17.87 ? 223 PHE A CD1 1 ATOM 1549 C CD2 . PHE A 1 223 ? 6.824 4.521 19.695 1.00 18.33 ? 223 PHE A CD2 1 ATOM 1550 C CE1 . PHE A 1 223 ? 9.370 5.530 19.203 1.00 16.82 ? 223 PHE A CE1 1 ATOM 1551 C CE2 . PHE A 1 223 ? 7.471 4.240 18.487 1.00 22.10 ? 223 PHE A CE2 1 ATOM 1552 C CZ . PHE A 1 223 ? 8.750 4.748 18.243 1.00 18.51 ? 223 PHE A CZ 1 ATOM 1553 N N . GLU A 1 224 ? 6.331 5.299 25.157 1.00 20.52 ? 224 GLU A N 1 ATOM 1554 C CA . GLU A 1 224 ? 5.659 5.712 26.383 1.00 22.51 ? 224 GLU A CA 1 ATOM 1555 C C . GLU A 1 224 ? 6.722 6.187 27.373 1.00 21.00 ? 224 GLU A C 1 ATOM 1556 O O . GLU A 1 224 ? 6.603 7.252 27.984 1.00 18.84 ? 224 GLU A O 1 ATOM 1557 C CB . GLU A 1 224 ? 4.905 4.528 26.985 1.00 25.78 ? 224 GLU A CB 1 ATOM 1558 C CG . GLU A 1 224 ? 4.233 4.822 28.312 1.00 33.97 ? 224 GLU A CG 1 ATOM 1559 C CD . GLU A 1 224 ? 2.920 5.554 28.138 1.00 38.55 ? 224 GLU A CD 1 ATOM 1560 O OE1 . GLU A 1 224 ? 2.104 5.085 27.316 1.00 40.67 ? 224 GLU A OE1 1 ATOM 1561 O OE2 . GLU A 1 224 ? 2.703 6.581 28.821 1.00 40.72 ? 224 GLU A OE2 1 ATOM 1562 N N . LYS A 1 225 ? 7.761 5.377 27.534 1.00 19.89 ? 225 LYS A N 1 ATOM 1563 C CA . LYS A 1 225 ? 8.848 5.708 28.446 1.00 20.42 ? 225 LYS A CA 1 ATOM 1564 C C . LYS A 1 225 ? 9.531 7.026 28.094 1.00 19.42 ? 225 LYS A C 1 ATOM 1565 O O . LYS A 1 225 ? 9.717 7.880 28.957 1.00 18.98 ? 225 LYS A O 1 ATOM 1566 C CB . LYS A 1 225 ? 9.885 4.584 28.455 1.00 23.61 ? 225 LYS A CB 1 ATOM 1567 C CG . LYS A 1 225 ? 9.374 3.276 29.040 1.00 24.30 ? 225 LYS A CG 1 ATOM 1568 C CD . LYS A 1 225 ? 10.387 2.165 28.846 1.00 25.42 ? 225 LYS A CD 1 ATOM 1569 C CE . LYS A 1 225 ? 9.806 0.816 29.226 1.00 27.65 ? 225 LYS A CE 1 ATOM 1570 N NZ . LYS A 1 225 ? 10.771 -0.279 28.966 1.00 28.12 ? 225 LYS A NZ 1 ATOM 1571 N N . LEU A 1 226 ? 9.900 7.211 26.831 1.00 19.11 ? 226 LEU A N 1 ATOM 1572 C CA . LEU A 1 226 ? 10.568 8.452 26.466 1.00 20.69 ? 226 LEU A CA 1 ATOM 1573 C C . LEU A 1 226 ? 9.654 9.672 26.569 1.00 19.29 ? 226 LEU A C 1 ATOM 1574 O O . LEU A 1 226 ? 10.111 10.765 26.896 1.00 19.24 ? 226 LEU A O 1 ATOM 1575 C CB . LEU A 1 226 ? 11.163 8.349 25.060 1.00 23.84 ? 226 LEU A CB 1 ATOM 1576 C CG . LEU A 1 226 ? 10.253 8.290 23.837 1.00 25.11 ? 226 LEU A CG 1 ATOM 1577 C CD1 . LEU A 1 226 ? 9.770 9.692 23.483 1.00 28.77 ? 226 LEU A CD1 1 ATOM 1578 C CD2 . LEU A 1 226 ? 11.044 7.696 22.667 1.00 26.36 ? 226 LEU A CD2 1 ATOM 1579 N N . SER A 1 227 ? 8.365 9.480 26.309 1.00 18.81 ? 227 SER A N 1 ATOM 1580 C CA . SER A 1 227 ? 7.402 10.580 26.364 1.00 19.35 ? 227 SER A CA 1 ATOM 1581 C C . SER A 1 227 ? 7.256 11.182 27.755 1.00 20.47 ? 227 SER A C 1 ATOM 1582 O O . SER A 1 227 ? 6.949 12.365 27.899 1.00 19.77 ? 227 SER A O 1 ATOM 1583 C CB . SER A 1 227 ? 6.032 10.110 25.876 1.00 21.10 ? 227 SER A CB 1 ATOM 1584 O OG . SER A 1 227 ? 6.059 9.781 24.499 1.00 20.38 ? 227 SER A OG 1 ATOM 1585 N N . LYS A 1 228 ? 7.483 10.365 28.778 1.00 21.68 ? 228 LYS A N 1 ATOM 1586 C CA . LYS A 1 228 ? 7.358 10.822 30.154 1.00 24.47 ? 228 LYS A CA 1 ATOM 1587 C C . LYS A 1 228 ? 8.686 11.256 30.752 1.00 24.76 ? 228 LYS A C 1 ATOM 1588 O O . LYS A 1 228 ? 8.740 11.668 31.907 1.00 25.90 ? 228 LYS A O 1 ATOM 1589 C CB . LYS A 1 228 ? 6.764 9.709 31.023 1.00 26.50 ? 228 LYS A CB 1 ATOM 1590 C CG . LYS A 1 228 ? 5.373 9.245 30.608 1.00 29.55 ? 228 LYS A CG 1 ATOM 1591 C CD . LYS A 1 228 ? 4.354 10.357 30.737 1.00 31.97 ? 228 LYS A CD 1 ATOM 1592 C CE . LYS A 1 228 ? 2.938 9.831 30.544 1.00 34.70 ? 228 LYS A CE 1 ATOM 1593 N NZ . LYS A 1 228 ? 1.925 10.924 30.619 1.00 33.87 ? 228 LYS A NZ 1 ATOM 1594 N N . THR A 1 229 ? 9.758 11.181 29.971 1.00 24.24 ? 229 THR A N 1 ATOM 1595 C CA . THR A 1 229 ? 11.064 11.546 30.493 1.00 21.95 ? 229 THR A CA 1 ATOM 1596 C C . THR A 1 229 ? 11.814 12.673 29.784 1.00 20.84 ? 229 THR A C 1 ATOM 1597 O O . THR A 1 229 ? 13.022 12.806 29.957 1.00 21.49 ? 229 THR A O 1 ATOM 1598 C CB . THR A 1 229 ? 11.971 10.299 30.569 1.00 22.59 ? 229 THR A CB 1 ATOM 1599 O OG1 . THR A 1 229 ? 12.060 9.681 29.278 1.00 22.45 ? 229 THR A OG1 1 ATOM 1600 C CG2 . THR A 1 229 ? 11.399 9.301 31.573 1.00 24.05 ? 229 THR A CG2 1 ATOM 1601 N N . PHE A 1 230 ? 11.113 13.474 28.984 1.00 19.71 ? 230 PHE A N 1 ATOM 1602 C CA . PHE A 1 230 ? 11.750 14.608 28.323 1.00 20.84 ? 230 PHE A CA 1 ATOM 1603 C C . PHE A 1 230 ? 12.191 15.521 29.468 1.00 22.58 ? 230 PHE A C 1 ATOM 1604 O O . PHE A 1 230 ? 11.483 15.633 30.476 1.00 21.98 ? 230 PHE A O 1 ATOM 1605 C CB . PHE A 1 230 ? 10.754 15.349 27.426 1.00 21.07 ? 230 PHE A CB 1 ATOM 1606 C CG . PHE A 1 230 ? 10.423 14.626 26.149 1.00 20.23 ? 230 PHE A CG 1 ATOM 1607 C CD1 . PHE A 1 230 ? 11.412 14.370 25.204 1.00 18.02 ? 230 PHE A CD1 1 ATOM 1608 C CD2 . PHE A 1 230 ? 9.120 14.212 25.884 1.00 18.99 ? 230 PHE A CD2 1 ATOM 1609 C CE1 . PHE A 1 230 ? 11.107 13.709 24.008 1.00 19.01 ? 230 PHE A CE1 1 ATOM 1610 C CE2 . PHE A 1 230 ? 8.802 13.553 24.693 1.00 19.65 ? 230 PHE A CE2 1 ATOM 1611 C CZ . PHE A 1 230 ? 9.801 13.301 23.752 1.00 18.31 ? 230 PHE A CZ 1 ATOM 1612 N N . SER A 1 231 ? 13.348 16.165 29.331 1.00 20.05 ? 231 SER A N 1 ATOM 1613 C CA . SER A 1 231 ? 13.849 17.027 30.401 1.00 22.47 ? 231 SER A CA 1 ATOM 1614 C C . SER A 1 231 ? 13.977 18.512 30.068 1.00 23.46 ? 231 SER A C 1 ATOM 1615 O O . SER A 1 231 ? 14.599 18.894 29.077 1.00 23.16 ? 231 SER A O 1 ATOM 1616 C CB . SER A 1 231 ? 15.203 16.514 30.894 1.00 21.77 ? 231 SER A CB 1 ATOM 1617 O OG . SER A 1 231 ? 15.697 17.327 31.945 1.00 22.74 ? 231 SER A OG 1 ATOM 1618 N N . GLN A 1 232 ? 13.403 19.348 30.927 1.00 25.41 ? 232 GLN A N 1 ATOM 1619 C CA . GLN A 1 232 ? 13.451 20.790 30.734 1.00 25.89 ? 232 GLN A CA 1 ATOM 1620 C C . GLN A 1 232 ? 14.876 21.330 30.875 1.00 23.48 ? 232 GLN A C 1 ATOM 1621 O O . GLN A 1 232 ? 15.169 22.445 30.456 1.00 24.05 ? 232 GLN A O 1 ATOM 1622 C CB . GLN A 1 232 ? 12.540 21.480 31.751 1.00 30.59 ? 232 GLN A CB 1 ATOM 1623 C CG . GLN A 1 232 ? 12.284 22.942 31.445 1.00 35.89 ? 232 GLN A CG 1 ATOM 1624 C CD . GLN A 1 232 ? 11.724 23.141 30.049 1.00 39.76 ? 232 GLN A CD 1 ATOM 1625 O OE1 . GLN A 1 232 ? 10.657 22.626 29.716 1.00 41.31 ? 232 GLN A OE1 1 ATOM 1626 N NE2 . GLN A 1 232 ? 12.447 23.889 29.221 1.00 44.72 ? 232 GLN A NE2 1 ATOM 1627 N N . THR A 1 233 ? 15.766 20.533 31.450 1.00 21.33 ? 233 THR A N 1 ATOM 1628 C CA . THR A 1 233 ? 17.148 20.966 31.648 1.00 20.76 ? 233 THR A CA 1 ATOM 1629 C C . THR A 1 233 ? 18.026 20.924 30.396 1.00 20.06 ? 233 THR A C 1 ATOM 1630 O O . THR A 1 233 ? 19.123 21.478 30.393 1.00 19.75 ? 233 THR A O 1 ATOM 1631 C CB . THR A 1 233 ? 17.841 20.115 32.712 1.00 20.95 ? 233 THR A CB 1 ATOM 1632 O OG1 . THR A 1 233 ? 17.906 18.760 32.256 1.00 19.72 ? 233 THR A OG1 1 ATOM 1633 C CG2 . THR A 1 233 ? 17.077 20.174 34.026 1.00 22.49 ? 233 THR A CG2 1 ATOM 1634 N N . ILE A 1 234 ? 17.554 20.269 29.339 1.00 18.89 ? 234 ILE A N 1 ATOM 1635 C CA . ILE A 1 234 ? 18.330 20.160 28.104 1.00 18.93 ? 234 ILE A CA 1 ATOM 1636 C C . ILE A 1 234 ? 18.071 21.332 27.160 1.00 20.28 ? 234 ILE A C 1 ATOM 1637 O O . ILE A 1 234 ? 16.961 21.513 26.666 1.00 22.40 ? 234 ILE A O 1 ATOM 1638 C CB . ILE A 1 234 ? 18.011 18.835 27.364 1.00 17.25 ? 234 ILE A CB 1 ATOM 1639 C CG1 . ILE A 1 234 ? 18.300 17.641 28.283 1.00 19.04 ? 234 ILE A CG1 1 ATOM 1640 C CG2 . ILE A 1 234 ? 18.821 18.747 26.063 1.00 18.67 ? 234 ILE A CG2 1 ATOM 1641 C CD1 . ILE A 1 234 ? 19.763 17.470 28.674 1.00 18.07 ? 234 ILE A CD1 1 ATOM 1642 N N . PRO A 1 235 ? 19.105 22.138 26.885 1.00 20.95 ? 235 PRO A N 1 ATOM 1643 C CA . PRO A 1 235 ? 18.982 23.299 25.998 1.00 21.67 ? 235 PRO A CA 1 ATOM 1644 C C . PRO A 1 235 ? 19.037 22.926 24.523 1.00 21.06 ? 235 PRO A C 1 ATOM 1645 O O . PRO A 1 235 ? 19.456 21.823 24.169 1.00 19.47 ? 235 PRO A O 1 ATOM 1646 C CB . PRO A 1 235 ? 20.171 24.153 26.408 1.00 24.22 ? 235 PRO A CB 1 ATOM 1647 C CG . PRO A 1 235 ? 21.230 23.101 26.647 1.00 23.43 ? 235 PRO A CG 1 ATOM 1648 C CD . PRO A 1 235 ? 20.472 22.039 27.436 1.00 22.95 ? 235 PRO A CD 1 ATOM 1649 N N . ASP A 1 236 ? 18.604 23.841 23.662 1.00 20.98 ? 236 ASP A N 1 ATOM 1650 C CA . ASP A 1 236 ? 18.653 23.582 22.230 1.00 21.18 ? 236 ASP A CA 1 ATOM 1651 C C . ASP A 1 236 ? 20.107 23.723 21.817 1.00 20.70 ? 236 ASP A C 1 ATOM 1652 O O . ASP A 1 236 ? 20.813 24.601 22.311 1.00 18.84 ? 236 ASP A O 1 ATOM 1653 C CB . ASP A 1 236 ? 17.807 24.589 21.438 1.00 22.64 ? 236 ASP A CB 1 ATOM 1654 C CG . ASP A 1 236 ? 16.315 24.406 21.648 1.00 27.80 ? 236 ASP A CG 1 ATOM 1655 O OD1 . ASP A 1 236 ? 15.868 23.274 21.946 1.00 26.46 ? 236 ASP A OD1 1 ATOM 1656 O OD2 . ASP A 1 236 ? 15.582 25.401 21.489 1.00 31.40 ? 236 ASP A OD2 1 ATOM 1657 N N . ILE A 1 237 ? 20.549 22.851 20.921 1.00 19.12 ? 237 ILE A N 1 ATOM 1658 C CA . ILE A 1 237 ? 21.922 22.870 20.431 1.00 19.73 ? 237 ILE A CA 1 ATOM 1659 C C . ILE A 1 237 ? 21.863 23.004 18.914 1.00 19.34 ? 237 ILE A C 1 ATOM 1660 O O . ILE A 1 237 ? 21.260 22.174 18.239 1.00 23.41 ? 237 ILE A O 1 ATOM 1661 C CB . ILE A 1 237 ? 22.658 21.557 20.795 1.00 17.34 ? 237 ILE A CB 1 ATOM 1662 C CG1 . ILE A 1 237 ? 22.709 21.395 22.318 1.00 16.37 ? 237 ILE A CG1 1 ATOM 1663 C CG2 . ILE A 1 237 ? 24.073 21.572 20.208 1.00 19.46 ? 237 ILE A CG2 1 ATOM 1664 C CD1 . ILE A 1 237 ? 23.281 20.064 22.770 1.00 16.29 ? 237 ILE A CD1 1 ATOM 1665 N N . PHE A 1 238 ? 22.487 24.047 18.384 1.00 19.56 ? 238 PHE A N 1 ATOM 1666 C CA . PHE A 1 238 ? 22.486 24.297 16.944 1.00 20.54 ? 238 PHE A CA 1 ATOM 1667 C C . PHE A 1 238 ? 23.834 23.970 16.315 1.00 19.51 ? 238 PHE A C 1 ATOM 1668 O O . PHE A 1 238 ? 24.872 24.429 16.784 1.00 19.44 ? 238 PHE A O 1 ATOM 1669 C CB . PHE A 1 238 ? 22.138 25.762 16.680 1.00 22.52 ? 238 PHE A CB 1 ATOM 1670 C CG . PHE A 1 238 ? 20.783 26.156 17.188 1.00 26.58 ? 238 PHE A CG 1 ATOM 1671 C CD1 . PHE A 1 238 ? 19.676 26.119 16.354 1.00 28.24 ? 238 PHE A CD1 1 ATOM 1672 C CD2 . PHE A 1 238 ? 20.607 26.523 18.519 1.00 27.29 ? 238 PHE A CD2 1 ATOM 1673 C CE1 . PHE A 1 238 ? 18.405 26.441 16.842 1.00 28.64 ? 238 PHE A CE1 1 ATOM 1674 C CE2 . PHE A 1 238 ? 19.342 26.845 19.012 1.00 26.22 ? 238 PHE A CE2 1 ATOM 1675 C CZ . PHE A 1 238 ? 18.244 26.803 18.170 1.00 25.08 ? 238 PHE A CZ 1 ATOM 1676 N N . VAL A 1 239 ? 23.815 23.175 15.253 1.00 18.70 ? 239 VAL A N 1 ATOM 1677 C CA . VAL A 1 239 ? 25.050 22.809 14.583 1.00 19.81 ? 239 VAL A CA 1 ATOM 1678 C C . VAL A 1 239 ? 25.028 23.264 13.127 1.00 20.70 ? 239 VAL A C 1 ATOM 1679 O O . VAL A 1 239 ? 23.973 23.315 12.491 1.00 18.68 ? 239 VAL A O 1 ATOM 1680 C CB . VAL A 1 239 ? 25.306 21.275 14.671 1.00 20.36 ? 239 VAL A CB 1 ATOM 1681 C CG1 . VAL A 1 239 ? 25.330 20.845 16.135 1.00 21.08 ? 239 VAL A CG1 1 ATOM 1682 C CG2 . VAL A 1 239 ? 24.243 20.515 13.920 1.00 22.42 ? 239 VAL A CG2 1 ATOM 1683 N N . PRO A 1 240 ? 26.205 23.614 12.584 1.00 21.15 ? 240 PRO A N 1 ATOM 1684 C CA . PRO A 1 240 ? 26.327 24.072 11.199 1.00 18.93 ? 240 PRO A CA 1 ATOM 1685 C C . PRO A 1 240 ? 26.016 23.009 10.151 1.00 20.40 ? 240 PRO A C 1 ATOM 1686 O O . PRO A 1 240 ? 26.052 21.806 10.422 1.00 18.82 ? 240 PRO A O 1 ATOM 1687 C CB . PRO A 1 240 ? 27.773 24.546 11.127 1.00 18.34 ? 240 PRO A CB 1 ATOM 1688 C CG . PRO A 1 240 ? 28.469 23.596 12.066 1.00 19.95 ? 240 PRO A CG 1 ATOM 1689 C CD . PRO A 1 240 ? 27.525 23.578 13.242 1.00 20.56 ? 240 PRO A CD 1 ATOM 1690 N N . GLY A 1 241 ? 25.694 23.477 8.952 1.00 20.54 ? 241 GLY A N 1 ATOM 1691 C CA . GLY A 1 241 ? 25.403 22.587 7.848 1.00 21.45 ? 241 GLY A CA 1 ATOM 1692 C C . GLY A 1 241 ? 26.334 23.001 6.730 1.00 22.30 ? 241 GLY A C 1 ATOM 1693 O O . GLY A 1 241 ? 27.118 23.931 6.898 1.00 23.77 ? 241 GLY A O 1 ATOM 1694 N N . PHE A 1 242 ? 26.263 22.323 5.593 1.00 23.81 ? 242 PHE A N 1 ATOM 1695 C CA . PHE A 1 242 ? 27.119 22.677 4.475 1.00 25.77 ? 242 PHE A CA 1 ATOM 1696 C C . PHE A 1 242 ? 26.282 23.104 3.272 1.00 28.60 ? 242 PHE A C 1 ATOM 1697 O O . PHE A 1 242 ? 25.460 22.337 2.770 1.00 28.53 ? 242 PHE A O 1 ATOM 1698 C CB . PHE A 1 242 ? 28.008 21.496 4.082 1.00 23.20 ? 242 PHE A CB 1 ATOM 1699 C CG . PHE A 1 242 ? 29.110 21.865 3.131 1.00 25.25 ? 242 PHE A CG 1 ATOM 1700 C CD1 . PHE A 1 242 ? 30.227 22.562 3.579 1.00 23.11 ? 242 PHE A CD1 1 ATOM 1701 C CD2 . PHE A 1 242 ? 29.021 21.542 1.780 1.00 26.74 ? 242 PHE A CD2 1 ATOM 1702 C CE1 . PHE A 1 242 ? 31.241 22.935 2.699 1.00 24.39 ? 242 PHE A CE1 1 ATOM 1703 C CE2 . PHE A 1 242 ? 30.034 21.914 0.890 1.00 27.15 ? 242 PHE A CE2 1 ATOM 1704 C CZ . PHE A 1 242 ? 31.145 22.612 1.356 1.00 25.77 ? 242 PHE A CZ 1 ATOM 1705 N N . ASN A 1 243 ? 26.486 24.336 2.824 1.00 31.25 ? 243 ASN A N 1 ATOM 1706 C CA . ASN A 1 243 ? 25.771 24.850 1.664 1.00 34.15 ? 243 ASN A CA 1 ATOM 1707 C C . ASN A 1 243 ? 26.565 24.446 0.425 1.00 34.88 ? 243 ASN A C 1 ATOM 1708 O O . ASN A 1 243 ? 27.592 25.050 0.118 1.00 34.47 ? 243 ASN A O 1 ATOM 1709 C CB . ASN A 1 243 ? 25.673 26.371 1.740 1.00 36.69 ? 243 ASN A CB 1 ATOM 1710 C CG . ASN A 1 243 ? 24.867 26.960 0.603 1.00 38.25 ? 243 ASN A CG 1 ATOM 1711 O OD1 . ASN A 1 243 ? 25.159 26.725 -0.568 1.00 39.86 ? 243 ASN A OD1 1 ATOM 1712 N ND2 . ASN A 1 243 ? 23.847 27.736 0.945 1.00 40.27 ? 243 ASN A ND2 1 ATOM 1713 N N . HIS A 1 244 ? 26.096 23.418 -0.275 1.00 36.87 ? 244 HIS A N 1 ATOM 1714 C CA . HIS A 1 244 ? 26.774 22.928 -1.470 1.00 39.01 ? 244 HIS A CA 1 ATOM 1715 C C . HIS A 1 244 ? 26.811 23.940 -2.606 1.00 39.99 ? 244 HIS A C 1 ATOM 1716 O O . HIS A 1 244 ? 27.601 23.801 -3.541 1.00 40.60 ? 244 HIS A O 1 ATOM 1717 C CB . HIS A 1 244 ? 26.121 21.629 -1.946 1.00 40.75 ? 244 HIS A CB 1 ATOM 1718 C CG . HIS A 1 244 ? 26.446 20.447 -1.086 1.00 43.46 ? 244 HIS A CG 1 ATOM 1719 N ND1 . HIS A 1 244 ? 27.693 19.859 -1.071 1.00 44.33 ? 244 HIS A ND1 1 ATOM 1720 C CD2 . HIS A 1 244 ? 25.701 19.773 -0.177 1.00 43.96 ? 244 HIS A CD2 1 ATOM 1721 C CE1 . HIS A 1 244 ? 27.704 18.875 -0.189 1.00 43.63 ? 244 HIS A CE1 1 ATOM 1722 N NE2 . HIS A 1 244 ? 26.508 18.802 0.367 1.00 44.80 ? 244 HIS A NE2 1 ATOM 1723 N N . ALA A 1 245 ? 25.964 24.962 -2.521 1.00 40.31 ? 245 ALA A N 1 ATOM 1724 C CA . ALA A 1 245 ? 25.920 25.996 -3.548 1.00 40.76 ? 245 ALA A CA 1 ATOM 1725 C C . ALA A 1 245 ? 27.051 26.995 -3.342 1.00 40.72 ? 245 ALA A C 1 ATOM 1726 O O . ALA A 1 245 ? 27.770 27.331 -4.283 1.00 42.14 ? 245 ALA A O 1 ATOM 1727 C CB . ALA A 1 245 ? 24.578 26.715 -3.513 1.00 39.73 ? 245 ALA A CB 1 ATOM 1728 N N . LEU A 1 246 ? 27.206 27.465 -2.107 1.00 40.68 ? 246 LEU A N 1 ATOM 1729 C CA . LEU A 1 246 ? 28.250 28.431 -1.781 1.00 39.69 ? 246 LEU A CA 1 ATOM 1730 C C . LEU A 1 246 ? 29.569 27.747 -1.440 1.00 38.16 ? 246 LEU A C 1 ATOM 1731 O O . LEU A 1 246 ? 30.569 28.414 -1.168 1.00 38.41 ? 246 LEU A O 1 ATOM 1732 C CB . LEU A 1 246 ? 27.811 29.313 -0.608 1.00 41.13 ? 246 LEU A CB 1 ATOM 1733 C CG . LEU A 1 246 ? 26.574 30.191 -0.833 1.00 43.12 ? 246 LEU A CG 1 ATOM 1734 C CD1 . LEU A 1 246 ? 26.280 30.986 0.431 1.00 43.56 ? 246 LEU A CD1 1 ATOM 1735 C CD2 . LEU A 1 246 ? 26.809 31.129 -2.008 1.00 42.71 ? 246 LEU A CD2 1 ATOM 1736 N N . LYS A 1 247 ? 29.562 26.417 -1.457 1.00 35.46 ? 247 LYS A N 1 ATOM 1737 C CA . LYS A 1 247 ? 30.754 25.624 -1.159 1.00 35.02 ? 247 LYS A CA 1 ATOM 1738 C C . LYS A 1 247 ? 31.363 25.996 0.201 1.00 31.03 ? 247 LYS A C 1 ATOM 1739 O O . LYS A 1 247 ? 32.581 26.138 0.324 1.00 29.51 ? 247 LYS A O 1 ATOM 1740 C CB . LYS A 1 247 ? 31.809 25.821 -2.258 1.00 38.44 ? 247 LYS A CB 1 ATOM 1741 C CG . LYS A 1 247 ? 31.251 26.113 -3.651 1.00 44.27 ? 247 LYS A CG 1 ATOM 1742 C CD . LYS A 1 247 ? 30.394 24.976 -4.191 1.00 47.38 ? 247 LYS A CD 1 ATOM 1743 C CE . LYS A 1 247 ? 29.744 25.357 -5.522 1.00 48.81 ? 