data_3M5Q # _entry.id 3M5Q # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.287 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 3M5Q RCSB RCSB058141 WWPDB D_1000058141 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 1MNP . unspecified PDB 1YYD . unspecified PDB 1YYG . unspecified PDB 1YZP . unspecified PDB 1YZR . unspecified PDB 3M8M . unspecified # _pdbx_database_status.entry_id 3M5Q _pdbx_database_status.status_code REL _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.recvd_initial_deposition_date 2010-03-12 _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 ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Sundaramoorthy, M.' 1 'Gold, M.H.' 2 'Poulos, T.L.' 3 # loop_ _citation.id _citation.title _citation.journal_abbrev _citation.journal_volume _citation.page_first _citation.page_last _citation.year _citation.journal_id_ASTM _citation.country _citation.journal_id_ISSN _citation.journal_id_CSD _citation.book_publisher _citation.pdbx_database_id_PubMed _citation.pdbx_database_id_DOI primary ;Ultrahigh (0.93A) resolution structure of manganese peroxidase from Phanerochaete chrysosporium: implications for the catalytic mechanism. ; J.Inorg.Biochem. 104 683 690 2010 JIBIDJ US 0162-0134 0525 ? 20356630 10.1016/j.jinorgbio.2010.02.011 1 'High-resolution crystal structure of manganese peroxidase: substrate and inhibitor complexes.' Biochemistry 44 6463 6470 2005 BICHAW US 0006-2960 0033 ? 15850380 10.1021/bi047318e 2 'The crystal structure of manganese peroxidase from Phanerochaete chrysosporium at 2.06-A resolution.' J.Biol.Chem. 269 32759 32767 1994 JBCHA3 US 0021-9258 0071 ? 7806497 ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Sundaramoorthy, M.' 1 primary 'Gold, M.H.' 2 primary 'Poulos, T.L.' 3 1 'Sundaramoorthy, M.' 4 1 'Youngs, H.L.' 5 1 'Gold, M.H.' 6 1 'Poulos, T.L.' 7 2 'Sundaramoorthy, M.' 8 2 'Kishi, K.' 9 2 'Gold, M.H.' 10 2 'Poulos, T.L.' 11 # _cell.entry_id 3M5Q _cell.length_a 160.570 _cell.length_b 45.300 _cell.length_c 52.830 _cell.angle_alpha 90.000 _cell.angle_beta 97.310 _cell.angle_gamma 90.000 _cell.pdbx_unique_axis ? _cell.Z_PDB 4 _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 3M5Q _symmetry.space_group_name_H-M 'C 1 2 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.Int_Tables_number 5 _symmetry.cell_setting ? _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 nat 'Manganese peroxidase 1' 37482.973 1 1.11.1.13 ? ? ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 2 ? ? ? ? 3 non-polymer man ALPHA-D-MANNOSE 180.156 1 ? ? ? ? 4 non-polymer syn 'CALCIUM ION' 40.078 2 ? ? ? ? 5 non-polymer syn 'MANGANESE (II) ION' 54.938 1 ? ? ? ? 6 non-polymer syn GLYCEROL 92.094 1 ? ? ? ? 7 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487 1 ? ? ? ? 8 water nat water 18.015 476 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'MnP-1, MnP1, Manganese peroxidase isozyme 1, Peroxidase manganese-dependent 1, Peroxidase manganese-dependent I' # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer no _entity_poly.pdbx_seq_one_letter_code ;AVCPDGTRVSHAACCAFIPLAQDLQETIFQNECGEDAHEVIRLTFHDAIAISRSQGPKAGGGADGSMLLFPTVEPNFSAN NGIDDSVNNLIPFMQKHNTISAADLVQFAGAVALSNCPGAPRLEFLAGRPNKTIAAVDGLIPEPQDSVTKILQRFEDAGG FTPFEVVSLLASHSVARADKVDQTIDAAPFDSTPFTFDTQVFLEVLLKGVGFPGSANNTGEVASPLPLGSGSDTGEMRLQ SDFALAHDPRTACIWQGFVNEQAFMAASFRAAMSKLAVLGHNRNSLIDCSDVVPVPKPATGQPAMFPASTGPQDLELSCP SERFPTLTTQPGASQSLIAHCPDGSMSCPGVQFNGPA ; _entity_poly.pdbx_seq_one_letter_code_can ;AVCPDGTRVSHAACCAFIPLAQDLQETIFQNECGEDAHEVIRLTFHDAIAISRSQGPKAGGGADGSMLLFPTVEPNFSAN NGIDDSVNNLIPFMQKHNTISAADLVQFAGAVALSNCPGAPRLEFLAGRPNKTIAAVDGLIPEPQDSVTKILQRFEDAGG FTPFEVVSLLASHSVARADKVDQTIDAAPFDSTPFTFDTQVFLEVLLKGVGFPGSANNTGEVASPLPLGSGSDTGEMRLQ SDFALAHDPRTACIWQGFVNEQAFMAASFRAAMSKLAVLGHNRNSLIDCSDVVPVPKPATGQPAMFPASTGPQDLELSCP SERFPTLTTQPGASQSLIAHCPDGSMSCPGVQFNGPA ; _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 ALA n 1 2 VAL n 1 3 CYS n 1 4 PRO n 1 5 ASP n 1 6 GLY n 1 7 THR n 1 8 ARG n 1 9 VAL n 1 10 SER n 1 11 HIS n 1 12 ALA n 1 13 ALA n 1 14 CYS n 1 15 CYS n 1 16 ALA n 1 17 PHE n 1 18 ILE n 1 19 PRO n 1 20 LEU n 1 21 ALA n 1 22 GLN n 1 23 ASP n 1 24 LEU n 1 25 GLN n 1 26 GLU n 1 27 THR n 1 28 ILE n 1 29 PHE n 1 30 GLN n 1 31 ASN n 1 32 GLU n 1 33 CYS n 1 34 GLY n 1 35 GLU n 1 36 ASP n 1 37 ALA n 1 38 HIS n 1 39 GLU n 1 40 VAL n 1 41 ILE n 1 42 ARG n 1 43 LEU n 1 44 THR n 1 45 PHE n 1 46 HIS n 1 47 ASP n 1 48 ALA n 1 49 ILE n 1 50 ALA n 1 51 ILE n 1 52 SER n 1 53 ARG n 1 54 SER n 1 55 GLN n 1 56 GLY n 1 57 PRO n 1 58 LYS n 1 59 ALA n 1 60 GLY n 1 61 GLY n 1 62 GLY n 1 63 ALA n 1 64 ASP n 1 65 GLY n 1 66 SER n 1 67 MET n 1 68 LEU n 1 69 LEU n 1 70 PHE n 1 71 PRO n 1 72 THR n 1 73 VAL n 1 74 GLU n 1 75 PRO n 1 76 ASN n 1 77 PHE n 1 78 SER n 1 79 ALA n 1 80 ASN n 1 81 ASN n 1 82 GLY n 1 83 ILE n 1 84 ASP n 1 85 ASP n 1 86 SER n 1 87 VAL n 1 88 ASN n 1 89 ASN n 1 90 LEU n 1 91 ILE n 1 92 PRO n 1 93 PHE n 1 94 MET n 1 95 GLN n 1 96 LYS n 1 97 HIS n 1 98 ASN n 1 99 THR n 1 100 ILE n 1 101 SER n 1 102 ALA n 1 103 ALA n 1 104 ASP n 1 105 LEU n 1 106 VAL n 1 107 GLN n 1 108 PHE n 1 109 ALA n 1 110 GLY n 1 111 ALA n 1 112 VAL n 1 113 ALA n 1 114 LEU n 1 115 SER n 1 116 ASN n 1 117 CYS n 1 118 PRO n 1 119 GLY n 1 120 ALA n 1 121 PRO n 1 122 ARG n 1 123 LEU n 1 124 GLU n 1 125 PHE n 1 126 LEU n 1 127 ALA n 1 128 GLY n 1 129 ARG n 1 130 PRO n 1 131 ASN n 1 132 LYS n 1 133 THR n 1 134 ILE n 1 135 ALA n 1 136 ALA n 1 137 VAL n 1 138 ASP n 1 139 GLY n 1 140 LEU n 1 141 ILE n 1 142 PRO n 1 143 GLU n 1 144 PRO n 1 145 GLN n 1 146 ASP n 1 147 SER n 1 148 VAL n 1 149 THR n 1 150 LYS n 1 151 ILE n 1 152 LEU n 1 153 GLN n 1 154 ARG n 1 155 PHE n 1 156 GLU n 1 157 ASP n 1 158 ALA n 1 159 GLY n 1 160 GLY n 1 161 PHE n 1 162 THR n 1 163 PRO n 1 164 PHE n 1 165 GLU n 1 166 VAL n 1 167 VAL n 1 168 SER n 1 169 LEU n 1 170 LEU n 1 171 ALA n 1 172 SER n 1 173 HIS n 1 174 SER n 1 175 VAL n 1 176 ALA n 1 177 ARG n 1 178 ALA n 1 179 ASP n 1 180 LYS n 1 181 VAL n 1 182 ASP n 1 183 GLN n 1 184 THR n 1 185 ILE n 1 186 ASP n 1 187 ALA n 1 188 ALA n 1 189 PRO n 1 190 PHE n 1 191 ASP n 1 192 SER n 1 193 THR n 1 194 PRO n 1 195 PHE n 1 196 THR n 1 197 PHE n 1 198 ASP n 1 199 THR n 1 200 GLN n 1 201 VAL n 1 202 PHE n 1 203 LEU n 1 204 GLU n 1 205 VAL n 1 206 LEU n 1 207 LEU n 1 208 LYS n 1 209 GLY n 1 210 VAL n 1 211 GLY n 1 212 PHE n 1 213 PRO n 1 214 GLY n 1 215 SER n 1 216 ALA n 1 217 ASN n 1 218 ASN n 1 219 THR n 1 220 GLY n 1 221 GLU n 1 222 VAL n 1 223 ALA n 1 224 SER n 1 225 PRO n 1 226 LEU n 1 227 PRO n 1 228 LEU n 1 229 GLY n 1 230 SER n 1 231 GLY n 1 232 SER n 1 233 ASP n 1 234 THR n 1 235 GLY n 1 236 GLU n 1 237 MET n 1 238 ARG n 1 239 LEU n 1 240 GLN n 1 241 SER n 1 242 ASP n 1 243 PHE n 1 244 ALA n 1 245 LEU n 1 246 ALA n 1 247 HIS n 1 248 ASP n 1 249 PRO n 1 250 ARG n 1 251 THR n 1 252 ALA n 1 253 CYS n 1 254 ILE n 1 255 TRP n 1 256 GLN n 1 257 GLY n 1 258 PHE n 1 259 VAL n 1 260 ASN n 1 261 GLU n 1 262 GLN n 1 263 ALA n 1 264 PHE n 1 265 MET n 1 266 ALA n 1 267 ALA n 1 268 SER n 1 269 PHE n 1 270 ARG n 1 271 ALA n 1 272 ALA n 1 273 MET n 1 274 SER n 1 275 LYS n 1 276 LEU n 1 277 ALA n 1 278 VAL n 1 279 LEU n 1 280 GLY n 1 281 HIS n 1 282 ASN n 1 283 ARG n 1 284 ASN n 1 285 SER n 1 286 LEU n 1 287 ILE n 1 288 ASP n 1 289 CYS n 1 290 SER n 1 291 ASP n 1 292 VAL n 1 293 VAL n 1 294 PRO n 1 295 VAL n 1 296 PRO n 1 297 LYS n 1 298 PRO n 1 299 ALA n 1 300 THR n 1 301 GLY n 1 302 GLN n 1 303 PRO n 1 304 ALA n 1 305 MET n 1 306 PHE n 1 307 PRO n 1 308 ALA n 1 309 SER n 1 310 THR n 1 311 GLY n 1 312 PRO n 1 313 GLN n 1 314 ASP n 1 315 LEU n 1 316 GLU n 1 317 LEU n 1 318 SER n 1 319 CYS n 1 320 PRO n 1 321 SER n 1 322 GLU n 1 323 ARG n 1 324 PHE n 1 325 PRO n 1 326 THR n 1 327 LEU n 1 328 THR n 1 329 THR n 1 330 GLN n 1 331 PRO n 1 332 GLY n 1 333 ALA n 1 334 SER n 1 335 GLN n 1 336 SER n 1 337 LEU n 1 338 ILE n 1 339 ALA n 1 340 HIS n 1 341 CYS n 1 342 PRO n 1 343 ASP n 1 344 GLY n 1 345 SER n 1 346 MET n 1 347 SER n 1 348 CYS n 1 349 PRO n 1 350 GLY n 1 351 VAL n 1 352 GLN n 1 353 PHE n 1 354 ASN n 1 355 GLY n 1 356 PRO n 1 357 ALA n # _entity_src_nat.entity_id 1 _entity_src_nat.pdbx_src_id 1 _entity_src_nat.pdbx_alt_source_flag sample _entity_src_nat.pdbx_beg_seq_num ? _entity_src_nat.pdbx_end_seq_num ? _entity_src_nat.common_name 'White-rot fungus' _entity_src_nat.pdbx_organism_scientific 'Phanerochaete chrysosporium' _entity_src_nat.pdbx_ncbi_taxonomy_id 5306 _entity_src_nat.genus ? _entity_src_nat.species ? _entity_src_nat.strain ? _entity_src_nat.tissue ? _entity_src_nat.tissue_fraction ? _entity_src_nat.pdbx_secretion ? _entity_src_nat.pdbx_fragment ? _entity_src_nat.pdbx_variant ? _entity_src_nat.pdbx_cell_line ? _entity_src_nat.pdbx_atcc ? _entity_src_nat.pdbx_cellular_location ? _entity_src_nat.pdbx_organ ? _entity_src_nat.pdbx_organelle ? _entity_src_nat.pdbx_cell ? _entity_src_nat.pdbx_plasmid_name ? _entity_src_nat.pdbx_plasmid_details ? _entity_src_nat.details ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code PEM1_PHACH _struct_ref.pdbx_db_accession Q02567 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;AVCPDGTRVSHAACCAFIPLAQDLQETIFQNECGEDAHEVIRLTFHDAIAISRSQGPKAGGGADGSMLLFPTVEPNFSAN NGIDDSVNNLIPFMQKHNTISAADLVQFAGAVALSNCPGAPRLEFLAGRPNKTIAAVDGLIPEPQDSVTKILQRFEDAGG FTPFEVVSLLASHSVARADKVDQTIDAAPFDSTPFTFDTQVFLEVLLKGVGFPGSANNTGEVASPLPLGSGSDTGEMRLQ SDFALAHDPRTACIWQGFVNEQAFMAASFRAAMSKLAVLGHNRNSLIDCSDVVPVPKPATGQPAMFPASTGPQDLELSCP SERFPTLTTQPGASQSLIAHCPDGSMSCPGVQFNGPA ; _struct_ref.pdbx_align_begin 22 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 3M5Q _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 357 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession Q02567 _struct_ref_seq.db_align_beg 22 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 378 _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 357 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CA non-polymer . 'CALCIUM ION' ? 'Ca 2' 40.078 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 HEM non-polymer . 'PROTOPORPHYRIN IX CONTAINING FE' HEME 'C34 H32 Fe N4 O4' 616.487 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 MN non-polymer . 'MANGANESE (II) ION' ? 'Mn 2' 54.938 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.crystals_number 1 _exptl.entry_id 3M5Q _exptl.method 'X-RAY DIFFRACTION' # _exptl_crystal.id 1 _exptl_crystal.density_Matthews 2.54 _exptl_crystal.density_meas ? _exptl_crystal.density_percent_sol 51.62 _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.pH 6.5 _exptl_crystal_grow.temp 298 _exptl_crystal_grow.pdbx_details '20% PEG 8000, 0.2 M ammonium sulfate, 0.1 M sodium cacodylate, pH 6.5, Vapor diffusion, hanging drop, temperature 298K' _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.id 1 _diffrn.ambient_temp 110 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector 'IMAGE PLATE' _diffrn_detector.type 'MAR scanner 345 mm plate' _diffrn_detector.pdbx_collection_date 1999-06-01 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.monochromator GRAPHITE _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.08 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'SSRL BEAMLINE BL7-1' _diffrn_source.pdbx_wavelength_list 1.08 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_synchrotron_site SSRL _diffrn_source.pdbx_synchrotron_beamline BL7-1 # _reflns.entry_id 3M5Q _reflns.observed_criterion_sigma_F 1.4 _reflns.observed_criterion_sigma_I 2 _reflns.d_resolution_high 0.93 _reflns.d_resolution_low 160 _reflns.number_all ? _reflns.number_obs 264958 _reflns.percent_possible_obs 93.0 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value 0.066 _reflns.pdbx_netI_over_sigmaI 26.3 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 4.9 _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 0.93 _reflns_shell.d_res_low 0.95 _reflns_shell.number_measured_obs ? _reflns_shell.number_measured_all ? _reflns_shell.number_unique_obs ? _reflns_shell.Rmerge_I_obs ? _reflns_shell.meanI_over_sigI_obs 1.9 _reflns_shell.pdbx_Rsym_value 0.512 _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_redundancy 2.0 _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.percent_possible_all 93.0 _reflns_shell.pdbx_diffrn_id ? _reflns_shell.pdbx_ordinal 1 # _refine.entry_id 3M5Q _refine.ls_d_res_high 0.930 _refine.ls_d_res_low 8.000 _refine.pdbx_ls_sigma_F 2 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.ls_percent_reflns_obs 96.700 _refine.ls_number_reflns_obs 191300 _refine.ls_number_reflns_all 243170 _refine.pdbx_ls_cross_valid_method 'FREE R' _refine.pdbx_R_Free_selection_details RANDOM _refine.details 'ANISOTROPIC REFINEMENT REDUCED FREE R (NO CUTOFF) BY 3.6%' _refine.ls_R_factor_all 0.124 _refine.ls_R_factor_obs ? _refine.ls_R_factor_R_work 0.107 _refine.ls_wR_factor_R_work ? _refine.ls_R_factor_R_free 0.134 _refine.ls_wR_factor_R_free ? _refine.ls_percent_reflns_R_free 2.0 _refine.ls_number_reflns_R_free 3967 _refine.ls_R_factor_R_free_error ? _refine.B_iso_mean 13.927 _refine.solvent_model_param_bsol ? _refine.solvent_model_param_ksol ? _refine.pdbx_isotropic_thermal_model ? _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.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML ? _refine.overall_SU_B ? _refine.solvent_model_details 'MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-228' _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.ls_number_parameters 29226 _refine.ls_number_restraints 35571 _refine.pdbx_starting_model 1YYD _refine.pdbx_method_to_determine_struct 'FOURIER SYNTHESIS' _refine.pdbx_stereochemistry_target_values 'ENGH AND HUBER' _refine.pdbx_stereochem_target_val_spec_case ? _refine.overall_FOM_work_R_set ? _refine.B_iso_max 126.62 _refine.B_iso_min 5.42 _refine.occupancy_max 1.02 _refine.occupancy_min 0.52 _refine.pdbx_ls_sigma_I 4 _refine.ls_redundancy_reflns_obs ? _refine.ls_R_factor_R_free_error_details ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.overall_FOM_free_R_set ? _refine.pdbx_overall_phase_error ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_overall_ESU_R ? _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 2629 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 91 _refine_hist.number_atoms_solvent 476 _refine_hist.number_atoms_total 3196 _refine_hist.d_res_high 0.930 _refine_hist.d_res_low 8.000 # loop_ _refine_ls_restr.type _refine_ls_restr.number _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function s_bond_d ? 0.018 ? ? 'X-RAY DIFFRACTION' ? s_angle_d ? 0.033 ? ? 'X-RAY DIFFRACTION' ? s_similar_dist ? 0.000 ? ? 'X-RAY DIFFRACTION' ? s_from_restr_planes ? 0.028 ? ? 'X-RAY DIFFRACTION' ? s_zero_chiral_vol ? 0.096 ? ? 'X-RAY DIFFRACTION' ? s_non_zero_chiral_vol ? 0.106 ? ? 'X-RAY DIFFRACTION' ? s_anti_bump_dis_restr ? 0.062 ? ? 'X-RAY DIFFRACTION' ? s_rigid_bond_adp_cmpnt ? 0.007 ? ? 'X-RAY DIFFRACTION' ? s_similar_adp_cmpnt ? 0.050 ? ? 'X-RAY DIFFRACTION' ? s_approx_iso_adps ? 0.112 ? ? 'X-RAY DIFFRACTION' ? # _pdbx_refine.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine.R_factor_all_4sig_cutoff 0.107 _pdbx_refine.R_factor_all_no_cutoff 0.124 _pdbx_refine.free_R_val_test_set_size_perc_4sig_cutoff 0.000 _pdbx_refine.free_R_val_test_set_size_perc_no_cutoff 0.000 _pdbx_refine.number_reflns_obs_4sig_cutoff 191300 _pdbx_refine.entry_id 3M5Q _pdbx_refine.R_factor_obs_no_cutoff ? _pdbx_refine.free_R_factor_no_cutoff ? _pdbx_refine.free_R_error_no_cutoff ? _pdbx_refine.free_R_val_test_set_ct_no_cutoff ? _pdbx_refine.R_factor_obs_4sig_cutoff ? _pdbx_refine.free_R_factor_4sig_cutoff ? _pdbx_refine.free_R_val_test_set_ct_4sig_cutoff ? # _struct.entry_id 3M5Q _struct.title '0.93 A Structure of Manganese-Bound Manganese Peroxidase' _struct.pdbx_descriptor '0.93 A Structure of Manganese-Bound Manganese Peroxidase' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3M5Q _struct_keywords.text ;Peroxidase, Heme, Mn(II)-binding site, Ca(II)-binding site, Glycosylation, Ultrahigh resolution, Calcium, Disulfide bond, Glycoprotein, Hydrogen peroxide, Iron, Lignin degradation, Manganese, Metal-binding, Oxidoreductase, Secreted ; _struct_keywords.pdbx_keywords OXIDOREDUCTASE # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 2 ? D N N 3 ? E N N 4 ? F N N 4 ? G N N 5 ? H N N 6 ? I N N 7 ? J N N 8 ? # _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 HIS A 11 ? CYS A 15 ? HIS A 11 CYS A 15 5 ? 5 HELX_P HELX_P2 2 ALA A 16 ? ILE A 28 ? ALA A 16 ILE A 28 1 ? 13 HELX_P HELX_P3 3 GLY A 34 ? ALA A 50 ? GLY A 34 ALA A 50 1 ? 17 HELX_P HELX_P4 4 GLY A 56 ? GLY A 60 ? GLY A 56 GLY A 60 5 ? 5 HELX_P HELX_P5 5 GLY A 65 ? PHE A 70 ? GLY A 65 PHE A 70 1 ? 6 HELX_P HELX_P6 6 VAL A 73 ? ASN A 81 ? VAL A 73 ASN A 81 5 ? 9 HELX_P HELX_P7 7 ILE A 83 ? HIS A 97 ? ILE A 83 HIS A 97 1 ? 15 HELX_P HELX_P8 8 SER A 101 ? ASN A 116 ? SER A 101 ASN A 116 1 ? 16 HELX_P HELX_P9 9 SER A 147 ? GLY A 160 ? SER A 147 GLY A 160 1 ? 14 HELX_P HELX_P10 10 THR A 162 ? LEU A 170 ? THR A 162 LEU A 170 1 ? 9 HELX_P HELX_P11 11 ALA A 171 ? VAL A 175 ? ALA A 171 VAL A 175 5 ? 5 HELX_P HELX_P12 12 THR A 199 ? LEU A 206 ? THR A 199 LEU A 206 1 ? 8 HELX_P HELX_P13 13 GLN A 240 ? ASP A 248 ? GLN A 240 ASP A 248 1 ? 9 HELX_P HELX_P14 14 THR A 251 ? PHE A 258 ? THR A 251 PHE A 258 1 ? 8 HELX_P HELX_P15 15 GLU A 261 ? ALA A 277 ? GLU A 261 ALA A 277 1 ? 17 HELX_P HELX_P16 16 ASN A 282 ? LEU A 286 ? ASN A 282 LEU A 286 5 ? 5 HELX_P HELX_P17 17 SER A 290 ? VAL A 293 ? SER A 290 VAL A 293 5 ? 4 HELX_P HELX_P18 18 GLY A 311 ? LEU A 315 ? GLY A 311 LEU A 315 5 ? 5 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 3 SG A ? ? 1_555 A CYS 15 SG ? ? A CYS 3 A CYS 15 1_555 ? ? ? ? ? ? ? 2.162 ? disulf2 disulf ? ? A CYS 14 SG A ? ? 1_555 A CYS 289 SG ? ? A CYS 14 A CYS 289 1_555 ? ? ? ? ? ? ? 2.058 ? disulf3 disulf ? ? A CYS 33 SG ? ? ? 1_555 A CYS 117 SG ? ? A CYS 33 A CYS 117 1_555 ? ? ? ? ? ? ? 2.080 ? disulf4 disulf ? ? A CYS 253 SG A ? ? 1_555 A CYS 319 SG ? ? A CYS 253 A CYS 319 1_555 ? ? ? ? ? ? ? 2.115 ? disulf5 disulf ? ? A CYS 341 SG ? ? ? 1_555 A CYS 348 SG ? ? A CYS 341 A CYS 348 1_555 ? ? ? ? ? ? ? 2.049 ? covale1 covale ? ? B NAG . O4 ? ? ? 1_555 C NAG . C1 ? ? A NAG 361 A NAG 362 1_555 ? ? ? ? ? ? ? 1.400 ? covale2 covale ? ? A ASN 131 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 131 A NAG 361 1_555 ? ? ? ? ? ? ? 1.453 ? metalc1 metalc ? ? A HIS 173 NE2 ? ? ? 1_555 I HEM . FE ? ? A HIS 173 A HEM 396 1_555 ? ? ? ? ? ? ? 2.076 ? metalc2 metalc ? ? G MN . MN ? ? ? 1_555 I HEM . O1D ? ? A MN 381 A HEM 396 1_555 ? ? ? ? ? ? ? 2.131 ? metalc3 metalc ? ? A GLU 39 OE2 ? ? ? 1_555 G MN . MN ? ? A GLU 39 A MN 381 1_555 ? ? ? ? ? ? ? 2.140 ? metalc4 metalc ? ? G MN . MN ? ? ? 1_555 J HOH . O ? ? A MN 381 A HOH 1040 1_555 ? ? ? ? ? ? ? 2.259 ? metalc5 metalc ? ? G MN . MN ? ? ? 1_555 J HOH . O ? ? A MN 381 A HOH 1108 1_555 ? ? ? ? ? ? ? 2.263 ? metalc6 metalc ? ? A ASP 179 OD2 ? ? ? 1_555 G MN . MN ? ? A ASP 179 A MN 381 1_555 ? ? ? ? ? ? ? 2.266 ? metalc7 metalc ? ? A GLU 35 OE1 ? ? ? 1_555 G MN . MN ? ? A GLU 35 A MN 381 1_555 ? ? ? ? ? ? ? 2.272 ? metalc8 metalc ? ? A ASP 47 OD2 ? ? ? 1_555 F CA . CA ? ? A ASP 47 A CA 372 1_555 ? ? ? ? ? ? ? 2.306 ? metalc9 metalc ? ? F CA . CA ? ? ? 1_555 J HOH . O ? ? A CA 372 A HOH 1127 1_555 ? ? ? ? ? ? ? 2.329 ? metalc10 metalc ? ? A SER 174 O ? ? ? 1_555 E CA . CA ? ? A SER 174 A CA 371 1_555 ? ? ? ? ? ? ? 2.367 ? metalc11 metalc ? ? A THR 193 O ? ? ? 1_555 E CA . CA ? ? A THR 193 A CA 371 1_555 ? ? ? ? ? ? ? 2.379 ? metalc12 metalc ? ? F CA . CA ? ? ? 1_555 J HOH . O ? ? A CA 372 A HOH 1085 1_555 ? ? ? ? ? ? ? 2.408 ? metalc13 metalc ? ? A ASP 64 OD1 ? ? ? 1_555 F CA . CA ? ? A ASP 64 A CA 372 1_555 ? ? ? ? ? ? ? 2.423 ? metalc14 metalc ? ? A ASP 191 OD2 ? ? ? 1_555 E CA . CA ? ? A ASP 191 A CA 371 1_555 ? ? ? ? ? ? ? 2.438 ? metalc15 metalc ? ? A ASP 47 O ? ? ? 1_555 F CA . CA ? ? A ASP 47 A CA 372 1_555 ? ? ? ? ? ? ? 2.440 ? metalc16 metalc ? ? A ASP 198 OD1 ? ? ? 1_555 E CA . CA ? ? A ASP 198 A CA 371 1_555 ? ? ? ? ? ? ? 2.457 ? metalc17 metalc ? ? A GLY 62 O ? ? ? 1_555 F CA . CA ? ? A GLY 62 A CA 372 1_555 ? ? ? ? ? ? ? 2.459 ? metalc18 metalc ? ? A SER 174 OG ? ? ? 1_555 E CA . CA ? ? A SER 174 A CA 371 1_555 ? ? ? ? ? ? ? 2.473 ? metalc19 metalc ? ? A SER 66 OG ? ? ? 1_555 F CA . CA ? ? A SER 66 A CA 372 1_555 ? ? ? ? ? ? ? 2.489 ? metalc20 metalc ? ? A THR 193 OG1 ? ? ? 1_555 E CA . CA ? ? A THR 193 A CA 371 1_555 ? ? ? ? ? ? ? 2.492 ? metalc21 metalc ? ? A THR 196 O ? ? ? 1_555 E CA . CA ? ? A THR 196 A CA 371 1_555 ? ? ? ? ? ? ? 2.513 ? metalc22 metalc ? ? I HEM . FE ? ? ? 1_555 J HOH . O ? ? A HEM 396 A HOH 1137 1_555 ? ? ? ? ? ? ? 2.569 ? metalc23 metalc ? ? A ASP 191 OD1 ? ? ? 1_555 E CA . CA ? ? A ASP 191 A CA 371 1_555 ? ? ? ? ? ? ? 2.667 ? covale3 covale ? ? A SER 336 OG ? ? ? 1_555 D MAN . C1 ? ? A SER 336 A MAN 364 1_555 ? ? ? ? ? ? ? 1.389 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 2 ? B ? 2 ? C ? 2 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel B 1 2 ? anti-parallel C 1 2 ? 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 LEU A 126 ? ALA A 127 ? LEU A 126 ALA A 127 A 2 ILE A 287 ? ASP A 288 ? ILE A 287 ASP A 288 B 1 ARG A 177 ? ALA A 178 ? ARG A 177 ALA A 178 B 2 ALA A 188 ? PRO A 189 ? ALA A 188 PRO A 189 C 1 GLU A 221 ? VAL A 222 ? GLU A 221 VAL A 222 C 2 ARG A 238 ? LEU A 239 ? ARG A 238 LEU A 239 # 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 ALA A 127 ? N ALA A 127 O ILE A 287 ? O ILE A 287 B 1 2 N ALA A 178 ? N ALA A 178 O ALA A 188 ? O ALA A 188 C 1 2 N VAL A 222 ? N VAL A 222 O ARG A 238 ? O ARG A 238 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE NAG A 361' AC2 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE NAG A 362' AC3 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE MAN A 364' AC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA A 371' AC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CA A 372' AC6 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE MN A 381' AC7 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE GOL A 391' AC8 Software ? ? ? ? 25 'BINDING SITE FOR RESIDUE HEM A 396' # 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 8 ASN A 98 ? ASN A 98 . ? 1_555 ? 2 AC1 8 THR A 99 ? THR A 99 . ? 1_555 ? 3 AC1 8 ASN A 131 ? ASN A 131 . ? 1_555 ? 4 AC1 8 NAG C . ? NAG A 362 . ? 1_555 ? 5 AC1 8 HOH J . ? HOH A 1090 . ? 1_555 ? 6 AC1 8 HOH J . ? HOH A 1117 . ? 1_555 ? 7 AC1 8 HOH J . ? HOH A 1240 . ? 1_555 ? 8 AC1 8 HOH J . ? HOH A 1297 . ? 1_555 ? 9 AC2 9 MET A 94 ? MET A 94 . ? 1_555 ? 10 AC2 9 GLN A 95 ? GLN A 95 . ? 1_555 ? 11 AC2 9 ASN A 98 ? ASN A 98 . ? 1_555 ? 12 AC2 9 NAG B . ? NAG A 361 . ? 1_555 ? 13 AC2 9 HOH J . ? HOH A 1226 . ? 1_555 ? 14 AC2 9 HOH J . ? HOH A 1409 . ? 1_555 ? 15 AC2 9 HOH J . ? HOH A 1557 . ? 1_555 ? 16 AC2 9 HOH J . ? HOH A 1558 . ? 1_555 ? 17 AC2 9 HOH J . ? HOH A 1566 . ? 1_555 ? 18 AC3 7 HIS A 11 ? HIS A 11 . ? 1_554 ? 19 AC3 7 PRO A 331 ? PRO A 331 . ? 1_555 ? 20 AC3 7 GLY A 332 ? GLY A 332 . ? 1_555 ? 21 AC3 7 SER A 334 ? SER A 334 . ? 1_555 ? 22 AC3 7 GLN A 335 ? GLN A 335 . ? 1_555 ? 23 AC3 7 SER A 336 ? SER A 336 . ? 1_555 ? 24 AC3 7 HOH J . ? HOH A 1238 . ? 1_554 ? 25 AC4 5 SER A 174 ? SER A 174 . ? 1_555 ? 26 AC4 5 ASP A 191 ? ASP A 191 . ? 1_555 ? 27 AC4 5 THR A 193 ? THR A 193 . ? 1_555 ? 28 AC4 5 THR A 196 ? THR A 196 . ? 1_555 ? 29 AC4 5 ASP A 198 ? ASP A 198 . ? 1_555 ? 30 AC5 6 ASP A 47 ? ASP A 47 . ? 1_555 ? 31 AC5 6 GLY A 62 ? GLY A 62 . ? 1_555 ? 32 AC5 6 ASP A 64 ? ASP A 64 . ? 1_555 ? 33 AC5 6 SER A 66 ? SER A 66 . ? 1_555 ? 34 AC5 6 HOH J . ? HOH A 1085 . ? 1_555 ? 35 AC5 6 HOH J . ? HOH A 1127 . ? 1_555 ? 36 AC6 6 GLU A 35 ? GLU A 35 . ? 1_555 ? 37 AC6 6 GLU A 39 ? GLU A 39 . ? 1_555 ? 38 AC6 6 ASP A 179 ? ASP A 179 . ? 1_555 ? 39 AC6 6 HEM I . ? HEM A 396 . ? 1_555 ? 40 AC6 6 HOH J . ? HOH A 1040 . ? 1_555 ? 41 AC6 6 HOH J . ? HOH A 1108 . ? 1_555 ? 42 AC7 6 ASP A 23 ? ASP A 23 . ? 1_555 ? 43 AC7 6 THR A 27 ? THR A 27 . ? 1_555 ? 44 AC7 6 PRO A 92 ? PRO A 92 . ? 1_555 ? 45 AC7 6 LYS A 96 ? LYS A 96 . ? 1_555 ? 46 AC7 6 GLU A 156 ? GLU A 156 . ? 1_565 ? 47 AC7 6 HOH J . ? HOH A 1092 . ? 1_565 ? 48 AC8 25 GLU A 35 ? GLU A 35 . ? 1_555 ? 49 AC8 25 HIS A 38 ? HIS A 38 . ? 1_555 ? 50 AC8 25 GLU A 39 ? GLU A 39 . ? 1_555 ? 51 AC8 25 ARG A 42 ? ARG A 42 . ? 1_555 ? 52 AC8 25 PHE A 45 ? PHE A 45 . ? 1_555 ? 53 AC8 25 GLU A 143 ? GLU A 143 . ? 1_555 ? 54 AC8 25 PRO A 144 ? PRO A 144 . ? 1_555 ? 55 AC8 25 PHE A 155 ? PHE A 155 . ? 1_555 ? 56 AC8 25 LEU A 169 ? LEU A 169 . ? 1_555 ? 57 AC8 25 LEU A 170 ? LEU A 170 . ? 1_555 ? 58 AC8 25 SER A 172 ? SER A 172 . ? 1_555 ? 59 AC8 25 HIS A 173 ? HIS A 173 . ? 1_555 ? 60 AC8 25 ALA A 176 ? ALA A 176 . ? 1_555 ? 61 AC8 25 ARG A 177 ? ARG A 177 . ? 1_555 ? 62 AC8 25 ALA A 178 ? ALA A 178 . ? 1_555 ? 63 AC8 25 ASP A 179 ? ASP A 179 . ? 1_555 ? 64 AC8 25 LYS A 180 ? LYS A 180 . ? 1_555 ? 65 AC8 25 VAL A 181 ? VAL A 181 . ? 1_555 ? 66 AC8 25 SER A 241 ? SER A 241 . ? 1_555 ? 67 AC8 25 MN G . ? MN A 381 . ? 1_555 ? 68 AC8 25 HOH J . ? HOH A 1074 . ? 1_555 ? 69 AC8 25 HOH J . ? HOH A 1108 . ? 1_555 ? 70 AC8 25 HOH J . ? HOH A 1137 . ? 1_555 ? 71 AC8 25 HOH J . ? HOH A 1190 . ? 1_555 ? 72 AC8 25 HOH J . ? HOH A 1223 . ? 1_555 ? # _database_PDB_matrix.entry_id 3M5Q _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] 0.000000 _database_PDB_matrix.origx_vector[2] 0.000000 _database_PDB_matrix.origx_vector[3] 0.000000 # _atom_sites.entry_id 3M5Q _atom_sites.fract_transf_matrix[1][1] 0.006228 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000799 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.022075 _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] 0.019084 _atom_sites.fract_transf_vector[1] 0.000000 _atom_sites.fract_transf_vector[2] 0.000000 _atom_sites.fract_transf_vector[3] 0.000000 # loop_ _atom_type.symbol C CA FE MN 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 . ALA A 1 1 ? 37.689 38.060 64.638 1.00 25.70 ? 1 ALA A N 1 ATOM 2 C CA . ALA A 1 1 ? 38.374 39.368 64.709 1.00 22.76 ? 1 ALA A CA 1 ATOM 3 C C . ALA A 1 1 ? 37.978 40.231 63.509 1.00 21.90 ? 1 ALA A C 1 ATOM 4 O O . ALA A 1 1 ? 37.686 39.832 62.427 1.00 25.56 ? 1 ALA A O 1 ATOM 5 C CB . ALA A 1 1 ? 39.908 39.193 64.817 1.00 32.69 ? 1 ALA A CB 1 ATOM 6 N N . VAL A 1 2 ? 38.026 41.542 63.754 1.00 23.59 ? 2 VAL A N 1 ATOM 7 C CA . VAL A 1 2 ? 37.777 42.542 62.733 1.00 22.91 ? 2 VAL A CA 1 ATOM 8 C C . VAL A 1 2 ? 39.117 43.196 62.405 1.00 27.76 ? 2 VAL A C 1 ATOM 9 O O . VAL A 1 2 ? 39.727 43.772 63.315 1.00 39.87 ? 2 VAL A O 1 ATOM 10 C CB . VAL A 1 2 ? 36.763 43.601 63.201 1.00 25.95 ? 2 VAL A CB 1 ATOM 11 C CG1 . VAL A 1 2 ? 36.653 44.671 62.121 1.00 33.66 ? 2 VAL A CG1 1 ATOM 12 C CG2 . VAL A 1 2 ? 35.414 42.977 63.511 1.00 32.63 ? 2 VAL A CG2 1 ATOM 13 N N . CYS A 1 3 ? 39.602 43.174 61.185 1.00 24.10 ? 3 CYS A N 1 ATOM 14 C CA . CYS A 1 3 ? 40.860 43.755 60.762 1.00 27.33 ? 3 CYS A CA 1 ATOM 15 C C . CYS A 1 3 ? 40.784 45.261 60.720 1.00 36.41 ? 3 CYS A C 1 ATOM 16 O O . CYS A 1 3 ? 39.695 45.843 60.732 1.00 36.60 ? 3 CYS A O 1 ATOM 17 C CB A CYS A 1 3 ? 41.299 42.969 59.518 0.52 25.19 ? 3 CYS A CB 1 ATOM 18 C CB B CYS A 1 3 ? 41.091 43.544 59.253 0.52 31.03 ? 3 CYS A CB 1 ATOM 19 S SG A CYS A 1 3 ? 41.368 41.168 59.901 0.52 16.91 ? 3 CYS A SG 1 ATOM 20 S SG B CYS A 1 3 ? 41.415 41.904 58.649 0.52 36.44 ? 3 CYS A SG 1 ATOM 21 N N . PRO A 1 4 ? 41.881 45.977 60.661 1.00 41.12 ? 4 PRO A N 1 ATOM 22 C CA . PRO A 1 4 ? 41.761 47.449 60.716 1.00 43.90 ? 4 PRO A CA 1 ATOM 23 C C . PRO A 1 4 ? 41.022 47.958 59.483 1.00 47.40 ? 4 PRO A C 1 ATOM 24 O O . PRO A 1 4 ? 40.264 48.936 59.477 1.00 51.65 ? 4 PRO A O 1 ATOM 25 C CB . PRO A 1 4 ? 43.199 47.939 60.722 1.00 49.38 ? 4 PRO A CB 1 ATOM 26 C CG . PRO A 1 4 ? 43.926 46.759 61.296 1.00 45.43 ? 4 PRO A CG 1 ATOM 27 C CD . PRO A 1 4 ? 43.288 45.620 60.555 1.00 40.50 ? 4 PRO A CD 1 ATOM 28 N N . ASP A 1 5 ? 41.297 47.202 58.422 1.00 54.02 ? 5 ASP A N 1 ATOM 29 C CA . ASP A 1 5 ? 40.538 47.388 57.181 1.00 69.23 ? 5 ASP A CA 1 ATOM 30 C C . ASP A 1 5 ? 39.443 46.289 57.302 1.00 62.15 ? 5 ASP A C 1 ATOM 31 O O . ASP A 1 5 ? 39.745 45.150 56.793 1.00 40.95 ? 5 ASP A O 1 ATOM 32 C CB . ASP A 1 5 ? 41.417 47.327 55.958 1.00 86.40 ? 5 ASP A CB 1 ATOM 33 C CG . ASP A 1 5 ? 42.342 48.528 55.792 1.00 99.44 ? 5 ASP A CG 1 ATOM 34 O OD1 . ASP A 1 5 ? 43.584 48.379 55.900 1.00 112.18 ? 5 ASP A OD1 1 ATOM 35 O OD2 . ASP A 1 5 ? 41.830 49.652 55.552 1.00 119.08 ? 5 ASP A OD2 1 ATOM 36 N N . GLY A 1 6 ? 38.355 46.672 57.973 1.00 52.69 ? 6 GLY A N 1 ATOM 37 C CA . GLY A 1 6 ? 37.092 46.254 58.492 1.00 42.75 ? 6 GLY A CA 1 ATOM 38 C C . GLY A 1 6 ? 36.619 44.858 58.137 1.00 35.64 ? 6 GLY A C 1 ATOM 39 O O . GLY A 1 6 ? 35.465 44.446 58.319 1.00 34.53 ? 6 GLY A O 1 ATOM 40 N N . THR A 1 7 ? 37.507 44.040 57.585 1.00 28.89 ? 7 THR A N 1 ATOM 41 C CA . THR A 1 7 ? 37.196 42.664 57.321 1.00 23.90 ? 7 THR A CA 1 ATOM 42 C C . THR A 1 7 ? 37.057 41.817 58.579 1.00 22.31 ? 7 THR A C 1 ATOM 43 O O . THR A 1 7 ? 37.960 41.812 59.369 1.00 23.95 ? 7 THR A O 1 ATOM 44 C CB . THR A 1 7 ? 38.328 42.058 56.464 1.00 24.71 ? 7 THR A CB 1 ATOM 45 O OG1 . THR A 1 7 ? 38.599 42.928 55.350 1.00 32.23 ? 7 THR A OG1 1 ATOM 46 C CG2 . THR A 1 7 ? 37.862 40.727 55.877 1.00 24.24 ? 7 THR A CG2 1 ATOM 47 N N . ARG A 1 8 ? 35.933 41.103 58.762 1.00 24.93 ? 8 ARG A N 1 ATOM 48 C CA . ARG A 1 8 ? 35.825 40.055 59.789 1.00 19.55 ? 8 ARG A CA 1 ATOM 49 C C . ARG A 1 8 ? 36.506 38.786 59.302 1.00 19.77 ? 8 ARG A C 1 ATOM 50 O O . ARG A 1 8 ? 36.258 38.257 58.205 1.00 23.59 ? 8 ARG A O 1 ATOM 51 C CB . ARG A 1 8 ? 34.359 39.786 60.135 1.00 22.14 ? 8 ARG A CB 1 ATOM 52 C CG . ARG A 1 8 ? 34.015 39.198 61.477 1.00 33.65 ? 8 ARG A CG 1 ATOM 53 C CD . ARG A 1 8 ? 32.539 39.218 61.789 1.00 39.54 ? 8 ARG A CD 1 ATOM 54 N NE . ARG A 1 8 ? 31.735 38.312 60.972 1.00 42.64 ? 8 ARG A NE 1 ATOM 55 C CZ . ARG A 1 8 ? 31.373 37.072 61.234 1.00 41.07 ? 8 ARG A CZ 1 ATOM 56 N NH1 . ARG A 1 8 ? 31.744 36.486 62.380 1.00 38.67 ? 8 ARG A NH1 1 ATOM 57 N NH2 . ARG A 1 8 ? 30.634 36.461 60.298 1.00 42.39 ? 8 ARG A NH2 1 ATOM 58 N N . VAL A 1 9 ? 37.389 38.285 60.133 1.00 19.20 ? 9 VAL A N 1 ATOM 59 C CA . VAL A 1 9 ? 38.141 37.073 59.873 1.00 17.61 ? 9 VAL A CA 1 ATOM 60 C C . VAL A 1 9 ? 38.079 36.099 61.062 1.00 17.78 ? 9 VAL A C 1 ATOM 61 O O . VAL A 1 9 ? 37.641 36.474 62.176 1.00 17.80 ? 9 VAL A O 1 ATOM 62 C CB . VAL A 1 9 ? 39.613 37.386 59.555 1.00 19.27 ? 9 VAL A CB 1 ATOM 63 C CG1 . VAL A 1 9 ? 39.722 38.229 58.298 1.00 21.95 ? 9 VAL A CG1 1 ATOM 64 C CG2 . VAL A 1 9 ? 40.245 38.105 60.732 1.00 25.94 ? 9 VAL A CG2 1 ATOM 65 N N . SER A 1 10 ? 38.516 34.871 60.822 1.00 19.05 ? 10 SER A N 1 ATOM 66 C CA . SER A 1 10 ? 38.438 33.809 61.782 1.00 19.25 ? 10 SER A CA 1 ATOM 67 C C . SER A 1 10 ? 39.300 34.057 63.017 1.00 22.63 ? 10 SER A C 1 ATOM 68 O O . SER A 1 10 ? 38.914 33.722 64.156 1.00 26.45 ? 10 SER A O 1 ATOM 69 C CB . SER A 1 10 ? 38.838 32.506 61.084 1.00 23.49 ? 10 SER A CB 1 ATOM 70 O OG . SER A 1 10 ? 40.161 32.589 60.507 1.00 28.93 ? 10 SER A OG 1 ATOM 71 N N . HIS A 1 11 ? 40.469 34.591 62.826 1.00 16.85 ? 11 HIS A N 1 ATOM 72 C CA . HIS A 1 11 ? 41.485 34.740 63.858 1.00 17.87 ? 11 HIS A CA 1 ATOM 73 C C . HIS A 1 11 ? 42.233 36.032 63.599 1.00 16.24 ? 11 HIS A C 1 ATOM 74 O O . HIS A 1 11 ? 42.494 36.420 62.471 1.00 15.46 ? 11 HIS A O 1 ATOM 75 C CB . HIS A 1 11 ? 42.424 33.589 63.883 1.00 19.13 ? 11 HIS A CB 1 ATOM 76 C CG . HIS A 1 11 ? 41.884 32.192 63.873 1.00 20.38 ? 11 HIS A CG 1 ATOM 77 N ND1 . HIS A 1 11 ? 41.665 31.518 65.063 1.00 33.65 ? 11 HIS A ND1 1 ATOM 78 C CD2 . HIS A 1 11 ? 41.602 31.353 62.852 1.00 22.43 ? 11 HIS A CD2 1 ATOM 79 C CE1 . HIS A 1 11 ? 41.247 30.327 64.728 1.00 39.03 ? 11 HIS A CE1 1 ATOM 80 N NE2 . HIS A 1 11 ? 41.180 30.192 63.411 1.00 33.53 ? 11 HIS A NE2 1 ATOM 81 N N . ALA A 1 12 ? 42.600 36.668 64.685 1.00 19.69 ? 12 ALA A N 1 ATOM 82 C CA . ALA A 1 12 ? 43.411 37.888 64.550 1.00 18.54 ? 12 ALA A CA 1 ATOM 83 C C . ALA A 1 12 ? 44.683 37.609 63.757 1.00 16.99 ? 12 ALA A C 1 ATOM 84 O O . ALA A 1 12 ? 45.055 38.529 63.054 1.00 16.86 ? 12 ALA A O 1 ATOM 85 C CB . ALA A 1 12 ? 43.675 38.421 65.942 1.00 27.39 ? 12 ALA A CB 1 ATOM 86 N N . ALA A 1 13 ? 45.311 36.403 63.880 1.00 18.09 ? 13 ALA A N 1 ATOM 87 C CA . ALA A 1 13 ? 46.614 36.275 63.151 1.00 19.14 ? 13 ALA A CA 1 ATOM 88 C C . ALA A 1 13 ? 46.419 36.232 61.664 1.00 15.19 ? 13 ALA A C 1 ATOM 89 O O . ALA A 1 13 ? 47.314 36.344 60.855 1.00 19.60 ? 13 ALA A O 1 ATOM 90 C CB . ALA A 1 13 ? 47.279 35.087 63.769 1.00 38.66 ? 13 ALA A CB 1 ATOM 91 N N . CYS A 1 14 ? 45.139 36.056 61.209 1.00 12.85 ? 14 CYS A N 1 ATOM 92 C CA . CYS A 1 14 ? 44.875 36.053 59.786 1.00 12.48 ? 14 CYS A CA 1 ATOM 93 C C . CYS A 1 14 ? 44.886 37.455 59.175 1.00 11.01 ? 14 CYS A C 1 ATOM 94 O O . CYS A 1 14 ? 44.969 37.594 57.945 1.00 11.19 ? 14 CYS A O 1 ATOM 95 C CB A CYS A 1 14 ? 43.652 35.230 59.421 0.52 12.09 ? 14 CYS A CB 1 ATOM 96 C CB B CYS A 1 14 ? 43.409 35.714 59.557 0.52 20.78 ? 14 CYS A CB 1 ATOM 97 S SG A CYS A 1 14 ? 43.609 33.557 60.110 0.52 9.69 ? 14 CYS A SG 1 ATOM 98 S SG B CYS A 1 14 ? 42.545 34.230 59.972 0.52 27.23 ? 14 CYS A SG 1 ATOM 99 N N . CYS A 1 15 ? 44.708 38.490 60.025 1.00 11.16 ? 15 CYS A N 1 ATOM 100 C CA . CYS A 1 15 ? 44.509 39.818 59.473 1.00 11.92 ? 15 CYS A CA 1 ATOM 101 C C . CYS A 1 15 ? 45.614 40.308 58.538 1.00 10.27 ? 15 CYS A C 1 ATOM 102 O O . CYS A 1 15 ? 45.323 40.936 57.533 1.00 11.96 ? 15 CYS A O 1 ATOM 103 C CB . CYS A 1 15 ? 44.288 40.842 60.612 1.00 13.51 ? 15 CYS A CB 1 ATOM 104 S SG . CYS A 1 15 ? 42.742 40.670 61.494 1.00 18.95 ? 15 CYS A SG 1 ATOM 105 N N . ALA A 1 16 ? 46.889 40.043 58.888 1.00 10.51 ? 16 ALA A N 1 ATOM 106 C CA . ALA A 1 16 ? 47.987 40.576 58.092 1.00 10.59 ? 16 ALA A CA 1 ATOM 107 C C . ALA A 1 16 ? 48.033 40.015 56.681 1.00 9.18 ? 16 ALA A C 1 ATOM 108 O O . ALA A 1 16 ? 48.674 40.603 55.785 1.00 9.76 ? 16 ALA A O 1 ATOM 109 C CB . ALA A 1 16 ? 49.326 40.285 58.788 1.00 13.65 ? 16 ALA A CB 1 ATOM 110 N N . PHE A 1 17 ? 47.382 38.859 56.452 1.00 8.86 ? 17 PHE A N 1 ATOM 111 C CA . PHE A 1 17 ? 47.370 38.271 55.110 1.00 8.67 ? 17 PHE A CA 1 ATOM 112 C C . PHE A 1 17 ? 46.500 39.036 54.154 1.00 8.99 ? 17 PHE A C 1 ATOM 113 O O . PHE A 1 17 ? 46.698 38.934 52.922 1.00 9.92 ? 17 PHE A O 1 ATOM 114 C CB . PHE A 1 17 ? 46.947 36.800 55.187 1.00 8.61 ? 17 PHE A CB 1 ATOM 115 C CG . PHE A 1 17 ? 47.972 35.938 55.866 1.00 8.41 ? 17 PHE A CG 1 ATOM 116 C CD1 . PHE A 1 17 ? 47.902 35.672 57.230 1.00 9.50 ? 17 PHE A CD1 1 ATOM 117 C CD2 . PHE A 1 17 ? 49.050 35.424 55.138 1.00 8.31 ? 17 PHE A CD2 1 ATOM 118 C CE1 . PHE A 1 17 ? 48.890 34.901 57.842 1.00 10.03 ? 17 PHE A CE1 1 ATOM 119 C CE2 . PHE A 1 17 ? 50.049 34.673 55.740 1.00 8.11 ? 17 PHE A CE2 1 ATOM 120 C CZ . PHE A 1 17 ? 49.967 34.427 57.104 1.00 8.48 ? 17 PHE A CZ 1 ATOM 121 N N . ILE A 1 18 ? 45.545 39.836 54.635 1.00 9.86 ? 18 ILE A N 1 ATOM 122 C CA . ILE A 1 18 ? 44.678 40.602 53.749 1.00 10.61 ? 18 ILE A CA 1 ATOM 123 C C . ILE A 1 18 ? 45.440 41.646 52.941 1.00 10.34 ? 18 ILE A C 1 ATOM 124 O O . ILE A 1 18 ? 45.404 41.627 51.698 1.00 11.16 ? 18 ILE A O 1 ATOM 125 C CB . ILE A 1 18 ? 43.471 41.171 54.501 1.00 12.48 ? 18 ILE A CB 1 ATOM 126 C CG1 . ILE A 1 18 ? 42.625 40.030 55.101 1.00 15.89 ? 18 ILE A CG1 1 ATOM 127 C CG2 . ILE A 1 18 ? 42.659 42.067 53.564 1.00 16.32 ? 18 ILE A CG2 1 ATOM 128 C CD1 . ILE A 1 18 ? 41.382 40.453 55.818 1.00 27.15 ? 18 ILE A CD1 1 ATOM 129 N N . PRO A 1 19 ? 46.211 42.544 53.575 1.00 10.43 ? 19 PRO A N 1 ATOM 130 C CA . PRO A 1 19 ? 47.033 43.474 52.806 1.00 11.36 ? 19 PRO A CA 1 ATOM 131 C C . PRO A 1 19 ? 48.149 42.760 51.987 1.00 9.68 ? 19 PRO A C 1 ATOM 132 O O . PRO A 1 19 ? 48.531 43.270 50.938 1.00 10.10 ? 19 PRO A O 1 ATOM 133 C CB . PRO A 1 19 ? 47.596 44.444 53.810 1.00 13.57 ? 19 PRO A CB 1 ATOM 134 C CG . PRO A 1 19 ? 47.504 43.777 55.095 1.00 14.87 ? 19 PRO A CG 1 ATOM 135 C CD . PRO A 1 19 ? 46.259 42.896 54.999 1.00 11.57 ? 19 PRO A CD 1 ATOM 136 N N . LEU A 1 20 ? 48.641 41.642 52.495 1.00 9.09 ? 20 LEU A N 1 ATOM 137 C CA . LEU A 1 20 ? 49.635 40.887 51.692 1.00 8.41 ? 20 LEU A CA 1 ATOM 138 C C . LEU A 1 20 ? 49.018 40.417 50.363 1.00 8.21 ? 20 LEU A C 1 ATOM 139 O O . LEU A 1 20 ? 49.640 40.570 49.300 1.00 8.38 ? 20 LEU A O 1 ATOM 140 C CB . LEU A 1 20 ? 50.220 39.729 52.502 1.00 8.49 ? 20 LEU A CB 1 ATOM 141 C CG . LEU A 1 20 ? 51.132 38.768 51.680 1.00 8.01 ? 20 LEU A CG 1 ATOM 142 C CD1 . LEU A 1 20 ? 52.313 39.506 51.121 1.00 8.74 ? 20 LEU A CD1 1 ATOM 143 C CD2 . LEU A 1 20 ? 51.567 37.630 52.581 1.00 8.64 ? 20 LEU A CD2 1 ATOM 144 N N . ALA A 1 21 ? 47.818 39.809 50.409 1.00 8.33 ? 21 ALA A N 1 ATOM 145 C CA . ALA A 1 21 ? 47.181 39.385 49.167 1.00 8.22 ? 21 ALA A CA 1 ATOM 146 C C . ALA A 1 21 ? 47.007 40.555 48.218 1.00 8.34 ? 21 ALA A C 1 ATOM 147 O O . ALA A 1 21 ? 47.238 40.446 47.013 1.00 8.86 ? 21 ALA A O 1 ATOM 148 C CB . ALA A 1 21 ? 45.858 38.695 49.452 1.00 9.93 ? 21 ALA A CB 1 ATOM 149 N N . GLN A 1 22 ? 46.517 41.698 48.751 1.00 8.95 ? 22 GLN A N 1 ATOM 150 C CA . GLN A 1 22 ? 46.300 42.857 47.909 1.00 9.50 ? 22 GLN A CA 1 ATOM 151 C C . GLN A 1 22 ? 47.592 43.300 47.250 1.00 8.86 ? 22 GLN A C 1 ATOM 152 O O . GLN A 1 22 ? 47.631 43.666 46.076 1.00 9.74 ? 22 GLN A O 1 ATOM 153 C CB . GLN A 1 22 ? 45.652 43.981 48.720 1.00 11.66 ? 22 GLN A CB 1 ATOM 154 C CG . GLN A 1 22 ? 44.293 43.689 49.255 1.00 16.22 ? 22 GLN A CG 1 ATOM 155 C CD . GLN A 1 22 ? 43.660 44.679 50.182 1.00 23.56 ? 22 GLN A CD 1 ATOM 156 O OE1 . GLN A 1 22 ? 42.483 44.535 50.623 1.00 36.46 ? 22 GLN A OE1 1 ATOM 157 N NE2 . GLN A 1 22 ? 44.358 45.747 50.492 1.00 42.78 ? 22 GLN A NE2 1 ATOM 158 N N . ASP A 1 23 ? 48.683 43.329 48.019 1.00 8.72 ? 23 ASP A N 1 ATOM 159 C CA . ASP A 1 23 ? 49.972 43.774 47.522 1.00 8.66 ? 23 ASP A CA 1 ATOM 160 C C . ASP A 1 23 ? 50.499 42.817 46.455 1.00 7.83 ? 23 ASP A C 1 ATOM 161 O O . ASP A 1 23 ? 51.037 43.231 45.390 1.00 8.81 ? 23 ASP A O 1 ATOM 162 C CB . ASP A 1 23 ? 50.949 43.959 48.679 1.00 9.40 ? 23 ASP A CB 1 ATOM 163 C CG . ASP A 1 23 ? 52.119 44.829 48.396 1.00 10.42 ? 23 ASP A CG 1 ATOM 164 O OD1 . ASP A 1 23 ? 52.261 45.427 47.300 1.00 12.08 ? 23 ASP A OD1 1 ATOM 165 O OD2 . ASP A 1 23 ? 52.988 44.947 49.324 1.00 11.36 ? 23 ASP A OD2 1 ATOM 166 N N . LEU A 1 24 ? 50.386 41.516 46.703 1.00 7.71 ? 24 LEU A N 1 ATOM 167 C CA . LEU A 1 24 ? 50.826 40.526 45.693 1.00 7.57 ? 24 LEU A CA 1 ATOM 168 C C . LEU A 1 24 ? 50.058 40.709 44.390 1.00 7.92 ? 24 LEU A C 1 ATOM 169 O O . LEU A 1 24 ? 50.630 40.678 43.279 1.00 8.35 ? 24 LEU A O 1 ATOM 170 C CB . LEU A 1 24 ? 50.627 39.105 46.231 1.00 7.87 ? 24 LEU A CB 1 ATOM 171 C CG . LEU A 1 24 ? 51.579 38.669 47.335 1.00 7.88 ? 24 LEU A CG 1 ATOM 172 C CD1 . LEU A 1 24 ? 50.998 37.415 47.984 1.00 9.20 ? 24 LEU A CD1 1 ATOM 173 C CD2 . LEU A 1 24 ? 52.973 38.414 46.839 1.00 9.79 ? 24 LEU A CD2 1 ATOM 174 N N . GLN A 1 25 ? 48.738 40.871 44.488 1.00 8.32 ? 25 GLN A N 1 ATOM 175 C CA . GLN A 1 25 ? 47.925 41.019 43.293 1.00 9.39 ? 25 GLN A CA 1 ATOM 176 C C . GLN A 1 25 ? 48.279 42.297 42.554 1.00 9.82 ? 25 GLN A C 1 ATOM 177 O O . GLN A 1 25 ? 48.471 42.352 41.343 1.00 12.50 ? 25 GLN A O 1 ATOM 178 C CB . GLN A 1 25 ? 46.434 40.990 43.662 1.00 10.30 ? 25 GLN A CB 1 ATOM 179 C CG . GLN A 1 25 ? 45.899 39.641 44.167 1.00 10.67 ? 25 GLN A CG 1 ATOM 180 C CD . GLN A 1 25 ? 45.709 38.624 43.040 1.00 9.86 ? 25 GLN A CD 1 ATOM 181 O OE1 . GLN A 1 25 ? 46.477 38.585 42.017 1.00 10.83 ? 25 GLN A OE1 1 ATOM 182 N NE2 . GLN A 1 25 ? 44.688 37.811 43.194 1.00 10.09 ? 25 GLN A NE2 1 ATOM 183 N N . GLU A 1 26 ? 48.391 43.412 43.259 1.00 9.40 ? 26 GLU A N 1 ATOM 184 C CA . GLU A 1 26 ? 48.670 44.679 42.581 1.00 11.01 ? 26 GLU A CA 1 ATOM 185 C C . GLU A 1 26 ? 50.033 44.666 41.940 1.00 9.28 ? 26 GLU A C 1 ATOM 186 O O . GLU A 1 26 ? 50.279 45.220 40.863 1.00 11.12 ? 26 GLU A O 1 ATOM 187 C CB . GLU A 1 26 ? 48.574 45.860 43.601 1.00 15.48 ? 26 GLU A CB 1 ATOM 188 C CG . GLU A 1 26 ? 47.180 46.156 44.152 1.00 24.79 ? 26 GLU A CG 1 ATOM 189 C CD . GLU A 1 26 ? 46.977 47.085 45.321 1.00 29.02 ? 26 GLU A CD 1 ATOM 190 O OE1 . GLU A 1 26 ? 47.960 47.613 45.889 1.00 47.09 ? 26 GLU A OE1 1 ATOM 191 O OE2 . GLU A 1 26 ? 45.796 47.276 45.753 1.00 49.62 ? 26 GLU A OE2 1 ATOM 192 N N . THR A 1 27 ? 51.021 44.081 42.648 1.00 8.44 ? 27 THR A N 1 ATOM 193 C CA . THR A 1 27 ? 52.419 44.248 42.290 1.00 8.20 ? 27 THR A CA 1 ATOM 194 C C . THR A 1 27 ? 52.978 43.218 41.335 1.00 7.94 ? 27 THR A C 1 ATOM 195 O O . THR A 1 27 ? 53.682 43.581 40.372 1.00 9.36 ? 27 THR A O 1 ATOM 196 C CB . THR A 1 27 ? 53.265 44.262 43.573 1.00 8.63 ? 27 THR A CB 1 ATOM 197 O OG1 . THR A 1 27 ? 52.735 45.276 44.466 1.00 10.58 ? 27 THR A OG1 1 ATOM 198 C CG2 . THR A 1 27 ? 54.711 44.622 43.286 1.00 10.03 ? 27 THR A CG2 1 ATOM 199 N N . ILE A 1 28 ? 52.693 41.922 41.565 1.00 7.62 ? 28 ILE A N 1 ATOM 200 C CA . ILE A 1 28 ? 53.296 40.892 40.729 1.00 7.61 ? 28 ILE A CA 1 ATOM 201 C C . ILE A 1 28 ? 52.299 40.050 39.939 1.00 7.58 ? 28 ILE A C 1 ATOM 202 O O . ILE A 1 28 ? 52.731 39.501 38.901 1.00 8.59 ? 28 ILE A O 1 ATOM 203 C CB . ILE A 1 28 ? 54.343 40.009 41.451 1.00 8.15 ? 28 ILE A CB 1 ATOM 204 C CG1 . ILE A 1 28 ? 53.773 39.249 42.620 1.00 8.01 ? 28 ILE A CG1 1 ATOM 205 C CG2 . ILE A 1 28 ? 55.547 40.866 41.825 1.00 9.28 ? 28 ILE A CG2 1 ATOM 206 C CD1 . ILE A 1 28 ? 54.743 38.211 43.204 1.00 8.72 ? 28 ILE A CD1 1 ATOM 207 N N . PHE A 1 29 ? 51.028 39.853 40.364 1.00 7.46 ? 29 PHE A N 1 ATOM 208 C CA . PHE A 1 29 ? 50.164 38.950 39.604 1.00 7.87 ? 29 PHE A CA 1 ATOM 209 C C . PHE A 1 29 ? 49.136 39.662 38.695 1.00 8.29 ? 29 PHE A C 1 ATOM 210 O O . PHE A 1 29 ? 48.718 39.097 37.705 1.00 9.52 ? 29 PHE A O 1 ATOM 211 C CB . PHE A 1 29 ? 49.385 38.022 40.519 1.00 8.14 ? 29 PHE A CB 1 ATOM 212 C CG . PHE A 1 29 ? 50.265 37.180 41.461 1.00 7.81 ? 29 PHE A CG 1 ATOM 213 C CD1 . PHE A 1 29 ? 49.829 36.929 42.741 1.00 8.54 ? 29 PHE A CD1 1 ATOM 214 C CD2 . PHE A 1 29 ? 51.488 36.655 41.049 1.00 7.88 ? 29 PHE A CD2 1 ATOM 215 C CE1 . PHE A 1 29 ? 50.580 36.153 43.617 1.00 9.11 ? 29 PHE A CE1 1 ATOM 216 C CE2 . PHE A 1 29 ? 52.265 35.888 41.930 1.00 8.57 ? 29 PHE A CE2 1 ATOM 217 C CZ . PHE A 1 29 ? 51.805 35.638 43.209 1.00 8.55 ? 29 PHE A CZ 1 ATOM 218 N N . GLN A 1 30 ? 48.690 40.842 39.144 1.00 9.15 ? 30 GLN A N 1 ATOM 219 C CA . GLN A 1 30 ? 47.621 41.607 38.453 1.00 9.54 ? 30 GLN A CA 1 ATOM 220 C C . GLN A 1 30 ? 46.386 40.786 38.212 1.00 9.57 ? 30 GLN A C 1 ATOM 221 O O . GLN A 1 30 ? 45.716 40.921 37.205 1.00 10.54 ? 30 GLN A O 1 ATOM 222 C CB . GLN A 1 30 ? 48.154 42.262 37.168 1.00 10.96 ? 30 GLN A CB 1 ATOM 223 C CG . GLN A 1 30 ? 49.181 43.338 37.454 1.00 12.46 ? 30 GLN A CG 1 ATOM 224 C CD . GLN A 1 30 ? 50.593 42.845 37.606 1.00 10.16 ? 30 GLN A CD 1 ATOM 225 O OE1 . GLN A 1 30 ? 51.087 41.982 36.863 1.00 11.21 ? 30 GLN A OE1 1 ATOM 226 N NE2 . GLN A 1 30 ? 51.304 43.426 38.569 1.00 10.96 ? 30 GLN A NE2 1 ATOM 227 N N . ASN A 1 31 ? 46.009 39.929 39.184 1.00 9.50 ? 31 ASN A N 1 ATOM 228 C CA . ASN A 1 31 ? 44.831 39.090 39.103 1.00 10.08 ? 31 ASN A CA 1 ATOM 229 C C . ASN A 1 31 ? 44.909 38.117 37.909 1.00 9.81 ? 31 ASN A C 1 ATOM 230 O O . ASN A 1 31 ? 43.849 37.594 37.529 1.00 14.30 ? 31 ASN A O 1 ATOM 231 C CB . ASN A 1 31 ? 43.551 39.887 39.069 1.00 12.99 ? 31 ASN A CB 1 ATOM 232 C CG . ASN A 1 31 ? 43.469 40.857 40.206 1.00 18.84 ? 31 ASN A CG 1 ATOM 233 O OD1 . ASN A 1 31 ? 43.227 42.058 39.938 1.00 42.11 ? 31 ASN A OD1 1 ATOM 234 N ND2 . ASN A 1 31 ? 43.695 40.594 41.444 1.00 25.35 ? 31 ASN A ND2 1 ATOM 235 N N . GLU A 1 32 ? 46.081 37.847 37.375 1.00 9.75 ? 32 GLU A N 1 ATOM 236 C CA . GLU A 1 32 ? 46.278 36.969 36.215 1.00 10.01 ? 32 GLU A CA 1 ATOM 237 C C . GLU A 1 32 ? 46.969 35.679 36.603 1.00 8.47 ? 32 GLU A C 1 ATOM 238 O O . GLU A 1 32 ? 47.820 35.669 37.535 1.00 9.10 ? 32 GLU A O 1 ATOM 239 C CB . GLU A 1 32 ? 47.141 37.629 35.112 1.00 13.90 ? 32 GLU A CB 1 ATOM 240 C CG . GLU A 1 32 ? 46.580 38.842 34.497 1.00 16.61 ? 32 GLU A CG 1 ATOM 241 C CD . GLU A 1 32 ? 45.491 38.667 33.488 1.00 23.13 ? 32 GLU A CD 1 ATOM 242 O OE1 . GLU A 1 32 ? 44.966 39.756 33.013 1.00 39.92 ? 32 GLU A OE1 1 ATOM 243 O OE2 . GLU A 1 32 ? 45.013 37.552 33.089 1.00 26.68 ? 32 GLU A OE2 1 ATOM 244 N N . CYS A 1 33 ? 46.681 34.635 35.873 1.00 9.28 ? 33 CYS A N 1 ATOM 245 C CA . CYS A 1 33 ? 47.389 33.370 35.923 1.00 9.56 ? 33 CYS A CA 1 ATOM 246 C C . CYS A 1 33 ? 48.542 33.363 34.927 1.00 9.16 ? 33 CYS A C 1 ATOM 247 O O . CYS A 1 33 ? 48.580 32.495 34.035 1.00 12.29 ? 33 CYS A O 1 ATOM 248 C CB . CYS A 1 33 ? 46.389 32.228 35.560 1.00 11.45 ? 33 CYS A CB 1 ATOM 249 S SG . CYS A 1 33 ? 47.004 30.549 35.798 1.00 11.08 ? 33 CYS A SG 1 ATOM 250 N N . GLY A 1 34 ? 49.409 34.355 35.015 1.00 8.82 ? 34 GLY A N 1 ATOM 251 C CA . GLY A 1 34 ? 50.473 34.616 34.045 1.00 9.35 ? 34 GLY A CA 1 ATOM 252 C C . GLY A 1 34 ? 51.847 34.205 34.565 1.00 7.45 ? 34 GLY A C 1 ATOM 253 O O . GLY A 1 34 ? 51.965 33.428 35.514 1.00 7.98 ? 34 GLY A O 1 ATOM 254 N N . GLU A 1 35 ? 52.890 34.736 33.929 1.00 7.98 ? 35 GLU A N 1 ATOM 255 C CA . GLU A 1 35 ? 54.264 34.317 34.184 1.00 7.16 ? 35 GLU A CA 1 ATOM 256 C C . GLU A 1 35 ? 54.601 34.361 35.676 1.00 6.85 ? 35 GLU A C 1 ATOM 257 O O . GLU A 1 35 ? 55.113 33.399 36.240 1.00 7.46 ? 35 GLU A O 1 ATOM 258 C CB . GLU A 1 35 ? 55.254 35.146 33.375 1.00 8.76 ? 35 GLU A CB 1 ATOM 259 C CG . GLU A 1 35 ? 56.701 34.740 33.628 1.00 9.87 ? 35 GLU A CG 1 ATOM 260 C CD . GLU A 1 35 ? 57.026 33.357 33.184 1.00 9.74 ? 35 GLU A CD 1 ATOM 261 O OE1 . GLU A 1 35 ? 58.026 32.734 33.722 1.00 11.08 ? 35 GLU A OE1 1 ATOM 262 O OE2 . GLU A 1 35 ? 56.382 32.787 32.267 1.00 9.69 ? 35 GLU A OE2 1 ATOM 263 N N . ASP A 1 36 ? 54.343 35.526 36.308 1.00 6.97 ? 36 ASP A N 1 ATOM 264 C CA . ASP A 1 36 ? 54.817 35.659 37.698 1.00 6.84 ? 36 ASP A CA 1 ATOM 265 C C . ASP A 1 36 ? 54.019 34.714 38.628 1.00 6.83 ? 36 ASP A C 1 ATOM 266 O O . ASP A 1 36 ? 54.607 34.182 39.598 1.00 7.21 ? 36 ASP A O 1 ATOM 267 C CB . ASP A 1 36 ? 54.730 37.084 38.178 1.00 7.87 ? 36 ASP A CB 1 ATOM 268 C CG . ASP A 1 36 ? 55.804 37.958 37.663 1.00 7.93 ? 36 ASP A CG 1 ATOM 269 O OD1 . ASP A 1 36 ? 55.775 39.180 38.094 1.00 10.00 ? 36 ASP A OD1 1 ATOM 270 O OD2 . ASP A 1 36 ? 56.705 37.563 36.896 1.00 10.67 ? 36 ASP A OD2 1 ATOM 271 N N . ALA A 1 37 ? 52.736 34.547 38.379 1.00 6.79 ? 37 ALA A N 1 ATOM 272 C CA . ALA A 1 37 ? 51.922 33.591 39.155 1.00 6.82 ? 37 ALA A CA 1 ATOM 273 C C . ALA A 1 37 ? 52.465 32.173 38.998 1.00 6.31 ? 37 ALA A C 1 ATOM 274 O O . ALA A 1 37 ? 52.618 31.443 39.982 1.00 6.79 ? 37 ALA A O 1 ATOM 275 C CB . ALA A 1 37 ? 50.454 33.665 38.707 1.00 7.55 ? 37 ALA A CB 1 ATOM 276 N N . HIS A 1 38 ? 52.729 31.752 37.758 1.00 6.53 ? 38 HIS A N 1 ATOM 277 C CA . HIS A 1 38 ? 53.244 30.423 37.519 1.00 6.47 ? 38 HIS A CA 1 ATOM 278 C C . HIS A 1 38 ? 54.557 30.166 38.260 1.00 6.06 ? 38 HIS A C 1 ATOM 279 O O . HIS A 1 38 ? 54.753 29.104 38.861 1.00 6.82 ? 38 HIS A O 1 ATOM 280 C CB . HIS A 1 38 ? 53.479 30.185 36.025 1.00 7.42 ? 38 HIS A CB 1 ATOM 281 C CG . HIS A 1 38 ? 52.225 30.246 35.219 1.00 8.73 ? 38 HIS A CG 1 ATOM 282 N ND1 . HIS A 1 38 ? 52.324 30.419 33.848 1.00 10.01 ? 38 HIS A ND1 1 ATOM 283 C CD2 . HIS A 1 38 ? 50.911 30.117 35.519 1.00 10.64 ? 38 HIS A CD2 1 ATOM 284 C CE1 . HIS A 1 38 ? 51.047 30.361 33.396 1.00 11.83 ? 38 HIS A CE1 1 ATOM 285 N NE2 . HIS A 1 38 ? 50.209 30.208 34.383 1.00 13.07 ? 38 HIS A NE2 1 ATOM 286 N N . GLU A 1 39 ? 55.464 31.155 38.189 1.00 6.22 ? 39 GLU A N 1 ATOM 287 C CA . GLU A 1 39 ? 56.766 30.980 38.864 1.00 6.35 ? 39 GLU A CA 1 ATOM 288 C C . GLU A 1 39 ? 56.571 30.812 40.369 1.00 6.18 ? 39 GLU A C 1 ATOM 289 O O . GLU A 1 39 ? 57.271 30.002 41.008 1.00 6.81 ? 39 GLU A O 1 ATOM 290 C CB . GLU A 1 39 ? 57.648 32.161 38.522 1.00 7.95 ? 39 GLU A CB 1 ATOM 291 C CG . GLU A 1 39 ? 58.176 32.137 37.086 1.00 10.75 ? 39 GLU A CG 1 ATOM 292 C CD . GLU A 1 39 ? 59.181 30.981 36.763 1.00 14.27 ? 39 GLU A CD 1 ATOM 293 O OE1 . GLU A 1 39 ? 59.556 29.925 37.558 1.00 20.16 ? 39 GLU A OE1 1 ATOM 294 O OE2 . GLU A 1 39 ? 59.692 30.855 35.573 1.00 14.60 ? 39 GLU A OE2 1 ATOM 295 N N . VAL A 1 40 ? 55.656 31.567 40.981 1.00 5.98 ? 40 VAL A N 1 ATOM 296 C CA . VAL A 1 40 ? 55.382 31.423 42.419 1.00 6.11 ? 40 VAL A CA 1 ATOM 297 C C . VAL A 1 40 ? 54.756 30.063 42.753 1.00 6.20 ? 40 VAL A C 1 ATOM 298 O O . VAL A 1 40 ? 55.080 29.461 43.782 1.00 6.73 ? 40 VAL A O 1 ATOM 299 C CB . VAL A 1 40 ? 54.560 32.625 42.947 1.00 6.75 ? 40 VAL A CB 1 ATOM 300 C CG1 . VAL A 1 40 ? 54.001 32.327 44.316 1.00 8.84 ? 40 VAL A CG1 1 ATOM 301 C CG2 . VAL A 1 40 ? 55.434 33.877 42.969 1.00 7.53 ? 40 VAL A CG2 1 ATOM 302 N N . ILE A 1 41 ? 53.855 29.571 41.910 1.00 6.47 ? 41 ILE A N 1 ATOM 303 C CA . ILE A 1 41 ? 53.273 28.224 42.160 1.00 6.55 ? 41 ILE A CA 1 ATOM 304 C C . ILE A 1 41 ? 54.399 27.198 42.148 1.00 6.51 ? 41 ILE A C 1 ATOM 305 O O . ILE A 1 41 ? 54.453 26.314 43.027 1.00 7.00 ? 41 ILE A O 1 ATOM 306 C CB . ILE A 1 41 ? 52.165 27.929 41.143 1.00 6.64 ? 41 ILE A CB 1 ATOM 307 C CG1 . ILE A 1 41 ? 50.998 28.913 41.307 1.00 7.60 ? 41 ILE A CG1 1 ATOM 308 C CG2 . ILE A 1 41 ? 51.691 26.484 41.285 1.00 7.77 ? 41 ILE A CG2 1 ATOM 309 C CD1 . ILE A 1 41 ? 50.057 28.970 40.107 1.00 8.68 ? 41 ILE A CD1 1 ATOM 310 N N . ARG A 1 42 ? 55.325 27.277 41.188 1.00 6.48 ? 42 ARG A N 1 ATOM 311 C CA . ARG A 1 42 ? 56.460 26.365 41.112 1.00 6.35 ? 42 ARG A CA 1 ATOM 312 C C . ARG A 1 42 ? 57.293 26.455 42.401 1.00 6.49 ? 42 ARG A C 1 ATOM 313 O O . ARG A 1 42 ? 57.740 25.441 42.947 1.00 6.84 ? 42 ARG A O 1 ATOM 314 C CB A ARG A 1 42 ? 57.302 26.647 39.856 0.52 6.64 ? 42 ARG A CB 1 ATOM 315 C CB B ARG A 1 42 ? 57.302 26.695 39.893 0.52 8.10 ? 42 ARG A CB 1 ATOM 316 C CG A ARG A 1 42 ? 58.409 25.659 39.591 0.52 7.09 ? 42 ARG A CG 1 ATOM 317 C CG B ARG A 1 42 ? 58.583 25.878 39.782 0.52 10.11 ? 42 ARG A CG 1 ATOM 318 C CD A ARG A 1 42 ? 59.208 25.794 38.338 0.52 7.24 ? 42 ARG A CD 1 ATOM 319 C CD B ARG A 1 42 ? 59.312 26.435 38.598 0.52 12.55 ? 42 ARG A CD 1 ATOM 320 N NE A ARG A 1 42 ? 60.289 24.860 38.163 0.52 10.99 ? 42 ARG A NE 1 ATOM 321 N NE B ARG A 1 42 ? 60.600 25.938 38.322 0.52 17.02 ? 42 ARG A NE 1 ATOM 322 C CZ A ARG A 1 42 ? 61.581 25.061 37.829 0.52 16.27 ? 42 ARG A CZ 1 ATOM 323 C CZ B ARG A 1 42 ? 61.595 26.612 37.765 0.52 20.29 ? 42 ARG A CZ 1 ATOM 324 N NH1 A ARG A 1 42 ? 62.027 26.261 37.547 0.52 21.21 ? 42 ARG A NH1 1 ATOM 325 N NH1 B ARG A 1 42 ? 61.540 27.892 37.395 0.52 27.58 ? 42 ARG A NH1 1 ATOM 326 N NH2 A ARG A 1 42 ? 62.408 24.042 37.743 0.52 26.50 ? 42 ARG A NH2 1 ATOM 327 N NH2 B ARG A 1 42 ? 62.704 25.926 37.591 0.52 27.92 ? 42 ARG A NH2 1 ATOM 328 N N . LEU A 1 43 ? 57.518 27.688 42.888 1.00 6.91 ? 43 LEU A N 1 ATOM 329 C CA . LEU A 1 43 ? 58.279 27.875 44.129 1.00 7.04 ? 43 LEU A CA 1 ATOM 330 C C . LEU A 1 43 ? 57.600 27.202 45.326 1.00 6.75 ? 43 LEU A C 1 ATOM 331 O O . LEU A 1 43 ? 58.320 26.692 46.194 1.00 7.04 ? 43 LEU A O 1 ATOM 332 C CB . LEU A 1 43 ? 58.464 29.376 44.366 1.00 7.38 ? 43 LEU A CB 1 ATOM 333 C CG . LEU A 1 43 ? 59.226 29.730 45.660 1.00 7.02 ? 43 LEU A CG 1 ATOM 334 C CD1 . LEU A 1 43 ? 60.623 29.173 45.676 1.00 8.44 ? 43 LEU A CD1 1 ATOM 335 C CD2 . LEU A 1 43 ? 59.227 31.233 45.817 1.00 8.73 ? 43 LEU A CD2 1 ATOM 336 N N . THR A 1 44 ? 56.273 27.177 45.412 1.00 7.71 ? 44 THR A N 1 ATOM 337 C CA . THR A 1 44 ? 55.633 26.502 46.548 1.00 8.12 ? 44 THR A CA 1 ATOM 338 C C . THR A 1 44 ? 56.107 25.063 46.641 1.00 7.26 ? 44 THR A C 1 ATOM 339 O O . THR A 1 44 ? 56.332 24.547 47.758 1.00 7.80 ? 44 THR A O 1 ATOM 340 C CB . THR A 1 44 ? 54.054 26.530 46.543 1.00 11.82 ? 44 THR A CB 1 ATOM 341 O OG1 . THR A 1 44 ? 53.496 25.607 45.578 1.00 11.15 ? 44 THR A OG1 1 ATOM 342 C CG2 . THR A 1 44 ? 53.668 27.995 46.454 1.00 15.25 ? 44 THR A CG2 1 ATOM 343 N N . PHE A 1 45 ? 56.201 24.406 45.473 1.00 6.63 ? 45 PHE A N 1 ATOM 344 C CA . PHE A 1 45 ? 56.647 23.015 45.418 1.00 6.78 ? 45 PHE A CA 1 ATOM 345 C C . PHE A 1 45 ? 58.128 22.892 45.717 1.00 6.12 ? 45 PHE A C 1 ATOM 346 O O . PHE A 1 45 ? 58.516 22.046 46.517 1.00 7.14 ? 45 PHE A O 1 ATOM 347 C CB . PHE A 1 45 ? 56.287 22.465 43.992 1.00 7.19 ? 45 PHE A CB 1 ATOM 348 C CG . PHE A 1 45 ? 56.930 21.150 43.667 1.00 7.78 ? 45 PHE A CG 1 ATOM 349 C CD1 . PHE A 1 45 ? 57.661 21.019 42.521 1.00 10.40 ? 45 PHE A CD1 1 ATOM 350 C CD2 . PHE A 1 45 ? 56.788 20.048 44.494 1.00 10.02 ? 45 PHE A CD2 1 ATOM 351 C CE1 . PHE A 1 45 ? 58.255 19.819 42.190 1.00 13.92 ? 45 PHE A CE1 1 ATOM 352 C CE2 . PHE A 1 45 ? 57.397 18.830 44.176 1.00 12.84 ? 45 PHE A CE2 1 ATOM 353 C CZ . PHE A 1 45 ? 58.126 18.734 43.020 1.00 13.87 ? 45 PHE A CZ 1 ATOM 354 N N . HIS A 1 46 ? 58.987 23.715 45.079 1.00 5.82 ? 46 HIS A N 1 ATOM 355 C CA . HIS A 1 46 ? 60.420 23.560 45.328 1.00 5.88 ? 46 HIS A CA 1 ATOM 356 C C . HIS A 1 46 ? 60.745 23.890 46.794 1.00 5.90 ? 46 HIS A C 1 ATOM 357 O O . HIS A 1 46 ? 61.663 23.289 47.365 1.00 7.10 ? 46 HIS A O 1 ATOM 358 C CB . HIS A 1 46 ? 61.258 24.440 44.372 1.00 6.68 ? 46 HIS A CB 1 ATOM 359 C CG . HIS A 1 46 ? 61.282 23.909 42.968 1.00 6.90 ? 46 HIS A CG 1 ATOM 360 N ND1 . HIS A 1 46 ? 62.463 23.691 42.263 1.00 6.94 ? 46 HIS A ND1 1 ATOM 361 C CD2 . HIS A 1 46 ? 60.275 23.534 42.120 1.00 9.01 ? 46 HIS A CD2 1 ATOM 362 C CE1 . HIS A 1 46 ? 62.157 23.215 41.062 1.00 7.85 ? 46 HIS A CE1 1 ATOM 363 N NE2 . HIS A 1 46 ? 60.857 23.091 40.951 1.00 8.94 ? 46 HIS A NE2 1 ATOM 364 N N . ASP A 1 47 ? 60.044 24.860 47.383 1.00 5.75 ? 47 ASP A N 1 ATOM 365 C CA . ASP A 1 47 ? 60.284 25.121 48.819 1.00 5.42 ? 47 ASP A CA 1 ATOM 366 C C . ASP A 1 47 ? 59.866 23.889 49.624 1.00 5.85 ? 47 ASP A C 1 ATOM 367 O O . ASP A 1 47 ? 60.636 23.393 50.475 1.00 6.41 ? 47 ASP A O 1 ATOM 368 C CB . ASP A 1 47 ? 59.551 26.375 49.304 1.00 6.02 ? 47 ASP A CB 1 ATOM 369 C CG . ASP A 1 47 ? 59.968 26.814 50.698 1.00 6.42 ? 47 ASP A CG 1 ATOM 370 O OD1 . ASP A 1 47 ? 59.237 27.608 51.325 1.00 7.82 ? 47 ASP A OD1 1 ATOM 371 O OD2 . ASP A 1 47 ? 61.086 26.403 51.138 1.00 7.54 ? 47 ASP A OD2 1 ATOM 372 N N . ALA A 1 48 ? 58.652 23.384 49.423 1.00 5.87 ? 48 ALA A N 1 ATOM 373 C CA . ALA A 1 48 ? 58.081 22.361 50.306 1.00 5.97 ? 48 ALA A CA 1 ATOM 374 C C . ALA A 1 48 ? 58.765 21.009 50.181 1.00 6.01 ? 48 ALA A C 1 ATOM 375 O O . ALA A 1 48 ? 58.891 20.294 51.187 1.00 6.90 ? 48 ALA A O 1 ATOM 376 C CB . ALA A 1 48 ? 56.602 22.221 50.023 1.00 6.68 ? 48 ALA A CB 1 ATOM 377 N N . ILE A 1 49 ? 59.136 20.570 48.959 1.00 6.12 ? 49 ILE A N 1 ATOM 378 C CA . ILE A 1 49 ? 59.510 19.165 48.745 1.00 6.24 ? 49 ILE A CA 1 ATOM 379 C C . ILE A 1 49 ? 60.922 18.850 49.205 1.00 6.31 ? 49 ILE A C 1 ATOM 380 O O . ILE A 1 49 ? 61.309 17.679 49.274 1.00 6.91 ? 49 ILE A O 1 ATOM 381 C CB . ILE A 1 49 ? 59.313 18.774 47.257 1.00 6.50 ? 49 ILE A CB 1 ATOM 382 C CG1 . ILE A 1 49 ? 59.084 17.280 47.061 1.00 7.96 ? 49 ILE A CG1 1 ATOM 383 C CG2 . ILE A 1 49 ? 60.475 19.266 46.380 1.00 7.29 ? 49 ILE A CG2 1 ATOM 384 C CD1 . ILE A 1 49 ? 57.761 16.781 47.646 1.00 8.69 ? 49 ILE A CD1 1 ATOM 385 N N . ALA A 1 50 ? 61.710 19.892 49.546 1.00 6.28 ? 50 ALA A N 1 ATOM 386 C CA . ALA A 1 50 ? 63.108 19.722 49.961 1.00 6.32 ? 50 ALA A CA 1 ATOM 387 C C . ALA A 1 50 ? 63.124 19.335 51.472 1.00 6.42 ? 50 ALA A C 1 ATOM 388 O O . ALA A 1 50 ? 63.428 20.135 52.359 1.00 7.07 ? 50 ALA A O 1 ATOM 389 C CB . ALA A 1 50 ? 63.920 20.942 49.619 1.00 7.45 ? 50 ALA A CB 1 ATOM 390 N N . ILE A 1 51 ? 62.785 18.062 51.684 1.00 6.47 ? 51 ILE A N 1 ATOM 391 C CA . ILE A 1 51 ? 62.671 17.427 53.003 1.00 6.92 ? 51 ILE A CA 1 ATOM 392 C C . ILE A 1 51 ? 62.817 15.938 52.722 1.00 7.00 ? 51 ILE A C 1 ATOM 393 O O . ILE A 1 51 ? 62.385 15.463 51.657 1.00 7.08 ? 51 ILE A O 1 ATOM 394 C CB . ILE A 1 51 ? 61.349 17.784 53.708 1.00 6.83 ? 51 ILE A CB 1 ATOM 395 C CG1 . ILE A 1 51 ? 61.252 17.196 55.120 1.00 8.12 ? 51 ILE A CG1 1 ATOM 396 C CG2 . ILE A 1 51 ? 60.135 17.442 52.881 1.00 7.62 ? 51 ILE A CG2 1 ATOM 397 C CD1 . ILE A 1 51 ? 60.159 17.777 55.978 1.00 10.11 ? 51 ILE A CD1 1 ATOM 398 N N . SER A 1 52 ? 63.380 15.183 53.672 1.00 7.50 ? 52 SER A N 1 ATOM 399 C CA . SER A 1 52 ? 63.569 13.748 53.509 1.00 7.38 ? 52 SER A CA 1 ATOM 400 C C . SER A 1 52 ? 63.357 13.034 54.850 1.00 8.07 ? 52 SER A C 1 ATOM 401 O O . SER A 1 52 ? 64.107 13.276 55.820 1.00 9.27 ? 52 SER A O 1 ATOM 402 C CB . SER A 1 52 ? 64.973 13.476 53.031 1.00 8.50 ? 52 SER A CB 1 ATOM 403 O OG . SER A 1 52 ? 65.332 12.077 53.094 1.00 9.27 ? 52 SER A OG 1 ATOM 404 N N . ARG A 1 53 ? 62.408 12.102 54.875 1.00 8.47 ? 53 ARG A N 1 ATOM 405 C CA . ARG A 1 53 ? 62.195 11.274 56.056 1.00 9.87 ? 53 ARG A CA 1 ATOM 406 C C . ARG A 1 53 ? 63.466 10.430 56.331 1.00 10.68 ? 53 ARG A C 1 ATOM 407 O O . ARG A 1 53 ? 63.868 10.284 57.490 1.00 13.33 ? 53 ARG A O 1 ATOM 408 C CB . ARG A 1 53 ? 61.002 10.327 55.840 1.00 11.93 ? 53 ARG A CB 1 ATOM 409 C CG . ARG A 1 53 ? 59.647 11.053 55.879 1.00 13.46 ? 53 ARG A CG 1 ATOM 410 C CD . ARG A 1 53 ? 58.595 10.186 55.297 1.00 20.36 ? 53 ARG A CD 1 ATOM 411 N NE . ARG A 1 53 ? 57.251 10.524 55.655 1.00 26.67 ? 53 ARG A NE 1 ATOM 412 C CZ . ARG A 1 53 ? 56.185 9.710 55.446 1.00 36.31 ? 53 ARG A CZ 1 ATOM 413 N NH1 . ARG A 1 53 ? 56.420 8.560 54.786 1.00 40.47 ? 53 ARG A NH1 1 ATOM 414 N NH2 . ARG A 1 53 ? 55.007 10.118 55.834 1.00 55.31 ? 53 ARG A NH2 1 ATOM 415 N N . SER A 1 54 ? 64.059 9.850 55.296 1.00 10.45 ? 54 SER A N 1 ATOM 416 C CA . SER A 1 54 ? 65.197 8.947 55.496 1.00 11.80 ? 54 SER A CA 1 ATOM 417 C C . SER A 1 54 ? 66.447 9.670 55.907 1.00 11.42 ? 54 SER A C 1 ATOM 418 O O . SER A 1 54 ? 67.225 9.159 56.708 1.00 13.83 ? 54 SER A O 1 ATOM 419 C CB . SER A 1 54 ? 65.399 8.052 54.265 1.00 13.49 ? 54 SER A CB 1 ATOM 420 O OG . SER A 1 54 ? 65.779 8.838 53.160 1.00 14.44 ? 54 SER A OG 1 ATOM 421 N N . GLN A 1 55 ? 66.727 10.836 55.332 1.00 11.13 ? 55 GLN A N 1 ATOM 422 C CA . GLN A 1 55 ? 67.925 11.569 55.642 1.00 11.09 ? 55 GLN A CA 1 ATOM 423 C C . GLN A 1 55 ? 67.816 12.310 56.965 1.00 11.46 ? 55 GLN A C 1 ATOM 424 O O . GLN A 1 55 ? 68.864 12.634 57.603 1.00 15.14 ? 55 GLN A O 1 ATOM 425 C CB . GLN A 1 55 ? 68.331 12.526 54.522 1.00 11.58 ? 55 GLN A CB 1 ATOM 426 C CG . GLN A 1 55 ? 68.694 11.844 53.198 1.00 12.83 ? 55 GLN A CG 1 ATOM 427 C CD . GLN A 1 55 ? 69.280 12.803 52.192 1.00 17.74 ? 55 GLN A CD 1 ATOM 428 O OE1 . GLN A 1 55 ? 70.319 13.481 52.393 1.00 24.69 ? 55 GLN A OE1 1 ATOM 429 N NE2 . GLN A 1 55 ? 68.624 12.919 51.043 1.00 24.31 ? 55 GLN A NE2 1 ATOM 430 N N . GLY A 1 56 ? 66.633 12.639 57.423 1.00 11.09 ? 56 GLY A N 1 ATOM 431 C CA . GLY A 1 56 ? 66.423 13.367 58.657 1.00 11.45 ? 56 GLY A CA 1 ATOM 432 C C . GLY A 1 56 ? 66.424 14.882 58.465 1.00 9.43 ? 56 GLY A C 1 ATOM 433 O O . GLY A 1 56 ? 66.636 15.387 57.345 1.00 9.21 ? 56 GLY A O 1 ATOM 434 N N . PRO A 1 57 ? 66.175 15.605 59.561 1.00 10.94 ? 57 PRO A N 1 ATOM 435 C CA . PRO A 1 57 ? 65.939 17.039 59.475 1.00 11.72 ? 57 PRO A CA 1 ATOM 436 C C . PRO A 1 57 ? 67.102 17.836 58.885 1.00 11.24 ? 57 PRO A C 1 ATOM 437 O O . PRO A 1 57 ? 66.875 18.899 58.290 1.00 11.48 ? 57 PRO A O 1 ATOM 438 C CB . PRO A 1 57 ? 65.563 17.458 60.917 1.00 17.31 ? 57 PRO A CB 1 ATOM 439 C CG . PRO A 1 57 ? 65.311 16.224 61.619 1.00 21.08 ? 57 PRO A CG 1 ATOM 440 C CD . PRO A 1 57 ? 65.892 15.068 60.915 1.00 13.87 ? 57 PRO A CD 1 ATOM 441 N N . LYS A 1 58 ? 68.352 17.377 58.983 1.00 11.70 ? 58 LYS A N 1 ATOM 442 C CA . LYS A 1 58 ? 69.463 18.159 58.424 1.00 12.92 ? 58 LYS A CA 1 ATOM 443 C C . LYS A 1 58 ? 69.442 18.250 56.916 1.00 11.52 ? 58 LYS A C 1 ATOM 444 O O . LYS A 1 58 ? 70.095 19.132 56.347 1.00 13.62 ? 58 LYS A O 1 ATOM 445 C CB . LYS A 1 58 ? 70.768 17.517 58.946 1.00 20.40 ? 58 LYS A CB 1 ATOM 446 C CG . LYS A 1 58 ? 70.882 17.721 60.471 1.00 29.54 ? 58 LYS A CG 1 ATOM 447 C CD . LYS A 1 58 ? 72.206 17.218 61.042 1.00 31.73 ? 58 LYS A CD 1 ATOM 448 C CE . LYS A 1 58 ? 72.436 17.604 62.509 1.00 38.92 ? 58 LYS A CE 1 ATOM 449 N NZ . LYS A 1 58 ? 73.472 16.878 63.186 1.00 44.57 ? 58 LYS A NZ 1 ATOM 450 N N . ALA A 1 59 ? 68.695 17.391 56.230 1.00 9.26 ? 59 ALA A N 1 ATOM 451 C CA . ALA A 1 59 ? 68.606 17.497 54.777 1.00 9.06 ? 59 ALA A CA 1 ATOM 452 C C . ALA A 1 59 ? 67.700 18.666 54.346 1.00 7.83 ? 59 ALA A C 1 ATOM 453 O O . ALA A 1 59 ? 67.793 19.055 53.166 1.00 8.49 ? 59 ALA A O 1 ATOM 454 C CB . ALA A 1 59 ? 68.077 16.199 54.180 1.00 10.39 ? 59 ALA A CB 1 ATOM 455 N N . GLY A 1 60 ? 66.824 19.140 55.227 1.00 7.80 ? 60 GLY A N 1 ATOM 456 C CA . GLY A 1 60 ? 65.903 20.213 54.876 1.00 7.83 ? 60 GLY A CA 1 ATOM 457 C C . GLY A 1 60 ? 64.657 20.208 55.680 1.00 6.99 ? 60 GLY A C 1 ATOM 458 O O . GLY A 1 60 ? 64.187 19.159 56.160 1.00 8.23 ? 60 GLY A O 1 ATOM 459 N N . GLY A 1 61 ? 64.062 21.378 55.818 1.00 6.94 ? 61 GLY A N 1 ATOM 460 C CA . GLY A 1 61 ? 62.896 21.575 56.656 1.00 7.18 ? 61 GLY A CA 1 ATOM 461 C C . GLY A 1 61 ? 61.566 21.688 55.949 1.00 6.82 ? 61 GLY A C 1 ATOM 462 O O . GLY A 1 61 ? 60.571 22.064 56.582 1.00 8.03 ? 61 GLY A O 1 ATOM 463 N N . GLY A 1 62 ? 61.493 21.341 54.662 1.00 6.47 ? 62 GLY A N 1 ATOM 464 C CA . GLY A 1 62 ? 60.206 21.346 53.980 1.00 6.65 ? 62 GLY A CA 1 ATOM 465 C C . GLY A 1 62 ? 59.707 22.735 53.682 1.00 5.99 ? 62 GLY A C 1 ATOM 466 O O . GLY A 1 62 ? 60.471 23.577 53.176 1.00 6.25 ? 62 GLY A O 1 ATOM 467 N N . ALA A 1 63 ? 58.412 22.993 53.916 1.00 6.11 ? 63 ALA A N 1 ATOM 468 C CA . ALA A 1 63 ? 57.755 24.265 53.612 1.00 6.44 ? 63 ALA A CA 1 ATOM 469 C C . ALA A 1 63 ? 58.137 25.277 54.680 1.00 6.17 ? 63 ALA A C 1 ATOM 470 O O . ALA A 1 63 ? 57.400 25.523 55.641 1.00 7.05 ? 63 ALA A O 1 ATOM 471 C CB . ALA A 1 63 ? 56.240 24.059 53.545 1.00 6.75 ? 63 ALA A CB 1 ATOM 472 N N . ASP A 1 64 ? 59.342 25.819 54.522 1.00 6.25 ? 64 ASP A N 1 ATOM 473 C CA . ASP A 1 64 ? 60.032 26.522 55.594 1.00 6.40 ? 64 ASP A CA 1 ATOM 474 C C . ASP A 1 64 ? 60.627 27.854 55.118 1.00 6.34 ? 64 ASP A C 1 ATOM 475 O O . ASP A 1 64 ? 61.334 28.508 55.903 1.00 7.16 ? 64 ASP A O 1 ATOM 476 C CB . ASP A 1 64 ? 61.140 25.658 56.186 1.00 6.83 ? 64 ASP A CB 1 ATOM 477 C CG . ASP A 1 64 ? 62.252 25.303 55.219 1.00 6.51 ? 64 ASP A CG 1 ATOM 478 O OD1 . ASP A 1 64 ? 62.172 25.642 54.008 1.00 6.17 ? 64 ASP A OD1 1 ATOM 479 O OD2 . ASP A 1 64 ? 63.242 24.652 55.693 1.00 7.26 ? 64 ASP A OD2 1 ATOM 480 N N . GLY A 1 65 ? 60.360 28.275 53.869 1.00 6.23 ? 65 GLY A N 1 ATOM 481 C CA . GLY A 1 65 ? 60.918 29.510 53.388 1.00 6.62 ? 65 GLY A CA 1 ATOM 482 C C . GLY A 1 65 ? 62.413 29.477 53.145 1.00 6.22 ? 65 GLY A C 1 ATOM 483 O O . GLY A 1 65 ? 63.026 30.547 52.941 1.00 6.72 ? 65 GLY A O 1 ATOM 484 N N . SER A 1 66 ? 63.029 28.295 53.089 1.00 6.27 ? 66 SER A N 1 ATOM 485 C CA . SER A 1 66 ? 64.487 28.179 52.926 1.00 6.12 ? 66 SER A CA 1 ATOM 486 C C . SER A 1 66 ? 64.969 28.846 51.651 1.00 6.02 ? 66 SER A C 1 ATOM 487 O O . SER A 1 66 ? 66.081 29.389 51.607 1.00 6.89 ? 66 SER A O 1 ATOM 488 C CB . SER A 1 66 ? 64.928 26.716 52.976 1.00 6.14 ? 66 SER A CB 1 ATOM 489 O OG . SER A 1 66 ? 64.352 25.946 51.929 1.00 6.21 ? 66 SER A OG 1 ATOM 490 N N . MET A 1 67 ? 64.147 28.805 50.600 1.00 6.66 ? 67 MET A N 1 ATOM 491 C CA . MET A 1 67 ? 64.504 29.427 49.313 1.00 7.59 ? 67 MET A CA 1 ATOM 492 C C . MET A 1 67 ? 64.695 30.939 49.440 1.00 7.09 ? 67 MET A C 1 ATOM 493 O O . MET A 1 67 ? 65.509 31.528 48.714 1.00 8.37 ? 67 MET A O 1 ATOM 494 C CB . MET A 1 67 ? 63.376 29.105 48.305 1.00 9.43 ? 67 MET A CB 1 ATOM 495 C CG . MET A 1 67 ? 63.333 27.638 47.891 1.00 9.92 ? 67 MET A CG 1 ATOM 496 S SD . MET A 1 67 ? 64.592 27.344 46.601 1.00 12.91 ? 67 MET A SD 1 ATOM 497 C CE . MET A 1 67 ? 64.335 25.616 46.309 1.00 9.87 ? 67 MET A CE 1 ATOM 498 N N . LEU A 1 68 ? 63.864 31.587 50.296 1.00 6.68 ? 68 LEU A N 1 ATOM 499 C CA . LEU A 1 68 ? 63.946 33.009 50.528 1.00 6.60 ? 68 LEU A CA 1 ATOM 500 C C . LEU A 1 68 ? 65.007 33.386 51.533 1.00 6.91 ? 68 LEU A C 1 ATOM 501 O O . LEU A 1 68 ? 65.635 34.442 51.432 1.00 8.22 ? 68 LEU A O 1 ATOM 502 C CB . LEU A 1 68 ? 62.593 33.611 51.001 1.00 6.75 ? 68 LEU A CB 1 ATOM 503 C CG . LEU A 1 68 ? 61.361 33.398 50.122 1.00 9.78 ? 68 LEU A CG 1 ATOM 504 C CD1 . LEU A 1 68 ? 60.247 34.319 50.618 1.00 9.73 ? 68 LEU A CD1 1 ATOM 505 C CD2 . LEU A 1 68 ? 61.551 33.461 48.682 1.00 12.07 ? 68 LEU A CD2 1 ATOM 506 N N . LEU A 1 69 ? 65.151 32.561 52.589 1.00 6.67 ? 69 LEU A N 1 ATOM 507 C CA . LEU A 1 69 ? 66.046 32.863 53.699 1.00 6.87 ? 69 LEU A CA 1 ATOM 508 C C . LEU A 1 69 ? 67.516 32.545 53.370 1.00 6.93 ? 69 LEU A C 1 ATOM 509 O O . LEU A 1 69 ? 68.405 33.154 53.976 1.00 7.67 ? 69 LEU A O 1 ATOM 510 C CB . LEU A 1 69 ? 65.576 32.118 54.944 1.00 7.21 ? 69 LEU A CB 1 ATOM 511 C CG . LEU A 1 69 ? 64.219 32.550 55.516 1.00 8.03 ? 69 LEU A CG 1 ATOM 512 C CD1 . LEU A 1 69 ? 63.700 31.615 56.590 1.00 9.89 ? 69 LEU A CD1 1 ATOM 513 C CD2 . LEU A 1 69 ? 64.250 33.983 56.033 1.00 9.98 ? 69 LEU A CD2 1 ATOM 514 N N . PHE A 1 70 ? 67.745 31.636 52.437 1.00 6.61 ? 70 PHE A N 1 ATOM 515 C CA . PHE A 1 70 ? 69.078 31.262 51.967 1.00 6.75 ? 70 PHE A CA 1 ATOM 516 C C . PHE A 1 70 ? 69.091 31.343 50.430 1.00 6.67 ? 70 PHE A C 1 ATOM 517 O O . PHE A 1 70 ? 69.216 30.348 49.719 1.00 7.34 ? 70 PHE A O 1 ATOM 518 C CB . PHE A 1 70 ? 69.485 29.845 52.419 1.00 7.37 ? 70 PHE A CB 1 ATOM 519 C CG . PHE A 1 70 ? 69.499 29.703 53.942 1.00 7.04 ? 70 PHE A CG 1 ATOM 520 C CD1 . PHE A 1 70 ? 70.652 29.965 54.656 1.00 7.61 ? 70 PHE A CD1 1 ATOM 521 C CD2 . PHE A 1 70 ? 68.355 29.312 54.620 1.00 7.94 ? 70 PHE A CD2 1 ATOM 522 C CE1 . PHE A 1 70 ? 70.660 29.775 56.036 1.00 8.61 ? 70 PHE A CE1 1 ATOM 523 C CE2 . PHE A 1 70 ? 68.355 29.163 56.014 1.00 8.57 ? 70 PHE A CE2 1 ATOM 524 C CZ . PHE A 1 70 ? 69.523 29.415 56.693 1.00 9.21 ? 70 PHE A CZ 1 ATOM 525 N N . PRO A 1 71 ? 68.943 32.566 49.897 1.00 7.10 ? 71 PRO A N 1 ATOM 526 C CA . PRO A 1 71 ? 68.718 32.709 48.437 1.00 7.38 ? 71 PRO A CA 1 ATOM 527 C C . PRO A 1 71 ? 69.898 32.362 47.563 1.00 7.43 ? 71 PRO A C 1 ATOM 528 O O . PRO A 1 71 ? 69.737 32.178 46.348 1.00 8.04 ? 71 PRO A O 1 ATOM 529 C CB . PRO A 1 71 ? 68.298 34.160 48.293 1.00 9.35 ? 71 PRO A CB 1 ATOM 530 C CG . PRO A 1 71 ? 69.005 34.861 49.430 1.00 8.58 ? 71 PRO A CG 1 ATOM 531 C CD . PRO A 1 71 ? 68.884 33.869 50.568 1.00 7.63 ? 71 PRO A CD 1 ATOM 532 N N . THR A 1 72 ? 71.121 32.264 48.136 1.00 7.23 ? 72 THR A N 1 ATOM 533 C CA . THR A 1 72 ? 72.298 31.907 47.359 1.00 7.78 ? 72 THR A CA 1 ATOM 534 C C . THR A 1 72 ? 72.597 30.395 47.349 1.00 7.47 ? 72 THR A C 1 ATOM 535 O O . THR A 1 72 ? 73.541 29.982 46.671 1.00 8.31 ? 72 THR A O 1 ATOM 536 C CB . THR A 1 72 ? 73.558 32.661 47.816 1.00 8.52 ? 72 THR A CB 1 ATOM 537 O OG1 . THR A 1 72 ? 73.903 32.160 49.096 1.00 8.74 ? 72 THR A OG1 1 ATOM 538 C CG2 . THR A 1 72 ? 73.318 34.162 47.861 1.00 10.54 ? 72 THR A CG2 1 ATOM 539 N N . VAL A 1 73 ? 71.813 29.591 48.098 1.00 7.12 ? 73 VAL A N 1 ATOM 540 C CA . VAL A 1 73 ? 72.103 28.169 48.245 1.00 7.03 ? 73 VAL A CA 1 ATOM 541 C C . VAL A 1 73 ? 71.263 27.396 47.236 1.00 6.59 ? 73 VAL A C 1 ATOM 542 O O . VAL A 1 73 ? 71.678 27.117 46.088 1.00 7.34 ? 73 VAL A O 1 ATOM 543 C CB . VAL A 1 73 ? 71.981 27.704 49.693 1.00 7.52 ? 73 VAL A CB 1 ATOM 544 C CG1 . VAL A 1 73 ? 72.315 26.215 49.798 1.00 8.75 ? 73 VAL A CG1 1 ATOM 545 C CG2 . VAL A 1 73 ? 72.928 28.512 50.564 1.00 9.13 ? 73 VAL A CG2 1 ATOM 546 N N . GLU A 1 74 ? 70.026 26.993 47.640 1.00 6.79 ? 74 GLU A N 1 ATOM 547 C CA . GLU A 1 74 ? 69.234 26.104 46.806 1.00 6.63 ? 74 GLU A CA 1 ATOM 548 C C . GLU A 1 74 ? 68.929 26.669 45.423 1.00 6.48 ? 74 GLU A C 1 ATOM 549 O O . GLU A 1 74 ? 68.929 25.904 44.451 1.00 6.98 ? 74 GLU A O 1 ATOM 550 C CB . GLU A 1 74 ? 67.947 25.680 47.511 1.00 6.90 ? 74 GLU A CB 1 ATOM 551 C CG . GLU A 1 74 ? 68.108 24.887 48.790 1.00 7.08 ? 74 GLU A CG 1 ATOM 552 C CD . GLU A 1 74 ? 66.778 24.814 49.533 1.00 7.11 ? 74 GLU A CD 1 ATOM 553 O OE1 . GLU A 1 74 ? 66.636 25.499 50.610 1.00 7.78 ? 74 GLU A OE1 1 ATOM 554 O OE2 . GLU A 1 74 ? 65.860 24.126 49.028 1.00 7.53 ? 74 GLU A OE2 1 ATOM 555 N N . PRO A 1 75 ? 68.645 27.964 45.269 1.00 7.11 ? 75 PRO A N 1 ATOM 556 C CA . PRO A 1 75 ? 68.340 28.459 43.892 1.00 7.31 ? 75 PRO A CA 1 ATOM 557 C C . PRO A 1 75 ? 69.434 28.231 42.898 1.00 8.10 ? 75 PRO A C 1 ATOM 558 O O . PRO A 1 75 ? 69.165 28.260 41.672 1.00 9.99 ? 75 PRO A O 1 ATOM 559 C CB . PRO A 1 75 ? 68.020 29.935 44.155 1.00 8.46 ? 75 PRO A CB 1 ATOM 560 C CG . PRO A 1 75 ? 67.436 29.972 45.540 1.00 8.16 ? 75 PRO A CG 1 ATOM 561 C CD . PRO A 1 75 ? 68.369 29.020 46.283 1.00 7.47 ? 75 PRO A CD 1 ATOM 562 N N . ASN A 1 76 ? 70.677 28.031 43.336 1.00 7.78 ? 76 ASN A N 1 ATOM 563 C CA . ASN A 1 76 ? 71.801 27.770 42.416 1.00 8.74 ? 76 ASN A CA 1 ATOM 564 C C . ASN A 1 76 ? 72.061 26.311 42.167 1.00 8.56 ? 76 ASN A C 1 ATOM 565 O O . ASN A 1 76 ? 72.966 25.991 41.367 1.00 11.20 ? 76 ASN A O 1 ATOM 566 C CB A ASN A 1 76 ? 73.082 28.490 42.855 0.52 9.00 ? 76 ASN A CB 1 ATOM 567 C CB B ASN A 1 76 ? 73.005 28.526 42.998 0.52 10.63 ? 76 ASN A CB 1 ATOM 568 C CG A ASN A 1 76 ? 72.847 29.980 42.780 0.52 8.66 ? 76 ASN A CG 1 ATOM 569 C CG B ASN A 1 76 ? 73.967 28.974 41.915 0.52 19.53 ? 76 ASN A CG 1 ATOM 570 O OD1 A ASN A 1 76 ? 73.028 30.710 43.806 0.52 12.10 ? 76 ASN A OD1 1 ATOM 571 O OD1 B ASN A 1 76 ? 73.532 29.317 40.828 0.52 29.55 ? 76 ASN A OD1 1 ATOM 572 N ND2 A ASN A 1 76 ? 72.442 30.479 41.670 0.52 9.05 ? 76 ASN A ND2 1 ATOM 573 N ND2 B ASN A 1 76 ? 75.263 28.959 42.234 0.52 37.74 ? 76 ASN A ND2 1 ATOM 574 N N . PHE A 1 77 ? 71.301 25.368 42.750 1.00 7.68 ? 77 PHE A N 1 ATOM 575 C CA . PHE A 1 77 ? 71.399 23.977 42.390 1.00 7.77 ? 77 PHE A CA 1 ATOM 576 C C . PHE A 1 77 ? 70.874 23.787 40.960 1.00 7.70 ? 77 PHE A C 1 ATOM 577 O O . PHE A 1 77 ? 69.907 24.467 40.558 1.00 8.12 ? 77 PHE A O 1 ATOM 578 C CB . PHE A 1 77 ? 70.593 23.075 43.307 1.00 7.57 ? 77 PHE A CB 1 ATOM 579 C CG . PHE A 1 77 ? 70.974 23.070 44.787 1.00 7.87 ? 77 PHE A CG 1 ATOM 580 C CD1 . PHE A 1 77 ? 72.220 23.479 45.224 1.00 9.40 ? 77 PHE A CD1 1 ATOM 581 C CD2 . PHE A 1 77 ? 70.043 22.607 45.723 1.00 8.61 ? 77 PHE A CD2 1 ATOM 582 C CE1 . PHE A 1 77 ? 72.530 23.417 46.577 1.00 10.95 ? 77 PHE A CE1 1 ATOM 583 C CE2 . PHE A 1 77 ? 70.369 22.547 47.060 1.00 9.73 ? 77 PHE A CE2 1 ATOM 584 C CZ . PHE A 1 77 ? 71.601 22.951 47.483 1.00 11.08 ? 77 PHE A CZ 1 ATOM 585 N N . SER A 1 78 ? 71.431 22.841 40.202 1.00 8.66 ? 78 SER A N 1 ATOM 586 C CA . SER A 1 78 ? 71.023 22.671 38.816 1.00 9.47 ? 78 SER A CA 1 ATOM 587 C C . SER A 1 78 ? 69.530 22.367 38.713 1.00 8.44 ? 78 SER A C 1 ATOM 588 O O . SER A 1 78 ? 68.840 22.903 37.805 1.00 9.67 ? 78 SER A O 1 ATOM 589 C CB . SER A 1 78 ? 71.877 21.601 38.172 1.00 13.53 ? 78 SER A CB 1 ATOM 590 O OG . SER A 1 78 ? 71.861 20.397 38.810 1.00 20.75 ? 78 SER A OG 1 ATOM 591 N N . ALA A 1 79 ? 68.963 21.570 39.618 1.00 7.93 ? 79 ALA A N 1 ATOM 592 C CA . ALA A 1 79 ? 67.540 21.209 39.557 1.00 8.30 ? 79 ALA A CA 1 ATOM 593 C C . ALA A 1 79 ? 66.605 22.381 39.867 1.00 7.88 ? 79 ALA A C 1 ATOM 594 O O . ALA A 1 79 ? 65.400 22.292 39.602 1.00 9.08 ? 79 ALA A O 1 ATOM 595 C CB . ALA A 1 79 ? 67.215 20.075 40.504 1.00 8.98 ? 79 ALA A CB 1 ATOM 596 N N . ASN A 1 80 ? 67.143 23.466 40.400 1.00 7.56 ? 80 ASN A N 1 ATOM 597 C CA . ASN A 1 80 ? 66.378 24.666 40.723 1.00 7.10 ? 80 ASN A CA 1 ATOM 598 C C . ASN A 1 80 ? 66.620 25.791 39.696 1.00 7.11 ? 80 ASN A C 1 ATOM 599 O O . ASN A 1 80 ? 66.261 26.932 39.971 1.00 8.15 ? 80 ASN A O 1 ATOM 600 C CB . ASN A 1 80 ? 66.704 25.150 42.118 1.00 7.06 ? 80 ASN A CB 1 ATOM 601 C CG . ASN A 1 80 ? 66.137 24.241 43.190 1.00 7.13 ? 80 ASN A CG 1 ATOM 602 O OD1 . ASN A 1 80 ? 64.985 23.787 43.095 1.00 8.67 ? 80 ASN A OD1 1 ATOM 603 N ND2 . ASN A 1 80 ? 66.910 23.924 44.238 1.00 7.09 ? 80 ASN A ND2 1 ATOM 604 N N . ASN A 1 81 ? 67.150 25.468 38.526 1.00 8.29 ? 81 ASN A N 1 ATOM 605 C CA . ASN A 1 81 ? 67.412 26.504 37.526 1.00 9.10 ? 81 ASN A CA 1 ATOM 606 C C . ASN A 1 81 ? 66.141 27.253 37.199 1.00 8.42 ? 81 ASN A C 1 ATOM 607 O O . ASN A 1 81 ? 65.132 26.648 36.872 1.00 10.54 ? 81 ASN A O 1 ATOM 608 C CB . ASN A 1 81 ? 68.040 25.859 36.307 1.00 11.01 ? 81 ASN A CB 1 ATOM 609 C CG . ASN A 1 81 ? 68.674 26.839 35.345 1.00 11.99 ? 81 ASN A CG 1 ATOM 610 O OD1 . ASN A 1 81 ? 68.910 27.990 35.675 1.00 14.61 ? 81 ASN A OD1 1 ATOM 611 N ND2 . ASN A 1 81 ? 68.965 26.390 34.103 1.00 13.83 ? 81 ASN A ND2 1 ATOM 612 N N . GLY A 1 82 ? 66.185 28.594 37.270 1.00 8.48 ? 82 GLY A N 1 ATOM 613 C CA . GLY A 1 82 ? 65.063 29.428 37.017 1.00 9.36 ? 82 GLY A CA 1 ATOM 614 C C . GLY A 1 82 ? 64.226 29.817 38.238 1.00 8.15 ? 82 GLY A C 1 ATOM 615 O O . GLY A 1 82 ? 63.365 30.716 38.130 1.00 9.43 ? 82 GLY A O 1 ATOM 616 N N . ILE A 1 83 ? 64.441 29.208 39.383 1.00 7.36 ? 83 ILE A N 1 ATOM 617 C CA . ILE A 1 83 ? 