From 2bdd550c67324666e6948b3a2daa2a7f45e1cafa Mon Sep 17 00:00:00 2001 From: Navan Chauhan Date: Fri, 13 Mar 2020 19:05:29 +0530 Subject: Added ligands, targets and results --- Docking/Target/6y84.cif | 7803 +++++++++++++++++++++++++++++++++++++++++++++++ 1 file changed, 7803 insertions(+) create mode 100755 Docking/Target/6y84.cif (limited to 'Docking/Target/6y84.cif') diff --git a/Docking/Target/6y84.cif b/Docking/Target/6y84.cif new file mode 100755 index 0000000..3b8aa38 --- /dev/null +++ b/Docking/Target/6y84.cif @@ -0,0 +1,7803 @@ +data_6Y84 +# +_entry.id 6Y84 +# +_audit_conform.dict_name mmcif_pdbx.dic +_audit_conform.dict_version 5.322 +_audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic +# +loop_ +_database_2.database_id +_database_2.database_code +PDB 6Y84 +WWPDB D_1292107053 +# +_pdbx_database_status.status_code REL +_pdbx_database_status.status_code_sf REL +_pdbx_database_status.status_code_mr ? +_pdbx_database_status.entry_id 6Y84 +_pdbx_database_status.recvd_initial_deposition_date 2020-03-03 +_pdbx_database_status.SG_entry N +_pdbx_database_status.deposit_site PDBE +_pdbx_database_status.process_site PDBE +_pdbx_database_status.status_code_cs ? +_pdbx_database_status.methods_development_category ? +_pdbx_database_status.pdb_format_compatible Y +# +loop_ +_audit_author.name +_audit_author.pdbx_ordinal +_audit_author.identifier_ORCID +'Owen, C.D.' 1 ? +'Lukacik, P.' 2 ? +'Strain-Damerell, C.M.' 3 ? +'Douangamath, A.' 4 ? +'Powell, A.J.' 5 ? +'Fearon, D.' 6 ? +'Brandao-Neto, J.' 7 ? +'Crawshaw, A.D.' 8 ? +'Aragao, D.' 9 ? +'Williams, M.' 10 ? +'Flaig, R.' 11 ? +'Hall, D.' 12 ? +'McAauley, K.' 13 ? +'Stuart, D.I.' 14 ? +'von Delft, F.' 15 ? +'Walsh, M.A.' 16 ? +# +_citation.abstract ? +_citation.abstract_id_CAS ? +_citation.book_id_ISBN ? +_citation.book_publisher ? +_citation.book_publisher_city ? +_citation.book_title ? +_citation.coordinate_linkage ? +_citation.country ? +_citation.database_id_Medline ? +_citation.details ? +_citation.id primary +_citation.journal_abbrev 'To Be Published' +_citation.journal_id_ASTM ? +_citation.journal_id_CSD 0353 +_citation.journal_id_ISSN ? +_citation.journal_full ? +_citation.journal_issue ? +_citation.journal_volume ? +_citation.language ? +_citation.page_first ? +_citation.page_last ? +_citation.title 'COVID-19 main protease with unliganded active site' +_citation.year ? +_citation.database_id_CSD ? +_citation.pdbx_database_id_DOI ? +_citation.pdbx_database_id_PubMed ? +_citation.unpublished_flag ? +# +loop_ +_citation_author.citation_id +_citation_author.name +_citation_author.ordinal +_citation_author.identifier_ORCID +primary 'Owen, C.D.' 1 ? +primary 'Lukacik, P.' 2 ? +primary 'Strain-Damerell, C.M.' 3 ? +primary 'Douangamath, A.' 4 ? +primary 'Powell, A.J.' 5 ? +primary 'Fearon, D.' 6 ? +primary 'Brandao-Neto, J.' 7 ? +primary 'Crawshaw, A.D.' 8 ? +primary 'Aragao, D.' 9 ? +primary 'Williams, M.' 10 ? +primary 'Flaig, R.' 11 ? +primary 'Hall, D.' 12 ? +primary 'McAauley, K.' 13 ? +primary 'Stuart, D.I.' 14 ? +primary 'von Delft, F.' 15 ? +primary 'Walsh, M.A.' 16 ? +# +_cell.angle_alpha 90.000 +_cell.angle_alpha_esd ? +_cell.angle_beta 103.160 +_cell.angle_beta_esd ? +_cell.angle_gamma 90.000 +_cell.angle_gamma_esd ? +_cell.entry_id 6Y84 +_cell.details ? +_cell.formula_units_Z ? +_cell.length_a 112.812 +_cell.length_a_esd ? +_cell.length_b 52.949 +_cell.length_b_esd ? +_cell.length_c 44.631 +_cell.length_c_esd ? +_cell.volume ? +_cell.volume_esd ? +_cell.Z_PDB 4 +_cell.reciprocal_angle_alpha ? +_cell.reciprocal_angle_beta ? +_cell.reciprocal_angle_gamma ? +_cell.reciprocal_angle_alpha_esd ? +_cell.reciprocal_angle_beta_esd ? +_cell.reciprocal_angle_gamma_esd ? +_cell.reciprocal_length_a ? +_cell.reciprocal_length_b ? +_cell.reciprocal_length_c ? +_cell.reciprocal_length_a_esd ? +_cell.reciprocal_length_b_esd ? +_cell.reciprocal_length_c_esd ? +_cell.pdbx_unique_axis ? +# +_symmetry.entry_id 6Y84 +_symmetry.cell_setting ? +_symmetry.Int_Tables_number 5 +_symmetry.space_group_name_Hall ? +_symmetry.space_group_name_H-M 'C 1 2 1' +_symmetry.pdbx_full_space_group_name_H-M ? +# +loop_ +_entity.id +_entity.type +_entity.src_method +_entity.pdbx_description +_entity.formula_weight +_entity.pdbx_number_of_molecules +_entity.pdbx_ec +_entity.pdbx_mutation +_entity.pdbx_fragment +_entity.details +1 polymer man 'Non-structural polyprotein 1ab' 33825.547 1 ? ? ? ? +2 non-polymer syn 'DIMETHYL SULFOXIDE' 78.133 4 ? ? ? ? +3 water nat water 18.015 391 ? ? ? ? +# +_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 +;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH +SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC +YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE +PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ +; +_entity_poly.pdbx_seq_one_letter_code_can +;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH +SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC +YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE +PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ +; +_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 SER n +1 2 GLY n +1 3 PHE n +1 4 ARG n +1 5 LYS n +1 6 MET n +1 7 ALA n +1 8 PHE n +1 9 PRO n +1 10 SER n +1 11 GLY n +1 12 LYS n +1 13 VAL n +1 14 GLU n +1 15 GLY n +1 16 CYS n +1 17 MET n +1 18 VAL n +1 19 GLN n +1 20 VAL n +1 21 THR n +1 22 CYS n +1 23 GLY n +1 24 THR n +1 25 THR n +1 26 THR n +1 27 LEU n +1 28 ASN n +1 29 GLY n +1 30 LEU n +1 31 TRP n +1 32 LEU n +1 33 ASP n +1 34 ASP n +1 35 VAL n +1 36 VAL n +1 37 TYR n +1 38 CYS n +1 39 PRO n +1 40 ARG n +1 41 HIS n +1 42 VAL n +1 43 ILE n +1 44 CYS n +1 45 THR n +1 46 SER n +1 47 GLU n +1 48 ASP n +1 49 MET n +1 50 LEU n +1 51 ASN n +1 52 PRO n +1 53 ASN n +1 54 TYR n +1 55 GLU n +1 56 ASP n +1 57 LEU n +1 58 LEU n +1 59 ILE n +1 60 ARG n +1 61 LYS n +1 62 SER n +1 63 ASN n +1 64 HIS n +1 65 ASN n +1 66 PHE n +1 67 LEU n +1 68 VAL n +1 69 GLN n +1 70 ALA n +1 71 GLY n +1 72 ASN n +1 73 VAL n +1 74 GLN n +1 75 LEU n +1 76 ARG n +1 77 VAL n +1 78 ILE n +1 79 GLY n +1 80 HIS n +1 81 SER n +1 82 MET n +1 83 GLN n +1 84 ASN n +1 85 CYS n +1 86 VAL n +1 87 LEU n +1 88 LYS n +1 89 LEU n +1 90 LYS n +1 91 VAL n +1 92 ASP n +1 93 THR n +1 94 ALA n +1 95 ASN n +1 96 PRO n +1 97 LYS n +1 98 THR n +1 99 PRO n +1 100 LYS n +1 101 TYR n +1 102 LYS n +1 103 PHE n +1 104 VAL n +1 105 ARG n +1 106 ILE n +1 107 GLN n +1 108 PRO n +1 109 GLY n +1 110 GLN n +1 111 THR n +1 112 PHE n +1 113 SER n +1 114 VAL n +1 115 LEU n +1 116 ALA n +1 117 CYS n +1 118 TYR n +1 119 ASN n +1 120 GLY n +1 121 SER n +1 122 PRO n +1 123 SER n +1 124 GLY n +1 125 VAL n +1 126 TYR n +1 127 GLN n +1 128 CYS n +1 129 ALA n +1 130 MET n +1 131 ARG n +1 132 PRO n +1 133 ASN n +1 134 PHE n +1 135 THR n +1 136 ILE n +1 137 LYS n +1 138 GLY n +1 139 SER n +1 140 PHE n +1 141 LEU n +1 142 ASN n +1 143 GLY n +1 144 SER n +1 145 CYS n +1 146 GLY n +1 147 SER n +1 148 VAL n +1 149 GLY n +1 150 PHE n +1 151 ASN n +1 152 ILE n +1 153 ASP n +1 154 TYR n +1 155 ASP n +1 156 CYS n +1 157 VAL n +1 158 SER n +1 159 PHE n +1 160 CYS n +1 161 TYR n +1 162 MET n +1 163 HIS n +1 164 HIS n +1 165 MET n +1 166 GLU n +1 167 LEU n +1 168 PRO n +1 169 THR n +1 170 GLY n +1 171 VAL n +1 172 HIS n +1 173 ALA n +1 174 GLY n +1 175 THR n +1 176 ASP n +1 177 LEU n +1 178 GLU n +1 179 GLY n +1 180 ASN n +1 181 PHE n +1 182 TYR n +1 183 GLY n +1 184 PRO n +1 185 PHE n +1 186 VAL n +1 187 ASP n +1 188 ARG n +1 189 GLN n +1 190 THR n +1 191 ALA n +1 192 GLN n +1 193 ALA n +1 194 ALA n +1 195 GLY n +1 196 THR n +1 197 ASP n +1 198 THR n +1 199 THR n +1 200 ILE n +1 201 THR n +1 202 VAL n +1 203 ASN n +1 204 VAL n +1 205 LEU n +1 206 ALA n +1 207 TRP n +1 208 LEU n +1 209 TYR n +1 210 ALA n +1 211 ALA n +1 212 VAL n +1 213 ILE n +1 214 ASN n +1 215 GLY n +1 216 ASP n +1 217 ARG n +1 218 TRP n +1 219 PHE n +1 220 LEU n +1 221 ASN n +1 222 ARG n +1 223 PHE n +1 224 THR n +1 225 THR n +1 226 THR n +1 227 LEU n +1 228 ASN n +1 229 ASP n +1 230 PHE n +1 231 ASN n +1 232 LEU n +1 233 VAL n +1 234 ALA n +1 235 MET n +1 236 LYS n +1 237 TYR n +1 238 ASN n +1 239 TYR n +1 240 GLU n +1 241 PRO n +1 242 LEU n +1 243 THR n +1 244 GLN n +1 245 ASP n +1 246 HIS n +1 247 VAL n +1 248 ASP n +1 249 ILE n +1 250 LEU n +1 251 GLY n +1 252 PRO n +1 253 LEU n +1 254 SER n +1 255 ALA n +1 256 GLN n +1 257 THR n +1 258 GLY n +1 259 ILE n +1 260 ALA n +1 261 VAL n +1 262 LEU n +1 263 ASP n +1 264 MET n +1 265 CYS n +1 266 ALA n +1 267 SER n +1 268 LEU n +1 269 LYS n +1 270 GLU n +1 271 LEU n +1 272 LEU n +1 273 GLN n +1 274 ASN n +1 275 GLY n +1 276 MET n +1 277 ASN n +1 278 GLY n +1 279 ARG n +1 280 THR n +1 281 ILE n +1 282 LEU n +1 283 GLY n +1 284 SER n +1 285 ALA n +1 286 LEU n +1 287 LEU n +1 288 GLU n +1 289 ASP n +1 290 GLU n +1 291 PHE n +1 292 THR n +1 293 PRO n +1 294 PHE n +1 295 ASP n +1 296 VAL n +1 297 VAL n +1 298 ARG n +1 299 GLN n +1 300 CYS n +1 301 SER n +1 302 GLY n +1 303 VAL n +1 304 THR n +1 305 PHE n +1 306 GLN n +# +_entity_src_gen.entity_id 1 +_entity_src_gen.pdbx_src_id 1 +_entity_src_gen.pdbx_alt_source_flag sample +_entity_src_gen.pdbx_seq_type 'Biological sequence' +_entity_src_gen.pdbx_beg_seq_num 1 +_entity_src_gen.pdbx_end_seq_num 306 +_entity_src_gen.gene_src_common_name ? +_entity_src_gen.gene_src_genus ? +_entity_src_gen.pdbx_gene_src_gene ? +_entity_src_gen.gene_src_species ? +_entity_src_gen.gene_src_strain COVID-19 +_entity_src_gen.gene_src_tissue ? +_entity_src_gen.gene_src_tissue_fraction ? +_entity_src_gen.gene_src_details ? +_entity_src_gen.pdbx_gene_src_fragment ? +_entity_src_gen.pdbx_gene_src_scientific_name 'Severe acute respiratory syndrome coronavirus 2' +_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 2697049 +_entity_src_gen.pdbx_gene_src_variant ? +_entity_src_gen.pdbx_gene_src_cell_line ? +_entity_src_gen.pdbx_gene_src_atcc ? +_entity_src_gen.pdbx_gene_src_organ ? +_entity_src_gen.pdbx_gene_src_organelle ? +_entity_src_gen.pdbx_gene_src_cell ? +_entity_src_gen.pdbx_gene_src_cellular_location ? +_entity_src_gen.host_org_common_name ? +_entity_src_gen.pdbx_host_org_scientific_name 'Escherichia coli' +_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 562 +_entity_src_gen.host_org_genus ? +_entity_src_gen.pdbx_host_org_gene ? +_entity_src_gen.pdbx_host_org_organ ? +_entity_src_gen.host_org_species ? +_entity_src_gen.pdbx_host_org_tissue ? +_entity_src_gen.pdbx_host_org_tissue_fraction ? +_entity_src_gen.pdbx_host_org_strain ? +_entity_src_gen.pdbx_host_org_variant ? +_entity_src_gen.pdbx_host_org_cell_line ? +_entity_src_gen.pdbx_host_org_atcc ? +_entity_src_gen.pdbx_host_org_culture_collection ? +_entity_src_gen.pdbx_host_org_cell ? +_entity_src_gen.pdbx_host_org_organelle ? +_entity_src_gen.pdbx_host_org_cellular_location ? +_entity_src_gen.pdbx_host_org_vector_type ? +_entity_src_gen.pdbx_host_org_vector ? +_entity_src_gen.host_org_details ? +_entity_src_gen.expression_system_id ? +_entity_src_gen.plasmid_name ? +_entity_src_gen.plasmid_details ? +_entity_src_gen.pdbx_description ? +# +_struct_ref.id 1 +_struct_ref.db_name PDB +_struct_ref.db_code 6Y84 +_struct_ref.pdbx_db_accession 6Y84 +_struct_ref.pdbx_db_isoform ? +_struct_ref.entity_id 1 +_struct_ref.pdbx_seq_one_letter_code ? +_struct_ref.pdbx_align_begin 1 +# +_struct_ref_seq.align_id 1 +_struct_ref_seq.ref_id 1 +_struct_ref_seq.pdbx_PDB_id_code 6Y84 +_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 306 +_struct_ref_seq.pdbx_seq_align_end_ins_code ? +_struct_ref_seq.pdbx_db_accession 6Y84 +_struct_ref_seq.db_align_beg 1 +_struct_ref_seq.pdbx_db_align_beg_ins_code ? +_struct_ref_seq.db_align_end 306 +_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 306 +# +loop_ +_chem_comp.id +_chem_comp.type +_chem_comp.mon_nstd_flag +_chem_comp.name +_chem_comp.pdbx_synonyms +_chem_comp.formula +_chem_comp.formula_weight +ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 +ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 +ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 +ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 +CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 +DMS non-polymer . 'DIMETHYL SULFOXIDE' ? 'C2 H6 O S' 78.133 +GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 +GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 +GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 +HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 +HOH non-polymer . WATER ? 'H2 O' 18.015 +ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 +LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 +LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 +MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 +PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 +PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 +SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 +THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 +TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 +TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 +VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 +# +_exptl.absorpt_coefficient_mu ? +_exptl.absorpt_correction_T_max ? +_exptl.absorpt_correction_T_min ? +_exptl.absorpt_correction_type ? +_exptl.absorpt_process_details ? +_exptl.entry_id 6Y84 +_exptl.crystals_number 1 +_exptl.details ? +_exptl.method 'X-RAY DIFFRACTION' +_exptl.method_details ? +# +_exptl_crystal.colour ? +_exptl_crystal.density_diffrn ? +_exptl_crystal.density_Matthews 1.92 +_exptl_crystal.density_method ? +_exptl_crystal.density_percent_sol 35.89 +_exptl_crystal.description ? +_exptl_crystal.F_000 ? +_exptl_crystal.id 1 +_exptl_crystal.preparation ? +_exptl_crystal.size_max ? +_exptl_crystal.size_mid ? +_exptl_crystal.size_min ? +_exptl_crystal.size_rad ? +_exptl_crystal.colour_lustre ? +_exptl_crystal.colour_modifier ? +_exptl_crystal.colour_primary ? +_exptl_crystal.density_meas ? +_exptl_crystal.density_meas_esd ? +_exptl_crystal.density_meas_gt ? +_exptl_crystal.density_meas_lt ? +_exptl_crystal.density_meas_temp ? +_exptl_crystal.density_meas_temp_esd ? +_exptl_crystal.density_meas_temp_gt ? +_exptl_crystal.density_meas_temp_lt ? +_exptl_crystal.pdbx_crystal_image_url ? +_exptl_crystal.pdbx_crystal_image_format ? +_exptl_crystal.pdbx_mosaicity ? +_exptl_crystal.pdbx_mosaicity_esd ? +# +_exptl_crystal_grow.apparatus ? +_exptl_crystal_grow.atmosphere ? +_exptl_crystal_grow.crystal_id 1 +_exptl_crystal_grow.details ? +_exptl_crystal_grow.method 'VAPOR DIFFUSION, SITTING DROP' +_exptl_crystal_grow.method_ref ? +_exptl_crystal_grow.pH 6.5 +_exptl_crystal_grow.pressure ? +_exptl_crystal_grow.pressure_esd ? +_exptl_crystal_grow.seeding ? +_exptl_crystal_grow.seeding_ref ? +_exptl_crystal_grow.temp 293 +_exptl_crystal_grow.temp_details ? +_exptl_crystal_grow.temp_esd ? +_exptl_crystal_grow.time ? +_exptl_crystal_grow.pdbx_details +;15% PEG 4000, 5% DMSO, 0.1M MES pH 6.5. +0.15 microlitre protein + 0.3 microlitre reservoir + 0.05 microlitre seed stock +; +_exptl_crystal_grow.pdbx_pH_range ? +# +_diffrn.ambient_environment ? +_diffrn.ambient_temp 100 +_diffrn.ambient_temp_details ? +_diffrn.ambient_temp_esd ? +_diffrn.crystal_id 1 +_diffrn.crystal_support ? +_diffrn.crystal_treatment ? +_diffrn.details ? +_diffrn.id 1 +_diffrn.ambient_pressure ? +_diffrn.ambient_pressure_esd ? +_diffrn.ambient_pressure_gt ? +_diffrn.ambient_pressure_lt ? +_diffrn.ambient_temp_gt ? +_diffrn.ambient_temp_lt ? +_diffrn.pdbx_serial_crystal_experiment N +# +_diffrn_detector.details ? +_diffrn_detector.detector PIXEL +_diffrn_detector.diffrn_id 1 +_diffrn_detector.type 'DECTRIS PILATUS3 6M' +_diffrn_detector.area_resol_mean ? +_diffrn_detector.dtime ? +_diffrn_detector.pdbx_frames_total ? +_diffrn_detector.pdbx_collection_time_total ? +_diffrn_detector.pdbx_collection_date 2020-02-24 +_diffrn_detector.pdbx_frequency ? +# +_diffrn_radiation.collimation ? +_diffrn_radiation.diffrn_id 1 +_diffrn_radiation.filter_edge ? +_diffrn_radiation.inhomogeneity ? +_diffrn_radiation.monochromator ? +_diffrn_radiation.polarisn_norm ? +_diffrn_radiation.polarisn_ratio ? +_diffrn_radiation.probe ? +_diffrn_radiation.type ? +_diffrn_radiation.xray_symbol ? +_diffrn_radiation.wavelength_id 1 +_diffrn_radiation.pdbx_monochromatic_or_laue_m_l M +_diffrn_radiation.pdbx_wavelength_list ? +_diffrn_radiation.pdbx_wavelength ? +_diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' +_diffrn_radiation.pdbx_analyzer ? +_diffrn_radiation.pdbx_scattering_type x-ray +# +_diffrn_radiation_wavelength.id 1 +_diffrn_radiation_wavelength.wavelength 0.9126 +_diffrn_radiation_wavelength.wt 1.0 +# +_diffrn_source.current ? +_diffrn_source.details ? +_diffrn_source.diffrn_id 1 +_diffrn_source.power ? +_diffrn_source.size ? +_diffrn_source.source SYNCHROTRON +_diffrn_source.target ? +_diffrn_source.type 'DIAMOND BEAMLINE I04-1' +_diffrn_source.voltage ? +_diffrn_source.take-off_angle ? +_diffrn_source.pdbx_wavelength_list 0.9126 +_diffrn_source.pdbx_wavelength ? +_diffrn_source.pdbx_synchrotron_beamline I04-1 +_diffrn_source.pdbx_synchrotron_site Diamond +# +_reflns.B_iso_Wilson_estimate 17.330 +_reflns.entry_id 6Y84 +_reflns.data_reduction_details ? +_reflns.data_reduction_method ? +_reflns.d_resolution_high 1.390 +_reflns.d_resolution_low 54.930 +_reflns.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.number_all ? +_reflns.number_obs 50348 +_reflns.observed_criterion ? +_reflns.observed_criterion_F_max ? +_reflns.observed_criterion_F_min ? +_reflns.observed_criterion_I_max ? +_reflns.observed_criterion_I_min ? +_reflns.observed_criterion_sigma_F ? +_reflns.observed_criterion_sigma_I ? +_reflns.percent_possible_obs 97.500 +_reflns.R_free_details ? +_reflns.Rmerge_F_all ? +_reflns.Rmerge_F_obs ? +_reflns.Friedel_coverage ? +_reflns.number_gt ? +_reflns.threshold_expression ? +_reflns.pdbx_redundancy 3.600 +_reflns.pdbx_Rmerge_I_obs 0.059 +_reflns.pdbx_Rmerge_I_all ? +_reflns.pdbx_Rsym_value ? +_reflns.pdbx_netI_over_av_sigmaI ? +_reflns.pdbx_netI_over_sigmaI 9.700 +_reflns.pdbx_res_netI_over_av_sigmaI_2 ? +_reflns.pdbx_res_netI_over_sigmaI_2 ? +_reflns.pdbx_chi_squared ? +_reflns.pdbx_scaling_rejects 602 +_reflns.pdbx_d_res_high_opt ? +_reflns.pdbx_d_res_low_opt ? +_reflns.pdbx_d_res_opt_method ? +_reflns.phase_calculation_details ? +_reflns.pdbx_Rrim_I_all 0.069 +_reflns.pdbx_Rpim_I_all 0.034 +_reflns.pdbx_d_opt ? +_reflns.pdbx_number_measured_all 179937 +_reflns.pdbx_diffrn_id 1 +_reflns.pdbx_ordinal 1 +_reflns.pdbx_CC_half 0.997 +_reflns.pdbx_CC_star ? +_reflns.pdbx_R_split ? +# +loop_ +_reflns_shell.d_res_high +_reflns_shell.d_res_low +_reflns_shell.meanI_over_sigI_all +_reflns_shell.meanI_over_sigI_obs +_reflns_shell.number_measured_all +_reflns_shell.number_measured_obs +_reflns_shell.number_possible +_reflns_shell.number_unique_all +_reflns_shell.number_unique_obs +_reflns_shell.percent_possible_all +_reflns_shell.percent_possible_obs +_reflns_shell.Rmerge_F_all +_reflns_shell.Rmerge_F_obs +_reflns_shell.Rmerge_I_all +_reflns_shell.Rmerge_I_obs +_reflns_shell.meanI_over_sigI_gt +_reflns_shell.meanI_over_uI_all +_reflns_shell.meanI_over_uI_gt +_reflns_shell.number_measured_gt +_reflns_shell.number_unique_gt +_reflns_shell.percent_possible_gt +_reflns_shell.Rmerge_F_gt +_reflns_shell.Rmerge_I_gt +_reflns_shell.pdbx_redundancy +_reflns_shell.pdbx_Rsym_value +_reflns_shell.pdbx_chi_squared +_reflns_shell.pdbx_netI_over_sigmaI_all +_reflns_shell.pdbx_netI_over_sigmaI_obs +_reflns_shell.pdbx_Rrim_I_all +_reflns_shell.pdbx_Rpim_I_all +_reflns_shell.pdbx_rejects +_reflns_shell.pdbx_ordinal +_reflns_shell.pdbx_diffrn_id +_reflns_shell.pdbx_CC_half +_reflns_shell.pdbx_CC_star +_reflns_shell.pdbx_R_split +1.390 1.410 ? ? 4394 ? ? ? 2074 80.700 ? ? ? ? 0.929 ? ? ? ? ? ? ? ? 2.100 ? ? ? 0.800 1.141 0.650 ? 1 1 0.481 ? ? +7.610 54.930 ? ? 1425 ? ? ? 339 99.800 ? ? ? ? 0.022 ? ? ? ? ? ? ? ? 4.200 ? ? ? 32.500 0.025 0.012 ? 2 1 0.999 ? ? +# +_refine.aniso_B[1][1] -3.7809 +_refine.aniso_B[1][2] 0.0000 +_refine.aniso_B[1][3] 0.0422 +_refine.aniso_B[2][2] 0.6978 +_refine.aniso_B[2][3] 0.0000 +_refine.aniso_B[3][3] 3.0831 +_refine.B_iso_max 97.940 +_refine.B_iso_mean 21.0000 +_refine.B_iso_min 10.280 +_refine.correlation_coeff_Fo_to_Fc 0.9630 +_refine.correlation_coeff_Fo_to_Fc_free 0.9560 +_refine.details ? +_refine.diff_density_max ? +_refine.diff_density_max_esd ? +_refine.diff_density_min ? +_refine.diff_density_min_esd ? +_refine.diff_density_rms ? +_refine.diff_density_rms_esd ? +_refine.entry_id 6Y84 +_refine.pdbx_refine_id 'X-RAY DIFFRACTION' +_refine.ls_abs_structure_details ? +_refine.ls_abs_structure_Flack ? +_refine.ls_abs_structure_Flack_esd ? +_refine.ls_abs_structure_Rogers ? +_refine.ls_abs_structure_Rogers_esd ? +_refine.ls_d_res_high 1.3900 +_refine.ls_d_res_low 54.9300 +_refine.ls_extinction_coef ? +_refine.ls_extinction_coef_esd ? +_refine.ls_extinction_expression ? +_refine.ls_extinction_method ? +_refine.ls_goodness_of_fit_all ? +_refine.ls_goodness_of_fit_all_esd ? +_refine.ls_goodness_of_fit_obs ? +_refine.ls_goodness_of_fit_obs_esd ? +_refine.ls_hydrogen_treatment ? +_refine.ls_matrix_type ? +_refine.ls_number_constraints ? +_refine.ls_number_parameters ? +_refine.ls_number_reflns_all ? +_refine.ls_number_reflns_obs 50331 +_refine.ls_number_reflns_R_free 2498 +_refine.ls_number_reflns_R_work ? +_refine.ls_number_restraints ? +_refine.ls_percent_reflns_obs 97.5000 +_refine.ls_percent_reflns_R_free 4.9600 +_refine.ls_R_factor_all ? +_refine.ls_R_factor_obs 0.1790 +_refine.ls_R_factor_R_free 0.2000 +_refine.ls_R_factor_R_free_error ? +_refine.ls_R_factor_R_free_error_details ? +_refine.ls_R_factor_R_work 0.1779 +_refine.ls_R_Fsqd_factor_obs ? +_refine.ls_R_I_factor_obs ? +_refine.ls_redundancy_reflns_all ? +_refine.ls_redundancy_reflns_obs ? +_refine.ls_restrained_S_all ? +_refine.ls_restrained_S_obs ? +_refine.ls_shift_over_esd_max ? +_refine.ls_shift_over_esd_mean ? +_refine.ls_structure_factor_coef ? +_refine.ls_weighting_details ? +_refine.ls_weighting_scheme ? +_refine.ls_wR_factor_all ? +_refine.ls_wR_factor_obs ? +_refine.ls_wR_factor_R_free ? +_refine.ls_wR_factor_R_work ? +_refine.occupancy_max ? +_refine.occupancy_min ? +_refine.solvent_model_details ? +_refine.solvent_model_param_bsol ? +_refine.solvent_model_param_ksol ? +_refine.pdbx_R_complete ? +_refine.ls_R_factor_gt ? +_refine.ls_goodness_of_fit_gt ? +_refine.ls_goodness_of_fit_ref ? +_refine.ls_shift_over_su_max ? +_refine.ls_shift_over_su_max_lt ? +_refine.ls_shift_over_su_mean ? +_refine.ls_shift_over_su_mean_lt ? +_refine.pdbx_ls_sigma_I ? +_refine.pdbx_ls_sigma_F 0.000 +_refine.pdbx_ls_sigma_Fsqd ? +_refine.pdbx_data_cutoff_high_absF ? +_refine.pdbx_data_cutoff_high_rms_absF ? +_refine.pdbx_data_cutoff_low_absF ? +_refine.pdbx_isotropic_thermal_model ? +_refine.pdbx_ls_cross_valid_method THROUGHOUT +_refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' +_refine.pdbx_starting_model 6LU7 +_refine.pdbx_stereochemistry_target_values ? +_refine.pdbx_R_Free_selection_details RANDOM +_refine.pdbx_stereochem_target_val_spec_case ? +_refine.pdbx_overall_ESU_R ? +_refine.pdbx_overall_ESU_R_Free ? +_refine.pdbx_solvent_vdw_probe_radii ? +_refine.pdbx_solvent_ion_probe_radii ? +_refine.pdbx_solvent_shrinkage_radii ? +_refine.pdbx_real_space_R ? +_refine.pdbx_density_correlation ? +_refine.pdbx_pd_number_of_powder_patterns ? +_refine.pdbx_pd_number_of_points ? +_refine.pdbx_pd_meas_number_of_points ? +_refine.pdbx_pd_proc_ls_prof_R_factor ? +_refine.pdbx_pd_proc_ls_prof_wR_factor ? +_refine.pdbx_pd_Marquardt_correlation_coeff ? +_refine.pdbx_pd_Fsqrd_R_factor ? +_refine.pdbx_pd_ls_matrix_band_width ? +_refine.pdbx_overall_phase_error ? +_refine.pdbx_overall_SU_R_free_Cruickshank_DPI 0.0680 +_refine.pdbx_overall_SU_R_free_Blow_DPI 0.0710 +_refine.pdbx_overall_SU_R_Blow_DPI 0.0740 +_refine.pdbx_TLS_residual_ADP_flag ? +_refine.pdbx_diffrn_id 1 +_refine.overall_SU_B ? +_refine.overall_SU_ML ? +_refine.overall_SU_R_Cruickshank_DPI 0.0690 +_refine.overall_SU_R_free ? +_refine.overall_FOM_free_R_set ? +_refine.overall_FOM_work_R_set ? +_refine.pdbx_average_fsc_overall ? +_refine.pdbx_average_fsc_work ? +_refine.pdbx_average_fsc_free ? +# +_refine_analyze.entry_id 6Y84 +_refine_analyze.pdbx_refine_id 'X-RAY DIFFRACTION' +_refine_analyze.Luzzati_coordinate_error_free ? +_refine_analyze.Luzzati_coordinate_error_obs 0.190 +_refine_analyze.Luzzati_d_res_low_free ? +_refine_analyze.Luzzati_d_res_low_obs ? +_refine_analyze.Luzzati_sigma_a_free ? +_refine_analyze.Luzzati_sigma_a_free_details ? +_refine_analyze.Luzzati_sigma_a_obs ? +_refine_analyze.Luzzati_sigma_a_obs_details ? +_refine_analyze.number_disordered_residues ? +_refine_analyze.occupancy_sum_hydrogen ? +_refine_analyze.occupancy_sum_non_hydrogen ? +_refine_analyze.RG_d_res_high ? +_refine_analyze.RG_d_res_low ? +_refine_analyze.RG_free ? +_refine_analyze.RG_work ? +_refine_analyze.RG_free_work_ratio ? +_refine_analyze.pdbx_Luzzati_d_res_high_obs ? +# +_refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' +_refine_hist.cycle_id final +_refine_hist.details ? +_refine_hist.d_res_high 1.3900 +_refine_hist.d_res_low 54.9300 +_refine_hist.number_atoms_solvent 391 +_refine_hist.number_atoms_total 2754 +_refine_hist.number_reflns_all ? +_refine_hist.number_reflns_obs ? +_refine_hist.number_reflns_R_free ? +_refine_hist.number_reflns_R_work ? +_refine_hist.R_factor_all ? +_refine_hist.R_factor_obs ? +_refine_hist.R_factor_R_free ? +_refine_hist.R_factor_R_work ? +_refine_hist.pdbx_number_residues_total 304 +_refine_hist.pdbx_B_iso_mean_ligand 33.83 +_refine_hist.pdbx_B_iso_mean_solvent 32.89 +_refine_hist.pdbx_number_atoms_protein 2347 +_refine_hist.pdbx_number_atoms_nucleic_acid 0 +_refine_hist.pdbx_number_atoms_ligand 16 +_refine_hist.pdbx_number_atoms_lipid ? +_refine_hist.pdbx_number_atoms_carb ? +_refine_hist.pdbx_pseudo_atom_details ? +# +loop_ +_refine_ls_restr.pdbx_refine_id +_refine_ls_restr.criterion +_refine_ls_restr.dev_ideal +_refine_ls_restr.dev_ideal_target +_refine_ls_restr.number +_refine_ls_restr.rejects +_refine_ls_restr.type +_refine_ls_restr.weight +_refine_ls_restr.pdbx_restraint_function +'X-RAY DIFFRACTION' ? ? ? 909 ? t_dihedral_angle_d 2.000 SINUSOIDAL +'X-RAY DIFFRACTION' ? ? ? ? ? t_trig_c_planes ? ? +'X-RAY DIFFRACTION' ? ? ? 466 ? t_gen_planes 5.000 HARMONIC +'X-RAY DIFFRACTION' ? ? ? 2628 ? t_it 10.000 HARMONIC +'X-RAY DIFFRACTION' ? ? ? ? ? t_nbd ? ? +'X-RAY DIFFRACTION' ? ? ? ? ? t_improper_torsion ? ? +'X-RAY DIFFRACTION' ? ? ? ? ? t_pseud_angle ? ? +'X-RAY DIFFRACTION' ? ? ? 340 ? t_chiral_improper_torsion 5.000 SEMIHARMONIC +'X-RAY DIFFRACTION' ? ? ? ? ? t_sum_occupancies ? ? +'X-RAY DIFFRACTION' ? ? ? ? ? t_utility_distance ? ? +'X-RAY DIFFRACTION' ? ? ? ? ? t_utility_angle ? ? +'X-RAY DIFFRACTION' ? ? ? ? ? t_utility_torsion ? ? +'X-RAY DIFFRACTION' ? ? ? 3017 ? t_ideal_dist_contact 4.000 SEMIHARMONIC +'X-RAY DIFFRACTION' ? 0.007 ? 2628 ? t_bond_d 2.000 HARMONIC +'X-RAY DIFFRACTION' ? 0.980 ? 3595 ? t_angle_deg 2.000 HARMONIC +'X-RAY DIFFRACTION' ? 3.920 ? ? ? t_omega_torsion ? ? +'X-RAY DIFFRACTION' ? 14.640 ? ? ? t_other_torsion ? ? +# +_refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' +_refine_ls_shell.d_res_high 1.3900 +_refine_ls_shell.d_res_low 1.4000 +_refine_ls_shell.number_reflns_all 1007 +_refine_ls_shell.number_reflns_obs ? +_refine_ls_shell.number_reflns_R_free 66 +_refine_ls_shell.number_reflns_R_work 941 +_refine_ls_shell.percent_reflns_obs 77.9900 +_refine_ls_shell.percent_reflns_R_free 6.5500 +_refine_ls_shell.R_factor_all 0.2107 +_refine_ls_shell.R_factor_obs ? +_refine_ls_shell.R_factor_R_free 0.2075 +_refine_ls_shell.R_factor_R_free_error 0.0000 +_refine_ls_shell.R_factor_R_work 0.2109 +_refine_ls_shell.redundancy_reflns_all ? +_refine_ls_shell.redundancy_reflns_obs ? +_refine_ls_shell.wR_factor_all ? +_refine_ls_shell.wR_factor_obs ? +_refine_ls_shell.wR_factor_R_free ? +_refine_ls_shell.wR_factor_R_work ? +_refine_ls_shell.pdbx_R_complete ? +_refine_ls_shell.pdbx_total_number_of_bins_used 51 +_refine_ls_shell.pdbx_phase_error ? +_refine_ls_shell.pdbx_fsc_work ? +_refine_ls_shell.pdbx_fsc_free ? +# +_struct.entry_id 6Y84 +_struct.title +'COVID-19 main protease with unliganded active site (2019-nCoV, coronavirus disease 2019, SARS-CoV-2)' +_struct.pdbx_descriptor 'Non-structural polyprotein 1ab' +_struct.pdbx_model_details ? +_struct.pdbx_formula_weight ? +_struct.pdbx_formula_weight_method ? +_struct.pdbx_model_type_details ? +_struct.pdbx_CASP_flag N +# +_struct_keywords.entry_id 6Y84 +_struct_keywords.text 'protease, cysteine protease, VIRAL PROTEIN' +_struct_keywords.pdbx_keywords 'VIRAL PROTEIN' +# +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 2 ? +E N N 2 ? +F N N 3 ? +# +loop_ +_struct_conf.conf_type_id +_struct_conf.id +_struct_conf.pdbx_PDB_helix_id +_struct_conf.beg_label_comp_id +_struct_conf.beg_label_asym_id +_struct_conf.beg_label_seq_id +_struct_conf.pdbx_beg_PDB_ins_code +_struct_conf.end_label_comp_id +_struct_conf.end_label_asym_id +_struct_conf.end_label_seq_id +_struct_conf.pdbx_end_PDB_ins_code +_struct_conf.beg_auth_comp_id +_struct_conf.beg_auth_asym_id +_struct_conf.beg_auth_seq_id +_struct_conf.end_auth_comp_id +_struct_conf.end_auth_asym_id +_struct_conf.end_auth_seq_id +_struct_conf.pdbx_PDB_helix_class +_struct_conf.details +_struct_conf.pdbx_PDB_helix_length +HELX_P HELX_P1 AA1 SER A 10 ? GLY A 15 ? SER A 10 GLY A 15 1 ? 6 +HELX_P HELX_P2 AA2 HIS A 41 ? CYS A 44 ? HIS A 41 CYS A 44 5 ? 4 +HELX_P HELX_P3 AA3 GLU A 47 ? ASN A 51 ? GLU A 47 ASN A 51 5 ? 5 +HELX_P HELX_P4 AA4 ASN A 53 ? ARG A 60 ? ASN A 53 ARG A 60 1 ? 8 +HELX_P HELX_P5 AA5 LYS A 61 ? HIS A 64 ? LYS A 61 HIS A 64 5 ? 4 +HELX_P HELX_P6 AA6 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15 +HELX_P HELX_P7 AA7 THR A 226 ? TYR A 237 ? THR A 226 TYR A 237 1 ? 12 +HELX_P HELX_P8 AA8 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8 +HELX_P HELX_P9 AA9 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9 +HELX_P HELX_P10 AB1 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 +HELX_P HELX_P11 AB2 THR A 292 ? GLY A 302 ? THR A 292 GLY A 302 1 ? 11 +# +_struct_conf_type.id HELX_P +_struct_conf_type.criteria ? +_struct_conf_type.reference ? +# +loop_ +_struct_sheet.id +_struct_sheet.type +_struct_sheet.number_strands +_struct_sheet.details +AA1 ? 7 ? +AA2 ? 5 ? +AA3 ? 3 ? +# +loop_ +_struct_sheet_order.sheet_id +_struct_sheet_order.range_id_1 +_struct_sheet_order.range_id_2 +_struct_sheet_order.offset +_struct_sheet_order.sense +AA1 1 2 ? anti-parallel +AA1 2 3 ? anti-parallel +AA1 3 4 ? anti-parallel +AA1 4 5 ? anti-parallel +AA1 5 6 ? anti-parallel +AA1 6 7 ? anti-parallel +AA2 1 2 ? parallel +AA2 2 3 ? anti-parallel +AA2 3 4 ? anti-parallel +AA2 4 5 ? anti-parallel +AA3 1 2 ? parallel +AA3 2 3 ? 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 +AA1 1 VAL A 73 ? LEU A 75 ? VAL A 73 LEU A 75 +AA1 2 PHE A 66 ? ALA A 70 ? PHE A 66 ALA A 70 +AA1 3 MET A 17 ? CYS A 22 ? MET A 17 CYS A 22 +AA1 4 THR A 25 ? LEU A 32 ? THR A 25 LEU A 32 +AA1 5 VAL A 35 ? PRO A 39 ? VAL A 35 PRO A 39 +AA1 6 VAL A 86 ? VAL A 91 ? VAL A 86 VAL A 91 +AA1 7 VAL A 77 ? GLN A 83 ? VAL A 77 GLN A 83 +AA2 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 +AA2 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 +AA2 3 VAL A 148 ? ASP A 153 ? VAL A 148 ASP A 153 +AA2 4 THR A 111 ? TYR A 118 ? THR A 111 TYR A 118 +AA2 5 SER A 121 ? ALA A 129 ? SER A 121 ALA A 129 +AA3 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 +AA3 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 +AA3 3 HIS A 172 ? THR A 175 ? HIS A 172 THR A 175 +# +loop_ +_pdbx_struct_sheet_hbond.sheet_id +_pdbx_struct_sheet_hbond.range_id_1 +_pdbx_struct_sheet_hbond.range_id_2 +_pdbx_struct_sheet_hbond.range_1_label_atom_id +_pdbx_struct_sheet_hbond.range_1_label_comp_id +_pdbx_struct_sheet_hbond.range_1_label_asym_id +_pdbx_struct_sheet_hbond.range_1_label_seq_id +_pdbx_struct_sheet_hbond.range_1_PDB_ins_code +_pdbx_struct_sheet_hbond.range_1_auth_atom_id +_pdbx_struct_sheet_hbond.range_1_auth_comp_id +_pdbx_struct_sheet_hbond.range_1_auth_asym_id +_pdbx_struct_sheet_hbond.range_1_auth_seq_id +_pdbx_struct_sheet_hbond.range_2_label_atom_id +_pdbx_struct_sheet_hbond.range_2_label_comp_id +_pdbx_struct_sheet_hbond.range_2_label_asym_id +_pdbx_struct_sheet_hbond.range_2_label_seq_id +_pdbx_struct_sheet_hbond.range_2_PDB_ins_code +_pdbx_struct_sheet_hbond.range_2_auth_atom_id +_pdbx_struct_sheet_hbond.range_2_auth_comp_id +_pdbx_struct_sheet_hbond.range_2_auth_asym_id +_pdbx_struct_sheet_hbond.range_2_auth_seq_id +AA1 1 2 O LEU A 75 ? O LEU A 75 N VAL A 68 ? N VAL A 68 +AA1 2 3 O GLN A 69 ? O GLN A 69 N GLN A 19 ? N GLN A 19 +AA1 3 4 N VAL A 20 ? N VAL A 20 O LEU A 27 ? O LEU A 27 +AA1 4 5 N LEU A 30 ? N LEU A 30 O TYR A 37 ? O TYR A 37 +AA1 5 6 N CYS A 38 ? N CYS A 38 O LEU A 87 ? O LEU A 87 +AA1 6 7 O LYS A 88 ? O LYS A 88 N SER A 81 ? N SER A 81 +AA2 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 +AA2 2 3 O SER A 158 ? O SER A 158 N ASN A 151 ? N ASN A 151 +AA2 3 4 O PHE A 150 ? O PHE A 150 N SER A 113 ? N SER A 113 +AA2 4 5 N ALA A 116 ? N ALA A 116 O SER A 123 ? O SER A 123 +AA3 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 +AA3 2 3 N MET A 165 ? N MET A 165 O ALA A 173 ? O ALA A 173 +# +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 A DMS 401 ? 8 'binding site for residue DMS A 401' +AC2 Software A DMS 402 ? 2 'binding site for residue DMS A 402' +AC3 Software A DMS 403 ? 6 'binding site for residue DMS A 403' +AC4 Software A DMS 404 ? 5 'binding site for residue DMS A 404' +# +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 GLN A 74 ? GLN A 74 . ? 1_555 ? +2 AC1 8 LEU A 75 ? LEU A 75 . ? 1_555 ? +3 AC1 8 ARG A 76 ? ARG A 76 . ? 1_555 ? +4 AC1 8 PHE A 223 ? PHE A 223 . ? 1_546 ? +5 AC1 8 THR A 224 ? THR A 224 . ? 1_546 ? +6 AC1 8 ASP A 263 ? ASP A 263 . ? 1_546 ? +7 AC1 8 HOH F . ? HOH A 570 . ? 1_546 ? +8 AC1 8 HOH F . ? HOH A 579 . ? 1_555 ? +9 AC2 2 HIS A 64 ? HIS A 64 . ? 1_555 ? +10 AC2 2 ASN A 65 ? ASN A 65 . ? 1_555 ? +11 AC3 6 MET A 6 ? MET A 6 . ? 1_555 ? +12 AC3 6 PHE A 8 ? PHE A 8 . ? 1_555 ? +13 AC3 6 SER A 123 ? SER A 123 . ? 2_555 ? +14 AC3 6 GLN A 127 ? GLN A 127 . ? 1_555 ? +15 AC3 6 ASP A 295 ? ASP A 295 . ? 1_555 ? +16 AC3 6 ARG A 298 ? ARG A 298 . ? 1_555 ? +17 AC4 5 GLY A 15 ? GLY A 15 . ? 1_555 ? +18 AC4 5 MET A 17 ? MET A 17 . ? 1_555 ? +19 AC4 5 LYS A 97 ? LYS A 97 . ? 1_555 ? +20 AC4 5 HOH F . ? HOH A 620 . ? 1_555 ? +21 AC4 5 HOH F . ? HOH A 654 . ? 1_555 ? +# +_atom_sites.entry_id 6Y84 +_atom_sites.Cartn_transf_matrix[1][1] ? +_atom_sites.Cartn_transf_matrix[1][2] ? +_atom_sites.Cartn_transf_matrix[1][3] ? +_atom_sites.Cartn_transf_matrix[2][1] ? +_atom_sites.Cartn_transf_matrix[2][2] ? +_atom_sites.Cartn_transf_matrix[2][3] ? +_atom_sites.Cartn_transf_matrix[3][1] ? +_atom_sites.Cartn_transf_matrix[3][2] ? +_atom_sites.Cartn_transf_matrix[3][3] ? +_atom_sites.Cartn_transf_vector[1] ? +_atom_sites.Cartn_transf_vector[2] ? +_atom_sites.Cartn_transf_vector[3] ? +_atom_sites.fract_transf_matrix[1][1] 0.008864 +_atom_sites.fract_transf_matrix[1][2] 0.000000 +_atom_sites.fract_transf_matrix[1][3] 0.002073 +_atom_sites.fract_transf_matrix[2][1] 0.000000 +_atom_sites.fract_transf_matrix[2][2] 0.018886 +_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] 0.023010 +_atom_sites.fract_transf_vector[1] 0.00000 +_atom_sites.fract_transf_vector[2] 0.00000 +_atom_sites.fract_transf_vector[3] 0.00000 +_atom_sites.solution_primary ? +_atom_sites.solution_secondary ? +_atom_sites.solution_hydrogens ? +_atom_sites.special_details ? +# +loop_ +_atom_type.symbol +C +N +O +S +# +loop_ +_atom_site.group_PDB +_atom_site.id +_atom_site.type_symbol +_atom_site.label_atom_id +_atom_site.label_alt_id +_atom_site.label_comp_id +_atom_site.label_asym_id +_atom_site.label_entity_id +_atom_site.label_seq_id +_atom_site.pdbx_PDB_ins_code +_atom_site.Cartn_x +_atom_site.Cartn_y +_atom_site.Cartn_z +_atom_site.occupancy +_atom_site.B_iso_or_equiv +_atom_site.pdbx_formal_charge +_atom_site.auth_seq_id +_atom_site.auth_comp_id +_atom_site.auth_asym_id +_atom_site.auth_atom_id +_atom_site.pdbx_PDB_model_num +ATOM 1 N N A SER A 1 1 ? -2.185 4.397 -17.079 0.50 26.55 ? 1 SER A N 1 +ATOM 2 N N B SER A 1 1 ? -2.224 4.310 -17.137 0.50 25.36 ? 1 SER A N 1 +ATOM 3 C CA A SER A 1 1 ? -2.021 5.695 -16.438 0.50 26.71 ? 1 SER A CA 1 +ATOM 4 C CA B SER A 1 1 ? -1.882 5.526 -16.417 0.50 25.40 ? 1 SER A CA 1 +ATOM 5 C C A SER A 1 1 ? -2.350 5.650 -14.945 0.50 25.98 ? 1 SER A C 1 +ATOM 6 C C B SER A 1 1 ? -2.298 5.476 -14.933 0.50 24.98 ? 1 SER A C 1 +ATOM 7 O O A SER A 1 1 ? -2.957 4.696 -14.446 0.50 25.86 ? 1 SER A O 1 +ATOM 8 O O B SER A 1 1 ? -2.988 4.551 -14.492 0.50 24.74 ? 1 SER A O 1 +ATOM 9 C CB A SER A 1 1 ? -2.819 6.777 -17.164 0.50 28.89 ? 1 SER A CB 1 +ATOM 10 C CB B SER A 1 1 ? -2.440 6.757 -17.134 0.50 27.08 ? 1 SER A CB 1 +ATOM 11 O OG A SER A 1 1 ? -2.052 7.417 -18.170 0.50 31.95 ? 1 SER A OG 1 +ATOM 12 O OG B SER A 1 1 ? -3.797 7.000 -16.801 0.50 29.72 ? 1 SER A OG 1 +ATOM 13 N N A GLY A 1 2 ? -1.917 6.679 -14.240 0.50 25.04 ? 2 GLY A N 1 +ATOM 14 N N B GLY A 1 2 ? -1.852 6.467 -14.178 0.50 24.37 ? 2 GLY A N 1 +ATOM 15 C CA A GLY A 1 2 ? -2.078 6.745 -12.803 0.50 24.62 ? 2 GLY A CA 1 +ATOM 16 C CA B GLY A 1 2 ? -2.122 6.541 -12.756 0.50 24.27 ? 2 GLY A CA 1 +ATOM 17 C C A GLY A 1 2 ? -0.786 6.340 -12.129 0.50 23.89 ? 2 GLY A C 1 +ATOM 18 C C B GLY A 1 2 ? -0.877 6.134 -12.010 0.50 23.87 ? 2 GLY A C 1 +ATOM 19 O O A GLY A 1 2 ? -0.004 5.553 -12.671 0.50 24.05 ? 2 GLY A O 1 +ATOM 20 O O B GLY A 1 2 ? -0.206 5.169 -12.398 0.50 24.00 ? 2 GLY A O 1 +ATOM 21 N N . PHE A 1 3 ? -0.560 6.863 -10.941 1.00 22.93 ? 3 PHE A N 1 +ATOM 22 C CA . PHE A 1 3 ? 0.639 6.585 -10.184 1.00 22.04 ? 3 PHE A CA 1 +ATOM 23 C C . PHE A 1 3 ? 0.290 6.604 -8.729 1.00 21.78 ? 3 PHE A C 1 +ATOM 24 O O . PHE A 1 3 ? -0.157 7.619 -8.198 1.00 23.62 ? 3 PHE A O 1 +ATOM 25 C CB . PHE A 1 3 ? 1.732 7.609 -10.538 1.00 21.01 ? 3 PHE A CB 1 +ATOM 26 C CG . PHE A 1 3 ? 3.117 7.084 -10.258 1.00 21.05 ? 3 PHE A CG 1 +ATOM 27 C CD1 . PHE A 1 3 ? 3.724 6.190 -11.120 1.00 21.40 ? 3 PHE A CD1 1 +ATOM 28 C CD2 . PHE A 1 3 ? 3.799 7.464 -9.122 1.00 21.44 ? 3 PHE A CD2 1 +ATOM 29 C CE1 . PHE A 1 3 ? 4.993 5.696 -10.852 1.00 22.14 ? 3 PHE A CE1 1 +ATOM 30 C CE2 . PHE A 1 3 ? 5.075 6.985 -8.870 1.00 21.61 ? 3 PHE A CE2 1 +ATOM 31 C CZ . PHE A 1 3 ? 5.652 6.081 -9.717 1.00 21.71 ? 3 PHE A CZ 1 +ATOM 32 N N . ARG A 1 4 ? 0.443 5.457 -8.087 1.00 19.43 ? 4 ARG A N 1 +ATOM 33 C CA . ARG A 1 4 ? 0.091 5.280 -6.693 1.00 18.12 ? 4 ARG A CA 1 +ATOM 34 C C . ARG A 1 4 ? 1.257 4.818 -5.846 1.00 17.46 ? 4 ARG A C 1 +ATOM 35 O O . ARG A 1 4 ? 2.173 4.183 -6.358 1.00 18.03 ? 4 ARG A O 1 +ATOM 36 C CB . ARG A 1 4 ? -0.984 4.179 -6.615 1.00 19.34 ? 4 ARG A CB 1 +ATOM 37 C CG . ARG A 1 4 ? -2.389 4.693 -6.846 1.00 22.46 ? 4 ARG A CG 1 +ATOM 38 C CD . ARG A 1 4 ? -2.962 5.187 -5.525 1.00 25.30 ? 4 ARG A CD 1 +ATOM 39 N NE . ARG A 1 4 ? -4.352 5.630 -5.666 1.00 28.96 ? 4 ARG A NE 1 +ATOM 40 C CZ . ARG A 1 4 ? -5.041 6.254 -4.713 1.00 31.07 ? 4 ARG A CZ 1 +ATOM 41 N NH1 . ARG A 1 4 ? -4.479 6.508 -3.538 1.00 31.07 ? 4 ARG A NH1 1 +ATOM 42 N NH2 . ARG A 1 4 ? -6.295 6.632 -4.932 1.00 28.97 ? 4 ARG A NH2 1 +ATOM 43 N N A LYS A 1 5 ? 1.185 5.069 -4.531 0.50 16.58 ? 5 LYS A N 1 +ATOM 44 N N B LYS A 1 5 ? 1.202 5.059 -4.523 0.50 16.76 ? 5 LYS A N 1 +ATOM 45 C CA A LYS A 1 5 ? 2.185 4.556 -3.613 0.50 16.63 ? 5 LYS A CA 1 +ATOM 46 C CA B LYS A 1 5 ? 2.235 4.584 -3.597 0.50 16.99 ? 5 LYS A CA 1 +ATOM 47 C C A LYS A 1 5 ? 1.841 3.080 -3.508 0.50 17.04 ? 5 LYS A C 1 +ATOM 48 C C B LYS A 1 5 ? 1.980 3.098 -3.369 0.50 17.63 ? 5 LYS A C 1 +ATOM 49 O O A LYS A 1 5 ? 0.747 2.726 -3.077 0.50 17.39 ? 5 LYS A O 1 +ATOM 50 O O B LYS A 1 5 ? 1.203 2.711 -2.496 0.50 18.57 ? 5 LYS A O 1 +ATOM 51 C CB A LYS A 1 5 ? 2.120 5.253 -2.246 0.50 17.92 ? 5 LYS A CB 1 +ATOM 52 C CB B LYS A 1 5 ? 2.196 5.363 -2.273 0.50 18.19 ? 5 LYS A CB 1 +ATOM 53 C CG A LYS A 1 5 ? 3.300 4.911 -1.342 0.50 21.29 ? 5 LYS A CG 1 +ATOM 54 C CG B LYS A 1 5 ? 3.332 5.005 -1.326 0.50 21.43 ? 5 LYS A CG 1 +ATOM 55 C CD A LYS A 1 5 ? 4.637 5.388 -1.894 0.50 24.62 ? 5 LYS A CD 1 +ATOM 56 C CD B LYS A 1 5 ? 4.694 5.391 -1.868 0.50 24.70 ? 5 LYS A CD 1 +ATOM 57 C CE A LYS A 1 5 ? 4.810 6.884 -1.795 0.50 27.77 ? 5 LYS A CE 1 +ATOM 58 C CE B LYS A 1 5 ? 4.925 6.879 -1.800 0.50 27.68 ? 5 LYS A CE 1 +ATOM 59 N NZ A LYS A 1 5 ? 4.611 7.386 -0.415 0.50 29.14 ? 5 LYS A NZ 1 +ATOM 60 N NZ B LYS A 1 5 ? 4.633 7.433 -0.457 0.50 28.93 ? 5 LYS A NZ 1 +ATOM 61 N N . MET A 1 6 ? 2.663 2.273 -4.148 1.00 17.01 ? 6 MET A N 1 +ATOM 62 C CA . MET A 1 6 ? 2.427 0.855 -4.239 1.00 17.12 ? 6 MET A CA 1 +ATOM 63 C C . MET A 1 6 ? 3.367 0.015 -3.454 1.00 15.93 ? 6 MET A C 1 +ATOM 64 O O . MET A 1 6 ? 4.570 0.202 -3.547 1.00 16.36 ? 6 MET A O 1 +ATOM 65 C CB . MET A 1 6 ? 2.580 0.517 -5.725 1.00 19.42 ? 6 MET A CB 1 +ATOM 66 C CG . MET A 1 6 ? 2.137 -0.836 -6.077 1.00 24.58 ? 6 MET A CG 1 +ATOM 67 S SD . MET A 1 6 ? 2.195 -0.979 -7.868 1.00 31.98 ? 6 MET A SD 1 +ATOM 68 C CE . MET A 1 6 ? 0.949 0.182 -8.339 1.00 27.76 ? 6 MET A CE 1 +ATOM 69 N N . ALA A 1 7 ? 2.820 -0.956 -2.733 1.00 14.89 ? 7 ALA A N 1 +ATOM 70 C CA . ALA A 1 7 ? 3.639 -1.900 -1.989 1.00 15.29 ? 7 ALA A CA 1 +ATOM 71 C C . ALA A 1 7 ? 3.744 -3.190 -2.803 1.00 15.57 ? 7 ALA A C 1 +ATOM 72 O O . ALA A 1 7 ? 2.963 -3.405 -3.734 1.00 16.04 ? 7 ALA A O 1 +ATOM 73 C CB . ALA A 1 7 ? 3.006 -2.185 -0.630 1.00 15.59 ? 7 ALA A CB 1 +ATOM 74 N N . PHE A 1 8 ? 4.742 -4.010 -2.521 1.00 15.58 ? 8 PHE A N 1 +ATOM 75 C CA . PHE A 1 8 ? 4.868 -5.305 -3.172 1.00 16.87 ? 8 PHE A CA 1 +ATOM 76 C C . PHE A 1 8 ? 3.750 -6.202 -2.661 1.00 16.69 ? 8 PHE A C 1 +ATOM 77 O O . PHE A 1 8 ? 3.298 -6.088 -1.511 1.00 16.04 ? 8 PHE A O 1 +ATOM 78 C CB . PHE A 1 8 ? 6.222 -5.940 -2.834 1.00 17.33 ? 8 PHE A CB 1 +ATOM 79 C CG . PHE A 1 8 ? 7.358 -5.313 -3.588 1.00 19.06 ? 8 PHE A CG 1 +ATOM 80 C CD1 . PHE A 1 8 ? 7.607 -5.651 -4.907 1.00 20.90 ? 8 PHE A CD1 1 +ATOM 81 C CD2 . PHE A 1 8 ? 8.164 -4.366 -2.990 1.00 20.60 ? 8 PHE A CD2 1 +ATOM 82 C CE1 . PHE A 1 8 ? 8.640 -5.049 -5.607 1.00 22.00 ? 8 PHE A CE1 1 +ATOM 83 C CE2 . PHE A 1 8 ? 9.209 -3.787 -3.685 1.00 21.94 ? 8 PHE A CE2 1 +ATOM 84 C CZ . PHE A 1 8 ? 9.433 -4.123 -4.991 1.00 22.08 ? 8 PHE A CZ 1 +ATOM 85 N N . PRO A 1 9 ? 3.322 -7.176 -3.489 1.00 17.15 ? 9 PRO A N 1 +ATOM 86 C CA . PRO A 1 9 ? 2.348 -8.173 -3.002 1.00 17.33 ? 9 PRO A CA 1 +ATOM 87 C C . PRO A 1 9 ? 2.939 -8.881 -1.771 1.00 17.30 ? 9 PRO A C 1 +ATOM 88 O O . PRO A 1 9 ? 4.125 -9.203 -1.771 1.00 19.22 ? 9 PRO A O 1 +ATOM 89 C CB . PRO A 1 9 ? 2.198 -9.124 -4.195 1.00 19.02 ? 9 PRO A CB 1 +ATOM 90 C CG . PRO A 1 9 ? 2.667 -8.338 -5.372 1.00 19.72 ? 9 PRO A CG 1 +ATOM 91 C CD . PRO A 1 9 ? 3.768 -7.478 -4.860 1.00 17.41 ? 9 PRO A CD 1 +ATOM 92 N N . SER A 1 10 ? 2.170 -8.982 -0.714 1.00 15.92 ? 10 SER A N 1 +ATOM 93 C CA . SER A 1 10 ? 2.701 -9.448 0.569 1.00 15.16 ? 10 SER A CA 1 +ATOM 94 C C . SER A 1 10 ? 2.612 -10.944 0.842 1.00 15.12 ? 10 SER A C 1 +ATOM 95 O O . SER A 1 10 ? 3.100 -11.378 1.869 1.00 14.73 ? 10 SER A O 1 +ATOM 96 C CB . SER A 1 10 ? 2.029 -8.690 1.705 1.00 15.91 ? 10 SER A CB 1 +ATOM 97 O OG . SER A 1 10 ? 0.623 -8.864 1.658 1.00 17.96 ? 10 SER A OG 1 +ATOM 98 N N . GLY A 1 11 ? 2.001 -11.708 -0.041 1.00 15.29 ? 11 GLY A N 1 +ATOM 99 C CA . GLY A 1 11 ? 1.797 -13.135 0.179 1.00 15.09 ? 11 GLY A CA 1 +ATOM 100 C C . GLY A 1 11 ? 3.008 -13.943 0.596 1.00 14.62 ? 11 GLY A C 1 +ATOM 101 O O . GLY A 1 11 ? 2.943 -14.731 1.548 1.00 15.34 ? 11 GLY A O 1 +ATOM 102 N N . LYS A 1 12 ? 4.126 -13.735 -0.106 1.00 13.99 ? 12 LYS A N 1 +ATOM 103 C CA . LYS A 1 12 ? 5.345 -14.487 0.193 1.00 14.02 ? 12 LYS A CA 1 +ATOM 104 C C . LYS A 1 12 ? 5.831 -14.217 1.613 1.00 14.16 ? 12 LYS A C 1 +ATOM 105 O O . LYS A 1 12 ? 6.375 -15.110 2.261 1.00 14.81 ? 12 LYS A O 1 +ATOM 106 C CB . LYS A 1 12 ? 6.449 -14.195 -0.821 1.00 15.54 ? 12 LYS A CB 1 +ATOM 107 C CG . LYS A 1 12 ? 6.209 -14.833 -2.180 1.00 19.84 ? 12 LYS A CG 1 +ATOM 108 C CD . LYS A 1 12 ? 7.166 -14.268 -3.223 1.00 25.38 ? 12 LYS A CD 1 +ATOM 109 C CE . LYS A 1 12 ? 6.905 -14.864 -4.589 1.00 30.94 ? 12 LYS A CE 1 +ATOM 110 N NZ . LYS A 1 12 ? 7.019 -16.342 -4.559 1.00 34.47 ? 12 LYS A NZ 1 +ATOM 111 N N . VAL A 1 13 ? 5.605 -12.996 2.114 1.00 13.22 ? 13 VAL A N 1 +ATOM 112 C CA . VAL A 1 13 ? 6.032 -12.646 3.468 1.00 12.21 ? 13 VAL A CA 1 +ATOM 113 C C . VAL A 1 13 ? 5.000 -13.074 4.500 1.00 11.66 ? 13 VAL A C 1 +ATOM 114 O O . VAL A 1 13 ? 5.364 -13.520 5.588 1.00 11.73 ? 13 VAL A O 1 +ATOM 115 C CB . VAL A 1 13 ? 6.355 -11.145 3.551 1.00 13.09 ? 13 VAL A CB 1 +ATOM 116 C CG1 . VAL A 1 13 ? 6.822 -10.761 4.950 1.00 14.14 ? 13 VAL A CG1 1 +ATOM 117 C CG2 . VAL A 1 13 ? 7.411 -10.784 2.519 1.00 14.34 ? 13 VAL A CG2 1 +ATOM 118 N N . GLU A 1 14 ? 3.701 -13.021 4.159 1.00 11.62 ? 14 GLU A N 1 +ATOM 119 C CA . GLU A 1 14 ? 2.641 -13.473 5.068 1.00 11.63 ? 14 GLU A CA 1 +ATOM 120 C C . GLU A 1 14 ? 2.876 -14.916 5.521 1.00 12.71 ? 14 GLU A C 1 +ATOM 121 O O . GLU A 1 14 ? 2.716 -15.224 6.703 1.00 13.03 ? 14 GLU A O 1 +ATOM 122 C CB . GLU A 1 14 ? 1.275 -13.399 4.373 1.00 12.59 ? 14 GLU A CB 1 +ATOM 123 C CG . GLU A 1 14 ? 0.756 -11.988 4.211 1.00 15.46 ? 14 GLU A CG 1 +ATOM 124 C CD . GLU A 1 14 ? -0.445 -11.950 3.292 1.00 18.75 ? 14 GLU A CD 1 +ATOM 125 O OE1 . GLU A 1 14 ? -1.417 -12.694 3.553 1.00 21.44 ? 14 GLU A OE1 1 +ATOM 126 O OE2 . GLU A 1 14 ? -0.390 -11.204 2.289 1.00 19.65 ? 14 GLU A OE2 1 +ATOM 127 N N . GLY A 1 15 ? 3.357 -15.745 4.598 1.00 12.90 ? 15 GLY A N 1 +ATOM 128 C CA . GLY A 1 15 ? 3.649 -17.145 4.878 1.00 12.73 ? 15 GLY A CA 1 +ATOM 129 C C . GLY A 1 15 ? 4.818 -17.392 5.810 1.00 12.45 ? 15 GLY A C 1 +ATOM 130 O O . GLY A 1 15 ? 5.068 -18.532 6.200 1.00 13.52 ? 15 GLY A O 1 +ATOM 131 N N . CYS A 1 16 ? 5.547 -16.341 6.161 1.00 11.59 ? 16 CYS A N 1 +ATOM 132 C CA . CYS A 1 16 ? 6.690 -16.411 7.064 1.00 11.47 ? 16 CYS A CA 1 +ATOM 133 C C . CYS A 1 16 ? 6.412 -15.838 8.439 1.00 11.91 ? 16 CYS A C 1 +ATOM 134 O O . CYS A 1 16 ? 7.299 -15.910 9.283 1.00 12.77 ? 16 CYS A O 1 +ATOM 135 C CB . CYS A 1 16 ? 7.899 -15.722 6.446 1.00 12.44 ? 16 CYS A CB 1 +ATOM 136 S SG . CYS A 1 16 ? 8.356 -16.342 4.810 1.00 15.98 ? 16 CYS A SG 1 +ATOM 137 N N . MET A 1 17 ? 5.240 -15.226 8.673 1.00 11.61 ? 17 MET A N 1 +ATOM 138 C CA . MET A 1 17 ? 5.017 -14.567 9.953 1.00 12.03 ? 17 MET A CA 1 +ATOM 139 C C . MET A 1 17 ? 4.535 -15.499 11.022 1.00 12.33 ? 17 MET A C 1 +ATOM 140 O O . MET A 1 17 ? 3.618 -16.266 10.806 1.00 12.97 ? 17 MET A O 1 +ATOM 141 C CB . MET A 1 17 ? 4.077 -13.372 9.816 1.00 12.21 ? 17 MET A CB 1 +ATOM 142 C CG . MET A 1 17 ? 4.535 -12.353 8.787 1.00 13.24 ? 17 MET A CG 1 +ATOM 143 S SD . MET A 1 17 ? 6.217 -11.703 9.005 1.00 14.39 ? 17 MET A SD 1 +ATOM 144 C CE . MET A 1 17 ? 6.158 -11.181 10.754 1.00 15.96 ? 17 MET A CE 1 +ATOM 145 N N . VAL A 1 18 ? 5.186 -15.438 12.176 1.00 11.86 ? 18 VAL A N 1 +ATOM 146 C CA . VAL A 1 18 ? 4.849 -16.234 13.343 1.00 12.74 ? 18 VAL A CA 1 +ATOM 147 C C . VAL A 1 18 ? 4.775 -15.312 14.559 1.00 12.62 ? 18 VAL A C 1 +ATOM 148 O O . VAL A 1 18 ? 5.220 -14.160 14.518 1.00 12.38 ? 18 VAL A O 1 +ATOM 149 C CB . VAL A 1 18 ? 5.882 -17.373 13.576 1.00 13.97 ? 18 VAL A CB 1 +ATOM 150 C CG1 . VAL A 1 18 ? 5.917 -18.341 12.404 1.00 14.87 ? 18 VAL A CG1 1 +ATOM 151 C CG2 . VAL A 1 18 ? 7.262 -16.802 13.868 1.00 13.93 ? 18 VAL A CG2 1 +ATOM 152 N N . GLN A 1 19 ? 4.185 -15.818 15.633 1.00 12.65 ? 19 GLN A N 1 +ATOM 153 C CA . GLN A 1 19 ? 4.107 -15.113 16.896 1.00 13.10 ? 19 GLN A CA 1 +ATOM 154 C C . GLN A 1 19 ? 5.221 -15.641 17.802 1.00 12.93 ? 19 GLN A C 1 +ATOM 155 O O . GLN A 1 19 ? 5.433 -16.850 17.868 1.00 12.86 ? 19 GLN A O 1 +ATOM 156 C CB . GLN A 1 19 ? 2.735 -15.376 17.520 1.00 14.90 ? 19 GLN A CB 1 +ATOM 157 C CG . GLN A 1 19 ? 2.552 -14.741 18.881 1.00 18.61 ? 19 GLN A CG 1 +ATOM 158 C CD . GLN A 1 19 ? 1.293 -15.237 19.530 1.00 24.25 ? 19 GLN A CD 1 +ATOM 159 O OE1 . GLN A 1 19 ? 1.285 -16.257 20.224 1.00 26.10 ? 19 GLN A OE1 1 +ATOM 160 N NE2 . GLN A 1 19 ? 0.206 -14.527 19.326 1.00 25.55 ? 19 GLN A NE2 1 +ATOM 161 N N . VAL A 1 20 ? 5.940 -14.742 18.500 1.00 12.43 ? 20 VAL A N 1 +ATOM 162 C CA . VAL A 1 20 ? 6.962 -15.171 19.450 1.00 13.22 ? 20 VAL A CA 1 +ATOM 163 C C . VAL A 1 20 ? 6.631 -14.580 20.807 1.00 13.82 ? 20 VAL A C 1 +ATOM 164 O O . VAL A 1 20 ? 6.435 -13.367 20.921 1.00 14.21 ? 20 VAL A O 1 +ATOM 165 C CB . VAL A 1 20 ? 8.405 -14.806 19.036 1.00 13.47 ? 20 VAL A CB 1 +ATOM 166 C CG1 . VAL A 1 20 ? 9.408 -15.330 20.066 1.00 14.22 ? 20 VAL A CG1 1 +ATOM 167 C CG2 . VAL A 1 20 ? 8.731 -15.348 17.650 1.00 13.91 ? 20 VAL A CG2 1 +ATOM 168 N N . THR A 1 21 ? 6.537 -15.429 21.823 1.00 14.34 ? 21 THR A N 1 +ATOM 169 C CA . THR A 1 21 ? 6.264 -14.970 23.174 1.00 15.62 ? 21 THR A CA 1 +ATOM 170 C C . THR A 1 21 ? 7.382 -15.417 24.085 1.00 16.58 ? 21 THR A C 1 +ATOM 171 O O . THR A 1 21 ? 7.797 -16.567 24.035 1.00 16.63 ? 21 THR A O 1 +ATOM 172 C CB . THR A 1 21 ? 4.920 -15.534 23.681 1.00 18.06 ? 21 THR A CB 1 +ATOM 173 O OG1 . THR A 1 21 ? 3.855 -15.130 22.823 1.00 19.40 ? 21 THR A OG1 1 +ATOM 174 C CG2 . THR A 1 21 ? 4.614 -15.109 25.110 1.00 19.50 ? 21 THR A CG2 1 +ATOM 175 N N . CYS A 1 22 ? 7.882 -14.511 24.909 1.00 17.62 ? 22 CYS A N 1 +ATOM 176 C CA . CYS A 1 22 ? 8.866 -14.862 25.915 1.00 19.68 ? 22 CYS A CA 1 +ATOM 177 C C . CYS A 1 22 ? 8.353 -14.192 27.181 1.00 22.21 ? 22 CYS A C 1 +ATOM 178 O O . CYS A 1 22 ? 8.185 -12.976 27.221 1.00 22.29 ? 22 CYS A O 1 +ATOM 179 C CB . CYS A 1 22 ? 10.273 -14.403 25.535 1.00 19.81 ? 22 CYS A CB 1 +ATOM 180 S SG . CYS A 1 22 ? 11.574 -15.049 26.614 1.00 26.04 ? 22 CYS A SG 1 +ATOM 181 N N . GLY A 1 23 ? 7.977 -15.014 28.151 1.00 24.20 ? 23 GLY A N 1 +ATOM 182 C CA . GLY A 1 23 ? 7.401 -14.541 29.403 1.00 25.86 ? 23 GLY A CA 1 +ATOM 183 C C . GLY A 1 23 ? 6.078 -13.859 29.141 1.00 27.25 ? 23 GLY A C 1 +ATOM 184 O O . GLY A 1 23 ? 5.164 -14.465 28.577 1.00 28.42 ? 23 GLY A O 1 +ATOM 185 N N . THR A 1 24 ? 6.013 -12.564 29.424 1.00 27.33 ? 24 THR A N 1 +ATOM 186 C CA . THR A 1 24 ? 4.800 -11.787 29.185 1.00 27.90 ? 24 THR A CA 1 +ATOM 187 C C . THR A 1 24 ? 4.849 -10.946 27.898 1.00 26.48 ? 24 THR A C 1 +ATOM 188 O O . THR A 1 24 ? 3.899 -10.223 27.618 1.00 27.56 ? 24 THR A O 1 +ATOM 189 C CB . THR A 1 24 ? 4.514 -10.899 30.395 1.00 31.42 ? 24 THR A CB 1 +ATOM 190 O OG1 . THR A 1 24 ? 5.534 -9.903 30.499 1.00 33.89 ? 24 THR A OG1 1 +ATOM 191 C CG2 . THR A 1 24 ? 4.440 -11.691 31.681 1.00 32.45 ? 24 THR A CG2 1 +ATOM 192 N N . THR A 1 25 ? 5.938 -11.023 27.128 1.00 24.11 ? 25 THR A N 1 +ATOM 193 C CA . THR A 1 25 ? 6.082 -10.214 25.922 1.00 22.53 ? 25 THR A CA 1 +ATOM 194 C C . THR A 1 25 ? 5.755 -11.009 24.671 1.00 21.00 ? 25 THR A C 1 +ATOM 195 O O . THR A 1 25 ? 6.304 -12.083 24.490 1.00 21.49 ? 25 THR A O 1 +ATOM 196 C CB . THR A 1 25 ? 7.503 -9.662 25.850 1.00 23.52 ? 25 THR A CB 1 +ATOM 197 O OG1 . THR A 1 25 ? 7.752 -8.858 27.011 1.00 24.80 ? 25 THR A OG1 1 +ATOM 198 C CG2 . THR A 1 25 ? 7.756 -8.862 24.584 1.00 23.98 ? 25 THR A CG2 1 +ATOM 199 N N . THR A 1 26 ? 4.880 -10.486 23.817 1.00 19.91 ? 26 THR A N 1 +ATOM 200 C CA . THR A 1 26 ? 4.539 -11.124 22.554 1.00 19.02 ? 26 THR A CA 1 +ATOM 201 C C . THR A 1 26 ? 4.814 -10.164 21.401 1.00 17.49 ? 26 THR A C 1 +ATOM 202 O O . THR A 1 26 ? 4.376 -9.013 21.413 1.00 18.04 ? 26 THR A O 1 +ATOM 203 C CB . THR A 1 26 ? 3.074 -11.584 22.541 1.00 20.95 ? 26 THR A CB 1 +ATOM 204 O OG1 . THR A 1 26 ? 2.900 -12.636 23.488 1.00 22.53 ? 26 THR A OG1 1 +ATOM 205 C CG2 . THR A 1 26 ? 2.634 -12.069 21.182 1.00 21.72 ? 26 THR A CG2 1 +ATOM 206 N N . LEU A 1 27 ? 5.539 -10.637 20.411 1.00 15.55 ? 27 LEU A N 1 +ATOM 207 C CA . LEU A 1 27 ? 5.787 -9.858 19.200 1.00 14.34 ? 27 LEU A CA 1 +ATOM 208 C C . LEU A 1 27 ? 5.841 -10.794 17.990 1.00 13.54 ? 27 LEU A C 1 +ATOM 209 O O . LEU A 1 27 ? 5.400 -11.943 18.087 1.00 13.86 ? 27 LEU A O 1 +ATOM 210 C CB . LEU A 1 27 ? 7.007 -8.909 19.344 1.00 13.99 ? 27 LEU A CB 1 +ATOM 211 C CG . LEU A 1 27 ? 8.263 -9.503 19.968 1.00 14.11 ? 27 LEU A CG 1 +ATOM 212 C CD1 . LEU A 1 27 ? 8.801 -10.671 19.161 1.00 14.29 ? 27 LEU A CD1 1 +ATOM 213 C CD2 . LEU A 1 27 ? 9.349 -8.450 20.127 1.00 14.70 ? 27 LEU A CD2 1 +ATOM 214 N N . ASN A 1 28 ? 6.313 -10.302 16.845 1.00 12.24 ? 28 ASN A N 1 +ATOM 215 C CA . ASN A 1 28 ? 6.346 -11.091 15.631 1.00 11.92 ? 28 ASN A CA 1 +ATOM 216 C C . ASN A 1 28 ? 7.714 -11.653 15.355 1.00 11.52 ? 28 ASN A C 1 +ATOM 217 O O . ASN A 1 28 ? 8.725 -11.066 15.710 1.00 11.85 ? 28 ASN A O 1 +ATOM 218 C CB . ASN A 1 28 ? 5.884 -10.259 14.427 1.00 13.05 ? 28 ASN A CB 1 +ATOM 219 C CG . ASN A 1 28 ? 4.569 -9.595 14.702 1.00 15.18 ? 28 ASN A CG 1 +ATOM 220 O OD1 . ASN A 1 28 ? 3.512 -10.223 14.621 1.00 15.52 ? 28 ASN A OD1 1 +ATOM 221 N ND2 . ASN A 1 28 ? 4.620 -8.331 15.068 1.00 15.66 ? 28 ASN A ND2 1 +ATOM 222 N N . GLY A 1 29 ? 7.713 -12.775 14.686 1.00 11.02 ? 29 GLY A N 1 +ATOM 223 C CA . GLY A 1 29 ? 8.925 -13.411 14.219 1.00 11.06 ? 29 GLY A CA 1 +ATOM 224 C C . GLY A 1 29 ? 8.812 -13.718 12.738 1.00 11.20 ? 29 GLY A C 1 +ATOM 225 O O . GLY A 1 29 ? 7.714 -13.803 12.179 1.00 11.95 ? 29 GLY A O 1 +ATOM 226 N N . LEU A 1 30 ? 9.956 -13.877 12.090 1.00 10.90 ? 30 LEU A N 1 +ATOM 227 C CA . LEU A 1 30 ? 10.046 -14.190 10.667 1.00 10.82 ? 30 LEU A CA 1 +ATOM 228 C C . LEU A 1 30 ? 10.616 -15.606 10.560 1.00 10.79 ? 30 LEU A C 1 +ATOM 229 O O . LEU A 1 30 ? 11.740 -15.840 11.002 1.00 11.77 ? 30 LEU A O 1 +ATOM 230 C CB . LEU A 1 30 ? 10.994 -13.195 9.995 1.00 10.42 ? 30 LEU A CB 1 +ATOM 231 C CG . LEU A 1 30 ? 11.086 -13.328 8.477 1.00 11.21 ? 30 LEU A CG 1 +ATOM 232 C CD1 . LEU A 1 30 ? 9.784 -12.894 7.816 1.00 12.16 ? 30 LEU A CD1 1 +ATOM 233 C CD2 . LEU A 1 30 ? 12.245 -12.507 7.952 1.00 12.12 ? 30 LEU A CD2 1 +ATOM 234 N N . TRP A 1 31 ? 9.866 -16.535 9.979 1.00 10.46 ? 31 TRP A N 1 +ATOM 235 C CA . TRP A 1 31 ? 10.255 -17.943 9.908 1.00 10.74 ? 31 TRP A CA 1 +ATOM 236 C C . TRP A 1 31 ? 10.711 -18.287 8.502 1.00 11.18 ? 31 TRP A C 1 +ATOM 237 O O . TRP A 1 31 ? 9.923 -18.273 7.553 1.00 11.15 ? 31 TRP A O 1 +ATOM 238 C CB . TRP A 1 31 ? 9.054 -18.777 10.353 1.00 11.08 ? 31 TRP A CB 1 +ATOM 239 C CG . TRP A 1 31 ? 9.218 -20.262 10.334 1.00 11.19 ? 31 TRP A CG 1 +ATOM 240 C CD1 . TRP A 1 31 ? 10.371 -20.974 10.511 1.00 11.87 ? 31 TRP A CD1 1 +ATOM 241 C CD2 . TRP A 1 31 ? 8.153 -21.221 10.295 1.00 11.18 ? 31 TRP A CD2 1 +ATOM 242 N NE1 . TRP A 1 31 ? 10.090 -22.323 10.513 1.00 11.94 ? 31 TRP A NE1 1 +ATOM 243 C CE2 . TRP A 1 31 ? 8.734 -22.499 10.412 1.00 11.98 ? 31 TRP A CE2 1 +ATOM 244 C CE3 . TRP A 1 31 ? 6.763 -21.123 10.121 1.00 11.96 ? 31 TRP A CE3 1 +ATOM 245 C CZ2 . TRP A 1 31 ? 7.976 -23.673 10.353 1.00 12.16 ? 31 TRP A CZ2 1 +ATOM 246 C CZ3 . TRP A 1 31 ? 6.013 -22.284 10.075 1.00 12.27 ? 31 TRP A CZ3 1 +ATOM 247 C CH2 . TRP A 1 31 ? 6.621 -23.544 10.169 1.00 12.25 ? 31 TRP A CH2 1 +ATOM 248 N N . LEU A 1 32 ? 12.025 -18.505 8.356 1.00 11.11 ? 32 LEU A N 1 +ATOM 249 C CA . LEU A 1 32 ? 12.646 -18.808 7.060 1.00 12.05 ? 32 LEU A CA 1 +ATOM 250 C C . LEU A 1 32 ? 13.464 -20.041 7.259 1.00 12.52 ? 32 LEU A C 1 +ATOM 251 O O . LEU A 1 32 ? 14.277 -20.097 8.192 1.00 12.39 ? 32 LEU A O 1 +ATOM 252 C CB . LEU A 1 32 ? 13.563 -17.678 6.627 1.00 12.45 ? 32 LEU A CB 1 +ATOM 253 C CG . LEU A 1 32 ? 12.892 -16.342 6.393 1.00 13.71 ? 32 LEU A CG 1 +ATOM 254 C CD1 . LEU A 1 32 ? 13.907 -15.285 6.173 1.00 13.62 ? 32 LEU A CD1 1 +ATOM 255 C CD2 . LEU A 1 32 ? 11.959 -16.400 5.210 1.00 14.51 ? 32 LEU A CD2 1 +ATOM 256 N N . ASP A 1 33 ? 13.193 -21.093 6.468 1.00 12.93 ? 33 ASP A N 1 +ATOM 257 C CA . ASP A 1 33 ? 13.854 -22.381 6.675 1.00 13.70 ? 33 ASP A CA 1 +ATOM 258 C C . ASP A 1 33 ? 13.561 -22.852 8.132 1.00 13.91 ? 33 ASP A C 1 +ATOM 259 O O . ASP A 1 33 ? 12.412 -22.706 8.557 1.00 14.60 ? 33 ASP A O 1 +ATOM 260 C CB . ASP A 1 33 ? 15.356 -22.306 6.311 1.00 16.27 ? 33 ASP A CB 1 +ATOM 261 C CG . ASP A 1 33 ? 15.597 -21.887 4.883 1.00 21.63 ? 33 ASP A CG 1 +ATOM 262 O OD1 . ASP A 1 33 ? 14.817 -22.304 4.008 1.00 23.84 ? 33 ASP A OD1 1 +ATOM 263 O OD2 . ASP A 1 33 ? 16.574 -21.142 4.642 1.00 23.06 ? 33 ASP A OD2 1 +ATOM 264 N N . ASP A 1 34 ? 14.549 -23.299 8.901 1.00 12.95 ? 34 ASP A N 1 +ATOM 265 C CA . ASP A 1 34 ? 14.306 -23.727 10.265 1.00 12.62 ? 34 ASP A CA 1 +ATOM 266 C C . ASP A 1 34 ? 14.745 -22.702 11.278 1.00 12.42 ? 34 ASP A C 1 +ATOM 267 O O . ASP A 1 34 ? 15.104 -23.073 12.395 1.00 13.06 ? 34 ASP A O 1 +ATOM 268 C CB . ASP A 1 34 ? 14.988 -25.077 10.522 1.00 13.51 ? 34 ASP A CB 1 +ATOM 269 C CG . ASP A 1 34 ? 16.497 -25.078 10.331 1.00 17.85 ? 34 ASP A CG 1 +ATOM 270 O OD1 . ASP A 1 34 ? 17.037 -24.076 9.798 1.00 17.68 ? 34 ASP A OD1 1 +ATOM 271 O OD2 . ASP A 1 34 ? 17.138 -26.087 10.709 1.00 20.21 ? 34 ASP A OD2 1 +ATOM 272 N N . VAL A 1 35 ? 14.689 -21.404 10.928 1.00 11.43 ? 35 VAL A N 1 +ATOM 273 C CA . VAL A 1 35 ? 15.074 -20.358 11.868 1.00 12.04 ? 35 VAL A CA 1 +ATOM 274 C C . VAL A 1 35 ? 13.987 -19.307 11.950 1.00 11.65 ? 35 VAL A C 1 +ATOM 275 O O . VAL A 1 35 ? 13.400 -18.939 10.930 1.00 12.01 ? 35 VAL A O 1 +ATOM 276 C CB . VAL A 1 35 ? 16.424 -19.702 11.481 1.00 13.42 ? 35 VAL A CB 1 +ATOM 277 C CG1 . VAL A 1 35 ? 16.824 -18.604 12.473 1.00 13.93 ? 35 VAL A CG1 1 +ATOM 278 C CG2 . VAL A 1 35 ? 17.519 -20.750 11.384 1.00 14.17 ? 35 VAL A CG2 1 +ATOM 279 N N . VAL A 1 36 ? 13.699 -18.861 13.164 1.00 11.24 ? 36 VAL A N 1 +ATOM 280 C CA . VAL A 1 36 ? 12.775 -17.774 13.408 1.00 11.41 ? 36 VAL A CA 1 +ATOM 281 C C . VAL A 1 36 ? 13.589 -16.584 13.895 1.00 11.05 ? 36 VAL A C 1 +ATOM 282 O O . VAL A 1 36 ? 14.339 -16.704 14.855 1.00 10.78 ? 36 VAL A O 1 +ATOM 283 C CB . VAL A 1 36 ? 11.676 -18.169 14.404 1.00 12.20 ? 36 VAL A CB 1 +ATOM 284 C CG1 . VAL A 1 36 ? 10.833 -16.957 14.781 1.00 12.52 ? 36 VAL A CG1 1 +ATOM 285 C CG2 . VAL A 1 36 ? 10.810 -19.281 13.826 1.00 12.70 ? 36 VAL A CG2 1 +ATOM 286 N N . TYR A 1 37 ? 13.465 -15.444 13.220 1.00 11.02 ? 37 TYR A N 1 +ATOM 287 C CA . TYR A 1 37 ? 14.205 -14.229 13.566 1.00 10.75 ? 37 TYR A CA 1 +ATOM 288 C C . TYR A 1 37 ? 13.256 -13.286 14.257 1.00 11.13 ? 37 TYR A C 1 +ATOM 289 O O . TYR A 1 37 ? 12.130 -13.095 13.787 1.00 11.97 ? 37 TYR A O 1 +ATOM 290 C CB . TYR A 1 37 ? 14.693 -13.529 12.285 1.00 10.59 ? 37 TYR A CB 1 +ATOM 291 C CG . TYR A 1 37 ? 15.597 -14.400 11.453 1.00 11.51 ? 37 TYR A CG 1 +ATOM 292 C CD1 . TYR A 1 37 ? 15.076 -15.318 10.558 1.00 12.49 ? 37 TYR A CD1 1 +ATOM 293 C CD2 . TYR A 1 37 ? 16.974 -14.306 11.565 1.00 12.68 ? 37 TYR A CD2 1 +ATOM 294 C CE1 . TYR A 1 37 ? 15.904 -16.163 9.830 1.00 13.67 ? 37 TYR A CE1 1 +ATOM 295 C CE2 . TYR A 1 37 ? 17.814 -15.115 10.809 1.00 13.61 ? 37 TYR A CE2 1 +ATOM 296 C CZ . TYR A 1 37 ? 17.275 -16.032 9.932 1.00 14.78 ? 37 TYR A CZ 1 +ATOM 297 O OH . TYR A 1 37 ? 18.101 -16.885 9.229 1.00 17.25 ? 37 TYR A OH 1 +ATOM 298 N N . CYS A 1 38 ? 13.677 -12.713 15.375 1.00 10.69 ? 38 CYS A N 1 +ATOM 299 C CA . CYS A 1 38 ? 12.825 -11.757 16.071 1.00 10.98 ? 38 CYS A CA 1 +ATOM 300 C C . CYS A 1 38 ? 13.672 -10.755 16.841 1.00 11.25 ? 38 CYS A C 1 +ATOM 301 O O . CYS A 1 38 ? 14.846 -11.012 17.094 1.00 11.69 ? 38 CYS A O 1 +ATOM 302 C CB . CYS A 1 38 ? 11.815 -12.484 16.958 1.00 11.60 ? 38 CYS A CB 1 +ATOM 303 S SG . CYS A 1 38 ? 12.515 -13.143 18.487 1.00 13.48 ? 38 CYS A SG 1 +ATOM 304 N N . PRO A 1 39 ? 13.111 -9.604 17.244 1.00 10.96 ? 39 PRO A N 1 +ATOM 305 C CA . PRO A 1 39 ? 13.899 -8.651 18.033 1.00 10.74 ? 39 PRO A CA 1 +ATOM 306 C C . PRO A 1 39 ? 14.331 -9.281 19.350 1.00 11.52 ? 39 PRO A C 1 +ATOM 307 O O . PRO A 1 39 ? 13.544 -9.987 19.992 1.00 12.03 ? 39 PRO A O 1 +ATOM 308 C CB . PRO A 1 39 ? 12.903 -7.512 18.282 1.00 11.14 ? 39 PRO A CB 1 +ATOM 309 C CG . PRO A 1 39 ? 11.956 -7.602 17.126 1.00 11.48 ? 39 PRO A CG 1 +ATOM 310 C CD . PRO A 1 39 ? 11.753 -9.084 16.998 1.00 10.66 ? 39 PRO A CD 1 +ATOM 311 N N . ARG A 1 40 ? 15.581 -9.024 19.762 1.00 11.03 ? 40 ARG A N 1 +ATOM 312 C CA . ARG A 1 40 ? 16.049 -9.593 21.020 1.00 11.30 ? 40 ARG A CA 1 +ATOM 313 C C . ARG A 1 40 ? 15.284 -9.013 22.218 1.00 12.95 ? 40 ARG A C 1 +ATOM 314 O O . ARG A 1 40 ? 15.228 -9.680 23.250 1.00 13.60 ? 40 ARG A O 1 +ATOM 315 C CB . ARG A 1 40 ? 17.549 -9.444 21.184 1.00 11.64 ? 40 ARG A CB 1 +ATOM 316 C CG . ARG A 1 40 ? 17.977 -8.012 21.332 1.00 12.88 ? 40 ARG A CG 1 +ATOM 317 C CD . ARG A 1 40 ? 19.457 -7.968 21.572 1.00 13.12 ? 40 ARG A CD 1 +ATOM 318 N NE . ARG A 1 40 ? 19.935 -6.599 21.666 1.00 14.21 ? 40 ARG A NE 1 +ATOM 319 C CZ . ARG A 1 40 ? 21.174 -6.261 21.996 1.00 15.68 ? 40 ARG A CZ 1 +ATOM 320 N NH1 . ARG A 1 40 ? 22.082 -7.197 22.248 1.00 15.22 ? 40 ARG A NH1 1 +ATOM 321 N NH2 . ARG A 1 40 ? 21.519 -4.983 22.070 1.00 15.20 ? 40 ARG A NH2 1 +ATOM 322 N N . HIS A 1 41 ? 14.628 -7.836 22.073 1.00 13.07 ? 41 HIS A N 1 +ATOM 323 C CA . HIS A 1 41 ? 13.892 -7.269 23.196 1.00 13.76 ? 41 HIS A CA 1 +ATOM 324 C C . HIS A 1 41 ? 12.612 -8.048 23.529 1.00 14.57 ? 41 HIS A C 1 +ATOM 325 O O . HIS A 1 41 ? 11.970 -7.700 24.519 1.00 14.99 ? 41 HIS A O 1 +ATOM 326 C CB . HIS A 1 41 ? 13.651 -5.754 23.097 1.00 14.02 ? 41 HIS A CB 1 +ATOM 327 C CG . HIS A 1 41 ? 12.654 -5.295 22.083 1.00 16.36 ? 41 HIS A CG 1 +ATOM 328 N ND1 . HIS A 1 41 ? 11.296 -5.507 22.253 1.00 19.44 ? 41 HIS A ND1 1 +ATOM 329 C CD2 . HIS A 1 41 ? 12.838 -4.516 20.993 1.00 17.15 ? 41 HIS A CD2 1 +ATOM 330 C CE1 . HIS A 1 41 ? 10.708 -4.914 21.223 1.00 19.39 ? 41 HIS A CE1 1 +ATOM 331 N NE2 . HIS A 1 41 ? 11.596 -4.303 20.441 1.00 18.52 ? 41 HIS A NE2 1 +ATOM 332 N N . VAL A 1 42 ? 12.320 -9.175 22.827 1.00 14.08 ? 42 VAL A N 1 +ATOM 333 C CA . VAL A 1 42 ? 11.239 -10.064 23.272 1.00 14.58 ? 42 VAL A CA 1 +ATOM 334 C C . VAL A 1 42 ? 11.547 -10.606 24.697 1.00 15.27 ? 42 VAL A C 1 +ATOM 335 O O . VAL A 1 42 ? 10.628 -10.903 25.447 1.00 16.44 ? 42 VAL A O 1 +ATOM 336 C CB . VAL A 1 42 ? 10.982 -11.221 22.276 1.00 14.96 ? 42 VAL A CB 1 +ATOM 337 C CG1 . VAL A 1 42 ? 12.125 -12.225 22.274 1.00 14.97 ? 42 VAL A CG1 1 +ATOM 338 C CG2 . VAL A 1 42 ? 9.651 -11.914 22.559 1.00 15.69 ? 42 VAL A CG2 1 +ATOM 339 N N . ILE A 1 43 ? 12.839 -10.667 25.091 1.00 14.68 ? 43 ILE A N 1 +ATOM 340 C CA . ILE A 1 43 ? 13.211 -11.149 26.424 1.00 15.70 ? 43 ILE A CA 1 +ATOM 341 C C . ILE A 1 43 ? 13.082 -10.078 27.518 1.00 18.13 ? 43 ILE A C 1 +ATOM 342 O O . ILE A 1 43 ? 13.347 -10.366 28.682 1.00 18.87 ? 43 ILE A O 1 +ATOM 343 C CB . ILE A 1 43 ? 14.635 -11.767 26.406 1.00 15.42 ? 43 ILE A CB 1 +ATOM 344 C CG1 . ILE A 1 43 ? 15.718 -10.687 26.276 1.00 15.89 ? 43 ILE A CG1 1 +ATOM 345 C CG2 . ILE A 1 43 ? 14.757 -12.817 25.294 1.00 15.89 ? 43 ILE A CG2 1 +ATOM 346 C CD1 . ILE A 1 43 ? 17.155 -11.214 26.301 1.00 17.16 ? 43 ILE A CD1 1 +ATOM 347 N N . CYS A 1 44 ? 12.700 -8.851 27.161 1.00 19.70 ? 44 CYS A N 1 +ATOM 348 C CA . CYS A 1 44 ? 12.587 -7.761 28.109 1.00 22.56 ? 44 CYS A CA 1 +ATOM 349 C C . CYS A 1 44 ? 11.166 -7.545 28.562 1.00 26.82 ? 44 CYS A C 1 +ATOM 350 O O . CYS A 1 44 ? 10.221 -7.737 27.806 1.00 27.66 ? 44 CYS A O 1 +ATOM 351 C CB . CYS A 1 44 ? 13.121 -6.476 27.485 1.00 22.30 ? 44 CYS A CB 1 +ATOM 352 S SG . CYS A 1 44 ? 14.871 -6.530 27.050 1.00 22.16 ? 44 CYS A SG 1 +ATOM 353 N N . THR A 1 45 ? 11.039 -7.011 29.755 1.00 29.51 ? 45 THR A N 1 +ATOM 354 C CA . THR A 1 45 ? 9.787 -6.494 30.270 1.00 32.18 ? 45 THR A CA 1 +ATOM 355 C C . THR A 1 45 ? 9.827 -4.970 29.895 1.00 34.36 ? 45 THR A C 1 +ATOM 356 O O . THR A 1 45 ? 10.846 -4.488 29.368 1.00 34.59 ? 45 THR A O 1 +ATOM 357 C CB . THR A 1 45 ? 9.740 -6.707 31.794 1.00 34.04 ? 45 THR A CB 1 +ATOM 358 O OG1 . THR A 1 45 ? 10.699 -5.849 32.419 1.00 35.60 ? 45 THR A OG1 1 +ATOM 359 C CG2 . THR A 1 45 ? 