247 LYS A CE 1 ATOM 1744 N NZ . LYS A 1 247 ? 30.744 25.701 -6.579 1.00 49.63 ? 247 LYS A NZ 1 ATOM 1745 N N . ASP A 1 248 ? 30.514 26.154 1.212 1.00 27.61 ? 248 ASP A N 1 ATOM 1746 C CA . ASP A 1 248 ? 30.968 26.506 2.557 1.00 27.30 ? 248 ASP A CA 1 ATOM 1747 C C . ASP A 1 248 ? 29.944 26.155 3.629 1.00 27.99 ? 248 ASP A C 1 ATOM 1748 O O . ASP A 1 248 ? 28.763 25.957 3.339 1.00 26.56 ? 248 ASP A O 1 ATOM 1749 C CB . ASP A 1 248 ? 31.278 28.006 2.660 1.00 26.39 ? 248 ASP A CB 1 ATOM 1750 C CG . ASP A 1 248 ? 32.721 28.337 2.322 1.00 27.37 ? 248 ASP A CG 1 ATOM 1751 O OD1 . ASP A 1 248 ? 33.624 27.567 2.707 1.00 25.05 ? 248 ASP A OD1 1 ATOM 1752 O OD2 . ASP A 1 248 ? 32.957 29.381 1.686 1.00 29.68 ? 248 ASP A OD2 1 ATOM 1753 N N . PRO A 1 249 ? 30.391 26.073 4.894 1.00 28.87 ? 249 PRO A N 1 ATOM 1754 C CA . PRO A 1 249 ? 29.485 25.748 5.998 1.00 30.53 ? 249 PRO A CA 1 ATOM 1755 C C . PRO A 1 249 ? 28.527 26.904 6.276 1.00 31.86 ? 249 PRO A C 1 ATOM 1756 O O . PRO A 1 249 ? 28.855 28.066 6.037 1.00 32.04 ? 249 PRO A O 1 ATOM 1757 C CB . PRO A 1 249 ? 30.440 25.489 7.161 1.00 29.00 ? 249 PRO A CB 1 ATOM 1758 C CG . PRO A 1 249 ? 31.576 26.405 6.868 1.00 29.93 ? 249 PRO A CG 1 ATOM 1759 C CD . PRO A 1 249 ? 31.775 26.220 5.379 1.00 28.99 ? 249 PRO A CD 1 ATOM 1760 N N . THR A 1 250 ? 27.337 26.574 6.766 1.00 31.43 ? 250 THR A N 1 ATOM 1761 C CA . THR A 1 250 ? 26.336 27.580 7.079 1.00 32.89 ? 250 THR A CA 1 ATOM 1762 C C . THR A 1 250 ? 25.792 27.306 8.483 1.00 32.59 ? 250 THR A C 1 ATOM 1763 O O . THR A 1 250 ? 25.544 26.158 8.858 1.00 32.12 ? 250 THR A O 1 ATOM 1764 C CB . THR A 1 250 ? 25.202 27.575 6.026 1.00 33.63 ? 250 THR A CB 1 ATOM 1765 O OG1 . THR A 1 250 ? 24.220 28.555 6.375 1.00 36.44 ? 250 THR A OG1 1 ATOM 1766 C CG2 . THR A 1 250 ? 24.557 26.207 5.932 1.00 33.68 ? 250 THR A CG2 1 ATOM 1767 N N . PRO A 1 251 ? 25.603 28.366 9.279 1.00 32.35 ? 251 PRO A N 1 ATOM 1768 C CA . PRO A 1 251 ? 25.105 28.277 10.653 1.00 31.12 ? 251 PRO A CA 1 ATOM 1769 C C . PRO A 1 251 ? 23.738 27.667 10.934 1.00 30.49 ? 251 PRO A C 1 ATOM 1770 O O . PRO A 1 251 ? 22.836 27.677 10.099 1.00 30.54 ? 251 PRO A O 1 ATOM 1771 C CB . PRO A 1 251 ? 25.198 29.723 11.141 1.00 31.27 ? 251 PRO A CB 1 ATOM 1772 C CG . PRO A 1 251 ? 24.936 30.506 9.902 1.00 31.77 ? 251 PRO A CG 1 ATOM 1773 C CD . PRO A 1 251 ? 25.775 29.776 8.879 1.00 32.10 ? 251 PRO A CD 1 ATOM 1774 N N . ASP A 1 252 ? 23.630 27.129 12.147 1.00 31.08 ? 252 ASP A N 1 ATOM 1775 C CA . ASP A 1 252 ? 22.425 26.518 12.698 1.00 30.61 ? 252 ASP A CA 1 ATOM 1776 C C . ASP A 1 252 ? 21.475 25.802 11.750 1.00 30.03 ? 252 ASP A C 1 ATOM 1777 O O . ASP A 1 252 ? 20.279 26.097 11.737 1.00 32.53 ? 252 ASP A O 1 ATOM 1778 C CB . ASP A 1 252 ? 21.639 27.581 13.463 1.00 31.53 ? 252 ASP A CB 1 ATOM 1779 C CG . ASP A 1 252 ? 22.539 28.553 14.191 1.00 32.49 ? 252 ASP A CG 1 ATOM 1780 O OD1 . ASP A 1 252 ? 23.562 28.111 14.753 1.00 33.91 ? 252 ASP A OD1 1 ATOM 1781 O OD2 . ASP A 1 252 ? 22.220 29.758 14.210 1.00 34.23 ? 252 ASP A OD2 1 ATOM 1782 N N . GLN A 1 253 ? 21.985 24.846 10.984 1.00 27.54 ? 253 GLN A N 1 ATOM 1783 C CA . GLN A 1 253 ? 21.147 24.109 10.045 1.00 26.51 ? 253 GLN A CA 1 ATOM 1784 C C . GLN A 1 253 ? 20.445 22.938 10.709 1.00 27.05 ? 253 GLN A C 1 ATOM 1785 O O . GLN A 1 253 ? 19.439 22.443 10.211 1.00 25.66 ? 253 GLN A O 1 ATOM 1786 C CB . GLN A 1 253 ? 21.990 23.599 8.878 1.00 27.76 ? 253 GLN A CB 1 ATOM 1787 C CG . GLN A 1 253 ? 22.688 24.711 8.118 1.00 31.63 ? 253 GLN A CG 1 ATOM 1788 C CD . GLN A 1 253 ? 21.705 25.617 7.407 1.00 32.74 ? 253 GLN A CD 1 ATOM 1789 O OE1 . GLN A 1 253 ? 21.828 26.842 7.444 1.00 34.22 ? 253 GLN A OE1 1 ATOM 1790 N NE2 . GLN A 1 253 ? 20.724 25.015 6.748 1.00 34.39 ? 253 GLN A NE2 1 ATOM 1791 N N . TYR A 1 254 ? 20.975 22.490 11.840 1.00 25.53 ? 254 TYR A N 1 ATOM 1792 C CA . TYR A 1 254 ? 20.375 21.362 12.534 1.00 25.45 ? 254 TYR A CA 1 ATOM 1793 C C . TYR A 1 254 ? 20.245 21.674 14.013 1.00 25.13 ? 254 TYR A C 1 ATOM 1794 O O . TYR A 1 254 ? 21.210 22.078 14.656 1.00 23.48 ? 254 TYR A O 1 ATOM 1795 C CB . TYR A 1 254 ? 21.235 20.112 12.329 1.00 26.35 ? 254 TYR A CB 1 ATOM 1796 C CG . TYR A 1 254 ? 21.503 19.804 10.867 1.00 29.94 ? 254 TYR A CG 1 ATOM 1797 C CD1 . TYR A 1 254 ? 20.563 19.125 10.091 1.00 31.38 ? 254 TYR A CD1 1 ATOM 1798 C CD2 . TYR A 1 254 ? 22.682 20.229 10.251 1.00 29.86 ? 254 TYR A CD2 1 ATOM 1799 C CE1 . TYR A 1 254 ? 20.791 18.878 8.736 1.00 32.61 ? 254 TYR A CE1 1 ATOM 1800 C CE2 . TYR A 1 254 ? 22.919 19.988 8.902 1.00 31.83 ? 254 TYR A CE2 1 ATOM 1801 C CZ . TYR A 1 254 ? 21.970 19.312 8.151 1.00 33.74 ? 254 TYR A CZ 1 ATOM 1802 O OH . TYR A 1 254 ? 22.204 19.069 6.817 1.00 36.90 ? 254 TYR A OH 1 ATOM 1803 N N . CYS A 1 255 ? 19.043 21.486 14.546 1.00 23.20 ? 255 CYS A N 1 ATOM 1804 C CA . CYS A 1 255 ? 18.787 21.747 15.951 1.00 23.50 ? 255 CYS A CA 1 ATOM 1805 C C . CYS A 1 255 ? 18.546 20.460 16.726 1.00 21.24 ? 255 CYS A C 1 ATOM 1806 O O . CYS A 1 255 ? 17.689 19.660 16.363 1.00 21.51 ? 255 CYS A O 1 ATOM 1807 C CB . CYS A 1 255 ? 17.568 22.662 16.114 1.00 24.13 ? 255 CYS A CB 1 ATOM 1808 S SG . CYS A 1 255 ? 17.128 23.003 17.851 1.00 29.72 ? 255 CYS A SG 1 ATOM 1809 N N . ILE A 1 256 ? 19.321 20.268 17.787 1.00 20.26 ? 256 ILE A N 1 ATOM 1810 C CA . ILE A 1 256 ? 19.184 19.108 18.656 1.00 18.19 ? 256 ILE A CA 1 ATOM 1811 C C . ILE A 1 256 ? 18.590 19.676 19.942 1.00 19.79 ? 256 ILE A C 1 ATOM 1812 O O . ILE A 1 256 ? 19.245 20.460 20.635 1.00 17.52 ? 256 ILE A O 1 ATOM 1813 C CB . ILE A 1 256 ? 20.554 18.478 18.965 1.00 17.49 ? 256 ILE A CB 1 ATOM 1814 C CG1 . ILE A 1 256 ? 21.208 18.003 17.667 1.00 17.77 ? 256 ILE A CG1 1 ATOM 1815 C CG2 . ILE A 1 256 ? 20.387 17.321 19.945 1.00 17.39 ? 256 ILE A CG2 1 ATOM 1816 C CD1 . ILE A 1 256 ? 22.672 17.681 17.808 1.00 19.84 ? 256 ILE A CD1 1 ATOM 1817 N N . SER A 1 257 ? 17.353 19.295 20.252 1.00 20.25 ? 257 SER A N 1 ATOM 1818 C CA . SER A 1 257 ? 16.681 19.806 21.446 1.00 20.79 ? 257 SER A CA 1 ATOM 1819 C C . SER A 1 257 ? 16.391 18.735 22.488 1.00 20.96 ? 257 SER A C 1 ATOM 1820 O O . SER A 1 257 ? 16.754 17.569 22.320 1.00 21.34 ? 257 SER A O 1 ATOM 1821 C CB . SER A 1 257 ? 15.358 20.471 21.056 1.00 21.34 ? 257 SER A CB 1 ATOM 1822 O OG . SER A 1 257 ? 14.394 19.492 20.689 1.00 22.80 ? 257 SER A OG 1 ATOM 1823 N N . LYS A 1 258 ? 15.726 19.147 23.565 1.00 19.68 ? 258 LYS A N 1 ATOM 1824 C CA . LYS A 1 258 ? 15.348 18.237 24.642 1.00 20.02 ? 258 LYS A CA 1 ATOM 1825 C C . LYS A 1 258 ? 14.495 17.095 24.097 1.00 20.91 ? 258 LYS A C 1 ATOM 1826 O O . LYS A 1 258 ? 14.424 16.026 24.698 1.00 22.30 ? 258 LYS A O 1 ATOM 1827 C CB . LYS A 1 258 ? 14.531 18.974 25.709 1.00 20.62 ? 258 LYS A CB 1 ATOM 1828 C CG . LYS A 1 258 ? 13.163 19.449 25.202 1.00 21.61 ? 258 LYS A CG 1 ATOM 1829 C CD . LYS A 1 258 ? 12.259 19.991 26.317 1.00 21.59 ? 258 LYS A CD 1 ATOM 1830 C CE . LYS A 1 258 ? 12.860 21.210 26.995 1.00 21.17 ? 258 LYS A CE 1 ATOM 1831 N NZ . LYS A 1 258 ? 13.163 22.301 26.035 1.00 23.49 ? 258 LYS A NZ 1 ATOM 1832 N N . PHE A 1 259 ? 13.832 17.320 22.968 1.00 20.33 ? 259 PHE A N 1 ATOM 1833 C CA . PHE A 1 259 ? 12.980 16.278 22.402 1.00 20.13 ? 259 PHE A CA 1 ATOM 1834 C C . PHE A 1 259 ? 13.782 15.262 21.607 1.00 19.06 ? 259 PHE A C 1 ATOM 1835 O O . PHE A 1 259 ? 13.333 14.142 21.379 1.00 19.03 ? 259 PHE A O 1 ATOM 1836 C CB . PHE A 1 259 ? 11.882 16.902 21.532 1.00 21.99 ? 259 PHE A CB 1 ATOM 1837 C CG . PHE A 1 259 ? 10.906 17.737 22.312 1.00 23.10 ? 259 PHE A CG 1 ATOM 1838 C CD1 . PHE A 1 259 ? 10.097 17.156 23.283 1.00 24.29 ? 259 PHE A CD1 1 ATOM 1839 C CD2 . PHE A 1 259 ? 10.827 19.109 22.111 1.00 25.78 ? 259 PHE A CD2 1 ATOM 1840 C CE1 . PHE A 1 259 ? 9.226 17.930 24.048 1.00 23.61 ? 259 PHE A CE1 1 ATOM 1841 C CE2 . PHE A 1 259 ? 9.963 19.891 22.867 1.00 25.41 ? 259 PHE A CE2 1 ATOM 1842 C CZ . PHE A 1 259 ? 9.161 19.299 23.839 1.00 25.31 ? 259 PHE A CZ 1 ATOM 1843 N N . THR A 1 260 ? 14.983 15.648 21.195 1.00 19.69 ? 260 THR A N 1 ATOM 1844 C CA . THR A 1 260 ? 15.826 14.735 20.447 1.00 17.09 ? 260 THR A CA 1 ATOM 1845 C C . THR A 1 260 ? 16.401 13.693 21.402 1.00 16.60 ? 260 THR A C 1 ATOM 1846 O O . THR A 1 260 ? 17.222 14.015 22.260 1.00 17.61 ? 260 THR A O 1 ATOM 1847 C CB . THR A 1 260 ? 16.988 15.469 19.776 1.00 18.15 ? 260 THR A CB 1 ATOM 1848 O OG1 . THR A 1 260 ? 16.503 16.660 19.139 1.00 18.28 ? 260 THR A OG1 1 ATOM 1849 C CG2 . THR A 1 260 ? 17.638 14.555 18.740 1.00 14.37 ? 260 THR A CG2 1 ATOM 1850 N N . ARG A 1 261 ? 15.965 12.447 21.248 1.00 14.12 ? 261 ARG A N 1 ATOM 1851 C CA . ARG A 1 261 ? 16.440 11.369 22.102 1.00 15.91 ? 261 ARG A CA 1 ATOM 1852 C C . ARG A 1 261 ? 17.307 10.396 21.298 1.00 14.08 ? 261 ARG A C 1 ATOM 1853 O O . ARG A 1 261 ? 17.865 9.450 21.844 1.00 12.61 ? 261 ARG A O 1 ATOM 1854 C CB . ARG A 1 261 ? 15.244 10.648 22.733 1.00 17.17 ? 261 ARG A CB 1 ATOM 1855 C CG . ARG A 1 261 ? 14.303 11.580 23.507 1.00 15.15 ? 261 ARG A CG 1 ATOM 1856 C CD . ARG A 1 261 ? 14.988 12.221 24.723 1.00 15.80 ? 261 ARG A CD 1 ATOM 1857 N NE . ARG A 1 261 ? 15.055 11.316 25.872 1.00 15.44 ? 261 ARG A NE 1 ATOM 1858 C CZ . ARG A 1 261 ? 14.008 11.005 26.637 1.00 16.25 ? 261 ARG A CZ 1 ATOM 1859 N NH1 . ARG A 1 261 ? 12.815 11.530 26.379 1.00 15.79 ? 261 ARG A NH1 1 ATOM 1860 N NH2 . ARG A 1 261 ? 14.148 10.156 27.647 1.00 14.65 ? 261 ARG A NH2 1 ATOM 1861 N N . ILE A 1 262 ? 17.416 10.654 19.997 1.00 13.63 ? 262 ILE A N 1 ATOM 1862 C CA . ILE A 1 262 ? 18.210 9.834 19.092 1.00 15.13 ? 262 ILE A CA 1 ATOM 1863 C C . ILE A 1 262 ? 18.993 10.756 18.174 1.00 15.45 ? 262 ILE A C 1 ATOM 1864 O O . ILE A 1 262 ? 18.410 11.567 17.450 1.00 15.50 ? 262 ILE A O 1 ATOM 1865 C CB . ILE A 1 262 ? 17.313 8.911 18.230 1.00 17.15 ? 262 ILE A CB 1 ATOM 1866 C CG1 . ILE A 1 262 ? 16.570 7.929 19.138 1.00 17.87 ? 262 ILE A CG1 1 ATOM 1867 C CG2 . ILE A 1 262 ? 18.158 8.149 17.212 1.00 13.48 ? 262 ILE A CG2 1 ATOM 1868 C CD1 . ILE A 1 262 ? 15.521 7.130 18.433 1.00 20.24 ? 262 ILE A CD1 1 ATOM 1869 N N . VAL A 1 263 ? 20.316 10.646 18.214 1.00 15.37 ? 263 VAL A N 1 ATOM 1870 C CA . VAL A 1 263 ? 21.157 11.490 17.382 1.00 15.49 ? 263 VAL A CA 1 ATOM 1871 C C . VAL A 1 263 ? 21.932 10.634 16.403 1.00 15.83 ? 263 VAL A C 1 ATOM 1872 O O . VAL A 1 263 ? 22.704 9.753 16.789 1.00 16.54 ? 263 VAL A O 1 ATOM 1873 C CB . VAL A 1 263 ? 22.138 12.320 18.231 1.00 15.50 ? 263 VAL A CB 1 ATOM 1874 C CG1 . VAL A 1 263 ? 22.959 13.233 17.334 1.00 16.70 ? 263 VAL A CG1 1 ATOM 1875 C CG2 . VAL A 1 263 ? 21.365 13.148 19.243 1.00 16.06 ? 263 VAL A CG2 1 ATOM 1876 N N . ILE A 1 264 ? 21.714 10.897 15.124 1.00 16.23 ? 264 ILE A N 1 ATOM 1877 C CA . ILE A 1 264 ? 22.372 10.136 14.087 1.00 15.06 ? 264 ILE A CA 1 ATOM 1878 C C . ILE A 1 264 ? 23.480 10.974 13.461 1.00 15.02 ? 264 ILE A C 1 ATOM 1879 O O . ILE A 1 264 ? 23.221 11.893 12.691 1.00 15.65 ? 264 ILE A O 1 ATOM 1880 C CB . ILE A 1 264 ? 21.346 9.700 13.018 1.00 15.29 ? 264 ILE A CB 1 ATOM 1881 C CG1 . ILE A 1 264 ? 20.211 8.929 13.701 1.00 15.63 ? 264 ILE A CG1 1 ATOM 1882 C CG2 . ILE A 1 264 ? 22.019 8.827 11.961 1.00 13.23 ? 264 ILE A CG2 1 ATOM 1883 C CD1 . ILE A 1 264 ? 18.936 8.861 12.895 1.00 18.53 ? 264 ILE A CD1 1 ATOM 1884 N N . LEU A 1 265 ? 24.715 10.666 13.833 1.00 13.59 ? 265 LEU A N 1 ATOM 1885 C CA . LEU A 1 265 ? 25.869 11.367 13.295 1.00 15.29 ? 265 LEU A CA 1 ATOM 1886 C C . LEU A 1 265 ? 26.384 10.578 12.103 1.00 14.74 ? 265 LEU A C 1 ATOM 1887 O O . LEU A 1 265 ? 26.658 9.381 12.213 1.00 14.35 ? 265 LEU A O 1 ATOM 1888 C CB . LEU A 1 265 ? 26.971 11.480 14.348 1.00 15.41 ? 265 LEU A CB 1 ATOM 1889 C CG . LEU A 1 265 ? 26.570 12.222 15.623 1.00 14.88 ? 265 LEU A CG 1 ATOM 1890 C CD1 . LEU A 1 265 ? 26.069 11.233 16.660 1.00 18.61 ? 265 LEU A CD1 1 ATOM 1891 C CD2 . LEU A 1 265 ? 27.766 12.978 16.161 1.00 17.64 ? 265 LEU A CD2 1 ATOM 1892 N N . GLU A 1 266 ? 26.513 11.248 10.964 1.00 14.57 ? 266 GLU A N 1 ATOM 1893 C CA . GLU A 1 266 ? 26.995 10.587 9.763 1.00 14.78 ? 266 GLU A CA 1 ATOM 1894 C C . GLU A 1 266 ? 28.126 11.388 9.143 1.00 15.34 ? 266 GLU A C 1 ATOM 1895 O O . GLU A 1 266 ? 28.084 12.617 9.106 1.00 13.75 ? 266 GLU A O 1 ATOM 1896 C CB . GLU A 1 266 ? 25.845 10.402 8.767 1.00 15.83 ? 266 GLU A CB 1 ATOM 1897 C CG . GLU A 1 266 ? 25.173 11.687 8.308 1.00 16.84 ? 266 GLU A CG 1 ATOM 1898 C CD . GLU A 1 266 ? 25.769 12.241 7.023 1.00 19.04 ? 266 GLU A CD 1 ATOM 1899 O OE1 . GLU A 1 266 ? 26.743 11.656 6.501 1.00 18.35 ? 266 GLU A OE1 1 ATOM 1900 O OE2 . GLU A 1 266 ? 25.256 13.270 6.536 1.00 21.30 ? 266 GLU A OE2 1 ATOM 1901 N N . GLY A 1 267 ? 29.154 10.690 8.681 1.00 13.72 ? 267 GLY A N 1 ATOM 1902 C CA . GLY A 1 267 ? 30.271 11.384 8.074 1.00 14.04 ? 267 GLY A CA 1 ATOM 1903 C C . GLY A 1 267 ? 31.388 10.467 7.638 1.00 14.30 ? 267 GLY A C 1 ATOM 1904 O O . GLY A 1 267 ? 31.326 9.252 7.810 1.00 15.39 ? 267 GLY A O 1 ATOM 1905 N N . LEU A 1 268 ? 32.429 11.068 7.083 1.00 15.93 ? 268 LEU A N 1 ATOM 1906 C CA . LEU A 1 268 ? 33.579 10.332 6.581 1.00 15.52 ? 268 LEU A CA 1 ATOM 1907 C C . LEU A 1 268 ? 34.533 9.806 7.644 1.00 15.29 ? 268 LEU A C 1 ATOM 1908 O O . LEU A 1 268 ? 34.964 8.648 7.589 1.00 13.27 ? 268 LEU A O 1 ATOM 1909 C CB . LEU A 1 268 ? 34.380 11.229 5.635 1.00 15.74 ? 268 LEU A CB 1 ATOM 1910 C CG . LEU A 1 268 ? 33.743 11.734 4.339 1.00 17.71 ? 268 LEU A CG 1 ATOM 1911 C CD1 . LEU A 1 268 ? 34.524 12.939 3.851 1.00 16.32 ? 268 LEU A CD1 1 ATOM 1912 C CD2 . LEU A 1 268 ? 33.722 10.622 3.281 1.00 15.85 ? 268 LEU A CD2 1 ATOM 1913 N N . TYR A 1 269 ? 34.840 10.655 8.622 1.00 15.98 ? 269 TYR A N 1 ATOM 1914 C CA . TYR A 1 269 ? 35.830 10.324 9.636 1.00 15.61 ? 269 TYR A CA 1 ATOM 1915 C C . TYR A 1 269 ? 35.398 10.098 11.089 1.00 16.76 ? 269 TYR A C 1 ATOM 1916 O O . TYR A 1 269 ? 36.191 10.306 12.008 1.00 17.40 ? 269 TYR A O 1 ATOM 1917 C CB . TYR A 1 269 ? 36.911 11.410 9.572 1.00 17.52 ? 269 TYR A CB 1 ATOM 1918 C CG . TYR A 1 269 ? 37.364 11.704 8.146 1.00 17.70 ? 269 TYR A CG 1 ATOM 1919 C CD1 . TYR A 1 269 ? 37.960 10.713 7.366 1.00 19.09 ? 269 TYR A CD1 1 ATOM 1920 C CD2 . TYR A 1 269 ? 37.161 12.958 7.569 1.00 17.86 ? 269 TYR A CD2 1 ATOM 1921 C CE1 . TYR A 1 269 ? 38.344 10.966 6.038 1.00 20.79 ? 269 TYR A CE1 1 ATOM 1922 C CE2 . TYR A 1 269 ? 37.539 13.220 6.245 1.00 18.69 ? 269 TYR A CE2 1 ATOM 1923 C CZ . TYR A 1 269 ? 38.129 12.218 5.488 1.00 19.74 ? 269 TYR A CZ 1 ATOM 1924 O OH . TYR A 1 269 ? 38.502 12.468 4.181 1.00 20.39 ? 269 TYR A OH 1 ATOM 1925 N N . LEU A 1 270 ? 34.171 9.647 11.312 1.00 14.66 ? 270 LEU A N 1 ATOM 1926 C CA . LEU A 1 270 ? 33.720 9.428 12.681 1.00 15.23 ? 270 LEU A CA 1 ATOM 1927 C C . LEU A 1 270 ? 34.446 8.255 13.342 1.00 16.68 ? 270 LEU A C 1 ATOM 1928 O O . LEU A 1 270 ? 34.443 8.128 14.570 1.00 15.65 ? 270 LEU A O 1 ATOM 1929 C CB . LEU A 1 270 ? 32.205 9.196 12.706 1.00 15.33 ? 270 LEU A CB 1 ATOM 1930 C CG . LEU A 1 270 ? 31.386 10.279 11.989 1.00 16.84 ? 270 LEU A CG 1 ATOM 1931 C CD1 . LEU A 1 270 ? 29.891 10.027 12.204 1.00 16.59 ? 270 LEU A CD1 1 ATOM 1932 C CD2 . LEU A 1 270 ? 31.777 11.655 12.514 1.00 16.67 ? 270 LEU A CD2 1 ATOM 1933 N N . LEU A 1 271 ? 35.078 7.411 12.520 1.00 16.88 ? 271 LEU A N 1 ATOM 1934 C CA . LEU A 1 271 ? 35.809 6.240 13.009 1.00 16.05 ? 271 LEU A CA 1 ATOM 1935 C C . LEU A 1 271 ? 37.267 6.259 12.531 1.00 17.96 ? 271 LEU A C 1 ATOM 1936 O O . LEU A 1 271 ? 37.896 5.206 12.384 1.00 19.68 ? 271 LEU A O 1 ATOM 1937 C CB . LEU A 1 271 ? 35.115 4.952 12.520 1.00 14.69 ? 271 LEU A CB 1 ATOM 1938 C CG . LEU A 1 271 ? 33.665 4.717 12.986 1.00 17.21 ? 