63.686 29.518 40.607 1.00 7.65 ? 83 ILE A CA 1 ATOM 618 C C . ILE A 1 83 ? 64.054 30.885 41.137 1.00 7.75 ? 83 ILE A C 1 ATOM 619 O O . ILE A 1 83 ? 63.289 31.519 41.888 1.00 8.21 ? 83 ILE A O 1 ATOM 620 C CB A ILE A 1 83 ? 63.726 28.374 41.647 0.52 7.86 ? 83 ILE A CB 1 ATOM 621 C CB B ILE A 1 83 ? 64.015 28.443 41.689 0.52 8.57 ? 83 ILE A CB 1 ATOM 622 C CG1 A ILE A 1 83 ? 62.415 28.247 42.424 0.52 7.46 ? 83 ILE A CG1 1 ATOM 623 C CG1 B ILE A 1 83 ? 63.285 27.135 41.350 0.52 9.78 ? 83 ILE A CG1 1 ATOM 624 C CG2 A ILE A 1 83 ? 64.963 28.569 42.503 0.52 7.60 ? 83 ILE A CG2 1 ATOM 625 C CG2 B ILE A 1 83 ? 63.800 28.912 43.111 0.52 12.92 ? 83 ILE A CG2 1 ATOM 626 C CD1 A ILE A 1 83 ? 61.226 27.691 41.689 0.52 9.56 ? 83 ILE A CD1 1 ATOM 627 C CD1 B ILE A 1 83 ? 61.810 27.200 41.644 0.52 11.87 ? 83 ILE A CD1 1 ATOM 628 N N . ASP A 1 84 ? 65.221 31.414 40.757 1.00 7.95 ? 84 ASP A N 1 ATOM 629 C CA . ASP A 1 84 ? 65.627 32.738 41.160 1.00 8.76 ? 84 ASP A CA 1 ATOM 630 C C . ASP A 1 84 ? 64.591 33.821 40.908 1.00 8.37 ? 84 ASP A C 1 ATOM 631 O O . ASP A 1 84 ? 64.466 34.720 41.747 1.00 9.02 ? 84 ASP A O 1 ATOM 632 C CB . ASP A 1 84 ? 66.975 33.149 40.471 1.00 10.86 ? 84 ASP A CB 1 ATOM 633 C CG . ASP A 1 84 ? 67.008 33.069 38.963 1.00 12.85 ? 84 ASP A CG 1 ATOM 634 O OD1 . ASP A 1 84 ? 68.052 33.451 38.378 1.00 24.37 ? 84 ASP A OD1 1 ATOM 635 O OD2 . ASP A 1 84 ? 66.126 32.592 38.266 1.00 14.00 ? 84 ASP A OD2 1 ATOM 636 N N . ASP A 1 85 ? 63.851 33.771 39.794 1.00 8.82 ? 85 ASP A N 1 ATOM 637 C CA . ASP A 1 85 ? 62.890 34.831 39.521 1.00 10.05 ? 85 ASP A CA 1 ATOM 638 C C . ASP A 1 85 ? 61.823 34.932 40.594 1.00 8.76 ? 85 ASP A C 1 ATOM 639 O O . ASP A 1 85 ? 61.519 36.047 41.089 1.00 9.33 ? 85 ASP A O 1 ATOM 640 C CB . ASP A 1 85 ? 62.279 34.614 38.142 1.00 13.56 ? 85 ASP A CB 1 ATOM 641 C CG . ASP A 1 85 ? 63.205 34.993 37.019 1.00 20.86 ? 85 ASP A CG 1 ATOM 642 O OD1 . ASP A 1 85 ? 64.250 35.700 37.148 1.00 22.18 ? 85 ASP A OD1 1 ATOM 643 O OD2 . ASP A 1 85 ? 62.830 34.566 35.883 1.00 34.06 ? 85 ASP A OD2 1 ATOM 644 N N . SER A 1 86 ? 61.233 33.820 41.003 1.00 8.17 ? 86 SER A N 1 ATOM 645 C CA . SER A 1 86 ? 60.193 33.823 42.032 1.00 7.63 ? 86 SER A CA 1 ATOM 646 C C . SER A 1 86 ? 60.765 34.247 43.402 1.00 7.02 ? 86 SER A C 1 ATOM 647 O O . SER A 1 86 ? 60.126 35.003 44.137 1.00 7.50 ? 86 SER A O 1 ATOM 648 C CB . SER A 1 86 ? 59.495 32.466 42.136 1.00 8.66 ? 86 SER A CB 1 ATOM 649 O OG . SER A 1 86 ? 60.402 31.433 42.470 1.00 8.83 ? 86 SER A OG 1 ATOM 650 N N . VAL A 1 87 ? 61.978 33.750 43.719 1.00 7.10 ? 87 VAL A N 1 ATOM 651 C CA . VAL A 1 87 ? 62.596 34.123 44.989 1.00 7.02 ? 87 VAL A CA 1 ATOM 652 C C . VAL A 1 87 ? 62.815 35.605 45.045 1.00 7.23 ? 87 VAL A C 1 ATOM 653 O O . VAL A 1 87 ? 62.508 36.292 46.062 1.00 7.94 ? 87 VAL A O 1 ATOM 654 C CB . VAL A 1 87 ? 63.907 33.316 45.166 1.00 7.68 ? 87 VAL A CB 1 ATOM 655 C CG1 . VAL A 1 87 ? 64.715 33.879 46.346 1.00 8.92 ? 87 VAL A CG1 1 ATOM 656 C CG2 . VAL A 1 87 ? 63.611 31.844 45.357 1.00 8.34 ? 87 VAL A CG2 1 ATOM 657 N N . ASN A 1 88 ? 63.406 36.174 43.987 1.00 7.38 ? 88 ASN A N 1 ATOM 658 C CA . ASN A 1 88 ? 63.688 37.596 43.957 1.00 7.75 ? 88 ASN A CA 1 ATOM 659 C C . ASN A 1 88 ? 62.394 38.433 43.960 1.00 7.57 ? 88 ASN A C 1 ATOM 660 O O . ASN A 1 88 ? 62.379 39.566 44.497 1.00 8.31 ? 88 ASN A O 1 ATOM 661 C CB . ASN A 1 88 ? 64.586 37.936 42.752 1.00 8.43 ? 88 ASN A CB 1 ATOM 662 C CG . ASN A 1 88 ? 66.014 37.431 42.965 1.00 8.68 ? 88 ASN A CG 1 ATOM 663 O OD1 . ASN A 1 88 ? 66.477 37.287 44.093 1.00 10.09 ? 88 ASN A OD1 1 ATOM 664 N ND2 . ASN A 1 88 ? 66.709 37.174 41.848 1.00 11.05 ? 88 ASN A ND2 1 ATOM 665 N N . ASN A 1 89 ? 61.304 37.897 43.380 1.00 7.22 ? 89 ASN A N 1 ATOM 666 C CA . ASN A 1 89 ? 60.029 38.615 43.461 1.00 7.63 ? 89 ASN A CA 1 ATOM 667 C C . ASN A 1 89 ? 59.405 38.573 44.844 1.00 7.99 ? 89 ASN A C 1 ATOM 668 O O . ASN A 1 89 ? 58.676 39.522 45.206 1.00 9.88 ? 89 ASN A O 1 ATOM 669 C CB . ASN A 1 89 ? 59.030 38.086 42.444 1.00 7.76 ? 89 ASN A CB 1 ATOM 670 C CG . ASN A 1 89 ? 59.199 38.779 41.084 1.00 8.30 ? 89 ASN A CG 1 ATOM 671 O OD1 . ASN A 1 89 ? 59.867 39.810 40.966 1.00 9.41 ? 89 ASN A OD1 1 ATOM 672 N ND2 . ASN A 1 89 ? 58.500 38.254 40.082 1.00 12.12 ? 89 ASN A ND2 1 ATOM 673 N N . LEU A 1 90 ? 59.610 37.520 45.649 1.00 6.95 ? 90 LEU A N 1 ATOM 674 C CA . LEU A 1 90 ? 58.965 37.447 46.968 1.00 7.01 ? 90 LEU A CA 1 ATOM 675 C C . LEU A 1 90 ? 59.791 38.081 48.081 1.00 7.53 ? 90 LEU A C 1 ATOM 676 O O . LEU A 1 90 ? 59.171 38.542 49.091 1.00 8.16 ? 90 LEU A O 1 ATOM 677 C CB . LEU A 1 90 ? 58.595 36.020 47.344 1.00 7.16 ? 90 LEU A CB 1 ATOM 678 C CG . LEU A 1 90 ? 57.478 35.385 46.529 1.00 7.33 ? 90 LEU A CG 1 ATOM 679 C CD1 . LEU A 1 90 ? 57.090 34.032 47.129 1.00 8.81 ? 90 LEU A CD1 1 ATOM 680 C CD2 . LEU A 1 90 ? 56.240 36.268 46.404 1.00 9.33 ? 90 LEU A CD2 1 ATOM 681 N N . ILE A 1 91 ? 61.117 38.158 47.974 1.00 7.83 ? 91 ILE A N 1 ATOM 682 C CA . ILE A 1 91 ? 61.907 38.752 49.053 1.00 8.38 ? 91 ILE A CA 1 ATOM 683 C C . ILE A 1 91 ? 61.413 40.139 49.431 1.00 8.33 ? 91 ILE A C 1 ATOM 684 O O . ILE A 1 91 ? 61.322 40.434 50.656 1.00 8.80 ? 91 ILE A O 1 ATOM 685 C CB . ILE A 1 91 ? 63.429 38.681 48.723 1.00 8.81 ? 91 ILE A CB 1 ATOM 686 C CG1 . ILE A 1 91 ? 63.937 37.250 48.932 1.00 9.18 ? 91 ILE A CG1 1 ATOM 687 C CG2 . ILE A 1 91 ? 64.231 39.724 49.468 1.00 10.96 ? 91 ILE A CG2 1 ATOM 688 C CD1 . ILE A 1 91 ? 65.349 36.998 48.451 1.00 11.02 ? 91 ILE A CD1 1 ATOM 689 N N . PRO A 1 92 ? 61.075 41.052 48.519 1.00 8.63 ? 92 PRO A N 1 ATOM 690 C CA . PRO A 1 92 ? 60.597 42.386 48.959 1.00 9.69 ? 92 PRO A CA 1 ATOM 691 C C . PRO A 1 92 ? 59.335 42.309 49.801 1.00 9.17 ? 92 PRO A C 1 ATOM 692 O O . PRO A 1 92 ? 59.134 43.187 50.684 1.00 10.12 ? 92 PRO A O 1 ATOM 693 C CB . PRO A 1 92 ? 60.419 43.123 47.632 1.00 11.13 ? 92 PRO A CB 1 ATOM 694 C CG . PRO A 1 92 ? 61.347 42.447 46.698 1.00 12.66 ? 92 PRO A CG 1 ATOM 695 C CD . PRO A 1 92 ? 61.305 40.997 47.053 1.00 10.06 ? 92 PRO A CD 1 ATOM 696 N N . PHE A 1 93 ? 58.484 41.330 49.583 1.00 8.36 ? 93 PHE A N 1 ATOM 697 C CA . PHE A 1 93 ? 57.282 41.177 50.382 1.00 8.64 ? 93 PHE A CA 1 ATOM 698 C C . PHE A 1 93 ? 57.603 40.680 51.779 1.00 8.55 ? 93 PHE A C 1 ATOM 699 O O . PHE A 1 93 ? 56.943 41.075 52.763 1.00 9.48 ? 93 PHE A O 1 ATOM 700 C CB . PHE A 1 93 ? 56.242 40.253 49.710 1.00 8.59 ? 93 PHE A CB 1 ATOM 701 C CG . PHE A 1 93 ? 55.734 40.792 48.412 1.00 8.49 ? 93 PHE A CG 1 ATOM 702 C CD1 . PHE A 1 93 ? 56.410 40.564 47.226 1.00 8.87 ? 93 PHE A CD1 1 ATOM 703 C CD2 . PHE A 1 93 ? 54.558 41.567 48.341 1.00 9.98 ? 93 PHE A CD2 1 ATOM 704 C CE1 . PHE A 1 93 ? 56.004 41.061 46.004 1.00 10.17 ? 93 PHE A CE1 1 ATOM 705 C CE2 . PHE A 1 93 ? 54.145 42.088 47.126 1.00 11.50 ? 93 PHE A CE2 1 ATOM 706 C CZ . PHE A 1 93 ? 54.855 41.820 45.985 1.00 11.00 ? 93 PHE A CZ 1 ATOM 707 N N . MET A 1 94 ? 58.575 39.770 51.867 1.00 8.71 ? 94 MET A N 1 ATOM 708 C CA . MET A 1 94 ? 59.048 39.307 53.185 1.00 8.94 ? 94 MET A CA 1 ATOM 709 C C . MET A 1 94 ? 59.533 40.465 54.002 1.00 9.02 ? 94 MET A C 1 ATOM 710 O O . MET A 1 94 ? 59.282 40.556 55.235 1.00 10.60 ? 94 MET A O 1 ATOM 711 C CB . MET A 1 94 ? 60.169 38.288 52.963 1.00 9.37 ? 94 MET A CB 1 ATOM 712 C CG . MET A 1 94 ? 60.812 37.746 54.226 1.00 10.20 ? 94 MET A CG 1 ATOM 713 S SD . MET A 1 94 ? 62.260 36.745 53.943 1.00 10.96 ? 94 MET A SD 1 ATOM 714 C CE . MET A 1 94 ? 63.455 37.986 53.501 1.00 13.95 ? 94 MET A CE 1 ATOM 715 N N . GLN A 1 95 ? 60.282 41.398 53.368 1.00 9.15 ? 95 GLN A N 1 ATOM 716 C CA . GLN A 1 95 ? 60.847 42.524 54.080 1.00 10.61 ? 95 GLN A CA 1 ATOM 717 C C . GLN A 1 95 ? 59.788 43.514 54.544 1.00 10.95 ? 95 GLN A C 1 ATOM 718 O O . GLN A 1 95 ? 59.910 44.111 55.625 1.00 13.25 ? 95 GLN A O 1 ATOM 719 C CB . GLN A 1 95 ? 61.886 43.227 53.178 1.00 11.61 ? 95 GLN A CB 1 ATOM 720 C CG . GLN A 1 95 ? 63.050 42.293 52.816 1.00 11.65 ? 95 GLN A CG 1 ATOM 721 C CD . GLN A 1 95 ? 64.076 42.880 51.883 1.00 14.50 ? 95 GLN A CD 1 ATOM 722 O OE1 . GLN A 1 95 ? 65.305 42.555 52.035 1.00 19.01 ? 95 GLN A OE1 1 ATOM 723 N NE2 . GLN A 1 95 ? 63.665 43.666 50.948 1.00 16.17 ? 95 GLN A NE2 1 ATOM 724 N N . LYS A 1 96 ? 58.757 43.720 53.756 1.00 10.79 ? 96 LYS A N 1 ATOM 725 C CA . LYS A 1 96 ? 57.684 44.701 54.005 1.00 11.41 ? 96 LYS A CA 1 ATOM 726 C C . LYS A 1 96 ? 56.628 44.147 54.952 1.00 10.68 ? 96 LYS A C 1 ATOM 727 O O . LYS A 1 96 ? 56.239 44.794 55.937 1.00 12.47 ? 96 LYS A O 1 ATOM 728 C CB . LYS A 1 96 ? 57.080 45.138 52.708 1.00 12.38 ? 96 LYS A CB 1 ATOM 729 C CG . LYS A 1 96 ? 55.898 46.063 52.789 1.00 15.04 ? 96 LYS A CG 1 ATOM 730 C CD . LYS A 1 96 ? 55.442 46.439 51.396 1.00 19.46 ? 96 LYS A CD 1 ATOM 731 C CE . LYS A 1 96 ? 54.221 47.380 51.339 1.00 31.16 ? 96 LYS A CE 1 ATOM 732 N NZ . LYS A 1 96 ? 53.959 47.647 49.894 1.00 32.52 ? 96 LYS A NZ 1 ATOM 733 N N . HIS A 1 97 ? 56.123 42.958 54.652 1.00 10.06 ? 97 HIS A N 1 ATOM 734 C CA . HIS A 1 97 ? 55.058 42.311 55.392 1.00 10.11 ? 97 HIS A CA 1 ATOM 735 C C . HIS A 1 97 ? 55.703 41.458 56.470 1.00 10.26 ? 97 HIS A C 1 ATOM 736 O O . HIS A 1 97 ? 55.681 40.229 56.479 1.00 10.08 ? 97 HIS A O 1 ATOM 737 C CB . HIS A 1 97 ? 54.149 41.491 54.471 1.00 10.06 ? 97 HIS A CB 1 ATOM 738 C CG . HIS A 1 97 ? 53.418 42.378 53.489 1.00 9.69 ? 97 HIS A CG 1 ATOM 739 N ND1 . HIS A 1 97 ? 52.197 42.933 53.763 1.00 11.35 ? 97 HIS A ND1 1 ATOM 740 C CD2 . HIS A 1 97 ? 53.791 42.797 52.265 1.00 10.65 ? 97 HIS A CD2 1 ATOM 741 C CE1 . HIS A 1 97 ? 51.834 43.680 52.725 1.00 11.86 ? 97 HIS A CE1 1 ATOM 742 N NE2 . HIS A 1 97 ? 52.799 43.618 51.790 1.00 10.97 ? 97 HIS A NE2 1 ATOM 743 N N . ASN A 1 98 ? 56.322 42.170 57.448 1.00 11.05 ? 98 ASN A N 1 ATOM 744 C CA . ASN A 1 98 ? 57.306 41.591 58.328 1.00 11.70 ? 98 ASN A CA 1 ATOM 745 C C . ASN A 1 98 ? 56.714 41.040 59.592 1.00 11.48 ? 98 ASN A C 1 ATOM 746 O O . ASN A 1 98 ? 57.454 40.740 60.521 1.00 12.90 ? 98 ASN A O 1 ATOM 747 C CB . ASN A 1 98 ? 58.458 42.535 58.583 1.00 13.18 ? 98 ASN A CB 1 ATOM 748 C CG . ASN A 1 98 ? 58.027 43.728 59.438 1.00 16.13 ? 98 ASN A CG 1 ATOM 749 O OD1 . ASN A 1 98 ? 56.843 43.982 59.646 1.00 18.90 ? 98 ASN A OD1 1 ATOM 750 N ND2 . ASN A 1 98 ? 59.010 44.441 59.923 1.00 17.96 ? 98 ASN A ND2 1 ATOM 751 N N . THR A 1 99 ? 55.410 40.772 59.614 1.00 10.84 ? 99 THR A N 1 ATOM 752 C CA . THR A 1 99 ? 54.813 39.935 60.644 1.00 11.06 ? 99 THR A CA 1 ATOM 753 C C . THR A 1 99 ? 54.517 38.528 60.124 1.00 9.84 ? 99 THR A C 1 ATOM 754 O O . THR A 1 99 ? 54.008 37.681 60.913 1.00 12.25 ? 99 THR A O 1 ATOM 755 C CB . THR A 1 99 ? 53.545 40.535 61.300 1.00 12.95 ? 99 THR A CB 1 ATOM 756 O OG1 . THR A 1 99 ? 52.460 40.518 60.371 1.00 14.03 ? 99 THR A OG1 1 ATOM 757 C CG2 . THR A 1 99 ? 53.810 41.967 61.791 1.00 16.84 ? 99 THR A CG2 1 ATOM 758 N N . ILE A 1 100 ? 54.750 38.264 58.838 1.00 8.87 ? 100 ILE A N 1 ATOM 759 C CA . ILE A 1 100 ? 54.439 36.972 58.211 1.00 8.40 ? 100 ILE A CA 1 ATOM 760 C C . ILE A 1 100 ? 55.743 36.273 57.857 1.00 7.94 ? 100 ILE A C 1 ATOM 761 O O . ILE A 1 100 ? 56.611 36.838 57.173 1.00 8.70 ? 100 ILE A O 1 ATOM 762 C CB . ILE A 1 100 ? 53.550 37.228 56.974 1.00 8.29 ? 100 ILE A CB 1 ATOM 763 C CG1 . ILE A 1 100 ? 52.180 37.746 57.403 1.00 9.57 ? 100 ILE A CG1 1 ATOM 764 C CG2 . ILE A 1 100 ? 53.453 35.960 56.136 1.00 8.13 ? 100 ILE A CG2 1 ATOM 765 C CD1 . ILE A 1 100 ? 51.336 38.266 56.293 1.00 10.52 ? 100 ILE A CD1 1 ATOM 766 N N . SER A 1 101 ? 55.937 35.043 58.326 1.00 7.47 ? 101 SER A N 1 ATOM 767 C CA . SER A 1 101 ? 57.175 34.320 58.066 1.00 7.26 ? 101 SER A CA 1 ATOM 768 C C . SER A 1 101 ? 57.386 34.086 56.552 1.00 6.90 ? 101 SER A C 1 ATOM 769 O O . SER A 1 101 ? 56.436 34.008 55.763 1.00 7.08 ? 101 SER A O 1 ATOM 770 C CB . SER A 1 101 ? 57.192 32.989 58.789 1.00 7.60 ? 101 SER A CB 1 ATOM 771 O OG . SER A 1 101 ? 56.207 32.116 58.256 1.00 7.79 ? 101 SER A OG 1 ATOM 772 N N . ALA A 1 102 ? 58.664 33.912 56.187 1.00 7.03 ? 102 ALA A N 1 ATOM 773 C CA . ALA A 1 102 ? 59.002 33.544 54.802 1.00 6.93 ? 102 ALA A CA 1 ATOM 774 C C . ALA A 1 102 ? 58.243 32.288 54.355 1.00 6.51 ? 102 ALA A C 1 ATOM 775 O O . ALA A 1 102 ? 57.733 32.236 53.226 1.00 6.66 ? 102 ALA A O 1 ATOM 776 C CB . ALA A 1 102 ? 60.515 33.321 54.667 1.00 7.98 ? 102 ALA A CB 1 ATOM 777 N N . ALA A 1 103 ? 58.167 31.291 55.231 1.00 6.53 ? 103 ALA A N 1 ATOM 778 C CA . ALA A 1 103 ? 57.482 30.039 54.894 1.00 6.46 ? 103 ALA A CA 1 ATOM 779 C C . ALA A 1 103 ? 56.000 30.248 54.576 1.00 6.36 ? 103 ALA A C 1 ATOM 780 O O . ALA A 1 103 ? 55.453 29.692 53.640 1.00 6.49 ? 103 ALA A O 1 ATOM 781 C CB . ALA A 1 103 ? 57.635 29.035 56.028 1.00 7.21 ? 103 ALA A CB 1 ATOM 782 N N . ASP A 1 104 ? 55.339 31.042 55.482 1.00 6.27 ? 104 ASP A N 1 ATOM 783 C CA . ASP A 1 104 ? 53.913 31.341 55.283 1.00 6.28 ? 104 ASP A CA 1 ATOM 784 C C . ASP A 1 104 ? 53.717 32.174 53.999 1.00 6.33 ? 104 ASP A C 1 ATOM 785 O O . ASP A 1 104 ? 52.745 31.954 53.283 1.00 6.89 ? 104 ASP A O 1 ATOM 786 C CB . ASP A 1 104 ? 53.349 32.099 56.478 1.00 6.43 ? 104 ASP A CB 1 ATOM 787 C CG . ASP A 1 104 ? 53.025 31.302 57.721 1.00 7.24 ? 104 ASP A CG 1 ATOM 788 O OD1 . ASP A 1 104 ? 53.289 30.066 57.773 1.00 7.76 ? 104 ASP A OD1 1 ATOM 789 O OD2 . ASP A 1 104 ? 52.502 31.933 58.689 1.00 8.24 ? 104 ASP A OD2 1 ATOM 790 N N . LEU A 1 105 ? 54.630 33.132 53.767 1.00 6.45 ? 105 LEU A N 1 ATOM 791 C CA . LEU A 1 105 ? 54.563 33.963 52.536 1.00 6.37 ? 105 LEU A CA 1 ATOM 792 C C . LEU A 1 105 ? 54.582 33.095 51.289 1.00 6.36 ? 105 LEU A C 1 ATOM 793 O O . LEU A 1 105 ? 53.802 33.305 50.358 1.00 6.76 ? 105 LEU A O 1 ATOM 794 C CB . LEU A 1 105 ? 55.729 34.948 52.545 1.00 6.77 ? 105 LEU A CB 1 ATOM 795 C CG . LEU A 1 105 ? 56.007 35.702 51.237 1.00 6.94 ? 105 LEU A CG 1 ATOM 796 C CD1 . LEU A 1 105 ? 54.838 36.551 50.815 1.00 8.34 ? 105 LEU A CD1 1 ATOM 797 C CD2 . LEU A 1 105 ? 57.263 36.549 51.391 1.00 7.94 ? 105 LEU A CD2 1 ATOM 798 N N . VAL A 1 106 ? 55.514 32.118 51.221 1.00 6.29 ? 106 VAL A N 1 ATOM 799 C CA . VAL A 1 106 ? 55.612 31.277 50.031 1.00 5.88 ? 106 VAL A CA 1 ATOM 800 C C . VAL A 1 106 ? 54.296 30.556 49.802 1.00 6.03 ? 106 VAL A C 1 ATOM 801 O O . VAL A 1 106 ? 53.745 30.552 48.692 1.00 6.76 ? 106 VAL A O 1 ATOM 802 C CB . VAL A 1 106 ? 56.808 30.321 50.134 1.00 6.38 ? 106 VAL A CB 1 ATOM 803 C CG1 . VAL A 1 106 ? 56.741 29.248 49.057 1.00 7.47 ? 106 VAL A CG1 1 ATOM 804 C CG2 . VAL A 1 106 ? 58.139 31.068 50.063 1.00 7.44 ? 106 VAL A CG2 1 ATOM 805 N N . GLN A 1 107 ? 53.770 29.865 50.851 1.00 6.12 ? 107 GLN A N 1 ATOM 806 C CA . GLN A 1 107 ? 52.568 29.058 50.654 1.00 6.06 ? 107 GLN A CA 1 ATOM 807 C C . GLN A 1 107 ? 51.357 29.944 50.340 1.00 6.06 ? 107 GLN A C 1 ATOM 808 O O . GLN A 1 107 ? 50.525 29.595 49.495 1.00 6.74 ? 107 GLN A O 1 ATOM 809 C CB . GLN A 1 107 ? 52.299 28.116 51.844 1.00 6.48 ? 107 GLN A CB 1 ATOM 810 C CG . GLN A 1 107 ? 53.357 27.072 52.016 1.00 6.91 ? 107 GLN A CG 1 ATOM 811 C CD . GLN A 1 107 ? 53.667 26.239 50.759 1.00 6.69 ? 107 GLN A CD 1 ATOM 812 O OE1 . GLN A 1 107 ? 54.932 26.009 50.474 1.00 8.59 ? 107 GLN A OE1 1 ATOM 813 N NE2 . GLN A 1 107 ? 52.721 25.825 50.088 1.00 6.64 ? 107 GLN A NE2 1 ATOM 814 N N . PHE A 1 108 ? 51.228 31.063 51.039 1.00 6.25 ? 108 PHE A N 1 ATOM 815 C CA . PHE A 1 108 ? 50.103 31.962 50.816 1.00 6.42 ? 108 PHE A CA 1 ATOM 816 C C . PHE A 1 108 ? 50.173 32.564 49.393 1.00 6.37 ? 108 PHE A C 1 ATOM 817 O O . PHE A 1 108 ? 49.153 32.645 48.694 1.00 6.74 ? 108 PHE A O 1 ATOM 818 C CB . PHE A 1 108 ? 50.063 33.087 51.850 1.00 7.11 ? 108 PHE A CB 1 ATOM 819 C CG . PHE A 1 108 ? 48.832 33.965 51.737 1.00 7.00 ? 108 PHE A CG 1 ATOM 820 C CD1 . PHE A 1 108 ? 48.937 35.281 51.328 1.00 7.57 ? 108 PHE A CD1 1 ATOM 821 C CD2 . PHE A 1 108 ? 47.591 33.448 52.049 1.00 7.39 ? 108 PHE A CD2 1 ATOM 822 C CE1 . PHE A 1 108 ? 47.811 36.094 51.271 1.00 8.15 ? 108 PHE A CE1 1 ATOM 823 C CE2 . PHE A 1 108 ? 46.463 34.260 51.955 1.00 8.19 ? 108 PHE A CE2 1 ATOM 824 C CZ . PHE A 1 108 ? 46.570 35.572 51.579 1.00 8.41 ? 108 PHE A CZ 1 ATOM 825 N N . ALA A 1 109 ? 51.349 32.985 48.983 1.00 6.45 ? 109 ALA A N 1 ATOM 826 C CA . ALA A 1 109 ? 51.517 33.584 47.644 1.00 6.38 ? 109 ALA A CA 1 ATOM 827 C C . ALA A 1 109 ? 51.113 32.564 46.566 1.00 6.23 ? 109 ALA A C 1 ATOM 828 O O . ALA A 1 109 ? 50.511 32.947 45.572 1.00 6.91 ? 109 ALA A O 1 ATOM 829 C CB . ALA A 1 109 ? 52.938 34.097 47.426 1.00 7.35 ? 109 ALA A CB 1 ATOM 830 N N . GLY A 1 110 ? 51.449 31.293 46.749 1.00 6.39 ? 110 GLY A N 1 ATOM 831 C CA . GLY A 1 110 ? 51.010 30.269 45.819 1.00 6.88 ? 110 GLY A CA 1 ATOM 832 C C . GLY A 1 110 ? 49.504 30.105 45.773 1.00 6.68 ? 110 GLY A C 1 ATOM 833 O O . GLY A 1 110 ? 48.946 29.934 44.691 1.00 7.25 ? 110 GLY A O 1 ATOM 834 N N . ALA A 1 111 ? 48.853 30.143 46.964 1.00 6.95 ? 111 ALA A N 1 ATOM 835 C CA . ALA A 1 111 ? 47.381 30.058 47.010 1.00 7.09 ? 111 ALA A CA 1 ATOM 836 C C . ALA A 1 111 ? 46.728 31.251 46.285 1.00 7.03 ? 111 ALA A C 1 ATOM 837 O O . ALA A 1 111 ? 45.743 31.091 45.556 1.00 7.63 ? 111 ALA A O 1 ATOM 838 C CB . ALA A 1 111 ? 46.909 29.957 48.460 1.00 7.94 ? 111 ALA A CB 1 ATOM 839 N N . VAL A 1 112 ? 47.281 32.448 46.495 1.00 7.04 ? 112 VAL A N 1 ATOM 840 C CA . VAL A 1 112 ? 46.800 33.660 45.820 1.00 6.87 ? 112 VAL A CA 1 ATOM 841 C C . VAL A 1 112 ? 47.001 33.525 44.299 1.00 6.86 ? 112 VAL A C 1 ATOM 842 O O . VAL A 1 112 ? 46.074 33.771 43.503 1.00 7.81 ? 112 VAL A O 1 ATOM 843 C CB . VAL A 1 112 ? 47.462 34.915 46.371 1.00 7.50 ? 112 VAL A CB 1 ATOM 844 C CG1 . VAL A 1 112 ? 47.109 36.138 45.546 1.00 8.91 ? 112 VAL A CG1 1 ATOM 845 C CG2 . VAL A 1 112 ? 47.131 35.160 47.849 1.00 8.28 ? 112 VAL A CG2 1 ATOM 846 N N . ALA A 1 113 ? 48.224 33.127 43.889 1.00 6.95 ? 113 ALA A N 1 ATOM 847 C CA . ALA A 1 113 ? 48.510 32.944 42.446 1.00 7.04 ? 113 ALA A CA 1 ATOM 848 C C . ALA A 1 113 ? 47.539 31.987 41.806 1.00 7.24 ? 113 ALA A C 1 ATOM 849 O O . ALA A 1 113 ? 46.976 32.247 40.728 1.00 7.90 ? 113 ALA A O 1 ATOM 850 C CB . ALA A 1 113 ? 49.952 32.482 42.297 1.00 7.25 ? 113 ALA A CB 1 ATOM 851 N N . LEU A 1 114 ? 47.340 30.820 42.458 1.00 7.70 ? 114 LEU A N 1 ATOM 852 C CA . LEU A 1 114 ? 46.445 29.793 41.892 1.00 7.82 ? 114 LEU A CA 1 ATOM 853 C C . LEU A 1 114 ? 45.018 30.306 41.762 1.00 7.95 ? 114 LEU A C 1 ATOM 854 O O . LEU A 1 114 ? 44.310 29.927 40.823 1.00 8.93 ? 114 LEU A O 1 ATOM 855 C CB A LEU A 1 114 ? 46.365 28.510 42.729 0.52 8.39 ? 114 LEU A CB 1 ATOM 856 C CB B LEU A 1 114 ? 46.642 28.580 42.803 0.52 9.06 ? 114 LEU A CB 1 ATOM 857 C CG A LEU A 1 114 ? 47.530 27.572 42.505 0.52 7.42 ? 114 LEU A CG 1 ATOM 858 C CG B LEU A 1 114 ? 45.998 27.378 42.131 0.52 9.41 ? 114 LEU A CG 1 ATOM 859 C CD1 A LEU A 1 114 ? 47.796 26.690 43.748 0.52 9.68 ? 114 LEU A CD1 1 ATOM 860 C CD1 B LEU A 1 114 ? 46.860 26.889 40.975 0.52 15.82 ? 114 LEU A CD1 1 ATOM 861 C CD2 A LEU A 1 114 ? 47.280 26.688 41.280 0.52 8.58 ? 114 LEU A CD2 1 ATOM 862 C CD2 B LEU A 1 114 ? 45.739 26.332 43.191 0.52 12.12 ? 114 LEU A CD2 1 ATOM 863 N N . SER A 1 115 ? 44.590 31.152 42.699 1.00 8.10 ? 115 SER A N 1 ATOM 864 C CA . SER A 1 115 ? 43.225 31.655 42.659 1.00 8.66 ? 115 SER A CA 1 ATOM 865 C C . SER A 1 115 ? 42.947 32.442 41.390 1.00 8.36 ? 115 SER A C 1 ATOM 866 O O . SER A 1 115 ? 41.769 32.638 41.035 1.00 9.96 ? 115 SER A O 1 ATOM 867 C CB . SER A 1 115 ? 42.899 32.490 43.912 1.00 9.67 ? 115 SER A CB 1 ATOM 868 O OG . SER A 1 115 ? 43.405 33.841 43.819 1.00 10.77 ? 115 SER A OG 1 ATOM 869 N N . ASN A 1 116 ? 43.980 32.926 40.715 1.00 8.02 ? 116 ASN A N 1 ATOM 870 C CA . ASN A 1 116 ? 43.812 33.658 39.445 1.00 7.67 ? 116 ASN A CA 1 ATOM 871 C C . ASN A 1 116 ? 43.624 32.760 38.227 1.00 8.12 ? 116 ASN A C 1 ATOM 872 O O . ASN A 1 116 ? 43.422 33.317 37.118 1.00 10.19 ? 116 ASN A O 1 ATOM 873 C CB . ASN A 1 116 ? 45.031 34.538 39.217 1.00 8.22 ? 116 ASN A CB 1 ATOM 874 C CG . ASN A 1 116 ? 45.194 35.615 40.233 1.00 8.40 ? 116 ASN A CG 1 ATOM 875 O OD1 . ASN A 1 116 ? 44.241 36.054 40.901 1.00 10.32 ? 116 ASN A OD1 1 ATOM 876 N ND2 . ASN A 1 116 ? 46.406 36.111 40.396 1.00 9.78 ? 116 ASN A ND2 1 ATOM 877 N N . CYS A 1 117 ? 43.727 31.450 38.397 1.00 7.74 ? 117 CYS A N 1 ATOM 878 C CA . CYS A 1 117 ? 43.689 30.503 37.292 1.00 7.99 ? 117 CYS A CA 1 ATOM 879 C C . CYS A 1 117 ? 42.268 29.901 37.205 1.00 7.91 ? 117 CYS A C 1 ATOM 880 O O . CYS A 1 117 ? 41.917 29.138 38.124 1.00 8.78 ? 117 CYS A O 1 ATOM 881 C CB . CYS A 1 117 ? 44.752 29.415 37.477 1.00 8.63 ? 117 CYS A CB 1 ATOM 882 S SG . CYS A 1 117 ? 46.422 29.988 37.715 1.00 9.45 ? 117 CYS A SG 1 ATOM 883 N N . PRO A 1 118 ? 41.489 30.201 36.176 1.00 7.79 ? 118 PRO A N 1 ATOM 884 C CA . PRO A 1 118 ? 40.138 29.657 36.105 1.00 8.00 ? 118 PRO A CA 1 ATOM 885 C C . PRO A 1 118 ? 40.115 28.146 36.296 1.00 7.58 ? 118 PRO A C 1 ATOM 886 O O . PRO A 1 118 ? 40.865 27.405 35.631 1.00 7.96 ? 118 PRO A O 1 ATOM 887 C CB . PRO A 1 118 ? 39.681 30.070 34.694 1.00 9.01 ? 118 PRO A CB 1 ATOM 888 C CG . PRO A 1 118 ? 40.409 31.365 34.465 1.00 9.95 ? 118 PRO A CG 1 ATOM 889 C CD . PRO A 1 118 ? 41.780 31.131 35.053 1.00 8.25 ? 118 PRO A CD 1 ATOM 890 N N . GLY A 1 119 ? 39.229 27.712 37.210 1.00 8.16 ? 119 GLY A N 1 ATOM 891 C CA . GLY A 1 119 ? 39.083 26.319 37.562 1.00 8.48 ? 119 GLY A CA 1 ATOM 892 C C . GLY A 1 119 ? 39.851 25.838 38.758 1.00 8.12 ? 119 GLY A C 1 ATOM 893 O O . GLY A 1 119 ? 39.631 24.742 39.260 1.00 8.88 ? 119 GLY A O 1 ATOM 894 N N . ALA A 1 120 ? 40.815 26.661 39.236 1.00 8.10 ? 120 ALA A N 1 ATOM 895 C CA . ALA A 1 120 ? 41.631 26.196 40.364 1.00 7.79 ? 120 ALA A CA 1 ATOM 896 C C . ALA A 1 120 ? 40.798 26.116 41.639 1.00 8.08 ? 120 ALA A C 1 ATOM 897 O O . ALA A 1 120 ? 39.834 26.864 41.845 1.00 9.58 ? 120 ALA A O 1 ATOM 898 C CB . ALA A 1 120 ? 42.766 27.144 40.574 1.00 10.50 ? 120 ALA A CB 1 ATOM 899 N N . PRO A 1 121 ? 41.196 25.232 42.559 1.00 7.84 ? 121 PRO A N 1 ATOM 900 C CA . PRO A 1 121 ? 40.565 25.215 43.891 1.00 7.87 ? 121 PRO A CA 1 ATOM 901 C C . PRO A 1 121 ? 41.061 26.401 44.718 1.00 7.71 ? 121 PRO A C 1 ATOM 902 O O . PRO A 1 121 ? 42.095 27.016 44.448 1.00 9.25 ? 121 PRO A O 1 ATOM 903 C CB . PRO A 1 121 ? 41.059 23.903 44.486 1.00 9.00 ? 121 PRO A CB 1 ATOM 904 C CG . PRO A 1 121 ? 42.404 23.681 43.843 1.00 9.00 ? 121 PRO A CG 1 ATOM 905 C CD . PRO A 1 121 ? 42.274 24.233 42.423 1.00 8.19 ? 121 PRO A CD 1 ATOM 906 N N . ARG A 1 122 ? 40.296 26.651 45.786 1.00 8.55 ? 122 ARG A N 1 ATOM 907 C CA . ARG A 1 122 ? 40.620 27.603 46.855 1.00 7.98 ? 122 ARG A CA 1 ATOM 908 C C . ARG A 1 122 ? 41.431 26.837 47.880 1.00 8.03 ? 122 ARG A C 1 ATOM 909 O O . ARG A 1 122 ? 40.835 26.010 48.626 1.00 9.37 ? 122 ARG A O 1 ATOM 910 C CB . ARG A 1 122 ? 39.358 28.206 47.443 1.00 8.70 ? 122 ARG A CB 1 ATOM 911 C CG . ARG A 1 122 ? 39.583 29.438 48.274 1.00 8.76 ? 122 ARG A CG 1 ATOM 912 C CD . ARG A 1 122 ? 38.286 29.958 48.859 1.00 10.44 ? 122 ARG A CD 1 ATOM 913 N NE . ARG A 1 122 ? 38.496 31.157 49.644 1.00 10.67 ? 122 ARG A NE 1 ATOM 914 C CZ . ARG A 1 122 ? 37.590 31.638 50.510 1.00 13.44 ? 122 ARG A CZ 1 ATOM 915 N NH1 . ARG A 1 122 ? 36.410 31.027 50.625 1.00 16.54 ? 122 ARG A NH1 1 ATOM 916 N NH2 . ARG A 1 122 ? 37.899 32.718 51.250 1.00 14.60 ? 122 ARG A NH2 1 ATOM 917 N N . LEU A 1 123 ? 42.746 26.955 47.887 1.00 7.84 ? 123 LEU A N 1 ATOM 918 C CA . LEU A 1 123 ? 43.550 26.080 48.727 1.00 7.57 ? 123 LEU A CA 1 ATOM 919 C C . LEU A 1 123 ? 43.271 26.318 50.219 1.00 7.77 ? 123 LEU A C 1 ATOM 920 O O . LEU A 1 123 ? 43.056 27.437 50.652 1.00 8.82 ? 123 LEU A O 1 ATOM 921 C CB . LEU A 1 123 ? 45.049 26.310 48.493 1.00 8.25 ? 123 LEU A CB 1 ATOM 922 C CG . LEU A 1 123 ? 45.598 25.941 47.101 1.00 8.72 ? 123 LEU A CG 1 ATOM 923 C CD1 . LEU A 1 123 ? 47.105 25.995 47.115 1.00 10.78 ? 123 LEU A CD1 1 ATOM 924 C CD2 . LEU A 1 123 ? 45.143 24.562 46.619 1.00 9.38 ? 123 LEU A CD2 1 ATOM 925 N N . GLU A 1 124 ? 43.379 25.224 50.990 1.00 7.71 ? 124 GLU A N 1 ATOM 926 C CA . GLU A 1 124 ? 43.530 25.389 52.425 1.00 7.96 ? 124 GLU A CA 1 ATOM 927 C C . GLU A 1 124 ? 44.755 26.248 52.678 1.00 7.74 ? 124 GLU A C 1 ATOM 928 O O . GLU A 1 124 ? 45.814 26.071 51.991 1.00 8.89 ? 124 GLU A O 1 ATOM 929 C CB . GLU A 1 124 ? 43.713 24.039 53.103 1.00 8.68 ? 124 GLU A CB 1 ATOM 930 C CG . GLU A 1 124 ? 43.853 24.146 54.611 1.00 9.69 ? 124 GLU A CG 1 ATOM 931 C CD . GLU A 1 124 ? 44.027 22.776 55.271 1.00 10.41 ? 124 GLU A CD 1 ATOM 932 O OE1 . GLU A 1 124 ? 43.100 22.310 55.975 1.00 16.30 ? 124 GLU A OE1 1 ATOM 933 O OE2 . GLU A 1 124 ? 45.117 22.169 55.087 1.00 10.20 ? 124 GLU A OE2 1 ATOM 934 N N . PHE A 1 125 ? 44.696 27.143 53.670 1.00 7.73 ? 125 PHE A N 1 ATOM 935 C CA . PHE A 1 125 ? 45.884 27.884 54.050 1.00 7.27 ? 125 PHE A CA 1 ATOM 936 C C . PHE A 1 125 ? 45.927 27.922 55.588 1.00 7.17 ? 125 PHE A C 1 ATOM 937 O O . PHE A 1 125 ? 45.091 28.573 56.251 1.00 8.58 ? 125 PHE A O 1 ATOM 938 C CB . PHE A 1 125 ? 45.905 29.310 53.488 1.00 8.07 ? 125 PHE A CB 1 ATOM 939 C CG . PHE A 1 125 ? 47.116 30.073 54.003 1.00 7.44 ? 125 PHE A CG 1 ATOM 940 C CD1 . PHE A 1 125 ? 48.403 29.663 53.658 1.00 8.07 ? 125 PHE A CD1 1 ATOM 941 C CD2 . PHE A 1 125 ? 46.916 31.149 54.842 1.00 7.92 ? 125 PHE A CD2 1 ATOM 942 C CE1 . PHE A 1 125 ? 49.500 30.313 54.216 1.00 8.09 ? 125 PHE A CE1 1 ATOM 943 C CE2 . PHE A 1 125 ? 48.032 31.799 55.410 1.00 8.62 ? 125 PHE A CE2 1 ATOM 944 C CZ . PHE A 1 125 ? 49.309 31.360 55.093 1.00 8.29 ? 125 PHE A CZ 1 ATOM 945 N N . LEU A 1 126 ? 46.911 27.192 56.109 1.00 7.45 ? 126 LEU A N 1 ATOM 946 C CA . LEU A 1 126 ? 47.243 27.209 57.525 1.00 7.48 ? 126 LEU A CA 1 ATOM 947 C C . LEU A 1 126 ? 48.445 28.137 57.705 1.00 7.56 ? 126 LEU A C 1 ATOM 948 O O . LEU A 1 126 ? 49.297 28.185 56.803 1.00 8.82 ? 126 LEU A O 1 ATOM 949 C CB . LEU A 1 126 ? 47.549 25.813 58.047 1.00 8.12 ? 126 LEU A CB 1 ATOM 950 C CG . LEU A 1 126 ? 46.535 24.709 57.729 1.00 8.59 ? 126 LEU A CG 1 ATOM 951 C CD1 . LEU A 1 126 ? 46.968 23.416 58.389 1.00 10.21 ? 126 LEU A CD1 1 ATOM 952 C CD2 . LEU A 1 126 ? 45.107 25.111 58.099 1.00 9.60 ? 126 LEU A CD2 1 ATOM 953 N N . ALA A 1 127 ? 48.502 28.854 58.806 1.00 8.47 ? 127 ALA A N 1 ATOM 954 C CA . ALA A 1 127 ? 49.552 29.836 59.085 1.00 8.00 ? 127 ALA A CA 1 ATOM 955 C C . ALA A 1 127 ? 50.253 29.493 60.404 1.00 7.66 ? 127 ALA A C 1 ATOM 956 O O . ALA A 1 127 ? 49.764 28.711 61.224 1.00 9.26 ? 127 ALA A O 1 ATOM 957 C CB . ALA A 1 127 ? 48.959 31.221 59.127 1.00 10.06 ? 127 ALA A CB 1 ATOM 958 N N . GLY A 1 128 ? 51.404 30.132 60.581 1.00 7.94 ? 128 GLY A N 1 ATOM 959 C CA . GLY A 1 128 ? 52.165 29.959 61.788 1.00 8.38 ? 128 GLY A CA 1 ATOM 960 C C . GLY A 1 128 ? 53.445 29.186 61.640 1.00 8.30 ? 128 GLY A C 1 ATOM 961 O O . GLY A 1 128 ? 54.064 28.818 62.659 1.00 10.03 ? 128 GLY A O 1 ATOM 962 N N . ARG A 1 129 ? 53.952 28.959 60.412 1.00 7.57 ? 129 ARG A N 1 ATOM 963 C CA . ARG A 1 129 ? 55.245 28.329 60.254 1.00 7.72 ? 129 ARG A CA 1 ATOM 964 C C . ARG A 1 129 ? 56.342 29.257 60.759 1.00 7.71 ? 129 ARG A C 1 ATOM 965 O O . ARG A 1 129 ? 56.303 30.464 60.471 1.00 8.20 ? 129 ARG A O 1 ATOM 966 C CB . ARG A 1 129 ? 55.496 28.024 58.767 1.00 7.10 ? 129 ARG A CB 1 ATOM 967 C CG . ARG A 1 129 ? 54.461 27.092 58.141 1.00 7.43 ? 129 ARG A CG 1 ATOM 968 C CD . ARG A 1 129 ? 54.591 27.103 56.592 1.00 7.26 ? 129 ARG A CD 1 ATOM 969 N NE . ARG A 1 129 ? 53.511 26.373 55.948 1.00 7.43 ? 129 ARG A NE 1 ATOM 970 C CZ . ARG A 1 129 ? 52.262 26.865 55.856 1.00 7.31 ? 129 ARG A CZ 1 ATOM 971 N NH1 . ARG A 1 129 ? 51.968 28.083 56.277 1.00 7.77 ? 129 ARG A NH1 1 ATOM 972 N NH2 . ARG A 1 129 ? 51.334 26.089 55.305 1.00 8.46 ? 129 ARG A NH2 1 ATOM 973 N N . PRO A 1 130 ? 57.345 28.760 61.460 1.00 8.19 ? 130 PRO A N 1 ATOM 974 C CA . PRO A 1 130 ? 58.444 29.643 61.950 1.00 9.29 ? 130 PRO A CA 1 ATOM 975 C C . PRO A 1 130 ? 59.209 30.311 60.822 1.00 7.89 ? 130 PRO A C 1 ATOM 976 O O . PRO A 1 130 ? 59.255 29.871 59.685 1.00 8.69 ? 130 PRO A O 1 ATOM 977 C CB . PRO A 1 130 ? 59.351 28.682 62.730 1.00 12.16 ? 130 PRO A CB 1 ATOM 978 C CG . PRO A 1 130 ? 58.465 27.580 63.148 1.00 15.29 ? 130 PRO A CG 1 ATOM 979 C CD . PRO A 1 130 ? 57.458 27.411 62.044 1.00 9.83 ? 130 PRO A CD 1 ATOM 980 N N . ASN A 1 131 ? 59.886 31.399 61.213 1.00 8.62 ? 131 ASN A N 1 ATOM 981 C CA . ASN A 1 131 ? 60.738 32.213 60.323 1.00 8.57 ? 131 ASN A CA 1 ATOM 982 C C . ASN A 1 131 ? 62.218 31.872 60.425 1.00 9.01 ? 131 ASN A C 1 ATOM 983 O O . ASN A 1 131 ? 63.040 32.669 59.975 1.00 11.66 ? 131 ASN A O 1 ATOM 984 C CB . ASN A 1 131 ? 60.530 33.685 60.592 1.00 8.95 ? 131 ASN A CB 1 ATOM 985 C CG . ASN A 1 131 ? 60.973 34.553 59.391 1.00 8.79 ? 131 ASN A CG 1 ATOM 986 O OD1 . ASN A 1 131 ? 60.612 34.287 58.256 1.00 8.95 ? 131 ASN A OD1 1 ATOM 987 N ND2 . ASN A 1 131 ? 61.704 35.626 59.724 1.00 9.93 ? 131 ASN A ND2 1 ATOM 988 N N . LYS A 1 132 ? 62.582 30.736 60.971 1.00 10.10 ? 132 LYS A N 1 ATOM 989 C CA . LYS A 1 132 ? 63.957 30.293 61.087 1.00 10.29 ? 132 LYS A CA 1 ATOM 990 C C . LYS A 1 132 ? 64.074 28.887 60.565 1.00 9.58 ? 132 LYS A C 1 ATOM 991 O O . LYS A 1 132 ? 63.212 28.036 60.916 1.00 10.77 ? 132 LYS A O 1 ATOM 992 C CB . LYS A 1 132 ? 64.415 30.350 62.556 1.00 14.08 ? 132 LYS A CB 1 ATOM 993 C CG . LYS A 1 132 ? 64.465 31.779 63.148 1.00 27.09 ? 132 LYS A CG 1 ATOM 994 C CD . LYS A 1 132 ? 64.414 31.775 64.637 1.00 39.24 ? 132 LYS A CD 1 ATOM 995 C CE . LYS A 1 132 ? 63.697 30.658 65.382 1.00 56.36 ? 132 LYS A CE 1 ATOM 996 N NZ . LYS A 1 132 ? 62.238 30.394 65.103 1.00 73.78 ? 132 LYS A NZ 1 ATOM 997 N N . THR A 1 133 ? 65.088 28.585 59.782 1.00 9.09 ? 133 THR A N 1 ATOM 998 C CA . THR A 1 133 ? 65.325 27.254 59.249 1.00 8.55 ? 133 THR A CA 1 ATOM 999 C C . THR A 1 133 ? 66.791 27.106 58.848 1.00 8.15 ? 133 THR A C 1 ATOM 1000 O O . THR A 1 133 ? 67.650 27.882 59.244 1.00 10.19 ? 133 THR A O 1 ATOM 1001 C CB . THR A 1 133 ? 64.301 26.926 58.122 1.00 8.37 ? 133 THR A CB 1 ATOM 1002 O OG1 . THR A 1 133 ? 64.350 25.500 57.944 1.00 8.49 ? 133 THR A OG1 1 ATOM 1003 C CG2 . THR A 1 133 ? 64.575 27.693 56.819 1.00 8.86 ? 133 THR A CG2 1 ATOM 1004 N N . ILE A 1 134 ? 67.059 26.103 58.039 1.00 8.36 ? 134 ILE A N 1 ATOM 1005 C CA . ILE A 1 134 ? 68.357 25.766 57.423 1.00 7.80 ? 134 ILE A CA 1 ATOM 1006 C C . ILE A 1 134 ? 68.174 25.711 55.920 1.00 7.68 ? 134 ILE A C 1 ATOM 1007 O O . ILE A 1 134 ? 67.074 25.522 55.397 1.00 7.86 ? 134 ILE A O 1 ATOM 1008 C CB . ILE A 1 134 ? 68.886 24.425 57.973 1.00 9.26 ? 134 ILE A CB 1 ATOM 1009 C CG1 . ILE A 1 134 ? 67.887 23.266 57.657 1.00 11.93 ? 134 ILE A CG1 1 ATOM 1010 C CG2 . ILE A 1 134 ? 69.213 24.531 59.437 1.00 12.42 ? 134 ILE A CG2 1 ATOM 1011 C CD1 . ILE A 1 134 ? 68.437 21.897 57.682 1.00 16.02 ? 134 ILE A CD1 1 ATOM 1012 N N . ALA A 1 135 ? 69.289 25.820 55.194 1.00 7.99 ? 135 ALA A N 1 ATOM 1013 C CA . ALA A 1 135 ? 69.292 25.566 53.755 1.00 7.60 ? 135 ALA A CA 1 ATOM 1014 C C . ALA A 1 135 ? 69.174 24.068 53.497 1.00 7.60 ? 135 ALA A C 1 ATOM 1015 O O . ALA A 1 135 ? 69.822 23.257 54.173 1.00 8.67 ? 135 ALA A O 1 ATOM 1016 C CB . ALA A 1 135 ? 70.567 26.120 53.126 1.00 8.63 ? 135 ALA A CB 1 ATOM 1017 N N . ALA A 1 136 ? 68.369 23.656 52.513 1.00 7.55 ? 136 ALA A N 1 ATOM 1018 C CA . ALA A 1 136 ? 68.305 22.254 52.165 1.00 7.43 ? 136 ALA A CA 1 ATOM 1019 C C . ALA A 1 136 ? 69.534 21.814 51.380 1.00 7.55 ? 136 ALA A C 1 ATOM 1020 O O . ALA A 1 136 ? 70.292 22.606 50.819 1.00 8.73 ? 136 ALA A O 1 ATOM 1021 C CB . ALA A 1 136 ? 67.040 21.931 51.369 1.00 8.08 ? 136 ALA A CB 1 ATOM 1022 N N . VAL A 1 137 ? 69.710 20.486 51.326 1.00 7.81 ? 137 VAL A N 1 ATOM 1023 C CA . VAL A 1 137 ? 70.753 19.860 50.531 1.00 8.20 ? 137 VAL A CA 1 ATOM 1024 C C . VAL A 1 137 ? 70.271 19.624 49.085 1.00 7.53 ? 137 VAL A C 1 ATOM 1025 O O . VAL A 1 137 ? 69.081 19.655 48.790 1.00 9.17 ? 137 VAL A O 1 ATOM 1026 C CB . VAL A 1 137 ? 71.251 18.555 51.173 1.00 9.73 ? 137 VAL A CB 1 ATOM 1027 C CG1 . VAL A 1 137 ? 71.711 18.864 52.596 1.00 11.70 ? 137 VAL A CG1 1 ATOM 1028 C CG2 . VAL A 1 137 ? 70.172 17.471 51.161 1.00 10.54 ? 137 VAL A CG2 1 ATOM 1029 N N . ASP A 1 138 ? 71.231 19.395 48.191 1.00 7.71 ? 138 ASP A N 1 ATOM 1030 C CA . ASP A 1 138 ? 70.959 19.120 46.788 1.00 7.73 ? 138 ASP A CA 1 ATOM 1031 C C . ASP A 1 138 ? 70.377 17.693 46.645 1.00 8.41 ? 138 ASP A C 1 ATOM 1032 O O . ASP A 1 138 ? 70.435 16.859 47.528 1.00 11.49 ? 138 ASP A O 1 ATOM 1033 C CB . ASP A 1 138 ? 72.214 19.361 45.946 1.00 8.76 ? 138 ASP A CB 1 ATOM 1034 C CG . ASP A 1 138 ? 72.053 19.649 44.482 1.00 7.82 ? 138 ASP A CG 1 ATOM 1035 O OD1 . ASP A 1 138 ? 73.090 19.932 43.854 1.00 9.99 ? 138 ASP A OD1 1 ATOM 1036 O OD2 . ASP A 1 138 ? 70.920 19.564 43.944 1.00 8.71 ? 138 ASP A OD2 1 ATOM 1037 N N . GLY A 1 139 ? 69.715 17.456 45.530 1.00 7.81 ? 139 GLY A N 1 ATOM 1038 C CA . GLY A 1 139 ? 69.193 16.107 45.200 1.00 8.52 ? 139 GLY A CA 1 ATOM 1039 C C . GLY A 1 139 ? 67.765 15.836 45.609 1.00 8.06 ? 139 GLY A C 1 ATOM 1040 O O . GLY A 1 139 ? 67.291 14.732 45.382 1.00 9.73 ? 139 GLY A O 1 ATOM 1041 N N . LEU A 1 140 ? 67.067 16.802 46.214 1.00 7.03 ? 140 LEU A N 1 ATOM 1042 C CA . LEU A 1 140 ? 65.711 16.580 46.739 1.00 7.26 ? 140 LEU A CA 1 ATOM 1043 C C . LEU A 1 140 ? 64.605 16.990 45.771 1.00 7.17 ? 140 LEU A C 1 ATOM 1044 O O . LEU A 1 140 ? 63.420 16.735 46.047 1.00 7.91 ? 140 LEU A O 1 ATOM 1045 C CB . LEU A 1 140 ? 65.518 17.291 48.081 1.00 7.07 ? 140 LEU A CB 1 ATOM 1046 C CG . LEU A 1 140 ? 66.507 16.849 49.180 1.00 8.15 ? 140 LEU A CG 1 ATOM 1047 C CD1 . LEU A 1 140 ? 66.333 17.721 50.401 1.00 10.04 ? 140 LEU A CD1 1 ATOM 1048 C CD2 . LEU A 1 140 ? 66.329 15.354 49.499 1.00 12.19 ? 140 LEU A CD2 1 ATOM 1049 N N . ILE A 1 141 ? 64.978 17.654 44.681 1.00 6.81 ? 141 ILE A N 1 ATOM 1050 C CA . ILE A 1 141 ? 64.002 18.172 43.720 1.00 6.89 ? 141 ILE A CA 1 ATOM 1051 C C . ILE A 1 141 ? 63.927 17.225 42.524 1.00 6.92 ? 141 ILE A C 1 ATOM 1052 O O . ILE A 1 141 ? 64.944 16.963 41.857 1.00 7.34 ? 141 ILE A O 1 ATOM 1053 C CB . ILE A 1 141 ? 64.459 19.569 43.211 1.00 7.18 ? 141 ILE A CB 1 ATOM 1054 C CG1 . ILE A 1 141 ? 64.689 20.578 44.349 1.00 7.54 ? 141 ILE A CG1 1 ATOM 1055 C CG2 . ILE A 1 141 ? 63.505 20.109 42.171 1.00 8.77 ? 141 ILE A CG2 1 ATOM 1056 C CD1 . ILE A 1 141 ? 63.489 20.885 45.210 1.00 9.12 ? 141 ILE A CD1 1 ATOM 1057 N N . PRO A 1 142 ? 62.736 16.721 42.206 1.00 7.52 ? 142 PRO A N 1 ATOM 1058 C CA . PRO A 1 142 ? 62.584 15.894 40.990 1.00 8.06 ? 142 PRO A CA 1 ATOM 1059 C C . PRO A 1 142 ? 63.000 16.689 39.734 1.00 8.09 ? 142 PRO A C 1 ATOM 1060 O O . PRO A 1 142 ? 62.796 17.876 39.633 1.00 9.09 ? 142 PRO A O 1 ATOM 1061 C CB . PRO A 1 142 ? 61.093 15.600 40.974 1.00 10.06 ? 142 PRO A CB 1 ATOM 1062 C CG . PRO A 1 142 ? 60.654 15.704 42.400 1.00 10.60 ? 142 PRO A CG 1 ATOM 1063 C CD . PRO A 1 142 ? 61.482 16.842 42.954 1.00 8.37 ? 142 PRO A CD 1 ATOM 1064 N N . GLU A 1 143 ? 63.569 15.925 38.772 1.00 8.05 ? 143 GLU A N 1 ATOM 1065 C CA . GLU A 1 143 ? 64.003 16.468 37.497 1.00 7.88 ? 143 GLU A CA 1 ATOM 1066 C C . GLU A 1 143 ? 63.292 15.731 36.353 1.00 7.29 ? 143 GLU A C 1 ATOM 1067 O O . GLU A 1 143 ? 62.928 14.551 36.506 1.00 7.48 ? 143 GLU A O 1 ATOM 1068 C CB . GLU A 1 143 ? 65.508 16.367 37.321 1.00 9.11 ? 143 GLU A CB 1 ATOM 1069 C CG . GLU A 1 143 ? 66.247 17.248 38.343 1.00 10.26 ? 143 GLU A CG 1 ATOM 1070 C CD . GLU A 1 143 ? 67.695 17.339 38.021 1.00 14.57 ? 143 GLU A CD 1 ATOM 1071 O OE1 . GLU A 1 143 ? 68.413 16.533 38.662 1.00 21.66 ? 143 GLU A OE1 1 ATOM 1072 O OE2 . GLU A 1 143 ? 68.102 18.212 37.216 1.00 24.14 ? 143 GLU A OE2 1 ATOM 1073 N N . PRO A 1 144 ? 63.126 16.400 35.202 1.00 7.43 ? 144 PRO A N 1 ATOM 1074 C CA . PRO A 1 144 ? 62.273 15.811 34.152 1.00 7.10 ? 144 PRO A CA 1 ATOM 1075 C C . PRO A 1 144 ? 62.849 14.579 33.497 1.00 7.29 ? 144 PRO A C 1 ATOM 1076 O O . PRO A 1 144 ? 62.105 13.836 32.860 1.00 7.96 ? 144 PRO A O 1 ATOM 1077 C CB . PRO A 1 144 ? 62.080 16.991 33.179 1.00 7.95 ? 144 PRO A CB 1 ATOM 1078 C CG . PRO A 1 144 ? 63.318 17.864 33.381 1.00 8.33 ? 144 PRO A CG 1 ATOM 1079 C CD . PRO A 1 144 ? 63.516 17.775 34.892 1.00 7.96 ? 144 PRO A CD 1 ATOM 1080 N N . GLN A 1 145 ? 64.178 14.355 33.608 1.00 7.40 ? 145 GLN A N 1 ATOM 1081 C CA . GLN A 1 145 ? 64.822 13.147 33.089 1.00 8.28 ? 145 GLN A CA 1 ATOM 1082 C C . GLN A 1 145 ? 64.652 11.953 34.034 1.00 8.04 ? 145 GLN A C 1 ATOM 1083 O O . GLN A 1 145 ? 65.080 10.837 33.661 1.00 9.59 ? 145 GLN A O 1 ATOM 1084 C CB . GLN A 1 145 ? 66.309 13.411 32.802 1.00 9.44 ? 145 GLN A CB 1 ATOM 1085 C CG . GLN A 1 145 ? 67.170 13.729 33.986 1.00 10.67 ? 145 GLN A CG 1 ATOM 1086 C CD . GLN A 1 145 ? 67.276 15.203 34.333 1.00 10.72 ? 145 GLN A CD 1 ATOM 1087 O OE1 . GLN A 1 145 ? 66.399 16.002 34.052 1.00 10.42 ? 145 GLN A OE1 1 ATOM 1088 N NE2 . GLN A 1 145 ? 68.367 15.571 34.997 1.00 15.51 ? 145 GLN A NE2 1 ATOM 1089 N N . ASP A 1 146 ? 64.109 12.133 35.227 1.00 7.96 ? 146 ASP A N 1 ATOM 1090 C CA . ASP A 1 146 ? 64.027 11.046 36.203 1.00 8.14 ? 146 ASP A CA 1 ATOM 1091 C C . ASP A 1 146 ? 62.989 10.004 35.814 1.00 8.06 ? 146 ASP A C 1 ATOM 1092 O O . ASP A 1 146 ? 61.973 10.284 35.177 1.00 9.17 ? 146 ASP A O 1 ATOM 1093 C CB . ASP A 1 146 ? 63.675 11.643 37.597 1.00 8.35 ? 146 ASP A CB 1 ATOM 1094 C CG . ASP A 1 146 ? 64.793 12.526 38.189 1.00 9.68 ? 146 ASP A CG 1 ATOM 1095 O OD1 . ASP A 1 146 ? 64.459 13.177 39.270 1.00 9.95 ? 146 ASP A OD1 1 ATOM 1096 O OD2 . ASP A 1 146 ? 65.934 12.542 37.675 1.00 11.13 ? 146 ASP A OD2 1 ATOM 1097 N N . SER A 1 147 ? 63.261 8.773 36.255 1.00 8.46 ? 147 SER A N 1 ATOM 1098 C CA . SER A 1 147 ? 62.331 7.680 36.065 1.00 8.51 ? 147 SER A CA 1 ATOM 1099 C C . SER A 1 147 ? 61.126 7.811 37.007 1.00 7.75 ? 147 SER A C 1 ATOM 1100 O O . SER A 1 147 ? 61.175 8.461 38.060 1.00 7.99 ? 147 SER A O 1 ATOM 1101 C CB . SER A 1 147 ? 63.005 6.337 36.318 1.00 9.37 ? 147 SER A CB 1 ATOM 1102 O OG . SER A 1 147 ? 63.255 6.182 37.731 1.00 9.66 ? 147 SER A OG 1 ATOM 1103 N N . VAL A 1 148 ? 60.038 7.101 36.661 1.00 7.61 ? 148 VAL A N 1 ATOM 1104 C CA . VAL A 1 148 ? 58.879 7.021 37.546 1.00 7.31 ? 148 VAL A CA 1 ATOM 1105 C C . VAL A 1 148 ? 59.251 6.428 38.910 1.00 7.34 ? 148 VAL A C 1 ATOM 1106 O O . VAL A 1 148 ? 58.813 6.916 39.971 1.00 7.51 ? 148 VAL A O 1 ATOM 1107 C CB . VAL A 1 148 ? 57.708 6.282 36.886 1.00 7.75 ? 148 VAL A CB 1 ATOM 1108 C CG1 . VAL A 1 148 ? 56.559 6.035 37.865 1.00 7.88 ? 148 VAL A CG1 1 ATOM 1109 C CG2 . VAL A 1 148 ? 57.222 7.126 35.691 1.00 8.63 ? 148 VAL A CG2 1 ATOM 1110 N N . THR A 1 149 ? 60.064 5.353 38.926 1.00 7.32 ? 149 THR A N 1 ATOM 1111 C CA . THR A 1 149 ? 60.468 4.796 40.198 1.00 7.60 ? 149 THR A CA 1 ATOM 1112 C C . THR A 1 149 ? 61.136 5.865 41.081 1.00 7.31 ? 149 THR A C 1 ATOM 1113 O O . THR A 1 149 ? 60.821 5.999 42.285 1.00 7.77 ? 149 THR A O 1 ATOM 1114 C CB . THR A 1 149 ? 61.399 3.599 40.009 1.00 8.16 ? 149 THR A CB 1 ATOM 1115 O OG1 . THR A 1 149 ? 60.577 2.570 39.428 1.00 8.56 ? 149 THR A OG1 1 ATOM 1116 C CG2 . THR A 1 149 ? 61.992 3.104 41.316 1.00 10.03 ? 149 THR A CG2 1 ATOM 1117 N N . LYS A 1 150 ? 62.061 6.616 40.478 1.00 7.52 ? 150 LYS A N 1 ATOM 1118 C CA . LYS A 1 150 ? 62.794 7.648 41.213 1.00 7.50 ? 150 LYS A CA 1 ATOM 1119 C C . LYS A 1 150 ? 61.876 8.747 41.718 1.00 7.24 ? 150 LYS A C 1 ATOM 1120 O O . LYS A 1 150 ? 61.955 9.206 42.876 1.00 7.81 ? 150 LYS A O 1 ATOM 1121 C CB . LYS A 1 150 ? 63.933 8.180 40.347 1.00 8.21 ? 150 LYS A CB 1 ATOM 1122 C CG . LYS A 1 150 ? 64.797 9.249 41.013 1.00 9.48 ? 150 LYS A CG 1 ATOM 1123 C CD . LYS A 1 150 ? 65.992 9.659 40.163 1.00 11.29 ? 150 LYS A CD 1 ATOM 1124 C CE . LYS A 1 150 ? 66.822 10.778 40.715 1.00 13.03 ? 150 LYS A CE 1 ATOM 1125 N NZ A LYS A 1 150 ? 68.235 10.712 40.264 0.52 20.51 ? 150 LYS A NZ 1 ATOM 1126 N NZ B LYS A 1 150 ? 67.554 10.404 41.926 0.52 14.46 ? 150 LYS A NZ 1 ATOM 1127 N N . ILE A 1 151 ? 60.957 9.218 40.854 1.00 7.33 ? 151 ILE A N 1 ATOM 1128 C CA . ILE A 1 151 ? 60.005 10.269 41.224 1.00 7.12 ? 151 ILE A CA 1 ATOM 1129 C C . ILE A 1 151 ? 59.100 9.826 42.366 1.00 6.85 ? 151 ILE A C 1 ATOM 1130 O O . ILE A 1 151 ? 58.913 10.518 43.371 1.00 7.27 ? 151 ILE A O 1 ATOM 1131 C CB . ILE A 1 151 ? 59.188 10.690 39.984 1.00 8.01 ? 151 ILE A CB 1 ATOM 1132 C CG1 . ILE A 1 151 ? 60.092 11.435 38.977 1.00 9.43 ? 151 ILE A CG1 1 ATOM 1133 C CG2 . ILE A 1 151 ? 57.954 11.490 40.418 1.00 9.84 ? 151 ILE A CG2 1 ATOM 1134 C CD1 . ILE A 1 151 ? 59.429 11.545 37.592 1.00 11.40 ? 151 ILE A CD1 1 ATOM 1135 N N . LEU A 1 152 ? 58.502 8.625 42.220 1.00 7.10 ? 152 LEU A N 1 ATOM 1136 C CA . LEU A 1 152 ? 57.562 8.163 43.260 1.00 7.46 ? 152 LEU A CA 1 ATOM 1137 C C . LEU A 1 152 ? 58.310 7.988 44.591 1.00 7.36 ? 152 LEU A C 1 ATOM 1138 O O . LEU A 1 152 ? 57.746 8.306 45.658 1.00 7.89 ? 152 LEU A O 1 ATOM 1139 C CB . LEU A 1 152 ? 56.867 6.861 42.844 1.00 7.53 ? 152 LEU A CB 1 ATOM 1140 C CG . LEU A 1 152 ? 55.915 7.035 41.627 1.00 8.02 ? 152 LEU A CG 1 ATOM 1141 C CD1 . LEU A 1 152 ? 55.309 5.662 41.318 1.00 9.03 ? 152 LEU A CD1 1 ATOM 1142 C CD2 . LEU A 1 152 ? 54.830 8.043 41.896 1.00 9.52 ? 152 LEU A CD2 1 ATOM 1143 N N . GLN A 1 153 ? 59.544 7.476 44.519 1.00 7.73 ? 153 GLN A N 1 ATOM 1144 C CA . GLN A 1 153 ? 60.307 7.298 45.771 1.00 8.26 ? 153 GLN A CA 1 ATOM 1145 C C . GLN A 1 153 ? 60.602 8.637 46.409 1.00 7.57 ? 153 GLN A C 1 ATOM 1146 O O . GLN A 1 153 ? 60.591 8.749 47.637 1.00 8.08 ? 153 GLN A O 1 ATOM 1147 C CB . GLN A 1 153 ? 61.587 6.512 45.465 1.00 9.77 ? 153 GLN A CB 1 ATOM 1148 C CG . GLN A 1 153 ? 62.347 6.161 46.739 1.00 14.85 ? 153 GLN A CG 1 ATOM 1149 C CD . GLN A 1 153 ? 63.126 7.068 47.555 1.00 16.24 ? 153 GLN A CD 1 ATOM 1150 O OE1 . GLN A 1 153 ? 63.545 8.092 46.941 1.00 17.86 ? 153 GLN A OE1 1 ATOM 1151 N NE2 . GLN A 1 153 ? 63.282 6.783 48.824 1.00 22.38 ? 153 GLN A NE2 1 ATOM 1152 N N . ARG A 1 154 ? 60.934 9.658 45.600 1.00 7.26 ? 154 ARG A N 1 ATOM 1153 C CA . ARG A 1 154 ? 61.261 10.971 46.134 1.00 6.95 ? 154 ARG A CA 1 ATOM 1154 C C . ARG A 1 154 ? 60.062 11.534 46.904 1.00 7.05 ? 154 ARG A C 1 ATOM 1155 O O . ARG A 1 154 ? 60.172 12.089 48.009 1.00 7.44 ? 154 ARG A O 1 ATOM 1156 C CB . ARG A 1 154 ? 61.710 11.904 44.994 1.00 7.21 ? 154 ARG A CB 1 ATOM 1157 C CG . ARG A 1 154 ? 62.157 13.294 45.403 1.00 7.65 ? 154 ARG A CG 1 ATOM 1158 C CD . ARG A 1 154 ? 63.468 13.369 46.153 1.00 8.12 ? 154 ARG A CD 1 ATOM 1159 N NE . ARG A 1 154 ? 63.401 13.044 47.579 1.00 7.74 ? 154 ARG A NE 1 ATOM 1160 C CZ . ARG A 1 154 ? 62.933 13.855 48.537 1.00 7.26 ? 154 ARG A CZ 1 ATOM 1161 N NH1 . ARG A 1 154 ? 62.524 15.083 48.267 1.00 7.23 ? 154 ARG A NH1 1 ATOM 1162 N NH2 . ARG A 1 154 ? 62.885 13.407 49.780 1.00 7.82 ? 154 ARG A NH2 1 ATOM 1163 N N . PHE A 1 155 ? 58.859 11.457 46.279 1.00 7.16 ? 155 PHE A N 1 ATOM 1164 C CA . PHE A 1 155 ? 57.648 11.965 46.955 1.00 7.05 ? 155 PHE A CA 1 ATOM 1165 C C . PHE A 1 155 ? 57.270 11.141 48.190 1.00 7.40 ? 155 PHE A C 1 ATOM 1166 O O . PHE A 1 155 ? 56.788 11.687 49.180 1.00 8.23 ? 155 PHE A O 1 ATOM 1167 C CB . PHE A 1 155 ? 56.478 11.992 45.941 1.00 7.62 ? 155 PHE A CB 1 ATOM 1168 C CG . PHE A 1 155 ? 56.478 13.243 45.052 1.00 7.12 ? 155 PHE A CG 1 ATOM 1169 C CD1 . PHE A 1 155 ? 55.741 14.362 45.434 1.00 8.59 ? 155 PHE A CD1 1 ATOM 1170 C CD2 . PHE A 1 155 ? 57.156 13.276 43.845 1.00 7.46 ? 155 PHE A CD2 1 ATOM 1171 C CE1 . PHE A 1 155 ? 55.663 15.466 44.611 1.00 8.98 ? 155 PHE A CE1 1 ATOM 1172 C CE2 . PHE A 1 155 ? 57.089 14.379 42.994 1.00 7.78 ? 155 PHE A CE2 1 ATOM 1173 C CZ . PHE A 1 155 ? 56.351 15.460 43.388 1.00 8.48 ? 155 PHE A CZ 1 ATOM 1174 N N . GLU A 1 156 ? 57.479 9.817 48.137 1.00 7.68 ? 156 GLU A N 1 ATOM 1175 C CA . GLU A 1 156 ? 57.194 8.995 49.319 1.00 8.18 ? 156 GLU A CA 1 ATOM 1176 C C . GLU A 1 156 ? 58.146 9.386 50.448 1.00 8.07 ? 156 GLU A C 1 ATOM 1177 O O . GLU A 1 156 ? 57.738 9.506 51.622 1.00 9.00 ? 156 GLU A O 1 ATOM 1178 C CB . GLU A 1 156 ? 57.344 7.507 48.958 1.00 10.64 ? 156 GLU A CB 1 ATOM 1179 C CG . GLU A 1 156 ? 57.048 6.612 50.141 1.00 18.13 ? 156 GLU A CG 1 ATOM 1180 C CD . GLU A 1 156 ? 57.153 5.147 49.788 1.00 28.68 ? 156 GLU A CD 1 ATOM 1181 O OE1 . GLU A 1 156 ? 56.867 4.308 50.624 1.00 38.86 ? 156 GLU A OE1 1 ATOM 1182 O OE2 . GLU A 1 156 ? 57.499 4.777 48.650 1.00 38.93 ? 156 GLU A OE2 1 ATOM 1183 N N . ASP A 1 157 ? 59.424 9.577 50.130 1.00 8.18 ? 157 ASP A N 1 ATOM 1184 C CA . ASP A 1 157 ? 60.439 9.949 51.125 1.00 8.52 ? 157 ASP A CA 1 ATOM 1185 C C . ASP A 1 157 ? 60.185 11.365 51.651 1.00 8.17 ? 157 ASP A C 1 ATOM 1186 O O . ASP A 1 157 ? 60.492 11.635 52.834 1.00 9.06 ? 157 ASP A O 1 ATOM 1187 C CB . ASP A 1 157 ? 61.834 9.819 50.532 1.00 9.08 ? 157 ASP A CB 1 ATOM 1188 C CG . ASP A 1 157 ? 62.945 10.156 51.512 1.00 9.73 ? 157 ASP A CG 1 ATOM 1189 O OD1 . ASP A 1 157 ? 63.718 11.089 51.209 1.00 10.53 ? 157 ASP A OD1 1 ATOM 1190 O OD2 . ASP A 1 157 ? 62.996 9.493 52.561 1.00 11.38 ? 157 ASP A OD2 1 ATOM 1191 N N . ALA A 1 158 ? 59.697 12.279 50.826 1.00 7.65 ? 158 ALA A N 1 ATOM 1192 C CA . ALA A 1 158 ? 59.468 13.642 51.291 1.00 7.60 ? 158 ALA A CA 1 ATOM 1193 C C . ALA A 1 158 ? 58.316 13.737 52.305 1.00 8.17 ? 158 ALA A C 1 ATOM 1194 O O . ALA A 1 158 ? 58.388 14.476 53.273 1.00 9.68 ? 158 ALA A O 1 ATOM 1195 C CB . ALA A 1 158 ? 59.205 14.560 50.110 1.00 8.29 ? 158 ALA A CB 1 ATOM 1196 N N . GLY A 1 159 ? 57.222 13.013 52.003 1.00 9.58 ? 159 GLY A N 1 ATOM 1197 C CA . GLY A 1 159 ? 56.003 13.232 52.808 1.00 13.65 ? 159 GLY A CA 1 ATOM 1198 C C . GLY A 1 159 ? 54.982 12.120 52.782 1.00 9.83 ? 159 GLY A C 1 ATOM 1199 O O . GLY A 1 159 ? 53.814 12.350 53.110 1.00 10.82 ? 159 GLY A O 1 ATOM 1200 N N . GLY A 1 160 ? 55.391 10.917 52.367 1.00 9.29 ? 160 GLY A N 1 ATOM 1201 C CA . GLY A 1 160 ? 54.444 9.807 52.345 1.00 9.47 ? 160 GLY A CA 1 ATOM 1202 C C . GLY A 1 160 ? 53.414 9.961 51.266 1.00 8.92 ? 160 GLY A C 1 ATOM 1203 O O . GLY A 1 160 ? 52.328 9.355 51.376 1.00 12.24 ? 160 GLY A O 1 ATOM 1204 N N . PHE A 1 161 ? 53.664 10.746 50.220 1.00 8.09 ? 161 PHE A N 1 ATOM 1205 C CA . PHE A 1 161 ? 52.658 10.902 49.172 1.00 8.52 ? 161 PHE A CA 1 ATOM 1206 C C . PHE A 1 161 ? 52.462 9.625 48.408 1.00 8.68 ? 161 PHE A C 1 ATOM 1207 O O . PHE A 1 161 ? 53.464 8.906 48.082 1.00 9.55 ? 161 PHE A O 1 ATOM 1208 C CB . PHE A 1 161 ? 53.120 11.972 48.142 1.00 8.50 ? 161 PHE A CB 1 ATOM 1209 C CG . PHE A 1 161 ? 53.170 13.360 48.698 1.00 8.27 ? 161 PHE A CG 1 ATOM 1210 C CD1 . PHE A 1 161 ? 54.369 13.923 49.115 1.00 9.86 ? 161 PHE A CD1 1 ATOM 1211 C CD2 . PHE A 1 161 ? 52.010 14.153 48.781 1.00 10.63 ? 161 PHE A CD2 1 ATOM 1212 C CE1 . PHE A 1 161 ? 54.355 15.212 49.612 1.00 13.28 ? 161 PHE A CE1 1 ATOM 1213 C CE2 . PHE A 1 161 ? 52.049 15.415 49.310 1.00 12.17 ? 161 PHE A CE2 1 ATOM 1214 C CZ . PHE A 1 161 ? 53.231 15.953 49.694 1.00 12.51 ? 161 PHE A CZ 1 ATOM 1215 N N . THR A 1 162 ? 51.217 9.325 48.120 1.00 8.79 ? 162 THR A N 1 ATOM 1216 C CA . THR A 1 162 ? 50.878 8.191 47.278 1.00 8.84 ? 162 THR A CA 1 ATOM 1217 C C . THR A 1 162 ? 51.027 8.579 45.818 1.00 8.27 ? 162 THR A C 1 ATOM 1218 O O . THR A 1 162 ? 51.017 9.756 45.453 1.00 7.92 ? 162 THR A O 1 ATOM 1219 C CB . THR A 1 162 ? 49.430 7.753 47.554 1.00 10.38 ? 162 THR A CB 1 ATOM 1220 O OG1 . THR A 1 162 ? 48.594 8.845 47.139 1.00 10.21 ? 162 THR A OG1 1 ATOM 1221 C CG2 . THR A 1 162 ? 49.154 7.419 49.027 1.00 13.76 ? 162 THR A CG2 1 ATOM 1222 N N . PRO A 1 163 ? 51.100 7.584 44.905 1.00 8.21 ? 163 PRO A N 1 ATOM 1223 C CA . PRO A 1 163 ? 51.096 7.927 43.473 1.00 8.28 ? 163 PRO A CA 1 ATOM 1224 C C . PRO A 1 163 ? 49.885 8.758 43.064 1.00 7.36 ? 163 PRO A C 1 ATOM 1225 O O . PRO A 1 163 ? 50.034 9.647 42.214 1.00 7.81 ? 163 PRO A O 1 ATOM 1226 C CB . PRO A 1 163 ? 51.154 6.540 42.817 1.00 10.12 ? 163 PRO A CB 1 ATOM 1227 C CG . PRO A 1 163 ? 51.911 5.714 43.850 1.00 10.84 ? 163 PRO A CG 1 ATOM 1228 C CD . PRO A 1 163 ? 51.361 6.138 45.151 1.00 9.65 ? 163 PRO A CD 1 ATOM 1229 N N . PHE A 1 164 ? 48.706 8.481 43.655 1.00 7.96 ? 164 PHE A N 1 ATOM 1230 C CA . PHE A 1 164 ? 47.535 9.296 43.366 1.00 7.48 ? 164 PHE A CA 1 ATOM 1231 C C . PHE A 1 164 ? 47.804 10.765 43.689 1.00 7.26 ? 164 PHE A C 1 ATOM 1232 O O . PHE A 1 164 ? 47.487 11.663 42.908 1.00 7.30 ? 164 PHE A O 1 ATOM 1233 C CB . PHE A 1 164 ? 46.295 8.788 44.112 1.00 8.32 ? 164 PHE A CB 1 ATOM 1234 C CG . PHE A 1 164 ? 45.061 9.598 43.860 1.00 8.01 ? 164 PHE A CG 1 ATOM 1235 C CD1 . PHE A 1 164 ? 44.351 9.357 42.676 1.00 9.43 ? 164 PHE A CD1 1 ATOM 1236 C CD2 . PHE A 1 164 ? 44.626 10.590 44.694 1.00 9.03 ? 164 PHE A CD2 1 ATOM 1237 C CE1 . PHE A 1 164 ? 43.248 10.114 42.383 1.00 10.02 ? 164 PHE A CE1 1 ATOM 1238 C CE2 . PHE A 1 164 ? 43.522 11.342 44.378 1.00 9.77 ? 164 PHE A CE2 1 ATOM 1239 C CZ . PHE A 1 164 ? 42.840 11.117 43.205 1.00 9.75 ? 164 PHE A CZ 1 ATOM 1240 N N . GLU A 1 165 ? 48.385 11.022 44.873 1.00 7.27 ? 165 GLU A N 1 ATOM 1241 C CA . GLU A 1 165 ? 48.693 12.389 45.256 1.00 7.21 ? 165 GLU A CA 1 ATOM 1242 C C . GLU A 1 165 ? 49.745 13.037 44.344 1.00 6.87 ? 165 GLU A C 1 ATOM 1243 O O . GLU A 1 165 ? 49.676 14.232 44.074 1.00 7.13 ? 165 GLU A O 1 ATOM 1244 C CB . GLU A 1 165 ? 49.120 12.438 46.739 1.00 7.65 ? 165 GLU A CB 1 ATOM 1245 C CG . GLU A 1 165 ? 47.950 12.120 47.687 1.00 8.82 ? 165 GLU A CG 1 ATOM 1246 C CD . GLU A 1 165 ? 48.366 11.838 49.124 1.00 9.41 ? 165 GLU A CD 1 ATOM 1247 O OE1 . GLU A 1 165 ? 47.565 12.106 50.040 1.00 14.57 ? 165 GLU A OE1 1 ATOM 1248 O OE2 . GLU A 1 165 ? 49.457 11.320 49.388 1.00 10.93 ? 165 GLU A OE2 1 ATOM 1249 N N . VAL A 1 166 ? 50.757 12.260 43.908 1.00 7.01 ? 166 VAL A N 1 ATOM 1250 C CA . VAL A 1 166 ? 51.793 12.788 43.015 1.00 6.78 ? 166 VAL A CA 1 ATOM 1251 C C . VAL A 1 166 ? 51.172 13.273 41.695 1.00 6.42 ? 166 VAL A C 1 ATOM 1252 O O . VAL A 1 166 ? 51.413 14.397 41.224 1.00 7.07 ? 166 VAL A O 1 ATOM 1253 C CB . VAL A 1 166 ? 52.894 11.770 42.732 1.00 7.47 ? 166 VAL A CB 1 ATOM 1254 C CG1 . VAL A 1 166 ? 53.912 12.285 41.700 1.00 8.80 ? 166 VAL A CG1 1 ATOM 1255 C CG2 . VAL A 1 166 ? 53.605 11.383 44.039 1.00 8.30 ? 166 VAL A CG2 1 ATOM 1256 N N . VAL A 1 167 ? 50.388 12.397 41.069 1.00 6.77 ? 167 VAL A N 1 ATOM 1257 C CA . VAL A 1 167 ? 49.757 12.788 39.789 1.00 6.56 ? 167 VAL A CA 1 ATOM 1258 C C . VAL A 1 167 ? 48.792 13.947 40.012 1.00 6.22 ? 167 VAL A C 1 ATOM 1259 O O . VAL A 1 167 ? 48.717 14.848 39.163 1.00 6.87 ? 167 VAL A O 1 ATOM 1260 C CB . VAL A 1 167 ? 49.110 11.586 39.116 1.00 7.09 ? 167 VAL A CB 1 ATOM 1261 C CG1 . VAL A 1 167 ? 48.429 12.011 37.806 1.00 8.24 ? 167 VAL A CG1 1 ATOM 1262 C CG2 . VAL A 1 167 ? 50.125 10.487 38.819 1.00 9.08 ? 167 VAL A CG2 1 ATOM 1263 N N . SER A 1 168 ? 48.059 13.933 41.138 1.00 6.24 ? 168 SER A N 1 ATOM 1264 C CA . SER A 1 168 ? 47.183 15.049 41.476 1.00 6.17 ? 168 SER A CA 1 ATOM 1265 C C . SER A 1 168 ? 47.934 16.383 41.492 1.00 6.07 ? 168 SER A C 1 ATOM 1266 O O . SER A 1 168 ? 47.457 17.399 41.004 1.00 6.73 ? 168 SER A O 1 ATOM 1267 C CB . SER A 1 168 ? 46.526 14.845 42.852 1.00 6.84 ? 168 SER A CB 1 ATOM 1268 O OG . SER A 1 168 ? 45.645 13.709 42.911 1.00 7.20 ? 168 SER A OG 1 ATOM 1269 N N . LEU A 1 169 ? 49.144 16.382 42.111 1.00 6.38 ? 169 LEU A N 1 ATOM 1270 C CA . LEU A 1 169 ? 49.935 17.603 42.194 1.00 6.28 ? 169 LEU A CA 1 ATOM 1271 C C . LEU A 1 169 ? 50.394 18.091 40.806 1.00 6.27 ? 169 LEU A C 1 ATOM 1272 O O . LEU A 1 169 ? 50.572 19.297 40.615 1.00 7.43 ? 169 LEU A O 1 ATOM 1273 C CB . LEU A 1 169 ? 51.146 17.365 43.079 1.00 6.78 ? 169 LEU A CB 1 ATOM 1274 C CG . LEU A 1 169 ? 50.838 17.306 44.577 1.00 7.03 ? 169 LEU A CG 1 ATOM 1275 C CD1 . LEU A 1 169 ? 52.088 16.820 45.313 1.00 9.35 ? 169 LEU A CD1 1 ATOM 1276 C CD2 . LEU A 1 169 ? 50.385 18.634 45.137 1.00 8.34 ? 169 LEU A CD2 1 ATOM 1277 N N . LEU A 1 170 ? 50.553 17.175 39.851 1.00 6.77 ? 170 LEU A N 1 ATOM 1278 C CA . LEU A 1 170 ? 50.939 17.523 38.462 1.00 7.14 ? 170 LEU A CA 1 ATOM 1279 C C . LEU A 1 170 ? 49.788 18.153 37.706 1.00 7.06 ? 170 LEU A C 1 ATOM 1280 O O . LEU A 1 170 ? 50.049 18.631 36.573 1.00 7.54 ? 170 LEU A O 1 ATOM 1281 C CB . LEU A 1 170 ? 51.554 16.332 37.751 1.00 7.79 ? 170 LEU A CB 1 ATOM 1282 C CG . LEU A 1 170 ? 52.996 16.080 38.099 1.00 9.02 ? 170 LEU A CG 1 ATOM 1283 C CD1 . LEU A 1 170 ? 53.435 14.719 37.614 1.00 11.45 ? 170 LEU A CD1 1 ATOM 1284 C CD2 . LEU A 1 170 ? 53.941 17.134 37.523 1.00 10.01 ? 170 LEU A CD2 1 ATOM 1285 N N . ALA A 1 171 ? 48.602 18.324 38.277 1.00 6.94 ? 171 ALA A N 1 ATOM 1286 C CA . ALA A 1 171 ? 47.631 19.211 37.698 1.00 7.16 ? 171 ALA A CA 1 ATOM 1287 C C . ALA A 1 171 ? 48.201 20.632 37.539 1.00 6.39 ? 171 ALA A C 1 ATOM 1288 O O . ALA A 1 171 ? 47.761 21.394 36.685 1.00 6.83 ? 171 ALA A O 1 ATOM 1289 C CB . ALA A 1 171 ? 46.341 19.255 38.518 1.00 7.71 ? 171 ALA A CB 1 ATOM 1290 N N . SER A 1 172 ? 49.186 20.993 38.382 1.00 6.47 ? 172 SER A N 1 ATOM 1291 C CA . SER A 1 172 ? 49.876 22.268 38.212 1.00 6.44 ? 172 SER A CA 1 ATOM 1292 C C . SER A 1 172 ? 50.483 22.449 36.805 1.00 5.93 ? 172 SER A C 1 ATOM 1293 O O . SER A 1 172 ? 50.654 23.605 36.387 1.00 6.38 ? 172 SER A O 1 ATOM 1294 C CB . SER A 1 172 ? 51.013 22.359 39.237 1.00 7.77 ? 172 SER A CB 1 ATOM 1295 O OG . SER A 1 172 ? 51.942 21.256 38.963 1.00 9.84 ? 172 SER A OG 1 ATOM 1296 N N . HIS A 1 173 ? 50.821 21.354 36.117 1.00 5.73 ? 173 HIS A N 1 ATOM 1297 C CA . HIS A 1 173 ? 51.382 21.494 34.759 1.00 5.77 ? 173 HIS A CA 1 ATOM 1298 C C . HIS A 1 173 ? 50.327 21.902 33.742 1.00 5.86 ? 173 HIS A C 1 ATOM 1299 O O . HIS A 1 173 ? 50.675 22.214 32.593 1.00 7.03 ? 173 HIS A O 1 ATOM 1300 C CB . HIS A 1 173 ? 52.161 20.243 34.347 1.00 6.07 ? 173 HIS A CB 1 ATOM 1301 C CG . HIS A 1 173 ? 53.494 20.189 34.989 1.00 6.05 ? 173 HIS A CG 1 ATOM 1302 N ND1 . HIS A 1 173 ? 54.481 19.281 34.614 1.00 6.42 ? 173 HIS A ND1 1 ATOM 1303 C CD2 . HIS A 1 173 ? 54.062 20.954 35.967 1.00 6.42 ? 173 HIS A CD2 1 ATOM 1304 C CE1 . HIS A 1 173 ? 55.577 19.528 35.379 1.00 6.63 ? 173 HIS A CE1 1 ATOM 1305 N NE2 . HIS A 1 173 ? 55.385 20.529 36.208 1.00 6.28 ? 173 HIS A NE2 1 ATOM 1306 N N . SER A 1 174 ? 49.067 22.038 34.180 1.00 5.99 ? 174 SER A N 1 ATOM 1307 C CA . SER A 1 174 ? 48.026 22.691 33.380 1.00 5.80 ? 174 SER A CA 1 ATOM 1308 C C . SER A 1 174 ? 48.231 24.202 33.258 1.00 5.85 ? 174 SER A C 1 ATOM 1309 O O . SER A 1 174 ? 47.624 24.830 32.374 1.00 6.52 ? 174 SER A O 1 ATOM 1310 C CB . SER A 1 174 ? 46.663 22.403 33.984 1.00 6.33 ? 174 SER A CB 1 ATOM 1311 O OG . SER A 1 174 ? 45.638 22.861 33.103 1.00 6.40 ? 174 SER A OG 1 ATOM 1312 N N . VAL A 1 175 ? 49.040 24.798 34.131 1.00 5.73 ? 175 VAL A N 1 ATOM 1313 C CA . VAL A 1 175 ? 49.308 26.234 34.142 1.00 6.41 ? 175 VAL A CA 1 ATOM 1314 C C . VAL A 1 175 ? 50.807 26.468 34.220 1.00 6.47 ? 175 VAL A C 1 ATOM 1315 O O . VAL A 1 175 ? 51.313 27.094 35.187 1.00 8.76 ? 175 VAL A O 1 ATOM 1316 C CB . VAL A 1 175 ? 48.516 26.944 35.260 1.00 6.97 ? 175 VAL A CB 1 ATOM 1317 C CG1 . VAL A 1 175 ? 47.034 26.948 34.990 1.00 7.51 ? 175 VAL A CG1 1 ATOM 1318 C CG2 . VAL A 1 175 ? 48.770 26.366 36.659 1.00 8.48 ? 175 VAL A CG2 1 ATOM 1319 N N . ALA A 1 176 ? 51.546 25.913 33.283 1.00 7.65 ? 176 ALA A N 1 ATOM 1320 C CA . ALA A 1 176 ? 52.995 25.813 33.420 1.00 6.45 ? 176 ALA A CA 1 ATOM 1321 C C . ALA A 1 176 ? 53.694 25.859 32.063 1.00 6.09 ? 176 ALA A C 1 ATOM 1322 O O . ALA A 1 176 ? 53.225 25.317 31.064 1.00 6.74 ? 176 ALA A O 1 ATOM 1323 C CB . ALA A 1 176 ? 53.408 24.493 34.092 1.00 7.53 ? 176 ALA A CB 1 ATOM 1324 N N . ARG A 1 177 ? 54.865 26.523 32.077 1.00 6.06 ? 177 ARG A N 1 ATOM 1325 C CA . ARG A 1 177 ? 55.713 26.660 30.883 1.00 6.24 ? 177 ARG A CA 1 ATOM 1326 C C . ARG A 1 177 ? 57.176 26.479 31.275 1.00 6.52 ? 177 ARG A C 1 ATOM 1327 O O . ARG A 1 177 ? 57.512 26.566 32.473 1.00 7.43 ? 177 ARG A O 1 ATOM 1328 C CB . ARG A 1 177 ? 55.476 28.023 30.201 1.00 6.89 ? 177 ARG A CB 1 ATOM 1329 C CG . ARG A 1 177 ? 54.014 28.380 30.066 1.00 6.70 ? 177 ARG A CG 1 ATOM 1330 C CD . ARG A 1 177 ? 53.736 29.589 29.177 1.00 7.16 ? 177 ARG A CD 1 ATOM 1331 N NE . ARG A 1 177 ? 54.210 30.811 29.855 1.00 7.64 ? 177 ARG A NE 1 ATOM 1332 C CZ . ARG A 1 177 ? 53.986 32.036 29.389 1.00 7.25 ? 177 ARG A CZ 1 ATOM 1333 N NH1 . ARG A 1 177 ? 53.370 32.207 28.245 1.00 8.20 ? 177 ARG A NH1 1 ATOM 1334 N NH2 . ARG A 1 177 ? 54.415 33.076 30.089 1.00 9.04 ? 177 ARG A NH2 1 ATOM 1335 N N . ALA A 1 178 ? 58.037 26.238 30.262 1.00 6.50 ? 178 ALA A N 1 ATOM 1336 C CA . ALA A 1 178 ? 59.462 25.986 30.484 1.00 6.67 ? 178 ALA A CA 1 ATOM 1337 C C . ALA A 1 178 ? 60.340 27.050 29.808 1.00 7.29 ? 178 ALA A C 1 ATOM 1338 O O . ALA A 1 178 ? 60.202 27.299 28.590 1.00 7.69 ? 178 ALA A O 1 ATOM 1339 C CB . ALA A 1 178 ? 59.873 24.637 29.957 1.00 7.69 ? 178 ALA A CB 1 ATOM 1340 N N . ASP A 1 179 ? 61.274 27.596 30.569 1.00 7.66 ? 179 ASP A N 1 ATOM 1341 C CA . ASP A 1 179 ? 62.251 28.586 30.118 1.00 9.08 ? 179 ASP A CA 1 ATOM 1342 C C . ASP A 1 179 ? 63.661 28.029 29.989 1.00 9.51 ? 179 ASP A C 1 ATOM 1343 O O . ASP A 1 179 ? 64.477 28.625 29.259 1.00 13.88 ? 179 ASP A O 1 ATOM 1344 C CB . ASP A 1 179 ? 62.259 29.777 31.086 1.00 10.56 ? 179 ASP A CB 1 ATOM 1345 C CG . ASP A 1 179 ? 60.853 30.434 31.342 1.00 11.32 ? 179 ASP A CG 1 ATOM 1346 O OD1 . ASP A 1 179 ? 60.095 30.490 30.346 1.00 11.58 ? 179 ASP A OD1 1 ATOM 1347 O OD2 . ASP A 1 179 ? 60.546 30.851 32.557 1.00 13.41 ? 179 ASP A OD2 1 ATOM 1348 N N . LYS A 1 180 ? 63.999 26.991 30.737 1.00 9.00 ? 180 LYS A N 1 ATOM 1349 C CA . LYS A 1 180 ? 65.385 26.525 30.833 1.00 9.93 ? 180 LYS A CA 1 ATOM 1350 C C . LYS A 1 180 ? 65.624 25.171 30.187 1.00 10.07 ? 180 LYS A C 1 ATOM 1351 O O . LYS A 1 180 ? 66.801 24.823 29.895 1.00 12.55 ? 180 LYS A O 1 ATOM 1352 C CB . LYS A 1 180 ? 65.831 26.410 32.325 1.00 11.11 ? 180 LYS A CB 1 ATOM 1353 C CG . LYS A 1 180 ? 65.674 27.633 33.127 1.00 12.03 ? 180 LYS A CG 1 ATOM 1354 C CD . LYS A 1 180 ? 66.384 28.821 32.575 1.00 14.44 ? 180 LYS A CD 1 ATOM 1355 C CE . LYS A 1 180 ? 66.295 29.999 33.526 1.00 21.14 ? 180 LYS A CE 1 ATOM 1356 N NZ . LYS A 1 180 ? 67.244 31.045 33.018 1.00 38.37 ? 180 LYS A NZ 1 ATOM 1357 N N . VAL A 1 181 ? 64.603 24.365 29.903 1.00 9.34 ? 181 VAL A N 1 ATOM 1358 C CA . VAL A 1 181 ? 64.787 23.048 29.336 1.00 9.49 ? 181 VAL A CA 1 ATOM 1359 C C . VAL A 1 181 ? 65.460 23.169 27.971 1.00 10.02 ? 181 VAL A C 1 ATOM 1360 O O . VAL A 1 181 ? 66.395 22.384 27.656 1.00 11.24 ? 181 VAL A O 1 ATOM 1361 C CB . VAL A 1 181 ? 63.480 22.308 29.242 1.00 9.50 ? 181 VAL A CB 1 ATOM 1362 C CG1 . VAL A 1 181 ? 63.656 20.968 28.483 1.00 11.10 ? 181 VAL A CG1 1 ATOM 1363 C CG2 . VAL A 1 181 ? 62.838 22.045 30.629 1.00 10.30 ? 181 VAL A CG2 1 ATOM 1364 N N . ASP A 1 182 ? 65.020 24.097 27.160 1.00 10.51 ? 182 ASP A N 1 ATOM 1365 C CA . ASP A 1 182 ? 65.600 24.387 25.856 1.00 11.51 ? 182 ASP A CA 1 ATOM 1366 C C . ASP A 1 182 ? 66.172 25.766 25.865 1.00 13.45 ? 182 ASP A C 1 ATOM 1367 O O . ASP A 1 182 ? 65.378 26.652 26.076 1.00 25.05 ? 182 ASP A O 1 ATOM 1368 C CB A ASP A 1 182 ? 64.487 24.122 24.828 0.52 14.71 ? 182 ASP A CB 1 ATOM 1369 C CB B ASP A 1 182 ? 64.570 24.353 24.716 0.52 15.44 ? 182 ASP A CB 1 ATOM 1370 C CG A ASP A 1 182 ? 64.977 24.204 23.393 0.52 10.74 ? 182 ASP A CG 1 ATOM 1371 C CG B ASP A 1 182 ? 65.189 24.693 23.373 0.52 15.07 ? 182 ASP A CG 1 ATOM 1372 O OD1 A ASP A 1 182 ? 66.113 24.725 23.194 0.52 13.53 ? 182 ASP A OD1 1 ATOM 1373 O OD1 B ASP A 1 182 ? 65.582 25.816 23.006 0.52 16.14 ? 182 ASP A OD1 1 ATOM 1374 O OD2 A ASP A 1 182 ? 64.248 23.757 22.493 0.52 8.85 ? 182 ASP A OD2 1 ATOM 1375 O OD2 B ASP A 1 182 ? 65.318 23.785 22.552 0.52 20.24 ? 182 ASP A OD2 1 ATOM 1376 N N . GLN A 1 183 ? 67.456 25.896 25.593 1.00 18.04 ? 183 GLN A N 1 ATOM 1377 C CA . GLN A 1 183 ? 68.137 27.213 25.705 1.00 24.89 ? 183 GLN A CA 1 ATOM 1378 C C . GLN A 1 183 ? 67.773 28.182 24.593 1.00 18.13 ? 183 GLN A C 1 ATOM 1379 O O . GLN A 1 183 ? 68.030 29.387 24.656 1.00 27.16 ? 183 GLN A O 1 ATOM 1380 C CB . GLN A 1 183 ? 69.636 26.969 25.801 1.00 31.82 ? 183 GLN A CB 1 ATOM 1381 C CG . GLN A 1 183 ? 70.267 25.882 24.986 1.00 45.73 ? 183 GLN A CG 1 ATOM 1382 C CD . GLN A 1 183 ? 70.440 24.514 25.587 1.00 50.12 ? 183 GLN A CD 1 ATOM 1383 O OE1 . GLN A 1 183 ? 69.436 23.828 25.896 1.00 72.34 ? 183 GLN A OE1 1 ATOM 1384 N NE2 . GLN A 1 183 ? 71.669 24.012 25.765 1.00 62.36 ? 183 GLN A NE2 1 ATOM 1385 N N . THR A 1 184 ? 67.113 27.696 23.557 1.00 16.19 ? 184 THR A N 1 ATOM 1386 C CA . THR A 1 184 ? 66.773 28.441 22.372 1.00 17.20 ? 184 THR A CA 1 ATOM 1387 C C . THR A 1 184 ? 65.386 29.064 22.362 1.00 17.03 ? 184 THR A C 1 ATOM 1388 O O . THR A 1 184 ? 65.099 29.889 21.448 1.00 20.66 ? 184 THR A O 1 ATOM 1389 C CB . THR A 1 184 ? 66.890 27.622 21.040 1.00 18.60 ? 184 THR A CB 1 ATOM 1390 O OG1 . THR A 1 184 ? 65.860 26.588 20.907 1.00 20.36 ? 184 THR A OG1 1 ATOM 1391 C CG2 . THR A 1 184 ? 68.265 27.009 20.976 1.00 29.62 ? 184 THR A CG2 1 ATOM 1392 N N . ILE A 1 185 ? 64.525 28.684 23.246 1.00 11.82 ? 185 ILE A N 1 ATOM 1393 C CA . ILE A 1 185 ? 63.152 29.163 23.352 1.00 11.34 ? 185 ILE A CA 1 ATOM 1394 C C . ILE A 1 185 ? 62.785 29.442 24.802 1.00 10.85 ? 185 ILE A C 1 ATOM 1395 O O . ILE A 1 185 ? 63.340 28.832 25.719 1.00 13.08 ? 185 ILE A O 1 ATOM 1396 C CB . ILE A 1 185 ? 62.140 28.148 22.694 1.00 10.97 ? 185 ILE A CB 1 ATOM 1397 C CG1 . ILE A 1 185 ? 62.178 26.795 23.411 1.00 12.07 ? 185 ILE A CG1 1 ATOM 1398 C CG2 . ILE A 1 185 ? 62.365 28.037 21.211 1.00 15.71 ? 185 ILE A CG2 1 ATOM 1399 C CD1 . ILE A 1 185 ? 61.207 25.734 22.998 1.00 11.41 ? 185 ILE A CD1 1 ATOM 1400 N N . ASP A 1 186 ? 61.819 30.319 25.011 1.00 11.89 ? 186 ASP A N 1 ATOM 1401 C CA . ASP A 1 186 ? 61.325 30.595 26.350 1.00 15.22 ? 186 ASP A CA 1 ATOM 1402 C C . ASP A 1 186 ? 59.815 30.394 26.413 1.00 9.33 ? 186 ASP A C 1 ATOM 1403 O O . ASP A 1 186 ? 59.099 30.418 25.406 1.00 10.63 ? 186 ASP A O 1 ATOM 1404 C CB . ASP A 1 186 ? 61.722 31.997 26.814 1.00 31.23 ? 186 ASP A CB 1 ATOM 1405 C CG . ASP A 1 186 ? 60.628 32.914 26.354 1.00 40.84 ? 186 ASP A CG 1 ATOM 1406 O OD1 . ASP A 1 186 ? 60.267 32.844 25.156 1.00 80.70 ? 186 ASP A OD1 1 ATOM 1407 O OD2 . ASP A 1 186 ? 60.133 33.668 27.229 1.00 78.41 ? 186 ASP A OD2 1 ATOM 1408 N N . ALA A 1 187 ? 59.340 30.149 27.616 1.00 8.54 ? 187 ALA A N 1 ATOM 1409 C CA . ALA A 1 187 ? 57.909 30.074 27.872 1.00 8.21 ? 187 ALA A CA 1 ATOM 1410 C C . ALA A 1 187 ? 57.217 29.023 26.986 1.00 7.19 ? 187 ALA A C 1 ATOM 1411 O O . ALA A 1 187 ? 56.128 29.275 26.451 1.00 7.76 ? 187 ALA A O 1 ATOM 1412 C CB . ALA A 1 187 ? 57.290 31.422 27.787 1.00 9.64 ? 187 ALA A CB 1 ATOM 1413 N N . ALA A 1 188 ? 57.766 27.814 26.931 1.00 6.93 ? 188 ALA A N 1 ATOM 1414 C CA . ALA A 1 188 ? 57.180 26.730 26.165 1.00 6.70 ? 188 ALA A CA 1 ATOM 1415 C C . ALA A 1 188 ? 56.101 26.038 27.050 1.00 6.28 ? 188 ALA A C 1 ATOM 1416 O O . ALA A 1 188 ? 56.466 25.415 28.072 1.00 6.45 ? 188 ALA A O 1 ATOM 1417 C CB . ALA A 1 188 ? 58.248 25.721 25.760 1.00 7.47 ? 188 ALA A CB 1 ATOM 1418 N N . PRO A 1 189 ? 54.820 26.138 26.709 1.00 6.30 ? 189 PRO A N 1 ATOM 1419 C CA . PRO A 1 189 ? 53.776 25.642 27.629 1.00 6.23 ? 189 PRO A CA 1 ATOM 1420 C C . PRO A 1 189 ? 53.655 24.129 27.613 1.00 5.87 ? 189 PRO A C 1 ATOM 1421 O O . PRO A 1 189 ? 53.896 23.463 26.592 1.00 6.58 ? 189 PRO A O 1 ATOM 1422 C CB . PRO A 1 189 ? 52.499 26.317 27.076 1.00 6.68 ? 189 PRO A CB 1 ATOM 1423 C CG . PRO A 1 189 ? 52.780 26.435 25.597 1.00 7.04 ? 189 PRO A CG 1 ATOM 1424 C CD . PRO A 1 189 ? 54.262 26.802 25.516 1.00 6.89 ? 189 PRO A CD 1 ATOM 1425 N N . PHE A 1 190 ? 53.176 23.564 28.743 1.00 5.93 ? 190 PHE A N 1 ATOM 1426 C CA . PHE A 1 190 ? 52.961 22.119 28.833 1.00 5.84 ? 190 PHE A CA 1 ATOM 1427 C C . PHE A 1 190 ? 51.567 21.693 28.384 1.00 5.92 ? 190 PHE A C 1 ATOM 1428 O O . PHE A 1 190 ? 51.342 20.507 28.117 1.00 7.01 ? 190 PHE A O 1 ATOM 1429 C CB . PHE A 1 190 ? 53.255 21.596 30.241 1.00 6.33 ? 190 PHE A CB 1 ATOM 1430 C CG . PHE A 1 190 ? 54.663 21.825 30.703 1.00 6.16 ? 190 PHE A CG 1 ATOM 1431 C CD1 . PHE A 1 190 ? 55.742 21.937 29.839 1.00 7.26 ? 190 PHE A CD1 1 ATOM 1432 C CD2 . PHE A 1 190 ? 54.918 21.920 32.076 1.00 7.27 ? 190 PHE A CD2 1 ATOM 1433 C CE1 . PHE A 1 190 ? 57.053 22.140 30.311 1.00 8.21 ? 190 PHE A CE1 1 ATOM 1434 C CE2 . PHE A 1 190 ? 56.207 22.106 32.550 1.00 7.95 ? 190 PHE A CE2 1 ATOM 1435 C CZ . PHE A 1 190 ? 57.267 22.239 31.679 1.00 8.17 ? 190 PHE A CZ 1 ATOM 1436 N N . ASP A 1 191 ? 50.627 22.633 28.268 1.00 6.01 ? 191 ASP A N 1 ATOM 1437 C CA . ASP A 1 191 ? 49.367 22.351 27.586 1.00 6.04 ? 191 ASP A CA 1 ATOM 1438 C C . ASP A 1 191 ? 48.993 23.584 26.774 1.00 6.16 ? 191 ASP A C 1 ATOM 1439 O O . ASP A 1 191 ? 49.615 24.642 26.839 1.00 6.94 ? 191 ASP A O 1 ATOM 1440 C CB . ASP A 1 191 ? 48.271 21.802 28.499 1.00 6.16 ? 191 ASP A CB 1 ATOM 1441 C CG . ASP A 1 191 ? 47.499 22.758 29.409 1.00 5.83 ? 191 ASP A CG 1 ATOM 1442 O OD1 . ASP A 1 191 ? 47.646 23.987 29.291 1.00 6.52 ? 191 ASP A OD1 1 ATOM 1443 O OD2 . ASP A 1 191 ? 46.685 22.231 30.255 1.00 6.40 ? 191 ASP A OD2 1 ATOM 1444 N N . SER A 1 192 ? 47.917 23.414 25.992 1.00 6.24 ? 192 SER A N 1 ATOM 1445 C CA . SER A 1 192 ? 47.472 24.453 25.076 1.00 6.69 ? 192 SER A CA 1 ATOM 1446 C C . SER A 1 192 ? 46.691 25.590 25.759 1.00 6.70 ? 192 SER A C 1 ATOM 1447 O O . SER A 1 192 ? 46.303 26.528 25.091 1.00 7.88 ? 192 SER A O 1 ATOM 1448 C CB . SER A 1 192 ? 46.639 23.855 23.957 1.00 7.52 ? 192 SER A CB 1 ATOM 1449 O OG . SER A 1 192 ? 45.422 23.317 24.447 1.00 8.37 ? 192 SER A OG 1 ATOM 1450 N N . THR A 1 193 ? 46.532 25.477 27.093 1.00 6.56 ? 193 THR A N 1 ATOM 1451 C CA . THR A 1 193 ? 45.784 26.439 27.880 1.00 6.57 ? 193 THR A CA 1 ATOM 1452 C C . THR A 1 193 ? 46.569 26.763 29.160 1.00 6.32 ? 193 THR A C 1 ATOM 1453 O O . THR A 1 193 ? 46.092 26.508 30.295 1.00 6.43 ? 193 THR A O 1 ATOM 1454 C CB . THR A 1 193 ? 44.370 25.933 28.224 1.00 7.16 ? 193 THR A CB 1 ATOM 1455 O OG1 . THR A 1 193 ? 44.492 24.682 28.950 1.00 6.88 ? 193 THR A OG1 1 ATOM 1456 C CG2 . THR A 1 193 ? 43.538 25.702 26.979 1.00 8.15 ? 193 THR A CG2 1 ATOM 1457 N N . PRO A 1 194 ? 47.747 27.379 29.010 1.00 6.46 ? 194 PRO A N 1 ATOM 1458 C CA . PRO A 1 194 ? 48.625 27.583 30.200 1.00 6.53 ? 194 PRO A CA 1 ATOM 1459 C C . PRO A 1 194 ? 48.119 28.656 31.177 1.00 6.66 ? 194 PRO A C 1 ATOM 1460 O O . PRO A 1 194 ? 48.745 28.815 32.223 1.00 7.36 ? 194 PRO A O 1 ATOM 1461 C CB . PRO A 1 194 ? 49.947 27.950 29.557 1.00 7.56 ? 194 PRO A CB 1 ATOM 1462 C CG . PRO A 1 194 ? 49.574 28.651 28.274 1.00 7.73 ? 194 PRO A CG 1 ATOM 1463 C CD . PRO A 1 194 ? 48.426 27.810 27.762 1.00 7.08 ? 194 PRO A CD 1 ATOM 1464 N N . PHE A 1 195 ? 47.025 29.337 30.858 1.00 6.61 ? 195 PHE A N 1 ATOM 1465 C CA . PHE A 1 195 ? 46.422 30.331 31.752 1.00 6.97 ? 195 PHE A CA 1 ATOM 1466 C C . PHE A 1 195 ? 45.115 29.809 32.363 1.00 7.68 ? 195 PHE A C 1 ATOM 1467 O O . PHE A 1 195 ? 44.398 30.582 33.032 1.00 9.56 ? 195 PHE A O 1 ATOM 1468 C CB . PHE A 1 195 ? 46.256 31.673 31.062 1.00 7.98 ? 195 PHE A CB 1 ATOM 1469 C CG . PHE A 1 195 ? 47.492 32.080 30.279 1.00 8.21 ? 195 PHE A CG 1 ATOM 1470 C CD1 . PHE A 1 195 ? 48.695 32.305 30.900 1.00 10.46 ? 195 PHE A CD1 1 ATOM 1471 C CD2 . PHE A 1 195 ? 47.495 32.173 28.907 1.00 10.93 ? 195 PHE A CD2 1 ATOM 1472 C CE1 . PHE A 1 195 ? 49.852 32.630 30.158 1.00 14.51 ? 195 PHE A CE1 1 ATOM 1473 C CE2 . PHE A 1 195 ? 48.594 32.512 28.171 1.00 14.56 ? 195 PHE A CE2 1 ATOM 1474 C CZ . PHE A 1 195 ? 49.780 32.768 28.786 1.00 14.73 ? 195 PHE A CZ 1 ATOM 1475 N N . THR A 1 196 ? 44.804 28.510 32.160 1.00 6.91 ? 196 THR A N 1 ATOM 1476 C CA . THR A 1 196 ? 43.534 27.914 32.598 1.00 7.34 ? 196 THR A CA 1 ATOM 1477 C C . THR A 1 196 ? 43.828 26.636 33.327 1.00 6.54 ? 196 THR A C 1 ATOM 1478 O O . THR A 1 196 ? 44.502 25.740 32.764 1.00 7.04 ? 196 THR A O 1 ATOM 1479 C CB . THR A 1 196 ? 42.603 27.601 31.383 1.00 9.34 ? 196 THR A CB 1 ATOM 1480 O OG1 . THR A 1 196 ? 42.559 28.709 30.514 1.00 12.68 ? 196 THR A OG1 1 ATOM 1481 C CG2 . THR A 1 196 ? 41.255 27.107 31.883 1.00 9.60 ? 196 THR A CG2 1 ATOM 1482 N N . PHE A 1 197 ? 43.325 26.480 34.561 1.00 6.83 ? 197 PHE A N 1 ATOM 1483 C CA . PHE A 1 197 ? 43.528 25.287 35.372 1.00 6.44 ? 197 PHE A CA 1 ATOM 1484 C C . PHE A 1 197 ? 42.442 24.259 35.049 1.00 6.77 ? 197 PHE A C 1 ATOM 1485 O O . PHE A 1 197 ? 41.474 24.030 35.767 1.00 9.39 ? 197 PHE A O 1 ATOM 1486 C CB . PHE A 1 197 ? 43.479 25.657 36.876 1.00 7.13 ? 197 PHE A CB 1 ATOM 1487 C CG . PHE A 1 197 ? 44.092 24.611 37.782 1.00 7.86 ? 197 PHE A CG 1 ATOM 1488 C CD1 . PHE A 1 197 ? 43.361 23.626 38.366 1.00 10.28 ? 197 PHE A CD1 1 ATOM 1489 C CD2 . PHE A 1 197 ? 45.448 24.683 38.043 1.00 10.55 ? 197 PHE A CD2 1 ATOM 1490 C CE1 . PHE A 1 197 ? 44.004 22.710 39.230 1.00 13.15 ? 197 PHE A CE1 1 ATOM 1491 C CE2 . PHE A 1 197 ? 46.073 23.796 38.890 1.00 14.60 ? 197 PHE A CE2 1 ATOM 1492 C CZ . PHE A 1 197 ? 45.342 22.800 39.477 1.00 14.13 ? 197 PHE A CZ 1 ATOM 1493 N N . ASP A 1 198 ? 42.667 23.634 33.891 1.00 7.83 ? 198 ASP A N 1 ATOM 1494 C CA . ASP A 1 198 ? 41.765 22.641 33.269 1.00 7.19 ? 198 ASP A CA 1 ATOM 1495 C C . ASP A 1 198 ? 42.480 21.325 33.109 1.00 6.55 ? 198 ASP A C 1 ATOM 1496 O O . ASP A 1 198 ? 43.636 21.131 33.573 1.00 6.94 ? 198 ASP A O 1 ATOM 1497 C CB . ASP A 1 198 ? 41.255 23.201 31.936 1.00 7.27 ? 198 ASP A CB 1 ATOM 1498 C CG . ASP A 1 198 ? 42.357 23.519 30.923 1.00 7.06 ? 198 ASP A CG 1 ATOM 1499 O OD1 . ASP A 1 198 ? 43.539 23.144 31.194 1.00 6.89 ? 198 ASP A OD1 1 ATOM 1500 O OD2 . ASP A 1 198 ? 42.065 24.153 29.890 1.00 8.24 ? 198 ASP A OD2 1 ATOM 1501 N N . THR A 1 199 ? 41.849 20.362 32.464 1.00 6.75 ? 199 THR A N 1 ATOM 1502 C CA . THR A 1 199 ? 42.406 19.011 32.331 1.00 6.86 ? 199 THR A CA 1 ATOM 1503 C C . THR A 1 199 ? 43.179 18.790 31.028 1.00 6.49 ? 199 THR A C 1 ATOM 1504 O O . THR A 1 199 ? 43.573 17.660 30.728 1.00 7.33 ? 199 THR A O 1 ATOM 1505 C CB . THR A 1 199 ? 41.332 17.933 32.547 1.00 6.96 ? 199 THR A CB 1 ATOM 1506 O OG1 . THR A 1 199 ? 40.483 17.816 31.378 1.00 7.65 ? 199 THR A OG1 1 ATOM 1507 C CG2 . THR A 1 199 ? 40.483 18.167 33.791 1.00 7.61 ? 199 THR A CG2 1 ATOM 1508 N N . GLN A 1 200 ? 43.439 19.872 30.252 1.00 6.75 ? 200 GLN A N 1 ATOM 1509 C CA . GLN A 1 200 ? 44.073 19.711 28.960 1.00 6.62 ? 200 GLN A CA 1 ATOM 1510 C C . GLN A 1 200 ? 45.423 19.023 29.056 1.00 6.55 ? 200 GLN A C 1 ATOM 1511 O O . GLN A 1 200 ? 45.740 18.194 28.165 1.00 7.04 ? 200 GLN A O 1 ATOM 1512 C CB . GLN A 1 200 ? 44.203 21.031 28.194 1.00 7.03 ? 200 GLN A CB 1 ATOM 1513 C CG . GLN A 1 200 ? 42.866 21.604 27.710 1.00 7.52 ? 200 GLN A CG 1 ATOM 1514 C CD . GLN A 1 200 ? 42.095 20.751 26.713 1.00 7.72 ? 200 GLN A CD 1 ATOM 1515 O OE1 . GLN A 1 200 ? 40.853 20.618 26.843 1.00 9.16 ? 200 GLN A OE1 1 ATOM 1516 N NE2 . GLN A 1 200 ? 42.762 20.201 25.718 1.00 8.43 ? 200 GLN A NE2 1 ATOM 1517 N N . VAL A 1 201 ? 46.254 19.305 30.051 1.00 6.36 ? 201 VAL A N 1 ATOM 1518 C CA . VAL A 1 201 ? 47.570 18.660 30.109 1.00 6.25 ? 201 VAL A CA 1 ATOM 1519 C C . VAL A 1 201 ? 47.441 17.147 30.141 1.00 6.39 ? 201 VAL A C 1 ATOM 1520 O O . VAL A 1 201 ? 48.263 16.421 29.559 1.00 6.71 ? 201 VAL A O 1 ATOM 1521 C CB . VAL A 1 201 ? 48.412 19.196 31.285 1.00 6.74 ? 201 VAL A CB 1 ATOM 1522 C CG1 . VAL A 1 201 ? 47.777 18.858 32.650 1.00 7.66 ? 201 VAL A CG1 1 ATOM 1523 C CG2 . VAL A 1 201 ? 49.856 18.728 31.189 1.00 7.77 ? 201 VAL A CG2 1 ATOM 1524 N N . PHE A 1 202 ? 46.442 16.626 30.873 1.00 6.37 ? 202 PHE A N 1 ATOM 1525 C CA . PHE A 1 202 ? 46.291 15.182 30.982 1.00 6.50 ? 202 PHE A CA 1 ATOM 1526 C C . PHE A 1 202 ? 45.972 14.562 29.603 1.00 6.73 ? 202 PHE A C 1 ATOM 1527 O O . PHE A 1 202 ? 46.509 13.515 29.237 1.00 7.37 ? 202 PHE A O 1 ATOM 1528 C CB . PHE A 1 202 ? 45.256 14.799 32.062 1.00 6.89 ? 202 PHE A CB 1 ATOM 1529 C CG . PHE A 1 202 ? 45.758 15.173 33.455 1.00 6.63 ? 202 PHE A CG 1 ATOM 1530 C CD1 . PHE A 1 202 ? 45.319 16.330 34.119 1.00 6.99 ? 202 PHE A CD1 1 ATOM 1531 C CD2 . PHE A 1 202 ? 46.689 14.369 34.070 1.00 7.12 ? 202 PHE A CD2 1 ATOM 1532 C CE1 . PHE A 1 202 ? 45.861 16.681 35.359 1.00 7.62 ? 202 PHE A CE1 1 ATOM 1533 C CE2 . PHE A 1 202 ? 47.236 14.730 35.286 1.00 7.65 ? 202 PHE A CE2 1 ATOM 1534 C CZ . PHE A 1 202 ? 46.807 15.885 35.921 1.00 7.84 ? 202 PHE A CZ 1 ATOM 1535 N N . LEU A 1 203 ? 45.067 15.225 28.878 1.00 6.57 ? 203 LEU A N 1 ATOM 1536 C CA . LEU A 1 203 ? 44.761 14.785 27.523 1.00 6.80 ? 203 LEU A CA 1 ATOM 1537 C C . LEU A 1 203 ? 45.975 14.870 26.595 1.00 6.60 ? 203 LEU A C 1 ATOM 1538 O O . LEU A 1 203 ? 46.281 13.949 25.822 1.00 7.44 ? 203 LEU A O 1 ATOM 1539 C CB A LEU A 1 203 ? 43.576 15.628 27.025 0.52 6.70 ? 203 LEU A CB 1 ATOM 1540 C CB B LEU A 1 203 ? 43.630 15.639 26.931 0.52 8.94 ? 203 LEU A CB 1 ATOM 1541 C CG A LEU A 1 203 ? 43.239 15.438 25.539 0.52 6.73 ? 203 LEU A CG 1 ATOM 1542 C CG B LEU A 1 203 ? 43.115 15.250 25.530 0.52 10.44 ? 203 LEU A CG 1 ATOM 1543 C CD1 A LEU A 1 203 ? 42.777 14.049 25.286 0.52 8.51 ? 