10.010 -8.155 32.194 1.00 34.58 ? 45 THR A CG2 1 +ATOM 360 N N . SER A 1 46 ? 8.754 -4.205 30.188 1.00 35.48 ? 46 SER A N 1 +ATOM 361 C CA . SER A 1 46 ? 8.778 -2.760 29.936 1.00 36.69 ? 46 SER A CA 1 +ATOM 362 C C . SER A 1 46 ? 9.855 -2.090 30.824 1.00 37.23 ? 46 SER A C 1 +ATOM 363 O O . SER A 1 46 ? 10.511 -1.144 30.383 1.00 37.54 ? 46 SER A O 1 +ATOM 364 C CB . SER A 1 46 ? 7.409 -2.137 30.185 1.00 38.60 ? 46 SER A CB 1 +ATOM 365 O OG . SER A 1 46 ? 7.293 -0.915 29.474 1.00 42.31 ? 46 SER A OG 1 +ATOM 366 N N . GLU A 1 47 ? 10.064 -2.620 32.051 1.00 37.15 ? 47 GLU A N 1 +ATOM 367 C CA . GLU A 1 47 ? 11.067 -2.151 33.007 1.00 37.30 ? 47 GLU A CA 1 +ATOM 368 C C . GLU A 1 47 ? 12.485 -2.408 32.486 1.00 36.61 ? 47 GLU A C 1 +ATOM 369 O O . GLU A 1 47 ? 13.323 -1.506 32.541 1.00 37.19 ? 47 GLU A O 1 +ATOM 370 C CB . GLU A 1 47 ? 10.871 -2.832 34.379 1.00 40.16 ? 47 GLU A CB 1 +ATOM 371 C CG . GLU A 1 47 ? 11.899 -2.401 35.412 1.00 46.08 ? 47 GLU A CG 1 +ATOM 372 C CD . GLU A 1 47 ? 11.871 -3.137 36.739 1.00 53.53 ? 47 GLU A CD 1 +ATOM 373 O OE1 . GLU A 1 47 ? 11.167 -4.168 36.840 1.00 55.04 ? 47 GLU A OE1 1 +ATOM 374 O OE2 . GLU A 1 47 ? 12.559 -2.680 37.681 1.00 56.09 ? 47 GLU A OE2 1 +ATOM 375 N N . ASP A 1 48 ? 12.752 -3.629 31.971 1.00 35.12 ? 48 ASP A N 1 +ATOM 376 C CA . ASP A 1 48 ? 14.071 -3.994 31.442 1.00 34.07 ? 48 ASP A CA 1 +ATOM 377 C C . ASP A 1 48 ? 14.517 -3.050 30.338 1.00 32.73 ? 48 ASP A C 1 +ATOM 378 O O . ASP A 1 48 ? 15.695 -2.736 30.268 1.00 32.68 ? 48 ASP A O 1 +ATOM 379 C CB . ASP A 1 48 ? 14.089 -5.430 30.884 1.00 35.22 ? 48 ASP A CB 1 +ATOM 380 C CG . ASP A 1 48 ? 14.024 -6.544 31.907 1.00 39.53 ? 48 ASP A CG 1 +ATOM 381 O OD1 . ASP A 1 48 ? 14.540 -6.353 33.029 1.00 39.78 ? 48 ASP A OD1 1 +ATOM 382 O OD2 . ASP A 1 48 ? 13.467 -7.614 31.581 1.00 41.68 ? 48 ASP A OD2 1 +ATOM 383 N N . MET A 1 49 ? 13.587 -2.587 29.486 1.00 31.75 ? 49 MET A N 1 +ATOM 384 C CA . MET A 1 49 ? 13.915 -1.698 28.369 1.00 31.02 ? 49 MET A CA 1 +ATOM 385 C C . MET A 1 49 ? 14.627 -0.405 28.761 1.00 30.28 ? 49 MET A C 1 +ATOM 386 O O . MET A 1 49 ? 15.313 0.164 27.924 1.00 29.65 ? 49 MET A O 1 +ATOM 387 C CB . MET A 1 49 ? 12.679 -1.384 27.513 1.00 31.35 ? 49 MET A CB 1 +ATOM 388 C CG . MET A 1 49 ? 12.174 -2.572 26.724 1.00 32.65 ? 49 MET A CG 1 +ATOM 389 S SD . MET A 1 49 ? 13.436 -3.315 25.650 1.00 33.34 ? 49 MET A SD 1 +ATOM 390 C CE . MET A 1 49 ? 13.560 -2.060 24.368 1.00 27.71 ? 49 MET A CE 1 +ATOM 391 N N . LEU A 1 50 ? 14.493 0.050 30.009 1.00 30.11 ? 50 LEU A N 1 +ATOM 392 C CA . LEU A 1 50 ? 15.162 1.274 30.453 1.00 30.70 ? 50 LEU A CA 1 +ATOM 393 C C . LEU A 1 50 ? 16.689 1.159 30.403 1.00 30.56 ? 50 LEU A C 1 +ATOM 394 O O . LEU A 1 50 ? 17.345 2.089 29.955 1.00 31.26 ? 50 LEU A O 1 +ATOM 395 C CB . LEU A 1 50 ? 14.682 1.683 31.851 1.00 31.34 ? 50 LEU A CB 1 +ATOM 396 C CG . LEU A 1 50 ? 13.191 1.988 31.949 1.00 33.68 ? 50 LEU A CG 1 +ATOM 397 C CD1 . LEU A 1 50 ? 12.778 2.229 33.387 1.00 34.43 ? 50 LEU A CD1 1 +ATOM 398 C CD2 . LEU A 1 50 ? 12.806 3.173 31.059 1.00 34.52 ? 50 LEU A CD2 1 +ATOM 399 N N . ASN A 1 51 ? 17.251 0.022 30.820 1.00 29.29 ? 51 ASN A N 1 +ATOM 400 C CA . ASN A 1 51 ? 18.701 -0.204 30.771 1.00 28.56 ? 51 ASN A CA 1 +ATOM 401 C C . ASN A 1 51 ? 18.964 -1.718 30.692 1.00 26.51 ? 51 ASN A C 1 +ATOM 402 O O . ASN A 1 51 ? 19.400 -2.327 31.674 1.00 26.96 ? 51 ASN A O 1 +ATOM 403 C CB . ASN A 1 51 ? 19.381 0.398 32.009 1.00 30.92 ? 51 ASN A CB 1 +ATOM 404 C CG . ASN A 1 51 ? 20.892 0.388 31.942 1.00 35.07 ? 51 ASN A CG 1 +ATOM 405 O OD1 . ASN A 1 51 ? 21.493 0.225 30.873 1.00 36.86 ? 51 ASN A OD1 1 +ATOM 406 N ND2 . ASN A 1 51 ? 21.539 0.567 33.085 1.00 36.16 ? 51 ASN A ND2 1 +ATOM 407 N N . PRO A 1 52 ? 18.640 -2.362 29.557 1.00 23.74 ? 52 PRO A N 1 +ATOM 408 C CA . PRO A 1 52 ? 18.791 -3.824 29.494 1.00 22.58 ? 52 PRO A CA 1 +ATOM 409 C C . PRO A 1 52 ? 20.203 -4.339 29.261 1.00 21.84 ? 52 PRO A C 1 +ATOM 410 O O . PRO A 1 52 ? 20.938 -3.775 28.461 1.00 23.02 ? 52 PRO A O 1 +ATOM 411 C CB . PRO A 1 52 ? 17.858 -4.228 28.347 1.00 23.00 ? 52 PRO A CB 1 +ATOM 412 C CG . PRO A 1 52 ? 17.799 -3.012 27.462 1.00 23.84 ? 52 PRO A CG 1 +ATOM 413 C CD . PRO A 1 52 ? 18.087 -1.804 28.306 1.00 23.00 ? 52 PRO A CD 1 +ATOM 414 N N . ASN A 1 53 ? 20.579 -5.426 29.948 1.00 20.08 ? 53 ASN A N 1 +ATOM 415 C CA . ASN A 1 53 ? 21.843 -6.098 29.676 1.00 19.44 ? 53 ASN A CA 1 +ATOM 416 C C . ASN A 1 53 ? 21.378 -7.382 29.004 1.00 19.09 ? 53 ASN A C 1 +ATOM 417 O O . ASN A 1 53 ? 20.976 -8.328 29.682 1.00 19.86 ? 53 ASN A O 1 +ATOM 418 C CB . ASN A 1 53 ? 22.650 -6.418 30.934 1.00 20.41 ? 53 ASN A CB 1 +ATOM 419 C CG . ASN A 1 53 ? 24.001 -6.990 30.569 1.00 23.36 ? 53 ASN A CG 1 +ATOM 420 O OD1 . ASN A 1 53 ? 24.112 -7.970 29.818 1.00 24.42 ? 53 ASN A OD1 1 +ATOM 421 N ND2 . ASN A 1 53 ? 25.063 -6.397 31.086 1.00 23.75 ? 53 ASN A ND2 1 +ATOM 422 N N . TYR A 1 54 ? 21.348 -7.382 27.684 1.00 18.47 ? 54 TYR A N 1 +ATOM 423 C CA . TYR A 1 54 ? 20.814 -8.489 26.923 1.00 17.26 ? 54 TYR A CA 1 +ATOM 424 C C . TYR A 1 54 ? 21.500 -9.801 27.153 1.00 17.52 ? 54 TYR A C 1 +ATOM 425 O O . TYR A 1 54 ? 20.800 -10.791 27.331 1.00 17.53 ? 54 TYR A O 1 +ATOM 426 C CB . TYR A 1 54 ? 20.781 -8.147 25.448 1.00 15.88 ? 54 TYR A CB 1 +ATOM 427 C CG . TYR A 1 54 ? 19.666 -7.180 25.141 1.00 15.71 ? 54 TYR A CG 1 +ATOM 428 C CD1 . TYR A 1 54 ? 18.353 -7.614 25.039 1.00 16.04 ? 54 TYR A CD1 1 +ATOM 429 C CD2 . TYR A 1 54 ? 19.916 -5.823 25.004 1.00 15.93 ? 54 TYR A CD2 1 +ATOM 430 C CE1 . TYR A 1 54 ? 17.320 -6.725 24.759 1.00 16.34 ? 54 TYR A CE1 1 +ATOM 431 C CE2 . TYR A 1 54 ? 18.897 -4.929 24.714 1.00 16.57 ? 54 TYR A CE2 1 +ATOM 432 C CZ . TYR A 1 54 ? 17.596 -5.382 24.598 1.00 17.28 ? 54 TYR A CZ 1 +ATOM 433 O OH . TYR A 1 54 ? 16.582 -4.489 24.330 1.00 18.46 ? 54 TYR A OH 1 +ATOM 434 N N . GLU A 1 55 ? 22.849 -9.837 27.217 1.00 18.17 ? 55 GLU A N 1 +ATOM 435 C CA . GLU A 1 55 ? 23.536 -11.110 27.478 1.00 18.88 ? 55 GLU A CA 1 +ATOM 436 C C . GLU A 1 55 ? 23.132 -11.677 28.833 1.00 19.05 ? 55 GLU A C 1 +ATOM 437 O O . GLU A 1 55 ? 22.911 -12.883 28.953 1.00 19.30 ? 55 GLU A O 1 +ATOM 438 C CB . GLU A 1 55 ? 25.069 -10.991 27.409 1.00 22.09 ? 55 GLU A CB 1 +ATOM 439 C CG . GLU A 1 55 ? 25.638 -10.894 26.003 1.00 27.99 ? 55 GLU A CG 1 +ATOM 440 C CD . GLU A 1 55 ? 25.669 -12.141 25.133 1.00 34.81 ? 55 GLU A CD 1 +ATOM 441 O OE1 . GLU A 1 55 ? 25.127 -13.194 25.538 1.00 33.74 ? 55 GLU A OE1 1 +ATOM 442 O OE2 . GLU A 1 55 ? 26.209 -12.043 24.007 1.00 39.00 ? 55 GLU A OE2 1 +ATOM 443 N N . ASP A 1 56 ? 22.991 -10.802 29.841 1.00 18.58 ? 56 ASP A N 1 +ATOM 444 C CA . ASP A 1 56 ? 22.594 -11.263 31.171 1.00 18.89 ? 56 ASP A CA 1 +ATOM 445 C C . ASP A 1 56 ? 21.151 -11.742 31.203 1.00 19.04 ? 56 ASP A C 1 +ATOM 446 O O . ASP A 1 56 ? 20.872 -12.782 31.794 1.00 20.06 ? 56 ASP A O 1 +ATOM 447 C CB . ASP A 1 56 ? 22.838 -10.181 32.232 1.00 20.13 ? 56 ASP A CB 1 +ATOM 448 C CG . ASP A 1 56 ? 24.304 -9.937 32.525 1.00 23.92 ? 56 ASP A CG 1 +ATOM 449 O OD1 . ASP A 1 56 ? 25.133 -10.830 32.216 1.00 23.66 ? 56 ASP A OD1 1 +ATOM 450 O OD2 . ASP A 1 56 ? 24.630 -8.853 33.067 1.00 25.46 ? 56 ASP A OD2 1 +ATOM 451 N N . LEU A 1 57 ? 20.235 -11.002 30.566 1.00 18.53 ? 57 LEU A N 1 +ATOM 452 C CA . LEU A 1 57 ? 18.835 -11.405 30.531 1.00 18.71 ? 57 LEU A CA 1 +ATOM 453 C C . LEU A 1 57 ? 18.663 -12.733 29.781 1.00 18.63 ? 57 LEU A C 1 +ATOM 454 O O . LEU A 1 57 ? 17.847 -13.565 30.166 1.00 18.76 ? 57 LEU A O 1 +ATOM 455 C CB . LEU A 1 57 ? 17.989 -10.323 29.851 1.00 19.11 ? 57 LEU A CB 1 +ATOM 456 C CG . LEU A 1 57 ? 17.861 -9.013 30.615 1.00 21.19 ? 57 LEU A CG 1 +ATOM 457 C CD1 . LEU A 1 57 ? 17.170 -7.968 29.770 1.00 22.03 ? 57 LEU A CD1 1 +ATOM 458 C CD2 . LEU A 1 57 ? 17.084 -9.216 31.913 1.00 22.04 ? 57 LEU A CD2 1 +ATOM 459 N N . LEU A 1 58 ? 19.446 -12.932 28.724 1.00 17.87 ? 58 LEU A N 1 +ATOM 460 C CA . LEU A 1 58 ? 19.353 -14.126 27.908 1.00 18.31 ? 58 LEU A CA 1 +ATOM 461 C C . LEU A 1 58 ? 19.824 -15.379 28.634 1.00 18.99 ? 58 LEU A C 1 +ATOM 462 O O . LEU A 1 58 ? 19.291 -16.458 28.361 1.00 19.97 ? 58 LEU A O 1 +ATOM 463 C CB . LEU A 1 58 ? 20.098 -13.912 26.579 1.00 18.33 ? 58 LEU A CB 1 +ATOM 464 C CG . LEU A 1 58 ? 19.768 -14.878 25.447 1.00 19.20 ? 58 LEU A CG 1 +ATOM 465 C CD1 . LEU A 1 58 ? 18.284 -14.903 25.133 1.00 18.38 ? 58 LEU A CD1 1 +ATOM 466 C CD2 . LEU A 1 58 ? 20.620 -14.581 24.225 1.00 20.01 ? 58 LEU A CD2 1 +ATOM 467 N N . ILE A 1 59 ? 20.748 -15.251 29.613 1.00 18.93 ? 59 ILE A N 1 +ATOM 468 C CA . ILE A 1 59 ? 21.213 -16.402 30.410 1.00 20.28 ? 59 ILE A CA 1 +ATOM 469 C C . ILE A 1 59 ? 20.039 -17.065 31.138 1.00 20.86 ? 59 ILE A C 1 +ATOM 470 O O . ILE A 1 59 ? 20.042 -18.276 31.340 1.00 21.11 ? 59 ILE A O 1 +ATOM 471 C CB . ILE A 1 59 ? 22.308 -15.997 31.439 1.00 22.03 ? 59 ILE A CB 1 +ATOM 472 C CG1 . ILE A 1 59 ? 23.587 -15.552 30.751 1.00 24.25 ? 59 ILE A CG1 1 +ATOM 473 C CG2 . ILE A 1 59 ? 22.606 -17.132 32.438 1.00 23.10 ? 59 ILE A CG2 1 +ATOM 474 C CD1 . ILE A 1 59 ? 24.600 -14.933 31.734 1.00 26.45 ? 59 ILE A CD1 1 +ATOM 475 N N . ARG A 1 60 ? 19.043 -16.267 31.544 1.00 21.21 ? 60 ARG A N 1 +ATOM 476 C CA . ARG A 1 60 ? 17.885 -16.790 32.250 1.00 22.07 ? 60 ARG A CA 1 +ATOM 477 C C . ARG A 1 60 ? 16.844 -17.440 31.336 1.00 21.30 ? 60 ARG A C 1 +ATOM 478 O O . ARG A 1 60 ? 15.812 -17.882 31.826 1.00 22.28 ? 60 ARG A O 1 +ATOM 479 C CB . ARG A 1 60 ? 17.247 -15.694 33.120 1.00 24.65 ? 60 ARG A CB 1 +ATOM 480 C CG . ARG A 1 60 ? 18.246 -14.947 33.999 1.00 29.44 ? 60 ARG A CG 1 +ATOM 481 C CD . ARG A 1 60 ? 18.917 -15.852 35.008 1.00 33.62 ? 60 ARG A CD 1 +ATOM 482 N NE . ARG A 1 60 ? 20.227 -15.335 35.399 1.00 37.98 ? 60 ARG A NE 1 +ATOM 483 C CZ . ARG A 1 60 ? 21.142 -16.030 36.067 1.00 40.16 ? 60 ARG A CZ 1 +ATOM 484 N NH1 . ARG A 1 60 ? 22.307 -15.479 36.372 1.00 39.79 ? 60 ARG A NH1 1 +ATOM 485 N NH2 . ARG A 1 60 ? 20.898 -17.284 36.432 1.00 40.17 ? 60 ARG A NH2 1 +ATOM 486 N N . LYS A 1 61 ? 17.089 -17.491 30.014 1.00 19.36 ? 61 LYS A N 1 +ATOM 487 C CA . LYS A 1 61 ? 16.134 -18.067 29.078 1.00 18.81 ? 61 LYS A CA 1 +ATOM 488 C C . LYS A 1 61 ? 16.645 -19.373 28.501 1.00 19.17 ? 61 LYS A C 1 +ATOM 489 O O . LYS A 1 61 ? 17.832 -19.513 28.216 1.00 20.35 ? 61 LYS A O 1 +ATOM 490 C CB . LYS A 1 61 ? 15.853 -17.072 27.936 1.00 19.82 ? 61 LYS A CB 1 +ATOM 491 C CG . LYS A 1 61 ? 15.324 -15.717 28.401 1.00 22.51 ? 61 LYS A CG 1 +ATOM 492 C CD . LYS A 1 61 ? 14.023 -15.821 29.196 1.00 26.00 ? 61 LYS A CD 1 +ATOM 493 C CE . LYS A 1 61 ? 13.493 -14.456 29.568 1.00 29.36 ? 61 LYS A CE 1 +ATOM 494 N NZ . LYS A 1 61 ? 12.260 -14.538 30.405 1.00 32.04 ? 61 LYS A NZ 1 +ATOM 495 N N . SER A 1 62 ? 15.745 -20.338 28.359 1.00 17.84 ? 62 SER A N 1 +ATOM 496 C CA . SER A 1 62 ? 16.030 -21.625 27.751 1.00 17.70 ? 62 SER A CA 1 +ATOM 497 C C . SER A 1 62 ? 15.168 -21.747 26.476 1.00 16.11 ? 62 SER A C 1 +ATOM 498 O O . SER A 1 62 ? 14.219 -20.985 26.286 1.00 15.44 ? 62 SER A O 1 +ATOM 499 C CB . SER A 1 62 ? 15.673 -22.756 28.709 1.00 20.52 ? 62 SER A CB 1 +ATOM 500 O OG . SER A 1 62 ? 16.454 -22.685 29.891 1.00 23.82 ? 62 SER A OG 1 +ATOM 501 N N . ASN A 1 63 ? 15.466 -22.730 25.611 1.00 15.74 ? 63 ASN A N 1 +ATOM 502 C CA . ASN A 1 63 ? 14.663 -22.963 24.399 1.00 15.24 ? 63 ASN A CA 1 +ATOM 503 C C . ASN A 1 63 ? 13.166 -23.023 24.663 1.00 15.14 ? 63 ASN A C 1 +ATOM 504 O O . ASN A 1 63 ? 12.399 -22.427 23.914 1.00 15.00 ? 63 ASN A O 1 +ATOM 505 C CB . ASN A 1 63 ? 15.077 -24.261 23.732 1.00 15.61 ? 63 ASN A CB 1 +ATOM 506 C CG . ASN A 1 63 ? 16.449 -24.203 23.162 1.00 17.36 ? 63 ASN A CG 1 +ATOM 507 O OD1 . ASN A 1 63 ? 16.926 -23.144 22.757 1.00 17.17 ? 63 ASN A OD1 1 +ATOM 508 N ND2 . ASN A 1 63 ? 17.110 -25.341 23.087 1.00 17.34 ? 63 ASN A ND2 1 +ATOM 509 N N . HIS A 1 64 ? 12.750 -23.729 25.736 1.00 15.18 ? 64 HIS A N 1 +ATOM 510 C CA . HIS A 1 64 ? 11.332 -23.876 26.064 1.00 15.34 ? 64 HIS A CA 1 +ATOM 511 C C . HIS A 1 64 ? 10.643 -22.586 26.518 1.00 15.59 ? 64 HIS A C 1 +ATOM 512 O O . HIS A 1 64 ? 9.414 -22.564 26.635 1.00 16.33 ? 64 HIS A O 1 +ATOM 513 C CB . HIS A 1 64 ? 11.090 -25.001 27.087 1.00 16.13 ? 64 HIS A CB 1 +ATOM 514 C CG . HIS A 1 64 ? 11.550 -24.698 28.481 1.00 17.26 ? 64 HIS A CG 1 +ATOM 515 N ND1 . HIS A 1 64 ? 12.805 -25.063 28.912 1.00 18.51 ? 64 HIS A ND1 1 +ATOM 516 C CD2 . HIS A 1 64 ? 10.890 -24.109 29.506 1.00 18.35 ? 64 HIS A CD2 1 +ATOM 517 C CE1 . HIS A 1 64 ? 12.887 -24.663 30.171 1.00 18.91 ? 64 HIS A CE1 1 +ATOM 518 N NE2 . HIS A 1 64 ? 11.768 -24.069 30.566 1.00 19.00 ? 64 HIS A NE2 1 +ATOM 519 N N . ASN A 1 65 ? 11.413 -21.525 26.808 1.00 14.89 ? 65 ASN A N 1 +ATOM 520 C CA . ASN A 1 65 ? 10.825 -20.244 27.197 1.00 15.45 ? 65 ASN A CA 1 +ATOM 521 C C . ASN A 1 65 ? 10.364 -19.437 25.979 1.00 15.62 ? 65 ASN A C 1 +ATOM 522 O O . ASN A 1 65 ? 9.615 -18.487 26.144 1.00 16.44 ? 65 ASN A O 1 +ATOM 523 C CB . ASN A 1 65 ? 11.814 -19.399 27.993 1.00 16.32 ? 65 ASN A CB 1 +ATOM 524 C CG . ASN A 1 65 ? 12.130 -19.936 29.354 1.00 20.06 ? 65 ASN A CG 1 +ATOM 525 O OD1 . ASN A 1 65 ? 13.288 -19.972 29.757 1.00 21.53 ? 65 ASN A OD1 1 +ATOM 526 N ND2 . ASN A 1 65 ? 11.113 -20.354 30.094 1.00 20.32 ? 65 ASN A ND2 1 +ATOM 527 N N . PHE A 1 66 ? 10.834 -19.782 24.766 1.00 14.81 ? 66 PHE A N 1 +ATOM 528 C CA . PHE A 1 66 ? 10.445 -19.072 23.556 1.00 14.55 ? 66 PHE A CA 1 +ATOM 529 C C . PHE A 1 66 ? 9.285 -19.790 22.901 1.00 15.70 ? 66 PHE A C 1 +ATOM 530 O O . PHE A 1 66 ? 9.473 -20.833 22.284 1.00 17.06 ? 66 PHE A O 1 +ATOM 531 C CB . PHE A 1 66 ? 11.624 -18.973 22.581 1.00 13.81 ? 66 PHE A CB 1 +ATOM 532 C CG . PHE A 1 66 ? 12.755 -18.158 23.140 1.00 14.30 ? 66 PHE A CG 1 +ATOM 533 C CD1 . PHE A 1 66 ? 12.739 -16.779 23.058 1.00 15.07 ? 66 PHE A CD1 1 +ATOM 534 C CD2 . PHE A 1 66 ? 13.840 -18.771 23.734 1.00 14.97 ? 66 PHE A CD2 1 +ATOM 535 C CE1 . PHE A 1 66 ? 13.791 -16.027 23.574 1.00 15.66 ? 66 PHE A CE1 1 +ATOM 536 C CE2 . PHE A 1 66 ? 14.884 -18.017 24.257 1.00 15.64 ? 66 PHE A CE2 1 +ATOM 537 C CZ . PHE A 1 66 ? 14.840 -16.648 24.190 1.00 15.18 ? 66 PHE A CZ 1 +ATOM 538 N N . LEU A 1 67 ? 8.095 -19.249 23.059 1.00 14.73 ? 67 LEU A N 1 +ATOM 539 C CA . LEU A 1 67 ? 6.890 -19.851 22.496 1.00 15.02 ? 67 LEU A CA 1 +ATOM 540 C C . LEU A 1 67 ? 6.660 -19.315 21.087 1.00 14.82 ? 67 LEU A C 1 +ATOM 541 O O . LEU A 1 67 ? 6.407 -18.125 20.903 1.00 14.57 ? 67 LEU A O 1 +ATOM 542 C CB . LEU A 1 67 ? 5.687 -19.563 23.389 1.00 16.22 ? 67 LEU A CB 1 +ATOM 543 C CG . LEU A 1 67 ? 5.825 -20.012 24.845 1.00 19.15 ? 67 LEU A CG 1 +ATOM 544 C CD1 . LEU A 1 67 ? 4.603 -19.600 25.664 1.00 20.19 ? 67 LEU A CD1 1 +ATOM 545 C CD2 . LEU A 1 67 ? 6.082 -21.512 24.947 1.00 20.70 ? 67 LEU A CD2 1 +ATOM 546 N N . VAL A 1 68 ? 6.797 -20.185 20.094 1.00 13.69 ? 68 VAL A N 1 +ATOM 547 C CA . VAL A 1 68 ? 6.672 -19.779 18.702 1.00 13.84 ? 68 VAL A CA 1 +ATOM 548 C C . VAL A 1 68 ? 5.478 -20.455 18.106 1.00 14.57 ? 68 VAL A C 1 +ATOM 549 O O . VAL A 1 68 ? 5.380 -21.671 18.188 1.00 14.93 ? 68 VAL A O 1 +ATOM 550 C CB . VAL A 1 68 ? 7.958 -20.136 17.936 1.00 14.82 ? 68 VAL A CB 1 +ATOM 551 C CG1 . VAL A 1 68 ? 7.847 -19.711 16.467 1.00 14.89 ? 68 VAL A CG1 1 +ATOM 552 C CG2 . VAL A 1 68 ? 9.173 -19.485 18.597 1.00 15.58 ? 68 VAL A CG2 1 +ATOM 553 N N . GLN A 1 69 ? 4.540 -19.672 17.571 1.00 14.79 ? 69 GLN A N 1 +ATOM 554 C CA . GLN A 1 69 ? 3.320 -20.238 17.038 1.00 16.19 ? 69 GLN A CA 1 +ATOM 555 C C . GLN A 1 69 ? 3.083 -19.685 15.636 1.00 17.21 ? 69 GLN A C 1 +ATOM 556 O O . GLN A 1 69 ? 3.122 -18.475 15.425 1.00 16.72 ? 69 GLN A O 1 +ATOM 557 C CB . GLN A 1 69 ? 2.170 -19.888 17.999 1.00 18.04 ? 69 GLN A CB 1 +ATOM 558 C CG . GLN A 1 69 ? 0.888 -20.656 17.771 1.00 21.51 ? 69 GLN A CG 1 +ATOM 559 C CD . GLN A 1 69 ? -0.161 -20.174 18.731 1.00 25.03 ? 69 GLN A CD 1 +ATOM 560 O OE1 . GLN A 1 69 ? 0.106 -19.927 19.909 1.00 25.84 ? 69 GLN A OE1 1 +ATOM 561 N NE2 . GLN A 1 69 ? -1.385 -20.021 18.241 1.00 26.21 ? 69 GLN A NE2 1 +ATOM 562 N N . ALA A 1 70 ? 2.875 -20.594 14.677 1.00 19.00 ? 70 ALA A N 1 +ATOM 563 C CA . ALA A 1 70 ? 2.620 -20.293 13.267 1.00 20.96 ? 70 ALA A CA 1 +ATOM 564 C C . ALA A 1 70 ? 1.139 -20.600 13.043 1.00 23.17 ? 70 ALA A C 1 +ATOM 565 O O . ALA A 1 70 ? 0.751 -21.762 13.002 1.00 23.52 ? 70 ALA A O 1 +ATOM 566 C CB . ALA A 1 70 ? 3.471 -21.204 12.398 1.00 20.97 ? 70 ALA A CB 1 +ATOM 567 N N . GLY A 1 71 ? 0.297 -19.573 13.046 1.00 24.68 ? 71 GLY A N 1 +ATOM 568 C CA . GLY A 1 71 ? -1.148 -19.764 12.969 1.00 25.82 ? 71 GLY A CA 1 +ATOM 569 C C . GLY A 1 71 ? -1.586 -20.403 14.272 1.00 26.30 ? 71 GLY A C 1 +ATOM 570 O O . GLY A 1 71 ? -1.283 -19.875 15.340 1.00 27.29 ? 71 GLY A O 1 +ATOM 571 N N A ASN A 1 72 ? -2.203 -21.577 14.195 0.50 25.88 ? 72 ASN A N 1 +ATOM 572 N N B ASN A 1 72 ? -2.232 -21.574 14.208 0.50 26.13 ? 72 ASN A N 1 +ATOM 573 C CA A ASN A 1 72 ? -2.607 -22.309 15.390 0.50 25.81 ? 72 ASN A CA 1 +ATOM 574 C CA B ASN A 1 72 ? -2.637 -22.282 15.426 0.50 26.29 ? 72 ASN A CA 1 +ATOM 575 C C A ASN A 1 72 ? -1.585 -23.402 15.775 0.50 25.30 ? 72 ASN A C 1 +ATOM 576 C C B ASN A 1 72 ? -1.713 -23.458 15.794 0.50 25.45 ? 72 ASN A C 1 +ATOM 577 O O A ASN A 1 72 ? -1.765 -24.044 16.810 0.50 25.73 ? 72 ASN A O 1 +ATOM 578 O O B ASN A 1 72 ? -2.036 -24.222 16.705 0.50 25.81 ? 72 ASN A O 1 +ATOM 579 C CB A ASN A 1 72 ? -3.990 -22.935 15.174 0.50 27.13 ? 72 ASN A CB 1 +ATOM 580 C CB B ASN A 1 72 ? -4.102 -22.729 15.351 0.50 28.37 ? 72 ASN A CB 1 +ATOM 581 C CG A ASN A 1 72 ? -4.706 -23.325 16.447 0.50 29.97 ? 72 ASN A CG 1 +ATOM 582 C CG B ASN A 1 72 ? -4.444 -23.658 14.208 0.50 32.49 ? 72 ASN A CG 1 +ATOM 583 O OD1 A ASN A 1 72 ? -4.849 -22.526 17.378 0.50 30.90 ? 72 ASN A OD1 1 +ATOM 584 O OD1 B ASN A 1 72 ? -3.749 -24.647 13.927 0.50 34.05 ? 72 ASN A OD1 1 +ATOM 585 N ND2 A ASN A 1 72 ? -5.171 -24.566 16.514 0.50 30.55 ? 72 ASN A ND2 1 +ATOM 586 N ND2 B ASN A 1 72 ? -5.547 -23.372 13.532 0.50 33.10 ? 72 ASN A ND2 1 +ATOM 587 N N A VAL A 1 73 ? -0.530 -23.633 14.956 0.75 24.08 ? 73 VAL A N 1 +ATOM 588 N N B VAL A 1 73 ? -0.584 -23.618 15.080 0.25 23.95 ? 73 VAL A N 1 +ATOM 589 C CA A VAL A 1 73 ? 0.414 -24.705 15.245 0.75 23.44 ? 73 VAL A CA 1 +ATOM 590 C CA B VAL A 1 73 ? 0.344 -24.718 15.304 0.25 22.97 ? 73 VAL A CA 1 +ATOM 591 C C A VAL A 1 73 ? 1.668 -24.214 15.976 0.75 21.47 ? 73 VAL A C 1 +ATOM 592 C C B VAL A 1 73 ? 1.640 -24.244 15.966 0.25 21.72 ? 73 VAL A C 1 +ATOM 593 O O A VAL A 1 73 ? 2.283 -23.222 15.597 0.75 20.54 ? 73 VAL A O 1 +ATOM 594 O O B VAL A 1 73 ? 2.279 -23.304 15.502 0.25 21.51 ? 73 VAL A O 1 +ATOM 595 C CB A VAL A 1 73 ? 0.763 -25.565 14.001 0.75 24.81 ? 73 VAL A CB 1 +ATOM 596 C CB B VAL A 1 73 ? 0.577 -25.518 13.997 0.25 23.51 ? 73 VAL A CB 1 +ATOM 597 C CG1 A VAL A 1 73 ? 1.636 -24.807 13.009 0.75 25.84 ? 73 VAL A CG1 1 +ATOM 598 C CG1 B VAL A 1 73 ? 1.798 -26.431 14.097 0.25 24.00 ? 73 VAL A CG1 1 +ATOM 599 C CG2 A VAL A 1 73 ? 1.436 -26.868 14.414 0.75 25.38 ? 73 VAL A CG2 1 +ATOM 600 C CG2 B VAL A 1 73 ? -0.667 -26.320 13.638 0.25 23.85 ? 73 VAL A CG2 1 +ATOM 601 N N . GLN A 1 74 ? 2.014 -24.909 17.059 1.00 20.75 ? 74 GLN A N 1 +ATOM 602 C CA . GLN A 1 74 ? 3.186 -24.589 17.836 1.00 19.17 ? 74 GLN A CA 1 +ATOM 603 C C . GLN A 1 74 ? 4.454 -25.134 17.203 1.00 18.22 ? 74 GLN A C 1 +ATOM 604 O O . GLN A 1 74 ? 4.478 -26.264 16.693 1.00 18.47 ? 74 GLN A O 1 +ATOM 605 C CB . GLN A 1 74 ? 3.034 -25.162 19.243 1.00 19.18 ? 74 GLN A CB 1 +ATOM 606 C CG . GLN A 1 74 ? 3.779 -24.366 20.307 1.00 19.39 ? 74 GLN A CG 1 +ATOM 607 C CD . GLN A 1 74 ? 3.183 -23.013 20.563 1.00 21.32 ? 74 GLN A CD 1 +ATOM 608 O OE1 . GLN A 1 74 ? 2.013 -22.747 20.265 1.00 21.97 ? 74 GLN A OE1 1 +ATOM 609 N NE2 . GLN A 1 74 ? 3.972 -22.133 21.159 1.00 21.51 ? 74 GLN A NE2 1 +ATOM 610 N N . LEU A 1 75 ? 5.519 -24.334 17.242 1.00 17.05 ? 75 LEU A N 1 +ATOM 611 C CA . LEU A 1 75 ? 6.809 -24.770 16.729 1.00 17.04 ? 75 LEU A CA 1 +ATOM 612 C C . LEU A 1 75 ? 7.735 -25.145 17.865 1.00 16.56 ? 75 LEU A C 1 +ATOM 613 O O . LEU A 1 75 ? 7.725 -24.505 18.912 1.00 17.40 ? 75 LEU A O 1 +ATOM 614 C CB . LEU A 1 75 ? 7.454 -23.702 15.837 1.00 17.69 ? 75 LEU A CB 1 +ATOM 615 C CG . LEU A 1 75 ? 6.621 -23.233 14.636 1.00 19.89 ? 75 LEU A CG 1 +ATOM 616 C CD1 . LEU A 1 75 ? 7.402 -22.256 13.792 1.00 20.45 ? 75 LEU A CD1 1 +ATOM 617 C CD2 . LEU A 1 75 ? 6.150 -24.405 13.778 1.00 21.66 ? 75 LEU A CD2 1 +ATOM 618 N N . ARG A 1 76 ? 8.516 -26.197 17.669 1.00 14.98 ? 76 ARG A N 1 +ATOM 619 C CA . ARG A 1 76 ? 9.440 -26.670 18.686 1.00 14.65 ? 76 ARG A CA 1 +ATOM 620 C C . ARG A 1 76 ? 10.784 -25.974 18.535 1.00 15.18 ? 76 ARG A C 1 +ATOM 621 O O . ARG A 1 76 ? 11.405 -26.099 17.487 1.00 16.02 ? 76 ARG A O 1 +ATOM 622 C CB . ARG A 1 76 ? 9.611 -28.184 18.570 1.00 15.16 ? 76 ARG A CB 1 +ATOM 623 C CG . ARG A 1 76 ? 10.429 -28.788 19.702 1.00 15.73 ? 76 ARG A CG 1 +ATOM 624 C CD . ARG A 1 76 ? 10.493 -30.311 19.588 1.00 16.39 ? 76 ARG A CD 1 +ATOM 625 N NE . ARG A 1 76 ? 9.152 -30.898 19.628 1.00 17.45 ? 76 ARG A NE 1 +ATOM 626 C CZ . ARG A 1 76 ? 8.486 -31.179 20.744 1.00 18.47 ? 76 ARG A CZ 1 +ATOM 627 N NH1 . ARG A 1 76 ? 9.049 -30.980 21.932 1.00 17.24 ? 76 ARG A NH1 1 +ATOM 628 N NH2 . ARG A 1 76 ? 7.256 -31.675 20.681 1.00 18.11 ? 76 ARG A NH2 1 +ATOM 629 N N . VAL A 1 77 ? 11.234 -25.254 19.574 1.00 14.60 ? 77 VAL A N 1 +ATOM 630 C CA . VAL A 1 77 ? 12.504 -24.530 19.581 1.00 14.79 ? 77 VAL A CA 1 +ATOM 631 C C . VAL A 1 77 ? 13.634 -25.433 20.060 1.00 15.27 ? 77 VAL A C 1 +ATOM 632 O O . VAL A 1 77 ? 13.610 -25.910 21.200 1.00 15.58 ? 77 VAL A O 1 +ATOM 633 C CB . VAL A 1 77 ? 12.396 -23.241 20.417 1.00 14.63 ? 77 VAL A CB 1 +ATOM 634 C CG1 . VAL A 1 77 ? 13.738 -22.496 20.457 1.00 15.23 ? 77 VAL A CG1 1 +ATOM 635 C CG2 . VAL A 1 77 ? 11.286 -22.353 19.859 1.00 15.19 ? 77 VAL A CG2 1 +ATOM 636 N N . ILE A 1 78 ? 14.606 -25.704 19.183 1.00 14.95 ? 78 ILE A N 1 +ATOM 637 C CA . ILE A 1 78 ? 15.726 -26.579 19.519 1.00 15.44 ? 78 ILE A CA 1 +ATOM 638 C C . ILE A 1 78 ? 17.072 -25.865 19.681 1.00 15.44 ? 78 ILE A C 1 +ATOM 639 O O . ILE A 1 78 ? 18.089 -26.513 19.933 1.00 16.12 ? 78 ILE A O 1 +ATOM 640 C CB . ILE A 1 78 ? 15.821 -27.724 18.493 1.00 16.42 ? 78 ILE A CB 1 +ATOM 641 C CG1 . ILE A 1 78 ? 16.122 -27.179 17.085 1.00 17.67 ? 78 ILE A CG1 1 +ATOM 642 C CG2 . ILE A 1 78 ? 14.532 -28.525 18.490 1.00 16.90 ? 78 ILE A CG2 1 +ATOM 643 C CD1 . ILE A 1 78 ? 16.430 -28.295 16.044 1.00 18.94 ? 78 ILE A CD1 1 +ATOM 644 N N . GLY A 1 79 ? 17.071 -24.547 19.607 1.00 15.03 ? 79 GLY A N 1 +ATOM 645 C CA . GLY A 1 79 ? 18.273 -23.758 19.811 1.00 15.04 ? 79 GLY A CA 1 +ATOM 646 C C . GLY A 1 79 ? 17.946 -22.286 19.759 1.00 15.10 ? 79 GLY A C 1 +ATOM 647 O O . GLY A 1 79 ? 16.938 -21.896 19.168 1.00 14.94 ? 79 GLY A O 1 +ATOM 648 N N . HIS A 1 80 ? 18.773 -21.465 20.388 1.00 14.85 ? 80 HIS A N 1 +ATOM 649 C CA . HIS A 1 80 ? 18.582 -20.020 20.321 1.00 14.66 ? 80 HIS A CA 1 +ATOM 650 C C . HIS A 1 80 ? 19.904 -19.333 20.423 1.00 15.30 ? 80 HIS A C 1 +ATOM 651 O O . HIS A 1 80 ? 20.814 -19.802 21.123 1.00 15.86 ? 80 HIS A O 1 +ATOM 652 C CB . HIS A 1 80 ? 17.588 -19.490 21.366 1.00 14.91 ? 80 HIS A CB 1 +ATOM 653 C CG . HIS A 1 80 ? 18.070 -19.617 22.771 1.00 16.66 ? 80 HIS A CG 1 +ATOM 654 N ND1 . HIS A 1 80 ? 17.910 -20.787 23.482 1.00 17.48 ? 80 HIS A ND1 1 +ATOM 655 C CD2 . HIS A 1 80 ? 18.705 -18.716 23.556 1.00 17.84 ? 80 HIS A CD2 1 +ATOM 656 C CE1 . HIS A 1 80 ? 18.440 -20.563 24.674 1.00 18.30 ? 80 HIS A CE1 1 +ATOM 657 N NE2 . HIS A 1 80 ? 18.929 -19.326 24.760 1.00 18.47 ? 80 HIS A NE2 1 +ATOM 658 N N . SER A 1 81 ? 20.031 -18.237 19.705 1.00 14.84 ? 81 SER A N 1 +ATOM 659 C CA . SER A 1 81 ? 21.265 -17.465 19.755 1.00 14.86 ? 81 SER A CA 1 +ATOM 660 C C . SER A 1 81 ? 20.972 -16.018 19.462 1.00 14.66 ? 81 SER A C 1 +ATOM 661 O O . SER A 1 81 ? 19.970 -15.697 18.822 1.00 15.19 ? 81 SER A O 1 +ATOM 662 C CB . SER A 1 81 ? 22.291 -18.011 18.768 1.00 16.73 ? 81 SER A CB 1 +ATOM 663 O OG . SER A 1 81 ? 21.809 -17.919 17.441 1.00 20.31 ? 81 SER A OG 1 +ATOM 664 N N A MET A 1 82 ? 21.828 -15.125 19.951 0.50 14.30 ? 82 MET A N 1 +ATOM 665 N N B MET A 1 82 ? 21.839 -15.141 19.938 0.50 14.04 ? 82 MET A N 1 +ATOM 666 C CA A MET A 1 82 ? 21.664 -13.700 19.723 0.50 14.74 ? 82 MET A CA 1 +ATOM 667 C CA B MET A 1 82 ? 21.699 -13.721 19.712 0.50 14.21 ? 82 MET A CA 1 +ATOM 668 C C A MET A 1 82 ? 22.712 -13.224 18.723 0.50 15.23 ? 82 MET A C 1 +ATOM 669 C C B MET A 1 82 ? 22.718 -13.294 18.664 0.50 14.88 ? 82 MET A C 1 +ATOM 670 O O A MET A 1 82 ? 23.905 -13.470 18.919 0.50 16.17 ? 82 MET A O 1 +ATOM 671 O O B MET A 1 82 ? 23.890 -13.665 18.753 0.50 15.61 ? 82 MET A O 1 +ATOM 672 C CB A MET A 1 82 ? 21.801 -12.929 21.041 0.50 15.23 ? 82 MET A CB 1 +ATOM 673 C CB B MET A 1 82 ? 21.937 -12.966 21.026 0.50 14.18 ? 82 MET A CB 1 +ATOM 674 C CG A MET A 1 82 ? 21.614 -11.442 20.874 0.50 17.47 ? 82 MET A CG 1 +ATOM 675 C CG B MET A 1 82 ? 21.759 -11.474 20.898 0.50 15.64 ? 82 MET A CG 1 +ATOM 676 S SD A MET A 1 82 ? 21.828 -10.548 22.424 0.50 20.86 ? 82 MET A SD 1 +ATOM 677 S SD B MET A 1 82 ? 21.374 -10.707 22.484 0.50 15.97 ? 82 MET A SD 1 +ATOM 678 C CE A MET A 1 82 ? 20.402 -11.108 23.302 0.50 20.46 ? 82 MET A CE 1 +ATOM 679 C CE B MET A 1 82 ? 22.877 -11.090 23.413 0.50 12.42 ? 82 MET A CE 1 +ATOM 680 N N . GLN A 1 83 ? 22.270 -12.561 17.647 1.00 15.01 ? 83 GLN A N 1 +ATOM 681 C CA . GLN A 1 83 ? 23.164 -12.017 16.627 1.00 15.04 ? 83 GLN A CA 1 +ATOM 682 C C . GLN A 1 83 ? 22.849 -10.536 16.608 1.00 13.84 ? 83 GLN A C 1 +ATOM 683 O O . GLN A 1 83 ? 21.761 -10.157 16.187 1.00 14.15 ? 83 GLN A O 1 +ATOM 684 C CB . GLN A 1 83 ? 22.915 -12.619 15.247 1.00 17.78 ? 83 GLN A CB 1 +ATOM 685 C CG . GLN A 1 83 ? 23.871 -12.027 14.206 1.00 22.38 ? 83 GLN A CG 1 +ATOM 686 C CD . GLN A 1 83 ? 23.630 -12.527 12.802 1.00 27.19 ? 83 GLN A CD 1 +ATOM 687 O OE1 . GLN A 1 83 ? 22.667 -13.246 12.515 1.00 27.58 ? 83 GLN A OE1 1 +ATOM 688 N NE2 . GLN A 1 83 ? 24.504 -12.142 11.883 1.00 28.65 ? 83 GLN A NE2 1 +ATOM 689 N N . ASN A 1 84 ? 23.741 -9.705 17.152 1.00 13.13 ? 84 ASN A N 1 +ATOM 690 C CA . ASN A 1 84 ? 23.516 -8.266 17.264 1.00 12.86 ? 84 ASN A CA 1 +ATOM 691 C C . ASN A 1 84 ? 22.187 -8.003 18.043 1.00 12.30 ? 84 ASN A C 1 +ATOM 692 O O . ASN A 1 84 ? 22.073 -8.505 19.170 1.00 13.18 ? 84 ASN A O 1 +ATOM 693 C CB . ASN A 1 84 ? 23.643 -7.595 15.893 1.00 13.60 ? 84 ASN A CB 1 +ATOM 694 C CG . ASN A 1 84 ? 24.979 -7.902 15.287 1.00 16.97 ? 84 ASN A CG 1 +ATOM 695 O OD1 . ASN A 1 84 ? 26.030 -7.659 15.897 1.00 18.65 ? 84 ASN A OD1 1 +ATOM 696 N ND2 . ASN A 1 84 ? 24.965 -8.478 14.103 1.00 17.35 ? 84 ASN A ND2 1 +ATOM 697 N N . CYS A 1 85 ? 21.183 -7.327 17.448 1.00 11.65 ? 85 CYS A N 1 +ATOM 698 C CA . CYS A 1 85 ? 19.935 -7.077 18.150 1.00 11.74 ? 85 CYS A CA 1 +ATOM 699 C C . CYS A 1 85 ? 18.805 -8.021 17.785 1.00 11.93 ? 85 CYS A C 1 +ATOM 700 O O . CYS A 1 85 ? 17.658 -7.743 18.135 1.00 12.25 ? 85 CYS A O 1 +ATOM 701 C CB . CYS A 1 85 ? 19.518 -5.626 17.998 1.00 12.25 ? 85 CYS A CB 1 +ATOM 702 S SG . CYS A 1 85 ? 20.771 -4.475 18.599 1.00 14.49 ? 85 CYS A SG 1 +ATOM 703 N N . VAL A 1 86 ? 19.106 -9.142 17.124 1.00 11.92 ? 86 VAL A N 1 +ATOM 704 C CA A VAL A 1 86 ? 18.063 -10.123 16.816 0.80 12.69 ? 86 VAL A CA 1 +ATOM 705 C CA B VAL A 1 86 ? 18.084 -10.108 16.770 0.20 12.62 ? 86 VAL A CA 1 +ATOM 706 C C . VAL A 1 86 ? 18.368 -11.466 17.447 1.00 13.31 ? 86 VAL A C 1 +ATOM 707 O O . VAL A 1 86 ? 19.522 -11.792 17.744 1.00 13.89 ? 86 VAL A O 1 +ATOM 708 C CB A VAL A 1 86 ? 17.715 -10.290 15.315 0.80 13.96 ? 86 VAL A CB 1 +ATOM 709 C CB B VAL A 1 86 ? 17.964 -10.163 15.216 0.20 13.40 ? 86 VAL A CB 1 +ATOM 710 C CG1 A VAL A 1 86 ? 17.232 -8.980 14.704 0.80 14.98 ? 86 VAL A CG1 1 +ATOM 711 C CG1 B VAL A 1 86 ? 17.427 -11.492 14.704 0.20 13.91 ? 86 VAL A CG1 1 +ATOM 712 C CG2 A VAL A 1 86 ? 18.874 -10.884 14.538 0.80 14.71 ? 86 VAL A CG2 1 +ATOM 713 C CG2 B VAL A 1 86 ? 17.115 -9.007 14.699 0.20 14.01 ? 86 VAL A CG2 1 +ATOM 714 N N . LEU A 1 87 ? 17.311 -12.214 17.743 1.00 12.95 ? 87 LEU A N 1 +ATOM 715 C CA . LEU A 1 87 ? 17.437 -13.555 18.248 1.00 13.45 ? 87 LEU A CA 1 +ATOM 716 C C . LEU A 1 87 ? 17.087 -14.460 17.060 1.00 12.81 ? 87 LEU A C 1 +ATOM 717 O O . LEU A 1 87 ? 16.214 -14.148 16.232 1.00 12.84 ? 87 LEU A O 1 +ATOM 718 C CB . LEU A 1 87 ? 16.456 -13.848 19.385 1.00 14.73 ? 87 LEU A CB 1 +ATOM 719 C CG . LEU A 1 87 ? 16.676 -13.104 20.677 1.00 17.21 ? 87 LEU A CG 1 +ATOM 720 C CD1 . LEU A 1 87 ? 15.555 -13.409 21.659 1.00 17.72 ? 87 LEU A CD1 1 +ATOM 721 C CD2 . LEU A 1 87 ? 18.026 -13.431 21.279 1.00 19.12 ? 87 LEU A CD2 1 +ATOM 722 N N . LYS A 1 88 ? 17.808 -15.569 16.962 1.00 12.70 ? 88 LYS A N 1 +ATOM 723 C CA . LYS A 1 88 ? 17.600 -16.588 15.957 1.00 12.67 ? 88 LYS A CA 1 +ATOM 724 C C . LYS A 1 88 ? 17.188 -17.806 16.736 1.00 12.90 ? 88 LYS A C 1 +ATOM 725 O O . LYS A 1 88 ? 17.975 -18.321 17.525 1.00 13.84 ? 88 LYS A O 1 +ATOM 726 C CB . LYS A 1 88 ? 18.899 -16.875 15.190 1.00 13.93 ? 88 LYS A CB 1 +ATOM 727 C CG . LYS A 1 88 ? 19.258 -15.755 14.219 1.00 17.96 ? 88 LYS A CG 1 +ATOM 728 C CD . LYS A 1 88 ? 20.490 -16.070 13.376 1.00 22.34 ? 88 LYS A CD 1 +ATOM 729 C CE . LYS A 1 88 ? 21.738 -16.137 14.208 1.00 26.94 ? 88 LYS A CE 1 +ATOM 730 N NZ . LYS A 1 88 ? 22.952 -15.999 13.363 1.00 28.94 ? 88 LYS A NZ 1 +ATOM 731 N N . LEU A 1 89 ? 15.950 -18.220 16.574 1.00 12.44 ? 89 LEU A N 1 +ATOM 732 C CA . LEU A 1 89 ? 15.403 -19.373 17.256 1.00 12.59 ? 89 LEU A CA 1 +ATOM 733 C C . LEU A 1 89 ? 15.367 -20.511 16.264 1.00 12.94 ? 89 LEU A C 1 +ATOM 734 O O . LEU A 1 89 ? 14.620 -20.459 15.287 1.00 13.54 ? 89 LEU A O 1 +ATOM 735 C CB . LEU A 1 89 ? 13.982 -19.063 17.753 1.00 12.75 ? 89 LEU A CB 1 +ATOM 736 C CG . LEU A 1 89 ? 13.831 -17.772 18.569 1.00 13.26 ? 89 LEU A CG 1 +ATOM 737 C CD1 . LEU A 1 89 ? 12.360 -17.539 18.932 1.00 14.00 ? 89 LEU A CD1 1 +ATOM 738 C CD2 . LEU A 1 89 ? 14.701 -17.814 19.810 1.00 14.04 ? 89 LEU A CD2 1 +ATOM 739 N N . LYS A 1 90 ? 16.203 -21.522 16.472 1.00 12.58 ? 90 LYS A N 1 +ATOM 740 C CA . LYS A 1 90 ? 16.232 -22.674 15.595 1.00 13.10 ? 90 LYS A CA 1 +ATOM 741 C C . LYS A 1 90 ? 15.051 -23.539 15.962 1.00 13.08 ? 90 LYS A C 1 +ATOM 742 O O . LYS A 1 90 ? 14.830 -23.805 17.137 1.00 13.52 ? 90 LYS A O 1 +ATOM 743 C CB . LYS A 1 90 ? 17.536 -23.458 15.769 1.00 15.25 ? 90 LYS A CB 1 +ATOM 744 C CG . LYS A 1 90 ? 17.687 -24.519 14.697 1.00 19.98 ? 90 LYS A CG 1 +ATOM 745 C CD . LYS A 1 90 ? 18.937 -25.357 14.862 1.00 26.70 ? 90 LYS A CD 1 +ATOM 746 C CE . LYS A 1 90 ? 18.950 -26.460 13.827 1.00 31.95 ? 90 LYS A CE 1 +ATOM 747 N NZ . LYS A 1 90 ? 20.250 -27.184 13.784 1.00 34.61 ? 90 LYS A NZ 1 +ATOM 748 N N . VAL A 1 91 ? 14.239 -23.892 14.982 1.00 13.01 ? 91 VAL A N 1 +ATOM 749 C CA . VAL A 1 91 ? 13.080 -24.738 15.204 1.00 13.59 ? 91 VAL A CA 1 +ATOM 750 C C . VAL A 1 91 ? 13.290 -26.080 14.510 1.00 13.94 ? 91 VAL A C 1 +ATOM 751 O O . VAL A 1 91 ? 14.153 -26.193 13.635 1.00 14.24 ? 91 VAL A O 1 +ATOM 752 C CB . VAL A 1 91 ? 11.760 -24.046 14.810 1.00 13.54 ? 91 VAL A CB 1 +ATOM 753 C CG1 . VAL A 1 91 ? 11.470 -22.870 15.748 1.00 13.86 ? 91 VAL A CG1 1 +ATOM 754 C CG2 . VAL A 1 91 ? 11.792 -23.576 13.358 1.00 13.61 ? 91 VAL A CG2 1 +ATOM 755 N N . ASP A 1 92 ? 12.510 -27.098 14.887 1.00 14.52 ? 92 ASP A N 1 +ATOM 756 C CA . ASP A 1 92 ? 12.713 -28.432 14.308 1.00 15.39 ? 92 ASP A CA 1 +ATOM 757 C C . ASP A 1 92 ? 12.040 -28.640 12.940 1.00 16.15 ? 92 ASP A C 1 +ATOM 758 O O . ASP A 1 92 ? 12.151 -29.724 12.366 1.00 17.58 ? 92 ASP A O 1 +ATOM 759 C CB . ASP A 1 92 ? 12.298 -29.535 15.300 1.00 16.92 ? 92 ASP A CB 1 +ATOM 760 C CG . ASP A 1 92 ? 10.803 -29.782 15.434 1.00 21.75 ? 92 ASP A CG 1 +ATOM 761 O OD1 . ASP A 1 92 ? 10.011 -28.950 14.931 1.00 21.92 ? 92 ASP A OD1 1 +ATOM 762 O OD2 . ASP A 1 92 ? 10.423 -30.804 16.052 1.00 24.89 ? 92 ASP A OD2 1 +ATOM 763 N N . THR A 1 93 ? 11.319 -27.629 12.442 1.00 15.46 ? 93 THR A N 1 +ATOM 764 C CA . THR A 1 93 ? 10.601 -27.740 11.184 1.00 15.98 ? 93 THR A CA 1 +ATOM 765 C C . THR A 1 93 ? 10.936 -26.576 10.273 1.00 15.60 ? 93 THR A C 1 +ATOM 766 O O . THR A 1 93 ? 10.857 -25.414 10.682 1.00 15.87 ? 93 THR A O 1 +ATOM 767 C CB . THR A 1 93 ? 9.091 -27.772 11.474 1.00 18.02 ? 93 THR A CB 1 +ATOM 768 O OG1 . THR A 1 93 ? 8.807 -28.909 12.282 1.00 19.65 ? 93 THR A OG1 1 +ATOM 769 C CG2 . THR A 1 93 ? 8.231 -27.818 10.214 1.00 18.56 ? 93 THR A CG2 1 +ATOM 770 N N . ALA A 1 94 ? 11.321 -26.885 9.036 1.00 15.11 ? 94 ALA A N 1 +ATOM 771 C CA . ALA A 1 94 ? 11.580 -25.846 8.051 1.00 15.27 ? 94 ALA A CA 1 +ATOM 772 C C . ALA A 1 94 ? 10.227 -25.287 7.629 1.00 14.37 ? 94 ALA A C 1 +ATOM 773 O O . ALA A 1 94 ? 9.266 -26.049 7.472 1.00 14.40 ? 94 ALA A O 1 +ATOM 774 C CB . ALA A 1 94 ? 12.280 -26.436 6.838 1.00 15.99 ? 94 ALA A CB 1 +ATOM 775 N N . ASN A 1 95 ? 10.133 -23.953 7.445 1.00 13.14 ? 95 ASN A N 1 +ATOM 776 C CA . ASN A 1 95 ? 8.883 -23.366 6.989 1.00 12.83 ? 95 ASN A CA 1 +ATOM 777 C C . ASN A 1 95 ? 8.594 -23.845 5.583 1.00 14.44 ? 95 ASN A C 1 +ATOM 778 O O . ASN A 1 95 ? 9.373 -23.554 4.678 1.00 15.01 ? 95 ASN A O 1 +ATOM 779 C CB . ASN A 1 95 ? 8.974 -21.836 7.015 1.00 11.70 ? 95 ASN A CB 1 +ATOM 780 C CG . ASN A 1 95 ? 7.671 -21.166 6.662 1.00 12.68 ? 95 ASN A CG 1 +ATOM 781 O OD1 . ASN A 1 95 ? 6.665 -21.818 6.312 1.00 12.65 ? 95 ASN A OD1 1 +ATOM 782 N ND2 . ASN A 1 95 ? 7.654 -19.854 6.755 1.00 13.33 ? 95 ASN A ND2 1 +ATOM 783 N N . PRO A 1 96 ? 7.498 -24.592 5.381 1.00 15.09 ? 96 PRO A N 1 +ATOM 784 C CA . PRO A 1 96 ? 7.194 -25.071 4.022 1.00 15.91 ? 96 PRO A CA 1 +ATOM 785 C C . PRO A 1 96 ? 6.869 -23.969 3.029 1.00 16.81 ? 96 PRO A C 1 +ATOM 786 O O . PRO A 1 96 ? 6.955 -24.177 1.819 1.00 18.67 ? 96 PRO A O 1 +ATOM 787 C CB . PRO A 1 96 ? 6.007 -26.020 4.234 1.00 16.85 ? 96 PRO A CB 1 +ATOM 788 C CG . PRO A 1 96 ? 5.365 -25.537 5.452 1.00 17.21 ? 96 PRO A CG 1 +ATOM 789 C CD . PRO A 1 96 ? 6.454 -24.999 6.343 1.00 15.27 ? 96 PRO A CD 1 +ATOM 790 N N A LYS A 1 97 ? 6.497 -22.792 3.536 0.50 16.18 ? 97 LYS A N 1 +ATOM 791 N N B LYS A 1 97 ? 6.498 -22.794 3.526 0.50 15.87 ? 97 LYS A N 1 +ATOM 792 C CA A LYS A 1 97 ? 6.197 -21.633 2.715 0.50 16.25 ? 97 LYS A CA 1 +ATOM 793 C CA B LYS A 1 97 ? 6.186 -21.657 2.678 0.50 15.62 ? 97 LYS A CA 1 +ATOM 794 C C A LYS A 1 97 ? 7.398 -20.685 2.599 0.50 16.20 ? 97 LYS A C 1 +ATOM 795 C C B LYS A 1 97 ? 7.397 -20.733 2.479 0.50 15.87 ? 97 LYS A C 1 +ATOM 796 O O A LYS A 1 97 ? 7.196 -19.507 2.312 0.50 16.30 ? 97 LYS A O 1 +ATOM 797 O O B LYS A 1 97 ? 7.210 -19.616 1.997 0.50 15.98 ? 97 LYS A O 1 +ATOM 798 C CB A LYS A 1 97 ? 4.997 -20.876 3.290 0.50 17.71 ? 97 LYS A CB 1 +ATOM 799 C CB B LYS A 1 97 ? 5.028 -20.859 3.292 0.50 16.13 ? 97 LYS A CB 1 +ATOM 800 C CG A LYS A 1 97 ? 3.707 -21.681 3.258 0.50 21.36 ? 97 LYS A CG 1 +ATOM 801 C CG B LYS A 1 97 ? 3.787 -21.702 3.563 0.50 18.13 ? 97 LYS A CG 1 +ATOM 802 C CD A LYS A 1 97 ? 2.514 -20.817 3.626 0.50 25.21 ? 97 LYS A CD 1 +ATOM 803 C CD B LYS A 1 97 ? 2.659 -20.874 4.168 0.50 20.47 ? 97 LYS A CD 1 +ATOM 804 C CE A LYS A 1 97 ? 1.247 -21.628 3.735 0.50 28.84 ? 97 LYS A CE 1 +ATOM 805 C CE B LYS A 1 97 ? 1.497 -21.748 4.586 0.50 23.28 ? 97 LYS A CE 1 +ATOM 806 N NZ A LYS A 1 97 ? 1.311 -22.583 4.872 0.50 31.00 ? 97 LYS A NZ 1 +ATOM 807 N NZ B LYS A 1 97 ? 0.450 -20.970 5.306 0.50 24.86 ? 97 LYS A NZ 1 +ATOM 808 N N . THR A 1 98 ? 8.635 -21.173 2.838 1.00 15.64 ? 98 THR A N 1 +ATOM 809 C CA . THR A 1 98 ? 9.819 -20.315 2.707 1.00 15.75 ? 98 THR A CA 1 +ATOM 810 C C . THR A 1 98 ? 10.036 -19.955 1.256 1.00 17.30 ? 98 THR A C 1 +ATOM 811 O O . THR A 1 98 ? 10.207 -20.836 0.419 1.00 18.89 ? 98 THR A O 1 +ATOM 812 C CB . THR A 1 98 ? 11.098 -20.973 3.223 1.00 15.79 ? 98 THR A CB 1 +ATOM 813 O OG1 . THR A 1 98 ? 10.913 -21.371 4.576 1.00 14.95 ? 98 THR A OG1 1 +ATOM 814 C CG2 . THR A 1 98 ? 12.291 -20.020 3.161 1.00 16.33 ? 98 THR A CG2 1 +ATOM 815 N N . PRO A 1 99 ? 9.971 -18.662 0.943 1.00 17.35 ? 99 PRO A N 1 +ATOM 816 C CA . PRO A 1 99 ? 10.220 -18.251 -0.440 1.00 17.36 ? 99 PRO A CA 1 +ATOM 817 C C . PRO A 1 99 ? 11.719 -18.183 -0.682 1.00 17.89 ? 99 PRO A C 1 +ATOM 818 O O . PRO A 1 99 ? 12.539 -18.301 0.246 1.00 18.10 ? 99 PRO A O 1 +ATOM 819 C CB . PRO A 1 99 ? 9.616 -16.844 -0.472 1.00 17.74 ? 99 PRO A CB 1 +ATOM 820 C CG . PRO A 1 99 ? 9.944 -16.303 0.908 1.00 18.63 ? 99 PRO A CG 1 +ATOM 821 C CD . PRO A 1 99 ? 9.806 -17.493 1.835 1.00 16.90 ? 99 PRO A CD 1 +ATOM 822 N N . LYS A 1 100 ? 12.124 -17.929 -1.950 1.00 18.01 ? 100 LYS A N 1 +ATOM 823 C CA . LYS A 1 100 ? 13.535 -17.625 -2.236 1.00 17.86 ? 100 LYS A CA 1 +ATOM 824 C C . LYS A 1 100 ? 13.794 -16.281 -1.557 1.00 16.86 ? 100 LYS A C 1 +ATOM 825 O O . LYS A 1 100 ? 12.915 -15.410 -1.609 1.00 17.12 ? 100 LYS A O 1 +ATOM 826 C CB . LYS A 1 100 ? 13.781 -17.459 -3.727 1.00 20.30 ? 100 LYS A CB 1 +ATOM 827 C CG . LYS A 1 100 ? 13.806 -18.781 -4.460 1.00 25.36 ? 100 LYS A CG 1 +ATOM 828 C CD . LYS A 1 100 ? 13.957 -18.552 -5.942 1.00 30.62 ? 100 LYS A CD 1 +ATOM 829 C CE . LYS A 1 100 ? 13.870 -19.846 -6.690 1.00 34.80 ? 100 LYS A CE 1 +ATOM 830 N NZ . LYS A 1 100 ? 13.923 -19.616 -8.154 1.00 37.87 ? 100 LYS A NZ 1 +ATOM 831 N N . TYR A 1 101 ? 14.880 -16.181 -0.805 1.00 16.48 ? 101 TYR A N 1 +ATOM 832 C CA . TYR A 1 101 ? 15.128 -14.952 -0.066 1.00 16.55 ? 101 TYR A CA 1 +ATOM 833 C C . TYR A 1 101 ? 16.581 -14.602 0.070 1.00 17.45 ? 101 TYR A C 1 +ATOM 834 O O . TYR A 1 101 ? 17.465 -15.432 -0.117 1.00 18.21 ? 101 TYR A O 1 +ATOM 835 C CB . TYR A 1 101 ? 14.446 -14.990 1.329 1.00 15.77 ? 101 TYR A CB 1 +ATOM 836 C CG . TYR A 1 101 ? 15.146 -15.902 2.316 1.00 15.73 ? 101 TYR A CG 1 +ATOM 837 C CD1 . TYR A 1 101 ? 14.886 -17.261 2.336 1.00 15.94 ? 101 TYR A CD1 1 +ATOM 838 C CD2 . TYR A 1 101 ? 16.069 -15.402 3.228 1.00 16.30 ? 101 TYR A CD2 1 +ATOM 839 C CE1 . TYR A 1 101 ? 15.528 -18.107 3.223 1.00 17.03 ? 101 TYR A CE1 1 +ATOM 840 C CE2 . TYR A 1 101 ? 16.721 -16.242 4.126 1.00 16.87 ? 101 TYR A CE2 1 +ATOM 841 C CZ . TYR A 1 101 ? 16.426 -17.592 4.137 1.00 18.00 ? 101 TYR A CZ 1 +ATOM 842 O OH . TYR A 1 101 ? 17.050 -18.451 5.005 1.00 19.69 ? 101 TYR A OH 1 +ATOM 843 N N . LYS A 1 102 ? 16.813 -13.342 0.419 1.00 17.07 ? 102 LYS A N 1 +ATOM 844 C CA . LYS A 1 102 ? 18.117 -12.782 0.702 1.00 17.29 ? 102 LYS A CA 1 +ATOM 845 C C . LYS A 1 102 ? 17.931 -11.785 1.830 1.00 17.01 ? 102 LYS A C 1 +ATOM 846 O O . LYS A 1 102 ? 16.841 -11.228 2.005 1.00 17.36 ? 102 LYS A O 1 +ATOM 847 C CB . LYS A 1 102 ? 18.666 -12.018 -0.521 1.00 19.57 ? 102 LYS A CB 1 +ATOM 848 C CG . LYS A 1 102 ? 19.172 -12.891 -1.652 1.00 25.57 ? 102 LYS A CG 1 +ATOM 849 C CD . LYS A 1 102 ? 19.560 -12.019 -2.838 1.00 30.51 ? 102 LYS A CD 1 +ATOM 850 C CE . LYS A 1 102 ? 19.942 -12.850 -4.039 1.00 34.71 ? 102 LYS A CE 1 +ATOM 851 N NZ . LYS A 1 102 ? 20.222 -11.998 -5.223 1.00 37.67 ? 102 LYS A NZ 1 +ATOM 852 N N . PHE A 1 103 ? 18.997 -11.533 2.573 1.00 16.41 ? 103 PHE A N 1 +ATOM 853 C CA . PHE A 1 103 ? 18.994 -10.484 3.584 1.00 16.22 ? 103 PHE A CA 1 +ATOM 854 C C . PHE A 1 103 ? 19.847 -9.382 3.004 1.00 16.98 ? 103 PHE A C 1 +ATOM 855 O O . PHE A 1 103 ? 20.994 -9.634 2.601 1.00 18.29 ? 103 PHE A O 1 +ATOM 856 C CB . PHE A 1 103 ? 19.613 -10.957 4.902 1.00 15.69 ? 103 PHE A CB 1 +ATOM 857 C CG . PHE A 1 103 ? 18.795 -11.943 5.708 1.00 15.24 ? 103 PHE A CG 1 +ATOM 858 C CD1 . PHE A 1 103 ? 17.445 -12.132 5.446 1.00 15.08 ? 103 PHE A CD1 1 +ATOM 859 C CD2 . PHE A 1 103 ? 19.352 -12.609 6.784 1.00 15.50 ? 103 PHE A CD2 1 +ATOM 860 C CE1 . PHE A 1 103 ? 16.690 -13.014 6.217 1.00 15.35 ? 103 PHE A CE1 1 +ATOM 861 C CE2 . PHE A 1 103 ? 18.597 -13.493 7.545 1.00 15.76 ? 103 PHE A CE2 1 +ATOM 862 C CZ . PHE A 1 103 ? 17.267 -13.671 7.274 1.00 15.43 ? 103 PHE A CZ 1 +ATOM 863 N N . VAL A 1 104 ? 19.279 -8.182 2.889 1.00 16.37 ? 104 VAL A N 1 +ATOM 864 C CA . VAL A 1 104 ? 20.033 -7.044 2.376 1.00 17.50 ? 104 VAL A CA 1 +ATOM 865 C C . VAL A 1 104 ? 19.980 -5.887 3.348 1.00 17.45 ? 104 VAL A C 1 +ATOM 866 O O . VAL A 1 104 ? 18.977 -5.694 4.025 1.00 18.38 ? 104 VAL A O 1 +ATOM 867 C CB . VAL A 1 104 ? 19.568 -6.605 0.972 1.00 19.51 ? 104 VAL A CB 1 +ATOM 868 C CG1 . VAL A 1 104 ? 19.602 -7.772 -0.011 1.00 20.51 ? 104 VAL A CG1 1 +ATOM 869 C CG2 . VAL A 1 104 ? 18.188 -5.980 1.030 1.00 21.03 ? 104 VAL A CG2 1 +ATOM 870 N N . ARG A 1 105 ? 21.056 -5.114 3.423 1.00 15.80 ? 105 ARG A N 1 +ATOM 871 C CA . ARG A 1 105 ? 21.085 -3.918 4.245 1.00 15.43 ? 105 ARG A CA 1 +ATOM 872 C C . ARG A 1 105 ? 20.948 -2.766 3.265 1.00 16.07 ? 105 ARG A C 1 +ATOM 873 O O . ARG A 1 105 ? 21.814 -2.585 2.403 1.00 16.45 ? 105 ARG A O 1 +ATOM 874 C CB . ARG A 1 105 ? 22.391 -3.812 5.050 1.00 15.61 ? 105 ARG A CB 1 +ATOM 875 C CG . ARG A 1 105 ? 22.422 -2.551 5.896 1.00 16.10 ? 105 ARG A CG 1 +ATOM 876 C CD . ARG A 1 105 ? 23.630 -2.518 6.815 1.00 16.65 ? 105 ARG A CD 1 +ATOM 877 N NE . ARG A 1 105 ? 23.615 -1.344 7.690 1.00 16.81 ? 105 ARG A NE 1 +ATOM 878 C CZ . ARG A 1 105 ? 22.963 -1.276 8.847 1.00 17.76 ? 105 ARG A CZ 1 +ATOM 879 N NH1 . ARG A 1 105 ? 22.257 -2.313 9.283 1.00 15.50 ? 105 ARG A NH1 1 +ATOM 880 N NH2 . ARG A 1 105 ? 23.019 -0.174 9.580 1.00 16.68 ? 105 ARG A NH2 1 +ATOM 881 N N . ILE A 1 106 ? 19.843 -2.020 3.359 1.00 16.34 ? 106 ILE A N 1 +ATOM 882 C CA . ILE A 1 106 ? 19.591 -0.952 2.403 1.00 17.54 ? 106 ILE A CA 1 +ATOM 883 C C . ILE A 1 106 ? 20.273 0.351 2.775 1.00 18.38 ? 106 ILE A C 1 +ATOM 884 O O . ILE A 1 106 ? 20.686 0.548 3.914 1.00 18.30 ? 106 ILE A O 1 +ATOM 885 C CB . ILE A 1 106 ? 18.079 -0.754 2.154 1.00 18.39 ? 106 ILE A CB 1 +ATOM 886 C CG1 . ILE A 1 106 ? 17.349 -0.412 3.456 1.00 18.46 ? 106 ILE A CG1 1 +ATOM 887 C CG2 . ILE A 1 106 ? 17.482 -1.941 1.420 1.00 19.36 ? 106 ILE A CG2 1 +ATOM 888 C CD1 . ILE A 1 106 ? 15.965 0.091 3.254 1.00 19.73 ? 106 ILE A CD1 1 +ATOM 889 N N . GLN A 1 107 ? 20.428 1.226 1.782 1.00 19.23 ? 107 GLN A N 1 +ATOM 890 C CA . GLN A 1 107 ? 20.997 2.545 1.964 1.00 19.73 ? 107 GLN A CA 1 +ATOM 891 C C . GLN A 1 107 ? 19.865 3.537 2.207 1.00 18.47 ? 107 GLN A C 1 +ATOM 892 O O . GLN A 1 107 ? 18.742 3.340 1.721 1.00 17.38 ? 107 GLN A O 1 +ATOM 893 C CB . GLN A 1 107 ? 21.745 2.950 0.676 1.00 23.23 ? 107 GLN A CB 1 +ATOM 894 C CG . GLN A 1 107 ? 22.876 1.997 0.305 1.00 29.27 ? 107 GLN A CG 1 +ATOM 895 C CD . GLN A 1 107 ? 24.026 2.049 1.285 1.00 36.32 ? 107 GLN A CD 1 +ATOM 896 O OE1 . GLN A 1 107 ? 24.225 3.026 2.019 1.00 38.70 ? 107 GLN A OE1 1 +ATOM 897 N NE2 . GLN A 1 107 ? 24.829 0.996 1.300 1.00 37.97 ? 107 GLN A NE2 1 +ATOM 898 N N . PRO A 1 108 ? 20.146 4.681 2.862 1.00 18.14 ? 108 PRO A N 1 +ATOM 899 C CA . PRO A 1 108 ? 19.108 5.716 2.987 1.00 17.93 ? 108 PRO A CA 1 +ATOM 900 C C . PRO A 1 108 ? 18.660 6.165 1.590 1.00 17.22 ? 108 PRO A C 1 +ATOM 901 O O . PRO A 1 108 ? 19.462 6.189 0.647 1.00 17.68 ? 108 PRO A O 1 +ATOM 902 C CB . PRO A 1 108 ? 19.811 6.845 3.755 1.00 19.73 ? 108 PRO A CB 1 +ATOM 903 C CG . PRO A 1 108 ? 21.269 6.568 3.594 1.00 21.30 ? 108 PRO A CG 1 +ATOM 904 C CD . PRO A 1 108 ? 21.423 5.100 3.467 1.00 19.01 ? 108 PRO A CD 1 +ATOM 905 N N . GLY A 1 109 ? 17.382 6.434 1.449 1.00 15.99 ? 109 GLY A N 1 +ATOM 906 C CA . GLY A 1 109 ? 16.807 6.791 0.158 1.00 16.21 ? 109 GLY A CA 1 +ATOM 907 C C . GLY A 1 109 ? 16.074 5.638 -0.506 1.00 16.96 ? 109 GLY A C 1 +ATOM 908 O O . GLY A 1 109 ? 15.191 5.862 -1.338 1.00 18.41 ? 109 GLY A O 1 +ATOM 909 N N A GLN A 1 110 ? 16.422 4.397 -0.138 0.75 16.76 ? 110 GLN A N 1 +ATOM 910 N N B GLN A 1 110 ? 16.445 4.390 -0.161 0.25 16.16 ? 110 GLN A N 1 +ATOM 911 C CA A GLN A 1 110 ? 15.768 3.237 -0.714 0.75 16.95 ? 110 GLN A CA 1 +ATOM 912 C CA B GLN A 1 110 ? 15.829 3.187 -0.717 0.25 15.84 ? 110 GLN A CA 1 +ATOM 913 C C A GLN A 1 110 ? 14.440 2.952 -0.068 0.75 16.11 ? 110 GLN A C 1 +ATOM 914 C C B GLN A 1 110 ? 14.470 2.926 -0.075 0.25 15.71 ? 110 GLN A C 1 +ATOM 915 O O A GLN A 1 110 ? 14.240 3.191 1.125 0.75 16.11 ? 110 GLN A O 1 +ATOM 916 O O B GLN A 1 110 ? 14.293 3.143 1.123 0.25 15.80 ? 110 GLN A O 1 +ATOM 917 C CB A GLN A 1 110 ? 16.693 2.020 -0.709 0.75 19.14 ? 110 GLN A CB 1 +ATOM 918 C CB B GLN A 1 110 ? 16.764 1.974 -0.537 0.25 16.49 ? 110 GLN A CB 1 +ATOM 919 C CG A GLN A 1 110 ? 17.940 2.248 -1.555 0.75 23.45 ? 110 GLN A CG 1 +ATOM 920 C CG B GLN A 1 110 ? 16.218 0.644 -1.057 0.25 17.81 ? 110 GLN A CG 1 +ATOM 921 C CD A GLN A 1 110 ? 17.625 2.582 -2.992 0.75 30.28 ? 110 GLN A CD 1 +ATOM 922 C CD B GLN A 1 110 ? 15.922 0.672 -2.535 0.25 19.23 ? 110 GLN A CD 1 +ATOM 923 O OE1 A GLN A 1 110 ? 17.015 1.792 -3.727 0.75 33.04 ? 110 GLN A OE1 1 +ATOM 924 O OE1 B GLN A 1 110 ? 16.709 1.161 -3.348 0.25 20.49 ? 110 GLN A OE1 1 +ATOM 925 N NE2 A GLN A 1 110 ? 18.015 3.774 -3.418 0.75 30.91 ? 110 GLN A NE2 1 +ATOM 926 N NE2 B GLN A 1 110 ? 14.760 0.153 -2.910 0.25 17.17 ? 110 GLN A NE2 1 +ATOM 927 N N . THR A 1 111 ? 13.508 2.467 -0.876 1.00 15.42 ? 111 THR A N 1 +ATOM 928 C CA . THR A 1 111 ? 12.177 2.177 -0.420 1.00 15.01 ? 111 THR A CA 1 +ATOM 929 C C . THR A 1 111 ? 12.007 0.676 -0.190 1.00 14.44 ? 111 THR A C 1 +ATOM 930 O O . THR A 1 111 ? 12.800 -0.137 -0.654 1.00 15.56 ? 111 THR A O 1 +ATOM 931 C CB . THR A 1 111 ? 11.189 2.708 -1.461 1.00 15.57 ? 111 THR A CB 1 +ATOM 932 O OG1 . THR A 1 111 ? 11.488 2.051 -2.697 1.00 16.40 ? 111 THR A OG1 1 +ATOM 933 C CG2 . THR A 1 111 ? 11.297 4.211 -1.623 1.00 15.53 ? 111 THR A CG2 1 +ATOM 934 N N . PHE A 1 112 ? 10.950 0.319 0.518 1.00 13.51 ? 112 PHE A N 1 +ATOM 935 C CA . PHE A 1 112 ? 10.598 -1.063 0.784 1.00 13.06 ? 112 PHE A CA 1 +ATOM 936 C C . PHE A 1 112 ? 9.173 -1.129 1.275 1.00 12.87 ? 112 PHE A C 1 +ATOM 937 O O . PHE A 1 112 ? 8.617 -0.121 1.728 1.00 12.86 ? 112 PHE A O 1 +ATOM 938 C CB . PHE A 1 112 ? 11.550 -1.690 1.813 1.00 13.30 ? 112 PHE A CB 1 +ATOM 939 C CG . PHE A 1 112 ? 11.648 -0.996 3.149 1.00 13.25 ? 112 PHE A CG 1 +ATOM 940 C CD1 . PHE A 1 112 ? 12.527 0.058 3.340 1.00 14.26 ? 112 PHE A CD1 1 +ATOM 941 C CD2 . PHE A 1 112 ? 10.881 -1.409 4.218 1.00 13.58 ? 112 PHE A CD2 1 +ATOM 942 C CE1 . PHE A 1 112 ? 12.649 0.667 4.581 1.00 14.94 ? 112 PHE A CE1 1 +ATOM 943 C CE2 . PHE A 1 112 ? 11.024 -0.820 5.466 1.00 14.05 ? 112 PHE A CE2 1 +ATOM 944 C CZ . PHE A 1 112 ? 11.895 0.226 5.637 1.00 14.59 ? 112 PHE A CZ 1 +ATOM 945 N N . SER A 1 113 ? 8.584 -2.325 1.254 1.00 12.27 ? 113 SER A N 1 +ATOM 946 C CA . SER A 1 113 ? 7.231 -2.520 1.754 1.00 12.47 ? 113 SER A CA 1 +ATOM 947 C C . SER A 1 113 ? 7.324 -3.072 3.152 1.00 12.94 ? 113 SER A C 1 +ATOM 948 O O . SER A 1 113 ? 8.199 -3.891 3.424 1.00 13.55 ? 113 SER A O 1 +ATOM 949 C CB . SER A 1 113 ? 6.494 -3.535 0.894 1.00 13.09 ? 113 SER A CB 1 +ATOM 950 O OG . SER A 1 113 ? 6.426 -3.026 -0.426 1.00 14.30 ? 113 SER A OG 1 +ATOM 951 N N . VAL A 1 114 ? 6.388 -2.710 4.000 1.00 12.29 ? 114 VAL A N 1 +ATOM 952 C CA . VAL A 1 114 ? 6.309 -3.243 5.354 1.00 12.81 ? 114 VAL A CA 1 +ATOM 953 C C . VAL A 1 114 ? 5.016 -4.014 5.481 1.00 13.03 ? 114 VAL A C 1 +ATOM 954 O O . VAL A 1 114 ? 3.956 -3.520 5.093 1.00 13.21 ? 114 VAL A O 1 +ATOM 955 C CB . VAL A 1 114 ? 6.321 -2.096 6.393 1.00 12.98 ? 114 VAL A CB 1 +ATOM 956 C CG1 . VAL A 1 114 ? 5.995 -2.605 7.800 1.00 13.23 ? 114 VAL A CG1 1 +ATOM 957 C CG2 . VAL A 1 114 ? 7.642 -1.359 6.377 1.00 13.58 ? 114 VAL A CG2 1 +ATOM 958 N N . LEU A 1 115 ? 5.084 -5.218 6.060 1.00 12.47 ? 115 LEU A N 1 +ATOM 959 C CA . LEU A 1 115 ? 3.894 -5.974 6.346 1.00 12.54 ? 115 LEU A CA 1 +ATOM 960 C C . LEU A 1 115 ? 3.703 -5.818 7.851 1.00 12.81 ? 115 LEU A C 1 +ATOM 961 O O . LEU A 1 115 ? 4.403 -6.474 8.629 1.00 13.18 ? 115 LEU A O 1 +ATOM 962 C CB . LEU A 1 115 ? 4.037 -7.458 5.964 1.00 12.90 ? 115 LEU A CB 1 +ATOM 963 C CG . LEU A 1 115 ? 2.822 -8.307 6.284 1.00 14.50 ? 115 LEU A CG 1 +ATOM 964 C CD1 . LEU A 1 115 ? 1.620 -7.870 5.469 1.00 15.37 ? 115 LEU A CD1 1 +ATOM 965 C CD2 . LEU A 1 115 ? 3.100 -9.764 6.033 1.00 14.68 ? 115 LEU A CD2 1 +ATOM 966 N N A ALA A 1 116 ? 2.831 -4.892 8.282 0.50 12.53 ? 116 ALA A N 1 +ATOM 967 N N B ALA A 1 116 ? 2.781 -4.931 8.250 0.50 12.98 ? 116 ALA A N 1 +ATOM 968 C CA A ALA A 1 116 ? 2.624 -4.675 9.718 0.50 13.17 ? 116 ALA A CA 1 +ATOM 969 C CA B ALA A 1 116 ? 2.439 -4.683 9.648 0.50 14.18 ? 116 ALA A CA 1 +ATOM 970 C C A ALA A 1 116 ? 1.810 -5.835 10.275 0.50 13.37 ? 116 ALA A C 1 +ATOM 971 C C B ALA A 1 116 ? 1.816 -5.963 10.194 0.50 14.72 ? 116 ALA A C 1 +ATOM 972 O O A ALA A 1 116 ? 0.739 -6.137 9.755 0.50 13.60 ? 116 ALA A O 1 +ATOM 973 O O B ALA A 1 116 ? 0.984 -6.577 9.520 0.50 15.10 ? 116 ALA A O 1 +ATOM 974 C CB A ALA A 1 116 ? 1.907 -3.354 9.963 0.50 13.83 ? 116 ALA A CB 1 +ATOM 975 C CB B ALA A 1 116 ? 1.442 -3.535 9.736 0.50 14.78 ? 116 ALA A CB 1 +ATOM 976 N N A CYS A 1 117 ? 2.327 -6.495 11.304 0.75 13.30 ? 117 CYS A N 1 +ATOM 977 N N B CYS A 1 117 ? 2.247 -6.387 11.372 0.25 14.79 ? 117 CYS A N 1 +ATOM 978 C CA A CYS A 1 117 ? 1.697 -7.643 11.954 0.75 13.87 ? 117 CYS A CA 1 +ATOM 979 C CA B CYS A 1 117 ? 1.815 -7.651 11.942 0.25 15.40 ? 117 CYS A CA 1 +ATOM 980 C C A CYS A 1 117 ? 1.506 -7.426 13.414 0.75 14.56 ? 117 CYS A C 1 +ATOM 981 C C B CYS A 1 117 ? 1.597 -7.519 13.450 0.25 15.40 ? 117 CYS A C 1 +ATOM 982 O O A CYS A 1 117 ? 2.265 -6.683 14.028 0.75 14.38 ? 117 CYS A O 1 +ATOM 983 O O B CYS A 1 117 ? 2.357 -6.821 14.110 0.25 15.48 ? 117 CYS A O 1 +ATOM 984 C CB A CYS A 1 117 ? 2.543 -8.892 11.752 0.75 14.43 ? 117 CYS A CB 1 +ATOM 985 C CB B CYS A 1 117 ? 2.882 -8.701 11.636 0.25 16.62 ? 117 CYS A CB 1 +ATOM 986 S SG A CYS A 1 117 ? 2.803 -9.323 10.034 0.75 14.59 ? 117 CYS A SG 1 +ATOM 987 S SG B CYS A 1 117 ? 2.292 -10.412 11.656 0.25 20.52 ? 117 CYS A SG 1 +ATOM 988 N N . TYR A 1 118 ? 0.570 -8.188 13.997 1.00 15.18 ? 118 TYR A N 1 +ATOM 989 C CA . TYR A 1 118 ? 0.296 -8.220 15.447 1.00 16.61 ? 118 TYR A CA 1 +ATOM 990 C C . TYR A 1 118 ? -0.002 -9.668 15.797 1.00 18.17 ? 118 TYR A C 1 +ATOM 991 O O . TYR A 1 118 ? -0.763 -10.310 15.085 1.00 18.33 ? 118 TYR A O 1 +ATOM 992 C CB . TYR A 1 118 ? -0.905 -7.330 15.835 1.00 17.19 ? 118 TYR A CB 1 +ATOM 993 C CG . TYR A 1 118 ? -0.613 -5.889 15.531 1.00 17.88 ? 118 TYR A CG 1 +ATOM 994 C CD1 . TYR A 1 118 ? 0.120 -5.113 16.416 1.00 18.60 ? 118 TYR A CD1 1 +ATOM 995 C CD2 . TYR A 1 118 ? -0.904 -5.351 14.286 1.00 18.85 ? 118 TYR A CD2 1 +ATOM 996 C CE1 . TYR A 1 118 ? 0.471 -3.810 16.108 1.00 19.34 ? 118 TYR A CE1 1 +ATOM 997 C CE2 . TYR A 1 118 ? -0.509 -4.069 13.946 1.00 19.60 ? 118 TYR A CE2 1 +ATOM 998 C CZ . TYR A 1 118 ? 0.167 -3.297 14.865 1.00 20.22 ? 118 TYR A CZ 1 +ATOM 999 O OH . TYR A 1 118 ? 0.539 -2.027 14.526 1.00 21.79 ? 118 TYR A OH 1 +ATOM 1000 N N . ASN A 1 119 ? 0.643 -10.210 16.842 1.00 18.87 ? 119 ASN A N 1 +ATOM 1001 C CA . ASN A 1 119 ? 0.439 -11.600 17.254 1.00 20.10 ? 119 ASN A CA 1 +ATOM 1002 C C . ASN A 1 119 ? 0.702 -12.594 16.117 1.00 19.55 ? 119 ASN A C 1 +ATOM 1003 O O . ASN A 1 119 ? -0.008 -13.593 15.977 1.00 20.20 ? 119 ASN A O 1 +ATOM 1004 C CB . ASN A 1 119 ? -0.981 -11.790 17.805 1.00 22.64 ? 119 ASN A CB 1 +ATOM 1005 C CG . ASN A 1 119 ? -1.294 -10.896 18.970 1.00 27.97 ? 119 ASN A CG 1 +ATOM 1006 O OD1 . ASN A 1 119 ? -2.158 -10.021 18.891 1.00 30.85 ? 119 ASN A OD1 1 +ATOM 1007 N ND2 . ASN A 1 119 ? -0.591 -11.091 20.070 1.00 29.18 ? 119 ASN A ND2 1 +ATOM 1008 N N . GLY A 1 120 ? 1.679 -12.285 15.272 1.00 18.20 ? 120 GLY A N 1 +ATOM 1009 C CA . GLY A 1 120 ? 2.021 -13.141 14.143 1.00 17.98 ? 120 GLY A CA 1 +ATOM 1010 C C . GLY A 1 120 ? 1.039 -13.089 12.987 1.00 18.05 ? 120 GLY A C 1 +ATOM 1011 O O . GLY A 1 120 ? 1.168 -13.860 12.037 1.00 18.15 ? 120 GLY A O 1 +ATOM 1012 N N . SER A 1 121 ? 0.031 -12.200 13.059 1.00 17.88 ? 121 SER A N 1 +ATOM 1013 C CA . SER A 1 121 ? -0.988 -12.098 12.025 1.00 19.05 ? 121 SER A CA 1 +ATOM 1014 C C . SER A 1 121 ? -0.884 -10.784 11.263 1.00 19.31 ? 121 SER A C 1 +ATOM 1015 O O . SER A 1 121 ? -0.858 -9.709 11.855 1.00 18.83 ? 121 SER A O 1 +ATOM 1016 C CB . SER A 1 121 ? -2.379 -12.227 12.637 1.00 21.46 ? 121 SER A CB 1 +ATOM 1017 O OG . SER A 1 121 ? -2.553 -13.527 13.175 1.00 25.54 ? 121 SER A OG 1 +ATOM 1018 N N . PRO A 1 122 ? -0.842 -10.855 9.929 1.00 20.18 ? 122 PRO A N 1 +ATOM 1019 C CA . PRO A 1 122 ? -0.716 -9.623 9.136 1.00 20.36 ? 122 PRO A CA 1 +ATOM 1020 C C . PRO A 1 122 ? -1.952 -8.725 9.210 1.00 20.01 ? 122 PRO A C 1 +ATOM 1021 O O . PRO A 1 122 ? -3.095 -9.193 9.177 1.00 20.24 ? 122 PRO A O 1 +ATOM 1022 C CB . PRO A 1 122 ? -0.453 -10.148 7.715 1.00 22.14 ? 122 PRO A CB 1 +ATOM 1023 C CG . PRO A 1 122 ? 0.095 -11.574 7.925 1.00 22.93 ? 122 PRO A CG 1 +ATOM 1024 C CD . PRO A 1 122 ? -0.761 -12.055 9.076 1.00 20.91 ? 122 PRO A CD 1 +ATOM 1025 N N . SER A 1 123 ? -1.723 -7.421 9.339 1.00 19.28 ? 123 SER A N 1 +ATOM 1026 C CA . SER A 1 123 ? -2.812 -6.455 9.398 1.00 19.98 ? 123 SER A CA 1 +ATOM 1027 C C . SER A 1 123 ? -2.866 -5.587 8.166 1.00 19.22 ? 123 SER A C 1 +ATOM 1028 O O . SER A 1 123 ? -3.958 -5.209 7.743 1.00 19.82 ? 123 SER A O 1 +ATOM 1029 C CB . SER A 1 123 ? -2.716 -5.583 10.640 1.00 23.07 ? 123 SER A CB 1 +ATOM 1030 O OG . SER A 1 123 ? -1.507 -4.852 10.632 1.00 27.68 ? 123 SER A OG 1 +ATOM 1031 N N . GLY A 1 124 ? -1.705 -5.226 7.622 1.00 17.37 ? 124 GLY A N 1 +ATOM 1032 C CA . GLY A 1 124 ? -1.677 -4.368 6.453 1.00 16.81 ? 124 GLY A CA 1 +ATOM 1033 C C . GLY A 1 124 ? -0.319 -4.237 5.824 1.00 15.64 ? 124 GLY A C 1 +ATOM 1034 O O . GLY A 1 124 ? 0.683 -4.635 6.408 1.00 14.83 ? 124 GLY A O 1 +ATOM 1035 N N . VAL A 1 125 ? -0.281 -3.697 4.620 1.00 15.52 ? 125 VAL A N 1 +ATOM 1036 C CA . VAL A 1 125 ? 0.955 -3.526 3.900 1.00 16.15 ? 125 VAL A CA 1 +ATOM 1037 C C . VAL A 1 125 ? 1.037 -2.116 3.362 1.00 16.23 ? 125 VAL A C 1 +ATOM 1038 O O . VAL A 1 125 ? 0.028 -1.552 2.933 1.00 16.69 ? 125 VAL A O 1 +ATOM 1039 C CB . VAL A 1 125 ? 1.136 -4.627 2.825 1.00 18.52 ? 125 VAL A CB 1 +ATOM 1040 C CG1 . VAL A 1 125 ? 0.022 -4.589 1.791 1.00 20.02 ? 125 VAL A CG1 1 +ATOM 1041 C CG2 . VAL A 1 125 ? 2.511 -4.563 2.175 1.00 19.01 ? 125 VAL A CG2 1 +ATOM 1042 N N . TYR A 1 126 ? 2.205 -1.514 3.481 1.00 16.20 ? 126 TYR A N 1 +ATOM 1043 C CA . TYR A 1 126 ? 2.408 -0.148 3.015 1.00 16.17 ? 126 TYR A CA 1 +ATOM 1044 C C . TYR A 1 126 ? 3.842 0.066 2.588 1.00 15.60 ? 126 TYR A C 1 +ATOM 1045 O O . TYR A 1 126 ? 4.736 -0.688 2.960 1.00 15.94 ? 126 TYR A O 1 +ATOM 1046 C CB . TYR A 1 126 ? 1.958 0.884 4.064 1.00 16.49 ? 126 TYR A CB 1 +ATOM 1047 C CG . TYR A 1 126 ? 2.669 0.757 5.389 1.00 17.12 ? 126 TYR A CG 1 +ATOM 1048 C CD1 . TYR A 1 126 ? 3.901 1.356 5.601 1.00 17.77 ? 126 TYR A CD1 1 +ATOM 1049 C CD2 . TYR A 1 126 ? 2.115 0.027 6.430 1.00 18.46 ? 126 TYR A CD2 1 +ATOM 1050 C CE1 . TYR A 1 126 ? 4.560 1.241 6.817 1.00 18.59 ? 126 TYR A CE1 1 +ATOM 1051 C CE2 . TYR A 1 126 ? 2.758 -0.085 7.654 1.00 19.26 ? 126 TYR A CE2 1 +ATOM 1052 C CZ . TYR A 1 126 ? 3.979 0.529 7.845 1.00 19.71 ? 126 TYR A CZ 1 +ATOM 1053 O OH . TYR A 1 126 ? 4.608 0.427 9.064 1.00 22.38 ? 126 TYR A OH 1 +ATOM 1054 N N A GLN A 1 127 ? 4.050 1.061 1.748 0.50 15.62 ? 127 GLN A N 1 +ATOM 1055 N N B GLN A 1 127 ? 4.090 1.164 1.886 0.50 15.49 ? 127 GLN A N 1 +ATOM 1056 C CA A GLN A 1 127 ? 5.336 1.360 1.175 0.50 15.80 ? 127 GLN A CA 1 +ATOM 1057 C CA B GLN A 1 127 ? 5.413 1.506 1.423 0.50 15.72 ? 127 GLN A CA 1 +ATOM 1058 C C A GLN A 1 127 ? 5.965 2.540 1.890 0.50 16.49 ? 127 GLN A C 1 +ATOM 1059 C C B GLN A 1 127 ? 6.095 2.480 2.372 0.50 16.20 ? 127 GLN A C 1 +ATOM 1060 O O A GLN A 1 127 ? 5.306 3.560 2.092 0.50 16.63 ? 127 GLN A O 1 +ATOM 1061 O O B GLN A 1 127 ? 5.462 3.402 2.878 0.50 16.36 ? 127 GLN A O 1 +ATOM 1062 C CB A GLN A 1 127 ? 5.117 1.674 -0.313 0.50 16.38 ? 127 GLN A CB 1 +ATOM 1063 C CB B GLN A 1 127 ? 5.315 2.096 0.015 0.50 17.00 ? 127 GLN A CB 1 +ATOM 1064 C CG A GLN A 1 127 ? 6.368 1.792 -1.131 0.50 18.09 ? 127 GLN A CG 1 +ATOM 1065 C CG B GLN A 1 127 ? 6.631 2.112 -0.715 0.50 19.17 ? 127 GLN A CG 1 +ATOM 1066 C CD A GLN A 1 127 ? 7.089 0.490 -1.349 0.50 18.85 ? 127 GLN A CD 1 +ATOM 1067 C CD B GLN A 1 127 ? 7.033 0.761 -1.249 0.50 19.69 ? 127 GLN A CD 1 +ATOM 1068 O OE1 A GLN A 1 127 ? 6.666 -0.598 -0.912 0.50 18.45 ? 127 GLN A OE1 1 +ATOM 1069 O OE1 B GLN A 1 127 ? 6.501 -0.300 -0.868 0.50 20.09 ? 127 GLN A OE1 1 +ATOM 1070 N NE2 A GLN A 1 127 ? 8.210 0.583 -2.023 0.50 19.51 ? 127 GLN A NE2 1 +ATOM 1071 N NE2 B GLN A 1 127 ? 8.008 0.774 -2.125 0.50 19.03 ? 127 GLN A NE2 1 +ATOM 1072 N N A CYS A 1 128 ? 7.225 2.400 2.294 0.50 16.47 ? 128 CYS A N 1 +ATOM 1073 N N B CYS A 1 128 ? 7.382 2.261 2.606 0.50 16.43 ? 128 CYS A N 1 +ATOM 1074 C CA A CYS A 1 128 ? 7.942 3.478 2.975 0.50 16.78 ? 128 CYS A CA 1 +ATOM 1075 C CA B CYS A 1 128 ? 8.255 3.071 3.448 0.50 17.09 ? 128 CYS A CA 1 +ATOM 1076 C C A CYS A 1 128 ? 9.416 3.592 2.486 0.50 16.85 ? 128 CYS A C 1 +ATOM 1077 C C B CYS A 1 128 ? 9.557 3.356 2.718 0.50 17.04 ? 128 CYS A C 1 +ATOM 1078 O O A CYS A 1 128 ? 9.746 3.008 1.463 0.50 16.70 ? 128 CYS A O 1 +ATOM 1079 O O B CYS A 1 128 ? 9.936 2.632 1.810 0.50 16.87 ? 128 CYS A O 1 +ATOM 1080 C CB A CYS A 1 128 ? 7.831 3.331 4.489 0.50 17.30 ? 128 CYS A CB 1 +ATOM 1081 C CB B CYS A 1 128 ? 8.549 2.332 4.751 0.50 18.43 ? 128 CYS A CB 1 +ATOM 1082 S SG A CYS A 1 128 ? 8.691 1.883 5.141 0.50 19.72 ? 128 CYS A SG 1 +ATOM 1083 S SG B CYS A 1 128 ? 7.272 2.509 6.011 0.50 23.03 ? 128 CYS A SG 1 +ATOM 1084 N N . ALA A 1 129 ? 10.286 4.364 3.171 1.00 17.09 ? 129 ALA A N 1 +ATOM 1085 C CA . ALA A 1 129 ? 11.650 4.578 2.712 1.00 17.20 ? 129 ALA A CA 1 +ATOM 1086 C C . ALA A 1 129 ? 12.538 4.679 3.922 1.00 16.36 ? 129 ALA A C 1 +ATOM 1087 O O . ALA A 1 129 ? 12.115 5.142 4.987 1.00 17.23 ? 129 ALA A O 1 +ATOM 1088 C CB . ALA A 1 129 ? 11.767 5.848 1.894 1.00 17.51 ? 129 ALA A CB 1 +ATOM 1089 N N . MET A 1 130 ? 13.787 4.272 3.753 1.00 14.85 ? 130 MET A N 1 +ATOM 1090 C CA . MET A 1 130 ? 14.793 4.474 4.787 1.00 14.43 ? 130 MET A CA 1 +ATOM 1091 C C . MET A 1 130 ? 15.149 5.964 4.667 1.00 14.95 ? 130 MET A C 1 +ATOM 1092 O O . MET A 1 130 ? 15.626 6.382 3.618 1.00 15.32 ? 130 MET A O 1 +ATOM 1093 C CB . MET A 1 130 ? 16.023 3.600 4.511 1.00 14.88 ? 130 MET A CB 1 +ATOM 1094 C CG . MET A 1 130 ? 17.144 3.773 5.526 1.00 16.66 ? 130 MET A CG 1 +ATOM 1095 S SD . MET A 1 130 ? 16.663 3.502 7.255 1.00 17.10 ? 130 MET A SD 1 +ATOM 1096 C CE . MET A 1 130 ? 15.931 1.868 7.146 1.00 15.89 ? 130 MET A CE 1 +ATOM 1097 N N . ARG A 1 131 ? 14.805 6.763 5.672 1.00 14.67 ? 131 ARG A N 1 +ATOM 1098 C CA . ARG A 1 131 ? 15.075 8.199 5.615 1.00 14.63 ? 131 ARG A CA 1 +ATOM 1099 C C . ARG A 1 131 ? 16.579 8.470 5.700 1.00 15.11 ? 131 ARG A C 1 +ATOM 1100 O O . ARG A 1 131 ? 17.321 7.663 6.261 1.00 15.31 ? 131 ARG A O 1 +ATOM 1101 C CB . ARG A 1 131 ? 14.359 8.906 6.784 1.00 14.75 ? 131 ARG A CB 1 +ATOM 1102 C CG . ARG A 1 131 ? 12.853 8.693 6.868 1.00 15.21 ? 131 ARG A CG 1 +ATOM 1103 C CD . ARG A 1 131 ? 12.112 9.087 5.600 1.00 15.22 ? 131 ARG A CD 1 +ATOM 1104 N NE . ARG A 1 131 ? 12.512 10.422 5.144 1.00 14.93 ? 131 ARG A NE 1 +ATOM 1105 C CZ . ARG A 1 131 ? 12.205 10.925 3.951 1.00 14.97 ? 131 ARG A CZ 1 +ATOM 1106 N NH1 . ARG A 1 131 ? 11.460 10.230 3.101 1.00 14.04 ? 131 ARG A NH1 1 +ATOM 1107 N NH2 . ARG A 1 131 ? 12.629 12.136 3.606 1.00 14.38 ? 131 ARG A NH2 1 +ATOM 1108 N N . PRO A 1 132 ? 17.057 9.636 5.226 1.00 15.38 ? 132 PRO A N 1 +ATOM 1109 C CA . PRO A 1 132 ? 18.491 9.948 5.366 1.00 15.82 ? 132 PRO A CA 1 +ATOM 1110 C C . PRO A 1 132 ? 18.982 9.985 6.832 1.00 16.21 ? 132 PRO A C 1 +ATOM 1111 O O . PRO A 1 132 ? 20.180 9.803 7.070 1.00 17.50 ? 132 PRO A O 1 +ATOM 1112 C CB . PRO A 1 132 ? 18.614 11.299 4.676 1.00 16.65 ? 132 PRO A CB 1 +ATOM 1113 C CG . PRO A 1 132 ? 17.506 11.284 3.656 1.00 16.44 ? 132 PRO A CG 1 +ATOM 1114 C CD . PRO A 1 132 ? 16.361 10.665 4.424 1.00 15.17 ? 132 PRO A CD 1 +ATOM 1115 N N . ASN A 1 133 ? 18.087 10.206 7.816 1.00 14.91 ? 133 ASN A N 1 +ATOM 1116 C CA . ASN A 1 133 ? 18.488 10.161 9.234 1.00 14.67 ? 133 ASN A CA 1 +ATOM 1117 C C . ASN A 1 133 ? 18.338 8.731 9.835 1.00 14.76 ? 133 ASN A C 1 +ATOM 1118 O O . ASN A 1 133 ? 18.393 8.562 11.050 1.00 14.97 ? 133 ASN A O 1 +ATOM 1119 C CB . ASN A 1 133 ? 17.697 11.176 10.071 1.00 15.33 ? 133 ASN A CB 1 +ATOM 1120 C CG . ASN A 1 133 ? 16.214 10.909 10.098 1.00 15.79 ? 133 ASN A CG 1 +ATOM 1121 O OD1 . ASN A 1 133 ? 15.728 9.883 9.605 1.00 15.06 ? 133 ASN A OD1 1 +ATOM 1122 N ND2 . ASN A 1 133 ? 15.454 11.831 10.669 1.00 16.61 ? 133 ASN A ND2 1 +ATOM 1123 N N . PHE A 1 134 ? 18.104 7.718 8.982 1.00 14.43 ? 134 PHE A N 1 +ATOM 1124 C CA . PHE A 1 134 ? 18.012 6.312 9.351 1.00 15.16 ? 134 PHE A CA 1 +ATOM 1125 C C . PHE A 1 134 ? 16.803 5.931 10.198 1.00 15.02 ? 134 PHE A C 1 +ATOM 1126 O O . PHE A 1 134 ? 16.792 4.877 10.839 1.00 15.26 ? 134 PHE A O 1 +ATOM 1127 C CB . PHE A 1 134 ? 19.291 5.830 10.006 1.00 15.66 ? 134 PHE A CB 1 +ATOM 1128 C CG . PHE A 1 134 ? 20.480 5.964 9.086 1.00 17.62 ? 134 PHE A CG 1 +ATOM 1129 C CD1 . PHE A 1 134 ? 20.732 5.016 8.114 1.00 19.31 ? 134 PHE A CD1 1 +ATOM 1130 C CD2 . PHE A 1 134 ? 21.369 7.012 9.226 1.00 19.06 ? 134 PHE A CD2 1 +ATOM 1131 C CE1 . PHE A 1 134 ? 21.843 5.131 7.281 1.00 20.53 ? 134 PHE A CE1 1 +ATOM 1132 C CE2 . PHE A 1 134 ? 22.476 7.120 8.396 1.00 20.32 ? 134 PHE A CE2 1 +ATOM 1133 C CZ . PHE A 1 134 ? 22.710 6.176 7.437 1.00 20.35 ? 134 PHE A CZ 1 +ATOM 1134 N N . THR A 1 135 ? 15.760 6.743 10.140 1.00 14.48 ? 135 THR A N 1 +ATOM 1135 C CA . THR A 1 135 ? 14.475 6.389 10.724 1.00 14.62 ? 135 THR A CA 1 +ATOM 1136 C C . THR A 1 135 ? 13.558 5.992 9.541 1.00 14.74 ? 135 THR A C 1 +ATOM 1137 O O . THR A 1 135 ? 13.902 6.189 8.367 1.00 14.52 ? 135 THR A O 1 +ATOM 1138 C CB . THR A 1 135 ? 13.860 7.611 11.436 1.00 15.36 ? 135 THR A CB 1 +ATOM 1139 O OG1 . THR A 1 135 ? 13.529 8.620 10.477 1.00 16.63 ? 135 THR A OG1 1 +ATOM 1140 C CG2 . THR A 1 135 ? 14.745 8.161 12.529 1.00 15.23 ? 135 THR A CG2 1 +ATOM 1141 N N . ILE A 1 136 ? 12.395 5.430 9.852 1.00 14.48 ? 136 ILE A N 1 +ATOM 1142 C CA . ILE A 1 136 ? 11.362 5.231 8.863 1.00 15.24 ? 136 ILE A CA 1 +ATOM 1143 C C . ILE A 1 136 ? 10.103 5.840 9.436 1.00 15.66 ? 136 ILE A C 1 +ATOM 1144 O O . ILE A 1 136 ? 9.949 5.927 10.654 1.00 15.42 ? 136 ILE A O 1 +ATOM 1145 C CB . ILE A 1 136 ? 11.154 3.773 8.380 1.00 16.56 ? 136 ILE A CB 1 +ATOM 1146 C CG1 . ILE A 1 136 ? 10.532 2.890 9.459 1.00 17.44 ? 136 ILE A CG1 1 +ATOM 1147 C CG2 . ILE A 1 136 ? 12.448 3.165 7.826 1.00 17.63 ? 136 ILE A CG2 1 +ATOM 1148 C CD1 . ILE A 1 136 ? 9.987 1.590 8.900 1.00 18.35 ? 136 ILE A CD1 1 +ATOM 1149 N N A LYS A 1 137 ? 9.196 6.293 8.569 0.50 16.39 ? 137 LYS A N 1 +ATOM 1150 N N B LYS A 1 137 ? 9.209 6.274 8.558 0.50 16.47 ? 137 LYS A N 1 +ATOM 1151 C CA A LYS A 1 137 ? 7.929 6.844 9.037 0.50 17.56 ? 137 LYS A CA 1 +ATOM 1152 C CA B LYS A 1 137 ? 7.936 6.833 8.974 0.50 17.72 ? 137 LYS A CA 1 +ATOM 1153 C C A LYS A 1 137 ? 6.887 5.782 8.750 0.50 17.91 ? 137 LYS A C 1 +ATOM 1154 C C B LYS A 1 137 ? 6.920 5.736 8.717 0.50 17.94 ? 137 LYS A C 1 +ATOM 1155 O O A LYS A 1 137 ? 6.343 5.738 7.658 0.50 18.13 ? 137 LYS A O 1 +ATOM 1156 O O B LYS A 1 137 ? 6.413 5.631 7.608 0.50 18.10 ? 137 LYS A O 1 +ATOM 1157 C CB A LYS A 1 137 ? 7.610 8.173 8.334 0.50 20.10 ? 137 LYS A CB 1 +ATOM 1158 C CB B LYS A 1 137 ? 7.601 8.067 8.115 0.50 20.49 ? 137 LYS A CB 1 +ATOM 1159 C CG A LYS A 1 137 ? 8.672 9.240 8.580 0.50 24.65 ? 137 LYS A CG 1 +ATOM 1160 C CG B LYS A 1 137 ? 8.547 9.239 8.322 0.50 25.54 ? 137 LYS A CG 1 +ATOM 1161 C CD A LYS A 1 137 ? 8.340 10.542 7.865 0.50 28.93 ? 137 LYS A CD 1 +ATOM 1162 C CD B LYS A 1 137 ? 8.454 10.239 7.173 0.50 29.94 ? 137 LYS A CD 1 +ATOM 1163 C CE A LYS A 1 137 ? 7.600 11.508 8.754 0.50 32.40 ? 137 LYS A CE 1 +ATOM 1164 C CE B LYS A 1 137 ? 8.724 11.649 7.635 0.50 33.45 ? 137 LYS A CE 1 +ATOM 1165 N NZ A LYS A 1 137 ? 8.483 12.051 9.819 0.50 34.48 ? 137 LYS A NZ 1 +ATOM 1166 N NZ B LYS A 1 137 ? 9.352 12.475 6.565 0.50 34.98 ? 137 LYS A NZ 1 +ATOM 1167 N N . GLY A 1 138 ? 6.673 4.891 9.709 1.00 17.84 ? 138 GLY A N 1 +ATOM 1168 C CA . GLY A 1 138 ? 5.745 3.780 9.550 1.00 18.27 ? 138 GLY A CA 1 +ATOM 1169 C C . GLY A 1 138 ? 4.449 3.921 10.307 1.00 17.75 ? 138 GLY A C 1 +ATOM 1170 O O . GLY A 1 138 ? 