271 LEU A CG 1 ATOM 1939 C CD1 . LEU A 1 271 ? 33.054 3.540 12.244 1.00 17.08 ? 271 LEU A CD1 1 ATOM 1940 C CD2 . LEU A 1 271 ? 33.635 4.466 14.494 1.00 14.18 ? 271 LEU A CD2 1 ATOM 1941 N N . TYR A 1 272 ? 37.798 7.462 12.306 1.00 17.02 ? 272 TYR A N 1 ATOM 1942 C CA . TYR A 1 272 ? 39.168 7.649 11.821 1.00 16.57 ? 272 TYR A CA 1 ATOM 1943 C C . TYR A 1 272 ? 40.150 7.644 12.996 1.00 19.20 ? 272 TYR A C 1 ATOM 1944 O O . TYR A 1 272 ? 40.005 8.428 13.944 1.00 17.22 ? 272 TYR A O 1 ATOM 1945 C CB . TYR A 1 272 ? 39.255 8.972 11.059 1.00 15.97 ? 272 TYR A CB 1 ATOM 1946 C CG . TYR A 1 272 ? 40.361 9.045 10.029 1.00 17.31 ? 272 TYR A CG 1 ATOM 1947 C CD1 . TYR A 1 272 ? 40.233 8.414 8.796 1.00 15.80 ? 272 TYR A CD1 1 ATOM 1948 C CD2 . TYR A 1 272 ? 41.523 9.775 10.275 1.00 17.06 ? 272 TYR A CD2 1 ATOM 1949 C CE1 . TYR A 1 272 ? 41.233 8.514 7.824 1.00 18.32 ? 272 TYR A CE1 1 ATOM 1950 C CE2 . TYR A 1 272 ? 42.529 9.877 9.309 1.00 19.13 ? 272 TYR A CE2 1 ATOM 1951 C CZ . TYR A 1 272 ? 42.371 9.245 8.089 1.00 16.14 ? 272 TYR A CZ 1 ATOM 1952 O OH . TYR A 1 272 ? 43.346 9.361 7.123 1.00 21.88 ? 272 TYR A OH 1 ATOM 1953 N N . ASP A 1 273 ? 41.159 6.777 12.922 1.00 20.92 ? 273 ASP A N 1 ATOM 1954 C CA . ASP A 1 273 ? 42.128 6.623 14.010 1.00 22.19 ? 273 ASP A CA 1 ATOM 1955 C C . ASP A 1 273 ? 43.197 7.697 14.192 1.00 22.10 ? 273 ASP A C 1 ATOM 1956 O O . ASP A 1 273 ? 44.250 7.423 14.767 1.00 22.40 ? 273 ASP A O 1 ATOM 1957 C CB . ASP A 1 273 ? 42.824 5.252 13.912 1.00 23.08 ? 273 ASP A CB 1 ATOM 1958 C CG . ASP A 1 273 ? 43.707 5.114 12.670 1.00 25.18 ? 273 ASP A CG 1 ATOM 1959 O OD1 . ASP A 1 273 ? 44.074 6.137 12.056 1.00 23.53 ? 273 ASP A OD1 1 ATOM 1960 O OD2 . ASP A 1 273 ? 44.047 3.966 12.313 1.00 25.87 ? 273 ASP A OD2 1 ATOM 1961 N N . GLN A 1 274 ? 42.928 8.916 13.738 1.00 20.56 ? 274 GLN A N 1 ATOM 1962 C CA . GLN A 1 274 ? 43.901 9.991 13.862 1.00 20.78 ? 274 GLN A CA 1 ATOM 1963 C C . GLN A 1 274 ? 43.399 11.220 14.613 1.00 20.46 ? 274 GLN A C 1 ATOM 1964 O O . GLN A 1 274 ? 42.205 11.530 14.615 1.00 20.35 ? 274 GLN A O 1 ATOM 1965 C CB . GLN A 1 274 ? 44.384 10.419 12.473 1.00 24.08 ? 274 GLN A CB 1 ATOM 1966 C CG . GLN A 1 274 ? 45.157 9.345 11.732 1.00 24.44 ? 274 GLN A CG 1 ATOM 1967 C CD . GLN A 1 274 ? 46.383 8.899 12.499 1.00 25.25 ? 274 GLN A CD 1 ATOM 1968 O OE1 . GLN A 1 274 ? 47.266 9.707 12.808 1.00 28.50 ? 274 GLN A OE1 1 ATOM 1969 N NE2 . GLN A 1 274 ? 46.445 7.612 12.817 1.00 24.82 ? 274 GLN A NE2 1 ATOM 1970 N N . GLU A 1 275 ? 44.340 11.913 15.241 1.00 19.38 ? 275 GLU A N 1 ATOM 1971 C CA . GLU A 1 275 ? 44.079 13.131 15.998 1.00 18.98 ? 275 GLU A CA 1 ATOM 1972 C C . GLU A 1 275 ? 42.746 13.182 16.753 1.00 18.16 ? 275 GLU A C 1 ATOM 1973 O O . GLU A 1 275 ? 42.431 12.290 17.542 1.00 16.33 ? 275 GLU A O 1 ATOM 1974 C CB . GLU A 1 275 ? 44.209 14.352 15.073 1.00 17.75 ? 275 GLU A CB 1 ATOM 1975 C CG . GLU A 1 275 ? 43.478 14.225 13.735 1.00 17.92 ? 275 GLU A CG 1 ATOM 1976 C CD . GLU A 1 275 ? 42.697 15.479 13.388 1.00 17.69 ? 275 GLU A CD 1 ATOM 1977 O OE1 . GLU A 1 275 ? 42.033 16.023 14.297 1.00 16.36 ? 275 GLU A OE1 1 ATOM 1978 O OE2 . GLU A 1 275 ? 42.731 15.916 12.217 1.00 15.59 ? 275 GLU A OE2 1 ATOM 1979 N N . ASN A 1 276 ? 41.962 14.228 16.512 1.00 16.00 ? 276 ASN A N 1 ATOM 1980 C CA . ASN A 1 276 ? 40.691 14.387 17.214 1.00 14.90 ? 276 ASN A CA 1 ATOM 1981 C C . ASN A 1 276 ? 39.629 13.371 16.800 1.00 14.91 ? 276 ASN A C 1 ATOM 1982 O O . ASN A 1 276 ? 38.740 13.049 17.589 1.00 15.54 ? 276 ASN A O 1 ATOM 1983 C CB . ASN A 1 276 ? 40.165 15.810 17.008 1.00 15.13 ? 276 ASN A CB 1 ATOM 1984 C CG . ASN A 1 276 ? 41.055 16.865 17.658 1.00 16.15 ? 276 ASN A CG 1 ATOM 1985 O OD1 . ASN A 1 276 ? 41.205 17.980 17.141 1.00 15.75 ? 276 ASN A OD1 1 ATOM 1986 N ND2 . ASN A 1 276 ? 41.634 16.524 18.800 1.00 13.57 ? 276 ASN A ND2 1 ATOM 1987 N N . TRP A 1 277 ? 39.714 12.865 15.572 1.00 15.54 ? 277 TRP A N 1 ATOM 1988 C CA . TRP A 1 277 ? 38.728 11.890 15.095 1.00 15.92 ? 277 TRP A CA 1 ATOM 1989 C C . TRP A 1 277 ? 38.712 10.635 15.952 1.00 17.28 ? 277 TRP A C 1 ATOM 1990 O O . TRP A 1 277 ? 37.655 10.078 16.242 1.00 19.22 ? 277 TRP A O 1 ATOM 1991 C CB . TRP A 1 277 ? 39.013 11.496 13.650 1.00 13.62 ? 277 TRP A CB 1 ATOM 1992 C CG . TRP A 1 277 ? 39.076 12.653 12.724 1.00 14.71 ? 277 TRP A CG 1 ATOM 1993 C CD1 . TRP A 1 277 ? 40.177 13.108 12.053 1.00 14.20 ? 277 TRP A CD1 1 ATOM 1994 C CD2 . TRP A 1 277 ? 37.993 13.513 12.358 1.00 14.21 ? 277 TRP A CD2 1 ATOM 1995 N NE1 . TRP A 1 277 ? 39.842 14.203 11.289 1.00 17.01 ? 277 TRP A NE1 1 ATOM 1996 C CE2 . TRP A 1 277 ? 38.507 14.470 11.456 1.00 15.17 ? 277 TRP A CE2 1 ATOM 1997 C CE3 . TRP A 1 277 ? 36.633 13.568 12.703 1.00 14.88 ? 277 TRP A CE3 1 ATOM 1998 C CZ2 . TRP A 1 277 ? 37.710 15.472 10.890 1.00 15.95 ? 277 TRP A CZ2 1 ATOM 1999 C CZ3 . TRP A 1 277 ? 35.843 14.562 12.141 1.00 16.51 ? 277 TRP A CZ3 1 ATOM 2000 C CH2 . TRP A 1 277 ? 36.385 15.500 11.243 1.00 16.70 ? 277 TRP A CH2 1 ATOM 2001 N N . LYS A 1 278 ? 39.893 10.196 16.357 1.00 19.68 ? 278 LYS A N 1 ATOM 2002 C CA . LYS A 1 278 ? 40.029 9.002 17.172 1.00 21.72 ? 278 LYS A CA 1 ATOM 2003 C C . LYS A 1 278 ? 39.286 9.119 18.495 1.00 21.83 ? 278 LYS A C 1 ATOM 2004 O O . LYS A 1 278 ? 38.771 8.133 19.008 1.00 24.14 ? 278 LYS A O 1 ATOM 2005 C CB . LYS A 1 278 ? 41.513 8.725 17.424 1.00 23.69 ? 278 LYS A CB 1 ATOM 2006 C CG . LYS A 1 278 ? 41.798 7.421 18.147 1.00 30.62 ? 278 LYS A CG 1 ATOM 2007 C CD . LYS A 1 278 ? 43.297 7.166 18.231 1.00 33.91 ? 278 LYS A CD 1 ATOM 2008 C CE . LYS A 1 278 ? 43.596 5.801 18.841 1.00 38.17 ? 278 LYS A CE 1 ATOM 2009 N NZ . LYS A 1 278 ? 45.059 5.485 18.805 1.00 39.94 ? 278 LYS A NZ 1 ATOM 2010 N N . LYS A 1 279 ? 39.213 10.328 19.041 1.00 20.94 ? 279 LYS A N 1 ATOM 2011 C CA . LYS A 1 279 ? 38.534 10.534 20.312 1.00 21.87 ? 279 LYS A CA 1 ATOM 2012 C C . LYS A 1 279 ? 37.009 10.539 20.211 1.00 22.15 ? 279 LYS A C 1 ATOM 2013 O O . LYS A 1 279 ? 36.317 10.453 21.230 1.00 19.37 ? 279 LYS A O 1 ATOM 2014 C CB . LYS A 1 279 ? 39.025 11.835 20.957 1.00 22.10 ? 279 LYS A CB 1 ATOM 2015 C CG . LYS A 1 279 ? 40.532 11.859 21.177 1.00 24.17 ? 279 LYS A CG 1 ATOM 2016 C CD . LYS A 1 279 ? 41.003 13.207 21.688 1.00 29.13 ? 279 LYS A CD 1 ATOM 2017 C CE . LYS A 1 279 ? 42.521 13.258 21.801 1.00 32.65 ? 279 LYS A CE 1 ATOM 2018 N NZ . LYS A 1 279 ? 43.000 14.602 22.227 1.00 33.03 ? 279 LYS A NZ 1 ATOM 2019 N N . ILE A 1 280 ? 36.486 10.626 18.989 1.00 23.46 ? 280 ILE A N 1 ATOM 2020 C CA . ILE A 1 280 ? 35.037 10.639 18.779 1.00 23.01 ? 280 ILE A CA 1 ATOM 2021 C C . ILE A 1 280 ? 34.340 9.370 19.240 1.00 24.23 ? 280 ILE A C 1 ATOM 2022 O O . ILE A 1 280 ? 33.372 9.431 19.996 1.00 23.30 ? 280 ILE A O 1 ATOM 2023 C CB . ILE A 1 280 ? 34.676 10.846 17.289 1.00 22.87 ? 280 ILE A CB 1 ATOM 2024 C CG1 . ILE A 1 280 ? 35.001 12.276 16.874 1.00 16.52 ? 280 ILE A CG1 1 ATOM 2025 C CG2 . ILE A 1 280 ? 33.195 10.551 17.057 1.00 22.29 ? 280 ILE A CG2 1 ATOM 2026 C CD1 . ILE A 1 280 ? 34.786 12.524 15.397 1.00 21.53 ? 280 ILE A CD1 1 ATOM 2027 N N . TYR A 1 281 ? 34.816 8.224 18.759 1.00 24.28 ? 281 TYR A N 1 ATOM 2028 C CA . TYR A 1 281 ? 34.216 6.949 19.123 1.00 25.23 ? 281 TYR A CA 1 ATOM 2029 C C . TYR A 1 281 ? 34.188 6.762 20.632 1.00 24.14 ? 281 TYR A C 1 ATOM 2030 O O . TYR A 1 281 ? 33.132 6.512 21.211 1.00 24.15 ? 281 TYR A O 1 ATOM 2031 C CB . TYR A 1 281 ? 34.980 5.783 18.478 1.00 24.49 ? 281 TYR A CB 1 ATOM 2032 C CG . TYR A 1 281 ? 34.540 4.423 18.976 1.00 23.85 ? 281 TYR A CG 1 ATOM 2033 C CD1 . TYR A 1 281 ? 33.344 3.849 18.545 1.00 23.26 ? 281 TYR A CD1 1 ATOM 2034 C CD2 . TYR A 1 281 ? 35.298 3.731 19.919 1.00 24.58 ? 281 TYR A CD2 1 ATOM 2035 C CE1 . TYR A 1 281 ? 32.909 2.613 19.049 1.00 24.01 ? 281 TYR A CE1 1 ATOM 2036 C CE2 . TYR A 1 281 ? 34.873 2.502 20.430 1.00 25.42 ? 281 TYR A CE2 1 ATOM 2037 C CZ . TYR A 1 281 ? 33.678 1.951 19.993 1.00 26.71 ? 281 TYR A CZ 1 ATOM 2038 O OH . TYR A 1 281 ? 33.251 0.749 20.517 1.00 27.56 ? 281 TYR A OH 1 ATOM 2039 N N . LYS A 1 282 ? 35.349 6.875 21.268 1.00 24.91 ? 282 LYS A N 1 ATOM 2040 C CA . LYS A 1 282 ? 35.427 6.704 22.713 1.00 24.15 ? 282 LYS A CA 1 ATOM 2041 C C . LYS A 1 282 ? 34.506 7.660 23.461 1.00 21.00 ? 282 LYS A C 1 ATOM 2042 O O . LYS A 1 282 ? 33.857 7.271 24.430 1.00 21.43 ? 282 LYS A O 1 ATOM 2043 C CB . LYS A 1 282 ? 36.861 6.905 23.209 1.00 26.58 ? 282 LYS A CB 1 ATOM 2044 C CG . LYS A 1 282 ? 36.963 6.917 24.724 1.00 29.70 ? 282 LYS A CG 1 ATOM 2045 C CD . LYS A 1 282 ? 38.399 6.834 25.208 1.00 33.24 ? 282 LYS A CD 1 ATOM 2046 C CE . LYS A 1 282 ? 38.449 6.892 26.728 1.00 33.20 ? 282 LYS A CE 1 ATOM 2047 N NZ . LYS A 1 282 ? 37.561 5.867 27.334 1.00 34.26 ? 282 LYS A NZ 1 ATOM 2048 N N . THR A 1 283 ? 34.456 8.909 23.013 1.00 20.20 ? 283 THR A N 1 ATOM 2049 C CA . THR A 1 283 ? 33.616 9.906 23.663 1.00 20.69 ? 283 THR A CA 1 ATOM 2050 C C . THR A 1 283 ? 32.142 9.500 23.637 1.00 19.87 ? 283 THR A C 1 ATOM 2051 O O . THR A 1 283 ? 31.449 9.601 24.648 1.00 17.19 ? 283 THR A O 1 ATOM 2052 C CB . THR A 1 283 ? 33.792 11.281 22.999 1.00 22.81 ? 283 THR A CB 1 ATOM 2053 O OG1 . THR A 1 283 ? 35.169 11.666 23.083 1.00 24.26 ? 283 THR A OG1 1 ATOM 2054 C CG2 . THR A 1 283 ? 32.944 12.330 23.696 1.00 19.59 ? 283 THR A CG2 1 ATOM 2055 N N . LEU A 1 284 ? 31.665 9.028 22.488 1.00 19.53 ? 284 LEU A N 1 ATOM 2056 C CA . LEU A 1 284 ? 30.272 8.605 22.383 1.00 20.06 ? 284 LEU A CA 1 ATOM 2057 C C . LEU A 1 284 ? 30.085 7.189 22.929 1.00 20.37 ? 284 LEU A C 1 ATOM 2058 O O . LEU A 1 284 ? 29.066 6.884 23.553 1.00 19.72 ? 284 LEU A O 1 ATOM 2059 C CB . LEU A 1 284 ? 29.796 8.668 20.923 1.00 20.02 ? 284 LEU A CB 1 ATOM 2060 C CG . LEU A 1 284 ? 29.867 10.041 20.238 1.00 21.86 ? 284 LEU A CG 1 ATOM 2061 C CD1 . LEU A 1 284 ? 29.272 9.939 18.833 1.00 17.72 ? 284 LEU A CD1 1 ATOM 2062 C CD2 . LEU A 1 284 ? 29.115 11.081 21.059 1.00 19.13 ? 284 LEU A CD2 1 ATOM 2063 N N . ALA A 1 285 ? 31.068 6.323 22.695 1.00 20.87 ? 285 ALA A N 1 ATOM 2064 C CA . ALA A 1 285 ? 30.988 4.947 23.177 1.00 21.68 ? 285 ALA A CA 1 ATOM 2065 C C . ALA A 1 285 ? 30.857 4.912 24.699 1.00 22.58 ? 285 ALA A C 1 ATOM 2066 O O . ALA A 1 285 ? 30.036 4.165 25.242 1.00 21.40 ? 285 ALA A O 1 ATOM 2067 C CB . ALA A 1 285 ? 32.221 4.163 22.740 1.00 22.64 ? 285 ALA A CB 1 ATOM 2068 N N . ASP A 1 286 ? 31.646 5.739 25.383 1.00 20.83 ? 286 ASP A N 1 ATOM 2069 C CA . ASP A 1 286 ? 31.613 5.775 26.840 1.00 22.75 ? 286 ASP A CA 1 ATOM 2070 C C . ASP A 1 286 ? 30.258 6.121 27.453 1.00 22.56 ? 286 ASP A C 1 ATOM 2071 O O . ASP A 1 286 ? 30.066 5.951 28.660 1.00 22.23 ? 286 ASP A O 1 ATOM 2072 C CB . ASP A 1 286 ? 32.673 6.737 27.389 1.00 25.02 ? 286 ASP A CB 1 ATOM 2073 C CG . ASP A 1 286 ? 34.095 6.205 27.229 1.00 27.43 ? 286 ASP A CG 1 ATOM 2074 O OD1 . ASP A 1 286 ? 34.271 4.979 27.063 1.00 27.28 ? 286 ASP A OD1 1 ATOM 2075 O OD2 . ASP A 1 286 ? 35.041 7.017 27.286 1.00 28.81 ? 286 ASP A OD2 1 ATOM 2076 N N . THR A 1 287 ? 29.318 6.615 26.651 1.00 21.59 ? 287 THR A N 1 ATOM 2077 C CA . THR A 1 287 ? 28.000 6.933 27.195 1.00 20.05 ? 287 THR A CA 1 ATOM 2078 C C . THR A 1 287 ? 27.267 5.627 27.491 1.00 19.65 ? 287 THR A C 1 ATOM 2079 O O . THR A 1 287 ? 26.363 5.585 28.319 1.00 20.67 ? 287 THR A O 1 ATOM 2080 C CB . THR A 1 287 ? 27.123 7.747 26.204 1.00 19.57 ? 287 THR A CB 1 ATOM 2081 O OG1 . THR A 1 287 ? 26.939 6.995 24.999 1.00 18.71 ? 287 THR A OG1 1 ATOM 2082 C CG2 . THR A 1 287 ? 27.766 9.091 25.885 1.00 20.74 ? 287 THR A CG2 1 ATOM 2083 N N . GLY A 1 288 ? 27.663 4.563 26.800 1.00 21.16 ? 288 GLY A N 1 ATOM 2084 C CA . GLY A 1 288 ? 27.017 3.275 26.982 1.00 19.02 ? 288 GLY A CA 1 ATOM 2085 C C . GLY A 1 288 ? 25.754 3.185 26.140 1.00 19.94 ? 288 GLY A C 1 ATOM 2086 O O . GLY A 1 288 ? 24.959 2.256 26.279 1.00 19.83 ? 288 GLY A O 1 ATOM 2087 N N . ALA A 1 289 ? 25.567 4.155 25.253 1.00 17.14 ? 289 ALA A N 1 ATOM 2088 C CA . ALA A 1 289 ? 24.385 4.179 24.403 1.00 17.32 ? 289 ALA A CA 1 ATOM 2089 C C . ALA A 1 289 ? 24.777 4.588 22.986 1.00 17.08 ? 289 ALA A C 1 ATOM 2090 O O . ALA A 1 289 ? 24.365 5.640 22.493 1.00 17.55 ? 289 ALA A O 1 ATOM 2091 C CB . ALA A 1 289 ? 23.362 5.156 24.972 1.00 15.44 ? 289 ALA A CB 1 ATOM 2092 N N . LEU A 1 290 ? 25.577 3.743 22.342 1.00 16.94 ? 290 LEU A N 1 ATOM 2093 C CA . LEU A 1 290 ? 26.047 4.001 20.988 1.00 16.14 ? 290 LEU A CA 1 ATOM 2094 C C . LEU A 1 290 ? 25.915 2.796 20.062 1.00 15.43 ? 290 LEU A C 1 ATOM 2095 O O . LEU A 1 290 ? 26.231 1.673 20.440 1.00 15.55 ? 290 LEU A O 1 ATOM 2096 C CB . LEU A 1 290 ? 27.522 4.416 21.020 1.00 16.12 ? 290 LEU A CB 1 ATOM 2097 C CG . LEU A 1 290 ? 28.220 4.548 19.661 1.00 16.80 ? 290 LEU A CG 1 ATOM 2098 C CD1 . LEU A 1 290 ? 27.714 5.790 18.950 1.00 14.65 ? 290 LEU A CD1 1 ATOM 2099 C CD2 . LEU A 1 290 ? 29.726 4.626 19.849 1.00 17.71 ? 290 LEU A CD2 1 ATOM 2100 N N . LEU A 1 291 ? 25.427 3.039 18.853 1.00 15.67 ? 291 LEU A N 1 ATOM 2101 C CA . LEU A 1 291 ? 25.335 2.000 17.834 1.00 15.87 ? 291 LEU A CA 1 ATOM 2102 C C . LEU A 1 291 ? 26.277 2.540 16.764 1.00 17.96 ? 291 LEU A C 1 ATOM 2103 O O . LEU A 1 291 ? 26.305 3.747 16.520 1.00 16.77 ? 291 LEU A O 1 ATOM 2104 C CB . LEU A 1 291 ? 23.917 1.867 17.286 1.00 17.33 ? 291 LEU A CB 1 ATOM 2105 C CG . LEU A 1 291 ? 22.984 1.028 18.166 1.00 16.62 ? 291 LEU A CG 1 ATOM 2106 C CD1 . LEU A 1 291 ? 21.590 1.017 17.582 1.00 16.60 ? 291 LEU A CD1 1 ATOM 2107 C CD2 . LEU A 1 291 ? 23.535 -0.389 18.273 1.00 18.36 ? 291 LEU A CD2 1 ATOM 2108 N N . VAL A 1 292 ? 27.061 1.660 16.150 1.00 16.67 ? 292 VAL A N 1 ATOM 2109 C CA . VAL A 1 292 ? 28.031 2.077 15.142 1.00 16.17 ? 292 VAL A CA 1 ATOM 2110 C C . VAL A 1 292 ? 27.892 1.280 13.850 1.00 16.83 ? 292 VAL A C 1 ATOM 2111 O O . VAL A 1 292 ? 27.896 0.046 13.868 1.00 16.91 ? 292 VAL A O 1 ATOM 2112 C CB . VAL A 1 292 ? 29.472 1.907 15.671 1.00 14.22 ? 292 VAL A CB 1 ATOM 2113 C CG1 . VAL A 1 292 ? 30.476 2.403 14.624 1.00 15.61 ? 292 VAL A CG1 1 ATOM 2114 C CG2 . VAL A 1 292 ? 29.641 2.673 16.982 1.00 14.09 ? 292 VAL A CG2 1 ATOM 2115 N N . TYR A 1 293 ? 27.773 1.997 12.734 1.00 17.63 ? 293 TYR A N 1 ATOM 2116 C CA . TYR A 1 293 ? 27.639 1.372 11.421 1.00 18.50 ? 293 TYR A CA 1 ATOM 2117 C C . TYR A 1 293 ? 28.667 1.921 10.455 1.00 19.81 ? 293 TYR A C 1 ATOM 2118 O O . TYR A 1 293 ? 28.987 3.117 10.464 1.00 18.71 ? 293 TYR A O 1 ATOM 2119 C CB . TYR A 1 293 ? 26.251 1.623 10.843 1.00 18.37 ? 293 TYR A CB 1 ATOM 2120 C CG . TYR A 1 293 ? 25.145 1.089 11.711 1.00 19.33 ? 293 TYR A CG 1 ATOM 2121 C CD1 . TYR A 1 293 ? 24.872 -0.279 11.769 1.00 18.17 ? 293 TYR A CD1 1 ATOM 2122 C CD2 . TYR A 1 293 ? 24.387 1.949 12.502 1.00 18.97 ? 293 TYR A CD2 1 ATOM 2123 C CE1 . TYR A 1 293 ? 23.869 -0.773 12.598 1.00 18.52 ? 293 TYR A CE1 1 ATOM 2124 C CE2 . TYR A 1 293 ? 23.387 1.469 13.329 1.00 20.15 ? 293 TYR A CE2 1 ATOM 2125 C CZ . TYR A 1 293 ? 23.129 0.112 13.375 1.00 19.56 ? 293 TYR A CZ 1 ATOM 2126 O OH . TYR A 1 293 ? 22.120 -0.344 14.192 1.00 19.36 ? 293 TYR A OH 1 ATOM 2127 N N . LYS A 1 294 ? 29.182 1.031 9.619 1.00 20.14 ? 294 LYS A N 1 ATOM 2128 C CA . LYS A 1 294 ? 30.171 1.401 8.626 1.00 20.93 ? 294 LYS A CA 1 ATOM 2129 C C . LYS A 1 294 ? 29.702 0.781 7.315 1.00 21.63 ? 294 LYS A C 1 ATOM 2130 O O . LYS A 1 294 ? 29.479 -0.423 7.232 1.00 22.18 ? 294 LYS A O 1 ATOM 2131 C CB . LYS A 1 294 ? 31.546 0.867 9.046 1.00 23.28 ? 294 LYS A CB 1 ATOM 2132 C CG . LYS A 1 294 ? 32.732 1.506 8.333 1.00 23.97 ? 294 LYS A CG 1 ATOM 2133 C CD . LYS A 1 294 ? 32.864 0.986 6.924 1.00 26.30 ? 294 LYS A CD 1 ATOM 2134 C CE . LYS A 1 294 ? 34.095 1.561 6.236 1.00 26.51 ? 