203 LEU A CD1 1 ATOM 1544 C CD1 B LEU A 1 203 ? 43.837 15.885 24.362 0.52 15.72 ? 203 LEU A CD1 1 ATOM 1545 C CD2 A LEU A 1 203 ? 42.105 16.397 25.141 0.52 8.90 ? 203 LEU A CD2 1 ATOM 1546 C CD2 B LEU A 1 203 ? 43.196 13.763 25.334 0.52 26.75 ? 203 LEU A CD2 1 ATOM 1547 N N . GLU A 1 204 ? 46.625 16.034 26.593 1.00 6.38 ? 204 GLU A N 1 ATOM 1548 C CA . GLU A 1 204 ? 47.601 16.341 25.542 1.00 6.55 ? 204 GLU A CA 1 ATOM 1549 C C . GLU A 1 204 ? 48.860 15.535 25.688 1.00 6.12 ? 204 GLU A C 1 ATOM 1550 O O . GLU A 1 204 ? 49.492 15.189 24.665 1.00 7.03 ? 204 GLU A O 1 ATOM 1551 C CB . GLU A 1 204 ? 47.851 17.857 25.481 1.00 6.90 ? 204 GLU A CB 1 ATOM 1552 C CG . GLU A 1 204 ? 46.622 18.598 24.972 1.00 7.47 ? 204 GLU A CG 1 ATOM 1553 C CD . GLU A 1 204 ? 46.657 20.104 25.041 1.00 7.20 ? 204 GLU A CD 1 ATOM 1554 O OE1 . GLU A 1 204 ? 47.762 20.689 25.157 1.00 7.50 ? 204 GLU A OE1 1 ATOM 1555 O OE2 . GLU A 1 204 ? 45.554 20.725 25.009 1.00 8.26 ? 204 GLU A OE2 1 ATOM 1556 N N . VAL A 1 205 ? 49.243 15.150 26.899 1.00 6.41 ? 205 VAL A N 1 ATOM 1557 C CA . VAL A 1 205 ? 50.422 14.291 27.073 1.00 6.47 ? 205 VAL A CA 1 ATOM 1558 C C . VAL A 1 205 ? 50.173 12.893 26.468 1.00 6.76 ? 205 VAL A C 1 ATOM 1559 O O . VAL A 1 205 ? 51.156 12.221 26.114 1.00 7.36 ? 205 VAL A O 1 ATOM 1560 C CB . VAL A 1 205 ? 50.816 14.240 28.569 1.00 6.91 ? 205 VAL A CB 1 ATOM 1561 C CG1 . VAL A 1 205 ? 51.845 13.156 28.875 1.00 8.33 ? 205 VAL A CG1 1 ATOM 1562 C CG2 . VAL A 1 205 ? 51.383 15.610 28.964 1.00 7.10 ? 205 VAL A CG2 1 ATOM 1563 N N . LEU A 1 206 ? 48.917 12.463 26.355 1.00 6.63 ? 206 LEU A N 1 ATOM 1564 C CA . LEU A 1 206 ? 48.576 11.160 25.793 1.00 7.23 ? 206 LEU A CA 1 ATOM 1565 C C . LEU A 1 206 ? 48.536 11.136 24.265 1.00 7.72 ? 206 LEU A C 1 ATOM 1566 O O . LEU A 1 206 ? 48.297 10.085 23.677 1.00 10.71 ? 206 LEU A O 1 ATOM 1567 C CB . LEU A 1 206 ? 47.231 10.664 26.357 1.00 7.46 ? 206 LEU A CB 1 ATOM 1568 C CG . LEU A 1 206 ? 47.271 10.235 27.841 1.00 8.60 ? 206 LEU A CG 1 ATOM 1569 C CD1 . LEU A 1 206 ? 45.879 9.970 28.374 1.00 10.02 ? 206 LEU A CD1 1 ATOM 1570 C CD2 . LEU A 1 206 ? 48.166 9.017 27.999 1.00 9.70 ? 206 LEU A CD2 1 ATOM 1571 N N . LEU A 1 207 ? 48.761 12.251 23.595 1.00 6.97 ? 207 LEU A N 1 ATOM 1572 C CA . LEU A 1 207 ? 48.778 12.292 22.133 1.00 7.61 ? 207 LEU A CA 1 ATOM 1573 C C . LEU A 1 207 ? 50.152 11.901 21.590 1.00 7.76 ? 207 LEU A C 1 ATOM 1574 O O . LEU A 1 207 ? 51.206 12.129 22.214 1.00 9.47 ? 207 LEU A O 1 ATOM 1575 C CB . LEU A 1 207 ? 48.424 13.709 21.668 1.00 8.28 ? 207 LEU A CB 1 ATOM 1576 C CG . LEU A 1 207 ? 47.075 14.208 22.067 1.00 9.55 ? 207 LEU A CG 1 ATOM 1577 C CD1 . LEU A 1 207 ? 46.935 15.688 21.749 1.00 11.98 ? 207 LEU A CD1 1 ATOM 1578 C CD2 . LEU A 1 207 ? 45.947 13.416 21.388 1.00 14.89 ? 207 LEU A CD2 1 ATOM 1579 N N . LYS A 1 208 ? 50.219 11.327 20.398 1.00 8.64 ? 208 LYS A N 1 ATOM 1580 C CA . LYS A 1 208 ? 51.521 11.038 19.771 1.00 9.26 ? 208 LYS A CA 1 ATOM 1581 C C . LYS A 1 208 ? 52.304 12.332 19.542 1.00 8.56 ? 208 LYS A C 1 ATOM 1582 O O . LYS A 1 208 ? 51.831 13.308 18.994 1.00 9.75 ? 208 LYS A O 1 ATOM 1583 C CB . LYS A 1 208 ? 51.326 10.315 18.429 1.00 13.98 ? 208 LYS A CB 1 ATOM 1584 C CG . LYS A 1 208 ? 52.596 9.938 17.713 1.00 23.09 ? 208 LYS A CG 1 ATOM 1585 C CD . LYS A 1 208 ? 52.719 10.739 16.446 1.00 38.63 ? 208 LYS A CD 1 ATOM 1586 C CE . LYS A 1 208 ? 51.632 10.344 15.464 1.00 51.11 ? 208 LYS A CE 1 ATOM 1587 N NZ . LYS A 1 208 ? 50.943 11.468 14.740 1.00 57.64 ? 208 LYS A NZ 1 ATOM 1588 N N . GLY A 1 209 ? 53.567 12.327 19.931 1.00 8.70 ? 209 GLY A N 1 ATOM 1589 C CA . GLY A 1 209 ? 54.455 13.438 19.632 1.00 8.46 ? 209 GLY A CA 1 ATOM 1590 C C . GLY A 1 209 ? 54.864 13.478 18.157 1.00 9.24 ? 209 GLY A C 1 ATOM 1591 O O . GLY A 1 209 ? 55.101 12.438 17.547 1.00 12.13 ? 209 GLY A O 1 ATOM 1592 N N . VAL A 1 210 ? 54.940 14.684 17.604 1.00 8.68 ? 210 VAL A N 1 ATOM 1593 C CA . VAL A 1 210 ? 55.208 14.892 16.167 1.00 9.29 ? 210 VAL A CA 1 ATOM 1594 C C . VAL A 1 210 ? 56.373 15.817 15.894 1.00 9.19 ? 210 VAL A C 1 ATOM 1595 O O . VAL A 1 210 ? 56.790 15.958 14.722 1.00 12.00 ? 210 VAL A O 1 ATOM 1596 C CB . VAL A 1 210 ? 53.941 15.373 15.403 1.00 10.52 ? 210 VAL A CB 1 ATOM 1597 C CG1 . VAL A 1 210 ? 52.864 14.289 15.536 1.00 13.19 ? 210 VAL A CG1 1 ATOM 1598 C CG2 . VAL A 1 210 ? 53.537 16.777 15.804 1.00 11.43 ? 210 VAL A CG2 1 ATOM 1599 N N . GLY A 1 211 ? 56.946 16.505 16.890 1.00 8.92 ? 211 GLY A N 1 ATOM 1600 C CA . GLY A 1 211 ? 58.093 17.344 16.681 1.00 9.13 ? 211 GLY A CA 1 ATOM 1601 C C . GLY A 1 211 ? 58.458 18.016 17.984 1.00 8.42 ? 211 GLY A C 1 ATOM 1602 O O . GLY A 1 211 ? 58.000 17.573 19.057 1.00 9.77 ? 211 GLY A O 1 ATOM 1603 N N . PHE A 1 212 ? 59.302 19.040 17.912 1.00 9.08 ? 212 PHE A N 1 ATOM 1604 C CA . PHE A 1 212 ? 59.810 19.711 19.111 1.00 8.96 ? 212 PHE A CA 1 ATOM 1605 C C . PHE A 1 212 ? 59.613 21.208 18.938 1.00 8.45 ? 212 PHE A C 1 ATOM 1606 O O . PHE A 1 212 ? 59.770 21.731 17.818 1.00 9.68 ? 212 PHE A O 1 ATOM 1607 C CB . PHE A 1 212 ? 61.294 19.449 19.326 1.00 9.94 ? 212 PHE A CB 1 ATOM 1608 C CG . PHE A 1 212 ? 61.573 17.983 19.657 1.00 10.23 ? 212 PHE A CG 1 ATOM 1609 C CD1 . PHE A 1 212 ? 61.729 17.052 18.651 1.00 12.58 ? 212 PHE A CD1 1 ATOM 1610 C CD2 . PHE A 1 212 ? 61.668 17.558 20.984 1.00 10.64 ? 212 PHE A CD2 1 ATOM 1611 C CE1 . PHE A 1 212 ? 61.970 15.721 19.012 1.00 14.86 ? 212 PHE A CE1 1 ATOM 1612 C CE2 . PHE A 1 212 ? 61.906 16.262 21.326 1.00 13.08 ? 212 PHE A CE2 1 ATOM 1613 C CZ . PHE A 1 212 ? 62.070 15.334 20.316 1.00 14.29 ? 212 PHE A CZ 1 ATOM 1614 N N . PRO A 1 213 ? 59.308 21.929 20.018 1.00 8.15 ? 213 PRO A N 1 ATOM 1615 C CA . PRO A 1 213 ? 59.100 23.392 19.903 1.00 8.61 ? 213 PRO A CA 1 ATOM 1616 C C . PRO A 1 213 ? 60.382 24.149 19.617 1.00 9.02 ? 213 PRO A C 1 ATOM 1617 O O . PRO A 1 213 ? 60.326 25.287 19.126 1.00 10.88 ? 213 PRO A O 1 ATOM 1618 C CB . PRO A 1 213 ? 58.439 23.714 21.243 1.00 9.05 ? 213 PRO A CB 1 ATOM 1619 C CG . PRO A 1 213 ? 58.970 22.702 22.210 1.00 8.63 ? 213 PRO A CG 1 ATOM 1620 C CD . PRO A 1 213 ? 59.030 21.441 21.398 1.00 8.46 ? 213 PRO A CD 1 ATOM 1621 N N . GLY A 1 214 ? 61.531 23.574 19.978 1.00 9.13 ? 214 GLY A N 1 ATOM 1622 C CA . GLY A 1 214 ? 62.847 24.148 19.749 1.00 10.66 ? 214 GLY A CA 1 ATOM 1623 C C . GLY A 1 214 ? 63.757 23.113 19.148 1.00 12.87 ? 214 GLY A C 1 ATOM 1624 O O . GLY A 1 214 ? 63.480 22.561 18.105 1.00 17.11 ? 214 GLY A O 1 ATOM 1625 N N . SER A 1 215 ? 64.844 22.816 19.852 1.00 14.03 ? 215 SER A N 1 ATOM 1626 C CA . SER A 1 215 ? 65.774 21.697 19.427 1.00 16.22 ? 215 SER A CA 1 ATOM 1627 C C . SER A 1 215 ? 65.297 20.337 19.949 1.00 14.05 ? 215 SER A C 1 ATOM 1628 O O . SER A 1 215 ? 64.468 20.158 20.829 1.00 16.05 ? 215 SER A O 1 ATOM 1629 C CB . SER A 1 215 ? 67.145 22.183 19.841 1.00 19.99 ? 215 SER A CB 1 ATOM 1630 O OG . SER A 1 215 ? 67.207 22.298 21.219 1.00 23.12 ? 215 SER A OG 1 ATOM 1631 N N . ALA A 1 216 ? 65.835 19.266 19.338 1.00 17.88 ? 216 ALA A N 1 ATOM 1632 C CA . ALA A 1 216 ? 65.434 17.870 19.464 1.00 18.93 ? 216 ALA A CA 1 ATOM 1633 C C . ALA A 1 216 ? 66.304 17.124 20.478 1.00 21.92 ? 216 ALA A C 1 ATOM 1634 O O . ALA A 1 216 ? 66.023 15.933 20.736 1.00 31.30 ? 216 ALA A O 1 ATOM 1635 C CB . ALA A 1 216 ? 65.423 17.076 18.156 1.00 20.54 ? 216 ALA A CB 1 ATOM 1636 N N . ASN A 1 217 ? 67.231 17.840 21.080 1.00 20.95 ? 217 ASN A N 1 ATOM 1637 C CA . ASN A 1 217 ? 68.368 17.349 21.850 1.00 27.54 ? 217 ASN A CA 1 ATOM 1638 C C . ASN A 1 217 ? 68.434 17.750 23.291 1.00 26.52 ? 217 ASN A C 1 ATOM 1639 O O . ASN A 1 217 ? 69.521 17.855 23.803 1.00 37.72 ? 217 ASN A O 1 ATOM 1640 C CB . ASN A 1 217 ? 69.731 17.887 21.263 1.00 33.51 ? 217 ASN A CB 1 ATOM 1641 C CG . ASN A 1 217 ? 69.614 19.398 21.039 1.00 42.67 ? 217 ASN A CG 1 ATOM 1642 O OD1 . ASN A 1 217 ? 68.868 20.185 21.592 1.00 50.19 ? 217 ASN A OD1 1 ATOM 1643 N ND2 . ASN A 1 217 ? 70.427 19.914 20.124 1.00 72.78 ? 217 ASN A ND2 1 ATOM 1644 N N . ASN A 1 218 ? 67.326 17.999 23.961 1.00 15.53 ? 218 ASN A N 1 ATOM 1645 C CA . ASN A 1 218 ? 67.394 18.480 25.299 1.00 12.57 ? 218 ASN A CA 1 ATOM 1646 C C . ASN A 1 218 ? 67.113 17.380 26.341 1.00 11.55 ? 218 ASN A C 1 ATOM 1647 O O . ASN A 1 218 ? 66.133 16.642 26.251 1.00 11.95 ? 218 ASN A O 1 ATOM 1648 C CB . ASN A 1 218 ? 66.388 19.617 25.521 1.00 11.66 ? 218 ASN A CB 1 ATOM 1649 C CG . ASN A 1 218 ? 66.623 20.741 24.535 1.00 13.17 ? 218 ASN A CG 1 ATOM 1650 O OD1 . ASN A 1 218 ? 65.705 21.149 23.790 1.00 19.54 ? 218 ASN A OD1 1 ATOM 1651 N ND2 . ASN A 1 218 ? 67.763 21.294 24.498 1.00 14.82 ? 218 ASN A ND2 1 ATOM 1652 N N . THR A 1 219 ? 67.928 17.362 27.376 1.00 12.76 ? 219 THR A N 1 ATOM 1653 C CA . THR A 1 219 ? 67.686 16.464 28.510 1.00 11.86 ? 219 THR A CA 1 ATOM 1654 C C . THR A 1 219 ? 66.323 16.708 29.117 1.00 9.71 ? 219 THR A C 1 ATOM 1655 O O . THR A 1 219 ? 65.934 17.839 29.369 1.00 11.31 ? 219 THR A O 1 ATOM 1656 C CB . THR A 1 219 ? 68.813 16.653 29.559 1.00 15.46 ? 219 THR A CB 1 ATOM 1657 O OG1 . THR A 1 219 ? 70.069 16.372 28.922 1.00 20.09 ? 219 THR A OG1 1 ATOM 1658 C CG2 . THR A 1 219 ? 68.634 15.749 30.766 1.00 15.87 ? 219 THR A CG2 1 ATOM 1659 N N . GLY A 1 220 ? 65.588 15.629 29.413 1.00 9.28 ? 220 GLY A N 1 ATOM 1660 C CA . GLY A 1 220 ? 64.310 15.724 30.058 1.00 9.88 ? 220 GLY A CA 1 ATOM 1661 C C . GLY A 1 220 ? 63.126 16.073 29.206 1.00 8.16 ? 220 GLY A C 1 ATOM 1662 O O . GLY A 1 220 ? 62.029 16.264 29.752 1.00 8.24 ? 220 GLY A O 1 ATOM 1663 N N . GLU A 1 221 ? 63.326 16.133 27.875 1.00 8.44 ? 221 GLU A N 1 ATOM 1664 C CA . GLU A 1 221 ? 62.270 16.513 26.949 1.00 7.85 ? 221 GLU A CA 1 ATOM 1665 C C . GLU A 1 221 ? 62.029 15.368 25.966 1.00 7.94 ? 221 GLU A C 1 ATOM 1666 O O . GLU A 1 221 ? 62.995 14.699 25.547 1.00 9.44 ? 221 GLU A O 1 ATOM 1667 C CB . GLU A 1 221 ? 62.704 17.770 26.202 1.00 8.94 ? 221 GLU A CB 1 ATOM 1668 C CG . GLU A 1 221 ? 61.677 18.352 25.261 1.00 9.74 ? 221 GLU A CG 1 ATOM 1669 C CD . GLU A 1 221 ? 62.108 19.571 24.507 1.00 10.61 ? 221 GLU A CD 1 ATOM 1670 O OE1 . GLU A 1 221 ? 63.223 20.050 24.677 1.00 16.68 ? 221 GLU A OE1 1 ATOM 1671 O OE2 . GLU A 1 221 ? 61.296 20.085 23.693 1.00 10.24 ? 221 GLU A OE2 1 ATOM 1672 N N . VAL A 1 222 ? 60.774 15.188 25.540 1.00 7.76 ? 222 VAL A N 1 ATOM 1673 C CA . VAL A 1 222 ? 60.417 14.230 24.479 1.00 7.83 ? 222 VAL A CA 1 ATOM 1674 C C . VAL A 1 222 ? 59.534 14.979 23.484 1.00 7.79 ? 222 VAL A C 1 ATOM 1675 O O . VAL A 1 222 ? 59.131 16.122 23.692 1.00 8.02 ? 222 VAL A O 1 ATOM 1676 C CB . VAL A 1 222 ? 59.723 12.980 25.072 1.00 8.21 ? 222 VAL A CB 1 ATOM 1677 C CG1 . VAL A 1 222 ? 60.729 12.161 25.918 1.00 9.91 ? 222 VAL A CG1 1 ATOM 1678 C CG2 . VAL A 1 222 ? 58.496 13.343 25.865 1.00 9.01 ? 222 VAL A CG2 1 ATOM 1679 N N . ALA A 1 223 ? 59.205 14.291 22.367 1.00 7.91 ? 223 ALA A N 1 ATOM 1680 C CA . ALA A 1 223 ? 58.465 14.957 21.309 1.00 7.85 ? 223 ALA A CA 1 ATOM 1681 C C . ALA A 1 223 ? 57.082 15.391 21.792 1.00 7.44 ? 223 ALA A C 1 ATOM 1682 O O . ALA A 1 223 ? 56.402 14.705 22.572 1.00 7.84 ? 223 ALA A O 1 ATOM 1683 C CB . ALA A 1 223 ? 58.332 14.011 20.105 1.00 9.14 ? 223 ALA A CB 1 ATOM 1684 N N . SER A 1 224 ? 56.667 16.556 21.289 1.00 7.56 ? 224 SER A N 1 ATOM 1685 C CA . SER A 1 224 ? 55.414 17.208 21.590 1.00 7.63 ? 224 SER A CA 1 ATOM 1686 C C . SER A 1 224 ? 54.378 16.992 20.498 1.00 7.29 ? 224 SER A C 1 ATOM 1687 O O . SER A 1 224 ? 54.759 16.904 19.309 1.00 7.96 ? 224 SER A O 1 ATOM 1688 C CB . SER A 1 224 ? 55.762 18.730 21.629 1.00 9.52 ? 224 SER A CB 1 ATOM 1689 O OG . SER A 1 224 ? 54.573 19.494 21.586 1.00 8.52 ? 224 SER A OG 1 ATOM 1690 N N . PRO A 1 225 ? 53.079 16.974 20.840 1.00 7.37 ? 225 PRO A N 1 ATOM 1691 C CA . PRO A 1 225 ? 52.046 16.849 19.816 1.00 7.97 ? 225 PRO A CA 1 ATOM 1692 C C . PRO A 1 225 ? 51.666 18.175 19.172 1.00 8.31 ? 225 PRO A C 1 ATOM 1693 O O . PRO A 1 225 ? 50.936 18.177 18.171 1.00 9.10 ? 225 PRO A O 1 ATOM 1694 C CB . PRO A 1 225 ? 50.869 16.302 20.675 1.00 8.45 ? 225 PRO A CB 1 ATOM 1695 C CG . PRO A 1 225 ? 51.015 17.003 21.984 1.00 7.94 ? 225 PRO A CG 1 ATOM 1696 C CD . PRO A 1 225 ? 52.529 17.060 22.220 1.00 8.30 ? 225 PRO A CD 1 ATOM 1697 N N . LEU A 1 226 ? 52.096 19.294 19.757 1.00 7.79 ? 226 LEU A N 1 ATOM 1698 C CA . LEU A 1 226 ? 51.690 20.631 19.344 1.00 7.90 ? 226 LEU A CA 1 ATOM 1699 C C . LEU A 1 226 ? 52.900 21.550 19.286 1.00 7.43 ? 226 LEU A C 1 ATOM 1700 O O . LEU A 1 226 ? 52.943 22.580 19.974 1.00 8.08 ? 226 LEU A O 1 ATOM 1701 C CB . LEU A 1 226 ? 50.568 21.190 20.256 1.00 8.63 ? 226 LEU A CB 1 ATOM 1702 C CG . LEU A 1 226 ? 49.245 20.372 20.257 1.00 10.33 ? 226 LEU A CG 1 ATOM 1703 C CD1 . LEU A 1 226 ? 48.380 20.692 21.490 1.00 15.19 ? 226 LEU A CD1 1 ATOM 1704 C CD2 . LEU A 1 226 ? 48.424 20.640 19.026 1.00 10.81 ? 226 LEU A CD2 1 ATOM 1705 N N . PRO A 1 227 ? 53.921 21.206 18.484 1.00 7.79 ? 227 PRO A N 1 ATOM 1706 C CA . PRO A 1 227 ? 55.198 21.911 18.586 1.00 8.07 ? 227 PRO A CA 1 ATOM 1707 C C . PRO A 1 227 ? 55.282 23.263 17.865 1.00 7.95 ? 227 PRO A C 1 ATOM 1708 O O . PRO A 1 227 ? 56.278 23.957 17.981 1.00 8.83 ? 227 PRO A O 1 ATOM 1709 C CB . PRO A 1 227 ? 56.180 20.936 17.902 1.00 9.20 ? 227 PRO A CB 1 ATOM 1710 C CG . PRO A 1 227 ? 55.330 20.264 16.856 1.00 9.23 ? 227 PRO A CG 1 ATOM 1711 C CD . PRO A 1 227 ? 53.994 20.060 17.554 1.00 8.40 ? 227 PRO A CD 1 ATOM 1712 N N . LEU A 1 228 ? 54.315 23.653 17.098 1.00 8.06 ? 228 LEU A N 1 ATOM 1713 C CA . LEU A 1 228 ? 54.342 24.859 16.308 1.00 8.43 ? 228 LEU A CA 1 ATOM 1714 C C . LEU A 1 228 ? 54.381 26.094 17.197 1.00 8.44 ? 228 LEU A C 1 ATOM 1715 O O . LEU A 1 228 ? 53.495 26.280 18.065 1.00 8.61 ? 228 LEU A O 1 ATOM 1716 C CB . LEU A 1 228 ? 53.096 24.990 15.391 1.00 8.86 ? 228 LEU A CB 1 ATOM 1717 C CG . LEU A 1 228 ? 53.058 26.242 14.556 1.00 9.71 ? 228 LEU A CG 1 ATOM 1718 C CD1 . LEU A 1 228 ? 54.223 26.270 13.558 1.00 12.14 ? 228 LEU A CD1 1 ATOM 1719 C CD2 . LEU A 1 228 ? 51.695 26.278 13.845 1.00 12.15 ? 228 LEU A CD2 1 ATOM 1720 N N . GLY A 1 229 ? 55.306 26.979 16.901 1.00 9.40 ? 229 GLY A N 1 ATOM 1721 C CA . GLY A 1 229 ? 55.384 28.296 17.498 1.00 10.90 ? 229 GLY A CA 1 ATOM 1722 C C . GLY A 1 229 ? 55.663 29.362 16.430 1.00 10.30 ? 229 GLY A C 1 ATOM 1723 O O . GLY A 1 229 ? 56.026 29.042 15.268 1.00 12.95 ? 229 GLY A O 1 ATOM 1724 N N . SER A 1 230 ? 55.467 30.597 16.826 1.00 9.95 ? 230 SER A N 1 ATOM 1725 C CA . SER A 1 230 ? 55.735 31.727 15.928 1.00 10.89 ? 230 SER A CA 1 ATOM 1726 C C . SER A 1 230 ? 55.940 32.940 16.815 1.00 11.37 ? 230 SER A C 1 ATOM 1727 O O . SER A 1 230 ? 55.146 33.179 17.741 1.00 11.52 ? 230 SER A O 1 ATOM 1728 C CB . SER A 1 230 ? 54.574 31.998 14.978 1.00 15.21 ? 230 SER A CB 1 ATOM 1729 O OG . SER A 1 230 ? 54.901 33.043 14.088 1.00 20.71 ? 230 SER A OG 1 ATOM 1730 N N . GLY A 1 231 ? 56.977 33.726 16.582 1.00 12.88 ? 231 GLY A N 1 ATOM 1731 C CA . GLY A 1 231 ? 57.207 34.891 17.413 1.00 14.06 ? 231 GLY A CA 1 ATOM 1732 C C . GLY A 1 231 ? 57.429 34.468 18.880 1.00 13.31 ? 231 GLY A C 1 ATOM 1733 O O . GLY A 1 231 ? 58.149 33.525 19.198 1.00 14.60 ? 231 GLY A O 1 ATOM 1734 N N . SER A 1 232 ? 56.734 35.173 19.783 1.00 13.33 ? 232 SER A N 1 ATOM 1735 C CA . SER A 1 232 ? 56.805 34.829 21.212 1.00 13.15 ? 232 SER A CA 1 ATOM 1736 C C . SER A 1 232 ? 55.818 33.714 21.567 1.00 10.39 ? 232 SER A C 1 ATOM 1737 O O . SER A 1 232 ? 55.834 33.255 22.724 1.00 10.64 ? 232 SER A O 1 ATOM 1738 C CB A SER A 1 232 ? 56.442 36.029 22.088 0.52 18.32 ? 232 SER A CB 1 ATOM 1739 C CB B SER A 1 232 ? 56.594 36.053 22.102 0.52 13.72 ? 232 SER A CB 1 ATOM 1740 O OG A SER A 1 232 ? 56.979 37.255 21.647 0.52 23.73 ? 232 SER A OG 1 ATOM 1741 O OG B SER A 1 232 ? 55.269 36.442 21.818 0.52 13.91 ? 232 SER A OG 1 ATOM 1742 N N . ASP A 1 233 ? 54.976 33.268 20.627 1.00 9.76 ? 233 ASP A N 1 ATOM 1743 C CA . ASP A 1 233 ? 54.008 32.179 20.910 1.00 8.71 ? 233 ASP A CA 1 ATOM 1744 C C . ASP A 1 233 ? 54.716 30.847 20.737 1.00 8.90 ? 233 ASP A C 1 ATOM 1745 O O . ASP A 1 233 ? 54.579 30.171 19.704 1.00 10.77 ? 233 ASP A O 1 ATOM 1746 C CB . ASP A 1 233 ? 52.810 32.284 20.034 1.00 9.50 ? 233 ASP A CB 1 ATOM 1747 C CG . ASP A 1 233 ? 51.904 33.455 20.274 1.00 11.22 ? 233 ASP A CG 1 ATOM 1748 O OD1 . ASP A 1 233 ? 52.036 34.196 21.273 1.00 11.48 ? 233 ASP A OD1 1 ATOM 1749 O OD2 . ASP A 1 233 ? 50.992 33.665 19.412 1.00 16.35 ? 233 ASP A OD2 1 ATOM 1750 N N . THR A 1 234 ? 55.467 30.417 21.750 1.00 8.21 ? 234 THR A N 1 ATOM 1751 C CA . THR A 1 234 ? 56.220 29.200 21.682 1.00 7.75 ? 234 THR A CA 1 ATOM 1752 C C . THR A 1 234 ? 55.310 27.976 21.641 1.00 7.73 ? 234 THR A C 1 ATOM 1753 O O . THR A 1 234 ? 54.245 27.941 22.271 1.00 7.96 ? 234 THR A O 1 ATOM 1754 C CB . THR A 1 234 ? 57.132 29.126 22.916 1.00 8.42 ? 234 THR A CB 1 ATOM 1755 O OG1 . THR A 1 234 ? 57.853 30.351 22.970 1.00 10.36 ? 234 THR A OG1 1 ATOM 1756 C CG2 . THR A 1 234 ? 58.088 27.953 22.877 1.00 8.54 ? 234 THR A CG2 1 ATOM 1757 N N . GLY A 1 235 ? 55.755 26.933 20.893 1.00 7.71 ? 235 GLY A N 1 ATOM 1758 C CA . GLY A 1 235 ? 55.028 25.703 20.853 1.00 8.17 ? 235 GLY A CA 1 ATOM 1759 C C . GLY A 1 235 ? 55.041 24.925 22.185 1.00 6.81 ? 235 GLY A C 1 ATOM 1760 O O . GLY A 1 235 ? 55.825 25.187 23.071 1.00 7.31 ? 235 GLY A O 1 ATOM 1761 N N . GLU A 1 236 ? 54.133 23.942 22.269 1.00 6.76 ? 236 GLU A N 1 ATOM 1762 C CA . GLU A 1 236 ? 54.041 23.093 23.456 1.00 6.61 ? 236 GLU A CA 1 ATOM 1763 C C . GLU A 1 236 ? 55.280 22.246 23.587 1.00 6.67 ? 236 GLU A C 1 ATOM 1764 O O . GLU A 1 236 ? 55.813 21.646 22.607 1.00 7.10 ? 236 GLU A O 1 ATOM 1765 C CB . GLU A 1 236 ? 52.785 22.210 23.349 1.00 7.03 ? 236 GLU A CB 1 ATOM 1766 C CG . GLU A 1 236 ? 52.603 21.204 24.486 1.00 6.94 ? 236 GLU A CG 1 ATOM 1767 C CD . GLU A 1 236 ? 51.273 20.516 24.445 1.00 6.96 ? 236 GLU A CD 1 ATOM 1768 O OE1 . GLU A 1 236 ? 51.125 19.290 24.362 1.00 8.22 ? 236 GLU A OE1 1 ATOM 1769 O OE2 . GLU A 1 236 ? 50.256 21.333 24.540 1.00 7.81 ? 236 GLU A OE2 1 ATOM 1770 N N . MET A 1 237 ? 55.744 22.114 24.850 1.00 6.41 ? 237 MET A N 1 ATOM 1771 C CA . MET A 1 237 ? 56.807 21.212 25.216 1.00 6.54 ? 237 MET A CA 1 ATOM 1772 C C . MET A 1 237 ? 56.235 20.026 26.013 1.00 6.12 ? 237 MET A C 1 ATOM 1773 O O . MET A 1 237 ? 55.270 20.219 26.774 1.00 6.69 ? 237 MET A O 1 ATOM 1774 C CB . MET A 1 237 ? 57.832 21.956 26.089 1.00 7.01 ? 237 MET A CB 1 ATOM 1775 C CG . MET A 1 237 ? 58.994 21.100 26.552 1.00 7.92 ? 237 MET A CG 1 ATOM 1776 S SD . MET A 1 237 ? 60.271 22.006 27.421 1.00 9.00 ? 237 MET A SD 1 ATOM 1777 C CE . MET A 1 237 ? 61.001 22.932 26.104 1.00 9.75 ? 237 MET A CE 1 ATOM 1778 N N . ARG A 1 238 ? 56.860 18.859 25.854 1.00 6.44 ? 238 ARG A N 1 ATOM 1779 C CA . ARG A 1 238 ? 56.504 17.695 26.660 1.00 6.21 ? 238 ARG A CA 1 ATOM 1780 C C . ARG A 1 238 ? 57.733 17.237 27.454 1.00 6.36 ? 238 ARG A C 1 ATOM 1781 O O . ARG A 1 238 ? 58.817 16.971 26.898 1.00 7.15 ? 238 ARG A O 1 ATOM 1782 C CB . ARG A 1 238 ? 55.990 16.538 25.791 1.00 6.65 ? 238 ARG A CB 1 ATOM 1783 C CG . ARG A 1 238 ? 55.508 15.356 26.632 1.00 6.78 ? 238 ARG A CG 1 ATOM 1784 C CD . ARG A 1 238 ? 54.988 14.223 25.760 1.00 7.94 ? 238 ARG A CD 1 ATOM 1785 N NE . ARG A 1 238 ? 53.765 14.604 25.089 1.00 7.10 ? 238 ARG A NE 1 ATOM 1786 C CZ . ARG A 1 238 ? 53.138 13.846 24.220 1.00 6.90 ? 238 ARG A CZ 1 ATOM 1787 N NH1 . ARG A 1 238 ? 53.683 12.716 23.774 1.00 7.64 ? 238 ARG A NH1 1 ATOM 1788 N NH2 . ARG A 1 238 ? 51.962 14.226 23.756 1.00 7.39 ? 238 ARG A NH2 1 ATOM 1789 N N . LEU A 1 239 ? 57.540 17.134 28.784 1.00 6.20 ? 239 LEU A N 1 ATOM 1790 C CA . LEU A 1 239 ? 58.578 16.613 29.651 1.00 6.43 ? 239 LEU A CA 1 ATOM 1791 C C . LEU A 1 239 ? 58.592 15.075 29.602 1.00 6.48 ? 239 LEU A C 1 ATOM 1792 O O . LEU A 1 239 ? 57.545 14.416 29.576 1.00 7.11 ? 239 LEU A O 1 ATOM 1793 C CB . LEU A 1 239 ? 58.357 17.070 31.082 1.00 6.63 ? 239 LEU A CB 1 ATOM 1794 C CG . LEU A 1 239 ? 58.383 18.582 31.307 1.00 7.27 ? 239 LEU A CG 1 ATOM 1795 C CD1 . LEU A 1 239 ? 58.182 18.846 32.805 1.00 8.77 ? 239 LEU A CD1 1 ATOM 1796 C CD2 . LEU A 1 239 ? 59.642 19.229 30.773 1.00 8.34 ? 239 LEU A CD2 1 ATOM 1797 N N . GLN A 1 240 ? 59.799 14.515 29.669 1.00 6.88 ? 240 GLN A N 1 ATOM 1798 C CA . GLN A 1 240 ? 59.950 13.077 29.769 1.00 7.10 ? 240 GLN A CA 1 ATOM 1799 C C . GLN A 1 240 ? 59.230 12.520 30.981 1.00 6.79 ? 240 GLN A C 1 ATOM 1800 O O . GLN A 1 240 ? 58.645 11.410 30.916 1.00 7.64 ? 240 GLN A O 1 ATOM 1801 C CB . GLN A 1 240 ? 61.453 12.677 29.778 1.00 7.51 ? 240 GLN A CB 1 ATOM 1802 C CG . GLN A 1 240 ? 61.690 11.187 29.810 1.00 9.20 ? 240 GLN A CG 1 ATOM 1803 C CD . GLN A 1 240 ? 61.588 10.382 31.107 1.00 9.49 ? 240 GLN A CD 1 ATOM 1804 O OE1 . GLN A 1 240 ? 61.314 9.151 31.073 1.00 10.58 ? 240 GLN A OE1 1 ATOM 1805 N NE2 . GLN A 1 240 ? 61.736 11.002 32.319 1.00 9.47 ? 240 GLN A NE2 1 ATOM 1806 N N . SER A 1 241 ? 59.242 13.217 32.109 1.00 6.73 ? 241 SER A N 1 ATOM 1807 C CA . SER A 1 241 ? 58.623 12.745 33.335 1.00 7.05 ? 241 SER A CA 1 ATOM 1808 C C . SER A 1 241 ? 57.112 12.653 33.215 1.00 6.83 ? 241 SER A C 1 ATOM 1809 O O . SER A 1 241 ? 56.490 11.654 33.669 1.00 7.34 ? 241 SER A O 1 ATOM 1810 C CB . SER A 1 241 ? 59.031 13.658 34.500 1.00 7.47 ? 241 SER A CB 1 ATOM 1811 O OG . SER A 1 241 ? 58.933 15.025 34.128 1.00 7.70 ? 241 SER A OG 1 ATOM 1812 N N . ASP A 1 242 ? 56.471 13.678 32.626 1.00 6.91 ? 242 ASP A N 1 ATOM 1813 C CA . ASP A 1 242 ? 55.024 13.637 32.447 1.00 6.88 ? 242 ASP A CA 1 ATOM 1814 C C . ASP A 1 242 ? 54.648 12.492 31.500 1.00 6.89 ? 242 ASP A C 1 ATOM 1815 O O . ASP A 1 242 ? 53.699 11.720 31.764 1.00 7.11 ? 242 ASP A O 1 ATOM 1816 C CB . ASP A 1 242 ? 54.528 14.994 31.905 1.00 7.58 ? 242 ASP A CB 1 ATOM 1817 C CG . ASP A 1 242 ? 54.532 16.089 33.023 1.00 8.02 ? 242 ASP A CG 1 ATOM 1818 O OD1 . ASP A 1 242 ? 54.475 17.318 32.581 1.00 8.79 ? 242 ASP A OD1 1 ATOM 1819 O OD2 . ASP A 1 242 ? 54.585 15.778 34.217 1.00 9.52 ? 242 ASP A OD2 1 ATOM 1820 N N . PHE A 1 243 ? 55.393 12.367 30.390 1.00 6.68 ? 243 PHE A N 1 ATOM 1821 C CA . PHE A 1 243 ? 55.179 11.254 29.457 1.00 6.94 ? 243 PHE A CA 1 ATOM 1822 C C . PHE A 1 243 ? 55.300 9.911 30.179 1.00 6.56 ? 243 PHE A C 1 ATOM 1823 O O . PHE A 1 243 ? 54.471 9.007 30.009 1.00 7.53 ? 243 PHE A O 1 ATOM 1824 C CB . PHE A 1 243 ? 56.195 11.380 28.324 1.00 7.47 ? 243 PHE A CB 1 ATOM 1825 C CG . PHE A 1 243 ? 56.173 10.284 27.290 1.00 8.07 ? 243 PHE A CG 1 ATOM 1826 C CD1 . PHE A 1 243 ? 57.129 9.268 27.347 1.00 11.12 ? 243 PHE A CD1 1 ATOM 1827 C CD2 . PHE A 1 243 ? 55.201 10.257 26.296 1.00 9.04 ? 243 PHE A CD2 1 ATOM 1828 C CE1 . PHE A 1 243 ? 57.114 8.240 26.388 1.00 14.13 ? 243 PHE A CE1 1 ATOM 1829 C CE2 . PHE A 1 243 ? 55.190 9.227 25.310 1.00 10.65 ? 243 PHE A CE2 1 ATOM 1830 C CZ . PHE A 1 243 ? 56.166 8.237 25.413 1.00 12.97 ? 243 PHE A CZ 1 ATOM 1831 N N . ALA A 1 244 ? 56.375 9.746 30.955 1.00 7.05 ? 244 ALA A N 1 ATOM 1832 C CA . ALA A 1 244 ? 56.597 8.484 31.630 1.00 7.25 ? 244 ALA A CA 1 ATOM 1833 C C . ALA A 1 244 ? 55.463 8.168 32.605 1.00 6.69 ? 244 ALA A C 1 ATOM 1834 O O . ALA A 1 244 ? 55.012 7.010 32.701 1.00 7.51 ? 244 ALA A O 1 ATOM 1835 C CB . ALA A 1 244 ? 57.962 8.477 32.313 1.00 7.97 ? 244 ALA A CB 1 ATOM 1836 N N . LEU A 1 245 ? 55.028 9.163 33.385 1.00 6.80 ? 245 LEU A N 1 ATOM 1837 C CA . LEU A 1 245 ? 53.921 8.993 34.337 1.00 6.70 ? 245 LEU A CA 1 ATOM 1838 C C . LEU A 1 245 ? 52.617 8.624 33.627 1.00 7.02 ? 245 LEU A C 1 ATOM 1839 O O . LEU A 1 245 ? 51.818 7.801 34.129 1.00 8.03 ? 245 LEU A O 1 ATOM 1840 C CB . LEU A 1 245 ? 53.733 10.225 35.196 1.00 7.52 ? 245 LEU A CB 1 ATOM 1841 C CG . LEU A 1 245 ? 54.859 10.437 36.226 1.00 7.87 ? 245 LEU A CG 1 ATOM 1842 C CD1 . LEU A 1 245 ? 54.822 11.881 36.699 1.00 9.85 ? 245 LEU A CD1 1 ATOM 1843 C CD2 . LEU A 1 245 ? 54.695 9.509 37.443 1.00 8.78 ? 245 LEU A CD2 1 ATOM 1844 N N . ALA A 1 246 ? 52.383 9.207 32.457 1.00 6.83 ? 246 ALA A N 1 ATOM 1845 C CA . ALA A 1 246 ? 51.160 8.926 31.724 1.00 7.00 ? 246 ALA A CA 1 ATOM 1846 C C . ALA A 1 246 ? 51.102 7.477 31.249 1.00 7.43 ? 246 ALA A C 1 ATOM 1847 O O . ALA A 1 246 ? 50.024 6.952 31.001 1.00 8.79 ? 246 ALA A O 1 ATOM 1848 C CB . ALA A 1 246 ? 51.041 9.886 30.557 1.00 7.59 ? 246 ALA A CB 1 ATOM 1849 N N . HIS A 1 247 ? 52.276 6.830 31.080 1.00 7.10 ? 247 HIS A N 1 ATOM 1850 C CA . HIS A 1 247 ? 52.339 5.479 30.508 1.00 7.76 ? 247 HIS A CA 1 ATOM 1851 C C . HIS A 1 247 ? 52.749 4.400 31.488 1.00 8.02 ? 247 HIS A C 1 ATOM 1852 O O . HIS A 1 247 ? 52.593 3.213 31.165 1.00 11.23 ? 247 HIS A O 1 ATOM 1853 C CB . HIS A 1 247 ? 53.236 5.451 29.274 1.00 8.53 ? 247 HIS A CB 1 ATOM 1854 C CG . HIS A 1 247 ? 52.698 6.336 28.186 1.00 8.59 ? 247 HIS A CG 1 ATOM 1855 N ND1 . HIS A 1 247 ? 51.481 6.059 27.574 1.00 10.12 ? 247 HIS A ND1 1 ATOM 1856 C CD2 . HIS A 1 247 ? 53.140 7.480 27.645 1.00 8.48 ? 247 HIS A CD2 1 ATOM 1857 C CE1 . HIS A 1 247 ? 51.255 7.018 26.683 1.00 9.98 ? 247 HIS A CE1 1 ATOM 1858 N NE2 . HIS A 1 247 ? 52.225 7.897 26.692 1.00 9.16 ? 247 HIS A NE2 1 ATOM 1859 N N . ASP A 1 248 ? 53.252 4.733 32.657 1.00 7.45 ? 248 ASP A N 1 ATOM 1860 C CA . ASP A 1 248 ? 53.729 3.714 33.585 1.00 7.38 ? 248 ASP A CA 1 ATOM 1861 C C . ASP A 1 248 ? 52.552 3.006 34.212 1.00 7.35 ? 248 ASP A C 1 ATOM 1862 O O . ASP A 1 248 ? 51.555 3.639 34.577 1.00 7.77 ? 248 ASP A O 1 ATOM 1863 C CB . ASP A 1 248 ? 54.592 4.401 34.652 1.00 7.45 ? 248 ASP A CB 1 ATOM 1864 C CG . ASP A 1 248 ? 55.287 3.401 35.578 1.00 7.49 ? 248 ASP A CG 1 ATOM 1865 O OD1 . ASP A 1 248 ? 54.597 2.859 36.503 1.00 8.40 ? 248 ASP A OD1 1 ATOM 1866 O OD2 . ASP A 1 248 ? 56.502 3.156 35.380 1.00 8.37 ? 248 ASP A OD2 1 ATOM 1867 N N . PRO A 1 249 ? 52.607 1.656 34.406 1.00 8.42 ? 249 PRO A N 1 ATOM 1868 C CA . PRO A 1 249 ? 51.455 0.974 35.037 1.00 9.19 ? 249 PRO A CA 1 ATOM 1869 C C . PRO A 1 249 ? 51.041 1.479 36.398 1.00 8.29 ? 249 PRO A C 1 ATOM 1870 O O . PRO A 1 249 ? 49.860 1.309 36.785 1.00 9.04 ? 249 PRO A O 1 ATOM 1871 C CB . PRO A 1 249 ? 51.970 -0.479 35.150 1.00 12.37 ? 249 PRO A CB 1 ATOM 1872 C CG . PRO A 1 249 ? 52.976 -0.591 34.083 1.00 12.30 ? 249 PRO A CG 1 ATOM 1873 C CD . PRO A 1 249 ? 53.677 0.712 34.005 1.00 9.57 ? 249 PRO A CD 1 ATOM 1874 N N . ARG A 1 250 ? 51.961 2.074 37.168 1.00 7.77 ? 250 ARG A N 1 ATOM 1875 C CA . ARG A 1 250 ? 51.586 2.578 38.490 1.00 7.82 ? 250 ARG A CA 1 ATOM 1876 C C . ARG A 1 250 ? 50.666 3.801 38.449 1.00 8.05 ? 250 ARG A C 1 ATOM 1877 O O . ARG A 1 250 ? 49.910 4.063 39.388 1.00 10.83 ? 250 ARG A O 1 ATOM 1878 C CB . ARG A 1 250 ? 52.856 2.912 39.271 1.00 7.80 ? 250 ARG A CB 1 ATOM 1879 C CG . ARG A 1 250 ? 53.639 1.641 39.576 1.00 8.54 ? 250 ARG A CG 1 ATOM 1880 C CD . ARG A 1 250 ? 55.044 1.936 40.127 1.00 8.16 ? 250 ARG A CD 1 ATOM 1881 N NE . ARG A 1 250 ? 55.882 2.326 38.966 1.00 7.94 ? 250 ARG A NE 1 ATOM 1882 C CZ . ARG A 1 250 ? 57.196 2.377 39.023 1.00 7.62 ? 250 ARG A CZ 1 ATOM 1883 N NH1 . ARG A 1 250 ? 57.859 2.199 40.162 1.00 8.35 ? 250 ARG A NH1 1 ATOM 1884 N NH2 . ARG A 1 250 ? 57.893 2.612 37.916 1.00 8.26 ? 250 ARG A NH2 1 ATOM 1885 N N . THR A 1 251 ? 50.801 4.585 37.354 1.00 7.17 ? 251 THR A N 1 ATOM 1886 C CA . THR A 1 251 ? 50.205 5.924 37.314 1.00 7.09 ? 251 THR A CA 1 ATOM 1887 C C . THR A 1 251 ? 49.302 6.156 36.099 1.00 7.30 ? 251 THR A C 1 ATOM 1888 O O . THR A 1 251 ? 48.608 7.166 36.092 1.00 7.57 ? 251 THR A O 1 ATOM 1889 C CB . THR A 1 251 ? 51.332 6.967 37.378 1.00 7.09 ? 251 THR A CB 1 ATOM 1890 O OG1 . THR A 1 251 ? 52.382 6.638 36.467 1.00 7.31 ? 251 THR A OG1 1 ATOM 1891 C CG2 . THR A 1 251 ? 51.912 7.057 38.790 1.00 8.73 ? 251 THR A CG2 1 ATOM 1892 N N . ALA A 1 252 ? 49.302 5.270 35.109 1.00 7.39 ? 252 ALA A N 1 ATOM 1893 C CA . ALA A 1 252 ? 48.586 5.531 33.863 1.00 7.80 ? 252 ALA A CA 1 ATOM 1894 C C . ALA A 1 252 ? 47.071 5.721 34.090 1.00 7.62 ? 252 ALA A C 1 ATOM 1895 O O . ALA A 1 252 ? 46.445 6.555 33.485 1.00 8.09 ? 252 ALA A O 1 ATOM 1896 C CB . ALA A 1 252 ? 48.834 4.425 32.865 1.00 9.15 ? 252 ALA A CB 1 ATOM 1897 N N . CYS A 1 253 ? 46.485 4.833 34.942 1.00 8.32 ? 253 CYS A N 1 ATOM 1898 C CA . CYS A 1 253 ? 45.039 4.948 35.208 1.00 9.18 ? 253 CYS A CA 1 ATOM 1899 C C . CYS A 1 253 ? 44.688 6.233 35.946 1.00 7.96 ? 253 CYS A C 1 ATOM 1900 O O . CYS A 1 253 ? 43.659 6.877 35.653 1.00 8.92 ? 253 CYS A O 1 ATOM 1901 C CB . CYS A 1 253 ? 44.502 3.714 35.954 1.00 11.62 ? 253 CYS A CB 1 ATOM 1902 S SG A CYS A 1 253 ? 44.414 2.289 34.674 0.52 10.91 ? 253 CYS A SG 1 ATOM 1903 S SG B CYS A 1 253 ? 45.367 3.546 37.642 0.52 35.20 ? 253 CYS A SG 1 ATOM 1904 N N . ILE A 1 254 ? 45.522 6.641 36.869 1.00 7.76 ? 254 ILE A N 1 ATOM 1905 C CA . ILE A 1 254 ? 45.312 7.892 37.572 1.00 7.74 ? 254 ILE A CA 1 ATOM 1906 C C . ILE A 1 254 ? 45.414 9.075 36.604 1.00 7.46 ? 254 ILE A C 1 ATOM 1907 O O . ILE A 1 254 ? 44.581 9.991 36.615 1.00 7.98 ? 254 ILE A O 1 ATOM 1908 C CB . ILE A 1 254 ? 46.324 8.052 38.752 1.00 8.50 ? 254 ILE A CB 1 ATOM 1909 C CG1 . ILE A 1 254 ? 46.144 6.931 39.784 1.00 9.67 ? 254 ILE A CG1 1 ATOM 1910 C CG2 . ILE A 1 254 ? 46.173 9.411 39.358 1.00 9.13 ? 254 ILE A CG2 1 ATOM 1911 C CD1 . ILE A 1 254 ? 47.402 6.706 40.641 1.00 11.84 ? 254 ILE A CD1 1 ATOM 1912 N N . TRP A 1 255 ? 46.439 9.072 35.739 1.00 7.19 ? 255 TRP A N 1 ATOM 1913 C CA . TRP A 1 255 ? 46.647 10.122 34.750 1.00 6.88 ? 255 TRP A CA 1 ATOM 1914 C C . TRP A 1 255 ? 45.393 10.282 33.866 1.00 7.02 ? 255 TRP A C 1 ATOM 1915 O O . TRP A 1 255 ? 44.841 11.350 33.691 1.00 7.30 ? 255 TRP A O 1 ATOM 1916 C CB . TRP A 1 255 ? 47.945 9.791 33.918 1.00 6.82 ? 255 TRP A CB 1 ATOM 1917 C CG . TRP A 1 255 ? 48.281 10.919 33.010 1.00 6.61 ? 255 TRP A CG 1 ATOM 1918 C CD1 . TRP A 1 255 ? 47.733 11.219 31.790 1.00 7.13 ? 255 TRP A CD1 1 ATOM 1919 C CD2 . TRP A 1 255 ? 49.243 11.973 33.243 1.00 7.02 ? 255 TRP A CD2 1 ATOM 1920 N NE1 . TRP A 1 255 ? 48.270 12.361 31.263 1.00 6.99 ? 255 TRP A NE1 1 ATOM 1921 C CE2 . TRP A 1 255 ? 49.196 12.868 32.133 1.00 6.71 ? 255 TRP A CE2 1 ATOM 1922 C CE3 . TRP A 1 255 ? 50.137 12.240 34.291 1.00 7.22 ? 255 TRP A CE3 1 ATOM 1923 C CZ2 . TRP A 1 255 ? 50.000 14.022 32.080 1.00 7.57 ? 255 TRP A CZ2 1 ATOM 1924 C CZ3 . TRP A 1 255 ? 50.911 13.399 34.209 1.00 8.33 ? 255 TRP A CZ3 1 ATOM 1925 C CH2 . TRP A 1 255 ? 50.833 14.275 33.118 1.00 8.53 ? 255 TRP A CH2 1 ATOM 1926 N N . GLN A 1 256 ? 44.982 9.131 33.275 1.00 7.37 ? 256 GLN A N 1 ATOM 1927 C CA . GLN A 1 256 ? 43.819 9.146 32.413 1.00 7.37 ? 256 GLN A CA 1 ATOM 1928 C C . GLN A 1 256 ? 42.546 9.580 33.152 1.00 7.68 ? 256 GLN A C 1 ATOM 1929 O O . GLN A 1 256 ? 41.660 10.211 32.577 1.00 8.08 ? 256 GLN A O 1 ATOM 1930 C CB . GLN A 1 256 ? 43.639 7.793 31.730 1.00 8.16 ? 256 GLN A CB 1 ATOM 1931 C CG . GLN A 1 256 ? 42.561 7.876 30.630 1.00 9.57 ? 256 GLN A CG 1 ATOM 1932 C CD . GLN A 1 256 ? 42.313 6.538 30.028 1.00 9.94 ? 256 GLN A CD 1 ATOM 1933 O OE1 . GLN A 1 256 ? 43.108 5.997 29.263 1.00 10.64 ? 256 GLN A OE1 1 ATOM 1934 N NE2 . GLN A 1 256 ? 41.142 5.956 30.350 1.00 13.68 ? 256 GLN A NE2 1 ATOM 1935 N N . GLY A 1 257 ? 42.444 9.209 34.433 1.00 7.87 ? 257 GLY A N 1 ATOM 1936 C CA . GLY A 1 257 ? 41.252 9.492 35.216 1.00 7.99 ? 257 GLY A CA 1 ATOM 1937 C C . GLY A 1 257 ? 40.968 10.946 35.450 1.00 7.61 ? 257 GLY A C 1 ATOM 1938 O O . GLY A 1 257 ? 39.855 11.305 35.838 1.00 8.91 ? 257 GLY A O 1 ATOM 1939 N N . PHE A 1 258 ? 41.965 11.842 35.196 1.00 7.01 ? 258 PHE A N 1 ATOM 1940 C CA . PHE A 1 258 ? 41.708 13.273 35.289 1.00 6.89 ? 258 PHE A CA 1 ATOM 1941 C C . PHE A 1 258 ? 41.252 13.874 33.955 1.00 7.02 ? 258 PHE A C 1 ATOM 1942 O O . PHE A 1 258 ? 40.770 15.011 33.948 1.00 7.87 ? 258 PHE A O 1 ATOM 1943 C CB . PHE A 1 258 ? 42.928 14.030 35.823 1.00 6.90 ? 258 PHE A CB 1 ATOM 1944 C CG . PHE A 1 258 ? 43.179 13.728 37.300 1.00 6.84 ? 258 PHE A CG 1 ATOM 1945 C CD1 . PHE A 1 258 ? 44.460 13.390 37.723 1.00 7.61 ? 258 PHE A CD1 1 ATOM 1946 C CD2 . PHE A 1 258 ? 42.172 13.776 38.241 1.00 7.60 ? 258 PHE A CD2 1 ATOM 1947 C CE1 . PHE A 1 258 ? 44.723 13.132 39.062 1.00 8.49 ? 258 PHE A CE1 1 ATOM 1948 C CE2 . PHE A 1 258 ? 42.405 13.517 39.603 1.00 8.14 ? 258 PHE A CE2 1 ATOM 1949 C CZ . PHE A 1 258 ? 43.709 13.204 40.014 1.00 8.20 ? 258 PHE A CZ 1 ATOM 1950 N N . VAL A 1 259 ? 41.414 13.165 32.829 1.00 7.10 ? 259 VAL A N 1 ATOM 1951 C CA . VAL A 1 259 ? 40.987 13.720 31.546 1.00 7.09 ? 259 VAL A CA 1 ATOM 1952 C C . VAL A 1 259 ? 39.489 14.017 31.593 1.00 7.38 ? 259 VAL A C 1 ATOM 1953 O O . VAL A 1 259 ? 38.669 13.100 31.852 1.00 7.98 ? 259 VAL A O 1 ATOM 1954 C CB . VAL A 1 259 ? 41.313 12.764 30.382 1.00 7.41 ? 259 VAL A CB 1 ATOM 1955 C CG1 . VAL A 1 259 ? 40.729 13.275 29.076 1.00 8.58 ? 259 VAL A CG1 1 ATOM 1956 C CG2 . VAL A 1 259 ? 42.812 12.527 30.249 1.00 8.19 ? 259 VAL A CG2 1 ATOM 1957 N N . ASN A 1 260 ? 39.095 15.251 31.317 1.00 7.41 ? 260 ASN A N 1 ATOM 1958 C CA . ASN A 1 260 ? 37.678 15.618 31.301 1.00 7.74 ? 260 ASN A CA 1 ATOM 1959 C C . ASN A 1 260 ? 36.953 15.443 32.650 1.00 7.83 ? 260 ASN A C 1 ATOM 1960 O O . ASN A 1 260 ? 35.747 15.361 32.678 1.00 9.59 ? 260 ASN A O 1 ATOM 1961 C CB . ASN A 1 260 ? 36.887 14.914 30.202 1.00 8.56 ? 260 ASN A CB 1 ATOM 1962 C CG . ASN A 1 260 ? 35.609 15.649 29.891 1.00 9.28 ? 260 ASN A CG 1 ATOM 1963 O OD1 . ASN A 1 260 ? 35.590 16.855 29.768 1.00 10.44 ? 260 ASN A OD1 1 ATOM 1964 N ND2 . ASN A 1 260 ? 34.526 14.894 29.647 1.00 11.80 ? 260 ASN A ND2 1 ATOM 1965 N N . GLU A 1 261 ? 37.740 15.491 33.746 1.00 8.01 ? 261 GLU A N 1 ATOM 1966 C CA . GLU A 1 261 ? 37.163 15.358 35.109 1.00 8.38 ? 261 GLU A CA 1 ATOM 1967 C C . GLU A 1 261 ? 37.645 16.581 35.943 1.00 8.23 ? 261 GLU A C 1 ATOM 1968 O O . GLU A 1 261 ? 38.477 16.417 36.860 1.00 8.59 ? 261 GLU A O 1 ATOM 1969 C CB . GLU A 1 261 ? 37.513 14.019 35.704 1.00 9.07 ? 261 GLU A CB 1 ATOM 1970 C CG . GLU A 1 261 ? 36.857 12.858 34.990 1.00 10.52 ? 261 GLU A CG 1 ATOM 1971 C CD . GLU A 1 261 ? 35.362 12.785 35.201 1.00 14.01 ? 261 GLU A CD 1 ATOM 1972 O OE1 . GLU A 1 261 ? 34.767 11.965 34.450 1.00 26.05 ? 261 GLU A OE1 1 ATOM 1973 O OE2 . GLU A 1 261 ? 34.788 13.454 36.086 1.00 17.26 ? 261 GLU A OE2 1 ATOM 1974 N N . GLN A 1 262 ? 37.171 17.764 35.601 1.00 8.83 ? 262 GLN A N 1 ATOM 1975 C CA . GLN A 1 262 ? 37.691 18.980 36.141 1.00 9.60 ? 262 GLN A CA 1 ATOM 1976 C C . GLN A 1 262 ? 37.485 19.064 37.674 1.00 8.88 ? 262 GLN A C 1 ATOM 1977 O O . GLN A 1 262 ? 38.443 19.413 38.392 1.00 8.84 ? 262 GLN A O 1 ATOM 1978 C CB A GLN A 1 262 ? 36.769 20.102 35.589 0.52 8.39 ? 262 GLN A CB 1 ATOM 1979 C CB B GLN A 1 262 ? 37.357 20.265 35.353 0.52 14.33 ? 262 GLN A CB 1 ATOM 1980 C CG A GLN A 1 262 ? 37.133 21.474 36.152 0.52 7.05 ? 262 GLN A CG 1 ATOM 1981 C CG B GLN A 1 262 ? 38.425 21.400 35.455 0.52 13.22 ? 262 GLN A CG 1 ATOM 1982 C CD A GLN A 1 262 ? 38.556 21.931 35.820 0.52 7.01 ? 262 GLN A CD 1 ATOM 1983 C CD B GLN A 1 262 ? 38.189 22.115 36.766 0.52 14.54 ? 262 GLN A CD 1 ATOM 1984 O OE1 A GLN A 1 262 ? 39.096 21.614 34.759 0.52 8.11 ? 262 GLN A OE1 1 ATOM 1985 O OE1 B GLN A 1 262 ? 37.079 21.963 37.294 0.52 14.99 ? 262 GLN A OE1 1 ATOM 1986 N NE2 A GLN A 1 262 ? 39.191 22.644 36.802 0.52 7.44 ? 262 GLN A NE2 1 ATOM 1987 N NE2 B GLN A 1 262 ? 39.140 22.854 37.338 0.52 20.84 ? 262 GLN A NE2 1 ATOM 1988 N N . ALA A 1 263 ? 36.278 18.818 38.168 1.00 10.33 ? 263 ALA A N 1 ATOM 1989 C CA . ALA A 1 263 ? 36.031 18.963 39.597 1.00 10.39 ? 263 ALA A CA 1 ATOM 1990 C C . ALA A 1 263 ? 36.857 17.944 40.373 1.00 9.14 ? 263 ALA A C 1 ATOM 1991 O O . ALA A 1 263 ? 37.350 18.267 41.460 1.00 9.59 ? 263 ALA A O 1 ATOM 1992 C CB . ALA A 1 263 ? 34.524 18.805 39.932 1.00 14.38 ? 263 ALA A CB 1 ATOM 1993 N N . PHE A 1 264 ? 36.964 16.719 39.862 1.00 8.85 ? 264 PHE A N 1 ATOM 1994 C CA . PHE A 1 264 ? 37.778 15.689 40.504 1.00 8.39 ? 264 PHE A CA 1 ATOM 1995 C C . PHE A 1 264 ? 39.235 16.109 40.531 1.00 7.38 ? 264 PHE A C 1 ATOM 1996 O O . PHE A 1 264 ? 39.921 15.969 41.564 1.00 7.95 ? 264 PHE A O 1 ATOM 1997 C CB . PHE A 1 264 ? 37.561 14.394 39.732 1.00 9.20 ? 264 PHE A CB 1 ATOM 1998 C CG . PHE A 1 264 ? 38.359 13.176 40.193 1.00 8.91 ? 264 PHE A CG 1 ATOM 1999 C CD1 . PHE A 1 264 ? 38.523 12.877 41.532 1.00 9.86 ? 264 PHE A CD1 1 ATOM 2000 C CD2 . PHE A 1 264 ? 38.878 12.331 39.240 1.00 10.23 ? 264 PHE A CD2 1 ATOM 2001 C CE1 . PHE A 1 264 ? 39.210 11.702 41.913 1.00 11.63 ? 264 PHE A CE1 1 ATOM 2002 C CE2 . PHE A 1 264 ? 39.565 11.184 39.622 1.00 11.64 ? 264 PHE A CE2 1 ATOM 2003 C CZ . PHE A 1 264 ? 39.721 10.867 40.947 1.00 11.64 ? 264 PHE A CZ 1 ATOM 2004 N N . MET A 1 265 ? 39.757 16.592 39.396 1.00 7.55 ? 265 MET A N 1 ATOM 2005 C CA . MET A 1 265 ? 41.159 17.070 39.343 1.00 7.29 ? 265 MET A CA 1 ATOM 2006 C C . MET A 1 265 ? 41.377 18.183 40.375 1.00 7.09 ? 265 MET A C 1 ATOM 2007 O O . MET A 1 265 ? 42.361 18.152 41.132 1.00 7.42 ? 265 MET A O 1 ATOM 2008 C CB . MET A 1 265 ? 41.489 17.534 37.909 1.00 7.52 ? 265 MET A CB 1 ATOM 2009 C CG . MET A 1 265 ? 42.935 18.018 37.757 1.00 7.72 ? 265 MET A CG 1 ATOM 2010 S SD . MET A 1 265 ? 43.263 18.991 36.279 1.00 8.18 ? 265 MET A SD 1 ATOM 2011 C CE . MET A 1 265 ? 42.331 20.437 36.668 1.00 10.73 ? 265 MET A CE 1 ATOM 2012 N N . ALA A 1 266 ? 40.496 19.196 40.392 1.00 7.74 ? 266 ALA A N 1 ATOM 2013 C CA . ALA A 1 266 ? 40.693 20.322 41.288 1.00 7.53 ? 266 ALA A CA 1 ATOM 2014 C C . ALA A 1 266 ? 40.623 19.882 42.749 1.00 7.41 ? 266 ALA A C 1 ATOM 2015 O O . ALA A 1 266 ? 41.436 20.331 43.584 1.00 7.79 ? 266 ALA A O 1 ATOM 2016 C CB . ALA A 1 266 ? 39.674 21.437 40.993 1.00 9.34 ? 266 ALA A CB 1 ATOM 2017 N N . ALA A 1 267 ? 39.664 19.029 43.105 1.00 7.74 ? 267 ALA A N 1 ATOM 2018 C CA . ALA A 1 267 ? 39.552 18.557 44.495 1.00 7.94 ? 267 ALA A CA 1 ATOM 2019 C C . ALA A 1 267 ? 40.755 17.765 44.877 1.00 7.68 ? 267 ALA A C 1 ATOM 2020 O O . ALA A 1 267 ? 41.238 17.824 46.029 1.00 7.79 ? 267 ALA A O 1 ATOM 2021 C CB . ALA A 1 267 ? 38.272 17.767 44.684 1.00 9.47 ? 267 ALA A CB 1 ATOM 2022 N N . SER A 1 268 ? 41.248 16.908 43.971 1.00 7.31 ? 268 SER A N 1 ATOM 2023 C CA . SER A 1 268 ? 42.392 16.062 44.236 1.00 7.19 ? 268 SER A CA 1 ATOM 2024 C C . SER A 1 268 ? 43.662 16.918 44.425 1.00 6.58 ? 268 SER A C 1 ATOM 2025 O O . SER A 1 268 ? 44.482 16.650 45.308 1.00 7.12 ? 268 SER A O 1 ATOM 2026 C CB . SER A 1 268 ? 42.584 15.043 43.106 1.00 7.50 ? 268 SER A CB 1 ATOM 2027 O OG . SER A 1 268 ? 41.430 14.202 43.017 1.00 7.81 ? 268 SER A OG 1 ATOM 2028 N N . PHE A 1 269 ? 43.835 17.914 43.578 1.00 6.88 ? 269 PHE A N 1 ATOM 2029 C CA . PHE A 1 269 ? 44.943 18.852 43.700 1.00 6.97 ? 269 PHE A CA 1 ATOM 2030 C C . PHE A 1 269 ? 44.858 19.567 45.070 1.00 6.72 ? 269 PHE A C 1 ATOM 2031 O O . PHE A 1 269 ? 45.876 19.682 45.761 1.00 7.21 ? 269 PHE A O 1 ATOM 2032 C CB . PHE A 1 269 ? 44.935 19.842 42.535 1.00 7.37 ? 269 PHE A CB 1 ATOM 2033 C CG . PHE A 1 269 ? 46.067 20.867 42.589 1.00 6.87 ? 269 PHE A CG 1 ATOM 2034 C CD1 . PHE A 1 269 ? 47.358 20.506 42.186 1.00 6.71 ? 269 PHE A CD1 1 ATOM 2035 C CD2 . PHE A 1 269 ? 45.843 22.155 43.012 1.00 9.12 ? 269 PHE A CD2 1 ATOM 2036 C CE1 . PHE A 1 269 ? 48.414 21.409 42.213 1.00 7.70 ? 269 PHE A CE1 1 ATOM 2037 C CE2 . PHE A 1 269 ? 46.873 23.067 43.017 1.00 10.47 ? 269 PHE A CE2 1 ATOM 2038 C CZ . PHE A 1 269 ? 48.172 22.695 42.622 1.00 10.13 ? 269 PHE A CZ 1 ATOM 2039 N N . ARG A 1 270 ? 43.675 20.037 45.453 1.00 6.98 ? 270 ARG A N 1 ATOM 2040 C CA . ARG A 1 270 ? 43.521 20.716 46.742 1.00 7.07 ? 270 ARG A CA 1 ATOM 2041 C C . ARG A 1 270 ? 43.941 19.811 47.881 1.00 6.89 ? 270 ARG A C 1 ATOM 2042 O O . ARG A 1 270 ? 44.661 20.229 48.807 1.00 7.57 ? 270 ARG A O 1 ATOM 2043 C CB . ARG A 1 270 ? 42.068 21.174 46.962 1.00 7.41 ? 270 ARG A CB 1 ATOM 2044 C CG . ARG A 1 270 ? 41.911 22.018 48.208 1.00 8.48 ? 270 ARG A CG 1 ATOM 2045 C CD . ARG A 1 270 ? 40.465 22.450 48.500 1.00 9.22 ? 270 ARG A CD 1 ATOM 2046 N NE . ARG A 1 270 ? 40.339 23.378 49.628 1.00 11.34 ? 270 ARG A NE 1 ATOM 2047 C CZ . ARG A 1 270 ? 40.318 23.186 50.923 1.00 12.16 ? 270 ARG A CZ 1 ATOM 2048 N NH1 . ARG A 1 270 ? 40.418 21.983 51.393 1.00 14.74 ? 270 ARG A NH1 1 ATOM 2049 N NH2 . ARG A 1 270 ? 40.175 24.178 51.797 1.00 14.82 ? 270 ARG A NH2 1 ATOM 2050 N N . ALA A 1 271 ? 43.508 18.540 47.865 1.00 6.92 ? 271 ALA A N 1 ATOM 2051 C CA . ALA A 1 271 ? 43.830 17.628 48.971 1.00 7.45 ? 271 ALA A CA 1 ATOM 2052 C C . ALA A 1 271 ? 45.321 17.394 49.034 1.00 7.36 ? 271 ALA A C 1 ATOM 2053 O O . ALA A 1 271 ? 45.921 17.381 50.138 1.00 8.67 ? 271 ALA A O 1 ATOM 2054 C CB . ALA A 1 271 ? 43.055 16.312 48.800 1.00 8.83 ? 271 ALA A CB 1 ATOM 2055 N N . ALA A 1 272 ? 45.985 17.173 47.892 1.00 6.92 ? 272 ALA A N 1 ATOM 2056 C CA . ALA A 1 272 ? 47.441 16.921 47.919 1.00 7.46 ? 272 ALA A CA 1 ATOM 2057 C C . ALA A 1 272 ? 48.211 18.172 48.306 1.00 6.71 ? 272 ALA A C 1 ATOM 2058 O O . ALA A 1 272 ? 49.194 18.082 49.039 1.00 7.63 ? 272 ALA A O 1 ATOM 2059 C CB . ALA A 1 272 ? 47.879 16.403 46.561 1.00 8.26 ? 272 ALA A CB 1 ATOM 2060 N N . MET A 1 273 ? 47.763 19.365 47.877 1.00 7.05 ? 273 MET A N 1 ATOM 2061 C CA . MET A 1 273 ? 48.392 20.611 48.272 1.00 7.21 ? 273 MET A CA 1 ATOM 2062 C C . MET A 1 273 ? 48.245 20.840 49.781 1.00 7.26 ? 273 MET A C 1 ATOM 2063 O O . MET A 1 273 ? 49.125 21.489 50.396 1.00 8.26 ? 273 MET A O 1 ATOM 2064 C CB . MET A 1 273 ? 47.799 21.808 47.517 1.00 7.87 ? 273 MET A CB 1 ATOM 2065 C CG . MET A 1 273 ? 48.314 21.927 46.081 1.00 9.14 ? 273 MET A CG 1 ATOM 2066 S SD . MET A 1 273 ? 50.089 22.199 45.913 1.00 10.00 ? 273 MET A SD 1 ATOM 2067 C CE . MET A 1 273 ? 50.255 23.774 46.711 1.00 22.31 ? 273 MET A CE 1 ATOM 2068 N N . SER A 1 274 ? 47.151 20.407 50.395 1.00 7.65 ? 274 SER A N 1 ATOM 2069 C CA . SER A 1 274 ? 46.965 20.568 51.840 1.00 8.05 ? 274 SER A CA 1 ATOM 2070 C C . SER A 1 274 ? 48.098 19.876 52.582 1.00 7.87 ? 274 SER A C 1 ATOM 2071 O O . SER A 1 274 ? 48.546 20.358 53.636 1.00 9.54 ? 274 SER A O 1 ATOM 2072 C CB A SER A 1 274 ? 45.620 19.954 52.258 0.52 9.49 ? 274 SER A CB 1 ATOM 2073 C CB B SER A 1 274 ? 45.566 20.099 52.239 0.52 10.92 ? 274 SER A CB 1 ATOM 2074 O OG A SER A 1 274 ? 45.450 19.863 53.675 0.52 8.36 ? 274 SER A OG 1 ATOM 2075 O OG B SER A 1 274 ? 45.448 18.701 52.269 0.52 19.67 ? 274 SER A OG 1 ATOM 2076 N N . LYS A 1 275 ? 48.525 18.712 52.065 1.00 7.28 ? 275 LYS A N 1 ATOM 2077 C CA . LYS A 1 275 ? 49.635 17.959 52.619 1.00 7.71 ? 275 LYS A CA 1 ATOM 2078 C C . LYS A 1 275 ? 50.992 18.596 52.246 1.00 7.35 ? 275 LYS A C 1 ATOM 2079 O O . LYS A 1 275 ? 51.882 18.753 53.101 1.00 8.44 ? 275 LYS A O 1 ATOM 2080 C CB A LYS A 1 275 ? 49.453 16.536 52.147 0.52 9.04 ? 275 LYS A CB 1 ATOM 2081 C CB B LYS A 1 275 ? 49.673 16.528 52.136 0.52 9.55 ? 275 LYS A CB 1 ATOM 2082 C CG A LYS A 1 275 ? 50.460 15.480 52.525 0.52 9.54 ? 275 LYS A CG 1 ATOM 2083 C CG B LYS A 1 275 ? 48.570 15.783 52.869 0.52 12.72 ? 275 LYS A CG 1 ATOM 2084 C CD A LYS A 1 275 ? 50.026 14.099 52.054 0.52 12.69 ? 275 LYS A CD 1 ATOM 2085 C CD B LYS A 1 275 ? 48.396 14.406 52.315 0.52 15.75 ? 275 LYS A CD 1 ATOM 2086 C CE A LYS A 1 275 ? 50.913 12.919 52.280 0.52 13.43 ? 275 LYS A CE 1 ATOM 2087 C CE B LYS A 1 275 ? 49.305 13.354 52.882 0.52 22.33 ? 275 LYS A CE 1 ATOM 2088 N NZ A LYS A 1 275 ? 50.096 11.646 52.120 0.52 14.27 ? 275 LYS A NZ 1 ATOM 2089 N NZ B LYS A 1 275 ? 48.560 12.049 52.665 0.52 24.01 ? 275 LYS A NZ 1 ATOM 2090 N N . LEU A 1 276 ? 51.177 18.999 50.985 1.00 6.58 ? 276 LEU A N 1 ATOM 2091 C CA . LEU A 1 276 ? 52.451 19.593 50.533 1.00 6.59 ? 276 LEU A CA 1 ATOM 2092 C C . LEU A 1 276 ? 52.785 20.844 51.334 1.00 6.64 ? 276 LEU A C 1 ATOM 2093 O O . LEU A 1 276 ? 53.937 21.060 51.740 1.00 7.07 ? 276 LEU A O 1 ATOM 2094 C CB . LEU A 1 276 ? 52.366 19.885 49.028 1.00 6.96 ? 276 LEU A CB 1 ATOM 2095 C CG . LEU A 1 276 ? 53.676 20.437 48.413 1.00 7.36 ? 276 LEU A CG 1 ATOM 2096 C CD1 . LEU A 1 276 ? 54.763 19.358 48.366 1.00 10.75 ? 276 LEU A CD1 1 ATOM 2097 C CD2 . LEU A 1 276 ? 53.421 20.869 46.961 1.00 14.46 ? 276 LEU A CD2 1 ATOM 2098 N N . ALA A 1 277 ? 51.778 21.722 51.548 1.00 6.66 ? 277 ALA A N 1 ATOM 2099 C CA . ALA A 1 277 ? 52.017 23.025 52.134 1.00 6.70 ? 277 ALA A CA 1 ATOM 2100 C C . ALA A 1 277 ? 52.469 22.964 53.579 1.00 7.33 ? 277 ALA A C 1 ATOM 2101 O O . ALA A 1 277 ? 52.916 23.994 54.117 1.00 8.07 ? 277 ALA A O 1 ATOM 2102 C CB . ALA A 1 277 ? 50.772 23.879 52.003 1.00 7.67 ? 277 ALA A CB 1 ATOM 2103 N N . VAL A 1 278 ? 52.287 21.828 54.242 1.00 7.37 ? 278 VAL A N 1 ATOM 2104 C CA . VAL A 1 278 ? 52.659 21.680 55.657 1.00 8.08 ? 278 VAL A CA 1 ATOM 2105 C C . VAL A 1 278 ? 53.806 20.722 55.850 1.00 7.41 ? 278 VAL A C 1 ATOM 2106 O O . VAL A 1 278 ? 54.105 20.378 57.007 1.00 7.97 ? 278 VAL A O 1 ATOM 2107 C CB . VAL A 1 278 ? 51.453 21.373 56.552 1.00 10.54 ? 278 VAL A CB 1 ATOM 2108 C CG1 . VAL A 1 278 ? 50.409 22.487 56.413 1.00 13.80 ? 278 VAL A CG1 1 ATOM 2109 C CG2 . VAL A 1 278 ? 50.891 20.040 56.282 1.00 11.09 ? 278 VAL A CG2 1 ATOM 2110 N N . LEU A 1 279 ? 54.499 20.279 54.791 1.00 7.02 ? 279 LEU A N 1 ATOM 2111 C CA . LEU A 1 279 ? 55.676 19.465 54.983 1.00 6.92 ? 279 LEU A CA 1 ATOM 2112 C C . LEU A 1 279 ? 56.659 20.202 55.889 1.00 6.77 ? 279 LEU A C 1 ATOM 2113 O O . LEU A 1 279 ? 56.908 21.389 55.747 1.00 7.32 ? 279 LEU A O 1 ATOM 2114 C CB . LEU A 1 279 ? 56.384 19.110 53.663 1.00 7.31 ? 279 LEU A CB 1 ATOM 2115 C CG . LEU A 1 279 ? 55.632 18.186 52.737 1.00 7.33 ? 279 LEU A CG 1 ATOM 2116 C CD1 . LEU A 1 279 ? 56.446 17.941 51.457 1.00 10.59 ? 279 LEU A CD1 1 ATOM 2117 C CD2 . LEU A 1 279 ? 55.324 16.857 53.409 1.00 11.16 ? 279 LEU A CD2 1 ATOM 2118 N N . GLY A 1 280 ? 57.213 19.464 56.861 1.00 7.24 ? 280 GLY A N 1 ATOM 2119 C CA . GLY A 1 280 ? 58.102 20.004 57.847 1.00 8.27 ? 280 GLY A CA 1 ATOM 2120 C C . GLY A 1 280 ? 57.388 20.500 59.112 1.00 7.87 ? 280 GLY A C 1 ATOM 2121 O O . GLY A 1 280 ? 58.075 21.018 60.010 1.00 9.88 ? 280 GLY A O 1 ATOM 2122 N N . HIS A 1 281 ? 56.076 20.365 59.183 1.00 7.35 ? 281 HIS A N 1 ATOM 2123 C CA . HIS A 1 281 ? 55.282 20.889 60.279 1.00 7.65 ? 281 HIS A CA 1 ATOM 2124 C C . HIS A 1 281 ? 54.203 19.883 60.680 1.00 7.98 ? 281 HIS A C 1 ATOM 2125 O O . HIS A 1 281 ? 53.774 19.049 59.893 1.00 9.61 ? 281 HIS A O 1 ATOM 2126 C CB . HIS A 1 281 ? 54.562 22.187 59.860 1.00 8.53 ? 281 HIS A CB 1 ATOM 2127 C CG . HIS A 1 281 ? 55.521 23.202 59.342 1.00 8.94 ? 281 HIS A CG 1 ATOM 2128 N ND1 . HIS A 1 281 ? 55.889 23.468 58.067 1.00 10.61 ? 281 HIS A ND1 1 ATOM 2129 C CD2 . HIS A 1 281 ? 56.239 23.999 60.145 1.00 9.17 ? 281 HIS A CD2 1 ATOM 2130 C CE1 . HIS A 1 281 ? 56.832 24.401 58.106 1.00 8.64 ? 281 HIS A CE1 1 ATOM 2131 N NE2 . HIS A 1 281 ? 57.055 24.735 59.349 1.00 12.50 ? 281 HIS A NE2 1 ATOM 2132 N N . ASN A 1 282 ? 53.735 19.997 61.932 1.00 9.29 ? 282 ASN A N 1 ATOM 2133 C CA . ASN A 1 282 ? 52.569 19.284 62.407 1.00 9.42 ? 282 ASN A CA 1 ATOM 2134 C C . ASN A 1 282 ? 51.356 20.195 62.138 1.00 9.10 ? 282 ASN A C 1 ATOM 2135 O O . ASN A 1 282 ? 51.256 21.313 62.642 1.00 9.89 ? 282 ASN A O 1 ATOM 2136 C CB . ASN A 1 282 ? 52.721 19.078 63.917 1.00 9.88 ? 282 ASN A CB 1 ATOM 2137 C CG . ASN A 1 282 ? 51.657 18.197 64.519 1.00 10.07 ? 282 ASN A CG 1 ATOM 2138 O OD1 . ASN A 1 282 ? 50.506 18.200 64.079 1.00 11.39 ? 282 ASN A OD1 1 ATOM 2139 N ND2 . ASN A 1 282 ? 52.021 17.392 65.543 1.00 12.11 ? 282 ASN A ND2 1 ATOM 2140 N N . ARG A 1 283 ? 50.417 19.734 61.291 1.00 10.01 ? 283 ARG A N 1 ATOM 2141 C CA . ARG A 1 283 ? 49.280 20.594 60.946 1.00 11.17 ? 283 ARG A CA 1 ATOM 2142 C C . ARG A 1 283 ? 48.436 20.987 62.179 1.00 9.44 ? 283 ARG A C 1 ATOM 2143 O O . ARG A 1 283 ? 47.762 21.978 62.141 1.00 10.92 ? 283 ARG A O 1 ATOM 2144 C CB . ARG A 1 283 ? 48.398 20.001 59.874 1.00 12.10 ? 283 ARG A CB 1 ATOM 2145 C CG . ARG A 1 283 ? 47.705 18.751 60.274 1.00 12.57 ? 283 ARG A CG 1 ATOM 2146 C CD . ARG A 1 283 ? 46.654 18.270 59.201 1.00 14.43 ? 283 ARG A CD 1 ATOM 2147 N NE . ARG A 1 283 ? 45.472 19.183 59.160 1.00 15.46 ? 283 ARG A NE 1 ATOM 2148 C CZ . ARG A 1 283 ? 45.040 20.002 58.209 1.00 13.94 ? 283 ARG A CZ 1 ATOM 2149 N NH1 . ARG A 1 283 ? 45.675 20.069 57.048 1.00 12.59 ? 283 ARG A NH1 1 ATOM 2150 N NH2 . ARG A 1 283 ? 43.974 20.802 58.309 1.00 18.19 ? 283 ARG A NH2 1 ATOM 2151 N N . ASN A 1 284 ? 48.539 20.182 63.266 1.00 9.56 ? 284 ASN A N 1 ATOM 2152 C CA . ASN A 1 284 ? 47.782 20.517 64.488 1.00 9.13 ? 284 ASN A CA 1 ATOM 2153 C C . ASN A 1 284 ? 48.357 21.736 65.212 1.00 9.11 ? 284 ASN A C 1 ATOM 2154 O O . ASN A 1 284 ? 47.735 22.215 66.167 1.00 10.40 ? 284 ASN A O 1 ATOM 2155 C CB . ASN A 1 284 ? 47.764 19.323 65.430 1.00 9.78 ? 284 ASN A CB 1 ATOM 2156 C CG . ASN A 1 284 ? 47.127 18.126 64.781 1.00 11.33 ? 284 ASN A CG 1 ATOM 2157 O OD1 . ASN A 1 284 ? 47.844 17.125 64.435 1.00 14.71 ? 284 ASN A OD1 1 ATOM 2158 N ND2 . ASN A 1 284 ? 45.879 18.136 64.573 1.00 12.81 ? 284 ASN A ND2 1 ATOM 2159 N N . SER A 1 285 ? 49.532 22.226 64.751 1.00 9.32 ? 285 SER A N 1 ATOM 2160 C CA . SER A 1 285 ? 50.203 23.375 65.325 1.00 9.61 ? 285 SER A CA 1 ATOM 2161 C C . SER A 1 285 ? 50.131 24.640 64.464 1.00 9.08 ? 285 SER A C 1 ATOM 2162 O O . SER A 1 285 ? 50.729 25.636 64.799 1.00 10.74 ? 285 SER A O 1 ATOM 2163 C CB . SER A 1 285 ? 51.656 23.005 65.602 1.00 11.95 ? 285 SER A CB 1 ATOM 2164 O OG . SER A 1 285 ? 51.666 22.013 66.663 1.00 16.19 ? 285 SER A OG 1 ATOM 2165 N N . LEU A 1 286 ? 49.337 24.596 63.382 1.00 8.17 ? 286 LEU A N 1 ATOM 2166 C CA . LEU A 1 286 ? 49.166 25.728 62.477 1.00 8.07 ? 286 LEU A CA 1 ATOM 2167 C C . LEU A 1 286 ? 47.702 26.173 62.529 1.00 8.30 ? 286 LEU A C 1 ATOM 2168 O O . LEU A 1 286 ? 46.805 25.333 62.593 1.00 10.56 ? 286 LEU A O 1 ATOM 2169 C CB . LEU A 1 286 ? 49.583 25.343 61.054 1.00 8.13 ? 286 LEU A CB 1 ATOM 2170 C CG . LEU A 1 286 ? 51.015 24.891 60.881 1.00 8.61 ? 286 LEU A CG 1 ATOM 2171 C CD1 . LEU A 1 286 ? 51.288 24.417 59.431 1.00 10.66 ? 286 LEU A CD1 1 ATOM 2172 C CD2 . LEU A 1 286 ? 52.012 25.958 61.247 1.00 10.49 ? 286 LEU A CD2 1 ATOM 2173 N N . ILE A 1 287 ? 47.462 27.478 62.517 1.00 9.03 ? 287 ILE A N 1 ATOM 2174 C CA . ILE A 1 287 ? 46.131 28.032 62.631 1.00 9.07 ? 287 ILE A CA 1 ATOM 2175 C C . ILE A 1 287 ? 45.455 28.105 61.262 1.00 8.53 ? 287 ILE A C 1 ATOM 2176 O O . ILE A 1 287 ? 46.116 28.311 60.243 1.00 10.15 ? 287 ILE A O 1 ATOM 2177 C CB . ILE A 1 287 ? 46.184 29.427 63.293 1.00 11.48 ? 287 ILE A CB 1 ATOM 2178 C CG1 . ILE A 1 287 ? 44.812 29.852 63.782 1.00 18.64 ? 287 ILE A CG1 1 ATOM 2179 C CG2 . ILE A 1 287 ? 46.934 30.445 62.462 1.00 13.02 ? 287 ILE A CG2 1 ATOM 2180 C CD1 . ILE A 1 287 ? 44.799 30.868 64.917 1.00 20.12 ? 287 ILE A CD1 1 ATOM 2181 N N . ASP A 1 288 ? 44.152 27.900 61.218 1.00 10.13 ? 288 ASP A N 1 ATOM 2182 C CA . ASP A 1 288 ? 43.437 27.907 59.934 1.00 10.30 ? 288 ASP A CA 1 ATOM 2183 C C . ASP A 1 288 ? 43.061 29.300 59.528 1.00 10.06 ? 288 ASP A C 1 ATOM 2184 O O . ASP A 1 288 ? 42.204 29.940 60.151 1.00 13.85 ? 288 ASP A O 1 ATOM 2185 C CB . ASP A 1 288 ? 42.212 26.998 60.071 1.00 11.74 ? 288 ASP A CB 1 ATOM 2186 C CG . ASP A 1 288 ? 41.602 26.677 58.723 1.00 14.29 ? 288 ASP A CG 1 ATOM 2187 O OD1 . ASP A 1 288 ? 40.729 25.798 58.638 1.00 19.18 ? 288 ASP A OD1 1 ATOM 2188 O OD2 . ASP A 1 288 ? 41.998 27.294 57.694 1.00 12.67 ? 288 ASP A OD2 1 ATOM 2189 N N . CYS A 1 289 ? 43.735 29.766 58.452 1.00 9.43 ? 289 CYS A N 1 ATOM 2190 C CA . CYS A 1 289 ? 43.519 31.077 57.848 1.00 9.92 ? 289 CYS A CA 1 ATOM 2191 C C . CYS A 1 289 ? 42.951 30.897 56.441 1.00 9.73 ? 289 CYS A C 1 ATOM 2192 O O . CYS A 1 289 ? 43.140 31.743 55.586 1.00 10.56 ? 289 CYS A O 1 ATOM 2193 C CB . CYS A 1 289 ? 44.764 31.953 57.840 1.00 10.55 ? 289 CYS A CB 1 ATOM 2194 S SG . CYS A 1 289 ? 45.265 32.522 59.461 1.00 12.64 ? 289 CYS A SG 1 ATOM 2195 N N . SER A 1 290 ? 42.207 29.829 56.194 1.00 9.50 ? 290 SER A N 1 ATOM 2196 C CA . SER A 1 290 ? 41.719 29.570 54.817 1.00 9.40 ? 290 SER A CA 1 ATOM 2197 C C . SER A 1 290 ? 40.785 30.650 54.333 1.00 9.56 ? 290 SER A C 1 ATOM 2198 O O . SER A 1 290 ? 40.658 30.837 53.119 1.00 10.14 ? 290 SER A O 1 ATOM 2199 C CB . SER A 1 290 ? 41.041 28.219 54.774 1.00 9.91 ? 290 SER A CB 1 ATOM 2200 O OG . SER A 1 290 ? 41.987 27.149 55.018 1.00 9.89 ? 290 SER A OG 1 ATOM 2201 N N . ASP A 1 291 ? 40.097 31.351 55.247 1.00 9.76 ? 291 ASP A N 1 ATOM 2202 C CA . ASP A 1 291 ? 39.117 32.358 54.833 1.00 11.13 ? 291 ASP A CA 1 ATOM 2203 C C . ASP A 1 291 ? 39.745 33.584 54.227 1.00 10.59 ? 291 ASP A C 1 ATOM 2204 O O . ASP A 1 291 ? 39.012 34.379 53.614 1.00 12.87 ? 291 ASP A O 1 ATOM 2205 C CB . ASP A 1 291 ? 38.272 32.748 56.068 1.00 13.46 ? 291 ASP A CB 1 ATOM 2206 C CG . ASP A 1 291 ? 39.019 33.242 57.289 1.00 16.80 ? 291 ASP A CG 1 ATOM 2207 O OD1 . ASP A 1 291 ? 38.655 34.281 57.922 1.00 22.49 ? 291 ASP A OD1 1 ATOM 2208 O OD2 . ASP A 1 291 ? 40.010 32.617 57.784 1.00 27.28 ? 291 ASP A OD2 1 ATOM 2209 N N . VAL A 1 292 ? 41.055 33.808 54.324 1.00 9.53 ? 292 VAL A N 1 ATOM 2210 C CA . VAL A 1 292 ? 41.690 34.950 53.709 1.00 9.99 ? 292 VAL A CA 1 ATOM 2211 C C . VAL A 1 292 ? 42.346 34.589 52.365 1.00 9.26 ? 292 VAL A C 1 ATOM 2212 O O . VAL A 1 292 ? 42.933 35.502 51.718 1.00 10.90 ? 292 VAL A O 1 ATOM 2213 C CB . VAL A 1 292 ? 42.652 35.700 54.651 1.00 11.50 ? 292 VAL A CB 1 ATOM 2214 C CG1 . VAL A 1 292 ? 41.894 36.266 55.875 1.00 16.54 ? 292 VAL A CG1 1 ATOM 2215 C CG2 . VAL A 1 292 ? 43.830 34.834 55.098 1.00 13.86 ? 292 VAL A CG2 1 ATOM 2216 N N . VAL A 1 293 ? 42.245 33.365 51.910 1.00 8.83 ? 293 VAL A N 1 ATOM 2217 C CA . VAL A 1 293 ? 42.618 33.028 50.520 1.00 8.91 ? 293 VAL A CA 1 ATOM 2218 C C . VAL A 1 293 ? 41.565 33.604 49.606 1.00 8.86 ? 293 VAL A C 1 ATOM 2219 O O . VAL A 1 293 ? 40.362 33.375 49.838 1.00 9.66 ? 293 VAL A O 1 ATOM 2220 C CB . VAL A 1 293 ? 42.729 31.512 50.310 1.00 9.30 ? 293 VAL A CB 1 ATOM 2221 C CG1 . VAL A 1 293 ? 43.073 31.166 48.859 1.00 9.66 ? 293 VAL A CG1 1 ATOM 2222 C CG2 . VAL A 1 293 ? 43.795 30.892 51.233 1.00 10.04 ? 293 VAL A CG2 1 ATOM 2223 N N . PRO A 1 294 ? 41.930 34.332 48.535 1.00 9.27 ? 294 PRO A N 1 ATOM 2224 C CA . PRO A 1 294 ? 40.909 34.826 47.623 1.00 10.24 ? 294 PRO A CA 1 ATOM 2225 C C . PRO A 1 294 ? 40.057 33.721 47.032 1.00 9.72 ? 294 PRO A C 1 ATOM 2226 O O . PRO A 1 294 ? 40.546 32.633 46.775 1.00 10.77 ? 294 PRO A O 1 ATOM 2227 C CB . PRO A 1 294 ? 41.752 35.537 46.539 1.00 12.06 ? 294 PRO A CB 1 ATOM 2228 C CG . PRO A 1 294 ? 43.033 35.917 47.210 1.00 13.20 ? 294 PRO A CG 1 ATOM 2229 C CD . PRO A 1 294 ? 43.262 34.803 48.192 1.00 10.75 ? 294 PRO A CD 1 ATOM 2230 N N . VAL A 1 295 ? 38.791 34.024 46.723 1.00 12.01 ? 295 VAL A N 1 ATOM 2231 C CA . VAL A 1 295 ? 37.939 33.109 46.021 1.00 11.98 ? 295 VAL A CA 1 ATOM 2232 C C . VAL A 1 295 ? 38.454 32.933 44.601 1.00 10.21 ? 295 VAL A C 1 ATOM 2233 O O . VAL A 1 295 ? 38.716 33.936 43.877 1.00 12.50 ? 295 VAL A O 1 ATOM 2234 C CB . VAL A 1 295 ? 36.481 33.617 46.030 1.00 15.80 ? 295 VAL A CB 1 ATOM 2235 C CG1 . VAL A 1 295 ? 35.585 32.770 45.162 1.00 17.45 ? 295 VAL A CG1 1 ATOM 2236 C CG2 . VAL A 1 295 ? 35.974 33.602 47.496 1.00 21.28 ? 295 VAL A CG2 1 ATOM 2237 N N . PRO A 1 296 ? 38.646 31.710 44.088 1.00 9.80 ? 296 PRO A N 1 ATOM 2238 C CA . PRO A 1 296 ? 39.241 31.515 42.763 1.00 9.29 ? 296 PRO A CA 1 ATOM 2239 C C . PRO A 1 296 ? 38.306 31.857 41.637 1.00 9.53 ? 296 PRO A C 1 ATOM 2240 O O . PRO A 1 296 ? 37.060 31.782 41.755 1.00 11.17 ? 296 PRO A O 1 ATOM 2241 C CB . PRO A 1 296 ? 39.570 30.038 42.724 1.00 9.82 ? 296 PRO A CB 1 ATOM 2242 C CG A PRO A 1 296 ? 38.569 29.421 43.659 0.52 8.66 ? 296 PRO A CG 1 ATOM 2243 C CG B PRO A 1 296 ? 39.627 29.634 44.100 0.52 14.78 ? 296 PRO A CG 1 ATOM 2244 C CD . PRO A 1 296 ? 38.498 30.426 44.787 1.00 12.35 ? 296 PRO A CD 1 ATOM 2245 N N . LYS A 1 297 ? 38.911 32.219 40.503 1.00 9.16 ? 297 LYS A N 1 ATOM 2246 C CA . LYS A 1 297 ? 38.129 32.372 39.269 1.00 9.58 ? 297 LYS A CA 1 ATOM 2247 C C . LYS A 1 297 ? 37.472 31.041 38.894 1.00 9.96 ? 297 LYS A C 1 ATOM 2248 O O . LYS A 1 297 ? 38.113 30.013 38.868 1.00 10.34 ? 297 LYS A O 1 ATOM 2249 C CB . LYS A 1 297 ? 39.055 32.814 38.134 1.00 10.54 ? 297 LYS A CB 1 ATOM 2250 C CG . LYS A 1 297 ? 39.667 34.176 38.274 1.00 11.52 ? 297 LYS A CG 1 ATOM 2251 C CD . LYS A 1 297 ? 40.401 34.502 36.964 1.00 11.88 ? 297 LYS A CD 1 ATOM 2252 C CE . LYS A 1 297 ? 41.257 35.752 37.035 1.00 12.60 ? 297 LYS A CE 1 ATOM 2253 N NZ . LYS A 1 297 ? 42.358 35.658 36.020 1.00 14.42 ? 297 LYS A NZ 1 ATOM 2254 N N . PRO A 1 298 ? 36.168 31.067 38.520 1.00 11.92 ? 298 PRO A N 1 ATOM 2255 C CA . PRO A 1 298 ? 35.478 29.818 38.111 1.00 12.83 ? 298 PRO A CA 1 ATOM 2256 C C . PRO A 1 298 ? 35.889 29.378 36.711 1.00 13.58 ? 298 PRO A C 1 ATOM 2257 O O . PRO A 1 298 ? 36.225 30.184 35.865 1.00 16.65 ? 298 PRO A O 1 ATOM 2258 C CB . PRO A 1 298 ? 34.003 30.225 38.172 1.00 17.00 ? 298 PRO A CB 1 ATOM 2259 C CG . PRO A 1 298 ? 34.048 31.669 37.870 1.00 22.38 ? 298 PRO A CG 1 ATOM 2260 C CD . PRO A 1 298 ? 35.276 32.237 38.528 1.00 16.71 ? 298 PRO A CD 1 ATOM 2261 N N . ALA A 1 299 ? 35.796 28.077 36.501 1.00 15.38 ? 299 ALA A N 1 ATOM 2262 C CA . ALA A 1 299 ? 35.902 27.585 35.154 1.00 15.40 ? 299 ALA A CA 1 ATOM 2263 C C . ALA A 1 299 ? 34.679 28.010 34.320 1.00 15.19 ? 299 ALA A C 1 ATOM 2264 O O . ALA A 1 299 ? 33.620 28.342 34.826 1.00 17.54 ? 299 ALA A O 1 ATOM 2265 C CB . ALA A 1 299 ? 35.976 26.070 35.239 1.00 18.88 ? 299 ALA A CB 1 ATOM 2266 N N . THR A 1 300 ? 34.777 27.917 32.991 1.00 13.84 ? 300 THR A N 1 ATOM 2267 C CA . THR A 1 300 ? 33.608 28.065 32.140 1.00 12.76 ? 300 THR A CA 1 ATOM 2268 C C . THR A 1 300 ? 32.679 26.830 32.240 1.00 12.13 ? 300 THR A C 1 ATOM 2269 O O . THR A 1 300 ? 31.480 26.912 31.893 1.00 15.91 ? 300 THR A O 1 ATOM 2270 C CB . THR A 1 300 ? 33.944 28.258 30.640 1.00 13.65 ? 300 THR A CB 1 ATOM 2271 O OG1 . THR A 1 300 ? 34.571 27.044 30.257 1.00 13.98 ? 300 THR A OG1 1 ATOM 2272 C CG2 . THR A 1 300 ? 34.857 29.448 30.492 1.00 15.62 ? 300 THR A CG2 1 ATOM 2273 N N . GLY A 1 301 ? 33.142 25.685 32.635 1.00 12.70 ? 301 GLY A N 1 ATOM 2274 C CA . GLY A 1 301 ? 32.374 24.477 32.689 1.00 13.08 ? 301 GLY A CA 1 ATOM 2275 C C . GLY A 1 301 ? 32.444 23.641 31.417 1.00 12.38 ? 301 GLY A C 1 ATOM 2276 O O . GLY A 1 301 ? 31.879 22.538 31.333 1.00 13.91 ? 301 GLY A O 1 ATOM 2277 N N . GLN A 1 302 ? 33.152 24.070 30.394 1.00 9.97 ? 302 GLN A N 1 ATOM 2278 C CA . GLN A 1 302 ? 33.221 23.307 29.157 1.00 9.75 ? 302 GLN A CA 1 ATOM 2279 C C . GLN A 1 302 ? 34.030 22.034 29.335 1.00 9.07 ? 302 GLN A C 1 ATOM 2280 O O . GLN A 1 302 ? 35.064 22.039 30.035 1.00 9.92 ? 302 GLN A O 1 ATOM 2281 C CB . GLN A 1 302 ? 33.909 24.157 28.070 1.00 11.75 ? 302 GLN A CB 1 ATOM 2282 C CG . GLN A 1 302 ? 33.206 25.299 27.501 1.00 16.49 ? 302 GLN A CG 1 ATOM 2283 C CD . GLN A 1 302 ? 33.869 25.796 26.180 1.00 16.79 ? 302 GLN A CD 1 ATOM 2284 O OE1 . GLN A 1 302 ? 34.977 26.213 26.261 1.00 21.70 ? 302 GLN A OE1 1 ATOM 2285 N NE2 . GLN A 1 302 ? 33.116 25.625 25.162 1.00 22.58 ? 302 GLN A NE2 1 ATOM 2286 N N . PRO A 1 303 ? 33.686 20.972 28.636 1.00 9.22 ? 303 PRO A N 1 ATOM 2287 C CA . PRO A 1 303 ? 34.521 19.761 28.596 1.00 8.99 ? 303 PRO A CA 1 ATOM 2288 C C . PRO A 1 303 ? 35.859 19.968 27.950 1.00 8.58 ? 303 PRO A C 1 ATOM 2289 O O . PRO A 1 303 ? 36.079 20.893 27.166 1.00 9.51 ? 303 PRO A O 1 ATOM 2290 C CB . PRO A 1 303 ? 33.701 18.772 27.770 1.00 10.59 ? 303 PRO A CB 1 ATOM 2291 C CG . PRO A 1 303 ? 32.348 19.296 27.730 1.00 22.29 ? 303 PRO A CG 1 ATOM 2292 C CD . PRO A 1 303 ? 32.415 20.792 27.885 1.00 14.90 ? 303 PRO A CD 1 ATOM 2293 N N . ALA A 1 304 ? 36.809 19.057 28.266 1.00 8.23 ? 304 ALA A N 1 ATOM 2294 C CA . ALA A 1 304 ? 38.050 18.973 27.529 1.00 8.42 ? 304 ALA A CA 1 ATOM 2295 C C . ALA A 1 304 ? 37.781 18.666 26.052 1.00 8.00 ? 304 ALA A C 1 ATOM 2296 O O . ALA A 1 304 ? 36.790 18.016 25.716 1.00 8.86 ? 304 ALA A O 1 ATOM 2297 C CB . ALA A 1 304 ? 38.946 17.870 28.094 1.00 9.04 ? 304 ALA A CB 1 ATOM 2298 N N . MET A 1 305 ? 38.683 19.153 25.176 1.00 8.45 ? 305 MET A N 1 ATOM 2299 C CA . MET A 1 305 ? 38.540 18.954 23.744 1.00 8.37 ? 305 MET A CA 1 ATOM 2300 C C . MET A 1 305 ? 39.914 18.658 23.124 1.00 8.19 ? 305 MET A C 1 ATOM 2301 O O . MET A 1 305 ? 40.940 19.210 23.582 1.00 9.39 ? 305 MET A O 1 ATOM 2302 C CB . MET A 1 305 ? 37.942 20.168 23.038 1.00 9.17 ? 305 MET A CB 1 ATOM 2303 C CG . MET A 1 305 ? 36.571 20.556 23.566 1.00 9.44 ? 305 MET A CG 1 ATOM 2304 S SD . MET A 1 305 ? 36.000 22.112 22.843 1.00 12.06 ? 305 MET A SD 1 ATOM 2305 C CE . MET A 1 305 ? 37.054 23.160 23.275 1.00 13.02 ? 305 MET A CE 1 ATOM 2306 N N . PHE A 1 306 ? 39.958 17.886 22.043 1.00 8.22 ? 306 PHE A N 1 ATOM 2307 C CA . PHE A 1 306 ? 41.173 17.746 21.267 1.00 8.51 ? 306 PHE A CA 1 ATOM 2308 C C . PHE A 1 306 ? 41.507 19.081 20.561 1.00 9.20 ? 306 PHE A C 1 ATOM 2309 O O . PHE A 1 306 ? 40.652 19.615 19.859 1.00 10.18 ? 306 PHE A O 1 ATOM 2310 C CB . PHE A 1 306 ? 41.085 16.662 20.187 1.00 8.95 ? 306 PHE A CB 1 ATOM 2311 C CG . PHE A 1 306 ? 40.986 15.267 20.780 1.00 8.85 ? 306 PHE A CG 1 ATOM 2312 C CD1 . PHE A 1 306 ? 39.772 14.684 21.089 1.00 9.84 ? 306 PHE A CD1 1 ATOM 2313 C CD2 . PHE A 1 306 ? 42.144 14.554 21.012 1.00 9.65 ? 306 PHE A CD2 1 ATOM 2314 C CE1 . PHE A 1 306 ? 39.730 13.395 21.611 1.00 11.63 ? 306 PHE A CE1 1 ATOM 2315 C CE2 . PHE A 1 306 ? 42.098 13.302 21.540 1.00 10.81 ? 306 PHE A CE2 1 ATOM 2316 C CZ . PHE A 1 306 ? 40.895 12.722 21.855 1.00 11.59 ? 306 PHE A CZ 1 ATOM 2317 N N . PRO A 1 307 ? 42.715 19.599 20.712 1.00 9.71 ? 307 PRO A N 1 ATOM 2318 C CA . PRO A 1 307 ? 43.115 20.785 19.929 1.00 10.34 ? 307 PRO A CA 1 ATOM 2319 C C . PRO A 1 307 ? 43.108 20.502 18.429 1.00 9.88 ? 307 PRO A C 1 ATOM 2320 O O . PRO A 1 307 ? 43.316 19.390 17.979 1.00 10.94 ? 307 PRO A O 1 ATOM 2321 C CB . PRO A 1 307 ? 44.527 21.064 20.403 1.00 12.82 ? 307 PRO A CB 1 ATOM 2322 C CG . PRO A 1 307 ? 44.576 20.539 21.787 1.00 15.53 ? 307 PRO A CG 1 ATOM 2323 C CD . PRO A 1 307 ? 43.776 19.241 21.665 1.00 11.63 ? 307 PRO A CD 1 ATOM 2324 N N . ALA A 1 308 ? 42.920 21.566 17.651 1.00 11.23 ? 308 ALA A N 1 ATOM 2325 C CA . ALA A 1 308 ? 43.020 21.425 16.167 1.00 12.77 ? 308 ALA A CA 1 ATOM 2326 C C . ALA A 1 308 ? 44.366 20.803 15.815 1.00 11.04 ? 308 ALA A C 1 ATOM 2327 O O . ALA A 1 308 ? 45.395 21.186 16.399 1.00 12.05 ? 308 ALA A O 1 ATOM 2328 C CB . ALA A 1 308 ? 42.786 22.774 15.492 1.00 14.14 ? 308 ALA A CB 1 ATOM 2329 N N . SER A 1 309 ? 44.440 19.908 14.866 1.00 12.73 ? 309 SER A N 1 ATOM 2330 C CA . SER A 1 309 ? 45.535 19.143 14.332 1.00 12.95 ? 309 SER A CA 1 ATOM 2331 C C . SER A 1 309 ? 45.669 17.809 15.082 1.00 12.54 ? 309 SER A C 1 ATOM 2332 O O . SER A 1 309 ? 46.551 17.001 14.681 1.00 15.47 ? 309 SER A O 1 ATOM 2333 C CB . SER A 1 309 ? 46.856 19.868 14.339 1.00 12.95 ? 309 SER A CB 1 ATOM 2334 O OG . SER A 1 309 ? 47.541 19.953 15.557 1.00 13.73 ? 309 SER A OG 1 ATOM 2335 N N . THR A 1 310 ? 44.848 17.540 16.099 1.00 11.80 ? 310 THR A N 1 ATOM 2336 C CA . THR A 1 310 ? 44.877 16.292 16.845 1.00 11.14 ? 310 THR A CA 1 ATOM 2337 C C . THR A 1 310 ? 43.496 15.652 16.858 1.00 11.66 ? 310 THR A C 1 ATOM 2338 O O . THR A 1 310 ? 42.477 16.257 16.554 1.00 14.64 ? 310 THR A O 1 ATOM 2339 C CB . THR A 1 310 ? 45.383 16.488 18.268 1.00 11.07 ? 310 THR A CB 1 ATOM 2340 O OG1 . THR A 1 310 ? 44.364 17.084 19.128 1.00 12.39 ? 310 THR A OG1 1 ATOM 2341 C CG2 . THR A 1 310 ? 46.606 17.341 18.286 1.00 17.50 ? 310 THR A CG2 1 ATOM 2342 N N . GLY A 1 311 ? 43.440 14.393 17.304 1.00 11.79 ? 311 GLY A N 1 ATOM 2343 C CA . GLY A 1 311 ? 42.179 13.688 17.492 1.00 11.41 ? 311 GLY A CA 1 ATOM 2344 C C . GLY A 1 311 ? 42.400 12.347 18.129 1.00 10.32 ? 311 GLY A C 1 ATOM 2345 O O . GLY A 1 311 ? 43.517 11.961 18.443 1.00 10.32 ? 311 GLY A O 1 ATOM 2346 N N . PRO A 1 312 ? 41.296 11.582 18.325 1.00 11.01 ? 312 PRO A N 1 ATOM 2347 C CA . PRO A 1 312 ? 41.414 10.278 18.996 1.00 11.75 ? 312 PRO A CA 1 ATOM 2348 C C . PRO A 1 312 ? 42.360 9.295 18.336 1.00 10.25 ? 312 PRO A C 1 ATOM 2349 O O . PRO A 1 312 ? 42.923 8.454 19.018 1.00 11.52 ? 312 PRO A O 1 ATOM 2350 C CB . PRO A 1 312 ? 39.957 9.762 18.955 1.00 14.31 ? 312 PRO A CB 1 ATOM 2351 C CG . PRO A 1 312 ? 39.117 10.950 18.730 1.00 19.78 ? 312 PRO A CG 1 ATOM 2352 C CD . PRO A 1 312 ? 39.930 11.980 18.048 1.00 12.73 ? 312 PRO A CD 1 ATOM 2353 N N . GLN A 1 313 ? 42.569 9.393 17.011 1.00 10.52 ? 313 GLN A N 1 ATOM 2354 C CA . GLN A 1 313 ? 43.492 8.525 16.312 1.00 11.54 ? 313 GLN A CA 1 ATOM 2355 C C . GLN A 1 313 ? 44.933 8.709 16.772 1.00 10.94 ? 313 GLN A C 1 ATOM 2356 O O . GLN A 1 313 ? 45.772 7.839 16.557 1.00 12.92 ? 313 GLN A O 1 ATOM 2357 C CB . GLN A 1 313 ? 43.439 8.735 14.801 1.00 14.21 ? 313 GLN A CB 1 ATOM 2358 C CG . GLN A 1 313 ? 43.977 10.050 14.280 1.00 16.84 ? 313 GLN A CG 1 ATOM 2359 C CD . GLN A 1 313 ? 43.007 11.209 14.304 1.00 16.55 ? 313 GLN A CD 1 ATOM 2360 O OE1 . GLN A 1 313 ? 42.048 11.277 15.069 1.00 14.48 ? 313 GLN A OE1 1 ATOM 2361 N NE2 . GLN A 1 313 ? 43.253 12.167 13.413 1.00 29.42 ? 313 GLN A NE2 1 ATOM 2362 N N . ASP A 1 314 ? 45.202 9.835 17.432 1.00 9.16 ? 314 ASP A N 1 ATOM 2363 C CA . ASP A 1 314 ? 46.548 10.169 17.900 1.00 9.68 ? 314 ASP A CA 1 ATOM 2364 C C . ASP A 1 314 ? 46.799 9.689 19.329 1.00 9.20 ? 314 ASP A C 1 ATOM 2365 O O . ASP A 1 314 ? 47.921 9.875 19.818 1.00 11.29 ? 314 ASP A O 1 ATOM 2366 C CB . ASP A 1 314 ? 46.768 11.661 17.784 1.00 10.97 ? 314 ASP A CB 1 ATOM 2367 C CG . ASP A 1 314 ? 46.643 12.211 16.404 1.00 12.85 ? 314 ASP A CG 1 ATOM 2368 O OD1 . ASP A 1 314 ? 46.124 13.325 16.244 1.00 17.76 ? 314 ASP A OD1 1 ATOM 2369 O OD2 . ASP A 1 314 ? 47.083 11.540 15.424 1.00 16.25 ? 314 ASP A OD2 1 ATOM 2370 N N . LEU A 1 315 ? 45.818 9.142 20.015 1.00 9.17 ? 315 LEU A N 1 ATOM 2371 C CA . LEU A 1 315 ? 46.007 8.733 21.405 1.00 9.66 ? 315 LEU A CA 1 ATOM 2372 C C . LEU A 1 315 ? 46.947 7.537 21.539 1.00 9.61 ? 315 LEU A C 1 ATOM 2373 O O . LEU A 1 315 ? 46.892 6.581 20.761 1.00 12.35 ? 315 LEU A O 1 ATOM 2374 C CB . LEU A 1 315 ? 44.652 8.332 22.062 1.00 10.58 ? 315 LEU A CB 1 ATOM 2375 C CG . LEU A 1 315 ? 43.691 9.505 22.283 1.00 11.49 ? 315 LEU A CG 1 ATOM 2376 C CD1 . LEU A 1 315 ? 42.285 8.973 22.527 1.00 12.93 ? 315 LEU A CD1 1 ATOM 2377 C CD2 . LEU A 1 315 ? 44.149 10.366 23.437 1.00 13.45 ? 315 LEU A CD2 1 ATOM 2378 N N . GLU A 1 316 ? 47.766 7.587 22.568 1.00 9.08 ? 316 GLU A N 1 ATOM 2379 C CA . GLU A 1 316 ? 48.658 6.502 22.996 1.00 9.17 ? 316 GLU A CA 1 ATOM 2380 C C . GLU A 1 316 ? 48.169 6.068 24.370 1.00 9.31 ? 316 GLU A C 1 ATOM 2381 O O . GLU A 1 316 ? 48.590 6.608 25.395 1.00 12.79 ? 316 GLU A O 1 ATOM 2382 C CB . GLU A 1 316 ? 50.109 7.005 23.021 1.00 9.93 ? 316 GLU A CB 1 ATOM 2383 C CG . GLU A 1 316 ? 50.587 7.498 21.691 1.00 13.24 ? 316 GLU A CG 1 ATOM 2384 C CD . GLU A 1 316 ? 52.026 7.917 21.649 1.00 14.52 ? 316 GLU A CD 1 ATOM 2385 O OE1 . GLU A 1 316 ? 52.590 8.717 22.462 1.00 13.31 ? 316 GLU A OE1 1 ATOM 2386 O OE2 . GLU A 1 316 ? 52.738 7.506 20.677 1.00 29.35 ? 316 GLU A OE2 1 ATOM 2387 N N . LEU A 1 317 ? 47.223 5.130 24.430 1.00 9.43 ? 317 LEU A N 1 ATOM 2388 C CA . LEU A 1 317 ? 46.529 4.798 25.677 1.00 9.26 ? 317 LEU A CA 1 ATOM 2389 C C . LEU A 1 317 ? 47.263 3.684 26.450 1.00 9.26 ? 317 LEU A C 1 ATOM 2390 O O . LEU A 1 317 ? 47.818 2.765 25.847 1.00 11.78 ? 317 LEU A O 1 ATOM 2391 C CB . LEU A 1 317 ? 45.093 4.414 25.386 1.00 11.20 ? 317 LEU A CB 1 ATOM 2392 C CG . LEU A 1 317 ? 44.231 5.514 24.802 1.00 12.07 ? 317 LEU A CG 1 ATOM 2393 C CD1 . LEU A 1 317 ? 42.814 4.995 24.631 1.00 16.86 ? 317 LEU A CD1 1 ATOM 2394 C CD2 . LEU A 1 317 ? 44.293 6.803 25.618 1.00 13.92 ? 317 LEU A CD2 1 ATOM 2395 N N . SER A 1 318 ? 47.165 3.744 27.764 1.00 9.69 ? 318 SER A N 1 ATOM 2396 C CA . SER A 1 318 ? 47.892 2.855 28.651 1.00 10.71 ? 318 SER A CA 1 ATOM 2397 C C . SER A 1 318 ? 47.082 2.383 29.876 1.00 11.33 ? 318 SER A C 1 ATOM 2398 O O . SER A 1 318 ? 47.678 1.871 30.825 1.00 15.47 ? 318 SER A O 1 ATOM 2399 C CB . SER A 1 318 ? 49.160 3.524 29.179 1.00 10.10 ? 318 SER A CB 1 ATOM 2400 O OG . SER A 1 318 ? 50.076 3.781 28.087 1.00 11.48 ? 318 SER A OG 1 ATOM 2401 N N . CYS A 1 319 ? 45.795 2.624 29.932 1.00 11.69 ? 319 CYS A N 1 ATOM 2402 C CA . CYS A 1 319 ? 44.952 2.193 31.063 1.00 11.99 ? 319 CYS A CA 1 ATOM 2403 C C . CYS A 1 319 ? 43.933 1.190 30.652 1.00 12.18 ? 319 CYS A C 1 ATOM 2404 O O . CYS A 1 319 ? 42.911 1.535 30.065 1.00 17.67 ? 319 CYS A O 1 ATOM 2405 C CB . CYS A 1 319 ? 44.261 3.410 31.712 1.00 12.46 ? 319 CYS A CB 1 ATOM 2406 S SG . CYS A 1 319 ? 43.160 2.879 33.076 1.00 14.85 ? 319 CYS A SG 1 ATOM 2407 N N . PRO A 1 320 ? 44.153 -0.105 30.896 1.00 12.89 ? 320 PRO A N 1 ATOM 2408 C CA . PRO A 1 320 ? 43.239 -1.122 30.360 1.00 13.53 ? 320 PRO A CA 1 ATOM 2409 C C . PRO A 1 320 ? 41.888 -1.132 31.007 1.00 12.89 ? 320 PRO A C 1 ATOM 2410 O O . PRO A 1 320 ? 40.936 -1.689 30.439 1.00 19.07 ? 320 PRO A O 1 ATOM 2411 C CB . PRO A 1 320 ? 43.968 -2.439 30.646 1.00 21.52 ? 320 PRO A CB 1 ATOM 2412 C CG . PRO A 1 320 ? 45.233 -2.100 31.263 1.00 28.70 ? 320 PRO A CG 1 ATOM 2413 C CD . PRO A 1 320 ? 45.290 -0.660 31.615 1.00 20.58 ? 320 PRO A CD 1 ATOM 2414 N N . SER A 1 321 ? 41.697 -0.596 32.149 1.00 15.92 ? 321 SER A N 1 ATOM 2415 C CA . SER A 1 321 ? 40.472 -0.832 32.891 1.00 18.47 ? 321 SER A CA 1 ATOM 2416 C C . SER A 1 321 ? 39.543 0.356 32.960 1.00 16.85 ? 321 SER A C 1 ATOM 2417 O O . SER A 1 321 ? 38.509 0.246 33.672 1.00 20.35 ? 321 SER A O 1 ATOM 2418 C CB . SER A 1 321 ? 40.865 -1.230 34.325 1.00 19.90 ? 321 SER A CB 1 ATOM 2419 O OG . SER A 1 321 ? 41.702 -0.182 34.856 1.00 30.66 ? 321 SER A OG 1 ATOM 2420 N N . GLU A 1 322 ? 39.832 1.438 32.251 1.00 14.35 ? 322 GLU A N 1 ATOM 2421 C CA . GLU A 1 322 ? 38.967 2.588 32.352 1.00 15.00 ? 322 GLU A CA 1 ATOM 2422 C C . GLU A 1 322 ? 38.702 3.136 30.936 1.00 13.96 ? 322 GLU A C 1 ATOM 2423 O O . GLU A 1 322 ? 39.633 3.313 30.109 1.00 15.26 ? 322 GLU A O 1 ATOM 2424 C CB . GLU A 1 322 ? 39.540 3.732 33.225 1.00 18.67 ? 322 GLU A CB 1 ATOM 2425 C CG . GLU A 1 322 ? 39.792 3.374 34.686 1.00 32.74 ? 322 GLU A CG 1 ATOM 2426 C CD . GLU A 1 322 ? 40.485 4.416 35.541 1.00 40.04 ? 322 GLU A CD 1 ATOM 2427 O OE1 . GLU A 1 322 ? 40.985 3.956 36.606 1.00 37.74 ? 322 GLU A OE1 1 ATOM 2428 O OE2 . GLU A 1 322 ? 40.543 5.641 35.147 1.00 57.67 ? 322 GLU A OE2 1 ATOM 2429 N N . ARG A 1 323 ? 37.443 3.394 30.641 1.00 14.36 ? 323 ARG A N 1 ATOM 2430 C CA . ARG A 1 323 ? 37.082 3.870 29.314 1.00 14.76 ? 323 ARG A CA 1 ATOM 2431 C C . ARG A 1 323 ? 37.522 5.334 29.081 1.00 13.83 ? 323 ARG A C 1 ATOM 2432 O O . ARG A 1 323 ? 37.204 6.196 29.872 1.00 14.77 ? 323 ARG A O 1 ATOM 2433 C CB . ARG A 1 323 ? 35.561 3.767 29.072 1.00 19.60 ? 323 ARG A CB 1 ATOM 2434 C CG . ARG A 1 323 ? 35.082 4.165 27.729 1.00 20.71 ? 323 ARG A CG 1 ATOM 2435 C CD . ARG A 1 323 ? 33.968 4.014 26.733 1.00 32.17 ? 323 ARG A CD 1 ATOM 2436 N NE . ARG A 1 323 ? 33.472 2.625 26.633 1.00 35.93 ? 323 ARG A NE 1 ATOM 2437 C CZ . ARG A 1 323 ? 32.545 2.054 27.394 1.00 38.54 ? 323 ARG A CZ 1 ATOM 2438 N NH1 . ARG A 1 323 ? 32.005 2.779 28.364 1.00 35.07 ? 323 ARG A NH1 1 ATOM 2439 N NH2 . ARG A 1 323 ? 32.150 0.839 27.298 1.00 47.40 ? 323 ARG A NH2 1 ATOM 2440 N N . PHE A 1 324 ? 38.212 5.630 28.024 1.00 16.12 ? 324 PHE A N 1 ATOM 2441 C CA . PHE A 1 324 ? 38.671 6.943 27.668 1.00 14.76 ? 324 PHE A CA 1 ATOM 2442 C C . PHE A 1 324 ? 37.421 7.731 27.210 1.00 15.12 ? 324 PHE A C 1 ATOM 2443 O O . PHE A 1 324 ? 36.680 7.182 26.397 1.00 21.71 ? 324 PHE A O 1 ATOM 2444 C CB . PHE A 1 324 ? 39.726 6.903 26.564 1.00 17.95 ? 324 PHE A CB 1 ATOM 2445 C CG . PHE A 1 324 ? 40.304 8.273 26.288 1.00 13.93 ? 324 PHE A CG 1 ATOM 2446 C CD1 . PHE A 1 324 ? 39.706 9.149 25.408 1.00 14.30 ? 324 PHE A CD1 1 ATOM 2447 C CD2 . PHE A 1 324 ? 41.440 8.679 26.958 1.00 16.14 ? 324 PHE A CD2 1 ATOM 2448 C CE1 . PHE A 1 324 ? 40.138 10.411 25.208 1.00 14.71 ? 324 PHE A CE1 1 ATOM 2449 C CE2 . PHE A 1 324 ? 41.951 9.990 26.752 1.00 16.16 ? 324 PHE A CE2 1 ATOM 2450 C CZ . PHE A 1 324 ? 41.262 10.790 25.855 1.00 16.29 ? 324 PHE A CZ 1 ATOM 2451 N N . PRO A 1 325 ? 37.210 8.963 27.676 1.00 12.85 ? 325 PRO A N 1 ATOM 2452 C CA . PRO A 1 325 ? 35.947 9.624 27.329 1.00 15.66 ? 325 PRO A CA 1 ATOM 2453 C C . PRO A 1 325 ? 35.834 10.044 25.884 1.00 14.07 ? 325 PRO A C 1 ATOM 2454 O O . PRO A 1 325 ? 36.807 10.191 25.164 1.00 15.98 ? 325 PRO A O 1 ATOM 2455 C CB . PRO A 1 325 ? 36.022 10.858 28.213 1.00 17.50 ? 325 PRO A CB 1 ATOM 2456 C CG . PRO A 1 325 ? 37.418 11.065 28.647 1.00 16.04 ? 325 PRO A CG 1 ATOM 2457 C CD . PRO A 1 325 ? 38.101 9.710 28.583 1.00 12.03 ? 325 PRO A CD 1 ATOM 2458 N N . THR A 1 326 ? 34.563 10.252 25.478 1.00 18.10 ? 326 THR A N 1 ATOM 2459 C CA . THR A 1 326 ? 34.244 10.800 24.162 1.00 19.30 ? 326 THR A CA 1 ATOM 2460 C C . THR A 1 326 ? 34.299 12.323 24.187 1.00 16.71 ? 326 THR A C 1 ATOM 2461 O O . THR A 1 326 ? 33.523 12.912 24.899 1.00 20.34 ? 326 THR A O 1 ATOM 2462 C CB . THR A 1 326 ? 