4.066 5.022 10.697 1.00 18.35 ? 138 GLY A O 1 +ATOM 1171 N N . SER A 1 139 ? 3.747 2.813 10.483 1.00 16.95 ? 139 SER A N 1 +ATOM 1172 C CA . SER A 1 139 ? 2.511 2.779 11.237 1.00 17.34 ? 139 SER A CA 1 +ATOM 1173 C C . SER A 1 139 ? 2.627 1.538 12.081 1.00 18.01 ? 139 SER A C 1 +ATOM 1174 O O . SER A 1 139 ? 2.438 0.427 11.594 1.00 18.46 ? 139 SER A O 1 +ATOM 1175 C CB . SER A 1 139 ? 1.310 2.717 10.300 1.00 18.70 ? 139 SER A CB 1 +ATOM 1176 O OG . SER A 1 139 ? 0.131 2.477 11.049 1.00 23.01 ? 139 SER A OG 1 +ATOM 1177 N N . PHE A 1 140 ? 3.090 1.719 13.311 1.00 17.22 ? 140 PHE A N 1 +ATOM 1178 C CA . PHE A 1 140 ? 3.374 0.600 14.192 1.00 17.88 ? 140 PHE A CA 1 +ATOM 1179 C C . PHE A 1 140 ? 2.824 0.838 15.576 1.00 20.15 ? 140 PHE A C 1 +ATOM 1180 O O . PHE A 1 140 ? 3.184 1.818 16.205 1.00 21.50 ? 140 PHE A O 1 +ATOM 1181 C CB . PHE A 1 140 ? 4.896 0.431 14.317 1.00 16.98 ? 140 PHE A CB 1 +ATOM 1182 C CG . PHE A 1 140 ? 5.648 0.038 13.067 1.00 16.74 ? 140 PHE A CG 1 +ATOM 1183 C CD1 . PHE A 1 140 ? 5.592 -1.254 12.584 1.00 17.75 ? 140 PHE A CD1 1 +ATOM 1184 C CD2 . PHE A 1 140 ? 6.484 0.939 12.430 1.00 16.89 ? 140 PHE A CD2 1 +ATOM 1185 C CE1 . PHE A 1 140 ? 6.315 -1.619 11.454 1.00 17.58 ? 140 PHE A CE1 1 +ATOM 1186 C CE2 . PHE A 1 140 ? 7.224 0.564 11.320 1.00 17.58 ? 140 PHE A CE2 1 +ATOM 1187 C CZ . PHE A 1 140 ? 7.144 -0.713 10.843 1.00 17.08 ? 140 PHE A CZ 1 +ATOM 1188 N N . LEU A 1 141 ? 2.006 -0.071 16.069 1.00 20.53 ? 141 LEU A N 1 +ATOM 1189 C CA . LEU A 1 141 ? 1.467 0.022 17.427 1.00 22.25 ? 141 LEU A CA 1 +ATOM 1190 C C . LEU A 1 141 ? 2.194 -0.996 18.303 1.00 22.71 ? 141 LEU A C 1 +ATOM 1191 O O . LEU A 1 141 ? 3.009 -1.765 17.799 1.00 22.61 ? 141 LEU A O 1 +ATOM 1192 C CB . LEU A 1 141 ? -0.022 -0.321 17.412 1.00 23.61 ? 141 LEU A CB 1 +ATOM 1193 C CG . LEU A 1 141 ? -0.880 0.558 16.561 1.00 26.86 ? 141 LEU A CG 1 +ATOM 1194 C CD1 . LEU A 1 141 ? -2.217 -0.070 16.370 1.00 28.11 ? 141 LEU A CD1 1 +ATOM 1195 C CD2 . LEU A 1 141 ? -1.000 1.953 17.161 1.00 27.94 ? 141 LEU A CD2 1 +ATOM 1196 N N . ASN A 1 142 ? 1.876 -1.054 19.615 1.00 23.13 ? 142 ASN A N 1 +ATOM 1197 C CA . ASN A 1 142 ? 2.473 -2.056 20.495 1.00 23.46 ? 142 ASN A CA 1 +ATOM 1198 C C . ASN A 1 142 ? 2.080 -3.453 20.002 1.00 21.95 ? 142 ASN A C 1 +ATOM 1199 O O . ASN A 1 142 ? 0.950 -3.667 19.566 1.00 22.17 ? 142 ASN A O 1 +ATOM 1200 C CB . ASN A 1 142 ? 2.077 -1.814 21.953 1.00 26.50 ? 142 ASN A CB 1 +ATOM 1201 C CG . ASN A 1 142 ? 2.744 -0.586 22.522 1.00 33.37 ? 142 ASN A CG 1 +ATOM 1202 O OD1 . ASN A 1 142 ? 3.924 -0.317 22.266 1.00 35.67 ? 142 ASN A OD1 1 +ATOM 1203 N ND2 . ASN A 1 142 ? 2.005 0.198 23.302 1.00 35.11 ? 142 ASN A ND2 1 +ATOM 1204 N N . GLY A 1 143 ? 3.065 -4.323 19.913 1.00 20.23 ? 143 GLY A N 1 +ATOM 1205 C CA . GLY A 1 143 ? 2.872 -5.658 19.374 1.00 18.71 ? 143 GLY A CA 1 +ATOM 1206 C C . GLY A 1 143 ? 3.365 -5.788 17.939 1.00 16.65 ? 143 GLY A C 1 +ATOM 1207 O O . GLY A 1 143 ? 3.442 -6.903 17.428 1.00 16.13 ? 143 GLY A O 1 +ATOM 1208 N N . SER A 1 144 ? 3.691 -4.663 17.268 1.00 15.41 ? 144 SER A N 1 +ATOM 1209 C CA . SER A 1 144 ? 4.151 -4.716 15.875 1.00 14.02 ? 144 SER A CA 1 +ATOM 1210 C C . SER A 1 144 ? 5.623 -5.030 15.716 1.00 13.25 ? 144 SER A C 1 +ATOM 1211 O O . SER A 1 144 ? 6.059 -5.283 14.594 1.00 12.34 ? 144 SER A O 1 +ATOM 1212 C CB . SER A 1 144 ? 3.856 -3.411 15.150 1.00 14.75 ? 144 SER A CB 1 +ATOM 1213 O OG . SER A 1 144 ? 4.555 -2.361 15.795 1.00 16.91 ? 144 SER A OG 1 +ATOM 1214 N N . CYS A 1 145 ? 6.413 -5.035 16.803 1.00 13.27 ? 145 CYS A N 1 +ATOM 1215 C CA . CYS A 1 145 ? 7.837 -5.364 16.678 1.00 13.16 ? 145 CYS A CA 1 +ATOM 1216 C C . CYS A 1 145 ? 8.043 -6.722 16.046 1.00 12.44 ? 145 CYS A C 1 +ATOM 1217 O O . CYS A 1 145 ? 7.218 -7.618 16.221 1.00 12.76 ? 145 CYS A O 1 +ATOM 1218 C CB . CYS A 1 145 ? 8.549 -5.254 18.016 1.00 14.52 ? 145 CYS A CB 1 +ATOM 1219 S SG . CYS A 1 145 ? 8.542 -3.580 18.699 1.00 19.18 ? 145 CYS A SG 1 +ATOM 1220 N N . GLY A 1 146 ? 9.054 -6.812 15.211 1.00 11.62 ? 146 GLY A N 1 +ATOM 1221 C CA . GLY A 1 146 ? 9.297 -8.040 14.474 1.00 11.65 ? 146 GLY A CA 1 +ATOM 1222 C C . GLY A 1 146 ? 8.639 -8.028 13.111 1.00 11.50 ? 146 GLY A C 1 +ATOM 1223 O O . GLY A 1 146 ? 8.938 -8.880 12.282 1.00 12.48 ? 146 GLY A O 1 +ATOM 1224 N N . SER A 1 147 ? 7.753 -7.040 12.831 1.00 11.19 ? 147 SER A N 1 +ATOM 1225 C CA . SER A 1 147 ? 7.204 -6.880 11.475 1.00 11.25 ? 147 SER A CA 1 +ATOM 1226 C C . SER A 1 147 ? 8.385 -6.510 10.565 1.00 11.68 ? 147 SER A C 1 +ATOM 1227 O O . SER A 1 147 ? 9.322 -5.827 11.010 1.00 11.33 ? 147 SER A O 1 +ATOM 1228 C CB . SER A 1 147 ? 6.210 -5.723 11.428 1.00 12.25 ? 147 SER A CB 1 +ATOM 1229 O OG . SER A 1 147 ? 5.054 -6.012 12.198 1.00 13.30 ? 147 SER A OG 1 +ATOM 1230 N N . VAL A 1 148 ? 8.354 -6.970 9.308 1.00 11.17 ? 148 VAL A N 1 +ATOM 1231 C CA . VAL A 1 148 ? 9.493 -6.779 8.444 1.00 11.78 ? 148 VAL A CA 1 +ATOM 1232 C C . VAL A 1 148 ? 9.223 -5.923 7.220 1.00 12.04 ? 148 VAL A C 1 +ATOM 1233 O O . VAL A 1 148 ? 8.088 -5.781 6.767 1.00 11.94 ? 148 VAL A O 1 +ATOM 1234 C CB . VAL A 1 148 ? 10.129 -8.138 8.036 1.00 12.63 ? 148 VAL A CB 1 +ATOM 1235 C CG1 . VAL A 1 148 ? 10.607 -8.914 9.260 1.00 12.66 ? 148 VAL A CG1 1 +ATOM 1236 C CG2 . VAL A 1 148 ? 9.180 -8.973 7.195 1.00 13.55 ? 148 VAL A CG2 1 +ATOM 1237 N N . GLY A 1 149 ? 10.312 -5.371 6.699 1.00 12.16 ? 149 GLY A N 1 +ATOM 1238 C CA . GLY A 1 149 ? 10.362 -4.619 5.460 1.00 12.30 ? 149 GLY A CA 1 +ATOM 1239 C C . GLY A 1 149 ? 11.095 -5.441 4.419 1.00 12.43 ? 149 GLY A C 1 +ATOM 1240 O O . GLY A 1 149 ? 12.033 -6.187 4.731 1.00 12.20 ? 149 GLY A O 1 +ATOM 1241 N N . PHE A 1 150 ? 10.650 -5.327 3.175 1.00 12.00 ? 150 PHE A N 1 +ATOM 1242 C CA . PHE A 1 150 ? 11.198 -6.146 2.114 1.00 13.19 ? 150 PHE A CA 1 +ATOM 1243 C C . PHE A 1 150 ? 10.981 -5.537 0.748 1.00 14.59 ? 150 PHE A C 1 +ATOM 1244 O O . PHE A 1 150 ? 10.124 -4.675 0.576 1.00 14.07 ? 150 PHE A O 1 +ATOM 1245 C CB . PHE A 1 150 ? 10.498 -7.529 2.164 1.00 13.42 ? 150 PHE A CB 1 +ATOM 1246 C CG . PHE A 1 150 ? 8.997 -7.465 1.967 1.00 14.35 ? 150 PHE A CG 1 +ATOM 1247 C CD1 . PHE A 1 150 ? 8.154 -7.170 3.021 1.00 15.42 ? 150 PHE A CD1 1 +ATOM 1248 C CD2 . PHE A 1 150 ? 8.432 -7.691 0.721 1.00 15.45 ? 150 PHE A CD2 1 +ATOM 1249 C CE1 . PHE A 1 150 ? 6.783 -7.040 2.825 1.00 16.35 ? 150 PHE A CE1 1 +ATOM 1250 C CE2 . PHE A 1 150 ? 7.052 -7.611 0.541 1.00 16.30 ? 150 PHE A CE2 1 +ATOM 1251 C CZ . PHE A 1 150 ? 6.239 -7.292 1.593 1.00 15.96 ? 150 PHE A CZ 1 +ATOM 1252 N N . ASN A 1 151 ? 11.734 -6.041 -0.222 1.00 15.13 ? 151 ASN A N 1 +ATOM 1253 C CA . ASN A 1 151 ? 11.561 -5.768 -1.644 1.00 16.70 ? 151 ASN A CA 1 +ATOM 1254 C C . ASN A 1 151 ? 11.469 -7.132 -2.334 1.00 18.24 ? 151 ASN A C 1 +ATOM 1255 O O . ASN A 1 151 ? 11.926 -8.137 -1.785 1.00 17.68 ? 151 ASN A O 1 +ATOM 1256 C CB . ASN A 1 151 ? 12.736 -4.982 -2.203 1.00 17.55 ? 151 ASN A CB 1 +ATOM 1257 C CG . ASN A 1 151 ? 12.678 -3.526 -1.848 1.00 21.16 ? 151 ASN A CG 1 +ATOM 1258 O OD1 . ASN A 1 151 ? 12.018 -2.729 -2.525 1.00 23.71 ? 151 ASN A OD1 1 +ATOM 1259 N ND2 . ASN A 1 151 ? 13.342 -3.149 -0.770 1.00 19.82 ? 151 ASN A ND2 1 +ATOM 1260 N N . ILE A 1 152 ? 10.860 -7.188 -3.527 1.00 19.82 ? 152 ILE A N 1 +ATOM 1261 C CA . ILE A 1 152 ? 10.779 -8.458 -4.255 1.00 22.59 ? 152 ILE A CA 1 +ATOM 1262 C C . ILE A 1 152 ? 11.333 -8.271 -5.655 1.00 25.21 ? 152 ILE A C 1 +ATOM 1263 O O . ILE A 1 152 ? 11.049 -7.265 -6.296 1.00 25.64 ? 152 ILE A O 1 +ATOM 1264 C CB . ILE A 1 152 ? 9.350 -9.069 -4.286 1.00 23.47 ? 152 ILE A CB 1 +ATOM 1265 C CG1 . ILE A 1 152 ? 8.720 -9.144 -2.884 1.00 24.58 ? 152 ILE A CG1 1 +ATOM 1266 C CG2 . ILE A 1 152 ? 9.360 -10.453 -4.972 1.00 24.13 ? 152 ILE A CG2 1 +ATOM 1267 C CD1 . ILE A 1 152 ? 7.304 -9.608 -2.866 1.00 25.76 ? 152 ILE A CD1 1 +ATOM 1268 N N . ASP A 1 153 ? 12.157 -9.211 -6.114 1.00 26.83 ? 153 ASP A N 1 +ATOM 1269 C CA . ASP A 1 153 ? 12.655 -9.198 -7.484 1.00 28.74 ? 153 ASP A CA 1 +ATOM 1270 C C . ASP A 1 153 ? 12.170 -10.512 -8.056 1.00 29.83 ? 153 ASP A C 1 +ATOM 1271 O O . ASP A 1 153 ? 12.773 -11.548 -7.779 1.00 30.55 ? 153 ASP A O 1 +ATOM 1272 C CB . ASP A 1 153 ? 14.184 -9.123 -7.546 1.00 31.89 ? 153 ASP A CB 1 +ATOM 1273 C CG . ASP A 1 153 ? 14.688 -8.981 -8.971 1.00 40.02 ? 153 ASP A CG 1 +ATOM 1274 O OD1 . ASP A 1 153 ? 13.977 -8.356 -9.795 1.00 41.47 ? 153 ASP A OD1 1 +ATOM 1275 O OD2 . ASP A 1 153 ? 15.789 -9.501 -9.268 1.00 43.80 ? 153 ASP A OD2 1 +ATOM 1276 N N . TYR A 1 154 ? 11.037 -10.469 -8.789 1.00 29.57 ? 154 TYR A N 1 +ATOM 1277 C CA . TYR A 1 154 ? 10.327 -11.603 -9.381 1.00 30.13 ? 154 TYR A CA 1 +ATOM 1278 C C . TYR A 1 154 ? 9.896 -12.627 -8.298 1.00 29.86 ? 154 TYR A C 1 +ATOM 1279 O O . TYR A 1 154 ? 8.809 -12.476 -7.736 1.00 30.57 ? 154 TYR A O 1 +ATOM 1280 C CB . TYR A 1 154 ? 11.081 -12.243 -10.574 0.50 30.31 ? 154 TYR A CB 1 +ATOM 1281 C CG . TYR A 1 154 ? 10.357 -13.446 -11.143 0.50 31.41 ? 154 TYR A CG 1 +ATOM 1282 C CD1 . TYR A 1 154 ? 9.054 -13.341 -11.609 0.50 32.51 ? 154 TYR A CD1 1 +ATOM 1283 C CD2 . TYR A 1 154 ? 10.964 -14.693 -11.188 0.50 32.38 ? 154 TYR A CD2 1 +ATOM 1284 C CE1 . TYR A 1 154 ? 8.372 -14.447 -12.100 0.50 33.48 ? 154 TYR A CE1 1 +ATOM 1285 C CE2 . TYR A 1 154 ? 10.290 -15.808 -11.669 0.50 33.42 ? 154 TYR A CE2 1 +ATOM 1286 C CZ . TYR A 1 154 ? 8.994 -15.680 -12.131 0.50 34.48 ? 154 TYR A CZ 1 +ATOM 1287 O OH . TYR A 1 154 ? 8.328 -16.774 -12.627 0.50 36.31 ? 154 TYR A OH 1 +ATOM 1288 N N . ASP A 1 155 ? 10.732 -13.629 -7.970 1.00 28.99 ? 155 ASP A N 1 +ATOM 1289 C CA . ASP A 1 155 ? 10.368 -14.624 -6.961 1.00 28.27 ? 155 ASP A CA 1 +ATOM 1290 C C . ASP A 1 155 ? 11.249 -14.600 -5.720 1.00 26.66 ? 155 ASP A C 1 +ATOM 1291 O O . ASP A 1 155 ? 11.085 -15.455 -4.854 1.00 27.06 ? 155 ASP A O 1 +ATOM 1292 C CB . ASP A 1 155 ? 10.346 -16.038 -7.566 1.00 30.93 ? 155 ASP A CB 1 +ATOM 1293 C CG . ASP A 1 155 ? 11.673 -16.511 -8.140 1.00 36.67 ? 155 ASP A CG 1 +ATOM 1294 O OD1 . ASP A 1 155 ? 12.607 -15.683 -8.250 1.00 37.43 ? 155 ASP A OD1 1 +ATOM 1295 O OD2 . ASP A 1 155 ? 11.772 -17.708 -8.495 1.00 39.58 ? 155 ASP A OD2 1 +ATOM 1296 N N . CYS A 1 156 ? 12.175 -13.637 -5.622 1.00 24.66 ? 156 CYS A N 1 +ATOM 1297 C CA . CYS A 1 156 ? 13.076 -13.566 -4.484 1.00 23.25 ? 156 CYS A CA 1 +ATOM 1298 C C . CYS A 1 156 ? 12.758 -12.398 -3.587 1.00 20.76 ? 156 CYS A C 1 +ATOM 1299 O O . CYS A 1 156 ? 12.827 -11.248 -4.023 1.00 20.48 ? 156 CYS A O 1 +ATOM 1300 C CB . CYS A 1 156 ? 14.525 -13.518 -4.955 1.00 24.48 ? 156 CYS A CB 1 +ATOM 1301 S SG . CYS A 1 156 ? 15.738 -13.478 -3.610 1.00 27.04 ? 156 CYS A SG 1 +ATOM 1302 N N . VAL A 1 157 ? 12.484 -12.680 -2.310 1.00 18.60 ? 157 VAL A N 1 +ATOM 1303 C CA . VAL A 1 157 ? 12.218 -11.620 -1.344 1.00 17.05 ? 157 VAL A CA 1 +ATOM 1304 C C . VAL A 1 157 ? 13.514 -11.180 -0.700 1.00 15.71 ? 157 VAL A C 1 +ATOM 1305 O O . VAL A 1 157 ? 14.196 -11.995 -0.084 1.00 15.50 ? 157 VAL A O 1 +ATOM 1306 C CB . VAL A 1 157 ? 11.247 -12.102 -0.243 1.00 17.28 ? 157 VAL A CB 1 +ATOM 1307 C CG1 . VAL A 1 157 ? 10.950 -10.990 0.757 1.00 17.60 ? 157 VAL A CG1 1 +ATOM 1308 C CG2 . VAL A 1 157 ? 9.958 -12.653 -0.847 1.00 18.06 ? 157 VAL A CG2 1 +ATOM 1309 N N . SER A 1 158 ? 13.840 -9.894 -0.794 1.00 15.06 ? 158 SER A N 1 +ATOM 1310 C CA . SER A 1 158 ? 15.008 -9.358 -0.111 1.00 14.90 ? 158 SER A CA 1 +ATOM 1311 C C . SER A 1 158 ? 14.517 -8.654 1.138 1.00 14.32 ? 158 SER A C 1 +ATOM 1312 O O . SER A 1 158 ? 13.944 -7.567 1.050 1.00 14.24 ? 158 SER A O 1 +ATOM 1313 C CB . SER A 1 158 ? 15.755 -8.366 -0.997 1.00 17.17 ? 158 SER A CB 1 +ATOM 1314 O OG . SER A 1 158 ? 16.436 -9.063 -2.024 1.00 20.62 ? 158 SER A OG 1 +ATOM 1315 N N . PHE A 1 159 ? 14.725 -9.276 2.299 1.00 13.50 ? 159 PHE A N 1 +ATOM 1316 C CA . PHE A 1 159 ? 14.327 -8.676 3.565 1.00 13.12 ? 159 PHE A CA 1 +ATOM 1317 C C . PHE A 1 159 ? 15.366 -7.649 3.959 1.00 12.99 ? 159 PHE A C 1 +ATOM 1318 O O . PHE A 1 159 ? 16.559 -7.954 3.983 1.00 13.40 ? 159 PHE A O 1 +ATOM 1319 C CB . PHE A 1 159 ? 14.245 -9.749 4.654 1.00 12.61 ? 159 PHE A CB 1 +ATOM 1320 C CG . PHE A 1 159 ? 13.131 -10.726 4.411 1.00 11.64 ? 159 PHE A CG 1 +ATOM 1321 C CD1 . PHE A 1 159 ? 11.819 -10.392 4.702 1.00 12.23 ? 159 PHE A CD1 1 +ATOM 1322 C CD2 . PHE A 1 159 ? 13.391 -11.978 3.887 1.00 11.94 ? 159 PHE A CD2 1 +ATOM 1323 C CE1 . PHE A 1 159 ? 10.793 -11.300 4.508 1.00 12.59 ? 159 PHE A CE1 1 +ATOM 1324 C CE2 . PHE A 1 159 ? 12.357 -12.881 3.669 1.00 12.59 ? 159 PHE A CE2 1 +ATOM 1325 C CZ . PHE A 1 159 ? 11.064 -12.538 3.991 1.00 12.27 ? 159 PHE A CZ 1 +ATOM 1326 N N . CYS A 1 160 ? 14.918 -6.444 4.317 1.00 12.93 ? 160 CYS A N 1 +ATOM 1327 C CA . CYS A 1 160 ? 15.839 -5.365 4.668 1.00 13.50 ? 160 CYS A CA 1 +ATOM 1328 C C . CYS A 1 160 ? 15.596 -4.739 6.011 1.00 13.22 ? 160 CYS A C 1 +ATOM 1329 O O . CYS A 1 160 ? 16.451 -3.984 6.456 1.00 13.85 ? 160 CYS A O 1 +ATOM 1330 C CB . CYS A 1 160 ? 15.838 -4.296 3.580 1.00 14.93 ? 160 CYS A CB 1 +ATOM 1331 S SG . CYS A 1 160 ? 14.213 -3.572 3.272 1.00 15.19 ? 160 CYS A SG 1 +ATOM 1332 N N . TYR A 1 161 ? 14.433 -4.952 6.614 1.00 12.04 ? 161 TYR A N 1 +ATOM 1333 C CA . TYR A 1 161 ? 14.112 -4.270 7.849 1.00 11.92 ? 161 TYR A CA 1 +ATOM 1334 C C . TYR A 1 161 ? 13.335 -5.134 8.797 1.00 11.21 ? 161 TYR A C 1 +ATOM 1335 O O . TYR A 1 161 ? 12.520 -5.929 8.377 1.00 11.05 ? 161 TYR A O 1 +ATOM 1336 C CB . TYR A 1 161 ? 13.272 -3.020 7.497 1.00 11.04 ? 161 TYR A CB 1 +ATOM 1337 C CG . TYR A 1 161 ? 12.873 -2.174 8.686 1.00 11.13 ? 161 TYR A CG 1 +ATOM 1338 C CD1 . TYR A 1 161 ? 13.734 -1.221 9.206 1.00 12.22 ? 161 TYR A CD1 1 +ATOM 1339 C CD2 . TYR A 1 161 ? 11.614 -2.292 9.256 1.00 11.72 ? 161 TYR A CD2 1 +ATOM 1340 C CE1 . TYR A 1 161 ? 13.370 -0.445 10.303 1.00 12.77 ? 161 TYR A CE1 1 +ATOM 1341 C CE2 . TYR A 1 161 ? 11.245 -1.535 10.356 1.00 12.42 ? 161 TYR A CE2 1 +ATOM 1342 C CZ . TYR A 1 161 ? 12.120 -0.604 10.873 1.00 12.57 ? 161 TYR A CZ 1 +ATOM 1343 O OH . TYR A 1 161 ? 11.751 0.138 11.977 1.00 12.95 ? 161 TYR A OH 1 +ATOM 1344 N N . MET A 1 162 ? 13.585 -4.974 10.085 1.00 10.28 ? 162 MET A N 1 +ATOM 1345 C CA . MET A 1 162 ? 12.783 -5.594 11.126 1.00 10.68 ? 162 MET A CA 1 +ATOM 1346 C C . MET A 1 162 ? 12.509 -4.476 12.131 1.00 10.72 ? 162 MET A C 1 +ATOM 1347 O O . MET A 1 162 ? 13.429 -3.757 12.531 1.00 10.71 ? 162 MET A O 1 +ATOM 1348 C CB . MET A 1 162 ? 13.469 -6.782 11.785 1.00 11.91 ? 162 MET A CB 1 +ATOM 1349 C CG . MET A 1 162 ? 12.631 -7.332 12.936 1.00 12.92 ? 162 MET A CG 1 +ATOM 1350 S SD . MET A 1 162 ? 13.162 -8.961 13.503 1.00 15.17 ? 162 MET A SD 1 +ATOM 1351 C CE . MET A 1 162 ? 12.432 -9.997 12.218 1.00 16.30 ? 162 MET A CE 1 +ATOM 1352 N N . HIS A 1 163 ? 11.245 -4.306 12.496 1.00 10.85 ? 163 HIS A N 1 +ATOM 1353 C CA . HIS A 1 163 ? 10.862 -3.230 13.394 1.00 10.78 ? 163 HIS A CA 1 +ATOM 1354 C C . HIS A 1 163 ? 11.218 -3.501 14.829 1.00 10.88 ? 163 HIS A C 1 +ATOM 1355 O O . HIS A 1 163 ? 10.858 -4.554 15.333 1.00 11.36 ? 163 HIS A O 1 +ATOM 1356 C CB . HIS A 1 163 ? 9.363 -2.967 13.299 1.00 11.80 ? 163 HIS A CB 1 +ATOM 1357 C CG . HIS A 1 163 ? 8.995 -1.754 14.072 1.00 12.60 ? 163 HIS A CG 1 +ATOM 1358 N ND1 . HIS A 1 163 ? 9.637 -0.545 13.857 1.00 13.89 ? 163 HIS A ND1 1 +ATOM 1359 C CD2 . HIS A 1 163 ? 8.139 -1.619 15.105 1.00 13.61 ? 163 HIS A CD2 1 +ATOM 1360 C CE1 . HIS A 1 163 ? 9.124 0.289 14.740 1.00 14.58 ? 163 HIS A CE1 1 +ATOM 1361 N NE2 . HIS A 1 163 ? 8.222 -0.307 15.514 1.00 14.16 ? 163 HIS A NE2 1 +ATOM 1362 N N . HIS A 1 164 ? 11.850 -2.524 15.504 1.00 10.72 ? 164 HIS A N 1 +ATOM 1363 C CA . HIS A 1 164 ? 12.191 -2.691 16.911 1.00 12.02 ? 164 HIS A CA 1 +ATOM 1364 C C . HIS A 1 164 ? 11.654 -1.626 17.827 1.00 13.54 ? 164 HIS A C 1 +ATOM 1365 O O . HIS A 1 164 ? 11.296 -1.961 18.960 1.00 14.57 ? 164 HIS A O 1 +ATOM 1366 C CB . HIS A 1 164 ? 13.720 -2.699 17.140 1.00 12.32 ? 164 HIS A CB 1 +ATOM 1367 C CG . HIS A 1 164 ? 14.408 -3.927 16.654 1.00 11.31 ? 164 HIS A CG 1 +ATOM 1368 N ND1 . HIS A 1 164 ? 15.090 -4.762 17.524 1.00 11.61 ? 164 HIS A ND1 1 +ATOM 1369 C CD2 . HIS A 1 164 ? 14.549 -4.392 15.393 1.00 11.50 ? 164 HIS A CD2 1 +ATOM 1370 C CE1 . HIS A 1 164 ? 15.623 -5.706 16.765 1.00 11.94 ? 164 HIS A CE1 1 +ATOM 1371 N NE2 . HIS A 1 164 ? 15.308 -5.537 15.478 1.00 12.33 ? 164 HIS A NE2 1 +ATOM 1372 N N A MET A 1 165 ? 11.586 -0.360 17.376 0.50 14.49 ? 165 MET A N 1 +ATOM 1373 N N B MET A 1 165 ? 11.783 -0.326 17.439 0.50 13.59 ? 165 MET A N 1 +ATOM 1374 C CA A MET A 1 165 ? 11.139 0.666 18.305 0.50 16.09 ? 165 MET A CA 1 +ATOM 1375 C CA B MET A 1 165 ? 11.504 0.797 18.336 0.50 14.00 ? 165 MET A CA 1 +ATOM 1376 C C A MET A 1 165 ? 10.595 1.912 17.722 0.50 15.90 ? 165 MET A C 1 +ATOM 1377 C C B MET A 1 165 ? 10.702 1.944 17.739 0.50 14.88 ? 165 MET A C 1 +ATOM 1378 O O A MET A 1 165 ? 10.776 2.215 16.550 0.50 15.72 ? 165 MET A O 1 +ATOM 1379 O O B MET A 1 165 ? 10.842 2.241 16.560 0.50 14.65 ? 165 MET A O 1 +ATOM 1380 C CB A MET A 1 165 ? 12.260 1.033 19.260 0.50 18.07 ? 165 MET A CB 1 +ATOM 1381 C CB B MET A 1 165 ? 12.844 1.448 18.767 0.50 13.85 ? 165 MET A CB 1 +ATOM 1382 C CG A MET A 1 165 ? 13.510 1.441 18.567 0.50 21.85 ? 165 MET A CG 1 +ATOM 1383 C CG B MET A 1 165 ? 13.883 0.481 19.312 0.50 14.29 ? 165 MET A CG 1 +ATOM 1384 S SD A MET A 1 165 ? 14.871 1.411 19.737 0.50 29.90 ? 165 MET A SD 1 +ATOM 1385 S SD B MET A 1 165 ? 13.470 -0.155 20.945 0.50 15.29 ? 165 MET A SD 1 +ATOM 1386 C CE A MET A 1 165 ? 14.286 0.130 20.907 0.50 30.34 ? 165 MET A CE 1 +ATOM 1387 C CE B MET A 1 165 ? 13.829 1.249 21.920 0.50 19.00 ? 165 MET A CE 1 +ATOM 1388 N N . GLU A 1 166 ? 9.962 2.669 18.591 1.00 16.13 ? 166 GLU A N 1 +ATOM 1389 C CA . GLU A 1 166 ? 9.355 3.908 18.240 1.00 17.53 ? 166 GLU A CA 1 +ATOM 1390 C C . GLU A 1 166 ? 10.049 4.945 19.115 1.00 19.53 ? 166 GLU A C 1 +ATOM 1391 O O . GLU A 1 166 ? 10.099 4.793 20.337 1.00 20.14 ? 166 GLU A O 1 +ATOM 1392 C CB . GLU A 1 166 ? 7.885 3.883 18.595 1.00 19.56 ? 166 GLU A CB 1 +ATOM 1393 C CG . GLU A 1 166 ? 7.200 5.177 18.243 1.00 23.51 ? 166 GLU A CG 1 +ATOM 1394 C CD . GLU A 1 166 ? 5.719 4.914 18.267 1.00 27.84 ? 166 GLU A CD 1 +ATOM 1395 O OE1 . GLU A 1 166 ? 5.148 4.841 19.378 1.00 29.33 ? 166 GLU A OE1 1 +ATOM 1396 O OE2 . GLU A 1 166 ? 5.144 4.697 17.176 1.00 27.18 ? 166 GLU A OE2 1 +ATOM 1397 N N . LEU A 1 167 ? 10.596 5.973 18.494 1.00 20.80 ? 167 LEU A N 1 +ATOM 1398 C CA . LEU A 1 167 ? 11.246 7.053 19.220 1.00 23.30 ? 167 LEU A CA 1 +ATOM 1399 C C . LEU A 1 167 ? 10.170 7.948 19.834 1.00 25.62 ? 167 LEU A C 1 +ATOM 1400 O O . LEU A 1 167 ? 9.054 8.016 19.312 1.00 25.54 ? 167 LEU A O 1 +ATOM 1401 C CB . LEU A 1 167 ? 12.109 7.853 18.227 1.00 24.19 ? 167 LEU A CB 1 +ATOM 1402 C CG . LEU A 1 167 ? 13.150 7.045 17.422 1.00 26.98 ? 167 LEU A CG 1 +ATOM 1403 C CD1 . LEU A 1 167 ? 14.029 7.967 16.621 1.00 28.28 ? 167 LEU A CD1 1 +ATOM 1404 C CD2 . LEU A 1 167 ? 14.022 6.155 18.327 1.00 27.79 ? 167 LEU A CD2 1 +ATOM 1405 N N . PRO A 1 168 ? 10.502 8.716 20.885 1.00 27.44 ? 168 PRO A N 1 +ATOM 1406 C CA . PRO A 1 168 ? 9.495 9.604 21.486 1.00 28.84 ? 168 PRO A CA 1 +ATOM 1407 C C . PRO A 1 168 ? 8.854 10.601 20.525 1.00 30.15 ? 168 PRO A C 1 +ATOM 1408 O O . PRO A 1 168 ? 7.806 11.147 20.853 1.00 31.65 ? 168 PRO A O 1 +ATOM 1409 C CB . PRO A 1 168 ? 10.264 10.307 22.605 1.00 29.60 ? 168 PRO A CB 1 +ATOM 1410 C CG . PRO A 1 168 ? 11.376 9.380 22.945 1.00 29.87 ? 168 PRO A CG 1 +ATOM 1411 C CD . PRO A 1 168 ? 11.767 8.736 21.646 1.00 27.74 ? 168 PRO A CD 1 +ATOM 1412 N N . THR A 1 169 ? 9.448 10.838 19.342 1.00 29.64 ? 169 THR A N 1 +ATOM 1413 C CA . THR A 1 169 ? 8.869 11.743 18.351 1.00 29.70 ? 169 THR A CA 1 +ATOM 1414 C C . THR A 1 169 ? 7.931 11.078 17.330 1.00 29.13 ? 169 THR A C 1 +ATOM 1415 O O . THR A 1 169 ? 7.497 11.738 16.388 1.00 29.33 ? 169 THR A O 1 +ATOM 1416 C CB . THR A 1 169 ? 9.946 12.533 17.623 1.00 31.65 ? 169 THR A CB 1 +ATOM 1417 O OG1 . THR A 1 169 ? 10.933 11.626 17.118 1.00 32.87 ? 169 THR A OG1 1 +ATOM 1418 C CG2 . THR A 1 169 ? 10.574 13.602 18.502 1.00 32.20 ? 169 THR A CG2 1 +ATOM 1419 N N . GLY A 1 170 ? 7.618 9.799 17.517 1.00 28.09 ? 170 GLY A N 1 +ATOM 1420 C CA . GLY A 1 170 ? 6.690 9.104 16.634 1.00 27.29 ? 170 GLY A CA 1 +ATOM 1421 C C . GLY A 1 170 ? 7.276 8.478 15.392 1.00 25.98 ? 170 GLY A C 1 +ATOM 1422 O O . GLY A 1 170 ? 6.531 7.969 14.548 1.00 26.76 ? 170 GLY A O 1 +ATOM 1423 N N . VAL A 1 171 ? 8.602 8.553 15.235 1.00 23.64 ? 171 VAL A N 1 +ATOM 1424 C CA . VAL A 1 171 ? 9.262 7.930 14.096 1.00 21.19 ? 171 VAL A CA 1 +ATOM 1425 C C . VAL A 1 171 ? 9.803 6.561 14.543 1.00 17.38 ? 171 VAL A C 1 +ATOM 1426 O O . VAL A 1 171 ? 9.847 6.266 15.735 1.00 17.18 ? 171 VAL A O 1 +ATOM 1427 C CB . VAL A 1 171 ? 10.323 8.817 13.418 1.00 22.74 ? 171 VAL A CB 1 +ATOM 1428 C CG1 . VAL A 1 171 ? 9.690 10.084 12.853 1.00 23.85 ? 171 VAL A CG1 1 +ATOM 1429 C CG2 . VAL A 1 171 ? 11.443 9.141 14.386 1.00 23.08 ? 171 VAL A CG2 1 +ATOM 1430 N N . HIS A 1 172 ? 10.166 5.722 13.586 1.00 15.44 ? 172 HIS A N 1 +ATOM 1431 C CA . HIS A 1 172 ? 10.508 4.343 13.854 1.00 13.98 ? 172 HIS A CA 1 +ATOM 1432 C C . HIS A 1 172 ? 11.940 3.965 13.543 1.00 13.47 ? 172 HIS A C 1 +ATOM 1433 O O . HIS A 1 172 ? 12.551 4.481 12.612 1.00 13.64 ? 172 HIS A O 1 +ATOM 1434 C CB . HIS A 1 172 ? 9.512 3.472 13.081 1.00 13.55 ? 172 HIS A CB 1 +ATOM 1435 C CG . HIS A 1 172 ? 8.096 3.784 13.471 1.00 13.40 ? 172 HIS A CG 1 +ATOM 1436 N ND1 . HIS A 1 172 ? 7.228 4.426 12.601 1.00 14.72 ? 172 HIS A ND1 1 +ATOM 1437 C CD2 . HIS A 1 172 ? 7.501 3.693 14.686 1.00 14.40 ? 172 HIS A CD2 1 +ATOM 1438 C CE1 . HIS A 1 172 ? 6.107 4.609 13.283 1.00 15.27 ? 172 HIS A CE1 1 +ATOM 1439 N NE2 . HIS A 1 172 ? 6.228 4.194 14.544 1.00 15.66 ? 172 HIS A NE2 1 +ATOM 1440 N N . ALA A 1 173 ? 12.452 3.012 14.322 1.00 12.95 ? 173 ALA A N 1 +ATOM 1441 C CA . ALA A 1 173 ? 13.821 2.530 14.168 1.00 12.79 ? 173 ALA A CA 1 +ATOM 1442 C C . ALA A 1 173 ? 13.843 1.028 14.231 1.00 12.27 ? 173 ALA A C 1 +ATOM 1443 O O . ALA A 1 173 ? 13.033 0.406 14.916 1.00 12.33 ? 173 ALA A O 1 +ATOM 1444 C CB . ALA A 1 173 ? 14.713 3.092 15.263 1.00 13.06 ? 173 ALA A CB 1 +ATOM 1445 N N . GLY A 1 174 ? 14.761 0.447 13.481 1.00 11.78 ? 174 GLY A N 1 +ATOM 1446 C CA . GLY A 1 174 ? 14.888 -0.994 13.445 1.00 11.54 ? 174 GLY A CA 1 +ATOM 1447 C C . GLY A 1 174 ? 16.188 -1.435 12.847 1.00 11.18 ? 174 GLY A C 1 +ATOM 1448 O O . GLY A 1 174 ? 17.097 -0.636 12.618 1.00 11.32 ? 174 GLY A O 1 +ATOM 1449 N N . THR A 1 175 ? 16.261 -2.716 12.564 1.00 10.81 ? 175 THR A N 1 +ATOM 1450 C CA . THR A 1 175 ? 17.491 -3.329 12.129 1.00 10.66 ? 175 THR A CA 1 +ATOM 1451 C C . THR A 1 175 ? 17.367 -3.974 10.774 1.00 10.85 ? 175 THR A C 1 +ATOM 1452 O O . THR A 1 175 ? 16.261 -4.147 10.274 1.00 11.09 ? 175 THR A O 1 +ATOM 1453 C CB . THR A 1 175 ? 17.861 -4.455 13.166 1.00 11.46 ? 175 THR A CB 1 +ATOM 1454 O OG1 . THR A 1 175 ? 16.924 -5.534 13.087 1.00 11.86 ? 175 THR A OG1 1 +ATOM 1455 C CG2 . THR A 1 175 ? 17.958 -3.963 14.586 1.00 10.45 ? 175 THR A CG2 1 +ATOM 1456 N N . ASP A 1 176 ? 18.499 -4.410 10.211 1.00 10.92 ? 176 ASP A N 1 +ATOM 1457 C CA . ASP A 1 176 ? 18.444 -5.296 9.071 1.00 11.27 ? 176 ASP A CA 1 +ATOM 1458 C C . ASP A 1 176 ? 18.223 -6.736 9.677 1.00 12.10 ? 176 ASP A C 1 +ATOM 1459 O O . ASP A 1 176 ? 18.096 -6.893 10.907 1.00 12.09 ? 176 ASP A O 1 +ATOM 1460 C CB . ASP A 1 176 ? 19.709 -5.176 8.218 1.00 12.43 ? 176 ASP A CB 1 +ATOM 1461 C CG . ASP A 1 176 ? 20.997 -5.503 8.928 1.00 14.28 ? 176 ASP A CG 1 +ATOM 1462 O OD1 . ASP A 1 176 ? 20.945 -6.153 10.000 1.00 12.59 ? 176 ASP A OD1 1 +ATOM 1463 O OD2 . ASP A 1 176 ? 22.059 -5.109 8.421 1.00 16.57 ? 176 ASP A OD2 1 +ATOM 1464 N N . LEU A 1 177 ? 18.214 -7.776 8.839 1.00 12.56 ? 177 LEU A N 1 +ATOM 1465 C CA . LEU A 1 177 ? 17.977 -9.134 9.340 1.00 13.37 ? 177 LEU A CA 1 +ATOM 1466 C C . LEU A 1 177 ? 19.229 -9.788 9.950 1.00 14.68 ? 177 LEU A C 1 +ATOM 1467 O O . LEU A 1 177 ? 19.141 -10.901 10.466 1.00 15.23 ? 177 LEU A O 1 +ATOM 1468 C CB . LEU A 1 177 ? 17.292 -10.027 8.318 1.00 13.37 ? 177 LEU A CB 1 +ATOM 1469 C CG . LEU A 1 177 ? 15.764 -9.973 8.325 1.00 14.51 ? 177 LEU A CG 1 +ATOM 1470 C CD1 . LEU A 1 177 ? 15.215 -10.582 9.597 1.00 15.35 ? 177 LEU A CD1 1 +ATOM 1471 C CD2 . LEU A 1 177 ? 15.227 -8.547 8.101 1.00 15.65 ? 177 LEU A CD2 1 +ATOM 1472 N N . GLU A 1 178 ? 20.370 -9.083 9.938 1.00 14.29 ? 178 GLU A N 1 +ATOM 1473 C CA . GLU A 1 178 ? 21.541 -9.484 10.702 1.00 13.76 ? 178 GLU A CA 1 +ATOM 1474 C C . GLU A 1 178 ? 21.486 -8.861 12.125 1.00 13.43 ? 178 GLU A C 1 +ATOM 1475 O O . GLU A 1 178 ? 22.376 -9.100 12.928 1.00 13.86 ? 178 GLU A O 1 +ATOM 1476 C CB . GLU A 1 178 ? 22.832 -9.097 9.978 1.00 15.67 ? 178 GLU A CB 1 +ATOM 1477 C CG . GLU A 1 178 ? 22.961 -9.834 8.661 1.00 20.95 ? 178 GLU A CG 1 +ATOM 1478 C CD . GLU A 1 178 ? 24.223 -9.546 7.877 1.00 29.38 ? 178 GLU A CD 1 +ATOM 1479 O OE1 . GLU A 1 178 ? 24.984 -8.632 8.273 1.00 29.50 ? 178 GLU A OE1 1 +ATOM 1480 O OE2 . GLU A 1 178 ? 24.452 -10.242 6.861 1.00 33.24 ? 178 GLU A OE2 1 +ATOM 1481 N N . GLY A 1 179 ? 20.467 -8.044 12.419 1.00 13.13 ? 179 GLY A N 1 +ATOM 1482 C CA . GLY A 1 179 ? 20.307 -7.465 13.737 1.00 12.66 ? 179 GLY A CA 1 +ATOM 1483 C C . GLY A 1 179 ? 21.024 -6.160 13.973 1.00 12.23 ? 179 GLY A C 1 +ATOM 1484 O O . GLY A 1 179 ? 21.067 -5.710 15.109 1.00 12.53 ? 179 GLY A O 1 +ATOM 1485 N N . ASN A 1 180 ? 21.583 -5.550 12.928 1.00 11.78 ? 180 ASN A N 1 +ATOM 1486 C CA . ASN A 1 180 ? 22.268 -4.273 13.077 1.00 12.01 ? 180 ASN A CA 1 +ATOM 1487 C C . ASN A 1 180 ? 21.296 -3.149 12.821 1.00 11.40 ? 180 ASN A C 1 +ATOM 1488 O O . ASN A 1 180 ? 20.701 -3.072 11.748 1.00 10.73 ? 180 ASN A O 1 +ATOM 1489 C CB . ASN A 1 180 ? 23.447 -4.180 12.113 1.00 13.42 ? 180 ASN A CB 1 +ATOM 1490 C CG . ASN A 1 180 ? 24.560 -5.117 12.483 1.00 16.66 ? 180 ASN A CG 1 +ATOM 1491 O OD1 . ASN A 1 180 ? 25.033 -5.908 11.663 1.00 18.84 ? 180 ASN A OD1 1 +ATOM 1492 N ND2 . ASN A 1 180 ? 24.992 -5.054 13.726 1.00 16.09 ? 180 ASN A ND2 1 +ATOM 1493 N N . PHE A 1 181 ? 21.136 -2.246 13.795 1.00 11.37 ? 181 PHE A N 1 +ATOM 1494 C CA . PHE A 1 181 ? 20.248 -1.104 13.610 1.00 11.91 ? 181 PHE A CA 1 +ATOM 1495 C C . PHE A 1 181 ? 20.686 -0.235 12.452 1.00 12.38 ? 181 PHE A C 1 +ATOM 1496 O O . PHE A 1 181 ? 21.881 -0.094 12.176 1.00 12.34 ? 181 PHE A O 1 +ATOM 1497 C CB . PHE A 1 181 ? 20.201 -0.235 14.871 1.00 12.24 ? 181 PHE A CB 1 +ATOM 1498 C CG . PHE A 1 181 ? 19.085 -0.590 15.813 1.00 12.39 ? 181 PHE A CG 1 +ATOM 1499 C CD1 . PHE A 1 181 ? 19.280 -1.514 16.825 1.00 12.74 ? 181 PHE A CD1 1 +ATOM 1500 C CD2 . PHE A 1 181 ? 17.854 0.039 15.721 1.00 12.69 ? 181 PHE A CD2 1 +ATOM 1501 C CE1 . PHE A 1 181 ? 18.258 -1.822 17.714 1.00 12.99 ? 181 PHE A CE1 1 +ATOM 1502 C CE2 . PHE A 1 181 ? 16.828 -0.277 16.600 1.00 13.19 ? 181 PHE A CE2 1 +ATOM 1503 C CZ . PHE A 1 181 ? 17.031 -1.207 17.593 1.00 13.05 ? 181 PHE A CZ 1 +ATOM 1504 N N . TYR A 1 182 ? 19.702 0.341 11.784 1.00 11.78 ? 182 TYR A N 1 +ATOM 1505 C CA . TYR A 1 182 ? 19.973 1.380 10.817 1.00 12.63 ? 182 TYR A CA 1 +ATOM 1506 C C . TYR A 1 182 ? 20.218 2.634 11.653 1.00 13.60 ? 182 TYR A C 1 +ATOM 1507 O O . TYR A 1 182 ? 19.486 2.909 12.615 1.00 14.08 ? 182 TYR A O 1 +ATOM 1508 C CB . TYR A 1 182 ? 18.765 1.574 9.929 1.00 12.36 ? 182 TYR A CB 1 +ATOM 1509 C CG . TYR A 1 182 ? 18.689 0.495 8.878 1.00 12.38 ? 182 TYR A CG 1 +ATOM 1510 C CD1 . TYR A 1 182 ? 19.511 0.528 7.766 1.00 12.83 ? 182 TYR A CD1 1 +ATOM 1511 C CD2 . TYR A 1 182 ? 17.862 -0.604 9.045 1.00 12.57 ? 182 TYR A CD2 1 +ATOM 1512 C CE1 . TYR A 1 182 ? 19.456 -0.465 6.802 1.00 12.90 ? 182 TYR A CE1 1 +ATOM 1513 C CE2 . TYR A 1 182 ? 17.792 -1.601 8.089 1.00 12.93 ? 182 TYR A CE2 1 +ATOM 1514 C CZ . TYR A 1 182 ? 18.601 -1.534 6.970 1.00 13.28 ? 182 TYR A CZ 1 +ATOM 1515 O OH . TYR A 1 182 ? 18.538 -2.508 5.998 1.00 13.15 ? 182 TYR A OH 1 +ATOM 1516 N N . GLY A 1 183 ? 21.282 3.338 11.320 1.00 13.88 ? 183 GLY A N 1 +ATOM 1517 C CA . GLY A 1 183 ? 21.632 4.549 12.030 1.00 15.00 ? 183 GLY A CA 1 +ATOM 1518 C C . GLY A 1 183 ? 22.167 4.279 13.408 1.00 15.58 ? 183 GLY A C 1 +ATOM 1519 O O . GLY A 1 183 ? 22.626 3.178 13.716 1.00 15.49 ? 183 GLY A O 1 +ATOM 1520 N N . PRO A 1 184 ? 22.081 5.295 14.261 1.00 15.71 ? 184 PRO A N 1 +ATOM 1521 C CA . PRO A 1 184 ? 22.700 5.199 15.592 1.00 15.80 ? 184 PRO A CA 1 +ATOM 1522 C C . PRO A 1 184 ? 21.818 4.666 16.712 1.00 15.71 ? 184 PRO A C 1 +ATOM 1523 O O . PRO A 1 184 ? 22.202 4.708 17.880 1.00 16.85 ? 184 PRO A O 1 +ATOM 1524 C CB . PRO A 1 184 ? 23.004 6.662 15.886 1.00 16.92 ? 184 PRO A CB 1 +ATOM 1525 C CG . PRO A 1 184 ? 21.820 7.366 15.282 1.00 17.42 ? 184 PRO A CG 1 +ATOM 1526 C CD . PRO A 1 184 ? 21.576 6.658 13.991 1.00 15.87 ? 184 PRO A CD 1 +ATOM 1527 N N . PHE A 1 185 ? 20.626 4.205 16.356 1.00 15.02 ? 185 PHE A N 1 +ATOM 1528 C CA . PHE A 1 185 ? 19.631 3.816 17.322 1.00 15.08 ? 185 PHE A CA 1 +ATOM 1529 C C . PHE A 1 185 ? 19.972 2.543 18.048 1.00 15.67 ? 185 PHE A C 1 +ATOM 1530 O O . PHE A 1 185 ? 20.717 1.701 17.548 1.00 15.41 ? 185 PHE A O 1 +ATOM 1531 C CB . PHE A 1 185 ? 18.245 3.763 16.665 1.00 14.67 ? 185 PHE A CB 1 +ATOM 1532 C CG . PHE A 1 185 ? 17.918 5.097 16.038 1.00 14.96 ? 185 PHE A CG 1 +ATOM 1533 C CD1 . PHE A 1 185 ? 17.777 6.231 16.819 1.00 15.71 ? 185 PHE A CD1 1 +ATOM 1534 C CD2 . PHE A 1 185 ? 17.856 5.235 14.665 1.00 15.58 ? 185 PHE A CD2 1 +ATOM 1535 C CE1 . PHE A 1 185 ? 17.550 7.473 16.232 1.00 15.86 ? 185 PHE A CE1 1 +ATOM 1536 C CE2 . PHE A 1 185 ? 17.627 6.471 14.088 1.00 15.63 ? 185 PHE A CE2 1 +ATOM 1537 C CZ . PHE A 1 185 ? 17.450 7.580 14.874 1.00 15.37 ? 185 PHE A CZ 1 +ATOM 1538 N N . VAL A 1 186 ? 19.484 2.448 19.269 1.00 16.07 ? 186 VAL A N 1 +ATOM 1539 C CA . VAL A 1 186 ? 19.714 1.295 20.124 1.00 16.52 ? 186 VAL A CA 1 +ATOM 1540 C C . VAL A 1 186 ? 18.408 0.767 20.679 1.00 16.78 ? 186 VAL A C 1 +ATOM 1541 O O . VAL A 1 186 ? 17.436 1.513 20.778 1.00 17.71 ? 186 VAL A O 1 +ATOM 1542 C CB . VAL A 1 186 ? 20.699 1.623 21.273 1.00 17.66 ? 186 VAL A CB 1 +ATOM 1543 C CG1 . VAL A 1 186 ? 22.088 1.924 20.725 1.00 18.92 ? 186 VAL A CG1 1 +ATOM 1544 C CG2 . VAL A 1 186 ? 20.188 2.782 22.130 1.00 18.38 ? 186 VAL A CG2 1 +ATOM 1545 N N . ASP A 1 187 ? 18.386 -0.515 21.077 1.00 15.60 ? 187 ASP A N 1 +ATOM 1546 C CA . ASP A 1 187 ? 17.180 -1.106 21.642 1.00 15.58 ? 187 ASP A CA 1 +ATOM 1547 C C . ASP A 1 187 ? 17.101 -0.911 23.133 1.00 16.90 ? 187 ASP A C 1 +ATOM 1548 O O . ASP A 1 187 ? 17.132 -1.857 23.916 1.00 16.91 ? 187 ASP A O 1 +ATOM 1549 C CB . ASP A 1 187 ? 16.973 -2.565 21.246 1.00 15.08 ? 187 ASP A CB 1 +ATOM 1550 C CG . ASP A 1 187 ? 18.169 -3.478 21.361 1.00 15.13 ? 187 ASP A CG 1 +ATOM 1551 O OD1 . ASP A 1 187 ? 19.244 -3.005 21.797 1.00 15.07 ? 187 ASP A OD1 1 +ATOM 1552 O OD2 . ASP A 1 187 ? 18.030 -4.666 21.026 1.00 14.64 ? 187 ASP A OD2 1 +ATOM 1553 N N . ARG A 1 188 ? 16.993 0.352 23.513 1.00 18.27 ? 188 ARG A N 1 +ATOM 1554 C CA . ARG A 1 188 ? 16.915 0.803 24.882 1.00 20.54 ? 188 ARG A CA 1 +ATOM 1555 C C . ARG A 1 188 ? 15.979 2.000 24.892 1.00 22.19 ? 188 ARG A C 1 +ATOM 1556 O O . ARG A 1 188 ? 16.006 2.826 23.979 1.00 21.85 ? 188 ARG A O 1 +ATOM 1557 C CB . ARG A 1 188 ? 18.315 1.222 25.371 1.00 23.06 ? 188 ARG A CB 1 +ATOM 1558 C CG . ARG A 1 188 ? 18.378 1.486 26.858 1.00 28.82 ? 188 ARG A CG 1 +ATOM 1559 C CD . ARG A 1 188 ? 19.755 1.913 27.332 1.00 34.58 ? 188 ARG A CD 1 +ATOM 1560 N NE . ARG A 1 188 ? 19.637 2.726 28.541 1.00 39.48 ? 188 ARG A NE 1 +ATOM 1561 C CZ . ARG A 1 188 ? 20.650 3.073 29.325 1.00 42.92 ? 188 ARG A CZ 1 +ATOM 1562 N NH1 . ARG A 1 188 ? 21.884 2.678 29.040 1.00 43.29 ? 188 ARG A NH1 1 +ATOM 1563 N NH2 . ARG A 1 188 ? 20.434 3.803 30.412 1.00 43.34 ? 188 ARG A NH2 1 +ATOM 1564 N N . GLN A 1 189 ? 15.143 2.089 25.912 1.00 24.10 ? 189 GLN A N 1 +ATOM 1565 C CA . GLN A 1 189 ? 14.193 3.177 26.044 1.00 26.30 ? 189 GLN A CA 1 +ATOM 1566 C C . GLN A 1 189 ? 14.930 4.350 26.661 1.00 28.13 ? 189 GLN A C 1 +ATOM 1567 O O . GLN A 1 189 ? 14.955 4.501 27.883 1.00 28.84 ? 189 GLN A O 1 +ATOM 1568 C CB . GLN A 1 189 ? 13.013 2.731 26.905 1.00 28.62 ? 189 GLN A CB 1 +ATOM 1569 C CG . GLN A 1 189 ? 11.848 3.700 26.891 1.00 33.55 ? 189 GLN A CG 1 +ATOM 1570 C CD . GLN A 1 189 ? 10.793 3.236 27.855 1.00 39.90 ? 189 GLN A CD 1 +ATOM 1571 O OE1 . GLN A 1 189 ? 10.375 2.071 27.855 1.00 41.94 ? 189 GLN A OE1 1 +ATOM 1572 N NE2 . GLN A 1 189 ? 10.354 4.137 28.711 1.00 40.98 ? 189 GLN A NE2 1 +ATOM 1573 N N . THR A 1 190 ? 15.597 5.137 25.811 1.00 29.21 ? 190 THR A N 1 +ATOM 1574 C CA . THR A 1 190 ? 16.412 6.287 26.208 1.00 30.97 ? 190 THR A CA 1 +ATOM 1575 C C . THR A 1 190 ? 16.145 7.506 25.303 1.00 31.77 ? 190 THR A C 1 +ATOM 1576 O O . THR A 1 190 ? 15.420 7.392 24.308 1.00 32.40 ? 190 THR A O 1 +ATOM 1577 C CB . THR A 1 190 ? 17.915 5.902 26.162 1.00 33.71 ? 190 THR A CB 1 +ATOM 1578 O OG1 . THR A 1 190 ? 18.225 5.263 24.922 1.00 35.59 ? 190 THR A OG1 1 +ATOM 1579 C CG2 . THR A 1 190 ? 18.348 5.087 27.338 1.00 34.74 ? 190 THR A CG2 1 +ATOM 1580 N N . ALA A 1 191 ? 16.753 8.667 25.625 1.00 31.73 ? 191 ALA A N 1 +ATOM 1581 C CA . ALA A 1 191 ? 16.636 9.844 24.794 1.00 32.04 ? 191 ALA A CA 1 +ATOM 1582 C C . ALA A 1 191 ? 17.438 9.584 23.530 1.00 32.03 ? 191 ALA A C 1 +ATOM 1583 O O . ALA A 1 191 ? 18.667 9.639 23.539 1.00 33.57 ? 191 ALA A O 1 +ATOM 1584 C CB . ALA A 1 191 ? 17.189 11.058 25.515 1.00 32.37 ? 191 ALA A CB 1 +ATOM 1585 N N . GLN A 1 192 ? 16.744 9.214 22.473 1.00 30.11 ? 192 GLN A N 1 +ATOM 1586 C CA . GLN A 1 192 ? 17.362 8.979 21.185 1.00 28.86 ? 192 GLN A CA 1 +ATOM 1587 C C . GLN A 1 192 ? 16.641 9.910 20.261 1.00 28.78 ? 192 GLN A C 1 +ATOM 1588 O O . GLN A 1 192 ? 15.459 9.689 19.992 1.00 30.27 ? 192 GLN A O 1 +ATOM 1589 C CB . GLN A 1 192 ? 17.121 7.544 20.715 1.00 28.03 ? 192 GLN A CB 1 +ATOM 1590 C CG . GLN A 1 192 ? 17.466 6.488 21.725 1.00 27.39 ? 192 GLN A CG 1 +ATOM 1591 C CD . GLN A 1 192 ? 17.504 5.185 21.001 1.00 24.21 ? 192 GLN A CD 1 +ATOM 1592 O OE1 . GLN A 1 192 ? 18.318 5.000 20.097 1.00 22.45 ? 192 GLN A OE1 1 +ATOM 1593 N NE2 . GLN A 1 192 ? 16.608 4.276 21.359 1.00 23.00 ? 192 GLN A NE2 1 +ATOM 1594 N N . ALA A 1 193 ? 17.306 10.977 19.816 1.00 27.11 ? 193 ALA A N 1 +ATOM 1595 C CA . ALA A 1 193 ? 16.657 11.916 18.912 1.00 26.29 ? 193 ALA A CA 1 +ATOM 1596 C C . ALA A 1 193 ? 17.154 11.718 17.499 1.00 25.22 ? 193 ALA A C 1 +ATOM 1597 O O . ALA A 1 193 ? 18.320 11.376 17.282 1.00 25.57 ? 193 ALA A O 1 +ATOM 1598 C CB . ALA A 1 193 ? 16.894 13.340 19.361 1.00 26.29 ? 193 ALA A CB 1 +ATOM 1599 N N . ALA A 1 194 ? 16.261 11.895 16.535 1.00 23.81 ? 194 ALA A N 1 +ATOM 1600 C CA . ALA A 1 194 ? 16.617 11.758 15.133 1.00 22.55 ? 194 ALA A CA 1 +ATOM 1601 C C . ALA A 1 194 ? 17.257 13.041 14.614 1.00 20.69 ? 194 ALA A C 1 +ATOM 1602 O O . ALA A 1 194 ? 16.939 14.141 15.065 1.00 20.78 ? 194 ALA A O 1 +ATOM 1603 C CB . ALA A 1 194 ? 15.384 11.422 14.309 1.00 22.80 ? 194 ALA A CB 1 +ATOM 1604 N N . GLY A 1 195 ? 18.140 12.891 13.641 1.00 18.81 ? 195 GLY A N 1 +ATOM 1605 C CA . GLY A 1 195 ? 18.752 14.027 12.981 1.00 18.20 ? 195 GLY A CA 1 +ATOM 1606 C C . GLY A 1 195 ? 17.782 14.641 11.989 1.00 17.45 ? 195 GLY A C 1 +ATOM 1607 O O . GLY A 1 195 ? 16.600 14.274 11.937 1.00 17.25 ? 195 GLY A O 1 +ATOM 1608 N N . THR A 1 196 ? 18.293 15.530 11.144 1.00 16.59 ? 196 THR A N 1 +ATOM 1609 C CA . THR A 1 196 ? 17.483 16.239 10.165 1.00 16.96 ? 196 THR A CA 1 +ATOM 1610 C C . THR A 1 196 ? 16.846 15.288 9.210 1.00 17.50 ? 196 THR A C 1 +ATOM 1611 O O . THR A 1 196 ? 17.541 14.425 8.663 1.00 17.04 ? 196 THR A O 1 +ATOM 1612 C CB . THR A 1 196 ? 18.339 17.238 9.386 1.00 18.41 ? 196 THR A CB 1 +ATOM 1613 O OG1 . THR A 1 196 ? 19.041 18.066 10.303 1.00 19.49 ? 196 THR A OG1 1 +ATOM 1614 C CG2 . THR A 1 196 ? 17.516 18.113 8.465 1.00 19.24 ? 196 THR A CG2 1 +ATOM 1615 N N . ASP A 1 197 ? 15.517 15.412 9.024 1.00 17.89 ? 197 ASP A N 1 +ATOM 1616 C CA . ASP A 1 197 ? 14.850 14.565 8.047 1.00 18.28 ? 197 ASP A CA 1 +ATOM 1617 C C . ASP A 1 197 ? 14.922 15.240 6.692 1.00 17.83 ? 197 ASP A C 1 +ATOM 1618 O O . ASP A 1 197 ? 13.995 15.929 6.257 1.00 20.27 ? 197 ASP A O 1 +ATOM 1619 C CB . ASP A 1 197 ? 13.431 14.139 8.441 1.00 20.37 ? 197 ASP A CB 1 +ATOM 1620 C CG . ASP A 1 197 ? 12.899 12.932 7.682 1.00 23.82 ? 197 ASP A CG 1 +ATOM 1621 O OD1 . ASP A 1 197 ? 13.654 12.353 6.864 1.00 20.44 ? 197 ASP A OD1 1 +ATOM 1622 O OD2 . ASP A 1 197 ? 11.747 12.542 7.934 1.00 28.73 ? 197 ASP A OD2 1 +ATOM 1623 N N A THR A 1 198 ? 16.073 15.084 6.036 0.50 16.35 ? 198 THR A N 1 +ATOM 1624 N N B THR A 1 198 ? 16.027 14.973 6.021 0.50 16.18 ? 198 THR A N 1 +ATOM 1625 C CA A THR A 1 198 ? 16.273 15.688 4.726 0.50 15.97 ? 198 THR A CA 1 +ATOM 1626 C CA B THR A 1 198 ? 16.431 15.485 4.722 0.50 15.73 ? 198 THR A CA 1 +ATOM 1627 C C A THR A 1 198 ? 15.435 14.991 3.669 0.50 15.27 ? 198 THR A C 1 +ATOM 1628 C C B THR A 1 198 ? 15.577 14.886 3.597 0.50 15.16 ? 198 THR A C 1 +ATOM 1629 O O A THR A 1 198 ? 14.972 13.861 3.855 0.50 15.28 ? 198 THR A O 1 +ATOM 1630 O O B THR A 1 198 ? 15.248 13.702 3.663 0.50 15.19 ? 198 THR A O 1 +ATOM 1631 C CB A THR A 1 198 ? 17.753 15.778 4.371 0.50 17.51 ? 198 THR A CB 1 +ATOM 1632 C CB B THR A 1 198 ? 17.918 15.133 4.570 0.50 16.74 ? 198 THR A CB 1 +ATOM 1633 O OG1 A THR A 1 198 ? 18.310 14.471 4.399 0.50 18.42 ? 198 THR A OG1 1 +ATOM 1634 O OG1 B THR A 1 198 ? 18.659 15.683 5.672 0.50 17.41 ? 198 THR A OG1 1 +ATOM 1635 C CG2 A THR A 1 198 ? 18.524 16.703 5.296 0.50 17.78 ? 198 THR A CG2 1 +ATOM 1636 C CG2 B THR A 1 198 ? 18.499 15.622 3.285 0.50 17.17 ? 198 THR A CG2 1 +ATOM 1637 N N . THR A 1 199 ? 15.201 15.692 2.578 1.00 14.19 ? 199 THR A N 1 +ATOM 1638 C CA . THR A 1 199 ? 14.404 15.175 1.472 1.00 13.47 ? 199 THR A CA 1 +ATOM 1639 C C . THR A 1 199 ? 15.302 14.448 0.475 1.00 12.86 ? 199 THR A C 1 +ATOM 1640 O O . THR A 1 199 ? 16.404 14.913 0.194 1.00 13.34 ? 199 THR A O 1 +ATOM 1641 C CB . THR A 1 199 ? 13.546 16.279 0.859 1.00 14.60 ? 199 THR A CB 1 +ATOM 1642 O OG1 . THR A 1 199 ? 12.711 16.839 1.874 1.00 15.22 ? 199 THR A OG1 1 +ATOM 1643 C CG2 . THR A 1 199 ? 12.667 15.765 -0.281 1.00 15.03 ? 199 THR A CG2 1 +ATOM 1644 N N . ILE A 1 200 ? 14.861 13.264 -0.011 1.00 12.06 ? 200 ILE A N 1 +ATOM 1645 C CA . ILE A 1 200 ? 15.633 12.442 -0.950 1.00 12.31 ? 200 ILE A CA 1 +ATOM 1646 C C . ILE A 1 200 ? 15.432 12.991 -2.363 1.00 11.85 ? 200 ILE A C 1 +ATOM 1647 O O . ILE A 1 200 ? 14.510 12.616 -3.089 1.00 11.58 ? 200 ILE A O 1 +ATOM 1648 C CB . ILE A 1 200 ? 15.218 10.951 -0.852 1.00 12.52 ? 200 ILE A CB 1 +ATOM 1649 C CG1 . ILE A 1 200 ? 15.204 10.474 0.626 1.00 12.89 ? 200 ILE A CG1 1 +ATOM 1650 C CG2 . ILE A 1 200 ? 16.162 10.099 -1.689 1.00 12.93 ? 200 ILE A CG2 1 +ATOM 1651 C CD1 . ILE A 1 200 ? 14.183 9.365 0.910 1.00 14.24 ? 200 ILE A CD1 1 +ATOM 1652 N N . THR A 1 201 ? 16.317 13.911 -2.732 1.00 11.75 ? 201 THR A N 1 +ATOM 1653 C CA . THR A 1 201 ? 16.264 14.631 -3.995 1.00 12.03 ? 201 THR A CA 1 +ATOM 1654 C C . THR A 1 201 ? 16.083 13.743 -5.217 1.00 12.46 ? 201 THR A C 1 +ATOM 1655 O O . THR A 1 201 ? 15.218 14.024 -6.052 1.00 13.25 ? 201 THR A O 1 +ATOM 1656 C CB . THR A 1 201 ? 17.526 15.476 -4.150 1.00 13.15 ? 201 THR A CB 1 +ATOM 1657 O OG1 . THR A 1 201 ? 17.749 16.207 -2.951 1.00 13.77 ? 201 THR A OG1 1 +ATOM 1658 C CG2 . THR A 1 201 ? 17.479 16.386 -5.360 1.00 14.00 ? 201 THR A CG2 1 +ATOM 1659 N N . VAL A 1 202 ? 16.888 12.675 -5.341 1.00 11.54 ? 202 VAL A N 1 +ATOM 1660 C CA . VAL A 1 202 ? 16.798 11.804 -6.519 1.00 12.15 ? 202 VAL A CA 1 +ATOM 1661 C C . VAL A 1 202 ? 15.402 11.170 -6.634 1.00 12.21 ? 202 VAL A C 1 +ATOM 1662 O O . VAL A 1 202 ? 14.899 10.999 -7.736 1.00 12.15 ? 202 VAL A O 1 +ATOM 1663 C CB . VAL A 1 202 ? 17.929 10.751 -6.579 1.00 13.19 ? 202 VAL A CB 1 +ATOM 1664 C CG1 . VAL A 1 202 ? 17.770 9.698 -5.480 1.00 14.16 ? 202 VAL A CG1 1 +ATOM 1665 C CG2 . VAL A 1 202 ? 18.012 10.102 -7.959 1.00 14.05 ? 202 VAL A CG2 1 +ATOM 1666 N N . ASN A 1 203 ? 14.756 10.889 -5.487 1.00 12.28 ? 203 ASN A N 1 +ATOM 1667 C CA . ASN A 1 203 ? 13.419 10.315 -5.495 1.00 12.14 ? 203 ASN A CA 1 +ATOM 1668 C C . ASN A 1 203 ? 12.385 11.343 -5.906 1.00 12.09 ? 203 ASN A C 1 +ATOM 1669 O O . ASN A 1 203 ? 11.470 11.014 -6.664 1.00 12.27 ? 203 ASN A O 1 +ATOM 1670 C CB . ASN A 1 203 ? 13.086 9.747 -4.116 1.00 12.23 ? 203 ASN A CB 1 +ATOM 1671 C CG . ASN A 1 203 ? 13.839 8.482 -3.781 1.00 12.94 ? 203 ASN A CG 1 +ATOM 1672 O OD1 . ASN A 1 203 ? 14.704 8.031 -4.528 1.00 12.49 ? 203 ASN A OD1 1 +ATOM 1673 N ND2 . ASN A 1 203 ? 13.543 7.903 -2.603 1.00 12.93 ? 203 ASN A ND2 1 +ATOM 1674 N N . VAL A 1 204 ? 12.549 12.612 -5.486 1.00 11.53 ? 204 VAL A N 1 +ATOM 1675 C CA . VAL A 1 204 ? 11.614 13.665 -5.908 1.00 11.74 ? 204 VAL A CA 1 +ATOM 1676 C C . VAL A 1 204 ? 11.696 13.853 -7.408 1.00 12.06 ? 204 VAL A C 1 +ATOM 1677 O O . VAL A 1 204 ? 10.667 13.959 -8.069 1.00 12.65 ? 204 VAL A O 1 +ATOM 1678 C CB . VAL A 1 204 ? 11.899 14.998 -5.193 1.00 12.37 ? 204 VAL A CB 1 +ATOM 1679 C CG1 . VAL A 1 204 ? 10.971 16.096 -5.711 1.00 12.86 ? 204 VAL A CG1 1 +ATOM 1680 C CG2 . VAL A 1 204 ? 11.731 14.836 -3.687 1.00 11.91 ? 204 VAL A CG2 1 +ATOM 1681 N N . LEU A 1 205 ? 12.920 13.831 -7.961 1.00 11.62 ? 205 LEU A N 1 +ATOM 1682 C CA . LEU A 1 205 ? 13.080 13.980 -9.409 1.00 11.61 ? 205 LEU A CA 1 +ATOM 1683 C C . LEU A 1 205 ? 12.439 12.817 -10.129 1.00 12.03 ? 205 LEU A C 1 +ATOM 1684 O O . LEU A 1 205 ? 11.742 13.024 -11.120 1.00 11.50 ? 205 LEU A O 1 +ATOM 1685 C CB . LEU A 1 205 ? 14.560 14.080 -9.785 1.00 11.82 ? 205 LEU A CB 1 +ATOM 1686 C CG . LEU A 1 205 ? 15.223 15.375 -9.349 1.00 12.51 ? 205 LEU A CG 1 +ATOM 1687 C CD1 . LEU A 1 205 ? 16.733 15.246 -9.360 1.00 13.36 ? 205 LEU A CD1 1 +ATOM 1688 C CD2 . LEU A 1 205 ? 14.733 16.542 -10.186 1.00 13.75 ? 205 LEU A CD2 1 +ATOM 1689 N N . ALA A 1 206 ? 12.630 11.587 -9.620 1.00 12.01 ? 206 ALA A N 1 +ATOM 1690 C CA . ALA A 1 206 ? 12.019 10.411 -10.254 1.00 12.58 ? 206 ALA A CA 1 +ATOM 1691 C C . ALA A 1 206 ? 10.483 10.546 -10.260 1.00 13.06 ? 206 ALA A C 1 +ATOM 1692 O O . ALA A 1 206 ? 9.841 10.284 -11.270 1.00 12.97 ? 206 ALA A O 1 +ATOM 1693 C CB . ALA A 1 206 ? 12.426 9.154 -9.509 1.00 13.02 ? 206 ALA A CB 1 +ATOM 1694 N N . TRP A 1 207 ? 9.924 11.046 -9.151 1.00 12.31 ? 207 TRP A N 1 +ATOM 1695 C CA . TRP A 1 207 ? 8.484 11.237 -9.044 1.00 12.72 ? 207 TRP A CA 1 +ATOM 1696 C C . TRP A 1 207 ? 7.993 12.353 -9.993 1.00 12.88 ? 207 TRP A C 1 +ATOM 1697 O O . TRP A 1 207 ? 6.919 12.226 -10.565 1.00 13.64 ? 207 TRP A O 1 +ATOM 1698 C CB . TRP A 1 207 ? 8.134 11.468 -7.574 1.00 13.10 ? 207 TRP A CB 1 +ATOM 1699 C CG . TRP A 1 207 ? 6.764 11.990 -7.302 1.00 13.61 ? 207 TRP A CG 1 +ATOM 1700 C CD1 . TRP A 1 207 ? 5.613 11.271 -7.141 1.00 14.89 ? 207 TRP A CD1 1 +ATOM 1701 C CD2 . TRP A 1 207 ? 6.432 13.349 -7.037 1.00 13.53 ? 207 TRP A CD2 1 +ATOM 1702 N NE1 . TRP A 1 207 ? 4.581 12.114 -6.796 1.00 15.38 ? 207 TRP A NE1 1 +ATOM 1703 C CE2 . TRP A 1 207 ? 5.061 13.396 -6.721 1.00 14.69 ? 207 TRP A CE2 1 +ATOM 1704 C CE3 . TRP A 1 207 ? 7.177 14.530 -6.990 1.00 14.59 ? 207 TRP A CE3 1 +ATOM 1705 C CZ2 . TRP A 1 207 ? 4.421 14.585 -6.382 1.00 15.53 ? 207 TRP A CZ2 1 +ATOM 1706 C CZ3 . TRP A 1 207 ? 6.536 15.709 -6.670 1.00 15.61 ? 207 TRP A CZ3 1 +ATOM 1707 C CH2 . TRP A 1 207 ? 5.175 15.729 -6.384 1.00 15.54 ? 207 TRP A CH2 1 +ATOM 1708 N N . LEU A 1 208 ? 8.814 13.381 -10.235 1.00 12.37 ? 208 LEU A N 1 +ATOM 1709 C CA . LEU A 1 208 ? 8.452 14.412 -11.218 1.00 12.13 ? 208 LEU A CA 1 +ATOM 1710 C C . LEU A 1 208 ? 8.433 13.799 -12.619 1.00 12.89 ? 208 LEU A C 1 +ATOM 1711 O O . LEU A 1 208 ? 7.538 14.110 -13.409 1.00 13.49 ? 208 LEU A O 1 +ATOM 1712 C CB . LEU A 1 208 ? 9.446 15.566 -11.142 1.00 11.68 ? 208 LEU A CB 1 +ATOM 1713 C CG . LEU A 1 208 ? 9.330 16.445 -9.891 1.00 13.13 ? 208 LEU A CG 1 +ATOM 1714 C CD1 . LEU A 1 208 ? 10.419 17.506 -9.884 1.00 13.35 ? 208 LEU A CD1 1 +ATOM 1715 C CD2 . LEU A 1 208 ? 7.956 17.130 -9.824 1.00 13.49 ? 208 LEU A CD2 1 +ATOM 1716 N N . TYR A 1 209 ? 9.367 12.870 -12.916 1.00 12.85 ? 209 TYR A N 1 +ATOM 1717 C CA . TYR A 1 209 ? 9.341 12.143 -14.193 1.00 13.30 ? 209 TYR A CA 1 +ATOM 1718 C C . TYR A 1 209 ? 8.069 11.310 -14.283 1.00 14.51 ? 209 TYR A C 1 +ATOM 1719 O O . TYR A 1 209 ? 7.423 11.315 -15.316 1.00 15.06 ? 209 TYR A O 1 +ATOM 1720 C CB . TYR A 1 209 ? 10.556 11.234 -14.364 1.00 12.99 ? 209 TYR A CB 1 +ATOM 1721 C CG . TYR A 1 209 ? 11.758 11.992 -14.871 1.00 13.05 ? 209 TYR A CG 1 +ATOM 1722 C CD1 . TYR A 1 209 ? 11.814 12.446 -16.178 1.00 13.88 ? 209 TYR A CD1 1 +ATOM 1723 C CD2 . TYR A 1 209 ? 12.843 12.240 -14.048 1.00 13.62 ? 209 TYR A CD2 1 +ATOM 1724 C CE1 . TYR A 1 209 ? 12.907 13.155 -16.649 1.00 14.59 ? 209 TYR A CE1 1 +ATOM 1725 C CE2 . TYR A 1 209 ? 13.943 12.953 -14.506 1.00 14.55 ? 209 TYR A CE2 1 +ATOM 1726 C CZ . TYR A 1 209 ? 13.975 13.397 -15.814 1.00 14.96 ? 209 TYR A CZ 1 +ATOM 1727 O OH . TYR A 1 209 ? 15.049 14.115 -16.279 1.00 16.11 ? 209 TYR A OH 1 +ATOM 1728 N N . ALA A 1 210 ? 7.680 10.629 -13.183 1.00 14.89 ? 210 ALA A N 1 +ATOM 1729 C CA . ALA A 1 210 ? 6.429 9.851 -13.171 1.00 15.35 ? 210 ALA A CA 1 +ATOM 1730 C C . ALA A 1 210 ? 5.231 10.755 -13.445 1.00 16.18 ? 210 ALA A C 1 +ATOM 1731 O O . ALA A 1 210 ? 4.309 10.368 -14.163 1.00 16.64 ? 210 ALA A O 1 +ATOM 1732 C CB . ALA A 1 210 ? 6.246 9.164 -11.820 1.00 15.41 ? 210 ALA A CB 1 +ATOM 1733 N N . ALA A 1 211 ? 5.247 11.971 -12.900 1.00 15.83 ? 211 ALA A N 1 +ATOM 1734 C CA . ALA A 1 211 ? 4.178 12.927 -13.105 1.00 15.93 ? 211 ALA A CA 1 +ATOM 1735 C C . ALA A 1 211 ? 4.077 13.306 -14.578 1.00 16.27 ? 211 ALA A C 1 +ATOM 1736 O O . ALA A 1 211 ? 2.978 13.279 -15.138 1.00 17.39 ? 211 ALA A O 1 +ATOM 1737 C CB . ALA A 1 211 ? 4.407 14.152 -12.240 1.00 16.23 ? 211 ALA A CB 1 +ATOM 1738 N N . VAL A 1 212 ? 5.210 13.588 -15.237 1.00 15.64 ? 212 VAL A N 1 +ATOM 1739 C CA . VAL A 1 212 ? 5.187 13.927 -16.663 1.00 16.48 ? 212 VAL A CA 1 +ATOM 1740 C C . VAL A 1 212 ? 4.654 12.777 -17.487 1.00 18.29 ? 212 VAL A C 1 +ATOM 1741 O O . VAL A 1 212 ? 3.796 12.996 -18.351 1.00 19.31 ? 212 VAL A O 1 +ATOM 1742 C CB . VAL A 1 212 ? 6.574 14.389 -17.150 1.00 16.59 ? 212 VAL A CB 1 +ATOM 1743 C CG1 . VAL A 1 212 ? 6.583 14.581 -18.668 1.00 16.85 ? 212 VAL A CG1 1 +ATOM 1744 C CG2 . VAL A 1 212 ? 6.969 15.674 -16.451 1.00 17.06 ? 212 VAL A CG2 1 +ATOM 1745 N N . ILE A 1 213 ? 5.112 11.552 -17.202 1.00 19.03 ? 213 ILE A N 1 +ATOM 1746 C CA . ILE A 1 213 ? 4.654 10.357 -17.930 1.00 20.91 ? 213 ILE A CA 1 +ATOM 1747 C C . ILE A 1 213 ? 3.142 10.195 -17.791 1.00 23.56 ? 213 ILE A C 1 +ATOM 1748 O O . ILE A 1 213 ? 2.457 9.941 -18.777 1.00 24.76 ? 213 ILE A O 1 +ATOM 1749 C CB . ILE A 1 213 ? 5.416 9.109 -17.418 1.00 21.25 ? 213 ILE A CB 1 +ATOM 1750 C CG1 . ILE A 1 213 ? 6.904 9.189 -17.803 1.00 21.73 ? 213 ILE A CG1 1 +ATOM 1751 C CG2 . ILE A 1 213 ? 4.783 7.803 -17.918 1.00 21.99 ? 213 ILE A CG2 1 +ATOM 1752 C CD1 . ILE A 1 213 ? 7.788 8.246 -17.083 1.00 22.87 ? 213 ILE A CD1 1 +ATOM 1753 N N . ASN A 1 214 ? 2.620 10.439 -16.588 1.00 24.22 ? 214 ASN A N 1 +ATOM 1754 C CA . ASN A 1 214 ? 1.204 10.282 -16.300 1.00 26.05 ? 214 ASN A CA 1 +ATOM 1755 C C . ASN A 1 214 ? 0.343 11.544 -16.522 1.00 27.69 ? 214 ASN A C 1 +ATOM 1756 O O . ASN A 1 214 ? -0.799 11.581 -16.055 1.00 29.91 ? 214 ASN A O 1 +ATOM 1757 C CB . ASN A 1 214 ? 1.016 9.716 -14.899 1.00 27.31 ? 214 ASN A CB 1 +ATOM 1758 C CG . ASN A 1 214 ? 1.479 8.279 -14.822 1.00 30.24 ? 214 ASN A CG 1 +ATOM 1759 O OD1 . ASN A 1 214 ? 0.744 7.346 -15.163 1.00 32.47 ? 214 ASN A OD1 1 +ATOM 1760 N ND2 . ASN A 1 214 ? 2.714 8.047 -14.430 1.00 29.78 ? 214 ASN A ND2 1 +ATOM 1761 N N . GLY A 1 215 ? 0.848 12.529 -17.260 1.00 26.51 ? 215 GLY A N 1 +ATOM 1762 C CA . GLY A 1 215 ? 0.065 13.709 -17.623 1.00 26.05 ? 215 GLY A CA 1 +ATOM 1763 C C . GLY A 1 215 ? 0.186 15.021 -16.870 1.00 24.55 ? 215 GLY A C 1 +ATOM 1764 O O . GLY A 1 215 ? -0.239 16.059 -17.380 1.00 25.20 ? 215 GLY A O 1 +ATOM 1765 N N A ASP A 1 216 ? 0.744 14.999 -15.654 0.50 23.04 ? 216 ASP A N 1 +ATOM 1766 N N B ASP A 1 216 ? 0.748 14.992 -15.660 0.50 23.39 ? 216 ASP A N 1 +ATOM 1767 C CA A ASP A 1 216 ? 0.891 16.222 -14.868 0.50 22.25 ? 216 ASP A CA 1 +ATOM 1768 C CA B ASP A 1 216 ? 0.909 16.203 -14.862 0.50 22.94 ? 216 ASP A CA 1 +ATOM 1769 C C A ASP A 1 216 ? 2.182 16.909 -15.280 0.50 22.70 ? 216 ASP A C 1 +ATOM 1770 C C B ASP A 1 216 ? 2.192 16.893 -15.307 0.50 23.02 ? 216 ASP A C 1 +ATOM 1771 O O A ASP A 1 216 ? 3.265 16.409 -14.988 0.50 23.46 ? 216 ASP A O 1 +ATOM 1772 O O B ASP A 1 216 ? 3.280 16.379 -15.060 0.50 23.77 ? 216 ASP A O 1 +ATOM 1773 C CB A ASP A 1 216 ? 0.863 15.910 -13.369 0.50 22.37 ? 216 ASP A CB 1 +ATOM 1774 C CB B ASP A 1 216 ? 0.959 15.849 -13.368 0.50 24.09 ? 216 ASP A CB 1 +ATOM 1775 C CG A ASP A 1 216 ? -0.442 15.298 -12.907 0.50 24.19 ? 216 ASP A CG 1 +ATOM 1776 C CG B ASP A 1 216 ? -0.170 16.456 -12.563 0.50 27.89 ? 216 ASP A CG 1 +ATOM 1777 O OD1 A ASP A 1 216 ? -1.477 15.540 -13.561 0.50 24.19 ? 216 ASP A OD1 1 +ATOM 1778 O OD1 B ASP A 1 216 ? -0.595 17.580 -12.895 0.50 28.66 ? 216 ASP A OD1 1 +ATOM 1779 O OD2 A ASP A 1 216 ? -0.430 14.579 -11.889 0.50 25.07 ? 216 ASP A OD2 1 +ATOM 1780 O OD2 B ASP A 1 216 ? -0.618 15.812 -11.589 0.50 29.52 ? 216 ASP A OD2 1 +ATOM 1781 N N . ARG A 1 217 ? 2.073 18.016 -16.019 1.00 21.99 ? 217 ARG A N 1 +ATOM 1782 C CA . ARG A 1 217 ? 3.233 18.713 -16.564 1.00 20.81 ? 217 ARG A CA 1 +ATOM 1783 C C . ARG A 1 217 ? 3.263 20.218 -16.299 1.00 19.92 ? 217 ARG A C 1 +ATOM 1784 O O . ARG A 1 217 ? 4.105 20.898 -16.881 1.00 19.51 ? 217 ARG A O 1 +ATOM 1785 C CB . ARG A 1 217 ? 3.252 18.535 -18.107 0.50 21.37 ? 217 ARG A CB 1 +ATOM 1786 C CG . ARG A 1 217 ? 2.978 17.127 -18.645 0.50 23.57 ? 217 ARG A CG 1 +ATOM 1787 C CD . ARG A 1 217 ? 2.523 17.152 -20.100 0.50 25.14 ? 217 ARG A CD 1 +ATOM 1788 N NE . ARG A 1 217 ? 3.525 17.746 -20.981 0.50 25.70 ? 217 ARG A NE 1 +ATOM 1789 C CZ . ARG A 1 217 ? 4.427 17.041 -21.650 0.50 25.29 ? 217 ARG A CZ 1 +ATOM 1790 N NH1 . ARG A 1 217 ? 5.318 17.652 -22.418 0.50 24.48 ? 217 ARG A NH1 1 +ATOM 1791 N NH2 . ARG A 1 217 ? 4.448 15.719 -21.555 0.50 23.66 ? 217 ARG A NH2 1 +ATOM 1792 N N . TRP A 1 218 ? 2.347 20.759 -15.483 1.00 19.50 ? 218 TRP A N 1 +ATOM 1793 C CA . TRP A 1 218 ? 2.290 22.214 -15.276 1.00 19.27 ? 218 TRP A CA 1 +ATOM 1794 C C . TRP A 1 218 ? 3.589 22.829 -14.740 1.00 19.18 ? 218 TRP A C 1 +ATOM 1795 O O . TRP A 1 218 ? 3.833 24.006 -14.958 1.00 19.69 ? 218 TRP A O 1 +ATOM 1796 C CB . TRP A 1 218 ? 1.102 22.617 -14.384 1.00 19.08 ? 218 TRP A CB 1 +ATOM 1797 C CG . TRP A 1 218 ? 1.172 22.070 -12.987 1.00 18.92 ? 218 TRP A CG 1 +ATOM 1798 C CD1 . TRP A 1 218 ? 0.547 20.956 -12.513 1.00 19.63 ? 218 TRP A CD1 1 +ATOM 1799 C CD2 . TRP A 1 218 ? 1.858 22.655 -11.864 1.00 19.21 ? 218 TRP A CD2 1 +ATOM 1800 N NE1 . TRP A 1 218 ? 0.866 20.766 -11.187 1.00 19.83 ? 218 TRP A NE1 1 +ATOM 1801 C CE2 . TRP A 1 218 ? 1.651 21.805 -10.761 1.00 19.68 ? 218 TRP A CE2 1 +ATOM 1802 C CE3 . TRP A 1 218 ? 2.647 23.803 -11.692 1.00 19.71 ? 218 TRP A CE3 1 +ATOM 1803 C CZ2 . TRP A 1 218 ? 2.230 22.048 -9.514 1.00 19.83 ? 218 TRP A CZ2 1 +ATOM 1804 C CZ3 . TRP A 1 218 ? 3.229 24.034 -10.460 1.00 20.19 ? 218 TRP A CZ3 1 +ATOM 1805 C CH2 . TRP A 1 218 ? 3.000 23.174 -9.383 1.00 20.04 ? 218 TRP A CH2 1 +ATOM 1806 N N . PHE A 1 219 ? 4.383 22.040 -14.003 1.00 18.30 ? 219 PHE A N 1 +ATOM 1807 C CA . PHE A 1 219 ? 5.624 22.483 -13.356 1.00 17.79 ? 219 PHE A CA 1 +ATOM 1808 C C . PHE A 1 219 ? 6.842 22.530 -14.276 1.00 18.51 ? 219 PHE A C 1 +ATOM 1809 O O . PHE A 1 219 ? 7.911 22.994 -13.861 1.00 18.69 ? 219 PHE A O 1 +ATOM 1810 C CB . PHE A 1 219 ? 5.920 21.590 -12.136 1.00 16.65 ? 219 PHE A CB 1 +ATOM 1811 C CG . PHE A 1 219 ? 5.997 20.133 -12.506 1.00 15.65 ? 219 PHE A CG 1 +ATOM 1812 C CD1 . PHE A 1 219 ? 7.163 19.591 -13.018 1.00 15.83 ? 219 PHE A CD1 1 +ATOM 1813 C CD2 . PHE A 1 219 ? 4.885 19.316 -12.400 1.00 15.39 ? 219 PHE A CD2 1 +ATOM 1814 C CE1 . PHE A 1 219 ? 7.210 18.266 -13.417 1.00 15.82 ? 219 PHE A CE1 1 +ATOM 1815 C CE2 . PHE A 1 219 ? 4.956 17.985 -12.749 1.00 15.80 ? 219 PHE A CE2 1 +ATOM 1816 C CZ . PHE A 1 219 ? 6.103 17.475 -13.293 1.00 15.51 ? 219 PHE A CZ 1 +ATOM 1817 N N . LEU A 1 220 ? 6.703 22.044 -15.520 1.00 18.09 ? 220 LEU A N 1 +ATOM 1818 C CA . LEU A 1 220 ? 7.800 22.117 -16.472 1.00 19.03 ? 220 LEU A CA 1 +ATOM 1819 C C . LEU A 1 220 ? 7.971 23.571 -16.859 1.00 20.12 ? 220 LEU A C 1 +ATOM 1820 O O . LEU A 1 220 ? 6.988 24.309 -16.991 1.00 20.85 ? 220 LEU A O 1 +ATOM 1821 C CB . LEU A 1 220 ? 7.525 21.266 -17.709 1.00 19.05 ? 220 LEU A CB 1 +ATOM 1822 C CG . LEU A 1 220 ? 7.424 19.768 -17.467 1.00 19.56 ? 220 LEU A CG 1 +ATOM 1823 C CD1 . LEU A 1 220 ? 7.122 19.044 -18.764 1.00 19.47 ? 220 LEU A CD1 1 +ATOM 1824 C CD2 . LEU A 1 220 ? 8.694 19.212 -16.777 1.00 20.00 ? 220 LEU A CD2 1 +ATOM 1825 N N . ASN A 1 221 ? 9.214 23.996 -16.965 1.00 20.10 ? 221 ASN A N 1 +ATOM 1826 C CA . ASN A 1 221 ? 9.510 25.383 -17.252 1.00 20.10 ? 221 ASN A CA 1 +ATOM 1827 C C . ASN A 1 221 ? 10.545 25.542 -18.362 1.00 19.74 ? 221 ASN A C 1 +ATOM 1828 O O . ASN A 1 221 ? 11.001 24.563 -18.944 1.00 20.14 ? 221 ASN A O 1 +ATOM 1829 C CB . ASN A 1 221 ? 9.905 26.097 -15.960 1.00 20.92 ? 221 ASN A CB 1 +ATOM 1830 C CG . ASN A 1 221 ? 11.146 25.546 -15.329 1.00 23.14 ? 221 ASN A CG 1 +ATOM 1831 O OD1 . ASN A 1 221 ? 12.101 25.106 -15.998 1.00 22.57 ? 221 ASN A OD1 1 +ATOM 1832 N ND2 . ASN A 1 221 ? 11.167 25.582 -14.017 1.00 23.81 ? 221 ASN A ND2 1 +ATOM 1833 N N . ARG A 1 222 ? 10.877 26.784 -18.683 1.00 18.88 ? 222 ARG A N 1 +ATOM 1834 C CA . ARG A 1 222 ? 11.832 27.102 -19.726 1.00 18.93 ? 222 ARG A CA 1 +ATOM 1835 C C . ARG A 1 222 ? 13.271 27.127 -19.238 1.00 18.41 ? 222 ARG A C 1 +ATOM 1836 O O . ARG A 1 222 ? 14.134 27.579 -19.982 1.00 18.72 ? 222 ARG A O 1 +ATOM 1837 C CB . ARG A 1 222 ? 11.491 28.498 -20.253 1.00 20.02 ? 222 ARG A CB 1 +ATOM 1838 C CG . ARG A 1 222 ? 10.094 28.584 -20.823 1.00 23.44 ? 222 ARG A CG 1 +ATOM 1839 C CD . ARG A 1 222 ? 9.746 29.989 -21.277 1.00 26.45 ? 222 ARG A CD 1 +ATOM 1840 N NE . ARG A 1 222 ? 8.499 29.999 -22.037 1.00 28.59 ? 222 ARG A NE 1 +ATOM 1841 C CZ . ARG A 1 222 ? 8.402 29.730 -23.335 1.00 31.63 ? 222 ARG A CZ 1 +ATOM 1842 N NH1 . ARG A 1 222 ? 9.488 29.449 -24.047 1.00 31.12 ? 222 ARG A NH1 1 +ATOM 1843 N NH2 . ARG A 1 222 ? 7.218 29.741 -23.933 1.00 31.84 ? 222 ARG A NH2 1 +ATOM 1844 N N . PHE A 1 223 ? 13.552 26.663 -18.016 1.00 17.24 ? 223 PHE A N 1 +ATOM 1845 C CA . PHE A 1 223 ? 14.877 26.810 -17.437 1.00 17.43 ? 223 PHE A CA 1 +ATOM 1846 C C . PHE A 1 223 ? 15.704 25.551 -17.362 1.00 15.35 ? 223 PHE A C 1 +ATOM 1847 O O . PHE A 1 223 ? 15.192 24.438 -17.466 1.00 15.55 ? 223 PHE A O 1 +ATOM 1848 C CB . PHE A 1 223 ? 14.761 27.413 -16.009 1.00 18.71 ? 223 PHE A CB 1 +ATOM 1849 C CG . PHE A 1 223 ? 13.758 28.531 -15.821 1.00 20.74 ? 223 PHE A CG 1 +ATOM 1850 C CD1 . PHE A 1 223 ? 13.624 29.530 -16.768 1.00 22.13 ? 223 PHE A CD1 1 +ATOM 1851 C CD2 . PHE A 1 223 ? 12.977 28.595 -14.684 1.00 22.23 ? 223 PHE A CD2 1 +ATOM 1852 C CE1 . PHE A 1 223 ? 12.696 30.547 -16.598 1.00 23.38 ? 223 PHE A CE1 1 +ATOM 1853 C CE2 . PHE A 1 223 ? 12.071 29.627 -14.501 1.00 23.56 ? 223 PHE A CE2 1 +ATOM 1854 C CZ . PHE A 1 223 ? 11.935 30.596 -15.459 1.00 23.59 ? 223 PHE A CZ 1 +ATOM 1855 N N . THR A 1 224 ? 17.002 25.743 -17.157 1.00 14.22 ? 224 THR A N 1 +ATOM 1856 C CA . THR A 1 224 ? 17.923 24.681 -16.819 1.00 13.87 ? 224 THR A CA 1 +ATOM 1857 C C . THR A 1 224 ? 18.777 25.156 -15.619 1.00 14.09 ? 224 THR A C 1 +ATOM 1858 O O . THR A 1 224 ? 18.645 26.293 -15.133 1.00 14.76 ? 224 THR A O 1 +ATOM 1859 C CB . THR A 1 224 ? 18.695 24.154 -18.032 1.00 14.52 ? 224 THR A CB 1 +ATOM 1860 O OG1 . THR A 1 224 ? 19.214 22.865 -17.666 1.00 14.05 ? 224 THR A OG1 1 +ATOM 1861 C CG2 . THR A 1 224 ? 19.849 25.052 -18.412 1.00 14.98 ? 224 THR A CG2 1 +ATOM 1862 N N . THR A 1 225 ? 19.601 24.275 -15.099 1.00 13.19 ? 225 THR A N 1 +ATOM 1863 C CA . THR A 1 225 ? 20.500 24.563 -14.003 1.00 13.50 ? 225 THR A CA 1 +ATOM 1864 C C . THR A 1 225 ? 21.729 23.647 -14.160 1.00 13.55 ? 225 THR A C 1 +ATOM 1865 O O . THR A 1 225 ? 21.844 22.918 -15.145 1.00 13.01 ? 225 THR A O 1 +ATOM 1866 C CB . THR A 1 225 ? 19.759 24.407 -12.648 1.00 15.53 ? 225 THR A CB 1 +ATOM 1867 O OG1 . THR A 1 225 ? 20.659 24.812 -11.628 1.00 17.08 ? 225 THR A OG1 1 +ATOM 1868 C CG2 . THR A 1 225 ? 19.333 22.975 -12.374 1.00 16.36 ? 225 THR A CG2 1 +ATOM 1869 N N . THR A 1 226 ? 22.671 23.746 -13.226 1.00 13.79 ? 226 THR A N 1 +ATOM 1870 C CA . THR A 1 226 ? 23.834 22.885 -13.142 1.00 13.97 ? 226 THR A CA 1 +ATOM 1871 C C . THR A 1 226 ? 23.718 22.116 -11.827 1.00 14.17 ? 226 THR A C 1 +ATOM 1872 O O . THR A 1 226 ? 22.936 22.501 -10.957 1.00 13.64 ? 226 THR A O 1 +ATOM 1873 C CB . THR A 1 226 ? 25.130 23.738 -13.146 1.00 16.08 ? 226 THR A CB 1 +ATOM 1874 O OG1 . THR A 1 226 ? 25.192 24.499 -11.938 1.00 16.64 ? 226 THR A OG1 1 +ATOM 1875 C CG2 . THR A 1 226 ? 25.245 24.618 -14.361 1.00 17.33 ? 226 THR A CG2 1 +ATOM 1876 N N A LEU A 1 227 ? 24.519 21.061 -11.653 0.50 14.30 ? 227 LEU A N 1 +ATOM 1877 N N B LEU A 1 227 ? 24.524 21.056 -11.640 0.50 14.01 ? 227 LEU A N 1 +ATOM 1878 C CA A LEU A 1 227 ? 24.520 20.302 -10.408 0.50 15.27 ? 227 LEU A CA 1 +ATOM 1879 C CA B LEU A 1 227 ? 24.508 20.322 -10.373 0.50 14.69 ? 227 LEU A CA 1 +ATOM 1880 C C A LEU A 1 227 ? 24.897 21.190 -9.216 0.50 15.82 ? 227 LEU A C 1 +ATOM 1881 C C B LEU A 1 227 ? 24.873 21.224 -9.206 0.50 15.51 ? 227 LEU A C 1 +ATOM 1882 O O A LEU A 1 227 ? 24.223 21.149 -8.192 0.50 16.27 ? 227 LEU A O 1 +ATOM 1883 O O B LEU A 1 227 ? 24.172 21.226 -8.197 0.50 15.90 ? 227 LEU A O 1 +ATOM 1884 C CB A LEU A 1 227 ? 25.476 19.108 -10.535 0.50 15.64 ? 227 LEU A CB 1 +ATOM 1885 C CB B LEU A 1 227 ? 25.440 19.112 -10.410 0.50 14.62 ? 227 LEU A CB 1 +ATOM 1886 C CG A LEU A 1 227 ? 25.138 17.847 -9.735 0.50 17.11 ? 227 LEU A CG 1 +ATOM 1887 C CG B LEU A 1 227 ? 24.906 17.875 -11.109 0.50 15.35 ? 227 LEU A CG 1 +ATOM 1888 C CD1 A LEU A 1 227 ? 23.676 17.439 -9.907 0.50 17.60 ? 227 LEU A CD1 1 +ATOM 1889 C CD1 B LEU A 1 227 ? 25.881 16.725 -10.955 0.50 15.25 ? 227 LEU A CD1 1 +ATOM 1890 C CD2 A LEU A 1 227 ? 26.019 16.702 -10.161 0.50 17.33 ? 227 LEU A CD2 1 +ATOM 1891 C CD2 B LEU A 1 227 ? 23.531 17.463 -10.562 0.50 15.94 ? 227 LEU A CD2 1 +ATOM 1892 N N . ASN A 1 228 ? 25.916 22.051 -9.374 1.00 15.51 ? 228 ASN A N 1 +ATOM 1893 C CA . ASN A 1 228 ? 26.326 22.950 -8.300 1.00 15.00 ? 228 ASN A CA 1 +ATOM 1894 C C . ASN A 1 228 ? 25.286 24.033 -7.986 1.00 14.90 ? 228 ASN A C 1 +ATOM 1895 O O . ASN A 1 228 ? 25.056 24.317 -6.813 1.00 15.98 ? 228 ASN A O 1 +ATOM 1896 C CB . ASN A 1 228 ? 27.700 23.551 -8.581 1.00 15.85 ? 228 ASN A CB 1 +ATOM 1897 C CG . ASN A 1 228 ? 28.840 22.550 -8.522 1.00 19.59 ? 228 ASN A CG 1 +ATOM 1898 O OD1 . ASN A 1 228 ? 29.929 22.794 -9.060 1.00 21.73 ? 228 ASN A OD1 1 +ATOM 1899 N ND2 . ASN A 1 228 ? 28.635 21.411 -7.881 1.00 20.10 ? 228 ASN A ND2 1 +ATOM 1900 N N . ASP A 1 229 ? 24.638 24.604 -9.002 1.00 14.47 ? 229 ASP A N 1 +ATOM 1901 C CA . ASP A 1 229 ? 23.626 25.638 -8.756 1.00 14.83 ? 229 ASP A CA 1 +ATOM 1902 C C . ASP A 1 229 ? 22.417 25.008 -8.087 1.00 15.00 ? 229 ASP A C 1 +ATOM 1903 O O . ASP A 1 229 ? 21.915 25.535 -7.090 1.00 15.74 ? 229 ASP A O 1 +ATOM 1904 C CB . ASP A 1 229 ? 23.213 26.348 -10.049 1.00 17.00 ? 229 ASP A CB 1 +ATOM 1905 C CG . ASP A 1 229 ? 22.101 27.337 -9.811 1.00 23.28 ? 229 ASP A CG 1 +ATOM 1906 O OD1 . ASP A 1 229 ? 22.347 28.337 -9.109 1.00 25.03 ? 229 ASP A OD1 1 +ATOM 1907 O OD2 . ASP A 1 229 ? 20.957 27.068 -10.265 1.00 24.97 ? 229 ASP A OD2 1 +ATOM 1908 N N . PHE A 1 230 ? 21.979 23.838 -8.584 1.00 14.41 ? 230 PHE A N 1 +ATOM 1909 C CA . PHE A 1 230 ? 20.850 23.142 -7.980 1.00 14.40 ? 230 PHE A CA 1 +ATOM 1910 C C . PHE A 1 230 ? 21.151 22.818 -6.516 1.00 15.23 ? 230 PHE A C 1 +ATOM 1911 O O . PHE A 1 230 ? 20.308 23.067 -5.661 1.00 16.01 ? 230 PHE A O 1 +ATOM 1912 C CB . PHE A 1 230 ? 20.527 21.845 -8.745 1.00 13.67 ? 230 PHE A CB 1 +ATOM 1913 C CG . PHE A 1 230 ? 19.422 21.092 -8.049 1.00 14.69 ? 230 PHE A CG 1 +ATOM 1914 C CD1 . PHE A 1 230 ? 18.100 21.467 -8.213 1.00 15.26 ? 230 PHE A CD1 1 +ATOM 1915 C CD2 . PHE A 1 230 ? 19.715 20.119 -7.106 1.00 15.80 ? 230 PHE A CD2 1 +ATOM 1916 C CE1 . PHE A 1 230 ? 17.088 20.834 -7.504 1.00 16.46 ? 230 PHE A CE1 1 +ATOM 1917 C CE2 . PHE A 1 230 ? 18.704 19.520 -6.370 1.00 16.25 ? 230 PHE A CE2 1 +ATOM 1918 C CZ . PHE A 1 230 ? 17.399 19.868 -6.589 1.00 16.71 ? 230 PHE A CZ 1 +ATOM 1919 N N . ASN A 1 231 ? 22.374 22.361 -6.232 1.00 15.00 ? 231 ASN A N 1 +ATOM 1920 C CA . ASN A 1 231 ? 22.758 22.003 -4.873 1.00 15.46 ? 231 ASN A CA 1 +ATOM 1921 C C . ASN A 1 231 ? 22.802 23.158 -3.914 1.00 16.96 ? 231 ASN A C 1 +ATOM 1922 O O . ASN A 1 231 ? 22.591 22.932 -2.725 1.00 17.72 ? 231 ASN A O 1 +ATOM 1923 C CB . ASN A 1 231 ? 24.050 21.215 -4.849 1.00 16.36 ? 231 ASN A CB 1 +ATOM 1924 C CG . ASN A 1 231 ? 23.829 19.796 -5.314 1.00 18.15 ? 231 ASN A CG 1 +ATOM 1925 O OD1 . ASN A 1 231 ? 22.721 19.254 -5.242 1.00 18.68 ? 231 ASN A OD1 1 +ATOM 1926 N ND2 . ASN A 1 231 ? 24.868 19.145 -5.804 1.00 19.47 ? 231 ASN A ND2 1 +ATOM 1927 N N . LEU A 1 232 ? 22.976 24.394 -4.396 1.00 17.68 ? 232 LEU A N 1 +ATOM 1928 C CA . LEU A 1 232 ? 22.885 25.567 -3.519 1.00 19.22 ? 232 LEU A CA 1 +ATOM 1929 C C . LEU A 1 232 ? 21.437 25.670 -3.002 1.00 19.67 ? 232 LEU A C 1 +ATOM 1930 O O . LEU A 1 232 ? 21.223 25.880 -1.806 1.00 20.80 ? 232 LEU A O 1 +ATOM 1931 C CB . LEU A 1 232 ? 23.257 26.842 -4.289 1.00 20.79 ? 232 LEU A CB 1 +ATOM 1932 C CG . LEU A 1 232 ? 24.717 26.974 -4.677 1.00 23.66 ? 232 LEU A CG 1 +ATOM 1933 C CD1 . LEU A 1 232 ? 24.933 28.250 -5.452 1.00 24.78 ? 232 LEU A CD1 1 +ATOM 1934 C CD2 . LEU A 1 232 ? 25.615 26.984 -3.447 1.00 24.66 ? 232 LEU A CD2 1 +ATOM 1935 N N . VAL A 1 233 ? 20.459 25.417 -3.886 1.00 18.99 ? 233 VAL A N 1 +ATOM 1936 C CA . VAL A 1 233 ? 19.045 25.406 -3.533 1.00 18.83 ? 233 VAL A CA 1 +ATOM 1937 C C . VAL A 1 233 ? 18.700 24.193 -2.684 1.00 18.78 ? 233 VAL A C 1 +ATOM 1938 O O . VAL A 1 233 ? 18.008 24.331 -1.675 1.00 19.12 ? 233 VAL A O 1 +ATOM 1939 C CB . VAL A 1 233 ? 18.177 25.464 -4.804 1.00 20.10 ? 233 VAL A CB 1 +ATOM 1940 C CG1 . VAL A 1 233 ? 16.694 25.454 -4.446 1.00 20.95 ? 233 VAL A CG1 1 +ATOM 1941 C CG2 . VAL A 1 233 ? 18.525 26.699 -5.624 1.00 20.92 ? 233 VAL A CG2 1 +ATOM 1942 N N . ALA A 1 234 ? 19.239 23.018 -3.016 1.00 18.51 ? 234 ALA A N 1 +ATOM 1943 C CA . ALA A 1 234 ? 18.996 21.802 -2.227 1.00 19.45 ? 234 ALA A CA 1 +ATOM 1944 C C . ALA A 1 234 ? 19.449 22.000 -0.771 1.00 20.44 ? 234 ALA A C 1 +ATOM 1945 O O . ALA A 1 234 ? 18.700 21.699 0.153 1.00 20.35 ? 234 ALA A O 1 +ATOM 1946 C CB . ALA A 1 234 ? 19.732 20.621 -2.849 1.00 19.88 ? 234 ALA A CB 1 +ATOM 1947 N N . MET A 1 235 ? 20.620 22.616 -0.569 1.00 20.53 ? 235 MET A N 1 +ATOM 1948 C CA . MET A 1 235 ? 21.139 22.894 0.770 1.00 21.06 ? 235 MET A CA 1 +ATOM 1949 C C . MET A 1 235 ? 20.163 23.771 1.556 1.00 19.75 ? 235 MET A C 1 +ATOM 1950 O O . MET A 1 235 ? 19.813 23.447 2.691 1.00 19.72 ? 235 MET A O 1 +ATOM 1951 C CB . MET A 1 235 ? 22.522 23.574 0.668 1.00 23.60 ? 235 MET A CB 1 +ATOM 1952 C CG . MET A 1 235 ? 23.037 24.121 1.984 1.00 29.30 ? 235 MET A CG 1 +ATOM 1953 S SD . MET A 1 235 ? 24.257 23.025 2.705 1.00 42.88 ? 235 MET A SD 1 +ATOM 1954 C CE . MET A 1 235 ? 25.589 23.247 1.552 1.00 39.42 ? 235 MET A CE 1 +ATOM 1955 N N . LYS A 1 236 ? 19.700 24.853 0.927 1.00 18.47 ? 236 LYS A N 1 +ATOM 1956 C CA . LYS A 1 236 ? 18.792 25.785 1.563 1.00 17.97 ? 236 LYS A CA 1 +ATOM 1957 C C . LYS A 1 236 ? 17.493 25.121 2.014 1.00 17.43 ? 236 LYS A C 1 +ATOM 1958 O O . LYS A 1 236 ? 16.951 25.470 3.058 1.00 18.51 ? 236 LYS A O 1 +ATOM 1959 C CB . LYS A 1 236 ? 18.530 26.978 0.623 1.00 20.89 ? 236 LYS A CB 1 +ATOM 1960 C CG . LYS A 1 236 ? 17.528 27.986 1.164 1.00 26.53 ? 236 LYS A CG 1 +ATOM 1961 C CD . LYS A 1 236 ? 