294 LYS A CE 1 ATOM 2135 N NZ . LYS A 1 294 ? 34.219 0.989 4.876 1.00 27.27 ? 294 LYS A NZ 1 ATOM 2136 N N . ILE A 1 295 ? 29.527 1.617 6.300 1.00 22.30 ? 295 ILE A N 1 ATOM 2137 C CA . ILE A 1 295 ? 29.067 1.154 4.997 1.00 24.87 ? 295 ILE A CA 1 ATOM 2138 C C . ILE A 1 295 ? 30.187 0.592 4.125 1.00 26.30 ? 295 ILE A C 1 ATOM 2139 O O . ILE A 1 295 ? 31.215 1.236 3.933 1.00 26.09 ? 295 ILE A O 1 ATOM 2140 C CB . ILE A 1 295 ? 28.393 2.301 4.210 1.00 23.54 ? 295 ILE A CB 1 ATOM 2141 C CG1 . ILE A 1 295 ? 27.181 2.824 4.983 1.00 21.38 ? 295 ILE A CG1 1 ATOM 2142 C CG2 . ILE A 1 295 ? 27.987 1.821 2.824 1.00 24.05 ? 295 ILE A CG2 1 ATOM 2143 C CD1 . ILE A 1 295 ? 26.587 4.079 4.382 1.00 22.84 ? 295 ILE A CD1 1 ATOM 2144 N N . ASP A 1 296 ? 29.983 -0.613 3.603 1.00 28.15 ? 296 ASP A N 1 ATOM 2145 C CA . ASP A 1 296 ? 30.959 -1.227 2.712 1.00 30.99 ? 296 ASP A CA 1 ATOM 2146 C C . ASP A 1 296 ? 30.426 -0.954 1.316 1.00 30.61 ? 296 ASP A C 1 ATOM 2147 O O . ASP A 1 296 ? 29.292 -1.311 1.001 1.00 32.84 ? 296 ASP A O 1 ATOM 2148 C CB . ASP A 1 296 ? 31.070 -2.734 2.960 1.00 31.40 ? 296 ASP A CB 1 ATOM 2149 C CG . ASP A 1 296 ? 31.754 -3.061 4.278 1.00 34.22 ? 296 ASP A CG 1 ATOM 2150 O OD1 . ASP A 1 296 ? 32.574 -2.241 4.753 1.00 31.09 ? 296 ASP A OD1 1 ATOM 2151 O OD2 . ASP A 1 296 ? 31.485 -4.149 4.826 1.00 36.28 ? 296 ASP A OD2 1 ATOM 2152 N N . ILE A 1 297 ? 31.241 -0.320 0.482 1.00 31.43 ? 297 ILE A N 1 ATOM 2153 C CA . ILE A 1 297 ? 30.806 0.053 -0.860 1.00 32.94 ? 297 ILE A CA 1 ATOM 2154 C C . ILE A 1 297 ? 31.039 -0.932 -1.995 1.00 32.97 ? 297 ILE A C 1 ATOM 2155 O O . ILE A 1 297 ? 32.000 -1.700 -1.991 1.00 34.68 ? 297 ILE A O 1 ATOM 2156 C CB . ILE A 1 297 ? 31.463 1.380 -1.309 1.00 32.97 ? 297 ILE A CB 1 ATOM 2157 C CG1 . ILE A 1 297 ? 32.972 1.174 -1.477 1.00 33.43 ? 297 ILE A CG1 1 ATOM 2158 C CG2 . ILE A 1 297 ? 31.180 2.477 -0.298 1.00 33.07 ? 297 ILE A CG2 1 ATOM 2159 C CD1 . ILE A 1 297 ? 33.686 2.339 -2.123 1.00 33.47 ? 297 ILE A CD1 1 ATOM 2160 N N . ASP A 1 298 ? 30.131 -0.891 -2.965 1.00 32.87 ? 298 ASP A N 1 ATOM 2161 C CA . ASP A 1 298 ? 30.239 -1.700 -4.170 1.00 34.04 ? 298 ASP A CA 1 ATOM 2162 C C . ASP A 1 298 ? 31.128 -0.784 -5.002 1.00 32.87 ? 298 ASP A C 1 ATOM 2163 O O . ASP A 1 298 ? 30.687 0.278 -5.452 1.00 30.66 ? 298 ASP A O 1 ATOM 2164 C CB . ASP A 1 298 ? 28.866 -1.868 -4.830 1.00 37.46 ? 298 ASP A CB 1 ATOM 2165 C CG . ASP A 1 298 ? 28.936 -2.628 -6.144 1.00 41.02 ? 298 ASP A CG 1 ATOM 2166 O OD1 . ASP A 1 298 ? 29.542 -2.110 -7.108 1.00 42.98 ? 298 ASP A OD1 1 ATOM 2167 O OD2 . ASP A 1 298 ? 28.387 -3.748 -6.213 1.00 43.88 ? 298 ASP A OD2 1 ATOM 2168 N N . TYR A 1 299 ? 32.385 -1.176 -5.175 1.00 31.16 ? 299 TYR A N 1 ATOM 2169 C CA . TYR A 1 299 ? 33.345 -0.359 -5.904 1.00 31.88 ? 299 TYR A CA 1 ATOM 2170 C C . TYR A 1 299 ? 32.870 0.233 -7.229 1.00 32.44 ? 299 TYR A C 1 ATOM 2171 O O . TYR A 1 299 ? 32.844 1.451 -7.391 1.00 29.76 ? 299 TYR A O 1 ATOM 2172 C CB . TYR A 1 299 ? 34.625 -1.147 -6.158 1.00 31.91 ? 299 TYR A CB 1 ATOM 2173 C CG . TYR A 1 299 ? 35.786 -0.266 -6.562 1.00 33.20 ? 299 TYR A CG 1 ATOM 2174 C CD1 . TYR A 1 299 ? 36.590 0.338 -5.599 1.00 31.96 ? 299 TYR A CD1 1 ATOM 2175 C CD2 . TYR A 1 299 ? 36.077 -0.030 -7.909 1.00 34.00 ? 299 TYR A CD2 1 ATOM 2176 C CE1 . TYR A 1 299 ? 37.659 1.149 -5.958 1.00 31.65 ? 299 TYR A CE1 1 ATOM 2177 C CE2 . TYR A 1 299 ? 37.148 0.786 -8.282 1.00 33.38 ? 299 TYR A CE2 1 ATOM 2178 C CZ . TYR A 1 299 ? 37.935 1.367 -7.298 1.00 34.27 ? 299 TYR A CZ 1 ATOM 2179 O OH . TYR A 1 299 ? 39.014 2.143 -7.647 1.00 34.38 ? 299 TYR A OH 1 ATOM 2180 N N . GLU A 1 300 ? 32.515 -0.625 -8.180 1.00 32.54 ? 300 GLU A N 1 ATOM 2181 C CA . GLU A 1 300 ? 32.073 -0.155 -9.488 1.00 34.01 ? 300 GLU A CA 1 ATOM 2182 C C . GLU A 1 300 ? 30.925 0.844 -9.415 1.00 32.09 ? 300 GLU A C 1 ATOM 2183 O O . GLU A 1 300 ? 31.004 1.933 -9.985 1.00 30.58 ? 300 GLU A O 1 ATOM 2184 C CB . GLU A 1 300 ? 31.673 -1.340 -10.372 1.00 37.18 ? 300 GLU A CB 1 ATOM 2185 C CG . GLU A 1 300 ? 32.850 -2.047 -11.025 1.00 44.12 ? 300 GLU A CG 1 ATOM 2186 C CD . GLU A 1 300 ? 33.540 -1.189 -12.075 1.00 48.27 ? 300 GLU A CD 1 ATOM 2187 O OE1 . GLU A 1 300 ? 34.542 -1.651 -12.666 1.00 51.32 ? 300 GLU A OE1 1 ATOM 2188 O OE2 . GLU A 1 300 ? 33.080 -0.053 -12.314 1.00 50.94 ? 300 GLU A OE2 1 ATOM 2189 N N . ALA A 1 301 ? 29.862 0.472 -8.711 1.00 29.84 ? 301 ALA A N 1 ATOM 2190 C CA . ALA A 1 301 ? 28.704 1.340 -8.580 1.00 28.81 ? 301 ALA A CA 1 ATOM 2191 C C . ALA A 1 301 ? 29.082 2.679 -7.958 1.00 28.13 ? 301 ALA A C 1 ATOM 2192 O O . ALA A 1 301 ? 28.596 3.726 -8.383 1.00 27.91 ? 301 ALA A O 1 ATOM 2193 C CB . ALA A 1 301 ? 27.625 0.655 -7.740 1.00 29.27 ? 301 ALA A CB 1 ATOM 2194 N N . THR A 1 302 ? 29.948 2.647 -6.951 1.00 26.57 ? 302 THR A N 1 ATOM 2195 C CA . THR A 1 302 ? 30.364 3.874 -6.282 1.00 25.01 ? 302 THR A CA 1 ATOM 2196 C C . THR A 1 302 ? 31.273 4.717 -7.164 1.00 24.91 ? 302 THR A C 1 ATOM 2197 O O . THR A 1 302 ? 31.176 5.945 -7.175 1.00 23.99 ? 302 THR A O 1 ATOM 2198 C CB . THR A 1 302 ? 31.096 3.568 -4.972 1.00 26.45 ? 302 THR A CB 1 ATOM 2199 O OG1 . THR A 1 302 ? 30.248 2.774 -4.132 1.00 28.21 ? 302 THR A OG1 1 ATOM 2200 C CG2 . THR A 1 302 ? 31.458 4.864 -4.250 1.00 23.15 ? 302 THR A CG2 1 ATOM 2201 N N . GLU A 1 303 ? 32.158 4.051 -7.900 1.00 24.18 ? 303 GLU A N 1 ATOM 2202 C CA . GLU A 1 303 ? 33.077 4.739 -8.801 1.00 25.78 ? 303 GLU A CA 1 ATOM 2203 C C . GLU A 1 303 ? 32.276 5.554 -9.817 1.00 26.25 ? 303 GLU A C 1 ATOM 2204 O O . GLU A 1 303 ? 32.547 6.736 -10.041 1.00 25.22 ? 303 GLU A O 1 ATOM 2205 C CB . GLU A 1 303 ? 33.945 3.725 -9.546 1.00 25.69 ? 303 GLU A CB 1 ATOM 2206 C CG . GLU A 1 303 ? 34.958 4.357 -10.488 1.00 28.61 ? 303 GLU A CG 1 ATOM 2207 C CD . GLU A 1 303 ? 35.636 3.333 -11.373 1.00 30.66 ? 303 GLU A CD 1 ATOM 2208 O OE1 . GLU A 1 303 ? 34.996 2.850 -12.330 1.00 32.11 ? 303 GLU A OE1 1 ATOM 2209 O OE2 . GLU A 1 303 ? 36.803 2.997 -11.103 1.00 32.44 ? 303 GLU A OE2 1 ATOM 2210 N N . GLU A 1 304 ? 31.294 4.904 -10.433 1.00 26.86 ? 304 GLU A N 1 ATOM 2211 C CA . GLU A 1 304 ? 30.448 5.555 -11.423 1.00 29.42 ? 304 GLU A CA 1 ATOM 2212 C C . GLU A 1 304 ? 29.717 6.733 -10.798 1.00 28.13 ? 304 GLU A C 1 ATOM 2213 O O . GLU A 1 304 ? 29.692 7.828 -11.355 1.00 28.94 ? 304 GLU A O 1 ATOM 2214 C CB . GLU A 1 304 ? 29.419 4.568 -11.977 1.00 31.47 ? 304 GLU A CB 1 ATOM 2215 C CG . GLU A 1 304 ? 28.506 5.173 -13.035 1.00 37.06 ? 304 GLU A CG 1 ATOM 2216 C CD . GLU A 1 304 ? 27.378 4.244 -13.438 1.00 41.11 ? 304 GLU A CD 1 ATOM 2217 O OE1 . GLU A 1 304 ? 26.460 4.024 -12.616 1.00 44.92 ? 304 GLU A OE1 1 ATOM 2218 O OE2 . GLU A 1 304 ? 27.410 3.731 -14.575 1.00 43.25 ? 304 GLU A OE2 1 ATOM 2219 N N . ARG A 1 305 ? 29.122 6.492 -9.636 1.00 28.21 ? 305 ARG A N 1 ATOM 2220 C CA . ARG A 1 305 ? 28.368 7.511 -8.921 1.00 28.04 ? 305 ARG A CA 1 ATOM 2221 C C . ARG A 1 305 ? 29.203 8.752 -8.630 1.00 25.91 ? 305 ARG A C 1 ATOM 2222 O O . ARG A 1 305 ? 28.770 9.876 -8.892 1.00 26.11 ? 305 ARG A O 1 ATOM 2223 C CB . ARG A 1 305 ? 27.813 6.926 -7.614 1.00 30.34 ? 305 ARG A CB 1 ATOM 2224 C CG . ARG A 1 305 ? 26.904 7.866 -6.842 1.00 34.61 ? 305 ARG A CG 1 ATOM 2225 C CD . ARG A 1 305 ? 26.235 7.178 -5.653 1.00 36.72 ? 305 ARG A CD 1 ATOM 2226 N NE . ARG A 1 305 ? 25.423 6.029 -6.053 1.00 40.93 ? 305 ARG A NE 1 ATOM 2227 C CZ . ARG A 1 305 ? 25.851 4.768 -6.052 1.00 44.00 ? 305 ARG A CZ 1 ATOM 2228 N NH1 . ARG A 1 305 ? 27.088 4.483 -5.665 1.00 44.27 ? 305 ARG A NH1 1 ATOM 2229 N NH2 . ARG A 1 305 ? 25.042 3.790 -6.441 1.00 46.15 ? 305 ARG A NH2 1 ATOM 2230 N N . VAL A 1 306 ? 30.398 8.553 -8.087 1.00 23.09 ? 306 VAL A N 1 ATOM 2231 C CA . VAL A 1 306 ? 31.274 9.672 -7.769 1.00 21.05 ? 306 VAL A CA 1 ATOM 2232 C C . VAL A 1 306 ? 31.808 10.332 -9.042 1.00 20.44 ? 306 VAL A C 1 ATOM 2233 O O . VAL A 1 306 ? 32.016 11.544 -9.079 1.00 20.13 ? 306 VAL A O 1 ATOM 2234 C CB . VAL A 1 306 ? 32.465 9.222 -6.893 1.00 22.02 ? 306 VAL A CB 1 ATOM 2235 C CG1 . VAL A 1 306 ? 33.438 10.386 -6.694 1.00 25.01 ? 306 VAL A CG1 1 ATOM 2236 C CG2 . VAL A 1 306 ? 31.962 8.743 -5.541 1.00 22.48 ? 306 VAL A CG2 1 ATOM 2237 N N . ALA A 1 307 ? 32.038 9.533 -10.079 1.00 19.74 ? 307 ALA A N 1 ATOM 2238 C CA . ALA A 1 307 ? 32.530 10.069 -11.347 1.00 20.28 ? 307 ALA A CA 1 ATOM 2239 C C . ALA A 1 307 ? 31.474 11.014 -11.920 1.00 22.00 ? 307 ALA A C 1 ATOM 2240 O O . ALA A 1 307 ? 31.786 12.119 -12.353 1.00 22.62 ? 307 ALA A O 1 ATOM 2241 C CB . ALA A 1 307 ? 32.811 8.935 -12.322 1.00 18.69 ? 307 ALA A CB 1 ATOM 2242 N N . LYS A 1 308 ? 30.218 10.577 -11.910 1.00 24.66 ? 308 LYS A N 1 ATOM 2243 C CA . LYS A 1 308 ? 29.128 11.404 -12.425 1.00 26.47 ? 308 LYS A CA 1 ATOM 2244 C C . LYS A 1 308 ? 28.974 12.687 -11.619 1.00 26.86 ? 308 LYS A C 1 ATOM 2245 O O . LYS A 1 308 ? 28.713 13.745 -12.185 1.00 26.60 ? 308 LYS A O 1 ATOM 2246 C CB . LYS A 1 308 ? 27.806 10.641 -12.399 1.00 27.86 ? 308 LYS A CB 1 ATOM 2247 C CG . LYS A 1 308 ? 27.716 9.478 -13.354 1.00 29.10 ? 308 LYS A CG 1 ATOM 2248 C CD . LYS A 1 308 ? 26.303 8.918 -13.330 1.00 33.15 ? 308 LYS A CD 1 ATOM 2249 C CE . LYS A 1 308 ? 26.137 7.740 -14.262 1.00 33.97 ? 308 LYS A CE 1 ATOM 2250 N NZ . LYS A 1 308 ? 24.743 7.217 -14.190 1.00 37.19 ? 308 LYS A NZ 1 ATOM 2251 N N . ARG A 1 309 ? 29.134 12.601 -10.300 1.00 27.95 ? 309 ARG A N 1 ATOM 2252 C CA . ARG A 1 309 ? 29.006 13.789 -9.457 1.00 29.01 ? 309 ARG A CA 1 ATOM 2253 C C . ARG A 1 309 ? 30.036 14.848 -9.822 1.00 27.88 ? 309 ARG A C 1 ATOM 2254 O O . ARG A 1 309 ? 29.715 16.032 -9.930 1.00 28.43 ? 309 ARG A O 1 ATOM 2255 C CB . ARG A 1 309 ? 29.158 13.430 -7.980 1.00 32.13 ? 309 ARG A CB 1 ATOM 2256 C CG . ARG A 1 309 ? 28.009 12.622 -7.421 1.00 35.64 ? 309 ARG A CG 1 ATOM 2257 C CD . ARG A 1 309 ? 28.184 12.429 -5.926 1.00 37.83 ? 309 ARG A CD 1 ATOM 2258 N NE . ARG A 1 309 ? 27.137 11.594 -5.344 1.00 38.79 ? 309 ARG A NE 1 ATOM 2259 C CZ . ARG A 1 309 ? 27.125 11.209 -4.071 1.00 37.54 ? 309 ARG A CZ 1 ATOM 2260 N NH1 . ARG A 1 309 ? 28.104 11.590 -3.258 1.00 35.12 ? 309 ARG A NH1 1 ATOM 2261 N NH2 . ARG A 1 309 ? 26.142 10.443 -3.615 1.00 37.06 ? 309 ARG A NH2 1 ATOM 2262 N N . HIS A 1 310 ? 31.277 14.418 -10.008 1.00 26.64 ? 310 HIS A N 1 ATOM 2263 C CA . HIS A 1 310 ? 32.348 15.329 -10.374 1.00 26.92 ? 310 HIS A CA 1 ATOM 2264 C C . HIS A 1 310 ? 32.106 15.932 -11.752 1.00 26.05 ? 310 HIS A C 1 ATOM 2265 O O . HIS A 1 310 ? 32.481 17.071 -12.009 1.00 23.86 ? 310 HIS A O 1 ATOM 2266 C CB . HIS A 1 310 ? 33.688 14.594 -10.347 1.00 30.74 ? 310 HIS A CB 1 ATOM 2267 C CG . HIS A 1 310 ? 34.166 14.268 -8.966 1.00 35.26 ? 310 HIS A CG 1 ATOM 2268 N ND1 . HIS A 1 310 ? 33.326 13.799 -7.980 1.00 37.93 ? 310 HIS A ND1 1 ATOM 2269 C CD2 . HIS A 1 310 ? 35.395 14.344 -8.407 1.00 37.04 ? 310 HIS A CD2 1 ATOM 2270 C CE1 . HIS A 1 310 ? 34.017 13.603 -6.871 1.00 38.26 ? 310 HIS A CE1 1 ATOM 2271 N NE2 . HIS A 1 310 ? 35.275 13.926 -7.104 1.00 39.58 ? 310 HIS A NE2 1 ATOM 2272 N N . LEU A 1 311 ? 31.486 15.162 -12.643 1.00 26.17 ? 311 LEU A N 1 ATOM 2273 C CA . LEU A 1 311 ? 31.198 15.650 -13.986 1.00 26.19 ? 311 LEU A CA 1 ATOM 2274 C C . LEU A 1 311 ? 30.113 16.718 -13.924 1.00 27.90 ? 311 LEU A C 1 ATOM 2275 O O . LEU A 1 311 ? 30.243 17.782 -14.523 1.00 29.36 ? 311 LEU A O 1 ATOM 2276 C CB . LEU A 1 311 ? 30.739 14.500 -14.891 1.00 24.71 ? 311 LEU A CB 1 ATOM 2277 C CG . LEU A 1 311 ? 30.375 14.892 -16.328 1.00 24.05 ? 311 LEU A CG 1 ATOM 2278 C CD1 . LEU A 1 311 ? 31.601 15.460 -17.032 1.00 23.69 ? 311 LEU A CD1 1 ATOM 2279 C CD2 . LEU A 1 311 ? 29.854 13.678 -17.081 1.00 21.80 ? 311 LEU A CD2 1 ATOM 2280 N N . GLN A 1 312 ? 29.047 16.429 -13.186 1.00 30.55 ? 312 GLN A N 1 ATOM 2281 C CA . GLN A 1 312 ? 27.930 17.355 -13.041 1.00 32.94 ? 312 GLN A CA 1 ATOM 2282 C C . GLN A 1 312 ? 28.367 18.624 -12.314 1.00 34.52 ? 312 GLN A C 1 ATOM 2283 O O . GLN A 1 312 ? 27.768 19.682 -12.486 1.00 33.80 ? 312 GLN A O 1 ATOM 2284 C CB . GLN A 1 312 ? 26.792 16.691 -12.260 1.00 34.69 ? 312 GLN A CB 1 ATOM 2285 C CG . GLN A 1 312 ? 26.412 15.305 -12.760 1.00 40.30 ? 312 GLN A CG 1 ATOM 2286 C CD . GLN A 1 312 ? 25.367 14.631 -11.884 1.00 44.00 ? 312 GLN A CD 1 ATOM 2287 O OE1 . GLN A 1 312 ? 25.356 14.807 -10.662 1.00 46.29 ? 312 GLN A OE1 1 ATOM 2288 N NE2 . GLN A 1 312 ? 24.496 13.837 -12.501 1.00 44.28 ? 312 GLN A NE2 1 ATOM 2289 N N . SER A 1 313 ? 29.412 18.513 -11.503 1.00 35.71 ? 313 SER A N 1 ATOM 2290 C CA . SER A 1 313 ? 29.916 19.651 -10.743 1.00 37.50 ? 313 SER A CA 1 ATOM 2291 C C . SER A 1 313 ? 30.960 20.450 -11.515 1.00 37.72 ? 313 SER A C 1 ATOM 2292 O O . SER A 1 313 ? 31.326 21.548 -11.113 1.00 38.89 ? 313 SER A O 1 ATOM 2293 C CB . SER A 1 313 ? 30.516 19.175 -9.418 1.00 39.12 ? 313 SER A CB 1 ATOM 2294 O OG . SER A 1 313 ? 29.578 18.408 -8.684 1.00 40.49 ? 313 SER A OG 1 ATOM 2295 N N . GLY A 1 314 ? 31.446 19.894 -12.618 1.00 38.22 ? 314 GLY A N 1 ATOM 2296 C CA . GLY A 1 314 ? 32.433 20.600 -13.416 1.00 37.29 ? 314 GLY A CA 1 ATOM 2297 C C . GLY A 1 314 ? 33.886 20.288 -13.113 1.00 37.21 ? 314 GLY A C 1 ATOM 2298 O O . GLY A 1 314 ? 34.777 20.783 -13.801 1.00 37.53 ? 314 GLY A O 1 ATOM 2299 N N . LEU A 1 315 ? 34.136 19.469 -12.095 1.00 37.57 ? 315 LEU A N 1 ATOM 2300 C CA . LEU A 1 315 ? 35.505 19.112 -11.724 1.00 37.60 ? 315 LEU A CA 1 ATOM 2301 C C . LEU A 1 315 ? 36.253 18.394 -12.844 1.00 36.48 ? 315 LEU A C 1 ATOM 2302 O O . LEU A 1 315 ? 37.476 18.484 -12.936 1.00 38.03 ? 315 LEU A O 1 ATOM 2303 C CB . LEU A 1 315 ? 35.506 18.234 -10.467 1.00 40.43 ? 315 LEU A CB 1 ATOM 2304 C CG . LEU A 1 315 ? 35.191 18.901 -9.123 1.00 42.85 ? 315 LEU A CG 1 ATOM 2305 C CD1 . LEU A 1 315 ? 33.819 19.555 -9.157 1.00 44.53 ? 315 LEU A CD1 1 ATOM 2306 C CD2 . LEU A 1 315 ? 35.252 17.855 -8.020 1.00 44.77 ? 315 LEU A CD2 1 ATOM 2307 N N . VAL A 1 316 ? 35.519 17.673 -13.685 1.00 34.14 ? 316 VAL A N 1 ATOM 2308 C CA . VAL A 1 316 ? 36.120 16.948 -14.801 1.00 31.17 ? 316 VAL A CA 1 ATOM 2309 C C . VAL A 1 316 ? 35.318 17.219 -16.071 1.00 29.05 ? 316 VAL A C 1 ATOM 2310 O O . VAL A 1 316 ? 34.168 17.639 -15.998 1.00 29.13 ? 316 VAL A O 1 ATOM 2311 C CB . VAL A 1 316 ? 36.157 15.426 -14.525 1.00 30.07 ? 316 VAL A CB 1 ATOM 2312 C CG1 . VAL A 1 316 ? 37.021 15.145 -13.294 1.00 30.83 ? 316 VAL A CG1 1 ATOM 2313 C CG2 . VAL A 1 316 ? 34.747 14.897 -14.314 1.00 24.93 ? 316 VAL A CG2 1 ATOM 2314 N N . THR A 1 317 ? 35.918 16.980 -17.233 1.00 29.00 ? 317 THR A N 1 ATOM 2315 C CA . THR A 1 317 ? 35.216 17.234 -18.489 1.00 28.05 ? 317 THR A CA 1 ATOM 2316 C C . THR A 1 317 ? 34.511 16.007 -19.060 1.00 25.86 ? 317 THR A C 1 ATOM 2317 O O . THR A 1 317 ? 33.619 16.139 -19.896 1.00 26.56 ? 317 THR A O 1 ATOM 2318 C CB . THR A 1 317 ? 36.171 17.794 -19.565 1.00 28.71 ? 317 THR A CB 1 ATOM 2319 O OG1 . THR A 1 317 ? 37.036 16.753 -20.036 1.00 30.20 ? 317 THR A OG1 1 ATOM 2320 C CG2 . THR A 1 317 ? 37.005 18.924 -18.987 1.00 26.77 ? 317 THR A CG2 1 ATOM 2321 N N . THR A 1 318 ? 34.913 14.822 -18.610 1.00 23.85 ? 318 THR A N 1 ATOM 2322 C CA . THR A 1 318 ? 34.311 13.574 -19.077 1.00 23.86 ? 318 THR A CA 1 ATOM 2323 C C . THR A 1 318 ? 34.192 12.595 -17.918 1.00 24.18 ? 318 THR A C 1 ATOM 2324 O O . THR A 1 318 ? 34.877 12.739 -16.902 1.00 25.40 ? 318 THR A O 1 ATOM 2325 C CB . THR A 1 318 ? 35.164 12.881 -20.152 1.00 23.88 ? 318 THR A CB 1 ATOM 2326 O OG1 . THR A 1 318 ? 36.413 12.493 -19.570 1.00 21.71 ? 318 THR A OG1 1 ATOM 2327 C CG2 . THR A 1 318 ? 35.413 13.804 -21.350 1.00 23.33 ? 318 THR A CG2 1 ATOM 2328 N N . ILE A 1 319 ? 