32.848 10.304 23.748 1.00 26.73 ? 326 THR A CB 1 ATOM 2463 O OG1 . THR A 1 326 ? 32.856 8.892 23.821 1.00 35.42 ? 326 THR A OG1 1 ATOM 2464 C CG2 . THR A 1 326 ? 32.554 10.693 22.333 1.00 33.65 ? 326 THR A CG2 1 ATOM 2465 N N . LEU A 1 327 ? 35.222 12.902 23.452 1.00 13.33 ? 327 LEU A N 1 ATOM 2466 C CA . LEU A 1 327 ? 35.487 14.303 23.426 1.00 11.79 ? 327 LEU A CA 1 ATOM 2467 C C . LEU A 1 327 ? 35.406 14.846 21.983 1.00 11.65 ? 327 LEU A C 1 ATOM 2468 O O . LEU A 1 327 ? 35.693 14.098 21.032 1.00 12.87 ? 327 LEU A O 1 ATOM 2469 C CB . LEU A 1 327 ? 36.870 14.588 23.953 1.00 10.94 ? 327 LEU A CB 1 ATOM 2470 C CG . LEU A 1 327 ? 37.226 14.027 25.324 1.00 10.90 ? 327 LEU A CG 1 ATOM 2471 C CD1 . LEU A 1 327 ? 38.645 14.387 25.665 1.00 12.95 ? 327 LEU A CD1 1 ATOM 2472 C CD2 . LEU A 1 327 ? 36.302 14.560 26.390 1.00 13.62 ? 327 LEU A CD2 1 ATOM 2473 N N . THR A 1 328 ? 35.041 16.111 21.857 1.00 11.22 ? 328 THR A N 1 ATOM 2474 C CA . THR A 1 328 ? 35.041 16.781 20.584 1.00 10.74 ? 328 THR A CA 1 ATOM 2475 C C . THR A 1 328 ? 36.416 17.247 20.207 1.00 10.54 ? 328 THR A C 1 ATOM 2476 O O . THR A 1 328 ? 37.310 17.332 21.066 1.00 10.59 ? 328 THR A O 1 ATOM 2477 C CB . THR A 1 328 ? 34.053 17.956 20.559 1.00 11.19 ? 328 THR A CB 1 ATOM 2478 O OG1 . THR A 1 328 ? 34.524 18.921 21.447 1.00 14.01 ? 328 THR A OG1 1 ATOM 2479 C CG2 . THR A 1 328 ? 32.635 17.487 20.959 1.00 14.17 ? 328 THR A CG2 1 ATOM 2480 N N . THR A 1 329 ? 36.635 17.552 18.923 1.00 13.22 ? 329 THR A N 1 ATOM 2481 C CA . THR A 1 329 ? 37.831 18.119 18.365 1.00 13.99 ? 329 THR A CA 1 ATOM 2482 C C . THR A 1 329 ? 37.510 19.519 17.860 1.00 14.08 ? 329 THR A C 1 ATOM 2483 O O . THR A 1 329 ? 36.540 19.702 17.150 1.00 17.26 ? 329 THR A O 1 ATOM 2484 C CB . THR A 1 329 ? 38.343 17.271 17.208 1.00 17.06 ? 329 THR A CB 1 ATOM 2485 O OG1 . THR A 1 329 ? 38.654 15.955 17.681 1.00 19.30 ? 329 THR A OG1 1 ATOM 2486 C CG2 . THR A 1 329 ? 39.640 17.890 16.613 1.00 21.90 ? 329 THR A CG2 1 ATOM 2487 N N . GLN A 1 330 ? 38.353 20.474 18.237 1.00 13.83 ? 330 GLN A N 1 ATOM 2488 C CA . GLN A 1 330 ? 38.234 21.811 17.705 1.00 15.13 ? 330 GLN A CA 1 ATOM 2489 C C . GLN A 1 330 ? 38.460 21.839 16.225 1.00 14.78 ? 330 GLN A C 1 ATOM 2490 O O . GLN A 1 330 ? 39.414 21.178 15.749 1.00 15.18 ? 330 GLN A O 1 ATOM 2491 C CB . GLN A 1 330 ? 39.229 22.747 18.415 1.00 16.81 ? 330 GLN A CB 1 ATOM 2492 C CG . GLN A 1 330 ? 38.736 22.694 19.876 1.00 25.07 ? 330 GLN A CG 1 ATOM 2493 C CD . GLN A 1 330 ? 38.969 24.045 20.511 1.00 31.00 ? 330 GLN A CD 1 ATOM 2494 O OE1 . GLN A 1 330 ? 38.308 25.047 20.084 1.00 24.95 ? 330 GLN A OE1 1 ATOM 2495 N NE2 . GLN A 1 330 ? 39.882 24.000 21.456 1.00 32.95 ? 330 GLN A NE2 1 ATOM 2496 N N . PRO A 1 331 ? 37.652 22.548 15.445 1.00 14.78 ? 331 PRO A N 1 ATOM 2497 C CA . PRO A 1 331 ? 37.849 22.528 13.965 1.00 16.13 ? 331 PRO A CA 1 ATOM 2498 C C . PRO A 1 331 ? 39.169 23.147 13.535 1.00 15.74 ? 331 PRO A C 1 ATOM 2499 O O . PRO A 1 331 ? 39.724 24.028 14.194 1.00 16.56 ? 331 PRO A O 1 ATOM 2500 C CB . PRO A 1 331 ? 36.687 23.380 13.471 1.00 21.78 ? 331 PRO A CB 1 ATOM 2501 C CG . PRO A 1 331 ? 35.701 23.355 14.571 1.00 27.30 ? 331 PRO A CG 1 ATOM 2502 C CD . PRO A 1 331 ? 36.483 23.376 15.830 1.00 20.05 ? 331 PRO A CD 1 ATOM 2503 N N . GLY A 1 332 ? 39.667 22.735 12.365 1.00 16.46 ? 332 GLY A N 1 ATOM 2504 C CA . GLY A 1 332 ? 40.839 23.240 11.697 1.00 18.53 ? 332 GLY A CA 1 ATOM 2505 C C . GLY A 1 332 ? 41.828 22.165 11.333 1.00 19.91 ? 332 GLY A C 1 ATOM 2506 O O . GLY A 1 332 ? 42.008 21.193 12.025 1.00 25.77 ? 332 GLY A O 1 ATOM 2507 N N . ALA A 1 333 ? 42.535 22.383 10.208 1.00 27.47 ? 333 ALA A N 1 ATOM 2508 C CA . ALA A 1 333 ? 43.455 21.321 9.811 1.00 34.10 ? 333 ALA A CA 1 ATOM 2509 C C . ALA A 1 333 ? 44.816 21.474 10.458 1.00 22.85 ? 333 ALA A C 1 ATOM 2510 O O . ALA A 1 333 ? 45.535 20.485 10.552 1.00 40.39 ? 333 ALA A O 1 ATOM 2511 C CB . ALA A 1 333 ? 43.722 21.295 8.297 1.00 48.51 ? 333 ALA A CB 1 ATOM 2512 N N . SER A 1 334 ? 45.170 22.729 10.789 1.00 15.30 ? 334 SER A N 1 ATOM 2513 C CA . SER A 1 334 ? 46.513 22.888 11.276 1.00 15.15 ? 334 SER A CA 1 ATOM 2514 C C . SER A 1 334 ? 46.447 23.392 12.714 1.00 11.93 ? 334 SER A C 1 ATOM 2515 O O . SER A 1 334 ? 45.400 23.829 13.226 1.00 12.42 ? 334 SER A O 1 ATOM 2516 C CB . SER A 1 334 ? 47.315 23.754 10.328 1.00 21.05 ? 334 SER A CB 1 ATOM 2517 O OG . SER A 1 334 ? 46.940 25.083 10.450 1.00 22.42 ? 334 SER A OG 1 ATOM 2518 N N . GLN A 1 335 ? 47.601 23.286 13.367 1.00 11.64 ? 335 GLN A N 1 ATOM 2519 C CA . GLN A 1 335 ? 47.639 23.689 14.790 1.00 10.43 ? 335 GLN A CA 1 ATOM 2520 C C . GLN A 1 335 ? 47.473 25.179 14.944 1.00 10.39 ? 335 GLN A C 1 ATOM 2521 O O . GLN A 1 335 ? 48.048 25.965 14.184 1.00 11.50 ? 335 GLN A O 1 ATOM 2522 C CB . GLN A 1 335 ? 49.026 23.323 15.338 1.00 10.86 ? 335 GLN A CB 1 ATOM 2523 C CG . GLN A 1 335 ? 49.113 23.553 16.822 1.00 11.21 ? 335 GLN A CG 1 ATOM 2524 C CD . GLN A 1 335 ? 50.501 23.589 17.393 1.00 9.32 ? 335 GLN A CD 1 ATOM 2525 O OE1 . GLN A 1 335 ? 50.794 24.551 18.203 1.00 14.22 ? 335 GLN A OE1 1 ATOM 2526 N NE2 . GLN A 1 335 ? 51.291 22.667 17.037 1.00 7.81 ? 335 GLN A NE2 1 ATOM 2527 N N . SER A 1 336 ? 46.709 25.564 15.975 1.00 10.51 ? 336 SER A N 1 ATOM 2528 C CA . SER A 1 336 ? 46.643 26.964 16.392 1.00 11.00 ? 336 SER A CA 1 ATOM 2529 C C . SER A 1 336 ? 47.841 27.296 17.264 1.00 10.37 ? 336 SER A C 1 ATOM 2530 O O . SER A 1 336 ? 48.290 26.463 18.087 1.00 11.52 ? 336 SER A O 1 ATOM 2531 C CB . SER A 1 336 ? 45.303 27.108 17.236 1.00 13.43 ? 336 SER A CB 1 ATOM 2532 O OG . SER A 1 336 ? 44.219 26.939 16.366 1.00 15.01 ? 336 SER A OG 1 ATOM 2533 N N . LEU A 1 337 ? 48.294 28.516 17.184 1.00 10.07 ? 337 LEU A N 1 ATOM 2534 C CA . LEU A 1 337 ? 49.317 28.987 18.099 1.00 9.79 ? 337 LEU A CA 1 ATOM 2535 C C . LEU A 1 337 ? 48.713 29.049 19.515 1.00 9.77 ? 337 LEU A C 1 ATOM 2536 O O . LEU A 1 337 ? 47.549 29.373 19.744 1.00 12.31 ? 337 LEU A O 1 ATOM 2537 C CB . LEU A 1 337 ? 49.777 30.381 17.670 1.00 11.09 ? 337 LEU A CB 1 ATOM 2538 C CG . LEU A 1 337 ? 50.540 30.454 16.356 1.00 12.17 ? 337 LEU A CG 1 ATOM 2539 C CD1 . LEU A 1 337 ? 50.865 31.911 16.021 1.00 16.14 ? 337 LEU A CD1 1 ATOM 2540 C CD2 . LEU A 1 337 ? 51.805 29.617 16.372 1.00 13.94 ? 337 LEU A CD2 1 ATOM 2541 N N . ILE A 1 338 ? 49.602 28.761 20.495 1.00 8.55 ? 338 ILE A N 1 ATOM 2542 C CA . ILE A 1 338 ? 49.284 28.916 21.896 1.00 8.42 ? 338 ILE A CA 1 ATOM 2543 C C . ILE A 1 338 ? 49.766 30.305 22.290 1.00 8.38 ? 338 ILE A C 1 ATOM 2544 O O . ILE A 1 338 ? 50.959 30.622 22.248 1.00 8.82 ? 338 ILE A O 1 ATOM 2545 C CB . ILE A 1 338 ? 49.910 27.790 22.725 1.00 8.36 ? 338 ILE A CB 1 ATOM 2546 C CG1 . ILE A 1 338 ? 49.491 26.404 22.209 1.00 9.27 ? 338 ILE A CG1 1 ATOM 2547 C CG2 . ILE A 1 338 ? 49.570 27.986 24.195 1.00 8.77 ? 338 ILE A CG2 1 ATOM 2548 C CD1 . ILE A 1 338 ? 50.377 25.286 22.653 1.00 10.55 ? 338 ILE A CD1 1 ATOM 2549 N N . ALA A 1 339 ? 48.852 31.211 22.655 1.00 9.42 ? 339 ALA A N 1 ATOM 2550 C CA . ALA A 1 339 ? 49.202 32.566 22.940 1.00 10.09 ? 339 ALA A CA 1 ATOM 2551 C C . ALA A 1 339 ? 50.192 32.699 24.089 1.00 9.19 ? 339 ALA A C 1 ATOM 2552 O O . ALA A 1 339 ? 50.050 32.026 25.114 1.00 9.22 ? 339 ALA A O 1 ATOM 2553 C CB . ALA A 1 339 ? 47.964 33.397 23.261 1.00 14.03 ? 339 ALA A CB 1 ATOM 2554 N N . HIS A 1 340 ? 51.118 33.623 23.925 1.00 8.78 ? 340 HIS A N 1 ATOM 2555 C CA . HIS A 1 340 ? 52.087 33.939 24.950 1.00 8.41 ? 340 HIS A CA 1 ATOM 2556 C C . HIS A 1 340 ? 51.485 34.701 26.141 1.00 8.52 ? 340 HIS A C 1 ATOM 2557 O O . HIS A 1 340 ? 52.073 34.644 27.228 1.00 8.55 ? 340 HIS A O 1 ATOM 2558 C CB . HIS A 1 340 ? 53.195 34.783 24.329 1.00 8.91 ? 340 HIS A CB 1 ATOM 2559 C CG . HIS A 1 340 ? 54.329 35.087 25.218 1.00 8.79 ? 340 HIS A CG 1 ATOM 2560 N ND1 . HIS A 1 340 ? 55.148 34.079 25.737 1.00 9.44 ? 340 HIS A ND1 1 ATOM 2561 C CD2 . HIS A 1 340 ? 54.842 36.256 25.655 1.00 10.44 ? 340 HIS A CD2 1 ATOM 2562 C CE1 . HIS A 1 340 ? 56.101 34.671 26.468 1.00 10.70 ? 340 HIS A CE1 1 ATOM 2563 N NE2 . HIS A 1 340 ? 55.941 35.974 26.454 1.00 11.96 ? 340 HIS A NE2 1 ATOM 2564 N N . CYS A 1 341 ? 50.407 35.435 25.932 1.00 10.06 ? 341 CYS A N 1 ATOM 2565 C CA . CYS A 1 341 ? 49.764 36.242 26.956 1.00 11.27 ? 341 CYS A CA 1 ATOM 2566 C C . CYS A 1 341 ? 48.336 35.854 27.213 1.00 11.95 ? 341 CYS A C 1 ATOM 2567 O O . CYS A 1 341 ? 47.651 35.414 26.294 1.00 13.80 ? 341 CYS A O 1 ATOM 2568 C CB . CYS A 1 341 ? 49.782 37.717 26.477 1.00 12.34 ? 341 CYS A CB 1 ATOM 2569 S SG . CYS A 1 341 ? 51.460 38.342 26.202 1.00 14.12 ? 341 CYS A SG 1 ATOM 2570 N N . PRO A 1 342 ? 47.871 36.032 28.470 1.00 13.87 ? 342 PRO A N 1 ATOM 2571 C CA . PRO A 1 342 ? 46.454 35.681 28.805 1.00 16.35 ? 342 PRO A CA 1 ATOM 2572 C C . PRO A 1 342 ? 45.406 36.362 27.978 1.00 17.67 ? 342 PRO A C 1 ATOM 2573 O O . PRO A 1 342 ? 44.379 35.713 27.872 1.00 24.82 ? 342 PRO A O 1 ATOM 2574 C CB . PRO A 1 342 ? 46.313 36.103 30.262 1.00 21.59 ? 342 PRO A CB 1 ATOM 2575 C CG . PRO A 1 342 ? 47.692 36.101 30.802 1.00 21.03 ? 342 PRO A CG 1 ATOM 2576 C CD . PRO A 1 342 ? 48.624 36.419 29.651 1.00 15.99 ? 342 PRO A CD 1 ATOM 2577 N N . ASP A 1 343 ? 45.665 37.528 27.420 1.00 17.71 ? 343 ASP A N 1 ATOM 2578 C CA . ASP A 1 343 ? 44.679 38.180 26.551 1.00 21.61 ? 343 ASP A CA 1 ATOM 2579 C C . ASP A 1 343 ? 44.823 37.825 25.070 1.00 25.19 ? 343 ASP A C 1 ATOM 2580 O O . ASP A 1 343 ? 44.078 38.319 24.235 1.00 27.70 ? 343 ASP A O 1 ATOM 2581 C CB . ASP A 1 343 ? 44.689 39.673 26.631 1.00 27.96 ? 343 ASP A CB 1 ATOM 2582 C CG . ASP A 1 343 ? 45.991 40.356 26.294 1.00 37.18 ? 343 ASP A CG 1 ATOM 2583 O OD1 . ASP A 1 343 ? 45.941 41.616 26.349 1.00 44.47 ? 343 ASP A OD1 1 ATOM 2584 O OD2 . ASP A 1 343 ? 46.975 39.668 25.956 1.00 51.20 ? 343 ASP A OD2 1 ATOM 2585 N N . GLY A 1 344 ? 45.728 36.912 24.732 1.00 27.44 ? 344 GLY A N 1 ATOM 2586 C CA . GLY A 1 344 ? 45.837 36.311 23.412 1.00 27.64 ? 344 GLY A CA 1 ATOM 2587 C C . GLY A 1 344 ? 46.947 36.838 22.550 1.00 28.72 ? 344 GLY A C 1 ATOM 2588 O O . GLY A 1 344 ? 47.314 36.369 21.437 1.00 32.19 ? 344 GLY A O 1 ATOM 2589 N N . SER A 1 345 ? 47.511 37.894 23.152 1.00 29.23 ? 345 SER A N 1 ATOM 2590 C CA . SER A 1 345 ? 48.559 38.531 22.382 1.00 26.05 ? 345 SER A CA 1 ATOM 2591 C C . SER A 1 345 ? 49.919 37.868 22.629 1.00 19.55 ? 345 SER A C 1 ATOM 2592 O O . SER A 1 345 ? 50.024 36.792 23.248 1.00 17.88 ? 345 SER A O 1 ATOM 2593 C CB . SER A 1 345 ? 48.440 39.991 22.785 1.00 30.76 ? 345 SER A CB 1 ATOM 2594 O OG . SER A 1 345 ? 49.105 40.356 23.945 1.00 41.36 ? 345 SER A OG 1 ATOM 2595 N N . MET A 1 346 ? 50.802 38.675 22.046 1.00 28.53 ? 346 MET A N 1 ATOM 2596 C CA . MET A 1 346 ? 52.216 38.345 21.935 1.00 22.94 ? 346 MET A CA 1 ATOM 2597 C C . MET A 1 346 ? 53.133 38.918 22.967 1.00 21.27 ? 346 MET A C 1 ATOM 2598 O O . MET A 1 346 ? 54.198 38.454 23.294 1.00 20.76 ? 346 MET A O 1 ATOM 2599 C CB . MET A 1 346 ? 52.663 38.984 20.562 1.00 41.88 ? 346 MET A CB 1 ATOM 2600 C CG . MET A 1 346 ? 51.645 38.484 19.537 1.00 53.55 ? 346 MET A CG 1 ATOM 2601 S SD . MET A 1 346 ? 51.680 36.693 19.686 1.00 126.62 ? 346 MET A SD 1 ATOM 2602 C CE . MET A 1 346 ? 53.377 36.239 19.719 1.00 96.24 ? 346 MET A CE 1 ATOM 2603 N N . SER A 1 347 ? 52.710 40.084 23.490 1.00 24.21 ? 347 SER A N 1 ATOM 2604 C CA . SER A 1 347 ? 53.517 40.816 24.465 1.00 28.31 ? 347 SER A CA 1 ATOM 2605 C C . SER A 1 347 ? 52.881 41.417 25.706 1.00 24.39 ? 347 SER A C 1 ATOM 2606 O O . SER A 1 347 ? 51.896 42.133 25.724 1.00 34.20 ? 347 SER A O 1 ATOM 2607 C CB . SER A 1 347 ? 54.126 41.973 23.657 1.00 36.22 ? 347 SER A CB 1 ATOM 2608 O OG . SER A 1 347 ? 54.306 41.396 22.371 1.00 50.28 ? 347 SER A OG 1 ATOM 2609 N N . CYS A 1 348 ? 53.405 41.114 26.875 1.00 19.08 ? 348 CYS A N 1 ATOM 2610 C CA . CYS A 1 348 ? 52.894 41.294 28.201 1.00 17.59 ? 348 CYS A CA 1 ATOM 2611 C C . CYS A 1 348 ? 53.991 41.090 29.251 1.00 16.21 ? 348 CYS A C 1 ATOM 2612 O O . CYS A 1 348 ? 53.924 40.136 30.034 1.00 15.74 ? 348 CYS A O 1 ATOM 2613 C CB . CYS A 1 348 ? 51.769 40.265 28.528 1.00 17.00 ? 348 CYS A CB 1 ATOM 2614 S SG . CYS A 1 348 ? 52.132 38.547 28.127 1.00 15.21 ? 348 CYS A SG 1 ATOM 2615 N N . PRO A 1 349 ? 55.015 41.955 29.224 1.00 20.24 ? 349 PRO A N 1 ATOM 2616 C CA . PRO A 1 349 ? 56.146 41.713 30.140 1.00 18.45 ? 349 PRO A CA 1 ATOM 2617 C C . PRO A 1 349 ? 55.724 41.843 31.569 1.00 19.62 ? 349 PRO A C 1 ATOM 2618 O O . PRO A 1 349 ? 55.095 42.797 31.956 1.00 28.21 ? 349 PRO A O 1 ATOM 2619 C CB . PRO A 1 349 ? 57.219 42.776 29.723 1.00 23.50 ? 349 PRO A CB 1 ATOM 2620 C CG . PRO A 1 349 ? 56.323 43.856 29.218 1.00 30.85 ? 349 PRO A CG 1 ATOM 2621 C CD . PRO A 1 349 ? 55.265 43.123 28.396 1.00 26.87 ? 349 PRO A CD 1 ATOM 2622 N N . GLY A 1 350 ? 56.092 40.903 32.389 1.00 18.02 ? 350 GLY A N 1 ATOM 2623 C CA . GLY A 1 350 ? 55.755 40.891 33.781 1.00 18.91 ? 350 GLY A CA 1 ATOM 2624 C C . GLY A 1 350 ? 56.696 41.683 34.638 1.00 13.00 ? 350 GLY A C 1 ATOM 2625 O O . GLY A 1 350 ? 57.823 42.018 34.260 1.00 20.03 ? 350 GLY A O 1 ATOM 2626 N N . VAL A 1 351 ? 56.307 41.888 35.878 1.00 9.52 ? 351 VAL A N 1 ATOM 2627 C CA . VAL A 1 351 ? 57.156 42.549 36.835 1.00 8.49 ? 351 VAL A CA 1 ATOM 2628 C C . VAL A 1 351 ? 58.233 41.613 37.337 1.00 8.12 ? 351 VAL A C 1 ATOM 2629 O O . VAL A 1 351 ? 57.965 40.454 37.710 1.00 9.37 ? 351 VAL A O 1 ATOM 2630 C CB . VAL A 1 351 ? 56.273 43.073 37.994 1.00 9.33 ? 351 VAL A CB 1 ATOM 2631 C CG1 . VAL A 1 351 ? 57.127 43.684 39.104 1.00 10.91 ? 351 VAL A CG1 1 ATOM 2632 C CG2 . VAL A 1 351 ? 55.251 44.075 37.463 1.00 11.01 ? 351 VAL A CG2 1 ATOM 2633 N N . GLN A 1 352 ? 59.476 42.085 37.396 1.00 8.48 ? 352 GLN A N 1 ATOM 2634 C CA . GLN A 1 352 ? 60.574 41.288 37.930 1.00 8.95 ? 352 GLN A CA 1 ATOM 2635 C C . GLN A 1 352 ? 61.486 42.176 38.749 1.00 8.98 ? 352 GLN A C 1 ATOM 2636 O O . GLN A 1 352 ? 62.077 43.145 38.217 1.00 10.98 ? 352 GLN A O 1 ATOM 2637 C CB . GLN A 1 352 ? 61.367 40.581 36.798 1.00 10.00 ? 352 GLN A CB 1 ATOM 2638 C CG . GLN A 1 352 ? 62.463 39.661 37.368 1.00 11.34 ? 352 GLN A CG 1 ATOM 2639 C CD . GLN A 1 352 ? 61.967 38.558 38.255 1.00 10.76 ? 352 GLN A CD 1 ATOM 2640 O OE1 . GLN A 1 352 ? 62.345 38.421 39.469 1.00 12.37 ? 352 GLN A OE1 1 ATOM 2641 N NE2 . GLN A 1 352 ? 61.086 37.738 37.743 1.00 11.21 ? 352 GLN A NE2 1 ATOM 2642 N N . PHE A 1 353 ? 61.638 41.865 40.013 1.00 9.05 ? 353 PHE A N 1 ATOM 2643 C CA . PHE A 1 353 ? 62.578 42.520 40.879 1.00 9.25 ? 353 PHE A CA 1 ATOM 2644 C C . PHE A 1 353 ? 63.932 41.843 40.774 1.00 9.47 ? 353 PHE A C 1 ATOM 2645 O O . PHE A 1 353 ? 64.061 40.622 40.680 1.00 11.43 ? 353 PHE A O 1 ATOM 2646 C CB . PHE A 1 353 ? 62.105 42.495 42.340 1.00 9.07 ? 353 PHE A CB 1 ATOM 2647 C CG . PHE A 1 353 ? 60.842 43.274 42.586 1.00 9.33 ? 353 PHE A CG 1 ATOM 2648 C CD1 . PHE A 1 353 ? 60.810 44.655 42.455 1.00 14.22 ? 353 PHE A CD1 1 ATOM 2649 C CD2 . PHE A 1 353 ? 59.634 42.682 42.952 1.00 12.11 ? 353 PHE A CD2 1 ATOM 2650 C CE1 . PHE A 1 353 ? 59.645 45.374 42.648 1.00 13.62 ? 353 PHE A CE1 1 ATOM 2651 C CE2 . PHE A 1 353 ? 58.474 43.425 43.150 1.00 13.76 ? 353 PHE A CE2 1 ATOM 2652 C CZ . PHE A 1 353 ? 58.477 44.769 43.002 1.00 10.84 ? 353 PHE A CZ 1 ATOM 2653 N N . ASN A 1 354 ? 64.982 42.653 40.822 1.00 11.37 ? 354 ASN A N 1 ATOM 2654 C CA . ASN A 1 354 ? 66.355 42.173 41.062 1.00 11.76 ? 354 ASN A CA 1 ATOM 2655 C C . ASN A 1 354 ? 66.507 41.663 42.448 1.00 10.81 ? 354 ASN A C 1 ATOM 2656 O O . ASN A 1 354 ? 65.787 42.146 43.349 1.00 12.42 ? 354 ASN A O 1 ATOM 2657 C CB . ASN A 1 354 ? 67.394 43.281 40.755 1.00 17.53 ? 354 ASN A CB 1 ATOM 2658 C CG . ASN A 1 354 ? 67.385 43.657 39.267 1.00 28.64 ? 354 ASN A CG 1 ATOM 2659 O OD1 . ASN A 1 354 ? 67.596 44.832 38.913 1.00 57.22 ? 354 ASN A OD1 1 ATOM 2660 N ND2 . ASN A 1 354 ? 67.184 42.765 38.311 1.00 39.23 ? 354 ASN A ND2 1 ATOM 2661 N N . GLY A 1 355 ? 67.427 40.748 42.693 1.00 11.33 ? 355 GLY A N 1 ATOM 2662 C CA . GLY A 1 355 ? 67.660 40.286 44.032 1.00 10.95 ? 355 GLY A CA 1 ATOM 2663 C C . GLY A 1 355 ? 68.819 39.370 44.139 1.00 11.15 ? 355 GLY A C 1 ATOM 2664 O O . GLY A 1 355 ? 69.563 39.169 43.153 1.00 13.09 ? 355 GLY A O 1 ATOM 2665 N N . PRO A 1 356 ? 69.007 38.770 45.311 1.00 11.06 ? 356 PRO A N 1 ATOM 2666 C CA . PRO A 1 356 ? 70.215 37.990 45.596 1.00 11.57 ? 356 PRO A CA 1 ATOM 2667 C C . PRO A 1 356 ? 70.226 36.570 45.059 1.00 11.88 ? 356 PRO A C 1 ATOM 2668 O O . PRO A 1 356 ? 71.312 35.957 45.064 1.00 14.65 ? 356 PRO A O 1 ATOM 2669 C CB . PRO A 1 356 ? 70.245 37.937 47.132 1.00 13.29 ? 356 PRO A CB 1 ATOM 2670 C CG . PRO A 1 356 ? 68.775 38.030 47.554 1.00 12.58 ? 356 PRO A CG 1 ATOM 2671 C CD . PRO A 1 356 ? 68.175 38.957 46.520 1.00 11.62 ? 356 PRO A CD 1 ATOM 2672 N N . ALA A 1 357 ? 69.100 36.030 44.622 1.00 11.07 ? 357 ALA A N 1 ATOM 2673 C CA . ALA A 1 357 ? 69.085 34.685 44.094 1.00 11.99 ? 357 ALA A CA 1 ATOM 2674 C C . ALA A 1 357 ? 69.549 34.648 42.636 1.00 15.13 ? 357 ALA A C 1 ATOM 2675 O O . ALA A 1 357 ? 70.116 33.607 42.185 1.00 22.78 ? 357 ALA A O 1 ATOM 2676 C CB . ALA A 1 357 ? 67.719 34.040 44.236 1.00 12.47 ? 357 ALA A CB 1 ATOM 2677 O OXT . ALA A 1 357 ? 69.360 35.686 41.926 1.00 20.04 ? 357 ALA A OXT 1 HETATM 2678 C C1 . NAG B 2 . ? 61.987 36.687 58.772 1.00 10.49 ? 361 NAG A C1 1 HETATM 2679 C C2 . NAG B 2 . ? 61.533 38.021 59.305 1.00 10.51 ? 361 NAG A C2 1 HETATM 2680 C C3 . NAG B 2 . ? 61.954 39.159 58.393 1.00 11.48 ? 361 NAG A C3 1 HETATM 2681 C C4 . NAG B 2 . ? 63.436 39.076 58.077 1.00 11.49 ? 361 NAG A C4 1 HETATM 2682 C C5 . NAG B 2 . ? 63.774 37.690 57.551 1.00 12.32 ? 361 NAG A C5 1 HETATM 2683 C C6 . NAG B 2 . ? 65.207 37.514 57.216 1.00 15.98 ? 361 NAG A C6 1 HETATM 2684 C C7 . NAG B 2 . ? 59.447 37.657 60.612 1.00 10.67 ? 361 NAG A C7 1 HETATM 2685 C C8 . NAG B 2 . ? 57.949 37.521 60.580 1.00 11.93 ? 361 NAG A C8 1 HETATM 2686 N N2 . NAG B 2 . ? 60.084 37.993 59.475 1.00 11.14 ? 361 NAG A N2 1 HETATM 2687 O O3 . NAG B 2 . ? 61.626 40.375 59.045 1.00 13.30 ? 361 NAG A O3 1 HETATM 2688 O O4 . NAG B 2 . ? 63.813 39.966 57.010 1.00 12.75 ? 361 NAG A O4 1 HETATM 2689 O O5 . NAG B 2 . ? 63.402 36.702 58.543 1.00 11.24 ? 361 NAG A O5 1 HETATM 2690 O O6 . NAG B 2 . ? 65.999 37.614 58.394 1.00 18.59 ? 361 NAG A O6 1 HETATM 2691 O O7 . NAG B 2 . ? 60.056 37.438 61.673 1.00 12.58 ? 361 NAG A O7 1 HETATM 2692 C C1 . NAG C 2 . ? 64.286 41.219 57.417 1.00 13.45 ? 362 NAG A C1 1 HETATM 2693 C C2 . NAG C 2 . ? 65.167 41.793 56.287 1.00 15.01 ? 362 NAG A C2 1 HETATM 2694 C C3 . NAG C 2 . ? 65.587 43.215 56.653 1.00 17.06 ? 362 NAG A C3 1 HETATM 2695 C C4 . NAG C 2 . ? 64.422 44.106 57.113 1.00 16.86 ? 362 NAG A C4 1 HETATM 2696 C C5 . NAG C 2 . ? 63.539 43.374 58.134 1.00 15.30 ? 362 NAG A C5 1 HETATM 2697 C C6 . NAG C 2 . ? 62.228 44.121 58.455 1.00 16.72 ? 362 NAG A C6 1 HETATM 2698 C C7 . NAG C 2 . ? 66.696 40.342 54.969 1.00 15.03 ? 362 NAG A C7 1 HETATM 2699 C C8 . NAG C 2 . ? 67.922 39.474 54.982 1.00 18.42 ? 362 NAG A C8 1 HETATM 2700 N N2 . NAG C 2 . ? 66.322 40.920 56.101 1.00 15.55 ? 362 NAG A N2 1 HETATM 2701 O O3 . NAG C 2 . ? 66.232 43.798 55.536 1.00 20.34 ? 362 NAG A O3 1 HETATM 2702 O O4 . NAG C 2 . ? 64.925 45.289 57.752 1.00 20.45 ? 362 NAG A O4 1 HETATM 2703 O O5 . NAG C 2 . ? 63.160 42.110 57.609 1.00 14.14 ? 362 NAG A O5 1 HETATM 2704 O O6 . NAG C 2 . ? 61.658 43.458 59.544 1.00 17.43 ? 362 NAG A O6 1 HETATM 2705 O O7 . NAG C 2 . ? 66.013 40.494 53.952 1.00 15.04 ? 362 NAG A O7 1 HETATM 2706 C C1 . MAN D 3 . ? 43.713 28.028 15.668 1.00 16.61 ? 364 MAN A C1 1 HETATM 2707 C C2 . MAN D 3 . ? 42.289 27.680 15.213 1.00 19.10 ? 364 MAN A C2 1 HETATM 2708 C C3 . MAN D 3 . ? 42.268 26.472 14.254 1.00 18.89 ? 364 MAN A C3 1 HETATM 2709 C C4 . MAN D 3 . ? 43.221 26.740 13.101 1.00 17.88 ? 364 MAN A C4 1 HETATM 2710 C C5 . MAN D 3 . ? 44.589 27.140 13.622 1.00 15.97 ? 364 MAN A C5 1 HETATM 2711 C C6 . MAN D 3 . ? 45.509 27.582 12.501 1.00 19.22 ? 364 MAN A C6 1 HETATM 2712 O O2 . MAN D 3 . ? 41.761 28.799 14.528 1.00 22.96 ? 364 MAN A O2 1 HETATM 2713 O O3 . MAN D 3 . ? 40.979 26.270 13.749 1.00 24.09 ? 364 MAN A O3 1 HETATM 2714 O O4 . MAN D 3 . ? 43.314 25.525 12.338 1.00 21.60 ? 364 MAN A O4 1 HETATM 2715 O O5 . MAN D 3 . ? 44.522 28.258 14.463 1.00 16.32 ? 364 MAN A O5 1 HETATM 2716 O O6 A MAN D 3 . ? 46.746 27.966 13.054 0.52 24.22 ? 364 MAN A O6 1 HETATM 2717 O O6 B MAN D 3 . ? 44.984 28.594 11.663 0.52 35.59 ? 364 MAN A O6 1 HETATM 2718 CA CA . CA E 4 . ? 45.705 24.300 31.093 1.00 5.94 ? 371 CA A CA 1 HETATM 2719 CA CA . CA F 4 . ? 62.285 24.563 51.841 1.00 5.75 ? 372 CA A CA 1 HETATM 2720 MN MN . MN G 5 . ? 58.636 30.545 33.738 1.00 10.26 ? 381 MN A MN 1 HETATM 2721 C C1 . GOL H 6 . ? 57.480 45.802 46.651 1.00 37.19 ? 391 GOL A C1 1 HETATM 2722 O O1 . GOL H 6 . ? 58.779 46.250 47.056 1.00 46.58 ? 391 GOL A O1 1 HETATM 2723 C C2 . GOL H 6 . ? 56.324 46.336 47.515 1.00 8.02 ? 391 GOL A C2 1 HETATM 2724 O O2 . GOL H 6 . ? 56.553 47.502 48.308 1.00 19.84 ? 391 GOL A O2 1 HETATM 2725 C C3 . GOL H 6 . ? 55.043 45.689 47.259 1.00 24.78 ? 391 GOL A C3 1 HETATM 2726 O O3 . GOL H 6 . ? 54.518 46.782 46.626 1.00 17.89 ? 391 GOL A O3 1 HETATM 2727 C CHA . HEM I 7 . ? 57.606 24.029 35.550 1.00 6.96 ? 396 HEM A CHA 1 HETATM 2728 C CHB . HEM I 7 . ? 59.476 19.605 36.205 1.00 7.14 ? 396 HEM A CHB 1 HETATM 2729 C CHC . HEM I 7 . ? 56.215 18.758 39.718 1.00 7.18 ? 396 HEM A CHC 1 HETATM 2730 C CHD . HEM I 7 . ? 54.621 23.330 39.335 1.00 6.93 ? 396 HEM A CHD 1 HETATM 2731 C C1A . HEM I 7 . ? 58.444 22.911 35.442 1.00 6.83 ? 396 HEM A C1A 1 HETATM 2732 C C2A . HEM I 7 . ? 59.581 22.812 34.563 1.00 6.70 ? 396 HEM A C2A 1 HETATM 2733 C C3A . HEM I 7 . ? 60.116 21.575 34.765 1.00 6.93 ? 396 HEM A C3A 1 HETATM 2734 C C4A . HEM I 7 . ? 59.281 20.912 35.748 1.00 6.91 ? 396 HEM A C4A 1 HETATM 2735 C CMA . HEM I 7 . ? 61.329 20.943 34.103 1.00 8.01 ? 396 HEM A CMA 1 HETATM 2736 C CAA . HEM I 7 . ? 60.119 23.883 33.655 1.00 6.80 ? 396 HEM A CAA 1 HETATM 2737 C CBA . HEM I 7 . ? 61.127 24.809 34.351 1.00 8.19 ? 396 HEM A CBA 1 HETATM 2738 C CGA . HEM I 7 . ? 61.821 25.710 33.338 1.00 7.94 ? 396 HEM A CGA 1 HETATM 2739 O O1A . HEM I 7 . ? 62.638 25.185 32.506 1.00 9.71 ? 396 HEM A O1A 1 HETATM 2740 O O2A . HEM I 7 . ? 61.549 26.937 33.323 1.00 8.82 ? 396 HEM A O2A 1 HETATM 2741 C C1B . HEM I 7 . ? 58.713 18.949 37.189 1.00 6.71 ? 396 HEM A C1B 1 HETATM 2742 C C2B . HEM I 7 . ? 58.931 17.601 37.634 1.00 6.83 ? 396 HEM A C2B 1 HETATM 2743 C C3B . HEM I 7 . ? 57.942 17.331 38.576 1.00 7.07 ? 396 HEM A C3B 1 HETATM 2744 C C4B . HEM I 7 . ? 57.180 18.556 38.774 1.00 7.17 ? 396 HEM A C4B 1 HETATM 2745 C CMB . HEM I 7 . ? 60.036 16.704 37.113 1.00 7.94 ? 396 HEM A CMB 1 HETATM 2746 C CAB . HEM I 7 . ? 57.673 16.112 39.284 1.00 8.50 ? 396 HEM A CAB 1 HETATM 2747 C CBB A HEM I 7 . ? 57.951 14.877 38.850 0.52 7.42 ? 396 HEM A CBB 1 HETATM 2748 C CBB B HEM I 7 . ? 56.467 15.398 39.641 0.52 12.06 ? 396 HEM A CBB 1 HETATM 2749 C C1C . HEM I 7 . ? 55.583 19.982 39.997 1.00 7.10 ? 396 HEM A C1C 1 HETATM 2750 C C2C . HEM I 7 . ? 54.608 20.184 41.070 1.00 6.89 ? 396 HEM A C2C 1 HETATM 2751 C C3C . HEM I 7 . ? 54.207 21.495 41.022 1.00 6.69 ? 396 HEM A C3C 1 HETATM 2752 C C4C . HEM I 7 . ? 54.883 22.060 39.857 1.00 6.86 ? 396 HEM A C4C 1 HETATM 2753 C CMC . HEM I 7 . ? 54.289 19.139 42.105 1.00 8.23 ? 396 HEM A CMC 1 HETATM 2754 C CAC . HEM I 7 . ? 53.343 22.217 41.909 1.00 7.95 ? 396 HEM A CAC 1 HETATM 2755 C CBC . HEM I 7 . ? 52.294 21.793 42.625 1.00 9.11 ? 396 HEM A CBC 1 HETATM 2756 C C1D . HEM I 7 . ? 55.203 23.869 38.173 1.00 6.83 ? 396 HEM A C1D 1 HETATM 2757 C C2D . HEM I 7 . ? 54.853 25.146 37.611 1.00 6.24 ? 396 HEM A C2D 1 HETATM 2758 C C3D . HEM I 7 . ? 55.699 25.350 36.567 1.00 6.49 ? 396 HEM A C3D 1 HETATM 2759 C C4D . HEM I 7 . ? 56.568 24.205 36.460 1.00 6.76 ? 396 HEM A C4D 1 HETATM 2760 C CMD . HEM I 7 . ? 53.662 25.974 38.020 1.00 6.89 ? 396 HEM A CMD 1 HETATM 2761 C CAD . HEM I 7 . ? 55.692 26.500 35.588 1.00 6.62 ? 396 HEM A CAD 1 HETATM 2762 C CBD . HEM I 7 . ? 56.547 27.693 35.904 1.00 7.95 ? 396 HEM A CBD 1 HETATM 2763 C CGD . HEM I 7 . ? 56.385 28.817 34.852 1.00 8.86 ? 396 HEM A CGD 1 HETATM 2764 O O1D . HEM I 7 . ? 57.029 29.889 34.974 1.00 11.77 ? 396 HEM A O1D 1 HETATM 2765 O O2D . HEM I 7 . ? 55.559 28.646 33.951 1.00 9.51 ? 396 HEM A O2D 1 HETATM 2766 N NA . HEM I 7 . ? 58.260 21.750 36.170 1.00 7.07 ? 396 HEM A NA 1 HETATM 2767 N NB . HEM I 7 . ? 57.659 19.518 37.876 1.00 6.75 ? 396 HEM A NB 1 HETATM 2768 N NC . HEM I 7 . ? 55.692 21.116 39.214 1.00 7.04 ? 396 HEM A NC 1 HETATM 2769 N ND . HEM I 7 . ? 56.232 23.286 37.449 1.00 7.15 ? 396 HEM A ND 1 HETATM 2770 FE FE . HEM I 7 . ? 56.788 21.315 37.521 1.00 6.20 ? 396 HEM A FE 1 HETATM 2771 O O . HOH J 8 . ? 54.972 17.700 29.920 1.00 8.23 ? 1001 HOH A O 1 HETATM 2772 O O . HOH J 8 . ? 62.731 26.113 27.390 1.00 10.60 ? 1002 HOH A O 1 HETATM 2773 O O . HOH J 8 . ? 53.245 18.603 27.813 1.00 6.88 ? 1003 HOH A O 1 HETATM 2774 O O . HOH J 8 . ? 48.659 25.660 54.304 1.00 8.07 ? 1004 HOH A O 1 HETATM 2775 O O . HOH J 8 . ? 47.268 7.380 30.959 1.00 8.72 ? 1005 HOH A O 1 HETATM 2776 O O . HOH J 8 . ? 44.948 29.337 28.875 1.00 11.30 ? 1006 HOH A O 1 HETATM 2777 O O . HOH J 8 . ? 51.781 9.837 24.895 1.00 10.21 ? 1007 HOH A O 1 HETATM 2778 O O . HOH J 8 . ? 51.991 30.395 26.466 1.00 8.37 ? 1008 HOH A O 1 HETATM 2779 O O . HOH J 8 . ? 61.821 6.853 32.469 1.00 14.51 ? 1009 HOH A O 1 HETATM 2780 O O . HOH J 8 . ? 68.183 20.156 44.084 1.00 9.56 ? 1010 HOH A O 1 HETATM 2781 O O . HOH J 8 . ? 44.715 22.892 49.883 1.00 9.69 ? 1011 HOH A O 1 HETATM 2782 O O . HOH J 8 . ? 60.228 30.782 57.215 1.00 7.99 ? 1012 HOH A O 1 HETATM 2783 O O . HOH J 8 . ? 52.241 27.966 19.824 1.00 12.43 ? 1013 HOH A O 1 HETATM 2784 O O . HOH J 8 . ? 59.018 27.134 58.751 1.00 9.63 ? 1014 HOH A O 1 HETATM 2785 O O . HOH J 8 . ? 35.109 15.665 37.763 1.00 12.13 ? 1015 HOH A O 1 HETATM 2786 O O . HOH J 8 . ? 66.341 22.556 46.740 1.00 8.00 ? 1016 HOH A O 1 HETATM 2787 O O . HOH J 8 . ? 53.041 29.852 23.872 1.00 8.53 ? 1017 HOH A O 1 HETATM 2788 O O . HOH J 8 . ? 43.824 28.898 45.915 1.00 9.10 ? 1018 HOH A O 1 HETATM 2789 O O . HOH J 8 . ? 55.024 31.415 25.096 1.00 9.54 ? 1019 HOH A O 1 HETATM 2790 O O . HOH J 8 . ? 37.752 27.758 40.279 1.00 12.35 ? 1020 HOH A O 1 HETATM 2791 O O . HOH J 8 . ? 57.366 35.511 40.147 1.00 11.82 ? 1021 HOH A O 1 HETATM 2792 O O . HOH J 8 . ? 57.012 2.547 42.901 1.00 9.78 ? 1022 HOH A O 1 HETATM 2793 O O . HOH J 8 . ? 72.089 23.283 55.638 1.00 9.60 ? 1023 HOH A O 1 HETATM 2794 O O . HOH J 8 . ? 50.299 24.475 30.774 1.00 8.98 ? 1024 HOH A O 1 HETATM 2795 O O . HOH J 8 . ? 50.704 36.465 36.911 1.00 12.13 ? 1025 HOH A O 1 HETATM 2796 O O . HOH J 8 . ? 52.371 17.035 25.683 1.00 7.87 ? 1026 HOH A O 1 HETATM 2797 O O . HOH J 8 . ? 67.344 19.774 46.697 1.00 7.62 ? 1027 HOH A O 1 HETATM 2798 O O . HOH J 8 . ? 52.990 41.907 58.056 1.00 12.83 ? 1028 HOH A O 1 HETATM 2799 O O . HOH J 8 . ? 50.150 26.733 49.364 1.00 8.40 ? 1029 HOH A O 1 HETATM 2800 O O . HOH J 8 . ? 45.193 13.985 45.767 1.00 9.46 ? 1030 HOH A O 1 HETATM 2801 O O . HOH J 8 . ? 67.452 17.645 42.899 1.00 8.83 ? 1031 HOH A O 1 HETATM 2802 O O . HOH J 8 . ? 45.937 5.940 29.012 1.00 11.52 ? 1032 HOH A O 1 HETATM 2803 O O . HOH J 8 . ? 58.676 10.190 23.141 1.00 24.53 ? 1033 HOH A O 1 HETATM 2804 O O . HOH J 8 . ? 45.678 23.600 17.805 1.00 13.96 ? 1034 HOH A O 1 HETATM 2805 O O . HOH J 8 . ? 70.130 27.019 39.363 1.00 13.04 ? 1035 HOH A O 1 HETATM 2806 O O . HOH J 8 . ? 56.460 11.960 23.183 1.00 9.67 ? 1036 HOH A O 1 HETATM 2807 O O . HOH J 8 . ? 34.442 17.522 24.353 1.00 12.86 ? 1037 HOH A O 1 HETATM 2808 O O . HOH J 8 . ? 52.254 36.391 31.649 1.00 12.79 ? 1038 HOH A O 1 HETATM 2809 O O . HOH J 8 . ? 53.669 40.793 36.628 1.00 12.14 ? 1039 HOH A O 1 HETATM 2810 O O . HOH J 8 . ? 57.676 30.375 31.700 1.00 11.66 ? 1040 HOH A O 1 HETATM 2811 O O . HOH J 8 . ? 47.904 5.962 44.949 1.00 13.15 ? 1041 HOH A O 1 HETATM 2812 O O . HOH J 8 . ? 47.596 23.050 54.183 1.00 9.95 ? 1042 HOH A O 1 HETATM 2813 O O . HOH J 8 . ? 71.748 25.898 56.596 1.00 9.27 ? 1043 HOH A O 1 HETATM 2814 O O . HOH J 8 . ? 70.585 19.708 41.245 1.00 9.85 ? 1044 HOH A O 1 HETATM 2815 O O . HOH J 8 . ? 58.070 26.876 19.200 1.00 20.38 ? 1045 HOH A O 1 HETATM 2816 O O . HOH J 8 . ? 67.628 41.005 49.560 1.00 27.63 ? 1046 HOH A O 1 HETATM 2817 O O . HOH J 8 . ? 56.165 38.039 54.530 1.00 10.55 ? 1047 HOH A O 1 HETATM 2818 O O . HOH J 8 . ? 39.634 18.344 48.218 1.00 11.63 ? 1048 HOH A O 1 HETATM 2819 O O . HOH J 8 . ? 53.693 17.374 57.565 1.00 15.20 ? 1049 HOH A O 1 HETATM 2820 O O . HOH J 8 . ? 56.842 16.019 35.519 1.00 11.37 ? 1050 HOH A O 1 HETATM 2821 O O . HOH J 8 . ? 44.291 43.512 57.941 1.00 26.84 ? 1051 HOH A O 1 HETATM 2822 O O . HOH J 8 . ? 62.568 21.712 21.936 1.00 10.63 ? 1052 HOH A O 1 HETATM 2823 O O . HOH J 8 . ? 64.593 16.465 55.911 1.00 9.82 ? 1053 HOH A O 1 HETATM 2824 O O . HOH J 8 . ? 59.878 -0.594 36.125 1.00 14.98 ? 1054 HOH A O 1 HETATM 2825 O O . HOH J 8 . ? 71.791 21.093 57.333 1.00 12.20 ? 1055 HOH A O 1 HETATM 2826 O O . HOH J 8 . ? 67.660 29.841 39.806 1.00 11.64 ? 1056 HOH A O 1 HETATM 2827 O O . HOH J 8 . ? 59.618 33.436 30.193 1.00 34.35 ? 1057 HOH A O 1 HETATM 2828 O O . HOH J 8 . ? 62.748 12.474 41.457 1.00 15.07 ? 1058 HOH A O 1 HETATM 2829 O O . HOH J 8 . ? 39.475 29.867 58.739 1.00 33.65 ? 1059 HOH A O 1 HETATM 2830 O O . HOH J 8 . ? 50.881 42.299 56.133 1.00 12.17 ? 1060 HOH A O 1 HETATM 2831 O O . HOH J 8 . ? 64.077 20.324 38.110 1.00 23.67 ? 1061 HOH A O 1 HETATM 2832 O O . HOH J 8 . ? 64.475 45.513 40.924 1.00 19.51 ? 1062 HOH A O 1 HETATM 2833 O O . HOH J 8 . ? 58.236 5.816 29.442 1.00 19.01 ? 1063 HOH A O 1 HETATM 2834 O O . HOH J 8 . ? 64.610 40.840 45.517 1.00 12.52 ? 1064 HOH A O 1 HETATM 2835 O O . HOH J 8 . ? 55.246 21.624 63.794 1.00 16.59 ? 1065 HOH A O 1 HETATM 2836 O O . HOH J 8 . ? 73.114 22.587 51.067 1.00 17.43 ? 1066 HOH A O 1 HETATM 2837 O O . HOH J 8 . ? 37.294 11.016 22.466 1.00 16.66 ? 1067 HOH A O 1 HETATM 2838 O O . HOH J 8 . ? 71.921 32.385 51.028 1.00 11.06 ? 1068 HOH A O 1 HETATM 2839 O O . HOH J 8 . ? 75.354 21.205 44.743 1.00 16.88 ? 1069 HOH A O 1 HETATM 2840 O O . HOH J 8 . ? 67.012 36.626 52.438 1.00 19.63 ? 1070 HOH A O 1 HETATM 2841 O O . HOH J 8 . ? 58.144 33.236 24.366 1.00 15.71 ? 1071 HOH A O 1 HETATM 2842 O O . HOH J 8 . ? 48.538 26.723 51.698 1.00 9.39 ? 1072 HOH A O 1 HETATM 2843 O O . HOH J 8 . ? 56.125 24.113 62.890 1.00 21.96 ? 1073 HOH A O 1 HETATM 2844 O O . HOH J 8 . ? 64.434 23.363 33.515 1.00 15.57 ? 1074 HOH A O 1 HETATM 2845 O O . HOH J 8 . ? 58.002 14.634 56.002 1.00 12.34 ? 1075 HOH A O 1 HETATM 2846 O O . HOH J 8 . ? 64.919 13.292 43.271 1.00 30.60 ? 1076 HOH A O 1 HETATM 2847 O O . HOH J 8 . ? 62.890 35.942 62.346 1.00 20.38 ? 1077 HOH A O 1 HETATM 2848 O O . HOH J 8 . ? 36.314 20.471 42.783 1.00 17.30 ? 1078 HOH A O 1 HETATM 2849 O O . HOH J 8 . ? 42.328 18.039 14.121 1.00 24.49 ? 1079 HOH A O 1 HETATM 2850 O O . HOH J 8 . ? 69.576 17.050 41.236 1.00 14.33 ? 1080 HOH A O 1 HETATM 2851 O O . HOH J 8 . ? 37.985 23.459 32.925 1.00 17.57 ? 1081 HOH A O 1 HETATM 2852 O O . HOH J 8 . ? 47.083 24.648 19.940 1.00 18.50 ? 1082 HOH A O 1 HETATM 2853 O O . HOH J 8 . ? 66.077 8.174 36.924 1.00 12.36 ? 1083 HOH A O 1 HETATM 2854 O O . HOH J 8 . ? 56.740 27.318 52.412 1.00 7.68 ? 1084 HOH A O 1 HETATM 2855 O O . HOH J 8 . ? 63.303 24.299 49.675 1.00 6.52 ? 1085 HOH A O 1 HETATM 2856 O O . HOH J 8 . ? 42.566 10.206 38.440 1.00 9.34 ? 1086 HOH A O 1 HETATM 2857 O O . HOH J 8 . ? 65.352 23.610 54.478 1.00 7.20 ? 1087 HOH A O 1 HETATM 2858 O O . HOH J 8 . ? 54.855 8.045 45.734 1.00 10.00 ? 1088 HOH A O 1 HETATM 2859 O O . HOH J 8 . ? 58.686 18.855 23.544 1.00 7.86 ? 1089 HOH A O 1 HETATM 2860 O O . HOH J 8 . ? 58.789 38.539 57.049 1.00 11.49 ? 1090 HOH A O 1 HETATM 2861 O O . HOH J 8 . ? 68.344 27.706 49.884 1.00 10.15 ? 1091 HOH A O 1 HETATM 2862 O O . HOH J 8 . ? 54.658 3.159 44.414 1.00 11.79 ? 1092 HOH A O 1 HETATM 2863 O O . HOH J 8 . ? 54.704 10.307 21.600 1.00 13.32 ? 1093 HOH A O 1 HETATM 2864 O O . HOH J 8 . ? 40.663 28.652 51.341 1.00 11.26 ? 1094 HOH A O 1 HETATM 2865 O O . HOH J 8 . ? 47.149 23.862 50.661 1.00 10.35 ? 1095 HOH A O 1 HETATM 2866 O O . HOH J 8 . ? 38.701 29.980 31.265 1.00 16.89 ? 1096 HOH A O 1 HETATM 2867 O O . HOH J 8 . ? 39.192 20.185 31.254 1.00 9.67 ? 1097 HOH A O 1 HETATM 2868 O O . HOH J 8 . ? 50.948 17.419 59.694 1.00 18.44 ? 1098 HOH A O 1 HETATM 2869 O O . HOH J 8 . ? 52.171 17.026 55.287 1.00 11.84 ? 1099 HOH A O 1 HETATM 2870 O O . HOH J 8 . ? 65.487 29.504 27.045 1.00 22.10 ? 1100 HOH A O 1 HETATM 2871 O O . HOH J 8 . ? 42.568 26.476 63.710 1.00 20.48 ? 1101 HOH A O 1 HETATM 2872 O O . HOH J 8 . ? 45.811 29.139 24.860 1.00 31.12 ? 1102 HOH A O 1 HETATM 2873 O O . HOH J 8 . ? 39.787 7.236 32.682 1.00 37.87 ? 1103 HOH A O 1 HETATM 2874 O O . HOH J 8 . ? 53.583 35.683 29.266 1.00 11.12 ? 1104 HOH A O 1 HETATM 2875 O O . HOH J 8 . ? 57.489 45.783 35.080 1.00 12.80 ? 1105 HOH A O 1 HETATM 2876 O O . HOH J 8 . ? 52.446 47.637 43.030 1.00 18.02 ? 1106 HOH A O 1 HETATM 2877 O O . HOH J 8 . ? 59.946 8.014 28.976 1.00 18.72 ? 1107 HOH A O 1 HETATM 2878 O O . HOH J 8 . ? 59.199 28.357 33.614 1.00 12.22 ? 1108 HOH A O 1 HETATM 2879 O O . HOH J 8 . ? 57.871 4.827 45.987 1.00 14.62 ? 1109 HOH A O 1 HETATM 2880 O O . HOH J 8 . ? 64.469 10.398 47.851 1.00 17.61 ? 1110 HOH A O 1 HETATM 2881 O O . HOH J 8 . ? 36.165 9.540 20.251 1.00 18.24 ? 1111 HOH A O 1 HETATM 2882 O O . HOH J 8 . ? 68.612 23.783 23.595 1.00 19.62 ? 1112 HOH A O 1 HETATM 2883 O O . HOH J 8 . ? 56.647 16.674 57.271 1.00 12.92 ? 1113 HOH A O 1 HETATM 2884 O O . HOH J 8 . ? 43.855 10.100 48.232 1.00 29.66 ? 1114 HOH A O 1 HETATM 2885 O O . HOH J 8 . ? 44.003 2.639 21.712 1.00 18.64 ? 1115 HOH A O 1 HETATM 2886 O O . HOH J 8 . ? 65.116 20.815 59.402 1.00 14.41 ? 1116 HOH A O 1 HETATM 2887 O O . HOH J 8 . ? 65.107 34.479 59.655 1.00 15.16 ? 1117 HOH A O 1 HETATM 2888 O O . HOH J 8 . ? 43.302 3.443 28.280 1.00 15.88 ? 1118 HOH A O 1 HETATM 2889 O O . HOH J 8 . ? 40.923 27.947 28.217 1.00 21.11 ? 1119 HOH A O 1 HETATM 2890 O O . HOH J 8 . ? 55.267 37.780 29.277 1.00 20.88 ? 1120 HOH A O 1 HETATM 2891 O O . HOH J 8 . ? 66.065 14.481 41.045 1.00 12.75 ? 1121 HOH A O 1 HETATM 2892 O O . HOH J 8 . ? 55.116 32.489 61.915 1.00 15.76 ? 1122 HOH A O 1 HETATM 2893 O O . HOH J 8 . ? 60.588 11.811 21.776 1.00 15.54 ? 1123 HOH A O 1 HETATM 2894 O O . HOH J 8 . ? 36.509 20.505 31.832 1.00 14.15 ? 1124 HOH A O 1 HETATM 2895 O O . HOH J 8 . ? 53.716 33.987 59.922 1.00 10.17 ? 1125 HOH A O 1 HETATM 2896 O O . HOH J 8 . ? 61.635 7.322 53.405 1.00 23.37 ? 1126 HOH A O 1 HETATM 2897 O O . HOH J 8 . ? 63.666 22.821 52.534 1.00 6.56 ? 1127 HOH A O 1 HETATM 2898 O O . HOH J 8 . ? 40.204 13.059 45.257 1.00 18.71 ? 1128 HOH A O 1 HETATM 2899 O O . HOH J 8 . ? 58.069 4.056 33.341 1.00 9.78 ? 1129 HOH A O 1 HETATM 2900 O O . HOH J 8 . ? 36.189 27.349 27.997 1.00 25.72 ? 1130 HOH A O 1 HETATM 2901 O O . HOH J 8 . ? 56.378 4.956 31.359 1.00 10.15 ? 1131 HOH A O 1 HETATM 2902 O O A HOH J 8 . ? 47.274 4.329 37.939 1.00 12.92 ? 1132 HOH A O 1 HETATM 2903 O O . HOH J 8 . ? 48.274 1.076 39.366 1.00 14.12 ? 1133 HOH A O 1 HETATM 2904 O O . HOH J 8 . ? 46.802 30.351 15.533 1.00 24.84 ? 1134 HOH A O 1 HETATM 2905 O O . HOH J 8 . ? 72.718 26.561 59.152 1.00 9.94 ? 1135 HOH A O 1 HETATM 2906 O O . HOH J 8 . ? 64.543 23.482 59.853 1.00 13.69 ? 1136 HOH A O 1 HETATM 2907 O O . HOH J 8 . ? 58.699 22.166 39.012 1.00 29.16 ? 1137 HOH A O 1 HETATM 2908 O O . HOH J 8 . ? 43.923 5.856 19.023 1.00 23.10 ? 1138 HOH A O 1 HETATM 2909 O O . HOH J 8 . ? 53.505 19.691 67.645 1.00 29.70 ? 1139 HOH A O 1 HETATM 2910 O O . HOH J 8 . ? 45.512 -3.390 34.662 1.00 29.72 ? 1140 HOH A O 1 HETATM 2911 O O . HOH J 8 . ? 53.480 38.110 35.186 1.00 12.71 ? 1141 HOH A O 1 HETATM 2912 O O . HOH J 8 . ? 42.415 38.210 51.595 1.00 24.89 ? 1142 HOH A O 1 HETATM 2913 O O . HOH J 8 . ? 38.758 34.371 32.660 1.00 24.71 ? 1143 HOH A O 1 HETATM 2914 O O . HOH J 8 . ? 46.351 3.936 21.901 1.00 16.60 ? 1144 HOH A O 1 HETATM 2915 O O . HOH J 8 . ? 31.529 27.757 36.291 1.00 33.88 ? 1145 HOH A O 1 HETATM 2916 O O . HOH J 8 . ? 41.140 19.453 50.248 1.00 14.20 ? 1146 HOH A O 1 HETATM 2917 O O . HOH J 8 . ? 49.681 13.427 17.345 1.00 25.02 ? 1147 HOH A O 1 HETATM 2918 O O . HOH J 8 . ? 70.094 14.415 48.729 1.00 39.42 ? 1148 HOH A O 1 HETATM 2919 O O . HOH J 8 . ? 57.863 38.070 31.446 1.00 36.52 ? 1149 HOH A O 1 HETATM 2920 O O . HOH J 8 . ? 67.389 20.298 29.274 1.00 20.40 ? 1150 HOH A O 1 HETATM 2921 O O . HOH J 8 . ? 61.337 26.164 59.935 1.00 17.43 ? 1151 HOH A O 1 HETATM 2922 O O . HOH J 8 . ? 41.615 36.527 40.509 1.00 17.58 ? 1152 HOH A O 1 HETATM 2923 O O . HOH J 8 . ? 69.213 15.016 60.325 1.00 28.23 ? 1153 HOH A O 1 HETATM 2924 O O . HOH J 8 . ? 50.046 29.127 65.016 1.00 26.56 ? 1154 HOH A O 1 HETATM 2925 O O . HOH J 8 . ? 68.297 13.798 38.456 1.00 19.92 ? 1155 HOH A O 1 HETATM 2926 O O . HOH J 8 . ? 30.870 1.605 33.773 1.00 23.86 ? 1156 HOH A O 1 HETATM 2927 O O . HOH J 8 . ? 64.562 18.077 22.983 1.00 16.94 ? 1157 HOH A O 1 HETATM 2928 O O . HOH J 8 . ? 44.773 35.110 33.885 1.00 18.71 ? 1158 HOH A O 1 HETATM 2929 O O . HOH J 8 . ? 45.391 13.561 49.965 1.00 31.53 ? 1159 HOH A O 1 HETATM 2930 O O . HOH J 8 . ? 60.484 3.752 36.501 1.00 9.34 ? 1160 HOH A O 1 HETATM 2931 O O . HOH J 8 . ? 50.980 26.188 67.539 1.00 13.15 ? 1161 HOH A O 1 HETATM 2932 O O . HOH J 8 . ? 61.121 31.415 39.470 1.00 16.96 ? 1162 HOH A O 1 HETATM 2933 O O . HOH J 8 . ? 59.289 4.047 43.716 1.00 10.38 ? 1163 HOH A O 1 HETATM 2934 O O . HOH J 8 . ? 60.556 21.948 59.335 1.00 17.15 ? 1164 HOH A O 1 HETATM 2935 O O . HOH J 8 . ? 43.395 33.132 32.530 1.00 12.38 ? 1165 HOH A O 1 HETATM 2936 O O . HOH J 8 . ? 64.151 8.989 44.576 1.00 12.47 ? 1166 HOH A O 1 HETATM 2937 O O . HOH J 8 . ? 38.811 10.333 32.185 1.00 13.80 ? 1167 HOH A O 1 HETATM 2938 O O . HOH J 8 . ? 49.482 17.826 15.854 1.00 21.07 ? 1168 HOH A O 1 HETATM 2939 O O . HOH J 8 . ? 58.564 23.844 16.227 1.00 18.18 ? 1169 HOH A O 1 HETATM 2940 O O . HOH J 8 . ? 73.481 21.266 41.466 1.00 13.47 ? 1170 HOH A O 1 HETATM 2941 O O . HOH J 8 . ? 38.125 24.854 46.581 1.00 18.83 ? 1171 HOH A O 1 HETATM 2942 O O . HOH J 8 . ? 47.557 2.278 35.754 1.00 17.18 ? 1172 HOH A O 1 HETATM 2943 O O . HOH J 8 . ? 41.126 1.396 37.166 1.00 32.93 ? 1173 HOH A O 1 HETATM 2944 O O . HOH J 8 . ? 61.246 31.962 22.620 1.00 24.43 ? 1174 HOH A O 1 HETATM 2945 O O . HOH J 8 . ? 55.072 5.351 45.989 1.00 12.76 ? 1175 HOH A O 1 HETATM 2946 O O . HOH J 8 . ? 42.703 5.291 38.615 1.00 24.57 ? 1176 HOH A O 1 HETATM 2947 O O . HOH J 8 . ? 32.303 8.177 21.157 1.00 22.31 ? 1177 HOH A O 1 HETATM 2948 O O . HOH J 8 . ? 58.885 28.013 12.302 1.00 23.79 ? 1178 HOH A O 1 HETATM 2949 O O . HOH J 8 . ? 50.299 41.312 34.385 1.00 26.87 ? 1179 HOH A O 1 HETATM 2950 O O . HOH J 8 . ? 37.955 9.493 36.650 1.00 19.34 ? 1180 HOH A O 1 HETATM 2951 O O . HOH J 8 . ? 30.147 23.802 25.998 1.00 26.52 ? 1181 HOH A O 1 HETATM 2952 O O . HOH J 8 . ? 42.535 37.695 29.235 1.00 32.99 ? 1182 HOH A O 1 HETATM 2953 O O . HOH J 8 . ? 51.917 21.399 14.663 1.00 16.28 ? 1184 HOH A O 1 HETATM 2954 O O . HOH J 8 . ? 32.397 16.227 25.388 1.00 25.09 ? 1185 HOH A O 1 HETATM 2955 O O . HOH J 8 . ? 62.700 15.273 57.914 1.00 15.04 ? 1186 HOH A O 1 HETATM 2956 O O . HOH J 8 . ? 59.034 31.497 20.821 1.00 20.19 ? 1187 HOH A O 1 HETATM 2957 O O . HOH J 8 . ? 61.500 23.362 16.154 1.00 25.77 ? 1188 HOH A O 1 HETATM 2958 O O . HOH J 8 . ? 51.672 35.400 61.202 1.00 28.02 ? 1189 HOH A O 1 HETATM 2959 O O . HOH J 8 . ? 54.708 30.698 32.654 1.00 10.53 ? 1190 HOH A O 1 HETATM 2960 O O . HOH J 8 . ? 60.139 5.507 34.266 1.00 9.92 ? 1191 HOH A O 1 HETATM 2961 O O . HOH J 8 . ? 39.039 25.764 33.919 1.00 13.68 ? 1192 HOH A O 1 HETATM 2962 O O . HOH J 8 . ? 47.766 18.560 55.831 1.00 15.53 ? 1193 HOH A O 1 HETATM 2963 O O . HOH J 8 . ? 42.617 38.881 45.255 1.00 18.86 ? 1194 HOH A O 1 HETATM 2964 O O . HOH J 8 . ? 76.234 33.470 49.643 1.00 14.45 ? 1195 HOH A O 1 HETATM 2965 O O . HOH J 8 . ? 37.625 27.564 32.181 1.00 13.80 ? 1196 HOH A O 1 HETATM 2966 O O . HOH J 8 . ? 66.159 42.023 47.484 1.00 19.19 ? 1197 HOH A O 1 HETATM 2967 O O . HOH J 8 . ? 33.263 37.587 64.606 1.00 32.19 ? 1198 HOH A O 1 HETATM 2968 O O . HOH J 8 . ? 60.134 14.279 57.617 1.00 19.11 ? 1199 HOH A O 1 HETATM 2969 O O . HOH J 8 . ? 64.783 23.901 36.208 1.00 19.41 ? 1200 HOH A O 1 HETATM 2970 O O . HOH J 8 . ? 50.074 3.393 42.051 1.00 14.93 ? 1201 HOH A O 1 HETATM 2971 O O . HOH J 8 . ? 66.782 31.071 59.603 1.00 20.45 ? 1202 HOH A O 1 HETATM 2972 O O . HOH J 8 . ? 38.858 26.757 51.259 1.00 19.92 ? 1203 HOH A O 1 HETATM 2973 O O . HOH J 8 . ? 67.639 10.494 37.022 1.00 17.53 ? 1204 HOH A O 1 HETATM 2974 O O . HOH J 8 . ? 52.872 14.394 54.844 1.00 19.24 ? 1205 HOH A O 1 HETATM 2975 O O . HOH J 8 . ? 73.569 37.158 46.079 1.00 30.05 ? 1206 HOH A O 1 HETATM 2976 O O . HOH J 8 . ? 40.476 19.765 13.667 1.00 27.41 ? 1207 HOH A O 1 HETATM 2977 O O . HOH J 8 . ? 66.112 19.966 36.003 1.00 21.59 ? 1208 HOH A O 1 HETATM 2978 O O . HOH J 8 . ? 62.587 19.865 60.055 1.00 18.85 ? 1209 HOH A O 1 HETATM 2979 O O . HOH J 8 . ? 65.735 32.818 35.592 1.00 23.35 ? 1210 HOH A O 1 HETATM 2980 O O . HOH J 8 . ? 41.582 7.864 39.379 1.00 18.45 ? 1211 HOH A O 1 HETATM 2981 O O . HOH J 8 . ? 43.948 12.785 47.850 1.00 15.92 ? 1212 HOH A O 1 HETATM 2982 O O . HOH J 8 . ? 48.039 49.157 43.487 1.00 27.92 ? 1213 HOH A O 1 HETATM 2983 O O . HOH J 8 . ? 58.409 34.798 28.807 1.00 36.88 ? 1214 HOH A O 1 HETATM 2984 O O . HOH J 8 . ? 37.364 25.488 49.271 1.00 29.77 ? 1215 HOH A O 1 HETATM 2985 O O . HOH J 8 . ? 37.592 20.087 47.708 1.00 16.12 ? 1216 HOH A O 1 HETATM 2986 O O . HOH J 8 . ? 41.468 38.278 24.283 1.00 22.66 ? 1217 HOH A O 1 HETATM 2987 O O . HOH J 8 . ? 49.853 17.023 56.960 1.00 18.15 ? 1218 HOH A O 1 HETATM 2988 O O . HOH J 8 . ? 67.905 35.712 54.934 1.00 21.13 ? 1219 HOH A O 1 HETATM 2989 O O . HOH J 8 . ? 43.813 0.923 23.861 1.00 19.46 ? 1220 HOH A O 1 HETATM 2990 O O . HOH J 8 . ? 65.853 36.694 38.929 1.00 21.57 ? 1221 HOH A O 1 HETATM 2991 O O . HOH J 8 . ? 75.007 25.118 43.397 1.00 24.19 ? 1222 HOH A O 1 HETATM 2992 O O . HOH J 8 . ? 62.490 28.933 35.009 1.00 22.23 ? 1223 HOH A O 1 HETATM 2993 O O . HOH J 8 . ? 41.232 21.935 22.863 1.00 18.00 ? 1224 HOH A O 1 HETATM 2994 O O . HOH J 8 . ? 46.005 8.537 48.057 1.00 19.87 ? 1225 HOH A O 1 HETATM 2995 O O . HOH J 8 . ? 66.994 39.222 51.684 1.00 18.74 ? 1226 HOH A O 1 HETATM 2996 O O . HOH J 8 . ? 67.324 18.457 33.501 1.00 26.40 ? 1227 HOH A O 1 HETATM 2997 O O . HOH J 8 . ? 37.274 36.234 56.428 1.00 26.31 ? 1228 HOH A O 1 HETATM 2998 O O . HOH J 8 . ? 32.501 19.610 24.270 1.00 29.61 ? 1229 HOH A O 1 HETATM 2999 O O . HOH J 8 . ? 41.359 34.757 33.419 1.00 16.54 ? 1230 HOH A O 1 HETATM 3000 O O . HOH J 8 . ? 59.912 2.380 32.333 1.00 19.25 ? 1231 HOH A O 1 HETATM 3001 O O . HOH J 8 . ? 45.561 17.054 54.886 1.00 30.24 ? 1232 HOH A O 1 HETATM 3002 O O . HOH J 8 . ? 43.054 40.505 50.368 1.00 18.46 ? 1234 HOH A O 1 HETATM 3003 O O . HOH J 8 . ? 39.317 7.372 37.853 1.00 32.54 ? 1235 HOH A O 1 HETATM 3004 O O . HOH J 8 . ? 50.634 33.352 62.753 1.00 28.84 ? 1236 HOH A O 1 HETATM 3005 O O . HOH J 8 . ? 59.417 29.585 18.925 1.00 27.95 ? 1237 HOH A O 1 HETATM 3006 O O . HOH J 8 . ? 38.847 28.366 61.423 1.00 40.24 ? 1238 HOH A O 1 HETATM 3007 O O . HOH J 8 . ? 75.655 22.794 42.969 1.00 18.85 ? 1239 HOH A O 1 HETATM 3008 O O . HOH J 8 . ? 60.137 40.845 61.436 1.00 18.40 ? 1240 HOH A O 1 HETATM 3009 O O . HOH J 8 . ? 67.984 23.688 33.368 1.00 26.38 ? 1241 HOH A O 1 HETATM 3010 O O . HOH J 8 . ? 61.849 23.647 60.822 1.00 20.44 ? 1242 HOH A O 1 HETATM 3011 O O . HOH J 8 . ? 51.016 47.920 46.540 1.00 31.72 ? 1243 HOH A O 1 HETATM 3012 O O . HOH J 8 . ? 37.842 26.245 29.726 1.00 23.17 ? 1245 HOH A O 1 HETATM 3013 O O . HOH J 8 . ? 33.846 41.288 56.619 1.00 28.83 ? 1246 HOH A O 1 HETATM 3014 O O . HOH J 8 . ? 60.089 8.334 24.305 1.00 27.42 ? 1247 HOH A O 1 HETATM 3015 O O . HOH J 8 . ? 64.751 44.077 48.584 1.00 26.23 ? 1248 HOH A O 1 HETATM 3016 O O . HOH J 8 . ? 35.379 18.694 46.774 1.00 22.01 ? 1249 HOH A O 1 HETATM 3017 O O . HOH J 8 . ? 37.171 23.456 39.229 1.00 22.44 ? 1250 HOH A O 1 HETATM 3018 O O . HOH J 8 . ? 46.241 -0.148 35.684 1.00 40.15 ? 1251 HOH A O 1 HETATM 3019 O O . HOH J 8 . ? 38.284 37.084 54.147 1.00 26.98 ? 1252 HOH A O 1 HETATM 3020 O O . HOH J 8 . ? 43.429 40.464 47.519 1.00 31.86 ? 1253 HOH A O 1 HETATM 3021 O O . HOH J 8 . ? 42.667 41.186 43.639 1.00 33.16 ? 1254 HOH A O 1 HETATM 3022 O O . HOH J 8 . ? 43.893 19.181 66.113 1.00 25.61 ? 1255 HOH A O 1 HETATM 3023 O O . HOH J 8 . ? 68.748 39.981 40.232 1.00 25.24 ? 1256 HOH A O 1 HETATM 3024 O O . HOH J 8 . ? 72.803 33.712 44.000 1.00 22.96 ? 1257 HOH A O 1 HETATM 3025 O O . HOH J 8 . ? 70.736 28.351 59.917 1.00 24.94 ? 1258 HOH A O 1 HETATM 3026 O O . HOH J 8 . ? 45.346 28.188 20.849 1.00 34.10 ? 1260 HOH A O 1 HETATM 3027 O O . HOH J 8 . ? 61.347 8.432 26.678 1.00 30.59 ? 1261 HOH A O 1 HETATM 3028 O O . HOH J 8 . ? 55.827 2.251 30.787 1.00 19.91 ? 1262 HOH A O 1 HETATM 3029 O O . HOH J 8 . ? 47.592 39.499 61.610 1.00 27.14 ? 1263 HOH A O 1 HETATM 3030 O O . HOH J 8 . ? 57.231 34.408 62.267 1.00 25.28 ? 1264 HOH A O 1 HETATM 3031 O O . HOH J 8 . ? 60.035 37.170 35.391 1.00 37.05 ? 1266 HOH A O 1 HETATM 3032 O O . HOH J 8 . ? 36.820 14.313 18.408 1.00 26.32 ? 1268 HOH A O 1 HETATM 3033 O O . HOH J 8 . ? 35.001 28.895 49.142 1.00 33.36 ? 1269 HOH A O 1 HETATM 3034 O O . HOH J 8 . ? 53.279 49.851 48.064 1.00 42.42 ? 1270 HOH A O 1 HETATM 3035 O O . HOH J 8 . ? 65.278 10.332 30.883 1.00 23.35 ? 1271 HOH A O 1 HETATM 3036 O O . HOH J 8 . ? 56.463 14.145 12.727 1.00 24.66 ? 1272 HOH A O 1 HETATM 3037 O O . HOH J 8 . ? 39.849 38.363 39.616 1.00 30.15 ? 1273 HOH A O 1 HETATM 3038 O O . HOH J 8 . ? 50.791 38.275 61.246 1.00 36.32 ? 1274 HOH A O 1 HETATM 3039 O O . HOH J 8 . ? 56.620 45.246 32.483 1.00 21.73 ? 1275 HOH A O 1 HETATM 3040 O O . HOH J 8 . ? 46.161 -0.566 38.697 1.00 30.46 ? 1277 HOH A O 1 HETATM 3041 O O . HOH J 8 . ? 70.051 19.258 27.474 1.00 34.60 ? 1278 HOH A O 1 HETATM 3042 O O . HOH J 8 . ? 64.855 15.498 23.576 1.00 28.94 ? 1279 HOH A O 1 HETATM 3043 O O . HOH J 8 . ? 34.909 30.352 42.555 1.00 30.13 ? 1280 HOH A O 1 HETATM 3044 O O . HOH J 8 . ? 39.897 24.665 54.473 1.00 31.76 ? 1281 HOH A O 1 HETATM 3045 O O . HOH J 8 . ? 41.527 35.767 43.111 1.00 32.51 ? 1282 HOH A O 1 HETATM 3046 O O . HOH J 8 . ? 37.610 22.338 46.205 1.00 35.46 ? 1283 HOH A O 1 HETATM 3047 O O . HOH J 8 . ? 35.694 28.933 46.291 1.00 33.13 ? 1284 HOH A O 1 HETATM 3048 O O . HOH J 8 . ? 56.652 32.157 12.176 1.00 29.42 ? 1285 HOH A O 1 HETATM 3049 O O . HOH J 8 . ? 51.529 11.054 54.246 1.00 36.55 ? 1286 HOH A O 1 HETATM 3050 O O . HOH J 8 . ? 58.488 17.062 59.586 1.00 31.08 ? 1287 HOH A O 1 HETATM 3051 O O . HOH J 8 . ? 42.551 36.995 31.899 1.00 34.83 ? 1288 HOH A O 1 HETATM 3052 O O . HOH J 8 . ? 66.428 11.203 50.080 1.00 31.16 ? 1289 HOH A O 1 HETATM 3053 O O . HOH J 8 . ? 64.132 12.516 27.117 1.00 18.94 ? 1290 HOH A O 1 HETATM 3054 O O . HOH J 8 . ? 62.608 26.778 63.430 1.00 28.41 ? 1291 HOH A O 1 HETATM 3055 O O . HOH J 8 . ? 67.041 22.471 35.956 1.00 34.59 ? 1292 HOH A O 1 HETATM 3056 O O . HOH J 8 . ? 41.295 13.474 47.599 1.00 24.90 ? 1293 HOH A O 1 HETATM 3057 O O . HOH J 8 . ? 71.986 13.898 50.535 1.00 28.90 ? 1294 HOH A O 1 HETATM 3058 O O . HOH J 8 . ? 45.567 33.184 26.041 1.00 25.57 ? 1295 HOH A O 1 HETATM 3059 O O . HOH J 8 . ? 75.763 30.941 45.181 1.00 28.45 ? 1296 HOH A O 1 HETATM 3060 O O . HOH J 8 . ? 59.093 35.763 63.604 1.00 33.10 ? 1297 HOH A O 1 HETATM 3061 O O . HOH J 8 . ? 66.398 19.966 31.432 1.00 33.52 ? 1298 HOH A O 1 HETATM 3062 O O . HOH J 8 . ? 63.097 12.294 22.537 1.00 36.22 ? 1299 HOH A O 1 HETATM 3063 O O . HOH J 8 . ? 35.187 27.971 41.473 1.00 30.15 ? 1300 HOH A O 1 HETATM 3064 O O . HOH J 8 . ? 69.770 21.528 26.286 1.00 37.02 ? 1301 HOH A O 1 HETATM 3065 O O . HOH J 8 . ? 38.054 36.844 47.038 1.00 31.91 ? 1302 HOH A O 1 HETATM 3066 O O . HOH J 8 . ? 35.327 6.773 24.060 1.00 25.61 ? 1303 HOH A O 1 HETATM 3067 O O . HOH J 8 . ? 60.834 11.311 19.093 1.00 36.79 ? 1304 HOH A O 1 HETATM 3068 O O . HOH J 8 . ? 65.148 26.217 18.335 1.00 28.84 ? 1305 HOH A O 1 HETATM 3069 O O . HOH J 8 . ? 33.697 17.729 31.504 1.00 37.03 ? 1306 HOH A O 1 HETATM 3070 O O . HOH J 8 . ? 75.010 34.796 52.360 1.00 32.69 ? 1307 HOH A O 1 HETATM 3071 O O . HOH J 8 . ? 40.929 23.684 56.770 1.00 35.09 ? 1308 HOH A O 1 HETATM 3072 O O . HOH J 8 . ? 64.436 6.379 32.755 1.00 26.07 ? 1309 HOH A O 1 HETATM 3073 O O . HOH J 8 . ? 38.930 15.760 48.832 1.00 35.59 ? 1310 HOH A O 1 HETATM 3074 O O . HOH J 8 . ? 40.856 42.184 50.284 1.00 25.84 ? 1311 HOH A O 1 HETATM 3075 O O . HOH J 8 . ? 48.788 15.167 15.583 1.00 34.98 ? 1312 HOH A O 1 HETATM 3076 O O . HOH J 8 . ? 60.145 45.763 50.389 1.00 26.86 ? 1313 HOH A O 1 HETATM 3077 O O . HOH J 8 . ? 50.799 13.027 56.055 1.00 38.27 ? 1314 HOH A O 1 HETATM 3078 O O . HOH J 8 . ? 36.166 26.622 45.276 1.00 31.62 ? 1315 HOH A O 1 HETATM 3079 O O . HOH J 8 . ? 59.674 12.398 59.463 1.00 28.90 ? 1316 HOH A O 1 HETATM 3080 O O . HOH J 8 . ? 37.926 20.806 10.813 1.00 34.71 ? 1317 HOH A O 1 HETATM 3081 O O . HOH J 8 . ? 66.020 8.282 34.094 1.00 22.56 ? 1319 HOH A O 1 HETATM 3082 O O . HOH J 8 . ? 53.863 44.487 58.869 1.00 26.61 ? 1320 HOH A O 1 HETATM 3083 O O . HOH J 8 . ? 41.830 17.663 52.248 1.00 36.69 ? 1321 HOH A O 1 HETATM 3084 O O . HOH J 8 . ? 55.851 13.031 56.969 1.00 39.56 ? 1322 HOH A O 1 HETATM 3085 O O . HOH J 8 . ? 50.823 38.389 35.021 1.00 34.24 ? 1324 HOH A O 1 HETATM 3086 O O . HOH J 8 . ? 71.195 32.062 43.644 1.00 33.36 ? 1328 HOH A O 1 HETATM 3087 O O . HOH J 8 . ? 71.874 15.806 42.967 1.00 42.10 ? 1329 HOH A O 1 HETATM 3088 O O . HOH J 8 . ? 68.433 43.247 46.509 1.00 29.04 ? 1330 HOH A O 1 HETATM 3089 O O . HOH J 8 . ? 39.027 25.727 56.476 1.00 38.81 ? 1331 HOH A O 1 HETATM 3090 O O . HOH J 8 . ? 64.936 20.797 33.516 1.00 24.35 ? 1333 HOH A O 1 HETATM 3091 O O . HOH J 8 . ? 70.239 13.407 35.746 1.00 38.06 ? 1334 HOH A O 1 HETATM 3092 O O . HOH J 8 . ? 42.427 19.349 55.020 1.00 43.60 ? 1335 HOH A O 1 HETATM 3093 O O . HOH J 8 . ? 50.140 22.201 12.277 1.00 20.93 ? 1336 HOH A O 1 HETATM 3094 O O . HOH J 8 . ? 44.206 24.692 62.714 1.00 25.01 ? 1337 HOH A O 1 HETATM 3095 O O . HOH J 8 . ? 67.125 20.963 61.508 1.00 24.47 ? 1338 HOH A O 1 HETATM 3096 O O . HOH J 8 . ? 61.429 21.471 13.992 1.00 33.96 ? 1340 HOH A O 1 HETATM 3097 O O . HOH J 8 . ? 32.961 15.330 33.528 1.00 36.61 ? 1341 HOH A O 1 HETATM 3098 O O . HOH J 8 . ? 77.534 20.274 43.347 1.00 39.26 ? 1342 HOH A O 1 HETATM 3099 O O . HOH J 8 . ? 49.048 35.399 20.143 1.00 36.84 ? 1343 HOH A O 1 HETATM 3100 O O . HOH J 8 . ? 65.952 10.957 44.214 1.00 21.27 ? 1345 HOH A O 1 HETATM 3101 O O . HOH J 8 . ? 48.416 46.114 50.507 1.00 31.22 ? 1346 HOH A O 1 HETATM 3102 O O . HOH J 8 . ? 44.342 32.471 22.283 1.00 42.80 ? 1347 HOH A O 1 HETATM 3103 O O . HOH J 8 . ? 31.068 38.832 58.099 1.00 27.31 ? 1348 HOH A O 1 HETATM 3104 O O . HOH J 8 . ? 59.761 34.185 35.427 1.00 38.85 ? 1349 HOH A O 1 HETATM 3105 O O . HOH J 8 . ? 32.230 42.696 60.168 1.00 25.62 ? 1350 HOH A O 1 HETATM 3106 O O . HOH J 8 . ? 59.862 29.537 39.761 1.00 22.79 ? 1351 HOH A O 1 HETATM 3107 O O . HOH J 8 . ? 65.931 24.480 61.968 1.00 39.44 ? 1354 HOH A O 1 HETATM 3108 O O . HOH J 8 . ? 68.658 23.174 62.775 1.00 30.81 ? 1355 HOH A O 1 HETATM 3109 O O . HOH J 8 . ? 67.912 20.000 17.117 1.00 38.95 ? 1356 HOH A O 1 HETATM 3110 O O . HOH J 8 . ? 51.552 22.420 10.238 1.00 39.60 ? 1358 HOH A O 1 HETATM 3111 O O . HOH J 8 . ? 46.052 30.373 22.941 1.00 19.34 ? 1359 HOH A O 1 HETATM 3112 O O . HOH J 8 . ? 47.426 30.910 25.814 1.00 20.47 ? 1360 HOH A O 1 HETATM 3113 O O . HOH J 8 . ? 73.670 37.510 48.828 1.00 35.08 ? 1362 HOH A O 1 HETATM 3114 O O . HOH J 8 . ? 44.568 39.662 30.464 1.00 31.24 ? 1364 HOH A O 1 HETATM 3115 O O . HOH J 8 . ? 55.512 39.496 26.782 1.00 24.36 ? 1365 HOH A O 1 HETATM 3116 O O . HOH J 8 . ? 65.552 12.696 29.261 1.00 35.99 ? 1366 HOH A O 1 HETATM 3117 O O . HOH J 8 . ? 75.880 35.969 49.923 1.00 37.47 ? 1367 HOH A O 1 HETATM 3118 O O . HOH J 8 . ? 39.926 38.614 52.871 1.00 31.82 ? 1369 HOH A O 1 HETATM 3119 O O . HOH J 8 . ? 36.552 5.955 32.784 1.00 37.12 ? 1370 HOH A O 1 HETATM 3120 O O . HOH J 8 . ? 63.417 9.913 26.605 1.00 29.85 ? 1371 HOH A O 1 HETATM 3121 O O . HOH J 8 . ? 67.791 43.439 50.382 1.00 48.07 ? 1372 HOH A O 1 HETATM 3122 O O . HOH J 8 . ? 37.075 32.476 35.088 1.00 23.53 ? 1373 HOH A O 1 HETATM 3123 O O . HOH J 8 . ? 44.747 34.614 66.125 1.00 29.22 ? 1374 HOH A O 1 HETATM 3124 O O . HOH J 8 . ? 69.950 18.693 32.947 1.00 42.20 ? 1376 HOH A O 1 HETATM 3125 O O . HOH J 8 . ? 57.969 37.762 27.190 1.00 36.87 ? 1377 HOH A O 1 HETATM 3126 O O . HOH J 8 . ? 67.366 12.265 47.011 1.00 40.08 ? 1380 HOH A O 1 HETATM 3127 O O . HOH J 8 . ? 54.992 17.208 66.536 1.00 33.48 ? 1381 HOH A O 1 HETATM 3128 O O . HOH J 8 . ? 50.509 46.445 51.655 1.00 30.45 ? 1383 HOH A O 1 HETATM 3129 O O . HOH J 8 . ? 62.466 46.297 51.306 1.00 37.15 ? 1385 HOH A O 1 HETATM 3130 O O . HOH J 8 . ? 48.146 49.670 47.072 1.00 41.30 ? 1386 HOH A O 1 HETATM 3131 O O . HOH J 8 . ? 60.716 -1.926 33.945 1.00 33.89 ? 1387 HOH A O 1 HETATM 3132 O O . HOH J 8 . ? 56.428 10.147 18.884 1.00 34.70 ? 1388 HOH A O 1 HETATM 3133 O O . HOH J 8 . ? 44.617 16.365 52.389 1.00 29.42 ? 1389 HOH A O 1 HETATM 3134 O O . HOH J 8 . ? 77.335 25.964 42.114 1.00 35.85 ? 1390 HOH A O 1 HETATM 3135 O O . HOH J 8 . ? 36.698 34.984 36.011 1.00 31.50 ? 1391 HOH A O 1 HETATM 3136 O O . HOH J 8 . ? 56.447 4.982 53.164 1.00 42.77 ? 1392 HOH A O 1 HETATM 3137 O O . HOH J 8 . ? 43.869 13.942 51.803 1.00 43.03 ? 1393 HOH A O 1 HETATM 3138 O O . HOH J 8 . ? 37.973 22.146 43.968 1.00 36.62 ? 1394 HOH A O 1 HETATM 3139 O O . HOH J 8 . ? 43.222 23.873 23.040 1.00 35.06 ? 1395 HOH A O 1 HETATM 3140 O O . HOH J 8 . ? 55.520 37.416 18.555 1.00 45.87 ? 1397 HOH A O 1 HETATM 3141 O O . HOH J 8 . ? 37.735 24.238 41.755 1.00 23.53 ? 1398 HOH A O 1 HETATM 3142 O O . HOH J 8 . ? 64.459 42.965 36.583 1.00 39.60 ? 1399 HOH A O 1 HETATM 3143 O O . HOH J 8 . ? 31.017 4.991 28.739 1.00 35.93 ? 1400 HOH A O 1 HETATM 3144 O O . HOH J 8 . ? 39.756 10.386 45.603 1.00 37.39 ? 1401 HOH A O 1 HETATM 3145 O O . HOH J 8 . ? 52.394 40.359 32.137 1.00 52.89 ? 1402 HOH A O 1 HETATM 3146 O O . HOH J 8 . ? 40.253 37.921 44.104 1.00 28.73 ? 1403 HOH A O 1 HETATM 3147 O O . HOH J 8 . ? 60.724 4.533 30.226 1.00 40.04 ? 1404 HOH A O 1 HETATM 3148 O O . HOH J 8 . ? 39.609 14.895 15.429 1.00 31.76 ? 1405 HOH A O 1 HETATM 3149 O O . HOH J 8 . ? 64.611 45.445 53.781 1.00 32.74 ? 1409 HOH A O 1 HETATM 3150 O O . HOH J 8 . ? 43.341 42.397 45.897 1.00 32.62 ? 1410 HOH A O 1 HETATM 3151 O O . HOH J 8 . ? 37.297 29.358 54.218 1.00 36.34 ? 1411 HOH A O 1 HETATM 3152 O O . HOH J 8 . ? 68.207 30.411 37.162 1.00 38.78 ? 1414 HOH A O 1 HETATM 3153 O O . HOH J 8 . ? 40.801 6.991 41.805 1.00 39.23 ? 1415 HOH A O 1 HETATM 3154 O O A HOH J 8 . ? 33.235 18.151 35.593 0.52 16.83 ? 1417 HOH A O 1 HETATM 3155 O O B HOH J 8 . ? 58.301 21.342 62.765 0.52 26.98 ? 1417 HOH A O 1 HETATM 3156 O O . HOH J 8 . ? 39.869 12.674 14.405 1.00 30.95 ? 1418 HOH A O 1 HETATM 3157 O O . HOH J 8 . ? 57.056 47.198 56.838 1.00 29.75 ? 1419 HOH A O 1 HETATM 3158 O O . HOH J 8 . ? 62.388 1.662 33.438 1.00 35.47 ? 1420 HOH A O 1 HETATM 3159 O O . HOH J 8 . ? 62.552 6.511 55.908 1.00 30.22 ? 1423 HOH A O 1 HETATM 3160 O O . HOH J 8 . ? 60.333 42.965 63.164 1.00 41.57 ? 1424 HOH A O 1 HETATM 3161 O O . HOH J 8 . ? 66.864 6.027 38.337 1.00 34.31 ? 1427 HOH A O 1 HETATM 3162 O O . HOH J 8 . ? 35.869 33.435 52.986 1.00 34.17 ? 1428 HOH A O 1 HETATM 3163 O O . HOH J 8 . ? 68.331 13.427 42.141 1.00 39.68 ? 1430 HOH A O 1 HETATM 3164 O O . HOH J 8 . ? 78.994 28.229 42.855 1.00 40.27 ? 1432 HOH A O 1 HETATM 3165 O O . HOH J 8 . ? 71.071 9.032 54.596 1.00 37.97 ? 1437 HOH A O 1 HETATM 3166 O O . HOH J 8 . ? 64.873 5.061 42.477 1.00 39.90 ? 1438 HOH A O 1 HETATM 3167 O O . HOH J 8 . ? 61.248 34.232 64.395 1.00 31.71 ? 1440 HOH A O 1 HETATM 3168 O O . HOH J 8 . ? 63.791 20.195 16.646 1.00 33.98 ? 1442 HOH A O 1 HETATM 3169 O O . HOH J 8 . ? 55.777 30.827 46.491 1.00 29.70 ? 1444 HOH A O 1 HETATM 3170 O O . HOH J 8 . ? 45.850 6.166 46.874 1.00 32.20 ? 1447 HOH A O 1 HETATM 3171 O O . HOH J 8 . ? 39.692 21.713 29.119 1.00 10.33 ? 1448 HOH A O 1 HETATM 3172 O O . HOH J 8 . ? 37.903 22.976 29.734 1.00 37.78 ? 1449 HOH A O 1 HETATM 3173 O O . HOH J 8 . ? 39.879 25.186 28.820 1.00 25.20 ? 1450 HOH A O 1 HETATM 3174 O O . HOH J 8 . ? 45.655 25.658 8.286 1.00 37.41 ? 1451 HOH A O 1 HETATM 3175 O O . HOH J 8 . ? 58.629 13.225 16.543 1.00 36.88 ? 1452 HOH A O 1 HETATM 3176 O O . HOH J 8 . ? 62.327 0.579 38.674 1.00 16.49 ? 1454 HOH A O 1 HETATM 3177 O O . HOH J 8 . ? 38.019 22.752 26.538 1.00 24.85 ? 1455 HOH A O 1 HETATM 3178 O O . HOH J 8 . ? 35.539 23.887 32.384 1.00 39.59 ? 1456 HOH A O 1 HETATM 3179 O O . HOH J 8 . ? 61.269 2.771 45.124 1.00 30.53 ? 1457 HOH A O 1 HETATM 3180 O O . HOH J 8 . ? 34.358 16.138 17.236 1.00 33.44 ? 1460 HOH A O 1 HETATM 3181 O O . HOH J 8 . ? 76.823 36.647 52.071 1.00 32.14 ? 1461 HOH A O 1 HETATM 3182 O O . HOH J 8 . ? 42.098 38.455 34.739 1.00 28.43 ? 1462 HOH A O 1 HETATM 3183 O O . HOH J 8 . ? 34.764 12.207 31.228 1.00 34.46 ? 1463 HOH A O 1 HETATM 3184 O O . HOH J 8 . ? 65.819 38.918 39.344 1.00 38.14 ? 1470 HOH A O 1 HETATM 3185 O O . HOH J 8 . ? 32.296 19.842 31.402 1.00 30.95 ? 1473 HOH A O 1 HETATM 3186 O O . HOH J 8 . ? 73.270 19.731 55.676 1.00 21.10 ? 1475 HOH A O 1 HETATM 3187 O O . HOH J 8 . ? 58.821 35.360 37.733 1.00 21.88 ? 1476 HOH A O 1 HETATM 3188 O O . HOH J 8 . ? 35.308 18.250 33.433 1.00 29.21 ? 1477 HOH A O 1 HETATM 3189 O O . HOH J 8 . ? 59.766 32.398 63.883 1.00 30.13 ? 1478 HOH A O 1 HETATM 3190 O O . HOH J 8 . ? 68.672 26.970 29.574 1.00 26.93 ? 1479 HOH A O 1 HETATM 3191 O O . HOH J 8 . ? 45.021 25.740 21.344 1.00 43.04 ? 1481 HOH A O 1 HETATM 3192 O O . HOH J 8 . ? 73.896 15.632 51.135 1.00 35.93 ? 1482 HOH A O 1 HETATM 3193 O O . HOH J 8 . ? 43.685 43.165 26.768 1.00 41.93 ? 1484 HOH A O 1 HETATM 3194 O O . HOH J 8 . ? 60.563 6.397 49.513 1.00 30.26 ? 1485 HOH A O 1 HETATM 3195 O O . HOH J 8 . ? 48.443 0.577 32.927 1.00 35.52 ? 1487 HOH A O 1 HETATM 3196 O O . HOH J 8 . ? 49.839 44.216 57.997 1.00 30.44 ? 1488 HOH A O 1 HETATM 3197 O O . HOH J 8 . ? 50.195 37.914 32.127 1.00 34.15 ? 1489 HOH A O 1 HETATM 3198 O O . HOH J 8 . ? 50.936 0.980 31.440 1.00 37.11 ? 1492 HOH A O 1 HETATM 3199 O O . HOH J 8 . ? 67.926 29.516 28.626 1.00 31.18 ? 1494 HOH A O 1 HETATM 3200 O O . HOH J 8 . ? 61.343 27.371 17.534 1.00 35.55 ? 1495 HOH A O 1 HETATM 3201 O O . HOH J 8 . ? 67.384 33.544 58.209 1.00 20.88 ? 1496 HOH A O 1 HETATM 3202 O O . HOH J 8 . ? 58.067 38.553 34.740 1.00 26.08 ? 1497 HOH A O 1 HETATM 3203 O O . HOH J 8 . ? 76.984 33.507 46.834 1.00 26.95 ? 1498 HOH A O 1 HETATM 3204 O O . HOH J 8 . ? 61.654 1.262 36.185 1.00 36.77 ? 1499 HOH A O 1 HETATM 3205 O O . HOH J 8 . ? 48.087 -2.121 33.619 1.00 41.20 ? 1502 HOH A O 1 HETATM 3206 O O . HOH J 8 . ? 63.297 13.153 59.319 1.00 40.40 ? 1503 HOH A O 1 HETATM 3207 O O . HOH J 8 . ? 35.417 26.280 38.822 1.00 42.59 ? 1504 HOH A O 1 HETATM 3208 O O . HOH J 8 . ? 65.310 4.348 38.175 1.00 39.49 ? 1505 HOH A O 1 HETATM 3209 O O . HOH J 8 . ? 72.414 19.993 65.373 1.00 35.91 ? 1507 HOH A O 1 HETATM 3210 O O . HOH J 8 . ? 70.193 27.784 31.952 1.00 34.93 ? 1508 HOH A O 1 HETATM 3211 O O . HOH J 8 . ? 33.313 45.110 59.692 1.00 40.91 ? 1509 HOH A O 1 HETATM 3212 O O . HOH J 8 . ? 66.895 6.870 57.872 1.00 46.31 ? 1510 HOH A O 1 HETATM 3213 O O . HOH J 8 . ? 47.505 39.506 28.741 1.00 31.84 ? 1511 HOH A O 1 HETATM 3214 O O . HOH J 8 . ? 62.937 17.899 58.212 1.00 36.96 ? 1512 HOH A O 1 HETATM 3215 O O . HOH J 8 . ? 70.640 18.773 36.721 1.00 47.22 ? 1513 HOH A O 1 HETATM 3216 O O . HOH J 8 . ? 74.620 17.178 49.296 1.00 36.43 ? 1514 HOH A O 1 HETATM 3217 O O . HOH J 8 . ? 61.824 21.664 37.897 1.00 42.77 ? 1517 HOH A O 1 HETATM 3218 O O . HOH J 8 . ? 34.173 17.673 37.461 1.00 53.29 ? 1518 HOH A O 1 HETATM 3219 O O . HOH J 8 . ? 50.126 3.055 24.273 1.00 45.77 ? 1520 HOH A O 1 HETATM 3220 O O . HOH J 8 . ? 29.791 11.284 22.548 1.00 26.20 ? 1521 HOH A O 1 HETATM 3221 O O . HOH J 8 . ? 59.865 4.291 48.174 1.00 36.23 ? 1523 HOH A O 1 HETATM 3222 O O . HOH J 8 . ? 63.419 2.645 36.671 1.00 42.07 ? 1524 HOH A O 1 HETATM 3223 O O . HOH J 8 . ? 51.135 1.241 27.585 1.00 40.50 ? 1526 HOH A O 1 HETATM 3224 O O . HOH J 8 . ? 35.925 19.183 14.695 1.00 45.62 ? 1528 HOH A O 1 HETATM 3225 O O . HOH J 8 . ? 44.047 31.149 27.912 1.00 40.75 ? 1529 HOH A O 1 HETATM 3226 O O . HOH J 8 . ? 36.195 25.673 43.182 1.00 39.24 ? 1531 HOH A O 1 HETATM 3227 O O . HOH J 8 . ? 68.238 40.557 58.917 1.00 43.60 ? 1532 HOH A O 1 HETATM 3228 O O . HOH J 8 . ? 74.143 18.599 64.852 1.00 33.83 ? 1533 HOH A O 1 HETATM 3229 O O . HOH J 8 . ? 62.524 31.436 35.389 1.00 39.08 ? 1534 HOH A O 1 HETATM 3230 O O . HOH J 8 . ? 71.765 13.560 54.379 1.00 39.48 ? 1537 HOH A O 1 HETATM 3231 O O . HOH J 8 . ? 65.714 6.802 43.722 1.00 35.54 ? 1541 HOH A O 1 HETATM 3232 O O . HOH J 8 . ? 48.654 40.003 31.053 1.00 36.33 ? 1543 HOH A O 1 HETATM 3233 O O . HOH J 8 . ? 55.616 30.309 64.415 1.00 37.89 ? 1547 HOH A O 1 HETATM 3234 O O . HOH J 8 . ? 47.037 5.867 18.136 1.00 45.89 ? 1550 HOH A O 1 HETATM 3235 O O . HOH J 8 . ? 52.235 42.653 32.095 1.00 80.92 ? 1551 HOH A O 1 HETATM 3236 O O . HOH J 8 . ? 68.773 36.618 57.192 1.00 40.43 ? 1554 HOH A O 1 HETATM 3237 O O . HOH J 8 . ? 52.639 28.352 67.723 1.00 43.95 ? 1555 HOH A O 1 HETATM 3238 O O . HOH J 8 . ? 64.212 44.200 44.065 1.00 54.53 ? 1556 HOH A O 1 HETATM 3239 O O . HOH J 8 . ? 62.982 43.505 61.767 1.00 43.71 ? 1557 HOH A O 1 HETATM 3240 O O . HOH J 8 . ? 68.502 42.878 54.109 1.00 46.92 ? 1558 HOH A O 1 HETATM 3241 O O . HOH J 8 . ? 50.819 41.198 21.976 1.00 43.55 ? 1564 HOH A O 1 HETATM 3242 O O . HOH J 8 . ? 53.814 38.567 32.401 1.00 29.41 ? 1565 HOH A O 1 HETATM 3243 O O . HOH J 8 . ? 65.647 47.415 59.058 1.00 36.10 ? 1566 HOH A O 1 HETATM 3244 O O . HOH J 8 . ? 35.906 10.444 38.689 1.00 40.58 ? 1567 HOH A O 1 HETATM 3245 O O . HOH J 8 . ? 53.657 51.946 49.976 1.00 37.64 ? 1568 HOH A O 1 HETATM 3246 O O . HOH J 8 . ? 75.636 34.909 45.175 1.00 40.53 ? 1570 HOH A O 1 HETATM 3247 O O . HOH J 8 . ? 64.742 4.255 57.900 1.00 49.64 ? 1571 HOH A O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . ALA A 1 ? 0.3290 0.3389 0.3085 0.0842 0.0894 -0.0628 1 ALA A N 2 C CA . ALA A 1 ? 0.2351 0.3361 0.2935 0.1256 -0.0354 -0.0702 1 ALA A CA 3 C C . ALA A 1 ? 0.2692 0.2883 0.2745 0.1219 -0.0216 -0.0925 1 ALA A C 4 O O . ALA A 1 ? 0.3911 0.2834 0.2965 0.1331 -0.0844 -0.1000 1 ALA A O 5 C CB . ALA A 1 ? 0.2323 0.6014 0.4086 0.1255 -0.0406 0.0173 1 ALA A CB 6 N N . VAL A 2 ? 0.3077 0.2918 0.2967 0.0754 -0.0347 -0.1019 2 VAL A N 7 C CA . VAL A 2 ? 0.2440 0.2880 0.3387 0.0328 0.0661 -0.0482 2 VAL A CA 8 C C . VAL A 2 ? 0.2089 0.4688 0.3772 -0.0064 0.0709 -0.1248 2 VAL A C 9 O O . VAL A 2 ? 0.2676 0.8485 0.3987 -0.1101 0.0332 -0.1676 2 VAL A O 10 C CB . VAL A 2 ? 0.2094 0.2885 0.4880 0.0428 0.0967 -0.0023 2 VAL A CB 11 C CG1 . VAL A 2 ? 0.4587 0.3167 0.5038 0.1087 0.0919 0.0094 2 VAL A CG1 12 C CG2 . VAL A 2 ? 0.2570 0.4013 0.5814 -0.0632 0.1559 -0.1754 2 VAL A CG2 13 N N . CYS A 3 ? 0.2410 0.2749 0.3997 0.0045 0.0982 -0.1041 3 CYS A N 14 C CA . CYS A 3 ? 0.2749 0.2261 0.5374 0.0114 0.1615 -0.0884 3 CYS A CA 15 C C . CYS A 3 ? 0.4011 0.2186 0.7639 -0.0031 0.1910 -0.1330 3 CYS A C 16 O O . CYS A 3 ? 0.4264 0.1805 0.7836 0.0032 0.3082 -0.0423 3 CYS A O 17 C CB A CYS A 3 ? 0.2913 0.2067 0.4590 0.1252 0.1507 0.0122 3 CYS A CB 18 C CB B CYS A 3 ? 0.3034 0.3220 0.5537 0.0841 0.2283 -0.0750 3 CYS A CB 19 S SG A CYS A 3 ? 0.1810 0.1958 0.2656 0.0453 0.0611 -0.0135 3 CYS A SG 20 S SG B CYS A 3 ? 0.7305 0.3148 0.3394 0.1764 -0.1607 -0.0706 3 CYS A SG 21 N N . PRO A 4 ? 0.4282 0.2408 0.8936 -0.0287 0.2312 -0.1049 4 PRO A N 22 C CA . PRO A 4 ? 0.5245 0.2288 0.9147 -0.0406 0.2275 0.0294 4 PRO A CA 23 C C . PRO A 4 ? 0.5846 0.3529 0.8635 0.0427 0.2000 -0.0660 4 PRO A C 24 O O . PRO A 4 ? 0.4742 0.5261 0.9622 0.1125 0.2379 0.0167 4 PRO A O 25 C CB . PRO A 4 ? 0.5645 0.2760 1.0357 -0.1032 0.1643 0.1471 4 PRO A CB 26 C CG . PRO A 4 ? 0.5440 0.1960 0.9862 -0.1162 0.1003 0.0279 4 PRO A CG 27 C CD . PRO A 4 ? 0.4277 0.3192 0.7919 -0.0483 0.3165 -0.1588 4 PRO A CD 28 N N . ASP A 5 ? 0.7704 0.3473 0.9346 -0.1517 0.2620 -0.1563 5 ASP A N 29 C CA . ASP A 5 ? 1.0666 0.6390 0.9250 -0.2107 0.1581 -0.1802 5 ASP A CA 30 C C . ASP A 5 ? 0.8984 0.5895 0.8737 -0.1106 0.1298 -0.2370 5 ASP A C 31 O O . ASP A 5 ? 0.5703 0.5224 0.4633 0.0022 0.0221 -0.0121 5 ASP A O 32 C CB . ASP A 5 ? 1.2929 1.0433 0.9468 -0.3157 0.2684 -0.0330 5 ASP A CB 33 C CG . ASP A 5 ? 1.4988 1.1641 1.1155 -0.4363 0.2175 0.1856 5 ASP A CG 34 O OD1 . ASP A 5 ? 1.4496 1.6074 1.2056 -0.5980 0.3391 0.5309 5 ASP A OD1 35 O OD2 . ASP A 5 ? 1.9024 1.2614 1.3607 -0.3823 0.2734 0.5319 5 ASP A OD2 36 N N . GLY A 6 ? 0.8268 0.3657 0.8095 -0.0219 -0.0365 -0.2758 6 GLY A N 37 C CA . GLY A 6 ? 0.7685 0.2241 0.6317 0.2329 -0.0495 -0.0065 6 GLY A CA 38 C C . GLY A 6 ? 0.5454 0.2521 0.5567 0.2043 0.0242 0.0202 6 GLY A C 39 O O . GLY A 6 ? 0.5278 0.4029 0.3812 0.2273 0.0715 0.0290 6 GLY A O 40 N N . THR A 7 ? 0.4371 0.2221 0.4384 0.1127 0.0071 0.0091 7 THR A N 41 C CA . THR A 7 ? 0.2972 0.2589 0.3521 0.0823 0.0126 -0.0114 7 THR A CA 42 C C . THR A 7 ? 0.2169 0.2384 0.3926 0.0922 -0.0333 0.0196 7 THR A C 43 O O . THR A 7 ? 0.2282 0.2903 0.3916 0.0761 -0.0377 -0.0070 7 THR A O 44 C CB . THR A 7 ? 0.2322 0.2127 0.4941 0.0700 0.0503 0.0225 7 THR A CB 45 O OG1 . THR A 7 ? 0.3823 0.3258 0.5165 0.0984 0.1467 0.0658 7 THR A OG1 46 C CG2 . THR A 7 ? 0.2095 0.2771 0.4344 0.0971 -0.0129 -0.0416 7 THR A CG2 47 N N . ARG A 8 ? 0.2375 0.2979 0.4118 0.0609 -0.0287 0.0287 8 ARG A N 48 C CA . ARG A 8 ? 0.1679 0.2893 0.2856 0.0833 0.0205 -0.0376 8 ARG A CA 49 C C . ARG A 8 ? 0.2186 0.2905 0.2420 0.1020 -0.0329 -0.0525 8 ARG A C 50 O O . ARG A 8 ? 0.3260 0.3426 0.2277 0.1133 -0.0361 -0.0552 8 ARG A O 51 C CB . ARG A 8 ? 0.1681 0.3072 0.3659 0.0189 -0.0012 -0.1299 8 ARG A CB 52 C CG . ARG A 8 ? 0.2963 0.4318 0.5506 0.0365 0.1807 0.0166 8 ARG A CG 53 C CD . ARG A 8 ? 0.3184 0.4864 0.6975 0.1253 0.2455 -0.0413 8 ARG A CD 54 N NE . ARG A 8 ? 0.2500 0.5474 0.8228 0.0468 0.2138 0.0103 8 ARG A NE 55 C CZ . ARG A 8 ? 0.2493 0.6026 0.7085 -0.0093 0.2566 0.0423 8 ARG A CZ 56 N NH1 . ARG A 8 ? 0.3545 0.5434 0.5715 0.0047 0.2650 -0.0913 8 ARG A NH1 57 N NH2 . ARG A 8 ? 0.6167 0.4890 0.5049 -0.0168 0.2545 0.0626 8 ARG A NH2 58 N N . VAL A 9 ? 0.2004 0.2534 0.2757 0.0796 -0.0460 -0.0660 9 VAL A N 59 C CA . VAL A 9 ? 0.1929 0.2222 0.2540 0.0619 0.0396 0.0038 9 VAL A CA 60 C C . VAL A 9 ? 0.2545 0.1976 0.2236 0.0024 0.0418 -0.0386 9 VAL A C 61 O O . VAL A 9 ? 0.1996 0.2556 0.2211 0.0036 0.0254 -0.0454 9 VAL A O 62 C CB . VAL A 9 ? 0.1890 0.2403 0.3028 0.0430 0.0303 0.0372 9 VAL A CB 63 C CG1 . VAL A 9 ? 0.1879 0.3331 0.3130 0.0454 0.0308 0.0781 9 VAL A CG1 64 C CG2 . VAL A 9 ? 0.2876 0.3414 0.3567 0.0034 -0.0979 0.0785 9 VAL A CG2 65 N N . SER A 10 ? 0.3071 0.1900 0.2268 0.0148 0.0380 -0.0122 10 SER A N 66 C CA . SER A 10 ? 0.2781 0.1989 0.2544 -0.0116 0.0629 -0.0023 10 SER A CA 67 C C . SER A 10 ? 0.3062 0.3356 0.2180 -0.0484 0.0689 0.0500 10 SER A C 68 O O . SER A 10 ? 0.3318 0.4397 0.2334 -0.0191 0.1155 0.0377 10 SER A O 69 C CB . SER A 10 ? 0.2998 0.2130 0.3795 0.0902 0.0230 -0.0170 10 SER A CB 70 O OG . SER A 10 ? 0.2979 0.4539 0.3472 0.1587 0.0211 -0.0188 10 SER A OG 71 N N . HIS A 11 ? 0.2539 0.2084 0.1779 0.0338 0.0578 0.0149 11 HIS A N 72 C CA . HIS A 11 ? 0.2793 0.2591 0.1405 0.0334 0.0603 0.0395 11 HIS A CA 73 C C . HIS A 11 ? 0.2220 0.2598 0.1353 0.0376 0.0528 0.0174 11 HIS A C 74 O O . HIS A 11 ? 0.2062 0.2459 0.1355 0.0453 0.0345 0.0340 11 HIS A O 75 C CB . HIS A 11 ? 0.2643 0.2604 0.2023 0.0291 0.0340 0.0399 11 HIS A CB 76 C CG . HIS A 11 ? 0.3443 0.2613 0.1688 0.0294 0.0577 0.0425 11 HIS A CG 77 N ND1 . HIS A 11 ? 0.5855 0.4327 0.2602 -0.1161 0.0266 0.1495 11 HIS A ND1 78 C CD2 . HIS A 11 ? 0.3189 0.2555 0.2778 0.0412 0.0593 -0.0145 11 HIS A CD2 79 C CE1 . HIS A 11 ? 0.6056 0.4092 0.4681 -0.1415 0.0820 0.1697 11 HIS A CE1 80 N NE2 . HIS A 11 ? 0.5118 0.2622 0.4998 -0.0093 0.0319 0.0378 11 HIS A NE2 81 N N . ALA A 12 ? 0.3257 0.2793 0.1431 0.0272 0.0706 -0.0054 12 ALA A N 82 C CA . ALA A 12 ? 0.3353 0.2273 0.1420 0.0562 0.0438 -0.0138 12 ALA A CA 83 C C . ALA A 12 ? 0.3001 0.2264 0.1191 0.0449 0.0230 0.0130 12 ALA A C 84 O O . ALA A 12 ? 0.2868 0.2112 0.1424 0.0178 -0.0065 -0.0125 12 ALA A O 85 C CB . ALA A 12 ? 0.5099 0.3719 0.1590 -0.0121 0.0734 -0.0913 12 ALA A CB 86 N N . ALA A 13 ? 0.2976 0.2674 0.1222 0.0751 -0.0007 0.0114 13 ALA A N 87 C CA . ALA A 13 ? 0.2242 0.3160 0.1871 0.0656 -0.0450 0.0194 13 ALA A CA 88 C C . ALA A 13 ? 0.1769 0.2209 0.1793 -0.0015 0.0182 -0.0477 13 ALA A C 89 O O . ALA A 13 ? 0.1910 0.3104 0.2434 0.0353 0.0589 -0.0449 13 ALA A O 90 C CB . ALA A 13 ? 0.4711 0.5952 0.4028 0.3230 0.0511 0.1951 13 ALA A CB 91 N N . CYS A 14 ? 0.2015 0.1609 0.1258 -0.0027 -0.0022 -0.0141 14 CYS A N 92 C CA . CYS A 14 ? 0.2032 0.1528 0.1181 -0.0126 0.0298 -0.0138 14 CYS A CA 93 C C . CYS A 14 ? 0.1427 0.1474 0.1284 0.0060 0.0177 -0.0206 14 CYS A C 94 O O . CYS A 14 ? 0.1496 0.1614 0.1142 0.0095 0.0284 -0.0078 14 CYS A O 95 C CB A CYS A 14 ? 0.2473 0.1262 0.0858 -0.0172 0.0093 -0.0185 14 CYS A CB 96 C CB B CYS A 14 ? 0.2824 0.3524 0.1548 -0.1696 -0.0268 -0.0121 14 CYS A CB 97 S SG A CYS A 14 ? 0.1545 0.1295 0.0842 -0.0208 0.0060 -0.0091 14 CYS A SG 98 S SG B CYS A 14 ? 0.3295 0.3795 0.3255 -0.1610 0.0969 -0.0096 14 CYS A SG 99 N N . CYS A 15 ? 0.1591 0.1463 0.1186 0.0124 0.0338 -0.0092 15 CYS A N 100 C CA . CYS A 15 ? 0.1685 0.1434 0.1408 0.0225 0.0383 -0.0064 15 CYS A CA 101 C C . CYS A 15 ? 0.1489 0.1261 0.1152 0.0272 0.0219 -0.0098 15 CYS A C 102 O O . CYS A 15 ? 0.1709 0.1496 0.1339 0.0474 0.0293 0.0165 15 CYS A O 103 C CB . CYS A 15 ? 0.1966 0.1662 0.1505 0.0316 0.0437 -0.0235 15 CYS A CB 104 S SG . CYS A 15 ? 0.2439 0.2396 0.2364 0.0327 0.0910 -0.0387 15 CYS A SG 105 N N . ALA A 16 ? 0.1560 0.1367 0.1067 0.0136 0.0091 -0.0088 16 ALA A N 106 C CA . ALA A 16 ? 0.1502 0.1336 0.1187 0.0020 0.0114 -0.0212 16 ALA A CA 107 C C . ALA A 16 ? 0.1358 0.1054 0.1077 0.0242 0.0085 -0.0054 16 ALA A C 108 O O . ALA A 16 ? 0.1437 0.1090 0.1183 0.0116 0.0179 -0.0108 16 ALA A O 109 C CB . ALA A 16 ? 0.1632 0.2343 0.1210 -0.0028 -0.0127 -0.0470 16 ALA A CB 110 N N . PHE A 17 ? 0.1266 0.1091 0.1009 0.0157 0.0103 -0.0044 17 PHE A N 111 C CA . PHE A 17 ? 0.1298 0.1063 0.0935 0.0109 0.0091 0.0016 17 PHE A CA 112 C C . PHE A 17 ? 0.1244 0.1121 0.1051 0.0224 0.0075 -0.0010 17 PHE A C 113 O O . PHE A 17 ? 0.1612 0.1124 0.1033 0.0245 0.0072 0.0119 17 PHE A O 114 C CB . PHE A 17 ? 0.1098 0.1091 0.1083 0.0029 0.0040 -0.0004 17 PHE A CB 115 C CG . PHE A 17 ? 0.1248 0.1011 0.0937 0.0060 0.0071 0.0022 17 PHE A CG 116 C CD1 . PHE A 17 ? 0.1279 0.1341 0.0989 0.0254 0.0171 0.0022 17 PHE A CD1 117 C CD2 . PHE A 17 ? 0.1254 0.0999 0.0903 -0.0004 0.0054 -0.0036 17 PHE A CD2 118 C CE1 . PHE A 17 ? 0.1515 0.1312 0.0983 0.0294 0.0136 0.0101 17 PHE A CE1 119 C CE2 . PHE A 17 ? 0.1084 0.0990 0.1006 0.0002 0.0050 -0.0030 17 PHE A CE2 120 C CZ . PHE A 17 ? 0.1212 0.0997 0.1013 0.0047 -0.0040 -0.0068 17 PHE A CZ 121 N N . ILE A 18 ? 0.1293 0.1296 0.1158 0.0211 0.0109 0.0054 18 ILE A N 122 C CA . ILE A 18 ? 0.1464 0.1295 0.1274 0.0385 0.0125 0.0063 18 ILE A CA 123 C C . ILE A 18 ? 0.1432 0.1212 0.1284 0.0362 0.0049 0.0044 18 ILE A C 124 O O . ILE A 18 ? 0.1558 0.1423 0.1259 0.0386 -0.0024 0.0133 18 ILE A O 125 C CB . ILE A 18 ? 0.1512 0.1624 0.1605 0.0503 0.0145 0.0092 18 ILE A CB 126 C CG1 . ILE A 18 ? 0.1876 0.2074 0.2088 0.0479 0.0665 0.0354 18 ILE A CG1 127 C CG2 . ILE A 18 ? 0.1588 0.2206 0.2407 0.0713 0.0051 0.0610 18 ILE A CG2 128 C CD1 . ILE A 18 ? 0.2428 0.3732 0.4158 0.1221 0.1758 0.1374 18 ILE A CD1 129 N N . PRO A 19 ? 0.1660 0.1173 0.1128 0.0409 0.0152 -0.0024 19 PRO A N 130 C CA . PRO A 19 ? 0.1861 0.1035 0.1418 0.0314 0.0317 0.0002 19 PRO A CA 131 C C . PRO A 19 ? 0.1541 0.0982 0.1156 0.0248 0.0100 0.0034 19 PRO A C 132 O O . PRO A 19 ? 0.1646 0.1038 0.1155 0.0228 0.0094 0.0047 19 PRO A O 133 C CB . PRO A 19 ? 0.2517 0.1224 0.1415 0.0174 0.0447 -0.0192 19 PRO A CB 134 C CG . PRO A 19 ? 0.2643 0.1394 0.1616 -0.0073 -0.0192 -0.0133 19 PRO A CG 135 C CD . PRO A 19 ? 0.1905 0.1204 0.1286 0.0403 0.0181 -0.0139 19 PRO A CD 136 N N . LEU A 20 ? 0.1431 0.1021 0.1000 0.0220 0.0066 -0.0024 20 LEU A N 137 C CA . LEU A 20 ? 