17.172 29.030 0.127 1.00 33.01 ? 236 LYS A CD 1 +ATOM 1962 C CE . LYS A 1 236 ? 15.990 29.854 0.572 1.00 37.50 ? 236 LYS A CE 1 +ATOM 1963 N NZ . LYS A 1 236 ? 16.358 30.835 1.631 1.00 40.05 ? 236 LYS A NZ 1 +ATOM 1964 N N . TYR A 1 237 ? 17.020 24.124 1.260 1.00 15.66 ? 237 TYR A N 1 +ATOM 1965 C CA . TYR A 1 237 ? 15.746 23.472 1.564 1.00 14.78 ? 237 TYR A CA 1 +ATOM 1966 C C . TYR A 1 237 ? 15.852 22.109 2.238 1.00 14.96 ? 237 TYR A C 1 +ATOM 1967 O O . TYR A 1 237 ? 14.861 21.366 2.262 1.00 15.72 ? 237 TYR A O 1 +ATOM 1968 C CB . TYR A 1 237 ? 14.899 23.373 0.286 1.00 14.56 ? 237 TYR A CB 1 +ATOM 1969 C CG . TYR A 1 237 ? 14.367 24.728 -0.118 1.00 15.63 ? 237 TYR A CG 1 +ATOM 1970 C CD1 . TYR A 1 237 ? 13.223 25.245 0.467 1.00 16.68 ? 237 TYR A CD1 1 +ATOM 1971 C CD2 . TYR A 1 237 ? 15.067 25.534 -1.005 1.00 16.39 ? 237 TYR A CD2 1 +ATOM 1972 C CE1 . TYR A 1 237 ? 12.778 26.527 0.169 1.00 17.54 ? 237 TYR A CE1 1 +ATOM 1973 C CE2 . TYR A 1 237 ? 14.617 26.808 -1.333 1.00 16.88 ? 237 TYR A CE2 1 +ATOM 1974 C CZ . TYR A 1 237 ? 13.486 27.312 -0.721 1.00 18.39 ? 237 TYR A CZ 1 +ATOM 1975 O OH . TYR A 1 237 ? 13.013 28.560 -1.046 1.00 19.90 ? 237 TYR A OH 1 +ATOM 1976 N N A ASN A 1 238 ? 17.029 21.783 2.777 0.50 14.71 ? 238 ASN A N 1 +ATOM 1977 N N B ASN A 1 238 ? 17.031 21.780 2.788 0.50 14.49 ? 238 ASN A N 1 +ATOM 1978 C CA A ASN A 1 238 ? 17.254 20.514 3.458 0.50 15.20 ? 238 ASN A CA 1 +ATOM 1979 C CA B ASN A 1 238 ? 17.284 20.504 3.467 0.50 14.74 ? 238 ASN A CA 1 +ATOM 1980 C C A ASN A 1 238 ? 16.986 19.323 2.549 0.50 14.96 ? 238 ASN A C 1 +ATOM 1981 C C B ASN A 1 238 ? 17.054 19.295 2.568 0.50 14.80 ? 238 ASN A C 1 +ATOM 1982 O O A ASN A 1 238 ? 16.317 18.373 2.941 0.50 15.04 ? 238 ASN A O 1 +ATOM 1983 O O B ASN A 1 238 ? 16.509 18.281 3.000 0.50 14.95 ? 238 ASN A O 1 +ATOM 1984 C CB A ASN A 1 238 ? 16.460 20.437 4.761 0.50 17.13 ? 238 ASN A CB 1 +ATOM 1985 C CB B ASN A 1 238 ? 16.506 20.379 4.782 0.50 15.99 ? 238 ASN A CB 1 +ATOM 1986 C CG A ASN A 1 238 ? 16.882 21.508 5.733 0.50 21.05 ? 238 ASN A CG 1 +ATOM 1987 C CG B ASN A 1 238 ? 17.068 21.220 5.903 0.50 18.49 ? 238 ASN A CG 1 +ATOM 1988 O OD1 A ASN A 1 238 ? 16.104 22.393 6.115 0.50 22.39 ? 238 ASN A OD1 1 +ATOM 1989 O OD1 B ASN A 1 238 ? 18.118 21.861 5.772 0.50 18.96 ? 238 ASN A OD1 1 +ATOM 1990 N ND2 A ASN A 1 238 ? 18.142 21.469 6.126 0.50 21.55 ? 238 ASN A ND2 1 +ATOM 1991 N ND2 B ASN A 1 238 ? 16.368 21.244 7.026 0.50 19.10 ? 238 ASN A ND2 1 +ATOM 1992 N N . TYR A 1 239 ? 17.462 19.417 1.309 1.00 14.63 ? 239 TYR A N 1 +ATOM 1993 C CA . TYR A 1 239 ? 17.378 18.342 0.336 1.00 14.81 ? 239 TYR A CA 1 +ATOM 1994 C C . TYR A 1 239 ? 18.779 17.746 0.260 1.00 15.52 ? 239 TYR A C 1 +ATOM 1995 O O . TYR A 1 239 ? 19.769 18.452 0.460 1.00 16.11 ? 239 TYR A O 1 +ATOM 1996 C CB . TYR A 1 239 ? 17.039 18.905 -1.050 1.00 14.64 ? 239 TYR A CB 1 +ATOM 1997 C CG . TYR A 1 239 ? 15.569 18.840 -1.373 1.00 14.52 ? 239 TYR A CG 1 +ATOM 1998 C CD1 . TYR A 1 239 ? 14.637 19.491 -0.584 1.00 14.91 ? 239 TYR A CD1 1 +ATOM 1999 C CD2 . TYR A 1 239 ? 15.115 18.175 -2.502 1.00 14.55 ? 239 TYR A CD2 1 +ATOM 2000 C CE1 . TYR A 1 239 ? 13.281 19.426 -0.871 1.00 15.52 ? 239 TYR A CE1 1 +ATOM 2001 C CE2 . TYR A 1 239 ? 13.766 18.114 -2.809 1.00 15.01 ? 239 TYR A CE2 1 +ATOM 2002 C CZ . TYR A 1 239 ? 12.850 18.743 -1.992 1.00 15.84 ? 239 TYR A CZ 1 +ATOM 2003 O OH . TYR A 1 239 ? 11.509 18.631 -2.269 1.00 16.32 ? 239 TYR A OH 1 +ATOM 2004 N N A GLU A 1 240 ? 18.870 16.448 -0.030 0.50 15.37 ? 240 GLU A N 1 +ATOM 2005 N N B GLU A 1 240 ? 18.868 16.461 -0.067 0.50 15.60 ? 240 GLU A N 1 +ATOM 2006 C CA A GLU A 1 240 ? 20.154 15.777 -0.186 0.50 16.23 ? 240 GLU A CA 1 +ATOM 2007 C CA B GLU A 1 240 ? 20.151 15.796 -0.223 0.50 16.61 ? 240 GLU A CA 1 +ATOM 2008 C C A GLU A 1 240 ? 20.879 16.322 -1.420 0.50 16.43 ? 240 GLU A C 1 +ATOM 2009 C C B GLU A 1 240 ? 20.878 16.350 -1.428 0.50 16.61 ? 240 GLU A C 1 +ATOM 2010 O O A GLU A 1 240 ? 20.244 16.585 -2.438 0.50 15.69 ? 240 GLU A O 1 +ATOM 2011 O O B GLU A 1 240 ? 20.249 16.611 -2.453 0.50 15.86 ? 240 GLU A O 1 +ATOM 2012 C CB A GLU A 1 240 ? 19.925 14.265 -0.355 0.50 18.78 ? 240 GLU A CB 1 +ATOM 2013 C CB B GLU A 1 240 ? 19.929 14.302 -0.446 0.50 19.82 ? 240 GLU A CB 1 +ATOM 2014 C CG A GLU A 1 240 ? 19.511 13.580 0.931 0.50 23.01 ? 240 GLU A CG 1 +ATOM 2015 C CG B GLU A 1 240 ? 19.757 13.549 0.847 0.50 25.74 ? 240 GLU A CG 1 +ATOM 2016 C CD A GLU A 1 240 ? 20.607 13.558 1.976 0.50 27.97 ? 240 GLU A CD 1 +ATOM 2017 C CD B GLU A 1 240 ? 19.839 12.057 0.654 0.50 32.83 ? 240 GLU A CD 1 +ATOM 2018 O OE1 A GLU A 1 240 ? 21.558 12.757 1.825 0.50 28.30 ? 240 GLU A OE1 1 +ATOM 2019 O OE1 B GLU A 1 240 ? 19.029 11.520 -0.134 0.50 34.72 ? 240 GLU A OE1 1 +ATOM 2020 O OE2 A GLU A 1 240 ? 20.521 14.346 2.943 0.50 29.56 ? 240 GLU A OE2 1 +ATOM 2021 O OE2 B GLU A 1 240 ? 20.715 11.421 1.281 0.50 35.82 ? 240 GLU A OE2 1 +ATOM 2022 N N . PRO A 1 241 ? 22.205 16.501 -1.358 1.00 17.14 ? 241 PRO A N 1 +ATOM 2023 C CA . PRO A 1 241 ? 22.942 16.989 -2.541 1.00 18.08 ? 241 PRO A CA 1 +ATOM 2024 C C . PRO A 1 241 ? 22.812 15.998 -3.698 1.00 17.98 ? 241 PRO A C 1 +ATOM 2025 O O . PRO A 1 241 ? 22.874 14.796 -3.468 1.00 18.99 ? 241 PRO A O 1 +ATOM 2026 C CB . PRO A 1 241 ? 24.400 17.037 -2.063 1.00 19.59 ? 241 PRO A CB 1 +ATOM 2027 C CG . PRO A 1 241 ? 24.323 17.034 -0.568 1.00 19.93 ? 241 PRO A CG 1 +ATOM 2028 C CD . PRO A 1 241 ? 23.111 16.247 -0.217 1.00 17.24 ? 241 PRO A CD 1 +ATOM 2029 N N . LEU A 1 242 ? 22.540 16.485 -4.895 1.00 17.16 ? 242 LEU A N 1 +ATOM 2030 C CA . LEU A 1 242 ? 22.418 15.624 -6.060 1.00 17.79 ? 242 LEU A CA 1 +ATOM 2031 C C . LEU A 1 242 ? 23.822 15.392 -6.612 1.00 17.81 ? 242 LEU A C 1 +ATOM 2032 O O . LEU A 1 242 ? 24.618 16.325 -6.735 1.00 17.96 ? 242 LEU A O 1 +ATOM 2033 C CB . LEU A 1 242 ? 21.514 16.262 -7.115 1.00 18.10 ? 242 LEU A CB 1 +ATOM 2034 C CG . LEU A 1 242 ? 20.945 15.279 -8.128 1.00 19.57 ? 242 LEU A CG 1 +ATOM 2035 C CD1 . LEU A 1 242 ? 19.885 14.396 -7.492 1.00 20.27 ? 242 LEU A CD1 1 +ATOM 2036 C CD2 . LEU A 1 242 ? 20.350 16.000 -9.280 1.00 19.83 ? 242 LEU A CD2 1 +ATOM 2037 N N . THR A 1 243 ? 24.131 14.138 -6.881 1.00 18.16 ? 243 THR A N 1 +ATOM 2038 C CA . THR A 1 243 ? 25.435 13.756 -7.399 1.00 18.67 ? 243 THR A CA 1 +ATOM 2039 C C . THR A 1 243 ? 25.333 13.318 -8.861 1.00 19.12 ? 243 THR A C 1 +ATOM 2040 O O . THR A 1 243 ? 24.223 13.074 -9.370 1.00 18.82 ? 243 THR A O 1 +ATOM 2041 C CB . THR A 1 243 ? 26.018 12.618 -6.543 1.00 19.51 ? 243 THR A CB 1 +ATOM 2042 O OG1 . THR A 1 243 ? 25.257 11.425 -6.756 1.00 19.15 ? 243 THR A OG1 1 +ATOM 2043 C CG2 . THR A 1 243 ? 26.099 12.973 -5.073 1.00 20.65 ? 243 THR A CG2 1 +ATOM 2044 N N . GLN A 1 244 ? 26.491 13.150 -9.526 1.00 19.36 ? 244 GLN A N 1 +ATOM 2045 C CA . GLN A 1 244 ? 26.496 12.626 -10.886 1.00 19.60 ? 244 GLN A CA 1 +ATOM 2046 C C . GLN A 1 244 ? 25.936 11.192 -10.896 1.00 19.31 ? 244 GLN A C 1 +ATOM 2047 O O . GLN A 1 244 ? 25.228 10.841 -11.832 1.00 19.52 ? 244 GLN A O 1 +ATOM 2048 C CB . GLN A 1 244 ? 27.908 12.662 -11.481 1.00 21.32 ? 244 GLN A CB 1 +ATOM 2049 C CG . GLN A 1 244 ? 27.948 12.291 -12.963 1.00 24.67 ? 244 GLN A CG 1 +ATOM 2050 C CD . GLN A 1 244 ? 27.099 13.215 -13.796 1.00 27.50 ? 244 GLN A CD 1 +ATOM 2051 O OE1 . GLN A 1 244 ? 27.194 14.445 -13.689 1.00 28.95 ? 244 GLN A OE1 1 +ATOM 2052 N NE2 . GLN A 1 244 ? 26.239 12.644 -14.629 1.00 26.25 ? 244 GLN A NE2 1 +ATOM 2053 N N . ASP A 1 245 ? 26.150 10.409 -9.818 1.00 18.53 ? 245 ASP A N 1 +ATOM 2054 C CA . ASP A 1 245 ? 25.574 9.066 -9.707 1.00 18.09 ? 245 ASP A CA 1 +ATOM 2055 C C . ASP A 1 245 ? 24.045 9.134 -9.768 1.00 16.92 ? 245 ASP A C 1 +ATOM 2056 O O . ASP A 1 245 ? 23.437 8.335 -10.466 1.00 17.01 ? 245 ASP A O 1 +ATOM 2057 C CB . ASP A 1 245 ? 26.001 8.387 -8.399 1.00 20.87 ? 245 ASP A CB 1 +ATOM 2058 C CG . ASP A 1 245 ? 27.274 7.574 -8.483 1.00 27.71 ? 245 ASP A CG 1 +ATOM 2059 O OD1 . ASP A 1 245 ? 28.003 7.709 -9.493 1.00 28.66 ? 245 ASP A OD1 1 +ATOM 2060 O OD2 . ASP A 1 245 ? 27.551 6.809 -7.530 1.00 30.69 ? 245 ASP A OD2 1 +ATOM 2061 N N . HIS A 1 246 ? 23.429 10.114 -9.083 1.00 15.98 ? 246 HIS A N 1 +ATOM 2062 C CA . HIS A 1 246 ? 21.969 10.269 -9.127 1.00 15.49 ? 246 HIS A CA 1 +ATOM 2063 C C . HIS A 1 246 ? 21.504 10.639 -10.533 1.00 15.40 ? 246 HIS A C 1 +ATOM 2064 O O . HIS A 1 246 ? 20.479 10.138 -10.994 1.00 15.05 ? 246 HIS A O 1 +ATOM 2065 C CB . HIS A 1 246 ? 21.508 11.368 -8.176 1.00 15.78 ? 246 HIS A CB 1 +ATOM 2066 C CG . HIS A 1 246 ? 21.770 11.078 -6.743 1.00 17.82 ? 246 HIS A CG 1 +ATOM 2067 N ND1 . HIS A 1 246 ? 22.203 12.070 -5.882 1.00 19.11 ? 246 HIS A ND1 1 +ATOM 2068 C CD2 . HIS A 1 246 ? 21.645 9.920 -6.061 1.00 19.14 ? 246 HIS A CD2 1 +ATOM 2069 C CE1 . HIS A 1 246 ? 22.337 11.483 -4.706 1.00 19.83 ? 246 HIS A CE1 1 +ATOM 2070 N NE2 . HIS A 1 246 ? 21.998 10.194 -4.760 1.00 20.16 ? 246 HIS A NE2 1 +ATOM 2071 N N . VAL A 1 247 ? 22.246 11.522 -11.204 1.00 15.42 ? 247 VAL A N 1 +ATOM 2072 C CA . VAL A 1 247 ? 21.930 11.926 -12.569 1.00 15.51 ? 247 VAL A CA 1 +ATOM 2073 C C . VAL A 1 247 ? 21.958 10.715 -13.495 1.00 16.08 ? 247 VAL A C 1 +ATOM 2074 O O . VAL A 1 247 ? 21.051 10.539 -14.308 1.00 16.35 ? 247 VAL A O 1 +ATOM 2075 C CB . VAL A 1 247 ? 22.896 13.023 -13.073 1.00 16.23 ? 247 VAL A CB 1 +ATOM 2076 C CG1 . VAL A 1 247 ? 22.681 13.298 -14.560 1.00 17.00 ? 247 VAL A CG1 1 +ATOM 2077 C CG2 . VAL A 1 247 ? 22.733 14.297 -12.255 1.00 17.00 ? 247 VAL A CG2 1 +ATOM 2078 N N . ASP A 1 248 ? 22.964 9.855 -13.327 1.00 16.47 ? 248 ASP A N 1 +ATOM 2079 C CA . ASP A 1 248 ? 23.084 8.653 -14.146 1.00 17.07 ? 248 ASP A CA 1 +ATOM 2080 C C . ASP A 1 248 ? 21.953 7.675 -13.877 1.00 17.14 ? 248 ASP A C 1 +ATOM 2081 O O . ASP A 1 248 ? 21.438 7.067 -14.812 1.00 17.79 ? 248 ASP A O 1 +ATOM 2082 C CB . ASP A 1 248 ? 24.433 7.972 -13.911 1.00 18.42 ? 248 ASP A CB 1 +ATOM 2083 C CG . ASP A 1 248 ? 25.621 8.798 -14.361 1.00 21.95 ? 248 ASP A CG 1 +ATOM 2084 O OD1 . ASP A 1 248 ? 25.426 9.733 -15.170 1.00 22.47 ? 248 ASP A OD1 1 +ATOM 2085 O OD2 . ASP A 1 248 ? 26.742 8.511 -13.904 1.00 24.76 ? 248 ASP A OD2 1 +ATOM 2086 N N . ILE A 1 249 ? 21.549 7.528 -12.614 1.00 16.87 ? 249 ILE A N 1 +ATOM 2087 C CA . ILE A 1 249 ? 20.432 6.648 -12.257 1.00 17.46 ? 249 ILE A CA 1 +ATOM 2088 C C . ILE A 1 249 ? 19.119 7.132 -12.904 1.00 16.76 ? 249 ILE A C 1 +ATOM 2089 O O . ILE A 1 249 ? 18.263 6.320 -13.253 1.00 17.06 ? 249 ILE A O 1 +ATOM 2090 C CB . ILE A 1 249 ? 20.323 6.530 -10.715 1.00 19.59 ? 249 ILE A CB 1 +ATOM 2091 C CG1 . ILE A 1 249 ? 21.526 5.765 -10.147 1.00 20.92 ? 249 ILE A CG1 1 +ATOM 2092 C CG2 . ILE A 1 249 ? 19.034 5.855 -10.297 1.00 21.07 ? 249 ILE A CG2 1 +ATOM 2093 C CD1 . ILE A 1 249 ? 21.709 5.942 -8.653 1.00 22.51 ? 249 ILE A CD1 1 +ATOM 2094 N N . LEU A 1 250 ? 18.972 8.455 -13.087 1.00 15.50 ? 250 LEU A N 1 +ATOM 2095 C CA . LEU A 1 250 ? 17.794 9.034 -13.730 1.00 15.60 ? 250 LEU A CA 1 +ATOM 2096 C C . LEU A 1 250 ? 17.834 8.995 -15.268 1.00 16.87 ? 250 LEU A C 1 +ATOM 2097 O O . LEU A 1 250 ? 16.844 9.354 -15.898 1.00 17.10 ? 250 LEU A O 1 +ATOM 2098 C CB . LEU A 1 250 ? 17.591 10.474 -13.267 1.00 14.27 ? 250 LEU A CB 1 +ATOM 2099 C CG . LEU A 1 250 ? 17.215 10.646 -11.808 1.00 14.27 ? 250 LEU A CG 1 +ATOM 2100 C CD1 . LEU A 1 250 ? 17.430 12.094 -11.372 1.00 14.67 ? 250 LEU A CD1 1 +ATOM 2101 C CD2 . LEU A 1 250 ? 15.762 10.236 -11.577 1.00 14.78 ? 250 LEU A CD2 1 +ATOM 2102 N N . GLY A 1 251 ? 18.940 8.525 -15.843 1.00 17.02 ? 251 GLY A N 1 +ATOM 2103 C CA . GLY A 1 251 ? 19.134 8.385 -17.284 1.00 18.15 ? 251 GLY A CA 1 +ATOM 2104 C C . GLY A 1 251 ? 17.975 7.739 -18.021 1.00 19.09 ? 251 GLY A C 1 +ATOM 2105 O O . GLY A 1 251 ? 17.410 8.357 -18.923 1.00 19.38 ? 251 GLY A O 1 +ATOM 2106 N N . PRO A 1 252 ? 17.540 6.528 -17.623 1.00 19.11 ? 252 PRO A N 1 +ATOM 2107 C CA . PRO A 1 252 ? 16.394 5.908 -18.309 1.00 19.24 ? 252 PRO A CA 1 +ATOM 2108 C C . PRO A 1 252 ? 15.110 6.745 -18.294 1.00 18.83 ? 252 PRO A C 1 +ATOM 2109 O O . PRO A 1 252 ? 14.431 6.798 -19.315 1.00 19.47 ? 252 PRO A O 1 +ATOM 2110 C CB . PRO A 1 252 ? 16.246 4.562 -17.589 1.00 20.19 ? 252 PRO A CB 1 +ATOM 2111 C CG . PRO A 1 252 ? 17.626 4.268 -17.093 1.00 20.99 ? 252 PRO A CG 1 +ATOM 2112 C CD . PRO A 1 252 ? 18.109 5.617 -16.617 1.00 19.33 ? 252 PRO A CD 1 +ATOM 2113 N N . LEU A 1 253 ? 14.785 7.429 -17.181 1.00 18.06 ? 253 LEU A N 1 +ATOM 2114 C CA . LEU A 1 253 ? 13.586 8.275 -17.140 1.00 17.83 ? 253 LEU A CA 1 +ATOM 2115 C C . LEU A 1 253 ? 13.741 9.519 -18.012 1.00 18.44 ? 253 LEU A C 1 +ATOM 2116 O O . LEU A 1 253 ? 12.785 9.977 -18.635 1.00 19.17 ? 253 LEU A O 1 +ATOM 2117 C CB . LEU A 1 253 ? 13.221 8.666 -15.706 1.00 17.36 ? 253 LEU A CB 1 +ATOM 2118 C CG . LEU A 1 253 ? 12.642 7.523 -14.882 1.00 18.39 ? 253 LEU A CG 1 +ATOM 2119 C CD1 . LEU A 1 253 ? 12.522 7.914 -13.415 1.00 18.47 ? 253 LEU A CD1 1 +ATOM 2120 C CD2 . LEU A 1 253 ? 11.285 7.102 -15.419 1.00 19.76 ? 253 LEU A CD2 1 +ATOM 2121 N N . SER A 1 254 ? 14.956 10.052 -18.077 1.00 18.35 ? 254 SER A N 1 +ATOM 2122 C CA . SER A 1 254 ? 15.269 11.190 -18.918 1.00 18.83 ? 254 SER A CA 1 +ATOM 2123 C C . SER A 1 254 ? 15.130 10.789 -20.399 1.00 19.74 ? 254 SER A C 1 +ATOM 2124 O O . SER A 1 254 ? 14.617 11.567 -21.210 1.00 20.29 ? 254 SER A O 1 +ATOM 2125 C CB . SER A 1 254 ? 16.703 11.640 -18.638 1.00 19.93 ? 254 SER A CB 1 +ATOM 2126 O OG . SER A 1 254 ? 17.063 12.706 -19.494 1.00 22.09 ? 254 SER A OG 1 +ATOM 2127 N N . ALA A 1 255 ? 15.585 9.585 -20.748 1.00 19.75 ? 255 ALA A N 1 +ATOM 2128 C CA . ALA A 1 255 ? 15.515 9.100 -22.123 1.00 20.73 ? 255 ALA A CA 1 +ATOM 2129 C C . ALA A 1 255 ? 14.080 8.868 -22.550 1.00 22.35 ? 255 ALA A C 1 +ATOM 2130 O O . ALA A 1 255 ? 13.724 9.175 -23.692 1.00 22.53 ? 255 ALA A O 1 +ATOM 2131 C CB . ALA A 1 255 ? 16.321 7.819 -22.267 1.00 20.66 ? 255 ALA A CB 1 +ATOM 2132 N N . GLN A 1 256 ? 13.260 8.330 -21.643 1.00 22.99 ? 256 GLN A N 1 +ATOM 2133 C CA . GLN A 1 256 ? 11.861 8.039 -21.931 1.00 24.03 ? 256 GLN A CA 1 +ATOM 2134 C C . GLN A 1 256 ? 11.033 9.298 -22.174 1.00 23.74 ? 256 GLN A C 1 +ATOM 2135 O O . GLN A 1 256 ? 10.254 9.350 -23.132 1.00 24.91 ? 256 GLN A O 1 +ATOM 2136 C CB . GLN A 1 256 ? 11.252 7.200 -20.805 1.00 26.63 ? 256 GLN A CB 1 +ATOM 2137 C CG . GLN A 1 256 ? 9.818 6.770 -21.073 1.00 31.24 ? 256 GLN A CG 1 +ATOM 2138 C CD . GLN A 1 256 ? 9.199 6.054 -19.898 1.00 36.62 ? 256 GLN A CD 1 +ATOM 2139 O OE1 . GLN A 1 256 ? 9.885 5.560 -18.983 1.00 38.38 ? 256 GLN A OE1 1 +ATOM 2140 N NE2 . GLN A 1 256 ? 7.876 5.983 -19.902 1.00 37.67 ? 256 GLN A NE2 1 +ATOM 2141 N N . THR A 1 257 ? 11.226 10.325 -21.350 1.00 21.63 ? 257 THR A N 1 +ATOM 2142 C CA . THR A 1 257 ? 10.447 11.552 -21.456 1.00 20.74 ? 257 THR A CA 1 +ATOM 2143 C C . THR A 1 257 ? 11.055 12.627 -22.354 1.00 20.66 ? 257 THR A C 1 +ATOM 2144 O O . THR A 1 257 ? 10.367 13.578 -22.708 1.00 21.25 ? 257 THR A O 1 +ATOM 2145 C CB . THR A 1 257 ? 10.244 12.132 -20.061 1.00 21.06 ? 257 THR A CB 1 +ATOM 2146 O OG1 . THR A 1 257 ? 11.535 12.470 -19.536 1.00 21.29 ? 257 THR A OG1 1 +ATOM 2147 C CG2 . THR A 1 257 ? 9.565 11.151 -19.127 1.00 21.27 ? 257 THR A CG2 1 +ATOM 2148 N N . GLY A 1 258 ? 12.336 12.508 -22.660 1.00 19.65 ? 258 GLY A N 1 +ATOM 2149 C CA . GLY A 1 258 ? 13.033 13.522 -23.440 1.00 19.47 ? 258 GLY A CA 1 +ATOM 2150 C C . GLY A 1 258 ? 13.360 14.765 -22.637 1.00 18.75 ? 258 GLY A C 1 +ATOM 2151 O O . GLY A 1 258 ? 13.782 15.770 -23.207 1.00 18.83 ? 258 GLY A O 1 +ATOM 2152 N N . ILE A 1 259 ? 13.206 14.712 -21.284 1.00 17.30 ? 259 ILE A N 1 +ATOM 2153 C CA . ILE A 1 259 ? 13.516 15.858 -20.450 1.00 17.01 ? 259 ILE A CA 1 +ATOM 2154 C C . ILE A 1 259 ? 14.840 15.605 -19.784 1.00 16.46 ? 259 ILE A C 1 +ATOM 2155 O O . ILE A 1 259 ? 14.980 14.653 -19.015 1.00 16.95 ? 259 ILE A O 1 +ATOM 2156 C CB . ILE A 1 259 ? 12.396 16.138 -19.416 1.00 18.00 ? 259 ILE A CB 1 +ATOM 2157 C CG1 . ILE A 1 259 ? 11.064 16.389 -20.148 1.00 19.63 ? 259 ILE A CG1 1 +ATOM 2158 C CG2 . ILE A 1 259 ? 12.766 17.336 -18.557 1.00 18.35 ? 259 ILE A CG2 1 +ATOM 2159 C CD1 . ILE A 1 259 ? 9.876 16.454 -19.229 1.00 21.54 ? 259 ILE A CD1 1 +ATOM 2160 N N . ALA A 1 260 ? 15.837 16.436 -20.095 1.00 15.60 ? 260 ALA A N 1 +ATOM 2161 C CA . ALA A 1 260 ? 17.170 16.324 -19.512 1.00 15.26 ? 260 ALA A CA 1 +ATOM 2162 C C . ALA A 1 260 ? 17.099 16.416 -17.996 1.00 14.60 ? 260 ALA A C 1 +ATOM 2163 O O . ALA A 1 260 ? 16.278 17.168 -17.463 1.00 14.60 ? 260 ALA A O 1 +ATOM 2164 C CB . ALA A 1 260 ? 18.067 17.431 -20.055 1.00 16.18 ? 260 ALA A CB 1 +ATOM 2165 N N . VAL A 1 261 ? 17.925 15.638 -17.296 1.00 13.65 ? 261 VAL A N 1 +ATOM 2166 C CA . VAL A 1 261 ? 17.923 15.636 -15.837 1.00 13.86 ? 261 VAL A CA 1 +ATOM 2167 C C . VAL A 1 261 ? 18.078 17.028 -15.244 1.00 13.55 ? 261 VAL A C 1 +ATOM 2168 O O . VAL A 1 261 ? 17.313 17.391 -14.351 1.00 14.19 ? 261 VAL A O 1 +ATOM 2169 C CB . VAL A 1 261 ? 18.954 14.647 -15.258 1.00 15.10 ? 261 VAL A CB 1 +ATOM 2170 C CG1 . VAL A 1 261 ? 19.013 14.754 -13.744 1.00 14.97 ? 261 VAL A CG1 1 +ATOM 2171 C CG2 . VAL A 1 261 ? 18.624 13.214 -15.680 1.00 16.65 ? 261 VAL A CG2 1 +ATOM 2172 N N . LEU A 1 262 ? 19.005 17.831 -15.794 1.00 13.28 ? 262 LEU A N 1 +ATOM 2173 C CA . LEU A 1 262 ? 19.208 19.180 -15.273 1.00 13.56 ? 262 LEU A CA 1 +ATOM 2174 C C . LEU A 1 262 ? 18.028 20.109 -15.552 1.00 13.51 ? 262 LEU A C 1 +ATOM 2175 O O . LEU A 1 262 ? 17.795 21.025 -14.755 1.00 13.73 ? 262 LEU A O 1 +ATOM 2176 C CB . LEU A 1 262 ? 20.526 19.768 -15.738 1.00 13.70 ? 262 LEU A CB 1 +ATOM 2177 C CG . LEU A 1 262 ? 21.765 19.061 -15.162 1.00 15.11 ? 262 LEU A CG 1 +ATOM 2178 C CD1 . LEU A 1 262 ? 23.038 19.609 -15.783 1.00 15.85 ? 262 LEU A CD1 1 +ATOM 2179 C CD2 . LEU A 1 262 ? 21.832 19.171 -13.652 1.00 15.29 ? 262 LEU A CD2 1 +ATOM 2180 N N . ASP A 1 263 ? 17.252 19.857 -16.630 1.00 13.50 ? 263 ASP A N 1 +ATOM 2181 C CA . ASP A 1 263 ? 16.044 20.647 -16.866 1.00 13.09 ? 263 ASP A CA 1 +ATOM 2182 C C . ASP A 1 263 ? 15.008 20.287 -15.786 1.00 14.28 ? 263 ASP A C 1 +ATOM 2183 O O . ASP A 1 263 ? 14.352 21.181 -15.249 1.00 15.00 ? 263 ASP A O 1 +ATOM 2184 C CB . ASP A 1 263 ? 15.460 20.397 -18.251 1.00 13.77 ? 263 ASP A CB 1 +ATOM 2185 C CG . ASP A 1 263 ? 16.333 20.842 -19.408 1.00 14.89 ? 263 ASP A CG 1 +ATOM 2186 O OD1 . ASP A 1 263 ? 17.440 21.396 -19.156 1.00 14.07 ? 263 ASP A OD1 1 +ATOM 2187 O OD2 . ASP A 1 263 ? 15.912 20.661 -20.549 1.00 16.19 ? 263 ASP A OD2 1 +ATOM 2188 N N . MET A 1 264 ? 14.883 18.991 -15.442 1.00 13.23 ? 264 MET A N 1 +ATOM 2189 C CA . MET A 1 264 ? 13.973 18.598 -14.358 1.00 12.75 ? 264 MET A CA 1 +ATOM 2190 C C . MET A 1 264 ? 14.443 19.193 -13.029 1.00 13.28 ? 264 MET A C 1 +ATOM 2191 O O . MET A 1 264 ? 13.626 19.638 -12.230 1.00 14.09 ? 264 MET A O 1 +ATOM 2192 C CB . MET A 1 264 ? 13.808 17.085 -14.252 1.00 13.83 ? 264 MET A CB 1 +ATOM 2193 C CG . MET A 1 264 ? 12.620 16.710 -13.385 1.00 14.70 ? 264 MET A CG 1 +ATOM 2194 S SD . MET A 1 264 ? 11.043 17.204 -14.145 1.00 16.49 ? 264 MET A SD 1 +ATOM 2195 C CE . MET A 1 264 ? 10.741 15.784 -15.174 1.00 18.99 ? 264 MET A CE 1 +ATOM 2196 N N . CYS A 1 265 ? 15.767 19.296 -12.823 1.00 12.88 ? 265 CYS A N 1 +ATOM 2197 C CA . CYS A 1 265 ? 16.310 19.936 -11.623 1.00 13.13 ? 265 CYS A CA 1 +ATOM 2198 C C . CYS A 1 265 ? 15.888 21.399 -11.572 1.00 13.37 ? 265 CYS A C 1 +ATOM 2199 O O . CYS A 1 265 ? 15.599 21.895 -10.489 1.00 13.84 ? 265 CYS A O 1 +ATOM 2200 C CB . CYS A 1 265 ? 17.828 19.815 -11.597 1.00 13.18 ? 265 CYS A CB 1 +ATOM 2201 S SG . CYS A 1 265 ? 18.430 18.150 -11.239 1.00 13.95 ? 265 CYS A SG 1 +ATOM 2202 N N . ALA A 1 266 ? 15.814 22.076 -12.734 1.00 13.18 ? 266 ALA A N 1 +ATOM 2203 C CA . ALA A 1 266 ? 15.388 23.477 -12.773 1.00 14.34 ? 266 ALA A CA 1 +ATOM 2204 C C . ALA A 1 266 ? 13.907 23.600 -12.453 1.00 15.13 ? 266 ALA A C 1 +ATOM 2205 O O . ALA A 1 266 ? 13.510 24.582 -11.826 1.00 16.07 ? 266 ALA A O 1 +ATOM 2206 C CB . ALA A 1 266 ? 15.692 24.101 -14.119 1.00 15.34 ? 266 ALA A CB 1 +ATOM 2207 N N . SER A 1 267 ? 13.093 22.600 -12.841 1.00 14.73 ? 267 SER A N 1 +ATOM 2208 C CA . SER A 1 267 ? 11.680 22.574 -12.475 1.00 15.16 ? 267 SER A CA 1 +ATOM 2209 C C . SER A 1 267 ? 11.573 22.402 -10.957 1.00 14.35 ? 267 SER A C 1 +ATOM 2210 O O . SER A 1 267 ? 10.788 23.086 -10.302 1.00 14.65 ? 267 SER A O 1 +ATOM 2211 C CB . SER A 1 267 ? 10.953 21.421 -13.163 1.00 17.63 ? 267 SER A CB 1 +ATOM 2212 O OG . SER A 1 267 ? 10.610 21.744 -14.499 1.00 21.64 ? 267 SER A OG 1 +ATOM 2213 N N . LEU A 1 268 ? 12.371 21.488 -10.401 1.00 13.19 ? 268 LEU A N 1 +ATOM 2214 C CA . LEU A 1 268 ? 12.359 21.248 -8.965 1.00 13.02 ? 268 LEU A CA 1 +ATOM 2215 C C . LEU A 1 268 ? 12.836 22.482 -8.205 1.00 13.76 ? 268 LEU A C 1 +ATOM 2216 O O . LEU A 1 268 ? 12.237 22.854 -7.203 1.00 13.46 ? 268 LEU A O 1 +ATOM 2217 C CB . LEU A 1 268 ? 13.191 20.007 -8.611 1.00 12.54 ? 268 LEU A CB 1 +ATOM 2218 C CG . LEU A 1 268 ? 13.338 19.701 -7.124 1.00 13.38 ? 268 LEU A CG 1 +ATOM 2219 C CD1 . LEU A 1 268 ? 11.961 19.546 -6.450 1.00 14.09 ? 268 LEU A CD1 1 +ATOM 2220 C CD2 . LEU A 1 268 ? 14.098 18.421 -6.934 1.00 13.76 ? 268 LEU A CD2 1 +ATOM 2221 N N . LYS A 1 269 ? 13.869 23.160 -8.705 1.00 12.82 ? 269 LYS A N 1 +ATOM 2222 C CA . LYS A 1 269 ? 14.363 24.389 -8.097 1.00 12.60 ? 269 LYS A CA 1 +ATOM 2223 C C . LYS A 1 269 ? 13.255 25.446 -8.026 1.00 13.34 ? 269 LYS A C 1 +ATOM 2224 O O . LYS A 1 269 ? 13.062 26.038 -6.976 1.00 13.99 ? 269 LYS A O 1 +ATOM 2225 C CB . LYS A 1 269 ? 15.546 24.917 -8.911 1.00 13.63 ? 269 LYS A CB 1 +ATOM 2226 C CG . LYS A 1 269 ? 16.062 26.292 -8.492 1.00 17.21 ? 269 LYS A CG 1 +ATOM 2227 C CD . LYS A 1 269 ? 17.254 26.664 -9.357 1.00 20.23 ? 269 LYS A CD 1 +ATOM 2228 C CE . LYS A 1 269 ? 17.557 28.150 -9.315 1.00 23.68 ? 269 LYS A CE 1 +ATOM 2229 N NZ . LYS A 1 269 ? 18.553 28.518 -10.362 1.00 25.16 ? 269 LYS A NZ 1 +ATOM 2230 N N . GLU A 1 270 ? 12.479 25.616 -9.107 1.00 13.60 ? 270 GLU A N 1 +ATOM 2231 C CA . GLU A 1 270 ? 11.380 26.581 -9.098 1.00 14.67 ? 270 GLU A CA 1 +ATOM 2232 C C . GLU A 1 270 ? 10.288 26.174 -8.115 1.00 15.62 ? 270 GLU A C 1 +ATOM 2233 O O . GLU A 1 270 ? 9.749 27.026 -7.415 1.00 16.25 ? 270 GLU A O 1 +ATOM 2234 C CB . GLU A 1 270 ? 10.813 26.806 -10.505 1.00 17.51 ? 270 GLU A CB 1 +ATOM 2235 C CG . GLU A 1 270 ? 11.804 27.456 -11.453 1.00 24.81 ? 270 GLU A CG 1 +ATOM 2236 C CD . GLU A 1 270 ? 12.368 28.793 -11.016 1.00 32.43 ? 270 GLU A CD 1 +ATOM 2237 O OE1 . GLU A 1 270 ? 11.568 29.730 -10.794 1.00 33.99 ? 270 GLU A OE1 1 +ATOM 2238 O OE2 . GLU A 1 270 ? 13.611 28.907 -10.900 1.00 33.71 ? 270 GLU A OE2 1 +ATOM 2239 N N . LEU A 1 271 ? 9.974 24.877 -8.043 1.00 15.19 ? 271 LEU A N 1 +ATOM 2240 C CA . LEU A 1 271 ? 8.984 24.384 -7.082 1.00 15.27 ? 271 LEU A CA 1 +ATOM 2241 C C . LEU A 1 271 ? 9.434 24.628 -5.646 1.00 15.62 ? 271 LEU A C 1 +ATOM 2242 O O . LEU A 1 271 ? 8.598 24.933 -4.792 1.00 17.11 ? 271 LEU A O 1 +ATOM 2243 C CB . LEU A 1 271 ? 8.749 22.894 -7.289 1.00 15.27 ? 271 LEU A CB 1 +ATOM 2244 C CG . LEU A 1 271 ? 7.915 22.555 -8.510 1.00 16.49 ? 271 LEU A CG 1 +ATOM 2245 C CD1 . LEU A 1 271 ? 7.962 21.084 -8.777 1.00 16.95 ? 271 LEU A CD1 1 +ATOM 2246 C CD2 . LEU A 1 271 ? 6.477 23.030 -8.321 1.00 17.56 ? 271 LEU A CD2 1 +ATOM 2247 N N . LEU A 1 272 ? 10.737 24.490 -5.367 1.00 14.10 ? 272 LEU A N 1 +ATOM 2248 C CA . LEU A 1 272 ? 11.233 24.723 -4.011 1.00 14.76 ? 272 LEU A CA 1 +ATOM 2249 C C . LEU A 1 272 ? 11.164 26.195 -3.655 1.00 16.26 ? 272 LEU A C 1 +ATOM 2250 O O . LEU A 1 272 ? 10.760 26.536 -2.543 1.00 17.01 ? 272 LEU A O 1 +ATOM 2251 C CB . LEU A 1 272 ? 12.669 24.214 -3.869 1.00 14.74 ? 272 LEU A CB 1 +ATOM 2252 C CG . LEU A 1 272 ? 12.797 22.705 -3.843 1.00 16.78 ? 272 LEU A CG 1 +ATOM 2253 C CD1 . LEU A 1 272 ? 14.257 22.274 -3.868 1.00 17.63 ? 272 LEU A CD1 1 +ATOM 2254 C CD2 . LEU A 1 272 ? 12.062 22.119 -2.657 1.00 18.76 ? 272 LEU A CD2 1 +ATOM 2255 N N . GLN A 1 273 ? 11.531 27.061 -4.599 1.00 16.06 ? 273 GLN A N 1 +ATOM 2256 C CA . GLN A 1 273 ? 11.587 28.499 -4.374 1.00 17.33 ? 273 GLN A CA 1 +ATOM 2257 C C . GLN A 1 273 ? 10.240 29.180 -4.375 1.00 19.69 ? 273 GLN A C 1 +ATOM 2258 O O . GLN A 1 273 ? 10.080 30.197 -3.708 1.00 20.97 ? 273 GLN A O 1 +ATOM 2259 C CB . GLN A 1 273 ? 12.515 29.162 -5.409 1.00 17.71 ? 273 GLN A CB 1 +ATOM 2260 C CG . GLN A 1 273 ? 13.968 28.758 -5.252 1.00 19.36 ? 273 GLN A CG 1 +ATOM 2261 C CD . GLN A 1 273 ? 14.860 29.396 -6.286 1.00 22.80 ? 273 GLN A CD 1 +ATOM 2262 O OE1 . GLN A 1 273 ? 14.437 29.745 -7.391 1.00 24.43 ? 273 GLN A OE1 1 +ATOM 2263 N NE2 . GLN A 1 273 ? 16.125 29.546 -5.950 1.00 23.28 ? 273 GLN A NE2 1 +ATOM 2264 N N . ASN A 1 274 ? 9.280 28.656 -5.133 1.00 20.29 ? 274 ASN A N 1 +ATOM 2265 C CA . ASN A 1 274 ? 7.976 29.304 -5.249 1.00 21.83 ? 274 ASN A CA 1 +ATOM 2266 C C . ASN A 1 274 ? 6.801 28.527 -4.690 1.00 22.69 ? 274 ASN A C 1 +ATOM 2267 O O . ASN A 1 274 ? 5.697 29.063 -4.637 1.00 23.59 ? 274 ASN A O 1 +ATOM 2268 C CB . ASN A 1 274 ? 7.716 29.658 -6.695 1.00 23.76 ? 274 ASN A CB 1 +ATOM 2269 C CG . ASN A 1 274 ? 8.780 30.577 -7.217 1.00 29.54 ? 274 ASN A CG 1 +ATOM 2270 O OD1 . ASN A 1 274 ? 8.793 31.778 -6.927 1.00 32.28 ? 274 ASN A OD1 1 +ATOM 2271 N ND2 . ASN A 1 274 ? 9.721 30.023 -7.954 1.00 30.78 ? 274 ASN A ND2 1 +ATOM 2272 N N . GLY A 1 275 ? 7.023 27.287 -4.285 1.00 22.59 ? 275 GLY A N 1 +ATOM 2273 C CA . GLY A 1 275 ? 5.948 26.444 -3.791 1.00 22.92 ? 275 GLY A CA 1 +ATOM 2274 C C . GLY A 1 275 ? 5.080 25.943 -4.929 1.00 23.41 ? 275 GLY A C 1 +ATOM 2275 O O . GLY A 1 275 ? 5.379 26.177 -6.111 1.00 23.66 ? 275 GLY A O 1 +ATOM 2276 N N A MET A 1 276 ? 3.995 25.255 -4.586 0.75 23.76 ? 276 MET A N 1 +ATOM 2277 N N B MET A 1 276 ? 3.999 25.241 -4.587 0.25 23.17 ? 276 MET A N 1 +ATOM 2278 C CA A MET A 1 276 ? 3.106 24.713 -5.607 0.75 24.64 ? 276 MET A CA 1 +ATOM 2279 C CA B MET A 1 276 ? 3.087 24.717 -5.599 0.25 23.44 ? 276 MET A CA 1 +ATOM 2280 C C A MET A 1 276 ? 1.887 25.618 -5.902 0.75 25.05 ? 276 MET A C 1 +ATOM 2281 C C B MET A 1 276 ? 1.968 25.686 -5.984 0.25 24.43 ? 276 MET A C 1 +ATOM 2282 O O A MET A 1 276 ? 1.113 25.299 -6.801 0.75 25.20 ? 276 MET A O 1 +ATOM 2283 O O B MET A 1 276 ? 1.294 25.437 -6.974 0.25 24.50 ? 276 MET A O 1 +ATOM 2284 C CB A MET A 1 276 ? 2.723 23.269 -5.272 0.75 25.92 ? 276 MET A CB 1 +ATOM 2285 C CB B MET A 1 276 ? 2.506 23.358 -5.181 0.25 23.19 ? 276 MET A CB 1 +ATOM 2286 C CG A MET A 1 276 ? 3.943 22.341 -5.362 0.75 28.07 ? 276 MET A CG 1 +ATOM 2287 C CG B MET A 1 276 ? 3.463 22.203 -5.391 0.25 23.17 ? 276 MET A CG 1 +ATOM 2288 S SD A MET A 1 276 ? 3.789 20.735 -4.570 0.75 35.78 ? 276 MET A SD 1 +ATOM 2289 S SD B MET A 1 276 ? 2.590 20.634 -5.587 0.25 19.97 ? 276 MET A SD 1 +ATOM 2290 C CE A MET A 1 276 ? 2.500 20.047 -5.545 0.75 30.19 ? 276 MET A CE 1 +ATOM 2291 C CE B MET A 1 276 ? 3.918 19.512 -5.312 0.25 18.54 ? 276 MET A CE 1 +ATOM 2292 N N . ASN A 1 277 ? 1.774 26.783 -5.227 1.00 24.94 ? 277 ASN A N 1 +ATOM 2293 C CA . ASN A 1 277 ? 0.711 27.772 -5.473 1.00 25.60 ? 277 ASN A CA 1 +ATOM 2294 C C . ASN A 1 277 ? -0.709 27.189 -5.412 1.00 25.41 ? 277 ASN A C 1 +ATOM 2295 O O . ASN A 1 277 ? -1.567 27.570 -6.209 1.00 26.11 ? 277 ASN A O 1 +ATOM 2296 C CB . ASN A 1 277 ? 0.942 28.527 -6.787 1.00 27.55 ? 277 ASN A CB 1 +ATOM 2297 C CG . ASN A 1 277 ? 2.030 29.565 -6.712 1.00 32.36 ? 277 ASN A CG 1 +ATOM 2298 O OD1 . ASN A 1 277 ? 3.087 29.452 -7.353 1.00 34.44 ? 277 ASN A OD1 1 +ATOM 2299 N ND2 . ASN A 1 277 ? 1.795 30.607 -5.933 1.00 32.85 ? 277 ASN A ND2 1 +ATOM 2300 N N . GLY A 1 278 ? -0.939 26.258 -4.495 1.00 24.04 ? 278 GLY A N 1 +ATOM 2301 C CA . GLY A 1 278 ? -2.250 25.630 -4.362 1.00 23.26 ? 278 GLY A CA 1 +ATOM 2302 C C . GLY A 1 278 ? -2.558 24.555 -5.391 1.00 22.48 ? 278 GLY A C 1 +ATOM 2303 O O . GLY A 1 278 ? -3.689 24.070 -5.468 1.00 22.88 ? 278 GLY A O 1 +ATOM 2304 N N A ARG A 1 279 ? -1.553 24.151 -6.167 0.50 21.95 ? 279 ARG A N 1 +ATOM 2305 N N B ARG A 1 279 ? -1.550 24.164 -6.183 0.50 21.71 ? 279 ARG A N 1 +ATOM 2306 C CA A ARG A 1 279 ? -1.722 23.116 -7.173 0.50 21.79 ? 279 ARG A CA 1 +ATOM 2307 C CA B ARG A 1 279 ? -1.691 23.135 -7.207 0.50 21.30 ? 279 ARG A CA 1 +ATOM 2308 C C A ARG A 1 279 ? -1.216 21.759 -6.668 0.50 21.02 ? 279 ARG A C 1 +ATOM 2309 C C B ARG A 1 279 ? -1.203 21.769 -6.683 0.50 20.81 ? 279 ARG A C 1 +ATOM 2310 O O A ARG A 1 279 ? -0.595 21.677 -5.602 0.50 20.83 ? 279 ARG A O 1 +ATOM 2311 O O B ARG A 1 279 ? -0.560 21.694 -5.629 0.50 20.66 ? 279 ARG A O 1 +ATOM 2312 C CB A ARG A 1 279 ? -1.035 23.533 -8.485 0.50 23.35 ? 279 ARG A CB 1 +ATOM 2313 C CB B ARG A 1 279 ? -0.911 23.540 -8.475 0.50 22.14 ? 279 ARG A CB 1 +ATOM 2314 C CG A ARG A 1 279 ? -1.623 24.814 -9.067 0.50 27.22 ? 279 ARG A CG 1 +ATOM 2315 C CG B ARG A 1 279 ? -1.238 24.939 -9.002 0.50 24.89 ? 279 ARG A CG 1 +ATOM 2316 C CD A ARG A 1 279 ? -1.199 25.050 -10.505 0.50 31.04 ? 279 ARG A CD 1 +ATOM 2317 C CD B ARG A 1 279 ? -0.110 25.483 -9.868 0.50 27.42 ? 279 ARG A CD 1 +ATOM 2318 N NE A ARG A 1 279 ? -1.606 23.954 -11.383 0.50 34.59 ? 279 ARG A NE 1 +ATOM 2319 N NE B ARG A 1 279 ? -0.302 26.894 -10.206 0.50 30.09 ? 279 ARG A NE 1 +ATOM 2320 C CZ A ARG A 1 279 ? -2.790 23.867 -11.981 0.50 37.85 ? 279 ARG A CZ 1 +ATOM 2321 C CZ B ARG A 1 279 ? 0.680 27.785 -10.306 0.50 31.90 ? 279 ARG A CZ 1 +ATOM 2322 N NH1 A ARG A 1 279 ? -3.697 24.824 -11.819 0.50 37.97 ? 279 ARG A NH1 1 +ATOM 2323 N NH1 B ARG A 1 279 ? 1.940 27.424 -10.088 0.50 31.04 ? 279 ARG A NH1 1 +ATOM 2324 N NH2 A ARG A 1 279 ? -3.068 22.834 -12.764 0.50 38.37 ? 279 ARG A NH2 1 +ATOM 2325 N NH2 B ARG A 1 279 ? 0.413 29.041 -10.636 0.50 31.90 ? 279 ARG A NH2 1 +ATOM 2326 N N . THR A 1 280 ? -1.531 20.684 -7.398 1.00 20.29 ? 280 THR A N 1 +ATOM 2327 C CA . THR A 1 280 ? -1.107 19.344 -7.010 1.00 19.70 ? 280 THR A CA 1 +ATOM 2328 C C . THR A 1 280 ? -0.346 18.658 -8.148 1.00 18.60 ? 280 THR A C 1 +ATOM 2329 O O . THR A 1 280 ? -0.473 19.032 -9.320 1.00 18.37 ? 280 THR A O 1 +ATOM 2330 C CB . THR A 1 280 ? -2.305 18.475 -6.574 1.00 21.75 ? 280 THR A CB 1 +ATOM 2331 O OG1 . THR A 1 280 ? -3.207 18.341 -7.675 1.00 22.42 ? 280 THR A OG1 1 +ATOM 2332 C CG2 . THR A 1 280 ? -3.016 19.017 -5.348 1.00 22.81 ? 280 THR A CG2 1 +ATOM 2333 N N . ILE A 1 281 ? 0.475 17.669 -7.786 1.00 17.32 ? 281 ILE A N 1 +ATOM 2334 C CA . ILE A 1 281 ? 1.241 16.844 -8.713 1.00 17.17 ? 281 ILE A CA 1 +ATOM 2335 C C . ILE A 1 281 ? 0.971 15.413 -8.307 1.00 17.06 ? 281 ILE A C 1 +ATOM 2336 O O . ILE A 1 281 ? 1.194 15.057 -7.152 1.00 16.72 ? 281 ILE A O 1 +ATOM 2337 C CB . ILE A 1 281 ? 2.749 17.150 -8.631 1.00 17.81 ? 281 ILE A CB 1 +ATOM 2338 C CG1 . ILE A 1 281 ? 3.047 18.602 -9.014 1.00 18.05 ? 281 ILE A CG1 1 +ATOM 2339 C CG2 . ILE A 1 281 ? 3.527 16.160 -9.502 1.00 18.38 ? 281 ILE A CG2 1 +ATOM 2340 C CD1 . ILE A 1 281 ? 4.518 19.020 -8.861 1.00 18.34 ? 281 ILE A CD1 1 +ATOM 2341 N N . LEU A 1 282 ? 0.390 14.603 -9.206 1.00 17.24 ? 282 LEU A N 1 +ATOM 2342 C CA . LEU A 1 282 ? 0.041 13.212 -8.889 1.00 17.35 ? 282 LEU A CA 1 +ATOM 2343 C C . LEU A 1 282 ? -0.763 13.066 -7.587 1.00 18.42 ? 282 LEU A C 1 +ATOM 2344 O O . LEU A 1 282 ? -0.449 12.228 -6.754 1.00 19.49 ? 282 LEU A O 1 +ATOM 2345 C CB . LEU A 1 282 ? 1.267 12.292 -8.890 1.00 16.82 ? 282 LEU A CB 1 +ATOM 2346 C CG . LEU A 1 282 ? 1.936 12.047 -10.240 1.00 17.52 ? 282 LEU A CG 1 +ATOM 2347 C CD1 . LEU A 1 282 ? 3.136 11.159 -10.080 1.00 17.37 ? 282 LEU A CD1 1 +ATOM 2348 C CD2 . LEU A 1 282 ? 0.969 11.447 -11.235 1.00 18.50 ? 282 LEU A CD2 1 +ATOM 2349 N N . GLY A 1 283 ? -1.725 13.970 -7.411 1.00 19.57 ? 283 GLY A N 1 +ATOM 2350 C CA . GLY A 1 283 ? -2.606 13.998 -6.248 1.00 20.20 ? 283 GLY A CA 1 +ATOM 2351 C C . GLY A 1 283 ? -1.975 14.425 -4.940 1.00 20.33 ? 283 GLY A C 1 +ATOM 2352 O O . GLY A 1 283 ? -2.567 14.232 -3.877 1.00 21.64 ? 283 GLY A O 1 +ATOM 2353 N N A SER A 1 284 ? -0.758 14.973 -4.996 0.75 19.07 ? 284 SER A N 1 +ATOM 2354 N N B SER A 1 284 ? -0.757 14.979 -4.998 0.25 19.33 ? 284 SER A N 1 +ATOM 2355 C CA A SER A 1 284 ? -0.061 15.413 -3.798 0.75 18.29 ? 284 SER A CA 1 +ATOM 2356 C CA B SER A 1 284 ? -0.033 15.409 -3.809 0.25 18.82 ? 284 SER A CA 1 +ATOM 2357 C C A SER A 1 284 ? 0.123 16.915 -3.823 0.75 18.11 ? 284 SER A C 1 +ATOM 2358 C C B SER A 1 284 ? 0.197 16.911 -3.813 0.25 18.48 ? 284 SER A C 1 +ATOM 2359 O O A SER A 1 284 ? 0.390 17.488 -4.872 0.75 17.64 ? 284 SER A O 1 +ATOM 2360 O O B SER A 1 284 ? 0.554 17.481 -4.841 0.25 18.38 ? 284 SER A O 1 +ATOM 2361 C CB A SER A 1 284 ? 1.311 14.752 -3.713 0.75 18.83 ? 284 SER A CB 1 +ATOM 2362 C CB B SER A 1 284 ? 1.319 14.705 -3.725 0.25 19.61 ? 284 SER A CB 1 +ATOM 2363 O OG A SER A 1 284 ? 2.022 15.192 -2.566 0.75 20.77 ? 284 SER A OG 1 +ATOM 2364 O OG B SER A 1 284 ? 1.181 13.310 -3.519 0.25 21.27 ? 284 SER A OG 1 +ATOM 2365 N N . ALA A 1 285 ? 0.040 17.547 -2.650 1.00 18.03 ? 285 ALA A N 1 +ATOM 2366 C CA . ALA A 1 285 ? 0.290 18.982 -2.522 1.00 18.74 ? 285 ALA A CA 1 +ATOM 2367 C C . ALA A 1 285 ? 1.728 19.259 -1.985 1.00 18.86 ? 285 ALA A C 1 +ATOM 2368 O O . ALA A 1 285 ? 2.067 20.400 -1.676 1.00 20.19 ? 285 ALA A O 1 +ATOM 2369 C CB . ALA A 1 285 ? -0.755 19.620 -1.623 1.00 19.27 ? 285 ALA A CB 1 +ATOM 2370 N N . LEU A 1 286 ? 2.561 18.233 -1.874 1.00 17.88 ? 286 LEU A N 1 +ATOM 2371 C CA . LEU A 1 286 ? 3.951 18.373 -1.497 1.00 18.08 ? 286 LEU A CA 1 +ATOM 2372 C C . LEU A 1 286 ? 4.832 17.526 -2.431 1.00 17.12 ? 286 LEU A C 1 +ATOM 2373 O O . LEU A 1 286 ? 4.316 16.735 -3.234 1.00 17.43 ? 286 LEU A O 1 +ATOM 2374 C CB . LEU A 1 286 ? 4.191 18.099 -0.005 1.00 19.14 ? 286 LEU A CB 1 +ATOM 2375 C CG . LEU A 1 286 ? 3.662 16.806 0.562 1.00 21.28 ? 286 LEU A CG 1 +ATOM 2376 C CD1 . LEU A 1 286 ? 4.491 15.630 0.105 1.00 22.70 ? 286 LEU A CD1 1 +ATOM 2377 C CD2 . LEU A 1 286 ? 3.721 16.839 2.088 1.00 22.17 ? 286 LEU A CD2 1 +ATOM 2378 N N . LEU A 1 287 ? 6.135 17.757 -2.402 1.00 15.55 ? 287 LEU A N 1 +ATOM 2379 C CA . LEU A 1 287 ? 7.059 17.031 -3.258 1.00 15.39 ? 287 LEU A CA 1 +ATOM 2380 C C . LEU A 1 287 ? 7.339 15.664 -2.641 1.00 15.22 ? 287 LEU A C 1 +ATOM 2381 O O . LEU A 1 287 ? 7.958 15.571 -1.591 1.00 16.81 ? 287 LEU A O 1 +ATOM 2382 C CB . LEU A 1 287 ? 8.323 17.863 -3.459 1.00 16.06 ? 287 LEU A CB 1 +ATOM 2383 C CG . LEU A 1 287 ? 8.026 19.223 -4.104 1.00 18.18 ? 287 LEU A CG 1 +ATOM 2384 C CD1 . LEU A 1 287 ? 9.204 20.138 -3.991 1.00 18.93 ? 287 LEU A CD1 1 +ATOM 2385 C CD2 . LEU A 1 287 ? 7.575 19.068 -5.566 1.00 19.33 ? 287 LEU A CD2 1 +ATOM 2386 N N A GLU A 1 288 ? 6.855 14.602 -3.286 0.50 13.98 ? 288 GLU A N 1 +ATOM 2387 N N B GLU A 1 288 ? 6.866 14.610 -3.293 0.50 14.00 ? 288 GLU A N 1 +ATOM 2388 C CA A GLU A 1 288 ? 6.993 13.231 -2.776 0.50 13.48 ? 288 GLU A CA 1 +ATOM 2389 C CA B GLU A 1 288 ? 6.991 13.233 -2.807 0.50 13.54 ? 288 GLU A CA 1 +ATOM 2390 C C A GLU A 1 288 ? 8.376 12.638 -2.986 0.50 13.16 ? 288 GLU A C 1 +ATOM 2391 C C B GLU A 1 288 ? 8.390 12.654 -2.992 0.50 13.22 ? 288 GLU A C 1 +ATOM 2392 O O A GLU A 1 288 ? 8.883 12.653 -4.105 0.50 13.26 ? 288 GLU A O 1 +ATOM 2393 O O B GLU A 1 288 ? 8.917 12.689 -4.102 0.50 13.37 ? 288 GLU A O 1 +ATOM 2394 C CB A GLU A 1 288 ? 5.916 12.318 -3.382 0.50 14.44 ? 288 GLU A CB 1 +ATOM 2395 C CB B GLU A 1 288 ? 5.938 12.358 -3.504 0.50 14.59 ? 288 GLU A CB 1 +ATOM 2396 C CG A GLU A 1 288 ? 4.495 12.789 -3.115 0.50 16.46 ? 288 GLU A CG 1 +ATOM 2397 C CG B GLU A 1 288 ? 6.026 10.881 -3.187 0.50 16.96 ? 288 GLU A CG 1 +ATOM 2398 C CD A GLU A 1 288 ? 3.946 12.471 -1.736 0.50 20.85 ? 288 GLU A CD 1 +ATOM 2399 C CD B GLU A 1 288 ? 5.638 10.508 -1.773 0.50 19.50 ? 288 GLU A CD 1 +ATOM 2400 O OE1 A GLU A 1 288 ? 4.624 11.747 -0.972 0.50 22.15 ? 288 GLU A OE1 1 +ATOM 2401 O OE1 B GLU A 1 288 ? 6.458 9.855 -1.089 0.50 16.00 ? 288 GLU A OE1 1 +ATOM 2402 O OE2 A GLU A 1 288 ? 2.824 12.931 -1.426 0.50 21.03 ? 288 GLU A OE2 1 +ATOM 2403 O OE2 B GLU A 1 288 ? 4.514 10.867 -1.350 0.50 22.07 ? 288 GLU A OE2 1 +ATOM 2404 N N . ASP A 1 289 ? 8.971 12.078 -1.927 1.00 12.93 ? 289 ASP A N 1 +ATOM 2405 C CA . ASP A 1 289 ? 10.310 11.516 -2.024 1.00 12.60 ? 289 ASP A CA 1 +ATOM 2406 C C . ASP A 1 289 ? 10.423 10.047 -1.666 1.00 13.43 ? 289 ASP A C 1 +ATOM 2407 O O . ASP A 1 289 ? 11.543 9.594 -1.414 1.00 13.88 ? 289 ASP A O 1 +ATOM 2408 C CB . ASP A 1 289 ? 11.323 12.330 -1.215 1.00 12.56 ? 289 ASP A CB 1 +ATOM 2409 C CG . ASP A 1 289 ? 11.288 12.143 0.274 1.00 14.92 ? 289 ASP A CG 1 +ATOM 2410 O OD1 . ASP A 1 289 ? 10.301 11.554 0.778 1.00 14.82 ? 289 ASP A OD1 1 +ATOM 2411 O OD2 . ASP A 1 289 ? 12.243 12.583 0.934 1.00 15.48 ? 289 ASP A OD2 1 +ATOM 2412 N N . GLU A 1 290 ? 9.296 9.306 -1.633 1.00 13.33 ? 290 GLU A N 1 +ATOM 2413 C CA . GLU A 1 290 ? 9.409 7.892 -1.299 1.00 13.90 ? 290 GLU A CA 1 +ATOM 2414 C C . GLU A 1 290 ? 9.082 6.995 -2.504 1.00 14.27 ? 290 GLU A C 1 +ATOM 2415 O O . GLU A 1 290 ? 8.544 5.902 -2.363 1.00 14.58 ? 290 GLU A O 1 +ATOM 2416 C CB . GLU A 1 290 ? 8.658 7.524 -0.006 1.00 14.67 ? 290 GLU A CB 1 +ATOM 2417 C CG . GLU A 1 290 ? 9.218 8.275 1.202 1.00 16.76 ? 290 GLU A CG 1 +ATOM 2418 C CD . GLU A 1 290 ? 8.875 7.717 2.576 1.00 18.56 ? 290 GLU A CD 1 +ATOM 2419 O OE1 . GLU A 1 290 ? 7.986 6.840 2.655 1.00 16.60 ? 290 GLU A OE1 1 +ATOM 2420 O OE2 . GLU A 1 290 ? 9.511 8.133 3.572 1.00 19.92 ? 290 GLU A OE2 1 +ATOM 2421 N N . PHE A 1 291 ? 9.510 7.433 -3.696 1.00 13.63 ? 291 PHE A N 1 +ATOM 2422 C CA . PHE A 1 291 ? 9.546 6.589 -4.879 1.00 14.24 ? 291 PHE A CA 1 +ATOM 2423 C C . PHE A 1 291 ? 10.925 6.730 -5.436 1.00 14.69 ? 291 PHE A C 1 +ATOM 2424 O O . PHE A 1 291 ? 11.307 7.844 -5.781 1.00 15.37 ? 291 PHE A O 1 +ATOM 2425 C CB . PHE A 1 291 ? 8.614 7.038 -5.997 1.00 14.36 ? 291 PHE A CB 1 +ATOM 2426 C CG . PHE A 1 291 ? 7.153 6.969 -5.703 1.00 15.75 ? 291 PHE A CG 1 +ATOM 2427 C CD1 . PHE A 1 291 ? 6.458 5.787 -5.858 1.00 16.87 ? 291 PHE A CD1 1 +ATOM 2428 C CD2 . PHE A 1 291 ? 6.457 8.100 -5.333 1.00 17.27 ? 291 PHE A CD2 1 +ATOM 2429 C CE1 . PHE A 1 291 ? 5.089 5.746 -5.646 1.00 18.29 ? 291 PHE A CE1 1 +ATOM 2430 C CE2 . PHE A 1 291 ? 5.090 8.060 -5.145 1.00 18.48 ? 291 PHE A CE2 1 +ATOM 2431 C CZ . PHE A 1 291 ? 4.414 6.885 -5.307 1.00 18.11 ? 291 PHE A CZ 1 +ATOM 2432 N N . THR A 1 292 ? 11.657 5.637 -5.560 1.00 14.58 ? 292 THR A N 1 +ATOM 2433 C CA . THR A 1 292 ? 12.980 5.663 -6.157 1.00 14.64 ? 292 THR A CA 1 +ATOM 2434 C C . THR A 1 292 ? 12.849 5.681 -7.683 1.00 14.39 ? 292 THR A C 1 +ATOM 2435 O O . THR A 1 292 ? 11.814 5.278 -8.228 1.00 14.19 ? 292 THR A O 1 +ATOM 2436 C CB . THR A 1 292 ? 13.753 4.380 -5.771 1.00 15.84 ? 292 THR A CB 1 +ATOM 2437 O OG1 . THR A 1 292 ? 13.148 3.243 -6.396 1.00 17.07 ? 292 THR A OG1 1 +ATOM 2438 C CG2 . THR A 1 292 ? 13.836 4.168 -4.275 1.00 15.86 ? 292 THR A CG2 1 +ATOM 2439 N N . PRO A 1 293 ? 13.938 5.984 -8.406 1.00 14.84 ? 293 PRO A N 1 +ATOM 2440 C CA . PRO A 1 293 ? 13.897 5.872 -9.875 1.00 14.67 ? 293 PRO A CA 1 +ATOM 2441 C C . PRO A 1 293 ? 13.499 4.455 -10.322 1.00 15.65 ? 293 PRO A C 1 +ATOM 2442 O O . PRO A 1 293 ? 12.761 4.300 -11.296 1.00 16.06 ? 293 PRO A O 1 +ATOM 2443 C CB . PRO A 1 293 ? 15.339 6.206 -10.275 1.00 15.78 ? 293 PRO A CB 1 +ATOM 2444 C CG . PRO A 1 293 ? 15.801 7.141 -9.190 1.00 16.06 ? 293 PRO A CG 1 +ATOM 2445 C CD . PRO A 1 293 ? 15.229 6.536 -7.942 1.00 14.54 ? 293 PRO A CD 1 +ATOM 2446 N N . PHE A 1 294 ? 13.961 3.420 -9.593 1.00 16.05 ? 294 PHE A N 1 +ATOM 2447 C CA A PHE A 1 294 ? 13.614 2.037 -9.947 0.60 17.63 ? 294 PHE A CA 1 +ATOM 2448 C CA B PHE A 1 294 ? 13.625 2.042 -9.943 0.40 17.39 ? 294 PHE A CA 1 +ATOM 2449 C C . PHE A 1 294 ? 12.129 1.806 -9.755 1.00 17.49 ? 294 PHE A C 1 +ATOM 2450 O O . PHE A 1 294 ? 11.509 1.147 -10.587 1.00 18.53 ? 294 PHE A O 1 +ATOM 2451 C CB A PHE A 1 294 ? 14.414 1.007 -9.126 0.60 18.71 ? 294 PHE A CB 1 +ATOM 2452 C CB B PHE A 1 294 ? 14.457 1.057 -9.109 0.40 18.14 ? 294 PHE A CB 1 +ATOM 2453 C CG A PHE A 1 294 ? 15.839 0.729 -9.559 0.60 20.73 ? 294 PHE A CG 1 +ATOM 2454 C CG B PHE A 1 294 ? 14.453 -0.377 -9.584 0.40 19.78 ? 294 PHE A CG 1 +ATOM 2455 C CD1 A PHE A 1 294 ? 16.370 1.325 -10.689 0.60 22.07 ? 294 PHE A CD1 1 +ATOM 2456 C CD1 B PHE A 1 294 ? 14.237 -0.685 -10.916 0.40 21.21 ? 294 PHE A CD1 1 +ATOM 2457 C CD2 A PHE A 1 294 ? 16.668 -0.076 -8.794 0.60 22.36 ? 294 PHE A CD2 1 +ATOM 2458 C CD2 B PHE A 1 294 ? 14.733 -1.411 -8.711 0.40 21.02 ? 294 PHE A CD2 1 +ATOM 2459 C CE1 A PHE A 1 294 ? 17.685 1.092 -11.061 0.60 23.04 ? 294 PHE A CE1 1 +ATOM 2460 C CE1 B PHE A 1 294 ? 14.239 -2.002 -11.348 0.40 22.18 ? 294 PHE A CE1 1 +ATOM 2461 C CE2 A PHE A 1 294 ? 17.988 -0.290 -9.162 0.60 23.26 ? 294 PHE A CE2 1 +ATOM 2462 C CE2 B PHE A 1 294 ? 14.734 -2.729 -9.147 0.40 21.90 ? 294 PHE A CE2 1 +ATOM 2463 C CZ A PHE A 1 294 ? 18.485 0.292 -10.294 0.60 23.11 ? 294 PHE A CZ 1 +ATOM 2464 C CZ B PHE A 1 294 ? 14.485 -3.015 -10.461 0.40 21.80 ? 294 PHE A CZ 1 +ATOM 2465 N N . ASP A 1 295 ? 11.540 2.357 -8.678 1.00 16.66 ? 295 ASP A N 1 +ATOM 2466 C CA . ASP A 1 295 ? 10.103 2.218 -8.410 1.00 16.33 ? 295 ASP A CA 1 +ATOM 2467 C C . ASP A 1 295 ? 9.308 2.848 -9.537 1.00 17.17 ? 295 ASP A C 1 +ATOM 2468 O O . ASP A 1 295 ? 8.307 2.286 -9.970 1.00 18.29 ? 295 ASP A O 1 +ATOM 2469 C CB . ASP A 1 295 ? 9.693 2.913 -7.106 1.00 17.12 ? 295 ASP A CB 1 +ATOM 2470 C CG . ASP A 1 295 ? 10.224 2.304 -5.838 1.00 18.41 ? 295 ASP A CG 1 +ATOM 2471 O OD1 . ASP A 1 295 ? 10.556 1.095 -5.850 1.00 19.16 ? 295 ASP A OD1 1 +ATOM 2472 O OD2 . ASP A 1 295 ? 10.319 3.037 -4.827 1.00 18.01 ? 295 ASP A OD2 1 +ATOM 2473 N N . VAL A 1 296 ? 9.741 4.040 -9.998 1.00 16.16 ? 296 VAL A N 1 +ATOM 2474 C CA . VAL A 1 296 ? 9.047 4.738 -11.073 1.00 16.40 ? 296 VAL A CA 1 +ATOM 2475 C C . VAL A 1 296 ? 9.068 3.925 -12.358 1.00 18.06 ? 296 VAL A C 1 +ATOM 2476 O O . VAL A 1 296 ? 8.017 3.731 -12.959 1.00 19.14 ? 296 VAL A O 1 +ATOM 2477 C CB . VAL A 1 296 ? 9.581 6.179 -11.258 1.00 16.18 ? 296 VAL A CB 1 +ATOM 2478 C CG1 . VAL A 1 296 ? 8.940 6.830 -12.468 1.00 16.59 ? 296 VAL A CG1 1 +ATOM 2479 C CG2 . VAL A 1 296 ? 9.293 7.003 -10.012 1.00 16.05 ? 296 VAL A CG2 1 +ATOM 2480 N N . VAL A 1 297 ? 10.238 3.395 -12.748 1.00 18.39 ? 297 VAL A N 1 +ATOM 2481 C CA . VAL A 1 297 ? 10.337 2.563 -13.952 1.00 19.89 ? 297 VAL A CA 1 +ATOM 2482 C C . VAL A 1 297 ? 9.473 1.298 -13.807 1.00 20.88 ? 297 VAL A C 1 +ATOM 2483 O O . VAL A 1 297 ? 8.737 0.942 -14.739 1.00 21.36 ? 297 VAL A O 1 +ATOM 2484 C CB . VAL A 1 297 ? 11.811 2.192 -14.251 1.00 21.55 ? 297 VAL A CB 1 +ATOM 2485 C CG1 . VAL A 1 297 ? 11.910 1.180 -15.391 1.00 22.49 ? 297 VAL A CG1 1 +ATOM 2486 C CG2 . VAL A 1 297 ? 12.640 3.438 -14.563 1.00 22.68 ? 297 VAL A CG2 1 +ATOM 2487 N N . ARG A 1 298 ? 9.549 0.644 -12.641 1.00 21.24 ? 298 ARG A N 1 +ATOM 2488 C CA . ARG A 1 298 ? 8.807 -0.585 -12.372 1.00 22.55 ? 298 ARG A CA 1 +ATOM 2489 C C . ARG A 1 298 ? 7.308 -0.361 -12.501 1.00 22.93 ? 298 ARG A C 1 +ATOM 2490 O O . ARG A 1 298 ? 6.636 -1.115 -13.208 1.00 22.97 ? 298 ARG A O 1 +ATOM 2491 C CB . ARG A 1 298 ? 9.156 -1.144 -10.976 1.00 25.03 ? 298 ARG A CB 1 +ATOM 2492 C CG . ARG A 1 298 ? 8.689 -2.583 -10.744 1.00 29.79 ? 298 ARG A CG 1 +ATOM 2493 C CD . ARG A 1 298 ? 8.979 -3.085 -9.331 1.00 34.67 ? 298 ARG A CD 1 +ATOM 2494 N NE . ARG A 1 298 ? 10.404 -3.075 -8.999 1.00 39.16 ? 298 ARG A NE 1 +ATOM 2495 C CZ . ARG A 1 298 ? 10.970 -2.244 -8.127 1.00 42.47 ? 298 ARG A CZ 1 +ATOM 2496 N NH1 . ARG A 1 298 ? 12.272 -2.306 -7.894 1.00 43.09 ? 298 ARG A NH1 1 +ATOM 2497 N NH2 . ARG A 1 298 ? 10.237 -1.347 -7.482 1.00 42.21 ? 298 ARG A NH2 1 +ATOM 2498 N N . GLN A 1 299 ? 6.784 0.674 -11.846 1.00 23.07 ? 299 GLN A N 1 +ATOM 2499 C CA . GLN A 1 299 ? 5.354 0.958 -11.884 1.00 23.81 ? 299 GLN A CA 1 +ATOM 2500 C C . GLN A 1 299 ? 4.900 1.427 -13.238 1.00 25.68 ? 299 GLN A C 1 +ATOM 2501 O O . GLN A 1 299 ? 3.853 0.988 -13.714 1.00 26.69 ? 299 GLN A O 1 +ATOM 2502 C CB . GLN A 1 299 ? 4.957 1.970 -10.809 1.00 23.65 ? 299 GLN A CB 1 +ATOM 2503 C CG . GLN A 1 299 ? 3.447 2.122 -10.708 1.00 23.14 ? 299 GLN A CG 1 +ATOM 2504 C CD . GLN A 1 299 ? 2.957 2.977 -9.576 1.00 22.18 ? 299 GLN A CD 1 +ATOM 2505 O OE1 . GLN A 1 299 ? 1.844 3.497 -9.627 1.00 22.38 ? 299 GLN A OE1 1 +ATOM 2506 N NE2 . GLN A 1 299 ? 3.758 3.156 -8.534 1.00 20.10 ? 299 GLN A NE2 1 +ATOM 2507 N N . CYS A 1 300 ? 5.691 2.286 -13.886 1.00 26.06 ? 300 CYS A N 1 +ATOM 2508 C CA . CYS A 1 300 ? 5.337 2.786 -15.204 1.00 27.01 ? 300 CYS A CA 1 +ATOM 2509 C C . CYS A 1 300 ? 5.445 1.714 -16.315 1.00 28.98 ? 300 CYS A C 1 +ATOM 2510 O O . CYS A 1 300 ? 4.855 1.899 -17.375 1.00 29.26 ? 300 CYS A O 1 +ATOM 2511 C CB . CYS A 1 300 ? 6.127 4.045 -15.545 1.00 26.34 ? 300 CYS A CB 1 +ATOM 2512 S SG . CYS A 1 300 ? 5.721 5.471 -14.500 1.00 27.90 ? 300 CYS A SG 1 +ATOM 2513 N N . SER A 1 301 ? 6.132 0.583 -16.063 1.00 30.28 ? 301 SER A N 1 +ATOM 2514 C CA . SER A 1 301 ? 6.245 -0.481 -17.069 1.00 32.04 ? 301 SER A CA 1 +ATOM 2515 C C . SER A 1 301 ? 5.465 -1.768 -16.734 1.00 33.71 ? 301 SER A C 1 +ATOM 2516 O O . SER A 1 301 ? 5.292 -2.617 -17.604 1.00 34.43 ? 301 SER A O 1 +ATOM 2517 C CB . SER A 1 301 ? 7.705 -0.806 -17.369 1.00 33.84 ? 301 SER A CB 1 +ATOM 2518 O OG . SER A 1 301 ? 8.315 -1.500 -16.296 1.00 36.40 ? 301 SER A OG 1 +ATOM 2519 N N . GLY A 1 302 ? 5.019 -1.910 -15.491 1.00 34.12 ? 302 GLY A N 1 +ATOM 2520 C CA . GLY A 1 302 ? 4.222 -3.058 -15.071 1.00 35.05 ? 302 GLY A CA 1 +ATOM 2521 C C . GLY A 1 302 ? 4.997 -4.334 -14.820 1.00 35.61 ? 302 GLY A C 1 +ATOM 2522 O O . GLY A 1 302 ? 4.571 -5.413 -15.243 1.00 36.15 ? 302 GLY A O 1 +ATOM 2523 N N . VAL A 1 303 ? 6.128 -4.228 -14.109 1.00 35.32 ? 303 VAL A N 1 +ATOM 2524 C CA . VAL A 1 303 ? 6.954 -5.389 -13.780 1.00 35.32 ? 303 VAL A CA 1 +ATOM 2525 C C . VAL A 1 303 ? 6.215 -6.275 -12.784 1.00 34.93 ? 303 VAL A C 1 +ATOM 2526 O O . VAL A 1 303 ? 5.658 -5.767 -11.815 1.00 34.71 ? 303 VAL A O 1 +ATOM 2527 C CB . VAL A 1 303 ? 8.320 -4.942 -13.211 1.00 36.13 ? 303 VAL A CB 1 +ATOM 2528 C CG1 . VAL A 1 303 ? 9.179 -6.136 -12.804 1.00 36.86 ? 303 VAL A CG1 1 +ATOM 2529 C CG2 . VAL A 1 303 ? 9.059 -4.069 -14.209 1.00 36.62 ? 303 VAL A CG2 1 +ATOM 2530 N N A THR A 1 304 ? 6.200 -7.599 -13.004 0.50 34.73 ? 304 THR A N 1 +ATOM 2531 N N B THR A 1 304 ? 6.201 -7.585 -13.044 0.50 34.72 ? 304 THR A N 1 +ATOM 2532 C CA A THR A 1 304 ? 5.514 -8.516 -12.093 0.50 34.97 ? 304 THR A CA 1 +ATOM 2533 C CA B THR A 1 304 ? 5.553 -8.566 -12.184 0.50 34.96 ? 304 THR A CA 1 +ATOM 2534 C C A THR A 1 304 ? 6.476 -9.352 -11.246 0.50 35.09 ? 304 THR A C 1 +ATOM 2535 C C B THR A 1 304 ? 6.556 -9.620 -11.706 0.50 35.18 ? 304 THR A C 1 +ATOM 2536 O O A THR A 1 304 ? 6.038 -10.116 -10.384 0.50 34.91 ? 304 THR A O 1 +ATOM 2537 O O B THR A 1 304 ? 7.751 -9.347 -11.597 0.50 35.09 ? 304 THR A O 1 +ATOM 2538 C CB A THR A 1 304 ? 4.532 -9.384 -12.868 0.50 36.14 ? 304 THR A CB 1 +ATOM 2539 C CB B THR A 1 304 ? 4.394 -9.205 -12.939 0.50 35.98 ? 304 THR A CB 1 +ATOM 2540 O OG1 A THR A 1 304 ? 5.255 -10.142 -13.839 0.50 37.13 ? 304 THR A OG1 1 +ATOM 2541 O OG1 B THR A 1 304 ? 4.903 -9.804 -14.134 0.50 36.92 ? 304 THR A OG1 1 +ATOM 2542 C CG2 A THR A 1 304 ? 3.471 -8.559 -13.555 0.50 36.53 ? 304 THR A CG2 1 +ATOM 2543 C CG2 B THR A 1 304 ? 3.329 -8.196 -13.297 0.50 36.25 ? 304 THR A CG2 1 +HETATM 2544 S S . DMS B 2 . ? 6.882 -28.125 21.472 1.00 20.06 ? 401 DMS A S 1 +HETATM 2545 O O . DMS B 2 . ? 7.674 -27.206 22.316 1.00 20.48 ? 401 DMS A O 1 +HETATM 2546 C C1 . DMS B 2 . ? 5.955 -27.138 20.370 1.00 19.79 ? 401 DMS A C1 1 +HETATM 2547 C C2 . DMS B 2 . ? 5.581 -28.752 22.497 1.00 19.86 ? 401 DMS A C2 1 +HETATM 2548 S S . DMS C 2 . ? 7.044 -21.256 28.847 1.00 48.64 ? 402 DMS A S 1 +HETATM 2549 O O . DMS C 2 . ? 6.922 -22.717 28.688 1.00 48.54 ? 402 DMS A O 1 +HETATM 2550 C C1 . DMS C 2 . ? 5.390 -20.729 29.206 1.00 48.61 ? 402 DMS A C1 1 +HETATM 2551 C C2 . DMS C 2 . ? 7.732 -21.050 30.463 1.00 48.75 ? 402 DMS A C2 1 +HETATM 2552 S S . DMS D 2 . ? 6.261 -1.076 -6.323 1.00 29.95 ? 403 DMS A S 1 +HETATM 2553 O O . DMS D 2 . ? 5.958 -2.533 -6.360 1.00 30.71 ? 403 DMS A O 1 +HETATM 2554 C C1 . DMS D 2 . ? 7.022 -0.725 -7.858 1.00 30.37 ? 403 DMS A C1 1 +HETATM 2555 C C2 . DMS D 2 . ? 7.596 -0.894 -5.175 1.00 30.14 ? 403 DMS A C2 1 +HETATM 2556 S S . DMS E 2 . ? 2.371 -18.855 7.984 1.00 36.23 ? 404 DMS A S 1 +HETATM 2557 O O . DMS E 2 . ? 1.975 -20.201 7.546 1.00 36.88 ? 404 DMS A O 1 +HETATM 2558 C C1 . DMS E 2 . ? 3.628 -19.160 9.196 1.00 36.02 ? 404 DMS A C1 1 +HETATM 2559 C C2 . DMS E 2 . ? 1.058 -18.333 9.062 1.00 36.25 ? 404 DMS A C2 1 +HETATM 2560 O O . HOH F 3 . ? 16.168 1.473 -5.859 1.00 46.52 ? 501 HOH A O 1 +HETATM 2561 O O . HOH F 3 . ? 14.078 -19.491 32.277 1.00 41.46 ? 502 HOH A O 1 +HETATM 2562 O O . HOH F 3 . ? 6.880 13.380 21.324 1.00 29.25 ? 503 HOH A O 1 +HETATM 2563 O O . HOH F 3 . ? 13.998 -10.881 31.006 1.00 35.36 ? 504 HOH A O 1 +HETATM 2564 O O . HOH F 3 . ? -0.912 17.057 -19.539 1.00 38.93 ? 505 HOH A O 1 +HETATM 2565 O O . HOH F 3 . ? -3.061 10.895 -16.794 1.00 40.86 ? 506 HOH A O 1 +HETATM 2566 O O . HOH F 3 . ? 6.044 5.803 1.306 1.00 24.97 ? 507 HOH A O 1 +HETATM 2567 O O . HOH F 3 . ? 2.799 4.893 20.226 1.00 34.61 ? 508 HOH A O 1 +HETATM 2568 O O . HOH F 3 . ? 24.406 -5.758 8.993 1.00 17.99 ? 509 HOH A O 1 +HETATM 2569 O O . HOH F 3 . ? 21.426 -20.287 30.771 1.00 23.30 ? 510 HOH A O 1 +HETATM 2570 O O . HOH F 3 . ? 11.397 31.677 -2.156 1.00 25.90 ? 511 HOH A O 1 +HETATM 2571 O O . HOH F 3 . ? 12.195 -27.051 22.943 1.00 19.83 ? 512 HOH A O 1 +HETATM 2572 O O . HOH F 3 . ? 19.756 10.134 -2.112 1.00 30.96 ? 513 HOH A O 1 +HETATM 2573 O O . HOH F 3 . ? 5.478 -17.689 1.918 1.00 19.67 ? 514 HOH A O 1 +HETATM 2574 O O . HOH F 3 . ? 8.621 24.377 -11.854 1.00 26.34 ? 515 HOH A O 1 +HETATM 2575 O O . HOH F 3 . ? 0.090 -17.755 15.613 1.00 35.61 ? 516 HOH A O 1 +HETATM 2576 O O . HOH F 3 . ? 9.022 -26.606 14.754 1.00 40.22 ? 517 HOH A O 1 +HETATM 2577 O O . HOH F 3 . ? 9.601 -23.263 23.053 1.00 21.34 ? 518 HOH A O 1 +HETATM 2578 O O . HOH F 3 . ? 7.168 -26.153 0.208 1.00 33.81 ? 519 HOH A O 1 +HETATM 2579 O O . HOH F 3 . ? 16.939 -5.562 33.520 1.00 37.83 ? 520 HOH A O 1 +HETATM 2580 O O . HOH F 3 . ? 8.175 -31.641 17.026 1.00 31.45 ? 521 HOH A O 1 +HETATM 2581 O O . HOH F 3 . ? 20.485 8.740 25.153 1.00 39.46 ? 522 HOH A O 1 +HETATM 2582 O O . HOH F 3 . ? 6.032 -8.497 8.633 1.00 14.96 ? 523 HOH A O 1 +HETATM 2583 O O . HOH F 3 . ? 13.232 10.946 19.529 1.00 48.19 ? 524 HOH A O 1 +HETATM 2584 O O . HOH F 3 . ? 3.638 22.182 -0.621 1.00 34.15 ? 525 HOH A O 1 +HETATM 2585 O O . HOH F 3 . ? 6.136 4.320 21.727 1.00 40.25 ? 526 HOH A O 1 +HETATM 2586 O O . HOH F 3 . ? 24.549 4.929 18.980 1.00 27.73 ? 527 HOH A O 1 +HETATM 2587 O O . HOH F 3 . ? 21.248 -12.985 34.361 1.00 37.99 ? 528 HOH A O 1 +HETATM 2588 O O . HOH F 3 . ? 4.472 26.774 -8.479 1.00 30.69 ? 529 HOH A O 1 +HETATM 2589 O O . HOH F 3 . ? 16.252 12.230 7.025 1.00 30.97 ? 530 HOH A O 1 +HETATM 2590 O O . HOH F 3 . ? 6.267 8.345 11.973 1.00 33.79 ? 531 HOH A O 1 +HETATM 2591 O O . HOH F 3 . ? 14.837 -9.578 -4.136 1.00 34.69 ? 532 HOH A O 1 +HETATM 2592 O O . HOH F 3 . ? 23.775 -14.714 27.189 1.00 19.51 ? 533 HOH A O 1 +HETATM 2593 O O . HOH F 3 . ? 12.117 31.027 -8.579 1.00 28.22 ? 534 HOH A O 1 +HETATM 2594 O O . HOH F 3 . ? 10.798 -24.784 2.844 1.00 18.90 ? 535 HOH A O 1 +HETATM 2595 O O . HOH F 3 . ? 18.416 -28.970 20.813 1.00 44.66 ? 536 HOH A O 1 +HETATM 2596 O O . HOH F 3 . ? 13.207 23.157 -18.628 1.00 23.28 ? 537 HOH A O 1 +HETATM 2597 O O . HOH F 3 . ? 1.305 22.918 -1.525 1.00 39.57 ? 538 HOH A O 1 +HETATM 2598 O O . HOH F 3 . ? 13.733 -16.538 32.742 1.00 42.72 ? 539 HOH A O 1 +HETATM 2599 O O . HOH F 3 . ? 20.769 -13.106 10.684 1.00 24.31 ? 540 HOH A O 1 +HETATM 2600 O O . HOH F 3 . ? 8.621 5.486 22.418 1.00 37.97 ? 541 HOH A O 1 +HETATM 2601 O O . HOH F 3 . ? 19.369 9.113 0.911 0.50 21.92 ? 542 HOH A O 1 +HETATM 2602 O O . HOH F 3 . ? 20.059 10.278 15.617 1.00 20.33 ? 543 HOH A O 1 +HETATM 2603 O O . HOH F 3 . ? 13.595 0.797 -5.476 1.00 24.59 ? 544 HOH A O 1 +HETATM 2604 O O . HOH F 3 . ? 15.233 18.533 -21.978 1.00 20.38 ? 545 HOH A O 1 +HETATM 2605 O O . HOH F 3 . ? 4.305 7.616 10.196 1.00 32.91 ? 546 HOH A O 1 +HETATM 2606 O O . HOH F 3 . ? 28.704 8.986 -11.711 1.00 37.15 ? 547 HOH A O 1 +HETATM 2607 O O . HOH F 3 . ? 20.309 -18.432 26.843 1.00 19.13 ? 548 HOH A O 1 +HETATM 2608 O O . HOH F 3 . ? -0.916 1.911 13.421 1.00 31.81 ? 549 HOH A O 1 +HETATM 2609 O O . HOH F 3 . ? 22.855 27.060 -0.065 1.00 31.20 ? 550 HOH A O 1 +HETATM 2610 O O . HOH F 3 . ? 14.655 26.081 4.261 1.00 21.96 ? 551 HOH A O 1 +HETATM 2611 O O . HOH F 3 . ? 3.751 4.190 -18.169 1.00 34.28 ? 552 HOH A O 1 +HETATM 2612 O O . HOH F 3 . ? 13.326 -24.508 3.825 1.00 22.78 ? 553 HOH A O 1 +HETATM 2613 O O . HOH F 3 . ? 27.169 26.220 -11.432 1.00 21.90 ? 554 HOH A O 1 +HETATM 2614 O O . HOH F 3 . ? 9.882 19.723 -0.456 1.00 21.00 ? 555 HOH A O 1 +HETATM 2615 O O . HOH F 3 . ? -3.265 28.392 -8.099 1.00 21.52 ? 556 HOH A O 1 +HETATM 2616 O O . HOH F 3 . ? 20.738 21.420 4.165 1.00 27.07 ? 557 HOH A O 1 +HETATM 2617 O O . HOH F 3 . ? 6.867 -23.050 20.986 1.00 15.42 ? 558 HOH A O 1 +HETATM 2618 O O . HOH F 3 . ? 8.877 28.045 -1.387 1.00 22.94 ? 559 HOH A O 1 +HETATM 2619 O O . HOH F 3 . ? 0.113 -1.132 12.039 1.00 27.87 ? 560 HOH A O 1 +HETATM 2620 O O . HOH F 3 . ? 2.365 -8.994 18.707 1.00 22.91 ? 561 HOH A O 1 +HETATM 2621 O O . HOH F 3 . ? 4.775 24.485 -18.488 1.00 38.08 ? 562 HOH A O 1 +HETATM 2622 O O . HOH F 3 . ? 11.512 21.778 -17.020 1.00 21.35 ? 563 HOH A O 1 +HETATM 2623 O O . HOH F 3 . ? -1.260 -19.317 22.131 1.00 37.41 ? 564 HOH A O 1 +HETATM 2624 O O . HOH F 3 . ? 23.016 1.706 15.920 1.00 19.55 ? 565 HOH A O 1 +HETATM 2625 O O . HOH F 3 . ? 22.194 19.573 0.676 1.00 26.37 ? 566 HOH A O 1 +HETATM 2626 O O . HOH F 3 . ? 8.161 -17.907 28.320 1.00 34.19 ? 567 HOH A O 1 +HETATM 2627 O O . HOH F 3 . ? 7.958 3.525 -3.456 1.00 17.12 ? 568 HOH A O 1 +HETATM 2628 O O . HOH F 3 . ? 15.855 -27.834 12.287 1.00 23.48 ? 569 HOH A O 1 +HETATM 2629 O O . HOH F 3 . ? 16.709 28.254 -20.308 1.00 19.84 ? 570 HOH A O 1 +HETATM 2630 O O . HOH F 3 . ? 8.450 15.959 1.017 1.00 29.83 ? 571 HOH A O 1 +HETATM 2631 O O . HOH F 3 . ? 9.777 6.249 5.698 1.00 15.43 ? 572 HOH A O 1 +HETATM 2632 O O . HOH F 3 . ? 17.679 -25.053 30.209 1.00 30.30 ? 573 HOH A O 1 +HETATM 2633 O O . HOH F 3 . ? -5.912 -4.357 9.377 1.00 39.55 ? 574 HOH A O 1 +HETATM 2634 O O . HOH F 3 . ? 25.363 9.442 -4.945 1.00 28.46 ? 575 HOH A O 1 +HETATM 2635 O O . HOH F 3 . ? 16.878 6.559 -3.938 1.00 17.95 ? 576 HOH A O 1 +HETATM 2636 O O . HOH F 3 . ? 12.105 -32.691 16.980 1.00 31.58 ? 577 HOH A O 1 +HETATM 2637 O O . HOH F 3 . ? 12.237 21.928 2.499 1.00 20.92 ? 578 HOH A O 1 +HETATM 2638 O O . HOH F 3 . ? 9.918 -25.725 22.117 1.00 14.76 ? 579 HOH A O 1 +HETATM 2639 O O . HOH F 3 . ? 21.216 28.768 -6.698 1.00 41.88 ? 580 HOH A O 1 +HETATM 2640 O O . HOH F 3 . ? 10.267 17.926 1.520 1.00 26.08 ? 581 HOH A O 1 +HETATM 2641 O O . HOH F 3 . ? 24.873 29.260 -8.891 1.00 23.50 ? 582 HOH A O 1 +HETATM 2642 O O . HOH F 3 . ? 18.869 10.206 13.140 1.00 19.66 ? 583 HOH A O 1 +HETATM 2643 O O . HOH F 3 . ? -1.740 -15.236 2.695 1.00 33.35 ? 584 HOH A O 1 +HETATM 2644 O O . HOH F 3 . ? 10.507 -0.544 -3.024 1.00 21.42 ? 585 HOH A O 1 +HETATM 2645 O O . HOH F 3 . ? 23.489 22.748 -17.286 1.00 16.05 ? 586 HOH A O 1 +HETATM 2646 O O . HOH F 3 . ? 13.322 21.382 -20.851 1.00 26.01 ? 587 HOH A O 1 +HETATM 2647 O O . HOH F 3 . ? 18.541 -8.076 -3.408 1.00 40.63 ? 588 HOH A O 1 +HETATM 2648 O O . HOH F 3 . ? 8.071 3.586 30.056 1.00 37.79 ? 589 HOH A O 1 +HETATM 2649 O O . HOH F 3 . ? -1.477 3.593 -1.801 1.00 42.67 ? 590 HOH A O 1 +HETATM 2650 O O . HOH F 3 . ? 3.602 22.218 -19.191 1.00 32.60 ? 591 HOH A O 1 +HETATM 2651 O O . HOH F 3 . ? 9.993 -17.767 -3.963 1.00 21.80 ? 592 HOH A O 1 +HETATM 2652 O O . HOH F 3 . ? 22.259 16.293 3.670 1.00 37.29 ? 593 HOH A O 1 +HETATM 2653 O O . HOH F 3 . ? 10.599 32.889 -5.240 1.00 50.44 ? 594 HOH A O 1 +HETATM 2654 O O . HOH F 3 . ? 13.521 12.427 17.221 1.00 36.62 ? 595 HOH A O 1 +HETATM 2655 O O . HOH F 3 . ? -3.864 -12.103 2.544 1.00 20.32 ? 596 HOH A O 1 +HETATM 2656 O O . HOH F 3 . ? 26.359 -5.686 17.729 1.00 34.04 ? 597 HOH A O 1 +HETATM 2657 O O . HOH F 3 . ? 0.896 -16.433 2.082 1.00 39.32 ? 598 HOH A O 1 +HETATM 2658 O O . HOH F 3 . ? 28.921 9.379 -15.273 1.00 32.13 ? 599 HOH A O 1 +HETATM 2659 O O . HOH F 3 . ? 24.011 13.123 -1.655 1.00 31.18 ? 600 HOH A O 1 +HETATM 2660 O O . HOH F 3 . ? 21.433 21.717 -18.735 1.00 17.60 ? 601 HOH A O 1 +HETATM 2661 O O . HOH F 3 . ? 1.773 1.863 0.024 1.00 26.63 ? 602 HOH A O 1 +HETATM 2662 O O . HOH F 3 . ? 7.494 -28.340 15.770 1.00 33.19 ? 603 HOH A O 1 +HETATM 2663 O O . HOH F 3 . ? 15.633 -5.640 20.179 1.00 12.60 ? 604 HOH A O 1 +HETATM 2664 O O . HOH F 3 . ? 22.115 9.845 5.153 1.00 29.86 ? 605 HOH A O 1 +HETATM 2665 O O . HOH F 3 . ? 24.327 -8.927 20.642 1.00 20.53 ? 606 HOH A O 1 +HETATM 2666 O O . HOH F 3 . ? 16.826 -18.849 7.693 1.00 18.59 ? 607 HOH A O 1 +HETATM 2667 O O . HOH F 3 . ? 28.679 18.724 -8.356 1.00 35.42 ? 608 HOH A O 1 +HETATM 2668 O O . HOH F 3 . ? 24.424 -0.652 12.999 1.00 27.63 ? 609 HOH A O 1 +HETATM 2669 O O . HOH F 3 . ? -0.724 22.828 -3.129 1.00 39.81 ? 610 HOH A O 1 +HETATM 2670 O O . HOH F 3 . ? 19.959 5.204 -1.851 1.00 27.89 ? 611 HOH A O 1 +HETATM 2671 O O . HOH F 3 . ? 15.062 26.996 -12.204 1.00 18.02 ? 612 HOH A O 1 +HETATM 2672 O O . HOH F 3 . ? 8.199 -28.395 6.565 1.00 25.90 ? 613 HOH A O 1 +HETATM 2673 O O . HOH F 3 . ? 7.788 -24.522 25.639 1.00 18.95 ? 614 HOH A O 1 +HETATM 2674 O O . HOH F 3 . ? 10.042 -5.817 25.008 1.00 36.65 ? 615 HOH A O 1 +HETATM 2675 O O . HOH F 3 . ? 22.116 2.055 5.700 1.00 36.41 ? 616 HOH A O 1 +HETATM 2676 O O . HOH F 3 . ? 3.693 -17.399 20.860 1.00 18.97 ? 617 HOH A O 1 +HETATM 2677 O O . HOH F 3 . ? 26.732 23.577 -4.772 1.00 19.11 ? 618 HOH A O 1 +HETATM 2678 O O . HOH F 3 . ? 9.585 10.091 -4.896 1.00 12.16 ? 619 HOH A O 1 +HETATM 2679 O O . HOH F 3 . ? 1.295 -21.833 9.645 1.00 55.13 ? 620 HOH A O 1 +HETATM 2680 O O . HOH F 3 . ? 22.839 -7.292 34.441 1.00 27.63 ? 621 HOH A O 1 +HETATM 2681 O O . HOH F 3 . ? 18.961 -27.689 9.426 1.00 43.04 ? 622 HOH A O 1 +HETATM 2682 O O . HOH F 3 . ? 21.521 10.599 -17.013 1.00 25.46 ? 623 HOH A O 1 +HETATM 2683 O O . HOH F 3 . ? 13.990 14.918 12.502 1.00 32.85 ? 624 HOH A O 1 +HETATM 2684 O O . HOH F 3 . ? 1.918 -11.990 25.974 1.00 35.35 ? 625 HOH A O 1 +HETATM 2685 O O . HOH F 3 . ? -4.038 -9.431 16.969 1.00 48.81 ? 626 HOH A O 1 +HETATM 2686 O O . HOH F 3 . ? 13.366 19.059 3.371 1.00 28.20 ? 627 HOH A O 1 +HETATM 2687 O O . HOH F 3 . ? 24.678 1.909 12.377 1.00 46.47 ? 628 HOH A O 1 +HETATM 2688 O O . HOH F 3 . ? 14.580 -25.790 26.928 1.00 17.27 ? 629 HOH A O 1 +HETATM 2689 O O . HOH F 3 . ? 15.757 -12.840 31.816 1.00 22.74 ? 630 HOH A O 1 +HETATM 2690 O O . HOH F 3 . ? 14.529 -20.206 0.077 1.00 29.75 ? 631 HOH A O 1 +HETATM 2691 O O . HOH F 3 . ? 10.744 -23.544 0.343 1.00 18.47 ? 632 HOH A O 1 +HETATM 2692 O O . HOH F 3 . ? 2.570 13.675 -20.732 1.00 43.65 ? 633 HOH A O 1 +HETATM 2693 O O . HOH F 3 . ? 5.372 -6.477 21.881 1.00 27.60 ? 634 HOH A O 1 +HETATM 2694 O O . HOH F 3 . ? 3.140 9.142 -21.338 1.00 30.01 ? 635 HOH A O 1 +HETATM 2695 O O . HOH F 3 . ? 19.977 -21.182 28.743 1.00 32.10 ? 636 HOH A O 1 +HETATM 2696 O O . HOH F 3 . ? 7.570 12.013 0.722 1.00 33.53 ? 637 HOH A O 1 +HETATM 2697 O O . HOH F 3 . ? 12.447 11.173 10.477 1.00 26.80 ? 638 HOH A O 1 +HETATM 2698 O O . HOH F 3 . ? 15.757 6.369 -14.440 1.00 24.76 ? 639 HOH A O 1 +HETATM 2699 O O . HOH F 3 . ? 17.547 27.500 -12.889 1.00 19.19 ? 640 HOH A O 1 +HETATM 2700 O O . HOH F 3 . ? 5.057 -17.229 28.359 1.00 47.39 ? 641 HOH A O 1 +HETATM 2701 O O . HOH F 3 . ? -2.486 12.802 -14.220 1.00 42.13 ? 642 HOH A O 1 +HETATM 2702 O O . HOH F 3 . ? -4.994 23.645 -3.052 1.00 32.21 ? 643 HOH A O 1 +HETATM 2703 O O . HOH F 3 . ? -0.389 -15.332 10.266 1.00 36.06 ? 644 HOH A O 1 +HETATM 2704 O O . HOH F 3 . ? 5.665 2.461 -4.750 1.00 17.90 ? 645 HOH A O 1 +HETATM 2705 O O . HOH F 3 . ? 5.266 -27.778 14.491 1.00 36.75 ? 646 HOH A O 1 +HETATM 2706 O O . HOH F 3 . ? 2.594 25.678 -16.824 1.00 30.95 ? 647 HOH A O 1 +HETATM 2707 O O . HOH F 3 . ? 22.547 8.950 -2.317 1.00 43.74 ? 648 HOH A O 1 +HETATM 2708 O O . HOH F 3 . ? 15.056 -5.071 0.319 1.00 20.13 ? 649 HOH A O 1 +HETATM 2709 O O . HOH F 3 . ? 18.804 -7.696 6.107 1.00 16.54 ? 650 HOH A O 1 +HETATM 2710 O O . HOH F 3 . ? 6.258 2.386 -7.542 1.00 22.14 ? 651 HOH A O 1 +HETATM 2711 O O . HOH F 3 . ? 25.440 -15.867 12.089 1.00 45.56 ? 652 HOH A O 1 +HETATM 2712 O O . HOH F 3 . ? 13.858 31.054 -2.000 1.00 31.40 ? 653 HOH A O 1 +HETATM 2713 O O . HOH F 3 . ? 3.992 -22.184 7.072 1.00 17.77 ? 654 HOH A O 1 +HETATM 2714 O O . HOH F 3 . ? 16.781 4.789 30.472 1.00 57.67 ? 655 HOH A O 1 +HETATM 2715 O O . HOH F 3 . ? 14.653 -22.055 31.952 1.00 32.65 ? 656 HOH A O 1 +HETATM 2716 O O . HOH F 3 . ? 13.879 4.396 -20.671 1.00 28.86 ? 657 HOH A O 1 +HETATM 2717 O O . HOH F 3 . ? 27.708 -4.709 14.373 1.00 45.60 ? 658 HOH A O 1 +HETATM 2718 O O . HOH F 3 . ? -2.375 19.163 -11.398 1.00 31.14 ? 659 HOH A O 1 +HETATM 2719 O O . HOH F 3 . ? 9.946 -10.999 28.175 1.00 34.34 ? 660 HOH A O 1 +HETATM 2720 O O . HOH F 3 . ? 16.584 2.526 12.374 1.00 14.44 ? 661 HOH A O 1 +HETATM 2721 O O . HOH F 3 . ? 7.870 23.887 -2.281 1.00 26.01 ? 662 HOH A O 1 +HETATM 2722 O O . HOH F 3 . ? 15.076 11.269 -25.013 1.00 30.97 ? 663 HOH A O 1 +HETATM 2723 O O . HOH F 3 . ? 12.776 -3.174 -5.257 1.00 33.42 ? 664 HOH A O 1 +HETATM 2724 O O . HOH F 3 . ? 17.673 16.856 14.835 1.00 35.96 ? 665 HOH A O 1 +HETATM 2725 O O . HOH F 3 . ? -5.618 24.316 -7.513 1.00 20.87 ? 666 HOH A O 1 +HETATM 2726 O O . HOH F 3 . ? 29.467 15.778 -12.676 1.00 32.03 ? 667 HOH A O 1 +HETATM 2727 O O . HOH F 3 . ? -2.615 16.225 -9.453 1.00 26.89 ? 668 HOH A O 1 +HETATM 2728 O O . HOH F 3 . ? 20.970 6.298 19.867 1.00 27.96 ? 669 HOH A O 1 +HETATM 2729 O O . HOH F 3 . ? 22.051 -18.298 38.812 1.00 31.27 ? 670 HOH A O 1 +HETATM 2730 O O . HOH F 3 . ? 22.550 7.382 -17.399 1.00 24.21 ? 671 HOH A O 1 +HETATM 2731 O O . HOH F 3 . ? 20.505 18.890 3.164 1.00 33.29 ? 672 HOH A O 1 +HETATM 2732 O O . HOH F 3 . ? 21.340 -1.629 20.448 1.00 16.34 ? 673 HOH A O 1 +HETATM 2733 O O . HOH F 3 . ? -0.741 -15.736 14.250 1.00 30.76 ? 674 HOH A O 1 +HETATM 2734 O O . HOH F 3 . ? 23.323 20.417 -1.600 1.00 29.58 ? 675 HOH A O 1 +HETATM 2735 O O . HOH F 3 . ? 1.456 8.663 -6.092 1.00 38.82 ? 676 HOH A O 1 +HETATM 2736 O O . HOH F 3 . ? 17.887 4.741 -6.103 1.00 34.71 ? 677 HOH A O 1 +HETATM 2737 O O . HOH F 3 . ? 14.269 5.280 22.766 1.00 24.58 ? 678 HOH A O 1 +HETATM 2738 O O . HOH F 3 . ? 27.355 20.815 -5.391 1.00 24.25 ? 679 HOH A O 1 +HETATM 2739 O O . HOH F 3 . ? 9.720 -1.209 21.229 1.00 30.93 ? 680 HOH A O 1 +HETATM 2740 O O . HOH F 3 . ? 2.024 11.322 -5.624 1.00 22.74 ? 681 HOH A O 1 +HETATM 2741 O O . HOH F 3 . ? 9.861 24.688 -0.545 1.00 22.75 ? 682 HOH A O 1 +HETATM 2742 O O . HOH F 3 . ? 20.486 -1.656 24.001 1.00 24.64 ? 683 HOH A O 1 +HETATM 2743 O O . HOH F 3 . ? 23.225 2.694 9.309 1.00 22.82 ? 684 HOH A O 1 +HETATM 2744 O O . HOH F 3 . ? 27.418 16.923 -6.933 1.00 31.40 ? 685 HOH A O 1 +HETATM 2745 O O . HOH F 3 . ? 16.157 -27.895 23.992 1.00 21.03 ? 686 HOH A O 1 +HETATM 2746 O O . HOH F 3 . ? 18.371 -16.308 -2.702 1.00 39.26 ? 687 HOH A O 1 +HETATM 2747 O O . HOH F 3 . ? 25.461 -11.702 20.577 1.00 40.43 ? 688 HOH A O 1 +HETATM 2748 O O . HOH F 3 . ? 22.395 -0.560 18.161 1.00 15.98 ? 689 HOH A O 1 +HETATM 2749 O O . HOH F 3 . ? 11.106 -22.190 32.650 1.00 28.72 ? 690 HOH A O 1 +HETATM 2750 O O . HOH F 3 . ? 13.906 15.879 -26.087 1.00 40.25 ? 691 HOH A O 1 +HETATM 2751 O O . HOH F 3 . ? 3.233 28.434 -3.275 1.00 28.74 ? 692 HOH A O 1 +HETATM 2752 O O . HOH F 3 . ? 22.874 -2.369 16.096 1.00 16.71 ? 693 HOH A O 1 +HETATM 2753 O O . HOH F 3 . ? 5.924 -4.719 19.944 1.00 29.98 ? 694 HOH A O 1 +HETATM 2754 O O . HOH F 3 . ? 13.872 17.335 10.417 1.00 36.01 ? 695 HOH A O 1 +HETATM 2755 O O . HOH F 3 . ? -3.730 23.139 -15.560 1.00 97.94 ? 