33.341 11.589 -18.079 1.00 23.11 ? 319 ILE A N 1 ATOM 2329 C CA . ILE A 1 319 ? 33.150 10.582 -17.037 1.00 22.50 ? 319 ILE A CA 1 ATOM 2330 C C . ILE A 1 319 ? 34.448 9.778 -16.834 1.00 21.54 ? 319 ILE A C 1 ATOM 2331 O O . ILE A 1 319 ? 34.753 9.353 -15.717 1.00 19.78 ? 319 ILE A O 1 ATOM 2332 C CB . ILE A 1 319 ? 31.970 9.629 -17.404 1.00 22.97 ? 319 ILE A CB 1 ATOM 2333 C CG1 . ILE A 1 319 ? 31.570 8.781 -16.196 1.00 23.10 ? 319 ILE A CG1 1 ATOM 2334 C CG2 . ILE A 1 319 ? 32.353 8.740 -18.563 1.00 20.02 ? 319 ILE A CG2 1 ATOM 2335 C CD1 . ILE A 1 319 ? 30.725 9.526 -15.191 1.00 27.95 ? 319 ILE A CD1 1 ATOM 2336 N N . ALA A 1 320 ? 35.213 9.583 -17.908 1.00 19.89 ? 320 ALA A N 1 ATOM 2337 C CA . ALA A 1 320 ? 36.477 8.847 -17.825 1.00 21.19 ? 320 ALA A CA 1 ATOM 2338 C C . ALA A 1 320 ? 37.446 9.540 -16.860 1.00 20.36 ? 320 ALA A C 1 ATOM 2339 O O . ALA A 1 320 ? 38.125 8.889 -16.064 1.00 21.03 ? 320 ALA A O 1 ATOM 2340 C CB . ALA A 1 320 ? 37.117 8.729 -19.208 1.00 21.10 ? 320 ALA A CB 1 ATOM 2341 N N . GLU A 1 321 ? 37.516 10.862 -16.940 1.00 21.61 ? 321 GLU A N 1 ATOM 2342 C CA . GLU A 1 321 ? 38.385 11.619 -16.052 1.00 22.10 ? 321 GLU A CA 1 ATOM 2343 C C . GLU A 1 321 ? 37.875 11.456 -14.620 1.00 22.18 ? 321 GLU A C 1 ATOM 2344 O O . GLU A 1 321 ? 38.658 11.297 -13.680 1.00 21.66 ? 321 GLU A O 1 ATOM 2345 C CB . GLU A 1 321 ? 38.387 13.089 -16.461 1.00 24.58 ? 321 GLU A CB 1 ATOM 2346 C CG . GLU A 1 321 ? 39.252 13.378 -17.683 1.00 28.50 ? 321 GLU A CG 1 ATOM 2347 C CD . GLU A 1 321 ? 38.868 14.665 -18.383 1.00 30.46 ? 321 GLU A CD 1 ATOM 2348 O OE1 . GLU A 1 321 ? 38.536 15.647 -17.690 1.00 35.98 ? 321 GLU A OE1 1 ATOM 2349 O OE2 . GLU A 1 321 ? 38.904 14.699 -19.628 1.00 35.83 ? 321 GLU A OE2 1 ATOM 2350 N N . GLY A 1 322 ? 36.554 11.480 -14.467 1.00 21.15 ? 322 GLY A N 1 ATOM 2351 C CA . GLY A 1 322 ? 35.957 11.319 -13.154 1.00 21.54 ? 322 GLY A CA 1 ATOM 2352 C C . GLY A 1 322 ? 36.335 9.989 -12.534 1.00 21.74 ? 322 GLY A C 1 ATOM 2353 O O . GLY A 1 322 ? 36.653 9.926 -11.349 1.00 21.58 ? 322 GLY A O 1 ATOM 2354 N N . ARG A 1 323 ? 36.305 8.925 -13.334 1.00 22.26 ? 323 ARG A N 1 ATOM 2355 C CA . ARG A 1 323 ? 36.646 7.586 -12.854 1.00 24.87 ? 323 ARG A CA 1 ATOM 2356 C C . ARG A 1 323 ? 38.109 7.473 -12.429 1.00 25.66 ? 323 ARG A C 1 ATOM 2357 O O . ARG A 1 323 ? 38.421 6.885 -11.395 1.00 25.81 ? 323 ARG A O 1 ATOM 2358 C CB . ARG A 1 323 ? 36.362 6.537 -13.940 1.00 24.98 ? 323 ARG A CB 1 ATOM 2359 C CG . ARG A 1 323 ? 34.892 6.358 -14.298 1.00 25.27 ? 323 ARG A CG 1 ATOM 2360 C CD . ARG A 1 323 ? 34.739 5.398 -15.482 1.00 29.80 ? 323 ARG A CD 1 ATOM 2361 N NE . ARG A 1 323 ? 33.343 5.136 -15.829 1.00 31.75 ? 323 ARG A NE 1 ATOM 2362 C CZ . ARG A 1 323 ? 32.495 4.449 -15.068 1.00 34.85 ? 323 ARG A CZ 1 ATOM 2363 N NH1 . ARG A 1 323 ? 32.893 3.945 -13.905 1.00 34.79 ? 323 ARG A NH1 1 ATOM 2364 N NH2 . ARG A 1 323 ? 31.244 4.263 -15.468 1.00 35.65 ? 323 ARG A NH2 1 ATOM 2365 N N . GLU A 1 324 ? 39.007 8.021 -13.238 1.00 29.32 ? 324 GLU A N 1 ATOM 2366 C CA . GLU A 1 324 ? 40.429 7.961 -12.928 1.00 31.84 ? 324 GLU A CA 1 ATOM 2367 C C . GLU A 1 324 ? 40.714 8.717 -11.643 1.00 32.61 ? 324 GLU A C 1 ATOM 2368 O O . GLU A 1 324 ? 41.543 8.296 -10.839 1.00 33.44 ? 324 GLU A O 1 ATOM 2369 C CB . GLU A 1 324 ? 41.254 8.554 -14.071 1.00 34.87 ? 324 GLU A CB 1 ATOM 2370 C CG . GLU A 1 324 ? 42.761 8.534 -13.815 1.00 42.41 ? 324 GLU A CG 1 ATOM 2371 C CD . GLU A 1 324 ? 43.275 7.149 -13.439 1.00 45.95 ? 324 GLU A CD 1 ATOM 2372 O OE1 . GLU A 1 324 ? 43.108 6.208 -14.248 1.00 48.41 ? 324 GLU A OE1 1 ATOM 2373 O OE2 . GLU A 1 324 ? 43.846 7.000 -12.336 1.00 46.13 ? 324 GLU A OE2 1 ATOM 2374 N N . LYS A 1 325 ? 40.017 9.834 -11.456 1.00 31.17 ? 325 LYS A N 1 ATOM 2375 C CA . LYS A 1 325 ? 40.177 10.654 -10.263 1.00 31.73 ? 325 LYS A CA 1 ATOM 2376 C C . LYS A 1 325 ? 39.776 9.849 -9.029 1.00 28.40 ? 325 LYS A C 1 ATOM 2377 O O . LYS A 1 325 ? 40.408 9.936 -7.979 1.00 28.63 ? 325 LYS A O 1 ATOM 2378 C CB . LYS A 1 325 ? 39.306 11.907 -10.380 1.00 34.40 ? 325 LYS A CB 1 ATOM 2379 C CG . LYS A 1 325 ? 39.343 12.810 -9.171 1.00 39.60 ? 325 LYS A CG 1 ATOM 2380 C CD . LYS A 1 325 ? 38.531 14.069 -9.404 1.00 44.01 ? 325 LYS A CD 1 ATOM 2381 C CE . LYS A 1 325 ? 38.565 14.974 -8.184 1.00 47.04 ? 325 LYS A CE 1 ATOM 2382 N NZ . LYS A 1 325 ? 37.748 16.199 -8.396 1.00 49.89 ? 325 LYS A NZ 1 ATOM 2383 N N . PHE A 1 326 ? 38.721 9.061 -9.173 1.00 26.38 ? 326 PHE A N 1 ATOM 2384 C CA . PHE A 1 326 ? 38.222 8.228 -8.088 1.00 25.84 ? 326 PHE A CA 1 ATOM 2385 C C . PHE A 1 326 ? 39.238 7.135 -7.766 1.00 26.90 ? 326 PHE A C 1 ATOM 2386 O O . PHE A 1 326 ? 39.586 6.912 -6.606 1.00 25.89 ? 326 PHE A O 1 ATOM 2387 C CB . PHE A 1 326 ? 36.899 7.590 -8.512 1.00 25.22 ? 326 PHE A CB 1 ATOM 2388 C CG . PHE A 1 326 ? 36.298 6.670 -7.484 1.00 26.36 ? 326 PHE A CG 1 ATOM 2389 C CD1 . PHE A 1 326 ? 35.528 7.176 -6.439 1.00 25.43 ? 326 PHE A CD1 1 ATOM 2390 C CD2 . PHE A 1 326 ? 36.474 5.289 -7.582 1.00 24.98 ? 326 PHE A CD2 1 ATOM 2391 C CE1 . PHE A 1 326 ? 34.937 6.320 -5.511 1.00 24.68 ? 326 PHE A CE1 1 ATOM 2392 C CE2 . PHE A 1 326 ? 35.889 4.428 -6.660 1.00 25.72 ? 326 PHE A CE2 1 ATOM 2393 C CZ . PHE A 1 326 ? 35.117 4.944 -5.622 1.00 24.55 ? 326 PHE A CZ 1 ATOM 2394 N N . ARG A 1 327 ? 39.717 6.463 -8.808 1.00 28.18 ? 327 ARG A N 1 ATOM 2395 C CA . ARG A 1 327 ? 40.672 5.371 -8.656 1.00 30.14 ? 327 ARG A CA 1 ATOM 2396 C C . ARG A 1 327 ? 42.018 5.769 -8.053 1.00 29.73 ? 327 ARG A C 1 ATOM 2397 O O . ARG A 1 327 ? 42.604 5.004 -7.284 1.00 29.47 ? 327 ARG A O 1 ATOM 2398 C CB . ARG A 1 327 ? 40.899 4.689 -10.011 1.00 31.33 ? 327 ARG A CB 1 ATOM 2399 C CG . ARG A 1 327 ? 39.647 4.026 -10.574 1.00 34.89 ? 327 ARG A CG 1 ATOM 2400 C CD . ARG A 1 327 ? 39.893 3.359 -11.925 1.00 38.12 ? 327 ARG A CD 1 ATOM 2401 N NE . ARG A 1 327 ? 40.377 4.301 -12.935 1.00 43.29 ? 327 ARG A NE 1 ATOM 2402 C CZ . ARG A 1 327 ? 40.516 4.011 -14.228 1.00 45.22 ? 327 ARG A CZ 1 ATOM 2403 N NH1 . ARG A 1 327 ? 40.204 2.801 -14.677 1.00 46.69 ? 327 ARG A NH1 1 ATOM 2404 N NH2 . ARG A 1 327 ? 40.976 4.928 -15.073 1.00 43.39 ? 327 ARG A NH2 1 ATOM 2405 N N . SER A 1 328 ? 42.504 6.960 -8.390 1.00 28.13 ? 328 SER A N 1 ATOM 2406 C CA . SER A 1 328 ? 43.793 7.406 -7.885 1.00 29.76 ? 328 SER A CA 1 ATOM 2407 C C . SER A 1 328 ? 43.743 8.223 -6.594 1.00 29.51 ? 328 SER A C 1 ATOM 2408 O O . SER A 1 328 ? 44.786 8.487 -5.998 1.00 29.98 ? 328 SER A O 1 ATOM 2409 C CB . SER A 1 328 ? 44.524 8.207 -8.964 1.00 31.92 ? 328 SER A CB 1 ATOM 2410 O OG . SER A 1 328 ? 43.827 9.398 -9.273 1.00 32.22 ? 328 SER A OG 1 ATOM 2411 N N . ASN A 1 329 ? 42.546 8.623 -6.166 1.00 28.26 ? 329 ASN A N 1 ATOM 2412 C CA . ASN A 1 329 ? 42.399 9.410 -4.942 1.00 26.37 ? 329 ASN A CA 1 ATOM 2413 C C . ASN A 1 329 ? 41.830 8.560 -3.804 1.00 26.34 ? 329 ASN A C 1 ATOM 2414 O O . ASN A 1 329 ? 40.622 8.328 -3.739 1.00 24.53 ? 329 ASN A O 1 ATOM 2415 C CB . ASN A 1 329 ? 41.476 10.605 -5.185 1.00 27.32 ? 329 ASN A CB 1 ATOM 2416 C CG . ASN A 1 329 ? 41.532 11.624 -4.057 1.00 29.06 ? 329 ASN A CG 1 ATOM 2417 O OD1 . ASN A 1 329 ? 41.812 11.280 -2.909 1.00 27.99 ? 329 ASN A OD1 1 ATOM 2418 N ND2 . ASN A 1 329 ? 41.252 12.880 -4.378 1.00 27.32 ? 329 ASN A ND2 1 ATOM 2419 N N . ASP A 1 330 ? 42.699 8.110 -2.902 1.00 26.20 ? 330 ASP A N 1 ATOM 2420 C CA . ASP A 1 330 ? 42.267 7.281 -1.782 1.00 28.61 ? 330 ASP A CA 1 ATOM 2421 C C . ASP A 1 330 ? 41.295 7.963 -0.827 1.00 29.63 ? 330 ASP A C 1 ATOM 2422 O O . ASP A 1 330 ? 40.776 7.325 0.088 1.00 30.04 ? 330 ASP A O 1 ATOM 2423 C CB . ASP A 1 330 ? 43.473 6.765 -0.994 1.00 28.75 ? 330 ASP A CB 1 ATOM 2424 C CG . ASP A 1 330 ? 44.249 5.703 -1.747 1.00 30.17 ? 330 ASP A CG 1 ATOM 2425 O OD1 . ASP A 1 330 ? 43.688 5.105 -2.690 1.00 31.79 ? 330 ASP A OD1 1 ATOM 2426 O OD2 . ASP A 1 330 ? 45.416 5.455 -1.387 1.00 31.17 ? 330 ASP A OD2 1 ATOM 2427 N N . LEU A 1 331 ? 41.060 9.257 -1.019 1.00 30.58 ? 331 LEU A N 1 ATOM 2428 C CA . LEU A 1 331 ? 40.115 9.974 -0.170 1.00 30.24 ? 331 LEU A CA 1 ATOM 2429 C C . LEU A 1 331 ? 38.727 9.776 -0.772 1.00 31.29 ? 331 LEU A C 1 ATOM 2430 O O . LEU A 1 331 ? 37.713 9.853 -0.077 1.00 31.33 ? 331 LEU A O 1 ATOM 2431 C CB . LEU A 1 331 ? 40.449 11.468 -0.122 1.00 32.14 ? 331 LEU A CB 1 ATOM 2432 C CG . LEU A 1 331 ? 41.706 11.911 0.630 1.00 32.09 ? 331 LEU A CG 1 ATOM 2433 C CD1 . LEU A 1 331 ? 41.881 13.420 0.485 1.00 34.38 ? 331 LEU A CD1 1 ATOM 2434 C CD2 . LEU A 1 331 ? 41.593 11.526 2.103 1.00 33.11 ? 331 LEU A CD2 1 ATOM 2435 N N . LEU A 1 332 ? 38.697 9.498 -2.073 1.00 29.09 ? 332 LEU A N 1 ATOM 2436 C CA . LEU A 1 332 ? 37.445 9.294 -2.787 1.00 27.91 ? 332 LEU A CA 1 ATOM 2437 C C . LEU A 1 332 ? 37.016 7.837 -2.874 1.00 26.44 ? 332 LEU A C 1 ATOM 2438 O O . LEU A 1 332 ? 35.833 7.531 -2.730 1.00 26.17 ? 332 LEU A O 1 ATOM 2439 C CB . LEU A 1 332 ? 37.545 9.859 -4.208 1.00 27.96 ? 332 LEU A CB 1 ATOM 2440 C CG . LEU A 1 332 ? 37.711 11.366 -4.406 1.00 28.26 ? 332 LEU A CG 1 ATOM 2441 C CD1 . LEU A 1 332 ? 37.852 11.657 -5.900 1.00 27.72 ? 332 LEU A CD1 1 ATOM 2442 C CD2 . LEU A 1 332 ? 36.509 12.109 -3.829 1.00 28.33 ? 332 LEU A CD2 1 ATOM 2443 N N . ASN A 1 333 ? 37.968 6.938 -3.121 1.00 25.78 ? 333 ASN A N 1 ATOM 2444 C CA . ASN A 1 333 ? 37.639 5.522 -3.247 1.00 26.06 ? 333 ASN A CA 1 ATOM 2445 C C . ASN A 1 333 ? 37.441 4.811 -1.911 1.00 24.96 ? 333 ASN A C 1 ATOM 2446 O O . ASN A 1 333 ? 37.096 3.632 -1.880 1.00 24.79 ? 333 ASN A O 1 ATOM 2447 C CB . ASN A 1 333 ? 38.693 4.781 -4.091 1.00 26.10 ? 333 ASN A CB 1 ATOM 2448 C CG . ASN A 1 333 ? 40.106 4.968 -3.574 1.00 26.14 ? 333 ASN A CG 1 ATOM 2449 O OD1 . ASN A 1 333 ? 40.360 4.881 -2.372 1.00 25.49 ? 333 ASN A OD1 1 ATOM 2450 N ND2 . ASN A 1 333 ? 41.037 5.212 -4.486 1.00 22.57 ? 333 ASN A ND2 1 ATOM 2451 N N . GLY A 1 334 ? 37.660 5.533 -0.817 1.00 25.84 ? 334 GLY A N 1 ATOM 2452 C CA . GLY A 1 334 ? 37.460 4.963 0.504 1.00 26.52 ? 334 GLY A CA 1 ATOM 2453 C C . GLY A 1 334 ? 38.623 4.225 1.140 1.00 27.30 ? 334 GLY A C 1 ATOM 2454 O O . GLY A 1 334 ? 38.534 3.815 2.301 1.00 26.06 ? 334 GLY A O 1 ATOM 2455 N N . ARG A 1 335 ? 39.714 4.051 0.402 1.00 26.93 ? 335 ARG A N 1 ATOM 2456 C CA . ARG A 1 335 ? 40.871 3.343 0.942 1.00 27.17 ? 335 ARG A CA 1 ATOM 2457 C C . ARG A 1 335 ? 41.452 3.988 2.195 1.00 24.58 ? 335 ARG A C 1 ATOM 2458 O O . ARG A 1 335 ? 41.838 3.293 3.131 1.00 23.83 ? 335 ARG A O 1 ATOM 2459 C CB . ARG A 1 335 ? 41.956 3.217 -0.128 1.00 29.72 ? 335 ARG A CB 1 ATOM 2460 C CG . ARG A 1 335 ? 41.525 2.331 -1.282 1.00 36.83 ? 335 ARG A CG 1 ATOM 2461 C CD . ARG A 1 335 ? 42.640 2.090 -2.282 1.00 39.74 ? 335 ARG A CD 1 ATOM 2462 N NE . ARG A 1 335 ? 42.165 1.264 -3.387 1.00 44.64 ? 335 ARG A NE 1 ATOM 2463 C CZ . ARG A 1 335 ? 42.945 0.761 -4.336 1.00 47.07 ? 335 ARG A CZ 1 ATOM 2464 N NH1 . ARG A 1 335 ? 44.251 0.999 -4.319 1.00 46.94 ? 335 ARG A NH1 1 ATOM 2465 N NH2 . ARG A 1 335 ? 42.416 0.015 -5.301 1.00 47.50 ? 335 ARG A NH2 1 ATOM 2466 N N . ASP A 1 336 ? 41.512 5.313 2.218 1.00 24.72 ? 336 ASP A N 1 ATOM 2467 C CA . ASP A 1 336 ? 42.057 6.011 3.374 1.00 23.60 ? 336 ASP A CA 1 ATOM 2468 C C . ASP A 1 336 ? 41.243 5.669 4.621 1.00 23.19 ? 336 ASP A C 1 ATOM 2469 O O . ASP A 1 336 ? 41.799 5.312 5.660 1.00 22.87 ? 336 ASP A O 1 ATOM 2470 C CB . ASP A 1 336 ? 42.043 7.516 3.135 1.00 28.86 ? 336 ASP A CB 1 ATOM 2471 C CG . ASP A 1 336 ? 42.853 8.273 4.165 1.00 33.40 ? 336 ASP A CG 1 ATOM 2472 O OD1 . ASP A 1 336 ? 44.088 8.089 4.198 1.00 37.16 ? 336 ASP A OD1 1 ATOM 2473 O OD2 . ASP A 1 336 ? 42.260 9.047 4.943 1.00 36.73 ? 336 ASP A OD2 1 ATOM 2474 N N . ILE A 1 337 ? 39.924 5.775 4.502 1.00 21.03 ? 337 ILE A N 1 ATOM 2475 C CA . ILE A 1 337 ? 39.007 5.468 5.597 1.00 21.06 ? 337 ILE A CA 1 ATOM 2476 C C . ILE A 1 337 ? 39.137 4.020 6.087 1.00 20.87 ? 337 ILE A C 1 ATOM 2477 O O . ILE A 1 337 ? 39.163 3.773 7.294 1.00 20.48 ? 337 ILE A O 1 ATOM 2478 C CB . ILE A 1 337 ? 37.543 5.738 5.166 1.00 19.99 ? 337 ILE A CB 1 ATOM 2479 C CG1 . ILE A 1 337 ? 37.331 7.247 4.995 1.00 19.16 ? 337 ILE A CG1 1 ATOM 2480 C CG2 . ILE A 1 337 ? 36.574 5.141 6.173 1.00 19.31 ? 337 ILE A CG2 1 ATOM 2481 C CD1 . ILE A 1 337 ? 35.972 7.621 4.428 1.00 20.84 ? 337 ILE A CD1 1 ATOM 2482 N N . ASP A 1 338 ? 39.210 3.065 5.162 1.00 20.03 ? 338 ASP A N 1 ATOM 2483 C CA . ASP A 1 338 ? 39.345 1.662 5.554 1.00 22.10 ? 338 ASP A CA 1 ATOM 2484 C C . ASP A 1 338 ? 40.689 1.398 6.225 1.00 22.37 ? 338 ASP A C 1 ATOM 2485 O O . ASP A 1 338 ? 40.775 0.607 7.163 1.00 22.96 ? 338 ASP A O 1 ATOM 2486 C CB . ASP A 1 338 ? 39.197 0.727 4.344 1.00 24.90 ? 338 ASP A CB 1 ATOM 2487 C CG . ASP A 1 338 ? 37.771 0.665 3.819 1.00 28.30 ? 338 ASP A CG 1 ATOM 2488 O OD1 . ASP A 1 338 ? 36.834 0.924 4.603 1.00 30.38 ? 338 ASP A OD1 1 ATOM 2489 O OD2 . ASP A 1 338 ? 37.582 0.342 2.625 1.00 29.40 ? 338 ASP A OD2 1 ATOM 2490 N N . ASN A 1 339 ? 41.738 2.059 5.741 1.00 22.01 ? 339 ASN A N 1 ATOM 2491 C CA . ASN A 1 339 ? 43.071 1.884 6.303 1.00 24.46 ? 339 ASN A CA 1 ATOM 2492 C C . ASN A 1 339 ? 43.180 2.479 7.700 1.00 24.36 ? 339 ASN A C 1 ATOM 2493 O O . ASN A 1 339 ? 43.961 2.009 8.522 1.00 23.07 ? 339 ASN A O 1 ATOM 2494 C CB . ASN A 1 339 ? 44.138 2.534 5.409 1.00 25.94 ? 339 ASN A CB 1 ATOM 2495 C CG . ASN A 1 339 ? 44.270 1.855 4.055 1.00 27.49 ? 339 ASN A CG 1 ATOM 2496 O OD1 . ASN A 1 339 ? 43.893 0.698 3.885 1.00 32.06 ? 339 ASN A OD1 1 ATOM 2497 N ND2 . ASN A 1 339 ? 44.831 2.572 3.088 1.00 30.00 ? 339 ASN A ND2 1 ATOM 2498 N N . HIS A 1 340 ? 42.394 3.515 7.968 1.00 22.83 ? 340 HIS A N 1 ATOM 2499 C CA . HIS A 1 340 ? 42.439 4.173 9.270 1.00 21.16 ? 340 HIS A CA 1 ATOM 2500 C C . HIS A 1 340 ? 41.222 3.908 10.160 1.00 21.59 ? 340 HIS A C 1 ATOM 2501 O O . HIS A 1 340 ? 40.937 4.680 11.080 1.00 19.74 ? 340 HIS A O 1 ATOM 2502 C CB . HIS A 1 340 ? 42.619 5.674 9.068 1.00 20.59 ? 340 HIS A CB 1 ATOM 2503 C CG . HIS A 1 340 ? 43.987 6.059 8.600 1.00 21.32 ? 340 HIS A CG 1 ATOM 2504 N ND1 . HIS A 1 340 ? 45.067 6.145 9.452 1.00 19.61 ? 340 HIS A ND1 1 ATOM 2505 C CD2 . HIS A 1 340 ? 44.451 6.391 7.371 1.00 23.28 ? 340 HIS A CD2 1 ATOM 2506 C CE1 . HIS A 1 340 ? 46.135 6.518 8.770 1.00 23.59 ? 340 HIS A CE1 1 ATOM 2507 N NE2 . HIS A 1 340 ? 45.788 6.674 7.505 1.00 24.65 ? 340 HIS A NE2 1 ATOM 2508 N N . LEU A 1 341 ? 40.511 2.815 9.890 1.00 21.47 ? 341 LEU A N 1 ATOM 2509 C CA . LEU A 1 341 ? 39.338 2.463 10.681 1.00 23.62 ? 341 LEU A CA 1 ATOM 2510 C C . LEU A 1 341 ? 39.780 2.034 12.076 1.00 25.73 ? 341 LEU A C 1 ATOM 2511 O O . LEU A 1 341 ? 40.550 1.081 12.218 1.00 24.92 ? 341 LEU A O 1 ATOM 2512 C CB . LEU A 1 341 ? 38.572 1.321 10.011 1.00 23.21 ? 341 LEU A CB 1 ATOM 2513 C CG . LEU A 1 341 ? 37.135 1.115 10.492 1.00 24.76 ? 341 LEU A CG 1 ATOM 2514 C CD1 . LEU A 1 341 ? 36.298 2.341 10.141 1.00 21.78 ? 341 LEU A CD1 1 ATOM 2515 C CD2 . LEU A 1 341 ? 36.548 -0.131 9.837 1.00 25.16 ? 341 LEU A CD2 1 ATOM 2516 N N . ILE A 1 342 ? 39.300 2.731 13.105 1.00 25.80 ? 342 ILE A N 1 ATOM 2517 C CA . ILE A 1 342 ? 39.683 2.395 14.471 1.00 27.91 ? 342 ILE A CA 1 ATOM 2518 C C . ILE A 1 342 ? 39.401 0.928 14.768 1.00 29.92 ? 342 ILE A C 1 ATOM 2519 O O . ILE A 1 342 ? 38.402 0.374 14.311 1.00 27.10 ? 342 ILE A O 1 ATOM 2520 C CB . ILE A 1 342 ? 38.945 3.265 15.503 1.00 27.82 ? 342 ILE A CB 1 ATOM 2521 C CG1 . ILE A 1 342 ? 37.438 3.073 15.369 1.00 27.28 ? 342 ILE A CG1 1 ATOM 2522 C CG2 . ILE A 1 342 ? 39.321 4.719 15.311 1.00 26.43 ? 342 ILE A CG2 1 ATOM 2523 C CD1 . ILE A 1 342 ? 36.652 3.777 16.442 1.00 28.91 ? 342 ILE A CD1 1 ATOM 2524 N N . LYS A 1 343 ? 