0.1216 0.1004 0.0975 0.0198 0.0059 -0.0004 20 LEU A CA 138 C C . LEU A 20 ? 0.1248 0.0908 0.0963 0.0197 -0.0078 0.0030 20 LEU A C 139 O O . LEU A 20 ? 0.1267 0.0992 0.0925 0.0222 -0.0028 0.0059 20 LEU A O 140 C CB . LEU A 20 ? 0.1297 0.1013 0.0915 0.0121 0.0027 0.0025 20 LEU A CB 141 C CG . LEU A 20 ? 0.1186 0.0884 0.0974 0.0094 0.0063 0.0024 20 LEU A CG 142 C CD1 . LEU A 20 ? 0.1114 0.1049 0.1159 0.0057 -0.0034 0.0091 20 LEU A CD1 143 C CD2 . LEU A 20 ? 0.1173 0.0974 0.1135 0.0076 -0.0104 0.0117 20 LEU A CD2 144 N N . ALA A 21 ? 0.1280 0.0934 0.0952 0.0162 -0.0002 0.0062 21 ALA A N 145 C CA . ALA A 21 ? 0.1168 0.0985 0.0969 0.0129 0.0038 -0.0007 21 ALA A CA 146 C C . ALA A 21 ? 0.1093 0.0991 0.1084 0.0130 -0.0091 0.0051 21 ALA A C 147 O O . ALA A 21 ? 0.1235 0.1179 0.0953 0.0170 -0.0021 0.0023 21 ALA A O 148 C CB . ALA A 21 ? 0.1216 0.1204 0.1352 0.0070 -0.0058 0.0239 21 ALA A CB 149 N N . GLN A 22 ? 0.1247 0.1040 0.1113 0.0205 0.0040 0.0077 22 GLN A N 150 C CA . GLN A 22 ? 0.1407 0.1000 0.1205 0.0272 -0.0039 0.0123 22 GLN A CA 151 C C . GLN A 22 ? 0.1301 0.0871 0.1193 0.0292 -0.0020 0.0123 22 GLN A C 152 O O . GLN A 22 ? 0.1441 0.1106 0.1154 0.0249 -0.0100 0.0143 22 GLN A O 153 C CB . GLN A 22 ? 0.1795 0.1069 0.1565 0.0444 0.0205 0.0140 22 GLN A CB 154 C CG . GLN A 22 ? 0.2135 0.1965 0.2064 0.0353 0.0569 0.0048 22 GLN A CG 155 C CD . GLN A 22 ? 0.3081 0.2175 0.3695 0.1320 0.1443 0.0243 22 GLN A CD 156 O OE1 . GLN A 22 ? 0.2682 0.5824 0.5347 0.1978 0.1500 -0.0218 22 GLN A OE1 157 N NE2 . GLN A 22 ? 0.4383 0.3878 0.7994 0.1010 0.1133 -0.3490 22 GLN A NE2 158 N N . ASP A 23 ? 0.1350 0.0881 0.1081 0.0199 0.0013 0.0043 23 ASP A N 159 C CA . ASP A 23 ? 0.1277 0.0878 0.1135 0.0223 -0.0001 0.0125 23 ASP A CA 160 C C . ASP A 23 ? 0.1207 0.0783 0.0985 0.0108 -0.0133 0.0042 23 ASP A C 161 O O . ASP A 23 ? 0.1442 0.0846 0.1058 0.0055 0.0004 0.0116 23 ASP A O 162 C CB . ASP A 23 ? 0.1455 0.0990 0.1127 0.0094 -0.0056 -0.0074 23 ASP A CB 163 C CG . ASP A 23 ? 0.1664 0.1128 0.1169 -0.0037 -0.0113 -0.0049 23 ASP A CG 164 O OD1 . ASP A 23 ? 0.2067 0.1273 0.1251 -0.0247 -0.0192 0.0088 23 ASP A OD1 165 O OD2 . ASP A 23 ? 0.1709 0.1345 0.1263 -0.0124 -0.0153 -0.0032 23 ASP A OD2 166 N N . LEU A 24 ? 0.1211 0.0836 0.0882 0.0095 -0.0047 0.0059 24 LEU A N 167 C CA . LEU A 24 ? 0.1240 0.0745 0.0893 0.0183 -0.0027 0.0072 24 LEU A CA 168 C C . LEU A 24 ? 0.1264 0.0788 0.0957 0.0185 -0.0151 0.0052 24 LEU A C 169 O O . LEU A 24 ? 0.1374 0.0875 0.0925 0.0120 -0.0057 0.0084 24 LEU A O 170 C CB . LEU A 24 ? 0.1284 0.0795 0.0910 0.0053 -0.0049 0.0081 24 LEU A CB 171 C CG . LEU A 24 ? 0.1232 0.0813 0.0950 0.0100 -0.0043 0.0062 24 LEU A CG 172 C CD1 . LEU A 24 ? 0.1393 0.1020 0.1081 0.0169 -0.0061 0.0246 24 LEU A CD1 173 C CD2 . LEU A 24 ? 0.1265 0.1250 0.1206 0.0240 -0.0008 0.0195 24 LEU A CD2 174 N N . GLN A 25 ? 0.1284 0.0880 0.0996 0.0145 -0.0144 0.0107 25 GLN A N 175 C CA . GLN A 25 ? 0.1381 0.1071 0.1117 0.0131 -0.0360 -0.0029 25 GLN A CA 176 C C . GLN A 25 ? 0.1506 0.1158 0.1066 0.0312 -0.0277 0.0081 25 GLN A C 177 O O . GLN A 25 ? 0.2182 0.1524 0.1046 0.0497 -0.0209 0.0182 25 GLN A O 178 C CB . GLN A 25 ? 0.1434 0.1118 0.1362 0.0261 -0.0241 -0.0177 25 GLN A CB 179 C CG . GLN A 25 ? 0.1336 0.1291 0.1426 0.0045 -0.0210 -0.0117 25 GLN A CG 180 C CD . GLN A 25 ? 0.1291 0.1222 0.1236 -0.0059 -0.0315 -0.0052 25 GLN A CD 181 O OE1 . GLN A 25 ? 0.1370 0.1425 0.1319 -0.0008 -0.0166 -0.0171 25 GLN A OE1 182 N NE2 . GLN A 25 ? 0.1330 0.1191 0.1311 -0.0060 -0.0149 -0.0052 25 GLN A NE2 183 N N . GLU A 26 ? 0.1362 0.1040 0.1169 0.0161 -0.0094 0.0215 26 GLU A N 184 C CA . GLU A 26 ? 0.1455 0.1034 0.1694 0.0336 0.0023 0.0478 26 GLU A CA 185 C C . GLU A 26 ? 0.1453 0.0847 0.1227 0.0244 -0.0105 0.0240 26 GLU A C 186 O O . GLU A 26 ? 0.1433 0.1304 0.1490 0.0215 -0.0101 0.0599 26 GLU A O 187 C CB . GLU A 26 ? 0.2595 0.0925 0.2361 0.0559 0.0864 0.0452 26 GLU A CB 188 C CG . GLU A 26 ? 0.3600 0.3067 0.2751 0.1990 0.1505 0.1005 26 GLU A CG 189 C CD . GLU A 26 ? 0.4958 0.3355 0.2713 0.1755 0.2099 0.0916 26 GLU A CD 190 O OE1 . GLU A 26 ? 0.6772 0.3535 0.7585 0.2327 -0.0140 -0.1638 26 GLU A OE1 191 O OE2 . GLU A 26 ? 0.5912 0.8008 0.4935 0.3309 0.2736 -0.0805 26 GLU A OE2 192 N N . THR A 27 ? 0.1356 0.0743 0.1109 0.0152 -0.0047 0.0157 27 THR A N 193 C CA . THR A 27 ? 0.1355 0.0706 0.1057 0.0058 -0.0134 0.0121 27 THR A CA 194 C C . THR A 27 ? 0.1311 0.0687 0.1019 0.0080 -0.0142 0.0087 27 THR A C 195 O O . THR A 27 ? 0.1586 0.0816 0.1154 0.0003 0.0110 0.0119 27 THR A O 196 C CB . THR A 27 ? 0.1347 0.0779 0.1154 0.0055 -0.0102 -0.0045 27 THR A CB 197 O OG1 . THR A 27 ? 0.1813 0.1035 0.1171 -0.0152 -0.0024 -0.0179 27 THR A OG1 198 C CG2 . THR A 27 ? 0.1425 0.0900 0.1485 -0.0102 -0.0228 0.0057 27 THR A CG2 199 N N . ILE A 28 ? 0.1231 0.0729 0.0934 0.0063 -0.0079 0.0085 28 ILE A N 200 C CA . ILE A 28 ? 0.1189 0.0691 0.1011 0.0056 0.0012 0.0028 28 ILE A CA 201 C C . ILE A 28 ? 0.1210 0.0710 0.0961 0.0100 -0.0149 0.0109 28 ILE A C 202 O O . ILE A 28 ? 0.1336 0.0917 0.1013 0.0010 -0.0021 0.0020 28 ILE A O 203 C CB . ILE A 28 ? 0.1271 0.0741 0.1082 0.0063 -0.0215 0.0022 28 ILE A CB 204 C CG1 . ILE A 28 ? 0.1124 0.0812 0.1108 0.0057 -0.0143 -0.0004 28 ILE A CG1 205 C CG2 . ILE A 28 ? 0.1200 0.0927 0.1398 0.0040 -0.0124 0.0018 28 ILE A CG2 206 C CD1 . ILE A 28 ? 0.1241 0.0886 0.1186 0.0069 -0.0188 0.0114 28 ILE A CD1 207 N N . PHE A 29 ? 0.1124 0.0775 0.0936 0.0068 -0.0082 0.0075 29 PHE A N 208 C CA . PHE A 29 ? 0.1263 0.0773 0.0955 -0.0017 -0.0204 0.0032 29 PHE A CA 209 C C . PHE A 29 ? 0.1235 0.0727 0.1189 -0.0043 -0.0156 0.0074 29 PHE A C 210 O O . PHE A 29 ? 0.1331 0.1130 0.1156 -0.0066 -0.0374 -0.0045 29 PHE A O 211 C CB . PHE A 29 ? 0.1126 0.0819 0.1148 0.0053 -0.0110 0.0066 29 PHE A CB 212 C CG . PHE A 29 ? 0.1246 0.0743 0.0978 0.0008 -0.0059 0.0108 29 PHE A CG 213 C CD1 . PHE A 29 ? 0.1285 0.0834 0.1123 0.0121 0.0101 0.0104 29 PHE A CD1 214 C CD2 . PHE A 29 ? 0.1201 0.0813 0.0978 0.0026 -0.0072 -0.0018 29 PHE A CD2 215 C CE1 . PHE A 29 ? 0.1527 0.0957 0.0978 0.0037 -0.0072 0.0087 29 PHE A CE1 216 C CE2 . PHE A 29 ? 0.1369 0.0766 0.1120 0.0117 -0.0116 0.0039 29 PHE A CE2 217 C CZ . PHE A 29 ? 0.1422 0.0785 0.1042 0.0063 -0.0202 0.0023 29 PHE A CZ 218 N N . GLN A 30 ? 0.1409 0.0872 0.1197 0.0051 -0.0321 0.0124 30 GLN A N 219 C CA . GLN A 30 ? 0.1492 0.0876 0.1258 0.0136 -0.0443 0.0145 30 GLN A CA 220 C C . GLN A 30 ? 0.1512 0.0813 0.1310 0.0102 -0.0352 0.0196 30 GLN A C 221 O O . GLN A 30 ? 0.1492 0.1026 0.1487 0.0061 -0.0509 0.0291 30 GLN A O 222 C CB . GLN A 30 ? 0.1532 0.1122 0.1511 -0.0104 -0.0510 0.0437 30 GLN A CB 223 C CG . GLN A 30 ? 0.1684 0.1002 0.2047 0.0027 -0.0423 0.0366 30 GLN A CG 224 C CD . GLN A 30 ? 0.1580 0.0948 0.1333 -0.0097 -0.0469 0.0261 30 GLN A CD 225 O OE1 . GLN A 30 ? 0.1657 0.1070 0.1533 0.0017 -0.0507 0.0217 30 GLN A OE1 226 N NE2 . GLN A 30 ? 0.1681 0.1059 0.1423 -0.0065 -0.0237 0.0332 30 GLN A NE2 227 N N . ASN A 31 ? 0.1471 0.0940 0.1198 0.0120 -0.0225 0.0133 31 ASN A N 228 C CA . ASN A 31 ? 0.1354 0.1062 0.1415 0.0120 -0.0219 0.0207 31 ASN A CA 229 C C . ASN A 31 ? 0.1412 0.1011 0.1305 -0.0017 -0.0334 0.0178 31 ASN A C 230 O O . ASN A 31 ? 0.1501 0.1960 0.1973 -0.0298 -0.0410 -0.0004 31 ASN A O 231 C CB . ASN A 31 ? 0.1391 0.1385 0.2159 0.0227 -0.0066 0.0319 31 ASN A CB 232 C CG . ASN A 31 ? 0.2149 0.2146 0.2863 0.1150 -0.0304 -0.0307 31 ASN A CG 233 O OD1 . ASN A 31 ? 0.9200 0.2018 0.4782 0.1929 -0.0023 -0.0235 31 ASN A OD1 234 N ND2 . ASN A 31 ? 0.3082 0.3909 0.2641 0.2023 -0.0672 -0.0799 31 ASN A ND2 235 N N . GLU A 32 ? 0.1387 0.0930 0.1389 0.0113 -0.0385 0.0088 32 GLU A N 236 C CA . GLU A 32 ? 0.1625 0.1034 0.1145 0.0143 -0.0462 0.0136 32 GLU A CA 237 C C . GLU A 32 ? 0.1184 0.0873 0.1162 0.0064 -0.0281 0.0203 32 GLU A C 238 O O . GLU A 32 ? 0.1207 0.1096 0.1155 0.0068 -0.0291 0.0109 32 GLU A O 239 C CB . GLU A 32 ? 0.2826 0.1143 0.1312 -0.0144 -0.0181 0.0373 32 GLU A CB 240 C CG . GLU A 32 ? 0.2916 0.1676 0.1717 0.0244 -0.0031 0.0698 32 GLU A CG 241 C CD . GLU A 32 ? 0.4973 0.1436 0.2380 0.0544 -0.1496 0.0132 32 GLU A CD 242 O OE1 . GLU A 32 ? 0.8118 0.1867 0.5184 0.1115 -0.4134 0.0089 32 GLU A OE1 243 O OE2 . GLU A 32 ? 0.5252 0.1701 0.3183 0.0409 -0.0894 -0.0520 32 GLU A OE2 244 N N . CYS A 33 ? 0.1409 0.1004 0.1113 0.0058 -0.0340 0.0064 33 CYS A N 245 C CA . CYS A 33 ? 0.1353 0.1098 0.1181 0.0139 -0.0132 -0.0081 33 CYS A CA 246 C C . CYS A 33 ? 0.1341 0.1072 0.1066 -0.0094 -0.0184 -0.0031 33 CYS A C 247 O O . CYS A 33 ? 0.1954 0.1307 0.1408 -0.0037 -0.0019 -0.0187 33 CYS A O 248 C CB . CYS A 33 ? 0.1345 0.1162 0.1844 -0.0258 -0.0008 0.0047 33 CYS A CB 249 S SG . CYS A 33 ? 0.1520 0.1092 0.1598 -0.0029 0.0013 -0.0073 33 CYS A SG 250 N N . GLY A 34 ? 0.1207 0.1141 0.1002 0.0075 -0.0267 0.0105 34 GLY A N 251 C CA . GLY A 34 ? 0.1124 0.1326 0.1102 -0.0004 -0.0304 0.0311 34 GLY A CA 252 C C . GLY A 34 ? 0.1159 0.0760 0.0911 0.0032 -0.0194 0.0122 34 GLY A C 253 O O . GLY A 34 ? 0.1205 0.0900 0.0929 0.0013 -0.0261 0.0156 34 GLY A O 254 N N . GLU A 35 ? 0.1199 0.0926 0.0906 0.0036 -0.0185 0.0242 35 GLU A N 255 C CA . GLU A 35 ? 0.1114 0.0828 0.0780 -0.0005 -0.0127 0.0021 35 GLU A CA 256 C C . GLU A 35 ? 0.1015 0.0705 0.0885 -0.0111 -0.0131 0.0017 35 GLU A C 257 O O . GLU A 35 ? 0.1132 0.0746 0.0955 0.0034 -0.0163 0.0011 35 GLU A O 258 C CB . GLU A 35 ? 0.1339 0.1114 0.0873 -0.0087 -0.0030 0.0071 35 GLU A CB 259 C CG . GLU A 35 ? 0.1235 0.1424 0.1090 -0.0306 -0.0003 -0.0100 35 GLU A CG 260 C CD . GLU A 35 ? 0.1247 0.1523 0.0933 0.0033 -0.0193 -0.0170 35 GLU A CD 261 O OE1 . GLU A 35 ? 0.1519 0.1540 0.1152 -0.0175 -0.0254 -0.0063 35 GLU A OE1 262 O OE2 . GLU A 35 ? 0.1384 0.1200 0.1097 0.0072 -0.0306 -0.0042 35 GLU A OE2 263 N N . ASP A 36 ? 0.1192 0.0676 0.0779 0.0016 -0.0147 0.0093 36 ASP A N 264 C CA . ASP A 36 ? 0.1191 0.0619 0.0789 -0.0021 -0.0125 0.0055 36 ASP A CA 265 C C . ASP A 36 ? 0.1151 0.0645 0.0801 0.0066 -0.0096 0.0046 36 ASP A C 266 O O . ASP A 36 ? 0.1111 0.0803 0.0826 0.0014 -0.0189 0.0079 36 ASP A O 267 C CB . ASP A 36 ? 0.1395 0.0687 0.0907 -0.0094 -0.0111 0.0026 36 ASP A CB 268 C CG . ASP A 36 ? 0.1287 0.0719 0.1009 -0.0054 -0.0158 0.0042 36 ASP A CG 269 O OD1 . ASP A 36 ? 0.1614 0.0798 0.1389 -0.0104 -0.0015 -0.0076 36 ASP A OD1 270 O OD2 . ASP A 36 ? 0.1500 0.0870 0.1685 -0.0150 0.0247 -0.0063 36 ASP A OD2 271 N N . ALA A 37 ? 0.1057 0.0700 0.0825 0.0023 -0.0190 0.0075 37 ALA A N 272 C CA . ALA A 37 ? 0.1008 0.0790 0.0793 0.0013 -0.0110 0.0065 37 ALA A CA 273 C C . ALA A 37 ? 0.0893 0.0672 0.0833 0.0031 -0.0270 0.0074 37 ALA A C 274 O O . ALA A 37 ? 0.0997 0.0781 0.0803 0.0044 -0.0236 0.0089 37 ALA A O 275 C CB . ALA A 37 ? 0.0944 0.0848 0.1078 0.0129 -0.0225 0.0124 37 ALA A CB 276 N N . HIS A 38 ? 0.1015 0.0676 0.0789 0.0023 -0.0233 0.0077 38 HIS A N 277 C CA . HIS A 38 ? 0.0936 0.0686 0.0837 0.0006 -0.0241 0.0048 38 HIS A CA 278 C C . HIS A 38 ? 0.0964 0.0661 0.0678 0.0092 -0.0185 -0.0009 38 HIS A C 279 O O . HIS A 38 ? 0.1095 0.0670 0.0824 0.0056 -0.0283 0.0031 38 HIS A O 280 C CB . HIS A 38 ? 0.1244 0.0684 0.0890 0.0081 -0.0410 -0.0030 38 HIS A CB 281 C CG . HIS A 38 ? 0.1551 0.0621 0.1146 -0.0025 -0.0635 0.0065 38 HIS A CG 282 N ND1 . HIS A 38 ? 0.1880 0.0880 0.1045 0.0030 -0.0766 0.0062 38 HIS A ND1 283 C CD2 . HIS A 38 ? 0.1436 0.1061 0.1544 -0.0353 -0.0783 0.0352 38 HIS A CD2 284 C CE1 . HIS A 38 ? 0.2011 0.1023 0.1463 -0.0243 -0.1083 0.0132 38 HIS A CE1 285 N NE2 . HIS A 38 ? 0.1729 0.1414 0.1821 -0.0493 -0.1141 0.0614 38 HIS A NE2 286 N N . GLU A 39 ? 0.0893 0.0766 0.0703 0.0028 -0.0215 -0.0031 39 GLU A N 287 C CA . GLU A 39 ? 0.0862 0.0787 0.0765 0.0015 -0.0173 -0.0007 39 GLU A CA 288 C C . GLU A 39 ? 0.0824 0.0697 0.0828 -0.0003 -0.0245 0.0020 39 GLU A C 289 O O . GLU A 39 ? 0.0885 0.0829 0.0873 0.0066 -0.0208 0.0025 39 GLU A O 290 C CB . GLU A 39 ? 0.0891 0.1287 0.0843 -0.0244 -0.0126 0.0121 39 GLU A CB 291 C CG . GLU A 39 ? 0.1028 0.2304 0.0751 -0.0314 -0.0089 0.0137 39 GLU A CG 292 C CD . GLU A 39 ? 0.1611 0.2870 0.0942 0.0389 -0.0104 0.0166 39 GLU A CD 293 O OE1 . GLU A 39 ? 0.1587 0.3729 0.2342 0.0303 -0.0296 0.1221 39 GLU A OE1 294 O OE2 . GLU A 39 ? 0.1504 0.2825 0.1220 -0.0255 -0.0067 -0.0284 39 GLU A OE2 295 N N . VAL A 40 ? 0.0871 0.0717 0.0684 0.0026 -0.0137 0.0080 40 VAL A N 296 C CA . VAL A 40 ? 0.0928 0.0673 0.0721 0.0048 -0.0158 0.0044 40 VAL A CA 297 C C . VAL A 40 ? 0.0845 0.0679 0.0830 0.0071 -0.0143 0.0065 40 VAL A C 298 O O . VAL A 40 ? 0.1021 0.0800 0.0737 0.0048 -0.0220 0.0121 40 VAL A O 299 C CB . VAL A 40 ? 0.1042 0.0710 0.0814 0.0068 -0.0054 -0.0008 40 VAL A CB 300 C CG1 . VAL A 40 ? 0.1381 0.1020 0.0957 0.0141 0.0178 -0.0026 40 VAL A CG1 301 C CG2 . VAL A 40 ? 0.1249 0.0731 0.0879 -0.0003 -0.0210 -0.0001 40 VAL A CG2 302 N N . ILE A 41 ? 0.0996 0.0683 0.0780 -0.0056 -0.0294 0.0111 41 ILE A N 303 C CA . ILE A 41 ? 0.0942 0.0761 0.0786 -0.0076 -0.0151 0.0103 41 ILE A CA 304 C C . ILE A 41 ? 0.1022 0.0617 0.0833 0.0005 -0.0292 0.0098 41 ILE A C 305 O O . ILE A 41 ? 0.1088 0.0752 0.0819 -0.0017 -0.0229 0.0158 41 ILE A O 306 C CB . ILE A 41 ? 0.0866 0.0806 0.0852 -0.0015 -0.0178 0.0036 41 ILE A CB 307 C CG1 . ILE A 41 ? 0.0982 0.0932 0.0974 0.0082 -0.0213 0.0009 41 ILE A CG1 308 C CG2 . ILE A 41 ? 0.1083 0.0813 0.1055 -0.0081 -0.0177 0.0047 41 ILE A CG2 309 C CD1 . ILE A 41 ? 0.1027 0.1185 0.1084 0.0020 -0.0295 0.0111 41 ILE A CD1 310 N N . ARG A 42 ? 0.1012 0.0651 0.0800 0.0024 -0.0282 0.0096 42 ARG A N 311 C CA . ARG A 42 ? 0.0991 0.0722 0.0701 -0.0016 -0.0280 0.0032 42 ARG A CA 312 C C . ARG A 42 ? 0.0979 0.0704 0.0783 0.0027 -0.0196 0.0048 42 ARG A C 313 O O . ARG A 42 ? 0.1059 0.0731 0.0808 0.0093 -0.0237 0.0086 42 ARG A O 314 C CB A ARG A 42 ? 0.0906 0.0897 0.0720 -0.0075 -0.0280 0.0114 42 ARG A CB 315 C CB B ARG A 42 ? 0.1229 0.1076 0.0774 -0.0291 -0.0120 0.0060 42 ARG A CB 316 C CG A ARG A 42 ? 0.0931 0.1188 0.0573 0.0115 -0.0368 0.0075 42 ARG A CG 317 C CG B ARG A 42 ? 0.1011 0.1915 0.0914 -0.0217 -0.0170 -0.0108 42 ARG A CG 318 C CD A ARG A 42 ? 0.0968 0.1012 0.0770 -0.0023 -0.0192 0.0004 42 ARG A CD 319 C CD B ARG A 42 ? 0.1365 0.2300 0.1104 -0.0440 0.0056 -0.0064 42 ARG A CD 320 N NE A ARG A 42 ? 0.1072 0.2232 0.0872 0.0560 -0.0060 0.0530 42 ARG A NE 321 N NE B ARG A 42 ? 0.1483 0.3448 0.1535 -0.0157 0.0194 -0.0219 42 ARG A NE 322 C CZ A ARG A 42 ? 0.1016 0.4718 0.0447 0.0539 0.0009 0.0269 42 ARG A CZ 323 C CZ B ARG A 42 ? 0.1594 0.5045 0.1069 -0.0619 0.0433 -0.0489 42 ARG A CZ 324 N NH1 A ARG A 42 ? 0.1539 0.5790 0.0731 -0.1523 -0.0036 -0.0561 42 ARG A NH1 325 N NH1 B ARG A 42 ? 0.1777 0.4986 0.3718 -0.1978 0.0329 0.0097 42 ARG A NH1 326 N NH2 A ARG A 42 ? 0.1876 0.7405 0.0789 0.2449 0.0348 0.1044 42 ARG A NH2 327 N NH2 B ARG A 42 ? 0.1365 0.7143 0.2099 -0.0131 -0.0057 -0.1409 42 ARG A NH2 328 N N . LEU A 43 ? 0.1169 0.0714 0.0742 0.0044 -0.0338 0.0055 43 LEU A N 329 C CA . LEU A 43 ? 0.1032 0.0778 0.0865 0.0067 -0.0379 0.0002 43 LEU A CA 330 C C . LEU A 43 ? 0.0986 0.0754 0.0825 0.0173 -0.0382 -0.0004 43 LEU A C 331 O O . LEU A 43 ? 0.1012 0.0838 0.0826 0.0078 -0.0359 0.0059 43 LEU A O 332 C CB . LEU A 43 ? 0.1093 0.0831 0.0879 0.0111 -0.0440 -0.0022 43 LEU A CB 333 C CG . LEU A 43 ? 0.0919 0.0905 0.0844 -0.0033 -0.0232 0.0001 43 LEU A CG 334 C CD1 . LEU A 43 ? 0.0964 0.1135 0.1110 -0.0021 -0.0346 -0.0044 43 LEU A CD1 335 C CD2 . LEU A 43 ? 0.1263 0.1030 0.1025 0.0000 -0.0386 -0.0128 43 LEU A CD2 336 N N . THR A 44 ? 0.1029 0.1103 0.0797 0.0271 -0.0334 -0.0004 44 THR A N 337 C CA . THR A 44 ? 0.1021 0.1320 0.0743 0.0183 -0.0204 -0.0141 44 THR A CA 338 C C . THR A 44 ? 0.0788 0.1051 0.0917 -0.0130 -0.0131 -0.0064 44 THR A C 339 O O . THR A 44 ? 0.0980 0.1215 0.0770 0.0018 -0.0161 -0.0014 44 THR A O 340 C CB . THR A 44 ? 0.0891 0.2076 0.1524 0.0349 -0.0399 -0.0431 44 THR A CB 341 O OG1 . THR A 44 ? 0.1268 0.1720 0.1249 -0.0047 -0.0281 0.0140 44 THR A OG1 342 C CG2 . THR A 44 ? 0.1421 0.2413 0.1962 0.1133 -0.0641 -0.1115 44 THR A CG2 343 N N . PHE A 45 ? 0.0789 0.1001 0.0731 -0.0120 -0.0100 -0.0039 45 PHE A N 344 C CA . PHE A 45 ? 0.0927 0.0948 0.0700 -0.0125 -0.0046 0.0042 45 PHE A CA 345 C C . PHE A 45 ? 0.0885 0.0747 0.0692 -0.0110 -0.0192 0.0036 45 PHE A C 346 O O . PHE A 45 ? 0.1087 0.0839 0.0789 -0.0178 -0.0242 0.0093 45 PHE A O 347 C CB . PHE A 45 ? 0.0949 0.0986 0.0797 -0.0207 -0.0272 -0.0025 45 PHE A CB 348 C CG . PHE A 45 ? 0.1002 0.0978 0.0975 -0.0086 -0.0401 -0.0142 45 PHE A CG 349 C CD1 . PHE A 45 ? 0.1182 0.1236 0.1533 -0.0300 0.0150 -0.0399 45 PHE A CD1 350 C CD2 . PHE A 45 ? 0.1609 0.1052 0.1145 -0.0129 -0.0551 -0.0019 45 PHE A CD2 351 C CE1 . PHE A 45 ? 0.1309 0.1531 0.2447 -0.0261 0.0203 -0.0953 45 PHE A CE1 352 C CE2 . PHE A 45 ? 0.2017 0.0979 0.1884 -0.0018 -0.1198 -0.0122 45 PHE A CE2 353 C CZ . PHE A 45 ? 0.1342 0.1363 0.2563 0.0275 -0.0887 -0.0863 45 PHE A CZ 354 N N . HIS A 46 ? 0.0721 0.0798 0.0693 -0.0068 -0.0096 0.0018 46 HIS A N 355 C CA . HIS A 46 ? 0.0803 0.0756 0.0676 0.0003 -0.0177 0.0030 46 HIS A CA 356 C C . HIS A 46 ? 0.0793 0.0728 0.0720 -0.0020 -0.0143 0.0034 46 HIS A C 357 O O . HIS A 46 ? 0.0932 0.0919 0.0848 0.0152 -0.0313 0.0010 46 HIS A O 358 C CB . HIS A 46 ? 0.0738 0.1047 0.0753 -0.0094 -0.0102 -0.0023 46 HIS A CB 359 C CG . HIS A 46 ? 0.0784 0.1047 0.0792 -0.0027 -0.0087 0.0022 46 HIS A CG 360 N ND1 . HIS A 46 ? 0.0787 0.1041 0.0807 0.0013 -0.0131 0.0060 46 HIS A ND1 361 C CD2 . HIS A 46 ? 0.0881 0.1699 0.0842 -0.0007 -0.0217 -0.0250 46 HIS A CD2 362 C CE1 . HIS A 46 ? 0.1013 0.1204 0.0764 0.0037 -0.0123 0.0017 46 HIS A CE1 363 N NE2 . HIS A 46 ? 0.0917 0.1619 0.0862 0.0059 -0.0173 -0.0143 46 HIS A NE2 364 N N . ASP A 47 ? 0.0774 0.0758 0.0651 -0.0017 -0.0171 0.0051 47 ASP A N 365 C CA . ASP A 47 ? 0.0666 0.0695 0.0697 -0.0028 -0.0176 0.0048 47 ASP A CA 366 C C . ASP A 47 ? 0.0738 0.0795 0.0691 -0.0026 -0.0171 0.0041 47 ASP A C 367 O O . ASP A 47 ? 0.0787 0.0828 0.0821 -0.0054 -0.0219 0.0182 47 ASP A O 368 C CB . ASP A 47 ? 0.0788 0.0775 0.0722 -0.0023 -0.0195 0.0070 47 ASP A CB 369 C CG . ASP A 47 ? 0.0895 0.0745 0.0800 0.0024 -0.0138 0.0087 47 ASP A CG 370 O OD1 . ASP A 47 ? 0.0847 0.1170 0.0952 0.0065 -0.0067 -0.0175 47 ASP A OD1 371 O OD2 . ASP A 47 ? 0.1139 0.0913 0.0813 0.0168 -0.0318 0.0006 47 ASP A OD2 372 N N . ALA A 48 ? 0.0747 0.0781 0.0700 -0.0091 -0.0184 0.0121 48 ALA A N 373 C CA . ALA A 48 ? 0.0781 0.0843 0.0645 -0.0087 -0.0102 0.0066 48 ALA A CA 374 C C . ALA A 48 ? 0.0749 0.0810 0.0724 -0.0088 -0.0157 0.0096 48 ALA A C 375 O O . ALA A 48 ? 0.0944 0.0870 0.0808 -0.0071 -0.0169 0.0149 48 ALA A O 376 C CB . ALA A 48 ? 0.0763 0.0909 0.0866 -0.0089 -0.0083 0.0061 48 ALA A CB 377 N N . ILE A 49 ? 0.0810 0.0765 0.0750 -0.0014 -0.0173 0.0093 49 ILE A N 378 C CA . ILE A 49 ? 0.0803 0.0781 0.0787 -0.0072 -0.0192 0.0028 49 ILE A CA 379 C C . ILE A 49 ? 0.0861 0.0793 0.0744 -0.0042 -0.0181 0.0109 49 ILE A C 380 O O . ILE A 49 ? 0.0974 0.0762 0.0889 -0.0026 -0.0265 0.0073 49 ILE A O 381 C CB . ILE A 49 ? 0.0896 0.0789 0.0784 -0.0017 -0.0200 -0.0015 49 ILE A CB 382 C CG1 . ILE A 49 ? 0.1132 0.0827 0.1065 0.0012 -0.0313 -0.0024 49 ILE A CG1 383 C CG2 . ILE A 49 ? 0.0967 0.0981 0.0823 0.0071 -0.0163 -0.0010 49 ILE A CG2 384 C CD1 . ILE A 49 ? 0.1201 0.0839 0.1260 -0.0201 -0.0389 0.0088 49 ILE A CD1 385 N N . ALA A 50 ? 0.0826 0.0738 0.0820 -0.0030 -0.0232 0.0111 50 ALA A N 386 C CA . ALA A 50 ? 0.0803 0.0780 0.0816 -0.0060 -0.0212 0.0086 50 ALA A CA 387 C C . ALA A 50 ? 0.0807 0.0769 0.0863 -0.0005 -0.0183 0.0113 50 ALA A C 388 O O . ALA A 50 ? 0.1028 0.0788 0.0870 -0.0092 -0.0313 0.0072 50 ALA A O 389 C CB . ALA A 50 ? 0.0905 0.0991 0.0932 -0.0186 -0.0222 0.0208 50 ALA A CB 390 N N . ILE A 51 ? 0.0936 0.0743 0.0781 0.0017 -0.0212 0.0066 51 ILE A N 391 C CA . ILE A 51 ? 0.1014 0.0763 0.0853 0.0001 -0.0244 0.0103 51 ILE A CA 392 C C . ILE A 51 ? 0.0901 0.0749 0.1010 0.0047 -0.0224 0.0122 51 ILE A C 393 O O . ILE A 51 ? 0.1019 0.0764 0.0906 -0.0039 -0.0277 0.0061 51 ILE A O 394 C CB . ILE A 51 ? 0.0900 0.0782 0.0914 -0.0019 -0.0162 0.0096 51 ILE A CB 395 C CG1 . ILE A 51 ? 0.1094 0.1079 0.0913 -0.0009 -0.0102 0.0134 51 ILE A CG1 396 C CG2 . ILE A 51 ? 0.0970 0.0945 0.0980 -0.0058 -0.0116 0.0144 51 ILE A CG2 397 C CD1 . ILE A 51 ? 0.1437 0.1221 0.1185 0.0068 0.0178 0.0123 51 ILE A CD1 398 N N . SER A 52 ? 0.1112 0.0757 0.0979 0.0032 -0.0335 0.0153 52 SER A N 399 C CA . SER A 52 ? 0.1085 0.0766 0.0953 0.0030 -0.0345 0.0076 52 SER A CA 400 C C . SER A 52 ? 0.1175 0.0777 0.1116 0.0042 -0.0371 0.0186 52 SER A C 401 O O . SER A 52 ? 0.1432 0.1004 0.1085 -0.0125 -0.0539 0.0259 52 SER A O 402 C CB . SER A 52 ? 0.1207 0.0885 0.1138 0.0133 -0.0277 0.0131 52 SER A CB 403 O OG . SER A 52 ? 0.1335 0.0875 0.1312 0.0191 -0.0353 0.0105 52 SER A OG 404 N N . ARG A 53 ? 0.1287 0.0946 0.0983 -0.0120 -0.0409 0.0251 53 ARG A N 405 C CA . ARG A 53 ? 0.1588 0.1086 0.1074 -0.0183 -0.0333 0.0333 53 ARG A CA 406 C C . ARG A 53 ? 0.1775 0.0991 0.1291 -0.0118 -0.0638 0.0371 53 ARG A C 407 O O . ARG A 53 ? 0.2247 0.1496 0.1321 -0.0051 -0.0723 0.0548 53 ARG A O 408 C CB . ARG A 53 ? 0.1776 0.1376 0.1382 -0.0457 -0.0486 0.0483 53 ARG A CB 409 C CG . ARG A 53 ? 0.1746 0.2008 0.1361 -0.0389 -0.0386 0.0567 53 ARG A CG 410 C CD . ARG A 53 ? 0.1932 0.2831 0.2974 -0.1049 -0.1067 0.1326 53 ARG A CD 411 N NE . ARG A 53 ? 0.2127 0.5542 0.2465 -0.0955 -0.0698 0.1176 53 ARG A NE 412 C CZ . ARG A 53 ? 0.2352 0.8854 0.2592 -0.2480 -0.1342 0.2519 53 ARG A CZ 413 N NH1 . ARG A 53 ? 0.5188 0.5697 0.4490 -0.3738 -0.3523 0.3780 53 ARG A NH1 414 N NH2 . ARG A 53 ? 0.2276 1.5963 0.2776 -0.1669 -0.0547 0.3873 53 ARG A NH2 415 N N . SER A 54 ? 0.1588 0.1000 0.1383 -0.0044 -0.0649 0.0339 54 SER A N 416 C CA . SER A 54 ? 0.1871 0.0850 0.1764 0.0038 -0.0726 0.0373 54 SER A CA 417 C C . SER A 54 ? 0.1703 0.1023 0.1613 0.0123 -0.0673 0.0359 54 SER A C 418 O O . SER A 54 ? 0.2044 0.1257 0.1955 0.0151 -0.0973 0.0448 54 SER A O 419 C CB . SER A 54 ? 0.1945 0.1044 0.2138 0.0225 -0.0852 0.0141 54 SER A CB 420 O OG . SER A 54 ? 0.2208 0.1547 0.1731 0.0335 -0.0748 -0.0008 54 SER A OG 421 N N . GLN A 55 ? 0.1568 0.0946 0.1717 0.0125 -0.0777 0.0252 55 GLN A N 422 C CA . GLN A 55 ? 0.1395 0.1078 0.1741 0.0125 -0.0618 0.0254 55 GLN A CA 423 C C . GLN A 55 ? 0.1422 0.1296 0.1638 -0.0091 -0.0615 0.0259 55 GLN A C 424 O O . GLN A 55 ? 0.1787 0.2029 0.1936 -0.0057 -0.0910 0.0121 55 GLN A O 425 C CB . GLN A 55 ? 0.1446 0.1172 0.1783 0.0170 -0.0456 0.0235 55 GLN A CB 426 C CG . GLN A 55 ? 0.1598 0.1398 0.1880 0.0295 -0.0277 0.0219 55 GLN A CG 427 C CD . GLN A 55 ? 0.2287 0.2124 0.2328 0.0819 0.0294 0.0760 55 GLN A CD 428 O OE1 . GLN A 55 ? 0.3857 0.1786 0.3738 -0.0585 0.0929 0.0386 55 GLN A OE1 429 N NE2 . GLN A 55 ? 0.3658 0.3569 0.2011 0.2016 0.0284 0.1102 55 GLN A NE2 430 N N . GLY A 56 ? 0.1625 0.1147 0.1443 -0.0192 -0.0562 0.0223 56 GLY A N 431 C CA . GLY A 56 ? 0.1811 0.1224 0.1315 -0.0164 -0.0474 0.0348 56 GLY A CA 432 C C . GLY A 56 ? 0.1169 0.1190 0.1222 -0.0211 -0.0400 0.0301 56 GLY A C 433 O O . GLY A 56 ? 0.1222 0.1178 0.1098 -0.0100 -0.0412 0.0307 56 GLY A O 434 N N . PRO A 57 ? 0.1734 0.1351 0.1072 -0.0312 -0.0310 0.0312 57 PRO A N 435 C CA . PRO A 57 ? 0.1988 0.1415 0.1051 -0.0245 -0.0160 0.0176 57 PRO A CA 436 C C . PRO A 57 ? 0.1812 0.1389 0.1071 -0.0372 -0.0571 0.0363 57 PRO A C 437 O O . PRO A 57 ? 0.1871 0.1296 0.1196 -0.0180 -0.0519 0.0301 57 PRO A O 438 C CB . PRO A 57 ? 0.3508 0.1783 0.1287 -0.0174 0.0359 0.0154 57 PRO A CB 439 C CG . PRO A 57 ? 0.4416 0.2089 0.1504 0.0147 0.0743 0.0535 57 PRO A CG 440 C CD . PRO A 57 ? 0.2432 0.1683 0.1155 -0.0521 -0.0290 0.0365 57 PRO A CD 441 N N . LYS A 58 ? 0.1791 0.1297 0.1355 -0.0419 -0.0747 0.0361 58 LYS A N 442 C CA . LYS A 58 ? 0.1654 0.1638 0.1617 -0.0548 -0.0845 0.0666 58 LYS A CA 443 C C . LYS A 58 ? 0.1432 0.1361 0.1583 -0.0385 -0.0771 0.0661 58 LYS A C 444 O O . LYS A 58 ? 0.1625 0.1830 0.1719 -0.0645 -0.0686 0.0763 58 LYS A O 445 C CB . LYS A 58 ? 0.1925 0.2796 0.3027 -0.0874 -0.1632 0.1811 58 LYS A CB 446 C CG . LYS A 58 ? 0.4430 0.3602 0.3193 -0.1423 -0.2548 0.1778 58 LYS A CG 447 C CD . LYS A 58 ? 0.5448 0.2756 0.3852 -0.0416 -0.3192 0.0917 58 LYS A CD 448 C CE . LYS A 58 ? 0.7604 0.3638 0.3544 -0.1543 -0.3792 0.1694 58 LYS A CE 449 N NZ . LYS A 58 ? 0.5062 0.7961 0.3911 -0.0504 -0.2772 0.1356 58 LYS A NZ 450 N N . ALA A 59 ? 0.1050 0.1149 0.1319 0.0007 -0.0338 0.0417 59 ALA A N 451 C CA . ALA A 59 ? 0.1007 0.1120 0.1314 0.0115 -0.0204 0.0390 59 ALA A CA 452 C C . ALA A 59 ? 0.0912 0.0994 0.1069 0.0012 -0.0261 0.0149 59 ALA A C 453 O O . ALA A 59 ? 0.1032 0.1166 0.1030 0.0096 -0.0144 0.0227 59 ALA A O 454 C CB . ALA A 59 ? 0.1581 0.1049 0.1318 0.0093 -0.0079 0.0185 59 ALA A CB 455 N N . GLY A 60 ? 0.0948 0.1040 0.0974 0.0023 -0.0226 0.0200 60 GLY A N 456 C CA . GLY A 60 ? 0.0953 0.1057 0.0963 0.0048 -0.0178 0.0191 60 GLY A CA 457 C C . GLY A 60 ? 0.0927 0.0874 0.0855 -0.0036 -0.0236 0.0135 60 GLY A C 458 O O . GLY A 60 ? 0.1064 0.0981 0.1082 -0.0061 -0.0072 0.0166 60 GLY A O 459 N N . GLY A 61 ? 0.0883 0.0902 0.0852 -0.0027 -0.0194 0.0184 61 GLY A N 460 C CA . GLY A 61 ? 0.0959 0.1002 0.0768 -0.0018 -0.0201 0.0141 61 GLY A CA 461 C C . GLY A 61 ? 0.0830 0.0925 0.0836 -0.0148 -0.0160 0.0095 61 GLY A C 462 O O . GLY A 61 ? 0.0863 0.1366 0.0822 -0.0144 -0.0092 -0.0011 61 GLY A O 463 N N . GLY A 62 ? 0.0788 0.0898 0.0772 -0.0022 -0.0180 0.0093 62 GLY A N 464 C CA . GLY A 62 ? 0.0874 0.0861 0.0794 -0.0099 -0.0139 0.0057 62 GLY A CA 465 C C . GLY A 62 ? 0.0767 0.0810 0.0699 -0.0124 -0.0131 0.0084 62 GLY A C 466 O O . GLY A 62 ? 0.0729 0.0843 0.0802 0.0004 -0.0121 0.0084 62 GLY A O 467 N N . ALA A 63 ? 0.0782 0.0781 0.0756 -0.0121 -0.0117 0.0097 63 ALA A N 468 C CA . ALA A 63 ? 0.0799 0.0888 0.0758 -0.0039 -0.0172 0.0076 63 ALA A CA 469 C C . ALA A 63 ? 0.0793 0.0803 0.0748 -0.0060 -0.0137 0.0144 63 ALA A C 470 O O . ALA A 63 ? 0.0866 0.0980 0.0833 -0.0136 0.0012 0.0041 63 ALA A O 471 C CB . ALA A 63 ? 0.0737 0.0938 0.0892 -0.0073 -0.0169 0.0061 63 ALA A CB 472 N N . ASP A 64 ? 0.0773 0.0877 0.0724 -0.0085 -0.0079 0.0043 64 ASP A N 473 C CA . ASP A 64 ? 0.0790 0.0908 0.0735 -0.0016 -0.0082 0.0056 64 ASP A CA 474 C C . ASP A 64 ? 0.0741 0.0821 0.0847 -0.0056 -0.0123 -0.0010 64 ASP A C 475 O O . ASP A 64 ? 0.0895 0.0930 0.0896 -0.0067 -0.0147 -0.0014 64 ASP A O 476 C CB . ASP A 64 ? 0.0857 0.0974 0.0764 -0.0044 -0.0118 0.0112 64 ASP A CB 477 C CG . ASP A 64 ? 0.0895 0.0784 0.0794 -0.0065 -0.0205 0.0005 64 ASP A CG 478 O OD1 . ASP A 64 ? 0.0780 0.0843 0.0722 -0.0022 -0.0147 0.0066 64 ASP A OD1 479 O OD2 . ASP A 64 ? 0.0890 0.1057 0.0813 0.0064 -0.0178 0.0101 64 ASP A OD2 480 N N . GLY A 65 ? 0.0729 0.0819 0.0820 -0.0042 -0.0089 0.0034 65 GLY A N 481 C CA . GLY A 65 ? 0.0761 0.0868 0.0887 -0.0001 -0.0130 0.0057 65 GLY A CA 482 C C . GLY A 65 ? 0.0829 0.0733 0.0800 -0.0036 -0.0181 -0.0033 65 GLY A C 483 O O . GLY A 65 ? 0.0850 0.0803 0.0900 -0.0016 -0.0149 0.0035 65 GLY A O 484 N N . SER A 66 ? 0.0713 0.0745 0.0925 -0.0070 -0.0071 0.0047 66 SER A N 485 C CA . SER A 66 ? 0.0724 0.0778 0.0824 -0.0084 -0.0212 0.0098 66 SER A CA 486 C C . SER A 66 ? 0.0673 0.0812 0.0801 0.0020 -0.0197 0.0054 66 SER A C 487 O O . SER A 66 ? 0.0764 0.0920 0.0933 -0.0069 -0.0136 0.0107 66 SER A O 488 C CB . SER A 66 ? 0.0702 0.0858 0.0772 -0.0054 -0.0197 0.0094 66 SER A CB 489 O OG . SER A 66 ? 0.0704 0.0789 0.0867 -0.0110 -0.0211 0.0043 66 SER A OG 490 N N . MET A 67 ? 0.0856 0.0870 0.0803 -0.0021 -0.0162 0.0155 67 MET A N 491 C CA . MET A 67 ? 0.1240 0.0935 0.0709 0.0118 -0.0123 0.0115 67 MET A CA 492 C C . MET A 67 ? 0.0960 0.0942 0.0791 0.0084 -0.0146 0.0111 67 MET A C 493 O O . MET A 67 ? 0.1113 0.0970 0.1097 0.0046 0.0041 0.0200 67 MET A O 494 C CB . MET A 67 ? 0.1631 0.1058 0.0893 -0.0107 -0.0411 0.0058 67 MET A CB 495 C CG . MET A 67 ? 0.1701 0.1027 0.1042 -0.0068 -0.0250 -0.0071 67 MET A CG 496 S SD . MET A 67 ? 0.1576 0.1149 0.2180 0.0033 0.0298 -0.0026 67 MET A SD 497 C CE . MET A 67 ? 0.1254 0.1236 0.1260 -0.0041 -0.0292 -0.0151 67 MET A CE 498 N N . LEU A 68 ? 0.0838 0.0845 0.0855 -0.0005 -0.0172 0.0069 68 LEU A N 499 C CA . LEU A 68 ? 0.0814 0.0800 0.0893 -0.0004 -0.0218 0.0103 68 LEU A CA 500 C C . LEU A 68 ? 0.0838 0.0818 0.0969 -0.0024 -0.0154 0.0061 68 LEU A C 501 O O . LEU A 68 ? 0.1041 0.0960 0.1122 -0.0142 -0.0275 0.0126 68 LEU A O 502 C CB . LEU A 68 ? 0.0828 0.0870 0.0868 0.0054 -0.0150 0.0093 68 LEU A CB 503 C CG . LEU A 68 ? 0.0929 0.1764 0.1024 0.0339 -0.0192 -0.0104 68 LEU A CG 504 C CD1 . LEU A 68 ? 0.0994 0.1732 0.0971 0.0412 -0.0209 0.0085 68 LEU A CD1 505 C CD2 . LEU A 68 ? 0.1175 0.2345 0.1064 0.0353 -0.0352 -0.0455 68 LEU A CD2 506 N N . LEU A 69 ? 0.0768 0.0839 0.0926 0.0001 -0.0221 0.0015 69 LEU A N 507 C CA . LEU A 69 ? 0.0786 0.0890 0.0934 0.0030 -0.0179 0.0013 69 LEU A CA 508 C C . LEU A 69 ? 0.0798 0.0788 0.1046 -0.0005 -0.0276 -0.0012 69 LEU A C 509 O O . LEU A 69 ? 0.0836 0.1004 0.1073 -0.0029 -0.0280 -0.0121 69 LEU A O 510 C CB . LEU A 69 ? 0.0929 0.0948 0.0863 -0.0004 -0.0265 -0.0043 69 LEU A CB 511 C CG . LEU A 69 ? 0.0784 0.1251 0.1015 -0.0075 -0.0170 -0.0051 69 LEU A CG 512 C CD1 . LEU A 69 ? 0.1084 0.1593 0.1081 -0.0106 -0.0116 0.0091 69 LEU A CD1 513 C CD2 . LEU A 69 ? 0.1218 0.1294 0.1280 0.0049 -0.0152 -0.0242 69 LEU A CD2 514 N N . PHE A 70 ? 0.0669 0.0876 0.0965 -0.0065 -0.0209 0.0021 70 PHE A N 515 C CA . PHE A 70 ? 0.0759 0.0891 0.0914 -0.0004 -0.0200 0.0038 70 PHE A CA 516 C C . PHE A 70 ? 0.0670 0.0895 0.0970 -0.0022 -0.0206 0.0083 70 PHE A C 517 O O . PHE A 70 ? 0.0870 0.0950 0.0969 -0.0045 -0.0199 0.0000 70 PHE A O 518 C CB . PHE A 70 ? 0.0929 0.0916 0.0955 0.0076 -0.0235 0.0056 70 PHE A CB 519 C CG . PHE A 70 ? 0.0850 0.0833 0.0993 0.0055 -0.0261 0.0106 70 PHE A CG 520 C CD1 . PHE A 70 ? 0.0782 0.0997 0.1111 0.0025 -0.0288 0.0034 70 PHE A CD1 521 C CD2 . PHE A 70 ? 0.0849 0.1130 0.1037 -0.0108 -0.0313 0.0124 70 PHE A CD2 522 C CE1 . PHE A 70 ? 0.0931 0.1208 0.1133 -0.0130 -0.0361 0.0121 70 PHE A CE1 523 C CE2 . PHE A 70 ? 0.0947 0.1249 0.1059 -0.0133 -0.0199 0.0192 70 PHE A CE2 524 C CZ . PHE A 70 ? 0.1220 0.1269 0.1009 -0.0155 -0.0328 0.0188 70 PHE A CZ 525 N N . PRO A 71 ? 0.0819 0.0906 0.0972 0.0030 -0.0204 0.0034 71 PRO A N 526 C CA . PRO A 71 ? 0.0859 0.1021 0.0924 -0.0023 -0.0234 0.0131 71 PRO A CA 527 C C . PRO A 71 ? 0.0835 0.0959 0.1029 -0.0029 -0.0182 0.0113 71 PRO A C 528 O O . PRO A 71 ? 0.0985 0.1145 0.0924 -0.0040 -0.0244 0.0082 71 PRO A O 529 C CB . PRO A 71 ? 0.1272 0.1172 0.1108 0.0297 -0.0266 0.0046 71 PRO A CB 530 C CG . PRO A 71 ? 0.1177 0.0939 0.1144 -0.0013 -0.0143 0.0143 71 PRO A CG 531 C CD . PRO A 71 ? 0.0936 0.0909 0.1053 0.0034 -0.0138 0.0037 71 PRO A CD 532 N N . THR A 72 ? 0.0752 0.1064 0.0933 0.0000 -0.0168 0.0067 72 THR A N 533 C CA . THR A 72 ? 0.0883 0.1091 0.0982 -0.0060 -0.0117 0.0212 72 THR A CA 534 C C . THR A 72 ? 0.0809 0.1072 0.0959 -0.0082 -0.0176 0.0020 72 THR A C 535 O O . THR A 72 ? 0.0828 0.1259 0.1071 -0.0052 0.0022 0.0025 72 THR A O 536 C CB . THR A 72 ? 0.0801 0.1110 0.1327 -0.0089 -0.0169 0.0145 72 THR A CB 537 O OG1 . THR A 72 ? 0.0876 0.1191 0.1252 -0.0099 -0.0282 0.0036 72 THR A OG1 538 C CG2 . THR A 72 ? 0.1015 0.1076 0.1915 -0.0204 -0.0275 0.0208 72 THR A CG2 539 N N . VAL A 73 ? 0.0736 0.1045 0.0924 -0.0056 -0.0179 -0.0003 73 VAL A N 540 C CA . VAL A 73 ? 0.0705 0.1038 0.0928 -0.0050 -0.0167 0.0002 73 VAL A CA 541 C C . VAL A 73 ? 0.0660 0.0898 0.0945 0.0041 -0.0145 0.0035 73 VAL A C 542 O O . VAL A 73 ? 0.0730 0.1151 0.0908 -0.0033 -0.0082 -0.0020 73 VAL A O 543 C CB . VAL A 73 ? 0.0721 0.1173 0.0966 -0.0013 -0.0248 0.0013 73 VAL A CB 544 C CG1 . VAL A 73 ? 0.1016 0.1130 0.1178 0.0102 -0.0208 0.0172 73 VAL A CG1 545 C CG2 . VAL A 73 ? 0.0900 0.1533 0.1037 -0.0143 -0.0371 -0.0034 73 VAL A CG2 546 N N . GLU A 74 ? 0.0752 0.0991 0.0837 -0.0017 -0.0151 -0.0045 74 GLU A N 547 C CA . GLU A 74 ? 0.0742 0.0934 0.0841 -0.0104 -0.0167 -0.0030 74 GLU A CA 548 C C . GLU A 74 ? 0.0658 0.0873 0.0932 -0.0103 -0.0161 -0.0007 74 GLU A C 549 O O . GLU A 74 ? 0.0806 0.0969 0.0877 -0.0120 -0.0125 -0.0006 74 GLU A O 550 C CB . GLU A 74 ? 0.0754 0.0950 0.0918 -0.0069 -0.0127 -0.0005 74 GLU A CB 551 C CG . GLU A 74 ? 0.0803 0.0953 0.0936 -0.0004 -0.0130 0.0030 74 GLU A CG 552 C CD . GLU A 74 ? 0.0856 0.0970 0.0876 -0.0026 -0.0162 0.0034 74 GLU A CD 553 O OE1 . GLU A 74 ? 0.0892 0.1113 0.0951 -0.0093 -0.0069 -0.0086 74 GLU A OE1 554 O OE2 . GLU A 74 ? 0.0815 0.1111 0.0933 -0.0045 -0.0141 -0.0023 74 GLU A OE2 555 N N . PRO A 75 ? 0.0827 0.0989 0.0885 -0.0031 -0.0178 0.0003 75 PRO A N 556 C CA . PRO A 75 ? 0.0858 0.0946 0.0974 -0.0076 -0.0294 0.0043 75 PRO A CA 557 C C . PRO A 75 ? 0.1049 0.1002 0.1028 -0.0029 -0.0214 0.0062 75 PRO A C 558 O O . PRO A 75 ? 0.1131 0.1740 0.0926 0.0116 -0.0231 0.0146 75 PRO A O 559 C CB . PRO A 75 ? 0.1030 0.0969 0.1217 0.0021 -0.0251 0.0110 75 PRO A CB 560 C CG . PRO A 75 ? 0.1024 0.0889 0.1189 -0.0027 -0.0276 -0.0037 75 PRO A CG 561 C CD . PRO A 75 ? 0.0866 0.0926 0.1046 0.0017 -0.0239 -0.0100 75 PRO A CD 562 N N . ASN A 76 ? 0.0934 0.1050 0.0972 -0.0076 -0.0150 0.0094 76 ASN A N 563 C CA . ASN A 76 ? 0.0985 0.1249 0.1086 -0.0203 -0.0024 0.0212 76 ASN A CA 564 C C . ASN A 76 ? 0.0846 0.1351 0.1054 -0.0059 -0.0056 0.0157 76 ASN A C 565 O O . ASN A 76 ? 0.1170 0.1574 0.1512 0.0085 0.0315 0.0306 76 ASN A O 566 C CB A ASN A 76 ? 0.0998 0.1315 0.1105 -0.0176 -0.0132 0.0422 76 ASN A CB 567 C CB B ASN A 76 ? 0.1073 0.1607 0.1357 -0.0149 -0.0152 -0.0107 76 ASN A CB 568 C CG A ASN A 76 ? 0.0874 0.1273 0.1142 -0.0261 -0.0129 0.0139 76 ASN A CG 569 C CG B ASN A 76 ? 0.2027 0.3332 0.2063 -0.1548 -0.0230 0.0999 76 ASN A CG 570 O OD1 A ASN A 76 ? 0.1694 0.1674 0.1230 -0.0024 -0.0375 -0.0047 76 ASN A OD1 571 O OD1 B ASN A 76 ? 0.4020 0.4847 0.2361 -0.2709 -0.0837 0.1878 76 ASN A OD1 572 N ND2 A ASN A 76 ? 0.1504 0.0818 0.1118 -0.0248 -0.0200 0.0072 76 ASN A ND2 573 N ND2 B ASN A 76 ? 0.1984 0.9250 0.3106 -0.2864 -0.0157 0.1349 76 ASN A ND2 574 N N . PHE A 77 ? 0.0781 0.1125 0.1013 -0.0052 -0.0035 -0.0020 77 PHE A N 575 C CA . PHE A 77 ? 0.0832 0.1209 0.0910 0.0009 -0.0054 -0.0060 77 PHE A CA 576 C C . PHE A 77 ? 0.0835 0.1171 0.0918 0.0008 0.0007 0.0028 77 PHE A C 577 O O . PHE A 77 ? 0.0988 0.1121 0.0977 0.0076 -0.0168 0.0089 77 PHE A O 578 C CB . PHE A 77 ? 0.1004 0.0983 0.0890 0.0048 -0.0195 -0.0027 77 PHE A CB 579 C CG . PHE A 77 ? 0.1117 0.0936 0.0939 0.0104 -0.0210 0.0019 77 PHE A CG 580 C CD1 . PHE A 77 ? 0.1188 0.1258 0.1123 -0.0005 -0.0377 0.0059 77 PHE A CD1 581 C CD2 . PHE A 77 ? 0.1254 0.0963 0.1053 0.0196 -0.0024 0.0114 77 PHE A CD2 582 C CE1 . PHE A 77 ? 0.1710 0.1296 0.1155 -0.0129 -0.0533 -0.0048 77 PHE A CE1 583 C CE2 . PHE A 77 ? 0.1698 0.1009 0.0990 0.0369 -0.0062 0.0107 77 PHE A CE2 584 C CZ . PHE A 77 ? 0.2102 0.1105 0.1002 0.0241 -0.0372 0.0040 77 PHE A CZ 585 N N . SER A 78 ? 0.1057 0.1277 0.0955 0.0140 -0.0040 -0.0107 78 SER A N 586 C CA . SER A 78 ? 0.1075 0.1627 0.0897 0.0148 -0.0049 -0.0007 78 SER A CA 587 C C . SER A 78 ? 0.1255 0.1064 0.0888 0.0104 -0.0192 -0.0051 78 SER A C 588 O O . SER A 78 ? 0.1331 0.1435 0.0909 0.0192 -0.0155 0.0037 78 SER A O 589 C CB . SER A 78 ? 0.1665 0.2324 0.1150 0.0503 -0.0077 -0.0599 78 SER A CB 590 O OG . SER A 78 ? 0.2426 0.1934 0.3526 0.0397 0.0388 -0.0377 78 SER A OG 591 N N . ALA A 79 ? 0.1120 0.0934 0.0958 0.0143 -0.0196 -0.0063 79 ALA A N 592 C CA . ALA A 79 ? 0.1238 0.0899 0.1015 0.0105 -0.0274 -0.0108 79 ALA A CA 593 C C . ALA A 79 ? 0.1048 0.1014 0.0930 0.0073 -0.0290 -0.0093 79 ALA A C 594 O O . ALA A 79 ? 0.1082 0.1133 0.1234 0.0089 -0.0367 -0.0193 79 ALA A O 595 C CB . ALA A 79 ? 0.1307 0.1026 0.1080 0.0051 -0.0170 -0.0075 79 ALA A CB 596 N N . ASN A 80 ? 0.1020 0.0922 0.0930 0.0091 -0.0226 0.0020 80 ASN A N 597 C CA . ASN A 80 ? 0.0858 0.0919 0.0922 0.0048 -0.0175 0.0047 80 ASN A CA 598 C C . ASN A 80 ? 0.0902 0.0882 0.0918 0.0059 -0.0180 0.0037 80 ASN A C 599 O O . ASN A 80 ? 0.1165 0.1002 0.0928 0.0121 -0.0133 0.0072 80 ASN A O 600 C CB . ASN A 80 ? 0.0937 0.0887 0.0860 0.0052 -0.0161 0.0014 80 ASN A CB 601 C CG . ASN A 80 ? 0.0778 0.0941 0.0988 0.0030 -0.0210 0.0048 80 ASN A CG 602 O OD1 . ASN A 80 ? 0.0815 0.1251 0.1229 -0.0121 -0.0308 0.0104 80 ASN A OD1 603 N ND2 . ASN A 80 ? 0.0800 0.0929 0.0964 0.0025 -0.0200 0.0054 80 ASN A ND2 604 N N . ASN A 81 ? 0.1220 0.1025 0.0906 0.0146 -0.0073 0.0062 81 ASN A N 605 C CA . ASN A 81 ? 0.1307 0.1168 0.0982 0.0206 0.0054 0.0148 81 ASN A CA 606 C C . ASN A 81 ? 0.1239 0.1124 0.0838 0.0092 -0.0075 0.0031 81 ASN A C 607 O O . ASN A 81 ? 0.1527 0.1187 0.1290 0.0018 -0.0489 -0.0041 81 ASN A O 608 C CB . ASN A 81 ? 0.1665 0.1469 0.1048 0.0395 0.0180 0.0198 81 ASN A CB 609 C CG . ASN A 81 ? 0.1348 0.2002 0.1208 0.0087 0.0127 0.0226 81 ASN A CG 610 O OD1 . ASN A 81 ? 0.1957 0.1939 0.1655 -0.0250 0.0356 0.0376 81 ASN A OD1 611 N ND2 . ASN A 81 ? 0.1390 0.2659 0.1206 0.0096 0.0199 0.0171 81 ASN A ND2 612 N N . GLY A 82 ? 0.1086 0.1131 0.1004 0.0009 -0.0076 0.0071 82 GLY A N 613 C CA . GLY A 82 ? 0.1375 0.1142 0.1037 0.0163 -0.0072 0.0161 82 GLY A CA 614 C C . GLY A 82 ? 0.0972 0.0994 0.1131 0.0032 -0.0183 0.0147 82 GLY A C 615 O O . GLY A 82 ? 0.1189 0.1171 0.1225 0.0212 -0.0163 0.0236 82 GLY A O 616 N N . ILE A 83 ? 0.0883 0.0931 0.0982 0.0099 -0.0138 0.0064 83 ILE A N 617 C CA . ILE A 83 ? 0.0943 0.0847 0.1116 0.0103 -0.0082 0.0065 83 ILE A CA 618 C C . ILE A 83 ? 0.0924 0.1007 0.1013 0.0114 -0.0063 0.0078 83 ILE A C 619 O O . ILE A 83 ? 0.0973 0.1014 0.1134 0.0132 -0.0007 0.0016 83 ILE A O 620 C CB A ILE A 83 ? 0.1102 0.0978 0.0905 0.0085 -0.0052 0.0037 83 ILE A CB 621 C CB B ILE A 83 ? 0.0990 0.1031 0.1235 0.0071 0.0143 0.0264 83 ILE A CB 622 C CG1 A ILE A 83 ? 0.1052 0.0911 0.0872 0.0111 -0.0122 0.0122 83 ILE A CG1 623 C CG1 B ILE A 83 ? 0.1290 0.1038 0.1386 -0.0013 0.0195 0.0109 83 ILE A CG1 624 C CG2 A ILE A 83 ? 0.1077 0.0968 0.0842 0.0200 -0.0115 -0.0069 83 ILE A CG2 625 C CG2 B ILE A 83 ? 0.2476 0.1139 0.1294 0.0484 -0.0267 0.0047 83 ILE A CG2 626 C CD1 A ILE A 83 ? 0.1114 0.1207 0.1311 0.0057 -0.0266 0.0059 83 ILE A CD1 627 C CD1 B ILE A 83 ? 0.1069 0.1326 0.2114 -0.0038 -0.0202 0.0471 83 ILE A CD1 628 N N . ASP A 84 ? 0.0969 0.0950 0.1103 -0.0007 0.0011 -0.0055 84 ASP A N 629 C CA . ASP A 84 ? 0.1127 0.1033 0.1169 -0.0089 -0.0104 0.0021 84 ASP A CA 630 C C . ASP A 84 ? 0.1140 0.0896 0.1145 -0.0122 0.0027 0.0013 84 ASP A C 631 O O . ASP A 84 ? 0.1292 0.0960 0.1176 -0.0146 0.0135 -0.0073 84 ASP A O 632 C CB . ASP A 84 ? 0.1164 0.1236 0.1727 -0.0174 0.0059 -0.0096 84 ASP A CB 633 C CG . ASP A 84 ? 0.1490 0.1782 0.1609 -0.0185 0.0304 0.0120 84 ASP A CG 634 O OD1 . ASP A 84 ? 0.2486 0.4129 0.2645 -0.1128 0.0991 0.0186 84 ASP A OD1 635 O OD2 . ASP A 84 ? 0.2103 0.1665 0.1553 -0.0142 0.0147 -0.0043 84 ASP A OD2 636 N N . ASP A 85 ? 0.1374 0.1021 0.0955 0.0202 0.0035 0.0015 85 ASP A N 637 C CA . ASP A 85 ? 0.1704 0.1155 0.0961 0.0305 0.0131 0.0226 85 ASP A CA 638 C C . ASP A 85 ? 0.1370 0.1005 0.0953 0.0303 -0.0007 0.0209 85 ASP A C 639 O O . ASP A 85 ? 0.1531 0.0968 0.1046 0.0243 0.0100 0.0248 85 ASP A O 640 C CB . ASP A 85 ? 0.2250 0.2008 0.0894 0.0890 -0.0060 0.0276 85 ASP A CB 641 C CG . ASP A 85 ? 0.4070 0.2848 0.1007 0.0131 0.0452 0.0462 85 ASP A CG 642 O OD1 . ASP A 85 ? 0.3945 0.2671 0.1813 0.0203 0.0853 0.0764 85 ASP A OD1 643 O OD2 . ASP A 85 ? 0.7431 0.4539 0.0972 -0.0996 0.0435 -0.0004 85 ASP A OD2 644 N N . SER A 86 ? 0.1344 0.0945 0.0815 0.0274 -0.0095 0.0082 86 SER A N 645 C CA . SER A 86 ? 0.1124 0.0942 0.0833 0.0192 -0.0167 0.0095 86 SER A CA 646 C C . SER A 86 ? 0.0971 0.0852 0.0847 0.0052 -0.0093 0.0138 86 SER A C 647 O O . SER A 86 ? 0.1049 0.0913 0.0886 0.0094 -0.0051 0.0087 86 SER A O 648 C CB . SER A 86 ? 0.1220 0.0970 0.1100 0.0024 -0.0308 -0.0025 86 SER A CB 649 O OG . SER A 86 ? 0.1186 0.0903 0.1268 0.0056 -0.0180 0.0053 86 SER A OG 650 N N . VAL A 87 ? 0.1024 0.0906 0.0768 0.0127 -0.0159 0.0087 87 VAL A N 651 C CA . VAL A 87 ? 0.0975 0.0877 0.0816 0.0065 -0.0096 0.0114 87 VAL A CA 652 C C . VAL A 87 ? 0.0934 0.0949 0.0863 0.0107 -0.0153 0.0133 87 VAL A C 653 O O . VAL A 87 ? 0.1210 0.0875 0.0933 0.0136 -0.0130 0.0109 87 VAL A O 654 C CB . VAL A 87 ? 0.1042 0.1013 0.0863 0.0116 -0.0146 0.0156 87 VAL A CB 655 C CG1 . VAL A 87 ? 0.1283 0.1015 0.1091 0.0071 -0.0262 0.0162 87 VAL A CG1 656 C CG2 . VAL A 87 ? 0.1080 0.0897 0.1192 0.0144 -0.0186 0.0183 87 VAL A CG2 657 N N . ASN A 88 ? 0.1080 0.0775 0.0950 0.0068 -0.0080 0.0082 88 ASN A N 658 C CA . ASN A 88 ? 0.1049 0.0883 0.1014 0.0045 -0.0081 0.0114 88 ASN A CA 659 C C . ASN A 88 ? 0.1109 0.0810 0.0957 -0.0012 -0.0067 0.0170 88 ASN A C 660 O O . ASN A 88 ? 0.1199 0.0848 0.1110 0.0030 -0.0067 0.0089 88 ASN A O 661 C CB . ASN A 88 ? 0.1038 0.0965 0.1200 -0.0005 -0.0041 0.0171 88 ASN A CB 662 C CG . ASN A 88 ? 0.1048 0.1002 0.1248 -0.0042 -0.0061 0.0062 88 ASN A CG 663 O OD1 . ASN A 88 ? 0.1097 0.1321 0.1416 0.0003 -0.0298 0.0015 88 ASN A OD1 664 N ND2 . ASN A 88 ? 0.1172 0.1518 0.1508 0.0108 0.0204 0.0202 88 ASN A ND2 665 N N . ASN A 89 ? 0.1031 0.0807 0.0904 0.0049 -0.0066 0.0142 89 ASN A N 666 C CA . ASN A 89 ? 0.1136 0.0804 0.0960 0.0091 -0.0078 0.0251 89 ASN A CA 667 C C . ASN A 89 ? 0.1241 0.0857 0.0937 0.0199 -0.0051 0.0073 89 ASN A C 668 O O . ASN A 89 ? 0.1698 0.0990 0.1065 0.0353 0.0147 0.0250 89 ASN A O 669 C CB . ASN A 89 ? 0.1185 0.0876 0.0886 0.0077 -0.0111 0.0200 89 ASN A CB 670 C CG . ASN A 89 ? 0.1347 0.0869 0.0936 0.0043 -0.0036 0.0177 89 ASN A CG 671 O OD1 . ASN A 89 ? 0.1607 0.0963 0.1005 -0.0176 -0.0123 0.0238 89 ASN A OD1 672 N ND2 . ASN A 89 ? 0.2192 0.1472 0.0942 -0.0575 -0.0314 0.0221 89 ASN A ND2 673 N N . LEU A 90 ? 0.1090 0.0771 0.0777 0.0089 -0.0034 0.0131 90 LEU A N 674 C CA . LEU A 90 ? 0.0936 0.0873 0.0854 0.0087 -0.0053 0.0060 90 LEU A CA 675 C C . LEU A 90 ? 0.1179 0.0827 0.0854 0.0072 -0.0019 0.0120 90 LEU A C 676 O O . LEU A 90 ? 0.1292 0.0861 0.0949 -0.0085 0.0057 0.0011 90 LEU A O 677 C CB . LEU A 90 ? 0.0981 0.0912 0.0827 0.0076 -0.0060 0.0071 90 LEU A CB 678 C CG . LEU A 90 ? 0.0897 0.1075 0.0815 0.0054 -0.0032 -0.0003 90 LEU A CG 679 C CD1 . LEU A 90 ? 0.1232 0.0964 0.1150 0.0023 -0.0016 -0.0040 90 LEU A CD1 680 C CD2 . LEU A 90 ? 0.1093 0.1167 0.1286 0.0060 -0.0206 0.0249 90 LEU A CD2 681 N N . ILE A 91 ? 0.1088 0.0969 0.0918 -0.0077 -0.0113 0.0006 91 ILE A N 682 C CA . ILE A 91 ? 0.1261 0.0976 0.0948 -0.0035 -0.0130 0.0077 91 ILE A CA 683 C C . ILE A 91 ? 0.1250 0.0931 0.0983 -0.0169 -0.0082 0.0021 91 ILE A C 684 O O . ILE A 91 ? 0.1268 0.1037 0.1038 -0.0129 -0.0115 -0.0060 91 ILE A O 685 C CB . ILE A 91 ? 0.1148 0.1051 0.1147 -0.0131 -0.0137 0.0010 91 ILE A CB 686 C CG1 . ILE A 91 ? 0.1256 0.1087 0.1143 -0.0046 -0.0123 -0.0040 91 ILE A CG1 687 C CG2 . ILE A 91 ? 0.1389 0.1292 0.1482 -0.0242 -0.0173 -0.0135 91 ILE A CG2 688 C CD1 . ILE A 91 ? 0.1149 0.1477 0.1561 0.0014 -0.0163 -0.0045 91 ILE A CD1 689 N N . PRO A 92 ? 0.1301 0.0913 0.1066 -0.0093 0.0019 0.0044 92 PRO A N 690 C CA . PRO A 92 ? 0.1575 0.0878 0.1228 -0.0184 0.0008 0.0016 92 PRO A CA 691 C C . PRO A 92 ? 0.1543 0.0867 0.1075 -0.0038 -0.0084 -0.0060 92 PRO A C 692 O O . PRO A 92 ? 0.1651 0.0872 0.1322 -0.0104 -0.0019 -0.0103 92 PRO A O 693 C CB . PRO A 92 ? 0.1837 0.1005 0.1387 0.0058 0.0102 0.0269 92 PRO A CB 694 C CG . PRO A 92 ? 0.2469 0.1006 0.1337 0.0115 0.0242 0.0156 92 PRO A CG 695 C CD . PRO A 92 ? 0.1741 0.1105 0.0977 -0.0056 0.0005 0.0150 92 PRO A CD 696 N N . PHE A 93 ? 0.1330 0.0810 0.1038 -0.0021 0.0025 -0.0020 93 PHE A N 697 C CA . PHE A 93 ? 0.1382 0.0846 0.1053 0.0061 0.0022 -0.0019 93 PHE A CA 698 C C . PHE A 93 ? 0.1266 0.0938 0.1043 -0.0033 0.0016 -0.0093 93 PHE A C 699 O O . PHE A 93 ? 0.1538 0.1064 0.1000 0.0000 -0.0009 -0.0127 93 PHE A O 700 C CB . PHE A 93 ? 0.1227 0.0916 0.1120 0.0011 0.0003 -0.0035 93 PHE A CB 701 C CG . PHE A 93 ? 0.1158 0.0904 0.1166 0.0114 -0.0060 0.0031 93 PHE A CG 702 C CD1 . PHE A 93 ? 0.1177 0.1015 0.1179 0.0271 -0.0016 0.0044 93 PHE A CD1 703 C CD2 . PHE A 93 ? 0.1243 0.1313 0.1238 0.0256 0.0060 -0.0065 93 PHE A CD2 704 C CE1 . PHE A 93 ? 0.1419 0.1228 0.1217 0.0258 -0.0128 0.0155 93 PHE A CE1 705 C CE2 . PHE A 93 ? 0.1585 0.1416 0.1367 0.0483 -0.0197 0.0001 93 PHE A CE2 706 C CZ . PHE A 93 ? 0.1628 0.1295 0.1256 0.0437 -0.0179 0.0244 93 PHE A CZ 707 N N . MET A 94 ? 0.1367 0.0930 0.1011 -0.0066 -0.0064 0.0062 94 MET A N 708 C CA . MET A 94 ? 0.1428 0.0920 0.1050 -0.0093 -0.0145 -0.0011 94 MET A CA 709 C C . MET A 94 ? 0.1418 0.0987 0.1023 -0.0048 -0.0073 0.0006 94 MET A C 710 O O . MET A 94 ? 0.1844 0.1172 0.1011 -0.0230 -0.0178 -0.0066 94 MET A O 711 C CB . MET A 94 ? 0.1501 0.1009 0.1051 -0.0054 -0.0227 -0.0046 94 MET A CB 712 C CG . MET A 94 ? 0.1420 0.1236 0.1220 -0.0071 -0.0171 0.0108 94 MET A CG 713 S SD . MET A 94 ? 0.1623 0.1112 0.1430 -0.0100 -0.0363 0.0004 94 MET A SD 714 C CE . MET A 94 ? 0.1332 0.2193 0.1776 -0.0354 -0.0129 -0.0001 94 MET A CE 715 N N . GLN A 95 ? 0.1409 0.0960 0.1109 -0.0144 -0.0120 -0.0009 95 GLN A N 716 C CA . GLN A 95 ? 0.1777 0.1074 0.1178 -0.0261 -0.0178 -0.0084 95 GLN A CA 717 C C . GLN A 95 ? 0.1913 0.0992 0.1257 -0.0173 -0.0130 -0.0044 95 GLN A C 718 O O . GLN A 95 ? 0.2296 0.1318 0.1421 -0.0098 -0.0318 -0.0321 95 GLN A O 719 C CB . GLN A 95 ? 0.1803 0.1173 0.1434 -0.0332 -0.0081 -0.0055 95 GLN A CB 720 C CG . GLN A 95 ? 0.1654 0.1341 0.1431 -0.0317 -0.0156 -0.0066 95 GLN A CG 721 C CD . GLN A 95 ? 0.1847 0.1534 0.2130 -0.0323 0.0200 0.0065 95 GLN A CD 722 O OE1 . GLN A 95 ? 0.1719 0.2523 0.2979 -0.0317 0.0122 0.0189 95 GLN A OE1 723 N NE2 . GLN A 95 ? 0.2057 0.1443 0.2645 -0.0084 0.0645 0.0507 95 GLN A NE2 724 N N . LYS A 96 ? 0.1847 0.0976 0.1275 -0.0116 -0.0112 -0.0061 96 LYS A N 725 C CA . LYS A 96 ? 0.1994 0.0924 0.1416 -0.0084 -0.0032 -0.0071 96 LYS A CA 726 C C . LYS A 96 ? 0.1800 0.0980 0.1278 -0.0124 -0.0124 -0.0308 96 LYS A C 727 O O . LYS A 96 ? 0.2219 0.1010 0.1508 -0.0110 0.0011 -0.0258 96 LYS A O 728 C CB . LYS A 96 ? 0.2026 0.0975 0.1704 -0.0026 -0.0250 0.0090 96 LYS A CB 729 C CG . LYS A 96 ? 0.2413 0.1126 0.2175 0.0232 -0.0424 -0.0136 96 LYS A CG 730 C CD . LYS A 96 ? 0.3184 0.1354 0.2854 0.0151 -0.1030 0.0706 96 LYS A CD 731 C CE . LYS A 96 ? 0.5068 0.1795 0.4976 0.1465 -0.3121 -0.1142 96 LYS A CE 732 N NZ . LYS A 96 ? 0.5417 0.1181 0.5758 0.0015 -0.4003 0.0285 96 LYS A NZ 733 N N . HIS A 97 ? 0.1730 0.0954 0.1138 -0.0104 -0.0032 -0.0108 97 HIS A N 734 C CA . HIS A 97 ? 0.1619 0.1130 0.1091 -0.0034 -0.0028 -0.0061 97 HIS A CA 735 C C . HIS A 97 ? 0.1826 0.1039 0.1034 -0.0134 -0.0081 -0.0169 97 HIS A C 736 O O . HIS A 97 ? 0.1703 0.1010 0.1116 -0.0060 -0.0131 -0.0112 97 HIS A O 737 C CB . HIS A 97 ? 0.1615 0.1056 0.1151 -0.0185 -0.0099 -0.0139 97 HIS A CB 738 C CG . HIS A 97 ? 0.1481 0.0989 0.1212 -0.0142 -0.0059 -0.0099 97 HIS A CG 739 N ND1 . HIS A 97 ? 0.1673 0.1291 0.1350 0.0096 0.0032 0.0001 97 HIS A ND1 740 C CD2 . HIS A 97 ? 0.1658 0.1255 0.1136 0.0060 -0.0069 -0.0030 97 HIS A CD2 741 C CE1 . HIS A 97 ? 0.1748 0.1446 0.1311 0.0116 0.0056 0.0142 97 HIS A CE1 742 N NE2 . HIS A 97 ? 0.1562 0.1247 0.1359 0.0018 -0.0085 0.0055 97 HIS A NE2 743 N N . ASN A 98 ? 0.1904 0.1027 0.1266 -0.0107 -0.0294 -0.0119 98 ASN A N 744 C CA . ASN A 98 ? 0.1992 0.1158 0.1295 -0.0119 -0.0258 -0.0074 98 ASN A CA 745 C C . ASN A 98 ? 0.2001 0.1275 0.1086 -0.0127 -0.0350 -0.0235 98 ASN A C 746 O O . ASN A 98 ? 0.2026 0.1613 0.1262 -0.0181 -0.0267 -0.0092 98 ASN A O 747 C CB . ASN A 98 ? 0.2098 0.1330 0.1579 -0.0244 -0.0428 -0.0225 98 ASN A CB 748 C CG . ASN A 98 ? 0.2506 0.1728 0.1893 -0.0423 -0.0212 -0.0704 98 ASN A CG 749 O OD1 . ASN A 98 ? 0.2523 0.1720 0.2937 -0.0257 -0.0271 -0.1104 98 ASN A OD1 750 N ND2 . ASN A 98 ? 0.2611 0.1834 0.2379 -0.0360 -0.0528 -0.0781 98 ASN A ND2 751 N N . THR A 99 ? 0.1958 0.1167 0.0995 -0.0002 -0.0218 -0.0182 99 THR A N 752 C CA . THR A 99 ? 0.1943 0.1232 0.1026 0.0141 -0.0049 -0.0189 99 THR A CA 753 C C . THR A 99 ? 0.1483 0.1301 0.0954 0.0003 0.0060 -0.0185 99 THR A C 754 O O . THR A 99 ? 0.2228 0.1393 0.1033 -0.0095 0.0161 -0.0128 99 THR A O 755 C CB . THR A 99 ? 0.2191 0.1503 0.1227 0.0291 0.0031 -0.0354 99 THR A CB 756 O OG1 . THR A 99 ? 0.2046 0.1844 0.1440 0.0499 0.0036 -0.0062 99 THR A OG1 757 C CG2 . THR A 99 ? 0.2959 0.1664 0.1774 0.0462 0.0226 -0.0690 99 THR A CG2 758 N N . ILE A 100 ? 0.1402 0.1038 0.0929 -0.0012 -0.0009 -0.0182 100 ILE A N 759 C CA . ILE A 100 ? 0.1306 0.0979 0.0907 0.0040 0.0000 -0.0091 100 ILE A CA 760 C C . ILE A 100 ? 0.1114 0.1034 0.0871 -0.0066 -0.0039 -0.0064 100 ILE A C 761 O O . ILE A 100 ? 0.1285 0.0986 0.1033 0.0017 0.0049 -0.0019 100 ILE A O 762 C CB . ILE A 100 ? 0.1204 0.0961 0.0985 0.0062 -0.0091 -0.0147 100 ILE A CB 763 C CG1 . ILE A 100 ? 0.1296 0.1094 0.1247 0.0163 -0.0014 -0.0235 100 ILE A CG1 764 C CG2 . ILE A 100 ? 0.1088 0.0889 0.1111 0.0053 -0.0014 -0.0183 100 ILE A CG2 765 C CD1 . ILE A 100 ? 0.1491 0.1226 0.1278 0.0254 -0.0224 -0.0172 100 ILE A CD1 766 N N . SER A 101 ? 0.1006 0.1024 0.0807 -0.0040 -0.0026 -0.0064 101 SER A N 767 C CA . SER A 101 ? 0.1009 0.0967 0.0783 -0.0102 -0.0078 -0.0079 101 SER A CA 768 C C . SER A 101 ? 0.1027 0.0828 0.0768 -0.0043 -0.0072 0.0021 101 SER A C 769 O O . SER A 101 ? 0.0904 0.0994 0.0793 -0.0040 -0.0130 -0.0020 101 SER A O 770 C CB . SER A 101 ? 0.1136 0.1030 0.0722 -0.0002 -0.0128 -0.0026 101 SER A CB 771 O OG . SER A 101 ? 0.1102 0.0980 0.0879 -0.0066 -0.0156 0.0020 101 SER A OG 772 N N . ALA A 102 ? 0.0920 0.0933 0.0819 -0.0086 -0.0120 -0.0102 102 ALA A N 773 C CA . ALA A 102 ? 0.0987 0.0868 0.0777 -0.0005 -0.0066 -0.0001 102 ALA A CA 774 C C . ALA A 102 ? 0.0732 0.0872 0.0870 0.0000 -0.0104 0.0006 102 ALA A C 775 O O . ALA A 102 ? 0.0883 0.0900 0.0746 -0.0080 -0.0084 0.0051 102 ALA A O 776 C CB . ALA A 102 ? 0.0917 0.1059 0.1057 -0.0165 -0.0120 -0.0003 102 ALA A CB 777 N N . ALA A 103 ? 0.0843 0.0836 0.0804 -0.0019 -0.0137 -0.0025 103 ALA A N 778 C CA . ALA A 103 ? 0.0846 0.0812 0.0799 -0.0018 -0.0036 0.0004 103 ALA A CA 779 C C . ALA A 103 ? 0.0755 0.0858 0.0803 -0.0042 0.0008 0.0117 103 ALA A C 780 O O . ALA A 103 ? 0.0809 0.0900 0.0757 -0.0035 -0.0051 -0.0005 103 ALA A O 781 C CB . ALA A 103 ? 0.0891 0.0857 0.0992 0.0015 -0.0118 0.0069 103 ALA A CB 782 N N . ASP A 104 ? 0.0820 0.0880 0.0683 0.0011 -0.0019 0.0029 104 ASP A N 783 C CA . ASP A 104 ? 0.0801 0.0878 0.0707 0.0016 -0.0054 0.0054 104 ASP A CA 784 C C . ASP A 104 ? 0.0885 0.0836 0.0684 -0.0003 -0.0006 0.0068 104 ASP A C 785 O O . ASP A 104 ? 0.0775 0.1065 0.0777 0.0004 -0.0090 0.0059 104 ASP A O 786 C CB . ASP A 104 ? 0.0806 0.0899 0.0739 0.0034 -0.0067 0.0027 104 ASP A CB 787 C CG . ASP A 104 ? 0.1013 0.0997 0.0740 0.0032 0.0005 0.0066 104 ASP A CG 788 O OD1 . ASP A 104 ? 0.1151 0.0953 0.0844 -0.0029 -0.0045 0.0027 104 ASP A OD1 789 O OD2 . ASP A 104 ? 0.1282 0.1056 0.0794 -0.0068 0.0106 -0.0033 104 ASP A OD2 790 N N . LEU A 105 ? 0.0928 0.0836 0.0687 -0.0006 -0.0106 0.0039 105 LEU A N 791 C CA . LEU A 105 ? 0.0831 0.0827 0.0761 0.0028 -0.0005 0.0045 105 LEU A CA 792 C C . LEU A 105 ? 0.0896 0.0819 0.0701 -0.0023 -0.0001 0.0065 105 LEU A C 793 O O . LEU A 105 ? 0.0928 0.0861 0.0781 0.0029 -0.0151 0.0074 105 LEU A O 794 C CB . LEU A 105 ? 0.0991 0.0780 0.0799 0.0021 -0.0041 0.0074 105 LEU A CB 795 C CG . LEU A 105 ? 0.1017 0.0826 0.0793 -0.0001 -0.0014 0.0045 105 LEU A CG 796 C CD1 . LEU A 105 ? 0.1208 0.0972 0.0991 0.0075 -0.0047 0.0152 105 LEU A CD1 797 C CD2 . LEU A 105 ? 0.1122 0.0854 0.1042 -0.0079 0.0093 0.0023 105 LEU A CD2 798 N N . VAL A 106 ? 0.0840 0.0848 0.0702 0.0006 -0.0086 0.0060 106 VAL A N 799 C CA . VAL A 106 ? 0.0765 0.0770 0.0701 0.0000 -0.0033 0.0034 106 VAL A CA 800 C C . VAL A 106 ? 0.0710 0.0840 0.0740 0.0019 -0.0016 0.0059 106 VAL A C 801 O O . VAL A 106 ? 0.0933 0.0928 0.0706 -0.0106 -0.0109 0.0049 106 VAL A O 802 C CB . VAL A 106 ? 0.0790 0.0836 0.0796 -0.0011 -0.0001 0.0075 106 VAL A CB 803 C CG1 . VAL A 106 ? 0.0997 0.0951 0.0891 0.0059 -0.0024 -0.0051 106 VAL A CG1 804 C CG2 . VAL A 106 ? 0.0843 0.1073 0.0911 -0.0015 -0.0007 0.0015 106 VAL A CG2 805 N N . GLN A 107 ? 0.0773 0.0800 0.0754 0.0007 -0.0040 0.0133 107 GLN A N 806 C CA . GLN A 107 ? 0.0772 0.0819 0.0709 -0.0014 -0.0014 0.0072 107 GLN A CA 807 C C . GLN A 107 ? 0.0788 0.0784 0.0729 0.0032 0.0015 0.0110 107 GLN A C 808 O O . GLN A 107 ? 0.0853 0.0880 0.0829 0.0026 -0.0158 0.0034 107 GLN A O 809 C CB . GLN A 107 ? 0.0848 0.0774 0.0838 -0.0032 -0.0034 0.0118 107 GLN A CB 810 C CG . GLN A 107 ? 0.0916 0.0829 0.0879 -0.0036 -0.0066 0.0112 107 GLN A CG 811 C CD . GLN A 107 ? 0.0894 0.0779 0.0868 -0.0009 -0.0136 0.0118 107 GLN A CD 812 O OE1 . GLN A 107 ? 0.0989 0.1084 0.1193 0.0094 -0.0089 0.0154 107 GLN A OE1 813 N NE2 . GLN A 107 ? 0.0701 0.0799 0.1023 0.0047 -0.0140 -0.0165 107 GLN A NE2 814 N N . PHE A 108 ? 0.0776 0.0835 0.0765 0.0029 -0.0078 0.0070 108 PHE A N 815 C CA . PHE A 108 ? 0.0851 0.0853 0.0737 0.0089 -0.0072 0.0064 108 PHE A CA 816 C C . PHE A 108 ? 0.0869 0.0826 0.0726 0.0056 -0.0035 -0.0002 108 PHE A C 817 O O . PHE A 108 ? 0.0854 0.0944 0.0762 0.0055 -0.0121 0.0057 108 PHE A O 818 C CB . PHE A 108 ? 0.1038 0.0897 0.0766 0.0099 0.0002 0.0036 108 PHE A CB 819 C CG . PHE A 108 ? 0.1004 0.0957 0.0699 0.0136 -0.0071 -0.0018 108 PHE A CG 820 C CD1 . PHE A 108 ? 0.1070 0.0942 0.0864 0.0083 -0.0033 -0.0030 108 PHE A CD1 821 C CD2 . PHE A 108 ? 0.1020 0.0992 0.0795 0.0123 0.0025 0.0069 108 PHE A CD2 822 C CE1 . PHE A 108 ? 0.1197 0.0926 0.0976 0.0241 -0.0020 0.0048 108 PHE A CE1 823 C CE2 . PHE A 108 ? 0.0995 0.1198 0.0918 0.0108 0.0044 0.0045 108 PHE A CE2 824 C CZ . PHE A 108 ? 0.1163 0.1079 0.0953 0.0332 0.0041 0.0011 108 PHE A CZ 825 N N . ALA A 109 ? 0.0860 0.0888 0.0701 0.0037 -0.0093 0.0111 109 ALA A N 826 C CA . ALA A 109 ? 0.0824 0.0867 0.0733 0.0019 -0.0090 0.0124 109 ALA A CA 827 C C . ALA A 109 ? 0.0779 0.0860 0.0726 -0.0013 -0.0027 0.0056 109 ALA A C 828 O O . ALA A 109 ? 0.0910 0.0910 0.0806 0.0031 -0.0115 0.0110 109 ALA A O 829 C CB . ALA A 109 ? 0.0989 0.0958 0.0844 -0.0090 -0.0016 0.0019 109 ALA A CB 830 N N . GLY A 110 ? 0.0828 0.0868 0.0732 0.0021 -0.0108 0.0080 110 GLY A N 831 C CA . GLY A 110 ? 0.0911 0.0859 0.0844 0.0062 -0.0125 -0.0002 110 GLY A CA 832 C C . GLY A 110 ? 0.0855 0.0746 0.0939 0.0008 -0.0122 0.0021 110 GLY A C 833 O O . GLY A 110 ? 0.0980 0.0955 0.0819 -0.0026 -0.0162 0.0031 110 GLY A O 834 N N . ALA A 111 ? 0.0913 0.0936 0.0792 -0.0014 -0.0092 0.0085 111 ALA A N 835 C CA . ALA A 111 ? 0.0926 0.0910 0.0858 -0.0014 -0.0107 0.0127 111 ALA A CA 836 C C . ALA A 111 ? 0.0942 0.0874 0.0854 0.0016 -0.0086 0.0010 111 ALA A C 837 O O . ALA A 111 ? 0.0871 0.1075 0.0956 0.0003 -0.0190 0.0114 111 ALA A O 838 C CB . ALA A 111 ? 0.0975 0.1118 0.0925 -0.0026 -0.0033 0.0098 111 ALA A CB 839 N N . VAL A 112 ? 0.0914 0.0961 0.0799 0.0079 -0.0156 0.0062 112 VAL A N 840 C CA . VAL A 112 ? 0.0872 0.0860 0.0878 0.0132 -0.0043 0.0051 112 VAL A CA 841 C C . VAL A 112 ? 0.0888 0.0869 0.0851 0.0013 -0.0091 0.0076 112 VAL A C 842 O O . VAL A 112 ? 0.0955 0.1047 0.0965 0.0125 -0.0241 0.0104 112 VAL A O 843 C CB . VAL A 112 ? 0.1040 0.0971 0.0838 0.0097 -0.0057 0.0023 112 VAL A CB 844 C CG1 . VAL A 112 ? 0.1304 0.0966 0.1114 0.0157 -0.0179 0.0035 112 VAL A CG1 845 C CG2 . VAL A 112 ? 0.1172 0.1065 0.0911 0.0190 -0.0082 -0.0055 112 VAL A CG2 846 N N . ALA A 113 ? 0.0911 0.0941 0.0787 0.0080 -0.0124 0.0035 113 ALA A N 847 C CA . ALA A 113 ? 0.1057 0.0922 0.0696 0.0093 -0.0066 0.0094 113 ALA A CA 848 C C . ALA A 113 ? 0.0895 0.0999 0.0857 0.0064 -0.0180 0.0019 113 ALA A C 849 O O . ALA A 113 ? 0.1078 0.1118 0.0804 0.0052 -0.0202 0.0114 113 ALA A O 850 C CB . ALA A 113 ? 0.0922 0.0976 0.0856 0.0035 -0.0072 0.0072 113 ALA A CB 851 N N . LEU A 114 ? 0.1087 0.0944 0.0896 0.0052 -0.0292 0.0076 114 LEU A N 852 C CA . LEU A 114 ? 0.1096 0.0912 0.0961 0.0017 -0.0309 -0.0064 114 LEU A CA 853 C C . LEU A 114 ? 0.1099 0.0881 0.1040 0.0015 -0.0326 0.0054 114 LEU A C 854 O O . LEU A 114 ? 0.1229 0.1015 0.1150 -0.0059 -0.0484 0.0059 114 LEU A O 855 C CB A LEU A 114 ? 0.1260 0.0933 0.0995 -0.0012 -0.0398 0.0065 114 LEU A CB 856 C CB B LEU A 114 ? 0.1262 0.0980 0.1200 0.0049 -0.0482 0.0037 114 LEU A CB 857 C CG A LEU A 114 ? 0.1184 0.0762 0.0872 -0.0136 -0.0255 0.0044 114 LEU A CG 858 C CG B LEU A 114 ? 0.1091 0.1005 0.1481 -0.0135 -0.0262 -0.0111 114 LEU A CG 859 C CD1 A LEU A 114 ? 0.1746 0.0734 0.1196 -0.0192 -0.0711 0.0235 114 LEU A CD1 860 C CD1 B LEU A 114 ? 0.2624 0.1836 0.1552 0.0145 0.0177 -0.0474 114 LEU A CD1 861 C CD2 A LEU A 114 ? 0.1563 0.0731 0.0964 -0.0240 -0.0287 0.0073 114 LEU A CD2 862 C CD2 B LEU A 114 ? 0.1521 0.1185 0.1898 0.0040 -0.0114 0.0207 114 LEU A CD2 863 N N . SER A 115 ? 0.0956 0.1080 0.1041 -0.0025 -0.0219 0.0068 115 SER A N 864 C CA . SER A 115 ? 0.0928 0.1262 0.1100 0.0007 -0.0165 0.0026 115 SER A CA 865 C C . SER A 115 ? 0.1007 0.1131 0.1040 0.0066 -0.0119 0.0036 115 SER A C 866 O O . SER A 115 ? 0.0948 0.1508 0.1328 0.0040 -0.0204 0.0174 115 SER A O 867 C CB . SER A 115 ? 0.1054 0.1518 0.1103 0.0093 -0.0085 0.0012 115 SER A CB 868 O OG . SER A 115 ? 0.1197 0.1495 0.1401 0.0149 -0.0136 -0.0203 115 SER A OG 869 N N . ASN A 116 ? 0.0917 0.0996 0.1134 0.0052 -0.0250 0.0057 116 ASN A N 870 C CA . ASN A 116 ? 0.1002 0.0916 0.0999 0.0113 -0.0199 0.0072 116 ASN A CA 871 C C . ASN A 116 ? 0.1058 0.0931 0.1097 0.0058 -0.0275 -0.0067 116 ASN A C 872 O O . ASN A 116 ? 0.1576 0.1131 0.1165 0.0244 -0.0556 0.0111 116 ASN A O 873 C CB . ASN A 116 ? 0.1126 0.0872 0.1126 0.0087 -0.0279 0.0006 116 ASN A CB 874 C CG . ASN A 116 ? 0.1094 0.0970 0.1129 0.0011 -0.0329 0.0141 116 ASN A CG 875 O OD1 . ASN A 116 ? 0.1346 0.1160 0.1415 0.0048 -0.0093 -0.0188 116 ASN A OD1 876 N ND2 . ASN A 116 ? 0.1284 0.1074 0.1359 0.0000 -0.0338 -0.0092 116 ASN A ND2 877 N N . CYS A 117 ? 0.0963 0.0874 0.1103 0.0023 -0.0239 0.0069 117 CYS A N 878 C CA . CYS A 117 ? 0.1054 0.0993 0.0986 0.0005 -0.0240 -0.0016 117 CYS A CA 879 C C . CYS A 117 ? 0.0899 0.1069 0.1038 0.0008 -0.0210 0.0026 117 CYS A C 880 O O . CYS A 117 ? 0.1031 0.1190 0.1117 -0.0096 -0.0273 0.0131 117 CYS A O 881 C CB . CYS A 117 ? 0.1031 0.0944 0.1304 0.0029 -0.0215 -0.0007 117 CYS A CB 882 S SG . CYS A 117 ? 0.1043 0.1219 0.1329 0.0057 -0.0272 -0.0145 117 CYS A SG 883 N N . PRO A 118 ? 0.0963 0.1012 0.0985 0.0127 -0.0218 -0.0003 118 PRO A N 884 C CA . PRO A 118 ? 0.0810 0.1173 0.1057 0.0084 -0.0232 0.0003 118 PRO A CA 885 C C . PRO A 118 ? 0.0964 0.1065 0.0852 0.0090 -0.0236 -0.0057 118 PRO A C 886 O O . PRO A 118 ? 0.0977 0.1110 0.0939 0.0103 -0.0119 0.0021 118 PRO A O 887 C CB . PRO A 118 ? 0.1133 0.1124 0.1166 0.0168 -0.0301 0.0041 118 PRO A CB 888 C CG . PRO A 118 ? 0.1418 0.1230 0.1133 0.0151 -0.0473 0.0032 118 PRO A CG 889 C CD . PRO A 118 ? 0.1141 0.0950 0.1044 0.0115 -0.0144 0.0082 118 PRO A CD 890 N N . GLY A 119 ? 0.0853 0.1301 0.0946 0.0042 -0.0161 -0.0117 119 GLY A N 891 C CA . GLY A 119 ? 0.1025 0.1246 0.0953 -0.0083 -0.0252 0.0018 119 GLY A CA 892 C C . GLY A 119 ? 0.0841 0.1213 0.1031 -0.0105 -0.0184 -0.0077 119 GLY A C 893 O O . GLY A 119 ? 0.1070 0.1211 0.1091 -0.0190 -0.0186 0.0007 119 GLY A O 894 N N . ALA A 120 ? 0.1096 0.1136 0.0847 -0.0125 -0.0247 0.0028 120 ALA A N 895 C CA . ALA A 120 ? 0.0927 0.1144 0.0888 -0.0096 -0.0202 0.0054 120 ALA A CA 896 C C . ALA A 120 ? 0.1116 0.1070 0.0886 0.0022 -0.0187 0.0006 120 ALA A C 897 O O . ALA A 120 ? 0.1407 0.1315 0.0920 0.0326 -0.0128 0.0060 120 ALA A O 898 C CB . ALA A 120 ? 0.1318 0.1531 0.1139 -0.0431 -0.0461 0.0298 120 ALA A CB 899 N N . PRO A 121 ? 0.1026 0.1079 0.0875 0.0043 -0.0100 0.0004 121 PRO A N 900 C CA . PRO A 121 ? 0.0976 0.1200 0.0812 0.0045 -0.0016 0.0043 121 PRO A CA 901 C C . PRO A 121 ? 0.0896 0.1144 0.0890 0.0096 -0.0064 0.0087 121 PRO A C 902 O O . PRO A 121 ? 0.1110 0.1352 0.1052 -0.0084 -0.0022 -0.0138 121 PRO A O 903 C CB . PRO A 121 ? 0.1258 0.1123 0.1038 -0.0023 -0.0086 0.0084 121 PRO A CB 904 C CG . PRO A 121 ? 0.1092 0.1187 0.1139 0.0088 -0.0265 0.0032 121 PRO A CG 905 C CD . PRO A 121 ? 0.0857 0.1151 0.1102 0.0067 -0.0106 -0.0026 121 PRO A CD 906 N N . ARG A 122 ? 0.0910 0.1371 0.0968 0.0128 -0.0069 -0.0045 122 ARG A N 907 C CA . ARG A 122 ? 0.0881 0.1246 0.0907 0.0144 -0.0082 -0.0015 122 ARG A CA 908 C C . ARG A 122 ? 0.0911 0.1209 0.0932 0.0069 -0.0081 0.0012 122 ARG A C 909 O O . ARG A 122 ? 0.0989 0.1473 0.1097 0.0113 -0.0035 0.0169 122 ARG A O 910 C CB . ARG A 122 ? 0.0890 0.1453 0.0961 0.0200 -0.0018 -0.0050 122 ARG A CB 911 C CG . ARG A 122 ? 0.0959 0.1336 0.1035 0.0095 -0.0036 -0.0035 122 ARG A CG 912 C CD . ARG A 122 ? 0.1086 0.1550 0.1330 0.0186 0.0059 -0.0222 122 ARG A CD 913 N NE . ARG A 122 ? 0.1056 0.1589 0.1408 0.0172 0.0019 -0.0323 122 ARG A NE 914 C CZ . ARG A 122 ? 0.1214 0.2087 0.1807 -0.0046 0.0414 -0.0639 122 ARG A CZ 915 N NH1 . ARG A 122 ? 0.1410 0.2335 0.2539 -0.0360 0.0655 -0.0973 122 ARG A NH1 916 N NH2 . ARG A 122 ? 0.1476 0.2025 0.2047 -0.0175 0.0393 -0.0706 122 ARG A NH2 917 N N . LEU A 123 ? 0.1025 0.1074 0.0879 0.0019 -0.0135 0.0003 123 LEU A N 918 C CA . LEU A 123 ? 0.0964 0.1029 0.0885 0.0034 -0.0203 -0.0063 123 LEU A CA 919 C C . LEU A 123 ? 0.0973 0.1084 0.0896 0.0053 -0.0117 -0.0072 123 LEU A C 920 O O . LEU A 123 ? 0.1279 0.1123 0.0950 0.0120 -0.0095 -0.0070 123 LEU A O 921 C CB . LEU A 123 ? 0.0969 0.1160 0.1006 0.0032 -0.0108 0.0004 123 LEU A CB 922 C CG . LEU A 123 ? 0.1044 0.1205 0.1063 0.0118 0.0026 0.0045 123 LEU A CG 923 C CD1 . LEU A 123 ? 0.1015 0.1369 0.1711 0.0101 0.0088 0.0049 123 LEU A CD1 924 C CD2 . LEU A 123 ? 0.1136 0.1435 0.0993 0.0079 -0.0025 -0.0074 123 LEU A CD2 925 N N . GLU A 124 ? 0.0917 0.1048 0.0966 0.0015 -0.0130 -0.0042 124 GLU A N 926 C CA . GLU A 124 ? 0.0887 0.1208 0.0929 -0.0057 -0.0124 -0.0002 124 GLU A CA 927 C C . GLU A 124 ? 0.0859 0.1165 0.0918 0.0054 -0.0124 -0.0016 124 GLU A C 928 O O . GLU A 124 ? 0.0958 0.1435 0.0984 -0.0132 -0.0087 -0.0143 124 GLU A O 929 C CB . GLU A 124 ? 0.0971 0.1252 0.1074 -0.0043 -0.0093 0.0034 124 GLU A CB 930 C CG . GLU A 124 ? 0.1307 0.1423 0.0953 0.0117 0.0024 0.0143 124 GLU A CG 931 C CD . GLU A 124 ? 0.1261 0.1256 0.1439 -0.0046 -0.0088 0.0186 124 GLU A CD 932 O OE1 . GLU A 124 ? 0.1587 0.1963 0.2645 -0.0141 0.0545 0.0817 124 GLU A OE1 933 O OE2 . GLU A 124 ? 0.1385 0.1276 0.1214 -0.0073 -0.0018 0.0054 124 GLU A OE2 934 N N . PHE A 125 ? 0.0909 0.1155 0.0872 0.0018 -0.0153 -0.0051 125 PHE A N 935 C CA . PHE A 125 ? 0.0845 0.1135 0.0783 -0.0005 -0.0067 -0.0003 125 PHE A CA 936 C C . PHE A 125 ? 0.0947 0.0976 0.0803 -0.0013 -0.0093 0.0007 125 PHE A C 937 O O . PHE A 125 ? 0.1041 0.1290 0.0929 0.0175 -0.0025 -0.0069 125 PHE A O 938 C CB . PHE A 125 ? 0.1097 0.1067 0.0903 0.0085 -0.0116 0.0050 125 PHE A CB 939 C CG . PHE A 125 ? 0.0990 0.0948 0.0891 0.0050 -0.0107 0.0112 125 PHE A CG 940 C CD1 . PHE A 125 ? 0.1169 0.0989 0.0907 -0.0025 0.0009 0.0055 125 PHE A CD1 941 C CD2 . PHE A 125 ? 0.1004 0.1076 0.0928 0.0039 0.0019 0.0088 125 PHE A CD2 942 C CE1 . PHE A 125 ? 0.1018 0.0942 0.1115 -0.0024 0.0041 0.0108 125 PHE A CE1 943 C CE2 . PHE A 125 ? 0.1134 0.1195 0.0945 -0.0034 0.0019 -0.0018 125 PHE A CE2 944 C CZ . PHE A 125 ? 0.1055 0.1039 0.1055 -0.0104 -0.0083 0.0065 125 PHE A CZ 945 N N . LEU A 126 ? 0.0941 0.1133 0.0755 0.0034 -0.0041 0.0002 126 LEU A N 946 C CA . LEU A 126 ? 0.0875 0.1194 0.0773 0.0027 -0.0104 0.0100 126 LEU A CA 947 C C . LEU A 126 ? 0.0862 0.1109 0.0900 0.0047 -0.0093 0.0011 126 LEU A C 948 O O . LEU A 126 ? 0.0956 0.1324 0.1071 -0.0097 0.0057 -0.0190 126 LEU A O 949 C CB . LEU A 126 ? 0.1058 0.1237 0.0792 -0.0075 -0.0144 0.0099 126 LEU A CB 950 C CG . LEU A 126 ? 0.1152 0.1179 0.0932 -0.0085 -0.0069 0.0017 126 LEU A CG 951 C CD1 . LEU A 126 ? 0.1405 0.1227 0.1249 -0.0054 0.0048 0.0101 126 LEU A CD1 952 C CD2 . LEU A 126 ? 0.1110 0.1316 0.1222 -0.0175 -0.0037 0.0019 126 LEU A CD2 953 N N . ALA A 127 ? 0.1008 0.1342 0.0868 -0.0159 -0.0018 0.0026 127 ALA A N 954 C CA . ALA A 127 ? 0.1045 0.1159 0.0837 -0.0188 -0.0119 0.0065 127 ALA A CA 955 C C . ALA A 127 ? 0.1090 0.1068 0.0753 -0.0064 -0.0022 0.0048 127 ALA A C 956 O O . ALA A 127 ? 0.1297 0.1333 0.0888 -0.0237 -0.0113 0.0254 127 ALA A O 957 C CB . ALA A 127 ? 0.1351 0.1195 0.1277 -0.0076 -0.0272 0.0203 127 ALA A CB 958 N N . GLY A 128 ? 0.1074 0.1205 0.0736 -0.0143 -0.0077 0.0022 128 GLY A N 959 C CA . GLY A 128 ? 0.1179 0.1218 0.0789 -0.0053 -0.0067 0.0036 128 GLY A CA 960 C C . GLY A 128 ? 0.1158 0.1293 0.0704 -0.0100 -0.0132 0.0051 128 GLY A C 961 O O . GLY A 128 ? 0.1242 0.1725 0.0845 0.0031 -0.0103 0.0130 128 GLY A O 962 N N . ARG A 129 ? 0.1019 0.1122 0.0733 -0.0072 -0.0031 0.0042 129 ARG A N 963 C CA . ARG A 129 ? 0.1156 0.0955 0.0821 -0.0040 -0.0132 0.0045 129 ARG A CA 964 C C . ARG A 129 ? 0.1012 0.1126 0.0792 -0.0019 -0.0120 0.0099 129 ARG A C 965 O O . ARG A 129 ? 0.1159 0.1031 0.0927 -0.0115 -0.0149 0.0073 129 ARG A O 966 C CB . ARG A 129 ? 0.0983 0.0956 0.0759 -0.0021 -0.0065 0.0065 129 ARG A CB 967 C CG . ARG A 129 ? 0.1032 0.0993 0.0796 -0.0044 -0.0115 0.0059 129 ARG A CG 968 C CD . ARG A 129 ? 0.0966 0.0991 0.0800 -0.0035 -0.0086 -0.0020 129 ARG A CD 969 N NE . ARG A 129 ? 0.0936 0.0981 0.0905 -0.0043 -0.0025 -0.0050 129 ARG A NE 970 C CZ . ARG A 129 ? 0.0857 0.1143 0.0778 -0.0025 -0.0022 0.0003 129 ARG A CZ 971 N NH1 . ARG A 129 ? 0.0961 0.0929 0.1064 0.0058 -0.0045 -0.0018 129 ARG A NH1 972 N NH2 . ARG A 129 ? 0.0915 0.1171 0.1130 -0.0035 -0.0075 -0.0206 129 ARG A NH2 973 N N . PRO A 130 ? 0.1151 0.1178 0.0780 -0.0122 -0.0164 0.0071 130 PRO A N 974 C CA . PRO A 130 ? 0.1244 0.1459 0.0826 -0.0196 -0.0197 0.0028 130 PRO A CA 975 C C . PRO A 130 ? 0.1023 0.1064 0.0911 -0.0041 -0.0174 -0.0028 130 PRO A C 976 O O . PRO A 130 ? 0.1196 0.1196 0.0909 -0.0226 -0.0057 -0.0099 130 PRO A O 977 C CB . PRO A 130 ? 0.1500 0.1870 0.1249 -0.0274 -0.0549 0.0407 130 PRO A CB 978 C CG . PRO A 130 ? 0.2146 0.1674 0.1990 -0.0490 -0.1098 0.0622 130 PRO A CG 979 C CD . PRO A 130 ? 0.1503 0.1220 0.1011 0.0025 -0.0333 0.0179 130 PRO A CD 980 N N . ASN A 131 ? 0.1167 0.1225 0.0881 -0.0150 -0.0158 -0.0106 131 ASN A N 981 C CA . ASN A 131 ? 0.1186 0.1231 0.0839 -0.0174 -0.0164 -0.0098 131 ASN A CA 982 C C . ASN A 131 ? 0.1197 0.1234 0.0991 -0.0175 -0.0120 -0.0111 131 ASN A C 983 O O . ASN A 131 ? 0.1221 0.1613 0.1596 -0.0204 -0.0074 0.0154 131 ASN A O 984 C CB . ASN A 131 ? 0.1200 0.1207 0.0993 -0.0156 -0.0159 -0.0148 131 ASN A CB 985 C CG . ASN A 131 ? 0.1131 0.1132 0.1078 -0.0227 -0.0100 -0.0131 131 ASN A CG 986 O OD1 . ASN A 131 ? 0.1232 0.1168 0.1001 -0.0188 -0.0302 -0.0107 131 ASN A OD1 987 N ND2 . ASN A 131 ? 0.1437 0.1195 0.1140 -0.0308 -0.0292 -0.0109 131 ASN A ND2 988 N N . LYS A 132 ? 0.1114 0.1340 0.1382 -0.0096 -0.0090 -0.0067 132 LYS A N 989 C CA . LYS A 132 ? 0.1253 0.1433 0.1225 -0.0006 -0.0126 -0.0181 132 LYS A CA 990 C C . LYS A 132 ? 0.1171 0.1360 0.1110 -0.0057 -0.0139 0.0009 132 LYS A C 991 O O . LYS A 132 ? 0.1380 0.1433 0.1277 -0.0148 0.0052 -0.0121 132 LYS A O 992 C CB . LYS A 132 ? 0.1593 0.2185 0.1570 0.0317 -0.0536 -0.0459 132 LYS A CB 993 C CG . LYS A 132 ? 0.4077 0.3220 0.2996 0.1224 -0.1931 -0.1954 132 LYS A CG 994 C CD . LYS A 132 ? 0.9315 0.2630 0.2963 0.1569 -0.2647 -0.1308 132 LYS A CD 995 C CE . LYS A 132 ? 0.9897 0.6738 0.4781 0.0007 -0.3262 0.1620 132 LYS A CE 996 N NZ . LYS A 132 ? 1.1779 1.0696 0.5558 -0.3546 -0.6375 0.2467 132 LYS A NZ 997 N N . THR A 133 ? 0.1206 0.1155 0.1094 -0.0130 -0.0225 -0.0038 133 THR A N 998 C CA . THR A 133 ? 0.1078 0.1297 0.0873 -0.0032 -0.0240 -0.0026 133 THR A CA 999 C C . THR A 133 ? 0.1010 0.1187 0.0898 -0.0159 -0.0224 0.0059 133 THR A C 1000 O O . THR A 133 ? 0.1205 0.1522 0.1146 -0.0315 -0.0125 -0.0235 133 THR A O 1001 C CB . THR A 133 ? 0.0953 0.1198 0.1029 -0.0066 -0.0232 0.0040 133 THR A CB 1002 O OG1 . THR A 133 ? 0.1068 0.1209 0.0951 -0.0065 -0.0331 0.0061 133 THR A OG1 1003 C CG2 . THR A 133 ? 0.1086 0.1213 0.1065 -0.0064 -0.0384 0.0159 133 THR A CG2 1004 N N . ILE A 134 ? 0.0907 0.1211 0.1059 -0.0110 -0.0286 0.0027 134 ILE A N 1005 C CA . ILE A 134 ? 0.0903 0.1079 0.0980 -0.0117 -0.0295 0.0027 134 ILE A CA 1006 C C . ILE A 134 ? 0.0845 0.1083 0.0992 -0.0054 -0.0307 0.0058 134 ILE A C 1007 O O . ILE A 134 ? 0.0789 0.1186 0.1010 -0.0072 -0.0277 -0.0082 134 ILE A O 1008 C CB . ILE A 134 ? 0.0908 0.1271 0.1338 -0.0038 -0.0251 0.0307 134 ILE A CB 1009 C CG1 . ILE A 134 ? 0.1223 0.1337 0.1974 -0.0263 -0.0312 0.0414 134 ILE A CG1 1010 C CG2 . ILE A 134 ? 0.1578 0.1709 0.1431 -0.0066 -0.0549 0.0497 134 ILE A CG2 1011 C CD1 . ILE A 134 ? 0.1818 0.1310 0.2958 -0.0104 -0.0066 0.0460 134 ILE A CD1 1012 N N . ALA A 135 ? 0.0852 0.1161 0.1022 -0.0089 -0.0262 -0.0021 135 ALA A N 1013 C CA . ALA A 135 ? 0.0889 0.1067 0.0930 -0.0009 -0.0236 0.0071 135 ALA A CA 1014 C C . ALA A 135 ? 0.0803 0.1162 0.0923 -0.0091 -0.0281 0.0067 135 ALA A C 1015 O O . ALA A 135 ? 0.1113 0.1053 0.1128 -0.0049 -0.0439 0.0029 135 ALA A O 1016 C CB . ALA A 135 ? 0.0956 0.1110 0.1215 -0.0078 -0.0105 0.0123 135 ALA A CB 1017 N N . ALA A 136 ? 0.0857 0.1071 0.0940 -0.0072 -0.0280 0.0071 136 ALA A N 1018 C CA . ALA A 136 ? 0.0777 0.1071 0.0976 -0.0121 -0.0253 0.0066 136 ALA A CA 1019 C C . ALA A 136 ? 0.0824 0.1084 0.0960 -0.0116 -0.0293 0.0081 136 ALA A C 1020 O O . ALA A 136 ? 0.0847 0.1335 0.1136 -0.0159 -0.0109 0.0117 136 ALA A O 1021 C CB . ALA A 136 ? 0.0841 0.1069 0.1162 -0.0116 -0.0305 -0.0002 136 ALA A CB 1022 N N . VAL A 137 ? 0.0808 0.1209 0.0949 -0.0062 -0.0165 0.0017 137 VAL A N 1023 C CA . VAL A 137 ? 0.0836 0.1312 0.0968 0.0063 -0.0213 0.0107 137 VAL A CA 1024 C C . VAL A 137 ? 0.0866 0.1038 0.0957 0.0092 -0.0223 0.0048 137 VAL A C 1025 O O . VAL A 137 ? 0.0802 0.1779 0.0904 0.0099 -0.0187 0.0160 137 VAL A O 1026 C CB . VAL A 137 ? 0.1003 0.1538 0.1155 0.0231 -0.0161 0.0299 137 VAL A CB 1027 C CG1 . VAL A 137 ? 0.1010 0.2281 0.1155 0.0150 -0.0252 0.0419 137 VAL A CG1 1028 C CG2 . VAL A 137 ? 0.1254 0.1410 0.1340 0.0226 -0.0156 0.0398 137 VAL A CG2 1029 N N . ASP A 138 ? 0.0817 0.1095 0.1016 0.0031 -0.0239 0.0042 138 ASP A N 1030 C CA . ASP A 138 ? 0.0827 0.1137 0.0971 0.0098 -0.0145 -0.0013 138 ASP A CA 1031 C C . ASP A 138 ? 0.1110 0.0911 0.1177 0.0224 -0.0278 0.0035 138 ASP A C 1032 O O . ASP A 138 ? 0.1996 0.1001 0.1368 0.0038 -0.0539 0.0136 138 ASP A O 1033 C CB . ASP A 138 ? 0.0868 0.1435 0.1025 0.0096 -0.0168 -0.0111 138 ASP A CB 1034 C CG . ASP A 138 ? 0.0803 0.1095 0.1073 0.0115 -0.0063 0.0008 138 ASP A CG 1035 O OD1 . ASP A 138 ? 0.0951 0.1745 0.1099 -0.0039 -0.0117 -0.0103 138 ASP A OD1 1036 O OD2 . ASP A 138 ? 0.0955 0.1282 0.1070 0.0048 -0.0201 0.0033 138 ASP A OD2 1037 N N . GLY A 139 ? 0.0887 0.0913 0.1169 0.0102 -0.0118 0.0007 139 GLY A N 1038 C CA . GLY A 139 ? 0.1006 0.0958 0.1272 0.0092 -0.0106 -0.0083 139 GLY A CA 1039 C C . GLY A 139 ? 0.1004 0.0883 0.1175 0.0033 -0.0155 0.0009 139 GLY A C 1040 O O . GLY A 139 ? 0.1268 0.0859 0.1570 -0.0013 -0.0162 -0.0113 139 GLY A O 1041 N N . LEU A 140 ? 0.0861 0.0818 0.0993 0.0008 -0.0194 0.0038 140 LEU A N 1042 C CA . LEU A 140 ? 0.0888 0.0869 0.1001 -0.0012 -0.0208 0.0077 140 LEU A CA 1043 C C . LEU A 140 ? 0.0915 0.0789 0.1022 -0.0034 -0.0208 0.0072 140 LEU A C 1044 O O . LEU A 140 ? 0.0891 0.1049 0.1065 -0.0073 -0.0208 0.0240 140 LEU A O 1045 C CB . LEU A 140 ? 0.0816 0.0910 0.0960 0.0007 -0.0166 0.0043 140 LEU A CB 1046 C CG . LEU A 140 ? 0.0893 0.1256 0.0948 0.0033 -0.0258 0.0079 140 LEU A CG 1047 C CD1 . LEU A 140 ? 0.0967 0.1680 0.1167 0.0101 -0.0380 -0.0222 140 LEU A CD1 1048 C CD2 . LEU A 140 ? 0.1923 0.1340 0.1371 -0.0057 -0.0717 0.0450 140 LEU A CD2 1049 N N . ILE A 141 ? 0.0791 0.0884 0.0911 0.0004 -0.0196 0.0055 141 ILE A N 1050 C CA . ILE A 141 ? 0.0839 0.0845 0.0933 0.0001 -0.0193 0.0028 141 ILE A CA 1051 C C . ILE A 141 ? 0.0844 0.0857 0.0929 -0.0050 -0.0202 0.0020 141 ILE A C 1052 O O . ILE A 141 ? 0.0908 0.0962 0.0920 0.0005 -0.0151 -0.0068 141 ILE A O 1053 C CB . ILE A 141 ? 0.0960 0.0839 0.0929 0.0025 -0.0176 0.0021 141 ILE A CB 1054 C CG1 . ILE A 141 ? 0.0992 0.0817 0.1054 -0.0029 -0.0153 -0.0024 141 ILE A CG1 1055 C CG2 . ILE A 141 ? 0.1367 0.0833 0.1134 0.0046 -0.0379 0.0080 141 ILE A CG2 1056 C CD1 . ILE A 141 ? 0.0986 0.1156 0.1322 -0.0036 0.0029 -0.0263 141 ILE A CD1 1057 N N . PRO A 142 ? 0.0919 0.0997 0.0941 -0.0001 -0.0142 -0.0077 142 PRO A N 1058 C CA . PRO A 142 ? 0.1017 0.0968 0.1077 -0.0008 -0.0220 -0.0145 142 PRO A CA 1059 C C . PRO A 142 ? 0.1037 0.1083 0.0956 0.0126 -0.0283 -0.0084 142 PRO A C 1060 O O . PRO A 142 ? 0.1403 0.0995 0.1056 0.0204 -0.0312 -0.0051 142 PRO A O 1061 C CB . PRO A 142 ? 0.1043 0.1320 0.1458 -0.0213 -0.0355 -0.0193 142 PRO A CB 1062 C CG . PRO A 142 ? 0.1047 0.1432 0.1549 -0.0199 -0.0118 -0.0256 142 PRO A CG 1063 C CD . PRO A 142 ? 0.0904 0.1121 0.1154 -0.0019 -0.0043 -0.0096 142 PRO A CD 1064 N N . GLU A 143 ? 