696 HOH A O 1 +HETATM 2756 O O . HOH F 3 . ? 8.299 -10.717 30.288 1.00 47.50 ? 697 HOH A O 1 +HETATM 2757 O O . HOH F 3 . ? 21.543 -1.801 26.438 1.00 47.98 ? 698 HOH A O 1 +HETATM 2758 O O . HOH F 3 . ? 18.028 -23.973 26.108 1.00 19.47 ? 699 HOH A O 1 +HETATM 2759 O O . HOH F 3 . ? 12.908 18.528 -23.180 1.00 41.68 ? 700 HOH A O 1 +HETATM 2760 O O . HOH F 3 . ? 2.949 30.284 -11.274 1.00 37.62 ? 701 HOH A O 1 +HETATM 2761 O O . HOH F 3 . ? 20.081 -20.090 16.613 1.00 22.76 ? 702 HOH A O 1 +HETATM 2762 O O . HOH F 3 . ? 18.378 30.888 -7.178 1.00 34.12 ? 703 HOH A O 1 +HETATM 2763 O O . HOH F 3 . ? 5.351 -31.635 18.500 1.00 40.71 ? 704 HOH A O 1 +HETATM 2764 O O . HOH F 3 . ? 0.701 25.514 -2.225 1.00 36.15 ? 705 HOH A O 1 +HETATM 2765 O O . HOH F 3 . ? 25.191 16.426 -14.367 1.00 24.82 ? 706 HOH A O 1 +HETATM 2766 O O . HOH F 3 . ? 21.234 -13.358 2.280 1.00 27.41 ? 707 HOH A O 1 +HETATM 2767 O O . HOH F 3 . ? 7.239 19.679 -0.526 1.00 19.53 ? 708 HOH A O 1 +HETATM 2768 O O . HOH F 3 . ? 26.231 -10.821 18.148 1.00 29.32 ? 709 HOH A O 1 +HETATM 2769 O O . HOH F 3 . ? 18.272 24.759 5.918 1.00 42.75 ? 710 HOH A O 1 +HETATM 2770 O O . HOH F 3 . ? 23.954 -16.170 21.645 1.00 23.30 ? 711 HOH A O 1 +HETATM 2771 O O . HOH F 3 . ? 10.555 -16.892 30.368 1.00 33.54 ? 712 HOH A O 1 +HETATM 2772 O O . HOH F 3 . ? -3.214 21.063 -9.741 1.00 34.02 ? 713 HOH A O 1 +HETATM 2773 O O . HOH F 3 . ? -2.136 9.260 -10.450 1.00 40.46 ? 714 HOH A O 1 +HETATM 2774 O O . HOH F 3 . ? 11.910 -29.685 8.498 1.00 34.74 ? 715 HOH A O 1 +HETATM 2775 O O . HOH F 3 . ? 1.343 -16.891 12.512 1.00 27.31 ? 716 HOH A O 1 +HETATM 2776 O O . HOH F 3 . ? 13.914 19.690 7.284 1.00 37.82 ? 717 HOH A O 1 +HETATM 2777 O O . HOH F 3 . ? -0.234 16.076 -0.146 0.50 11.47 ? 718 HOH A O 1 +HETATM 2778 O O . HOH F 3 . ? 24.548 -7.687 26.198 1.00 36.32 ? 719 HOH A O 1 +HETATM 2779 O O . HOH F 3 . ? 18.171 27.334 4.952 1.00 53.03 ? 720 HOH A O 1 +HETATM 2780 O O . HOH F 3 . ? 11.863 12.861 14.635 1.00 54.98 ? 721 HOH A O 1 +HETATM 2781 O O . HOH F 3 . ? 19.214 -6.192 32.419 1.00 25.40 ? 722 HOH A O 1 +HETATM 2782 O O . HOH F 3 . ? -0.227 7.570 -3.969 1.00 37.09 ? 723 HOH A O 1 +HETATM 2783 O O . HOH F 3 . ? 19.243 12.398 -3.622 1.00 19.12 ? 724 HOH A O 1 +HETATM 2784 O O . HOH F 3 . ? 23.410 -6.008 1.926 1.00 25.91 ? 725 HOH A O 1 +HETATM 2785 O O . HOH F 3 . ? 7.624 -8.536 -15.424 1.00 46.55 ? 726 HOH A O 1 +HETATM 2786 O O . HOH F 3 . ? 23.169 -8.425 4.161 1.00 50.23 ? 727 HOH A O 1 +HETATM 2787 O O . HOH F 3 . ? 20.967 16.913 -17.778 1.00 17.97 ? 728 HOH A O 1 +HETATM 2788 O O . HOH F 3 . ? 3.435 -8.065 24.643 1.00 37.20 ? 729 HOH A O 1 +HETATM 2789 O O . HOH F 3 . ? 2.421 -19.701 21.721 1.00 19.80 ? 730 HOH A O 1 +HETATM 2790 O O . HOH F 3 . ? 20.354 -26.799 18.082 1.00 35.93 ? 731 HOH A O 1 +HETATM 2791 O O . HOH F 3 . ? 26.885 -9.220 10.443 1.00 44.15 ? 732 HOH A O 1 +HETATM 2792 O O . HOH F 3 . ? 1.564 -8.119 21.531 1.00 37.29 ? 733 HOH A O 1 +HETATM 2793 O O . HOH F 3 . ? 15.456 24.744 7.786 1.00 37.81 ? 734 HOH A O 1 +HETATM 2794 O O . HOH F 3 . ? 27.760 21.772 -11.674 1.00 17.55 ? 735 HOH A O 1 +HETATM 2795 O O . HOH F 3 . ? -5.506 20.181 -8.002 1.00 40.32 ? 736 HOH A O 1 +HETATM 2796 O O . HOH F 3 . ? 11.915 15.221 4.229 1.00 32.50 ? 737 HOH A O 1 +HETATM 2797 O O . HOH F 3 . ? 30.151 25.265 -10.687 1.00 30.25 ? 738 HOH A O 1 +HETATM 2798 O O . HOH F 3 . ? 20.827 -22.801 22.064 1.00 21.95 ? 739 HOH A O 1 +HETATM 2799 O O . HOH F 3 . ? 13.583 -14.012 33.010 1.00 38.07 ? 740 HOH A O 1 +HETATM 2800 O O . HOH F 3 . ? 0.455 1.284 20.771 1.00 47.74 ? 741 HOH A O 1 +HETATM 2801 O O . HOH F 3 . ? -0.514 19.449 -15.740 1.00 36.34 ? 742 HOH A O 1 +HETATM 2802 O O . HOH F 3 . ? 23.836 -4.507 23.876 1.00 50.45 ? 743 HOH A O 1 +HETATM 2803 O O . HOH F 3 . ? 3.878 20.684 -21.337 1.00 32.39 ? 744 HOH A O 1 +HETATM 2804 O O . HOH F 3 . ? 24.290 -15.929 16.833 1.00 38.93 ? 745 HOH A O 1 +HETATM 2805 O O . HOH F 3 . ? 23.201 -5.397 26.412 1.00 24.88 ? 746 HOH A O 1 +HETATM 2806 O O . HOH F 3 . ? 26.273 20.548 -14.032 1.00 22.96 ? 747 HOH A O 1 +HETATM 2807 O O . HOH F 3 . ? 2.975 2.530 24.921 1.00 30.68 ? 748 HOH A O 1 +HETATM 2808 O O . HOH F 3 . ? 10.919 -11.853 30.486 1.00 37.95 ? 749 HOH A O 1 +HETATM 2809 O O . HOH F 3 . ? 20.396 13.586 9.082 1.00 33.87 ? 750 HOH A O 1 +HETATM 2810 O O . HOH F 3 . ? 11.865 4.048 22.653 1.00 33.22 ? 751 HOH A O 1 +HETATM 2811 O O . HOH F 3 . ? 27.729 -7.194 12.023 1.00 36.54 ? 752 HOH A O 1 +HETATM 2812 O O . HOH F 3 . ? 17.618 22.329 9.554 1.00 40.97 ? 753 HOH A O 1 +HETATM 2813 O O . HOH F 3 . ? 8.941 -7.897 -8.369 1.00 32.94 ? 754 HOH A O 1 +HETATM 2814 O O . HOH F 3 . ? 11.761 -29.800 22.589 1.00 19.37 ? 755 HOH A O 1 +HETATM 2815 O O . HOH F 3 . ? 28.635 10.717 -8.101 1.00 30.16 ? 756 HOH A O 1 +HETATM 2816 O O . HOH F 3 . ? 9.498 1.361 21.295 1.00 24.46 ? 757 HOH A O 1 +HETATM 2817 O O . HOH F 3 . ? 9.182 28.999 -17.474 1.00 26.72 ? 758 HOH A O 1 +HETATM 2818 O O . HOH F 3 . ? 16.203 30.204 -2.976 1.00 42.95 ? 759 HOH A O 1 +HETATM 2819 O O . HOH F 3 . ? 11.088 -31.620 10.226 1.00 43.15 ? 760 HOH A O 1 +HETATM 2820 O O . HOH F 3 . ? 20.093 -25.462 22.433 1.00 26.03 ? 761 HOH A O 1 +HETATM 2821 O O . HOH F 3 . ? 28.829 14.538 -8.128 1.00 34.41 ? 762 HOH A O 1 +HETATM 2822 O O . HOH F 3 . ? 3.441 24.795 -1.613 1.00 34.84 ? 763 HOH A O 1 +HETATM 2823 O O . HOH F 3 . ? 20.202 14.527 -19.039 1.00 33.34 ? 764 HOH A O 1 +HETATM 2824 O O . HOH F 3 . ? 0.115 -27.182 17.907 1.00 30.24 ? 765 HOH A O 1 +HETATM 2825 O O . HOH F 3 . ? 1.044 -16.222 23.465 1.00 44.28 ? 766 HOH A O 1 +HETATM 2826 O O . HOH F 3 . ? -2.627 17.627 -15.519 1.00 60.97 ? 767 HOH A O 1 +HETATM 2827 O O . HOH F 3 . ? 16.474 3.496 -7.806 1.00 29.34 ? 768 HOH A O 1 +HETATM 2828 O O . HOH F 3 . ? 24.409 -4.330 16.668 1.00 28.43 ? 769 HOH A O 1 +HETATM 2829 O O . HOH F 3 . ? 16.789 -18.630 -0.780 1.00 27.06 ? 770 HOH A O 1 +HETATM 2830 O O . HOH F 3 . ? 25.012 13.875 -17.225 1.00 25.24 ? 771 HOH A O 1 +HETATM 2831 O O . HOH F 3 . ? 6.492 -8.329 -7.853 1.00 39.75 ? 772 HOH A O 1 +HETATM 2832 O O . HOH F 3 . ? 20.068 -0.155 -1.012 1.00 35.16 ? 773 HOH A O 1 +HETATM 2833 O O . HOH F 3 . ? -0.000 -0.407 -0.000 0.50 24.99 ? 774 HOH A O 1 +HETATM 2834 O O . HOH F 3 . ? 11.274 -2.559 -16.545 1.00 43.12 ? 775 HOH A O 1 +HETATM 2835 O O . HOH F 3 . ? -1.568 6.148 -2.378 1.00 39.83 ? 776 HOH A O 1 +HETATM 2836 O O . HOH F 3 . ? -4.782 26.408 -9.310 1.00 22.16 ? 777 HOH A O 1 +HETATM 2837 O O . HOH F 3 . ? 16.309 -2.605 -2.855 1.00 41.31 ? 778 HOH A O 1 +HETATM 2838 O O . HOH F 3 . ? 30.825 20.967 -5.604 1.00 39.69 ? 779 HOH A O 1 +HETATM 2839 O O . HOH F 3 . ? 15.578 -19.046 34.790 1.00 41.80 ? 780 HOH A O 1 +HETATM 2840 O O . HOH F 3 . ? -2.125 -3.200 18.826 1.00 41.36 ? 781 HOH A O 1 +HETATM 2841 O O . HOH F 3 . ? 23.956 -20.421 20.945 1.00 45.16 ? 782 HOH A O 1 +HETATM 2842 O O . HOH F 3 . ? 12.859 22.637 6.077 1.00 35.21 ? 783 HOH A O 1 +HETATM 2843 O O . HOH F 3 . ? 25.214 -7.886 22.805 1.00 37.18 ? 784 HOH A O 1 +HETATM 2844 O O . HOH F 3 . ? 6.955 -15.138 -8.159 1.00 53.30 ? 785 HOH A O 1 +HETATM 2845 O O . HOH F 3 . ? 26.675 27.198 -8.963 1.00 30.23 ? 786 HOH A O 1 +HETATM 2846 O O . HOH F 3 . ? 5.969 2.060 28.913 1.00 39.92 ? 787 HOH A O 1 +HETATM 2847 O O . HOH F 3 . ? 3.824 -29.082 18.300 1.00 39.98 ? 788 HOH A O 1 +HETATM 2848 O O . HOH F 3 . ? 5.982 -23.035 -1.144 1.00 38.34 ? 789 HOH A O 1 +HETATM 2849 O O . HOH F 3 . ? 2.922 -18.050 1.197 1.00 32.81 ? 790 HOH A O 1 +HETATM 2850 O O . HOH F 3 . ? 21.637 -7.541 6.163 1.00 28.51 ? 791 HOH A O 1 +HETATM 2851 O O . HOH F 3 . ? 20.695 25.668 5.052 1.00 48.77 ? 792 HOH A O 1 +HETATM 2852 O O . HOH F 3 . ? 21.965 -17.907 23.656 1.00 32.28 ? 793 HOH A O 1 +HETATM 2853 O O . HOH F 3 . ? 3.738 9.887 14.440 1.00 38.47 ? 794 HOH A O 1 +HETATM 2854 O O . HOH F 3 . ? 7.546 -34.937 19.762 1.00 35.53 ? 795 HOH A O 1 +HETATM 2855 O O . HOH F 3 . ? 19.252 -11.117 34.347 1.00 37.85 ? 796 HOH A O 1 +HETATM 2856 O O . HOH F 3 . ? 17.203 15.425 -23.516 1.00 36.42 ? 797 HOH A O 1 +HETATM 2857 O O . HOH F 3 . ? 25.973 23.296 -2.028 1.00 29.90 ? 798 HOH A O 1 +HETATM 2858 O O . HOH F 3 . ? 17.194 -10.402 -5.842 1.00 42.68 ? 799 HOH A O 1 +HETATM 2859 O O . HOH F 3 . ? 8.784 -4.353 26.547 1.00 44.39 ? 800 HOH A O 1 +HETATM 2860 O O . HOH F 3 . ? 17.638 -17.925 37.524 1.00 49.93 ? 801 HOH A O 1 +HETATM 2861 O O . HOH F 3 . ? 12.370 32.802 -12.287 1.00 44.37 ? 802 HOH A O 1 +HETATM 2862 O O . HOH F 3 . ? 2.872 -1.757 -11.757 1.00 38.02 ? 803 HOH A O 1 +HETATM 2863 O O . HOH F 3 . ? 20.613 4.079 -5.766 1.00 40.55 ? 804 HOH A O 1 +HETATM 2864 O O . HOH F 3 . ? 14.640 -29.204 9.936 1.00 30.84 ? 805 HOH A O 1 +HETATM 2865 O O . HOH F 3 . ? 17.978 -19.808 33.834 1.00 31.41 ? 806 HOH A O 1 +HETATM 2866 O O . HOH F 3 . ? 15.789 -25.802 6.748 1.00 34.39 ? 807 HOH A O 1 +HETATM 2867 O O . HOH F 3 . ? 5.765 11.051 11.864 1.00 47.77 ? 808 HOH A O 1 +HETATM 2868 O O . HOH F 3 . ? 20.630 8.871 18.299 1.00 34.56 ? 809 HOH A O 1 +HETATM 2869 O O . HOH F 3 . ? 28.704 24.207 -12.425 1.00 28.48 ? 810 HOH A O 1 +HETATM 2870 O O . HOH F 3 . ? 0.105 -17.197 4.667 1.00 37.28 ? 811 HOH A O 1 +HETATM 2871 O O . HOH F 3 . ? 22.401 -22.767 19.930 1.00 34.52 ? 812 HOH A O 1 +HETATM 2872 O O . HOH F 3 . ? 18.717 -18.428 1.379 1.00 41.70 ? 813 HOH A O 1 +HETATM 2873 O O . HOH F 3 . ? 17.792 -22.269 33.181 1.00 42.81 ? 814 HOH A O 1 +HETATM 2874 O O . HOH F 3 . ? 20.668 -22.530 17.546 1.00 24.89 ? 815 HOH A O 1 +HETATM 2875 O O . HOH F 3 . ? 7.721 -5.547 22.694 1.00 46.81 ? 816 HOH A O 1 +HETATM 2876 O O . HOH F 3 . ? 20.766 5.826 -19.089 1.00 39.70 ? 817 HOH A O 1 +HETATM 2877 O O . HOH F 3 . ? 28.111 9.358 -5.026 1.00 37.59 ? 818 HOH A O 1 +HETATM 2878 O O . HOH F 3 . ? 25.908 -14.886 15.182 1.00 37.07 ? 819 HOH A O 1 +HETATM 2879 O O . HOH F 3 . ? 14.701 -6.924 -4.448 1.00 39.83 ? 820 HOH A O 1 +HETATM 2880 O O . HOH F 3 . ? 21.178 6.636 -5.226 1.00 32.30 ? 821 HOH A O 1 +HETATM 2881 O O . HOH F 3 . ? 24.874 10.464 -2.477 1.00 28.16 ? 822 HOH A O 1 +HETATM 2882 O O . HOH F 3 . ? -2.947 28.034 -1.971 1.00 40.10 ? 823 HOH A O 1 +HETATM 2883 O O . HOH F 3 . ? 14.364 20.232 9.961 1.00 64.02 ? 824 HOH A O 1 +HETATM 2884 O O . HOH F 3 . ? 1.998 9.130 -3.466 1.00 43.88 ? 825 HOH A O 1 +HETATM 2885 O O . HOH F 3 . ? 11.115 20.848 -19.436 1.00 28.04 ? 826 HOH A O 1 +HETATM 2886 O O . HOH F 3 . ? 10.569 -34.359 21.224 1.00 30.05 ? 827 HOH A O 1 +HETATM 2887 O O . HOH F 3 . ? 7.992 2.820 22.784 1.00 30.45 ? 828 HOH A O 1 +HETATM 2888 O O . HOH F 3 . ? 23.890 6.960 -5.408 1.00 41.41 ? 829 HOH A O 1 +HETATM 2889 O O . HOH F 3 . ? -4.860 -11.927 5.027 1.00 34.53 ? 830 HOH A O 1 +HETATM 2890 O O . HOH F 3 . ? -5.504 22.417 -9.461 1.00 35.31 ? 831 HOH A O 1 +HETATM 2891 O O . HOH F 3 . ? 21.823 -25.766 20.312 1.00 35.08 ? 832 HOH A O 1 +HETATM 2892 O O . HOH F 3 . ? 24.913 4.376 10.687 1.00 37.92 ? 833 HOH A O 1 +HETATM 2893 O O . HOH F 3 . ? 1.269 20.703 -21.897 1.00 32.97 ? 834 HOH A O 1 +HETATM 2894 O O . HOH F 3 . ? 3.771 11.637 -21.977 1.00 31.92 ? 835 HOH A O 1 +HETATM 2895 O O . HOH F 3 . ? 12.626 24.742 -22.470 1.00 40.86 ? 836 HOH A O 1 +HETATM 2896 O O . HOH F 3 . ? 16.595 -4.924 -1.942 1.00 35.09 ? 837 HOH A O 1 +HETATM 2897 O O . HOH F 3 . ? 11.940 -2.105 -13.997 1.00 81.21 ? 838 HOH A O 1 +HETATM 2898 O O . HOH F 3 . ? 22.261 -14.167 8.754 1.00 42.15 ? 839 HOH A O 1 +HETATM 2899 O O . HOH F 3 . ? 25.901 3.885 16.892 1.00 35.17 ? 840 HOH A O 1 +HETATM 2900 O O . HOH F 3 . ? 6.955 0.869 24.448 1.00 37.90 ? 841 HOH A O 1 +HETATM 2901 O O . HOH F 3 . ? 19.400 7.494 -3.277 1.00 24.50 ? 842 HOH A O 1 +HETATM 2902 O O . HOH F 3 . ? 22.943 -1.301 22.523 1.00 28.74 ? 843 HOH A O 1 +HETATM 2903 O O . HOH F 3 . ? -4.289 9.192 -7.451 1.00 33.71 ? 844 HOH A O 1 +HETATM 2904 O O . HOH F 3 . ? 24.338 2.535 6.965 1.00 50.58 ? 845 HOH A O 1 +HETATM 2905 O O . HOH F 3 . ? 12.482 24.156 3.931 1.00 27.61 ? 846 HOH A O 1 +HETATM 2906 O O . HOH F 3 . ? 13.627 -27.685 25.198 1.00 17.11 ? 847 HOH A O 1 +HETATM 2907 O O . HOH F 3 . ? 21.105 -20.304 14.193 1.00 35.35 ? 848 HOH A O 1 +HETATM 2908 O O . HOH F 3 . ? 22.677 -16.948 26.065 1.00 22.28 ? 849 HOH A O 1 +HETATM 2909 O O . HOH F 3 . ? 8.193 2.892 -22.627 1.00 55.19 ? 850 HOH A O 1 +HETATM 2910 O O . HOH F 3 . ? 17.203 -26.064 27.384 1.00 25.61 ? 851 HOH A O 1 +HETATM 2911 O O . HOH F 3 . ? 6.147 21.871 -1.733 1.00 31.41 ? 852 HOH A O 1 +HETATM 2912 O O . HOH F 3 . ? 20.037 -8.416 33.885 1.00 27.89 ? 853 HOH A O 1 +HETATM 2913 O O . HOH F 3 . ? 15.046 17.762 14.001 1.00 56.06 ? 854 HOH A O 1 +HETATM 2914 O O . HOH F 3 . ? 25.051 -3.698 20.136 1.00 53.04 ? 855 HOH A O 1 +HETATM 2915 O O . HOH F 3 . ? 10.109 25.184 -23.031 1.00 38.82 ? 856 HOH A O 1 +HETATM 2916 O O . HOH F 3 . ? 27.648 -2.076 15.145 1.00 34.17 ? 857 HOH A O 1 +HETATM 2917 O O . HOH F 3 . ? 19.976 14.798 -21.747 1.00 35.44 ? 858 HOH A O 1 +HETATM 2918 O O . HOH F 3 . ? 11.374 -33.896 23.985 1.00 24.95 ? 859 HOH A O 1 +HETATM 2919 O O . HOH F 3 . ? 25.999 20.692 -1.475 1.00 31.16 ? 860 HOH A O 1 +HETATM 2920 O O . HOH F 3 . ? 8.111 -2.686 22.688 1.00 44.34 ? 861 HOH A O 1 +HETATM 2921 O O . HOH F 3 . ? 10.912 0.306 23.988 1.00 62.89 ? 862 HOH A O 1 +HETATM 2922 O O . HOH F 3 . ? 0.810 22.459 -19.140 1.00 42.26 ? 863 HOH A O 1 +HETATM 2923 O O . HOH F 3 . ? 9.569 31.573 -18.134 1.00 44.74 ? 864 HOH A O 1 +HETATM 2924 O O . HOH F 3 . ? 4.943 1.282 26.322 1.00 29.80 ? 865 HOH A O 1 +HETATM 2925 O O . HOH F 3 . ? 8.400 -28.634 3.942 1.00 32.60 ? 866 HOH A O 1 +HETATM 2926 O O . HOH F 3 . ? 13.703 12.434 22.929 1.00 44.31 ? 867 HOH A O 1 +HETATM 2927 O O . HOH F 3 . ? 10.378 -27.381 2.773 1.00 30.68 ? 868 HOH A O 1 +HETATM 2928 O O . HOH F 3 . ? 28.747 25.438 -4.710 1.00 33.95 ? 869 HOH A O 1 +HETATM 2929 O O . HOH F 3 . ? 16.308 -29.927 22.132 1.00 41.46 ? 870 HOH A O 1 +HETATM 2930 O O . HOH F 3 . ? 20.530 -15.652 4.907 1.00 37.96 ? 871 HOH A O 1 +HETATM 2931 O O . HOH F 3 . ? 1.363 -29.462 16.883 1.00 43.05 ? 872 HOH A O 1 +HETATM 2932 O O . HOH F 3 . ? 28.290 -3.921 16.901 1.00 33.06 ? 873 HOH A O 1 +HETATM 2933 O O . HOH F 3 . ? 21.119 -26.362 24.834 1.00 28.95 ? 874 HOH A O 1 +HETATM 2934 O O . HOH F 3 . ? 27.101 14.413 -1.879 1.00 33.91 ? 875 HOH A O 1 +HETATM 2935 O O . HOH F 3 . ? 25.873 21.448 -16.628 1.00 22.36 ? 876 HOH A O 1 +HETATM 2936 O O . HOH F 3 . ? 25.161 31.405 -7.246 1.00 39.01 ? 877 HOH A O 1 +HETATM 2937 O O . HOH F 3 . ? 25.157 -0.742 15.399 1.00 32.15 ? 878 HOH A O 1 +HETATM 2938 O O . HOH F 3 . ? 18.090 -7.289 35.812 1.00 56.43 ? 879 HOH A O 1 +HETATM 2939 O O . HOH F 3 . ? 16.073 13.714 23.421 1.00 31.52 ? 880 HOH A O 1 +HETATM 2940 O O . HOH F 3 . ? 21.892 0.520 24.913 1.00 47.37 ? 881 HOH A O 1 +HETATM 2941 O O . HOH F 3 . ? 10.432 22.183 0.548 1.00 21.18 ? 882 HOH A O 1 +HETATM 2942 O O . HOH F 3 . ? 16.365 -11.946 34.322 1.00 44.91 ? 883 HOH A O 1 +HETATM 2943 O O . HOH F 3 . ? 14.946 -32.152 15.788 1.00 37.75 ? 884 HOH A O 1 +HETATM 2944 O O . HOH F 3 . ? 21.901 12.848 -18.345 1.00 27.03 ? 885 HOH A O 1 +HETATM 2945 O O . HOH F 3 . ? 23.819 16.236 -16.712 1.00 22.25 ? 886 HOH A O 1 +HETATM 2946 O O . HOH F 3 . ? 24.099 18.963 2.615 1.00 30.17 ? 887 HOH A O 1 +HETATM 2947 O O . HOH F 3 . ? 13.977 -31.276 21.409 1.00 26.57 ? 888 HOH A O 1 +HETATM 2948 O O . HOH F 3 . ? 24.747 17.900 -18.867 1.00 37.61 ? 889 HOH A O 1 +HETATM 2949 O O . HOH F 3 . ? 26.570 31.349 -4.896 1.00 34.25 ? 890 HOH A O 1 +HETATM 2950 O O . HOH F 3 . ? 25.523 16.140 -20.792 1.00 39.96 ? 891 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 A SER A 1 ? 0.3790 0.3658 0.2638 -0.1331 -0.1030 0.0674 1 SER A N +2 N N B SER A 1 ? 0.3647 0.3506 0.2482 -0.1342 -0.1039 0.0678 1 SER A N +3 C CA A SER A 1 ? 0.3697 0.3711 0.2741 -0.1239 -0.0975 0.0694 1 SER A CA +4 C CA B SER A 1 ? 0.3548 0.3538 0.2566 -0.1238 -0.0970 0.0677 1 SER A CA +5 C C A SER A 1 ? 0.3512 0.3620 0.2738 -0.1150 -0.0937 0.0712 1 SER A C +6 C C B SER A 1 ? 0.3399 0.3488 0.2604 -0.1153 -0.0938 0.0702 1 SER A C +7 O O A SER A 1 ? 0.3500 0.3592 0.2735 -0.1169 -0.0968 0.0737 1 SER A O +8 O O B SER A 1 ? 0.3368 0.3447 0.2586 -0.1178 -0.0975 0.0736 1 SER A O +9 C CB A SER A 1 ? 0.3908 0.4027 0.3042 -0.1293 -0.1027 0.0802 1 SER A CB +10 C CB B SER A 1 ? 0.3697 0.3791 0.2803 -0.1274 -0.1004 0.0766 1 SER A CB +11 O OG A SER A 1 ? 0.4343 0.4421 0.3375 -0.1310 -0.1009 0.0760 1 SER A OG +12 O OG B SER A 1 ? 0.3934 0.4150 0.3207 -0.1305 -0.1062 0.0898 1 SER A OG +13 N N A GLY A 2 ? 0.3321 0.3515 0.2678 -0.1055 -0.0870 0.0696 2 GLY A N +14 N N B GLY A 2 ? 0.3248 0.3424 0.2586 -0.1055 -0.0869 0.0684 2 GLY A N +15 C CA A GLY A 2 ? 0.3196 0.3459 0.2699 -0.0962 -0.0822 0.0700 2 GLY A CA +16 C CA B GLY A 2 ? 0.3159 0.3411 0.2651 -0.0967 -0.0827 0.0698 2 GLY A CA +17 C C A GLY A 2 ? 0.3152 0.3338 0.2586 -0.0888 -0.0752 0.0577 2 GLY A C +18 C C B GLY A 2 ? 0.3152 0.3333 0.2584 -0.0889 -0.0756 0.0578 2 GLY A C +19 O O A GLY A 2 ? 0.3266 0.3335 0.2538 -0.0916 -0.0748 0.0500 2 GLY A O +20 O O B GLY A 2 ? 0.3260 0.3323 0.2536 -0.0917 -0.0755 0.0505 2 GLY A O +21 N N . PHE A 3 ? 0.2972 0.3216 0.2523 -0.0793 -0.0695 0.0563 3 PHE A N +22 C CA . PHE A 3 ? 0.2893 0.3080 0.2403 -0.0721 -0.0633 0.0461 3 PHE A CA +23 C C . PHE A 3 ? 0.2801 0.3044 0.2431 -0.0646 -0.0601 0.0477 3 PHE A C +24 O O . PHE A 3 ? 0.2968 0.3290 0.2718 -0.0601 -0.0580 0.0527 3 PHE A O +25 C CB . PHE A 3 ? 0.2768 0.2952 0.2263 -0.0688 -0.0591 0.0409 3 PHE A CB +26 C CG . PHE A 3 ? 0.2827 0.2930 0.2240 -0.0645 -0.0542 0.0307 3 PHE A CG +27 C CD1 . PHE A 3 ? 0.2957 0.2956 0.2219 -0.0689 -0.0544 0.0255 3 PHE A CD1 +28 C CD2 . PHE A 3 ? 0.2846 0.2969 0.2329 -0.0562 -0.0493 0.0269 3 PHE A CD2 +29 C CE1 . PHE A 3 ? 0.3093 0.3023 0.2298 -0.0646 -0.0492 0.0174 3 PHE A CE1 +30 C CE2 . PHE A 3 ? 0.2909 0.2968 0.2333 -0.0528 -0.0452 0.0189 3 PHE A CE2 +31 C CZ . PHE A 3 ? 0.2995 0.2964 0.2291 -0.0566 -0.0449 0.0146 3 PHE A CZ +32 N N . ARG A 4 ? 0.2533 0.2727 0.2124 -0.0633 -0.0595 0.0440 4 ARG A N +33 C CA . ARG A 4 ? 0.2321 0.2556 0.2008 -0.0566 -0.0566 0.0454 4 ARG A CA +34 C C . ARG A 4 ? 0.2271 0.2449 0.1914 -0.0506 -0.0517 0.0360 4 ARG A C +35 O O . ARG A 4 ? 0.2404 0.2504 0.1940 -0.0527 -0.0512 0.0292 4 ARG A O +36 C CB . ARG A 4 ? 0.2469 0.2710 0.2168 -0.0613 -0.0615 0.0515 4 ARG A CB +37 C CG . ARG A 4 ? 0.2796 0.3131 0.2608 -0.0646 -0.0656 0.0640 4 ARG A CG +38 C CD . ARG A 4 ? 0.3081 0.3495 0.3037 -0.0561 -0.0610 0.0691 4 ARG A CD +39 N NE . ARG A 4 ? 0.3468 0.3979 0.3555 -0.0584 -0.0639 0.0826 4 ARG A NE +40 C CZ . ARG A 4 ? 0.3666 0.4250 0.3888 -0.0513 -0.0594 0.0896 4 ARG A CZ +41 N NH1 . ARG A 4 ? 0.3673 0.4234 0.3900 -0.0420 -0.0523 0.0836 4 ARG A NH1 +42 N NH2 . ARG A 4 ? 0.3326 0.4003 0.3678 -0.0535 -0.0618 0.1030 4 ARG A NH2 +43 N N A LYS A 5 ? 0.2120 0.2334 0.1844 -0.0433 -0.0480 0.0363 5 LYS A N +44 N N B LYS A 5 ? 0.2144 0.2357 0.1867 -0.0432 -0.0480 0.0362 5 LYS A N +45 C CA A LYS A 5 ? 0.2153 0.2320 0.1845 -0.0381 -0.0442 0.0287 5 LYS A CA +46 C CA B LYS A 5 ? 0.2199 0.2365 0.1890 -0.0379 -0.0441 0.0285 5 LYS A CA +47 C C A LYS A 5 ? 0.2227 0.2362 0.1884 -0.0413 -0.0467 0.0289 5 LYS A C +48 C C B LYS A 5 ? 0.2302 0.2435 0.1960 -0.0403 -0.0460 0.0280 5 LYS A C +49 O O A LYS A 5 ? 0.2236 0.2416 0.1956 -0.0420 -0.0489 0.0356 5 LYS A O +50 O O B LYS A 5 ? 0.2387 0.2557 0.2110 -0.0380 -0.0461 0.0322 5 LYS A O +51 C CB A LYS A 5 ? 0.2280 0.2480 0.2048 -0.0301 -0.0401 0.0295 5 LYS A CB +52 C CB B LYS A 5 ? 0.2315 0.2515 0.2083 -0.0300 -0.0399 0.0293 5 LYS A CB +53 C CG A LYS A 5 ? 0.2735 0.2887 0.2467 -0.0254 -0.0368 0.0217 5 LYS A CG +54 C CG B LYS A 5 ? 0.2752 0.2905 0.2486 -0.0252 -0.0367 0.0218 5 LYS A CG +55 C CD A LYS A 5 ? 0.3187 0.3300 0.2866 -0.0257 -0.0355 0.0155 5 LYS A CD +56 C CD B LYS A 5 ? 0.3199 0.3310 0.2877 -0.0255 -0.0354 0.0153 5 LYS A CD +57 C CE A LYS A 5 ? 0.3569 0.3701 0.3282 -0.0227 -0.0339 0.0162 5 LYS A CE +58 C CE B LYS A 5 ? 0.3559 0.3690 0.3270 -0.0227 -0.0339 0.0160 5 LYS A CE +59 N NZ A LYS A 5 ? 0.3728 0.3864 0.3481 -0.0165 -0.0312 0.0172 5 LYS A NZ +60 N NZ B LYS A 5 ? 0.3701 0.3837 0.3454 -0.0165 -0.0312 0.0172 5 LYS A NZ +61 N N . MET A 6 ? 0.2284 0.2341 0.1838 -0.0444 -0.0468 0.0227 6 MET A N +62 C CA . MET A 6 ? 0.2335 0.2339 0.1832 -0.0482 -0.0492 0.0221 6 MET A CA +63 C C . MET A 6 ? 0.2208 0.2164 0.1681 -0.0440 -0.0454 0.0155 6 MET A C +64 O O . MET A 6 ? 0.2287 0.2206 0.1722 -0.0415 -0.0417 0.0095 6 MET A O +65 C CB . MET A 6 ? 0.2693 0.2619 0.2066 -0.0561 -0.0522 0.0206 6 MET A CB +66 C CG . MET A 6 ? 0.3399 0.3251 0.2691 -0.0619 -0.0558 0.0208 6 MET A CG +67 S SD . MET A 6 ? 0.4425 0.4174 0.3551 -0.0716 -0.0596 0.0200 6 MET A SD +68 C CE . MET A 6 ? 0.3824 0.3682 0.3041 -0.0757 -0.0652 0.0303 6 MET A CE +69 N N . ALA A 7 ? 0.2066 0.2027 0.1567 -0.0436 -0.0466 0.0174 7 ALA A N +70 C CA . ALA A 7 ? 0.2137 0.2054 0.1620 -0.0401 -0.0434 0.0119 7 ALA A CA +71 C C . ALA A 7 ? 0.2240 0.2060 0.1616 -0.0459 -0.0451 0.0093 7 ALA A C +72 O O . ALA A 7 ? 0.2328 0.2119 0.1649 -0.0528 -0.0498 0.0128 7 ALA A O +73 C CB . ALA A 7 ? 0.2122 0.2101 0.1700 -0.0356 -0.0430 0.0154 7 ALA A CB +74 N N . PHE A 8 ? 0.2275 0.2033 0.1611 -0.0435 -0.0413 0.0035 8 PHE A N +75 C CA . PHE A 8 ? 0.2512 0.2159 0.1740 -0.0482 -0.0419 0.0008 8 PHE A CA +76 C C . PHE A 8 ? 0.2471 0.2136 0.1735 -0.0506 -0.0463 0.0055 8 PHE A C +77 O O . PHE A 8 ? 0.2320 0.2076 0.1699 -0.0462 -0.0464 0.0090 8 PHE A O +78 C CB . PHE A 8 ? 0.2598 0.2187 0.1802 -0.0438 -0.0357 -0.0056 8 PHE A CB +79 C CG . PHE A 8 ? 0.2847 0.2396 0.1998 -0.0426 -0.0313 -0.0096 8 PHE A CG +80 C CD1 . PHE A 8 ? 0.3166 0.2600 0.2176 -0.0474 -0.0304 -0.0122 8 PHE A CD1 +81 C CD2 . PHE A 8 ? 0.2990 0.2610 0.2225 -0.0369 -0.0282 -0.0105 8 PHE A CD2 +82 C CE1 . PHE A 8 ? 0.3331 0.2732 0.2298 -0.0458 -0.0259 -0.0152 8 PHE A CE1 +83 C CE2 . PHE A 8 ? 0.3182 0.2773 0.2381 -0.0358 -0.0244 -0.0134 8 PHE A CE2 +84 C CZ . PHE A 8 ? 0.3277 0.2764 0.2349 -0.0400 -0.0230 -0.0155 8 PHE A CZ +85 N N . PRO A 9 ? 0.2598 0.2165 0.1755 -0.0577 -0.0500 0.0058 9 PRO A N +86 C CA . PRO A 9 ? 0.2606 0.2180 0.1797 -0.0604 -0.0544 0.0103 9 PRO A CA +87 C C . PRO A 9 ? 0.2575 0.2167 0.1833 -0.0537 -0.0498 0.0072 9 PRO A C +88 O O . PRO A 9 ? 0.2854 0.2383 0.2066 -0.0505 -0.0442 0.0008 9 PRO A O +89 C CB . PRO A 9 ? 0.2926 0.2349 0.1951 -0.0690 -0.0579 0.0086 9 PRO A CB +90 C CG . PRO A 9 ? 0.3068 0.2437 0.1989 -0.0719 -0.0570 0.0060 9 PRO A CG +91 C CD . PRO A 9 ? 0.2731 0.2162 0.1721 -0.0635 -0.0498 0.0018 9 PRO A CD +92 N N . SER A 10 ? 0.2329 0.2016 0.1705 -0.0510 -0.0516 0.0125 10 SER A N +93 C CA . SER A 10 ? 0.2194 0.1919 0.1648 -0.0441 -0.0474 0.0103 10 SER A CA +94 C C . SER A 10 ? 0.2215 0.1881 0.1649 -0.0458 -0.0482 0.0097 10 SER A C +95 O O . SER A 10 ? 0.2135 0.1831 0.1632 -0.0404 -0.0448 0.0080 10 SER A O +96 C CB . SER A 10 ? 0.2200 0.2056 0.1788 -0.0388 -0.0475 0.0160 10 SER A CB +97 O OG . SER A 10 ? 0.2428 0.2330 0.2066 -0.0426 -0.0530 0.0242 10 SER A OG +98 N N . GLY A 11 ? 0.2295 0.1874 0.1641 -0.0534 -0.0530 0.0111 11 GLY A N +99 C CA . GLY A 11 ? 0.2298 0.1812 0.1622 -0.0558 -0.0546 0.0111 11 GLY A CA +100 C C . GLY A 11 ? 0.2268 0.1718 0.1570 -0.0512 -0.0480 0.0044 11 GLY A C +101 O O . GLY A 11 ? 0.2323 0.1805 0.1699 -0.0483 -0.0473 0.0055 11 GLY A O +102 N N . LYS A 12 ? 0.2248 0.1612 0.1455 -0.0504 -0.0428 -0.0020 12 LYS A N +103 C CA . LYS A 12 ? 0.2278 0.1579 0.1471 -0.0461 -0.0359 -0.0075 12 LYS A CA +104 C C . LYS A 12 ? 0.2202 0.1631 0.1547 -0.0382 -0.0326 -0.0068 12 LYS A C +105 O O . LYS A 12 ? 0.2276 0.1691 0.1658 -0.0351 -0.0292 -0.0082 12 LYS A O +106 C CB . LYS A 12 ? 0.2543 0.1739 0.1622 -0.0460 -0.0303 -0.0132 12 LYS A CB +107 C CG . LYS A 12 ? 0.3209 0.2229 0.2099 -0.0536 -0.0318 -0.0155 12 LYS A CG +108 C CD . LYS A 12 ? 0.3976 0.2910 0.2756 -0.0533 -0.0264 -0.0200 12 LYS A CD +109 C CE . LYS A 12 ? 0.4817 0.3558 0.3382 -0.0610 -0.0278 -0.0224 12 LYS A CE +110 N NZ . LYS A 12 ? 0.5337 0.3937 0.3822 -0.0623 -0.0255 -0.0248 12 LYS A NZ +111 N N . VAL A 13 ? 0.2016 0.1563 0.1443 -0.0351 -0.0337 -0.0041 13 VAL A N +112 C CA . VAL A 13 ? 0.1813 0.1466 0.1360 -0.0282 -0.0311 -0.0033 13 VAL A CA +113 C C . VAL A 13 ? 0.1687 0.1420 0.1324 -0.0272 -0.0345 0.0020 13 VAL A C +114 O O . VAL A 13 ? 0.1657 0.1433 0.1367 -0.0227 -0.0324 0.0021 13 VAL A O +115 C CB . VAL A 13 ? 0.1893 0.1613 0.1468 -0.0253 -0.0301 -0.0035 13 VAL A CB +116 C CG1 . VAL A 13 ? 0.1965 0.1771 0.1637 -0.0189 -0.0280 -0.0028 13 VAL A CG1 +117 C CG2 . VAL A 13 ? 0.2103 0.1748 0.1597 -0.0262 -0.0265 -0.0082 13 VAL A CG2 +118 N N . GLU A 14 ? 0.1675 0.1426 0.1312 -0.0315 -0.0400 0.0072 14 GLU A N +119 C CA . GLU A 14 ? 0.1621 0.1448 0.1350 -0.0306 -0.0432 0.0135 14 GLU A CA +120 C C . GLU A 14 ? 0.1768 0.1554 0.1508 -0.0305 -0.0424 0.0123 14 GLU A C +121 O O . GLU A 14 ? 0.1752 0.1613 0.1585 -0.0261 -0.0416 0.0149 14 GLU A O +122 C CB . GLU A 14 ? 0.1742 0.1577 0.1464 -0.0368 -0.0496 0.0200 14 GLU A CB +123 C CG . GLU A 14 ? 0.2071 0.1980 0.1825 -0.0359 -0.0505 0.0238 14 GLU A CG +124 C CD . GLU A 14 ? 0.2494 0.2399 0.2232 -0.0433 -0.0572 0.0303 14 GLU A CD +125 O OE1 . GLU A 14 ? 0.2807 0.2738 0.2599 -0.0459 -0.0616 0.0368 14 GLU A OE1 +126 O OE2 . GLU A 14 ? 0.2641 0.2514 0.2313 -0.0469 -0.0584 0.0294 14 GLU A OE2 +127 N N . GLY A 15 ? 0.1868 0.1528 0.1505 -0.0348 -0.0418 0.0079 15 GLY A N +128 C CA . GLY A 15 ? 0.1869 0.1467 0.1502 -0.0351 -0.0405 0.0063 15 GLY A CA +129 C C . GLY A 15 ? 0.1802 0.1431 0.1499 -0.0284 -0.0343 0.0031 15 GLY A C +130 O O . GLY A 15 ? 0.1941 0.1536 0.1659 -0.0278 -0.0328 0.0025 15 GLY A O +131 N N . CYS A 16 ? 0.1662 0.1350 0.1391 -0.0239 -0.0310 0.0014 16 CYS A N +132 C CA . CYS A 16 ? 0.1612 0.1338 0.1407 -0.0181 -0.0261 -0.0007 16 CYS A CA +133 C C . CYS A 16 ? 0.1592 0.1443 0.1489 -0.0133 -0.0270 0.0029 16 CYS A C +134 O O . CYS A 16 ? 0.1672 0.1557 0.1622 -0.0092 -0.0239 0.0020 16 CYS A O +135 C CB . CYS A 16 ? 0.1764 0.1450 0.1513 -0.0169 -0.0216 -0.0051 16 CYS A CB +136 S SG . CYS A 16 ? 0.2316 0.1834 0.1921 -0.0216 -0.0188 -0.0097 16 CYS A SG +137 N N . MET A 17 ? 0.1526 0.1440 0.1446 -0.0137 -0.0308 0.0074 17 MET A N +138 C CA . MET A 17 ? 0.1522 0.1534 0.1515 -0.0085 -0.0305 0.0105 17 MET A CA +139 C C . MET A 17 ? 0.1518 0.1579 0.1587 -0.0065 -0.0311 0.0143 17 MET A C +140 O O . MET A 17 ? 0.1596 0.1653 0.1680 -0.0094 -0.0341 0.0178 17 MET A O +141 C CB . MET A 17 ? 0.1531 0.1588 0.1521 -0.0085 -0.0326 0.0140 17 MET A CB +142 C CG . MET A 17 ? 0.1697 0.1714 0.1618 -0.0104 -0.0321 0.0106 17 MET A CG +143 S SD . MET A 17 ? 0.1856 0.1854 0.1757 -0.0071 -0.0278 0.0048 17 MET A SD +144 C CE . MET A 17 ? 0.2009 0.2086 0.1971 -0.0010 -0.0269 0.0074 17 MET A CE +145 N N . VAL A 18 ? 0.1429 0.1536 0.1543 -0.0018 -0.0287 0.0140 18 VAL A N +146 C CA . VAL A 18 ? 0.1498 0.1659 0.1684 0.0009 -0.0289 0.0176 18 VAL A CA +147 C C . VAL A 18 ? 0.1456 0.1680 0.1660 0.0060 -0.0278 0.0197 18 VAL A C +148 O O . VAL A 18 ? 0.1443 0.1657 0.1602 0.0072 -0.0267 0.0174 18 VAL A O +149 C CB . VAL A 18 ? 0.1652 0.1787 0.1868 0.0011 -0.0267 0.0150 18 VAL A CB +150 C CG1 . VAL A 18 ? 0.1808 0.1855 0.1986 -0.0036 -0.0270 0.0128 18 VAL A CG1 +151 C CG2 . VAL A 18 ? 0.1651 0.1782 0.1858 0.0034 -0.0238 0.0115 18 VAL A CG2 +152 N N . GLN A 19 ? 0.1422 0.1701 0.1683 0.0088 -0.0280 0.0241 19 GLN A N +153 C CA . GLN A 19 ? 0.1465 0.1786 0.1726 0.0138 -0.0264 0.0262 19 GLN A CA +154 C C . GLN A 19 ? 0.1436 0.1763 0.1715 0.0154 -0.0252 0.0242 19 GLN A C +155 O O . GLN A 19 ? 0.1405 0.1740 0.1740 0.0142 -0.0255 0.0247 19 GLN A O +156 C CB . GLN A 19 ? 0.1656 0.2034 0.1970 0.0161 -0.0268 0.0332 19 GLN A CB +157 C CG . GLN A 19 ? 0.2122 0.2528 0.2420 0.0218 -0.0243 0.0357 19 GLN A CG +158 C CD . GLN A 19 ? 0.2795 0.3260 0.3160 0.0245 -0.0240 0.0433 19 GLN A CD +159 O OE1 . GLN A 19 ? 0.2999 0.3499 0.3420 0.0254 -0.0242 0.0455 19 GLN A OE1 +160 N NE2 . GLN A 19 ? 0.2951 0.3434 0.3321 0.0261 -0.0232 0.0481 19 GLN A NE2 +161 N N . VAL A 20 ? 0.1391 0.1710 0.1624 0.0177 -0.0242 0.0225 20 VAL A N +162 C CA . VAL A 20 ? 0.1480 0.1811 0.1733 0.0187 -0.0239 0.0219 20 VAL A CA +163 C C . VAL A 20 ? 0.1564 0.1910 0.1775 0.0226 -0.0234 0.0245 20 VAL A C +164 O O . VAL A 20 ? 0.1651 0.1964 0.1783 0.0241 -0.0228 0.0238 20 VAL A O +165 C CB . VAL A 20 ? 0.1530 0.1826 0.1763 0.0167 -0.0238 0.0177 20 VAL A CB +166 C CG1 . VAL A 20 ? 0.1603 0.1924 0.1876 0.0173 -0.0241 0.0188 20 VAL A CG1 +167 C CG2 . VAL A 20 ? 0.1588 0.1853 0.1843 0.0134 -0.0231 0.0150 20 VAL A CG2 +168 N N . THR A 21 ? 0.1601 0.1987 0.1858 0.0244 -0.0234 0.0277 21 THR A N +169 C CA . THR A 21 ? 0.1782 0.2169 0.1984 0.0281 -0.0225 0.0302 21 THR A CA +170 C C . THR A 21 ? 0.1897 0.2293 0.2108 0.0274 -0.0239 0.0300 21 THR A C +171 O O . THR A 21 ? 0.1860 0.2296 0.2163 0.0258 -0.0245 0.0309 21 THR A O +172 C CB . THR A 21 ? 0.2060 0.2495 0.2307 0.0314 -0.0211 0.0358 21 THR A CB +173 O OG1 . THR A 21 ? 0.2226 0.2663 0.2481 0.0316 -0.0204 0.0375 21 THR A OG1 +174 C CG2 . THR A 21 ? 0.2269 0.2694 0.2447 0.0358 -0.0192 0.0387 21 THR A CG2 +175 N N . CYS A 22 ? 0.2077 0.2429 0.2189 0.0281 -0.0245 0.0292 22 CYS A N +176 C CA . CYS A 22 ? 0.2335 0.2695 0.2447 0.0270 -0.0266 0.0302 22 CYS A CA +177 C C . CYS A 22 ? 0.2710 0.3026 0.2700 0.0302 -0.0258 0.0320 22 CYS A C +178 O O . CYS A 22 ? 0.2785 0.3027 0.2655 0.0312 -0.0250 0.0301 22 CYS A O +179 C CB . CYS A 22 ? 0.2364 0.2697 0.2468 0.0230 -0.0292 0.0274 22 CYS A CB +180 S SG . CYS A 22 ? 0.3129 0.3491 0.3273 0.0205 -0.0326 0.0304 22 CYS A SG +181 N N . GLY A 23 ? 0.2938 0.3296 0.2959 0.0323 -0.0252 0.0360 23 GLY A N +182 C CA . GLY A 23 ? 0.3204 0.3516 0.3105 0.0360 -0.0235 0.0383 23 GLY A CA +183 C C . GLY A 23 ? 0.3405 0.3689 0.3258 0.0405 -0.0191 0.0393 23 GLY A C +184 O O . GLY A 23 ? 0.3496 0.3845 0.3455 0.0421 -0.0173 0.0419 23 GLY A O +185 N N . THR A 24 ? 0.3500 0.3684 0.3199 0.0420 -0.0176 0.0372 24 THR A N +186 C CA . THR A 24 ? 0.3600 0.3750 0.3251 0.0468 -0.0126 0.0387 24 THR A CA +187 C C . THR A 24 ? 0.3425 0.3554 0.3082 0.0448 -0.0129 0.0352 24 THR A C +188 O O . THR A 24 ? 0.3580 0.3683 0.3207 0.0484 -0.0090 0.0367 24 THR A O +189 C CB . THR A 24 ? 0.4144 0.4183 0.3611 0.0508 -0.0092 0.0394 24 THR A CB +190 O OG1 . THR A 24 ? 0.4539 0.4472 0.3867 0.0473 -0.0122 0.0343 24 THR A OG1 +191 C CG2 . THR A 24 ? 0.4277 0.4329 0.3722 0.0528 -0.0086 0.0431 24 THR A CG2 +192 N N . THR A 25 ? 0.3104 0.3248 0.2808 0.0395 -0.0172 0.0312 25 THR A N +193 C CA . THR A 25 ? 0.2916 0.3033 0.2612 0.0375 -0.0177 0.0277 25 THR A CA +194 C C . THR A 25 ? 0.2647 0.2846 0.2487 0.0354 -0.0183 0.0281 25 THR A C +195 O O . THR A 25 ? 0.2662 0.2913 0.2590 0.0329 -0.0204 0.0281 25 THR A O +196 C CB . THR A 25 ? 0.3080 0.3144 0.2715 0.0330 -0.0217 0.0233 25 THR A CB +197 O OG1 . THR A 25 ? 0.3325 0.3293 0.2804 0.0341 -0.0218 0.0229 25 THR A OG1 +198 C CG2 . THR A 25 ? 0.3143 0.3188 0.2782 0.0307 -0.0223 0.0198 25 THR A CG2 +199 N N . THR A 26 ? 0.2504 0.2704 0.2356 0.0365 -0.0163 0.0289 26 THR A N +200 C CA . THR A 26 ? 0.2337 0.2594 0.2297 0.0337 -0.0176 0.0293 26 THR A CA +201 C C . THR A 26 ? 0.2166 0.2386 0.2093 0.0312 -0.0182 0.0256 26 THR A C +202 O O . THR A 26 ? 0.2275 0.2450 0.2130 0.0334 -0.0162 0.0257 26 THR A O +203 C CB . THR A 26 ? 0.2539 0.2850 0.2569 0.0365 -0.0155 0.0355 26 THR A CB +204 O OG1 . THR A 26 ? 0.2709 0.3065 0.2788 0.0383 -0.0153 0.0390 26 THR A OG1 +205 C CG2 . THR A 26 ? 0.2595 0.2945 0.2711 0.0327 -0.0176 0.0361 26 THR A CG2 +206 N N . LEU A 27 ? 0.1900 0.2133 0.1877 0.0268 -0.0206 0.0225 27 LEU A N +207 C CA . LEU A 27 ? 0.1763 0.1967 0.1717 0.0241 -0.0212 0.0193 27 LEU A CA +208 C C . LEU A 27 ? 0.1629 0.1858 0.1657 0.0201 -0.0227 0.0183 27 LEU A C +209 O O . LEU A 27 ? 0.1637 0.1902 0.1728 0.0199 -0.0230 0.0208 27 LEU A O +210 C CB . LEU A 27 ? 0.1762 0.1911 0.1642 0.0230 -0.0222 0.0151 27 LEU A CB +211 C CG . LEU A 27 ? 0.1771 0.1923 0.1666 0.0215 -0.0240 0.0137 27 LEU A CG +212 C CD1 . LEU A 27 ? 0.1749 0.1939 0.1740 0.0186 -0.0246 0.0130 27 LEU A CD1 +213 C CD2 . LEU A 27 ? 0.1888 0.1986 0.1711 0.0199 -0.0258 0.0109 27 LEU A CD2 +214 N N . ASN A 28 ? 0.1481 0.1682 0.1488 0.0171 -0.0233 0.0150 28 ASN A N +215 C CA . ASN A 28 ? 0.1428 0.1628 0.1474 0.0132 -0.0242 0.0138 28 ASN A CA +216 C C . ASN A 28 ? 0.1380 0.1558 0.1440 0.0112 -0.0240 0.0101 28 ASN A C +217 O O . ASN A 28 ? 0.1433 0.1598 0.1471 0.0117 -0.0238 0.0082 28 ASN A O +218 C CB . ASN A 28 ? 0.1590 0.1768 0.1601 0.0110 -0.0247 0.0131 28 ASN A CB +219 C CG . ASN A 28 ? 0.1851 0.2055 0.1862 0.0134 -0.0244 0.0178 28 ASN A CG +220 O OD1 . ASN A 28 ? 0.1866 0.2104 0.1926 0.0130 -0.0252 0.0224 28 ASN A OD1 +221 N ND2 . ASN A 28 ? 0.1936 0.2120 0.1895 0.0160 -0.0230 0.0173 28 ASN A ND2 +222 N N . GLY A 29 ? 0.1306 0.1477 0.1402 0.0088 -0.0239 0.0097 29 GLY A N +223 C CA . GLY A 29 ? 0.1316 0.1457 0.1430 0.0071 -0.0224 0.0068 29 GLY A CA +224 C C . GLY A 29 ? 0.1363 0.1448 0.1445 0.0035 -0.0219 0.0046 29 GLY A C +225 O O . GLY A 29 ? 0.1468 0.1545 0.1528 0.0015 -0.0237 0.0059 29 GLY A O +226 N N . LEU A 30 ? 0.1341 0.1384 0.1416 0.0024 -0.0195 0.0016 30 LEU A N +227 C CA . LEU A 30 ? 0.1373 0.1342 0.1396 -0.0008 -0.0180 -0.0011 30 LEU A CA +228 C C . LEU A 30 ? 0.1373 0.1300 0.1426 -0.0011 -0.0150 -0.0017 30 LEU A C +229 O O . LEU A 30 ? 0.1475 0.1416 0.1582 0.0010 -0.0121 -0.0015 30 LEU A O +230 C CB . LEU A 30 ? 0.1341 0.1286 0.1331 -0.0010 -0.0162 -0.0037 30 LEU A CB +231 C CG . LEU A 30 ? 0.1495 0.1355 0.1410 -0.0042 -0.0143 -0.0065 30 LEU A CG +232 C CD1 . LEU A 30 ? 0.1640 0.1487 0.1493 -0.0073 -0.0180 -0.0060 30 LEU A CD1 +233 C CD2 . LEU A 30 ? 0.1619 0.1464 0.1524 -0.0034 -0.0116 -0.0084 30 LEU A CD2 +234 N N . TRP A 31 ? 0.1360 0.1233 0.1380 -0.0039 -0.0156 -0.0018 31 TRP A N +235 C CA . TRP A 31 ? 0.1406 0.1227 0.1448 -0.0042 -0.0127 -0.0022 31 TRP A CA +236 C C . TRP A 31 ? 0.1535 0.1230 0.1484 -0.0069 -0.0091 -0.0060 31 TRP A C +237 O O . TRP A 31 ? 0.1585 0.1212 0.1440 -0.0111 -0.0114 -0.0072 31 TRP A O +238 C CB . TRP A 31 ? 0.1435 0.1275 0.1500 -0.0056 -0.0164 0.0007 31 TRP A CB +239 C CG . TRP A 31 ? 0.1463 0.1244 0.1545 -0.0063 -0.0142 0.0006 31 TRP A CG +240 C CD1 . TRP A 31 ? 0.1544 0.1298 0.1669 -0.0040 -0.0090 -0.0003 31 TRP A CD1 +241 C CD2 . TRP A 31 ? 0.1473 0.1227 0.1548 -0.0093 -0.0176 0.0027 31 TRP A CD2 +242 N NE1 . TRP A 31 ? 0.1567 0.1268 0.1702 -0.0052 -0.0083 0.0003 31 TRP A NE1 +243 C CE2 . TRP A 31 ? 0.1583 0.1284 0.1687 -0.0086 -0.0139 0.0021 31 TRP A CE2 +244 C CE3 . TRP A 31 ? 0.1574 0.1343 0.1627 -0.0126 -0.0234 0.0056 31 TRP A CE3 +245 C CZ2 . TRP A 31 ? 0.1623 0.1274 0.1721 -0.0115 -0.0162 0.0035 31 TRP A CZ2 +246 C CZ3 . TRP A 31 ? 0.1626 0.1355 0.1682 -0.0157 -0.0261 0.0078 31 TRP A CZ3 +247 C CH2 . TRP A 31 ? 0.1640 0.1305 0.1711 -0.0153 -0.0226 0.0063 31 TRP A CH2 +248 N N . LEU A 32 ? 0.1528 0.1193 0.1501 -0.0046 -0.0033 -0.0072 32 LEU A N +249 C CA . LEU A 32 ? 0.1720 0.1257 0.1602 -0.0059 0.0020 -0.0106 32 LEU A CA +250 C C . LEU A 32 ? 0.1779 0.1269 0.1710 -0.0036 0.0080 -0.0101 32 LEU A C +251 O O . LEU A 32 ? 0.1695 0.1268 0.1746 0.0001 0.0099 -0.0072 32 LEU A O +252 C CB . LEU A 32 ? 0.1767 0.1319 0.1644 -0.0044 0.0045 -0.0115 32 LEU A CB +253 C CG . LEU A 32 ? 0.1925 0.1523 0.1759 -0.0062 -0.0006 -0.0120 32 LEU A CG +254 C CD1 . LEU A 32 ? 0.1900 0.1524 0.1752 -0.0043 0.0018 -0.0122 32 LEU A CD1 +255 C CD2 . LEU A 32 ? 0.2102 0.1605 0.1805 -0.0111 -0.0028 -0.0142 32 LEU A CD2 +256 N N . ASP A 33 ? 0.1908 0.1261 0.1746 -0.0061 0.0105 -0.0124 33 ASP A N +257 C CA . ASP A 33 ? 0.2009 0.1304 0.1891 -0.0038 0.0166 -0.0117 33 ASP A CA +258 C C . ASP A 33 ? 0.1946 0.1369 0.1970 -0.0019 0.0130 -0.0076 33 ASP A C +259 O O . ASP A 33 ? 0.2016 0.1493 0.2037 -0.0042 0.0060 -0.0065 33 ASP A O +260 C CB . ASP A 33 ? 0.2335 0.1598 0.2250 0.0003 0.0255 -0.0115 33 ASP A CB +261 C CG . ASP A 33 ? 0.3105 0.2238 0.2874 -0.0013 0.0295 -0.0153 33 ASP A CG +262 O OD1 . ASP A 33 ? 0.3480 0.2480 0.3097 -0.0056 0.0283 -0.0188 33 ASP A OD1 +263 O OD2 . ASP A 33 ? 0.3265 0.2427 0.3068 0.0015 0.0337 -0.0145 33 ASP A OD2 +264 N N . ASP A 34 ? 0.1764 0.1244 0.1914 0.0022 0.0173 -0.0046 34 ASP A N +265 C CA . ASP A 34 ? 0.1641 0.1238 0.1917 0.0038 0.0139 -0.0005 34 ASP A CA +266 C C . ASP A 34 ? 0.1535 0.1277 0.1907 0.0061 0.0110 0.0026 34 ASP A C +267 O O . ASP A 34 ? 0.1547 0.1379 0.2036 0.0083 0.0105 0.0066 34 ASP A O +268 C CB . ASP A 34 ? 0.1742 0.1298 0.2092 0.0061 0.0201 0.0014 34 ASP A CB +269 C CG . ASP A 34 ? 0.2272 0.1819 0.2691 0.0099 0.0282 0.0033 34 ASP A CG +270 O OD1 . ASP A 34 ? 0.2261 0.1809 0.2648 0.0103 0.0295 0.0023 34 ASP A OD1 +271 O OD2 . ASP A 34 ? 0.2542 0.2083 0.3054 0.0125 0.0334 0.0063 34 ASP A OD2 +272 N N . VAL A 35 ? 0.1421 0.1184 0.1739 0.0053 0.0084 0.0010 35 VAL A N +273 C CA . VAL A 35 ? 0.1436 0.1316 0.1821 0.0069 0.0051 0.0037 35 VAL A CA +274 C C . VAL A 35 ? 0.1399 0.1313 0.1715 0.0051 -0.0011 0.0023 35 VAL A C +275 O O . VAL A 35 ? 0.1499 0.1347 0.1716 0.0027 -0.0017 -0.0008 35 VAL A O +276 C CB . VAL A 35 ? 0.1601 0.1481 0.2015 0.0084 0.0091 0.0044 35 VAL A CB +277 C CG1 . VAL A 35 ? 0.1611 0.1599 0.2082 0.0091 0.0045 0.0072 35 VAL A CG1 +278 C CG2 . VAL A 35 ? 0.1679 0.1529 0.2177 0.0107 0.0163 0.0069 35 VAL A CG2 +279 N N . VAL A 36 ? 0.1299 0.1308 0.1664 0.0064 -0.0053 0.0050 36 VAL A N +280 C CA . VAL A 36 ? 0.1327 0.1371 0.1637 0.0058 -0.0101 0.0046 36 VAL A CA +281 C C . VAL A 36 ? 0.1263 0.1352 0.1584 0.0070 -0.0112 0.0053 36 VAL A C +282 O O . VAL A 36 ? 0.1188 0.1327 0.1579 0.0084 -0.0115 0.0082 36 VAL A O +283 C CB . VAL A 36 ? 0.1401 0.1500 0.1736 0.0065 -0.0136 0.0073 36 VAL A CB +284 C CG1 . VAL A 36 ? 0.1445 0.1580 0.1732 0.0070 -0.0172 0.0078 36 VAL A CG1 +285 C CG2 . VAL A 36 ? 0.1485 0.1535 0.1807 0.0045 -0.0135 0.0070 36 VAL A CG2 +286 N N . TYR A 37 ? 0.1289 0.1355 0.1541 0.0060 -0.0122 0.0030 37 TYR A N +287 C CA . TYR A 37 ? 0.1248 0.1341 0.1497 0.0065 -0.0137 0.0034 37 TYR A CA +288 C C . TYR A 37 ? 0.1305 0.1425 0.1501 0.0071 -0.0177 0.0037 37 TYR A C +289 O O . TYR A 37 ? 0.1433 0.1537 0.1579 0.0064 -0.0186 0.0027 37 TYR A O +290 C CB . TYR A 37 ? 0.1259 0.1303 0.1462 0.0052 -0.0117 0.0008 37 TYR A CB +291 C CG . TYR A 37 ? 0.1381 0.1378 0.1616 0.0052 -0.0062 0.0005 37 TYR A CG +292 C CD1 . TYR A 37 ? 0.1543 0.1469 0.1734 0.0041 -0.0034 -0.0017 37 TYR A CD1 +293 C CD2 . TYR A 37 ? 0.1499 0.1515 0.1806 0.0063 -0.0038 0.0029 37 TYR A CD2 +294 C CE1 . TYR A 37 ? 0.1709 0.1572 0.1914 0.0046 0.0027 -0.0021 37 TYR A CE1 +295 C CE2 . TYR A 37 ? 0.1620 0.1589 0.1962 0.0072 0.0026 0.0034 37 TYR A CE2 +296 C CZ . TYR A 37 ? 0.1816 0.1701 0.2098 0.0066 0.0062 0.0005 37 TYR A CZ +297 O OH . TYR A 37 ? 0.2143 0.1962 0.2448 0.0079 0.0135 0.0010 37 TYR A OH +298 N N . CYS A 38 ? 0.1233 0.1388 0.1439 0.0081 -0.0201 0.0056 38 CYS A N +299 C CA . CYS A 38 ? 0.1292 0.1452 0.1430 0.0092 -0.0229 0.0058 38 CYS A CA +300 C C . CYS A 38 ? 0.1335 0.1493 0.1447 0.0091 -0.0254 0.0065 38 CYS A C +301 O O . CYS A 38 ? 0.1367 0.1541 0.1535 0.0081 -0.0258 0.0082 38 CYS A O +302 C CB . CYS A 38 ? 0.1355 0.1545 0.1507 0.0110 -0.0234 0.0081 38 CYS A CB +303 S SG . CYS A 38 ? 0.1562 0.1794 0.1768 0.0121 -0.0247 0.0115 38 CYS A SG +304 N N . PRO A 39 ? 0.1337 0.1469 0.1360 0.0098 -0.0274 0.0058 39 PRO A N +305 C CA . PRO A 39 ? 0.1342 0.1442 0.1298 0.0092 -0.0309 0.0063 39 PRO A CA +306 C C . PRO A 39 ? 0.1415 0.1548 0.1415 0.0092 -0.0323 0.0095 39 PRO A C +307 O O . PRO A 39 ? 0.1469 0.1622 0.1478 0.0111 -0.0313 0.0107 39 PRO A O +308 C CB . PRO A 39 ? 0.1438 0.1499 0.1296 0.0112 -0.0305 0.0050 39 PRO A CB +309 C CG . PRO A 39 ? 0.1467 0.1541 0.1352 0.0113 -0.0279 0.0037 39 PRO A CG +310 C CD . PRO A 39 ? 0.1321 0.1439 0.1290 0.0113 -0.0265 0.0050 39 PRO A CD +311 N N . ARG A 40 ? 0.1347 0.1480 0.1365 0.0068 -0.0353 0.0114 40 ARG A N +312 C CA . ARG A 40 ? 0.1363 0.1522 0.1409 0.0061 -0.0378 0.0151 40 ARG A CA +313 C C . ARG A 40 ? 0.1631 0.1740 0.1549 0.0073 -0.0400 0.0150 40 ARG A C +314 O O . ARG A 40 ? 0.1704 0.1833 0.1629 0.0078 -0.0407 0.0175 40 ARG A O +315 C CB . ARG A 40 ? 0.1380 0.1555 0.1486 0.0025 -0.0411 0.0184 40 ARG A CB +316 C CG . ARG A 40 ? 0.1592 0.1704 0.1596 0.0001 -0.0455 0.0177 40 ARG A CG +317 C CD . ARG A 40 ? 0.1588 0.1727 0.1669 -0.0040 -0.0497 0.0227 40 ARG A CD +318 N NE . ARG A 40 ? 0.1780 0.1853 0.1766 -0.0069 -0.0543 0.0221 40 ARG A NE +319 C CZ . ARG A 40 ? 0.1952 0.2032 0.1976 -0.0113 -0.0597 0.0268 40 ARG A CZ +320 N NH1 . ARG A 40 ? 0.1822 0.1977 0.1982 -0.0129 -0.0605 0.0328 40 ARG A NH1 +321 N NH2 . ARG A 40 ? 0.1947 0.1956 0.1873 -0.0143 -0.0643 0.0261 40 ARG A NH2 +322 N N . HIS A 41 ? 0.1708 0.1750 0.1508 0.0084 -0.0397 0.0121 41 HIS A N +323 C CA . HIS A 41 ? 0.1863 0.1838 0.1525 0.0106 -0.0399 0.0119 41 HIS A CA +324 C C . HIS A 41 ? 0.1951 0.1958 0.1627 0.0149 -0.0359 0.0129 41 HIS A C +325 O O . HIS A 41 ? 0.2054 0.2012 0.1629 0.0172 -0.0354 0.0136 41 HIS A O +326 C CB . HIS A 41 ? 0.1972 0.1853 0.1502 0.0106 -0.0406 0.0091 41 HIS A CB +327 C CG . HIS A 41 ? 0.2270 0.2150 0.1798 0.0134 -0.0364 0.0069 41 HIS A CG +328 N ND1 . HIS A 41 ? 0.2661 0.2548 0.2175 0.0176 -0.0323 0.0076 41 HIS A ND1 +329 C CD2 . HIS A 41 ? 0.2370 0.2239 0.1905 0.0124 -0.0360 0.0046 41 HIS A CD2 +330 C CE1 . HIS A 41 ? 0.2654 0.2539 0.2173 0.0188 -0.0298 0.0062 41 HIS A CE1 +331 N NE2 . HIS A 41 ? 0.2544 0.2419 0.2074 0.0157 -0.0320 0.0041 41 HIS A NE2 +332 N N . VAL A 42 ? 0.1822 0.1906 0.1623 0.0156 -0.0336 0.0136 42 VAL A N +333 C CA . VAL A 42 ? 0.1859 0.1985 0.1696 0.0188 -0.0310 0.0159 42 VAL A CA +334 C C . VAL A 42 ? 0.1949 0.2082 0.1770 0.0189 -0.0329 0.0189 42 VAL A C +335 O O . VAL A 42 ? 0.2105 0.2241 0.1898 0.0221 -0.0310 0.0207 42 VAL A O +336 C CB . VAL A 42 ? 0.1841 0.2034 0.1807 0.0184 -0.0292 0.0161 42 VAL A CB +337 C CG1 . VAL A 42 ? 0.1795 0.2032 0.1863 0.0160 -0.0303 0.0173 42 VAL A CG1 +338 C CG2 . VAL A 42 ? 0.1914 0.2140 0.1907 0.0215 -0.0268 0.0185 42 VAL A CG2 +339 N N . ILE A 43 ? 0.1867 0.2004 0.1707 0.0153 -0.0367 0.0199 43 ILE A N +340 C CA . ILE A 43 ? 0.2001 0.2144 0.1822 0.0145 -0.0394 0.0234 43 ILE A CA +341 C C . ILE A 43 ? 0.2405 0.2444 0.2041 0.0146 -0.0414 0.0228 43 ILE A C +342 O O . ILE A 43 ? 0.2518 0.2544 0.2107 0.0138 -0.0437 0.0255 43 ILE A O +343 C CB . ILE A 43 ? 0.1911 0.2105 0.1842 0.0102 -0.0429 0.0260 43 ILE A CB +344 C CG1 . ILE A 43 ? 0.2007 0.2149 0.1882 0.0061 -0.0472 0.0255 43 ILE A CG1 +345 C CG2 . ILE A 43 ? 0.1891 0.2162 0.1985 0.0106 -0.0396 0.0261 43 ILE A CG2 +346 C CD1 . ILE A 43 ? 0.2105 0.2308 0.2108 0.0020 -0.0504 0.0297 43 ILE A CD1 +347 N N . CYS A 44 ? 0.2667 0.2625 0.2191 0.0156 -0.0403 0.0196 44 CYS A N +348 C CA . CYS A 44 ? 0.3137 0.2971 0.2464 0.0156 -0.0418 0.0188 44 CYS A CA +349 C C . CYS A 44 ? 0.3723 0.3510 0.2957 0.0217 -0.0360 0.0186 44 CYS A C +350 O O . CYS A 44 ? 0.3787 0.3624 0.3097 0.0251 -0.0317 0.0185 44 CYS A O +351 C CB . CYS A 44 ? 0.3157 0.2911 0.2403 0.0133 -0.0436 0.0155 44 CYS A CB +352 S SG . CYS A 44 ? 0.3091 0.2889 0.2438 0.0063 -0.0504 0.0168 44 CYS A SG +353 N N . THR A 45 ? 0.4158 0.3836 0.3217 0.0226 -0.0363 0.0189 45 THR A N +354 C CA . THR A 45 ? 0.4565 0.4164 0.3498 0.0287 -0.0301 0.0190 45 THR A CA +355 C C . THR A 45 ? 0.4930 0.4402 0.3723 0.0283 -0.0296 0.0152 45 THR A C +356 O O . THR A 45 ? 0.4961 0.4420 0.3762 0.0231 -0.0348 0.0130 45 THR A O +357 C CB . THR A 45 ? 0.4873 0.4397 0.3665 0.0295 -0.0304 0.0212 45 THR A CB +358 O OG1 . THR A 45 ? 0.5172 0.4565 0.3790 0.0245 -0.0359 0.0193 45 THR A OG1 +359 C CG2 . THR A 45 ? 0.4854 0.4501 0.3785 0.0283 -0.0326 0.0250 45 THR A CG2 +360 N N . SER A 46 ? 0.5146 0.4523 0.3813 0.0340 -0.0232 0.0150 46 SER A N +361 C CA . SER A 46 ? 0.5392 0.4636 0.3915 0.0340 -0.0223 0.0116 46 SER A CA +362 C C . SER A 46 ? 0.5572 0.4670 0.3904 0.0286 -0.0286 0.0095 46 SER A C +363 O O . SER A 46 ? 0.5653 0.4683 0.3928 0.0247 -0.0323 0.0065 46 SER A O +364 C CB . SER A 46 ? 0.5692 0.4857 0.4118 0.0418 -0.0133 0.0128 46 SER A CB +365 O OG . SER A 46 ? 0.6206 0.5295 0.4576 0.0423 -0.0115 0.0101 46 SER A OG +366 N N . GLU A 47 ? 0.5606 0.4662 0.3845 0.0278 -0.0303 0.0114 47 GLU A N +367 C CA . GLU A 47 ? 0.5733 0.4653 0.3785 0.0217 -0.0373 0.0104 47 GLU A CA +368 C C . GLU A 47 ? 0.5575 0.4580 0.3755 0.0133 -0.0468 0.0109 47 GLU A C +369 O O . GLU A 47 ? 0.5721 0.4620 0.3788 0.0078 -0.0527 0.0091 47 GLU A O +370 C CB . GLU A 47 ? 0.6141 0.5023 0.4093 0.0228 -0.0369 0.0133 47 GLU A CB +371 C CG . GLU A 47 ? 0.7008 0.5744 0.4757 0.0154 -0.0451 0.0130 47 GLU A CG +372 C CD . GLU A 47 ? 0.7996 0.6698 0.5645 0.0150 -0.0462 0.0161 47 GLU A CD +373 O OE1 . GLU A 47 ? 0.8102 0.6928 0.5882 0.0202 -0.0412 0.0191 47 GLU A OE1 +374 O OE2 . GLU A 47 ? 0.8443 0.6991 0.5879 0.0092 -0.0525 0.0159 47 GLU A OE2 +375 N N . ASP A 48 ? 0.5245 0.4437 0.3662 0.0125 -0.0481 0.0136 48 ASP A N +376 C CA . ASP A 48 ? 0.5032 0.4319 0.3596 0.0056 -0.0555 0.0152 48 ASP A CA +377 C C . ASP A 48 ? 0.4859 0.4129 0.3449 0.0034 -0.0570 0.0124 48 ASP A C +378 O O . ASP A 48 ? 0.4853 0.4111 0.3451 -0.0031 -0.0643 0.0134 48 ASP A O +379 C CB . ASP A 48 ? 0.5029 0.4508 0.3845 0.0067 -0.0541 0.0181 48 ASP A CB +380 C CG . ASP A 48 ? 0.5549 0.5080 0.4393 0.0072 -0.0546 0.0220 48 ASP A CG +381 O OD1 . ASP A 48 ? 0.5653 0.5100 0.4362 0.0033 -0.0596 0.0238 48 ASP A OD1 +382 O OD2 . ASP A 48 ? 0.5728 0.5380 0.4728 0.0109 -0.0503 0.0236 48 ASP A OD2 +383 N N . MET A 49 ? 0.4729 0.4001 0.3335 0.0086 -0.0505 0.0095 49 MET A N +384 C CA . MET A 49 ? 0.4625 0.3892 0.3268 0.0069 -0.0514 0.0069 49 MET A CA +385 C C . MET A 49 ? 0.4647 0.3753 0.3103 0.0022 -0.0568 0.0051 49 MET A C +386 O O . MET A 49 ? 0.4547 0.3665 0.3055 -0.0011 -0.0601 0.0043 49 MET A O +387 C CB . MET A 49 ? 0.4649 0.3936 0.3326 0.0132 -0.0435 0.0048 49 MET A CB +388 C CG . MET A 49 ? 0.4693 0.4140 0.3572 0.0161 -0.0398 0.0065 49 MET A CG +389 S SD . MET A 49 ? 0.4666 0.4249 0.3751 0.0107 -0.0446 0.0075 49 MET A SD +390 C CE . MET A 49 ? 0.3963 0.3518 0.3049 0.0097 -0.0444 0.0042 49 MET A CE +391 N N . LEU A 50 ? 0.4750 0.3702 0.2988 0.0018 -0.0579 0.0048 50 LEU A N +392 C CA . LEU A 50 ? 0.4951 0.3727 0.2988 -0.0035 -0.0638 0.0031 50 LEU A CA +393 C C . LEU A 50 ? 0.4892 0.3714 0.3007 -0.0125 -0.0744 0.0062 50 LEU A C +394 O O . LEU A 50 ? 0.5008 0.3775 0.3094 -0.0168 -0.0790 0.0053 50 LEU A O +395 C CB . LEU A 50 ? 0.5188 0.3769 0.2950 -0.0022 -0.0625 0.0021 50 LEU A CB +396 C CG . LEU A 50 ? 0.5538 0.4051 0.3208 0.0072 -0.0512 -0.0002 50 LEU A CG +397 C CD1 . LEU A 50 ? 0.5787 0.4107 0.3185 0.0088 -0.0492 -0.0005 50 LEU A CD1 +398 C CD2 . LEU A 50 ? 0.5675 0.4125 0.3316 0.0097 -0.0473 -0.0035 50 LEU A CD2 +399 N N . ASN A 51 ? 0.4655 0.3587 0.2886 -0.0153 -0.0781 0.0107 51 ASN A N +400 C CA . ASN A 51 ? 0.4505 0.3502 0.2843 -0.0236 -0.0877 0.0154 51 ASN A CA +401 C C . ASN A 51 ? 0.4106 0.3292 0.2674 -0.0231 -0.0871 0.0201 51 ASN A C +402 O O . ASN A 51 ? 0.4166 0.3359 0.2718 -0.0268 -0.0920 0.0243 51 ASN A O +403 C CB . ASN A 51 ? 0.4934 0.3764 0.3050 -0.0310 -0.0968 0.0172 51 ASN A CB +404 C CG . ASN A 51 ? 0.5408 0.4292 0.3627 -0.0404 -0.1077 0.0232 51 ASN A CG +405 O OD1 . ASN A 51 ? 0.5517 0.4536 0.3951 -0.0411 -0.1081 0.0253 51 ASN A OD1 +406 N ND2 . ASN A 51 ? 0.5631 0.4408 0.3698 -0.0478 -0.1167 0.0266 51 ASN A ND2 +407 N N . PRO A 52 ? 0.3637 0.2970 0.2411 -0.0183 -0.0808 0.0193 52 PRO A N +408 C CA . PRO A 52 ? 0.3370 0.2864 0.2345 -0.0171 -0.0792 0.0233 52 PRO A CA +409 C C . PRO A 52 ? 0.3183 0.2781 0.2333 -0.0231 -0.0854 0.0295 52 PRO A C +410 O O . PRO A 52 ? 0.3308 0.2919 0.2521 -0.0260 -0.0879 0.0301 52 PRO A O +411 C CB . PRO A 52 ? 0.3352 0.2934 0.2451 -0.0104 -0.0704 0.0200 52 PRO A CB +412 C CG . PRO A 52 ? 0.3498 0.3017 0.2544 -0.0104 -0.0698 0.0161 52 PRO A CG +413 C CD . PRO A 52 ? 0.3524 0.2872 0.2342 -0.0139 -0.0749 0.0150 52 PRO A CD +414 N N . ASN A 53 ? 0.2904 0.2581 0.2144 -0.0247 -0.0874 0.0346 53 ASN A N +415 C CA . ASN A 53 ? 0.2714 0.2513 0.2160 -0.0292 -0.0915 0.0417 53 ASN A CA +416 C C . ASN A 53 ? 0.2561 0.2495 0.2199 -0.0233 -0.0835 0.0415 53 ASN A C +417 O O . ASN A 53 ? 0.2636 0.2611 0.2298 -0.0214 -0.0818 0.0432 53 ASN A O +418 C CB . ASN A 53 ? 0.2848 0.2640 0.2268 -0.0357 -0.0999 0.0486 53 ASN A CB +419 C CG . ASN A 53 ? 0.3101 0.3024 0.2753 -0.0401 -0.1038 0.0571 53 ASN A CG +420 O OD1 . ASN A 53 ? 0.3120 0.3174 0.2984 -0.0364 -0.0978 0.0589 53 ASN A OD1 +421 N ND2 . ASN A 53 ? 0.3174 0.3058 0.2792 -0.0483 -0.1136 0.0631 53 ASN A ND2 +422 N N . TYR A 54 ? 0.2424 0.2414 0.2180 -0.0206 -0.0786 0.0394 54 TYR A N +423 C CA . TYR A 54 ? 0.2190 0.2277 0.2090 -0.0151 -0.0706 0.0380 54 TYR A CA +424 C C . TYR A 54 ? 0.2126 0.2325 0.2207 -0.0161 -0.0708 0.0446 54 TYR A C +425 O O . TYR A 54 ? 0.2098 0.2340 0.2224 -0.0125 -0.0664 0.0439 54 TYR A O +426 C CB . TYR A 54 ? 0.1991 0.2092 0.1952 -0.0128 -0.0659 0.0343 54 TYR A CB +427 C CG . TYR A 54 ? 0.2051 0.2062 0.1857 -0.0098 -0.0634 0.0275 54 TYR A CG +428 C CD1 . TYR A 54 ? 0.2100 0.2115 0.1881 -0.0046 -0.0576 0.0238 54 TYR A CD1 +429 C CD2 . TYR A 54 ? 0.2146 0.2070 0.1837 -0.0123 -0.0670 0.0256 54 TYR A CD2 +430 C CE1 . TYR A 54 ? 0.2203 0.2145 0.1861 -0.0017 -0.0549 0.0189 54 TYR A CE1 +431 C CE2 . TYR A 54 ? 0.2297 0.2141 0.1858 -0.0093 -0.0641 0.0200 54 TYR A CE2 +432 C CZ . TYR A 54 ? 0.2388 0.2243 0.1935 -0.0039 -0.0578 0.0169 54 TYR A CZ +433 O OH . TYR A 54 ? 0.2600 0.2383 0.2033 -0.0007 -0.0547 0.0126 54 TYR A OH +434 N N . GLU A 55 ? 0.2157 0.2401 0.2346 -0.0210 -0.0755 0.0513 55 GLU A N +435 C CA . GLU A 55 ? 0.2147 0.2503 0.2523 -0.0216 -0.0749 0.0585 55 GLU A CA +436 C C . GLU A 55 ? 0.2191 0.2544 0.2503 -0.0224 -0.0778 0.0605 55 GLU A C +437 O O . GLU A 55 ? 0.2158 0.2588 0.2585 -0.0196 -0.0739 0.0625 55 GLU A O +438 C CB . GLU A 55 ? 0.2489 0.2902 0.3003 -0.0271 -0.0801 0.0674 55 GLU A CB +439 C CG . GLU A 55 ? 0.3177 0.3632 0.3827 -0.0252 -0.0751 0.0679 55 GLU A CG +440 C CD . GLU A 55 ? 0.3953 0.4491 0.4783 -0.0201 -0.0658 0.0687 55 GLU A CD +441 O OE1 . GLU A 55 ? 0.3796 0.4366 0.4658 -0.0173 -0.0623 0.0681 55 GLU A OE1 +442 O OE2 . GLU A 55 ? 0.4443 0.5004 0.5372 -0.0188 -0.0615 0.0697 55 GLU A OE2 +443 N N . ASP A 56 ? 0.2230 0.2482 0.2347 -0.0260 -0.0845 0.0597 56 ASP A N +444 C CA . ASP A 56 ? 0.2304 0.2538 0.2334 -0.0269 -0.0872 0.0616 56 ASP A CA +445 C C . ASP A 56 ? 0.2346 0.2569 0.2318 -0.0198 -0.0798 0.0556 56 ASP A C +446 O O . ASP A 56 ? 0.2434 0.2719 0.2470 -0.0182 -0.0783 0.0583 56 ASP A O +447 C CB . ASP A 56 ? 0.2578 0.2683 0.2388 -0.0329 -0.0960 0.0623 56 ASP A CB +448 C CG . ASP A 56 ? 0.3026 0.3156 0.2907 -0.0413 -0.1053 0.0708 56 ASP A CG +449 O OD1 . ASP A 56 ? 0.2869 0.3134 0.2985 -0.0422 -0.1049 0.0781 56 ASP A OD1 +450 O OD2 . ASP A 56 ? 0.3320 0.3330 0.3023 -0.0470 -0.1130 0.0709 56 ASP A OD2 +451 N N . LEU A 57 ? 0.2342 0.2493 0.2205 -0.0158 -0.0754 0.0482 57 LEU A N +452 C CA . LEU A 57 ? 0.2381 0.2527 0.2202 -0.0093 -0.0686 0.0437 57 LEU A CA +453 C C . LEU A 57 ? 0.2260 0.2529 0.2289 -0.0057 -0.0628 0.0448 57 LEU A C +454 O O . LEU A 57 ? 0.2258 0.2561 0.2308 -0.0021 -0.0595 0.0449 57 LEU A O +455 C CB . LEU A 57 ? 0.2503 0.2561 0.2198 -0.0060 -0.0651 0.0369 57 LEU A CB +456 C CG . LEU A 57 ? 0.2895 0.2804 0.2353 -0.0081 -0.0690 0.0346 57 LEU A CG +457 C CD1 . LEU A 57 ? 0.3054 0.2892 0.2426 -0.0049 -0.0650 0.0287 57 LEU A CD1 +458 C CD2 . LEU A 57 ? 0.3070 0.2920 0.2385 -0.0060 -0.0683 0.0350 57 LEU A CD2 +459 N N . LEU A 58 ? 0.2097 0.2422 0.2272 -0.0068 -0.0616 0.0459 58 LEU A N +460 C CA . LEU A 58 ? 0.2064 0.2478 0.2414 -0.0036 -0.0557 0.0464 58 LEU A CA +461 C C . LEU A 58 ? 0.2077 0.2577 0.2561 -0.0045 -0.0564 0.0529 58 LEU A C +462 O O . LEU A 58 ? 0.2154 0.2705 0.2731 -0.0010 -0.0514 0.0525 58 LEU A O +463 C CB . LEU A 58 ? 0.2030 0.2459 0.2476 -0.0042 -0.0534 0.0458 58 LEU A CB +464 C CG . LEU A 58 ? 0.2085 0.2557 0.2651 -0.0005 -0.0460 0.0438 58 LEU A CG +465 C CD1 . LEU A 58 ? 0.2022 0.2459 0.2502 0.0035 -0.0423 0.0379 58 LEU A CD1 +466 C CD2 . LEU A 58 ? 0.2163 0.2637 0.2805 -0.0013 -0.0438 0.0438 58 LEU A CD2 +467 N N . ILE A 59 ? 0.2065 0.2578 0.2550 -0.0094 -0.0630 0.0590 59 ILE A N +468 C CA . ILE A 59 ? 0.2165 0.2764 0.2778 -0.0106 -0.0643 0.0661 59 ILE A CA +469 C C . ILE A 59 ? 0.2255 0.2857 0.2813 -0.0069 -0.0619 0.0643 59 ILE A C +470 O O . ILE A 59 ? 0.2214 0.2898 0.2908 -0.0055 -0.0597 0.0681 59 ILE A O +471 C CB . ILE A 59 ? 0.2392 0.2992 0.2986 -0.0174 -0.0732 0.0734 59 ILE A CB +472 C CG1 . ILE A 59 ? 0.2630 0.3255 0.3329 -0.0213 -0.0757 0.0777 59 ILE A CG1 +473 C CG2 . ILE A 59 ? 0.2463 0.3149 0.3164 -0.0188 -0.0750 0.0808 59 ILE A CG2 +474 C CD1 . ILE A 59 ? 0.2926 0.3538 0.3584 -0.0292 -0.0861 0.0852 59 ILE A CD1 +475 N N . ARG A 60 ? 0.2395 0.2907 0.2757 -0.0051 -0.0622 0.0591 60 ARG A N +476 C CA . ARG A 60 ? 0.2522 0.3034 0.2828 -0.0012 -0.0596 0.0581 60 ARG A CA +477 C C . ARG A 60 ? 0.2388 0.2934 0.2769 0.0044 -0.0524 0.0543 60 ARG A C +478 O O . ARG A 60 ? 0.2522 0.3074 0.2870 0.0080 -0.0500 0.0539 60 ARG A O +479 C CB . ARG A 60 ? 0.2970 0.3364 0.3034 -0.0011 -0.0620 0.0552 60 ARG A CB +480 C CG . ARG A 60 ? 0.3633 0.3965 0.3587 -0.0077 -0.0701 0.0585 60 ARG A CG +481 C CD . ARG A 60 ? 0.4112 0.4515 0.4147 -0.0112 -0.0745 0.0661 60 ARG A CD +482 N NE . ARG A 60 ? 0.4675 0.5059 0.4695 -0.0189 -0.0830 0.0711 60 ARG A NE +483 C CZ . ARG A 60 ? 0.4890 0.5351 0.5020 -0.0237 -0.0881 0.0793 60 ARG A CZ +484 N NH1 . ARG A 60 ? 0.4853 0.5294 0.4970 -0.0313 -0.0964 0.0846 60 ARG A NH1 +485 N NH2 . ARG A 60 ? 0.4813 0.5375 0.5075 -0.0212 -0.0853 0.0830 60 ARG A NH2 +486 N N . LYS A 61 ? 0.2107 0.2668 0.2580 0.0050 -0.0491 0.0517 61 LYS A N +487 C CA . LYS A 61 ? 0.2015 0.2591 0.2540 0.0092 -0.0432 0.0481 61 LYS A CA +488 C C . LYS A 61 ? 0.1973 0.2624 0.2687 0.0094 -0.0401 0.0509 61 LYS A C +489 O O . LYS A 61 ? 0.2081 0.2760 0.2892 0.0068 -0.0408 0.0540 61 LYS A O +490 C CB . LYS A 61 ? 0.2188 0.2701 0.2642 0.0098 -0.0414 0.0424 61 LYS A CB +491 C CG . LYS A 61 ? 0.2620 0.3046 0.2885 0.0101 -0.0435 0.0394 61 LYS A CG +492 C CD . LYS A 61 ? 0.3096 0.3507 0.3275 0.0139 -0.0418 0.0394 61 LYS A CD +493 C CE . LYS A 61 ? 0.3620 0.3928 0.3608 0.0150 -0.0423 0.0363 61 LYS A CE +494 N NZ . LYS A 61 ? 0.3994 0.4282 0.3897 0.0193 -0.0397 0.0373 61 LYS A NZ +495 N N . SER A 62 ? 0.1776 0.2457 0.2545 0.0125 -0.0365 0.0504 62 SER A N +496 C CA . SER A 62 ? 0.1690 0.2418 0.2617 0.0132 -0.0327 0.0521 62 SER A CA +497 C C . SER A 62 ? 0.1510 0.2194 0.2419 0.0152 -0.0285 0.0468 62 SER A C +498 O O . SER A 62 ? 0.1477 0.2118 0.2273 0.0164 -0.0288 0.0431 62 SER A O +499 C CB . SER A 62 ? 0.2000 0.2793 0.3004 0.0144 -0.0328 0.0566 62 SER A CB +500 O OG . SER A 62 ? 0.2401 0.3234 0.3417 0.0120 -0.0372 0.0620 62 SER A OG +501 N N . ASN A 63 ? 0.1426 0.2113 0.2442 0.0155 -0.0244 0.0467 63 ASN A N +502 C CA . ASN A 63 ? 0.1389 0.2022 0.2378 0.0164 -0.0210 0.0420 63 ASN A CA +503 C C . ASN A 63 ? 0.1396 0.2029 0.2325 0.0181 -0.0221 0.0410 63 ASN A C +504 O O . ASN A 63 ? 0.1422 0.2008 0.2270 0.0182 -0.0218 0.0372 63 ASN A O +505 C CB . ASN A 63 ? 0.1400 0.2028 0.2503 0.0167 -0.0165 0.0429 63 ASN A CB +506 C CG . ASN A 63 ? 0.1606 0.2220 0.2770 0.0158 -0.0136 0.0440 63 ASN A CG +507 O OD1 . ASN A 63 ? 0.1610 0.2198 0.2717 0.0147 -0.0145 0.0422 63 ASN A OD1 +508 N ND2 . ASN A 63 ? 0.1556 0.2186 0.2845 0.0164 -0.0096 0.0474 63 ASN A ND2 +509 N N . HIS A 64 ? 0.1366 0.2058 0.2344 0.0194 -0.0233 0.0450 64 HIS A N +510 C CA . HIS A 64 ? 0.1395 0.2098 0.2337 0.0214 -0.0239 0.0456 64 HIS A CA +511 C C . HIS A 64 ? 0.1476 0.2159 0.2288 0.0228 -0.0257 0.0445 64 HIS A C +512 O O . HIS A 64 ? 0.1578 0.2267 0.2361 0.0249 -0.0255 0.0453 64 HIS A O +513 C CB . HIS A 64 ? 0.1440 0.2214 0.2474 0.0228 -0.0243 0.0507 64 HIS A CB +514 C CG . HIS A 64 ? 0.1574 0.2393 0.2592 0.0231 -0.0269 0.0545 64 HIS A CG +515 N ND1 . HIS A 64 ? 0.1694 0.2548 0.2790 0.0213 -0.0277 0.0575 64 HIS A ND1 +516 C CD2 . HIS A 64 ? 0.1738 0.2566 0.2667 0.0250 -0.0286 0.0562 64 HIS A CD2 +517 C CE1 . HIS A 64 ? 0.1754 0.2634 0.2797 0.0213 -0.0308 0.0606 64 HIS A CE1 +518 N NE2 . HIS A 64 ? 0.1810 0.2667 0.2742 0.0237 -0.0311 0.0595 64 HIS A NE2 +519 N N . ASN A 65 ? 0.1421 0.2078 0.2157 0.0217 -0.0274 0.0433 65 ASN A N +520 C CA . ASN A 65 ? 0.1553 0.2168 0.2150 0.0231 -0.0285 0.0418 65 ASN A CA +521 C C . ASN A 65 ? 0.1613 0.2173 0.2150 0.0229 -0.0272 0.0373 65 ASN A C +522 O O . ASN A 65 ? 0.1761 0.2288 0.2198 0.0247 -0.0271 0.0365 65 ASN A O +523 C CB . ASN A 65 ? 0.1695 0.2287 0.2218 0.0213 -0.0315 0.0422 65 ASN A CB +524 C CG . ASN A 65 ? 0.2148 0.2782 0.2691 0.0212 -0.0336 0.0470 65 ASN A CG +525 O OD1 . ASN A 65 ? 0.2319 0.2968 0.2893 0.0182 -0.0363 0.0491 65 ASN A OD1 +526 N ND2 . ASN A 65 ? 0.2177 0.2836 0.2708 0.0243 -0.0325 0.0495 65 ASN A ND2 +527 N N . PHE A 66 ? 0.1497 0.2042 0.2089 0.0208 -0.0259 0.0348 66 PHE A N +528 C CA . PHE A 66 ? 0.1500 0.1993 0.2036 0.0201 -0.0250 0.0308 66 PHE A CA +529 C C . PHE A 66 ? 0.1633 0.2130 0.2202 0.0205 -0.0239 0.0311 66 PHE A C +530 O O . PHE A 66 ? 0.1783 0.2277 0.2423 0.0190 -0.0227 0.0309 66 PHE A O +531 C CB . PHE A 66 ? 0.1409 0.1871 0.1969 0.0175 -0.0240 0.0280 66 PHE A CB +532 C CG . PHE A 66 ? 0.1481 0.1940 0.2013 0.0164 -0.0260 0.0284 66 PHE A CG +533 C CD1 . PHE A 66 ? 0.1628 0.2043 0.2053 0.0161 -0.0275 0.0261 66 PHE A CD1 +534 C CD2 . PHE A 66 ? 0.1524 0.2022 0.2140 0.0153 -0.0266 0.0318 66 PHE A CD2 +535 C CE1 . PHE A 66 ? 0.1717 0.2122 0.2112 0.0143 -0.0302 0.0269 66 PHE A CE1 +536 C CE2 . PHE A 66 ? 0.1617 0.2114 0.2212 0.0134 -0.0295 0.0333 66 PHE A CE2 +537 C CZ . PHE A 66 ? 0.1615 0.2061 0.2093 0.0127 -0.0316 0.0307 66 PHE A CZ +538 N N . LEU A 67 ? 0.1528 0.2026 0.2045 0.0223 -0.0242 0.0323 67 LEU A N +539 C CA . LEU A 67 ? 0.1549 0.2058 0.2102 0.0223 -0.0241 0.0341 67 LEU A CA +540 C C . LEU A 67 ? 0.1556 0.2011 0.2063 0.0197 -0.0242 0.0307 67 LEU A C +541 O O . LEU A 67 ? 0.1556 0.1989 0.1989 0.0204 -0.0242 0.0295 67 LEU A O +542 C CB . LEU A 67 ? 0.1694 0.2240 0.2231 0.0259 -0.0240 0.0387 67 LEU A CB +543 C CG . LEU A 67 ? 0.2040 0.2634 0.2603 0.0286 -0.0238 0.0424 67 LEU A CG +544 C CD1 . LEU A 67 ? 0.2174 0.2792 0.2706 0.0330 -0.0225 0.0471 67 LEU A CD1 +545 C CD2 . LEU A 67 ? 0.2184 0.2820 0.2861 0.0273 -0.0243 0.0444 67 LEU A CD2 +546 N N . VAL A 68 ? 0.1411 0.1836 0.1954 0.0166 -0.0241 0.0291 68 VAL A N +547 C CA . VAL A 68 ? 0.1470 0.1832 0.1958 0.0135 -0.0243 0.0257 68 VAL A CA +548 C C . VAL A 68 ? 0.1559 0.1913 0.2065 0.0113 -0.0262 0.0282 68 VAL A C +549 O O . VAL A 68 ? 0.1585 0.1941 0.2148 0.0103 -0.0265 0.0298 68 VAL A O +550 C CB . VAL A 68 ? 0.1612 0.1918 0.2099 0.0114 -0.0221 0.0215 68 VAL A CB +551 C CG1 . VAL A 68 ? 0.1670 0.1902 0.2084 0.0082 -0.0220 0.0178 68 VAL A CG1 +552 C CG2 . VAL A 68 ? 0.1702 0.2028 0.2190 0.0132 -0.0210 0.0205 68 VAL A CG2 +553 N N . GLN A 69 ? 0.1602 0.1952 0.2065 0.0104 -0.0278 0.0294 69 GLN A N +554 C CA . GLN A 69 ? 0.1772 0.2122 0.2259 0.0077 -0.0307 0.0333 69 GLN A CA +555 C C . GLN A 69 ? 0.1946 0.2232 0.2361 0.0033 -0.0323 0.0309 69 GLN A C +556 O O . GLN A 69 ? 0.1901 0.2187 0.2267 0.0043 -0.0316 0.0296 69 GLN A O +557 C CB . GLN A 69 ? 0.1963 0.2396 0.2497 0.0114 -0.0313 0.0402 69 GLN A CB +558 C CG . GLN A 69 ? 0.2373 0.2833 0.2968 0.0091 -0.0347 0.0466 69 GLN A CG +559 C CD . GLN A 69 ? 0.2773 0.3317 0.3418 0.0139 -0.0339 0.0540 69 GLN A CD +560 O OE1 . GLN A 69 ? 0.2862 0.3444 0.3514 0.0190 -0.0309 0.0547 69 GLN A OE1 +561 N NE2 . GLN A 69 ? 0.2905 0.3473 0.3582 0.0121 -0.0365 0.0602 69 GLN A NE2 +562 N N . ALA A 70 ? 0.2201 0.2421 0.2599 -0.0017 -0.0344 0.0301 70 ALA A N +563 C CA . ALA A 70 ? 0.2502 0.2644 0.2818 -0.0071 -0.0366 0.0280 70 ALA A CA +564 C C . ALA A 70 ? 0.2762 0.2930 0.3110 -0.0104 -0.0418 0.0350 70 ALA A C +565 O O . ALA A 70 ? 0.2803 0.2952 0.3183 -0.0131 -0.0442 0.0374 70 ALA A O +566 C CB . ALA A 70 ? 0.2561 0.2590 0.2818 -0.0106 -0.0351 0.0226 70 ALA A CB +567 N N . GLY A 71 ? 0.2932 0.3155 0.3291 -0.0097 -0.0433 0.0393 71 GLY A N +568 C CA . GLY A 71 ? 0.3039 0.3312 0.3459 -0.0122 -0.0480 0.0480 71 GLY A CA +569 C C . GLY A 71 ? 0.3035 0.3394 0.3562 -0.0076 -0.0472 0.0536 71 GLY A C +570 O O . GLY A 71 ? 0.3133 0.3550 0.3687 -0.0011 -0.0430 0.0534 71 GLY A O +571 N N A ASN A 72 ? 0.2967 0.3324 0.3544 -0.0112 -0.0512 0.0581 72 ASN A N +572 N N B ASN A 72 ? 0.2996 0.3356 0.3576 -0.0112 -0.0512 0.0583 72 ASN A N +573 C CA A ASN A 72 ? 0.2894 0.3333 0.3579 -0.0072 -0.0506 0.0637 72 ASN A CA +574 C CA B ASN A 72 ? 0.2953 0.3396 0.3641 -0.0070 -0.0505 0.0639 72 ASN A CA +575 C C A ASN A 72 ? 0.2844 0.3241 0.3527 -0.0065 -0.0484 0.0581 72 ASN A C +576 C C B ASN A 72 ? 0.2858 0.3261 0.3550 -0.0067 -0.0489 0.0590 72 ASN A C +577 O O A ASN A 72 ? 0.2848 0.3311 0.3618 -0.0030 -0.0476 0.0620 72 ASN A O +578 O O B ASN A 72 ? 0.2853 0.3318 0.3635 -0.0041 -0.0489 0.0637 72 ASN A O +579 C CB A ASN A 72 ? 0.3023 0.3498 0.3786 -0.0113 -0.0566 0.0734 72 ASN A CB +580 C CB B ASN A 72 ? 0.3169 0.3666 0.3945 -0.0100 -0.0560 0.0746 72 ASN A CB +581 C CG A ASN A 72 ? 0.3301 0.3891 0.4194 -0.0061 -0.0557 0.0819 72 ASN A CG +582 C CG B ASN A 72 ? 0.3733 0.4141 0.4471 -0.0192 -0.0627 0.0749 72 ASN A CG +583 O OD1 A ASN A 72 ? 0.3382 0.4048 0.4309 0.0010 -0.0511 0.0846 72 ASN A OD1 +584 O OD1 B ASN A 72 ? 0.3977 0.4295 0.4666 -0.0221 -0.0629 0.0691 72 ASN A OD1 +585 N ND2 A ASN A 72 ? 0.3352 0.3945 0.4310 -0.0093 -0.0598 0.0863 72 ASN A ND2 +586 N ND2 B ASN A 72 ? 0.3798 0.4222 0.4556 -0.0241 -0.0683 0.0824 72 ASN A ND2 +587 N N A VAL A 73 ? 0.2756 0.3045 0.3347 -0.0096 -0.0471 0.0497 73 VAL A N +588 N N B VAL A 73 ? 0.2733 0.3034 0.3335 -0.0091 -0.0471 0.0504 73 VAL A N +589 C CA A VAL A 73 ? 0.2687 0.2933 0.3288 -0.0090 -0.0446 0.0455 73 VAL A CA +590 C CA B VAL A 73 ? 0.2623 0.2875 0.3231 -0.0089 -0.0448 0.0461 73 VAL A CA +591 C C A VAL A 73 ? 0.2429 0.2701 0.3030 -0.0034 -0.0389 0.0407 73 VAL A C +592 C C B VAL A 73 ? 0.2460 0.2730 0.3061 -0.0036 -0.0390 0.0408 73 VAL A C +593 O O A VAL A 73 ? 0.2341 0.2588 0.2876 -0.0027 -0.0367 0.0363 73 VAL A O +594 O O B VAL A 73 ? 0.2468 0.2705 0.2999 -0.0032 -0.0369 0.0361 73 VAL A O +595 C CB A VAL A 73 ? 0.2938 0.3038 0.3449 -0.0155 -0.0460 0.0407 73 VAL A CB +596 C CB B VAL A 73 ? 0.2769 0.2878 0.3287 -0.0159 -0.0468 0.0418 73 VAL A CB +597 C CG1 A VAL A 73 ? 0.3138 0.3149 0.3532 -0.0169 -0.0432 0.0334 73 VAL A CG1 +598 C CG1 B VAL A 73 ? 0.2857 0.2897 0.3364 -0.0147 -0.0422 0.0361 73 VAL A CG1 +599 C CG2 A VAL A 73 ? 0.3009 0.3074 0.3558 -0.0147 -0.0435 0.0388 73 VAL A CG2 +600 C CG2 B VAL A 73 ? 0.2809 0.2903 0.3351 -0.0215 -0.0535 0.0482 73 VAL A CG2 +601 N N . GLN A 74 ? 0.2292 0.2618 0.2972 0.0002 -0.0370 0.0423 74 GLN A N +602 C CA . GLN A 74 ? 0.2079 0.2433 0.2770 0.0046 -0.0327 0.0391 74 GLN A CA +603 C C . GLN A 74 ? 0.2000 0.2265 0.2658 0.0028 -0.0296 0.0331 74 GLN A C +604 O O . GLN A 74 ? 0.2053 0.2250 0.2715 -0.0002 -0.0298 0.0324 74 GLN A O +605 C CB . GLN A 74 ? 0.2017 0.2464 0.2807 0.0086 -0.0322 0.0440 74 GLN A CB +606 C CG . GLN A 74 ? 0.2025 0.2529 0.2815 0.0135 -0.0293 0.0433 74 GLN A CG +607 C CD . GLN A 74 ? 0.2277 0.2810 0.3015 0.0159 -0.0294 0.0447 74 GLN A CD +608 O OE1 . GLN A 74 ? 0.2352 0.2901 0.3093 0.0154 -0.0314 0.0487 74 GLN A OE1 +609 N NE2 . GLN A 74 ? 0.2313 0.2853 0.3008 0.0187 -0.0273 0.0422 74 GLN A NE2 +610 N N . LEU A 75 ? 0.1864 0.2124 0.2489 0.0049 -0.0264 0.0291 75 LEU A N +611 C CA . LEU A 75 ? 0.1892 0.2081 0.2503 0.0042 -0.0224 0.0246 75 LEU A CA +612 C C . LEU A 75 ? 0.1778 0.2034 0.2479 0.0079 -0.0199 0.0263 75 LEU A C +613 O O . LEU A 75 ? 0.1848 0.2187 0.2575 0.0108 -0.0208 0.0287 75 LEU A O +614 C CB . LEU A 75 ? 0.2020 0.2155 0.2545 0.0034 -0.0207 0.0199 75 LEU A CB +615 C CG . LEU A 75 ? 0.2354 0.2421 0.2782 -0.0007 -0.0233 0.0183 75 LEU A CG +616 C CD1 . LEU A 75 ? 0.2468 0.2484 0.2818 -0.0012 -0.0210 0.0136 75 LEU A CD1 +617 C CD2 . LEU A 75 ? 0.2622 0.2593 0.3016 -0.0052 -0.0245 0.0178 75 LEU A CD2 +618 N N . ARG A 76 ? 0.1580 0.1790 0.2321 0.0075 -0.0166 0.0253 76 ARG A N +619 C CA . ARG A 76 ? 0.1483 0.1758 0.2325 0.0104 -0.0142 0.0278 76 ARG A CA +620 C C . ARG A 76 ? 