40.288 0.310 15.541 1.00 33.49 ? 343 LYS A N 1 ATOM 2525 C CA . LYS A 1 343 ? 40.164 -1.103 15.879 1.00 37.14 ? 343 LYS A CA 1 ATOM 2526 C C . LYS A 1 343 ? 39.248 -1.365 17.065 1.00 37.99 ? 343 LYS A C 1 ATOM 2527 O O . LYS A 1 343 ? 39.707 -1.432 18.205 1.00 38.07 ? 343 LYS A O 1 ATOM 2528 C CB . LYS A 1 343 ? 41.543 -1.697 16.183 1.00 36.46 ? 343 LYS A CB 1 ATOM 2529 C CG . LYS A 1 343 ? 42.574 -1.540 15.077 1.00 40.51 ? 343 LYS A CG 1 ATOM 2530 C CD . LYS A 1 343 ? 42.236 -2.369 13.853 1.00 43.46 ? 343 LYS A CD 1 ATOM 2531 C CE . LYS A 1 343 ? 43.339 -2.259 12.808 1.00 46.73 ? 343 LYS A CE 1 ATOM 2532 N NZ . LYS A 1 343 ? 43.040 -3.046 11.575 1.00 48.38 ? 343 LYS A NZ 1 ATOM 2533 N N . VAL A 1 344 ? 37.956 -1.511 16.790 1.00 38.85 ? 344 VAL A N 1 ATOM 2534 C CA . VAL A 1 344 ? 36.972 -1.802 17.825 1.00 40.77 ? 344 VAL A CA 1 ATOM 2535 C C . VAL A 1 344 ? 36.014 -2.840 17.251 1.00 43.06 ? 344 VAL A C 1 ATOM 2536 O O . VAL A 1 344 ? 35.652 -2.782 16.077 1.00 44.20 ? 344 VAL A O 1 ATOM 2537 C CB . VAL A 1 344 ? 36.190 -0.537 18.265 1.00 40.27 ? 344 VAL A CB 1 ATOM 2538 C CG1 . VAL A 1 344 ? 37.154 0.497 18.828 1.00 37.86 ? 344 VAL A CG1 1 ATOM 2539 C CG2 . VAL A 1 344 ? 35.406 0.034 17.100 1.00 39.00 ? 344 VAL A CG2 1 ATOM 2540 N N . ASP A 1 345 ? 35.608 -3.789 18.085 1.00 45.82 ? 345 ASP A N 1 ATOM 2541 C CA . ASP A 1 345 ? 34.733 -4.875 17.659 1.00 48.16 ? 345 ASP A CA 1 ATOM 2542 C C . ASP A 1 345 ? 33.243 -4.570 17.577 1.00 47.99 ? 345 ASP A C 1 ATOM 2543 O O . ASP A 1 345 ? 32.452 -5.460 17.264 1.00 49.24 ? 345 ASP A O 1 ATOM 2544 C CB . ASP A 1 345 ? 34.934 -6.075 18.582 1.00 52.16 ? 345 ASP A CB 1 ATOM 2545 C CG . ASP A 1 345 ? 34.786 -5.710 20.045 1.00 55.75 ? 345 ASP A CG 1 ATOM 2546 O OD1 . ASP A 1 345 ? 35.651 -4.968 20.559 1.00 58.36 ? 345 ASP A OD1 1 ATOM 2547 O OD2 . ASP A 1 345 ? 33.803 -6.155 20.677 1.00 57.37 ? 345 ASP A OD2 1 ATOM 2548 N N . ASN A 1 346 ? 32.852 -3.331 17.849 1.00 46.61 ? 346 ASN A N 1 ATOM 2549 C CA . ASN A 1 346 ? 31.436 -2.980 17.809 1.00 45.02 ? 346 ASN A CA 1 ATOM 2550 C C . ASN A 1 346 ? 30.980 -2.313 16.514 1.00 41.47 ? 346 ASN A C 1 ATOM 2551 O O . ASN A 1 346 ? 29.850 -1.837 16.427 1.00 41.00 ? 346 ASN A O 1 ATOM 2552 C CB . ASN A 1 346 ? 31.093 -2.085 19.003 1.00 47.98 ? 346 ASN A CB 1 ATOM 2553 C CG . ASN A 1 346 ? 31.125 -2.838 20.322 1.00 52.10 ? 346 ASN A CG 1 ATOM 2554 O OD1 . ASN A 1 346 ? 31.057 -2.239 21.396 1.00 53.16 ? 346 ASN A OD1 1 ATOM 2555 N ND2 . ASN A 1 346 ? 31.220 -4.163 20.244 1.00 51.99 ? 346 ASN A ND2 1 ATOM 2556 N N . ILE A 1 347 ? 31.848 -2.285 15.508 1.00 37.82 ? 347 ILE A N 1 ATOM 2557 C CA . ILE A 1 347 ? 31.496 -1.670 14.229 1.00 34.02 ? 347 ILE A CA 1 ATOM 2558 C C . ILE A 1 347 ? 30.726 -2.640 13.331 1.00 32.10 ? 347 ILE A C 1 ATOM 2559 O O . ILE A 1 347 ? 31.278 -3.629 12.852 1.00 31.63 ? 347 ILE A O 1 ATOM 2560 C CB . ILE A 1 347 ? 32.754 -1.186 13.474 1.00 32.11 ? 347 ILE A CB 1 ATOM 2561 C CG1 . ILE A 1 347 ? 33.529 -0.192 14.344 1.00 32.70 ? 347 ILE A CG1 1 ATOM 2562 C CG2 . ILE A 1 347 ? 32.347 -0.522 12.161 1.00 30.66 ? 347 ILE A CG2 1 ATOM 2563 C CD1 . ILE A 1 347 ? 34.830 0.295 13.728 1.00 31.80 ? 347 ILE A CD1 1 ATOM 2564 N N . VAL A 1 348 ? 29.446 -2.349 13.112 1.00 30.65 ? 348 VAL A N 1 ATOM 2565 C CA . VAL A 1 348 ? 28.589 -3.181 12.273 1.00 29.14 ? 348 VAL A CA 1 ATOM 2566 C C . VAL A 1 348 ? 28.679 -2.753 10.807 1.00 29.71 ? 348 VAL A C 1 ATOM 2567 O O . VAL A 1 348 ? 28.201 -1.680 10.432 1.00 29.24 ? 348 VAL A O 1 ATOM 2568 C CB . VAL A 1 348 ? 27.104 -3.087 12.719 1.00 29.04 ? 348 VAL A CB 1 ATOM 2569 C CG1 . VAL A 1 348 ? 26.224 -3.889 11.775 1.00 26.62 ? 348 VAL A CG1 1 ATOM 2570 C CG2 . VAL A 1 348 ? 26.950 -3.595 14.151 1.00 29.89 ? 348 VAL A CG2 1 ATOM 2571 N N . HIS A 1 349 ? 29.293 -3.594 9.979 1.00 29.41 ? 349 HIS A N 1 ATOM 2572 C CA . HIS A 1 349 ? 29.430 -3.290 8.558 1.00 28.61 ? 349 HIS A CA 1 ATOM 2573 C C . HIS A 1 349 ? 28.139 -3.574 7.813 1.00 28.38 ? 349 HIS A C 1 ATOM 2574 O O . HIS A 1 349 ? 27.577 -4.660 7.921 1.00 30.37 ? 349 HIS A O 1 ATOM 2575 C CB . HIS A 1 349 ? 30.565 -4.107 7.935 1.00 26.27 ? 349 HIS A CB 1 ATOM 2576 C CG . HIS A 1 349 ? 31.929 -3.654 8.348 1.00 27.90 ? 349 HIS A CG 1 ATOM 2577 N ND1 . HIS A 1 349 ? 32.392 -3.767 9.640 1.00 27.93 ? 349 HIS A ND1 1 ATOM 2578 C CD2 . HIS A 1 349 ? 32.921 -3.059 7.643 1.00 26.16 ? 349 HIS A CD2 1 ATOM 2579 C CE1 . HIS A 1 349 ? 33.609 -3.259 9.715 1.00 28.29 ? 349 HIS A CE1 1 ATOM 2580 N NE2 . HIS A 1 349 ? 33.953 -2.822 8.517 1.00 29.89 ? 349 HIS A NE2 1 ATOM 2581 N N . ILE A 1 350 ? 27.667 -2.587 7.059 1.00 27.77 ? 350 ILE A N 1 ATOM 2582 C CA . ILE A 1 350 ? 26.443 -2.747 6.289 1.00 27.15 ? 350 ILE A CA 1 ATOM 2583 C C . ILE A 1 350 ? 26.693 -2.444 4.818 1.00 28.35 ? 350 ILE A C 1 ATOM 2584 O O . ILE A 1 350 ? 27.656 -1.762 4.465 1.00 26.76 ? 350 ILE A O 1 ATOM 2585 C CB . ILE A 1 350 ? 25.317 -1.827 6.807 1.00 26.39 ? 350 ILE A CB 1 ATOM 2586 C CG1 . ILE A 1 350 ? 25.794 -0.372 6.835 1.00 25.32 ? 350 ILE A CG1 1 ATOM 2587 C CG2 . ILE A 1 350 ? 24.878 -2.275 8.199 1.00 27.46 ? 350 ILE A CG2 1 ATOM 2588 C CD1 . ILE A 1 350 ? 24.714 0.613 7.235 1.00 22.97 ? 350 ILE A CD1 1 ATOM 2589 N N . ARG A 1 351 ? 25.825 -2.972 3.964 1.00 30.59 ? 351 ARG A N 1 ATOM 2590 C CA . ARG A 1 351 ? 25.946 -2.763 2.528 1.00 33.67 ? 351 ARG A CA 1 ATOM 2591 C C . ARG A 1 351 ? 24.846 -1.827 2.060 1.00 34.77 ? 351 ARG A C 1 ATOM 2592 O O . ARG A 1 351 ? 23.781 -1.747 2.670 1.00 35.78 ? 351 ARG A O 1 ATOM 2593 C CB . ARG A 1 351 ? 25.817 -4.095 1.778 1.00 33.39 ? 351 ARG A CB 1 ATOM 2594 C CG . ARG A 1 351 ? 26.821 -5.172 2.177 1.00 34.24 ? 351 ARG A CG 1 ATOM 2595 C CD . ARG A 1 351 ? 28.231 -4.878 1.665 1.00 32.01 ? 351 ARG A CD 1 ATOM 2596 N NE . ARG A 1 351 ? 28.253 -4.684 0.217 1.00 31.30 ? 351 ARG A NE 1 ATOM 2597 C CZ . ARG A 1 351 ? 29.360 -4.568 -0.512 1.00 29.34 ? 351 ARG A CZ 1 ATOM 2598 N NH1 . ARG A 1 351 ? 30.557 -4.631 0.060 1.00 27.59 ? 351 ARG A NH1 1 ATOM 2599 N NH2 . ARG A 1 351 ? 29.267 -4.376 -1.819 1.00 29.92 ? 351 ARG A NH2 1 ATOM 2600 N N . ASN A 1 352 ? 25.113 -1.110 0.979 1.00 36.78 ? 352 ASN A N 1 ATOM 2601 C CA . ASN A 1 352 ? 24.133 -0.202 0.407 1.00 41.35 ? 352 ASN A CA 1 ATOM 2602 C C . ASN A 1 352 ? 24.210 -0.355 -1.102 1.00 44.30 ? 352 ASN A C 1 ATOM 2603 O O . ASN A 1 352 ? 24.375 0.619 -1.832 1.00 44.18 ? 352 ASN A O 1 ATOM 2604 C CB . ASN A 1 352 ? 24.434 1.240 0.805 1.00 41.62 ? 352 ASN A CB 1 ATOM 2605 C CG . ASN A 1 352 ? 23.365 2.199 0.340 1.00 42.65 ? 352 ASN A CG 1 ATOM 2606 O OD1 . ASN A 1 352 ? 22.172 1.954 0.531 1.00 43.17 ? 352 ASN A OD1 1 ATOM 2607 N ND2 . ASN A 1 352 ? 23.782 3.301 -0.271 1.00 42.89 ? 352 ASN A ND2 1 ATOM 2608 N N . ASP A 1 353 ? 24.099 -1.598 -1.557 1.00 48.36 ? 353 ASP A N 1 ATOM 2609 C CA . ASP A 1 353 ? 24.168 -1.906 -2.978 1.00 52.91 ? 353 ASP A CA 1 ATOM 2610 C C . ASP A 1 353 ? 22.852 -1.601 -3.680 1.00 55.37 ? 353 ASP A C 1 ATOM 2611 O O . ASP A 1 353 ? 21.774 -1.872 -3.150 1.00 55.85 ? 353 ASP A O 1 ATOM 2612 C CB . ASP A 1 353 ? 24.533 -3.378 -3.176 1.00 52.97 ? 353 ASP A CB 1 ATOM 2613 C CG . ASP A 1 353 ? 25.808 -3.765 -2.447 1.00 53.86 ? 353 ASP A CG 1 ATOM 2614 O OD1 . ASP A 1 353 ? 26.849 -3.106 -2.670 1.00 53.28 ? 353 ASP A OD1 1 ATOM 2615 O OD2 . ASP A 1 353 ? 25.769 -4.729 -1.652 1.00 54.20 ? 353 ASP A OD2 1 ATOM 2616 N N . HIS A 1 354 ? 22.953 -1.031 -4.876 1.00 58.24 ? 354 HIS A N 1 ATOM 2617 C CA . HIS A 1 354 ? 21.782 -0.684 -5.671 1.00 60.49 ? 354 HIS A CA 1 ATOM 2618 C C . HIS A 1 354 ? 21.743 -1.500 -6.958 1.00 60.86 ? 354 HIS A C 1 ATOM 2619 O O . HIS A 1 354 ? 22.583 -2.415 -7.100 1.00 61.34 ? 354 HIS A O 1 ATOM 2620 C CB . HIS A 1 354 ? 21.795 0.809 -6.011 1.00 62.53 ? 354 HIS A CB 1 ATOM 2621 C CG . HIS A 1 354 ? 21.530 1.701 -4.838 1.00 64.41 ? 354 HIS A CG 1 ATOM 2622 N ND1 . HIS A 1 354 ? 20.393 1.596 -4.065 1.00 65.20 ? 354 HIS A ND1 1 ATOM 2623 C CD2 . HIS A 1 354 ? 22.245 2.727 -4.318 1.00 65.58 ? 354 HIS A CD2 1 ATOM 2624 C CE1 . HIS A 1 354 ? 20.418 2.520 -3.121 1.00 65.92 ? 354 HIS A CE1 1 ATOM 2625 N NE2 . HIS A 1 354 ? 21.531 3.220 -3.253 1.00 65.77 ? 354 HIS A NE2 1 HETATM 2626 S S . SO4 B 2 . ? 27.463 10.102 0.324 1.00 36.92 ? 2847 SO4 A S 1 HETATM 2627 O O1 . SO4 B 2 . ? 28.565 10.772 -0.399 1.00 37.91 ? 2847 SO4 A O1 1 HETATM 2628 O O2 . SO4 B 2 . ? 28.024 9.083 1.231 1.00 32.91 ? 2847 SO4 A O2 1 HETATM 2629 O O3 . SO4 B 2 . ? 26.690 11.091 1.100 1.00 36.26 ? 2847 SO4 A O3 1 HETATM 2630 O O4 . SO4 B 2 . ? 26.585 9.455 -0.671 1.00 38.84 ? 2847 SO4 A O4 1 HETATM 2631 O O . HOH C 3 . ? 22.674 9.149 33.077 1.00 38.66 ? 2848 HOH A O 1 HETATM 2632 O O . HOH C 3 . ? 24.630 5.746 32.248 1.00 31.51 ? 2849 HOH A O 1 HETATM 2633 O O . HOH C 3 . ? 29.323 2.241 29.816 1.00 50.43 ? 2850 HOH A O 1 HETATM 2634 O O . HOH C 3 . ? 22.397 6.017 35.995 1.00 47.81 ? 2851 HOH A O 1 HETATM 2635 O O . HOH C 3 . ? 16.189 8.308 28.623 1.00 20.03 ? 2852 HOH A O 1 HETATM 2636 O O . HOH C 3 . ? 35.559 2.976 3.103 1.00 34.19 ? 2853 HOH A O 1 HETATM 2637 O O . HOH C 3 . ? 32.482 3.227 2.980 1.00 29.98 ? 2854 HOH A O 1 HETATM 2638 O O . HOH C 3 . ? 31.391 13.616 5.972 1.00 16.30 ? 2855 HOH A O 1 HETATM 2639 O O . HOH C 3 . ? 31.893 15.155 3.533 1.00 36.16 ? 2856 HOH A O 1 HETATM 2640 O O . HOH C 3 . ? 23.933 9.892 -0.068 1.00 34.93 ? 2857 HOH A O 1 HETATM 2641 O O . HOH C 3 . ? 35.881 7.080 9.649 1.00 13.54 ? 2858 HOH A O 1 HETATM 2642 O O . HOH C 3 . ? 12.446 8.805 -0.022 1.00 52.31 ? 2859 HOH A O 1 HETATM 2643 O O . HOH C 3 . ? 11.248 13.612 10.374 1.00 32.77 ? 2860 HOH A O 1 HETATM 2644 O O . HOH C 3 . ? 5.057 4.454 11.321 1.00 37.23 ? 2861 HOH A O 1 HETATM 2645 O O . HOH C 3 . ? 4.319 3.655 15.694 1.00 29.00 ? 2862 HOH A O 1 HETATM 2646 O O . HOH C 3 . ? 2.075 2.879 17.766 1.00 40.80 ? 2863 HOH A O 1 HETATM 2647 O O . HOH C 3 . ? 21.118 37.550 20.819 1.00 50.94 ? 2864 HOH A O 1 HETATM 2648 O O . HOH C 3 . ? 18.486 39.496 19.502 1.00 59.29 ? 2865 HOH A O 1 HETATM 2649 O O . HOH C 3 . ? 26.038 15.074 32.557 1.00 23.39 ? 2866 HOH A O 1 HETATM 2650 O O . HOH C 3 . ? 9.424 10.737 35.192 1.00 45.00 ? 2867 HOH A O 1 HETATM 2651 O O . HOH C 3 . ? 7.481 10.053 41.603 1.00 59.06 ? 2868 HOH A O 1 HETATM 2652 O O . HOH C 3 . ? 12.255 6.241 36.251 1.00 51.84 ? 2869 HOH A O 1 HETATM 2653 O O . HOH C 3 . ? 11.085 10.279 38.695 1.00 56.16 ? 2870 HOH A O 1 HETATM 2654 O O . HOH C 3 . ? 24.910 14.216 -1.624 1.00 57.73 ? 2871 HOH A O 1 HETATM 2655 O O . HOH C 3 . ? 27.186 16.710 -3.147 1.00 43.32 ? 2872 HOH A O 1 HETATM 2656 O O . HOH C 3 . ? 31.390 12.464 1.677 1.00 34.73 ? 2873 HOH A O 1 HETATM 2657 O O . HOH C 3 . ? 26.091 14.427 4.584 1.00 35.79 ? 2874 HOH A O 1 HETATM 2658 O O . HOH C 3 . ? 9.341 -1.790 10.713 1.00 44.15 ? 2875 HOH A O 1 HETATM 2659 O O . HOH C 3 . ? 12.881 -2.538 18.514 1.00 25.11 ? 2876 HOH A O 1 HETATM 2660 O O . HOH C 3 . ? 20.191 -2.587 19.505 1.00 21.79 ? 2877 HOH A O 1 HETATM 2661 O O . HOH C 3 . ? 13.304 -2.392 29.645 1.00 38.62 ? 2878 HOH A O 1 HETATM 2662 O O . HOH C 3 . ? 10.275 5.334 32.425 1.00 45.47 ? 2879 HOH A O 1 HETATM 2663 O O . HOH C 3 . ? 19.807 19.356 23.031 1.00 17.61 ? 2880 HOH A O 1 HETATM 2664 O O . HOH C 3 . ? 14.584 15.890 17.383 1.00 24.50 ? 2881 HOH A O 1 HETATM 2665 O O . HOH C 3 . ? 32.344 10.506 26.928 1.00 25.30 ? 2882 HOH A O 1 HETATM 2666 O O . HOH C 3 . ? 34.839 9.563 27.593 1.00 20.53 ? 2883 HOH A O 1 HETATM 2667 O O . HOH C 3 . ? 36.419 7.497 16.513 1.00 22.59 ? 2884 HOH A O 1 HETATM 2668 O O . HOH C 3 . ? 36.860 10.554 26.135 1.00 40.97 ? 2885 HOH A O 1 HETATM 2669 O O . HOH C 3 . ? 38.764 7.182 1.949 1.00 21.88 ? 2886 HOH A O 1 HETATM 2670 O O . HOH C 3 . ? 33.773 5.920 -2.107 1.00 29.05 ? 2887 HOH A O 1 HETATM 2671 O O . HOH C 3 . ? 12.211 -4.749 11.275 1.00 41.94 ? 2888 HOH A O 1 HETATM 2672 O O . HOH C 3 . ? -0.866 2.000 15.920 1.00 47.73 ? 2889 HOH A O 1 HETATM 2673 O O . HOH C 3 . ? -2.693 10.771 26.222 1.00 21.62 ? 2890 HOH A O 1 HETATM 2674 O O . HOH C 3 . ? 1.418 14.767 23.990 1.00 34.54 ? 2891 HOH A O 1 HETATM 2675 O O . HOH C 3 . ? 12.368 19.322 38.951 1.00 28.64 ? 2892 HOH A O 1 HETATM 2676 O O . HOH C 3 . ? 6.611 13.097 33.517 1.00 40.61 ? 2893 HOH A O 1 HETATM 2677 O O . HOH C 3 . ? 20.137 19.917 36.201 1.00 33.90 ? 2894 HOH A O 1 HETATM 2678 O O . HOH C 3 . ? 20.051 27.214 35.090 1.00 42.25 ? 2895 HOH A O 1 HETATM 2679 O O . HOH C 3 . ? 36.166 20.181 26.403 1.00 24.51 ? 2896 HOH A O 1 HETATM 2680 O O . HOH C 3 . ? 38.776 26.297 26.452 1.00 26.75 ? 2897 HOH A O 1 HETATM 2681 O O . HOH C 3 . ? 41.191 27.495 25.709 1.00 34.24 ? 2898 HOH A O 1 HETATM 2682 O O . HOH C 3 . ? 44.250 25.805 23.086 1.00 24.36 ? 2899 HOH A O 1 HETATM 2683 O O . HOH C 3 . ? 41.771 27.676 23.108 1.00 18.91 ? 2900 HOH A O 1 HETATM 2684 O O . HOH C 3 . ? 33.320 37.293 25.894 1.00 25.18 ? 2901 HOH A O 1 HETATM 2685 O O . HOH C 3 . ? 30.339 43.487 13.554 1.00 52.61 ? 2902 HOH A O 1 HETATM 2686 O O . HOH C 3 . ? 35.007 42.977 15.869 1.00 38.67 ? 2903 HOH A O 1 HETATM 2687 O O . HOH C 3 . ? 35.286 31.399 7.807 1.00 23.49 ? 2904 HOH A O 1 HETATM 2688 O O . HOH C 3 . ? 34.978 30.974 3.011 1.00 27.00 ? 2905 HOH A O 1 HETATM 2689 O O . HOH C 3 . ? 48.587 28.042 9.044 1.00 41.13 ? 2906 HOH A O 1 HETATM 2690 O O . HOH C 3 . ? 47.623 26.621 12.515 1.00 26.90 ? 2907 HOH A O 1 HETATM 2691 O O . HOH C 3 . ? 44.737 33.529 16.264 1.00 42.77 ? 2908 HOH A O 1 HETATM 2692 O O . HOH C 3 . ? 49.387 23.591 5.019 1.00 29.71 ? 2909 HOH A O 1 HETATM 2693 O O . HOH C 3 . ? 47.151 20.864 7.504 1.00 31.60 ? 2910 HOH A O 1 HETATM 2694 O O . HOH C 3 . ? 41.177 17.890 11.240 1.00 13.42 ? 2911 HOH A O 1 HETATM 2695 O O . HOH C 3 . ? 41.888 17.892 21.222 1.00 41.81 ? 2912 HOH A O 1 HETATM 2696 O O . HOH C 3 . ? 40.928 20.155 20.295 1.00 27.72 ? 2913 HOH A O 1 HETATM 2697 O O . HOH C 3 . ? 23.595 -5.300 4.800 1.00 43.63 ? 2914 HOH A O 1 HETATM 2698 O O . HOH C 3 . ? 29.374 37.937 18.284 1.00 49.74 ? 2915 HOH A O 1 HETATM 2699 O O . HOH C 3 . ? 34.656 26.459 15.123 1.00 15.02 ? 2916 HOH A O 1 HETATM 2700 O O . HOH C 3 . ? 35.967 27.249 8.998 1.00 19.55 ? 2917 HOH A O 1 HETATM 2701 O O . HOH C 3 . ? 35.070 31.016 10.466 1.00 21.08 ? 2918 HOH A O 1 HETATM 2702 O O . HOH C 3 . ? 27.647 28.266 12.565 1.00 34.01 ? 2919 HOH A O 1 HETATM 2703 O O . HOH C 3 . ? 25.578 26.305 14.261 1.00 23.29 ? 2920 HOH A O 1 HETATM 2704 O O . HOH C 3 . ? 13.016 31.812 27.553 1.00 40.08 ? 2921 HOH A O 1 HETATM 2705 O O . HOH C 3 . ? 10.995 18.287 17.579 1.00 29.67 ? 2922 HOH A O 1 HETATM 2706 O O . HOH C 3 . ? 34.597 23.404 -2.522 1.00 44.84 ? 2923 HOH A O 1 HETATM 2707 O O . HOH C 3 . ? 47.915 22.229 2.869 1.00 36.72 ? 2924 HOH A O 1 HETATM 2708 O O . HOH C 3 . ? 39.716 14.961 -2.337 1.00 49.77 ? 2925 HOH A O 1 HETATM 2709 O O . HOH C 3 . ? 44.645 12.972 4.190 1.00 38.99 ? 2926 HOH A O 1 HETATM 2710 O O . HOH C 3 . ? 42.003 13.792 -7.309 1.00 36.78 ? 2927 HOH A O 1 HETATM 2711 O O . HOH C 3 . ? 31.528 14.832 27.704 1.00 20.37 ? 2928 HOH A O 1 HETATM 2712 O O . HOH C 3 . ? 32.387 18.761 28.663 1.00 34.27 ? 2929 HOH A O 1 HETATM 2713 O O . HOH C 3 . ? 6.059 2.606 37.703 1.00 57.04 ? 2930 HOH A O 1 HETATM 2714 O O . HOH C 3 . ? 8.302 -4.290 30.357 1.00 32.98 ? 2931 HOH A O 1 HETATM 2715 O O . HOH C 3 . ? 10.364 -3.077 29.097 1.00 43.96 ? 2932 HOH A O 1 HETATM 2716 O O . HOH C 3 . ? 7.280 24.319 28.406 1.00 38.15 ? 2933 HOH A O 1 HETATM 2717 O O . HOH C 3 . ? 15.645 22.042 24.435 1.00 21.02 ? 2934 HOH A O 1 HETATM 2718 O O . HOH C 3 . ? 13.161 23.087 22.617 1.00 38.14 ? 2935 HOH A O 1 HETATM 2719 O O . HOH C 3 . ? 19.490 28.109 5.739 1.00 44.01 ? 2936 HOH A O 1 HETATM 2720 O O . HOH C 3 . ? 