0.1165 0.0921 0.0971 0.0031 -0.0329 -0.0074 143 GLU A N 1065 C CA . GLU A 143 ? 0.1077 0.0917 0.1001 0.0032 -0.0261 -0.0113 143 GLU A CA 1066 C C . GLU A 143 ? 0.0893 0.0881 0.0998 0.0121 -0.0201 -0.0034 143 GLU A C 1067 O O . GLU A 143 ? 0.0964 0.0886 0.0993 0.0023 -0.0172 -0.0076 143 GLU A O 1068 C CB . GLU A 143 ? 0.1120 0.1174 0.1170 -0.0035 -0.0343 -0.0119 143 GLU A CB 1069 C CG . GLU A 143 ? 0.1336 0.1270 0.1292 -0.0117 -0.0528 -0.0114 143 GLU A CG 1070 C CD . GLU A 143 ? 0.1350 0.1886 0.2300 -0.0254 -0.0509 -0.0616 143 GLU A CD 1071 O OE1 . GLU A 143 ? 0.1750 0.2268 0.4211 0.0467 -0.1350 -0.0868 143 GLU A OE1 1072 O OE2 . GLU A 143 ? 0.2591 0.2451 0.4130 -0.0793 0.0898 -0.0074 143 GLU A OE2 1073 N N . PRO A 144 ? 0.0932 0.0873 0.1020 -0.0003 -0.0185 -0.0053 144 PRO A N 1074 C CA . PRO A 144 ? 0.0839 0.0953 0.0904 -0.0020 -0.0129 -0.0061 144 PRO A CA 1075 C C . PRO A 144 ? 0.0852 0.0991 0.0926 -0.0016 -0.0170 -0.0004 144 PRO A C 1076 O O . PRO A 144 ? 0.0969 0.0997 0.1057 0.0006 -0.0157 -0.0136 144 PRO A O 1077 C CB . PRO A 144 ? 0.1054 0.0953 0.1013 0.0025 -0.0232 0.0038 144 PRO A CB 1078 C CG . PRO A 144 ? 0.1115 0.0958 0.1093 0.0072 -0.0068 -0.0030 144 PRO A CG 1079 C CD . PRO A 144 ? 0.1035 0.0842 0.1148 0.0002 -0.0205 0.0032 144 PRO A CD 1080 N N . GLN A 145 ? 0.0916 0.0954 0.0941 0.0030 -0.0079 -0.0064 145 GLN A N 1081 C CA . GLN A 145 ? 0.1000 0.1099 0.1048 0.0082 0.0009 -0.0037 145 GLN A CA 1082 C C . GLN A 145 ? 0.1016 0.0919 0.1119 0.0023 -0.0085 -0.0127 145 GLN A C 1083 O O . GLN A 145 ? 0.1338 0.1052 0.1253 0.0132 0.0073 -0.0107 145 GLN A O 1084 C CB . GLN A 145 ? 0.0967 0.1301 0.1318 0.0085 0.0092 0.0023 145 GLN A CB 1085 C CG . GLN A 145 ? 0.0794 0.1619 0.1640 0.0040 0.0006 0.0190 145 GLN A CG 1086 C CD . GLN A 145 ? 0.1015 0.1706 0.1350 -0.0186 -0.0098 0.0028 145 GLN A CD 1087 O OE1 . GLN A 145 ? 0.1138 0.1353 0.1468 -0.0169 -0.0090 -0.0149 145 GLN A OE1 1088 N NE2 . GLN A 145 ? 0.1180 0.2544 0.2169 -0.0212 -0.0475 -0.0265 145 GLN A NE2 1089 N N . ASP A 146 ? 0.1094 0.0920 0.1009 0.0046 -0.0096 -0.0025 146 ASP A N 1090 C CA . ASP A 146 ? 0.1066 0.0934 0.1094 0.0033 -0.0118 -0.0056 146 ASP A CA 1091 C C . ASP A 146 ? 0.1180 0.0862 0.1020 0.0080 -0.0080 -0.0040 146 ASP A C 1092 O O . ASP A 146 ? 0.1077 0.0946 0.1463 -0.0007 -0.0208 -0.0093 146 ASP A O 1093 C CB . ASP A 146 ? 0.1165 0.0968 0.1038 -0.0058 -0.0026 -0.0086 146 ASP A CB 1094 C CG . ASP A 146 ? 0.1317 0.0940 0.1422 0.0024 -0.0283 -0.0101 146 ASP A CG 1095 O OD1 . ASP A 146 ? 0.1578 0.1003 0.1201 0.0132 -0.0251 -0.0054 146 ASP A OD1 1096 O OD2 . ASP A 146 ? 0.1329 0.1369 0.1531 -0.0181 -0.0142 -0.0222 146 ASP A OD2 1097 N N . SER A 147 ? 0.1158 0.0920 0.1138 -0.0028 -0.0082 -0.0152 147 SER A N 1098 C CA . SER A 147 ? 0.1297 0.0904 0.1034 -0.0083 -0.0097 -0.0114 147 SER A CA 1099 C C . SER A 147 ? 0.1100 0.0791 0.1052 -0.0010 -0.0148 -0.0042 147 SER A C 1100 O O . SER A 147 ? 0.1183 0.0816 0.1039 0.0009 -0.0171 -0.0090 147 SER A O 1101 C CB . SER A 147 ? 0.1278 0.0898 0.1383 -0.0034 -0.0076 -0.0195 147 SER A CB 1102 O OG . SER A 147 ? 0.1317 0.1034 0.1318 0.0125 -0.0036 -0.0045 147 SER A OG 1103 N N . VAL A 148 ? 0.1167 0.0737 0.0988 0.0029 -0.0173 -0.0085 148 VAL A N 1104 C CA . VAL A 148 ? 0.1107 0.0671 0.1001 0.0038 -0.0213 -0.0071 148 VAL A CA 1105 C C . VAL A 148 ? 0.1123 0.0606 0.1059 0.0047 -0.0269 0.0020 148 VAL A C 1106 O O . VAL A 148 ? 0.1087 0.0756 0.1009 0.0068 -0.0275 -0.0006 148 VAL A O 1107 C CB . VAL A 148 ? 0.1227 0.0684 0.1032 0.0020 -0.0274 -0.0077 148 VAL A CB 1108 C CG1 . VAL A 148 ? 0.1139 0.0768 0.1088 -0.0046 -0.0239 -0.0009 148 VAL A CG1 1109 C CG2 . VAL A 148 ? 0.1309 0.0894 0.1075 0.0008 -0.0429 0.0038 148 VAL A CG2 1110 N N . THR A 149 ? 0.1063 0.0722 0.0995 0.0065 -0.0224 -0.0007 149 THR A N 1111 C CA . THR A 149 ? 0.1042 0.0704 0.1142 0.0076 -0.0284 0.0011 149 THR A CA 1112 C C . THR A 149 ? 0.1016 0.0621 0.1141 0.0096 -0.0245 0.0055 149 THR A C 1113 O O . THR A 149 ? 0.1152 0.0753 0.1049 0.0056 -0.0263 0.0058 149 THR A O 1114 C CB . THR A 149 ? 0.1083 0.0723 0.1292 0.0124 -0.0236 -0.0051 149 THR A CB 1115 O OG1 . THR A 149 ? 0.1178 0.0725 0.1349 0.0072 -0.0227 -0.0033 149 THR A OG1 1116 C CG2 . THR A 149 ? 0.1506 0.0800 0.1505 0.0274 -0.0536 -0.0043 149 THR A CG2 1117 N N . LYS A 150 ? 0.1023 0.0741 0.1093 0.0061 -0.0167 -0.0061 150 LYS A N 1118 C CA . LYS A 150 ? 0.0961 0.0769 0.1121 0.0024 -0.0241 -0.0008 150 LYS A CA 1119 C C . LYS A 150 ? 0.0998 0.0706 0.1046 0.0009 -0.0194 0.0023 150 LYS A C 1120 O O . LYS A 150 ? 0.1071 0.0828 0.1069 0.0004 -0.0323 -0.0053 150 LYS A O 1121 C CB . LYS A 150 ? 0.0946 0.0868 0.1305 0.0078 -0.0181 -0.0011 150 LYS A CB 1122 C CG . LYS A 150 ? 0.1130 0.1068 0.1402 -0.0081 -0.0231 -0.0072 150 LYS A CG 1123 C CD . LYS A 150 ? 0.1022 0.1436 0.1830 -0.0180 -0.0222 0.0095 150 LYS A CD 1124 C CE . LYS A 150 ? 0.1455 0.1836 0.1661 -0.0443 -0.0128 -0.0041 150 LYS A CE 1125 N NZ A LYS A 150 ? 0.1567 0.2796 0.3429 -0.1128 0.0367 -0.0819 150 LYS A NZ 1126 N NZ B LYS A 150 ? 0.1433 0.1860 0.2203 -0.0315 -0.0563 0.0020 150 LYS A NZ 1127 N N . ILE A 151 ? 0.1065 0.0689 0.1030 0.0067 -0.0250 -0.0003 151 ILE A N 1128 C CA . ILE A 151 ? 0.1015 0.0676 0.1016 0.0044 -0.0186 -0.0025 151 ILE A CA 1129 C C . ILE A 151 ? 0.0988 0.0704 0.0911 0.0054 -0.0265 0.0054 151 ILE A C 1130 O O . ILE A 151 ? 0.1078 0.0725 0.0958 0.0008 -0.0252 -0.0013 151 ILE A O 1131 C CB . ILE A 151 ? 0.1236 0.0854 0.0953 0.0164 -0.0151 0.0102 151 ILE A CB 1132 C CG1 . ILE A 151 ? 0.1591 0.0931 0.1059 0.0206 -0.0044 0.0172 151 ILE A CG1 1133 C CG2 . ILE A 151 ? 0.1447 0.1251 0.1040 0.0518 -0.0214 0.0212 151 ILE A CG2 1134 C CD1 . ILE A 151 ? 0.1776 0.1545 0.1012 0.0596 0.0054 0.0343 151 ILE A CD1 1135 N N . LEU A 152 ? 0.1040 0.0737 0.0922 -0.0022 -0.0168 -0.0010 152 LEU A N 1136 C CA . LEU A 152 ? 0.1000 0.0852 0.0981 -0.0071 -0.0240 0.0059 152 LEU A CA 1137 C C . LEU A 152 ? 0.1120 0.0722 0.0954 -0.0052 -0.0234 0.0025 152 LEU A C 1138 O O . LEU A 152 ? 0.1106 0.0962 0.0928 -0.0144 -0.0190 0.0057 152 LEU A O 1139 C CB . LEU A 152 ? 0.1030 0.0775 0.1055 -0.0050 -0.0265 0.0025 152 LEU A CB 1140 C CG . LEU A 152 ? 0.1104 0.0814 0.1129 -0.0016 -0.0367 -0.0042 152 LEU A CG 1141 C CD1 . LEU A 152 ? 0.1199 0.0914 0.1319 -0.0087 -0.0357 -0.0093 152 LEU A CD1 1142 C CD2 . LEU A 152 ? 0.1251 0.0924 0.1442 0.0088 -0.0498 -0.0100 152 LEU A CD2 1143 N N . GLN A 153 ? 0.1188 0.0728 0.1021 -0.0008 -0.0356 0.0064 153 GLN A N 1144 C CA . GLN A 153 ? 0.1308 0.0804 0.1026 0.0013 -0.0368 0.0067 153 GLN A CA 1145 C C . GLN A 153 ? 0.1002 0.0805 0.1069 0.0029 -0.0295 0.0028 153 GLN A C 1146 O O . GLN A 153 ? 0.1220 0.0878 0.0970 -0.0048 -0.0267 0.0090 153 GLN A O 1147 C CB . GLN A 153 ? 0.1427 0.0859 0.1428 0.0218 -0.0460 0.0011 153 GLN A CB 1148 C CG . GLN A 153 ? 0.2166 0.1494 0.1982 0.0733 -0.0981 -0.0227 153 GLN A CG 1149 C CD . GLN A 153 ? 0.2850 0.1468 0.1851 0.0328 -0.0906 -0.0056 153 GLN A CD 1150 O OE1 . GLN A 153 ? 0.2656 0.1678 0.2451 0.0298 -0.0868 0.0186 153 GLN A OE1 1151 N NE2 . GLN A 153 ? 0.4700 0.1778 0.2026 0.0706 -0.1610 0.0098 153 GLN A NE2 1152 N N . ARG A 154 ? 0.1026 0.0775 0.0956 0.0006 -0.0214 0.0033 154 ARG A N 1153 C CA . ARG A 154 ? 0.1043 0.0734 0.0863 -0.0017 -0.0246 0.0029 154 ARG A CA 1154 C C . ARG A 154 ? 0.0914 0.0771 0.0993 -0.0063 -0.0171 0.0156 154 ARG A C 1155 O O . ARG A 154 ? 0.1077 0.0845 0.0906 -0.0062 -0.0225 0.0033 154 ARG A O 1156 C CB . ARG A 154 ? 0.0983 0.0817 0.0940 -0.0051 -0.0145 -0.0019 154 ARG A CB 1157 C CG . ARG A 154 ? 0.1131 0.0801 0.0975 -0.0056 -0.0116 0.0028 154 ARG A CG 1158 C CD . ARG A 154 ? 0.1101 0.1001 0.0983 -0.0163 -0.0130 -0.0065 154 ARG A CD 1159 N NE . ARG A 154 ? 0.1024 0.0855 0.1060 0.0012 -0.0262 -0.0040 154 ARG A NE 1160 C CZ . ARG A 154 ? 0.0940 0.0815 0.1004 -0.0049 -0.0205 0.0004 154 ARG A CZ 1161 N NH1 . ARG A 154 ? 0.1020 0.0780 0.0949 -0.0099 -0.0173 0.0044 154 ARG A NH1 1162 N NH2 . ARG A 154 ? 0.1132 0.0844 0.0996 0.0039 -0.0231 0.0023 154 ARG A NH2 1163 N N . PHE A 155 ? 0.0986 0.0819 0.0915 -0.0074 -0.0237 0.0075 155 PHE A N 1164 C CA . PHE A 155 ? 0.0898 0.0825 0.0955 -0.0033 -0.0218 0.0098 155 PHE A CA 1165 C C . PHE A 155 ? 0.1042 0.0901 0.0868 -0.0107 -0.0282 0.0032 155 PHE A C 1166 O O . PHE A 155 ? 0.1136 0.1012 0.0979 0.0008 -0.0226 0.0042 155 PHE A O 1167 C CB . PHE A 155 ? 0.0971 0.0961 0.0964 -0.0068 -0.0192 0.0107 155 PHE A CB 1168 C CG . PHE A 155 ? 0.0935 0.0798 0.0972 -0.0055 -0.0272 0.0060 155 PHE A CG 1169 C CD1 . PHE A 155 ? 0.1035 0.0946 0.1282 0.0042 -0.0026 -0.0034 155 PHE A CD1 1170 C CD2 . PHE A 155 ? 0.1043 0.0736 0.1058 0.0064 -0.0191 0.0063 155 PHE A CD2 1171 C CE1 . PHE A 155 ? 0.1081 0.0796 0.1536 0.0132 -0.0117 -0.0023 155 PHE A CE1 1172 C CE2 . PHE A 155 ? 0.1116 0.0757 0.1083 0.0011 -0.0221 0.0085 155 PHE A CE2 1173 C CZ . PHE A 155 ? 0.1168 0.0754 0.1299 0.0114 -0.0310 0.0093 155 PHE A CZ 1174 N N . GLU A 156 ? 0.1110 0.0882 0.0928 -0.0155 -0.0202 0.0112 156 GLU A N 1175 C CA . GLU A 156 ? 0.1215 0.0949 0.0943 -0.0107 -0.0130 0.0064 156 GLU A CA 1176 C C . GLU A 156 ? 0.1228 0.0801 0.1038 0.0026 -0.0198 0.0133 156 GLU A C 1177 O O . GLU A 156 ? 0.1434 0.1055 0.0930 -0.0058 -0.0141 0.0152 156 GLU A O 1178 C CB . GLU A 156 ? 0.2045 0.0903 0.1094 -0.0412 -0.0218 0.0096 156 GLU A CB 1179 C CG . GLU A 156 ? 0.4349 0.1207 0.1333 -0.1149 0.0216 0.0103 156 GLU A CG 1180 C CD . GLU A 156 ? 0.8148 0.1097 0.1652 -0.0678 -0.0658 0.0265 156 GLU A CD 1181 O OE1 . GLU A 156 ? 1.0027 0.1674 0.3063 -0.1391 -0.0191 0.0844 156 GLU A OE1 1182 O OE2 . GLU A 156 ? 1.1529 0.1302 0.1960 0.0228 -0.0489 -0.0209 156 GLU A OE2 1183 N N . ASP A 157 ? 0.1287 0.0872 0.0950 -0.0015 -0.0199 0.0088 157 ASP A N 1184 C CA . ASP A 157 ? 0.1334 0.0902 0.0999 -0.0041 -0.0315 0.0085 157 ASP A CA 1185 C C . ASP A 157 ? 0.1157 0.0958 0.0991 -0.0053 -0.0343 0.0075 157 ASP A C 1186 O O . ASP A 157 ? 0.1356 0.1040 0.1046 -0.0022 -0.0371 0.0036 157 ASP A O 1187 C CB . ASP A 157 ? 0.1308 0.0902 0.1240 0.0088 -0.0381 0.0052 157 ASP A CB 1188 C CG . ASP A 157 ? 0.1406 0.0860 0.1429 0.0075 -0.0466 0.0159 157 ASP A CG 1189 O OD1 . ASP A 157 ? 0.1555 0.0961 0.1487 -0.0075 -0.0565 0.0082 157 ASP A OD1 1190 O OD2 . ASP A 157 ? 0.1659 0.1148 0.1515 -0.0084 -0.0712 0.0368 157 ASP A OD2 1191 N N . ALA A 158 ? 0.1133 0.0843 0.0930 -0.0078 -0.0218 0.0096 158 ALA A N 1192 C CA . ALA A 158 ? 0.1065 0.0835 0.0987 -0.0119 -0.0238 0.0084 158 ALA A CA 1193 C C . ALA A 158 ? 0.1203 0.0916 0.0985 -0.0144 -0.0103 0.0074 158 ALA A C 1194 O O . ALA A 158 ? 0.1494 0.1156 0.1028 -0.0395 -0.0067 -0.0123 158 ALA A O 1195 C CB . ALA A 158 ? 0.1178 0.0919 0.1054 -0.0006 -0.0245 0.0125 158 ALA A CB 1196 N N . GLY A 159 ? 0.1177 0.1158 0.1304 -0.0230 0.0036 -0.0231 159 GLY A N 1197 C CA . GLY A 159 ? 0.1370 0.1685 0.2132 -0.0610 0.0462 -0.0683 159 GLY A CA 1198 C C . GLY A 159 ? 0.1326 0.1300 0.1109 -0.0404 0.0041 -0.0128 159 GLY A C 1199 O O . GLY A 159 ? 0.1265 0.1449 0.1395 -0.0319 0.0141 -0.0157 159 GLY A O 1200 N N . GLY A 160 ? 0.1244 0.1190 0.1097 -0.0300 -0.0109 0.0081 160 GLY A N 1201 C CA . GLY A 160 ? 0.1404 0.1071 0.1123 -0.0275 -0.0224 0.0148 160 GLY A CA 1202 C C . GLY A 160 ? 0.1321 0.1007 0.1061 -0.0277 -0.0218 0.0166 160 GLY A C 1203 O O . GLY A 160 ? 0.1496 0.1906 0.1249 -0.0641 -0.0283 0.0433 160 GLY A O 1204 N N . PHE A 161 ? 0.1151 0.0944 0.0980 -0.0114 -0.0175 0.0090 161 PHE A N 1205 C CA . PHE A 161 ? 0.1283 0.0945 0.1009 -0.0064 -0.0266 0.0103 161 PHE A CA 1206 C C . PHE A 161 ? 0.1253 0.1022 0.1022 -0.0059 -0.0321 0.0132 161 PHE A C 1207 O O . PHE A 161 ? 0.1252 0.1057 0.1320 -0.0066 -0.0221 -0.0088 161 PHE A O 1208 C CB . PHE A 161 ? 0.1275 0.1030 0.0924 -0.0022 -0.0103 0.0089 161 PHE A CB 1209 C CG . PHE A 161 ? 0.1280 0.0924 0.0940 0.0039 -0.0112 0.0095 161 PHE A CG 1210 C CD1 . PHE A 161 ? 0.1241 0.1048 0.1458 -0.0106 0.0144 -0.0082 161 PHE A CD1 1211 C CD2 . PHE A 161 ? 0.1413 0.1379 0.1246 0.0273 -0.0322 -0.0121 161 PHE A CD2 1212 C CE1 . PHE A 161 ? 0.1647 0.1012 0.2386 -0.0325 0.0342 -0.0357 161 PHE A CE1 1213 C CE2 . PHE A 161 ? 0.1899 0.1246 0.1479 0.0413 0.0011 0.0014 161 PHE A CE2 1214 C CZ . PHE A 161 ? 0.2050 0.0999 0.1706 0.0013 0.0146 -0.0112 161 PHE A CZ 1215 N N . THR A 162 ? 0.1289 0.0968 0.1082 -0.0106 -0.0289 0.0136 162 THR A N 1216 C CA . THR A 162 ? 0.1431 0.0843 0.1085 -0.0064 -0.0330 0.0179 162 THR A CA 1217 C C . THR A 162 ? 0.1274 0.0759 0.1108 -0.0018 -0.0406 0.0166 162 THR A C 1218 O O . THR A 162 ? 0.1221 0.0754 0.1036 -0.0085 -0.0298 0.0143 162 THR A O 1219 C CB . THR A 162 ? 0.1499 0.1180 0.1265 -0.0289 -0.0436 0.0444 162 THR A CB 1220 O OG1 . THR A 162 ? 0.1318 0.1269 0.1291 -0.0194 -0.0168 0.0284 162 THR A OG1 1221 C CG2 . THR A 162 ? 0.2060 0.1809 0.1361 -0.0478 -0.0218 0.0622 162 THR A CG2 1222 N N . PRO A 163 ? 0.1199 0.0764 0.1158 0.0013 -0.0308 0.0175 163 PRO A N 1223 C CA . PRO A 163 ? 0.1245 0.0800 0.1103 0.0043 -0.0332 0.0118 163 PRO A CA 1224 C C . PRO A 163 ? 0.1027 0.0775 0.0994 -0.0038 -0.0268 -0.0003 163 PRO A C 1225 O O . PRO A 163 ? 0.1063 0.0833 0.1073 0.0012 -0.0243 0.0162 163 PRO A O 1226 C CB . PRO A 163 ? 0.1679 0.0870 0.1296 0.0161 -0.0443 0.0025 163 PRO A CB 1227 C CG . PRO A 163 ? 0.1741 0.0831 0.1547 0.0249 -0.0420 0.0040 163 PRO A CG 1228 C CD . PRO A 163 ? 0.1532 0.0787 0.1349 0.0057 -0.0476 0.0126 163 PRO A CD 1229 N N . PHE A 164 ? 0.1103 0.0797 0.1125 -0.0085 -0.0273 0.0175 164 PHE A N 1230 C CA . PHE A 164 ? 0.0987 0.0867 0.0988 -0.0130 -0.0175 0.0101 164 PHE A CA 1231 C C . PHE A 164 ? 0.0921 0.0849 0.0990 -0.0080 -0.0124 0.0107 164 PHE A C 1232 O O . PHE A 164 ? 0.0900 0.0853 0.1022 -0.0020 -0.0195 0.0210 164 PHE A O 1233 C CB . PHE A 164 ? 0.1128 0.0894 0.1138 -0.0182 -0.0139 0.0196 164 PHE A CB 1234 C CG . PHE A 164 ? 0.0981 0.0979 0.1083 -0.0276 -0.0121 0.0178 164 PHE A CG 1235 C CD1 . PHE A 164 ? 0.1214 0.1276 0.1093 -0.0054 -0.0211 0.0044 164 PHE A CD1 1236 C CD2 . PHE A 164 ? 0.1077 0.1113 0.1240 -0.0230 -0.0145 -0.0021 164 PHE A CD2 1237 C CE1 . PHE A 164 ? 0.1017 0.1564 0.1228 -0.0068 -0.0157 0.0112 164 PHE A CE1 1238 C CE2 . PHE A 164 ? 0.1054 0.1202 0.1454 -0.0171 0.0032 0.0069 164 PHE A CE2 1239 C CZ . PHE A 164 ? 0.1110 0.1141 0.1454 -0.0149 -0.0091 0.0162 164 PHE A CZ 1240 N N . GLU A 165 ? 0.0993 0.0815 0.0952 -0.0073 -0.0237 0.0174 165 GLU A N 1241 C CA . GLU A 165 ? 0.0970 0.0867 0.0903 -0.0047 -0.0174 0.0116 165 GLU A CA 1242 C C . GLU A 165 ? 0.0870 0.0858 0.0884 -0.0085 -0.0171 0.0034 165 GLU A C 1243 O O . GLU A 165 ? 0.1028 0.0733 0.0947 -0.0029 -0.0154 0.0142 165 GLU A O 1244 C CB . GLU A 165 ? 0.1051 0.0914 0.0942 -0.0062 -0.0131 0.0030 165 GLU A CB 1245 C CG . GLU A 165 ? 0.1189 0.1189 0.0972 -0.0015 -0.0078 0.0161 165 GLU A CG 1246 C CD . GLU A 165 ? 0.1269 0.1338 0.0967 0.0022 -0.0082 0.0149 165 GLU A CD 1247 O OE1 . GLU A 165 ? 0.1909 0.2574 0.1052 0.0655 0.0000 0.0159 165 GLU A OE1 1248 O OE2 . GLU A 165 ? 0.1339 0.1748 0.1066 0.0061 -0.0154 0.0238 165 GLU A OE2 1249 N N . VAL A 166 ? 0.0998 0.0757 0.0909 -0.0086 -0.0187 0.0122 166 VAL A N 1250 C CA . VAL A 166 ? 0.0865 0.0721 0.0989 -0.0057 -0.0213 0.0050 166 VAL A CA 1251 C C . VAL A 166 ? 0.0774 0.0739 0.0927 0.0046 -0.0140 0.0018 166 VAL A C 1252 O O . VAL A 166 ? 0.0833 0.0837 0.1016 -0.0038 -0.0109 0.0099 166 VAL A O 1253 C CB . VAL A 166 ? 0.0888 0.0881 0.1069 -0.0015 -0.0297 0.0126 166 VAL A CB 1254 C CG1 . VAL A 166 ? 0.0893 0.1116 0.1336 0.0140 -0.0118 0.0158 166 VAL A CG1 1255 C CG2 . VAL A 166 ? 0.0932 0.0957 0.1263 0.0051 -0.0381 0.0112 166 VAL A CG2 1256 N N . VAL A 167 ? 0.0873 0.0766 0.0932 -0.0032 -0.0195 0.0114 167 VAL A N 1257 C CA . VAL A 167 ? 0.0851 0.0819 0.0821 -0.0064 -0.0121 0.0145 167 VAL A CA 1258 C C . VAL A 167 ? 0.0753 0.0762 0.0850 -0.0029 -0.0146 0.0053 167 VAL A C 1259 O O . VAL A 167 ? 0.0899 0.0815 0.0896 -0.0039 -0.0120 0.0140 167 VAL A O 1260 C CB . VAL A 167 ? 0.1017 0.0819 0.0857 0.0034 -0.0133 0.0049 167 VAL A CB 1261 C CG1 . VAL A 167 ? 0.1270 0.0971 0.0890 0.0031 -0.0299 -0.0033 167 VAL A CG1 1262 C CG2 . VAL A 167 ? 0.1396 0.0924 0.1128 0.0244 -0.0179 -0.0048 167 VAL A CG2 1263 N N . SER A 168 ? 0.0847 0.0707 0.0817 -0.0067 -0.0104 0.0089 168 SER A N 1264 C CA . SER A 168 ? 0.0723 0.0760 0.0860 -0.0055 -0.0129 0.0133 168 SER A CA 1265 C C . SER A 168 ? 0.0739 0.0767 0.0801 -0.0070 -0.0095 0.0058 168 SER A C 1266 O O . SER A 168 ? 0.0839 0.0740 0.0977 -0.0018 -0.0161 0.0123 168 SER A O 1267 C CB . SER A 168 ? 0.0833 0.0839 0.0928 -0.0145 -0.0059 0.0039 168 SER A CB 1268 O OG . SER A 168 ? 0.0864 0.0869 0.1000 -0.0191 -0.0001 0.0153 168 SER A OG 1269 N N . LEU A 169 ? 0.0842 0.0733 0.0848 -0.0109 -0.0117 0.0142 169 LEU A N 1270 C CA . LEU A 169 ? 0.0783 0.0747 0.0854 -0.0111 -0.0085 0.0081 169 LEU A CA 1271 C C . LEU A 169 ? 0.0820 0.0735 0.0827 -0.0065 -0.0126 0.0060 169 LEU A C 1272 O O . LEU A 169 ? 0.1165 0.0771 0.0886 -0.0162 -0.0152 0.0104 169 LEU A O 1273 C CB . LEU A 169 ? 0.0845 0.0824 0.0907 -0.0126 -0.0125 0.0081 169 LEU A CB 1274 C CG . LEU A 169 ? 0.0899 0.0921 0.0850 -0.0062 -0.0134 0.0035 169 LEU A CG 1275 C CD1 . LEU A 169 ? 0.1334 0.1098 0.1123 0.0113 -0.0421 0.0072 169 LEU A CD1 1276 C CD2 . LEU A 169 ? 0.1192 0.0924 0.1052 -0.0022 -0.0052 -0.0045 169 LEU A CD2 1277 N N . LEU A 170 ? 0.0883 0.0778 0.0909 -0.0102 -0.0004 0.0168 170 LEU A N 1278 C CA . LEU A 170 ? 0.0979 0.0860 0.0874 -0.0146 0.0000 0.0078 170 LEU A CA 1279 C C . LEU A 170 ? 0.1047 0.0812 0.0823 -0.0131 -0.0075 0.0064 170 LEU A C 1280 O O . LEU A 170 ? 0.1168 0.0827 0.0870 -0.0156 -0.0047 0.0026 170 LEU A O 1281 C CB . LEU A 170 ? 0.1069 0.0828 0.1061 -0.0142 0.0041 0.0017 170 LEU A CB 1282 C CG . LEU A 170 ? 0.1302 0.0888 0.1237 -0.0019 -0.0116 0.0213 170 LEU A CG 1283 C CD1 . LEU A 170 ? 0.1511 0.0973 0.1865 0.0191 0.0130 0.0093 170 LEU A CD1 1284 C CD2 . LEU A 170 ? 0.1057 0.0963 0.1782 -0.0074 0.0032 -0.0080 170 LEU A CD2 1285 N N . ALA A 171 ? 0.0923 0.0879 0.0837 -0.0159 -0.0146 0.0072 171 ALA A N 1286 C CA . ALA A 171 ? 0.0900 0.1010 0.0812 -0.0184 -0.0174 0.0127 171 ALA A CA 1287 C C . ALA A 171 ? 0.0695 0.0971 0.0762 -0.0069 -0.0099 0.0076 171 ALA A C 1288 O O . ALA A 171 ? 0.0778 0.1030 0.0785 -0.0033 -0.0117 0.0147 171 ALA A O 1289 C CB . ALA A 171 ? 0.0854 0.1132 0.0943 -0.0119 -0.0176 0.0220 171 ALA A CB 1290 N N . SER A 172 ? 0.0864 0.0829 0.0765 -0.0100 -0.0157 0.0101 172 SER A N 1291 C CA . SER A 172 ? 0.0938 0.0786 0.0724 -0.0084 -0.0142 0.0021 172 SER A CA 1292 C C . SER A 172 ? 0.0684 0.0803 0.0766 -0.0005 -0.0188 0.0073 172 SER A C 1293 O O . SER A 172 ? 0.0874 0.0690 0.0861 -0.0043 -0.0139 0.0078 172 SER A O 1294 C CB . SER A 172 ? 0.1228 0.0929 0.0795 -0.0261 -0.0238 0.0010 172 SER A CB 1295 O OG . SER A 172 ? 0.1163 0.1365 0.1211 -0.0134 -0.0326 0.0291 172 SER A OG 1296 N N . HIS A 173 ? 0.0759 0.0696 0.0722 -0.0056 -0.0144 0.0058 173 HIS A N 1297 C CA . HIS A 173 ? 0.0786 0.0668 0.0738 -0.0015 -0.0085 0.0105 173 HIS A CA 1298 C C . HIS A 173 ? 0.0807 0.0744 0.0678 0.0004 -0.0113 0.0082 173 HIS A C 1299 O O . HIS A 173 ? 0.0842 0.1032 0.0798 0.0117 -0.0043 0.0186 173 HIS A O 1300 C CB . HIS A 173 ? 0.0757 0.0738 0.0811 -0.0029 -0.0095 0.0034 173 HIS A CB 1301 C CG . HIS A 173 ? 0.0885 0.0689 0.0723 0.0083 -0.0105 0.0064 173 HIS A CG 1302 N ND1 . HIS A 173 ? 0.0809 0.0825 0.0803 0.0081 -0.0126 0.0054 173 HIS A ND1 1303 C CD2 . HIS A 173 ? 0.0834 0.0763 0.0843 -0.0012 -0.0124 0.0150 173 HIS A CD2 1304 C CE1 . HIS A 173 ? 0.0912 0.0877 0.0729 0.0035 -0.0173 0.0064 173 HIS A CE1 1305 N NE2 . HIS A 173 ? 0.0877 0.0783 0.0725 0.0062 -0.0101 0.0091 173 HIS A NE2 1306 N N . SER A 174 ? 0.0770 0.0758 0.0747 -0.0033 -0.0141 0.0094 174 SER A N 1307 C CA . SER A 174 ? 0.0741 0.0731 0.0733 0.0011 -0.0191 0.0088 174 SER A CA 1308 C C . SER A 174 ? 0.0773 0.0774 0.0677 -0.0011 -0.0076 0.0026 174 SER A C 1309 O O . SER A 174 ? 0.0871 0.0800 0.0806 0.0011 -0.0261 0.0104 174 SER A O 1310 C CB . SER A 174 ? 0.0747 0.0844 0.0812 -0.0027 -0.0128 0.0081 174 SER A CB 1311 O OG . SER A 174 ? 0.0786 0.0869 0.0777 0.0009 -0.0193 0.0147 174 SER A OG 1312 N N . VAL A 175 ? 0.0727 0.0717 0.0733 0.0012 -0.0116 0.0022 175 VAL A N 1313 C CA . VAL A 175 ? 0.0890 0.0768 0.0776 0.0005 -0.0152 0.0045 175 VAL A CA 1314 C C . VAL A 175 ? 0.0839 0.0676 0.0942 -0.0015 -0.0229 0.0022 175 VAL A C 1315 O O . VAL A 175 ? 0.1034 0.1099 0.1194 -0.0010 -0.0152 -0.0270 175 VAL A O 1316 C CB . VAL A 175 ? 0.0968 0.0785 0.0895 0.0070 -0.0179 -0.0061 175 VAL A CB 1317 C CG1 . VAL A 175 ? 0.0876 0.0979 0.0998 0.0051 -0.0170 0.0014 175 VAL A CG1 1318 C CG2 . VAL A 175 ? 0.1116 0.1313 0.0792 0.0122 -0.0156 -0.0018 175 VAL A CG2 1319 N N . ALA A 176 ? 0.0830 0.1267 0.0810 -0.0161 -0.0087 -0.0199 176 ALA A N 1320 C CA . ALA A 176 ? 0.0864 0.0893 0.0695 -0.0119 -0.0079 0.0011 176 ALA A CA 1321 C C . ALA A 176 ? 0.0801 0.0767 0.0748 -0.0016 -0.0091 0.0079 176 ALA A C 1322 O O . ALA A 176 ? 0.0915 0.0869 0.0778 -0.0048 -0.0119 -0.0088 176 ALA A O 1323 C CB . ALA A 176 ? 0.1161 0.0876 0.0823 -0.0236 -0.0118 0.0096 176 ALA A CB 1324 N N . ARG A 177 ? 0.0826 0.0846 0.0631 -0.0006 -0.0094 0.0011 177 ARG A N 1325 C CA . ARG A 177 ? 0.0875 0.0837 0.0660 -0.0091 -0.0038 0.0052 177 ARG A CA 1326 C C . ARG A 177 ? 0.0911 0.0843 0.0723 -0.0116 -0.0053 0.0003 177 ARG A C 1327 O O . ARG A 177 ? 0.0915 0.1145 0.0761 -0.0075 -0.0101 0.0009 177 ARG A O 1328 C CB . ARG A 177 ? 0.1046 0.0862 0.0708 -0.0073 -0.0036 0.0032 177 ARG A CB 1329 C CG . ARG A 177 ? 0.1041 0.0732 0.0774 0.0004 -0.0094 0.0005 177 ARG A CG 1330 C CD . ARG A 177 ? 0.1162 0.0791 0.0766 -0.0025 -0.0135 0.0052 177 ARG A CD 1331 N NE . ARG A 177 ? 0.1354 0.0812 0.0735 0.0066 -0.0201 0.0038 177 ARG A NE 1332 C CZ . ARG A 177 ? 0.1150 0.0806 0.0798 0.0015 -0.0116 0.0065 177 ARG A CZ 1333 N NH1 . ARG A 177 ? 0.1465 0.0777 0.0875 -0.0004 -0.0287 0.0116 177 ARG A NH1 1334 N NH2 . ARG A 177 ? 0.1772 0.0763 0.0900 0.0060 -0.0355 0.0074 177 ARG A NH2 1335 N N . ALA A 178 ? 0.0815 0.0940 0.0714 -0.0057 -0.0084 0.0058 178 ALA A N 1336 C CA . ALA A 178 ? 0.0828 0.0933 0.0775 -0.0117 -0.0105 0.0092 178 ALA A CA 1337 C C . ALA A 178 ? 0.0927 0.1015 0.0827 -0.0121 -0.0063 0.0124 178 ALA A C 1338 O O . ALA A 178 ? 0.0990 0.1116 0.0815 -0.0183 -0.0078 0.0170 178 ALA A O 1339 C CB . ALA A 178 ? 0.0938 0.0961 0.1023 -0.0055 0.0008 0.0037 178 ALA A CB 1340 N N . ASP A 179 ? 0.1034 0.1050 0.0827 -0.0253 -0.0129 0.0134 179 ASP A N 1341 C CA . ASP A 179 ? 0.1150 0.1230 0.1070 -0.0387 -0.0225 0.0274 179 ASP A CA 1342 C C . ASP A 179 ? 0.1076 0.1509 0.1026 -0.0473 -0.0140 0.0225 179 ASP A C 1343 O O . ASP A 179 ? 0.1299 0.2505 0.1469 -0.0802 -0.0110 0.0762 179 ASP A O 1344 C CB . ASP A 179 ? 0.1517 0.1231 0.1264 -0.0408 -0.0473 0.0129 179 ASP A CB 1345 C CG . ASP A 179 ? 0.1811 0.1049 0.1440 -0.0121 -0.0573 -0.0028 179 ASP A CG 1346 O OD1 . ASP A 179 ? 0.1782 0.1300 0.1319 -0.0094 -0.0558 0.0118 179 ASP A OD1 1347 O OD2 . ASP A 179 ? 0.1922 0.1661 0.1513 -0.0123 -0.0573 -0.0418 179 ASP A OD2 1348 N N . LYS A 180 ? 0.0901 0.1540 0.0979 -0.0269 -0.0016 0.0159 180 LYS A N 1349 C CA . LYS A 180 ? 0.0947 0.1709 0.1117 -0.0267 -0.0081 0.0018 180 LYS A CA 1350 C C . LYS A 180 ? 0.0880 0.1771 0.1176 -0.0179 -0.0071 -0.0066 180 LYS A C 1351 O O . LYS A 180 ? 0.0943 0.2034 0.1791 -0.0086 -0.0038 -0.0171 180 LYS A O 1352 C CB . LYS A 180 ? 0.0994 0.2097 0.1128 -0.0138 -0.0218 -0.0081 180 LYS A CB 1353 C CG . LYS A 180 ? 0.1366 0.2100 0.1106 -0.0060 -0.0178 0.0058 180 LYS A CG 1354 C CD . LYS A 180 ? 0.2070 0.2110 0.1308 -0.0459 -0.0031 -0.0033 180 LYS A CD 1355 C CE . LYS A 180 ? 0.3868 0.2198 0.1965 -0.0435 -0.0454 -0.0283 180 LYS A CE 1356 N NZ . LYS A 180 ? 0.8388 0.2753 0.3439 -0.2774 -0.0982 0.0586 180 LYS A NZ 1357 N N . VAL A 181 ? 0.0878 0.1659 0.1011 -0.0121 -0.0051 -0.0099 181 VAL A N 1358 C CA . VAL A 181 ? 0.0972 0.1575 0.1060 0.0010 -0.0053 -0.0033 181 VAL A CA 1359 C C . VAL A 181 ? 0.0938 0.1736 0.1134 -0.0034 -0.0032 -0.0100 181 VAL A C 1360 O O . VAL A 181 ? 0.1196 0.1919 0.1157 0.0193 0.0030 -0.0001 181 VAL A O 1361 C CB . VAL A 181 ? 0.1092 0.1509 0.1009 -0.0059 -0.0114 -0.0098 181 VAL A CB 1362 C CG1 . VAL A 181 ? 0.1100 0.1706 0.1411 -0.0007 0.0033 -0.0352 181 VAL A CG1 1363 C CG2 . VAL A 181 ? 0.1110 0.1632 0.1171 -0.0181 0.0099 -0.0125 181 VAL A CG2 1364 N N . ASP A 182 ? 0.1129 0.1855 0.1011 0.0138 0.0019 -0.0073 182 ASP A N 1365 C CA . ASP A 182 ? 0.1251 0.2036 0.1087 0.0127 -0.0008 -0.0015 182 ASP A CA 1366 C C . ASP A 182 ? 0.2270 0.1797 0.1044 0.0108 0.0181 0.0154 182 ASP A C 1367 O O . ASP A 182 ? 0.4440 0.2144 0.2936 0.1015 0.2356 0.0969 182 ASP A O 1368 C CB A ASP A 182 ? 0.1169 0.3522 0.0897 -0.0050 0.0065 -0.0010 182 ASP A CB 1369 C CB B ASP A 182 ? 0.1695 0.3161 0.1011 0.0282 -0.0183 -0.0135 182 ASP A CB 1370 C CG A ASP A 182 ? 0.1179 0.1849 0.1053 -0.0253 0.0019 0.0153 182 ASP A CG 1371 C CG B ASP A 182 ? 0.2597 0.2001 0.1127 0.0844 -0.0013 0.0110 182 ASP A CG 1372 O OD1 A ASP A 182 ? 0.1367 0.2282 0.1493 -0.0540 0.0419 -0.0435 182 ASP A OD1 1373 O OD1 B ASP A 182 ? 0.2022 0.2551 0.1557 -0.0456 0.0213 -0.0610 182 ASP A OD1 1374 O OD2 A ASP A 182 ? 0.1041 0.1456 0.0867 -0.0068 0.0157 0.0080 182 ASP A OD2 1375 O OD2 B ASP A 182 ? 0.4275 0.1964 0.1450 0.0533 0.0846 0.0052 182 ASP A OD2 1376 N N . GLN A 183 ? 0.1997 0.2341 0.2519 -0.0488 -0.0829 0.0307 183 GLN A N 1377 C CA . GLN A 183 ? 0.3437 0.2991 0.3030 -0.1429 -0.1662 0.0704 183 GLN A CA 1378 C C . GLN A 183 ? 0.2645 0.2385 0.1860 -0.0612 -0.0022 0.0009 183 GLN A C 1379 O O . GLN A 183 ? 0.5256 0.2505 0.2558 -0.0968 -0.0090 0.0114 183 GLN A O 1380 C CB . GLN A 183 ? 0.3217 0.3770 0.5103 -0.1816 -0.1974 0.1513 183 GLN A CB 1381 C CG . GLN A 183 ? 0.3850 0.5958 0.7569 -0.0599 -0.0095 0.0940 183 GLN A CG 1382 C CD . GLN A 183 ? 0.5740 0.4949 0.8354 -0.0218 -0.0477 -0.0142 183 GLN A CD 1383 O OE1 . GLN A 183 ? 0.9709 0.7734 1.0044 -0.3970 -0.1342 0.1970 183 GLN A OE1 1384 N NE2 . GLN A 183 ? 0.8263 0.8618 0.6814 0.2195 -0.5031 -0.1839 183 GLN A NE2 1385 N N . THR A 184 ? 0.1541 0.3063 0.1549 -0.0198 0.0278 0.0046 184 THR A N 1386 C CA . THR A 184 ? 0.1588 0.3340 0.1608 -0.0533 0.0338 0.0238 184 THR A CA 1387 C C . THR A 184 ? 0.1785 0.2844 0.1842 -0.0359 0.0450 0.0715 184 THR A C 1388 O O . THR A 184 ? 0.2168 0.3496 0.2184 -0.0670 0.0155 0.1141 184 THR A O 1389 C CB . THR A 184 ? 0.2056 0.3373 0.1638 -0.0665 0.0540 0.0076 184 THR A CB 1390 O OG1 . THR A 184 ? 0.2281 0.3209 0.2247 -0.0638 0.0627 -0.0198 184 THR A OG1 1391 C CG2 . THR A 184 ? 0.2036 0.6865 0.2356 -0.0059 0.1081 -0.0792 184 THR A CG2 1392 N N . ILE A 185 ? 0.1457 0.1818 0.1215 -0.0357 0.0118 0.0062 185 ILE A N 1393 C CA . ILE A 185 ? 0.1497 0.1644 0.1169 -0.0386 0.0087 0.0059 185 ILE A CA 1394 C C . ILE A 185 ? 0.1489 0.1400 0.1233 -0.0408 0.0097 -0.0021 185 ILE A C 1395 O O . ILE A 185 ? 0.1768 0.1949 0.1253 -0.0378 -0.0098 -0.0062 185 ILE A O 1396 C CB . ILE A 185 ? 0.1435 0.1668 0.1064 -0.0224 -0.0035 0.0078 185 ILE A CB 1397 C CG1 . ILE A 185 ? 0.1468 0.1437 0.1681 -0.0156 -0.0286 0.0017 185 ILE A CG1 1398 C CG2 . ILE A 185 ? 0.2248 0.2567 0.1154 -0.0746 0.0074 -0.0145 185 ILE A CG2 1399 C CD1 . ILE A 185 ? 0.1402 0.1602 0.1331 -0.0230 0.0103 -0.0095 185 ILE A CD1 1400 N N . ASP A 186 ? 0.1407 0.1670 0.1439 -0.0402 0.0159 -0.0024 186 ASP A N 1401 C CA . ASP A 186 ? 0.1351 0.2813 0.1618 -0.0664 0.0211 -0.0734 186 ASP A CA 1402 C C . ASP A 186 ? 0.1138 0.1166 0.1241 -0.0342 -0.0090 -0.0105 186 ASP A C 1403 O O . ASP A 186 ? 0.1501 0.1595 0.0943 -0.0523 -0.0032 0.0038 186 ASP A O 1404 C CB . ASP A 186 ? 0.2902 0.4568 0.4396 -0.2744 0.1913 -0.2866 186 ASP A CB 1405 C CG . ASP A 186 ? 0.7078 0.1853 0.6585 -0.1651 0.3081 -0.0150 186 ASP A CG 1406 O OD1 . ASP A 186 ? 1.3585 0.8010 0.9066 0.5261 -0.1942 -0.3006 186 ASP A OD1 1407 O OD2 . ASP A 186 ? 1.1410 0.8974 0.9410 0.3472 0.2801 -0.2958 186 ASP A OD2 1408 N N . ALA A 187 ? 0.1260 0.0947 0.1038 -0.0218 -0.0234 0.0037 187 ALA A N 1409 C CA . ALA A 187 ? 0.1276 0.0957 0.0888 -0.0302 -0.0143 0.0081 187 ALA A CA 1410 C C . ALA A 187 ? 0.1149 0.0851 0.0731 -0.0153 -0.0067 0.0127 187 ALA A C 1411 O O . ALA A 187 ? 0.1148 0.0869 0.0932 -0.0098 -0.0124 0.0059 187 ALA A O 1412 C CB . ALA A 187 ? 0.1369 0.1008 0.1286 -0.0173 -0.0019 -0.0183 187 ALA A CB 1413 N N . ALA A 188 ? 0.0979 0.0836 0.0817 -0.0151 -0.0090 0.0119 188 ALA A N 1414 C CA . ALA A 188 ? 0.0899 0.0860 0.0785 -0.0092 -0.0023 0.0060 188 ALA A CA 1415 C C . ALA A 188 ? 0.0951 0.0702 0.0732 -0.0012 -0.0041 -0.0003 188 ALA A C 1416 O O . ALA A 188 ? 0.0879 0.0877 0.0694 -0.0019 -0.0075 0.0083 188 ALA A O 1417 C CB . ALA A 188 ? 0.1045 0.0949 0.0845 0.0018 0.0017 0.0101 188 ALA A CB 1418 N N . PRO A 189 ? 0.0900 0.0837 0.0656 -0.0133 -0.0122 0.0075 189 PRO A N 1419 C CA . PRO A 189 ? 0.0886 0.0832 0.0649 -0.0051 -0.0077 0.0014 189 PRO A CA 1420 C C . PRO A 189 ? 0.0807 0.0760 0.0664 -0.0054 -0.0133 -0.0012 189 PRO A C 1421 O O . PRO A 189 ? 0.1050 0.0768 0.0683 -0.0051 -0.0062 0.0006 189 PRO A O 1422 C CB . PRO A 189 ? 0.0906 0.0768 0.0866 -0.0029 -0.0132 0.0064 189 PRO A CB 1423 C CG . PRO A 189 ? 0.0968 0.0851 0.0857 0.0005 -0.0241 0.0042 189 PRO A CG 1424 C CD . PRO A 189 ? 0.1089 0.0818 0.0710 0.0000 -0.0161 0.0089 189 PRO A CD 1425 N N . PHE A 190 ? 0.0825 0.0742 0.0687 -0.0034 -0.0063 0.0001 190 PHE A N 1426 C CA . PHE A 190 ? 0.0891 0.0665 0.0664 0.0005 -0.0080 0.0069 190 PHE A CA 1427 C C . PHE A 190 ? 0.0842 0.0721 0.0687 -0.0014 -0.0102 0.0078 190 PHE A C 1428 O O . PHE A 190 ? 0.0916 0.0677 0.1072 0.0017 -0.0233 -0.0018 190 PHE A O 1429 C CB . PHE A 190 ? 0.0816 0.0856 0.0735 0.0004 -0.0079 0.0150 190 PHE A CB 1430 C CG . PHE A 190 ? 0.0903 0.0752 0.0687 -0.0040 -0.0137 0.0093 190 PHE A CG 1431 C CD1 . PHE A 190 ? 0.0877 0.1050 0.0831 -0.0077 -0.0132 0.0029 190 PHE A CD1 1432 C CD2 . PHE A 190 ? 0.0975 0.1019 0.0768 -0.0018 -0.0124 0.0084 190 PHE A CD2 1433 C CE1 . PHE A 190 ? 0.0899 0.1369 0.0852 -0.0085 -0.0057 -0.0013 190 PHE A CE1 1434 C CE2 . PHE A 190 ? 0.1173 0.1034 0.0813 -0.0061 -0.0223 0.0019 190 PHE A CE2 1435 C CZ . PHE A 190 ? 0.0974 0.1169 0.0962 -0.0115 -0.0341 0.0093 190 PHE A CZ 1436 N N . ASP A 191 ? 0.0817 0.0716 0.0751 -0.0006 -0.0130 0.0023 191 ASP A N 1437 C CA . ASP A 191 ? 0.0740 0.0758 0.0798 -0.0007 -0.0132 -0.0019 191 ASP A CA 1438 C C . ASP A 191 ? 0.0885 0.0759 0.0698 -0.0001 -0.0085 0.0040 191 ASP A C 1439 O O . ASP A 191 ? 0.0970 0.0776 0.0890 -0.0036 -0.0146 0.0043 191 ASP A O 1440 C CB . ASP A 191 ? 0.0785 0.0742 0.0815 -0.0002 -0.0152 0.0059 191 ASP A CB 1441 C CG . ASP A 191 ? 0.0808 0.0674 0.0734 0.0032 -0.0221 -0.0050 191 ASP A CG 1442 O OD1 . ASP A 191 ? 0.0927 0.0729 0.0820 0.0041 -0.0177 0.0006 191 ASP A OD1 1443 O OD2 . ASP A 191 ? 0.0847 0.0814 0.0771 0.0020 -0.0162 -0.0021 191 ASP A OD2 1444 N N . SER A 192 ? 0.0865 0.0732 0.0775 -0.0027 -0.0161 0.0038 192 SER A N 1445 C CA . SER A 192 ? 0.1017 0.0811 0.0714 0.0031 -0.0153 0.0113 192 SER A CA 1446 C C . SER A 192 ? 0.1032 0.0730 0.0783 -0.0016 -0.0187 0.0018 192 SER A C 1447 O O . SER A 192 ? 0.1347 0.0853 0.0795 0.0165 -0.0236 0.0102 192 SER A O 1448 C CB . SER A 192 ? 0.1168 0.0866 0.0822 0.0025 -0.0272 -0.0019 192 SER A CB 1449 O OG . SER A 192 ? 0.1060 0.0928 0.1194 -0.0015 -0.0336 0.0016 192 SER A OG 1450 N N . THR A 193 ? 0.1021 0.0746 0.0727 0.0068 -0.0201 0.0005 193 THR A N 1451 C CA . THR A 193 ? 0.1037 0.0728 0.0732 0.0078 -0.0275 -0.0026 193 THR A CA 1452 C C . THR A 193 ? 0.0870 0.0722 0.0808 0.0119 -0.0181 -0.0039 193 THR A C 1453 O O . THR A 193 ? 0.0937 0.0771 0.0736 0.0069 -0.0134 0.0038 193 THR A O 1454 C CB . THR A 193 ? 0.1073 0.0784 0.0864 0.0036 -0.0323 0.0082 193 THR A CB 1455 O OG1 . THR A 193 ? 0.0985 0.0833 0.0798 0.0050 -0.0280 0.0056 193 THR A OG1 1456 C CG2 . THR A 193 ? 0.1103 0.1031 0.0964 0.0049 -0.0414 0.0035 193 THR A CG2 1457 N N . PRO A 194 ? 0.0961 0.0759 0.0735 0.0056 -0.0176 -0.0001 194 PRO A N 1458 C CA . PRO A 194 ? 0.0826 0.0835 0.0818 0.0062 -0.0192 -0.0007 194 PRO A CA 1459 C C . PRO A 194 ? 0.1030 0.0706 0.0794 0.0015 -0.0164 0.0042 194 PRO A C 1460 O O . PRO A 194 ? 0.1072 0.0877 0.0847 0.0000 -0.0281 0.0019 194 PRO A O 1461 C CB . PRO A 194 ? 0.0944 0.0954 0.0976 -0.0005 -0.0081 -0.0094 194 PRO A CB 1462 C CG . PRO A 194 ? 0.1035 0.0890 0.1010 -0.0036 -0.0045 -0.0004 194 PRO A CG 1463 C CD . PRO A 194 ? 0.1084 0.0868 0.0739 0.0064 -0.0027 0.0060 194 PRO A CD 1464 N N . PHE A 195 ? 0.0924 0.0783 0.0804 0.0046 -0.0121 0.0030 195 PHE A N 1465 C CA . PHE A 195 ? 0.0972 0.0839 0.0837 0.0008 -0.0107 -0.0043 195 PHE A CA 1466 C C . PHE A 195 ? 0.0981 0.0912 0.1025 0.0059 -0.0042 0.0024 195 PHE A C 1467 O O . PHE A 195 ? 0.1209 0.0992 0.1431 0.0072 0.0215 -0.0133 195 PHE A O 1468 C CB . PHE A 195 ? 0.1208 0.0844 0.0979 0.0124 -0.0062 0.0045 195 PHE A CB 1469 C CG . PHE A 195 ? 0.1355 0.0754 0.1012 0.0074 -0.0026 0.0110 195 PHE A CG 1470 C CD1 . PHE A 195 ? 0.1498 0.1140 0.1335 -0.0168 -0.0075 0.0167 195 PHE A CD1 1471 C CD2 . PHE A 195 ? 0.1863 0.1222 0.1067 0.0256 0.0122 0.0312 195 PHE A CD2 1472 C CE1 . PHE A 195 ? 0.1590 0.1479 0.2446 -0.0374 0.0112 0.0501 195 PHE A CE1 1473 C CE2 . PHE A 195 ? 0.2355 0.1734 0.1443 0.0686 0.0642 0.0666 195 PHE A CE2 1474 C CZ . PHE A 195 ? 0.1879 0.1365 0.2352 0.0521 0.0913 0.0788 195 PHE A CZ 1475 N N . THR A 196 ? 0.0867 0.0882 0.0875 0.0021 -0.0100 0.0011 196 THR A N 1476 C CA . THR A 196 ? 0.0882 0.0921 0.0985 0.0042 -0.0073 0.0127 196 THR A CA 1477 C C . THR A 196 ? 0.0848 0.0778 0.0860 0.0071 -0.0172 -0.0016 196 THR A C 1478 O O . THR A 196 ? 0.0921 0.0835 0.0919 0.0073 -0.0118 0.0051 196 THR A O 1479 C CB . THR A 196 ? 0.0962 0.1278 0.1307 0.0013 -0.0381 0.0278 196 THR A CB 1480 O OG1 . THR A 196 ? 0.1695 0.1515 0.1606 -0.0169 -0.0636 0.0576 196 THR A OG1 1481 C CG2 . THR A 196 ? 0.1068 0.1257 0.1324 -0.0042 -0.0275 -0.0064 196 THR A CG2 1482 N N . PHE A 197 ? 0.0969 0.0754 0.0874 0.0042 -0.0107 0.0003 197 PHE A N 1483 C CA . PHE A 197 ? 0.0844 0.0802 0.0800 0.0065 -0.0103 0.0033 197 PHE A CA 1484 C C . PHE A 197 ? 0.0884 0.0852 0.0838 0.0079 -0.0129 -0.0013 197 PHE A C 1485 O O . PHE A 197 ? 0.0947 0.1469 0.1149 -0.0188 0.0072 -0.0248 197 PHE A O 1486 C CB . PHE A 197 ? 0.1079 0.0802 0.0826 -0.0031 -0.0180 0.0004 197 PHE A CB 1487 C CG . PHE A 197 ? 0.1251 0.0961 0.0775 0.0104 -0.0109 -0.0040 197 PHE A CG 1488 C CD1 . PHE A 197 ? 0.1964 0.0852 0.1090 -0.0122 -0.0210 0.0042 197 PHE A CD1 1489 C CD2 . PHE A 197 ? 0.1184 0.1841 0.0985 0.0477 -0.0072 0.0194 197 PHE A CD2 1490 C CE1 . PHE A 197 ? 0.3011 0.1082 0.0902 0.0095 -0.0365 0.0068 197 PHE A CE1 1491 C CE2 . PHE A 197 ? 0.1777 0.2628 0.1141 0.1061 -0.0039 0.0282 197 PHE A CE2 1492 C CZ . PHE A 197 ? 0.2879 0.1640 0.0849 0.0916 -0.0308 -0.0024 197 PHE A CZ 1493 N N . ASP A 198 ? 0.0998 0.0985 0.0992 -0.0196 0.0015 -0.0149 198 ASP A N 1494 C CA . ASP A 198 ? 0.0873 0.0874 0.0983 -0.0046 -0.0095 -0.0109 198 ASP A CA 1495 C C . ASP A 198 ? 0.0804 0.0908 0.0775 -0.0051 -0.0141 0.0057 198 ASP A C 1496 O O . ASP A 198 ? 0.0869 0.0863 0.0906 -0.0083 -0.0195 0.0024 198 ASP A O 1497 C CB . ASP A 198 ? 0.0875 0.0809 0.1077 0.0050 -0.0107 -0.0055 198 ASP A CB 1498 C CG . ASP A 198 ? 0.0801 0.0807 0.1072 0.0058 -0.0215 0.0029 198 ASP A CG 1499 O OD1 . ASP A 198 ? 0.0818 0.0874 0.0927 0.0027 -0.0188 0.0033 198 ASP A OD1 1500 O OD2 . ASP A 198 ? 0.0895 0.1144 0.1091 0.0099 -0.0237 0.0185 198 ASP A OD2 1501 N N . THR A 199 ? 0.0803 0.0820 0.0941 -0.0022 -0.0205 -0.0001 199 THR A N 1502 C CA . THR A 199 ? 0.0803 0.0862 0.0943 -0.0067 -0.0232 0.0005 199 THR A CA 1503 C C . THR A 199 ? 0.0764 0.0785 0.0918 -0.0033 -0.0227 -0.0024 199 THR A C 1504 O O . THR A 199 ? 0.0894 0.0780 0.1109 -0.0015 -0.0158 0.0019 199 THR A O 1505 C CB . THR A 199 ? 0.0933 0.0800 0.0912 -0.0047 -0.0228 0.0054 199 THR A CB 1506 O OG1 . THR A 199 ? 0.0945 0.0991 0.0972 -0.0155 -0.0249 -0.0012 199 THR A OG1 1507 C CG2 . THR A 199 ? 0.0954 0.0920 0.1018 -0.0048 -0.0164 0.0007 199 THR A CG2 1508 N N . GLN A 200 ? 0.0887 0.0740 0.0937 0.0031 -0.0207 0.0037 200 GLN A N 1509 C CA . GLN A 200 ? 0.0933 0.0737 0.0845 0.0038 -0.0240 -0.0008 200 GLN A CA 1510 C C . GLN A 200 ? 0.0951 0.0710 0.0827 -0.0035 -0.0263 0.0036 200 GLN A C 1511 O O . GLN A 200 ? 0.1017 0.0791 0.0865 0.0046 -0.0232 -0.0040 200 GLN A O 1512 C CB . GLN A 200 ? 0.0995 0.0770 0.0907 -0.0007 -0.0346 0.0024 200 GLN A CB 1513 C CG . GLN A 200 ? 0.0878 0.0881 0.1098 0.0022 -0.0257 0.0037 200 GLN A CG 1514 C CD . GLN A 200 ? 0.0917 0.1034 0.0984 0.0031 -0.0348 0.0091 200 GLN A CD 1515 O OE1 . GLN A 200 ? 0.0984 0.1426 0.1069 -0.0122 -0.0269 -0.0106 200 GLN A OE1 1516 N NE2 . GLN A 200 ? 0.0931 0.1202 0.1072 -0.0105 -0.0296 0.0021 200 GLN A NE2 1517 N N . VAL A 201 ? 0.0843 0.0718 0.0857 -0.0004 -0.0188 0.0014 201 VAL A N 1518 C CA . VAL A 201 ? 0.0861 0.0720 0.0796 -0.0033 -0.0164 0.0031 201 VAL A CA 1519 C C . VAL A 201 ? 0.0765 0.0812 0.0853 0.0015 -0.0194 0.0043 201 VAL A C 1520 O O . VAL A 201 ? 0.0879 0.0757 0.0912 0.0011 -0.0164 0.0061 201 VAL A O 1521 C CB . VAL A 201 ? 0.0864 0.0789 0.0909 -0.0068 -0.0226 0.0042 201 VAL A CB 1522 C CG1 . VAL A 201 ? 0.1238 0.0864 0.0808 -0.0141 -0.0182 0.0027 201 VAL A CG1 1523 C CG2 . VAL A 201 ? 0.0934 0.0948 0.1071 -0.0044 -0.0280 0.0024 201 VAL A CG2 1524 N N . PHE A 202 ? 0.0811 0.0706 0.0901 -0.0019 -0.0161 0.0009 202 PHE A N 1525 C CA . PHE A 202 ? 0.0871 0.0780 0.0817 -0.0026 -0.0212 0.0039 202 PHE A CA 1526 C C . PHE A 202 ? 0.0907 0.0789 0.0861 -0.0141 -0.0151 0.0023 202 PHE A C 1527 O O . PHE A 202 ? 0.1110 0.0740 0.0950 0.0019 -0.0288 -0.0010 202 PHE A O 1528 C CB . PHE A 202 ? 0.0975 0.0782 0.0858 -0.0084 -0.0177 0.0058 202 PHE A CB 1529 C CG . PHE A 202 ? 0.0896 0.0733 0.0891 -0.0094 -0.0146 0.0044 202 PHE A CG 1530 C CD1 . PHE A 202 ? 0.0925 0.0766 0.0964 -0.0041 -0.0112 0.0037 202 PHE A CD1 1531 C CD2 . PHE A 202 ? 0.1029 0.0780 0.0897 -0.0049 -0.0152 0.0094 202 PHE A CD2 1532 C CE1 . PHE A 202 ? 0.1008 0.0918 0.0969 -0.0100 -0.0093 -0.0055 202 PHE A CE1 1533 C CE2 . PHE A 202 ? 0.0898 0.1054 0.0953 -0.0046 -0.0198 0.0177 202 PHE A CE2 1534 C CZ . PHE A 202 ? 0.1162 0.0941 0.0875 -0.0186 -0.0237 0.0034 202 PHE A CZ 1535 N N . LEU A 203 ? 0.0881 0.0760 0.0856 -0.0027 -0.0239 0.0049 203 LEU A N 1536 C CA . LEU A 203 ? 0.0919 0.0800 0.0865 -0.0115 -0.0232 0.0020 203 LEU A CA 1537 C C . LEU A 203 ? 0.0941 0.0697 0.0868 -0.0029 -0.0282 -0.0002 203 LEU A C 1538 O O . LEU A 203 ? 0.1040 0.0791 0.0995 -0.0030 -0.0258 -0.0050 203 LEU A O 1539 C CB A LEU A 203 ? 0.0969 0.0722 0.0854 -0.0023 -0.0209 0.0016 203 LEU A CB 1540 C CB B LEU A 203 ? 0.0877 0.1384 0.1137 -0.0015 -0.0247 0.0196 203 LEU A CB 1541 C CG A LEU A 203 ? 0.0845 0.0812 0.0900 -0.0012 -0.0247 0.0099 203 LEU A CG 1542 C CG B LEU A 203 ? 0.1092 0.1592 0.1281 0.0080 -0.0503 -0.0053 203 LEU A CG 1543 C CD1 A LEU A 203 ? 0.1347 0.0858 0.1028 0.0074 -0.0569 -0.0016 203 LEU A CD1 1544 C CD1 B LEU A 203 ? 0.1973 0.2924 0.1077 -0.0263 -0.0234 -0.0147 203 LEU A CD1 1545 C CD2 A LEU A 203 ? 0.1304 0.1102 0.0976 0.0422 -0.0694 -0.0129 203 LEU A CD2 1546 C CD2 B LEU A 203 ? 0.4882 0.1725 0.3556 -0.0683 -0.0222 -0.0901 203 LEU A CD2 1547 N N . GLU A 204 ? 0.0816 0.0802 0.0807 -0.0039 -0.0173 0.0012 204 GLU A N 1548 C CA . GLU A 204 ? 0.0888 0.0760 0.0842 0.0020 -0.0125 -0.0034 204 GLU A CA 1549 C C . GLU A 204 ? 0.0845 0.0729 0.0749 -0.0091 -0.0113 0.0032 204 GLU A C 1550 O O . GLU A 204 ? 0.0959 0.0877 0.0834 -0.0014 -0.0125 0.0079 204 GLU A O 1551 C CB . GLU A 204 ? 0.1001 0.0763 0.0857 -0.0140 -0.0143 0.0055 204 GLU A CB 1552 C CG . GLU A 204 ? 0.1031 0.0843 0.0963 -0.0044 -0.0252 0.0043 204 GLU A CG 1553 C CD . GLU A 204 ? 0.1016 0.0886 0.0832 -0.0022 -0.0318 -0.0026 204 GLU A CD 1554 O OE1 . GLU A 204 ? 0.0976 0.0777 0.1095 -0.0032 -0.0245 -0.0011 204 GLU A OE1 1555 O OE2 . GLU A 204 ? 0.0953 0.0886 0.1300 0.0010 -0.0262 0.0115 204 GLU A OE2 1556 N N . VAL A 205 ? 0.0749 0.0780 0.0905 -0.0016 -0.0145 0.0041 205 VAL A N 1557 C CA . VAL A 205 ? 0.0859 0.0750 0.0851 -0.0040 -0.0162 0.0009 205 VAL A CA 1558 C C . VAL A 205 ? 0.1028 0.0767 0.0773 0.0002 -0.0132 0.0054 205 VAL A C 1559 O O . VAL A 205 ? 0.0974 0.0880 0.0943 0.0006 -0.0155 -0.0052 205 VAL A O 1560 C CB . VAL A 205 ? 0.0947 0.0870 0.0810 -0.0030 -0.0177 0.0061 205 VAL A CB 1561 C CG1 . VAL A 205 ? 0.1241 0.0880 0.1045 0.0119 -0.0278 0.0064 205 VAL A CG1 1562 C CG2 . VAL A 205 ? 0.0992 0.0879 0.0828 -0.0071 -0.0206 0.0034 205 VAL A CG2 1563 N N . LEU A 206 ? 0.0929 0.0722 0.0866 -0.0050 -0.0183 -0.0005 206 LEU A N 1564 C CA . LEU A 206 ? 0.1071 0.0792 0.0883 -0.0019 -0.0114 -0.0041 206 LEU A CA 1565 C C . LEU A 206 ? 0.1222 0.0775 0.0934 -0.0055 -0.0186 -0.0057 206 LEU A C 1566 O O . LEU A 206 ? 0.2205 0.0924 0.0939 -0.0342 -0.0230 -0.0123 206 LEU A O 1567 C CB . LEU A 206 ? 0.1025 0.0775 0.1034 -0.0086 -0.0143 -0.0009 206 LEU A CB 1568 C CG . LEU A 206 ? 0.1245 0.1010 0.1011 -0.0350 -0.0123 -0.0104 206 LEU A CG 1569 C CD1 . LEU A 206 ? 0.1401 0.1211 0.1194 -0.0381 0.0041 -0.0039 206 LEU A CD1 1570 C CD2 . LEU A 206 ? 0.1414 0.1194 0.1078 -0.0201 -0.0273 0.0226 206 LEU A CD2 1571 N N . LEU A 207 ? 0.0999 0.0825 0.0826 -0.0100 -0.0122 -0.0055 207 LEU A N 1572 C CA . LEU A 207 ? 0.1001 0.0993 0.0897 -0.0212 -0.0163 -0.0026 207 LEU A CA 1573 C C . LEU A 207 ? 0.1059 0.0987 0.0903 -0.0184 -0.0070 -0.0105 207 LEU A C 1574 O O . LEU A 207 ? 0.1013 0.1448 0.1139 -0.0202 -0.0081 -0.0424 207 LEU A O 1575 C CB . LEU A 207 ? 0.1272 0.0999 0.0876 -0.0081 -0.0179 -0.0029 207 LEU A CB 1576 C CG . LEU A 207 ? 0.1195 0.1220 0.1215 0.0008 -0.0333 -0.0044 207 LEU A CG 1577 C CD1 . LEU A 207 ? 0.2038 0.1238 0.1275 0.0303 -0.0583 -0.0117 207 LEU A CD1 1578 C CD2 . LEU A 207 ? 0.1389 0.1600 0.2669 0.0133 -0.0809 -0.0616 207 LEU A CD2 1579 N N . LYS A 208 ? 0.1169 0.1186 0.0927 -0.0232 -0.0058 -0.0148 208 LYS A N 1580 C CA . LYS A 208 ? 0.1289 0.1142 0.1089 -0.0226 0.0082 -0.0195 208 LYS A CA 1581 C C . LYS A 208 ? 0.1277 0.1072 0.0902 -0.0138 0.0072 -0.0047 208 LYS A C 1582 O O . LYS A 208 ? 0.1325 0.1226 0.1155 -0.0070 0.0064 0.0075 208 LYS A O 1583 C CB . LYS A 208 ? 0.2200 0.1544 0.1568 -0.0356 0.0206 -0.0740 208 LYS A CB 1584 C CG . LYS A 208 ? 0.2848 0.3683 0.2240 -0.1414 0.1285 -0.1911 208 LYS A CG 1585 C CD . LYS A 208 ? 0.4297 0.7612 0.2767 -0.0360 0.1529 -0.0113 208 LYS A CD 1586 C CE . LYS A 208 ? 0.8755 0.7087 0.3578 0.0899 -0.1163 -0.1839 208 LYS A CE 1587 N NZ . LYS A 208 ? 1.3336 0.4752 0.3813 -0.5523 -0.4998 0.1627 208 LYS A NZ 1588 N N . GLY A 209 ? 0.1236 0.1084 0.0985 -0.0153 0.0077 0.0068 209 GLY A N 1589 C CA . GLY A 209 ? 0.1366 0.0935 0.0915 -0.0209 0.0055 0.0053 209 GLY A CA 1590 C C . GLY A 209 ? 0.1382 0.1043 0.1084 -0.0191 0.0296 0.0011 209 GLY A C 1591 O O . GLY A 209 ? 0.2125 0.1065 0.1420 -0.0202 0.0697 -0.0146 209 GLY A O 1592 N N . VAL A 210 ? 0.1464 0.1012 0.0824 -0.0228 0.0156 -0.0026 210 VAL A N 1593 C CA . VAL A 210 ? 0.1535 0.1164 0.0830 -0.0308 0.0163 -0.0059 210 VAL A CA 1594 C C . VAL A 210 ? 0.1373 0.1227 0.0892 -0.0257 0.0128 -0.0037 210 VAL A C 1595 O O . VAL A 210 ? 0.2039 0.1603 0.0918 -0.0713 0.0345 -0.0154 210 VAL A O 1596 C CB . VAL A 210 ? 0.1483 0.1602 0.0911 -0.0422 0.0027 -0.0135 210 VAL A CB 1597 C CG1 . VAL A 210 ? 0.1620 0.2139 0.1253 -0.0573 -0.0039 0.0155 210 VAL A CG1 1598 C CG2 . VAL A 210 ? 0.1641 0.1807 0.0897 0.0083 0.0111 0.0081 210 VAL A CG2 1599 N N . GLY A 211 ? 0.1356 0.1150 0.0883 -0.0262 0.0150 -0.0014 211 GLY A N 1600 C CA . GLY A 211 ? 0.1382 0.1181 0.0905 -0.0217 0.0091 -0.0012 211 GLY A CA 1601 C C . GLY A 211 ? 0.1198 0.1127 0.0874 -0.0131 0.0026 0.0088 211 GLY A C 1602 O O . GLY A 211 ? 0.1356 0.1462 0.0894 -0.0357 0.0030 0.0102 211 GLY A O 1603 N N . PHE A 212 ? 0.1377 0.1213 0.0862 -0.0262 0.0121 -0.0017 212 PHE A N 1604 C CA . PHE A 212 ? 0.1155 0.1210 0.1040 -0.0125 0.0065 -0.0040 212 PHE A CA 1605 C C . PHE A 212 ? 0.1196 0.1106 0.0907 -0.0160 0.0058 0.0018 212 PHE A C 1606 O O . PHE A 212 ? 0.1521 0.1258 0.0899 -0.0174 0.0125 0.0092 212 PHE A O 1607 C CB . PHE A 212 ? 0.1235 0.1315 0.1225 -0.0024 0.0096 -0.0053 212 PHE A CB 1608 C CG . PHE A 212 ? 0.1157 0.1278 0.1452 -0.0020 0.0208 -0.0126 212 PHE A CG 1609 C CD1 . PHE A 212 ? 0.1630 0.1486 0.1665 0.0032 0.0102 -0.0354 212 PHE A CD1 1610 C CD2 . PHE A 212 ? 0.1104 0.1452 0.1487 0.0093 0.0201 0.0119 212 PHE A CD2 1611 C CE1 . PHE A 212 ? 0.1740 0.1403 0.2504 0.0096 -0.0069 -0.0408 212 PHE A CE1 1612 C CE2 . PHE A 212 ? 0.1272 0.1552 0.2146 0.0042 0.0017 0.0356 212 PHE A CE2 1613 C CZ . PHE A 212 ? 0.1405 0.1275 0.2749 -0.0032 -0.0016 0.0108 212 PHE A CZ 1614 N N . PRO A 213 ? 0.1153 0.1119 0.0825 -0.0097 -0.0033 0.0039 213 PRO A N 1615 C CA . PRO A 213 ? 0.1278 0.1096 0.0900 -0.0126 -0.0023 0.0030 213 PRO A CA 1616 C C . PRO A 213 ? 0.1340 0.1190 0.0896 -0.0074 0.0061 0.0018 213 PRO A C 1617 O O . PRO A 213 ? 0.1544 0.1294 0.1297 -0.0185 0.0041 0.0273 213 PRO A O 1618 C CB . PRO A 213 ? 0.1217 0.1194 0.1027 -0.0064 0.0084 -0.0050 213 PRO A CB 1619 C CG . PRO A 213 ? 0.1143 0.1272 0.0864 -0.0250 -0.0004 -0.0076 213 PRO A CG 1620 C CD . PRO A 213 ? 0.1226 0.1157 0.0833 -0.0093 0.0109 0.0111 213 PRO A CD 1621 N N . GLY A 214 ? 0.1194 0.1284 0.0991 -0.0180 0.0111 0.0047 214 GLY A N 1622 C CA . GLY A 214 ? 0.1290 0.1489 0.1271 -0.0272 0.0158 0.0032 214 GLY A CA 1623 C C . GLY A 214 ? 0.1203 0.2390 0.1297 -0.0298 0.0354 -0.0351 214 GLY A C 1624 O O . GLY A 214 ? 0.1558 0.3367 0.1577 -0.0157 0.0258 -0.0906 214 GLY A O 1625 N N . SER A 215 ? 0.1509 0.2493 0.1328 0.0145 0.0324 -0.0350 215 SER A N 1626 C CA . SER A 215 ? 0.1612 0.2521 0.2030 0.0114 0.0603 -0.0214 215 SER A CA 1627 C C . SER A 215 ? 0.1512 0.2544 0.1280 0.0432 0.0247 -0.0058 215 SER A C 1628 O O . SER A 215 ? 0.1527 0.2533 0.2037 -0.0106 0.0402 -0.0289 215 SER A O 1629 C CB . SER A 215 ? 0.1551 0.3546 0.2497 0.0104 0.0377 -0.0409 215 SER A CB 1630 O OG . SER A 215 ? 0.1925 0.4611 0.2251 0.0480 0.0004 0.0428 215 SER A OG 1631 N N . ALA A 216 ? 0.2005 0.2549 0.2239 0.0147 0.0065 -0.0722 216 ALA A N 1632 C CA . ALA A 216 ? 0.2033 0.2683 0.2479 0.0059 0.0224 -0.0790 216 ALA A CA 1633 C C . ALA A 216 ? 0.3001 0.2558 0.2770 0.0857 0.0199 -0.0722 216 ALA A C 1634 O O . ALA A 216 ? 0.4710 0.2607 0.4577 0.0866 0.1072 -0.0161 216 ALA A O 1635 C CB . ALA A 216 ? 0.2558 0.2492 0.2756 0.0383 0.0184 -0.0916 216 ALA A CB 1636 N N . ASN A 217 ? 0.1898 0.4252 0.1811 0.0661 0.0532 -0.0316 217 ASN A N 1637 C CA . ASN A 217 ? 0.2383 0.6081 0.1999 0.1857 0.0657 -0.0460 217 ASN A CA 1638 C C . ASN A 217 ? 0.1823 0.6219 0.2033 0.1843 0.0250 -0.0309 217 ASN A C 1639 O O . ASN A 217 ? 0.1771 0.9552 0.3011 0.1925 0.0113 -0.1336 217 ASN A O 1640 C CB . ASN A 217 ? 0.2008 0.8385 0.2341 0.1477 0.0416 -0.0240 217 ASN A CB 1641 C CG . ASN A 217 ? 0.3160 0.8673 0.4378 0.0643 0.1365 0.1427 217 ASN A CG 1642 O OD1 . ASN A 217 ? 0.4316 0.6385 0.8371 -0.0173 0.3063 0.1414 217 ASN A OD1 1643 N ND2 . ASN A 217 ? 0.5509 1.2997 0.9147 0.2356 0.4310 0.5321 217 ASN A ND2 1644 N N . ASN A 218 ? 0.1544 0.3084 0.1272 0.0588 0.0257 0.0126 218 ASN A N 1645 C CA . ASN A 218 ? 0.1190 0.2216 0.1370 0.0027 -0.0010 0.0234 218 ASN A CA 1646 C C . ASN A 218 ? 0.1007 0.2030 0.1353 0.0205 0.0096 0.0144 218 ASN A C 1647 O O . ASN A 218 ? 0.1376 0.1686 0.1476 0.0113 0.0013 -0.0022 218 ASN A O 1648 C CB . ASN A 218 ? 0.1167 0.1870 0.1393 -0.0138 0.0046 0.0253 218 ASN A CB 1649 C CG . ASN A 218 ? 0.1346 0.2026 0.1632 -0.0409 -0.0044 0.0425 218 ASN A CG 1650 O OD1 . ASN A 218 ? 0.2182 0.2908 0.2335 -0.0969 -0.0983 0.1165 218 ASN A OD1 1651 N ND2 . ASN A 218 ? 0.1472 0.2452 0.1708 -0.0584 -0.0258 0.0809 218 ASN A ND2 1652 N N . THR A 219 ? 0.0917 0.2271 0.1660 -0.0074 -0.0004 0.0561 219 THR A N 1653 C CA . THR A 219 ? 0.0950 0.2003 0.1551 0.0092 0.0050 0.0398 219 THR A CA 1654 C C . THR A 219 ? 0.0949 0.1512 0.1230 -0.0033 -0.0078 0.0017 219 THR A C 1655 O O . THR A 219 ? 0.1319 0.1347 0.1631 -0.0071 -0.0134 -0.0123 219 THR A O 1656 C CB . THR A 219 ? 0.0886 0.3214 0.1773 -0.0168 -0.0133 0.0786 219 THR A CB 1657 O OG1 . THR A 219 ? 0.1027 0.4316 0.2291 0.0092 0.0002 0.0971 219 THR A OG1 1658 C CG2 . THR A 219 ? 0.1124 0.3021 0.1884 -0.0154 -0.0211 0.0776 219 THR A CG2 1659 N N . GLY A 220 ? 0.0920 0.1343 0.1264 0.0068 -0.0110 0.0115 220 GLY A N 1660 C CA . GLY A 220 ? 0.0920 0.1690 0.1143 -0.0003 -0.0136 0.0141 220 GLY A CA 1661 C C . GLY A 220 ? 0.0867 0.1256 0.0976 -0.0139 -0.0090 0.0005 220 GLY A C 1662 O O . GLY A 220 ? 0.0867 0.1285 0.0978 -0.0148 -0.0093 0.0022 220 GLY A O 1663 N N . GLU A 221 ? 0.0915 0.1258 0.1033 0.0131 -0.0127 -0.0015 221 GLU A N 1664 C CA . GLU A 221 ? 0.0902 0.1122 0.0959 0.0082 -0.0088 -0.0040 221 GLU A CA 1665 C C . GLU A 221 ? 0.0939 0.1135 0.0942 0.0108 0.0026 -0.0095 221 GLU A C 1666 O O . GLU A 221 ? 0.0956 0.1363 0.1266 0.0125 -0.0061 -0.0256 221 GLU A O 1667 C CB . GLU A 221 ? 0.1235 0.1113 0.1048 0.0088 -0.0039 -0.0017 221 GLU A CB 1668 C CG . GLU A 221 ? 0.1272 0.1261 0.1167 0.0135 -0.0098 0.0077 221 GLU A CG 1669 C CD . GLU A 221 ? 0.1183 0.1392 0.1455 0.0136 0.0011 0.0274 221 GLU A CD 1670 O OE1 . GLU A 221 ? 0.1257 0.2510 0.2572 -0.0216 -0.0290 0.1280 221 GLU A OE1 1671 O OE2 . GLU A 221 ? 0.1403 0.1231 0.1259 -0.0122 -0.0249 0.0135 221 GLU A OE2 1672 N N . VAL A 222 ? 0.0930 0.1125 0.0892 0.0130 -0.0043 -0.0103 222 VAL A N 1673 C CA . VAL A 222 ? 0.0997 0.1099 0.0880 0.0103 -0.0015 -0.0087 222 VAL A CA 1674 C C . VAL A 222 ? 0.1033 0.1037 0.0889 -0.0033 -0.0001 -0.0016 222 VAL A C 1675 O O . VAL A 222 ? 0.1176 0.0959 0.0911 0.0031 -0.0039 -0.0037 222 VAL A O 1676 C CB . VAL A 222 ? 0.1068 0.1042 0.1010 0.0070 -0.0087 -0.0001 222 VAL A CB 1677 C CG1 . VAL A 222 ? 0.1384 0.1177 0.1206 0.0221 -0.0101 0.0033 222 VAL A CG1 1678 C CG2 . VAL A 222 ? 0.1086 0.1202 0.1134 0.0045 0.0020 0.0207 222 VAL A CG2 1679 N N . ALA A 223 ? 0.1073 0.1025 0.0907 0.0066 -0.0061 -0.0116 223 ALA A N 1680 C CA . ALA A 223 ? 0.1092 0.1035 0.0857 0.0011 0.0026 -0.0028 223 ALA A CA 1681 C C . ALA A 223 ? 0.1026 0.1041 0.0760 -0.0029 -0.0025 -0.0031 223 ALA A C 1682 O O . ALA A 223 ? 0.1057 0.0971 0.0950 -0.0010 0.0021 0.0042 223 ALA A O 1683 C CB . ALA A 223 ? 0.1101 0.1449 0.0925 0.0067 0.0023 -0.0219 223 ALA A CB 1684 N N . SER A 224 ? 0.1085 0.0991 0.0796 0.0010 -0.0079 0.0045 224 SER A N 1685 C CA . SER A 224 ? 0.1094 0.0967 0.0837 -0.0033 -0.0120 -0.0025 224 SER A CA 1686 C C . SER A 224 ? 0.1140 0.0850 0.0781 -0.0023 -0.0098 -0.0005 224 SER A C 1687 O O . SER A 224 ? 0.1236 0.1016 0.0771 -0.0141 -0.0005 -0.0041 224 SER A O 1688 C CB . SER A 224 ? 0.1255 0.1044 0.1318 0.0017 -0.0329 -0.0201 224 SER A CB 1689 O OG . SER A 224 ? 0.1243 0.1018 0.0977 0.0033 -0.0208 -0.0014 224 SER A OG 1690 N N . PRO A 225 ? 0.1089 0.0974 0.0737 -0.0124 -0.0048 0.0016 225 PRO A N 1691 C CA . PRO A 225 ? 0.1033 0.1091 0.0903 -0.0163 -0.0111 -0.0041 225 PRO A CA 1692 C C . PRO A 225 ? 0.1256 0.1094 0.0808 -0.0158 -0.0114 -0.0069 225 PRO A C 1693 O O . PRO A 225 ? 0.1290 0.1287 0.0879 -0.0066 -0.0262 -0.0041 225 PRO A O 1694 C CB . PRO A 225 ? 0.1100 0.1028 0.1083 -0.0132 -0.0069 0.0047 225 PRO A CB 1695 C CG . PRO A 225 ? 0.1071 0.0973 0.0974 -0.0041 0.0007 0.0145 225 PRO A CG 1696 C CD . PRO A 225 ? 0.1224 0.1145 0.0786 -0.0130 0.0023 0.0003 225 PRO A CD 1697 N N . LEU A 226 ? 0.1196 0.1066 0.0698 -0.0106 -0.0129 0.0104 226 LEU A N 1698 C CA . LEU A 226 ? 0.1177 0.1036 0.0790 -0.0070 -0.0179 0.0062 226 LEU A CA 1699 C C . LEU A 226 ? 0.1166 0.0957 0.0700 -0.0011 -0.0206 0.0054 226 LEU A C 1700 O O . LEU A 226 ? 0.1311 0.1077 0.0681 -0.0089 -0.0117 0.0016 226 LEU A O 1701 C CB . LEU A 226 ? 0.1138 0.1352 0.0787 0.0022 -0.0166 0.0043 226 LEU A CB 1702 C CG . LEU A 226 ? 0.1153 0.1758 0.1014 -0.0037 -0.0147 -0.0023 226 LEU A CG 1703 C CD1 . LEU A 226 ? 0.1221 0.3356 0.1193 -0.0254 0.0003 -0.0192 226 LEU A CD1 1704 C CD2 . LEU A 226 ? 0.1311 0.1531 0.1265 -0.0126 -0.0345 -0.0116 226 LEU A CD2 1705 N N . PRO A 227 ? 0.1179 0.0982 0.0798 -0.0077 -0.0110 0.0063 227 PRO A N 1706 C CA . PRO A 227 ? 0.1195 0.0973 0.0899 -0.0008 -0.0153 0.0105 227 PRO A CA 1707 C C . PRO A 227 ? 0.1324 0.0991 0.0707 -0.0035 -0.0066 0.0014 227 PRO A C 1708 O O . PRO A 227 ? 0.1344 0.1092 0.0920 -0.0164 -0.0082 0.0094 227 PRO A O 1709 C CB . PRO A 227 ? 0.1265 0.1072 0.1158 -0.0027 -0.0024 0.0134 227 PRO A CB 1710 C CG . PRO A 227 ? 0.1356 0.1078 0.1072 -0.0030 0.0064 -0.0004 227 PRO A CG 1711 C CD . PRO A 227 ? 0.1280 0.0961 0.0952 -0.0002 -0.0009 -0.0022 227 PRO A CD 1712 N N . LEU A 228 ? 0.1403 0.0895 0.0765 -0.0096 -0.0114 0.0064 228 LEU A N 1713 C CA . LEU A 228 ? 0.1545 0.0986 0.0672 -0.0053 -0.0062 0.0131 228 LEU A CA 1714 C C . LEU A 228 ? 0.1517 0.0988 0.0700 0.0012 -0.0093 0.0143 228 LEU A C 1715 O O . LEU A 228 ? 0.1478 0.1072 0.0722 0.0029 0.0004 0.0111 228 LEU A O 1716 C CB . LEU A 228 ? 0.1443 0.1065 0.0859 0.0025 -0.0179 0.0027 228 LEU A CB 1717 C CG . LEU A 228 ? 0.1627 0.1247 0.0816 0.0028 -0.0024 0.0165 228 LEU A CG 1718 C CD1 . LEU A 228 ? 0.2053 0.1793 0.0766 0.0107 0.0209 0.0233 228 LEU A CD1 1719 C CD2 . LEU A 228 ? 0.1897 0.1593 0.1125 0.0244 -0.0346 0.0417 228 LEU A CD2 1720 N N . GLY A 229 ? 0.1718 0.1036 0.0818 -0.0106 0.0044 0.0060 229 GLY A N 1721 C CA . GLY A 229 ? 0.2337 0.1022 0.0781 -0.0190 -0.0087 0.0110 229 GLY A CA 1722 C C . GLY A 229 ? 0.1959 0.1071 0.0885 -0.0222 0.0087 0.0084 229 GLY A C 1723 O O . GLY A 229 ? 0.2759 0.1324 0.0836 -0.0240 0.0303 0.0050 229 GLY A O 1724 N N . SER A 230 ? 0.1861 0.1003 0.0915 -0.0111 -0.0004 0.0155 230 SER A N 1725 C CA . SER A 230 ? 0.2006 0.1185 0.0948 -0.0295 -0.0073 0.0235 230 SER A CA 1726 C C . SER A 230 ? 0.2285 0.1089 0.0948 -0.0272 0.0108 0.0229 230 SER A C 1727 O O . SER A 230 ? 0.2118 0.1277 0.0982 -0.0053 0.0062 0.0294 230 SER A O 1728 C CB . SER A 230 ? 0.2841 0.1625 0.1315 -0.0355 -0.0668 0.0531 230 SER A CB 1729 O OG . SER A 230 ? 0.4627 0.1822 0.1421 -0.0623 -0.0881 0.0680 230 SER A OG 1730 N N . GLY A 231 ? 0.2348 0.1354 0.1193 -0.0429 0.0288 0.0087 231 GLY A N 1731 C CA . GLY A 231 ? 0.2675 0.1415 0.1250 -0.0649 0.0346 0.0059 231 GLY A CA 1732 C C . GLY A 231 ? 0.2380 0.1438 0.1239 -0.0436 0.0265 -0.0014 231 GLY A C 1733 O O . GLY A 231 ? 0.2420 0.1815 0.1314 -0.0165 0.0223 -0.0133 231 GLY A O 1734 N N . SER A 232 ? 0.2597 0.1241 0.1229 -0.0462 0.0310 -0.0039 232 SER A N 1735 C CA . SER A 232 ? 0.2362 0.1367 0.1268 -0.0560 0.0255 -0.0107 232 SER A CA 1736 C C . SER A 232 ? 0.1826 0.1005 0.1117 -0.0232 -0.0060 -0.0014 232 SER A C 1737 O O . SER A 232 ? 0.1816 0.1250 0.0978 -0.0085 -0.0146 -0.0041 232 SER A O 1738 C CB A SER A 232 ? 0.4154 0.1355 0.1452 -0.0898 0.0294 -0.0404 232 SER A CB 1739 C CB B SER A 232 ? 0.2799 0.1180 0.1235 -0.0334 -0.0421 -0.0075 232 SER A CB 1740 O OG A SER A 232 ? 0.4652 0.1749 0.2616 -0.1544 0.1079 -0.0614 232 SER A OG 1741 O OG B SER A 232 ? 0.3148 0.1089 0.1049 0.0155 -0.0756 -0.0049 232 SER A OG 1742 N N . ASP A 233 ? 0.1796 0.1003 0.0910 -0.0201 -0.0101 0.0103 233 ASP A N 1743 C CA . ASP A 233 ? 0.1566 0.0964 0.0778 -0.0097 -0.0054 0.0066 233 ASP A CA 1744 C C . ASP A 233 ? 0.1706 0.0964 0.0712 -0.0021 -0.0107 0.0112 233 ASP A C 1745 O O . ASP A 233 ? 0.2158 0.1121 0.0813 0.0212 -0.0260 0.0033 233 ASP A O 1746 C CB . ASP A 233 ? 0.1604 0.1177 0.0828 -0.0072 -0.0131 0.0160 233 ASP A CB 1747 C CG . ASP A 233 ? 0.1944 0.1350 0.0971 0.0258 -0.0236 0.0104 233 ASP A CG 1748 O OD1 . ASP A 233 ? 0.2118 0.1241 0.1004 0.0113 -0.0182 0.0150 233 ASP A OD1 1749 O OD2 . ASP A 233 ? 0.2212 0.2599 0.1402 0.0677 -0.0657 -0.0288 233 ASP A OD2 1750 N N . THR A 234 ? 0.1378 0.0952 0.0789 -0.0061 -0.0110 0.0062 234 THR A N 1751 C CA . THR A 234 ? 0.1349 0.0914 0.0682 -0.0122 -0.0038 0.0110 234 THR A CA 1752 C C . THR A 234 ? 0.1277 0.0957 0.0705 -0.0070 -0.0136 0.0126 234 THR A C 1753 O O . THR A 234 ? 0.1198 0.0936 0.0892 -0.0067 -0.0039 0.0102 234 THR A O 1754 C CB . THR A 234 ? 0.1316 0.0973 0.0912 -0.0072 -0.0194 0.0108 234 THR A CB 1755 O OG1 . THR A 234 ? 0.1674 0.1068 0.1193 -0.0268 -0.0300 0.0136 234 THR A OG1 1756 C CG2 . THR A 234 ? 0.1190 0.1211 0.0843 -0.0018 -0.0021 0.0044 234 THR A CG2 1757 N N . GLY A 235 ? 0.1301 0.0917 0.0712 -0.0075 -0.0057 0.0145 235 GLY A N 1758 C CA . GLY A 235 ? 0.1462 0.0922 0.0719 -0.0011 -0.0090 0.0115 235 GLY A CA 1759 C C . GLY A 235 ? 0.1109 0.0809 0.0671 0.0010 -0.0065 0.0011 235 GLY A C 1760 O O . GLY A 235 ? 0.1145 0.0918 0.0713 -0.0100 -0.0083 0.0098 235 GLY A O 1761 N N . GLU A 236 ? 0.1064 0.0882 0.0624 -0.0046 -0.0080 0.0073 236 GLU A N 1762 C CA . GLU A 236 ? 0.1012 0.0817 0.0683 -0.0050 -0.0071 0.0042 236 GLU A CA 1763 C C . GLU A 236 ? 0.1033 0.0773 0.0728 -0.0108 -0.0114 0.0039 236 GLU A C 1764 O O . GLU A 236 ? 0.1032 0.0944 0.0721 -0.0065 -0.0007 -0.0013 236 GLU A O 1765 C CB . GLU A 236 ? 0.1007 0.0966 0.0697 -0.0061 -0.0134 0.0063 236 GLU A CB 1766 C CG . GLU A 236 ? 0.1013 0.0914 0.0711 -0.0051 -0.0096 0.0053 236 GLU A CG 1767 C CD . GLU A 236 ? 0.1063 0.0833 0.0749 -0.0038 -0.0201 0.0013 236 GLU A CD 1768 O OE1 . GLU A 236 ? 0.1117 0.0950 0.1056 -0.0029 -0.0199 -0.0015 236 GLU A OE1 1769 O OE2 . GLU A 236 ? 0.1010 0.0931 0.1027 0.0025 -0.0158 0.0002 236 GLU A OE2 1770 N N . MET A 237 ? 0.0961 0.0787 0.0689 0.0008 -0.0066 0.0055 237 MET A N 1771 C CA . MET A 237 ? 0.0927 0.0790 0.0768 -0.0044 -0.0064 0.0031 237 MET A CA 1772 C C . MET A 237 ? 0.0853 0.0735 0.0738 -0.0130 -0.0095 -0.0007 237 MET A C 1773 O O . MET A 237 ? 0.0939 0.0789 0.0813 -0.0030 0.0004 0.0065 237 MET A O 1774 C CB . MET A 237 ? 0.0951 0.0827 0.0887 -0.0109 -0.0121 0.0090 237 MET A CB 1775 C CG . MET A 237 ? 0.0961 0.1056 0.0993 -0.0042 -0.0117 -0.0008 237 MET A CG 1776 S SD . MET A 237 ? 0.1025 0.1297 0.1099 -0.0126 -0.0190 -0.0120 237 MET A SD 1777 C CE . MET A 237 ? 0.1284 0.1161 0.1258 -0.0118 -0.0154 -0.0014 237 MET A CE 1778 N N . ARG A 238 ? 0.0848 0.0821 0.0779 0.0020 -0.0032 0.0126 238 ARG A N 1779 C CA . ARG A 238 ? 0.0879 0.0729 0.0750 -0.0011 -0.0094 0.0047 238 ARG A CA 1780 C C . ARG A 238 ? 0.0905 0.0762 0.0748 -0.0082 -0.0063 0.0015 238 ARG A C 1781 O O . ARG A 238 ? 0.0882 0.1012 0.0820 0.0052 -0.0032 0.0000 238 ARG A O 1782 C CB . ARG A 238 ? 0.0978 0.0795 0.0754 -0.0006 -0.0059 -0.0008 238 ARG A CB 1783 C CG . ARG A 238 ? 0.0919 0.0792 0.0865 -0.0095 -0.0174 -0.0005 238 ARG A CG 1784 C CD . ARG A 238 ? 0.1144 0.0850 0.1023 -0.0060 -0.0276 0.0037 238 ARG A CD 1785 N NE . ARG A 238 ? 0.0924 0.0834 0.0938 -0.0085 -0.0139 -0.0030 238 ARG A NE 1786 C CZ . ARG A 238 ? 0.0958 0.0804 0.0858 -0.0091 -0.0081 -0.0032 238 ARG A CZ 1787 N NH1 . ARG A 238 ? 0.1025 0.0813 0.1064 -0.0015 -0.0206 -0.0099 238 ARG A NH1 1788 N NH2 . ARG A 238 ? 0.0972 0.0955 0.0881 -0.0087 -0.0166 -0.0049 238 ARG A NH2 1789 N N . LEU A 239 ? 0.0762 0.0837 0.0757 -0.0015 -0.0074 0.0035 239 LEU A N 1790 C CA . LEU A 239 ? 0.0821 0.0860 0.0762 -0.0069 -0.0047 0.0057 239 LEU A CA 1791 C C . LEU A 239 ? 0.0824 0.0894 0.0744 -0.0006 -0.0137 0.0000 239 LEU A C 1792 O O . LEU A 239 ? 0.0881 0.0832 0.0988 -0.0032 -0.0196 0.0054 239 LEU A O 1793 C CB . LEU A 239 ? 0.0931 0.0832 0.0756 -0.0073 -0.0152 -0.0001 239 LEU A CB 1794 C CG . LEU A 239 ? 0.0994 0.0896 0.0873 0.0018 -0.0215 0.0032 239 LEU A CG 1795 C CD1 . LEU A 239 ? 0.1355 0.1079 0.0896 0.0120 -0.0270 -0.0181 239 LEU A CD1 1796 C CD2 . LEU A 239 ? 0.1019 0.0875 0.1276 -0.0088 -0.0192 -0.0018 239 LEU A CD2 1797 N N . GLN A 240 ? 0.0849 0.0855 0.0911 -0.0058 -0.0117 0.0014 240 GLN A N 1798 C CA . GLN A 240 ? 0.0891 0.0949 0.0858 0.0074 -0.0191 -0.0065 240 GLN A CA 1799 C C . GLN A 240 ? 0.0855 0.0789 0.0935 0.0004 -0.0179 -0.0041 240 GLN A C 1800 O O . GLN A 240 ? 0.0919 0.0825 0.1158 0.0011 -0.0194 -0.0067 240 GLN A O 1801 C CB . GLN A 240 ? 0.0921 0.1012 0.0923 0.0055 -0.0066 -0.0022 240 GLN A CB 1802 C CG . GLN A 240 ? 0.1175 0.1097 0.1224 0.0230 -0.0091 -0.0140 240 GLN A CG 1803 C CD . GLN A 240 ? 0.1272 0.0992 0.1341 0.0159 -0.0167 -0.0067 240 GLN A CD 1804 O OE1 . GLN A 240 ? 0.1566 0.1119 0.1336 0.0114 -0.0149 -0.0083 240 GLN A OE1 1805 N NE2 . GLN A 240 ? 0.1129 0.0960 0.1510 0.0158 -0.0273 -0.0090 240 GLN A NE2 1806 N N . SER A 241 ? 0.0821 0.0788 0.0947 -0.0050 -0.0142 0.0038 241 SER A N 1807 C CA . SER A 241 ? 0.0957 0.0824 0.0896 -0.0047 -0.0189 0.0049 241 SER A CA 1808 C C . SER A 241 ? 0.0950 0.0762 0.0884 -0.0052 -0.0223 -0.0008 241 SER A C 1809 O O . SER A 241 ? 0.0956 0.0835 0.0996 -0.0047 -0.0152 0.0085 241 SER A O 1810 C CB . SER A 241 ? 0.0945 0.0985 0.0910 -0.0090 -0.0277 0.0018 241 SER A CB 1811 O OG . SER A 241 ? 0.1115 0.0862 0.0949 -0.0048 -0.0185 0.0001 241 SER A OG 1812 N N . ASP A 242 ? 0.0901 0.0761 0.0963 0.0003 -0.0221 0.0066 242 ASP A N 1813 C CA . ASP A 242 ? 0.0850 0.0750 0.1012 -0.0010 -0.0252 -0.0007 242 ASP A CA 1814 C C . ASP A 242 ? 0.0884 0.0755 0.0979 0.0062 -0.0192 0.0022 242 ASP A C 1815 O O . ASP A 242 ? 0.0903 0.0750 0.1050 -0.0085 -0.0199 0.0038 242 ASP A O 1816 C CB . ASP A 242 ? 0.1087 0.0761 0.1033 0.0067 -0.0241 0.0018 242 ASP A CB 1817 C CG . ASP A 242 ? 0.1272 0.0767 0.1009 0.0020 -0.0218 -0.0008 242 ASP A CG 1818 O OD1 . ASP A 242 ? 0.1349 0.0905 0.1086 0.0035 -0.0234 -0.0046 242 ASP A OD1 1819 O OD2 . ASP A 242 ? 0.1609 0.1018 0.0991 0.0066 -0.0270 0.0051 242 ASP A OD2 1820 N N . PHE A 243 ? 0.0918 0.0687 0.0932 -0.0048 -0.0197 0.0014 243 PHE A N 1821 C CA . PHE A 243 ? 0.0977 0.0752 0.0909 0.0006 -0.0204 -0.0016 243 PHE A CA 1822 C C . PHE A 243 ? 0.0915 0.0728 0.0847 -0.0037 -0.0158 -0.0044 243 PHE A C 1823 O O . PHE A 243 ? 0.1110 0.0790 0.0960 -0.0083 -0.0204 -0.0014 243 PHE A O 1824 C CB . PHE A 243 ? 0.1035 0.0886 0.0917 -0.0098 -0.0192 0.0027 243 PHE A CB 1825 C CG . PHE A 243 ? 0.1093 0.0994 0.0979 -0.0075 -0.0076 -0.0046 243 PHE A CG 1826 C CD1 . PHE A 243 ? 0.1518 0.1334 0.1373 0.0242 -0.0284 -0.0306 243 PHE A CD1 1827 C CD2 . PHE A 243 ? 0.1422 0.0950 0.1062 -0.0232 -0.0216 0.0020 243 PHE A CD2 1828 C CE1 . PHE A 243 ? 0.1825 0.1691 0.1853 0.0455 -0.0138 -0.0629 243 PHE A CE1 1829 C CE2 . PHE A 243 ? 0.1784 0.1180 0.1083 -0.0308 -0.0185 -0.0094 243 PHE A CE2 1830 C CZ . PHE A 243 ? 0.2027 0.1477 0.1426 -0.0024 -0.0103 -0.0453 243 PHE A CZ 1831 N N . ALA A 244 ? 0.1015 0.0731 0.0934 -0.0084 -0.0177 0.0038 244 ALA A N 1832 C CA . ALA A 244 ? 0.0979 0.0759 0.1018 0.0054 -0.0178 -0.0015 244 ALA A CA 1833 C C . ALA A 244 ? 0.0934 0.0671 0.0936 0.0069 -0.0243 -0.0002 244 ALA A C 1834 O O . ALA A 244 ? 0.1050 0.0702 0.1103 0.0001 -0.0153 0.0026 244 ALA A O 1835 C CB . ALA A 244 ? 0.0929 0.0929 0.1169 0.0108 -0.0136 0.0170 244 ALA A CB 1836 N N . LEU A 245 ? 0.0982 0.0711 0.0892 -0.0043 -0.0152 0.0040 245 LEU A N 1837 C CA . LEU A 245 ? 0.0926 0.0730 0.0890 0.0016 -0.0172 0.0035 245 LEU A CA 1838 C C . LEU A 245 ? 0.0967 0.0768 0.0933 -0.0051 -0.0137 0.0061 245 LEU A C 1839 O O . LEU A 245 ? 0.1006 0.1023 0.1020 -0.0147 -0.0221 0.0154 245 LEU A O 1840 C CB . LEU A 245 ? 0.1035 0.0804 0.1021 -0.0009 -0.0128 0.0032 245 LEU A CB 1841 C CG . LEU A 245 ? 0.1164 0.0777 0.1050 -0.0127 -0.0222 -0.0006 245 LEU A CG 1842 C CD1 . LEU A 245 ? 0.1566 0.0930 0.1245 -0.0175 -0.0169 -0.0088 245 LEU A CD1 1843 C CD2 . LEU A 245 ? 0.1358 0.0968 0.1008 -0.0099 -0.0203 -0.0015 245 LEU A CD2 1844 N N . ALA A 246 ? 0.0908 0.0776 0.0910 -0.0058 -0.0154 0.0083 246 ALA A N 1845 C CA . ALA A 246 ? 0.0847 0.0833 0.0980 0.0011 -0.0143 0.0089 246 ALA A CA 1846 C C . ALA A 246 ? 0.0965 0.0875 0.0982 -0.0061 -0.0304 0.0081 246 ALA A C 1847 O O . ALA A 246 ? 0.1016 0.0953 0.1371 -0.0089 -0.0262 0.0050 246 ALA A O 1848 C CB . ALA A 246 ? 0.0996 0.0800 0.1089 -0.0037 -0.0255 0.0146 246 ALA A CB 1849 N N . HIS A 247 ? 0.1017 0.0775 0.0905 -0.0024 -0.0262 -0.0031 247 HIS A N 1850 C CA . HIS A 247 ? 0.1198 0.0738 0.1011 -0.0060 -0.0291 0.0005 247 HIS A CA 1851 C C . HIS A 247 ? 0.1205 0.0790 0.1051 -0.0068 -0.0298 -0.0014 247 HIS A C 1852 O O . HIS A 247 ? 0.2305 0.0723 0.1238 -0.0096 -0.0603 -0.0011 247 HIS A O 1853 C CB . HIS A 247 ? 0.1336 0.0941 0.0963 0.0036 -0.0259 -0.0015 247 HIS A CB 1854 C CG . HIS A 247 ? 0.1237 0.0967 0.1059 -0.0048 -0.0337 -0.0008 247 HIS A CG 1855 N ND1 . HIS A 247 ? 0.1514 0.1079 0.1252 -0.0200 -0.0546 0.0031 247 HIS A ND1 1856 C CD2 . HIS A 247 ? 0.1327 0.0924 0.0970 -0.0086 -0.0342 -0.0032 247 HIS A CD2 1857 C CE1 . HIS A 247 ? 0.1483 0.1251 0.1056 -0.0034 -0.0513 0.0094 247 HIS A CE1 1858 N NE2 . HIS A 247 ? 0.1447 0.0971 0.1063 -0.0041 -0.0394 -0.0041 247 HIS A NE2 1859 N N . ASP A 248 ? 0.1098 0.0653 0.1080 -0.0057 -0.0348 0.0030 248 ASP A N 1860 C CA . ASP A 248 ? 0.1097 0.0673 0.1035 0.0019 -0.0271 0.0048 248 ASP A CA 1861 C C . ASP A 248 ? 0.1144 0.0589 0.1061 -0.0014 -0.0239 0.0009 248 ASP A C 1862 O O . ASP A 248 ? 0.1072 0.0697 0.1183 0.0033 -0.0256 0.0096 248 ASP A O 1863 C CB . ASP A 248 ? 0.1101 0.0734 0.0998 -0.0047 -0.0260 -0.0005 248 ASP A CB 1864 C CG . ASP A 248 ? 0.1052 0.0790 0.1002 -0.0074 -0.0232 0.0003 248 ASP A CG 1865 O OD1 . ASP A 248 ? 0.1086 0.0956 0.1149 -0.0039 -0.0267 0.0188 248 ASP A OD1 1866 O OD2 . ASP A 248 ? 0.1108 0.0866 0.1206 0.0029 -0.0205 0.0090 248 ASP A OD2 1867 N N . PRO A 249 ? 0.1267 0.0622 0.1311 -0.0018 -0.0305 0.0086 249 PRO A N 1868 C CA . PRO A 249 ? 0.1390 0.0709 0.1394 -0.0182 -0.0267 0.0006 249 PRO A CA 1869 C C . PRO A 249 ? 0.1161 0.0633 0.1357 -0.0008 -0.0317 0.0175 249 PRO A C 1870 O O . PRO A 249 ? 0.1144 0.0855 0.1436 -0.0138 -0.0332 0.0137 249 PRO A O 1871 C CB . PRO A 249 ? 0.2331 0.0581 0.1787 -0.0107 0.0038 0.0003 249 PRO A CB 1872 C CG . PRO A 249 ? 0.2030 0.0725 0.1918 0.0123 0.0020 0.0059 249 PRO A CG 1873 C CD . PRO A 249 ? 0.1714 0.0615 0.1305 0.0220 -0.0113 -0.0020 249 PRO A CD 1874 N N . ARG A 250 ? 0.1093 0.0692 0.1165 -0.0015 -0.0306 0.0112 250 ARG A N 1875 C CA . ARG A 250 ? 0.1159 0.0711 0.1101 0.0036 -0.0208 0.0181 250 ARG A CA 1876 C C . ARG A 250 ? 0.1120 0.0796 0.1141 0.0069 -0.0199 0.0231 250 ARG A C 1877 O O . ARG A 250 ? 0.1422 0.1398 0.1293 0.0396 0.0165 0.0507 250 ARG A O 1878 C CB . ARG A 250 ? 0.1109 0.0718 0.1135 0.0022 -0.0211 0.0159 250 ARG A CB 1879 C CG . ARG A 250 ? 0.1140 0.0732 0.1372 -0.0022 -0.0293 0.0230 250 ARG A CG 1880 C CD . ARG A 250 ? 0.1160 0.0773 0.1168 -0.0002 -0.0299 0.0216 250 ARG A CD 1881 N NE . ARG A 250 ? 0.1073 0.0777 0.1169 -0.0009 -0.0305 0.0150 250 ARG A NE 1882 C CZ . ARG A 250 ? 0.1091 0.0645 0.1158 0.0039 -0.0281 0.0016 250 ARG A CZ 1883 N NH1 . ARG A 250 ? 0.1176 0.0794 0.1203 0.0020 -0.0365 0.0039 250 ARG A NH1 1884 N NH2 . ARG A 250 ? 0.1123 0.0882 0.1134 0.0108 -0.0249 -0.0001 250 ARG A NH2 1885 N N . THR A 251 ? 0.1058 0.0647 0.1021 0.0000 -0.0237 0.0101 251 THR A N 1886 C CA . THR A 251 ? 0.1010 0.0672 0.1011 0.0048 -0.0163 0.0085 251 THR A CA 1887 C C . THR A 251 ? 0.1012 0.0652 0.1110 -0.0051 -0.0240 0.0163 251 THR A C 1888 O O . THR A 251 ? 0.1030 0.0756 0.1090 0.0006 -0.0201 0.0123 251 THR A O 1889 C CB . THR A 251 ? 0.1054 0.0702 0.0937 0.0040 -0.0193 0.0099 251 THR A CB 1890 O OG1 . THR A 251 ? 0.0971 0.0765 0.1040 -0.0032 -0.0177 0.0117 251 THR A OG1 1891 C CG2 . THR A 251 ? 0.1339 0.0955 0.1021 -0.0048 -0.0346 0.0038 251 THR A CG2 1892 N N . ALA A 252 ? 0.1048 0.0726 0.1035 0.0088 -0.0245 0.0116 252 ALA A N 1893 C CA . ALA A 252 ? 0.1089 0.0795 0.1078 0.0002 -0.0273 0.0089 252 ALA A CA 1894 C C . ALA A 252 ? 0.1123 0.0708 0.1065 -0.0037 -0.0246 0.0031 252 ALA A C 1895 O O . ALA A 252 ? 0.1151 0.0823 0.1100 0.0094 -0.0333 0.0121 252 ALA A O 1896 C CB . ALA A 252 ? 0.1394 0.0994 0.1088 0.0104 -0.0217 0.0000 252 ALA A CB 1897 N N . CYS A 253 ? 0.1108 0.0773 0.1278 0.0024 -0.0208 0.0137 253 CYS A N 1898 C CA . CYS A 253 ? 0.1099 0.0663 0.1727 -0.0158 -0.0291 0.0010 253 CYS A CA 1899 C C . CYS A 253 ? 0.1059 0.0866 0.1098 -0.0161 -0.0235 0.0085 253 CYS A C 1900 O O . CYS A 253 ? 0.1047 0.0890 0.1453 -0.0053 -0.0268 0.0101 253 CYS A O 1901 C CB . CYS A 253 ? 0.1416 0.0895 0.2105 -0.0217 0.0327 -0.0071 253 CYS A CB 1902 S SG A CYS A 253 ? 0.1637 0.0587 0.1923 -0.0330 -0.0253 -0.0007 253 CYS A SG 1903 S SG B CYS A 253 ? 0.8518 0.2247 0.2609 -0.1306 -0.1500 0.0765 253 CYS A SG 1904 N N . ILE A 254 ? 0.0976 0.0841 0.1132 0.0005 -0.0191 0.0131 254 ILE A N 1905 C CA . ILE A 254 ? 0.1052 0.0861 0.1027 -0.0108 -0.0191 0.0097 254 ILE A CA 1906 C C . ILE A 254 ? 0.0951 0.0894 0.0989 -0.0046 -0.0152 0.0048 254 ILE A C 1907 O O . ILE A 254 ? 0.1079 0.0921 0.1031 0.0032 -0.0173 0.0048 254 ILE A O 1908 C CB . ILE A 254 ? 0.1082 0.1062 0.1084 -0.0111 -0.0200 0.0118 254 ILE A CB 1909 C CG1 . ILE A 254 ? 0.1536 0.1129 0.1007 0.0070 -0.0124 0.0251 254 ILE A CG1 1910 C CG2 . ILE A 254 ? 0.1429 0.1044 0.0995 -0.0269 -0.0298 0.0145 254 ILE A CG2 1911 C CD1 . ILE A 254 ? 0.1886 0.1503 0.1111 0.0445 -0.0266 0.0097 254 ILE A CD1 1912 N N . TRP A 255 ? 0.0945 0.0760 0.1026 0.0027 -0.0213 0.0093 255 TRP A N 1913 C CA . TRP A 255 ? 0.0967 0.0722 0.0926 -0.0009 -0.0220 0.0086 255 TRP A CA 1914 C C . TRP A 255 ? 0.0912 0.0819 0.0938 -0.0039 -0.0218 0.0092 255 TRP A C 1915 O O . TRP A 255 ? 0.0942 0.0713 0.1119 0.0036 -0.0220 0.0084 255 TRP A O 1916 C CB . TRP A 255 ? 0.0851 0.0745 0.0996 0.0024 -0.0223 0.0064 255 TRP A CB 1917 C CG . TRP A 255 ? 0.0861 0.0756 0.0894 0.0063 -0.0172 0.0064 255 TRP A CG 1918 C CD1 . TRP A 255 ? 0.1016 0.0715 0.0978 0.0050 -0.0298 0.0003 255 TRP A CD1 1919 C CD2 . TRP A 255 ? 0.0993 0.0705 0.0970 0.0000 -0.0223 0.0011 255 TRP A CD2 1920 N NE1 . TRP A 255 ? 0.1086 0.0688 0.0882 0.0069 -0.0192 0.0039 255 TRP A NE1 1921 C CE2 . TRP A 255 ? 0.0978 0.0714 0.0858 0.0029 -0.0170 0.0031 255 TRP A CE2 1922 C CE3 . TRP A 255 ? 0.0906 0.0915 0.0922 0.0010 -0.0192 -0.0033 255 TRP A CE3 1923 C CZ2 . TRP A 255 ? 0.1179 0.0833 0.0863 -0.0095 -0.0042 -0.0044 255 TRP A CZ2 1924 C CZ3 . TRP A 255 ? 0.0989 0.1176 0.0999 -0.0223 -0.0196 -0.0054 255 TRP A CZ3 1925 C CH2 . TRP A 255 ? 0.1163 0.0997 0.1082 -0.0236 -0.0039 -0.0105 255 TRP A CH2 1926 N N . GLN A 256 ? 0.1008 0.0708 0.1085 0.0013 -0.0298 0.0039 256 GLN A N 1927 C CA . GLN A 256 ? 0.0935 0.0756 0.1109 -0.0033 -0.0338 -0.0004 256 GLN A CA 1928 C C . GLN A 256 ? 0.1067 0.0780 0.1073 -0.0089 -0.0259 -0.0055 256 GLN A C 1929 O O . GLN A 256 ? 0.0992 0.0900 0.1178 0.0009 -0.0366 0.0033 256 GLN A O 1930 C CB . GLN A 256 ? 0.1062 0.0928 0.1110 -0.0009 -0.0295 -0.0081 256 GLN A CB 1931 C CG . GLN A 256 ? 0.1261 0.1026 0.1349 -0.0045 -0.0551 -0.0092 256 GLN A CG 1932 C CD . GLN A 256 ? 0.1341 0.1169 0.1267 -0.0150 -0.0351 -0.0232 256 GLN A CD 1933 O OE1 . GLN A 256 ? 0.1473 0.1130 0.1439 -0.0179 -0.0281 -0.0203 256 GLN A OE1 1934 N NE2 . GLN A 256 ? 0.1494 0.1447 0.2257 -0.0390 -0.0117 -0.0448 256 GLN A NE2 1935 N N . GLY A 257 ? 0.0966 0.0869 0.1156 -0.0046 -0.0266 0.0076 257 GLY A N 1936 C CA . GLY A 257 ? 0.0918 0.0879 0.1238 -0.0111 -0.0172 0.0122 257 GLY A CA 1937 C C . GLY A 257 ? 0.0915 0.0925 0.1051 -0.0131 -0.0189 0.0040 257 GLY A C 1938 O O . GLY A 257 ? 0.0860 0.1046 0.1479 -0.0134 -0.0022 0.0079 257 GLY A O 1939 N N . PHE A 258 ? 0.0810 0.0865 0.0990 -0.0069 -0.0211 0.0047 258 PHE A N 1940 C CA . PHE A 258 ? 0.0817 0.0844 0.0956 -0.0060 -0.0173 0.0033 258 PHE A CA 1941 C C . PHE A 258 ? 0.0887 0.0831 0.0950 -0.0080 -0.0256 0.0070 258 PHE A C 1942 O O . PHE A 258 ? 0.1092 0.0889 0.1011 0.0005 -0.0271 -0.0001 258 PHE A O 1943 C CB . PHE A 258 ? 0.0873 0.0856 0.0894 -0.0019 -0.0284 0.0029 258 PHE A CB 1944 C CG . PHE A 258 ? 0.0859 0.0833 0.0907 -0.0041 -0.0168 0.0051 258 PHE A CG 1945 C CD1 . PHE A 258 ? 0.0892 0.1006 0.0995 -0.0123 -0.0190 0.0090 258 PHE A CD1 1946 C CD2 . PHE A 258 ? 0.0916 0.0987 0.0983 -0.0002 -0.0163 0.0072 258 PHE A CD2 1947 C CE1 . PHE A 258 ? 0.1047 0.1161 0.1018 0.0039 -0.0327 -0.0001 258 PHE A CE1 1948 C CE2 . PHE A 258 ? 0.1023 0.1066 0.1003 -0.0111 -0.0081 0.0093 258 PHE A CE2 1949 C CZ . PHE A 258 ? 0.1187 0.0967 0.0961 -0.0013 -0.0268 0.0037 258 PHE A CZ 1950 N N . VAL A 259 ? 0.0857 0.0868 0.0970 0.0024 -0.0237 0.0010 259 VAL A N 1951 C CA . VAL A 259 ? 0.0928 0.0845 0.0919 -0.0027 -0.0274 -0.0010 259 VAL A CA 1952 C C . VAL A 259 ? 0.0868 0.0936 0.1001 -0.0048 -0.0290 0.0040 259 VAL A C 1953 O O . VAL A 259 ? 0.0961 0.0885 0.1187 -0.0100 -0.0256 0.0064 259 VAL A O 1954 C CB . VAL A 259 ? 0.0926 0.0886 0.1004 -0.0093 -0.0206 -0.0004 259 VAL A CB 1955 C CG1 . VAL A 259 ? 0.1163 0.1106 0.0993 -0.0024 -0.0264 0.0010 259 VAL A CG1 1956 C CG2 . VAL A 259 ? 0.0877 0.1100 0.1135 -0.0074 -0.0191 -0.0025 259 VAL A CG2 1957 N N . ASN A 260 ? 0.0934 0.0849 0.1034 -0.0073 -0.0324 0.0076 260 ASN A N 1958 C CA . ASN A 260 ? 0.0901 0.0971 0.1067 0.0040 -0.0291 0.0051 260 ASN A CA 1959 C C . ASN A 260 ? 0.0914 0.0973 0.1088 -0.0019 -0.0304 0.0026 260 ASN A C 1960 O O . ASN A 260 ? 0.0841 0.1563 0.1241 -0.0169 -0.0301 0.0026 260 ASN A O 1961 C CB . ASN A 260 ? 0.1011 0.1156 0.1083 -0.0053 -0.0355 0.0038 260 ASN A CB 1962 C CG . ASN A 260 ? 0.0918 0.1404 0.1206 -0.0057 -0.0331 0.0165 260 ASN A CG 1963 O OD1 . ASN A 260 ? 