0.1556 0.1822 0.2391 0.0115 -0.0110 0.0257 76 ARG A C +621 O O . ARG A 76 ? 0.1705 0.1882 0.2501 0.0103 -0.0073 0.0224 76 ARG A O +622 C CB . ARG A 76 ? 0.1542 0.1774 0.2447 0.0098 -0.0118 0.0289 76 ARG A CB +623 C CG . ARG A 76 ? 0.1544 0.1859 0.2574 0.0127 -0.0099 0.0329 76 ARG A CG +624 C CD . ARG A 76 ? 0.1620 0.1890 0.2716 0.0122 -0.0073 0.0342 76 ARG A CD +625 N NE . ARG A 76 ? 0.1758 0.2025 0.2848 0.0104 -0.0115 0.0359 76 ARG A NE +626 C CZ . ARG A 76 ? 0.1826 0.2198 0.2994 0.0120 -0.0148 0.0409 76 ARG A CZ +627 N NH1 . ARG A 76 ? 0.1608 0.2087 0.2855 0.0151 -0.0144 0.0443 76 ARG A NH1 +628 N NH2 . ARG A 76 ? 0.1781 0.2151 0.2948 0.0101 -0.0186 0.0432 76 ARG A NH2 +629 N N . VAL A 77 ? 0.1442 0.1795 0.2310 0.0136 -0.0124 0.0281 77 VAL A N +630 C CA . VAL A 77 ? 0.1462 0.1822 0.2336 0.0142 -0.0106 0.0274 77 VAL A CA +631 C C . VAL A 77 ? 0.1473 0.1863 0.2465 0.0153 -0.0074 0.0309 77 VAL A C +632 O O . VAL A 77 ? 0.1462 0.1929 0.2530 0.0164 -0.0091 0.0352 77 VAL A O +633 C CB . VAL A 77 ? 0.1438 0.1855 0.2267 0.0150 -0.0144 0.0283 77 VAL A CB +634 C CG1 . VAL A 77 ? 0.1508 0.1931 0.2347 0.0148 -0.0136 0.0284 77 VAL A CG1 +635 C CG2 . VAL A 77 ? 0.1555 0.1939 0.2278 0.0143 -0.0166 0.0254 77 VAL A CG2 +636 N N . ILE A 78 ? 0.1447 0.1776 0.2457 0.0151 -0.0024 0.0296 78 ILE A N +637 C CA . ILE A 78 ? 0.1458 0.1813 0.2595 0.0165 0.0018 0.0339 78 ILE A CA +638 C C . ILE A 78 ? 0.1428 0.1822 0.2617 0.0169 0.0029 0.0366 78 ILE A C +639 O O . ILE A 78 ? 0.1463 0.1887 0.2773 0.0181 0.0065 0.0414 78 ILE A O +640 C CB . ILE A 78 ? 0.1617 0.1865 0.2757 0.0167 0.0081 0.0319 78 ILE A CB +641 C CG1 . ILE A 78 ? 0.1846 0.1983 0.2883 0.0159 0.0119 0.0270 78 ILE A CG1 +642 C CG2 . ILE A 78 ? 0.1700 0.1918 0.2805 0.0156 0.0057 0.0305 78 ILE A CG2 +643 C CD1 . ILE A 78 ? 0.2057 0.2061 0.3078 0.0164 0.0196 0.0251 78 ILE A CD1 +644 N N . GLY A 79 ? 0.1401 0.1801 0.2510 0.0159 -0.0006 0.0346 79 GLY A N +645 C CA . GLY A 79 ? 0.1374 0.1814 0.2527 0.0155 -0.0010 0.0377 79 GLY A CA +646 C C . GLY A 79 ? 0.1422 0.1855 0.2460 0.0141 -0.0057 0.0345 79 GLY A C +647 O O . GLY A 79 ? 0.1454 0.1836 0.2384 0.0138 -0.0065 0.0295 79 GLY A O +648 N N . HIS A 80 ? 0.1366 0.1849 0.2427 0.0130 -0.0091 0.0379 80 HIS A N +649 C CA . HIS A 80 ? 0.1385 0.1849 0.2335 0.0116 -0.0132 0.0350 80 HIS A CA +650 C C . HIS A 80 ? 0.1440 0.1931 0.2443 0.0101 -0.0145 0.0390 80 HIS A C +651 O O . HIS A 80 ? 0.1452 0.2003 0.2570 0.0095 -0.0151 0.0455 80 HIS A O +652 C CB . HIS A 80 ? 0.1439 0.1924 0.2301 0.0114 -0.0188 0.0341 80 HIS A CB +653 C CG . HIS A 80 ? 0.1623 0.2172 0.2534 0.0105 -0.0229 0.0397 80 HIS A CG +654 N ND1 . HIS A 80 ? 0.1682 0.2281 0.2678 0.0115 -0.0222 0.0432 80 HIS A ND1 +655 C CD2 . HIS A 80 ? 0.1778 0.2344 0.2659 0.0082 -0.0280 0.0424 80 HIS A CD2 +656 C CE1 . HIS A 80 ? 0.1764 0.2412 0.2779 0.0098 -0.0268 0.0480 80 HIS A CE1 +657 N NE2 . HIS A 80 ? 0.1818 0.2442 0.2758 0.0076 -0.0306 0.0477 80 HIS A NE2 +658 N N . SER A 81 ? 0.1420 0.1870 0.2347 0.0092 -0.0151 0.0359 81 SER A N +659 C CA . SER A 81 ? 0.1398 0.1873 0.2373 0.0074 -0.0171 0.0401 81 SER A CA +660 C C . SER A 81 ? 0.1430 0.1863 0.2279 0.0059 -0.0208 0.0359 81 SER A C +661 O O . SER A 81 ? 0.1548 0.1929 0.2294 0.0069 -0.0196 0.0299 81 SER A O +662 C CB . SER A 81 ? 0.1600 0.2070 0.2686 0.0087 -0.0103 0.0429 81 SER A CB +663 O OG . SER A 81 ? 0.2105 0.2497 0.3114 0.0102 -0.0053 0.0368 81 SER A OG +664 N N A MET A 82 ? 0.1375 0.1829 0.2230 0.0032 -0.0258 0.0397 82 MET A N +665 N N B MET A 82 ? 0.1341 0.1796 0.2199 0.0033 -0.0256 0.0397 82 MET A N +666 C CA A MET A 82 ? 0.1484 0.1893 0.2223 0.0016 -0.0295 0.0362 82 MET A CA +667 C CA B MET A 82 ? 0.1415 0.1826 0.2160 0.0016 -0.0294 0.0364 82 MET A CA +668 C C A MET A 82 ? 0.1526 0.1934 0.2328 0.0010 -0.0272 0.0382 82 MET A C +669 C C B MET A 82 ? 0.1480 0.1888 0.2288 0.0012 -0.0266 0.0382 82 MET A C +670 O O A MET A 82 ? 0.1586 0.2045 0.2514 -0.0002 -0.0274 0.0453 82 MET A O +671 O O B MET A 82 ? 0.1511 0.1969 0.2453 0.0005 -0.0257 0.0451 82 MET A O +672 C CB A MET A 82 ? 0.1567 0.1980 0.2242 -0.0015 -0.0375 0.0388 82 MET A CB +673 C CB B MET A 82 ? 0.1426 0.1844 0.2116 -0.0017 -0.0375 0.0395 82 MET A CB +674 C CG A MET A 82 ? 0.1915 0.2267 0.2458 -0.0031 -0.0413 0.0351 82 MET A CG +675 C CG B MET A 82 ? 0.1675 0.2033 0.2234 -0.0034 -0.0415 0.0359 82 MET A CG +676 S SD A MET A 82 ? 0.2388 0.2711 0.2825 -0.0073 -0.0506 0.0379 82 MET A SD +677 S SD B MET A 82 ? 0.1780 0.2095 0.2192 -0.0061 -0.0495 0.0362 82 MET A SD +678 C CE A MET A 82 ? 0.2376 0.2679 0.2717 -0.0043 -0.0496 0.0344 82 MET A CE +679 C CE B MET A 82 ? 0.1267 0.1648 0.1803 -0.0108 -0.0552 0.0463 82 MET A CE +680 N N . GLN A 83 ? 0.1542 0.1897 0.2265 0.0019 -0.0248 0.0327 83 GLN A N +681 C CA . GLN A 83 ? 0.1533 0.1881 0.2299 0.0016 -0.0223 0.0341 83 GLN A CA +682 C C . GLN A 83 ? 0.1433 0.1744 0.2080 -0.0004 -0.0275 0.0308 83 GLN A C +683 O O . GLN A 83 ? 0.1526 0.1789 0.2062 0.0006 -0.0269 0.0245 83 GLN A O +684 C CB . GLN A 83 ? 0.1894 0.2200 0.2662 0.0045 -0.0140 0.0304 83 GLN A CB +685 C CG . GLN A 83 ? 0.2466 0.2763 0.3275 0.0046 -0.0109 0.0324 83 GLN A CG +686 C CD . GLN A 83 ? 0.3106 0.3341 0.3886 0.0072 -0.0026 0.0284 83 GLN A CD +687 O OE1 . GLN A 83 ? 0.3192 0.3381 0.3906 0.0083 0.0001 0.0235 83 GLN A OE1 +688 N NE2 . GLN A 83 ? 0.3279 0.3504 0.4102 0.0079 0.0015 0.0307 83 GLN A NE2 +689 N N . ASN A 84 ? 0.1329 0.1659 0.1999 -0.0036 -0.0333 0.0354 84 ASN A N +690 C CA . ASN A 84 ? 0.1351 0.1634 0.1902 -0.0059 -0.0388 0.0327 84 ASN A CA +691 C C . ASN A 84 ? 0.1344 0.1580 0.1748 -0.0053 -0.0415 0.0273 84 ASN A C +692 O O . ASN A 84 ? 0.1453 0.1703 0.1853 -0.0060 -0.0442 0.0295 84 ASN A O +693 C CB . ASN A 84 ? 0.1455 0.1714 0.1997 -0.0050 -0.0352 0.0300 84 ASN A CB +694 C CG . ASN A 84 ? 0.1817 0.2124 0.2509 -0.0050 -0.0321 0.0365 84 ASN A CG +695 O OD1 . ASN A 84 ? 0.1987 0.2336 0.2761 -0.0080 -0.0368 0.0437 84 ASN A OD1 +696 N ND2 . ASN A 84 ? 0.1855 0.2154 0.2584 -0.0019 -0.0241 0.0348 84 ASN A ND2 +697 N N . CYS A 85 ? 0.1317 0.1500 0.1611 -0.0038 -0.0400 0.0211 85 CYS A N +698 C CA . CYS A 85 ? 0.1382 0.1524 0.1553 -0.0026 -0.0414 0.0172 85 CYS A CA +699 C C . CYS A 85 ? 0.1403 0.1555 0.1577 0.0007 -0.0364 0.0141 85 CYS A C +700 O O . CYS A 85 ? 0.1484 0.1605 0.1564 0.0022 -0.0366 0.0113 85 CYS A O +701 C CB . CYS A 85 ? 0.1510 0.1586 0.1558 -0.0033 -0.0439 0.0138 85 CYS A CB +702 S SG . CYS A 85 ? 0.1812 0.1858 0.1834 -0.0081 -0.0513 0.0176 85 CYS A SG +703 N N . VAL A 86 ? 0.1354 0.1543 0.1631 0.0017 -0.0318 0.0152 86 VAL A N +704 C CA A VAL A 86 ? 0.1452 0.1642 0.1728 0.0040 -0.0279 0.0128 86 VAL A CA +705 C CA B VAL A 86 ? 0.1442 0.1632 0.1719 0.0040 -0.0279 0.0127 86 VAL A CA +706 C C . VAL A 86 ? 0.1483 0.1718 0.1854 0.0047 -0.0267 0.0163 86 VAL A C +707 O O . VAL A 86 ? 0.1515 0.1785 0.1978 0.0036 -0.0272 0.0209 86 VAL A O +708 C CB A VAL A 86 ? 0.1624 0.1787 0.1895 0.0047 -0.0232 0.0093 86 VAL A CB +709 C CB B VAL A 86 ? 0.1550 0.1713 0.1828 0.0044 -0.0232 0.0096 86 VAL A CB +710 C CG1 A VAL A 86 ? 0.1797 0.1922 0.1975 0.0041 -0.0245 0.0060 86 VAL A CG1 +711 C CG1 B VAL A 86 ? 0.1607 0.1764 0.1916 0.0057 -0.0188 0.0085 86 VAL A CG1 +712 C CG2 A VAL A 86 ? 0.1683 0.1855 0.2049 0.0046 -0.0191 0.0115 86 VAL A CG2 +713 C CG2 B VAL A 86 ? 0.1676 0.1800 0.1849 0.0042 -0.0245 0.0058 86 VAL A CG2 +714 N N . LEU A 87 ? 0.1444 0.1682 0.1797 0.0063 -0.0256 0.0150 87 LEU A N +715 C CA . LEU A 87 ? 0.1464 0.1742 0.1906 0.0072 -0.0239 0.0179 87 LEU A CA +716 C C . LEU A 87 ? 0.1383 0.1635 0.1851 0.0082 -0.0185 0.0155 87 LEU A C +717 O O . LEU A 87 ? 0.1425 0.1635 0.1819 0.0082 -0.0176 0.0116 87 LEU A O +718 C CB . LEU A 87 ? 0.1632 0.1927 0.2037 0.0084 -0.0262 0.0185 87 LEU A CB +719 C CG . LEU A 87 ? 0.1963 0.2262 0.2314 0.0075 -0.0312 0.0207 87 LEU A CG +720 C CD1 . LEU A 87 ? 0.2043 0.2347 0.2342 0.0095 -0.0320 0.0209 87 LEU A CD1 +721 C CD2 . LEU A 87 ? 0.2162 0.2502 0.2602 0.0053 -0.0333 0.0259 87 LEU A CD2 +722 N N . LYS A 88 ? 0.1328 0.1598 0.1898 0.0087 -0.0150 0.0182 88 LYS A N +723 C CA . LYS A 88 ? 0.1334 0.1560 0.1921 0.0095 -0.0095 0.0163 88 LYS A CA +724 C C . LYS A 88 ? 0.1333 0.1590 0.1978 0.0105 -0.0093 0.0185 88 LYS A C +725 O O . LYS A 88 ? 0.1402 0.1711 0.2146 0.0109 -0.0093 0.0232 88 LYS A O +726 C CB . LYS A 88 ? 0.1473 0.1683 0.2136 0.0100 -0.0042 0.0184 88 LYS A CB +727 C CG . LYS A 88 ? 0.2015 0.2189 0.2621 0.0092 -0.0036 0.0161 88 LYS A CG +728 C CD . LYS A 88 ? 0.2553 0.2703 0.3230 0.0103 0.0028 0.0185 88 LYS A CD +729 C CE . LYS A 88 ? 0.3066 0.3292 0.3880 0.0106 0.0021 0.0258 88 LYS A CE +730 N NZ . LYS A 88 ? 0.3299 0.3515 0.4180 0.0116 0.0074 0.0291 88 LYS A NZ +731 N N . LEU A 89 ? 0.1301 0.1534 0.1893 0.0106 -0.0097 0.0159 89 LEU A N +732 C CA . LEU A 89 ? 0.1294 0.1554 0.1937 0.0114 -0.0098 0.0179 89 LEU A CA +733 C C . LEU A 89 ? 0.1356 0.1549 0.2012 0.0113 -0.0048 0.0163 89 LEU A C +734 O O . LEU A 89 ? 0.1483 0.1607 0.2054 0.0100 -0.0042 0.0125 89 LEU A O +735 C CB . LEU A 89 ? 0.1331 0.1607 0.1908 0.0116 -0.0137 0.0171 89 LEU A CB +736 C CG . LEU A 89 ? 0.1403 0.1710 0.1923 0.0120 -0.0178 0.0176 89 LEU A CG +737 C CD1 . LEU A 89 ? 0.1515 0.1830 0.1976 0.0129 -0.0200 0.0174 89 LEU A CD1 +738 C CD2 . LEU A 89 ? 0.1466 0.1827 0.2044 0.0123 -0.0197 0.0217 89 LEU A CD2 +739 N N . LYS A 90 ? 0.1274 0.1477 0.2030 0.0124 -0.0010 0.0194 90 LYS A N +740 C CA . LYS A 90 ? 0.1365 0.1485 0.2125 0.0126 0.0046 0.0179 90 LYS A CA +741 C C . LYS A 90 ? 0.1366 0.1485 0.2118 0.0120 0.0022 0.0178 90 LYS A C +742 O O . LYS A 90 ? 0.1371 0.1575 0.2191 0.0129 -0.0008 0.0213 90 LYS A O +743 C CB . LYS A 90 ? 0.1591 0.1726 0.2476 0.0146 0.0101 0.0223 90 LYS A CB +744 C CG . LYS A 90 ? 0.2237 0.2255 0.3100 0.0152 0.0174 0.0202 90 LYS A CG +745 C CD . LYS A 90 ? 0.3041 0.3069 0.4037 0.0179 0.0242 0.0252 90 LYS A CD +746 C CE . LYS A 90 ? 0.3769 0.3655 0.4717 0.0188 0.0320 0.0225 90 LYS A CE +747 N NZ . LYS A 90 ? 0.4068 0.3943 0.5138 0.0222 0.0407 0.0276 90 LYS A NZ +748 N N . VAL A 91 ? 0.1419 0.1445 0.2081 0.0102 0.0029 0.0140 91 VAL A N +749 C CA . VAL A 91 ? 0.1498 0.1516 0.2152 0.0089 0.0001 0.0144 91 VAL A CA +750 C C . VAL A 91 ? 0.1577 0.1489 0.2230 0.0084 0.0052 0.0133 91 VAL A C +751 O O . VAL A 91 ? 0.1654 0.1478 0.2276 0.0088 0.0111 0.0113 91 VAL A O +752 C CB . VAL A 91 ? 0.1528 0.1533 0.2083 0.0064 -0.0051 0.0124 91 VAL A CB +753 C CG1 . VAL A 91 ? 0.1531 0.1640 0.2097 0.0079 -0.0093 0.0143 91 VAL A CG1 +754 C CG2 . VAL A 91 ? 0.1613 0.1508 0.2049 0.0039 -0.0033 0.0078 91 VAL A CG2 +755 N N . ASP A 92 ? 0.1643 0.1553 0.2322 0.0075 0.0033 0.0149 92 ASP A N +756 C CA . ASP A 92 ? 0.1792 0.1588 0.2466 0.0069 0.0081 0.0140 92 ASP A CA +757 C C . ASP A 92 ? 0.1994 0.1631 0.2511 0.0028 0.0081 0.0092 92 ASP A C +758 O O . ASP A 92 ? 0.2231 0.1741 0.2708 0.0018 0.0121 0.0077 92 ASP A O +759 C CB . ASP A 92 ? 0.1931 0.1787 0.2710 0.0077 0.0064 0.0181 92 ASP A CB +760 C CG . ASP A 92 ? 0.2553 0.2417 0.3296 0.0047 -0.0003 0.0188 92 ASP A CG +761 O OD1 . ASP A 92 ? 0.2611 0.2460 0.3260 0.0022 -0.0045 0.0169 92 ASP A OD1 +762 O OD2 . ASP A 92 ? 0.2915 0.2806 0.3734 0.0049 -0.0014 0.0220 92 ASP A OD2 +763 N N . THR A 93 ? 0.1939 0.1574 0.2361 0.0001 0.0033 0.0071 93 THR A N +764 C CA . THR A 93 ? 0.2104 0.1596 0.2373 -0.0047 0.0018 0.0033 93 THR A CA +765 C C . THR A 93 ? 0.2101 0.1555 0.2272 -0.0055 0.0029 -0.0002 93 THR A C +766 O O . THR A 93 ? 0.2088 0.1651 0.2291 -0.0043 -0.0001 0.0009 93 THR A O +767 C CB . THR A 93 ? 0.2348 0.1888 0.2611 -0.0082 -0.0067 0.0059 93 THR A CB +768 O OG1 . THR A 93 ? 0.2512 0.2085 0.2869 -0.0075 -0.0075 0.0093 93 THR A OG1 +769 C CG2 . THR A 93 ? 0.2512 0.1918 0.2621 -0.0145 -0.0103 0.0033 93 THR A CG2 +770 N N . ALA A 94 ? 0.2136 0.1424 0.2181 -0.0075 0.0076 -0.0044 94 ALA A N +771 C CA . ALA A 94 ? 0.2209 0.1446 0.2147 -0.0087 0.0087 -0.0077 94 ALA A CA +772 C C . ALA A 94 ? 0.2124 0.1362 0.1976 -0.0140 0.0003 -0.0079 94 ALA A C +773 O O . ALA A 94 ? 0.2162 0.1342 0.1968 -0.0183 -0.0041 -0.0072 94 ALA A O +774 C CB . ALA A 94 ? 0.2408 0.1451 0.2218 -0.0095 0.0164 -0.0119 94 ALA A CB +775 N N . ASN A 95 ? 0.1950 0.1255 0.1786 -0.0141 -0.0022 -0.0083 95 ASN A N +776 C CA . ASN A 95 ? 0.1934 0.1243 0.1698 -0.0190 -0.0096 -0.0076 95 ASN A CA +777 C C . ASN A 95 ? 0.2259 0.1381 0.1848 -0.0249 -0.0097 -0.0111 95 ASN A C +778 O O . ASN A 95 ? 0.2395 0.1421 0.1889 -0.0248 -0.0045 -0.0150 95 ASN A O +779 C CB . ASN A 95 ? 0.1754 0.1158 0.1533 -0.0175 -0.0111 -0.0075 95 ASN A CB +780 C CG . ASN A 95 ? 0.1885 0.1314 0.1617 -0.0219 -0.0184 -0.0054 95 ASN A CG +781 O OD1 . ASN A 95 ? 0.1915 0.1291 0.1601 -0.0268 -0.0232 -0.0037 95 ASN A OD1 +782 N ND2 . ASN A 95 ? 0.1933 0.1446 0.1685 -0.0204 -0.0197 -0.0048 95 ASN A ND2 +783 N N . PRO A 96 ? 0.2378 0.1442 0.1916 -0.0304 -0.0156 -0.0095 96 PRO A N +784 C CA . PRO A 96 ? 0.2611 0.1476 0.1956 -0.0371 -0.0165 -0.0128 96 PRO A CA +785 C C . PRO A 96 ? 0.2771 0.1609 0.2007 -0.0411 -0.0196 -0.0140 96 PRO A C +786 O O . PRO A 96 ? 0.3125 0.1787 0.2182 -0.0458 -0.0185 -0.0178 96 PRO A O +787 C CB . PRO A 96 ? 0.2739 0.1579 0.2084 -0.0424 -0.0239 -0.0091 96 PRO A CB +788 C CG . PRO A 96 ? 0.2656 0.1705 0.2179 -0.0394 -0.0285 -0.0032 96 PRO A CG +789 C CD . PRO A 96 ? 0.2328 0.1500 0.1975 -0.0311 -0.0220 -0.0040 96 PRO A CD +790 N N A LYS A 97 ? 0.2603 0.1608 0.1938 -0.0391 -0.0232 -0.0109 97 LYS A N +791 N N B LYS A 97 ? 0.2564 0.1568 0.1898 -0.0392 -0.0232 -0.0109 97 LYS A N +792 C CA A LYS A 97 ? 0.2636 0.1643 0.1896 -0.0422 -0.0261 -0.0113 97 LYS A CA +793 C CA B LYS A 97 ? 0.2560 0.1561 0.1815 -0.0424 -0.0262 -0.0113 97 LYS A CA +794 C C A LYS A 97 ? 0.2614 0.1653 0.1889 -0.0368 -0.0193 -0.0146 97 LYS A C +795 C C B LYS A 97 ? 0.2585 0.1605 0.1841 -0.0374 -0.0192 -0.0149 97 LYS A C +796 O O A LYS A 97 ? 0.2606 0.1709 0.1879 -0.0373 -0.0216 -0.0138 97 LYS A O +797 O O B LYS A 97 ? 0.2598 0.1652 0.1823 -0.0387 -0.0213 -0.0148 97 LYS A O +798 C CB A LYS A 97 ? 0.2736 0.1897 0.2095 -0.0434 -0.0339 -0.0050 97 LYS A CB +799 C CB B LYS A 97 ? 0.2533 0.1698 0.1896 -0.0431 -0.0337 -0.0051 97 LYS A CB +800 C CG A LYS A 97 ? 0.3212 0.2347 0.2559 -0.0497 -0.0418 -0.0003 97 LYS A CG +801 C CG B LYS A 97 ? 0.2776 0.1946 0.2165 -0.0478 -0.0409 0.0002 97 LYS A CG +802 C CD A LYS A 97 ? 0.3618 0.2900 0.3060 -0.0508 -0.0487 0.0069 97 LYS A CD +803 C CD B LYS A 97 ? 0.2981 0.2314 0.2485 -0.0476 -0.0472 0.0074 97 LYS A CD +804 C CE A LYS A 97 ? 0.4069 0.3352 0.3536 -0.0564 -0.0565 0.0134 97 LYS A CE +805 C CE B LYS A 97 ? 0.3308 0.2666 0.2870 -0.0513 -0.0538 0.0139 97 LYS A CE +806 N NZ A LYS A 97 ? 0.4286 0.3624 0.3867 -0.0522 -0.0549 0.0151 97 LYS A NZ +807 N NZ B LYS A 97 ? 0.3407 0.2934 0.3103 -0.0497 -0.0582 0.0220 97 LYS A NZ +808 N N . THR A 98 ? 0.2547 0.1549 0.1848 -0.0317 -0.0110 -0.0174 98 THR A N +809 C CA . THR A 98 ? 0.2542 0.1576 0.1867 -0.0270 -0.0048 -0.0195 98 THR A CA +810 C C . THR A 98 ? 0.2842 0.1736 0.1997 -0.0305 -0.0026 -0.0232 98 THR A C +811 O O . THR A 98 ? 0.3148 0.1866 0.2165 -0.0332 0.0009 -0.0263 98 THR A O +812 C CB . THR A 98 ? 0.2523 0.1549 0.1925 -0.0210 0.0037 -0.0202 98 THR A CB +813 O OG1 . THR A 98 ? 0.2326 0.1476 0.1878 -0.0181 0.0015 -0.0166 98 THR A OG1 +814 C CG2 . THR A 98 ? 0.2558 0.1638 0.2009 -0.0164 0.0090 -0.0207 98 THR A CG2 +815 N N . PRO A 99 ? 0.2825 0.1788 0.1980 -0.0308 -0.0048 -0.0229 99 PRO A N +816 C CA . PRO A 99 ? 0.2921 0.1759 0.1916 -0.0340 -0.0026 -0.0262 99 PRO A CA +817 C C . PRO A 99 ? 0.3000 0.1796 0.2001 -0.0284 0.0075 -0.0286 99 PRO A C +818 O O . PRO A 99 ? 0.2949 0.1834 0.2093 -0.0225 0.0117 -0.0271 99 PRO A O +819 C CB . PRO A 99 ? 0.2916 0.1876 0.1950 -0.0354 -0.0086 -0.0239 99 PRO A CB +820 C CG . PRO A 99 ? 0.2906 0.2044 0.2130 -0.0291 -0.0083 -0.0211 99 PRO A CG +821 C CD . PRO A 99 ? 0.2660 0.1807 0.1953 -0.0276 -0.0083 -0.0197 99 PRO A CD +822 N N . LYS A 100 ? 0.3110 0.1775 0.1960 -0.0303 0.0116 -0.0318 100 LYS A N +823 C CA . LYS A 100 ? 0.3088 0.1736 0.1961 -0.0246 0.0211 -0.0328 100 LYS A CA +824 C C . LYS A 100 ? 0.2847 0.1688 0.1873 -0.0214 0.0182 -0.0300 100 LYS A C +825 O O . LYS A 100 ? 0.2856 0.1769 0.1878 -0.0249 0.0106 -0.0290 100 LYS A O +826 C CB . LYS A 100 ? 0.3518 0.2000 0.2196 -0.0274 0.0254 -0.0363 100 LYS A CB +827 C CG . LYS A 100 ? 0.4294 0.2549 0.2793 -0.0297 0.0305 -0.0396 100 LYS A CG +828 C CD . LYS A 100 ? 0.5093 0.3170 0.3371 -0.0332 0.0340 -0.0431 100 LYS A CD +829 C CE . LYS A 100 ? 0.5777 0.3601 0.3843 -0.0365 0.0383 -0.0468 100 LYS A CE +830 N NZ . LYS A 100 ? 0.6311 0.3946 0.4134 -0.0404 0.0413 -0.0503 100 LYS A NZ +831 N N . TYR A 101 ? 0.2722 0.1649 0.1891 -0.0152 0.0233 -0.0279 101 TYR A N +832 C CA . TYR A 101 ? 0.2629 0.1725 0.1935 -0.0127 0.0198 -0.0252 101 TYR A CA +833 C C . TYR A 101 ? 0.2697 0.1834 0.2099 -0.0073 0.0267 -0.0232 101 TYR A C +834 O O . TYR A 101 ? 0.2816 0.1879 0.2224 -0.0042 0.0348 -0.0229 101 TYR A O +835 C CB . TYR A 101 ? 0.2444 0.1674 0.1873 -0.0121 0.0131 -0.0225 101 TYR A CB +836 C CG . TYR A 101 ? 0.2390 0.1652 0.1934 -0.0080 0.0170 -0.0204 101 TYR A CG +837 C CD1 . TYR A 101 ? 0.2457 0.1632 0.1967 -0.0088 0.0191 -0.0212 101 TYR A CD1 +838 C CD2 . TYR A 101 ? 0.2376 0.1754 0.2064 -0.0037 0.0181 -0.0172 101 TYR A CD2 +839 C CE1 . TYR A 101 ? 0.2546 0.1755 0.2170 -0.0049 0.0228 -0.0188 101 TYR A CE1 +840 C CE2 . TYR A 101 ? 0.2398 0.1813 0.2199 -0.0003 0.0212 -0.0144 101 TYR A CE2 +841 C CZ . TYR A 101 ? 0.2577 0.1913 0.2351 -0.0008 0.0236 -0.0152 101 TYR A CZ +842 O OH . TYR A 101 ? 0.2740 0.2112 0.2629 0.0025 0.0269 -0.0122 101 TYR A OH +843 N N . LYS A 102 ? 0.2583 0.1839 0.2065 -0.0062 0.0232 -0.0213 102 LYS A N +844 C CA . LYS A 102 ? 0.2549 0.1875 0.2147 -0.0018 0.0273 -0.0181 102 LYS A CA +845 C C . LYS A 102 ? 0.2427 0.1902 0.2135 -0.0015 0.0200 -0.0157 102 LYS A C +846 O O . LYS A 102 ? 0.2472 0.1982 0.2143 -0.0044 0.0132 -0.0169 102 LYS A O +847 C CB . LYS A 102 ? 0.2879 0.2152 0.2405 -0.0019 0.0314 -0.0190 102 LYS A CB +848 C CG . LYS A 102 ? 0.3730 0.2843 0.3144 -0.0009 0.0408 -0.0209 102 LYS A CG +849 C CD . LYS A 102 ? 0.4398 0.3464 0.3730 -0.0013 0.0439 -0.0217 102 LYS A CD +850 C CE . LYS A 102 ? 0.5043 0.3923 0.4223 -0.0008 0.0534 -0.0241 102 LYS A CE +851 N NZ . LYS A 102 ? 0.5466 0.4297 0.4550 -0.0015 0.0561 -0.0250 102 LYS A NZ +852 N N . PHE A 103 ? 0.2279 0.1836 0.2119 0.0018 0.0214 -0.0118 103 PHE A N +853 C CA . PHE A 103 ? 0.2188 0.1863 0.2111 0.0019 0.0147 -0.0095 103 PHE A CA +854 C C . PHE A 103 ? 0.2271 0.1966 0.2214 0.0025 0.0161 -0.0080 103 PHE A C +855 O O . PHE A 103 ? 0.2426 0.2103 0.2420 0.0050 0.0225 -0.0052 103 PHE A O +856 C CB . PHE A 103 ? 0.2052 0.1803 0.2106 0.0041 0.0140 -0.0053 103 PHE A CB +857 C CG . PHE A 103 ? 0.1993 0.1748 0.2051 0.0038 0.0119 -0.0060 103 PHE A CG +858 C CD1 . PHE A 103 ? 0.2018 0.1733 0.1978 0.0012 0.0087 -0.0095 103 PHE A CD1 +859 C CD2 . PHE A 103 ? 0.1970 0.1780 0.2139 0.0057 0.0123 -0.0022 103 PHE A CD2 +860 C CE1 . PHE A 103 ? 0.2043 0.1770 0.2018 0.0010 0.0065 -0.0093 103 PHE A CE1 +861 C CE2 . PHE A 103 ? 0.1998 0.1817 0.2174 0.0055 0.0102 -0.0025 103 PHE A CE2 +862 C CZ . PHE A 103 ? 0.2000 0.1780 0.2082 0.0033 0.0073 -0.0060 103 PHE A CZ +863 N N . VAL A 104 ? 0.2197 0.1924 0.2100 0.0005 0.0107 -0.0093 104 VAL A N +864 C CA . VAL A 104 ? 0.2324 0.2076 0.2249 0.0008 0.0110 -0.0077 104 VAL A CA +865 C C . VAL A 104 ? 0.2271 0.2109 0.2250 0.0002 0.0039 -0.0060 104 VAL A C +866 O O . VAL A 104 ? 0.2392 0.2249 0.2341 -0.0010 -0.0012 -0.0076 104 VAL A O +867 C CB . VAL A 104 ? 0.2641 0.2325 0.2449 -0.0012 0.0127 -0.0110 104 VAL A CB +868 C CG1 . VAL A 104 ? 0.2834 0.2403 0.2554 -0.0011 0.0197 -0.0131 104 VAL A CG1 +869 C CG2 . VAL A 104 ? 0.2852 0.2550 0.2590 -0.0044 0.0060 -0.0136 104 VAL A CG2 +870 N N . ARG A 105 ? 0.2023 0.1904 0.2078 0.0010 0.0037 -0.0024 105 ARG A N +871 C CA . ARG A 105 ? 0.1946 0.1886 0.2031 -0.0001 -0.0031 -0.0009 105 ARG A CA +872 C C . ARG A 105 ? 0.2048 0.1975 0.2081 -0.0013 -0.0037 -0.0024 105 ARG A C +873 O O . ARG A 105 ? 0.2089 0.2009 0.2150 -0.0006 0.0004 -0.0004 105 ARG A O +874 C CB . ARG A 105 ? 0.1910 0.1905 0.2118 0.0007 -0.0042 0.0050 105 ARG A CB +875 C CG . ARG A 105 ? 0.1958 0.1989 0.2171 -0.0012 -0.0119 0.0062 105 ARG A CG +876 C CD . ARG A 105 ? 0.1972 0.2054 0.2298 -0.0016 -0.0147 0.0126 105 ARG A CD +877 N NE . ARG A 105 ? 0.1998 0.2089 0.2299 -0.0042 -0.0226 0.0133 105 ARG A NE +878 C CZ . ARG A 105 ? 0.2140 0.2221 0.2387 -0.0051 -0.0276 0.0117 105 ARG A CZ +879 N NH1 . ARG A 105 ? 0.1863 0.1938 0.2090 -0.0038 -0.0257 0.0096 105 ARG A NH1 +880 N NH2 . ARG A 105 ? 0.2021 0.2088 0.2227 -0.0074 -0.0342 0.0122 105 ARG A NH2 +881 N N . ILE A 106 ? 0.2107 0.2033 0.2069 -0.0030 -0.0083 -0.0053 106 ILE A N +882 C CA . ILE A 106 ? 0.2279 0.2195 0.2192 -0.0043 -0.0089 -0.0066 106 ILE A CA +883 C C . ILE A 106 ? 0.2356 0.2311 0.2318 -0.0047 -0.0128 -0.0040 106 ILE A C +884 O O . ILE A 106 ? 0.2320 0.2302 0.2331 -0.0046 -0.0166 -0.0018 106 ILE A O +885 C CB . ILE A 106 ? 0.2423 0.2319 0.2246 -0.0060 -0.0113 -0.0099 106 ILE A CB +886 C CG1 . ILE A 106 ? 0.2423 0.2345 0.2247 -0.0057 -0.0162 -0.0099 106 ILE A CG1 +887 C CG2 . ILE A 106 ? 0.2585 0.2427 0.2345 -0.0068 -0.0076 -0.0122 106 ILE A CG2 +888 C CD1 . ILE A 106 ? 0.2607 0.2523 0.2368 -0.0069 -0.0185 -0.0114 106 ILE A CD1 +889 N N . GLN A 107 ? 0.2470 0.2421 0.2414 -0.0055 -0.0122 -0.0041 107 GLN A N +890 C CA . GLN A 107 ? 0.2511 0.2492 0.2493 -0.0062 -0.0161 -0.0018 107 GLN A CA +891 C C . GLN A 107 ? 0.2377 0.2349 0.2291 -0.0075 -0.0206 -0.0044 107 GLN A C +892 O O . GLN A 107 ? 0.2268 0.2221 0.2116 -0.0080 -0.0196 -0.0072 107 GLN A O +893 C CB . GLN A 107 ? 0.2947 0.2930 0.2949 -0.0061 -0.0123 -0.0001 107 GLN A CB +894 C CG . GLN A 107 ? 0.3689 0.3673 0.3760 -0.0041 -0.0061 0.0033 107 GLN A CG +895 C CD . GLN A 107 ? 0.4527 0.4559 0.4716 -0.0036 -0.0086 0.0088 107 GLN A CD +896 O OE1 . GLN A 107 ? 0.4809 0.4869 0.5026 -0.0053 -0.0152 0.0106 107 GLN A OE1 +897 N NE2 . GLN A 107 ? 0.4710 0.4747 0.4969 -0.0014 -0.0034 0.0122 107 GLN A NE2 +898 N N . PRO A 108 ? 0.2328 0.2308 0.2256 -0.0082 -0.0254 -0.0030 108 PRO A N +899 C CA . PRO A 108 ? 0.2328 0.2291 0.2193 -0.0088 -0.0285 -0.0051 108 PRO A CA +900 C C . PRO A 108 ? 0.2246 0.2212 0.2084 -0.0096 -0.0261 -0.0061 108 PRO A C +901 O O . PRO A 108 ? 0.2289 0.2269 0.2161 -0.0099 -0.0235 -0.0046 108 PRO A O +902 C CB . PRO A 108 ? 0.2553 0.2507 0.2435 -0.0098 -0.0334 -0.0030 108 PRO A CB +903 C CG . PRO A 108 ? 0.2711 0.2697 0.2685 -0.0102 -0.0330 0.0010 108 PRO A CG +904 C CD . PRO A 108 ? 0.2406 0.2406 0.2409 -0.0088 -0.0284 0.0011 108 PRO A CD +905 N N . GLY A 109 ? 0.2113 0.2069 0.1895 -0.0099 -0.0266 -0.0079 109 GLY A N +906 C CA . GLY A 109 ? 0.2149 0.2110 0.1901 -0.0113 -0.0251 -0.0083 109 GLY A CA +907 C C . GLY A 109 ? 0.2262 0.2210 0.1971 -0.0123 -0.0223 -0.0097 109 GLY A C +908 O O . GLY A 109 ? 0.2460 0.2407 0.2128 -0.0141 -0.0223 -0.0099 109 GLY A O +909 N N A GLN A 110 ? 0.2239 0.2173 0.1955 -0.0114 -0.0202 -0.0104 110 GLN A N +910 N N B GLN A 110 ? 0.2164 0.2097 0.1880 -0.0114 -0.0201 -0.0104 110 GLN A N +911 C CA A GLN A 110 ? 0.2291 0.2196 0.1955 -0.0126 -0.0179 -0.0118 110 GLN A CA +912 C CA B GLN A 110 ? 0.2150 0.2054 0.1816 -0.0125 -0.0177 -0.0118 110 GLN A CA +913 C C A GLN A 110 ? 0.2190 0.2100 0.1832 -0.0129 -0.0203 -0.0120 110 GLN A C +914 C C B GLN A 110 ? 0.2140 0.2049 0.1782 -0.0129 -0.0202 -0.0120 110 GLN A C +915 O O A GLN A 110 ? 0.2176 0.2103 0.1844 -0.0110 -0.0224 -0.0114 110 GLN A O +916 O O B GLN A 110 ? 0.2136 0.2063 0.1806 -0.0110 -0.0223 -0.0114 110 GLN A O +917 C CB A GLN A 110 ? 0.2570 0.2450 0.2251 -0.0114 -0.0138 -0.0121 110 GLN A CB +918 C CB B GLN A 110 ? 0.2230 0.2113 0.1920 -0.0111 -0.0139 -0.0120 110 GLN A CB +919 C CG A GLN A 110 ? 0.3110 0.2983 0.2815 -0.0108 -0.0101 -0.0110 110 GLN A CG +920 C CG B GLN A 110 ? 0.2436 0.2268 0.2063 -0.0123 -0.0112 -0.0138 110 GLN A CG +921 C CD A GLN A 110 ? 0.4009 0.3852 0.3643 -0.0131 -0.0084 -0.0118 110 GLN A CD +922 C CD B GLN A 110 ? 0.2659 0.2445 0.2201 -0.0152 -0.0094 -0.0149 110 GLN A CD +923 O OE1 A GLN A 110 ? 0.4405 0.4194 0.3954 -0.0150 -0.0065 -0.0137 110 GLN A OE1 +924 O OE1 B GLN A 110 ? 0.2822 0.2600 0.2362 -0.0150 -0.0068 -0.0144 110 GLN A OE1 +925 N NE2 A GLN A 110 ? 0.4069 0.3944 0.3730 -0.0133 -0.0095 -0.0103 110 GLN A NE2 +926 N NE2 B GLN A 110 ? 0.2433 0.2187 0.1903 -0.0181 -0.0110 -0.0158 110 GLN A NE2 +927 N N . THR A 111 ? 0.2128 0.2018 0.1715 -0.0155 -0.0202 -0.0122 111 THR A N +928 C CA . THR A 111 ? 0.2075 0.1977 0.1651 -0.0162 -0.0225 -0.0111 111 THR A CA +929 C C . THR A 111 ? 0.2020 0.1891 0.1577 -0.0166 -0.0214 -0.0120 111 THR A C +930 O O . THR A 111 ? 0.2183 0.2012 0.1718 -0.0169 -0.0183 -0.0138 111 THR A O +931 C CB . THR A 111 ? 0.2156 0.2063 0.1695 -0.0197 -0.0243 -0.0094 111 THR A CB +932 O OG1 . THR A 111 ? 0.2302 0.2157 0.1773 -0.0229 -0.0226 -0.0109 111 THR A OG1 +933 C CG2 . THR A 111 ? 0.2132 0.2071 0.1698 -0.0190 -0.0254 -0.0081 111 THR A CG2 +934 N N . PHE A 112 ? 0.1891 0.1782 0.1460 -0.0163 -0.0234 -0.0104 112 PHE A N +935 C CA . PHE A 112 ? 0.1846 0.1713 0.1403 -0.0170 -0.0231 -0.0107 112 PHE A CA +936 C C . PHE A 112 ? 0.1805 0.1706 0.1378 -0.0175 -0.0261 -0.0074 112 PHE A C +937 O O . PHE A 112 ? 0.1779 0.1722 0.1383 -0.0158 -0.0274 -0.0050 112 PHE A O +938 C CB . PHE A 112 ? 0.1862 0.1730 0.1462 -0.0136 -0.0210 -0.0121 112 PHE A CB +939 C CG . PHE A 112 ? 0.1824 0.1736 0.1476 -0.0101 -0.0224 -0.0109 112 PHE A CG +940 C CD1 . PHE A 112 ? 0.1942 0.1864 0.1613 -0.0087 -0.0225 -0.0112 112 PHE A CD1 +941 C CD2 . PHE A 112 ? 0.1852 0.1784 0.1524 -0.0084 -0.0236 -0.0094 112 PHE A CD2 +942 C CE1 . PHE A 112 ? 0.2015 0.1953 0.1709 -0.0061 -0.0241 -0.0105 112 PHE A CE1 +943 C CE2 . PHE A 112 ? 0.1897 0.1848 0.1592 -0.0052 -0.0244 -0.0086 112 PHE A CE2 +944 C CZ . PHE A 112 ? 0.1967 0.1914 0.1664 -0.0043 -0.0248 -0.0094 112 PHE A CZ +945 N N . SER A 113 ? 0.1742 0.1622 0.1298 -0.0194 -0.0268 -0.0068 113 SER A N +946 C CA . SER A 113 ? 0.1744 0.1662 0.1331 -0.0198 -0.0296 -0.0025 113 SER A CA +947 C C . SER A 113 ? 0.1779 0.1720 0.1416 -0.0156 -0.0286 -0.0023 113 SER A C +948 O O . SER A 113 ? 0.1868 0.1781 0.1502 -0.0147 -0.0266 -0.0053 113 SER A O +949 C CB . SER A 113 ? 0.1853 0.1730 0.1390 -0.0252 -0.0320 -0.0012 113 SER A CB +950 O OG . SER A 113 ? 0.2038 0.1885 0.1513 -0.0296 -0.0333 -0.0013 113 SER A OG +951 N N . VAL A 114 ? 0.1666 0.1656 0.1348 -0.0132 -0.0296 0.0016 114 VAL A N +952 C CA . VAL A 114 ? 0.1711 0.1722 0.1433 -0.0093 -0.0287 0.0025 114 VAL A CA +953 C C . VAL A 114 ? 0.1720 0.1758 0.1472 -0.0107 -0.0308 0.0073 114 VAL A C +954 O O . VAL A 114 ? 0.1727 0.1794 0.1497 -0.0122 -0.0325 0.0121 114 VAL A O +955 C CB . VAL A 114 ? 0.1719 0.1753 0.1458 -0.0046 -0.0275 0.0034 114 VAL A CB +956 C CG1 . VAL A 114 ? 0.1736 0.1787 0.1503 -0.0006 -0.0266 0.0052 114 VAL A CG1 +957 C CG2 . VAL A 114 ? 0.1813 0.1819 0.1527 -0.0037 -0.0264 -0.0007 114 VAL A CG2 +958 N N . LEU A 115 ? 0.1646 0.1679 0.1415 -0.0102 -0.0306 0.0070 115 LEU A N +959 C CA . LEU A 115 ? 0.1630 0.1694 0.1439 -0.0111 -0.0327 0.0122 115 LEU A CA +960 C C . LEU A 115 ? 0.1635 0.1741 0.1492 -0.0051 -0.0306 0.0143 115 LEU A C +961 O O . LEU A 115 ? 0.1683 0.1779 0.1546 -0.0029 -0.0292 0.0116 115 LEU A O +962 C CB . LEU A 115 ? 0.1697 0.1718 0.1487 -0.0147 -0.0340 0.0106 115 LEU A CB +963 C CG . LEU A 115 ? 0.1872 0.1925 0.1710 -0.0160 -0.0368 0.0165 115 LEU A CG +964 C CD1 . LEU A 115 ? 0.1973 0.2049 0.1819 -0.0202 -0.0406 0.0224 115 LEU A CD1 +965 C CD2 . LEU A 115 ? 0.1923 0.1921 0.1735 -0.0192 -0.0377 0.0142 115 LEU A CD2 +966 N N A ALA A 116 ? 0.1576 0.1721 0.1462 -0.0022 -0.0299 0.0190 116 ALA A N +967 N N B ALA A 116 ? 0.1632 0.1778 0.1520 -0.0024 -0.0300 0.0193 116 ALA A N +968 C CA A ALA A 116 ? 0.1643 0.1809 0.1552 0.0039 -0.0271 0.0210 116 ALA A CA +969 C CA B ALA A 116 ? 0.1766 0.1938 0.1682 0.0036 -0.0274 0.0220 116 ALA A CA +970 C C A ALA A 116 ? 0.1638 0.1840 0.1603 0.0043 -0.0280 0.0257 116 ALA A C +971 C C B ALA A 116 ? 0.1808 0.2010 0.1775 0.0037 -0.0283 0.0256 116 ALA A C +972 O O A ALA A 116 ? 0.1640 0.1877 0.1651 0.0017 -0.0302 0.0314 116 ALA A O +973 O O B ALA A 116 ? 0.1837 0.2061 0.1839 -0.0002 -0.0313 0.0298 116 ALA A O +974 C CB A ALA A 116 ? 0.1721 0.1901 0.1635 0.0074 -0.0249 0.0250 116 ALA A CB +975 C CB B ALA A 116 ? 0.1826 0.2025 0.1765 0.0062 -0.0258 0.0276 116 ALA A CB +976 N N A CYS A 117 ? 0.1629 0.1828 0.1597 0.0071 -0.0266 0.0237 117 CYS A N +977 N N B CYS A 117 ? 0.1817 0.2018 0.1786 0.0076 -0.0264 0.0241 117 CYS A N +978 C CA A CYS A 117 ? 0.1670 0.1905 0.1694 0.0080 -0.0272 0.0278 117 CYS A CA +979 C CA B CYS A 117 ? 0.1867 0.2097 0.1886 0.0078 -0.0272 0.0270 117 CYS A CA +980 C C A CYS A 117 ? 0.1750 0.2001 0.1782 0.0142 -0.0240 0.0300 117 CYS A C +981 C C B CYS A 117 ? 0.1857 0.2107 0.1888 0.0141 -0.0240 0.0295 117 CYS A C +982 O O A CYS A 117 ? 0.1758 0.1973 0.1732 0.0170 -0.0218 0.0262 117 CYS A O +983 O O B CYS A 117 ? 0.1897 0.2112 0.1872 0.0170 -0.0219 0.0258 117 CYS A O +984 C CB A CYS A 117 ? 0.1751 0.1960 0.1771 0.0049 -0.0287 0.0233 117 CYS A CB +985 C CB B CYS A 117 ? 0.2039 0.2234 0.2040 0.0047 -0.0284 0.0214 117 CYS A CB +986 S SG A CYS A 117 ? 0.1800 0.1960 0.1782 -0.0024 -0.0317 0.0203 117 CYS A SG +987 S SG B CYS A 117 ? 0.2509 0.2722 0.2567 0.0020 -0.0309 0.0245 117 CYS A SG +988 N N . TYR A 118 ? 0.1791 0.2090 0.1887 0.0158 -0.0239 0.0360 118 TYR A N +989 C CA . TYR A 118 ? 0.1964 0.2278 0.2067 0.0219 -0.0205 0.0388 118 TYR A CA +990 C C . TYR A 118 ? 0.2126 0.2481 0.2297 0.0210 -0.0223 0.0416 118 TYR A C +991 O O . TYR A 118 ? 0.2115 0.2504 0.2348 0.0173 -0.0253 0.0459 118 TYR A O +992 C CB . TYR A 118 ? 0.2023 0.2361 0.2148 0.0267 -0.0169 0.0462 118 TYR A CB +993 C CG . TYR A 118 ? 0.2149 0.2438 0.2205 0.0279 -0.0148 0.0434 118 TYR A CG +994 C CD1 . TYR A 118 ? 0.2294 0.2518 0.2255 0.0318 -0.0117 0.0390 118 TYR A CD1 +995 C CD2 . TYR A 118 ? 0.2263 0.2562 0.2337 0.0240 -0.0169 0.0444 118 TYR A CD2 +996 C CE1 . TYR A 118 ? 0.2428 0.2598 0.2321 0.0323 -0.0102 0.0360 118 TYR A CE1 +997 C CE2 . TYR A 118 ? 0.2393 0.2647 0.2406 0.0246 -0.0153 0.0412 118 TYR A CE2 +998 C CZ . TYR A 118 ? 0.2523 0.2712 0.2448 0.0289 -0.0119 0.0371 118 TYR A CZ +999 O OH . TYR A 118 ? 0.2759 0.2898 0.2623 0.0292 -0.0107 0.0342 118 TYR A OH +1000 N N . ASN A 119 ? 0.2222 0.2571 0.2379 0.0235 -0.0211 0.0393 119 ASN A N +1001 C CA . ASN A 119 ? 0.2341 0.2729 0.2567 0.0229 -0.0226 0.0418 119 ASN A CA +1002 C C . ASN A 119 ? 0.2266 0.2644 0.2519 0.0164 -0.0266 0.0395 119 ASN A C +1003 O O . ASN A 119 ? 0.2314 0.2726 0.2635 0.0144 -0.0290 0.0439 119 ASN A O +1004 C CB . ASN A 119 ? 0.2617 0.3068 0.2918 0.0263 -0.0213 0.0512 119 ASN A CB +1005 C CG . ASN A 119 ? 0.3308 0.3751 0.3568 0.0333 -0.0160 0.0538 119 ASN A CG +1006 O OD1 . ASN A 119 ? 0.3668 0.4120 0.3934 0.0362 -0.0133 0.0588 119 ASN A OD1 +1007 N ND2 . ASN A 119 ? 0.3485 0.3905 0.3698 0.0362 -0.0143 0.0508 119 ASN A ND2 +1008 N N . GLY A 120 ? 0.2131 0.2457 0.2328 0.0131 -0.0274 0.0329 120 GLY A N +1009 C CA . GLY A 120 ? 0.2116 0.2406 0.2310 0.0073 -0.0301 0.0300 120 GLY A CA +1010 C C . GLY A 120 ? 0.2124 0.2411 0.2323 0.0027 -0.0334 0.0335 120 GLY A C +1011 O O . GLY A 120 ? 0.2158 0.2400 0.2337 -0.0027 -0.0360 0.0316 120 GLY A O +1012 N N . SER A 121 ? 0.2081 0.2410 0.2303 0.0045 -0.0332 0.0393 121 SER A N +1013 C CA . SER A 121 ? 0.2219 0.2559 0.2461 -0.0002 -0.0369 0.0444 121 SER A CA +1014 C C . SER A 121 ? 0.2273 0.2595 0.2467 -0.0010 -0.0363 0.0428 121 SER A C +1015 O O . SER A 121 ? 0.2210 0.2548 0.2397 0.0040 -0.0327 0.0432 121 SER A O +1016 C CB . SER A 121 ? 0.2465 0.2885 0.2805 0.0022 -0.0374 0.0548 121 SER A CB +1017 O OG . SER A 121 ? 0.2958 0.3397 0.3349 0.0018 -0.0389 0.0568 121 SER A OG +1018 N N . PRO A 122 ? 0.2413 0.2691 0.2563 -0.0075 -0.0399 0.0411 122 PRO A N +1019 C CA . PRO A 122 ? 0.2456 0.2719 0.2562 -0.0087 -0.0395 0.0397 122 PRO A CA +1020 C C . PRO A 122 ? 0.2367 0.2697 0.2538 -0.0069 -0.0395 0.0485 122 PRO A C +1021 O O . PRO A 122 ? 0.2354 0.2734 0.2600 -0.0088 -0.0424 0.0570 122 PRO A O +1022 C CB . PRO A 122 ? 0.2727 0.2920 0.2764 -0.0165 -0.0436 0.0364 122 PRO A CB +1023 C CG . PRO A 122 ? 0.2849 0.2995 0.2868 -0.0178 -0.0438 0.0324 122 PRO A CG +1024 C CD . PRO A 122 ? 0.2534 0.2757 0.2652 -0.0142 -0.0439 0.0393 122 PRO A CD +1025 N N . SER A 123 ? 0.2282 0.2613 0.2432 -0.0032 -0.0360 0.0472 123 SER A N +1026 C CA . SER A 123 ? 0.2331 0.2718 0.2542 -0.0008 -0.0348 0.0555 123 SER A CA +1027 C C . SER A 123 ? 0.2247 0.2623 0.2433 -0.0052 -0.0369 0.0555 123 SER A C +1028 O O . SER A 123 ? 0.2283 0.2711 0.2537 -0.0068 -0.0386 0.0643 123 SER A O +1029 C CB . SER A 123 ? 0.2721 0.3113 0.2931 0.0077 -0.0283 0.0556 123 SER A CB +1030 O OG . SER A 123 ? 0.3356 0.3686 0.3475 0.0089 -0.0263 0.0467 123 SER A OG +1031 N N . GLY A 124 ? 0.2063 0.2377 0.2159 -0.0069 -0.0366 0.0466 124 GLY A N +1032 C CA . GLY A 124 ? 0.2006 0.2308 0.2073 -0.0109 -0.0383 0.0464 124 GLY A CA +1033 C C . GLY A 124 ? 0.1914 0.2145 0.1884 -0.0130 -0.0381 0.0366 124 GLY A C +1034 O O . GLY A 124 ? 0.1835 0.2030 0.1769 -0.0105 -0.0358 0.0302 124 GLY A O +1035 N N . VAL A 125 ? 0.1915 0.2130 0.1850 -0.0177 -0.0403 0.0362 125 VAL A N +1036 C CA . VAL A 125 ? 0.2046 0.2196 0.1894 -0.0198 -0.0398 0.0280 125 VAL A CA +1037 C C . VAL A 125 ? 0.2054 0.2216 0.1896 -0.0194 -0.0388 0.0283 125 VAL A C +1038 O O . VAL A 125 ? 0.2082 0.2289 0.1970 -0.0211 -0.0406 0.0352 125 VAL A O +1039 C CB . VAL A 125 ? 0.2389 0.2477 0.2169 -0.0270 -0.0434 0.0256 125 VAL A CB +1040 C CG1 . VAL A 125 ? 0.2575 0.2676 0.2356 -0.0337 -0.0487 0.0322 125 VAL A CG1 +1041 C CG2 . VAL A 125 ? 0.2505 0.2520 0.2196 -0.0278 -0.0413 0.0171 125 VAL A CG2 +1042 N N . TYR A 126 ? 0.2076 0.2204 0.1874 -0.0167 -0.0359 0.0217 126 TYR A N +1043 C CA . TYR A 126 ? 0.2073 0.2207 0.1864 -0.0161 -0.0349 0.0215 126 TYR A CA +1044 C C . TYR A 126 ? 0.2039 0.2122 0.1767 -0.0165 -0.0336 0.0139 126 TYR A C +1045 O O . TYR A 126 ? 0.2102 0.2149 0.1804 -0.0156 -0.0324 0.0092 126 TYR A O +1046 C CB . TYR A 126 ? 0.2086 0.2252 0.1926 -0.0098 -0.0316 0.0249 126 TYR A CB +1047 C CG . TYR A 126 ? 0.2180 0.2320 0.2004 -0.0043 -0.0285 0.0209 126 TYR A CG +1048 C CD1 . TYR A 126 ? 0.2293 0.2390 0.2069 -0.0027 -0.0271 0.0147 126 TYR A CD1 +1049 C CD2 . TYR A 126 ? 0.2334 0.2491 0.2190 -0.0013 -0.0275 0.0237 126 TYR A CD2 +1050 C CE1 . TYR A 126 ? 0.2413 0.2482 0.2168 0.0014 -0.0252 0.0117 126 TYR A CE1 +1051 C CE2 . TYR A 126 ? 0.2452 0.2581 0.2283 0.0033 -0.0250 0.0202 126 TYR A CE2 +1052 C CZ . TYR A 126 ? 0.2542 0.2625 0.2320 0.0043 -0.0241 0.0143 126 TYR A CZ +1053 O OH . TYR A 126 ? 0.2901 0.2953 0.2649 0.0080 -0.0226 0.0116 126 TYR A OH +1054 N N A GLN A 127 ? 0.2048 0.2129 0.1759 -0.0181 -0.0338 0.0136 127 GLN A N +1055 N N B GLN A 127 ? 0.2029 0.2111 0.1743 -0.0174 -0.0334 0.0134 127 GLN A N +1056 C CA A GLN A 127 ? 0.2100 0.2140 0.1761 -0.0189 -0.0326 0.0078 127 GLN A CA +1057 C CA B GLN A 127 ? 0.2088 0.2131 0.1755 -0.0177 -0.0321 0.0075 127 GLN A CA +1058 C C A GLN A 127 ? 0.2180 0.2225 0.1858 -0.0142 -0.0304 0.0061 127 GLN A C +1059 C C B GLN A 127 ? 0.2144 0.2186 0.1826 -0.0125 -0.0297 0.0055 127 GLN A C +1060 O O A GLN A 127 ? 0.2180 0.2252 0.1888 -0.0123 -0.0300 0.0097 127 GLN A O +1061 O O B GLN A 127 ? 0.2147 0.2211 0.1858 -0.0097 -0.0289 0.0088 127 GLN A O +1062 C CB A GLN A 127 ? 0.2189 0.2223 0.1814 -0.0245 -0.0349 0.0091 127 GLN A CB +1063 C CB B GLN A 127 ? 0.2260 0.2301 0.1899 -0.0223 -0.0338 0.0085 127 GLN A CB +1064 C CG A GLN A 127 ? 0.2441 0.2428 0.2006 -0.0261 -0.0336 0.0039 127 GLN A CG +1065 C CG B GLN A 127 ? 0.2569 0.2563 0.2152 -0.0236 -0.0324 0.0030 127 GLN A CG +1066 C CD A GLN A 127 ? 0.2576 0.2501 0.2085 -0.0274 -0.0323 -0.0004 127 GLN A CD +1067 C CD B GLN A 127 ? 0.2674 0.2610 0.2195 -0.0268 -0.0323 0.0000 127 GLN A CD +1068 O OE1 A GLN A 127 ? 0.2529 0.2441 0.2039 -0.0277 -0.0329 0.0001 127 GLN A OE1 +1069 O OE1 B GLN A 127 ? 0.2729 0.2655 0.2250 -0.0275 -0.0333 0.0010 127 GLN A OE1 +1070 N NE2 A GLN A 127 ? 0.2689 0.2572 0.2154 -0.0278 -0.0299 -0.0043 127 GLN A NE2 +1071 N NE2 B GLN A 127 ? 0.2625 0.2514 0.2090 -0.0283 -0.0305 -0.0036 127 GLN A NE2 +1072 N N A CYS A 128 ? 0.2195 0.2209 0.1853 -0.0124 -0.0288 0.0013 128 CYS A N +1073 N N B CYS A 128 ? 0.2191 0.2201 0.1851 -0.0114 -0.0285 0.0006 128 CYS A N +1074 C CA A CYS A 128 ? 0.2236 0.2241 0.1898 -0.0089 -0.0277 -0.0004 128 CYS A CA +1075 C CA B CYS A 128 ? 0.2279 0.2275 0.1941 -0.0078 -0.0273 -0.0016 128 CYS A CA +1076 C C A CYS A 128 ? 0.2259 0.2239 0.1904 -0.0099 -0.0272 -0.0044 128 CYS A C +1077 C C B CYS A 128 ? 0.2284 0.2260 0.1930 -0.0094 -0.0270 -0.0049 128 CYS A C +1078 O O A CYS A 128 ? 0.2252 0.2219 0.1876 -0.0130 -0.0269 -0.0057 128 CYS A O +1079 O O B CYS A 128 ? 0.2274 0.2236 0.1902 -0.0123 -0.0266 -0.0063 128 CYS A O +1080 C CB A CYS A 128 ? 0.2301 0.2299 0.1972 -0.0046 -0.0267 -0.0001 128 CYS A CB +1081 C CB B CYS A 128 ? 0.2450 0.2435 0.2118 -0.0049 -0.0266 -0.0027 128 CYS A CB +1082 S SG A CYS A 128 ? 0.2613 0.2596 0.2283 -0.0042 -0.0265 -0.0031 128 CYS A SG +1083 S SG B CYS A 128 ? 0.3024 0.3023 0.2705 -0.0008 -0.0258 0.0013 128 CYS A SG +1084 N N . ALA A 129 ? 0.2293 0.2258 0.1942 -0.0075 -0.0270 -0.0059 129 ALA A N +1085 C CA . ALA A 129 ? 0.2310 0.2263 0.1962 -0.0084 -0.0268 -0.0082 129 ALA A CA +1086 C C . ALA A 129 ? 0.2206 0.2142 0.1869 -0.0061 -0.0274 -0.0091 129 ALA A C +1087 O O . ALA A 129 ? 0.2327 0.2246 0.1972 -0.0039 -0.0283 -0.0085 129 ALA A O +1088 C CB . ALA A 129 ? 0.2348 0.2306 0.1999 -0.0096 -0.0273 -0.0076 129 ALA A CB +1089 N N . MET A 130 ? 0.2008 0.1942 0.1694 -0.0068 -0.0270 -0.0101 130 MET A N +1090 C CA . MET A 130 ? 0.1952 0.1873 0.1656 -0.0057 -0.0286 -0.0099 130 MET A CA +1091 C C . MET A 130 ? 0.2025 0.1933 0.1720 -0.0061 -0.0307 -0.0095 130 MET A C +1092 O O . MET A 130 ? 0.2061 0.1984 0.1776 -0.0075 -0.0301 -0.0092 130 MET A O +1093 C CB . MET A 130 ? 0.1989 0.1922 0.1742 -0.0063 -0.0271 -0.0096 130 MET A CB +1094 C CG . MET A 130 ? 0.2203 0.2135 0.1991 -0.0060 -0.0295 -0.0081 130 MET A CG +1095 S SD . MET A 130 ? 0.2278 0.2187 0.2031 -0.0045 -0.0322 -0.0081 130 MET A SD +1096 C CE . MET A 130 ? 0.2113 0.2043 0.1880 -0.0035 -0.0287 -0.0088 130 MET A CE +1097 N N . ARG A 131 ? 0.2015 0.1887 0.1670 -0.0048 -0.0327 -0.0094 131 ARG A N +1098 C CA . ARG A 131 ? 0.2027 0.1870 0.1662 -0.0053 -0.0347 -0.0091 131 ARG A CA +1099 C C . ARG A 131 ? 0.2077 0.1917 0.1747 -0.0072 -0.0374 -0.0082 131 ARG A C +1100 O O . ARG A 131 ? 0.2090 0.1938 0.1788 -0.0075 -0.0383 -0.0074 131 ARG A O +1101 C CB . ARG A 131 ? 0.2088 0.1867 0.1650 -0.0032 -0.0355 -0.0094 131 ARG A CB +1102 C CG . ARG A 131 ? 0.2152 0.1936 0.1693 -0.0008 -0.0325 -0.0088 131 ARG A CG +1103 C CD . ARG A 131 ? 0.2128 0.1956 0.1700 -0.0015 -0.0307 -0.0075 131 ARG A CD +1104 N NE . ARG A 131 ? 0.2100 0.1907 0.1667 -0.0024 -0.0319 -0.0075 131 ARG A NE +1105 C CZ . ARG A 131 ? 0.2081 0.1926 0.1680 -0.0038 -0.0312 -0.0063 131 ARG A CZ +1106 N NH1 . ARG A 131 ? 0.1936 0.1834 0.1563 -0.0048 -0.0297 -0.0050 131 ARG A NH1 +1107 N NH2 . ARG A 131 ? 0.2013 0.1839 0.1611 -0.0045 -0.0325 -0.0061 131 ARG A NH2 +1108 N N . PRO A 132 ? 0.2112 0.1942 0.1788 -0.0085 -0.0393 -0.0075 132 PRO A N +1109 C CA . PRO A 132 ? 0.2154 0.1985 0.1874 -0.0105 -0.0426 -0.0054 132 PRO A CA +1110 C C . PRO A 132 ? 0.2233 0.2010 0.1915 -0.0113 -0.0469 -0.0047 132 PRO A C +1111 O O . PRO A 132 ? 0.2373 0.2166 0.2109 -0.0134 -0.0498 -0.0019 132 PRO A O +1112 C CB . PRO A 132 ? 0.2262 0.2083 0.1981 -0.0116 -0.0440 -0.0048 132 PRO A CB +1113 C CG . PRO A 132 ? 0.2227 0.2079 0.1941 -0.0105 -0.0399 -0.0061 132 PRO A CG +1114 C CD . PRO A 132 ? 0.2092 0.1921 0.1752 -0.0084 -0.0383 -0.0077 132 PRO A CD +1115 N N . ASN A 133 ? 0.2123 0.1833 0.1710 -0.0098 -0.0473 -0.0067 133 ASN A N +1116 C CA . ASN A 133 ? 0.2134 0.1779 0.1661 -0.0109 -0.0513 -0.0062 133 ASN A CA +1117 C C . ASN A 133 ? 0.2127 0.1806 0.1674 -0.0096 -0.0496 -0.0062 133 ASN A C +1118 O O . ASN A 133 ? 0.2193 0.1818 0.1678 -0.0099 -0.0521 -0.0061 133 ASN A O +1119 C CB . ASN A 133 ? 0.2299 0.1833 0.1694 -0.0097 -0.0521 -0.0083 133 ASN A CB +1120 C CG . ASN A 133 ? 0.2370 0.1903 0.1728 -0.0056 -0.0467 -0.0100 133 ASN A CG +1121 O OD1 . ASN A 133 ? 0.2231 0.1841 0.1651 -0.0041 -0.0433 -0.0099 133 ASN A OD1 +1122 N ND2 . ASN A 133 ? 0.2540 0.1978 0.1793 -0.0036 -0.0456 -0.0112 133 ASN A ND2 +1123 N N . PHE A 134 ? 0.2034 0.1791 0.1657 -0.0083 -0.0454 -0.0063 134 PHE A N +1124 C CA . PHE A 134 ? 0.2103 0.1897 0.1760 -0.0072 -0.0434 -0.0060 134 PHE A CA +1125 C C . PHE A 134 ? 0.2120 0.1882 0.1706 -0.0047 -0.0419 -0.0077 134 PHE A C +1126 O O . PHE A 134 ? 0.2138 0.1918 0.1740 -0.0040 -0.0414 -0.0072 134 PHE A O +1127 C CB . PHE A 134 ? 0.2145 0.1952 0.1854 -0.0093 -0.0468 -0.0029 134 PHE A CB +1128 C CG . PHE A 134 ? 0.2344 0.2200 0.2151 -0.0112 -0.0470 0.0000 134 PHE A CG +1129 C CD1 . PHE A 134 ? 0.2511 0.2428 0.2400 -0.0101 -0.0422 0.0008 134 PHE A CD1 +1130 C CD2 . PHE A 134 ? 0.2532 0.2365 0.2344 -0.0140 -0.0520 0.0026 134 PHE A CD2 +1131 C CE1 . PHE A 134 ? 0.2621 0.2578 0.2600 -0.0110 -0.0413 0.0042 134 PHE A CE1 +1132 C CE2 . PHE A 134 ? 0.2640 0.2525 0.2556 -0.0153 -0.0519 0.0064 134 PHE A CE2 +1133 C CZ . PHE A 134 ? 0.2594 0.2543 0.2595 -0.0135 -0.0462 0.0073 134 PHE A CZ +1134 N N . THR A 135 ? 0.2087 0.1810 0.1607 -0.0029 -0.0404 -0.0091 135 THR A N +1135 C CA . THR A 135 ? 0.2126 0.1833 0.1598 0.0002 -0.0376 -0.0096 135 THR A CA +1136 C C . THR A 135 ? 0.2102 0.1872 0.1627 0.0010 -0.0340 -0.0095 135 THR A C +1137 O O . THR A 135 ? 0.2047 0.1852 0.1617 -0.0008 -0.0337 -0.0095 135 THR A O +1138 C CB . THR A 135 ? 0.2285 0.1900 0.1652 0.0020 -0.0376 -0.0102 135 THR A CB +1139 O OG1 . THR A 135 ? 0.2442 0.2059 0.1817 0.0019 -0.0365 -0.0103 135 THR A OG1 +1140 C CG2 . THR A 135 ? 0.2325 0.1852 0.1610 0.0002 -0.0420 -0.0105 135 THR A CG2 +1141 N N . ILE A 136 ? 0.2069 0.1849 0.1584 0.0034 -0.0314 -0.0087 136 ILE A N +1142 C CA . ILE A 136 ? 0.2138 0.1964 0.1688 0.0036 -0.0290 -0.0076 136 ILE A CA +1143 C C . ILE A 136 ? 0.2215 0.2012 0.1722 0.0069 -0.0267 -0.0057 136 ILE A C +1144 O O . ILE A 136 ? 0.2221 0.1966 0.1672 0.0095 -0.0262 -0.0057 136 ILE A O +1145 C CB . ILE A 136 ? 0.2269 0.2151 0.1873 0.0025 -0.0280 -0.0073 136 ILE A CB +1146 C CG1 . ILE A 136 ? 0.2382 0.2265 0.1980 0.0048 -0.0272 -0.0061 136 ILE A CG1 +1147 C CG2 . ILE A 136 ? 0.2386 0.2284 0.2029 0.0000 -0.0288 -0.0088 136 ILE A CG2 +1148 C CD1 . ILE A 136 ? 0.2465 0.2396 0.2111 0.0037 -0.0262 -0.0052 136 ILE A CD1 +1149 N N A LYS A 137 ? 0.2290 0.2116 0.1822 0.0070 -0.0251 -0.0036 137 LYS A N +1150 N N B LYS A 137 ? 0.2299 0.2126 0.1832 0.0069 -0.0252 -0.0037 137 LYS A N +1151 C CA A LYS A 137 ? 0.2450 0.2258 0.1963 0.0107 -0.0221 -0.0004 137 LYS A CA +1152 C CA B LYS A 137 ? 0.2468 0.2279 0.1985 0.0105 -0.0222 -0.0004 137 LYS A CA +1153 C C A LYS A 137 ? 0.2452 0.2327 0.2025 0.0107 -0.0210 0.0030 137 LYS A C +1154 C C B LYS A 137 ? 0.2455 0.2332 0.2030 0.0105 -0.0211 0.0029 137 LYS A C +1155 O O A LYS A 137 ? 0.2446 0.2372 0.2069 0.0083 -0.0214 0.0052 137 LYS A O +1156 O O B LYS A 137 ? 0.2441 0.2371 0.2066 0.0080 -0.0216 0.0050 137 LYS A O +1157 C CB A LYS A 137 ? 0.2776 0.2572 0.2288 0.0108 -0.0211 0.0009 137 LYS A CB +1158 C CB B LYS A 137 ? 0.2817 0.2627 0.2342 0.0101 -0.0214 0.0010 137 LYS A CB +1159 C CG A LYS A 137 ? 0.3396 0.3121 0.2850 0.0101 -0.0229 -0.0023 137 LYS A CG +1160 C CG B LYS A 137 ? 0.3499 0.3238 0.2966 0.0098 -0.0227 -0.0018 137 LYS A CG +1161 C CD A LYS A 137 ? 0.3939 0.3654 0.3399 0.0102 -0.0218 -0.0008 137 LYS A CD +1162 C CD B LYS A 137 ? 0.4039 0.3799 0.3538 0.0082 -0.0228 -0.0007 137 LYS A CD +1163 C CE A LYS A 137 ? 0.4429 0.4061 0.3822 0.0148 -0.0181 0.0008 137 LYS A CE +1164 C CE B LYS A 137 ? 0.4534 0.4206 0.3967 0.0098 -0.0225 -0.0017 137 LYS A CE +1165 N NZ A LYS A 137 ? 0.4766 0.4283 0.4051 0.0152 -0.0197 -0.0028 137 LYS A NZ +1166 N NZ B LYS A 137 ? 0.4711 0.4404 0.4176 0.0067 -0.0246 -0.0024 137 LYS A NZ +1167 N N . GLY A 138 ? 0.2446 0.2319 0.2013 0.0127 -0.0202 0.0035 138 GLY A N +1168 C CA . GLY A 138 ? 0.2460 0.2394 0.2086 0.0125 -0.0198 0.0070 138 GLY A CA +1169 C C . GLY A 138 ? 0.2391 0.2328 0.2027 0.0170 -0.0163 0.0123 138 GLY A C +1170 O O . GLY A 138 ? 0.2492 0.2386 0.2092 0.0205 -0.0133 0.0139 138 GLY A O +1171 N N . SER A 139 ? 0.2255 0.2242 0.1942 0.0172 -0.0163 0.0156 139 SER A N +1172 C CA . SER A 139 ? 0.2291 0.2292 0.2003 0.0218 -0.0127 0.0217 139 SER A CA +1173 C C . SER A 139 ? 0.2372 0.2384 0.2089 0.0226 -0.0132 0.0213 139 SER A C +1174 O O . SER A 139 ? 0.2391 0.2458 0.2167 0.0194 -0.0158 0.0224 139 SER A O +1175 C CB . SER A 139 ? 0.2409 0.2483 0.2211 0.0202 -0.0129 0.0287 139 SER A CB +1176 O OG . SER A 139 ? 0.2930 0.3033 0.2779 0.0245 -0.0096 0.0358 139 SER A OG +1177 N N . PHE A 140 ? 0.2317 0.2266 0.1959 0.0262 -0.0113 0.0188 140 PHE A N +1178 C CA . PHE A 140 ? 0.2400 0.2355 0.2040 0.0268 -0.0120 0.0179 140 PHE A CA +1179 C C . PHE A 140 ? 0.2721 0.2629 0.2306 0.0328 -0.0076 0.0206 140 PHE A C +1180 O O . PHE A 140 ? 0.2955 0.2774 0.2439 0.0353 -0.0056 0.0183 140 PHE A O +1181 C CB . PHE A 140 ? 0.2313 0.2232 0.1906 0.0238 -0.0153 0.0113 140 PHE A CB +1182 C CG . PHE A 140 ? 0.2256 0.2211 0.1894 0.0184 -0.0188 0.0083 140 PHE A CG +1183 C CD1 . PHE A 140 ? 0.2344 0.2352 0.2047 0.0157 -0.0205 0.0088 140 PHE A CD1 +1184 C CD2 . PHE A 140 ? 0.2295 0.2219 0.1902 0.0162 -0.0202 0.0049 140 PHE A CD2 +1185 C CE1 . PHE A 140 ? 0.2311 0.2331 0.2036 0.0112 -0.0227 0.0059 140 PHE A CE1 +1186 C CE2 . PHE A 140 ? 0.2363 0.2312 0.2005 0.0118 -0.0225 0.0024 140 PHE A CE2 +1187 C CZ . PHE A 140 ? 0.2268 0.2259 0.1962 0.0095 -0.0234 0.0027 140 PHE A CZ +1188 N N . LEU A 141 ? 0.2734 0.2692 0.2374 0.0351 -0.0061 0.0253 141 LEU A N +1189 C CA . LEU A 141 ? 0.2985 0.2898 0.2571 0.0412 -0.0013 0.0283 141 LEU A CA +1190 C C . LEU A 141 ? 0.3053 0.2961 0.2613 0.0405 -0.0035 0.0254 141 LEU A C +1191 O O . LEU A 141 ? 0.3014 0.2961 0.2616 0.0356 -0.0082 0.0219 141 LEU A O +1192 C CB . LEU A 141 ? 0.3101 0.3085 0.2785 0.0446 0.0022 0.0372 141 LEU A CB +1193 C CG . LEU A 141 ? 0.3488 0.3495 0.3224 0.0453 0.0044 0.0422 141 LEU A CG +1194 C CD1 . LEU A 141 ? 0.3570 0.3675 0.3437 0.0466 0.0057 0.0518 141 LEU A CD1 +1195 C CD2 . LEU A 141 ? 0.3693 0.3596 0.3325 0.0508 0.0105 0.0421 141 LEU A CD2 +1196 N N . ASN A 142 ? 0.3145 0.3005 0.2638 0.0455 0.0003 0.0273 142 ASN A N +1197 C CA . ASN A 142 ? 0.3191 0.3055 0.2668 0.0448 -0.0019 0.0255 142 ASN A CA +1198 C C . ASN A 142 ? 0.2914 0.2895 0.2533 0.0425 -0.0043 0.0287 142 ASN A C +1199 O O . ASN A 142 ? 0.2891 0.2935 0.2599 0.0439 -0.0025 0.0346 142 ASN A O +1200 C CB . ASN A 142 ? 0.3638 0.3423 0.3007 0.0507 0.0031 0.0276 142 ASN A CB +1201 C CG . ASN A 142 ? 0.4614 0.4256 0.3811 0.0514 0.0040 0.0230 142 ASN A CG +1202 O OD1 . ASN A 142 ? 0.4930 0.4539 0.4085 0.0465 -0.0011 0.0174 142 ASN A OD1 +1203 N ND2 . ASN A 142 ? 0.4901 0.4448 0.3992 0.0576 0.0107 0.0256 142 ASN A ND2 +1204 N N . GLY A 143 ? 0.2679 0.2684 0.2323 0.0383 -0.0087 0.0248 143 GLY A N +1205 C CA . GLY A 143 ? 0.2418 0.2512 0.2180 0.0354 -0.0114 0.0266 143 GLY A CA +1206 C C . GLY A 143 ? 0.2132 0.2251 0.1943 0.0298 -0.0149 0.0234 143 GLY A C +1207 O O . GLY A 143 ? 0.2026 0.2193 0.1911 0.0266 -0.0173 0.0235 143 GLY A O +1208 N N . SER A 144 ? 0.2005 0.2082 0.1767 0.0286 -0.0150 0.0207 144 SER A N +1209 C CA . SER A 144 ? 0.1811 0.1906 0.1609 0.0235 -0.0179 0.0178 144 SER A CA +1210 C C . SER A 144 ? 0.1726 0.1799 0.1508 0.0202 -0.0204 0.0123 144 SER A C +1211 O O . SER A 144 ? 0.1598 0.1682 0.1408 0.0163 -0.0220 0.0101 144 SER A O +1212 C CB . SER A 144 ? 0.1922 0.1992 0.1689 0.0234 -0.0170 0.0179 144 SER A CB +1213 O OG . SER A 144 ? 0.2250 0.2249 0.1925 0.0253 -0.0159 0.0147 144 SER A OG +1214 N N . CYS A 145 ? 0.1754 0.1797 0.1493 0.0216 -0.0206 0.0107 145 CYS A N +1215 C CA . CYS A 145 ? 0.1740 0.1774 0.1484 0.0185 -0.0230 0.0069 145 CYS A CA +1216 C C . CYS A 145 ? 0.1604 0.1686 0.1434 0.0158 -0.0237 0.0069 145 CYS A C +1217 O O . CYS A 145 ? 0.1619 0.1736 0.1494 0.0167 -0.0232 0.0096 145 CYS A O +1218 C CB . CYS A 145 ? 0.1941 0.1942 0.1633 0.0197 -0.0239 0.0066 145 CYS A CB +1219 S SG . CYS A 145 ? 0.2609 0.2515 0.2164 0.0219 -0.0233 0.0055 145 CYS A SG +1220 N N . GLY A 146 ? 0.1498 0.1572 0.1345 0.0128 -0.0246 0.0039 146 GLY A N +1221 C CA . GLY A 146 ? 0.1474 0.1568 0.1383 0.0104 -0.0244 0.0034 146 GLY A CA +1222 C C . GLY A 146 ? 0.1458 0.1546 0.1365 0.0080 -0.0242 0.0030 146 GLY A C +1223 O O . GLY A 146 ? 0.1578 0.1655 0.1507 0.0055 -0.0237 0.0017 146 GLY A O +1224 N N . SER A 147 ? 0.1431 0.1517 0.1305 0.0086 -0.0243 0.0043 147 SER A N +1225 C CA . SER A 147 ? 0.1443 0.1522 0.1310 0.0055 -0.0249 0.0043 147 SER A CA +1226 C C . SER A 147 ? 0.1516 0.1561 0.1359 0.0031 -0.0246 0.0002 147 SER A C +1227 O O . SER A 147 ? 0.1480 0.1514 0.1310 0.0044 -0.0243 -0.0015 147 SER A O +1228 C CB . SER A 147 ? 0.1573 0.1662 0.1420 0.0069 -0.0249 0.0071 147 SER A CB +1229 O OG . SER A 147 ? 0.1685 0.1807 0.1562 0.0096 -0.0244 0.0120 147 SER A OG +1230 N N . VAL A 148 ? 0.1463 0.1485 0.1295 -0.0004 -0.0246 -0.0010 148 VAL A N +1231 C CA . VAL A 148 ? 0.1560 0.1546 0.1370 -0.0022 -0.0233 -0.0044 148 VAL A CA +1232 C C . VAL A 148 ? 0.1614 0.1581 0.1381 -0.0047 -0.0239 -0.0051 148 VAL A C +1233 O O . VAL A 148 ? 0.1603 0.1578 0.1356 -0.0065 -0.0256 -0.0028 148 VAL A O +1234 C CB . VAL A 148 ? 0.1675 0.1627 0.1497 -0.0036 -0.0213 -0.0060 148 VAL A CB +1235 C CG1 . VAL A 148 ? 0.1651 0.1630 0.1529 -0.0010 -0.0206 -0.0050 148 VAL A CG1 +1236 C CG2 . VAL A 148 ? 0.1812 0.1732 0.1603 -0.0071 -0.0223 -0.0055 148 VAL A CG2 +1237 N N . GLY A 149 ? 0.1641 0.1587 0.1394 -0.0051 -0.0225 -0.0076 149 GLY A N +1238 C CA . GLY A 149 ? 0.1680 0.1602 0.1390 -0.0076 -0.0224 -0.0087 149 GLY A CA +1239 C C . GLY A 149 ? 0.1725 0.1592 0.1405 -0.0098 -0.0198 -0.0111 149 GLY A C +1240 O O . GLY A 149 ? 0.1692 0.1545 0.1400 -0.0084 -0.0172 -0.0121 149 GLY A O +1241 N N . PHE A 150 ? 0.1703 0.1533 0.1322 -0.0134 -0.0202 -0.0117 150 PHE A N +1242 C CA . PHE A 150 ? 0.1901 0.1652 0.1460 -0.0157 -0.0172 -0.0141 150 PHE A CA +1243 C C . PHE A 150 ? 0.2117 0.1828 0.1599 -0.0193 -0.0176 -0.0148 150 PHE A C +1244 O O . PHE A 150 ? 0.2039 0.1788 0.1519 -0.0209 -0.0211 -0.0128 150 PHE A O +1245 C CB . PHE A 150 ? 0.1951 0.1662 0.1486 -0.0177 -0.0178 -0.0138 150 PHE A CB +1246 C CG . PHE A 150 ? 0.2071 0.1797 0.1583 -0.0212 -0.0228 -0.0110 150 PHE A CG +1247 C CD1 . PHE A 150 ? 0.2157 0.1963 0.1740 -0.0192 -0.0256 -0.0074 150 PHE A CD1 +1248 C CD2 . PHE A 150 ? 0.2264 0.1922 0.1683 -0.0267 -0.0246 -0.0111 150 PHE A CD2 +1249 C CE1 . PHE A 150 ? 0.2266 0.2097 0.1848 -0.0220 -0.0297 -0.0033 150 PHE A CE1 +1250 C CE2 . PHE A 150 ? 0.2366 0.2048 0.1780 -0.0305 -0.0299 -0.0070 150 PHE A CE2 +1251 C CZ . PHE A 150 ? 0.2261 0.2036 0.1767 -0.0279 -0.0322 -0.0028 150 PHE A CZ +1252 N N . ASN A 151 ? 0.2234 0.1864 0.1650 -0.0206 -0.0137 -0.0174 151 ASN A N +1253 C CA . ASN A 151 ? 0.2490 0.2054 0.1802 -0.0247 -0.0136 -0.0185 151 ASN A CA +1254 C C . ASN A 151 ? 0.2759 0.2203 0.1967 -0.0277 -0.0115 -0.0205 151 ASN A C +1255 O O . ASN A 151 ? 0.2690 0.2107 0.1922 -0.0254 -0.0083 -0.0215 151 ASN A O +1256 C CB . ASN A 151 ? 0.2598 0.2158 0.1913 -0.0227 -0.0096 -0.0196 151 ASN A CB +1257 C CG . ASN A 151 ? 0.3002 0.2653 0.2385 -0.0214 -0.0125 -0.0177 151 ASN A CG +1258 O OD1 . ASN A 151 ? 0.3333 0.2995 0.2679 -0.0243 -0.0154 -0.0168 151 ASN A OD1 +1259 N ND2 . ASN A 151 ? 0.2779 0.2494 0.2257 -0.0172 -0.0122 -0.0169 151 ASN A ND2 +1260 N N . ILE A 152 ? 0.3027 0.2392 0.2112 -0.0333 -0.0133 -0.0211 152 ILE A N +1261 C CA . ILE A 152 ? 0.3469 0.2691 0.2424 -0.0368 -0.0114 -0.0235 152 ILE A CA +1262 C C . ILE A 152 ? 0.3883 0.2993 0.2701 -0.0391 -0.0075 -0.0260 152 ILE A C +1263 O O . ILE A 152 ? 0.3936 0.3075 0.2730 -0.0415 -0.0102 -0.0249 152 ILE A O +1264 C CB . ILE A 152 ? 0.3603 0.2802 0.2511 -0.0428 -0.0184 -0.0213 152 ILE A CB +1265 C CG1 . ILE A 152 ? 0.3656 0.2977 0.2707 -0.0401 -0.0221 -0.0178 152 ILE A CG1 +1266 C CG2 . ILE A 152 ? 0.3794 0.2822 0.2552 -0.0466 -0.0163 -0.0242 152 ILE A CG2 +1267 C CD1 . ILE A 152 ? 0.3812 0.3132 0.2845 -0.0455 -0.0290 -0.0141 152 ILE A CD1 +1268 N N . ASP A 153 ? 0.4161 0.3142 0.2891 -0.0379 -0.0005 -0.0292 153 ASP A N +1269 C CA . ASP A 153 ? 0.4501 0.3347 0.3071 -0.0400 0.0042 -0.0317 153 ASP A CA +1270 C C . ASP A 153 ? 0.4755 0.3426 0.3155 -0.0448 0.0044 -0.0342 153 ASP A C +1271 O O . ASP A 153 ? 0.4875 0.3468 0.3264 -0.0416 0.0105 -0.0360 153 ASP A O +1272 C CB . ASP A 153 ? 0.4891 0.3723 0.3503 -0.0332 0.0141 -0.0327 153 ASP A CB +1273 C CG . ASP A 153 ? 0.6021 0.4717 0.4468 -0.0348 0.0196 -0.0349 153 ASP A CG +1274 O OD1 . ASP A 153 ? 0.6244 0.4920 0.4593 -0.0404 0.0145 -0.0348 153 ASP A OD1 +1275 O OD2 . ASP A 153 ? 0.6541 0.5147 0.4955 -0.0303 0.0293 -0.0361 153 ASP A OD2 +1276 N N . TYR A 154 ? 0.4783 0.3395 0.3057 -0.0529 -0.0029 -0.0336 154 TYR A N +1277 C CA . TYR A 154 ? 0.4970 0.3411 0.3065 -0.0599 -0.0057 -0.0351 154 TYR A CA +1278 C C . TYR A 154 ? 0.4899 0.3367 0.3080 -0.0589 -0.0080 -0.0341 154 TYR A C +1279 O O . TYR A 154 ? 0.4925 0.3498 0.3191 -0.0620 -0.0165 -0.0302 154 TYR A O +1280 C CB . TYR A 154 ? 0.5145 0.3358 0.3015 -0.0610 0.0024 -0.0398 154 TYR A CB +1281 C CG . TYR A 154 ? 0.5418 0.3431 0.3083 -0.0686 -0.0009 -0.0418 154 TYR A CG +1282 C CD1 . TYR A 154 ? 0.5593 0.3587 0.3171 -0.0784 -0.0120 -0.0392 154 TYR A CD1 +1283 C CD2 . TYR A 154 ? 0.5632 0.3475 0.3196 -0.0663 0.0070 -0.0455 154 TYR A CD2 +1284 C CE1 . TYR A 154 ? 0.5842 0.3648 0.3230 -0.0863 -0.0162 -0.0403 154 TYR A CE1 +1285 C CE2 . TYR A 154 ? 0.5893 0.3541 0.3262 -0.0736 0.0036 -0.0474 154 TYR A CE2 +1286 C CZ . TYR A 154 ? 0.6066 0.3693 0.3342 -0.0840 -0.0084 -0.0449 154 TYR A CZ +1287 O OH . TYR A 154 ? 0.6433 0.3857 0.3507 -0.0922 -0.0128 -0.0463 154 TYR A OH +1288 N N . ASP A 155 ? 0.4819 0.3204 0.2992 -0.0543 -0.0001 -0.0370 155 ASP A N +1289 C CA . ASP A 155 ? 0.4692 0.3101 0.2947 -0.0533 -0.0020 -0.0360 155 ASP A CA +1290 C C . ASP A 155 ? 0.4375 0.2920 0.2834 -0.0445 0.0033 -0.0350 155 ASP A C +1291 O O . ASP A 155 ? 0.4396 0.2961 0.2927 -0.0429 0.0028 -0.0342 155 ASP A O +1292 C CB . ASP A 155 ? 0.5167 0.3350 0.3233 -0.0570 0.0010 -0.0394 155 ASP A CB +1293 C CG . ASP A 155 ? 0.5979 0.4010 0.3946 -0.0521 0.0136 -0.0436 155 ASP A CG +1294 O OD1 . ASP A 155 ? 0.6029 0.4128 0.4064 -0.0465 0.0196 -0.0435 155 ASP A OD1 +1295 O OD2 . ASP A 155 ? 0.6460 0.4298 0.4281 -0.0537 0.0176 -0.0465 155 ASP A OD2 +1296 N N . CYS A 156 ? 0.4061 0.2698 0.2611 -0.0390 0.0078 -0.0346 156 CYS A N +1297 C CA . CYS A 156 ? 0.3780 0.2540 0.2516 -0.0314 0.0122 -0.0330 156 CYS A CA +1298 C C . CYS A 156 ? 0.3346 0.2300 0.2241 -0.0297 0.0062 -0.0297 156 CYS A C +1299 O O . CYS A 156 ? 0.3294 0.2298 0.2191 -0.0301 0.0050 -0.0292 156 CYS A O +1300 C CB . CYS A 156 ? 0.3957 0.2659 0.2683 -0.0262 0.0226 -0.0343 156 CYS A CB +1301 S SG . CYS A 156 ? 0.4155 0.3003 0.3114 -0.0177 0.0276 -0.0310 156 CYS A SG +1302 N N . VAL A 157 ? 0.2993 0.2052 0.2021 -0.0273 0.0034 -0.0275 157 VAL A N +1303 C CA . VAL A 157 ? 0.2695 0.1921 0.1862 -0.0250 -0.0013 -0.0245 157 VAL A CA +1304 C C . VAL A 157 ? 0.2462 0.1761 0.1745 -0.0190 0.0035 -0.0237 157 VAL A C +1305 O O . VAL A 157 ? 0.2416 0.1712 0.1762 -0.0156 0.0077 -0.0233 157 VAL A O +1306 C CB . VAL A 157 ? 0.2674 0.1973 0.1918 -0.0254 -0.0067 -0.0219 157 VAL A CB +1307 C CG1 . VAL A 157 ? 0.2624 0.2074 0.1989 -0.0227 -0.0108 -0.0189 157 VAL A CG1 +1308 C CG2 . VAL A 157 ? 0.2831 0.2058 0.1974 -0.0319 -0.0121 -0.0214 157 VAL A CG2 +1309 N N . SER A 158 ? 0.2344 0.1714 0.1665 -0.0178 0.0025 -0.0229 158 SER A N +1310 C CA . SER A 158 ? 0.2258 0.1707 0.1698 -0.0129 0.0054 -0.0212 158 SER A CA +1311 C C . SER A 158 ? 0.2111 0.1683 0.1649 -0.0118 -0.0005 -0.0189 158 SER A C +1312 O O . SER A 158 ? 0.2087 0.1705 0.1618 -0.0132 -0.0047 -0.0183 158 SER A O +1313 C CB . SER A 158 ? 0.2555 0.1997 0.1973 -0.0125 0.0081 -0.0214 158 SER A CB +1314 O OG . SER A 158 ? 0.3059 0.2382 0.2392 -0.0122 0.0154 -0.0230 158 SER A OG +1315 N N . PHE A 159 ? 0.1963 0.1580 0.1587 -0.0092 -0.0006 -0.0174 159 PHE A N +1316 C CA . PHE A 159 ? 0.1856 0.1572 0.1557 -0.0078 -0.0055 -0.0152 159 PHE A CA +1317 C C . PHE A 159 ? 0.1799 0.1570 0.1566 -0.0054 -0.0052 -0.0138 159 PHE A C +1318 O O . PHE A 159 ? 0.1835 0.1603 0.1655 -0.0034 -0.0012 -0.0127 159 PHE A O +1319 C CB . PHE A 159 ? 0.1763 0.1503 0.1525 -0.0061 -0.0055 -0.0139 159 PHE A CB +1320 C CG . PHE A 159 ? 0.1674 0.1367 0.1381 -0.0086 -0.0069 -0.0146 159 PHE A CG +1321 C CD1 . PHE A 159 ? 0.1742 0.1471 0.1436 -0.0104 -0.0121 -0.0133 159 PHE A CD1 +1322 C CD2 . PHE A 159 ? 0.1754 0.1360 0.1424 -0.0094 -0.0028 -0.0160 159 PHE A CD2 +1323 C CE1 . PHE A 159 ? 0.1811 0.1504 0.1468 -0.0132 -0.0142 -0.0128 159 PHE A CE1 +1324 C CE2 . PHE A 159 ? 0.1872 0.1425 0.1485 -0.0125 -0.0050 -0.0164 159 PHE A CE2 +1325 C CZ . PHE A 159 ? 0.1816 0.1420 0.1428 -0.0146 -0.0111 -0.0145 159 PHE A CZ +1326 N N . CYS A 160 ? 0.1774 0.1596 0.1544 -0.0056 -0.0096 -0.0132 160 CYS A N +1327 C CA . CYS A 160 ? 0.1816 0.1679 0.1634 -0.0042 -0.0104 -0.0118 160 CYS A CA +1328 C C . CYS A 160 ? 0.1752 0.1668 0.1604 -0.0030 -0.0148 -0.0103 160 CYS A C +1329 O O . CYS A 160 ? 0.1811 0.1751 0.1700 -0.0023 -0.0161 -0.0089 160 CYS A O +1330 C CB . CYS A 160 ? 0.2017 0.1866 0.1789 -0.0058 -0.0105 -0.0128 160 CYS A CB +1331 S SG . CYS A 160 ? 0.2072 0.1925 0.1776 -0.0081 -0.0147 -0.0136 160 CYS A SG +1332 N N . TYR A 161 ? 0.1606 0.1533 0.1436 -0.0029 -0.0171 -0.0103 161 TYR A N +1333 C CA . TYR A 161 ? 0.1578 0.1535 0.1414 -0.0014 -0.0205 -0.0090 161 TYR A CA +1334 C C . TYR A 161 ? 0.1479 0.1452 0.1326 -0.0001 -0.0212 -0.0080 161 TYR A C +1335 O O . TYR A 161 ? 0.1466 0.1431 0.1302 -0.0010 -0.0204 -0.0081 161 TYR A O +1336 C CB . TYR A 161 ? 0.1484 0.1439 0.1270 -0.0019 -0.0224 -0.0094 161 TYR A CB +1337 C CG . TYR A 161 ? 0.1499 0.1462 0.1268 0.0001 -0.0248 -0.0083 161 TYR A CG +1338 C CD1 . TYR A 161 ? 0.1642 0.1594 0.1405 0.0004 -0.0266 -0.0082 161 TYR A CD1 +1339 C CD2 . TYR A 161 ? 0.1577 0.1549 0.1328 0.0015 -0.0253 -0.0070 161 TYR A CD2 +1340 C CE1 . TYR A 161 ? 0.1733 0.1666 0.1453 0.0020 -0.0286 -0.0076 161 TYR A CE1 +1341 C CE2 . TYR A 161 ? 0.1680 0.1641 0.1399 0.0039 -0.0263 -0.0060 161 TYR A CE2 +1342 C CZ . TYR A 161 ? 0.1717 0.1649 0.1409 0.0041 -0.0279 -0.0067 161 TYR A CZ +1343 O OH . TYR A 161 ? 0.1797 0.1693 0.1430 0.0063 -0.0287 -0.0061 161 TYR A OH +1344 N N . MET A 162 ? 0.1349 0.1341 0.1214 0.0016 -0.0230 -0.0066 162 MET A N +1345 C CA . MET A 162 ? 0.1393 0.1402 0.1261 0.0032 -0.0238 -0.0051 162 MET A CA +1346 C C . MET A 162 ? 0.1416 0.1418 0.1238 0.0049 -0.0260 -0.0044 162 MET A C +1347 O O . MET A 162 ? 0.1424 0.1411 0.1235 0.0045 -0.0277 -0.0045 162 MET A O +1348 C CB . MET A 162 ? 0.1523 0.1551 0.1451 0.0037 -0.0230 -0.0039 162 MET A CB +1349 C CG . MET A 162 ? 0.1644 0.1693 0.1574 0.0056 -0.0240 -0.0021 162 MET A CG +1350 S SD . MET A 162 ? 0.1893 0.1969 0.1903 0.0060 -0.0227 -0.0004 162 MET A SD +1351 C CE . MET A 162 ? 0.2042 0.2095 0.2055 0.0044 -0.0201 -0.0018 162 MET A CE +1352 N N . HIS A 163 ? 0.1442 0.1446 0.1233 0.0066 -0.0259 -0.0033 163 HIS A N +1353 C CA . HIS A 163 ? 0.1463 0.1439 0.1192 0.0088 -0.0267 -0.0027 163 HIS A CA +1354 C C . HIS A 163 ? 0.1486 0.1451 0.1197 0.0103 -0.0278 -0.0017 163 HIS A C +1355 O O . HIS A 163 ? 0.1525 0.1519 0.1271 0.0113 -0.0271 -0.0001 163 HIS A O +1356 C CB . HIS A 163 ? 0.1596 0.1579 0.1309 0.0107 -0.0252 -0.0006 163 HIS A CB +1357 C CG . HIS A 163 ? 0.1737 0.1674 0.1376 0.0134 -0.0246 -0.0001 163 HIS A CG +1358 N ND1 . HIS A 163 ? 0.1932 0.1824 0.1522 0.0125 -0.0257 -0.0021 163 HIS A ND1 +1359 C CD2 . HIS A 163 ? 0.1884 0.1803 0.1484 0.0172 -0.0229 0.0023 163 HIS A CD2 +1360 C CE1 . HIS A 163 ? 0.2062 0.1900 0.1576 0.0155 -0.0245 -0.0012 163 HIS A CE1 +1361 N NE2 . HIS A 163 ? 0.2005 0.1855 0.1519 0.0186 -0.0224 0.0014 163 HIS A NE2 +1362 N N . HIS A 164 ? 0.1504 0.1420 0.1151 0.0102 -0.0297 -0.0023 164 HIS A N +1363 C CA . HIS A 164 ? 0.1691 0.1581 0.1297 0.0109 -0.0315 -0.0012 164 HIS A CA +1364 C C . HIS A 164 ? 0.1951 0.1761 0.1434 0.0131 -0.0314 -0.0013 164 HIS A C +1365 O O . HIS A 164 ? 0.2104 0.1892 0.1541 0.0150 -0.0310 -0.0001 164 HIS A O +1366 C CB . HIS A 164 ? 0.1722 0.1610 0.1352 0.0075 -0.0351 -0.0010 164 HIS A CB +1367 C CG . HIS A 164 ? 0.1532 0.1487 0.1278 0.0062 -0.0345 0.0001 164 HIS A CG +1368 N ND1 . HIS A 164 ? 0.1547 0.1526 0.1337 0.0053 -0.0361 0.0025 164 HIS A ND1 +1369 C CD2 . HIS A 164 ? 0.1520 0.1510 0.1338 0.0054 -0.0321 -0.0006 164 HIS A CD2 +1370 C CE1 . HIS A 164 ? 0.1538 0.1568 0.1431 0.0046 -0.0342 0.0033 164 HIS A CE1 +1371 N NE2 . HIS A 164 ? 0.1584 0.1614 0.1487 0.0047 -0.0316 0.0011 164 HIS A NE2 +1372 N N A MET A 165 ? 0.2107 0.1865 0.1532 0.0126 -0.0317 -0.0029 165 MET A N +1373 N N B MET A 165 ? 0.1993 0.1751 0.1418 0.0126 -0.0317 -0.0029 165 MET A N +1374 C CA A MET A 165 ? 0.2385 0.2048 0.1679 0.0154 -0.0305 -0.0030 165 MET A CA +1375 C CA B MET A 165 ? 0.2125 0.1782 0.1414 0.0148 -0.0313 -0.0032 165 MET A CA +1376 C C A MET A 165 ? 0.2389 0.2011 0.1640 0.0169 -0.0281 -0.0037 165 MET A C +1377 C C B MET A 165 ? 0.2261 0.1882 0.1511 0.0168 -0.0283 -0.0038 165 MET A C +1378 O O A MET A 165 ? 0.2340 0.1991 0.1642 0.0146 -0.0292 -0.0048 165 MET A O +1379 O O B MET A 165 ? 0.2205 0.1856 0.1506 0.0147 -0.0292 -0.0048 165 MET A O +1380 C CB A MET A 165 ? 0.2700 0.2275 0.1892 0.0129 -0.0348 -0.0039 165 MET A CB +1381 C CB B MET A 165 ? 0.2153 0.1739 0.1371 0.0111 -0.0364 -0.0044 165 MET A CB +1382 C CG A MET A 165 ? 0.3156 0.2749 0.2397 0.0085 -0.0389 -0.0047 165 MET A CG +1383 C CG B MET A 165 ? 0.2179 0.1802 0.1450 0.0075 -0.0407 -0.0030 165 MET A CG +1384 S SD A MET A 165 ? 0.4189 0.3763 0.3410 0.0048 -0.0446 -0.0030 165 MET A SD +1385 S SD B MET A 165 ? 0.2343 0.1928 0.1536 0.0091 -0.0411 -0.0013 165 MET A SD +1386 C CE A MET A 165 ? 0.4248 0.3833 0.3446 0.0084 -0.0417 -0.0014 165 MET A CE +1387 C CE B MET A 165 ? 0.2937 0.2357 0.1926 0.0073 -0.0447 -0.0026 165 MET A CE +1388 N N . GLU A 166 ? 0.2493 0.2015 0.1619 0.0199 -0.0262 -0.0036 166 GLU A N +1389 C CA . GLU A 166 ? 0.2711 0.2172 0.1777 0.0221 -0.0233 -0.0039 166 GLU A CA +1390 C C . GLU A 166 ? 0.3063 0.2383 0.1974 0.0209 -0.0257 -0.0062 166 GLU A C +1391 O O . GLU A 166 ? 0.3201 0.2445 0.2007 0.0219 -0.0259 -0.0061 166 GLU A O +1392 C CB . GLU A 166 ? 0.2977 0.2430 0.2027 0.0279 -0.0169 -0.0007 166 GLU A CB +1393 C CG . GLU A 166 ? 0.3512 0.2905 0.2515 0.0306 -0.0131 -0.0001 166 GLU A CG +1394 C CD . GLU A 166 ? 0.4030 0.3466 0.3083 0.0360 -0.0068 0.0049 166 GLU A CD +1395 O OE1 . GLU A 166 ? 0.4265 0.3640 0.3240 0.0405 -0.0028 0.0068 166 GLU A OE1 +1396 O OE2 . GLU A 166 ? 0.3872 0.3407 0.3047 0.0354 -0.0062 0.0075 166 GLU A OE2 +1397 N N . LEU A 167 ? 0.3244 0.2526 0.2134 0.0184 -0.0279 -0.0079 167 LEU A N +1398 C CA . LEU A 167 ? 0.3661 0.2796 0.2395 0.0166 -0.0309 -0.0100 167 LEU A CA +1399 C C . LEU A 167 ? 0.4043 0.3052 0.2639 0.0220 -0.0247 -0.0099 167 LEU A C +1400 O O . LEU A 167 ? 0.3997 0.3053 0.2653 0.0264 -0.0187 -0.0078 167 LEU A O +1401 C CB . LEU A 167 ? 0.3754 0.2902 0.2534 0.0124 -0.0348 -0.0113 167 LEU A CB +1402 C CG . LEU A 167 ? 0.4016 0.3291 0.2946 0.0079 -0.0394 -0.0107 167 LEU A CG +1403 C CD1 . LEU A 167 ? 0.4176 0.3442 0.3127 0.0040 -0.0432 -0.0114 167 LEU A CD1 +1404 C CD2 . LEU A 167 ? 0.4117 0.3399 0.3045 0.0050 -0.0439 -0.0097 167 LEU A CD2 +1405 N N . PRO A 168 ? 0.4393 0.3232 0.2800 0.0214 -0.0261 -0.0117 168 PRO A N +1406 C CA . PRO A 168 ? 0.4669 0.3364 0.2926 0.0271 -0.0190 -0.0117 168 PRO A CA +1407 C C . PRO A 168 ? 0.4820 0.3517 0.3119 0.0298 -0.0144 -0.0111 168 PRO A C +1408 O O . PRO A 168 ? 0.5059 0.3678 0.3287 0.0360 -0.0067 -0.0095 168 PRO A O +1409 C CB . PRO A 168 ? 