14.767 24.654 17.357 1.00 39.18 ? 2937 HOH A O 1 HETATM 2721 O O . HOH C 3 . ? 38.185 5.740 9.243 1.00 19.50 ? 2938 HOH A O 1 HETATM 2722 O O . HOH C 3 . ? 44.132 10.939 19.073 1.00 36.99 ? 2939 HOH A O 1 HETATM 2723 O O . HOH C 3 . ? 45.996 2.679 18.034 1.00 50.06 ? 2940 HOH A O 1 HETATM 2724 O O . HOH C 3 . ? 44.334 16.264 19.285 1.00 29.85 ? 2941 HOH A O 1 HETATM 2725 O O . HOH C 3 . ? 46.994 15.513 11.975 1.00 39.69 ? 2942 HOH A O 1 HETATM 2726 O O . HOH C 3 . ? 47.552 12.241 11.864 1.00 32.17 ? 2943 HOH A O 1 HETATM 2727 O O . HOH C 3 . ? 47.143 11.802 15.329 1.00 39.38 ? 2944 HOH A O 1 HETATM 2728 O O . HOH C 3 . ? 26.699 1.369 23.603 1.00 30.36 ? 2945 HOH A O 1 HETATM 2729 O O . HOH C 3 . ? 29.116 1.900 24.094 1.00 28.78 ? 2946 HOH A O 1 HETATM 2730 O O . HOH C 3 . ? 27.341 -0.880 17.301 1.00 21.84 ? 2947 HOH A O 1 HETATM 2731 O O . HOH C 3 . ? 35.530 -2.107 21.574 1.00 51.75 ? 2948 HOH A O 1 HETATM 2732 O O . HOH C 3 . ? 37.505 -1.533 -10.821 1.00 37.24 ? 2949 HOH A O 1 HETATM 2733 O O . HOH C 3 . ? 39.455 -2.151 -12.344 1.00 37.45 ? 2950 HOH A O 1 HETATM 2734 O O . HOH C 3 . ? 30.908 1.074 -13.148 1.00 55.27 ? 2951 HOH A O 1 HETATM 2735 O O . HOH C 3 . ? 26.220 3.976 -9.621 1.00 32.16 ? 2952 HOH A O 1 HETATM 2736 O O . HOH C 3 . ? 25.737 1.507 -11.133 1.00 52.40 ? 2953 HOH A O 1 HETATM 2737 O O . HOH C 3 . ? 31.241 12.200 -19.903 1.00 15.94 ? 2954 HOH A O 1 HETATM 2738 O O . HOH C 3 . ? 45.462 8.842 -3.081 1.00 30.28 ? 2955 HOH A O 1 HETATM 2739 O O . HOH C 3 . ? 35.612 -3.079 11.738 1.00 32.20 ? 2956 HOH A O 1 HETATM 2740 O O . HOH C 3 . ? 38.523 -4.036 14.512 1.00 39.80 ? 2957 HOH A O 1 HETATM 2741 O O . HOH C 3 . ? 29.695 -6.476 10.884 1.00 29.98 ? 2958 HOH A O 1 HETATM 2742 O O . HOH C 3 . ? 21.076 2.570 -8.213 1.00 49.93 ? 2959 HOH A O 1 HETATM 2743 O O . HOH C 3 . ? 20.138 8.481 34.529 1.00 36.77 ? 2960 HOH A O 1 HETATM 2744 O O . HOH C 3 . ? 28.678 14.371 6.582 1.00 21.82 ? 2961 HOH A O 1 HETATM 2745 O O . HOH C 3 . ? 13.984 14.459 41.206 1.00 51.21 ? 2962 HOH A O 1 HETATM 2746 O O . HOH C 3 . ? 23.680 16.086 3.646 1.00 40.29 ? 2963 HOH A O 1 HETATM 2747 O O . HOH C 3 . ? 32.027 13.803 -3.846 1.00 48.35 ? 2964 HOH A O 1 HETATM 2748 O O . HOH C 3 . ? 1.258 16.559 26.343 1.00 33.33 ? 2965 HOH A O 1 HETATM 2749 O O . HOH C 3 . ? 20.307 17.817 35.040 1.00 41.98 ? 2966 HOH A O 1 HETATM 2750 O O . HOH C 3 . ? 39.147 23.487 27.612 1.00 40.08 ? 2967 HOH A O 1 HETATM 2751 O O . HOH C 3 . ? 42.982 26.005 27.020 1.00 42.85 ? 2968 HOH A O 1 HETATM 2752 O O . HOH C 3 . ? 19.118 35.069 19.825 1.00 56.05 ? 2969 HOH A O 1 HETATM 2753 O O . HOH C 3 . ? 37.147 13.600 0.189 1.00 45.28 ? 2970 HOH A O 1 HETATM 2754 O O . HOH C 3 . ? 44.277 15.132 5.954 1.00 38.15 ? 2971 HOH A O 1 HETATM 2755 O O . HOH C 3 . ? 16.693 29.824 16.937 1.00 42.04 ? 2972 HOH A O 1 HETATM 2756 O O . HOH C 3 . ? 35.787 -1.475 5.962 1.00 42.72 ? 2973 HOH A O 1 HETATM 2757 O O . HOH C 3 . ? 37.806 -1.882 12.656 1.00 35.22 ? 2974 HOH A O 1 HETATM 2758 O O . HOH C 3 . ? 26.151 10.601 -9.069 1.00 30.31 ? 2975 HOH A O 1 HETATM 2759 O O . HOH C 3 . ? 38.155 6.365 20.635 1.00 30.87 ? 2976 HOH A O 1 HETATM 2760 O O . HOH C 3 . ? 41.264 5.637 23.400 1.00 49.68 ? 2977 HOH A O 1 HETATM 2761 O O . HOH C 3 . ? 44.669 3.070 20.698 1.00 34.42 ? 2978 HOH A O 1 HETATM 2762 O O . HOH C 3 . ? 24.586 8.606 24.181 1.00 28.76 ? 2979 HOH A O 1 HETATM 2763 O O . HOH C 3 . ? 31.895 35.827 11.904 1.00 36.51 ? 2980 HOH A O 1 HETATM 2764 O O . HOH C 3 . ? 30.699 30.203 5.852 1.00 33.67 ? 2981 HOH A O 1 HETATM 2765 O O . HOH C 3 . ? 33.412 38.213 10.823 1.00 48.14 ? 2982 HOH A O 1 HETATM 2766 O O . HOH C 3 . ? -3.551 2.710 20.868 1.00 37.23 ? 2983 HOH A O 1 HETATM 2767 O O . HOH C 3 . ? 35.350 43.244 8.687 1.00 39.98 ? 2984 HOH A O 1 HETATM 2768 O O . HOH C 3 . ? 0.523 12.253 15.635 1.00 41.52 ? 2985 HOH A O 1 HETATM 2769 O O . HOH C 3 . ? 12.991 -5.439 17.886 1.00 39.49 ? 2986 HOH A O 1 HETATM 2770 O O . HOH C 3 . ? 22.511 24.739 29.143 1.00 45.96 ? 2987 HOH A O 1 HETATM 2771 O O . HOH C 3 . ? 14.776 16.725 14.741 1.00 56.56 ? 2988 HOH A O 1 HETATM 2772 O O . HOH C 3 . ? 48.837 6.234 14.150 1.00 40.45 ? 2989 HOH A O 1 HETATM 2773 O O . HOH C 3 . ? 48.750 8.579 15.664 1.00 43.37 ? 2990 HOH A O 1 HETATM 2774 O O . HOH C 3 . ? 33.912 16.215 1.960 1.00 45.56 ? 2991 HOH A O 1 HETATM 2775 O O . HOH C 3 . ? 23.720 -3.699 16.170 1.00 39.96 ? 2992 HOH A O 1 HETATM 2776 O O . HOH C 3 . ? 25.915 -3.178 17.334 1.00 36.89 ? 2993 HOH A O 1 HETATM 2777 O O . HOH C 3 . ? 21.993 -3.020 14.481 1.00 40.00 ? 2994 HOH A O 1 HETATM 2778 O O . HOH C 3 . ? 23.822 -5.934 13.937 1.00 46.26 ? 2995 HOH A O 1 HETATM 2779 O O . HOH C 3 . ? 34.896 14.871 0.069 1.00 45.54 ? 2996 HOH A O 1 HETATM 2780 O O . HOH C 3 . ? 45.307 17.536 3.474 1.00 47.24 ? 2997 HOH A O 1 HETATM 2781 O O . HOH C 3 . ? 42.602 30.366 23.207 1.00 46.46 ? 2998 HOH A O 1 HETATM 2782 O O . HOH C 3 . ? 45.910 24.162 25.243 1.00 40.01 ? 2999 HOH A O 1 HETATM 2783 O O . HOH C 3 . ? 47.404 24.745 20.784 1.00 40.85 ? 3000 HOH A O 1 HETATM 2784 O O . HOH C 3 . ? 52.647 22.898 25.276 1.00 47.94 ? 3001 HOH A O 1 HETATM 2785 O O . HOH C 3 . ? 25.640 -7.146 12.390 1.00 49.59 ? 3002 HOH A O 1 HETATM 2786 O O . HOH C 3 . ? 42.167 1.939 17.111 1.00 46.58 ? 3003 HOH A O 1 HETATM 2787 O O . HOH C 3 . ? 46.521 14.488 18.379 1.00 36.39 ? 3004 HOH A O 1 HETATM 2788 O O . HOH C 3 . ? 28.608 12.928 0.757 1.00 44.46 ? 3005 HOH A O 1 HETATM 2789 O O . HOH C 3 . ? 25.831 14.121 0.811 1.00 51.60 ? 3006 HOH A O 1 HETATM 2790 O O . HOH C 3 . ? 23.570 17.317 -1.842 1.00 58.14 ? 3007 HOH A O 1 HETATM 2791 O O . HOH C 3 . ? 32.305 19.404 -0.933 1.00 48.77 ? 3008 HOH A O 1 HETATM 2792 O O . HOH C 3 . ? 17.667 2.322 -4.835 1.00 58.06 ? 3009 HOH A O 1 HETATM 2793 O O . HOH C 3 . ? 14.400 0.851 -3.800 1.00 48.25 ? 3010 HOH A O 1 HETATM 2794 O O . HOH C 3 . ? 11.903 1.912 -3.131 1.00 42.27 ? 3011 HOH A O 1 HETATM 2795 O O . HOH C 3 . ? 18.188 41.450 17.018 1.00 44.00 ? 3012 HOH A O 1 HETATM 2796 O O . HOH C 3 . ? -0.273 3.451 18.804 1.00 43.85 ? 3013 HOH A O 1 HETATM 2797 O O . HOH C 3 . ? 11.766 -3.409 5.673 1.00 39.06 ? 3014 HOH A O 1 HETATM 2798 O O . HOH C 3 . ? 16.332 -0.821 32.892 1.00 40.28 ? 3015 HOH A O 1 HETATM 2799 O O . HOH C 3 . ? 35.086 5.606 30.246 1.00 36.46 ? 3016 HOH A O 1 HETATM 2800 O O . HOH C 3 . ? 36.983 4.050 30.757 1.00 45.86 ? 3017 HOH A O 1 HETATM 2801 O O . HOH C 3 . ? 51.472 31.355 7.206 1.00 48.50 ? 3018 HOH A O 1 HETATM 2802 O O . HOH C 3 . ? 39.901 29.963 11.900 1.00 29.16 ? 3019 HOH A O 1 HETATM 2803 O O . HOH C 3 . ? 10.299 27.440 24.625 1.00 44.71 ? 3020 HOH A O 1 HETATM 2804 O O . HOH C 3 . ? 35.523 3.216 24.220 1.00 42.44 ? 3021 HOH A O 1 HETATM 2805 O O . HOH C 3 . ? 38.839 -1.848 -15.408 1.00 37.84 ? 3022 HOH A O 1 HETATM 2806 O O . HOH C 3 . ? 38.533 2.060 31.094 1.00 48.01 ? 3023 HOH A O 1 HETATM 2807 O O . HOH C 3 . ? 33.045 2.498 29.667 1.00 53.14 ? 3024 HOH A O 1 HETATM 2808 O O . HOH C 3 . ? 34.186 29.770 -6.817 1.00 52.75 ? 3025 HOH A O 1 HETATM 2809 O O . HOH C 3 . ? 33.872 27.707 -8.214 1.00 47.39 ? 3026 HOH A O 1 HETATM 2810 O O . HOH C 3 . ? 38.029 24.969 -2.225 1.00 44.89 ? 3027 HOH A O 1 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 MET 1 1 ? ? ? A . n A 1 2 VAL 2 2 2 VAL VAL A . n A 1 3 ASP 3 3 3 ASP ASP A . n A 1 4 THR 4 4 4 THR THR A . n A 1 5 HIS 5 5 5 HIS HIS A . n A 1 6 LYS 6 6 6 LYS LYS A . n A 1 7 LEU 7 7 7 LEU LEU A . n A 1 8 ALA 8 8 8 ALA ALA A . n A 1 9 ASP 9 9 9 ASP ASP A . n A 1 10 ASP 10 10 10 ASP ASP A . n A 1 11 VAL 11 11 11 VAL VAL A . n A 1 12 LEU 12 12 12 LEU LEU A . n A 1 13 GLN 13 13 13 GLN GLN A . n A 1 14 LEU 14 14 14 LEU LEU A . n A 1 15 LEU 15 15 15 LEU LEU A . n A 1 16 ASP 16 16 16 ASP ASP A . n A 1 17 ASN 17 17 17 ASN ASN A . n A 1 18 ARG 18 18 18 ARG ARG A . n A 1 19 ILE 19 19 19 ILE ILE A . n A 1 20 GLU 20 20 20 GLU GLU A . n A 1 21 ASP 21 21 21 ASP ASP A . n A 1 22 ASN 22 22 22 ASN ASN A . n A 1 23 TYR 23 23 23 TYR TYR A . n A 1 24 ARG 24 24 24 ARG ARG A . n A 1 25 VAL 25 25 25 VAL VAL A . n A 1 26 CYS 26 26 26 CYS CYS A . n A 1 27 VAL 27 27 27 VAL VAL A . n A 1 28 ILE 28 28 28 ILE ILE A . n A 1 29 LEU 29 29 29 LEU LEU A . n A 1 30 VAL 30 30 30 VAL VAL A . n A 1 31 GLY 31 31 31 GLY GLY A . n A 1 32 SER 32 32 32 SER SER A . n A 1 33 PRO 33 33 33 PRO PRO A . n A 1 34 GLY 34 34 34 GLY GLY A . n A 1 35 SER 35 35 35 SER SER A . n A 1 36 GLY 36 36 36 GLY GLY A . n A 1 37 LYS 37 37 37 LYS LYS A . n A 1 38 SER 38 38 38 SER SER A . n A 1 39 THR 39 39 39 THR THR A . n A 1 40 ILE 40 40 40 ILE ILE A . n A 1 41 ALA 41 41 41 ALA ALA A . n A 1 42 GLU 42 42 42 GLU GLU A . n A 1 43 GLU 43 43 43 GLU GLU A . n A 1 44 LEU 44 44 44 LEU LEU A . n A 1 45 CME 45 45 45 CME CYB A . n A 1 46 GLN 46 46 46 GLN GLN A . n A 1 47 ILE 47 47 47 ILE ILE A . n A 1 48 ILE 48 48 48 ILE ILE A . n A 1 49 ASN 49 49 49 ASN ASN A . n A 1 50 GLU 50 50 50 GLU GLU A . n A 1 51 LYS 51 51 51 LYS LYS A . n A 1 52 TYR 52 52 52 TYR TYR A . n A 1 53 HIS 53 53 53 HIS HIS A . n A 1 54 THR 54 54 54 THR THR A . n A 1 55 PHE 55 55 55 PHE PHE A . n A 1 56 LEU 56 56 56 LEU LEU A . n A 1 57 SER 57 57 57 SER SER A . n A 1 58 GLU 58 58 58 GLU GLU A . n A 1 59 HIS 59 59 59 HIS HIS A . n A 1 60 PRO 60 60 60 PRO PRO A . n A 1 61 ASN 61 61 61 ASN ASN A . n A 1 62 VAL 62 62 62 VAL VAL A . n A 1 63 ILE 63 63 63 ILE ILE A . n A 1 64 GLU 64 64 64 GLU GLU A . n A 1 65 VAL 65 65 65 VAL VAL A . n A 1 66 ASN 66 66 66 ASN ASN A . n A 1 67 ASP 67 67 67 ASP ASP A . n A 1 68 ARG 68 68 68 ARG ARG A . n A 1 69 LEU 69 69 69 LEU LEU A . n A 1 70 LYS 70 70 70 LYS LYS A . n A 1 71 PRO 71 71 71 PRO PRO A . n A 1 72 MET 72 72 72 MET MET A . n A 1 73 VAL 73 73 73 VAL VAL A . n A 1 74 ASN 74 74 74 ASN ASN A . n A 1 75 LEU 75 75 75 LEU LEU A . n A 1 76 VAL 76 76 76 VAL VAL A . n A 1 77 ASP 77 77 77 ASP ASP A . n A 1 78 SER 78 78 78 SER SER A . n A 1 79 LEU 79 79 79 LEU LEU A . n A 1 80 LYS 80 80 80 LYS LYS A . n A 1 81 THR 81 81 81 THR THR A . n A 1 82 LEU 82 82 82 LEU LEU A . n A 1 83 GLN 83 83 83 GLN GLN A . n A 1 84 PRO 84 84 84 PRO PRO A . n A 1 85 ASN 85 85 85 ASN ASN A . n A 1 86 LYS 86 86 86 LYS LYS A . n A 1 87 VAL 87 87 87 VAL VAL A . n A 1 88 ALA 88 88 88 ALA ALA A . n A 1 89 GLU 89 89 89 GLU GLU A . n A 1 90 MET 90 90 90 MET MET A . n A 1 91 ILE 91 91 91 ILE ILE A . n A 1 92 GLU 92 92 92 GLU GLU A . n A 1 93 ASN 93 93 93 ASN ASN A . n A 1 94 GLN 94 94 94 GLN GLN A . n A 1 95 GLY 95 95 95 GLY GLY A . n A 1 96 LEU 96 96 96 LEU LEU A . n A 1 97 PHE 97 97 97 PHE PHE A . n A 1 98 LYS 98 98 98 LYS LYS A . n A 1 99 ASP 99 99 99 ASP ASP A . n A 1 100 HIS 100 100 100 HIS HIS A . n A 1 101 VAL 101 101 101 VAL VAL A . n A 1 102 GLU 102 102 102 GLU GLU A . n A 1 103 ASP 103 103 103 ASP ASP A . n A 1 104 VAL 104 104 104 VAL VAL A . n A 1 105 ASN 105 105 105 ASN ASN A . n A 1 106 PHE 106 106 106 PHE PHE A . n A 1 107 GLN 107 107 107 GLN GLN A . n A 1 108 PRO 108 108 108 PRO PRO A . n A 1 109 VAL 109 109 109 VAL VAL A . n A 1 110 LYS 110 110 110 LYS LYS A . n A 1 111 TYR 111 111 111 TYR TYR A . n A 1 112 SER 112 112 112 SER SER A . n A 1 113 ALA 113 113 113 ALA ALA A . n A 1 114 LEU 114 114 ? ? ? A . n A 1 115 THR 115 115 ? ? ? A . n A 1 116 SER 116 116 ? ? ? A . n A 1 117 ASN 117 117 ? ? ? A . n A 1 118 ASN 118 118 ? ? ? A . n A 1 119 GLU 119 119 119 GLU GLU A . n A 1 120 GLU 120 120 120 GLU GLU A . n A 1 121 CME 121 121 121 CME CYB A . n A 1 122 THR 122 122 122 THR THR A . n A 1 123 ALA 123 123 123 ALA ALA A . n A 1 124 VAL 124 124 124 VAL VAL A . n A 1 125 VAL 125 125 125 VAL VAL A . n A 1 126 ALA 126 126 126 ALA ALA A . n A 1 127 ARG 127 127 127 ARG ARG A . n A 1 128 GLY 128 128 128 GLY GLY A . n A 1 129 GLY 129 129 129 GLY GLY A . n A 1 130 THR 130 130 130 THR THR A . n A 1 131 ALA 131 131 131 ALA ALA A . n A 1 132 ASN 132 132 132 ASN ASN A . n A 1 133 ALA 133 133 133 ALA ALA A . n A 1 134 ILE 134 134 134 ILE ILE A . n A 1 135 ARG 135 135 135 ARG ARG A . n A 1 136 ILE 136 136 136 ILE ILE A . n A 1 137 ALA 137 137 137 ALA ALA A . n A 1 138 ALA 138 138 138 ALA ALA A . n A 1 139 VAL 139 139 ? ? ? A . n A 1 140 ASP 140 140 ? ? ? A . n A 1 141 ASN 141 141 ? ? ? A . n A 1 142 PRO 142 142 ? ? ? A . n A 1 143 VAL 143 143 ? ? ? A . n A 1 144 ASN 144 144 ? ? ? A . n A 1 145 VAL 145 145 ? ? ? A . n A 1 146 ASN 146 146 ? ? ? A . n A 1 147 LYS 147 147 ? ? ? A . n A 1 148 LEU 148 148 ? ? ? A . n A 1 149 ALA 149 149 ? ? ? A . n A 1 150 GLN 150 150 ? ? ? A . n A 1 151 ASP 151 151 ? ? ? A . n A 1 152 SER 152 152 152 SER SER A . n A 1 153 ILE 153 153 153 ILE ILE A . n A 1 154 ASN 154 154 154 ASN ASN A . n A 1 155 ILE 155 155 155 ILE ILE A . n A 1 156 ALA 156 156 156 ALA ALA A . n A 1 157 GLN 157 157 157 GLN GLN A . n A 1 158 ILE 158 158 158 ILE ILE A . n A 1 159 VAL 159 159 159 VAL VAL A . n A 1 160 PRO 160 160 160 PRO PRO A . n A 1 161 MET 161 161 161 MET MET A . n A 1 162 ASP 162 162 162 ASP ASP A . n A 1 163 GLY 163 163 163 GLY GLY A . n A 1 164 PHE 164 164 164 PHE PHE A . n A 1 165 HIS 165 165 165 HIS HIS A . n A 1 166 LEU 166 166 166 LEU LEU A . n A 1 167 SER 167 167 167 SER SER A . n A 1 168 ARG 168 168 168 ARG ARG A . n A 1 169 ARG 169 169 169 ARG ARG A . n A 1 170 CYS 170 170 170 CYS CYS A . n A 1 171 LEU 171 171 171 LEU LEU A . n A 1 172 ASP 172 172 172 ASP ASP A . n A 1 173 LEU 173 173 173 LEU LEU A . n A 1 174 PHE 174 174 174 PHE PHE A . n A 1 175 LYS 175 175 175 LYS LYS A . n A 1 176 ASP 176 176 176 ASP ASP A . n A 1 177 PRO 177 177 177 PRO PRO A . n A 1 178 GLN 178 178 178 GLN GLN A . n A 1 179 THR 179 179 179 THR THR A . n A 1 180 ALA 180 180 180 ALA ALA A . n A 1 181 HIS 181 181 181 HIS HIS A . n A 1 182 LYS 182 182 182 LYS LYS A . n A 1 183 ARG 183 183 183 ARG ARG A . n A 1 184 ARG 184 184 184 ARG ARG A . n A 1 185 GLY 185 185 185 GLY GLY A . n A 1 186 SER 186 186 186 SER SER A . n A 1 187 PRO 187 187 187 PRO PRO A . n A 1 188 SER 188 188 188 SER SER A . n A 1 189 THR 189 189 189 THR THR A . n A 1 190 PHE 190 190 190 PHE PHE A . n A 1 191 ASP 191 191 191 ASP ASP A . n A 1 192 SER 192 192 192 SER SER A . n A 1 193 ASN 193 193 193 ASN ASN A . n A 1 194 ASN 194 194 194 ASN ASN A . n A 1 195 PHE 195 195 195 PHE PHE A . n A 1 196 LEU 196 196 196 LEU LEU A . n A 1 197 GLN 197 197 197 GLN GLN A . n A 1 198 LEU 198 198 198 LEU LEU A . n A 1 199 CYS 199 199 199 CYS CYS A . n A 1 200 LYS 200 200 200 LYS LYS A . n A 1 201 ILE 201 201 201 ILE ILE A . n A 1 202 LEU 202 202 202 LEU LEU A . n A 1 203 ALA 203 203 203 ALA ALA A . n A 1 204 LYS 204 204 204 LYS LYS A . n A 1 205 THR 205 205 205 THR THR A . n A 1 206 SER 206 206 206 SER SER A . n A 1 207 LEU 207 207 207 LEU LEU A . n A 1 208 CME 208 208 208 CME CYB A . n A 1 209 LYS 209 209 209 LYS LYS A . n A 1 210 VAL 210 210 210 VAL VAL A . n A 1 211 SER 211 211 211 SER SER A . n A 1 212 SER 212 212 ? ? ? A . n A 1 213 HIS 213 213 ? ? ? A . n A 1 214 HIS 214 214 ? ? ? A . n A 1 215 LYS 215 215 ? ? ? A . n A 1 216 PHE 216 216 ? ? ? A . n A 1 217 TYR 217 217 ? ? ? A . n A 1 218 SER 218 218 218 SER SER A . n A 1 219 THR 219 219 219 THR THR A . n A 1 220 SER 220 220 220 SER SER A . n A 1 221 SER 221 221 221 SER SER A . n A 1 222 VAL 222 222 222 VAL VAL A . n A 1 223 PHE 223 223 223 PHE PHE A . n A 1 224 GLU 224 224 224 GLU GLU A . n A 1 225 LYS 225 225 225 LYS LYS A . n A 1 226 LEU 226 226 226 LEU LEU A . n A 1 227 SER 227 227 227 SER SER A . n A 1 228 LYS 228 228 228 LYS LYS A . n A 1 229 THR 229 229 229 THR THR A . n A 1 230 PHE 230 230 230 PHE PHE A . n A 1 231 SER 231 231 231 SER SER A . n A 1 232 GLN 232 232 232 GLN GLN A . n A 1 233 THR 233 233 233 THR THR A . n