0.0991 0.1436 0.1539 0.0092 -0.0232 0.0325 260 ASN A OD1 1964 N ND2 . ASN A 260 ? 0.0892 0.2141 0.1449 -0.0274 -0.0383 0.0023 260 ASN A ND2 1965 N N . GLU A 261 ? 0.0886 0.1073 0.1087 -0.0090 -0.0236 0.0022 261 GLU A N 1966 C CA . GLU A 261 ? 0.0916 0.1146 0.1122 -0.0166 -0.0204 0.0005 261 GLU A CA 1967 C C . GLU A 261 ? 0.0882 0.1251 0.0996 -0.0057 -0.0222 0.0033 261 GLU A C 1968 O O . GLU A 261 ? 0.0938 0.1328 0.0998 -0.0029 -0.0297 -0.0003 261 GLU A O 1969 C CB . GLU A 261 ? 0.1018 0.1259 0.1170 -0.0112 -0.0223 0.0066 261 GLU A CB 1970 C CG . GLU A 261 ? 0.1428 0.1157 0.1413 -0.0186 -0.0329 0.0125 261 GLU A CG 1971 C CD . GLU A 261 ? 0.1428 0.1710 0.2183 -0.0556 -0.0230 -0.0231 261 GLU A CD 1972 O OE1 . GLU A 261 ? 0.1984 0.3072 0.4841 -0.0879 -0.0389 -0.1879 261 GLU A OE1 1973 O OE2 . GLU A 261 ? 0.1674 0.2292 0.2593 -0.0633 0.0270 -0.0461 261 GLU A OE2 1974 N N . GLN A 262 ? 0.1085 0.1159 0.1110 -0.0039 -0.0436 -0.0057 262 GLN A N 1975 C CA . GLN A 262 ? 0.1365 0.1180 0.1103 -0.0092 -0.0358 0.0015 262 GLN A CA 1976 C C . GLN A 262 ? 0.1070 0.1234 0.1070 0.0135 -0.0360 -0.0082 262 GLN A C 1977 O O . GLN A 262 ? 0.0992 0.1232 0.1136 0.0053 -0.0274 -0.0092 262 GLN A O 1978 C CB A GLN A 262 ? 0.1015 0.1066 0.1106 -0.0136 -0.0243 0.0000 262 GLN A CB 1979 C CB B GLN A 262 ? 0.2623 0.1323 0.1499 -0.0399 -0.0866 0.0304 262 GLN A CB 1980 C CG A GLN A 262 ? 0.0744 0.1070 0.0866 -0.0042 -0.0149 -0.0061 262 GLN A CG 1981 C CG B GLN A 262 ? 0.1937 0.1444 0.1640 -0.0207 -0.0255 0.0349 262 GLN A CG 1982 C CD A GLN A 262 ? 0.0743 0.0968 0.0953 0.0026 -0.0169 -0.0097 262 GLN A CD 1983 C CD B GLN A 262 ? 0.1296 0.1545 0.2685 -0.0062 -0.0105 -0.0559 262 GLN A CD 1984 O OE1 A GLN A 262 ? 0.0864 0.1140 0.1077 -0.0061 -0.0064 -0.0106 262 GLN A OE1 1985 O OE1 B GLN A 262 ? 0.1380 0.2086 0.2231 -0.0107 -0.0131 0.0065 262 GLN A OE1 1986 N NE2 A GLN A 262 ? 0.0698 0.0842 0.1285 -0.0022 -0.0204 -0.0107 262 GLN A NE2 1987 N NE2 B GLN A 262 ? 0.2160 0.2728 0.3030 -0.1161 0.0246 -0.0908 262 GLN A NE2 1988 N N . ALA A 263 ? 0.0965 0.1704 0.1257 0.0137 -0.0373 -0.0056 263 ALA A N 1989 C CA . ALA A 263 ? 0.0985 0.1657 0.1307 0.0272 -0.0178 -0.0077 263 ALA A CA 1990 C C . ALA A 263 ? 0.0814 0.1508 0.1152 0.0004 -0.0064 -0.0012 263 ALA A C 1991 O O . ALA A 263 ? 0.0912 0.1564 0.1169 0.0032 -0.0161 -0.0093 263 ALA A O 1992 C CB . ALA A 263 ? 0.0910 0.2648 0.1905 0.0188 -0.0172 -0.0053 263 ALA A CB 1993 N N . PHE A 264 ? 0.0789 0.1451 0.1122 -0.0013 -0.0163 -0.0003 264 PHE A N 1994 C CA . PHE A 264 ? 0.0788 0.1343 0.1057 -0.0098 -0.0136 0.0064 264 PHE A CA 1995 C C . PHE A 264 ? 0.0759 0.1097 0.0949 -0.0039 -0.0118 0.0048 264 PHE A C 1996 O O . PHE A 264 ? 0.0871 0.1182 0.0970 -0.0089 -0.0126 0.0045 264 PHE A O 1997 C CB . PHE A 264 ? 0.0930 0.1352 0.1214 -0.0200 -0.0162 0.0018 264 PHE A CB 1998 C CG . PHE A 264 ? 0.0825 0.1287 0.1273 -0.0172 -0.0105 0.0057 264 PHE A CG 1999 C CD1 . PHE A 264 ? 0.1083 0.1307 0.1358 -0.0217 -0.0199 0.0045 264 PHE A CD1 2000 C CD2 . PHE A 264 ? 0.0928 0.1499 0.1460 -0.0151 -0.0109 -0.0023 264 PHE A CD2 2001 C CE1 . PHE A 264 ? 0.1294 0.1405 0.1719 -0.0176 -0.0367 0.0173 264 PHE A CE1 2002 C CE2 . PHE A 264 ? 0.1083 0.1503 0.1836 -0.0055 -0.0030 0.0067 264 PHE A CE2 2003 C CZ . PHE A 264 ? 0.1138 0.1395 0.1890 -0.0102 -0.0340 0.0093 264 PHE A CZ 2004 N N . MET A 265 ? 0.0729 0.1165 0.0977 -0.0097 -0.0135 -0.0025 265 MET A N 2005 C CA . MET A 265 ? 0.0774 0.1113 0.0883 -0.0087 -0.0135 0.0039 265 MET A CA 2006 C C . MET A 265 ? 0.0785 0.1028 0.0883 -0.0092 -0.0136 0.0041 265 MET A C 2007 O O . MET A 265 ? 0.0814 0.1113 0.0891 -0.0035 -0.0162 0.0014 265 MET A O 2008 C CB . MET A 265 ? 0.0811 0.1175 0.0871 -0.0114 -0.0172 0.0057 265 MET A CB 2009 C CG . MET A 265 ? 0.0817 0.1184 0.0932 -0.0124 -0.0142 0.0045 265 MET A CG 2010 S SD . MET A 265 ? 0.0977 0.1180 0.0952 -0.0095 -0.0169 0.0073 265 MET A SD 2011 C CE . MET A 265 ? 0.1840 0.0972 0.1266 -0.0140 0.0133 0.0011 265 MET A CE 2012 N N . ALA A 266 ? 0.0906 0.1085 0.0950 0.0002 -0.0210 -0.0010 266 ALA A N 2013 C CA . ALA A 266 ? 0.0832 0.1034 0.0993 0.0032 -0.0118 0.0009 266 ALA A CA 2014 C C . ALA A 266 ? 0.0808 0.1037 0.0970 0.0046 -0.0122 -0.0021 266 ALA A C 2015 O O . ALA A 266 ? 0.0888 0.1130 0.0943 -0.0049 -0.0132 -0.0087 266 ALA A O 2016 C CB . ALA A 266 ? 0.1286 0.1079 0.1185 0.0184 -0.0292 -0.0003 266 ALA A CB 2017 N N . ALA A 267 ? 0.0782 0.1283 0.0875 0.0013 -0.0084 -0.0072 267 ALA A N 2018 C CA . ALA A 267 ? 0.0798 0.1225 0.0994 -0.0012 0.0018 -0.0020 267 ALA A CA 2019 C C . ALA A 267 ? 0.0850 0.1132 0.0937 -0.0100 -0.0041 -0.0038 267 ALA A C 2020 O O . ALA A 267 ? 0.0870 0.1177 0.0913 -0.0149 -0.0044 -0.0032 267 ALA A O 2021 C CB . ALA A 267 ? 0.0832 0.1550 0.1216 -0.0146 0.0002 -0.0053 267 ALA A CB 2022 N N . SER A 268 ? 0.0788 0.1070 0.0917 -0.0070 -0.0055 -0.0022 268 SER A N 2023 C CA . SER A 268 ? 0.0842 0.0967 0.0923 -0.0179 -0.0111 0.0006 268 SER A CA 2024 C C . SER A 268 ? 0.0782 0.0930 0.0789 -0.0036 -0.0059 -0.0037 268 SER A C 2025 O O . SER A 268 ? 0.0845 0.0982 0.0878 -0.0037 -0.0122 0.0084 268 SER A O 2026 C CB . SER A 268 ? 0.0780 0.0981 0.1087 -0.0104 -0.0132 0.0003 268 SER A CB 2027 O OG . SER A 268 ? 0.0870 0.1061 0.1036 -0.0228 -0.0157 0.0026 268 SER A OG 2028 N N . PHE A 269 ? 0.0778 0.0957 0.0877 -0.0067 -0.0146 0.0050 269 PHE A N 2029 C CA . PHE A 269 ? 0.0842 0.0991 0.0818 -0.0086 -0.0110 0.0018 269 PHE A CA 2030 C C . PHE A 269 ? 0.0837 0.0989 0.0727 -0.0087 -0.0105 0.0047 269 PHE A C 2031 O O . PHE A 269 ? 0.0824 0.1122 0.0795 -0.0139 -0.0074 0.0032 269 PHE A O 2032 C CB . PHE A 269 ? 0.0866 0.1137 0.0796 -0.0087 -0.0068 0.0113 269 PHE A CB 2033 C CG . PHE A 269 ? 0.0971 0.0902 0.0739 -0.0050 -0.0072 0.0080 269 PHE A CG 2034 C CD1 . PHE A 269 ? 0.0934 0.0782 0.0832 -0.0077 -0.0152 0.0045 269 PHE A CD1 2035 C CD2 . PHE A 269 ? 0.1351 0.0923 0.1192 0.0055 0.0072 -0.0095 269 PHE A CD2 2036 C CE1 . PHE A 269 ? 0.1002 0.1081 0.0843 -0.0165 -0.0099 0.0094 269 PHE A CE1 2037 C CE2 . PHE A 269 ? 0.1881 0.0793 0.1306 -0.0118 0.0042 -0.0033 269 PHE A CE2 2038 C CZ . PHE A 269 ? 0.1662 0.0956 0.1233 -0.0465 -0.0013 -0.0074 269 PHE A CZ 2039 N N . ARG A 270 ? 0.0817 0.1044 0.0791 -0.0076 -0.0072 0.0004 270 ARG A N 2040 C CA . ARG A 270 ? 0.0865 0.0960 0.0863 -0.0116 -0.0081 0.0007 270 ARG A CA 2041 C C . ARG A 270 ? 0.0773 0.0993 0.0853 0.0008 -0.0097 -0.0003 270 ARG A C 2042 O O . ARG A 270 ? 0.0913 0.1127 0.0837 -0.0107 -0.0127 -0.0032 270 ARG A O 2043 C CB . ARG A 270 ? 0.0838 0.1082 0.0897 -0.0043 -0.0066 0.0094 270 ARG A CB 2044 C CG . ARG A 270 ? 0.0999 0.1180 0.1042 -0.0127 0.0102 -0.0061 270 ARG A CG 2045 C CD . ARG A 270 ? 0.0925 0.1324 0.1254 0.0022 0.0012 -0.0074 270 ARG A CD 2046 N NE . ARG A 270 ? 0.1294 0.1527 0.1488 0.0102 0.0284 -0.0195 270 ARG A NE 2047 C CZ . ARG A 270 ? 0.1326 0.1788 0.1505 -0.0028 0.0163 -0.0228 270 ARG A CZ 2048 N NH1 . ARG A 270 ? 0.2362 0.1813 0.1424 -0.0272 0.0001 -0.0106 270 ARG A NH1 2049 N NH2 . ARG A 270 ? 0.1712 0.2042 0.1878 0.0056 0.0287 -0.0486 270 ARG A NH2 2050 N N . ALA A 271 ? 0.0847 0.0975 0.0808 -0.0078 -0.0082 0.0057 271 ALA A N 2051 C CA . ALA A 271 ? 0.0940 0.1040 0.0850 -0.0110 -0.0023 0.0058 271 ALA A CA 2052 C C . ALA A 271 ? 0.0931 0.0979 0.0886 -0.0057 -0.0110 0.0092 271 ALA A C 2053 O O . ALA A 271 ? 0.1068 0.1356 0.0872 -0.0068 -0.0195 0.0108 271 ALA A O 2054 C CB . ALA A 271 ? 0.1077 0.1069 0.1210 -0.0231 -0.0136 0.0216 271 ALA A CB 2055 N N . ALA A 272 ? 0.0812 0.0927 0.0889 -0.0113 -0.0127 0.0008 272 ALA A N 2056 C CA . ALA A 272 ? 0.0930 0.0976 0.0930 -0.0045 -0.0117 -0.0073 272 ALA A CA 2057 C C . ALA A 272 ? 0.0801 0.0964 0.0784 -0.0070 -0.0115 0.0000 272 ALA A C 2058 O O . ALA A 272 ? 0.0894 0.0973 0.1034 -0.0052 -0.0241 0.0033 272 ALA A O 2059 C CB . ALA A 272 ? 0.0893 0.1086 0.1159 -0.0104 -0.0030 -0.0199 272 ALA A CB 2060 N N . MET A 273 ? 0.0841 0.0964 0.0874 -0.0056 -0.0139 0.0019 273 MET A N 2061 C CA . MET A 273 ? 0.0871 0.0903 0.0966 -0.0089 -0.0086 0.0022 273 MET A CA 2062 C C . MET A 273 ? 0.0908 0.0894 0.0957 -0.0020 -0.0235 0.0042 273 MET A C 2063 O O . MET A 273 ? 0.1052 0.1023 0.1064 -0.0103 -0.0359 0.0052 273 MET A O 2064 C CB . MET A 273 ? 0.0928 0.0979 0.1085 -0.0101 -0.0152 0.0195 273 MET A CB 2065 C CG . MET A 273 ? 0.1069 0.1198 0.1204 -0.0052 -0.0082 0.0261 273 MET A CG 2066 S SD . MET A 273 ? 0.1039 0.1171 0.1591 -0.0034 0.0056 0.0303 273 MET A SD 2067 C CE . MET A 273 ? 0.1168 0.1499 0.5809 -0.0230 0.0297 -0.0833 273 MET A CE 2068 N N . SER A 274 ? 0.0923 0.1153 0.0832 -0.0023 -0.0165 -0.0037 274 SER A N 2069 C CA . SER A 274 ? 0.1079 0.1121 0.0859 0.0038 -0.0174 -0.0048 274 SER A CA 2070 C C . SER A 274 ? 0.0975 0.1115 0.0900 -0.0083 -0.0178 0.0012 274 SER A C 2071 O O . SER A 274 ? 0.1297 0.1316 0.1009 0.0070 -0.0353 -0.0069 274 SER A O 2072 C CB A SER A 274 ? 0.0927 0.1837 0.0842 0.0137 -0.0110 0.0126 274 SER A CB 2073 C CB B SER A 274 ? 0.0965 0.2119 0.1068 -0.0030 -0.0024 -0.0203 274 SER A CB 2074 O OG A SER A 274 ? 0.1064 0.1352 0.0760 -0.0033 -0.0086 0.0004 274 SER A OG 2075 O OG B SER A 274 ? 0.1540 0.2217 0.3715 -0.0669 -0.0377 0.0270 274 SER A OG 2076 N N . LYS A 275 ? 0.0869 0.0996 0.0902 -0.0120 -0.0084 0.0061 275 LYS A N 2077 C CA . LYS A 275 ? 0.0961 0.1107 0.0861 -0.0111 -0.0067 0.0178 275 LYS A CA 2078 C C . LYS A 275 ? 0.0926 0.1008 0.0858 -0.0027 -0.0084 0.0130 275 LYS A C 2079 O O . LYS A 275 ? 0.1007 0.1369 0.0832 -0.0061 -0.0169 0.0154 275 LYS A O 2080 C CB A LYS A 275 ? 0.1186 0.1069 0.1182 -0.0011 0.0286 0.0088 275 LYS A CB 2081 C CB B LYS A 275 ? 0.1225 0.0998 0.1407 -0.0074 -0.0135 0.0376 275 LYS A CB 2082 C CG A LYS A 275 ? 0.1628 0.1064 0.0931 0.0026 0.0027 0.0189 275 LYS A CG 2083 C CG B LYS A 275 ? 0.2007 0.1442 0.1385 -0.0721 0.0098 0.0186 275 LYS A CG 2084 C CD A LYS A 275 ? 0.2662 0.0922 0.1238 -0.0106 -0.0023 0.0257 275 LYS A CD 2085 C CD B LYS A 275 ? 0.2297 0.1333 0.2357 -0.0708 0.0881 0.0020 275 LYS A CD 2086 C CE A LYS A 275 ? 0.2347 0.1235 0.1520 0.0062 -0.0530 0.0042 275 LYS A CE 2087 C CE B LYS A 275 ? 0.3793 0.1680 0.3012 -0.0078 -0.0345 -0.0513 275 LYS A CE 2088 N NZ A LYS A 275 ? 0.2687 0.1063 0.1670 0.0110 -0.0108 -0.0021 275 LYS A NZ 2089 N NZ B LYS A 275 ? 0.6356 0.1357 0.1410 -0.0493 -0.1243 0.0078 275 LYS A NZ 2090 N N . LEU A 276 ? 0.0836 0.0889 0.0776 -0.0121 -0.0099 0.0086 276 LEU A N 2091 C CA . LEU A 276 ? 0.0801 0.0938 0.0766 -0.0004 -0.0084 0.0056 276 LEU A CA 2092 C C . LEU A 276 ? 0.0850 0.0918 0.0754 -0.0082 -0.0137 0.0004 276 LEU A C 2093 O O . LEU A 276 ? 0.0838 0.0968 0.0881 -0.0073 -0.0145 0.0014 276 LEU A O 2094 C CB . LEU A 276 ? 0.0862 0.1016 0.0768 -0.0141 -0.0092 0.0024 276 LEU A CB 2095 C CG . LEU A 276 ? 0.0775 0.1200 0.0823 -0.0168 -0.0093 0.0057 276 LEU A CG 2096 C CD1 . LEU A 276 ? 0.1047 0.1430 0.1609 -0.0021 0.0253 -0.0071 276 LEU A CD1 2097 C CD2 . LEU A 276 ? 0.1091 0.3288 0.1116 -0.0641 -0.0121 0.0817 276 LEU A CD2 2098 N N . ALA A 277 ? 0.0793 0.0886 0.0851 -0.0079 -0.0066 0.0029 277 ALA A N 2099 C CA . ALA A 277 ? 0.0860 0.0848 0.0840 -0.0068 -0.0066 -0.0014 277 ALA A CA 2100 C C . ALA A 277 ? 0.0847 0.0935 0.1001 -0.0022 -0.0131 -0.0033 277 ALA A C 2101 O O . ALA A 277 ? 0.0902 0.1108 0.1055 -0.0114 -0.0126 -0.0247 277 ALA A O 2102 C CB . ALA A 277 ? 0.0845 0.1033 0.1035 0.0035 -0.0126 -0.0033 277 ALA A CB 2103 N N . VAL A 278 ? 0.0967 0.1073 0.0762 0.0040 -0.0167 -0.0050 278 VAL A N 2104 C CA . VAL A 278 ? 0.0998 0.1354 0.0717 0.0131 -0.0160 -0.0035 278 VAL A CA 2105 C C . VAL A 278 ? 0.0895 0.1119 0.0801 -0.0019 -0.0078 0.0047 278 VAL A C 2106 O O . VAL A 278 ? 0.0849 0.1374 0.0804 -0.0030 -0.0085 0.0107 278 VAL A O 2107 C CB . VAL A 278 ? 0.1159 0.1936 0.0909 0.0286 0.0038 0.0106 278 VAL A CB 2108 C CG1 . VAL A 278 ? 0.1408 0.2593 0.1242 0.0853 0.0176 0.0093 278 VAL A CG1 2109 C CG2 . VAL A 278 ? 0.1077 0.2163 0.0973 -0.0069 0.0035 0.0180 278 VAL A CG2 2110 N N . LEU A 279 ? 0.0881 0.0997 0.0788 0.0006 -0.0116 0.0032 279 LEU A N 2111 C CA . LEU A 279 ? 0.0846 0.0984 0.0799 -0.0041 -0.0085 0.0126 279 LEU A CA 2112 C C . LEU A 279 ? 0.0895 0.0971 0.0706 -0.0016 -0.0002 0.0063 279 LEU A C 2113 O O . LEU A 279 ? 0.0975 0.0992 0.0812 -0.0135 -0.0064 0.0088 279 LEU A O 2114 C CB . LEU A 279 ? 0.0888 0.1060 0.0831 -0.0065 -0.0067 0.0030 279 LEU A CB 2115 C CG . LEU A 279 ? 0.0967 0.0890 0.0929 -0.0050 -0.0079 0.0041 279 LEU A CG 2116 C CD1 . LEU A 279 ? 0.1377 0.1637 0.1009 -0.0379 0.0033 -0.0367 279 LEU A CD1 2117 C CD2 . LEU A 279 ? 0.2195 0.0962 0.1084 -0.0325 -0.0187 -0.0032 279 LEU A CD2 2118 N N . GLY A 280 ? 0.0921 0.1085 0.0743 -0.0059 -0.0119 0.0076 280 GLY A N 2119 C CA . GLY A 280 ? 0.0963 0.1425 0.0754 -0.0005 -0.0109 0.0034 280 GLY A CA 2120 C C . GLY A 280 ? 0.0993 0.1224 0.0772 -0.0083 -0.0084 0.0076 280 GLY A C 2121 O O . GLY A 280 ? 0.1030 0.1912 0.0811 -0.0192 -0.0099 -0.0075 280 GLY A O 2122 N N . HIS A 281 ? 0.1007 0.1081 0.0705 -0.0133 -0.0035 0.0098 281 HIS A N 2123 C CA . HIS A 281 ? 0.1118 0.1059 0.0729 -0.0111 0.0031 0.0106 281 HIS A CA 2124 C C . HIS A 281 ? 0.1178 0.1019 0.0836 -0.0114 0.0075 0.0108 281 HIS A C 2125 O O . HIS A 281 ? 0.1374 0.1309 0.0968 -0.0394 0.0211 -0.0040 281 HIS A O 2126 C CB . HIS A 281 ? 0.1257 0.1030 0.0954 -0.0026 0.0113 0.0126 281 HIS A CB 2127 C CG . HIS A 281 ? 0.1516 0.0979 0.0902 -0.0117 0.0082 0.0095 281 HIS A CG 2128 N ND1 . HIS A 281 ? 0.1716 0.1255 0.1058 -0.0152 0.0178 0.0138 281 HIS A ND1 2129 C CD2 . HIS A 281 ? 0.1499 0.1127 0.0858 -0.0277 -0.0014 0.0083 281 HIS A CD2 2130 C CE1 . HIS A 281 ? 0.1395 0.0883 0.1004 0.0018 0.0280 0.0170 281 HIS A CE1 2131 N NE2 . HIS A 281 ? 0.2076 0.1301 0.1374 -0.0449 0.0065 0.0195 281 HIS A NE2 2132 N N . ASN A 282 ? 0.1353 0.1258 0.0919 -0.0289 0.0269 -0.0032 282 ASN A N 2133 C CA . ASN A 282 ? 0.1458 0.1189 0.0931 -0.0321 0.0267 0.0036 282 ASN A CA 2134 C C . ASN A 282 ? 0.1333 0.1233 0.0892 -0.0295 0.0260 0.0005 282 ASN A C 2135 O O . ASN A 282 ? 0.1564 0.1206 0.0987 -0.0300 0.0240 -0.0054 282 ASN A O 2136 C CB . ASN A 282 ? 0.1407 0.1387 0.0959 -0.0241 0.0228 0.0166 282 ASN A CB 2137 C CG . ASN A 282 ? 0.1496 0.1186 0.1143 -0.0146 0.0383 0.0142 282 ASN A CG 2138 O OD1 . ASN A 282 ? 0.1370 0.1471 0.1489 -0.0204 0.0260 0.0420 282 ASN A OD1 2139 N ND2 . ASN A 282 ? 0.1772 0.1774 0.1055 -0.0410 0.0089 0.0313 282 ASN A ND2 2140 N N . ARG A 283 ? 0.1467 0.1408 0.0928 -0.0287 0.0292 -0.0089 283 ARG A N 2141 C CA . ARG A 283 ? 0.1780 0.1667 0.0796 -0.0013 0.0092 0.0070 283 ARG A CA 2142 C C . ARG A 283 ? 0.1493 0.1211 0.0884 -0.0148 0.0100 0.0057 283 ARG A C 2143 O O . ARG A 283 ? 0.1655 0.1550 0.0945 0.0044 0.0057 0.0222 283 ARG A O 2144 C CB . ARG A 283 ? 0.2050 0.1625 0.0923 -0.0134 0.0121 -0.0046 283 ARG A CB 2145 C CG . ARG A 283 ? 0.2221 0.1510 0.1046 -0.0062 0.0160 0.0090 283 ARG A CG 2146 C CD . ARG A 283 ? 0.2571 0.1570 0.1341 -0.0243 -0.0151 -0.0053 283 ARG A CD 2147 N NE . ARG A 283 ? 0.2361 0.2077 0.1435 -0.0226 0.0043 0.0411 283 ARG A NE 2148 C CZ . ARG A 283 ? 0.2194 0.1765 0.1338 -0.0246 0.0091 0.0235 283 ARG A CZ 2149 N NH1 . ARG A 283 ? 0.2164 0.1512 0.1107 -0.0297 -0.0091 0.0113 283 ARG A NH1 2150 N NH2 . ARG A 283 ? 0.2534 0.2410 0.1966 0.0257 0.0427 0.0409 283 ARG A NH2 2151 N N . ASN A 284 ? 0.1491 0.1289 0.0851 -0.0117 0.0123 0.0022 284 ASN A N 2152 C CA . ASN A 284 ? 0.1186 0.1404 0.0878 0.0015 0.0123 0.0043 284 ASN A CA 2153 C C . ASN A 284 ? 0.1429 0.1193 0.0841 0.0159 0.0141 0.0075 284 ASN A C 2154 O O . ASN A 284 ? 0.1699 0.1350 0.0901 0.0032 0.0200 0.0095 284 ASN A O 2155 C CB . ASN A 284 ? 0.1354 0.1356 0.1006 -0.0063 0.0179 0.0150 284 ASN A CB 2156 C CG . ASN A 284 ? 0.1453 0.1596 0.1257 -0.0207 0.0207 0.0026 284 ASN A CG 2157 O OD1 . ASN A 284 ? 0.2015 0.1506 0.2067 -0.0024 0.0169 -0.0083 284 ASN A OD1 2158 N ND2 . ASN A 284 ? 0.1430 0.1786 0.1653 -0.0154 0.0020 -0.0330 284 ASN A ND2 2159 N N . SER A 285 ? 0.1497 0.1202 0.0842 -0.0027 0.0033 0.0071 285 SER A N 2160 C CA . SER A 285 ? 0.1454 0.1395 0.0803 0.0047 -0.0095 0.0118 285 SER A CA 2161 C C . SER A 285 ? 0.1408 0.1322 0.0720 -0.0188 -0.0100 0.0090 285 SER A C 2162 O O . SER A 285 ? 0.1623 0.1520 0.0939 -0.0389 -0.0253 0.0124 285 SER A O 2163 C CB . SER A 285 ? 0.1591 0.1734 0.1214 0.0162 -0.0316 -0.0055 285 SER A CB 2164 O OG . SER A 285 ? 0.2275 0.2170 0.1705 0.0233 -0.0559 0.0487 285 SER A OG 2165 N N . LEU A 286 ? 0.1197 0.1167 0.0742 -0.0202 -0.0035 0.0072 286 LEU A N 2166 C CA . LEU A 286 ? 0.1191 0.1153 0.0722 -0.0132 -0.0086 0.0070 286 LEU A CA 2167 C C . LEU A 286 ? 0.1187 0.1275 0.0691 -0.0133 0.0017 0.0140 286 LEU A C 2168 O O . LEU A 286 ? 0.1269 0.1396 0.1348 -0.0206 0.0064 -0.0042 286 LEU A O 2169 C CB . LEU A 286 ? 0.1117 0.1267 0.0706 -0.0049 -0.0039 0.0130 286 LEU A CB 2170 C CG . LEU A 286 ? 0.1181 0.1271 0.0819 0.0023 -0.0007 0.0109 286 LEU A CG 2171 C CD1 . LEU A 286 ? 0.1703 0.1507 0.0842 0.0123 0.0146 0.0000 286 LEU A CD1 2172 C CD2 . LEU A 286 ? 0.1187 0.1668 0.1129 -0.0230 0.0118 -0.0017 286 LEU A CD2 2173 N N . ILE A 287 ? 0.1189 0.1332 0.0912 -0.0070 -0.0049 0.0284 287 ILE A N 2174 C CA . ILE A 287 ? 0.1311 0.1337 0.0800 -0.0006 0.0029 0.0140 287 ILE A CA 2175 C C . ILE A 287 ? 0.1184 0.1246 0.0811 0.0047 0.0057 0.0028 287 ILE A C 2176 O O . ILE A 287 ? 0.1180 0.1890 0.0786 -0.0144 0.0027 0.0130 287 ILE A O 2177 C CB . ILE A 287 ? 0.1848 0.1486 0.1028 -0.0148 -0.0085 -0.0154 287 ILE A CB 2178 C CG1 . ILE A 287 ? 0.2806 0.1952 0.2326 0.0596 0.0938 -0.0021 287 ILE A CG1 2179 C CG2 . ILE A 287 ? 0.2156 0.1238 0.1551 -0.0063 -0.0012 -0.0126 287 ILE A CG2 2180 C CD1 . ILE A 287 ? 0.3013 0.2515 0.2118 0.0678 0.0473 -0.0228 287 ILE A CD1 2181 N N . ASP A 288 ? 0.1188 0.1767 0.0895 -0.0011 0.0126 0.0039 288 ASP A N 2182 C CA . ASP A 288 ? 0.1167 0.1685 0.1063 -0.0026 0.0026 -0.0044 288 ASP A CA 2183 C C . ASP A 288 ? 0.1197 0.1489 0.1137 0.0046 -0.0006 -0.0220 288 ASP A C 2184 O O . ASP A 288 ? 0.1643 0.2159 0.1460 0.0432 0.0431 -0.0115 288 ASP A O 2185 C CB . ASP A 288 ? 0.1409 0.1773 0.1279 -0.0251 -0.0016 -0.0016 288 ASP A CB 2186 C CG . ASP A 288 ? 0.1656 0.2223 0.1551 -0.0493 -0.0161 -0.0075 288 ASP A CG 2187 O OD1 . ASP A 288 ? 0.2622 0.2787 0.1879 -0.1268 -0.0407 0.0001 288 ASP A OD1 2188 O OD2 . ASP A 288 ? 0.1601 0.1864 0.1350 -0.0096 -0.0379 -0.0108 288 ASP A OD2 2189 N N . CYS A 289 ? 0.1205 0.1447 0.0930 0.0168 -0.0010 -0.0139 289 CYS A N 2190 C CA . CYS A 289 ? 0.1271 0.1362 0.1135 0.0104 -0.0131 -0.0178 289 CYS A CA 2191 C C . CYS A 289 ? 0.1138 0.1425 0.1134 0.0185 -0.0137 -0.0061 289 CYS A C 2192 O O . CYS A 289 ? 0.1230 0.1538 0.1245 0.0003 -0.0251 -0.0038 289 CYS A O 2193 C CB . CYS A 289 ? 0.1421 0.1482 0.1105 0.0015 -0.0156 -0.0109 289 CYS A CB 2194 S SG . CYS A 289 ? 0.1734 0.1755 0.1313 -0.0130 -0.0406 -0.0148 289 CYS A SG 2195 N N . SER A 290 ? 0.1138 0.1441 0.1032 0.0133 -0.0109 -0.0094 290 SER A N 2196 C CA . SER A 290 ? 0.1071 0.1381 0.1121 0.0111 -0.0092 -0.0092 290 SER A CA 2197 C C . SER A 290 ? 0.0929 0.1570 0.1134 0.0204 -0.0098 -0.0124 290 SER A C 2198 O O . SER A 290 ? 0.1246 0.1458 0.1148 0.0047 -0.0124 -0.0018 290 SER A O 2199 C CB . SER A 290 ? 0.1054 0.1458 0.1254 0.0126 -0.0093 -0.0142 290 SER A CB 2200 O OG . SER A 290 ? 0.1249 0.1356 0.1155 0.0103 -0.0089 -0.0137 290 SER A OG 2201 N N . ASP A 291 ? 0.1050 0.1411 0.1248 0.0172 -0.0053 -0.0098 291 ASP A N 2202 C CA . ASP A 291 ? 0.1011 0.1612 0.1607 0.0297 0.0002 -0.0023 291 ASP A CA 2203 C C . ASP A 291 ? 0.1107 0.1485 0.1432 0.0274 -0.0025 -0.0101 291 ASP A C 2204 O O . ASP A 291 ? 0.1289 0.1679 0.1922 0.0315 -0.0416 -0.0051 291 ASP A O 2205 C CB . ASP A 291 ? 0.1520 0.1823 0.1770 0.0438 0.0335 0.0017 291 ASP A CB 2206 C CG . ASP A 291 ? 0.1844 0.2607 0.1933 0.0486 0.0205 -0.0513 291 ASP A CG 2207 O OD1 . ASP A 291 ? 0.3485 0.2738 0.2321 0.0900 -0.0121 -0.0710 291 ASP A OD1 2208 O OD2 . ASP A 291 ? 0.2150 0.4949 0.3266 0.1529 -0.0709 -0.1643 291 ASP A OD2 2209 N N . VAL A 292 ? 0.1154 0.1338 0.1129 0.0163 -0.0160 -0.0071 292 VAL A N 2210 C CA . VAL A 292 ? 0.1301 0.1389 0.1105 0.0072 -0.0060 -0.0132 292 VAL A CA 2211 C C . VAL A 292 ? 0.1229 0.1200 0.1090 0.0119 -0.0186 -0.0083 292 VAL A C 2212 O O . VAL A 292 ? 0.1541 0.1300 0.1302 0.0065 0.0049 -0.0118 292 VAL A O 2213 C CB . VAL A 292 ? 0.1715 0.1541 0.1116 -0.0130 -0.0173 -0.0139 292 VAL A CB 2214 C CG1 . VAL A 292 ? 0.2491 0.2486 0.1306 -0.0187 0.0085 -0.0595 292 VAL A CG1 2215 C CG2 . VAL A 292 ? 0.1447 0.2055 0.1763 -0.0358 -0.0393 0.0304 292 VAL A CG2 2216 N N . VAL A 293 ? 0.1149 0.1248 0.0957 0.0169 -0.0087 -0.0045 293 VAL A N 2217 C CA . VAL A 293 ? 0.1078 0.1295 0.1011 0.0062 -0.0124 -0.0061 293 VAL A CA 2218 C C . VAL A 293 ? 0.1076 0.1209 0.1080 0.0210 -0.0086 -0.0048 293 VAL A C 2219 O O . VAL A 293 ? 0.1050 0.1519 0.1102 0.0160 -0.0062 -0.0010 293 VAL A O 2220 C CB . VAL A 293 ? 0.1106 0.1384 0.1044 0.0291 -0.0148 -0.0079 293 VAL A CB 2221 C CG1 . VAL A 293 ? 0.1259 0.1360 0.1051 0.0201 -0.0172 -0.0069 293 VAL A CG1 2222 C CG2 . VAL A 293 ? 0.1188 0.1480 0.1146 0.0166 -0.0270 0.0005 293 VAL A CG2 2223 N N . PRO A 294 ? 0.1049 0.1355 0.1119 0.0240 -0.0087 0.0005 294 PRO A N 2224 C CA . PRO A 294 ? 0.1449 0.1401 0.1041 0.0341 -0.0175 0.0001 294 PRO A CA 2225 C C . PRO A 294 ? 0.1349 0.1373 0.0969 0.0315 -0.0160 0.0026 294 PRO A C 2226 O O . PRO A 294 ? 0.1418 0.1360 0.1313 0.0338 -0.0304 -0.0032 294 PRO A O 2227 C CB . PRO A 294 ? 0.1917 0.1503 0.1163 -0.0004 -0.0186 0.0165 294 PRO A CB 2228 C CG . PRO A 294 ? 0.1723 0.1801 0.1490 0.0027 -0.0096 0.0293 294 PRO A CG 2229 C CD . PRO A 294 ? 0.1300 0.1585 0.1201 0.0077 0.0081 0.0104 294 PRO A CD 2230 N N . VAL A 295 ? 0.1423 0.1722 0.1416 0.0533 -0.0383 -0.0275 295 VAL A N 2231 C CA . VAL A 295 ? 0.1209 0.2050 0.1292 0.0377 -0.0191 -0.0258 295 VAL A CA 2232 C C . VAL A 295 ? 0.1271 0.1465 0.1145 0.0283 -0.0302 -0.0081 295 VAL A C 2233 O O . VAL A 295 ? 0.1869 0.1437 0.1444 0.0323 -0.0312 0.0012 295 VAL A O 2234 C CB . VAL A 295 ? 0.1318 0.3171 0.1513 0.0619 -0.0246 -0.0590 295 VAL A CB 2235 C CG1 . VAL A 295 ? 0.1371 0.3543 0.1717 0.0279 -0.0396 -0.0347 295 VAL A CG1 2236 C CG2 . VAL A 295 ? 0.1544 0.4838 0.1706 0.0544 0.0156 -0.0955 295 VAL A CG2 2237 N N . PRO A 296 ? 0.1251 0.1452 0.1019 0.0115 -0.0263 0.0019 296 PRO A N 2238 C CA . PRO A 296 ? 0.1052 0.1388 0.1091 0.0131 -0.0214 -0.0051 296 PRO A CA 2239 C C . PRO A 296 ? 0.1076 0.1477 0.1068 0.0160 -0.0180 0.0054 296 PRO A C 2240 O O . PRO A 296 ? 0.0981 0.2174 0.1090 0.0109 -0.0200 0.0121 296 PRO A O 2241 C CB . PRO A 296 ? 0.1074 0.1439 0.1217 0.0084 -0.0231 0.0013 296 PRO A CB 2242 C CG A PRO A 296 ? 0.0881 0.1375 0.1034 0.0042 -0.0355 0.0001 296 PRO A CG 2243 C CG B PRO A 296 ? 0.2446 0.1918 0.1251 0.0790 -0.0127 0.0264 296 PRO A CG 2244 C CD . PRO A 296 ? 0.2111 0.1488 0.1092 0.0250 -0.0157 0.0076 296 PRO A CD 2245 N N . LYS A 297 ? 0.0981 0.1406 0.1094 0.0195 -0.0136 0.0077 297 LYS A N 2246 C CA . LYS A 297 ? 0.1162 0.1448 0.1029 0.0349 -0.0142 0.0015 297 LYS A CA 2247 C C . LYS A 297 ? 0.1119 0.1587 0.1078 0.0182 -0.0328 -0.0025 297 LYS A C 2248 O O . LYS A 297 ? 0.1157 0.1548 0.1225 0.0188 -0.0245 -0.0142 297 LYS A O 2249 C CB . LYS A 297 ? 0.1331 0.1434 0.1239 0.0269 -0.0088 0.0142 297 LYS A CB 2250 C CG . LYS A 297 ? 0.1610 0.1350 0.1417 0.0320 -0.0097 0.0193 297 LYS A CG 2251 C CD . LYS A 297 ? 0.1705 0.1418 0.1390 0.0028 -0.0281 0.0150 297 LYS A CD 2252 C CE . LYS A 297 ? 0.1657 0.1569 0.1563 0.0056 -0.0294 0.0227 297 LYS A CE 2253 N NZ . LYS A 297 ? 0.1745 0.2165 0.1568 -0.0172 -0.0155 0.0322 297 LYS A NZ 2254 N N . PRO A 298 ? 0.1070 0.2079 0.1380 0.0278 -0.0385 -0.0124 298 PRO A N 2255 C CA . PRO A 298 ? 0.1050 0.2516 0.1309 -0.0028 -0.0292 -0.0372 298 PRO A CA 2256 C C . PRO A 298 ? 0.1032 0.2848 0.1279 -0.0248 -0.0282 -0.0434 298 PRO A C 2257 O O . PRO A 298 ? 0.1538 0.3407 0.1382 -0.0086 -0.0243 -0.0065 298 PRO A O 2258 C CB . PRO A 298 ? 0.1067 0.3482 0.1908 0.0097 -0.0305 -0.0735 298 PRO A CB 2259 C CG . PRO A 298 ? 0.1171 0.3382 0.3951 0.0638 -0.0777 -0.0734 298 PRO A CG 2260 C CD . PRO A 298 ? 0.1402 0.2517 0.2432 0.0672 -0.0662 -0.0176 298 PRO A CD 2261 N N . ALA A 299 ? 0.1309 0.2904 0.1629 -0.0139 -0.0453 -0.0779 299 ALA A N 2262 C CA . ALA A 299 ? 0.1146 0.3256 0.1447 0.0133 -0.0367 -0.0680 299 ALA A CA 2263 C C . ALA A 299 ? 0.1210 0.2981 0.1581 0.0306 -0.0469 -0.0945 299 ALA A C 2264 O O . ALA A 299 ? 0.1217 0.3640 0.1805 0.0298 -0.0543 -0.1122 299 ALA A O 2265 C CB . ALA A 299 ? 0.1662 0.3298 0.2213 0.0813 -0.0697 -0.1132 299 ALA A CB 2266 N N . THR A 300 ? 0.1351 0.2307 0.1599 0.0109 -0.0454 -0.0525 300 THR A N 2267 C CA . THR A 300 ? 0.1448 0.1837 0.1565 0.0179 -0.0509 -0.0304 300 THR A CA 2268 C C . THR A 300 ? 0.1331 0.1772 0.1505 0.0308 -0.0513 -0.0470 300 THR A C 2269 O O . THR A 300 ? 0.1300 0.2231 0.2513 0.0255 -0.0695 -0.0839 300 THR A O 2270 C CB . THR A 300 ? 0.1844 0.1698 0.1643 0.0301 -0.0325 -0.0353 300 THR A CB 2271 O OG1 . THR A 300 ? 0.1799 0.1802 0.1711 0.0334 -0.0364 -0.0334 300 THR A OG1 2272 C CG2 . THR A 300 ? 0.2186 0.1710 0.2040 0.0244 -0.0120 -0.0082 300 THR A CG2 2273 N N . GLY A 301 ? 0.1611 0.1761 0.1452 0.0173 -0.0346 -0.0435 301 GLY A N 2274 C CA . GLY A 301 ? 0.1729 0.1986 0.1256 -0.0068 -0.0107 -0.0273 301 GLY A CA 2275 C C . GLY A 301 ? 0.1520 0.1758 0.1425 -0.0045 -0.0014 -0.0355 301 GLY A C 2276 O O . GLY A 301 ? 0.1813 0.1756 0.1718 -0.0241 -0.0209 -0.0025 301 GLY A O 2277 N N . GLN A 302 ? 0.1105 0.1388 0.1294 0.0077 -0.0184 -0.0337 302 GLN A N 2278 C CA . GLN A 302 ? 0.1167 0.1321 0.1218 0.0268 -0.0256 -0.0297 302 GLN A CA 2279 C C . GLN A 302 ? 0.1034 0.1267 0.1145 0.0054 -0.0308 -0.0056 302 GLN A C 2280 O O . GLN A 302 ? 0.1073 0.1382 0.1314 0.0095 -0.0387 -0.0140 302 GLN A O 2281 C CB . GLN A 302 ? 0.2121 0.1325 0.1019 0.0225 -0.0340 -0.0071 302 GLN A CB 2282 C CG . GLN A 302 ? 0.2713 0.1506 0.2045 0.0655 -0.0548 -0.0113 302 GLN A CG 2283 C CD . GLN A 302 ? 0.3240 0.1247 0.1894 0.0632 -0.0839 0.0290 302 GLN A CD 2284 O OE1 . GLN A 302 ? 0.3850 0.1769 0.2625 -0.0167 -0.0291 0.0397 302 GLN A OE1 2285 N NE2 . GLN A 302 ? 0.3453 0.3146 0.1980 0.1631 -0.0743 -0.0366 302 GLN A NE2 2286 N N . PRO A 303 ? 0.1139 0.1092 0.1272 0.0108 -0.0401 0.0005 303 PRO A N 2287 C CA . PRO A 303 ? 0.1066 0.1114 0.1235 0.0059 -0.0240 0.0068 303 PRO A CA 2288 C C . PRO A 303 ? 0.1230 0.1089 0.0943 0.0024 -0.0248 0.0021 303 PRO A C 2289 O O . PRO A 303 ? 0.1283 0.1143 0.1187 0.0090 -0.0179 0.0082 303 PRO A O 2290 C CB . PRO A 303 ? 0.1332 0.1220 0.1472 -0.0086 -0.0238 -0.0125 303 PRO A CB 2291 C CG . PRO A 303 ? 0.2193 0.1637 0.4640 0.0681 -0.2363 -0.1130 303 PRO A CG 2292 C CD . PRO A 303 ? 0.1766 0.1476 0.2419 0.0343 -0.1351 -0.0428 303 PRO A CD 2293 N N . ALA A 304 ? 0.1063 0.1148 0.0917 0.0019 -0.0180 0.0034 304 ALA A N 2294 C CA . ALA A 304 ? 0.1017 0.1230 0.0954 -0.0032 -0.0229 -0.0035 304 ALA A CA 2295 C C . ALA A 304 ? 0.1104 0.0994 0.0942 0.0042 -0.0300 0.0002 304 ALA A C 2296 O O . ALA A 304 ? 0.1072 0.1225 0.1072 -0.0150 -0.0288 -0.0083 304 ALA A O 2297 C CB . ALA A 304 ? 0.1026 0.1480 0.0929 0.0047 -0.0320 0.0112 304 ALA A CB 2298 N N . MET A 305 ? 0.1022 0.1262 0.0926 -0.0108 -0.0274 -0.0102 305 MET A N 2299 C CA . MET A 305 ? 0.1153 0.1054 0.0973 0.0065 -0.0130 -0.0051 305 MET A CA 2300 C C . MET A 305 ? 0.1024 0.1062 0.1028 0.0040 -0.0256 0.0023 305 MET A C 2301 O O . MET A 305 ? 0.1039 0.1427 0.1102 -0.0002 -0.0300 -0.0168 305 MET A O 2302 C CB . MET A 305 ? 0.1242 0.1201 0.1042 0.0160 -0.0287 -0.0018 305 MET A CB 2303 C CG . MET A 305 ? 0.1169 0.1166 0.1252 0.0079 -0.0294 -0.0093 305 MET A CG 2304 S SD . MET A 305 ? 0.1428 0.1339 0.1815 0.0287 -0.0141 0.0149 305 MET A SD 2305 C CE . MET A 305 ? 0.1284 0.0951 0.2714 0.0166 0.0095 0.0245 305 MET A CE 2306 N N . PHE A 306 ? 0.1029 0.1169 0.0925 0.0045 -0.0185 -0.0050 306 PHE A N 2307 C CA . PHE A 306 ? 0.1060 0.1201 0.0974 0.0074 -0.0234 -0.0006 306 PHE A CA 2308 C C . PHE A 306 ? 0.1242 0.1220 0.1032 -0.0062 -0.0174 0.0026 306 PHE A C 2309 O O . PHE A 306 ? 0.1320 0.1276 0.1273 0.0042 -0.0259 0.0220 306 PHE A O 2310 C CB . PHE A 306 ? 0.1184 0.1199 0.1017 0.0124 -0.0131 -0.0007 306 PHE A CB 2311 C CG . PHE A 306 ? 0.1159 0.1246 0.0956 0.0147 -0.0188 -0.0077 306 PHE A CG 2312 C CD1 . PHE A 306 ? 0.1284 0.1254 0.1201 0.0043 -0.0141 -0.0066 306 PHE A CD1 2313 C CD2 . PHE A 306 ? 0.1188 0.1258 0.1220 0.0130 -0.0231 -0.0052 306 PHE A CD2 2314 C CE1 . PHE A 306 ? 0.1505 0.1316 0.1597 0.0008 0.0102 -0.0090 306 PHE A CE1 2315 C CE2 . PHE A 306 ? 0.1517 0.1348 0.1243 0.0215 -0.0363 -0.0040 306 PHE A CE2 2316 C CZ . PHE A 306 ? 0.1837 0.1110 0.1456 0.0138 -0.0059 0.0116 306 PHE A CZ 2317 N N . PRO A 307 ? 0.1215 0.1456 0.1017 -0.0085 -0.0172 0.0057 307 PRO A N 2318 C CA . PRO A 307 ? 0.1446 0.1338 0.1146 -0.0172 -0.0113 0.0013 307 PRO A CA 2319 C C . PRO A 307 ? 0.1343 0.1331 0.1080 -0.0034 -0.0120 0.0022 307 PRO A C 2320 O O . PRO A 307 ? 0.1734 0.1302 0.1122 0.0038 -0.0155 0.0097 307 PRO A O 2321 C CB . PRO A 307 ? 0.1658 0.2076 0.1139 -0.0614 -0.0135 -0.0020 307 PRO A CB 2322 C CG . PRO A 307 ? 0.1848 0.2687 0.1364 -0.0917 -0.0470 0.0278 307 PRO A CG 2323 C CD . PRO A 307 ? 0.1415 0.1951 0.1052 -0.0170 -0.0275 0.0177 307 PRO A CD 2324 N N . ALA A 308 ? 0.1518 0.1484 0.1266 0.0036 -0.0116 0.0188 308 ALA A N 2325 C CA . ALA A 308 ? 0.2012 0.1598 0.1242 0.0029 -0.0367 0.0292 308 ALA A CA 2326 C C . ALA A 308 ? 0.1938 0.1365 0.0890 -0.0175 -0.0258 0.0160 308 ALA A C 2327 O O . ALA A 308 ? 0.1941 0.1464 0.1172 -0.0034 -0.0125 -0.0003 308 ALA A O 2328 C CB . ALA A 308 ? 0.2184 0.1638 0.1550 0.0109 -0.0100 0.0523 308 ALA A CB 2329 N N . SER A 309 ? 0.2079 0.1613 0.1146 -0.0077 -0.0343 0.0156 309 SER A N 2330 C CA . SER A 309 ? 0.2198 0.1617 0.1106 -0.0077 -0.0156 -0.0029 309 SER A CA 2331 C C . SER A 309 ? 0.1866 0.1633 0.1266 -0.0047 -0.0085 0.0063 309 SER A C 2332 O O . SER A 309 ? 0.2498 0.1715 0.1666 0.0112 0.0305 -0.0124 309 SER A O 2333 C CB . SER A 309 ? 0.2242 0.1537 0.1139 -0.0115 0.0051 0.0064 309 SER A CB 2334 O OG . SER A 309 ? 0.1884 0.1923 0.1409 -0.0031 -0.0136 0.0042 309 SER A OG 2335 N N . THR A 310 ? 0.1854 0.1425 0.1206 -0.0011 -0.0148 0.0053 310 THR A N 2336 C CA . THR A 310 ? 0.1596 0.1336 0.1300 0.0116 -0.0133 0.0037 310 THR A CA 2337 C C . THR A 310 ? 0.1638 0.1347 0.1446 0.0086 -0.0384 0.0009 310 THR A C 2338 O O . THR A 310 ? 0.1696 0.1602 0.2267 0.0182 -0.0469 0.0140 310 THR A O 2339 C CB . THR A 310 ? 0.1409 0.1298 0.1499 -0.0149 -0.0280 0.0139 310 THR A CB 2340 O OG1 . THR A 310 ? 0.2045 0.1393 0.1269 0.0031 -0.0063 0.0118 310 THR A OG1 2341 C CG2 . THR A 310 ? 0.2214 0.2793 0.1643 -0.1250 -0.0271 0.0519 310 THR A CG2 2342 N N . GLY A 311 ? 0.1537 0.1318 0.1626 0.0085 -0.0323 0.0024 311 GLY A N 2343 C CA . GLY A 311 ? 0.1519 0.1376 0.1442 0.0039 -0.0345 -0.0211 311 GLY A CA 2344 C C . GLY A 311 ? 0.1179 0.1520 0.1223 0.0007 -0.0223 -0.0180 311 GLY A C 2345 O O . GLY A 311 ? 0.1306 0.1341 0.1275 -0.0046 -0.0365 -0.0105 311 GLY A O 2346 N N . PRO A 312 ? 0.1285 0.1699 0.1201 -0.0044 -0.0209 -0.0038 312 PRO A N 2347 C CA . PRO A 312 ? 0.1258 0.1836 0.1369 -0.0112 -0.0200 0.0056 312 PRO A CA 2348 C C . PRO A 312 ? 0.1236 0.1458 0.1200 -0.0277 -0.0317 0.0038 312 PRO A C 2349 O O . PRO A 312 ? 0.1509 0.1438 0.1429 -0.0315 -0.0395 0.0045 312 PRO A O 2350 C CB . PRO A 312 ? 0.1340 0.2323 0.1773 -0.0335 0.0053 0.0132 312 PRO A CB 2351 C CG . PRO A 312 ? 0.1248 0.2874 0.3395 -0.0159 -0.0316 0.0867 312 PRO A CG 2352 C CD . PRO A 312 ? 0.1183 0.2100 0.1553 0.0041 -0.0316 -0.0133 312 PRO A CD 2353 N N . GLN A 313 ? 0.1229 0.1512 0.1254 -0.0259 -0.0363 -0.0085 313 GLN A N 2354 C CA . GLN A 313 ? 0.1294 0.1666 0.1426 -0.0278 -0.0386 -0.0402 313 GLN A CA 2355 C C . GLN A 313 ? 0.1335 0.1348 0.1475 0.0034 -0.0574 -0.0392 313 GLN A C 2356 O O . GLN A 313 ? 0.1452 0.1593 0.1864 0.0034 -0.0402 -0.0582 313 GLN A O 2357 C CB . GLN A 313 ? 0.1508 0.2549 0.1342 0.0043 -0.0553 -0.0431 313 GLN A CB 2358 C CG . GLN A 313 ? 0.1935 0.3176 0.1285 -0.0226 -0.0347 0.0026 313 GLN A CG 2359 C CD . GLN A 313 ? 0.2284 0.2468 0.1539 -0.0558 -0.0222 0.0253 313 GLN A CD 2360 O OE1 . GLN A 313 ? 0.2077 0.1975 0.1449 -0.0432 -0.0355 0.0098 313 GLN A OE1 2361 N NE2 . GLN A 313 ? 0.4790 0.3578 0.2811 0.0083 0.1164 0.1450 313 GLN A NE2 2362 N N . ASP A 314 ? 0.1069 0.1237 0.1176 -0.0141 -0.0298 -0.0104 314 ASP A N 2363 C CA . ASP A 314 ? 0.1138 0.1314 0.1224 -0.0184 -0.0369 -0.0091 314 ASP A CA 2364 C C . ASP A 314 ? 0.1123 0.1271 0.1100 -0.0010 -0.0240 -0.0168 314 ASP A C 2365 O O . ASP A 314 ? 0.1214 0.1800 0.1274 -0.0279 -0.0418 -0.0061 314 ASP A O 2366 C CB . ASP A 314 ? 0.1216 0.1406 0.1545 -0.0243 -0.0364 0.0012 314 ASP A CB 2367 C CG . ASP A 314 ? 0.1479 0.1673 0.1729 -0.0103 0.0182 0.0279 314 ASP A CG 2368 O OD1 . ASP A 314 ? 0.2583 0.1989 0.2175 0.0508 0.0189 0.0621 314 ASP A OD1 2369 O OD2 . ASP A 314 ? 0.2137 0.2283 0.1755 0.0028 0.0236 0.0103 314 ASP A OD2 2370 N N . LEU A 315 ? 0.1143 0.1224 0.1116 -0.0039 -0.0303 -0.0088 315 LEU A N 2371 C CA . LEU A 315 ? 0.1423 0.1094 0.1153 -0.0013 -0.0328 -0.0130 315 LEU A CA 2372 C C . LEU A 315 ? 0.1405 0.1004 0.1241 -0.0013 -0.0463 -0.0173 315 LEU A C 2373 O O . LEU A 315 ? 0.1951 0.1164 0.1578 0.0168 -0.0783 -0.0396 315 LEU A O 2374 C CB . LEU A 315 ? 0.1595 0.1173 0.1253 0.0123 -0.0140 0.0102 315 LEU A CB 2375 C CG . LEU A 315 ? 0.1764 0.1370 0.1231 0.0359 -0.0068 0.0135 315 LEU A CG 2376 C CD1 . LEU A 315 ? 0.1680 0.1944 0.1291 0.0335 -0.0002 0.0342 315 LEU A CD1 2377 C CD2 . LEU A 315 ? 0.2254 0.1509 0.1347 0.0444 -0.0198 -0.0011 315 LEU A CD2 2378 N N . GLU A 316 ? 0.1393 0.1021 0.1036 -0.0007 -0.0306 -0.0129 316 GLU A N 2379 C CA . GLU A 316 ? 0.1341 0.0973 0.1170 0.0022 -0.0330 -0.0167 316 GLU A CA 2380 C C . GLU A 316 ? 0.1384 0.0926 0.1226 -0.0167 -0.0303 -0.0005 316 GLU A C 2381 O O . GLU A 316 ? 0.1902 0.1751 0.1208 -0.0722 -0.0565 0.0002 316 GLU A O 2382 C CB . GLU A 316 ? 0.1315 0.1222 0.1235 -0.0061 -0.0252 0.0032 316 GLU A CB 2383 C CG . GLU A 316 ? 0.1837 0.1805 0.1390 -0.0073 -0.0153 0.0255 316 GLU A CG 2384 C CD . GLU A 316 ? 0.2165 0.1521 0.1830 -0.0535 0.0397 -0.0270 316 GLU A CD 2385 O OE1 . GLU A 316 ? 0.2015 0.1843 0.1198 -0.0009 -0.0115 -0.0005 316 GLU A OE1 2386 O OE2 . GLU A 316 ? 0.2859 0.3784 0.4509 -0.1039 0.1562 -0.2738 316 GLU A OE2 2387 N N . LEU A 317 ? 0.1304 0.1059 0.1219 -0.0147 -0.0368 -0.0198 317 LEU A N 2388 C CA . LEU A 317 ? 0.1286 0.1063 0.1171 -0.0096 -0.0320 -0.0006 317 LEU A CA 2389 C C . LEU A 317 ? 0.1277 0.0877 0.1364 -0.0061 -0.0335 -0.0126 317 LEU A C 2390 O O . LEU A 317 ? 0.1664 0.1111 0.1700 0.0086 -0.0225 -0.0272 317 LEU A O 2391 C CB . LEU A 317 ? 0.1232 0.1509 0.1515 -0.0115 -0.0349 0.0177 317 LEU A CB 2392 C CG . LEU A 317 ? 0.1355 0.1781 0.1450 -0.0068 -0.0288 0.0304 317 LEU A CG 2393 C CD1 . LEU A 317 ? 0.1059 0.3016 0.2332 -0.0074 -0.0292 0.0560 317 LEU A CD1 2394 C CD2 . LEU A 317 ? 0.1907 0.1978 0.1404 0.0553 0.0030 0.0100 317 LEU A CD2 2395 N N . SER A 318 ? 0.1365 0.1032 0.1285 0.0079 -0.0393 -0.0060 318 SER A N 2396 C CA . SER A 318 ? 0.1545 0.1072 0.1453 -0.0109 -0.0455 0.0138 318 SER A CA 2397 C C . SER A 318 ? 0.1533 0.1095 0.1675 -0.0078 -0.0470 0.0357 318 SER A C 2398 O O . SER A 318 ? 0.1805 0.1941 0.2131 -0.0099 -0.0445 0.0902 318 SER A O 2399 C CB . SER A 318 ? 0.1440 0.1086 0.1313 -0.0048 -0.0371 0.0005 318 SER A CB 2400 O OG . SER A 318 ? 0.1494 0.1357 0.1512 -0.0233 -0.0324 -0.0013 318 SER A OG 2401 N N . CYS A 319 ? 0.1586 0.1368 0.1488 -0.0085 -0.0519 0.0180 319 CYS A N 2402 C CA . CYS A 319 ? 0.1708 0.1289 0.1558 -0.0118 -0.0465 0.0108 319 CYS A CA 2403 C C . CYS A 319 ? 0.1784 0.1050 0.1794 -0.0111 -0.0648 -0.0038 319 CYS A C 2404 O O . CYS A 319 ? 0.2523 0.1194 0.2997 -0.0092 -0.1632 -0.0038 319 CYS A O 2405 C CB . CYS A 319 ? 0.1843 0.1065 0.1827 -0.0245 -0.0401 -0.0046 319 CYS A CB 2406 S SG . CYS A 319 ? 0.2046 0.1593 0.2004 -0.0556 -0.0228 -0.0267 319 CYS A SG 2407 N N . PRO A 320 ? 0.1504 0.1215 0.2179 -0.0095 -0.0461 0.0187 320 PRO A N 2408 C CA . PRO A 320 ? 0.1736 0.1042 0.2364 -0.0162 -0.0431 0.0092 320 PRO A CA 2409 C C . PRO A 320 ? 0.1663 0.1111 0.2125 -0.0175 -0.0626 0.0198 320 PRO A C 2410 O O . PRO A 320 ? 0.2121 0.2299 0.2825 -0.0955 -0.0789 0.0347 320 PRO A O 2411 C CB . PRO A 320 ? 0.1820 0.1211 0.5144 0.0037 -0.0433 0.0036 320 PRO A CB 2412 C CG . PRO A 320 ? 0.2951 0.1524 0.6431 0.0068 -0.2152 0.0826 320 PRO A CG 2413 C CD . PRO A 320 ? 0.1997 0.1715 0.4106 -0.0113 -0.1407 0.0668 320 PRO A CD 2414 N N . SER A 321 ? 0.2191 0.1440 0.2417 -0.0435 -0.0005 0.0052 321 SER A N 2415 C CA . SER A 321 ? 0.2507 0.1436 0.3075 -0.0473 0.0387 0.0495 321 SER A CA 2416 C C . SER A 321 ? 0.2039 0.1425 0.2940 -0.0610 0.0245 0.0274 321 SER A C 2417 O O . SER A 321 ? 0.2426 0.2265 0.3042 -0.0693 0.0636 0.0400 321 SER A O 2418 C CB . SER A 321 ? 0.2517 0.1989 0.3053 0.0065 0.0612 0.0578 321 SER A CB 2419 O OG . SER A 321 ? 0.5681 0.3357 0.2613 -0.1428 0.0020 0.0227 321 SER A OG 2420 N N . GLU A 322 ? 0.1850 0.1414 0.2189 -0.0417 0.0158 0.0108 322 GLU A N 2421 C CA . GLU A 322 ? 0.2179 0.1411 0.2110 -0.0329 -0.0163 -0.0056 322 GLU A CA 2422 C C . GLU A 322 ? 0.2057 0.1327 0.1920 -0.0330 -0.0075 -0.0316 322 GLU A C 2423 O O . GLU A 322 ? 0.2048 0.1671 0.2077 -0.0445 -0.0024 -0.0133 322 GLU A O 2424 C CB . GLU A 322 ? 0.2890 0.1799 0.2406 0.0106 -0.0979 -0.0368 322 GLU A CB 2425 C CG . GLU A 322 ? 0.5784 0.4653 0.2005 -0.0735 -0.0741 -0.0453 322 GLU A CG 2426 C CD . GLU A 322 ? 0.8598 0.4212 0.2405 -0.0668 -0.2234 -0.0190 322 GLU A CD 2427 O OE1 . GLU A 322 ? 0.6496 0.4129 0.3714 0.0141 -0.2628 -0.0184 322 GLU A OE1 2428 O OE2 . GLU A 322 ? 1.1103 0.3102 0.7706 0.1633 -0.6684 -0.0429 322 GLU A OE2 2429 N N . ARG A 323 ? 0.1982 0.1365 0.2109 -0.0430 -0.0213 -0.0103 323 ARG A N 2430 C CA . ARG A 323 ? 0.2272 0.1255 0.2081 -0.0445 -0.0253 -0.0228 323 ARG A CA 2431 C C . ARG A 323 ? 0.2309 0.1209 0.1737 -0.0402 -0.0208 -0.0400 323 ARG A C 2432 O O . ARG A 323 ? 0.2022 0.1318 0.2271 -0.0379 0.0148 -0.0492 323 ARG A O 2433 C CB . ARG A 323 ? 0.2512 0.1295 0.3640 -0.0508 -0.0966 0.0589 323 ARG A CB 2434 C CG . ARG A 323 ? 0.3135 0.1550 0.3185 -0.0364 -0.1079 0.0146 323 ARG A CG 2435 C CD . ARG A 323 ? 0.3696 0.2921 0.5606 -0.0057 -0.2508 0.0234 323 ARG A CD 2436 N NE . ARG A 323 ? 0.3185 0.3733 0.6732 -0.0718 -0.1595 -0.1239 323 ARG A NE 2437 C CZ . ARG A 323 ? 0.3465 0.3952 0.7227 -0.1427 -0.1212 -0.1929 323 ARG A CZ 2438 N NH1 . ARG A 323 ? 0.9121 0.2733 0.1470 -0.2120 -0.1865 0.0262 323 ARG A NH1 2439 N NH2 . ARG A 323 ? 0.8104 0.4246 0.5660 -0.2733 -0.0503 -0.2124 323 ARG A NH2 2440 N N . PHE A 324 ? 0.3402 0.1252 0.1471 -0.0489 -0.0049 -0.0351 324 PHE A N 2441 C CA . PHE A 324 ? 0.2946 0.1220 0.1443 -0.0306 0.0068 -0.0382 324 PHE A CA 2442 C C . PHE A 324 ? 0.2694 0.1453 0.1599 -0.0833 -0.0570 -0.0033 324 PHE A C 2443 O O . PHE A 324 ? 0.4521 0.1850 0.1877 -0.1584 -0.1459 0.0267 324 PHE A O 2444 C CB . PHE A 324 ? 0.3755 0.1463 0.1604 -0.0143 0.0531 -0.0328 324 PHE A CB 2445 C CG . PHE A 324 ? 0.2447 0.1495 0.1352 0.0109 0.0170 -0.0400 324 PHE A CG 2446 C CD1 . PHE A 324 ? 0.2077 0.1856 0.1500 -0.0105 0.0357 0.0017 324 PHE A CD1 2447 C CD2 . PHE A 324 ? 0.2233 0.2013 0.1886 0.0471 0.0032 -0.0592 324 PHE A CD2 2448 C CE1 . PHE A 324 ? 0.1537 0.1834 0.2219 0.0130 0.0419 0.0275 324 PHE A CE1 2449 C CE2 . PHE A 324 ? 0.1663 0.2517 0.1959 0.0039 0.0100 -0.0787 324 PHE A CE2 2450 C CZ . PHE A 324 ? 0.1778 0.2089 0.2321 -0.0094 0.0609 -0.0175 324 PHE A CZ 2451 N N . PRO A 325 ? 0.1896 0.1534 0.1453 -0.0575 -0.0344 0.0044 325 PRO A N 2452 C CA . PRO A 325 ? 0.1875 0.2599 0.1475 -0.0383 -0.0386 0.0153 325 PRO A CA 2453 C C . PRO A 325 ? 0.2066 0.1737 0.1544 -0.0346 -0.0374 0.0150 325 PRO A C 2454 O O . PRO A 325 ? 0.2292 0.2250 0.1530 -0.0523 -0.0315 0.0237 325 PRO A O 2455 C CB . PRO A 325 ? 0.1871 0.3208 0.1570 0.0378 -0.0036 -0.0371 325 PRO A CB 2456 C CG . PRO A 325 ? 0.1855 0.1527 0.2711 -0.0095 -0.0098 -0.0486 325 PRO A CG 2457 C CD . PRO A 325 ? 0.1843 0.1184 0.1546 -0.0316 -0.0254 -0.0169 325 PRO A CD 2458 N N . THR A 326 ? 0.2172 0.3010 0.1697 -0.1098 -0.0670 0.0739 326 THR A N 2459 C CA . THR A 326 ? 0.2567 0.2960 0.1808 -0.1544 -0.1135 0.0829 326 THR A CA 2460 C C . THR A 326 ? 0.1681 0.2947 0.1721 -0.0712 -0.0657 0.0777 326 THR A C 2461 O O . THR A 326 ? 0.1440 0.3744 0.2546 -0.0734 -0.0092 0.0923 326 THR A O 2462 C CB . THR A 326 ? 0.2931 0.4762 0.2464 -0.2436 -0.1417 0.1649 326 THR A CB 2463 O OG1 . THR A 326 ? 0.5583 0.4765 0.3108 -0.3766 -0.2164 0.1149 326 THR A OG1 2464 C CG2 . THR A 326 ? 0.3745 0.6454 0.2587 -0.3171 -0.1986 0.1877 326 THR A CG2 2465 N N . LEU A 327 ? 0.1688 0.1972 0.1405 -0.0453 -0.0479 0.0169 327 LEU A N 2466 C CA . LEU A 327 ? 0.1310 0.1938 0.1232 -0.0213 -0.0355 0.0128 327 LEU A CA 2467 C C . LEU A 327 ? 0.1396 0.1878 0.1153 0.0023 -0.0423 -0.0052 327 LEU A C 2468 O O . LEU A 327 ? 0.1838 0.1662 0.1388 0.0130 -0.0412 -0.0106 327 LEU A O 2469 C CB . LEU A 327 ? 0.1295 0.1702 0.1160 -0.0095 -0.0355 -0.0053 327 LEU A CB 2470 C CG . LEU A 327 ? 0.1521 0.1371 0.1247 -0.0040 -0.0459 0.0056 327 LEU A CG 2471 C CD1 . LEU A 327 ? 0.1671 0.1797 0.1454 -0.0008 -0.0674 -0.0181 327 LEU A CD1 2472 C CD2 . LEU A 327 ? 0.1956 0.2103 0.1117 -0.0157 -0.0238 -0.0007 327 LEU A CD2 2473 N N . THR A 328 ? 0.1329 0.1705 0.1230 -0.0055 -0.0509 -0.0081 328 THR A N 2474 C CA . THR A 328 ? 0.1346 0.1576 0.1159 0.0080 -0.0489 -0.0186 328 THR A CA 2475 C C . THR A 328 ? 0.1356 0.1555 0.1095 0.0187 -0.0450 -0.0088 328 THR A C 2476 O O . THR A 328 ? 0.1187 0.1749 0.1089 0.0068 -0.0385 -0.0113 328 THR A O 2477 C CB . THR A 328 ? 0.1201 0.1446 0.1605 0.0039 -0.0478 -0.0298 328 THR A CB 2478 O OG1 . THR A 328 ? 0.1323 0.1675 0.2324 0.0076 -0.0604 -0.0547 328 THR A OG1 2479 C CG2 . THR A 328 ? 0.1185 0.1938 0.2261 -0.0141 -0.0553 -0.0288 328 THR A CG2 2480 N N . THR A 329 ? 0.1501 0.2445 0.1078 0.0140 -0.0406 -0.0035 329 THR A N 2481 C CA . THR A 329 ? 0.1538 0.2566 0.1211 0.0482 -0.0175 0.0267 329 THR A CA 2482 C C . THR A 329 ? 0.1505 0.2599 0.1246 0.0453 -0.0223 0.0380 329 THR A C 2483 O O . THR A 329 ? 0.1668 0.3332 0.1556 0.0460 -0.0524 0.0643 329 THR A O 2484 C CB . THR A 329 ? 0.2112 0.3081 0.1288 0.0949 -0.0162 0.0072 329 THR A CB 2485 O OG1 . THR A 329 ? 0.2981 0.3042 0.1311 0.1010 -0.0344 -0.0116 329 THR A OG1 2486 C CG2 . THR A 329 ? 0.2318 0.4144 0.1860 0.1279 0.0488 0.0625 329 THR A CG2 2487 N N . GLN A 330 ? 0.1443 0.2654 0.1159 0.0437 -0.0090 0.0398 330 GLN A N 2488 C CA . GLN A 330 ? 0.1633 0.2611 0.1506 0.0476 -0.0015 0.0484 330 GLN A CA 2489 C C . GLN A 330 ? 0.1696 0.2404 0.1517 0.0400 -0.0093 0.0579 330 GLN A C 2490 O O . GLN A 330 ? 0.1772 0.2800 0.1194 0.0437 -0.0188 0.0227 330 GLN A O 2491 C CB . GLN A 330 ? 0.1946 0.2526 0.1913 0.0517 -0.0097 0.0255 330 GLN A CB 2492 C CG . GLN A 330 ? 0.4758 0.3048 0.1721 0.0693 0.0068 -0.0093 330 GLN A CG 2493 C CD . GLN A 330 ? 0.5540 0.3514 0.2725 0.1694 -0.1706 -0.0835 330 GLN A CD 2494 O OE1 . GLN A 330 ? 0.4129 0.3009 0.2344 0.0794 -0.0164 0.0368 330 GLN A OE1 2495 N NE2 . GLN A 330 ? 0.4767 0.4671 0.3080 0.2036 -0.1525 -0.1174 330 GLN A NE2 2496 N N . PRO A 331 ? 0.1572 0.2430 0.1615 0.0102 -0.0242 0.0618 331 PRO A N 2497 C CA . PRO A 331 ? 0.1509 0.3087 0.1533 -0.0156 -0.0471 0.0706 331 PRO A CA 2498 C C . PRO A 331 ? 0.1644 0.3002 0.1333 -0.0295 -0.0421 0.0464 331 PRO A C 2499 O O . PRO A 331 ? 0.1988 0.2627 0.1675 -0.0281 -0.0453 0.0385 331 PRO A O 2500 C CB . PRO A 331 ? 0.1802 0.4306 0.2165 0.0503 -0.0631 0.0909 331 PRO A CB 2501 C CG . PRO A 331 ? 0.2471 0.5532 0.2368 0.1572 -0.0291 0.0628 331 PRO A CG 2502 C CD . PRO A 331 ? 0.1770 0.3619 0.2230 0.0844 0.0103 0.1389 331 PRO A CD 2503 N N . GLY A 332 ? 0.1834 0.2962 0.1459 -0.0405 -0.0306 0.0437 332 GLY A N 2504 C CA . GLY A 332 ? 0.2340 0.3145 0.1555 -0.0584 0.0052 0.0526 332 GLY A CA 2505 C C . GLY A 332 ? 0.1892 0.4177 0.1494 -0.0503 -0.0339 -0.0547 332 GLY A C 2506 O O . GLY A 332 ? 0.2724 0.2860 0.4208 -0.0328 0.0604 -0.0382 332 GLY A O 2507 N N . ALA A 333 ? 0.1617 0.7260 0.1562 -0.0732 -0.0279 -0.0836 333 ALA A N 2508 C CA . ALA A 333 ? 0.2404 0.6881 0.3672 -0.1798 0.0580 -0.3322 333 ALA A CA 2509 C C . ALA A 333 ? 0.2118 0.3280 0.3286 -0.0594 0.0588 -0.1635 333 ALA A C 2510 O O . ALA A 333 ? 0.4420 0.3283 0.7644 0.0399 0.0659 -0.2599 333 ALA A O 2511 C CB . ALA A 333 ? 0.2492 1.2195 0.3744 -0.2240 0.0526 -0.4475 333 ALA A CB 2512 N N . SER A 334 ? 0.1872 0.2597 0.1342 -0.0414 -0.0591 -0.0024 334 SER A N 2513 C CA . SER A 334 ? 0.1674 0.2788 0.1296 0.0042 -0.0417 -0.0313 334 SER A CA 2514 C C . SER A 334 ? 0.1481 0.1577 0.1476 0.0020 -0.0455 -0.0273 334 SER A C 2515 O O . SER A 334 ? 0.1354 0.1833 0.1534 0.0095 -0.0494 -0.0194 334 SER A O 2516 C CB . SER A 334 ? 0.2352 0.3887 0.1760 -0.0898 0.0107 -0.0586 334 SER A CB 2517 O OG . SER A 334 ? 0.2851 0.3687 0.1980 -0.0625 -0.0200 0.0561 334 SER A OG 2518 N N . GLN A 335 ? 0.1455 0.1681 0.1286 0.0177 -0.0340 -0.0183 335 GLN A N 2519 C CA . GLN A 335 ? 0.1284 0.1464 0.1216 0.0102 -0.0203 -0.0113 335 GLN A CA 2520 C C . GLN A 335 ? 0.1318 0.1459 0.1169 0.0174 -0.0322 0.0012 335 GLN A C 2521 O O . GLN A 335 ? 0.1496 0.1506 0.1366 0.0150 -0.0273 0.0048 335 GLN A O 2522 C CB . GLN A 335 ? 0.1522 0.1332 0.1273 0.0142 -0.0371 0.0037 335 GLN A CB 2523 C CG . GLN A 335 ? 0.1264 0.1784 0.1212 0.0249 -0.0131 0.0166 335 GLN A CG 2524 C CD . GLN A 335 ? 0.1208 0.1275 0.1057 0.0192 -0.0020 0.0238 335 GLN A CD 2525 O OE1 . GLN A 335 ? 0.1871 0.1661 0.1870 0.0112 -0.0112 -0.0440 335 GLN A OE1 2526 N NE2 . GLN A 335 ? 0.1149 0.1073 0.0747 0.0040 -0.0217 0.0085 335 GLN A NE2 2527 N N . SER A 336 ? 0.1389 0.1378 0.1227 0.0215 -0.0321 -0.0075 336 SER A N 2528 C CA . SER A 336 ? 0.1610 0.1321 0.1250 0.0192 -0.0436 -0.0090 336 SER A CA 2529 C C . SER A 336 ? 0.1565 0.1213 0.1162 0.0150 -0.0297 0.0017 336 SER A C 2530 O O . SER A 336 ? 0.1710 0.1257 0.1411 0.0134 -0.0452 0.0142 336 SER A O 2531 C CB . SER A 336 ? 0.1560 0.1682 0.1863 0.0475 -0.0323 -0.0258 336 SER A CB 2532 O OG . SER A 336 ? 0.1619 0.1993 0.2092 0.0384 -0.0404 -0.0110 336 SER A OG 2533 N N . LEU A 337 ? 0.1777 0.1228 0.0821 0.0142 -0.0350 0.0004 337 LEU A N 2534 C CA . LEU A 337 ? 0.1658 0.1235 0.0825 0.0127 -0.0306 -0.0025 337 LEU A CA 2535 C C . LEU A 337 ? 0.1550 0.1272 0.0889 0.0310 -0.0315 -0.0012 337 LEU A C 2536 O O . LEU A 337 ? 0.1540 0.2177 0.0960 0.0479 -0.0267 -0.0006 337 LEU A O 2537 C CB . LEU A 337 ? 0.2072 0.1191 0.0949 0.0075 -0.0310 0.0032 337 LEU A CB 2538 C CG . LEU A 337 ? 0.2063 0.1424 0.1136 -0.0017 -0.0181 0.0152 337 LEU A CG 2539 C CD1 . LEU A 337 ? 0.3063 0.1481 0.1588 0.0135 0.0211 0.0494 337 LEU A CD1 2540 C CD2 . LEU A 337 ? 0.2246 0.1583 0.1470 0.0162 0.0037 0.0099 337 LEU A CD2 2541 N N . ILE A 338 ? 0.1359 0.1103 0.0787 0.0154 -0.0186 0.0034 338 ILE A N 2542 C CA . ILE A 338 ? 0.1281 0.1184 0.0733 0.0089 -0.0222 0.0001 338 ILE A CA 2543 C C . ILE A 338 ? 0.1316 0.1156 0.0713 0.0085 -0.0172 0.0099 338 ILE A C 2544 O O . ILE A 338 ? 0.1376 0.1158 0.0816 -0.0018 -0.0093 0.0032 338 ILE A O 2545 C CB . ILE A 338 ? 0.1214 0.1134 0.0828 -0.0019 -0.0081 0.0040 338 ILE A CB 2546 C CG1 . ILE A 338 ? 0.1444 0.1176 0.0902 -0.0044 -0.0179 0.0112 338 ILE A CG1 2547 C CG2 . ILE A 338 ? 0.1244 0.1332 0.0755 -0.0005 -0.0083 0.0049 338 ILE A CG2 2548 C CD1 . ILE A 338 ? 0.1698 0.1181 0.1129 0.0134 -0.0136 0.0022 338 ILE A CD1 2549 N N . ALA A 339 ? 0.1390 0.1130 0.1061 0.0147 -0.0284 -0.0026 339 ALA A N 2550 C CA . ALA A 339 ? 0.1638 0.1077 0.1121 0.0084 -0.0320 -0.0018 339 ALA A CA 2551 C C . ALA A 339 ? 0.1632 0.0930 0.0930 0.0091 -0.0231 -0.0014 339 ALA A C 2552 O O . ALA A 339 ? 0.1438 0.1080 0.0986 -0.0030 -0.0102 0.0015 339 ALA A O 2553 C CB . ALA A 339 ? 0.1933 0.1331 0.2067 0.0547 -0.0624 -0.0157 339 ALA A CB 2554 N N . HIS A 340 ? 0.1478 0.1018 0.0842 0.0079 -0.0210 0.0063 340 HIS A N 2555 C CA . HIS A 340 ? 0.1500 0.0874 0.0822 0.0031 -0.0183 0.0049 340 HIS A CA 2556 C C . HIS A 340 ? 0.1477 0.0922 0.0840 0.0029 -0.0131 0.0087 340 HIS A C 2557 O O . HIS A 340 ? 0.1547 0.0857 0.0847 -0.0037 -0.0132 0.0071 340 HIS A O 2558 C CB . HIS A 340 ? 0.1489 0.0986 0.0909 0.0036 -0.0025 0.0088 340 HIS A CB 2559 C CG . HIS A 340 ? 0.1433 0.0910 0.0999 -0.0020 -0.0049 0.0167 340 HIS A CG 2560 N ND1 . HIS A 340 ? 0.1550 0.0911 0.1128 -0.0064 -0.0168 0.0086 340 HIS A ND1 2561 C CD2 . HIS A 340 ? 0.1879 0.0949 0.1137 -0.0070 -0.0159 0.0067 340 HIS A CD2 2562 C CE1 . HIS A 340 ? 0.1596 0.1050 0.1420 -0.0103 -0.0318 0.0058 340 HIS A CE1 2563 N NE2 . HIS A 340 ? 0.1945 0.1054 0.1548 -0.0222 -0.0388 0.0066 340 HIS A NE2 2564 N N . CYS A 341 ? 0.1551 0.1237 0.1034 0.0238 -0.0205 -0.0046 341 CYS A N 2565 C CA . CYS A 341 ? 0.1787 0.1398 0.1098 0.0413 -0.0203 -0.0149 341 CYS A CA 2566 C C . CYS A 341 ? 0.1687 0.1429 0.1425 0.0438 -0.0012 0.0012 341 CYS A C 2567 O O . CYS A 341 ? 0.1521 0.2106 0.1618 0.0504 -0.0168 0.0008 341 CYS A O 2568 C CB . CYS A 341 ? 0.1924 0.1327 0.1436 0.0356 -0.0220 -0.0150 341 CYS A CB 2569 S SG . CYS A 341 ? 0.2115 0.1711 0.1540 0.0090 -0.0214 -0.0220 341 CYS A SG 2570 N N . PRO A 342 ? 0.2205 0.1500 0.1564 0.0511 0.0257 0.0006 342 PRO A N 2571 C CA . PRO A 342 ? 0.2410 0.1549 0.2251 0.0583 0.0722 0.0516 342 PRO A CA 2572 C C . PRO A 342 ? 0.2042 0.1638 0.3033 0.0555 0.0568 0.0559 342 PRO A C 2573 O O . PRO A 342 ? 0.2085 0.2721 0.4626 0.0228 0.0481 0.1022 342 PRO A O 2574 C CB . PRO A 342 ? 0.3788 0.2135 0.2280 0.1289 0.1313 0.0621 342 PRO A CB 2575 C CG . PRO A 342 ? 0.4388 0.2014 0.1589 0.0647 0.0702 0.0074 342 PRO A CG 2576 C CD . PRO A 342 ? 0.3285 0.1386 0.1405 0.0512 0.0033 -0.0021 342 PRO A CD 2577 N N . ASP A 343 ? 0.1985 0.1997 0.2747 0.0676 0.0493 0.0841 343 ASP A N 2578 C CA . ASP A 343 ? 0.2137 0.2197 0.3877 0.0746 -0.0044 0.0994 343 ASP A CA 2579 C C . ASP A 343 ? 0.2031 0.3861 0.3677 0.0994 -0.0624 0.0897 343 ASP A C 2580 O O . ASP A 343 ? 0.2338 0.3844 0.4342 0.1103 -0.0620 0.1625 343 ASP A O 2581 C CB . ASP A 343 ? 0.2748 0.2181 0.5696 0.0573 -0.1183 0.0985 343 ASP A CB 2582 C CG . ASP A 343 ? 0.2891 0.2827 0.8411 -0.0232 -0.1924 0.1277 343 ASP A CG 2583 O OD1 . ASP A 343 ? 0.5668 0.2787 0.8442 -0.0825 -0.2054 0.1613 343 ASP A OD1 2584 O OD2 . ASP A 343 ? 0.2551 0.4497 1.2408 0.0850 -0.0643 0.4305 343 ASP A OD2 2585 N N . GLY A 344 ? 0.1968 0.5515 0.2943 0.1716 -0.0220 0.1001 344 GLY A N 2586 C CA . GLY A 344 ? 0.2127 0.5431 0.2945 0.1112 -0.0246 0.0945 344 GLY A CA 2587 C C . GLY A 344 ? 0.2695 0.5325 0.2893 0.0963 -0.0012 0.1070 344 GLY A C 2588 O O . GLY A 344 ? 0.5149 0.3803 0.3278 0.0871 0.1041 0.1349 344 GLY A O 2589 N N . SER A 345 ? 0.2928 0.5974 0.2203 0.0486 0.0014 0.1135 345 SER A N 2590 C CA . SER A 345 ? 0.3395 0.3481 0.3021 0.1604 0.0563 0.1463 345 SER A CA 2591 C C . SER A 345 ? 0.2822 0.2551 0.2055 0.0513 -0.0190 0.0823 345 SER A C 2592 O O . SER A 345 ? 0.3007 0.2368 0.1418 0.0939 -0.0093 0.0586 345 SER A O 2593 C CB . SER A 345 ? 0.4491 0.3873 0.3324 0.2119 -0.0888 0.0656 345 SER A CB 2594 O OG . SER A 345 ? 0.5104 0.4797 0.5813 -0.2209 -0.2500 0.1665 345 SER A OG 2595 N N . MET A 346 ? 0.3044 0.3304 0.4493 -0.0367 -0.1216 0.2119 346 MET A N 2596 C CA . MET A 346 ? 0.3083 0.3520 0.2114 -0.0847 -0.0481 0.0520 346 MET A CA 2597 C C . MET A 346 ? 0.2876 0.3821 0.1384 0.0916 -0.0383 -0.0720 346 MET A C 2598 O O . MET A 346 ? 0.3081 0.2730 0.2077 0.0607 -0.0422 -0.0342 346 MET A O 2599 C CB . MET A 346 ? 0.7068 0.7876 0.0968 -0.0971 0.0213 0.0202 346 MET A CB 2600 C CG . MET A 346 ? 1.0379 0.8306 0.1661 -0.3024 -0.0658 -0.0182 346 MET A CG 2601 S SD . MET A 346 ? 2.0726 0.7382 2.0000 0.4433 -1.0738 -0.7411 346 MET A SD 2602 C CE . MET A 346 ? 1.7399 0.8031 1.1136 -0.1066 -1.1510 -0.2711 346 MET A CE 2603 N N . SER A 347 ? 0.4328 0.3237 0.1636 0.1415 -0.0250 0.0049 347 SER A N 2604 C CA . SER A 347 ? 0.6695 0.2311 0.1752 0.0165 -0.0167 0.0061 347 SER A CA 2605 C C . SER A 347 ? 0.4649 0.2815 0.1802 0.1204 -0.0716 0.0271 347 SER A C 2606 O O . SER A 347 ? 0.5448 0.3396 0.4151 0.2027 -0.0679 0.1251 347 SER A O 2607 C CB . SER A 347 ? 0.7687 0.3285 0.2792 0.0038 0.0274 0.1086 347 SER A CB 2608 O OG . SER A 347 ? 1.1933 0.3965 0.3207 0.0787 0.2189 0.1011 347 SER A OG 2609 N N . CYS A 348 ? 0.3747 0.1891 0.1613 0.0228 -0.0526 0.0379 348 CYS A N 2610 C CA . CYS A 348 ? 0.3521 0.1261 0.1901 0.0322 -0.0510 -0.0180 348 CYS A CA 2611 C C . CYS A 348 ? 0.3334 0.1119 0.1707 -0.0085 -0.0458 -0.0244 348 CYS A C 2612 O O . CYS A 348 ? 0.3008 0.1545 0.1427 -0.0101 -0.0347 -0.0125 348 CYS A O 2613 C CB . CYS A 348 ? 0.2944 0.1730 0.1785 0.0335 -0.0537 -0.0362 348 CYS A CB 2614 S SG . CYS A 348 ? 0.2599 0.1349 0.1831 0.0231 -0.0643 0.0001 348 CYS A SG 2615 N N . PRO A 349 ? 0.4168 0.1397 0.2126 -0.0655 -0.0550 -0.0306 349 PRO A N 2616 C CA . PRO A 349 ? 0.3379 0.2039 0.1592 -0.0748 0.0048 -0.0527 349 PRO A CA 2617 C C . PRO A 349 ? 0.3224 0.2390 0.1840 -0.0186 0.0076 -0.0895 349 PRO A C 2618 O O . PRO A 349 ? 0.3905 0.3835 0.2979 0.0857 -0.0289 -0.1954 349 PRO A O 2619 C CB . PRO A 349 ? 0.3809 0.1821 0.3297 -0.0807 0.0354 -0.0303 349 PRO A CB 2620 C CG . PRO A 349 ? 0.4793 0.1550 0.5377 -0.0925 -0.0866 -0.0209 349 PRO A CG 2621 C CD . PRO A 349 ? 0.5454 0.1272 0.3482 -0.0917 -0.0813 0.0185 349 PRO A CD 2622 N N . GLY A 350 ? 0.2567 0.3036 0.1243 -0.0745 0.0142 -0.0654 350 GLY A N 2623 C CA . GLY A 350 ? 0.2405 0.3439 0.1341 -0.1169 0.0232 -0.1024 350 GLY A CA 2624 C C . GLY A 350 ? 0.1570 0.2221 0.1150 -0.0450 0.0021 -0.0248 350 GLY A C 2625 O O . GLY A 350 ? 0.2297 0.3918 0.1395 -0.1466 0.0451 -0.0974 350 GLY A O 2626 N N . VAL A 351 ? 0.1359 0.1215 0.1042 -0.0256 -0.0153 0.0009 351 VAL A N 2627 C CA . VAL A 351 ? 0.1332 0.0919 0.0976 -0.0069 -0.0147 0.0102 351 VAL A CA 2628 C C . VAL A 351 ? 0.1318 0.0751 0.1016 -0.0156 -0.0057 0.0025 351 VAL A C 2629 O O . VAL A 351 ? 0.1497 0.0884 0.1178 -0.0214 -0.0212 0.0126 351 VAL A O 2630 C CB . VAL A 351 ? 0.1543 0.0885 0.1119 -0.0084 0.0020 0.0110 351 VAL A CB 2631 C CG1 . VAL A 351 ? 0.1816 0.1100 0.1229 -0.0161 0.0037 -0.0188 351 VAL A CG1 2632 C CG2 . VAL A 351 ? 0.1653 0.1217 0.1314 0.0220 0.0198 0.0224 351 VAL A CG2 2633 N N . GLN A 352 ? 0.1330 0.0809 0.1083 -0.0085 -0.0167 0.0164 352 GLN A N 2634 C CA . GLN A 352 ? 0.1359 0.0894 0.1147 0.0006 -0.0086 0.0163 352 GLN A CA 2635 C C . GLN A 352 ? 0.1185 0.1077 0.1151 -0.0014 -0.0086 0.0272 352 GLN A C 2636 O O . GLN A 352 ? 0.1596 0.1263 0.1313 -0.0288 -0.0084 0.0362 352 GLN A O 2637 C CB . GLN A 352 ? 0.1509 0.1165 0.1127 0.0124 0.0070 0.0255 352 GLN A CB 2638 C CG . GLN A 352 ? 0.1539 0.1345 0.1423 0.0234 0.0131 0.0337 352 GLN A CG 2639 C CD . GLN A 352 ? 0.1655 0.1049 0.1386 0.0257 -0.0009 0.0263 352 GLN A CD 2640 O OE1 . GLN A 352 ? 0.1923 0.1393 0.1385 0.0337 0.0091 0.0230 352 GLN A OE1 2641 N NE2 . GLN A 352 ? 0.1821 0.1116 0.1322 0.0197 -0.0029 0.0307 352 GLN A NE2 2642 N N . PHE A 353 ? 0.1377 0.0912 0.1149 -0.0046 -0.0172 0.0168 353 PHE A N 2643 C CA . PHE A 353 ? 0.1343 0.0987 0.1186 0.0003 -0.0259 0.0214 353 PHE A CA 2644 C C . PHE A 353 ? 0.1335 0.1082 0.1180 0.0022 -0.0109 0.0329 353 PHE A C 2645 O O . PHE A 353 ? 0.1623 0.1094 0.1624 0.0169 -0.0208 0.0187 353 PHE A O 2646 C CB . PHE A 353 ? 0.1388 0.0901 0.1159 0.0050 -0.0244 0.0216 353 PHE A CB 2647 C CG . PHE A 353 ? 0.1396 0.0932 0.1217 0.0058 -0.0276 0.0144 353 PHE A CG 2648 C CD1 . PHE A 353 ? 0.1538 0.0909 0.2955 0.0041 -0.0235 0.0230 353 PHE A CD1 2649 C CD2 . PHE A 353 ? 0.1500 0.0955 0.2147 0.0054 0.0069 0.0131 353 PHE A CD2 2650 C CE1 . PHE A 353 ? 0.1512 0.0947 0.2715 0.0050 -0.0122 0.0295 353 PHE A CE1 2651 C CE2 . PHE A 353 ? 0.1592 0.0959 0.2678 -0.0004 0.0233 -0.0049 353 PHE A CE2 2652 C CZ . PHE A 353 ? 0.1511 0.1001 0.1605 0.0011 -0.0292 0.0045 353 PHE A CZ 2653 N N . ASN A 354 ? 0.1391 0.1226 0.1705 0.0015 -0.0216 0.0439 354 ASN A N 2654 C CA . ASN A 354 ? 0.1339 0.1551 0.1580 0.0151 0.0006 0.0508 354 ASN A CA 2655 C C . ASN A 354 ? 0.1391 0.1221 0.1496 0.0014 -0.0134 0.0320 354 ASN A C 2656 O O . ASN A 354 ? 0.1696 0.1410 0.1613 0.0047 0.0063 0.0320 354 ASN A O 2657 C CB . ASN A 354 ? 0.1352 0.2677 0.2631 -0.0159 0.0007 0.1360 354 ASN A CB 2658 C CG . ASN A 354 ? 0.3090 0.4455 0.3338 0.0977 0.1054 0.2838 354 ASN A CG 2659 O OD1 . ASN A 354 ? 0.8692 0.5725 0.7325 0.0497 0.2451 0.5114 354 ASN A OD1 2660 N ND2 . ASN A 354 ? 0.3812 0.9010 0.2084 -0.1054 0.0546 0.1909 354 ASN A ND2 2661 N N . GLY A 355 ? 0.1386 0.1287 0.1633 0.0000 -0.0260 0.0388 355 GLY A N 2662 C CA . GLY A 355 ? 0.1524 0.1166 0.1471 0.0017 -0.0213 0.0299 355 GLY A CA 2663 C C . GLY A 355 ? 0.1376 0.1224 0.1638 -0.0018 -0.0222 0.0418 355 GLY A C 2664 O O . GLY A 355 ? 0.1439 0.1684 0.1850 0.0101 -0.0135 0.0453 355 GLY A O 2665 N N . PRO A 356 ? 0.1354 0.1203 0.1646 -0.0068 -0.0350 0.0266 356 PRO A N 2666 C CA . PRO A 356 ? 0.1288 0.1309 0.1801 -0.0101 -0.0467 0.0344 356 PRO A CA 2667 C C . PRO A 356 ? 0.1253 0.1231 0.2032 -0.0026 -0.0457 0.0352 356 PRO A C 2668 O O . PRO A 356 ? 0.1323 0.1607 0.2638 0.0093 -0.0626 0.0240 356 PRO A O 2669 C CB . PRO A 356 ? 0.1557 0.1642 0.1850 -0.0204 -0.0660 0.0389 356 PRO A CB 2670 C CG . PRO A 356 ? 0.1770 0.1485 0.1525 -0.0110 -0.0452 0.0333 356 PRO A CG 2671 C CD . PRO A 356 ? 0.1695 0.1182 0.1540 -0.0023 -0.0286 0.0170 356 PRO A CD 2672 N N . ALA A 357 ? 0.1210 0.1306 0.1691 -0.0075 -0.0339 0.0177 357 ALA A N 2673 C CA . ALA A 357 ? 0.1426 0.1375 0.1756 0.0002 -0.0578 0.0089 357 ALA A CA 2674 C C . ALA A 357 ? 0.1876 0.2152 0.1721 0.0169 -0.0357 -0.0028 357 ALA A C 2675 O O . ALA A 357 ? 0.2441 0.3558 0.2655 0.1155 -0.0403 -0.0597 357 ALA A O 2676 C CB . ALA A 357 ? 0.1471 0.1300 0.1968 -0.0091 -0.0538 0.0055 357 ALA A CB 2677 O OXT . ALA A 357 ? 0.2472 0.3212 0.1929 0.0290 -0.0231 0.0660 357 ALA A OXT 2678 C C1 . NAG B . ? 0.1497 0.1232 0.1255 -0.0392 -0.0253 -0.0078 361 NAG A C1 2679 C C2 . NAG B . ? 0.1532 0.1216 0.1247 -0.0287 -0.0341 -0.0088 361 NAG A C2 2680 C C3 . NAG B . ? 0.1800 0.1244 0.1318 -0.0365 -0.0343 0.0017 361 NAG A C3 2681 C C4 . NAG B . ? 0.1830 0.1243 0.1293 -0.0506 -0.0330 -0.0075 361 NAG A C4 2682 C C5 . NAG B . ? 0.2012 0.1330 0.1337 -0.0614 0.0080 -0.0256 361 NAG A C5 2683 C C6 . NAG B . ? 0.2142 0.1539 0.2392 -0.0588 0.0471 -0.0260 361 NAG A C6 2684 C C7 . NAG B . ? 0.1501 0.1326 0.1226 -0.0051 -0.0231 -0.0090 361 NAG A C7 2685 C C8 . NAG B . ? 0.1602 0.1574 0.1357 -0.0213 -0.0158 -0.0075 361 NAG A C8 2686 N N2 . NAG B . ? 0.1583 0.1493 0.1158 -0.0245 -0.0247 -0.0045 361 NAG A N2 2687 O O3 . NAG B . ? 0.2070 0.1244 0.1739 -0.0318 -0.0232 -0.0088 361 NAG A O3 2688 O O4 . NAG B . ? 0.1986 0.1491 0.1369 -0.0605 -0.0199 -0.0105 361 NAG A O4 2689 O O5 . NAG B . ? 0.1589 0.1285 0.1398 -0.0353 -0.0137 -0.0148 361 NAG A O5 2690 O O6 . NAG B . ? 0.1730 0.2331 0.3004 -0.0605 0.0158 -0.0407 361 NAG A O6 2691 O O7 . NAG B . ? 0.1708 0.1866 0.1208 -0.0300 -0.0283 0.0049 361 NAG A O7 2692 C C1 . NAG C . ? 0.1981 0.1352 0.1776 -0.0667 -0.0304 0.0037 362 NAG A C1 2693 C C2 . NAG C . ? 0.1975 0.1889 0.1838 -0.0684 -0.0247 0.0190 362 NAG A C2 2694 C C3 . NAG C . ? 0.2408 0.1614 0.2458 -0.0688 -0.0212 0.0607 362 NAG A C3 2695 C C4 . NAG C . ? 0.2291 0.1574 0.2540 -0.0665 -0.0481 0.0374 362 NAG A C4 2696 C C5 . NAG C . ? 0.2484 0.1338 0.1992 -0.0586 -0.0401 -0.0007 362 NAG A C5 2697 C C6 . NAG C . ? 0.2691 0.1438 0.2225 -0.0552 -0.0204 -0.0205 362 NAG A C6 2698 C C7 . NAG C . ? 0.1671 0.1858 0.2182 -0.0624 -0.0339 0.0172 362 NAG A C7 2699 C C8 . NAG C . ? 0.1812 0.2147 0.3039 -0.0355 -0.0616 -0.0028 362 NAG A C8 2700 N N2 . NAG C . ? 0.2102 0.1781 0.2028 -0.0741 -0.0152 0.0354 362 NAG A N2 2701 O O3 . NAG C . ? 0.3012 0.1969 0.2748 -0.0615 0.0117 0.0697 362 NAG A O3 2702 O O4 . NAG C . ? 0.2646 0.1409 0.3714 -0.0558 -0.1017 0.0329 362 NAG A O4 2703 O O5 . NAG C . ? 0.2224 0.1481 0.1669 -0.0562 -0.0254 -0.0061 362 NAG A O5 2704 O O6 . NAG C . ? 0.2605 0.1724 0.2294 -0.0643 -0.0156 -0.0234 362 NAG A O6 2705 O O7 . NAG C . ? 0.1915 0.1695 0.2104 -0.0482 -0.0459 0.0064 362 NAG A O7 2706 C C1 . MAN D . ? 0.2071 0.1846 0.2395 0.0277 -0.0726 0.0157 364 MAN A C1 2707 C C2 . MAN D . ? 0.1754 0.2336 0.3165 0.0512 -0.0562 0.0190 364 MAN A C2 2708 C C3 . MAN D . ? 0.2229 0.2519 0.2429 -0.0198 -0.1005 0.0427 364 MAN A C3 2709 C C4 . MAN D . ? 0.2465 0.2006 0.2324 -0.0052 -0.0948 0.0281 364 MAN A C4 2710 C C5 . MAN D . ? 0.2239 0.1914 0.1915 0.0189 -0.0843 0.0339 364 MAN A C5 2711 C C6 . MAN D . ? 0.2482 0.2693 0.2126 0.0028 -0.0704 0.0744 364 MAN A C6 2712 O O2 . MAN D . ? 0.2121 0.2733 0.3870 0.0441 -0.1083 0.0553 364 MAN A O2 2713 O O3 . MAN D . ? 0.2042 0.3127 0.3984 0.0140 -0.1344 0.0384 364 MAN A O3 2714 O O4 . MAN D . ? 0.2633 0.2302 0.3271 0.0335 -0.1214 -0.0369 364 MAN A O4 2715 O O5 . MAN D . ? 0.1948 0.1648 0.2605 0.0150 -0.0763 0.0203 364 MAN A O5 2716 O O6 A MAN D . ? 0.3216 0.3293 0.2693 -0.1238 -0.1150 0.1511 364 MAN A O6 2717 O O6 B MAN D . ? 0.2646 0.5879 0.4997 -0.0762 -0.1603 0.3874 364 MAN A O6 2718 CA CA . CA E . ? 0.0768 0.0741 0.0749 0.0029 -0.0188 0.0042 371 CA A CA 2719 CA CA . CA F . ? 0.0696 0.0771 0.0719 -0.0028 -0.0157 0.0077 372 CA A CA 2720 MN MN . MN G . ? 0.1470 0.1325 0.1105 -0.0102 -0.0165 -0.0016 381 MN A MN 2721 C C1 . GOL H . ? 0.4177 0.5461 0.4494 0.1669 0.1978 -0.0576 391 GOL A C1 2722 O O1 . GOL H . ? 0.2742 0.5089 0.9866 0.1931 0.2007 0.3027 391 GOL A O1 2723 C C2 . GOL H . ? 0.1663 0.0510 0.0873 0.0122 -0.0378 -0.0031 391 GOL A C2 2724 O O2 . GOL H . ? 0.3477 0.1437 0.2626 -0.0122 -0.1403 -0.0383 391 GOL A O2 2725 C C3 . GOL H . ? 0.2635 0.1997 0.4784 -0.0243 -0.1670 -0.0466 391 GOL A C3 2726 O O3 . GOL H . ? 0.2287 0.2762 0.1749 -0.0846 -0.0733 0.0662 391 GOL A O3 2727 C CHA . HEM I . ? 0.0979 0.0807 0.0860 0.0040 -0.0051 0.0202 396 HEM A CHA 2728 C CHB . HEM I . ? 0.1021 0.0884 0.0809 0.0009 -0.0044 0.0028 396 HEM A CHB 2729 C CHC . HEM I . ? 0.0856 0.0872 0.1000 0.0049 -0.0045 0.0302 396 HEM A CHC 2730 C CHD . HEM I . ? 0.0897 0.0877 0.0860 -0.0015 -0.0045 0.0054 396 HEM A CHD 2731 C C1A . HEM I . ? 0.0923 0.0840 0.0831 0.0040 -0.0095 0.0157 396 HEM A C1A 2732 C C2A . HEM I . ? 0.0882 0.0899 0.0766 -0.0060 -0.0036 0.0060 396 HEM A C2A 2733 C C3A . HEM I . ? 0.0862 0.0972 0.0798 -0.0071 -0.0053 0.0024 396 HEM A C3A 2734 C C4A . HEM I . ? 0.0898 0.0913 0.0815 -0.0015 -0.0085 0.0108 396 HEM A C4A 2735 C CMA . HEM I . ? 0.0891 0.1144 0.1010 0.0020 -0.0014 0.0046 396 HEM A CMA 2736 C CAA . HEM I . ? 0.0834 0.0999 0.0751 -0.0080 -0.0066 0.0108 396 HEM A CAA 2737 C CBA . HEM I . ? 0.1029 0.1206 0.0878 -0.0206 -0.0069 0.0231 396 HEM A CBA 2738 C CGA . HEM I . ? 0.1016 0.1159 0.0842 -0.0285 -0.0201 0.0199 396 HEM A CGA 2739 O O1A . HEM I . ? 0.1056 0.1430 0.1202 -0.0176 0.0051 0.0223 396 HEM A O1A 2740 O O2A . HEM I . ? 0.1167 0.1207 0.0977 -0.0292 -0.0185 0.0267 396 HEM A O2A 2741 C C1B . HEM I . ? 0.0877 0.0864 0.0808 -0.0065 -0.0113 0.0011 396 HEM A C1B 2742 C C2B . HEM I . ? 0.0835 0.0849 0.0913 0.0058 -0.0192 0.0071 396 HEM A C2B 2743 C C3B . HEM I . ? 0.0852 0.0840 0.0993 0.0121 -0.0190 0.0136 396 HEM A C3B 2744 C C4B . HEM I . ? 0.1012 0.0831 0.0882 0.0036 -0.0032 0.0226 396 HEM A C4B 2745 C CMB . HEM I . ? 0.1027 0.0929 0.1059 0.0133 -0.0164 0.0053 396 HEM A CMB 2746 C CAB . HEM I . ? 0.1018 0.1055 0.1156 0.0088 -0.0061 0.0302 396 HEM A CAB 2747 C CBB A HEM I . ? 0.0963 0.0848 0.1010 -0.0017 -0.0001 0.0221 396 HEM A CBB 2748 C CBB B HEM I . ? 0.1482 0.1493 0.1608 -0.0563 -0.0335 0.0288 396 HEM A CBB 2749 C C1C . HEM I . ? 0.0876 0.0907 0.0916 0.0028 -0.0110 0.0218 396 HEM A C1C 2750 C C2C . HEM I . ? 0.0708 0.1030 0.0881 -0.0046 -0.0126 0.0227 396 HEM A C2C 2751 C C3C . HEM I . ? 0.0788 0.0968 0.0785 -0.0076 -0.0130 0.0159 396 HEM A C3C 2752 C C4C . HEM I . ? 0.0821 0.0901 0.0886 -0.0031 -0.0085 0.0151 396 HEM A C4C 2753 C CMC . HEM I . ? 0.0797 0.1138 0.1194 0.0033 -0.0004 0.0479 396 HEM A CMC 2754 C CAC . HEM I . ? 0.0853 0.1332 0.0836 0.0047 -0.0175 0.0159 396 HEM A CAC 2755 C CBC . HEM I . ? 0.1086 0.1369 0.1008 0.0074 -0.0041 0.0168 396 HEM A CBC 2756 C C1D . HEM I . ? 0.0826 0.0906 0.0862 -0.0018 -0.0114 0.0130 396 HEM A C1D 2757 C C2D . HEM I . ? 0.0829 0.0763 0.0778 -0.0031 -0.0176 0.0011 396 HEM A C2D 2758 C C3D . HEM I . ? 0.0950 0.0753 0.0761 0.0048 -0.0141 0.0061 396 HEM A C3D 2759 C C4D . HEM I . ? 0.0872 0.0825 0.0870 0.0031 -0.0085 0.0191 396 HEM A C4D 2760 C CMD . HEM I . ? 0.0966 0.0809 0.0845 0.0105 -0.0056 0.0020 396 HEM A CMD 2761 C CAD . HEM I . ? 0.1036 0.0768 0.0711 -0.0013 -0.0106 0.0050 396 HEM A CAD 2762 C CBD . HEM I . ? 0.1150 0.0973 0.0898 -0.0153 -0.0068 0.0061 396 HEM A CBD 2763 C CGD . HEM I . ? 0.1617 0.0701 0.1049 -0.0158 0.0188 -0.0128 396 HEM A CGD 2764 O O1D . HEM I . ? 0.2139 0.0842 0.1491 -0.0364 0.0331 -0.0193 396 HEM A O1D 2765 O O2D . HEM I . ? 0.2086 0.0791 0.0738 0.0110 0.0027 -0.0001 396 HEM A O2D 2766 N NA . HEM I . ? 0.0997 0.0856 0.0834 0.0045 -0.0034 0.0134 396 HEM A NA 2767 N NB . HEM I . ? 0.0838 0.0800 0.0925 0.0030 -0.0036 0.0147 396 HEM A NB 2768 N NC . HEM I . ? 0.0845 0.0816 0.1016 0.0084 -0.0082 0.0176 396 HEM A NC 2769 N ND . HEM I . ? 0.0883 0.0894 0.0939 0.0113 0.0073 0.0227 396 HEM A ND 2770 FE FE . HEM I . ? 0.0824 0.0787 0.0744 -0.0003 -0.0110 0.0093 396 HEM A FE 2771 O O . HOH J . ? 0.0977 0.1262 0.0887 0.0108 -0.0025 0.0170 1001 HOH A O 2772 O O . HOH J . ? 0.1209 0.1603 0.1214 -0.0085 0.0052 0.0161 1002 HOH A O 2773 O O . HOH J . ? 0.0864 0.0815 0.0935 0.0023 -0.0098 -0.0016 1003 HOH A O 2774 O O . HOH J . ? 0.0927 0.1170 0.0969 0.0100 -0.0071 -0.0076 1004 HOH A O 2775 O O . HOH J . ? 0.1110 0.1149 0.1056 -0.0028 -0.0209 0.0149 1005 HOH A O 2776 O O . HOH J . ? 0.1725 0.1140 0.1427 0.0356 -0.0789 -0.0087 1006 HOH A O 2777 O O . HOH J . ? 0.1700 0.0957 0.1224 0.0204 -0.0175 0.0062 1007 HOH A O 2778 O O . HOH J . ? 0.1294 0.1085 0.0800 -0.0116 -0.0072 0.0056 1008 HOH A O 2779 O O . HOH J . ? 0.2053 0.1622 0.1840 0.0162 0.0242 0.0288 1009 HOH A O 2780 O O . HOH J . ? 0.1056 0.1532 0.1042 -0.0157 -0.0191 0.0047 1010 HOH A O 2781 O O . HOH J . ? 0.1173 0.1126 0.1383 0.0123 -0.0309 -0.0235 1011 HOH A O 2782 O O . HOH J . ? 0.1079 0.1077 0.0879 -0.0039 -0.0200 -0.0028 1012 HOH A O 2783 O O . HOH J . ? 0.1376 0.2054 0.1292 0.0187 -0.0179 -0.0538 1013 HOH A O 2784 O O . HOH J . ? 0.1399 0.1214 0.1047 -0.0218 -0.0065 -0.0074 1014 HOH A O 2785 O O . HOH J . ? 0.1088 0.1895 0.1625 0.0038 -0.0257 -0.0056 1015 HOH A O 2786 O O . HOH J . ? 0.1148 0.0944 0.0946 -0.0024 -0.0153 0.0013 1016 HOH A O 2787 O O . HOH J . ? 0.1266 0.1164 0.0810 -0.0028 -0.0101 0.0020 1017 HOH A O 2788 O O . HOH J . ? 0.1138 0.1278 0.1040 -0.0050 -0.0011 0.0081 1018 HOH A O 2789 O O . HOH J . ? 0.1545 0.0963 0.1117 -0.0054 -0.0213 0.0191 1019 HOH A O 2790 O O . HOH J . ? 0.1373 0.1841 0.1478 0.0192 -0.0303 -0.0062 1020 HOH A O 2791 O O . HOH J . ? 0.1784 0.1384 0.1322 -0.0473 -0.0460 0.0065 1021 HOH A O 2792 O O . HOH J . ? 0.1365 0.1033 0.1319 0.0006 -0.0308 -0.0023 1022 HOH A O 2793 O O . HOH J . ? 0.1010 0.1359 0.1280 -0.0086 -0.0444 0.0198 1023 HOH A O 2794 O O . HOH J . ? 0.1137 0.1051 0.1224 -0.0004 -0.0241 -0.0231 1024 HOH A O 2795 O O . HOH J . ? 0.1891 0.1305 0.1412 0.0315 -0.0292 -0.0034 1025 HOH A O 2796 O O . HOH J . ? 0.1164 0.0838 0.0987 0.0038 -0.0153 -0.0059 1026 HOH A O 2797 O O . HOH J . ? 0.0831 0.1018 0.1047 0.0040 -0.0214 0.0024 1027 HOH A O 2798 O O . HOH J . ? 0.1900 0.1554 0.1420 0.0094 -0.0103 -0.0158 1028 HOH A O 2799 O O . HOH J . ? 0.0973 0.1106 0.1113 -0.0051 -0.0074 -0.0015 1029 HOH A O 2800 O O . HOH J . ? 0.1144 0.1188 0.1263 -0.0147 -0.0177 0.0131 1030 HOH A O 2801 O O . HOH J . ? 0.1035 0.1225 0.1096 -0.0024 -0.0226 0.0019 1031 HOH A O 2802 O O . HOH J . ? 0.1477 0.1288 0.1612 -0.0064 -0.0311 -0.0450 1032 HOH A O 2803 O O . HOH J . ? 0.1878 0.1689 0.5754 0.0409 -0.0467 -0.1385 1033 HOH A O 2804 O O . HOH J . ? 0.2167 0.1626 0.1512 -0.0219 0.0053 -0.0108 1034 HOH A O 2805 O O . HOH J . ? 0.1484 0.1958 0.1513 0.0088 -0.0307 0.0079 1035 HOH A O 2806 O O . HOH J . ? 0.1214 0.1107 0.1353 0.0131 0.0014 0.0044 1036 HOH A O 2807 O O . HOH J . ? 0.1573 0.1816 0.1497 -0.0015 -0.0713 -0.0241 1037 HOH A O 2808 O O . HOH J . ? 0.2019 0.1578 0.1263 0.0125 -0.0280 0.0555 1038 HOH A O 2809 O O . HOH J . ? 0.1447 0.1834 0.1332 -0.0003 -0.0113 0.0467 1039 HOH A O 2810 O O . HOH J . ? 0.1773 0.1303 0.1355 -0.0128 -0.0384 -0.0142 1040 HOH A O 2811 O O . HOH J . ? 0.1723 0.1216 0.2057 -0.0204 -0.0530 0.0494 1041 HOH A O 2812 O O . HOH J . ? 0.1175 0.1258 0.1347 -0.0064 -0.0061 -0.0153 1042 HOH A O 2813 O O . HOH J . ? 0.0814 0.1490 0.1218 -0.0101 -0.0355 0.0039 1043 HOH A O 2814 O O . HOH J . ? 0.1243 0.1348 0.1151 0.0135 -0.0161 0.0038 1044 HOH A O 2815 O O . HOH J . ? 0.2637 0.3575 0.1530 0.1477 0.0934 0.1211 1045 HOH A O 2816 O O . HOH J . ? 0.2636 0.4446 0.3415 -0.1302 -0.1079 0.1079 1046 HOH A O 2817 O O . HOH J . ? 0.1671 0.1206 0.1132 -0.0114 0.0078 -0.0073 1047 HOH A O 2818 O O . HOH J . ? 0.1257 0.1954 0.1207 -0.0137 0.0122 -0.0102 1048 HOH A O 2819 O O . HOH J . ? 0.2931 0.1401 0.1441 -0.0464 -0.0579 0.0174 1049 HOH A O 2820 O O . HOH J . ? 0.1135 0.1993 0.1191 0.0144 -0.0181 -0.0243 1050 HOH A O 2821 O O . HOH J . ? 0.5339 0.2580 0.2279 0.1580 0.1524 0.0425 1051 HOH A O 2822 O O . HOH J . ? 0.1398 0.1297 0.1344 -0.0109 -0.0216 0.0180 1052 HOH A O 2823 O O . HOH J . ? 0.1397 0.1017 0.1316 -0.0008 -0.0568 0.0033 1053 HOH A O 2824 O O . HOH J . ? 0.1875 0.1243 0.2572 -0.0081 -0.0132 0.0623 1054 HOH A O 2825 O O . HOH J . ? 0.1506 0.1648 0.1480 -0.0428 -0.0602 0.0426 1055 HOH A O 2826 O O . HOH J . ? 0.1227 0.1422 0.1774 0.0257 -0.0122 0.0261 1056 HOH A O 2827 O O . HOH J . ? 0.5423 0.3567 0.4060 0.0145 -0.0906 0.0151 1057 HOH A O 2828 O O . HOH J . ? 0.2282 0.1178 0.2266 -0.0129 0.0552 0.0199 1058 HOH A O 2829 O O . HOH J . ? 0.3455 0.5480 0.3849 0.1862 -0.0159 -0.1157 1059 HOH A O 2830 O O . HOH J . ? 0.1924 0.1267 0.1432 0.0071 0.0159 -0.0078 1060 HOH A O 2831 O O . HOH J . ? 0.2808 0.2772 0.3414 0.0312 -0.1386 -0.1703 1061 HOH A O 2832 O O . HOH J . ? 0.1926 0.1183 0.4306 0.0051 -0.0380 0.0086 1062 HOH A O 2833 O O . HOH J . ? 0.3436 0.1901 0.1884 -0.0282 0.0370 -0.0133 1063 HOH A O 2834 O O . HOH J . ? 0.1711 0.1645 0.1401 -0.0408 -0.0057 -0.0134 1064 HOH A O 2835 O O . HOH J . ? 0.2514 0.2382 0.1406 -0.0979 0.0169 -0.0364 1065 HOH A O 2836 O O . HOH J . ? 0.1017 0.3422 0.2185 -0.0687 -0.0618 0.1272 1066 HOH A O 2837 O O . HOH J . ? 0.2369 0.2095 0.1867 -0.0628 -0.0522 0.0216 1067 HOH A O 2838 O O . HOH J . ? 0.0916 0.2072 0.1216 -0.0177 -0.0260 0.0045 1068 HOH A O 2839 O O . HOH J . ? 0.0976 0.3859 0.1577 -0.0706 0.0045 -0.0938 1069 HOH A O 2840 O O . HOH J . ? 0.3200 0.1572 0.2686 -0.0936 -0.0774 -0.0346 1070 HOH A O 2841 O O . HOH J . ? 0.2365 0.1603 0.2000 -0.0078 -0.0431 -0.0082 1071 HOH A O 2842 O O . HOH J . ? 0.1014 0.1457 0.1098 0.0072 0.0019 0.0074 1072 HOH A O 2843 O O . HOH J . ? 0.4734 0.2330 0.1280 -0.1007 -0.0509 0.0076 1073 HOH A O 2844 O O . HOH J . ? 0.2066 0.2171 0.1680 0.0660 -0.0480 -0.0021 1074 HOH A O 2845 O O . HOH J . ? 0.1947 0.1627 0.1114 0.0151 -0.0060 0.0134 1075 HOH A O 2846 O O . HOH J . ? 0.3956 0.5142 0.2529 0.1770 0.1465 0.0909 1076 HOH A O 2847 O O . HOH J . ? 0.2867 0.3120 0.1755 -0.0198 -0.1115 -0.0706 1077 HOH A O 2848 O O . HOH J . ? 0.2054 0.2072 0.2448 0.0436 0.0364 -0.0170 1078 HOH A O 2849 O O . HOH J . ? 0.2380 0.4233 0.2694 0.0044 -0.0407 -0.1054 1079 HOH A O 2850 O O . HOH J . ? 0.1373 0.1800 0.2272 0.0174 0.0123 -0.0187 1080 HOH A O 2851 O O . HOH J . ? 0.1900 0.2505 0.2272 0.0316 -0.0548 -0.0152 1081 HOH A O 2852 O O . HOH J . ? 0.2874 0.2266 0.1889 -0.0234 -0.0460 0.0352 1082 HOH A O 2853 O O . HOH J . ? 0.1383 0.1321 0.1993 0.0159 -0.0274 -0.0009 1083 HOH A O 2854 O O . HOH J . ? 0.0965 0.0994 0.0959 0.0002 -0.0154 0.0047 1084 HOH A O 2855 O O . HOH J . ? 0.0864 0.0798 0.0816 -0.0032 -0.0114 0.0056 1085 HOH A O 2856 O O . HOH J . ? 0.1165 0.1014 0.1370 -0.0130 -0.0046 0.0025 1086 HOH A O 2857 O O . HOH J . ? 0.0879 0.0912 0.0943 -0.0077 -0.0323 0.0144 1087 HOH A O 2858 O O . HOH J . ? 0.1323 0.1197 0.1281 -0.0053 -0.0226 0.0052 1088 HOH A O 2859 O O . HOH J . ? 0.1082 0.1017 0.0887 0.0051 0.0046 -0.0005 1089 HOH A O 2860 O O . HOH J . ? 0.1489 0.1535 0.1343 -0.0388 -0.0257 0.0247 1090 HOH A O 2861 O O . HOH J . ? 0.1270 0.1262 0.1323 -0.0336 0.0250 -0.0460 1091 HOH A O 2862 O O . HOH J . ? 0.1717 0.1015 0.1746 -0.0099 -0.0141 -0.0008 1092 HOH A O 2863 O O . HOH J . ? 0.2465 0.1278 0.1320 0.0111 -0.0499 -0.0089 1093 HOH A O 2864 O O . HOH J . ? 0.1455 0.1583 0.1241 0.0126 -0.0173 -0.0146 1094 HOH A O 2865 O O . HOH J . ? 0.1311 0.1067 0.1553 -0.0063 -0.0400 -0.0094 1095 HOH A O 2866 O O . HOH J . ? 0.2690 0.1928 0.1798 -0.0241 -0.0143 0.0045 1096 HOH A O 2867 O O . HOH J . ? 0.1097 0.1124 0.1452 -0.0020 -0.0468 0.0006 1097 HOH A O 2868 O O . HOH J . ? 