0.4906 0.3403 0.2940 0.0240 -0.0231 -0.0145 168 PRO A CB +1410 C CG . PRO A 168 ? 0.4903 0.3464 0.2981 0.0179 -0.0313 -0.0145 168 PRO A CG +1411 C CD . PRO A 168 ? 0.4489 0.3251 0.2801 0.0155 -0.0339 -0.0133 168 PRO A CD +1412 N N . THR A 169 ? 0.4686 0.3473 0.3103 0.0257 -0.0187 -0.0118 169 THR A N +1413 C CA . THR A 169 ? 0.4668 0.3475 0.3142 0.0278 -0.0149 -0.0108 169 THR A CA +1414 C C . THR A 169 ? 0.4478 0.3455 0.3136 0.0302 -0.0111 -0.0070 169 THR A C +1415 O O . THR A 169 ? 0.4469 0.3484 0.3194 0.0311 -0.0089 -0.0055 169 THR A O +1416 C CB . THR A 169 ? 0.4914 0.3711 0.3402 0.0222 -0.0211 -0.0131 169 THR A CB +1417 O OG1 . THR A 169 ? 0.4986 0.3909 0.3595 0.0169 -0.0276 -0.0134 169 THR A OG1 +1418 C CG2 . THR A 169 ? 0.5117 0.3714 0.3405 0.0203 -0.0239 -0.0159 169 THR A CG2 +1419 N N . GLY A 170 ? 0.4288 0.3363 0.3024 0.0310 -0.0107 -0.0052 170 GLY A N +1420 C CA . GLY A 170 ? 0.4084 0.3306 0.2979 0.0327 -0.0078 -0.0012 170 GLY A CA +1421 C C . GLY A 170 ? 0.3825 0.3184 0.2863 0.0276 -0.0126 -0.0018 170 GLY A C +1422 O O . GLY A 170 ? 0.3849 0.3314 0.3003 0.0280 -0.0110 0.0014 170 GLY A O +1423 N N . VAL A 171 ? 0.3537 0.2884 0.2562 0.0226 -0.0185 -0.0054 171 VAL A N +1424 C CA . VAL A 171 ? 0.3148 0.2609 0.2295 0.0182 -0.0223 -0.0060 171 VAL A CA +1425 C C . VAL A 171 ? 0.2636 0.2147 0.1821 0.0166 -0.0248 -0.0064 171 VAL A C +1426 O O . VAL A 171 ? 0.2655 0.2109 0.1765 0.0180 -0.0248 -0.0066 171 VAL A O +1427 C CB . VAL A 171 ? 0.3351 0.2792 0.2497 0.0143 -0.0262 -0.0082 171 VAL A CB +1428 C CG1 . VAL A 171 ? 0.3511 0.2915 0.2636 0.0161 -0.0234 -0.0074 171 VAL A CG1 +1429 C CG2 . VAL A 171 ? 0.3457 0.2805 0.2507 0.0118 -0.0307 -0.0104 171 VAL A CG2 +1430 N N . HIS A 172 ? 0.2320 0.1932 0.1615 0.0137 -0.0265 -0.0064 172 HIS A N +1431 C CA . HIS A 172 ? 0.2098 0.1766 0.1447 0.0127 -0.0277 -0.0062 172 HIS A CA +1432 C C . HIS A 172 ? 0.2010 0.1704 0.1405 0.0086 -0.0317 -0.0076 172 HIS A C +1433 O O . HIS A 172 ? 0.2016 0.1725 0.1443 0.0062 -0.0330 -0.0084 172 HIS A O +1434 C CB . HIS A 172 ? 0.1986 0.1740 0.1423 0.0134 -0.0251 -0.0041 172 HIS A CB +1435 C CG . HIS A 172 ? 0.1979 0.1719 0.1392 0.0177 -0.0211 -0.0010 172 HIS A CG +1436 N ND1 . HIS A 172 ? 0.2129 0.1892 0.1572 0.0184 -0.0190 0.0013 172 HIS A ND1 +1437 C CD2 . HIS A 172 ? 0.2140 0.1836 0.1495 0.0216 -0.0186 0.0006 172 HIS A CD2 +1438 C CE1 . HIS A 172 ? 0.2212 0.1955 0.1633 0.0229 -0.0150 0.0048 172 HIS A CE1 +1439 N NE2 . HIS A 172 ? 0.2297 0.1995 0.1659 0.0252 -0.0143 0.0044 172 HIS A NE2 +1440 N N . ALA A 173 ? 0.1934 0.1642 0.1343 0.0080 -0.0331 -0.0072 173 ALA A N +1441 C CA . ALA A 173 ? 0.1885 0.1623 0.1353 0.0046 -0.0364 -0.0072 173 ALA A CA +1442 C C . ALA A 173 ? 0.1771 0.1575 0.1317 0.0048 -0.0352 -0.0061 173 ALA A C +1443 O O . ALA A 173 ? 0.1781 0.1590 0.1312 0.0072 -0.0336 -0.0053 173 ALA A O +1444 C CB . ALA A 173 ? 0.1967 0.1635 0.1362 0.0027 -0.0408 -0.0069 173 ALA A CB +1445 N N . GLY A 174 ? 0.1663 0.1516 0.1295 0.0026 -0.0356 -0.0057 174 GLY A N +1446 C CA . GLY A 174 ? 0.1590 0.1496 0.1298 0.0028 -0.0340 -0.0047 174 GLY A CA +1447 C C . GLY A 174 ? 0.1505 0.1445 0.1298 0.0006 -0.0341 -0.0036 174 GLY A C +1448 O O . GLY A 174 ? 0.1524 0.1453 0.1323 -0.0012 -0.0363 -0.0029 174 GLY A O +1449 N N . THR A 175 ? 0.1423 0.1401 0.1283 0.0010 -0.0314 -0.0030 175 THR A N +1450 C CA . THR A 175 ? 0.1365 0.1372 0.1314 -0.0001 -0.0302 -0.0010 175 THR A CA +1451 C C . THR A 175 ? 0.1378 0.1390 0.1355 0.0001 -0.0256 -0.0025 175 THR A C +1452 O O . THR A 175 ? 0.1427 0.1426 0.1360 0.0006 -0.0241 -0.0047 175 THR A O +1453 C CB . THR A 175 ? 0.1438 0.1473 0.1442 0.0003 -0.0307 0.0017 175 THR A CB +1454 O OG1 . THR A 175 ? 0.1485 0.1530 0.1492 0.0019 -0.0277 0.0004 175 THR A OG1 +1455 C CG2 . THR A 175 ? 0.1331 0.1350 0.1289 -0.0004 -0.0355 0.0032 175 THR A CG2 +1456 N N . ASP A 176 ? 0.1357 0.1384 0.1409 -0.0003 -0.0231 -0.0006 176 ASP A N +1457 C CA . ASP A 176 ? 0.1402 0.1414 0.1467 0.0002 -0.0177 -0.0019 176 ASP A CA +1458 C C . ASP A 176 ? 0.1491 0.1512 0.1593 0.0014 -0.0159 -0.0011 176 ASP A C +1459 O O . ASP A 176 ? 0.1476 0.1524 0.1594 0.0017 -0.0190 0.0005 176 ASP A O +1460 C CB . ASP A 176 ? 0.1529 0.1542 0.1652 0.0002 -0.0144 0.0002 176 ASP A CB +1461 C CG . ASP A 176 ? 0.1714 0.1768 0.1944 0.0005 -0.0146 0.0055 176 ASP A CG +1462 O OD1 . ASP A 176 ? 0.1481 0.1558 0.1743 0.0008 -0.0165 0.0072 176 ASP A OD1 +1463 O OD2 . ASP A 176 ? 0.1979 0.2047 0.2269 0.0004 -0.0132 0.0086 176 ASP A OD2 +1464 N N . LEU A 177 ? 0.1557 0.1549 0.1667 0.0018 -0.0108 -0.0021 177 LEU A N +1465 C CA . LEU A 177 ? 0.1647 0.1641 0.1791 0.0028 -0.0091 -0.0014 177 LEU A CA +1466 C C . LEU A 177 ? 0.1765 0.1794 0.2020 0.0040 -0.0071 0.0031 177 LEU A C +1467 O O . LEU A 177 ? 0.1817 0.1855 0.2115 0.0049 -0.0057 0.0043 177 LEU A O +1468 C CB . LEU A 177 ? 0.1687 0.1618 0.1774 0.0023 -0.0052 -0.0044 177 LEU A CB +1469 C CG . LEU A 177 ? 0.1860 0.1781 0.1872 0.0009 -0.0085 -0.0067 177 LEU A CG +1470 C CD1 . LEU A 177 ? 0.1940 0.1903 0.1990 0.0020 -0.0110 -0.0050 177 LEU A CD1 +1471 C CD2 . LEU A 177 ? 0.2019 0.1950 0.1976 -0.0001 -0.0120 -0.0078 177 LEU A CD2 +1472 N N . GLU A 178 ? 0.1687 0.1743 0.1999 0.0038 -0.0076 0.0064 178 GLU A N +1473 C CA . GLU A 178 ? 0.1564 0.1671 0.1995 0.0043 -0.0076 0.0123 178 GLU A CA +1474 C C . GLU A 178 ? 0.1508 0.1657 0.1938 0.0026 -0.0152 0.0143 178 GLU A C +1475 O O . GLU A 178 ? 0.1516 0.1712 0.2037 0.0020 -0.0171 0.0198 178 GLU A O +1476 C CB . GLU A 178 ? 0.1777 0.1894 0.2282 0.0047 -0.0044 0.0162 178 GLU A CB +1477 C CG . GLU A 178 ? 0.2469 0.2527 0.2963 0.0068 0.0043 0.0145 178 GLU A CG +1478 C CD . GLU A 178 ? 0.3511 0.3573 0.4079 0.0081 0.0092 0.0189 178 GLU A CD +1479 O OE1 . GLU A 178 ? 0.3485 0.3603 0.4119 0.0068 0.0049 0.0235 178 GLU A OE1 +1480 O OE2 . GLU A 178 ? 0.4024 0.4025 0.4580 0.0103 0.0175 0.0182 178 GLU A OE2 +1481 N N . GLY A 179 ? 0.1512 0.1640 0.1836 0.0018 -0.0194 0.0105 179 GLY A N +1482 C CA . GLY A 179 ? 0.1460 0.1601 0.1751 0.0006 -0.0257 0.0117 179 GLY A CA +1483 C C . GLY A 179 ? 0.1411 0.1548 0.1686 -0.0018 -0.0306 0.0136 179 GLY A C +1484 O O . GLY A 179 ? 0.1464 0.1596 0.1702 -0.0034 -0.0361 0.0151 179 GLY A O +1485 N N . ASN A 180 ? 0.1351 0.1482 0.1645 -0.0022 -0.0289 0.0137 180 ASN A N +1486 C CA . ASN A 180 ? 0.1386 0.1510 0.1668 -0.0047 -0.0339 0.0158 180 ASN A CA +1487 C C . ASN A 180 ? 0.1367 0.1440 0.1525 -0.0048 -0.0357 0.0106 180 ASN A C +1488 O O . ASN A 180 ? 0.1297 0.1355 0.1425 -0.0035 -0.0318 0.0071 180 ASN A O +1489 C CB . ASN A 180 ? 0.1521 0.1674 0.1905 -0.0049 -0.0310 0.0197 180 ASN A CB +1490 C CG . ASN A 180 ? 0.1866 0.2074 0.2390 -0.0049 -0.0296 0.0267 180 ASN A CG +1491 O OD1 . ASN A 180 ? 0.2108 0.2333 0.2715 -0.0025 -0.0227 0.0285 180 ASN A OD1 +1492 N ND2 . ASN A 180 ? 0.1778 0.2009 0.2326 -0.0074 -0.0358 0.0310 180 ASN A ND2 +1493 N N . PHE A 181 ? 0.1401 0.1438 0.1479 -0.0066 -0.0415 0.0105 181 PHE A N +1494 C CA . PHE A 181 ? 0.1528 0.1509 0.1490 -0.0063 -0.0427 0.0062 181 PHE A CA +1495 C C . PHE A 181 ? 0.1580 0.1562 0.1561 -0.0071 -0.0419 0.0060 181 PHE A C +1496 O O . PHE A 181 ? 0.1538 0.1548 0.1602 -0.0089 -0.0430 0.0100 181 PHE A O +1497 C CB . PHE A 181 ? 0.1623 0.1544 0.1484 -0.0081 -0.0487 0.0065 181 PHE A CB +1498 C CG . PHE A 181 ? 0.1681 0.1570 0.1456 -0.0060 -0.0481 0.0043 181 PHE A CG +1499 C CD1 . PHE A 181 ? 0.1711 0.1620 0.1510 -0.0062 -0.0494 0.0068 181 PHE A CD1 +1500 C CD2 . PHE A 181 ? 0.1768 0.1609 0.1444 -0.0036 -0.0461 0.0005 181 PHE A CD2 +1501 C CE1 . PHE A 181 ? 0.1778 0.1658 0.1498 -0.0040 -0.0486 0.0052 181 PHE A CE1 +1502 C CE2 . PHE A 181 ? 0.1865 0.1678 0.1470 -0.0011 -0.0449 -0.0005 181 PHE A CE2 +1503 C CZ . PHE A 181 ? 0.1834 0.1666 0.1458 -0.0012 -0.0461 0.0017 181 PHE A CZ +1504 N N . TYR A 182 ? 0.1537 0.1491 0.1449 -0.0058 -0.0398 0.0019 182 TYR A N +1505 C CA . TYR A 182 ? 0.1648 0.1594 0.1557 -0.0067 -0.0400 0.0014 182 TYR A CA +1506 C C . TYR A 182 ? 0.1812 0.1704 0.1651 -0.0089 -0.0460 0.0020 182 TYR A C +1507 O O . TYR A 182 ? 0.1923 0.1761 0.1665 -0.0083 -0.0478 0.0002 182 TYR A O +1508 C CB . TYR A 182 ? 0.1636 0.1569 0.1491 -0.0050 -0.0364 -0.0026 182 TYR A CB +1509 C CG . TYR A 182 ? 0.1610 0.1576 0.1518 -0.0041 -0.0312 -0.0031 182 TYR A CG +1510 C CD1 . TYR A 182 ? 0.1643 0.1626 0.1605 -0.0046 -0.0286 -0.0020 182 TYR A CD1 +1511 C CD2 . TYR A 182 ? 0.1635 0.1606 0.1534 -0.0027 -0.0287 -0.0044 182 TYR A CD2 +1512 C CE1 . TYR A 182 ? 0.1644 0.1631 0.1626 -0.0038 -0.0232 -0.0028 182 TYR A CE1 +1513 C CE2 . TYR A 182 ? 0.1670 0.1648 0.1595 -0.0023 -0.0242 -0.0052 182 TYR A CE2 +1514 C CZ . TYR A 182 ? 0.1702 0.1681 0.1661 -0.0029 -0.0212 -0.0046 182 TYR A CZ +1515 O OH . TYR A 182 ? 0.1692 0.1653 0.1651 -0.0025 -0.0162 -0.0057 182 TYR A OH +1516 N N . GLY A 183 ? 0.1830 0.1729 0.1714 -0.0113 -0.0488 0.0049 183 GLY A N +1517 C CA . GLY A 183 ? 0.2017 0.1853 0.1830 -0.0142 -0.0551 0.0058 183 GLY A CA +1518 C C . GLY A 183 ? 0.2106 0.1916 0.1898 -0.0167 -0.0605 0.0087 183 GLY A C +1519 O O . GLY A 183 ? 0.2050 0.1914 0.1923 -0.0166 -0.0597 0.0118 183 GLY A O +1520 N N . PRO A 184 ? 0.2194 0.1910 0.1864 -0.0190 -0.0659 0.0079 184 PRO A N +1521 C CA . PRO A 184 ? 0.2234 0.1908 0.1861 -0.0227 -0.0724 0.0112 184 PRO A CA +1522 C C . PRO A 184 ? 0.2274 0.1897 0.1796 -0.0209 -0.0716 0.0086 184 PRO A C +1523 O O . PRO A 184 ? 0.2463 0.2028 0.1912 -0.0241 -0.0773 0.0107 184 PRO A O +1524 C CB . PRO A 184 ? 0.2447 0.2017 0.1965 -0.0264 -0.0787 0.0110 184 PRO A CB +1525 C CG . PRO A 184 ? 0.2552 0.2077 0.1988 -0.0224 -0.0734 0.0051 184 PRO A CG +1526 C CD . PRO A 184 ? 0.2274 0.1912 0.1842 -0.0190 -0.0667 0.0046 184 PRO A CD +1527 N N . PHE A 185 ? 0.2187 0.1827 0.1693 -0.0159 -0.0649 0.0045 185 PHE A N +1528 C CA . PHE A 185 ? 0.2245 0.1836 0.1649 -0.0134 -0.0632 0.0022 185 PHE A CA +1529 C C . PHE A 185 ? 0.2280 0.1925 0.1746 -0.0138 -0.0639 0.0052 185 PHE A C +1530 O O . PHE A 185 ? 0.2167 0.1908 0.1780 -0.0146 -0.0631 0.0084 185 PHE A O +1531 C CB . PHE A 185 ? 0.2196 0.1798 0.1582 -0.0083 -0.0562 -0.0017 185 PHE A CB +1532 C CG . PHE A 185 ? 0.2271 0.1816 0.1595 -0.0080 -0.0557 -0.0041 185 PHE A CG +1533 C CD1 . PHE A 185 ? 0.2458 0.1877 0.1632 -0.0089 -0.0586 -0.0054 185 PHE A CD1 +1534 C CD2 . PHE A 185 ? 0.2299 0.1909 0.1710 -0.0072 -0.0527 -0.0047 185 PHE A CD2 +1535 C CE1 . PHE A 185 ? 0.2512 0.1878 0.1637 -0.0087 -0.0581 -0.0071 185 PHE A CE1 +1536 C CE2 . PHE A 185 ? 0.2336 0.1901 0.1701 -0.0073 -0.0526 -0.0062 185 PHE A CE2 +1537 C CZ . PHE A 185 ? 0.2389 0.1835 0.1617 -0.0078 -0.0552 -0.0074 185 PHE A CZ +1538 N N . VAL A 186 ? 0.2393 0.1970 0.1744 -0.0134 -0.0652 0.0045 186 VAL A N +1539 C CA . VAL A 186 ? 0.2422 0.2041 0.1814 -0.0139 -0.0663 0.0074 186 VAL A CA +1540 C C . VAL A 186 ? 0.2486 0.2085 0.1806 -0.0092 -0.0614 0.0047 186 VAL A C +1541 O O . VAL A 186 ? 0.2669 0.2189 0.1870 -0.0063 -0.0588 0.0013 186 VAL A O +1542 C CB . VAL A 186 ? 0.2610 0.2167 0.1934 -0.0196 -0.0747 0.0112 186 VAL A CB +1543 C CG1 . VAL A 186 ? 0.2715 0.2320 0.2153 -0.0245 -0.0797 0.0160 186 VAL A CG1 +1544 C CG2 . VAL A 186 ? 0.2830 0.2224 0.1930 -0.0204 -0.0773 0.0080 186 VAL A CG2 +1545 N N . ASP A 187 ? 0.2285 0.1956 0.1684 -0.0081 -0.0601 0.0069 187 ASP A N +1546 C CA . ASP A 187 ? 0.2303 0.1966 0.1651 -0.0037 -0.0557 0.0053 187 ASP A CA +1547 C C . ASP A 187 ? 0.2549 0.2120 0.1752 -0.0047 -0.0590 0.0061 187 ASP A C +1548 O O . ASP A 187 ? 0.2531 0.2136 0.1759 -0.0047 -0.0597 0.0085 187 ASP A O +1549 C CB . ASP A 187 ? 0.2152 0.1930 0.1649 -0.0016 -0.0519 0.0067 187 ASP A CB +1550 C CG . ASP A 187 ? 0.2089 0.1944 0.1717 -0.0048 -0.0548 0.0111 187 ASP A CG +1551 O OD1 . ASP A 187 ? 0.2092 0.1923 0.1709 -0.0092 -0.0606 0.0141 187 ASP A OD1 +1552 O OD2 . ASP A 187 ? 0.1961 0.1897 0.1704 -0.0029 -0.0512 0.0121 187 ASP A OD2 +1553 N N . ARG A 188 ? 0.2821 0.2263 0.1859 -0.0057 -0.0611 0.0040 188 ARG A N +1554 C CA . ARG A 188 ? 0.3215 0.2525 0.2064 -0.0070 -0.0642 0.0040 188 ARG A CA +1555 C C . ARG A 188 ? 0.3521 0.2702 0.2206 -0.0035 -0.0603 0.0000 188 ARG A C +1556 O O . ARG A 188 ? 0.3475 0.2648 0.2178 -0.0036 -0.0596 -0.0019 188 ARG A O +1557 C CB . ARG A 188 ? 0.3562 0.2825 0.2376 -0.0146 -0.0735 0.0070 188 ARG A CB +1558 C CG . ARG A 188 ? 0.4405 0.3529 0.3017 -0.0173 -0.0780 0.0076 188 ARG A CG +1559 C CD . ARG A 188 ? 0.5164 0.4237 0.3738 -0.0260 -0.0885 0.0114 188 ARG A CD +1560 N NE . ARG A 188 ? 0.5940 0.4813 0.4246 -0.0288 -0.0924 0.0099 188 ARG A NE +1561 C CZ . ARG A 188 ? 0.6437 0.5225 0.4646 -0.0369 -0.1024 0.0134 188 ARG A CZ +1562 N NH1 . ARG A 188 ? 0.6388 0.5290 0.4771 -0.0431 -0.1096 0.0195 188 ARG A NH1 +1563 N NH2 . ARG A 188 ? 0.6649 0.5232 0.4584 -0.0392 -0.1053 0.0113 188 ARG A NH2 +1564 N N . GLN A 189 ? 0.3850 0.2930 0.2379 -0.0002 -0.0573 -0.0009 189 GLN A N +1565 C CA . GLN A 189 ? 0.4227 0.3172 0.2593 0.0041 -0.0522 -0.0040 189 GLN A CA +1566 C C . GLN A 189 ? 0.4583 0.3352 0.2753 -0.0010 -0.0582 -0.0054 189 GLN A C +1567 O O . GLN A 189 ? 0.4780 0.3414 0.2765 -0.0022 -0.0601 -0.0054 189 GLN A O +1568 C CB . GLN A 189 ? 0.4560 0.3469 0.2846 0.0103 -0.0454 -0.0036 189 GLN A CB +1569 C CG . GLN A 189 ? 0.5266 0.4059 0.3421 0.0164 -0.0378 -0.0056 189 GLN A CG +1570 C CD . GLN A 189 ? 0.6110 0.4864 0.4185 0.0225 -0.0312 -0.0040 189 GLN A CD +1571 O OE1 . GLN A 189 ? 0.6280 0.5166 0.4490 0.0248 -0.0292 -0.0013 189 GLN A OE1 +1572 N NE2 . GLN A 189 ? 0.6387 0.4950 0.4234 0.0254 -0.0275 -0.0054 189 GLN A NE2 +1573 N N . THR A 190 ? 0.4705 0.3476 0.2918 -0.0045 -0.0618 -0.0063 190 THR A N +1574 C CA . THR A 190 ? 0.5034 0.3648 0.3086 -0.0104 -0.0687 -0.0071 190 THR A CA +1575 C C . THR A 190 ? 0.5160 0.3722 0.3190 -0.0089 -0.0662 -0.0100 190 THR A C +1576 O O . THR A 190 ? 0.5161 0.3828 0.3322 -0.0039 -0.0597 -0.0107 190 THR A O +1577 C CB . THR A 190 ? 0.5318 0.4010 0.3480 -0.0186 -0.0788 -0.0031 190 THR A CB +1578 O OG1 . THR A 190 ? 0.5408 0.4293 0.3822 -0.0179 -0.0774 -0.0014 190 THR A OG1 +1579 C CG2 . THR A 190 ? 0.5465 0.4150 0.3586 -0.0220 -0.0835 0.0001 190 THR A CG2 +1580 N N . ALA A 191 ? 0.5262 0.3663 0.3131 -0.0138 -0.0719 -0.0112 191 ALA A N +1581 C CA . ALA A 191 ? 0.5322 0.3675 0.3178 -0.0132 -0.0705 -0.0134 191 ALA A CA +1582 C C . ALA A 191 ? 0.5178 0.3715 0.3276 -0.0162 -0.0740 -0.0110 191 ALA A C +1583 O O . ALA A 191 ? 0.5351 0.3910 0.3496 -0.0232 -0.0828 -0.0080 191 ALA A O +1584 C CB . ALA A 191 ? 0.5515 0.3644 0.3138 -0.0185 -0.0768 -0.0149 191 ALA A CB +1585 N N . GLN A 192 ? 0.4838 0.3510 0.3093 -0.0110 -0.0671 -0.0115 192 GLN A N +1586 C CA . GLN A 192 ? 0.4556 0.3388 0.3022 -0.0128 -0.0686 -0.0098 192 GLN A CA +1587 C C . GLN A 192 ? 0.4553 0.3366 0.3017 -0.0092 -0.0634 -0.0122 192 GLN A C +1588 O O . GLN A 192 ? 0.4729 0.3568 0.3204 -0.0031 -0.0556 -0.0134 192 GLN A O +1589 C CB . GLN A 192 ? 0.4330 0.3339 0.2979 -0.0100 -0.0647 -0.0081 192 GLN A CB +1590 C CG . GLN A 192 ? 0.4245 0.3272 0.2891 -0.0117 -0.0676 -0.0057 192 GLN A CG +1591 C CD . GLN A 192 ? 0.3715 0.2920 0.2566 -0.0101 -0.0647 -0.0038 192 GLN A CD +1592 O OE1 . GLN A 192 ? 0.3411 0.2712 0.2406 -0.0125 -0.0666 -0.0019 192 GLN A OE1 +1593 N NE2 . GLN A 192 ? 0.3545 0.2788 0.2407 -0.0057 -0.0597 -0.0041 192 GLN A NE2 +1594 N N . ALA A 193 ? 0.4362 0.3127 0.2810 -0.0129 -0.0677 -0.0124 193 ALA A N +1595 C CA . ALA A 193 ? 0.4262 0.3013 0.2715 -0.0096 -0.0629 -0.0143 193 ALA A CA +1596 C C . ALA A 193 ? 0.4005 0.2918 0.2661 -0.0109 -0.0634 -0.0126 193 ALA A C +1597 O O . ALA A 193 ? 0.3993 0.2976 0.2745 -0.0157 -0.0693 -0.0099 193 ALA A O +1598 C CB . ALA A 193 ? 0.4384 0.2947 0.2658 -0.0122 -0.0662 -0.0160 193 ALA A CB +1599 N N . ALA A 194 ? 0.3784 0.2757 0.2506 -0.0066 -0.0571 -0.0136 194 ALA A N +1600 C CA . ALA A 194 ? 0.3522 0.2633 0.2414 -0.0076 -0.0568 -0.0123 194 ALA A CA +1601 C C . ALA A 194 ? 0.3308 0.2368 0.2184 -0.0108 -0.0606 -0.0122 194 ALA A C +1602 O O . ALA A 194 ? 0.3411 0.2333 0.2150 -0.0104 -0.0607 -0.0139 194 ALA A O +1603 C CB . ALA A 194 ? 0.3502 0.2696 0.2465 -0.0025 -0.0493 -0.0129 194 ALA A CB +1604 N N . GLY A 195 ? 0.2987 0.2156 0.2004 -0.0136 -0.0632 -0.0100 195 GLY A N +1605 C CA . GLY A 195 ? 0.2911 0.2060 0.1945 -0.0164 -0.0665 -0.0092 195 GLY A CA +1606 C C . GLY A 195 ? 0.2800 0.1973 0.1857 -0.0127 -0.0606 -0.0108 195 GLY A C +1607 O O . GLY A 195 ? 0.2772 0.1964 0.1819 -0.0082 -0.0544 -0.0122 195 GLY A O +1608 N N . THR A 196 ? 0.2668 0.1859 0.1776 -0.0148 -0.0627 -0.0097 196 THR A N +1609 C CA . THR A 196 ? 0.2699 0.1913 0.1834 -0.0121 -0.0581 -0.0105 196 THR A CA +1610 C C . THR A 196 ? 0.2685 0.2034 0.1931 -0.0095 -0.0527 -0.0101 196 THR A C +1611 O O . THR A 196 ? 0.2559 0.2007 0.1909 -0.0111 -0.0536 -0.0087 196 THR A O +1612 C CB . THR A 196 ? 0.2861 0.2086 0.2049 -0.0155 -0.0621 -0.0088 196 THR A CB +1613 O OG1 . THR A 196 ? 0.3079 0.2169 0.2157 -0.0191 -0.0684 -0.0087 196 THR A OG1 +1614 C CG2 . THR A 196 ? 0.2955 0.2193 0.2161 -0.0131 -0.0578 -0.0092 196 THR A CG2 +1615 N N . ASP A 197 ? 0.2743 0.2089 0.1966 -0.0054 -0.0470 -0.0110 197 ASP A N +1616 C CA . ASP A 197 ? 0.2719 0.2186 0.2041 -0.0038 -0.0428 -0.0102 197 ASP A CA +1617 C C . ASP A 197 ? 0.2617 0.2144 0.2013 -0.0050 -0.0423 -0.0090 197 ASP A C +1618 O O . ASP A 197 ? 0.2930 0.2452 0.2321 -0.0030 -0.0392 -0.0083 197 ASP A O +1619 C CB . ASP A 197 ? 0.2997 0.2457 0.2285 0.0004 -0.0377 -0.0102 197 ASP A CB +1620 C CG . ASP A 197 ? 0.3365 0.2940 0.2744 0.0008 -0.0350 -0.0091 197 ASP A CG +1621 O OD1 . ASP A 197 ? 0.2888 0.2537 0.2342 -0.0018 -0.0366 -0.0090 197 ASP A OD1 +1622 O OD2 . ASP A 197 ? 0.3987 0.3570 0.3357 0.0038 -0.0313 -0.0081 197 ASP A OD2 +1623 N N A THR A 198 ? 0.2387 0.1970 0.1855 -0.0081 -0.0454 -0.0081 198 THR A N +1624 N N B THR A 198 ? 0.2362 0.1952 0.1834 -0.0080 -0.0451 -0.0081 198 THR A N +1625 C CA A THR A 198 ? 0.2296 0.1938 0.1834 -0.0094 -0.0450 -0.0068 198 THR A CA +1626 C CA B THR A 198 ? 0.2258 0.1911 0.1806 -0.0097 -0.0452 -0.0067 198 THR A CA +1627 C C A THR A 198 ? 0.2161 0.1890 0.1751 -0.0084 -0.0407 -0.0063 198 THR A C +1628 C C B THR A 198 ? 0.2140 0.1880 0.1741 -0.0088 -0.0409 -0.0063 198 THR A C +1629 O O A THR A 198 ? 0.2153 0.1908 0.1743 -0.0073 -0.0386 -0.0069 198 THR A O +1630 O O B THR A 198 ? 0.2128 0.1903 0.1740 -0.0081 -0.0390 -0.0068 198 THR A O +1631 C CB A THR A 198 ? 0.2460 0.2133 0.2061 -0.0126 -0.0489 -0.0051 198 THR A CB +1632 C CB B THR A 198 ? 0.2355 0.2043 0.1965 -0.0126 -0.0488 -0.0051 198 THR A CB +1633 O OG1 A THR A 198 ? 0.2540 0.2270 0.2191 -0.0130 -0.0483 -0.0046 198 THR A OG1 +1634 O OG1 B THR A 198 ? 0.2486 0.2088 0.2041 -0.0145 -0.0540 -0.0048 198 THR A OG1 +1635 C CG2 A THR A 198 ? 0.2543 0.2123 0.2089 -0.0148 -0.0545 -0.0046 198 THR A CG2 +1636 C CG2 B THR A 198 ? 0.2360 0.2113 0.2051 -0.0142 -0.0487 -0.0032 198 THR A CG2 +1637 N N . THR A 199 ? 0.1998 0.1767 0.1627 -0.0091 -0.0398 -0.0051 199 THR A N +1638 C CA . THR A 199 ? 0.1870 0.1712 0.1538 -0.0093 -0.0367 -0.0041 199 THR A CA +1639 C C . THR A 199 ? 0.1754 0.1658 0.1475 -0.0115 -0.0366 -0.0039 199 THR A C +1640 O O . THR A 199 ? 0.1801 0.1711 0.1555 -0.0128 -0.0384 -0.0031 199 THR A O +1641 C CB . THR A 199 ? 0.2008 0.1857 0.1684 -0.0089 -0.0355 -0.0022 199 THR A CB +1642 O OG1 . THR A 199 ? 0.2126 0.1907 0.1749 -0.0059 -0.0342 -0.0021 199 THR A OG1 +1643 C CG2 . THR A 199 ? 0.2025 0.1949 0.1736 -0.0100 -0.0333 -0.0004 199 THR A CG2 +1644 N N . ILE A 200 ? 0.1639 0.1580 0.1363 -0.0118 -0.0342 -0.0043 200 ILE A N +1645 C CA . ILE A 200 ? 0.1650 0.1627 0.1402 -0.0134 -0.0327 -0.0044 200 ILE A CA +1646 C C . ILE A 200 ? 0.1575 0.1587 0.1338 -0.0153 -0.0318 -0.0030 200 ILE A C +1647 O O . ILE A 200 ? 0.1543 0.1573 0.1284 -0.0166 -0.0304 -0.0027 200 ILE A O +1648 C CB . ILE A 200 ? 0.1682 0.1662 0.1412 -0.0132 -0.0306 -0.0057 200 ILE A CB +1649 C CG1 . ILE A 200 ? 0.1744 0.1693 0.1460 -0.0112 -0.0317 -0.0067 200 ILE A CG1 +1650 C CG2 . ILE A 200 ? 0.1724 0.1717 0.1471 -0.0142 -0.0282 -0.0059 200 ILE A CG2 +1651 C CD1 . ILE A 200 ? 0.1923 0.1873 0.1614 -0.0105 -0.0302 -0.0073 200 ILE A CD1 +1652 N N . THR A 201 ? 0.1548 0.1570 0.1348 -0.0158 -0.0329 -0.0018 201 THR A N +1653 C CA . THR A 201 ? 0.1566 0.1622 0.1383 -0.0175 -0.0324 -0.0001 201 THR A CA +1654 C C . THR A 201 ? 0.1622 0.1698 0.1412 -0.0193 -0.0294 -0.0002 201 THR A C +1655 O O . THR A 201 ? 0.1723 0.1817 0.1493 -0.0212 -0.0293 0.0008 201 THR A O +1656 C CB . THR A 201 ? 0.1688 0.1753 0.1557 -0.0177 -0.0339 0.0016 201 THR A CB +1657 O OG1 . THR A 201 ? 0.1778 0.1802 0.1650 -0.0168 -0.0373 0.0015 201 THR A OG1 +1658 C CG2 . THR A 201 ? 0.1775 0.1876 0.1668 -0.0192 -0.0336 0.0037 201 THR A CG2 +1659 N N . VAL A 202 ? 0.1512 0.1577 0.1297 -0.0189 -0.0270 -0.0012 202 VAL A N +1660 C CA . VAL A 202 ? 0.1608 0.1665 0.1342 -0.0206 -0.0235 -0.0018 202 VAL A CA +1661 C C . VAL A 202 ? 0.1642 0.1685 0.1313 -0.0225 -0.0241 -0.0028 202 VAL A C +1662 O O . VAL A 202 ? 0.1653 0.1690 0.1273 -0.0253 -0.0233 -0.0023 202 VAL A O +1663 C CB . VAL A 202 ? 0.1747 0.1781 0.1485 -0.0192 -0.0197 -0.0024 202 VAL A CB +1664 C CG1 . VAL A 202 ? 0.1879 0.1889 0.1611 -0.0177 -0.0196 -0.0042 202 VAL A CG1 +1665 C CG2 . VAL A 202 ? 0.1887 0.1892 0.1558 -0.0207 -0.0153 -0.0028 202 VAL A CG2 +1666 N N . ASN A 203 ? 0.1651 0.1688 0.1328 -0.0211 -0.0257 -0.0035 203 ASN A N +1667 C CA . ASN A 203 ? 0.1648 0.1681 0.1284 -0.0228 -0.0266 -0.0032 203 ASN A CA +1668 C C . ASN A 203 ? 0.1626 0.1693 0.1276 -0.0244 -0.0287 -0.0002 203 ASN A C +1669 O O . ASN A 203 ? 0.1657 0.1731 0.1272 -0.0277 -0.0295 0.0015 203 ASN A O +1670 C CB . ASN A 203 ? 0.1660 0.1681 0.1308 -0.0203 -0.0272 -0.0042 203 ASN A CB +1671 C CG . ASN A 203 ? 0.1764 0.1755 0.1397 -0.0193 -0.0251 -0.0065 203 ASN A CG +1672 O OD1 . ASN A 203 ? 0.1717 0.1691 0.1335 -0.0200 -0.0225 -0.0074 203 ASN A OD1 +1673 N ND2 . ASN A 203 ? 0.1763 0.1746 0.1404 -0.0173 -0.0256 -0.0072 203 ASN A ND2 +1674 N N . VAL A 204 ? 0.1532 0.1617 0.1232 -0.0225 -0.0298 0.0010 204 VAL A N +1675 C CA . VAL A 204 ? 0.1539 0.1657 0.1264 -0.0236 -0.0311 0.0045 204 VAL A CA +1676 C C . VAL A 204 ? 0.1578 0.1719 0.1285 -0.0274 -0.0312 0.0060 204 VAL A C +1677 O O . VAL A 204 ? 0.1647 0.1814 0.1347 -0.0304 -0.0325 0.0092 204 VAL A O +1678 C CB . VAL A 204 ? 0.1605 0.1719 0.1374 -0.0207 -0.0318 0.0051 204 VAL A CB +1679 C CG1 . VAL A 204 ? 0.1644 0.1793 0.1447 -0.0216 -0.0324 0.0092 204 VAL A CG1 +1680 C CG2 . VAL A 204 ? 0.1563 0.1636 0.1325 -0.0172 -0.0317 0.0037 204 VAL A CG2 +1681 N N . LEU A 205 ? 0.1529 0.1659 0.1227 -0.0275 -0.0297 0.0042 205 LEU A N +1682 C CA . LEU A 205 ? 0.1534 0.1676 0.1201 -0.0309 -0.0291 0.0055 205 LEU A CA +1683 C C . LEU A 205 ? 0.1627 0.1739 0.1206 -0.0346 -0.0288 0.0051 205 LEU A C +1684 O O . LEU A 205 ? 0.1567 0.1691 0.1112 -0.0388 -0.0304 0.0076 205 LEU A O +1685 C CB . LEU A 205 ? 0.1561 0.1693 0.1238 -0.0295 -0.0266 0.0043 205 LEU A CB +1686 C CG . LEU A 205 ? 0.1609 0.1772 0.1370 -0.0272 -0.0280 0.0057 205 LEU A CG +1687 C CD1 . LEU A 205 ? 0.1710 0.1866 0.1501 -0.0253 -0.0259 0.0052 205 LEU A CD1 +1688 C CD2 . LEU A 205 ? 0.1744 0.1949 0.1530 -0.0293 -0.0295 0.0089 205 LEU A CD2 +1689 N N . ALA A 206 ? 0.1654 0.1719 0.1192 -0.0337 -0.0273 0.0021 206 ALA A N +1690 C CA . ALA A 206 ? 0.1774 0.1791 0.1214 -0.0376 -0.0273 0.0015 206 ALA A CA +1691 C C . ALA A 206 ? 0.1821 0.1871 0.1269 -0.0409 -0.0315 0.0053 206 ALA A C +1692 O O . ALA A 206 ? 0.1838 0.1872 0.1217 -0.0462 -0.0334 0.0073 206 ALA A O +1693 C CB . ALA A 206 ? 0.1854 0.1822 0.1269 -0.0354 -0.0251 -0.0019 206 ALA A CB +1694 N N . TRP A 207 ? 0.1684 0.1778 0.1215 -0.0378 -0.0327 0.0070 207 TRP A N +1695 C CA . TRP A 207 ? 0.1712 0.1846 0.1275 -0.0399 -0.0358 0.0120 207 TRP A CA +1696 C C . TRP A 207 ? 0.1705 0.1890 0.1298 -0.0430 -0.0378 0.0168 207 TRP A C +1697 O O . TRP A 207 ? 0.1798 0.2004 0.1382 -0.0476 -0.0409 0.0215 207 TRP A O +1698 C CB . TRP A 207 ? 0.1730 0.1883 0.1366 -0.0347 -0.0352 0.0125 207 TRP A CB +1699 C CG . TRP A 207 ? 0.1756 0.1960 0.1455 -0.0349 -0.0368 0.0187 207 TRP A CG +1700 C CD1 . TRP A 207 ? 0.1911 0.2131 0.1617 -0.0369 -0.0387 0.0226 207 TRP A CD1 +1701 C CD2 . TRP A 207 ? 0.1708 0.1951 0.1482 -0.0323 -0.0362 0.0222 207 TRP A CD2 +1702 N NE1 . TRP A 207 ? 0.1926 0.2200 0.1718 -0.0353 -0.0388 0.0290 207 TRP A NE1 +1703 C CE2 . TRP A 207 ? 0.1823 0.2106 0.1652 -0.0322 -0.0369 0.0286 207 TRP A CE2 +1704 C CE3 . TRP A 207 ? 0.1833 0.2076 0.1635 -0.0297 -0.0349 0.0208 207 TRP A CE3 +1705 C CZ2 . TRP A 207 ? 0.1891 0.2210 0.1800 -0.0292 -0.0355 0.0335 207 TRP A CZ2 +1706 C CZ3 . TRP A 207 ? 0.1929 0.2200 0.1800 -0.0272 -0.0341 0.0251 207 TRP A CZ3 +1707 C CH2 . TRP A 207 ? 0.1892 0.2198 0.1814 -0.0268 -0.0340 0.0314 207 TRP A CH2 +1708 N N . LEU A 208 ? 0.1624 0.1825 0.1250 -0.0411 -0.0364 0.0160 208 LEU A N +1709 C CA . LEU A 208 ? 0.1569 0.1818 0.1222 -0.0441 -0.0381 0.0204 208 LEU A CA +1710 C C . LEU A 208 ? 0.1709 0.1928 0.1260 -0.0504 -0.0394 0.0206 208 LEU A C +1711 O O . LEU A 208 ? 0.1774 0.2027 0.1324 -0.0554 -0.0427 0.0258 208 LEU A O +1712 C CB . LEU A 208 ? 0.1490 0.1754 0.1195 -0.0407 -0.0363 0.0191 208 LEU A CB +1713 C CG . LEU A 208 ? 0.1641 0.1919 0.1430 -0.0354 -0.0357 0.0196 208 LEU A CG +1714 C CD1 . LEU A 208 ? 0.1654 0.1935 0.1482 -0.0330 -0.0348 0.0182 208 LEU A CD1 +1715 C CD2 . LEU A 208 ? 0.1647 0.1975 0.1502 -0.0360 -0.0369 0.0260 208 LEU A CD2 +1716 N N . TYR A 209 ? 0.1759 0.1907 0.1216 -0.0505 -0.0369 0.0155 209 TYR A N +1717 C CA . TYR A 209 ? 0.1880 0.1968 0.1206 -0.0564 -0.0375 0.0150 209 TYR A CA +1718 C C . TYR A 209 ? 0.2056 0.2126 0.1332 -0.0617 -0.0417 0.0179 209 TYR A C +1719 O O . TYR A 209 ? 0.2150 0.2212 0.1362 -0.0682 -0.0452 0.0215 209 TYR A O +1720 C CB . TYR A 209 ? 0.1901 0.1901 0.1135 -0.0545 -0.0327 0.0093 209 TYR A CB +1721 C CG . TYR A 209 ? 0.1898 0.1909 0.1153 -0.0518 -0.0291 0.0083 209 TYR A CG +1722 C CD1 . TYR A 209 ? 0.2026 0.2029 0.1217 -0.0557 -0.0292 0.0102 209 TYR A CD1 +1723 C CD2 . TYR A 209 ? 0.1937 0.1964 0.1272 -0.0457 -0.0258 0.0060 209 TYR A CD2 +1724 C CE1 . TYR A 209 ? 0.2103 0.2121 0.1321 -0.0531 -0.0257 0.0100 209 TYR A CE1 +1725 C CE2 . TYR A 209 ? 0.2039 0.2083 0.1406 -0.0434 -0.0229 0.0063 209 TYR A CE2 +1726 C CZ . TYR A 209 ? 0.2111 0.2151 0.1421 -0.0469 -0.0226 0.0082 209 TYR A CZ +1727 O OH . TYR A 209 ? 0.2235 0.2299 0.1587 -0.0445 -0.0196 0.0092 209 TYR A OH +1728 N N . ALA A 210 ? 0.2094 0.2161 0.1404 -0.0591 -0.0418 0.0170 210 ALA A N +1729 C CA . ALA A 210 ? 0.2163 0.2224 0.1447 -0.0640 -0.0463 0.0208 210 ALA A CA +1730 C C . ALA A 210 ? 0.2209 0.2359 0.1579 -0.0673 -0.0507 0.0291 210 ALA A C +1731 O O . ALA A 210 ? 0.2286 0.2430 0.1608 -0.0745 -0.0557 0.0340 210 ALA A O +1732 C CB . ALA A 210 ? 0.2153 0.2215 0.1488 -0.0595 -0.0452 0.0192 210 ALA A CB +1733 N N . ALA A 211 ? 0.2098 0.2324 0.1593 -0.0624 -0.0491 0.0314 211 ALA A N +1734 C CA . ALA A 211 ? 0.2048 0.2362 0.1643 -0.0643 -0.0520 0.0398 211 ALA A CA +1735 C C . ALA A 211 ? 0.2108 0.2428 0.1647 -0.0714 -0.0553 0.0430 211 ALA A C +1736 O O . ALA A 211 ? 0.2234 0.2590 0.1784 -0.0777 -0.0603 0.0504 211 ALA A O +1737 C CB . ALA A 211 ? 0.2027 0.2395 0.1745 -0.0571 -0.0485 0.0402 211 ALA A CB +1738 N N . VAL A 212 ? 0.2063 0.2345 0.1535 -0.0709 -0.0527 0.0380 212 VAL A N +1739 C CA . VAL A 212 ? 0.2194 0.2472 0.1595 -0.0775 -0.0554 0.0407 212 VAL A CA +1740 C C . VAL A 212 ? 0.2499 0.2699 0.1751 -0.0858 -0.0596 0.0415 212 VAL A C +1741 O O . VAL A 212 ? 0.2625 0.2852 0.1860 -0.0933 -0.0650 0.0483 212 VAL A O +1742 C CB . VAL A 212 ? 0.2233 0.2480 0.1591 -0.0745 -0.0509 0.0353 212 VAL A CB +1743 C CG1 . VAL A 212 ? 0.2307 0.2533 0.1563 -0.0815 -0.0532 0.0376 212 VAL A CG1 +1744 C CG2 . VAL A 212 ? 0.2217 0.2542 0.1723 -0.0679 -0.0483 0.0360 212 VAL A CG2 +1745 N N . ILE A 213 ? 0.2661 0.2762 0.1805 -0.0851 -0.0576 0.0352 213 ILE A N +1746 C CA . ILE A 213 ? 0.2989 0.2988 0.1967 -0.0932 -0.0615 0.0351 213 ILE A CA +1747 C C . ILE A 213 ? 0.3284 0.3341 0.2324 -0.0989 -0.0688 0.0438 213 ILE A C +1748 O O . ILE A 213 ? 0.3478 0.3505 0.2427 -0.1081 -0.0749 0.0486 213 ILE A O +1749 C CB . ILE A 213 ? 0.3102 0.2991 0.1982 -0.0898 -0.0572 0.0270 213 ILE A CB +1750 C CG1 . ILE A 213 ? 0.3208 0.3032 0.2015 -0.0853 -0.0501 0.0200 213 ILE A CG1 +1751 C CG2 . ILE A 213 ? 0.3287 0.3063 0.2006 -0.0978 -0.0616 0.0272 213 ILE A CG2 +1752 C CD1 . ILE A 213 ? 0.3387 0.3140 0.2162 -0.0797 -0.0445 0.0132 213 ILE A CD1 +1753 N N . ASN A 214 ? 0.3286 0.3431 0.2488 -0.0934 -0.0681 0.0468 214 ASN A N +1754 C CA . ASN A 214 ? 0.3465 0.3677 0.2756 -0.0973 -0.0738 0.0560 214 ASN A CA +1755 C C . ASN A 214 ? 0.3578 0.3920 0.3022 -0.0985 -0.0764 0.0662 214 ASN A C +1756 O O . ASN A 214 ? 0.3792 0.4213 0.3358 -0.0992 -0.0794 0.0750 214 ASN A O +1757 C CB . ASN A 214 ? 0.3592 0.3819 0.2964 -0.0909 -0.0712 0.0545 214 ASN A CB +1758 C CG . ASN A 214 ? 0.4054 0.4159 0.3279 -0.0923 -0.0708 0.0474 214 ASN A CG +1759 O OD1 . ASN A 214 ? 0.4375 0.4434 0.3529 -0.0994 -0.0763 0.0505 214 ASN A OD1 +1760 N ND2 . ASN A 214 ? 0.4032 0.4076 0.3206 -0.0863 -0.0645 0.0381 214 ASN A ND2 +1761 N N . GLY A 215 ? 0.3423 0.3787 0.2864 -0.0988 -0.0753 0.0660 215 GLY A N +1762 C CA . GLY A 215 ? 0.3281 0.3761 0.2856 -0.1007 -0.0778 0.0759 215 GLY A CA +1763 C C . GLY A 215 ? 0.3001 0.3575 0.2753 -0.0920 -0.0726 0.0778 215 GLY A C +1764 O O . GLY A 215 ? 0.3024 0.3681 0.2871 -0.0937 -0.0741 0.0852 215 GLY A O +1765 N N A ASP A 216 ? 0.2803 0.3359 0.2594 -0.0829 -0.0667 0.0714 216 ASP A N +1766 N N B ASP A 216 ? 0.2847 0.3402 0.2637 -0.0830 -0.0668 0.0714 216 ASP A N +1767 C CA A ASP A 216 ? 0.2635 0.3253 0.2567 -0.0747 -0.0618 0.0725 216 ASP A CA +1768 C CA B ASP A 216 ? 0.2724 0.3339 0.2653 -0.0747 -0.0617 0.0722 216 ASP A CA +1769 C C A ASP A 216 ? 0.2716 0.3305 0.2605 -0.0722 -0.0585 0.0655 216 ASP A C +1770 C C B ASP A 216 ? 0.2758 0.3346 0.2642 -0.0724 -0.0587 0.0654 216 ASP A C +1771 O O A ASP A 216 ? 0.2864 0.3380 0.2669 -0.0689 -0.0555 0.0565 216 ASP A O +1772 O O B ASP A 216 ? 0.2909 0.3421 0.2703 -0.0696 -0.0558 0.0564 216 ASP A O +1773 C CB A ASP A 216 ? 0.2639 0.3240 0.2621 -0.0669 -0.0575 0.0695 216 ASP A CB +1774 C CB B ASP A 216 ? 0.2863 0.3457 0.2833 -0.0669 -0.0574 0.0686 216 ASP A CB +1775 C CG A ASP A 216 ? 0.2835 0.3475 0.2882 -0.0685 -0.0600 0.0774 216 ASP A CG +1776 C CG B ASP A 216 ? 0.3267 0.3938 0.3393 -0.0629 -0.0559 0.0775 216 ASP A CG +1777 O OD1 A ASP A 216 ? 0.2790 0.3500 0.2902 -0.0743 -0.0644 0.0877 216 ASP A OD1 +1778 O OD1 B ASP A 216 ? 0.3309 0.4047 0.3535 -0.0626 -0.0554 0.0842 216 ASP A OD1 +1779 O OD2 A ASP A 216 ? 0.2960 0.3567 0.3001 -0.0642 -0.0577 0.0741 216 ASP A OD2 +1780 O OD2 B ASP A 216 ? 0.3469 0.4129 0.3618 -0.0597 -0.0546 0.0781 216 ASP A OD2 +1781 N N . ARG A 217 ? 0.2585 0.3236 0.2534 -0.0740 -0.0594 0.0705 217 ARG A N +1782 C CA . ARG A 217 ? 0.2453 0.3087 0.2367 -0.0726 -0.0572 0.0655 217 ARG A CA +1783 C C . ARG A 217 ? 0.2271 0.2973 0.2323 -0.0678 -0.0545 0.0689 217 ARG A C +1784 O O . ARG A 217 ? 0.2224 0.2927 0.2263 -0.0675 -0.0535 0.0665 217 ARG A O +1785 C CB . ARG A 217 ? 0.2559 0.3186 0.2373 -0.0814 -0.0615 0.0677 217 ARG A CB +1786 C CG . ARG A 217 ? 0.2916 0.3465 0.2575 -0.0885 -0.0654 0.0663 217 ARG A CG +1787 C CD . ARG A 217 ? 0.3143 0.3693 0.2718 -0.0984 -0.0710 0.0717 217 ARG A CD +1788 N NE . ARG A 217 ? 0.3240 0.3770 0.2753 -0.0983 -0.0686 0.0679 217 ARG A NE +1789 C CZ . ARG A 217 ? 0.3284 0.3705 0.2620 -0.1002 -0.0669 0.0609 217 ARG A CZ +1790 N NH1 . ARG A 217 ? 0.3197 0.3610 0.2493 -0.0996 -0.0642 0.0587 217 ARG A NH1 +1791 N NH2 . ARG A 217 ? 0.3159 0.3476 0.2355 -0.1029 -0.0676 0.0567 217 ARG A NH2 +1792 N N . TRP A 218 ? 0.2159 0.2912 0.2339 -0.0640 -0.0532 0.0750 218 TRP A N +1793 C CA . TRP A 218 ? 0.2071 0.2875 0.2374 -0.0597 -0.0503 0.0788 218 TRP A CA +1794 C C . TRP A 218 ? 0.2084 0.2834 0.2369 -0.0535 -0.0463 0.0704 218 TRP A C +1795 O O . TRP A 218 ? 0.2116 0.2896 0.2469 -0.0518 -0.0450 0.0724 218 TRP A O +1796 C CB . TRP A 218 ? 0.1990 0.2837 0.2422 -0.0556 -0.0480 0.0866 218 TRP A CB +1797 C CG . TRP A 218 ? 0.1998 0.2781 0.2409 -0.0491 -0.0442 0.0816 218 TRP A CG +1798 C CD1 . TRP A 218 ? 0.2098 0.2871 0.2488 -0.0499 -0.0453 0.0828 218 TRP A CD1 +1799 C CD2 . TRP A 218 ? 0.2055 0.2774 0.2468 -0.0410 -0.0390 0.0754 218 TRP A CD2 +1800 N NE1 . TRP A 218 ? 0.2152 0.2860 0.2523 -0.0426 -0.0408 0.0770 218 TRP A NE1 +1801 C CE2 . TRP A 218 ? 0.2142 0.2813 0.2523 -0.0373 -0.0370 0.0726 218 TRP A CE2 +1802 C CE3 . TRP A 218 ? 0.2123 0.2814 0.2553 -0.0370 -0.0363 0.0720 218 TRP A CE3 +1803 C CZ2 . TRP A 218 ? 0.2196 0.2788 0.2549 -0.0302 -0.0327 0.0663 218 TRP A CZ2 +1804 C CZ3 . TRP A 218 ? 0.2220 0.2828 0.2621 -0.0302 -0.0323 0.0658 218 TRP A CZ3 +1805 C CH2 . TRP A 218 ? 0.2233 0.2790 0.2592 -0.0270 -0.0306 0.0631 218 TRP A CH2 +1806 N N . PHE A 219 ? 0.2026 0.2700 0.2228 -0.0503 -0.0446 0.0619 219 PHE A N +1807 C CA . PHE A 219 ? 0.1985 0.2603 0.2170 -0.0448 -0.0415 0.0545 219 PHE A CA +1808 C C . PHE A 219 ? 0.2102 0.2707 0.2225 -0.0472 -0.0423 0.0502 219 PHE A C +1809 O O . PHE A 219 ? 0.2134 0.2706 0.2260 -0.0434 -0.0405 0.0455 219 PHE A O +1810 C CB . PHE A 219 ? 0.1881 0.2429 0.2014 -0.0407 -0.0396 0.0485 219 PHE A CB +1811 C CG . PHE A 219 ? 0.1796 0.2318 0.1831 -0.0447 -0.0415 0.0455 219 PHE A CG +1812 C CD1 . PHE A 219 ? 0.1862 0.2342 0.1810 -0.0461 -0.0414 0.0395 219 PHE A CD1 +1813 C CD2 . PHE A 219 ? 0.1759 0.2296 0.1791 -0.0472 -0.0432 0.0495 219 PHE A CD2 +1814 C CE1 . PHE A 219 ? 0.1908 0.2348 0.1755 -0.0497 -0.0425 0.0369 219 PHE A CE1 +1815 C CE2 . PHE A 219 ? 0.1857 0.2356 0.1790 -0.0512 -0.0452 0.0467 219 PHE A CE2 +1816 C CZ . PHE A 219 ? 0.1871 0.2316 0.1705 -0.0526 -0.0447 0.0402 219 PHE A CZ +1817 N N . LEU A 220 ? 0.2060 0.2687 0.2125 -0.0536 -0.0450 0.0522 220 LEU A N +1818 C CA . LEU A 220 ? 0.2204 0.2817 0.2208 -0.0556 -0.0448 0.0490 220 LEU A CA +1819 C C . LEU A 220 ? 0.2291 0.2963 0.2392 -0.0547 -0.0447 0.0528 220 LEU A C +1820 O O . LEU A 220 ? 0.2333 0.3066 0.2522 -0.0558 -0.0460 0.0597 220 LEU A O +1821 C CB . LEU A 220 ? 0.2247 0.2850 0.2142 -0.0629 -0.0475 0.0503 220 LEU A CB +1822 C CG . LEU A 220 ? 0.2373 0.2904 0.2156 -0.0645 -0.0477 0.0463 220 LEU A CG +1823 C CD1 . LEU A 220 ? 0.2414 0.2915 0.2069 -0.0725 -0.0507 0.0479 220 LEU A CD1 +1824 C CD2 . LEU A 220 ? 0.2467 0.2928 0.2205 -0.0591 -0.0436 0.0381 220 LEU A CD2 +1825 N N . ASN A 221 ? 0.2295 0.2950 0.2392 -0.0523 -0.0430 0.0490 221 ASN A N +1826 C CA . ASN A 221 ? 0.2248 0.2950 0.2438 -0.0510 -0.0429 0.0521 221 ASN A CA +1827 C C . ASN A 221 ? 0.2211 0.2925 0.2365 -0.0531 -0.0427 0.0511 221 ASN A C +1828 O O . ASN A 221 ? 0.2310 0.2986 0.2357 -0.0554 -0.0421 0.0482 221 ASN A O +1829 C CB . ASN A 221 ? 0.2341 0.3011 0.2598 -0.0448 -0.0412 0.0496 221 ASN A CB +1830 C CG . ASN A 221 ? 0.2661 0.3267 0.2866 -0.0417 -0.0398 0.0428 221 ASN A CG +1831 O OD1 . ASN A 221 ? 0.2607 0.3206 0.2763 -0.0430 -0.0393 0.0405 221 ASN A OD1 +1832 N ND2 . ASN A 221 ? 0.2758 0.3312 0.2975 -0.0375 -0.0390 0.0400 221 ASN A ND2 +1833 N N . ARG A 222 ? 0.2057 0.2819 0.2299 -0.0522 -0.0429 0.0542 222 ARG A N +1834 C CA . ARG A 222 ? 0.2060 0.2843 0.2288 -0.0537 -0.0424 0.0545 222 ARG A CA +1835 C C . ARG A 222 ? 0.2006 0.2750 0.2238 -0.0493 -0.0403 0.0498 222 ARG A C +1836 O O . ARG A 222 ? 0.2032 0.2802 0.2280 -0.0496 -0.0395 0.0510 222 ARG A O +1837 C CB . ARG A 222 ? 0.2137 0.2997 0.2475 -0.0546 -0.0439 0.0607 222 ARG A CB +1838 C CG . ARG A 222 ? 0.2546 0.3462 0.2899 -0.0595 -0.0463 0.0672 222 ARG A CG +1839 C CD . ARG A 222 ? 0.2858 0.3854 0.3336 -0.0601 -0.0474 0.0740 222 ARG A CD +1840 N NE . ARG A 222 ? 0.3103 0.4163 0.3597 -0.0658 -0.0502 0.0815 222 ARG A NE +1841 C CZ . ARG A 222 ? 0.3500 0.4591 0.3926 -0.0722 -0.0526 0.0845 222 ARG A CZ +1842 N NH1 . ARG A 222 ? 0.3476 0.4538 0.3813 -0.0730 -0.0515 0.0807 222 ARG A NH1 +1843 N NH2 . ARG A 222 ? 0.3501 0.4649 0.3946 -0.0780 -0.0560 0.0921 222 ARG A NH2 +1844 N N . PHE A 223 ? 0.1880 0.2567 0.2104 -0.0456 -0.0395 0.0453 223 PHE A N +1845 C CA . PHE A 223 ? 0.1905 0.2561 0.2156 -0.0418 -0.0384 0.0423 223 PHE A CA +1846 C C . PHE A 223 ? 0.1685 0.2292 0.1855 -0.0409 -0.0360 0.0381 223 PHE A C +1847 O O . PHE A 223 ? 0.1751 0.2326 0.1831 -0.0425 -0.0350 0.0360 223 PHE A O +1848 C CB . PHE A 223 ? 0.2060 0.2680 0.2368 -0.0381 -0.0397 0.0409 223 PHE A CB +1849 C CG . PHE A 223 ? 0.2286 0.2930 0.2664 -0.0380 -0.0409 0.0447 223 PHE A CG +1850 C CD1 . PHE A 223 ? 0.2419 0.3129 0.2861 -0.0400 -0.0417 0.0496 223 PHE A CD1 +1851 C CD2 . PHE A 223 ? 0.2490 0.3088 0.2870 -0.0355 -0.0406 0.0437 223 PHE A CD2 +1852 C CE1 . PHE A 223 ? 0.2545 0.3277 0.3060 -0.0396 -0.0421 0.0538 223 PHE A CE1 +1853 C CE2 . PHE A 223 ? 0.2631 0.3243 0.3077 -0.0346 -0.0405 0.0478 223 PHE A CE2 +1854 C CZ . PHE A 223 ? 0.2589 0.3269 0.3106 -0.0367 -0.0412 0.0529 223 PHE A CZ +1855 N N . THR A 224 ? 0.1530 0.2131 0.1741 -0.0383 -0.0350 0.0374 224 THR A N +1856 C CA . THR A 224 ? 0.1516 0.2071 0.1683 -0.0362 -0.0324 0.0342 224 THR A CA +1857 C C . THR A 224 ? 0.1523 0.2060 0.1769 -0.0330 -0.0344 0.0335 224 THR A C +1858 O O . THR A 224 ? 0.1582 0.2130 0.1898 -0.0326 -0.0376 0.0351 224 THR A O +1859 C CB . THR A 224 ? 0.1613 0.2174 0.1731 -0.0369 -0.0284 0.0352 224 THR A CB +1860 O OG1 . THR A 224 ? 0.1594 0.2096 0.1648 -0.0351 -0.0251 0.0318 224 THR A OG1 +1861 C CG2 . THR A 224 ? 0.1625 0.2231 0.1837 -0.0353 -0.0280 0.0390 224 THR A CG2 +1862 N N . THR A 225 ? 0.1427 0.1930 0.1656 -0.0310 -0.0327 0.0314 225 THR A N +1863 C CA . THR A 225 ? 0.1450 0.1933 0.1745 -0.0289 -0.0350 0.0314 225 THR A CA +1864 C C . THR A 225 ? 0.1455 0.1935 0.1756 -0.0272 -0.0316 0.0321 225 THR A C +1865 O O . THR A 225 ? 0.1403 0.1888 0.1651 -0.0273 -0.0269 0.0323 225 THR A O +1866 C CB . THR A 225 ? 0.1737 0.2164 0.2000 -0.0281 -0.0375 0.0279 225 THR A CB +1867 O OG1 . THR A 225 ? 0.1926 0.2324 0.2239 -0.0269 -0.0407 0.0283 225 THR A OG1 +1868 C CG2 . THR A 225 ? 0.1881 0.2273 0.2060 -0.0277 -0.0349 0.0242 225 THR A CG2 +1869 N N . THR A 226 ? 0.1469 0.1936 0.1834 -0.0257 -0.0339 0.0332 226 THR A N +1870 C CA . THR A 226 ? 0.1483 0.1950 0.1876 -0.0238 -0.0308 0.0348 226 THR A CA +1871 C C . THR A 226 ? 0.1535 0.1950 0.1898 -0.0231 -0.0325 0.0314 226 THR A C +1872 O O . THR A 226 ? 0.1489 0.1869 0.1823 -0.0239 -0.0365 0.0286 226 THR A O +1873 C CB . THR A 226 ? 0.1692 0.2204 0.2212 -0.0234 -0.0332 0.0409 226 THR A CB +1874 O OG1 . THR A 226 ? 0.1760 0.2243 0.2318 -0.0246 -0.0401 0.0409 226 THR A OG1 +1875 C CG2 . THR A 226 ? 0.1819 0.2387 0.2379 -0.0240 -0.0320 0.0448 226 THR A CG2 +1876 N N A LEU A 227 ? 0.1551 0.1958 0.1924 -0.0213 -0.0291 0.0321 227 LEU A N +1877 N N B LEU A 227 ? 0.1515 0.1922 0.1888 -0.0213 -0.0291 0.0321 227 LEU A N +1878 C CA A LEU A 227 ? 0.1694 0.2059 0.2049 -0.0206 -0.0308 0.0296 227 LEU A CA +1879 C CA B LEU A 227 ? 0.1621 0.1985 0.1977 -0.0207 -0.0310 0.0295 227 LEU A CA +1880 C C A LEU A 227 ? 0.1749 0.2099 0.2162 -0.0218 -0.0380 0.0311 227 LEU A C +1881 C C B LEU A 227 ? 0.1711 0.2060 0.2123 -0.0219 -0.0382 0.0311 227 LEU A C +1882 O O A LEU A 227 ? 0.1842 0.2140 0.2200 -0.0224 -0.0412 0.0274 227 LEU A O +1883 O O B LEU A 227 ? 0.1795 0.2093 0.2152 -0.0225 -0.0414 0.0273 227 LEU A O +1884 C CB A LEU A 227 ? 0.1732 0.2100 0.2112 -0.0183 -0.0254 0.0317 227 LEU A CB +1885 C CB B LEU A 227 ? 0.1603 0.1969 0.1982 -0.0184 -0.0260 0.0314 227 LEU A CB +1886 C CG A LEU A 227 ? 0.1952 0.2274 0.2273 -0.0174 -0.0240 0.0278 227 LEU A CG +1887 C CG B LEU A 227 ? 0.1740 0.2074 0.2019 -0.0174 -0.0192 0.0279 227 LEU A CG +1888 C CD1 A LEU A 227 ? 0.2069 0.2351 0.2268 -0.0185 -0.0232 0.0217 227 LEU A CD1 +1889 C CD1 B LEU A 227 ? 0.1720 0.2045 0.2030 -0.0146 -0.0141 0.0300 227 LEU A CD1 +1890 C CD2 A LEU A 227 ? 0.1975 0.2297 0.2314 -0.0147 -0.0170 0.0301 227 LEU A CD2 +1891 C CD2 B LEU A 227 ? 0.1864 0.2153 0.2040 -0.0187 -0.0211 0.0218 227 LEU A CD2 +1892 N N . ASN A 228 ? 0.1664 0.2052 0.2179 -0.0225 -0.0408 0.0368 228 ASN A N +1893 C CA . ASN A 228 ? 0.1596 0.1953 0.2151 -0.0245 -0.0486 0.0386 228 ASN A CA +1894 C C . ASN A 228 ? 0.1620 0.1930 0.2114 -0.0260 -0.0525 0.0350 228 ASN A C +1895 O O . ASN A 228 ? 0.1794 0.2032 0.2243 -0.0271 -0.0572 0.0328 228 ASN A O +1896 C CB . ASN A 228 ? 0.1641 0.2053 0.2327 -0.0253 -0.0510 0.0464 228 ASN A CB +1897 C CG . ASN A 228 ? 0.2077 0.2526 0.2841 -0.0237 -0.0480 0.0514 228 ASN A CG +1898 O OD1 . ASN A 228 ? 0.2288 0.2799 0.3169 -0.0233 -0.0473 0.0588 228 ASN A OD1 +1899 N ND2 . ASN A 228 ? 0.2169 0.2585 0.2882 -0.0226 -0.0459 0.0482 228 ASN A ND2 +1900 N N . ASP A 229 ? 0.1556 0.1898 0.2042 -0.0260 -0.0501 0.0347 229 ASP A N +1901 C CA . ASP A 229 ? 0.1631 0.1932 0.2073 -0.0269 -0.0529 0.0323 229 ASP A CA +1902 C C . ASP A 229 ? 0.1704 0.1950 0.2044 -0.0259 -0.0513 0.0267 229 ASP A C +1903 O O . ASP A 229 ? 0.1840 0.2011 0.2132 -0.0261 -0.0544 0.0245 229 ASP A O +1904 C CB . ASP A 229 ? 0.1876 0.2237 0.2347 -0.0273 -0.0507 0.0342 229 ASP A CB +1905 C CG . ASP A 229 ? 0.2696 0.3018 0.3131 -0.0278 -0.0525 0.0323 229 ASP A CG +1906 O OD1 . ASP A 229 ? 0.2930 0.3199 0.3380 -0.0287 -0.0572 0.0331 229 ASP A OD1 +1907 O OD2 . ASP A 229 ? 0.2923 0.3257 0.3308 -0.0273 -0.0492 0.0302 229 ASP A OD2 +1908 N N . PHE A 230 ? 0.1635 0.1907 0.1935 -0.0249 -0.0463 0.0247 230 PHE A N +1909 C CA . PHE A 230 ? 0.1676 0.1905 0.1891 -0.0240 -0.0449 0.0203 230 PHE A CA +1910 C C . PHE A 230 ? 0.1813 0.1975 0.2000 -0.0235 -0.0479 0.0184 230 PHE A C +1911 O O . PHE A 230 ? 0.1952 0.2052 0.2080 -0.0229 -0.0491 0.0157 230 PHE A O +1912 C CB . PHE A 230 ? 0.1586 0.1845 0.1762 -0.0236 -0.0398 0.0189 230 PHE A CB +1913 C CG . PHE A 230 ? 0.1754 0.1973 0.1855 -0.0229 -0.0389 0.0150 230 PHE A CG +1914 C CD1 . PHE A 230 ? 0.1837 0.2056 0.1905 -0.0233 -0.0387 0.0144 230 PHE A CD1 +1915 C CD2 . PHE A 230 ? 0.1914 0.2097 0.1991 -0.0218 -0.0389 0.0129 230 PHE A CD2 +1916 C CE1 . PHE A 230 ? 0.2018 0.2204 0.2030 -0.0225 -0.0380 0.0119 230 PHE A CE1 +1917 C CE2 . PHE A 230 ? 0.2005 0.2151 0.2019 -0.0210 -0.0385 0.0099 230 PHE A CE2 +1918 C CZ . PHE A 230 ? 0.2073 0.2221 0.2056 -0.0212 -0.0379 0.0095 230 PHE A CZ +1919 N N . ASN A 231 ? 0.1764 0.1935 0.1998 -0.0237 -0.0491 0.0205 231 ASN A N +1920 C CA . ASN A 231 ? 0.1851 0.1963 0.2061 -0.0239 -0.0525 0.0195 231 ASN A CA +1921 C C . ASN A 231 ? 0.2076 0.2110 0.2259 -0.0255 -0.0585 0.0195 231 ASN A C +1922 O O . ASN A 231 ? 0.2219 0.2178 0.2334 -0.0255 -0.0607 0.0170 231 ASN A O +1923 C CB . ASN A 231 ? 0.1929 0.2078 0.2210 -0.0240 -0.0523 0.0231 231 ASN A CB +1924 C CG . ASN A 231 ? 0.2152 0.2331 0.2414 -0.0220 -0.0461 0.0213 231 ASN A CG +1925 O OD1 . ASN A 231 ? 0.2253 0.2409 0.2436 -0.0211 -0.0436 0.0169 231 ASN A OD1 +1926 N ND2 . ASN A 231 ? 0.2279 0.2506 0.2612 -0.0211 -0.0431 0.0250 231 ASN A ND2 +1927 N N . LEU A 232 ? 0.2152 0.2191 0.2374 -0.0267 -0.0609 0.0220 232 LEU A N +1928 C CA . LEU A 232 ? 0.2396 0.2337 0.2569 -0.0283 -0.0662 0.0214 232 LEU A CA +1929 C C . LEU A 232 ? 0.2511 0.2382 0.2580 -0.0261 -0.0634 0.0166 232 LEU A C +1930 O O . LEU A 232 ? 0.2721 0.2482 0.2700 -0.0262 -0.0658 0.0142 232 LEU A O +1931 C CB . LEU A 232 ? 0.2564 0.2531 0.2805 -0.0298 -0.0684 0.0250 232 LEU A CB +1932 C CG . LEU A 232 ? 0.2869 0.2897 0.3222 -0.0320 -0.0719 0.0310 232 LEU A CG +1933 C CD1 . LEU A 232 ? 0.2982 0.3035 0.3398 -0.0333 -0.0739 0.0345 232 LEU A CD1 +1934 C CD2 . LEU A 232 ? 0.3027 0.2980 0.3364 -0.0349 -0.0789 0.0327 232 LEU A CD2 +1935 N N . VAL A 233 ? 0.2402 0.2334 0.2479 -0.0243 -0.0580 0.0157 233 VAL A N +1936 C CA . VAL A 233 ? 0.2420 0.2309 0.2424 -0.0220 -0.0547 0.0128 233 VAL A CA +1937 C C . VAL A 233 ? 0.2444 0.2304 0.2386 -0.0206 -0.0531 0.0097 233 VAL A C +1938 O O . VAL A 233 ? 0.2544 0.2316 0.2405 -0.0190 -0.0528 0.0074 233 VAL A O +1939 C CB . VAL A 233 ? 0.2538 0.2514 0.2584 -0.0214 -0.0505 0.0142 233 VAL A CB +1940 C CG1 . VAL A 233 ? 0.2676 0.2618 0.2668 -0.0191 -0.0471 0.0128 233 VAL A CG1 +1941 C CG2 . VAL A 233 ? 0.2610 0.2616 0.2722 -0.0228 -0.0521 0.0175 233 VAL A CG2 +1942 N N . ALA A 234 ? 0.2379 0.2302 0.2354 -0.0209 -0.0520 0.0099 234 ALA A N +1943 C CA . ALA A 234 ? 0.2521 0.2423 0.2446 -0.0197 -0.0506 0.0073 234 ALA A CA +1944 C C . ALA A 234 ? 0.2700 0.2501 0.2564 -0.0201 -0.0549 0.0061 234 ALA A C +1945 O O . ALA A 234 ? 0.2737 0.2472 0.2521 -0.0185 -0.0538 0.0034 234 ALA A O +1946 C CB . ALA A 234 ? 0.2534 0.2510 0.2511 -0.0201 -0.0488 0.0082 234 ALA A CB +1947 N N . MET A 235 ? 0.2708 0.2489 0.2605 -0.0227 -0.0599 0.0085 235 MET A N +1948 C CA . MET A 235 ? 0.2833 0.2506 0.2661 -0.0244 -0.0653 0.0080 235 MET A CA +1949 C C . MET A 235 ? 0.2748 0.2297 0.2458 -0.0231 -0.0651 0.0050 235 MET A C +1950 O O . MET A 235 ? 0.2808 0.2267 0.2418 -0.0223 -0.0654 0.0024 235 MET A O +1951 C CB . MET A 235 ? 0.3132 0.2810 0.3027 -0.0282 -0.0716 0.0124 235 MET A CB +1952 C CG . MET A 235 ? 0.3926 0.3474 0.3734 -0.0313 -0.0786 0.0124 235 MET A CG +1953 S SD . MET A 235 ? 0.5622 0.5196 0.5473 -0.0340 -0.0831 0.0157 235 MET A SD +1954 C CE . MET A 235 ? 0.5082 0.4783 0.5112 -0.0362 -0.0851 0.0231 235 MET A CE +1955 N N . LYS A 236 ? 0.2583 0.2127 0.2306 -0.0226 -0.0639 0.0057 236 LYS A N +1956 C CA . LYS A 236 ? 0.2595 0.2016 0.2215 -0.0208 -0.0625 0.0036 236 LYS A CA +1957 C C . LYS A 236 ? 0.2555 0.1957 0.2112 -0.0167 -0.0566 0.0010 236 LYS A C +1958 O O . LYS A 236 ? 0.2773 0.2045 0.2214 -0.0149 -0.0556 -0.0012 236 LYS A O +1959 C CB . LYS A 236 ? 0.2939 0.2384 0.2613 -0.0207 -0.0616 0.0056 236 LYS A CB +1960 C CG . LYS A 236 ? 0.3727 0.3048 0.3307 -0.0180 -0.0586 0.0042 236 LYS A CG +1961 C CD . LYS A 236 ? 0.4508 0.3874 0.4161 -0.0177 -0.0569 0.0068 236 LYS A CD +1962 C CE . LYS A 236 ? 0.5137 0.4397 0.4715 -0.0139 -0.0519 0.0061 236 LYS A CE +1963 N NZ . LYS A 236 ? 0.5567 0.4634 0.5015 -0.0148 -0.0550 0.0042 236 LYS A NZ +1964 N N . TYR A 237 ? 0.2267 0.1790 0.1895 -0.0153 -0.0527 0.0015 237 TYR A N +1965 C CA . TYR A 237 ? 0.2168 0.1692 0.1758 -0.0118 -0.0474 0.0002 237 TYR A CA +1966 C C . TYR A 237 ? 0.2196 0.1729 0.1759 -0.0114 -0.0473 -0.0016 237 TYR A C +1967 O O . TYR A 237 ? 0.2282 0.1848 0.1841 -0.0089 -0.0431 -0.0019 237 TYR A O +1968 C CB . TYR A 237 ? 0.2073 0.1712 0.1748 -0.0110 -0.0433 0.0026 237 TYR A CB +1969 C CG . TYR A 237 ? 0.2211 0.1826 0.1900 -0.0101 -0.0420 0.0047 237 TYR A CG +1970 C CD1 . TYR A 237 ? 0.2387 0.1928 0.2023 -0.0065 -0.0377 0.0051 237 TYR A CD1 +1971 C CD2 . TYR A 237 ? 0.2272 0.1928 0.2027 -0.0126 -0.0446 0.0066 237 TYR A CD2 +1972 C CE1 . TYR A 237 ? 0.2503 0.2010 0.2152 -0.0053 -0.0360 0.0073 237 TYR A CE1 +1973 C CE2 . TYR A 237 ? 0.2339 0.1968 0.2108 -0.0118 -0.0434 0.0086 237 TYR A CE2 +1974 C CZ . TYR A 237 ? 0.2574 0.2123 0.2289 -0.0082 -0.0391 0.0089 237 TYR A CZ +1975 O OH . TYR A 237 ? 0.2769 0.2289 0.2504 -0.0070 -0.0372 0.0114 237 TYR A OH +1976 N N A ASN A 238 ? 0.2175 0.1685 0.1729 -0.0140 -0.0520 -0.0021 238 ASN A N +1977 N N B ASN A 238 ? 0.2148 0.1657 0.1700 -0.0140 -0.0520 -0.0021 238 ASN A N +1978 C CA A ASN A 238 ? 0.2240 0.1759 0.1775 -0.0138 -0.0523 -0.0033 238 ASN A CA +1979 C CA B ASN A 238 ? 0.2182 0.1701 0.1718 -0.0139 -0.0524 -0.0033 238 ASN A CA +1980 C C A ASN A 238 ? 0.2143 0.1785 0.1758 -0.0131 -0.0487 -0.0028 238 ASN A C +1981 C C B ASN A 238 ? 0.2122 0.1765 0.1739 -0.0133 -0.0489 -0.0028 238 ASN A C +1982 O O A ASN A 238 ? 0.2159 0.1809 0.1749 -0.0112 -0.0459 -0.0041 238 ASN A O +1983 O O B ASN A 238 ? 0.2144 0.1796 0.1739 -0.0117 -0.0466 -0.0041 238 ASN A O +1984 C CB A ASN A 238 ? 0.2562 0.1969 0.1976 -0.0112 -0.0506 -0.0057 238 ASN A CB +1985 C CB B ASN A 238 ? 0.2416 0.1827 0.1832 -0.0114 -0.0508 -0.0057 238 ASN A CB +1986 C CG A ASN A 238 ? 0.3145 0.2403 0.2451 -0.0126 -0.0546 -0.0066 238 ASN A CG +1987 C CG B ASN A 238 ? 0.2820 0.2082 0.2124 -0.0131 -0.0554 -0.0067 238 ASN A CG +1988 O OD1 A ASN A 238 ? 0.3377 0.2533 0.2598 -0.0103 -0.0521 -0.0075 238 ASN A OD1 +1989 O OD1 B ASN A 238 ? 0.2879 0.2122 0.2202 -0.0168 -0.0609 -0.0053 238 ASN A OD1 +1990 N ND2 A ASN A 238 ? 0.3215 0.2452 0.2521 -0.0167 -0.0611 -0.0058 238 ASN A ND2 +1991 N ND2 B ASN A 238 ? 0.2978 0.2124 0.2157 -0.0105 -0.0534 -0.0089 238 ASN A ND2 +1992 N N . TYR A 239 ? 0.2042 0.1771 0.1744 -0.0147 -0.0485 -0.0008 239 TYR A N +1993 C CA . TYR A 239 ? 0.2014 0.1840 0.1775 -0.0147 -0.0454 -0.0004 239 TYR A CA +1994 C C . TYR A 239 ? 0.2074 0.1933 0.1890 -0.0165 -0.0474 0.0010 239 TYR A C +1995 O O . TYR A 239 ? 0.2147 0.1986 0.1987 -0.0183 -0.0514 0.0029 239 TYR A O +1996 C CB . TYR A 239 ? 0.1953 0.1844 0.1764 -0.0154 -0.0435 0.0014 239 TYR A CB +1997 C CG . TYR A 239 ? 0.1940 0.1846 0.1730 -0.0140 -0.0401 0.0013 239 TYR A CG +1998 C CD1 . TYR A 239 ? 0.2026 0.1870 0.1769 -0.0118 -0.0394 0.0012 239 TYR A CD1 +1999 C CD2 . TYR A 239 ? 0.1911 0.1889 0.1728 -0.0151 -0.0376 0.0022 239 TYR A CD2 +2000 C CE1 . TYR A 239 ? 0.2095 0.1964 0.1839 -0.0104 -0.0361 0.0026 239 TYR A CE1 +2001 C CE2 . TYR A 239 ? 0.1965 0.1964 0.1773 -0.0146 -0.0355 0.0034 239 TYR A CE2 +2002 C CZ . TYR A 239 ? 0.2094 0.2047 0.1877 -0.0121 -0.0347 0.0041 239 TYR A CZ +2003 O OH . TYR A 239 ? 0.2142 0.2126 0.1936 -0.0115 -0.0324 0.0067 239 TYR A OH +2004 N N A GLU A 240 ? 0.2031 0.1938 0.1870 -0.0160 -0.0446 0.0006 240 GLU A N +2005 N N B GLU A 240 ? 0.2060 0.1969 0.1900 -0.0160 -0.0446 0.0006 240 GLU A N +2006 C CA A GLU A 240 ? 0.2106 0.2050 0.2009 -0.0169 -0.0451 0.0028 240 GLU A CA +2007 C CA B GLU A 240 ? 0.2154 0.2099 0.2058 -0.0169 -0.0450 0.0028 240 GLU A CA +2008 C C A GLU A 240 ? 0.2090 0.2088 0.2064 -0.0180 -0.0444 0.0058 240 GLU A C +2009 C C B GLU A 240 ? 0.2113 0.2111 0.2087 -0.0180 -0.0444 0.0058 240 GLU A C +2010 O O A GLU A 240 ? 0.1989 0.2015 0.1956 -0.0179 -0.0417 0.0053 240 GLU A O +2011 O O B GLU A 240 ? 0.2011 0.2037 0.1979 -0.0179 -0.0417 0.0053 240 GLU A O +2012 C CB A GLU A 240 ? 0.2421 0.2394 0.2322 -0.0157 -0.0409 0.0014 240 GLU A CB +2013 C CB B GLU A 240 ? 0.2550 0.2526 0.2454 -0.0157 -0.0408 0.0015 240 GLU A CB +2014 C CG A GLU A 240 ? 0.2988 0.2918 0.2839 -0.0147 -0.0418 -0.0006 240 GLU A CG +2015 C CG B GLU A 240 ? 0.3326 0.3262 0.3190 -0.0149 -0.0418 -0.0001 240 GLU A CG +2016 C CD A GLU A 240 ? 0.3616 0.3521 0.3489 -0.0158 -0.0460 0.0013 240 GLU A CD +2017 C CD B GLU A 240 ? 0.4209 0.4175 0.4091 -0.0139 -0.0381 -0.0006 240 GLU A CD +2018 O OE1 A GLU A 240 ? 0.3622 0.3567 0.3563 -0.0160 -0.0451 0.0038 240 GLU A OE1 +2019 O OE1 B GLU A 240 ? 0.4450 0.4433 0.4308 -0.0135 -0.0343 -0.0022 240 GLU A OE1 +2020 O OE2 A GLU A 240 ? 0.3858 0.3697 0.3677 -0.0165 -0.0502 0.0008 240 GLU A OE2 +2021 O OE2 B GLU A 240 ? 0.4574 0.4543 0.4493 -0.0140 -0.0390 0.0010 240 GLU A OE2 +2022 N N . PRO A 241 ? 0.2153 0.2168 0.2193 -0.0191 -0.0466 0.0092 241 PRO A N +2023 C CA . PRO A 241 ? 0.2227 0.2298 0.2344 -0.0196 -0.0454 0.0129 241 PRO A CA +2024 C C . PRO A 241 ? 0.2198 0.2315 0.2320 -0.0182 -0.0387 0.0124 241 PRO A C +2025 O O . PRO A 241 ? 0.2329 0.2443 0.2441 -0.0171 -0.0359 0.0115 241 PRO A O +2026 C CB . PRO A 241 ? 0.2383 0.2473 0.2589 -0.0208 -0.0485 0.0182 241 PRO A CB +2027 C CG . PRO A 241 ? 0.2465 0.2487 0.2620 -0.0222 -0.0542 0.0169 241 PRO A CG +2028 C CD . PRO A 241 ? 0.2168 0.2155 0.2229 -0.0203 -0.0511 0.0114 241 PRO A CD +2029 N N . LEU A 242 ? 0.2081 0.2229 0.2211 -0.0185 -0.0365 0.0132 242 LEU A N +2030 C CA . LEU A 242 ? 0.2160 0.2329 0.2268 -0.0176 -0.0302 0.0127 242 LEU A CA +2031 C C . LEU A 242 ? 0.2124 0.2329 0.2316 -0.0165 -0.0271 0.0175 242 LEU A C +2032 O O . LEU A 242 ? 0.2108 0.2343 0.2374 -0.0171 -0.0297 0.0215 242 LEU A O +2033 C CB . LEU A 242 ? 0.2211 0.2391 0.2274 -0.0188 -0.0292 0.0115 242 LEU A CB +2034 C CG . LEU A 242 ? 0.2425 0.2597 0.2415 -0.0191 -0.0240 0.0096 242 LEU A CG +2035 C CD1 . LEU A 242 ? 0.2550 0.2685 0.2468 -0.0192 -0.0238 0.0058 242 LEU A CD1 +2036 C CD2 . LEU A 242 ? 0.2458 0.2652 0.2423 -0.0210 -0.0238 0.0103 242 LEU A CD2 +2037 N N . THR A 243 ? 0.2176 0.2371 0.2353 -0.0148 -0.0216 0.0171 243 THR A N +2038 C CA . THR A 243 ? 0.2205 0.2427 0.2461 -0.0129 -0.0169 0.0223 243 THR A CA +2039 C C . THR A 243 ? 0.2288 0.2496 0.2482 -0.0118 -0.0094 0.0215 243 THR A C +2040 O O . THR A 243 ? 0.2298 0.2470 0.2382 -0.0132 -0.0085 0.0168 243 THR A O +2041 C CB . THR A 243 ? 0.2302 0.2515 0.2595 -0.0111 -0.0150 0.0234 243 THR A CB +2042 O OG1 . THR A 243 ? 0.2306 0.2470 0.2500 -0.0103 -0.0103 0.0186 243 THR A OG1 +2043 C CG2 . THR A 243 ? 0.2434 0.2647 0.2764 -0.0127 -0.0225 0.0239 243 THR A CG2 +2044 N N . GLN A 244 ? 0.2287 0.2517 0.2550 -0.0095 -0.0042 0.0267 244 GLN A N +2045 C CA . GLN A 244 ? 0.2356 0.2551 0.2540 -0.0081 0.0041 0.0261 244 GLN A CA +2046 C C . GLN A 244 ? 0.2382 0.2500 0.2454 -0.0073 0.0089 0.0213 244 GLN A C +2047 O O . GLN A 244 ? 0.2468 0.2530 0.2417 -0.0083 0.0125 0.0179 244 GLN A O +2048 C CB . GLN A 244 ? 0.2529 0.2757 0.2816 -0.0048 0.0101 0.0335 244 GLN A CB +2049 C CG . GLN A 244 ? 0.3001 0.3180 0.3193 -0.0031 0.0191 0.0332 244 GLN A CG +2050 C CD . GLN A 244 ? 0.3381 0.3566 0.3501 -0.0062 0.0161 0.0309 244 GLN A CD +2051 O OE1 . GLN A 244 ? 0.3514 0.3767 0.3719 -0.0076 0.0105 0.0337 244 GLN A OE1 +2052 N NE2 . GLN A 244 ? 0.3302 0.3412 0.3261 -0.0076 0.0196 0.0259 244 GLN A NE2 +2053 N N . ASP A 245 ? 0.2271 0.2384 0.2386 -0.0060 0.0086 0.0214 245 ASP A N +2054 C CA . ASP A 245 ? 0.2274 0.2313 0.2287 -0.0056 0.0124 0.0166 245 ASP A CA +2055 C C . ASP A 245 ? 0.2178 0.2185 0.2068 -0.0093 0.0079 0.0104 245 ASP A C +2056 O O . ASP A 245 ? 0.2251 0.2189 0.2021 -0.0101 0.0116 0.0070 245 ASP A O +2057 C CB . ASP A 245 ? 0.2592 0.2649 0.2687 -0.0042 0.0107 0.0180 245 ASP A CB +2058 C CG . ASP A 245 ? 0.3428 0.3489 0.3613 -0.0002 0.0180 0.0237 245 ASP A CG +2059 O OD1 . ASP A 245 ? 0.3544 0.3601 0.3744 0.0020 0.0244 0.0273 245 ASP A OD1 +2060 O OD2 . ASP A 245 ? 0.3785 0.3852 0.4024 0.0008 0.0174 0.0248 245 ASP A OD2 +2061 N N . HIS A 246 ? 0.2032 0.2084 0.1955 -0.0114 0.0000 0.0096 246 HIS A N +2062 C CA . HIS A 246 ? 0.2009 0.2041 0.1837 -0.0146 -0.0039 0.0052 246 HIS A CA +2063 C C . HIS A 246 ? 0.2030 0.2044 0.1775 -0.0167 -0.0019 0.0047 246 HIS A C +2064 O O . HIS A 246 ? 0.2037 0.2007 0.1676 -0.0192 -0.0020 0.0017 246 HIS A O +2065 C CB . HIS A 246 ? 0.2012 0.2089 0.1896 -0.0157 -0.0114 0.0055 246 HIS A CB +2066 C CG . HIS A 246 ? 0.2251 0.2332 0.2186 -0.0144 -0.0143 0.0054 246 HIS A CG +2067 N ND1 . HIS A 246 ? 0.2381 0.2491 0.2389 -0.0146 -0.0197 0.0075 246 HIS A ND1 +2068 C CD2 . HIS A 246 ? 0.2434 0.2488 0.2352 -0.0134 -0.0129 0.0037 246 HIS A CD2 +2069 C CE1 . HIS A 246 ? 0.2470 0.2568 0.2495 -0.0138 -0.0215 0.0070 246 HIS A CE1 +2070 N NE2 . HIS A 246 ? 0.2537 0.2608 0.2516 -0.0129 -0.0174 0.0048 246 HIS A NE2 +2071 N N . VAL A 247 ? 0.2002 0.2054 0.1801 -0.0161 -0.0010 0.0083 247 VAL A N +2072 C CA . VAL A 247 ? 0.2044 0.2082 0.1767 -0.0182 0.0010 0.0085 247 VAL A CA +2073 C C . VAL A 247 ? 0.2190 0.2136 0.1784 -0.0181 0.0082 0.0065 247 VAL A C +2074 O O . VAL A 247 ? 0.2279 0.2181 0.1753 -0.0215 0.0078 0.0042 247 VAL A O +2075 C CB . VAL A 247 ? 0.2085 0.2181 0.1902 -0.0168 0.0018 0.0134 247 VAL A CB +2076 C CG1 . VAL A 247 ? 0.2220 0.2293 0.1947 -0.0186 0.0050 0.0137 247 VAL A CG1 +2077 C CG2 . VAL A 247 ? 0.2124 0.2290 0.2044 -0.0177 -0.0057 0.0150 247 VAL A CG2 +2078 N N . ASP A 248 ? 0.2240 0.2157 0.1861 -0.0143 0.0144 0.0078 248 ASP A N +2079 C CA . ASP A 248 ? 0.2398 0.2205 0.1885 -0.0134 0.0226 0.0058 248 ASP A CA +2080 C C . ASP A 248 ? 0.2470 0.2205 0.1838 -0.0164 0.0205 0.0006 248 ASP A C +2081 O O . ASP A 248 ? 0.2636 0.2275 0.1848 -0.0189 0.0234 -0.0021 248 ASP A O +2082 C CB . ASP A 248 ? 0.2546 0.2342 0.2111 -0.0081 0.0302 0.0092 248 ASP A CB +2083 C CG . ASP A 248 ? 0.2938 0.2793 0.2610 -0.0051 0.0336 0.0155 248 ASP A CG +2084 O OD1 . ASP A 248 ? 0.3003 0.2881 0.2652 -0.0070 0.0318 0.0162 248 ASP A OD1 +2085 O OD2 . ASP A 248 ? 0.3247 0.3128 0.3031 -0.0010 0.0376 0.0200 248 ASP A OD2 +2086 N N . ILE A 249 ? 0.2398 0.2176 0.1835 -0.0165 0.0152 -0.0006 249 ILE A N +2087 C CA . ILE A 249 ? 0.2522 0.2245 0.1865 -0.0193 0.0126 -0.0048 249 ILE A CA +2088 C C . ILE A 249 ? 0.2467 0.2183 0.1717 -0.0247 0.0074 -0.0062 249 ILE A C +2089 O O . ILE A 249 ? 0.2569 0.2212 0.1701 -0.0279 0.0069 -0.0089 249 ILE A O +2090 C CB . ILE A 249 ? 0.2738 0.2517 0.2187 -0.0177 0.0083 -0.0049 249 ILE A CB +2091 C CG1 . ILE A 249 ? 0.2886 0.2655 0.2407 -0.0132 0.0136 -0.0033 249 ILE A CG1 +2092 C CG2 . ILE A 249 ? 0.2960 0.2709 0.2335 -0.0209 0.0042 -0.0082 249 ILE A CG2 +2093 C CD1 . ILE A 249 ? 0.3018 0.2864 0.2672 -0.0115 0.0089 -0.0017 249 ILE A CD1 +2094 N N . LEU A 250 ? 0.2261 0.2054 0.1573 -0.0259 0.0032 -0.0039 250 LEU A N +2095 C CA . LEU A 250 ? 0.2291 0.2096 0.1540 -0.0310 -0.0018 -0.0037 250 LEU A CA +2096 C C . LEU A 250 ? 0.2518 0.2255 0.1636 -0.0339 0.0017 -0.0036 250 LEU A C +2097 O O . LEU A 250 ? 0.2569 0.2306 0.1623 -0.0388 -0.0024 -0.0030 250 LEU A O +2098 C CB . LEU A 250 ? 0.2045 0.1956 0.1420 -0.0306 -0.0071 -0.0010 250 LEU A CB +2099 C CG . LEU A 250 ? 0.1998 0.1957 0.1467 -0.0288 -0.0113 -0.0014 250 LEU A CG +2100 C CD1 . LEU A 250 ? 0.1986 0.2022 0.1567 -0.0275 -0.0148 0.0013 250 LEU A CD1 +2101 C CD2 . LEU A 250 ? 0.2085 0.2031 0.1500 -0.0320 -0.0152 -0.0024 250 LEU A CD2 +2102 N N . GLY A 251 ? 0.2570 0.2248 0.1650 -0.0307 0.0094 -0.0036 251 GLY A N +2103 C CA . GLY A 251 ? 0.2790 0.2382 0.1725 -0.0327 0.0142 -0.0036 251 GLY A CA +2104 C C . GLY A 251 ? 0.3006 0.2497 0.1753 -0.0393 0.0116 -0.0062 251 GLY A C +2105 O O . GLY A 251 ? 0.3064 0.2557 0.1743 -0.0440 0.0085 -0.0049 251 GLY A O +2106 N N . PRO A 252 ? 0.3063 0.2471 0.1729 -0.0404 0.0118 -0.0095 252 PRO A N +2107 C CA . PRO A 252 ? 0.3173 0.2481 0.1658 -0.0477 0.0081 -0.0113 252 PRO A CA +2108 C C . PRO A 252 ? 0.3076 0.2475 0.1604 -0.0534 -0.0017 -0.0086 252 PRO A C +2109 O O . PRO A 252 ? 0.3219 0.2563 0.1613 -0.0599 -0.0047 -0.0078 252 PRO A O +2110 C CB . PRO A 252 ? 0.3331 0.2562 0.1776 -0.0468 0.0095 -0.0146 252 PRO A CB +2111 C CG . PRO A 252 ? 0.3405 0.2637 0.1935 -0.0389 0.0180 -0.0148 252 PRO A CG +2112 C CD . PRO A 252 ? 0.3076 0.2467 0.1802 -0.0356 0.0156 -0.0111 252 PRO A CD +2113 N N . LEU A 253 ? 0.2874 0.2407 0.1582 -0.0512 -0.0065 -0.0066 253 LEU A N +2114 C CA . LEU A 253 ? 0.2797 0.2418 0.1560 -0.0557 -0.0145 -0.0031 253 LEU A CA +2115 C C . LEU A 253 ? 0.2847 0.2525 0.1635 -0.0570 -0.0153 0.0001 253 LEU A C +2116 O O . LEU A 253 ? 0.2944 0.2644 0.1698 -0.0629 -0.0206 0.0032 253 LEU A O +2117 C CB . LEU A 253 ? 0.2645 0.2373 0.1577 -0.0522 -0.0181 -0.0020 253 LEU A CB +2118 C CG . LEU A 253 ? 0.2797 0.2484 0.1705 -0.0525 -0.0193 -0.0040 253 LEU A CG +2119 C CD1 . LEU A 253 ? 0.2723 0.2503 0.1790 -0.0479 -0.0212 -0.0033 253 LEU A CD1 +2120 C CD2 . LEU A 253 ? 0.3014 0.2666 0.1826 -0.0600 -0.0251 -0.0021 253 LEU A CD2 +2121 N N . SER A 254 ? 0.2804 0.2509 0.1657 -0.0518 -0.0101 0.0001 254 SER A N +2122 C CA . SER A 254 ? 0.2840 0.2596 0.1720 -0.0525 -0.0100 0.0032 254 SER A CA +2123 C C . SER A 254 ? 0.3057 0.2704 0.1738 -0.0578 -0.0082 0.0029 254 SER A C +2124 O O . SER A 254 ? 0.3123 0.2805 0.1782 -0.0624 -0.0119 0.0061 254 SER A O +2125 C CB . SER A 254 ? 0.2930 0.2724 0.1917 -0.0456 -0.0043 0.0035 254 SER A CB +2126 O OG . SER A 254 ? 0.3179 0.3022 0.2193 -0.0461 -0.0039 0.0068 254 SER A OG +2127 N N . ALA A 255 ? 0.3155 0.2664 0.1685 -0.0573 -0.0023 -0.0008 255 ALA A N +2128 C CA . ALA A 255 ? 0.3400 0.2771 0.1707 -0.0623 0.0002 -0.0017 255 ALA A CA +2129 C C . ALA A 255 ? 0.3655 0.2991 0.1848 -0.0715 -0.0082 -0.0007 255 ALA A C +2130 O O . ALA A 255 ? 0.3732 0.3025 0.1802 -0.0774 -0.0103 0.0012 255 ALA A O +2131 C CB . ALA A 255 ? 0.3488 0.2704 0.1658 -0.0590 0.0091 -0.0060 255 ALA A CB +2132 N N . GLN A 256 ? 0.3714 0.3069 0.1952 -0.0729 -0.0131 -0.0013 256 GLN A N +2133 C CA . GLN A 256 ? 0.3882 0.3212 0.2036 -0.0818 -0.0217 0.0009 256 GLN A CA +2134 C C . GLN A 256 ? 0.3764 0.3230 0.2027 -0.0857 -0.0289 0.0071 256 GLN A C +2135 O O . GLN A 256 ? 0.3964 0.3390 0.2109 -0.0941 -0.0342 0.0102 256 GLN A O +2136 C CB . GLN A 256 ? 0.4192 0.3527 0.2398 -0.0813 -0.0246 -0.0004 256 GLN A CB +2137 C CG . GLN A 256 ? 0.4812 0.4119 0.2938 -0.0905 -0.0335 0.0028 256 GLN A CG +2138 C CD . GLN A 256 ? 0.5459 0.4792 0.3663 -0.0894 -0.0364 0.0025 256 GLN A CD +2139 O OE1 . GLN A 256 ? 0.5664 0.4991 0.3928 -0.0825 -0.0312 -0.0015 256 GLN A OE1 +2140 N NE2 . GLN A 256 ? 0.5577 0.4944 0.3791 -0.0964 -0.0450 0.0075 256 GLN A NE2 +2141 N N . THR A 257 ? 0.3374 0.2991 0.1853 -0.0801 -0.0291 0.0093 257 THR A N +2142 C CA . THR A 257 ? 0.3177 0.2924 0.1780 -0.0828 -0.0352 0.0154 257 THR A CA +2143 C C . THR A 257 ? 0.3148 0.2937 0.1766 -0.0824 -0.0332 0.0176 257 THR A C +2144 O O . THR A 257 ? 0.3169 0.3048 0.1857 -0.0860 -0.0382 0.0231 257 THR A O +2145 C CB . THR A 257 ? 0.3105 0.2976 0.1920 -0.0770 -0.0364 0.0167 257 THR A CB +2146 O OG1 . THR A 257 ? 0.3100 0.2992 0.1997 -0.0691 -0.0302 0.0135 257 THR A OG1 +2147 C CG2 . THR A 257 ? 0.3140 0.2985 0.1956 -0.0772 -0.0386 0.0155 257 THR A CG2 +2148 N N . GLY A 258 ? 0.3055 0.2787 0.1625 -0.0777 -0.0256 0.0140 258 GLY A N +2149 C CA . GLY A 258 ? 0.3007 0.2784 0.1606 -0.0763 -0.0230 0.0162 258 GLY A CA +2150 C C . GLY A 258 ? 0.2790 0.2716 0.1619 -0.0707 -0.0237 0.0188 258 GLY A C +2151 O O . GLY A 258 ? 0.2760 0.2747 0.1645 -0.0699 -0.0229 0.0217 258 GLY A O +2152 N N . ILE A 259 ? 0.2544 0.2524 0.1504 -0.0664 -0.0249 0.0176 259 ILE A N +2153 C CA . ILE A 259 ? 0.2404 0.2499 0.1558 -0.0614 -0.0257 0.0196 259 ILE A CA +2154 C C . ILE A 259 ? 0.2324 0.2402 0.1529 -0.0544 -0.0200 0.0163 259 ILE A C +2155 O O . ILE A 259 ? 0.2410 0.2438 0.1594 -0.0521 -0.0183 0.0128 259 ILE A O +2156 C CB . ILE A 259 ? 0.2472 0.2634 0.1733 -0.0617 -0.0310 0.0216 259 ILE A CB +2157 C CG1 . ILE A 259 ? 0.2679 0.2870 0.1908 -0.0690 -0.0367 0.0267 259 ILE A CG1 +2158 C CG2 . ILE A 259 ? 0.2428 0.2682 0.1863 -0.0565 -0.0312 0.0231 259 ILE A CG2 +2159 C CD1 . ILE A 259 ? 0.2874 0.3119 0.2193 -0.0695 -0.0411 0.0296 259 ILE A CD1 +2160 N N . ALA A 260 ? 0.2177 0.2297 0.1452 -0.0512 -0.0172 0.0179 260 ALA A N +2161 C CA . ALA A 260 ? 0.2111 0.2229 0.1457 -0.0449 -0.0123 0.0165 260 ALA A CA +2162 C C . ALA A 260 ? 0.1974 0.2133 0.1439 -0.0416 -0.0150 0.0154 260 ALA A C +2163 O O . ALA A 260 ? 0.1930 0.2148 0.1470 -0.0426 -0.0201 0.0169 260 ALA A O +2164 C CB . ALA A 260 ? 0.2178 0.2359 0.1611 -0.0428 -0.0106 0.0202 260 ALA A CB +2165 N N . VAL A 261 ? 0.1862 0.1984 0.1340 -0.0375 -0.0114 0.0130 261 VAL A N +2166 C CA . VAL A 261 ? 0.1849 0.1997 0.1422 -0.0346 -0.0140 0.0118 261 VAL A CA +2167 C C . VAL A 261 ? 0.1738 0.1965 0.1447 -0.0331 -0.0179 0.0145 261 VAL A C +2168 O O . VAL A 261 ? 0.1797 0.2045 0.1548 -0.0332 -0.0219 0.0141 261 VAL A O +2169 C CB . VAL A 261 ? 0.2018 0.2123 0.1596 -0.0306 -0.0094 0.0099 261 VAL A CB +2170 C CG1 . VAL A 261 ? 0.1959 0.2093 0.1635 -0.0281 -0.0127 0.0092 261 VAL A CG1 +2171 C CG2 . VAL A 261 ? 0.2294 0.2303 0.1728 -0.0321 -0.0058 0.0066 261 VAL A CG2 +2172 N N . LEU A 262 ? 0.1670 0.1935 0.1440 -0.0319 -0.0165 0.0175 262 LEU A N +2173 C CA . LEU A 262 ? 0.1643 0.1971 0.1536 -0.0308 -0.0205 0.0201 262 LEU A CA +2174 C C . LEU A 262 ? 0.1622 0.1988 0.1522 -0.0338 -0.0245 0.0217 262 LEU A C +2175 O O . LEU A 262 ? 0.1616 0.2008 0.1595 -0.0329 -0.0281 0.0226 262 LEU A O +2176 C CB . LEU A 262 ? 0.1625 0.1988 0.1594 -0.0288 -0.0184 0.0237 262 LEU A CB +2177 C CG . LEU A 262 ? 0.1797 0.2140 0.1806 -0.0252 -0.0152 0.0239 262 LEU A CG +2178 C CD1 . LEU A 262 ? 0.1849 0.2233 0.1941 -0.0233 -0.0126 0.0290 262 LEU A CD1 +2179 C CD2 . LEU A 262 ? 0.1798 0.2139 0.1872 -0.0239 -0.0195 0.0228 262 LEU A CD2 +2180 N N . ASP A 263 ? 0.1652 0.2012 0.1467 -0.0376 -0.0240 0.0223 263 ASP A N +2181 C CA . ASP A 263 ? 0.1578 0.1982 0.1413 -0.0407 -0.0279 0.0249 263 ASP A CA +2182 C C . ASP A 263 ? 0.1734 0.2122 0.1570 -0.0405 -0.0304 0.0233 263 ASP A C +2183 O O . ASP A 263 ? 0.1790 0.2213 0.1698 -0.0400 -0.0331 0.0254 263 ASP A O +2184 C CB . ASP A 263 ? 0.1698 0.2097 0.1437 -0.0457 -0.0277 0.0267 263 ASP A CB +2185 C CG . ASP A 263 ? 