A 1 234 ILE 234 234 234 ILE ILE A . n A 1 235 PRO 235 235 235 PRO PRO A . n A 1 236 ASP 236 236 236 ASP ASP A . n A 1 237 ILE 237 237 237 ILE ILE A . n A 1 238 PHE 238 238 238 PHE PHE A . n A 1 239 VAL 239 239 239 VAL VAL A . n A 1 240 PRO 240 240 240 PRO PRO A . n A 1 241 GLY 241 241 241 GLY GLY A . n A 1 242 PHE 242 242 242 PHE PHE A . n A 1 243 ASN 243 243 243 ASN ASN A . n A 1 244 HIS 244 244 244 HIS HIS A . n A 1 245 ALA 245 245 245 ALA ALA A . n A 1 246 LEU 246 246 246 LEU LEU A . n A 1 247 LYS 247 247 247 LYS LYS A . n A 1 248 ASP 248 248 248 ASP ASP A . n A 1 249 PRO 249 249 249 PRO PRO A . n A 1 250 THR 250 250 250 THR THR A . n A 1 251 PRO 251 251 251 PRO PRO A . n A 1 252 ASP 252 252 252 ASP ASP A . n A 1 253 GLN 253 253 253 GLN GLN A . n A 1 254 TYR 254 254 254 TYR TYR A . n A 1 255 CYS 255 255 255 CYS CYS A . n A 1 256 ILE 256 256 256 ILE ILE A . n A 1 257 SER 257 257 257 SER SER A . n A 1 258 LYS 258 258 258 LYS LYS A . n A 1 259 PHE 259 259 259 PHE PHE A . n A 1 260 THR 260 260 260 THR THR A . n A 1 261 ARG 261 261 261 ARG ARG A . n A 1 262 ILE 262 262 262 ILE ILE A . n A 1 263 VAL 263 263 263 VAL VAL A . n A 1 264 ILE 264 264 264 ILE ILE A . n A 1 265 LEU 265 265 265 LEU LEU A . n A 1 266 GLU 266 266 266 GLU GLU A . n A 1 267 GLY 267 267 267 GLY GLY A . n A 1 268 LEU 268 268 268 LEU LEU A . n A 1 269 TYR 269 269 269 TYR TYR A . n A 1 270 LEU 270 270 270 LEU LEU A . n A 1 271 LEU 271 271 271 LEU LEU A . n A 1 272 TYR 272 272 272 TYR TYR A . n A 1 273 ASP 273 273 273 ASP ASP A . n A 1 274 GLN 274 274 274 GLN GLN A . n A 1 275 GLU 275 275 275 GLU GLU A . n A 1 276 ASN 276 276 276 ASN ASN A . n A 1 277 TRP 277 277 277 TRP TRP A . n A 1 278 LYS 278 278 278 LYS LYS A . n A 1 279 LYS 279 279 279 LYS LYS A . n A 1 280 ILE 280 280 280 ILE ILE A . n A 1 281 TYR 281 281 281 TYR TYR A . n A 1 282 LYS 282 282 282 LYS LYS A . n A 1 283 THR 283 283 283 THR THR A . n A 1 284 LEU 284 284 284 LEU LEU A . n A 1 285 ALA 285 285 285 ALA ALA A . n A 1 286 ASP 286 286 286 ASP ASP A . n A 1 287 THR 287 287 287 THR THR A . n A 1 288 GLY 288 288 288 GLY GLY A . n A 1 289 ALA 289 289 289 ALA ALA A . n A 1 290 LEU 290 290 290 LEU LEU A . n A 1 291 LEU 291 291 291 LEU LEU A . n A 1 292 VAL 292 292 292 VAL VAL A . n A 1 293 TYR 293 293 293 TYR TYR A . n A 1 294 LYS 294 294 294 LYS LYS A . n A 1 295 ILE 295 295 295 ILE ILE A . n A 1 296 ASP 296 296 296 ASP ASP A . n A 1 297 ILE 297 297 297 ILE ILE A . n A 1 298 ASP 298 298 298 ASP ASP A . n A 1 299 TYR 299 299 299 TYR TYR A . n A 1 300 GLU 300 300 300 GLU GLU A . n A 1 301 ALA 301 301 301 ALA ALA A . n A 1 302 THR 302 302 302 THR THR A . n A 1 303 GLU 303 303 303 GLU GLU A . n A 1 304 GLU 304 304 304 GLU GLU A . n A 1 305 ARG 305 305 305 ARG ARG A . n A 1 306 VAL 306 306 306 VAL VAL A . n A 1 307 ALA 307 307 307 ALA ALA A . n A 1 308 LYS 308 308 308 LYS LYS A . n A 1 309 ARG 309 309 309 ARG ARG A . n A 1 310 HIS 310 310 310 HIS HIS A . n A 1 311 LEU 311 311 311 LEU LEU A . n A 1 312 GLN 312 312 312 GLN GLN A . n A 1 313 SER 313 313 313 SER SER A . n A 1 314 GLY 314 314 314 GLY GLY A . n A 1 315 LEU 315 315 315 LEU LEU A . n A 1 316 VAL 316 316 316 VAL VAL A . n A 1 317 THR 317 317 317 THR THR A . n A 1 318 THR 318 318 318 THR THR A . n A 1 319 ILE 319 319 319 ILE ILE A . n A 1 320 ALA 320 320 320 ALA ALA A . n A 1 321 GLU 321 321 321 GLU GLU A . n A 1 322 GLY 322 322 322 GLY GLY A . n A 1 323 ARG 323 323 323 ARG ARG A . n A 1 324 GLU 324 324 324 GLU GLU A . n A 1 325 LYS 325 325 325 LYS LYS A . n A 1 326 PHE 326 326 326 PHE PHE A . n A 1 327 ARG 327 327 327 ARG ARG A . n A 1 328 SER 328 328 328 SER SER A . n A 1 329 ASN 329 329 329 ASN ASN A . n A 1 330 ASP 330 330 330 ASP ASP A . n A 1 331 LEU 331 331 331 LEU LEU A . n A 1 332 LEU 332 332 332 LEU LEU A . n A 1 333 ASN 333 333 333 ASN ASN A . n A 1 334 GLY 334 334 334 GLY GLY A . n A 1 335 ARG 335 335 335 ARG ARG A . n A 1 336 ASP 336 336 336 ASP ASP A . n A 1 337 ILE 337 337 337 ILE ILE A . n A 1 338 ASP 338 338 338 ASP ASP A . n A 1 339 ASN 339 339 339 ASN ASN A . n A 1 340 HIS 340 340 340 HIS HIS A . n A 1 341 LEU 341 341 341 LEU LEU A . n A 1 342 ILE 342 342 342 ILE ILE A . n A 1 343 LYS 343 343 343 LYS LYS A . n A 1 344 VAL 344 344 344 VAL VAL A . n A 1 345 ASP 345 345 345 ASP ASP A . n A 1 346 ASN 346 346 346 ASN ASN A . n A 1 347 ILE 347 347 347 ILE ILE A . n A 1 348 VAL 348 348 348 VAL VAL A . n A 1 349 HIS 349 349 349 HIS HIS A . n A 1 350 ILE 350 350 350 ILE ILE A . n A 1 351 ARG 351 351 351 ARG ARG A . n A 1 352 ASN 352 352 352 ASN ASN A . n A 1 353 ASP 353 353 353 ASP ASP A . n A 1 354 HIS 354 354 354 HIS HIS A . n A 1 355 HIS 355 355 ? ? ? A . n A 1 356 HIS 356 356 ? ? ? A . n A 1 357 HIS 357 357 ? ? ? A . n A 1 358 HIS 358 358 ? ? ? A . n A 1 359 HIS 359 359 ? ? ? A . n # 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 CME 45 A CME 45 ? CYS 'S,S-(2-HYDROXYETHYL)THIOCYSTEINE' 2 A CME 121 A CME 121 ? CYS 'S,S-(2-HYDROXYETHYL)THIOCYSTEINE' 3 A CME 208 A CME 208 ? CYS 'S,S-(2-HYDROXYETHYL)THIOCYSTEINE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_defined_assembly _pdbx_struct_assembly.method_details ? _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2007-03-27 2 'Structure model' 1 1 2007-12-12 3 'Structure model' 1 2 2011-07-13 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal DENZO 'data reduction' . ? 1 SCALEPACK 'data scaling' . ? 2 CNS refinement . ? 3 CNS phasing . ? 4 # loop_ _pdbx_validate_rmsd_bond.id _pdbx_validate_rmsd_bond.PDB_model_num _pdbx_validate_rmsd_bond.auth_atom_id_1 _pdbx_validate_rmsd_bond.auth_asym_id_1 _pdbx_validate_rmsd_bond.auth_comp_id_1 _pdbx_validate_rmsd_bond.auth_seq_id_1 _pdbx_validate_rmsd_bond.PDB_ins_code_1 _pdbx_validate_rmsd_bond.label_alt_id_1 _pdbx_validate_rmsd_bond.auth_atom_id_2 _pdbx_validate_rmsd_bond.auth_asym_id_2 _pdbx_validate_rmsd_bond.auth_comp_id_2 _pdbx_validate_rmsd_bond.auth_seq_id_2 _pdbx_validate_rmsd_bond.PDB_ins_code_2 _pdbx_validate_rmsd_bond.label_alt_id_2 _pdbx_validate_rmsd_bond.bond_value _pdbx_validate_rmsd_bond.bond_target_value _pdbx_validate_rmsd_bond.bond_deviation _pdbx_validate_rmsd_bond.bond_standard_deviation _pdbx_validate_rmsd_bond.linker_flag 1 1 C A GLN 46 ? ? N A ILE 47 ? ? 1.177 1.336 -0.159 0.023 Y 2 1 C A CME 121 ? ? N A THR 122 ? ? 1.551 1.336 0.215 0.023 Y 3 1 C A LEU 207 ? ? N A CME 208 ? ? 1.138 1.336 -0.198 0.023 Y 4 1 C A LYS 209 ? ? N A VAL 210 ? ? 1.529 1.336 0.193 0.023 Y # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 CA A CME 45 ? ? C A CME 45 ? ? N A GLN 46 ? ? 100.35 117.20 -16.85 2.20 Y 2 1 C A CME 45 ? ? N A GLN 46 ? ? CA A GLN 46 ? ? 100.68 121.70 -21.02 2.50 Y 3 1 O A GLN 46 ? ? C A GLN 46 ? ? N A ILE 47 ? ? 110.91 122.70 -11.79 1.60 Y 4 1 C A HIS 59 ? ? N A PRO 60 ? ? CA A PRO 60 ? ? 129.43 119.30 10.13 1.50 Y 5 1 O A GLU 120 ? ? C A GLU 120 ? ? N A CME 121 ? ? 104.15 122.70 -18.55 1.60 Y 6 1 CA A CME 121 ? ? C A CME 121 ? ? N A THR 122 ? ? 98.58 117.20 -18.62 2.20 Y 7 1 O A CME 208 ? ? C A CME 208 ? ? N A LYS 209 ? ? 106.92 122.70 -15.78 1.60 Y # 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 ASN A 93 ? ? -86.80 41.94 2 1 TYR A 111 ? ? -171.16 149.48 3 1 CME A 121 ? ? 169.07 125.28 4 1 ALA A 126 ? ? -131.74 -149.42 5 1 CME A 208 ? ? -74.74 -165.39 6 1 ASP A 252 ? ? 32.42 54.55 7 1 ASP A 273 ? ? -75.53 25.01 8 1 GLU A 275 ? ? 35.23 -125.98 # loop_ _pdbx_validate_main_chain_plane.id _pdbx_validate_main_chain_plane.PDB_model_num _pdbx_validate_main_chain_plane.auth_comp_id _pdbx_validate_main_chain_plane.auth_asym_id _pdbx_validate_main_chain_plane.auth_seq_id _pdbx_validate_main_chain_plane.PDB_ins_code _pdbx_validate_main_chain_plane.label_alt_id _pdbx_validate_main_chain_plane.improper_torsion_angle 1 1 CME A 45 ? ? -13.97 2 1 GLN A 46 ? ? 19.64 3 1 GLU A 120 ? ? -18.38 4 1 CME A 121 ? ? 16.87 5 1 CME A 208 ? ? -17.65 6 1 LYS A 209 ? ? 14.02 # loop_ _pdbx_validate_polymer_linkage.id _pdbx_validate_polymer_linkage.PDB_model_num _pdbx_validate_polymer_linkage.auth_atom_id_1 _pdbx_validate_polymer_linkage.auth_asym_id_1 _pdbx_validate_polymer_linkage.auth_comp_id_1 _pdbx_validate_polymer_linkage.auth_seq_id_1 _pdbx_validate_polymer_linkage.PDB_ins_code_1 _pdbx_validate_polymer_linkage.label_alt_id_1 _pdbx_validate_polymer_linkage.auth_atom_id_2 _pdbx_validate_polymer_linkage.auth_asym_id_2 _pdbx_validate_polymer_linkage.auth_comp_id_2 _pdbx_validate_polymer_linkage.auth_seq_id_2 _pdbx_validate_polymer_linkage.PDB_ins_code_2 _pdbx_validate_polymer_linkage.label_alt_id_2 _pdbx_validate_polymer_linkage.dist 1 1 C A GLN 46 ? ? N A ILE 47 ? ? 1.18 2 1 C A LEU 207 ? ? N A CME 208 ? ? 1.14 # 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 MET 1 ? A MET 1 2 1 Y 1 A LEU 114 ? A LEU 114 3 1 Y 1 A THR 115 ? A THR 115 4 1 Y 1 A SER 116 ? A SER 116 5 1 Y 1 A ASN 117 ? A ASN 117 6 1 Y 1 A ASN 118 ? A ASN 118 7 1 Y 1 A VAL 139 ? A VAL 139 8 1 Y 1 A ASP 140 ? A ASP 140 9 1 Y 1 A ASN 141 ? A ASN 141 10 1 Y 1 A PRO 142 ? A PRO 142 11 1 Y 1 A VAL 143 ? A VAL 143 12 1 Y 1 A ASN 144 ? A ASN 144 13 1 Y 1 A VAL 145 ? A VAL 145 14 1 Y 1 A ASN 146 ? A ASN 146 15 1 Y 1 A LYS 147 ? A LYS 147 16 1 Y 1 A LEU 148 ? A LEU 148 17 1 Y 1 A ALA 149 ? A ALA 149 18 1 Y 1 A GLN 150 ? A GLN 150 19 1 Y 1 A ASP 151 ? A ASP 151 20 1 Y 1 A SER 212 ? A SER 212 21 1 Y 1 A HIS 213 ? A HIS 213 22 1 Y 1 A HIS 214 ? A HIS 214 23 1 Y 1 A LYS 215 ? A LYS 215 24 1 Y 1 A PHE 216 ? A PHE 216 25 1 Y 1 A TYR 217 ? A TYR 217 26 1 Y 1 A HIS 355 ? A HIS 355 27 1 Y 1 A HIS 356 ? A HIS 356 28 1 Y 1 A HIS 357 ? A HIS 357 29 1 Y 1 A HIS 358 ? A HIS 358 30 1 Y 1 A HIS 359 ? A HIS 359 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 'SULFATE ION' SO4 3 water HOH # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 SO4 1 2847 2847 SO4 SO4 A . C 3 HOH 1 2848 1 HOH HOH A . C 3 HOH 2 2849 2 HOH HOH A . C 3 HOH 3 2850 3 HOH HOH A . C 3 HOH 4 2851 4 HOH HOH A . C 3 HOH 5 2852 5 HOH HOH A . C 3 HOH 6 2853 6 HOH HOH A . C 3 HOH 7 2854 7 HOH HOH A . C 3 HOH 8 2855 8 HOH HOH A . C 3 HOH 9 2856 10 HOH HOH A . C 3 HOH 10 2857 11 HOH HOH A . C 3 HOH 11 2858 12 HOH HOH A . C 3 HOH 12 2859 13 HOH HOH A . C 3 HOH 13 2860 14 HOH HOH A . C 3 HOH 14 2861 15 HOH HOH A . C 3 HOH 15 2862 16 HOH HOH A . C 3 HOH 16 2863 17 HOH HOH A . C 3 HOH 17 2864 18 HOH HOH A . C 3 HOH 18 2865 19 HOH HOH A . C 3 HOH 19 2866 21 HOH HOH A . C 3 HOH 20 2867 22 HOH HOH A . C 3 HOH 21 2868 23 HOH HOH A . C 3 HOH 22 2869 25 HOH HOH A . C 3 HOH 23 2870 26 HOH HOH A . C 3 HOH 24 2871 27 HOH HOH A . C 3 HOH 25 2872 28 HOH HOH A . C 3 HOH 26 2873 30 HOH HOH A . C 3 HOH 27 2874 31 HOH HOH A . C 3 HOH 28 2875 50 HOH HOH A . C 3 HOH 29 2876 52 HOH HOH A . C 3 HOH 30 2877 53 HOH HOH A . C 3 HOH 31 2878 54 HOH HOH A . C 3 HOH 32 2879 55 HOH HOH A . C 3 HOH 33 2880 56 HOH HOH A . C 3 HOH 34 2881 57 HOH HOH A . C 3 HOH 35 2882 58 HOH HOH A . C 3 HOH 36 2883 59 HOH HOH A . C 3 HOH 37 2884 61 HOH HOH A . C 3 HOH 38 2885 62 HOH HOH A . C 3 HOH 39 2886 63 HOH HOH A . C 3 HOH 40 2887 64 HOH HOH A . C 3 HOH 41 2888 65 HOH HOH A . C 3 HOH 42 2889 66 HOH HOH A . C 3 HOH 43 2890 67 HOH HOH A . C 3 HOH 44 2891 68 HOH HOH A . C 3 HOH 45 2892 69 HOH HOH A . C 3 HOH 46 2893 71 HOH HOH A . C 3 HOH 47 2894 72 HOH HOH A . C 3 HOH 48 2895 73 HOH HOH A . C 3 HOH 49 2896 74 HOH HOH A . C 3 HOH 50 2897 75 HOH HOH A . C 3 HOH 51 2898 76 HOH HOH A . C 3 HOH 52 2899 77 HOH HOH A . C 3 HOH 53 2900 78 HOH HOH A . C 3 HOH 54 2901 79 HOH HOH A . C 3 HOH 55 2902 80 HOH HOH A . C 3 HOH 56 2903 81 HOH HOH A . C 3 HOH 57 2904 82 HOH HOH A . C 3 HOH 58 2905 83 HOH HOH A . C 3 HOH 59 2906 84 HOH HOH A . C 3 HOH 60 2907 85 HOH HOH A . C 3 HOH 61 2908 86 HOH HOH A . C 3 HOH 62 2909 87 HOH HOH A . C 3 HOH 63 2910 88 HOH HOH A . C 3 HOH 64 2911 89 HOH HOH A . C 3 HOH 65 2912 90 HOH HOH A . C 3 HOH 66 2913 91 HOH HOH A . C 3 HOH 67 2914 92 HOH HOH A . C 3 HOH 68 2915 93 HOH HOH A . C 3 HOH 69 2916 95 HOH HOH A . C 3 HOH 70 2917 96 HOH HOH A . C 3 HOH 71 2918 97 HOH HOH A . C 3 HOH 72 2919 98 HOH HOH A . C 3 HOH 73 2920 99 HOH HOH A . C 3 HOH 74 2921 100 HOH HOH A . C 3 HOH 75 2922 101 HOH HOH A . C 3 HOH 76 2923 102 HOH HOH A . C 3 HOH 77 2924 103 HOH HOH A . C 3 HOH 78 2925 104 HOH HOH A . C 3 HOH 79 2926 105 HOH HOH A . C 3 HOH 80 2927 106 HOH HOH A . C 3 HOH 81 2928 107 HOH HOH A . C 3 HOH 82 2929 108 HOH HOH A . C 3 HOH 83 2930 109 HOH HOH A . C 3 HOH 84 2931 110 HOH HOH A . C 3 HOH 85 2932 111 HOH HOH A . C 3 HOH 86 2933 112 HOH HOH A . C 3 HOH 87 2934 113 HOH HOH A . C 3 HOH 88 2935 114 HOH HOH A . C 3 HOH 89 2936 115 HOH HOH A . C 3 HOH 90 2937 116 HOH HOH A . C 3 HOH 91 2938 117 HOH HOH A . C 3 HOH 92 2939 118 HOH HOH A . C 3 HOH 93 2940 119 HOH HOH A . C 3 HOH 94 2941 120 HOH HOH A . C 3 HOH 95 2942 121 HOH HOH A . C 3 HOH 96 2943 122 HOH HOH A . C 3 HOH 97 2944 123 HOH HOH A . C 3 HOH 98 2945 124 HOH HOH A . C 3 HOH 99 2946 125 HOH HOH A . C 3 HOH 100 2947 126 HOH HOH A . C 3 HOH 101 2948 127 HOH HOH A . C 3 HOH 102 2949 128 HOH HOH A . C 3 HOH 103 2950 129 HOH HOH A . C 3 HOH 104 2951 130 HOH HOH A . C 3 HOH 105 2952 131 HOH HOH A . C 3 HOH 106 2953 132 HOH HOH A . C 3 HOH 107 2954 133 HOH HOH A . C 3 HOH 108 2955 135 HOH HOH A . C 3 HOH 109 2956 137 HOH HOH A . C 3 HOH 110 2957 138 HOH HOH A . C 3 HOH 111 2958 139 HOH HOH A . C 3 HOH 112 2959 140 HOH HOH A . C 3 HOH 113 2960 141 HOH HOH A . C 3 HOH 114 2961 142 HOH HOH A . C 3 HOH 115 2962 143 HOH HOH A . C 3 HOH 116 2963 144 HOH HOH A . C 3 HOH 117 2964 145 HOH HOH A . C 3 HOH 118 2965 146 HOH HOH A . C 3 HOH 119 2966 147 HOH HOH A . C 3 HOH 120 2967 148 HOH HOH A . C 3 HOH 121 2968 149 HOH HOH A . C 3 HOH 122 2969 150 HOH HOH A . C 3 HOH 123 2970 151 HOH HOH A . C 3 HOH 124 2971 152 HOH HOH A . C 3 HOH 125 2972 153 HOH HOH A . C 3 HOH 126 2973 154 HOH HOH A . C 3 HOH 127 2974 155 HOH HOH A . C 3 HOH 128 2975 156 HOH HOH A . C 3 HOH 129 2976 157 HOH HOH A . C 3 HOH 130 2977 158 HOH HOH A . C 3 HOH 131 2978 159 HOH HOH A . C 3 HOH 132 2979 160 HOH HOH A . C 3 HOH 133 2980 161 HOH HOH A . C 3 HOH 134 2981 162 HOH HOH A . C 3 HOH 135 2982 163 HOH HOH A . C 3 HOH 136 2983 164 HOH HOH A . C 3 HOH 137 2984 165 HOH HOH A . C 3 HOH 138 2985 166 HOH HOH A . C 3 HOH 139 2986 167 HOH HOH A . C 3 HOH 140 2987 168 HOH HOH A . C 3 HOH 141 2988 169 HOH HOH A . C 3 HOH 142 2989 170 HOH HOH A . C 3 HOH 143 2990 171 HOH HOH A . C 3 HOH 144 2991 172 HOH HOH A . C 3 HOH 145 2992 173 HOH HOH A . C 3 HOH 146 2993 174 HOH HOH A . C 3 HOH 147 2994 175 HOH HOH A . C 3 HOH 148 2995 176 HOH HOH A . C 3 HOH 149 2996 177 HOH HOH A . C 3 HOH 150 2997 178 HOH HOH A . C 3 HOH 151 2998 179 HOH HOH A . C 3 HOH 152 2999 180 HOH HOH A . C 3 HOH 153 3000 181 HOH HOH A . C 3 HOH 154 3001 182 HOH HOH A . C 3 HOH 155 3002 184 HOH HOH A . C 3 HOH 156 3003 185 HOH HOH A . C 3 HOH 157 3004 186 HOH HOH A . C 3 HOH 158 3005 187 HOH HOH A . C 3 HOH 159 3006 188 HOH HOH A . C 3 HOH 160 3007 189 HOH HOH A . C 3 HOH 161 3008 290 HOH HOH A . C 3 HOH 162 3009 291 HOH HOH A . C 3 HOH 163 3010 292 HOH HOH A . C 3 HOH 164 3011 293 HOH HOH A . C 3 HOH 165 3012 190 HOH HOH A . C 3 HOH 166 3013 191 HOH HOH A . C 3 HOH 167 3014 192 HOH HOH A . C 3 HOH 168 3015 193 HOH HOH A . C 3 HOH 169 3016 194 HOH HOH A . C 3 HOH 170 3017 195 HOH HOH A . C 3 HOH 171 3018 196 HOH HOH A . C 3 HOH 172 3019 197 HOH HOH A . C 3 HOH 173 3020 198 HOH HOH A . C 3 HOH 174 3021 199 HOH HOH A . C 3 HOH 175 3022 200 HOH HOH A . C 3 HOH 176 3023 201 HOH HOH A . C 3 HOH 177 3024 203 HOH HOH A . C 3 HOH 178 3025 204 HOH HOH A . C 3 HOH 179 3026 205 HOH HOH A . C 3 HOH 180 3027 206 HOH HOH A . #