0.2378 0.2406 0.2223 0.0149 -0.0125 -0.0775 1098 HOH A O 2869 O O . HOH J . ? 0.1875 0.1604 0.1021 -0.0070 -0.0112 0.0312 1099 HOH A O 2870 O O . HOH J . ? 0.2190 0.4221 0.1987 0.0015 -0.0304 -0.0178 1100 HOH A O 2871 O O . HOH J . ? 0.1845 0.4045 0.1893 0.0175 -0.0208 -0.0395 1101 HOH A O 2872 O O . HOH J . ? 0.6088 0.1755 0.3981 0.0450 -0.2102 0.0341 1102 HOH A O 2873 O O . HOH J . ? 0.4585 0.3034 0.6770 -0.1645 0.3003 -0.2749 1103 HOH A O 2874 O O . HOH J . ? 0.2181 0.0960 0.1083 0.0013 -0.0404 0.0104 1104 HOH A O 2875 O O . HOH J . ? 0.1910 0.1233 0.1721 0.0342 -0.0101 0.0183 1105 HOH A O 2876 O O . HOH J . ? 0.3004 0.0783 0.3059 -0.0026 -0.1521 0.0099 1106 HOH A O 2877 O O . HOH J . ? 0.2660 0.2297 0.2157 -0.0118 -0.0802 -0.0214 1107 HOH A O 2878 O O . HOH J . ? 0.1515 0.1444 0.1683 -0.0175 -0.0240 -0.0366 1108 HOH A O 2879 O O . HOH J . ? 0.2146 0.1722 0.1688 -0.0378 -0.0007 -0.0185 1109 HOH A O 2880 O O . HOH J . ? 0.1871 0.1579 0.3240 0.0618 -0.0093 0.0496 1110 HOH A O 2881 O O . HOH J . ? 0.1992 0.2727 0.2212 -0.0624 -0.0114 0.0039 1111 HOH A O 2882 O O . HOH J . ? 0.1942 0.2796 0.2718 -0.0346 0.0136 -0.0005 1112 HOH A O 2883 O O . HOH J . ? 0.2014 0.1342 0.1553 0.0036 0.0328 0.0524 1113 HOH A O 2884 O O . HOH J . ? 0.4471 0.2473 0.4325 0.0692 0.1902 0.1467 1114 HOH A O 2885 O O . HOH J . ? 0.2057 0.2166 0.2859 -0.0683 -0.1103 0.0595 1115 HOH A O 2886 O O . HOH J . ? 0.2136 0.1726 0.1614 0.0082 -0.0197 0.0260 1116 HOH A O 2887 O O . HOH J . ? 0.1830 0.2165 0.1766 -0.0422 -0.0296 0.0026 1117 HOH A O 2888 O O . HOH J . ? 0.2683 0.1396 0.1955 0.0127 -0.0311 -0.0482 1118 HOH A O 2889 O O . HOH J . ? 0.2526 0.3449 0.2047 0.1062 -0.0836 -0.0471 1119 HOH A O 2890 O O . HOH J . ? 0.2561 0.1639 0.3733 -0.0399 -0.0268 -0.0672 1120 HOH A O 2891 O O . HOH J . ? 0.1813 0.1248 0.1786 0.0076 -0.0466 -0.0129 1121 HOH A O 2892 O O . HOH J . ? 0.2614 0.1942 0.1431 0.0429 0.0146 -0.0097 1122 HOH A O 2893 O O . HOH J . ? 0.2642 0.1675 0.1586 0.0810 -0.0032 -0.0187 1123 HOH A O 2894 O O . HOH J . ? 0.1433 0.2459 0.1484 0.0282 -0.0412 0.0179 1124 HOH A O 2895 O O . HOH J . ? 0.1444 0.1226 0.1193 -0.0176 0.0174 -0.0131 1125 HOH A O 2896 O O . HOH J . ? 0.4023 0.1680 0.3176 -0.0819 -0.1537 0.0949 1126 HOH A O 2897 O O . HOH J . ? 0.0826 0.0858 0.0808 0.0029 -0.0200 0.0098 1127 HOH A O 2898 O O . HOH J . ? 0.1998 0.3047 0.2062 -0.0783 0.0149 0.0773 1128 HOH A O 2899 O O . HOH J . ? 0.1289 0.1110 0.1316 0.0040 -0.0165 -0.0057 1129 HOH A O 2900 O O . HOH J . ? 0.3176 0.2343 0.4255 0.0864 0.1390 0.0640 1130 HOH A O 2901 O O . HOH J . ? 0.1498 0.1074 0.1286 0.0269 -0.0238 -0.0140 1131 HOH A O 2902 O O A HOH J . ? 0.1695 0.1387 0.1827 -0.0086 -0.0338 0.0121 1132 HOH A O 2903 O O . HOH J . ? 0.1668 0.1310 0.2387 -0.0138 -0.0508 0.0511 1133 HOH A O 2904 O O . HOH J . ? 0.3781 0.2820 0.2836 0.0566 -0.1165 0.1316 1134 HOH A O 2905 O O . HOH J . ? 0.0869 0.1641 0.1269 -0.0019 -0.0168 -0.0194 1135 HOH A O 2906 O O . HOH J . ? 0.1967 0.1716 0.1518 -0.0067 -0.0184 0.0341 1136 HOH A O 2907 O O . HOH J . ? 0.5803 0.2094 0.3184 0.1872 0.2906 0.1222 1137 HOH A O 2908 O O . HOH J . ? 0.2893 0.2015 0.3870 0.0056 0.0221 0.0069 1138 HOH A O 2909 O O . HOH J . ? 0.5709 0.3897 0.1679 -0.2331 0.1777 -0.0487 1139 HOH A O 2910 O O . HOH J . ? 0.5257 0.2690 0.3345 0.1152 -0.0801 0.0784 1140 HOH A O 2911 O O . HOH J . ? 0.2506 0.0940 0.1383 0.0120 -0.0439 0.0195 1141 HOH A O 2912 O O . HOH J . ? 0.3579 0.1918 0.3958 0.0289 0.1003 0.0811 1142 HOH A O 2913 O O . HOH J . ? 0.2897 0.2588 0.3901 0.0828 -0.1929 0.0081 1143 HOH A O 2914 O O . HOH J . ? 0.2190 0.2484 0.1635 -0.0670 -0.0231 -0.0712 1144 HOH A O 2915 O O . HOH J . ? 0.5738 0.3772 0.3364 0.1762 0.1447 0.0892 1145 HOH A O 2916 O O . HOH J . ? 0.2009 0.1818 0.1566 0.0078 -0.0009 -0.0201 1146 HOH A O 2917 O O . HOH J . ? 0.1873 0.4590 0.3044 -0.0973 -0.0850 0.1214 1147 HOH A O 2918 O O . HOH J . ? 0.9451 0.2265 0.3263 0.2300 0.2265 0.1272 1148 HOH A O 2919 O O . HOH J . ? 0.6850 0.1158 0.5869 -0.0204 -0.5087 0.0255 1149 HOH A O 2920 O O . HOH J . ? 0.2581 0.2810 0.2358 0.0401 -0.0818 0.0381 1150 HOH A O 2921 O O . HOH J . ? 0.2005 0.2198 0.2418 -0.0022 -0.0864 0.0120 1151 HOH A O 2922 O O . HOH J . ? 0.1970 0.2670 0.2042 0.0245 -0.0295 0.0126 1152 HOH A O 2923 O O . HOH J . ? 0.2540 0.2381 0.5804 -0.0089 -0.0302 0.2380 1153 HOH A O 2924 O O . HOH J . ? 0.3083 0.5835 0.1172 -0.1433 0.0487 0.0090 1154 HOH A O 2925 O O . HOH J . ? 0.2304 0.1904 0.3363 -0.0141 -0.0935 -0.0418 1155 HOH A O 2926 O O . HOH J . ? 0.4376 0.1596 0.3094 -0.0368 0.0482 0.0094 1156 HOH A O 2927 O O . HOH J . ? 0.2055 0.2896 0.1484 -0.0595 0.0207 -0.0315 1157 HOH A O 2928 O O . HOH J . ? 0.3069 0.1736 0.2303 -0.0139 -0.1601 0.0142 1158 HOH A O 2929 O O . HOH J . ? 0.3092 0.6147 0.2740 0.2682 -0.0991 -0.1593 1159 HOH A O 2930 O O . HOH J . ? 0.1429 0.0893 0.1229 -0.0003 -0.0071 -0.0108 1160 HOH A O 2931 O O . HOH J . ? 0.1910 0.2013 0.1074 -0.0180 -0.0070 -0.0066 1161 HOH A O 2932 O O . HOH J . ? 0.1368 0.2887 0.2188 0.0758 -0.0718 -0.1266 1162 HOH A O 2933 O O . HOH J . ? 0.1627 0.1025 0.1293 -0.0205 -0.0332 0.0055 1163 HOH A O 2934 O O . HOH J . ? 0.1571 0.4011 0.0936 -0.0957 0.0003 -0.0269 1164 HOH A O 2935 O O . HOH J . ? 0.1763 0.1491 0.1448 0.0416 -0.0416 -0.0034 1165 HOH A O 2936 O O . HOH J . ? 0.1219 0.1728 0.1793 0.0065 -0.0447 0.0192 1166 HOH A O 2937 O O . HOH J . ? 0.1627 0.1218 0.2399 -0.0011 -0.0533 0.0012 1167 HOH A O 2938 O O . HOH J . ? 0.2619 0.3561 0.1824 0.0289 -0.0402 -0.0509 1168 HOH A O 2939 O O . HOH J . ? 0.2605 0.3172 0.1131 0.0291 -0.0259 0.0269 1169 HOH A O 2940 O O . HOH J . ? 0.1302 0.2115 0.1701 0.0556 0.0139 0.0359 1170 HOH A O 2941 O O . HOH J . ? 0.1422 0.2950 0.2784 -0.0416 -0.0257 0.1033 1171 HOH A O 2942 O O . HOH J . ? 0.1774 0.1589 0.3163 -0.0063 -0.0493 0.0923 1172 HOH A O 2943 O O . HOH J . ? 0.4554 0.4716 0.3243 0.0200 -0.0174 -0.0001 1173 HOH A O 2944 O O . HOH J . ? 0.2978 0.2643 0.3663 -0.0428 -0.1078 0.1185 1174 HOH A O 2945 O O . HOH J . ? 0.1883 0.1190 0.1777 -0.0228 -0.0050 -0.0040 1175 HOH A O 2946 O O . HOH J . ? 0.2440 0.2703 0.4192 -0.0244 0.0275 -0.0445 1176 HOH A O 2947 O O . HOH J . ? 0.2661 0.2527 0.3286 -0.0708 -0.0414 0.0513 1177 HOH A O 2948 O O . HOH J . ? 0.4204 0.2797 0.2039 -0.0569 0.0583 0.0241 1178 HOH A O 2949 O O . HOH J . ? 0.2588 0.4954 0.2668 -0.0062 -0.0705 -0.1371 1179 HOH A O 2950 O O . HOH J . ? 0.1509 0.1986 0.3852 -0.0498 0.0061 0.0959 1180 HOH A O 2951 O O . HOH J . ? 0.4091 0.3152 0.2835 -0.0052 0.0568 -0.0309 1181 HOH A O 2952 O O . HOH J . ? 0.4315 0.4964 0.3258 0.2939 0.0177 0.0219 1182 HOH A O 2953 O O . HOH J . ? 0.1861 0.2169 0.2156 -0.0351 0.0408 -0.0910 1184 HOH A O 2954 O O . HOH J . ? 0.1750 0.4669 0.3116 -0.1158 0.0239 -0.1536 1185 HOH A O 2955 O O . HOH J . ? 0.1775 0.2623 0.1315 -0.0653 -0.0163 0.0370 1186 HOH A O 2956 O O . HOH J . ? 0.2878 0.2281 0.2511 -0.0338 0.0581 0.0676 1187 HOH A O 2957 O O . HOH J . ? 0.3188 0.4532 0.2071 -0.1382 -0.0220 0.0466 1188 HOH A O 2958 O O . HOH J . ? 0.4653 0.3296 0.2696 0.1939 0.0685 -0.0459 1189 HOH A O 2959 O O . HOH J . ? 0.2221 0.0992 0.0787 0.0100 -0.0347 0.0040 1190 HOH A O 2960 O O . HOH J . ? 0.1399 0.1144 0.1225 0.0036 -0.0132 -0.0120 1191 HOH A O 2961 O O . HOH J . ? 0.1634 0.2075 0.1488 -0.0199 -0.0549 -0.0024 1192 HOH A O 2962 O O . HOH J . ? 0.1841 0.2532 0.1527 -0.0364 -0.0026 0.0598 1193 HOH A O 2963 O O . HOH J . ? 0.2756 0.2019 0.2391 0.0069 0.0349 0.0074 1194 HOH A O 2964 O O . HOH J . ? 0.1082 0.1468 0.2941 -0.0205 -0.0898 0.0391 1195 HOH A O 2965 O O . HOH J . ? 0.1438 0.2143 0.1661 -0.0012 -0.0218 0.0239 1196 HOH A O 2966 O O . HOH J . ? 0.3039 0.2319 0.1934 -0.0781 -0.0182 -0.0048 1197 HOH A O 2967 O O . HOH J . ? 0.2061 0.5998 0.4170 0.0702 0.0535 -0.1196 1198 HOH A O 2968 O O . HOH J . ? 0.2315 0.2516 0.2429 -0.0863 -0.1002 0.1021 1199 HOH A O 2969 O O . HOH J . ? 0.3079 0.1958 0.2339 -0.0162 -0.0184 -0.0126 1200 HOH A O 2970 O O . HOH J . ? 0.2067 0.2075 0.1530 -0.0280 -0.0373 0.0305 1201 HOH A O 2971 O O . HOH J . ? 0.1869 0.2429 0.3471 -0.0460 -0.0560 0.0068 1202 HOH A O 2972 O O . HOH J . ? 0.2243 0.2811 0.2513 -0.0273 0.0126 -0.0228 1203 HOH A O 2973 O O . HOH J . ? 0.1624 0.2004 0.3034 0.0092 -0.0049 -0.0494 1204 HOH A O 2974 O O . HOH J . ? 0.3786 0.1432 0.2092 -0.0215 0.1245 -0.0079 1205 HOH A O 2975 O O . HOH J . ? 0.2416 0.2322 0.6679 -0.0635 -0.2280 0.1535 1206 HOH A O 2976 O O . HOH J . ? 0.5060 0.3456 0.1900 0.1667 0.1079 0.0790 1207 HOH A O 2977 O O . HOH J . ? 0.3859 0.2090 0.2254 -0.1178 -0.0786 0.0049 1208 HOH A O 2978 O O . HOH J . ? 0.2503 0.2839 0.1820 -0.0284 -0.0183 0.0299 1209 HOH A O 2979 O O . HOH J . ? 0.4030 0.2748 0.2092 -0.0896 0.0322 -0.0075 1210 HOH A O 2980 O O . HOH J . ? 0.2750 0.1542 0.2717 -0.0437 0.0733 0.0283 1211 HOH A O 2981 O O . HOH J . ? 0.2884 0.1592 0.1571 -0.0231 0.0357 0.0269 1212 HOH A O 2982 O O . HOH J . ? 0.4749 0.1861 0.3998 -0.0378 0.1770 -0.0667 1213 HOH A O 2983 O O . HOH J . ? 0.4791 0.2976 0.6245 -0.0927 -0.2242 -0.0440 1214 HOH A O 2984 O O . HOH J . ? 0.2661 0.5175 0.3474 -0.1591 -0.0740 0.1968 1215 HOH A O 2985 O O . HOH J . ? 0.1415 0.2330 0.2378 0.0020 -0.0099 -0.0196 1216 HOH A O 2986 O O . HOH J . ? 0.1487 0.2878 0.4243 0.0207 -0.0857 -0.0476 1217 HOH A O 2987 O O . HOH J . ? 0.2024 0.2687 0.2184 -0.0215 0.0287 0.0440 1218 HOH A O 2988 O O . HOH J . ? 0.2131 0.1601 0.4296 0.0486 -0.1348 -0.1299 1219 HOH A O 2989 O O . HOH J . ? 0.2547 0.2197 0.2649 -0.0219 -0.1033 0.0033 1220 HOH A O 2990 O O . HOH J . ? 0.2286 0.4003 0.1907 -0.0462 -0.0208 0.0875 1221 HOH A O 2991 O O . HOH J . ? 0.1291 0.5875 0.2025 0.0758 -0.0483 -0.1440 1222 HOH A O 2992 O O . HOH J . ? 0.3555 0.2470 0.2420 -0.0894 -0.1386 -0.0233 1223 HOH A O 2993 O O . HOH J . ? 0.2056 0.2266 0.2516 -0.0383 -0.0644 0.0098 1224 HOH A O 2994 O O . HOH J . ? 0.1765 0.2729 0.3056 -0.0167 0.0339 0.1161 1225 HOH A O 2995 O O . HOH J . ? 0.2960 0.2217 0.1943 0.0225 -0.0687 0.0063 1226 HOH A O 2996 O O . HOH J . ? 0.4176 0.2879 0.2975 -0.1875 -0.1132 0.0720 1227 HOH A O 2997 O O . HOH J . ? 0.4668 0.2293 0.3035 0.0487 -0.0322 -0.0323 1228 HOH A O 2998 O O . HOH J . ? 0.4718 0.3815 0.2718 0.1879 -0.0304 0.0978 1229 HOH A O 2999 O O . HOH J . ? 0.2309 0.2364 0.1613 0.0628 -0.0315 0.0021 1230 HOH A O 3000 O O . HOH J . ? 0.2209 0.2089 0.3015 0.0361 0.0214 -0.0734 1231 HOH A O 3001 O O . HOH J . ? 0.4309 0.4564 0.2616 -0.2077 -0.0350 0.0269 1232 HOH A O 3002 O O . HOH J . ? 0.2310 0.2506 0.2199 0.0490 0.0118 0.0076 1234 HOH A O 3003 O O . HOH J . ? 0.3339 0.2283 0.6740 -0.1052 -0.1328 0.1875 1235 HOH A O 3004 O O . HOH J . ? 0.3702 0.4471 0.2785 0.0912 0.0087 -0.0418 1236 HOH A O 3005 O O . HOH J . ? 0.4287 0.2227 0.4105 -0.0445 0.1887 -0.0072 1237 HOH A O 3006 O O . HOH J . ? 0.4722 0.5189 0.5378 -0.0621 0.1903 -0.2486 1238 HOH A O 3007 O O . HOH J . ? 0.2523 0.2582 0.2056 -0.0145 -0.0522 -0.0438 1239 HOH A O 3008 O O . HOH J . ? 0.2891 0.2097 0.2003 -0.0216 -0.0214 -0.0038 1240 HOH A O 3009 O O . HOH J . ? 0.4997 0.2730 0.2296 -0.0610 -0.0107 0.0326 1241 HOH A O 3010 O O . HOH J . ? 0.3133 0.2756 0.1879 -0.0883 -0.0723 0.0274 1242 HOH A O 3011 O O . HOH J . ? 0.5379 0.2795 0.3876 0.1084 0.0555 0.1244 1243 HOH A O 3012 O O . HOH J . ? 0.2589 0.2396 0.3818 0.0600 -0.1536 -0.0629 1245 HOH A O 3013 O O . HOH J . ? 0.2412 0.5393 0.3149 0.1049 -0.0254 -0.0171 1246 HOH A O 3014 O O . HOH J . ? 0.3948 0.3810 0.2659 0.1792 0.0506 0.0199 1247 HOH A O 3015 O O . HOH J . ? 0.3937 0.3201 0.2830 -0.0320 -0.0107 0.0035 1248 HOH A O 3016 O O . HOH J . ? 0.1322 0.4013 0.3026 -0.0338 -0.0079 -0.0092 1249 HOH A O 3017 O O . HOH J . ? 0.3630 0.2483 0.2413 -0.0819 -0.0390 -0.0378 1250 HOH A O 3018 O O . HOH J . ? 0.4544 0.2523 0.8188 -0.0321 -0.3944 0.1689 1251 HOH A O 3019 O O . HOH J . ? 0.3056 0.3505 0.3688 0.0736 0.0394 -0.0675 1252 HOH A O 3020 O O . HOH J . ? 0.3429 0.4755 0.3923 0.0897 -0.1189 -0.0104 1253 HOH A O 3021 O O . HOH J . ? 0.3535 0.2881 0.6183 0.0987 0.0395 0.1513 1254 HOH A O 3022 O O . HOH J . ? 0.2229 0.3702 0.3800 -0.0493 0.0278 -0.1322 1255 HOH A O 3023 O O . HOH J . ? 0.3017 0.3505 0.3067 0.1423 0.0357 0.0774 1256 HOH A O 3024 O O . HOH J . ? 0.2730 0.3077 0.2915 0.0240 -0.0250 0.0491 1257 HOH A O 3025 O O . HOH J . ? 0.3614 0.3924 0.1939 0.2090 -0.1261 -0.0724 1258 HOH A O 3026 O O . HOH J . ? 0.2138 0.7734 0.3084 -0.0625 0.0029 0.1518 1260 HOH A O 3027 O O . HOH J . ? 0.5284 0.2277 0.4061 0.0753 0.1235 0.0341 1261 HOH A O 3028 O O . HOH J . ? 0.2703 0.1933 0.2928 -0.0293 -0.0234 -0.0552 1262 HOH A O 3029 O O . HOH J . ? 0.2882 0.5524 0.1904 -0.1574 -0.0817 0.1057 1263 HOH A O 3030 O O . HOH J . ? 0.4206 0.3207 0.2193 -0.0954 0.0589 -0.0814 1264 HOH A O 3031 O O . HOH J . ? 0.6632 0.2502 0.4943 0.0012 -0.3636 0.0127 1266 HOH A O 3032 O O . HOH J . ? 0.5783 0.2334 0.1883 0.0230 -0.0169 -0.0550 1268 HOH A O 3033 O O . HOH J . ? 0.2070 0.5393 0.5214 -0.1040 -0.0011 -0.2238 1269 HOH A O 3034 O O . HOH J . ? 0.6960 0.5236 0.3922 0.0109 0.0931 0.2977 1270 HOH A O 3035 O O . HOH J . ? 0.3259 0.3421 0.2192 -0.0051 0.0045 -0.0456 1271 HOH A O 3036 O O . HOH J . ? 0.3799 0.2900 0.2670 -0.0161 0.0262 -0.1329 1272 HOH A O 3037 O O . HOH J . ? 0.3883 0.4080 0.3493 0.1468 -0.0508 0.0896 1273 HOH A O 3038 O O . HOH J . ? 0.3294 0.7448 0.3056 -0.1916 -0.1299 0.2553 1274 HOH A O 3039 O O . HOH J . ? 0.2871 0.2486 0.2902 0.0037 -0.0367 -0.1128 1275 HOH A O 3040 O O . HOH J . ? 0.2270 0.2064 0.7241 -0.0364 0.0066 -0.0250 1277 HOH A O 3041 O O . HOH J . ? 0.2677 0.5832 0.4639 -0.2405 -0.1945 0.2977 1278 HOH A O 3042 O O . HOH J . ? 0.2905 0.5350 0.2741 0.0583 0.1199 -0.0521 1279 HOH A O 3043 O O . HOH J . ? 0.2558 0.3320 0.5571 -0.0376 0.1570 -0.0866 1280 HOH A O 3044 O O . HOH J . ? 0.4172 0.5044 0.2852 0.0929 -0.0319 -0.0761 1281 HOH A O 3045 O O . HOH J . ? 0.5811 0.4549 0.1993 0.3141 0.0830 0.1145 1282 HOH A O 3046 O O . HOH J . ? 0.5148 0.4063 0.4262 -0.1203 -0.1903 0.0871 1283 HOH A O 3047 O O . HOH J . ? 0.2346 0.4939 0.5303 -0.1446 0.0008 0.1041 1284 HOH A O 3048 O O . HOH J . ? 0.5098 0.3763 0.2317 -0.0294 -0.0383 0.0943 1285 HOH A O 3049 O O . HOH J . ? 0.3451 0.4163 0.6272 -0.1548 0.1945 -0.1794 1286 HOH A O 3050 O O . HOH J . ? 0.4957 0.4268 0.2584 -0.0900 -0.0735 0.0917 1287 HOH A O 3051 O O . HOH J . ? 0.6342 0.2715 0.4179 0.1622 0.0767 0.1740 1288 HOH A O 3052 O O . HOH J . ? 0.3101 0.6031 0.2707 0.1159 -0.0346 -0.0959 1289 HOH A O 3053 O O . HOH J . ? 0.2388 0.1980 0.2826 0.0376 -0.0758 0.0009 1290 HOH A O 3054 O O . HOH J . ? 0.3895 0.4240 0.2660 -0.0474 -0.0982 0.0588 1291 HOH A O 3055 O O . HOH J . ? 0.6916 0.2760 0.3467 -0.1681 -0.2871 0.1089 1292 HOH A O 3056 O O . HOH J . ? 0.3279 0.2678 0.3505 -0.0105 -0.0602 -0.0437 1293 HOH A O 3057 O O . HOH J . ? 0.4477 0.3206 0.3297 0.0658 -0.1060 0.0225 1294 HOH A O 3058 O O . HOH J . ? 0.4247 0.3484 0.1983 0.0135 -0.0332 0.0103 1295 HOH A O 3059 O O . HOH J . ? 0.2462 0.6292 0.2054 0.0158 0.0277 0.0906 1296 HOH A O 3060 O O . HOH J . ? 0.4179 0.5776 0.2622 0.0013 0.0527 0.1904 1297 HOH A O 3061 O O . HOH J . ? 0.3534 0.4044 0.5159 -0.0517 -0.0998 0.2005 1298 HOH A O 3062 O O . HOH J . ? 0.3084 0.6211 0.4466 0.1912 0.0618 0.1034 1299 HOH A O 3063 O O . HOH J . ? 0.3045 0.4381 0.4030 -0.0557 0.0227 0.1270 1300 HOH A O 3064 O O . HOH J . ? 0.3427 0.5314 0.5325 -0.2042 -0.1428 0.0961 1301 HOH A O 3065 O O . HOH J . ? 0.3509 0.2528 0.6087 0.1695 -0.2004 -0.1187 1302 HOH A O 3066 O O . HOH J . ? 0.3801 0.3937 0.1994 -0.0639 -0.0587 -0.0880 1303 HOH A O 3067 O O . HOH J . ? 0.7249 0.4073 0.2656 0.2214 -0.0823 -0.1558 1304 HOH A O 3068 O O . HOH J . ? 0.4086 0.4985 0.1887 -0.0817 0.0275 0.0429 1305 HOH A O 3069 O O . HOH J . ? 0.6426 0.3970 0.3674 0.3091 0.2091 0.0971 1306 HOH A O 3070 O O . HOH J . ? 0.2821 0.3214 0.6385 -0.0924 -0.2645 0.2504 1307 HOH A O 3071 O O . HOH J . ? 0.3473 0.4563 0.5294 0.0219 0.1674 0.0872 1308 HOH A O 3072 O O . HOH J . ? 0.2850 0.3716 0.3341 0.0020 -0.0103 -0.0736 1309 HOH A O 3073 O O . HOH J . ? 0.5130 0.3610 0.4784 -0.2130 0.0369 0.1015 1310 HOH A O 3074 O O . HOH J . ? 0.2855 0.3448 0.3514 0.0887 -0.0673 -0.0091 1311 HOH A O 3075 O O . HOH J . ? 0.3920 0.3694 0.5678 0.0788 -0.2174 -0.0305 1312 HOH A O 3076 O O . HOH J . ? 0.5050 0.1236 0.3918 -0.0651 0.1414 -0.0203 1313 HOH A O 3077 O O . HOH J . ? 0.6310 0.4189 0.4042 -0.1822 -0.0618 0.0279 1314 HOH A O 3078 O O . HOH J . ? 0.3342 0.4510 0.4161 -0.0239 -0.0501 -0.0581 1315 HOH A O 3079 O O . HOH J . ? 0.5264 0.3250 0.2468 -0.0220 0.0818 0.0574 1316 HOH A O 3080 O O . HOH J . ? 0.3950 0.5192 0.4047 -0.0343 -0.0417 -0.2031 1317 HOH A O 3081 O O . HOH J . ? 0.2817 0.2546 0.3207 0.0512 0.0538 0.0263 1319 HOH A O 3082 O O . HOH J . ? 0.4933 0.2661 0.2518 -0.0771 0.0189 -0.0280 1320 HOH A O 3083 O O . HOH J . ? 0.5679 0.6209 0.2051 0.2479 0.0782 0.1322 1321 HOH A O 3084 O O . HOH J . ? 0.6804 0.4433 0.3793 -0.3563 -0.0610 -0.0688 1322 HOH A O 3085 O O . HOH J . ? 0.2876 0.4386 0.5746 -0.0093 -0.0126 0.3133 1324 HOH A O 3086 O O . HOH J . ? 0.3860 0.4605 0.4209 0.0820 -0.0353 -0.2129 1328 HOH A O 3087 O O . HOH J . ? 0.2978 0.4870 0.8148 -0.0617 0.2735 -0.1499 1329 HOH A O 3088 O O . HOH J . ? 0.3994 0.3160 0.3880 -0.0929 0.0297 -0.0623 1330 HOH A O 3089 O O . HOH J . ? 0.4124 0.6126 0.4495 -0.1308 -0.1293 0.0917 1331 HOH A O 3090 O O . HOH J . ? 0.2335 0.2426 0.4490 -0.0075 0.0152 -0.0751 1333 HOH A O 3091 O O . HOH J . ? 0.2584 0.4655 0.7223 -0.0058 -0.2126 0.1256 1334 HOH A O 3092 O O . HOH J . ? 0.5222 0.5891 0.5454 -0.3622 -0.1779 0.1618 1335 HOH A O 3093 O O . HOH J . ? 0.2558 0.3426 0.1969 0.0981 0.0317 -0.0050 1336 HOH A O 3094 O O . HOH J . ? 0.1677 0.3589 0.4235 -0.0379 0.0760 -0.0753 1337 HOH A O 3095 O O . HOH J . ? 0.3139 0.3963 0.2197 -0.0951 -0.0287 -0.0244 1338 HOH A O 3096 O O . HOH J . ? 0.6679 0.2656 0.3566 0.0978 -0.1472 -0.0149 1340 HOH A O 3097 O O . HOH J . ? 0.1743 0.4286 0.7881 -0.0236 0.0167 -0.0064 1341 HOH A O 3098 O O . HOH J . ? 0.1860 0.9891 0.3165 -0.0745 0.0663 -0.3078 1342 HOH A O 3099 O O . HOH J . ? 0.4133 0.4131 0.5734 0.2012 -0.2235 -0.0688 1343 HOH A O 3100 O O . HOH J . ? 0.3263 0.2109 0.2709 -0.0746 0.0030 -0.0242 1345 HOH A O 3101 O O . HOH J . ? 0.4365 0.2406 0.5092 -0.0009 0.1340 -0.1296 1346 HOH A O 3102 O O . HOH J . ? 0.3224 0.2408 1.0630 0.0245 -0.0455 -0.0272 1347 HOH A O 3103 O O . HOH J . ? 0.2919 0.3698 0.3760 0.1371 0.0668 -0.0558 1348 HOH A O 3104 O O . HOH J . ? 0.4158 0.3717 0.6885 -0.1590 -0.1533 -0.2151 1349 HOH A O 3105 O O . HOH J . ? 0.2276 0.4867 0.2591 0.0138 0.0463 0.0051 1350 HOH A O 3106 O O . HOH J . ? 0.2025 0.2252 0.4382 0.0345 0.0436 0.0932 1351 HOH A O 3107 O O . HOH J . ? 0.5689 0.6391 0.2906 0.1057 -0.2039 -0.1346 1354 HOH A O 3108 O O . HOH J . ? 0.3762 0.5617 0.2327 -0.0533 -0.0120 0.0831 1355 HOH A O 3109 O O . HOH J . ? 0.6653 0.5221 0.2927 0.0806 0.1903 -0.0896 1356 HOH A O 3110 O O . HOH J . ? 0.3395 0.5750 0.5902 0.0974 -0.1670 0.0719 1358 HOH A O 3111 O O . HOH J . ? 0.1612 0.2058 0.3679 -0.0105 -0.0115 0.0106 1359 HOH A O 3112 O O . HOH J . ? 0.2964 0.2859 0.1956 0.0419 -0.0100 0.0073 1360 HOH A O 3113 O O . HOH J . ? 0.3365 0.4983 0.4980 -0.0378 -0.0876 -0.1072 1362 HOH A O 3114 O O . HOH J . ? 0.2687 0.1862 0.7322 0.0570 0.0136 -0.0142 1364 HOH A O 3115 O O . HOH J . ? 0.4274 0.2631 0.2352 0.0387 -0.0587 -0.0551 1365 HOH A O 3116 O O . HOH J . ? 0.8145 0.2582 0.2948 0.2503 -0.3134 -0.1010 1366 HOH A O 3117 O O . HOH J . ? 0.4832 0.3096 0.6309 0.0799 -0.3152 -0.1447 1367 HOH A O 3118 O O . HOH J . ? 0.2877 0.5088 0.4123 -0.0129 -0.0128 0.1345 1369 HOH A O 3119 O O . HOH J . ? 0.5620 0.3309 0.5173 0.1217 0.0072 -0.1063 1370 HOH A O 3120 O O . HOH J . ? 0.3275 0.2549 0.5518 0.0616 -0.0366 0.0232 1371 HOH A O 3121 O O . HOH J . ? 0.4029 0.6960 0.7275 -0.2897 0.1134 0.1178 1372 HOH A O 3122 O O . HOH J . ? 0.2614 0.3383 0.2943 0.0692 -0.1169 0.0527 1373 HOH A O 3123 O O . HOH J . ? 0.5812 0.3354 0.1936 0.0246 -0.0132 0.0892 1374 HOH A O 3124 O O . HOH J . ? 0.4452 0.5220 0.6365 -0.2762 0.2079 -0.1267 1376 HOH A O 3125 O O . HOH J . ? 0.5170 0.4564 0.4274 -0.2284 -0.1706 -0.0926 1377 HOH A O 3126 O O . HOH J . ? 0.6702 0.2382 0.6146 -0.0023 -0.0048 0.1205 1380 HOH A O 3127 O O . HOH J . ? 0.2555 0.4709 0.5456 0.0214 0.0591 -0.0817 1381 HOH A O 3128 O O . HOH J . ? 0.4259 0.3203 0.4107 0.0241 0.0244 0.0131 1383 HOH A O 3129 O O . HOH J . ? 0.4493 0.3056 0.6568 -0.0574 0.0398 0.1576 1385 HOH A O 3130 O O . HOH J . ? 0.6665 0.4285 0.4744 -0.2530 -0.1003 0.1459 1386 HOH A O 3131 O O . HOH J . ? 0.4997 0.3321 0.4559 0.0444 0.1810 0.0262 1387 HOH A O 3132 O O . HOH J . ? 0.4752 0.3445 0.4987 0.1423 0.0283 0.0052 1388 HOH A O 3133 O O . HOH J . ? 0.3438 0.5479 0.2261 -0.2367 -0.0519 0.1461 1389 HOH A O 3134 O O . HOH J . ? 0.4077 0.7212 0.2334 -0.0437 0.0066 0.0695 1390 HOH A O 3135 O O . HOH J . ? 0.4140 0.4351 0.3478 -0.0358 -0.2352 0.0413 1391 HOH A O 3136 O O . HOH J . ? 0.8165 0.3710 0.4375 -0.3345 0.0139 -0.0523 1392 HOH A O 3137 O O . HOH J . ? 0.6375 0.5437 0.4538 -0.0403 -0.0948 0.1897 1393 HOH A O 3138 O O . HOH J . ? 0.2175 0.3305 0.8432 -0.0789 0.0906 -0.2878 1394 HOH A O 3139 O O . HOH J . ? 0.3252 0.2850 0.7218 -0.0878 -0.3514 0.2396 1395 HOH A O 3140 O O . HOH J . ? 1.1469 0.3678 0.2283 0.2900 0.0242 -0.0585 1397 HOH A O 3141 O O . HOH J . ? 0.2491 0.2945 0.3504 -0.0069 -0.0724 0.0103 1398 HOH A O 3142 O O . HOH J . ? 0.5060 0.6041 0.3943 -0.1713 0.0991 -0.0130 1399 HOH A O 3143 O O . HOH J . ? 0.3441 0.7123 0.3088 0.2735 0.0548 0.1754 1400 HOH A O 3144 O O . HOH J . ? 0.5101 0.4714 0.4391 -0.2929 -0.0698 0.1413 1401 HOH A O 3145 O O . HOH J . ? 0.6373 0.6648 0.7075 -0.0853 0.0005 0.4150 1402 HOH A O 3146 O O . HOH J . ? 0.2694 0.3249 0.4973 0.0943 -0.0532 0.0627 1403 HOH A O 3147 O O . HOH J . ? 0.4815 0.5425 0.4972 0.0698 0.2034 0.1799 1404 HOH A O 3148 O O . HOH J . ? 0.5197 0.3658 0.3214 0.1550 -0.0143 -0.0561 1405 HOH A O 3149 O O . HOH J . ? 0.3079 0.3925 0.5434 -0.0938 -0.0296 -0.0904 1409 HOH A O 3150 O O . HOH J . ? 0.3624 0.5887 0.2884 0.0099 -0.0494 0.0249 1410 HOH A O 3151 O O . HOH J . ? 0.5075 0.5039 0.3694 -0.1529 0.0226 -0.0076 1411 HOH A O 3152 O O . HOH J . ? 0.6149 0.3216 0.5369 -0.1808 0.1400 -0.0783 1414 HOH A O 3153 O O . HOH J . ? 0.7819 0.3565 0.3523 -0.1060 0.0907 0.0954 1415 HOH A O 3154 O O A HOH J . ? 0.1769 0.1534 0.3090 -0.0079 -0.2411 -0.0019 1417 HOH A O 3155 O O B HOH J . ? 0.3868 0.5158 0.1224 -0.0658 -0.0518 -0.0176 1417 HOH A O 3156 O O . HOH J . ? 0.5246 0.3662 0.2852 0.0250 -0.0754 -0.0303 1418 HOH A O 3157 O O . HOH J . ? 0.5769 0.2421 0.3113 -0.0900 0.0395 -0.1135 1419 HOH A O 3158 O O . HOH J . ? 0.4246 0.5316 0.3917 0.1263 -0.0811 -0.0851 1420 HOH A O 3159 O O . HOH J . ? 0.3643 0.4033 0.3807 0.0436 -0.0009 0.1931 1423 HOH A O 3160 O O . HOH J . ? 0.8155 0.3738 0.3901 -0.1204 -0.1704 -0.0068 1424 HOH A O 3161 O O . HOH J . ? 0.4475 0.2914 0.5645 0.0932 0.0479 0.1676 1427 HOH A O 3162 O O . HOH J . ? 0.2737 0.6346 0.3901 0.1379 0.0621 -0.1286 1428 HOH A O 3163 O O . HOH J . ? 0.4518 0.2455 0.8103 -0.0449 -0.3425 -0.0882 1430 HOH A O 3164 O O . HOH J . ? 0.4646 0.6459 0.4194 -0.2023 -0.2540 0.1631 1432 HOH A O 3165 O O . HOH J . ? 0.3304 0.5241 0.5881 -0.0430 0.0302 0.0942 1437 HOH A O 3166 O O . HOH J . ? 0.3790 0.2685 0.8685 -0.0125 -0.3088 0.1703 1438 HOH A O 3167 O O . HOH J . ? 0.5017 0.4360 0.2671 0.0847 -0.1101 -0.0362 1440 HOH A O 3168 O O . HOH J . ? 0.4119 0.4647 0.4144 -0.1019 0.0124 0.0208 1442 HOH A O 3169 O O . HOH J . ? 0.5476 0.2765 0.3043 -0.0050 0.0061 -0.0384 1444 HOH A O 3170 O O . HOH J . ? 0.4154 0.3327 0.4752 -0.0799 0.1604 -0.0237 1447 HOH A O 3171 O O . HOH J . ? 0.1211 0.1301 0.1411 0.0038 -0.0320 0.0003 1448 HOH A O 3172 O O . HOH J . ? 0.4306 0.4082 0.5965 -0.2186 -0.3571 0.2649 1449 HOH A O 3173 O O . HOH J . ? 0.2344 0.4382 0.2850 0.1838 -0.1347 -0.0762 1450 HOH A O 3174 O O . HOH J . ? 0.3186 0.7438 0.3591 -0.2333 -0.1480 0.2814 1451 HOH A O 3175 O O . HOH J . ? 0.7195 0.4310 0.2509 0.0978 0.0550 -0.0795 1452 HOH A O 3176 O O . HOH J . ? 0.2127 0.1091 0.3048 0.0189 0.0860 -0.0213 1454 HOH A O 3177 O O . HOH J . ? 0.3234 0.2167 0.4042 -0.0853 0.0589 -0.0730 1455 HOH A O 3178 O O . HOH J . ? 0.2979 0.4771 0.7293 0.2043 -0.3035 -0.4475 1456 HOH A O 3179 O O . HOH J . ? 0.6457 0.1843 0.3302 0.0717 -0.2535 0.0201 1457 HOH A O 3180 O O . HOH J . ? 0.4446 0.6107 0.2151 0.0638 -0.1947 -0.0283 1460 HOH A O 3181 O O . HOH J . ? 0.3689 0.2501 0.6021 -0.0453 0.1325 -0.0456 1461 HOH A O 3182 O O . HOH J . ? 0.4836 0.2727 0.3240 0.1193 0.0791 0.1108 1462 HOH A O 3183 O O . HOH J . ? 0.6244 0.1982 0.4867 -0.0722 0.3131 -0.0273 1463 HOH A O 3184 O O . HOH J . ? 0.2357 0.6031 0.6105 0.0863 -0.1629 0.0082 1470 HOH A O 3185 O O . HOH J . ? 0.3862 0.3043 0.4853 0.1037 0.0456 0.0024 1473 HOH A O 3186 O O . HOH J . ? 0.1229 0.4998 0.1788 0.0192 -0.0486 -0.0759 1475 HOH A O 3187 O O . HOH J . ? 0.1612 0.4229 0.2472 0.0302 0.0208 0.0893 1476 HOH A O 3188 O O . HOH J . ? 0.3534 0.2401 0.5165 0.0916 -0.3308 -0.1343 1477 HOH A O 3189 O O . HOH J . ? 0.6592 0.3144 0.1715 -0.2123 0.0785 -0.0600 1478 HOH A O 3190 O O . HOH J . ? 0.2232 0.3484 0.4517 -0.0319 0.0820 -0.0334 1479 HOH A O 3191 O O . HOH J . ? 0.3292 0.6641 0.6418 0.2453 0.1721 0.4741 1481 HOH A O 3192 O O . HOH J . ? 0.3965 0.2132 0.7553 -0.0230 0.2708 -0.1340 1482 HOH A O 3193 O O . HOH J . ? 0.7301 0.3856 0.4776 -0.2305 -0.2819 0.0520 1484 HOH A O 3194 O O . HOH J . ? 0.4051 0.2717 0.4731 0.0216 -0.1131 -0.0473 1485 HOH A O 3195 O O . HOH J . ? 0.6765 0.2143 0.4589 -0.0409 -0.3603 0.0504 1487 HOH A O 3196 O O . HOH J . ? 0.4244 0.2902 0.4418 0.1566 -0.1026 -0.1538 1488 HOH A O 3197 O O . HOH J . ? 0.4207 0.5276 0.3494 0.2523 -0.1309 -0.0616 1489 HOH A O 3198 O O . HOH J . ? 0.6641 0.2296 0.5164 -0.1719 -0.3658 0.0955 1492 HOH A O 3199 O O . HOH J . ? 0.5662 0.3648 0.2536 -0.0995 0.0418 0.0102 1494 HOH A O 3200 O O . HOH J . ? 0.5757 0.4261 0.3490 -0.2159 -0.0065 0.1609 1495 HOH A O 3201 O O . HOH J . ? 0.2150 0.3345 0.2437 0.0203 0.0352 -0.0132 1496 HOH A O 3202 O O . HOH J . ? 0.4535 0.3474 0.1902 0.0531 -0.0274 0.0434 1497 HOH A O 3203 O O . HOH J . ? 0.1497 0.5278 0.3464 0.0253 0.0210 0.2116 1498 HOH A O 3204 O O . HOH J . ? 0.5341 0.2522 0.6109 0.1003 0.0715 -0.0655 1499 HOH A O 3205 O O . HOH J . ? 0.3280 0.9312 0.3063 0.1591 -0.0584 0.2594 1502 HOH A O 3206 O O . HOH J . ? 0.3594 0.6261 0.5494 -0.0894 -0.2918 0.1926 1503 HOH A O 3207 O O . HOH J . ? 0.5348 0.7227 0.3609 -0.0828 0.1002 0.0915 1504 HOH A O 3208 O O . HOH J . ? 0.7083 0.2245 0.5679 0.2381 0.0693 0.1255 1505 HOH A O 3209 O O . HOH J . ? 0.3584 0.6696 0.3364 -0.2007 0.0247 -0.0637 1507 HOH A O 3210 O O . HOH J . ? 0.3999 0.6431 0.2841 -0.0674 0.1385 0.1346 1508 HOH A O 3211 O O . HOH J . ? 0.4014 0.6324 0.5206 -0.0787 0.2384 -0.0699 1509 HOH A O 3212 O O . HOH J . ? 0.7428 0.2818 0.7349 -0.1916 -0.4029 0.1909 1510 HOH A O 3213 O O . HOH J . ? 0.4266 0.2012 0.5819 0.0996 0.0403 0.0785 1511 HOH A O 3214 O O . HOH J . ? 0.4970 0.4873 0.4202 0.0799 -0.1349 -0.0452 1512 HOH A O 3215 O O . HOH J . ? 0.5440 0.6393 0.6107 -0.2278 -0.1362 -0.2426 1513 HOH A O 3216 O O . HOH J . ? 0.5364 0.5718 0.2760 -0.3147 0.0900 -0.1590 1514 HOH A O 3217 O O . HOH J . ? 0.4436 0.9062 0.2752 -0.1397 -0.1364 -0.1276 1517 HOH A O 3218 O O . HOH J . ? 0.3196 0.6911 1.0139 -0.1875 0.3352 -0.3122 1518 HOH A O 3219 O O . HOH J . ? 0.6895 0.5303 0.5194 0.2157 0.3521 0.0919 1520 HOH A O 3220 O O . HOH J . ? 0.3432 0.3525 0.2996 0.0213 -0.0334 -0.1073 1521 HOH A O 3221 O O . HOH J . ? 0.7137 0.3490 0.3139 0.1838 -0.1936 -0.0704 1523 HOH A O 3222 O O . HOH J . ? 0.8390 0.3069 0.4524 0.1197 0.1832 0.0857 1524 HOH A O 3223 O O . HOH J . ? 0.5083 0.3816 0.6490 0.2112 -0.1803 -0.1505 1526 HOH A O 3224 O O . HOH J . ? 0.7750 0.6244 0.3340 -0.2397 -0.2276 0.0059 1528 HOH A O 3225 O O . HOH J . ? 0.1484 1.1522 0.2475 0.0329 -0.0323 -0.2038 1529 HOH A O 3226 O O . HOH J . ? 0.5179 0.5597 0.4134 0.0899 -0.0181 0.0674 1531 HOH A O 3227 O O . HOH J . ? 0.6474 0.3952 0.6140 -0.2491 -0.3550 -0.0637 1532 HOH A O 3228 O O . HOH J . ? 0.3385 0.4044 0.5427 0.0412 -0.0375 -0.0509 1533 HOH A O 3229 O O . HOH J . ? 0.4361 0.4912 0.5576 -0.0133 -0.1889 0.1357 1534 HOH A O 3230 O O . HOH J . ? 0.4104 0.6817 0.4080 -0.3016 -0.0220 0.0715 1537 HOH A O 3231 O O . HOH J . ? 0.5716 0.3688 0.4098 0.2132 0.0400 0.0798 1541 HOH A O 3232 O O . HOH J . ? 0.6012 0.4995 0.2797 0.0924 -0.0505 -0.1396 1543 HOH A O 3233 O O . HOH J . ? 0.6449 0.5622 0.2324 -0.2498 -0.0838 -0.0636 1547 HOH A O 3234 O O . HOH J . ? 0.9914 0.5046 0.2478 0.2318 -0.1653 -0.0517 1550 HOH A O 3235 O O . HOH J . ? 0.9655 1.0634 1.0455 0.0847 0.0332 -0.2429 1551 HOH A O 3236 O O . HOH J . ? 0.7624 0.3233 0.4506 0.2337 0.0252 0.0021 1554 HOH A O 3237 O O . HOH J . ? 0.3202 0.4763 0.8733 -0.1661 -0.0038 -0.2033 1555 HOH A O 3238 O O . HOH J . ? 0.7731 0.4440 0.8547 0.3989 0.0297 0.0381 1556 HOH A O 3239 O O . HOH J . ? 0.5303 0.7562 0.3744 -0.1600 -0.1369 0.0064 1557 HOH A O 3240 O O . HOH J . ? 0.4908 0.4351 0.8570 -0.0320 0.3205 0.1428 1558 HOH A O 3241 O O . HOH J . ? 0.5364 0.7601 0.3581 0.0662 -0.1686 0.1920 1564 HOH A O 3242 O O . HOH J . ? 0.7680 0.1716 0.1777 -0.1255 -0.0636 0.0132 1565 HOH A O 3243 O O . HOH J . ? 0.6407 0.1890 0.5420 -0.1301 -0.0835 -0.0707 1566 HOH A O 3244 O O . HOH J . ? 0.3211 0.6447 0.5761 -0.2388 0.1006 -0.0295 1567 HOH A O 3245 O O . HOH J . ? 0.7484 0.2552 0.4266 0.1517 -0.1670 0.0203 1568 HOH A O 3246 O O . HOH J . ? 0.3665 0.7839 0.3897 0.2760 0.1319 0.3053 1570 HOH A O 3247 O O . HOH J . ? 0.4701 0.4843 0.9316 -0.0422 -0.2031 0.3560 1571 HOH A O # 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 ALA 1 1 1 ALA ALA A . n A 1 2 VAL 2 2 2 VAL VAL A . n A 1 3 CYS 3 3 3 CYS CYS A . n A 1 4 PRO 4 4 4 PRO PRO A . n A 1 5 ASP 5 5 5 ASP ASP A . n A 1 6 GLY 6 6 6 GLY GLY A . n A 1 7 THR 7 7 7 THR THR A . n A 1 8 ARG 8 8 8 ARG ARG A . n A 1 9 VAL 9 9 9 VAL VAL A . n A 1 10 SER 10 10 10 SER SER A . n A 1 11 HIS 11 11 11 HIS HIS A . n A 1 12 ALA 12 12 12 ALA ALA A . n A 1 13 ALA 13 13 13 ALA ALA A . n A 1 14 CYS 14 14 14 CYS CYS A . n A 1 15 CYS 15 15 15 CYS CYS A . n A 1 16 ALA 16 16 16 ALA ALA A . n A 1 17 PHE 17 17 17 PHE PHE A . n A 1 18 ILE 18 18 18 ILE ILE A . n A 1 19 PRO 19 19 19 PRO PRO A . n A 1 20 LEU 20 20 20 LEU LEU A . n A 1 21 ALA 21 21 21 ALA ALA A . n A 1 22 GLN 22 22 22 GLN GLN A . n A 1 23 ASP 23 23 23 ASP ASP A . n A 1 24 LEU 24 24 24 LEU LEU A . n A 1 25 GLN 25 25 25 GLN GLN A . n A 1 26 GLU 26 26 26 GLU GLU A . n A 1 27 THR 27 27 27 THR THR A . n A 1 28 ILE 28 28 28 ILE ILE A . n A 1 29 PHE 29 29 29 PHE PHE A . n A 1 30 GLN 30 30 30 GLN GLN A . n A 1 31 ASN 31 31 31 ASN ASN A . n A 1 32 GLU 32 32 32 GLU GLU A . n A 1 33 CYS 33 33 33 CYS CYS A . n A 1 34 GLY 34 34 34 GLY GLY A . n A 1 35 GLU 35 35 35 GLU GLU A . n A 1 36 ASP 36 36 36 ASP ASP A . n A 1 37 ALA 37 37 37 ALA ALA A . n A 1 38 HIS 38 38 38 HIS HIS A . n A 1 39 GLU 39 39 39 GLU GLU A . n A 1 40 VAL 40 40 40 VAL VAL A . n A 1 41 ILE 41 41 41 ILE ILE A . n A 1 42 ARG 42 42 42 ARG ARG A . n A 1 43 LEU 43 43 43 LEU LEU A . n A 1 44 THR 44 44 44 THR THR A . n A 1 45 PHE 45 45 45 PHE PHE A . n A 1 46 HIS 46 46 46 HIS HIS A . n A 1 47 ASP 47 47 47 ASP ASP A . n A 1 48 ALA 48 48 48 ALA ALA A . n A 1 49 ILE 49 49 49 ILE ILE A . n A 1 50 ALA 50 50 50 ALA ALA A . n A 1 51 ILE 51 51 51 ILE ILE A . n A 1 52 SER 52 52 52 SER SER A . n A 1 53 ARG 53 53 53 ARG ARG A . n A 1 54 SER 54 54 54 SER SER A . n A 1 55 GLN 55 55 55 GLN GLN A . n A 1 56 GLY 56 56 56 GLY GLY A . n A 1 57 PRO 57 57 57 PRO PRO A . n A 1 58 LYS 58 58 58 LYS LYS A . n A 1 59 ALA 59 59 59 ALA ALA A . n A 1 60 GLY 60 60 60 GLY GLY A . n A 1 61 GLY 61 61 61 GLY GLY A . n A 1 62 GLY 62 62 62 GLY GLY A . n A 1 63 ALA 63 63 63 ALA ALA A . n A 1 64 ASP 64 64 64 ASP ASP A . n A 1 65 GLY 65 65 65 GLY GLY A . n A 1 66 SER 66 66 66 SER SER A . n A 1 67 MET 67 67 67 MET MET A . n A 1 68 LEU 68 68 68 LEU LEU A . n A 1 69 LEU 69 69 69 LEU LEU A . n A 1 70 PHE 70 70 70 PHE PHE A . n A 1 71 PRO 71 71 71 PRO PRO A . n A 1 72 THR 72 72 72 THR THR A . n A 1 73 VAL 73 73 73 VAL VAL A . n A 1 74 GLU 74 74 74 GLU GLU A . n A 1 75 PRO 75 75 75 PRO PRO A . n A 1 76 ASN 76 76 76 ASN ASN A . n A 1 77 PHE 77 77 77 PHE PHE A . n A 1 78 SER 78 78 78 SER SER A . n A 1 79 ALA 79 79 79 ALA ALA A . n A 1 80 ASN 80 80 80 ASN ASN A . n A 1 81 ASN 81 81 81 ASN ASN A . n A 1 82 GLY 82 82 82 GLY GLY A . n A 1 83 ILE 83 83 83 ILE ILE A . n A 1 84 ASP 84 84 84 ASP ASP A . n A 1 85 ASP 85 85 85 ASP ASP A . n A 1 86 SER 86 86 86 SER SER A . n A 1 87 VAL 87 87 87 VAL VAL A . n A 1 88 ASN 88 88 88 ASN ASN A . n A 1 89 ASN 89 89 89 ASN ASN A . n A 1 90 LEU 90 90 90 LEU LEU A . n A 1 91 ILE 91 91 91 ILE ILE A . n A 1 92 PRO 92 92 92 PRO PRO A . n A 1 93 PHE 93 93 93 PHE PHE A . n A 1 94 MET 94 94 94 MET MET A . n A 1 95 GLN 95 95 95 GLN GLN A . n A 1 96 LYS 96 96 96 LYS LYS A . n A 1 97 HIS 97 97 97 HIS HIS A . n A 1 98 ASN 98 98 98 ASN ASN A . n A 1 99 THR 99 99 99 THR THR A . n A 1 100 ILE 100 100 100 ILE ILE A . n A 1 101 SER 101 101 101 SER SER A . n A 1 102 ALA 102 102 102 ALA ALA A . n A 1 103 ALA 103 103 103 ALA ALA A . n A 1 104 ASP 104 104 104 ASP ASP A . n A 1 105 LEU 105 105 105 LEU LEU A . n A 1 106 VAL 106 106 106 VAL VAL A . n A 1 107 GLN 107 107 107 GLN GLN A . n A 1 108 PHE 108 108 108 PHE PHE A . n A 1 109 ALA 109 109 109 ALA ALA A . n A 1 110 GLY 110 110 110 GLY GLY A . n A 1 111 ALA 111 111 111 ALA ALA A . n A 1 112 VAL 112 112 112 VAL VAL A . n A 1 113 ALA 113 113 113 ALA ALA A . n A 1 114 LEU 114 114 114 LEU LEU A . n A 1 115 SER 115 115 115 SER SER A . n A 1 116 ASN 116 116 116 ASN ASN A . n A 1 117 CYS 117 117 117 CYS CYS A . n A 1 118 PRO 118 118 118 PRO PRO A . n A 1 119 GLY 119 119 119 GLY GLY A . n A 1 120 ALA 120 120 120 ALA ALA A . n A 1 121 PRO 121 121 121 PRO PRO A . n A 1 122 ARG 122 122 122 ARG ARG A . n A 1 123 LEU 123 123 123 LEU LEU A . n A 1 124 GLU 124 124 124 GLU GLU A . n A 1 125 PHE 125 125 125 PHE PHE A . n A 1 126 LEU 126 126 126 LEU LEU A . n A 1 127 ALA 127 127 127 ALA ALA A . n A 1 128 GLY 128 128 128 GLY GLY A . n A 1 129 ARG 129 129 129 ARG ARG A . n A 1 130 PRO 130 130 130 PRO PRO A . n A 1 131 ASN 131 131 131 ASN ASN A . n A 1 132 LYS 132 132 132 LYS LYS A . n A 1 133 THR 133 133 133 THR THR A . n A 1 134 ILE 134 134 134 ILE ILE A . n A 1 135 ALA 135 135 135 ALA ALA A . n A 1 136 ALA 136 136 136 ALA ALA A . n A 1 137 VAL 137 137 137 VAL VAL A . n A 1 138 ASP 138 138 138 ASP ASP A . n A 1 139 GLY 139 139 139 GLY GLY A . n A 1 140 LEU 140 140 140 LEU LEU A . n A 1 141 ILE 141 141 141 ILE ILE A . n A 1 142 PRO 142 142 142 PRO PRO A . n A 1 143 GLU 143 143 143 GLU GLU A . n A 1 144 PRO 144 144 144 PRO PRO A . n A 1 145 GLN 145 145 145 GLN GLN A . n A 1 146 ASP 146 146 146 ASP ASP A . n A 1 147 SER 147 147 147 SER SER A . n A 1 148 VAL 148 148 148 VAL VAL A . n A 1 149 THR 149 149 149 THR THR A . n A 1 150 LYS 150 150 150 LYS LYS A . n A 1 151 ILE 151 151 151 ILE ILE A . n A 1 152 LEU 152 152 152 LEU LEU A . n A 1 153 GLN 153 153 153 GLN GLN A . n A 1 154 ARG 154 154 154 ARG ARG A . n A 1 155 PHE 155 155 155 PHE PHE A . n A 1 156 GLU 156 156 156 GLU GLU A . n A 1 157 ASP 157 157 157 ASP ASP A . n A 1 158 ALA 158 158 158 ALA ALA A . n A 1 159 GLY 159 159 159 GLY GLY A . n A 1 160 GLY 160 160 160 GLY GLY A . n A 1 161 PHE 161 161 161 PHE PHE A . n A 1 162 THR 162 162 162 THR THR A . n A 1 163 PRO 163 163 163 PRO PRO A . n A 1 164 PHE 164 164 164 PHE PHE A . n A 1 165 GLU 165 165 165 GLU GLU A . n A 1 166 VAL 166 166 166 VAL VAL A . n A 1 167 VAL 167 167 167 VAL VAL A . n A 1 168 SER 168 168 168 SER SER A . n A 1 169 LEU 169 169 169 LEU LEU A . n A 1 170 LEU 170 170 170 LEU LEU A . n A 1 171 ALA 171 171 171 ALA ALA A . n A 1 172 SER 172 172 172 SER SER A . n A 1 173 HIS 173 173 173 HIS HIS A . n A 1 174 SER 174 174 174 SER SER A . n A 1 175 VAL 175 175 175 VAL VAL A . n A 1 176 ALA 176 176 176 ALA ALA A . n A 1 177 ARG 177 177 177 ARG ARG A . n A 1 178 ALA 178 178 178 ALA ALA A . n A 1 179 ASP 179 179 179 ASP ASP A . n A 1 180 LYS 180 180 180 LYS LYS A . n A 1 181 VAL 181 181 181 VAL VAL A . n A 1 182 ASP 182 182 182 ASP ASP A . n A 1 183 GLN 183 183 183 GLN GLN A . n A 1 184 THR 184 184 184 THR THR A . n A 1 185 ILE 185 185 185 ILE ILE A . n A 1 186 ASP 186 186 186 ASP ASP A . n A 1 187 ALA 187 187 187 ALA ALA A . n A 1 188 ALA 188 188 188 ALA ALA A . n A 1 189 PRO 189 189 189 PRO PRO 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 THR 193 193 193 THR THR A . n A 1 194 PRO 194 194 194 PRO PRO A . n A 1 195 PHE 195 195 195 PHE PHE A . n A 1 196 THR 196 196 196 THR THR A . n A 1 197 PHE 197 197 197 PHE PHE A . n A 1 198 ASP 198 198 198 ASP ASP A . n A 1 199 THR 199 199 199 THR THR A . n A 1 200 GLN 200 200 200 GLN GLN A . n A 1 201 VAL 201 201 201 VAL VAL A . n A 1 202 PHE 202 202 202 PHE PHE A . n A 1 203 LEU 203 203 203 LEU LEU A . n A 1 204 GLU 204 204 204 GLU GLU A . n A 1 205 VAL 205 205 205 VAL VAL A . n A 1 206 LEU 206 206 206 LEU LEU A . n A 1 207 LEU 207 207 207 LEU LEU A . n A 1 208 LYS 208 208 208 LYS LYS A . n A 1 209 GLY 209 209 209 GLY GLY A . n A 1 210 VAL 210 210 210 VAL VAL A . n A 1 211 GLY 211 211 211 GLY GLY A . n A 1 212 PHE 212 212 212 PHE PHE A . n A 1 213 PRO 213 213 213 PRO PRO A . n A 1 214 GLY 214 214 214 GLY GLY A . n A 1 215 SER 215 215 215 SER SER A . n A 1 216 ALA 216 216 216 ALA ALA A . n A 1 217 ASN 217 217 217 ASN ASN A . n A 1 218 ASN 218 218 218 ASN ASN A . n A 1 219 THR 219 219 219 THR THR A . n A 1 220 GLY 220 220 220 GLY GLY A . n A 1 221 GLU 221 221 221 GLU GLU A . n A 1 222 VAL 222 222 222 VAL VAL A . n A 1 223 ALA 223 223 223 ALA ALA A . n A 1 224 SER 224 224 224 SER SER A . n A 1 225 PRO 225 225 225 PRO PRO A . n A 1 226 LEU 226 226 226 LEU LEU A . n A 1 227 PRO 227 227 227 PRO PRO A . n A 1 228 LEU 228 228 228 LEU LEU A . n A 1 229 GLY 229 229 229 GLY GLY A . n A 1 230 SER 230 230 230 SER SER A . n A 1 231 GLY 231 231 231 GLY GLY A . n A 1 232 SER 232 232 232 SER SER A . n A 1 233 ASP 233 233 233 ASP ASP A . n A 1 234 THR 234 234 234 THR THR A . n A 1 235 GLY 235 235 235 GLY GLY A . n A 1 236 GLU 236 236 236 GLU GLU A . n A 1 237 MET 237 237 237 MET MET A . n A 1 238 ARG 238 238 238 ARG ARG A . n A 1 239 LEU 239 239 239 LEU LEU A . n A 1 240 GLN 240 240 240 GLN GLN A . n A 1 241 SER 241 241 241 SER SER A . n A 1 242 ASP 242 242 242 ASP ASP A . n A 1 243 PHE 243 243 243 PHE PHE A . n A 1 244 ALA 244 244 244 ALA ALA A . n A 1 245 LEU 245 245 245 LEU LEU A . n A 1 246 ALA 246 246 246 ALA ALA A . n A 1 247 HIS 247 247 247 HIS HIS 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 ARG 250 250 250 ARG ARG A . n A 1 251 THR 251 251 251 THR THR A . n A 1 252 ALA 252 252 252 ALA ALA A . n A 1 253 CYS 253 253 253 CYS CYS A . n A 1 254 ILE 254 254 254 ILE ILE A . n A 1 255 TRP 255 255 255 TRP TRP A . n A 1 256 GLN 256 256 256 GLN GLN A . n A 1 257 GLY 257 257 257 GLY GLY A . n A 1 258 PHE 258 258 258 PHE PHE A . n A 1 259 VAL 259 259 259 VAL VAL A . n A 1 260 ASN 260 260 260 ASN ASN A . n A 1 261 GLU 261 261 261 GLU GLU A . n A 1 262 GLN 262 262 262 GLN GLN A . n A 1 263 ALA 263 263 263 ALA ALA A . n A 1 264 PHE 264 264 264 PHE PHE A . n A 1 265 MET 265 265 265 MET MET A . n A 1 266 ALA 266 266 266 ALA ALA A . n A 1 267 ALA 267 267 267 ALA ALA A . n A 1 268 SER 268 268 268 SER SER A . n A 1 269 PHE 269 269 269 PHE PHE A . n A 1 270 ARG 270 270 270 ARG ARG A . n A 1 271 ALA 271 271 271 ALA ALA A . n A 1 272 ALA 272 272 272 ALA ALA A . n A 1 273 MET 273 273 273 MET MET A . n A 1 274 SER 274 274 274 SER SER A . n A 1 275 LYS 275 275 275 LYS LYS A . n A 1 276 LEU 276 276 276 LEU LEU A . n A 1 277 ALA 277 277 277 ALA ALA A . n A 1 278 VAL 278 278 278 VAL VAL A . n A 1 279 LEU 279 279 279 LEU LEU A . n A 1 280 GLY 280 280 280 GLY GLY A . n A 1 281 HIS 281 281 281 HIS HIS A . n A 1 282 ASN 282 282 282 ASN ASN A . n A 1 283 ARG 283 283 283 ARG ARG A . n A 1 284 ASN 284 284 284 ASN ASN A . n A 1 285 SER 285 285 285 SER SER A . n A 1 286 LEU 286 286 286 LEU LEU A . n A 1 287 ILE 287 287 287 ILE ILE A . n A 1 288 ASP 288 288 288 ASP ASP A . n A 1 289 CYS 289 289 289 CYS CYS A . n A 1 290 SER 290 290 290 SER SER A . n A 1 291 ASP 291 291 291 ASP ASP A . n A 1 292 VAL 292 292 292 VAL VAL A . n A 1 293 VAL 293 293 293 VAL VAL A . n A 1 294 PRO 294 294 294 PRO PRO A . n A 1 295 VAL 295 295 295 VAL VAL A . n A 1 296 PRO 296 296 296 PRO PRO A . n A 1 297 LYS 297 297 297 LYS LYS A . n A 1 298 PRO 298 298 298 PRO PRO A . n A 1 299 ALA 299 299 299 ALA ALA A . n A 1 300 THR 300 300 300 THR THR A . n A 1 301 GLY 301 301 301 GLY GLY A . n A 1 302 GLN 302 302 302 GLN GLN A . n A 1 303 PRO 303 303 303 PRO PRO A . n A 1 304 ALA 304 304 304 ALA ALA A . n A 1 305 MET 305 305 305 MET MET A . n A 1 306 PHE 306 306 306 PHE PHE A . n A 1 307 PRO 307 307 307 PRO PRO A . n A 1 308 ALA 308 308 308 ALA ALA A . n A 1 309 SER 309 309 309 SER SER A . n A 1 310 THR 310 310 310 THR THR A . n A 1 311 GLY 311 311 311 GLY GLY A . n A 1 312 PRO 312 312 312 PRO PRO A . n A 1 313 GLN 313 313 313 GLN GLN A . n A 1 314 ASP 314 314 314 ASP ASP A . n A 1 315 LEU 315 315 315 LEU LEU A . n A 1 316 GLU 316 316 316 GLU GLU A . n A 1 317 LEU 317 317 317 LEU LEU A . n A 1 318 SER 318 318 318 SER SER A . n A 1 319 CYS 319 319 319 CYS CYS A . n A 1 320 PRO 320 320 320 PRO PRO A . n A 1 321 SER 321 321 321 SER SER A . n A 1 322 GLU 322 322 322 GLU GLU A . n A 1 323 ARG 323 323 323 ARG ARG A . n A 1 324 PHE 324 324 324 PHE PHE A . n A 1 325 PRO 325 325 325 PRO PRO A . n A 1 326 THR 326 326 326 THR THR A . n A 1 327 LEU 327 327 327 LEU LEU A . n A 1 328 THR 328 328 328 THR THR A . n A 1 329 THR 329 329 329 THR THR A . n A 1 330 GLN 330 330 330 GLN GLN A . n A 1 331 PRO 331 331 331 PRO PRO A . n A 1 332 GLY 332 332 332 GLY GLY A . n A 1 333 ALA 333 333 333 ALA ALA A . n A 1 334 SER 334 334 334 SER SER A . n A 1 335 GLN 335 335 335 GLN GLN A . n A 1 336 SER 336 336 336 SER SER A . n A 1 337 LEU 337 337 337 LEU LEU A . n A 1 338 ILE 338 338 338 ILE ILE A . n A 1 339 ALA 339 339 339 ALA ALA A . n A 1 340 HIS 340 340 340 HIS HIS A . n A 1 341 CYS 341 341 341 CYS CYS A . n A 1 342 PRO 342 342 342 PRO PRO A . n A 1 343 ASP 343 343 343 ASP ASP A . n A 1 344 GLY 344 344 344 GLY GLY A . n A 1 345 SER 345 345 345 SER SER A . n A 1 346 MET 346 346 346 MET MET A . n A 1 347 SER 347 347 347 SER SER A . n A 1 348 CYS 348 348 348 CYS CYS A . n A 1 349 PRO 349 349 349 PRO PRO A . n A 1 350 GLY 350 350 350 GLY GLY A . n A 1 351 VAL 351 351 351 VAL VAL A . n A 1 352 GLN 352 352 352 GLN GLN A . n A 1 353 PHE 353 353 353 PHE PHE A . n A 1 354 ASN 354 354 354 ASN ASN A . n A 1 355 GLY 355 355 355 GLY GLY A . n A 1 356 PRO 356 356 356 PRO PRO A . n A 1 357 ALA 357 357 357 ALA ALA A . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 NAG 1 361 361 NAG NAG A . C 2 NAG 2 362 362 NAG NAG A . D 3 MAN 1 364 364 MAN MAN A . E 4 CA 1 371 371 CA CA A . F 4 CA 1 372 372 CA CA A . G 5 MN 1 381 381 MN MN A . H 6 GOL 1 391 391 GOL GOL A . I 7 HEM 1 396 396 HEM HEM A . J 8 HOH 1 1001 1001 HOH HOH A . J 8 HOH 2 1002 1002 HOH HOH A . J 8 HOH 3 1003 1003 HOH HOH A . J 8 HOH 4 1004 1004 HOH HOH A . J 8 HOH 5 1005 1005 HOH HOH A . J 8 HOH 6 1006 1006 HOH HOH A . J 8 HOH 7 1007 1007 HOH HOH A . J 8 HOH 8 1008 1008 HOH HOH A . J 8 HOH 9 1009 1009 HOH HOH A . J 8 HOH 10 1010 1010 HOH HOH A . J 8 HOH 11 1011 1011 HOH HOH A . J 8 HOH 12 1012 1012 HOH HOH A . J 8 HOH 13 1013 1013 HOH HOH A . J 8 HOH 14 1014 1014 HOH HOH A . J 8 HOH 15 1015 1015 HOH HOH A . J 8 HOH 16 1016 1016 HOH HOH A . J 8 HOH 17 1017 1017 HOH HOH A . J 8 HOH 18 1018 1018 HOH HOH A . J 8 HOH 19 1019 1019 HOH HOH A . J 8 HOH 20 1020 1020 HOH HOH A . J 8 HOH 21 1021 1021 HOH HOH A . J 8 HOH 22 1022 1022 HOH HOH A . J 8 HOH 23 1023 1023 HOH HOH A . J 8 HOH 24 1024 1024 HOH HOH A . J 8 HOH 25 1025 1025 HOH HOH A . J 8 HOH 26 1026 1026 HOH HOH A . J 8 HOH 27 1027 1027 HOH HOH A . J 8 HOH 28 1028 1028 HOH HOH A . J 8 HOH 29 1029 1029 HOH HOH A . J 8 HOH 30 1030 1030 HOH HOH A . J 8 HOH 31 1031 1031 HOH HOH A . J 8 HOH 32 1032 1032 HOH HOH A . J 8 HOH 33 1033 1033 HOH HOH A . J 8 HOH 34 1034 1034 HOH HOH A . J 8 HOH 35 1035 1035 HOH HOH A . J 8 HOH 36 1036 1036 HOH HOH A . J 8 HOH 37 1037 1037 HOH HOH A . J 8 HOH 38 1038 1038 HOH HOH A . J 8 HOH 39 1039 1039 HOH HOH A . J 8 HOH 40 1040 1040 HOH HOH A . J 8 HOH 41 1041 1041 HOH HOH A . J 8 HOH 42 1042 1042 HOH HOH A . J 8 HOH 43 1043 1043 HOH HOH A . J 8 HOH 44 1044 1044 HOH HOH A . J 8 HOH 45 1045 1045 HOH HOH A . J 8 HOH 46 1046 1046 HOH HOH A . J 8 HOH 47 1047 1047 HOH HOH A . J 8 HOH 48 1048 1048 HOH HOH A . J 8 HOH 49 1049 1049 HOH HOH A . J 8 HOH 50 1050 1050 HOH HOH A . J 8 HOH 51 1051 1051 HOH HOH A . J 8 HOH 52 1052 1052 HOH HOH A . J 8 HOH 53 1053 1053 HOH HOH A . J 8 HOH 54 1054 1054 HOH HOH A . J 8 HOH 55 1055 1055 HOH HOH A . J 8 HOH 56 1056 1056 HOH HOH A . J 8 HOH 57 1057 1057 HOH HOH A . J 8 HOH 58 1058 1058 HOH HOH A . J 8 HOH 59 1059 1059 HOH HOH A . J 8 HOH 60 1060 1060 HOH HOH A . J 8 HOH 61 1061 1061 HOH HOH A . J 8 HOH 62 1062 1062 HOH HOH A . J 8 HOH 63 1063 1063 HOH HOH A . J 8 HOH 64 1064 1064 HOH HOH A . J 8 HOH 65 1065 1065 HOH HOH A . J 8 HOH 66 1066 1066 HOH HOH A . J 8 HOH 67 1067 1067 HOH HOH A . J 8 HOH 68 1068 1068 HOH HOH A . J 8 HOH 69 1069 1069 HOH HOH A . J 8 HOH 70 1070 1070 HOH HOH A . J 8 HOH 71 1071 1071 HOH HOH A . J 8 HOH 72 1072 1072 HOH HOH A . J 8 HOH 73 1073 1073 HOH HOH A . J 8 HOH 74 1074 1074 HOH HOH A . J 8 HOH 75 1075 1075 HOH HOH A . J 8 HOH 76 1076 1076 HOH HOH A . J 8 HOH 77 1077 1077 HOH HOH A . J 8 HOH 78 1078 1078 HOH HOH A . J 8 HOH 79 1079 1079 HOH HOH A . J 8 HOH 80 1080 1080 HOH HOH A . J 8 HOH 81 1081 1081 HOH HOH A . J 8 HOH 82 1082 1082 HOH HOH A . J 8 HOH 83 1083 1083 HOH HOH A . J 8 HOH 84 1084 1084 HOH HOH A . J 8 HOH 85 1085 1085 HOH HOH A . J 8 HOH 86 1086 1086 HOH HOH A . J 8 HOH 87 1087 1087 HOH HOH A . J 8 HOH 88 1088 1088 HOH HOH A . J 8 HOH 89 1089 1089 HOH HOH A . J 8 HOH 90 1090 1090 HOH HOH A . J 8 HOH 91 1091 1091 HOH HOH A . J 8 HOH 92 1092 1092 HOH HOH A . J 8 HOH 93 1093 1093 HOH HOH A . J 8 HOH 94 1094 1094 HOH HOH A . J 8 HOH 95 1095 1095 HOH HOH A . J 8 HOH 96 1096 1096 HOH HOH A . J 8 HOH 97 1097 1097 HOH HOH A . J 8 HOH 98 1098 1098 HOH HOH A . J 8 HOH 99 1099 1099 HOH HOH A . J 8 HOH 100 1100 1100 HOH HOH A . J 8 HOH 101 1101 1101 HOH HOH A . J 8 HOH 102 1102 1102 HOH HOH A . J 8 HOH 103 1103 1103 HOH HOH A . J 8 HOH 104 1104 1104 HOH HOH A . J 8 HOH 105 1105 1105 HOH HOH A . J 8 HOH 106 1106 1106 HOH HOH A . J 8 HOH 107 1107 1107 HOH HOH A . J 8 HOH 108 1108 1108 HOH HOH A . J 8 HOH 109 1109 1109 HOH HOH A . J 8 HOH 110 1110 1110 HOH HOH A . J 8 HOH 111 1111 1111 HOH HOH A . J 8 HOH 112 1112 1112 HOH HOH A . J 8 HOH 113 1113 1113 HOH HOH A . J 8 HOH 114 1114 1114 HOH HOH A . J 8 HOH 115 1115 1115 HOH HOH A . J 8 HOH 116 1116 1116 HOH HOH A . J 8 HOH 117 1117 1117 HOH HOH A . J 8 HOH 118 1118 1118 HOH HOH A . J 8 HOH 119 1119 1119 HOH HOH A . J 8 HOH 120 1120 1120 HOH HOH A . J 8 HOH 121 1121 1121 HOH HOH A . J 8 HOH 122 1122 1122 HOH HOH A . J 8 HOH 123 1123 1123 HOH HOH A . J 8 HOH 124 1124 1124 HOH HOH A . J 8 HOH 125 1125 1125 HOH HOH A . J 8 HOH 126 1126 1126 HOH HOH A . J 8 HOH 127 1127 1127 HOH HOH A . J 8 HOH 128 1128 1128 HOH HOH A . J 8 HOH 129 1129 1129 HOH HOH A . J 8 HOH 130 1130 1130 HOH HOH A . J 8 HOH 131 1131 1131 HOH HOH A . J 8 HOH 132 1132 1132 HOH HOH A . J 8 HOH 133 1133 1133 HOH HOH A . J 8 HOH 134 1134 1134 HOH HOH A . J 8 HOH 135 1135 1135 HOH HOH A . J 8 HOH 136 1136 1136 HOH HOH A . J 8 HOH 137 1137 1137 HOH HOH A . J 8 HOH 138 1138 1138 HOH HOH A . J 8 HOH 139 1139 1139 HOH HOH A . J 8 HOH 140 1140 1140 HOH HOH A . J 8 HOH 141 1141 1141 HOH HOH A . J 8 HOH 142 1142 1142 HOH HOH A . J 8 HOH 143 1143 1143 HOH HOH A . J 8 HOH 144 1144 1144 HOH HOH A . J 8 HOH 145 1145 1145 HOH HOH A . J 8 HOH 146 1146 1146 HOH HOH A . J 8 HOH 147 1147 1147 HOH HOH A . J 8 HOH 148 1148 1148 HOH HOH A . J 8 HOH 149 1149 1149 HOH HOH A . J 8 HOH 150 1150 1150 HOH HOH A . J 8 HOH 151 1151 1151 HOH HOH A . J 8 HOH 152 1152 1152 HOH HOH A . J 8 HOH 153 1153 1153 HOH HOH A . J 8 HOH 154 1154 1154 HOH HOH A . J 8 HOH 155 1155 1155 HOH HOH A . J 8 HOH 156 1156 1156 HOH HOH A . J 8 HOH 157 1157 1157 HOH HOH A . J 8 HOH 158 1158 1158 HOH HOH A . J 8 HOH 159 1159 1159 HOH HOH A . J 8 HOH 160 1160 1160 HOH HOH A . J 8 HOH 161 1161 1161 HOH HOH A . J 8 HOH 162 1162 1162 HOH HOH A . J 8 HOH 163 1163 1163 HOH HOH A . J 8 HOH 164 1164 1164 HOH HOH A . J 8 HOH 165 1165 1165 HOH HOH A . J 8 HOH 166 1166 1166 HOH HOH A . J 8 HOH 167 1167 1167 HOH HOH A . J 8 HOH 168 1168 1168 HOH HOH A . J 8 HOH 169 1169 1169 HOH HOH A . J 8 HOH 170 1170 1170 HOH HOH A . J 8 HOH 171 1171 1171 HOH HOH A . J 8 HOH 172 1172 1172 HOH HOH A . J 8 HOH 173 1173 1173 HOH HOH A . J 8 HOH 174 1174 1174 HOH HOH A . J 8 HOH 175 1175 1175 HOH HOH A . J 8 HOH 176 1176 1176 HOH HOH A . J 8 HOH 177 1177 1177 HOH HOH A . J 8 HOH 178 1178 1178 HOH HOH A . J 8 HOH 179 1179 1179 HOH HOH A . J 8 HOH 180 1180 1180 HOH HOH A . J 8 HOH 181 1181 1181 HOH HOH A . J 8 HOH 182 1182 1182 HOH HOH A . J 8 HOH 183 1184 1184 HOH HOH A . J 8 HOH 184 1185 1185 HOH HOH A . J 8 HOH 185 1186 1186 HOH HOH A . J 8 HOH 186 1187 1187 HOH HOH A . J 8 HOH 187 1188 1188 HOH HOH A . J 8 HOH 188 1189 1189 HOH HOH A . J 8 HOH 189 1190 1190 HOH HOH A . J 8 HOH 190 1191 1191 HOH HOH A . J 8 HOH 191 1192 1192 HOH HOH A . J 8 HOH 192 1193 1193 HOH HOH A . J 8 HOH 193 1194 1194 HOH HOH A . J 8 HOH 194 1195 1195 HOH HOH A . J 8 HOH 195 1196 1196 HOH HOH A . J 8 HOH 196 1197 1197 HOH HOH A . J 8 HOH 197 1198 1198 HOH HOH A . J 8 HOH 198 1199 1199 HOH HOH A . J 8 HOH 199 1200 1200 HOH HOH A . J 8 HOH 200 1201 1201 HOH HOH A . J 8 HOH 201 1202 1202 HOH HOH A . J 8 HOH 202 1203 1203 HOH HOH A . J 8 HOH 203 1204 1204 HOH HOH A . J 8 HOH 204 1205 1205 HOH HOH A . J 8 HOH 205 1206 1206 HOH HOH A . J 8 HOH 206 1207 1207 HOH HOH A . J 8 HOH 207 1208 1208 HOH HOH A . J 8 HOH 208 1209 1209 HOH HOH A . J 8 HOH 209 1210 1210 HOH HOH A . J 8 HOH 210 1211 1211 HOH HOH A . J 8 HOH 211 1212 1212 HOH HOH A . J 8 HOH 212 1213 1213 HOH HOH A . J 8 HOH 213 1214 1214 HOH HOH A . J 8 HOH 214 1215 1215 HOH HOH A . J 8 HOH 215 1216 1216 HOH HOH A . J 8 HOH 216 1217 1217 HOH HOH A . J 8 HOH 217 1218 1218 HOH HOH A . J 8 HOH 218 1219 1219 HOH HOH A . J 8 HOH 219 1220 1220 HOH HOH A . J 8 HOH 220 1221 1221 HOH HOH A . J 8 HOH 221 1222 1222 HOH HOH A . J 8 HOH 222 1223 1223 HOH HOH A . J 8 HOH 223 1224 1224 HOH HOH A . J 8 HOH 224 1225 1225 HOH HOH A . J 8 HOH 225 1226 1226 HOH HOH A . J 8 HOH 226 1227 1227 HOH HOH A . J 8 HOH 227 1228 1228 HOH HOH A . J 8 HOH 228 1229 1229 HOH HOH A . J 8 HOH 229 1230 1230 HOH HOH A . J 8 HOH 230 1231 1231 HOH HOH A . J 8 HOH 231 1232 1232 HOH HOH A . J 8 HOH 232 1234 1234 HOH HOH A . J 8 HOH 233 1235 1235 HOH HOH A . J 8 HOH 234 1236 1236 HOH HOH A . J 8 HOH 235 1237 1237 HOH HOH A . J 8 HOH 236 1238 1238 HOH HOH A . J 8 HOH 237 1239 1239 HOH HOH A . J 8 HOH 238 1240 1240 HOH HOH A . J 8 HOH 239 1241 1241 HOH HOH A . J 8 HOH 240 1242 1242 HOH HOH A . J 8 HOH 241 1243 1243 HOH HOH A . J 8 HOH 242 1245 1245 HOH HOH A . J 8 HOH 243 1246 1246 HOH HOH A . J 8 HOH 244 1247 1247 HOH HOH A . J 8 HOH 245 1248 1248 HOH HOH A . J 8 HOH 246 1249 1249 HOH HOH A . J 8 HOH 247 1250 1250 HOH HOH A . J 8 HOH 248 1251 1251 HOH HOH A . J 8 HOH 249 1252 1252 HOH HOH A . J 8 HOH 250 1253 1253 HOH HOH A . J 8 HOH 251 1254 1254 HOH HOH A . J 8 HOH 252 1255 1255 HOH HOH A . J 8 HOH 253 1256 1256 HOH HOH A . J 8 HOH 254 1257 1257 HOH HOH A . J 8 HOH 255 1258 1258 HOH HOH A . J 8 HOH 256 1260 1260 HOH HOH A . J 8 HOH 257 1261 1261 HOH HOH A . J 8 HOH 258 1262 1262 HOH HOH A . J 8 HOH 259 1263 1263 HOH HOH A . J 8 HOH 260 1264 1264 HOH HOH A . J 8 HOH 261 1266 1266 HOH HOH A . J 8 HOH 262 1268 1268 HOH HOH A . J 8 HOH 263 1269 1269 HOH HOH A . J 8 HOH 264 1270 1270 HOH HOH A . J 8 HOH 265 1271 1271 HOH HOH A . J 8 HOH 266 1272 1272 HOH HOH A . J 8 HOH 267 1273 1273 HOH HOH A . J 8 HOH 268 1274 1274 HOH HOH A . J 8 HOH 269 1275 1275 HOH HOH A . J 8 HOH 270 1277 1277 HOH HOH A . J 8 HOH 271 1278 1278 HOH HOH A . J 8 HOH 272 1279 1279 HOH HOH A . J 8 HOH 273 1280 1280 HOH HOH A . J 8 HOH 274 1281 1281 HOH HOH A . J 8 HOH 275 1282 1282 HOH HOH A . J 8 HOH 276 1283 1283 HOH HOH A . J 8 HOH 277 1284 1284 HOH HOH A . J 8 HOH 278 1285 1285 HOH HOH A . J 8 HOH 279 1286 1286 HOH HOH A . J 8 HOH 280 1287 1287 HOH HOH A . J 8 HOH 281 1288 1288 HOH HOH A . J 8 HOH 282 1289 1289 HOH HOH A . J 8 HOH 283 1290 1290 HOH HOH A . J 8 HOH 284 1291 1291 HOH HOH A . J 8 HOH 285 1292 1292 HOH HOH A . J 8 HOH 286 1293 1293 HOH HOH A . J 8 HOH 287 1294 1294 HOH HOH A . J 8 HOH 288 1295 1295 HOH HOH A . J 8 HOH 289 1296 1296 HOH HOH A . J 8 HOH 290 1297 1297 HOH HOH A . J 8 HOH 291 1298 1298 HOH HOH A . J 8 HOH 292 1299 1299 HOH HOH A . J 8 HOH 293 1300 1300 HOH HOH A . J 8 HOH 294 1301 1301 HOH HOH A . J 8 HOH 295 1302 1302 HOH HOH A . J 8 HOH 296 1303 1303 HOH HOH A . J 8 HOH 297 1304 1304 HOH HOH A . J 8 HOH 298 1305 1305 HOH HOH A . J 8 HOH 299 1306 1306 HOH HOH A . J 8 HOH 300 1307 1307 HOH HOH A . J 8 HOH 301 1308 1308 HOH HOH A . J 8 HOH 302 1309 1309 HOH HOH A . J 8 HOH 303 1310 1310 HOH HOH A . J 8 HOH 304 1311 1311 HOH HOH A . J 8 HOH 305 1312 1312 HOH HOH A . J 8 HOH 306 1313 1313 HOH HOH A . J 8 HOH 307 1314 1314 HOH HOH A . J 8 HOH 308 1315 1315 HOH HOH A . J 8 HOH 309 1316 1316 HOH HOH A . J 8 HOH 310 1317 1317 HOH HOH A . J 8 HOH 311 1319 1319 HOH HOH A . J 8 HOH 312 1320 1320 HOH HOH A . J 8 HOH 313 1321 1321 HOH HOH A . J 8 HOH 314 1322 1322 HOH HOH A . J 8 HOH 315 1324 1324 HOH HOH A . J 8 HOH 316 1328 1328 HOH HOH A . J 8 HOH 317 1329 1329 HOH HOH A . J 8 HOH 318 1330 1330 HOH HOH A . J 8 HOH 319 1331 1331 HOH HOH A . J 8 HOH 320 1333 1333 HOH HOH A . J 8 HOH 321 1334 1334 HOH HOH A . J 8 HOH 322 1335 1335 HOH HOH A . J 8 HOH 323 1336 1336 HOH HOH A . J 8 HOH 324 1337 1337 HOH HOH A . J 8 HOH 325 1338 1338 HOH HOH A . J 8 HOH 326 1340 1340 HOH HOH A . J 8 HOH 327 1341 1341 HOH HOH A . J 8 HOH 328 1342 1342 HOH HOH A . J 8 HOH 329 1343 1343 HOH HOH A . J 8 HOH 330 1345 1345 HOH HOH A . J 8 HOH 331 1346 1346 HOH HOH A . J 8 HOH 332 1347 1347 HOH HOH A . J 8 HOH 333 1348 1348 HOH HOH A . J 8 HOH 334 1349 1349 HOH HOH A . J 8 HOH 335 1350 1350 HOH HOH A . J 8 HOH 336 1351 1351 HOH HOH A . J 8 HOH 337 1354 1354 HOH HOH A . J 8 HOH 338 1355 1355 HOH HOH A . J 8 HOH 339 1356 1356 HOH HOH A . J 8 HOH 340 1358 1358 HOH HOH A . J 8 HOH 341 1359 1359 HOH HOH A . J 8 HOH 342 1360 1360 HOH HOH A . J 8 HOH 343 1362 1362 HOH HOH A . J 8 HOH 344 1364 1364 HOH HOH A . J 8 HOH 345 1365 1365 HOH HOH A . J 8 HOH 346 1366 1366 HOH HOH A . J 8 HOH 347 1367 1367 HOH HOH A . J 8 HOH 348 1369 1369 HOH HOH A . J 8 HOH 349 1370 1370 HOH HOH A . J 8 HOH 350 1371 1371 HOH HOH A . J 8 HOH 351 1372 1372 HOH HOH A . J 8 HOH 352 1373 1373 HOH HOH A . J 8 HOH 353 1374 1374 HOH HOH A . J 8 HOH 354 1376 1376 HOH HOH A . J 8 HOH 355 1377 1377 HOH HOH A . J 8 HOH 356 1380 1380 HOH HOH A . J 8 HOH 357 1381 1381 HOH HOH A . J 8 HOH 358 1383 1383 HOH HOH A . J 8 HOH 359 1385 1385 HOH HOH A . J 8 HOH 360 1386 1386 HOH HOH A . J 8 HOH 361 1387 1387 HOH HOH A . J 8 HOH 362 1388 1388 HOH HOH A . J 8 HOH 363 1389 1389 HOH HOH A . J 8 HOH 364 1390 1390 HOH HOH A . J 8 HOH 365 1391 1391 HOH HOH A . J 8 HOH 366 1392 1392 HOH HOH A . J 8 HOH 367 1393 1393 HOH HOH A . J 8 HOH 368 1394 1394 HOH HOH A . J 8 HOH 369 1395 1395 HOH HOH A . J 8 HOH 370 1397 1397 HOH HOH A . J 8 HOH 371 1398 1398 HOH HOH A . J 8 HOH 372 1399 1399 HOH HOH A . J 8 HOH 373 1400 1400 HOH HOH A . J 8 HOH 374 1401 1401 HOH HOH A . J 8 HOH 375 1402 1402 HOH HOH A . J 8 HOH 376 1403 1403 HOH HOH A . J 8 HOH 377 1404 1404 HOH HOH A . J 8 HOH 378 1405 1405 HOH HOH A . J 8 HOH 379 1409 1409 HOH HOH A . J 8 HOH 380 1410 1410 HOH HOH A . J 8 HOH 381 1411 1411 HOH HOH A . J 8 HOH 382 1414 1414 HOH HOH A . J 8 HOH 383 1415 1415 HOH HOH A . J 8 HOH 384 1417 1417 HOH HOH A . J 8 HOH 385 1418 1418 HOH HOH A . J 8 HOH 386 1419 1419 HOH HOH A . J 8 HOH 387 1420 1420 HOH HOH A . J 8 HOH 388 1423 1423 HOH HOH A . J 8 HOH 389 1424 1424 HOH HOH A . J 8 HOH 390 1427 1427 HOH HOH A . J 8 HOH 391 1428 1428 HOH HOH A . J 8 HOH 392 1430 1430 HOH HOH A . J 8 HOH 393 1432 1432 HOH HOH A . J 8 HOH 394 1437 1437 HOH HOH A . J 8 HOH 395 1438 1438 HOH HOH A . J 8 HOH 396 1440 1440 HOH HOH A . J 8 HOH 397 1442 1442 HOH HOH A . J 8 HOH 398 1444 1444 HOH HOH A . J 8 HOH 399 1447 1447 HOH HOH A . J 8 HOH 400 1448 1448 HOH HOH A . J 8 HOH 401 1449 1449 HOH HOH A . J 8 HOH 402 1450 1450 HOH HOH A . J 8 HOH 403 1451 1451 HOH HOH A . J 8 HOH 404 1452 1452 HOH HOH A . J 8 HOH 405 1454 1454 HOH HOH A . J 8 HOH 406 1455 1455 HOH HOH A . J 8 HOH 407 1456 1456 HOH HOH A . J 8 HOH 408 1457 1457 HOH HOH A . J 8 HOH 409 1460 1460 HOH HOH A . J 8 HOH 410 1461 1461 HOH HOH A . J 8 HOH 411 1462 1462 HOH HOH A . J 8 HOH 412 1463 1463 HOH HOH A . J 8 HOH 413 1470 1470 HOH HOH A . J 8 HOH 414 1473 1473 HOH HOH A . J 8 HOH 415 1475 1475 HOH HOH A . J 8 HOH 416 1476 1476 HOH HOH A . J 8 HOH 417 1477 1477 HOH HOH A . J 8 HOH 418 1478 1478 HOH HOH A . J 8 HOH 419 1479 1479 HOH HOH A . J 8 HOH 420 1481 1481 HOH HOH A . J 8 HOH 421 1482 1482 HOH HOH A . J 8 HOH 422 1484 1484 HOH HOH A . J 8 HOH 423 1485 1485 HOH HOH A . J 8 HOH 424 1487 1487 HOH HOH A . J 8 HOH 425 1488 1488 HOH HOH A . J 8 HOH 426 1489 1489 HOH HOH A . J 8 HOH 427 1492 1492 HOH HOH A . J 8 HOH 428 1494 1494 HOH HOH A . J 8 HOH 429 1495 1495 HOH HOH A . J 8 HOH 430 1496 1496 HOH HOH A . J 8 HOH 431 1497 1497 HOH HOH A . J 8 HOH 432 1498 1498 HOH HOH A . J 8 HOH 433 1499 1499 HOH HOH A . J 8 HOH 434 1502 1502 HOH HOH A . J 8 HOH 435 1503 1503 HOH HOH A . J 8 HOH 436 1504 1504 HOH HOH A . J 8 HOH 437 1505 1505 HOH HOH A . J 8 HOH 438 1507 1507 HOH HOH A . J 8 HOH 439 1508 1508 HOH HOH A . J 8 HOH 440 1509 1509 HOH HOH A . J 8 HOH 441 1510 1510 HOH HOH A . J 8 HOH 442 1511 1511 HOH HOH A . J 8 HOH 443 1512 1512 HOH HOH A . J 8 HOH 444 1513 1513 HOH HOH A . J 8 HOH 445 1514 1514 HOH HOH A . J 8 HOH 446 1517 1517 HOH HOH A . J 8 HOH 447 1518 1518 HOH HOH A . J 8 HOH 448 1520 1520 HOH HOH A . J 8 HOH 449 1521 1521 HOH HOH A . J 8 HOH 450 1523 1523 HOH HOH A . J 8 HOH 451 1524 1524 HOH HOH A . J 8 HOH 452 1526 1526 HOH HOH A . J 8 HOH 453 1528 1528 HOH HOH A . J 8 HOH 454 1529 1529 HOH HOH A . J 8 HOH 455 1531 1531 HOH HOH A . J 8 HOH 456 1532 1532 HOH HOH A . J 8 HOH 457 1533 1533 HOH HOH A . J 8 HOH 458 1534 1534 HOH HOH A . J 8 HOH 459 1537 1537 HOH HOH A . J 8 HOH 460 1541 1541 HOH HOH A . J 8 HOH 461 1543 1543 HOH HOH A . J 8 HOH 462 1547 1547 HOH HOH A . J 8 HOH 463 1550 1550 HOH HOH A . J 8 HOH 464 1551 1551 HOH HOH A . J 8 HOH 465 1554 1554 HOH HOH A . J 8 HOH 466 1555 1555 HOH HOH A . J 8 HOH 467 1556 1556 HOH HOH A . J 8 HOH 468 1557 1557 HOH HOH A . J 8 HOH 469 1558 1558 HOH HOH A . J 8 HOH 470 1564 1564 HOH HOH A . J 8 HOH 471 1565 1565 HOH HOH A . J 8 HOH 472 1566 1566 HOH HOH A . J 8 HOH 473 1567 1567 HOH HOH A . J 8 HOH 474 1568 1568 HOH HOH A . J 8 HOH 475 1570 1570 HOH HOH A . J 8 HOH 476 1571 1571 HOH HOH A . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 131 A ASN 131 ? ASN 'GLYCOSYLATION SITE' 2 A SER 336 A SER 336 ? SER 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 NE2 ? A HIS 173 ? A HIS 173 ? 1_555 FE ? I HEM . ? A HEM 396 ? 1_555 NA ? I HEM . ? A HEM 396 ? 1_555 98.6 ? 2 NE2 ? A HIS 173 ? A HIS 173 ? 1_555 FE ? I HEM . ? A HEM 396 ? 1_555 NB ? I HEM . ? A HEM 396 ? 1_555 93.8 ? 3 NA ? I HEM . ? A HEM 396 ? 1_555 FE ? I HEM . ? A HEM 396 ? 1_555 NB ? I HEM . ? A HEM 396 ? 1_555 89.7 ? 4 NE2 ? A HIS 173 ? A HIS 173 ? 1_555 FE ? I HEM . ? A HEM 396 ? 1_555 NC ? I HEM . ? A HEM 396 ? 1_555 97.2 ? 5 NA ? I HEM . ? A HEM 396 ? 1_555 FE ? I HEM . ? A HEM 396 ? 1_555 NC ? I HEM . ? A HEM 396 ? 1_555 164.2 ? 6 NB ? I HEM . ? A HEM 396 ? 1_555 FE ? I HEM . ? A HEM 396 ? 1_555 NC ? I HEM . ? A HEM 396 ? 1_555 89.9 ? 7 NE2 ? A HIS 173 ? A HIS 173 ? 1_555 FE ? I HEM . ? A HEM 396 ? 1_555 ND ? I HEM . ? A HEM 396 ? 1_555 99.1 ? 8 NA ? I HEM . ? A HEM 396 ? 1_555 FE ? I HEM . ? A HEM 396 ? 1_555 ND ? I HEM . ? A HEM 396 ? 1_555 88.1 ? 9 NB ? I HEM . ? A HEM 396 ? 1_555 FE ? I HEM . ? A HEM 396 ? 1_555 ND ? I HEM . ? A HEM 396 ? 1_555 167.1 ? 10 NC ? I HEM . ? A HEM 396 ? 1_555 FE ? I HEM . ? A HEM 396 ? 1_555 ND ? I HEM . ? A HEM 396 ? 1_555 88.7 ? 11 NE2 ? A HIS 173 ? A HIS 173 ? 1_555 FE ? I HEM . ? A HEM 396 ? 1_555 O ? J HOH . ? A HOH 1137 ? 1_555 174.4 ? 12 NA ? I HEM . ? A HEM 396 ? 1_555 FE ? I HEM . ? A HEM 396 ? 1_555 O ? J HOH . ? A HOH 1137 ? 1_555 77.1 ? 13 NB ? I HEM . ? A HEM 396 ? 1_555 FE ? I HEM . ? A HEM 396 ? 1_555 O ? J HOH . ? A HOH 1137 ? 1_555 82.7 ? 14 NC ? I HEM . ? A HEM 396 ? 1_555 FE ? I HEM . ? A HEM 396 ? 1_555 O ? J HOH . ? A HOH 1137 ? 1_555 87.1 ? 15 ND ? I HEM . ? A HEM 396 ? 1_555 FE ? I HEM . ? A HEM 396 ? 1_555 O ? J HOH . ? A HOH 1137 ? 1_555 84.5 ? 16 O1D ? I HEM . ? A HEM 396 ? 1_555 MN ? G MN . ? A MN 381 ? 1_555 OE2 ? A GLU 39 ? A GLU 39 ? 1_555 85.4 ? 17 O1D ? I HEM . ? A HEM 396 ? 1_555 MN ? G MN . ? A MN 381 ? 1_555 O ? J HOH . ? A HOH 1040 ? 1_555 100.3 ? 18 OE2 ? A GLU 39 ? A GLU 39 ? 1_555 MN ? G MN . ? A MN 381 ? 1_555 O ? J HOH . ? A HOH 1040 ? 1_555 173.8 ? 19 O1D ? I HEM . ? A HEM 396 ? 1_555 MN ? G MN . ? A MN 381 ? 1_555 O ? J HOH . ? A HOH 1108 ? 1_555 85.5 ? 20 OE2 ? A GLU 39 ? A GLU 39 ? 1_555 MN ? G MN . ? A MN 381 ? 1_555 O ? J HOH . ? A HOH 1108 ? 1_555 93.7 ? 21 O ? J HOH . ? A HOH 1040 ? 1_555 MN ? G MN . ? A MN 381 ? 1_555 O ? J HOH . ? A HOH 1108 ? 1_555 89.1 ? 22 O1D ? I HEM . ? A HEM 396 ? 1_555 MN ? G MN . ? A MN 381 ? 1_555 OD2 ? A ASP 179 ? A ASP 179 ? 1_555 168.4 ? 23 OE2 ? A GLU 39 ? A GLU 39 ? 1_555 MN ? G MN . ? A MN 381 ? 1_555 OD2 ? A ASP 179 ? A ASP 179 ? 1_555 90.7 ? 24 O ? J HOH . ? A HOH 1040 ? 1_555 MN ? G MN . ? A MN 381 ? 1_555 OD2 ? A ASP 179 ? A ASP 179 ? 1_555 84.2 ? 25 O ? J HOH . ? A HOH 1108 ? 1_555 MN ? G MN . ? A MN 381 ? 1_555 OD2 ? A ASP 179 ? A ASP 179 ? 1_555 83.8 ? 26 O1D ? I HEM . ? A HEM 396 ? 1_555 MN ? G MN . ? A MN 381 ? 1_555 OE1 ? A GLU 35 ? A GLU 35 ? 1_555 95.6 ? 27 OE2 ? A GLU 39 ? A GLU 39 ? 1_555 MN ? G MN . ? A MN 381 ? 1_555 OE1 ? A GLU 35 ? A GLU 35 ? 1_555 89.9 ? 28 O ? J HOH . ? A HOH 1040 ? 1_555 MN ? G MN . ? A MN 381 ? 1_555 OE1 ? A GLU 35 ? A GLU 35 ? 1_555 87.3 ? 29 O ? J HOH . ? A HOH 1108 ? 1_555 MN ? G MN . ? A MN 381 ? 1_555 OE1 ? A GLU 35 ? A GLU 35 ? 1_555 176.3 ? 30 OD2 ? A ASP 179 ? A ASP 179 ? 1_555 MN ? G MN . ? A MN 381 ? 1_555 OE1 ? A GLU 35 ? A GLU 35 ? 1_555 95.3 ? 31 OD2 ? A ASP 47 ? A ASP 47 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 O ? J HOH . ? A HOH 1127 ? 1_555 174.9 ? 32 OD2 ? A ASP 47 ? A ASP 47 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 O ? J HOH . ? A HOH 1085 ? 1_555 91.9 ? 33 O ? J HOH . ? A HOH 1127 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 O ? J HOH . ? A HOH 1085 ? 1_555 86.3 ? 34 OD2 ? A ASP 47 ? A ASP 47 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 OD1 ? A ASP 64 ? A ASP 64 ? 1_555 83.9 ? 35 O ? J HOH . ? A HOH 1127 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 OD1 ? A ASP 64 ? A ASP 64 ? 1_555 95.4 ? 36 O ? J HOH . ? A HOH 1085 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 OD1 ? A ASP 64 ? A ASP 64 ? 1_555 150.8 ? 37 OD2 ? A ASP 47 ? A ASP 47 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 O ? A ASP 47 ? A ASP 47 ? 1_555 82.0 ? 38 O ? J HOH . ? A HOH 1127 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 O ? A ASP 47 ? A ASP 47 ? 1_555 102.0 ? 39 O ? J HOH . ? A HOH 1085 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 O ? A ASP 47 ? A ASP 47 ? 1_555 74.3 ? 40 OD1 ? A ASP 64 ? A ASP 64 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 O ? A ASP 47 ? A ASP 47 ? 1_555 133.0 ? 41 OD2 ? A ASP 47 ? A ASP 47 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 O ? A GLY 62 ? A GLY 62 ? 1_555 95.8 ? 42 O ? J HOH . ? A HOH 1127 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 O ? A GLY 62 ? A GLY 62 ? 1_555 88.6 ? 43 O ? J HOH . ? A HOH 1085 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 O ? A GLY 62 ? A GLY 62 ? 1_555 139.1 ? 44 OD1 ? A ASP 64 ? A ASP 64 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 O ? A GLY 62 ? A GLY 62 ? 1_555 70.0 ? 45 O ? A ASP 47 ? A ASP 47 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 O ? A GLY 62 ? A GLY 62 ? 1_555 67.2 ? 46 OD2 ? A ASP 47 ? A ASP 47 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 OG ? A SER 66 ? A SER 66 ? 1_555 90.0 ? 47 O ? J HOH . ? A HOH 1127 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 OG ? A SER 66 ? A SER 66 ? 1_555 85.0 ? 48 O ? J HOH . ? A HOH 1085 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 OG ? A SER 66 ? A SER 66 ? 1_555 75.0 ? 49 OD1 ? A ASP 64 ? A ASP 64 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 OG ? A SER 66 ? A SER 66 ? 1_555 76.1 ? 50 O ? A ASP 47 ? A ASP 47 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 OG ? A SER 66 ? A SER 66 ? 1_555 147.9 ? 51 O ? A GLY 62 ? A GLY 62 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 OG ? A SER 66 ? A SER 66 ? 1_555 144.7 ? 52 O ? A SER 174 ? A SER 174 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 O ? A THR 193 ? A THR 193 ? 1_555 80.9 ? 53 O ? A SER 174 ? A SER 174 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OD2 ? A ASP 191 ? A ASP 191 ? 1_555 92.9 ? 54 O ? A THR 193 ? A THR 193 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OD2 ? A ASP 191 ? A ASP 191 ? 1_555 127.4 ? 55 O ? A SER 174 ? A SER 174 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OD1 ? A ASP 198 ? A ASP 198 ? 1_555 142.9 ? 56 O ? A THR 193 ? A THR 193 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OD1 ? A ASP 198 ? A ASP 198 ? 1_555 126.4 ? 57 OD2 ? A ASP 191 ? A ASP 191 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OD1 ? A ASP 198 ? A ASP 198 ? 1_555 88.2 ? 58 O ? A SER 174 ? A SER 174 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OG ? A SER 174 ? A SER 174 ? 1_555 73.3 ? 59 O ? A THR 193 ? A THR 193 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OG ? A SER 174 ? A SER 174 ? 1_555 144.8 ? 60 OD2 ? A ASP 191 ? A ASP 191 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OG ? A SER 174 ? A SER 174 ? 1_555 78.3 ? 61 OD1 ? A ASP 198 ? A ASP 198 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OG ? A SER 174 ? A SER 174 ? 1_555 70.7 ? 62 O ? A SER 174 ? A SER 174 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OG1 ? A THR 193 ? A THR 193 ? 1_555 145.6 ? 63 O ? A THR 193 ? A THR 193 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OG1 ? A THR 193 ? A THR 193 ? 1_555 69.4 ? 64 OD2 ? A ASP 191 ? A ASP 191 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OG1 ? A THR 193 ? A THR 193 ? 1_555 91.7 ? 65 OD1 ? A ASP 198 ? A ASP 198 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OG1 ? A THR 193 ? A THR 193 ? 1_555 71.2 ? 66 OG ? A SER 174 ? A SER 174 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OG1 ? A THR 193 ? A THR 193 ? 1_555 140.8 ? 67 O ? A SER 174 ? A SER 174 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 O ? A THR 196 ? A THR 196 ? 1_555 84.3 ? 68 O ? A THR 193 ? A THR 193 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 O ? A THR 196 ? A THR 196 ? 1_555 76.6 ? 69 OD2 ? A ASP 191 ? A ASP 191 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 O ? A THR 196 ? A THR 196 ? 1_555 155.2 ? 70 OD1 ? A ASP 198 ? A ASP 198 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 O ? A THR 196 ? A THR 196 ? 1_555 79.6 ? 71 OG ? A SER 174 ? A SER 174 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 O ? A THR 196 ? A THR 196 ? 1_555 77.3 ? 72 OG1 ? A THR 193 ? A THR 193 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 O ? A THR 196 ? A THR 196 ? 1_555 104.5 ? 73 O ? A SER 174 ? A SER 174 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OD1 ? A ASP 191 ? A ASP 191 ? 1_555 78.6 ? 74 O ? A THR 193 ? A THR 193 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OD1 ? A ASP 191 ? A ASP 191 ? 1_555 76.3 ? 75 OD2 ? A ASP 191 ? A ASP 191 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OD1 ? A ASP 191 ? A ASP 191 ? 1_555 51.4 ? 76 OD1 ? A ASP 198 ? A ASP 198 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OD1 ? A ASP 191 ? A ASP 191 ? 1_555 127.9 ? 77 OG ? A SER 174 ? A SER 174 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OD1 ? A ASP 191 ? A ASP 191 ? 1_555 120.0 ? 78 OG1 ? A THR 193 ? A THR 193 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OD1 ? A ASP 191 ? A ASP 191 ? 1_555 77.9 ? 79 O ? A THR 196 ? A THR 196 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OD1 ? A ASP 191 ? A ASP 191 ? 1_555 149.9 ? # 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 2010-04-14 2 'Structure model' 1 1 2011-07-13 3 'Structure model' 1 2 2017-11-08 # _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' 'Refinement description' # _pdbx_audit_revision_category.ordinal 1 _pdbx_audit_revision_category.revision_ordinal 3 _pdbx_audit_revision_category.data_content_type 'Structure model' _pdbx_audit_revision_category.category software # _pdbx_audit_revision_item.ordinal 1 _pdbx_audit_revision_item.revision_ordinal 3 _pdbx_audit_revision_item.data_content_type 'Structure model' _pdbx_audit_revision_item.item '_software.name' # loop_ _software.pdbx_ordinal _software.name _software.version _software.date _software.type _software.contact_author _software.contact_author_email _software.classification _software.location _software.language _software.citation_id 1 SHELX . ? package 'George M. Sheldrick' gsheldr@shelx.uni-ac.gwdg.de refinement http://shelx.uni-ac.gwdg.de/SHELX/ Fortran_77 ? 2 PDB_EXTRACT 3.100 'Jan. 22, 2010' package PDB help@deposit.rcsb.org 'data extraction' http://sw-tools.pdb.org/apps/PDB_EXTRACT/ C++ ? 3 MAR345dtb . ? ? ? ? 'data collection' ? ? ? 4 DENZO . ? ? ? ? 'data reduction' ? ? ? 5 SCALEPACK . ? ? ? ? 'data scaling' ? ? ? 6 SHELXL-97 . ? ? ? ? phasing ? ? ? 7 SHELXL-97 . ? ? ? ? refinement ? ? ? # _pdbx_validate_rmsd_bond.id 1 _pdbx_validate_rmsd_bond.PDB_model_num 1 _pdbx_validate_rmsd_bond.auth_atom_id_1 CD _pdbx_validate_rmsd_bond.auth_asym_id_1 A _pdbx_validate_rmsd_bond.auth_comp_id_1 GLU _pdbx_validate_rmsd_bond.auth_seq_id_1 39 _pdbx_validate_rmsd_bond.PDB_ins_code_1 ? _pdbx_validate_rmsd_bond.label_alt_id_1 ? _pdbx_validate_rmsd_bond.auth_atom_id_2 OE1 _pdbx_validate_rmsd_bond.auth_asym_id_2 A _pdbx_validate_rmsd_bond.auth_comp_id_2 GLU _pdbx_validate_rmsd_bond.auth_seq_id_2 39 _pdbx_validate_rmsd_bond.PDB_ins_code_2 ? _pdbx_validate_rmsd_bond.label_alt_id_2 ? _pdbx_validate_rmsd_bond.bond_value 1.374 _pdbx_validate_rmsd_bond.bond_target_value 1.252 _pdbx_validate_rmsd_bond.bond_deviation 0.122 _pdbx_validate_rmsd_bond.bond_standard_deviation 0.011 _pdbx_validate_rmsd_bond.linker_flag N # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 CB A CYS 3 ? A CA A CYS 3 ? ? C A CYS 3 ? ? 120.19 111.50 8.69 1.20 N 2 1 CB A CYS 3 ? B CA A CYS 3 ? ? C A CYS 3 ? ? 96.72 110.40 -13.68 2.00 N 3 1 C A ASP 5 ? ? N A GLY 6 ? ? CA A GLY 6 ? ? 145.07 122.30 22.77 2.10 Y 4 1 NE A ARG 8 ? ? CZ A ARG 8 ? ? NH2 A ARG 8 ? ? 116.21 120.30 -4.09 0.50 N 5 1 CA A CYS 14 ? ? CB A CYS 14 ? B SG A CYS 14 ? B 128.52 114.20 14.32 1.10 N 6 1 OE1 A GLU 39 ? ? CD A GLU 39 ? ? OE2 A GLU 39 ? ? 110.34 123.30 -12.96 1.20 N 7 1 NE A ARG 42 ? B CZ A ARG 42 ? B NH1 A ARG 42 ? B 125.04 120.30 4.74 0.50 N 8 1 NE A ARG 42 ? B CZ A ARG 42 ? B NH2 A ARG 42 ? B 115.06 120.30 -5.24 0.50 N 9 1 NE A ARG 53 ? ? CZ A ARG 53 ? ? NH1 A ARG 53 ? ? 116.78 120.30 -3.52 0.50 N 10 1 CB A ASP 84 ? ? CG A ASP 84 ? ? OD2 A ASP 84 ? ? 125.08 118.30 6.78 0.90 N 11 1 CB A ASP 85 ? ? CG A ASP 85 ? ? OD1 A ASP 85 ? ? 124.88 118.30 6.58 0.90 N 12 1 CB A ASP 182 ? B CG A ASP 182 ? B OD1 A ASP 182 ? B 126.28 118.30 7.98 0.90 N 13 1 CD A ARG 270 ? ? NE A ARG 270 ? ? CZ A ARG 270 ? ? 132.03 123.60 8.43 1.40 N 14 1 NE A ARG 283 ? ? CZ A ARG 283 ? ? NH2 A ARG 283 ? ? 125.12 120.30 4.82 0.50 N 15 1 CB A ARG 323 ? ? CG A ARG 323 ? ? CD A ARG 323 ? ? 144.55 111.60 32.95 2.60 N 16 1 NE A ARG 323 ? ? CZ A ARG 323 ? ? NH2 A ARG 323 ? ? 125.44 120.30 5.14 0.50 N 17 1 O A SER 345 ? ? C A SER 345 ? ? N A MET 346 ? ? 133.28 122.70 10.58 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 CYS A 33 ? ? -90.16 54.11 2 1 VAL A 73 ? ? -96.32 -89.54 3 1 SER A 309 ? ? 90.85 -2.03 4 1 SER A 318 ? ? -140.82 10.28 5 1 CYS A 348 ? ? -166.66 63.50 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 ALPHA-D-MANNOSE MAN 4 'CALCIUM ION' CA 5 'MANGANESE (II) ION' MN 6 GLYCEROL GOL 7 'PROTOPORPHYRIN IX CONTAINING FE' HEM 8 water HOH #