0.1838 0.2253 0.1567 -0.0461 -0.0250 0.0288 263 ASP A CG +2186 O OD1 . ASP A 263 ? 0.1696 0.2137 0.1512 -0.0423 -0.0234 0.0296 263 ASP A OD1 +2187 O OD2 . ASP A 263 ? 0.2039 0.2440 0.1674 -0.0504 -0.0248 0.0302 263 ASP A OD2 +2188 N N . MET A 264 ? 0.1646 0.1978 0.1403 -0.0405 -0.0289 0.0199 264 MET A N +2189 C CA . MET A 264 ? 0.1588 0.1907 0.1351 -0.0398 -0.0309 0.0187 264 MET A CA +2190 C C . MET A 264 ? 0.1625 0.1947 0.1475 -0.0352 -0.0315 0.0177 264 MET A C +2191 O O . MET A 264 ? 0.1712 0.2041 0.1599 -0.0342 -0.0334 0.0186 264 MET A O +2192 C CB . MET A 264 ? 0.1777 0.2035 0.1444 -0.0407 -0.0293 0.0155 264 MET A CB +2193 C CG . MET A 264 ? 0.1885 0.2142 0.1558 -0.0409 -0.0317 0.0157 264 MET A CG +2194 S SD . MET A 264 ? 0.2095 0.2401 0.1771 -0.0463 -0.0356 0.0214 264 MET A SD +2195 C CE . MET A 264 ? 0.2483 0.2724 0.2007 -0.0520 -0.0357 0.0202 264 MET A CE +2196 N N . CYS A 265 ? 0.1567 0.1879 0.1448 -0.0327 -0.0301 0.0165 265 CYS A N +2197 C CA . CYS A 265 ? 0.1578 0.1883 0.1529 -0.0294 -0.0318 0.0160 265 CYS A CA +2198 C C . CYS A 265 ? 0.1576 0.1912 0.1591 -0.0295 -0.0343 0.0189 265 CYS A C +2199 O O . CYS A 265 ? 0.1637 0.1946 0.1675 -0.0276 -0.0360 0.0183 265 CYS A O +2200 C CB . CYS A 265 ? 0.1574 0.1875 0.1559 -0.0276 -0.0304 0.0160 265 CYS A CB +2201 S SG . CYS A 265 ? 0.1704 0.1959 0.1636 -0.0262 -0.0268 0.0129 265 CYS A SG +2202 N N . ALA A 266 ? 0.1530 0.1913 0.1565 -0.0317 -0.0343 0.0220 266 ALA A N +2203 C CA . ALA A 266 ? 0.1644 0.2059 0.1747 -0.0318 -0.0364 0.0252 266 ALA A CA +2204 C C . ALA A 266 ? 0.1744 0.2162 0.1842 -0.0323 -0.0370 0.0266 266 ALA A C +2205 O O . ALA A 266 ? 0.1850 0.2259 0.1996 -0.0305 -0.0379 0.0280 266 ALA A O +2206 C CB . ALA A 266 ? 0.1742 0.2213 0.1873 -0.0342 -0.0362 0.0287 266 ALA A CB +2207 N N . SER A 267 ? 0.1711 0.2133 0.1750 -0.0346 -0.0364 0.0266 267 SER A N +2208 C CA . SER A 267 ? 0.1762 0.2192 0.1808 -0.0350 -0.0370 0.0290 267 SER A CA +2209 C C . SER A 267 ? 0.1678 0.2053 0.1723 -0.0308 -0.0364 0.0261 267 SER A C +2210 O O . SER A 267 ? 0.1705 0.2073 0.1788 -0.0287 -0.0360 0.0283 267 SER A O +2211 C CB . SER A 267 ? 0.2095 0.2533 0.2072 -0.0390 -0.0373 0.0297 267 SER A CB +2212 O OG . SER A 267 ? 0.2588 0.3075 0.2561 -0.0436 -0.0386 0.0337 267 SER A OG +2213 N N . LEU A 268 ? 0.1561 0.1892 0.1560 -0.0295 -0.0358 0.0216 268 LEU A N +2214 C CA . LEU A 268 ? 0.1563 0.1837 0.1548 -0.0260 -0.0354 0.0188 268 LEU A CA +2215 C C . LEU A 268 ? 0.1657 0.1895 0.1678 -0.0233 -0.0363 0.0187 268 LEU A C +2216 O O . LEU A 268 ? 0.1637 0.1828 0.1651 -0.0206 -0.0357 0.0187 268 LEU A O +2217 C CB . LEU A 268 ? 0.1529 0.1770 0.1465 -0.0255 -0.0348 0.0147 268 LEU A CB +2218 C CG . LEU A 268 ? 0.1661 0.1844 0.1579 -0.0223 -0.0349 0.0118 268 LEU A CG +2219 C CD1 . LEU A 268 ? 0.1760 0.1930 0.1665 -0.0209 -0.0341 0.0130 268 LEU A CD1 +2220 C CD2 . LEU A 268 ? 0.1727 0.1891 0.1609 -0.0223 -0.0341 0.0087 268 LEU A CD2 +2221 N N . LYS A 269 ? 0.1523 0.1773 0.1577 -0.0241 -0.0375 0.0191 269 LYS A N +2222 C CA . LYS A 269 ? 0.1498 0.1707 0.1582 -0.0225 -0.0392 0.0194 269 LYS A CA +2223 C C . LYS A 269 ? 0.1584 0.1790 0.1695 -0.0214 -0.0383 0.0224 269 LYS A C +2224 O O . LYS A 269 ? 0.1699 0.1828 0.1789 -0.0188 -0.0381 0.0215 269 LYS A O +2225 C CB . LYS A 269 ? 0.1600 0.1846 0.1732 -0.0242 -0.0407 0.0208 269 LYS A CB +2226 C CG . LYS A 269 ? 0.2053 0.2261 0.2223 -0.0235 -0.0433 0.0219 269 LYS A CG +2227 C CD . LYS A 269 ? 0.2400 0.2659 0.2629 -0.0252 -0.0448 0.0241 269 LYS A CD +2228 C CE . LYS A 269 ? 0.2824 0.3067 0.3105 -0.0255 -0.0474 0.0265 269 LYS A CE +2229 N NZ . LYS A 269 ? 0.2965 0.3278 0.3318 -0.0272 -0.0484 0.0298 269 LYS A NZ +2230 N N . GLU A 270 ? 0.1579 0.1859 0.1729 -0.0234 -0.0374 0.0264 270 GLU A N +2231 C CA . GLU A 270 ? 0.1697 0.1985 0.1891 -0.0223 -0.0360 0.0306 270 GLU A CA +2232 C C . GLU A 270 ? 0.1841 0.2088 0.2007 -0.0194 -0.0335 0.0309 270 GLU A C +2233 O O . GLU A 270 ? 0.1935 0.2128 0.2111 -0.0162 -0.0315 0.0324 270 GLU A O +2234 C CB . GLU A 270 ? 0.2006 0.2393 0.2255 -0.0258 -0.0363 0.0358 270 GLU A CB +2235 C CG . GLU A 270 ? 0.2905 0.3331 0.3190 -0.0280 -0.0381 0.0365 270 GLU A CG +2236 C CD . GLU A 270 ? 0.3871 0.4255 0.4198 -0.0259 -0.0388 0.0367 270 GLU A CD +2237 O OE1 . GLU A 270 ? 0.4059 0.4431 0.4426 -0.0243 -0.0375 0.0400 270 GLU A OE1 +2238 O OE2 . GLU A 270 ? 0.4043 0.4403 0.4364 -0.0260 -0.0407 0.0342 270 GLU A OE2 +2239 N N . LEU A 271 ? 0.1794 0.2056 0.1921 -0.0203 -0.0333 0.0295 271 LEU A N +2240 C CA . LEU A 271 ? 0.1824 0.2050 0.1928 -0.0174 -0.0309 0.0300 271 LEU A CA +2241 C C . LEU A 271 ? 0.1924 0.2041 0.1972 -0.0133 -0.0299 0.0258 271 LEU A C +2242 O O . LEU A 271 ? 0.2133 0.2197 0.2169 -0.0095 -0.0268 0.0273 271 LEU A O +2243 C CB . LEU A 271 ? 0.1825 0.2083 0.1894 -0.0196 -0.0316 0.0289 271 LEU A CB +2244 C CG . LEU A 271 ? 0.1939 0.2284 0.2042 -0.0240 -0.0327 0.0340 271 LEU A CG +2245 C CD1 . LEU A 271 ? 0.2015 0.2366 0.2060 -0.0269 -0.0339 0.0316 271 LEU A CD1 +2246 C CD2 . LEU A 271 ? 0.2042 0.2418 0.2211 -0.0226 -0.0308 0.0409 271 LEU A CD2 +2247 N N . LEU A 272 ? 0.1758 0.1833 0.1766 -0.0139 -0.0325 0.0211 272 LEU A N +2248 C CA . LEU A 272 ? 0.1901 0.1864 0.1843 -0.0111 -0.0327 0.0173 272 LEU A CA +2249 C C . LEU A 272 ? 0.2116 0.2007 0.2057 -0.0091 -0.0319 0.0186 272 LEU A C +2250 O O . LEU A 272 ? 0.2267 0.2053 0.2144 -0.0057 -0.0297 0.0175 272 LEU A O +2251 C CB . LEU A 272 ? 0.1912 0.1860 0.1829 -0.0130 -0.0362 0.0135 272 LEU A CB +2252 C CG . LEU A 272 ? 0.2166 0.2148 0.2063 -0.0139 -0.0361 0.0114 272 LEU A CG +2253 C CD1 . LEU A 272 ? 0.2272 0.2256 0.2170 -0.0157 -0.0389 0.0091 272 LEU A CD1 +2254 C CD2 . LEU A 272 ? 0.2454 0.2379 0.2294 -0.0109 -0.0341 0.0099 272 LEU A CD2 +2255 N N . GLN A 273 ? 0.2054 0.1992 0.2057 -0.0112 -0.0335 0.0209 273 GLN A N +2256 C CA . GLN A 273 ? 0.2237 0.2105 0.2243 -0.0099 -0.0332 0.0221 273 GLN A CA +2257 C C . GLN A 273 ? 0.2527 0.2390 0.2565 -0.0068 -0.0283 0.0266 273 GLN A C +2258 O O . GLN A 273 ? 0.2737 0.2493 0.2739 -0.0040 -0.0263 0.0267 273 GLN A O +2259 C CB . GLN A 273 ? 0.2243 0.2171 0.2315 -0.0133 -0.0367 0.0234 273 GLN A CB +2260 C CG . GLN A 273 ? 0.2464 0.2378 0.2515 -0.0156 -0.0413 0.0202 273 GLN A CG +2261 C CD . GLN A 273 ? 0.2852 0.2832 0.2979 -0.0185 -0.0442 0.0225 273 GLN A CD +2262 O OE1 . GLN A 273 ? 0.3006 0.3075 0.3202 -0.0196 -0.0430 0.0261 273 GLN A OE1 +2263 N NE2 . GLN A 273 ? 0.2929 0.2871 0.3048 -0.0200 -0.0483 0.0211 273 GLN A NE2 +2264 N N . ASN A 274 ? 0.2545 0.2516 0.2649 -0.0075 -0.0264 0.0309 274 ASN A N +2265 C CA . ASN A 274 ? 0.2714 0.2704 0.2878 -0.0049 -0.0218 0.0371 274 ASN A CA +2266 C C . ASN A 274 ? 0.2823 0.2817 0.2981 -0.0020 -0.0178 0.0397 274 ASN A C +2267 O O . ASN A 274 ? 0.2916 0.2917 0.3129 0.0010 -0.0132 0.0457 274 ASN A O +2268 C CB . ASN A 274 ? 0.2879 0.2999 0.3149 -0.0086 -0.0232 0.0426 274 ASN A CB +2269 C CG . ASN A 274 ? 0.3608 0.3720 0.3895 -0.0106 -0.0263 0.0411 274 ASN A CG +2270 O OD1 . ASN A 274 ? 0.3974 0.4019 0.4271 -0.0083 -0.0247 0.0422 274 ASN A OD1 +2271 N ND2 . ASN A 274 ? 0.3745 0.3917 0.4032 -0.0146 -0.0305 0.0387 274 ASN A ND2 +2272 N N . GLY A 275 ? 0.2828 0.2823 0.2932 -0.0028 -0.0193 0.0359 275 GLY A N +2273 C CA . GLY A 275 ? 0.2865 0.2874 0.2970 -0.0005 -0.0161 0.0386 275 GLY A CA +2274 C C . GLY A 275 ? 0.2849 0.2996 0.3049 -0.0041 -0.0171 0.0452 275 GLY A C +2275 O O . GLY A 275 ? 0.2838 0.3064 0.3087 -0.0085 -0.0203 0.0469 275 GLY A O +2276 N N A MET A 276 ? 0.2877 0.3051 0.3100 -0.0024 -0.0146 0.0494 276 MET A N +2277 N N B MET A 276 ? 0.2802 0.2977 0.3025 -0.0025 -0.0147 0.0494 276 MET A N +2278 C CA A MET A 276 ? 0.2918 0.3217 0.3226 -0.0067 -0.0165 0.0565 276 MET A CA +2279 C CA B MET A 276 ? 0.2766 0.3065 0.3075 -0.0066 -0.0165 0.0566 276 MET A CA +2280 C C A MET A 276 ? 0.2913 0.3266 0.3338 -0.0049 -0.0128 0.0668 276 MET A C +2281 C C B MET A 276 ? 0.2834 0.3188 0.3259 -0.0052 -0.0132 0.0666 276 MET A C +2282 O O A MET A 276 ? 0.2868 0.3330 0.3374 -0.0092 -0.0151 0.0741 276 MET A O +2283 O O B MET A 276 ? 0.2781 0.3245 0.3285 -0.0099 -0.0158 0.0734 276 MET A O +2284 C CB A MET A 276 ? 0.3085 0.3402 0.3362 -0.0077 -0.0176 0.0558 276 MET A CB +2285 C CB B MET A 276 ? 0.2735 0.3053 0.3025 -0.0070 -0.0168 0.0572 276 MET A CB +2286 C CG A MET A 276 ? 0.3395 0.3688 0.3581 -0.0109 -0.0218 0.0471 276 MET A CG +2287 C CG B MET A 276 ? 0.2760 0.3074 0.2968 -0.0110 -0.0214 0.0498 276 MET A CG +2288 S SD A MET A 276 ? 0.4400 0.4671 0.4525 -0.0105 -0.0223 0.0438 276 MET A SD +2289 S SD B MET A 276 ? 0.2332 0.2709 0.2548 -0.0145 -0.0237 0.0531 276 MET A SD +2290 C CE A MET A 276 ? 0.3629 0.4010 0.3831 -0.0152 -0.0244 0.0528 276 MET A CE +2291 C CE B MET A 276 ? 0.2208 0.2526 0.2310 -0.0159 -0.0263 0.0426 276 MET A CE +2292 N N . ASN A 277 ? 0.2923 0.3197 0.3354 0.0008 -0.0075 0.0678 277 ASN A N +2293 C CA . ASN A 277 ? 0.2954 0.3270 0.3503 0.0034 -0.0029 0.0778 277 ASN A CA +2294 C C . ASN A 277 ? 0.2873 0.3268 0.3515 0.0043 -0.0004 0.0878 277 ASN A C +2295 O O . ASN A 277 ? 0.2883 0.3383 0.3654 0.0022 -0.0004 0.0980 277 ASN A O +2296 C CB . ASN A 277 ? 0.3146 0.3549 0.3771 -0.0016 -0.0066 0.0811 277 ASN A CB +2297 C CG . ASN A 277 ? 0.3801 0.4120 0.4375 -0.0004 -0.0067 0.0749 277 ASN A CG +2298 O OD1 . ASN A 277 ? 0.4070 0.4407 0.4607 -0.0050 -0.0120 0.0694 277 ASN A OD1 +2299 N ND2 . ASN A 277 ? 0.3897 0.4116 0.4467 0.0058 -0.0005 0.0760 277 ASN A ND2 +2300 N N . GLY A 278 ? 0.2732 0.3084 0.3318 0.0070 0.0013 0.0856 278 GLY A N +2301 C CA . GLY A 278 ? 0.2576 0.3004 0.3255 0.0080 0.0034 0.0955 278 GLY A CA +2302 C C . GLY A 278 ? 0.2420 0.2976 0.3147 -0.0003 -0.0042 0.0992 278 GLY A C +2303 O O . GLY A 278 ? 0.2411 0.3048 0.3234 -0.0011 -0.0039 0.1091 278 GLY A O +2304 N N A ARG A 279 ? 0.2374 0.2940 0.3026 -0.0066 -0.0109 0.0916 279 ARG A N +2305 N N B ARG A 279 ? 0.2343 0.2909 0.2996 -0.0067 -0.0110 0.0916 279 ARG A N +2306 C CA A ARG A 279 ? 0.2322 0.2977 0.2981 -0.0149 -0.0181 0.0936 279 ARG A CA +2307 C CA B ARG A 279 ? 0.2260 0.2915 0.2918 -0.0151 -0.0183 0.0935 279 ARG A CA +2308 C C A ARG A 279 ? 0.2276 0.2883 0.2826 -0.0159 -0.0206 0.0856 279 ARG A C +2309 C C B ARG A 279 ? 0.2250 0.2857 0.2799 -0.0160 -0.0206 0.0856 279 ARG A C +2310 O O A ARG A 279 ? 0.2311 0.2822 0.2782 -0.0106 -0.0172 0.0780 279 ARG A O +2311 O O B ARG A 279 ? 0.2290 0.2801 0.2759 -0.0107 -0.0173 0.0778 279 ARG A O +2312 C CB A ARG A 279 ? 0.2510 0.3206 0.3158 -0.0214 -0.0232 0.0918 279 ARG A CB +2313 C CB B ARG A 279 ? 0.2362 0.3051 0.2999 -0.0213 -0.0233 0.0907 279 ARG A CB +2314 C CG A ARG A 279 ? 0.2938 0.3698 0.3709 -0.0211 -0.0214 0.1010 279 ARG A CG +2315 C CG B ARG A 279 ? 0.2661 0.3395 0.3403 -0.0205 -0.0212 0.0976 279 ARG A CG +2316 C CD A ARG A 279 ? 0.3399 0.4224 0.4173 -0.0287 -0.0273 0.1016 279 ARG A CD +2317 C CD B ARG A 279 ? 0.2998 0.3726 0.3693 -0.0240 -0.0245 0.0916 279 ARG A CD +2318 N NE A ARG A 279 ? 0.3833 0.4723 0.4588 -0.0371 -0.0340 0.1049 279 ARG A NE +2319 N NE B ARG A 279 ? 0.3295 0.4052 0.4085 -0.0223 -0.0219 0.0973 279 ARG A NE +2320 C CZ A ARG A 279 ? 0.4179 0.5167 0.5037 -0.0417 -0.0368 0.1170 279 ARG A CZ +2321 C CZ B ARG A 279 ? 0.3550 0.4260 0.4310 -0.0209 -0.0213 0.0917 279 ARG A CZ +2322 N NH1 A ARG A 279 ? 0.4125 0.5171 0.5131 -0.0382 -0.0327 0.1276 279 ARG A NH1 +2323 N NH1 B ARG A 279 ? 0.3504 0.4141 0.4149 -0.0210 -0.0232 0.0809 279 ARG A NH1 +2324 N NH2 A ARG A 279 ? 0.4248 0.5272 0.5060 -0.0501 -0.0437 0.1190 279 ARG A NH2 +2325 N NH2 B ARG A 279 ? 0.3509 0.4248 0.4364 -0.0195 -0.0189 0.0976 279 ARG A NH2 +2326 N N . THR A 280 ? 0.2166 0.2832 0.2709 -0.0228 -0.0264 0.0879 280 THR A N +2327 C CA . THR A 280 ? 0.2139 0.2762 0.2585 -0.0242 -0.0287 0.0810 280 THR A CA +2328 C C . THR A 280 ? 0.2026 0.2653 0.2386 -0.0320 -0.0349 0.0758 280 THR A C +2329 O O . THR A 280 ? 0.1972 0.2652 0.2356 -0.0377 -0.0384 0.0798 280 THR A O +2330 C CB . THR A 280 ? 0.2364 0.3030 0.2869 -0.0242 -0.0288 0.0887 280 THR A CB +2331 O OG1 . THR A 280 ? 0.2391 0.3154 0.2973 -0.0315 -0.0340 0.0988 280 THR A OG1 +2332 C CG2 . THR A 280 ? 0.2482 0.3129 0.3057 -0.0154 -0.0213 0.0936 280 THR A CG2 +2333 N N . ILE A 281 ? 0.1921 0.2483 0.2175 -0.0321 -0.0358 0.0669 281 ILE A N +2334 C CA . ILE A 281 ? 0.1942 0.2484 0.2097 -0.0384 -0.0402 0.0613 281 ILE A CA +2335 C C . ILE A 281 ? 0.1954 0.2471 0.2059 -0.0398 -0.0418 0.0598 281 ILE A C +2336 O O . ILE A 281 ? 0.1929 0.2404 0.2021 -0.0344 -0.0387 0.0558 281 ILE A O +2337 C CB . ILE A 281 ? 0.2069 0.2547 0.2150 -0.0359 -0.0385 0.0514 281 ILE A CB +2338 C CG1 . ILE A 281 ? 0.2075 0.2576 0.2209 -0.0346 -0.0371 0.0531 281 ILE A CG1 +2339 C CG2 . ILE A 281 ? 0.2187 0.2634 0.2162 -0.0414 -0.0415 0.0459 281 ILE A CG2 +2340 C CD1 . ILE A 281 ? 0.2148 0.2592 0.2228 -0.0321 -0.0358 0.0447 281 ILE A CD1 +2341 N N . LEU A 282 ? 0.1976 0.2518 0.2056 -0.0474 -0.0470 0.0638 282 LEU A N +2342 C CA . LEU A 282 ? 0.2014 0.2530 0.2048 -0.0495 -0.0492 0.0632 282 LEU A CA +2343 C C . LEU A 282 ? 0.2114 0.2652 0.2233 -0.0435 -0.0461 0.0674 282 LEU A C +2344 O O . LEU A 282 ? 0.2279 0.2771 0.2354 -0.0406 -0.0446 0.0622 282 LEU A O +2345 C CB . LEU A 282 ? 0.2020 0.2448 0.1923 -0.0498 -0.0488 0.0523 282 LEU A CB +2346 C CG . LEU A 282 ? 0.2157 0.2547 0.1952 -0.0564 -0.0518 0.0488 282 LEU A CG +2347 C CD1 . LEU A 282 ? 0.2203 0.2506 0.1889 -0.0551 -0.0497 0.0390 282 LEU A CD1 +2348 C CD2 . LEU A 282 ? 0.2288 0.2691 0.2051 -0.0654 -0.0580 0.0555 282 LEU A CD2 +2349 N N . GLY A 283 ? 0.2195 0.2802 0.2437 -0.0412 -0.0443 0.0767 283 GLY A N +2350 C CA . GLY A 283 ? 0.2237 0.2868 0.2570 -0.0349 -0.0402 0.0826 283 GLY A CA +2351 C C . GLY A 283 ? 0.2283 0.2848 0.2593 -0.0257 -0.0334 0.0759 283 GLY A C +2352 O O . GLY A 283 ? 0.2436 0.2998 0.2788 -0.0202 -0.0296 0.0791 283 GLY A O +2353 N N A SER A 284 ? 0.2168 0.2675 0.2403 -0.0242 -0.0321 0.0668 284 SER A N +2354 N N B SER A 284 ? 0.2200 0.2707 0.2436 -0.0242 -0.0321 0.0669 284 SER A N +2355 C CA A SER A 284 ? 0.2108 0.2539 0.2303 -0.0166 -0.0269 0.0603 284 SER A CA +2356 C CA B SER A 284 ? 0.2176 0.2606 0.2369 -0.0167 -0.0270 0.0601 284 SER A CA +2357 C C A SER A 284 ? 0.2077 0.2497 0.2305 -0.0132 -0.0236 0.0613 284 SER A C +2358 C C B SER A 284 ? 0.2128 0.2543 0.2350 -0.0132 -0.0236 0.0607 284 SER A C +2359 O O A SER A 284 ? 0.2003 0.2455 0.2245 -0.0173 -0.0261 0.0621 284 SER A O +2360 O O B SER A 284 ? 0.2104 0.2546 0.2333 -0.0172 -0.0261 0.0607 284 SER A O +2361 C CB A SER A 284 ? 0.2234 0.2600 0.2319 -0.0177 -0.0285 0.0493 284 SER A CB +2362 C CB B SER A 284 ? 0.2334 0.2699 0.2416 -0.0179 -0.0287 0.0492 284 SER A CB +2363 O OG A SER A 284 ? 0.2520 0.2810 0.2562 -0.0114 -0.0246 0.0435 284 SER A OG +2364 O OG B SER A 284 ? 0.2558 0.2918 0.2605 -0.0199 -0.0308 0.0477 284 SER A OG +2365 N N . ALA A 285 ? 0.2088 0.2447 0.2314 -0.0058 -0.0178 0.0607 285 ALA A N +2366 C CA . ALA A 285 ? 0.2189 0.2508 0.2425 -0.0020 -0.0141 0.0606 285 ALA A CA +2367 C C . ALA A 285 ? 0.2274 0.2492 0.2400 -0.0003 -0.0142 0.0498 285 ALA A C +2368 O O . ALA A 285 ? 0.2469 0.2625 0.2578 0.0030 -0.0114 0.0483 285 ALA A O +2369 C CB . ALA A 285 ? 0.2244 0.2542 0.2537 0.0051 -0.0071 0.0676 285 ALA A CB +2370 N N . LEU A 286 ? 0.2180 0.2377 0.2235 -0.0026 -0.0174 0.0429 286 LEU A N +2371 C CA . LEU A 286 ? 0.2259 0.2381 0.2229 -0.0022 -0.0186 0.0342 286 LEU A CA +2372 C C . LEU A 286 ? 0.2134 0.2293 0.2079 -0.0080 -0.0234 0.0299 286 LEU A C +2373 O O . LEU A 286 ? 0.2143 0.2366 0.2113 -0.0123 -0.0257 0.0329 286 LEU A O +2374 C CB . LEU A 286 ? 0.2449 0.2477 0.2345 0.0028 -0.0159 0.0300 286 LEU A CB +2375 C CG . LEU A 286 ? 0.2717 0.2762 0.2607 0.0035 -0.0156 0.0307 286 LEU A CG +2376 C CD1 . LEU A 286 ? 0.2898 0.2969 0.2759 -0.0012 -0.0201 0.0258 286 LEU A CD1 +2377 C CD2 . LEU A 286 ? 0.2887 0.2833 0.2704 0.0092 -0.0120 0.0279 286 LEU A CD2 +2378 N N . LEU A 287 ? 0.1966 0.2080 0.1863 -0.0085 -0.0248 0.0238 287 LEU A N +2379 C CA . LEU A 287 ? 0.1945 0.2084 0.1818 -0.0129 -0.0280 0.0201 287 LEU A CA +2380 C C . LEU A 287 ? 0.1947 0.2063 0.1774 -0.0127 -0.0283 0.0165 287 LEU A C +2381 O O . LEU A 287 ? 0.2180 0.2238 0.1970 -0.0098 -0.0277 0.0127 287 LEU A O +2382 C CB . LEU A 287 ? 0.2044 0.2153 0.1904 -0.0131 -0.0290 0.0166 287 LEU A CB +2383 C CG . LEU A 287 ? 0.2287 0.2422 0.2198 -0.0134 -0.0287 0.0204 287 LEU A CG +2384 C CD1 . LEU A 287 ? 0.2400 0.2492 0.2299 -0.0128 -0.0297 0.0172 287 LEU A CD1 +2385 C CD2 . LEU A 287 ? 0.2392 0.2611 0.2341 -0.0183 -0.0304 0.0244 287 LEU A CD2 +2386 N N A GLU A 288 ? 0.1777 0.1933 0.1603 -0.0162 -0.0297 0.0179 288 GLU A N +2387 N N B GLU A 288 ? 0.1778 0.1935 0.1605 -0.0162 -0.0297 0.0179 288 GLU A N +2388 C CA A GLU A 288 ? 0.1732 0.1869 0.1521 -0.0162 -0.0299 0.0150 288 GLU A CA +2389 C CA B GLU A 288 ? 0.1739 0.1877 0.1528 -0.0164 -0.0299 0.0151 288 GLU A CA +2390 C C A GLU A 288 ? 0.1716 0.1824 0.1461 -0.0175 -0.0305 0.0093 288 GLU A C +2391 C C B GLU A 288 ? 0.1723 0.1831 0.1468 -0.0175 -0.0305 0.0093 288 GLU A C +2392 O O A GLU A 288 ? 0.1728 0.1850 0.1461 -0.0209 -0.0314 0.0087 288 GLU A O +2393 O O B GLU A 288 ? 0.1742 0.1863 0.1476 -0.0208 -0.0314 0.0086 288 GLU A O +2394 C CB A GLU A 288 ? 0.1836 0.2015 0.1635 -0.0199 -0.0314 0.0192 288 GLU A CB +2395 C CB B GLU A 288 ? 0.1855 0.2036 0.1653 -0.0203 -0.0316 0.0192 288 GLU A CB +2396 C CG A GLU A 288 ? 0.2056 0.2277 0.1921 -0.0185 -0.0306 0.0266 288 GLU A CG +2397 C CG B GLU A 288 ? 0.2176 0.2336 0.1934 -0.0213 -0.0322 0.0166 288 GLU A CG +2398 C CD A GLU A 288 ? 0.2616 0.2815 0.2492 -0.0134 -0.0280 0.0276 288 GLU A CD +2399 C CD B GLU A 288 ? 0.2499 0.2642 0.2269 -0.0166 -0.0304 0.0167 288 GLU A CD +2400 O OE1 A GLU A 288 ? 0.2810 0.2966 0.2640 -0.0115 -0.0275 0.0224 288 GLU A OE1 +2401 O OE1 B GLU A 288 ? 0.2080 0.2184 0.1815 -0.0149 -0.0297 0.0118 288 GLU A OE1 +2402 O OE2 A GLU A 288 ? 0.2609 0.2838 0.2546 -0.0111 -0.0261 0.0343 288 GLU A OE2 +2403 O OE2 B GLU A 288 ? 0.2800 0.2969 0.2618 -0.0145 -0.0293 0.0222 288 GLU A OE2 +2404 N N . ASP A 289 ? 0.1707 0.1775 0.1429 -0.0148 -0.0298 0.0058 289 ASP A N +2405 C CA . ASP A 289 ? 0.1681 0.1727 0.1380 -0.0155 -0.0300 0.0016 289 ASP A CA +2406 C C . ASP A 289 ? 0.1799 0.1831 0.1473 -0.0156 -0.0295 -0.0004 289 ASP A C +2407 O O . ASP A 289 ? 0.1866 0.1876 0.1533 -0.0150 -0.0290 -0.0033 289 ASP A O +2408 C CB . ASP A 289 ? 0.1686 0.1696 0.1389 -0.0129 -0.0303 -0.0004 289 ASP A CB +2409 C CG . ASP A 289 ? 0.2007 0.1974 0.1689 -0.0096 -0.0302 -0.0016 289 ASP A CG +2410 O OD1 . ASP A 289 ? 0.1995 0.1965 0.1670 -0.0083 -0.0291 -0.0004 289 ASP A OD1 +2411 O OD2 . ASP A 289 ? 0.2094 0.2023 0.1766 -0.0086 -0.0313 -0.0034 289 ASP A OD2 +2412 N N . GLU A 290 ? 0.1783 0.1828 0.1452 -0.0165 -0.0297 0.0017 290 GLU A N +2413 C CA . GLU A 290 ? 0.1869 0.1897 0.1516 -0.0168 -0.0293 -0.0002 290 GLU A CA +2414 C C . GLU A 290 ? 0.1929 0.1955 0.1537 -0.0215 -0.0299 0.0002 290 GLU A C +2415 O O . GLU A 290 ? 0.1977 0.1993 0.1568 -0.0227 -0.0304 0.0005 290 GLU A O +2416 C CB . GLU A 290 ? 0.1961 0.1989 0.1623 -0.0136 -0.0289 0.0010 290 GLU A CB +2417 C CG . GLU A 290 ? 0.2235 0.2234 0.1899 -0.0094 -0.0282 -0.0005 290 GLU A CG +2418 C CD . GLU A 290 ? 0.2471 0.2452 0.2128 -0.0061 -0.0274 -0.0005 290 GLU A CD +2419 O OE1 . GLU A 290 ? 0.2213 0.2215 0.1880 -0.0064 -0.0272 0.0016 290 GLU A OE1 +2420 O OE2 . GLU A 290 ? 0.2664 0.2605 0.2300 -0.0035 -0.0273 -0.0023 290 GLU A OE2 +2421 N N . PHE A 291 ? 0.1857 0.1881 0.1443 -0.0244 -0.0300 -0.0001 291 PHE A N +2422 C CA . PHE A 291 ? 0.1967 0.1958 0.1484 -0.0288 -0.0300 -0.0010 291 PHE A CA +2423 C C . PHE A 291 ? 0.2040 0.2004 0.1537 -0.0282 -0.0273 -0.0041 291 PHE A C +2424 O O . PHE A 291 ? 0.2109 0.2098 0.1633 -0.0278 -0.0274 -0.0032 291 PHE A O +2425 C CB . PHE A 291 ? 0.1984 0.1994 0.1479 -0.0337 -0.0326 0.0028 291 PHE A CB +2426 C CG . PHE A 291 ? 0.2136 0.2184 0.1665 -0.0352 -0.0355 0.0079 291 PHE A CG +2427 C CD1 . PHE A 291 ? 0.2299 0.2323 0.1787 -0.0387 -0.0375 0.0090 291 PHE A CD1 +2428 C CD2 . PHE A 291 ? 0.2284 0.2390 0.1890 -0.0331 -0.0361 0.0122 291 PHE A CD2 +2429 C CE1 . PHE A 291 ? 0.2449 0.2518 0.1984 -0.0404 -0.0406 0.0152 291 PHE A CE1 +2430 C CE2 . PHE A 291 ? 0.2408 0.2556 0.2059 -0.0343 -0.0383 0.0184 291 PHE A CE2 +2431 C CZ . PHE A 291 ? 0.2375 0.2511 0.1997 -0.0380 -0.0407 0.0202 291 PHE A CZ +2432 N N . THR A 292 ? 0.2058 0.1971 0.1510 -0.0281 -0.0247 -0.0071 292 THR A N +2433 C CA . THR A 292 ? 0.2080 0.1966 0.1518 -0.0272 -0.0211 -0.0090 292 THR A CA +2434 C C . THR A 292 ? 0.2090 0.1937 0.1441 -0.0315 -0.0204 -0.0088 292 THR A C +2435 O O . THR A 292 ? 0.2094 0.1919 0.1380 -0.0358 -0.0229 -0.0077 292 THR A O +2436 C CB . THR A 292 ? 0.2254 0.2090 0.1675 -0.0252 -0.0175 -0.0115 292 THR A CB +2437 O OG1 . THR A 292 ? 0.2463 0.2233 0.1789 -0.0286 -0.0170 -0.0126 292 THR A OG1 +2438 C CG2 . THR A 292 ? 0.2222 0.2088 0.1715 -0.0217 -0.0184 -0.0116 292 THR A CG2 +2439 N N . PRO A 293 ? 0.2156 0.1986 0.1496 -0.0306 -0.0169 -0.0094 293 PRO A N +2440 C CA . PRO A 293 ? 0.2189 0.1964 0.1422 -0.0345 -0.0154 -0.0096 293 PRO A CA +2441 C C . PRO A 293 ? 0.2387 0.2063 0.1496 -0.0376 -0.0141 -0.0118 293 PRO A C +2442 O O . PRO A 293 ? 0.2490 0.2119 0.1493 -0.0430 -0.0162 -0.0112 293 PRO A O +2443 C CB . PRO A 293 ? 0.2324 0.2092 0.1581 -0.0312 -0.0103 -0.0099 293 PRO A CB +2444 C CG . PRO A 293 ? 0.2285 0.2138 0.1679 -0.0274 -0.0122 -0.0083 293 PRO A CG +2445 C CD . PRO A 293 ? 0.2079 0.1941 0.1504 -0.0263 -0.0145 -0.0092 293 PRO A CD +2446 N N . PHE A 294 ? 0.2447 0.2087 0.1564 -0.0347 -0.0111 -0.0139 294 PHE A N +2447 C CA A PHE A 294 ? 0.2722 0.2257 0.1719 -0.0374 -0.0097 -0.0162 294 PHE A CA +2448 C CA B PHE A 294 ? 0.2692 0.2227 0.1690 -0.0374 -0.0096 -0.0162 294 PHE A CA +2449 C C . PHE A 294 ? 0.2707 0.2255 0.1683 -0.0420 -0.0162 -0.0146 294 PHE A C +2450 O O . PHE A 294 ? 0.2910 0.2372 0.1757 -0.0475 -0.0177 -0.0150 294 PHE A O +2451 C CB A PHE A 294 ? 0.2858 0.2362 0.1888 -0.0329 -0.0050 -0.0182 294 PHE A CB +2452 C CB B PHE A 294 ? 0.2783 0.2291 0.1819 -0.0327 -0.0049 -0.0181 294 PHE A CB +2453 C CG A PHE A 294 ? 0.3135 0.2587 0.2155 -0.0291 0.0029 -0.0192 294 PHE A CG +2454 C CG B PHE A 294 ? 0.3077 0.2455 0.1983 -0.0345 -0.0013 -0.0209 294 PHE A CG +2455 C CD1 A PHE A 294 ? 0.3332 0.2756 0.2298 -0.0297 0.0061 -0.0187 294 PHE A CD1 +2456 C CD1 B PHE A 294 ? 0.3351 0.2616 0.2092 -0.0392 0.0000 -0.0222 294 PHE A CD1 +2457 C CD2 A PHE A 294 ? 0.3325 0.2768 0.2404 -0.0247 0.0074 -0.0197 294 PHE A CD2 +2458 C CD2 B PHE A 294 ? 0.3229 0.2587 0.2170 -0.0316 0.0011 -0.0221 294 PHE A CD2 +2459 C CE1 A PHE A 294 ? 0.3467 0.2849 0.2437 -0.0255 0.0141 -0.0185 294 PHE A CE1 +2460 C CE1 B PHE A 294 ? 0.3569 0.2690 0.2170 -0.0411 0.0034 -0.0250 294 PHE A CE1 +2461 C CE2 A PHE A 294 ? 0.3446 0.2853 0.2539 -0.0207 0.0151 -0.0191 294 PHE A CE2 +2462 C CE2 B PHE A 294 ? 0.3424 0.2652 0.2243 -0.0331 0.0047 -0.0246 294 PHE A CE2 +2463 C CZ A PHE A 294 ? 0.3455 0.2831 0.2493 -0.0209 0.0187 -0.0184 294 PHE A CZ +2464 C CZ B PHE A 294 ? 0.3512 0.2615 0.2156 -0.0379 0.0059 -0.0263 294 PHE A CZ +2465 N N . ASP A 295 ? 0.2529 0.2177 0.1624 -0.0401 -0.0201 -0.0122 295 ASP A N +2466 C CA . ASP A 295 ? 0.2476 0.2153 0.1577 -0.0437 -0.0259 -0.0092 295 ASP A CA +2467 C C . ASP A 295 ? 0.2600 0.2280 0.1646 -0.0496 -0.0298 -0.0060 295 ASP A C +2468 O O . ASP A 295 ? 0.2774 0.2420 0.1754 -0.0553 -0.0340 -0.0039 295 ASP A O +2469 C CB . ASP A 295 ? 0.2495 0.2275 0.1733 -0.0396 -0.0279 -0.0067 295 ASP A CB +2470 C CG . ASP A 295 ? 0.2638 0.2425 0.1933 -0.0346 -0.0256 -0.0088 295 ASP A CG +2471 O OD1 . ASP A 295 ? 0.2773 0.2493 0.2015 -0.0349 -0.0234 -0.0113 295 ASP A OD1 +2472 O OD2 . ASP A 295 ? 0.2535 0.2386 0.1922 -0.0306 -0.0260 -0.0078 295 ASP A OD2 +2473 N N . VAL A 296 ? 0.2445 0.2169 0.1525 -0.0487 -0.0290 -0.0051 296 VAL A N +2474 C CA . VAL A 296 ? 0.2485 0.2222 0.1524 -0.0542 -0.0327 -0.0016 296 VAL A CA +2475 C C . VAL A 296 ? 0.2792 0.2410 0.1658 -0.0602 -0.0325 -0.0033 296 VAL A C +2476 O O . VAL A 296 ? 0.2957 0.2555 0.1759 -0.0670 -0.0378 0.0000 296 VAL A O +2477 C CB . VAL A 296 ? 0.2406 0.2216 0.1524 -0.0515 -0.0316 -0.0003 296 VAL A CB +2478 C CG1 . VAL A 296 ? 0.2471 0.2291 0.1541 -0.0575 -0.0351 0.0035 296 VAL A CG1 +2479 C CG2 . VAL A 296 ? 0.2309 0.2216 0.1572 -0.0468 -0.0328 0.0019 296 VAL A CG2 +2480 N N . VAL A 297 ? 0.2892 0.2421 0.1676 -0.0579 -0.0263 -0.0080 297 VAL A N +2481 C CA . VAL A 297 ? 0.3194 0.2578 0.1784 -0.0631 -0.0248 -0.0103 297 VAL A CA +2482 C C . VAL A 297 ? 0.3375 0.2679 0.1878 -0.0677 -0.0283 -0.0106 297 VAL A C +2483 O O . VAL A 297 ? 0.3512 0.2732 0.1873 -0.0755 -0.0325 -0.0093 297 VAL A O +2484 C CB . VAL A 297 ? 0.3451 0.2753 0.1985 -0.0581 -0.0158 -0.0147 297 VAL A CB +2485 C CG1 . VAL A 297 ? 0.3705 0.2827 0.2015 -0.0628 -0.0129 -0.0176 297 VAL A CG1 +2486 C CG2 . VAL A 297 ? 0.3543 0.2919 0.2157 -0.0545 -0.0128 -0.0135 297 VAL A CG2 +2487 N N . ARG A 298 ? 0.3385 0.2714 0.1970 -0.0634 -0.0271 -0.0119 298 ARG A N +2488 C CA . ARG A 298 ? 0.3595 0.2855 0.2117 -0.0670 -0.0301 -0.0122 298 ARG A CA +2489 C C . ARG A 298 ? 0.3621 0.2932 0.2158 -0.0738 -0.0391 -0.0063 298 ARG A C +2490 O O . ARG A 298 ? 0.3706 0.2916 0.2105 -0.0814 -0.0433 -0.0054 298 ARG A O +2491 C CB . ARG A 298 ? 0.3855 0.3161 0.2494 -0.0605 -0.0274 -0.0137 298 ARG A CB +2492 C CG . ARG A 298 ? 0.4514 0.3728 0.3077 -0.0632 -0.0286 -0.0150 298 ARG A CG +2493 C CD . ARG A 298 ? 0.5071 0.4343 0.3760 -0.0568 -0.0263 -0.0159 298 ARG A CD +2494 N NE . ARG A 298 ? 0.5627 0.4894 0.4357 -0.0499 -0.0184 -0.0195 298 ARG A NE +2495 C CZ . ARG A 298 ? 0.5959 0.5340 0.4836 -0.0439 -0.0169 -0.0186 298 ARG A CZ +2496 N NH1 . ARG A 298 ? 0.6028 0.5401 0.4942 -0.0386 -0.0104 -0.0208 298 ARG A NH1 +2497 N NH2 . ARG A 298 ? 0.5851 0.5349 0.4837 -0.0434 -0.0218 -0.0151 298 ARG A NH2 +2498 N N . GLN A 299 ? 0.3535 0.2995 0.2235 -0.0715 -0.0421 -0.0016 299 GLN A N +2499 C CA . GLN A 299 ? 0.3590 0.3118 0.2339 -0.0770 -0.0499 0.0056 299 GLN A CA +2500 C C . GLN A 299 ? 0.3870 0.3366 0.2520 -0.0848 -0.0542 0.0088 299 GLN A C +2501 O O . GLN A 299 ? 0.4029 0.3494 0.2619 -0.0928 -0.0611 0.0134 299 GLN A O +2502 C CB . GLN A 299 ? 0.3452 0.3136 0.2398 -0.0713 -0.0503 0.0098 299 GLN A CB +2503 C CG . GLN A 299 ? 0.3338 0.3097 0.2356 -0.0760 -0.0573 0.0184 299 GLN A CG +2504 C CD . GLN A 299 ? 0.3113 0.3003 0.2311 -0.0699 -0.0567 0.0229 299 GLN A CD +2505 O OE1 . GLN A 299 ? 0.3085 0.3054 0.2364 -0.0726 -0.0610 0.0310 299 GLN A OE1 +2506 N NE2 . GLN A 299 ? 0.2821 0.2734 0.2084 -0.0618 -0.0513 0.0185 299 GLN A NE2 +2507 N N . CYS A 300 ? 0.3924 0.3424 0.2554 -0.0831 -0.0507 0.0068 300 CYS A N +2508 C CA . CYS A 300 ? 0.4087 0.3556 0.2619 -0.0905 -0.0545 0.0098 300 CYS A CA +2509 C C . CYS A 300 ? 0.4480 0.3763 0.2769 -0.0979 -0.0552 0.0065 300 CYS A C +2510 O O . CYS A 300 ? 0.4564 0.3806 0.2748 -0.1063 -0.0607 0.0101 300 CYS A O +2511 C CB . CYS A 300 ? 0.3963 0.3494 0.2550 -0.0864 -0.0505 0.0091 300 CYS A CB +2512 S SG . CYS A 300 ? 0.4013 0.3739 0.2849 -0.0804 -0.0515 0.0145 300 CYS A SG +2513 N N . SER A 301 ? 0.4716 0.3880 0.2911 -0.0951 -0.0500 0.0001 301 SER A N +2514 C CA . SER A 301 ? 0.5089 0.4050 0.3035 -0.1017 -0.0498 -0.0035 301 SER A CA +2515 C C . SER A 301 ? 0.5350 0.4229 0.3229 -0.1066 -0.0546 -0.0031 301 SER A C +2516 O O . SER A 301 ? 0.5574 0.4275 0.3234 -0.1139 -0.0565 -0.0050 301 SER A O +2517 C CB . SER A 301 ? 0.5388 0.4236 0.3234 -0.0957 -0.0391 -0.0109 301 SER A CB +2518 O OG . SER A 301 ? 0.5687 0.4535 0.3609 -0.0883 -0.0335 -0.0146 301 SER A OG +2519 N N . GLY A 302 ? 0.5305 0.4300 0.3361 -0.1026 -0.0563 -0.0006 302 GLY A N +2520 C CA . GLY A 302 ? 0.5449 0.4392 0.3475 -0.1069 -0.0613 0.0010 302 GLY A CA +2521 C C . GLY A 302 ? 0.5606 0.4402 0.3523 -0.1038 -0.0550 -0.0062 302 GLY A C +2522 O O . GLY A 302 ? 0.5777 0.4425 0.3534 -0.1106 -0.0585 -0.0070 302 GLY A O +2523 N N . VAL A 303 ? 0.5526 0.4361 0.3534 -0.0937 -0.0459 -0.0110 303 VAL A N +2524 C CA . VAL A 303 ? 0.5589 0.4304 0.3526 -0.0896 -0.0389 -0.0171 303 VAL A CA +2525 C C . VAL A 303 ? 0.5504 0.4249 0.3518 -0.0901 -0.0431 -0.0151 303 VAL A C +2526 O O . VAL A 303 ? 0.5357 0.4270 0.3563 -0.0873 -0.0466 -0.0105 303 VAL A O +2527 C CB . VAL A 303 ? 0.5633 0.4412 0.3684 -0.0789 -0.0291 -0.0207 303 VAL A CB +2528 C CG1 . VAL A 303 ? 0.5777 0.4448 0.3782 -0.0742 -0.0215 -0.0257 303 VAL A CG1 +2529 C CG2 . VAL A 303 ? 0.5724 0.4479 0.3709 -0.0782 -0.0248 -0.0220 303 VAL A CG2 +2530 N N A THR A 304 ? 0.5584 0.4163 0.3449 -0.0934 -0.0424 -0.0183 304 THR A N +2531 N N B THR A 304 ? 0.5585 0.4161 0.3445 -0.0936 -0.0424 -0.0183 304 THR A N +2532 C CA A THR A 304 ? 0.5583 0.4185 0.3519 -0.0940 -0.0464 -0.0162 304 THR A CA +2533 C CA B THR A 304 ? 0.5595 0.4178 0.3510 -0.0944 -0.0461 -0.0167 304 THR A CA +2534 C C A THR A 304 ? 0.5592 0.4165 0.3575 -0.0859 -0.0379 -0.0212 304 THR A C +2535 C C B THR A 304 ? 0.5665 0.4152 0.3551 -0.0881 -0.0372 -0.0228 304 THR A C +2536 O O A THR A 304 ? 0.5537 0.4136 0.3592 -0.0853 -0.0403 -0.0199 304 THR A O +2537 O O B THR A 304 ? 0.5641 0.4134 0.3558 -0.0806 -0.0281 -0.0266 304 THR A O +2538 C CB A THR A 304 ? 0.5841 0.4294 0.3596 -0.1053 -0.0545 -0.0143 304 THR A CB +2539 C CB B THR A 304 ? 0.5814 0.4283 0.3575 -0.1062 -0.0558 -0.0133 304 THR A CB +2540 O OG1 A THR A 304 ? 0.6127 0.4346 0.3633 -0.1078 -0.0490 -0.0209 304 THR A OG1 +2541 O OG1 B THR A 304 ? 0.6100 0.4336 0.3593 -0.1110 -0.0526 -0.0187 304 THR A OG1 +2542 C CG2 A THR A 304 ? 0.5871 0.4386 0.3622 -0.1137 -0.0643 -0.0073 304 THR A CG2 +2543 C CG2 B THR A 304 ? 0.5784 0.4376 0.3615 -0.1123 -0.0651 -0.0054 304 THR A CG2 +2544 S S . DMS B . ? 0.2030 0.2530 0.3059 0.0142 -0.0223 0.0422 401 DMS A S +2545 O O . DMS B . ? 0.2067 0.2623 0.3090 0.0170 -0.0213 0.0422 401 DMS A O +2546 C C1 . DMS B . ? 0.2054 0.2497 0.2971 0.0117 -0.0247 0.0398 401 DMS A C1 +2547 C C2 . DMS B . ? 0.1948 0.2540 0.3057 0.0159 -0.0255 0.0493 401 DMS A C2 +2548 S S . DMS C . ? 0.5726 0.6429 0.6328 0.0331 -0.0250 0.0516 402 DMS A S +2549 O O . DMS C . ? 0.5645 0.6411 0.6389 0.0324 -0.0251 0.0544 402 DMS A O +2550 C C1 . DMS C . ? 0.5741 0.6444 0.6284 0.0381 -0.0224 0.0551 402 DMS A C1 +2551 C C2 . DMS C . ? 0.5761 0.6466 0.6296 0.0338 -0.0265 0.0540 402 DMS A C2 +2552 S S . DMS D . ? 0.4191 0.3868 0.3321 -0.0512 -0.0390 -0.0011 403 DMS A S +2553 O O . DMS D . ? 0.4341 0.3934 0.3396 -0.0547 -0.0404 -0.0021 403 DMS A O +2554 C C1 . DMS D . ? 0.4314 0.3907 0.3317 -0.0546 -0.0369 -0.0043 403 DMS A C1 +2555 C C2 . DMS D . ? 0.4176 0.3886 0.3391 -0.0424 -0.0329 -0.0054 403 DMS A C2 +2556 S S . DMS E . ? 0.4677 0.4488 0.4601 -0.0274 -0.0432 0.0179 404 DMS A S +2557 O O . DMS E . ? 0.4800 0.4523 0.4688 -0.0326 -0.0462 0.0186 404 DMS A O +2558 C C1 . DMS E . ? 0.4613 0.4467 0.4607 -0.0200 -0.0367 0.0144 404 DMS A C1 +2559 C C2 . DMS E . ? 0.4585 0.4549 0.4639 -0.0243 -0.0465 0.0272 404 DMS A C2 +# +loop_ +_pdbx_poly_seq_scheme.asym_id +_pdbx_poly_seq_scheme.entity_id +_pdbx_poly_seq_scheme.seq_id +_pdbx_poly_seq_scheme.mon_id +_pdbx_poly_seq_scheme.ndb_seq_num +_pdbx_poly_seq_scheme.pdb_seq_num +_pdbx_poly_seq_scheme.auth_seq_num +_pdbx_poly_seq_scheme.pdb_mon_id +_pdbx_poly_seq_scheme.auth_mon_id +_pdbx_poly_seq_scheme.pdb_strand_id +_pdbx_poly_seq_scheme.pdb_ins_code +_pdbx_poly_seq_scheme.hetero +A 1 1 SER 1 1 1 SER SER A . n +A 1 2 GLY 2 2 2 GLY GLY A . n +A 1 3 PHE 3 3 3 PHE PHE A . n +A 1 4 ARG 4 4 4 ARG ARG A . n +A 1 5 LYS 5 5 5 LYS LYS A . n +A 1 6 MET 6 6 6 MET MET A . n +A 1 7 ALA 7 7 7 ALA ALA A . n +A 1 8 PHE 8 8 8 PHE PHE A . n +A 1 9 PRO 9 9 9 PRO PRO A . n +A 1 10 SER 10 10 10 SER SER A . n +A 1 11 GLY 11 11 11 GLY GLY A . n +A 1 12 LYS 12 12 12 LYS LYS A . n +A 1 13 VAL 13 13 13 VAL VAL A . n +A 1 14 GLU 14 14 14 GLU GLU A . n +A 1 15 GLY 15 15 15 GLY GLY A . n +A 1 16 CYS 16 16 16 CYS CYS A . n +A 1 17 MET 17 17 17 MET MET A . n +A 1 18 VAL 18 18 18 VAL VAL A . n +A 1 19 GLN 19 19 19 GLN GLN A . n +A 1 20 VAL 20 20 20 VAL VAL A . n +A 1 21 THR 21 21 21 THR THR A . n +A 1 22 CYS 22 22 22 CYS CYS A . n +A 1 23 GLY 23 23 23 GLY GLY A . n +A 1 24 THR 24 24 24 THR THR A . n +A 1 25 THR 25 25 25 THR THR A . n +A 1 26 THR 26 26 26 THR THR A . n +A 1 27 LEU 27 27 27 LEU LEU A . n +A 1 28 ASN 28 28 28 ASN ASN A . n +A 1 29 GLY 29 29 29 GLY GLY A . n +A 1 30 LEU 30 30 30 LEU LEU A . n +A 1 31 TRP 31 31 31 TRP TRP A . n +A 1 32 LEU 32 32 32 LEU LEU A . n +A 1 33 ASP 33 33 33 ASP ASP A . n +A 1 34 ASP 34 34 34 ASP ASP A . n +A 1 35 VAL 35 35 35 VAL VAL A . n +A 1 36 VAL 36 36 36 VAL VAL A . n +A 1 37 TYR 37 37 37 TYR TYR A . n +A 1 38 CYS 38 38 38 CYS CYS A . n +A 1 39 PRO 39 39 39 PRO PRO A . n +A 1 40 ARG 40 40 40 ARG ARG A . n +A 1 41 HIS 41 41 41 HIS HIS A . n +A 1 42 VAL 42 42 42 VAL VAL A . n +A 1 43 ILE 43 43 43 ILE ILE A . n +A 1 44 CYS 44 44 44 CYS CYS A . n +A 1 45 THR 45 45 45 THR THR A . n +A 1 46 SER 46 46 46 SER SER A . n +A 1 47 GLU 47 47 47 GLU GLU A . n +A 1 48 ASP 48 48 48 ASP ASP A . n +A 1 49 MET 49 49 49 MET MET A . n +A 1 50 LEU 50 50 50 LEU LEU A . n +A 1 51 ASN 51 51 51 ASN ASN A . n +A 1 52 PRO 52 52 52 PRO PRO A . n +A 1 53 ASN 53 53 53 ASN ASN A . n +A 1 54 TYR 54 54 54 TYR TYR A . n +A 1 55 GLU 55 55 55 GLU GLU A . n +A 1 56 ASP 56 56 56 ASP ASP A . n +A 1 57 LEU 57 57 57 LEU LEU A . n +A 1 58 LEU 58 58 58 LEU LEU A . n +A 1 59 ILE 59 59 59 ILE ILE A . n +A 1 60 ARG 60 60 60 ARG ARG A . n +A 1 61 LYS 61 61 61 LYS LYS A . n +A 1 62 SER 62 62 62 SER SER A . n +A 1 63 ASN 63 63 63 ASN ASN A . n +A 1 64 HIS 64 64 64 HIS HIS A . n +A 1 65 ASN 65 65 65 ASN ASN A . n +A 1 66 PHE 66 66 66 PHE PHE A . n +A 1 67 LEU 67 67 67 LEU LEU A . n +A 1 68 VAL 68 68 68 VAL VAL A . n +A 1 69 GLN 69 69 69 GLN GLN A . n +A 1 70 ALA 70 70 70 ALA ALA A . n +A 1 71 GLY 71 71 71 GLY GLY A . n +A 1 72 ASN 72 72 72 ASN ASN A . n +A 1 73 VAL 73 73 73 VAL VAL A . n +A 1 74 GLN 74 74 74 GLN GLN A . n +A 1 75 LEU 75 75 75 LEU LEU A . n +A 1 76 ARG 76 76 76 ARG ARG A . n +A 1 77 VAL 77 77 77 VAL VAL A . n +A 1 78 ILE 78 78 78 ILE ILE A . n +A 1 79 GLY 79 79 79 GLY GLY A . n +A 1 80 HIS 80 80 80 HIS HIS A . n +A 1 81 SER 81 81 81 SER SER A . n +A 1 82 MET 82 82 82 MET MET A . n +A 1 83 GLN 83 83 83 GLN GLN A . n +A 1 84 ASN 84 84 84 ASN ASN A . n +A 1 85 CYS 85 85 85 CYS CYS A . n +A 1 86 VAL 86 86 86 VAL VAL A . n +A 1 87 LEU 87 87 87 LEU LEU A . n +A 1 88 LYS 88 88 88 LYS LYS A . n +A 1 89 LEU 89 89 89 LEU LEU A . n +A 1 90 LYS 90 90 90 LYS LYS A . n +A 1 91 VAL 91 91 91 VAL VAL A . n +A 1 92 ASP 92 92 92 ASP ASP A . n +A 1 93 THR 93 93 93 THR THR A . n +A 1 94 ALA 94 94 94 ALA ALA A . n +A 1 95 ASN 95 95 95 ASN ASN A . n +A 1 96 PRO 96 96 96 PRO PRO A . n +A 1 97 LYS 97 97 97 LYS LYS A . n +A 1 98 THR 98 98 98 THR THR A . n +A 1 99 PRO 99 99 99 PRO PRO A . n +A 1 100 LYS 100 100 100 LYS LYS A . n +A 1 101 TYR 101 101 101 TYR TYR A . n +A 1 102 LYS 102 102 102 LYS LYS A . n +A 1 103 PHE 103 103 103 PHE PHE A . n +A 1 104 VAL 104 104 104 VAL VAL A . n +A 1 105 ARG 105 105 105 ARG ARG A . n +A 1 106 ILE 106 106 106 ILE ILE A . n +A 1 107 GLN 107 107 107 GLN GLN A . n +A 1 108 PRO 108 108 108 PRO PRO A . n +A 1 109 GLY 109 109 109 GLY GLY A . n +A 1 110 GLN 110 110 110 GLN GLN A . n +A 1 111 THR 111 111 111 THR THR A . n +A 1 112 PHE 112 112 112 PHE PHE A . n +A 1 113 SER 113 113 113 SER SER A . n +A 1 114 VAL 114 114 114 VAL VAL A . n +A 1 115 LEU 115 115 115 LEU LEU A . n +A 1 116 ALA 116 116 116 ALA ALA A . n +A 1 117 CYS 117 117 117 CYS CYS A . n +A 1 118 TYR 118 118 118 TYR TYR A . n +A 1 119 ASN 119 119 119 ASN ASN A . n +A 1 120 GLY 120 120 120 GLY GLY A . n +A 1 121 SER 121 121 121 SER SER A . n +A 1 122 PRO 122 122 122 PRO PRO A . n +A 1 123 SER 123 123 123 SER SER A . n +A 1 124 GLY 124 124 124 GLY GLY A . n +A 1 125 VAL 125 125 125 VAL VAL A . n +A 1 126 TYR 126 126 126 TYR TYR A . n +A 1 127 GLN 127 127 127 GLN GLN A . n +A 1 128 CYS 128 128 128 CYS CYS A . n +A 1 129 ALA 129 129 129 ALA ALA A . n +A 1 130 MET 130 130 130 MET MET A . n +A 1 131 ARG 131 131 131 ARG ARG A . n +A 1 132 PRO 132 132 132 PRO PRO A . n +A 1 133 ASN 133 133 133 ASN ASN A . n +A 1 134 PHE 134 134 134 PHE PHE A . n +A 1 135 THR 135 135 135 THR THR A . n +A 1 136 ILE 136 136 136 ILE ILE A . n +A 1 137 LYS 137 137 137 LYS LYS A . n +A 1 138 GLY 138 138 138 GLY GLY A . n +A 1 139 SER 139 139 139 SER SER A . n +A 1 140 PHE 140 140 140 PHE PHE A . n +A 1 141 LEU 141 141 141 LEU LEU A . n +A 1 142 ASN 142 142 142 ASN ASN A . n +A 1 143 GLY 143 143 143 GLY GLY A . n +A 1 144 SER 144 144 144 SER SER A . n +A 1 145 CYS 145 145 145 CYS CYS A . n +A 1 146 GLY 146 146 146 GLY GLY 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 GLY 149 149 149 GLY GLY A . n +A 1 150 PHE 150 150 150 PHE PHE A . n +A 1 151 ASN 151 151 151 ASN ASN A . n +A 1 152 ILE 152 152 152 ILE ILE A . n +A 1 153 ASP 153 153 153 ASP ASP A . n +A 1 154 TYR 154 154 154 TYR TYR A . n +A 1 155 ASP 155 155 155 ASP ASP A . n +A 1 156 CYS 156 156 156 CYS CYS A . n +A 1 157 VAL 157 157 157 VAL VAL A . n +A 1 158 SER 158 158 158 SER SER A . n +A 1 159 PHE 159 159 159 PHE PHE A . n +A 1 160 CYS 160 160 160 CYS CYS A . n +A 1 161 TYR 161 161 161 TYR TYR A . n +A 1 162 MET 162 162 162 MET MET A . n +A 1 163 HIS 163 163 163 HIS HIS A . n +A 1 164 HIS 164 164 164 HIS HIS A . n +A 1 165 MET 165 165 165 MET MET A . n +A 1 166 GLU 166 166 166 GLU GLU A . n +A 1 167 LEU 167 167 167 LEU LEU A . n +A 1 168 PRO 168 168 168 PRO PRO A . n +A 1 169 THR 169 169 169 THR THR A . n +A 1 170 GLY 170 170 170 GLY GLY A . n +A 1 171 VAL 171 171 171 VAL VAL A . n +A 1 172 HIS 172 172 172 HIS HIS A . n +A 1 173 ALA 173 173 173 ALA ALA A . n +A 1 174 GLY 174 174 174 GLY GLY A . n +A 1 175 THR 175 175 175 THR THR A . n +A 1 176 ASP 176 176 176 ASP ASP A . n +A 1 177 LEU 177 177 177 LEU LEU A . n +A 1 178 GLU 178 178 178 GLU GLU A . n +A 1 179 GLY 179 179 179 GLY GLY A . n +A 1 180 ASN 180 180 180 ASN ASN A . n +A 1 181 PHE 181 181 181 PHE PHE A . n +A 1 182 TYR 182 182 182 TYR TYR A . n +A 1 183 GLY 183 183 183 GLY GLY A . n +A 1 184 PRO 184 184 184 PRO PRO A . n +A 1 185 PHE 185 185 185 PHE PHE A . n +A 1 186 VAL 186 186 186 VAL VAL A . n +A 1 187 ASP 187 187 187 ASP ASP A . n +A 1 188 ARG 188 188 188 ARG ARG A . n +A 1 189 GLN 189 189 189 GLN GLN A . n +A 1 190 THR 190 190 190 THR THR A . n +A 1 191 ALA 191 191 191 ALA ALA A . n +A 1 192 GLN 192 192 192 GLN GLN A . n +A 1 193 ALA 193 193 193 ALA ALA A . n +A 1 194 ALA 194 194 194 ALA ALA A . n +A 1 195 GLY 195 195 195 GLY GLY A . n +A 1 196 THR 196 196 196 THR THR A . n +A 1 197 ASP 197 197 197 ASP ASP A . n +A 1 198 THR 198 198 198 THR THR A . n +A 1 199 THR 199 199 199 THR THR A . n +A 1 200 ILE 200 200 200 ILE ILE A . n +A 1 201 THR 201 201 201 THR THR A . n +A 1 202 VAL 202 202 202 VAL VAL A . n +A 1 203 ASN 203 203 203 ASN ASN A . n +A 1 204 VAL 204 204 204 VAL VAL A . n +A 1 205 LEU 205 205 205 LEU LEU A . n +A 1 206 ALA 206 206 206 ALA ALA A . n +A 1 207 TRP 207 207 207 TRP TRP A . n +A 1 208 LEU 208 208 208 LEU LEU A . n +A 1 209 TYR 209 209 209 TYR TYR A . n +A 1 210 ALA 210 210 210 ALA ALA A . n +A 1 211 ALA 211 211 211 ALA ALA A . n +A 1 212 VAL 212 212 212 VAL VAL A . n +A 1 213 ILE 213 213 213 ILE ILE A . n +A 1 214 ASN 214 214 214 ASN ASN A . n +A 1 215 GLY 215 215 215 GLY GLY A . n +A 1 216 ASP 216 216 216 ASP ASP A . n +A 1 217 ARG 217 217 217 ARG ARG A . n +A 1 218 TRP 218 218 218 TRP TRP A . n +A 1 219 PHE 219 219 219 PHE PHE A . n +A 1 220 LEU 220 220 220 LEU LEU A . n +A 1 221 ASN 221 221 221 ASN ASN A . n +A 1 222 ARG 222 222 222 ARG ARG A . n +A 1 223 PHE 223 223 223 PHE PHE A . n +A 1 224 THR 224 224 224 THR THR A . n +A 1 225 THR 225 225 225 THR THR A . n +A 1 226 THR 226 226 226 THR THR A . n +A 1 227 LEU 227 227 227 LEU LEU A . n +A 1 228 ASN 228 228 228 ASN ASN A . n +A 1 229 ASP 229 229 229 ASP ASP A . n +A 1 230 PHE 230 230 230 PHE PHE A . n +A 1 231 ASN 231 231 231 ASN ASN A . n +A 1 232 LEU 232 232 232 LEU LEU A . n +A 1 233 VAL 233 233 233 VAL VAL A . n +A 1 234 ALA 234 234 234 ALA ALA A . n +A 1 235 MET 235 235 235 MET MET A . n +A 1 236 LYS 236 236 236 LYS LYS A . n +A 1 237 TYR 237 237 237 TYR TYR A . n +A 1 238 ASN 238 238 238 ASN ASN A . n +A 1 239 TYR 239 239 239 TYR TYR A . n +A 1 240 GLU 240 240 240 GLU GLU A . n +A 1 241 PRO 241 241 241 PRO PRO A . n +A 1 242 LEU 242 242 242 LEU LEU A . n +A 1 243 THR 243 243 243 THR THR A . n +A 1 244 GLN 244 244 244 GLN GLN A . n +A 1 245 ASP 245 245 245 ASP ASP A . n +A 1 246 HIS 246 246 246 HIS HIS A . n +A 1 247 VAL 247 247 247 VAL VAL A . n +A 1 248 ASP 248 248 248 ASP ASP A . n +A 1 249 ILE 249 249 249 ILE ILE A . n +A 1 250 LEU 250 250 250 LEU LEU A . n +A 1 251 GLY 251 251 251 GLY GLY A . n +A 1 252 PRO 252 252 252 PRO PRO A . n +A 1 253 LEU 253 253 253 LEU LEU A . n +A 1 254 SER 254 254 254 SER SER A . n +A 1 255 ALA 255 255 255 ALA ALA A . n +A 1 256 GLN 256 256 256 GLN GLN A . n +A 1 257 THR 257 257 257 THR THR A . n +A 1 258 GLY 258 258 258 GLY GLY A . n +A 1 259 ILE 259 259 259 ILE ILE A . n +A 1 260 ALA 260 260 260 ALA ALA A . n +A 1 261 VAL 261 261 261 VAL VAL A . n +A 1 262 LEU 262 262 262 LEU LEU A . n +A 1 263 ASP 263 263 263 ASP ASP A . n +A 1 264 MET 264 264 264 MET MET A . n +A 1 265 CYS 265 265 265 CYS CYS A . n +A 1 266 ALA 266 266 266 ALA ALA A . n +A 1 267 SER 267 267 267 SER SER A . n +A 1 268 LEU 268 268 268 LEU LEU A . n +A 1 269 LYS 269 269 269 LYS LYS A . n +A 1 270 GLU 270 270 270 GLU GLU A . n +A 1 271 LEU 271 271 271 LEU LEU A . n +A 1 272 LEU 272 272 272 LEU LEU A . n +A 1 273 GLN 273 273 273 GLN GLN A . n +A 1 274 ASN 274 274 274 ASN ASN A . n +A 1 275 GLY 275 275 275 GLY GLY A . n +A 1 276 MET 276 276 276 MET MET A . n +A 1 277 ASN 277 277 277 ASN ASN A . n +A 1 278 GLY 278 278 278 GLY GLY A . n +A 1 279 ARG 279 279 279 ARG ARG A . n +A 1 280 THR 280 280 280 THR THR A . n +A 1 281 ILE 281 281 281 ILE ILE A . n +A 1 282 LEU 282 282 282 LEU LEU A . n +A 1 283 GLY 283 283 283 GLY GLY A . n +A 1 284 SER 284 284 284 SER SER A . n +A 1 285 ALA 285 285 285 ALA ALA A . n +A 1 286 LEU 286 286 286 LEU LEU A . n +A 1 287 LEU 287 287 287 LEU LEU A . n +A 1 288 GLU 288 288 288 GLU GLU A . n +A 1 289 ASP 289 289 289 ASP ASP A . n +A 1 290 GLU 290 290 290 GLU GLU A . n +A 1 291 PHE 291 291 291 PHE PHE A . n +A 1 292 THR 292 292 292 THR THR A . n +A 1 293 PRO 293 293 293 PRO PRO A . n +A 1 294 PHE 294 294 294 PHE PHE A . n +A 1 295 ASP 295 295 295 ASP ASP A . n +A 1 296 VAL 296 296 296 VAL VAL A . n +A 1 297 VAL 297 297 297 VAL VAL A . n +A 1 298 ARG 298 298 298 ARG ARG A . n +A 1 299 GLN 299 299 299 GLN GLN A . n +A 1 300 CYS 300 300 300 CYS CYS A . n +A 1 301 SER 301 301 301 SER SER A . n +A 1 302 GLY 302 302 302 GLY GLY A . n +A 1 303 VAL 303 303 303 VAL VAL A . n +A 1 304 THR 304 304 304 THR THR A . n +A 1 305 PHE 305 305 ? ? ? A . n +A 1 306 GLN 306 306 ? ? ? 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 DMS 1 401 401 DMS DMS A . +C 2 DMS 1 402 501 DMS DMS A . +D 2 DMS 1 403 601 DMS DMS A . +E 2 DMS 1 404 701 DMS DMS A . +F 3 HOH 1 501 374 HOH HOH A . +F 3 HOH 2 502 340 HOH HOH A . +F 3 HOH 3 503 119 HOH HOH A . +F 3 HOH 4 504 199 HOH HOH A . +F 3 HOH 5 505 165 HOH HOH A . +F 3 HOH 6 506 275 HOH HOH A . +F 3 HOH 7 507 112 HOH HOH A . +F 3 HOH 8 508 162 HOH HOH A . +F 3 HOH 9 509 66 HOH HOH A . +F 3 HOH 10 510 25 HOH HOH A . +F 3 HOH 11 511 132 HOH HOH A . +F 3 HOH 12 512 35 HOH HOH A . +F 3 HOH 13 513 345 HOH HOH A . +F 3 HOH 14 514 29 HOH HOH A . +F 3 HOH 15 515 99 HOH HOH A . +F 3 HOH 16 516 129 HOH HOH A . +F 3 HOH 17 517 212 HOH HOH A . +F 3 HOH 18 518 93 HOH HOH A . +F 3 HOH 19 519 327 HOH HOH A . +F 3 HOH 20 520 120 HOH HOH A . +F 3 HOH 21 521 155 HOH HOH A . +F 3 HOH 22 522 373 HOH HOH A . +F 3 HOH 23 523 9 HOH HOH A . +F 3 HOH 24 524 335 HOH HOH A . +F 3 HOH 25 525 243 HOH HOH A . +F 3 HOH 26 526 358 HOH HOH A . +F 3 HOH 27 527 97 HOH HOH A . +F 3 HOH 28 528 264 HOH HOH A . +F 3 HOH 29 529 137 HOH HOH A . +F 3 HOH 30 530 352 HOH HOH A . +F 3 HOH 31 531 151 HOH HOH A . +F 3 HOH 32 532 256 HOH HOH A . +F 3 HOH 33 533 48 HOH HOH A . +F 3 HOH 34 534 107 HOH HOH A . +F 3 HOH 35 535 40 HOH HOH A . +F 3 HOH 36 536 313 HOH HOH A . +F 3 HOH 37 537 34 HOH HOH A . +F 3 HOH 38 538 277 HOH HOH A . +F 3 HOH 39 539 332 HOH HOH A . +F 3 HOH 40 540 73 HOH HOH A . +F 3 HOH 41 541 198 HOH HOH A . +F 3 HOH 42 542 251 HOH HOH A . +F 3 HOH 43 543 38 HOH HOH A . +F 3 HOH 44 544 55 HOH HOH A . +F 3 HOH 45 545 63 HOH HOH A . +F 3 HOH 46 546 247 HOH HOH A . +F 3 HOH 47 547 248 HOH HOH A . +F 3 HOH 48 548 44 HOH HOH A . +F 3 HOH 49 549 178 HOH HOH A . +F 3 HOH 50 550 154 HOH HOH A . +F 3 HOH 51 551 76 HOH HOH A . +F 3 HOH 52 552 242 HOH HOH A . +F 3 HOH 53 553 67 HOH HOH A . +F 3 HOH 54 554 104 HOH HOH A . +F 3 HOH 55 555 30 HOH HOH A . +F 3 HOH 56 556 157 HOH HOH A . +F 3 HOH 57 557 33 HOH HOH A . +F 3 HOH 58 558 1 HOH HOH A . +F 3 HOH 59 559 80 HOH HOH A . +F 3 HOH 60 560 77 HOH HOH A . +F 3 HOH 61 561 53 HOH HOH A . +F 3 HOH 62 562 179 HOH HOH A . +F 3 HOH 63 563 56 HOH HOH A . +F 3 HOH 64 564 319 HOH HOH A . +F 3 HOH 65 565 21 HOH HOH A . +F 3 HOH 66 566 181 HOH HOH A . +F 3 HOH 67 567 208 HOH HOH A . +F 3 HOH 68 568 3 HOH HOH A . +F 3 HOH 69 569 45 HOH HOH A . +F 3 HOH 70 570 82 HOH HOH A . +F 3 HOH 71 571 183 HOH HOH A . +F 3 HOH 72 572 20 HOH HOH A . +F 3 HOH 73 573 182 HOH HOH A . +F 3 HOH 74 574 390 HOH HOH A . +F 3 HOH 75 575 177 HOH HOH A . +F 3 HOH 76 576 24 HOH HOH A . +F 3 HOH 77 577 244 HOH HOH A . +F 3 HOH 78 578 116 HOH HOH A . +F 3 HOH 79 579 7 HOH HOH A . +F 3 HOH 80 580 241 HOH HOH A . +F 3 HOH 81 581 159 HOH HOH A . +F 3 HOH 82 582 347 HOH HOH A . +F 3 HOH 83 583 113 HOH HOH A . +F 3 HOH 84 584 142 HOH HOH A . +F 3 HOH 85 585 12 HOH HOH A . +F 3 HOH 86 586 10 HOH HOH A . +F 3 HOH 87 587 186 HOH HOH A . +F 3 HOH 88 588 266 HOH HOH A . +F 3 HOH 89 589 349 HOH HOH A . +F 3 HOH 90 590 175 HOH HOH A . +F 3 HOH 91 591 184 HOH HOH A . +F 3 HOH 92 592 42 HOH HOH A . +F 3 HOH 93 593 294 HOH HOH A . +F 3 HOH 94 594 304 HOH HOH A . +F 3 HOH 95 595 274 HOH HOH A . +F 3 HOH 96 596 26 HOH HOH A . +F 3 HOH 97 597 169 HOH HOH A . +F 3 HOH 98 598 368 HOH HOH A . +F 3 HOH 99 599 189 HOH HOH A . +F 3 HOH 100 600 105 HOH HOH A . +F 3 HOH 101 601 19 HOH HOH A . +F 3 HOH 102 602 259 HOH HOH A . +F 3 HOH 103 603 357 HOH HOH A . +F 3 HOH 104 604 6 HOH HOH A . +F 3 HOH 105 605 170 HOH HOH A . +F 3 HOH 106 606 58 HOH HOH A . +F 3 HOH 107 607 65 HOH HOH A . +F 3 HOH 108 608 361 HOH HOH A . +F 3 HOH 109 609 94 HOH HOH A . +F 3 HOH 110 610 236 HOH HOH A . +F 3 HOH 111 611 163 HOH HOH A . +F 3 HOH 112 612 86 HOH HOH A . +F 3 HOH 113 613 31 HOH HOH A . +F 3 HOH 114 614 27 HOH HOH A . +F 3 HOH 115 615 326 HOH HOH A . +F 3 HOH 116 616 306 HOH HOH A . +F 3 HOH 117 617 43 HOH HOH A . +F 3 HOH 118 618 92 HOH HOH A . +F 3 HOH 119 619 4 HOH HOH A . +F 3 HOH 120 620 272 HOH HOH A . +F 3 HOH 121 621 168 HOH HOH A . +F 3 HOH 122 622 342 HOH HOH A . +F 3 HOH 123 623 117 HOH HOH A . +F 3 HOH 124 624 263 HOH HOH A . +F 3 HOH 125 625 289 HOH HOH A . +F 3 HOH 126 626 171 HOH HOH A . +F 3 HOH 127 627 69 HOH HOH A . +F 3 HOH 128 628 269 HOH HOH A . +F 3 HOH 129 629 5 HOH HOH A . +F 3 HOH 130 630 68 HOH HOH A . +F 3 HOH 131 631 87 HOH HOH A . +F 3 HOH 132 632 89 HOH HOH A . +F 3 HOH 133 633 351 HOH HOH A . +F 3 HOH 134 634 172 HOH HOH A . +F 3 HOH 135 635 230 HOH HOH A . +F 3 HOH 136 636 54 HOH HOH A . +F 3 HOH 137 637 118 HOH HOH A . +F 3 HOH 138 638 60 HOH HOH A . +F 3 HOH 139 639 106 HOH HOH A . +F 3 HOH 140 640 79 HOH HOH A . +F 3 HOH 141 641 185 HOH HOH A . +F 3 HOH 142 642 381 HOH HOH A . +F 3 HOH 143 643 298 HOH HOH A . +F 3 HOH 144 644 295 HOH HOH A . +F 3 HOH 145 645 17 HOH HOH A . +F 3 HOH 146 646 164 HOH HOH A . +F 3 HOH 147 647 204 HOH HOH A . +F 3 HOH 148 648 310 HOH HOH A . +F 3 HOH 149 649 11 HOH HOH A . +F 3 HOH 150 650 15 HOH HOH A . +F 3 HOH 151 651 28 HOH HOH A . +F 3 HOH 152 652 392 HOH HOH A . +F 3 HOH 153 653 246 HOH HOH A . +F 3 HOH 154 654 37 HOH HOH A . +F 3 HOH 155 655 309 HOH HOH A . +F 3 HOH 156 656 200 HOH HOH A . +F 3 HOH 157 657 130 HOH HOH A . +F 3 HOH 158 658 285 HOH HOH A . +F 3 HOH 159 659 83 HOH HOH A . +F 3 HOH 160 660 102 HOH HOH A . +F 3 HOH 161 661 62 HOH HOH A . +F 3 HOH 162 662 101 HOH HOH A . +F 3 HOH 163 663 176 HOH HOH A . +F 3 HOH 164 664 325 HOH HOH A . +F 3 HOH 165 665 234 HOH HOH A . +F 3 HOH 166 666 52 HOH HOH A . +F 3 HOH 167 667 88 HOH HOH A . +F 3 HOH 168 668 72 HOH HOH A . +F 3 HOH 169 669 128 HOH HOH A . +F 3 HOH 170 670 228 HOH HOH A . +F 3 HOH 171 671 145 HOH HOH A . +F 3 HOH 172 672 173 HOH HOH A . +F 3 HOH 173 673 18 HOH HOH A . +F 3 HOH 174 674 125 HOH HOH A . +F 3 HOH 175 675 152 HOH HOH A . +F 3 HOH 176 676 299 HOH HOH A . +F 3 HOH 177 677 240 HOH HOH A . +F 3 HOH 178 678 111 HOH HOH A . +F 3 HOH 179 679 61 HOH HOH A . +F 3 HOH 180 680 203 HOH HOH A . +F 3 HOH 181 681 100 HOH HOH A . +F 3 HOH 182 682 156 HOH HOH A . +F 3 HOH 183 683 71 HOH HOH A . +F 3 HOH 184 684 59 HOH HOH A . +F 3 HOH 185 685 133 HOH HOH A . +F 3 HOH 186 686 64 HOH HOH A . +F 3 HOH 187 687 127 HOH HOH A . +F 3 HOH 188 688 386 HOH HOH A . +F 3 HOH 189 689 14 HOH HOH A . +F 3 HOH 190 690 78 HOH HOH A . +F 3 HOH 191 691 344 HOH HOH A . +F 3 HOH 192 692 131 HOH HOH A . +F 3 HOH 193 693 2 HOH HOH A . +F 3 HOH 194 694 135 HOH HOH A . +F 3 HOH 195 695 239 HOH HOH A . +F 3 HOH 196 696 276 HOH HOH A . +F 3 HOH 197 697 328 HOH HOH A . +F 3 HOH 198 698 213 HOH HOH A . +F 3 HOH 199 699 32 HOH HOH A . +F 3 HOH 200 700 360 HOH HOH A . +F 3 HOH 201 701 201 HOH HOH A . +F 3 HOH 202 702 136 HOH HOH A . +F 3 HOH 203 703 153 HOH HOH A . +F 3 HOH 204 704 379 HOH HOH A . +F 3 HOH 205 705 166 HOH HOH A . +F 3 HOH 206 706 84 HOH HOH A . +F 3 HOH 207 707 75 HOH HOH A . +F 3 HOH 208 708 231 HOH HOH A . +F 3 HOH 209 709 187 HOH HOH A . +F 3 HOH 210 710 290 HOH HOH A . +F 3 HOH 211 711 96 HOH HOH A . +F 3 HOH 212 712 211 HOH HOH A . +F 3 HOH 213 713 150 HOH HOH A . +F 3 HOH 214 714 267 HOH HOH A . +F 3 HOH 215 715 260 HOH HOH A . +F 3 HOH 216 716 103 HOH HOH A . +F 3 HOH 217 717 232 HOH HOH A . +F 3 HOH 218 718 8 HOH HOH A . +F 3 HOH 219 719 126 HOH HOH A . +F 3 HOH 220 720 330 HOH HOH A . +F 3 HOH 221 721 385 HOH HOH A . +F 3 HOH 222 722 188 HOH HOH A . +F 3 HOH 223 723 217 HOH HOH A . +F 3 HOH 224 724 47 HOH HOH A . +F 3 HOH 225 725 81 HOH HOH A . +F 3 HOH 226 726 329 HOH HOH A . +F 3 HOH 227 727 388 HOH HOH A . +F 3 HOH 228 728 51 HOH HOH A . +F 3 HOH 229 729 95 HOH HOH A . +F 3 HOH 230 730 13 HOH HOH A . +F 3 HOH 231 731 197 HOH HOH A . +F 3 HOH 232 732 296 HOH HOH A . +F 3 HOH 233 733 235 HOH HOH A . +F 3 HOH 234 734 148 HOH HOH A . +F 3 HOH 235 735 22 HOH HOH A . +F 3 HOH 236 736 268 HOH HOH A . +F 3 HOH 237 737 193 HOH HOH A . +F 3 HOH 238 738 261 HOH HOH A . +F 3 HOH 239 739 23 HOH HOH A . +F 3 HOH 240 740 308 HOH HOH A . +F 3 HOH 241 741 265 HOH HOH A . +F 3 HOH 242 742 146 HOH HOH A . +F 3 HOH 243 743 339 HOH HOH A . +F 3 HOH 244 744 252 HOH HOH A . +F 3 HOH 245 745 262 HOH HOH A . +F 3 HOH 246 746 16 HOH HOH A . +F 3 HOH 247 747 57 HOH HOH A . +F 3 HOH 248 748 143 HOH HOH A . +F 3 HOH 249 749 206 HOH HOH A . +F 3 HOH 250 750 139 HOH HOH A . +F 3 HOH 251 751 297 HOH HOH A . +F 3 HOH 252 752 123 HOH HOH A . +F 3 HOH 253 753 286 HOH HOH A . +F 3 HOH 254 754 237 HOH HOH A . +F 3 HOH 255 755 219 HOH HOH A . +F 3 HOH 256 756 109 HOH HOH A . +F 3 HOH 257 757 36 HOH HOH A . +F 3 HOH 258 758 144 HOH HOH A . +F 3 HOH 259 759 312 HOH HOH A . +F 3 HOH 260 760 291 HOH HOH A . +F 3 HOH 261 761 110 HOH HOH A . +F 3 HOH 262 762 233 HOH HOH A . +F 3 HOH 263 763 245 HOH HOH A . +F 3 HOH 264 764 149 HOH HOH A . +F 3 HOH 265 765 194 HOH HOH A . +F 3 HOH 266 766 370 HOH HOH A . +F 3 HOH 267 767 389 HOH HOH A . +F 3 HOH 268 768 39 HOH HOH A . +F 3 HOH 269 769 91 HOH HOH A . +F 3 HOH 270 770 138 HOH HOH A . +F 3 HOH 271 771 50 HOH HOH A . +F 3 HOH 272 772 140 HOH HOH A . +F 3 HOH 273 773 46 HOH HOH A . +F 3 HOH 274 774 250 HOH HOH A . +F 3 HOH 275 775 270 HOH HOH A . +F 3 HOH 276 776 353 HOH HOH A . +F 3 HOH 277 777 249 HOH HOH A . +F 3 HOH 278 778 322 HOH HOH A . +F 3 HOH 279 779 336 HOH HOH A . +F 3 HOH 280 780 192 HOH HOH A . +F 3 HOH 281 781 315 HOH HOH A . +F 3 HOH 282 782 377 HOH HOH A . +F 3 HOH 283 783 284 HOH HOH A . +F 3 HOH 284 784 300 HOH HOH A . +F 3 HOH 285 785 320 HOH HOH A . +F 3 HOH 286 786 121 HOH HOH A . +F 3 HOH 287 787 271 HOH HOH A . +F 3 HOH 288 788 371 HOH HOH A . +F 3 HOH 289 789 257 HOH HOH A . +F 3 HOH 290 790 318 HOH HOH A . +F 3 HOH 291 791 74 HOH HOH A . +F 3 HOH 292 792 341 HOH HOH A . +F 3 HOH 293 793 238 HOH HOH A . +F 3 HOH 294 794 365 HOH HOH A . +F 3 HOH 295 795 215 HOH HOH A . +F 3 HOH 296 796 366 HOH HOH A . +F 3 HOH 297 797 356 HOH HOH A . +F 3 HOH 298 798 214 HOH HOH A . +F 3 HOH 299 799 311 HOH HOH A . +F 3 HOH 300 800 331 HOH HOH A . +F 3 HOH 301 801 307 HOH HOH A . +F 3 HOH 302 802 387 HOH HOH A . +F 3 HOH 303 803 280 HOH HOH A . +F 3 HOH 304 804 305 HOH HOH A . +F 3 HOH 305 805 167 HOH HOH A . +F 3 HOH 306 806 220 HOH HOH A . +F 3 HOH 307 807 255 HOH HOH A . +F 3 HOH 308 808 314 HOH HOH A . +F 3 HOH 309 809 202 HOH HOH A . +F 3 HOH 310 810 191 HOH HOH A . +F 3 HOH 311 811 303 HOH HOH A . +F 3 HOH 312 812 346 HOH HOH A . +F 3 HOH 313 813 334 HOH HOH A . +F 3 HOH 314 814 364 HOH HOH A . +F 3 HOH 315 815 221 HOH HOH A . +F 3 HOH 316 816 378 HOH HOH A . +F 3 HOH 317 817 287 HOH HOH A . +F 3 HOH 318 818 293 HOH HOH A . +F 3 HOH 319 819 362 HOH HOH A . +F 3 HOH 320 820 384 HOH HOH A . +F 3 HOH 321 821 273 HOH HOH A . +F 3 HOH 322 822 174 HOH HOH A . +F 3 HOH 323 823 301 HOH HOH A . +F 3 HOH 324 824 317 HOH HOH A . +F 3 HOH 325 825 372 HOH HOH A . +F 3 HOH 326 826 180 HOH HOH A . +F 3 HOH 327 827 253 HOH HOH A . +F 3 HOH 328 828 161 HOH HOH A . +F 3 HOH 329 829 288 HOH HOH A . +F 3 HOH 330 830 190 HOH HOH A . +F 3 HOH 331 831 355 HOH HOH A . +F 3 HOH 332 832 278 HOH HOH A . +F 3 HOH 333 833 391 HOH HOH A . +F 3 HOH 334 834 226 HOH HOH A . +F 3 HOH 335 835 258 HOH HOH A . +F 3 HOH 336 836 227 HOH HOH A . +F 3 HOH 337 837 147 HOH HOH A . +F 3 HOH 338 838 323 HOH HOH A . +F 3 HOH 339 839 369 HOH HOH A . +F 3 HOH 340 840 354 HOH HOH A . +F 3 HOH 341 841 205 HOH HOH A . +F 3 HOH 342 842 108 HOH HOH A . +F 3 HOH 343 843 122 HOH HOH A . +F 3 HOH 344 844 229 HOH HOH A . +F 3 HOH 345 845 363 HOH HOH A . +F 3 HOH 346 846 158 HOH HOH A . +F 3 HOH 347 847 90 HOH HOH A . +F 3 HOH 348 848 210 HOH HOH A . +F 3 HOH 349 849 49 HOH HOH A . +F 3 HOH 350 850 338 HOH HOH A . +F 3 HOH 351 851 124 HOH HOH A . +F 3 HOH 352 852 218 HOH HOH A . +F 3 HOH 353 853 160 HOH HOH A . +F 3 HOH 354 854 333 HOH HOH A . +F 3 HOH 355 855 223 HOH HOH A . +F 3 HOH 356 856 207 HOH HOH A . +F 3 HOH 357 857 343 HOH HOH A . +F 3 HOH 358 858 282 HOH HOH A . +F 3 HOH 359 859 41 HOH HOH A . +F 3 HOH 360 860 225 HOH HOH A . +F 3 HOH 361 861 383 HOH HOH A . +F 3 HOH 362 862 216 HOH HOH A . +F 3 HOH 363 863 337 HOH HOH A . +F 3 HOH 364 864 380 HOH HOH A . +F 3 HOH 365 865 254 HOH HOH A . +F 3 HOH 366 866 292 HOH HOH A . +F 3 HOH 367 867 376 HOH HOH A . +F 3 HOH 368 868 70 HOH HOH A . +F 3 HOH 369 869 209 HOH HOH A . +F 3 HOH 370 870 134 HOH HOH A . +F 3 HOH 371 871 281 HOH HOH A . +F 3 HOH 372 872 382 HOH HOH A . +F 3 HOH 373 873 350 HOH HOH A . +F 3 HOH 374 874 141 HOH HOH A . +F 3 HOH 375 875 195 HOH HOH A . +F 3 HOH 376 876 114 HOH HOH A . +F 3 HOH 377 877 316 HOH HOH A . +F 3 HOH 378 878 359 HOH HOH A . +F 3 HOH 379 879 324 HOH HOH A . +F 3 HOH 380 880 279 HOH HOH A . +F 3 HOH 381 881 367 HOH HOH A . +F 3 HOH 382 882 98 HOH HOH A . +F 3 HOH 383 883 375 HOH HOH A . +F 3 HOH 384 884 302 HOH HOH A . +F 3 HOH 385 885 348 HOH HOH A . +F 3 HOH 386 886 115 HOH HOH A . +F 3 HOH 387 887 196 HOH HOH A . +F 3 HOH 388 888 224 HOH HOH A . +F 3 HOH 389 889 222 HOH HOH A . +F 3 HOH 390 890 283 HOH HOH A . +F 3 HOH 391 891 321 HOH HOH A . +# +_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 dimeric +_pdbx_struct_assembly.oligomeric_count 2 +# +_pdbx_struct_assembly_gen.assembly_id 1 +_pdbx_struct_assembly_gen.oper_expression 1,2 +_pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F +# +loop_ +_pdbx_struct_assembly_prop.biol_id +_pdbx_struct_assembly_prop.type +_pdbx_struct_assembly_prop.value +_pdbx_struct_assembly_prop.details +1 'ABSA (A^2)' 4410 ? +1 MORE -8 ? +1 'SSA (A^2)' 25910 ? +# +loop_ +_pdbx_struct_oper_list.id +_pdbx_struct_oper_list.type +_pdbx_struct_oper_list.name +_pdbx_struct_oper_list.symmetry_operation +_pdbx_struct_oper_list.matrix[1][1] +_pdbx_struct_oper_list.matrix[1][2] +_pdbx_struct_oper_list.matrix[1][3] +_pdbx_struct_oper_list.vector[1] +_pdbx_struct_oper_list.matrix[2][1] +_pdbx_struct_oper_list.matrix[2][2] +_pdbx_struct_oper_list.matrix[2][3] +_pdbx_struct_oper_list.vector[2] +_pdbx_struct_oper_list.matrix[3][1] +_pdbx_struct_oper_list.matrix[3][2] +_pdbx_struct_oper_list.matrix[3][3] +_pdbx_struct_oper_list.vector[3] +1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 +0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 +2 'crystal symmetry operation' 2_555 -x,y,-z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 +0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 +# +_pdbx_struct_special_symmetry.id 1 +_pdbx_struct_special_symmetry.PDB_model_num 1 +_pdbx_struct_special_symmetry.auth_asym_id A +_pdbx_struct_special_symmetry.auth_comp_id HOH +_pdbx_struct_special_symmetry.auth_seq_id 774 +_pdbx_struct_special_symmetry.PDB_ins_code ? +_pdbx_struct_special_symmetry.label_asym_id F +_pdbx_struct_special_symmetry.label_comp_id HOH +_pdbx_struct_special_symmetry.label_seq_id . +# +_pdbx_audit_revision_history.ordinal 1 +_pdbx_audit_revision_history.data_content_type 'Structure model' +_pdbx_audit_revision_history.major_revision 1 +_pdbx_audit_revision_history.minor_revision 0 +_pdbx_audit_revision_history.revision_date 2020-03-11 +# +_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 ? +_pdbx_audit_revision_details.details ? +# +_pdbx_refine_tls.id 1 +_pdbx_refine_tls.pdbx_refine_id 'X-RAY DIFFRACTION' +_pdbx_refine_tls.details ? +_pdbx_refine_tls.method refined +_pdbx_refine_tls.origin_x 11.7561 +_pdbx_refine_tls.origin_y 0.8392 +_pdbx_refine_tls.origin_z 4.6891 +_pdbx_refine_tls.T[1][1] -0.0121 +_pdbx_refine_tls.T[1][1]_esd ? +_pdbx_refine_tls.T[1][2] -0.0060 +_pdbx_refine_tls.T[1][2]_esd ? +_pdbx_refine_tls.T[1][3] -0.0248 +_pdbx_refine_tls.T[1][3]_esd ? +_pdbx_refine_tls.T[2][2] -0.0177 +_pdbx_refine_tls.T[2][2]_esd ? +_pdbx_refine_tls.T[2][3] -0.0095 +_pdbx_refine_tls.T[2][3]_esd ? +_pdbx_refine_tls.T[3][3] -0.0441 +_pdbx_refine_tls.T[3][3]_esd ? +_pdbx_refine_tls.L[1][1] 0.3373 +_pdbx_refine_tls.L[1][1]_esd ? +_pdbx_refine_tls.L[1][2] 0.1417 +_pdbx_refine_tls.L[1][2]_esd ? +_pdbx_refine_tls.L[1][3] -0.0841 +_pdbx_refine_tls.L[1][3]_esd ? +_pdbx_refine_tls.L[2][2] 0.9615 +_pdbx_refine_tls.L[2][2]_esd ? +_pdbx_refine_tls.L[2][3] -0.7793 +_pdbx_refine_tls.L[2][3]_esd ? +_pdbx_refine_tls.L[3][3] 0.4899 +_pdbx_refine_tls.L[3][3]_esd ? +_pdbx_refine_tls.S[1][1] -0.0543 +_pdbx_refine_tls.S[1][1]_esd ? +_pdbx_refine_tls.S[1][2] 0.0192 +_pdbx_refine_tls.S[1][2]_esd ? +_pdbx_refine_tls.S[1][3] -0.0247 +_pdbx_refine_tls.S[1][3]_esd ? +_pdbx_refine_tls.S[2][1] -0.0315 +_pdbx_refine_tls.S[2][1]_esd ? +_pdbx_refine_tls.S[2][2] 0.0611 +_pdbx_refine_tls.S[2][2]_esd ? +_pdbx_refine_tls.S[2][3] -0.0331 +_pdbx_refine_tls.S[2][3]_esd ? +_pdbx_refine_tls.S[3][1] 0.0069 +_pdbx_refine_tls.S[3][1]_esd ? +_pdbx_refine_tls.S[3][2] -0.0231 +_pdbx_refine_tls.S[3][2]_esd ? +_pdbx_refine_tls.S[3][3] -0.0068 +_pdbx_refine_tls.S[3][3]_esd ? +# +_pdbx_refine_tls_group.id 1 +_pdbx_refine_tls_group.pdbx_refine_id 'X-RAY DIFFRACTION' +_pdbx_refine_tls_group.refine_tls_id 1 +_pdbx_refine_tls_group.beg_label_asym_id ? +_pdbx_refine_tls_group.beg_label_seq_id ? +_pdbx_refine_tls_group.beg_auth_asym_id A +_pdbx_refine_tls_group.beg_auth_seq_id 1 +_pdbx_refine_tls_group.end_label_asym_id ? +_pdbx_refine_tls_group.end_label_seq_id ? +_pdbx_refine_tls_group.end_auth_asym_id A +_pdbx_refine_tls_group.end_auth_seq_id 304 +_pdbx_refine_tls_group.selection ? +_pdbx_refine_tls_group.selection_details '{ A|* }' +# +_pdbx_phasing_MR.entry_id 6Y84 +_pdbx_phasing_MR.method_rotation ? +_pdbx_phasing_MR.method_translation ? +_pdbx_phasing_MR.model_details ? +_pdbx_phasing_MR.R_factor ? +_pdbx_phasing_MR.R_rigid_body 0.468 +_pdbx_phasing_MR.correlation_coeff_Fo_to_Fc ? +_pdbx_phasing_MR.correlation_coeff_Io_to_Ic ? +_pdbx_phasing_MR.d_res_high_rotation 54.910 +_pdbx_phasing_MR.d_res_low_rotation 1.740 +_pdbx_phasing_MR.d_res_high_translation ? +_pdbx_phasing_MR.d_res_low_translation ? +_pdbx_phasing_MR.packing ? +_pdbx_phasing_MR.reflns_percent_rotation ? +_pdbx_phasing_MR.reflns_percent_translation ? +_pdbx_phasing_MR.sigma_F_rotation ? +_pdbx_phasing_MR.sigma_F_translation ? +_pdbx_phasing_MR.sigma_I_rotation ? +_pdbx_phasing_MR.sigma_I_translation ? +# +_phasing.method MR +# +loop_ +_software.citation_id +_software.classification +_software.compiler_name +_software.compiler_version +_software.contact_author +_software.contact_author_email +_software.date +_software.description +_software.dependencies +_software.hardware +_software.language +_software.location +_software.mods +_software.name +_software.os +_software.os_version +_software.type +_software.version +_software.pdbx_ordinal +? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? 0.7.4 1 +? phasing ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? . 2 +? refinement ? ? ? ? ? ? ? ? ? ? ? BUSTER ? ? ? . 3 +? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.25 4 +? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? DIALS ? ? ? . 5 +? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2 ? ? ? . 6 +? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot ? ? ? . 7 +? refinement ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 7.0.078 8 +# +_pdbx_entry_details.entry_id 6Y84 +_pdbx_entry_details.has_ligand_of_interest N +_pdbx_entry_details.compound_details ? +_pdbx_entry_details.source_details ? +_pdbx_entry_details.nonpolymer_details ? +_pdbx_entry_details.sequence_details ? +# +loop_ +_pdbx_validate_torsion.id +_pdbx_validate_torsion.PDB_model_num +_pdbx_validate_torsion.auth_comp_id +_pdbx_validate_torsion.auth_asym_id +_pdbx_validate_torsion.auth_seq_id +_pdbx_validate_torsion.PDB_ins_code +_pdbx_validate_torsion.label_alt_id +_pdbx_validate_torsion.phi +_pdbx_validate_torsion.psi +1 1 ASP A 33 ? ? 57.52 -132.67 +2 1 ASN A 51 ? ? -154.49 69.76 +3 1 ASN A 84 ? ? 56.10 -119.94 +4 1 TYR A 154 ? ? 58.72 -89.93 +# +loop_ +_pdbx_distant_solvent_atoms.id +_pdbx_distant_solvent_atoms.PDB_model_num +_pdbx_distant_solvent_atoms.auth_atom_id +_pdbx_distant_solvent_atoms.label_alt_id +_pdbx_distant_solvent_atoms.auth_asym_id +_pdbx_distant_solvent_atoms.auth_comp_id +_pdbx_distant_solvent_atoms.auth_seq_id +_pdbx_distant_solvent_atoms.PDB_ins_code +_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance +_pdbx_distant_solvent_atoms.neighbor_ligand_distance +1 1 O ? A HOH 889 ? 6.51 . +2 1 O ? A HOH 890 ? 6.68 . +3 1 O ? A HOH 891 ? 7.12 . +# +loop_ +_pdbx_unobs_or_zero_occ_residues.id +_pdbx_unobs_or_zero_occ_residues.PDB_model_num +_pdbx_unobs_or_zero_occ_residues.polymer_flag +_pdbx_unobs_or_zero_occ_residues.occupancy_flag +_pdbx_unobs_or_zero_occ_residues.auth_asym_id +_pdbx_unobs_or_zero_occ_residues.auth_comp_id +_pdbx_unobs_or_zero_occ_residues.auth_seq_id +_pdbx_unobs_or_zero_occ_residues.PDB_ins_code +_pdbx_unobs_or_zero_occ_residues.label_asym_id +_pdbx_unobs_or_zero_occ_residues.label_comp_id +_pdbx_unobs_or_zero_occ_residues.label_seq_id +1 1 Y 1 A PHE 305 ? A PHE 305 +2 1 Y 1 A GLN 306 ? A GLN 306 +# +loop_ +_pdbx_entity_nonpoly.entity_id +_pdbx_entity_nonpoly.name +_pdbx_entity_nonpoly.comp_id +2 'DIMETHYL SULFOXIDE' DMS +3 water HOH +# +loop_ +_pdbx_struct_assembly_auth_evidence.id +_pdbx_struct_assembly_auth_evidence.assembly_id +_pdbx_struct_assembly_auth_evidence.experimental_support +_pdbx_struct_assembly_auth_evidence.details +1 1 homology ? +2 1 'gel filtration' ? +# -- cgit v1.2.3